data_9J1I
# 
_entry.id   9J1I 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9J1I         pdb_00009j1i 10.2210/pdb9j1i/pdb 
WWPDB D_1300049927 ?            ?                   
# 
_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       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J1I 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              yanwupeng@sjtu.edu.cn 
_pdbx_contact_author.name_first         Wupeng 
_pdbx_contact_author.name_last          Yan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0210-9734 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, X.Y.' 1 ? 
'Wang, J.'   2 ? 
'Yan, W.P.'  3 ? 
# 
_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            'Catalysis Science And Technology' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2044-4753 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                386 
_citation.page_last                 395 
_citation.title                     
'Characterizing Y224 conformational flexibility in FtmOx1-catalysis using 19 F NMR spectroscopy.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1039/d4cy01077a 
_citation.pdbx_database_id_PubMed   39669701 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, X.'       1  ?                   
primary 'Yang, L.'       2  ?                   
primary 'Wang, S.'       3  ?                   
primary 'Wang, J.'       4  ?                   
primary 'Li, K.'         5  ?                   
primary 'Naowarojna, N.' 6  ?                   
primary 'Ju, Y.'         7  ?                   
primary 'Ye, K.'         8  ?                   
primary 'Han, Y.'        9  ?                   
primary 'Yan, W.'        10 ?                   
primary 'Liu, X.'        11 0000-0002-1322-8253 
primary 'Zhang, L.'      12 ?                   
primary 'Liu, P.'        13 0000-0002-7952-3458 
# 
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 'Verruculogen synthase' 35118.004 2   1.14.11.38 ? ? ? 
2 non-polymer syn 'FE (II) ION'           55.845    2   ?          ? ? ? 
3 non-polymer syn 'COBALT (II) ION'       58.933    1   ?          ? ? ? 
4 water       nat water                   18.015    222 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Fumitremorgin biosynthesis protein F' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVAT
TCPTFRNTVLINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPVSLSVIFPLTEFT
EENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLA(F2Y)FNSVQLTPFETY
RTMPREMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPALEVDLQGDHGLSAWSHPQFEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVAT
TCPTFRNTVLINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPVSLSVIFPLTEFT
EENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLAXFNSVQLTPFETYRTMP
REMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPALEVDLQGDHGLSAWSHPQFEK
;
_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 'FE (II) ION'     FE2 
3 'COBALT (II) ION' CO  
4 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   VAL n 
1 4   ASP n 
1 5   SER n 
1 6   LYS n 
1 7   PRO n 
1 8   GLN n 
1 9   LEU n 
1 10  GLN n 
1 11  ARG n 
1 12  LEU n 
1 13  ALA n 
1 14  ALA n 
1 15  ASP n 
1 16  ALA n 
1 17  ASP n 
1 18  VAL n 
1 19  ASP n 
1 20  ARG n 
1 21  MET n 
1 22  CYS n 
1 23  ARG n 
1 24  LEU n 
1 25  LEU n 
1 26  GLU n 
1 27  GLU n 
1 28  ASP n 
1 29  GLY n 
1 30  ALA n 
1 31  PHE n 
1 32  ILE n 
1 33  LEU n 
1 34  LYS n 
1 35  GLY n 
1 36  LEU n 
1 37  LEU n 
1 38  PRO n 
1 39  PHE n 
1 40  ASP n 
1 41  VAL n 
1 42  VAL n 
1 43  GLU n 
1 44  SER n 
1 45  PHE n 
1 46  ASN n 
1 47  ARG n 
1 48  GLU n 
1 49  LEU n 
1 50  ASP n 
1 51  VAL n 
1 52  GLN n 
1 53  MET n 
1 54  ALA n 
1 55  ILE n 
1 56  PRO n 
1 57  PRO n 
1 58  PRO n 
1 59  LYS n 
1 60  GLY n 
1 61  GLU n 
1 62  ARG n 
1 63  LEU n 
1 64  LEU n 
1 65  ALA n 
1 66  ASP n 
1 67  LYS n 
1 68  TYR n 
1 69  PRO n 
1 70  PRO n 
1 71  HIS n 
1 72  PHE n 
1 73  LYS n 
1 74  TYR n 
1 75  VAL n 
1 76  PRO n 
1 77  ASN n 
1 78  VAL n 
1 79  ALA n 
1 80  THR n 
1 81  THR n 
1 82  CYS n 
1 83  PRO n 
1 84  THR n 
1 85  PHE n 
1 86  ARG n 
1 87  ASN n 
1 88  THR n 
1 89  VAL n 
1 90  LEU n 
1 91  ILE n 
1 92  ASN n 
1 93  PRO n 
1 94  VAL n 
1 95  ILE n 
1 96  HIS n 
1 97  ALA n 
1 98  ILE n 
1 99  CYS n 
1 100 GLU n 
1 101 ALA n 
1 102 TYR n 
1 103 PHE n 
1 104 GLN n 
1 105 ARG n 
1 106 THR n 
1 107 GLY n 
1 108 ASP n 
1 109 TYR n 
1 110 TRP n 
1 111 LEU n 
1 112 SER n 
1 113 ALA n 
1 114 ALA n 
1 115 PHE n 
1 116 LEU n 
1 117 ARG n 
1 118 GLU n 
1 119 ILE n 
1 120 GLU n 
1 121 SER n 
1 122 GLY n 
1 123 MET n 
1 124 PRO n 
1 125 ALA n 
1 126 GLN n 
1 127 PRO n 
1 128 PHE n 
1 129 HIS n 
1 130 ARG n 
1 131 ASP n 
1 132 ASP n 
1 133 ALA n 
1 134 THR n 
1 135 HIS n 
1 136 PRO n 
1 137 LEU n 
1 138 MET n 
1 139 HIS n 
1 140 TYR n 
1 141 GLN n 
1 142 PRO n 
1 143 LEU n 
1 144 GLU n 
1 145 ALA n 
1 146 PRO n 
1 147 PRO n 
1 148 VAL n 
1 149 SER n 
1 150 LEU n 
1 151 SER n 
1 152 VAL n 
1 153 ILE n 
1 154 PHE n 
1 155 PRO n 
1 156 LEU n 
1 157 THR n 
1 158 GLU n 
1 159 PHE n 
1 160 THR n 
1 161 GLU n 
1 162 GLU n 
1 163 ASN n 
1 164 GLY n 
1 165 ALA n 
1 166 THR n 
1 167 GLU n 
1 168 VAL n 
1 169 ILE n 
1 170 LEU n 
1 171 GLY n 
1 172 SER n 
1 173 HIS n 
1 174 ARG n 
1 175 TRP n 
1 176 THR n 
1 177 GLU n 
1 178 VAL n 
1 179 GLY n 
1 180 THR n 
1 181 PRO n 
1 182 GLU n 
1 183 ARG n 
1 184 ASP n 
1 185 GLN n 
1 186 ALA n 
1 187 VAL n 
1 188 LEU n 
1 189 ALA n 
1 190 THR n 
1 191 MET n 
1 192 ASP n 
1 193 PRO n 
1 194 GLY n 
1 195 ASP n 
1 196 VAL n 
1 197 LEU n 
1 198 ILE n 
1 199 VAL n 
1 200 ARG n 
1 201 GLN n 
1 202 ARG n 
1 203 VAL n 
1 204 VAL n 
1 205 HIS n 
1 206 ALA n 
1 207 GLY n 
1 208 GLY n 
1 209 GLY n 
1 210 ASN n 
1 211 ARG n 
1 212 THR n 
1 213 THR n 
1 214 ALA n 
1 215 GLY n 
1 216 LYS n 
1 217 PRO n 
1 218 ARG n 
1 219 ARG n 
1 220 VAL n 
1 221 VAL n 
1 222 LEU n 
1 223 ALA n 
1 224 F2Y n 
1 225 PHE n 
1 226 ASN n 
1 227 SER n 
1 228 VAL n 
1 229 GLN n 
1 230 LEU n 
1 231 THR n 
1 232 PRO n 
1 233 PHE n 
1 234 GLU n 
1 235 THR n 
1 236 TYR n 
1 237 ARG n 
1 238 THR n 
1 239 MET n 
1 240 PRO n 
1 241 ARG n 
1 242 GLU n 
1 243 MET n 
1 244 VAL n 
1 245 GLU n 
1 246 SER n 
1 247 MET n 
1 248 THR n 
1 249 VAL n 
1 250 LEU n 
1 251 GLY n 
1 252 GLN n 
1 253 ARG n 
1 254 MET n 
1 255 LEU n 
1 256 GLY n 
1 257 TRP n 
1 258 ARG n 
1 259 THR n 
1 260 MET n 
1 261 LYS n 
1 262 PRO n 
1 263 SER n 
1 264 ASP n 
1 265 PRO n 
1 266 ASN n 
1 267 ILE n 
1 268 VAL n 
1 269 GLY n 
1 270 ILE n 
1 271 ASN n 
1 272 LEU n 
1 273 ILE n 
1 274 ASP n 
1 275 ASP n 
1 276 LYS n 
1 277 ARG n 
1 278 LEU n 
1 279 GLU n 
1 280 ASN n 
1 281 VAL n 
1 282 LEU n 
1 283 GLN n 
1 284 LEU n 
1 285 LYS n 
1 286 ALA n 
1 287 ALA n 
1 288 ASP n 
1 289 SER n 
1 290 PRO n 
1 291 ALA n 
1 292 LEU n 
1 293 GLU n 
1 294 VAL n 
1 295 ASP n 
1 296 LEU n 
1 297 GLN n 
1 298 GLY n 
1 299 ASP n 
1 300 HIS n 
1 301 GLY n 
1 302 LEU n 
1 303 SER n 
1 304 ALA n 
1 305 TRP n 
1 306 SER n 
1 307 HIS n 
1 308 PRO n 
1 309 GLN n 
1 310 PHE n 
1 311 GLU n 
1 312 LYS 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                   312 
_entity_src_gen.gene_src_common_name               'Neosartorya fumigata' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ftmOx1, ftmF, AFUA_8G00230' 
_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      'Aspergillus fumigatus Af293' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     330879 
_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 
CO  non-polymer         . 'COBALT (II) ION'       ? 'Co 2'           58.933  
CYS 'L-peptide linking' y CYSTEINE                ? 'C3 H7 N O2 S'   121.158 
F2Y 'L-peptide linking' n 3,5-difluoro-L-tyrosine ? 'C9 H9 F2 N O3'  217.169 
FE2 non-polymer         . 'FE (II) ION'           ? 'Fe 2'           55.845  
GLN 'L-peptide linking' y GLUTAMINE               ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE               ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  GLN 10  10  10  GLN GLN A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  ALA 14  14  14  ALA ALA 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  ASP 17  17  17  ASP ASP A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  MET 21  21  21  MET MET A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  GLU 48  48  48  GLU GLU A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  MET 53  53  53  MET MET A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  CYS 82  82  82  CYS CYS A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  CYS 99  99  99  CYS CYS A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 TRP 110 110 110 TRP TRP A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 HIS 129 129 129 HIS HIS A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 HIS 135 135 135 HIS HIS A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 MET 138 138 138 MET MET A . n 
A 1 139 HIS 139 139 139 HIS HIS A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 PRO 146 146 146 PRO PRO A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 TRP 175 175 175 TRP TRP A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 MET 191 191 191 MET MET A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 GLN 201 201 201 GLN GLN A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 F2Y 224 224 224 F2Y F2Y A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 MET 239 239 239 MET MET A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 MET 243 243 243 MET MET A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 MET 247 247 247 MET MET A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 MET 254 254 254 MET MET A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 ARG 258 258 258 ARG ARG A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 MET 260 260 260 MET MET A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 PRO 265 265 265 PRO PRO A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 ASP 275 275 275 ASP ASP A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLN 283 283 283 GLN GLN A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 PRO 290 290 ?   ?   ?   A . n 
A 1 291 ALA 291 291 ?   ?   ?   A . n 
A 1 292 LEU 292 292 ?   ?   ?   A . n 
A 1 293 GLU 293 293 ?   ?   ?   A . n 
A 1 294 VAL 294 294 ?   ?   ?   A . n 
A 1 295 ASP 295 295 ?   ?   ?   A . n 
A 1 296 LEU 296 296 ?   ?   ?   A . n 
A 1 297 GLN 297 297 ?   ?   ?   A . n 
A 1 298 GLY 298 298 ?   ?   ?   A . n 
A 1 299 ASP 299 299 ?   ?   ?   A . n 
A 1 300 HIS 300 300 ?   ?   ?   A . n 
A 1 301 GLY 301 301 ?   ?   ?   A . n 
A 1 302 LEU 302 302 ?   ?   ?   A . n 
A 1 303 SER 303 303 ?   ?   ?   A . n 
A 1 304 ALA 304 304 ?   ?   ?   A . n 
A 1 305 TRP 305 305 ?   ?   ?   A . n 
A 1 306 SER 306 306 ?   ?   ?   A . n 
A 1 307 HIS 307 307 ?   ?   ?   A . n 
A 1 308 PRO 308 308 ?   ?   ?   A . n 
A 1 309 GLN 309 309 ?   ?   ?   A . n 
A 1 310 PHE 310 310 ?   ?   ?   A . n 
A 1 311 GLU 311 311 ?   ?   ?   A . n 
A 1 312 LYS 312 312 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   VAL 3   3   ?   ?   ?   B . n 
B 1 4   ASP 4   4   ?   ?   ?   B . n 
B 1 5   SER 5   5   ?   ?   ?   B . n 
B 1 6   LYS 6   6   6   LYS LYS B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   GLN 8   8   8   GLN GLN B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  GLN 10  10  10  GLN GLN B . n 
B 1 11  ARG 11  11  11  ARG ARG B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  ALA 14  14  14  ALA ALA 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  ASP 17  17  17  ASP ASP B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  MET 21  21  21  MET MET B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  ARG 23  23  23  ARG ARG B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  PHE 39  39  39  PHE PHE B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  ASN 46  46  46  ASN ASN B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  GLU 48  48  48  GLU GLU B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  GLN 52  52  52  GLN GLN B . n 
B 1 53  MET 53  53  53  MET MET B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  PRO 57  57  57  PRO PRO B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  LEU 63  63  63  LEU LEU B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  PRO 69  69  69  PRO PRO B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  PHE 72  72  72  PHE PHE B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  TYR 74  74  74  TYR TYR B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  PRO 76  76  76  PRO PRO B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  THR 80  80  80  THR THR B . n 
B 1 81  THR 81  81  81  THR THR B . n 
B 1 82  CYS 82  82  82  CYS CYS B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  PHE 85  85  85  PHE PHE B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  ILE 98  98  98  ILE ILE B . n 
B 1 99  CYS 99  99  99  CYS CYS B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 TYR 102 102 102 TYR TYR B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 GLN 104 104 104 GLN GLN B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 TYR 109 109 109 TYR TYR B . n 
B 1 110 TRP 110 110 110 TRP TRP B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 PHE 115 115 115 PHE PHE B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 ILE 119 119 119 ILE ILE B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 MET 123 123 123 MET MET B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 GLN 126 126 126 GLN GLN B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 HIS 129 129 129 HIS HIS B . n 
B 1 130 ARG 130 130 130 ARG ARG B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 HIS 135 135 135 HIS HIS B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 MET 138 138 138 MET MET B . n 
B 1 139 HIS 139 139 139 HIS HIS B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 GLN 141 141 141 GLN GLN B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 PRO 146 146 146 PRO PRO B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 PHE 154 154 154 PHE PHE B . n 
B 1 155 PRO 155 155 155 PRO PRO B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 GLU 158 158 158 GLU GLU B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 THR 160 160 160 THR THR B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 ARG 174 174 174 ARG ARG B . n 
B 1 175 TRP 175 175 175 TRP TRP B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 PRO 181 181 181 PRO PRO B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 MET 191 191 191 MET MET B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 VAL 196 196 196 VAL VAL B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 ARG 200 200 200 ARG ARG B . n 
B 1 201 GLN 201 201 201 GLN GLN B . n 
B 1 202 ARG 202 202 202 ARG ARG B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 HIS 205 205 205 HIS HIS B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 GLY 207 207 207 GLY GLY B . n 
B 1 208 GLY 208 208 208 GLY GLY B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ASN 210 210 210 ASN ASN B . n 
B 1 211 ARG 211 211 211 ARG ARG B . n 
B 1 212 THR 212 212 212 THR THR B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 LYS 216 216 216 LYS LYS B . n 
B 1 217 PRO 217 217 217 PRO PRO B . n 
B 1 218 ARG 218 218 218 ARG ARG B . n 
B 1 219 ARG 219 219 219 ARG ARG B . n 
B 1 220 VAL 220 220 220 VAL VAL B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 F2Y 224 224 224 F2Y F2Y B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 ASN 226 226 226 ASN ASN B . n 
B 1 227 SER 227 227 227 SER SER B . n 
B 1 228 VAL 228 228 228 VAL VAL B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 PRO 232 232 232 PRO PRO B . n 
B 1 233 PHE 233 233 233 PHE PHE B . n 
B 1 234 GLU 234 234 234 GLU GLU B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 ARG 237 237 237 ARG ARG B . n 
B 1 238 THR 238 238 238 THR THR B . n 
B 1 239 MET 239 239 239 MET MET B . n 
B 1 240 PRO 240 240 240 PRO PRO B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 GLU 242 242 242 GLU GLU B . n 
B 1 243 MET 243 243 243 MET MET B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 GLU 245 245 245 GLU GLU B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 MET 247 247 247 MET MET B . n 
B 1 248 THR 248 248 248 THR THR B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 GLN 252 252 252 GLN GLN B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 MET 254 254 254 MET MET B . n 
B 1 255 LEU 255 255 255 LEU LEU B . n 
B 1 256 GLY 256 256 256 GLY GLY B . n 
B 1 257 TRP 257 257 257 TRP TRP B . n 
B 1 258 ARG 258 258 258 ARG ARG B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 MET 260 260 260 MET MET B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 SER 263 263 263 SER SER B . n 
B 1 264 ASP 264 264 264 ASP ASP B . n 
B 1 265 PRO 265 265 265 PRO PRO B . n 
B 1 266 ASN 266 266 266 ASN ASN B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 GLY 269 269 269 GLY GLY B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 ASN 271 271 271 ASN ASN B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 ILE 273 273 273 ILE ILE B . n 
B 1 274 ASP 274 274 274 ASP ASP B . n 
B 1 275 ASP 275 275 275 ASP ASP B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 ARG 277 277 277 ARG ARG B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 ASN 280 280 280 ASN ASN B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLN 283 283 283 GLN GLN B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 LYS 285 285 285 LYS LYS B . n 
B 1 286 ALA 286 286 286 ALA ALA B . n 
B 1 287 ALA 287 287 287 ALA ALA B . n 
B 1 288 ASP 288 288 288 ASP ASP B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 PRO 290 290 290 PRO PRO B . n 
B 1 291 ALA 291 291 ?   ?   ?   B . n 
B 1 292 LEU 292 292 ?   ?   ?   B . n 
B 1 293 GLU 293 293 ?   ?   ?   B . n 
B 1 294 VAL 294 294 ?   ?   ?   B . n 
B 1 295 ASP 295 295 ?   ?   ?   B . n 
B 1 296 LEU 296 296 ?   ?   ?   B . n 
B 1 297 GLN 297 297 ?   ?   ?   B . n 
B 1 298 GLY 298 298 ?   ?   ?   B . n 
B 1 299 ASP 299 299 ?   ?   ?   B . n 
B 1 300 HIS 300 300 ?   ?   ?   B . n 
B 1 301 GLY 301 301 ?   ?   ?   B . n 
B 1 302 LEU 302 302 ?   ?   ?   B . n 
B 1 303 SER 303 303 ?   ?   ?   B . n 
B 1 304 ALA 304 304 ?   ?   ?   B . n 
B 1 305 TRP 305 305 ?   ?   ?   B . n 
B 1 306 SER 306 306 ?   ?   ?   B . n 
B 1 307 HIS 307 307 ?   ?   ?   B . n 
B 1 308 PRO 308 308 ?   ?   ?   B . n 
B 1 309 GLN 309 309 ?   ?   ?   B . n 
B 1 310 PHE 310 310 ?   ?   ?   B . n 
B 1 311 GLU 311 311 ?   ?   ?   B . n 
B 1 312 LYS 312 312 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FE2 ? ? FE2 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CO  ? ? CO  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 FE2 1   401 402 FE2 FE2 A . 
D 3 CO  1   402 503 CO  CO  A . 
E 2 FE2 1   501 501 FE2 FE2 B . 
F 4 HOH 1   501 193 HOH HOH A . 
F 4 HOH 2   502 210 HOH HOH A . 
F 4 HOH 3   503 39  HOH HOH A . 
F 4 HOH 4   504 41  HOH HOH A . 
F 4 HOH 5   505 220 HOH HOH A . 
F 4 HOH 6   506 17  HOH HOH A . 
F 4 HOH 7   507 64  HOH HOH A . 
F 4 HOH 8   508 151 HOH HOH A . 
F 4 HOH 9   509 44  HOH HOH A . 
F 4 HOH 10  510 113 HOH HOH A . 
F 4 HOH 11  511 35  HOH HOH A . 
F 4 HOH 12  512 157 HOH HOH A . 
F 4 HOH 13  513 212 HOH HOH A . 
F 4 HOH 14  514 140 HOH HOH A . 
F 4 HOH 15  515 11  HOH HOH A . 
F 4 HOH 16  516 43  HOH HOH A . 
F 4 HOH 17  517 92  HOH HOH A . 
F 4 HOH 18  518 148 HOH HOH A . 
F 4 HOH 19  519 136 HOH HOH A . 
F 4 HOH 20  520 105 HOH HOH A . 
F 4 HOH 21  521 96  HOH HOH A . 
F 4 HOH 22  522 5   HOH HOH A . 
F 4 HOH 23  523 38  HOH HOH A . 
F 4 HOH 24  524 106 HOH HOH A . 
F 4 HOH 25  525 101 HOH HOH A . 
F 4 HOH 26  526 24  HOH HOH A . 
F 4 HOH 27  527 195 HOH HOH A . 
F 4 HOH 28  528 98  HOH HOH A . 
F 4 HOH 29  529 76  HOH HOH A . 
F 4 HOH 30  530 81  HOH HOH A . 
F 4 HOH 31  531 57  HOH HOH A . 
F 4 HOH 32  532 69  HOH HOH A . 
F 4 HOH 33  533 2   HOH HOH A . 
F 4 HOH 34  534 170 HOH HOH A . 
F 4 HOH 35  535 22  HOH HOH A . 
F 4 HOH 36  536 77  HOH HOH A . 
F 4 HOH 37  537 13  HOH HOH A . 
F 4 HOH 38  538 20  HOH HOH A . 
F 4 HOH 39  539 54  HOH HOH A . 
F 4 HOH 40  540 68  HOH HOH A . 
F 4 HOH 41  541 110 HOH HOH A . 
F 4 HOH 42  542 188 HOH HOH A . 
F 4 HOH 43  543 31  HOH HOH A . 
F 4 HOH 44  544 36  HOH HOH A . 
F 4 HOH 45  545 51  HOH HOH A . 
F 4 HOH 46  546 89  HOH HOH A . 
F 4 HOH 47  547 32  HOH HOH A . 
F 4 HOH 48  548 28  HOH HOH A . 
F 4 HOH 49  549 153 HOH HOH A . 
F 4 HOH 50  550 198 HOH HOH A . 
F 4 HOH 51  551 102 HOH HOH A . 
F 4 HOH 52  552 120 HOH HOH A . 
F 4 HOH 53  553 100 HOH HOH A . 
F 4 HOH 54  554 52  HOH HOH A . 
F 4 HOH 55  555 25  HOH HOH A . 
F 4 HOH 56  556 115 HOH HOH A . 
F 4 HOH 57  557 74  HOH HOH A . 
F 4 HOH 58  558 86  HOH HOH A . 
F 4 HOH 59  559 166 HOH HOH A . 
F 4 HOH 60  560 200 HOH HOH A . 
F 4 HOH 61  561 209 HOH HOH A . 
F 4 HOH 62  562 1   HOH HOH A . 
F 4 HOH 63  563 143 HOH HOH A . 
F 4 HOH 64  564 62  HOH HOH A . 
F 4 HOH 65  565 109 HOH HOH A . 
F 4 HOH 66  566 85  HOH HOH A . 
F 4 HOH 67  567 117 HOH HOH A . 
F 4 HOH 68  568 80  HOH HOH A . 
F 4 HOH 69  569 155 HOH HOH A . 
F 4 HOH 70  570 216 HOH HOH A . 
F 4 HOH 71  571 30  HOH HOH A . 
F 4 HOH 72  572 160 HOH HOH A . 
F 4 HOH 73  573 218 HOH HOH A . 
F 4 HOH 74  574 199 HOH HOH A . 
F 4 HOH 75  575 47  HOH HOH A . 
F 4 HOH 76  576 221 HOH HOH A . 
F 4 HOH 77  577 72  HOH HOH A . 
F 4 HOH 78  578 34  HOH HOH A . 
F 4 HOH 79  579 152 HOH HOH A . 
F 4 HOH 80  580 191 HOH HOH A . 
F 4 HOH 81  581 65  HOH HOH A . 
F 4 HOH 82  582 108 HOH HOH A . 
F 4 HOH 83  583 149 HOH HOH A . 
F 4 HOH 84  584 84  HOH HOH A . 
F 4 HOH 85  585 83  HOH HOH A . 
F 4 HOH 86  586 131 HOH HOH A . 
F 4 HOH 87  587 154 HOH HOH A . 
F 4 HOH 88  588 55  HOH HOH A . 
F 4 HOH 89  589 167 HOH HOH A . 
F 4 HOH 90  590 180 HOH HOH A . 
F 4 HOH 91  591 181 HOH HOH A . 
F 4 HOH 92  592 141 HOH HOH A . 
F 4 HOH 93  593 78  HOH HOH A . 
F 4 HOH 94  594 91  HOH HOH A . 
F 4 HOH 95  595 183 HOH HOH A . 
F 4 HOH 96  596 128 HOH HOH A . 
F 4 HOH 97  597 211 HOH HOH A . 
F 4 HOH 98  598 217 HOH HOH A . 
F 4 HOH 99  599 94  HOH HOH A . 
F 4 HOH 100 600 12  HOH HOH A . 
F 4 HOH 101 601 122 HOH HOH A . 
F 4 HOH 102 602 186 HOH HOH A . 
F 4 HOH 103 603 202 HOH HOH A . 
G 4 HOH 1   601 213 HOH HOH B . 
G 4 HOH 2   602 187 HOH HOH B . 
G 4 HOH 3   603 23  HOH HOH B . 
G 4 HOH 4   604 75  HOH HOH B . 
G 4 HOH 5   605 45  HOH HOH B . 
G 4 HOH 6   606 73  HOH HOH B . 
G 4 HOH 7   607 71  HOH HOH B . 
G 4 HOH 8   608 194 HOH HOH B . 
G 4 HOH 9   609 29  HOH HOH B . 
G 4 HOH 10  610 139 HOH HOH B . 
G 4 HOH 11  611 88  HOH HOH B . 
G 4 HOH 12  612 196 HOH HOH B . 
G 4 HOH 13  613 121 HOH HOH B . 
G 4 HOH 14  614 66  HOH HOH B . 
G 4 HOH 15  615 50  HOH HOH B . 
G 4 HOH 16  616 104 HOH HOH B . 
G 4 HOH 17  617 144 HOH HOH B . 
G 4 HOH 18  618 133 HOH HOH B . 
G 4 HOH 19  619 185 HOH HOH B . 
G 4 HOH 20  620 165 HOH HOH B . 
G 4 HOH 21  621 8   HOH HOH B . 
G 4 HOH 22  622 61  HOH HOH B . 
G 4 HOH 23  623 33  HOH HOH B . 
G 4 HOH 24  624 58  HOH HOH B . 
G 4 HOH 25  625 46  HOH HOH B . 
G 4 HOH 26  626 93  HOH HOH B . 
G 4 HOH 27  627 16  HOH HOH B . 
G 4 HOH 28  628 145 HOH HOH B . 
G 4 HOH 29  629 63  HOH HOH B . 
G 4 HOH 30  630 129 HOH HOH B . 
G 4 HOH 31  631 10  HOH HOH B . 
G 4 HOH 32  632 42  HOH HOH B . 
G 4 HOH 33  633 59  HOH HOH B . 
G 4 HOH 34  634 177 HOH HOH B . 
G 4 HOH 35  635 7   HOH HOH B . 
G 4 HOH 36  636 114 HOH HOH B . 
G 4 HOH 37  637 53  HOH HOH B . 
G 4 HOH 38  638 205 HOH HOH B . 
G 4 HOH 39  639 70  HOH HOH B . 
G 4 HOH 40  640 3   HOH HOH B . 
G 4 HOH 41  641 147 HOH HOH B . 
G 4 HOH 42  642 116 HOH HOH B . 
G 4 HOH 43  643 163 HOH HOH B . 
G 4 HOH 44  644 21  HOH HOH B . 
G 4 HOH 45  645 4   HOH HOH B . 
G 4 HOH 46  646 158 HOH HOH B . 
G 4 HOH 47  647 95  HOH HOH B . 
G 4 HOH 48  648 219 HOH HOH B . 
G 4 HOH 49  649 27  HOH HOH B . 
G 4 HOH 50  650 126 HOH HOH B . 
G 4 HOH 51  651 6   HOH HOH B . 
G 4 HOH 52  652 135 HOH HOH B . 
G 4 HOH 53  653 132 HOH HOH B . 
G 4 HOH 54  654 79  HOH HOH B . 
G 4 HOH 55  655 87  HOH HOH B . 
G 4 HOH 56  656 14  HOH HOH B . 
G 4 HOH 57  657 142 HOH HOH B . 
G 4 HOH 58  658 9   HOH HOH B . 
G 4 HOH 59  659 26  HOH HOH B . 
G 4 HOH 60  660 204 HOH HOH B . 
G 4 HOH 61  661 82  HOH HOH B . 
G 4 HOH 62  662 203 HOH HOH B . 
G 4 HOH 63  663 118 HOH HOH B . 
G 4 HOH 64  664 150 HOH HOH B . 
G 4 HOH 65  665 107 HOH HOH B . 
G 4 HOH 66  666 48  HOH HOH B . 
G 4 HOH 67  667 67  HOH HOH B . 
G 4 HOH 68  668 159 HOH HOH B . 
G 4 HOH 69  669 192 HOH HOH B . 
G 4 HOH 70  670 119 HOH HOH B . 
G 4 HOH 71  671 137 HOH HOH B . 
G 4 HOH 72  672 99  HOH HOH B . 
G 4 HOH 73  673 208 HOH HOH B . 
G 4 HOH 74  674 206 HOH HOH B . 
G 4 HOH 75  675 97  HOH HOH B . 
G 4 HOH 76  676 19  HOH HOH B . 
G 4 HOH 77  677 40  HOH HOH B . 
G 4 HOH 78  678 37  HOH HOH B . 
G 4 HOH 79  679 111 HOH HOH B . 
G 4 HOH 80  680 223 HOH HOH B . 
G 4 HOH 81  681 197 HOH HOH B . 
G 4 HOH 82  682 18  HOH HOH B . 
G 4 HOH 83  683 134 HOH HOH B . 
G 4 HOH 84  684 130 HOH HOH B . 
G 4 HOH 85  685 15  HOH HOH B . 
G 4 HOH 86  686 60  HOH HOH B . 
G 4 HOH 87  687 90  HOH HOH B . 
G 4 HOH 88  688 161 HOH HOH B . 
G 4 HOH 89  689 178 HOH HOH B . 
G 4 HOH 90  690 182 HOH HOH B . 
G 4 HOH 91  691 124 HOH HOH B . 
G 4 HOH 92  692 56  HOH HOH B . 
G 4 HOH 93  693 190 HOH HOH B . 
G 4 HOH 94  694 207 HOH HOH B . 
G 4 HOH 95  695 125 HOH HOH B . 
G 4 HOH 96  696 127 HOH HOH B . 
G 4 HOH 97  697 112 HOH HOH B . 
G 4 HOH 98  698 184 HOH HOH B . 
G 4 HOH 99  699 179 HOH HOH B . 
G 4 HOH 100 700 146 HOH HOH B . 
G 4 HOH 101 701 174 HOH HOH B . 
G 4 HOH 102 702 214 HOH HOH B . 
G 4 HOH 103 703 49  HOH HOH B . 
G 4 HOH 104 704 173 HOH HOH B . 
G 4 HOH 105 705 138 HOH HOH B . 
G 4 HOH 106 706 103 HOH HOH B . 
G 4 HOH 107 707 222 HOH HOH B . 
G 4 HOH 108 708 176 HOH HOH B . 
G 4 HOH 109 709 156 HOH HOH B . 
G 4 HOH 110 710 175 HOH HOH B . 
G 4 HOH 111 711 169 HOH HOH B . 
G 4 HOH 112 712 123 HOH HOH B . 
G 4 HOH 113 713 215 HOH HOH B . 
G 4 HOH 114 714 201 HOH HOH B . 
G 4 HOH 115 715 168 HOH HOH B . 
G 4 HOH 116 716 171 HOH HOH B . 
G 4 HOH 117 717 164 HOH HOH B . 
G 4 HOH 118 718 162 HOH HOH B . 
G 4 HOH 119 719 172 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B LYS 59 ? CG ? B LYS 59 CG 
2 1 Y 1 B LYS 59 ? CD ? B LYS 59 CD 
3 1 Y 1 B LYS 59 ? CE ? B LYS 59 CE 
4 1 Y 1 B LYS 59 ? NZ ? B LYS 59 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.020 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J1I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.443 
_cell.length_a_esd                 ? 
_cell.length_b                     45.610 
_cell.length_b_esd                 ? 
_cell.length_c                     105.148 
_cell.length_c_esd                 ? 
_cell.volume                       285451.153 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9J1I 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J1I 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.0 
_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    
;100 mM MES pH 6.0
50 mM CoCl2
1.8 M ammonium sulfate
;
_exptl_crystal_grow.pdbx_pH_range   5.6-6.4 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-17 
_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   0.9785 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          35.20 
_reflns.entry_id                                       9J1I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.11 
_reflns.d_resolution_low                               36.08 
_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                                     32539 
_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                           99.19 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.18 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.0830 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0691 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.11 
_reflns_shell.d_res_low                                     2.19 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3155 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.686 
_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                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               41.85 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9J1I 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.11 
_refine.ls_d_res_low                             36.08 
_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                     32531 
_refine.ls_number_reflns_R_free                  1627 
_refine.ls_number_reflns_R_work                  30904 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.19 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1744 
_refine.ls_R_factor_R_free                       0.2159 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1722 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4Y5S 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.4236 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2472 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.11 
_refine_hist.d_res_low                        36.08 
_refine_hist.number_atoms_solvent             222 
_refine_hist.number_atoms_total               4726 
_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        4501 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         3 
_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' ? 0.0074  ? 4612 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8527  ? 6286 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0517  ? 703  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0081  ? 830  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0077 ? 1762 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.11 2.17  . . 131 2497 96.83 . . . . 0.2403 . . . . . . . . . . . 0.2993 
'X-RAY DIFFRACTION' 2.17 2.24  . . 135 2564 99.56 . . . . 0.2219 . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 2.24 2.33  . . 135 2557 99.81 . . . . 0.2026 . . . . . . . . . . . 0.2482 
'X-RAY DIFFRACTION' 2.33 2.42  . . 135 2566 99.63 . . . . 0.1912 . . . . . . . . . . . 0.2594 
'X-RAY DIFFRACTION' 2.42 2.53  . . 135 2582 99.67 . . . . 0.1906 . . . . . . . . . . . 0.2487 
'X-RAY DIFFRACTION' 2.53 2.66  . . 135 2555 99.78 . . . . 0.1956 . . . . . . . . . . . 0.2546 
'X-RAY DIFFRACTION' 2.66 2.83  . . 135 2573 99.74 . . . . 0.1910 . . . . . . . . . . . 0.2487 
'X-RAY DIFFRACTION' 2.83 3.05  . . 137 2586 99.27 . . . . 0.1925 . . . . . . . . . . . 0.2399 
'X-RAY DIFFRACTION' 3.05 3.35  . . 134 2554 99.22 . . . . 0.1755 . . . . . . . . . . . 0.2397 
'X-RAY DIFFRACTION' 3.35 3.84  . . 137 2606 99.31 . . . . 0.1562 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 3.84 4.83  . . 137 2602 99.20 . . . . 0.1322 . . . . . . . . . . . 0.1622 
'X-RAY DIFFRACTION' 4.83 36.08 . . 141 2662 98.28 . . . . 0.1689 . . . . . . . . . . . 0.1918 
# 
_struct.entry_id                     9J1I 
_struct.title                        'Apo structure of the F2Y224-FtmOx1 mutant with metal Iron' 
_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        9J1I 
_struct_keywords.text            'dioxygenase, non-heme, iron dependent, oxidoreductase' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FTMF_ASPFU 
_struct_ref.pdbx_db_accession          Q4WAW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVAT
TCPTFRNTVLINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPVSLSVIFPLTEFT
EENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLAYFNSVQLTPFETYRTMP
REMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPA
;
_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 9J1I A 1 ? 291 ? Q4WAW9 1 ? 291 ? 1 291 
2 1 9J1I B 1 ? 291 ? Q4WAW9 1 ? 291 ? 1 291 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9J1I LEU A 292 ? UNP Q4WAW9 ? ? 'expression tag' 292 1  
1 9J1I GLU A 293 ? UNP Q4WAW9 ? ? 'expression tag' 293 2  
1 9J1I VAL A 294 ? UNP Q4WAW9 ? ? 'expression tag' 294 3  
1 9J1I ASP A 295 ? UNP Q4WAW9 ? ? 'expression tag' 295 4  
1 9J1I LEU A 296 ? UNP Q4WAW9 ? ? 'expression tag' 296 5  
1 9J1I GLN A 297 ? UNP Q4WAW9 ? ? 'expression tag' 297 6  
1 9J1I GLY A 298 ? UNP Q4WAW9 ? ? 'expression tag' 298 7  
1 9J1I ASP A 299 ? UNP Q4WAW9 ? ? 'expression tag' 299 8  
1 9J1I HIS A 300 ? UNP Q4WAW9 ? ? 'expression tag' 300 9  
1 9J1I GLY A 301 ? UNP Q4WAW9 ? ? 'expression tag' 301 10 
1 9J1I LEU A 302 ? UNP Q4WAW9 ? ? 'expression tag' 302 11 
1 9J1I SER A 303 ? UNP Q4WAW9 ? ? 'expression tag' 303 12 
1 9J1I ALA A 304 ? UNP Q4WAW9 ? ? 'expression tag' 304 13 
1 9J1I TRP A 305 ? UNP Q4WAW9 ? ? 'expression tag' 305 14 
1 9J1I SER A 306 ? UNP Q4WAW9 ? ? 'expression tag' 306 15 
1 9J1I HIS A 307 ? UNP Q4WAW9 ? ? 'expression tag' 307 16 
1 9J1I PRO A 308 ? UNP Q4WAW9 ? ? 'expression tag' 308 17 
1 9J1I GLN A 309 ? UNP Q4WAW9 ? ? 'expression tag' 309 18 
1 9J1I PHE A 310 ? UNP Q4WAW9 ? ? 'expression tag' 310 19 
1 9J1I GLU A 311 ? UNP Q4WAW9 ? ? 'expression tag' 311 20 
1 9J1I LYS A 312 ? UNP Q4WAW9 ? ? 'expression tag' 312 21 
2 9J1I LEU B 292 ? UNP Q4WAW9 ? ? 'expression tag' 292 22 
2 9J1I GLU B 293 ? UNP Q4WAW9 ? ? 'expression tag' 293 23 
2 9J1I VAL B 294 ? UNP Q4WAW9 ? ? 'expression tag' 294 24 
2 9J1I ASP B 295 ? UNP Q4WAW9 ? ? 'expression tag' 295 25 
2 9J1I LEU B 296 ? UNP Q4WAW9 ? ? 'expression tag' 296 26 
2 9J1I GLN B 297 ? UNP Q4WAW9 ? ? 'expression tag' 297 27 
2 9J1I GLY B 298 ? UNP Q4WAW9 ? ? 'expression tag' 298 28 
2 9J1I ASP B 299 ? UNP Q4WAW9 ? ? 'expression tag' 299 29 
2 9J1I HIS B 300 ? UNP Q4WAW9 ? ? 'expression tag' 300 30 
2 9J1I GLY B 301 ? UNP Q4WAW9 ? ? 'expression tag' 301 31 
2 9J1I LEU B 302 ? UNP Q4WAW9 ? ? 'expression tag' 302 32 
2 9J1I SER B 303 ? UNP Q4WAW9 ? ? 'expression tag' 303 33 
2 9J1I ALA B 304 ? UNP Q4WAW9 ? ? 'expression tag' 304 34 
2 9J1I TRP B 305 ? UNP Q4WAW9 ? ? 'expression tag' 305 35 
2 9J1I SER B 306 ? UNP Q4WAW9 ? ? 'expression tag' 306 36 
2 9J1I HIS B 307 ? UNP Q4WAW9 ? ? 'expression tag' 307 37 
2 9J1I PRO B 308 ? UNP Q4WAW9 ? ? 'expression tag' 308 38 
2 9J1I GLN B 309 ? UNP Q4WAW9 ? ? 'expression tag' 309 39 
2 9J1I PHE B 310 ? UNP Q4WAW9 ? ? 'expression tag' 310 40 
2 9J1I GLU B 311 ? UNP Q4WAW9 ? ? 'expression tag' 311 41 
2 9J1I LYS B 312 ? UNP Q4WAW9 ? ? 'expression tag' 312 42 
# 
_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)' 5280  ? 
1 MORE         -57   ? 
1 'SSA (A^2)'  23480 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 17  ? ASP A 28  ? ASP A 17  ASP A 28  1 ? 12 
HELX_P HELX_P2  AA2 PRO A 38  ? ALA A 54  ? PRO A 38  ALA A 54  1 ? 17 
HELX_P HELX_P3  AA3 LEU A 64  ? TYR A 68  ? LEU A 64  TYR A 68  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 77  ? THR A 81  ? ASN A 77  THR A 81  5 ? 5  
HELX_P HELX_P5  AA5 CYS A 82  ? THR A 88  ? CYS A 82  THR A 88  1 ? 7  
HELX_P HELX_P6  AA6 ASN A 92  ? PHE A 103 ? ASN A 92  PHE A 103 1 ? 12 
HELX_P HELX_P7  AA7 HIS A 135 ? GLN A 141 ? HIS A 135 GLN A 141 5 ? 7  
HELX_P HELX_P8  AA8 GLY A 171 ? TRP A 175 ? GLY A 171 TRP A 175 5 ? 5  
HELX_P HELX_P9  AA9 GLU A 182 ? ALA A 186 ? GLU A 182 ALA A 186 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 240 ? SER A 246 ? PRO A 240 SER A 246 1 ? 7  
HELX_P HELX_P11 AB2 THR A 248 ? LEU A 255 ? THR A 248 LEU A 255 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 278 ? GLN A 283 ? LEU A 278 GLN A 283 1 ? 6  
HELX_P HELX_P13 AB4 ASP B 17  ? ASP B 28  ? ASP B 17  ASP B 28  1 ? 12 
HELX_P HELX_P14 AB5 PRO B 38  ? ALA B 54  ? PRO B 38  ALA B 54  1 ? 17 
HELX_P HELX_P15 AB6 LEU B 64  ? TYR B 68  ? LEU B 64  TYR B 68  5 ? 5  
HELX_P HELX_P16 AB7 ASN B 77  ? THR B 81  ? ASN B 77  THR B 81  5 ? 5  
HELX_P HELX_P17 AB8 CYS B 82  ? THR B 88  ? CYS B 82  THR B 88  1 ? 7  
HELX_P HELX_P18 AB9 ASN B 92  ? PHE B 103 ? ASN B 92  PHE B 103 1 ? 12 
HELX_P HELX_P19 AC1 HIS B 135 ? GLN B 141 ? HIS B 135 GLN B 141 5 ? 7  
HELX_P HELX_P20 AC2 GLY B 171 ? TRP B 175 ? GLY B 171 TRP B 175 5 ? 5  
HELX_P HELX_P21 AC3 GLU B 182 ? ALA B 186 ? GLU B 182 ALA B 186 5 ? 5  
HELX_P HELX_P22 AC4 PRO B 240 ? MET B 247 ? PRO B 240 MET B 247 1 ? 8  
HELX_P HELX_P23 AC5 THR B 248 ? LEU B 255 ? THR B 248 LEU B 255 1 ? 8  
HELX_P HELX_P24 AC6 LEU B 278 ? LEU B 282 ? LEU B 278 LEU B 282 1 ? 5  
# 
_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 
covale1  covale both ? A ALA 223 C   ? ? ? 1_555 A F2Y 224 N   ? ? A ALA 223 A F2Y 224 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2  covale both ? A F2Y 224 C   ? ? ? 1_555 A PHE 225 N   ? ? A F2Y 224 A PHE 225 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale3  covale both ? B ALA 223 C   ? ? ? 1_555 B F2Y 224 N   ? ? B ALA 223 B F2Y 224 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale4  covale both ? B F2Y 224 C   ? ? ? 1_555 B PHE 225 N   ? ? B F2Y 224 B PHE 225 1_555 ? ? ? ? ? ? ? 1.321 ? ? 
metalc1  metalc ?    ? A HIS 129 NE2 ? ? ? 1_555 C FE2 .   FE  ? ? A HIS 129 A FE2 401 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc2  metalc ?    ? A ASP 131 OD1 ? ? ? 1_555 C FE2 .   FE  ? ? A ASP 131 A FE2 401 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc3  metalc ?    ? A GLU 182 OE1 ? ? ? 1_555 D CO  .   CO  ? ? A GLU 182 A CO  402 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc4  metalc ?    ? A ASP 184 OD2 ? ? ? 1_555 D CO  .   CO  ? ? A ASP 184 A CO  402 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc5  metalc ?    ? A HIS 205 NE2 ? ? ? 1_555 C FE2 .   FE  ? ? A HIS 205 A FE2 401 1_555 ? ? ? ? ? ? ? 2.389 ? ? 
metalc6  metalc ?    ? C FE2 .   FE  ? ? ? 1_555 F HOH .   O   ? ? A FE2 401 A HOH 563 1_555 ? ? ? ? ? ? ? 2.530 ? ? 
metalc7  metalc ?    ? C FE2 .   FE  ? ? ? 1_555 F HOH .   O   ? ? A FE2 401 A HOH 600 1_555 ? ? ? ? ? ? ? 2.619 ? ? 
metalc8  metalc ?    ? D CO  .   CO  ? ? ? 1_555 F HOH .   O   ? ? A CO  402 A HOH 508 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc9  metalc ?    ? D CO  .   CO  ? ? ? 1_555 F HOH .   O   ? ? A CO  402 A HOH 534 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc10 metalc ?    ? D CO  .   CO  ? ? ? 1_555 F HOH .   O   ? ? A CO  402 A HOH 599 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc11 metalc ?    ? D CO  .   CO  ? ? ? 2_454 B HIS 139 NE2 ? ? A CO  402 B HIS 139 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc12 metalc ?    ? B HIS 129 NE2 ? ? ? 1_555 E FE2 .   FE  ? ? B HIS 129 B FE2 501 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc13 metalc ?    ? B ASP 131 OD1 ? ? ? 1_555 E FE2 .   FE  ? ? B ASP 131 B FE2 501 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc14 metalc ?    ? B HIS 205 NE2 ? ? ? 1_555 E FE2 .   FE  ? ? B HIS 205 B FE2 501 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc15 metalc ?    ? E FE2 .   FE  ? ? ? 1_555 G HOH .   O   ? ? B FE2 501 B HOH 615 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc16 metalc ?    ? E FE2 .   FE  ? ? ? 1_555 G HOH .   O   ? ? B FE2 501 B HOH 712 1_555 ? ? ? ? ? ? ? 2.765 ? ? 
metalc17 metalc ?    ? E FE2 .   FE  ? ? ? 1_555 G HOH .   O   ? ? B FE2 501 B HOH 713 1_555 ? ? ? ? ? ? ? 2.531 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 92.8  ? 
2  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 NE2 ? A HIS 205 ? A HIS 205 ? 1_555 91.5  ? 
3  OD1 ? A ASP 131 ? A ASP 131 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 NE2 ? A HIS 205 ? A HIS 205 ? 1_555 90.1  ? 
4  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 563 ? 1_555 176.7 ? 
5  OD1 ? A ASP 131 ? A ASP 131 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 563 ? 1_555 90.4  ? 
6  NE2 ? A HIS 205 ? A HIS 205 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 563 ? 1_555 87.5  ? 
7  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 600 ? 1_555 89.2  ? 
8  OD1 ? A ASP 131 ? A ASP 131 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 600 ? 1_555 86.9  ? 
9  NE2 ? A HIS 205 ? A HIS 205 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 600 ? 1_555 177.0 ? 
10 O   ? F HOH .   ? A HOH 563 ? 1_555 FE ? C FE2 . ? A FE2 401 ? 1_555 O   ? F HOH .   ? A HOH 600 ? 1_555 92.0  ? 
11 OE1 ? A GLU 182 ? A GLU 182 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 OD2 ? A ASP 184 ? A ASP 184 ? 1_555 81.9  ? 
12 OE1 ? A GLU 182 ? A GLU 182 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 508 ? 1_555 85.5  ? 
13 OD2 ? A ASP 184 ? A ASP 184 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 508 ? 1_555 167.3 ? 
14 OE1 ? A GLU 182 ? A GLU 182 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 534 ? 1_555 82.2  ? 
15 OD2 ? A ASP 184 ? A ASP 184 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 534 ? 1_555 90.5  ? 
16 O   ? F HOH .   ? A HOH 508 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 534 ? 1_555 86.1  ? 
17 OE1 ? A GLU 182 ? A GLU 182 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 599 ? 1_555 163.7 ? 
18 OD2 ? A ASP 184 ? A ASP 184 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 599 ? 1_555 97.9  ? 
19 O   ? F HOH .   ? A HOH 508 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 599 ? 1_555 93.7  ? 
20 O   ? F HOH .   ? A HOH 534 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 O   ? F HOH .   ? A HOH 599 ? 1_555 81.5  ? 
21 OE1 ? A GLU 182 ? A GLU 182 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 NE2 ? B HIS 139 ? B HIS 139 ? 1_555 51.3  ? 
22 OD2 ? A ASP 184 ? A ASP 184 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 NE2 ? B HIS 139 ? B HIS 139 ? 1_555 83.5  ? 
23 O   ? F HOH .   ? A HOH 508 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 NE2 ? B HIS 139 ? B HIS 139 ? 1_555 87.3  ? 
24 O   ? F HOH .   ? A HOH 534 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 NE2 ? B HIS 139 ? B HIS 139 ? 1_555 31.1  ? 
25 O   ? F HOH .   ? A HOH 599 ? 1_555 CO ? D CO  . ? A CO  402 ? 1_555 NE2 ? B HIS 139 ? B HIS 139 ? 1_555 112.5 ? 
26 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 96.1  ? 
27 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 93.0  ? 
28 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 84.7  ? 
29 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 615 ? 1_555 173.5 ? 
30 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 615 ? 1_555 90.4  ? 
31 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 615 ? 1_555 87.7  ? 
32 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 712 ? 1_555 92.8  ? 
33 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 712 ? 1_555 93.5  ? 
34 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 712 ? 1_555 174.1 ? 
35 O   ? G HOH .   ? B HOH 615 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 712 ? 1_555 86.7  ? 
36 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 713 ? 1_555 107.3 ? 
37 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 713 ? 1_555 155.6 ? 
38 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 713 ? 1_555 100.5 ? 
39 O   ? G HOH .   ? B HOH 615 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 713 ? 1_555 66.2  ? 
40 O   ? G HOH .   ? B HOH 712 ? 1_555 FE ? E FE2 . ? B FE2 501 ? 1_555 O   ? G HOH .   ? B HOH 713 ? 1_555 78.9  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 F2Y A 224 ? . . . . F2Y A 224 ? 1_555 . . . . . . . TYR 1 F2Y Fluorination 'Named protein modification' 
2 F2Y B 224 ? . . . . F2Y B 224 ? 1_555 . . . . . . . TYR 1 F2Y Fluorination 'Named protein modification' 
# 
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 ASP 264 A . ? ASP 264 A PRO 265 A ? PRO 265 A 1 10.78 
2 ASP 264 B . ? ASP 264 B PRO 265 B ? PRO 265 B 1 10.06 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 11  ? ALA A 13  ? ARG A 11  ALA A 13  
AA1 2 ALA A 30  ? LYS A 34  ? ALA A 30  LYS A 34  
AA1 3 VAL A 196 ? ARG A 200 ? VAL A 196 ARG A 200 
AA1 4 SER A 149 ? PRO A 155 ? SER A 149 PRO A 155 
AA1 5 ARG A 218 ? SER A 227 ? ARG A 218 SER A 227 
AA1 6 TYR A 109 ? ILE A 119 ? TYR A 109 ILE A 119 
AA1 7 LYS A 73  ? VAL A 75  ? LYS A 73  VAL A 75  
AA2 1 VAL A 187 ? ALA A 189 ? VAL A 187 ALA A 189 
AA2 2 THR A 166 ? VAL A 168 ? THR A 166 VAL A 168 
AA2 3 HIS A 205 ? ALA A 206 ? HIS A 205 ALA A 206 
AA3 1 LEU A 272 ? ILE A 273 ? LEU A 272 ILE A 273 
AA3 2 LYS A 276 ? ARG A 277 ? LYS A 276 ARG A 277 
AA4 1 ARG B 11  ? LEU B 12  ? ARG B 11  LEU B 12  
AA4 2 ALA B 30  ? LEU B 33  ? ALA B 30  LEU B 33  
AA4 3 VAL B 196 ? ARG B 200 ? VAL B 196 ARG B 200 
AA4 4 SER B 149 ? PRO B 155 ? SER B 149 PRO B 155 
AA4 5 ARG B 218 ? SER B 227 ? ARG B 218 SER B 227 
AA4 6 TYR B 109 ? ILE B 119 ? TYR B 109 ILE B 119 
AA4 7 TYR B 74  ? VAL B 75  ? TYR B 74  VAL B 75  
AA5 1 VAL B 187 ? LEU B 188 ? VAL B 187 LEU B 188 
AA5 2 GLU B 167 ? VAL B 168 ? GLU B 167 VAL B 168 
AA5 3 HIS B 205 ? ALA B 206 ? HIS B 205 ALA B 206 
AA6 1 LEU B 272 ? ILE B 273 ? LEU B 272 ILE B 273 
AA6 2 LYS B 276 ? ARG B 277 ? LYS B 276 ARG B 277 
# 
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 LEU A 12  ? N LEU A 12  O LYS A 34  ? O LYS A 34  
AA1 2 3 N LEU A 33  ? N LEU A 33  O VAL A 196 ? O VAL A 196 
AA1 3 4 O LEU A 197 ? O LEU A 197 N ILE A 153 ? N ILE A 153 
AA1 4 5 N PHE A 154 ? N PHE A 154 O VAL A 221 ? O VAL A 221 
AA1 5 6 O VAL A 220 ? O VAL A 220 N ARG A 117 ? N ARG A 117 
AA1 6 7 O LEU A 116 ? O LEU A 116 N VAL A 75  ? N VAL A 75  
AA2 1 2 O VAL A 187 ? O VAL A 187 N VAL A 168 ? N VAL A 168 
AA2 2 3 N GLU A 167 ? N GLU A 167 O ALA A 206 ? O ALA A 206 
AA3 1 2 N ILE A 273 ? N ILE A 273 O LYS A 276 ? O LYS A 276 
AA4 1 2 N LEU B 12  ? N LEU B 12  O ILE B 32  ? O ILE B 32  
AA4 2 3 N LEU B 33  ? N LEU B 33  O VAL B 196 ? O VAL B 196 
AA4 3 4 O LEU B 197 ? O LEU B 197 N ILE B 153 ? N ILE B 153 
AA4 4 5 N PHE B 154 ? N PHE B 154 O VAL B 221 ? O VAL B 221 
AA4 5 6 O F2Y B 224 ? O F2Y B 224 N SER B 112 ? N SER B 112 
AA4 6 7 O LEU B 116 ? O LEU B 116 N VAL B 75  ? N VAL B 75  
AA5 1 2 O VAL B 187 ? O VAL B 187 N VAL B 168 ? N VAL B 168 
AA5 2 3 N GLU B 167 ? N GLU B 167 O ALA B 206 ? O ALA B 206 
AA6 1 2 N ILE B 273 ? N ILE B 273 O LYS B 276 ? O LYS B 276 
# 
_pdbx_entry_details.entry_id                   9J1I 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 GLU A 27  ? ? -95.20  -66.31 
2 1 ASN A 77  ? ? 30.34   65.84  
3 1 THR A 88  ? ? -132.10 -58.51 
4 1 ASN A 210 ? ? -173.55 98.04  
5 1 ASN B 77  ? ? 35.97   70.46  
6 1 THR B 88  ? ? -129.26 -58.58 
7 1 ASN B 210 ? ? -167.82 101.64 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A F2Y 224 A F2Y 224 ? TYR 'modified residue' 
2 B F2Y 224 B F2Y 224 ? TYR 'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 1.702   13.739  -46.019 0.416998658284 0.587617411741 0.385884892274 -0.0478403181818  
0.114151224063    -0.127352594332   2.89513657293  2.84344150244  3.85467370609 0.902565516673  0.524267984502  -0.981917760509  
-0.124214820336  0.0290857478576  0.0501044837631    0.435765938624   0.206052582914   -0.423823285274 0.013776276961   
-0.438553716556   0.881890973329  
'X-RAY DIFFRACTION' 2  ? refined -1.986  -12.550 -32.065 0.622112023331 0.715690921734 1.10579997466  0.184753554028    
-0.0130526741179  -0.157791331245   0.289090163612 0.354713588818 2.08922874963 0.326708965274  -0.768208145815 -0.855538222976  
0.601292387167   -0.133249879437  -0.419661956055    0.259046582457   -0.72753720144   -0.187048545133 -0.754285111956  
0.109179956206    -0.650486955611 
'X-RAY DIFFRACTION' 3  ? refined -13.456 -10.005 -37.638 0.857104232223 0.570786343348 0.671843584327 -0.0715774627514  
0.0566112688606   -0.138353151028   8.97992832332  6.18864269011  7.03183575513 -0.200639795891 -3.51234639478  0.466143480654   
-0.913324460762  0.0416554842089  0.856546399079     1.49851641607    -0.930719100813  -0.427087951394 -0.390041849606  
0.818492254782    -0.204886572162 
'X-RAY DIFFRACTION' 4  ? refined -9.245  9.236   -38.475 0.264795451049 0.281769098813 0.294133497714 -0.019526820666   
0.0559853820623   -0.0345261070412  2.10169999494  1.08836106575  2.38798249058 -0.284144660662 0.422320615324  0.158742846718   
0.0144689834912  0.0647467226687  -0.0749332228321   0.145573549737   -0.253508946181  -0.17570394406  -0.120485279392  
0.128851196721    0.171127726643  
'X-RAY DIFFRACTION' 5  ? refined -8.165  8.652   -52.023 0.381522822668 0.431984691332 0.273814279764 -0.00687414823044 
0.0659689415482   -0.0795789157183  2.75209403778  1.60126618501  4.05158924749 1.07828578828   2.40041407361   -0.573404529014  
0.0355114587329  0.115740495685   -0.15098286406     0.345674627257   -0.252736976493  -0.209151867601 -0.300817246178  
-0.00656810821689 0.473263539923  
'X-RAY DIFFRACTION' 6  ? refined -7.537  9.184   -29.729 0.211404063836 0.213625114426 0.297389117776 -0.0142756441946  
0.0307298549964   -0.0375694284104  1.77634394044  2.14285276871  3.06684478203 -0.267498159458 0.0997752806963 0.479198160773   
-0.0469132324761 0.0581812488503  0.0065253402218    0.101474174855   -0.231884167032  -0.127654553564 -0.0417935669095 
0.0856627976686   0.269334877551  
'X-RAY DIFFRACTION' 7  ? refined -4.955  16.343  -14.228 0.322061696725 0.437178526169 0.379793282124 0.0290071587913   
-0.0748147340745  -0.0583925378943  2.62992957898  2.12435165554  3.10892880581 -1.48857684505  -2.61414158428  1.16487860597    
-0.043404835273  0.319703226219   -0.264480776782    -0.940482731934  0.960633044925   -0.273308152373 0.351211326166   
-0.23981678833    0.493947617077  
'X-RAY DIFFRACTION' 8  ? refined -40.617 13.670  -14.331 0.290423835857 0.278626650702 0.353174651669 -0.00177068680791 
0.0587552491595   -0.0540169028985  4.8774258106   1.2616174878   3.70509844681 0.181437726932  1.85367148005   -0.684601672383  
-0.046912099372  0.0404004474093  -0.0091155550809   -0.194989758635  -0.283938417288  0.23695885065   0.0688447595669  
0.112259086574    -0.621738863182 
'X-RAY DIFFRACTION' 9  ? refined -19.494 27.025  -9.185  0.525184582742 0.410192738204 0.500747257605 -0.0193390239642  
0.0999816337408   -0.061810285332   6.86057040686  4.09083304519  2.64176742874 0.707381286057  -3.38707881853  1.60598845709    
0.786228799672   0.119089019963   -0.854019840805    -0.771714049568  0.97771513603    -0.187126161913 -0.132755694824  
-0.658777561223   0.318772799629  
'X-RAY DIFFRACTION' 10 ? refined -30.727 15.055  -21.289 0.235781105326 0.24976529395  0.284580923246 -0.0263927551637  
0.016483055856    -0.00334417375145 1.56921576778  1.535117586    1.83942356221 -0.639890244251 0.158248261622  -0.121443523622  
-0.0358177031038 0.00803529517778 0.0235228727845    0.0130374030368  -0.0158242963308 0.107346512995  0.048893504713   
-0.0316486536337  -0.167041342903 
'X-RAY DIFFRACTION' 11 ? refined -40.828 24.262  -20.899 0.201795557609 0.264889115784 0.310332265684 0.00215356740076  
-0.00754569311676 -0.0471736616173  3.73771962439  3.58151968822  4.6811816815  -1.18448853097  0.788723842889  -0.521744621778  
0.00117163468627 0.0571401145604  -0.0640253095405   -0.0542536829532 0.292074603418   0.149435230319  0.0211694381866  
-0.418224745467   -0.137778920659 
'X-RAY DIFFRACTION' 12 ? refined -35.603 24.832  -9.724  0.276610559735 0.294884521005 0.338452824879 -0.00180319154455 
-0.0340409869315  -0.050765323567   3.06080864791  6.05638373701  3.70964294208 -2.37379645843  -1.36200680712  3.45989205819    
-0.180655217258  0.0146549791231  0.147122598425     -0.274525570663  0.436809034422   0.0945373586571 0.0900468574326  
-0.22227063102    0.0312314242133 
'X-RAY DIFFRACTION' 13 ? refined -19.268 9.193   -19.169 0.273586347241 0.225004223046 0.304556162835 0.016378952157    
-0.00162427335276 -0.0224573734847  1.70707498548  1.11580753659  4.50809820269 0.716841343444  1.3084759963    -0.420597388366  
0.0775178473487  0.0837591825789  -0.148588048295    -0.319658391597  -0.0325435755349 0.0943444320314 0.346861272585   
-0.165604616664   -0.318009468287 
'X-RAY DIFFRACTION' 14 ? refined -20.142 -2.095  -21.173 0.321654930979 0.201101717239 0.386599188271 -0.0293014597282  
-0.0230735934666  -0.0277964727267  3.20685145332  2.9834885799   4.62069942696 -1.05844627177  -0.52625404     -0.0150075434143 
-0.0203932037553 0.0284019227576  -0.000653738312801 -0.0402184068668 -0.441578999103  0.01387754315   0.0166719137275  
0.501724273197    0.225717413061  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 6   A 50  '( CHAIN A AND RESID 6:50 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 51  A 59  '( CHAIN A AND RESID 51:59 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 60  A 72  '( CHAIN A AND RESID 60:72 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 73  A 150 '( CHAIN A AND RESID 73:150 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  A 151 A 206 '( CHAIN A AND RESID 151:206 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  A 207 A 274 '( CHAIN A AND RESID 207:274 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  A 275 A 289 '( CHAIN A AND RESID 275:289 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  B 6   B 57  '( CHAIN B AND RESID 6:57 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  B 58  B 76  '( CHAIN B AND RESID 58:76 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 77  B 150 '( CHAIN B AND RESID 77:150 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 151 B 209 '( CHAIN B AND RESID 151:209 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 210 B 225 '( CHAIN B AND RESID 210:225 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 B 226 B 241 '( CHAIN B AND RESID 226:241 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 B 242 B 290 '( CHAIN B AND RESID 242:290 )' ? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A VAL 3   ? A VAL 3   
4  1 Y 1 A ASP 4   ? A ASP 4   
5  1 Y 1 A SER 5   ? A SER 5   
6  1 Y 1 A PRO 290 ? A PRO 290 
7  1 Y 1 A ALA 291 ? A ALA 291 
8  1 Y 1 A LEU 292 ? A LEU 292 
9  1 Y 1 A GLU 293 ? A GLU 293 
10 1 Y 1 A VAL 294 ? A VAL 294 
11 1 Y 1 A ASP 295 ? A ASP 295 
12 1 Y 1 A LEU 296 ? A LEU 296 
13 1 Y 1 A GLN 297 ? A GLN 297 
14 1 Y 1 A GLY 298 ? A GLY 298 
15 1 Y 1 A ASP 299 ? A ASP 299 
16 1 Y 1 A HIS 300 ? A HIS 300 
17 1 Y 1 A GLY 301 ? A GLY 301 
18 1 Y 1 A LEU 302 ? A LEU 302 
19 1 Y 1 A SER 303 ? A SER 303 
20 1 Y 1 A ALA 304 ? A ALA 304 
21 1 Y 1 A TRP 305 ? A TRP 305 
22 1 Y 1 A SER 306 ? A SER 306 
23 1 Y 1 A HIS 307 ? A HIS 307 
24 1 Y 1 A PRO 308 ? A PRO 308 
25 1 Y 1 A GLN 309 ? A GLN 309 
26 1 Y 1 A PHE 310 ? A PHE 310 
27 1 Y 1 A GLU 311 ? A GLU 311 
28 1 Y 1 A LYS 312 ? A LYS 312 
29 1 Y 1 B MET 1   ? B MET 1   
30 1 Y 1 B THR 2   ? B THR 2   
31 1 Y 1 B VAL 3   ? B VAL 3   
32 1 Y 1 B ASP 4   ? B ASP 4   
33 1 Y 1 B SER 5   ? B SER 5   
34 1 Y 1 B ALA 291 ? B ALA 291 
35 1 Y 1 B LEU 292 ? B LEU 292 
36 1 Y 1 B GLU 293 ? B GLU 293 
37 1 Y 1 B VAL 294 ? B VAL 294 
38 1 Y 1 B ASP 295 ? B ASP 295 
39 1 Y 1 B LEU 296 ? B LEU 296 
40 1 Y 1 B GLN 297 ? B GLN 297 
41 1 Y 1 B GLY 298 ? B GLY 298 
42 1 Y 1 B ASP 299 ? B ASP 299 
43 1 Y 1 B HIS 300 ? B HIS 300 
44 1 Y 1 B GLY 301 ? B GLY 301 
45 1 Y 1 B LEU 302 ? B LEU 302 
46 1 Y 1 B SER 303 ? B SER 303 
47 1 Y 1 B ALA 304 ? B ALA 304 
48 1 Y 1 B TRP 305 ? B TRP 305 
49 1 Y 1 B SER 306 ? B SER 306 
50 1 Y 1 B HIS 307 ? B HIS 307 
51 1 Y 1 B PRO 308 ? B PRO 308 
52 1 Y 1 B GLN 309 ? B GLN 309 
53 1 Y 1 B PHE 310 ? B PHE 310 
54 1 Y 1 B GLU 311 ? B GLU 311 
55 1 Y 1 B LYS 312 ? B LYS 312 
# 
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  
CO  CO   CO N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
F2Y OXT  O  N N 89  
F2Y C    C  N N 90  
F2Y O    O  N N 91  
F2Y CA   C  N S 92  
F2Y N    N  N N 93  
F2Y CB   C  N N 94  
F2Y CG   C  Y N 95  
F2Y CD1  C  Y N 96  
F2Y CE1  C  Y N 97  
F2Y F1   F  N N 98  
F2Y CD2  C  Y N 99  
F2Y CE2  C  Y N 100 
F2Y F2   F  N N 101 
F2Y CZ   C  Y N 102 
F2Y OH   O  N N 103 
F2Y HXT  H  N N 104 
F2Y HA   H  N N 105 
F2Y H    H  N N 106 
F2Y H2   H  N N 107 
F2Y H6   H  N N 108 
F2Y H7   H  N N 109 
F2Y H8   H  N N 110 
F2Y H9   H  N N 111 
F2Y H10  H  N N 112 
FE2 FE   FE N N 113 
GLN N    N  N N 114 
GLN CA   C  N S 115 
GLN C    C  N N 116 
GLN O    O  N N 117 
GLN CB   C  N N 118 
GLN CG   C  N N 119 
GLN CD   C  N N 120 
GLN OE1  O  N N 121 
GLN NE2  N  N N 122 
GLN OXT  O  N N 123 
GLN H    H  N N 124 
GLN H2   H  N N 125 
GLN HA   H  N N 126 
GLN HB2  H  N N 127 
GLN HB3  H  N N 128 
GLN HG2  H  N N 129 
GLN HG3  H  N N 130 
GLN HE21 H  N N 131 
GLN HE22 H  N N 132 
GLN HXT  H  N N 133 
GLU N    N  N N 134 
GLU CA   C  N S 135 
GLU C    C  N N 136 
GLU O    O  N N 137 
GLU CB   C  N N 138 
GLU CG   C  N N 139 
GLU CD   C  N N 140 
GLU OE1  O  N N 141 
GLU OE2  O  N N 142 
GLU OXT  O  N N 143 
GLU H    H  N N 144 
GLU H2   H  N N 145 
GLU HA   H  N N 146 
GLU HB2  H  N N 147 
GLU HB3  H  N N 148 
GLU HG2  H  N N 149 
GLU HG3  H  N N 150 
GLU HE2  H  N N 151 
GLU HXT  H  N N 152 
GLY N    N  N N 153 
GLY CA   C  N N 154 
GLY C    C  N N 155 
GLY O    O  N N 156 
GLY OXT  O  N N 157 
GLY H    H  N N 158 
GLY H2   H  N N 159 
GLY HA2  H  N N 160 
GLY HA3  H  N N 161 
GLY HXT  H  N N 162 
HIS N    N  N N 163 
HIS CA   C  N S 164 
HIS C    C  N N 165 
HIS O    O  N N 166 
HIS CB   C  N N 167 
HIS CG   C  Y N 168 
HIS ND1  N  Y N 169 
HIS CD2  C  Y N 170 
HIS CE1  C  Y N 171 
HIS NE2  N  Y N 172 
HIS OXT  O  N N 173 
HIS H    H  N N 174 
HIS H2   H  N N 175 
HIS HA   H  N N 176 
HIS HB2  H  N N 177 
HIS HB3  H  N N 178 
HIS HD1  H  N N 179 
HIS HD2  H  N N 180 
HIS HE1  H  N N 181 
HIS HE2  H  N N 182 
HIS HXT  H  N N 183 
HOH O    O  N N 184 
HOH H1   H  N N 185 
HOH H2   H  N N 186 
ILE N    N  N N 187 
ILE CA   C  N S 188 
ILE C    C  N N 189 
ILE O    O  N N 190 
ILE CB   C  N S 191 
ILE CG1  C  N N 192 
ILE CG2  C  N N 193 
ILE CD1  C  N N 194 
ILE OXT  O  N N 195 
ILE H    H  N N 196 
ILE H2   H  N N 197 
ILE HA   H  N N 198 
ILE HB   H  N N 199 
ILE HG12 H  N N 200 
ILE HG13 H  N N 201 
ILE HG21 H  N N 202 
ILE HG22 H  N N 203 
ILE HG23 H  N N 204 
ILE HD11 H  N N 205 
ILE HD12 H  N N 206 
ILE HD13 H  N N 207 
ILE HXT  H  N N 208 
LEU N    N  N N 209 
LEU CA   C  N S 210 
LEU C    C  N N 211 
LEU O    O  N N 212 
LEU CB   C  N N 213 
LEU CG   C  N N 214 
LEU CD1  C  N N 215 
LEU CD2  C  N N 216 
LEU OXT  O  N N 217 
LEU H    H  N N 218 
LEU H2   H  N N 219 
LEU HA   H  N N 220 
LEU HB2  H  N N 221 
LEU HB3  H  N N 222 
LEU HG   H  N N 223 
LEU HD11 H  N N 224 
LEU HD12 H  N N 225 
LEU HD13 H  N N 226 
LEU HD21 H  N N 227 
LEU HD22 H  N N 228 
LEU HD23 H  N N 229 
LEU HXT  H  N N 230 
LYS N    N  N N 231 
LYS CA   C  N S 232 
LYS C    C  N N 233 
LYS O    O  N N 234 
LYS CB   C  N N 235 
LYS CG   C  N N 236 
LYS CD   C  N N 237 
LYS CE   C  N N 238 
LYS NZ   N  N N 239 
LYS OXT  O  N N 240 
LYS H    H  N N 241 
LYS H2   H  N N 242 
LYS HA   H  N N 243 
LYS HB2  H  N N 244 
LYS HB3  H  N N 245 
LYS HG2  H  N N 246 
LYS HG3  H  N N 247 
LYS HD2  H  N N 248 
LYS HD3  H  N N 249 
LYS HE2  H  N N 250 
LYS HE3  H  N N 251 
LYS HZ1  H  N N 252 
LYS HZ2  H  N N 253 
LYS HZ3  H  N N 254 
LYS HXT  H  N N 255 
MET N    N  N N 256 
MET CA   C  N S 257 
MET C    C  N N 258 
MET O    O  N N 259 
MET CB   C  N N 260 
MET CG   C  N N 261 
MET SD   S  N N 262 
MET CE   C  N N 263 
MET OXT  O  N N 264 
MET H    H  N N 265 
MET H2   H  N N 266 
MET HA   H  N N 267 
MET HB2  H  N N 268 
MET HB3  H  N N 269 
MET HG2  H  N N 270 
MET HG3  H  N N 271 
MET HE1  H  N N 272 
MET HE2  H  N N 273 
MET HE3  H  N N 274 
MET HXT  H  N N 275 
PHE N    N  N N 276 
PHE CA   C  N S 277 
PHE C    C  N N 278 
PHE O    O  N N 279 
PHE CB   C  N N 280 
PHE CG   C  Y N 281 
PHE CD1  C  Y N 282 
PHE CD2  C  Y N 283 
PHE CE1  C  Y N 284 
PHE CE2  C  Y N 285 
PHE CZ   C  Y N 286 
PHE OXT  O  N N 287 
PHE H    H  N N 288 
PHE H2   H  N N 289 
PHE HA   H  N N 290 
PHE HB2  H  N N 291 
PHE HB3  H  N N 292 
PHE HD1  H  N N 293 
PHE HD2  H  N N 294 
PHE HE1  H  N N 295 
PHE HE2  H  N N 296 
PHE HZ   H  N N 297 
PHE HXT  H  N N 298 
PRO N    N  N N 299 
PRO CA   C  N S 300 
PRO C    C  N N 301 
PRO O    O  N N 302 
PRO CB   C  N N 303 
PRO CG   C  N N 304 
PRO CD   C  N N 305 
PRO OXT  O  N N 306 
PRO H    H  N N 307 
PRO HA   H  N N 308 
PRO HB2  H  N N 309 
PRO HB3  H  N N 310 
PRO HG2  H  N N 311 
PRO HG3  H  N N 312 
PRO HD2  H  N N 313 
PRO HD3  H  N N 314 
PRO HXT  H  N N 315 
SER N    N  N N 316 
SER CA   C  N S 317 
SER C    C  N N 318 
SER O    O  N N 319 
SER CB   C  N N 320 
SER OG   O  N N 321 
SER OXT  O  N N 322 
SER H    H  N N 323 
SER H2   H  N N 324 
SER HA   H  N N 325 
SER HB2  H  N N 326 
SER HB3  H  N N 327 
SER HG   H  N N 328 
SER HXT  H  N N 329 
THR N    N  N N 330 
THR CA   C  N S 331 
THR C    C  N N 332 
THR O    O  N N 333 
THR CB   C  N R 334 
THR OG1  O  N N 335 
THR CG2  C  N N 336 
THR OXT  O  N N 337 
THR H    H  N N 338 
THR H2   H  N N 339 
THR HA   H  N N 340 
THR HB   H  N N 341 
THR HG1  H  N N 342 
THR HG21 H  N N 343 
THR HG22 H  N N 344 
THR HG23 H  N N 345 
THR HXT  H  N N 346 
TRP N    N  N N 347 
TRP CA   C  N S 348 
TRP C    C  N N 349 
TRP O    O  N N 350 
TRP CB   C  N N 351 
TRP CG   C  Y N 352 
TRP CD1  C  Y N 353 
TRP CD2  C  Y N 354 
TRP NE1  N  Y N 355 
TRP CE2  C  Y N 356 
TRP CE3  C  Y N 357 
TRP CZ2  C  Y N 358 
TRP CZ3  C  Y N 359 
TRP CH2  C  Y N 360 
TRP OXT  O  N N 361 
TRP H    H  N N 362 
TRP H2   H  N N 363 
TRP HA   H  N N 364 
TRP HB2  H  N N 365 
TRP HB3  H  N N 366 
TRP HD1  H  N N 367 
TRP HE1  H  N N 368 
TRP HE3  H  N N 369 
TRP HZ2  H  N N 370 
TRP HZ3  H  N N 371 
TRP HH2  H  N N 372 
TRP HXT  H  N N 373 
TYR N    N  N N 374 
TYR CA   C  N S 375 
TYR C    C  N N 376 
TYR O    O  N N 377 
TYR CB   C  N N 378 
TYR CG   C  Y N 379 
TYR CD1  C  Y N 380 
TYR CD2  C  Y N 381 
TYR CE1  C  Y N 382 
TYR CE2  C  Y N 383 
TYR CZ   C  Y N 384 
TYR OH   O  N N 385 
TYR OXT  O  N N 386 
TYR H    H  N N 387 
TYR H2   H  N N 388 
TYR HA   H  N N 389 
TYR HB2  H  N N 390 
TYR HB3  H  N N 391 
TYR HD1  H  N N 392 
TYR HD2  H  N N 393 
TYR HE1  H  N N 394 
TYR HE2  H  N N 395 
TYR HH   H  N N 396 
TYR HXT  H  N N 397 
VAL N    N  N N 398 
VAL CA   C  N S 399 
VAL C    C  N N 400 
VAL O    O  N N 401 
VAL CB   C  N N 402 
VAL CG1  C  N N 403 
VAL CG2  C  N N 404 
VAL OXT  O  N N 405 
VAL H    H  N N 406 
VAL H2   H  N N 407 
VAL HA   H  N N 408 
VAL HB   H  N N 409 
VAL HG11 H  N N 410 
VAL HG12 H  N N 411 
VAL HG13 H  N N 412 
VAL HG21 H  N N 413 
VAL HG22 H  N N 414 
VAL HG23 H  N N 415 
VAL HXT  H  N N 416 
# 
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  
F2Y F1  CE1  sing N N 83  
F2Y OH  CZ   sing N N 84  
F2Y CE1 CZ   doub Y N 85  
F2Y CE1 CD1  sing Y N 86  
F2Y CZ  CE2  sing Y N 87  
F2Y CD1 CG   doub Y N 88  
F2Y CE2 F2   sing N N 89  
F2Y CE2 CD2  doub Y N 90  
F2Y N   CA   sing N N 91  
F2Y CG  CD2  sing Y N 92  
F2Y CG  CB   sing N N 93  
F2Y CB  CA   sing N N 94  
F2Y CA  C    sing N N 95  
F2Y O   C    doub N N 96  
F2Y C   OXT  sing N N 97  
F2Y OXT HXT  sing N N 98  
F2Y CA  HA   sing N N 99  
F2Y N   H    sing N N 100 
F2Y N   H2   sing N N 101 
F2Y CB  H6   sing N N 102 
F2Y CB  H7   sing N N 103 
F2Y CD1 H8   sing N N 104 
F2Y CD2 H9   sing N N 105 
F2Y OH  H10  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
HOH O   H1   sing N N 174 
HOH O   H2   sing N N 175 
ILE N   CA   sing N N 176 
ILE N   H    sing N N 177 
ILE N   H2   sing N N 178 
ILE CA  C    sing N N 179 
ILE CA  CB   sing N N 180 
ILE CA  HA   sing N N 181 
ILE C   O    doub N N 182 
ILE C   OXT  sing N N 183 
ILE CB  CG1  sing N N 184 
ILE CB  CG2  sing N N 185 
ILE CB  HB   sing N N 186 
ILE CG1 CD1  sing N N 187 
ILE CG1 HG12 sing N N 188 
ILE CG1 HG13 sing N N 189 
ILE CG2 HG21 sing N N 190 
ILE CG2 HG22 sing N N 191 
ILE CG2 HG23 sing N N 192 
ILE CD1 HD11 sing N N 193 
ILE CD1 HD12 sing N N 194 
ILE CD1 HD13 sing N N 195 
ILE OXT HXT  sing N N 196 
LEU N   CA   sing N N 197 
LEU N   H    sing N N 198 
LEU N   H2   sing N N 199 
LEU CA  C    sing N N 200 
LEU CA  CB   sing N N 201 
LEU CA  HA   sing N N 202 
LEU C   O    doub N N 203 
LEU C   OXT  sing N N 204 
LEU CB  CG   sing N N 205 
LEU CB  HB2  sing N N 206 
LEU CB  HB3  sing N N 207 
LEU CG  CD1  sing N N 208 
LEU CG  CD2  sing N N 209 
LEU CG  HG   sing N N 210 
LEU CD1 HD11 sing N N 211 
LEU CD1 HD12 sing N N 212 
LEU CD1 HD13 sing N N 213 
LEU CD2 HD21 sing N N 214 
LEU CD2 HD22 sing N N 215 
LEU CD2 HD23 sing N N 216 
LEU OXT HXT  sing N N 217 
LYS N   CA   sing N N 218 
LYS N   H    sing N N 219 
LYS N   H2   sing N N 220 
LYS CA  C    sing N N 221 
LYS CA  CB   sing N N 222 
LYS CA  HA   sing N N 223 
LYS C   O    doub N N 224 
LYS C   OXT  sing N N 225 
LYS CB  CG   sing N N 226 
LYS CB  HB2  sing N N 227 
LYS CB  HB3  sing N N 228 
LYS CG  CD   sing N N 229 
LYS CG  HG2  sing N N 230 
LYS CG  HG3  sing N N 231 
LYS CD  CE   sing N N 232 
LYS CD  HD2  sing N N 233 
LYS CD  HD3  sing N N 234 
LYS CE  NZ   sing N N 235 
LYS CE  HE2  sing N N 236 
LYS CE  HE3  sing N N 237 
LYS NZ  HZ1  sing N N 238 
LYS NZ  HZ2  sing N N 239 
LYS NZ  HZ3  sing N N 240 
LYS OXT HXT  sing N N 241 
MET N   CA   sing N N 242 
MET N   H    sing N N 243 
MET N   H2   sing N N 244 
MET CA  C    sing N N 245 
MET CA  CB   sing N N 246 
MET CA  HA   sing N N 247 
MET C   O    doub N N 248 
MET C   OXT  sing N N 249 
MET CB  CG   sing N N 250 
MET CB  HB2  sing N N 251 
MET CB  HB3  sing N N 252 
MET CG  SD   sing N N 253 
MET CG  HG2  sing N N 254 
MET CG  HG3  sing N N 255 
MET SD  CE   sing N N 256 
MET CE  HE1  sing N N 257 
MET CE  HE2  sing N N 258 
MET CE  HE3  sing N N 259 
MET OXT HXT  sing N N 260 
PHE N   CA   sing N N 261 
PHE N   H    sing N N 262 
PHE N   H2   sing N N 263 
PHE CA  C    sing N N 264 
PHE CA  CB   sing N N 265 
PHE CA  HA   sing N N 266 
PHE C   O    doub N N 267 
PHE C   OXT  sing N N 268 
PHE CB  CG   sing N N 269 
PHE CB  HB2  sing N N 270 
PHE CB  HB3  sing N N 271 
PHE CG  CD1  doub Y N 272 
PHE CG  CD2  sing Y N 273 
PHE CD1 CE1  sing Y N 274 
PHE CD1 HD1  sing N N 275 
PHE CD2 CE2  doub Y N 276 
PHE CD2 HD2  sing N N 277 
PHE CE1 CZ   doub Y N 278 
PHE CE1 HE1  sing N N 279 
PHE CE2 CZ   sing Y N 280 
PHE CE2 HE2  sing N N 281 
PHE CZ  HZ   sing N N 282 
PHE OXT HXT  sing N N 283 
PRO N   CA   sing N N 284 
PRO N   CD   sing N N 285 
PRO N   H    sing N N 286 
PRO CA  C    sing N N 287 
PRO CA  CB   sing N N 288 
PRO CA  HA   sing N N 289 
PRO C   O    doub N N 290 
PRO C   OXT  sing N N 291 
PRO CB  CG   sing N N 292 
PRO CB  HB2  sing N N 293 
PRO CB  HB3  sing N N 294 
PRO CG  CD   sing N N 295 
PRO CG  HG2  sing N N 296 
PRO CG  HG3  sing N N 297 
PRO CD  HD2  sing N N 298 
PRO CD  HD3  sing N N 299 
PRO OXT HXT  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
THR N   CA   sing N N 314 
THR N   H    sing N N 315 
THR N   H2   sing N N 316 
THR CA  C    sing N N 317 
THR CA  CB   sing N N 318 
THR CA  HA   sing N N 319 
THR C   O    doub N N 320 
THR C   OXT  sing N N 321 
THR CB  OG1  sing N N 322 
THR CB  CG2  sing N N 323 
THR CB  HB   sing N N 324 
THR OG1 HG1  sing N N 325 
THR CG2 HG21 sing N N 326 
THR CG2 HG22 sing N N 327 
THR CG2 HG23 sing N N 328 
THR OXT HXT  sing N N 329 
TRP N   CA   sing N N 330 
TRP N   H    sing N N 331 
TRP N   H2   sing N N 332 
TRP CA  C    sing N N 333 
TRP CA  CB   sing N N 334 
TRP CA  HA   sing N N 335 
TRP C   O    doub N N 336 
TRP C   OXT  sing N N 337 
TRP CB  CG   sing N N 338 
TRP CB  HB2  sing N N 339 
TRP CB  HB3  sing N N 340 
TRP CG  CD1  doub Y N 341 
TRP CG  CD2  sing Y N 342 
TRP CD1 NE1  sing Y N 343 
TRP CD1 HD1  sing N N 344 
TRP CD2 CE2  doub Y N 345 
TRP CD2 CE3  sing Y N 346 
TRP NE1 CE2  sing Y N 347 
TRP NE1 HE1  sing N N 348 
TRP CE2 CZ2  sing Y N 349 
TRP CE3 CZ3  doub Y N 350 
TRP CE3 HE3  sing N N 351 
TRP CZ2 CH2  doub Y N 352 
TRP CZ2 HZ2  sing N N 353 
TRP CZ3 CH2  sing Y N 354 
TRP CZ3 HZ3  sing N N 355 
TRP CH2 HH2  sing N N 356 
TRP OXT HXT  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4Y5S 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9J1I 
_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]   0.016545 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002923 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021925 
_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]   0.009658 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CO ? ? 21.85313 5.04979 ? ? 2.45200  36.11361 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428  4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 6   ? -5.45900  15.96400  -66.02200 1.000 58.40992  ? 6   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 6   ? -6.32000  15.58000  -64.90500 1.000 62.71092  ? 6   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 6   ? -5.69200  15.88600  -63.53600 1.000 58.82861  ? 6   LYS A C   1 
ATOM   4    O  O   . LYS A 1 6   ? -4.63500  15.34800  -63.20300 1.000 57.21144  ? 6   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 6   ? -6.66200  14.09200  -64.99000 1.000 66.04126  ? 6   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 6   ? -7.46100  13.57900  -63.78800 1.000 59.63333  ? 6   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 6   ? -7.65100  12.07200  -63.87400 1.000 61.69392  ? 6   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 6   ? -8.53000  11.57300  -62.74100 1.000 54.52994  ? 6   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 6   ? -8.54800  10.08400  -62.72000 1.000 53.45256  ? 6   LYS A NZ  1 
ATOM   10   N  N   . PRO A 1 7   ? -6.35800  16.72500  -62.74300 1.000 56.05730  ? 7   PRO A N   1 
ATOM   11   C  CA  . PRO A 1 7   ? -5.77800  17.16000  -61.46000 1.000 56.52977  ? 7   PRO A CA  1 
ATOM   12   C  C   . PRO A 1 7   ? -5.41800  15.97500  -60.57300 1.000 54.75496  ? 7   PRO A C   1 
ATOM   13   O  O   . PRO A 1 7   ? -6.19700  15.03200  -60.42400 1.000 54.55351  ? 7   PRO A O   1 
ATOM   14   C  CB  . PRO A 1 7   ? -6.89400  18.00900  -60.83300 1.000 55.61099  ? 7   PRO A CB  1 
ATOM   15   C  CG  . PRO A 1 7   ? -7.83000  18.34100  -61.97000 1.000 57.19054  ? 7   PRO A CG  1 
ATOM   16   C  CD  . PRO A 1 7   ? -7.73600  17.20600  -62.93300 1.000 58.57081  ? 7   PRO A CD  1 
ATOM   17   N  N   . GLN A 1 8   ? -4.22800  16.03400  -59.98300 1.000 53.66348  ? 8   GLN A N   1 
ATOM   18   C  CA  . GLN A 1 8   ? -3.70900  14.98600  -59.11200 1.000 52.68373  ? 8   GLN A CA  1 
ATOM   19   C  C   . GLN A 1 8   ? -3.65300  15.47800  -57.66900 1.000 51.50897  ? 8   GLN A C   1 
ATOM   20   O  O   . GLN A 1 8   ? -3.80800  16.66800  -57.38200 1.000 53.81127  ? 8   GLN A O   1 
ATOM   21   C  CB  . GLN A 1 8   ? -2.31600  14.53300  -59.57300 1.000 52.75237  ? 8   GLN A CB  1 
ATOM   22   C  CG  . GLN A 1 8   ? -2.27600  13.84800  -60.96300 1.000 53.20255  ? 8   GLN A CG  1 
ATOM   23   C  CD  . GLN A 1 8   ? -2.85000  12.42700  -60.92800 1.000 54.19114  ? 8   GLN A CD  1 
ATOM   24   O  OE1 . GLN A 1 8   ? -2.50800  11.62600  -60.05600 1.000 52.61973  ? 8   GLN A OE1 1 
ATOM   25   N  NE2 . GLN A 1 8   ? -3.73600  12.12200  -61.86700 1.000 55.17844  ? 8   GLN A NE2 1 
ATOM   26   N  N   . LEU A 1 9   ? -3.43700  14.53500  -56.75400 1.000 48.51761  ? 9   LEU A N   1 
ATOM   27   C  CA  . LEU A 1 9   ? -3.20400  14.88400  -55.36100 1.000 50.68984  ? 9   LEU A CA  1 
ATOM   28   C  C   . LEU A 1 9   ? -1.93400  15.71300  -55.22500 1.000 50.36770  ? 9   LEU A C   1 
ATOM   29   O  O   . LEU A 1 9   ? -0.84900  15.26300  -55.60000 1.000 48.16101  ? 9   LEU A O   1 
ATOM   30   C  CB  . LEU A 1 9   ? -3.08900  13.62000  -54.51600 1.000 50.38156  ? 9   LEU A CB  1 
ATOM   31   C  CG  . LEU A 1 9   ? -4.39000  12.95200  -54.11400 1.000 47.36875  ? 9   LEU A CG  1 
ATOM   32   C  CD1 . LEU A 1 9   ? -4.09000  11.56700  -53.61300 1.000 46.93379  ? 9   LEU A CD1 1 
ATOM   33   C  CD2 . LEU A 1 9   ? -5.10000  13.78900  -53.05400 1.000 42.90560  ? 9   LEU A CD2 1 
ATOM   34   N  N   . GLN A 1 10  ? -2.06700  16.91400  -54.67100 1.000 48.10944  ? 10  GLN A N   1 
ATOM   35   C  CA  . GLN A 1 10  ? -0.90000  17.74200  -54.41300 1.000 50.37921  ? 10  GLN A CA  1 
ATOM   36   C  C   . GLN A 1 10  ? 0.02700   17.07200  -53.40100 1.000 50.94777  ? 10  GLN A C   1 
ATOM   37   O  O   . GLN A 1 10  ? -0.41100  16.59300  -52.34900 1.000 49.48848  ? 10  GLN A O   1 
ATOM   38   C  CB  . GLN A 1 10  ? -1.33800  19.12100  -53.91900 1.000 50.71256  ? 10  GLN A CB  1 
ATOM   39   C  CG  . GLN A 1 10  ? -2.12900  19.87700  -54.96300 1.000 48.24945  ? 10  GLN A CG  1 
ATOM   40   C  CD  . GLN A 1 10  ? -1.36500  19.99300  -56.26100 1.000 55.49299  ? 10  GLN A CD  1 
ATOM   41   O  OE1 . GLN A 1 10  ? -0.21600  20.43800  -56.27700 1.000 58.75028  ? 10  GLN A OE1 1 
ATOM   42   N  NE2 . GLN A 1 10  ? -1.98800  19.57000  -57.35900 1.000 52.63511  ? 10  GLN A NE2 1 
ATOM   43   N  N   . ARG A 1 11  ? 1.30700   17.01800  -53.74900 1.000 52.10818  ? 11  ARG A N   1 
ATOM   44   C  CA  . ARG A 1 11  ? 2.36700   16.49600  -52.89600 1.000 51.99819  ? 11  ARG A CA  1 
ATOM   45   C  C   . ARG A 1 11  ? 3.07600   17.68000  -52.25100 1.000 50.35563  ? 11  ARG A C   1 
ATOM   46   O  O   . ARG A 1 11  ? 3.64900   18.51800  -52.95500 1.000 52.62168  ? 11  ARG A O   1 
ATOM   47   C  CB  . ARG A 1 11  ? 3.36200   15.67000  -53.72100 1.000 51.21742  ? 11  ARG A CB  1 
ATOM   48   C  CG  . ARG A 1 11  ? 3.06500   14.18200  -53.84700 1.000 53.86550  ? 11  ARG A CG  1 
ATOM   49   C  CD  . ARG A 1 11  ? 1.89700   13.88200  -54.78400 1.000 53.37954  ? 11  ARG A CD  1 
ATOM   50   N  NE  . ARG A 1 11  ? 1.71500   12.44200  -54.95000 1.000 55.80137  ? 11  ARG A NE  1 
ATOM   51   C  CZ  . ARG A 1 11  ? 0.72800   11.87600  -55.63500 1.000 51.65797  ? 11  ARG A CZ  1 
ATOM   52   N  NH1 . ARG A 1 11  ? -0.19700  12.60100  -56.24400 1.000 51.20452  ? 11  ARG A NH1 1 
ATOM   53   N  NH2 . ARG A 1 11  ? 0.67000   10.54900  -55.71200 1.000 47.92164  ? 11  ARG A NH2 1 
ATOM   54   N  N   . LEU A 1 12  ? 3.04200   17.75500  -50.92600 1.000 48.72963  ? 12  LEU A N   1 
ATOM   55   C  CA  . LEU A 1 12  ? 3.62900   18.88000  -50.21600 1.000 51.13118  ? 12  LEU A CA  1 
ATOM   56   C  C   . LEU A 1 12  ? 4.75500   18.40900  -49.31000 1.000 50.82714  ? 12  LEU A C   1 
ATOM   57   O  O   . LEU A 1 12  ? 4.70100   17.31400  -48.74000 1.000 50.55726  ? 12  LEU A O   1 
ATOM   58   C  CB  . LEU A 1 12  ? 2.58000   19.63700  -49.38400 1.000 50.61829  ? 12  LEU A CB  1 
ATOM   59   C  CG  . LEU A 1 12  ? 1.79500   20.72600  -50.11300 1.000 54.87700  ? 12  LEU A CG  1 
ATOM   60   C  CD1 . LEU A 1 12  ? 0.95500   20.13900  -51.23500 1.000 54.86905  ? 12  LEU A CD1 1 
ATOM   61   C  CD2 . LEU A 1 12  ? 0.92200   21.50400  -49.14700 1.000 54.95171  ? 12  LEU A CD2 1 
ATOM   62   N  N   . ALA A 1 13  ? 5.78100   19.25200  -49.18900 1.000 50.14165  ? 13  ALA A N   1 
ATOM   63   C  CA  . ALA A 1 13  ? 6.86400   18.99300  -48.24800 1.000 51.97908  ? 13  ALA A CA  1 
ATOM   64   C  C   . ALA A 1 13  ? 6.35600   19.07700  -46.80900 1.000 55.57036  ? 13  ALA A C   1 
ATOM   65   O  O   . ALA A 1 13  ? 5.43600   19.83700  -46.49300 1.000 50.45250  ? 13  ALA A O   1 
ATOM   66   C  CB  . ALA A 1 13  ? 8.00700   19.98600  -48.46100 1.000 53.60406  ? 13  ALA A CB  1 
ATOM   67   N  N   . ALA A 1 14  ? 6.97100   18.27800  -45.92900 1.000 54.24433  ? 14  ALA A N   1 
ATOM   68   C  CA  . ALA A 1 14  ? 6.56000   18.27200  -44.52700 1.000 54.14183  ? 14  ALA A CA  1 
ATOM   69   C  C   . ALA A 1 14  ? 6.58700   19.67000  -43.91700 1.000 55.11856  ? 14  ALA A C   1 
ATOM   70   O  O   . ALA A 1 14  ? 5.80600   19.94900  -43.00500 1.000 52.20202  ? 14  ALA A O   1 
ATOM   71   C  CB  . ALA A 1 14  ? 7.44500   17.32300  -43.71600 1.000 48.96546  ? 14  ALA A CB  1 
ATOM   72   N  N   . ASP A 1 15  ? 7.45200   20.56400  -44.41000 1.000 54.24728  ? 15  ASP A N   1 
ATOM   73   C  CA  . ASP A 1 15  ? 7.59200   21.90300  -43.84700 1.000 55.82939  ? 15  ASP A CA  1 
ATOM   74   C  C   . ASP A 1 15  ? 6.80200   22.96800  -44.61200 1.000 55.39721  ? 15  ASP A C   1 
ATOM   75   O  O   . ASP A 1 15  ? 7.03400   24.16100  -44.39700 1.000 55.56831  ? 15  ASP A O   1 
ATOM   76   C  CB  . ASP A 1 15  ? 9.07800   22.29500  -43.76200 1.000 58.15940  ? 15  ASP A CB  1 
ATOM   77   C  CG  . ASP A 1 15  ? 9.74000   22.49000  -45.13600 1.000 66.23927  ? 15  ASP A CG  1 
ATOM   78   O  OD1 . ASP A 1 15  ? 9.13900   22.11900  -46.17000 1.000 63.11041  ? 15  ASP A OD1 1 
ATOM   79   O  OD2 . ASP A 1 15  ? 10.88200  23.01800  -45.17700 1.000 68.40261  ? 15  ASP A OD2 1 
ATOM   80   N  N   . ALA A 1 16  ? 5.87100   22.56900  -45.48500 1.000 53.79990  ? 16  ALA A N   1 
ATOM   81   C  CA  . ALA A 1 16  ? 5.08700   23.53500  -46.24400 1.000 54.80154  ? 16  ALA A CA  1 
ATOM   82   C  C   . ALA A 1 16  ? 4.17900   24.36400  -45.33100 1.000 57.15217  ? 16  ALA A C   1 
ATOM   83   O  O   . ALA A 1 16  ? 3.93600   24.02500  -44.17000 1.000 57.87499  ? 16  ALA A O   1 
ATOM   84   C  CB  . ALA A 1 16  ? 4.25000   22.82900  -47.30800 1.000 49.94087  ? 16  ALA A CB  1 
ATOM   85   N  N   . ASP A 1 17  ? 3.66900   25.46300  -45.88200 1.000 53.18265  ? 17  ASP A N   1 
ATOM   86   C  CA  . ASP A 1 17  ? 2.80800   26.37100  -45.13500 1.000 56.50464  ? 17  ASP A CA  1 
ATOM   87   C  C   . ASP A 1 17  ? 1.45400   25.73000  -44.84600 1.000 56.91052  ? 17  ASP A C   1 
ATOM   88   O  O   . ASP A 1 17  ? 0.83900   25.11800  -45.72600 1.000 56.71010  ? 17  ASP A O   1 
ATOM   89   C  CB  . ASP A 1 17  ? 2.62400   27.66900  -45.92000 1.000 58.64214  ? 17  ASP A CB  1 
ATOM   90   C  CG  . ASP A 1 17  ? 1.58700   28.59300  -45.30400 1.000 63.51396  ? 17  ASP A CG  1 
ATOM   91   O  OD1 . ASP A 1 17  ? 1.73200   28.98000  -44.12500 1.000 65.82049  ? 17  ASP A OD1 1 
ATOM   92   O  OD2 . ASP A 1 17  ? 0.63400   28.95700  -46.01600 1.000 65.56437  ? 17  ASP A OD2 1 
ATOM   93   N  N   . VAL A 1 18  ? 0.98100   25.88600  -43.60300 1.000 56.06210  ? 18  VAL A N   1 
ATOM   94   C  CA  . VAL A 1 18  ? -0.27000  25.24000  -43.20200 1.000 54.38302  ? 18  VAL A CA  1 
ATOM   95   C  C   . VAL A 1 18  ? -1.47100  25.89600  -43.87600 1.000 54.34148  ? 18  VAL A C   1 
ATOM   96   O  O   . VAL A 1 18  ? -2.47100  25.22300  -44.15400 1.000 51.93772  ? 18  VAL A O   1 
ATOM   97   C  CB  . VAL A 1 18  ? -0.41700  25.22100  -41.66000 1.000 54.18108  ? 18  VAL A CB  1 
ATOM   98   C  CG1 . VAL A 1 18  ? -0.82000  26.58600  -41.11800 1.000 54.62777  ? 18  VAL A CG1 1 
ATOM   99   C  CG2 . VAL A 1 18  ? -1.42700  24.16400  -41.23100 1.000 48.83255  ? 18  VAL A CG2 1 
ATOM   100  N  N   . ASP A 1 19  ? -1.39900  27.20300  -44.16100 1.000 54.22069  ? 19  ASP A N   1 
ATOM   101  C  CA  . ASP A 1 19  ? -2.48100  27.85800  -44.89500 1.000 58.33868  ? 19  ASP A CA  1 
ATOM   102  C  C   . ASP A 1 19  ? -2.70400  27.19400  -46.24900 1.000 58.56841  ? 19  ASP A C   1 
ATOM   103  O  O   . ASP A 1 19  ? -3.84400  27.07700  -46.70800 1.000 60.11298  ? 19  ASP A O   1 
ATOM   104  C  CB  . ASP A 1 19  ? -2.18800  29.35200  -45.09200 1.000 61.67617  ? 19  ASP A CB  1 
ATOM   105  C  CG  . ASP A 1 19  ? -2.28000  30.15800  -43.80400 1.000 66.66665  ? 19  ASP A CG  1 
ATOM   106  O  OD1 . ASP A 1 19  ? -2.97500  29.71800  -42.86000 1.000 64.33866  ? 19  ASP A OD1 1 
ATOM   107  O  OD2 . ASP A 1 19  ? -1.66400  31.24800  -43.74800 1.000 69.44655  ? 19  ASP A OD2 1 
ATOM   108  N  N   . ARG A 1 20  ? -1.62600  26.76300  -46.90900 1.000 55.83896  ? 20  ARG A N   1 
ATOM   109  C  CA  . ARG A 1 20  ? -1.76800  26.08300  -48.19300 1.000 54.42891  ? 20  ARG A CA  1 
ATOM   110  C  C   . ARG A 1 20  ? -2.36700  24.69200  -48.01000 1.000 52.99595  ? 20  ARG A C   1 
ATOM   111  O  O   . ARG A 1 20  ? -3.22200  24.27000  -48.80000 1.000 51.66524  ? 20  ARG A O   1 
ATOM   112  C  CB  . ARG A 1 20  ? -0.41100  26.02600  -48.90700 1.000 54.51477  ? 20  ARG A CB  1 
ATOM   113  C  CG  . ARG A 1 20  ? -0.33900  25.10800  -50.13500 1.000 60.96614  ? 20  ARG A CG  1 
ATOM   114  C  CD  . ARG A 1 20  ? 0.92800   25.38400  -50.98200 1.000 68.21838  ? 20  ARG A CD  1 
ATOM   115  N  NE  . ARG A 1 20  ? 1.34500   24.23100  -51.77700 1.000 70.41008  ? 20  ARG A NE  1 
ATOM   116  C  CZ  . ARG A 1 20  ? 0.74900   23.82700  -52.89300 1.000 71.72857  ? 20  ARG A CZ  1 
ATOM   117  N  NH1 . ARG A 1 20  ? -0.30400  24.46300  -53.38700 1.000 73.72306  ? 20  ARG A NH1 1 
ATOM   118  N  NH2 . ARG A 1 20  ? 1.21500   22.75400  -53.52700 1.000 68.02609  ? 20  ARG A NH2 1 
ATOM   119  N  N   . MET A 1 21  ? -1.94600  23.96800  -46.96500 1.000 47.16463  ? 21  MET A N   1 
ATOM   120  C  CA  . MET A 1 21  ? -2.56800  22.67700  -46.67600 1.000 50.27940  ? 21  MET A CA  1 
ATOM   121  C  C   . MET A 1 21  ? -4.06800  22.83600  -46.45700 1.000 48.85687  ? 21  MET A C   1 
ATOM   122  O  O   . MET A 1 21  ? -4.85800  21.99100  -46.88800 1.000 44.97342  ? 21  MET A O   1 
ATOM   123  C  CB  . MET A 1 21  ? -1.90400  22.02500  -45.45700 1.000 48.65746  ? 21  MET A CB  1 
ATOM   124  C  CG  . MET A 1 21  ? -0.38100  21.99800  -45.53000 1.000 51.07399  ? 21  MET A CG  1 
ATOM   125  S  SD  . MET A 1 21  ? 0.46200   20.92600  -44.34200 1.000 51.42477  ? 21  MET A SD  1 
ATOM   126  C  CE  . MET A 1 21  ? 0.95600   22.03600  -43.05300 1.000 54.44111  ? 21  MET A CE  1 
ATOM   127  N  N   . CYS A 1 22  ? -4.48100  23.94200  -45.83000 1.000 49.29511  ? 22  CYS A N   1 
ATOM   128  C  CA  . CYS A 1 22  ? -5.89400  24.15400  -45.53500 1.000 50.81963  ? 22  CYS A CA  1 
ATOM   129  C  C   . CYS A 1 22  ? -6.70200  24.51300  -46.78000 1.000 51.37885  ? 22  CYS A C   1 
ATOM   130  O  O   . CYS A 1 22  ? -7.82300  24.01800  -46.94900 1.000 50.85282  ? 22  CYS A O   1 
ATOM   131  C  CB  . CYS A 1 22  ? -6.04600  25.22900  -44.46300 1.000 56.59110  ? 22  CYS A CB  1 
ATOM   132  S  SG  . CYS A 1 22  ? -6.32700  24.50200  -42.85300 1.000 67.30620  ? 22  CYS A SG  1 
ATOM   133  N  N   . ARG A 1 23  ? -6.17100  25.38400  -47.64900 1.000 50.17971  ? 23  ARG A N   1 
ATOM   134  C  CA  . ARG A 1 23  ? -6.83100  25.64100  -48.92900 1.000 53.36960  ? 23  ARG A CA  1 
ATOM   135  C  C   . ARG A 1 23  ? -7.04900  24.34800  -49.70600 1.000 49.55432  ? 23  ARG A C   1 
ATOM   136  O  O   . ARG A 1 23  ? -8.07800  24.17700  -50.36700 1.000 46.47449  ? 23  ARG A O   1 
ATOM   137  C  CB  . ARG A 1 23  ? -6.01600  26.60600  -49.80000 1.000 55.96302  ? 23  ARG A CB  1 
ATOM   138  C  CG  . ARG A 1 23  ? -5.45100  27.81700  -49.11100 1.000 65.36491  ? 23  ARG A CG  1 
ATOM   139  C  CD  . ARG A 1 23  ? -6.50200  28.61200  -48.37300 1.000 71.57223  ? 23  ARG A CD  1 
ATOM   140  N  NE  . ARG A 1 23  ? -5.88200  29.69500  -47.62100 1.000 78.99999  ? 23  ARG A NE  1 
ATOM   141  C  CZ  . ARG A 1 23  ? -5.56100  30.87400  -48.13700 1.000 83.02601  ? 23  ARG A CZ  1 
ATOM   142  N  NH1 . ARG A 1 23  ? -5.83300  31.17500  -49.39800 1.000 85.59798  ? 23  ARG A NH1 1 
ATOM   143  N  NH2 . ARG A 1 23  ? -4.94700  31.77100  -47.37000 1.000 84.78337  ? 23  ARG A NH2 1 
ATOM   144  N  N   . LEU A 1 24  ? -6.07400  23.43800  -49.66300 1.000 47.19180  ? 24  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 24  ? -6.20500  22.19300  -50.41200 1.000 47.62787  ? 24  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 24  ? -7.34000  21.33900  -49.86400 1.000 47.49937  ? 24  LEU A C   1 
ATOM   147  O  O   . LEU A 1 24  ? -8.09400  20.73300  -50.63300 1.000 42.45749  ? 24  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 24  ? -4.88900  21.42400  -50.38400 1.000 45.58161  ? 24  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 24  ? -3.77000  22.09700  -51.18200 1.000 50.22659  ? 24  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 24  ? -2.47500  21.33300  -50.99200 1.000 51.68757  ? 24  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 24  ? -4.14000  22.19100  -52.65700 1.000 48.90967  ? 24  LEU A CD2 1 
ATOM   152  N  N   . LEU A 1 25  ? -7.48500  21.29300  -48.53700 1.000 45.58556  ? 25  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 25  ? -8.54600  20.49200  -47.93400 1.000 45.65587  ? 25  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 25  ? -9.92900  21.04400  -48.24700 1.000 47.27767  ? 25  LEU A C   1 
ATOM   155  O  O   . LEU A 1 25  ? -10.90200 20.28400  -48.29000 1.000 48.03449  ? 25  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 25  ? -8.34200  20.39500  -46.41700 1.000 44.14276  ? 25  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 25  ? -7.24400  19.39600  -46.04500 1.000 39.74056  ? 25  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 25  ? -7.12800  19.22700  -44.54000 1.000 39.07473  ? 25  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 25  ? -7.48500  18.05600  -46.72200 1.000 37.96630  ? 25  LEU A CD2 1 
ATOM   160  N  N   . GLU A 1 26  ? -10.05500 22.34900  -48.45500 1.000 47.05890  ? 26  GLU A N   1 
ATOM   161  C  CA  . GLU A 1 26  ? -11.35700 22.88200  -48.82400 1.000 48.01825  ? 26  GLU A CA  1 
ATOM   162  C  C   . GLU A 1 26  ? -11.57400 22.90100  -50.33200 1.000 50.10565  ? 26  GLU A C   1 
ATOM   163  O  O   . GLU A 1 26  ? -12.72600 22.93600  -50.78000 1.000 49.74906  ? 26  GLU A O   1 
ATOM   164  C  CB  . GLU A 1 26  ? -11.53500 24.27900  -48.22500 1.000 55.39893  ? 26  GLU A CB  1 
ATOM   165  C  CG  . GLU A 1 26  ? -11.58900 24.26700  -46.68300 1.000 57.75050  ? 26  GLU A CG  1 
ATOM   166  C  CD  . GLU A 1 26  ? -12.73000 23.39600  -46.12400 1.000 61.31707  ? 26  GLU A CD  1 
ATOM   167  O  OE1 . GLU A 1 26  ? -13.87000 23.48500  -46.65400 1.000 61.06154  ? 26  GLU A OE1 1 
ATOM   168  O  OE2 . GLU A 1 26  ? -12.48000 22.61800  -45.16400 1.000 56.97677  ? 26  GLU A OE2 1 
ATOM   169  N  N   . GLU A 1 27  ? -10.50200 22.83000  -51.12200 1.000 48.93338  ? 27  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 27  ? -10.61700 22.79400  -52.57400 1.000 50.24249  ? 27  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 27  ? -10.59500 21.35300  -53.08100 1.000 49.59367  ? 27  GLU A C   1 
ATOM   172  O  O   . GLU A 1 27  ? -11.60000 20.85800  -53.60300 1.000 48.73620  ? 27  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 27  ? -9.49300  23.61800  -53.21200 1.000 53.09224  ? 27  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 27  ? -9.71900  23.95200  -54.67600 1.000 58.08655  ? 27  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 27  ? -9.11800  22.92300  -55.61100 1.000 68.74758  ? 27  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 27  ? -7.86100  22.84900  -55.68700 1.000 72.22429  ? 27  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 27  ? -9.90200  22.18800  -56.26600 1.000 66.82033  ? 27  GLU A OE2 1 
ATOM   178  N  N   . ASP A 1 28  ? -9.45800  20.66800  -52.92100 1.000 46.65638  ? 28  ASP A N   1 
ATOM   179  C  CA  . ASP A 1 28  ? -9.35500  19.27000  -53.33200 1.000 48.53854  ? 28  ASP A CA  1 
ATOM   180  C  C   . ASP A 1 28  ? -9.99600  18.32200  -52.33100 1.000 44.25127  ? 28  ASP A C   1 
ATOM   181  O  O   . ASP A 1 28  ? -10.53400 17.28600  -52.73000 1.000 43.50000  ? 28  ASP A O   1 
ATOM   182  C  CB  . ASP A 1 28  ? -7.89100  18.87200  -53.53300 1.000 44.01901  ? 28  ASP A CB  1 
ATOM   183  C  CG  . ASP A 1 28  ? -7.30200  19.44600  -54.80100 1.000 49.50839  ? 28  ASP A CG  1 
ATOM   184  O  OD1 . ASP A 1 28  ? -8.07500  20.03000  -55.58100 1.000 52.61693  ? 28  ASP A OD1 1 
ATOM   185  O  OD2 . ASP A 1 28  ? -6.07900  19.30900  -55.02200 1.000 52.36604  ? 28  ASP A OD2 1 
ATOM   186  N  N   . GLY A 1 29  ? -9.95300  18.65300  -51.04400 1.000 44.66709  ? 29  GLY A N   1 
ATOM   187  C  CA  . GLY A 1 29  ? -10.40100 17.75600  -50.00400 1.000 40.71740  ? 29  GLY A CA  1 
ATOM   188  C  C   . GLY A 1 29  ? -9.34800  16.78000  -49.52800 1.000 40.38526  ? 29  GLY A C   1 
ATOM   189  O  O   . GLY A 1 29  ? -9.61700  16.00300  -48.60500 1.000 38.44435  ? 29  GLY A O   1 
ATOM   190  N  N   . ALA A 1 30  ? -8.15900  16.79100  -50.12300 1.000 39.19393  ? 30  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 30  ? -7.11000  15.87400  -49.70000 1.000 38.60229  ? 30  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 30  ? -5.77700  16.36300  -50.24000 1.000 37.93303  ? 30  ALA A C   1 
ATOM   193  O  O   . ALA A 1 30  ? -5.72300  17.16000  -51.17900 1.000 38.86498  ? 30  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 30  ? -7.38300  14.43900  -50.16600 1.000 36.75918  ? 30  ALA A CB  1 
ATOM   195  N  N   . PHE A 1 31  ? -4.70300  15.88200  -49.62000 1.000 38.92183  ? 31  PHE A N   1 
ATOM   196  C  CA  . PHE A 1 31  ? -3.35200  16.11200  -50.11100 1.000 40.39577  ? 31  PHE A CA  1 
ATOM   197  C  C   . PHE A 1 31  ? -2.43000  15.12900  -49.40800 1.000 42.37617  ? 31  PHE A C   1 
ATOM   198  O  O   . PHE A 1 31  ? -2.82700  14.42600  -48.47700 1.000 39.43034  ? 31  PHE A O   1 
ATOM   199  C  CB  . PHE A 1 31  ? -2.89000  17.56100  -49.88800 1.000 39.91233  ? 31  PHE A CB  1 
ATOM   200  C  CG  . PHE A 1 31  ? -2.76200  17.93600  -48.44400 1.000 41.06370  ? 31  PHE A CG  1 
ATOM   201  C  CD1 . PHE A 1 31  ? -3.84200  18.45300  -47.74900 1.000 40.97890  ? 31  PHE A CD1 1 
ATOM   202  C  CD2 . PHE A 1 31  ? -1.55700  17.77600  -47.78000 1.000 47.06310  ? 31  PHE A CD2 1 
ATOM   203  C  CE1 . PHE A 1 31  ? -3.71900  18.80200  -46.41300 1.000 42.98265  ? 31  PHE A CE1 1 
ATOM   204  C  CE2 . PHE A 1 31  ? -1.43600  18.12200  -46.44000 1.000 45.04459  ? 31  PHE A CE2 1 
ATOM   205  C  CZ  . PHE A 1 31  ? -2.51200  18.62900  -45.76200 1.000 39.18919  ? 31  PHE A CZ  1 
ATOM   206  N  N   . ILE A 1 32  ? -1.18700  15.09800  -49.86500 1.000 42.71349  ? 32  ILE A N   1 
ATOM   207  C  CA  . ILE A 1 32  ? -0.18400  14.15300  -49.40100 1.000 45.12753  ? 32  ILE A CA  1 
ATOM   208  C  C   . ILE A 1 32  ? 0.98900   14.94600  -48.84400 1.000 45.41623  ? 32  ILE A C   1 
ATOM   209  O  O   . ILE A 1 32  ? 1.48500   15.86900  -49.50100 1.000 46.15903  ? 32  ILE A O   1 
ATOM   210  C  CB  . ILE A 1 32  ? 0.27700   13.22100  -50.53900 1.000 47.38707  ? 32  ILE A CB  1 
ATOM   211  C  CG1 . ILE A 1 32  ? -0.77900  12.15400  -50.83400 1.000 43.41750  ? 32  ILE A CG1 1 
ATOM   212  C  CG2 . ILE A 1 32  ? 1.62200   12.57800  -50.21000 1.000 47.54208  ? 32  ILE A CG2 1 
ATOM   213  C  CD1 . ILE A 1 32  ? -0.50300  11.38900  -52.12600 1.000 43.19217  ? 32  ILE A CD1 1 
ATOM   214  N  N   . LEU A 1 33  ? 1.41200   14.60600  -47.63000 1.000 42.26186  ? 33  LEU A N   1 
ATOM   215  C  CA  . LEU A 1 33  ? 2.64500   15.13600  -47.06200 1.000 45.44455  ? 33  LEU A CA  1 
ATOM   216  C  C   . LEU A 1 33  ? 3.78500   14.18200  -47.39300 1.000 46.69781  ? 33  LEU A C   1 
ATOM   217  O  O   . LEU A 1 33  ? 3.69000   12.98600  -47.10500 1.000 47.34224  ? 33  LEU A O   1 
ATOM   218  C  CB  . LEU A 1 33  ? 2.51900   15.29800  -45.54500 1.000 44.55192  ? 33  LEU A CB  1 
ATOM   219  C  CG  . LEU A 1 33  ? 1.69100   16.47500  -45.01400 1.000 43.86196  ? 33  LEU A CG  1 
ATOM   220  C  CD1 . LEU A 1 33  ? 1.58100   16.41000  -43.49600 1.000 46.70182  ? 33  LEU A CD1 1 
ATOM   221  C  CD2 . LEU A 1 33  ? 2.30600   17.80900  -45.44600 1.000 45.84270  ? 33  LEU A CD2 1 
ATOM   222  N  N   . LYS A 1 34  ? 4.86000   14.70500  -47.98400 1.000 45.82829  ? 34  LYS A N   1 
ATOM   223  C  CA  . LYS A 1 34  ? 5.99300   13.87800  -48.39500 1.000 50.85073  ? 34  LYS A CA  1 
ATOM   224  C  C   . LYS A 1 34  ? 7.02800   13.80900  -47.27800 1.000 51.07232  ? 34  LYS A C   1 
ATOM   225  O  O   . LYS A 1 34  ? 7.42500   14.83900  -46.72100 1.000 53.85647  ? 34  LYS A O   1 
ATOM   226  C  CB  . LYS A 1 34  ? 6.65600   14.41400  -49.67200 1.000 50.15148  ? 34  LYS A CB  1 
ATOM   227  C  CG  . LYS A 1 34  ? 5.79800   14.34300  -50.93500 1.000 53.82884  ? 34  LYS A CG  1 
ATOM   228  C  CD  . LYS A 1 34  ? 5.39500   12.91700  -51.30200 1.000 52.66386  ? 34  LYS A CD  1 
ATOM   229  C  CE  . LYS A 1 34  ? 6.56300   12.14700  -51.88000 1.000 56.10550  ? 34  LYS A CE  1 
ATOM   230  N  NZ  . LYS A 1 34  ? 6.21200   10.73600  -52.19600 1.000 57.63515  ? 34  LYS A NZ  1 
ATOM   231  N  N   . GLY A 1 35  ? 7.46800   12.59400  -46.96500 1.000 49.53468  ? 35  GLY A N   1 
ATOM   232  C  CA  . GLY A 1 35  ? 8.55100   12.39900  -46.01600 1.000 49.09297  ? 35  GLY A CA  1 
ATOM   233  C  C   . GLY A 1 35  ? 8.32000   13.01700  -44.65500 1.000 49.31789  ? 35  GLY A C   1 
ATOM   234  O  O   . GLY A 1 35  ? 9.24500   13.61400  -44.08700 1.000 48.93146  ? 35  GLY A O   1 
ATOM   235  N  N   . LEU A 1 36  ? 7.10000   12.90700  -44.12200 1.000 45.83316  ? 36  LEU A N   1 
ATOM   236  C  CA  . LEU A 1 36  ? 6.84100   13.45100  -42.79500 1.000 47.16879  ? 36  LEU A CA  1 
ATOM   237  C  C   . LEU A 1 36  ? 7.55600   12.64500  -41.72000 1.000 45.19536  ? 36  LEU A C   1 
ATOM   238  O  O   . LEU A 1 36  ? 8.16200   13.21300  -40.80400 1.000 46.48529  ? 36  LEU A O   1 
ATOM   239  C  CB  . LEU A 1 36  ? 5.34000   13.48300  -42.51900 1.000 46.93337  ? 36  LEU A CB  1 
ATOM   240  C  CG  . LEU A 1 36  ? 4.95800   14.02300  -41.14600 1.000 42.64377  ? 36  LEU A CG  1 
ATOM   241  C  CD1 . LEU A 1 36  ? 5.57500   15.41200  -40.92600 1.000 43.74505  ? 36  LEU A CD1 1 
ATOM   242  C  CD2 . LEU A 1 36  ? 3.44400   14.08400  -41.02100 1.000 43.17824  ? 36  LEU A CD2 1 
ATOM   243  N  N   . LEU A 1 37  ? 7.47700   11.30900  -41.80200 1.000 47.77263  ? 37  LEU A N   1 
ATOM   244  C  CA  . LEU A 1 37  ? 8.07800   10.43700  -40.80000 1.000 47.55093  ? 37  LEU A CA  1 
ATOM   245  C  C   . LEU A 1 37  ? 9.42400   9.95400   -41.29500 1.000 51.11022  ? 37  LEU A C   1 
ATOM   246  O  O   . LEU A 1 37  ? 9.50500   9.40300   -42.40400 1.000 48.45254  ? 37  LEU A O   1 
ATOM   247  C  CB  . LEU A 1 37  ? 7.18300   9.23400   -40.50700 1.000 47.63800  ? 37  LEU A CB  1 
ATOM   248  C  CG  . LEU A 1 37  ? 5.72600   9.52900   -40.14700 1.000 46.48328  ? 37  LEU A CG  1 
ATOM   249  C  CD1 . LEU A 1 37  ? 4.99100   8.23300   -39.86400 1.000 44.21090  ? 37  LEU A CD1 1 
ATOM   250  C  CD2 . LEU A 1 37  ? 5.63200   10.47400  -38.96500 1.000 42.26710  ? 37  LEU A CD2 1 
ATOM   251  N  N   . PRO A 1 38  ? 10.49000  10.13500  -40.51600 1.000 52.64960  ? 38  PRO A N   1 
ATOM   252  C  CA  . PRO A 1 38  ? 11.79700  9.61800   -40.92800 1.000 52.87510  ? 38  PRO A CA  1 
ATOM   253  C  C   . PRO A 1 38  ? 11.77900  8.10100   -41.01300 1.000 55.77543  ? 38  PRO A C   1 
ATOM   254  O  O   . PRO A 1 38  ? 10.88300  7.42700   -40.49800 1.000 52.78884  ? 38  PRO A O   1 
ATOM   255  C  CB  . PRO A 1 38  ? 12.74300  10.10200  -39.82400 1.000 57.82994  ? 38  PRO A CB  1 
ATOM   256  C  CG  . PRO A 1 38  ? 11.99900  11.19500  -39.11900 1.000 58.38160  ? 38  PRO A CG  1 
ATOM   257  C  CD  . PRO A 1 38  ? 10.55200  10.84300  -39.22900 1.000 49.20279  ? 38  PRO A CD  1 
ATOM   258  N  N   . PHE A 1 39  ? 12.80200  7.56400   -41.67400 1.000 56.59579  ? 39  PHE A N   1 
ATOM   259  C  CA  . PHE A 1 39  ? 12.86900  6.12700   -41.90900 1.000 56.28392  ? 39  PHE A CA  1 
ATOM   260  C  C   . PHE A 1 39  ? 12.97400  5.34500   -40.60400 1.000 58.69176  ? 39  PHE A C   1 
ATOM   261  O  O   . PHE A 1 39  ? 12.41300  4.24800   -40.48300 1.000 57.85234  ? 39  PHE A O   1 
ATOM   262  C  CB  . PHE A 1 39  ? 14.05700  5.82100   -42.82100 1.000 62.77349  ? 39  PHE A CB  1 
ATOM   263  C  CG  . PHE A 1 39  ? 14.34400  4.35700   -42.97600 1.000 68.97763  ? 39  PHE A CG  1 
ATOM   264  C  CD1 . PHE A 1 39  ? 13.57400  3.56800   -43.82800 1.000 70.74329  ? 39  PHE A CD1 1 
ATOM   265  C  CD2 . PHE A 1 39  ? 15.39300  3.77000   -42.28300 1.000 69.00653  ? 39  PHE A CD2 1 
ATOM   266  C  CE1 . PHE A 1 39  ? 13.84200  2.21900   -43.98000 1.000 67.30433  ? 39  PHE A CE1 1 
ATOM   267  C  CE2 . PHE A 1 39  ? 15.66600  2.42200   -42.42900 1.000 73.00342  ? 39  PHE A CE2 1 
ATOM   268  C  CZ  . PHE A 1 39  ? 14.88800  1.64400   -43.27900 1.000 69.32915  ? 39  PHE A CZ  1 
ATOM   269  N  N   . ASP A 1 40  ? 13.70400  5.88000   -39.62100 1.000 62.52124  ? 40  ASP A N   1 
ATOM   270  C  CA  . ASP A 1 40  ? 13.85800  5.16800   -38.35400 1.000 63.32993  ? 40  ASP A CA  1 
ATOM   271  C  C   . ASP A 1 40  ? 12.53800  5.08700   -37.58600 1.000 62.15709  ? 40  ASP A C   1 
ATOM   272  O  O   . ASP A 1 40  ? 12.30000  4.11000   -36.86400 1.000 60.62536  ? 40  ASP A O   1 
ATOM   273  C  CB  . ASP A 1 40  ? 14.94500  5.83500   -37.50600 1.000 63.92449  ? 40  ASP A CB  1 
ATOM   274  C  CG  . ASP A 1 40  ? 14.66200  7.30900   -37.22900 1.000 69.50207  ? 40  ASP A CG  1 
ATOM   275  O  OD1 . ASP A 1 40  ? 13.61900  7.83700   -37.66900 1.000 68.20816  ? 40  ASP A OD1 1 
ATOM   276  O  OD2 . ASP A 1 40  ? 15.49600  7.94800   -36.56000 1.000 82.20939  ? 40  ASP A OD2 1 
ATOM   277  N  N   . VAL A 1 41  ? 11.67400  6.09500   -37.72800 1.000 57.81759  ? 41  VAL A N   1 
ATOM   278  C  CA  . VAL A 1 41  ? 10.33300  6.00700   -37.15500 1.000 58.26205  ? 41  VAL A CA  1 
ATOM   279  C  C   . VAL A 1 41  ? 9.51900   4.93900   -37.87200 1.000 56.36467  ? 41  VAL A C   1 
ATOM   280  O  O   . VAL A 1 41  ? 8.84400   4.11800   -37.23800 1.000 51.22517  ? 41  VAL A O   1 
ATOM   281  C  CB  . VAL A 1 41  ? 9.64300   7.38000   -37.22000 1.000 53.55126  ? 41  VAL A CB  1 
ATOM   282  C  CG1 . VAL A 1 41  ? 8.19400   7.26700   -36.79200 1.000 53.78630  ? 41  VAL A CG1 1 
ATOM   283  C  CG2 . VAL A 1 41  ? 10.38200  8.37100   -36.35100 1.000 51.92281  ? 41  VAL A CG2 1 
ATOM   284  N  N   . VAL A 1 42  ? 9.58600   4.92400   -39.20700 1.000 56.09064  ? 42  VAL A N   1 
ATOM   285  C  CA  . VAL A 1 42  ? 8.82000   3.96300   -39.99800 1.000 57.21907  ? 42  VAL A CA  1 
ATOM   286  C  C   . VAL A 1 42  ? 9.27200   2.53500   -39.70400 1.000 54.40647  ? 42  VAL A C   1 
ATOM   287  O  O   . VAL A 1 42  ? 8.45100   1.61100   -39.64600 1.000 53.04336  ? 42  VAL A O   1 
ATOM   288  C  CB  . VAL A 1 42  ? 8.93700   4.29800   -41.49900 1.000 58.49967  ? 42  VAL A CB  1 
ATOM   289  C  CG1 . VAL A 1 42  ? 8.34800   3.17800   -42.35600 1.000 51.99610  ? 42  VAL A CG1 1 
ATOM   290  C  CG2 . VAL A 1 42  ? 8.25800   5.63900   -41.80000 1.000 53.57070  ? 42  VAL A CG2 1 
ATOM   291  N  N   . GLU A 1 43  ? 10.57400  2.32900   -39.50100 1.000 57.13391  ? 43  GLU A N   1 
ATOM   292  C  CA  . GLU A 1 43  ? 11.07600  0.97200   -39.28400 1.000 58.26158  ? 43  GLU A CA  1 
ATOM   293  C  C   . GLU A 1 43  ? 10.68300  0.45000   -37.90500 1.000 56.16494  ? 43  GLU A C   1 
ATOM   294  O  O   . GLU A 1 43  ? 10.21500  -0.68600  -37.77700 1.000 57.21094  ? 43  GLU A O   1 
ATOM   295  C  CB  . GLU A 1 43  ? 12.59600  0.92700   -39.47000 1.000 62.71331  ? 43  GLU A CB  1 
ATOM   296  C  CG  . GLU A 1 43  ? 13.15200  -0.45400  -39.89100 1.000 67.57858  ? 43  GLU A CG  1 
ATOM   297  C  CD  . GLU A 1 43  ? 14.66000  -0.44600  -40.16400 1.000 77.98635  ? 43  GLU A CD  1 
ATOM   298  O  OE1 . GLU A 1 43  ? 15.29700  0.61300   -39.97100 1.000 76.18889  ? 43  GLU A OE1 1 
ATOM   299  O  OE2 . GLU A 1 43  ? 15.21200  -1.49900  -40.57300 1.000 78.47612  ? 43  GLU A OE2 1 
ATOM   300  N  N   . SER A 1 44  ? 10.85000  1.26800   -36.86100 1.000 53.89300  ? 44  SER A N   1 
ATOM   301  C  CA  . SER A 1 44  ? 10.50900  0.81300   -35.51400 1.000 54.67783  ? 44  SER A CA  1 
ATOM   302  C  C   . SER A 1 44  ? 9.00100   0.64300   -35.35400 1.000 53.11025  ? 44  SER A C   1 
ATOM   303  O  O   . SER A 1 44  ? 8.54100   -0.30500  -34.70700 1.000 50.97292  ? 44  SER A O   1 
ATOM   304  C  CB  . SER A 1 44  ? 11.06500  1.78500   -34.47400 1.000 54.58129  ? 44  SER A CB  1 
ATOM   305  O  OG  . SER A 1 44  ? 10.41600  3.04200   -34.54800 1.000 58.28464  ? 44  SER A OG  1 
ATOM   306  N  N   . PHE A 1 45  ? 8.21500   1.54200   -35.94300 1.000 52.28275  ? 45  PHE A N   1 
ATOM   307  C  CA  . PHE A 1 45  ? 6.77200   1.34300   -35.98100 1.000 51.63663  ? 45  PHE A CA  1 
ATOM   308  C  C   . PHE A 1 45  ? 6.43000   0.01300   -36.64600 1.000 50.48981  ? 45  PHE A C   1 
ATOM   309  O  O   . PHE A 1 45  ? 5.61600   -0.76100  -36.13000 1.000 49.93194  ? 45  PHE A O   1 
ATOM   310  C  CB  . PHE A 1 45  ? 6.11300   2.51400   -36.71400 1.000 49.47169  ? 45  PHE A CB  1 
ATOM   311  C  CG  . PHE A 1 45  ? 4.62800   2.61700   -36.51100 1.000 48.82436  ? 45  PHE A CG  1 
ATOM   312  C  CD1 . PHE A 1 45  ? 3.96900   1.79000   -35.61000 1.000 45.43186  ? 45  PHE A CD1 1 
ATOM   313  C  CD2 . PHE A 1 45  ? 3.88400   3.54300   -37.22900 1.000 42.42867  ? 45  PHE A CD2 1 
ATOM   314  C  CE1 . PHE A 1 45  ? 2.61000   1.89500   -35.42000 1.000 43.45066  ? 45  PHE A CE1 1 
ATOM   315  C  CE2 . PHE A 1 45  ? 2.52100   3.64100   -37.04600 1.000 41.78890  ? 45  PHE A CE2 1 
ATOM   316  C  CZ  . PHE A 1 45  ? 1.88400   2.81300   -36.13600 1.000 42.09907  ? 45  PHE A CZ  1 
ATOM   317  N  N   . ASN A 1 46  ? 7.06500   -0.28000  -37.78500 1.000 53.02862  ? 46  ASN A N   1 
ATOM   318  C  CA  . ASN A 1 46  ? 6.80400   -1.54500  -38.46600 1.000 52.65391  ? 46  ASN A CA  1 
ATOM   319  C  C   . ASN A 1 46  ? 7.21800   -2.73000  -37.60600 1.000 52.22922  ? 46  ASN A C   1 
ATOM   320  O  O   . ASN A 1 46  ? 6.51900   -3.75000  -37.57000 1.000 50.31616  ? 46  ASN A O   1 
ATOM   321  C  CB  . ASN A 1 46  ? 7.50800   -1.56900  -39.82500 1.000 51.35019  ? 46  ASN A CB  1 
ATOM   322  C  CG  . ASN A 1 46  ? 6.60700   -1.06800  -40.94900 1.000 51.75501  ? 46  ASN A CG  1 
ATOM   323  O  OD1 . ASN A 1 46  ? 5.41300   -1.35600  -40.96200 1.000 48.24251  ? 46  ASN A OD1 1 
ATOM   324  N  ND2 . ASN A 1 46  ? 7.16900   -0.30200  -41.88000 1.000 50.16377  ? 46  ASN A ND2 1 
ATOM   325  N  N   . ARG A 1 47  ? 8.32800   -2.59900  -36.87400 1.000 50.67925  ? 47  ARG A N   1 
ATOM   326  C  CA  . ARG A 1 47  ? 8.73100   -3.65800  -35.95100 1.000 54.84316  ? 47  ARG A CA  1 
ATOM   327  C  C   . ARG A 1 47  ? 7.71500   -3.83100  -34.82300 1.000 55.73252  ? 47  ARG A C   1 
ATOM   328  O  O   . ARG A 1 47  ? 7.41500   -4.96200  -34.42200 1.000 56.80404  ? 47  ARG A O   1 
ATOM   329  C  CB  . ARG A 1 47  ? 10.11700  -3.36000  -35.38300 1.000 56.47894  ? 47  ARG A CB  1 
ATOM   330  C  CG  . ARG A 1 47  ? 10.85100  -4.58000  -34.83300 1.000 68.43028  ? 47  ARG A CG  1 
ATOM   331  C  CD  . ARG A 1 47  ? 11.18800  -5.57000  -35.94300 1.000 73.30470  ? 47  ARG A CD  1 
ATOM   332  N  NE  . ARG A 1 47  ? 12.31700  -6.41200  -35.57100 1.000 82.09036  ? 47  ARG A NE  1 
ATOM   333  C  CZ  . ARG A 1 47  ? 13.58700  -6.05800  -35.71200 1.000 82.29461  ? 47  ARG A CZ  1 
ATOM   334  N  NH1 . ARG A 1 47  ? 13.92300  -4.89100  -36.24100 1.000 83.90762  ? 47  ARG A NH1 1 
ATOM   335  N  NH2 . ARG A 1 47  ? 14.54200  -6.89000  -35.30500 1.000 76.89686  ? 47  ARG A NH2 1 
ATOM   336  N  N   . GLU A 1 48  ? 7.17300   -2.72800  -34.29500 1.000 49.88513  ? 48  GLU A N   1 
ATOM   337  C  CA  . GLU A 1 48  ? 6.19600   -2.84700  -33.21600 1.000 50.51587  ? 48  GLU A CA  1 
ATOM   338  C  C   . GLU A 1 48  ? 4.90400   -3.49300  -33.70600 1.000 51.15478  ? 48  GLU A C   1 
ATOM   339  O  O   . GLU A 1 48  ? 4.28200   -4.27300  -32.97700 1.000 52.67757  ? 48  GLU A O   1 
ATOM   340  C  CB  . GLU A 1 48  ? 5.92900   -1.47800  -32.60200 1.000 51.27034  ? 48  GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 48  ? 7.15900   -0.87700  -31.93100 1.000 49.50538  ? 48  GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 48  ? 7.04000   0.61900   -31.74700 1.000 49.74606  ? 48  GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 48  ? 5.94300   1.15700   -32.01600 1.000 49.77251  ? 48  GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 48  ? 8.03900   1.25600   -31.34100 1.000 52.15033  ? 48  GLU A OE2 1 
ATOM   345  N  N   . LEU A 1 49  ? 4.50200   -3.20500  -34.94700 1.000 51.14449  ? 49  LEU A N   1 
ATOM   346  C  CA  . LEU A 1 49  ? 3.34100   -3.87200  -35.53100 1.000 52.87295  ? 49  LEU A CA  1 
ATOM   347  C  C   . LEU A 1 49  ? 3.61000   -5.33800  -35.86300 1.000 56.77035  ? 49  LEU A C   1 
ATOM   348  O  O   . LEU A 1 49  ? 2.69000   -6.15700  -35.77300 1.000 57.41722  ? 49  LEU A O   1 
ATOM   349  C  CB  . LEU A 1 49  ? 2.88500   -3.12700  -36.77900 1.000 48.41449  ? 49  LEU A CB  1 
ATOM   350  C  CG  . LEU A 1 49  ? 2.39900   -1.72700  -36.42500 1.000 50.78634  ? 49  LEU A CG  1 
ATOM   351  C  CD1 . LEU A 1 49  ? 2.38900   -0.89100  -37.65300 1.000 45.11680  ? 49  LEU A CD1 1 
ATOM   352  C  CD2 . LEU A 1 49  ? 1.01800   -1.78400  -35.79100 1.000 44.83384  ? 49  LEU A CD2 1 
ATOM   353  N  N   . ASP A 1 50  ? 4.83800   -5.68900  -36.26700 1.000 55.32889  ? 50  ASP A N   1 
ATOM   354  C  CA  . ASP A 1 50  ? 5.15600   -7.10000  -36.49400 1.000 54.78979  ? 50  ASP A CA  1 
ATOM   355  C  C   . ASP A 1 50  ? 4.92500   -7.92400  -35.23400 1.000 57.82777  ? 50  ASP A C   1 
ATOM   356  O  O   . ASP A 1 50  ? 4.45300   -9.06300  -35.30500 1.000 59.72561  ? 50  ASP A O   1 
ATOM   357  C  CB  . ASP A 1 50  ? 6.60200   -7.25900  -36.97000 1.000 57.87472  ? 50  ASP A CB  1 
ATOM   358  C  CG  . ASP A 1 50  ? 6.82700   -6.70500  -38.37100 1.000 62.32150  ? 50  ASP A CG  1 
ATOM   359  O  OD1 . ASP A 1 50  ? 5.83400   -6.55400  -39.12000 1.000 61.96841  ? 50  ASP A OD1 1 
ATOM   360  O  OD2 . ASP A 1 50  ? 7.99900   -6.42800  -38.72600 1.000 62.50854  ? 50  ASP A OD2 1 
ATOM   361  N  N   . VAL A 1 51  ? 5.24300   -7.35800  -34.06800 1.000 60.14992  ? 51  VAL A N   1 
ATOM   362  C  CA  . VAL A 1 51  ? 5.01300   -8.05100  -32.80200 1.000 60.86900  ? 51  VAL A CA  1 
ATOM   363  C  C   . VAL A 1 51  ? 3.52600   -8.33800  -32.61100 1.000 62.80893  ? 51  VAL A C   1 
ATOM   364  O  O   . VAL A 1 51  ? 3.12800   -9.45200  -32.24400 1.000 62.46772  ? 51  VAL A O   1 
ATOM   365  C  CB  . VAL A 1 51  ? 5.58100   -7.22100  -31.63500 1.000 61.29005  ? 51  VAL A CB  1 
ATOM   366  C  CG1 . VAL A 1 51  ? 5.22600   -7.85800  -30.29100 1.000 64.43087  ? 51  VAL A CG1 1 
ATOM   367  C  CG2 . VAL A 1 51  ? 7.08500   -7.06100  -31.77600 1.000 57.94293  ? 51  VAL A CG2 1 
ATOM   368  N  N   . GLN A 1 52  ? 2.67800   -7.33600  -32.85500 1.000 61.56389  ? 52  GLN A N   1 
ATOM   369  C  CA  . GLN A 1 52  ? 1.24600   -7.54200  -32.67000 1.000 62.43769  ? 52  GLN A CA  1 
ATOM   370  C  C   . GLN A 1 52  ? 0.68500   -8.49600  -33.71900 1.000 63.68158  ? 52  GLN A C   1 
ATOM   371  O  O   . GLN A 1 52  ? -0.18300  -9.32200  -33.41000 1.000 65.40093  ? 52  GLN A O   1 
ATOM   372  C  CB  . GLN A 1 52  ? 0.52200   -6.19700  -32.68900 1.000 59.68054  ? 52  GLN A CB  1 
ATOM   373  C  CG  . GLN A 1 52  ? 1.00200   -5.27200  -31.58600 1.000 58.13823  ? 52  GLN A CG  1 
ATOM   374  C  CD  . GLN A 1 52  ? 0.85300   -5.89700  -30.20000 1.000 57.41048  ? 52  GLN A CD  1 
ATOM   375  O  OE1 . GLN A 1 52  ? -0.25400  -6.22900  -29.77100 1.000 57.61961  ? 52  GLN A OE1 1 
ATOM   376  N  NE2 . GLN A 1 52  ? 1.97000   -6.05300  -29.49400 1.000 56.60660  ? 52  GLN A NE2 1 
ATOM   377  N  N   . MET A 1 53  ? 1.18100   -8.40800  -34.95700 1.000 63.24556  ? 53  MET A N   1 
ATOM   378  C  CA  . MET A 1 53  ? 0.76700   -9.32500  -36.02000 1.000 64.87852  ? 53  MET A CA  1 
ATOM   379  C  C   . MET A 1 53  ? 1.08200   -10.78100 -35.68900 1.000 68.43025  ? 53  MET A C   1 
ATOM   380  O  O   . MET A 1 53  ? 0.41500   -11.68200 -36.21000 1.000 67.18784  ? 53  MET A O   1 
ATOM   381  C  CB  . MET A 1 53  ? 1.43900   -8.94800  -37.35100 1.000 65.07976  ? 53  MET A CB  1 
ATOM   382  C  CG  . MET A 1 53  ? 1.01200   -7.60400  -37.94500 1.000 64.83607  ? 53  MET A CG  1 
ATOM   383  S  SD  . MET A 1 53  ? -0.72400  -7.56800  -38.40900 1.000 70.56798  ? 53  MET A SD  1 
ATOM   384  C  CE  . MET A 1 53  ? -0.73300  -8.95500  -39.55300 1.000 68.04544  ? 53  MET A CE  1 
ATOM   385  N  N   . ALA A 1 54  ? 2.07800   -11.03300 -34.83900 1.000 69.76876  ? 54  ALA A N   1 
ATOM   386  C  CA  . ALA A 1 54  ? 2.47300   -12.38500 -34.47400 1.000 69.86364  ? 54  ALA A CA  1 
ATOM   387  C  C   . ALA A 1 54  ? 1.75600   -12.89200 -33.23000 1.000 73.01864  ? 54  ALA A C   1 
ATOM   388  O  O   . ALA A 1 54  ? 2.11800   -13.95300 -32.71500 1.000 77.52143  ? 54  ALA A O   1 
ATOM   389  C  CB  . ALA A 1 54  ? 3.99000   -12.45000 -34.27000 1.000 65.83677  ? 54  ALA A CB  1 
ATOM   390  N  N   . ILE A 1 55  ? 0.76400   -12.16300 -32.73700 1.000 72.85643  ? 55  ILE A N   1 
ATOM   391  C  CA  . ILE A 1 55  ? 0.00200   -12.61400 -31.56800 1.000 78.07499  ? 55  ILE A CA  1 
ATOM   392  C  C   . ILE A 1 55  ? -0.97400  -13.69100 -32.01800 1.000 82.51160  ? 55  ILE A C   1 
ATOM   393  O  O   . ILE A 1 55  ? -1.67700  -13.50000 -33.02100 1.000 84.71347  ? 55  ILE A O   1 
ATOM   394  C  CB  . ILE A 1 55  ? -0.73200  -11.44500 -30.91500 1.000 78.50986  ? 55  ILE A CB  1 
ATOM   395  C  CG1 . ILE A 1 55  ? 0.25900   -10.38000 -30.42900 1.000 74.42190  ? 55  ILE A CG1 1 
ATOM   396  C  CG2 . ILE A 1 55  ? -1.59200  -11.93000 -29.76400 1.000 80.30820  ? 55  ILE A CG2 1 
ATOM   397  C  CD1 . ILE A 1 55  ? 1.32000   -10.89700 -29.47900 1.000 77.84246  ? 55  ILE A CD1 1 
ATOM   398  N  N   . PRO A 1 56  ? -1.03300  -14.82700 -31.32600 1.000 86.58206  ? 56  PRO A N   1 
ATOM   399  C  CA  . PRO A 1 56  ? -1.86100  -15.95600 -31.78600 1.000 91.91188  ? 56  PRO A CA  1 
ATOM   400  C  C   . PRO A 1 56  ? -3.33000  -15.57700 -31.90200 1.000 96.47981  ? 56  PRO A C   1 
ATOM   401  O  O   . PRO A 1 56  ? -3.80000  -14.63200 -31.24800 1.000 92.84008  ? 56  PRO A O   1 
ATOM   402  C  CB  . PRO A 1 56  ? -1.63700  -17.02600 -30.69900 1.000 95.09585  ? 56  PRO A CB  1 
ATOM   403  C  CG  . PRO A 1 56  ? -0.98800  -16.29400 -29.54500 1.000 95.06515  ? 56  PRO A CG  1 
ATOM   404  C  CD  . PRO A 1 56  ? -0.20600  -15.18200 -30.16400 1.000 88.78398  ? 56  PRO A CD  1 
ATOM   405  N  N   . PRO A 1 57  ? -4.08400  -16.29600 -32.73600 1.000 99.58358  ? 57  PRO A N   1 
ATOM   406  C  CA  . PRO A 1 57  ? -5.51000  -15.97900 -32.94100 1.000 100.44974 ? 57  PRO A CA  1 
ATOM   407  C  C   . PRO A 1 57  ? -6.29600  -16.04600 -31.64000 1.000 98.51271  ? 57  PRO A C   1 
ATOM   408  O  O   . PRO A 1 57  ? -6.09900  -16.95900 -30.82700 1.000 97.52119  ? 57  PRO A O   1 
ATOM   409  C  CB  . PRO A 1 57  ? -5.97900  -17.06000 -33.93400 1.000 103.70025 ? 57  PRO A CB  1 
ATOM   410  C  CG  . PRO A 1 57  ? -4.87400  -18.08200 -33.99000 1.000 103.69693 ? 57  PRO A CG  1 
ATOM   411  C  CD  . PRO A 1 57  ? -3.61500  -17.34600 -33.65500 1.000 100.04775 ? 57  PRO A CD  1 
ATOM   412  N  N   . PRO A 1 58  ? -7.20800  -15.10000 -31.42800 1.000 95.60632  ? 58  PRO A N   1 
ATOM   413  C  CA  . PRO A 1 58  ? -7.89400  -14.99300 -30.13100 1.000 88.67654  ? 58  PRO A CA  1 
ATOM   414  C  C   . PRO A 1 58  ? -8.87300  -16.13200 -29.87400 1.000 84.01258  ? 58  PRO A C   1 
ATOM   415  O  O   . PRO A 1 58  ? -9.35700  -16.80200 -30.78900 1.000 84.13979  ? 58  PRO A O   1 
ATOM   416  C  CB  . PRO A 1 58  ? -8.63900  -13.65600 -30.23800 1.000 83.74010  ? 58  PRO A CB  1 
ATOM   417  C  CG  . PRO A 1 58  ? -7.97500  -12.91700 -31.37400 1.000 88.18300  ? 58  PRO A CG  1 
ATOM   418  C  CD  . PRO A 1 58  ? -7.52300  -13.97800 -32.32300 1.000 95.35291  ? 58  PRO A CD  1 
ATOM   419  N  N   . LYS A 1 59  ? -9.18300  -16.32700 -28.58900 1.000 78.06120  ? 59  LYS A N   1 
ATOM   420  C  CA  . LYS A 1 59  ? -10.13600 -17.35300 -28.17600 1.000 77.04283  ? 59  LYS A CA  1 
ATOM   421  C  C   . LYS A 1 59  ? -11.55400 -16.82000 -28.02100 1.000 75.21056  ? 59  LYS A C   1 
ATOM   422  O  O   . LYS A 1 59  ? -12.51600 -17.60600 -28.05500 1.000 70.61590  ? 59  LYS A O   1 
ATOM   423  C  CB  . LYS A 1 59  ? -9.69700  -17.99300 -26.85300 1.000 73.04567  ? 59  LYS A CB  1 
ATOM   424  C  CG  . LYS A 1 59  ? -8.34000  -18.66900 -26.89600 1.000 75.79716  ? 59  LYS A CG  1 
ATOM   425  C  CD  . LYS A 1 59  ? -8.24300  -19.67900 -28.02600 1.000 73.87730  ? 59  LYS A CD  1 
ATOM   426  C  CE  . LYS A 1 59  ? -7.12000  -20.69200 -27.77600 1.000 70.76788  ? 59  LYS A CE  1 
ATOM   427  N  NZ  . LYS A 1 59  ? -7.45900  -21.64600 -26.67300 1.000 69.63320  ? 59  LYS A NZ  1 
ATOM   428  N  N   . GLY A 1 60  ? -11.70800 -15.50800 -27.85400 1.000 71.07640  ? 60  GLY A N   1 
ATOM   429  C  CA  . GLY A 1 60  ? -12.99800 -14.89700 -27.67200 1.000 65.04209  ? 60  GLY A CA  1 
ATOM   430  C  C   . GLY A 1 60  ? -13.43900 -14.07400 -28.86900 1.000 58.89064  ? 60  GLY A C   1 
ATOM   431  O  O   . GLY A 1 60  ? -12.79100 -14.03300 -29.91900 1.000 58.36676  ? 60  GLY A O   1 
ATOM   432  N  N   . GLU A 1 61  ? -14.58000 -13.41600 -28.69300 1.000 56.02652  ? 61  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 61  ? -15.13000 -12.58800 -29.75100 1.000 56.96626  ? 61  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 61  ? -14.22700 -11.38900 -30.01400 1.000 55.11679  ? 61  GLU A C   1 
ATOM   435  O  O   . GLU A 1 61  ? -13.61900 -10.82800 -29.09700 1.000 50.66845  ? 61  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 61  ? -16.54400 -12.11500 -29.39800 1.000 57.36326  ? 61  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 61  ? -16.61900 -11.17500 -28.21400 1.000 55.08254  ? 61  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 61  ? -17.79800 -10.20100 -28.27700 1.000 55.89384  ? 61  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 61  ? -18.60500 -10.25300 -29.23000 1.000 60.03099  ? 61  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 61  ? -17.90800 -9.37000  -27.35800 1.000 53.74563  ? 61  GLU A OE2 1 
ATOM   441  N  N   . ARG A 1 62  ? -14.11400 -11.03900 -31.29200 1.000 55.32272  ? 62  ARG A N   1 
ATOM   442  C  CA  . ARG A 1 62  ? -13.47700 -9.81900  -31.76400 1.000 52.73438  ? 62  ARG A CA  1 
ATOM   443  C  C   . ARG A 1 62  ? -14.54900 -9.01900  -32.49100 1.000 52.09321  ? 62  ARG A C   1 
ATOM   444  O  O   . ARG A 1 62  ? -15.07200 -9.47200  -33.51500 1.000 52.18397  ? 62  ARG A O   1 
ATOM   445  C  CB  . ARG A 1 62  ? -12.29700 -10.12700 -32.69400 1.000 54.72518  ? 62  ARG A CB  1 
ATOM   446  C  CG  . ARG A 1 62  ? -11.05300 -10.65200 -31.99300 1.000 60.08588  ? 62  ARG A CG  1 
ATOM   447  C  CD  . ARG A 1 62  ? -10.59000 -9.69100  -30.90300 1.000 57.33987  ? 62  ARG A CD  1 
ATOM   448  N  NE  . ARG A 1 62  ? -10.85500 -10.22800 -29.57500 1.000 62.19149  ? 62  ARG A NE  1 
ATOM   449  C  CZ  . ARG A 1 62  ? -9.92800  -10.73900 -28.77600 1.000 66.61058  ? 62  ARG A CZ  1 
ATOM   450  N  NH1 . ARG A 1 62  ? -8.65000  -10.74700 -29.12100 1.000 75.24890  ? 62  ARG A NH1 1 
ATOM   451  N  NH2 . ARG A 1 62  ? -10.29100 -11.24800 -27.60000 1.000 63.87501  ? 62  ARG A NH2 1 
ATOM   452  N  N   . LEU A 1 63  ? -14.86500 -7.82900  -31.96400 1.000 46.92835  ? 63  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 63  ? -16.04500 -7.10100  -32.42400 1.000 47.09892  ? 63  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 63  ? -15.97400 -6.80900  -33.91800 1.000 47.88599  ? 63  LEU A C   1 
ATOM   455  O  O   . LEU A 1 63  ? -16.95600 -7.00600  -34.64100 1.000 48.54407  ? 63  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 63  ? -16.20800 -5.80800  -31.61400 1.000 45.93816  ? 63  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 63  ? -16.46400 -6.08300  -30.12100 1.000 47.76776  ? 63  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 63  ? -16.53900 -4.80500  -29.29000 1.000 42.92090  ? 63  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 63  ? -17.71900 -6.94000  -29.93000 1.000 50.52602  ? 63  LEU A CD2 1 
ATOM   460  N  N   . LEU A 1 64  ? -14.81600 -6.36200  -34.40000 1.000 48.67614  ? 64  LEU A N   1 
ATOM   461  C  CA  . LEU A 1 64  ? -14.61500 -6.02500  -35.80600 1.000 50.81271  ? 64  LEU A CA  1 
ATOM   462  C  C   . LEU A 1 64  ? -14.15200 -7.23100  -36.63000 1.000 54.61592  ? 64  LEU A C   1 
ATOM   463  O  O   . LEU A 1 64  ? -14.75900 -7.55500  -37.65700 1.000 59.13853  ? 64  LEU A O   1 
ATOM   464  C  CB  . LEU A 1 64  ? -13.60800 -4.87100  -35.90400 1.000 48.16280  ? 64  LEU A CB  1 
ATOM   465  C  CG  . LEU A 1 64  ? -13.25900 -4.28600  -37.27400 1.000 54.06423  ? 64  LEU A CG  1 
ATOM   466  C  CD1 . LEU A 1 64  ? -14.50200 -4.13300  -38.11800 1.000 58.98621  ? 64  LEU A CD1 1 
ATOM   467  C  CD2 . LEU A 1 64  ? -12.58300 -2.94300  -37.10300 1.000 50.27136  ? 64  LEU A CD2 1 
ATOM   468  N  N   . ALA A 1 65  ? -13.09300 -7.91100  -36.17800 1.000 52.57121  ? 65  ALA A N   1 
ATOM   469  C  CA  . ALA A 1 65  ? -12.47300 -8.97300  -36.96700 1.000 58.02717  ? 65  ALA A CA  1 
ATOM   470  C  C   . ALA A 1 65  ? -13.45900 -10.08300 -37.31700 1.000 60.78807  ? 65  ALA A C   1 
ATOM   471  O  O   . ALA A 1 65  ? -13.41300 -10.63200 -38.42500 1.000 64.88526  ? 65  ALA A O   1 
ATOM   472  C  CB  . ALA A 1 65  ? -11.27200 -9.54700  -36.21600 1.000 55.40933  ? 65  ALA A CB  1 
ATOM   473  N  N   . ASP A 1 66  ? -14.34600 -10.44300 -36.38700 1.000 57.08576  ? 66  ASP A N   1 
ATOM   474  C  CA  . ASP A 1 66  ? -15.29900 -11.52000 -36.65800 1.000 63.61191  ? 66  ASP A CA  1 
ATOM   475  C  C   . ASP A 1 66  ? -16.30100 -11.16600 -37.76200 1.000 66.28961  ? 66  ASP A C   1 
ATOM   476  O  O   . ASP A 1 66  ? -16.94400 -12.06800 -38.30900 1.000 65.88955  ? 66  ASP A O   1 
ATOM   477  C  CB  . ASP A 1 66  ? -16.05100 -11.89900 -35.37600 1.000 60.25308  ? 66  ASP A CB  1 
ATOM   478  C  CG  . ASP A 1 66  ? -15.15200 -12.54100 -34.31800 1.000 57.31052  ? 66  ASP A CG  1 
ATOM   479  O  OD1 . ASP A 1 66  ? -14.02000 -12.96000 -34.63700 1.000 59.05223  ? 66  ASP A OD1 1 
ATOM   480  O  OD2 . ASP A 1 66  ? -15.59000 -12.62600 -33.15200 1.000 55.75421  ? 66  ASP A OD2 1 
ATOM   481  N  N   . LYS A 1 67  ? -16.45600 -9.88100  -38.09300 1.000 76.22804  ? 67  LYS A N   1 
ATOM   482  C  CA  . LYS A 1 67  ? -17.37100 -9.45000  -39.14500 1.000 74.53735  ? 67  LYS A CA  1 
ATOM   483  C  C   . LYS A 1 67  ? -16.84200 -9.71500  -40.54800 1.000 80.25017  ? 67  LYS A C   1 
ATOM   484  O  O   . LYS A 1 67  ? -17.61700 -9.63200  -41.50600 1.000 88.05091  ? 67  LYS A O   1 
ATOM   485  C  CB  . LYS A 1 67  ? -17.66900 -7.95300  -39.01100 1.000 73.86064  ? 67  LYS A CB  1 
ATOM   486  C  CG  . LYS A 1 67  ? -19.02200 -7.59900  -38.41200 1.000 72.92517  ? 67  LYS A CG  1 
ATOM   487  C  CD  . LYS A 1 67  ? -19.02600 -7.76900  -36.91100 1.000 71.12460  ? 67  LYS A CD  1 
ATOM   488  C  CE  . LYS A 1 67  ? -20.14100 -6.96900  -36.25600 1.000 66.62299  ? 67  LYS A CE  1 
ATOM   489  N  NZ  . LYS A 1 67  ? -21.48300 -7.34300  -36.76900 1.000 72.73086  ? 67  LYS A NZ  1 
ATOM   490  N  N   . TYR A 1 68  ? -15.56300 -10.01600 -40.71000 1.000 74.68835  ? 68  TYR A N   1 
ATOM   491  C  CA  . TYR A 1 68  ? -14.98000 -10.11900 -42.03800 1.000 79.75088  ? 68  TYR A CA  1 
ATOM   492  C  C   . TYR A 1 68  ? -14.26100 -11.44500 -42.21400 1.000 80.85505  ? 68  TYR A C   1 
ATOM   493  O  O   . TYR A 1 68  ? -13.94800 -12.12800 -41.23200 1.000 76.98569  ? 68  TYR A O   1 
ATOM   494  C  CB  . TYR A 1 68  ? -14.01900 -8.94700  -42.28700 1.000 79.32632  ? 68  TYR A CB  1 
ATOM   495  C  CG  . TYR A 1 68  ? -14.72800 -7.59900  -42.27700 1.000 80.36867  ? 68  TYR A CG  1 
ATOM   496  C  CD1 . TYR A 1 68  ? -15.53100 -7.22400  -43.35400 1.000 82.05941  ? 68  TYR A CD1 1 
ATOM   497  C  CD2 . TYR A 1 68  ? -14.58400 -6.73500  -41.19300 1.000 76.51577  ? 68  TYR A CD2 1 
ATOM   498  C  CE1 . TYR A 1 68  ? -16.16900 -6.00900  -43.33100 1.000 80.81339  ? 68  TYR A CE1 1 
ATOM   499  C  CE2 . TYR A 1 68  ? -15.23500 -5.52800  -41.20500 1.000 79.25952  ? 68  TYR A CE2 1 
ATOM   500  C  CZ  . TYR A 1 68  ? -16.03800 -5.13400  -42.26400 1.000 79.88409  ? 68  TYR A CZ  1 
ATOM   501  O  OH  . TYR A 1 68  ? -16.66500 -3.94100  -42.25400 1.000 80.52170  ? 68  TYR A OH  1 
ATOM   502  N  N   . PRO A 1 69  ? -14.01700 -11.85600 -43.46100 1.000 87.44688  ? 69  PRO A N   1 
ATOM   503  C  CA  . PRO A 1 69  ? -13.36400 -13.15000 -43.72600 1.000 87.09840  ? 69  PRO A CA  1 
ATOM   504  C  C   . PRO A 1 69  ? -11.97900 -13.22100 -43.10200 1.000 89.29426  ? 69  PRO A C   1 
ATOM   505  O  O   . PRO A 1 69  ? -11.47200 -12.21700 -42.57900 1.000 83.67656  ? 69  PRO A O   1 
ATOM   506  C  CB  . PRO A 1 69  ? -13.29600 -13.19900 -45.26500 1.000 88.84919  ? 69  PRO A CB  1 
ATOM   507  C  CG  . PRO A 1 69  ? -13.58700 -11.80400 -45.73000 1.000 86.71309  ? 69  PRO A CG  1 
ATOM   508  C  CD  . PRO A 1 69  ? -14.49100 -11.22500 -44.70600 1.000 84.77657  ? 69  PRO A CD  1 
ATOM   509  N  N   . PRO A 1 70  ? -11.33400 -14.39500 -43.12900 1.000 91.75192  ? 70  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 70  ? -10.06000 -14.55900 -42.40200 1.000 93.38636  ? 70  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 70  ? -8.85500  -13.83500 -43.00800 1.000 91.71121  ? 70  PRO A C   1 
ATOM   512  O  O   . PRO A 1 70  ? -7.81800  -13.76800 -42.33400 1.000 89.24528  ? 70  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 70  ? -9.84000  -16.07900 -42.42000 1.000 95.38099  ? 70  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 70  ? -11.17800 -16.66300 -42.69800 1.000 93.57124  ? 70  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 70  ? -11.86000 -15.69000 -43.59200 1.000 91.76201  ? 70  PRO A CD  1 
ATOM   516  N  N   . HIS A 1 71  ? -8.93000  -13.31100 -44.23900 1.000 95.11140  ? 71  HIS A N   1 
ATOM   517  C  CA  . HIS A 1 71  ? -7.81600  -12.52700 -44.77600 1.000 94.75650  ? 71  HIS A CA  1 
ATOM   518  C  C   . HIS A 1 71  ? -7.80500  -11.08700 -44.26000 1.000 93.94382  ? 71  HIS A C   1 
ATOM   519  O  O   . HIS A 1 71  ? -7.07000  -10.24800 -44.80200 1.000 94.79590  ? 71  HIS A O   1 
ATOM   520  C  CB  . HIS A 1 71  ? -7.82100  -12.53900 -46.31100 1.000 95.82708  ? 71  HIS A CB  1 
ATOM   521  C  CG  . HIS A 1 71  ? -9.18400  -12.47500 -46.92800 1.000 96.02735  ? 71  HIS A CG  1 
ATOM   522  N  ND1 . HIS A 1 71  ? -9.84100  -13.59500 -47.39200 1.000 96.85419  ? 71  HIS A ND1 1 
ATOM   523  C  CD2 . HIS A 1 71  ? -10.00000 -11.42600 -47.18600 1.000 95.99439  ? 71  HIS A CD2 1 
ATOM   524  C  CE1 . HIS A 1 71  ? -11.01000 -13.24100 -47.89500 1.000 96.19594  ? 71  HIS A CE1 1 
ATOM   525  N  NE2 . HIS A 1 71  ? -11.13100 -11.93000 -47.78300 1.000 97.12630  ? 71  HIS A NE2 1 
ATOM   526  N  N   . PHE A 1 72  ? -8.60200  -10.80700 -43.22700 1.000 85.34907  ? 72  PHE A N   1 
ATOM   527  C  CA  . PHE A 1 72  ? -8.65000  -9.51400  -42.54400 1.000 77.27314  ? 72  PHE A CA  1 
ATOM   528  C  C   . PHE A 1 72  ? -7.50000  -9.47500  -41.54600 1.000 70.64607  ? 72  PHE A C   1 
ATOM   529  O  O   . PHE A 1 72  ? -7.55400  -10.10700 -40.48700 1.000 69.41359  ? 72  PHE A O   1 
ATOM   530  C  CB  . PHE A 1 72  ? -10.00000 -9.33600  -41.85300 1.000 75.09834  ? 72  PHE A CB  1 
ATOM   531  C  CG  . PHE A 1 72  ? -10.38000 -7.90600  -41.57900 1.000 70.73720  ? 72  PHE A CG  1 
ATOM   532  C  CD1 . PHE A 1 72  ? -11.02000 -7.14500  -42.54700 1.000 72.18954  ? 72  PHE A CD1 1 
ATOM   533  C  CD2 . PHE A 1 72  ? -10.14500 -7.33700  -40.33400 1.000 67.24925  ? 72  PHE A CD2 1 
ATOM   534  C  CE1 . PHE A 1 72  ? -11.39500 -5.82700  -42.28800 1.000 71.41021  ? 72  PHE A CE1 1 
ATOM   535  C  CE2 . PHE A 1 72  ? -10.51500 -6.02300  -40.06900 1.000 63.05919  ? 72  PHE A CE2 1 
ATOM   536  C  CZ  . PHE A 1 72  ? -11.14700 -5.27100  -41.04500 1.000 64.28321  ? 72  PHE A CZ  1 
ATOM   537  N  N   . LYS A 1 73  ? -6.43400  -8.76800  -41.90500 1.000 65.98289  ? 73  LYS A N   1 
ATOM   538  C  CA  . LYS A 1 73  ? -5.33300  -8.51600  -40.99000 1.000 60.50220  ? 73  LYS A CA  1 
ATOM   539  C  C   . LYS A 1 73  ? -5.53700  -7.13700  -40.37100 1.000 56.73661  ? 73  LYS A C   1 
ATOM   540  O  O   . LYS A 1 73  ? -5.76400  -6.15400  -41.08600 1.000 52.91711  ? 73  LYS A O   1 
ATOM   541  C  CB  . LYS A 1 73  ? -3.99300  -8.61200  -41.71900 1.000 63.69534  ? 73  LYS A CB  1 
ATOM   542  C  CG  . LYS A 1 73  ? -3.32800  -10.00600 -41.68200 1.000 67.17567  ? 73  LYS A CG  1 
ATOM   543  C  CD  . LYS A 1 73  ? -4.30000  -11.15400 -41.95500 1.000 70.91183  ? 73  LYS A CD  1 
ATOM   544  C  CE  . LYS A 1 73  ? -3.56600  -12.50600 -42.11900 1.000 76.53644  ? 73  LYS A CE  1 
ATOM   545  N  NZ  . LYS A 1 73  ? -2.61000  -12.82500 -41.00200 1.000 73.93222  ? 73  LYS A NZ  1 
ATOM   546  N  N   . TYR A 1 74  ? -5.48900  -7.07100  -39.04400 1.000 53.74439  ? 74  TYR A N   1 
ATOM   547  C  CA  . TYR A 1 74  ? -5.98300  -5.89200  -38.33900 1.000 49.02854  ? 74  TYR A CA  1 
ATOM   548  C  C   . TYR A 1 74  ? -5.33900  -5.83500  -36.96900 1.000 42.65958  ? 74  TYR A C   1 
ATOM   549  O  O   . TYR A 1 74  ? -5.28400  -6.85100  -36.27200 1.000 42.38071  ? 74  TYR A O   1 
ATOM   550  C  CB  . TYR A 1 74  ? -7.50500  -5.95000  -38.22200 1.000 47.61567  ? 74  TYR A CB  1 
ATOM   551  C  CG  . TYR A 1 74  ? -8.19400  -4.93300  -37.32200 1.000 46.34749  ? 74  TYR A CG  1 
ATOM   552  C  CD1 . TYR A 1 74  ? -8.23200  -3.58300  -37.67400 1.000 43.82877  ? 74  TYR A CD1 1 
ATOM   553  C  CD2 . TYR A 1 74  ? -8.83700  -5.36100  -36.15900 1.000 46.22360  ? 74  TYR A CD2 1 
ATOM   554  C  CE1 . TYR A 1 74  ? -8.87400  -2.69300  -36.84800 1.000 43.72730  ? 74  TYR A CE1 1 
ATOM   555  C  CE2 . TYR A 1 74  ? -9.47800  -4.44300  -35.36300 1.000 44.08362  ? 74  TYR A CE2 1 
ATOM   556  C  CZ  . TYR A 1 74  ? -9.51000  -3.09500  -35.68300 1.000 42.40776  ? 74  TYR A CZ  1 
ATOM   557  O  OH  . TYR A 1 74  ? -10.15100 -2.21000  -34.89400 1.000 45.15126  ? 74  TYR A OH  1 
ATOM   558  N  N   . VAL A 1 75  ? -4.85000  -4.65700  -36.59600 1.000 41.10329  ? 75  VAL A N   1 
ATOM   559  C  CA  . VAL A 1 75  ? -4.33900  -4.40700  -35.25000 1.000 39.34800  ? 75  VAL A CA  1 
ATOM   560  C  C   . VAL A 1 75  ? -5.07400  -3.19600  -34.68700 1.000 41.43207  ? 75  VAL A C   1 
ATOM   561  O  O   . VAL A 1 75  ? -4.81300  -2.05700  -35.11400 1.000 35.47712  ? 75  VAL A O   1 
ATOM   562  C  CB  . VAL A 1 75  ? -2.82000  -4.16600  -35.24700 1.000 43.63205  ? 75  VAL A CB  1 
ATOM   563  C  CG1 . VAL A 1 75  ? -2.34500  -3.77900  -33.85100 1.000 41.27558  ? 75  VAL A CG1 1 
ATOM   564  C  CG2 . VAL A 1 75  ? -2.05700  -5.39300  -35.76600 1.000 43.49744  ? 75  VAL A CG2 1 
ATOM   565  N  N   . PRO A 1 76  ? -5.99400  -3.38700  -33.74600 1.000 41.04326  ? 76  PRO A N   1 
ATOM   566  C  CA  . PRO A 1 76  ? -6.71100  -2.24200  -33.17400 1.000 38.57565  ? 76  PRO A CA  1 
ATOM   567  C  C   . PRO A 1 76  ? -5.83100  -1.42500  -32.23800 1.000 37.23365  ? 76  PRO A C   1 
ATOM   568  O  O   . PRO A 1 76  ? -4.80000  -1.88600  -31.74500 1.000 39.46045  ? 76  PRO A O   1 
ATOM   569  C  CB  . PRO A 1 76  ? -7.85700  -2.89700  -32.40400 1.000 39.14409  ? 76  PRO A CB  1 
ATOM   570  C  CG  . PRO A 1 76  ? -7.29100  -4.21200  -31.98900 1.000 40.92894  ? 76  PRO A CG  1 
ATOM   571  C  CD  . PRO A 1 76  ? -6.41100  -4.66200  -33.13600 1.000 40.32822  ? 76  PRO A CD  1 
ATOM   572  N  N   . ASN A 1 77  ? -6.29100  -0.19600  -31.98600 1.000 37.62931  ? 77  ASN A N   1 
ATOM   573  C  CA  . ASN A 1 77  ? -5.71100  0.77500   -31.06100 1.000 39.88192  ? 77  ASN A CA  1 
ATOM   574  C  C   . ASN A 1 77  ? -4.20200  0.65300   -30.91300 1.000 36.75780  ? 77  ASN A C   1 
ATOM   575  O  O   . ASN A 1 77  ? -3.70100  0.35200   -29.82500 1.000 35.53229  ? 77  ASN A O   1 
ATOM   576  C  CB  . ASN A 1 77  ? -6.38200  0.69700   -29.67400 1.000 37.13909  ? 77  ASN A CB  1 
ATOM   577  C  CG  . ASN A 1 77  ? -6.69600  -0.72700  -29.22600 1.000 39.38570  ? 77  ASN A CG  1 
ATOM   578  O  OD1 . ASN A 1 77  ? -7.82300  -1.20600  -29.40400 1.000 37.92880  ? 77  ASN A OD1 1 
ATOM   579  N  ND2 . ASN A 1 77  ? -5.71700  -1.39400  -28.59800 1.000 37.59325  ? 77  ASN A ND2 1 
ATOM   580  N  N   . VAL A 1 78  ? -3.47400  0.93600   -31.99900 1.000 39.07693  ? 78  VAL A N   1 
ATOM   581  C  CA  . VAL A 1 78  ? -2.02100  0.81500   -31.99100 1.000 38.14654  ? 78  VAL A CA  1 
ATOM   582  C  C   . VAL A 1 78  ? -1.37400  1.74400   -30.97500 1.000 37.85262  ? 78  VAL A C   1 
ATOM   583  O  O   . VAL A 1 78  ? -0.20200  1.55500   -30.63400 1.000 39.20112  ? 78  VAL A O   1 
ATOM   584  C  CB  . VAL A 1 78  ? -1.43700  1.04500   -33.40900 1.000 38.10613  ? 78  VAL A CB  1 
ATOM   585  C  CG1 . VAL A 1 78  ? -1.88500  -0.07600  -34.36100 1.000 40.57746  ? 78  VAL A CG1 1 
ATOM   586  C  CG2 . VAL A 1 78  ? -1.80800  2.40000   -33.95500 1.000 33.30922  ? 78  VAL A CG2 1 
ATOM   587  N  N   . ALA A 1 79  ? -2.11400  2.72600   -30.44900 1.000 38.60796  ? 79  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 79  ? -1.53400  3.61900   -29.44800 1.000 36.76587  ? 79  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 79  ? -1.08900  2.85400   -28.20800 1.000 39.67528  ? 79  ALA A C   1 
ATOM   590  O  O   . ALA A 1 79  ? -0.06300  3.18700   -27.60400 1.000 43.04510  ? 79  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 79  ? -2.53100  4.71300   -29.07800 1.000 37.06615  ? 79  ALA A CB  1 
ATOM   592  N  N   . THR A 1 80  ? -1.82400  1.80700   -27.82600 1.000 36.58850  ? 80  THR A N   1 
ATOM   593  C  CA  . THR A 1 80  ? -1.53000  1.09700   -26.58600 1.000 40.43376  ? 80  THR A CA  1 
ATOM   594  C  C   . THR A 1 80  ? -0.45900  0.03100   -26.73200 1.000 43.02269  ? 80  THR A C   1 
ATOM   595  O  O   . THR A 1 80  ? 0.03600   -0.46400  -25.71200 1.000 43.60672  ? 80  THR A O   1 
ATOM   596  C  CB  . THR A 1 80  ? -2.78900  0.42200   -26.01300 1.000 39.80175  ? 80  THR A CB  1 
ATOM   597  O  OG1 . THR A 1 80  ? -3.19400  -0.65000  -26.87000 1.000 41.02114  ? 80  THR A OG1 1 
ATOM   598  C  CG2 . THR A 1 80  ? -3.92800  1.42100   -25.86700 1.000 37.56995  ? 80  THR A CG2 1 
ATOM   599  N  N   . THR A 1 81  ? -0.10800  -0.36000  -27.96000 1.000 42.28511  ? 81  THR A N   1 
ATOM   600  C  CA  . THR A 1 81  ? 0.85400   -1.42800  -28.17900 1.000 45.31711  ? 81  THR A CA  1 
ATOM   601  C  C   . THR A 1 81  ? 2.08200   -1.00600  -28.96000 1.000 43.00578  ? 81  THR A C   1 
ATOM   602  O  O   . THR A 1 81  ? 3.01800   -1.80000  -29.05900 1.000 47.10220  ? 81  THR A O   1 
ATOM   603  C  CB  . THR A 1 81  ? 0.21300   -2.61900  -28.92000 1.000 44.55576  ? 81  THR A CB  1 
ATOM   604  O  OG1 . THR A 1 81  ? -0.46100  -2.15100  -30.09600 1.000 45.33526  ? 81  THR A OG1 1 
ATOM   605  C  CG2 . THR A 1 81  ? -0.76500  -3.37500  -28.02000 1.000 45.46263  ? 81  THR A CG2 1 
ATOM   606  N  N   . CYS A 1 82  ? 2.12200   0.19900   -29.52000 1.000 43.79404  ? 82  CYS A N   1 
ATOM   607  C  CA  . CYS A 1 82  ? 3.26700   0.62000   -30.32900 1.000 45.72892  ? 82  CYS A CA  1 
ATOM   608  C  C   . CYS A 1 82  ? 3.80000   1.95200   -29.82000 1.000 44.03370  ? 82  CYS A C   1 
ATOM   609  O  O   . CYS A 1 82  ? 3.24900   3.01100   -30.16200 1.000 41.30389  ? 82  CYS A O   1 
ATOM   610  C  CB  . CYS A 1 82  ? 2.88600   0.70500   -31.80100 1.000 44.84142  ? 82  CYS A CB  1 
ATOM   611  S  SG  . CYS A 1 82  ? 2.11400   -0.84000  -32.39700 1.000 46.49040  ? 82  CYS A SG  1 
ATOM   612  N  N   . PRO A 1 83  ? 4.87100   1.93700   -29.01700 1.000 44.61838  ? 83  PRO A N   1 
ATOM   613  C  CA  . PRO A 1 83  ? 5.39400   3.19800   -28.45400 1.000 42.04713  ? 83  PRO A CA  1 
ATOM   614  C  C   . PRO A 1 83  ? 5.71500   4.25400   -29.50100 1.000 42.18844  ? 83  PRO A C   1 
ATOM   615  O  O   . PRO A 1 83  ? 5.45300   5.44200   -29.27200 1.000 41.60156  ? 83  PRO A O   1 
ATOM   616  C  CB  . PRO A 1 83  ? 6.66000   2.75000   -27.70300 1.000 43.50380  ? 83  PRO A CB  1 
ATOM   617  C  CG  . PRO A 1 83  ? 6.47300   1.29600   -27.45600 1.000 46.87523  ? 83  PRO A CG  1 
ATOM   618  C  CD  . PRO A 1 83  ? 5.66500   0.76700   -28.61300 1.000 44.93572  ? 83  PRO A CD  1 
ATOM   619  N  N   . THR A 1 84  ? 6.26600   3.85300   -30.65100 1.000 43.29729  ? 84  THR A N   1 
ATOM   620  C  CA  . THR A 1 84  ? 6.58300   4.81800   -31.69800 1.000 43.79276  ? 84  THR A CA  1 
ATOM   621  C  C   . THR A 1 84  ? 5.34500   5.58700   -32.14300 1.000 44.10063  ? 84  THR A C   1 
ATOM   622  O  O   . THR A 1 84  ? 5.40900   6.80400   -32.36600 1.000 42.72681  ? 84  THR A O   1 
ATOM   623  C  CB  . THR A 1 84  ? 7.22600   4.12000   -32.89500 1.000 46.88743  ? 84  THR A CB  1 
ATOM   624  O  OG1 . THR A 1 84  ? 8.36900   3.38200   -32.45900 1.000 48.35460  ? 84  THR A OG1 1 
ATOM   625  C  CG2 . THR A 1 84  ? 7.65900   5.14600   -33.92400 1.000 47.40351  ? 84  THR A CG2 1 
ATOM   626  N  N   . PHE A 1 85  ? 4.20500   4.91100   -32.27800 1.000 41.85706  ? 85  PHE A N   1 
ATOM   627  C  CA  . PHE A 1 85  ? 3.00200   5.67600   -32.58500 1.000 41.34265  ? 85  PHE A CA  1 
ATOM   628  C  C   . PHE A 1 85  ? 2.63200   6.58700   -31.42400 1.000 40.69483  ? 85  PHE A C   1 
ATOM   629  O  O   . PHE A 1 85  ? 2.34400   7.77300   -31.62200 1.000 38.56666  ? 85  PHE A O   1 
ATOM   630  C  CB  . PHE A 1 85  ? 1.82700   4.76400   -32.93600 1.000 38.99133  ? 85  PHE A CB  1 
ATOM   631  C  CG  . PHE A 1 85  ? 0.61400   5.52700   -33.38700 1.000 36.99045  ? 85  PHE A CG  1 
ATOM   632  C  CD1 . PHE A 1 85  ? 0.53200   6.00300   -34.68800 1.000 38.07107  ? 85  PHE A CD1 1 
ATOM   633  C  CD2 . PHE A 1 85  ? -0.41300  5.83100   -32.49500 1.000 35.95013  ? 85  PHE A CD2 1 
ATOM   634  C  CE1 . PHE A 1 85  ? -0.56800  6.73500   -35.10700 1.000 38.60824  ? 85  PHE A CE1 1 
ATOM   635  C  CE2 . PHE A 1 85  ? -1.50900  6.56400   -32.90900 1.000 37.74693  ? 85  PHE A CE2 1 
ATOM   636  C  CZ  . PHE A 1 85  ? -1.58700  7.01100   -34.22200 1.000 34.35194  ? 85  PHE A CZ  1 
ATOM   637  N  N   . ARG A 1 86  ? 2.67700   6.05500   -30.20300 1.000 40.74134  ? 86  ARG A N   1 
ATOM   638  C  CA  . ARG A 1 86  ? 2.18900   6.79400   -29.04400 1.000 44.00375  ? 86  ARG A CA  1 
ATOM   639  C  C   . ARG A 1 86  ? 3.10400   7.97100   -28.70400 1.000 42.28644  ? 86  ARG A C   1 
ATOM   640  O  O   . ARG A 1 86  ? 2.62700   9.04300   -28.32200 1.000 43.98187  ? 86  ARG A O   1 
ATOM   641  C  CB  . ARG A 1 86  ? 2.04100   5.82300   -27.86600 1.000 37.91329  ? 86  ARG A CB  1 
ATOM   642  C  CG  . ARG A 1 86  ? 1.76800   6.45200   -26.53200 1.000 41.51096  ? 86  ARG A CG  1 
ATOM   643  C  CD  . ARG A 1 86  ? 1.47900   5.38600   -25.46900 1.000 39.59241  ? 86  ARG A CD  1 
ATOM   644  N  NE  . ARG A 1 86  ? 2.67200   4.71400   -24.97200 1.000 37.59457  ? 86  ARG A NE  1 
ATOM   645  C  CZ  . ARG A 1 86  ? 2.96600   3.43900   -25.19500 1.000 39.34424  ? 86  ARG A CZ  1 
ATOM   646  N  NH1 . ARG A 1 86  ? 2.17900   2.66300   -25.91700 1.000 39.33598  ? 86  ARG A NH1 1 
ATOM   647  N  NH2 . ARG A 1 86  ? 4.05900   2.92400   -24.65400 1.000 39.92993  ? 86  ARG A NH2 1 
ATOM   648  N  N   . ASN A 1 87  ? 4.41800   7.80600   -28.86000 1.000 43.76691  ? 87  ASN A N   1 
ATOM   649  C  CA  . ASN A 1 87  ? 5.36900   8.83400   -28.44500 1.000 44.32600  ? 87  ASN A CA  1 
ATOM   650  C  C   . ASN A 1 87  ? 5.86000   9.72200   -29.58000 1.000 44.73173  ? 87  ASN A C   1 
ATOM   651  O  O   . ASN A 1 87  ? 6.49100   10.74800  -29.30700 1.000 47.03135  ? 87  ASN A O   1 
ATOM   652  C  CB  . ASN A 1 87  ? 6.58100   8.19000   -27.75600 1.000 42.74794  ? 87  ASN A CB  1 
ATOM   653  C  CG  . ASN A 1 87  ? 6.21600   7.56900   -26.41500 1.000 44.22106  ? 87  ASN A CG  1 
ATOM   654  O  OD1 . ASN A 1 87  ? 5.45200   8.15500   -25.63400 1.000 42.12366  ? 87  ASN A OD1 1 
ATOM   655  N  ND2 . ASN A 1 87  ? 6.73000   6.36200   -26.15700 1.000 44.68800  ? 87  ASN A ND2 1 
ATOM   656  N  N   . THR A 1 88  ? 5.59100   9.37300   -30.83500 1.000 42.80452  ? 88  THR A N   1 
ATOM   657  C  CA  . THR A 1 88  ? 6.18300   10.12500  -31.93300 1.000 43.50826  ? 88  THR A CA  1 
ATOM   658  C  C   . THR A 1 88  ? 5.13100   10.48600  -32.96700 1.000 41.14292  ? 88  THR A C   1 
ATOM   659  O  O   . THR A 1 88  ? 4.90800   11.67000  -33.23400 1.000 42.48283  ? 88  THR A O   1 
ATOM   660  C  CB  . THR A 1 88  ? 7.32400   9.33000   -32.58700 1.000 44.49579  ? 88  THR A CB  1 
ATOM   661  O  OG1 . THR A 1 88  ? 8.35600   9.08000   -31.62400 1.000 47.20482  ? 88  THR A OG1 1 
ATOM   662  C  CG2 . THR A 1 88  ? 7.91600   10.09000  -33.76100 1.000 43.77731  ? 88  THR A CG2 1 
ATOM   663  N  N   . VAL A 1 89  ? 4.46100   9.48100   -33.53600 1.000 38.58132  ? 89  VAL A N   1 
ATOM   664  C  CA  . VAL A 1 89  ? 3.57100   9.74700   -34.66200 1.000 38.27665  ? 89  VAL A CA  1 
ATOM   665  C  C   . VAL A 1 89  ? 2.29300   10.44300  -34.20300 1.000 38.28335  ? 89  VAL A C   1 
ATOM   666  O  O   . VAL A 1 89  ? 1.80900   11.36500  -34.86900 1.000 37.75051  ? 89  VAL A O   1 
ATOM   667  C  CB  . VAL A 1 89  ? 3.26900   8.44800   -35.42500 1.000 40.16717  ? 89  VAL A CB  1 
ATOM   668  C  CG1 . VAL A 1 89  ? 2.35300   8.73000   -36.59500 1.000 36.39104  ? 89  VAL A CG1 1 
ATOM   669  C  CG2 . VAL A 1 89  ? 4.55900   7.80600   -35.90300 1.000 40.48323  ? 89  VAL A CG2 1 
ATOM   670  N  N   . LEU A 1 90  ? 1.72900   10.01900  -33.06200 1.000 38.39305  ? 90  LEU A N   1 
ATOM   671  C  CA  . LEU A 1 90  ? 0.47500   10.59300  -32.56100 1.000 36.91109  ? 90  LEU A CA  1 
ATOM   672  C  C   . LEU A 1 90  ? 0.59500   12.08500  -32.26200 1.000 40.07395  ? 90  LEU A C   1 
ATOM   673  O  O   . LEU A 1 90  ? -0.39700  12.82000  -32.34600 1.000 38.61986  ? 90  LEU A O   1 
ATOM   674  C  CB  . LEU A 1 90  ? 0.02400   9.85700   -31.28900 1.000 35.58996  ? 90  LEU A CB  1 
ATOM   675  C  CG  . LEU A 1 90  ? -1.15100  10.45000  -30.49200 1.000 33.30052  ? 90  LEU A CG  1 
ATOM   676  C  CD1 . LEU A 1 90  ? -2.45100  10.35100  -31.26200 1.000 28.05784  ? 90  LEU A CD1 1 
ATOM   677  C  CD2 . LEU A 1 90  ? -1.30400  9.78400   -29.12000 1.000 33.73775  ? 90  LEU A CD2 1 
ATOM   678  N  N   . ILE A 1 91  ? 1.78000   12.55300  -31.89600 1.000 37.58831  ? 91  ILE A N   1 
ATOM   679  C  CA  . ILE A 1 91  ? 1.93700   13.92700  -31.45800 1.000 37.69437  ? 91  ILE A CA  1 
ATOM   680  C  C   . ILE A 1 91  ? 2.72100   14.74600  -32.47700 1.000 38.99401  ? 91  ILE A C   1 
ATOM   681  O  O   . ILE A 1 91  ? 3.23200   15.81500  -32.15200 1.000 38.05986  ? 91  ILE A O   1 
ATOM   682  C  CB  . ILE A 1 91  ? 2.58600   13.98100  -30.06800 1.000 38.22764  ? 91  ILE A CB  1 
ATOM   683  C  CG1 . ILE A 1 91  ? 3.92800   13.25700  -30.10800 1.000 38.57968  ? 91  ILE A CG1 1 
ATOM   684  C  CG2 . ILE A 1 91  ? 1.62900   13.35400  -29.02400 1.000 34.93327  ? 91  ILE A CG2 1 
ATOM   685  C  CD1 . ILE A 1 91  ? 4.72500   13.33700  -28.81100 1.000 42.47097  ? 91  ILE A CD1 1 
ATOM   686  N  N   . ASN A 1 92  ? 2.81800   14.25700  -33.70500 1.000 39.05430  ? 92  ASN A N   1 
ATOM   687  C  CA  . ASN A 1 92  ? 3.63700   14.92500  -34.70300 1.000 39.41855  ? 92  ASN A CA  1 
ATOM   688  C  C   . ASN A 1 92  ? 3.16700   16.36900  -34.86100 1.000 37.98879  ? 92  ASN A C   1 
ATOM   689  O  O   . ASN A 1 92  ? 1.96700   16.60500  -35.04500 1.000 36.98197  ? 92  ASN A O   1 
ATOM   690  C  CB  . ASN A 1 92  ? 3.54800   14.18400  -36.03700 1.000 39.84666  ? 92  ASN A CB  1 
ATOM   691  C  CG  . ASN A 1 92  ? 4.28800   14.89700  -37.13100 1.000 38.88532  ? 92  ASN A CG  1 
ATOM   692  O  OD1 . ASN A 1 92  ? 3.73800   15.77600  -37.78500 1.000 39.21425  ? 92  ASN A OD1 1 
ATOM   693  N  ND2 . ASN A 1 92  ? 5.55400   14.54600  -37.31900 1.000 38.76461  ? 92  ASN A ND2 1 
ATOM   694  N  N   . PRO A 1 93  ? 4.06900   17.35400  -34.80000 1.000 39.28478  ? 93  PRO A N   1 
ATOM   695  C  CA  . PRO A 1 93  ? 3.61200   18.75400  -34.73700 1.000 39.28696  ? 93  PRO A CA  1 
ATOM   696  C  C   . PRO A 1 93  ? 2.97600   19.24300  -36.02700 1.000 38.07677  ? 93  PRO A C   1 
ATOM   697  O  O   . PRO A 1 93  ? 2.12600   20.13900  -35.97900 1.000 36.37195  ? 93  PRO A O   1 
ATOM   698  C  CB  . PRO A 1 93  ? 4.89400   19.53600  -34.41000 1.000 44.93629  ? 93  PRO A CB  1 
ATOM   699  C  CG  . PRO A 1 93  ? 5.95100   18.48600  -34.07300 1.000 43.70696  ? 93  PRO A CG  1 
ATOM   700  C  CD  . PRO A 1 93  ? 5.53700   17.23900  -34.77800 1.000 39.18282  ? 93  PRO A CD  1 
ATOM   701  N  N   . VAL A 1 94  ? 3.35500   18.67900  -37.17700 1.000 39.08989  ? 94  VAL A N   1 
ATOM   702  C  CA  . VAL A 1 94  ? 2.73700   19.08200  -38.43700 1.000 39.30083  ? 94  VAL A CA  1 
ATOM   703  C  C   . VAL A 1 94  ? 1.30100   18.57700  -38.51700 1.000 36.69798  ? 94  VAL A C   1 
ATOM   704  O  O   . VAL A 1 94  ? 0.38900   19.32500  -38.89100 1.000 33.90779  ? 94  VAL A O   1 
ATOM   705  C  CB  . VAL A 1 94  ? 3.56200   18.58600  -39.63500 1.000 39.33696  ? 94  VAL A CB  1 
ATOM   706  C  CG1 . VAL A 1 94  ? 2.89600   19.00800  -40.93100 1.000 34.59069  ? 94  VAL A CG1 1 
ATOM   707  C  CG2 . VAL A 1 94  ? 4.97100   19.10400  -39.54700 1.000 39.62419  ? 94  VAL A CG2 1 
ATOM   708  N  N   . ILE A 1 95  ? 1.08300   17.29600  -38.19000 1.000 36.46325  ? 95  ILE A N   1 
ATOM   709  C  CA  . ILE A 1 95  ? -0.27700  16.76000  -38.14100 1.000 33.99059  ? 95  ILE A CA  1 
ATOM   710  C  C   . ILE A 1 95  ? -1.16600  17.65600  -37.29000 1.000 35.59918  ? 95  ILE A C   1 
ATOM   711  O  O   . ILE A 1 95  ? -2.29600  17.98300  -37.66700 1.000 34.09724  ? 95  ILE A O   1 
ATOM   712  C  CB  . ILE A 1 95  ? -0.27800  15.31300  -37.60900 1.000 37.91424  ? 95  ILE A CB  1 
ATOM   713  C  CG1 . ILE A 1 95  ? 0.50300   14.36500  -38.53600 1.000 37.61055  ? 95  ILE A CG1 1 
ATOM   714  C  CG2 . ILE A 1 95  ? -1.71600  14.82900  -37.39400 1.000 38.83855  ? 95  ILE A CG2 1 
ATOM   715  C  CD1 . ILE A 1 95  ? -0.00600  14.32800  -39.97000 1.000 39.39536  ? 95  ILE A CD1 1 
ATOM   716  N  N   . HIS A 1 96  ? -0.65700  18.09600  -36.14200 1.000 34.11901  ? 96  HIS A N   1 
ATOM   717  C  CA  . HIS A 1 96  ? -1.47900  18.90100  -35.24900 1.000 36.86278  ? 96  HIS A CA  1 
ATOM   718  C  C   . HIS A 1 96  ? -1.64800  20.34000  -35.71400 1.000 34.49619  ? 96  HIS A C   1 
ATOM   719  O  O   . HIS A 1 96  ? -2.69800  20.93100  -35.45700 1.000 32.56553  ? 96  HIS A O   1 
ATOM   720  C  CB  . HIS A 1 96  ? -0.90700  18.81200  -33.84300 1.000 36.18257  ? 96  HIS A CB  1 
ATOM   721  C  CG  . HIS A 1 96  ? -1.14200  17.46700  -33.25800 1.000 36.42608  ? 96  HIS A CG  1 
ATOM   722  N  ND1 . HIS A 1 96  ? -2.38300  17.08500  -32.80900 1.000 30.38042  ? 96  HIS A ND1 1 
ATOM   723  C  CD2 . HIS A 1 96  ? -0.35600  16.36600  -33.19700 1.000 36.78924  ? 96  HIS A CD2 1 
ATOM   724  C  CE1 . HIS A 1 96  ? -2.33400  15.82200  -32.42400 1.000 36.93641  ? 96  HIS A CE1 1 
ATOM   725  N  NE2 . HIS A 1 96  ? -1.11600  15.36100  -32.65100 1.000 38.45681  ? 96  HIS A NE2 1 
ATOM   726  N  N   . ALA A 1 97  ? -0.66300  20.90700  -36.42100 1.000 34.47215  ? 97  ALA A N   1 
ATOM   727  C  CA  . ALA A 1 97  ? -0.88400  22.20900  -37.04800 1.000 37.47759  ? 97  ALA A CA  1 
ATOM   728  C  C   . ALA A 1 97  ? -2.04000  22.13900  -38.04900 1.000 36.33891  ? 97  ALA A C   1 
ATOM   729  O  O   . ALA A 1 97  ? -2.91100  23.02000  -38.07200 1.000 33.42389  ? 97  ALA A O   1 
ATOM   730  C  CB  . ALA A 1 97  ? 0.40200   22.70600  -37.72400 1.000 34.72576  ? 97  ALA A CB  1 
ATOM   731  N  N   . ILE A 1 98  ? -2.08200  21.08300  -38.86400 1.000 36.42219  ? 98  ILE A N   1 
ATOM   732  C  CA  . ILE A 1 98  ? -3.21600  20.88800  -39.76800 1.000 35.17240  ? 98  ILE A CA  1 
ATOM   733  C  C   . ILE A 1 98  ? -4.51200  20.72700  -38.97900 1.000 33.45915  ? 98  ILE A C   1 
ATOM   734  O  O   . ILE A 1 98  ? -5.52800  21.35200  -39.29900 1.000 36.48745  ? 98  ILE A O   1 
ATOM   735  C  CB  . ILE A 1 98  ? -2.97400  19.68100  -40.68600 1.000 38.05215  ? 98  ILE A CB  1 
ATOM   736  C  CG1 . ILE A 1 98  ? -1.73500  19.92700  -41.54800 1.000 41.60268  ? 98  ILE A CG1 1 
ATOM   737  C  CG2 . ILE A 1 98  ? -4.21000  19.39500  -41.55200 1.000 32.12052  ? 98  ILE A CG2 1 
ATOM   738  C  CD1 . ILE A 1 98  ? -1.03500  18.65300  -41.94100 1.000 40.14746  ? 98  ILE A CD1 1 
ATOM   739  N  N   . CYS A 1 99  ? -4.50200  19.87700  -37.94800 1.000 33.88174  ? 99  CYS A N   1 
ATOM   740  C  CA  . CYS A 1 99  ? -5.72900  19.61200  -37.18800 1.000 35.88413  ? 99  CYS A CA  1 
ATOM   741  C  C   . CYS A 1 99  ? -6.27200  20.87600  -36.53000 1.000 33.20485  ? 99  CYS A C   1 
ATOM   742  O  O   . CYS A 1 99  ? -7.47200  21.16600  -36.61100 1.000 30.23291  ? 99  CYS A O   1 
ATOM   743  C  CB  . CYS A 1 99  ? -5.48300  18.54900  -36.12100 1.000 32.99749  ? 99  CYS A CB  1 
ATOM   744  S  SG  . CYS A 1 99  ? -5.36000  16.84500  -36.74000 1.000 37.39305  ? 99  CYS A SG  1 
ATOM   745  N  N   . GLU A 1 100 ? -5.40100  21.63100  -35.85600 1.000 34.88437  ? 100 GLU A N   1 
ATOM   746  C  CA  . GLU A 1 100 ? -5.83300  22.87100  -35.21700 1.000 36.80826  ? 100 GLU A CA  1 
ATOM   747  C  C   . GLU A 1 100 ? -6.48400  23.81600  -36.21300 1.000 36.95710  ? 100 GLU A C   1 
ATOM   748  O  O   . GLU A 1 100 ? -7.48400  24.46800  -35.89100 1.000 37.88898  ? 100 GLU A O   1 
ATOM   749  C  CB  . GLU A 1 100 ? -4.64900  23.56300  -34.55100 1.000 42.58266  ? 100 GLU A CB  1 
ATOM   750  C  CG  . GLU A 1 100 ? -4.23700  22.93600  -33.24700 1.000 50.15183  ? 100 GLU A CG  1 
ATOM   751  C  CD  . GLU A 1 100 ? -3.01100  23.60900  -32.66700 1.000 61.05253  ? 100 GLU A CD  1 
ATOM   752  O  OE1 . GLU A 1 100 ? -2.26200  24.25900  -33.44200 1.000 59.41652  ? 100 GLU A OE1 1 
ATOM   753  O  OE2 . GLU A 1 100 ? -2.81000  23.49400  -31.43900 1.000 64.29665  ? 100 GLU A OE2 1 
ATOM   754  N  N   . ALA A 1 101 ? -5.92900  23.91200  -37.42700 1.000 32.13699  ? 101 ALA A N   1 
ATOM   755  C  CA  . ALA A 1 101 ? -6.52100  24.78400  -38.43700 1.000 34.23592  ? 101 ALA A CA  1 
ATOM   756  C  C   . ALA A 1 101 ? -7.83200  24.20700  -38.96400 1.000 32.72075  ? 101 ALA A C   1 
ATOM   757  O  O   . ALA A 1 101 ? -8.82100  24.92900  -39.13100 1.000 33.02557  ? 101 ALA A O   1 
ATOM   758  C  CB  . ALA A 1 101 ? -5.52800  25.00500  -39.58100 1.000 35.63178  ? 101 ALA A CB  1 
ATOM   759  N  N   . TYR A 1 102 ? -7.85400  22.90800  -39.22700 1.000 32.34665  ? 102 TYR A N   1 
ATOM   760  C  CA  . TYR A 1 102 ? -9.03600  22.27100  -39.79300 1.000 32.63392  ? 102 TYR A CA  1 
ATOM   761  C  C   . TYR A 1 102 ? -10.21300 22.26900  -38.82000 1.000 31.15298  ? 102 TYR A C   1 
ATOM   762  O  O   . TYR A 1 102 ? -11.36400 22.44800  -39.23600 1.000 30.43666  ? 102 TYR A O   1 
ATOM   763  C  CB  . TYR A 1 102 ? -8.66700  20.85500  -40.19700 1.000 29.76758  ? 102 TYR A CB  1 
ATOM   764  C  CG  . TYR A 1 102 ? -9.79700  19.97200  -40.70300 1.000 33.58842  ? 102 TYR A CG  1 
ATOM   765  C  CD1 . TYR A 1 102 ? -10.25300 20.11300  -42.01100 1.000 31.74995  ? 102 TYR A CD1 1 
ATOM   766  C  CD2 . TYR A 1 102 ? -10.34100 18.98600  -39.87900 1.000 31.16925  ? 102 TYR A CD2 1 
ATOM   767  C  CE1 . TYR A 1 102 ? -11.25000 19.29000  -42.46500 1.000 36.31276  ? 102 TYR A CE1 1 
ATOM   768  C  CE2 . TYR A 1 102 ? -11.33900 18.18500  -40.36700 1.000 29.68634  ? 102 TYR A CE2 1 
ATOM   769  C  CZ  . TYR A 1 102 ? -11.80600 18.30600  -41.66600 1.000 32.02238  ? 102 TYR A CZ  1 
ATOM   770  O  OH  . TYR A 1 102 ? -12.77300 17.50500  -42.15100 1.000 32.57222  ? 102 TYR A OH  1 
ATOM   771  N  N   . PHE A 1 103 ? -9.95300  22.04700  -37.53200 1.000 28.47847  ? 103 PHE A N   1 
ATOM   772  C  CA  . PHE A 1 103 ? -11.00200 21.97900  -36.51800 1.000 30.63247  ? 103 PHE A CA  1 
ATOM   773  C  C   . PHE A 1 103 ? -11.27200 23.31400  -35.82800 1.000 34.96909  ? 103 PHE A C   1 
ATOM   774  O  O   . PHE A 1 103 ? -11.96100 23.32900  -34.79900 1.000 33.42967  ? 103 PHE A O   1 
ATOM   775  C  CB  . PHE A 1 103 ? -10.65000 20.94200  -35.45100 1.000 29.10599  ? 103 PHE A CB  1 
ATOM   776  C  CG  . PHE A 1 103 ? -10.73100 19.52500  -35.93500 1.000 30.17245  ? 103 PHE A CG  1 
ATOM   777  C  CD1 . PHE A 1 103 ? -11.96000 18.94000  -36.20700 1.000 30.36138  ? 103 PHE A CD1 1 
ATOM   778  C  CD2 . PHE A 1 103 ? -9.57900  18.77600  -36.11100 1.000 27.72631  ? 103 PHE A CD2 1 
ATOM   779  C  CE1 . PHE A 1 103 ? -12.03500 17.62100  -36.65300 1.000 28.92133  ? 103 PHE A CE1 1 
ATOM   780  C  CE2 . PHE A 1 103 ? -9.65400  17.46100  -36.56700 1.000 29.11089  ? 103 PHE A CE2 1 
ATOM   781  C  CZ  . PHE A 1 103 ? -10.88500 16.88900  -36.82700 1.000 28.60386  ? 103 PHE A CZ  1 
ATOM   782  N  N   . GLN A 1 104 ? -10.76100 24.42700  -36.37100 1.000 32.41123  ? 104 GLN A N   1 
ATOM   783  C  CA  . GLN A 1 104 ? -10.89600 25.71000  -35.68800 1.000 35.82862  ? 104 GLN A CA  1 
ATOM   784  C  C   . GLN A 1 104 ? -12.35200 26.02000  -35.35900 1.000 34.50420  ? 104 GLN A C   1 
ATOM   785  O  O   . GLN A 1 104 ? -12.65000 26.58200  -34.30200 1.000 35.70467  ? 104 GLN A O   1 
ATOM   786  C  CB  . GLN A 1 104 ? -10.29200 26.83000  -36.54300 1.000 36.12817  ? 104 GLN A CB  1 
ATOM   787  C  CG  . GLN A 1 104 ? -10.18000 28.20500  -35.84100 1.000 46.83947  ? 104 GLN A CG  1 
ATOM   788  C  CD  . GLN A 1 104 ? -11.51900 28.94800  -35.69400 1.000 51.93304  ? 104 GLN A CD  1 
ATOM   789  O  OE1 . GLN A 1 104 ? -12.31600 29.02100  -36.63500 1.000 52.47690  ? 104 GLN A OE1 1 
ATOM   790  N  NE2 . GLN A 1 104 ? -11.76500 29.50000  -34.50100 1.000 52.38800  ? 104 GLN A NE2 1 
ATOM   791  N  N   . ARG A 1 105 ? -13.27000 25.67200  -36.26100 1.000 33.61149  ? 105 ARG A N   1 
ATOM   792  C  CA  . ARG A 1 105 ? -14.67500 26.01900  -36.07500 1.000 34.00237  ? 105 ARG A CA  1 
ATOM   793  C  C   . ARG A 1 105 ? -15.36600 25.08400  -35.08800 1.000 32.79486  ? 105 ARG A C   1 
ATOM   794  O  O   . ARG A 1 105 ? -16.24200 25.52200  -34.33400 1.000 32.09213  ? 105 ARG A O   1 
ATOM   795  C  CB  . ARG A 1 105 ? -15.40400 26.00100  -37.42700 1.000 31.44970  ? 105 ARG A CB  1 
ATOM   796  C  CG  . ARG A 1 105 ? -14.91500 27.02200  -38.43200 1.000 33.71645  ? 105 ARG A CG  1 
ATOM   797  C  CD  . ARG A 1 105 ? -15.55000 26.78800  -39.82800 1.000 34.89023  ? 105 ARG A CD  1 
ATOM   798  N  NE  . ARG A 1 105 ? -16.99300 26.98000  -39.78100 1.000 38.06597  ? 105 ARG A NE  1 
ATOM   799  C  CZ  . ARG A 1 105 ? -17.86800 26.38400  -40.57900 1.000 36.51148  ? 105 ARG A CZ  1 
ATOM   800  N  NH1 . ARG A 1 105 ? -17.48000 25.53600  -41.51900 1.000 35.43967  ? 105 ARG A NH1 1 
ATOM   801  N  NH2 . ARG A 1 105 ? -19.16700 26.63200  -40.41400 1.000 32.70625  ? 105 ARG A NH2 1 
ATOM   802  N  N   . THR A 1 106 ? -14.99800 23.80600  -35.06200 1.000 32.71274  ? 106 THR A N   1 
ATOM   803  C  CA  . THR A 1 106 ? -15.63600 22.89800  -34.12000 1.000 31.31349  ? 106 THR A CA  1 
ATOM   804  C  C   . THR A 1 106 ? -14.96600 22.90500  -32.74600 1.000 32.77955  ? 106 THR A C   1 
ATOM   805  O  O   . THR A 1 106 ? -15.60500 22.51400  -31.75700 1.000 29.33260  ? 106 THR A O   1 
ATOM   806  C  CB  . THR A 1 106 ? -15.67100 21.46600  -34.69100 1.000 30.12590  ? 106 THR A CB  1 
ATOM   807  O  OG1 . THR A 1 106 ? -16.72300 20.72200  -34.05200 1.000 31.09359  ? 106 THR A OG1 1 
ATOM   808  C  CG2 . THR A 1 106 ? -14.35800 20.73600  -34.47600 1.000 27.82615  ? 106 THR A CG2 1 
ATOM   809  N  N   . GLY A 1 107 ? -13.71700 23.36100  -32.65000 1.000 30.96342  ? 107 GLY A N   1 
ATOM   810  C  CA  . GLY A 1 107 ? -13.03100 23.39100  -31.37200 1.000 28.93918  ? 107 GLY A CA  1 
ATOM   811  C  C   . GLY A 1 107 ? -12.03300 22.25600  -31.24400 1.000 31.03319  ? 107 GLY A C   1 
ATOM   812  O  O   . GLY A 1 107 ? -11.39600 21.87200  -32.24000 1.000 28.80853  ? 107 GLY A O   1 
ATOM   813  N  N   . ASP A 1 108 ? -11.90600 21.70600  -30.03900 1.000 23.99364  ? 108 ASP A N   1 
ATOM   814  C  CA  . ASP A 1 108 ? -10.92900 20.65500  -29.77400 1.000 29.72680  ? 108 ASP A CA  1 
ATOM   815  C  C   . ASP A 1 108 ? -11.27000 19.36200  -30.51500 1.000 25.36621  ? 108 ASP A C   1 
ATOM   816  O  O   . ASP A 1 108 ? -12.43500 19.05900  -30.77400 1.000 26.27319  ? 108 ASP A O   1 
ATOM   817  C  CB  . ASP A 1 108 ? -10.84800 20.36700  -28.26700 1.000 27.80059  ? 108 ASP A CB  1 
ATOM   818  C  CG  . ASP A 1 108 ? -9.96900  21.36800  -27.50300 1.000 31.83531  ? 108 ASP A CG  1 
ATOM   819  O  OD1 . ASP A 1 108 ? -9.27500  22.20300  -28.13100 1.000 35.10149  ? 108 ASP A OD1 1 
ATOM   820  O  OD2 . ASP A 1 108 ? -9.96600  21.31600  -26.25200 1.000 34.45703  ? 108 ASP A OD2 1 
ATOM   821  N  N   . TYR A 1 109 ? -10.23200 18.57700  -30.81200 1.000 24.09240  ? 109 TYR A N   1 
ATOM   822  C  CA  . TYR A 1 109 ? -10.33600 17.29000  -31.48900 1.000 23.89248  ? 109 TYR A CA  1 
ATOM   823  C  C   . TYR A 1 109 ? -9.56600  16.25700  -30.66900 1.000 24.72934  ? 109 TYR A C   1 
ATOM   824  O  O   . TYR A 1 109 ? -8.75000  16.61000  -29.81700 1.000 27.04223  ? 109 TYR A O   1 
ATOM   825  C  CB  . TYR A 1 109 ? -9.76700  17.39400  -32.93100 1.000 27.18536  ? 109 TYR A CB  1 
ATOM   826  C  CG  . TYR A 1 109 ? -8.30300  17.82200  -32.90200 1.000 28.46629  ? 109 TYR A CG  1 
ATOM   827  C  CD1 . TYR A 1 109 ? -7.95000  19.17200  -32.82500 1.000 30.15803  ? 109 TYR A CD1 1 
ATOM   828  C  CD2 . TYR A 1 109 ? -7.29900  16.85300  -32.89900 1.000 27.96411  ? 109 TYR A CD2 1 
ATOM   829  C  CE1 . TYR A 1 109 ? -6.61800  19.52100  -32.77100 1.000 30.86380  ? 109 TYR A CE1 1 
ATOM   830  C  CE2 . TYR A 1 109 ? -5.98000  17.23700  -32.84500 1.000 29.14715  ? 109 TYR A CE2 1 
ATOM   831  C  CZ  . TYR A 1 109 ? -5.60400  18.57000  -32.76800 1.000 32.22476  ? 109 TYR A CZ  1 
ATOM   832  O  OH  . TYR A 1 109 ? -4.29500  18.91100  -32.71200 1.000 35.05272  ? 109 TYR A OH  1 
ATOM   833  N  N   . TRP A 1 110 ? -9.84700  14.96900  -30.87800 1.000 24.40332  ? 110 TRP A N   1 
ATOM   834  C  CA  . TRP A 1 110 ? -9.00000  13.93700  -30.26900 1.000 25.52473  ? 110 TRP A CA  1 
ATOM   835  C  C   . TRP A 1 110 ? -9.01100  12.69900  -31.15500 1.000 25.59825  ? 110 TRP A C   1 
ATOM   836  O  O   . TRP A 1 110 ? -9.61700  12.69000  -32.22600 1.000 26.56927  ? 110 TRP A O   1 
ATOM   837  C  CB  . TRP A 1 110 ? -9.41400  13.60200  -28.81900 1.000 24.43569  ? 110 TRP A CB  1 
ATOM   838  C  CG  . TRP A 1 110 ? -10.87100 13.26400  -28.56600 1.000 23.68936  ? 110 TRP A CG  1 
ATOM   839  C  CD1 . TRP A 1 110 ? -11.83200 12.95400  -29.49500 1.000 20.92501  ? 110 TRP A CD1 1 
ATOM   840  C  CD2 . TRP A 1 110 ? -11.52800 13.22000  -27.28000 1.000 22.22659  ? 110 TRP A CD2 1 
ATOM   841  N  NE1 . TRP A 1 110 ? -13.03900 12.71300  -28.86500 1.000 23.18439  ? 110 TRP A NE1 1 
ATOM   842  C  CE2 . TRP A 1 110 ? -12.87700 12.85900  -27.51100 1.000 22.13638  ? 110 TRP A CE2 1 
ATOM   843  C  CE3 . TRP A 1 110 ? -11.09700 13.42800  -25.96200 1.000 21.72572  ? 110 TRP A CE3 1 
ATOM   844  C  CZ2 . TRP A 1 110 ? -13.80700 12.73900  -26.47700 1.000 21.60547  ? 110 TRP A CZ2 1 
ATOM   845  C  CZ3 . TRP A 1 110 ? -12.02400 13.29800  -24.93100 1.000 24.85633  ? 110 TRP A CZ3 1 
ATOM   846  C  CH2 . TRP A 1 110 ? -13.35900 12.94700  -25.19400 1.000 25.25738  ? 110 TRP A CH2 1 
ATOM   847  N  N   . LEU A 1 111 ? -8.33600  11.64000  -30.70100 1.000 25.71681  ? 111 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 111 ? -8.19800  10.42400  -31.50000 1.000 29.44489  ? 111 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 111 ? -9.40600  9.51300   -31.28300 1.000 27.18520  ? 111 LEU A C   1 
ATOM   850  O  O   . LEU A 1 111 ? -9.61600  9.00400   -30.17700 1.000 27.97763  ? 111 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 111 ? -6.89900  9.68700   -31.15800 1.000 28.00203  ? 111 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 111 ? -6.61400  8.47000   -32.04500 1.000 32.36218  ? 111 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 111 ? -6.17800  8.91200   -33.46200 1.000 31.42162  ? 111 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 111 ? -5.56400  7.56000   -31.41600 1.000 30.34164  ? 111 LEU A CD2 1 
ATOM   855  N  N   . SER A 1 112 ? -10.18100 9.28200   -32.34200 1.000 26.06672  ? 112 SER A N   1 
ATOM   856  C  CA  . SER A 1 112 ? -11.27000 8.30900   -32.25300 1.000 29.31551  ? 112 SER A CA  1 
ATOM   857  C  C   . SER A 1 112 ? -10.76100 6.87900   -32.41800 1.000 29.15444  ? 112 SER A C   1 
ATOM   858  O  O   . SER A 1 112 ? -11.26200 5.95900   -31.75800 1.000 27.54314  ? 112 SER A O   1 
ATOM   859  C  CB  . SER A 1 112 ? -12.34400 8.61400   -33.30700 1.000 28.37237  ? 112 SER A CB  1 
ATOM   860  O  OG  . SER A 1 112 ? -13.50300 7.79400   -33.13900 1.000 27.00559  ? 112 SER A OG  1 
ATOM   861  N  N   . ALA A 1 113 ? -9.75900  6.68400   -33.26900 1.000 28.11129  ? 113 ALA A N   1 
ATOM   862  C  CA  . ALA A 1 113 ? -9.23700  5.36700   -33.59400 1.000 30.18517  ? 113 ALA A CA  1 
ATOM   863  C  C   . ALA A 1 113 ? -7.91100  5.54000   -34.31500 1.000 30.50040  ? 113 ALA A C   1 
ATOM   864  O  O   . ALA A 1 113 ? -7.72700  6.50300   -35.06200 1.000 31.48644  ? 113 ALA A O   1 
ATOM   865  C  CB  . ALA A 1 113 ? -10.20600 4.57100   -34.48600 1.000 27.46406  ? 113 ALA A CB  1 
ATOM   866  N  N   . ALA A 1 114 ? -6.99900  4.60600   -34.08200 1.000 30.82271  ? 114 ALA A N   1 
ATOM   867  C  CA  . ALA A 1 114 ? -5.81700  4.46700   -34.92200 1.000 34.77933  ? 114 ALA A CA  1 
ATOM   868  C  C   . ALA A 1 114 ? -5.46700  2.99200   -34.92400 1.000 34.43200  ? 114 ALA A C   1 
ATOM   869  O  O   . ALA A 1 114 ? -5.28300  2.40300   -33.85400 1.000 34.65110  ? 114 ALA A O   1 
ATOM   870  C  CB  . ALA A 1 114 ? -4.65200  5.32700   -34.42800 1.000 30.36727  ? 114 ALA A CB  1 
ATOM   871  N  N   . PHE A 1 115 ? -5.41200  2.39700   -36.11200 1.000 32.43279  ? 115 PHE A N   1 
ATOM   872  C  CA  . PHE A 1 115 ? -5.32800  0.95200   -36.23600 1.000 35.87461  ? 115 PHE A CA  1 
ATOM   873  C  C   . PHE A 1 115 ? -4.57500  0.59100   -37.51100 1.000 38.02006  ? 115 PHE A C   1 
ATOM   874  O  O   . PHE A 1 115 ? -4.43200  1.40800   -38.42600 1.000 35.89830  ? 115 PHE A O   1 
ATOM   875  C  CB  . PHE A 1 115 ? -6.72500  0.31400   -36.22700 1.000 34.82027  ? 115 PHE A CB  1 
ATOM   876  C  CG  . PHE A 1 115 ? -7.62700  0.80200   -37.32500 1.000 37.43757  ? 115 PHE A CG  1 
ATOM   877  C  CD1 . PHE A 1 115 ? -8.33600  1.98500   -37.18200 1.000 35.76859  ? 115 PHE A CD1 1 
ATOM   878  C  CD2 . PHE A 1 115 ? -7.78400  0.06600   -38.49800 1.000 37.44300  ? 115 PHE A CD2 1 
ATOM   879  C  CE1 . PHE A 1 115 ? -9.18300  2.43500   -38.20200 1.000 41.08752  ? 115 PHE A CE1 1 
ATOM   880  C  CE2 . PHE A 1 115 ? -8.62200  0.50000   -39.51500 1.000 35.70677  ? 115 PHE A CE2 1 
ATOM   881  C  CZ  . PHE A 1 115 ? -9.32000  1.68900   -39.37700 1.000 38.17208  ? 115 PHE A CZ  1 
ATOM   882  N  N   . LEU A 1 116 ? -4.09400  -0.65000  -37.55400 1.000 36.90737  ? 116 LEU A N   1 
ATOM   883  C  CA  . LEU A 1 116 ? -3.35000  -1.18200  -38.69100 1.000 38.94296  ? 116 LEU A CA  1 
ATOM   884  C  C   . LEU A 1 116 ? -4.25100  -2.05900  -39.54700 1.000 41.03362  ? 116 LEU A C   1 
ATOM   885  O  O   . LEU A 1 116 ? -4.99300  -2.89200  -39.02300 1.000 42.64798  ? 116 LEU A O   1 
ATOM   886  C  CB  . LEU A 1 116 ? -2.14500  -2.00700  -38.21900 1.000 37.58509  ? 116 LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 116 ? -1.45600  -2.82700  -39.31900 1.000 45.34795  ? 116 LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 116 ? -0.92200  -1.89000  -40.36000 1.000 45.37249  ? 116 LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 116 ? -0.32700  -3.70400  -38.79000 1.000 50.41470  ? 116 LEU A CD2 1 
ATOM   890  N  N   . ARG A 1 117 ? -4.17900  -1.88900  -40.86600 1.000 42.84682  ? 117 ARG A N   1 
ATOM   891  C  CA  . ARG A 1 117 ? -4.76300  -2.86700  -41.77700 1.000 46.38629  ? 117 ARG A CA  1 
ATOM   892  C  C   . ARG A 1 117 ? -3.70700  -3.34800  -42.76300 1.000 47.46010  ? 117 ARG A C   1 
ATOM   893  O  O   . ARG A 1 117 ? -2.88900  -2.55900  -43.23600 1.000 45.05853  ? 117 ARG A O   1 
ATOM   894  C  CB  . ARG A 1 117 ? -5.97300  -2.29700  -42.52400 1.000 46.07157  ? 117 ARG A CB  1 
ATOM   895  C  CG  . ARG A 1 117 ? -7.17000  -2.07100  -41.60100 1.000 48.89160  ? 117 ARG A CG  1 
ATOM   896  C  CD  . ARG A 1 117 ? -8.51500  -2.04500  -42.32700 1.000 56.20153  ? 117 ARG A CD  1 
ATOM   897  N  NE  . ARG A 1 117 ? -8.60500  -3.00400  -43.42400 1.000 64.00652  ? 117 ARG A NE  1 
ATOM   898  C  CZ  . ARG A 1 117 ? -8.52500  -4.32400  -43.29600 1.000 63.28548  ? 117 ARG A CZ  1 
ATOM   899  N  NH1 . ARG A 1 117 ? -8.33100  -4.89600  -42.11900 1.000 63.24245  ? 117 ARG A NH1 1 
ATOM   900  N  NH2 . ARG A 1 117 ? -8.60800  -5.08900  -44.38200 1.000 68.71139  ? 117 ARG A NH2 1 
ATOM   901  N  N   . GLU A 1 118 ? -3.71500  -4.64900  -43.04700 1.000 50.06166  ? 118 GLU A N   1 
ATOM   902  C  CA  . GLU A 1 118 ? -2.87200  -5.25100  -44.07700 1.000 52.20779  ? 118 GLU A CA  1 
ATOM   903  C  C   . GLU A 1 118 ? -3.75700  -5.84600  -45.16100 1.000 51.74600  ? 118 GLU A C   1 
ATOM   904  O  O   . GLU A 1 118 ? -4.71600  -6.56200  -44.85700 1.000 57.44869  ? 118 GLU A O   1 
ATOM   905  C  CB  . GLU A 1 118 ? -1.96400  -6.34200  -43.50900 1.000 54.81071  ? 118 GLU A CB  1 
ATOM   906  C  CG  . GLU A 1 118 ? -0.72700  -5.82800  -42.81400 1.000 57.53489  ? 118 GLU A CG  1 
ATOM   907  C  CD  . GLU A 1 118 ? 0.26900   -6.93800  -42.51300 1.000 62.41004  ? 118 GLU A CD  1 
ATOM   908  O  OE1 . GLU A 1 118 ? -0.04000  -8.12600  -42.78500 1.000 65.64708  ? 118 GLU A OE1 1 
ATOM   909  O  OE2 . GLU A 1 118 ? 1.36600   -6.62100  -42.00700 1.000 63.46089  ? 118 GLU A OE2 1 
ATOM   910  N  N   . ILE A 1 119 ? -3.42700  -5.56600  -46.41600 1.000 53.90789  ? 119 ILE A N   1 
ATOM   911  C  CA  . ILE A 1 119 ? -4.25100  -5.96100  -47.55100 1.000 58.77671  ? 119 ILE A CA  1 
ATOM   912  C  C   . ILE A 1 119 ? -3.41200  -6.84100  -48.46000 1.000 58.30117  ? 119 ILE A C   1 
ATOM   913  O  O   . ILE A 1 119 ? -2.49500  -6.35200  -49.13200 1.000 58.54616  ? 119 ILE A O   1 
ATOM   914  C  CB  . ILE A 1 119 ? -4.79700  -4.74900  -48.30400 1.000 55.98107  ? 119 ILE A CB  1 
ATOM   915  C  CG1 . ILE A 1 119 ? -5.71100  -3.96000  -47.37300 1.000 55.30269  ? 119 ILE A CG1 1 
ATOM   916  C  CG2 . ILE A 1 119 ? -5.56200  -5.18700  -49.53400 1.000 57.91860  ? 119 ILE A CG2 1 
ATOM   917  C  CD1 . ILE A 1 119 ? -5.70200  -2.51700  -47.64100 1.000 55.97098  ? 119 ILE A CD1 1 
ATOM   918  N  N   . GLU A 1 120 ? -3.74000  -8.13100  -48.49900 1.000 61.04647  ? 120 GLU A N   1 
ATOM   919  C  CA  . GLU A 1 120 ? -2.94100  -9.11800  -49.21000 1.000 61.42837  ? 120 GLU A CA  1 
ATOM   920  C  C   . GLU A 1 120 ? -3.13200  -8.99900  -50.72200 1.000 62.00573  ? 120 GLU A C   1 
ATOM   921  O  O   . GLU A 1 120 ? -3.95400  -8.22700  -51.21800 1.000 61.13479  ? 120 GLU A O   1 
ATOM   922  C  CB  . GLU A 1 120 ? -3.30600  -10.53000 -48.75500 1.000 67.47962  ? 120 GLU A CB  1 
ATOM   923  C  CG  . GLU A 1 120 ? -2.72700  -10.92600 -47.40400 1.000 74.33766  ? 120 GLU A CG  1 
ATOM   924  C  CD  . GLU A 1 120 ? -3.80200  -11.16700 -46.35800 1.000 82.82493  ? 120 GLU A CD  1 
ATOM   925  O  OE1 . GLU A 1 120 ? -4.99600  -11.21800 -46.73300 1.000 85.53923  ? 120 GLU A OE1 1 
ATOM   926  O  OE2 . GLU A 1 120 ? -3.45500  -11.30500 -45.16300 1.000 83.72700  ? 120 GLU A OE2 1 
ATOM   927  N  N   . SER A 1 121 ? -2.35400  -9.79600  -51.45400 1.000 63.30751  ? 121 SER A N   1 
ATOM   928  C  CA  . SER A 1 121 ? -2.50400  -9.88000  -52.90100 1.000 65.68339  ? 121 SER A CA  1 
ATOM   929  C  C   . SER A 1 121 ? -3.86400  -10.46300 -53.26600 1.000 67.31785  ? 121 SER A C   1 
ATOM   930  O  O   . SER A 1 121 ? -4.43900  -11.27000 -52.52800 1.000 67.64408  ? 121 SER A O   1 
ATOM   931  C  CB  . SER A 1 121 ? -1.39800  -10.74600 -53.50800 1.000 68.24571  ? 121 SER A CB  1 
ATOM   932  O  OG  . SER A 1 121 ? -0.15300  -10.07800 -53.49800 1.000 71.12299  ? 121 SER A OG  1 
ATOM   933  N  N   . GLY A 1 122 ? -4.37300  -10.04800 -54.42600 1.000 66.81352  ? 122 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 122 ? -5.65700  -10.52300 -54.90300 1.000 67.04247  ? 122 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 122 ? -6.86400  -9.93400  -54.20500 1.000 68.41978  ? 122 GLY A C   1 
ATOM   936  O  O   . GLY A 1 122 ? -7.96200  -10.48500 -54.31800 1.000 70.73143  ? 122 GLY A O   1 
ATOM   937  N  N   . MET A 1 123 ? -6.69900  -8.83700  -53.48800 1.000 65.15363  ? 123 MET A N   1 
ATOM   938  C  CA  . MET A 1 123 ? -7.85200  -8.24700  -52.81500 1.000 67.87517  ? 123 MET A CA  1 
ATOM   939  C  C   . MET A 1 123 ? -8.50500  -7.20800  -53.71500 1.000 65.37943  ? 123 MET A C   1 
ATOM   940  O  O   . MET A 1 123 ? -7.80200  -6.36700  -54.28800 1.000 63.52430  ? 123 MET A O   1 
ATOM   941  C  CB  . MET A 1 123 ? -7.45000  -7.60300  -51.49700 1.000 64.85890  ? 123 MET A CB  1 
ATOM   942  C  CG  . MET A 1 123 ? -7.16600  -8.61000  -50.39700 1.000 70.07315  ? 123 MET A CG  1 
ATOM   943  S  SD  . MET A 1 123 ? -8.52100  -9.79200  -50.21000 1.000 80.11848  ? 123 MET A SD  1 
ATOM   944  C  CE  . MET A 1 123 ? -7.76100  -11.31200 -50.77800 1.000 78.52659  ? 123 MET A CE  1 
ATOM   945  N  N   . PRO A 1 124 ? -9.82500  -7.23900  -53.87100 1.000 64.57958  ? 124 PRO A N   1 
ATOM   946  C  CA  . PRO A 1 124 ? -10.49200 -6.25000  -54.71900 1.000 59.58869  ? 124 PRO A CA  1 
ATOM   947  C  C   . PRO A 1 124 ? -10.57600 -4.90500  -54.02600 1.000 57.92964  ? 124 PRO A C   1 
ATOM   948  O  O   . PRO A 1 124 ? -10.54900 -4.80300  -52.79900 1.000 59.97788  ? 124 PRO A O   1 
ATOM   949  C  CB  . PRO A 1 124 ? -11.88600 -6.84900  -54.92300 1.000 62.40048  ? 124 PRO A CB  1 
ATOM   950  C  CG  . PRO A 1 124 ? -12.12400 -7.59800  -53.64500 1.000 67.66704  ? 124 PRO A CG  1 
ATOM   951  C  CD  . PRO A 1 124 ? -10.78100 -8.17700  -53.25700 1.000 67.22949  ? 124 PRO A CD  1 
ATOM   952  N  N   . ALA A 1 125 ? -10.67900 -3.86300  -54.84000 1.000 57.36175  ? 125 ALA A N   1 
ATOM   953  C  CA  . ALA A 1 125 ? -10.80500 -2.52000  -54.30300 1.000 53.73394  ? 125 ALA A CA  1 
ATOM   954  C  C   . ALA A 1 125 ? -12.08900 -2.38400  -53.48500 1.000 51.50764  ? 125 ALA A C   1 
ATOM   955  O  O   . ALA A 1 125 ? -13.05000 -3.14200  -53.65100 1.000 51.38497  ? 125 ALA A O   1 
ATOM   956  C  CB  . ALA A 1 125 ? -10.78600 -1.49100  -55.43500 1.000 50.75973  ? 125 ALA A CB  1 
ATOM   957  N  N   . GLN A 1 126 ? -12.07600 -1.41900  -52.57200 1.000 48.95727  ? 126 GLN A N   1 
ATOM   958  C  CA  . GLN A 1 126 ? -13.26100 -1.05800  -51.80400 1.000 47.82003  ? 126 GLN A CA  1 
ATOM   959  C  C   . GLN A 1 126 ? -14.28100 -0.35700  -52.70100 1.000 46.27231  ? 126 GLN A C   1 
ATOM   960  O  O   . GLN A 1 126 ? -13.91700 0.27600   -53.69400 1.000 47.50991  ? 126 GLN A O   1 
ATOM   961  C  CB  . GLN A 1 126 ? -12.87500 -0.12000  -50.66700 1.000 43.96710  ? 126 GLN A CB  1 
ATOM   962  C  CG  . GLN A 1 126 ? -13.01500 -0.67700  -49.27400 1.000 47.14667  ? 126 GLN A CG  1 
ATOM   963  C  CD  . GLN A 1 126 ? -12.50700 0.29300   -48.22500 1.000 43.05837  ? 126 GLN A CD  1 
ATOM   964  O  OE1 . GLN A 1 126 ? -11.92800 1.33300   -48.54800 1.000 44.16478  ? 126 GLN A OE1 1 
ATOM   965  N  NE2 . GLN A 1 126 ? -12.70600 -0.04800  -46.96400 1.000 48.98219  ? 126 GLN A NE2 1 
ATOM   966  N  N   . PRO A 1 127 ? -15.56400 -0.44600  -52.37900 1.000 46.40836  ? 127 PRO A N   1 
ATOM   967  C  CA  . PRO A 1 127 ? -16.52000 0.47100   -53.00400 1.000 40.20736  ? 127 PRO A CA  1 
ATOM   968  C  C   . PRO A 1 127 ? -16.24400 1.90100   -52.56400 1.000 41.38226  ? 127 PRO A C   1 
ATOM   969  O  O   . PRO A 1 127 ? -15.73000 2.15900   -51.46700 1.000 38.26844  ? 127 PRO A O   1 
ATOM   970  C  CB  . PRO A 1 127 ? -17.88100 -0.02300  -52.49500 1.000 43.68041  ? 127 PRO A CB  1 
ATOM   971  C  CG  . PRO A 1 127 ? -17.56700 -0.82400  -51.26800 1.000 43.46737  ? 127 PRO A CG  1 
ATOM   972  C  CD  . PRO A 1 127 ? -16.22000 -1.43500  -51.50500 1.000 47.07147  ? 127 PRO A CD  1 
ATOM   973  N  N   . PHE A 1 128 ? -16.57500 2.84200   -53.44600 1.000 38.20256  ? 128 PHE A N   1 
ATOM   974  C  CA  . PHE A 1 128 ? -16.45800 4.24600   -53.08800 1.000 35.08158  ? 128 PHE A CA  1 
ATOM   975  C  C   . PHE A 1 128 ? -17.43800 4.57100   -51.96700 1.000 36.87484  ? 128 PHE A C   1 
ATOM   976  O  O   . PHE A 1 128 ? -18.56600 4.07600   -51.94600 1.000 34.58405  ? 128 PHE A O   1 
ATOM   977  C  CB  . PHE A 1 128 ? -16.70900 5.13000   -54.30400 1.000 36.52481  ? 128 PHE A CB  1 
ATOM   978  C  CG  . PHE A 1 128 ? -15.52200 5.23600   -55.23700 1.000 35.98416  ? 128 PHE A CG  1 
ATOM   979  C  CD1 . PHE A 1 128 ? -14.35400 5.86200   -54.82400 1.000 37.14156  ? 128 PHE A CD1 1 
ATOM   980  C  CD2 . PHE A 1 128 ? -15.58700 4.72800   -56.52500 1.000 36.78773  ? 128 PHE A CD2 1 
ATOM   981  C  CE1 . PHE A 1 128 ? -13.25700 5.96600   -55.69100 1.000 41.53288  ? 128 PHE A CE1 1 
ATOM   982  C  CE2 . PHE A 1 128 ? -14.49400 4.82100   -57.39600 1.000 39.17207  ? 128 PHE A CE2 1 
ATOM   983  C  CZ  . PHE A 1 128 ? -13.33100 5.44600   -56.97400 1.000 40.15858  ? 128 PHE A CZ  1 
ATOM   984  N  N   . HIS A 1 129 ? -16.99000 5.38400   -51.02000 1.000 34.53755  ? 129 HIS A N   1 
ATOM   985  C  CA  . HIS A 1 129 ? -17.76900 5.69500   -49.83700 1.000 36.76325  ? 129 HIS A CA  1 
ATOM   986  C  C   . HIS A 1 129 ? -17.18000 6.93900   -49.18900 1.000 36.02449  ? 129 HIS A C   1 
ATOM   987  O  O   . HIS A 1 129 ? -16.08300 7.38800   -49.53800 1.000 36.25212  ? 129 HIS A O   1 
ATOM   988  C  CB  . HIS A 1 129 ? -17.74300 4.53000   -48.84700 1.000 36.12254  ? 129 HIS A CB  1 
ATOM   989  C  CG  . HIS A 1 129 ? -16.38200 4.30100   -48.28300 1.000 37.83796  ? 129 HIS A CG  1 
ATOM   990  N  ND1 . HIS A 1 129 ? -15.43900 3.51600   -48.91600 1.000 39.33659  ? 129 HIS A ND1 1 
ATOM   991  C  CD2 . HIS A 1 129 ? -15.77100 4.82700   -47.19700 1.000 38.23439  ? 129 HIS A CD2 1 
ATOM   992  C  CE1 . HIS A 1 129 ? -14.31700 3.53800   -48.22100 1.000 38.69815  ? 129 HIS A CE1 1 
ATOM   993  N  NE2 . HIS A 1 129 ? -14.49800 4.31800   -47.16700 1.000 37.35509  ? 129 HIS A NE2 1 
ATOM   994  N  N   . ARG A 1 130 ? -17.92400 7.47800   -48.22800 1.000 35.05684  ? 130 ARG A N   1 
ATOM   995  C  CA  . ARG A 1 130 ? -17.43900 8.47300   -47.28200 1.000 35.91613  ? 130 ARG A CA  1 
ATOM   996  C  C   . ARG A 1 130 ? -17.26200 7.83400   -45.90800 1.000 37.69493  ? 130 ARG A C   1 
ATOM   997  O  O   . ARG A 1 130 ? -17.90600 6.82900   -45.58700 1.000 38.32380  ? 130 ARG A O   1 
ATOM   998  C  CB  . ARG A 1 130 ? -18.41100 9.65000   -47.17300 1.000 38.03863  ? 130 ARG A CB  1 
ATOM   999  C  CG  . ARG A 1 130 ? -18.71100 10.31800  -48.49700 1.000 37.57694  ? 130 ARG A CG  1 
ATOM   1000 C  CD  . ARG A 1 130 ? -19.90000 11.25300  -48.42100 1.000 37.66625  ? 130 ARG A CD  1 
ATOM   1001 N  NE  . ARG A 1 130 ? -19.66100 12.39900  -49.29100 1.000 39.73113  ? 130 ARG A NE  1 
ATOM   1002 C  CZ  . ARG A 1 130 ? -20.60500 13.14600  -49.84500 1.000 38.93761  ? 130 ARG A CZ  1 
ATOM   1003 N  NH1 . ARG A 1 130 ? -21.88900 12.87900  -49.67100 1.000 39.76556  ? 130 ARG A NH1 1 
ATOM   1004 N  NH2 . ARG A 1 130 ? -20.24900 14.17900  -50.60500 1.000 37.36616  ? 130 ARG A NH2 1 
ATOM   1005 N  N   . ASP A 1 131 ? -16.39900 8.43900   -45.08500 1.000 38.25718  ? 131 ASP A N   1 
ATOM   1006 C  CA  . ASP A 1 131 ? -16.14800 7.94500   -43.72300 1.000 39.42025  ? 131 ASP A CA  1 
ATOM   1007 C  C   . ASP A 1 131 ? -17.17300 8.52100   -42.73800 1.000 38.39440  ? 131 ASP A C   1 
ATOM   1008 O  O   . ASP A 1 131 ? -16.85800 9.32500   -41.86100 1.000 39.59850  ? 131 ASP A O   1 
ATOM   1009 C  CB  . ASP A 1 131 ? -14.73300 8.29400   -43.28600 1.000 38.13069  ? 131 ASP A CB  1 
ATOM   1010 C  CG  . ASP A 1 131 ? -13.69500 7.41700   -43.93200 1.000 42.10666  ? 131 ASP A CG  1 
ATOM   1011 O  OD1 . ASP A 1 131 ? -14.08500 6.32500   -44.38900 1.000 38.38589  ? 131 ASP A OD1 1 
ATOM   1012 O  OD2 . ASP A 1 131 ? -12.50000 7.81500   -43.97200 1.000 45.88447  ? 131 ASP A OD2 1 
ATOM   1013 N  N   . ASP A 1 132 ? -18.43100 8.07900   -42.88500 1.000 36.51033  ? 132 ASP A N   1 
ATOM   1014 C  CA  . ASP A 1 132 ? -19.51200 8.57000   -42.03400 1.000 35.49122  ? 132 ASP A CA  1 
ATOM   1015 C  C   . ASP A 1 132 ? -20.26800 7.43700   -41.34200 1.000 35.69038  ? 132 ASP A C   1 
ATOM   1016 O  O   . ASP A 1 132 ? -21.42900 7.62000   -40.95300 1.000 38.34793  ? 132 ASP A O   1 
ATOM   1017 C  CB  . ASP A 1 132 ? -20.48700 9.45200   -42.83400 1.000 35.80487  ? 132 ASP A CB  1 
ATOM   1018 C  CG  . ASP A 1 132 ? -21.16500 8.70600   -43.99900 1.000 44.17886  ? 132 ASP A CG  1 
ATOM   1019 O  OD1 . ASP A 1 132 ? -21.06700 7.45800   -44.08000 1.000 44.70951  ? 132 ASP A OD1 1 
ATOM   1020 O  OD2 . ASP A 1 132 ? -21.80000 9.37600   -44.85100 1.000 47.46476  ? 132 ASP A OD2 1 
ATOM   1021 N  N   . ALA A 1 133 ? -19.64400 6.27600   -41.17500 1.000 32.25037  ? 133 ALA A N   1 
ATOM   1022 C  CA  . ALA A 1 133 ? -20.36300 5.12100   -40.65800 1.000 33.96551  ? 133 ALA A CA  1 
ATOM   1023 C  C   . ALA A 1 133 ? -20.17700 4.92100   -39.15800 1.000 32.62032  ? 133 ALA A C   1 
ATOM   1024 O  O   . ALA A 1 133 ? -21.11500 4.48100   -38.48500 1.000 32.94892  ? 133 ALA A O   1 
ATOM   1025 C  CB  . ALA A 1 133 ? -19.93800 3.85100   -41.40700 1.000 37.45372  ? 133 ALA A CB  1 
ATOM   1026 N  N   . THR A 1 134 ? -19.00600 5.24000   -38.60500 1.000 28.76585  ? 134 THR A N   1 
ATOM   1027 C  CA  . THR A 1 134 ? -18.81600 5.05000   -37.16900 1.000 29.93499  ? 134 THR A CA  1 
ATOM   1028 C  C   . THR A 1 134 ? -19.71800 5.97800   -36.36100 1.000 28.40747  ? 134 THR A C   1 
ATOM   1029 O  O   . THR A 1 134 ? -20.27700 5.57700   -35.33700 1.000 29.24551  ? 134 THR A O   1 
ATOM   1030 C  CB  . THR A 1 134 ? -17.35900 5.27500   -36.79600 1.000 33.46749  ? 134 THR A CB  1 
ATOM   1031 O  OG1 . THR A 1 134 ? -16.54200 4.40300   -37.58900 1.000 40.84239  ? 134 THR A OG1 1 
ATOM   1032 C  CG2 . THR A 1 134 ? -17.14300 4.98200   -35.30000 1.000 32.06512  ? 134 THR A CG2 1 
ATOM   1033 N  N   . HIS A 1 135 ? -19.88800 7.21400   -36.82200 1.000 28.08969  ? 135 HIS A N   1 
ATOM   1034 C  CA  . HIS A 1 135 ? -20.76300 8.20100   -36.19900 1.000 28.16568  ? 135 HIS A CA  1 
ATOM   1035 C  C   . HIS A 1 135 ? -21.81700 8.60900   -37.22100 1.000 26.33557  ? 135 HIS A C   1 
ATOM   1036 O  O   . HIS A 1 135 ? -21.68000 9.64900   -37.88300 1.000 27.04020  ? 135 HIS A O   1 
ATOM   1037 C  CB  . HIS A 1 135 ? -19.95900 9.40200   -35.71200 1.000 27.22321  ? 135 HIS A CB  1 
ATOM   1038 C  CG  . HIS A 1 135 ? -18.99900 9.07500   -34.61600 1.000 29.78518  ? 135 HIS A CG  1 
ATOM   1039 N  ND1 . HIS A 1 135 ? -17.71400 8.63200   -34.85700 1.000 26.51803  ? 135 HIS A ND1 1 
ATOM   1040 C  CD2 . HIS A 1 135 ? -19.13500 9.13000   -33.26800 1.000 26.99387  ? 135 HIS A CD2 1 
ATOM   1041 C  CE1 . HIS A 1 135 ? -17.09600 8.43800   -33.70400 1.000 26.86399  ? 135 HIS A CE1 1 
ATOM   1042 N  NE2 . HIS A 1 135 ? -17.93500 8.73200   -32.72400 1.000 27.46256  ? 135 HIS A NE2 1 
ATOM   1043 N  N   . PRO A 1 136 ? -22.88000 7.81300   -37.37400 1.000 25.64492  ? 136 PRO A N   1 
ATOM   1044 C  CA  . PRO A 1 136 ? -23.84000 8.04400   -38.47300 1.000 30.22572  ? 136 PRO A CA  1 
ATOM   1045 C  C   . PRO A 1 136 ? -24.45400 9.44200   -38.50200 1.000 32.24223  ? 136 PRO A C   1 
ATOM   1046 O  O   . PRO A 1 136 ? -24.93900 9.86500   -39.56100 1.000 29.41086  ? 136 PRO A O   1 
ATOM   1047 C  CB  . PRO A 1 136 ? -24.92300 6.97800   -38.22100 1.000 31.49356  ? 136 PRO A CB  1 
ATOM   1048 C  CG  . PRO A 1 136 ? -24.23400 5.90700   -37.44100 1.000 30.37473  ? 136 PRO A CG  1 
ATOM   1049 C  CD  . PRO A 1 136 ? -23.17900 6.58700   -36.60900 1.000 28.46329  ? 136 PRO A CD  1 
ATOM   1050 N  N   . LEU A 1 137 ? -24.47700 10.15900  -37.37600 1.000 27.91592  ? 137 LEU A N   1 
ATOM   1051 C  CA  . LEU A 1 137 ? -25.03000 11.50800  -37.38300 1.000 30.75837  ? 137 LEU A CA  1 
ATOM   1052 C  C   . LEU A 1 137 ? -24.25500 12.42200  -38.32700 1.000 30.72648  ? 137 LEU A C   1 
ATOM   1053 O  O   . LEU A 1 137 ? -24.77800 13.46000  -38.73900 1.000 29.86521  ? 137 LEU A O   1 
ATOM   1054 C  CB  . LEU A 1 137 ? -25.05700 12.08900  -35.94700 1.000 27.08037  ? 137 LEU A CB  1 
ATOM   1055 C  CG  . LEU A 1 137 ? -23.72000 12.48200  -35.29400 1.000 29.26888  ? 137 LEU A CG  1 
ATOM   1056 C  CD1 . LEU A 1 137 ? -23.25700 13.88100  -35.73200 1.000 26.38762  ? 137 LEU A CD1 1 
ATOM   1057 C  CD2 . LEU A 1 137 ? -23.82200 12.42600  -33.77600 1.000 27.75187  ? 137 LEU A CD2 1 
ATOM   1058 N  N   . MET A 1 138 ? -23.01100 12.06700  -38.65400 1.000 30.48862  ? 138 MET A N   1 
ATOM   1059 C  CA  . MET A 1 138 ? -22.23200 12.84800  -39.61700 1.000 34.42719  ? 138 MET A CA  1 
ATOM   1060 C  C   . MET A 1 138 ? -22.90200 12.88600  -40.98400 1.000 32.51283  ? 138 MET A C   1 
ATOM   1061 O  O   . MET A 1 138 ? -22.71100 13.84000  -41.73500 1.000 37.07329  ? 138 MET A O   1 
ATOM   1062 C  CB  . MET A 1 138 ? -20.81500 12.27700  -39.74700 1.000 33.28250  ? 138 MET A CB  1 
ATOM   1063 C  CG  . MET A 1 138 ? -19.99600 12.33200  -38.43200 1.000 35.28071  ? 138 MET A CG  1 
ATOM   1064 S  SD  . MET A 1 138 ? -18.31700 11.64600  -38.60800 1.000 38.87147  ? 138 MET A SD  1 
ATOM   1065 C  CE  . MET A 1 138 ? -17.85100 12.39500  -40.18000 1.000 32.12489  ? 138 MET A CE  1 
ATOM   1066 N  N   . HIS A 1 139 ? -23.69800 11.87200  -41.32000 1.000 36.41588  ? 139 HIS A N   1 
ATOM   1067 C  CA  . HIS A 1 139 ? -24.32600 11.84400  -42.64100 1.000 39.87419  ? 139 HIS A CA  1 
ATOM   1068 C  C   . HIS A 1 139 ? -25.27400 13.02400  -42.83600 1.000 37.56022  ? 139 HIS A C   1 
ATOM   1069 O  O   . HIS A 1 139 ? -25.45300 13.48800  -43.96300 1.000 41.12228  ? 139 HIS A O   1 
ATOM   1070 C  CB  . HIS A 1 139 ? -25.05700 10.50800  -42.83000 1.000 37.18801  ? 139 HIS A CB  1 
ATOM   1071 C  CG  . HIS A 1 139 ? -25.76200 10.36400  -44.14500 1.000 40.94722  ? 139 HIS A CG  1 
ATOM   1072 N  ND1 . HIS A 1 139 ? -25.09100 10.19800  -45.33900 1.000 42.62661  ? 139 HIS A ND1 1 
ATOM   1073 C  CD2 . HIS A 1 139 ? -27.08200 10.33000  -44.44800 1.000 39.75455  ? 139 HIS A CD2 1 
ATOM   1074 C  CE1 . HIS A 1 139 ? -25.96800 10.08100  -46.32100 1.000 46.74081  ? 139 HIS A CE1 1 
ATOM   1075 N  NE2 . HIS A 1 139 ? -27.18400 10.15300  -45.80800 1.000 46.46988  ? 139 HIS A NE2 1 
ATOM   1076 N  N   . TYR A 1 140 ? -25.87000 13.53900  -41.75500 1.000 33.65288  ? 140 TYR A N   1 
ATOM   1077 C  CA  . TYR A 1 140 ? -26.89400 14.57200  -41.85400 1.000 34.38520  ? 140 TYR A CA  1 
ATOM   1078 C  C   . TYR A 1 140 ? -26.35400 15.98600  -41.65800 1.000 35.87892  ? 140 TYR A C   1 
ATOM   1079 O  O   . TYR A 1 140 ? -27.10100 16.94600  -41.85800 1.000 37.23386  ? 140 TYR A O   1 
ATOM   1080 C  CB  . TYR A 1 140 ? -28.00600 14.30200  -40.83500 1.000 32.70058  ? 140 TYR A CB  1 
ATOM   1081 C  CG  . TYR A 1 140 ? -28.54300 12.88100  -40.93900 1.000 35.91747  ? 140 TYR A CG  1 
ATOM   1082 C  CD1 . TYR A 1 140 ? -29.58600 12.55800  -41.81100 1.000 31.06164  ? 140 TYR A CD1 1 
ATOM   1083 C  CD2 . TYR A 1 140 ? -27.94800 11.88200  -40.17000 1.000 35.66879  ? 140 TYR A CD2 1 
ATOM   1084 C  CE1 . TYR A 1 140 ? -30.02200 11.25900  -41.87900 1.000 35.28198  ? 140 TYR A CE1 1 
ATOM   1085 C  CE2 . TYR A 1 140 ? -28.41400 10.59500  -40.26100 1.000 36.02143  ? 140 TYR A CE2 1 
ATOM   1086 C  CZ  . TYR A 1 140 ? -29.44600 10.25200  -41.11700 1.000 37.04201  ? 140 TYR A CZ  1 
ATOM   1087 O  OH  . TYR A 1 140 ? -29.85200 8.96800   -41.16600 1.000 44.07676  ? 140 TYR A OH  1 
ATOM   1088 N  N   . GLN A 1 141 ? -25.10700 16.14000  -41.26400 1.000 33.22145  ? 141 GLN A N   1 
ATOM   1089 C  CA  . GLN A 1 141 ? -24.53400 17.47200  -41.14200 1.000 34.74442  ? 141 GLN A CA  1 
ATOM   1090 C  C   . GLN A 1 141 ? -24.48200 18.15900  -42.50400 1.000 34.06596  ? 141 GLN A C   1 
ATOM   1091 O  O   . GLN A 1 141 ? -23.99900 17.56400  -43.46900 1.000 32.68531  ? 141 GLN A O   1 
ATOM   1092 C  CB  . GLN A 1 141 ? -23.13300 17.37400  -40.56200 1.000 33.95469  ? 141 GLN A CB  1 
ATOM   1093 C  CG  . GLN A 1 141 ? -23.11300 16.83600  -39.16700 1.000 37.00370  ? 141 GLN A CG  1 
ATOM   1094 C  CD  . GLN A 1 141 ? -23.09300 17.95300  -38.15200 1.000 40.64249  ? 141 GLN A CD  1 
ATOM   1095 O  OE1 . GLN A 1 141 ? -24.10600 18.24300  -37.47600 1.000 34.64638  ? 141 GLN A OE1 1 
ATOM   1096 N  NE2 . GLN A 1 141 ? -21.92800 18.59400  -38.02800 1.000 34.60098  ? 141 GLN A NE2 1 
ATOM   1097 N  N   . PRO A 1 142 ? -24.93500 19.40800  -42.60900 1.000 37.18363  ? 142 PRO A N   1 
ATOM   1098 C  CA  . PRO A 1 142 ? -24.76800 20.15800  -43.86200 1.000 33.51656  ? 142 PRO A CA  1 
ATOM   1099 C  C   . PRO A 1 142 ? -23.30400 20.27500  -44.24600 1.000 35.70313  ? 142 PRO A C   1 
ATOM   1100 O  O   . PRO A 1 142 ? -22.40800 20.21300  -43.39900 1.000 35.95448  ? 142 PRO A O   1 
ATOM   1101 C  CB  . PRO A 1 142 ? -25.35900 21.53800  -43.54000 1.000 35.93962  ? 142 PRO A CB  1 
ATOM   1102 C  CG  . PRO A 1 142 ? -26.13100 21.35700  -42.25100 1.000 33.51724  ? 142 PRO A CG  1 
ATOM   1103 C  CD  . PRO A 1 142 ? -25.50000 20.22700  -41.52200 1.000 33.18108  ? 142 PRO A CD  1 
ATOM   1104 N  N   . LEU A 1 143 ? -23.07300 20.44800  -45.54900 1.000 35.69294  ? 143 LEU A N   1 
ATOM   1105 C  CA  . LEU A 1 143 ? -21.72200 20.66500  -46.06000 1.000 36.15373  ? 143 LEU A CA  1 
ATOM   1106 C  C   . LEU A 1 143 ? -21.05800 21.86000  -45.38600 1.000 35.38476  ? 143 LEU A C   1 
ATOM   1107 O  O   . LEU A 1 143 ? -19.84900 21.84900  -45.13100 1.000 34.81573  ? 143 LEU A O   1 
ATOM   1108 C  CB  . LEU A 1 143 ? -21.77700 20.87100  -47.57900 1.000 37.59333  ? 143 LEU A CB  1 
ATOM   1109 C  CG  . LEU A 1 143 ? -20.53400 21.45800  -48.26000 1.000 41.05205  ? 143 LEU A CG  1 
ATOM   1110 C  CD1 . LEU A 1 143 ? -19.34000 20.50700  -48.16200 1.000 38.15372  ? 143 LEU A CD1 1 
ATOM   1111 C  CD2 . LEU A 1 143 ? -20.80100 21.82500  -49.71800 1.000 39.17543  ? 143 LEU A CD2 1 
ATOM   1112 N  N   . GLU A 1 144 ? -21.83900 22.90100  -45.09000 1.000 34.80385  ? 144 GLU A N   1 
ATOM   1113 C  CA  . GLU A 1 144 ? -21.29500 24.14400  -44.55500 1.000 35.51853  ? 144 GLU A CA  1 
ATOM   1114 C  C   . GLU A 1 144 ? -20.95800 24.07100  -43.07300 1.000 35.90675  ? 144 GLU A C   1 
ATOM   1115 O  O   . GLU A 1 144 ? -20.24000 24.94800  -42.57500 1.000 34.92645  ? 144 GLU A O   1 
ATOM   1116 C  CB  . GLU A 1 144 ? -22.28100 25.28600  -44.78400 1.000 37.56491  ? 144 GLU A CB  1 
ATOM   1117 C  CG  . GLU A 1 144 ? -22.54000 25.58100  -46.25300 1.000 36.63778  ? 144 GLU A CG  1 
ATOM   1118 C  CD  . GLU A 1 144 ? -23.58500 24.66300  -46.89900 1.000 38.84641  ? 144 GLU A CD  1 
ATOM   1119 O  OE1 . GLU A 1 144 ? -24.20300 23.83200  -46.18700 1.000 40.07263  ? 144 GLU A OE1 1 
ATOM   1120 O  OE2 . GLU A 1 144 ? -23.79500 24.79800  -48.13000 1.000 37.62353  ? 144 GLU A OE2 1 
ATOM   1121 N  N   . ALA A 1 145 ? -21.44700 23.05300  -42.36800 1.000 32.03936  ? 145 ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 145 ? -21.27700 22.98600  -40.92300 1.000 34.62843  ? 145 ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 145 ? -19.82100 22.66900  -40.55600 1.000 31.84599  ? 145 ALA A C   1 
ATOM   1124 O  O   . ALA A 1 145 ? -19.10100 22.02600  -41.32800 1.000 29.82326  ? 145 ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 145 ? -22.21300 21.92800  -40.32000 1.000 28.98861  ? 145 ALA A CB  1 
ATOM   1126 N  N   . PRO A 1 146 ? -19.37300 23.08700  -39.37000 1.000 31.91612  ? 146 PRO A N   1 
ATOM   1127 C  CA  . PRO A 1 146 ? -17.97400 22.83000  -38.96900 1.000 32.43651  ? 146 PRO A CA  1 
ATOM   1128 C  C   . PRO A 1 146 ? -17.63300 21.35700  -39.11000 1.000 30.83373  ? 146 PRO A C   1 
ATOM   1129 O  O   . PRO A 1 146 ? -18.37700 20.49300  -38.62500 1.000 29.75260  ? 146 PRO A O   1 
ATOM   1130 C  CB  . PRO A 1 146 ? -17.93900 23.26800  -37.49700 1.000 28.71169  ? 146 PRO A CB  1 
ATOM   1131 C  CG  . PRO A 1 146 ? -19.02600 24.29600  -37.37600 1.000 29.54154  ? 146 PRO A CG  1 
ATOM   1132 C  CD  . PRO A 1 146 ? -20.11700 23.84100  -38.33900 1.000 31.46423  ? 146 PRO A CD  1 
ATOM   1133 N  N   . PRO A 1 147 ? -16.54900 21.02400  -39.80600 1.000 31.89865  ? 147 PRO A N   1 
ATOM   1134 C  CA  . PRO A 1 147 ? -16.17300 19.60500  -39.91900 1.000 30.93095  ? 147 PRO A CA  1 
ATOM   1135 C  C   . PRO A 1 147 ? -15.83900 19.02900  -38.55400 1.000 31.73920  ? 147 PRO A C   1 
ATOM   1136 O  O   . PRO A 1 147 ? -15.28700 19.71700  -37.68700 1.000 29.90795  ? 147 PRO A O   1 
ATOM   1137 C  CB  . PRO A 1 147 ? -14.95400 19.61500  -40.85100 1.000 31.99265  ? 147 PRO A CB  1 
ATOM   1138 C  CG  . PRO A 1 147 ? -14.63100 21.07400  -41.12300 1.000 34.72586  ? 147 PRO A CG  1 
ATOM   1139 C  CD  . PRO A 1 147 ? -15.81300 21.89900  -40.73700 1.000 33.20475  ? 147 PRO A CD  1 
ATOM   1140 N  N   . VAL A 1 148 ? -16.22800 17.77100  -38.34800 1.000 29.70179  ? 148 VAL A N   1 
ATOM   1141 C  CA  . VAL A 1 148 ? -16.00700 17.07400  -37.08800 1.000 27.43556  ? 148 VAL A CA  1 
ATOM   1142 C  C   . VAL A 1 148 ? -15.11500 15.84800  -37.23700 1.000 30.91787  ? 148 VAL A C   1 
ATOM   1143 O  O   . VAL A 1 148 ? -14.91500 15.12800  -36.25000 1.000 28.56629  ? 148 VAL A O   1 
ATOM   1144 C  CB  . VAL A 1 148 ? -17.33700 16.67400  -36.41000 1.000 28.37551  ? 148 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A 1 148 ? -18.13100 17.89900  -35.96700 1.000 25.31400  ? 148 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A 1 148 ? -18.18300 15.75500  -37.32200 1.000 25.41916  ? 148 VAL A CG2 1 
ATOM   1147 N  N   . SER A 1 149 ? -14.56500 15.58100  -38.43100 1.000 27.45592  ? 149 SER A N   1 
ATOM   1148 C  CA  . SER A 1 149 ? -13.73500 14.40100  -38.63400 1.000 31.01225  ? 149 SER A CA  1 
ATOM   1149 C  C   . SER A 1 149 ? -12.65400 14.64100  -39.68700 1.000 30.17641  ? 149 SER A C   1 
ATOM   1150 O  O   . SER A 1 149 ? -12.89400 15.29400  -40.70200 1.000 29.76275  ? 149 SER A O   1 
ATOM   1151 C  CB  . SER A 1 149 ? -14.58000 13.19300  -39.05300 1.000 32.92661  ? 149 SER A CB  1 
ATOM   1152 O  OG  . SER A 1 149 ? -13.76800 12.02400  -39.07100 1.000 38.00652  ? 149 SER A OG  1 
ATOM   1153 N  N   . LEU A 1 150 ? -11.48100 14.06400  -39.45100 1.000 29.37627  ? 150 LEU A N   1 
ATOM   1154 C  CA  . LEU A 1 150 ? -10.36000 14.11400  -40.38800 1.000 33.61189  ? 150 LEU A CA  1 
ATOM   1155 C  C   . LEU A 1 150 ? -9.68200  12.75100  -40.44400 1.000 30.92046  ? 150 LEU A C   1 
ATOM   1156 O  O   . LEU A 1 150 ? -9.43800  12.13800  -39.40500 1.000 33.60706  ? 150 LEU A O   1 
ATOM   1157 C  CB  . LEU A 1 150 ? -9.33600  15.19200  -39.97600 1.000 31.61031  ? 150 LEU A CB  1 
ATOM   1158 C  CG  . LEU A 1 150 ? -8.12000  15.43400  -40.87900 1.000 35.06194  ? 150 LEU A CG  1 
ATOM   1159 C  CD1 . LEU A 1 150 ? -8.53500  16.10200  -42.19500 1.000 33.21615  ? 150 LEU A CD1 1 
ATOM   1160 C  CD2 . LEU A 1 150 ? -7.06400  16.25600  -40.13200 1.000 32.26282  ? 150 LEU A CD2 1 
ATOM   1161 N  N   . SER A 1 151 ? -9.36800  12.28200  -41.65100 1.000 33.25674  ? 151 SER A N   1 
ATOM   1162 C  CA  . SER A 1 151 ? -8.68000  11.00700  -41.84400 1.000 35.74916  ? 151 SER A CA  1 
ATOM   1163 C  C   . SER A 1 151 ? -7.20600  11.24900  -42.13100 1.000 35.19404  ? 151 SER A C   1 
ATOM   1164 O  O   . SER A 1 151 ? -6.86300  12.00500  -43.04700 1.000 31.08150  ? 151 SER A O   1 
ATOM   1165 C  CB  . SER A 1 151 ? -9.29300  10.20400  -42.99500 1.000 36.29439  ? 151 SER A CB  1 
ATOM   1166 O  OG  . SER A 1 151 ? -10.65000 9.90600   -42.74500 1.000 34.74249  ? 151 SER A OG  1 
ATOM   1167 N  N   . VAL A 1 152 ? -6.34600  10.58700  -41.36500 1.000 35.11189  ? 152 VAL A N   1 
ATOM   1168 C  CA  . VAL A 1 152 ? -4.90500  10.67100  -41.53100 1.000 36.29017  ? 152 VAL A CA  1 
ATOM   1169 C  C   . VAL A 1 152 ? -4.40500  9.26100   -41.84200 1.000 37.24300  ? 152 VAL A C   1 
ATOM   1170 O  O   . VAL A 1 152 ? -4.50300  8.35600   -41.00300 1.000 36.15227  ? 152 VAL A O   1 
ATOM   1171 C  CB  . VAL A 1 152 ? -4.23000  11.25200  -40.28200 1.000 37.19505  ? 152 VAL A CB  1 
ATOM   1172 C  CG1 . VAL A 1 152 ? -2.74900  11.43300  -40.51300 1.000 32.87123  ? 152 VAL A CG1 1 
ATOM   1173 C  CG2 . VAL A 1 152 ? -4.88800  12.58000  -39.91900 1.000 33.48415  ? 152 VAL A CG2 1 
ATOM   1174 N  N   . ILE A 1 153 ? -3.88100  9.06400   -43.04400 1.000 36.83346  ? 153 ILE A N   1 
ATOM   1175 C  CA  . ILE A 1 153 ? -3.56100  7.73200   -43.55100 1.000 36.71140  ? 153 ILE A CA  1 
ATOM   1176 C  C   . ILE A 1 153 ? -2.04600  7.61100   -43.68700 1.000 38.05671  ? 153 ILE A C   1 
ATOM   1177 O  O   . ILE A 1 153 ? -1.41500  8.37600   -44.42400 1.000 37.09883  ? 153 ILE A O   1 
ATOM   1178 C  CB  . ILE A 1 153 ? -4.26700  7.45200   -44.88300 1.000 36.87172  ? 153 ILE A CB  1 
ATOM   1179 C  CG1 . ILE A 1 153 ? -5.76700  7.25700   -44.64800 1.000 38.98140  ? 153 ILE A CG1 1 
ATOM   1180 C  CG2 . ILE A 1 153 ? -3.66700  6.22400   -45.57000 1.000 37.57057  ? 153 ILE A CG2 1 
ATOM   1181 C  CD1 . ILE A 1 153 ? -6.60300  8.37500   -45.14800 1.000 40.02005  ? 153 ILE A CD1 1 
ATOM   1182 N  N   . PHE A 1 154 ? -1.46600  6.65600   -42.96300 1.000 38.64085  ? 154 PHE A N   1 
ATOM   1183 C  CA  . PHE A 1 154 ? -0.02100  6.46200   -42.94500 1.000 39.93696  ? 154 PHE A CA  1 
ATOM   1184 C  C   . PHE A 1 154 ? 0.34000   5.21900   -43.74700 1.000 39.89608  ? 154 PHE A C   1 
ATOM   1185 O  O   . PHE A 1 154 ? 0.10200   4.09600   -43.27800 1.000 39.58024  ? 154 PHE A O   1 
ATOM   1186 C  CB  . PHE A 1 154 ? 0.49000   6.32900   -41.51100 1.000 39.31437  ? 154 PHE A CB  1 
ATOM   1187 C  CG  . PHE A 1 154 ? 0.27900   7.55400   -40.66100 1.000 38.70696  ? 154 PHE A CG  1 
ATOM   1188 C  CD1 . PHE A 1 154 ? 1.19400   8.59400   -40.68600 1.000 39.39312  ? 154 PHE A CD1 1 
ATOM   1189 C  CD2 . PHE A 1 154 ? -0.80600  7.64800   -39.81300 1.000 37.05091  ? 154 PHE A CD2 1 
ATOM   1190 C  CE1 . PHE A 1 154 ? 1.01900   9.70900   -39.89400 1.000 37.56294  ? 154 PHE A CE1 1 
ATOM   1191 C  CE2 . PHE A 1 154 ? -0.98500  8.76300   -38.99900 1.000 35.76926  ? 154 PHE A CE2 1 
ATOM   1192 C  CZ  . PHE A 1 154 ? -0.07500  9.79200   -39.04400 1.000 38.40155  ? 154 PHE A CZ  1 
ATOM   1193 N  N   . PRO A 1 155 ? 0.89900   5.35700   -44.94700 1.000 41.37840  ? 155 PRO A N   1 
ATOM   1194 C  CA  . PRO A 1 155 ? 1.43300   4.17800   -45.64900 1.000 45.57377  ? 155 PRO A CA  1 
ATOM   1195 C  C   . PRO A 1 155 ? 2.63900   3.63600   -44.89800 1.000 45.00983  ? 155 PRO A C   1 
ATOM   1196 O  O   . PRO A 1 155 ? 3.56900   4.37700   -44.58100 1.000 44.12123  ? 155 PRO A O   1 
ATOM   1197 C  CB  . PRO A 1 155 ? 1.83100   4.73100   -47.02200 1.000 40.84767  ? 155 PRO A CB  1 
ATOM   1198 C  CG  . PRO A 1 155 ? 2.16000   6.17700   -46.73900 1.000 43.30130  ? 155 PRO A CG  1 
ATOM   1199 C  CD  . PRO A 1 155 ? 1.17700   6.61200   -45.66200 1.000 38.02102  ? 155 PRO A CD  1 
ATOM   1200 N  N   . LEU A 1 156 ? 2.61900   2.34300   -44.59100 1.000 44.87389  ? 156 LEU A N   1 
ATOM   1201 C  CA  . LEU A 1 156 ? 3.79200   1.73300   -43.97900 1.000 47.59398  ? 156 LEU A CA  1 
ATOM   1202 C  C   . LEU A 1 156 ? 4.57300   0.83100   -44.92400 1.000 50.13044  ? 156 LEU A C   1 
ATOM   1203 O  O   . LEU A 1 156 ? 5.72100   0.50300   -44.62200 1.000 46.48877  ? 156 LEU A O   1 
ATOM   1204 C  CB  . LEU A 1 156 ? 3.40000   0.94400   -42.72700 1.000 46.10408  ? 156 LEU A CB  1 
ATOM   1205 C  CG  . LEU A 1 156 ? 2.98600   1.82900   -41.55500 1.000 48.82110  ? 156 LEU A CG  1 
ATOM   1206 C  CD1 . LEU A 1 156 ? 2.48600   0.93100   -40.47600 1.000 48.01709  ? 156 LEU A CD1 1 
ATOM   1207 C  CD2 . LEU A 1 156 ? 4.15400   2.66800   -41.04900 1.000 48.09752  ? 156 LEU A CD2 1 
ATOM   1208 N  N   . THR A 1 157 ? 3.97600   0.41000   -46.03200 1.000 48.03344  ? 157 THR A N   1 
ATOM   1209 C  CA  . THR A 1 157 ? 4.69600   -0.03100  -47.21600 1.000 50.49382  ? 157 THR A CA  1 
ATOM   1210 C  C   . THR A 1 157 ? 4.45700   0.99300   -48.32300 1.000 53.12189  ? 157 THR A C   1 
ATOM   1211 O  O   . THR A 1 157 ? 3.69500   1.95800   -48.15800 1.000 48.84922  ? 157 THR A O   1 
ATOM   1212 C  CB  . THR A 1 157 ? 4.25200   -1.43100  -47.66000 1.000 54.19354  ? 157 THR A CB  1 
ATOM   1213 O  OG1 . THR A 1 157 ? 2.89000   -1.39200  -48.09900 1.000 56.19871  ? 157 THR A OG1 1 
ATOM   1214 C  CG2 . THR A 1 157 ? 4.39000   -2.44500  -46.52400 1.000 52.23161  ? 157 THR A CG2 1 
ATOM   1215 N  N   . GLU A 1 158 ? 5.10800   0.78400   -49.46200 1.000 49.09826  ? 158 GLU A N   1 
ATOM   1216 C  CA  . GLU A 1 158 ? 4.84500   1.64700   -50.60300 1.000 53.50523  ? 158 GLU A CA  1 
ATOM   1217 C  C   . GLU A 1 158 ? 3.39900   1.47900   -51.07000 1.000 53.51853  ? 158 GLU A C   1 
ATOM   1218 O  O   . GLU A 1 158 ? 2.87900   0.36200   -51.14200 1.000 54.57381  ? 158 GLU A O   1 
ATOM   1219 C  CB  . GLU A 1 158 ? 5.82800   1.34800   -51.74600 1.000 54.63498  ? 158 GLU A CB  1 
ATOM   1220 C  CG  . GLU A 1 158 ? 6.05800   -0.12900  -52.05600 1.000 60.92814  ? 158 GLU A CG  1 
ATOM   1221 C  CD  . GLU A 1 158 ? 7.02600   -0.33900  -53.23100 1.000 72.52454  ? 158 GLU A CD  1 
ATOM   1222 O  OE1 . GLU A 1 158 ? 7.41300   0.66600   -53.88000 1.000 74.19020  ? 158 GLU A OE1 1 
ATOM   1223 O  OE2 . GLU A 1 158 ? 7.40100   -1.50400  -53.50800 1.000 71.05671  ? 158 GLU A OE2 1 
ATOM   1224 N  N   . PHE A 1 159 ? 2.73200   2.59600   -51.33400 1.000 49.57073  ? 159 PHE A N   1 
ATOM   1225 C  CA  . PHE A 1 159 ? 1.49500   2.58700   -52.10200 1.000 51.65269  ? 159 PHE A CA  1 
ATOM   1226 C  C   . PHE A 1 159 ? 1.84500   2.78700   -53.57200 1.000 54.31274  ? 159 PHE A C   1 
ATOM   1227 O  O   . PHE A 1 159 ? 2.44200   3.80900   -53.93700 1.000 53.48535  ? 159 PHE A O   1 
ATOM   1228 C  CB  . PHE A 1 159 ? 0.53200   3.68300   -51.64500 1.000 48.29908  ? 159 PHE A CB  1 
ATOM   1229 C  CG  . PHE A 1 159 ? -0.19900  3.37000   -50.36700 1.000 49.76463  ? 159 PHE A CG  1 
ATOM   1230 C  CD1 . PHE A 1 159 ? 0.26700   2.39700   -49.49800 1.000 49.71282  ? 159 PHE A CD1 1 
ATOM   1231 C  CD2 . PHE A 1 159 ? -1.35900  4.05400   -50.04300 1.000 44.59242  ? 159 PHE A CD2 1 
ATOM   1232 C  CE1 . PHE A 1 159 ? -0.40000  2.12100   -48.32400 1.000 50.47647  ? 159 PHE A CE1 1 
ATOM   1233 C  CE2 . PHE A 1 159 ? -2.04000  3.78300   -48.86900 1.000 48.08635  ? 159 PHE A CE2 1 
ATOM   1234 C  CZ  . PHE A 1 159 ? -1.56300  2.81400   -48.00700 1.000 49.75424  ? 159 PHE A CZ  1 
ATOM   1235 N  N   . THR A 1 160 ? 1.48600   1.81800   -54.41100 1.000 57.49879  ? 160 THR A N   1 
ATOM   1236 C  CA  . THR A 1 160 ? 1.70300   1.91100   -55.84700 1.000 58.32446  ? 160 THR A CA  1 
ATOM   1237 C  C   . THR A 1 160 ? 0.38000   1.68900   -56.56600 1.000 61.67193  ? 160 THR A C   1 
ATOM   1238 O  O   . THR A 1 160 ? -0.63600  1.33000   -55.96100 1.000 56.74394  ? 160 THR A O   1 
ATOM   1239 C  CB  . THR A 1 160 ? 2.74200   0.89200   -56.34400 1.000 62.13222  ? 160 THR A CB  1 
ATOM   1240 O  OG1 . THR A 1 160 ? 2.24600   -0.44100  -56.15000 1.000 60.97208  ? 160 THR A OG1 1 
ATOM   1241 C  CG2 . THR A 1 160 ? 4.07000   1.06200   -55.61000 1.000 62.03737  ? 160 THR A CG2 1 
ATOM   1242 N  N   . GLU A 1 161 ? 0.40000   1.89900   -57.88200 1.000 62.74527  ? 161 GLU A N   1 
ATOM   1243 C  CA  . GLU A 1 161 ? -0.78800  1.61800   -58.67600 1.000 66.32028  ? 161 GLU A CA  1 
ATOM   1244 C  C   . GLU A 1 161 ? -1.04200  0.12200   -58.79100 1.000 67.90895  ? 161 GLU A C   1 
ATOM   1245 O  O   . GLU A 1 161 ? -2.18000  -0.28800  -59.03900 1.000 73.79163  ? 161 GLU A O   1 
ATOM   1246 C  CB  . GLU A 1 161 ? -0.64400  2.26200   -60.05400 1.000 73.99092  ? 161 GLU A CB  1 
ATOM   1247 C  CG  . GLU A 1 161 ? -0.07400  3.67800   -59.98400 1.000 75.92158  ? 161 GLU A CG  1 
ATOM   1248 C  CD  . GLU A 1 161 ? -0.16000  4.42800   -61.29800 1.000 85.43875  ? 161 GLU A CD  1 
ATOM   1249 O  OE1 . GLU A 1 161 ? -1.02500  4.07600   -62.13200 1.000 84.78686  ? 161 GLU A OE1 1 
ATOM   1250 O  OE2 . GLU A 1 161 ? 0.64500   5.36900   -61.49100 1.000 89.10364  ? 161 GLU A OE2 1 
ATOM   1251 N  N   . GLU A 1 162 ? -0.00700  -0.69400  -58.59500 1.000 69.94868  ? 162 GLU A N   1 
ATOM   1252 C  CA  . GLU A 1 162 ? -0.16400  -2.14200  -58.58800 1.000 68.84792  ? 162 GLU A CA  1 
ATOM   1253 C  C   . GLU A 1 162 ? -0.81000  -2.63000  -57.29500 1.000 66.86061  ? 162 GLU A C   1 
ATOM   1254 O  O   . GLU A 1 162 ? -1.77100  -3.40600  -57.33200 1.000 66.80942  ? 162 GLU A O   1 
ATOM   1255 C  CB  . GLU A 1 162 ? 1.19700   -2.81200  -58.78800 1.000 71.31006  ? 162 GLU A CB  1 
ATOM   1256 C  CG  . GLU A 1 162 ? 1.94500   -2.34100  -60.02000 1.000 79.20415  ? 162 GLU A CG  1 
ATOM   1257 C  CD  . GLU A 1 162 ? 3.40200   -2.01400  -59.73300 1.000 84.96741  ? 162 GLU A CD  1 
ATOM   1258 O  OE1 . GLU A 1 162 ? 3.66500   -1.08700  -58.93000 1.000 78.58775  ? 162 GLU A OE1 1 
ATOM   1259 O  OE2 . GLU A 1 162 ? 4.28200   -2.69200  -60.31200 1.000 93.32158  ? 162 GLU A OE2 1 
ATOM   1260 N  N   . ASN A 1 163 ? -0.30000  -2.19500  -56.13900 1.000 63.64589  ? 163 ASN A N   1 
ATOM   1261 C  CA  . ASN A 1 163 ? -0.70900  -2.79900  -54.87500 1.000 61.01687  ? 163 ASN A CA  1 
ATOM   1262 C  C   . ASN A 1 163 ? -1.87000  -2.07800  -54.19900 1.000 60.66132  ? 163 ASN A C   1 
ATOM   1263 O  O   . ASN A 1 163 ? -2.21400  -2.42300  -53.06300 1.000 57.46992  ? 163 ASN A O   1 
ATOM   1264 C  CB  . ASN A 1 163 ? 0.48400   -2.92000  -53.91100 1.000 60.54193  ? 163 ASN A CB  1 
ATOM   1265 C  CG  . ASN A 1 163 ? 1.02700   -1.57800  -53.43000 1.000 60.13631  ? 163 ASN A CG  1 
ATOM   1266 O  OD1 . ASN A 1 163 ? 0.37900   -0.52900  -53.52700 1.000 55.87651  ? 163 ASN A OD1 1 
ATOM   1267 N  ND2 . ASN A 1 163 ? 2.23400   -1.61900  -52.88300 1.000 61.34503  ? 163 ASN A ND2 1 
ATOM   1268 N  N   . GLY A 1 164 ? -2.48700  -1.10500  -54.86000 1.000 61.11536  ? 164 GLY A N   1 
ATOM   1269 C  CA  . GLY A 1 164 ? -3.74800  -0.58600  -54.36700 1.000 54.75674  ? 164 GLY A CA  1 
ATOM   1270 C  C   . GLY A 1 164 ? -3.69100  0.72000   -53.60000 1.000 57.20213  ? 164 GLY A C   1 
ATOM   1271 O  O   . GLY A 1 164 ? -4.38900  0.88300   -52.58900 1.000 47.55351  ? 164 GLY A O   1 
ATOM   1272 N  N   . ALA A 1 165 ? -2.87200  1.66100   -54.07400 1.000 52.25837  ? 165 ALA A N   1 
ATOM   1273 C  CA  . ALA A 1 165 ? -2.87700  3.00300   -53.50500 1.000 52.61869  ? 165 ALA A CA  1 
ATOM   1274 C  C   . ALA A 1 165 ? -4.30000  3.55100   -53.44100 1.000 45.91599  ? 165 ALA A C   1 
ATOM   1275 O  O   . ALA A 1 165 ? -5.10500  3.35700   -54.35700 1.000 40.91299  ? 165 ALA A O   1 
ATOM   1276 C  CB  . ALA A 1 165 ? -1.98500  3.94000   -54.32700 1.000 49.99503  ? 165 ALA A CB  1 
ATOM   1277 N  N   . THR A 1 166 ? -4.59800  4.23700   -52.34200 1.000 43.18128  ? 166 THR A N   1 
ATOM   1278 C  CA  . THR A 1 166 ? -5.94600  4.73700   -52.09200 1.000 40.35423  ? 166 THR A CA  1 
ATOM   1279 C  C   . THR A 1 166 ? -6.43300  5.60800   -53.23800 1.000 41.40010  ? 166 THR A C   1 
ATOM   1280 O  O   . THR A 1 166 ? -5.68300  6.42000   -53.79400 1.000 43.67655  ? 166 THR A O   1 
ATOM   1281 C  CB  . THR A 1 166 ? -5.97500  5.54500   -50.79900 1.000 39.73968  ? 166 THR A CB  1 
ATOM   1282 O  OG1 . THR A 1 166 ? -5.12900  4.91000   -49.82700 1.000 42.63825  ? 166 THR A OG1 1 
ATOM   1283 C  CG2 . THR A 1 166 ? -7.39100  5.64100   -50.27500 1.000 35.47934  ? 166 THR A CG2 1 
ATOM   1284 N  N   . GLU A 1 167 ? -7.69600  5.42500   -53.59600 1.000 40.26413  ? 167 GLU A N   1 
ATOM   1285 C  CA  . GLU A 1 167 ? -8.33900  6.17700   -54.66000 1.000 38.47065  ? 167 GLU A CA  1 
ATOM   1286 C  C   . GLU A 1 167 ? -9.18600  7.27100   -54.02500 1.000 35.75862  ? 167 GLU A C   1 
ATOM   1287 O  O   . GLU A 1 167 ? -10.01200 6.99100   -53.15700 1.000 36.46787  ? 167 GLU A O   1 
ATOM   1288 C  CB  . GLU A 1 167 ? -9.19500  5.25300   -55.52400 1.000 35.33481  ? 167 GLU A CB  1 
ATOM   1289 C  CG  . GLU A 1 167 ? -8.39600  4.11400   -56.15500 1.000 41.48915  ? 167 GLU A CG  1 
ATOM   1290 C  CD  . GLU A 1 167 ? -9.23400  2.87600   -56.46500 1.000 48.61900  ? 167 GLU A CD  1 
ATOM   1291 O  OE1 . GLU A 1 167 ? -10.48200 2.96300   -56.51900 1.000 50.41670  ? 167 GLU A OE1 1 
ATOM   1292 O  OE2 . GLU A 1 167 ? -8.63400  1.79400   -56.65100 1.000 62.03796  ? 167 GLU A OE2 1 
ATOM   1293 N  N   . VAL A 1 168 ? -8.96600  8.50900   -54.45000 1.000 35.89205  ? 168 VAL A N   1 
ATOM   1294 C  CA  . VAL A 1 168 ? -9.62700  9.68300   -53.89500 1.000 36.04061  ? 168 VAL A CA  1 
ATOM   1295 C  C   . VAL A 1 168 ? -10.23200 10.47100  -55.04900 1.000 38.29505  ? 168 VAL A C   1 
ATOM   1296 O  O   . VAL A 1 168 ? -9.57100  10.68300  -56.07300 1.000 37.81892  ? 168 VAL A O   1 
ATOM   1297 C  CB  . VAL A 1 168 ? -8.64000  10.56000  -53.10600 1.000 38.03608  ? 168 VAL A CB  1 
ATOM   1298 C  CG1 . VAL A 1 168 ? -9.34000  11.78200  -52.54300 1.000 35.17204  ? 168 VAL A CG1 1 
ATOM   1299 C  CG2 . VAL A 1 168 ? -7.94300  9.75300   -52.01600 1.000 38.45373  ? 168 VAL A CG2 1 
ATOM   1300 N  N   . ILE A 1 169 ? -11.48400 10.89000  -54.89500 1.000 38.51997  ? 169 ILE A N   1 
ATOM   1301 C  CA  . ILE A 1 169 ? -12.15600 11.72800  -55.88300 1.000 35.79492  ? 169 ILE A CA  1 
ATOM   1302 C  C   . ILE A 1 169 ? -12.09500 13.15900  -55.36000 1.000 39.06095  ? 169 ILE A C   1 
ATOM   1303 O  O   . ILE A 1 169 ? -12.77100 13.50700  -54.38200 1.000 37.45231  ? 169 ILE A O   1 
ATOM   1304 C  CB  . ILE A 1 169 ? -13.60000 11.27100  -56.14400 1.000 32.56431  ? 169 ILE A CB  1 
ATOM   1305 C  CG1 . ILE A 1 169 ? -13.62500 9.81400   -56.64800 1.000 37.36871  ? 169 ILE A CG1 1 
ATOM   1306 C  CG2 . ILE A 1 169 ? -14.24500 12.15900  -57.18600 1.000 37.08609  ? 169 ILE A CG2 1 
ATOM   1307 C  CD1 . ILE A 1 169 ? -15.01800 9.16400   -56.70400 1.000 30.38008  ? 169 ILE A CD1 1 
ATOM   1308 N  N   . LEU A 1 170 ? -11.28000 13.98700  -56.01200 1.000 37.01862  ? 170 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 170 ? -11.03800 15.34600  -55.54900 1.000 41.87123  ? 170 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 170 ? -12.29600 16.19500  -55.67600 1.000 38.70097  ? 170 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 170 ? -13.02700 16.10600  -56.66200 1.000 38.66201  ? 170 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 170 ? -9.89200  15.97600  -56.35200 1.000 43.30098  ? 170 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 170 ? -8.57800  15.18700  -56.33600 1.000 43.84685  ? 170 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 170 ? -7.43700  15.96900  -56.98500 1.000 45.06555  ? 170 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 170 ? -8.22100  14.76800  -54.90100 1.000 38.38823  ? 170 LEU A CD2 1 
ATOM   1316 N  N   . GLY A 1 171 ? -12.54300 17.03400  -54.67500 1.000 39.99279  ? 171 GLY A N   1 
ATOM   1317 C  CA  . GLY A 1 171 ? -13.72000 17.88000  -54.67500 1.000 42.61948  ? 171 GLY A CA  1 
ATOM   1318 C  C   . GLY A 1 171 ? -15.03200 17.18500  -54.36200 1.000 40.36215  ? 171 GLY A C   1 
ATOM   1319 O  O   . GLY A 1 171 ? -16.07500 17.85100  -54.32600 1.000 40.71023  ? 171 GLY A O   1 
ATOM   1320 N  N   . SER A 1 172 ? -15.01800 15.87700  -54.12200 1.000 36.51048  ? 172 SER A N   1 
ATOM   1321 C  CA  . SER A 1 172 ? -16.25400 15.13800  -53.91800 1.000 35.98228  ? 172 SER A CA  1 
ATOM   1322 C  C   . SER A 1 172 ? -16.90000 15.40900  -52.56500 1.000 37.22211  ? 172 SER A C   1 
ATOM   1323 O  O   . SER A 1 172 ? -18.04400 14.99800  -52.36200 1.000 36.02520  ? 172 SER A O   1 
ATOM   1324 C  CB  . SER A 1 172 ? -15.99100 13.63500  -54.09000 1.000 34.16419  ? 172 SER A CB  1 
ATOM   1325 O  OG  . SER A 1 172 ? -15.05500 13.18600  -53.12800 1.000 32.72622  ? 172 SER A OG  1 
ATOM   1326 N  N   . HIS A 1 173 ? -16.21700 16.08100  -51.63200 1.000 35.70800  ? 173 HIS A N   1 
ATOM   1327 C  CA  . HIS A 1 173 ? -16.89700 16.46500  -50.40100 1.000 38.33085  ? 173 HIS A CA  1 
ATOM   1328 C  C   . HIS A 1 173 ? -18.03900 17.43600  -50.66600 1.000 39.71580  ? 173 HIS A C   1 
ATOM   1329 O  O   . HIS A 1 173 ? -18.95400 17.54100  -49.84100 1.000 40.73868  ? 173 HIS A O   1 
ATOM   1330 C  CB  . HIS A 1 173 ? -15.91100 17.06800  -49.39100 1.000 39.01392  ? 173 HIS A CB  1 
ATOM   1331 C  CG  . HIS A 1 173 ? -15.15200 18.25600  -49.90600 1.000 43.19561  ? 173 HIS A CG  1 
ATOM   1332 N  ND1 . HIS A 1 173 ? -14.20200 18.16100  -50.90000 1.000 40.12411  ? 173 HIS A ND1 1 
ATOM   1333 C  CD2 . HIS A 1 173 ? -15.18000 19.56000  -49.53500 1.000 42.90482  ? 173 HIS A CD2 1 
ATOM   1334 C  CE1 . HIS A 1 173 ? -13.67800 19.35400  -51.12400 1.000 43.29849  ? 173 HIS A CE1 1 
ATOM   1335 N  NE2 . HIS A 1 173 ? -14.25500 20.22100  -50.31000 1.000 47.16882  ? 173 HIS A NE2 1 
ATOM   1336 N  N   . ARG A 1 174 ? -18.02100 18.12100  -51.80800 1.000 40.42859  ? 174 ARG A N   1 
ATOM   1337 C  CA  . ARG A 1 174 ? -19.09800 19.01800  -52.20400 1.000 41.37308  ? 174 ARG A CA  1 
ATOM   1338 C  C   . ARG A 1 174 ? -20.25000 18.30700  -52.92200 1.000 39.36608  ? 174 ARG A C   1 
ATOM   1339 O  O   . ARG A 1 174 ? -21.23800 18.96000  -53.26000 1.000 40.29968  ? 174 ARG A O   1 
ATOM   1340 C  CB  . ARG A 1 174 ? -18.52600 20.14900  -53.07800 1.000 43.62917  ? 174 ARG A CB  1 
ATOM   1341 C  CG  . ARG A 1 174 ? -17.46000 20.98500  -52.34800 1.000 45.38489  ? 174 ARG A CG  1 
ATOM   1342 C  CD  . ARG A 1 174 ? -16.97500 22.19200  -53.16400 1.000 51.55712  ? 174 ARG A CD  1 
ATOM   1343 N  NE  . ARG A 1 174 ? -16.13200 21.77700  -54.28200 1.000 57.38540  ? 174 ARG A NE  1 
ATOM   1344 C  CZ  . ARG A 1 174 ? -14.80400 21.73700  -54.25700 1.000 54.84418  ? 174 ARG A CZ  1 
ATOM   1345 N  NH1 . ARG A 1 174 ? -14.11800 22.13800  -53.19600 1.000 51.31851  ? 174 ARG A NH1 1 
ATOM   1346 N  NH2 . ARG A 1 174 ? -14.14700 21.28400  -55.32400 1.000 56.84035  ? 174 ARG A NH2 1 
ATOM   1347 N  N   . TRP A 1 175 ? -20.17000 16.99600  -53.14900 1.000 41.09787  ? 175 TRP A N   1 
ATOM   1348 C  CA  . TRP A 1 175 ? -21.29600 16.27400  -53.73600 1.000 41.00935  ? 175 TRP A CA  1 
ATOM   1349 C  C   . TRP A 1 175 ? -22.40600 16.06900  -52.71100 1.000 41.91237  ? 175 TRP A C   1 
ATOM   1350 O  O   . TRP A 1 175 ? -22.15900 15.89800  -51.51400 1.000 38.73006  ? 175 TRP A O   1 
ATOM   1351 C  CB  . TRP A 1 175 ? -20.88400 14.89500  -54.25900 1.000 38.79208  ? 175 TRP A CB  1 
ATOM   1352 C  CG  . TRP A 1 175 ? -19.89500 14.89300  -55.34600 1.000 36.87092  ? 175 TRP A CG  1 
ATOM   1353 C  CD1 . TRP A 1 175 ? -19.36200 15.97900  -55.97700 1.000 40.13002  ? 175 TRP A CD1 1 
ATOM   1354 C  CD2 . TRP A 1 175 ? -19.29100 13.74400  -55.93800 1.000 34.76144  ? 175 TRP A CD2 1 
ATOM   1355 N  NE1 . TRP A 1 175 ? -18.46400 15.57700  -56.93500 1.000 40.10012  ? 175 TRP A NE1 1 
ATOM   1356 C  CE2 . TRP A 1 175 ? -18.39700 14.20700  -56.93100 1.000 40.35193  ? 175 TRP A CE2 1 
ATOM   1357 C  CE3 . TRP A 1 175 ? -19.41400 12.36600  -55.72300 1.000 34.82230  ? 175 TRP A CE3 1 
ATOM   1358 C  CZ2 . TRP A 1 175 ? -17.63700 13.34200  -57.71400 1.000 33.26929  ? 175 TRP A CZ2 1 
ATOM   1359 C  CZ3 . TRP A 1 175 ? -18.65500 11.51000  -56.48100 1.000 35.42040  ? 175 TRP A CZ3 1 
ATOM   1360 C  CH2 . TRP A 1 175 ? -17.78200 11.99800  -57.48300 1.000 35.96727  ? 175 TRP A CH2 1 
ATOM   1361 N  N   . THR A 1 176 ? -23.64200 16.04500  -53.20800 1.000 42.96764  ? 176 THR A N   1 
ATOM   1362 C  CA  . THR A 1 176 ? -24.78000 15.77600  -52.34100 1.000 44.75489  ? 176 THR A CA  1 
ATOM   1363 C  C   . THR A 1 176 ? -24.81800 14.31200  -51.92200 1.000 44.61248  ? 176 THR A C   1 
ATOM   1364 O  O   . THR A 1 176 ? -25.11700 14.00100  -50.76400 1.000 43.92668  ? 176 THR A O   1 
ATOM   1365 C  CB  . THR A 1 176 ? -26.07000 16.18200  -53.04500 1.000 48.11312  ? 176 THR A CB  1 
ATOM   1366 O  OG1 . THR A 1 176 ? -26.08700 17.60600  -53.20200 1.000 50.13477  ? 176 THR A OG1 1 
ATOM   1367 C  CG2 . THR A 1 176 ? -27.27500 15.75400  -52.23900 1.000 50.77104  ? 176 THR A CG2 1 
ATOM   1368 N  N   . GLU A 1 177 ? -24.49400 13.39600  -52.82900 1.000 43.59228  ? 177 GLU A N   1 
ATOM   1369 C  CA  . GLU A 1 177 ? -24.42300 11.98700  -52.46500 1.000 45.09187  ? 177 GLU A CA  1 
ATOM   1370 C  C   . GLU A 1 177 ? -23.21300 11.33900  -53.12000 1.000 42.94308  ? 177 GLU A C   1 
ATOM   1371 O  O   . GLU A 1 177 ? -22.58200 11.90100  -54.02100 1.000 40.82691  ? 177 GLU A O   1 
ATOM   1372 C  CB  . GLU A 1 177 ? -25.70400 11.24200  -52.84200 1.000 47.56344  ? 177 GLU A CB  1 
ATOM   1373 C  CG  . GLU A 1 177 ? -26.34100 11.74700  -54.10600 1.000 54.38993  ? 177 GLU A CG  1 
ATOM   1374 C  CD  . GLU A 1 177 ? -27.81400 11.40700  -54.18500 1.000 70.61822  ? 177 GLU A CD  1 
ATOM   1375 O  OE1 . GLU A 1 177 ? -28.20600 10.33600  -53.66900 1.000 74.18664  ? 177 GLU A OE1 1 
ATOM   1376 O  OE2 . GLU A 1 177 ? -28.58100 12.21600  -54.75800 1.000 77.70651  ? 177 GLU A OE2 1 
ATOM   1377 N  N   . VAL A 1 178 ? -22.88200 10.14400  -52.63300 1.000 38.98743  ? 178 VAL A N   1 
ATOM   1378 C  CA  . VAL A 1 178 ? -21.78900 9.38900   -53.22800 1.000 39.98886  ? 178 VAL A CA  1 
ATOM   1379 C  C   . VAL A 1 178 ? -22.09900 9.07700   -54.68900 1.000 40.91489  ? 178 VAL A C   1 
ATOM   1380 O  O   . VAL A 1 178 ? -21.25200 9.26600   -55.57100 1.000 37.32014  ? 178 VAL A O   1 
ATOM   1381 C  CB  . VAL A 1 178 ? -21.51400 8.12100   -52.40700 1.000 35.42426  ? 178 VAL A CB  1 
ATOM   1382 C  CG1 . VAL A 1 178 ? -20.50700 7.24300   -53.11900 1.000 38.54899  ? 178 VAL A CG1 1 
ATOM   1383 C  CG2 . VAL A 1 178 ? -20.98700 8.50200   -51.03300 1.000 39.13339  ? 178 VAL A CG2 1 
ATOM   1384 N  N   . GLY A 1 179 ? -23.32900 8.64400   -54.97600 1.000 39.12504  ? 179 GLY A N   1 
ATOM   1385 C  CA  . GLY A 1 179 ? -23.64000 8.31000   -56.35600 1.000 37.18230  ? 179 GLY A CA  1 
ATOM   1386 C  C   . GLY A 1 179 ? -22.95100 7.01400   -56.75200 1.000 36.39883  ? 179 GLY A C   1 
ATOM   1387 O  O   . GLY A 1 179 ? -22.61400 6.17800   -55.91500 1.000 37.91555  ? 179 GLY A O   1 
ATOM   1388 N  N   . THR A 1 180 ? -22.71000 6.86300   -58.05300 1.000 36.07927  ? 180 THR A N   1 
ATOM   1389 C  CA  . THR A 1 180 ? -22.07700 5.67200   -58.61900 1.000 37.48562  ? 180 THR A CA  1 
ATOM   1390 C  C   . THR A 1 180 ? -20.82100 6.06800   -59.40000 1.000 36.61086  ? 180 THR A C   1 
ATOM   1391 O  O   . THR A 1 180 ? -20.77500 5.92800   -60.62600 1.000 36.17910  ? 180 THR A O   1 
ATOM   1392 C  CB  . THR A 1 180 ? -23.05500 4.93000   -59.52700 1.000 37.11175  ? 180 THR A CB  1 
ATOM   1393 O  OG1 . THR A 1 180 ? -23.60200 5.84900   -60.48100 1.000 39.40279  ? 180 THR A OG1 1 
ATOM   1394 C  CG2 . THR A 1 180 ? -24.18100 4.30700   -58.72400 1.000 33.34122  ? 180 THR A CG2 1 
ATOM   1395 N  N   . PRO A 1 181 ? -19.79000 6.57300   -58.72100 1.000 33.57287  ? 181 PRO A N   1 
ATOM   1396 C  CA  . PRO A 1 181 ? -18.64000 7.12700   -59.45000 1.000 37.33605  ? 181 PRO A CA  1 
ATOM   1397 C  C   . PRO A 1 181 ? -17.77700 6.04800   -60.08000 1.000 35.78890  ? 181 PRO A C   1 
ATOM   1398 O  O   . PRO A 1 181 ? -17.60300 4.95600   -59.52200 1.000 35.06833  ? 181 PRO A O   1 
ATOM   1399 C  CB  . PRO A 1 181 ? -17.86600 7.88700   -58.36500 1.000 34.17538  ? 181 PRO A CB  1 
ATOM   1400 C  CG  . PRO A 1 181 ? -18.28200 7.22500   -57.07500 1.000 35.74689  ? 181 PRO A CG  1 
ATOM   1401 C  CD  . PRO A 1 181 ? -19.69100 6.80200   -57.26800 1.000 36.70472  ? 181 PRO A CD  1 
ATOM   1402 N  N   . GLU A 1 182 ? -17.23600 6.37400   -61.25400 1.000 34.10233  ? 182 GLU A N   1 
ATOM   1403 C  CA  . GLU A 1 182 ? -16.30400 5.49900   -61.94700 1.000 36.37460  ? 182 GLU A CA  1 
ATOM   1404 C  C   . GLU A 1 182 ? -14.94100 5.56500   -61.28600 1.000 37.40415  ? 182 GLU A C   1 
ATOM   1405 O  O   . GLU A 1 182 ? -14.57600 6.56500   -60.65800 1.000 37.98883  ? 182 GLU A O   1 
ATOM   1406 C  CB  . GLU A 1 182 ? -16.14700 5.89500   -63.41100 1.000 38.94873  ? 182 GLU A CB  1 
ATOM   1407 C  CG  . GLU A 1 182 ? -17.41300 5.95900   -64.20700 1.000 38.52532  ? 182 GLU A CG  1 
ATOM   1408 C  CD  . GLU A 1 182 ? -17.10800 6.12100   -65.66100 1.000 38.29104  ? 182 GLU A CD  1 
ATOM   1409 O  OE1 . GLU A 1 182 ? -15.93300 5.95800   -66.01100 1.000 43.25800  ? 182 GLU A OE1 1 
ATOM   1410 O  OE2 . GLU A 1 182 ? -18.02500 6.37200   -66.46700 1.000 43.53161  ? 182 GLU A OE2 1 
ATOM   1411 N  N   . ARG A 1 183 ? -14.17200 4.48900   -61.45200 1.000 37.99947  ? 183 ARG A N   1 
ATOM   1412 C  CA  . ARG A 1 183 ? -12.82500 4.47100   -60.89700 1.000 37.20111  ? 183 ARG A CA  1 
ATOM   1413 C  C   . ARG A 1 183 ? -11.94600 5.53400   -61.54600 1.000 38.26616  ? 183 ARG A C   1 
ATOM   1414 O  O   . ARG A 1 183 ? -11.03300 6.06300   -60.90100 1.000 37.76024  ? 183 ARG A O   1 
ATOM   1415 C  CB  . ARG A 1 183 ? -12.22400 3.08100   -61.06400 1.000 37.42543  ? 183 ARG A CB  1 
ATOM   1416 C  CG  . ARG A 1 183 ? -13.05800 2.00800   -60.36700 1.000 38.64750  ? 183 ARG A CG  1 
ATOM   1417 C  CD  . ARG A 1 183 ? -12.80000 2.02900   -58.86400 1.000 38.57959  ? 183 ARG A CD  1 
ATOM   1418 N  NE  . ARG A 1 183 ? -13.94300 1.54300   -58.10100 1.000 42.68336  ? 183 ARG A NE  1 
ATOM   1419 C  CZ  . ARG A 1 183 ? -13.92200 1.29000   -56.79700 1.000 47.08345  ? 183 ARG A CZ  1 
ATOM   1420 N  NH1 . ARG A 1 183 ? -12.80600 1.39800   -56.08600 1.000 42.22062  ? 183 ARG A NH1 1 
ATOM   1421 N  NH2 . ARG A 1 183 ? -15.04700 0.90900   -56.19100 1.000 44.71993  ? 183 ARG A NH2 1 
ATOM   1422 N  N   . ASP A 1 184 ? -12.21700 5.87900   -62.80600 1.000 37.50976  ? 184 ASP A N   1 
ATOM   1423 C  CA  . ASP A 1 184 ? -11.38700 6.85900   -63.49600 1.000 37.72305  ? 184 ASP A CA  1 
ATOM   1424 C  C   . ASP A 1 184 ? -11.70700 8.30000   -63.09200 1.000 41.71123  ? 184 ASP A C   1 
ATOM   1425 O  O   . ASP A 1 184 ? -11.08000 9.22600   -63.62600 1.000 41.75937  ? 184 ASP A O   1 
ATOM   1426 C  CB  . ASP A 1 184 ? -11.48900 6.66500   -65.02100 1.000 39.77531  ? 184 ASP A CB  1 
ATOM   1427 C  CG  . ASP A 1 184 ? -12.87900 6.93500   -65.57800 1.000 39.29597  ? 184 ASP A CG  1 
ATOM   1428 O  OD1 . ASP A 1 184 ? -13.65300 7.69700   -64.95800 1.000 37.61983  ? 184 ASP A OD1 1 
ATOM   1429 O  OD2 . ASP A 1 184 ? -13.20000 6.39500   -66.66700 1.000 40.84914  ? 184 ASP A OD2 1 
ATOM   1430 N  N   . GLN A 1 185 ? -12.66200 8.51200   -62.17100 1.000 37.41653  ? 185 GLN A N   1 
ATOM   1431 C  CA  . GLN A 1 185 ? -12.87200 9.81600   -61.54700 1.000 36.89272  ? 185 GLN A CA  1 
ATOM   1432 C  C   . GLN A 1 185 ? -11.95700 10.05000  -60.35500 1.000 38.11117  ? 185 GLN A C   1 
ATOM   1433 O  O   . GLN A 1 185 ? -11.88700 11.17700  -59.84500 1.000 36.84957  ? 185 GLN A O   1 
ATOM   1434 C  CB  . GLN A 1 185 ? -14.32200 9.97300   -61.08300 1.000 37.58563  ? 185 GLN A CB  1 
ATOM   1435 C  CG  . GLN A 1 185 ? -15.32800 10.11100  -62.21100 1.000 41.56290  ? 185 GLN A CG  1 
ATOM   1436 C  CD  . GLN A 1 185 ? -16.73900 10.09800  -61.69600 1.000 41.80169  ? 185 GLN A CD  1 
ATOM   1437 O  OE1 . GLN A 1 185 ? -17.49500 9.14900   -61.93300 1.000 44.67138  ? 185 GLN A OE1 1 
ATOM   1438 N  NE2 . GLN A 1 185 ? -17.10700 11.14600  -60.97000 1.000 40.57403  ? 185 GLN A NE2 1 
ATOM   1439 N  N   . ALA A 1 186 ? -11.27000 9.01700   -59.89900 1.000 37.26404  ? 186 ALA A N   1 
ATOM   1440 C  CA  . ALA A 1 186 ? -10.40500 9.11300   -58.74400 1.000 39.06476  ? 186 ALA A CA  1 
ATOM   1441 C  C   . ALA A 1 186 ? -8.95000  9.21900   -59.18600 1.000 42.53207  ? 186 ALA A C   1 
ATOM   1442 O  O   . ALA A 1 186 ? -8.58300  8.84300   -60.30500 1.000 42.67942  ? 186 ALA A O   1 
ATOM   1443 C  CB  . ALA A 1 186 ? -10.60500 7.90600   -57.82200 1.000 37.03809  ? 186 ALA A CB  1 
ATOM   1444 N  N   . VAL A 1 187 ? -8.13400  9.77400   -58.29600 1.000 40.56827  ? 187 VAL A N   1 
ATOM   1445 C  CA  . VAL A 1 187 ? -6.68800  9.80000   -58.44700 1.000 43.54596  ? 187 VAL A CA  1 
ATOM   1446 C  C   . VAL A 1 187 ? -6.08400  8.98900   -57.31100 1.000 43.62479  ? 187 VAL A C   1 
ATOM   1447 O  O   . VAL A 1 187 ? -6.70000  8.78200   -56.25900 1.000 40.61535  ? 187 VAL A O   1 
ATOM   1448 C  CB  . VAL A 1 187 ? -6.12500  11.23800  -58.46600 1.000 42.62772  ? 187 VAL A CB  1 
ATOM   1449 C  CG1 . VAL A 1 187 ? -6.58000  11.95200  -59.72200 1.000 48.12118  ? 187 VAL A CG1 1 
ATOM   1450 C  CG2 . VAL A 1 187 ? -6.54400  12.02200  -57.21100 1.000 43.00683  ? 187 VAL A CG2 1 
ATOM   1451 N  N   . LEU A 1 188 ? -4.86600  8.52100   -57.53400 1.000 42.28668  ? 188 LEU A N   1 
ATOM   1452 C  CA  . LEU A 1 188 ? -4.23100  7.54900   -56.66300 1.000 44.19097  ? 188 LEU A CA  1 
ATOM   1453 C  C   . LEU A 1 188 ? -3.26300  8.23700   -55.71900 1.000 43.90143  ? 188 LEU A C   1 
ATOM   1454 O  O   . LEU A 1 188 ? -2.44600  9.06600   -56.14200 1.000 44.68515  ? 188 LEU A O   1 
ATOM   1455 C  CB  . LEU A 1 188 ? -3.49100  6.48400   -57.47400 1.000 46.48266  ? 188 LEU A CB  1 
ATOM   1456 C  CG  . LEU A 1 188 ? -4.32400  5.31900   -57.99500 1.000 53.18048  ? 188 LEU A CG  1 
ATOM   1457 C  CD1 . LEU A 1 188 ? -5.07000  5.71300   -59.25100 1.000 57.46133  ? 188 LEU A CD1 1 
ATOM   1458 C  CD2 . LEU A 1 188 ? -3.42900  4.13100   -58.27000 1.000 59.50862  ? 188 LEU A CD2 1 
ATOM   1459 N  N   . ALA A 1 189 ? -3.36300  7.88500   -54.44200 1.000 45.37524  ? 189 ALA A N   1 
ATOM   1460 C  CA  . ALA A 1 189 ? -2.42000  8.34100   -53.42900 1.000 43.50134  ? 189 ALA A CA  1 
ATOM   1461 C  C   . ALA A 1 189 ? -1.23400  7.37800   -53.38900 1.000 45.43332  ? 189 ALA A C   1 
ATOM   1462 O  O   . ALA A 1 189 ? -1.05900  6.58600   -52.46700 1.000 46.66735  ? 189 ALA A O   1 
ATOM   1463 C  CB  . ALA A 1 189 ? -3.10600  8.44500   -52.07600 1.000 42.39716  ? 189 ALA A CB  1 
ATOM   1464 N  N   . THR A 1 190 ? -0.42400  7.44200   -54.44400 1.000 47.54915  ? 190 THR A N   1 
ATOM   1465 C  CA  . THR A 1 190 ? 0.81200   6.66800   -54.50000 1.000 46.51029  ? 190 THR A CA  1 
ATOM   1466 C  C   . THR A 1 190 ? 1.85000   7.32800   -53.59500 1.000 49.31392  ? 190 THR A C   1 
ATOM   1467 O  O   . THR A 1 190 ? 2.11900   8.52800   -53.72200 1.000 48.71966  ? 190 THR A O   1 
ATOM   1468 C  CB  . THR A 1 190 ? 1.31600   6.56700   -55.93700 1.000 49.47356  ? 190 THR A CB  1 
ATOM   1469 O  OG1 . THR A 1 190 ? 1.51100   7.87700   -56.48300 1.000 46.20283  ? 190 THR A OG1 1 
ATOM   1470 C  CG2 . THR A 1 190 ? 0.31300   5.81700   -56.80300 1.000 51.42745  ? 190 THR A CG2 1 
ATOM   1471 N  N   . MET A 1 191 ? 2.40900   6.55900   -52.66100 1.000 49.94760  ? 191 MET A N   1 
ATOM   1472 C  CA  . MET A 1 191 ? 3.26600   7.12400   -51.62700 1.000 49.45506  ? 191 MET A CA  1 
ATOM   1473 C  C   . MET A 1 191 ? 4.35500   6.13000   -51.24500 1.000 48.56168  ? 191 MET A C   1 
ATOM   1474 O  O   . MET A 1 191 ? 4.21400   4.91900   -51.41600 1.000 49.71482  ? 191 MET A O   1 
ATOM   1475 C  CB  . MET A 1 191 ? 2.46700   7.49600   -50.37000 1.000 43.98801  ? 191 MET A CB  1 
ATOM   1476 C  CG  . MET A 1 191 ? 1.42300   8.59300   -50.53600 1.000 45.04829  ? 191 MET A CG  1 
ATOM   1477 S  SD  . MET A 1 191 ? 0.40300   8.84200   -49.05000 1.000 44.36136  ? 191 MET A SD  1 
ATOM   1478 C  CE  . MET A 1 191 ? -0.53500  7.31700   -48.98300 1.000 44.44287  ? 191 MET A CE  1 
ATOM   1479 N  N   . ASP A 1 192 ? 5.43200   6.66000   -50.71200 1.000 48.04058  ? 192 ASP A N   1 
ATOM   1480 C  CA  . ASP A 1 192 ? 6.45700   5.90900   -50.01700 1.000 48.15144  ? 192 ASP A CA  1 
ATOM   1481 C  C   . ASP A 1 192 ? 6.16500   5.90900   -48.52600 1.000 48.09595  ? 192 ASP A C   1 
ATOM   1482 O  O   . ASP A 1 192 ? 5.47100   6.79900   -48.02800 1.000 45.10718  ? 192 ASP A O   1 
ATOM   1483 C  CB  . ASP A 1 192 ? 7.83300   6.53200   -50.26700 1.000 51.90493  ? 192 ASP A CB  1 
ATOM   1484 C  CG  . ASP A 1 192 ? 8.31600   6.33200   -51.68700 1.000 59.91231  ? 192 ASP A CG  1 
ATOM   1485 O  OD1 . ASP A 1 192 ? 8.18600   5.20000   -52.21300 1.000 61.88656  ? 192 ASP A OD1 1 
ATOM   1486 O  OD2 . ASP A 1 192 ? 8.83600   7.31000   -52.27000 1.000 64.26318  ? 192 ASP A OD2 1 
ATOM   1487 N  N   . PRO A 1 193 ? 6.67300   4.92300   -47.78300 1.000 47.51360  ? 193 PRO A N   1 
ATOM   1488 C  CA  . PRO A 1 193 ? 6.54500   4.95800   -46.31800 1.000 48.48588  ? 193 PRO A CA  1 
ATOM   1489 C  C   . PRO A 1 193 ? 7.20000   6.20800   -45.75600 1.000 49.27757  ? 193 PRO A C   1 
ATOM   1490 O  O   . PRO A 1 193 ? 8.31000   6.58000   -46.15100 1.000 48.68372  ? 193 PRO A O   1 
ATOM   1491 C  CB  . PRO A 1 193 ? 7.27600   3.69000   -45.86100 1.000 52.24212  ? 193 PRO A CB  1 
ATOM   1492 C  CG  . PRO A 1 193 ? 7.38200   2.83500   -47.07800 1.000 52.16639  ? 193 PRO A CG  1 
ATOM   1493 C  CD  . PRO A 1 193 ? 7.46800   3.77000   -48.23700 1.000 51.96893  ? 193 PRO A CD  1 
ATOM   1494 N  N   . GLY A 1 194 ? 6.49900   6.86000   -44.83400 1.000 49.68977  ? 194 GLY A N   1 
ATOM   1495 C  CA  . GLY A 1 194 ? 6.90100   8.14200   -44.31400 1.000 48.65323  ? 194 GLY A CA  1 
ATOM   1496 C  C   . GLY A 1 194 ? 6.11500   9.29900   -44.88800 1.000 48.24239  ? 194 GLY A C   1 
ATOM   1497 O  O   . GLY A 1 194 ? 6.16000   10.40500  -44.32700 1.000 46.25307  ? 194 GLY A O   1 
ATOM   1498 N  N   . ASP A 1 195 ? 5.41400   9.07200   -45.99900 1.000 44.15362  ? 195 ASP A N   1 
ATOM   1499 C  CA  . ASP A 1 195 ? 4.43300   10.01500  -46.49600 1.000 43.04181  ? 195 ASP A CA  1 
ATOM   1500 C  C   . ASP A 1 195 ? 3.16200   9.90100   -45.65800 1.000 41.64457  ? 195 ASP A C   1 
ATOM   1501 O  O   . ASP A 1 195 ? 3.00500   8.98200   -44.85200 1.000 41.34637  ? 195 ASP A O   1 
ATOM   1502 C  CB  . ASP A 1 195 ? 4.13000   9.75900   -47.97400 1.000 44.21427  ? 195 ASP A CB  1 
ATOM   1503 C  CG  . ASP A 1 195 ? 5.34300   9.97300   -48.87300 1.000 52.19598  ? 195 ASP A CG  1 
ATOM   1504 O  OD1 . ASP A 1 195 ? 6.31700   10.62400  -48.42600 1.000 52.34905  ? 195 ASP A OD1 1 
ATOM   1505 O  OD2 . ASP A 1 195 ? 5.31800   9.50000   -50.03500 1.000 51.08194  ? 195 ASP A OD2 1 
ATOM   1506 N  N   . VAL A 1 196 ? 2.24600   10.84800  -45.84400 1.000 39.42440  ? 196 VAL A N   1 
ATOM   1507 C  CA  . VAL A 1 196 ? 0.96700   10.85100  -45.13000 1.000 42.27932  ? 196 VAL A CA  1 
ATOM   1508 C  C   . VAL A 1 196 ? -0.11700  11.34400  -46.07500 1.000 40.49873  ? 196 VAL A C   1 
ATOM   1509 O  O   . VAL A 1 196 ? 0.04200   12.39000  -46.71300 1.000 42.00501  ? 196 VAL A O   1 
ATOM   1510 C  CB  . VAL A 1 196 ? 0.99400   11.73800  -43.86700 1.000 41.46189  ? 196 VAL A CB  1 
ATOM   1511 C  CG1 . VAL A 1 196 ? -0.38700  11.77500  -43.21800 1.000 40.26058  ? 196 VAL A CG1 1 
ATOM   1512 C  CG2 . VAL A 1 196 ? 2.04100   11.25200  -42.87300 1.000 40.92889  ? 196 VAL A CG2 1 
ATOM   1513 N  N   . LEU A 1 197 ? -1.21300  10.59900  -46.17000 1.000 36.37966  ? 197 LEU A N   1 
ATOM   1514 C  CA  . LEU A 1 197 ? -2.38500  11.05900  -46.90300 1.000 39.69474  ? 197 LEU A CA  1 
ATOM   1515 C  C   . LEU A 1 197 ? -3.37400  11.66900  -45.91300 1.000 38.61531  ? 197 LEU A C   1 
ATOM   1516 O  O   . LEU A 1 197 ? -3.70900  11.04800  -44.89500 1.000 33.58097  ? 197 LEU A O   1 
ATOM   1517 C  CB  . LEU A 1 197 ? -3.03700  9.92000   -47.69000 1.000 35.35962  ? 197 LEU A CB  1 
ATOM   1518 C  CG  . LEU A 1 197 ? -4.35800  10.25600  -48.39800 1.000 39.02042  ? 197 LEU A CG  1 
ATOM   1519 C  CD1 . LEU A 1 197 ? -4.17500  11.37400  -49.41400 1.000 36.99850  ? 197 LEU A CD1 1 
ATOM   1520 C  CD2 . LEU A 1 197 ? -4.98700  9.01800   -49.05400 1.000 34.99641  ? 197 LEU A CD2 1 
ATOM   1521 N  N   . ILE A 1 198 ? -3.84300  12.88000  -46.21300 1.000 36.85457  ? 198 ILE A N   1 
ATOM   1522 C  CA  . ILE A 1 198 ? -4.77900  13.60100  -45.34900 1.000 37.22103  ? 198 ILE A CA  1 
ATOM   1523 C  C   . ILE A 1 198 ? -6.06300  13.85700  -46.13200 1.000 35.55013  ? 198 ILE A C   1 
ATOM   1524 O  O   . ILE A 1 198 ? -6.02400  14.43800  -47.22400 1.000 37.27193  ? 198 ILE A O   1 
ATOM   1525 C  CB  . ILE A 1 198 ? -4.15300  14.89900  -44.81400 1.000 39.82257  ? 198 ILE A CB  1 
ATOM   1526 C  CG1 . ILE A 1 198 ? -2.96100  14.51200  -43.92600 1.000 37.92214  ? 198 ILE A CG1 1 
ATOM   1527 C  CG2 . ILE A 1 198 ? -5.18000  15.72400  -44.04400 1.000 36.65434  ? 198 ILE A CG2 1 
ATOM   1528 C  CD1 . ILE A 1 198 ? -2.29900  15.63800  -43.22700 1.000 44.31185  ? 198 ILE A CD1 1 
ATOM   1529 N  N   . VAL A 1 199 ? -7.19100  13.39400  -45.58900 1.000 34.87401  ? 199 VAL A N   1 
ATOM   1530 C  CA  . VAL A 1 199 ? -8.47800  13.35000  -46.28100 1.000 34.74056  ? 199 VAL A CA  1 
ATOM   1531 C  C   . VAL A 1 199 ? -9.54100  14.06500  -45.44100 1.000 33.48079  ? 199 VAL A C   1 
ATOM   1532 O  O   . VAL A 1 199 ? -9.79300  13.68600  -44.29000 1.000 31.85512  ? 199 VAL A O   1 
ATOM   1533 C  CB  . VAL A 1 199 ? -8.90000  11.90300  -46.58500 1.000 35.30925  ? 199 VAL A CB  1 
ATOM   1534 C  CG1 . VAL A 1 199 ? -10.30200 11.86300  -47.21100 1.000 33.85936  ? 199 VAL A CG1 1 
ATOM   1535 C  CG2 . VAL A 1 199 ? -7.88900  11.26700  -47.52400 1.000 37.15247  ? 199 VAL A CG2 1 
ATOM   1536 N  N   . ARG A 1 200 ? -10.13600 15.10800  -46.01900 1.000 35.73420  ? 200 ARG A N   1 
ATOM   1537 C  CA  . ARG A 1 200 ? -11.25000 15.84800  -45.43400 1.000 34.39626  ? 200 ARG A CA  1 
ATOM   1538 C  C   . ARG A 1 200 ? -12.48400 14.96300  -45.25300 1.000 36.35735  ? 200 ARG A C   1 
ATOM   1539 O  O   . ARG A 1 200 ? -12.69400 13.97500  -45.97000 1.000 30.58741  ? 200 ARG A O   1 
ATOM   1540 C  CB  . ARG A 1 200 ? -11.60300 17.03300  -46.33700 1.000 36.69161  ? 200 ARG A CB  1 
ATOM   1541 C  CG  . ARG A 1 200 ? -12.66000 17.96000  -45.79900 1.000 39.06581  ? 200 ARG A CG  1 
ATOM   1542 C  CD  . ARG A 1 200 ? -13.29600 18.76800  -46.90600 1.000 39.59003  ? 200 ARG A CD  1 
ATOM   1543 N  NE  . ARG A 1 200 ? -13.93500 19.96000  -46.35700 1.000 45.02480  ? 200 ARG A NE  1 
ATOM   1544 C  CZ  . ARG A 1 200 ? -15.11100 19.96000  -45.74100 1.000 48.99929  ? 200 ARG A CZ  1 
ATOM   1545 N  NH1 . ARG A 1 200 ? -15.82500 18.84600  -45.60200 1.000 43.64917  ? 200 ARG A NH1 1 
ATOM   1546 N  NH2 . ARG A 1 200 ? -15.58100 21.10100  -45.24000 1.000 45.60570  ? 200 ARG A NH2 1 
ATOM   1547 N  N   . GLN A 1 201 ? -13.31100 15.34400  -44.28300 1.000 36.19631  ? 201 GLN A N   1 
ATOM   1548 C  CA  . GLN A 1 201 ? -14.64300 14.76700  -44.14200 1.000 33.88894  ? 201 GLN A CA  1 
ATOM   1549 C  C   . GLN A 1 201 ? -15.44100 14.94400  -45.43400 1.000 34.00085  ? 201 GLN A C   1 
ATOM   1550 O  O   . GLN A 1 201 ? -15.30800 15.95600  -46.12900 1.000 33.59356  ? 201 GLN A O   1 
ATOM   1551 C  CB  . GLN A 1 201 ? -15.35300 15.44300  -42.96700 1.000 32.01391  ? 201 GLN A CB  1 
ATOM   1552 C  CG  . GLN A 1 201 ? -16.75500 14.99000  -42.66700 1.000 32.74477  ? 201 GLN A CG  1 
ATOM   1553 C  CD  . GLN A 1 201 ? -17.36200 15.81300  -41.53900 1.000 32.42543  ? 201 GLN A CD  1 
ATOM   1554 O  OE1 . GLN A 1 201 ? -16.63900 16.35500  -40.71400 1.000 33.89579  ? 201 GLN A OE1 1 
ATOM   1555 N  NE2 . GLN A 1 201 ? -18.67800 15.90700  -41.50100 1.000 32.15856  ? 201 GLN A NE2 1 
ATOM   1556 N  N   . ARG A 1 202 ? -16.26100 13.93900  -45.75800 1.000 35.50472  ? 202 ARG A N   1 
ATOM   1557 C  CA  . ARG A 1 202 ? -17.18900 13.85400  -46.89100 1.000 32.52230  ? 202 ARG A CA  1 
ATOM   1558 C  C   . ARG A 1 202 ? -16.50500 13.53000  -48.21100 1.000 35.87822  ? 202 ARG A C   1 
ATOM   1559 O  O   . ARG A 1 202 ? -17.19500 13.48100  -49.22300 1.000 31.30040  ? 202 ARG A O   1 
ATOM   1560 C  CB  . ARG A 1 202 ? -18.00100 15.13300  -47.13400 1.000 38.79374  ? 202 ARG A CB  1 
ATOM   1561 C  CG  . ARG A 1 202 ? -18.96100 15.52700  -46.05100 1.000 41.40185  ? 202 ARG A CG  1 
ATOM   1562 C  CD  . ARG A 1 202 ? -19.45000 16.93300  -46.33400 1.000 45.26489  ? 202 ARG A CD  1 
ATOM   1563 N  NE  . ARG A 1 202 ? -20.27300 16.97400  -47.53700 1.000 46.30009  ? 202 ARG A NE  1 
ATOM   1564 C  CZ  . ARG A 1 202 ? -21.59500 16.86100  -47.52900 1.000 47.40517  ? 202 ARG A CZ  1 
ATOM   1565 N  NH1 . ARG A 1 202 ? -22.26900 16.70500  -46.39300 1.000 45.27532  ? 202 ARG A NH1 1 
ATOM   1566 N  NH2 . ARG A 1 202 ? -22.25700 16.91500  -48.68200 1.000 42.51068  ? 202 ARG A NH2 1 
ATOM   1567 N  N   . VAL A 1 203 ? -15.19300 13.34400  -48.24500 1.000 32.69917  ? 203 VAL A N   1 
ATOM   1568 C  CA  . VAL A 1 203 ? -14.51700 13.05800  -49.49800 1.000 34.11116  ? 203 VAL A CA  1 
ATOM   1569 C  C   . VAL A 1 203 ? -14.76500 11.60100  -49.86300 1.000 34.58229  ? 203 VAL A C   1 
ATOM   1570 O  O   . VAL A 1 203 ? -14.55800 10.70000  -49.04500 1.000 31.40265  ? 203 VAL A O   1 
ATOM   1571 C  CB  . VAL A 1 203 ? -13.01900 13.37600  -49.39300 1.000 32.87269  ? 203 VAL A CB  1 
ATOM   1572 C  CG1 . VAL A 1 203 ? -12.31100 12.96900  -50.67900 1.000 35.68946  ? 203 VAL A CG1 1 
ATOM   1573 C  CG2 . VAL A 1 203 ? -12.83900 14.86400  -49.12300 1.000 33.77163  ? 203 VAL A CG2 1 
ATOM   1574 N  N   . VAL A 1 204 ? -15.25300 11.37700  -51.08500 1.000 32.44032  ? 204 VAL A N   1 
ATOM   1575 C  CA  . VAL A 1 204 ? -15.49700 10.02700  -51.57800 1.000 31.95199  ? 204 VAL A CA  1 
ATOM   1576 C  C   . VAL A 1 204 ? -14.17000 9.37600   -51.95200 1.000 32.77029  ? 204 VAL A C   1 
ATOM   1577 O  O   . VAL A 1 204 ? -13.30600 9.99300   -52.58700 1.000 35.46853  ? 204 VAL A O   1 
ATOM   1578 C  CB  . VAL A 1 204 ? -16.46200 10.07600  -52.77800 1.000 33.64489  ? 204 VAL A CB  1 
ATOM   1579 C  CG1 . VAL A 1 204 ? -16.67400 8.69900   -53.38300 1.000 32.67355  ? 204 VAL A CG1 1 
ATOM   1580 C  CG2 . VAL A 1 204 ? -17.77700 10.68400  -52.35400 1.000 33.71043  ? 204 VAL A CG2 1 
ATOM   1581 N  N   . HIS A 1 205 ? -13.99600 8.12100   -51.55800 1.000 32.32823  ? 205 HIS A N   1 
ATOM   1582 C  CA  . HIS A 1 205 ? -12.71100 7.46300   -51.72700 1.000 34.63050  ? 205 HIS A CA  1 
ATOM   1583 C  C   . HIS A 1 205 ? -12.90900 5.96700   -51.56100 1.000 37.13458  ? 205 HIS A C   1 
ATOM   1584 O  O   . HIS A 1 205 ? -13.99100 5.49800   -51.18800 1.000 34.69753  ? 205 HIS A O   1 
ATOM   1585 C  CB  . HIS A 1 205 ? -11.68000 7.97600   -50.72000 1.000 33.87222  ? 205 HIS A CB  1 
ATOM   1586 C  CG  . HIS A 1 205 ? -12.06500 7.69900   -49.31100 1.000 36.66663  ? 205 HIS A CG  1 
ATOM   1587 N  ND1 . HIS A 1 205 ? -13.04800 8.41500   -48.66800 1.000 36.39024  ? 205 HIS A ND1 1 
ATOM   1588 C  CD2 . HIS A 1 205 ? -11.66000 6.74200   -48.44500 1.000 35.48039  ? 205 HIS A CD2 1 
ATOM   1589 C  CE1 . HIS A 1 205 ? -13.21000 7.93200   -47.44800 1.000 40.83002  ? 205 HIS A CE1 1 
ATOM   1590 N  NE2 . HIS A 1 205 ? -12.36600 6.93100   -47.28300 1.000 40.90231  ? 205 HIS A NE2 1 
ATOM   1591 N  N   . ALA A 1 206 ? -11.84000 5.22300   -51.82600 1.000 35.34286  ? 206 ALA A N   1 
ATOM   1592 C  CA  . ALA A 1 206 ? -11.90600 3.77500   -51.70000 1.000 39.35027  ? 206 ALA A CA  1 
ATOM   1593 C  C   . ALA A 1 206 ? -10.50300 3.20300   -51.54900 1.000 44.39024  ? 206 ALA A C   1 
ATOM   1594 O  O   . ALA A 1 206 ? -9.57000  3.63300   -52.23300 1.000 40.64305  ? 206 ALA A O   1 
ATOM   1595 C  CB  . ALA A 1 206 ? -12.60800 3.14300   -52.90900 1.000 39.45032  ? 206 ALA A CB  1 
ATOM   1596 N  N   . GLY A 1 207 ? -10.36400 2.23900   -50.64100 1.000 45.79510  ? 207 GLY A N   1 
ATOM   1597 C  CA  . GLY A 1 207 ? -9.14800  1.44800   -50.61400 1.000 44.77810  ? 207 GLY A CA  1 
ATOM   1598 C  C   . GLY A 1 207 ? -8.91700  0.75900   -51.94500 1.000 47.55909  ? 207 GLY A C   1 
ATOM   1599 O  O   . GLY A 1 207 ? -9.83800  0.20800   -52.55700 1.000 48.12623  ? 207 GLY A O   1 
ATOM   1600 N  N   . GLY A 1 208 ? -7.66700  0.78700   -52.39600 1.000 49.78048  ? 208 GLY A N   1 
ATOM   1601 C  CA  . GLY A 1 208 ? -7.35600  0.25500   -53.70300 1.000 52.18711  ? 208 GLY A CA  1 
ATOM   1602 C  C   . GLY A 1 208 ? -7.32700  -1.25300  -53.79700 1.000 52.67580  ? 208 GLY A C   1 
ATOM   1603 O  O   . GLY A 1 208 ? -7.19500  -1.77200  -54.91000 1.000 54.31776  ? 208 GLY A O   1 
ATOM   1604 N  N   . GLY A 1 209 ? -7.45700  -1.96100  -52.68100 1.000 53.67130  ? 209 GLY A N   1 
ATOM   1605 C  CA  . GLY A 1 209 ? -7.28200  -3.40600  -52.72700 1.000 58.44886  ? 209 GLY A CA  1 
ATOM   1606 C  C   . GLY A 1 209 ? -5.81400  -3.75100  -52.90700 1.000 58.66327  ? 209 GLY A C   1 
ATOM   1607 O  O   . GLY A 1 209 ? -4.94300  -3.20200  -52.22200 1.000 59.14928  ? 209 GLY A O   1 
ATOM   1608 N  N   . ASN A 1 210 ? -5.53000  -4.65100  -53.85000 1.000 63.93911  ? 210 ASN A N   1 
ATOM   1609 C  CA  . ASN A 1 210 ? -4.16200  -5.05700  -54.16900 1.000 65.02428  ? 210 ASN A CA  1 
ATOM   1610 C  C   . ASN A 1 210 ? -4.15000  -5.97100  -55.38600 1.000 66.97481  ? 210 ASN A C   1 
ATOM   1611 O  O   . ASN A 1 210 ? -4.37100  -7.17800  -55.25700 1.000 69.71524  ? 210 ASN A O   1 
ATOM   1612 C  CB  . ASN A 1 210 ? -3.51700  -5.76800  -52.97500 1.000 64.42551  ? 210 ASN A CB  1 
ATOM   1613 C  CG  . ASN A 1 210 ? -2.02200  -5.93500  -53.12300 1.000 62.74547  ? 210 ASN A CG  1 
ATOM   1614 O  OD1 . ASN A 1 210 ? -1.48000  -5.90400  -54.23000 1.000 62.90817  ? 210 ASN A OD1 1 
ATOM   1615 N  ND2 . ASN A 1 210 ? -1.34500  -6.12200  -52.00000 1.000 56.95703  ? 210 ASN A ND2 1 
ATOM   1616 N  N   . ARG A 1 211 ? -3.86600  -5.41400  -56.56400 1.000 73.00369  ? 211 ARG A N   1 
ATOM   1617 C  CA  . ARG A 1 211 ? -3.88800  -6.17000  -57.80900 1.000 75.26907  ? 211 ARG A CA  1 
ATOM   1618 C  C   . ARG A 1 211 ? -2.65200  -7.03900  -58.01600 1.000 76.86605  ? 211 ARG A C   1 
ATOM   1619 O  O   . ARG A 1 211 ? -2.57700  -7.73100  -59.03600 1.000 78.34313  ? 211 ARG A O   1 
ATOM   1620 C  CB  . ARG A 1 211 ? -4.02600  -5.22700  -59.01300 1.000 78.94273  ? 211 ARG A CB  1 
ATOM   1621 C  CG  . ARG A 1 211 ? -5.01600  -4.06600  -58.84300 1.000 83.82876  ? 211 ARG A CG  1 
ATOM   1622 C  CD  . ARG A 1 211 ? -5.19200  -3.25800  -60.15300 1.000 87.87289  ? 211 ARG A CD  1 
ATOM   1623 N  NE  . ARG A 1 211 ? -4.00500  -2.51300  -60.57100 1.000 81.93452  ? 211 ARG A NE  1 
ATOM   1624 C  CZ  . ARG A 1 211 ? -3.10400  -2.95600  -61.43600 1.000 79.59607  ? 211 ARG A CZ  1 
ATOM   1625 N  NH1 . ARG A 1 211 ? -3.20000  -4.15600  -61.98500 1.000 80.20089  ? 211 ARG A NH1 1 
ATOM   1626 N  NH2 . ARG A 1 211 ? -2.07500  -2.17600  -61.75600 1.000 85.71365  ? 211 ARG A NH2 1 
ATOM   1627 N  N   . THR A 1 212 ? -1.68200  -7.01900  -57.10400 1.000 72.44405  ? 212 THR A N   1 
ATOM   1628 C  CA  . THR A 1 212 ? -0.48000  -7.81500  -57.31100 1.000 74.17107  ? 212 THR A CA  1 
ATOM   1629 C  C   . THR A 1 212 ? -0.78600  -9.30700  -57.15600 1.000 77.07826  ? 212 THR A C   1 
ATOM   1630 O  O   . THR A 1 212 ? -1.82000  -9.71100  -56.61700 1.000 76.71800  ? 212 THR A O   1 
ATOM   1631 C  CB  . THR A 1 212 ? 0.63300   -7.39800  -56.34100 1.000 71.73757  ? 212 THR A CB  1 
ATOM   1632 O  OG1 . THR A 1 212 ? 0.20700   -7.60200  -54.98800 1.000 68.13379  ? 212 THR A OG1 1 
ATOM   1633 C  CG2 . THR A 1 212 ? 1.00800   -5.93100  -56.53700 1.000 65.47219  ? 212 THR A CG2 1 
ATOM   1634 N  N   . THR A 1 213 ? 0.12600   -10.13200 -57.66600 1.000 79.38312  ? 213 THR A N   1 
ATOM   1635 C  CA  . THR A 1 213 ? 0.00300   -11.58100 -57.56000 1.000 84.49336  ? 213 THR A CA  1 
ATOM   1636 C  C   . THR A 1 213 ? 0.91400   -12.17600 -56.49900 1.000 86.98553  ? 213 THR A C   1 
ATOM   1637 O  O   . THR A 1 213 ? 0.54100   -13.16500 -55.85800 1.000 88.35841  ? 213 THR A O   1 
ATOM   1638 C  CB  . THR A 1 213 ? 0.31700   -12.24300 -58.90300 1.000 81.78753  ? 213 THR A CB  1 
ATOM   1639 O  OG1 . THR A 1 213 ? 1.67600   -11.95800 -59.26100 1.000 79.37151  ? 213 THR A OG1 1 
ATOM   1640 C  CG2 . THR A 1 213 ? -0.61200  -11.71200 -59.97600 1.000 82.55077  ? 213 THR A CG2 1 
ATOM   1641 N  N   . ALA A 1 214 ? 2.09900   -11.59800 -56.31400 1.000 86.89112  ? 214 ALA A N   1 
ATOM   1642 C  CA  . ALA A 1 214 ? 3.03300   -11.96900 -55.26600 1.000 84.25942  ? 214 ALA A CA  1 
ATOM   1643 C  C   . ALA A 1 214 ? 3.40300   -10.71800 -54.47900 1.000 84.31252  ? 214 ALA A C   1 
ATOM   1644 O  O   . ALA A 1 214 ? 2.97600   -9.60500  -54.80300 1.000 82.30805  ? 214 ALA A O   1 
ATOM   1645 C  CB  . ALA A 1 214 ? 4.28300   -12.63900 -55.85100 1.000 85.30199  ? 214 ALA A CB  1 
ATOM   1646 N  N   . GLY A 1 215 ? 4.19600   -10.90800 -53.43500 1.000 86.17893  ? 215 GLY A N   1 
ATOM   1647 C  CA  . GLY A 1 215 ? 4.64700   -9.81800  -52.59700 1.000 81.59714  ? 215 GLY A CA  1 
ATOM   1648 C  C   . GLY A 1 215 ? 3.98800   -9.83900  -51.22400 1.000 73.47570  ? 215 GLY A C   1 
ATOM   1649 O  O   . GLY A 1 215 ? 2.94300   -10.45700 -51.00700 1.000 72.74392  ? 215 GLY A O   1 
ATOM   1650 N  N   . LYS A 1 216 ? 4.63900   -9.15700  -50.27600 1.000 68.34471  ? 216 LYS A N   1 
ATOM   1651 C  CA  . LYS A 1 216 ? 4.09300   -9.00600  -48.93500 1.000 73.08181  ? 216 LYS A CA  1 
ATOM   1652 C  C   . LYS A 1 216 ? 2.88500   -8.06800  -48.96300 1.000 69.61609  ? 216 LYS A C   1 
ATOM   1653 O  O   . LYS A 1 216 ? 2.76600   -7.22400  -49.85700 1.000 68.28869  ? 216 LYS A O   1 
ATOM   1654 C  CB  . LYS A 1 216 ? 5.15000   -8.45900  -47.96900 1.000 73.85278  ? 216 LYS A CB  1 
ATOM   1655 C  CG  . LYS A 1 216 ? 6.08000   -9.51100  -47.35300 1.000 74.03649  ? 216 LYS A CG  1 
ATOM   1656 C  CD  . LYS A 1 216 ? 7.13500   -8.86000  -46.45300 1.000 76.09596  ? 216 LYS A CD  1 
ATOM   1657 C  CE  . LYS A 1 216 ? 8.07100   -9.89300  -45.82500 1.000 71.08579  ? 216 LYS A CE  1 
ATOM   1658 N  NZ  . LYS A 1 216 ? 8.78000   -10.74800 -46.82700 1.000 73.99132  ? 216 LYS A NZ  1 
ATOM   1659 N  N   . PRO A 1 217 ? 1.97500   -8.19400  -47.99500 1.000 68.50427  ? 217 PRO A N   1 
ATOM   1660 C  CA  . PRO A 1 217 ? 0.75300   -7.37900  -48.02300 1.000 61.63609  ? 217 PRO A CA  1 
ATOM   1661 C  C   . PRO A 1 217 ? 1.04800   -5.88900  -47.93200 1.000 61.41819  ? 217 PRO A C   1 
ATOM   1662 O  O   . PRO A 1 217 ? 2.05200   -5.46300  -47.35600 1.000 60.67299  ? 217 PRO A O   1 
ATOM   1663 C  CB  . PRO A 1 217 ? -0.02400  -7.86100  -46.78900 1.000 63.25506  ? 217 PRO A CB  1 
ATOM   1664 C  CG  . PRO A 1 217 ? 0.51600   -9.21600  -46.49000 1.000 67.14231  ? 217 PRO A CG  1 
ATOM   1665 C  CD  . PRO A 1 217 ? 1.96400   -9.17500  -46.89400 1.000 70.29590  ? 217 PRO A CD  1 
ATOM   1666 N  N   . ARG A 1 218 ? 0.15000   -5.09600  -48.51200 1.000 59.21830  ? 218 ARG A N   1 
ATOM   1667 C  CA  . ARG A 1 218 ? 0.20200   -3.65300  -48.33300 1.000 56.25723  ? 218 ARG A CA  1 
ATOM   1668 C  C   . ARG A 1 218 ? -0.26500  -3.29400  -46.92800 1.000 54.14631  ? 218 ARG A C   1 
ATOM   1669 O  O   . ARG A 1 218 ? -1.26400  -3.82200  -46.43200 1.000 54.60775  ? 218 ARG A O   1 
ATOM   1670 C  CB  . ARG A 1 218 ? -0.66200  -2.95000  -49.38100 1.000 57.26196  ? 218 ARG A CB  1 
ATOM   1671 C  CG  . ARG A 1 218 ? -0.71900  -1.43100  -49.21600 1.000 56.34138  ? 218 ARG A CG  1 
ATOM   1672 C  CD  . ARG A 1 218 ? -1.35500  -0.73400  -50.42400 1.000 56.31523  ? 218 ARG A CD  1 
ATOM   1673 N  NE  . ARG A 1 218 ? -2.74900  -1.11200  -50.64400 1.000 56.19627  ? 218 ARG A NE  1 
ATOM   1674 C  CZ  . ARG A 1 218 ? -3.77400  -0.65400  -49.93500 1.000 56.09531  ? 218 ARG A CZ  1 
ATOM   1675 N  NH1 . ARG A 1 218 ? -3.59600  0.17000   -48.91500 1.000 54.72079  ? 218 ARG A NH1 1 
ATOM   1676 N  NH2 . ARG A 1 218 ? -5.01000  -1.02800  -50.26000 1.000 54.17058  ? 218 ARG A NH2 1 
ATOM   1677 N  N   . ARG A 1 219 ? 0.46400   -2.39500  -46.28100 1.000 51.24913  ? 219 ARG A N   1 
ATOM   1678 C  CA  . ARG A 1 219 ? 0.27600   -2.12000  -44.86100 1.000 52.41705  ? 219 ARG A CA  1 
ATOM   1679 C  C   . ARG A 1 219 ? -0.04400  -0.64400  -44.66200 1.000 45.96485  ? 219 ARG A C   1 
ATOM   1680 O  O   . ARG A 1 219 ? 0.62800   0.21900   -45.23300 1.000 46.87796  ? 219 ARG A O   1 
ATOM   1681 C  CB  . ARG A 1 219 ? 1.53500   -2.53100  -44.09900 1.000 53.08938  ? 219 ARG A CB  1 
ATOM   1682 C  CG  . ARG A 1 219 ? 1.51600   -2.28000  -42.64200 1.000 51.46590  ? 219 ARG A CG  1 
ATOM   1683 C  CD  . ARG A 1 219 ? 2.82900   -2.73700  -42.01300 1.000 55.34131  ? 219 ARG A CD  1 
ATOM   1684 N  NE  . ARG A 1 219 ? 2.82100   -4.14600  -41.64200 1.000 54.56510  ? 219 ARG A NE  1 
ATOM   1685 C  CZ  . ARG A 1 219 ? 3.59500   -4.67300  -40.70200 1.000 56.45557  ? 219 ARG A CZ  1 
ATOM   1686 N  NH1 . ARG A 1 219 ? 4.46300   -3.93900  -40.02900 1.000 51.29519  ? 219 ARG A NH1 1 
ATOM   1687 N  NH2 . ARG A 1 219 ? 3.49400   -5.97100  -40.42800 1.000 60.19833  ? 219 ARG A NH2 1 
ATOM   1688 N  N   . VAL A 1 220 ? -1.07600  -0.34800  -43.87400 1.000 45.46659  ? 220 VAL A N   1 
ATOM   1689 C  CA  . VAL A 1 220 ? -1.49800  1.03900   -43.68700 1.000 42.21591  ? 220 VAL A CA  1 
ATOM   1690 C  C   . VAL A 1 220 ? -2.04300  1.22600   -42.27700 1.000 45.24706  ? 220 VAL A C   1 
ATOM   1691 O  O   . VAL A 1 220 ? -2.80100  0.39300   -41.76500 1.000 42.59539  ? 220 VAL A O   1 
ATOM   1692 C  CB  . VAL A 1 220 ? -2.54400  1.45200   -44.74900 1.000 40.39230  ? 220 VAL A CB  1 
ATOM   1693 C  CG1 . VAL A 1 220 ? -3.75800  0.53400   -44.70300 1.000 41.32546  ? 220 VAL A CG1 1 
ATOM   1694 C  CG2 . VAL A 1 220 ? -2.95900  2.88200   -44.55800 1.000 40.19950  ? 220 VAL A CG2 1 
ATOM   1695 N  N   . VAL A 1 221 ? -1.66600  2.34400   -41.65800 1.000 38.98032  ? 221 VAL A N   1 
ATOM   1696 C  CA  . VAL A 1 221 ? -2.18800  2.74500   -40.36700 1.000 39.31732  ? 221 VAL A CA  1 
ATOM   1697 C  C   . VAL A 1 221 ? -3.12500  3.92500   -40.59700 1.000 40.90573  ? 221 VAL A C   1 
ATOM   1698 O  O   . VAL A 1 221 ? -2.73200  4.94100   -41.19100 1.000 36.56206  ? 221 VAL A O   1 
ATOM   1699 C  CB  . VAL A 1 221 ? -1.06800  3.11100   -39.38400 1.000 38.33361  ? 221 VAL A CB  1 
ATOM   1700 C  CG1 . VAL A 1 221 ? -1.65400  3.83900   -38.20100 1.000 34.06317  ? 221 VAL A CG1 1 
ATOM   1701 C  CG2 . VAL A 1 221 ? -0.38100  1.86600   -38.91500 1.000 41.22468  ? 221 VAL A CG2 1 
ATOM   1702 N  N   . LEU A 1 222 ? -4.36200  3.79000   -40.12800 1.000 36.85081  ? 222 LEU A N   1 
ATOM   1703 C  CA  . LEU A 1 222 ? -5.37600  4.81500   -40.30600 1.000 37.30226  ? 222 LEU A CA  1 
ATOM   1704 C  C   . LEU A 1 222 ? -5.67200  5.43100   -38.95200 1.000 34.56381  ? 222 LEU A C   1 
ATOM   1705 O  O   . LEU A 1 222 ? -6.02800  4.71700   -38.01100 1.000 36.76579  ? 222 LEU A O   1 
ATOM   1706 C  CB  . LEU A 1 222 ? -6.64800  4.23600   -40.92000 1.000 35.06927  ? 222 LEU A CB  1 
ATOM   1707 C  CG  . LEU A 1 222 ? -6.52400  3.58000   -42.29200 1.000 42.71362  ? 222 LEU A CG  1 
ATOM   1708 C  CD1 . LEU A 1 222 ? -6.67700  2.05800   -42.17900 1.000 45.69997  ? 222 LEU A CD1 1 
ATOM   1709 C  CD2 . LEU A 1 222 ? -7.55400  4.15600   -43.25200 1.000 44.59410  ? 222 LEU A CD2 1 
ATOM   1710 N  N   . ALA A 1 223 ? -5.53900  6.74400   -38.86400 1.000 31.97373  ? 223 ALA A N   1 
ATOM   1711 C  CA  . ALA A 1 223 ? -5.91000  7.47100   -37.66700 1.000 33.47697  ? 223 ALA A CA  1 
ATOM   1712 C  C   . ALA A 1 223 ? -7.05900  8.41300   -37.98800 1.000 35.26559  ? 223 ALA A C   1 
ATOM   1713 O  O   . ALA A 1 223 ? -6.96100  9.24900   -38.89600 1.000 34.78500  ? 223 ALA A O   1 
ATOM   1714 C  CB  . ALA A 1 223 ? -4.72300  8.24500   -37.10200 1.000 27.62414  ? 223 ALA A CB  1 
HETATM 1715 C  C   . F2Y A 1 224 ? -9.31800  10.16800  -36.20800 1.000 31.18511  ? 224 F2Y A C   1 
HETATM 1716 O  O   . F2Y A 1 224 ? -9.41100  9.75300   -35.02100 1.000 30.02691  ? 224 F2Y A O   1 
HETATM 1717 C  CA  . F2Y A 1 224 ? -9.28900  9.13800   -37.37500 1.000 31.07536  ? 224 F2Y A CA  1 
HETATM 1718 N  N   . F2Y A 1 224 ? -8.14300  8.26600   -37.23500 1.000 28.91665  ? 224 F2Y A N   1 
HETATM 1719 C  CB  . F2Y A 1 224 ? -10.60700 8.33600   -37.43200 1.000 34.67438  ? 224 F2Y A CB  1 
HETATM 1720 C  CG  . F2Y A 1 224 ? -10.64300 7.37500   -38.58100 1.000 36.54127  ? 224 F2Y A CG  1 
HETATM 1721 C  CD1 . F2Y A 1 224 ? -9.85400  7.64400   -39.71400 1.000 38.30443  ? 224 F2Y A CD1 1 
HETATM 1722 C  CE1 . F2Y A 1 224 ? -9.85800  6.77100   -40.82100 1.000 43.97045  ? 224 F2Y A CE1 1 
HETATM 1723 F  F1  . F2Y A 1 224 ? -9.10500  7.02100   -41.92700 0.570 38.65994  ? 224 F2Y A F1  1 
HETATM 1724 C  CD2 . F2Y A 1 224 ? -11.42400 6.21400   -38.57100 1.000 38.21389  ? 224 F2Y A CD2 1 
HETATM 1725 C  CE2 . F2Y A 1 224 ? -11.42100 5.32500   -39.67000 1.000 38.38029  ? 224 F2Y A CE2 1 
HETATM 1726 F  F2  . F2Y A 1 224 ? -12.17000 4.20200   -39.64100 0.580 42.67696  ? 224 F2Y A F2  1 
HETATM 1727 C  CZ  . F2Y A 1 224 ? -10.64700 5.59900   -40.81400 1.000 43.37340  ? 224 F2Y A CZ  1 
HETATM 1728 O  OH  . F2Y A 1 224 ? -10.66400 4.71500   -41.88300 1.000 45.84115  ? 224 F2Y A OH  1 
ATOM   1729 N  N   . PHE A 1 225 ? -9.18100  11.45000  -36.53400 1.000 30.46784  ? 225 PHE A N   1 
ATOM   1730 C  CA  . PHE A 1 225 ? -9.26000  12.50800  -35.54500 1.000 29.46656  ? 225 PHE A CA  1 
ATOM   1731 C  C   . PHE A 1 225 ? -10.63300 13.18800  -35.61300 1.000 31.84528  ? 225 PHE A C   1 
ATOM   1732 O  O   . PHE A 1 225 ? -11.05200 13.66200  -36.67000 1.000 31.80557  ? 225 PHE A O   1 
ATOM   1733 C  CB  . PHE A 1 225 ? -8.14400  13.53200  -35.75800 1.000 30.56646  ? 225 PHE A CB  1 
ATOM   1734 C  CG  . PHE A 1 225 ? -6.77500  13.03500  -35.38400 1.000 32.21649  ? 225 PHE A CG  1 
ATOM   1735 C  CD1 . PHE A 1 225 ? -6.34100  13.08300  -34.06600 1.000 29.99258  ? 225 PHE A CD1 1 
ATOM   1736 C  CD2 . PHE A 1 225 ? -5.91700  12.53500  -36.35300 1.000 31.71725  ? 225 PHE A CD2 1 
ATOM   1737 C  CE1 . PHE A 1 225 ? -5.07900  12.65300  -33.72200 1.000 30.61158  ? 225 PHE A CE1 1 
ATOM   1738 C  CE2 . PHE A 1 225 ? -4.65100  12.08300  -36.01200 1.000 31.86408  ? 225 PHE A CE2 1 
ATOM   1739 C  CZ  . PHE A 1 225 ? -4.22400  12.15000  -34.70700 1.000 30.38752  ? 225 PHE A CZ  1 
ATOM   1740 N  N   . ASN A 1 226 ? -11.32800 13.24000  -34.48300 1.000 28.10568  ? 226 ASN A N   1 
ATOM   1741 C  CA  . ASN A 1 226 ? -12.68800 13.75200  -34.43800 1.000 26.54990  ? 226 ASN A CA  1 
ATOM   1742 C  C   . ASN A 1 226 ? -12.78400 14.91700  -33.46900 1.000 24.14525  ? 226 ASN A C   1 
ATOM   1743 O  O   . ASN A 1 226 ? -12.01400 15.00900  -32.50900 1.000 25.49639  ? 226 ASN A O   1 
ATOM   1744 C  CB  . ASN A 1 226 ? -13.68200 12.67100  -33.98600 1.000 25.67687  ? 226 ASN A CB  1 
ATOM   1745 C  CG  . ASN A 1 226 ? -13.96300 11.65100  -35.05500 1.000 29.91794  ? 226 ASN A CG  1 
ATOM   1746 O  OD1 . ASN A 1 226 ? -13.57700 11.81700  -36.22000 1.000 33.93442  ? 226 ASN A OD1 1 
ATOM   1747 N  ND2 . ASN A 1 226 ? -14.66700 10.60600  -34.67800 1.000 26.44798  ? 226 ASN A ND2 1 
ATOM   1748 N  N   . SER A 1 227 ? -13.78900 15.76400  -33.68700 1.000 24.59451  ? 227 SER A N   1 
ATOM   1749 C  CA  . SER A 1 227 ? -14.22000 16.68500  -32.64300 1.000 26.04988  ? 227 SER A CA  1 
ATOM   1750 C  C   . SER A 1 227 ? -14.41600 15.93000  -31.33200 1.000 24.58857  ? 227 SER A C   1 
ATOM   1751 O  O   . SER A 1 227 ? -14.92500 14.80300  -31.32100 1.000 23.01991  ? 227 SER A O   1 
ATOM   1752 C  CB  . SER A 1 227 ? -15.52600 17.37100  -33.04600 1.000 25.48660  ? 227 SER A CB  1 
ATOM   1753 O  OG  . SER A 1 227 ? -16.19100 17.94900  -31.91400 1.000 23.22221  ? 227 SER A OG  1 
ATOM   1754 N  N   . VAL A 1 228 ? -14.01100 16.55200  -30.22000 1.000 22.00388  ? 228 VAL A N   1 
ATOM   1755 C  CA  . VAL A 1 228 ? -14.22800 15.93200  -28.91500 1.000 22.23696  ? 228 VAL A CA  1 
ATOM   1756 C  C   . VAL A 1 228 ? -15.71200 15.81900  -28.56400 1.000 24.35439  ? 228 VAL A C   1 
ATOM   1757 O  O   . VAL A 1 228 ? -16.05900 15.17700  -27.56600 1.000 22.15929  ? 228 VAL A O   1 
ATOM   1758 C  CB  . VAL A 1 228 ? -13.47300 16.70400  -27.80800 1.000 23.98885  ? 228 VAL A CB  1 
ATOM   1759 C  CG1 . VAL A 1 228 ? -11.99100 16.73100  -28.11700 1.000 23.52350  ? 228 VAL A CG1 1 
ATOM   1760 C  CG2 . VAL A 1 228 ? -14.01900 18.14600  -27.65500 1.000 21.57680  ? 228 VAL A CG2 1 
ATOM   1761 N  N   . GLN A 1 229 ? -16.59600 16.42300  -29.36400 1.000 22.78348  ? 229 GLN A N   1 
ATOM   1762 C  CA  . GLN A 1 229 ? -18.02600 16.17800  -29.24400 1.000 23.76129  ? 229 GLN A CA  1 
ATOM   1763 C  C   . GLN A 1 229 ? -18.39100 14.74100  -29.56100 1.000 25.24188  ? 229 GLN A C   1 
ATOM   1764 O  O   . GLN A 1 229 ? -19.44900 14.27200  -29.11200 1.000 21.37462  ? 229 GLN A O   1 
ATOM   1765 C  CB  . GLN A 1 229 ? -18.79800 17.08100  -30.19200 1.000 23.58044  ? 229 GLN A CB  1 
ATOM   1766 C  CG  . GLN A 1 229 ? -18.62400 18.55600  -29.92600 1.000 26.20028  ? 229 GLN A CG  1 
ATOM   1767 C  CD  . GLN A 1 229 ? -19.41200 19.39200  -30.93300 1.000 26.98042  ? 229 GLN A CD  1 
ATOM   1768 O  OE1 . GLN A 1 229 ? -20.63900 19.45100  -30.88000 1.000 23.50234  ? 229 GLN A OE1 1 
ATOM   1769 N  NE2 . GLN A 1 229 ? -18.70600 20.01500  -31.86900 1.000 26.13248  ? 229 GLN A NE2 1 
ATOM   1770 N  N   . LEU A 1 230 ? -17.54200 14.05000  -30.32500 1.000 21.96948  ? 230 LEU A N   1 
ATOM   1771 C  CA  . LEU A 1 230 ? -17.81500 12.71700  -30.84400 1.000 25.12305  ? 230 LEU A CA  1 
ATOM   1772 C  C   . LEU A 1 230 ? -17.09300 11.66800  -30.01300 1.000 24.12823  ? 230 LEU A C   1 
ATOM   1773 O  O   . LEU A 1 230 ? -15.88100 11.77000  -29.78600 1.000 21.39919  ? 230 LEU A O   1 
ATOM   1774 C  CB  . LEU A 1 230 ? -17.37300 12.59500  -32.30500 1.000 24.12789  ? 230 LEU A CB  1 
ATOM   1775 C  CG  . LEU A 1 230 ? -18.17800 13.41300  -33.31500 1.000 26.74517  ? 230 LEU A CG  1 
ATOM   1776 C  CD1 . LEU A 1 230 ? -17.73300 13.12500  -34.74700 1.000 26.84984  ? 230 LEU A CD1 1 
ATOM   1777 C  CD2 . LEU A 1 230 ? -19.65700 13.10300  -33.12900 1.000 25.71394  ? 230 LEU A CD2 1 
ATOM   1778 N  N   . THR A 1 231 ? -17.82700 10.64000  -29.63000 1.000 25.40973  ? 231 THR A N   1 
ATOM   1779 C  CA  . THR A 1 231 ? -17.30700 9.63100   -28.73100 1.000 24.12312  ? 231 THR A CA  1 
ATOM   1780 C  C   . THR A 1 231 ? -16.22900 8.81300   -29.43100 1.000 23.40610  ? 231 THR A C   1 
ATOM   1781 O  O   . THR A 1 231 ? -16.45100 8.33600   -30.54500 1.000 25.36608  ? 231 THR A O   1 
ATOM   1782 C  CB  . THR A 1 231 ? -18.42400 8.72000   -28.27800 1.000 24.04077  ? 231 THR A CB  1 
ATOM   1783 O  OG1 . THR A 1 231 ? -19.43800 9.49900   -27.62100 1.000 25.54770  ? 231 THR A OG1 1 
ATOM   1784 C  CG2 . THR A 1 231 ? -17.87700 7.64500   -27.36000 1.000 21.97580  ? 231 THR A CG2 1 
ATOM   1785 N  N   . PRO A 1 232 ? -15.07000 8.61000   -28.80900 1.000 22.61223  ? 232 PRO A N   1 
ATOM   1786 C  CA  . PRO A 1 232 ? -14.01500 7.83500   -29.46700 1.000 26.37594  ? 232 PRO A CA  1 
ATOM   1787 C  C   . PRO A 1 232 ? -14.44800 6.38800   -29.66600 1.000 26.89466  ? 232 PRO A C   1 
ATOM   1788 O  O   . PRO A 1 232 ? -15.03400 5.76200   -28.77300 1.000 27.27441  ? 232 PRO A O   1 
ATOM   1789 C  CB  . PRO A 1 232 ? -12.82700 7.96300   -28.50700 1.000 26.78889  ? 232 PRO A CB  1 
ATOM   1790 C  CG  . PRO A 1 232 ? -13.11300 9.28400   -27.74100 1.000 25.29038  ? 232 PRO A CG  1 
ATOM   1791 C  CD  . PRO A 1 232 ? -14.59800 9.29400   -27.58500 1.000 22.85415  ? 232 PRO A CD  1 
ATOM   1792 N  N   . PHE A 1 233 ? -14.20400 5.88600   -30.87600 1.000 26.65833  ? 233 PHE A N   1 
ATOM   1793 C  CA  . PHE A 1 233 ? -14.47700 4.48400   -31.18000 1.000 29.67349  ? 233 PHE A CA  1 
ATOM   1794 C  C   . PHE A 1 233 ? -13.69100 3.57300   -30.24200 1.000 29.14384  ? 233 PHE A C   1 
ATOM   1795 O  O   . PHE A 1 233 ? -14.26400 2.68700   -29.59800 1.000 30.91614  ? 233 PHE A O   1 
ATOM   1796 C  CB  . PHE A 1 233 ? -14.13800 4.20400   -32.65000 1.000 28.76728  ? 233 PHE A CB  1 
ATOM   1797 C  CG  . PHE A 1 233 ? -14.27800 2.75100   -33.06300 1.000 30.81927  ? 233 PHE A CG  1 
ATOM   1798 C  CD1 . PHE A 1 233 ? -15.53400 2.18500   -33.26400 1.000 32.09549  ? 233 PHE A CD1 1 
ATOM   1799 C  CD2 . PHE A 1 233 ? -13.15700 1.97000   -33.29200 1.000 29.13922  ? 233 PHE A CD2 1 
ATOM   1800 C  CE1 . PHE A 1 233 ? -15.67000 0.85700   -33.66200 1.000 32.86421  ? 233 PHE A CE1 1 
ATOM   1801 C  CE2 . PHE A 1 233 ? -13.27800 0.63600   -33.68900 1.000 31.31144  ? 233 PHE A CE2 1 
ATOM   1802 C  CZ  . PHE A 1 233 ? -14.53900 0.07300   -33.87300 1.000 32.90009  ? 233 PHE A CZ  1 
ATOM   1803 N  N   . GLU A 1 234 ? -12.38700 3.81100   -30.12500 1.000 29.22284  ? 234 GLU A N   1 
ATOM   1804 C  CA  . GLU A 1 234 ? -11.50200 3.12800   -29.18800 1.000 30.67533  ? 234 GLU A CA  1 
ATOM   1805 C  C   . GLU A 1 234 ? -11.38200 3.96300   -27.92000 1.000 29.36771  ? 234 GLU A C   1 
ATOM   1806 O  O   . GLU A 1 234 ? -11.05300 5.15200   -27.99200 1.000 29.44210  ? 234 GLU A O   1 
ATOM   1807 C  CB  . GLU A 1 234 ? -10.10800 2.91900   -29.80400 1.000 31.13592  ? 234 GLU A CB  1 
ATOM   1808 C  CG  . GLU A 1 234 ? -10.09300 1.92700   -30.97800 1.000 35.21057  ? 234 GLU A CG  1 
ATOM   1809 C  CD  . GLU A 1 234 ? -8.83600  1.98800   -31.89700 1.000 38.39170  ? 234 GLU A CD  1 
ATOM   1810 O  OE1 . GLU A 1 234 ? -8.02600  2.95700   -31.82900 1.000 36.36736  ? 234 GLU A OE1 1 
ATOM   1811 O  OE2 . GLU A 1 234 ? -8.67200  1.03200   -32.70300 1.000 37.42300  ? 234 GLU A OE2 1 
ATOM   1812 N  N   . THR A 1 235 ? -11.64500 3.35200   -26.76700 1.000 29.51541  ? 235 THR A N   1 
ATOM   1813 C  CA  . THR A 1 235 ? -11.42600 4.02000   -25.48800 1.000 29.82202  ? 235 THR A CA  1 
ATOM   1814 C  C   . THR A 1 235 ? -10.07600 3.59600   -24.91500 1.000 31.24418  ? 235 THR A C   1 
ATOM   1815 O  O   . THR A 1 235 ? -9.79400  2.39300   -24.78100 1.000 31.56123  ? 235 THR A O   1 
ATOM   1816 C  CB  . THR A 1 235 ? -12.55100 3.72700   -24.48700 1.000 31.20715  ? 235 THR A CB  1 
ATOM   1817 O  OG1 . THR A 1 235 ? -12.22200 4.32800   -23.22400 1.000 32.23756  ? 235 THR A OG1 1 
ATOM   1818 C  CG2 . THR A 1 235 ? -12.75700 2.24000   -24.30200 1.000 28.47490  ? 235 THR A CG2 1 
ATOM   1819 N  N   . TYR A 1 236 ? -9.24700  4.58800   -24.58700 1.000 27.52649  ? 236 TYR A N   1 
ATOM   1820 C  CA  . TYR A 1 236 ? -7.89500  4.38000   -24.08200 1.000 28.57439  ? 236 TYR A CA  1 
ATOM   1821 C  C   . TYR A 1 236 ? -7.84400  4.41000   -22.56300 1.000 30.39355  ? 236 TYR A C   1 
ATOM   1822 O  O   . TYR A 1 236 ? -6.76200  4.51000   -21.97800 1.000 30.19641  ? 236 TYR A O   1 
ATOM   1823 C  CB  . TYR A 1 236 ? -6.94500  5.41400   -24.70600 1.000 29.25388  ? 236 TYR A CB  1 
ATOM   1824 C  CG  . TYR A 1 236 ? -6.88000  5.22000   -26.21800 1.000 34.78235  ? 236 TYR A CG  1 
ATOM   1825 C  CD1 . TYR A 1 236 ? -6.07600  4.21400   -26.76000 1.000 36.97386  ? 236 TYR A CD1 1 
ATOM   1826 C  CD2 . TYR A 1 236 ? -7.65500  6.00400   -27.06800 1.000 35.05532  ? 236 TYR A CD2 1 
ATOM   1827 C  CE1 . TYR A 1 236 ? -6.03900  4.03100   -28.12100 1.000 39.22251  ? 236 TYR A CE1 1 
ATOM   1828 C  CE2 . TYR A 1 236 ? -7.59300  5.79200   -28.42500 1.000 37.29958  ? 236 TYR A CE2 1 
ATOM   1829 C  CZ  . TYR A 1 236 ? -6.79500  4.80800   -28.98600 1.000 38.27355  ? 236 TYR A CZ  1 
ATOM   1830 O  OH  . TYR A 1 236 ? -6.76300  4.62800   -30.32600 1.000 43.61450  ? 236 TYR A OH  1 
ATOM   1831 N  N   . ARG A 1 237 ? -9.00000  4.24800   -21.91900 1.000 30.98960  ? 237 ARG A N   1 
ATOM   1832 C  CA  . ARG A 1 237 ? -9.13300  4.38700   -20.47800 1.000 31.11732  ? 237 ARG A CA  1 
ATOM   1833 C  C   . ARG A 1 237 ? -8.52200  3.23800   -19.69100 1.000 31.98290  ? 237 ARG A C   1 
ATOM   1834 O  O   . ARG A 1 237 ? -8.41000  3.35700   -18.47000 1.000 33.27495  ? 237 ARG A O   1 
ATOM   1835 C  CB  . ARG A 1 237 ? -10.60400 4.51700   -20.10800 1.000 31.68459  ? 237 ARG A CB  1 
ATOM   1836 C  CG  . ARG A 1 237 ? -11.42300 3.26800   -20.35300 1.000 30.10295  ? 237 ARG A CG  1 
ATOM   1837 C  CD  . ARG A 1 237 ? -12.92100 3.60400   -20.37100 1.000 30.74712  ? 237 ARG A CD  1 
ATOM   1838 N  NE  . ARG A 1 237 ? -13.47200 3.61100   -19.02400 1.000 38.82271  ? 237 ARG A NE  1 
ATOM   1839 C  CZ  . ARG A 1 237 ? -14.68800 4.03700   -18.70800 1.000 34.89651  ? 237 ARG A CZ  1 
ATOM   1840 N  NH1 . ARG A 1 237 ? -15.49100 4.57500   -19.61600 1.000 34.20418  ? 237 ARG A NH1 1 
ATOM   1841 N  NH2 . ARG A 1 237 ? -15.10900 3.91700   -17.45100 1.000 36.32838  ? 237 ARG A NH2 1 
ATOM   1842 N  N   . THR A 1 238 ? -8.14000  2.13200   -20.33000 1.000 33.82832  ? 238 THR A N   1 
ATOM   1843 C  CA  . THR A 1 238 ? -7.50400  1.04200   -19.60800 1.000 35.32696  ? 238 THR A CA  1 
ATOM   1844 C  C   . THR A 1 238 ? -5.99600  1.07400   -19.73300 1.000 35.79096  ? 238 THR A C   1 
ATOM   1845 O  O   . THR A 1 238 ? -5.32900  0.14400   -19.27200 1.000 38.43743  ? 238 THR A O   1 
ATOM   1846 C  CB  . THR A 1 238 ? -8.02000  -0.32100  -20.07400 1.000 35.78353  ? 238 THR A CB  1 
ATOM   1847 O  OG1 . THR A 1 238 ? -7.57400  -0.57900  -21.41200 1.000 37.76639  ? 238 THR A OG1 1 
ATOM   1848 C  CG2 . THR A 1 238 ? -9.53900  -0.37600  -20.00100 1.000 37.27025  ? 238 THR A CG2 1 
ATOM   1849 N  N   . MET A 1 239 ? -5.44800  2.09700   -20.36700 1.000 34.11299  ? 239 MET A N   1 
ATOM   1850 C  CA  . MET A 1 239 ? -4.00900  2.27900   -20.33900 1.000 38.23386  ? 239 MET A CA  1 
ATOM   1851 C  C   . MET A 1 239 ? -3.54000  2.39400   -18.89200 1.000 36.50527  ? 239 MET A C   1 
ATOM   1852 O  O   . MET A 1 239 ? -4.20700  3.04000   -18.07800 1.000 36.05883  ? 239 MET A O   1 
ATOM   1853 C  CB  . MET A 1 239 ? -3.61400  3.52900   -21.11900 1.000 35.63797  ? 239 MET A CB  1 
ATOM   1854 C  CG  . MET A 1 239 ? -3.70100  3.35400   -22.60100 1.000 37.91156  ? 239 MET A CG  1 
ATOM   1855 S  SD  . MET A 1 239 ? -3.26300  4.88500   -23.43600 1.000 46.40294  ? 239 MET A SD  1 
ATOM   1856 C  CE  . MET A 1 239 ? -1.69000  5.20200   -22.64100 1.000 33.93178  ? 239 MET A CE  1 
ATOM   1857 N  N   . PRO A 1 240 ? -2.41900  1.76300   -18.53200 1.000 40.74361  ? 240 PRO A N   1 
ATOM   1858 C  CA  . PRO A 1 240 ? -1.89300  1.91800   -17.16600 1.000 40.21374  ? 240 PRO A CA  1 
ATOM   1859 C  C   . PRO A 1 240 ? -1.43900  3.34700   -16.90500 1.000 41.78177  ? 240 PRO A C   1 
ATOM   1860 O  O   . PRO A 1 240 ? -1.05200  4.08300   -17.81800 1.000 39.59721  ? 240 PRO A O   1 
ATOM   1861 C  CB  . PRO A 1 240 ? -0.70900  0.94500   -17.12200 1.000 41.08620  ? 240 PRO A CB  1 
ATOM   1862 C  CG  . PRO A 1 240 ? -0.89000  0.04900   -18.29500 1.000 41.69060  ? 240 PRO A CG  1 
ATOM   1863 C  CD  . PRO A 1 240 ? -1.63900  0.80700   -19.33200 1.000 36.45761  ? 240 PRO A CD  1 
ATOM   1864 N  N   . ARG A 1 241 ? -1.48900  3.73200   -15.63000 1.000 41.20237  ? 241 ARG A N   1 
ATOM   1865 C  CA  . ARG A 1 241 ? -1.14300  5.09700   -15.26000 1.000 42.17690  ? 241 ARG A CA  1 
ATOM   1866 C  C   . ARG A 1 241 ? 0.29700   5.43500   -15.64400 1.000 43.88379  ? 241 ARG A C   1 
ATOM   1867 O  O   . ARG A 1 241 ? 0.56900   6.54500   -16.11600 1.000 44.90444  ? 241 ARG A O   1 
ATOM   1868 C  CB  . ARG A 1 241 ? -1.37300  5.29900   -13.76300 1.000 42.68723  ? 241 ARG A CB  1 
ATOM   1869 C  CG  . ARG A 1 241 ? -1.11200  6.70400   -13.28000 1.000 44.50146  ? 241 ARG A CG  1 
ATOM   1870 C  CD  . ARG A 1 241 ? -1.43700  6.82600   -11.79600 1.000 49.84533  ? 241 ARG A CD  1 
ATOM   1871 N  NE  . ARG A 1 241 ? -1.32700  8.20100   -11.33400 1.000 50.11173  ? 241 ARG A NE  1 
ATOM   1872 C  CZ  . ARG A 1 241 ? -2.31900  9.07900   -11.35000 1.000 47.46074  ? 241 ARG A CZ  1 
ATOM   1873 N  NH1 . ARG A 1 241 ? -3.53800  8.74200   -11.74600 1.000 49.63675  ? 241 ARG A NH1 1 
ATOM   1874 N  NH2 . ARG A 1 241 ? -2.08000  10.33100  -10.97400 1.000 44.17966  ? 241 ARG A NH2 1 
ATOM   1875 N  N   . GLU A 1 242 ? 1.23400   4.49500   -15.45200 1.000 42.33459  ? 242 GLU A N   1 
ATOM   1876 C  CA  . GLU A 1 242 ? 2.62000   4.75000   -15.85200 1.000 47.32502  ? 242 GLU A CA  1 
ATOM   1877 C  C   . GLU A 1 242 ? 2.71500   5.04900   -17.34300 1.000 42.00919  ? 242 GLU A C   1 
ATOM   1878 O  O   . GLU A 1 242 ? 3.42200   5.97700   -17.75200 1.000 41.95444  ? 242 GLU A O   1 
ATOM   1879 C  CB  . GLU A 1 242 ? 3.52700   3.56300   -15.50700 1.000 47.95653  ? 242 GLU A CB  1 
ATOM   1880 C  CG  . GLU A 1 242 ? 3.13900   2.79100   -14.25800 1.000 58.48794  ? 242 GLU A CG  1 
ATOM   1881 C  CD  . GLU A 1 242 ? 2.15200   1.65300   -14.55500 1.000 64.14023  ? 242 GLU A CD  1 
ATOM   1882 O  OE1 . GLU A 1 242 ? 2.54000   0.69000   -15.27700 1.000 64.29081  ? 242 GLU A OE1 1 
ATOM   1883 O  OE2 . GLU A 1 242 ? 0.99100   1.73500   -14.07400 1.000 56.58808  ? 242 GLU A OE2 1 
ATOM   1884 N  N   . MET A 1 243 ? 2.01500   4.26800   -18.16800 1.000 41.04360  ? 243 MET A N   1 
ATOM   1885 C  CA  . MET A 1 243 ? 1.98500   4.53900   -19.59900 1.000 39.72006  ? 243 MET A CA  1 
ATOM   1886 C  C   . MET A 1 243 ? 1.34700   5.89300   -19.90300 1.000 40.63217  ? 243 MET A C   1 
ATOM   1887 O  O   . MET A 1 243 ? 1.86500   6.64800   -20.73200 1.000 41.22045  ? 243 MET A O   1 
ATOM   1888 C  CB  . MET A 1 243 ? 1.24900   3.41800   -20.33100 1.000 41.52177  ? 243 MET A CB  1 
ATOM   1889 C  CG  . MET A 1 243 ? 1.29200   3.54500   -21.86000 1.000 42.80544  ? 243 MET A CG  1 
ATOM   1890 S  SD  . MET A 1 243 ? 0.47900   2.16800   -22.71500 1.000 46.99023  ? 243 MET A SD  1 
ATOM   1891 C  CE  . MET A 1 243 ? 1.67800   0.84100   -22.43600 1.000 38.89590  ? 243 MET A CE  1 
ATOM   1892 N  N   . VAL A 1 244 ? 0.21900   6.22200   -19.25300 1.000 37.45236  ? 244 VAL A N   1 
ATOM   1893 C  CA  . VAL A 1 244 ? -0.42000  7.51100   -19.53100 1.000 38.05214  ? 244 VAL A CA  1 
ATOM   1894 C  C   . VAL A 1 244 ? 0.49000   8.66500   -19.12000 1.000 36.65382  ? 244 VAL A C   1 
ATOM   1895 O  O   . VAL A 1 244 ? 0.63000   9.64900   -19.85200 1.000 35.17734  ? 244 VAL A O   1 
ATOM   1896 C  CB  . VAL A 1 244 ? -1.79600  7.61600   -18.84500 1.000 37.65862  ? 244 VAL A CB  1 
ATOM   1897 C  CG1 . VAL A 1 244 ? -2.36400  9.02800   -19.00800 1.000 33.13567  ? 244 VAL A CG1 1 
ATOM   1898 C  CG2 . VAL A 1 244 ? -2.75000  6.61000   -19.43600 1.000 37.19406  ? 244 VAL A CG2 1 
ATOM   1899 N  N   . GLU A 1 245 ? 1.13600   8.56000   -17.95600 1.000 38.48907  ? 245 GLU A N   1 
ATOM   1900 C  CA  . GLU A 1 245 ? 1.93900   9.66800   -17.44300 1.000 38.76358  ? 245 GLU A CA  1 
ATOM   1901 C  C   . GLU A 1 245 ? 3.30800   9.77700   -18.11500 1.000 39.81277  ? 245 GLU A C   1 
ATOM   1902 O  O   . GLU A 1 245 ? 4.00700   10.77800  -17.91600 1.000 39.63502  ? 245 GLU A O   1 
ATOM   1903 C  CB  . GLU A 1 245 ? 2.09000   9.54500   -15.92100 1.000 39.56137  ? 245 GLU A CB  1 
ATOM   1904 C  CG  . GLU A 1 245 ? 0.75500   9.72500   -15.17300 1.000 41.04036  ? 245 GLU A CG  1 
ATOM   1905 C  CD  . GLU A 1 245 ? 0.90700   9.72600   -13.64900 1.000 47.10090  ? 245 GLU A CD  1 
ATOM   1906 O  OE1 . GLU A 1 245 ? 1.77300   8.98800   -13.11800 1.000 49.38881  ? 245 GLU A OE1 1 
ATOM   1907 O  OE2 . GLU A 1 245 ? 0.15500   10.47200  -12.97800 1.000 46.03527  ? 245 GLU A OE2 1 
ATOM   1908 N  N   . SER A 1 246 ? 3.70300   8.78600   -18.91200 1.000 37.69794  ? 246 SER A N   1 
ATOM   1909 C  CA  . SER A 1 246 ? 4.88900   8.92500   -19.74200 1.000 38.59414  ? 246 SER A CA  1 
ATOM   1910 C  C   . SER A 1 246 ? 4.61900   9.73900   -20.99900 1.000 38.02952  ? 246 SER A C   1 
ATOM   1911 O  O   . SER A 1 246 ? 5.57000   10.17000  -21.65400 1.000 38.45822  ? 246 SER A O   1 
ATOM   1912 C  CB  . SER A 1 246 ? 5.42800   7.54900   -20.14000 1.000 39.85968  ? 246 SER A CB  1 
ATOM   1913 O  OG  . SER A 1 246 ? 4.62300   7.00600   -21.18000 1.000 43.46113  ? 246 SER A OG  1 
ATOM   1914 N  N   . MET A 1 247 ? 3.35700   9.96800   -21.34500 1.000 36.92667  ? 247 MET A N   1 
ATOM   1915 C  CA  . MET A 1 247 ? 3.04200   10.71400  -22.55100 1.000 37.35750  ? 247 MET A CA  1 
ATOM   1916 C  C   . MET A 1 247 ? 3.07500   12.21800  -22.28700 1.000 36.98098  ? 247 MET A C   1 
ATOM   1917 O  O   . MET A 1 247 ? 3.04900   12.67900  -21.14600 1.000 35.53031  ? 247 MET A O   1 
ATOM   1918 C  CB  . MET A 1 247 ? 1.66600   10.32300  -23.08500 1.000 33.98656  ? 247 MET A CB  1 
ATOM   1919 C  CG  . MET A 1 247 ? 1.52700   8.86000   -23.40300 1.000 36.44924  ? 247 MET A CG  1 
ATOM   1920 S  SD  . MET A 1 247 ? -0.04900  8.59500   -24.23000 1.000 37.68856  ? 247 MET A SD  1 
ATOM   1921 C  CE  . MET A 1 247 ? -1.19900  8.91300   -22.87500 1.000 33.06373  ? 247 MET A CE  1 
ATOM   1922 N  N   . THR A 1 248 ? 3.11200   12.98300  -23.37000 1.000 34.53948  ? 248 THR A N   1 
ATOM   1923 C  CA  . THR A 1 248 ? 3.00600   14.42600  -23.27400 1.000 34.06013  ? 248 THR A CA  1 
ATOM   1924 C  C   . THR A 1 248 ? 1.55600   14.83400  -23.00700 1.000 32.35778  ? 248 THR A C   1 
ATOM   1925 O  O   . THR A 1 248 ? 0.62700   14.04200  -23.14500 1.000 29.05679  ? 248 THR A O   1 
ATOM   1926 C  CB  . THR A 1 248 ? 3.49500   15.07600  -24.56500 1.000 34.44471  ? 248 THR A CB  1 
ATOM   1927 O  OG1 . THR A 1 248 ? 2.71300   14.58200  -25.66000 1.000 31.06014  ? 248 THR A OG1 1 
ATOM   1928 C  CG2 . THR A 1 248 ? 4.94600   14.74600  -24.81100 1.000 35.55478  ? 248 THR A CG2 1 
ATOM   1929 N  N   . VAL A 1 249 ? 1.37000   16.10500  -22.62900 1.000 32.94101  ? 249 VAL A N   1 
ATOM   1930 C  CA  . VAL A 1 249 ? 0.01600   16.63800  -22.45100 1.000 33.14165  ? 249 VAL A CA  1 
ATOM   1931 C  C   . VAL A 1 249 ? -0.79900  16.43500  -23.72100 1.000 30.22039  ? 249 VAL A C   1 
ATOM   1932 O  O   . VAL A 1 249 ? -1.93500  15.93800  -23.68600 1.000 30.46278  ? 249 VAL A O   1 
ATOM   1933 C  CB  . VAL A 1 249 ? 0.06800   18.12600  -22.04900 1.000 34.69278  ? 249 VAL A CB  1 
ATOM   1934 C  CG1 . VAL A 1 249 ? -1.30900  18.77900  -22.19400 1.000 32.33953  ? 249 VAL A CG1 1 
ATOM   1935 C  CG2 . VAL A 1 249 ? 0.58300   18.28100  -20.60300 1.000 35.46360  ? 249 VAL A CG2 1 
ATOM   1936 N  N   . LEU A 1 250 ? -0.22200  16.80200  -24.86400 1.000 29.29952  ? 250 LEU A N   1 
ATOM   1937 C  CA  . LEU A 1 250 ? -0.90200  16.61500  -26.13900 1.000 28.42724  ? 250 LEU A CA  1 
ATOM   1938 C  C   . LEU A 1 250 ? -1.29300  15.14900  -26.34800 1.000 29.37592  ? 250 LEU A C   1 
ATOM   1939 O  O   . LEU A 1 250 ? -2.43100  14.84500  -26.73300 1.000 30.06988  ? 250 LEU A O   1 
ATOM   1940 C  CB  . LEU A 1 250 ? -0.00300  17.13400  -27.27200 1.000 32.96281  ? 250 LEU A CB  1 
ATOM   1941 C  CG  . LEU A 1 250 ? -0.50300  16.87900  -28.70100 1.000 33.84092  ? 250 LEU A CG  1 
ATOM   1942 C  CD1 . LEU A 1 250 ? -1.83700  17.56000  -28.92100 1.000 30.07546  ? 250 LEU A CD1 1 
ATOM   1943 C  CD2 . LEU A 1 250 ? 0.54400   17.32200  -29.71700 1.000 32.79227  ? 250 LEU A CD2 1 
ATOM   1944 N  N   . GLY A 1 251 ? -0.38400  14.21800  -26.05400 1.000 28.73314  ? 251 GLY A N   1 
ATOM   1945 C  CA  . GLY A 1 251 ? -0.73500  12.80500  -26.18300 1.000 30.06950  ? 251 GLY A CA  1 
ATOM   1946 C  C   . GLY A 1 251 ? -1.90500  12.40400  -25.29300 1.000 29.01524  ? 251 GLY A C   1 
ATOM   1947 O  O   . GLY A 1 251 ? -2.83800  11.72200  -25.73400 1.000 29.26478  ? 251 GLY A O   1 
ATOM   1948 N  N   . GLN A 1 252 ? -1.87600  12.84200  -24.02900 1.000 29.89242  ? 252 GLN A N   1 
ATOM   1949 C  CA  . GLN A 1 252 ? -2.96300  12.54900  -23.09500 1.000 31.18716  ? 252 GLN A CA  1 
ATOM   1950 C  C   . GLN A 1 252 ? -4.29800  13.10900  -23.58500 1.000 26.88717  ? 252 GLN A C   1 
ATOM   1951 O  O   . GLN A 1 252 ? -5.34100  12.46600  -23.42900 1.000 26.45845  ? 252 GLN A O   1 
ATOM   1952 C  CB  . GLN A 1 252 ? -2.61800  13.09800  -21.71000 1.000 28.11721  ? 252 GLN A CB  1 
ATOM   1953 C  CG  . GLN A 1 252 ? -1.39900  12.42500  -21.06700 1.000 29.11824  ? 252 GLN A CG  1 
ATOM   1954 C  CD  . GLN A 1 252 ? -1.02500  13.02900  -19.71900 1.000 31.43497  ? 252 GLN A CD  1 
ATOM   1955 O  OE1 . GLN A 1 252 ? -1.56600  14.06100  -19.31200 1.000 33.81977  ? 252 GLN A OE1 1 
ATOM   1956 N  NE2 . GLN A 1 252 ? -0.11100  12.38100  -19.01500 1.000 29.98785  ? 252 GLN A NE2 1 
ATOM   1957 N  N   . ARG A 1 253 ? -4.28000  14.30400  -24.17900 1.000 28.39238  ? 253 ARG A N   1 
ATOM   1958 C  CA  . ARG A 1 253 ? -5.49800  14.89900  -24.72800 1.000 28.20428  ? 253 ARG A CA  1 
ATOM   1959 C  C   . ARG A 1 253 ? -6.04200  14.07700  -25.89300 1.000 25.71057  ? 253 ARG A C   1 
ATOM   1960 O  O   . ARG A 1 253 ? -7.25000  13.80900  -25.96300 1.000 24.82880  ? 253 ARG A O   1 
ATOM   1961 C  CB  . ARG A 1 253 ? -5.22000  16.34800  -25.15900 1.000 27.03241  ? 253 ARG A CB  1 
ATOM   1962 C  CG  . ARG A 1 253 ? -4.96000  17.26700  -23.96200 1.000 28.49128  ? 253 ARG A CG  1 
ATOM   1963 C  CD  . ARG A 1 253 ? -4.52300  18.69600  -24.33700 1.000 28.25418  ? 253 ARG A CD  1 
ATOM   1964 N  NE  . ARG A 1 253 ? -5.63500  19.48400  -24.85200 1.000 31.89703  ? 253 ARG A NE  1 
ATOM   1965 C  CZ  . ARG A 1 253 ? -5.82800  19.74200  -26.13800 1.000 36.36753  ? 253 ARG A CZ  1 
ATOM   1966 N  NH1 . ARG A 1 253 ? -4.92500  19.40600  -27.04700 1.000 34.81528  ? 253 ARG A NH1 1 
ATOM   1967 N  NH2 . ARG A 1 253 ? -6.94300  20.36500  -26.52000 1.000 32.62780  ? 253 ARG A NH2 1 
ATOM   1968 N  N   . MET A 1 254 ? -5.16500  13.65300  -26.81100 1.000 27.59366  ? 254 MET A N   1 
ATOM   1969 C  CA  . MET A 1 254 ? -5.61900  12.86100  -27.95300 1.000 25.78681  ? 254 MET A CA  1 
ATOM   1970 C  C   . MET A 1 254 ? -6.27000  11.55600  -27.51100 1.000 24.68679  ? 254 MET A C   1 
ATOM   1971 O  O   . MET A 1 254 ? -7.18000  11.07000  -28.18400 1.000 25.05433  ? 254 MET A O   1 
ATOM   1972 C  CB  . MET A 1 254 ? -4.45800  12.57100  -28.90200 1.000 26.86939  ? 254 MET A CB  1 
ATOM   1973 C  CG  . MET A 1 254 ? -3.92400  13.79500  -29.61000 1.000 28.65036  ? 254 MET A CG  1 
ATOM   1974 S  SD  . MET A 1 254 ? -5.23400  14.65200  -30.51000 1.000 27.86615  ? 254 MET A SD  1 
ATOM   1975 C  CE  . MET A 1 254 ? -5.40100  16.10700  -29.47300 1.000 28.41823  ? 254 MET A CE  1 
ATOM   1976 N  N   . LEU A 1 255 ? -5.84100  10.98600  -26.38100 1.000 25.03288  ? 255 LEU A N   1 
ATOM   1977 C  CA  . LEU A 1 255 ? -6.30000  9.67200   -25.94900 1.000 25.99045  ? 255 LEU A CA  1 
ATOM   1978 C  C   . LEU A 1 255 ? -7.38100  9.73900   -24.86700 1.000 24.81699  ? 255 LEU A C   1 
ATOM   1979 O  O   . LEU A 1 255 ? -7.65200  8.72700   -24.20600 1.000 26.59011  ? 255 LEU A O   1 
ATOM   1980 C  CB  . LEU A 1 255 ? -5.11300  8.82200   -25.48100 1.000 28.04273  ? 255 LEU A CB  1 
ATOM   1981 C  CG  . LEU A 1 255 ? -4.02600  8.56200   -26.54000 1.000 28.52306  ? 255 LEU A CG  1 
ATOM   1982 C  CD1 . LEU A 1 255 ? -3.00800  7.57400   -26.04000 1.000 28.05430  ? 255 LEU A CD1 1 
ATOM   1983 C  CD2 . LEU A 1 255 ? -4.60400  8.11400   -27.89000 1.000 28.30210  ? 255 LEU A CD2 1 
ATOM   1984 N  N   . GLY A 1 256 ? -8.02500  10.89200  -24.69000 1.000 23.17648  ? 256 GLY A N   1 
ATOM   1985 C  CA  . GLY A 1 256 ? -9.19300  10.97200  -23.83600 1.000 25.21260  ? 256 GLY A CA  1 
ATOM   1986 C  C   . GLY A 1 256 ? -8.93900  11.08600  -22.34900 1.000 26.57322  ? 256 GLY A C   1 
ATOM   1987 O  O   . GLY A 1 256 ? -9.88900  10.95700  -21.56900 1.000 26.26847  ? 256 GLY A O   1 
ATOM   1988 N  N   . TRP A 1 257 ? -7.70700  11.36200  -21.92500 1.000 26.39822  ? 257 TRP A N   1 
ATOM   1989 C  CA  . TRP A 1 257 ? -7.37700  11.40600  -20.50700 1.000 27.79555  ? 257 TRP A CA  1 
ATOM   1990 C  C   . TRP A 1 257 ? -7.48700  12.79600  -19.90700 1.000 27.68918  ? 257 TRP A C   1 
ATOM   1991 O  O   . TRP A 1 257 ? -7.15800  12.96800  -18.72900 1.000 27.49903  ? 257 TRP A O   1 
ATOM   1992 C  CB  . TRP A 1 257 ? -5.97000  10.86400  -20.27700 1.000 26.84067  ? 257 TRP A CB  1 
ATOM   1993 C  CG  . TRP A 1 257 ? -5.96500  9.38600   -20.34300 1.000 30.98498  ? 257 TRP A CG  1 
ATOM   1994 C  CD1 . TRP A 1 257 ? -5.79000  8.62200   -21.44900 1.000 30.26322  ? 257 TRP A CD1 1 
ATOM   1995 C  CD2 . TRP A 1 257 ? -6.19400  8.48200   -19.25700 1.000 33.30744  ? 257 TRP A CD2 1 
ATOM   1996 N  NE1 . TRP A 1 257 ? -5.88500  7.28700   -21.12400 1.000 32.01716  ? 257 TRP A NE1 1 
ATOM   1997 C  CE2 . TRP A 1 257 ? -6.13400  7.17600   -19.78200 1.000 31.26062  ? 257 TRP A CE2 1 
ATOM   1998 C  CE3 . TRP A 1 257 ? -6.45500  8.65200   -17.89600 1.000 34.62811  ? 257 TRP A CE3 1 
ATOM   1999 C  CZ2 . TRP A 1 257 ? -6.30000  6.03700   -18.98900 1.000 33.21728  ? 257 TRP A CZ2 1 
ATOM   2000 C  CZ3 . TRP A 1 257 ? -6.62500  7.51700   -17.10000 1.000 39.99293  ? 257 TRP A CZ3 1 
ATOM   2001 C  CH2 . TRP A 1 257 ? -6.54400  6.22400   -17.65200 1.000 37.66315  ? 257 TRP A CH2 1 
ATOM   2002 N  N   . ARG A 1 258 ? -7.94600  13.77800  -20.67700 1.000 24.14645  ? 258 ARG A N   1 
ATOM   2003 C  CA  . ARG A 1 258 ? -8.04700  15.14200  -20.19700 1.000 24.51813  ? 258 ARG A CA  1 
ATOM   2004 C  C   . ARG A 1 258 ? -9.38100  15.75500  -20.60500 1.000 27.19241  ? 258 ARG A C   1 
ATOM   2005 O  O   . ARG A 1 258 ? -10.02600 15.34400  -21.57400 1.000 26.35702  ? 258 ARG A O   1 
ATOM   2006 C  CB  . ARG A 1 258 ? -6.88700  16.00700  -20.71900 1.000 26.67276  ? 258 ARG A CB  1 
ATOM   2007 C  CG  . ARG A 1 258 ? -5.55500  15.55200  -20.14500 1.000 30.49273  ? 258 ARG A CG  1 
ATOM   2008 C  CD  . ARG A 1 258 ? -4.40700  16.52600  -20.37300 1.000 31.71865  ? 258 ARG A CD  1 
ATOM   2009 N  NE  . ARG A 1 258 ? -3.28000  16.10600  -19.55000 1.000 28.70697  ? 258 ARG A NE  1 
ATOM   2010 C  CZ  . ARG A 1 258 ? -2.70700  16.85300  -18.62300 1.000 33.15716  ? 258 ARG A CZ  1 
ATOM   2011 N  NH1 . ARG A 1 258 ? -3.01900  18.13300  -18.48100 1.000 33.17354  ? 258 ARG A NH1 1 
ATOM   2012 N  NH2 . ARG A 1 258 ? -1.80400  16.30000  -17.81100 1.000 31.62823  ? 258 ARG A NH2 1 
ATOM   2013 N  N   . THR A 1 259 ? -9.78200  16.75900  -19.83900 1.000 24.46588  ? 259 THR A N   1 
ATOM   2014 C  CA  . THR A 1 259 ? -10.94700 17.55000  -20.19400 1.000 27.96027  ? 259 THR A CA  1 
ATOM   2015 C  C   . THR A 1 259 ? -10.64600 18.39200  -21.43200 1.000 27.68296  ? 259 THR A C   1 
ATOM   2016 O  O   . THR A 1 259 ? -9.54600  18.91500  -21.58000 1.000 24.86618  ? 259 THR A O   1 
ATOM   2017 C  CB  . THR A 1 259 ? -11.31900 18.43000  -19.00300 1.000 29.09260  ? 259 THR A CB  1 
ATOM   2018 O  OG1 . THR A 1 259 ? -11.77200 17.58400  -17.93500 1.000 26.98745  ? 259 THR A OG1 1 
ATOM   2019 C  CG2 . THR A 1 259 ? -12.38600 19.45400  -19.38300 1.000 26.82106  ? 259 THR A CG2 1 
ATOM   2020 N  N   . MET A 1 260 ? -11.61900 18.49700  -22.33600 1.000 25.53659  ? 260 MET A N   1 
ATOM   2021 C  CA  . MET A 1 260 ? -11.43200 19.16200  -23.61800 1.000 24.90229  ? 260 MET A CA  1 
ATOM   2022 C  C   . MET A 1 260 ? -12.50800 20.22200  -23.79900 1.000 28.44911  ? 260 MET A C   1 
ATOM   2023 O  O   . MET A 1 260 ? -13.44900 20.32500  -23.01300 1.000 26.10909  ? 260 MET A O   1 
ATOM   2024 C  CB  . MET A 1 260 ? -11.47100 18.16600  -24.77500 1.000 24.10400  ? 260 MET A CB  1 
ATOM   2025 C  CG  . MET A 1 260 ? -10.58700 16.94200  -24.53600 1.000 25.19747  ? 260 MET A CG  1 
ATOM   2026 S  SD  . MET A 1 260 ? -8.85200  17.42000  -24.73800 1.000 27.23556  ? 260 MET A SD  1 
ATOM   2027 C  CE  . MET A 1 260 ? -8.70400  17.24200  -26.51700 1.000 29.48426  ? 260 MET A CE  1 
ATOM   2028 N  N   . LYS A 1 261 ? -12.36900 21.00400  -24.86800 1.000 28.69224  ? 261 LYS A N   1 
ATOM   2029 C  CA  . LYS A 1 261 ? -13.19500 22.18500  -25.08600 1.000 28.81468  ? 261 LYS A CA  1 
ATOM   2030 C  C   . LYS A 1 261 ? -13.74700 22.19000  -26.50700 1.000 27.81501  ? 261 LYS A C   1 
ATOM   2031 O  O   . LYS A 1 261 ? -13.02900 22.54100  -27.46200 1.000 26.90880  ? 261 LYS A O   1 
ATOM   2032 C  CB  . LYS A 1 261 ? -12.38800 23.45600  -24.80200 1.000 29.38157  ? 261 LYS A CB  1 
ATOM   2033 C  CG  . LYS A 1 261 ? -13.13500 24.77100  -25.00400 1.000 32.26345  ? 261 LYS A CG  1 
ATOM   2034 C  CD  . LYS A 1 261 ? -14.31200 24.92500  -24.03000 1.000 34.07698  ? 261 LYS A CD  1 
ATOM   2035 C  CE  . LYS A 1 261 ? -14.87100 26.35100  -24.06100 1.000 32.32773  ? 261 LYS A CE  1 
ATOM   2036 N  NZ  . LYS A 1 261 ? -15.40200 26.68100  -25.43700 1.000 36.11339  ? 261 LYS A NZ  1 
ATOM   2037 N  N   . PRO A 1 262 ? -15.01800 21.85100  -26.69200 1.000 26.63207  ? 262 PRO A N   1 
ATOM   2038 C  CA  . PRO A 1 262 ? -15.67500 22.21800  -27.94700 1.000 28.64500  ? 262 PRO A CA  1 
ATOM   2039 C  C   . PRO A 1 262 ? -15.79200 23.73700  -28.01600 1.000 31.19466  ? 262 PRO A C   1 
ATOM   2040 O  O   . PRO A 1 262 ? -15.63200 24.45500  -27.02500 1.000 29.04776  ? 262 PRO A O   1 
ATOM   2041 C  CB  . PRO A 1 262 ? -17.05200 21.54400  -27.85900 1.000 28.71214  ? 262 PRO A CB  1 
ATOM   2042 C  CG  . PRO A 1 262 ? -17.00000 20.66300  -26.61000 1.000 26.65437  ? 262 PRO A CG  1 
ATOM   2043 C  CD  . PRO A 1 262 ? -15.98200 21.31300  -25.71700 1.000 27.22607  ? 262 PRO A CD  1 
ATOM   2044 N  N   . SER A 1 263 ? -16.06400 24.22800  -29.21600 1.000 30.56182  ? 263 SER A N   1 
ATOM   2045 C  CA  . SER A 1 263 ? -16.12700 25.66600  -29.40400 1.000 32.66981  ? 263 SER A CA  1 
ATOM   2046 C  C   . SER A 1 263 ? -17.32800 26.23500  -28.66100 1.000 35.00626  ? 263 SER A C   1 
ATOM   2047 O  O   . SER A 1 263 ? -18.24400 25.50400  -28.26300 1.000 32.66683  ? 263 SER A O   1 
ATOM   2048 C  CB  . SER A 1 263 ? -16.20700 26.01000  -30.89600 1.000 37.05895  ? 263 SER A CB  1 
ATOM   2049 O  OG  . SER A 1 263 ? -17.37200 25.43000  -31.46400 1.000 40.05977  ? 263 SER A OG  1 
ATOM   2050 N  N   . ASP A 1 264 ? -17.29800 27.56200  -28.43700 1.000 34.32299  ? 264 ASP A N   1 
ATOM   2051 C  CA  . ASP A 1 264 ? -18.48700 28.27300  -27.98200 1.000 35.16067  ? 264 ASP A CA  1 
ATOM   2052 C  C   . ASP A 1 264 ? -19.62400 27.92300  -28.94200 1.000 39.27399  ? 264 ASP A C   1 
ATOM   2053 O  O   . ASP A 1 264 ? -19.38000 27.74900  -30.14200 1.000 36.21680  ? 264 ASP A O   1 
ATOM   2054 C  CB  . ASP A 1 264 ? -18.24200 29.78700  -27.94800 1.000 41.18571  ? 264 ASP A CB  1 
ATOM   2055 C  CG  . ASP A 1 264 ? -17.25900 30.22000  -26.84900 1.000 46.15465  ? 264 ASP A CG  1 
ATOM   2056 O  OD1 . ASP A 1 264 ? -16.70000 29.36300  -26.12200 1.000 46.58824  ? 264 ASP A OD1 1 
ATOM   2057 O  OD2 . ASP A 1 264 ? -17.04500 31.44400  -26.70600 1.000 50.02678  ? 264 ASP A OD2 1 
ATOM   2058 N  N   . PRO A 1 265 ? -20.87400 27.82200  -28.47200 1.000 36.84110  ? 265 PRO A N   1 
ATOM   2059 C  CA  . PRO A 1 265 ? -21.37700 28.21300  -27.15400 1.000 34.85389  ? 265 PRO A CA  1 
ATOM   2060 C  C   . PRO A 1 265 ? -21.19900 27.16000  -26.05200 1.000 34.95494  ? 265 PRO A C   1 
ATOM   2061 O  O   . PRO A 1 265 ? -21.76800 27.32800  -24.98900 1.000 32.98668  ? 265 PRO A O   1 
ATOM   2062 C  CB  . PRO A 1 265 ? -22.85900 28.48500  -27.44400 1.000 34.85647  ? 265 PRO A CB  1 
ATOM   2063 C  CG  . PRO A 1 265 ? -23.19700 27.45000  -28.46800 1.000 35.62333  ? 265 PRO A CG  1 
ATOM   2064 C  CD  . PRO A 1 265 ? -21.96500 27.35900  -29.34900 1.000 36.11319  ? 265 PRO A CD  1 
ATOM   2065 N  N   . ASN A 1 266 ? -20.46700 26.06300  -26.23100 1.000 32.67771  ? 266 ASN A N   1 
ATOM   2066 C  CA  . ASN A 1 266 ? -20.05500 25.27900  -25.07000 1.000 33.16491  ? 266 ASN A CA  1 
ATOM   2067 C  C   . ASN A 1 266 ? -18.97100 26.07300  -24.35200 1.000 36.82489  ? 266 ASN A C   1 
ATOM   2068 O  O   . ASN A 1 266 ? -17.83800 26.15200  -24.83500 1.000 38.84649  ? 266 ASN A O   1 
ATOM   2069 C  CB  . ASN A 1 266 ? -19.55100 23.89000  -25.47500 1.000 30.17292  ? 266 ASN A CB  1 
ATOM   2070 C  CG  . ASN A 1 266 ? -19.04000 23.08700  -24.28800 1.000 31.10676  ? 266 ASN A CG  1 
ATOM   2071 O  OD1 . ASN A 1 266 ? -18.30100 23.60700  -23.43600 1.000 31.38285  ? 266 ASN A OD1 1 
ATOM   2072 N  ND2 . ASN A 1 266 ? -19.43600 21.81700  -24.21200 1.000 28.56741  ? 266 ASN A ND2 1 
ATOM   2073 N  N   . ILE A 1 267 ? -19.29000 26.64900  -23.19100 1.000 34.66942  ? 267 ILE A N   1 
ATOM   2074 C  CA  . ILE A 1 267 ? -18.31500 27.49500  -22.50600 1.000 39.85748  ? 267 ILE A CA  1 
ATOM   2075 C  C   . ILE A 1 267 ? -17.65600 26.81500  -21.30200 1.000 36.12266  ? 267 ILE A C   1 
ATOM   2076 O  O   . ILE A 1 267 ? -16.82800 27.44600  -20.63300 1.000 36.88472  ? 267 ILE A O   1 
ATOM   2077 C  CB  . ILE A 1 267 ? -18.93100 28.84100  -22.06900 1.000 42.45712  ? 267 ILE A CB  1 
ATOM   2078 C  CG1 . ILE A 1 267 ? -20.12800 28.61200  -21.14400 1.000 41.33230  ? 267 ILE A CG1 1 
ATOM   2079 C  CG2 . ILE A 1 267 ? -19.26900 29.71600  -23.29700 1.000 41.53868  ? 267 ILE A CG2 1 
ATOM   2080 C  CD1 . ILE A 1 267 ? -20.51900 29.86100  -20.38700 1.000 50.96810  ? 267 ILE A CD1 1 
ATOM   2081 N  N   . VAL A 1 268 ? -17.96800 25.55300  -21.01800 1.000 30.81257  ? 268 VAL A N   1 
ATOM   2082 C  CA  . VAL A 1 268 ? -17.38800 24.83400  -19.89300 1.000 31.30409  ? 268 VAL A CA  1 
ATOM   2083 C  C   . VAL A 1 268 ? -16.35500 23.80000  -20.34100 1.000 33.46246  ? 268 VAL A C   1 
ATOM   2084 O  O   . VAL A 1 268 ? -15.30400 23.64000  -19.71300 1.000 31.03597  ? 268 VAL A O   1 
ATOM   2085 C  CB  . VAL A 1 268 ? -18.49700 24.16300  -19.05800 1.000 35.36467  ? 268 VAL A CB  1 
ATOM   2086 C  CG1 . VAL A 1 268 ? -17.88100 23.40000  -17.87000 1.000 32.62179  ? 268 VAL A CG1 1 
ATOM   2087 C  CG2 . VAL A 1 268 ? -19.48700 25.20300  -18.59500 1.000 37.31188  ? 268 VAL A CG2 1 
ATOM   2088 N  N   . GLY A 1 269 ? -16.65400 23.07300  -21.40600 1.000 28.98437  ? 269 GLY A N   1 
ATOM   2089 C  CA  . GLY A 1 269 ? -15.82500 21.96900  -21.81600 1.000 23.16722  ? 269 GLY A CA  1 
ATOM   2090 C  C   . GLY A 1 269 ? -16.62700 20.68500  -21.89100 1.000 26.39914  ? 269 GLY A C   1 
ATOM   2091 O  O   . GLY A 1 269 ? -17.86700 20.69600  -21.88900 1.000 26.71404  ? 269 GLY A O   1 
ATOM   2092 N  N   . ILE A 1 270 ? -15.90900 19.56500  -21.92800 1.000 27.31502  ? 270 ILE A N   1 
ATOM   2093 C  CA  . ILE A 1 270 ? -16.50200 18.24100  -22.07200 1.000 27.84171  ? 270 ILE A CA  1 
ATOM   2094 C  C   . ILE A 1 270 ? -15.50300 17.26200  -21.46900 1.000 27.42287  ? 270 ILE A C   1 
ATOM   2095 O  O   . ILE A 1 270 ? -14.30700 17.54800  -21.40700 1.000 28.00776  ? 270 ILE A O   1 
ATOM   2096 C  CB  . ILE A 1 270 ? -16.82700 17.95500  -23.56500 1.000 25.16217  ? 270 ILE A CB  1 
ATOM   2097 C  CG1 . ILE A 1 270 ? -17.94800 16.93000  -23.69500 1.000 27.60045  ? 270 ILE A CG1 1 
ATOM   2098 C  CG2 . ILE A 1 270 ? -15.58600 17.45900  -24.34000 1.000 22.93701  ? 270 ILE A CG2 1 
ATOM   2099 C  CD1 . ILE A 1 270 ? -18.55200 16.92400  -25.10800 1.000 29.70166  ? 270 ILE A CD1 1 
ATOM   2100 N  N   . ASN A 1 271 ? -16.00600 16.11900  -20.97500 1.000 25.87330  ? 271 ASN A N   1 
ATOM   2101 C  CA  . ASN A 1 271 ? -15.15600 15.08000  -20.37800 1.000 27.62187  ? 271 ASN A CA  1 
ATOM   2102 C  C   . ASN A 1 271 ? -14.53900 15.59200  -19.06900 1.000 28.33702  ? 271 ASN A C   1 
ATOM   2103 O  O   . ASN A 1 271 ? -13.32600 15.57300  -18.87700 1.000 27.62024  ? 271 ASN A O   1 
ATOM   2104 C  CB  . ASN A 1 271 ? -14.07800 14.62500  -21.37700 1.000 26.79511  ? 271 ASN A CB  1 
ATOM   2105 C  CG  . ASN A 1 271 ? -13.48200 13.26800  -21.06100 1.000 29.46612  ? 271 ASN A CG  1 
ATOM   2106 O  OD1 . ASN A 1 271 ? -14.17600 12.32900  -20.65600 1.000 28.46417  ? 271 ASN A OD1 1 
ATOM   2107 N  ND2 . ASN A 1 271 ? -12.17500 13.14700  -21.29300 1.000 25.56227  ? 271 ASN A ND2 1 
ATOM   2108 N  N   . LEU A 1 272 ? -15.39400 16.08100  -18.17600 1.000 28.63831  ? 272 LEU A N   1 
ATOM   2109 C  CA  . LEU A 1 272 ? -14.99300 16.51900  -16.84900 1.000 31.19006  ? 272 LEU A CA  1 
ATOM   2110 C  C   . LEU A 1 272 ? -15.79100 15.74800  -15.80500 1.000 28.51341  ? 272 LEU A C   1 
ATOM   2111 O  O   . LEU A 1 272 ? -16.69600 14.97700  -16.11700 1.000 27.40446  ? 272 LEU A O   1 
ATOM   2112 C  CB  . LEU A 1 272 ? -15.18600 18.03800  -16.68300 1.000 29.50396  ? 272 LEU A CB  1 
ATOM   2113 C  CG  . LEU A 1 272 ? -16.56000 18.52700  -17.13900 1.000 33.84258  ? 272 LEU A CG  1 
ATOM   2114 C  CD1 . LEU A 1 272 ? -17.26400 19.22300  -15.99900 1.000 37.66141  ? 272 LEU A CD1 1 
ATOM   2115 C  CD2 . LEU A 1 272 ? -16.47400 19.43400  -18.37400 1.000 30.88570  ? 272 LEU A CD2 1 
ATOM   2116 N  N   . ILE A 1 273 ? -15.42700 15.95200  -14.54600 1.000 29.05491  ? 273 ILE A N   1 
ATOM   2117 C  CA  . ILE A 1 273 ? -16.06700 15.26300  -13.44500 1.000 30.61813  ? 273 ILE A CA  1 
ATOM   2118 C  C   . ILE A 1 273 ? -15.90400 16.13400  -12.20900 1.000 31.62486  ? 273 ILE A C   1 
ATOM   2119 O  O   . ILE A 1 273 ? -14.88600 16.80800  -12.04200 1.000 29.89167  ? 273 ILE A O   1 
ATOM   2120 C  CB  . ILE A 1 273 ? -15.47800 13.84500  -13.23200 1.000 31.58154  ? 273 ILE A CB  1 
ATOM   2121 C  CG1 . ILE A 1 273 ? -16.28400 13.08700  -12.17000 1.000 38.75706  ? 273 ILE A CG1 1 
ATOM   2122 C  CG2 . ILE A 1 273 ? -14.05100 13.94000  -12.77300 1.000 34.30521  ? 273 ILE A CG2 1 
ATOM   2123 C  CD1 . ILE A 1 273 ? -17.73200 12.78700  -12.61000 1.000 35.73494  ? 273 ILE A CD1 1 
ATOM   2124 N  N   . ASP A 1 274 ? -16.92700 16.12400  -11.34900 1.000 28.98783  ? 274 ASP A N   1 
ATOM   2125 C  CA  . ASP A 1 274 ? -16.92900 16.88400  -10.10100 1.000 33.54349  ? 274 ASP A CA  1 
ATOM   2126 C  C   . ASP A 1 274 ? -16.72800 18.38000  -10.35900 1.000 32.48714  ? 274 ASP A C   1 
ATOM   2127 O  O   . ASP A 1 274 ? -16.13200 19.08900  -9.54900  1.000 33.86978  ? 274 ASP A O   1 
ATOM   2128 C  CB  . ASP A 1 274 ? -15.86800 16.35600  -9.12200  1.000 36.93981  ? 274 ASP A CB  1 
ATOM   2129 C  CG  . ASP A 1 274 ? -16.07100 14.88200  -8.76200  1.000 39.46110  ? 274 ASP A CG  1 
ATOM   2130 O  OD1 . ASP A 1 274 ? -17.24000 14.44200  -8.68300  1.000 41.35581  ? 274 ASP A OD1 1 
ATOM   2131 O  OD2 . ASP A 1 274 ? -15.06500 14.16100  -8.55400  1.000 41.95785  ? 274 ASP A OD2 1 
ATOM   2132 N  N   . ASP A 1 275 ? -17.22600 18.87000  -11.49200 1.000 31.98214  ? 275 ASP A N   1 
ATOM   2133 C  CA  . ASP A 1 275 ? -17.00400 20.25500  -11.90600 1.000 33.08780  ? 275 ASP A CA  1 
ATOM   2134 C  C   . ASP A 1 275 ? -15.51000 20.58600  -11.94400 1.000 33.36845  ? 275 ASP A C   1 
ATOM   2135 O  O   . ASP A 1 275 ? -15.11600 21.74000  -11.79100 1.000 34.96523  ? 275 ASP A O   1 
ATOM   2136 C  CB  . ASP A 1 275 ? -17.77200 21.23300  -11.00700 1.000 35.02594  ? 275 ASP A CB  1 
ATOM   2137 C  CG  . ASP A 1 275 ? -17.98100 22.58900  -11.66200 1.000 40.99525  ? 275 ASP A CG  1 
ATOM   2138 O  OD1 . ASP A 1 275 ? -17.78900 22.69700  -12.90100 1.000 41.24688  ? 275 ASP A OD1 1 
ATOM   2139 O  OD2 . ASP A 1 275 ? -18.32700 23.55500  -10.94200 1.000 38.30035  ? 275 ASP A OD2 1 
ATOM   2140 N  N   . LYS A 1 276 ? -14.66800 19.56800  -12.15700 1.000 32.03024  ? 276 LYS A N   1 
ATOM   2141 C  CA  . LYS A 1 276 ? -13.22600 19.73600  -12.23900 1.000 32.31519  ? 276 LYS A CA  1 
ATOM   2142 C  C   . LYS A 1 276 ? -12.69100 19.08800  -13.50900 1.000 32.15771  ? 276 LYS A C   1 
ATOM   2143 O  O   . LYS A 1 276 ? -13.34100 18.24500  -14.13500 1.000 29.84253  ? 276 LYS A O   1 
ATOM   2144 C  CB  . LYS A 1 276 ? -12.49700 19.13000  -11.02100 1.000 32.99437  ? 276 LYS A CB  1 
ATOM   2145 C  CG  . LYS A 1 276 ? -12.91600 19.74800  -9.68600  1.000 36.90055  ? 276 LYS A CG  1 
ATOM   2146 C  CD  . LYS A 1 276 ? -11.82400 19.63000  -8.63600  1.000 46.52356  ? 276 LYS A CD  1 
ATOM   2147 C  CE  . LYS A 1 276 ? -11.38900 18.17800  -8.43600  1.000 45.38684  ? 276 LYS A CE  1 
ATOM   2148 N  NZ  . LYS A 1 276 ? -10.03900 18.05200  -7.74800  1.000 50.26606  ? 276 LYS A NZ  1 
ATOM   2149 N  N   . ARG A 1 277 ? -11.47000 19.47600  -13.85800 1.000 31.30866  ? 277 ARG A N   1 
ATOM   2150 C  CA  . ARG A 1 277 ? -10.77500 18.84900  -14.97200 1.000 30.58501  ? 277 ARG A CA  1 
ATOM   2151 C  C   . ARG A 1 277 ? -10.38900 17.41400  -14.63100 1.000 31.54206  ? 277 ARG A C   1 
ATOM   2152 O  O   . ARG A 1 277 ? -9.88400  17.12700  -13.54000 1.000 29.00571  ? 277 ARG A O   1 
ATOM   2153 C  CB  . ARG A 1 277 ? -9.53200  19.64800  -15.34100 1.000 31.30762  ? 277 ARG A CB  1 
ATOM   2154 C  CG  . ARG A 1 277 ? -9.81400  21.06700  -15.79900 1.000 34.64620  ? 277 ARG A CG  1 
ATOM   2155 C  CD  . ARG A 1 277 ? -8.54400  21.76900  -16.21000 1.000 39.61734  ? 277 ARG A CD  1 
ATOM   2156 N  NE  . ARG A 1 277 ? -8.74000  23.20900  -16.34100 1.000 47.98088  ? 277 ARG A NE  1 
ATOM   2157 C  CZ  . ARG A 1 277 ? -9.29300  23.79300  -17.39700 1.000 54.69983  ? 277 ARG A CZ  1 
ATOM   2158 N  NH1 . ARG A 1 277 ? -9.69600  23.08800  -18.44900 1.000 51.15530  ? 277 ARG A NH1 1 
ATOM   2159 N  NH2 . ARG A 1 277 ? -9.45200  25.11700  -17.39700 1.000 51.89821  ? 277 ARG A NH2 1 
ATOM   2160 N  N   . LEU A 1 278 ? -10.61500 16.51000  -15.59000 1.000 29.88731  ? 278 LEU A N   1 
ATOM   2161 C  CA  . LEU A 1 278 ? -10.33900 15.09200  -15.37000 1.000 30.16282  ? 278 LEU A CA  1 
ATOM   2162 C  C   . LEU A 1 278 ? -8.90500  14.85800  -14.91800 1.000 31.03987  ? 278 LEU A C   1 
ATOM   2163 O  O   . LEU A 1 278 ? -8.66600  14.10100  -13.97200 1.000 31.89031  ? 278 LEU A O   1 
ATOM   2164 C  CB  . LEU A 1 278 ? -10.62600 14.30200  -16.64200 1.000 26.87050  ? 278 LEU A CB  1 
ATOM   2165 C  CG  . LEU A 1 278 ? -10.27600 12.81200  -16.62700 1.000 28.71373  ? 278 LEU A CG  1 
ATOM   2166 C  CD1 . LEU A 1 278 ? -11.03800 12.05500  -15.52400 1.000 25.33207  ? 278 LEU A CD1 1 
ATOM   2167 C  CD2 . LEU A 1 278 ? -10.57400 12.21700  -17.98700 1.000 26.28601  ? 278 LEU A CD2 1 
ATOM   2168 N  N   . GLU A 1 279 ? -7.93600  15.51300  -15.57100 1.000 28.85345  ? 279 GLU A N   1 
ATOM   2169 C  CA  . GLU A 1 279 ? -6.53500  15.34500  -15.18700 1.000 31.52035  ? 279 GLU A CA  1 
ATOM   2170 C  C   . GLU A 1 279 ? -6.25600  15.85200  -13.76600 1.000 33.52287  ? 279 GLU A C   1 
ATOM   2171 O  O   . GLU A 1 279 ? -5.35800  15.33300  -13.09400 1.000 35.76008  ? 279 GLU A O   1 
ATOM   2172 C  CB  . GLU A 1 279 ? -5.62500  16.04400  -16.20200 1.000 28.34773  ? 279 GLU A CB  1 
ATOM   2173 C  CG  . GLU A 1 279 ? -5.84700  17.54400  -16.34100 1.000 30.85169  ? 279 GLU A CG  1 
ATOM   2174 C  CD  . GLU A 1 279 ? -6.90600  17.92800  -17.37900 1.000 29.21545  ? 279 GLU A CD  1 
ATOM   2175 O  OE1 . GLU A 1 279 ? -7.83900  17.15000  -17.63800 1.000 29.19371  ? 279 GLU A OE1 1 
ATOM   2176 O  OE2 . GLU A 1 279 ? -6.80400  19.03500  -17.93900 1.000 33.81586  ? 279 GLU A OE2 1 
ATOM   2177 N  N   . ASN A 1 280 ? -7.01800  16.83400  -13.27800 1.000 33.03373  ? 280 ASN A N   1 
ATOM   2178 C  CA  . ASN A 1 280 ? -6.82700  17.31100  -11.90700 1.000 33.38536  ? 280 ASN A CA  1 
ATOM   2179 C  C   . ASN A 1 280 ? -7.44400  16.36300  -10.88500 1.000 33.90195  ? 280 ASN A C   1 
ATOM   2180 O  O   . ASN A 1 280 ? -6.90400  16.18800  -9.79000  1.000 35.95234  ? 280 ASN A O   1 
ATOM   2181 C  CB  . ASN A 1 280 ? -7.41100  18.71600  -11.75600 1.000 34.03904  ? 280 ASN A CB  1 
ATOM   2182 C  CG  . ASN A 1 280 ? -6.54900  19.76600  -12.42900 1.000 37.60921  ? 280 ASN A CG  1 
ATOM   2183 O  OD1 . ASN A 1 280 ? -5.37400  19.52200  -12.70700 1.000 40.50324  ? 280 ASN A OD1 1 
ATOM   2184 N  ND2 . ASN A 1 280 ? -7.11800  20.93100  -12.69600 1.000 37.21235  ? 280 ASN A ND2 1 
ATOM   2185 N  N   . VAL A 1 281 ? -8.58000  15.75600  -11.22100 1.000 35.56850  ? 281 VAL A N   1 
ATOM   2186 C  CA  . VAL A 1 281 ? -9.15600  14.72100  -10.37100 1.000 33.55218  ? 281 VAL A CA  1 
ATOM   2187 C  C   . VAL A 1 281 ? -8.21300  13.52600  -10.29400 1.000 37.19225  ? 281 VAL A C   1 
ATOM   2188 O  O   . VAL A 1 281 ? -8.02000  12.93500  -9.22600  1.000 36.17147  ? 281 VAL A O   1 
ATOM   2189 C  CB  . VAL A 1 281 ? -10.54800 14.32300  -10.90600 1.000 37.18990  ? 281 VAL A CB  1 
ATOM   2190 C  CG1 . VAL A 1 281 ? -11.07700 13.10900  -10.17300 1.000 36.68304  ? 281 VAL A CG1 1 
ATOM   2191 C  CG2 . VAL A 1 281 ? -11.51400 15.48600  -10.75300 1.000 33.80021  ? 281 VAL A CG2 1 
ATOM   2192 N  N   . LEU A 1 282 ? -7.59200  13.16800  -11.42200 1.000 31.94450  ? 282 LEU A N   1 
ATOM   2193 C  CA  . LEU A 1 282 ? -6.68900  12.02300  -11.46400 1.000 37.02750  ? 282 LEU A CA  1 
ATOM   2194 C  C   . LEU A 1 282 ? -5.27400  12.35400  -11.02800 1.000 36.91656  ? 282 LEU A C   1 
ATOM   2195 O  O   . LEU A 1 282 ? -4.46400  11.43000  -10.89900 1.000 36.75751  ? 282 LEU A O   1 
ATOM   2196 C  CB  . LEU A 1 282 ? -6.62000  11.42800  -12.87300 1.000 33.55794  ? 282 LEU A CB  1 
ATOM   2197 C  CG  . LEU A 1 282 ? -7.87600  10.75800  -13.41900 1.000 32.85752  ? 282 LEU A CG  1 
ATOM   2198 C  CD1 . LEU A 1 282 ? -7.64500  10.41000  -14.85800 1.000 36.54408  ? 282 LEU A CD1 1 
ATOM   2199 C  CD2 . LEU A 1 282 ? -8.17900  9.51800   -12.63000 1.000 37.14283  ? 282 LEU A CD2 1 
ATOM   2200 N  N   . GLN A 1 283 ? -4.95900  13.63400  -10.80900 1.000 36.34055  ? 283 GLN A N   1 
ATOM   2201 C  CA  . GLN A 1 283 ? -3.61600  14.04800  -10.40000 1.000 38.52917  ? 283 GLN A CA  1 
ATOM   2202 C  C   . GLN A 1 283 ? -2.59000  13.52400  -11.40200 1.000 39.10862  ? 283 GLN A C   1 
ATOM   2203 O  O   . GLN A 1 283 ? -1.55400  12.95900  -11.05100 1.000 35.47155  ? 283 GLN A O   1 
ATOM   2204 C  CB  . GLN A 1 283 ? -3.31100  13.59000  -8.96900  1.000 41.11057  ? 283 GLN A CB  1 
ATOM   2205 C  CG  . GLN A 1 283 ? -4.18500  14.28200  -7.90300  1.000 43.50521  ? 283 GLN A CG  1 
ATOM   2206 C  CD  . GLN A 1 283 ? -4.08600  13.60900  -6.53100  1.000 54.53448  ? 283 GLN A CD  1 
ATOM   2207 O  OE1 . GLN A 1 283 ? -3.80500  14.25700  -5.53000  1.000 53.40899  ? 283 GLN A OE1 1 
ATOM   2208 N  NE2 . GLN A 1 283 ? -4.30900  12.29600  -6.49200  1.000 60.35338  ? 283 GLN A NE2 1 
ATOM   2209 N  N   . LEU A 1 284 ? -2.92700  13.69700  -12.67500 1.000 34.79461  ? 284 LEU A N   1 
ATOM   2210 C  CA  . LEU A 1 284 ? -2.16500  13.14800  -13.78000 1.000 37.93974  ? 284 LEU A CA  1 
ATOM   2211 C  C   . LEU A 1 284 ? -0.89700  13.95800  -14.00900 1.000 37.98320  ? 284 LEU A C   1 
ATOM   2212 O  O   . LEU A 1 284 ? -0.96900  15.15000  -14.32700 1.000 38.00479  ? 284 LEU A O   1 
ATOM   2213 C  CB  . LEU A 1 284 ? -3.03700  13.17000  -15.02700 1.000 38.09623  ? 284 LEU A CB  1 
ATOM   2214 C  CG  . LEU A 1 284 ? -2.93500  11.99800  -15.97900 1.000 42.81772  ? 284 LEU A CG  1 
ATOM   2215 C  CD1 . LEU A 1 284 ? -3.17600  10.70600  -15.21000 1.000 41.22768  ? 284 LEU A CD1 1 
ATOM   2216 C  CD2 . LEU A 1 284 ? -3.95200  12.21100  -17.10000 1.000 35.94141  ? 284 LEU A CD2 1 
ATOM   2217 N  N   . LYS A 1 285 ? 0.26000   13.31300  -13.85700 1.000 39.27810  ? 285 LYS A N   1 
ATOM   2218 C  CA  . LYS A 1 285 ? 1.51400   13.84800  -14.37900 1.000 40.09317  ? 285 LYS A CA  1 
ATOM   2219 C  C   . LYS A 1 285 ? 1.57600   13.68000  -15.89900 1.000 37.25639  ? 285 LYS A C   1 
ATOM   2220 O  O   . LYS A 1 285 ? 0.85100   12.87600  -16.48900 1.000 36.91447  ? 285 LYS A O   1 
ATOM   2221 C  CB  . LYS A 1 285 ? 2.71500   13.13900  -13.74700 1.000 40.11880  ? 285 LYS A CB  1 
ATOM   2222 C  CG  . LYS A 1 285 ? 2.82100   13.24100  -12.23000 1.000 45.30439  ? 285 LYS A CG  1 
ATOM   2223 C  CD  . LYS A 1 285 ? 3.94300   12.34300  -11.72400 1.000 47.90426  ? 285 LYS A CD  1 
ATOM   2224 C  CE  . LYS A 1 285 ? 4.28400   12.62300  -10.27200 1.000 52.30351  ? 285 LYS A CE  1 
ATOM   2225 N  NZ  . LYS A 1 285 ? 5.44000   11.78200  -9.80600  1.000 58.84647  ? 285 LYS A NZ  1 
ATOM   2226 N  N   . ALA A 1 286 ? 2.46300   14.45100  -16.53400 1.000 38.27747  ? 286 ALA A N   1 
ATOM   2227 C  CA  . ALA A 1 286 ? 2.73800   14.30800  -17.96300 1.000 39.00375  ? 286 ALA A CA  1 
ATOM   2228 C  C   . ALA A 1 286 ? 4.21300   14.58700  -18.22700 1.000 42.34964  ? 286 ALA A C   1 
ATOM   2229 O  O   . ALA A 1 286 ? 4.89500   15.24200  -17.43400 1.000 40.74310  ? 286 ALA A O   1 
ATOM   2230 C  CB  . ALA A 1 286 ? 1.86800   15.23900  -18.82000 1.000 38.14515  ? 286 ALA A CB  1 
ATOM   2231 N  N   . ALA A 1 287 ? 4.70200   14.08600  -19.36500 1.000 40.80150  ? 287 ALA A N   1 
ATOM   2232 C  CA  . ALA A 1 287 ? 6.12900   14.20200  -19.67200 1.000 41.46795  ? 287 ALA A CA  1 
ATOM   2233 C  C   . ALA A 1 287 ? 6.58400   15.64900  -19.72000 1.000 40.48748  ? 287 ALA A C   1 
ATOM   2234 O  O   . ALA A 1 287 ? 7.73600   15.94300  -19.38600 1.000 42.58281  ? 287 ALA A O   1 
ATOM   2235 C  CB  . ALA A 1 287 ? 6.45800   13.51800  -21.00700 1.000 36.96889  ? 287 ALA A CB  1 
ATOM   2236 N  N   . ASP A 1 288 ? 5.70700   16.56400  -20.12200 1.000 43.87325  ? 288 ASP A N   1 
ATOM   2237 C  CA  . ASP A 1 288 ? 6.07700   17.94900  -20.39400 1.000 47.29565  ? 288 ASP A CA  1 
ATOM   2238 C  C   . ASP A 1 288 ? 5.21600   18.92300  -19.59400 1.000 48.57306  ? 288 ASP A C   1 
ATOM   2239 O  O   . ASP A 1 288 ? 4.81600   19.97800  -20.09200 1.000 50.85024  ? 288 ASP A O   1 
ATOM   2240 C  CB  . ASP A 1 288 ? 5.95600   18.24200  -21.88500 1.000 42.97487  ? 288 ASP A CB  1 
ATOM   2241 C  CG  . ASP A 1 288 ? 4.57300   17.94300  -22.40500 1.000 40.46494  ? 288 ASP A CG  1 
ATOM   2242 O  OD1 . ASP A 1 288 ? 3.88600   17.11600  -21.77100 1.000 40.80469  ? 288 ASP A OD1 1 
ATOM   2243 O  OD2 . ASP A 1 288 ? 4.15500   18.53600  -23.42200 1.000 42.00420  ? 288 ASP A OD2 1 
ATOM   2244 N  N   . SER A 1 289 ? 4.90600   18.59300  -18.34800 1.000 61.87372  ? 289 SER A N   1 
ATOM   2245 C  CA  . SER A 1 289 ? 4.18400   19.53700  -17.49900 1.000 65.35885  ? 289 SER A CA  1 
ATOM   2246 C  C   . SER A 1 289 ? 4.74300   19.56500  -16.07300 1.000 71.35802  ? 289 SER A C   1 
ATOM   2247 O  O   . SER A 1 289 ? 5.59400   18.74600  -15.70300 1.000 72.48094  ? 289 SER A O   1 
ATOM   2248 C  CB  . SER A 1 289 ? 2.69900   19.19400  -17.46700 1.000 61.91104  ? 289 SER A CB  1 
ATOM   2249 O  OG  . SER A 1 289 ? 2.50000   17.95900  -16.80200 1.000 62.57539  ? 289 SER A OG  1 
ATOM   2250 N  N   . LYS B 1 6   ? -55.16300 27.78200  -24.74600 1.000 56.34897  ? 6   LYS B N   1 
ATOM   2251 C  CA  . LYS B 1 6   ? -53.93600 27.20600  -25.30400 1.000 60.87788  ? 6   LYS B CA  1 
ATOM   2252 C  C   . LYS B 1 6   ? -53.82300 25.70700  -25.01900 1.000 60.84221  ? 6   LYS B C   1 
ATOM   2253 O  O   . LYS B 1 6   ? -54.10700 25.26800  -23.90400 1.000 61.22181  ? 6   LYS B O   1 
ATOM   2254 C  CB  . LYS B 1 6   ? -52.69100 27.91100  -24.74700 1.000 60.04290  ? 6   LYS B CB  1 
ATOM   2255 C  CG  . LYS B 1 6   ? -52.42400 29.31800  -25.29500 1.000 63.05397  ? 6   LYS B CG  1 
ATOM   2256 C  CD  . LYS B 1 6   ? -50.94000 29.71600  -25.13600 1.000 58.14880  ? 6   LYS B CD  1 
ATOM   2257 C  CE  . LYS B 1 6   ? -50.01900 28.89500  -26.05300 1.000 55.77424  ? 6   LYS B CE  1 
ATOM   2258 N  NZ  . LYS B 1 6   ? -50.33100 29.07300  -27.51200 1.000 61.80021  ? 6   LYS B NZ  1 
ATOM   2259 N  N   . PRO B 1 7   ? -53.41300 24.92100  -26.01800 1.000 54.07329  ? 7   PRO B N   1 
ATOM   2260 C  CA  . PRO B 1 7   ? -53.11300 23.50600  -25.75500 1.000 49.58408  ? 7   PRO B CA  1 
ATOM   2261 C  C   . PRO B 1 7   ? -52.02400 23.37100  -24.70200 1.000 48.06875  ? 7   PRO B C   1 
ATOM   2262 O  O   . PRO B 1 7   ? -50.99100 24.03900  -24.76300 1.000 44.51136  ? 7   PRO B O   1 
ATOM   2263 C  CB  . PRO B 1 7   ? -52.65900 22.98000  -27.11900 1.000 46.39814  ? 7   PRO B CB  1 
ATOM   2264 C  CG  . PRO B 1 7   ? -53.33500 23.87500  -28.09500 1.000 49.14839  ? 7   PRO B CG  1 
ATOM   2265 C  CD  . PRO B 1 7   ? -53.34700 25.23400  -27.45600 1.000 51.59383  ? 7   PRO B CD  1 
ATOM   2266 N  N   . GLN B 1 8   ? -52.28400 22.52400  -23.71100 1.000 46.80991  ? 8   GLN B N   1 
ATOM   2267 C  CA  . GLN B 1 8   ? -51.39700 22.33600  -22.57100 1.000 44.22371  ? 8   GLN B CA  1 
ATOM   2268 C  C   . GLN B 1 8   ? -50.56200 21.07200  -22.73600 1.000 39.53956  ? 8   GLN B C   1 
ATOM   2269 O  O   . GLN B 1 8   ? -50.83700 20.21900  -23.58200 1.000 37.98638  ? 8   GLN B O   1 
ATOM   2270 C  CB  . GLN B 1 8   ? -52.20800 22.26600  -21.27300 1.000 39.38176  ? 8   GLN B CB  1 
ATOM   2271 C  CG  . GLN B 1 8   ? -52.99200 23.54300  -20.96300 1.000 47.82928  ? 8   GLN B CG  1 
ATOM   2272 C  CD  . GLN B 1 8   ? -52.08600 24.74800  -20.80600 1.000 45.03043  ? 8   GLN B CD  1 
ATOM   2273 O  OE1 . GLN B 1 8   ? -51.17000 24.74200  -19.98900 1.000 44.20070  ? 8   GLN B OE1 1 
ATOM   2274 N  NE2 . GLN B 1 8   ? -52.32900 25.78400  -21.60000 1.000 44.98607  ? 8   GLN B NE2 1 
ATOM   2275 N  N   . LEU B 1 9   ? -49.53400 20.95600  -21.89700 1.000 37.95032  ? 9   LEU B N   1 
ATOM   2276 C  CA  . LEU B 1 9   ? -48.75000 19.73000  -21.84100 1.000 36.58027  ? 9   LEU B CA  1 
ATOM   2277 C  C   . LEU B 1 9   ? -49.59900 18.59300  -21.30100 1.000 40.23716  ? 9   LEU B C   1 
ATOM   2278 O  O   . LEU B 1 9   ? -50.37800 18.76500  -20.35400 1.000 35.17329  ? 9   LEU B O   1 
ATOM   2279 C  CB  . LEU B 1 9   ? -47.52300 19.90800  -20.95200 1.000 36.74200  ? 9   LEU B CB  1 
ATOM   2280 C  CG  . LEU B 1 9   ? -46.42900 20.82100  -21.47600 1.000 36.01604  ? 9   LEU B CG  1 
ATOM   2281 C  CD1 . LEU B 1 9   ? -45.59400 21.35900  -20.32000 1.000 32.70030  ? 9   LEU B CD1 1 
ATOM   2282 C  CD2 . LEU B 1 9   ? -45.58300 20.04700  -22.45900 1.000 33.07524  ? 9   LEU B CD2 1 
ATOM   2283 N  N   . GLN B 1 10  ? -49.45300 17.42500  -21.91000 1.000 35.54662  ? 10  GLN B N   1 
ATOM   2284 C  CA  . GLN B 1 10  ? -50.18800 16.27400  -21.43600 1.000 37.18709  ? 10  GLN B CA  1 
ATOM   2285 C  C   . GLN B 1 10  ? -49.46200 15.65800  -20.24400 1.000 38.45497  ? 10  GLN B C   1 
ATOM   2286 O  O   . GLN B 1 10  ? -48.23000 15.52300  -20.24700 1.000 35.74189  ? 10  GLN B O   1 
ATOM   2287 C  CB  . GLN B 1 10  ? -50.37500 15.26000  -22.56300 1.000 37.47212  ? 10  GLN B CB  1 
ATOM   2288 C  CG  . GLN B 1 10  ? -51.09100 15.84700  -23.74900 1.000 38.05962  ? 10  GLN B CG  1 
ATOM   2289 C  CD  . GLN B 1 10  ? -51.69700 14.78900  -24.63900 1.000 42.53761  ? 10  GLN B CD  1 
ATOM   2290 O  OE1 . GLN B 1 10  ? -51.93900 13.65700  -24.20800 1.000 41.53401  ? 10  GLN B OE1 1 
ATOM   2291 N  NE2 . GLN B 1 10  ? -51.94700 15.14900  -25.89500 1.000 41.91228  ? 10  GLN B NE2 1 
ATOM   2292 N  N   . ARG B 1 11  ? -50.23900 15.31700  -19.21700 1.000 37.20027  ? 11  ARG B N   1 
ATOM   2293 C  CA  . ARG B 1 11  ? -49.76800 14.62200  -18.02700 1.000 35.62125  ? 11  ARG B CA  1 
ATOM   2294 C  C   . ARG B 1 11  ? -50.20300 13.16800  -18.13700 1.000 39.28125  ? 11  ARG B C   1 
ATOM   2295 O  O   . ARG B 1 11  ? -51.40500 12.88900  -18.23900 1.000 38.22051  ? 11  ARG B O   1 
ATOM   2296 C  CB  . ARG B 1 11  ? -50.36200 15.24600  -16.76100 1.000 38.64788  ? 11  ARG B CB  1 
ATOM   2297 C  CG  . ARG B 1 11  ? -49.67500 16.47400  -16.22700 1.000 42.09271  ? 11  ARG B CG  1 
ATOM   2298 C  CD  . ARG B 1 11  ? -50.19800 17.77200  -16.81800 1.000 44.03659  ? 11  ARG B CD  1 
ATOM   2299 N  NE  . ARG B 1 11  ? -49.55200 18.92600  -16.19000 1.000 40.62547  ? 11  ARG B NE  1 
ATOM   2300 C  CZ  . ARG B 1 11  ? -49.46900 20.13500  -16.73500 1.000 44.69308  ? 11  ARG B CZ  1 
ATOM   2301 N  NH1 . ARG B 1 11  ? -49.99700 20.39700  -17.92600 1.000 38.03246  ? 11  ARG B NH1 1 
ATOM   2302 N  NH2 . ARG B 1 11  ? -48.83500 21.10400  -16.07400 1.000 41.31047  ? 11  ARG B NH2 1 
ATOM   2303 N  N   . LEU B 1 12  ? -49.24600 12.24600  -18.09800 1.000 37.13559  ? 12  LEU B N   1 
ATOM   2304 C  CA  . LEU B 1 12  ? -49.52700 10.83000  -18.30000 1.000 41.21433  ? 12  LEU B CA  1 
ATOM   2305 C  C   . LEU B 1 12  ? -49.10600 10.01000  -17.07900 1.000 42.48515  ? 12  LEU B C   1 
ATOM   2306 O  O   . LEU B 1 12  ? -48.08200 10.29500  -16.44500 1.000 38.19407  ? 12  LEU B O   1 
ATOM   2307 C  CB  . LEU B 1 12  ? -48.80200 10.31000  -19.55500 1.000 39.65703  ? 12  LEU B CB  1 
ATOM   2308 C  CG  . LEU B 1 12  ? -49.41200 10.52500  -20.95300 1.000 45.33002  ? 12  LEU B CG  1 
ATOM   2309 C  CD1 . LEU B 1 12  ? -49.77000 11.97200  -21.25200 1.000 42.85974  ? 12  LEU B CD1 1 
ATOM   2310 C  CD2 . LEU B 1 12  ? -48.45100 10.00500  -22.01700 1.000 43.70076  ? 12  LEU B CD2 1 
ATOM   2311 N  N   . ALA B 1 13  ? -49.90000 8.99400   -16.74900 1.000 41.30349  ? 13  ALA B N   1 
ATOM   2312 C  CA  . ALA B 1 13  ? -49.50700 8.03700   -15.72300 1.000 41.78899  ? 13  ALA B CA  1 
ATOM   2313 C  C   . ALA B 1 13  ? -48.35500 7.16200   -16.21400 1.000 48.25381  ? 13  ALA B C   1 
ATOM   2314 O  O   . ALA B 1 13  ? -48.12100 7.00600   -17.41800 1.000 47.77656  ? 13  ALA B O   1 
ATOM   2315 C  CB  . ALA B 1 13  ? -50.68300 7.14500   -15.32500 1.000 46.78643  ? 13  ALA B CB  1 
ATOM   2316 N  N   . ALA B 1 14  ? -47.65900 6.54800   -15.24900 1.000 51.84391  ? 14  ALA B N   1 
ATOM   2317 C  CA  . ALA B 1 14  ? -46.47100 5.74900   -15.55000 1.000 50.18200  ? 14  ALA B CA  1 
ATOM   2318 C  C   . ALA B 1 14  ? -46.77500 4.57500   -16.47300 1.000 50.42910  ? 14  ALA B C   1 
ATOM   2319 O  O   . ALA B 1 14  ? -45.88800 4.11700   -17.20100 1.000 52.50172  ? 14  ALA B O   1 
ATOM   2320 C  CB  . ALA B 1 14  ? -45.84500 5.24100   -14.25000 1.000 51.16404  ? 14  ALA B CB  1 
ATOM   2321 N  N   . ASP B 1 15  ? -48.00200 4.06600   -16.45600 1.000 50.11286  ? 15  ASP B N   1 
ATOM   2322 C  CA  . ASP B 1 15  ? -48.37700 2.95100   -17.31100 1.000 49.93707  ? 15  ASP B CA  1 
ATOM   2323 C  C   . ASP B 1 15  ? -48.77400 3.38600   -18.71600 1.000 49.86426  ? 15  ASP B C   1 
ATOM   2324 O  O   . ASP B 1 15  ? -49.26200 2.55500   -19.48500 1.000 50.74051  ? 15  ASP B O   1 
ATOM   2325 C  CB  . ASP B 1 15  ? -49.52900 2.17100   -16.67800 1.000 56.67349  ? 15  ASP B CB  1 
ATOM   2326 C  CG  . ASP B 1 15  ? -50.79400 3.00100   -16.55200 1.000 58.25433  ? 15  ASP B CG  1 
ATOM   2327 O  OD1 . ASP B 1 15  ? -50.79300 3.94100   -15.73600 1.000 58.25595  ? 15  ASP B OD1 1 
ATOM   2328 O  OD2 . ASP B 1 15  ? -51.78100 2.72600   -17.28000 1.000 69.08702  ? 15  ASP B OD2 1 
ATOM   2329 N  N   . ALA B 1 16  ? -48.57500 4.65100   -19.07000 1.000 49.72567  ? 16  ALA B N   1 
ATOM   2330 C  CA  . ALA B 1 16  ? -49.06100 5.15000   -20.34500 1.000 51.33466  ? 16  ALA B CA  1 
ATOM   2331 C  C   . ALA B 1 16  ? -48.36700 4.45200   -21.51300 1.000 51.37993  ? 16  ALA B C   1 
ATOM   2332 O  O   . ALA B 1 16  ? -47.30000 3.84900   -21.37800 1.000 49.29307  ? 16  ALA B O   1 
ATOM   2333 C  CB  . ALA B 1 16  ? -48.85500 6.65800   -20.44700 1.000 48.76200  ? 16  ALA B CB  1 
ATOM   2334 N  N   . ASP B 1 17  ? -48.99600 4.55500   -22.67600 1.000 47.20547  ? 17  ASP B N   1 
ATOM   2335 C  CA  . ASP B 1 17  ? -48.53300 3.84600   -23.85400 1.000 49.19115  ? 17  ASP B CA  1 
ATOM   2336 C  C   . ASP B 1 17  ? -47.27400 4.49500   -24.42600 1.000 49.86059  ? 17  ASP B C   1 
ATOM   2337 O  O   . ASP B 1 17  ? -47.19200 5.71700   -24.58100 1.000 45.19528  ? 17  ASP B O   1 
ATOM   2338 C  CB  . ASP B 1 17  ? -49.65400 3.81700   -24.89100 1.000 49.53871  ? 17  ASP B CB  1 
ATOM   2339 C  CG  . ASP B 1 17  ? -49.31900 2.96700   -26.08200 1.000 57.54360  ? 17  ASP B CG  1 
ATOM   2340 O  OD1 . ASP B 1 17  ? -49.58900 1.73900   -26.04900 1.000 64.65429  ? 17  ASP B OD1 1 
ATOM   2341 O  OD2 . ASP B 1 17  ? -48.77900 3.53000   -27.05700 1.000 62.24605  ? 17  ASP B OD2 1 
ATOM   2342 N  N   . VAL B 1 18  ? -46.28500 3.66400   -24.75300 1.000 51.74377  ? 18  VAL B N   1 
ATOM   2343 C  CA  . VAL B 1 18  ? -45.00300 4.20600   -25.19300 1.000 53.09074  ? 18  VAL B CA  1 
ATOM   2344 C  C   . VAL B 1 18  ? -45.11400 4.78200   -26.60000 1.000 53.32890  ? 18  VAL B C   1 
ATOM   2345 O  O   . VAL B 1 18  ? -44.57000 5.85700   -26.88300 1.000 51.89599  ? 18  VAL B O   1 
ATOM   2346 C  CB  . VAL B 1 18  ? -43.90100 3.13700   -25.09000 1.000 55.93569  ? 18  VAL B CB  1 
ATOM   2347 C  CG1 . VAL B 1 18  ? -42.64200 3.59400   -25.81400 1.000 54.37300  ? 18  VAL B CG1 1 
ATOM   2348 C  CG2 . VAL B 1 18  ? -43.57900 2.87900   -23.63000 1.000 53.44200  ? 18  VAL B CG2 1 
ATOM   2349 N  N   . ASP B 1 19  ? -45.82800 4.09400   -27.49900 1.000 49.31237  ? 19  ASP B N   1 
ATOM   2350 C  CA  . ASP B 1 19  ? -46.09900 4.67100   -28.81300 1.000 49.96920  ? 19  ASP B CA  1 
ATOM   2351 C  C   . ASP B 1 19  ? -46.72100 6.05600   -28.67800 1.000 48.96057  ? 19  ASP B C   1 
ATOM   2352 O  O   . ASP B 1 19  ? -46.30400 7.00800   -29.34800 1.000 46.88726  ? 19  ASP B O   1 
ATOM   2353 C  CB  . ASP B 1 19  ? -47.01600 3.75000   -29.62700 1.000 57.11587  ? 19  ASP B CB  1 
ATOM   2354 C  CG  . ASP B 1 19  ? -46.36300 2.41800   -29.96600 1.000 66.88808  ? 19  ASP B CG  1 
ATOM   2355 O  OD1 . ASP B 1 19  ? -45.23600 2.16600   -29.47400 1.000 69.29066  ? 19  ASP B OD1 1 
ATOM   2356 O  OD2 . ASP B 1 19  ? -46.97700 1.62500   -30.72500 1.000 70.52810  ? 19  ASP B OD2 1 
ATOM   2357 N  N   . ARG B 1 20  ? -47.71200 6.18700   -27.79200 1.000 46.73868  ? 20  ARG B N   1 
ATOM   2358 C  CA  . ARG B 1 20  ? -48.34200 7.47900   -27.55400 1.000 45.12737  ? 20  ARG B CA  1 
ATOM   2359 C  C   . ARG B 1 20  ? -47.32100 8.52000   -27.11000 1.000 41.41592  ? 20  ARG B C   1 
ATOM   2360 O  O   . ARG B 1 20  ? -47.29300 9.63500   -27.63800 1.000 40.07949  ? 20  ARG B O   1 
ATOM   2361 C  CB  . ARG B 1 20  ? -49.44600 7.33500   -26.50800 1.000 46.29373  ? 20  ARG B CB  1 
ATOM   2362 C  CG  . ARG B 1 20  ? -50.10100 8.65900   -26.14300 1.000 44.55754  ? 20  ARG B CG  1 
ATOM   2363 C  CD  . ARG B 1 20  ? -51.11800 8.49000   -25.05300 1.000 45.66270  ? 20  ARG B CD  1 
ATOM   2364 N  NE  . ARG B 1 20  ? -51.74300 9.75900   -24.71200 1.000 46.70235  ? 20  ARG B NE  1 
ATOM   2365 C  CZ  . ARG B 1 20  ? -52.59400 9.91500   -23.71000 1.000 46.21905  ? 20  ARG B CZ  1 
ATOM   2366 N  NH1 . ARG B 1 20  ? -52.93900 8.89900   -22.93700 1.000 42.71523  ? 20  ARG B NH1 1 
ATOM   2367 N  NH2 . ARG B 1 20  ? -53.10900 11.12200  -23.47700 1.000 45.36631  ? 20  ARG B NH2 1 
ATOM   2368 N  N   . MET B 1 21  ? -46.48400 8.17900   -26.12900 1.000 40.59406  ? 21  MET B N   1 
ATOM   2369 C  CA  . MET B 1 21  ? -45.48000 9.12200   -25.64500 1.000 38.31420  ? 21  MET B CA  1 
ATOM   2370 C  C   . MET B 1 21  ? -44.53400 9.53800   -26.75900 1.000 42.33102  ? 21  MET B C   1 
ATOM   2371 O  O   . MET B 1 21  ? -44.27100 10.72900  -26.95900 1.000 38.67682  ? 21  MET B O   1 
ATOM   2372 C  CB  . MET B 1 21  ? -44.70400 8.50700   -24.48400 1.000 40.58933  ? 21  MET B CB  1 
ATOM   2373 C  CG  . MET B 1 21  ? -45.56900 8.30900   -23.23600 1.000 45.28033  ? 21  MET B CG  1 
ATOM   2374 S  SD  . MET B 1 21  ? -44.64700 7.70000   -21.81300 1.000 45.19558  ? 21  MET B SD  1 
ATOM   2375 C  CE  . MET B 1 21  ? -44.71300 5.93800   -22.07700 1.000 46.77965  ? 21  MET B CE  1 
ATOM   2376 N  N   . CYS B 1 22  ? -44.02100 8.55400   -27.49900 1.000 40.18452  ? 22  CYS B N   1 
ATOM   2377 C  CA  . CYS B 1 22  ? -43.17600 8.80800   -28.65700 1.000 43.55554  ? 22  CYS B CA  1 
ATOM   2378 C  C   . CYS B 1 22  ? -43.83600 9.77200   -29.64600 1.000 43.10228  ? 22  CYS B C   1 
ATOM   2379 O  O   . CYS B 1 22  ? -43.17600 10.67600  -30.17400 1.000 41.79541  ? 22  CYS B O   1 
ATOM   2380 C  CB  . CYS B 1 22  ? -42.84700 7.46200   -29.31700 1.000 49.15025  ? 22  CYS B CB  1 
ATOM   2381 S  SG  . CYS B 1 22  ? -41.59200 7.47700   -30.58800 1.000 67.94950  ? 22  CYS B SG  1 
ATOM   2382 N  N   . ARG B 1 23  ? -45.13700 9.59900   -29.91500 1.000 41.29241  ? 23  ARG B N   1 
ATOM   2383 C  CA  . ARG B 1 23  ? -45.81400 10.50600  -30.84200 1.000 40.71821  ? 23  ARG B CA  1 
ATOM   2384 C  C   . ARG B 1 23  ? -46.02800 11.88500  -30.22300 1.000 42.62115  ? 23  ARG B C   1 
ATOM   2385 O  O   . ARG B 1 23  ? -45.92300 12.89900  -30.92200 1.000 41.61028  ? 23  ARG B O   1 
ATOM   2386 C  CB  . ARG B 1 23  ? -47.14200 9.90800   -31.30300 1.000 46.08956  ? 23  ARG B CB  1 
ATOM   2387 C  CG  . ARG B 1 23  ? -47.01800 9.09900   -32.58000 1.000 51.37434  ? 23  ARG B CG  1 
ATOM   2388 C  CD  . ARG B 1 23  ? -48.35300 8.75800   -33.15600 1.000 54.14466  ? 23  ARG B CD  1 
ATOM   2389 N  NE  . ARG B 1 23  ? -48.90900 7.57400   -32.52100 1.000 58.30730  ? 23  ARG B NE  1 
ATOM   2390 C  CZ  . ARG B 1 23  ? -48.67400 6.33300   -32.92100 1.000 57.10429  ? 23  ARG B CZ  1 
ATOM   2391 N  NH1 . ARG B 1 23  ? -47.87300 6.07800   -33.94400 1.000 63.58052  ? 23  ARG B NH1 1 
ATOM   2392 N  NH2 . ARG B 1 23  ? -49.26000 5.32400   -32.27800 1.000 59.97779  ? 23  ARG B NH2 1 
ATOM   2393 N  N   . LEU B 1 24  ? -46.31700 11.94300  -28.91700 1.000 39.23188  ? 24  LEU B N   1 
ATOM   2394 C  CA  . LEU B 1 24  ? -46.39300 13.23000  -28.22900 1.000 41.80117  ? 24  LEU B CA  1 
ATOM   2395 C  C   . LEU B 1 24  ? -45.12100 14.03500  -28.42800 1.000 39.85840  ? 24  LEU B C   1 
ATOM   2396 O  O   . LEU B 1 24  ? -45.17200 15.25700  -28.62800 1.000 37.04706  ? 24  LEU B O   1 
ATOM   2397 C  CB  . LEU B 1 24  ? -46.64000 13.02100  -26.73800 1.000 38.68510  ? 24  LEU B CB  1 
ATOM   2398 C  CG  . LEU B 1 24  ? -48.09900 13.03800  -26.30800 1.000 40.58584  ? 24  LEU B CG  1 
ATOM   2399 C  CD1 . LEU B 1 24  ? -48.20600 12.79800  -24.81900 1.000 36.79779  ? 24  LEU B CD1 1 
ATOM   2400 C  CD2 . LEU B 1 24  ? -48.71800 14.36400  -26.69200 1.000 42.72843  ? 24  LEU B CD2 1 
ATOM   2401 N  N   . LEU B 1 25  ? -43.96500 13.36500  -28.36200 1.000 37.33031  ? 25  LEU B N   1 
ATOM   2402 C  CA  . LEU B 1 25  ? -42.69400 14.05400  -28.53100 1.000 39.03037  ? 25  LEU B CA  1 
ATOM   2403 C  C   . LEU B 1 25  ? -42.52400 14.59300  -29.94600 1.000 40.24269  ? 25  LEU B C   1 
ATOM   2404 O  O   . LEU B 1 25  ? -41.88900 15.63300  -30.14100 1.000 39.45406  ? 25  LEU B O   1 
ATOM   2405 C  CB  . LEU B 1 25  ? -41.54000 13.11300  -28.17700 1.000 39.96953  ? 25  LEU B CB  1 
ATOM   2406 C  CG  . LEU B 1 25  ? -41.29000 12.87400  -26.68500 1.000 35.68726  ? 25  LEU B CG  1 
ATOM   2407 C  CD1 . LEU B 1 25  ? -40.17200 11.85500  -26.47000 1.000 36.38160  ? 25  LEU B CD1 1 
ATOM   2408 C  CD2 . LEU B 1 25  ? -40.95300 14.18100  -25.98400 1.000 32.27341  ? 25  LEU B CD2 1 
ATOM   2409 N  N   . GLU B 1 26  ? -43.06200 13.91000  -30.94800 1.000 39.60005  ? 26  GLU B N   1 
ATOM   2410 C  CA  . GLU B 1 26  ? -42.87200 14.40900  -32.30400 1.000 39.20144  ? 26  GLU B CA  1 
ATOM   2411 C  C   . GLU B 1 26  ? -43.86000 15.51500  -32.65500 1.000 40.59738  ? 26  GLU B C   1 
ATOM   2412 O  O   . GLU B 1 26  ? -43.52700 16.40600  -33.44000 1.000 42.40157  ? 26  GLU B O   1 
ATOM   2413 C  CB  . GLU B 1 26  ? -42.96100 13.25500  -33.29800 1.000 42.68563  ? 26  GLU B CB  1 
ATOM   2414 C  CG  . GLU B 1 26  ? -41.76600 12.31200  -33.19000 1.000 53.22933  ? 26  GLU B CG  1 
ATOM   2415 C  CD  . GLU B 1 26  ? -40.41100 13.03400  -33.31400 1.000 52.83807  ? 26  GLU B CD  1 
ATOM   2416 O  OE1 . GLU B 1 26  ? -40.07700 13.50400  -34.43000 1.000 55.85025  ? 26  GLU B OE1 1 
ATOM   2417 O  OE2 . GLU B 1 26  ? -39.68800 13.13400  -32.29200 1.000 52.99390  ? 26  GLU B OE2 1 
ATOM   2418 N  N   . GLU B 1 27  ? -45.05700 15.49800  -32.06700 1.000 41.28723  ? 27  GLU B N   1 
ATOM   2419 C  CA  . GLU B 1 27  ? -46.09300 16.48200  -32.36900 1.000 41.37497  ? 27  GLU B CA  1 
ATOM   2420 C  C   . GLU B 1 27  ? -45.98000 17.72400  -31.47900 1.000 40.82195  ? 27  GLU B C   1 
ATOM   2421 O  O   . GLU B 1 27  ? -45.82500 18.83900  -31.98800 1.000 41.53525  ? 27  GLU B O   1 
ATOM   2422 C  CB  . GLU B 1 27  ? -47.47200 15.81400  -32.23900 1.000 47.10563  ? 27  GLU B CB  1 
ATOM   2423 C  CG  . GLU B 1 27  ? -47.55700 14.47100  -32.99700 1.000 50.81807  ? 27  GLU B CG  1 
ATOM   2424 C  CD  . GLU B 1 27  ? -48.97500 13.94300  -33.17100 1.000 67.67020  ? 27  GLU B CD  1 
ATOM   2425 O  OE1 . GLU B 1 27  ? -49.92700 14.74600  -33.07800 1.000 73.37096  ? 27  GLU B OE1 1 
ATOM   2426 O  OE2 . GLU B 1 27  ? -49.13800 12.72000  -33.41000 1.000 67.23348  ? 27  GLU B OE2 1 
ATOM   2427 N  N   . ASP B 1 28  ? -46.03900 17.53800  -30.14600 1.000 40.11730  ? 28  ASP B N   1 
ATOM   2428 C  CA  . ASP B 1 28  ? -45.90000 18.59200  -29.14100 1.000 37.82137  ? 28  ASP B CA  1 
ATOM   2429 C  C   . ASP B 1 28  ? -44.44500 18.88300  -28.76200 1.000 37.18534  ? 28  ASP B C   1 
ATOM   2430 O  O   . ASP B 1 28  ? -44.08100 20.03900  -28.52900 1.000 37.35109  ? 28  ASP B O   1 
ATOM   2431 C  CB  . ASP B 1 28  ? -46.66400 18.21300  -27.87100 1.000 38.62598  ? 28  ASP B CB  1 
ATOM   2432 C  CG  . ASP B 1 28  ? -48.17000 18.37800  -28.01700 1.000 44.97713  ? 28  ASP B CG  1 
ATOM   2433 O  OD1 . ASP B 1 28  ? -48.63400 18.68300  -29.13700 1.000 47.50629  ? 28  ASP B OD1 1 
ATOM   2434 O  OD2 . ASP B 1 28  ? -48.89500 18.20700  -27.00500 1.000 48.98549  ? 28  ASP B OD2 1 
ATOM   2435 N  N   . GLY B 1 29  ? -43.60200 17.86400  -28.66800 1.000 35.64462  ? 29  GLY B N   1 
ATOM   2436 C  CA  . GLY B 1 29  ? -42.21400 18.06800  -28.31600 1.000 32.61884  ? 29  GLY B CA  1 
ATOM   2437 C  C   . GLY B 1 29  ? -41.91500 17.93100  -26.84600 1.000 30.71566  ? 29  GLY B C   1 
ATOM   2438 O  O   . GLY B 1 29  ? -40.74600 18.03100  -26.45700 1.000 31.48732  ? 29  GLY B O   1 
ATOM   2439 N  N   . ALA B 1 30  ? -42.92900 17.69900  -26.01900 1.000 35.01823  ? 30  ALA B N   1 
ATOM   2440 C  CA  . ALA B 1 30  ? -42.74300 17.59800  -24.57700 1.000 32.39712  ? 30  ALA B CA  1 
ATOM   2441 C  C   . ALA B 1 30  ? -43.99300 16.98800  -23.96500 1.000 31.77754  ? 30  ALA B C   1 
ATOM   2442 O  O   . ALA B 1 30  ? -45.08600 17.09000  -24.53000 1.000 31.15952  ? 30  ALA B O   1 
ATOM   2443 C  CB  . ALA B 1 30  ? -42.45000 18.96600  -23.94500 1.000 27.71042  ? 30  ALA B CB  1 
ATOM   2444 N  N   . PHE B 1 31  ? -43.81500 16.34400  -22.81300 1.000 30.47241  ? 31  PHE B N   1 
ATOM   2445 C  CA  . PHE B 1 31  ? -44.93900 15.88200  -21.99800 1.000 34.31434  ? 31  PHE B CA  1 
ATOM   2446 C  C   . PHE B 1 31  ? -44.43100 15.58800  -20.58600 1.000 35.88599  ? 31  PHE B C   1 
ATOM   2447 O  O   . PHE B 1 31  ? -43.22200 15.60500  -20.32300 1.000 34.56284  ? 31  PHE B O   1 
ATOM   2448 C  CB  . PHE B 1 31  ? -45.63000 14.65600  -22.60600 1.000 33.56760  ? 31  PHE B CB  1 
ATOM   2449 C  CG  . PHE B 1 31  ? -44.80500 13.40600  -22.55200 1.000 34.96046  ? 31  PHE B CG  1 
ATOM   2450 C  CD1 . PHE B 1 31  ? -43.88200 13.12200  -23.55600 1.000 31.50598  ? 31  PHE B CD1 1 
ATOM   2451 C  CD2 . PHE B 1 31  ? -44.95200 12.51000  -21.50000 1.000 35.21568  ? 31  PHE B CD2 1 
ATOM   2452 C  CE1 . PHE B 1 31  ? -43.11400 11.96000  -23.50200 1.000 38.40836  ? 31  PHE B CE1 1 
ATOM   2453 C  CE2 . PHE B 1 31  ? -44.18300 11.35900  -21.43600 1.000 34.61273  ? 31  PHE B CE2 1 
ATOM   2454 C  CZ  . PHE B 1 31  ? -43.26600 11.07200  -22.43700 1.000 35.06934  ? 31  PHE B CZ  1 
ATOM   2455 N  N   . ILE B 1 32  ? -45.38100 15.33900  -19.67900 1.000 35.72602  ? 32  ILE B N   1 
ATOM   2456 C  CA  . ILE B 1 32  ? -45.11500 15.12800  -18.25800 1.000 35.42789  ? 32  ILE B CA  1 
ATOM   2457 C  C   . ILE B 1 32  ? -45.57600 13.72700  -17.86600 1.000 36.46419  ? 32  ILE B C   1 
ATOM   2458 O  O   . ILE B 1 32  ? -46.68500 13.31500  -18.21500 1.000 37.72984  ? 32  ILE B O   1 
ATOM   2459 C  CB  . ILE B 1 32  ? -45.82100 16.18400  -17.38900 1.000 33.04544  ? 32  ILE B CB  1 
ATOM   2460 C  CG1 . ILE B 1 32  ? -45.15200 17.54900  -17.55500 1.000 35.58635  ? 32  ILE B CG1 1 
ATOM   2461 C  CG2 . ILE B 1 32  ? -45.84900 15.75500  -15.90100 1.000 32.87493  ? 32  ILE B CG2 1 
ATOM   2462 C  CD1 . ILE B 1 32  ? -46.01200 18.70100  -17.07600 1.000 32.98838  ? 32  ILE B CD1 1 
ATOM   2463 N  N   . LEU B 1 33  ? -44.72600 13.00100  -17.14500 1.000 34.57956  ? 33  LEU B N   1 
ATOM   2464 C  CA  . LEU B 1 33  ? -45.11300 11.74900  -16.51300 1.000 34.60583  ? 33  LEU B CA  1 
ATOM   2465 C  C   . LEU B 1 33  ? -45.52100 12.06700  -15.08200 1.000 34.88380  ? 33  LEU B C   1 
ATOM   2466 O  O   . LEU B 1 33  ? -44.70400 12.55700  -14.29600 1.000 35.05813  ? 33  LEU B O   1 
ATOM   2467 C  CB  . LEU B 1 33  ? -43.96700 10.73700  -16.53600 1.000 37.37979  ? 33  LEU B CB  1 
ATOM   2468 C  CG  . LEU B 1 33  ? -43.62400 10.10300  -17.88400 1.000 39.45832  ? 33  LEU B CG  1 
ATOM   2469 C  CD1 . LEU B 1 33  ? -42.28600 9.36500   -17.82400 1.000 39.25085  ? 33  LEU B CD1 1 
ATOM   2470 C  CD2 . LEU B 1 33  ? -44.74000 9.17500   -18.30100 1.000 36.75214  ? 33  LEU B CD2 1 
ATOM   2471 N  N   . LYS B 1 34  ? -46.77400 11.79300  -14.74600 1.000 36.19093  ? 34  LYS B N   1 
ATOM   2472 C  CA  . LYS B 1 34  ? -47.30900 12.18100  -13.44900 1.000 37.96417  ? 34  LYS B CA  1 
ATOM   2473 C  C   . LYS B 1 34  ? -46.98100 11.11700  -12.40700 1.000 40.27095  ? 34  LYS B C   1 
ATOM   2474 O  O   . LYS B 1 34  ? -47.21800 9.92600   -12.62700 1.000 40.93394  ? 34  LYS B O   1 
ATOM   2475 C  CB  . LYS B 1 34  ? -48.81800 12.39100  -13.54800 1.000 38.99155  ? 34  LYS B CB  1 
ATOM   2476 C  CG  . LYS B 1 34  ? -49.41500 13.12500  -12.35800 1.000 49.75318  ? 34  LYS B CG  1 
ATOM   2477 C  CD  . LYS B 1 34  ? -49.15100 14.63200  -12.44400 1.000 50.32582  ? 34  LYS B CD  1 
ATOM   2478 C  CE  . LYS B 1 34  ? -49.58100 15.36400  -11.16900 1.000 53.43216  ? 34  LYS B CE  1 
ATOM   2479 N  NZ  . LYS B 1 34  ? -48.74900 15.01500  -9.96100  1.000 52.10314  ? 34  LYS B NZ  1 
ATOM   2480 N  N   . GLY B 1 35  ? -46.41900 11.54700  -11.27900 1.000 40.64317  ? 35  GLY B N   1 
ATOM   2481 C  CA  . GLY B 1 35  ? -46.19300 10.64000  -10.16200 1.000 36.31582  ? 35  GLY B CA  1 
ATOM   2482 C  C   . GLY B 1 35  ? -45.30200 9.45500   -10.46900 1.000 38.37675  ? 35  GLY B C   1 
ATOM   2483 O  O   . GLY B 1 35  ? -45.51900 8.37000   -9.92300  1.000 40.57255  ? 35  GLY B O   1 
ATOM   2484 N  N   . LEU B 1 36  ? -44.30600 9.62400   -11.34100 1.000 35.19407  ? 36  LEU B N   1 
ATOM   2485 C  CA  . LEU B 1 36  ? -43.40700 8.51500   -11.65500 1.000 39.49213  ? 36  LEU B CA  1 
ATOM   2486 C  C   . LEU B 1 36  ? -42.63800 8.05300   -10.42000 1.000 38.01614  ? 36  LEU B C   1 
ATOM   2487 O  O   . LEU B 1 36  ? -42.56200 6.85400   -10.12600 1.000 39.44516  ? 36  LEU B O   1 
ATOM   2488 C  CB  . LEU B 1 36  ? -42.43000 8.91600   -12.76400 1.000 34.77602  ? 36  LEU B CB  1 
ATOM   2489 C  CG  . LEU B 1 36  ? -41.42600 7.80700   -13.09100 1.000 38.55551  ? 36  LEU B CG  1 
ATOM   2490 C  CD1 . LEU B 1 36  ? -42.13800 6.55900   -13.61900 1.000 39.02247  ? 36  LEU B CD1 1 
ATOM   2491 C  CD2 . LEU B 1 36  ? -40.33600 8.26600   -14.05800 1.000 36.85146  ? 36  LEU B CD2 1 
ATOM   2492 N  N   . LEU B 1 37  ? -42.04700 8.98700   -9.69400  1.000 35.88569  ? 37  LEU B N   1 
ATOM   2493 C  CA  . LEU B 1 37  ? -41.20300 8.63700   -8.56400  1.000 38.95075  ? 37  LEU B CA  1 
ATOM   2494 C  C   . LEU B 1 37  ? -41.99600 8.76800   -7.27700  1.000 38.80300  ? 37  LEU B C   1 
ATOM   2495 O  O   . LEU B 1 37  ? -42.54600 9.84600   -7.00600  1.000 38.44543  ? 37  LEU B O   1 
ATOM   2496 C  CB  . LEU B 1 37  ? -39.97500 9.53600   -8.52000  1.000 37.42096  ? 37  LEU B CB  1 
ATOM   2497 C  CG  . LEU B 1 37  ? -39.16900 9.58500   -9.81000  1.000 35.47373  ? 37  LEU B CG  1 
ATOM   2498 C  CD1 . LEU B 1 37  ? -38.03400 10.55300  -9.63400  1.000 30.42873  ? 37  LEU B CD1 1 
ATOM   2499 C  CD2 . LEU B 1 37  ? -38.67100 8.18100   -10.15100 1.000 37.48724  ? 37  LEU B CD2 1 
ATOM   2500 N  N   . PRO B 1 38  ? -42.08900 7.72400   -6.46200  1.000 38.86320  ? 38  PRO B N   1 
ATOM   2501 C  CA  . PRO B 1 38  ? -42.78400 7.86500   -5.17900  1.000 42.90771  ? 38  PRO B CA  1 
ATOM   2502 C  C   . PRO B 1 38  ? -42.10100 8.90600   -4.30400  1.000 42.62265  ? 38  PRO B C   1 
ATOM   2503 O  O   . PRO B 1 38  ? -40.91800 9.22500   -4.46700  1.000 41.64143  ? 38  PRO B O   1 
ATOM   2504 C  CB  . PRO B 1 38  ? -42.70400 6.46100   -4.56200  1.000 39.15029  ? 38  PRO B CB  1 
ATOM   2505 C  CG  . PRO B 1 38  ? -41.59400 5.78000   -5.29500  1.000 44.04658  ? 38  PRO B CG  1 
ATOM   2506 C  CD  . PRO B 1 38  ? -41.54500 6.37200   -6.66700  1.000 38.46785  ? 38  PRO B CD  1 
ATOM   2507 N  N   . PHE B 1 39  ? -42.87900 9.45000   -3.37200  1.000 41.43301  ? 39  PHE B N   1 
ATOM   2508 C  CA  . PHE B 1 39  ? -42.38800 10.53200  -2.52700  1.000 45.46718  ? 39  PHE B CA  1 
ATOM   2509 C  C   . PHE B 1 39  ? -41.19800 10.11600  -1.66600  1.000 43.23728  ? 39  PHE B C   1 
ATOM   2510 O  O   . PHE B 1 39  ? -40.34200 10.95400  -1.35900  1.000 45.92277  ? 39  PHE B O   1 
ATOM   2511 C  CB  . PHE B 1 39  ? -43.51200 11.04300  -1.63600  1.000 48.24735  ? 39  PHE B CB  1 
ATOM   2512 C  CG  . PHE B 1 39  ? -43.16600 12.30100  -0.90000  1.000 53.15131  ? 39  PHE B CG  1 
ATOM   2513 C  CD1 . PHE B 1 39  ? -42.73000 13.42600  -1.59400  1.000 55.21017  ? 39  PHE B CD1 1 
ATOM   2514 C  CD2 . PHE B 1 39  ? -43.29100 12.36900  0.48700   1.000 56.29591  ? 39  PHE B CD2 1 
ATOM   2515 C  CE1 . PHE B 1 39  ? -42.41700 14.59700  -0.92100  1.000 53.28500  ? 39  PHE B CE1 1 
ATOM   2516 C  CE2 . PHE B 1 39  ? -42.98800 13.53500  1.16800   1.000 54.65069  ? 39  PHE B CE2 1 
ATOM   2517 C  CZ  . PHE B 1 39  ? -42.55000 14.65300  0.45900   1.000 57.62826  ? 39  PHE B CZ  1 
ATOM   2518 N  N   . ASP B 1 40  ? -41.11700 8.84700   -1.26400  1.000 40.83267  ? 40  ASP B N   1 
ATOM   2519 C  CA  . ASP B 1 40  ? -39.96400 8.41700   -0.47600  1.000 45.87874  ? 40  ASP B CA  1 
ATOM   2520 C  C   . ASP B 1 40  ? -38.68300 8.48700   -1.29900  1.000 44.89589  ? 40  ASP B C   1 
ATOM   2521 O  O   . ASP B 1 40  ? -37.62000 8.85000   -0.77700  1.000 43.69250  ? 40  ASP B O   1 
ATOM   2522 C  CB  . ASP B 1 40  ? -40.17200 7.00400   0.07800   1.000 45.85580  ? 40  ASP B CB  1 
ATOM   2523 C  CG  . ASP B 1 40  ? -40.11100 5.92000   -1.00600  1.000 56.27457  ? 40  ASP B CG  1 
ATOM   2524 O  OD1 . ASP B 1 40  ? -40.83300 6.03000   -2.02500  1.000 50.75487  ? 40  ASP B OD1 1 
ATOM   2525 O  OD2 . ASP B 1 40  ? -39.33600 4.94700   -0.83300  1.000 64.28278  ? 40  ASP B OD2 1 
ATOM   2526 N  N   . VAL B 1 41  ? -38.76800 8.15600   -2.59000  1.000 44.70903  ? 41  VAL B N   1 
ATOM   2527 C  CA  . VAL B 1 41  ? -37.60900 8.29300   -3.47300  1.000 39.96715  ? 41  VAL B CA  1 
ATOM   2528 C  C   . VAL B 1 41  ? -37.22100 9.75800   -3.60200  1.000 39.24002  ? 41  VAL B C   1 
ATOM   2529 O  O   . VAL B 1 41  ? -36.04000 10.12000  -3.50500  1.000 35.33173  ? 41  VAL B O   1 
ATOM   2530 C  CB  . VAL B 1 41  ? -37.90200 7.65900   -4.84500  1.000 38.65443  ? 41  VAL B CB  1 
ATOM   2531 C  CG1 . VAL B 1 41  ? -36.78600 7.98900   -5.86500  1.000 37.71929  ? 41  VAL B CG1 1 
ATOM   2532 C  CG2 . VAL B 1 41  ? -38.06600 6.14600   -4.69900  1.000 39.77833  ? 41  VAL B CG2 1 
ATOM   2533 N  N   . VAL B 1 42  ? -38.21400 10.62400  -3.81100  1.000 38.63314  ? 42  VAL B N   1 
ATOM   2534 C  CA  . VAL B 1 42  ? -37.94200 12.04600  -3.98800  1.000 40.92440  ? 42  VAL B CA  1 
ATOM   2535 C  C   . VAL B 1 42  ? -37.25400 12.60800  -2.75600  1.000 38.96726  ? 42  VAL B C   1 
ATOM   2536 O  O   . VAL B 1 42  ? -36.24400 13.31200  -2.85900  1.000 33.87570  ? 42  VAL B O   1 
ATOM   2537 C  CB  . VAL B 1 42  ? -39.23800 12.80900  -4.30900  1.000 40.47934  ? 42  VAL B CB  1 
ATOM   2538 C  CG1 . VAL B 1 42  ? -39.00300 14.30100  -4.19200  1.000 41.27464  ? 42  VAL B CG1 1 
ATOM   2539 C  CG2 . VAL B 1 42  ? -39.72600 12.44100  -5.70900  1.000 38.09891  ? 42  VAL B CG2 1 
ATOM   2540 N  N   . GLU B 1 43  ? -37.76100 12.26200  -1.56700  1.000 39.31360  ? 43  GLU B N   1 
ATOM   2541 C  CA  . GLU B 1 43  ? -37.18800 12.83600  -0.35700  1.000 38.81015  ? 43  GLU B CA  1 
ATOM   2542 C  C   . GLU B 1 43  ? -35.80800 12.25400  -0.04700  1.000 38.17104  ? 43  GLU B C   1 
ATOM   2543 O  O   . GLU B 1 43  ? -34.92700 12.99000  0.41100   1.000 38.93538  ? 43  GLU B O   1 
ATOM   2544 C  CB  . GLU B 1 43  ? -38.15000 12.67100  0.81900   1.000 46.62225  ? 43  GLU B CB  1 
ATOM   2545 C  CG  . GLU B 1 43  ? -39.38200 13.60100  0.75000   1.000 51.49745  ? 43  GLU B CG  1 
ATOM   2546 C  CD  . GLU B 1 43  ? -39.04600 15.09400  0.50700   1.000 54.76451  ? 43  GLU B CD  1 
ATOM   2547 O  OE1 . GLU B 1 43  ? -38.70800 15.48600  -0.64000  1.000 47.59461  ? 43  GLU B OE1 1 
ATOM   2548 O  OE2 . GLU B 1 43  ? -39.13900 15.88300  1.47500   1.000 59.85024  ? 43  GLU B OE2 1 
ATOM   2549 N  N   . SER B 1 44  ? -35.58400 10.95500  -0.29300  1.000 36.01896  ? 44  SER B N   1 
ATOM   2550 C  CA  . SER B 1 44  ? -34.22200 10.42100  -0.17500  1.000 38.35300  ? 44  SER B CA  1 
ATOM   2551 C  C   . SER B 1 44  ? -33.25400 11.16500  -1.09500  1.000 35.91975  ? 44  SER B C   1 
ATOM   2552 O  O   . SER B 1 44  ? -32.12800 11.49600  -0.70100  1.000 32.33747  ? 44  SER B O   1 
ATOM   2553 C  CB  . SER B 1 44  ? -34.17800 8.92900   -0.51100  1.000 36.69502  ? 44  SER B CB  1 
ATOM   2554 O  OG  . SER B 1 44  ? -35.02800 8.18200   0.32200   1.000 49.56333  ? 44  SER B OG  1 
ATOM   2555 N  N   . PHE B 1 45  ? -33.66700 11.40000  -2.34400  1.000 33.46212  ? 45  PHE B N   1 
ATOM   2556 C  CA  . PHE B 1 45  ? -32.82900 12.12500  -3.29600  1.000 33.18138  ? 45  PHE B CA  1 
ATOM   2557 C  C   . PHE B 1 45  ? -32.54900 13.54700  -2.80100  1.000 33.71424  ? 45  PHE B C   1 
ATOM   2558 O  O   . PHE B 1 45  ? -31.40200 14.00400  -2.81300  1.000 32.91633  ? 45  PHE B O   1 
ATOM   2559 C  CB  . PHE B 1 45  ? -33.51900 12.12400  -4.66700  1.000 34.31937  ? 45  PHE B CB  1 
ATOM   2560 C  CG  . PHE B 1 45  ? -32.63300 12.54600  -5.83400  1.000 33.81690  ? 45  PHE B CG  1 
ATOM   2561 C  CD1 . PHE B 1 45  ? -31.25600 12.63000  -5.70600  1.000 32.71264  ? 45  PHE B CD1 1 
ATOM   2562 C  CD2 . PHE B 1 45  ? -33.20800 12.85900  -7.06400  1.000 31.40382  ? 45  PHE B CD2 1 
ATOM   2563 C  CE1 . PHE B 1 45  ? -30.46300 13.01900  -6.77500  1.000 32.98980  ? 45  PHE B CE1 1 
ATOM   2564 C  CE2 . PHE B 1 45  ? -32.42800 13.25500  -8.13900  1.000 30.93912  ? 45  PHE B CE2 1 
ATOM   2565 C  CZ  . PHE B 1 45  ? -31.05000 13.32600  -8.00100  1.000 33.37281  ? 45  PHE B CZ  1 
ATOM   2566 N  N   . ASN B 1 46  ? -33.58700 14.25300  -2.32800  1.000 34.07768  ? 46  ASN B N   1 
ATOM   2567 C  CA  . ASN B 1 46  ? -33.38400 15.59400  -1.78200  1.000 35.29379  ? 46  ASN B CA  1 
ATOM   2568 C  C   . ASN B 1 46  ? -32.38100 15.59700  -0.63200  1.000 35.65772  ? 46  ASN B C   1 
ATOM   2569 O  O   . ASN B 1 46  ? -31.54200 16.50300  -0.54600  1.000 34.65660  ? 46  ASN B O   1 
ATOM   2570 C  CB  . ASN B 1 46  ? -34.71400 16.20600  -1.33300  1.000 35.53322  ? 46  ASN B CB  1 
ATOM   2571 C  CG  . ASN B 1 46  ? -35.39000 16.97000  -2.44300  1.000 37.65952  ? 46  ASN B CG  1 
ATOM   2572 O  OD1 . ASN B 1 46  ? -34.72000 17.53000  -3.31700  1.000 36.72955  ? 46  ASN B OD1 1 
ATOM   2573 N  ND2 . ASN B 1 46  ? -36.71500 16.98500  -2.43500  1.000 35.12871  ? 46  ASN B ND2 1 
ATOM   2574 N  N   . ARG B 1 47  ? -32.43600 14.59900  0.26100   1.000 34.33142  ? 47  ARG B N   1 
ATOM   2575 C  CA  . ARG B 1 47  ? -31.50200 14.61500  1.39100   1.000 37.61826  ? 47  ARG B CA  1 
ATOM   2576 C  C   . ARG B 1 47  ? -30.06400 14.36900  0.93900   1.000 35.16731  ? 47  ARG B C   1 
ATOM   2577 O  O   . ARG B 1 47  ? -29.13200 15.00700  1.44900   1.000 37.61990  ? 47  ARG B O   1 
ATOM   2578 C  CB  . ARG B 1 47  ? -31.90800 13.59500  2.45800   1.000 39.30689  ? 47  ARG B CB  1 
ATOM   2579 C  CG  . ARG B 1 47  ? -33.31100 13.77000  3.01100   1.000 48.33268  ? 47  ARG B CG  1 
ATOM   2580 C  CD  . ARG B 1 47  ? -33.51400 15.03300  3.88500   1.000 53.62539  ? 47  ARG B CD  1 
ATOM   2581 N  NE  . ARG B 1 47  ? -33.54900 16.28400  3.12400   1.000 51.02212  ? 47  ARG B NE  1 
ATOM   2582 C  CZ  . ARG B 1 47  ? -34.57700 16.70200  2.39300   1.000 51.34969  ? 47  ARG B CZ  1 
ATOM   2583 N  NH1 . ARG B 1 47  ? -35.67800 15.97100  2.25500   1.000 51.52230  ? 47  ARG B NH1 1 
ATOM   2584 N  NH2 . ARG B 1 47  ? -34.50100 17.88600  1.78900   1.000 45.90223  ? 47  ARG B NH2 1 
ATOM   2585 N  N   . GLU B 1 48  ? -29.85500 13.44300  -0.00300  1.000 33.15796  ? 48  GLU B N   1 
ATOM   2586 C  CA  . GLU B 1 48  ? -28.51300 13.25400  -0.56200  1.000 33.50075  ? 48  GLU B CA  1 
ATOM   2587 C  C   . GLU B 1 48  ? -27.99700 14.54200  -1.19600  1.000 34.13335  ? 48  GLU B C   1 
ATOM   2588 O  O   . GLU B 1 48  ? -26.83900 14.92800  -0.99100  1.000 32.23920  ? 48  GLU B O   1 
ATOM   2589 C  CB  . GLU B 1 48  ? -28.52600 12.10200  -1.57700  1.000 33.16801  ? 48  GLU B CB  1 
ATOM   2590 C  CG  . GLU B 1 48  ? -28.91100 10.76000  -0.93200  1.000 34.19293  ? 48  GLU B CG  1 
ATOM   2591 C  CD  . GLU B 1 48  ? -29.38500 9.68000   -1.92700  1.000 38.84319  ? 48  GLU B CD  1 
ATOM   2592 O  OE1 . GLU B 1 48  ? -29.29500 9.89100   -3.15000  1.000 35.85030  ? 48  GLU B OE1 1 
ATOM   2593 O  OE2 . GLU B 1 48  ? -29.85900 8.60500   -1.47400  1.000 40.83710  ? 48  GLU B OE2 1 
ATOM   2594 N  N   . LEU B 1 49  ? -28.85100 15.23200  -1.95300  1.000 34.48768  ? 49  LEU B N   1 
ATOM   2595 C  CA  . LEU B 1 49  ? -28.46600 16.50300  -2.55900  1.000 33.88456  ? 49  LEU B CA  1 
ATOM   2596 C  C   . LEU B 1 49  ? -28.15300 17.55800  -1.50200  1.000 38.47963  ? 49  LEU B C   1 
ATOM   2597 O  O   . LEU B 1 49  ? -27.20700 18.34000  -1.66500  1.000 37.90862  ? 49  LEU B O   1 
ATOM   2598 C  CB  . LEU B 1 49  ? -29.57800 16.97900  -3.48800  1.000 32.59113  ? 49  LEU B CB  1 
ATOM   2599 C  CG  . LEU B 1 49  ? -29.72300 16.04300  -4.69100  1.000 33.33167  ? 49  LEU B CG  1 
ATOM   2600 C  CD1 . LEU B 1 49  ? -30.99600 16.32900  -5.39100  1.000 29.02871  ? 49  LEU B CD1 1 
ATOM   2601 C  CD2 . LEU B 1 49  ? -28.53700 16.25900  -5.66200  1.000 30.83463  ? 49  LEU B CD2 1 
ATOM   2602 N  N   . ASP B 1 50  ? -28.93800 17.59100  -0.41600  1.000 34.96549  ? 50  ASP B N   1 
ATOM   2603 C  CA  . ASP B 1 50  ? -28.67700 18.52900  0.68000   1.000 37.75439  ? 50  ASP B CA  1 
ATOM   2604 C  C   . ASP B 1 50  ? -27.27100 18.35400  1.24000   1.000 37.39850  ? 50  ASP B C   1 
ATOM   2605 O  O   . ASP B 1 50  ? -26.57500 19.34000  1.51200   1.000 37.70452  ? 50  ASP B O   1 
ATOM   2606 C  CB  . ASP B 1 50  ? -29.70200 18.34200  1.80200   1.000 34.04311  ? 50  ASP B CB  1 
ATOM   2607 C  CG  . ASP B 1 50  ? -31.05000 18.97100  1.49300   1.000 41.03191  ? 50  ASP B CG  1 
ATOM   2608 O  OD1 . ASP B 1 50  ? -31.18300 19.65400  0.45500   1.000 46.41027  ? 50  ASP B OD1 1 
ATOM   2609 O  OD2 . ASP B 1 50  ? -31.98800 18.78100  2.30200   1.000 46.32921  ? 50  ASP B OD2 1 
ATOM   2610 N  N   . VAL B 1 51  ? -26.84800 17.10000  1.42800   1.000 34.93521  ? 51  VAL B N   1 
ATOM   2611 C  CA  . VAL B 1 51  ? -25.49500 16.79900  1.89500   1.000 36.69711  ? 51  VAL B CA  1 
ATOM   2612 C  C   . VAL B 1 51  ? -24.45400 17.43500  0.98200   1.000 38.09964  ? 51  VAL B C   1 
ATOM   2613 O  O   . VAL B 1 51  ? -23.47800 18.03900  1.44600   1.000 33.87627  ? 51  VAL B O   1 
ATOM   2614 C  CB  . VAL B 1 51  ? -25.29700 15.27400  1.99200   1.000 36.46711  ? 51  VAL B CB  1 
ATOM   2615 C  CG1 . VAL B 1 51  ? -23.86700 14.94500  2.37300   1.000 36.87292  ? 51  VAL B CG1 1 
ATOM   2616 C  CG2 . VAL B 1 51  ? -26.26200 14.68700  3.01800   1.000 38.41117  ? 51  VAL B CG2 1 
ATOM   2617 N  N   . GLN B 1 52  ? -24.65000 17.30900  -0.33500  1.000 33.95753  ? 52  GLN B N   1 
ATOM   2618 C  CA  . GLN B 1 52  ? -23.67200 17.84100  -1.27600  1.000 35.86895  ? 52  GLN B CA  1 
ATOM   2619 C  C   . GLN B 1 52  ? -23.62600 19.36500  -1.23200  1.000 36.82534  ? 52  GLN B C   1 
ATOM   2620 O  O   . GLN B 1 52  ? -22.54100 19.95600  -1.25800  1.000 34.32082  ? 52  GLN B O   1 
ATOM   2621 C  CB  . GLN B 1 52  ? -23.98200 17.34300  -2.69000  1.000 34.09750  ? 52  GLN B CB  1 
ATOM   2622 C  CG  . GLN B 1 52  ? -23.83100 15.83400  -2.82500  1.000 32.06206  ? 52  GLN B CG  1 
ATOM   2623 C  CD  . GLN B 1 52  ? -22.49000 15.36400  -2.31800  1.000 34.10973  ? 52  GLN B CD  1 
ATOM   2624 O  OE1 . GLN B 1 52  ? -22.40500 14.57100  -1.37900  1.000 36.04198  ? 52  GLN B OE1 1 
ATOM   2625 N  NE2 . GLN B 1 52  ? -21.43500 15.85800  -2.92400  1.000 30.80939  ? 52  GLN B NE2 1 
ATOM   2626 N  N   . MET B 1 53  ? -24.78600 20.01800  -1.15600  1.000 35.39973  ? 53  MET B N   1 
ATOM   2627 C  CA  . MET B 1 53  ? -24.80300 21.47800  -1.11700  1.000 38.60962  ? 53  MET B CA  1 
ATOM   2628 C  C   . MET B 1 53  ? -24.25900 22.03400  0.18500   1.000 37.25822  ? 53  MET B C   1 
ATOM   2629 O  O   . MET B 1 53  ? -23.84500 23.19500  0.22000   1.000 43.42300  ? 53  MET B O   1 
ATOM   2630 C  CB  . MET B 1 53  ? -26.21400 21.99100  -1.36200  1.000 36.19287  ? 53  MET B CB  1 
ATOM   2631 C  CG  . MET B 1 53  ? -26.60700 21.83600  -2.82700  1.000 44.03174  ? 53  MET B CG  1 
ATOM   2632 S  SD  . MET B 1 53  ? -28.35400 22.10100  -3.14800  1.000 55.30191  ? 53  MET B SD  1 
ATOM   2633 C  CE  . MET B 1 53  ? -28.61900 23.70600  -2.40700  1.000 50.94000  ? 53  MET B CE  1 
ATOM   2634 N  N   . ALA B 1 54  ? -24.23900 21.23400  1.24600   1.000 40.11958  ? 54  ALA B N   1 
ATOM   2635 C  CA  . ALA B 1 54  ? -23.69700 21.65500  2.52800   1.000 41.46998  ? 54  ALA B CA  1 
ATOM   2636 C  C   . ALA B 1 54  ? -22.17900 21.67300  2.55400   1.000 43.33167  ? 54  ALA B C   1 
ATOM   2637 O  O   . ALA B 1 54  ? -21.60400 22.24400  3.48600   1.000 43.57874  ? 54  ALA B O   1 
ATOM   2638 C  CB  . ALA B 1 54  ? -24.20100 20.72900  3.63200   1.000 38.91058  ? 54  ALA B CB  1 
ATOM   2639 N  N   . ILE B 1 55  ? -21.53000 21.06900  1.56900   1.000 41.60733  ? 55  ILE B N   1 
ATOM   2640 C  CA  . ILE B 1 55  ? -20.07300 20.94300  1.58900   1.000 43.95717  ? 55  ILE B CA  1 
ATOM   2641 C  C   . ILE B 1 55  ? -19.44600 22.31500  1.38800   1.000 48.83343  ? 55  ILE B C   1 
ATOM   2642 O  O   . ILE B 1 55  ? -19.80000 23.02100  0.42400   1.000 49.41150  ? 55  ILE B O   1 
ATOM   2643 C  CB  . ILE B 1 55  ? -19.61400 19.96600  0.50900   1.000 44.02851  ? 55  ILE B CB  1 
ATOM   2644 C  CG1 . ILE B 1 55  ? -20.04000 18.54200  0.87800   1.000 40.91065  ? 55  ILE B CG1 1 
ATOM   2645 C  CG2 . ILE B 1 55  ? -18.10400 20.05900  0.32600   1.000 47.31276  ? 55  ILE B CG2 1 
ATOM   2646 C  CD1 . ILE B 1 55  ? -19.93500 17.54800  -0.27100  1.000 40.64450  ? 55  ILE B CD1 1 
ATOM   2647 N  N   . PRO B 1 56  ? -18.53000 22.73700  2.25700   1.000 51.96476  ? 56  PRO B N   1 
ATOM   2648 C  CA  . PRO B 1 56  ? -17.87700 24.02500  2.06400   1.000 56.11625  ? 56  PRO B CA  1 
ATOM   2649 C  C   . PRO B 1 56  ? -17.12200 24.04500  0.75200   1.000 63.21093  ? 56  PRO B C   1 
ATOM   2650 O  O   . PRO B 1 56  ? -16.57800 23.01200  0.31300   1.000 63.85394  ? 56  PRO B O   1 
ATOM   2651 C  CB  . PRO B 1 56  ? -16.92400 24.12400  3.26300   1.000 55.45675  ? 56  PRO B CB  1 
ATOM   2652 C  CG  . PRO B 1 56  ? -17.46900 23.16800  4.26400   1.000 52.66009  ? 56  PRO B CG  1 
ATOM   2653 C  CD  . PRO B 1 56  ? -18.05800 22.04900  3.47100   1.000 48.19182  ? 56  PRO B CD  1 
ATOM   2654 N  N   . PRO B 1 57  ? -17.04900 25.19900  0.09400   1.000 66.10150  ? 57  PRO B N   1 
ATOM   2655 C  CA  . PRO B 1 57  ? -16.48700 25.26100  -1.26200  1.000 70.01419  ? 57  PRO B CA  1 
ATOM   2656 C  C   . PRO B 1 57  ? -14.99700 24.96000  -1.26200  1.000 74.02562  ? 57  PRO B C   1 
ATOM   2657 O  O   . PRO B 1 57  ? -14.25600 25.41300  -0.37400  1.000 69.91923  ? 57  PRO B O   1 
ATOM   2658 C  CB  . PRO B 1 57  ? -16.76200 26.71100  -1.69600  1.000 70.38772  ? 57  PRO B CB  1 
ATOM   2659 C  CG  . PRO B 1 57  ? -17.73400 27.26400  -0.68300  1.000 66.32302  ? 57  PRO B CG  1 
ATOM   2660 C  CD  . PRO B 1 57  ? -17.45500 26.52800  0.58400   1.000 66.63396  ? 57  PRO B CD  1 
ATOM   2661 N  N   . PRO B 1 58  ? -14.52300 24.19700  -2.24500  1.000 79.73494  ? 58  PRO B N   1 
ATOM   2662 C  CA  . PRO B 1 58  ? -13.10300 23.82500  -2.28700  1.000 82.74955  ? 58  PRO B CA  1 
ATOM   2663 C  C   . PRO B 1 58  ? -12.21100 25.02500  -2.56200  1.000 84.16499  ? 58  PRO B C   1 
ATOM   2664 O  O   . PRO B 1 58  ? -12.65300 26.10300  -2.96600  1.000 82.65481  ? 58  PRO B O   1 
ATOM   2665 C  CB  . PRO B 1 58  ? -13.02600 22.81400  -3.43600  1.000 81.27992  ? 58  PRO B CB  1 
ATOM   2666 C  CG  . PRO B 1 58  ? -14.43800 22.37300  -3.66900  1.000 81.28707  ? 58  PRO B CG  1 
ATOM   2667 C  CD  . PRO B 1 58  ? -15.29700 23.53800  -3.30700  1.000 80.29591  ? 58  PRO B CD  1 
ATOM   2668 N  N   . LYS B 1 59  ? -10.91300 24.81400  -2.34100  1.000 76.80777  ? 59  LYS B N   1 
ATOM   2669 C  CA  . LYS B 1 59  ? -9.93800  25.84900  -2.64500  1.000 78.11529  ? 59  LYS B CA  1 
ATOM   2670 C  C   . LYS B 1 59  ? -9.57800  25.88500  -4.12200  1.000 69.73884  ? 59  LYS B C   1 
ATOM   2671 O  O   . LYS B 1 59  ? -9.19400  26.94600  -4.62400  1.000 71.31162  ? 59  LYS B O   1 
ATOM   2672 C  CB  . LYS B 1 59  ? -8.67000  25.65200  -1.80700  1.000 74.43355  ? 59  LYS B CB  1 
ATOM   2673 N  N   . GLY B 1 60  ? -9.71600  24.76100  -4.82900  1.000 69.84385  ? 60  GLY B N   1 
ATOM   2674 C  CA  . GLY B 1 60  ? -9.26700  24.66100  -6.20000  1.000 61.48933  ? 60  GLY B CA  1 
ATOM   2675 C  C   . GLY B 1 60  ? -10.30800 25.10500  -7.21800  1.000 59.60285  ? 60  GLY B C   1 
ATOM   2676 O  O   . GLY B 1 60  ? -11.43800 25.47000  -6.88900  1.000 54.87083  ? 60  GLY B O   1 
ATOM   2677 N  N   . GLU B 1 61  ? -9.88600  25.05800  -8.48600  1.000 51.87104  ? 61  GLU B N   1 
ATOM   2678 C  CA  . GLU B 1 61  ? -10.72100 25.44600  -9.61900  1.000 49.94845  ? 61  GLU B CA  1 
ATOM   2679 C  C   . GLU B 1 61  ? -12.01700 24.63800  -9.67400  1.000 49.95572  ? 61  GLU B C   1 
ATOM   2680 O  O   . GLU B 1 61  ? -12.03300 23.43300  -9.40500  1.000 47.74561  ? 61  GLU B O   1 
ATOM   2681 C  CB  . GLU B 1 61  ? -9.92900  25.25500  -10.92000 1.000 50.06537  ? 61  GLU B CB  1 
ATOM   2682 C  CG  . GLU B 1 61  ? -10.76000 25.27900  -12.19700 1.000 48.67535  ? 61  GLU B CG  1 
ATOM   2683 C  CD  . GLU B 1 61  ? -9.94400  24.95900  -13.45300 1.000 54.19875  ? 61  GLU B CD  1 
ATOM   2684 O  OE1 . GLU B 1 61  ? -9.38100  23.83800  -13.55000 1.000 51.27578  ? 61  GLU B OE1 1 
ATOM   2685 O  OE2 . GLU B 1 61  ? -9.86500  25.83400  -14.35000 1.000 55.83556  ? 61  GLU B OE2 1 
ATOM   2686 N  N   . ARG B 1 62  ? -13.11700 25.31600  -10.01100 1.000 48.99359  ? 62  ARG B N   1 
ATOM   2687 C  CA  . ARG B 1 62  ? -14.38400 24.66700  -10.33000 1.000 43.04002  ? 62  ARG B CA  1 
ATOM   2688 C  C   . ARG B 1 62  ? -14.90000 25.22600  -11.64900 1.000 44.01345  ? 62  ARG B C   1 
ATOM   2689 O  O   . ARG B 1 62  ? -15.23000 26.41000  -11.73400 1.000 46.91002  ? 62  ARG B O   1 
ATOM   2690 C  CB  . ARG B 1 62  ? -15.40000 24.86400  -9.21100  1.000 47.41642  ? 62  ARG B CB  1 
ATOM   2691 C  CG  . ARG B 1 62  ? -15.22600 23.87700  -8.07200  1.000 51.09648  ? 62  ARG B CG  1 
ATOM   2692 C  CD  . ARG B 1 62  ? -15.38300 24.55900  -6.71900  1.000 64.14319  ? 62  ARG B CD  1 
ATOM   2693 N  NE  . ARG B 1 62  ? -16.67900 25.21100  -6.54100  1.000 65.98908  ? 62  ARG B NE  1 
ATOM   2694 C  CZ  . ARG B 1 62  ? -17.75700 24.62200  -6.04100  1.000 64.12661  ? 62  ARG B CZ  1 
ATOM   2695 N  NH1 . ARG B 1 62  ? -17.75000 23.34200  -5.69400  1.000 68.03278  ? 62  ARG B NH1 1 
ATOM   2696 N  NH2 . ARG B 1 62  ? -18.87000 25.33300  -5.88300  1.000 64.53881  ? 62  ARG B NH2 1 
ATOM   2697 N  N   . LEU B 1 63  ? -14.98900 24.36500  -12.66600 1.000 41.19668  ? 63  LEU B N   1 
ATOM   2698 C  CA  . LEU B 1 63  ? -15.13300 24.81700  -14.04800 1.000 39.12710  ? 63  LEU B CA  1 
ATOM   2699 C  C   . LEU B 1 63  ? -16.38300 25.67100  -14.24700 1.000 42.23274  ? 63  LEU B C   1 
ATOM   2700 O  O   . LEU B 1 63  ? -16.29600 26.81200  -14.70900 1.000 43.19339  ? 63  LEU B O   1 
ATOM   2701 C  CB  . LEU B 1 63  ? -15.13700 23.60900  -14.98900 1.000 39.07483  ? 63  LEU B CB  1 
ATOM   2702 C  CG  . LEU B 1 63  ? -13.78600 22.90000  -15.16900 1.000 42.82346  ? 63  LEU B CG  1 
ATOM   2703 C  CD1 . LEU B 1 63  ? -13.93600 21.61100  -15.97200 1.000 34.59633  ? 63  LEU B CD1 1 
ATOM   2704 C  CD2 . LEU B 1 63  ? -12.75100 23.82300  -15.82700 1.000 41.18067  ? 63  LEU B CD2 1 
ATOM   2705 N  N   . LEU B 1 64  ? -17.56000 25.14000  -13.90500 1.000 39.80612  ? 64  LEU B N   1 
ATOM   2706 C  CA  . LEU B 1 64  ? -18.78900 25.92200  -14.04800 1.000 43.20000  ? 64  LEU B CA  1 
ATOM   2707 C  C   . LEU B 1 64  ? -18.96000 26.93400  -12.91400 1.000 44.62347  ? 64  LEU B C   1 
ATOM   2708 O  O   . LEU B 1 64  ? -19.25600 28.11400  -13.15500 1.000 45.74892  ? 64  LEU B O   1 
ATOM   2709 C  CB  . LEU B 1 64  ? -20.00500 24.99100  -14.10500 1.000 42.33570  ? 64  LEU B CB  1 
ATOM   2710 C  CG  . LEU B 1 64  ? -21.32500 25.73900  -14.32100 1.000 44.33745  ? 64  LEU B CG  1 
ATOM   2711 C  CD1 . LEU B 1 64  ? -21.46500 26.20300  -15.77700 1.000 44.49330  ? 64  LEU B CD1 1 
ATOM   2712 C  CD2 . LEU B 1 64  ? -22.52700 24.90900  -13.88700 1.000 45.37344  ? 64  LEU B CD2 1 
ATOM   2713 N  N   . ALA B 1 65  ? -18.78400 26.48800  -11.66700 1.000 44.17700  ? 65  ALA B N   1 
ATOM   2714 C  CA  . ALA B 1 65  ? -19.15600 27.31700  -10.52100 1.000 44.96122  ? 65  ALA B CA  1 
ATOM   2715 C  C   . ALA B 1 65  ? -18.34200 28.60600  -10.44600 1.000 47.97388  ? 65  ALA B C   1 
ATOM   2716 O  O   . ALA B 1 65  ? -18.86100 29.63300  -9.99400  1.000 43.64158  ? 65  ALA B O   1 
ATOM   2717 C  CB  . ALA B 1 65  ? -19.00500 26.51800  -9.22900  1.000 45.85811  ? 65  ALA B CB  1 
ATOM   2718 N  N   . ASP B 1 66  ? -17.07900 28.58200  -10.88800 1.000 44.41531  ? 66  ASP B N   1 
ATOM   2719 C  CA  . ASP B 1 66  ? -16.22700 29.76200  -10.80000 1.000 47.90880  ? 66  ASP B CA  1 
ATOM   2720 C  C   . ASP B 1 66  ? -16.66800 30.88800  -11.72600 1.000 50.46632  ? 66  ASP B C   1 
ATOM   2721 O  O   . ASP B 1 66  ? -16.18600 32.01700  -11.57100 1.000 54.32921  ? 66  ASP B O   1 
ATOM   2722 C  CB  . ASP B 1 66  ? -14.77100 29.40400  -11.10800 1.000 49.83329  ? 66  ASP B CB  1 
ATOM   2723 C  CG  . ASP B 1 66  ? -14.08400 28.66200  -9.96500  1.000 51.29950  ? 66  ASP B CG  1 
ATOM   2724 O  OD1 . ASP B 1 66  ? -14.69300 28.48400  -8.87900  1.000 50.00626  ? 66  ASP B OD1 1 
ATOM   2725 O  OD2 . ASP B 1 66  ? -12.91900 28.25300  -10.16500 1.000 53.31342  ? 66  ASP B OD2 1 
ATOM   2726 N  N   . LYS B 1 67  ? -17.56100 30.61500  -12.67700 1.000 50.45600  ? 67  LYS B N   1 
ATOM   2727 C  CA  . LYS B 1 67  ? -18.10400 31.66000  -13.53300 1.000 49.99925  ? 67  LYS B CA  1 
ATOM   2728 C  C   . LYS B 1 67  ? -19.24600 32.42700  -12.88700 1.000 49.63991  ? 67  LYS B C   1 
ATOM   2729 O  O   . LYS B 1 67  ? -19.64600 33.46300  -13.42900 1.000 50.40394  ? 67  LYS B O   1 
ATOM   2730 C  CB  . LYS B 1 67  ? -18.58600 31.05600  -14.85400 1.000 51.82176  ? 67  LYS B CB  1 
ATOM   2731 C  CG  . LYS B 1 67  ? -17.49200 30.35000  -15.62800 1.000 52.19703  ? 67  LYS B CG  1 
ATOM   2732 C  CD  . LYS B 1 67  ? -18.06400 29.48100  -16.71700 1.000 51.91995  ? 67  LYS B CD  1 
ATOM   2733 C  CE  . LYS B 1 67  ? -17.14000 29.45600  -17.93000 1.000 57.30967  ? 67  LYS B CE  1 
ATOM   2734 N  NZ  . LYS B 1 67  ? -15.68900 29.31700  -17.57500 1.000 61.41383  ? 67  LYS B NZ  1 
ATOM   2735 N  N   . TYR B 1 68  ? -19.77400 31.95900  -11.75800 1.000 49.79534  ? 68  TYR B N   1 
ATOM   2736 C  CA  . TYR B 1 68  ? -20.98000 32.50500  -11.14800 1.000 50.49120  ? 68  TYR B CA  1 
ATOM   2737 C  C   . TYR B 1 68  ? -20.70100 33.04000  -9.74800  1.000 50.21207  ? 68  TYR B C   1 
ATOM   2738 O  O   . TYR B 1 68  ? -19.67100 32.71600  -9.14600  1.000 50.31691  ? 68  TYR B O   1 
ATOM   2739 C  CB  . TYR B 1 68  ? -22.07400 31.42600  -11.10100 1.000 47.70631  ? 68  TYR B CB  1 
ATOM   2740 C  CG  . TYR B 1 68  ? -22.44600 30.99400  -12.51100 1.000 54.66546  ? 68  TYR B CG  1 
ATOM   2741 C  CD1 . TYR B 1 68  ? -22.83700 31.96700  -13.43100 1.000 61.89323  ? 68  TYR B CD1 1 
ATOM   2742 C  CD2 . TYR B 1 68  ? -22.34400 29.66400  -12.91500 1.000 49.20454  ? 68  TYR B CD2 1 
ATOM   2743 C  CE1 . TYR B 1 68  ? -23.14900 31.59700  -14.71400 1.000 63.76408  ? 68  TYR B CE1 1 
ATOM   2744 C  CE2 . TYR B 1 68  ? -22.67000 29.32900  -14.20300 1.000 51.71269  ? 68  TYR B CE2 1 
ATOM   2745 C  CZ  . TYR B 1 68  ? -23.07300 30.27700  -15.13100 1.000 58.43496  ? 68  TYR B CZ  1 
ATOM   2746 O  OH  . TYR B 1 68  ? -23.39100 29.94100  -16.39700 1.000 63.31852  ? 68  TYR B OH  1 
ATOM   2747 N  N   . PRO B 1 69  ? -21.58300 33.88800  -9.21300  1.000 53.54089  ? 69  PRO B N   1 
ATOM   2748 C  CA  . PRO B 1 69  ? -21.40400 34.40400  -7.83000  1.000 56.51684  ? 69  PRO B CA  1 
ATOM   2749 C  C   . PRO B 1 69  ? -21.46600 33.28600  -6.80300  1.000 53.91940  ? 69  PRO B C   1 
ATOM   2750 O  O   . PRO B 1 69  ? -21.97100 32.19200  -7.09600  1.000 49.39394  ? 69  PRO B O   1 
ATOM   2751 C  CB  . PRO B 1 69  ? -22.58000 35.38000  -7.65300  1.000 55.56746  ? 69  PRO B CB  1 
ATOM   2752 C  CG  . PRO B 1 69  ? -23.02500 35.70300  -9.02800  1.000 57.25096  ? 69  PRO B CG  1 
ATOM   2753 C  CD  . PRO B 1 69  ? -22.73900 34.50200  -9.88700  1.000 53.05046  ? 69  PRO B CD  1 
ATOM   2754 N  N   . PRO B 1 70  ? -20.97800 33.53300  -5.57900  1.000 56.22892  ? 70  PRO B N   1 
ATOM   2755 C  CA  . PRO B 1 70  ? -20.90000 32.45500  -4.57600  1.000 56.51522  ? 70  PRO B CA  1 
ATOM   2756 C  C   . PRO B 1 70  ? -22.24100 31.85300  -4.18900  1.000 57.37432  ? 70  PRO B C   1 
ATOM   2757 O  O   . PRO B 1 70  ? -22.26900 30.71600  -3.70200  1.000 58.38213  ? 70  PRO B O   1 
ATOM   2758 C  CB  . PRO B 1 70  ? -20.24400 33.14300  -3.36900  1.000 56.79216  ? 70  PRO B CB  1 
ATOM   2759 C  CG  . PRO B 1 70  ? -19.57200 34.35900  -3.92000  1.000 59.82818  ? 70  PRO B CG  1 
ATOM   2760 C  CD  . PRO B 1 70  ? -20.41100 34.79900  -5.07700  1.000 58.37203  ? 70  PRO B CD  1 
ATOM   2761 N  N   . HIS B 1 71  ? -23.35000 32.57100  -4.37100  1.000 55.51391  ? 71  HIS B N   1 
ATOM   2762 C  CA  . HIS B 1 71  ? -24.65700 32.01800  -4.02400  1.000 54.89479  ? 71  HIS B CA  1 
ATOM   2763 C  C   . HIS B 1 71  ? -25.16100 30.98700  -5.04300  1.000 53.77533  ? 71  HIS B C   1 
ATOM   2764 O  O   . HIS B 1 71  ? -26.23700 30.42100  -4.83700  1.000 55.20630  ? 71  HIS B O   1 
ATOM   2765 C  CB  . HIS B 1 71  ? -25.66700 33.16000  -3.85700  1.000 52.49768  ? 71  HIS B CB  1 
ATOM   2766 C  CG  . HIS B 1 71  ? -25.86400 33.98000  -5.09200  1.000 57.97793  ? 71  HIS B CG  1 
ATOM   2767 N  ND1 . HIS B 1 71  ? -26.65400 33.56200  -6.14300  1.000 62.59133  ? 71  HIS B ND1 1 
ATOM   2768 C  CD2 . HIS B 1 71  ? -25.36800 35.19000  -5.45100  1.000 59.02050  ? 71  HIS B CD2 1 
ATOM   2769 C  CE1 . HIS B 1 71  ? -26.63600 34.47900  -7.09500  1.000 66.13405  ? 71  HIS B CE1 1 
ATOM   2770 N  NE2 . HIS B 1 71  ? -25.86800 35.48000  -6.69800  1.000 66.64040  ? 71  HIS B NE2 1 
ATOM   2771 N  N   . PHE B 1 72  ? -24.40500 30.73400  -6.11200  1.000 52.37177  ? 72  PHE B N   1 
ATOM   2772 C  CA  . PHE B 1 72  ? -24.76000 29.74600  -7.13000  1.000 50.68898  ? 72  PHE B CA  1 
ATOM   2773 C  C   . PHE B 1 72  ? -24.92800 28.35400  -6.52500  1.000 45.63271  ? 72  PHE B C   1 
ATOM   2774 O  O   . PHE B 1 72  ? -24.03400 27.85100  -5.83900  1.000 43.40378  ? 72  PHE B O   1 
ATOM   2775 C  CB  . PHE B 1 72  ? -23.66400 29.71900  -8.19400  1.000 45.43635  ? 72  PHE B CB  1 
ATOM   2776 C  CG  . PHE B 1 72  ? -23.96500 28.85300  -9.38800  1.000 47.62218  ? 72  PHE B CG  1 
ATOM   2777 C  CD1 . PHE B 1 72  ? -25.04900 29.12700  -10.21300 1.000 49.41833  ? 72  PHE B CD1 1 
ATOM   2778 C  CD2 . PHE B 1 72  ? -23.11800 27.80800  -9.72900  1.000 46.18734  ? 72  PHE B CD2 1 
ATOM   2779 C  CE1 . PHE B 1 72  ? -25.30100 28.34800  -11.33300 1.000 49.36469  ? 72  PHE B CE1 1 
ATOM   2780 C  CE2 . PHE B 1 72  ? -23.36200 27.02700  -10.85500 1.000 44.98334  ? 72  PHE B CE2 1 
ATOM   2781 C  CZ  . PHE B 1 72  ? -24.45500 27.30000  -11.65700 1.000 45.71565  ? 72  PHE B CZ  1 
ATOM   2782 N  N   . LYS B 1 73  ? -26.06000 27.71600  -6.81400  1.000 42.31435  ? 73  LYS B N   1 
ATOM   2783 C  CA  . LYS B 1 73  ? -26.40900 26.42000  -6.23000  1.000 42.08035  ? 73  LYS B CA  1 
ATOM   2784 C  C   . LYS B 1 73  ? -26.36800 25.35800  -7.32100  1.000 39.63945  ? 73  LYS B C   1 
ATOM   2785 O  O   . LYS B 1 73  ? -27.16200 25.39700  -8.26800  1.000 36.78986  ? 73  LYS B O   1 
ATOM   2786 C  CB  . LYS B 1 73  ? -27.78100 26.47100  -5.57200  1.000 41.59915  ? 73  LYS B CB  1 
ATOM   2787 C  CG  . LYS B 1 73  ? -27.89500 27.51200  -4.45400  1.000 49.93974  ? 73  LYS B CG  1 
ATOM   2788 C  CD  . LYS B 1 73  ? -27.11000 27.10200  -3.21400  1.000 50.82467  ? 73  LYS B CD  1 
ATOM   2789 C  CE  . LYS B 1 73  ? -27.28500 28.14400  -2.09100  1.000 56.01422  ? 73  LYS B CE  1 
ATOM   2790 N  NZ  . LYS B 1 73  ? -27.05300 27.54400  -0.74100  1.000 59.92684  ? 73  LYS B NZ  1 
ATOM   2791 N  N   . TYR B 1 74  ? -25.44700 24.41400  -7.18400  1.000 35.31686  ? 74  TYR B N   1 
ATOM   2792 C  CA  . TYR B 1 74  ? -25.15600 23.47900  -8.25800  1.000 34.64218  ? 74  TYR B CA  1 
ATOM   2793 C  C   . TYR B 1 74  ? -24.52000 22.23800  -7.65500  1.000 34.29939  ? 74  TYR B C   1 
ATOM   2794 O  O   . TYR B 1 74  ? -23.64400 22.34300  -6.79300  1.000 36.06031  ? 74  TYR B O   1 
ATOM   2795 C  CB  . TYR B 1 74  ? -24.22500 24.12500  -9.28100  1.000 35.78202  ? 74  TYR B CB  1 
ATOM   2796 C  CG  . TYR B 1 74  ? -23.73300 23.22900  -10.40800 1.000 38.06177  ? 74  TYR B CG  1 
ATOM   2797 C  CD1 . TYR B 1 74  ? -24.62000 22.76300  -11.38400 1.000 36.20692  ? 74  TYR B CD1 1 
ATOM   2798 C  CD2 . TYR B 1 74  ? -22.37900 22.89600  -10.48300 1.000 35.92122  ? 74  TYR B CD2 1 
ATOM   2799 C  CE1 . TYR B 1 74  ? -24.14800 21.96000  -12.39100 1.000 34.38348  ? 74  TYR B CE1 1 
ATOM   2800 C  CE2 . TYR B 1 74  ? -21.94400 22.09100  -11.50500 1.000 37.14834  ? 74  TYR B CE2 1 
ATOM   2801 C  CZ  . TYR B 1 74  ? -22.80800 21.61300  -12.47900 1.000 35.95695  ? 74  TYR B CZ  1 
ATOM   2802 O  OH  . TYR B 1 74  ? -22.34800 20.84800  -13.48800 1.000 37.98932  ? 74  TYR B OH  1 
ATOM   2803 N  N   . VAL B 1 75  ? -24.98400 21.07300  -8.08700  1.000 30.84370  ? 75  VAL B N   1 
ATOM   2804 C  CA  . VAL B 1 75  ? -24.34800 19.80400  -7.73100  1.000 30.45788  ? 75  VAL B CA  1 
ATOM   2805 C  C   . VAL B 1 75  ? -24.05400 19.05200  -9.02600  1.000 30.43747  ? 75  VAL B C   1 
ATOM   2806 O  O   . VAL B 1 75  ? -24.99500 18.65700  -9.72500  1.000 28.85923  ? 75  VAL B O   1 
ATOM   2807 C  CB  . VAL B 1 75  ? -25.23100 18.95700  -6.80300  1.000 32.08640  ? 75  VAL B CB  1 
ATOM   2808 C  CG1 . VAL B 1 75  ? -24.52400 17.64900  -6.46000  1.000 31.05653  ? 75  VAL B CG1 1 
ATOM   2809 C  CG2 . VAL B 1 75  ? -25.59200 19.73700  -5.51200  1.000 33.89011  ? 75  VAL B CG2 1 
ATOM   2810 N  N   . PRO B 1 76  ? -22.79000 18.86600  -9.40200  1.000 29.22172  ? 76  PRO B N   1 
ATOM   2811 C  CA  . PRO B 1 76  ? -22.48200 18.16100  -10.64600 1.000 30.23875  ? 76  PRO B CA  1 
ATOM   2812 C  C   . PRO B 1 76  ? -22.62000 16.65400  -10.47800 1.000 28.36805  ? 76  PRO B C   1 
ATOM   2813 O  O   . PRO B 1 76  ? -22.48700 16.11400  -9.38200  1.000 29.04946  ? 76  PRO B O   1 
ATOM   2814 C  CB  . PRO B 1 76  ? -21.02100 18.54500  -10.90500 1.000 29.15372  ? 76  PRO B CB  1 
ATOM   2815 C  CG  . PRO B 1 76  ? -20.43100 18.61600  -9.51000  1.000 30.71666  ? 76  PRO B CG  1 
ATOM   2816 C  CD  . PRO B 1 76  ? -21.56800 19.19800  -8.64200  1.000 30.79446  ? 76  PRO B CD  1 
ATOM   2817 N  N   . ASN B 1 77  ? -22.83400 15.98100  -11.61200 1.000 28.46028  ? 77  ASN B N   1 
ATOM   2818 C  CA  . ASN B 1 77  ? -22.82000 14.51900  -11.73900 1.000 29.35573  ? 77  ASN B CA  1 
ATOM   2819 C  C   . ASN B 1 77  ? -23.39200 13.81000  -10.51600 1.000 29.07971  ? 77  ASN B C   1 
ATOM   2820 O  O   . ASN B 1 77  ? -22.66200 13.17000  -9.75600  1.000 28.27300  ? 77  ASN B O   1 
ATOM   2821 C  CB  . ASN B 1 77  ? -21.40800 13.99100  -12.04900 1.000 28.52019  ? 77  ASN B CB  1 
ATOM   2822 C  CG  . ASN B 1 77  ? -20.31200 14.64600  -11.21100 1.000 31.53433  ? 77  ASN B CG  1 
ATOM   2823 O  OD1 . ASN B 1 77  ? -19.68500 15.60800  -11.64900 1.000 34.34345  ? 77  ASN B OD1 1 
ATOM   2824 N  ND2 . ASN B 1 77  ? -20.07000 14.12400  -10.01400 1.000 29.82364  ? 77  ASN B ND2 1 
ATOM   2825 N  N   . VAL B 1 78  ? -24.70800 13.92000  -10.33200 1.000 30.74960  ? 78  VAL B N   1 
ATOM   2826 C  CA  . VAL B 1 78  ? -25.31700 13.48600  -9.08000  1.000 32.11113  ? 78  VAL B CA  1 
ATOM   2827 C  C   . VAL B 1 78  ? -25.27000 11.97100  -8.92000  1.000 28.49090  ? 78  VAL B C   1 
ATOM   2828 O  O   . VAL B 1 78  ? -25.42200 11.47300  -7.80900  1.000 29.36904  ? 78  VAL B O   1 
ATOM   2829 C  CB  . VAL B 1 78  ? -26.75800 14.02200  -8.96600  1.000 29.68764  ? 78  VAL B CB  1 
ATOM   2830 C  CG1 . VAL B 1 78  ? -26.75600 15.55800  -8.78700  1.000 32.01291  ? 78  VAL B CG1 1 
ATOM   2831 C  CG2 . VAL B 1 78  ? -27.57600 13.61100  -10.17100 1.000 28.03111  ? 78  VAL B CG2 1 
ATOM   2832 N  N   . ALA B 1 79  ? -25.02200 11.22500  -9.99600  1.000 30.11438  ? 79  ALA B N   1 
ATOM   2833 C  CA  . ALA B 1 79  ? -24.96700 9.76700   -9.90600  1.000 30.78419  ? 79  ALA B CA  1 
ATOM   2834 C  C   . ALA B 1 79  ? -23.80800 9.25600   -9.05000  1.000 31.57795  ? 79  ALA B C   1 
ATOM   2835 O  O   . ALA B 1 79  ? -23.88400 8.13300   -8.54000  1.000 31.66594  ? 79  ALA B O   1 
ATOM   2836 C  CB  . ALA B 1 79  ? -24.88400 9.17400   -11.30900 1.000 29.84755  ? 79  ALA B CB  1 
ATOM   2837 N  N   . THR B 1 80  ? -22.73600 10.03700  -8.87300  1.000 27.89021  ? 80  THR B N   1 
ATOM   2838 C  CA  . THR B 1 80  ? -21.61900 9.55900   -8.06900  1.000 29.73298  ? 80  THR B CA  1 
ATOM   2839 C  C   . THR B 1 80  ? -21.78700 9.82400   -6.57300  1.000 33.19466  ? 80  THR B C   1 
ATOM   2840 O  O   . THR B 1 80  ? -21.10900 9.17400   -5.77000  1.000 35.61494  ? 80  THR B O   1 
ATOM   2841 C  CB  . THR B 1 80  ? -20.29800 10.19000  -8.52500  1.000 31.39871  ? 80  THR B CB  1 
ATOM   2842 O  OG1 . THR B 1 80  ? -20.31000 11.58700  -8.22600  1.000 34.08572  ? 80  THR B OG1 1 
ATOM   2843 C  CG2 . THR B 1 80  ? -20.07800 9.99800   -10.00900 1.000 31.12939  ? 80  THR B CG2 1 
ATOM   2844 N  N   . THR B 1 81  ? -22.65700 10.76200  -6.17800  1.000 32.17568  ? 81  THR B N   1 
ATOM   2845 C  CA  . THR B 1 81  ? -22.83900 11.13000  -4.77500  1.000 33.22484  ? 81  THR B CA  1 
ATOM   2846 C  C   . THR B 1 81  ? -24.24100 10.88300  -4.23200  1.000 32.89566  ? 81  THR B C   1 
ATOM   2847 O  O   . THR B 1 81  ? -24.44500 11.00800  -3.01500  1.000 32.22629  ? 81  THR B O   1 
ATOM   2848 C  CB  . THR B 1 81  ? -22.51200 12.61800  -4.55600  1.000 33.15666  ? 81  THR B CB  1 
ATOM   2849 O  OG1 . THR B 1 81  ? -23.30300 13.41100  -5.44800  1.000 31.73725  ? 81  THR B OG1 1 
ATOM   2850 C  CG2 . THR B 1 81  ? -21.04400 12.88500  -4.81600  1.000 33.32268  ? 81  THR B CG2 1 
ATOM   2851 N  N   . CYS B 1 82  ? -25.21300 10.56000  -5.08000  1.000 31.21448  ? 82  CYS B N   1 
ATOM   2852 C  CA  . CYS B 1 82  ? -26.59500 10.35600  -4.64800  1.000 32.94893  ? 82  CYS B CA  1 
ATOM   2853 C  C   . CYS B 1 82  ? -27.04200 8.93800   -4.98100  1.000 32.38143  ? 82  CYS B C   1 
ATOM   2854 O  O   . CYS B 1 82  ? -27.59300 8.69200   -6.06700  1.000 32.52568  ? 82  CYS B O   1 
ATOM   2855 C  CB  . CYS B 1 82  ? -27.50000 11.40100  -5.29500  1.000 32.99662  ? 82  CYS B CB  1 
ATOM   2856 S  SG  . CYS B 1 82  ? -26.93800 13.09600  -4.91300  1.000 34.54073  ? 82  CYS B SG  1 
ATOM   2857 N  N   . PRO B 1 83  ? -26.83000 7.97400   -4.07400  1.000 30.51656  ? 83  PRO B N   1 
ATOM   2858 C  CA  . PRO B 1 83  ? -27.22200 6.58000   -4.36200  1.000 33.16920  ? 83  PRO B CA  1 
ATOM   2859 C  C   . PRO B 1 83  ? -28.65700 6.42000   -4.83300  1.000 33.53308  ? 83  PRO B C   1 
ATOM   2860 O  O   . PRO B 1 83  ? -28.95700 5.45800   -5.54700  1.000 32.76017  ? 83  PRO B O   1 
ATOM   2861 C  CB  . PRO B 1 83  ? -27.01600 5.85900   -3.02000  1.000 33.16252  ? 83  PRO B CB  1 
ATOM   2862 C  CG  . PRO B 1 83  ? -26.06100 6.67800   -2.27300  1.000 35.83286  ? 83  PRO B CG  1 
ATOM   2863 C  CD  . PRO B 1 83  ? -26.24400 8.12200   -2.73000  1.000 34.19581  ? 83  PRO B CD  1 
ATOM   2864 N  N   . THR B 1 84  ? -29.56400 7.30900   -4.42900  1.000 32.09799  ? 84  THR B N   1 
ATOM   2865 C  CA  . THR B 1 84  ? -30.95000 7.17100   -4.85900  1.000 34.74442  ? 84  THR B CA  1 
ATOM   2866 C  C   . THR B 1 84  ? -31.08200 7.41100   -6.35200  1.000 33.98327  ? 84  THR B C   1 
ATOM   2867 O  O   . THR B 1 84  ? -31.84100 6.71000   -7.03500  1.000 33.07643  ? 84  THR B O   1 
ATOM   2868 C  CB  . THR B 1 84  ? -31.85300 8.12900   -4.08100  1.000 37.35081  ? 84  THR B CB  1 
ATOM   2869 O  OG1 . THR B 1 84  ? -31.94400 7.69400   -2.71800  1.000 37.01891  ? 84  THR B OG1 1 
ATOM   2870 C  CG2 . THR B 1 84  ? -33.25500 8.16400   -4.70000  1.000 33.99200  ? 84  THR B CG2 1 
ATOM   2871 N  N   . PHE B 1 85  ? -30.34500 8.38800   -6.88500  1.000 32.75373  ? 85  PHE B N   1 
ATOM   2872 C  CA  . PHE B 1 85  ? -30.37200 8.59600   -8.32700  1.000 31.37717  ? 85  PHE B CA  1 
ATOM   2873 C  C   . PHE B 1 85  ? -29.71900 7.42800   -9.05500  1.000 32.26336  ? 85  PHE B C   1 
ATOM   2874 O  O   . PHE B 1 85  ? -30.30300 6.84900   -9.98300  1.000 31.08076  ? 85  PHE B O   1 
ATOM   2875 C  CB  . PHE B 1 85  ? -29.68000 9.90800   -8.69300  1.000 31.73178  ? 85  PHE B CB  1 
ATOM   2876 C  CG  . PHE B 1 85  ? -29.72100 10.20300  -10.16000 1.000 30.14463  ? 85  PHE B CG  1 
ATOM   2877 C  CD1 . PHE B 1 85  ? -30.81100 10.82800  -10.71700 1.000 31.64721  ? 85  PHE B CD1 1 
ATOM   2878 C  CD2 . PHE B 1 85  ? -28.67100 9.82800   -10.98700 1.000 29.44773  ? 85  PHE B CD2 1 
ATOM   2879 C  CE1 . PHE B 1 85  ? -30.84700 11.09700  -12.08800 1.000 29.55341  ? 85  PHE B CE1 1 
ATOM   2880 C  CE2 . PHE B 1 85  ? -28.70500 10.09800  -12.33000 1.000 31.90778  ? 85  PHE B CE2 1 
ATOM   2881 C  CZ  . PHE B 1 85  ? -29.80500 10.73200  -12.87900 1.000 29.63045  ? 85  PHE B CZ  1 
ATOM   2882 N  N   . ARG B 1 86  ? -28.51700 7.05000   -8.61500  1.000 30.98197  ? 86  ARG B N   1 
ATOM   2883 C  CA  . ARG B 1 86  ? -27.73800 6.03100   -9.30400  1.000 33.51965  ? 86  ARG B CA  1 
ATOM   2884 C  C   . ARG B 1 86  ? -28.46600 4.69000   -9.34100  1.000 33.91662  ? 86  ARG B C   1 
ATOM   2885 O  O   . ARG B 1 86  ? -28.45200 4.00300   -10.36600 1.000 35.66574  ? 86  ARG B O   1 
ATOM   2886 C  CB  . ARG B 1 86  ? -26.37300 5.90200   -8.62400  1.000 33.08327  ? 86  ARG B CB  1 
ATOM   2887 C  CG  . ARG B 1 86  ? -25.48500 4.81700   -9.18800  1.000 34.32096  ? 86  ARG B CG  1 
ATOM   2888 C  CD  . ARG B 1 86  ? -24.07400 4.88800   -8.58400  1.000 34.95245  ? 86  ARG B CD  1 
ATOM   2889 N  NE  . ARG B 1 86  ? -24.01800 4.35400   -7.22500  1.000 31.71407  ? 86  ARG B NE  1 
ATOM   2890 C  CZ  . ARG B 1 86  ? -23.88800 5.07500   -6.11500  1.000 34.63996  ? 86  ARG B CZ  1 
ATOM   2891 N  NH1 . ARG B 1 86  ? -23.82100 6.40400   -6.14600  1.000 29.99707  ? 86  ARG B NH1 1 
ATOM   2892 N  NH2 . ARG B 1 86  ? -23.83000 4.44700   -4.94200  1.000 35.31460  ? 86  ARG B NH2 1 
ATOM   2893 N  N   . ASN B 1 87  ? -29.12600 4.30800   -8.24300  1.000 33.15820  ? 87  ASN B N   1 
ATOM   2894 C  CA  . ASN B 1 87  ? -29.71500 2.97400   -8.12100  1.000 33.55049  ? 87  ASN B CA  1 
ATOM   2895 C  C   . ASN B 1 87  ? -31.20200 2.91100   -8.43500  1.000 34.21741  ? 87  ASN B C   1 
ATOM   2896 O  O   . ASN B 1 87  ? -31.71700 1.80700   -8.62100  1.000 38.65567  ? 87  ASN B O   1 
ATOM   2897 C  CB  . ASN B 1 87  ? -29.51900 2.41400   -6.71100  1.000 32.69884  ? 87  ASN B CB  1 
ATOM   2898 C  CG  . ASN B 1 87  ? -28.07100 2.14600   -6.38400  1.000 35.09279  ? 87  ASN B CG  1 
ATOM   2899 O  OD1 . ASN B 1 87  ? -27.29300 1.69800   -7.23600  1.000 36.16238  ? 87  ASN B OD1 1 
ATOM   2900 N  ND2 . ASN B 1 87  ? -27.69300 2.42000   -5.13700  1.000 35.89479  ? 87  ASN B ND2 1 
ATOM   2901 N  N   . THR B 1 88  ? -31.90800 4.04300   -8.46700  1.000 32.63032  ? 88  THR B N   1 
ATOM   2902 C  CA  . THR B 1 88  ? -33.36100 4.02600   -8.61800  1.000 35.76166  ? 88  THR B CA  1 
ATOM   2903 C  C   . THR B 1 88  ? -33.83400 4.95400   -9.73600  1.000 35.53452  ? 88  THR B C   1 
ATOM   2904 O  O   . THR B 1 88  ? -34.46200 4.49500   -10.69800 1.000 36.74116  ? 88  THR B O   1 
ATOM   2905 C  CB  . THR B 1 88  ? -34.02400 4.38800   -7.28200  1.000 34.74898  ? 88  THR B CB  1 
ATOM   2906 O  OG1 . THR B 1 88  ? -33.58600 3.46200   -6.28500  1.000 36.40343  ? 88  THR B OG1 1 
ATOM   2907 C  CG2 . THR B 1 88  ? -35.52700 4.35000   -7.38300  1.000 32.95472  ? 88  THR B CG2 1 
ATOM   2908 N  N   . VAL B 1 89  ? -33.52300 6.25000   -9.64900  1.000 33.98493  ? 89  VAL B N   1 
ATOM   2909 C  CA  . VAL B 1 89  ? -33.98900 7.18900   -10.67400 1.000 31.53909  ? 89  VAL B CA  1 
ATOM   2910 C  C   . VAL B 1 89  ? -33.35600 6.88400   -12.03300 1.000 33.33719  ? 89  VAL B C   1 
ATOM   2911 O  O   . VAL B 1 89  ? -34.05000 6.81800   -13.05500 1.000 31.42949  ? 89  VAL B O   1 
ATOM   2912 C  CB  . VAL B 1 89  ? -33.71500 8.64300   -10.24400 1.000 35.55619  ? 89  VAL B CB  1 
ATOM   2913 C  CG1 . VAL B 1 89  ? -34.33000 9.61400   -11.23800 1.000 31.47580  ? 89  VAL B CG1 1 
ATOM   2914 C  CG2 . VAL B 1 89  ? -34.27400 8.90500   -8.85400  1.000 32.42484  ? 89  VAL B CG2 1 
ATOM   2915 N  N   . LEU B 1 90  ? -32.03000 6.71300   -12.06800 1.000 33.89194  ? 90  LEU B N   1 
ATOM   2916 C  CA  . LEU B 1 90  ? -31.30900 6.55200   -13.34100 1.000 28.09027  ? 90  LEU B CA  1 
ATOM   2917 C  C   . LEU B 1 90  ? -31.79300 5.35500   -14.14800 1.000 33.97295  ? 90  LEU B C   1 
ATOM   2918 O  O   . LEU B 1 90  ? -31.68500 5.35800   -15.38400 1.000 35.12658  ? 90  LEU B O   1 
ATOM   2919 C  CB  . LEU B 1 90  ? -29.79700 6.40200   -13.08900 1.000 30.46559  ? 90  LEU B CB  1 
ATOM   2920 C  CG  . LEU B 1 90  ? -28.84100 6.13000   -14.26900 1.000 33.56149  ? 90  LEU B CG  1 
ATOM   2921 C  CD1 . LEU B 1 90  ? -28.80500 7.31600   -15.24300 1.000 28.85058  ? 90  LEU B CD1 1 
ATOM   2922 C  CD2 . LEU B 1 90  ? -27.42700 5.80600   -13.79800 1.000 29.12160  ? 90  LEU B CD2 1 
ATOM   2923 N  N   . ILE B 1 91  ? -32.28800 4.31000   -13.49200 1.000 31.15418  ? 91  ILE B N   1 
ATOM   2924 C  CA  . ILE B 1 91  ? -32.62900 3.09100   -14.21500 1.000 34.61960  ? 91  ILE B CA  1 
ATOM   2925 C  C   . ILE B 1 91  ? -34.13600 2.86900   -14.25400 1.000 33.19190  ? 91  ILE B C   1 
ATOM   2926 O  O   . ILE B 1 91  ? -34.58500 1.76900   -14.53600 1.000 34.62185  ? 91  ILE B O   1 
ATOM   2927 C  CB  . ILE B 1 91  ? -31.89400 1.86900   -13.64600 1.000 35.04173  ? 91  ILE B CB  1 
ATOM   2928 C  CG1 . ILE B 1 91  ? -32.27100 1.64800   -12.17800 1.000 34.26435  ? 91  ILE B CG1 1 
ATOM   2929 C  CG2 . ILE B 1 91  ? -30.38400 2.07200   -13.81900 1.000 34.57247  ? 91  ILE B CG2 1 
ATOM   2930 C  CD1 . ILE B 1 91  ? -31.82800 0.28700   -11.61400 1.000 38.33867  ? 91  ILE B CD1 1 
ATOM   2931 N  N   . ASN B 1 92  ? -34.91700 3.90700   -13.98300 1.000 32.37056  ? 92  ASN B N   1 
ATOM   2932 C  CA  . ASN B 1 92  ? -36.36200 3.80900   -14.08100 1.000 34.64858  ? 92  ASN B CA  1 
ATOM   2933 C  C   . ASN B 1 92  ? -36.78900 3.21600   -15.42600 1.000 32.57473  ? 92  ASN B C   1 
ATOM   2934 O  O   . ASN B 1 92  ? -36.44100 3.77100   -16.47800 1.000 32.65852  ? 92  ASN B O   1 
ATOM   2935 C  CB  . ASN B 1 92  ? -36.99900 5.17800   -13.92000 1.000 32.31496  ? 92  ASN B CB  1 
ATOM   2936 C  CG  . ASN B 1 92  ? -38.49300 5.08800   -13.90300 1.000 38.38409  ? 92  ASN B CG  1 
ATOM   2937 O  OD1 . ASN B 1 92  ? -39.14300 5.13500   -14.94800 1.000 39.29948  ? 92  ASN B OD1 1 
ATOM   2938 N  ND2 . ASN B 1 92  ? -39.05200 4.90700   -12.71500 1.000 34.97928  ? 92  ASN B ND2 1 
ATOM   2939 N  N   . PRO B 1 93  ? -37.58000 2.13900   -15.43800 1.000 33.60672  ? 93  PRO B N   1 
ATOM   2940 C  CA  . PRO B 1 93  ? -37.86600 1.45600   -16.70700 1.000 33.66865  ? 93  PRO B CA  1 
ATOM   2941 C  C   . PRO B 1 93  ? -38.84200 2.21100   -17.59600 1.000 36.69862  ? 93  PRO B C   1 
ATOM   2942 O  O   . PRO B 1 93  ? -38.85300 1.97500   -18.81400 1.000 35.03080  ? 93  PRO B O   1 
ATOM   2943 C  CB  . PRO B 1 93  ? -38.42900 0.09800   -16.26600 1.000 33.84369  ? 93  PRO B CB  1 
ATOM   2944 C  CG  . PRO B 1 93  ? -38.96900 0.32600   -14.91100 1.000 40.17946  ? 93  PRO B CG  1 
ATOM   2945 C  CD  . PRO B 1 93  ? -38.23000 1.49300   -14.28600 1.000 32.64484  ? 93  PRO B CD  1 
ATOM   2946 N  N   . VAL B 1 94  ? -39.65600 3.10700   -17.03400 1.000 34.05610  ? 94  VAL B N   1 
ATOM   2947 C  CA  . VAL B 1 94  ? -40.50500 3.95200   -17.86600 1.000 31.93821  ? 94  VAL B CA  1 
ATOM   2948 C  C   . VAL B 1 94  ? -39.66400 4.95300   -18.64500 1.000 33.74848  ? 94  VAL B C   1 
ATOM   2949 O  O   . VAL B 1 94  ? -39.89600 5.17600   -19.83900 1.000 32.86784  ? 94  VAL B O   1 
ATOM   2950 C  CB  . VAL B 1 94  ? -41.57100 4.65100   -17.00700 1.000 35.48539  ? 94  VAL B CB  1 
ATOM   2951 C  CG1 . VAL B 1 94  ? -42.43100 5.58300   -17.87700 1.000 36.97697  ? 94  VAL B CG1 1 
ATOM   2952 C  CG2 . VAL B 1 94  ? -42.41700 3.60100   -16.26700 1.000 36.60445  ? 94  VAL B CG2 1 
ATOM   2953 N  N   . ILE B 1 95  ? -38.68400 5.58100   -17.98800 1.000 32.46544  ? 95  ILE B N   1 
ATOM   2954 C  CA  . ILE B 1 95  ? -37.78900 6.50100   -18.68700 1.000 33.27334  ? 95  ILE B CA  1 
ATOM   2955 C  C   . ILE B 1 95  ? -37.07400 5.78700   -19.84000 1.000 33.80153  ? 95  ILE B C   1 
ATOM   2956 O  O   . ILE B 1 95  ? -36.94900 6.32100   -20.95100 1.000 32.32320  ? 95  ILE B O   1 
ATOM   2957 C  CB  . ILE B 1 95  ? -36.78200 7.12500   -17.69600 1.000 32.51117  ? 95  ILE B CB  1 
ATOM   2958 C  CG1 . ILE B 1 95  ? -37.49100 7.93900   -16.60200 1.000 34.34450  ? 95  ILE B CG1 1 
ATOM   2959 C  CG2 . ILE B 1 95  ? -35.73200 7.98400   -18.44600 1.000 30.10946  ? 95  ILE B CG2 1 
ATOM   2960 C  CD1 . ILE B 1 95  ? -38.50600 8.94100   -17.12300 1.000 39.69027  ? 95  ILE B CD1 1 
ATOM   2961 N  N   . HIS B 1 96  ? -36.60600 4.56900   -19.59900 1.000 32.01662  ? 96  HIS B N   1 
ATOM   2962 C  CA  . HIS B 1 96  ? -35.82400 3.86900   -20.60400 1.000 33.06782  ? 96  HIS B CA  1 
ATOM   2963 C  C   . HIS B 1 96  ? -36.68300 3.29400   -21.71300 1.000 32.84743  ? 96  HIS B C   1 
ATOM   2964 O  O   . HIS B 1 96  ? -36.22200 3.21500   -22.85300 1.000 34.18642  ? 96  HIS B O   1 
ATOM   2965 C  CB  . HIS B 1 96  ? -34.98800 2.79900   -19.92900 1.000 31.42438  ? 96  HIS B CB  1 
ATOM   2966 C  CG  . HIS B 1 96  ? -33.84000 3.38600   -19.18800 1.000 33.56742  ? 96  HIS B CG  1 
ATOM   2967 N  ND1 . HIS B 1 96  ? -32.67300 3.76100   -19.81800 1.000 31.57073  ? 96  HIS B ND1 1 
ATOM   2968 C  CD2 . HIS B 1 96  ? -33.71300 3.76000   -17.89500 1.000 30.90351  ? 96  HIS B CD2 1 
ATOM   2969 C  CE1 . HIS B 1 96  ? -31.85700 4.30700   -18.93200 1.000 34.59802  ? 96  HIS B CE1 1 
ATOM   2970 N  NE2 . HIS B 1 96  ? -32.46500 4.31800   -17.75800 1.000 34.49226  ? 96  HIS B NE2 1 
ATOM   2971 N  N   . ALA B 1 97  ? -37.92900 2.92800   -21.41900 1.000 32.88437  ? 97  ALA B N   1 
ATOM   2972 C  CA  . ALA B 1 97  ? -38.86000 2.60600   -22.49600 1.000 35.15506  ? 97  ALA B CA  1 
ATOM   2973 C  C   . ALA B 1 97  ? -39.03400 3.79300   -23.43100 1.000 34.05976  ? 97  ALA B C   1 
ATOM   2974 O  O   . ALA B 1 97  ? -39.02000 3.64000   -24.65800 1.000 35.50021  ? 97  ALA B O   1 
ATOM   2975 C  CB  . ALA B 1 97  ? -40.20500 2.17500   -21.92300 1.000 33.69893  ? 97  ALA B CB  1 
ATOM   2976 N  N   . ILE B 1 98  ? -39.17500 4.99200   -22.87200 1.000 33.97893  ? 98  ILE B N   1 
ATOM   2977 C  CA  . ILE B 1 98  ? -39.29100 6.17900   -23.71100 1.000 31.65988  ? 98  ILE B CA  1 
ATOM   2978 C  C   . ILE B 1 98  ? -38.00900 6.38200   -24.50900 1.000 32.54718  ? 98  ILE B C   1 
ATOM   2979 O  O   . ILE B 1 98  ? -38.04200 6.58400   -25.72900 1.000 31.79317  ? 98  ILE B O   1 
ATOM   2980 C  CB  . ILE B 1 98  ? -39.60600 7.41100   -22.85000 1.000 31.31219  ? 98  ILE B CB  1 
ATOM   2981 C  CG1 . ILE B 1 98  ? -40.93600 7.23100   -22.13000 1.000 35.27500  ? 98  ILE B CG1 1 
ATOM   2982 C  CG2 . ILE B 1 98  ? -39.56300 8.69200   -23.70000 1.000 32.27013  ? 98  ILE B CG2 1 
ATOM   2983 C  CD1 . ILE B 1 98  ? -41.04000 8.09900   -20.91400 1.000 35.54567  ? 98  ILE B CD1 1 
ATOM   2984 N  N   . CYS B 1 99  ? -36.86300 6.35600   -23.81900 1.000 28.28475  ? 99  CYS B N   1 
ATOM   2985 C  CA  . CYS B 1 99  ? -35.58900 6.56200   -24.49800 1.000 33.88951  ? 99  CYS B CA  1 
ATOM   2986 C  C   . CYS B 1 99  ? -35.41700 5.57200   -25.64000 1.000 31.25877  ? 99  CYS B C   1 
ATOM   2987 O  O   . CYS B 1 99  ? -35.01900 5.95700   -26.74300 1.000 30.95428  ? 99  CYS B O   1 
ATOM   2988 C  CB  . CYS B 1 99  ? -34.42200 6.45100   -23.51600 1.000 30.16627  ? 99  CYS B CB  1 
ATOM   2989 S  SG  . CYS B 1 99  ? -34.29200 7.83400   -22.39700 1.000 34.38035  ? 99  CYS B SG  1 
ATOM   2990 N  N   . GLU B 1 100 ? -35.72000 4.29200   -25.40200 1.000 31.98680  ? 100 GLU B N   1 
ATOM   2991 C  CA  . GLU B 1 100 ? -35.47000 3.29800   -26.43800 1.000 35.04501  ? 100 GLU B CA  1 
ATOM   2992 C  C   . GLU B 1 100 ? -36.34500 3.54200   -27.65700 1.000 36.12561  ? 100 GLU B C   1 
ATOM   2993 O  O   . GLU B 1 100 ? -35.89300 3.36500   -28.79500 1.000 36.94803  ? 100 GLU B O   1 
ATOM   2994 C  CB  . GLU B 1 100 ? -35.67700 1.88400   -25.90200 1.000 36.53719  ? 100 GLU B CB  1 
ATOM   2995 C  CG  . GLU B 1 100 ? -34.43200 1.31200   -25.24700 1.000 40.74042  ? 100 GLU B CG  1 
ATOM   2996 C  CD  . GLU B 1 100 ? -34.69900 0.03900   -24.46400 1.000 49.71814  ? 100 GLU B CD  1 
ATOM   2997 O  OE1 . GLU B 1 100 ? -35.77500 -0.56400  -24.64100 1.000 51.31316  ? 100 GLU B OE1 1 
ATOM   2998 O  OE2 . GLU B 1 100 ? -33.82800 -0.35400  -23.65900 1.000 55.45854  ? 100 GLU B OE2 1 
ATOM   2999 N  N   . ALA B 1 101 ? -37.58900 3.97800   -27.44000 1.000 34.19590  ? 101 ALA B N   1 
ATOM   3000 C  CA  . ALA B 1 101 ? -38.46200 4.29800   -28.56200 1.000 35.17058  ? 101 ALA B CA  1 
ATOM   3001 C  C   . ALA B 1 101 ? -38.01500 5.57700   -29.24100 1.000 35.20255  ? 101 ALA B C   1 
ATOM   3002 O  O   . ALA B 1 101 ? -38.02700 5.66800   -30.47000 1.000 36.11549  ? 101 ALA B O   1 
ATOM   3003 C  CB  . ALA B 1 101 ? -39.90500 4.42800   -28.08100 1.000 37.45518  ? 101 ALA B CB  1 
ATOM   3004 N  N   . TYR B 1 102 ? -37.61300 6.57400   -28.45000 1.000 34.88897  ? 102 TYR B N   1 
ATOM   3005 C  CA  . TYR B 1 102 ? -37.19900 7.86100   -29.00100 1.000 33.08586  ? 102 TYR B CA  1 
ATOM   3006 C  C   . TYR B 1 102 ? -35.92400 7.73500   -29.82100 1.000 32.83413  ? 102 TYR B C   1 
ATOM   3007 O  O   . TYR B 1 102 ? -35.78000 8.39100   -30.86200 1.000 32.03624  ? 102 TYR B O   1 
ATOM   3008 C  CB  . TYR B 1 102 ? -36.99100 8.84300   -27.85300 1.000 30.45929  ? 102 TYR B CB  1 
ATOM   3009 C  CG  . TYR B 1 102 ? -36.46200 10.22600  -28.21200 1.000 31.78320  ? 102 TYR B CG  1 
ATOM   3010 C  CD1 . TYR B 1 102 ? -37.31700 11.17600  -28.77100 1.000 31.37981  ? 102 TYR B CD1 1 
ATOM   3011 C  CD2 . TYR B 1 102 ? -35.13600 10.56100  -27.95000 1.000 30.02005  ? 102 TYR B CD2 1 
ATOM   3012 C  CE1 . TYR B 1 102 ? -36.83500 12.42400  -29.07000 1.000 33.02523  ? 102 TYR B CE1 1 
ATOM   3013 C  CE2 . TYR B 1 102 ? -34.69300 11.82800  -28.24500 1.000 27.12365  ? 102 TYR B CE2 1 
ATOM   3014 C  CZ  . TYR B 1 102 ? -35.52400 12.78500  -28.80700 1.000 28.49864  ? 102 TYR B CZ  1 
ATOM   3015 O  OH  . TYR B 1 102 ? -35.08000 14.02200  -29.09300 1.000 29.01432  ? 102 TYR B OH  1 
ATOM   3016 N  N   . PHE B 1 103 ? -34.97400 6.92700   -29.34800 1.000 30.96911  ? 103 PHE B N   1 
ATOM   3017 C  CA  . PHE B 1 103 ? -33.65500 6.80800   -29.95300 1.000 30.78260  ? 103 PHE B CA  1 
ATOM   3018 C  C   . PHE B 1 103 ? -33.57900 5.66500   -30.97800 1.000 33.42156  ? 103 PHE B C   1 
ATOM   3019 O  O   . PHE B 1 103 ? -32.47600 5.25700   -31.36600 1.000 31.66440  ? 103 PHE B O   1 
ATOM   3020 C  CB  . PHE B 1 103 ? -32.59600 6.63200   -28.85500 1.000 26.18750  ? 103 PHE B CB  1 
ATOM   3021 C  CG  . PHE B 1 103 ? -32.26400 7.91400   -28.08500 1.000 29.71423  ? 103 PHE B CG  1 
ATOM   3022 C  CD1 . PHE B 1 103 ? -31.71900 9.02300   -28.73500 1.000 29.95856  ? 103 PHE B CD1 1 
ATOM   3023 C  CD2 . PHE B 1 103 ? -32.45900 7.99000   -26.71200 1.000 29.40188  ? 103 PHE B CD2 1 
ATOM   3024 C  CE1 . PHE B 1 103 ? -31.38900 10.18500  -28.03500 1.000 27.22371  ? 103 PHE B CE1 1 
ATOM   3025 C  CE2 . PHE B 1 103 ? -32.13100 9.15000   -25.99800 1.000 26.01149  ? 103 PHE B CE2 1 
ATOM   3026 C  CZ  . PHE B 1 103 ? -31.59100 10.24800  -26.66900 1.000 27.18664  ? 103 PHE B CZ  1 
ATOM   3027 N  N   . GLN B 1 104 ? -34.73100 5.16900   -31.43800 1.000 33.15382  ? 104 GLN B N   1 
ATOM   3028 C  CA  . GLN B 1 104 ? -34.78200 3.98500   -32.29500 1.000 34.73678  ? 104 GLN B CA  1 
ATOM   3029 C  C   . GLN B 1 104 ? -33.93600 4.14500   -33.55900 1.000 36.67935  ? 104 GLN B C   1 
ATOM   3030 O  O   . GLN B 1 104 ? -33.26500 3.20100   -33.99000 1.000 38.41241  ? 104 GLN B O   1 
ATOM   3031 C  CB  . GLN B 1 104 ? -36.23700 3.69800   -32.66200 1.000 37.92794  ? 104 GLN B CB  1 
ATOM   3032 C  CG  . GLN B 1 104 ? -36.47600 2.36400   -33.29700 1.000 45.52757  ? 104 GLN B CG  1 
ATOM   3033 C  CD  . GLN B 1 104 ? -37.93900 2.18300   -33.64000 1.000 58.60887  ? 104 GLN B CD  1 
ATOM   3034 O  OE1 . GLN B 1 104 ? -38.80200 2.88500   -33.09600 1.000 57.53721  ? 104 GLN B OE1 1 
ATOM   3035 N  NE2 . GLN B 1 104 ? -38.23100 1.25900   -34.55900 1.000 61.20906  ? 104 GLN B NE2 1 
ATOM   3036 N  N   . ARG B 1 105 ? -33.95800 5.32700   -34.17200 1.000 32.20289  ? 105 ARG B N   1 
ATOM   3037 C  CA  . ARG B 1 105 ? -33.21100 5.55500   -35.40600 1.000 37.28444  ? 105 ARG B CA  1 
ATOM   3038 C  C   . ARG B 1 105 ? -31.72900 5.84000   -35.17200 1.000 35.85357  ? 105 ARG B C   1 
ATOM   3039 O  O   . ARG B 1 105 ? -30.92500 5.62200   -36.08700 1.000 38.56135  ? 105 ARG B O   1 
ATOM   3040 C  CB  . ARG B 1 105 ? -33.82000 6.72000   -36.19800 1.000 35.27168  ? 105 ARG B CB  1 
ATOM   3041 C  CG  . ARG B 1 105 ? -35.22800 6.49000   -36.75400 1.000 41.10371  ? 105 ARG B CG  1 
ATOM   3042 C  CD  . ARG B 1 105 ? -35.86500 7.83900   -37.14100 1.000 41.61169  ? 105 ARG B CD  1 
ATOM   3043 N  NE  . ARG B 1 105 ? -35.12100 8.49000   -38.21400 1.000 40.21433  ? 105 ARG B NE  1 
ATOM   3044 C  CZ  . ARG B 1 105 ? -35.07400 9.80200   -38.42200 1.000 40.14251  ? 105 ARG B CZ  1 
ATOM   3045 N  NH1 . ARG B 1 105 ? -35.72200 10.65300  -37.64000 1.000 40.18811  ? 105 ARG B NH1 1 
ATOM   3046 N  NH2 . ARG B 1 105 ? -34.34300 10.27500  -39.43200 1.000 41.38887  ? 105 ARG B NH2 1 
ATOM   3047 N  N   . THR B 1 106 ? -31.33900 6.33500   -33.99400 1.000 33.30395  ? 106 THR B N   1 
ATOM   3048 C  CA  . THR B 1 106 ? -29.92200 6.60200   -33.75200 1.000 32.69330  ? 106 THR B CA  1 
ATOM   3049 C  C   . THR B 1 106 ? -29.21000 5.44500   -33.05600 1.000 31.31158  ? 106 THR B C   1 
ATOM   3050 O  O   . THR B 1 106 ? -27.97900 5.34700   -33.15100 1.000 28.19701  ? 106 THR B O   1 
ATOM   3051 C  CB  . THR B 1 106 ? -29.74400 7.89400   -32.92900 1.000 34.49231  ? 106 THR B CB  1 
ATOM   3052 O  OG1 . THR B 1 106 ? -28.41500 8.41000   -33.11600 1.000 32.28863  ? 106 THR B OG1 1 
ATOM   3053 C  CG2 . THR B 1 106 ? -29.95300 7.62500   -31.45700 1.000 31.93346  ? 106 THR B CG2 1 
ATOM   3054 N  N   . GLY B 1 107 ? -29.94500 4.55900   -32.38000 1.000 31.03561  ? 107 GLY B N   1 
ATOM   3055 C  CA  . GLY B 1 107 ? -29.33400 3.44100   -31.68500 1.000 30.32958  ? 107 GLY B CA  1 
ATOM   3056 C  C   . GLY B 1 107 ? -29.16900 3.72400   -30.20800 1.000 31.74334  ? 107 GLY B C   1 
ATOM   3057 O  O   . GLY B 1 107 ? -30.01700 4.40300   -29.60700 1.000 30.36396  ? 107 GLY B O   1 
ATOM   3058 N  N   . ASP B 1 108 ? -28.07900 3.23700   -29.61100 1.000 30.45958  ? 108 ASP B N   1 
ATOM   3059 C  CA  . ASP B 1 108 ? -27.92800 3.35400   -28.16700 1.000 27.16000  ? 108 ASP B CA  1 
ATOM   3060 C  C   . ASP B 1 108 ? -27.76800 4.80300   -27.72700 1.000 28.98175  ? 108 ASP B C   1 
ATOM   3061 O  O   . ASP B 1 108 ? -27.26200 5.65800   -28.46300 1.000 28.19768  ? 108 ASP B O   1 
ATOM   3062 C  CB  . ASP B 1 108 ? -26.73400 2.54600   -27.66400 1.000 29.63278  ? 108 ASP B CB  1 
ATOM   3063 C  CG  . ASP B 1 108 ? -27.00500 1.03800   -27.64000 1.000 33.21866  ? 108 ASP B CG  1 
ATOM   3064 O  OD1 . ASP B 1 108 ? -28.17200 0.61700   -27.83800 1.000 35.41413  ? 108 ASP B OD1 1 
ATOM   3065 O  OD2 . ASP B 1 108 ? -26.03600 0.27100   -27.44800 1.000 31.56567  ? 108 ASP B OD2 1 
ATOM   3066 N  N   . TYR B 1 109 ? -28.17200 5.05100   -26.48200 1.000 26.91812  ? 109 TYR B N   1 
ATOM   3067 C  CA  . TYR B 1 109 ? -28.03600 6.33400   -25.81200 1.000 26.93351  ? 109 TYR B CA  1 
ATOM   3068 C  C   . TYR B 1 109 ? -27.32400 6.09700   -24.48000 1.000 27.03640  ? 109 TYR B C   1 
ATOM   3069 O  O   . TYR B 1 109 ? -27.21900 4.96200   -24.01200 1.000 26.51321  ? 109 TYR B O   1 
ATOM   3070 C  CB  . TYR B 1 109 ? -29.43100 6.96300   -25.58700 1.000 26.71464  ? 109 TYR B CB  1 
ATOM   3071 C  CG  . TYR B 1 109 ? -30.29900 6.05300   -24.72900 1.000 28.37837  ? 109 TYR B CG  1 
ATOM   3072 C  CD1 . TYR B 1 109 ? -31.02100 5.01200   -25.31200 1.000 27.76414  ? 109 TYR B CD1 1 
ATOM   3073 C  CD2 . TYR B 1 109 ? -30.34600 6.23600   -23.35000 1.000 27.17004  ? 109 TYR B CD2 1 
ATOM   3074 C  CE1 . TYR B 1 109 ? -31.77000 4.18300   -24.51200 1.000 30.01552  ? 109 TYR B CE1 1 
ATOM   3075 C  CE2 . TYR B 1 109 ? -31.11000 5.39000   -22.58400 1.000 31.74395  ? 109 TYR B CE2 1 
ATOM   3076 C  CZ  . TYR B 1 109 ? -31.82900 4.34000   -23.13400 1.000 31.36558  ? 109 TYR B CZ  1 
ATOM   3077 O  OH  . TYR B 1 109 ? -32.56800 3.52500   -22.35000 1.000 30.68251  ? 109 TYR B OH  1 
ATOM   3078 N  N   . TRP B 1 110 ? -26.80600 7.15700   -23.87000 1.000 23.13840  ? 110 TRP B N   1 
ATOM   3079 C  CA  . TRP B 1 110 ? -26.31400 7.05200   -22.49700 1.000 25.15078  ? 110 TRP B CA  1 
ATOM   3080 C  C   . TRP B 1 110 ? -26.44800 8.41200   -21.83500 1.000 23.87720  ? 110 TRP B C   1 
ATOM   3081 O  O   . TRP B 1 110 ? -26.90700 9.38300   -22.44900 1.000 22.41568  ? 110 TRP B O   1 
ATOM   3082 C  CB  . TRP B 1 110 ? -24.86700 6.51900   -22.41600 1.000 23.94711  ? 110 TRP B CB  1 
ATOM   3083 C  CG  . TRP B 1 110 ? -23.83000 7.22200   -23.27000 1.000 26.07203  ? 110 TRP B CG  1 
ATOM   3084 C  CD1 . TRP B 1 110 ? -23.95100 8.42900   -23.89300 1.000 23.06677  ? 110 TRP B CD1 1 
ATOM   3085 C  CD2 . TRP B 1 110 ? -22.51600 6.72600   -23.60400 1.000 26.83544  ? 110 TRP B CD2 1 
ATOM   3086 N  NE1 . TRP B 1 110 ? -22.79400 8.71600   -24.58900 1.000 25.08470  ? 110 TRP B NE1 1 
ATOM   3087 C  CE2 . TRP B 1 110 ? -21.90200 7.69200   -24.42400 1.000 22.88674  ? 110 TRP B CE2 1 
ATOM   3088 C  CE3 . TRP B 1 110 ? -21.80700 5.56200   -23.27900 1.000 23.40665  ? 110 TRP B CE3 1 
ATOM   3089 C  CZ2 . TRP B 1 110 ? -20.60700 7.54000   -24.91600 1.000 26.21172  ? 110 TRP B CZ2 1 
ATOM   3090 C  CZ3 . TRP B 1 110 ? -20.52100 5.40200   -23.78200 1.000 25.59360  ? 110 TRP B CZ3 1 
ATOM   3091 C  CH2 . TRP B 1 110 ? -19.93800 6.38300   -24.59200 1.000 27.74165  ? 110 TRP B CH2 1 
ATOM   3092 N  N   . LEU B 1 111 ? -26.02100 8.48200   -20.57500 1.000 24.59532  ? 111 LEU B N   1 
ATOM   3093 C  CA  . LEU B 1 111 ? -26.20500 9.69400   -19.78700 1.000 26.86606  ? 111 LEU B CA  1 
ATOM   3094 C  C   . LEU B 1 111 ? -25.06800 10.66900  -20.07700 1.000 24.73888  ? 111 LEU B C   1 
ATOM   3095 O  O   . LEU B 1 111 ? -23.90200 10.35700  -19.82000 1.000 27.82247  ? 111 LEU B O   1 
ATOM   3096 C  CB  . LEU B 1 111 ? -26.27300 9.35700   -18.29700 1.000 28.94197  ? 111 LEU B CB  1 
ATOM   3097 C  CG  . LEU B 1 111 ? -26.52500 10.57000  -17.40000 1.000 24.66853  ? 111 LEU B CG  1 
ATOM   3098 C  CD1 . LEU B 1 111 ? -27.96500 11.07000  -17.62400 1.000 25.72788  ? 111 LEU B CD1 1 
ATOM   3099 C  CD2 . LEU B 1 111 ? -26.24600 10.27300  -15.90000 1.000 25.26523  ? 111 LEU B CD2 1 
ATOM   3100 N  N   . SER B 1 112 ? -25.39800 11.85800  -20.59600 1.000 25.36258  ? 112 SER B N   1 
ATOM   3101 C  CA  . SER B 1 112 ? -24.34700 12.86000  -20.81300 1.000 25.02969  ? 112 SER B CA  1 
ATOM   3102 C  C   . SER B 1 112 ? -24.06700 13.66600  -19.55700 1.000 23.98434  ? 112 SER B C   1 
ATOM   3103 O  O   . SER B 1 112 ? -22.90800 13.98900  -19.26700 1.000 24.68789  ? 112 SER B O   1 
ATOM   3104 C  CB  . SER B 1 112 ? -24.71100 13.81900  -21.94900 1.000 24.91432  ? 112 SER B CB  1 
ATOM   3105 O  OG  . SER B 1 112 ? -23.63100 14.73100  -22.17800 1.000 24.65857  ? 112 SER B OG  1 
ATOM   3106 N  N   . ALA B 1 113 ? -25.11600 14.00400  -18.80900 1.000 26.84147  ? 113 ALA B N   1 
ATOM   3107 C  CA  . ALA B 1 113 ? -24.99000 14.80000  -17.60200 1.000 24.84088  ? 113 ALA B CA  1 
ATOM   3108 C  C   . ALA B 1 113 ? -26.25700 14.62300  -16.77300 1.000 27.94900  ? 113 ALA B C   1 
ATOM   3109 O  O   . ALA B 1 113 ? -27.35400 14.44900  -17.32300 1.000 22.85366  ? 113 ALA B O   1 
ATOM   3110 C  CB  . ALA B 1 113 ? -24.78600 16.28500  -17.92100 1.000 26.50538  ? 113 ALA B CB  1 
ATOM   3111 N  N   . ALA B 1 114 ? -26.09300 14.68900  -15.45100 1.000 23.35907  ? 114 ALA B N   1 
ATOM   3112 C  CA  . ALA B 1 114 ? -27.23000 14.81600  -14.53700 1.000 26.61678  ? 114 ALA B CA  1 
ATOM   3113 C  C   . ALA B 1 114 ? -26.78500 15.63400  -13.33300 1.000 25.78679  ? 114 ALA B C   1 
ATOM   3114 O  O   . ALA B 1 114 ? -25.82600 15.26800  -12.64900 1.000 26.69110  ? 114 ALA B O   1 
ATOM   3115 C  CB  . ALA B 1 114 ? -27.76900 13.45100  -14.11400 1.000 27.16810  ? 114 ALA B CB  1 
ATOM   3116 N  N   . PHE B 1 115 ? -27.47800 16.73800  -13.07800 1.000 26.15887  ? 115 PHE B N   1 
ATOM   3117 C  CA  . PHE B 1 115 ? -26.99600 17.73300  -12.13500 1.000 27.87627  ? 115 PHE B CA  1 
ATOM   3118 C  C   . PHE B 1 115 ? -28.16700 18.47800  -11.50700 1.000 28.77751  ? 115 PHE B C   1 
ATOM   3119 O  O   . PHE B 1 115 ? -29.25200 18.58300  -12.08600 1.000 26.69539  ? 115 PHE B O   1 
ATOM   3120 C  CB  . PHE B 1 115 ? -26.03600 18.73300  -12.81000 1.000 27.85141  ? 115 PHE B CB  1 
ATOM   3121 C  CG  . PHE B 1 115 ? -26.64400 19.48700  -13.98200 1.000 29.30329  ? 115 PHE B CG  1 
ATOM   3122 C  CD1 . PHE B 1 115 ? -26.67900 18.91800  -15.25200 1.000 29.27576  ? 115 PHE B CD1 1 
ATOM   3123 C  CD2 . PHE B 1 115 ? -27.13600 20.77700  -13.82300 1.000 32.15357  ? 115 PHE B CD2 1 
ATOM   3124 C  CE1 . PHE B 1 115 ? -27.21600 19.61600  -16.33800 1.000 33.58008  ? 115 PHE B CE1 1 
ATOM   3125 C  CE2 . PHE B 1 115 ? -27.67500 21.48000  -14.90100 1.000 31.69587  ? 115 PHE B CE2 1 
ATOM   3126 C  CZ  . PHE B 1 115 ? -27.71800 20.90000  -16.15800 1.000 30.81668  ? 115 PHE B CZ  1 
ATOM   3127 N  N   . LEU B 1 116 ? -27.92300 18.99100  -10.31300 1.000 27.17558  ? 116 LEU B N   1 
ATOM   3128 C  CA  . LEU B 1 116 ? -28.89000 19.79000  -9.58600  1.000 28.41813  ? 116 LEU B CA  1 
ATOM   3129 C  C   . LEU B 1 116 ? -28.70500 21.27200  -9.89700  1.000 31.92297  ? 116 LEU B C   1 
ATOM   3130 O  O   . LEU B 1 116 ? -27.57300 21.77000  -9.95400  1.000 31.24050  ? 116 LEU B O   1 
ATOM   3131 C  CB  . LEU B 1 116 ? -28.70700 19.53800  -8.09300  1.000 29.14601  ? 116 LEU B CB  1 
ATOM   3132 C  CG  . LEU B 1 116 ? -29.60700 20.15000  -7.02900  1.000 33.69893  ? 116 LEU B CG  1 
ATOM   3133 C  CD1 . LEU B 1 116 ? -29.25800 21.60400  -6.78400  1.000 40.42473  ? 116 LEU B CD1 1 
ATOM   3134 C  CD2 . LEU B 1 116 ? -31.01000 19.99900  -7.49000  1.000 38.15636  ? 116 LEU B CD2 1 
ATOM   3135 N  N   . ARG B 1 117 ? -29.82200 21.96800  -10.11100 1.000 28.77191  ? 117 ARG B N   1 
ATOM   3136 C  CA  . ARG B 1 117 ? -29.88600 23.42300  -10.03500 1.000 33.05573  ? 117 ARG B CA  1 
ATOM   3137 C  C   . ARG B 1 117 ? -30.93400 23.80200  -8.99800  1.000 35.08015  ? 117 ARG B C   1 
ATOM   3138 O  O   . ARG B 1 117 ? -31.96300 23.12600  -8.87400  1.000 31.61789  ? 117 ARG B O   1 
ATOM   3139 C  CB  . ARG B 1 117 ? -30.24100 24.06100  -11.39000 1.000 35.43137  ? 117 ARG B CB  1 
ATOM   3140 C  CG  . ARG B 1 117 ? -29.10600 23.97900  -12.42600 1.000 34.76764  ? 117 ARG B CG  1 
ATOM   3141 C  CD  . ARG B 1 117 ? -27.91300 24.84900  -12.00400 1.000 40.13987  ? 117 ARG B CD  1 
ATOM   3142 N  NE  . ARG B 1 117 ? -28.14700 26.26300  -12.28600 1.000 45.34577  ? 117 ARG B NE  1 
ATOM   3143 C  CZ  . ARG B 1 117 ? -28.35800 27.19900  -11.37000 1.000 45.05498  ? 117 ARG B CZ  1 
ATOM   3144 N  NH1 . ARG B 1 117 ? -28.31000 26.92800  -10.07200 1.000 45.57326  ? 117 ARG B NH1 1 
ATOM   3145 N  NH2 . ARG B 1 117 ? -28.61700 28.44300  -11.76300 1.000 47.73829  ? 117 ARG B NH2 1 
ATOM   3146 N  N   . GLU B 1 118 ? -30.66600 24.87400  -8.25000  1.000 33.48556  ? 118 GLU B N   1 
ATOM   3147 C  CA  . GLU B 1 118 ? -31.62900 25.45500  -7.32500  1.000 37.67223  ? 118 GLU B CA  1 
ATOM   3148 C  C   . GLU B 1 118 ? -31.80600 26.92600  -7.66500  1.000 39.54252  ? 118 GLU B C   1 
ATOM   3149 O  O   . GLU B 1 118 ? -30.83900 27.69100  -7.63900  1.000 39.55227  ? 118 GLU B O   1 
ATOM   3150 C  CB  . GLU B 1 118 ? -31.17500 25.29400  -5.87200  1.000 38.77547  ? 118 GLU B CB  1 
ATOM   3151 C  CG  . GLU B 1 118 ? -32.28400 24.82100  -4.98000  1.000 43.89172  ? 118 GLU B CG  1 
ATOM   3152 C  CD  . GLU B 1 118 ? -31.88100 24.67500  -3.52200  1.000 48.28888  ? 118 GLU B CD  1 
ATOM   3153 O  OE1 . GLU B 1 118 ? -31.27600 25.61200  -2.95900  1.000 53.58286  ? 118 GLU B OE1 1 
ATOM   3154 O  OE2 . GLU B 1 118 ? -32.18200 23.61300  -2.93200  1.000 46.65567  ? 118 GLU B OE2 1 
ATOM   3155 N  N   . ILE B 1 119 ? -33.03600 27.32300  -7.96400  1.000 40.29989  ? 119 ILE B N   1 
ATOM   3156 C  CA  . ILE B 1 119 ? -33.34800 28.69600  -8.33800  1.000 39.40383  ? 119 ILE B CA  1 
ATOM   3157 C  C   . ILE B 1 119 ? -34.01100 29.38200  -7.14200  1.000 42.45929  ? 119 ILE B C   1 
ATOM   3158 O  O   . ILE B 1 119 ? -35.10200 28.98500  -6.71300  1.000 40.65423  ? 119 ILE B O   1 
ATOM   3159 C  CB  . ILE B 1 119 ? -34.23200 28.74900  -9.59100  1.000 40.07794  ? 119 ILE B CB  1 
ATOM   3160 C  CG1 . ILE B 1 119 ? -33.55500 28.01600  -10.76500 1.000 42.27673  ? 119 ILE B CG1 1 
ATOM   3161 C  CG2 . ILE B 1 119 ? -34.48200 30.19300  -9.99900  1.000 40.45263  ? 119 ILE B CG2 1 
ATOM   3162 C  CD1 . ILE B 1 119 ? -33.94300 26.55400  -10.91200 1.000 41.14126  ? 119 ILE B CD1 1 
ATOM   3163 N  N   . GLU B 1 120 ? -33.35200 30.41300  -6.60700  1.000 41.23193  ? 120 GLU B N   1 
ATOM   3164 C  CA  . GLU B 1 120 ? -33.81000 31.12600  -5.41600  1.000 43.58373  ? 120 GLU B CA  1 
ATOM   3165 C  C   . GLU B 1 120 ? -34.91600 32.12100  -5.75600  1.000 42.23351  ? 120 GLU B C   1 
ATOM   3166 O  O   . GLU B 1 120 ? -35.07800 32.53400  -6.90700  1.000 46.02573  ? 120 GLU B O   1 
ATOM   3167 C  CB  . GLU B 1 120 ? -32.66000 31.89300  -4.74900  1.000 40.91465  ? 120 GLU B CB  1 
ATOM   3168 C  CG  . GLU B 1 120 ? -31.49100 31.03700  -4.27100  1.000 47.10630  ? 120 GLU B CG  1 
ATOM   3169 C  CD  . GLU B 1 120 ? -30.41100 30.86500  -5.33800  1.000 56.33032  ? 120 GLU B CD  1 
ATOM   3170 O  OE1 . GLU B 1 120 ? -30.75300 30.75000  -6.54600  1.000 52.89648  ? 120 GLU B OE1 1 
ATOM   3171 O  OE2 . GLU B 1 120 ? -29.21500 30.86400  -4.96500  1.000 60.39783  ? 120 GLU B OE2 1 
ATOM   3172 N  N   . SER B 1 121 ? -35.66300 32.53000  -4.72100  1.000 43.30949  ? 121 SER B N   1 
ATOM   3173 C  CA  . SER B 1 121 ? -36.55700 33.67400  -4.83800  1.000 43.65644  ? 121 SER B CA  1 
ATOM   3174 C  C   . SER B 1 121 ? -35.82700 34.85100  -5.47800  1.000 47.44357  ? 121 SER B C   1 
ATOM   3175 O  O   . SER B 1 121 ? -34.62500 35.05600  -5.26400  1.000 45.35126  ? 121 SER B O   1 
ATOM   3176 C  CB  . SER B 1 121 ? -37.08700 34.09400  -3.46200  1.000 42.94437  ? 121 SER B CB  1 
ATOM   3177 O  OG  . SER B 1 121 ? -38.03900 33.17300  -2.95000  1.000 43.48060  ? 121 SER B OG  1 
ATOM   3178 N  N   . GLY B 1 122 ? -36.56000 35.62900  -6.27400  1.000 45.11387  ? 122 GLY B N   1 
ATOM   3179 C  CA  . GLY B 1 122 ? -36.00200 36.81700  -6.87900  1.000 47.35721  ? 122 GLY B CA  1 
ATOM   3180 C  C   . GLY B 1 122 ? -35.21500 36.59700  -8.15100  1.000 51.71775  ? 122 GLY B C   1 
ATOM   3181 O  O   . GLY B 1 122 ? -34.72600 37.57400  -8.73200  1.000 54.80961  ? 122 GLY B O   1 
ATOM   3182 N  N   . MET B 1 123 ? -35.08200 35.36200  -8.61000  1.000 45.57941  ? 123 MET B N   1 
ATOM   3183 C  CA  . MET B 1 123 ? -34.31800 35.12800  -9.82700  1.000 49.96642  ? 123 MET B CA  1 
ATOM   3184 C  C   . MET B 1 123 ? -35.19100 35.33100  -11.07100 1.000 50.03845  ? 123 MET B C   1 
ATOM   3185 O  O   . MET B 1 123 ? -36.36100 34.92800  -11.08900 1.000 49.13034  ? 123 MET B O   1 
ATOM   3186 C  CB  . MET B 1 123 ? -33.74000 33.71500  -9.82400  1.000 51.27368  ? 123 MET B CB  1 
ATOM   3187 C  CG  . MET B 1 123 ? -32.24300 33.66000  -10.09300 1.000 59.39060  ? 123 MET B CG  1 
ATOM   3188 S  SD  . MET B 1 123 ? -31.35300 34.93800  -9.17300  1.000 75.97161  ? 123 MET B SD  1 
ATOM   3189 C  CE  . MET B 1 123 ? -29.69400 34.75400  -9.85200  1.000 67.61091  ? 123 MET B CE  1 
ATOM   3190 N  N   . PRO B 1 124 ? -34.65600 35.95400  -12.11700 1.000 50.72009  ? 124 PRO B N   1 
ATOM   3191 C  CA  . PRO B 1 124 ? -35.42000 36.13000  -13.35500 1.000 50.04725  ? 124 PRO B CA  1 
ATOM   3192 C  C   . PRO B 1 124 ? -35.43700 34.85400  -14.19800 1.000 44.18060  ? 124 PRO B C   1 
ATOM   3193 O  O   . PRO B 1 124 ? -34.67600 33.91000  -13.98200 1.000 40.67517  ? 124 PRO B O   1 
ATOM   3194 C  CB  . PRO B 1 124 ? -34.67200 37.26500  -14.06700 1.000 50.32131  ? 124 PRO B CB  1 
ATOM   3195 C  CG  . PRO B 1 124 ? -33.26200 37.13200  -13.59000 1.000 48.92555  ? 124 PRO B CG  1 
ATOM   3196 C  CD  . PRO B 1 124 ? -33.35100 36.63600  -12.16800 1.000 53.78193  ? 124 PRO B CD  1 
ATOM   3197 N  N   . ALA B 1 125 ? -36.33200 34.84100  -15.17800 1.000 39.53385  ? 125 ALA B N   1 
ATOM   3198 C  CA  . ALA B 1 125 ? -36.46000 33.66900  -16.03500 1.000 42.45784  ? 125 ALA B CA  1 
ATOM   3199 C  C   . ALA B 1 125 ? -35.32000 33.60000  -17.05000 1.000 40.66053  ? 125 ALA B C   1 
ATOM   3200 O  O   . ALA B 1 125 ? -34.72100 34.61300  -17.41800 1.000 44.68481  ? 125 ALA B O   1 
ATOM   3201 C  CB  . ALA B 1 125 ? -37.80600 33.68600  -16.76100 1.000 42.92210  ? 125 ALA B CB  1 
ATOM   3202 N  N   . GLN B 1 126 ? -35.01900 32.38300  -17.49400 1.000 39.57323  ? 126 GLN B N   1 
ATOM   3203 C  CA  . GLN B 1 126 ? -34.06600 32.17800  -18.57100 1.000 41.16926  ? 126 GLN B CA  1 
ATOM   3204 C  C   . GLN B 1 126 ? -34.59100 32.75800  -19.87900 1.000 38.71079  ? 126 GLN B C   1 
ATOM   3205 O  O   . GLN B 1 126 ? -35.80200 32.80300  -20.10500 1.000 40.69061  ? 126 GLN B O   1 
ATOM   3206 C  CB  . GLN B 1 126 ? -33.80600 30.68600  -18.79300 1.000 40.39184  ? 126 GLN B CB  1 
ATOM   3207 C  CG  . GLN B 1 126 ? -32.72600 30.09500  -17.97200 1.000 39.02824  ? 126 GLN B CG  1 
ATOM   3208 C  CD  . GLN B 1 126 ? -32.59700 28.62000  -18.22700 1.000 42.26022  ? 126 GLN B CD  1 
ATOM   3209 O  OE1 . GLN B 1 126 ? -33.54900 27.97100  -18.65900 1.000 39.14431  ? 126 GLN B OE1 1 
ATOM   3210 N  NE2 . GLN B 1 126 ? -31.42300 28.07700  -17.96300 1.000 44.47714  ? 126 GLN B NE2 1 
ATOM   3211 N  N   . PRO B 1 127 ? -33.69800 33.14500  -20.78900 1.000 42.79408  ? 127 PRO B N   1 
ATOM   3212 C  CA  . PRO B 1 127 ? -34.12400 33.36700  -22.17800 1.000 44.30010  ? 127 PRO B CA  1 
ATOM   3213 C  C   . PRO B 1 127 ? -34.58000 32.05500  -22.80800 1.000 36.86877  ? 127 PRO B C   1 
ATOM   3214 O  O   . PRO B 1 127 ? -34.12900 30.97000  -22.43000 1.000 33.17285  ? 127 PRO B O   1 
ATOM   3215 C  CB  . PRO B 1 127 ? -32.85600 33.89500  -22.86900 1.000 42.78183  ? 127 PRO B CB  1 
ATOM   3216 C  CG  . PRO B 1 127 ? -31.85700 34.11900  -21.78500 1.000 47.79819  ? 127 PRO B CG  1 
ATOM   3217 C  CD  . PRO B 1 127 ? -32.23500 33.24500  -20.64100 1.000 42.81408  ? 127 PRO B CD  1 
ATOM   3218 N  N   . PHE B 1 128 ? -35.50300 32.16500  -23.76200 1.000 36.32919  ? 128 PHE B N   1 
ATOM   3219 C  CA  . PHE B 1 128 ? -35.88900 31.00200  -24.54800 1.000 36.25727  ? 128 PHE B CA  1 
ATOM   3220 C  C   . PHE B 1 128 ? -34.70200 30.52200  -25.37100 1.000 35.61610  ? 128 PHE B C   1 
ATOM   3221 O  O   . PHE B 1 128 ? -33.91700 31.32600  -25.87900 1.000 36.98289  ? 128 PHE B O   1 
ATOM   3222 C  CB  . PHE B 1 128 ? -37.06100 31.33100  -25.46000 1.000 34.40590  ? 128 PHE B CB  1 
ATOM   3223 C  CG  . PHE B 1 128 ? -38.38000 31.36400  -24.75800 1.000 39.68113  ? 128 PHE B CG  1 
ATOM   3224 C  CD1 . PHE B 1 128 ? -38.89700 30.20900  -24.18200 1.000 36.50542  ? 128 PHE B CD1 1 
ATOM   3225 C  CD2 . PHE B 1 128 ? -39.11300 32.54100  -24.67800 1.000 38.75081  ? 128 PHE B CD2 1 
ATOM   3226 C  CE1 . PHE B 1 128 ? -40.11900 30.22800  -23.53300 1.000 36.35523  ? 128 PHE B CE1 1 
ATOM   3227 C  CE2 . PHE B 1 128 ? -40.34000 32.55800  -24.03300 1.000 44.79546  ? 128 PHE B CE2 1 
ATOM   3228 C  CZ  . PHE B 1 128 ? -40.83800 31.39500  -23.45800 1.000 40.02217  ? 128 PHE B CZ  1 
ATOM   3229 N  N   . HIS B 1 129 ? -34.54800 29.20700  -25.47600 1.000 32.93184  ? 129 HIS B N   1 
ATOM   3230 C  CA  . HIS B 1 129 ? -33.38000 28.64900  -26.14400 1.000 35.10724  ? 129 HIS B CA  1 
ATOM   3231 C  C   . HIS B 1 129 ? -33.65700 27.20800  -26.53600 1.000 34.09367  ? 129 HIS B C   1 
ATOM   3232 O  O   . HIS B 1 129 ? -34.67600 26.62100  -26.16700 1.000 33.58782  ? 129 HIS B O   1 
ATOM   3233 C  CB  . HIS B 1 129 ? -32.15400 28.70300  -25.23700 1.000 33.42633  ? 129 HIS B CB  1 
ATOM   3234 C  CG  . HIS B 1 129 ? -32.33700 27.94200  -23.96600 1.000 34.20370  ? 129 HIS B CG  1 
ATOM   3235 N  ND1 . HIS B 1 129 ? -33.01600 28.46400  -22.88700 1.000 36.97614  ? 129 HIS B ND1 1 
ATOM   3236 C  CD2 . HIS B 1 129 ? -31.96700 26.69300  -23.61000 1.000 33.92566  ? 129 HIS B CD2 1 
ATOM   3237 C  CE1 . HIS B 1 129 ? -33.03900 27.57500  -21.91400 1.000 35.78820  ? 129 HIS B CE1 1 
ATOM   3238 N  NE2 . HIS B 1 129 ? -32.40500 26.49500  -22.32500 1.000 33.85270  ? 129 HIS B NE2 1 
ATOM   3239 N  N   . ARG B 1 130 ? -32.70500 26.63800  -27.25700 1.000 35.22495  ? 130 ARG B N   1 
ATOM   3240 C  CA  . ARG B 1 130 ? -32.62500 25.20900  -27.48900 1.000 35.59299  ? 130 ARG B CA  1 
ATOM   3241 C  C   . ARG B 1 130 ? -31.42600 24.65400  -26.73600 1.000 32.68721  ? 130 ARG B C   1 
ATOM   3242 O  O   . ARG B 1 130 ? -30.46800 25.36800  -26.45500 1.000 35.03922  ? 130 ARG B O   1 
ATOM   3243 C  CB  . ARG B 1 130 ? -32.51300 24.91000  -28.99100 1.000 34.97496  ? 130 ARG B CB  1 
ATOM   3244 C  CG  . ARG B 1 130 ? -33.79400 25.24300  -29.73800 1.000 33.25276  ? 130 ARG B CG  1 
ATOM   3245 C  CD  . ARG B 1 130 ? -33.63700 25.15100  -31.24600 1.000 28.07222  ? 130 ARG B CD  1 
ATOM   3246 N  NE  . ARG B 1 130 ? -34.95100 25.06500  -31.86700 1.000 31.24131  ? 130 ARG B NE  1 
ATOM   3247 C  CZ  . ARG B 1 130 ? -35.19400 25.24600  -33.15800 1.000 39.34924  ? 130 ARG B CZ  1 
ATOM   3248 N  NH1 . ARG B 1 130 ? -34.23500 25.60300  -34.00000 1.000 36.87471  ? 130 ARG B NH1 1 
ATOM   3249 N  NH2 . ARG B 1 130 ? -36.42800 25.05100  -33.61600 1.000 37.96959  ? 130 ARG B NH2 1 
ATOM   3250 N  N   . ASP B 1 131 ? -31.49400 23.36500  -26.40200 1.000 33.68432  ? 131 ASP B N   1 
ATOM   3251 C  CA  . ASP B 1 131 ? -30.41200 22.67300  -25.68700 1.000 31.69834  ? 131 ASP B CA  1 
ATOM   3252 C  C   . ASP B 1 131 ? -29.41000 22.11500  -26.69700 1.000 34.57792  ? 131 ASP B C   1 
ATOM   3253 O  O   . ASP B 1 131 ? -29.28700 20.90800  -26.90400 1.000 39.46710  ? 131 ASP B O   1 
ATOM   3254 C  CB  . ASP B 1 131 ? -30.97700 21.56000  -24.80800 1.000 32.15855  ? 131 ASP B CB  1 
ATOM   3255 C  CG  . ASP B 1 131 ? -31.66400 22.09300  -23.54500 1.000 36.18439  ? 131 ASP B CG  1 
ATOM   3256 O  OD1 . ASP B 1 131 ? -31.46700 23.28000  -23.24100 1.000 33.34550  ? 131 ASP B OD1 1 
ATOM   3257 O  OD2 . ASP B 1 131 ? -32.39000 21.32500  -22.87200 1.000 36.88692  ? 131 ASP B OD2 1 
ATOM   3258 N  N   . ASP B 1 132 ? -28.69800 23.02700  -27.35400 1.000 31.27359  ? 132 ASP B N   1 
ATOM   3259 C  CA  . ASP B 1 132 ? -27.74100 22.62700  -28.37700 1.000 32.90270  ? 132 ASP B CA  1 
ATOM   3260 C  C   . ASP B 1 132 ? -26.36100 23.23000  -28.13100 1.000 33.19884  ? 132 ASP B C   1 
ATOM   3261 O  O   . ASP B 1 132 ? -25.58400 23.39000  -29.07700 1.000 34.47462  ? 132 ASP B O   1 
ATOM   3262 C  CB  . ASP B 1 132 ? -28.24700 23.00500  -29.77400 1.000 34.88823  ? 132 ASP B CB  1 
ATOM   3263 C  CG  . ASP B 1 132 ? -28.57100 24.49900  -29.90900 1.000 40.76803  ? 132 ASP B CG  1 
ATOM   3264 O  OD1 . ASP B 1 132 ? -28.30100 25.28500  -28.96300 1.000 38.35018  ? 132 ASP B OD1 1 
ATOM   3265 O  OD2 . ASP B 1 132 ? -29.11700 24.88800  -30.97200 1.000 39.97953  ? 132 ASP B OD2 1 
ATOM   3266 N  N   . ALA B 1 133 ? -26.04300 23.56500  -26.88300 1.000 31.56784  ? 133 ALA B N   1 
ATOM   3267 C  CA  . ALA B 1 133 ? -24.80500 24.26400  -26.57300 1.000 32.56588  ? 133 ALA B CA  1 
ATOM   3268 C  C   . ALA B 1 133 ? -23.68800 23.33900  -26.11700 1.000 29.63749  ? 133 ALA B C   1 
ATOM   3269 O  O   . ALA B 1 133 ? -22.52800 23.59700  -26.42600 1.000 32.09698  ? 133 ALA B O   1 
ATOM   3270 C  CB  . ALA B 1 133 ? -25.04200 25.32800  -25.50000 1.000 31.08259  ? 133 ALA B CB  1 
ATOM   3271 N  N   . THR B 1 134 ? -23.99200 22.26700  -25.39500 1.000 28.07036  ? 134 THR B N   1 
ATOM   3272 C  CA  . THR B 1 134 ? -22.91000 21.43400  -24.89300 1.000 26.72319  ? 134 THR B CA  1 
ATOM   3273 C  C   . THR B 1 134 ? -22.21600 20.70200  -26.03600 1.000 27.42864  ? 134 THR B C   1 
ATOM   3274 O  O   . THR B 1 134 ? -20.98700 20.56100  -26.04700 1.000 23.82407  ? 134 THR B O   1 
ATOM   3275 C  CB  . THR B 1 134 ? -23.44200 20.45000  -23.86500 1.000 29.02864  ? 134 THR B CB  1 
ATOM   3276 O  OG1 . THR B 1 134 ? -24.12500 21.18100  -22.84000 1.000 35.02590  ? 134 THR B OG1 1 
ATOM   3277 C  CG2 . THR B 1 134 ? -22.27600 19.67700  -23.23800 1.000 28.14665  ? 134 THR B CG2 1 
ATOM   3278 N  N   . HIS B 1 135 ? -22.99600 20.25600  -27.01700 1.000 26.77167  ? 135 HIS B N   1 
ATOM   3279 C  CA  . HIS B 1 135 ? -22.50200 19.61000  -28.22800 1.000 28.01160  ? 135 HIS B CA  1 
ATOM   3280 C  C   . HIS B 1 135 ? -22.94900 20.50100  -29.37800 1.000 26.49317  ? 135 HIS B C   1 
ATOM   3281 O  O   . HIS B 1 135 ? -23.97100 20.22900  -30.02600 1.000 25.62128  ? 135 HIS B O   1 
ATOM   3282 C  CB  . HIS B 1 135 ? -23.05200 18.19400  -28.37100 1.000 27.21410  ? 135 HIS B CB  1 
ATOM   3283 C  CG  . HIS B 1 135 ? -22.62600 17.26800  -27.28100 1.000 27.59422  ? 135 HIS B CG  1 
ATOM   3284 N  ND1 . HIS B 1 135 ? -23.27700 17.19400  -26.06700 1.000 24.46344  ? 135 HIS B ND1 1 
ATOM   3285 C  CD2 . HIS B 1 135 ? -21.61200 16.36100  -27.23000 1.000 26.73465  ? 135 HIS B CD2 1 
ATOM   3286 C  CE1 . HIS B 1 135 ? -22.69200 16.27300  -25.31800 1.000 24.80400  ? 135 HIS B CE1 1 
ATOM   3287 N  NE2 . HIS B 1 135 ? -21.68100 15.75100  -26.00100 1.000 27.86654  ? 135 HIS B NE2 1 
ATOM   3288 N  N   . PRO B 1 136 ? -22.20800 21.57900  -29.64300 1.000 27.45287  ? 136 PRO B N   1 
ATOM   3289 C  CA  . PRO B 1 136 ? -22.63200 22.55500  -30.66500 1.000 26.63215  ? 136 PRO B CA  1 
ATOM   3290 C  C   . PRO B 1 136 ? -22.93700 21.96200  -32.04300 1.000 28.95838  ? 136 PRO B C   1 
ATOM   3291 O  O   . PRO B 1 136 ? -23.73600 22.55500  -32.76900 1.000 27.08765  ? 136 PRO B O   1 
ATOM   3292 C  CB  . PRO B 1 136 ? -21.44700 23.52600  -30.74200 1.000 25.73560  ? 136 PRO B CB  1 
ATOM   3293 C  CG  . PRO B 1 136 ? -20.64000 23.30500  -29.50100 1.000 30.30675  ? 136 PRO B CG  1 
ATOM   3294 C  CD  . PRO B 1 136 ? -20.89700 21.89800  -29.04300 1.000 26.29107  ? 136 PRO B CD  1 
ATOM   3295 N  N   . LEU B 1 137 ? -22.36200 20.80200  -32.41900 1.000 27.27159  ? 137 LEU B N   1 
ATOM   3296 C  CA  . LEU B 1 137 ? -22.70300 20.22100  -33.72600 1.000 28.55716  ? 137 LEU B CA  1 
ATOM   3297 C  C   . LEU B 1 137 ? -24.21000 20.00000  -33.86400 1.000 29.27988  ? 137 LEU B C   1 
ATOM   3298 O  O   . LEU B 1 137 ? -24.74600 20.03100  -34.98100 1.000 30.07426  ? 137 LEU B O   1 
ATOM   3299 C  CB  . LEU B 1 137 ? -21.94300 18.90400  -33.96100 1.000 26.83780  ? 137 LEU B CB  1 
ATOM   3300 C  CG  . LEU B 1 137 ? -22.20100 17.65600  -33.09000 1.000 26.49595  ? 137 LEU B CG  1 
ATOM   3301 C  CD1 . LEU B 1 137 ? -23.48800 16.95000  -33.47600 1.000 26.69253  ? 137 LEU B CD1 1 
ATOM   3302 C  CD2 . LEU B 1 137 ? -21.01200 16.64000  -33.09800 1.000 23.95974  ? 137 LEU B CD2 1 
ATOM   3303 N  N   . MET B 1 138 ? -24.89900 19.78500  -32.74100 1.000 25.81952  ? 138 MET B N   1 
ATOM   3304 C  CA  . MET B 1 138 ? -26.35300 19.58600  -32.73500 1.000 30.06299  ? 138 MET B CA  1 
ATOM   3305 C  C   . MET B 1 138 ? -27.09700 20.76600  -33.35100 1.000 30.02210  ? 138 MET B C   1 
ATOM   3306 O  O   . MET B 1 138 ? -28.18700 20.59700  -33.91400 1.000 28.69087  ? 138 MET B O   1 
ATOM   3307 C  CB  . MET B 1 138 ? -26.83800 19.37500  -31.29600 1.000 29.22929  ? 138 MET B CB  1 
ATOM   3308 C  CG  . MET B 1 138 ? -26.57000 17.97500  -30.71400 1.000 28.51257  ? 138 MET B CG  1 
ATOM   3309 S  SD  . MET B 1 138 ? -27.07400 17.87100  -28.96900 1.000 37.47087  ? 138 MET B SD  1 
ATOM   3310 C  CE  . MET B 1 138 ? -28.78900 18.36300  -29.06500 1.000 32.81993  ? 138 MET B CE  1 
ATOM   3311 N  N   . HIS B 1 139 ? -26.52000 21.96500  -33.26000 1.000 28.02363  ? 139 HIS B N   1 
ATOM   3312 C  CA  . HIS B 1 139 ? -27.14100 23.15600  -33.82000 1.000 30.58416  ? 139 HIS B CA  1 
ATOM   3313 C  C   . HIS B 1 139 ? -27.31300 23.07000  -35.33500 1.000 33.34743  ? 139 HIS B C   1 
ATOM   3314 O  O   . HIS B 1 139 ? -28.16100 23.77700  -35.89500 1.000 32.05732  ? 139 HIS B O   1 
ATOM   3315 C  CB  . HIS B 1 139 ? -26.28700 24.36800  -33.45500 1.000 32.71865  ? 139 HIS B CB  1 
ATOM   3316 C  CG  . HIS B 1 139 ? -26.87700 25.67200  -33.87500 1.000 36.18498  ? 139 HIS B CG  1 
ATOM   3317 N  ND1 . HIS B 1 139 ? -27.93800 26.25500  -33.21300 1.000 35.13269  ? 139 HIS B ND1 1 
ATOM   3318 C  CD2 . HIS B 1 139 ? -26.55100 26.50900  -34.88500 1.000 34.53935  ? 139 HIS B CD2 1 
ATOM   3319 C  CE1 . HIS B 1 139 ? -28.23700 27.39900  -33.80000 1.000 34.90858  ? 139 HIS B CE1 1 
ATOM   3320 N  NE2 . HIS B 1 139 ? -27.41700 27.57100  -34.82100 1.000 36.87023  ? 139 HIS B NE2 1 
ATOM   3321 N  N   . TYR B 1 140 ? -26.53700 22.22000  -36.01000 1.000 30.20087  ? 140 TYR B N   1 
ATOM   3322 C  CA  . TYR B 1 140 ? -26.58700 22.12300  -37.46400 1.000 31.45798  ? 140 TYR B CA  1 
ATOM   3323 C  C   . TYR B 1 140 ? -27.29800 20.86900  -37.95100 1.000 32.99453  ? 140 TYR B C   1 
ATOM   3324 O  O   . TYR B 1 140 ? -27.46800 20.70600  -39.16200 1.000 33.50026  ? 140 TYR B O   1 
ATOM   3325 C  CB  . TYR B 1 140 ? -25.16500 22.16200  -38.05200 1.000 28.94580  ? 140 TYR B CB  1 
ATOM   3326 C  CG  . TYR B 1 140 ? -24.27400 23.26700  -37.50100 1.000 30.54074  ? 140 TYR B CG  1 
ATOM   3327 C  CD1 . TYR B 1 140 ? -23.49200 23.02200  -36.37200 1.000 32.00973  ? 140 TYR B CD1 1 
ATOM   3328 C  CD2 . TYR B 1 140 ? -24.22800 24.52000  -38.11600 1.000 35.51911  ? 140 TYR B CD2 1 
ATOM   3329 C  CE1 . TYR B 1 140 ? -22.69700 24.02400  -35.87400 1.000 32.68548  ? 140 TYR B CE1 1 
ATOM   3330 C  CE2 . TYR B 1 140 ? -23.40800 25.49500  -37.60300 1.000 34.58963  ? 140 TYR B CE2 1 
ATOM   3331 C  CZ  . TYR B 1 140 ? -22.64200 25.27600  -36.46800 1.000 36.97341  ? 140 TYR B CZ  1 
ATOM   3332 O  OH  . TYR B 1 140 ? -21.84400 26.23700  -35.96600 1.000 41.45549  ? 140 TYR B OH  1 
ATOM   3333 N  N   . GLN B 1 141 ? -27.68600 19.97000  -37.05300 1.000 33.18860  ? 141 GLN B N   1 
ATOM   3334 C  CA  . GLN B 1 141 ? -28.47100 18.81300  -37.45500 1.000 31.60613  ? 141 GLN B CA  1 
ATOM   3335 C  C   . GLN B 1 141 ? -29.83200 19.26600  -37.97000 1.000 34.21366  ? 141 GLN B C   1 
ATOM   3336 O  O   . GLN B 1 141 ? -30.51100 20.06400  -37.30400 1.000 37.24482  ? 141 GLN B O   1 
ATOM   3337 C  CB  . GLN B 1 141 ? -28.65300 17.86400  -36.28000 1.000 32.32779  ? 141 GLN B CB  1 
ATOM   3338 C  CG  . GLN B 1 141 ? -27.37800 17.16600  -35.87000 1.000 31.16827  ? 141 GLN B CG  1 
ATOM   3339 C  CD  . GLN B 1 141 ? -27.18500 15.83200  -36.59500 1.000 37.26800  ? 141 GLN B CD  1 
ATOM   3340 O  OE1 . GLN B 1 141 ? -26.33200 15.70000  -37.49300 1.000 34.41242  ? 141 GLN B OE1 1 
ATOM   3341 N  NE2 . GLN B 1 141 ? -27.96500 14.82900  -36.18800 1.000 31.86876  ? 141 GLN B NE2 1 
ATOM   3342 N  N   . PRO B 1 142 ? -30.27000 18.78400  -39.12500 1.000 33.95230  ? 142 PRO B N   1 
ATOM   3343 C  CA  . PRO B 1 142 ? -31.61600 19.10700  -39.60300 1.000 37.50110  ? 142 PRO B CA  1 
ATOM   3344 C  C   . PRO B 1 142 ? -32.67400 18.41900  -38.76000 1.000 39.20634  ? 142 PRO B C   1 
ATOM   3345 O  O   . PRO B 1 142 ? -32.43100 17.38700  -38.12900 1.000 34.87655  ? 142 PRO B O   1 
ATOM   3346 C  CB  . PRO B 1 142 ? -31.63800 18.56400  -41.03600 1.000 39.09312  ? 142 PRO B CB  1 
ATOM   3347 C  CG  . PRO B 1 142 ? -30.24000 18.12000  -41.33500 1.000 40.44444  ? 142 PRO B CG  1 
ATOM   3348 C  CD  . PRO B 1 142 ? -29.56400 17.86600  -40.02800 1.000 36.44746  ? 142 PRO B CD  1 
ATOM   3349 N  N   . LEU B 1 143 ? -33.88300 18.99300  -38.80500 1.000 40.54381  ? 143 LEU B N   1 
ATOM   3350 C  CA  . LEU B 1 143 ? -34.99200 18.49200  -37.99500 1.000 40.70639  ? 143 LEU B CA  1 
ATOM   3351 C  C   . LEU B 1 143 ? -35.28800 17.01300  -38.26500 1.000 41.25531  ? 143 LEU B C   1 
ATOM   3352 O  O   . LEU B 1 143 ? -35.56900 16.25300  -37.33200 1.000 41.89519  ? 143 LEU B O   1 
ATOM   3353 C  CB  . LEU B 1 143 ? -36.24000 19.34100  -38.25200 1.000 43.37124  ? 143 LEU B CB  1 
ATOM   3354 C  CG  . LEU B 1 143 ? -37.54800 18.76000  -37.69500 1.000 42.43966  ? 143 LEU B CG  1 
ATOM   3355 C  CD1 . LEU B 1 143 ? -37.50300 18.63100  -36.17600 1.000 38.95184  ? 143 LEU B CD1 1 
ATOM   3356 C  CD2 . LEU B 1 143 ? -38.76800 19.56500  -38.16200 1.000 46.32984  ? 143 LEU B CD2 1 
ATOM   3357 N  N   . GLU B 1 144 ? -35.23200 16.58600  -39.53000 1.000 38.39700  ? 144 GLU B N   1 
ATOM   3358 C  CA  . GLU B 1 144 ? -35.55900 15.21500  -39.89600 1.000 42.13320  ? 144 GLU B CA  1 
ATOM   3359 C  C   . GLU B 1 144 ? -34.45900 14.20300  -39.57100 1.000 42.49633  ? 144 GLU B C   1 
ATOM   3360 O  O   . GLU B 1 144 ? -34.71300 12.99800  -39.67700 1.000 40.27176  ? 144 GLU B O   1 
ATOM   3361 C  CB  . GLU B 1 144 ? -35.88900 15.13300  -41.39200 1.000 46.56973  ? 144 GLU B CB  1 
ATOM   3362 C  CG  . GLU B 1 144 ? -34.68800 15.28400  -42.31100 1.000 46.45625  ? 144 GLU B CG  1 
ATOM   3363 C  CD  . GLU B 1 144 ? -34.37200 16.74000  -42.66800 1.000 54.20606  ? 144 GLU B CD  1 
ATOM   3364 O  OE1 . GLU B 1 144 ? -34.85200 17.67400  -41.96000 1.000 53.68359  ? 144 GLU B OE1 1 
ATOM   3365 O  OE2 . GLU B 1 144 ? -33.63000 16.94500  -43.65900 1.000 51.94962  ? 144 GLU B OE2 1 
ATOM   3366 N  N   . ALA B 1 145 ? -33.25900 14.64400  -39.18400 1.000 36.20330  ? 145 ALA B N   1 
ATOM   3367 C  CA  . ALA B 1 145 ? -32.21100 13.70500  -38.79600 1.000 37.11403  ? 145 ALA B CA  1 
ATOM   3368 C  C   . ALA B 1 145 ? -32.62800 12.91000  -37.55100 1.000 34.80565  ? 145 ALA B C   1 
ATOM   3369 O  O   . ALA B 1 145 ? -33.44100 13.37500  -36.75300 1.000 36.67132  ? 145 ALA B O   1 
ATOM   3370 C  CB  . ALA B 1 145 ? -30.90000 14.44900  -38.52700 1.000 34.17642  ? 145 ALA B CB  1 
ATOM   3371 N  N   . PRO B 1 146 ? -32.09500 11.70600  -37.36200 1.000 34.31075  ? 146 PRO B N   1 
ATOM   3372 C  CA  . PRO B 1 146 ? -32.38500 10.94400  -36.12600 1.000 35.23817  ? 146 PRO B CA  1 
ATOM   3373 C  C   . PRO B 1 146 ? -31.97900 11.73300  -34.89200 1.000 30.72100  ? 146 PRO B C   1 
ATOM   3374 O  O   . PRO B 1 146 ? -30.85000 12.23400  -34.81300 1.000 27.95498  ? 146 PRO B O   1 
ATOM   3375 C  CB  . PRO B 1 146 ? -31.53100 9.67600   -36.28100 1.000 33.96024  ? 146 PRO B CB  1 
ATOM   3376 C  CG  . PRO B 1 146 ? -31.27700 9.55600   -37.78200 1.000 37.91858  ? 146 PRO B CG  1 
ATOM   3377 C  CD  . PRO B 1 146 ? -31.24200 10.96000  -38.30600 1.000 34.75703  ? 146 PRO B CD  1 
ATOM   3378 N  N   . PRO B 1 147 ? -32.87200 11.89500  -33.91900 1.000 31.64207  ? 147 PRO B N   1 
ATOM   3379 C  CA  . PRO B 1 147 ? -32.52500 12.69500  -32.73000 1.000 27.92085  ? 147 PRO B CA  1 
ATOM   3380 C  C   . PRO B 1 147 ? -31.39700 12.06300  -31.93600 1.000 26.95989  ? 147 PRO B C   1 
ATOM   3381 O  O   . PRO B 1 147 ? -31.25700 10.84200  -31.88100 1.000 28.26952  ? 147 PRO B O   1 
ATOM   3382 C  CB  . PRO B 1 147 ? -33.82600 12.73100  -31.91900 1.000 33.22234  ? 147 PRO B CB  1 
ATOM   3383 C  CG  . PRO B 1 147 ? -34.72800 11.68000  -32.54900 1.000 36.07485  ? 147 PRO B CG  1 
ATOM   3384 C  CD  . PRO B 1 147 ? -34.31000 11.58600  -33.98600 1.000 35.26169  ? 147 PRO B CD  1 
ATOM   3385 N  N   . VAL B 1 148 ? -30.55900 12.91800  -31.35400 1.000 25.88224  ? 148 VAL B N   1 
ATOM   3386 C  CA  . VAL B 1 148 ? -29.39200 12.48700  -30.60200 1.000 23.68157  ? 148 VAL B CA  1 
ATOM   3387 C  C   . VAL B 1 148 ? -29.41600 12.95300  -29.15700 1.000 24.74088  ? 148 VAL B C   1 
ATOM   3388 O  O   . VAL B 1 148 ? -28.45700 12.70300  -28.42600 1.000 24.25760  ? 148 VAL B O   1 
ATOM   3389 C  CB  . VAL B 1 148 ? -28.08100 12.93400  -31.28200 1.000 26.79556  ? 148 VAL B CB  1 
ATOM   3390 C  CG1 . VAL B 1 148 ? -27.90700 12.21800  -32.63600 1.000 24.97055  ? 148 VAL B CG1 1 
ATOM   3391 C  CG2 . VAL B 1 148 ? -28.04100 14.46000  -31.46400 1.000 24.73417  ? 148 VAL B CG2 1 
ATOM   3392 N  N   . SER B 1 149 ? -30.49100 13.59700  -28.71000 1.000 27.32798  ? 149 SER B N   1 
ATOM   3393 C  CA  . SER B 1 149 ? -30.52300 14.14400  -27.36500 1.000 25.39520  ? 149 SER B CA  1 
ATOM   3394 C  C   . SER B 1 149 ? -31.95000 14.22000  -26.83400 1.000 25.44970  ? 149 SER B C   1 
ATOM   3395 O  O   . SER B 1 149 ? -32.89300 14.57200  -27.55400 1.000 26.44364  ? 149 SER B O   1 
ATOM   3396 C  CB  . SER B 1 149 ? -29.88700 15.53400  -27.33600 1.000 28.99620  ? 149 SER B CB  1 
ATOM   3397 O  OG  . SER B 1 149 ? -29.49700 15.86400  -26.01500 1.000 35.41448  ? 149 SER B OG  1 
ATOM   3398 N  N   . LEU B 1 150 ? -32.09400 13.93600  -25.55100 1.000 24.39340  ? 150 LEU B N   1 
ATOM   3399 C  CA  . LEU B 1 150 ? -33.39000 14.01000  -24.89500 1.000 27.62608  ? 150 LEU B CA  1 
ATOM   3400 C  C   . LEU B 1 150 ? -33.17100 14.60200  -23.51300 1.000 30.07876  ? 150 LEU B C   1 
ATOM   3401 O  O   . LEU B 1 150 ? -32.26000 14.16200  -22.80200 1.000 28.72298  ? 150 LEU B O   1 
ATOM   3402 C  CB  . LEU B 1 150 ? -34.03200 12.62000  -24.79700 1.000 27.34005  ? 150 LEU B CB  1 
ATOM   3403 C  CG  . LEU B 1 150 ? -35.38900 12.49500  -24.09500 1.000 30.36942  ? 150 LEU B CG  1 
ATOM   3404 C  CD1 . LEU B 1 150 ? -36.48500 13.09500  -24.97800 1.000 30.04389  ? 150 LEU B CD1 1 
ATOM   3405 C  CD2 . LEU B 1 150 ? -35.68500 11.02600  -23.77800 1.000 27.71898  ? 150 LEU B CD2 1 
ATOM   3406 N  N   . SER B 1 151 ? -33.98900 15.59900  -23.14000 1.000 30.75114  ? 151 SER B N   1 
ATOM   3407 C  CA  . SER B 1 151 ? -33.89500 16.26200  -21.84100 1.000 30.40252  ? 151 SER B CA  1 
ATOM   3408 C  C   . SER B 1 151 ? -34.94300 15.69000  -20.89200 1.000 29.13406  ? 151 SER B C   1 
ATOM   3409 O  O   . SER B 1 151 ? -36.12500 15.61900  -21.23100 1.000 27.74942  ? 151 SER B O   1 
ATOM   3410 C  CB  . SER B 1 151 ? -34.08000 17.78200  -21.97800 1.000 31.48821  ? 151 SER B CB  1 
ATOM   3411 O  OG  . SER B 1 151 ? -33.03700 18.36300  -22.75900 1.000 34.67380  ? 151 SER B OG  1 
ATOM   3412 N  N   . VAL B 1 152 ? -34.50700 15.27400  -19.70900 1.000 28.71088  ? 152 VAL B N   1 
ATOM   3413 C  CA  . VAL B 1 152 ? -35.39500 14.70800  -18.70700 1.000 28.77860  ? 152 VAL B CA  1 
ATOM   3414 C  C   . VAL B 1 152 ? -35.26300 15.56500  -17.45900 1.000 29.89911  ? 152 VAL B C   1 
ATOM   3415 O  O   . VAL B 1 152 ? -34.16900 15.68500  -16.89100 1.000 31.75625  ? 152 VAL B O   1 
ATOM   3416 C  CB  . VAL B 1 152 ? -35.07200 13.23800  -18.41300 1.000 32.43094  ? 152 VAL B CB  1 
ATOM   3417 C  CG1 . VAL B 1 152 ? -36.13300 12.64700  -17.49300 1.000 30.90802  ? 152 VAL B CG1 1 
ATOM   3418 C  CG2 . VAL B 1 152 ? -34.96600 12.44700  -19.71600 1.000 31.06437  ? 152 VAL B CG2 1 
ATOM   3419 N  N   . ILE B 1 153 ? -36.35800 16.18700  -17.05100 1.000 28.45814  ? 153 ILE B N   1 
ATOM   3420 C  CA  . ILE B 1 153 ? -36.32600 17.23500  -16.03700 1.000 31.94852  ? 153 ILE B CA  1 
ATOM   3421 C  C   . ILE B 1 153 ? -37.10500 16.76600  -14.80800 1.000 31.08150  ? 153 ILE B C   1 
ATOM   3422 O  O   . ILE B 1 153 ? -38.31500 16.50800  -14.88800 1.000 32.01577  ? 153 ILE B O   1 
ATOM   3423 C  CB  . ILE B 1 153 ? -36.87700 18.55100  -16.60400 1.000 30.20079  ? 153 ILE B CB  1 
ATOM   3424 C  CG1 . ILE B 1 153 ? -35.91600 19.04300  -17.69900 1.000 32.37905  ? 153 ILE B CG1 1 
ATOM   3425 C  CG2 . ILE B 1 153 ? -37.02400 19.57200  -15.50900 1.000 30.66638  ? 153 ILE B CG2 1 
ATOM   3426 C  CD1 . ILE B 1 153 ? -36.54200 19.86100  -18.78500 1.000 30.55041  ? 153 ILE B CD1 1 
ATOM   3427 N  N   . PHE B 1 154 ? -36.40000 16.63400  -13.67500 1.000 30.31543  ? 154 PHE B N   1 
ATOM   3428 C  CA  . PHE B 1 154 ? -36.99000 16.11700  -12.44600 1.000 32.08467  ? 154 PHE B CA  1 
ATOM   3429 C  C   . PHE B 1 154 ? -37.24800 17.26700  -11.48700 1.000 31.78782  ? 154 PHE B C   1 
ATOM   3430 O  O   . PHE B 1 154 ? -36.28900 17.79300  -10.89600 1.000 29.94380  ? 154 PHE B O   1 
ATOM   3431 C  CB  . PHE B 1 154 ? -36.08000 15.08900  -11.77400 1.000 28.99275  ? 154 PHE B CB  1 
ATOM   3432 C  CG  . PHE B 1 154 ? -35.82300 13.87100  -12.58400 1.000 31.19200  ? 154 PHE B CG  1 
ATOM   3433 C  CD1 . PHE B 1 154 ? -36.66400 12.77400  -12.49300 1.000 32.25002  ? 154 PHE B CD1 1 
ATOM   3434 C  CD2 . PHE B 1 154 ? -34.69800 13.79500  -13.40400 1.000 34.35021  ? 154 PHE B CD2 1 
ATOM   3435 C  CE1 . PHE B 1 154 ? -36.40900 11.62800  -13.23900 1.000 34.25335  ? 154 PHE B CE1 1 
ATOM   3436 C  CE2 . PHE B 1 154 ? -34.43500 12.64600  -14.15700 1.000 30.63943  ? 154 PHE B CE2 1 
ATOM   3437 C  CZ  . PHE B 1 154 ? -35.28200 11.56600  -14.06800 1.000 30.57867  ? 154 PHE B CZ  1 
ATOM   3438 N  N   . PRO B 1 155 ? -38.49500 17.68100  -11.29100 1.000 33.00038  ? 155 PRO B N   1 
ATOM   3439 C  CA  . PRO B 1 155 ? -38.80000 18.62900  -10.20600 1.000 33.79650  ? 155 PRO B CA  1 
ATOM   3440 C  C   . PRO B 1 155 ? -38.61500 17.97100  -8.84400  1.000 33.86700  ? 155 PRO B C   1 
ATOM   3441 O  O   . PRO B 1 155 ? -39.16300 16.89900  -8.58200  1.000 33.40715  ? 155 PRO B O   1 
ATOM   3442 C  CB  . PRO B 1 155 ? -40.27000 18.99800  -10.46000 1.000 32.97282  ? 155 PRO B CB  1 
ATOM   3443 C  CG  . PRO B 1 155 ? -40.84000 17.81100  -11.17500 1.000 31.42380  ? 155 PRO B CG  1 
ATOM   3444 C  CD  . PRO B 1 155 ? -39.69800 17.29800  -12.05500 1.000 30.36294  ? 155 PRO B CD  1 
ATOM   3445 N  N   . LEU B 1 156 ? -37.83900 18.62000  -7.97000  1.000 34.45737  ? 156 LEU B N   1 
ATOM   3446 C  CA  . LEU B 1 156 ? -37.64900 18.12600  -6.61100  1.000 34.73708  ? 156 LEU B CA  1 
ATOM   3447 C  C   . LEU B 1 156 ? -38.35900 18.96600  -5.56700  1.000 38.00620  ? 156 LEU B C   1 
ATOM   3448 O  O   . LEU B 1 156 ? -38.39700 18.56400  -4.39900  1.000 35.61897  ? 156 LEU B O   1 
ATOM   3449 C  CB  . LEU B 1 156 ? -36.16000 18.04100  -6.26000  1.000 32.46366  ? 156 LEU B CB  1 
ATOM   3450 C  CG  . LEU B 1 156 ? -35.45400 16.94900  -7.06100  1.000 38.24537  ? 156 LEU B CG  1 
ATOM   3451 C  CD1 . LEU B 1 156 ? -34.05900 16.82200  -6.56000  1.000 36.14338  ? 156 LEU B CD1 1 
ATOM   3452 C  CD2 . LEU B 1 156 ? -36.17700 15.63300  -6.92600  1.000 38.36117  ? 156 LEU B CD2 1 
ATOM   3453 N  N   . THR B 1 157 ? -38.88300 20.12600  -5.95400  1.000 35.72569  ? 157 THR B N   1 
ATOM   3454 C  CA  . THR B 1 157 ? -39.92100 20.85600  -5.25000  1.000 41.34132  ? 157 THR B CA  1 
ATOM   3455 C  C   . THR B 1 157 ? -41.08000 21.04800  -6.21900  1.000 40.34605  ? 157 THR B C   1 
ATOM   3456 O  O   . THR B 1 157 ? -40.98400 20.73000  -7.40700  1.000 39.42145  ? 157 THR B O   1 
ATOM   3457 C  CB  . THR B 1 157 ? -39.42700 22.22200  -4.75700  1.000 39.22364  ? 157 THR B CB  1 
ATOM   3458 O  OG1 . THR B 1 157 ? -39.00400 22.98400  -5.89700  1.000 42.87836  ? 157 THR B OG1 1 
ATOM   3459 C  CG2 . THR B 1 157 ? -38.27400 22.07000  -3.79700  1.000 36.47757  ? 157 THR B CG2 1 
ATOM   3460 N  N   . GLU B 1 158 ? -42.18200 21.58200  -5.71100  1.000 40.76997  ? 158 GLU B N   1 
ATOM   3461 C  CA  . GLU B 1 158 ? -43.27200 21.96900  -6.59500  1.000 42.46700  ? 158 GLU B CA  1 
ATOM   3462 C  C   . GLU B 1 158 ? -42.76900 22.94200  -7.65700  1.000 40.11157  ? 158 GLU B C   1 
ATOM   3463 O  O   . GLU B 1 158 ? -41.98600 23.85200  -7.37000  1.000 40.85067  ? 158 GLU B O   1 
ATOM   3464 C  CB  . GLU B 1 158 ? -44.40100 22.61200  -5.78800  1.000 40.31850  ? 158 GLU B CB  1 
ATOM   3465 C  CG  . GLU B 1 158 ? -43.96300 23.85800  -5.03800  1.000 46.38053  ? 158 GLU B CG  1 
ATOM   3466 C  CD  . GLU B 1 158 ? -45.06900 24.47500  -4.18300  1.000 58.12815  ? 158 GLU B CD  1 
ATOM   3467 O  OE1 . GLU B 1 158 ? -46.21200 23.94700  -4.18500  1.000 60.25167  ? 158 GLU B OE1 1 
ATOM   3468 O  OE2 . GLU B 1 158 ? -44.78400 25.48900  -3.49900  1.000 62.95913  ? 158 GLU B OE2 1 
ATOM   3469 N  N   . PHE B 1 159 ? -43.18700 22.71500  -8.89500  1.000 34.22579  ? 159 PHE B N   1 
ATOM   3470 C  CA  . PHE B 1 159 ? -43.11300 23.70700  -9.95700  1.000 39.56357  ? 159 PHE B CA  1 
ATOM   3471 C  C   . PHE B 1 159 ? -44.48500 24.36300  -10.04400 1.000 38.31956  ? 159 PHE B C   1 
ATOM   3472 O  O   . PHE B 1 159 ? -45.47900 23.68300  -10.31600 1.000 40.02046  ? 159 PHE B O   1 
ATOM   3473 C  CB  . PHE B 1 159 ? -42.75000 23.07800  -11.30600 1.000 35.86194  ? 159 PHE B CB  1 
ATOM   3474 C  CG  . PHE B 1 159 ? -41.28100 22.78300  -11.49200 1.000 36.85803  ? 159 PHE B CG  1 
ATOM   3475 C  CD1 . PHE B 1 159 ? -40.43500 22.61300  -10.41000 1.000 36.39147  ? 159 PHE B CD1 1 
ATOM   3476 C  CD2 . PHE B 1 159 ? -40.74900 22.69300  -12.78800 1.000 34.90563  ? 159 PHE B CD2 1 
ATOM   3477 C  CE1 . PHE B 1 159 ? -39.07600 22.33700  -10.60800 1.000 36.87688  ? 159 PHE B CE1 1 
ATOM   3478 C  CE2 . PHE B 1 159 ? -39.40200 22.41900  -12.99500 1.000 34.73883  ? 159 PHE B CE2 1 
ATOM   3479 C  CZ  . PHE B 1 159 ? -38.56400 22.25100  -11.90200 1.000 34.76468  ? 159 PHE B CZ  1 
ATOM   3480 N  N   . THR B 1 160 ? -44.54300 25.66800  -9.80800  1.000 39.43829  ? 160 THR B N   1 
ATOM   3481 C  CA  . THR B 1 160 ? -45.78200 26.42700  -9.86600  1.000 41.96648  ? 160 THR B CA  1 
ATOM   3482 C  C   . THR B 1 160 ? -45.60800 27.60600  -10.81400 1.000 47.38085  ? 160 THR B C   1 
ATOM   3483 O  O   . THR B 1 160 ? -44.49800 27.92200  -11.25800 1.000 42.41849  ? 160 THR B O   1 
ATOM   3484 C  CB  . THR B 1 160 ? -46.18000 26.95300  -8.48900  1.000 44.98565  ? 160 THR B CB  1 
ATOM   3485 O  OG1 . THR B 1 160 ? -45.38600 28.10900  -8.20200  1.000 43.68819  ? 160 THR B OG1 1 
ATOM   3486 C  CG2 . THR B 1 160 ? -45.95100 25.89100  -7.40900  1.000 42.49353  ? 160 THR B CG2 1 
ATOM   3487 N  N   . GLU B 1 161 ? -46.72700 28.26400  -11.12400 1.000 47.02598  ? 161 GLU B N   1 
ATOM   3488 C  CA  . GLU B 1 161 ? -46.66400 29.45200  -11.97300 1.000 53.13585  ? 161 GLU B CA  1 
ATOM   3489 C  C   . GLU B 1 161 ? -45.79000 30.52500  -11.34400 1.000 50.09667  ? 161 GLU B C   1 
ATOM   3490 O  O   . GLU B 1 161 ? -45.01300 31.19100  -12.03900 1.000 51.90835  ? 161 GLU B O   1 
ATOM   3491 C  CB  . GLU B 1 161 ? -48.06700 30.01000  -12.23300 1.000 52.25794  ? 161 GLU B CB  1 
ATOM   3492 C  CG  . GLU B 1 161 ? -48.05700 31.31700  -13.03800 1.000 64.08249  ? 161 GLU B CG  1 
ATOM   3493 C  CD  . GLU B 1 161 ? -49.43800 31.96400  -13.17000 1.000 74.50379  ? 161 GLU B CD  1 
ATOM   3494 O  OE1 . GLU B 1 161 ? -50.45900 31.27000  -12.95400 1.000 77.44892  ? 161 GLU B OE1 1 
ATOM   3495 O  OE2 . GLU B 1 161 ? -49.50100 33.17500  -13.48600 1.000 78.01638  ? 161 GLU B OE2 1 
ATOM   3496 N  N   . GLU B 1 162 ? -45.87400 30.67800  -10.02300 1.000 47.36090  ? 162 GLU B N   1 
ATOM   3497 C  CA  . GLU B 1 162 ? -45.16400 31.76300  -9.35900  1.000 48.81173  ? 162 GLU B CA  1 
ATOM   3498 C  C   . GLU B 1 162 ? -43.68300 31.45400  -9.18700  1.000 44.65818  ? 162 GLU B C   1 
ATOM   3499 O  O   . GLU B 1 162 ? -42.85600 32.37200  -9.25600  1.000 46.60584  ? 162 GLU B O   1 
ATOM   3500 C  CB  . GLU B 1 162 ? -45.80200 32.07000  -7.99900  1.000 52.60736  ? 162 GLU B CB  1 
ATOM   3501 C  CG  . GLU B 1 162 ? -47.33900 32.06000  -8.00500  1.000 62.67641  ? 162 GLU B CG  1 
ATOM   3502 C  CD  . GLU B 1 162 ? -47.91200 30.63700  -8.01500  1.000 66.05836  ? 162 GLU B CD  1 
ATOM   3503 O  OE1 . GLU B 1 162 ? -47.23100 29.72900  -7.48400  1.000 63.62875  ? 162 GLU B OE1 1 
ATOM   3504 O  OE2 . GLU B 1 162 ? -49.01800 30.42400  -8.56800  1.000 68.51530  ? 162 GLU B OE2 1 
ATOM   3505 N  N   . ASN B 1 163 ? -43.31300 30.19100  -8.95100  1.000 39.46635  ? 163 ASN B N   1 
ATOM   3506 C  CA  . ASN B 1 163 ? -41.92900 29.90800  -8.59800  1.000 41.73350  ? 163 ASN B CA  1 
ATOM   3507 C  C   . ASN B 1 163 ? -41.09000 29.46300  -9.78600  1.000 41.75683  ? 163 ASN B C   1 
ATOM   3508 O  O   . ASN B 1 163 ? -39.93400 29.08800  -9.60200  1.000 40.61259  ? 163 ASN B O   1 
ATOM   3509 C  CB  . ASN B 1 163 ? -41.84500 28.89300  -7.44000  1.000 40.06995  ? 163 ASN B CB  1 
ATOM   3510 C  CG  . ASN B 1 163 ? -42.01900 27.43600  -7.87500  1.000 41.67367  ? 163 ASN B CG  1 
ATOM   3511 O  OD1 . ASN B 1 163 ? -42.22600 27.11800  -9.04700  1.000 37.31195  ? 163 ASN B OD1 1 
ATOM   3512 N  ND2 . ASN B 1 163 ? -41.90700 26.53100  -6.89600  1.000 41.86735  ? 163 ASN B ND2 1 
ATOM   3513 N  N   . GLY B 1 164 ? -41.64000 29.49100  -10.99200 1.000 40.88817  ? 164 GLY B N   1 
ATOM   3514 C  CA  . GLY B 1 164 ? -40.82100 29.37800  -12.18000 1.000 37.38579  ? 164 GLY B CA  1 
ATOM   3515 C  C   . GLY B 1 164 ? -40.94000 28.08500  -12.95400 1.000 38.58533  ? 164 GLY B C   1 
ATOM   3516 O  O   . GLY B 1 164 ? -39.98300 27.68800  -13.61700 1.000 34.61276  ? 164 GLY B O   1 
ATOM   3517 N  N   . ALA B 1 165 ? -42.09600 27.42300  -12.89000 1.000 36.36085  ? 165 ALA B N   1 
ATOM   3518 C  CA  . ALA B 1 165 ? -42.30900 26.21800  -13.68100 1.000 34.64933  ? 165 ALA B CA  1 
ATOM   3519 C  C   . ALA B 1 165 ? -41.82900 26.41300  -15.12200 1.000 34.47217  ? 165 ALA B C   1 
ATOM   3520 O  O   . ALA B 1 165 ? -42.05700 27.46600  -15.72900 1.000 33.99874  ? 165 ALA B O   1 
ATOM   3521 C  CB  . ALA B 1 165 ? -43.78900 25.83900  -13.67100 1.000 35.35785  ? 165 ALA B CB  1 
ATOM   3522 N  N   . THR B 1 166 ? -41.15000 25.38800  -15.66000 1.000 32.44343  ? 166 THR B N   1 
ATOM   3523 C  CA  . THR B 1 166 ? -40.54800 25.45800  -16.99500 1.000 31.64102  ? 166 THR B CA  1 
ATOM   3524 C  C   . THR B 1 166 ? -41.56000 25.88900  -18.05400 1.000 30.79131  ? 166 THR B C   1 
ATOM   3525 O  O   . THR B 1 166 ? -42.68100 25.38100  -18.11200 1.000 29.99990  ? 166 THR B O   1 
ATOM   3526 C  CB  . THR B 1 166 ? -39.95500 24.09600  -17.38400 1.000 33.06525  ? 166 THR B CB  1 
ATOM   3527 O  OG1 . THR B 1 166 ? -39.24400 23.53000  -16.27300 1.000 29.52828  ? 166 THR B OG1 1 
ATOM   3528 C  CG2 . THR B 1 166 ? -38.99900 24.23700  -18.56600 1.000 31.00460  ? 166 THR B CG2 1 
ATOM   3529 N  N   . GLU B 1 167 ? -41.15700 26.83800  -18.88800 1.000 32.22438  ? 167 GLU B N   1 
ATOM   3530 C  CA  . GLU B 1 167 ? -41.97200 27.34200  -19.98600 1.000 31.62137  ? 167 GLU B CA  1 
ATOM   3531 C  C   . GLU B 1 167 ? -41.56400 26.61100  -21.25800 1.000 32.27286  ? 167 GLU B C   1 
ATOM   3532 O  O   . GLU B 1 167 ? -40.38100 26.59400  -21.61300 1.000 32.55574  ? 167 GLU B O   1 
ATOM   3533 C  CB  . GLU B 1 167 ? -41.78500 28.85600  -20.12200 1.000 32.07403  ? 167 GLU B CB  1 
ATOM   3534 C  CG  . GLU B 1 167 ? -42.08600 29.54700  -18.79800 1.000 38.03198  ? 167 GLU B CG  1 
ATOM   3535 C  CD  . GLU B 1 167 ? -41.56300 30.96100  -18.68200 1.000 45.43249  ? 167 GLU B CD  1 
ATOM   3536 O  OE1 . GLU B 1 167 ? -41.00200 31.51400  -19.66500 1.000 47.82013  ? 167 GLU B OE1 1 
ATOM   3537 O  OE2 . GLU B 1 167 ? -41.72300 31.52700  -17.57800 1.000 49.89958  ? 167 GLU B OE2 1 
ATOM   3538 N  N   . VAL B 1 168 ? -42.53400 25.99900  -21.92600 1.000 29.01880  ? 168 VAL B N   1 
ATOM   3539 C  CA  . VAL B 1 168 ? -42.29100 25.15300  -23.08300 1.000 31.03071  ? 168 VAL B CA  1 
ATOM   3540 C  C   . VAL B 1 168 ? -43.20300 25.63600  -24.20300 1.000 33.67480  ? 168 VAL B C   1 
ATOM   3541 O  O   . VAL B 1 168 ? -44.39500 25.87300  -23.97800 1.000 32.65251  ? 168 VAL B O   1 
ATOM   3542 C  CB  . VAL B 1 168 ? -42.55100 23.66600  -22.76800 1.000 33.30326  ? 168 VAL B CB  1 
ATOM   3543 C  CG1 . VAL B 1 168 ? -42.20900 22.78300  -23.96100 1.000 32.18168  ? 168 VAL B CG1 1 
ATOM   3544 C  CG2 . VAL B 1 168 ? -41.75800 23.21800  -21.53800 1.000 33.31716  ? 168 VAL B CG2 1 
ATOM   3545 N  N   . ILE B 1 169 ? -42.64500 25.81700  -25.39400 1.000 30.40512  ? 169 ILE B N   1 
ATOM   3546 C  CA  . ILE B 1 169 ? -43.42100 26.21300  -26.56300 1.000 32.30120  ? 169 ILE B CA  1 
ATOM   3547 C  C   . ILE B 1 169 ? -43.64300 24.96100  -27.39800 1.000 33.05147  ? 169 ILE B C   1 
ATOM   3548 O  O   . ILE B 1 169 ? -42.71600 24.47100  -28.04500 1.000 34.66210  ? 169 ILE B O   1 
ATOM   3549 C  CB  . ILE B 1 169 ? -42.72100 27.30700  -27.37600 1.000 32.34139  ? 169 ILE B CB  1 
ATOM   3550 C  CG1 . ILE B 1 169 ? -42.33300 28.48700  -26.47300 1.000 32.24059  ? 169 ILE B CG1 1 
ATOM   3551 C  CG2 . ILE B 1 169 ? -43.64700 27.77100  -28.51300 1.000 32.50173  ? 169 ILE B CG2 1 
ATOM   3552 C  CD1 . ILE B 1 169 ? -41.57900 29.59900  -27.21300 1.000 35.62078  ? 169 ILE B CD1 1 
ATOM   3553 N  N   . LEU B 1 170 ? -44.86900 24.45100  -27.39300 1.000 34.35888  ? 170 LEU B N   1 
ATOM   3554 C  CA  . LEU B 1 170 ? -45.17200 23.20300  -28.07900 1.000 35.97633  ? 170 LEU B CA  1 
ATOM   3555 C  C   . LEU B 1 170 ? -45.02100 23.37400  -29.59000 1.000 36.71994  ? 170 LEU B C   1 
ATOM   3556 O  O   . LEU B 1 170 ? -45.35600 24.42100  -30.15200 1.000 35.50084  ? 170 LEU B O   1 
ATOM   3557 C  CB  . LEU B 1 170 ? -46.59400 22.74500  -27.73200 1.000 38.58311  ? 170 LEU B CB  1 
ATOM   3558 C  CG  . LEU B 1 170 ? -46.99900 22.79400  -26.25100 1.000 35.86720  ? 170 LEU B CG  1 
ATOM   3559 C  CD1 . LEU B 1 170 ? -48.39200 22.22300  -26.03300 1.000 42.00467  ? 170 LEU B CD1 1 
ATOM   3560 C  CD2 . LEU B 1 170 ? -45.96700 22.07100  -25.37600 1.000 37.19672  ? 170 LEU B CD2 1 
ATOM   3561 N  N   . GLY B 1 171 ? -44.50300 22.33500  -30.24600 1.000 35.79067  ? 171 GLY B N   1 
ATOM   3562 C  CA  . GLY B 1 171 ? -44.28900 22.34300  -31.67500 1.000 37.44568  ? 171 GLY B CA  1 
ATOM   3563 C  C   . GLY B 1 171 ? -43.05800 23.08500  -32.13300 1.000 37.22517  ? 171 GLY B C   1 
ATOM   3564 O  O   . GLY B 1 171 ? -42.72800 23.03000  -33.32800 1.000 39.49811  ? 171 GLY B O   1 
ATOM   3565 N  N   . SER B 1 172 ? -42.34600 23.74900  -31.22400 1.000 33.73506  ? 172 SER B N   1 
ATOM   3566 C  CA  . SER B 1 172 ? -41.30400 24.69000  -31.61500 1.000 36.43149  ? 172 SER B CA  1 
ATOM   3567 C  C   . SER B 1 172 ? -40.04100 24.00700  -32.12100 1.000 34.60246  ? 172 SER B C   1 
ATOM   3568 O  O   . SER B 1 172 ? -39.16600 24.68900  -32.65400 1.000 33.68382  ? 172 SER B O   1 
ATOM   3569 C  CB  . SER B 1 172 ? -40.96700 25.62600  -30.44700 1.000 35.00416  ? 172 SER B CB  1 
ATOM   3570 O  OG  . SER B 1 172 ? -40.58200 24.91400  -29.28400 1.000 33.21858  ? 172 SER B OG  1 
ATOM   3571 N  N   . HIS B 1 173 ? -39.92500 22.69100  -31.97300 1.000 32.89994  ? 173 HIS B N   1 
ATOM   3572 C  CA  . HIS B 1 173 ? -38.82400 21.98100  -32.60000 1.000 33.68466  ? 173 HIS B CA  1 
ATOM   3573 C  C   . HIS B 1 173 ? -38.92000 22.01300  -34.12300 1.000 38.36306  ? 173 HIS B C   1 
ATOM   3574 O  O   . HIS B 1 173 ? -37.90900 21.78000  -34.79600 1.000 37.85901  ? 173 HIS B O   1 
ATOM   3575 C  CB  . HIS B 1 173 ? -38.76600 20.54000  -32.08200 1.000 33.47787  ? 173 HIS B CB  1 
ATOM   3576 C  CG  . HIS B 1 173 ? -40.04500 19.78100  -32.25900 1.000 35.26982  ? 173 HIS B CG  1 
ATOM   3577 N  ND1 . HIS B 1 173 ? -41.18300 20.05300  -31.52400 1.000 36.30675  ? 173 HIS B ND1 1 
ATOM   3578 C  CD2 . HIS B 1 173 ? -40.36300 18.74900  -33.07500 1.000 35.77432  ? 173 HIS B CD2 1 
ATOM   3579 C  CE1 . HIS B 1 173 ? -42.14900 19.22900  -31.89100 1.000 40.11744  ? 173 HIS B CE1 1 
ATOM   3580 N  NE2 . HIS B 1 173 ? -41.67700 18.42700  -32.83000 1.000 40.06122  ? 173 HIS B NE2 1 
ATOM   3581 N  N   . ARG B 1 174 ? -40.09400 22.33700  -34.68100 1.000 37.05396  ? 174 ARG B N   1 
ATOM   3582 C  CA  . ARG B 1 174 ? -40.23200 22.52200  -36.12600 1.000 38.67622  ? 174 ARG B CA  1 
ATOM   3583 C  C   . ARG B 1 174 ? -39.83200 23.92000  -36.60600 1.000 43.57819  ? 174 ARG B C   1 
ATOM   3584 O  O   . ARG B 1 174 ? -39.89100 24.17500  -37.81600 1.000 44.87559  ? 174 ARG B O   1 
ATOM   3585 C  CB  . ARG B 1 174 ? -41.67100 22.21900  -36.57500 1.000 39.41432  ? 174 ARG B CB  1 
ATOM   3586 C  CG  . ARG B 1 174 ? -42.06500 20.74000  -36.43900 1.000 41.24053  ? 174 ARG B CG  1 
ATOM   3587 C  CD  . ARG B 1 174 ? -43.44900 20.44000  -37.05300 1.000 43.23932  ? 174 ARG B CD  1 
ATOM   3588 N  NE  . ARG B 1 174 ? -44.51900 20.99600  -36.23100 1.000 49.60442  ? 174 ARG B NE  1 
ATOM   3589 C  CZ  . ARG B 1 174 ? -45.01800 20.40700  -35.15100 1.000 44.80421  ? 174 ARG B CZ  1 
ATOM   3590 N  NH1 . ARG B 1 174 ? -44.61100 19.20900  -34.76400 1.000 42.37313  ? 174 ARG B NH1 1 
ATOM   3591 N  NH2 . ARG B 1 174 ? -45.94200 21.04000  -34.43700 1.000 43.93103  ? 174 ARG B NH2 1 
ATOM   3592 N  N   . TRP B 1 175 ? -39.42000 24.82800  -35.72100 1.000 40.06659  ? 175 TRP B N   1 
ATOM   3593 C  CA  . TRP B 1 175 ? -39.06000 26.16900  -36.16500 1.000 42.19396  ? 175 TRP B CA  1 
ATOM   3594 C  C   . TRP B 1 175 ? -37.65900 26.18200  -36.74800 1.000 47.47942  ? 175 TRP B C   1 
ATOM   3595 O  O   . TRP B 1 175 ? -36.79600 25.38500  -36.37300 1.000 43.59087  ? 175 TRP B O   1 
ATOM   3596 C  CB  . TRP B 1 175 ? -39.10600 27.17800  -35.02400 1.000 42.48988  ? 175 TRP B CB  1 
ATOM   3597 C  CG  . TRP B 1 175 ? -40.44700 27.37900  -34.38900 1.000 45.42811  ? 175 TRP B CG  1 
ATOM   3598 C  CD1 . TRP B 1 175 ? -41.63900 26.81300  -34.75800 1.000 41.69012  ? 175 TRP B CD1 1 
ATOM   3599 C  CD2 . TRP B 1 175 ? -40.72800 28.21900  -33.26100 1.000 39.41761  ? 175 TRP B CD2 1 
ATOM   3600 N  NE1 . TRP B 1 175 ? -42.64500 27.25600  -33.92400 1.000 39.38621  ? 175 TRP B NE1 1 
ATOM   3601 C  CE2 . TRP B 1 175 ? -42.10900 28.11400  -32.99700 1.000 37.44869  ? 175 TRP B CE2 1 
ATOM   3602 C  CE3 . TRP B 1 175 ? -39.94100 29.05300  -32.45000 1.000 40.63325  ? 175 TRP B CE3 1 
ATOM   3603 C  CZ2 . TRP B 1 175 ? -42.72100 28.81400  -31.96000 1.000 36.53624  ? 175 TRP B CZ2 1 
ATOM   3604 C  CZ3 . TRP B 1 175 ? -40.54700 29.73700  -31.41600 1.000 38.32464  ? 175 TRP B CZ3 1 
ATOM   3605 C  CH2 . TRP B 1 175 ? -41.92400 29.61800  -31.18600 1.000 37.92132  ? 175 TRP B CH2 1 
ATOM   3606 N  N   . THR B 1 176 ? -37.42900 27.13000  -37.65100 1.000 51.99576  ? 176 THR B N   1 
ATOM   3607 C  CA  . THR B 1 176 ? -36.09900 27.30100  -38.22100 1.000 52.62349  ? 176 THR B CA  1 
ATOM   3608 C  C   . THR B 1 176 ? -35.12300 27.84000  -37.17700 1.000 52.76230  ? 176 THR B C   1 
ATOM   3609 O  O   . THR B 1 176 ? -34.08500 27.22300  -36.90300 1.000 52.94500  ? 176 THR B O   1 
ATOM   3610 C  CB  . THR B 1 176 ? -36.18900 28.21800  -39.43500 1.000 54.01115  ? 176 THR B CB  1 
ATOM   3611 O  OG1 . THR B 1 176 ? -36.78500 29.45900  -39.03900 1.000 64.14336  ? 176 THR B OG1 1 
ATOM   3612 C  CG2 . THR B 1 176 ? -37.07600 27.58100  -40.49100 1.000 56.61486  ? 176 THR B CG2 1 
ATOM   3613 N  N   . GLU B 1 177 ? -35.45500 28.96600  -36.55000 1.000 56.24388  ? 177 GLU B N   1 
ATOM   3614 C  CA  . GLU B 1 177 ? -34.61600 29.54500  -35.51000 1.000 56.14664  ? 177 GLU B CA  1 
ATOM   3615 C  C   . GLU B 1 177 ? -35.42500 29.68000  -34.22600 1.000 52.89706  ? 177 GLU B C   1 
ATOM   3616 O  O   . GLU B 1 177 ? -36.64000 29.45900  -34.20400 1.000 52.62614  ? 177 GLU B O   1 
ATOM   3617 C  CB  . GLU B 1 177 ? -34.05300 30.90900  -35.93900 1.000 59.70027  ? 177 GLU B CB  1 
ATOM   3618 C  CG  . GLU B 1 177 ? -35.12200 31.94300  -36.27300 1.000 63.48289  ? 177 GLU B CG  1 
ATOM   3619 C  CD  . GLU B 1 177 ? -34.54600 33.34400  -36.45100 1.000 78.30816  ? 177 GLU B CD  1 
ATOM   3620 O  OE1 . GLU B 1 177 ? -33.34000 33.45500  -36.77500 1.000 83.23139  ? 177 GLU B OE1 1 
ATOM   3621 O  OE2 . GLU B 1 177 ? -35.29500 34.33500  -36.26300 1.000 82.89566  ? 177 GLU B OE2 1 
ATOM   3622 N  N   . VAL B 1 178 ? -34.73200 30.02600  -33.13900 1.000 50.57560  ? 178 VAL B N   1 
ATOM   3623 C  CA  . VAL B 1 178 ? -35.43300 30.34600  -31.89900 1.000 48.08952  ? 178 VAL B CA  1 
ATOM   3624 C  C   . VAL B 1 178 ? -36.13800 31.68900  -32.03000 1.000 49.29862  ? 178 VAL B C   1 
ATOM   3625 O  O   . VAL B 1 178 ? -37.29400 31.84200  -31.61400 1.000 49.46230  ? 178 VAL B O   1 
ATOM   3626 C  CB  . VAL B 1 178 ? -34.46600 30.32600  -30.69400 1.000 46.20440  ? 178 VAL B CB  1 
ATOM   3627 C  CG1 . VAL B 1 178 ? -35.16600 30.80800  -29.42800 1.000 37.46674  ? 178 VAL B CG1 1 
ATOM   3628 C  CG2 . VAL B 1 178 ? -33.91800 28.93100  -30.46400 1.000 42.45264  ? 178 VAL B CG2 1 
ATOM   3629 N  N   . GLY B 1 179 ? -35.47100 32.67200  -32.63700 1.000 50.88357  ? 179 GLY B N   1 
ATOM   3630 C  CA  . GLY B 1 179 ? -36.00300 34.02000  -32.66200 1.000 53.26132  ? 179 GLY B CA  1 
ATOM   3631 C  C   . GLY B 1 179 ? -36.10500 34.61300  -31.26400 1.000 52.99941  ? 179 GLY B C   1 
ATOM   3632 O  O   . GLY B 1 179 ? -35.32000 34.30400  -30.35800 1.000 54.61251  ? 179 GLY B O   1 
ATOM   3633 N  N   . THR B 1 180 ? -37.09900 35.48000  -31.08900 1.000 52.76432  ? 180 THR B N   1 
ATOM   3634 C  CA  . THR B 1 180 ? -37.37500 36.14000  -29.81200 1.000 53.84800  ? 180 THR B CA  1 
ATOM   3635 C  C   . THR B 1 180 ? -38.84200 35.93200  -29.46100 1.000 50.85425  ? 180 THR B C   1 
ATOM   3636 O  O   . THR B 1 180 ? -39.64500 36.87000  -29.52300 1.000 51.40385  ? 180 THR B O   1 
ATOM   3637 C  CB  . THR B 1 180 ? -37.04300 37.63200  -29.88300 1.000 59.62819  ? 180 THR B CB  1 
ATOM   3638 O  OG1 . THR B 1 180 ? -37.81000 38.23800  -30.93300 1.000 60.65986  ? 180 THR B OG1 1 
ATOM   3639 C  CG2 . THR B 1 180 ? -35.55200 37.84600  -30.15600 1.000 56.99117  ? 180 THR B CG2 1 
ATOM   3640 N  N   . PRO B 1 181 ? -39.22900 34.70700  -29.10000 1.000 52.35246  ? 181 PRO B N   1 
ATOM   3641 C  CA  . PRO B 1 181 ? -40.64900 34.42800  -28.86900 1.000 49.35410  ? 181 PRO B CA  1 
ATOM   3642 C  C   . PRO B 1 181 ? -41.16600 35.15600  -27.64300 1.000 50.90420  ? 181 PRO B C   1 
ATOM   3643 O  O   . PRO B 1 181 ? -40.42100 35.48400  -26.71500 1.000 50.94221  ? 181 PRO B O   1 
ATOM   3644 C  CB  . PRO B 1 181 ? -40.69100 32.90500  -28.67100 1.000 44.01012  ? 181 PRO B CB  1 
ATOM   3645 C  CG  . PRO B 1 181 ? -39.32800 32.54000  -28.23200 1.000 43.60201  ? 181 PRO B CG  1 
ATOM   3646 C  CD  . PRO B 1 181 ? -38.38900 33.51500  -28.88300 1.000 48.98168  ? 181 PRO B CD  1 
ATOM   3647 N  N   . GLU B 1 182 ? -42.47000 35.39700  -27.64500 1.000 48.13524  ? 182 GLU B N   1 
ATOM   3648 C  CA  . GLU B 1 182 ? -43.10900 36.00900  -26.49200 1.000 54.49049  ? 182 GLU B CA  1 
ATOM   3649 C  C   . GLU B 1 182 ? -43.43300 34.94500  -25.44300 1.000 50.56652  ? 182 GLU B C   1 
ATOM   3650 O  O   . GLU B 1 182 ? -43.67100 33.77900  -25.76900 1.000 45.62899  ? 182 GLU B O   1 
ATOM   3651 C  CB  . GLU B 1 182 ? -44.37700 36.75600  -26.91600 1.000 54.44793  ? 182 GLU B CB  1 
ATOM   3652 C  CG  . GLU B 1 182 ? -44.87400 37.71400  -25.85400 1.000 65.21324  ? 182 GLU B CG  1 
ATOM   3653 C  CD  . GLU B 1 182 ? -43.77000 38.64500  -25.34800 1.000 73.87777  ? 182 GLU B CD  1 
ATOM   3654 O  OE1 . GLU B 1 182 ? -43.42000 39.60300  -26.08700 1.000 79.13584  ? 182 GLU B OE1 1 
ATOM   3655 O  OE2 . GLU B 1 182 ? -43.25100 38.40900  -24.22000 1.000 68.50193  ? 182 GLU B OE2 1 
ATOM   3656 N  N   . ARG B 1 183 ? -43.42500 35.35800  -24.17000 1.000 48.03617  ? 183 ARG B N   1 
ATOM   3657 C  CA  . ARG B 1 183 ? -43.66300 34.41100  -23.08300 1.000 49.68317  ? 183 ARG B CA  1 
ATOM   3658 C  C   . ARG B 1 183 ? -45.00700 33.71100  -23.23000 1.000 47.63082  ? 183 ARG B C   1 
ATOM   3659 O  O   . ARG B 1 183 ? -45.11500 32.50200  -22.99300 1.000 44.90310  ? 183 ARG B O   1 
ATOM   3660 C  CB  . ARG B 1 183 ? -43.59500 35.13100  -21.73800 1.000 52.54306  ? 183 ARG B CB  1 
ATOM   3661 C  CG  . ARG B 1 183 ? -42.23200 35.69000  -21.40800 1.000 52.81980  ? 183 ARG B CG  1 
ATOM   3662 C  CD  . ARG B 1 183 ? -41.25100 34.57300  -21.06300 1.000 49.70988  ? 183 ARG B CD  1 
ATOM   3663 N  NE  . ARG B 1 183 ? -39.89300 35.10000  -20.97900 1.000 52.95567  ? 183 ARG B NE  1 
ATOM   3664 C  CZ  . ARG B 1 183 ? -38.81500 34.38200  -20.69600 1.000 51.13293  ? 183 ARG B CZ  1 
ATOM   3665 N  NH1 . ARG B 1 183 ? -38.89800 33.09200  -20.41300 1.000 42.92101  ? 183 ARG B NH1 1 
ATOM   3666 N  NH2 . ARG B 1 183 ? -37.62000 34.97800  -20.69200 1.000 48.93020  ? 183 ARG B NH2 1 
ATOM   3667 N  N   . ASP B 1 184 ? -46.04100 34.44800  -23.63800 1.000 46.25173  ? 184 ASP B N   1 
ATOM   3668 C  CA  . ASP B 1 184 ? -47.38000 33.88100  -23.69800 1.000 45.94135  ? 184 ASP B CA  1 
ATOM   3669 C  C   . ASP B 1 184 ? -47.54400 32.84200  -24.80000 1.000 44.31770  ? 184 ASP B C   1 
ATOM   3670 O  O   . ASP B 1 184 ? -48.61000 32.22700  -24.87500 1.000 49.20486  ? 184 ASP B O   1 
ATOM   3671 C  CB  . ASP B 1 184 ? -48.41500 34.99400  -23.86600 1.000 50.98042  ? 184 ASP B CB  1 
ATOM   3672 C  CG  . ASP B 1 184 ? -48.07800 35.94100  -25.00700 1.000 59.58742  ? 184 ASP B CG  1 
ATOM   3673 O  OD1 . ASP B 1 184 ? -47.92200 35.46300  -26.16200 1.000 59.58061  ? 184 ASP B OD1 1 
ATOM   3674 O  OD2 . ASP B 1 184 ? -47.98000 37.16700  -24.75400 1.000 66.27626  ? 184 ASP B OD2 1 
ATOM   3675 N  N   . GLN B 1 185 ? -46.52900 32.62200  -25.64400 1.000 43.60498  ? 185 GLN B N   1 
ATOM   3676 C  CA  . GLN B 1 185 ? -46.54500 31.49000  -26.56400 1.000 42.53664  ? 185 GLN B CA  1 
ATOM   3677 C  C   . GLN B 1 185 ? -46.22400 30.17200  -25.87500 1.000 41.41944  ? 185 GLN B C   1 
ATOM   3678 O  O   . GLN B 1 185 ? -46.46800 29.11300  -26.45900 1.000 39.80409  ? 185 GLN B O   1 
ATOM   3679 C  CB  . GLN B 1 185 ? -45.53900 31.68800  -27.70300 1.000 44.89414  ? 185 GLN B CB  1 
ATOM   3680 C  CG  . GLN B 1 185 ? -45.75300 32.91200  -28.57100 1.000 48.16738  ? 185 GLN B CG  1 
ATOM   3681 C  CD  . GLN B 1 185 ? -44.63900 33.06900  -29.59500 1.000 49.00393  ? 185 GLN B CD  1 
ATOM   3682 O  OE1 . GLN B 1 185 ? -43.95600 34.09200  -29.63500 1.000 53.73514  ? 185 GLN B OE1 1 
ATOM   3683 N  NE2 . GLN B 1 185 ? -44.44800 32.05000  -30.42300 1.000 43.99552  ? 185 GLN B NE2 1 
ATOM   3684 N  N   . ALA B 1 186 ? -45.64800 30.21500  -24.67600 1.000 37.46559  ? 186 ALA B N   1 
ATOM   3685 C  CA  . ALA B 1 186 ? -45.26500 29.02200  -23.93800 1.000 36.12502  ? 186 ALA B CA  1 
ATOM   3686 C  C   . ALA B 1 186 ? -46.38100 28.57200  -22.99100 1.000 37.75636  ? 186 ALA B C   1 
ATOM   3687 O  O   . ALA B 1 186 ? -47.23800 29.35500  -22.57600 1.000 37.72418  ? 186 ALA B O   1 
ATOM   3688 C  CB  . ALA B 1 186 ? -43.97900 29.27200  -23.13800 1.000 34.01054  ? 186 ALA B CB  1 
ATOM   3689 N  N   . VAL B 1 187 ? -46.35800 27.28800  -22.65400 1.000 33.55420  ? 187 VAL B N   1 
ATOM   3690 C  CA  . VAL B 1 187 ? -47.18800 26.73700  -21.59500 1.000 35.49103  ? 187 VAL B CA  1 
ATOM   3691 C  C   . VAL B 1 187 ? -46.26500 26.29500  -20.46400 1.000 37.87570  ? 187 VAL B C   1 
ATOM   3692 O  O   . VAL B 1 187 ? -45.05000 26.10500  -20.65000 1.000 31.23534  ? 187 VAL B O   1 
ATOM   3693 C  CB  . VAL B 1 187 ? -48.06600 25.56100  -22.08100 1.000 39.06375  ? 187 VAL B CB  1 
ATOM   3694 C  CG1 . VAL B 1 187 ? -49.07800 26.04100  -23.10300 1.000 39.87520  ? 187 VAL B CG1 1 
ATOM   3695 C  CG2 . VAL B 1 187 ? -47.20300 24.45700  -22.67600 1.000 35.27518  ? 187 VAL B CG2 1 
ATOM   3696 N  N   . LEU B 1 188 ? -46.85800 26.09800  -19.28400 1.000 32.91748  ? 188 LEU B N   1 
ATOM   3697 C  CA  . LEU B 1 188 ? -46.10000 25.86800  -18.05800 1.000 36.49366  ? 188 LEU B CA  1 
ATOM   3698 C  C   . LEU B 1 188 ? -46.12400 24.39700  -17.68000 1.000 35.04373  ? 188 LEU B C   1 
ATOM   3699 O  O   . LEU B 1 188 ? -47.18800 23.77000  -17.64300 1.000 35.03644  ? 188 LEU B O   1 
ATOM   3700 C  CB  . LEU B 1 188 ? -46.64800 26.69600  -16.89400 1.000 35.69747  ? 188 LEU B CB  1 
ATOM   3701 C  CG  . LEU B 1 188 ? -46.58800 28.21400  -17.04300 1.000 38.30587  ? 188 LEU B CG  1 
ATOM   3702 C  CD1 . LEU B 1 188 ? -47.13500 28.89600  -15.77800 1.000 44.14710  ? 188 LEU B CD1 1 
ATOM   3703 C  CD2 . LEU B 1 188 ? -45.17600 28.65100  -17.33600 1.000 37.11181  ? 188 LEU B CD2 1 
ATOM   3704 N  N   . ALA B 1 189 ? -44.94700 23.86100  -17.37700 1.000 33.11485  ? 189 ALA B N   1 
ATOM   3705 C  CA  . ALA B 1 189 ? -44.82800 22.51900  -16.82400 1.000 33.81885  ? 189 ALA B CA  1 
ATOM   3706 C  C   . ALA B 1 189 ? -44.95500 22.56600  -15.29800 1.000 37.16328  ? 189 ALA B C   1 
ATOM   3707 O  O   . ALA B 1 189 ? -44.02300 22.25500  -14.55600 1.000 38.98612  ? 189 ALA B O   1 
ATOM   3708 C  CB  . ALA B 1 189 ? -43.51200 21.88800  -17.26400 1.000 30.95574  ? 189 ALA B CB  1 
ATOM   3709 N  N   . THR B 1 190 ? -46.13600 22.97700  -14.83300 1.000 36.86489  ? 190 THR B N   1 
ATOM   3710 C  CA  . THR B 1 190 ? -46.42700 22.93500  -13.40400 1.000 37.94607  ? 190 THR B CA  1 
ATOM   3711 C  C   . THR B 1 190 ? -46.51200 21.47900  -12.95500 1.000 38.55766  ? 190 THR B C   1 
ATOM   3712 O  O   . THR B 1 190 ? -47.14300 20.65800  -13.62500 1.000 37.89311  ? 190 THR B O   1 
ATOM   3713 C  CB  . THR B 1 190 ? -47.73400 23.67100  -13.09600 1.000 39.74415  ? 190 THR B CB  1 
ATOM   3714 O  OG1 . THR B 1 190 ? -48.77200 23.16600  -13.93900 1.000 35.21035  ? 190 THR B OG1 1 
ATOM   3715 C  CG2 . THR B 1 190 ? -47.59800 25.19700  -13.30900 1.000 39.60240  ? 190 THR B CG2 1 
ATOM   3716 N  N   . MET B 1 191 ? -45.87300 21.15600  -11.82700 1.000 36.07576  ? 191 MET B N   1 
ATOM   3717 C  CA  . MET B 1 191 ? -45.62400 19.76300  -11.46200 1.000 35.61274  ? 191 MET B CA  1 
ATOM   3718 C  C   . MET B 1 191 ? -45.45300 19.64700  -9.95800  1.000 38.03761  ? 191 MET B C   1 
ATOM   3719 O  O   . MET B 1 191 ? -45.10100 20.61100  -9.27900  1.000 38.18617  ? 191 MET B O   1 
ATOM   3720 C  CB  . MET B 1 191 ? -44.35900 19.21100  -12.13400 1.000 35.28912  ? 191 MET B CB  1 
ATOM   3721 C  CG  . MET B 1 191 ? -44.43700 18.99300  -13.62700 1.000 37.30613  ? 191 MET B CG  1 
ATOM   3722 S  SD  . MET B 1 191 ? -42.91400 18.25400  -14.30100 1.000 34.35621  ? 191 MET B SD  1 
ATOM   3723 C  CE  . MET B 1 191 ? -41.75000 19.63300  -14.13200 1.000 32.25611  ? 191 MET B CE  1 
ATOM   3724 N  N   . ASP B 1 192 ? -45.68400 18.43700  -9.44700  1.000 40.23927  ? 192 ASP B N   1 
ATOM   3725 C  CA  . ASP B 1 192 ? -45.34800 18.06100  -8.08900  1.000 37.90705  ? 192 ASP B CA  1 
ATOM   3726 C  C   . ASP B 1 192 ? -44.06600 17.23000  -8.08100  1.000 38.79565  ? 192 ASP B C   1 
ATOM   3727 O  O   . ASP B 1 192 ? -43.72900 16.59800  -9.08900  1.000 35.69845  ? 192 ASP B O   1 
ATOM   3728 C  CB  . ASP B 1 192 ? -46.48800 17.25900  -7.46400  1.000 42.59678  ? 192 ASP B CB  1 
ATOM   3729 C  CG  . ASP B 1 192 ? -47.74300 18.10200  -7.23800  1.000 52.87967  ? 192 ASP B CG  1 
ATOM   3730 O  OD1 . ASP B 1 192 ? -47.64500 19.16800  -6.58200  1.000 49.74470  ? 192 ASP B OD1 1 
ATOM   3731 O  OD2 . ASP B 1 192 ? -48.82400 17.69900  -7.72400  1.000 55.50818  ? 192 ASP B OD2 1 
ATOM   3732 N  N   . PRO B 1 193 ? -43.31600 17.23300  -6.97600  1.000 35.15394  ? 193 PRO B N   1 
ATOM   3733 C  CA  . PRO B 1 193 ? -42.15500 16.34500  -6.87700  1.000 36.59250  ? 193 PRO B CA  1 
ATOM   3734 C  C   . PRO B 1 193 ? -42.57000 14.91600  -7.18400  1.000 35.41298  ? 193 PRO B C   1 
ATOM   3735 O  O   . PRO B 1 193 ? -43.65000 14.47100  -6.80200  1.000 38.09631  ? 193 PRO B O   1 
ATOM   3736 C  CB  . PRO B 1 193 ? -41.70600 16.49800  -5.41800  1.000 39.08646  ? 193 PRO B CB  1 
ATOM   3737 C  CG  . PRO B 1 193 ? -42.26900 17.78700  -4.97100  1.000 40.50806  ? 193 PRO B CG  1 
ATOM   3738 C  CD  . PRO B 1 193 ? -43.54700 17.98000  -5.72500  1.000 42.46144  ? 193 PRO B CD  1 
ATOM   3739 N  N   . GLY B 1 194 ? -41.71500 14.20100  -7.89900  1.000 35.43175  ? 194 GLY B N   1 
ATOM   3740 C  CA  . GLY B 1 194 ? -42.05900 12.89500  -8.40000  1.000 37.64091  ? 194 GLY B CA  1 
ATOM   3741 C  C   . GLY B 1 194 ? -42.56000 12.89200  -9.83200  1.000 38.16222  ? 194 GLY B C   1 
ATOM   3742 O  O   . GLY B 1 194 ? -42.52000 11.84400  -10.48200 1.000 37.34646  ? 194 GLY B O   1 
ATOM   3743 N  N   . ASP B 1 195 ? -43.03600 14.02600  -10.33700 1.000 34.83737  ? 195 ASP B N   1 
ATOM   3744 C  CA  . ASP B 1 195 ? -43.34100 14.08700  -11.75200 1.000 32.47680  ? 195 ASP B CA  1 
ATOM   3745 C  C   . ASP B 1 195 ? -42.04100 14.17800  -12.55400 1.000 35.70881  ? 195 ASP B C   1 
ATOM   3746 O  O   . ASP B 1 195 ? -40.95700 14.43700  -12.01700 1.000 33.17759  ? 195 ASP B O   1 
ATOM   3747 C  CB  . ASP B 1 195 ? -44.22300 15.28600  -12.08400 1.000 35.57257  ? 195 ASP B CB  1 
ATOM   3748 C  CG  . ASP B 1 195 ? -45.59400 15.23700  -11.42200 1.000 37.95458  ? 195 ASP B CG  1 
ATOM   3749 O  OD1 . ASP B 1 195 ? -46.02500 14.17200  -10.94800 1.000 40.10155  ? 195 ASP B OD1 1 
ATOM   3750 O  OD2 . ASP B 1 195 ? -46.25400 16.29200  -11.40500 1.000 36.82559  ? 195 ASP B OD2 1 
ATOM   3751 N  N   . VAL B 1 196 ? -42.16000 13.97200  -13.86300 1.000 30.82515  ? 196 VAL B N   1 
ATOM   3752 C  CA  . VAL B 1 196 ? -41.02200 14.06300  -14.76500 1.000 33.08915  ? 196 VAL B CA  1 
ATOM   3753 C  C   . VAL B 1 196 ? -41.46900 14.76500  -16.03900 1.000 32.45508  ? 196 VAL B C   1 
ATOM   3754 O  O   . VAL B 1 196 ? -42.50900 14.42400  -16.61600 1.000 34.22552  ? 196 VAL B O   1 
ATOM   3755 C  CB  . VAL B 1 196 ? -40.41200 12.68400  -15.09700 1.000 33.89410  ? 196 VAL B CB  1 
ATOM   3756 C  CG1 . VAL B 1 196 ? -39.16000 12.87300  -15.92000 1.000 33.07976  ? 196 VAL B CG1 1 
ATOM   3757 C  CG2 . VAL B 1 196 ? -40.06300 11.91100  -13.81400 1.000 36.80349  ? 196 VAL B CG2 1 
ATOM   3758 N  N   . LEU B 1 197 ? -40.68200 15.74000  -16.47800 1.000 29.83173  ? 197 LEU B N   1 
ATOM   3759 C  CA  . LEU B 1 197 ? -40.90400 16.44000  -17.73600 1.000 30.23083  ? 197 LEU B CA  1 
ATOM   3760 C  C   . LEU B 1 197 ? -39.89500 15.96000  -18.77700 1.000 28.73813  ? 197 LEU B C   1 
ATOM   3761 O  O   . LEU B 1 197 ? -38.68600 15.94900  -18.51800 1.000 28.41301  ? 197 LEU B O   1 
ATOM   3762 C  CB  . LEU B 1 197 ? -40.79500 17.95000  -17.53200 1.000 27.04163  ? 197 LEU B CB  1 
ATOM   3763 C  CG  . LEU B 1 197 ? -40.65200 18.80000  -18.79200 1.000 28.00679  ? 197 LEU B CG  1 
ATOM   3764 C  CD1 . LEU B 1 197 ? -41.89500 18.69300  -19.66500 1.000 26.08347  ? 197 LEU B CD1 1 
ATOM   3765 C  CD2 . LEU B 1 197 ? -40.35300 20.25700  -18.42400 1.000 26.89579  ? 197 LEU B CD2 1 
ATOM   3766 N  N   . ILE B 1 198 ? -40.39300 15.54400  -19.93800 1.000 27.81692  ? 198 ILE B N   1 
ATOM   3767 C  CA  . ILE B 1 198 ? -39.58000 14.99300  -21.02200 1.000 27.46023  ? 198 ILE B CA  1 
ATOM   3768 C  C   . ILE B 1 198 ? -39.61900 15.98100  -22.17200 1.000 30.72468  ? 198 ILE B C   1 
ATOM   3769 O  O   . ILE B 1 198 ? -40.70600 16.31800  -22.65700 1.000 30.28366  ? 198 ILE B O   1 
ATOM   3770 C  CB  . ILE B 1 198 ? -40.10300 13.62300  -21.49200 1.000 32.43670  ? 198 ILE B CB  1 
ATOM   3771 C  CG1 . ILE B 1 198 ? -40.33900 12.66900  -20.31700 1.000 34.04191  ? 198 ILE B CG1 1 
ATOM   3772 C  CG2 . ILE B 1 198 ? -39.15000 12.98100  -22.50500 1.000 27.89668  ? 198 ILE B CG2 1 
ATOM   3773 C  CD1 . ILE B 1 198 ? -39.08500 12.22900  -19.62800 1.000 32.55073  ? 198 ILE B CD1 1 
ATOM   3774 N  N   . VAL B 1 199 ? -38.44700 16.42800  -22.63600 1.000 30.07133  ? 199 VAL B N   1 
ATOM   3775 C  CA  . VAL B 1 199 ? -38.36900 17.47600  -23.65500 1.000 30.92677  ? 199 VAL B CA  1 
ATOM   3776 C  C   . VAL B 1 199 ? -37.52900 16.99300  -24.83600 1.000 29.12374  ? 199 VAL B C   1 
ATOM   3777 O  O   . VAL B 1 199 ? -36.35500 16.64200  -24.67200 1.000 29.64359  ? 199 VAL B O   1 
ATOM   3778 C  CB  . VAL B 1 199 ? -37.80400 18.79000  -23.08700 1.000 31.30904  ? 199 VAL B CB  1 
ATOM   3779 C  CG1 . VAL B 1 199 ? -37.90900 19.89100  -24.14100 1.000 31.76982  ? 199 VAL B CG1 1 
ATOM   3780 C  CG2 . VAL B 1 199 ? -38.58700 19.18700  -21.82500 1.000 26.91669  ? 199 VAL B CG2 1 
ATOM   3781 N  N   . ARG B 1 200 ? -38.14200 16.96800  -26.01900 1.000 28.31681  ? 200 ARG B N   1 
ATOM   3782 C  CA  . ARG B 1 200 ? -37.48800 16.56500  -27.26100 1.000 27.45015  ? 200 ARG B CA  1 
ATOM   3783 C  C   . ARG B 1 200 ? -36.37200 17.54100  -27.62700 1.000 29.56023  ? 200 ARG B C   1 
ATOM   3784 O  O   . ARG B 1 200 ? -36.43000 18.73300  -27.30400 1.000 28.62419  ? 200 ARG B O   1 
ATOM   3785 C  CB  . ARG B 1 200 ? -38.53200 16.52300  -28.38500 1.000 30.12290  ? 200 ARG B CB  1 
ATOM   3786 C  CG  . ARG B 1 200 ? -38.04600 15.96500  -29.70200 1.000 31.66820  ? 200 ARG B CG  1 
ATOM   3787 C  CD  . ARG B 1 200 ? -38.87100 16.46000  -30.86100 1.000 34.64543  ? 200 ARG B CD  1 
ATOM   3788 N  NE  . ARG B 1 200 ? -38.52400 15.74800  -32.07900 1.000 38.57346  ? 200 ARG B NE  1 
ATOM   3789 C  CZ  . ARG B 1 200 ? -37.44000 15.98800  -32.80700 1.000 38.24744  ? 200 ARG B CZ  1 
ATOM   3790 N  NH1 . ARG B 1 200 ? -36.56800 16.93200  -32.46900 1.000 31.59199  ? 200 ARG B NH1 1 
ATOM   3791 N  NH2 . ARG B 1 200 ? -37.22600 15.26600  -33.90300 1.000 43.08458  ? 200 ARG B NH2 1 
ATOM   3792 N  N   . GLN B 1 201 ? -35.34900 17.02200  -28.30400 1.000 28.57324  ? 201 GLN B N   1 
ATOM   3793 C  CA  . GLN B 1 201 ? -34.34200 17.85700  -28.95700 1.000 30.04936  ? 201 GLN B CA  1 
ATOM   3794 C  C   . GLN B 1 201 ? -35.00700 18.95400  -29.78200 1.000 29.42694  ? 201 GLN B C   1 
ATOM   3795 O  O   . GLN B 1 201 ? -36.05000 18.73400  -30.40400 1.000 29.68459  ? 201 GLN B O   1 
ATOM   3796 C  CB  . GLN B 1 201 ? -33.44800 16.99500  -29.86000 1.000 26.50900  ? 201 GLN B CB  1 
ATOM   3797 C  CG  . GLN B 1 201 ? -32.33600 17.73500  -30.63300 1.000 31.30007  ? 201 GLN B CG  1 
ATOM   3798 C  CD  . GLN B 1 201 ? -31.49700 16.78500  -31.49700 1.000 33.19179  ? 201 GLN B CD  1 
ATOM   3799 O  OE1 . GLN B 1 201 ? -31.47100 15.58100  -31.23800 1.000 31.84710  ? 201 GLN B OE1 1 
ATOM   3800 N  NE2 . GLN B 1 201 ? -30.80400 17.32200  -32.51700 1.000 31.12520  ? 201 GLN B NE2 1 
ATOM   3801 N  N   . ARG B 1 202 ? -34.40400 20.14900  -29.76100 1.000 31.60386  ? 202 ARG B N   1 
ATOM   3802 C  CA  . ARG B 1 202 ? -34.80100 21.34100  -30.53000 1.000 30.37024  ? 202 ARG B CA  1 
ATOM   3803 C  C   . ARG B 1 202 ? -36.05800 22.03900  -30.04300 1.000 30.61102  ? 202 ARG B C   1 
ATOM   3804 O  O   . ARG B 1 202 ? -36.52300 22.95900  -30.71600 1.000 30.77704  ? 202 ARG B O   1 
ATOM   3805 C  CB  . ARG B 1 202 ? -35.04900 21.04900  -32.00900 1.000 32.21747  ? 202 ARG B CB  1 
ATOM   3806 C  CG  . ARG B 1 202 ? -33.83200 20.82400  -32.80300 1.000 36.43627  ? 202 ARG B CG  1 
ATOM   3807 C  CD  . ARG B 1 202 ? -34.24700 20.27900  -34.11700 1.000 38.93260  ? 202 ARG B CD  1 
ATOM   3808 N  NE  . ARG B 1 202 ? -35.06700 21.23000  -34.84400 1.000 40.73759  ? 202 ARG B NE  1 
ATOM   3809 C  CZ  . ARG B 1 202 ? -34.58700 22.12200  -35.70100 1.000 45.61765  ? 202 ARG B CZ  1 
ATOM   3810 N  NH1 . ARG B 1 202 ? -33.28600 22.25800  -35.90100 1.000 45.73962  ? 202 ARG B NH1 1 
ATOM   3811 N  NH2 . ARG B 1 202 ? -35.43600 22.88500  -36.38700 1.000 43.36723  ? 202 ARG B NH2 1 
ATOM   3812 N  N   . VAL B 1 203 ? -36.64800 21.62400  -28.93300 1.000 30.27562  ? 203 VAL B N   1 
ATOM   3813 C  CA  . VAL B 1 203 ? -37.83800 22.31200  -28.43900 1.000 31.55518  ? 203 VAL B CA  1 
ATOM   3814 C  C   . VAL B 1 203 ? -37.41400 23.58100  -27.70900 1.000 31.62715  ? 203 VAL B C   1 
ATOM   3815 O  O   . VAL B 1 203 ? -36.54500 23.54800  -26.82800 1.000 31.13468  ? 203 VAL B O   1 
ATOM   3816 C  CB  . VAL B 1 203 ? -38.66700 21.39300  -27.53000 1.000 31.29859  ? 203 VAL B CB  1 
ATOM   3817 C  CG1 . VAL B 1 203 ? -39.82500 22.16600  -26.92800 1.000 28.31247  ? 203 VAL B CG1 1 
ATOM   3818 C  CG2 . VAL B 1 203 ? -39.16800 20.17600  -28.31700 1.000 29.88845  ? 203 VAL B CG2 1 
ATOM   3819 N  N   . VAL B 1 204 ? -38.02500 24.70400  -28.08000 1.000 30.95813  ? 204 VAL B N   1 
ATOM   3820 C  CA  . VAL B 1 204 ? -37.72000 25.99700  -27.47500 1.000 30.22900  ? 204 VAL B CA  1 
ATOM   3821 C  C   . VAL B 1 204 ? -38.39000 26.06200  -26.10700 1.000 32.93631  ? 204 VAL B C   1 
ATOM   3822 O  O   . VAL B 1 204 ? -39.58100 25.75900  -25.97000 1.000 30.31711  ? 204 VAL B O   1 
ATOM   3823 C  CB  . VAL B 1 204 ? -38.19600 27.14500  -28.37900 1.000 30.08590  ? 204 VAL B CB  1 
ATOM   3824 C  CG1 . VAL B 1 204 ? -37.84400 28.50900  -27.74600 1.000 31.21067  ? 204 VAL B CG1 1 
ATOM   3825 C  CG2 . VAL B 1 204 ? -37.55900 27.01700  -29.77300 1.000 31.54019  ? 204 VAL B CG2 1 
ATOM   3826 N  N   . HIS B 1 205 ? -37.62600 26.45000  -25.09500 1.000 30.43686  ? 205 HIS B N   1 
ATOM   3827 C  CA  . HIS B 1 205 ? -38.10200 26.41200  -23.71700 1.000 32.56673  ? 205 HIS B CA  1 
ATOM   3828 C  C   . HIS B 1 205 ? -37.25600 27.37200  -22.89800 1.000 31.91987  ? 205 HIS B C   1 
ATOM   3829 O  O   . HIS B 1 205 ? -36.23200 27.87600  -23.36100 1.000 32.83462  ? 205 HIS B O   1 
ATOM   3830 C  CB  . HIS B 1 205 ? -38.00900 25.00100  -23.14100 1.000 29.70586  ? 205 HIS B CB  1 
ATOM   3831 C  CG  . HIS B 1 205 ? -36.61700 24.46100  -23.17400 1.000 31.81526  ? 205 HIS B CG  1 
ATOM   3832 N  ND1 . HIS B 1 205 ? -36.03600 23.99300  -24.33400 1.000 34.59664  ? 205 HIS B ND1 1 
ATOM   3833 C  CD2 . HIS B 1 205 ? -35.66600 24.38500  -22.21800 1.000 31.81230  ? 205 HIS B CD2 1 
ATOM   3834 C  CE1 . HIS B 1 205 ? -34.79800 23.61300  -24.08000 1.000 32.62823  ? 205 HIS B CE1 1 
ATOM   3835 N  NE2 . HIS B 1 205 ? -34.55900 23.82300  -22.80000 1.000 33.67187  ? 205 HIS B NE2 1 
ATOM   3836 N  N   . ALA B 1 206 ? -37.69400 27.60600  -21.65900 1.000 33.37400  ? 206 ALA B N   1 
ATOM   3837 C  CA  . ALA B 1 206 ? -36.96300 28.44900  -20.72400 1.000 31.65394  ? 206 ALA B CA  1 
ATOM   3838 C  C   . ALA B 1 206 ? -37.31200 28.04900  -19.29800 1.000 35.25693  ? 206 ALA B C   1 
ATOM   3839 O  O   . ALA B 1 206 ? -38.49400 27.87900  -18.97400 1.000 34.63842  ? 206 ALA B O   1 
ATOM   3840 C  CB  . ALA B 1 206 ? -37.29000 29.93300  -20.94600 1.000 36.08974  ? 206 ALA B CB  1 
ATOM   3841 N  N   . GLY B 1 207 ? -36.29800 27.92200  -18.44700 1.000 32.75778  ? 207 GLY B N   1 
ATOM   3842 C  CA  . GLY B 1 207 ? -36.56900 27.91700  -17.01900 1.000 34.84155  ? 207 GLY B CA  1 
ATOM   3843 C  C   . GLY B 1 207 ? -37.29200 29.19400  -16.61200 1.000 37.21056  ? 207 GLY B C   1 
ATOM   3844 O  O   . GLY B 1 207 ? -36.99300 30.28600  -17.10100 1.000 37.88357  ? 207 GLY B O   1 
ATOM   3845 N  N   . GLY B 1 208 ? -38.24900 29.06000  -15.70500 1.000 36.98604  ? 208 GLY B N   1 
ATOM   3846 C  CA  . GLY B 1 208 ? -39.05700 30.21000  -15.37400 1.000 35.24780  ? 208 GLY B CA  1 
ATOM   3847 C  C   . GLY B 1 208 ? -38.48300 31.12700  -14.32300 1.000 40.20392  ? 208 GLY B C   1 
ATOM   3848 O  O   . GLY B 1 208 ? -39.14500 32.10100  -13.96000 1.000 44.03127  ? 208 GLY B O   1 
ATOM   3849 N  N   . GLY B 1 209 ? -37.27000 30.86800  -13.83900 1.000 38.76855  ? 209 GLY B N   1 
ATOM   3850 C  CA  . GLY B 1 209 ? -36.75500 31.64800  -12.73200 1.000 41.86812  ? 209 GLY B CA  1 
ATOM   3851 C  C   . GLY B 1 209 ? -37.45600 31.26300  -11.43900 1.000 44.68461  ? 209 GLY B C   1 
ATOM   3852 O  O   . GLY B 1 209 ? -37.70600 30.07700  -11.17400 1.000 40.60170  ? 209 GLY B O   1 
ATOM   3853 N  N   . ASN B 1 210 ? -37.79100 32.28000  -10.63100 1.000 43.58803  ? 210 ASN B N   1 
ATOM   3854 C  CA  . ASN B 1 210 ? -38.55300 32.11300  -9.39100  1.000 45.11561  ? 210 ASN B CA  1 
ATOM   3855 C  C   . ASN B 1 210 ? -39.02300 33.46600  -8.86900  1.000 46.62374  ? 210 ASN B C   1 
ATOM   3856 O  O   . ASN B 1 210 ? -38.24300 34.19300  -8.24700  1.000 47.26141  ? 210 ASN B O   1 
ATOM   3857 C  CB  . ASN B 1 210 ? -37.70900 31.41200  -8.32300  1.000 46.42460  ? 210 ASN B CB  1 
ATOM   3858 C  CG  . ASN B 1 210 ? -38.52100 31.01900  -7.07300  1.000 43.97169  ? 210 ASN B CG  1 
ATOM   3859 O  OD1 . ASN B 1 210 ? -39.63200 31.50200  -6.85100  1.000 40.32645  ? 210 ASN B OD1 1 
ATOM   3860 N  ND2 . ASN B 1 210 ? -37.94900 30.13500  -6.25200  1.000 41.60653  ? 210 ASN B ND2 1 
ATOM   3861 N  N   . ARG B 1 211 ? -40.29400 33.80800  -9.08400  1.000 45.72980  ? 211 ARG B N   1 
ATOM   3862 C  CA  . ARG B 1 211 ? -40.78700 35.13400  -8.73900  1.000 49.97183  ? 211 ARG B CA  1 
ATOM   3863 C  C   . ARG B 1 211 ? -41.47600 35.18100  -7.38000  1.000 46.18769  ? 211 ARG B C   1 
ATOM   3864 O  O   . ARG B 1 211 ? -42.06100 36.21200  -7.03900  1.000 44.71225  ? 211 ARG B O   1 
ATOM   3865 C  CB  . ARG B 1 211 ? -41.73800 35.65800  -9.82800  1.000 49.70594  ? 211 ARG B CB  1 
ATOM   3866 C  CG  . ARG B 1 211 ? -41.15300 35.66400  -11.23900 1.000 54.72863  ? 211 ARG B CG  1 
ATOM   3867 C  CD  . ARG B 1 211 ? -39.72300 36.22000  -11.28200 1.000 57.74167  ? 211 ARG B CD  1 
ATOM   3868 N  NE  . ARG B 1 211 ? -39.59400 37.50000  -10.59300 1.000 64.87257  ? 211 ARG B NE  1 
ATOM   3869 C  CZ  . ARG B 1 211 ? -38.44200 38.11200  -10.34300 1.000 63.68583  ? 211 ARG B CZ  1 
ATOM   3870 N  NH1 . ARG B 1 211 ? -37.28600 37.60300  -10.74200 1.000 59.34111  ? 211 ARG B NH1 1 
ATOM   3871 N  NH2 . ARG B 1 211 ? -38.44900 39.26000  -9.66800  1.000 64.09953  ? 211 ARG B NH2 1 
ATOM   3872 N  N   . THR B 1 212 ? -41.42100 34.10300  -6.60100  1.000 43.95450  ? 212 THR B N   1 
ATOM   3873 C  CA  . THR B 1 212 ? -41.89000 34.16900  -5.22600  1.000 41.91172  ? 212 THR B CA  1 
ATOM   3874 C  C   . THR B 1 212 ? -40.94300 35.02400  -4.39000  1.000 45.55171  ? 212 THR B C   1 
ATOM   3875 O  O   . THR B 1 212 ? -39.76900 35.21700  -4.72200  1.000 48.16458  ? 212 THR B O   1 
ATOM   3876 C  CB  . THR B 1 212 ? -41.99900 32.77900  -4.59600  1.000 41.94144  ? 212 THR B CB  1 
ATOM   3877 O  OG1 . THR B 1 212 ? -40.69500 32.17900  -4.51500  1.000 38.71944  ? 212 THR B OG1 1 
ATOM   3878 C  CG2 . THR B 1 212 ? -42.94800 31.89700  -5.38200  1.000 39.09280  ? 212 THR B CG2 1 
ATOM   3879 N  N   . THR B 1 213 ? -41.47100 35.54500  -3.28800  1.000 45.29095  ? 213 THR B N   1 
ATOM   3880 C  CA  . THR B 1 213 ? -40.72600 36.45200  -2.42900  1.000 42.29658  ? 213 THR B CA  1 
ATOM   3881 C  C   . THR B 1 213 ? -40.64300 35.93500  -1.00100  1.000 42.49070  ? 213 THR B C   1 
ATOM   3882 O  O   . THR B 1 213 ? -40.22000 36.67700  -0.10600  1.000 41.60117  ? 213 THR B O   1 
ATOM   3883 C  CB  . THR B 1 213 ? -41.36000 37.84800  -2.44400  1.000 50.05866  ? 213 THR B CB  1 
ATOM   3884 O  OG1 . THR B 1 213 ? -42.72500 37.76300  -2.00400  1.000 52.87649  ? 213 THR B OG1 1 
ATOM   3885 C  CG2 . THR B 1 213 ? -41.31100 38.46100  -3.84700  1.000 46.48516  ? 213 THR B CG2 1 
ATOM   3886 N  N   . ALA B 1 214 ? -41.04100 34.68700  -0.76700  1.000 42.86020  ? 214 ALA B N   1 
ATOM   3887 C  CA  . ALA B 1 214 ? -41.10200 34.11400  0.57000   1.000 45.08580  ? 214 ALA B CA  1 
ATOM   3888 C  C   . ALA B 1 214 ? -39.83800 33.35300  0.94400   1.000 45.45066  ? 214 ALA B C   1 
ATOM   3889 O  O   . ALA B 1 214 ? -39.76200 32.81600  2.05900   1.000 47.38318  ? 214 ALA B O   1 
ATOM   3890 C  CB  . ALA B 1 214 ? -42.31500 33.17700  0.68400   1.000 45.24009  ? 214 ALA B CB  1 
ATOM   3891 N  N   . GLY B 1 215 ? -38.85700 33.28300  0.04300   1.000 37.88541  ? 215 GLY B N   1 
ATOM   3892 C  CA  . GLY B 1 215 ? -37.62000 32.58200  0.32000   1.000 38.29636  ? 215 GLY B CA  1 
ATOM   3893 C  C   . GLY B 1 215 ? -37.66700 31.07900  0.13500   1.000 42.63418  ? 215 GLY B C   1 
ATOM   3894 O  O   . GLY B 1 215 ? -36.95100 30.36100  0.83400   1.000 42.82745  ? 215 GLY B O   1 
ATOM   3895 N  N   . LYS B 1 216 ? -38.49200 30.57900  -0.78600  1.000 36.90663  ? 216 LYS B N   1 
ATOM   3896 C  CA  . LYS B 1 216 ? -38.60800 29.14700  -1.03700  1.000 41.01123  ? 216 LYS B CA  1 
ATOM   3897 C  C   . LYS B 1 216 ? -37.97600 28.83200  -2.38500  1.000 41.60632  ? 216 LYS B C   1 
ATOM   3898 O  O   . LYS B 1 216 ? -38.51400 29.25300  -3.42400  1.000 38.71907  ? 216 LYS B O   1 
ATOM   3899 C  CB  . LYS B 1 216 ? -40.07300 28.71600  -1.02500  1.000 44.49471  ? 216 LYS B CB  1 
ATOM   3900 C  CG  . LYS B 1 216 ? -40.80800 28.96500  0.29800   1.000 47.53105  ? 216 LYS B CG  1 
ATOM   3901 C  CD  . LYS B 1 216 ? -40.70400 27.74200  1.22300   1.000 56.07011  ? 216 LYS B CD  1 
ATOM   3902 C  CE  . LYS B 1 216 ? -41.04400 26.43600  0.46900   1.000 62.32136  ? 216 LYS B CE  1 
ATOM   3903 N  NZ  . LYS B 1 216 ? -42.38600 26.46600  -0.20800  1.000 64.91928  ? 216 LYS B NZ  1 
ATOM   3904 N  N   . PRO B 1 217 ? -36.85000 28.12500  -2.43300  1.000 39.10945  ? 217 PRO B N   1 
ATOM   3905 C  CA  . PRO B 1 217 ? -36.18900 27.87800  -3.72000  1.000 40.13573  ? 217 PRO B CA  1 
ATOM   3906 C  C   . PRO B 1 217 ? -36.79200 26.71500  -4.49300  1.000 39.62627  ? 217 PRO B C   1 
ATOM   3907 O  O   . PRO B 1 217 ? -37.22400 25.70500  -3.93300  1.000 43.76115  ? 217 PRO B O   1 
ATOM   3908 C  CB  . PRO B 1 217 ? -34.74200 27.57800  -3.31900  1.000 37.75755  ? 217 PRO B CB  1 
ATOM   3909 C  CG  . PRO B 1 217 ? -34.84100 27.05200  -1.93800  1.000 40.46581  ? 217 PRO B CG  1 
ATOM   3910 C  CD  . PRO B 1 217 ? -35.97800 27.80000  -1.29200  1.000 39.96123  ? 217 PRO B CD  1 
ATOM   3911 N  N   . ARG B 1 218 ? -36.81100 26.87100  -5.80900  1.000 38.01554  ? 218 ARG B N   1 
ATOM   3912 C  CA  . ARG B 1 218 ? -37.22500 25.79300  -6.69600  1.000 38.01209  ? 218 ARG B CA  1 
ATOM   3913 C  C   . ARG B 1 218 ? -36.02300 24.91700  -7.02100  1.000 36.14672  ? 218 ARG B C   1 
ATOM   3914 O  O   . ARG B 1 218 ? -34.98100 25.41500  -7.45000  1.000 37.03670  ? 218 ARG B O   1 
ATOM   3915 C  CB  . ARG B 1 218 ? -37.83900 26.35000  -7.97800  1.000 37.35352  ? 218 ARG B CB  1 
ATOM   3916 C  CG  . ARG B 1 218 ? -38.38100 25.28900  -8.90500  1.000 37.64779  ? 218 ARG B CG  1 
ATOM   3917 C  CD  . ARG B 1 218 ? -39.23500 25.91900  -9.99000  1.000 36.13341  ? 218 ARG B CD  1 
ATOM   3918 N  NE  . ARG B 1 218 ? -38.47700 26.92900  -10.71100 1.000 38.69039  ? 218 ARG B NE  1 
ATOM   3919 C  CZ  . ARG B 1 218 ? -37.62100 26.64400  -11.68100 1.000 40.18512  ? 218 ARG B CZ  1 
ATOM   3920 N  NH1 . ARG B 1 218 ? -37.40800 25.39200  -12.06400 1.000 36.33202  ? 218 ARG B NH1 1 
ATOM   3921 N  NH2 . ARG B 1 218 ? -36.96400 27.63400  -12.28200 1.000 37.38920  ? 218 ARG B NH2 1 
ATOM   3922 N  N   . ARG B 1 219 ? -36.17300 23.61600  -6.83300  1.000 34.79978  ? 219 ARG B N   1 
ATOM   3923 C  CA  . ARG B 1 219 ? -35.08700 22.66400  -7.01400  1.000 33.50729  ? 219 ARG B CA  1 
ATOM   3924 C  C   . ARG B 1 219 ? -35.38900 21.75800  -8.20000  1.000 35.50916  ? 219 ARG B C   1 
ATOM   3925 O  O   . ARG B 1 219 ? -36.49300 21.19900  -8.30000  1.000 32.29276  ? 219 ARG B O   1 
ATOM   3926 C  CB  . ARG B 1 219 ? -34.88600 21.83200  -5.74800  1.000 34.65335  ? 219 ARG B CB  1 
ATOM   3927 C  CG  . ARG B 1 219 ? -33.75800 20.86900  -5.84400  1.000 39.47249  ? 219 ARG B CG  1 
ATOM   3928 C  CD  . ARG B 1 219 ? -33.52800 20.11000  -4.54700  1.000 37.77165  ? 219 ARG B CD  1 
ATOM   3929 N  NE  . ARG B 1 219 ? -32.84100 20.89900  -3.53000  1.000 40.46180  ? 219 ARG B NE  1 
ATOM   3930 C  CZ  . ARG B 1 219 ? -32.42900 20.41300  -2.36500  1.000 40.79261  ? 219 ARG B CZ  1 
ATOM   3931 N  NH1 . ARG B 1 219 ? -32.60600 19.14000  -2.04600  1.000 32.00086  ? 219 ARG B NH1 1 
ATOM   3932 N  NH2 . ARG B 1 219 ? -31.82900 21.22500  -1.49600  1.000 44.36113  ? 219 ARG B NH2 1 
ATOM   3933 N  N   . VAL B 1 220 ? -34.40800 21.60400  -9.08900  1.000 31.85241  ? 220 VAL B N   1 
ATOM   3934 C  CA  . VAL B 1 220 ? -34.56400 20.79700  -10.29100 1.000 33.11542  ? 220 VAL B CA  1 
ATOM   3935 C  C   . VAL B 1 220 ? -33.29400 19.98600  -10.53300 1.000 30.03497  ? 220 VAL B C   1 
ATOM   3936 O  O   . VAL B 1 220 ? -32.17400 20.46700  -10.32500 1.000 28.79296  ? 220 VAL B O   1 
ATOM   3937 C  CB  . VAL B 1 220 ? -34.91800 21.67200  -11.51800 1.000 32.18861  ? 220 VAL B CB  1 
ATOM   3938 C  CG1 . VAL B 1 220 ? -33.74500 22.58000  -11.90700 1.000 31.18729  ? 220 VAL B CG1 1 
ATOM   3939 C  CG2 . VAL B 1 220 ? -35.31900 20.80100  -12.67600 1.000 33.26129  ? 220 VAL B CG2 1 
ATOM   3940 N  N   . VAL B 1 221 ? -33.47200 18.74000  -10.94600 1.000 29.17832  ? 221 VAL B N   1 
ATOM   3941 C  CA  . VAL B 1 221 ? -32.39400 17.92600  -11.48800 1.000 30.97175  ? 221 VAL B CA  1 
ATOM   3942 C  C   . VAL B 1 221 ? -32.65300 17.74500  -12.97700 1.000 29.98060  ? 221 VAL B C   1 
ATOM   3943 O  O   . VAL B 1 221 ? -33.76400 17.36600  -13.38300 1.000 29.24431  ? 221 VAL B O   1 
ATOM   3944 C  CB  . VAL B 1 221 ? -32.28000 16.57400  -10.76700 1.000 31.14333  ? 221 VAL B CB  1 
ATOM   3945 C  CG1 . VAL B 1 221 ? -31.50800 15.58200  -11.62400 1.000 27.84855  ? 221 VAL B CG1 1 
ATOM   3946 C  CG2 . VAL B 1 221 ? -31.59100 16.75900  -9.39300  1.000 30.32597  ? 221 VAL B CG2 1 
ATOM   3947 N  N   . LEU B 1 222 ? -31.65000 18.06000  -13.78800 1.000 25.38667  ? 222 LEU B N   1 
ATOM   3948 C  CA  . LEU B 1 222 ? -31.72400 17.88800  -15.23500 1.000 26.99249  ? 222 LEU B CA  1 
ATOM   3949 C  C   . LEU B 1 222 ? -30.84300 16.71400  -15.63800 1.000 28.08146  ? 222 LEU B C   1 
ATOM   3950 O  O   . LEU B 1 222 ? -29.68700 16.62300  -15.21000 1.000 26.74872  ? 222 LEU B O   1 
ATOM   3951 C  CB  . LEU B 1 222 ? -31.28800 19.15800  -15.97300 1.000 28.25721  ? 222 LEU B CB  1 
ATOM   3952 C  CG  . LEU B 1 222 ? -32.06400 20.42000  -15.54100 1.000 34.94086  ? 222 LEU B CG  1 
ATOM   3953 C  CD1 . LEU B 1 222 ? -31.18600 21.38300  -14.74400 1.000 32.86755  ? 222 LEU B CD1 1 
ATOM   3954 C  CD2 . LEU B 1 222 ? -32.66500 21.12000  -16.73300 1.000 37.55524  ? 222 LEU B CD2 1 
ATOM   3955 N  N   . ALA B 1 223 ? -31.40100 15.81100  -16.43500 1.000 28.01213  ? 223 ALA B N   1 
ATOM   3956 C  CA  . ALA B 1 223 ? -30.66200 14.68000  -16.97100 1.000 27.00565  ? 223 ALA B CA  1 
ATOM   3957 C  C   . ALA B 1 223 ? -30.72500 14.73800  -18.48800 1.000 29.22090  ? 223 ALA B C   1 
ATOM   3958 O  O   . ALA B 1 223 ? -31.81800 14.81200  -19.08300 1.000 28.44050  ? 223 ALA B O   1 
ATOM   3959 C  CB  . ALA B 1 223 ? -31.22300 13.36300  -16.45600 1.000 26.70186  ? 223 ALA B CB  1 
HETATM 3960 C  C   . F2Y B 1 224 ? -29.07300 13.29900  -21.04300 1.000 27.42873  ? 224 F2Y B C   1 
HETATM 3961 O  O   . F2Y B 1 224 ? -27.95000 12.84200  -20.70400 1.000 29.25086  ? 224 F2Y B O   1 
HETATM 3962 C  CA  . F2Y B 1 224 ? -29.50600 14.70800  -20.56400 1.000 27.98678  ? 224 F2Y B CA  1 
HETATM 3963 N  N   . F2Y B 1 224 ? -29.55600 14.71600  -19.11800 1.000 26.94790  ? 224 F2Y B N   1 
HETATM 3964 C  CB  . F2Y B 1 224 ? -28.55200 15.77600  -21.14600 1.000 29.97250  ? 224 F2Y B CB  1 
HETATM 3965 C  CG  . F2Y B 1 224 ? -28.92700 17.16600  -20.71900 1.000 33.89837  ? 224 F2Y B CG  1 
HETATM 3966 C  CD1 . F2Y B 1 224 ? -30.27300 17.46100  -20.47600 1.000 37.82866  ? 224 F2Y B CD1 1 
HETATM 3967 C  CE1 . F2Y B 1 224 ? -30.67900 18.74500  -20.08600 1.000 42.62740  ? 224 F2Y B CE1 1 
HETATM 3968 F  F1  . F2Y B 1 224 ? -31.99400 19.03600  -19.83200 0.610 35.37840  ? 224 F2Y B F1  1 
HETATM 3969 C  CD2 . F2Y B 1 224 ? -27.97800 18.17100  -20.56200 1.000 35.41424  ? 224 F2Y B CD2 1 
HETATM 3970 C  CE2 . F2Y B 1 224 ? -28.36900 19.45900  -20.16600 1.000 36.09492  ? 224 F2Y B CE2 1 
HETATM 3971 F  F2  . F2Y B 1 224 ? -27.43200 20.41600  -20.02300 0.770 42.19357  ? 224 F2Y B F2  1 
HETATM 3972 C  CZ  . F2Y B 1 224 ? -29.72100 19.76400  -19.92800 1.000 41.60428  ? 224 F2Y B CZ  1 
HETATM 3973 O  OH  . F2Y B 1 224 ? -30.08000 21.04300  -19.54300 1.000 43.85674  ? 224 F2Y B OH  1 
ATOM   3974 N  N   . PHE B 1 225 ? -29.95000 12.62600  -21.76700 1.000 27.14828  ? 225 PHE B N   1 
ATOM   3975 C  CA  . PHE B 1 225 ? -29.60600 11.38100  -22.41400 1.000 28.04580  ? 225 PHE B CA  1 
ATOM   3976 C  C   . PHE B 1 225 ? -29.28900 11.69600  -23.86200 1.000 27.52663  ? 225 PHE B C   1 
ATOM   3977 O  O   . PHE B 1 225 ? -30.05600 12.38600  -24.53700 1.000 29.05454  ? 225 PHE B O   1 
ATOM   3978 C  CB  . PHE B 1 225 ? -30.74800 10.36900  -22.29600 1.000 27.17473  ? 225 PHE B CB  1 
ATOM   3979 C  CG  . PHE B 1 225 ? -30.98900 9.91200   -20.88500 1.000 31.76842  ? 225 PHE B CG  1 
ATOM   3980 C  CD1 . PHE B 1 225 ? -30.26800 8.85000   -20.35800 1.000 30.61782  ? 225 PHE B CD1 1 
ATOM   3981 C  CD2 . PHE B 1 225 ? -31.90900 10.56300  -20.07800 1.000 32.61746  ? 225 PHE B CD2 1 
ATOM   3982 C  CE1 . PHE B 1 225 ? -30.46600 8.43300   -19.06700 1.000 34.41139  ? 225 PHE B CE1 1 
ATOM   3983 C  CE2 . PHE B 1 225 ? -32.12500 10.15400  -18.77600 1.000 31.44767  ? 225 PHE B CE2 1 
ATOM   3984 C  CZ  . PHE B 1 225 ? -31.40600 9.08800   -18.26200 1.000 34.36250  ? 225 PHE B CZ  1 
ATOM   3985 N  N   . ASN B 1 226 ? -28.14800 11.19400  -24.33000 1.000 27.41160  ? 226 ASN B N   1 
ATOM   3986 C  CA  . ASN B 1 226 ? -27.65700 11.44100  -25.67900 1.000 27.97321  ? 226 ASN B CA  1 
ATOM   3987 C  C   . ASN B 1 226 ? -27.32900 10.13000  -26.37000 1.000 26.70614  ? 226 ASN B C   1 
ATOM   3988 O  O   . ASN B 1 226 ? -26.97100 9.14600   -25.72500 1.000 24.40976  ? 226 ASN B O   1 
ATOM   3989 C  CB  . ASN B 1 226 ? -26.38600 12.26900  -25.69000 1.000 26.86117  ? 226 ASN B CB  1 
ATOM   3990 C  CG  . ASN B 1 226 ? -26.61800 13.71500  -25.30100 1.000 29.72020  ? 226 ASN B CG  1 
ATOM   3991 O  OD1 . ASN B 1 226 ? -27.75400 14.17900  -25.20800 1.000 31.83879  ? 226 ASN B OD1 1 
ATOM   3992 N  ND2 . ASN B 1 226 ? -25.52200 14.44300  -25.07800 1.000 28.23628  ? 226 ASN B ND2 1 
ATOM   3993 N  N   . SER B 1 227 ? -27.42300 10.14800  -27.69700 1.000 26.36351  ? 227 SER B N   1 
ATOM   3994 C  CA  . SER B 1 227 ? -26.76400 9.14300   -28.51900 1.000 28.11167  ? 227 SER B CA  1 
ATOM   3995 C  C   . SER B 1 227 ? -25.35300 8.85400   -28.01500 1.000 24.33779  ? 227 SER B C   1 
ATOM   3996 O  O   . SER B 1 227 ? -24.58400 9.76600   -27.69500 1.000 26.02956  ? 227 SER B O   1 
ATOM   3997 C  CB  . SER B 1 227 ? -26.69200 9.61400   -29.96900 1.000 25.47661  ? 227 SER B CB  1 
ATOM   3998 O  OG  . SER B 1 227 ? -25.85600 8.73500   -30.67200 1.000 25.41007  ? 227 SER B OG  1 
ATOM   3999 N  N   . VAL B 1 228 ? -25.00900 7.57100   -27.95300 1.000 22.86189  ? 228 VAL B N   1 
ATOM   4000 C  CA  . VAL B 1 228 ? -23.65400 7.17800   -27.59400 1.000 23.76154  ? 228 VAL B CA  1 
ATOM   4001 C  C   . VAL B 1 228 ? -22.62200 7.66000   -28.60400 1.000 24.26157  ? 228 VAL B C   1 
ATOM   4002 O  O   . VAL B 1 228 ? -21.42700 7.57300   -28.32600 1.000 24.77341  ? 228 VAL B O   1 
ATOM   4003 C  CB  . VAL B 1 228 ? -23.54800 5.64300   -27.41500 1.000 25.38428  ? 228 VAL B CB  1 
ATOM   4004 C  CG1 . VAL B 1 228 ? -24.50800 5.17500   -26.27500 1.000 23.36858  ? 228 VAL B CG1 1 
ATOM   4005 C  CG2 . VAL B 1 228 ? -23.86800 4.93200   -28.73000 1.000 22.38358  ? 228 VAL B CG2 1 
ATOM   4006 N  N   . GLN B 1 229 ? -23.05400 8.19900   -29.75600 1.000 24.36172  ? 229 GLN B N   1 
ATOM   4007 C  CA  . GLN B 1 229 ? -22.12200 8.91100   -30.63500 1.000 27.08800  ? 229 GLN B CA  1 
ATOM   4008 C  C   . GLN B 1 229 ? -21.56300 10.18400  -30.00300 1.000 24.37100  ? 229 GLN B C   1 
ATOM   4009 O  O   . GLN B 1 229 ? -20.47900 10.63400  -30.40000 1.000 23.83902  ? 229 GLN B O   1 
ATOM   4010 C  CB  . GLN B 1 229 ? -22.79000 9.29800   -31.95500 1.000 25.43000  ? 229 GLN B CB  1 
ATOM   4011 C  CG  . GLN B 1 229 ? -23.44200 8.17600   -32.71400 1.000 26.01842  ? 229 GLN B CG  1 
ATOM   4012 C  CD  . GLN B 1 229 ? -24.20400 8.71600   -33.91700 1.000 28.01600  ? 229 GLN B CD  1 
ATOM   4013 O  OE1 . GLN B 1 229 ? -23.61500 9.32100   -34.80900 1.000 26.21018  ? 229 GLN B OE1 1 
ATOM   4014 N  NE2 . GLN B 1 229 ? -25.51700 8.55500   -33.91600 1.000 27.84305  ? 229 GLN B NE2 1 
ATOM   4015 N  N   . LEU B 1 230 ? -22.27100 10.78100  -29.04700 1.000 24.77042  ? 230 LEU B N   1 
ATOM   4016 C  CA  . LEU B 1 230 ? -21.86000 12.04400  -28.44300 1.000 24.45986  ? 230 LEU B CA  1 
ATOM   4017 C  C   . LEU B 1 230 ? -21.14600 11.80500  -27.11400 1.000 27.42700  ? 230 LEU B C   1 
ATOM   4018 O  O   . LEU B 1 230 ? -21.64100 11.06700  -26.24200 1.000 27.61449  ? 230 LEU B O   1 
ATOM   4019 C  CB  . LEU B 1 230 ? -23.05300 12.97100  -28.23500 1.000 25.75613  ? 230 LEU B CB  1 
ATOM   4020 C  CG  . LEU B 1 230 ? -23.87500 13.30200  -29.48300 1.000 25.79436  ? 230 LEU B CG  1 
ATOM   4021 C  CD1 . LEU B 1 230 ? -25.02300 14.20200  -29.07900 1.000 26.65640  ? 230 LEU B CD1 1 
ATOM   4022 C  CD2 . LEU B 1 230 ? -23.01100 13.96700  -30.55500 1.000 27.42042  ? 230 LEU B CD2 1 
ATOM   4023 N  N   . THR B 1 231 ? -19.98400 12.41900  -26.98200 1.000 22.43667  ? 231 THR B N   1 
ATOM   4024 C  CA  . THR B 1 231 ? -19.18300 12.33100  -25.77200 1.000 24.02573  ? 231 THR B CA  1 
ATOM   4025 C  C   . THR B 1 231 ? -19.97300 12.76800  -24.54100 1.000 23.48573  ? 231 THR B C   1 
ATOM   4026 O  O   . THR B 1 231 ? -20.52600 13.87700  -24.52900 1.000 23.50666  ? 231 THR B O   1 
ATOM   4027 C  CB  . THR B 1 231 ? -17.96300 13.22900  -25.93200 1.000 25.47159  ? 231 THR B CB  1 
ATOM   4028 O  OG1 . THR B 1 231 ? -17.25100 12.82900  -27.12100 1.000 26.31791  ? 231 THR B OG1 1 
ATOM   4029 C  CG2 . THR B 1 231 ? -17.03900 13.13300  -24.68200 1.000 20.91717  ? 231 THR B CG2 1 
ATOM   4030 N  N   . PRO B 1 232 ? -20.02600 11.95800  -23.48600 1.000 24.21727  ? 232 PRO B N   1 
ATOM   4031 C  CA  . PRO B 1 232 ? -20.66600 12.42900  -22.24600 1.000 24.35030  ? 232 PRO B CA  1 
ATOM   4032 C  C   . PRO B 1 232 ? -19.95500 13.66500  -21.70500 1.000 25.05357  ? 232 PRO B C   1 
ATOM   4033 O  O   . PRO B 1 232 ? -18.72900 13.73400  -21.67900 1.000 24.70818  ? 232 PRO B O   1 
ATOM   4034 C  CB  . PRO B 1 232 ? -20.55100 11.22700  -21.29500 1.000 27.40400  ? 232 PRO B CB  1 
ATOM   4035 C  CG  . PRO B 1 232 ? -20.41800 10.00200  -22.24900 1.000 24.31538  ? 232 PRO B CG  1 
ATOM   4036 C  CD  . PRO B 1 232 ? -19.57400 10.55300  -23.39700 1.000 20.30014  ? 232 PRO B CD  1 
ATOM   4037 N  N   . PHE B 1 233 ? -20.74600 14.67200  -21.33100 1.000 23.41687  ? 233 PHE B N   1 
ATOM   4038 C  CA  . PHE B 1 233 ? -20.19500 15.87500  -20.70900 1.000 27.73470  ? 233 PHE B CA  1 
ATOM   4039 C  C   . PHE B 1 233 ? -19.51700 15.53000  -19.38600 1.000 30.39540  ? 233 PHE B C   1 
ATOM   4040 O  O   . PHE B 1 233 ? -18.40500 15.98800  -19.09300 1.000 27.99550  ? 233 PHE B O   1 
ATOM   4041 C  CB  . PHE B 1 233 ? -21.33200 16.88600  -20.50700 1.000 25.38831  ? 233 PHE B CB  1 
ATOM   4042 C  CG  . PHE B 1 233 ? -20.96400 18.11800  -19.70100 1.000 30.62074  ? 233 PHE B CG  1 
ATOM   4043 C  CD1 . PHE B 1 233 ? -20.21300 19.14100  -20.26000 1.000 29.15173  ? 233 PHE B CD1 1 
ATOM   4044 C  CD2 . PHE B 1 233 ? -21.44200 18.28200  -18.39800 1.000 29.41167  ? 233 PHE B CD2 1 
ATOM   4045 C  CE1 . PHE B 1 233 ? -19.91400 20.30400  -19.51400 1.000 31.00498  ? 233 PHE B CE1 1 
ATOM   4046 C  CE2 . PHE B 1 233 ? -21.14500 19.41600  -17.65300 1.000 31.97356  ? 233 PHE B CE2 1 
ATOM   4047 C  CZ  . PHE B 1 233 ? -20.38000 20.43700  -18.21200 1.000 32.60875  ? 233 PHE B CZ  1 
ATOM   4048 N  N   . GLU B 1 234 ? -20.18200 14.71400  -18.58100 1.000 28.35657  ? 234 GLU B N   1 
ATOM   4049 C  CA  . GLU B 1 234 ? -19.64900 14.19300  -17.33200 1.000 28.23783  ? 234 GLU B CA  1 
ATOM   4050 C  C   . GLU B 1 234 ? -19.11300 12.79500  -17.60700 1.000 28.28623  ? 234 GLU B C   1 
ATOM   4051 O  O   . GLU B 1 234 ? -19.81800 11.96200  -18.19000 1.000 29.66626  ? 234 GLU B O   1 
ATOM   4052 C  CB  . GLU B 1 234 ? -20.74500 14.15900  -16.24700 1.000 25.88677  ? 234 GLU B CB  1 
ATOM   4053 C  CG  . GLU B 1 234 ? -21.12100 15.55600  -15.72800 1.000 29.54216  ? 234 GLU B CG  1 
ATOM   4054 C  CD  . GLU B 1 234 ? -22.43300 15.62100  -14.89800 1.000 34.02169  ? 234 GLU B CD  1 
ATOM   4055 O  OE1 . GLU B 1 234 ? -23.19800 14.61200  -14.80100 1.000 30.62478  ? 234 GLU B OE1 1 
ATOM   4056 O  OE2 . GLU B 1 234 ? -22.69000 16.71700  -14.34100 1.000 35.21611  ? 234 GLU B OE2 1 
ATOM   4057 N  N   . THR B 1 235 ? -17.87500 12.53300  -17.21900 1.000 23.06294  ? 235 THR B N   1 
ATOM   4058 C  CA  . THR B 1 235 ? -17.35200 11.19000  -17.36800 1.000 28.50822  ? 235 THR B CA  1 
ATOM   4059 C  C   . THR B 1 235 ? -17.37000 10.50500  -16.00600 1.000 32.34199  ? 235 THR B C   1 
ATOM   4060 O  O   . THR B 1 235 ? -16.95700 11.09200  -14.99600 1.000 29.43426  ? 235 THR B O   1 
ATOM   4061 C  CB  . THR B 1 235 ? -15.95300 11.18300  -17.98000 1.000 27.90473  ? 235 THR B CB  1 
ATOM   4062 O  OG1 . THR B 1 235 ? -15.44700 9.85000   -17.94100 1.000 29.80972  ? 235 THR B OG1 1 
ATOM   4063 C  CG2 . THR B 1 235 ? -15.00900 12.14800  -17.24100 1.000 28.45909  ? 235 THR B CG2 1 
ATOM   4064 N  N   . TYR B 1 236 ? -17.89200 9.28000   -15.97500 1.000 25.74419  ? 236 TYR B N   1 
ATOM   4065 C  CA  . TYR B 1 236 ? -18.01000 8.53800   -14.73000 1.000 31.01825  ? 236 TYR B CA  1 
ATOM   4066 C  C   . TYR B 1 236 ? -16.87900 7.53000   -14.54900 1.000 30.54143  ? 236 TYR B C   1 
ATOM   4067 O  O   . TYR B 1 236 ? -16.97900 6.65100   -13.69500 1.000 29.96342  ? 236 TYR B O   1 
ATOM   4068 C  CB  . TYR B 1 236 ? -19.38800 7.86400   -14.65400 1.000 25.54262  ? 236 TYR B CB  1 
ATOM   4069 C  CG  . TYR B 1 236 ? -20.47700 8.92800   -14.57400 1.000 27.50757  ? 236 TYR B CG  1 
ATOM   4070 C  CD1 . TYR B 1 236 ? -20.77200 9.53700   -13.35400 1.000 33.42205  ? 236 TYR B CD1 1 
ATOM   4071 C  CD2 . TYR B 1 236 ? -21.14000 9.34600   -15.72600 1.000 32.00399  ? 236 TYR B CD2 1 
ATOM   4072 C  CE1 . TYR B 1 236 ? -21.73900 10.51400  -13.29900 1.000 34.53428  ? 236 TYR B CE1 1 
ATOM   4073 C  CE2 . TYR B 1 236 ? -22.09200 10.33000  -15.63900 1.000 30.17541  ? 236 TYR B CE2 1 
ATOM   4074 C  CZ  . TYR B 1 236 ? -22.41700 10.93300  -14.43400 1.000 34.98153  ? 236 TYR B CZ  1 
ATOM   4075 O  OH  . TYR B 1 236 ? -23.36100 11.90000  -14.38400 1.000 43.15531  ? 236 TYR B OH  1 
ATOM   4076 N  N   . ARG B 1 237 ? -15.77700 7.69000   -15.29400 1.000 28.61819  ? 237 ARG B N   1 
ATOM   4077 C  CA  . ARG B 1 237 ? -14.67400 6.72800   -15.30000 1.000 31.71986  ? 237 ARG B CA  1 
ATOM   4078 C  C   . ARG B 1 237 ? -13.86900 6.69800   -14.00200 1.000 30.83268  ? 237 ARG B C   1 
ATOM   4079 O  O   . ARG B 1 237 ? -13.09100 5.75900   -13.80500 1.000 32.30763  ? 237 ARG B O   1 
ATOM   4080 C  CB  . ARG B 1 237 ? -13.72800 7.03000   -16.46800 1.000 32.58158  ? 237 ARG B CB  1 
ATOM   4081 C  CG  . ARG B 1 237 ? -12.95800 8.35000   -16.31500 1.000 30.93718  ? 237 ARG B CG  1 
ATOM   4082 C  CD  . ARG B 1 237 ? -12.46500 8.83100   -17.67800 1.000 35.50245  ? 237 ARG B CD  1 
ATOM   4083 N  NE  . ARG B 1 237 ? -11.20000 8.20900   -18.04300 1.000 37.65190  ? 237 ARG B NE  1 
ATOM   4084 C  CZ  . ARG B 1 237 ? -10.63900 8.29300   -19.24300 1.000 37.43218  ? 237 ARG B CZ  1 
ATOM   4085 N  NH1 . ARG B 1 237 ? -11.22100 8.95200   -20.23800 1.000 33.15358  ? 237 ARG B NH1 1 
ATOM   4086 N  NH2 . ARG B 1 237 ? -9.47000  7.69600   -19.45000 1.000 35.14283  ? 237 ARG B NH2 1 
ATOM   4087 N  N   . THR B 1 238 ? -14.01600 7.68000   -13.12100 1.000 26.87227  ? 238 THR B N   1 
ATOM   4088 C  CA  . THR B 1 238 ? -13.30100 7.64400   -11.85500 1.000 30.62638  ? 238 THR B CA  1 
ATOM   4089 C  C   . THR B 1 238 ? -14.11600 6.99300   -10.74400 1.000 34.50729  ? 238 THR B C   1 
ATOM   4090 O  O   . THR B 1 238 ? -13.65900 6.96800   -9.59900  1.000 33.69943  ? 238 THR B O   1 
ATOM   4091 C  CB  . THR B 1 238 ? -12.87500 9.05700   -11.41700 1.000 33.54754  ? 238 THR B CB  1 
ATOM   4092 O  OG1 . THR B 1 238 ? -14.03400 9.85100   -11.14100 1.000 32.04757  ? 238 THR B OG1 1 
ATOM   4093 C  CG2 . THR B 1 238 ? -12.03400 9.76400   -12.52600 1.000 31.82593  ? 238 THR B CG2 1 
ATOM   4094 N  N   . MET B 1 239 ? -15.30700 6.49100   -11.04600 1.000 33.29603  ? 239 MET B N   1 
ATOM   4095 C  CA  . MET B 1 239 ? -16.06300 5.72800   -10.06000 1.000 33.70637  ? 239 MET B CA  1 
ATOM   4096 C  C   . MET B 1 239 ? -15.24800 4.52700   -9.58700  1.000 34.06504  ? 239 MET B C   1 
ATOM   4097 O  O   . MET B 1 239 ? -14.67700 3.80400   -10.41700 1.000 36.64696  ? 239 MET B O   1 
ATOM   4098 C  CB  . MET B 1 239 ? -17.39300 5.25000   -10.64400 1.000 33.61576  ? 239 MET B CB  1 
ATOM   4099 C  CG  . MET B 1 239 ? -18.43700 6.33300   -10.76400 1.000 35.83010  ? 239 MET B CG  1 
ATOM   4100 S  SD  . MET B 1 239 ? -20.01100 5.72700   -11.43100 1.000 45.66861  ? 239 MET B SD  1 
ATOM   4101 C  CE  . MET B 1 239 ? -20.36600 4.40700   -10.27500 1.000 35.37956  ? 239 MET B CE  1 
ATOM   4102 N  N   . PRO B 1 240 ? -15.16000 4.28500   -8.28300  1.000 37.55709  ? 240 PRO B N   1 
ATOM   4103 C  CA  . PRO B 1 240 ? -14.50400 3.06100   -7.80400  1.000 39.97237  ? 240 PRO B CA  1 
ATOM   4104 C  C   . PRO B 1 240 ? -15.17800 1.81100   -8.35600  1.000 38.11510  ? 240 PRO B C   1 
ATOM   4105 O  O   . PRO B 1 240 ? -16.39100 1.76800   -8.56600  1.000 38.45304  ? 240 PRO B O   1 
ATOM   4106 C  CB  . PRO B 1 240 ? -14.65300 3.15100   -6.28100  1.000 39.33151  ? 240 PRO B CB  1 
ATOM   4107 C  CG  . PRO B 1 240 ? -14.71900 4.62900   -6.01200  1.000 42.92924  ? 240 PRO B CG  1 
ATOM   4108 C  CD  . PRO B 1 240 ? -15.50100 5.20300   -7.18300  1.000 37.59308  ? 240 PRO B CD  1 
ATOM   4109 N  N   . ARG B 1 241 ? -14.36000 0.78700   -8.59800  1.000 40.57038  ? 241 ARG B N   1 
ATOM   4110 C  CA  . ARG B 1 241 ? -14.86400 -0.47900  -9.11900  1.000 38.19422  ? 241 ARG B CA  1 
ATOM   4111 C  C   . ARG B 1 241 ? -15.99100 -1.02800  -8.25600  1.000 38.12491  ? 241 ARG B C   1 
ATOM   4112 O  O   . ARG B 1 241 ? -16.99900 -1.53500  -8.77500  1.000 36.92703  ? 241 ARG B O   1 
ATOM   4113 C  CB  . ARG B 1 241 ? -13.71800 -1.48700  -9.21000  1.000 36.32723  ? 241 ARG B CB  1 
ATOM   4114 C  CG  . ARG B 1 241 ? -14.07200 -2.79100  -9.89400  1.000 42.36417  ? 241 ARG B CG  1 
ATOM   4115 C  CD  . ARG B 1 241 ? -12.83900 -3.65400  -10.09400 1.000 48.55885  ? 241 ARG B CD  1 
ATOM   4116 N  NE  . ARG B 1 241 ? -13.17500 -4.84900  -10.85400 1.000 54.15128  ? 241 ARG B NE  1 
ATOM   4117 C  CZ  . ARG B 1 241 ? -12.88100 -5.03500  -12.13300 1.000 52.70606  ? 241 ARG B CZ  1 
ATOM   4118 N  NH1 . ARG B 1 241 ? -12.16100 -4.15600  -12.81700 1.000 49.22088  ? 241 ARG B NH1 1 
ATOM   4119 N  NH2 . ARG B 1 241 ? -13.31300 -6.13700  -12.74000 1.000 53.19946  ? 241 ARG B NH2 1 
ATOM   4120 N  N   . GLU B 1 242 ? -15.83600 -0.93300  -6.93500  1.000 36.39029  ? 242 GLU B N   1 
ATOM   4121 C  CA  . GLU B 1 242 ? -16.86800 -1.41600  -6.02700  1.000 37.29932  ? 242 GLU B CA  1 
ATOM   4122 C  C   . GLU B 1 242 ? -18.20100 -0.73900  -6.30900  1.000 36.74024  ? 242 GLU B C   1 
ATOM   4123 O  O   . GLU B 1 242 ? -19.24000 -1.40300  -6.36800  1.000 35.36611  ? 242 GLU B O   1 
ATOM   4124 C  CB  . GLU B 1 242 ? -16.43800 -1.18500  -4.57300  1.000 41.46289  ? 242 GLU B CB  1 
ATOM   4125 C  CG  . GLU B 1 242 ? -14.96500 -1.55000  -4.29600  1.000 52.39468  ? 242 GLU B CG  1 
ATOM   4126 C  CD  . GLU B 1 242 ? -13.98400 -0.39100  -4.55900  1.000 56.02610  ? 242 GLU B CD  1 
ATOM   4127 O  OE1 . GLU B 1 242 ? -13.77100 0.42900   -3.62300  1.000 62.11903  ? 242 GLU B OE1 1 
ATOM   4128 O  OE2 . GLU B 1 242 ? -13.44400 -0.29400  -5.69600  1.000 49.39934  ? 242 GLU B OE2 1 
ATOM   4129 N  N   . MET B 1 243 ? -18.18500 0.58400   -6.51900  1.000 36.16105  ? 243 MET B N   1 
ATOM   4130 C  CA  . MET B 1 243 ? -19.41500 1.30100   -6.84800  1.000 35.69419  ? 243 MET B CA  1 
ATOM   4131 C  C   . MET B 1 243 ? -19.95700 0.88200   -8.21200  1.000 35.04064  ? 243 MET B C   1 
ATOM   4132 O  O   . MET B 1 243 ? -21.16100 0.63800   -8.36600  1.000 33.85451  ? 243 MET B O   1 
ATOM   4133 C  CB  . MET B 1 243 ? -19.17900 2.81400   -6.81500  1.000 35.16106  ? 243 MET B CB  1 
ATOM   4134 C  CG  . MET B 1 243 ? -20.48200 3.61000   -6.85500  1.000 37.18711  ? 243 MET B CG  1 
ATOM   4135 S  SD  . MET B 1 243 ? -20.26900 5.40700   -6.83200  1.000 45.39956  ? 243 MET B SD  1 
ATOM   4136 C  CE  . MET B 1 243 ? -19.62300 5.65000   -5.18200  1.000 37.03290  ? 243 MET B CE  1 
ATOM   4137 N  N   . VAL B 1 244 ? -19.08600 0.81600   -9.21700  1.000 34.15478  ? 244 VAL B N   1 
ATOM   4138 C  CA  . VAL B 1 244 ? -19.52900 0.45300   -10.56000 1.000 36.21322  ? 244 VAL B CA  1 
ATOM   4139 C  C   . VAL B 1 244 ? -20.19500 -0.91600  -10.53900 1.000 34.33570  ? 244 VAL B C   1 
ATOM   4140 O  O   . VAL B 1 244 ? -21.26700 -1.11600  -11.12400 1.000 31.99433  ? 244 VAL B O   1 
ATOM   4141 C  CB  . VAL B 1 244 ? -18.34600 0.48500   -11.54700 1.000 36.63319  ? 244 VAL B CB  1 
ATOM   4142 C  CG1 . VAL B 1 244 ? -18.77400 -0.05100  -12.91200 1.000 30.75868  ? 244 VAL B CG1 1 
ATOM   4143 C  CG2 . VAL B 1 244 ? -17.79900 1.89600   -11.67200 1.000 34.00245  ? 244 VAL B CG2 1 
ATOM   4144 N  N   . GLU B 1 245 ? -19.57300 -1.87600  -9.85200  1.000 34.34253  ? 245 GLU B N   1 
ATOM   4145 C  CA  . GLU B 1 245 ? -20.07500 -3.24400  -9.86600  1.000 35.44505  ? 245 GLU B CA  1 
ATOM   4146 C  C   . GLU B 1 245 ? -21.35800 -3.39900  -9.05900  1.000 36.50186  ? 245 GLU B C   1 
ATOM   4147 O  O   . GLU B 1 245 ? -22.12000 -4.33400  -9.30700  1.000 37.90012  ? 245 GLU B O   1 
ATOM   4148 C  CB  . GLU B 1 245 ? -18.97900 -4.19300  -9.38200  1.000 36.17160  ? 245 GLU B CB  1 
ATOM   4149 C  CG  . GLU B 1 245 ? -17.80400 -4.26000  -10.38200 1.000 37.80573  ? 245 GLU B CG  1 
ATOM   4150 C  CD  . GLU B 1 245 ? -16.83400 -5.40800  -10.13700 1.000 43.48669  ? 245 GLU B CD  1 
ATOM   4151 O  OE1 . GLU B 1 245 ? -16.65200 -5.80500  -8.96500  1.000 43.12092  ? 245 GLU B OE1 1 
ATOM   4152 O  OE2 . GLU B 1 245 ? -16.25500 -5.92700  -11.12900 1.000 46.01337  ? 245 GLU B OE2 1 
ATOM   4153 N  N   . SER B 1 246 ? -21.65000 -2.47400  -8.15100  1.000 35.23725  ? 246 SER B N   1 
ATOM   4154 C  CA  . SER B 1 246 ? -22.91100 -2.54900  -7.42500  1.000 37.61804  ? 246 SER B CA  1 
ATOM   4155 C  C   . SER B 1 246 ? -24.09800 -2.11900  -8.27700  1.000 36.01947  ? 246 SER B C   1 
ATOM   4156 O  O   . SER B 1 246 ? -25.23800 -2.38200  -7.89600  1.000 38.72279  ? 246 SER B O   1 
ATOM   4157 C  CB  . SER B 1 246 ? -22.84600 -1.69300  -6.16200  1.000 35.46408  ? 246 SER B CB  1 
ATOM   4158 O  OG  . SER B 1 246 ? -22.79200 -0.32100  -6.53200  1.000 39.05732  ? 246 SER B OG  1 
ATOM   4159 N  N   . MET B 1 247 ? -23.86000 -1.50000  -9.42800  1.000 32.73677  ? 247 MET B N   1 
ATOM   4160 C  CA  . MET B 1 247 ? -24.93900 -1.08900  -10.31300 1.000 36.15228  ? 247 MET B CA  1 
ATOM   4161 C  C   . MET B 1 247 ? -25.38400 -2.23100  -11.23000 1.000 36.37232  ? 247 MET B C   1 
ATOM   4162 O  O   . MET B 1 247 ? -24.66500 -3.21200  -11.43900 1.000 37.81703  ? 247 MET B O   1 
ATOM   4163 C  CB  . MET B 1 247 ? -24.50300 0.09300   -11.17900 1.000 34.28872  ? 247 MET B CB  1 
ATOM   4164 C  CG  . MET B 1 247 ? -23.98200 1.28400   -10.39700 1.000 36.46494  ? 247 MET B CG  1 
ATOM   4165 S  SD  . MET B 1 247 ? -23.86700 2.73700   -11.46700 1.000 36.38128  ? 247 MET B SD  1 
ATOM   4166 C  CE  . MET B 1 247 ? -22.55800 2.26100   -12.58800 1.000 35.62036  ? 247 MET B CE  1 
ATOM   4167 N  N   . THR B 1 248 ? -26.57200 -2.06200  -11.81300 1.000 33.29306  ? 248 THR B N   1 
ATOM   4168 C  CA  . THR B 1 248 ? -27.10000 -2.97100  -12.81900 1.000 36.73347  ? 248 THR B CA  1 
ATOM   4169 C  C   . THR B 1 248 ? -26.44200 -2.70400  -14.17200 1.000 34.49140  ? 248 THR B C   1 
ATOM   4170 O  O   . THR B 1 248 ? -25.83500 -1.65500  -14.40000 1.000 33.48558  ? 248 THR B O   1 
ATOM   4171 C  CB  . THR B 1 248 ? -28.61400 -2.81600  -12.94600 1.000 37.59935  ? 248 THR B CB  1 
ATOM   4172 O  OG1 . THR B 1 248 ? -28.90100 -1.51000  -13.45800 1.000 32.00212  ? 248 THR B OG1 1 
ATOM   4173 C  CG2 . THR B 1 248 ? -29.29000 -2.97700  -11.58700 1.000 33.14058  ? 248 THR B CG2 1 
ATOM   4174 N  N   . VAL B 1 249 ? -26.57600 -3.67100  -15.08300 1.000 35.83081  ? 249 VAL B N   1 
ATOM   4175 C  CA  . VAL B 1 249 ? -25.99900 -3.49800  -16.41800 1.000 34.47342  ? 249 VAL B CA  1 
ATOM   4176 C  C   . VAL B 1 249 ? -26.49600 -2.20600  -17.04300 1.000 31.52962  ? 249 VAL B C   1 
ATOM   4177 O  O   . VAL B 1 249 ? -25.71600 -1.43000  -17.61300 1.000 33.06723  ? 249 VAL B O   1 
ATOM   4178 C  CB  . VAL B 1 249 ? -26.32100 -4.70400  -17.32100 1.000 34.98884  ? 249 VAL B CB  1 
ATOM   4179 C  CG1 . VAL B 1 249 ? -25.76200 -4.45200  -18.74000 1.000 34.32452  ? 249 VAL B CG1 1 
ATOM   4180 C  CG2 . VAL B 1 249 ? -25.74500 -5.98500  -16.73800 1.000 32.87041  ? 249 VAL B CG2 1 
ATOM   4181 N  N   . LEU B 1 250 ? -27.80200 -1.95200  -16.93900 1.000 30.68302  ? 250 LEU B N   1 
ATOM   4182 C  CA  . LEU B 1 250 ? -28.36900 -0.73000  -17.49600 1.000 32.43073  ? 250 LEU B CA  1 
ATOM   4183 C  C   . LEU B 1 250 ? -27.65800 0.50100   -16.94100 1.000 29.30366  ? 250 LEU B C   1 
ATOM   4184 O  O   . LEU B 1 250 ? -27.22800 1.38300   -17.69900 1.000 28.78722  ? 250 LEU B O   1 
ATOM   4185 C  CB  . LEU B 1 250 ? -29.87100 -0.69000  -17.21500 1.000 27.85013  ? 250 LEU B CB  1 
ATOM   4186 C  CG  . LEU B 1 250 ? -30.61100 0.49900   -17.83300 1.000 30.74276  ? 250 LEU B CG  1 
ATOM   4187 C  CD1 . LEU B 1 250 ? -30.35600 0.56300   -19.30500 1.000 29.05494  ? 250 LEU B CD1 1 
ATOM   4188 C  CD2 . LEU B 1 250 ? -32.09800 0.39600   -17.55600 1.000 37.17244  ? 250 LEU B CD2 1 
ATOM   4189 N  N   . GLY B 1 251 ? -27.46500 0.54300   -15.61600 1.000 31.31563  ? 251 GLY B N   1 
ATOM   4190 C  CA  . GLY B 1 251 ? -26.74500 1.65700   -15.01500 1.000 29.21855  ? 251 GLY B CA  1 
ATOM   4191 C  C   . GLY B 1 251 ? -25.32000 1.78200   -15.52000 1.000 30.22133  ? 251 GLY B C   1 
ATOM   4192 O  O   . GLY B 1 251 ? -24.84900 2.88100   -15.83100 1.000 26.78433  ? 251 GLY B O   1 
ATOM   4193 N  N   . GLN B 1 252 ? -24.59900 0.65900   -15.57700 1.000 28.13700  ? 252 GLN B N   1 
ATOM   4194 C  CA  . GLN B 1 252 ? -23.24700 0.68500   -16.12200 1.000 30.49985  ? 252 GLN B CA  1 
ATOM   4195 C  C   . GLN B 1 252 ? -23.23400 1.20900   -17.55300 1.000 27.62683  ? 252 GLN B C   1 
ATOM   4196 O  O   . GLN B 1 252 ? -22.38100 2.02500   -17.90500 1.000 27.76339  ? 252 GLN B O   1 
ATOM   4197 C  CB  . GLN B 1 252 ? -22.63100 -0.71100  -16.05300 1.000 31.85099  ? 252 GLN B CB  1 
ATOM   4198 C  CG  . GLN B 1 252 ? -22.47500 -1.22100  -14.64000 1.000 32.18347  ? 252 GLN B CG  1 
ATOM   4199 C  CD  . GLN B 1 252 ? -21.83200 -2.58900  -14.59200 1.000 34.20605  ? 252 GLN B CD  1 
ATOM   4200 O  OE1 . GLN B 1 252 ? -21.74000 -3.27500  -15.61000 1.000 33.25204  ? 252 GLN B OE1 1 
ATOM   4201 N  NE2 . GLN B 1 252 ? -21.37100 -2.98500  -13.41100 1.000 34.22655  ? 252 GLN B NE2 1 
ATOM   4202 N  N   . ARG B 1 253 ? -24.17900 0.75500   -18.38300 1.000 26.20887  ? 253 ARG B N   1 
ATOM   4203 C  CA  . ARG B 1 253 ? -24.29400 1.25600   -19.74900 1.000 27.63079  ? 253 ARG B CA  1 
ATOM   4204 C  C   . ARG B 1 253 ? -24.52600 2.76300   -19.78600 1.000 29.51857  ? 253 ARG B C   1 
ATOM   4205 O  O   . ARG B 1 253 ? -23.91000 3.47100   -20.59700 1.000 27.04362  ? 253 ARG B O   1 
ATOM   4206 C  CB  . ARG B 1 253 ? -25.41600 0.52600   -20.48300 1.000 28.78775  ? 253 ARG B CB  1 
ATOM   4207 C  CG  . ARG B 1 253 ? -25.08900 -0.94500  -20.74100 1.000 29.02118  ? 253 ARG B CG  1 
ATOM   4208 C  CD  . ARG B 1 253 ? -26.22200 -1.68500  -21.44600 1.000 33.28390  ? 253 ARG B CD  1 
ATOM   4209 N  NE  . ARG B 1 253 ? -26.35000 -1.27400  -22.84000 1.000 34.73732  ? 253 ARG B NE  1 
ATOM   4210 C  CZ  . ARG B 1 253 ? -27.33400 -0.52100  -23.31400 1.000 40.27985  ? 253 ARG B CZ  1 
ATOM   4211 N  NH1 . ARG B 1 253 ? -28.34100 -0.12900  -22.54400 1.000 39.41423  ? 253 ARG B NH1 1 
ATOM   4212 N  NH2 . ARG B 1 253 ? -27.31300 -0.15500  -24.59600 1.000 37.93025  ? 253 ARG B NH2 1 
ATOM   4213 N  N   . MET B 1 254 ? -25.40300 3.27200   -18.91000 1.000 29.83832  ? 254 MET B N   1 
ATOM   4214 C  CA  . MET B 1 254 ? -25.69300 4.70000   -18.89800 1.000 27.02043  ? 254 MET B CA  1 
ATOM   4215 C  C   . MET B 1 254 ? -24.47500 5.52600   -18.50600 1.000 25.31597  ? 254 MET B C   1 
ATOM   4216 O  O   . MET B 1 254 ? -24.29400 6.64000   -19.01200 1.000 25.67987  ? 254 MET B O   1 
ATOM   4217 C  CB  . MET B 1 254 ? -26.85300 5.00200   -17.94600 1.000 26.13251  ? 254 MET B CB  1 
ATOM   4218 C  CG  . MET B 1 254 ? -28.19100 4.47400   -18.42400 1.000 29.70691  ? 254 MET B CG  1 
ATOM   4219 S  SD  . MET B 1 254 ? -28.63800 5.13000   -20.04900 1.000 29.83182  ? 254 MET B SD  1 
ATOM   4220 C  CE  . MET B 1 254 ? -28.52300 3.65200   -21.07700 1.000 30.25545  ? 254 MET B CE  1 
ATOM   4221 N  N   . LEU B 1 255 ? -23.62300 5.00400   -17.62900 1.000 23.65771  ? 255 LEU B N   1 
ATOM   4222 C  CA  . LEU B 1 255 ? -22.48400 5.75700   -17.12000 1.000 24.53148  ? 255 LEU B CA  1 
ATOM   4223 C  C   . LEU B 1 255 ? -21.19300 5.48600   -17.89500 1.000 24.26333  ? 255 LEU B C   1 
ATOM   4224 O  O   . LEU B 1 255 ? -20.09900 5.79000   -17.39900 1.000 26.31166  ? 255 LEU B O   1 
ATOM   4225 C  CB  . LEU B 1 255 ? -22.29800 5.48100   -15.62300 1.000 25.22713  ? 255 LEU B CB  1 
ATOM   4226 C  CG  . LEU B 1 255 ? -23.56400 5.84200   -14.81200 1.000 30.43432  ? 255 LEU B CG  1 
ATOM   4227 C  CD1 . LEU B 1 255 ? -23.29300 5.84900   -13.30000 1.000 28.03814  ? 255 LEU B CD1 1 
ATOM   4228 C  CD2 . LEU B 1 255 ? -24.18500 7.16800   -15.24300 1.000 23.56746  ? 255 LEU B CD2 1 
ATOM   4229 N  N   . GLY B 1 256 ? -21.29400 4.96500   -19.11000 1.000 23.67150  ? 256 GLY B N   1 
ATOM   4230 C  CA  . GLY B 1 256 ? -20.13700 4.88800   -19.99100 1.000 27.60957  ? 256 GLY B CA  1 
ATOM   4231 C  C   . GLY B 1 256 ? -19.16700 3.75900   -19.70900 1.000 28.50620  ? 256 GLY B C   1 
ATOM   4232 O  O   . GLY B 1 256 ? -18.04100 3.78500   -20.22500 1.000 28.71673  ? 256 GLY B O   1 
ATOM   4233 N  N   . TRP B 1 257 ? -19.55600 2.77300   -18.90600 1.000 25.77685  ? 257 TRP B N   1 
ATOM   4234 C  CA  . TRP B 1 257 ? -18.64400 1.71300   -18.48800 1.000 29.30539  ? 257 TRP B CA  1 
ATOM   4235 C  C   . TRP B 1 257 ? -18.68500 0.49000   -19.40400 1.000 27.56168  ? 257 TRP B C   1 
ATOM   4236 O  O   . TRP B 1 257 ? -17.95900 -0.47700  -19.15400 1.000 28.61283  ? 257 TRP B O   1 
ATOM   4237 C  CB  . TRP B 1 257 ? -18.95100 1.31100   -17.03400 1.000 28.61965  ? 257 TRP B CB  1 
ATOM   4238 C  CG  . TRP B 1 257 ? -18.30900 2.27500   -16.05400 1.000 29.73536  ? 257 TRP B CG  1 
ATOM   4239 C  CD1 . TRP B 1 257 ? -18.86900 3.41200   -15.51500 1.000 29.43940  ? 257 TRP B CD1 1 
ATOM   4240 C  CD2 . TRP B 1 257 ? -16.97000 2.22300   -15.56100 1.000 32.38597  ? 257 TRP B CD2 1 
ATOM   4241 N  NE1 . TRP B 1 257 ? -17.96000 4.04800   -14.69900 1.000 30.12389  ? 257 TRP B NE1 1 
ATOM   4242 C  CE2 . TRP B 1 257 ? -16.78500 3.34400   -14.71600 1.000 32.87571  ? 257 TRP B CE2 1 
ATOM   4243 C  CE3 . TRP B 1 257 ? -15.90900 1.33700   -15.74000 1.000 37.55784  ? 257 TRP B CE3 1 
ATOM   4244 C  CZ2 . TRP B 1 257 ? -15.59400 3.58500   -14.05200 1.000 32.22154  ? 257 TRP B CZ2 1 
ATOM   4245 C  CZ3 . TRP B 1 257 ? -14.71400 1.59000   -15.07700 1.000 35.88584  ? 257 TRP B CZ3 1 
ATOM   4246 C  CH2 . TRP B 1 257 ? -14.57400 2.70300   -14.23800 1.000 32.40611  ? 257 TRP B CH2 1 
ATOM   4247 N  N   . ARG B 1 258 ? -19.49800 0.52100   -20.46000 1.000 25.18719  ? 258 ARG B N   1 
ATOM   4248 C  CA  . ARG B 1 258 ? -19.69400 -0.62100  -21.34000 1.000 30.37800  ? 258 ARG B CA  1 
ATOM   4249 C  C   . ARG B 1 258 ? -19.62500 -0.17600  -22.79400 1.000 29.87512  ? 258 ARG B C   1 
ATOM   4250 O  O   . ARG B 1 258 ? -19.86400 0.98900   -23.12200 1.000 29.01810  ? 258 ARG B O   1 
ATOM   4251 C  CB  . ARG B 1 258 ? -21.04400 -1.32000  -21.08200 1.000 28.77017  ? 258 ARG B CB  1 
ATOM   4252 C  CG  . ARG B 1 258 ? -21.17700 -1.84800  -19.66100 1.000 31.52852  ? 258 ARG B CG  1 
ATOM   4253 C  CD  . ARG B 1 258 ? -22.27700 -2.89300  -19.54400 1.000 33.21082  ? 258 ARG B CD  1 
ATOM   4254 N  NE  . ARG B 1 258 ? -22.06500 -3.73800  -18.37500 1.000 33.21188  ? 258 ARG B NE  1 
ATOM   4255 C  CZ  . ARG B 1 258 ? -21.98600 -5.06000  -18.40400 1.000 33.44090  ? 258 ARG B CZ  1 
ATOM   4256 N  NH1 . ARG B 1 258 ? -22.19900 -5.74700  -19.52100 1.000 36.67519  ? 258 ARG B NH1 1 
ATOM   4257 N  NH2 . ARG B 1 258 ? -21.68400 -5.71100  -17.28400 1.000 36.80997  ? 258 ARG B NH2 1 
ATOM   4258 N  N   . THR B 1 259 ? -19.29800 -1.13000  -23.66300 1.000 26.50389  ? 259 THR B N   1 
ATOM   4259 C  CA  . THR B 1 259 ? -19.35100 -0.90800  -25.10200 1.000 27.61613  ? 259 THR B CA  1 
ATOM   4260 C  C   . THR B 1 259 ? -20.80100 -0.73900  -25.51800 1.000 28.86203  ? 259 THR B C   1 
ATOM   4261 O  O   . THR B 1 259 ? -21.68800 -1.39900  -24.97700 1.000 29.98256  ? 259 THR B O   1 
ATOM   4262 C  CB  . THR B 1 259 ? -18.70700 -2.09200  -25.84200 1.000 29.45537  ? 259 THR B CB  1 
ATOM   4263 O  OG1 . THR B 1 259 ? -17.31300 -2.15200  -25.51600 1.000 30.44358  ? 259 THR B OG1 1 
ATOM   4264 C  CG2 . THR B 1 259 ? -18.85600 -1.97500  -27.34400 1.000 27.51287  ? 259 THR B CG2 1 
ATOM   4265 N  N   . MET B 1 260 ? -21.04700 0.15400   -26.48000 1.000 28.86204  ? 260 MET B N   1 
ATOM   4266 C  CA  . MET B 1 260 ? -22.39700 0.51400   -26.89900 1.000 28.36549  ? 260 MET B CA  1 
ATOM   4267 C  C   . MET B 1 260 ? -22.50100 0.42600   -28.41500 1.000 31.38961  ? 260 MET B C   1 
ATOM   4268 O  O   . MET B 1 260 ? -21.50800 0.21800   -29.11500 1.000 32.30955  ? 260 MET B O   1 
ATOM   4269 C  CB  . MET B 1 260 ? -22.75900 1.92600   -26.40900 1.000 26.37186  ? 260 MET B CB  1 
ATOM   4270 C  CG  . MET B 1 260 ? -22.58600 2.10500   -24.90100 1.000 28.70397  ? 260 MET B CG  1 
ATOM   4271 S  SD  . MET B 1 260 ? -23.81500 1.20200   -23.91400 1.000 30.22392  ? 260 MET B SD  1 
ATOM   4272 C  CE  . MET B 1 260 ? -25.09500 2.47600   -23.80100 1.000 26.25597  ? 260 MET B CE  1 
ATOM   4273 N  N   . LYS B 1 261 ? -23.71000 0.60100   -28.94000 1.000 28.99125  ? 261 LYS B N   1 
ATOM   4274 C  CA  . LYS B 1 261 ? -23.95400 0.39600   -30.36900 1.000 31.87391  ? 261 LYS B CA  1 
ATOM   4275 C  C   . LYS B 1 261 ? -24.80600 1.52400   -30.95400 1.000 33.22585  ? 261 LYS B C   1 
ATOM   4276 O  O   . LYS B 1 261 ? -26.02900 1.57300   -30.72100 1.000 31.35139  ? 261 LYS B O   1 
ATOM   4277 C  CB  . LYS B 1 261 ? -24.60300 -0.97200  -30.58800 1.000 31.19702  ? 261 LYS B CB  1 
ATOM   4278 C  CG  . LYS B 1 261 ? -24.98800 -1.31900  -32.03100 1.000 35.13747  ? 261 LYS B CG  1 
ATOM   4279 C  CD  . LYS B 1 261 ? -23.78200 -1.54100  -32.93100 1.000 35.89731  ? 261 LYS B CD  1 
ATOM   4280 C  CE  . LYS B 1 261 ? -24.22600 -2.12900  -34.26800 1.000 41.45093  ? 261 LYS B CE  1 
ATOM   4281 N  NZ  . LYS B 1 261 ? -25.25300 -1.24400  -34.92100 1.000 41.07424  ? 261 LYS B NZ  1 
ATOM   4282 N  N   . PRO B 1 262 ? -24.19700 2.45600   -31.69900 1.000 29.86349  ? 262 PRO B N   1 
ATOM   4283 C  CA  . PRO B 1 262 ? -24.97300 3.28300   -32.63000 1.000 31.01778  ? 262 PRO B CA  1 
ATOM   4284 C  C   . PRO B 1 262 ? -25.63900 2.41500   -33.68800 1.000 30.58778  ? 262 PRO B C   1 
ATOM   4285 O  O   . PRO B 1 262 ? -25.24200 1.27600   -33.94500 1.000 34.50088  ? 262 PRO B O   1 
ATOM   4286 C  CB  . PRO B 1 262 ? -23.92100 4.20700   -33.26200 1.000 30.52619  ? 262 PRO B CB  1 
ATOM   4287 C  CG  . PRO B 1 262 ? -22.73400 4.11100   -32.39400 1.000 29.76280  ? 262 PRO B CG  1 
ATOM   4288 C  CD  . PRO B 1 262 ? -22.76100 2.75500   -31.77700 1.000 30.93253  ? 262 PRO B CD  1 
ATOM   4289 N  N   . SER B 1 263 ? -26.64600 2.97700   -34.34100 1.000 32.87972  ? 263 SER B N   1 
ATOM   4290 C  CA  . SER B 1 263 ? -27.31000 2.22700   -35.39500 1.000 36.43803  ? 263 SER B CA  1 
ATOM   4291 C  C   . SER B 1 263 ? -26.38600 1.98700   -36.59300 1.000 38.82915  ? 263 SER B C   1 
ATOM   4292 O  O   . SER B 1 263 ? -25.39200 2.70400   -36.81900 1.000 33.50847  ? 263 SER B O   1 
ATOM   4293 C  CB  . SER B 1 263 ? -28.57700 2.94400   -35.85800 1.000 39.42181  ? 263 SER B CB  1 
ATOM   4294 O  OG  . SER B 1 263 ? -29.62500 2.68600   -34.93900 1.000 46.45195  ? 263 SER B OG  1 
ATOM   4295 N  N   . ASP B 1 264 ? -26.72700 0.93500   -37.34800 1.000 38.90136  ? 264 ASP B N   1 
ATOM   4296 C  CA  . ASP B 1 264 ? -26.18400 0.76500   -38.68300 1.000 40.86858  ? 264 ASP B CA  1 
ATOM   4297 C  C   . ASP B 1 264 ? -26.31900 2.09500   -39.42400 1.000 39.26579  ? 264 ASP B C   1 
ATOM   4298 O  O   . ASP B 1 264 ? -27.33700 2.78400   -39.27400 1.000 40.54106  ? 264 ASP B O   1 
ATOM   4299 C  CB  . ASP B 1 264 ? -26.91900 -0.35700  -39.44600 1.000 42.31209  ? 264 ASP B CB  1 
ATOM   4300 C  CG  . ASP B 1 264 ? -27.00300 -1.69300  -38.65600 1.000 54.75863  ? 264 ASP B CG  1 
ATOM   4301 O  OD1 . ASP B 1 264 ? -26.19900 -1.93200  -37.72000 1.000 50.54410  ? 264 ASP B OD1 1 
ATOM   4302 O  OD2 . ASP B 1 264 ? -27.90000 -2.50600  -38.99500 1.000 63.40808  ? 264 ASP B OD2 1 
ATOM   4303 N  N   . PRO B 1 265 ? -25.35600 2.46500   -40.26900 1.000 40.63256  ? 265 PRO B N   1 
ATOM   4304 C  CA  . PRO B 1 265 ? -24.22000 1.67000   -40.77000 1.000 40.21277  ? 265 PRO B CA  1 
ATOM   4305 C  C   . PRO B 1 265 ? -23.01800 1.52800   -39.83400 1.000 38.27929  ? 265 PRO B C   1 
ATOM   4306 O  O   . PRO B 1 265 ? -22.03000 0.94600   -40.25400 1.000 38.99366  ? 265 PRO B O   1 
ATOM   4307 C  CB  . PRO B 1 265 ? -23.83300 2.41300   -42.05400 1.000 42.30825  ? 265 PRO B CB  1 
ATOM   4308 C  CG  . PRO B 1 265 ? -24.17900 3.86100   -41.75600 1.000 41.42048  ? 265 PRO B CG  1 
ATOM   4309 C  CD  . PRO B 1 265 ? -25.42600 3.80000   -40.90100 1.000 40.28745  ? 265 PRO B CD  1 
ATOM   4310 N  N   . ASN B 1 266 ? -23.02900 1.98900   -38.58700 1.000 35.73468  ? 266 ASN B N   1 
ATOM   4311 C  CA  . ASN B 1 266 ? -22.05200 1.48100   -37.63300 1.000 36.02674  ? 266 ASN B CA  1 
ATOM   4312 C  C   . ASN B 1 266 ? -22.46500 0.05400   -37.29100 1.000 41.94136  ? 266 ASN B C   1 
ATOM   4313 O  O   . ASN B 1 266 ? -23.48400 -0.16200  -36.62300 1.000 44.12897  ? 266 ASN B O   1 
ATOM   4314 C  CB  . ASN B 1 266 ? -21.98900 2.35700   -36.38200 1.000 33.14482  ? 266 ASN B CB  1 
ATOM   4315 C  CG  . ASN B 1 266 ? -20.92500 1.89300   -35.38500 1.000 36.01140  ? 266 ASN B CG  1 
ATOM   4316 O  OD1 . ASN B 1 266 ? -20.66700 0.69900   -35.23200 1.000 41.70191  ? 266 ASN B OD1 1 
ATOM   4317 N  ND2 . ASN B 1 266 ? -20.30800 2.84100   -34.70000 1.000 34.07498  ? 266 ASN B ND2 1 
ATOM   4318 N  N   . ILE B 1 267 ? -21.71000 -0.93400  -37.76600 1.000 39.92331  ? 267 ILE B N   1 
ATOM   4319 C  CA  . ILE B 1 267 ? -22.07700 -2.31600  -37.49900 1.000 46.09811  ? 267 ILE B CA  1 
ATOM   4320 C  C   . ILE B 1 267 ? -21.20100 -2.96200  -36.44100 1.000 45.92625  ? 267 ILE B C   1 
ATOM   4321 O  O   . ILE B 1 267 ? -21.38300 -4.15200  -36.14400 1.000 50.67197  ? 267 ILE B O   1 
ATOM   4322 C  CB  . ILE B 1 267 ? -22.09800 -3.15300  -38.79200 1.000 47.09942  ? 267 ILE B CB  1 
ATOM   4323 C  CG1 . ILE B 1 267 ? -20.77200 -3.05100  -39.54700 1.000 51.57207  ? 267 ILE B CG1 1 
ATOM   4324 C  CG2 . ILE B 1 267 ? -23.23600 -2.68200  -39.68500 1.000 45.76791  ? 267 ILE B CG2 1 
ATOM   4325 C  CD1 . ILE B 1 267 ? -19.79000 -4.15300  -39.21500 1.000 58.76506  ? 267 ILE B CD1 1 
ATOM   4326 N  N   . VAL B 1 268 ? -20.28800 -2.21700  -35.83100 1.000 43.51194  ? 268 VAL B N   1 
ATOM   4327 C  CA  . VAL B 1 268 ? -19.33500 -2.75600  -34.87300 1.000 41.95183  ? 268 VAL B CA  1 
ATOM   4328 C  C   . VAL B 1 268 ? -19.65700 -2.29900  -33.45400 1.000 41.65892  ? 268 VAL B C   1 
ATOM   4329 O  O   . VAL B 1 268 ? -19.75500 -3.11300  -32.53800 1.000 41.35113  ? 268 VAL B O   1 
ATOM   4330 C  CB  . VAL B 1 268 ? -17.88700 -2.37700  -35.25900 1.000 42.25101  ? 268 VAL B CB  1 
ATOM   4331 C  CG1 . VAL B 1 268 ? -16.91600 -2.88700  -34.22200 1.000 42.71566  ? 268 VAL B CG1 1 
ATOM   4332 C  CG2 . VAL B 1 268 ? -17.53800 -2.93000  -36.62800 1.000 46.10426  ? 268 VAL B CG2 1 
ATOM   4333 N  N   . GLY B 1 269 ? -19.79800 -0.99300  -33.25500 1.000 35.95508  ? 269 GLY B N   1 
ATOM   4334 C  CA  . GLY B 1 269 ? -20.11100 -0.44300  -31.95900 1.000 35.88544  ? 269 GLY B CA  1 
ATOM   4335 C  C   . GLY B 1 269 ? -19.28100 0.79700   -31.70000 1.000 32.83111  ? 269 GLY B C   1 
ATOM   4336 O  O   . GLY B 1 269 ? -18.74300 1.41000   -32.61900 1.000 30.95178  ? 269 GLY B O   1 
ATOM   4337 N  N   . ILE B 1 270 ? -19.17300 1.15300   -30.42300 1.000 29.63434  ? 270 ILE B N   1 
ATOM   4338 C  CA  . ILE B 1 270 ? -18.40400 2.31900   -30.00200 1.000 29.99210  ? 270 ILE B CA  1 
ATOM   4339 C  C   . ILE B 1 270 ? -18.00800 2.10700   -28.54800 1.000 28.42096  ? 270 ILE B C   1 
ATOM   4340 O  O   . ILE B 1 270 ? -18.64000 1.33100   -27.82800 1.000 29.36639  ? 270 ILE B O   1 
ATOM   4341 C  CB  . ILE B 1 270 ? -19.23900 3.60800   -30.20800 1.000 28.00998  ? 270 ILE B CB  1 
ATOM   4342 C  CG1 . ILE B 1 270 ? -18.33100 4.81400   -30.37700 1.000 29.06168  ? 270 ILE B CG1 1 
ATOM   4343 C  CG2 . ILE B 1 270 ? -20.26600 3.83000   -29.05900 1.000 28.62506  ? 270 ILE B CG2 1 
ATOM   4344 C  CD1 . ILE B 1 270 ? -19.00300 5.91100   -31.12800 1.000 32.30240  ? 270 ILE B CD1 1 
ATOM   4345 N  N   . ASN B 1 271 ? -16.94100 2.78600   -28.11600 1.000 28.71319  ? 271 ASN B N   1 
ATOM   4346 C  CA  . ASN B 1 271 ? -16.45200 2.71100   -26.73300 1.000 29.62852  ? 271 ASN B CA  1 
ATOM   4347 C  C   . ASN B 1 271 ? -15.94600 1.30100   -26.40300 1.000 31.24510  ? 271 ASN B C   1 
ATOM   4348 O  O   . ASN B 1 271 ? -16.39000 0.65600   -25.45100 1.000 28.47170  ? 271 ASN B O   1 
ATOM   4349 C  CB  . ASN B 1 271 ? -17.54900 3.15100   -25.74000 1.000 30.02376  ? 271 ASN B CB  1 
ATOM   4350 C  CG  . ASN B 1 271 ? -17.00700 3.39500   -24.35400 1.000 30.10685  ? 271 ASN B CG  1 
ATOM   4351 O  OD1 . ASN B 1 271 ? -15.94900 3.99200   -24.20100 1.000 30.41825  ? 271 ASN B OD1 1 
ATOM   4352 N  ND2 . ASN B 1 271 ? -17.73300 2.94200   -23.33600 1.000 27.27190  ? 271 ASN B ND2 1 
ATOM   4353 N  N   . LEU B 1 272 ? -15.00800 0.82200   -27.22700 1.000 31.82384  ? 272 LEU B N   1 
ATOM   4354 C  CA  . LEU B 1 272 ? -14.44600 -0.51500  -27.08200 1.000 32.40960  ? 272 LEU B CA  1 
ATOM   4355 C  C   . LEU B 1 272 ? -12.92400 -0.42000  -27.09200 1.000 30.57197  ? 272 LEU B C   1 
ATOM   4356 O  O   . LEU B 1 272 ? -12.35000 0.63300   -27.37600 1.000 30.81601  ? 272 LEU B O   1 
ATOM   4357 C  CB  . LEU B 1 272 ? -14.97200 -1.44900  -28.18800 1.000 29.38201  ? 272 LEU B CB  1 
ATOM   4358 C  CG  . LEU B 1 272 ? -14.80200 -1.03200  -29.65800 1.000 33.57376  ? 272 LEU B CG  1 
ATOM   4359 C  CD1 . LEU B 1 272 ? -14.03100 -2.07500  -30.42800 1.000 39.13230  ? 272 LEU B CD1 1 
ATOM   4360 C  CD2 . LEU B 1 272 ? -16.15500 -0.82000  -30.32900 1.000 33.57440  ? 272 LEU B CD2 1 
ATOM   4361 N  N   . ILE B 1 273 ? -12.26600 -1.52800  -26.77200 1.000 29.74310  ? 273 ILE B N   1 
ATOM   4362 C  CA  . ILE B 1 273 ? -10.81300 -1.54500  -26.66400 1.000 34.36508  ? 273 ILE B CA  1 
ATOM   4363 C  C   . ILE B 1 273 ? -10.33200 -2.95300  -26.98300 1.000 34.88467  ? 273 ILE B C   1 
ATOM   4364 O  O   . ILE B 1 273 ? -10.98300 -3.93600  -26.62400 1.000 36.28647  ? 273 ILE B O   1 
ATOM   4365 C  CB  . ILE B 1 273 ? -10.34600 -1.07400  -25.26100 1.000 33.88571  ? 273 ILE B CB  1 
ATOM   4366 C  CG1 . ILE B 1 273 ? -8.81400  -1.05900  -25.15400 1.000 37.12927  ? 273 ILE B CG1 1 
ATOM   4367 C  CG2 . ILE B 1 273 ? -10.98400 -1.91000  -24.15500 1.000 35.96777  ? 273 ILE B CG2 1 
ATOM   4368 C  CD1 . ILE B 1 273 ? -8.16200  -0.10200  -26.16000 1.000 36.80768  ? 273 ILE B CD1 1 
ATOM   4369 N  N   . ASP B 1 274 ? -9.19400  -3.04000  -27.67500 1.000 36.10556  ? 274 ASP B N   1 
ATOM   4370 C  CA  . ASP B 1 274 ? -8.58800  -4.31600  -28.07400 1.000 38.33508  ? 274 ASP B CA  1 
ATOM   4371 C  C   . ASP B 1 274 ? -9.52600  -5.15300  -28.94600 1.000 38.58422  ? 274 ASP B C   1 
ATOM   4372 O  O   . ASP B 1 274 ? -9.43600  -6.37900  -28.95300 1.000 39.48935  ? 274 ASP B O   1 
ATOM   4373 C  CB  . ASP B 1 274 ? -8.13900  -5.12800  -26.85300 1.000 39.29394  ? 274 ASP B CB  1 
ATOM   4374 C  CG  . ASP B 1 274 ? -7.14800  -4.37300  -25.98100 1.000 45.80494  ? 274 ASP B CG  1 
ATOM   4375 O  OD1 . ASP B 1 274 ? -6.32800  -3.60600  -26.53800 1.000 48.26834  ? 274 ASP B OD1 1 
ATOM   4376 O  OD2 . ASP B 1 274 ? -7.18600  -4.54500  -24.73800 1.000 49.20588  ? 274 ASP B OD2 1 
ATOM   4377 N  N   . ASP B 1 275 ? -10.43400 -4.50100  -29.68200 1.000 37.36019  ? 275 ASP B N   1 
ATOM   4378 C  CA  . ASP B 1 275 ? -11.47900 -5.17100  -30.45700 1.000 41.09146  ? 275 ASP B CA  1 
ATOM   4379 C  C   . ASP B 1 275 ? -12.38900 -6.02600  -29.57300 1.000 43.30191  ? 275 ASP B C   1 
ATOM   4380 O  O   . ASP B 1 275 ? -13.01800 -6.97400  -30.04500 1.000 38.13906  ? 275 ASP B O   1 
ATOM   4381 C  CB  . ASP B 1 275 ? -10.89100 -6.02000  -31.59400 1.000 43.36554  ? 275 ASP B CB  1 
ATOM   4382 C  CG  . ASP B 1 275 ? -11.86100 -6.17400  -32.76300 1.000 48.77947  ? 275 ASP B CG  1 
ATOM   4383 O  OD1 . ASP B 1 275 ? -12.89100 -5.46100  -32.76300 1.000 48.92553  ? 275 ASP B OD1 1 
ATOM   4384 O  OD2 . ASP B 1 275 ? -11.60900 -7.00100  -33.66700 1.000 46.50940  ? 275 ASP B OD2 1 
ATOM   4385 N  N   . LYS B 1 276 ? -12.47000 -5.69000  -28.29000 1.000 38.99997  ? 276 LYS B N   1 
ATOM   4386 C  CA  . LYS B 1 276 ? -13.29800 -6.39500  -27.32600 1.000 37.99007  ? 276 LYS B CA  1 
ATOM   4387 C  C   . LYS B 1 276 ? -14.24900 -5.41000  -26.65300 1.000 35.67097  ? 276 LYS B C   1 
ATOM   4388 O  O   . LYS B 1 276 ? -14.04100 -4.19100  -26.68100 1.000 34.00516  ? 276 LYS B O   1 
ATOM   4389 C  CB  . LYS B 1 276 ? -12.43400 -7.09300  -26.26800 1.000 37.94234  ? 276 LYS B CB  1 
ATOM   4390 C  CG  . LYS B 1 276 ? -11.57300 -8.20600  -26.82300 1.000 45.64346  ? 276 LYS B CG  1 
ATOM   4391 C  CD  . LYS B 1 276 ? -10.41600 -8.52200  -25.87600 1.000 50.92867  ? 276 LYS B CD  1 
ATOM   4392 C  CE  . LYS B 1 276 ? -10.92000 -8.92500  -24.49400 1.000 54.23874  ? 276 LYS B CE  1 
ATOM   4393 N  NZ  . LYS B 1 276 ? -9.80500  -8.99000  -23.48700 1.000 60.49886  ? 276 LYS B NZ  1 
ATOM   4394 N  N   . ARG B 1 277 ? -15.30000 -5.94600  -26.04200 1.000 33.04983  ? 277 ARG B N   1 
ATOM   4395 C  CA  . ARG B 1 277 ? -16.17300 -5.10100  -25.23700 1.000 33.75718  ? 277 ARG B CA  1 
ATOM   4396 C  C   . ARG B 1 277 ? -15.43900 -4.62800  -23.98500 1.000 32.78162  ? 277 ARG B C   1 
ATOM   4397 O  O   . ARG B 1 277 ? -14.69200 -5.38200  -23.35300 1.000 33.23537  ? 277 ARG B O   1 
ATOM   4398 C  CB  . ARG B 1 277 ? -17.46200 -5.83700  -24.85600 1.000 35.38275  ? 277 ARG B CB  1 
ATOM   4399 C  CG  . ARG B 1 277 ? -18.29100 -6.30300  -26.05800 1.000 42.71169  ? 277 ARG B CG  1 
ATOM   4400 C  CD  . ARG B 1 277 ? -19.58700 -7.02300  -25.65600 1.000 45.05107  ? 277 ARG B CD  1 
ATOM   4401 N  NE  . ARG B 1 277 ? -20.15200 -7.78000  -26.77300 1.000 52.94121  ? 277 ARG B NE  1 
ATOM   4402 C  CZ  . ARG B 1 277 ? -21.33700 -8.38300  -26.76400 1.000 63.43948  ? 277 ARG B CZ  1 
ATOM   4403 N  NH1 . ARG B 1 277 ? -22.16100 -8.28800  -25.72800 1.000 64.71604  ? 277 ARG B NH1 1 
ATOM   4404 N  NH2 . ARG B 1 277 ? -21.70700 -9.10600  -27.82000 1.000 62.41853  ? 277 ARG B NH2 1 
ATOM   4405 N  N   . LEU B 1 278 ? -15.67400 -3.36200  -23.63300 1.000 33.23308  ? 278 LEU B N   1 
ATOM   4406 C  CA  . LEU B 1 278 ? -14.98500 -2.72700  -22.51700 1.000 32.34393  ? 278 LEU B CA  1 
ATOM   4407 C  C   . LEU B 1 278 ? -15.24600 -3.46300  -21.20700 1.000 31.57046  ? 278 LEU B C   1 
ATOM   4408 O  O   . LEU B 1 278 ? -14.33100 -3.64500  -20.39400 1.000 29.66042  ? 278 LEU B O   1 
ATOM   4409 C  CB  . LEU B 1 278 ? -15.42800 -1.26200  -22.42300 1.000 29.67270  ? 278 LEU B CB  1 
ATOM   4410 C  CG  . LEU B 1 278 ? -15.04500 -0.50000  -21.15500 1.000 31.76525  ? 278 LEU B CG  1 
ATOM   4411 C  CD1 . LEU B 1 278 ? -13.53000 -0.45000  -21.00000 1.000 30.49347  ? 278 LEU B CD1 1 
ATOM   4412 C  CD2 . LEU B 1 278 ? -15.65100 0.92200   -21.16700 1.000 29.95668  ? 278 LEU B CD2 1 
ATOM   4413 N  N   . GLU B 1 279 ? -16.48600 -3.90400  -20.98800 1.000 29.87096  ? 279 GLU B N   1 
ATOM   4414 C  CA  . GLU B 1 279 ? -16.78100 -4.64400  -19.76700 1.000 34.15999  ? 279 GLU B CA  1 
ATOM   4415 C  C   . GLU B 1 279 ? -16.06500 -5.99600  -19.73000 1.000 36.35015  ? 279 GLU B C   1 
ATOM   4416 O  O   . GLU B 1 279 ? -15.79400 -6.50700  -18.64000 1.000 36.43920  ? 279 GLU B O   1 
ATOM   4417 C  CB  . GLU B 1 279 ? -18.30300 -4.81600  -19.59900 1.000 34.03408  ? 279 GLU B CB  1 
ATOM   4418 C  CG  . GLU B 1 279 ? -19.01400 -5.57900  -20.72900 1.000 34.65604  ? 279 GLU B CG  1 
ATOM   4419 C  CD  . GLU B 1 279 ? -19.42600 -4.68100  -21.91600 1.000 35.98691  ? 279 GLU B CD  1 
ATOM   4420 O  OE1 . GLU B 1 279 ? -18.76800 -3.64400  -22.19100 1.000 30.85563  ? 279 GLU B OE1 1 
ATOM   4421 O  OE2 . GLU B 1 279 ? -20.42800 -5.02100  -22.57400 1.000 35.84366  ? 279 GLU B OE2 1 
ATOM   4422 N  N   . ASN B 1 280 ? -15.71800 -6.56900  -20.88700 1.000 35.10533  ? 280 ASN B N   1 
ATOM   4423 C  CA  . ASN B 1 280 ? -14.93600 -7.80100  -20.88700 1.000 34.99525  ? 280 ASN B CA  1 
ATOM   4424 C  C   . ASN B 1 280 ? -13.47200 -7.54100  -20.53900 1.000 38.75571  ? 280 ASN B C   1 
ATOM   4425 O  O   . ASN B 1 280 ? -12.87000 -8.30600  -19.77800 1.000 36.10844  ? 280 ASN B O   1 
ATOM   4426 C  CB  . ASN B 1 280 ? -15.02100 -8.49200  -22.25100 1.000 36.83795  ? 280 ASN B CB  1 
ATOM   4427 C  CG  . ASN B 1 280 ? -16.37800 -9.11600  -22.51000 1.000 44.99943  ? 280 ASN B CG  1 
ATOM   4428 O  OD1 . ASN B 1 280 ? -17.16800 -9.35300  -21.58000 1.000 43.35145  ? 280 ASN B OD1 1 
ATOM   4429 N  ND2 . ASN B 1 280 ? -16.65600 -9.39900  -23.77800 1.000 45.19181  ? 280 ASN B ND2 1 
ATOM   4430 N  N   . VAL B 1 281 ? -12.86700 -6.49800  -21.12200 1.000 37.94989  ? 281 VAL B N   1 
ATOM   4431 C  CA  . VAL B 1 281 ? -11.47700 -6.17800  -20.79900 1.000 34.27406  ? 281 VAL B CA  1 
ATOM   4432 C  C   . VAL B 1 281 ? -11.35200 -5.83300  -19.31900 1.000 35.95888  ? 281 VAL B C   1 
ATOM   4433 O  O   . VAL B 1 281 ? -10.37000 -6.19600  -18.66200 1.000 36.23493  ? 281 VAL B O   1 
ATOM   4434 C  CB  . VAL B 1 281 ? -10.96600 -5.03200  -21.69400 1.000 38.05305  ? 281 VAL B CB  1 
ATOM   4435 C  CG1 . VAL B 1 281 ? -9.57400  -4.59600  -21.26500 1.000 34.89775  ? 281 VAL B CG1 1 
ATOM   4436 C  CG2 . VAL B 1 281 ? -10.96900 -5.45400  -23.17000 1.000 39.67473  ? 281 VAL B CG2 1 
ATOM   4437 N  N   . LEU B 1 282 ? -12.35400 -5.14200  -18.76600 1.000 34.61627  ? 282 LEU B N   1 
ATOM   4438 C  CA  . LEU B 1 282 ? -12.35700 -4.78900  -17.34900 1.000 37.37735  ? 282 LEU B CA  1 
ATOM   4439 C  C   . LEU B 1 282 ? -12.85400 -5.91500  -16.44500 1.000 38.95175  ? 282 LEU B C   1 
ATOM   4440 O  O   . LEU B 1 282 ? -12.74100 -5.78600  -15.22100 1.000 39.55275  ? 282 LEU B O   1 
ATOM   4441 C  CB  . LEU B 1 282 ? -13.22500 -3.55200  -17.10700 1.000 31.53471  ? 282 LEU B CB  1 
ATOM   4442 C  CG  . LEU B 1 282 ? -12.76200 -2.20900  -17.68100 1.000 35.91346  ? 282 LEU B CG  1 
ATOM   4443 C  CD1 . LEU B 1 282 ? -13.78600 -1.12500  -17.36700 1.000 34.85975  ? 282 LEU B CD1 1 
ATOM   4444 C  CD2 . LEU B 1 282 ? -11.38100 -1.81300  -17.16900 1.000 34.85361  ? 282 LEU B CD2 1 
ATOM   4445 N  N   . GLN B 1 283 ? -13.39100 -6.99900  -17.01200 1.000 38.77365  ? 283 GLN B N   1 
ATOM   4446 C  CA  . GLN B 1 283 ? -14.03400 -8.07900  -16.24900 1.000 41.30579  ? 283 GLN B CA  1 
ATOM   4447 C  C   . GLN B 1 283 ? -15.03000 -7.50400  -15.24700 1.000 38.89572  ? 283 GLN B C   1 
ATOM   4448 O  O   . GLN B 1 283 ? -14.99600 -7.78600  -14.04700 1.000 40.89941  ? 283 GLN B O   1 
ATOM   4449 C  CB  . GLN B 1 283 ? -12.99500 -8.96900  -15.56600 1.000 40.45333  ? 283 GLN B CB  1 
ATOM   4450 C  CG  . GLN B 1 283 ? -11.92800 -9.42300  -16.53500 1.000 44.67443  ? 283 GLN B CG  1 
ATOM   4451 C  CD  . GLN B 1 283 ? -10.99700 -10.42700 -15.93900 1.000 55.34830  ? 283 GLN B CD  1 
ATOM   4452 O  OE1 . GLN B 1 283 ? -10.06000 -10.06900 -15.22100 1.000 59.65402  ? 283 GLN B OE1 1 
ATOM   4453 N  NE2 . GLN B 1 283 ? -11.24800 -11.70600 -16.21900 1.000 60.79802  ? 283 GLN B NE2 1 
ATOM   4454 N  N   . LEU B 1 284 ? -15.91500 -6.66700  -15.76700 1.000 36.00602  ? 284 LEU B N   1 
ATOM   4455 C  CA  . LEU B 1 284 ? -16.89400 -5.94300  -14.97100 1.000 41.12739  ? 284 LEU B CA  1 
ATOM   4456 C  C   . LEU B 1 284 ? -18.02400 -6.86600  -14.52200 1.000 40.31382  ? 284 LEU B C   1 
ATOM   4457 O  O   . LEU B 1 284 ? -18.71800 -7.46000  -15.35300 1.000 40.92825  ? 284 LEU B O   1 
ATOM   4458 C  CB  . LEU B 1 284 ? -17.45300 -4.80000  -15.80500 1.000 39.65462  ? 284 LEU B CB  1 
ATOM   4459 C  CG  . LEU B 1 284 ? -17.79100 -3.49300  -15.11800 1.000 43.28695  ? 284 LEU B CG  1 
ATOM   4460 C  CD1 . LEU B 1 284 ? -16.60500 -3.06700  -14.26400 1.000 41.26757  ? 284 LEU B CD1 1 
ATOM   4461 C  CD2 . LEU B 1 284 ? -18.12700 -2.45700  -16.20100 1.000 38.59611  ? 284 LEU B CD2 1 
ATOM   4462 N  N   . LYS B 1 285 ? -18.24800 -6.86000  -13.22600 1.000 41.38255  ? 285 LYS B N   1 
ATOM   4463 C  CA  . LYS B 1 285 ? -19.43300 -7.57200  -12.73100 1.000 41.11721  ? 285 LYS B CA  1 
ATOM   4464 C  C   . LYS B 1 285 ? -20.53000 -6.52500  -12.61200 1.000 38.83300  ? 285 LYS B C   1 
ATOM   4465 O  O   . LYS B 1 285 ? -20.20500 -5.33300  -12.61200 1.000 39.85987  ? 285 LYS B O   1 
ATOM   4466 C  CB  . LYS B 1 285 ? -19.15400 -8.21700  -11.37400 1.000 43.20069  ? 285 LYS B CB  1 
ATOM   4467 C  CG  . LYS B 1 285 ? -18.01700 -9.22800  -11.35100 1.000 45.31195  ? 285 LYS B CG  1 
ATOM   4468 C  CD  . LYS B 1 285 ? -17.95200 -9.99900  -10.05600 1.000 48.39538  ? 285 LYS B CD  1 
ATOM   4469 C  CE  . LYS B 1 285 ? -16.97500 -11.15300 -10.10000 1.000 51.33400  ? 285 LYS B CE  1 
ATOM   4470 N  NZ  . LYS B 1 285 ? -15.59300 -10.69700 -9.83400  1.000 58.84441  ? 285 LYS B NZ  1 
ATOM   4471 N  N   . ALA B 1 286 ? -21.76500 -6.96800  -12.51300 1.000 42.19371  ? 286 ALA B N   1 
ATOM   4472 C  CA  . ALA B 1 286 ? -22.91300 -6.09500  -12.32400 1.000 41.96794  ? 286 ALA B CA  1 
ATOM   4473 C  C   . ALA B 1 286 ? -23.90800 -6.76200  -11.38000 1.000 45.64737  ? 286 ALA B C   1 
ATOM   4474 O  O   . ALA B 1 286 ? -23.96800 -7.99000  -11.28300 1.000 44.38230  ? 286 ALA B O   1 
ATOM   4475 C  CB  . ALA B 1 286 ? -23.58900 -5.77200  -13.65700 1.000 39.42197  ? 286 ALA B CB  1 
ATOM   4476 N  N   . ALA B 1 287 ? -24.71100 -5.93500  -10.70600 1.000 43.75277  ? 287 ALA B N   1 
ATOM   4477 C  CA  . ALA B 1 287 ? -25.62200 -6.45000  -9.68500  1.000 46.30478  ? 287 ALA B CA  1 
ATOM   4478 C  C   . ALA B 1 287 ? -26.58900 -7.47600  -10.25800 1.000 50.08741  ? 287 ALA B C   1 
ATOM   4479 O  O   . ALA B 1 287 ? -26.92800 -8.45500  -9.58900  1.000 48.67665  ? 287 ALA B O   1 
ATOM   4480 C  CB  . ALA B 1 287 ? -26.39100 -5.29800  -9.03400  1.000 40.73225  ? 287 ALA B CB  1 
ATOM   4481 N  N   . ASP B 1 288 ? -27.04100 -7.28000  -11.49700 1.000 48.29806  ? 288 ASP B N   1 
ATOM   4482 C  CA  . ASP B 1 288 ? -28.04200 -8.16400  -12.08600 1.000 55.02435  ? 288 ASP B CA  1 
ATOM   4483 C  C   . ASP B 1 288 ? -27.49900 -8.97200  -13.26300 1.000 56.43471  ? 288 ASP B C   1 
ATOM   4484 O  O   . ASP B 1 288 ? -28.26500 -9.38700  -14.14000 1.000 59.84158  ? 288 ASP B O   1 
ATOM   4485 C  CB  . ASP B 1 288 ? -29.28100 -7.37400  -12.50700 1.000 48.09658  ? 288 ASP B CB  1 
ATOM   4486 C  CG  . ASP B 1 288 ? -28.97100 -6.29400  -13.52400 1.000 47.01249  ? 288 ASP B CG  1 
ATOM   4487 O  OD1 . ASP B 1 288 ? -27.78000 -6.09600  -13.89100 1.000 42.89566  ? 288 ASP B OD1 1 
ATOM   4488 O  OD2 . ASP B 1 288 ? -29.94200 -5.63500  -13.95300 1.000 49.50484  ? 288 ASP B OD2 1 
ATOM   4489 N  N   . SER B 1 289 ? -26.18300 -9.19400  -13.29800 1.000 53.72552  ? 289 SER B N   1 
ATOM   4490 C  CA  . SER B 1 289 ? -25.60200 -10.18600 -14.20100 1.000 60.85807  ? 289 SER B CA  1 
ATOM   4491 C  C   . SER B 1 289 ? -26.34100 -11.52300 -14.20000 1.000 66.96027  ? 289 SER B C   1 
ATOM   4492 O  O   . SER B 1 289 ? -26.69000 -12.00600 -15.28800 1.000 66.23493  ? 289 SER B O   1 
ATOM   4493 C  CB  . SER B 1 289 ? -24.12900 -10.41200 -13.83900 1.000 58.79967  ? 289 SER B CB  1 
ATOM   4494 O  OG  . SER B 1 289 ? -23.30100 -9.40500  -14.37400 1.000 54.12640  ? 289 SER B OG  1 
ATOM   4495 N  N   . PRO B 1 290 ? -26.60600 -12.17400 -13.04300 1.000 78.85931  ? 290 PRO B N   1 
ATOM   4496 C  CA  . PRO B 1 290 ? -27.16300 -13.53300 -13.10600 1.000 75.25368  ? 290 PRO B CA  1 
ATOM   4497 C  C   . PRO B 1 290 ? -28.50600 -13.60000 -13.82700 1.000 80.64077  ? 290 PRO B C   1 
ATOM   4498 O  O   . PRO B 1 290 ? -28.57200 -14.23700 -14.88300 1.000 84.24308  ? 290 PRO B O   1 
ATOM   4499 C  CB  . PRO B 1 290 ? -27.32000 -13.91500 -11.63100 1.000 74.36036  ? 290 PRO B CB  1 
ATOM   4500 C  CG  . PRO B 1 290 ? -26.35800 -13.04700 -10.90300 1.000 71.99681  ? 290 PRO B CG  1 
ATOM   4501 C  CD  . PRO B 1 290 ? -26.37100 -11.75600 -11.64700 1.000 73.28726  ? 290 PRO B CD  1 
HETATM 4502 FE FE  . FE2 C 2 .   ? -12.68200 5.01200   -45.89600 1.000 44.69971  ? 401 FE2 A FE  1 
HETATM 4503 CO CO  . CO  D 3 .   ? -14.96100 6.71800   -67.83500 1.000 39.62985  ? 402 CO  A CO  1 
HETATM 4504 FE FE  . FE2 E 2 .   ? -32.58600 24.28000  -21.50100 1.000 37.25938  ? 501 FE2 B FE  1 
HETATM 4505 O  O   . HOH F 4 .   ? 1.17400   -9.92500  -41.96600 1.000 63.39836  ? 501 HOH A O   1 
HETATM 4506 O  O   . HOH F 4 .   ? 4.40900   6.19600   -23.40700 1.000 48.41289  ? 502 HOH A O   1 
HETATM 4507 O  O   . HOH F 4 .   ? -5.10200  18.91800  -57.16600 1.000 49.70644  ? 503 HOH A O   1 
HETATM 4508 O  O   . HOH F 4 .   ? -21.70900 15.99600  -44.16800 1.000 44.36795  ? 504 HOH A O   1 
HETATM 4509 O  O   . HOH F 4 .   ? -21.28100 11.65800  -45.40800 1.000 41.57191  ? 505 HOH A O   1 
HETATM 4510 O  O   . HOH F 4 .   ? -8.07600  20.24400  -19.61500 1.000 35.55049  ? 506 HOH A O   1 
HETATM 4511 O  O   . HOH F 4 .   ? -22.24600 25.66100  -49.81000 1.000 40.20599  ? 507 HOH A O   1 
HETATM 4512 O  O   . HOH F 4 .   ? -16.93400 6.93900   -68.59500 1.000 38.00215  ? 508 HOH A O   1 
HETATM 4513 O  O   . HOH F 4 .   ? 2.30200   18.31500  -25.02400 1.000 40.01904  ? 509 HOH A O   1 
HETATM 4514 O  O   . HOH F 4 .   ? 4.75800   22.03500  -42.22700 1.000 49.20951  ? 510 HOH A O   1 
HETATM 4515 O  O   . HOH F 4 .   ? -20.13000 18.32300  -39.68700 1.000 34.68490  ? 511 HOH A O   1 
HETATM 4516 O  O   . HOH F 4 .   ? 3.73800   8.92700   -56.64900 1.000 50.49321  ? 512 HOH A O   1 
HETATM 4517 O  O   . HOH F 4 .   ? 3.64000   16.80100  -14.93500 1.000 47.75670  ? 513 HOH A O   1 
HETATM 4518 O  O   . HOH F 4 .   ? 6.13000   12.53100  -35.21400 1.000 46.61686  ? 514 HOH A O   1 
HETATM 4519 O  O   . HOH F 4 .   ? -2.52100  11.62000  -57.56400 1.000 45.19783  ? 515 HOH A O   1 
HETATM 4520 O  O   . HOH F 4 .   ? -7.84700  1.42400   -22.94700 1.000 35.45490  ? 516 HOH A O   1 
HETATM 4521 O  O   . HOH F 4 .   ? 4.00600   -4.14500  -30.41200 1.000 49.43033  ? 517 HOH A O   1 
HETATM 4522 O  O   . HOH F 4 .   ? -28.12900 18.25400  -43.83600 1.000 41.69326  ? 518 HOH A O   1 
HETATM 4523 O  O   . HOH F 4 .   ? 1.88600   22.03700  -34.23600 1.000 42.42153  ? 519 HOH A O   1 
HETATM 4524 O  O   . HOH F 4 .   ? -12.78800 24.60300  -39.00800 1.000 35.90771  ? 520 HOH A O   1 
HETATM 4525 O  O   . HOH F 4 .   ? -6.14600  2.73000   -16.37800 1.000 40.32014  ? 521 HOH A O   1 
HETATM 4526 O  O   . HOH F 4 .   ? -15.01800 19.99700  -30.82300 1.000 25.38091  ? 522 HOH A O   1 
HETATM 4527 O  O   . HOH F 4 .   ? -9.02200  22.86300  -32.62400 1.000 35.85738  ? 523 HOH A O   1 
HETATM 4528 O  O   . HOH F 4 .   ? 9.83000   7.32100   -30.36500 1.000 47.48588  ? 524 HOH A O   1 
HETATM 4529 O  O   . HOH F 4 .   ? -11.93200 15.70100  -59.01400 1.000 43.78479  ? 525 HOH A O   1 
HETATM 4530 O  O   . HOH F 4 .   ? -9.08700  7.74900   -22.20600 1.000 28.74370  ? 526 HOH A O   1 
HETATM 4531 O  O   . HOH F 4 .   ? -18.16500 19.26200  -44.42400 1.000 41.86821  ? 527 HOH A O   1 
HETATM 4532 O  O   . HOH F 4 .   ? -11.84300 -2.68900  -32.90600 1.000 45.11493  ? 528 HOH A O   1 
HETATM 4533 O  O   . HOH F 4 .   ? -2.42800  25.56800  -37.49200 1.000 41.43966  ? 529 HOH A O   1 
HETATM 4534 O  O   . HOH F 4 .   ? -7.56000  20.28100  -23.19300 1.000 34.55756  ? 530 HOH A O   1 
HETATM 4535 O  O   . HOH F 4 .   ? -13.77700 6.83600   -35.62400 1.000 33.40935  ? 531 HOH A O   1 
HETATM 4536 O  O   . HOH F 4 .   ? 4.03200   6.85300   -43.59000 1.000 41.88720  ? 532 HOH A O   1 
HETATM 4537 O  O   . HOH F 4 .   ? -8.75300  14.02700  -23.53000 1.000 22.33907  ? 533 HOH A O   1 
HETATM 4538 O  O   . HOH F 4 .   ? -15.30200 8.74800   -66.79300 1.000 40.81141  ? 534 HOH A O   1 
HETATM 4539 O  O   . HOH F 4 .   ? -4.27100  17.85900  -53.44800 1.000 40.28652  ? 535 HOH A O   1 
HETATM 4540 O  O   . HOH F 4 .   ? -14.84900 6.12100   -26.09100 1.000 32.54027  ? 536 HOH A O   1 
HETATM 4541 O  O   . HOH F 4 .   ? -4.44500  3.80300   -31.48700 1.000 39.12764  ? 537 HOH A O   1 
HETATM 4542 O  O   . HOH F 4 .   ? -14.62300 10.36800  -31.77400 1.000 23.80542  ? 538 HOH A O   1 
HETATM 4543 O  O   . HOH F 4 .   ? -10.43600 -1.68100  -30.07300 1.000 39.50741  ? 539 HOH A O   1 
HETATM 4544 O  O   . HOH F 4 .   ? -10.32100 13.12700  -58.71000 1.000 39.39759  ? 540 HOH A O   1 
HETATM 4545 O  O   . HOH F 4 .   ? -22.87700 7.27100   -62.71700 1.000 47.95311  ? 541 HOH A O   1 
HETATM 4546 O  O   . HOH F 4 .   ? -0.07100  17.35600  -15.95900 1.000 43.63103  ? 542 HOH A O   1 
HETATM 4547 O  O   . HOH F 4 .   ? -15.31900 29.04500  -29.64200 1.000 42.37601  ? 543 HOH A O   1 
HETATM 4548 O  O   . HOH F 4 .   ? -20.44500 20.63800  -36.80700 1.000 26.60740  ? 544 HOH A O   1 
HETATM 4549 O  O   . HOH F 4 .   ? -7.70800  22.10200  -30.40500 1.000 37.71091  ? 545 HOH A O   1 
HETATM 4550 O  O   . HOH F 4 .   ? -13.18000 15.27700  -6.85100  1.000 43.88390  ? 546 HOH A O   1 
HETATM 4551 O  O   . HOH F 4 .   ? -9.31900  9.46700   -27.42600 1.000 25.49709  ? 547 HOH A O   1 
HETATM 4552 O  O   . HOH F 4 .   ? -14.31700 22.46800  -37.40300 1.000 33.31827  ? 548 HOH A O   1 
HETATM 4553 O  O   . HOH F 4 .   ? -14.82800 10.62900  -46.27100 1.000 36.00911  ? 549 HOH A O   1 
HETATM 4554 O  O   . HOH F 4 .   ? -10.956   5.695     -68.168   1.000 43.09784  ? 550 HOH A O   1 
HETATM 4555 O  O   . HOH F 4 .   ? -19.78800 21.54500  -14.47100 1.000 41.10136  ? 551 HOH A O   1 
HETATM 4556 O  O   . HOH F 4 .   ? -8.64500  22.20500  -23.95000 1.000 39.24352  ? 552 HOH A O   1 
HETATM 4557 O  O   . HOH F 4 .   ? -8.98800  14.84000  -60.28200 1.000 46.24081  ? 553 HOH A O   1 
HETATM 4558 O  O   . HOH F 4 .   ? -19.24300 23.00500  -8.34400  1.000 37.16224  ? 554 HOH A O   1 
HETATM 4559 O  O   . HOH F 4 .   ? -18.70100 17.59100  -13.51400 1.000 32.61409  ? 555 HOH A O   1 
HETATM 4560 O  O   . HOH F 4 .   ? 3.65500   16.67200  -27.29300 1.000 37.35315  ? 556 HOH A O   1 
HETATM 4561 O  O   . HOH F 4 .   ? -23.93900 13.20400  -46.33000 1.000 48.32048  ? 557 HOH A O   1 
HETATM 4562 O  O   . HOH F 4 .   ? -21.02300 27.98500  -38.74800 1.000 42.24823  ? 558 HOH A O   1 
HETATM 4563 O  O   . HOH F 4 .   ? -13.79100 -11.05300 -26.27200 1.000 49.24530  ? 559 HOH A O   1 
HETATM 4564 O  O   . HOH F 4 .   ? -22.26300 8.33800   -47.45300 1.000 48.33044  ? 560 HOH A O   1 
HETATM 4565 O  O   . HOH F 4 .   ? 1.44900   9.51500   -10.30600 1.000 50.91072  ? 561 HOH A O   1 
HETATM 4566 O  O   . HOH F 4 .   ? -19.45800 21.59100  -34.33200 1.000 22.59595  ? 562 HOH A O   1 
HETATM 4567 O  O   . HOH F 4 .   ? -10.61600 5.73000   -44.62400 1.000 47.26995  ? 563 HOH A O   1 
HETATM 4568 O  O   . HOH F 4 .   ? -19.66800 3.89100   -62.35100 1.000 31.91862  ? 564 HOH A O   1 
HETATM 4569 O  O   . HOH F 4 .   ? -17.57400 23.04800  -43.78000 1.000 40.78249  ? 565 HOH A O   1 
HETATM 4570 O  O   . HOH F 4 .   ? -14.92400 2.22300   -63.13100 1.000 32.61719  ? 566 HOH A O   1 
HETATM 4571 O  O   . HOH F 4 .   ? -25.65000 8.05300   -53.30200 1.000 44.42190  ? 567 HOH A O   1 
HETATM 4572 O  O   . HOH F 4 .   ? -19.80800 19.23400  -42.48700 1.000 35.11350  ? 568 HOH A O   1 
HETATM 4573 O  O   . HOH F 4 .   ? -13.98200 4.05500   -64.94200 1.000 38.81344  ? 569 HOH A O   1 
HETATM 4574 O  O   . HOH F 4 .   ? 7.16800   4.85800   -23.67400 1.000 50.66375  ? 570 HOH A O   1 
HETATM 4575 O  O   . HOH F 4 .   ? -16.384   2.239     -59.582   1.000 34.75171  ? 571 HOH A O   1 
HETATM 4576 O  O   . HOH F 4 .   ? -17.00700 19.14000  -56.80700 1.000 47.50595  ? 572 HOH A O   1 
HETATM 4577 O  O   . HOH F 4 .   ? 2.31300   18.01000  -56.34700 1.000 51.79495  ? 573 HOH A O   1 
HETATM 4578 O  O   . HOH F 4 .   ? 3.036     21.614    -21.805   1.000 48.84288  ? 574 HOH A O   1 
HETATM 4579 O  O   . HOH F 4 .   ? -20.65000 6.32500   -47.98200 1.000 40.38888  ? 575 HOH A O   1 
HETATM 4580 O  O   . HOH F 4 .   ? -6.33600  -3.25500  -21.86800 1.000 46.55880  ? 576 HOH A O   1 
HETATM 4581 O  O   . HOH F 4 .   ? -17.95500 8.48700   -38.71900 1.000 35.21003  ? 577 HOH A O   1 
HETATM 4582 O  O   . HOH F 4 .   ? -10.30100 7.30100   -26.04900 1.000 30.09806  ? 578 HOH A O   1 
HETATM 4583 O  O   . HOH F 4 .   ? -15.57800 8.64800   -37.00100 1.000 38.11684  ? 579 HOH A O   1 
HETATM 4584 O  O   . HOH F 4 .   ? 2.40800   27.25400  -41.30200 1.000 55.12735  ? 580 HOH A O   1 
HETATM 4585 O  O   . HOH F 4 .   ? -7.54500  19.36600  -29.37300 1.000 32.92282  ? 581 HOH A O   1 
HETATM 4586 O  O   . HOH F 4 .   ? -12.45200 23.37500  -41.92600 1.000 43.08570  ? 582 HOH A O   1 
HETATM 4587 O  O   . HOH F 4 .   ? 3.28700   -0.15900  -25.59700 1.000 44.75280  ? 583 HOH A O   1 
HETATM 4588 O  O   . HOH F 4 .   ? -17.15900 11.60900  -44.00800 1.000 35.70928  ? 584 HOH A O   1 
HETATM 4589 O  O   . HOH F 4 .   ? -13.63100 3.98800   -36.77500 1.000 43.45845  ? 585 HOH A O   1 
HETATM 4590 O  O   . HOH F 4 .   ? -14.67000 24.82800  -42.47500 1.000 43.06928  ? 586 HOH A O   1 
HETATM 4591 O  O   . HOH F 4 .   ? -2.14300  20.35000  -26.21900 1.000 37.38623  ? 587 HOH A O   1 
HETATM 4592 O  O   . HOH F 4 .   ? -9.74900  -13.63200 -25.74300 1.000 57.07303  ? 588 HOH A O   1 
HETATM 4593 O  O   . HOH F 4 .   ? -13.00100 11.09400  -44.86800 1.000 39.50199  ? 589 HOH A O   1 
HETATM 4594 O  O   . HOH F 4 .   ? -0.98600  19.65800  -16.70100 1.000 49.07223  ? 590 HOH A O   1 
HETATM 4595 O  O   . HOH F 4 .   ? -5.04700  20.74300  -29.87000 1.000 44.42136  ? 591 HOH A O   1 
HETATM 4596 O  O   . HOH F 4 .   ? -23.79400 28.62800  -22.95900 1.000 51.68811  ? 592 HOH A O   1 
HETATM 4597 O  O   . HOH F 4 .   ? -19.31200 24.30800  -33.72000 1.000 33.73666  ? 593 HOH A O   1 
HETATM 4598 O  O   . HOH F 4 .   ? 3.03800   11.43200  -26.16300 1.000 38.26256  ? 594 HOH A O   1 
HETATM 4599 O  O   . HOH F 4 .   ? 4.12400   -4.35200  -50.32800 1.000 60.19368  ? 595 HOH A O   1 
HETATM 4600 O  O   . HOH F 4 .   ? -16.408   -15.278   -31.526   1.000 50.66578  ? 596 HOH A O   1 
HETATM 4601 O  O   . HOH F 4 .   ? -25.16500 14.19100  -55.98700 1.000 51.45659  ? 597 HOH A O   1 
HETATM 4602 O  O   . HOH F 4 .   ? -24.30600 16.35500  -56.51400 1.000 52.55058  ? 598 HOH A O   1 
HETATM 4603 O  O   . HOH F 4 .   ? -13.96900 8.17400   -69.54500 1.000 35.47157  ? 599 HOH A O   1 
HETATM 4604 O  O   . HOH F 4 .   ? -13.08700 2.99000   -44.28200 1.000 35.23070  ? 600 HOH A O   1 
HETATM 4605 O  O   . HOH F 4 .   ? -24.50100 24.82000  -41.54100 1.000 31.90662  ? 601 HOH A O   1 
HETATM 4606 O  O   . HOH F 4 .   ? -13.08800 1.95100   -37.68100 1.000 44.25159  ? 602 HOH A O   1 
HETATM 4607 O  O   . HOH F 4 .   ? 2.64100   25.66500  -39.26900 1.000 53.37119  ? 603 HOH A O   1 
HETATM 4608 O  O   . HOH G 4 .   ? -39.48900 5.03800   -32.17700 1.000 47.94838  ? 601 HOH B O   1 
HETATM 4609 O  O   . HOH G 4 .   ? -21.24800 -10.14200 -13.44500 1.000 49.97518  ? 602 HOH B O   1 
HETATM 4610 O  O   . HOH G 4 .   ? -15.67300 -8.76900  -25.89200 1.000 42.18462  ? 603 HOH B O   1 
HETATM 4611 O  O   . HOH G 4 .   ? -21.04300 17.16200  -4.94100  1.000 34.80274  ? 604 HOH B O   1 
HETATM 4612 O  O   . HOH G 4 .   ? -24.65500 16.97700  -22.06300 1.000 29.21878  ? 605 HOH B O   1 
HETATM 4613 O  O   . HOH G 4 .   ? -48.08600 7.59200   -12.64600 1.000 40.55074  ? 606 HOH B O   1 
HETATM 4614 O  O   . HOH G 4 .   ? -42.51800 29.90300  -15.37600 1.000 38.54440  ? 607 HOH B O   1 
HETATM 4615 O  O   . HOH G 4 .   ? -16.02300 9.88500   -12.70700 1.000 35.78679  ? 608 HOH B O   1 
HETATM 4616 O  O   . HOH G 4 .   ? -13.56000 9.80700   -20.69700 1.000 38.39370  ? 609 HOH B O   1 
HETATM 4617 O  O   . HOH G 4 .   ? -9.19800  -7.79500  -33.69900 1.000 47.28056  ? 610 HOH B O   1 
HETATM 4618 O  O   . HOH G 4 .   ? -30.67400 19.82100  -33.01200 1.000 37.48537  ? 611 HOH B O   1 
HETATM 4619 O  O   . HOH G 4 .   ? -21.76100 15.39900  -7.02200  1.000 37.50006  ? 612 HOH B O   1 
HETATM 4620 O  O   . HOH G 4 .   ? -47.50500 22.62100  -5.97700  1.000 50.83627  ? 613 HOH B O   1 
HETATM 4621 O  O   . HOH G 4 .   ? -28.52700 22.76400  -40.33900 1.000 35.40488  ? 614 HOH B O   1 
HETATM 4622 O  O   . HOH G 4 .   ? -32.90500 22.08900  -20.42600 1.000 39.78646  ? 615 HOH B O   1 
HETATM 4623 O  O   . HOH G 4 .   ? -35.06100 7.73600   -33.29000 1.000 37.28350  ? 616 HOH B O   1 
HETATM 4624 O  O   . HOH G 4 .   ? -13.37600 27.18800  -6.48400  1.000 49.50606  ? 617 HOH B O   1 
HETATM 4625 O  O   . HOH G 4 .   ? -49.06000 27.27600  -10.43200 1.000 48.95407  ? 618 HOH B O   1 
HETATM 4626 O  O   . HOH G 4 .   ? -10.00500 21.55000  -12.40500 1.000 34.26715  ? 619 HOH B O   1 
HETATM 4627 O  O   . HOH G 4 .   ? -20.25500 30.12700  -7.80900  1.000 44.08680  ? 620 HOH B O   1 
HETATM 4628 O  O   . HOH G 4 .   ? -26.49500 6.19400   -31.05500 1.000 25.46241  ? 621 HOH B O   1 
HETATM 4629 O  O   . HOH G 4 .   ? -25.27200 25.63700  -30.45900 1.000 36.60121  ? 622 HOH B O   1 
HETATM 4630 O  O   . HOH G 4 .   ? -47.70700 17.37200  -24.18200 1.000 37.60497  ? 623 HOH B O   1 
HETATM 4631 O  O   . HOH G 4 .   ? -49.19500 23.02000  -19.52000 1.000 39.57407  ? 624 HOH B O   1 
HETATM 4632 O  O   . HOH G 4 .   ? -24.58200 1.75200   -7.16500  1.000 35.66682  ? 625 HOH B O   1 
HETATM 4633 O  O   . HOH G 4 .   ? -25.83000 -2.36800  -27.08300 1.000 39.83804  ? 626 HOH B O   1 
HETATM 4634 O  O   . HOH G 4 .   ? -39.58600 14.50700  -9.72200  1.000 33.31888  ? 627 HOH B O   1 
HETATM 4635 O  O   . HOH G 4 .   ? -31.75200 26.57600  -33.72700 1.000 43.31637  ? 628 HOH B O   1 
HETATM 4636 O  O   . HOH G 4 .   ? -12.29300 4.11900   -11.62100 1.000 36.13402  ? 629 HOH B O   1 
HETATM 4637 O  O   . HOH G 4 .   ? -36.09400 13.72000  -36.37900 1.000 44.14460  ? 630 HOH B O   1 
HETATM 4638 O  O   . HOH G 4 .   ? -16.77700 11.88300  -21.42700 1.000 26.41229  ? 631 HOH B O   1 
HETATM 4639 O  O   . HOH G 4 .   ? -31.99600 20.74600  -28.68600 1.000 36.89302  ? 632 HOH B O   1 
HETATM 4640 O  O   . HOH G 4 .   ? -15.12700 5.70900   -22.27300 1.000 35.91856  ? 633 HOH B O   1 
HETATM 4641 O  O   . HOH G 4 .   ? -45.18800 10.40900  -6.77200  1.000 46.87632  ? 634 HOH B O   1 
HETATM 4642 O  O   . HOH G 4 .   ? -28.48200 12.16200  -36.34600 1.000 27.81382  ? 635 HOH B O   1 
HETATM 4643 O  O   . HOH G 4 .   ? -49.61900 26.73500  -18.96400 1.000 39.72109  ? 636 HOH B O   1 
HETATM 4644 O  O   . HOH G 4 .   ? -17.37600 5.85300   -17.50100 1.000 31.39213  ? 637 HOH B O   1 
HETATM 4645 O  O   . HOH G 4 .   ? -21.62000 -7.45900  -22.31600 1.000 43.28341  ? 638 HOH B O   1 
HETATM 4646 O  O   . HOH G 4 .   ? -37.59300 -0.29000  -19.67100 1.000 40.72404  ? 639 HOH B O   1 
HETATM 4647 O  O   . HOH G 4 .   ? -21.50300 2.55900   -21.51100 1.000 24.58341  ? 640 HOH B O   1 
HETATM 4648 O  O   . HOH G 4 .   ? -12.07700 28.50900  -12.75200 1.000 51.82931  ? 641 HOH B O   1 
HETATM 4649 O  O   . HOH G 4 .   ? -34.33400 19.45600  -25.68800 1.000 33.10755  ? 642 HOH B O   1 
HETATM 4650 O  O   . HOH G 4 .   ? -49.57400 25.40900  -26.67600 1.000 41.72574  ? 643 HOH B O   1 
HETATM 4651 O  O   . HOH G 4 .   ? -30.21900 15.02600  -34.62200 1.000 30.24243  ? 644 HOH B O   1 
HETATM 4652 O  O   . HOH G 4 .   ? -23.17200 12.73700  -24.67900 1.000 25.18173  ? 645 HOH B O   1 
HETATM 4653 O  O   . HOH G 4 .   ? -37.44700 4.63300   -10.48500 1.000 42.92563  ? 646 HOH B O   1 
HETATM 4654 O  O   . HOH G 4 .   ? -13.78800 10.97200  -8.62700  1.000 42.62692  ? 647 HOH B O   1 
HETATM 4655 O  O   . HOH G 4 .   ? -38.73000 2.29000   -1.29800  1.000 53.87258  ? 648 HOH B O   1 
HETATM 4656 O  O   . HOH G 4 .   ? -24.95600 12.84700  -1.00300  1.000 33.88449  ? 649 HOH B O   1 
HETATM 4657 O  O   . HOH G 4 .   ? -31.44300 -1.84800  -14.53000 1.000 41.19031  ? 650 HOH B O   1 
HETATM 4658 O  O   . HOH G 4 .   ? -22.03900 8.31500   -19.50400 1.000 24.78038  ? 651 HOH B O   1 
HETATM 4659 O  O   . HOH G 4 .   ? -52.05700 19.22100  -25.87900 1.000 49.77582  ? 652 HOH B O   1 
HETATM 4660 O  O   . HOH G 4 .   ? -18.84000 14.94900  -2.46000  1.000 45.49550  ? 653 HOH B O   1 
HETATM 4661 O  O   . HOH G 4 .   ? -46.89600 26.35700  -26.39000 1.000 37.45592  ? 654 HOH B O   1 
HETATM 4662 O  O   . HOH G 4 .   ? -21.30700 -8.24900  -16.09100 1.000 41.35492  ? 655 HOH B O   1 
HETATM 4663 O  O   . HOH G 4 .   ? -29.88500 -3.85900  -16.13500 1.000 35.16876  ? 656 HOH B O   1 
HETATM 4664 O  O   . HOH G 4 .   ? -32.20500 16.45400  -35.48100 1.000 39.01489  ? 657 HOH B O   1 
HETATM 4665 O  O   . HOH G 4 .   ? -19.66100 9.17400   -18.58800 1.000 27.66328  ? 658 HOH B O   1 
HETATM 4666 O  O   . HOH G 4 .   ? -32.72200 8.50700   -32.83000 1.000 34.98057  ? 659 HOH B O   1 
HETATM 4667 O  O   . HOH G 4 .   ? -40.38400 10.53200  -30.61200 1.000 46.19505  ? 660 HOH B O   1 
HETATM 4668 O  O   . HOH G 4 .   ? -30.77800 28.41700  -28.32100 1.000 36.67030  ? 661 HOH B O   1 
HETATM 4669 O  O   . HOH G 4 .   ? -31.92500 29.66000  -33.16600 1.000 45.20947  ? 662 HOH B O   1 
HETATM 4670 O  O   . HOH G 4 .   ? -7.32300  -7.26800  -23.97000 1.000 48.09487  ? 663 HOH B O   1 
HETATM 4671 O  O   . HOH G 4 .   ? -25.74100 17.58400  -24.72000 1.000 32.77093  ? 664 HOH B O   1 
HETATM 4672 O  O   . HOH G 4 .   ? -30.77800 1.00700   -23.47700 1.000 41.85528  ? 665 HOH B O   1 
HETATM 4673 O  O   . HOH G 4 .   ? -34.14100 22.01500  -26.71900 1.000 32.48366  ? 666 HOH B O   1 
HETATM 4674 O  O   . HOH G 4 .   ? -42.23300 22.07300  -2.89900  1.000 44.22663  ? 667 HOH B O   1 
HETATM 4675 O  O   . HOH G 4 .   ? -23.83500 25.00500  -4.89400  1.000 42.83446  ? 668 HOH B O   1 
HETATM 4676 O  O   . HOH G 4 .   ? -40.70000 27.74000  -4.49500  1.000 44.18607  ? 669 HOH B O   1 
HETATM 4677 O  O   . HOH G 4 .   ? -24.74600 19.54000  -20.57000 1.000 37.32827  ? 670 HOH B O   1 
HETATM 4678 O  O   . HOH G 4 .   ? -31.16900 0.97200   -33.22400 1.000 52.21791  ? 671 HOH B O   1 
HETATM 4679 O  O   . HOH G 4 .   ? -33.90900 21.63000  -39.96300 1.000 42.05032  ? 672 HOH B O   1 
HETATM 4680 O  O   . HOH G 4 .   ? -45.11900 26.15900  -32.43700 1.000 47.44950  ? 673 HOH B O   1 
HETATM 4681 O  O   . HOH G 4 .   ? -17.34500 8.81900   -19.84800 1.000 38.68027  ? 674 HOH B O   1 
HETATM 4682 O  O   . HOH G 4 .   ? -30.38100 27.47100  -31.16900 1.000 40.06729  ? 675 HOH B O   1 
HETATM 4683 O  O   . HOH G 4 .   ? -34.86200 29.38500  -14.45200 1.000 36.29829  ? 676 HOH B O   1 
HETATM 4684 O  O   . HOH G 4 .   ? -36.20600 34.85700  -24.56700 1.000 41.03133  ? 677 HOH B O   1 
HETATM 4685 O  O   . HOH G 4 .   ? -37.67600 30.34500  3.64600   1.000 33.44778  ? 678 HOH B O   1 
HETATM 4686 O  O   . HOH G 4 .   ? -39.62300 1.02100   -25.76200 1.000 39.54356  ? 679 HOH B O   1 
HETATM 4687 O  O   . HOH G 4 .   ? -18.83100 -8.33800  -18.12300 1.000 43.45530  ? 680 HOH B O   1 
HETATM 4688 O  O   . HOH G 4 .   ? -25.05600 1.92000   -4.00300  1.000 41.20248  ? 681 HOH B O   1 
HETATM 4689 O  O   . HOH G 4 .   ? -27.57100 9.42700   -35.79400 1.000 28.67441  ? 682 HOH B O   1 
HETATM 4690 O  O   . HOH G 4 .   ? -23.26900 32.08100  -18.38200 1.000 54.54927  ? 683 HOH B O   1 
HETATM 4691 O  O   . HOH G 4 .   ? -25.87100 -4.68700  -36.79400 1.000 47.26765  ? 684 HOH B O   1 
HETATM 4692 O  O   . HOH G 4 .   ? -28.64200 2.45300   -24.65300 1.000 32.82862  ? 685 HOH B O   1 
HETATM 4693 O  O   . HOH G 4 .   ? -46.37100 0.87300   -23.86300 1.000 50.66099  ? 686 HOH B O   1 
HETATM 4694 O  O   . HOH G 4 .   ? -24.55000 -2.19600  -24.97800 1.000 36.46799  ? 687 HOH B O   1 
HETATM 4695 O  O   . HOH G 4 .   ? -46.21600 29.73600  -30.90400 1.000 44.81973  ? 688 HOH B O   1 
HETATM 4696 O  O   . HOH G 4 .   ? -47.60100 28.74800  -29.16100 1.000 47.49656  ? 689 HOH B O   1 
HETATM 4697 O  O   . HOH G 4 .   ? -47.65300 26.25900  -29.80500 1.000 44.15663  ? 690 HOH B O   1 
HETATM 4698 O  O   . HOH G 4 .   ? -11.54500 0.98300   -7.66200  1.000 47.14587  ? 691 HOH B O   1 
HETATM 4699 O  O   . HOH G 4 .   ? -22.70000 1.77300   -4.24600  1.000 40.92779  ? 692 HOH B O   1 
HETATM 4700 O  O   . HOH G 4 .   ? -30.97200 1.52500   -27.25200 1.000 43.88941  ? 693 HOH B O   1 
HETATM 4701 O  O   . HOH G 4 .   ? -23.99100 -4.68600  -21.68500 1.000 43.23057  ? 694 HOH B O   1 
HETATM 4702 O  O   . HOH G 4 .   ? -30.06400 22.56000  0.54100   1.000 45.44053  ? 695 HOH B O   1 
HETATM 4703 O  O   . HOH G 4 .   ? -27.96900 0.52300   -11.14900 1.000 38.15424  ? 696 HOH B O   1 
HETATM 4704 O  O   . HOH G 4 .   ? -20.89800 26.52500  -33.09100 1.000 46.37181  ? 697 HOH B O   1 
HETATM 4705 O  O   . HOH G 4 .   ? -13.74600 28.46300  -14.84200 1.000 52.07534  ? 698 HOH B O   1 
HETATM 4706 O  O   . HOH G 4 .   ? -28.49100 7.17100   -37.05900 1.000 34.50846  ? 699 HOH B O   1 
HETATM 4707 O  O   . HOH G 4 .   ? -52.42700 8.45500   -18.39200 1.000 43.24115  ? 700 HOH B O   1 
HETATM 4708 O  O   . HOH G 4 .   ? -29.04700 -0.87700  -36.47900 1.000 50.24665  ? 701 HOH B O   1 
HETATM 4709 O  O   . HOH G 4 .   ? -32.44700 2.72200   -28.73300 1.000 42.24873  ? 702 HOH B O   1 
HETATM 4710 O  O   . HOH G 4 .   ? -26.09500 19.94400  -26.76400 1.000 33.41392  ? 703 HOH B O   1 
HETATM 4711 O  O   . HOH G 4 .   ? -51.27800 19.96100  -28.04600 1.000 52.80760  ? 704 HOH B O   1 
HETATM 4712 O  O   . HOH G 4 .   ? -55.34400 21.84500  -23.44400 1.000 50.62808  ? 705 HOH B O   1 
HETATM 4713 O  O   . HOH G 4 .   ? -23.33500 25.69300  -32.59200 1.000 35.10776  ? 706 HOH B O   1 
HETATM 4714 O  O   . HOH G 4 .   ? -35.17600 23.76800  -39.49100 1.000 47.55898  ? 707 HOH B O   1 
HETATM 4715 O  O   . HOH G 4 .   ? -28.63600 11.58100  2.48500   1.000 44.09394  ? 708 HOH B O   1 
HETATM 4716 O  O   . HOH G 4 .   ? -31.74700 18.65000  -26.87800 1.000 38.00396  ? 709 HOH B O   1 
HETATM 4717 O  O   . HOH G 4 .   ? -34.499   31.220    -1.330    1.000 45.22887  ? 710 HOH B O   1 
HETATM 4718 O  O   . HOH G 4 .   ? -28.59600 -1.37900  -34.07000 1.000 47.54732  ? 711 HOH B O   1 
HETATM 4719 O  O   . HOH G 4 .   ? -30.30800 24.52700  -19.95400 1.000 42.55007  ? 712 HOH B O   1 
HETATM 4720 O  O   . HOH G 4 .   ? -33.58500 24.41900  -19.18000 1.000 46.45348  ? 713 HOH B O   1 
HETATM 4721 O  O   . HOH G 4 .   ? -17.41800 6.95300   -22.11300 1.000 38.10897  ? 714 HOH B O   1 
HETATM 4722 O  O   . HOH G 4 .   ? -48.14200 21.86200  -31.35000 1.000 47.96873  ? 715 HOH B O   1 
HETATM 4723 O  O   . HOH G 4 .   ? -34.528   34.171    -1.406    1.000 41.09727  ? 716 HOH B O   1 
HETATM 4724 O  O   . HOH G 4 .   ? -24.187   28.582    -32.772   1.000 44.38625  ? 717 HOH B O   1 
HETATM 4725 O  O   . HOH G 4 .   ? -50.10600 22.39800  -29.52000 1.000 49.48633  ? 718 HOH B O   1 
HETATM 4726 O  O   . HOH G 4 .   ? -50.14700 25.21200  -28.99700 1.000 48.05584  ? 719 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 6   ? 0.78715 1.05873 0.37344 -0.22205 0.12299  0.04468  6   LYS A N   
2    C CA  . LYS A 6   ? 0.84073 1.08219 0.45980 -0.19690 0.11183  0.03453  6   LYS A CA  
3    C C   . LYS A 6   ? 0.78117 1.01093 0.44312 -0.18163 0.11877  0.02605  6   LYS A C   
4    O O   . LYS A 6   ? 0.75065 1.00173 0.42139 -0.17628 0.13734  0.00409  6   LYS A O   
5    C CB  . LYS A 6   ? 0.88566 1.13209 0.49152 -0.18403 0.11673  0.00390  6   LYS A CB  
6    C CG  . LYS A 6   ? 0.80208 1.02173 0.44198 -0.15956 0.10772  -0.00762 6   LYS A CG  
7    C CD  . LYS A 6   ? 0.83243 1.05416 0.45750 -0.14952 0.11329  -0.03828 6   LYS A CD  
8    C CE  . LYS A 6   ? 0.73960 0.93631 0.39598 -0.12922 0.10298  -0.04553 6   LYS A CE  
9    N NZ  . LYS A 6   ? 0.73121 0.92520 0.37454 -0.11995 0.10932  -0.07626 6   LYS A NZ  
10   N N   . PRO A 7   ? 0.74857 0.94483 0.43653 -0.17379 0.10366  0.04290  7   PRO A N   
11   C CA  . PRO A 7   ? 0.74836 0.92907 0.47044 -0.16305 0.10829  0.03657  7   PRO A CA  
12   C C   . PRO A 7   ? 0.71730 0.90625 0.45690 -0.14244 0.12022  0.00360  7   PRO A C   
13   O O   . PRO A 7   ? 0.71689 0.89997 0.45593 -0.12789 0.11677  -0.01007 7   PRO A O   
14   C CB  . PRO A 7   ? 0.74437 0.88344 0.48516 -0.15284 0.08983  0.05553  7   PRO A CB  
15   C CG  . PRO A 7   ? 0.77214 0.91036 0.49049 -0.16404 0.07468  0.08074  7   PRO A CG  
16   C CD  . PRO A 7   ? 0.78858 0.96008 0.47676 -0.17157 0.08174  0.06599  7   PRO A CD  
17   N N   . GLN A 8   ? 0.69336 0.89632 0.44928 -0.14266 0.13278  -0.00714 8   GLN A N   
18   C CA  . GLN A 8   ? 0.67134 0.88415 0.44625 -0.12366 0.14345  -0.03546 8   GLN A CA  
19   C C   . GLN A 8   ? 0.65530 0.84172 0.46009 -0.11307 0.13765  -0.03629 8   GLN A C   
20   O O   . GLN A 8   ? 0.69093 0.85292 0.50073 -0.12175 0.12839  -0.01749 8   GLN A O   
21   C CB  . GLN A 8   ? 0.65812 0.91574 0.43050 -0.13035 0.16306  -0.04841 8   GLN A CB  
22   C CG  . GLN A 8   ? 0.66619 0.95126 0.40401 -0.13799 0.17342  -0.05492 8   GLN A CG  
23   C CD  . GLN A 8   ? 0.68425 0.96122 0.41354 -0.11800 0.17509  -0.08040 8   GLN A CD  
24   O OE1 . GLN A 8   ? 0.65767 0.92968 0.41196 -0.09683 0.17845  -0.09963 8   GLN A OE1 
25   N NE2 . GLN A 8   ? 0.71026 0.97930 0.40698 -0.12462 0.16801  -0.07747 8   GLN A NE2 
26   N N   . LEU A 9   ? 0.61113 0.79939 0.43292 -0.09423 0.14274  -0.05866 9   LEU A N   
27   C CA  . LEU A 9   ? 0.63720 0.80572 0.48306 -0.08573 0.13888  -0.06236 9   LEU A CA  
28   C C   . LEU A 9   ? 0.62438 0.80977 0.47960 -0.10282 0.14310  -0.05538 9   LEU A C   
29   O O   . LEU A 9   ? 0.58127 0.80766 0.44097 -0.10773 0.15541  -0.06332 9   LEU A O   
30   C CB  . LEU A 9   ? 0.62734 0.80010 0.48682 -0.06461 0.14346  -0.08596 9   LEU A CB  
31   C CG  . LEU A 9   ? 0.59851 0.74499 0.45630 -0.04814 0.13601  -0.09144 9   LEU A CG  
32   C CD1 . LEU A 9   ? 0.58742 0.74300 0.45284 -0.03155 0.14195  -0.11365 9   LEU A CD1 
33   C CD2 . LEU A 9   ? 0.55016 0.66105 0.41900 -0.04295 0.12619  -0.08226 9   LEU A CD2 
34   N N   . GLN A 10  ? 0.60503 0.75883 0.46408 -0.11169 0.13307  -0.04090 10  GLN A N   
35   C CA  . GLN A 10  ? 0.62731 0.79164 0.49523 -0.13104 0.13394  -0.03372 10  GLN A CA  
36   C C   . GLN A 10  ? 0.61989 0.80564 0.51026 -0.12213 0.13882  -0.05234 10  GLN A C   
37   O O   . GLN A 10  ? 0.60596 0.77002 0.50437 -0.10336 0.13451  -0.06533 10  GLN A O   
38   C CB  . GLN A 10  ? 0.64957 0.76377 0.51351 -0.14047 0.12049  -0.01726 10  GLN A CB  
39   C CG  . GLN A 10  ? 0.63105 0.72628 0.47593 -0.15033 0.11398  0.00555  10  GLN A CG  
40   C CD  . GLN A 10  ? 0.71328 0.84952 0.54568 -0.17398 0.12138  0.01839  10  GLN A CD  
41   O OE1 . GLN A 10  ? 0.74532 0.90342 0.58350 -0.19442 0.12559  0.02334  10  GLN A OE1 
42   N NE2 . GLN A 10  ? 0.67854 0.82853 0.49282 -0.17286 0.12318  0.02398  10  GLN A NE2 
43   N N   . ARG A 11  ? 0.61545 0.84771 0.51671 -0.13584 0.14793  -0.05203 11  ARG A N   
44   C CA  . ARG A 11  ? 0.59552 0.85746 0.52271 -0.13059 0.15129  -0.06499 11  ARG A CA  
45   C C   . ARG A 11  ? 0.57516 0.82756 0.51056 -0.15409 0.14140  -0.05264 11  ARG A C   
46   O O   . ARG A 11  ? 0.59957 0.86835 0.53146 -0.18027 0.14285  -0.03567 11  ARG A O   
47   C CB  . ARG A 11  ? 0.56057 0.88636 0.49910 -0.12951 0.16876  -0.07211 11  ARG A CB  
48   C CG  . ARG A 11  ? 0.59006 0.92709 0.52949 -0.10096 0.17811  -0.09348 11  ARG A CG  
49   C CD  . ARG A 11  ? 0.60154 0.91605 0.51059 -0.09583 0.17952  -0.09386 11  ARG A CD  
50   N NE  . ARG A 11  ? 0.62979 0.95321 0.53720 -0.07190 0.18820  -0.11533 11  ARG A NE  
51   C CZ  . ARG A 11  ? 0.59190 0.89674 0.47412 -0.06494 0.18836  -0.12071 11  ARG A CZ  
52   N NH1 . ARG A 11  ? 0.60177 0.88301 0.46076 -0.07838 0.18013  -0.10492 11  ARG A NH1 
53   N NH2 . ARG A 11  ? 0.54682 0.84241 0.43158 -0.04222 0.18799  -0.13552 11  ARG A NH2 
54   N N   . LEU A 12  ? 0.56113 0.78596 0.50442 -0.14716 0.13084  -0.06065 12  LEU A N   
55   C CA  . LEU A 12  ? 0.59706 0.80325 0.54244 -0.17046 0.11894  -0.05144 12  LEU A CA  
56   C C   . LEU A 12  ? 0.57238 0.81504 0.54378 -0.17107 0.11661  -0.06062 12  LEU A C   
57   O O   . LEU A 12  ? 0.56094 0.81595 0.54406 -0.14684 0.11902  -0.07618 12  LEU A O   
58   C CB  . LEU A 12  ? 0.62157 0.75478 0.54691 -0.16583 0.10625  -0.05163 12  LEU A CB  
59   C CG  . LEU A 12  ? 0.69687 0.78783 0.60038 -0.17688 0.10214  -0.03415 12  LEU A CG  
60   C CD1 . LEU A 12  ? 0.69520 0.79842 0.59115 -0.16296 0.11075  -0.03086 12  LEU A CD1 
61   C CD2 . LEU A 12  ? 0.72638 0.74703 0.61450 -0.16995 0.09114  -0.03664 12  LEU A CD2 
62   N N   . ALA A 13  ? 0.55470 0.81483 0.53563 -0.20050 0.11033  -0.04889 13  ALA A N   
63   C CA  . ALA A 13  ? 0.55826 0.85197 0.56474 -0.20583 0.10351  -0.05396 13  ALA A CA  
64   C C   . ALA A 13  ? 0.62587 0.86612 0.61942 -0.19666 0.08848  -0.06539 13  ALA A C   
65   O O   . ALA A 13  ? 0.59241 0.76707 0.55749 -0.19829 0.08140  -0.06509 13  ALA A O   
66   C CB  . ALA A 13  ? 0.56545 0.88784 0.58342 -0.24451 0.09791  -0.03639 13  ALA A CB  
67   N N   . ALA A 14  ? 0.59217 0.86211 0.60675 -0.18596 0.08410  -0.07518 14  ALA A N   
68   C CA  . ALA A 14  ? 0.61097 0.83559 0.61058 -0.17837 0.07031  -0.08604 14  ALA A CA  
69   C C   . ALA A 14  ? 0.64860 0.82187 0.62378 -0.20722 0.05497  -0.08058 14  ALA A C   
70   O O   . ALA A 14  ? 0.64045 0.75454 0.58844 -0.19991 0.04775  -0.09023 14  ALA A O   
71   C CB  . ALA A 14  ? 0.52062 0.79160 0.54824 -0.16907 0.06462  -0.09224 14  ALA A CB  
72   N N   . ASP A 15  ? 0.62873 0.82127 0.61115 -0.24041 0.05057  -0.06558 15  ASP A N   
73   C CA  . ASP A 15  ? 0.67413 0.81486 0.63228 -0.27153 0.03418  -0.06034 15  ASP A CA  
74   C C   . ASP A 15  ? 0.69635 0.78111 0.62738 -0.28106 0.03686  -0.05052 15  ASP A C   
75   O O   . ASP A 15  ? 0.71874 0.76152 0.63108 -0.31060 0.02416  -0.04292 15  ASP A O   
76   C CB  . ASP A 15  ? 0.67827 0.87070 0.66082 -0.30736 0.02325  -0.04799 15  ASP A CB  
77   C CG  . ASP A 15  ? 0.75384 1.00315 0.75980 -0.32540 0.03489  -0.02901 15  ASP A CG  
78   O OD1 . ASP A 15  ? 0.71195 0.96919 0.71677 -0.30721 0.05217  -0.02720 15  ASP A OD1 
79   O OD2 . ASP A 15  ? 0.76187 1.05055 0.78656 -0.35996 0.02642  -0.01518 15  ASP A OD2 
80   N N   . ALA A 16  ? 0.67861 0.75934 0.60620 -0.25746 0.05130  -0.04978 16  ALA A N   
81   C CA  . ALA A 16  ? 0.71566 0.74639 0.62015 -0.26421 0.05231  -0.03768 16  ALA A CA  
82   C C   . ALA A 16  ? 0.78544 0.72860 0.65748 -0.25888 0.04242  -0.04610 16  ALA A C   
83   O O   . ALA A 16  ? 0.80437 0.72626 0.66836 -0.24444 0.03844  -0.06367 16  ALA A O   
84   C CB  . ALA A 16  ? 0.64699 0.69581 0.55473 -0.23925 0.06777  -0.03557 16  ALA A CB  
85   N N   . ASP A 17  ? 0.75892 0.65057 0.61121 -0.26990 0.03914  -0.03291 17  ASP A N   
86   C CA  . ASP A 17  ? 0.84024 0.64475 0.66193 -0.26351 0.03155  -0.04016 17  ASP A CA  
87   C C   . ASP A 17  ? 0.85367 0.63762 0.67106 -0.22193 0.04167  -0.05360 17  ASP A C   
88   O O   . ASP A 17  ? 0.83760 0.64978 0.66735 -0.20349 0.05202  -0.04721 17  ASP A O   
89   C CB  . ASP A 17  ? 0.88870 0.64519 0.69424 -0.28394 0.02534  -0.01958 17  ASP A CB  
90   C CG  . ASP A 17  ? 0.99140 0.65449 0.76735 -0.27010 0.02029  -0.02674 17  ASP A CG  
91   O OD1 . ASP A 17  ? 1.04205 0.66057 0.79825 -0.27453 0.01244  -0.04358 17  ASP A OD1 
92   O OD2 . ASP A 17  ? 1.02842 0.66253 0.80020 -0.25481 0.02402  -0.01515 17  ASP A OD2 
93   N N   . VAL A 18  ? 0.86570 0.60071 0.66370 -0.20894 0.03858  -0.07209 18  VAL A N   
94   C CA  . VAL A 18  ? 0.84965 0.57107 0.64559 -0.17095 0.04914  -0.08484 18  VAL A CA  
95   C C   . VAL A 18  ? 0.86572 0.54387 0.65514 -0.15472 0.05351  -0.07425 18  VAL A C   
96   O O   . VAL A 18  ? 0.82696 0.51937 0.62707 -0.12661 0.06330  -0.07500 18  VAL A O   
97   C CB  . VAL A 18  ? 0.86635 0.55134 0.64094 -0.16259 0.04644  -0.10736 18  VAL A CB  
98   C CG1 . VAL A 18  ? 0.91143 0.51117 0.65300 -0.16798 0.04067  -0.11237 18  VAL A CG1 
99   C CG2 . VAL A 18  ? 0.79202 0.49076 0.57264 -0.12709 0.05868  -0.11931 18  VAL A CG2 
100  N N   . ASP A 19  ? 0.88723 0.51248 0.66042 -0.17258 0.04501  -0.06264 19  ASP A N   
101  C CA  . ASP A 19  ? 0.95313 0.53970 0.72378 -0.15720 0.04705  -0.04832 19  ASP A CA  
102  C C   . ASP A 19  ? 0.92935 0.57372 0.72227 -0.15304 0.05249  -0.02992 19  ASP A C   
103  O O   . ASP A 19  ? 0.94889 0.58692 0.74821 -0.12842 0.05740  -0.02328 19  ASP A O   
104  C CB  . ASP A 19  ? 1.02401 0.54536 0.77404 -0.18144 0.03480  -0.03535 19  ASP A CB  
105  C CG  . ASP A 19  ? 1.12245 0.56759 0.84299 -0.18029 0.03001  -0.05523 19  ASP A CG  
106  O OD1 . ASP A 19  ? 1.09883 0.53185 0.81390 -0.15205 0.03899  -0.07654 19  ASP A OD1 
107  O OD2 . ASP A 19  ? 1.18100 0.57640 0.88126 -0.20908 0.01735  -0.04942 19  ASP A OD2 
108  N N   . ARG A 20  ? 0.87152 0.57411 0.67599 -0.17728 0.05180  -0.02150 20  ARG A N   
109  C CA  . ARG A 20  ? 0.83012 0.58800 0.64993 -0.17465 0.05837  -0.00715 20  ARG A CA  
110  C C   . ARG A 20  ? 0.79381 0.59183 0.62796 -0.14528 0.06908  -0.02228 20  ARG A C   
111  O O   . ARG A 20  ? 0.77008 0.58306 0.60991 -0.12970 0.07348  -0.01437 20  ARG A O   
112  C CB  . ARG A 20  ? 0.81127 0.62145 0.63859 -0.20782 0.05760  0.00421  20  ARG A CB  
113  C CG  . ARG A 20  ? 0.86637 0.74340 0.70667 -0.20563 0.06772  0.01269  20  ARG A CG  
114  C CD  . ARG A 20  ? 0.94199 0.86361 0.78638 -0.24101 0.06829  0.02894  20  ARG A CD  
115  N NE  . ARG A 20  ? 0.94012 0.93638 0.79876 -0.23699 0.08181  0.02603  20  ARG A NE  
116  C CZ  . ARG A 20  ? 0.95194 0.96837 0.80505 -0.22895 0.08849  0.03469  20  ARG A CZ  
117  N NH1 . ARG A 20  ? 0.99669 0.97010 0.83435 -0.22397 0.08162  0.04991  20  ARG A NH1 
118  N NH2 . ARG A 20  ? 0.88051 0.96101 0.74316 -0.22521 0.10185  0.02772  20  ARG A NH2 
119  N N   . MET A 21  ? 0.71306 0.52710 0.55189 -0.13891 0.07167  -0.04285 21  MET A N   
120  C CA  . MET A 21  ? 0.73915 0.58203 0.58921 -0.11157 0.08043  -0.05662 21  MET A CA  
121  C C   . MET A 21  ? 0.73553 0.53964 0.58116 -0.08468 0.08315  -0.05745 21  MET A C   
122  O O   . MET A 21  ? 0.67456 0.50360 0.53062 -0.06647 0.08897  -0.05691 21  MET A O   
123  C CB  . MET A 21  ? 0.71324 0.56970 0.56582 -0.10993 0.08015  -0.07605 21  MET A CB  
124  C CG  . MET A 21  ? 0.72794 0.62324 0.58940 -0.13663 0.07566  -0.07399 21  MET A CG  
125  S SD  . MET A 21  ? 0.71675 0.64751 0.58964 -0.13225 0.07406  -0.09231 21  MET A SD  
126  C CE  . MET A 21  ? 0.77932 0.65936 0.62983 -0.15247 0.06017  -0.09891 21  MET A CE  
127  N N   . CYS A 22  ? 0.76643 0.50943 0.59713 -0.08233 0.07897  -0.05822 22  CYS A N   
128  C CA  . CYS A 22  ? 0.79744 0.50573 0.62774 -0.05398 0.08343  -0.05947 22  CYS A CA  
129  C C   . CYS A 22  ? 0.80161 0.51003 0.64053 -0.04845 0.08130  -0.03670 22  CYS A C   
130  O O   . CYS A 22  ? 0.78689 0.50690 0.63839 -0.02509 0.08608  -0.03444 22  CYS A O   
131  C CB  . CYS A 22  ? 0.89997 0.54043 0.70980 -0.05090 0.08142  -0.06983 22  CYS A CB  
132  S SG  . CYS A 22  ? 1.03970 0.67627 0.84136 -0.03182 0.09019  -0.09769 22  CYS A SG  
133  N N   . ARG A 23  ? 0.79266 0.48908 0.62486 -0.07113 0.07295  -0.01783 23  ARG A N   
134  C CA  . ARG A 23  ? 0.82866 0.53214 0.66700 -0.06955 0.06889  0.00673  23  ARG A CA  
135  C C   . ARG A 23  ? 0.75463 0.52238 0.60583 -0.06464 0.07401  0.00796  23  ARG A C   
136  O O   . ARG A 23  ? 0.71003 0.48627 0.56952 -0.05058 0.07253  0.02042  23  ARG A O   
137  C CB  . ARG A 23  ? 0.86959 0.56053 0.69622 -0.10076 0.05933  0.02810  23  ARG A CB  
138  C CG  . ARG A 23  ? 1.01461 0.64453 0.82443 -0.11601 0.05219  0.02629  23  ARG A CG  
139  C CD  . ARG A 23  ? 1.11771 0.67918 0.92253 -0.08989 0.05141  0.02161  23  ARG A CD  
140  N NE  . ARG A 23  ? 1.24020 0.73827 1.02317 -0.10601 0.04472  0.01479  23  ARG A NE  
141  C CZ  . ARG A 23  ? 1.31103 0.76304 1.08054 -0.12716 0.03300  0.03436  23  ARG A CZ  
142  N NH1 . ARG A 23  ? 1.33838 0.80013 1.11382 -0.13348 0.02670  0.06369  23  ARG A NH1 
143  N NH2 . ARG A 23  ? 1.36048 0.75342 1.10748 -0.14441 0.02617  0.02502  23  ARG A NH2 
144  N N   . LEU A 24  ? 0.70914 0.52193 0.56201 -0.07658 0.07912  -0.00444 24  LEU A N   
145  C CA  . LEU A 24  ? 0.69369 0.56133 0.55462 -0.07234 0.08447  -0.00604 24  LEU A CA  
146  C C   . LEU A 24  ? 0.68734 0.55839 0.55902 -0.04434 0.08885  -0.01733 24  LEU A C   
147  O O   . LEU A 24  ? 0.61386 0.50870 0.49063 -0.03694 0.08852  -0.01021 24  LEU A O   
148  C CB  . LEU A 24  ? 0.65253 0.56394 0.51542 -0.08709 0.09018  -0.01840 24  LEU A CB  
149  C CG  . LEU A 24  ? 0.70894 0.63452 0.56491 -0.11739 0.08785  -0.00405 24  LEU A CG  
150  C CD1 . LEU A 24  ? 0.70875 0.68168 0.57346 -0.12786 0.09477  -0.01735 24  LEU A CD1 
151  C CD2 . LEU A 24  ? 0.68881 0.63243 0.53710 -0.12568 0.08665  0.01653  24  LEU A CD2 
152  N N   . LEU A 25  ? 0.67028 0.51814 0.54362 -0.03075 0.09244  -0.03414 25  LEU A N   
153  C CA  . LEU A 25  ? 0.66599 0.51910 0.54963 -0.00615 0.09779  -0.04375 25  LEU A CA  
154  C C   . LEU A 25  ? 0.69019 0.52362 0.58252 0.01083  0.09543  -0.02881 25  LEU A C   
155  O O   . LEU A 25  ? 0.68857 0.54270 0.59383 0.02632  0.09788  -0.02861 25  LEU A O   
156  C CB  . LEU A 25  ? 0.65520 0.48772 0.53430 0.00236  0.10276  -0.06394 25  LEU A CB  
157  C CG  . LEU A 25  ? 0.58867 0.45411 0.46718 -0.00718 0.10462  -0.07849 25  LEU A CG  
158  C CD1 . LEU A 25  ? 0.58864 0.43575 0.46027 0.00073  0.10755  -0.09628 25  LEU A CD1 
159  C CD2 . LEU A 25  ? 0.54790 0.45763 0.43702 -0.00184 0.10749  -0.07922 25  LEU A CD2 
160  N N   . GLU A 26  ? 0.70226 0.49613 0.58963 0.00842  0.08990  -0.01511 26  GLU A N   
161  C CA  . GLU A 26  ? 0.71522 0.49374 0.61551 0.02686  0.08662  0.00185  26  GLU A CA  
162  C C   . GLU A 26  ? 0.73256 0.53594 0.63529 0.01548  0.07669  0.02643  26  GLU A C   
163  O O   . GLU A 26  ? 0.72065 0.53075 0.63884 0.03033  0.07227  0.04166  26  GLU A O   
164  C CB  . GLU A 26  ? 0.83143 0.54778 0.72571 0.03538  0.08560  0.00415  26  GLU A CB  
165  C CG  . GLU A 26  ? 0.87214 0.56150 0.76062 0.05049  0.09654  -0.02113 26  GLU A CG  
166  C CD  . GLU A 26  ? 0.90233 0.61767 0.80976 0.07673  0.10663  -0.02881 26  GLU A CD  
167  O OE1 . GLU A 26  ? 0.88850 0.61427 0.81729 0.09378  0.10524  -0.01242 26  GLU A OE1 
168  O OE2 . GLU A 26  ? 0.84513 0.57277 0.74696 0.07883  0.11491  -0.04922 26  GLU A OE2 
169  N N   . GLU A 27  ? 0.71641 0.53836 0.60447 -0.01094 0.07332  0.03094  27  GLU A N   
170  C CA  . GLU A 27  ? 0.72588 0.57382 0.60928 -0.02493 0.06494  0.05302  27  GLU A CA  
171  C C   . GLU A 27  ? 0.70009 0.60111 0.58313 -0.02814 0.06894  0.04336  27  GLU A C   
172  O O   . GLU A 27  ? 0.68013 0.60053 0.57109 -0.01931 0.06420  0.05189  27  GLU A O   
173  C CB  . GLU A 27  ? 0.77146 0.60926 0.63654 -0.05326 0.06044  0.06538  27  GLU A CB  
174  C CG  . GLU A 27  ? 0.83317 0.68488 0.68897 -0.06812 0.05012  0.09384  27  GLU A CG  
175  C CD  . GLU A 27  ? 0.95397 0.86086 0.79726 -0.08578 0.05468  0.08990  27  GLU A CD  
176  O OE1 . GLU A 27  ? 0.99615 0.91919 0.82885 -0.10586 0.06160  0.08222  27  GLU A OE1 
177  O OE2 . GLU A 27  ? 0.92006 0.85467 0.76414 -0.07963 0.05152  0.09405  27  GLU A OE2 
178  N N   . ASP A 28  ? 0.65808 0.58200 0.53265 -0.04052 0.07696  0.02556  28  ASP A N   
179  C CA  . ASP A 28  ? 0.66823 0.63540 0.54062 -0.04145 0.08198  0.01298  28  ASP A CA  
180  C C   . ASP A 28  ? 0.60842 0.57818 0.49475 -0.02044 0.08688  -0.00510 28  ASP A C   
181  O O   . ASP A 28  ? 0.59023 0.58494 0.47763 -0.01652 0.08646  -0.00892 28  ASP A O   
182  C CB  . ASP A 28  ? 0.60588 0.59858 0.46806 -0.05895 0.08987  0.00115  28  ASP A CB  
183  C CG  . ASP A 28  ? 0.67620 0.68297 0.52192 -0.08279 0.08733  0.01924  28  ASP A CG  
184  O OD1 . ASP A 28  ? 0.72095 0.71767 0.56058 -0.08591 0.07771  0.04114  28  ASP A OD1 
185  O OD2 . ASP A 28  ? 0.70637 0.73703 0.54627 -0.09847 0.09484  0.01309  28  ASP A OD2 
186  N N   . GLY A 29  ? 0.62003 0.56310 0.51402 -0.00887 0.09107  -0.01598 29  GLY A N   
187  C CA  . GLY A 29  ? 0.56555 0.51211 0.46941 0.00804  0.09695  -0.03299 29  GLY A CA  
188  C C   . GLY A 29  ? 0.55637 0.52204 0.45604 0.00331  0.10318  -0.05311 29  GLY A C   
189  O O   . GLY A 29  ? 0.52945 0.49623 0.43503 0.01559  0.10722  -0.06644 29  GLY A O   
190  N N   . ALA A 30  ? 0.53841 0.52122 0.42957 -0.01372 0.10421  -0.05429 30  ALA A N   
191  C CA  . ALA A 30  ? 0.52323 0.52804 0.41543 -0.01570 0.10997  -0.07196 30  ALA A CA  
192  C C   . ALA A 30  ? 0.51101 0.53188 0.39840 -0.03535 0.11151  -0.06879 30  ALA A C   
193  O O   . ALA A 30  ? 0.52559 0.54597 0.40514 -0.04925 0.10870  -0.05280 30  ALA A O   
194  C CB  . ALA A 30  ? 0.49086 0.52248 0.38334 -0.00917 0.11272  -0.08099 30  ALA A CB  
195  N N   . PHE A 31  ? 0.51596 0.55334 0.40955 -0.03702 0.11540  -0.08226 31  PHE A N   
196  C CA  . PHE A 31  ? 0.52463 0.59040 0.41983 -0.05489 0.11866  -0.08044 31  PHE A CA  
197  C C   . PHE A 31  ? 0.53671 0.62833 0.44506 -0.04803 0.12288  -0.09716 31  PHE A C   
198  O O   . PHE A 31  ? 0.50174 0.58208 0.41435 -0.03194 0.12154  -0.10832 31  PHE A O   
199  C CB  . PHE A 31  ? 0.52756 0.57004 0.41888 -0.07306 0.11271  -0.06823 31  PHE A CB  
200  C CG  . PHE A 31  ? 0.55148 0.56392 0.44483 -0.06925 0.10771  -0.07693 31  PHE A CG  
201  C CD1 . PHE A 31  ? 0.56800 0.53479 0.45422 -0.05690 0.10395  -0.07682 31  PHE A CD1 
202  C CD2 . PHE A 31  ? 0.61809 0.65002 0.52008 -0.07800 0.10691  -0.08515 31  PHE A CD2 
203  C CE1 . PHE A 31  ? 0.60464 0.54197 0.48653 -0.05411 0.10070  -0.08692 31  PHE A CE1 
204  C CE2 . PHE A 31  ? 0.60325 0.60647 0.50177 -0.07700 0.10063  -0.09338 31  PHE A CE2 
205  C CZ  . PHE A 31  ? 0.54966 0.50404 0.43531 -0.06547 0.09817  -0.09533 31  PHE A CZ  
206  N N   . ILE A 32  ? 0.52604 0.65471 0.44217 -0.06055 0.12791  -0.09698 32  ILE A N   
207  C CA  . ILE A 32  ? 0.53958 0.70183 0.47322 -0.05319 0.13233  -0.11029 32  ILE A CA  
208  C C   . ILE A 32  ? 0.53505 0.70999 0.48057 -0.07085 0.12794  -0.10526 32  ILE A C   
209  O O   . ILE A 32  ? 0.54193 0.72701 0.48489 -0.09249 0.12853  -0.09219 32  ILE A O   
210  C CB  . ILE A 32  ? 0.55320 0.75774 0.48956 -0.04909 0.14471  -0.11625 32  ILE A CB  
211  C CG1 . ILE A 32  ? 0.51140 0.70173 0.43655 -0.03069 0.14661  -0.12593 32  ILE A CG1 
212  C CG2 . ILE A 32  ? 0.53281 0.78019 0.49338 -0.04484 0.15042  -0.12538 32  ILE A CG2 
213  C CD1 . ILE A 32  ? 0.50083 0.72231 0.41797 -0.02921 0.15870  -0.13248 32  ILE A CD1 
214  N N   . LEU A 33  ? 0.49173 0.66538 0.44865 -0.06406 0.12199  -0.11395 33  LEU A N   
215  C CA  . LEU A 33  ? 0.52023 0.71482 0.49164 -0.08114 0.11604  -0.11040 33  LEU A CA  
216  C C   . LEU A 33  ? 0.50664 0.76234 0.50533 -0.07513 0.12412  -0.11544 33  LEU A C   
217  O O   . LEU A 33  ? 0.50890 0.77349 0.51640 -0.05217 0.12704  -0.12725 33  LEU A O   
218  C CB  . LEU A 33  ? 0.52144 0.68327 0.48806 -0.07838 0.10358  -0.11640 33  LEU A CB  
219  C CG  . LEU A 33  ? 0.54100 0.64321 0.48234 -0.08698 0.09582  -0.11260 33  LEU A CG  
220  C CD1 . LEU A 33  ? 0.58916 0.66338 0.52192 -0.08148 0.08637  -0.12232 33  LEU A CD1 
221  C CD2 . LEU A 33  ? 0.56915 0.66655 0.50611 -0.11629 0.09115  -0.09922 33  LEU A CD2 
222  N N   . LYS A 34  ? 0.47680 0.77448 0.48999 -0.09523 0.12802  -0.10586 34  LYS A N   
223  C CA  . LYS A 34  ? 0.50859 0.87161 0.55190 -0.08844 0.13872  -0.10971 34  LYS A CA  
224  C C   . LYS A 34  ? 0.49366 0.88244 0.56442 -0.09194 0.12759  -0.10937 34  LYS A C   
225  O O   . LYS A 34  ? 0.53233 0.91209 0.60188 -0.11691 0.11495  -0.09948 34  LYS A O   
226  C CB  . LYS A 34  ? 0.48400 0.88987 0.53166 -0.10850 0.15132  -0.09829 34  LYS A CB  
227  C CG  . LYS A 34  ? 0.54398 0.93645 0.56483 -0.10565 0.16305  -0.09786 34  LYS A CG  
228  C CD  . LYS A 34  ? 0.52755 0.92664 0.54680 -0.07518 0.17438  -0.11594 34  LYS A CD  
229  C CE  . LYS A 34  ? 0.54038 1.00581 0.58556 -0.06658 0.19158  -0.12301 34  LYS A CE  
230  N NZ  . LYS A 34  ? 0.56336 1.02236 0.60415 -0.03557 0.19990  -0.14131 34  LYS A NZ  
231  N N   . GLY A 35  ? 0.45614 0.87525 0.55070 -0.06758 0.13093  -0.11957 35  GLY A N   
232  C CA  . GLY A 35  ? 0.42806 0.88295 0.55430 -0.06887 0.12005  -0.11708 35  GLY A CA  
233  C C   . GLY A 35  ? 0.44997 0.86252 0.56136 -0.08150 0.09849  -0.11443 35  GLY A C   
234  O O   . GLY A 35  ? 0.43171 0.86847 0.55899 -0.10280 0.08612  -0.10547 35  GLY A O   
235  N N   . LEU A 36  ? 0.43688 0.78777 0.51680 -0.07031 0.09394  -0.12207 36  LEU A N   
236  C CA  . LEU A 36  ? 0.47410 0.78308 0.53502 -0.08035 0.07599  -0.12217 36  LEU A CA  
237  C C   . LEU A 36  ? 0.43374 0.76776 0.51571 -0.07015 0.06376  -0.12409 36  LEU A C   
238  O O   . LEU A 36  ? 0.44943 0.78512 0.53167 -0.08924 0.04707  -0.11904 36  LEU A O   
239  C CB  . LEU A 36  ? 0.50484 0.74858 0.52983 -0.06861 0.07736  -0.12959 36  LEU A CB  
240  C CG  . LEU A 36  ? 0.47458 0.67145 0.47424 -0.07624 0.06258  -0.13250 36  LEU A CG  
241  C CD1 . LEU A 36  ? 0.49442 0.68207 0.48562 -0.10889 0.05201  -0.12505 36  LEU A CD1 
242  C CD2 . LEU A 36  ? 0.51033 0.65087 0.47938 -0.06302 0.06817  -0.13882 36  LEU A CD2 
243  N N   . LEU A 37  ? 0.45574 0.80603 0.55337 -0.04069 0.07022  -0.13087 37  LEU A N   
244  C CA  . LEU A 37  ? 0.43943 0.81003 0.55726 -0.02733 0.05765  -0.13074 37  LEU A CA  
245  C C   . LEU A 37  ? 0.44358 0.88832 0.61006 -0.02164 0.06178  -0.12526 37  LEU A C   
246  O O   . LEU A 37  ? 0.39627 0.86675 0.57796 -0.00597 0.08051  -0.12995 37  LEU A O   
247  C CB  . LEU A 37  ? 0.45500 0.79394 0.56109 0.00193  0.06046  -0.13987 37  LEU A CB  
248  C CG  . LEU A 37  ? 0.47684 0.74963 0.53969 0.00126  0.06084  -0.14541 37  LEU A CG  
249  C CD1 . LEU A 37  ? 0.45718 0.70826 0.51438 0.02758  0.06263  -0.15178 37  LEU A CD1 
250  C CD2 . LEU A 37  ? 0.44187 0.68409 0.48000 -0.01938 0.04532  -0.14252 37  LEU A CD2 
251  N N   . PRO A 38  ? 0.44217 0.92446 0.63382 -0.03368 0.04519  -0.11559 38  PRO A N   
252  C CA  . PRO A 38  ? 0.40088 0.96173 0.64640 -0.02506 0.04929  -0.10890 38  PRO A CA  
253  C C   . PRO A 38  ? 0.42705 0.99871 0.69345 0.01542  0.05675  -0.11656 38  PRO A C   
254  O O   . PRO A 38  ? 0.41473 0.93531 0.65570 0.03275  0.05275  -0.12400 38  PRO A O   
255  C CB  . PRO A 38  ? 0.44855 1.03737 0.71136 -0.04726 0.02405  -0.09584 38  PRO A CB  
256  C CG  . PRO A 38  ? 0.49411 1.01784 0.70628 -0.07543 0.01081  -0.09710 38  PRO A CG  
257  C CD  . PRO A 38  ? 0.41395 0.87021 0.58532 -0.05654 0.02176  -0.11040 38  PRO A CD  
258  N N   . PHE A 39  ? 0.39892 1.03844 0.71302 0.03044  0.06824  -0.11432 39  PHE A N   
259  C CA  . PHE A 39  ? 0.38453 1.03367 0.72033 0.07128  0.07802  -0.12322 39  PHE A CA  
260  C C   . PHE A 39  ? 0.41660 1.05237 0.76105 0.08709  0.05520  -0.11791 39  PHE A C   
261  O O   . PHE A 39  ? 0.42063 1.02132 0.75617 0.11588  0.05718  -0.12638 39  PHE A O   
262  C CB  . PHE A 39  ? 0.42215 1.15245 0.81051 0.08421  0.09590  -0.12160 39  PHE A CB  
263  C CG  . PHE A 39  ? 0.48611 1.23103 0.90369 0.12860  0.10477  -0.13046 39  PHE A CG  
264  C CD1 . PHE A 39  ? 0.52932 1.23586 0.92275 0.15282  0.12497  -0.14922 39  PHE A CD1 
265  C CD2 . PHE A 39  ? 0.45240 1.24804 0.92150 0.14598  0.09180  -0.11965 39  PHE A CD2 
266  C CE1 . PHE A 39  ? 0.48604 1.17810 0.89311 0.18872  0.13007  -0.15410 39  PHE A CE1 
267  C CE2 . PHE A 39  ? 0.49255 1.29346 0.98778 0.18879  0.09945  -0.12689 39  PHE A CE2 
268  C CZ  . PHE A 39  ? 0.48025 1.21621 0.93773 0.20749  0.11818  -0.14309 39  PHE A CZ  
269  N N   . ASP A 40  ? 0.45078 1.11360 0.81114 0.06687  0.03204  -0.10282 40  ASP A N   
270  C CA  . ASP A 40  ? 0.46198 1.11546 0.82881 0.07937  0.00801  -0.09498 40  ASP A CA  
271  C C   . ASP A 40  ? 0.49434 1.06422 0.80313 0.07650  -0.00083 -0.10137 40  ASP A C   
272  O O   . ASP A 40  ? 0.48364 1.03034 0.78950 0.09742  -0.01181 -0.09958 40  ASP A O   
273  C CB  . ASP A 40  ? 0.44388 1.14754 0.83742 0.05374  -0.01656 -0.07674 40  ASP A CB  
274  C CG  . ASP A 40  ? 0.53622 1.21363 0.89091 0.00895  -0.02526 -0.07483 40  ASP A CG  
275  O OD1 . ASP A 40  ? 0.55349 1.17494 0.86316 -0.00009 -0.01215 -0.08647 40  ASP A OD1 
276  O OD2 . ASP A 40  ? 0.68065 1.39267 1.05026 -0.01756 -0.04650 -0.06118 40  ASP A OD2 
277  N N   . VAL A 41  ? 0.46925 0.99451 0.73305 0.05142  0.00412  -0.10762 41  VAL A N   
278  C CA  . VAL A 41  ? 0.51709 0.96776 0.72885 0.05175  0.00141  -0.11499 41  VAL A CA  
279  C C   . VAL A 41  ? 0.50450 0.92705 0.71005 0.08160  0.01903  -0.12654 41  VAL A C   
280  O O   . VAL A 41  ? 0.45878 0.84169 0.64585 0.09630  0.01254  -0.12784 41  VAL A O   
281  C CB  . VAL A 41  ? 0.48356 0.89685 0.65429 0.02096  0.00424  -0.11885 41  VAL A CB  
282  C CG1 . VAL A 41  ? 0.52609 0.86909 0.64846 0.02524  0.00669  -0.12724 41  VAL A CG1 
283  C CG2 . VAL A 41  ? 0.45848 0.88712 0.62724 -0.01017 -0.01652 -0.10901 41  VAL A CG2 
284  N N   . VAL A 42  ? 0.48990 0.93252 0.70876 0.08891  0.04096  -0.13459 42  VAL A N   
285  C CA  . VAL A 42  ? 0.51704 0.93132 0.72570 0.11378  0.05757  -0.14742 42  VAL A CA  
286  C C   . VAL A 42  ? 0.46913 0.89279 0.70527 0.14659  0.05297  -0.14741 42  VAL A C   
287  O O   . VAL A 42  ? 0.47361 0.85156 0.69023 0.16396  0.05430  -0.15419 42  VAL A O   
288  C CB  . VAL A 42  ? 0.52284 0.96199 0.73789 0.11218  0.08126  -0.15570 42  VAL A CB  
289  C CG1 . VAL A 42  ? 0.45093 0.86682 0.65787 0.13891  0.09735  -0.17037 42  VAL A CG1 
290  C CG2 . VAL A 42  ? 0.47934 0.89490 0.66121 0.08167  0.08443  -0.15445 42  VAL A CG2 
291  N N   . GLU A 43  ? 0.46845 0.95083 0.75154 0.15532  0.04644  -0.13848 43  GLU A N   
292  C CA  . GLU A 43  ? 0.46886 0.96159 0.78323 0.19037  0.04240  -0.13751 43  GLU A CA  
293  C C   . GLU A 43  ? 0.46138 0.91420 0.75844 0.19269  0.01758  -0.12706 43  GLU A C   
294  O O   . GLU A 43  ? 0.48977 0.90451 0.77948 0.21662  0.01640  -0.13068 43  GLU A O   
295  C CB  . GLU A 43  ? 0.47776 1.05180 0.85326 0.20085  0.04281  -0.12897 43  GLU A CB  
296  C CG  . GLU A 43  ? 0.52059 1.11243 0.93466 0.24499  0.05216  -0.13488 43  GLU A CG  
297  C CD  . GLU A 43  ? 0.60028 1.28197 1.08087 0.25742  0.05633  -0.12638 43  GLU A CD  
298  O OE1 . GLU A 43  ? 0.55528 1.28697 1.05258 0.22852  0.04921  -0.11386 43  GLU A OE1 
299  O OE2 . GLU A 43  ? 0.59414 1.28368 1.10391 0.29084  0.06632  -0.12909 43  GLU A OE2 
300  N N   . SER A 44  ? 0.43441 0.89239 0.72089 0.16619  -0.00273 -0.11402 44  SER A N   
301  C CA  . SER A 44  ? 0.46293 0.88601 0.72856 0.16578  -0.02629 -0.10308 44  SER A CA  
302  C C   . SER A 44  ? 0.48540 0.83550 0.69704 0.16177  -0.02098 -0.11165 44  SER A C   
303  O O   . SER A 44  ? 0.47465 0.78896 0.67313 0.17533  -0.03086 -0.10694 44  SER A O   
304  C CB  . SER A 44  ? 0.45539 0.90136 0.71709 0.13578  -0.04865 -0.08922 44  SER A CB  
305  O OG  . SER A 44  ? 0.52382 0.94480 0.74594 0.10458  -0.04255 -0.09639 44  SER A OG  
306  N N   . PHE A 45  ? 0.49186 0.82087 0.67377 0.14311  -0.00588 -0.12242 45  PHE A N   
307  C CA  . PHE A 45  ? 0.51825 0.78672 0.65699 0.14200  0.00210  -0.13051 45  PHE A CA  
308  C C   . PHE A 45  ? 0.50779 0.75622 0.65437 0.17056  0.01180  -0.13804 45  PHE A C   
309  O O   . PHE A 45  ? 0.52313 0.72711 0.64695 0.17712  0.00602  -0.13607 45  PHE A O   
310  C CB  . PHE A 45  ? 0.50211 0.75998 0.61762 0.12144  0.01765  -0.13979 45  PHE A CB  
311  C CG  . PHE A 45  ? 0.52692 0.72928 0.59890 0.11454  0.02250  -0.14449 45  PHE A CG  
312  C CD1 . PHE A 45  ? 0.50223 0.66918 0.55480 0.12167  0.01302  -0.13966 45  PHE A CD1 
313  C CD2 . PHE A 45  ? 0.45719 0.64536 0.50954 0.10074  0.03644  -0.15181 45  PHE A CD2 
314  C CE1 . PHE A 45  ? 0.50352 0.62713 0.52028 0.11468  0.01884  -0.14262 45  PHE A CE1 
315  C CE2 . PHE A 45  ? 0.47519 0.61898 0.49362 0.09623  0.04115  -0.15467 45  PHE A CE2 
316  C CZ  . PHE A 45  ? 0.49467 0.60850 0.49640 0.10308  0.03311  -0.15037 45  PHE A CZ  
317  N N   . ASN A 46  ? 0.51917 0.79932 0.69636 0.18692  0.02674  -0.14687 46  ASN A N   
318  C CA  . ASN A 46  ? 0.52066 0.77772 0.70223 0.21448  0.03647  -0.15714 46  ASN A CA  
319  C C   . ASN A 46  ? 0.51293 0.75989 0.71165 0.23714  0.01921  -0.14696 46  ASN A C   
320  O O   . ASN A 46  ? 0.51050 0.70918 0.69211 0.25060  0.01792  -0.15021 46  ASN A O   
321  C CB  . ASN A 46  ? 0.48173 0.77850 0.69084 0.22782  0.05749  -0.16996 46  ASN A CB  
322  C CG  . ASN A 46  ? 0.50367 0.78059 0.68220 0.21487  0.07669  -0.18391 46  ASN A CG  
323  O OD1 . ASN A 46  ? 0.48807 0.71335 0.63158 0.21056  0.07677  -0.18841 46  ASN A OD1 
324  N ND2 . ASN A 46  ? 0.46451 0.78484 0.65664 0.20688  0.09187  -0.18857 46  ASN A ND2 
325  N N   . ARG A 47  ? 0.46777 0.75845 0.69936 0.23952  0.00365  -0.13259 47  ARG A N   
326  C CA  . ARG A 47  ? 0.51809 0.79984 0.76587 0.25964  -0.01662 -0.11860 47  ARG A CA  
327  C C   . ARG A 47  ? 0.56237 0.78950 0.76571 0.24456  -0.03294 -0.10838 47  ARG A C   
328  O O   . ARG A 47  ? 0.59049 0.77966 0.78814 0.26132  -0.04232 -0.10253 47  ARG A O   
329  C CB  . ARG A 47  ? 0.50224 0.84861 0.79509 0.26143  -0.03227 -0.10275 47  ARG A CB  
330  C CG  . ARG A 47  ? 0.63948 0.99276 0.96780 0.29308  -0.04911 -0.08924 47  ARG A CG  
331  C CD  . ARG A 47  ? 0.69019 1.04564 1.04941 0.33121  -0.02978 -0.10399 47  ARG A CD  
332  N NE  . ARG A 47  ? 0.77233 1.16202 1.18471 0.36338  -0.04336 -0.09024 47  ARG A NE  
333  C CZ  . ARG A 47  ? 0.73036 1.19845 1.19801 0.37132  -0.04358 -0.08298 47  ARG A CZ  
334  N NH1 . ARG A 47  ? 0.73130 1.25005 1.20676 0.34775  -0.03071 -0.08830 47  ARG A NH1 
335  N NH2 . ARG A 47  ? 0.63540 1.13295 1.15337 0.40308  -0.05787 -0.06823 47  ARG A NH2 
336  N N   . GLU A 48  ? 0.50129 0.72236 0.67176 0.21309  -0.03584 -0.10599 48  GLU A N   
337  C CA  . GLU A 48  ? 0.53951 0.71341 0.66646 0.19864  -0.04799 -0.09713 48  GLU A CA  
338  C C   . GLU A 48  ? 0.57518 0.69505 0.67341 0.20326  -0.03513 -0.10679 48  GLU A C   
339  O O   . GLU A 48  ? 0.61480 0.69525 0.69146 0.20477  -0.04563 -0.09728 48  GLU A O   
340  C CB  . GLU A 48  ? 0.55703 0.73613 0.65488 0.16639  -0.05085 -0.09575 48  GLU A CB  
341  C CG  . GLU A 48  ? 0.51129 0.73846 0.63124 0.15626  -0.06888 -0.08399 48  GLU A CG  
342  C CD  . GLU A 48  ? 0.52004 0.75411 0.61598 0.12497  -0.06649 -0.08889 48  GLU A CD  
343  O OE1 . GLU A 48  ? 0.54370 0.74251 0.60492 0.11367  -0.05148 -0.09995 48  GLU A OE1 
344  O OE2 . GLU A 48  ? 0.53163 0.80558 0.64426 0.11163  -0.08032 -0.08124 48  GLU A OE2 
345  N N   . LEU A 49  ? 0.57564 0.69446 0.67316 0.20392  -0.01365 -0.12407 49  LEU A N   
346  C CA  . LEU A 49  ? 0.62111 0.69293 0.69489 0.20775  -0.00297 -0.13331 49  LEU A CA  
347  C C   . LEU A 49  ? 0.67209 0.72241 0.76251 0.23600  -0.00568 -0.13530 49  LEU A C   
348  O O   . LEU A 49  ? 0.70434 0.70589 0.77136 0.23688  -0.00786 -0.13467 49  LEU A O   
349  C CB  . LEU A 49  ? 0.56448 0.64343 0.63162 0.19922  0.01831  -0.14982 49  LEU A CB  
350  C CG  . LEU A 49  ? 0.59933 0.68541 0.64491 0.17220  0.02066  -0.14756 49  LEU A CG  
351  C CD1 . LEU A 49  ? 0.51944 0.62562 0.56918 0.16576  0.03831  -0.15986 49  LEU A CD1 
352  C CD2 . LEU A 49  ? 0.55066 0.59383 0.55899 0.15920  0.01884  -0.14305 49  LEU A CD2 
353  N N   . ASP A 50  ? 0.62878 0.71375 0.75971 0.25927  -0.00500 -0.13786 50  ASP A N   
354  C CA  . ASP A 50  ? 0.62461 0.68487 0.77228 0.28999  -0.00825 -0.13995 50  ASP A CA  
355  C C   . ASP A 50  ? 0.67895 0.70284 0.81539 0.29207  -0.03187 -0.11963 50  ASP A C   
356  O O   . ASP A 50  ? 0.72361 0.69679 0.84890 0.30500  -0.03544 -0.12034 50  ASP A O   
357  C CB  . ASP A 50  ? 0.62937 0.74155 0.82806 0.31676  -0.00386 -0.14344 50  ASP A CB  
358  C CG  . ASP A 50  ? 0.67218 0.81555 0.88021 0.31832  0.02227  -0.16465 50  ASP A CG  
359  O OD1 . ASP A 50  ? 0.68931 0.80144 0.86376 0.30582  0.03595  -0.17872 50  ASP A OD1 
360  O OD2 . ASP A 50  ? 0.64123 0.84315 0.89066 0.33115  0.02872  -0.16579 50  ASP A OD2 
361  N N   . VAL A 51  ? 0.67017 0.60046 1.01479 0.26167  0.17870  -0.19362 51  VAL A N   
362  C CA  . VAL A 51  ? 0.65121 0.60787 1.05366 0.24065  0.16222  -0.18253 51  VAL A CA  
363  C C   . VAL A 51  ? 0.66637 0.64924 1.07084 0.23660  0.13811  -0.17550 51  VAL A C   
364  O O   . VAL A 51  ? 0.64558 0.64215 1.08575 0.22225  0.11084  -0.17287 51  VAL A O   
365  C CB  . VAL A 51  ? 0.64993 0.61813 1.06068 0.22710  0.18064  -0.16685 51  VAL A CB  
366  C CG1 . VAL A 51  ? 0.66357 0.66262 1.12189 0.20190  0.15945  -0.15002 51  VAL A CG1 
367  C CG2 . VAL A 51  ? 0.61725 0.56574 1.01858 0.22349  0.19633  -0.16811 51  VAL A CG2 
368  N N   . GLN A 52  ? 0.66095 0.65179 1.02641 0.24936  0.14825  -0.17153 52  GLN A N   
369  C CA  . GLN A 52  ? 0.66191 0.68208 1.02835 0.24641  0.12650  -0.16271 52  GLN A CA  
370  C C   . GLN A 52  ? 0.68050 0.69575 1.04336 0.25264  0.10401  -0.17659 52  GLN A C   
371  O O   . GLN A 52  ? 0.68694 0.72516 1.07284 0.23985  0.07607  -0.17118 52  GLN A O   
372  C CB  . GLN A 52  ? 0.63800 0.66770 0.96188 0.26082  0.14564  -0.15354 52  GLN A CB  
373  C CG  . GLN A 52  ? 0.61732 0.64990 0.94177 0.25189  0.16748  -0.13919 52  GLN A CG  
374  C CD  . GLN A 52  ? 0.58267 0.64229 0.95637 0.22515  0.14850  -0.12350 52  GLN A CD  
375  O OE1 . GLN A 52  ? 0.57119 0.65986 0.95823 0.21850  0.12775  -0.11286 52  GLN A OE1 
376  N NE2 . GLN A 52  ? 0.56595 0.61793 0.96691 0.20953  0.15564  -0.12128 52  GLN A NE2 
377  N N   . MET A 53  ? 0.69504 0.67976 1.02824 0.27091  0.11578  -0.19460 53  MET A N   
378  C CA  . MET A 53  ? 0.72148 0.69592 1.04769 0.27594  0.09632  -0.20958 53  MET A CA  
379  C C   . MET A 53  ? 0.75330 0.72319 1.12354 0.25679  0.07207  -0.21310 53  MET A C   
380  O O   . MET A 53  ? 0.73692 0.70771 1.10821 0.25273  0.04864  -0.22019 53  MET A O   
381  C CB  . MET A 53  ? 0.74892 0.68719 1.03663 0.29849  0.11640  -0.22859 53  MET A CB  
382  C CG  . MET A 53  ? 0.76223 0.70132 0.99993 0.32053  0.13879  -0.22793 53  MET A CG  
383  S SD  . MET A 53  ? 0.83170 0.80309 1.04647 0.32654  0.11915  -0.22226 53  MET A SD  
384  C CE  . MET A 53  ? 0.80582 0.75651 1.02308 0.32426  0.09517  -0.24315 53  MET A CE  
385  N N   . ALA A 54  ? 0.76029 0.72523 1.16537 0.24452  0.07755  -0.20779 54  ALA A N   
386  C CA  . ALA A 54  ? 0.74937 0.70840 1.19673 0.22786  0.05753  -0.20971 54  ALA A CA  
387  C C   . ALA A 54  ? 0.76483 0.75856 1.25098 0.20467  0.03450  -0.19252 54  ALA A C   
388  O O   . ALA A 54  ? 0.80964 0.80119 1.33464 0.18909  0.01925  -0.19098 54  ALA A O   
389  C CB  . ALA A 54  ? 0.69966 0.63639 1.16545 0.22817  0.07594  -0.21238 54  ALA A CB  
390  N N   . ILE A 55  ? 0.75568 0.78066 1.23187 0.20283  0.03250  -0.17908 55  ILE A N   
391  C CA  . ILE A 55  ? 0.79839 0.85817 1.30994 0.18126  0.01023  -0.16222 55  ILE A CA  
392  C C   . ILE A 55  ? 0.85077 0.91772 1.36657 0.17387  -0.02058 -0.16772 55  ILE A C   
393  O O   . ILE A 55  ? 0.89114 0.95642 1.37116 0.18678  -0.02318 -0.17605 55  ILE A O   
394  C CB  . ILE A 55  ? 0.79897 0.88838 1.29567 0.18327  0.02022  -0.14540 55  ILE A CB  
395  C CG1 . ILE A 55  ? 0.75303 0.83222 1.24245 0.18755  0.05145  -0.14010 55  ILE A CG1 
396  C CG2 . ILE A 55  ? 0.79775 0.92396 1.32963 0.16180  -0.00373 -0.12812 55  ILE A CG2 
397  C CD1 . ILE A 55  ? 0.78266 0.85904 1.31596 0.16930  0.05160  -0.13475 55  ILE A CD1 
398  N N   . PRO A 56  ? 0.88607 0.96059 1.44307 0.15279  -0.04388 -0.16331 56  PRO A N   
399  C CA  . PRO A 56  ? 0.95231 1.02804 1.51187 0.14323  -0.07316 -0.17019 56  PRO A CA  
400  C C   . PRO A 56  ? 1.00526 1.11613 1.54440 0.14332  -0.08671 -0.16201 56  PRO A C   
401  O O   . PRO A 56  ? 0.95023 1.09072 1.48655 0.14551  -0.07843 -0.14625 56  PRO A O   
402  C CB  . PRO A 56  ? 0.97315 1.05607 1.58400 0.11921  -0.09202 -0.16174 56  PRO A CB  
403  C CG  . PRO A 56  ? 0.95980 1.05770 1.59454 0.11515  -0.07497 -0.14634 56  PRO A CG  
404  C CD  . PRO A 56  ? 0.89794 0.97567 1.49978 0.13681  -0.04297 -0.15325 56  PRO A CD  
405  N N   . PRO A 57  ? 1.05071 1.15928 1.57373 0.14083  -0.10706 -0.17176 57  PRO A N   
406  C CA  . PRO A 57  ? 1.05617 1.20185 1.55862 0.14107  -0.12101 -0.16337 57  PRO A CA  
407  C C   . PRO A 57  ? 1.00612 1.19556 1.54136 0.12263  -0.13744 -0.14175 57  PRO A C   
408  O O   . PRO A 57  ? 0.98005 1.17045 1.55486 0.10191  -0.15370 -0.13783 57  PRO A O   
409  C CB  . PRO A 57  ? 1.10706 1.23806 1.59502 0.13418  -0.14359 -0.17864 57  PRO A CB  
410  C CG  . PRO A 57  ? 1.11462 1.20224 1.62315 0.12665  -0.14458 -0.19232 57  PRO A CG  
411  C CD  . PRO A 57  ? 1.07191 1.14097 1.58848 0.13991  -0.11499 -0.19169 57  PRO A CD  
412  N N   . PRO A 58  ? 0.96258 1.18853 1.48150 0.13043  -0.13322 -0.12691 58  PRO A N   
413  C CA  . PRO A 58  ? 0.85118 1.11850 1.39962 0.11550  -0.14434 -0.10476 58  PRO A CA  
414  C C   . PRO A 58  ? 0.77616 1.06931 1.34662 0.09247  -0.18030 -0.10014 58  PRO A C   
415  O O   . PRO A 58  ? 0.78512 1.07340 1.33841 0.08970  -0.19707 -0.11137 58  PRO A O   
416  C CB  . PRO A 58  ? 0.79049 1.08521 1.30604 0.13473  -0.12776 -0.09193 58  PRO A CB  
417  C CG  . PRO A 58  ? 0.87179 1.13284 1.34592 0.16002  -0.10112 -0.10723 58  PRO A CG  
418  C CD  . PRO A 58  ? 0.97430 1.20240 1.44627 0.15581  -0.11345 -0.12892 58  PRO A CD  
419  N N   . LYS A 59  ? 0.67895 1.00044 1.28658 0.07469  -0.19199 -0.08287 59  LYS A N   
420  C CA  . LYS A 59  ? 0.64872 0.99848 1.28008 0.05106  -0.22592 -0.07586 59  LYS A CA  
421  C C   . LYS A 59  ? 0.61237 1.01408 1.23121 0.05270  -0.23582 -0.05787 59  LYS A C   
422  O O   . LYS A 59  ? 0.54324 0.97077 1.16907 0.03615  -0.26448 -0.05418 59  LYS A O   
423  C CB  . LYS A 59  ? 0.58041 0.93287 1.26213 0.02915  -0.23565 -0.06699 59  LYS A CB  
424  C CG  . LYS A 59  ? 0.62452 0.93087 1.32456 0.02547  -0.22875 -0.08175 59  LYS A CG  
425  C CD  . LYS A 59  ? 0.61650 0.89024 1.30026 0.02343  -0.24153 -0.10239 59  LYS A CD  
426  C CE  . LYS A 59  ? 0.58008 0.81548 1.29329 0.01303  -0.24308 -0.11217 59  LYS A CE  
427  N NZ  . LYS A 59  ? 0.54504 0.79903 1.30167 -0.01347 -0.26777 -0.10093 59  LYS A NZ  
428  N N   . GLY A 60  ? 1.21737 0.43993 1.04328 0.18029  0.16583  0.05703  60  GLY A N   
429  C CA  . GLY A 60  ? 1.15316 0.37350 0.94464 0.14617  0.15615  0.03736  60  GLY A CA  
430  C C   . GLY A 60  ? 1.05147 0.32959 0.85652 0.10331  0.13773  -0.00442 60  GLY A C   
431  O O   . GLY A 60  ? 1.02299 0.33718 0.85750 0.09554  0.13828  -0.02114 60  GLY A O   
432  N N   . GLU A 61  ? 1.01719 0.31099 0.80057 0.07715  0.12235  -0.01875 61  GLU A N   
433  C CA  . GLU A 61  ? 1.00440 0.36166 0.79840 0.04119  0.10078  -0.05054 61  GLU A CA  
434  C C   . GLU A 61  ? 0.95874 0.37443 0.76102 0.05125  0.05157  -0.03388 61  GLU A C   
435  O O   . GLU A 61  ? 0.90529 0.32182 0.69806 0.07700  0.02127  -0.00434 61  GLU A O   
436  C CB  . GLU A 61  ? 1.01200 0.37790 0.78964 0.01928  0.09462  -0.06363 61  GLU A CB  
437  C CG  . GLU A 61  ? 0.99250 0.35784 0.74255 0.04119  0.06013  -0.03509 61  GLU A CG  
438  C CD  . GLU A 61  ? 0.99042 0.39468 0.73861 0.02144  0.04027  -0.05041 61  GLU A CD  
439  O OE1 . GLU A 61  ? 1.02318 0.46481 0.79291 -0.00821 0.04859  -0.07963 61  GLU A OE1 
440  O OE2 . GLU A 61  ? 0.97169 0.37297 0.69743 0.03747  0.01580  -0.03410 61  GLU A OE2 
441  N N   . ARG A 62  ? 0.93916 0.40455 0.75830 0.02853  0.04655  -0.05443 62  ARG A N   
442  C CA  . ARG A 62  ? 0.88451 0.40569 0.71347 0.02762  0.00709  -0.04135 62  ARG A CA  
443  C C   . ARG A 62  ? 0.86584 0.42877 0.68470 -0.00018 -0.00874 -0.05735 62  ARG A C   
444  O O   . ARG A 62  ? 0.85925 0.44600 0.67751 -0.02445 0.01087  -0.08590 62  ARG A O   
445  C CB  . ARG A 62  ? 0.89230 0.43863 0.74838 0.03020  0.02068  -0.04318 62  ARG A CB  
446  C CG  . ARG A 62  ? 0.95902 0.48517 0.83880 0.06563  0.02592  -0.01876 62  ARG A CG  
447  C CD  . ARG A 62  ? 0.92018 0.45961 0.79886 0.08406  -0.02015 0.01169  62  ARG A CD  
448  N NE  . ARG A 62  ? 1.00614 0.49690 0.85995 0.10928  -0.01830 0.02776  62  ARG A NE  
449  C CZ  . ARG A 62  ? 1.06151 0.54344 0.92595 0.14564  -0.02090 0.05440  62  ARG A CZ  
450  N NH1 . ARG A 62  ? 1.14154 0.66588 1.05169 0.16102  -0.02774 0.06553  62  ARG A NH1 
451  N NH2 . ARG A 62  ? 1.05409 0.48949 0.88338 0.16894  -0.01598 0.07302  62  ARG A NH2 
452  N N   . LEU A 63  ? 0.79911 0.37339 0.61056 0.00483  -0.04412 -0.03997 63  LEU A N   
453  C CA  . LEU A 63  ? 0.79192 0.40018 0.59745 -0.01163 -0.05788 -0.04871 63  LEU A CA  
454  C C   . LEU A 63  ? 0.78131 0.44718 0.59096 -0.03008 -0.06111 -0.05505 63  LEU A C   
455  O O   . LEU A 63  ? 0.77897 0.48213 0.58335 -0.04897 -0.05563 -0.07639 63  LEU A O   
456  C CB  . LEU A 63  ? 0.78094 0.38219 0.58232 0.00207  -0.09087 -0.02746 63  LEU A CB  
457  C CG  . LEU A 63  ? 0.82687 0.37774 0.61034 0.01873  -0.08648 -0.02517 63  LEU A CG  
458  C CD1 . LEU A 63  ? 0.77184 0.31209 0.54687 0.03061  -0.11609 -0.01278 63  LEU A CD1 
459  C CD2 . LEU A 63  ? 0.86782 0.40704 0.64489 0.00863  -0.05666 -0.04595 63  LEU A CD2 
460  N N   . LEU A 64  ? 0.78342 0.46401 0.60204 -0.02600 -0.06920 -0.03713 64  LEU A N   
461  C CA  . LEU A 64  ? 0.79420 0.52833 0.60812 -0.04139 -0.06908 -0.03636 64  LEU A CA  
462  C C   . LEU A 64  ? 0.84006 0.58369 0.65140 -0.05369 -0.03296 -0.06512 64  LEU A C   
463  O O   . LEU A 64  ? 0.89021 0.67477 0.68202 -0.07486 -0.02252 -0.09016 64  LEU A O   
464  C CB  . LEU A 64  ? 0.75302 0.49550 0.58144 -0.03420 -0.08925 -0.00161 64  LEU A CB  
465  C CG  . LEU A 64  ? 0.81384 0.60632 0.63403 -0.04687 -0.08804 0.01308  64  LEU A CG  
466  C CD1 . LEU A 64  ? 0.87153 0.70800 0.66168 -0.05727 -0.09463 0.00637  64  LEU A CD1 
467  C CD2 . LEU A 64  ? 0.76159 0.54722 0.60128 -0.04210 -0.10832 0.05062  64  LEU A CD2 
468  N N   . ALA A 65  ? 0.81890 0.52804 0.65052 -0.03927 -0.01343 -0.06384 65  ALA A N   
469  C CA  . ALA A 65  ? 0.88546 0.59743 0.72187 -0.04546 0.02614  -0.08938 65  ALA A CA  
470  C C   . ALA A 65  ? 0.93046 0.62959 0.74963 -0.06652 0.05663  -0.13515 65  ALA A C   
471  O O   . ALA A 65  ? 0.97778 0.70346 0.78410 -0.08676 0.08275  -0.16823 65  ALA A O   
472  C CB  . ALA A 65  ? 0.85346 0.52791 0.72393 -0.01732 0.04108  -0.07535 65  ALA A CB  
473  N N   . ASP A 66  ? 0.89700 0.55622 0.71577 -0.06532 0.05726  -0.14134 66  ASP A N   
474  C CA  . ASP A 66  ? 0.98666 0.63123 0.79908 -0.09158 0.09030  -0.18805 66  ASP A CA  
475  C C   . ASP A 66  ? 1.00204 0.72297 0.79370 -0.12562 0.07557  -0.21704 66  ASP A C   
476  O O   . ASP A 66  ? 0.99585 0.72424 0.78341 -0.15650 0.10321  -0.26709 66  ASP A O   
477  C CB  . ASP A 66  ? 0.96086 0.54879 0.77969 -0.08419 0.09695  -0.18287 66  ASP A CB  
478  C CG  . ASP A 66  ? 0.94471 0.45694 0.77589 -0.04987 0.11794  -0.15695 66  ASP A CG  
479  O OD1 . ASP A 66  ? 0.96593 0.46661 0.81118 -0.03396 0.13577  -0.15253 66  ASP A OD1 
480  O OD2 . ASP A 66  ? 0.94108 0.40991 0.76742 -0.03620 0.11720  -0.13883 66  ASP A OD2 
481  N N   . LYS A 67  ? 1.11261 0.89124 0.89247 -0.12051 0.03311  -0.18677 67  LYS A N   
482  C CA  . LYS A 67  ? 1.07059 0.93294 0.82856 -0.14411 0.01285  -0.20295 67  LYS A CA  
483  C C   . LYS A 67  ? 1.13636 1.04758 0.86520 -0.16249 0.02764  -0.22596 67  LYS A C   
484  O O   . LYS A 67  ? 1.21857 1.20589 0.92107 -0.18609 0.01517  -0.24954 67  LYS A O   
485  C CB  . LYS A 67  ? 1.05095 0.94871 0.80670 -0.12484 -0.03322 -0.15393 67  LYS A CB  
486  C CG  . LYS A 67  ? 1.02838 0.94373 0.79872 -0.12406 -0.05419 -0.15387 67  LYS A CG  
487  C CD  . LYS A 67  ? 1.02430 0.86158 0.81653 -0.10664 -0.04528 -0.14403 67  LYS A CD  
488  C CE  . LYS A 67  ? 0.95691 0.81071 0.76374 -0.09539 -0.06965 -0.12888 67  LYS A CE  
489  N NZ  . LYS A 67  ? 1.00731 0.93005 0.82608 -0.11989 -0.06989 -0.16308 67  LYS A NZ  
490  N N   . TYR A 68  ? 1.07566 0.95437 0.80779 -0.15151 0.05330  -0.22021 68  TYR A N   
491  C CA  . TYR A 68  ? 1.13403 1.06151 0.83463 -0.16587 0.06995  -0.23718 68  TYR A CA  
492  C C   . TYR A 68  ? 1.16040 1.04027 0.87146 -0.17223 0.12513  -0.28159 68  TYR A C   
493  O O   . TYR A 68  ? 1.12461 0.92803 0.87247 -0.15546 0.14736  -0.28152 68  TYR A O   
494  C CB  . TYR A 68  ? 1.12247 1.07116 0.82041 -0.14509 0.05095  -0.18047 68  TYR A CB  
495  C CG  . TYR A 68  ? 1.12608 1.11593 0.81164 -0.13782 0.00289  -0.13599 68  TYR A CG  
496  C CD1 . TYR A 68  ? 1.13548 1.20594 0.77646 -0.15350 -0.01548 -0.14020 68  TYR A CD1 
497  C CD2 . TYR A 68  ? 1.08026 1.02885 0.79814 -0.11357 -0.02238 -0.09159 68  TYR A CD2 
498  C CE1 . TYR A 68  ? 1.11057 1.21382 0.74615 -0.13920 -0.05610 -0.09377 68  TYR A CE1 
499  C CE2 . TYR A 68  ? 1.10832 1.08438 0.81880 -0.10461 -0.05906 -0.05360 68  TYR A CE2 
500  C CZ  . TYR A 68  ? 1.10385 1.15498 0.77640 -0.11409 -0.07578 -0.05008 68  TYR A CZ  
501  O OH  . TYR A 68  ? 1.10492 1.17858 0.77595 -0.09763 -0.10938 -0.00620 68  TYR A OH  
502  N N   . PRO A 69  ? 1.24133 1.16368 0.91757 -0.19449 0.15085  -0.32032 69  PRO A N   
503  C CA  . PRO A 69  ? 1.24969 1.12302 0.93664 -0.20066 0.21102  -0.37020 69  PRO A CA  
504  C C   . PRO A 69  ? 1.28038 1.09868 1.01372 -0.16100 0.23211  -0.33263 69  PRO A C   
505  O O   . PRO A 69  ? 1.19948 1.02780 0.95205 -0.13570 0.19828  -0.27289 69  PRO A O   
506  C CB  . PRO A 69  ? 1.26613 1.21452 0.89521 -0.22943 0.22571  -0.40948 69  PRO A CB  
507  C CG  . PRO A 69  ? 1.22362 1.25514 0.81594 -0.22668 0.17269  -0.35888 69  PRO A CG  
508  C CD  . PRO A 69  ? 1.19418 1.21359 0.81336 -0.21637 0.12771  -0.32560 69  PRO A CD  
509  N N   . PRO A 70  ? 1.32236 1.08384 1.07996 -0.15414 0.28854  -0.36752 70  PRO A N   
510  C CA  . PRO A 70  ? 1.33988 1.05463 1.15375 -0.10975 0.30628  -0.32910 70  PRO A CA  
511  C C   . PRO A 70  ? 1.29697 1.06753 1.12012 -0.09506 0.30579  -0.29800 70  PRO A C   
512  O O   . PRO A 70  ? 1.25324 1.00567 1.13200 -0.05864 0.30819  -0.25991 70  PRO A O   
513  C CB  . PRO A 70  ? 1.38291 1.02191 1.21923 -0.10644 0.37327  -0.37926 70  PRO A CB  
514  C CG  . PRO A 70  ? 1.37602 1.00182 1.17744 -0.15081 0.38220  -0.43764 70  PRO A CG  
515  C CD  . PRO A 70  ? 1.33842 1.06431 1.08381 -0.18431 0.33810  -0.44330 70  PRO A CD  
516  N N   . HIS A 71  ? 1.33304 1.17511 1.10565 -0.12165 0.30417  -0.31125 71  HIS A N   
517  C CA  . HIS A 71  ? 1.30782 1.20211 1.09039 -0.11040 0.30636  -0.27464 71  HIS A CA  
518  C C   . HIS A 71  ? 1.28438 1.20811 1.07695 -0.10230 0.24864  -0.20766 71  HIS A C   
519  O O   . HIS A 71  ? 1.27875 1.25049 1.07257 -0.10253 0.24703  -0.17466 71  HIS A O   
520  C CB  . HIS A 71  ? 1.32253 1.27899 1.03947 -0.13997 0.33419  -0.31024 71  HIS A CB  
521  C CG  . HIS A 71  ? 1.33780 1.33083 0.97997 -0.17654 0.31033  -0.34362 71  HIS A CG  
522  N ND1 . HIS A 71  ? 1.36346 1.34192 0.97463 -0.20421 0.34204  -0.41992 71  HIS A ND1 
523  C CD2 . HIS A 71  ? 1.33353 1.38337 0.93046 -0.18954 0.25841  -0.31208 71  HIS A CD2 
524  C CE1 . HIS A 71  ? 1.35565 1.39186 0.90750 -0.23486 0.30587  -0.43581 71  HIS A CE1 
525  N NE2 . HIS A 71  ? 1.35578 1.43662 0.89795 -0.22271 0.25463  -0.36777 71  HIS A NE2 
526  N N   . PHE A 72  ? 1.18361 1.07480 0.98446 -0.09666 0.20730  -0.18958 72  PHE A N   
527  C CA  . PHE A 72  ? 1.07300 0.97446 0.88857 -0.08729 0.15579  -0.13335 72  PHE A CA  
528  C C   . PHE A 72  ? 0.97417 0.84960 0.86046 -0.05666 0.15453  -0.10302 72  PHE A C   
529  O O   . PHE A 72  ? 0.96610 0.79050 0.88081 -0.03603 0.15281  -0.10587 72  PHE A O   
530  C CB  . PHE A 72  ? 1.05981 0.93875 0.85483 -0.09299 0.11915  -0.13482 72  PHE A CB  
531  C CG  . PHE A 72  ? 0.99982 0.89972 0.78815 -0.09157 0.07052  -0.08779 72  PHE A CG  
532  C CD1 . PHE A 72  ? 1.01612 0.97015 0.75660 -0.10850 0.05383  -0.07716 72  PHE A CD1 
533  C CD2 . PHE A 72  ? 0.95473 0.81855 0.78189 -0.07173 0.04226  -0.05519 72  PHE A CD2 
534  C CE1 . PHE A 72  ? 1.00401 0.96632 0.74293 -0.10240 0.01429  -0.03084 72  PHE A CE1 
535  C CE2 . PHE A 72  ? 0.90027 0.77229 0.72340 -0.07123 0.00339  -0.01793 72  PHE A CE2 
536  C CZ  . PHE A 72  ? 0.91463 0.83076 0.69708 -0.08502 -0.00841 -0.00428 72  PHE A CZ  
537  N N   . LYS A 73  ? 0.89702 0.63485 0.97518 0.08287  -0.00332 -0.14811 73  LYS A N   
538  C CA  . LYS A 73  ? 0.81921 0.57260 0.90700 0.09642  -0.00160 -0.13800 73  LYS A CA  
539  C C   . LYS A 73  ? 0.75995 0.54800 0.84778 0.08418  0.00505  -0.12158 73  LYS A C   
540  O O   . LYS A 73  ? 0.70418 0.51986 0.78657 0.07627  0.01262  -0.12635 73  LYS A O   
541  C CB  . LYS A 73  ? 0.85161 0.62409 0.94443 0.11847  0.00292  -0.15641 73  LYS A CB  
542  C CG  . LYS A 73  ? 0.90520 0.64393 1.00324 0.13917  -0.00539 -0.16668 73  LYS A CG  
543  C CD  . LYS A 73  ? 0.97170 0.65993 1.06270 0.13213  -0.01508 -0.17225 73  LYS A CD  
544  C CE  . LYS A 73  ? 1.05342 0.70639 1.14822 0.15514  -0.02323 -0.18654 73  LYS A CE  
545  N NZ  . LYS A 73  ? 1.01811 0.66737 1.12360 0.17246  -0.02734 -0.17363 73  LYS A NZ  
546  N N   . TYR A 74  ? 0.72150 0.50643 0.81411 0.08280  0.00170  -0.10223 74  TYR A N   
547  C CA  . TYR A 74  ? 0.65435 0.46360 0.74491 0.06877  0.00589  -0.08614 74  TYR A CA  
548  C C   . TYR A 74  ? 0.56983 0.38389 0.66715 0.07597  0.00289  -0.07026 74  TYR A C   
549  O O   . TYR A 74  ? 0.57516 0.36049 0.67462 0.08200  -0.00495 -0.06263 74  TYR A O   
550  C CB  . TYR A 74  ? 0.64443 0.43725 0.72751 0.04872  0.00328  -0.07749 74  TYR A CB  
551  C CG  . TYR A 74  ? 0.62288 0.43468 0.70343 0.03507  0.00596  -0.05968 74  TYR A CG  
552  C CD1 . TYR A 74  ? 0.58106 0.42592 0.65831 0.02996  0.01355  -0.06132 74  TYR A CD1 
553  C CD2 . TYR A 74  ? 0.62693 0.42193 0.70743 0.02751  0.00079  -0.04161 74  TYR A CD2 
554  C CE1 . TYR A 74  ? 0.57583 0.43530 0.65031 0.01935  0.01523  -0.04677 74  TYR A CE1 
555  C CE2 . TYR A 74  ? 0.59441 0.40872 0.67185 0.01654  0.00359  -0.02721 74  TYR A CE2 
556  C CZ  . TYR A 74  ? 0.56353 0.40972 0.63806 0.01299  0.01053  -0.03032 74  TYR A CZ  
557  O OH  . TYR A 74  ? 0.59380 0.45687 0.66488 0.00390  0.01265  -0.01767 74  TYR A OH  
558  N N   . VAL A 75  ? 0.53754 0.38671 0.63749 0.07526  0.00849  -0.06535 75  VAL A N   
559  C CA  . VAL A 75  ? 0.51038 0.36947 0.61520 0.07978  0.00549  -0.05023 75  VAL A CA  
560  C C   . VAL A 75  ? 0.53220 0.41089 0.63115 0.06398  0.00926  -0.03857 75  VAL A C   
561  O O   . VAL A 75  ? 0.44722 0.35443 0.54632 0.06034  0.01605  -0.04386 75  VAL A O   
562  C CB  . VAL A 75  ? 0.55213 0.43744 0.66825 0.09676  0.00728  -0.05761 75  VAL A CB  
563  C CG1 . VAL A 75  ? 0.51614 0.41572 0.63643 0.09990  0.00353  -0.04256 75  VAL A CG1 
564  C CG2 . VAL A 75  ? 0.55439 0.42146 0.67686 0.11568  0.00323  -0.07011 75  VAL A CG2 
565  N N   . PRO A 76  ? 0.53387 0.39830 0.62728 0.05449  0.00527  -0.02275 76  PRO A N   
566  C CA  . PRO A 76  ? 0.49806 0.38206 0.58558 0.04152  0.00875  -0.01286 76  PRO A CA  
567  C C   . PRO A 76  ? 0.47121 0.38106 0.56244 0.04778  0.00892  -0.00712 76  PRO A C   
568  O O   . PRO A 76  ? 0.49668 0.40771 0.59493 0.06129  0.00477  -0.00616 76  PRO A O   
569  C CB  . PRO A 76  ? 0.51460 0.37637 0.59632 0.03153  0.00428  0.00219  76  PRO A CB  
570  C CG  . PRO A 76  ? 0.54482 0.37980 0.63050 0.04287  -0.00297 0.00627  76  PRO A CG  
571  C CD  . PRO A 76  ? 0.53683 0.36661 0.62885 0.05535  -0.00250 -0.01260 76  PRO A CD  
572  N N   . ASN A 77  ? 0.47108 0.40137 0.55730 0.03795  0.01303  -0.00368 77  ASN A N   
573  C CA  . ASN A 77  ? 0.49106 0.44576 0.57851 0.03990  0.01293  0.00134  77  ASN A CA  
574  C C   . ASN A 77  ? 0.44320 0.41154 0.54190 0.05402  0.01077  -0.00409 77  ASN A C   
575  O O   . ASN A 77  ? 0.42611 0.39693 0.52703 0.06180  0.00481  0.00447  77  ASN A O   
576  C CB  . ASN A 77  ? 0.45994 0.41098 0.54019 0.03618  0.00864  0.01792  77  ASN A CB  
577  C CG  . ASN A 77  ? 0.49806 0.42130 0.57712 0.03924  0.00285  0.02805  77  ASN A CG  
578  O OD1 . ASN A 77  ? 0.48723 0.39286 0.56103 0.02918  0.00326  0.03302  77  ASN A OD1 
579  N ND2 . ASN A 77  ? 0.47496 0.39439 0.55902 0.05273  -0.00308 0.03208  77  ASN A ND2 
580  N N   . VAL A 78  ? 0.46611 0.44680 0.57184 0.05729  0.01577  -0.01806 78  VAL A N   
581  C CA  . VAL A 78  ? 0.44396 0.44255 0.56288 0.07069  0.01466  -0.02483 78  VAL A CA  
582  C C   . VAL A 78  ? 0.43014 0.45484 0.55325 0.07052  0.01251  -0.01987 78  VAL A C   
583  O O   . VAL A 78  ? 0.43783 0.47888 0.57276 0.08216  0.00915  -0.02254 78  VAL A O   
584  C CB  . VAL A 78  ? 0.43710 0.44871 0.56205 0.07226  0.02223  -0.04058 78  VAL A CB  
585  C CG1 . VAL A 78  ? 0.47825 0.46375 0.59976 0.07630  0.02243  -0.04801 78  VAL A CG1 
586  C CG2 . VAL A 78  ? 0.37287 0.40046 0.49227 0.05798  0.02965  -0.04293 78  VAL A CG2 
587  N N   . ALA A 79  ? 0.44118 0.47070 0.55505 0.05839  0.01357  -0.01341 79  ALA A N   
588  C CA  . ALA A 79  ? 0.40928 0.46179 0.52587 0.05792  0.01049  -0.01024 79  ALA A CA  
589  C C   . ALA A 79  ? 0.44585 0.49726 0.56437 0.06949  0.00137  -0.00102 79  ALA A C   
590  O O   . ALA A 79  ? 0.47799 0.55223 0.60529 0.07573  -0.00273 -0.00263 79  ALA A O   
591  C CB  . ALA A 79  ? 0.41693 0.47025 0.52116 0.04464  0.01255  -0.00565 79  ALA A CB  
592  N N   . THR A 80  ? 0.41803 0.44352 0.52865 0.07226  -0.00233 0.00912  80  THR A N   
593  C CA  . THR A 80  ? 0.46851 0.49033 0.57745 0.08246  -0.01115 0.02107  80  THR A CA  
594  C C   . THR A 80  ? 0.49871 0.51655 0.61940 0.09988  -0.01626 0.01810  80  THR A C   
595  O O   . THR A 80  ? 0.50542 0.52507 0.62636 0.11090  -0.02451 0.02724  80  THR A O   
596  C CB  . THR A 80  ? 0.47403 0.46943 0.56882 0.07685  -0.01298 0.03602  80  THR A CB  
597  O OG1 . THR A 80  ? 0.49880 0.46523 0.59459 0.07760  -0.01186 0.03440  80  THR A OG1 
598  C CG2 . THR A 80  ? 0.44764 0.44861 0.53124 0.06139  -0.00784 0.03861  80  THR A CG2 
599  N N   . THR A 81  ? 0.48822 0.50079 0.61763 0.10392  -0.01194 0.00562  81  THR A N   
600  C CA  . THR A 81  ? 0.52475 0.53188 0.66522 0.12249  -0.01659 0.00107  81  THR A CA  
601  C C   . THR A 81  ? 0.47957 0.51762 0.63683 0.12979  -0.01252 -0.01498 81  THR A C   
602  O O   . THR A 81  ? 0.52680 0.56754 0.69533 0.14761  -0.01665 -0.01987 81  THR A O   
603  C CB  . THR A 81  ? 0.52948 0.49807 0.66537 0.12480  -0.01647 -0.00019 81  THR A CB  
604  O OG1 . THR A 81  ? 0.54129 0.50749 0.67375 0.11171  -0.00752 -0.01034 81  THR A OG1 
605  C CG2 . THR A 81  ? 0.55606 0.49260 0.67872 0.12096  -0.02248 0.01789  81  THR A CG2 
606  N N   . CYS A 82  ? 0.48091 0.54260 0.64046 0.11706  -0.00457 -0.02289 82  CYS A N   
607  C CA  . CYS A 82  ? 0.48950 0.58268 0.66531 0.12156  0.00075  -0.03714 82  CYS A CA  
608  C C   . CYS A 82  ? 0.45450 0.58222 0.63635 0.11211  0.00157  -0.03738 82  CYS A C   
609  O O   . CYS A 82  ? 0.42102 0.55231 0.59603 0.09538  0.00789  -0.03837 82  CYS A O   
610  C CB  . CYS A 82  ? 0.48128 0.56802 0.65447 0.11482  0.01080  -0.04814 82  CYS A CB  
611  S SG  . CYS A 82  ? 0.52006 0.56196 0.68441 0.12336  0.00857  -0.04951 82  CYS A SG  
612  N N   . PRO A 83  ? 0.44921 0.60217 0.64391 0.12259  -0.00539 -0.03694 83  PRO A N   
613  C CA  . PRO A 83  ? 0.40380 0.58904 0.60476 0.11252  -0.00620 -0.03801 83  PRO A CA  
614  C C   . PRO A 83  ? 0.39585 0.60265 0.60447 0.09880  0.00434  -0.04847 83  PRO A C   
615  O O   . PRO A 83  ? 0.38748 0.60176 0.59143 0.08288  0.00610  -0.04735 83  PRO A O   
616  C CB  . PRO A 83  ? 0.40788 0.61965 0.62541 0.12945  -0.01536 -0.03891 83  PRO A CB  
617  C CG  . PRO A 83  ? 0.46151 0.64531 0.67423 0.14762  -0.02173 -0.03242 83  PRO A CG  
618  C CD  . PRO A 83  ? 0.45001 0.60296 0.65439 0.14459  -0.01360 -0.03612 83  PRO A CD  
619  N N   . THR A 84  ? 0.40326 0.61936 0.62248 0.10479  0.01145  -0.05848 84  THR A N   
620  C CA  . THR A 84  ? 0.40041 0.63784 0.62568 0.09139  0.02240  -0.06676 84  THR A CA  
621  C C   . THR A 84  ? 0.41864 0.63234 0.62464 0.07343  0.02837  -0.06279 84  THR A C   
622  O O   . THR A 84  ? 0.39669 0.62386 0.60288 0.05763  0.03321  -0.06370 84  THR A O   
623  C CB  . THR A 84  ? 0.43215 0.68112 0.66823 0.10246  0.02970  -0.07786 84  THR A CB  
624  O OG1 . THR A 84  ? 0.43688 0.70873 0.69164 0.12158  0.02353  -0.08193 84  THR A OG1 
625  C CG2 . THR A 84  ? 0.42749 0.70354 0.67008 0.08811  0.04150  -0.08471 84  THR A CG2 
626  N N   . PHE A 85  ? 0.40749 0.58573 0.59716 0.07530  0.02766  -0.05818 85  PHE A N   
627  C CA  . PHE A 85  ? 0.41320 0.57217 0.58546 0.05933  0.03202  -0.05396 85  PHE A CA  
628  C C   . PHE A 85  ? 0.40704 0.56636 0.57282 0.05012  0.02644  -0.04606 85  PHE A C   
629  O O   . PHE A 85  ? 0.38068 0.54353 0.54115 0.03587  0.03039  -0.04617 85  PHE A O   
630  C CB  . PHE A 85  ? 0.39989 0.52395 0.55765 0.06204  0.03182  -0.05095 85  PHE A CB  
631  C CG  . PHE A 85  ? 0.38505 0.49373 0.52668 0.04703  0.03652  -0.04788 85  PHE A CG  
632  C CD1 . PHE A 85  ? 0.39823 0.51140 0.53690 0.03989  0.04556  -0.05461 85  PHE A CD1 
633  C CD2 . PHE A 85  ? 0.38123 0.47419 0.51052 0.04066  0.03196  -0.03809 85  PHE A CD2 
634  C CE1 . PHE A 85  ? 0.41442 0.51441 0.53811 0.02751  0.04900  -0.05135 85  PHE A CE1 
635  C CE2 . PHE A 85  ? 0.41226 0.49394 0.52801 0.02862  0.03591  -0.03588 85  PHE A CE2 
636  C CZ  . PHE A 85  ? 0.36929 0.45362 0.48231 0.02239  0.04397  -0.04239 85  PHE A CZ  
637  N N   . ARG A 86  ? 0.40886 0.56473 0.57440 0.05894  0.01693  -0.03941 86  ARG A N   
638  C CA  . ARG A 86  ? 0.45388 0.60815 0.60991 0.05202  0.01124  -0.03224 86  ARG A CA  
639  C C   . ARG A 86  ? 0.41889 0.60237 0.58543 0.04447  0.01003  -0.03745 86  ARG A C   
640  O O   . ARG A 86  ? 0.44407 0.62531 0.60173 0.03283  0.00959  -0.03621 86  ARG A O   
641  C CB  . ARG A 86  ? 0.38147 0.52583 0.53323 0.06425  0.00168  -0.02291 86  ARG A CB  
642  C CG  . ARG A 86  ? 0.42831 0.57765 0.57126 0.06077  -0.00524 -0.01634 86  ARG A CG  
643  C CD  . ARG A 86  ? 0.41077 0.54746 0.54610 0.07248  -0.01345 -0.00459 86  ARG A CD  
644  N NE  . ARG A 86  ? 0.37551 0.52890 0.52402 0.08754  -0.02106 -0.00485 86  ARG A NE  
645  C CZ  . ARG A 86  ? 0.39992 0.54142 0.55356 0.10160  -0.02338 -0.00224 86  ARG A CZ  
646  N NH1 . ARG A 86  ? 0.41186 0.52380 0.55892 0.10141  -0.01886 0.00009  86  ARG A NH1 
647  N NH2 . ARG A 86  ? 0.39760 0.55653 0.56303 0.11666  -0.03134 -0.00227 86  ARG A NH2 
648  N N   . ASN A 87  ? 0.42178 0.63323 0.60793 0.05071  0.00932  -0.04406 87  ASN A N   
649  C CA  . ASN A 87  ? 0.41446 0.65633 0.61340 0.04289  0.00675  -0.04908 87  ASN A CA  
650  C C   . ASN A 87  ? 0.41119 0.66886 0.61955 0.02936  0.01667  -0.05637 87  ASN A C   
651  O O   . ASN A 87  ? 0.43043 0.70880 0.64775 0.01812  0.01526  -0.05993 87  ASN A O   
652  C CB  . ASN A 87  ? 0.37925 0.64879 0.59618 0.05734  -0.00153 -0.05127 87  ASN A CB  
653  C CG  . ASN A 87  ? 0.40519 0.66330 0.61171 0.06857  -0.01289 -0.04239 87  ASN A CG  
654  O OD1 . ASN A 87  ? 0.38788 0.63381 0.57882 0.06119  -0.01654 -0.03732 87  ASN A OD1 
655  N ND2 . ASN A 87  ? 0.40767 0.66876 0.62151 0.08729  -0.01835 -0.04008 87  ASN A ND2 
656  N N   . THR A 88  ? 0.39062 0.63919 0.59656 0.02932  0.02641  -0.05851 88  THR A N   
657  C CA  . THR A 88  ? 0.39005 0.65782 0.60525 0.01761  0.03642  -0.06429 88  THR A CA  
658  C C   . THR A 88  ? 0.37447 0.61697 0.57180 0.00817  0.04519  -0.06205 88  THR A C   
659  O O   . THR A 88  ? 0.39423 0.63413 0.58580 -0.00782 0.04886  -0.06056 88  THR A O   
660  C CB  . THR A 88  ? 0.38631 0.68287 0.62146 0.02928  0.04061  -0.07174 88  THR A CB  
661  O OG1 . THR A 88  ? 0.40537 0.72948 0.65872 0.03829  0.03171  -0.07392 88  THR A OG1 
662  C CG2 . THR A 88  ? 0.36673 0.68605 0.61056 0.01635  0.05246  -0.07655 88  THR A CG2 
663  N N   . VAL A 89  ? 0.35182 0.57428 0.53981 0.01800  0.04767  -0.06178 89  VAL A N   
664  C CA  . VAL A 89  ? 0.35926 0.56314 0.53194 0.01023  0.05599  -0.06114 89  VAL A CA  
665  C C   . VAL A 89  ? 0.37470 0.55151 0.52838 0.00106  0.05282  -0.05376 89  VAL A C   
666  O O   . VAL A 89  ? 0.37373 0.54324 0.51738 -0.01094 0.05833  -0.05218 89  VAL A O   
667  C CB  . VAL A 89  ? 0.38840 0.58019 0.55758 0.02316  0.05866  -0.06508 89  VAL A CB  
668  C CG1 . VAL A 89  ? 0.35148 0.52686 0.50435 0.01523  0.06632  -0.06517 89  VAL A CG1 
669  C CG2 . VAL A 89  ? 0.37656 0.59698 0.56463 0.03422  0.06212  -0.07394 89  VAL A CG2 
670  N N   . LEU A 90  ? 0.38269 0.54532 0.53075 0.00727  0.04402  -0.04873 90  LEU A N   
671  C CA  . LEU A 90  ? 0.37726 0.51739 0.50781 0.00072  0.04116  -0.04232 90  LEU A CA  
672  C C   . LEU A 90  ? 0.41616 0.56172 0.54475 -0.01227 0.04080  -0.04222 90  LEU A C   
673  O O   . LEU A 90  ? 0.40855 0.53650 0.52233 -0.01932 0.04166  -0.03900 90  LEU A O   
674  C CB  . LEU A 90  ? 0.36517 0.49546 0.49163 0.00985  0.03222  -0.03648 90  LEU A CB  
675  C CG  . LEU A 90  ? 0.34685 0.46120 0.45722 0.00480  0.02854  -0.03016 90  LEU A CG  
676  C CD1 . LEU A 90  ? 0.29213 0.38528 0.38866 0.00115  0.03324  -0.02750 90  LEU A CD1 
677  C CD2 . LEU A 90  ? 0.35368 0.46641 0.46180 0.01357  0.01999  -0.02390 90  LEU A CD2 
678  N N   . ILE A 91  ? 0.37178 0.54099 0.51541 -0.01541 0.03884  -0.04611 91  ILE A N   
679  C CA  . ILE A 91  ? 0.37262 0.54448 0.51511 -0.02810 0.03650  -0.04682 91  ILE A CA  
680  C C   . ILE A 91  ? 0.38141 0.56730 0.53289 -0.04093 0.04439  -0.04987 91  ILE A C   
681  O O   . ILE A 91  ? 0.36536 0.55874 0.52200 -0.05265 0.04224  -0.05161 91  ILE A O   
682  C CB  . ILE A 91  ? 0.37138 0.55853 0.52257 -0.02449 0.02623  -0.04869 91  ILE A CB  
683  C CG1 . ILE A 91  ? 0.35843 0.57583 0.53159 -0.01738 0.02563  -0.05304 91  ILE A CG1 
684  C CG2 . ILE A 91  ? 0.33969 0.51044 0.47718 -0.01394 0.01915  -0.04334 91  ILE A CG2 
685  C CD1 . ILE A 91  ? 0.39727 0.63533 0.58111 -0.01384 0.01485  -0.05557 91  ILE A CD1 
686  N N   . ASN A 92  ? 0.38052 0.57001 0.53336 -0.03943 0.05347  -0.05053 92  ASN A N   
687  C CA  . ASN A 92  ? 0.37623 0.58357 0.53792 -0.05120 0.06222  -0.05229 92  ASN A CA  
688  C C   . ASN A 92  ? 0.36786 0.55793 0.51761 -0.06753 0.06330  -0.04805 92  ASN A C   
689  O O   . ASN A 92  ? 0.37089 0.53311 0.50115 -0.06728 0.06317  -0.04376 92  ASN A O   
690  C CB  . ASN A 92  ? 0.38182 0.59155 0.54062 -0.04586 0.07203  -0.05351 92  ASN A CB  
691  C CG  . ASN A 92  ? 0.36139 0.59001 0.52607 -0.05853 0.08247  -0.05365 92  ASN A CG  
692  O OD1 . ASN A 92  ? 0.37544 0.58855 0.52597 -0.06996 0.08711  -0.04837 92  ASN A OD1 
693  N ND2 . ASN A 92  ? 0.34115 0.60481 0.52692 -0.05652 0.08621  -0.05900 92  ASN A ND2 
694  N N   . PRO A 93  ? 0.37537 0.58064 0.53663 -0.08185 0.06393  -0.04910 93  PRO A N   
695  C CA  . PRO A 93  ? 0.38676 0.56981 0.53615 -0.09666 0.06237  -0.04530 93  PRO A CA  
696  C C   . PRO A 93  ? 0.38273 0.54790 0.51611 -0.10362 0.07153  -0.03874 93  PRO A C   
697  O O   . PRO A 93  ? 0.37624 0.51283 0.49290 -0.10910 0.06901  -0.03453 93  PRO A O   
698  C CB  . PRO A 93  ? 0.44381 0.65062 0.61295 -0.11126 0.06081  -0.04861 93  PRO A CB  
699  C CG  . PRO A 93  ? 0.40833 0.65227 0.60007 -0.10121 0.05966  -0.05467 93  PRO A CG  
700  C CD  . PRO A 93  ? 0.35299 0.59640 0.53938 -0.08536 0.06562  -0.05400 93  PRO A CD  
701  N N   . VAL A 94  ? 0.38883 0.57052 0.52589 -0.10229 0.08174  -0.03808 94  VAL A N   
702  C CA  . VAL A 94  ? 0.40229 0.56893 0.52203 -0.10770 0.09022  -0.03149 94  VAL A CA  
703  C C   . VAL A 94  ? 0.38512 0.52465 0.48459 -0.09547 0.08729  -0.02989 94  VAL A C   
704  O O   . VAL A 94  ? 0.36430 0.47871 0.44533 -0.09978 0.08732  -0.02389 94  VAL A O   
705  C CB  . VAL A 94  ? 0.39029 0.58574 0.51860 -0.10877 0.10217  -0.03238 94  VAL A CB  
706  C CG1 . VAL A 94  ? 0.34200 0.52258 0.44971 -0.11387 0.11044  -0.02499 94  VAL A CG1 
707  C CG2 . VAL A 94  ? 0.37614 0.60279 0.52661 -0.12201 0.10553  -0.03355 94  VAL A CG2 
708  N N   . ILE A 95  ? 0.37928 0.52377 0.48239 -0.08023 0.08450  -0.03491 95  ILE A N   
709  C CA  . ILE A 95  ? 0.36132 0.48224 0.44793 -0.07014 0.08089  -0.03354 95  ILE A CA  
710  C C   . ILE A 95  ? 0.39358 0.49049 0.46854 -0.07308 0.07324  -0.02981 95  ILE A C   
711  O O   . ILE A 95  ? 0.38730 0.46333 0.44492 -0.07229 0.07305  -0.02571 95  ILE A O   
712  C CB  . ILE A 95  ? 0.40614 0.53362 0.50080 -0.05527 0.07698  -0.03870 95  ILE A CB  
713  C CG1 . ILE A 95  ? 0.39207 0.54051 0.49645 -0.04941 0.08432  -0.04417 95  ILE A CG1 
714  C CG2 . ILE A 95  ? 0.43097 0.53446 0.51025 -0.04771 0.07244  -0.03635 95  ILE A CG2 
715  C CD1 . ILE A 95  ? 0.42116 0.56427 0.51142 -0.05094 0.09250  -0.04342 95  ILE A CD1 
716  N N   . HIS A 96  ? 0.37032 0.47148 0.45457 -0.07588 0.06653  -0.03202 96  HIS A N   
717  C CA  . HIS A 96  ? 0.41601 0.49572 0.48889 -0.07657 0.05884  -0.03060 96  HIS A CA  
718  C C   . HIS A 96  ? 0.39532 0.45741 0.45797 -0.08893 0.06026  -0.02657 96  HIS A C   
719  O O   . HIS A 96  ? 0.38375 0.42262 0.43097 -0.08650 0.05612  -0.02444 96  HIS A O   
720  C CB  . HIS A 96  ? 0.39993 0.49057 0.48427 -0.07396 0.05039  -0.03548 96  HIS A CB  
721  C CG  . HIS A 96  ? 0.39945 0.49743 0.48714 -0.05990 0.04726  -0.03663 96  HIS A CG  
722  N ND1 . HIS A 96  ? 0.33268 0.41463 0.40700 -0.05136 0.04381  -0.03394 96  HIS A ND1 
723  C CD2 . HIS A 96  ? 0.39249 0.51067 0.49466 -0.05278 0.04787  -0.03921 96  HIS A CD2 
724  C CE1 . HIS A 96  ? 0.41103 0.50120 0.49119 -0.04114 0.04204  -0.03397 96  HIS A CE1 
725  N NE2 . HIS A 96  ? 0.41806 0.52856 0.51456 -0.04083 0.04403  -0.03735 96  HIS A NE2 
726  N N   . ALA A 97  ? 0.38888 0.46139 0.45951 -0.10184 0.06622  -0.02490 97  ALA A N   
727  C CA  . ALA A 97  ? 0.43787 0.48967 0.49643 -0.11398 0.06844  -0.01857 97  ALA A CA  
728  C C   . ALA A 97  ? 0.43605 0.47018 0.47448 -0.10824 0.07251  -0.01230 97  ALA A C   
729  O O   . ALA A 97  ? 0.41345 0.42082 0.43568 -0.10875 0.06906  -0.00812 97  ALA A O   
730  C CB  . ALA A 97  ? 0.39284 0.46237 0.46421 -0.13023 0.07566  -0.01611 97  ALA A CB  
731  N N   . ILE A 98  ? 0.43196 0.48090 0.47101 -0.10159 0.07898  -0.01252 98  ILE A N   
732  C CA  . ILE A 98  ? 0.42686 0.46214 0.44740 -0.09517 0.08150  -0.00819 98  ILE A CA  
733  C C   . ILE A 98  ? 0.41421 0.43196 0.42513 -0.08404 0.07321  -0.00963 98  ILE A C   
734  O O   . ILE A 98  ? 0.46478 0.46247 0.45911 -0.08221 0.07131  -0.00495 98  ILE A O   
735  C CB  . ILE A 98  ? 0.45544 0.51088 0.47949 -0.08942 0.08876  -0.01102 98  ILE A CB  
736  C CG1 . ILE A 98  ? 0.49075 0.56693 0.52303 -0.10019 0.09836  -0.00920 98  ILE A CG1 
737  C CG2 . ILE A 98  ? 0.39086 0.43355 0.39603 -0.08240 0.08966  -0.00827 98  ILE A CG2 
738  C CD1 . ILE A 98  ? 0.45887 0.56268 0.50387 -0.09300 0.10387  -0.01652 98  ILE A CD1 
739  N N   . CYS A 99  ? 0.41318 0.43987 0.43430 -0.07603 0.06830  -0.01548 99  CYS A N   
740  C CA  . CYS A 99  ? 0.44522 0.46006 0.45815 -0.06594 0.06166  -0.01615 99  CYS A CA  
741  C C   . CYS A 99  ? 0.42112 0.41625 0.42426 -0.06755 0.05567  -0.01479 99  CYS A C   
742  O O   . CYS A 99  ? 0.39285 0.37358 0.38228 -0.06160 0.05320  -0.01238 99  CYS A O   
743  C CB  . CYS A 99  ? 0.40015 0.42818 0.42542 -0.05857 0.05761  -0.02088 99  CYS A CB  
744  S SG  . CYS A 99  ? 0.44861 0.49083 0.48132 -0.05121 0.06188  -0.02324 99  CYS A SG  
745  N N   . GLU A 100 ? 0.43993 0.43498 0.45054 -0.07501 0.05270  -0.01734 100 GLU A N   
746  C CA  . GLU A 100 ? 0.47455 0.44833 0.47567 -0.07639 0.04627  -0.01802 100 GLU A CA  
747  C C   . GLU A 100 ? 0.48942 0.44056 0.47422 -0.07917 0.04837  -0.01126 100 GLU A C   
748  O O   . GLU A 100 ? 0.51198 0.44390 0.48373 -0.07244 0.04321  -0.01111 100 GLU A O   
749  C CB  . GLU A 100 ? 0.54280 0.51983 0.55532 -0.08700 0.04298  -0.02241 100 GLU A CB  
750  C CG  . GLU A 100 ? 0.62905 0.62332 0.65317 -0.08166 0.03718  -0.02968 100 GLU A CG  
751  C CD  . GLU A 100 ? 0.76068 0.76162 0.79741 -0.09311 0.03331  -0.03490 100 GLU A CD  
752  O OE1 . GLU A 100 ? 0.73893 0.73817 0.78045 -0.10697 0.03764  -0.03194 100 GLU A OE1 
753  O OE2 . GLU A 100 ? 0.79750 0.80646 0.83902 -0.08883 0.02585  -0.04168 100 GLU A OE2 
754  N N   . ALA A 101 ? 0.42743 0.38156 0.41206 -0.08814 0.05590  -0.00535 101 ALA A N   
755  C CA  . ALA A 101 ? 0.46692 0.39965 0.43424 -0.09053 0.05788  0.00300  101 ALA A CA  
756  C C   . ALA A 101 ? 0.45243 0.38358 0.40723 -0.07783 0.05799  0.00517  101 ALA A C   
757  O O   . ALA A 101 ? 0.46816 0.37902 0.40765 -0.07216 0.05417  0.00884  101 ALA A O   
758  C CB  . ALA A 101 ? 0.48135 0.42134 0.45116 -0.10421 0.06670  0.00970  101 ALA A CB  
759  N N   . TYR A 102 ? 0.43835 0.39067 0.40001 -0.07305 0.06168  0.00241  102 TYR A N   
760  C CA  . TYR A 102 ? 0.44492 0.39831 0.39671 -0.06320 0.06163  0.00361  102 TYR A CA  
761  C C   . TYR A 102 ? 0.42961 0.37637 0.37769 -0.05231 0.05414  0.00067  102 TYR A C   
762  O O   . TYR A 102 ? 0.42702 0.36651 0.36293 -0.04522 0.05199  0.00348  102 TYR A O   
763  C CB  . TYR A 102 ? 0.39797 0.37344 0.35963 -0.06169 0.06650  -0.00033 102 TYR A CB  
764  C CG  . TYR A 102 ? 0.44736 0.42656 0.40229 -0.05307 0.06576  -0.00129 102 TYR A CG  
765  C CD1 . TYR A 102 ? 0.42942 0.40630 0.37063 -0.05310 0.06889  0.00285  102 TYR A CD1 
766  C CD2 . TYR A 102 ? 0.41187 0.39799 0.37443 -0.04609 0.06186  -0.00601 102 TYR A CD2 
767  C CE1 . TYR A 102 ? 0.48708 0.46917 0.42347 -0.04630 0.06729  0.00060  102 TYR A CE1 
768  C CE2 . TYR A 102 ? 0.39340 0.38315 0.35140 -0.04067 0.06096  -0.00703 102 TYR A CE2 
769  C CZ  . TYR A 102 ? 0.42757 0.41601 0.37312 -0.04073 0.06331  -0.00465 102 TYR A CZ  
770  O OH  . TYR A 102 ? 0.43404 0.42756 0.37599 -0.03628 0.06148  -0.00693 102 TYR A OH  
771  N N   . PHE A 103 ? 0.39051 0.34265 0.34889 -0.05036 0.05018  -0.00489 103 PHE A N   
772  C CA  . PHE A 103 ? 0.41925 0.36993 0.37472 -0.04016 0.04414  -0.00777 103 PHE A CA  
773  C C   . PHE A 103 ? 0.48321 0.41505 0.43041 -0.03791 0.03830  -0.00921 103 PHE A C   
774  O O   . PHE A 103 ? 0.46359 0.39715 0.40944 -0.02931 0.03347  -0.01321 103 PHE A O   
775  C CB  . PHE A 103 ? 0.38982 0.35750 0.35857 -0.03789 0.04282  -0.01238 103 PHE A CB  
776  C CG  . PHE A 103 ? 0.39627 0.37851 0.37164 -0.03651 0.04653  -0.01189 103 PHE A CG  
777  C CD1 . PHE A 103 ? 0.39964 0.38422 0.36973 -0.03048 0.04594  -0.01032 103 PHE A CD1 
778  C CD2 . PHE A 103 ? 0.35736 0.35116 0.34495 -0.04103 0.05008  -0.01377 103 PHE A CD2 
779  C CE1 . PHE A 103 ? 0.37598 0.37074 0.35216 -0.03022 0.04843  -0.01088 103 PHE A CE1 
780  C CE2 . PHE A 103 ? 0.36984 0.37345 0.36279 -0.03859 0.05276  -0.01458 103 PHE A CE2 
781  C CZ  . PHE A 103 ? 0.36590 0.36817 0.35274 -0.03377 0.05166  -0.01325 103 PHE A CZ  
782  N N   . GLN A 104 ? 0.45898 0.37247 0.40004 -0.04537 0.03868  -0.00607 104 GLN A N   
783  C CA  . GLN A 104 ? 0.51211 0.40347 0.44575 -0.04386 0.03223  -0.00882 104 GLN A CA  
784  C C   . GLN A 104 ? 0.50179 0.38562 0.42359 -0.02888 0.02726  -0.01011 104 GLN A C   
785  O O   . GLN A 104 ? 0.52029 0.39689 0.43943 -0.02223 0.02127  -0.01670 104 GLN A O   
786  C CB  . GLN A 104 ? 0.52575 0.39450 0.45246 -0.05474 0.03364  -0.00265 104 GLN A CB  
787  C CG  . GLN A 104 ? 0.67276 0.51366 0.59327 -0.05616 0.02630  -0.00642 104 GLN A CG  
788  C CD  . GLN A 104 ? 0.74968 0.56973 0.65380 -0.04105 0.02011  -0.00699 104 GLN A CD  
789  O OE1 . GLN A 104 ? 0.76224 0.57638 0.65526 -0.03501 0.02166  0.00051  104 GLN A OE1 
790  N NE2 . GLN A 104 ? 0.75911 0.56986 0.66154 -0.03384 0.01269  -0.01669 104 GLN A NE2 
791  N N   . ARG A 105 ? 0.49162 0.37914 0.40632 -0.02293 0.02946  -0.00468 105 ARG A N   
792  C CA  . ARG A 105 ? 0.50130 0.38481 0.40582 -0.00842 0.02484  -0.00543 105 ARG A CA  
793  C C   . ARG A 105 ? 0.47550 0.38285 0.38770 -0.00019 0.02387  -0.01076 105 ARG A C   
794  O O   . ARG A 105 ? 0.46847 0.37522 0.37566 0.01138  0.01934  -0.01494 105 ARG A O   
795  C CB  . ARG A 105 ? 0.47296 0.35448 0.36751 -0.00538 0.02670  0.00238  105 ARG A CB  
796  C CG  . ARG A 105 ? 0.51385 0.37033 0.39689 -0.01192 0.02746  0.01010  105 ARG A CG  
797  C CD  . ARG A 105 ? 0.53083 0.39116 0.40368 -0.00930 0.02982  0.01823  105 ARG A CD  
798  N NE  . ARG A 105 ? 0.57314 0.43511 0.43809 0.00657  0.02421  0.01762  105 ARG A NE  
799  C CZ  . ARG A 105 ? 0.54933 0.42717 0.41077 0.01220  0.02447  0.02031  105 ARG A CZ  
800  N NH1 . ARG A 105 ? 0.53060 0.42204 0.39391 0.00387  0.02997  0.02316  105 ARG A NH1 
801  N NH2 . ARG A 105 ? 0.50137 0.38345 0.35787 0.02697  0.01878  0.01899  105 ARG A NH2 
802  N N   . THR A 106 ? 0.46359 0.39185 0.38749 -0.00556 0.02809  -0.01047 106 THR A N   
803  C CA  . THR A 106 ? 0.43667 0.38581 0.36729 0.00058  0.02737  -0.01338 106 THR A CA  
804  C C   . THR A 106 ? 0.45187 0.40516 0.38844 0.00002  0.02501  -0.01901 106 THR A C   
805  O O   . THR A 106 ? 0.40302 0.37057 0.34091 0.00715  0.02340  -0.02131 106 THR A O   
806  C CB  . THR A 106 ? 0.41286 0.37953 0.35225 -0.00400 0.03188  -0.01019 106 THR A CB  
807  O OG1 . THR A 106 ? 0.41815 0.40242 0.36084 0.00234  0.03092  -0.01040 106 THR A OG1 
808  C CG2 . THR A 106 ? 0.37810 0.35021 0.32896 -0.01278 0.03472  -0.01127 106 THR A CG2 
809  N N   . GLY A 107 ? 0.43109 0.37433 0.37104 -0.00845 0.02461  -0.02114 107 GLY A N   
810  C CA  . GLY A 107 ? 0.40182 0.35052 0.34722 -0.00910 0.02123  -0.02725 107 GLY A CA  
811  C C   . GLY A 107 ? 0.41817 0.38350 0.37745 -0.01627 0.02421  -0.02602 107 GLY A C   
812  O O   . GLY A 107 ? 0.38793 0.35372 0.35295 -0.02401 0.02878  -0.02243 107 GLY A O   
813  N N   . ASP A 108 ? 0.32269 0.30242 0.28654 -0.01261 0.02164  -0.02885 108 ASP A N   
814  C CA  . ASP A 108 ? 0.38607 0.38068 0.36273 -0.01717 0.02299  -0.02773 108 ASP A CA  
815  C C   . ASP A 108 ? 0.32615 0.32950 0.30814 -0.01735 0.02806  -0.02153 108 ASP A C   
816  O O   . ASP A 108 ? 0.33905 0.34356 0.31565 -0.01281 0.02939  -0.01831 108 ASP A O   
817  C CB  . ASP A 108 ? 0.35709 0.36472 0.33449 -0.01160 0.01830  -0.03080 108 ASP A CB  
818  C CG  . ASP A 108 ? 0.40985 0.41286 0.38689 -0.01421 0.01241  -0.03902 108 ASP A CG  
819  O OD1 . ASP A 108 ? 0.45495 0.44478 0.43396 -0.02246 0.01225  -0.04163 108 ASP A OD1 
820  O OD2 . ASP A 108 ? 0.44052 0.45371 0.41497 -0.00867 0.00769  -0.04285 108 ASP A OD2 
821  N N   . TYR A 109 ? 0.30378 0.31440 0.29722 -0.02229 0.03033  -0.02081 109 TYR A N   
822  C CA  . TYR A 109 ? 0.29721 0.31392 0.29667 -0.02242 0.03432  -0.01696 109 TYR A CA  
823  C C   . TYR A 109 ? 0.30025 0.32902 0.31034 -0.02053 0.03249  -0.01651 109 TYR A C   
824  O O   . TYR A 109 ? 0.32638 0.36073 0.34037 -0.02059 0.02877  -0.01951 109 TYR A O   
825  C CB  . TYR A 109 ? 0.33972 0.35180 0.34140 -0.02877 0.03950  -0.01722 109 TYR A CB  
826  C CG  . TYR A 109 ? 0.35153 0.36775 0.36232 -0.03495 0.03994  -0.02051 109 TYR A CG  
827  C CD1 . TYR A 109 ? 0.37726 0.38452 0.38409 -0.04035 0.03827  -0.02254 109 TYR A CD1 
828  C CD2 . TYR A 109 ? 0.33631 0.36575 0.36045 -0.03511 0.04141  -0.02180 109 TYR A CD2 
829  C CE1 . TYR A 109 ? 0.38050 0.39437 0.39781 -0.04790 0.03849  -0.02547 109 TYR A CE1 
830  C CE2 . TYR A 109 ? 0.34493 0.38306 0.37947 -0.04072 0.04170  -0.02508 109 TYR A CE2 
831  C CZ  . TYR A 109 ? 0.38682 0.41866 0.41891 -0.04825 0.04034  -0.02688 109 TYR A CZ  
832  O OH  . TYR A 109 ? 0.41478 0.45783 0.45924 -0.05564 0.04053  -0.03007 109 TYR A OH  
833  N N   . TRP A 110 ? 0.29359 0.32566 0.30797 -0.01845 0.03415  -0.01278 110 TRP A N   
834  C CA  . TRP A 110 ? 0.30162 0.34198 0.32622 -0.01577 0.03223  -0.01162 110 TRP A CA  
835  C C   . TRP A 110 ? 0.30164 0.33904 0.33193 -0.01553 0.03543  -0.01020 110 TRP A C   
836  O O   . TRP A 110 ? 0.31743 0.34841 0.34367 -0.01822 0.03899  -0.01096 110 TRP A O   
837  C CB  . TRP A 110 ? 0.28686 0.33343 0.30816 -0.01052 0.02756  -0.00723 110 TRP A CB  
838  C CG  . TRP A 110 ? 0.28060 0.32574 0.29375 -0.00890 0.02825  -0.00149 110 TRP A CG  
839  C CD1 . TRP A 110 ? 0.24829 0.28758 0.25919 -0.01142 0.03166  0.00023  110 TRP A CD1 
840  C CD2 . TRP A 110 ? 0.26154 0.31481 0.26816 -0.00477 0.02550  0.00310  110 TRP A CD2 
841  N NE1 . TRP A 110 ? 0.27706 0.32138 0.28246 -0.00989 0.03123  0.00573  110 TRP A NE1 
842  C CE2 . TRP A 110 ? 0.26184 0.31505 0.26419 -0.00573 0.02809  0.00800  110 TRP A CE2 
843  C CE3 . TRP A 110 ? 0.25293 0.31582 0.25672 -0.00041 0.02108  0.00340  110 TRP A CE3 
844  C CZ2 . TRP A 110 ? 0.25372 0.31749 0.24970 -0.00288 0.02748  0.01369  110 TRP A CZ2 
845  C CZ3 . TRP A 110 ? 0.29238 0.36441 0.28764 0.00332  0.02030  0.00891  110 TRP A CZ3 
846  C CH2 . TRP A 110 ? 0.29826 0.37128 0.29013 0.00186  0.02401  0.01440  110 TRP A CH2 
847  N N   . LEU A 111 ? 0.29887 0.34032 0.33794 -0.01145 0.03339  -0.00864 111 LEU A N   
848  C CA  . LEU A 111 ? 0.34585 0.38202 0.39090 -0.00987 0.03548  -0.00911 111 LEU A CA  
849  C C   . LEU A 111 ? 0.32170 0.34908 0.36213 -0.00970 0.03424  -0.00278 111 LEU A C   
850  O O   . LEU A 111 ? 0.33155 0.35991 0.37156 -0.00689 0.03056  0.00403  111 LEU A O   
851  C CB  . LEU A 111 ? 0.32132 0.36421 0.37842 -0.00406 0.03327  -0.01063 111 LEU A CB  
852  C CG  . LEU A 111 ? 0.37663 0.41279 0.44020 -0.00045 0.03519  -0.01354 111 LEU A CG  
853  C CD1 . LEU A 111 ? 0.36298 0.40283 0.42807 -0.00383 0.04151  -0.02175 111 LEU A CD1 
854  C CD2 . LEU A 111 ? 0.34594 0.38655 0.42035 0.00849  0.03109  -0.01292 111 LEU A CD2 
855  N N   . SER A 112 ? 0.31114 0.33111 0.34817 -0.01334 0.03716  -0.00465 112 SER A N   
856  C CA  . SER A 112 ? 0.35542 0.36767 0.39076 -0.01522 0.03579  0.00056  112 SER A CA  
857  C C   . SER A 112 ? 0.35422 0.35617 0.39735 -0.01229 0.03411  0.00038  112 SER A C   
858  O O   . SER A 112 ? 0.33594 0.33068 0.37989 -0.01277 0.03112  0.00785  112 SER A O   
859  C CB  . SER A 112 ? 0.34634 0.35624 0.37544 -0.02038 0.03823  -0.00223 112 SER A CB  
860  O OG  . SER A 112 ? 0.33050 0.33644 0.35915 -0.02420 0.03654  0.00292  112 SER A OG  
861  N N   . ALA A 113 ? 0.33945 0.34054 0.38811 -0.00894 0.03603  -0.00779 113 ALA A N   
862  C CA  . ALA A 113 ? 0.36707 0.35704 0.42279 -0.00401 0.03440  -0.01070 113 ALA A CA  
863  C C   . ALA A 113 ? 0.36600 0.36446 0.42842 0.00154  0.03749  -0.02022 113 ALA A C   
864  O O   . ALA A 113 ? 0.37615 0.38451 0.43568 -0.00188 0.04217  -0.02531 113 ALA A O   
865  C CB  . ALA A 113 ? 0.33840 0.31409 0.39102 -0.00872 0.03440  -0.01354 113 ALA A CB  
866  N N   . ALA A 114 ? 0.36817 0.36341 0.43954 0.01030  0.03490  -0.02191 114 ALA A N   
867  C CA  . ALA A 114 ? 0.41271 0.41672 0.49202 0.01694  0.03821  -0.03241 114 ALA A CA  
868  C C   . ALA A 114 ? 0.41135 0.40002 0.49689 0.02678  0.03415  -0.03486 114 ALA A C   
869  O O   . ALA A 114 ? 0.41511 0.39725 0.50423 0.03221  0.02832  -0.02701 114 ALA A O   
870  C CB  . ALA A 114 ? 0.34681 0.37306 0.43394 0.01937  0.03921  -0.03290 114 ALA A CB  
871  N N   . PHE A 115 ? 0.38846 0.36999 0.47384 0.02950  0.03673  -0.04560 115 PHE A N   
872  C CA  . PHE A 115 ? 0.43811 0.39800 0.52696 0.03807  0.03211  -0.04931 115 PHE A CA  
873  C C   . PHE A 115 ? 0.46246 0.42742 0.55472 0.04624  0.03638  -0.06526 115 PHE A C   
874  O O   . PHE A 115 ? 0.43081 0.41346 0.51971 0.04209  0.04341  -0.07204 115 PHE A O   
875  C CB  . PHE A 115 ? 0.43583 0.37063 0.51655 0.02925  0.02833  -0.04443 115 PHE A CB  
876  C CG  . PHE A 115 ? 0.47130 0.40814 0.54302 0.01919  0.03248  -0.05077 115 PHE A CG  
877  C CD1 . PHE A 115 ? 0.44791 0.39823 0.51290 0.00910  0.03541  -0.04450 115 PHE A CD1 
878  C CD2 . PHE A 115 ? 0.47620 0.40109 0.54538 0.02090  0.03266  -0.06356 115 PHE A CD2 
879  C CE1 . PHE A 115 ? 0.51743 0.47013 0.57358 0.00124  0.03834  -0.04962 115 PHE A CE1 
880  C CE2 . PHE A 115 ? 0.45613 0.38459 0.51598 0.01224  0.03555  -0.06937 115 PHE A CE2 
881  C CZ  . PHE A 115 ? 0.48470 0.42753 0.53814 0.00259  0.03834  -0.06180 115 PHE A CZ  
882  N N   . LEU A 116 ? 0.45179 0.40062 0.54990 0.05857  0.03201  -0.07093 116 LEU A N   
883  C CA  . LEU A 116 ? 0.47524 0.42764 0.57678 0.06956  0.03530  -0.08768 116 LEU A CA  
884  C C   . LEU A 116 ? 0.51371 0.43889 0.60649 0.06693  0.03289  -0.09627 116 LEU A C   
885  O O   . LEU A 116 ? 0.54466 0.44045 0.63532 0.06406  0.02556  -0.09001 116 LEU A O   
886  C CB  . LEU A 116 ? 0.45368 0.40626 0.56813 0.08804  0.03127  -0.09082 116 LEU A CB  
887  C CG  . LEU A 116 ? 0.55130 0.50246 0.66926 0.10268  0.03326  -0.10945 116 LEU A CG  
888  C CD1 . LEU A 116 ? 0.54010 0.52590 0.65796 0.10038  0.04406  -0.11938 116 LEU A CD1 
889  C CD2 . LEU A 116 ? 0.61162 0.56113 0.74278 0.12324  0.02800  -0.11227 116 LEU A CD2 
890  N N   . ARG A 117 ? 0.53507 0.47045 0.62247 0.06732  0.03885  -0.11058 117 ARG A N   
891  C CA  . ARG A 117 ? 0.59028 0.50157 0.67062 0.06863  0.03573  -0.12341 117 ARG A CA  
892  C C   . ARG A 117 ? 0.59950 0.52083 0.68294 0.08483  0.03966  -0.14233 117 ARG A C   
893  O O   . ARG A 117 ? 0.55725 0.51170 0.64307 0.08808  0.04831  -0.14646 117 ARG A O   
894  C CB  . ARG A 117 ? 0.59041 0.50262 0.65747 0.05296  0.03784  -0.12409 117 ARG A CB  
895  C CG  . ARG A 117 ? 0.63122 0.53070 0.69573 0.03831  0.03296  -0.10760 117 ARG A CG  
896  C CD  . ARG A 117 ? 0.73016 0.62144 0.78380 0.02516  0.03129  -0.11073 117 ARG A CD  
897  N NE  . ARG A 117 ? 0.83572 0.71135 0.88489 0.02959  0.02865  -0.12867 117 ARG A NE  
898  C CZ  . ARG A 117 ? 0.83517 0.68068 0.88871 0.03572  0.02148  -0.13496 117 ARG A CZ  
899  N NH1 . ARG A 117 ? 0.83776 0.66509 0.90008 0.03855  0.01630  -0.12324 117 ARG A NH1 
900  N NH2 . ARG A 117 ? 0.91008 0.74255 0.95809 0.03987  0.01910  -0.15370 117 ARG A NH2 
901  N N   . GLU A 118 ? 0.64192 0.53458 0.72561 0.09498  0.03330  -0.15374 118 GLU A N   
902  C CA  . GLU A 118 ? 0.66692 0.56530 0.75144 0.11175  0.03623  -0.17485 118 GLU A CA  
903  C C   . GLU A 118 ? 0.67255 0.54976 0.74381 0.10727  0.03354  -0.18971 118 GLU A C   
904  O O   . GLU A 118 ? 0.75773 0.59942 0.82564 0.09939  0.02454  -0.18653 118 GLU A O   
905  C CB  . GLU A 118 ? 0.70144 0.58311 0.79801 0.13198  0.02992  -0.17887 118 GLU A CB  
906  C CG  . GLU A 118 ? 0.72060 0.63385 0.83161 0.14241  0.03377  -0.17207 118 GLU A CG  
907  C CD  . GLU A 118 ? 0.78246 0.68383 0.90501 0.16653  0.02792  -0.18006 118 GLU A CD  
908  O OE1 . GLU A 118 ? 0.83756 0.70074 0.95599 0.17482  0.02034  -0.18997 118 GLU A OE1 
909  O OE2 . GLU A 118 ? 0.78169 0.71172 0.91781 0.17747  0.03030  -0.17681 118 GLU A OE2 
910  N N   . ILE A 119 ? 0.69483 0.59490 0.75853 0.11179  0.04116  -0.20586 119 ILE A N   
911  C CA  . ILE A 119 ? 0.76578 0.65275 0.81472 0.10702  0.03918  -0.22120 119 ILE A CA  
912  C C   . ILE A 119 ? 0.76029 0.64655 0.80834 0.12753  0.04021  -0.24566 119 ILE A C   
913  O O   . ILE A 119 ? 0.75137 0.67390 0.79922 0.13712  0.05049  -0.25412 119 ILE A O   
914  C CB  . ILE A 119 ? 0.72505 0.64079 0.76119 0.09280  0.04704  -0.21791 119 ILE A CB  
915  C CG1 . ILE A 119 ? 0.71714 0.62996 0.75414 0.07439  0.04473  -0.19536 119 ILE A CG1 
916  C CG2 . ILE A 119 ? 0.75815 0.66413 0.77836 0.08991  0.04443  -0.23544 119 ILE A CG2 
917  C CD1 . ILE A 119 ? 0.71629 0.66294 0.74742 0.06535  0.05398  -0.18597 119 ILE A CD1 
918  N N   . GLU A 120 ? 0.80902 0.65423 0.85624 0.13390  0.02971  -0.25728 120 GLU A N   
919  C CA  . GLU A 120 ? 0.81643 0.65380 0.86376 0.15627  0.02860  -0.28159 120 GLU A CA  
920  C C   . GLU A 120 ? 0.82355 0.67820 0.85418 0.15712  0.03390  -0.30305 120 GLU A C   
921  O O   . GLU A 120 ? 0.81186 0.68057 0.83042 0.13998  0.03703  -0.29845 120 GLU A O   
922  C CB  . GLU A 120 ? 0.91049 0.69248 0.96095 0.16157  0.01439  -0.28677 120 GLU A CB  
923  C CG  . GLU A 120 ? 0.99763 0.76287 1.06399 0.17036  0.00917  -0.27082 120 GLU A CG  
924  C CD  . GLU A 120 ? 1.11675 0.84588 1.18434 0.15151  -0.00038 -0.24990 120 GLU A CD  
925  O OE1 . GLU A 120 ? 1.15982 0.87262 1.21767 0.13303  -0.00421 -0.25087 120 GLU A OE1 
926  O OE2 . GLU A 120 ? 1.12780 0.84735 1.20609 0.15516  -0.00400 -0.23238 120 GLU A OE2 
927  N N   . SER A 121 ? 0.84093 0.69571 0.86875 0.17620  0.03463  -0.32201 121 SER A N   
928  C CA  . SER A 121 ? 0.87272 0.74143 0.88151 0.17609  0.03844  -0.33765 121 SER A CA  
929  C C   . SER A 121 ? 0.91017 0.74150 0.90611 0.16179  0.02720  -0.34430 121 SER A C   
930  O O   . SER A 121 ? 0.92704 0.71401 0.92912 0.15707  0.01536  -0.34060 121 SER A O   
931  C CB  . SER A 121 ? 0.90366 0.77711 0.91225 0.19745  0.04050  -0.35129 121 SER A CB  
932  O OG  . SER A 121 ? 0.92163 0.84091 0.93981 0.20839  0.05273  -0.34708 121 SER A OG  
933  N N   . GLY A 122 ? 0.90330 0.75412 0.88119 0.15412  0.03083  -0.35307 122 GLY A N   
934  C CA  . GLY A 122 ? 0.91971 0.74256 0.88503 0.13991  0.02039  -0.36051 122 GLY A CA  
935  C C   . GLY A 122 ? 0.93943 0.75181 0.90840 0.11848  0.01514  -0.34768 122 GLY A C   
936  O O   . GLY A 122 ? 0.98000 0.76340 0.94407 0.10520  0.00419  -0.35141 122 GLY A O   
937  N N   . MET A 123 ? 0.88702 0.72382 0.86469 0.11304  0.02277  -0.32991 123 MET A N   
938  C CA  . MET A 123 ? 0.92277 0.75392 0.90226 0.09004  0.01873  -0.30790 123 MET A CA  
939  C C   . MET A 123 ? 0.88592 0.74922 0.84898 0.07853  0.02406  -0.30666 123 MET A C   
940  O O   . MET A 123 ? 0.85231 0.75291 0.80841 0.08510  0.03580  -0.30675 123 MET A O   
941  C CB  . MET A 123 ? 0.87680 0.71580 0.87174 0.08712  0.02299  -0.28185 123 MET A CB  
942  C CG  . MET A 123 ? 0.95010 0.75197 0.96039 0.09345  0.01477  -0.27690 123 MET A CG  
943  S SD  . MET A 123 ? 1.09516 0.84444 1.10453 0.07889  -0.00138 -0.28064 123 MET A SD  
944  C CE  . MET A 123 ? 1.08671 0.80123 1.09571 0.10131  -0.00839 -0.30920 123 MET A CE  
945  N N   . PRO A 124 ? 0.88196 0.73305 0.83872 0.06150  0.01567  -0.30500 124 PRO A N   
946  C CA  . PRO A 124 ? 0.81407 0.69541 0.75462 0.05180  0.01945  -0.30301 124 PRO A CA  
947  C C   . PRO A 124 ? 0.78360 0.68906 0.72840 0.04260  0.02704  -0.27617 124 PRO A C   
948  O O   . PRO A 124 ? 0.80810 0.70253 0.76826 0.03812  0.02614  -0.25839 124 PRO A O   
949  C CB  . PRO A 124 ? 0.85865 0.71669 0.79560 0.03679  0.00604  -0.30955 124 PRO A CB  
950  C CG  . PRO A 124 ? 0.93112 0.75285 0.88707 0.03060  -0.00177 -0.29863 124 PRO A CG  
951  C CD  . PRO A 124 ? 0.92647 0.73654 0.89141 0.04973  0.00209  -0.30375 124 PRO A CD  
952  N N   . ALA A 125 ? 0.77067 0.70853 0.70029 0.04024  0.03424  -0.27357 125 ALA A N   
953  C CA  . ALA A 125 ? 0.71719 0.67604 0.64841 0.03166  0.04083  -0.24954 125 ALA A CA  
954  C C   . ALA A 125 ? 0.69166 0.63561 0.62979 0.01558  0.03201  -0.23482 125 ALA A C   
955  O O   . ALA A 125 ? 0.69654 0.62188 0.63398 0.00820  0.02145  -0.24347 125 ALA A O   
956  C CB  . ALA A 125 ? 0.67517 0.66722 0.58625 0.03171  0.04880  -0.24968 125 ALA A CB  
957  N N   . GLN A 126 ? 0.65372 0.60705 0.59939 0.01007  0.03646  -0.21299 126 GLN A N   
958  C CA  . GLN A 126 ? 0.63951 0.58685 0.59058 -0.00396 0.03033  -0.19751 126 GLN A CA  
959  C C   . GLN A 126 ? 0.61933 0.58427 0.55454 -0.01129 0.02827  -0.19778 126 GLN A C   
960  O O   . GLN A 126 ? 0.63322 0.61918 0.55276 -0.00605 0.03450  -0.20202 126 GLN A O   
961  C CB  . GLN A 126 ? 0.58478 0.54011 0.54566 -0.00547 0.03628  -0.17625 126 GLN A CB  
962  C CG  . GLN A 126 ? 0.62636 0.56041 0.60459 -0.00922 0.03137  -0.16596 126 GLN A CG  
963  C CD  . GLN A 126 ? 0.56844 0.51339 0.55419 -0.00894 0.03743  -0.14753 126 GLN A CD  
964  O OE1 . GLN A 126 ? 0.57747 0.54355 0.55704 -0.00589 0.04545  -0.14336 126 GLN A OE1 
965  N NE2 . GLN A 126 ? 0.64408 0.57438 0.64264 -0.01261 0.03346  -0.13643 126 GLN A NE2 
966  N N   . PRO A 127 ? 0.62190 0.58070 0.56071 -0.02322 0.01962  -0.19262 127 PRO A N   
967  C CA  . PRO A 127 ? 0.54067 0.52038 0.46664 -0.02908 0.01804  -0.18784 127 PRO A CA  
968  C C   . PRO A 127 ? 0.55058 0.54748 0.47427 -0.02782 0.02640  -0.16838 127 PRO A C   
969  O O   . PRO A 127 ? 0.50887 0.50012 0.44503 -0.02725 0.03050  -0.15599 127 PRO A O   
970  C CB  . PRO A 127 ? 0.58450 0.55448 0.52067 -0.04219 0.00714  -0.18530 127 PRO A CB  
971  C CG  . PRO A 127 ? 0.58364 0.52919 0.53873 -0.04445 0.00586  -0.17997 127 PRO A CG  
972  C CD  . PRO A 127 ? 0.63344 0.56719 0.58787 -0.03194 0.01061  -0.19143 127 PRO A CD  
973  N N   . PHE A 128 ? 0.50929 0.52639 0.41584 -0.02712 0.02837  -0.16595 128 PHE A N   
974  C CA  . PHE A 128 ? 0.46673 0.49655 0.36965 -0.02689 0.03475  -0.14743 128 PHE A CA  
975  C C   . PHE A 128 ? 0.48667 0.51237 0.40203 -0.03446 0.02946  -0.13369 128 PHE A C   
976  O O   . PHE A 128 ? 0.45685 0.48100 0.37619 -0.04116 0.02051  -0.13721 128 PHE A O   
977  C CB  . PHE A 128 ? 0.48604 0.53532 0.36642 -0.02447 0.03663  -0.14683 128 PHE A CB  
978  C CG  . PHE A 128 ? 0.48027 0.53960 0.34737 -0.01664 0.04612  -0.15379 128 PHE A CG  
979  C CD1 . PHE A 128 ? 0.49242 0.55508 0.36371 -0.01355 0.05676  -0.14419 128 PHE A CD1 
980  C CD2 . PHE A 128 ? 0.49306 0.56114 0.34357 -0.01276 0.04440  -0.17018 128 PHE A CD2 
981  C CE1 . PHE A 128 ? 0.54706 0.62353 0.40747 -0.00720 0.06648  -0.15004 128 PHE A CE1 
982  C CE2 . PHE A 128 ? 0.52317 0.60440 0.36079 -0.00507 0.05421  -0.17671 128 PHE A CE2 
983  C CZ  . PHE A 128 ? 0.53207 0.61845 0.37532 -0.00260 0.06570  -0.16599 128 PHE A CZ  
984  N N   . HIS A 129 ? 0.45490 0.48037 0.37700 -0.03361 0.03501  -0.11877 129 HIS A N   
985  C CA  . HIS A 129 ? 0.48007 0.50270 0.41406 -0.03901 0.03137  -0.10615 129 HIS A CA  
986  C C   . HIS A 129 ? 0.46958 0.49611 0.40308 -0.03596 0.03828  -0.09165 129 HIS A C   
987  O O   . HIS A 129 ? 0.47346 0.50279 0.40117 -0.03140 0.04583  -0.09126 129 HIS A O   
988  C CB  . HIS A 129 ? 0.47154 0.47734 0.42361 -0.04292 0.02786  -0.10825 129 HIS A CB  
989  C CG  . HIS A 129 ? 0.49393 0.49037 0.45337 -0.03713 0.03416  -0.10751 129 HIS A CG  
990  N ND1 . HIS A 129 ? 0.51546 0.50574 0.47342 -0.03106 0.03652  -0.12083 129 HIS A ND1 
991  C CD2 . HIS A 129 ? 0.49661 0.49180 0.46433 -0.03533 0.03849  -0.09583 129 HIS A CD2 
992  C CE1 . HIS A 129 ? 0.50570 0.49235 0.47231 -0.02573 0.04191  -0.11674 129 HIS A CE1 
993  N NE2 . HIS A 129 ? 0.48583 0.47510 0.45839 -0.02882 0.04285  -0.10161 129 HIS A NE2 
994  N N   . ARG A 130 ? 0.45475 0.48230 0.39495 -0.03892 0.03556  -0.08032 130 ARG A N   
995  C CA  . ARG A 130 ? 0.46477 0.49152 0.40836 -0.03688 0.04023  -0.06784 130 ARG A CA  
996  C C   . ARG A 130 ? 0.48470 0.50205 0.44549 -0.03906 0.03926  -0.06433 130 ARG A C   
997  O O   . ARG A 130 ? 0.49136 0.50377 0.46100 -0.04366 0.03401  -0.06759 130 ARG A O   
998  C CB  . ARG A 130 ? 0.49121 0.52639 0.42770 -0.03631 0.03773  -0.05808 130 ARG A CB  
999  C CG  . ARG A 130 ? 0.48863 0.53258 0.40654 -0.03350 0.03742  -0.05926 130 ARG A CG  
1000 C CD  . ARG A 130 ? 0.48896 0.54102 0.40117 -0.03150 0.03242  -0.05122 130 ARG A CD  
1001 N NE  . ARG A 130 ? 0.52073 0.57464 0.41423 -0.02675 0.03515  -0.04551 130 ARG A NE  
1002 C CZ  . ARG A 130 ? 0.51208 0.57386 0.39351 -0.02270 0.03027  -0.04103 130 ARG A CZ  
1003 N NH1 . ARG A 130 ? 0.51703 0.58963 0.40425 -0.02271 0.02235  -0.04284 130 ARG A NH1 
1004 N NH2 . ARG A 130 ? 0.49891 0.55859 0.36225 -0.01864 0.03329  -0.03401 130 ARG A NH2 
1005 N N   . ASP A 131 ? 0.49117 0.50621 0.45622 -0.03644 0.04397  -0.05703 131 ASP A N   
1006 C CA  . ASP A 131 ? 0.50357 0.51138 0.48284 -0.03728 0.04307  -0.05232 131 ASP A CA  
1007 C C   . ASP A 131 ? 0.48806 0.50075 0.47000 -0.03949 0.03996  -0.04247 131 ASP A C   
1008 O O   . ASP A 131 ? 0.50246 0.51636 0.48575 -0.03719 0.04195  -0.03508 131 ASP A O   
1009 C CB  . ASP A 131 ? 0.48649 0.49271 0.46960 -0.03317 0.04865  -0.05040 131 ASP A CB  
1010 C CG  . ASP A 131 ? 0.53707 0.53996 0.52284 -0.02975 0.05144  -0.06049 131 ASP A CG  
1011 O OD1 . ASP A 131 ? 0.49180 0.48792 0.47878 -0.03053 0.04779  -0.06875 131 ASP A OD1 
1012 O OD2 . ASP A 131 ? 0.58281 0.59048 0.57012 -0.02631 0.05703  -0.06075 131 ASP A OD2 
1013 N N   . ASP A 132 ? 0.46225 0.47949 0.44548 -0.04403 0.03477  -0.04339 132 ASP A N   
1014 C CA  . ASP A 132 ? 0.44508 0.47193 0.43150 -0.04556 0.03217  -0.03507 132 ASP A CA  
1015 C C   . ASP A 132 ? 0.44363 0.47011 0.44234 -0.05298 0.02827  -0.03345 132 ASP A C   
1016 O O   . ASP A 132 ? 0.47179 0.51149 0.47376 -0.05609 0.02558  -0.02881 132 ASP A O   
1017 C CB  . ASP A 132 ? 0.44818 0.48786 0.42438 -0.04362 0.02978  -0.03508 132 ASP A CB  
1018 C CG  . ASP A 132 ? 0.55360 0.59774 0.52725 -0.04799 0.02518  -0.04400 132 ASP A CG  
1019 O OD1 . ASP A 132 ? 0.56042 0.59667 0.54167 -0.05381 0.02318  -0.05031 132 ASP A OD1 
1020 O OD2 . ASP A 132 ? 0.59515 0.64985 0.55845 -0.04522 0.02281  -0.04504 132 ASP A OD2 
1021 N N   . ALA A 133 ? 0.40251 0.41450 0.40836 -0.05582 0.02792  -0.03668 133 ALA A N   
1022 C CA  . ALA A 133 ? 0.42210 0.42975 0.43868 -0.06469 0.02378  -0.03465 133 ALA A CA  
1023 C C   . ALA A 133 ? 0.40339 0.40815 0.42788 -0.06536 0.02519  -0.02329 133 ALA A C   
1024 O O   . ALA A 133 ? 0.40317 0.41387 0.43487 -0.07307 0.02306  -0.01642 133 ALA A O   
1025 C CB  . ALA A 133 ? 0.47152 0.46116 0.49040 -0.06766 0.02098  -0.04526 133 ALA A CB  
1026 N N   . THR A 134 ? 0.35715 0.35537 0.38045 -0.05790 0.02869  -0.02076 134 THR A N   
1027 C CA  . THR A 134 ? 0.37048 0.36741 0.39951 -0.05771 0.02931  -0.01003 134 THR A CA  
1028 C C   . THR A 134 ? 0.34520 0.36158 0.37257 -0.05789 0.03037  -0.00173 134 THR A C   
1029 O O   . THR A 134 ? 0.35237 0.37386 0.38496 -0.06232 0.02988  0.00743  134 THR A O   
1030 C CB  . THR A 134 ? 0.41796 0.40738 0.44627 -0.04912 0.03192  -0.01039 134 THR A CB  
1031 O OG1 . THR A 134 ? 0.51578 0.48988 0.54617 -0.04717 0.03124  -0.01929 134 THR A OG1 
1032 C CG2 . THR A 134 ? 0.39898 0.38733 0.43202 -0.04832 0.03146  0.00068  134 THR A CG2 
1033 N N   . HIS A 135 ? 0.34015 0.36747 0.35966 -0.05267 0.03187  -0.00466 135 HIS A N   
1034 C CA  . HIS A 135 ? 0.33601 0.38137 0.35279 -0.05014 0.03243  0.00075  135 HIS A CA  
1035 C C   . HIS A 135 ? 0.31005 0.36716 0.32342 -0.05129 0.03030  -0.00374 135 HIS A C   
1036 O O   . HIS A 135 ? 0.32165 0.38007 0.32569 -0.04477 0.03084  -0.00727 135 HIS A O   
1037 C CB  . HIS A 135 ? 0.32659 0.37139 0.33638 -0.04111 0.03494  0.00153  135 HIS A CB  
1038 C CG  . HIS A 135 ? 0.36014 0.39816 0.37340 -0.03935 0.03598  0.00590  135 HIS A CG  
1039 N ND1 . HIS A 135 ? 0.32271 0.34683 0.33803 -0.03795 0.03664  0.00247  135 HIS A ND1 
1040 C CD2 . HIS A 135 ? 0.32182 0.36739 0.33643 -0.03786 0.03622  0.01331  135 HIS A CD2 
1041 C CE1 . HIS A 135 ? 0.32649 0.34946 0.34476 -0.03550 0.03651  0.00779  135 HIS A CE1 
1042 N NE2 . HIS A 135 ? 0.33040 0.36570 0.34735 -0.03563 0.03625  0.01457  135 HIS A NE2 
1043 N N   . PRO A 136 ? 0.29586 0.36187 0.31666 -0.05991 0.02740  -0.00320 136 PRO A N   
1044 C CA  . PRO A 136 ? 0.35052 0.42887 0.36905 -0.06145 0.02401  -0.00893 136 PRO A CA  
1045 C C   . PRO A 136 ? 0.37289 0.46809 0.38408 -0.05207 0.02413  -0.00753 136 PRO A C   
1046 O O   . PRO A 136 ? 0.33682 0.43861 0.34205 -0.04964 0.02122  -0.01252 136 PRO A O   
1047 C CB  . PRO A 136 ? 0.35881 0.44783 0.38998 -0.07383 0.02097  -0.00637 136 PRO A CB  
1048 C CG  . PRO A 136 ? 0.34849 0.41940 0.38621 -0.07978 0.02227  -0.00165 136 PRO A CG  
1049 C CD  . PRO A 136 ? 0.32870 0.39230 0.36047 -0.06976 0.02656  0.00278  136 PRO A CD  
1050 N N   . LEU A 137 ? 0.31598 0.41808 0.32661 -0.04592 0.02677  -0.00128 137 LEU A N   
1051 C CA  . LEU A 137 ? 0.35039 0.46487 0.35342 -0.03518 0.02626  -0.00102 137 LEU A CA  
1052 C C   . LEU A 137 ? 0.35974 0.45838 0.34935 -0.02793 0.02625  -0.00522 137 LEU A C   
1053 O O   . LEU A 137 ? 0.34947 0.45428 0.33100 -0.01952 0.02431  -0.00568 137 LEU A O   
1054 C CB  . LEU A 137 ? 0.30112 0.42316 0.30465 -0.02903 0.02905  0.00459  137 LEU A CB  
1055 C CG  . LEU A 137 ? 0.33706 0.44010 0.33493 -0.02483 0.03184  0.00536  137 LEU A CG  
1056 C CD1 . LEU A 137 ? 0.30829 0.40062 0.29370 -0.01473 0.03142  0.00192  137 LEU A CD1 
1057 C CD2 . LEU A 137 ? 0.31327 0.42645 0.31472 -0.02336 0.03399  0.01107  137 LEU A CD2 
1058 N N   . MET A 138 ? 0.36410 0.44308 0.35126 -0.03069 0.02853  -0.00760 138 MET A N   
1059 C CA  . MET A 138 ? 0.42235 0.48838 0.39735 -0.02610 0.02958  -0.01060 138 MET A CA  
1060 C C   . MET A 138 ? 0.39830 0.47053 0.36651 -0.02606 0.02624  -0.01457 138 MET A C   
1061 O O   . MET A 138 ? 0.46198 0.52910 0.41754 -0.02021 0.02621  -0.01435 138 MET A O   
1062 C CB  . MET A 138 ? 0.41286 0.46250 0.38923 -0.02980 0.03309  -0.01315 138 MET A CB  
1063 C CG  . MET A 138 ? 0.43826 0.48214 0.42011 -0.02871 0.03561  -0.00937 138 MET A CG  
1064 S SD  . MET A 138 ? 0.48743 0.51647 0.47304 -0.03132 0.03908  -0.01289 138 MET A SD  
1065 C CE  . MET A 138 ? 0.40766 0.43215 0.38079 -0.02977 0.04128  -0.01732 138 MET A CE  
1066 N N   . HIS A 139 ? 0.44155 0.52463 0.41746 -0.03296 0.02291  -0.01786 139 HIS A N   
1067 C CA  . HIS A 139 ? 0.48499 0.57589 0.45416 -0.03314 0.01865  -0.02298 139 HIS A CA  
1068 C C   . HIS A 139 ? 0.45352 0.55835 0.41524 -0.02365 0.01532  -0.01963 139 HIS A C   
1069 O O   . HIS A 139 ? 0.50219 0.60838 0.45189 -0.01946 0.01256  -0.02161 139 HIS A O   
1070 C CB  . HIS A 139 ? 0.44389 0.54424 0.42484 -0.04382 0.01464  -0.02793 139 HIS A CB  
1071 C CG  . HIS A 139 ? 0.48987 0.60095 0.46498 -0.04498 0.00892  -0.03485 139 HIS A CG  
1072 N ND1 . HIS A 139 ? 0.51857 0.61912 0.48193 -0.04448 0.00894  -0.04193 139 HIS A ND1 
1073 C CD2 . HIS A 139 ? 0.46559 0.59970 0.44519 -0.04656 0.00273  -0.03629 139 HIS A CD2 
1074 C CE1 . HIS A 139 ? 0.56714 0.68240 0.52639 -0.04545 0.00256  -0.04753 139 HIS A CE1 
1075 N NE2 . HIS A 139 ? 0.55331 0.68925 0.52308 -0.04693 -0.00169 -0.04433 139 HIS A NE2 
1076 N N   . TYR A 140 ? 0.39857 0.51397 0.36612 -0.01886 0.01542  -0.01459 140 TYR A N   
1077 C CA  . TYR A 140 ? 0.40435 0.53517 0.36697 -0.00806 0.01153  -0.01237 140 TYR A CA  
1078 C C   . TYR A 140 ? 0.43307 0.54781 0.38236 0.00379  0.01316  -0.00844 140 TYR A C   
1079 O O   . TYR A 140 ? 0.45006 0.57217 0.39248 0.01502  0.00934  -0.00670 140 TYR A O   
1080 C CB  . TYR A 140 ? 0.36963 0.52592 0.34693 -0.00870 0.01051  -0.01038 140 TYR A CB  
1081 C CG  . TYR A 140 ? 0.40081 0.57107 0.39282 -0.02314 0.00882  -0.01310 140 TYR A CG  
1082 C CD1 . TYR A 140 ? 0.33106 0.52224 0.32691 -0.02615 0.00265  -0.01722 140 TYR A CD1 
1083 C CD2 . TYR A 140 ? 0.39785 0.55815 0.39925 -0.03378 0.01276  -0.01146 140 TYR A CD2 
1084 C CE1 . TYR A 140 ? 0.37670 0.57739 0.38646 -0.04117 0.00063  -0.02024 140 TYR A CE1 
1085 C CE2 . TYR A 140 ? 0.39547 0.56350 0.40968 -0.04770 0.01074  -0.01334 140 TYR A CE2 
1086 C CZ  . TYR A 140 ? 0.40033 0.58778 0.41932 -0.05254 0.00468  -0.01815 140 TYR A CZ  
1087 O OH  . TYR A 140 ? 0.48353 0.67545 0.51574 -0.06805 0.00228  -0.02042 140 TYR A OH  
1088 N N   . GLN A 141 ? 0.40763 0.50086 0.35377 0.00173  0.01804  -0.00723 141 GLN A N   
1089 C CA  . GLN A 141 ? 0.43700 0.51231 0.37082 0.01051  0.01905  -0.00396 141 GLN A CA  
1090 C C   . GLN A 141 ? 0.43676 0.50308 0.35451 0.01467  0.01683  -0.00241 141 GLN A C   
1091 O O   . GLN A 141 ? 0.42148 0.48477 0.33565 0.00779  0.01820  -0.00448 141 GLN A O   
1092 C CB  . GLN A 141 ? 0.43261 0.48942 0.36809 0.00491  0.02436  -0.00369 141 GLN A CB  
1093 C CG  . GLN A 141 ? 0.46463 0.52860 0.41274 0.00247  0.02612  -0.00376 141 GLN A CG  
1094 C CD  . GLN A 141 ? 0.51375 0.57261 0.45787 0.01154  0.02575  -0.00237 141 GLN A CD  
1095 O OE1 . GLN A 141 ? 0.43174 0.50621 0.37845 0.01892  0.02363  -0.00226 141 GLN A OE1 
1096 N NE2 . GLN A 141 ? 0.44611 0.48426 0.38431 0.01101  0.02776  -0.00214 141 GLN A NE2 
1097 N N   . PRO A 142 ? 0.48172 0.54267 0.38841 0.02648  0.01341  0.00132  142 PRO A N   
1098 C CA  . PRO A 142 ? 0.44545 0.49380 0.33422 0.03053  0.01155  0.00536  142 PRO A CA  
1099 C C   . PRO A 142 ? 0.48295 0.50903 0.36458 0.02232  0.01760  0.00755  142 PRO A C   
1100 O O   . PRO A 142 ? 0.48711 0.50310 0.37590 0.01715  0.02206  0.00668  142 PRO A O   
1101 C CB  . PRO A 142 ? 0.48188 0.52206 0.36160 0.04540  0.00703  0.00958  142 PRO A CB  
1102 C CG  . PRO A 142 ? 0.44039 0.49844 0.33468 0.05030  0.00590  0.00566  142 PRO A CG  
1103 C CD  . PRO A 142 ? 0.42957 0.49276 0.33839 0.03727  0.01142  0.00215  142 PRO A CD  
1104 N N   . LEU A 143 ? 0.48920 0.51045 0.35652 0.02132  0.01770  0.01052  143 LEU A N   
1105 C CA  . LEU A 143 ? 0.50356 0.50730 0.36282 0.01376  0.02412  0.01374  143 LEU A CA  
1106 C C   . LEU A 143 ? 0.50305 0.48318 0.35822 0.01547  0.02575  0.01951  143 LEU A C   
1107 O O   . LEU A 143 ? 0.49810 0.46776 0.35697 0.00685  0.03166  0.01971  143 LEU A O   
1108 C CB  . LEU A 143 ? 0.52778 0.53196 0.36864 0.01468  0.02345  0.01783  143 LEU A CB  
1109 C CG  . LEU A 143 ? 0.58177 0.56846 0.40956 0.00860  0.03008  0.02469  143 LEU A CG  
1110 C CD1 . LEU A 143 ? 0.53996 0.53078 0.37893 -0.00282 0.03808  0.01848  143 LEU A CD1 
1111 C CD2 . LEU A 143 ? 0.56475 0.55292 0.37082 0.01186  0.02850  0.03094  143 LEU A CD2 
1112 N N   . GLU A 144 ? 0.50081 0.47269 0.34889 0.02691  0.01999  0.02342  144 GLU A N   
1113 C CA  . GLU A 144 ? 0.52093 0.46605 0.36256 0.02927  0.01995  0.02828  144 GLU A CA  
1114 C C   . GLU A 144 ? 0.52151 0.46505 0.37773 0.02785  0.02105  0.02227  144 GLU A C   
1115 O O   . GLU A 144 ? 0.51754 0.43883 0.37068 0.02623  0.02165  0.02415  144 GLU A O   
1116 C CB  . GLU A 144 ? 0.55508 0.48946 0.38276 0.04427  0.01240  0.03367  144 GLU A CB  
1117 C CG  . GLU A 144 ? 0.55029 0.48219 0.35959 0.04689  0.01045  0.04193  144 GLU A CG  
1118 C CD  . GLU A 144 ? 0.56711 0.52991 0.37897 0.05094  0.00677  0.03777  144 GLU A CD  
1119 O OE1 . GLU A 144 ? 0.56937 0.55498 0.39822 0.05153  0.00558  0.02919  144 GLU A OE1 
1120 O OE2 . GLU A 144 ? 0.55629 0.52074 0.35250 0.05304  0.00477  0.04352  144 GLU A OE2 
1121 N N   . ALA A 145 ? 0.45990 0.42624 0.33121 0.02768  0.02105  0.01545  145 ALA A N   
1122 C CA  . ALA A 145 ? 0.48826 0.45615 0.37131 0.02815  0.02150  0.01053  145 ALA A CA  
1123 C C   . ALA A 145 ? 0.45367 0.41278 0.34355 0.01593  0.02713  0.00928  145 ALA A C   
1124 O O   . ALA A 145 ? 0.42683 0.38837 0.31795 0.00667  0.03162  0.01012  145 ALA A O   
1125 C CB  . ALA A 145 ? 0.40293 0.39893 0.29957 0.02995  0.02054  0.00576  145 ALA A CB  
1126 N N   . PRO A 146 ? 0.45554 0.40688 0.35025 0.01650  0.02668  0.00630  146 PRO A N   
1127 C CA  . PRO A 146 ? 0.46142 0.40715 0.36387 0.00549  0.03101  0.00474  146 PRO A CA  
1128 C C   . PRO A 146 ? 0.43092 0.39518 0.34544 -0.00189 0.03520  0.00252  146 PRO A C   
1129 O O   . PRO A 146 ? 0.40898 0.39015 0.33133 0.00081  0.03407  0.00006  146 PRO A O   
1130 C CB  . PRO A 146 ? 0.41373 0.35660 0.32058 0.01005  0.02805  -0.00010 146 PRO A CB  
1131 C CG  . PRO A 146 ? 0.43056 0.36524 0.32664 0.02332  0.02250  -0.00006 146 PRO A CG  
1132 C CD  . PRO A 146 ? 0.45118 0.40018 0.34414 0.02821  0.02179  0.00321  146 PRO A CD  
1133 N N   . PRO A 147 ? 0.44467 0.40646 0.36088 -0.01109 0.04008  0.00343  147 PRO A N   
1134 C CA  . PRO A 147 ? 0.42360 0.40042 0.35122 -0.01635 0.04347  -0.00001 147 PRO A CA  
1135 C C   . PRO A 147 ? 0.42728 0.41064 0.36803 -0.01678 0.04281  -0.00339 147 PRO A C   
1136 O O   . PRO A 147 ? 0.40601 0.38221 0.34815 -0.01678 0.04167  -0.00402 147 PRO A O   
1137 C CB  . PRO A 147 ? 0.43889 0.41174 0.36495 -0.02438 0.04915  0.00109  147 PRO A CB  
1138 C CG  . PRO A 147 ? 0.48326 0.43825 0.39792 -0.02568 0.04901  0.00660  147 PRO A CG  
1139 C CD  . PRO A 147 ? 0.46978 0.41618 0.37567 -0.01613 0.04272  0.00841  147 PRO A CD  
1140 N N   . VAL A 148 ? 0.39422 0.39058 0.34373 -0.01716 0.04281  -0.00538 148 VAL A N   
1141 C CA  . VAL A 148 ? 0.35951 0.36277 0.32015 -0.01726 0.04203  -0.00666 148 VAL A CA  
1142 C C   . VAL A 148 ? 0.39894 0.40591 0.36989 -0.02232 0.04486  -0.00877 148 VAL A C   
1143 O O   . VAL A 148 ? 0.36460 0.37643 0.34436 -0.02212 0.04384  -0.00862 148 VAL A O   
1144 C CB  . VAL A 148 ? 0.36693 0.38171 0.32950 -0.01281 0.03898  -0.00546 148 VAL A CB  
1145 C CG1 . VAL A 148 ? 0.33151 0.34479 0.28552 -0.00493 0.03590  -0.00479 148 VAL A CG1 
1146 C CG2 . VAL A 148 ? 0.32632 0.34920 0.29030 -0.01512 0.03879  -0.00568 148 VAL A CG2 
1147 N N   . SER A 149 ? 0.35626 0.36134 0.32560 -0.02582 0.04828  -0.01071 149 SER A N   
1148 C CA  . SER A 149 ? 0.39696 0.40549 0.37587 -0.02839 0.05076  -0.01432 149 SER A CA  
1149 C C   . SER A 149 ? 0.38727 0.39521 0.36408 -0.03151 0.05592  -0.01669 149 SER A C   
1150 O O   . SER A 149 ? 0.38656 0.39206 0.35223 -0.03261 0.05773  -0.01537 149 SER A O   
1151 C CB  . SER A 149 ? 0.41940 0.43121 0.40045 -0.02861 0.04915  -0.01652 149 SER A CB  
1152 O OG  . SER A 149 ? 0.48066 0.49216 0.47126 -0.02943 0.05050  -0.02050 149 SER A OG  
1153 N N   . LEU A 150 ? 0.37217 0.38432 0.35967 -0.03240 0.05833  -0.01976 150 LEU A N   
1154 C CA  . LEU A 150 ? 0.42380 0.44100 0.41230 -0.03511 0.06426  -0.02277 150 LEU A CA  
1155 C C   . LEU A 150 ? 0.38388 0.40723 0.38373 -0.03213 0.06550  -0.02906 150 LEU A C   
1156 O O   . LEU A 150 ? 0.41437 0.43792 0.42462 -0.02930 0.06224  -0.02915 150 LEU A O   
1157 C CB  . LEU A 150 ? 0.39692 0.41545 0.38867 -0.03939 0.06627  -0.02017 150 LEU A CB  
1158 C CG  . LEU A 150 ? 0.43681 0.46450 0.43088 -0.04424 0.07344  -0.02163 150 LEU A CG  
1159 C CD1 . LEU A 150 ? 0.42005 0.44396 0.39806 -0.04746 0.07737  -0.01814 150 LEU A CD1 
1160 C CD2 . LEU A 150 ? 0.39715 0.42844 0.40024 -0.04961 0.07374  -0.02000 150 LEU A CD2 
1161 N N   . SER A 151 ? 0.44315 0.48500 0.33545 -0.02243 0.04320  -0.04492 151 SER A N   
1162 C CA  . SER A 151 ? 0.46327 0.51785 0.37719 -0.02611 0.04037  -0.04073 151 SER A CA  
1163 C C   . SER A 151 ? 0.45454 0.50903 0.37364 -0.03267 0.04180  -0.04118 151 SER A C   
1164 O O   . SER A 151 ? 0.40852 0.45452 0.31791 -0.03404 0.04617  -0.04373 151 SER A O   
1165 C CB  . SER A 151 ? 0.46785 0.52235 0.38882 -0.01951 0.04026  -0.04128 151 SER A CB  
1166 O OG  . SER A 151 ? 0.44712 0.50722 0.36572 -0.01585 0.03760  -0.03803 151 SER A OG  
1167 N N   . VAL A 152 ? 0.44394 0.51104 0.37911 -0.03810 0.03689  -0.03714 152 VAL A N   
1168 C CA  . VAL A 152 ? 0.45201 0.52869 0.39815 -0.04400 0.03751  -0.03616 152 VAL A CA  
1169 C C   . VAL A 152 ? 0.44991 0.54159 0.42357 -0.03711 0.03322  -0.03700 152 VAL A C   
1170 O O   . VAL A 152 ? 0.43072 0.52563 0.41727 -0.03740 0.02337  -0.03228 152 VAL A O   
1171 C CB  . VAL A 152 ? 0.46496 0.54231 0.40598 -0.05602 0.03301  -0.03067 152 VAL A CB  
1172 C CG1 . VAL A 152 ? 0.40129 0.49331 0.35436 -0.06394 0.03327  -0.02749 152 VAL A CG1 
1173 C CG2 . VAL A 152 ? 0.43540 0.49109 0.34576 -0.05892 0.03453  -0.03330 152 VAL A CG2 
1174 N N   . ILE A 153 ? 0.43935 0.53958 0.42057 -0.03087 0.03905  -0.04342 153 ILE A N   
1175 C CA  . ILE A 153 ? 0.42725 0.53667 0.43094 -0.01880 0.03475  -0.04926 153 ILE A CA  
1176 C C   . ILE A 153 ? 0.42817 0.56457 0.45324 -0.01752 0.03686  -0.05169 153 ILE A C   
1177 O O   . ILE A 153 ? 0.41250 0.56474 0.43235 -0.02189 0.04733  -0.05397 153 ILE A O   
1178 C CB  . ILE A 153 ? 0.43508 0.53617 0.42971 -0.00951 0.03983  -0.05793 153 ILE A CB  
1179 C CG1 . ILE A 153 ? 0.47320 0.55355 0.45437 -0.00965 0.03425  -0.05364 153 ILE A CG1 
1180 C CG2 . ILE A 153 ? 0.43408 0.54462 0.44882 0.00497  0.03641  -0.06850 153 ILE A CG2 
1181 C CD1 . ILE A 153 ? 0.49771 0.56772 0.45515 -0.01340 0.04233  -0.05297 153 ILE A CD1 
1182 N N   . PHE A 154 ? 0.42473 0.56893 0.47451 -0.01275 0.02544  -0.04971 154 PHE A N   
1183 C CA  . PHE A 154 ? 0.42222 0.59716 0.49803 -0.00952 0.02547  -0.05120 154 PHE A CA  
1184 C C   . PHE A 154 ? 0.41089 0.59541 0.50957 0.01256  0.02204  -0.06519 154 PHE A C   
1185 O O   . PHE A 154 ? 0.40786 0.57597 0.52004 0.02166  0.00565  -0.06547 154 PHE A O   
1186 C CB  . PHE A 154 ? 0.40904 0.58656 0.49817 -0.01919 0.01263  -0.03882 154 PHE A CB  
1187 C CG  . PHE A 154 ? 0.41250 0.58073 0.47746 -0.03971 0.01509  -0.02779 154 PHE A CG  
1188 C CD1 . PHE A 154 ? 0.41680 0.60235 0.47761 -0.05216 0.02165  -0.02323 154 PHE A CD1 
1189 C CD2 . PHE A 154 ? 0.40605 0.54992 0.45179 -0.04684 0.00946  -0.02222 154 PHE A CD2 
1190 C CE1 . PHE A 154 ? 0.40738 0.57724 0.44260 -0.07006 0.02072  -0.01482 154 PHE A CE1 
1191 C CE2 . PHE A 154 ? 0.40092 0.53539 0.42276 -0.06235 0.01120  -0.01583 154 PHE A CE2 
1192 C CZ  . PHE A 154 ? 0.43358 0.57660 0.44891 -0.07328 0.01586  -0.01289 154 PHE A CZ  
1193 N N   . PRO A 155 ? 0.42024 0.63001 0.52195 0.02137  0.03532  -0.07736 155 PRO A N   
1194 C CA  . PRO A 155 ? 0.46088 0.68467 0.58604 0.04602  0.03216  -0.09448 155 PRO A CA  
1195 C C   . PRO A 155 ? 0.43294 0.68259 0.59463 0.05392  0.02211  -0.09275 155 PRO A C   
1196 O O   . PRO A 155 ? 0.40693 0.69076 0.57871 0.04271  0.02883  -0.08450 155 PRO A O   
1197 C CB  . PRO A 155 ? 0.39340 0.64891 0.50972 0.04846  0.05219  -0.10610 155 PRO A CB  
1198 C CG  . PRO A 155 ? 0.42349 0.69540 0.52636 0.02306  0.06190  -0.09050 155 PRO A CG  
1199 C CD  . PRO A 155 ? 0.37698 0.60667 0.46097 0.00817  0.05218  -0.07565 155 PRO A CD  
1200 N N   . LEU A 156 ? 0.43079 0.66215 0.61206 0.07195  0.00318  -0.09891 156 LEU A N   
1201 C CA  . LEU A 156 ? 0.44428 0.70010 0.66398 0.08352  -0.00892 -0.09882 156 LEU A CA  
1202 C C   . LEU A 156 ? 0.45926 0.74040 0.70507 0.11621  -0.00823 -0.12306 156 LEU A C   
1203 O O   . LEU A 156 ? 0.38955 0.70568 0.67114 0.12882  -0.01344 -0.12555 156 LEU A O   
1204 C CB  . LEU A 156 ? 0.43530 0.65387 0.66257 0.07894  -0.03622 -0.08540 156 LEU A CB  
1205 C CG  . LEU A 156 ? 0.47913 0.68764 0.68821 0.04815  -0.03709 -0.06222 156 LEU A CG  
1206 C CD1 . LEU A 156 ? 0.47894 0.65350 0.69199 0.04287  -0.06393 -0.05003 156 LEU A CD1 
1207 C CD2 . LEU A 156 ? 0.45156 0.70027 0.67566 0.03630  -0.02974 -0.05261 156 LEU A CD2 
1208 N N   . THR A 157 ? 0.44368 0.70876 0.67261 0.13110  -0.00292 -0.14159 157 THR A N   
1209 C CA  . THR A 157 ? 0.45834 0.75909 0.70110 0.15902  0.00815  -0.16815 157 THR A CA  
1210 C C   . THR A 157 ? 0.49300 0.81856 0.70683 0.14606  0.03567  -0.17204 157 THR A C   
1211 O O   . THR A 157 ? 0.45461 0.76201 0.63943 0.11862  0.04255  -0.15492 157 THR A O   
1212 C CB  . THR A 157 ? 0.51903 0.77773 0.76235 0.18773  -0.01098 -0.18897 157 THR A CB  
1213 O OG1 . THR A 157 ? 0.57333 0.78463 0.77733 0.17590  -0.01153 -0.18693 157 THR A OG1 
1214 C CG2 . THR A 157 ? 0.49696 0.72227 0.76533 0.19638  -0.04379 -0.18128 157 THR A CG2 
1215 N N   . GLU A 158 ? 0.42539 0.79356 0.64656 0.16624  0.05043  -0.19513 158 GLU A N   
1216 C CA  . GLU A 158 ? 0.48387 0.87413 0.67495 0.15280  0.07402  -0.19887 158 GLU A CA  
1217 C C   . GLU A 158 ? 0.51691 0.84669 0.66986 0.14753  0.06907  -0.20048 158 GLU A C   
1218 O O   . GLU A 158 ? 0.54467 0.83240 0.69648 0.16727  0.05231  -0.21349 158 GLU A O   
1219 C CB  . GLU A 158 ? 0.47216 0.92590 0.67783 0.17620  0.09090  -0.22519 158 GLU A CB  
1220 C CG  . GLU A 158 ? 0.54902 0.99159 0.77438 0.21841  0.07790  -0.25536 158 GLU A CG  
1221 C CD  . GLU A 158 ? 0.67221 1.17767 0.90571 0.23897  0.09612  -0.27994 158 GLU A CD  
1222 O OE1 . GLU A 158 ? 0.68223 1.23541 0.90124 0.21544  0.11791  -0.27006 158 GLU A OE1 
1223 O OE2 . GLU A 158 ? 0.65384 1.14621 0.89978 0.27048  0.08386  -0.30066 158 GLU A OE2 
1224 N N   . PHE A 159 ? 0.47962 0.80234 0.60150 0.11979  0.08060  -0.18540 159 PHE A N   
1225 C CA  . PHE A 159 ? 0.53138 0.81365 0.61754 0.11479  0.08107  -0.18872 159 PHE A CA  
1226 C C   . PHE A 159 ? 0.55694 0.87808 0.62861 0.11927  0.10071  -0.20657 159 PHE A C   
1227 O O   . PHE A 159 ? 0.53233 0.89976 0.60011 0.10175  0.11763  -0.19901 159 PHE A O   
1228 C CB  . PHE A 159 ? 0.50695 0.76041 0.56778 0.08504  0.08133  -0.16415 159 PHE A CB  
1229 C CG  . PHE A 159 ? 0.53888 0.74816 0.60379 0.08049  0.06217  -0.14928 159 PHE A CG  
1230 C CD1 . PHE A 159 ? 0.53077 0.73409 0.62400 0.09509  0.04566  -0.15138 159 PHE A CD1 
1231 C CD2 . PHE A 159 ? 0.49237 0.66914 0.53281 0.06142  0.05993  -0.13303 159 PHE A CD2 
1232 C CE1 . PHE A 159 ? 0.55196 0.71941 0.64651 0.08677  0.02767  -0.13571 159 PHE A CE1 
1233 C CE2 . PHE A 159 ? 0.54613 0.69159 0.58934 0.05599  0.04415  -0.11962 159 PHE A CE2 
1234 C CZ  . PHE A 159 ? 0.56005 0.70142 0.62896 0.06671  0.02812  -0.12005 159 PHE A CZ  
1235 N N   . THR A 160 ? 0.60695 0.90946 0.66828 0.14061  0.09705  -0.22952 160 THR A N   
1236 C CA  . THR A 160 ? 0.61246 0.94887 0.65473 0.14505  0.11503  -0.24873 160 THR A CA  
1237 C C   . THR A 160 ? 0.68510 0.96866 0.68949 0.13986  0.10898  -0.25146 160 THR A C   
1238 O O   . THR A 160 ? 0.64454 0.86974 0.64173 0.13643  0.09037  -0.24052 160 THR A O   
1239 C CB  . THR A 160 ? 0.64115 1.01326 0.70633 0.17934  0.11732  -0.27844 160 THR A CB  
1240 O OG1 . THR A 160 ? 0.64388 0.96099 0.71179 0.20656  0.09497  -0.29577 160 THR A OG1 
1241 C CG2 . THR A 160 ? 0.60769 1.03504 0.71440 0.18489  0.12126  -0.27367 160 THR A CG2 
1242 N N   . GLU A 161 ? 0.69865 1.00715 0.67824 0.13751  0.12453  -0.26518 161 GLU A N   
1243 C CA  . GLU A 161 ? 0.77180 1.03320 0.71487 0.13336  0.11825  -0.26952 161 GLU A CA  
1244 C C   . GLU A 161 ? 0.80600 1.02412 0.75011 0.16266  0.09950  -0.29170 161 GLU A C   
1245 O O   . GLU A 161 ? 0.90692 1.07161 0.82522 0.15952  0.08585  -0.29159 161 GLU A O   
1246 C CB  . GLU A 161 ? 0.86829 1.15800 0.78503 0.11590  0.13438  -0.26689 161 GLU A CB  
1247 C CG  . GLU A 161 ? 0.87623 1.21286 0.79558 0.08785  0.14912  -0.24499 161 GLU A CG  
1248 C CD  . GLU A 161 ? 1.00074 1.35579 0.88974 0.06505  0.15979  -0.23775 161 GLU A CD  
1249 O OE1 . GLU A 161 ? 1.01310 1.33513 0.87329 0.06487  0.15590  -0.24450 161 GLU A OE1 
1250 O OE2 . GLU A 161 ? 1.02985 1.43231 0.92337 0.04580  0.17013  -0.22438 161 GLU A OE2 
1251 N N   . GLU A 162 ? 0.81581 1.05259 0.78933 0.18879  0.09544  -0.30706 162 GLU A N   
1252 C CA  . GLU A 162 ? 0.81648 1.00660 0.79284 0.21708  0.07281  -0.32673 162 GLU A CA  
1253 C C   . GLU A 162 ? 0.80444 0.94259 0.79337 0.22163  0.04693  -0.31899 162 GLU A C   
1254 O O   . GLU A 162 ? 0.83127 0.90661 0.80057 0.22319  0.02435  -0.31959 162 GLU A O   
1255 C CB  . GLU A 162 ? 0.82525 1.05400 0.83021 0.24383  0.07545  -0.34489 162 GLU A CB  
1256 C CG  . GLU A 162 ? 0.90907 1.19590 0.90443 0.23883  0.10021  -0.35177 162 GLU A CG  
1257 C CD  . GLU A 162 ? 0.94600 1.30419 0.97818 0.24564  0.11335  -0.35157 162 GLU A CD  
1258 O OE1 . GLU A 162 ? 0.85013 1.23670 0.89915 0.22767  0.12029  -0.33121 162 GLU A OE1 
1259 O OE2 . GLU A 162 ? 1.03864 1.42494 1.08222 0.26885  0.11601  -0.37201 162 GLU A OE2 
1260 N N   . ASN A 163 ? 0.74655 0.90469 0.76701 0.21408  0.04625  -0.29946 163 ASN A N   
1261 C CA  . ASN A 163 ? 0.72399 0.83403 0.76034 0.21315  0.01833  -0.28307 163 ASN A CA  
1262 C C   . ASN A 163 ? 0.73467 0.81533 0.75485 0.17926  0.01395  -0.24978 163 ASN A C   
1263 O O   . ASN A 163 ? 0.70013 0.75080 0.73266 0.17295  -0.00647 -0.23241 163 ASN A O   
1264 C CB  . ASN A 163 ? 0.69220 0.83570 0.77241 0.22625  0.01525  -0.28182 163 ASN A CB  
1265 C CG  . ASN A 163 ? 0.66519 0.86174 0.75798 0.20279  0.03696  -0.26065 163 ASN A CG  
1266 O OD1 . ASN A 163 ? 0.61878 0.81567 0.68860 0.17428  0.04926  -0.24182 163 ASN A OD1 
1267 N ND2 . ASN A 163 ? 0.65384 0.89330 0.78369 0.21516  0.03901  -0.26335 163 ASN A ND2 
1268 N N   . GLY A 164 ? 0.74635 0.83629 0.73946 0.15788  0.03135  -0.24079 164 GLY A N   
1269 C CA  . GLY A 164 ? 0.68240 0.73987 0.65824 0.13184  0.02449  -0.21421 164 GLY A CA  
1270 C C   . GLY A 164 ? 0.70270 0.78523 0.68548 0.10928  0.03710  -0.19049 164 GLY A C   
1271 O O   . GLY A 164 ? 0.58721 0.64752 0.57209 0.09576  0.02601  -0.16989 164 GLY A O   
1272 N N   . ALA A 165 ? 0.62401 0.75332 0.60825 0.10406  0.05919  -0.19322 165 ALA A N   
1273 C CA  . ALA A 165 ? 0.62343 0.76930 0.60654 0.08074  0.06918  -0.17139 165 ALA A CA  
1274 C C   . ALA A 165 ? 0.55872 0.66893 0.51694 0.06275  0.06428  -0.15429 165 ALA A C   
1275 O O   . ALA A 165 ? 0.50948 0.60035 0.44467 0.06173  0.06317  -0.15899 165 ALA A O   
1276 C CB  . ALA A 165 ? 0.57509 0.77095 0.55354 0.07273  0.09083  -0.17537 165 ALA A CB  
1277 N N   . THR A 166 ? 0.52457 0.62832 0.48781 0.04937  0.06098  -0.13509 166 THR A N   
1278 C CA  . THR A 166 ? 0.50424 0.57965 0.44939 0.03606  0.05558  -0.11961 166 THR A CA  
1279 C C   . THR A 166 ? 0.52593 0.60217 0.44491 0.02546  0.06596  -0.11849 166 THR A C   
1280 O O   . THR A 166 ? 0.54779 0.65014 0.46157 0.01826  0.07896  -0.12015 166 THR A O   
1281 C CB  . THR A 166 ? 0.49324 0.57061 0.44608 0.02491  0.05444  -0.10320 166 THR A CB  
1282 O OG1 . THR A 166 ? 0.51827 0.60521 0.49659 0.03202  0.04749  -0.10423 166 THR A OG1 
1283 C CG2 . THR A 166 ? 0.45141 0.50309 0.39355 0.01814  0.04523  -0.09038 166 THR A CG2 
1284 N N   . GLU A 167 ? 0.52615 0.57515 0.42855 0.02242  0.05833  -0.11374 167 GLU A N   
1285 C CA  . GLU A 167 ? 0.51336 0.55761 0.39073 0.01177  0.06398  -0.11033 167 GLU A CA  
1286 C C   . GLU A 167 ? 0.48434 0.51777 0.35656 0.00045  0.06168  -0.09242 167 GLU A C   
1287 O O   . GLU A 167 ? 0.49559 0.51523 0.37479 0.00227  0.05204  -0.08405 167 GLU A O   
1288 C CB  . GLU A 167 ? 0.48622 0.50784 0.34850 0.01614  0.05535  -0.11677 167 GLU A CB  
1289 C CG  . GLU A 167 ? 0.56165 0.58849 0.42625 0.03149  0.05550  -0.13873 167 GLU A CG  
1290 C CD  . GLU A 167 ? 0.66671 0.65904 0.52155 0.03857  0.03838  -0.14427 167 GLU A CD  
1291 O OE1 . GLU A 167 ? 0.70116 0.67128 0.54317 0.02806  0.02902  -0.13038 167 GLU A OE1 
1292 O OE2 . GLU A 167 ? 0.83666 0.82366 0.69684 0.05517  0.03246  -0.16268 167 GLU A OE2 
1293 N N   . VAL A 168 ? 0.48777 0.52870 0.34726 -0.01116 0.06929  -0.08687 168 VAL A N   
1294 C CA  . VAL A 168 ? 0.49598 0.52421 0.34919 -0.01902 0.06600  -0.07301 168 VAL A CA  
1295 C C   . VAL A 168 ? 0.53586 0.55366 0.36552 -0.02938 0.06547  -0.06765 168 VAL A C   
1296 O O   . VAL A 168 ? 0.52967 0.56042 0.34686 -0.03803 0.07199  -0.07161 168 VAL A O   
1297 C CB  . VAL A 168 ? 0.51519 0.55523 0.37478 -0.02496 0.07021  -0.06935 168 VAL A CB  
1298 C CG1 . VAL A 168 ? 0.48876 0.50929 0.33833 -0.03017 0.06455  -0.05840 168 VAL A CG1 
1299 C CG2 . VAL A 168 ? 0.50841 0.56084 0.39182 -0.01628 0.06977  -0.07376 168 VAL A CG2 
1300 N N   . ILE A 169 ? 0.54707 0.54530 0.37121 -0.02891 0.05720  -0.05827 169 ILE A N   
1301 C CA  . ILE A 169 ? 0.52387 0.50856 0.32762 -0.03834 0.05294  -0.05063 169 ILE A CA  
1302 C C   . ILE A 169 ? 0.57057 0.54427 0.36929 -0.04341 0.04911  -0.04213 169 ILE A C   
1303 O O   . ILE A 169 ? 0.55066 0.51476 0.35760 -0.03425 0.04383  -0.03871 169 ILE A O   
1304 C CB  . ILE A 169 ? 0.48788 0.45937 0.29005 -0.03347 0.04401  -0.04547 169 ILE A CB  
1305 C CG1 . ILE A 169 ? 0.54735 0.52216 0.35032 -0.02986 0.04401  -0.05416 169 ILE A CG1 
1306 C CG2 . ILE A 169 ? 0.55639 0.51389 0.33883 -0.04354 0.03780  -0.03651 169 ILE A CG2 
1307 C CD1 . ILE A 169 ? 0.46229 0.42600 0.26602 -0.02709 0.03273  -0.04702 169 ILE A CD1 
1308 N N   . LEU A 170 ? 0.54913 0.52484 0.33256 -0.05862 0.05060  -0.03901 170 LEU A N   
1309 C CA  . LEU A 170 ? 0.61882 0.57847 0.39362 -0.06615 0.04348  -0.03086 170 LEU A CA  
1310 C C   . LEU A 170 ? 0.59210 0.52138 0.35699 -0.06253 0.02963  -0.02268 170 LEU A C   
1311 O O   . LEU A 170 ? 0.59683 0.51977 0.35238 -0.06594 0.02502  -0.01839 170 LEU A O   
1312 C CB  . LEU A 170 ? 0.63854 0.60976 0.39694 -0.08827 0.04550  -0.02613 170 LEU A CB  
1313 C CG  . LEU A 170 ? 0.62842 0.63858 0.39898 -0.09054 0.05996  -0.03498 170 LEU A CG  
1314 C CD1 . LEU A 170 ? 0.64234 0.67209 0.39785 -0.11492 0.06151  -0.02748 170 LEU A CD1 
1315 C CD2 . LEU A 170 ? 0.54982 0.56511 0.34365 -0.07661 0.06296  -0.04055 170 LEU A CD2 
1316 N N   . GLY A 171 ? 0.61413 0.52469 0.38072 -0.05462 0.02206  -0.02134 171 GLY A N   
1317 C CA  . GLY A 171 ? 0.65855 0.54174 0.41905 -0.04568 0.00803  -0.01646 171 GLY A CA  
1318 C C   . GLY A 171 ? 0.62126 0.51372 0.39860 -0.02672 0.00887  -0.01902 171 GLY A C   
1319 O O   . GLY A 171 ? 0.63113 0.50781 0.40786 -0.01578 -0.00218 -0.01591 171 GLY A O   
1320 N N   . SER A 172 ? 0.55876 0.47698 0.35150 -0.02264 0.01968  -0.02388 172 SER A N   
1321 C CA  . SER A 172 ? 0.54333 0.47361 0.35023 -0.01026 0.01845  -0.02271 172 SER A CA  
1322 C C   . SER A 172 ? 0.55194 0.48967 0.37266 0.00680  0.01752  -0.02570 172 SER A C   
1323 O O   . SER A 172 ? 0.52770 0.48068 0.36041 0.01655  0.01519  -0.02264 172 SER A O   
1324 C CB  . SER A 172 ? 0.51097 0.46062 0.32649 -0.01366 0.02605  -0.02603 172 SER A CB  
1325 O OG  . SER A 172 ? 0.48527 0.44686 0.31131 -0.01192 0.03367  -0.03284 172 SER A OG  
1326 N N   . HIS A 173 ? 0.53590 0.46658 0.35426 0.00969  0.01906  -0.03140 173 HIS A N   
1327 C CA  . HIS A 173 ? 0.56385 0.50170 0.39084 0.02694  0.01802  -0.03644 173 HIS A CA  
1328 C C   . HIS A 173 ? 0.58692 0.51130 0.41080 0.04110  0.00699  -0.03537 173 HIS A C   
1329 O O   . HIS A 173 ? 0.59009 0.53233 0.42547 0.05909  0.00716  -0.03984 173 HIS A O   
1330 C CB  . HIS A 173 ? 0.57821 0.50580 0.39835 0.02613  0.01994  -0.04355 173 HIS A CB  
1331 C CG  . HIS A 173 ? 0.65018 0.54221 0.44885 0.01636  0.01103  -0.04218 173 HIS A CG  
1332 N ND1 . HIS A 173 ? 0.61615 0.50295 0.40544 -0.00372 0.01189  -0.03591 173 HIS A ND1 
1333 C CD2 . HIS A 173 ? 0.66226 0.52253 0.44540 0.02262  -0.00060 -0.04595 173 HIS A CD2 
1334 C CE1 . HIS A 173 ? 0.67340 0.52925 0.44250 -0.01293 0.00076  -0.03288 173 HIS A CE1 
1335 N NE2 . HIS A 173 ? 0.73120 0.56567 0.49534 0.00297  -0.00851 -0.03893 173 HIS A NE2 
1336 N N   . ARG A 174 ? 0.60999 0.50676 0.41935 0.03337  -0.00326 -0.02925 174 ARG A N   
1337 C CA  . ARG A 174 ? 0.62798 0.50842 0.43559 0.04665  -0.01734 -0.02666 174 ARG A CA  
1338 C C   . ARG A 174 ? 0.59074 0.49338 0.41160 0.04900  -0.01866 -0.01794 174 ARG A C   
1339 O O   . ARG A 174 ? 0.60397 0.49917 0.42806 0.06142  -0.03078 -0.01461 174 ARG A O   
1340 C CB  . ARG A 174 ? 0.67930 0.51561 0.46280 0.03375  -0.03226 -0.02118 174 ARG A CB  
1341 C CG  . ARG A 174 ? 0.71531 0.52582 0.48329 0.02986  -0.03543 -0.02767 174 ARG A CG  
1342 C CD  . ARG A 174 ? 0.81760 0.58188 0.55945 0.01444  -0.05518 -0.01928 174 ARG A CD  
1343 N NE  . ARG A 174 ? 0.89284 0.66377 0.62378 -0.01498 -0.05105 -0.00784 174 ARG A NE  
1344 C CZ  . ARG A 174 ? 0.86290 0.63754 0.58339 -0.03571 -0.04494 -0.00600 174 ARG A CZ  
1345 N NH1 . ARG A 174 ? 0.82220 0.58813 0.53953 -0.03338 -0.04461 -0.01261 174 ARG A NH1 
1346 N NH2 . ARG A 174 ? 0.88541 0.67606 0.59821 -0.05940 -0.03902 0.00239  174 ARG A NH2 
1347 N N   . TRP A 175 ? 0.60171 0.52960 0.43022 0.03799  -0.00884 -0.01402 175 TRP A N   
1348 C CA  . TRP A 175 ? 0.59015 0.53843 0.42959 0.03836  -0.01213 -0.00469 175 TRP A CA  
1349 C C   . TRP A 175 ? 0.58194 0.56655 0.44399 0.05730  -0.01034 -0.00582 175 TRP A C   
1350 O O   . TRP A 175 ? 0.53294 0.53587 0.40276 0.06460  -0.00174 -0.01378 175 TRP A O   
1351 C CB  . TRP A 175 ? 0.55913 0.51814 0.39666 0.02107  -0.00538 -0.00127 175 TRP A CB  
1352 C CG  . TRP A 175 ? 0.54923 0.48554 0.36615 0.00302  -0.00466 -0.00123 175 TRP A CG  
1353 C CD1 . TRP A 175 ? 0.60548 0.51481 0.40448 -0.00444 -0.01054 0.00010  175 TRP A CD1 
1354 C CD2 . TRP A 175 ? 0.52302 0.46405 0.33370 -0.01044 0.00159  -0.00307 175 TRP A CD2 
1355 N NE1 . TRP A 175 ? 0.61218 0.51669 0.39475 -0.02338 -0.00606 0.00004  175 TRP A NE1 
1356 C CE2 . TRP A 175 ? 0.60665 0.53015 0.39639 -0.02493 0.00218  -0.00396 175 TRP A CE2 
1357 C CE3 . TRP A 175 ? 0.51537 0.47282 0.33490 -0.01169 0.00492  -0.00433 175 TRP A CE3 
1358 C CZ2 . TRP A 175 ? 0.51938 0.44663 0.29808 -0.03724 0.00892  -0.00898 175 TRP A CZ2 
1359 C CZ3 . TRP A 175 ? 0.52855 0.48080 0.33647 -0.02253 0.00875  -0.00978 175 TRP A CZ3 
1360 C CH2 . TRP A 175 ? 0.54624 0.48598 0.33437 -0.03366 0.01214  -0.01347 175 TRP A CH2 
1361 N N   . THR A 176 ? 0.58668 0.58653 0.45936 0.06332  -0.01867 0.00346  176 THR A N   
1362 C CA  . THR A 176 ? 0.58608 0.63210 0.48231 0.07922  -0.01664 0.00473  176 THR A CA  
1363 C C   . THR A 176 ? 0.57044 0.64934 0.47529 0.06547  -0.00934 0.01110  176 THR A C   
1364 O O   . THR A 176 ? 0.54480 0.66079 0.46342 0.07269  -0.00265 0.00848  176 THR A O   
1365 C CB  . THR A 176 ? 0.62139 0.67793 0.52876 0.08879  -0.02912 0.01465  176 THR A CB  
1366 O OG1 . THR A 176 ? 0.65952 0.68446 0.56091 0.10576  -0.03900 0.00731  176 THR A OG1 
1367 C CG2 . THR A 176 ? 0.62618 0.74264 0.56024 0.10200  -0.02612 0.01856  176 THR A CG2 
1368 N N   . GLU A 177 ? 0.56569 0.63019 0.46042 0.04498  -0.01196 0.01904  177 GLU A N   
1369 C CA  . GLU A 177 ? 0.57652 0.66091 0.47586 0.03135  -0.00956 0.02447  177 GLU A CA  
1370 C C   . GLU A 177 ? 0.56653 0.61738 0.44773 0.01559  -0.00751 0.01980  177 GLU A C   
1371 O O   . GLU A 177 ? 0.55552 0.57524 0.42047 0.01187  -0.00756 0.01535  177 GLU A O   
1372 C CB  . GLU A 177 ? 0.59486 0.70762 0.50471 0.02438  -0.01936 0.04118  177 GLU A CB  
1373 C CG  . GLU A 177 ? 0.68845 0.78552 0.59260 0.02341  -0.02953 0.04902  177 GLU A CG  
1374 C CD  . GLU A 177 ? 0.87465 1.01199 0.79653 0.02310  -0.03909 0.06587  177 GLU A CD  
1375 O OE1 . GLU A 177 ? 0.90708 1.07454 0.83714 0.01218  -0.04093 0.07535  177 GLU A OE1 
1376 O OE2 . GLU A 177 ? 0.96154 1.10132 0.88964 0.03267  -0.04664 0.07111  177 GLU A OE2 
1377 N N   . VAL A 178 ? 0.51241 0.57225 0.39668 0.00638  -0.00668 0.02080  178 VAL A N   
1378 C CA  . VAL A 178 ? 0.53901 0.57135 0.40904 -0.00469 -0.00570 0.01426  178 VAL A CA  
1379 C C   . VAL A 178 ? 0.56270 0.57501 0.41687 -0.01486 -0.01366 0.01889  178 VAL A C   
1380 O O   . VAL A 178 ? 0.53097 0.51883 0.36819 -0.01933 -0.01002 0.01058  178 VAL A O   
1381 C CB  . VAL A 178 ? 0.47521 0.51793 0.35282 -0.01104 -0.00832 0.01555  178 VAL A CB  
1382 C CG1 . VAL A 178 ? 0.52868 0.54294 0.39307 -0.01845 -0.01000 0.00707  178 VAL A CG1 
1383 C CG2 . VAL A 178 ? 0.51300 0.57197 0.40193 -0.00337 0.00034  0.00971  178 VAL A CG2 
1384 N N   . GLY A 179 ? 0.53405 0.56000 0.39252 -0.02002 -0.02475 0.03295  179 GLY A N   
1385 C CA  . GLY A 179 ? 0.52238 0.52748 0.36290 -0.03167 -0.03381 0.03784  179 GLY A CA  
1386 C C   . GLY A 179 ? 0.52468 0.50806 0.35025 -0.04206 -0.03749 0.03095  179 GLY A C   
1387 O O   . GLY A 179 ? 0.53962 0.52787 0.37313 -0.04211 -0.03874 0.02866  179 GLY A O   
1388 N N   . THR A 180 ? 0.53688 0.49478 0.33919 -0.05036 -0.04034 0.02655  180 THR A N   
1389 C CA  . THR A 180 ? 0.56884 0.50259 0.35285 -0.05701 -0.04475 0.01596  180 THR A CA  
1390 C C   . THR A 180 ? 0.56852 0.48738 0.33514 -0.05501 -0.03185 -0.00216 180 THR A C   
1391 O O   . THR A 180 ? 0.57662 0.47907 0.31895 -0.06349 -0.03436 -0.00632 180 THR A O   
1392 C CB  . THR A 180 ? 0.57412 0.49432 0.34163 -0.07092 -0.06208 0.02679  180 THR A CB  
1393 O OG1 . THR A 180 ? 0.60662 0.52622 0.36429 -0.07617 -0.06254 0.03441  180 THR A OG1 
1394 C CG2 . THR A 180 ? 0.51445 0.45372 0.29864 -0.07662 -0.07657 0.04582  180 THR A CG2 
1395 N N   . PRO A 181 ? 0.52343 0.45126 0.30092 -0.04573 -0.01818 -0.01232 181 PRO A N   
1396 C CA  . PRO A 181 ? 0.57739 0.50094 0.34027 -0.04662 -0.00561 -0.02582 181 PRO A CA  
1397 C C   . PRO A 181 ? 0.56636 0.47907 0.31439 -0.04594 -0.00379 -0.04375 181 PRO A C   
1398 O O   . PRO A 181 ? 0.55653 0.46327 0.31264 -0.03938 -0.00976 -0.04990 181 PRO A O   
1399 C CB  . PRO A 181 ? 0.52635 0.46452 0.30764 -0.03789 0.00555  -0.02896 181 PRO A CB  
1400 C CG  . PRO A 181 ? 0.53606 0.48313 0.33903 -0.03086 0.00007  -0.02415 181 PRO A CG  
1401 C CD  . PRO A 181 ? 0.54863 0.49490 0.35108 -0.03643 -0.01396 -0.00965 181 PRO A CD  
1402 N N   . GLU A 182 ? 0.55319 0.46400 0.27855 -0.05269 0.00327  -0.05241 182 GLU A N   
1403 C CA  . GLU A 182 ? 0.58836 0.49559 0.29812 -0.04904 0.00831  -0.07381 182 GLU A CA  
1404 C C   . GLU A 182 ? 0.58924 0.51617 0.31578 -0.03762 0.02230  -0.08753 182 GLU A C   
1405 O O   . GLU A 182 ? 0.58668 0.52947 0.32726 -0.03849 0.03042  -0.08034 182 GLU A O   
1406 C CB  . GLU A 182 ? 0.63107 0.53895 0.30985 -0.06181 0.01322  -0.07849 182 GLU A CB  
1407 C CG  . GLU A 182 ? 0.63806 0.52784 0.29789 -0.07582 -0.00073 -0.06382 182 GLU A CG  
1408 C CD  . GLU A 182 ? 0.64637 0.53661 0.27190 -0.08913 0.00376  -0.07169 182 GLU A CD  
1409 O OE1 . GLU A 182 ? 0.70654 0.61323 0.32383 -0.08484 0.01788  -0.09139 182 GLU A OE1 
1410 O OE2 . GLU A 182 ? 0.72325 0.60089 0.32986 -0.10420 -0.00688 -0.05851 182 GLU A OE2 
1411 N N   . ARG A 183 ? 0.59825 0.52296 0.32259 -0.02626 0.02350  -0.10801 183 ARG A N   
1412 C CA  . ARG A 183 ? 0.57444 0.52216 0.31687 -0.01424 0.03610  -0.12171 183 ARG A CA  
1413 C C   . ARG A 183 ? 0.58074 0.55877 0.31443 -0.02294 0.05374  -0.12472 183 ARG A C   
1414 O O   . ARG A 183 ? 0.56044 0.56226 0.31201 -0.02029 0.06381  -0.12503 183 ARG A O   
1415 C CB  . ARG A 183 ? 0.58072 0.51898 0.32230 0.00261  0.03150  -0.14491 183 ARG A CB  
1416 C CG  . ARG A 183 ? 0.60507 0.50968 0.35368 0.00730  0.00942  -0.13878 183 ARG A CG  
1417 C CD  . ARG A 183 ? 0.59076 0.50347 0.37162 0.01312  0.00700  -0.12948 183 ARG A CD  
1418 N NE  . ARG A 183 ? 0.64782 0.53931 0.43464 0.00663  -0.01242 -0.11117 183 ARG A NE  
1419 C CZ  . ARG A 183 ? 0.69489 0.58894 0.50513 0.00901  -0.01972 -0.10188 183 ARG A CZ  
1420 N NH1 . ARG A 183 ? 0.62073 0.53211 0.45135 0.01917  -0.01109 -0.10977 183 ARG A NH1 
1421 N NH2 . ARG A 183 ? 0.66792 0.55032 0.48091 -0.00085 -0.03673 -0.08300 183 ARG A NH2 
1422 N N   . ASP A 184 ? 0.58065 0.55889 0.28566 -0.03643 0.05594  -0.12462 184 ASP A N   
1423 C CA  . ASP A 184 ? 0.57694 0.58629 0.27007 -0.04954 0.07045  -0.12505 184 ASP A CA  
1424 C C   . ASP A 184 ? 0.62613 0.63507 0.32364 -0.06484 0.06848  -0.10131 184 ASP A C   
1425 O O   . ASP A 184 ? 0.62348 0.65396 0.30923 -0.08046 0.07626  -0.09676 184 ASP A O   
1426 C CB  . ASP A 184 ? 0.61385 0.62599 0.27144 -0.06059 0.07285  -0.13411 184 ASP A CB  
1427 C CG  . ASP A 184 ? 0.62485 0.60568 0.26254 -0.07562 0.05801  -0.11648 184 ASP A CG  
1428 O OD1 . ASP A 184 ? 0.60418 0.57102 0.25419 -0.08126 0.04911  -0.09477 184 ASP A OD1 
1429 O OD2 . ASP A 184 ? 0.65721 0.62874 0.26614 -0.08133 0.05481  -0.12508 184 ASP A OD2 
1430 N N   . GLN A 185 ? 0.57429 0.56019 0.28718 -0.06095 0.05703  -0.08644 185 GLN A N   
1431 C CA  . GLN A 185 ? 0.56591 0.54904 0.28680 -0.06825 0.05427  -0.06875 185 GLN A CA  
1432 C C   . GLN A 185 ? 0.56853 0.56660 0.31292 -0.05995 0.06129  -0.07145 185 GLN A C   
1433 O O   . GLN A 185 ? 0.55229 0.54794 0.29989 -0.06628 0.05950  -0.05983 185 GLN A O   
1434 C CB  . GLN A 185 ? 0.58063 0.53928 0.30817 -0.06518 0.04002  -0.05385 185 GLN A CB  
1435 C CG  . GLN A 185 ? 0.64349 0.58679 0.34892 -0.07718 0.03010  -0.04458 185 GLN A CG  
1436 C CD  . GLN A 185 ? 0.64754 0.57573 0.36500 -0.07152 0.01656  -0.03083 185 GLN A CD  
1437 O OE1 . GLN A 185 ? 0.68756 0.60735 0.40240 -0.07007 0.00869  -0.03050 185 GLN A OE1 
1438 N NE2 . GLN A 185 ? 0.62839 0.55443 0.35881 -0.06804 0.01280  -0.01968 185 GLN A NE2 
1439 N N   . ALA A 186 ? 0.54866 0.55879 0.30842 -0.04591 0.06683  -0.08635 186 ALA A N   
1440 C CA  . ALA A 186 ? 0.55877 0.58347 0.34205 -0.03829 0.07191  -0.08834 186 ALA A CA  
1441 C C   . ALA A 186 ? 0.59094 0.65107 0.37402 -0.04175 0.08561  -0.09906 186 ALA A C   
1442 O O   . ALA A 186 ? 0.59256 0.66874 0.36032 -0.04419 0.09241  -0.11057 186 ALA A O   
1443 C CB  . ALA A 186 ? 0.52924 0.54489 0.33315 -0.02115 0.06569  -0.09490 186 ALA A CB  
1444 N N   . VAL A 187 ? 0.55555 0.63107 0.35479 -0.04301 0.08954  -0.09476 187 VAL A N   
1445 C CA  . VAL A 187 ? 0.57694 0.69357 0.38404 -0.04490 0.10186  -0.10318 187 VAL A CA  
1446 C C   . VAL A 187 ? 0.56509 0.68986 0.40259 -0.02673 0.10187  -0.11142 187 VAL A C   
1447 O O   . VAL A 187 ? 0.53135 0.63080 0.38104 -0.01950 0.09235  -0.10537 187 VAL A O   
1448 C CB  . VAL A 187 ? 0.56397 0.69410 0.36159 -0.06752 0.10375  -0.08767 187 VAL A CB  
1449 C CG1 . VAL A 187 ? 0.64556 0.77066 0.41216 -0.08746 0.10188  -0.07946 187 VAL A CG1 
1450 C CG2 . VAL A 187 ? 0.57570 0.67735 0.38102 -0.06906 0.09350  -0.07334 187 VAL A CG2 
1451 N N   . LEU A 188 ? 0.53083 0.69483 0.38104 -0.01963 0.11215  -0.12504 188 LEU A N   
1452 C CA  . LEU A 188 ? 0.54205 0.71506 0.42195 0.00050  0.11042  -0.13579 188 LEU A CA  
1453 C C   . LEU A 188 ? 0.52391 0.72142 0.42272 -0.00687 0.11341  -0.12575 188 LEU A C   
1454 O O   . LEU A 188 ? 0.52390 0.75634 0.41760 -0.02234 0.12277  -0.12076 188 LEU A O   
1455 C CB  . LEU A 188 ? 0.55970 0.76111 0.44533 0.01870  0.11798  -0.16035 188 LEU A CB  
1456 C CG  . LEU A 188 ? 0.65945 0.82707 0.53410 0.03450  0.10891  -0.17493 188 LEU A CG  
1457 C CD1 . LEU A 188 ? 0.72833 0.88668 0.56825 0.02043  0.11218  -0.17375 188 LEU A CD1 
1458 C CD2 . LEU A 188 ? 0.72727 0.91632 0.61747 0.06060  0.11140  -0.20161 188 LEU A CD2 
1459 N N   . ALA A 189 ? 0.54179 0.72166 0.46061 0.00153  0.10400  -0.12129 189 ALA A N   
1460 C CA  . ALA A 189 ? 0.50462 0.70522 0.44302 -0.00365 0.10457  -0.11299 189 ALA A CA  
1461 C C   . ALA A 189 ? 0.50685 0.74541 0.47400 0.01415  0.10874  -0.12822 189 ALA A C   
1462 O O   . ALA A 189 ? 0.51745 0.74788 0.50782 0.02803  0.09945  -0.13083 189 ALA A O   
1463 C CB  . ALA A 189 ? 0.50037 0.66646 0.44407 -0.00447 0.09233  -0.10103 189 ALA A CB  
1464 N N   . THR A 190 ? 0.51947 0.80246 0.48472 0.01389  0.12217  -0.13862 190 THR A N   
1465 C CA  . THR A 190 ? 0.48067 0.81131 0.47519 0.03246  0.12837  -0.15467 190 THR A CA  
1466 C C   . THR A 190 ? 0.49812 0.86157 0.51401 0.02054  0.12937  -0.14026 190 THR A C   
1467 O O   . THR A 190 ? 0.48983 0.86987 0.49142 -0.00558 0.13456  -0.12412 190 THR A O   
1468 C CB  . THR A 190 ? 0.50655 0.88260 0.49062 0.03559  0.14429  -0.17138 190 THR A CB  
1469 O OG1 . THR A 190 ? 0.46393 0.86508 0.42649 0.00496  0.15358  -0.15522 190 THR A OG1 
1470 C CG2 . THR A 190 ? 0.55086 0.89084 0.51231 0.04802  0.14123  -0.18696 190 THR A CG2 
1471 N N   . MET A 191 ? 0.49354 0.86229 0.54195 0.03764  0.12138  -0.14428 191 MET A N   
1472 C CA  . MET A 191 ? 0.47328 0.86434 0.54144 0.02526  0.11849  -0.12827 191 MET A CA  
1473 C C   . MET A 191 ? 0.43548 0.86439 0.54525 0.04924  0.11611  -0.14057 191 MET A C   
1474 O O   . MET A 191 ? 0.44973 0.86645 0.57276 0.07733  0.11005  -0.15976 191 MET A O   
1475 C CB  . MET A 191 ? 0.42468 0.76224 0.48443 0.01357  0.10396  -0.11067 191 MET A CB  
1476 C CG  . MET A 191 ? 0.46303 0.76297 0.48563 -0.00799 0.10380  -0.09765 191 MET A CG  
1477 S SD  . MET A 191 ? 0.47582 0.71933 0.49038 -0.01421 0.08817  -0.08334 191 MET A SD  
1478 C CE  . MET A 191 ? 0.48430 0.69674 0.50759 0.01005  0.07841  -0.09603 191 MET A CE  
1479 N N   . ASP A 192 ? 0.40776 0.87997 0.53759 0.03770  0.11835  -0.12864 192 ASP A N   
1480 C CA  . ASP A 192 ? 0.38416 0.88868 0.55670 0.05595  0.11186  -0.13315 192 ASP A CA  
1481 C C   . ASP A 192 ? 0.39591 0.85675 0.57476 0.04776  0.09327  -0.11585 192 ASP A C   
1482 O O   . ASP A 192 ? 0.37964 0.80329 0.53094 0.02347  0.08984  -0.09857 192 ASP A O   
1483 C CB  . ASP A 192 ? 0.39873 0.98283 0.59058 0.04448  0.12435  -0.12692 192 ASP A CB  
1484 C CG  . ASP A 192 ? 0.48001 1.12354 0.67285 0.05648  0.14349  -0.14693 192 ASP A CG  
1485 O OD1 . ASP A 192 ? 0.50224 1.14349 0.70568 0.09017  0.14413  -0.17358 192 ASP A OD1 
1486 O OD2 . ASP A 192 ? 0.52270 1.21524 0.70377 0.03103  0.15658  -0.13584 192 ASP A OD2 
1487 N N   . PRO A 193 ? 0.37575 0.83992 0.58963 0.06799  0.07985  -0.12060 193 PRO A N   
1488 C CA  . PRO A 193 ? 0.39675 0.82839 0.61710 0.05624  0.06199  -0.10195 193 PRO A CA  
1489 C C   . PRO A 193 ? 0.39965 0.85698 0.61570 0.02575  0.06599  -0.08003 193 PRO A C   
1490 O O   . PRO A 193 ? 0.36592 0.88438 0.59946 0.02158  0.07592  -0.07852 193 PRO A O   
1491 C CB  . PRO A 193 ? 0.42518 0.87093 0.68886 0.08408  0.04729  -0.11178 193 PRO A CB  
1492 C CG  . PRO A 193 ? 0.41535 0.87897 0.68776 0.11544  0.05469  -0.13985 193 PRO A CG  
1493 C CD  . PRO A 193 ? 0.40794 0.90897 0.65768 0.10259  0.07927  -0.14336 193 PRO A CD  
1494 N N   . GLY A 194 ? 0.42834 0.84008 0.61957 0.00393  0.05746  -0.06324 194 GLY A N   
1495 C CA  . GLY A 194 ? 0.41771 0.83728 0.59361 -0.02679 0.05847  -0.04338 194 GLY A CA  
1496 C C   . GLY A 194 ? 0.43572 0.82915 0.56812 -0.04641 0.06690  -0.03877 194 GLY A C   
1497 O O   . GLY A 194 ? 0.42262 0.80157 0.53322 -0.07206 0.06282  -0.02270 194 GLY A O   
1498 N N   . ASP A 195 ? 0.39147 0.77628 0.50989 -0.03486 0.07645  -0.05262 195 ASP A N   
1499 C CA  . ASP A 195 ? 0.40271 0.75215 0.48054 -0.04972 0.08053  -0.04885 195 ASP A CA  
1500 C C   . ASP A 195 ? 0.41064 0.70038 0.47129 -0.04713 0.07011  -0.04698 195 ASP A C   
1501 O O   . ASP A 195 ? 0.40491 0.68251 0.48355 -0.03454 0.06049  -0.04919 195 ASP A O   
1502 C CB  . ASP A 195 ? 0.41575 0.77915 0.48504 -0.03936 0.09326  -0.06338 195 ASP A CB  
1503 C CG  . ASP A 195 ? 0.48989 0.92110 0.57221 -0.04460 0.10591  -0.06525 195 ASP A CG  
1504 O OD1 . ASP A 195 ? 0.47811 0.94165 0.56926 -0.06320 0.10439  -0.05062 195 ASP A OD1 
1505 O OD2 . ASP A 195 ? 0.46788 0.92284 0.55016 -0.03150 0.11722  -0.08102 195 ASP A OD2 
1506 N N   . VAL A 196 ? 0.40580 0.66046 0.43168 -0.05963 0.07079  -0.04218 196 VAL A N   
1507 C CA  . VAL A 196 ? 0.46387 0.67015 0.47240 -0.05674 0.06315  -0.04124 196 VAL A CA  
1508 C C   . VAL A 196 ? 0.45890 0.64018 0.43968 -0.05672 0.06811  -0.04515 196 VAL A C   
1509 O O   . VAL A 196 ? 0.48447 0.66644 0.44509 -0.07148 0.07154  -0.03998 196 VAL A O   
1510 C CB  . VAL A 196 ? 0.46527 0.65062 0.45948 -0.07337 0.05427  -0.02891 196 VAL A CB  
1511 C CG1 . VAL A 196 ? 0.46990 0.61439 0.44543 -0.06853 0.04909  -0.03037 196 VAL A CG1 
1512 C CG2 . VAL A 196 ? 0.44180 0.65062 0.46270 -0.07587 0.04731  -0.02276 196 VAL A CG2 
1513 N N   . LEU A 197 ? 0.41457 0.57375 0.39394 -0.04229 0.06621  -0.05226 197 LEU A N   
1514 C CA  . LEU A 197 ? 0.47364 0.60670 0.42788 -0.04219 0.06842  -0.05401 197 LEU A CA  
1515 C C   . LEU A 197 ? 0.47645 0.57673 0.41402 -0.04552 0.06125  -0.04801 197 LEU A C   
1516 O O   . LEU A 197 ? 0.41104 0.50622 0.35867 -0.04012 0.05521  -0.04705 197 LEU A O   
1517 C CB  . LEU A 197 ? 0.41739 0.54813 0.37798 -0.02592 0.06986  -0.06467 197 LEU A CB  
1518 C CG  . LEU A 197 ? 0.48032 0.58473 0.41755 -0.02550 0.07018  -0.06500 197 LEU A CG  
1519 C CD1 . LEU A 197 ? 0.46095 0.56780 0.37703 -0.03843 0.07621  -0.06205 197 LEU A CD1 
1520 C CD2 . LEU A 197 ? 0.42916 0.52860 0.37195 -0.01129 0.06846  -0.07428 197 LEU A CD2 
1521 N N   . ILE A 198 ? 0.46981 0.54912 0.38138 -0.05422 0.06079  -0.04430 198 ILE A N   
1522 C CA  . ILE A 198 ? 0.49018 0.53994 0.38410 -0.05390 0.05450  -0.04207 198 ILE A CA  
1523 C C   . ILE A 198 ? 0.48054 0.51067 0.35953 -0.04650 0.05478  -0.04485 198 ILE A C   
1524 O O   . ILE A 198 ? 0.50855 0.53322 0.37440 -0.05254 0.05602  -0.04352 198 ILE A O   
1525 C CB  . ILE A 198 ? 0.53386 0.56977 0.40945 -0.06896 0.04885  -0.03590 198 ILE A CB  
1526 C CG1 . ILE A 198 ? 0.49645 0.55468 0.38974 -0.07637 0.04743  -0.03167 198 ILE A CG1 
1527 C CG2 . ILE A 198 ? 0.51208 0.51478 0.36584 -0.06432 0.04223  -0.03812 198 ILE A CG2 
1528 C CD1 . ILE A 198 ? 0.58788 0.63230 0.46346 -0.09300 0.03960  -0.02456 198 ILE A CD1 
1529 N N   . VAL A 199 ? 0.47328 0.49678 0.35500 -0.03523 0.05277  -0.04710 199 VAL A N   
1530 C CA  . VAL A 199 ? 0.47752 0.49039 0.35207 -0.02658 0.05253  -0.04871 199 VAL A CA  
1531 C C   . VAL A 199 ? 0.47026 0.46860 0.33326 -0.01961 0.04836  -0.04943 199 VAL A C   
1532 O O   . VAL A 199 ? 0.44412 0.45219 0.31404 -0.01630 0.04743  -0.04981 199 VAL A O   
1533 C CB  . VAL A 199 ? 0.47441 0.50113 0.36606 -0.01917 0.05330  -0.05034 199 VAL A CB  
1534 C CG1 . VAL A 199 ? 0.46161 0.47917 0.34573 -0.01246 0.05140  -0.04957 199 VAL A CG1 
1535 C CG2 . VAL A 199 ? 0.49022 0.53042 0.39098 -0.02136 0.05765  -0.05416 199 VAL A CG2 
1536 N N   . ARG A 200 ? 0.51194 0.48872 0.35708 -0.01729 0.04500  -0.04997 200 ARG A N   
1537 C CA  . ARG A 200 ? 0.50278 0.46653 0.33759 -0.00537 0.04068  -0.05372 200 ARG A CA  
1538 C C   . ARG A 200 ? 0.51597 0.50080 0.36465 0.00591  0.04309  -0.05361 200 ARG A C   
1539 O O   . ARG A 200 ? 0.43504 0.43201 0.29514 0.00422  0.04489  -0.04972 200 ARG A O   
1540 C CB  . ARG A 200 ? 0.54820 0.48221 0.36371 -0.00454 0.03334  -0.05329 200 ARG A CB  
1541 C CG  . ARG A 200 ? 0.58775 0.50434 0.39224 0.01164  0.02662  -0.05984 200 ARG A CG  
1542 C CD  . ARG A 200 ? 0.60687 0.49792 0.39945 0.01522  0.01737  -0.05744 200 ARG A CD  
1543 N NE  . ARG A 200 ? 0.68978 0.55342 0.46754 0.03086  0.00674  -0.06582 200 ARG A NE  
1544 C CZ  . ARG A 200 ? 0.73275 0.61060 0.51839 0.05286  0.00827  -0.07417 200 ARG A CZ  
1545 N NH1 . ARG A 200 ? 0.64398 0.56319 0.45130 0.05808  0.01869  -0.07194 200 ARG A NH1 
1546 N NH2 . ARG A 200 ? 0.70355 0.55483 0.47443 0.07001  -0.00207 -0.08521 200 ARG A NH2 
1547 N N   . GLN A 201 ? 0.51300 0.50337 0.35892 0.01693  0.04222  -0.05814 201 GLN A N   
1548 C CA  . GLN A 201 ? 0.47191 0.48685 0.32887 0.02704  0.04343  -0.05654 201 GLN A CA  
1549 C C   . GLN A 201 ? 0.47669 0.48252 0.33267 0.03215  0.04028  -0.05338 201 GLN A C   
1550 O O   . GLN A 201 ? 0.48568 0.46307 0.32766 0.03368  0.03554  -0.05538 201 GLN A O   
1551 C CB  . GLN A 201 ? 0.44671 0.47200 0.29767 0.04018  0.04406  -0.06477 201 GLN A CB  
1552 C CG  . GLN A 201 ? 0.43994 0.50138 0.30283 0.05070  0.04619  -0.06307 201 GLN A CG  
1553 C CD  . GLN A 201 ? 0.43411 0.50900 0.28891 0.06663  0.04845  -0.07527 201 GLN A CD  
1554 O OE1 . GLN A 201 ? 0.46196 0.52291 0.30302 0.06530  0.04868  -0.08343 201 GLN A OE1 
1555 N NE2 . GLN A 201 ? 0.41833 0.52234 0.28120 0.08205  0.04988  -0.07720 201 GLN A NE2 
1556 N N   . ARG A 202 ? 0.48371 0.51217 0.35314 0.03217  0.04048  -0.04660 202 ARG A N   
1557 C CA  . ARG A 202 ? 0.44597 0.47287 0.31686 0.03527  0.03658  -0.04120 202 ARG A CA  
1558 C C   . ARG A 202 ? 0.49704 0.50421 0.36197 0.02372  0.03549  -0.03810 202 ARG A C   
1559 O O   . ARG A 202 ? 0.44131 0.44396 0.30401 0.02374  0.03142  -0.03330 202 ARG A O   
1560 C CB  . ARG A 202 ? 0.53236 0.54639 0.39523 0.04996  0.03189  -0.04515 202 ARG A CB  
1561 C CG  . ARG A 202 ? 0.55494 0.59409 0.42405 0.06711  0.03324  -0.05096 202 ARG A CG  
1562 C CD  . ARG A 202 ? 0.61550 0.63005 0.47431 0.08435  0.02592  -0.05861 202 ARG A CD  
1563 N NE  . ARG A 202 ? 0.62856 0.63897 0.49166 0.08659  0.01887  -0.05037 202 ARG A NE  
1564 C CZ  . ARG A 202 ? 0.62716 0.66874 0.50528 0.10010  0.01735  -0.04751 202 ARG A CZ  
1565 N NH1 . ARG A 202 ? 0.58212 0.66579 0.47234 0.11290  0.02366  -0.05283 202 ARG A NH1 
1566 N NH2 . ARG A 202 ? 0.56659 0.60108 0.44754 0.09962  0.00917  -0.03839 202 ARG A NH2 
1567 N N   . VAL A 203 ? 0.46052 0.45932 0.32259 0.01408  0.03901  -0.04092 203 VAL A N   
1568 C CA  . VAL A 203 ? 0.48398 0.47218 0.33991 0.00438  0.03993  -0.04027 203 VAL A CA  
1569 C C   . VAL A 203 ? 0.48237 0.48303 0.34856 0.00219  0.03913  -0.03815 203 VAL A C   
1570 O O   . VAL A 203 ? 0.43353 0.44733 0.31230 0.00214  0.03872  -0.03810 203 VAL A O   
1571 C CB  . VAL A 203 ? 0.47131 0.45467 0.32303 -0.00431 0.04428  -0.04412 203 VAL A CB  
1572 C CG1 . VAL A 203 ? 0.50842 0.49227 0.35534 -0.01346 0.04749  -0.04506 203 VAL A CG1 
1573 C CG2 . VAL A 203 ? 0.49454 0.45764 0.33099 -0.00497 0.04048  -0.04450 203 VAL A CG2 
1574 N N   . VAL A 204 ? 0.46022 0.45348 0.31888 -0.00068 0.03624  -0.03565 204 VAL A N   
1575 C CA  . VAL A 204 ? 0.45143 0.44840 0.31420 -0.00337 0.03250  -0.03472 204 VAL A CA  
1576 C C   . VAL A 204 ? 0.46227 0.45772 0.32513 -0.00659 0.03714  -0.04398 204 VAL A C   
1577 O O   . VAL A 204 ? 0.50049 0.49314 0.35401 -0.01081 0.04363  -0.04886 204 VAL A O   
1578 C CB  . VAL A 204 ? 0.47956 0.46769 0.33110 -0.00623 0.02698  -0.02931 204 VAL A CB  
1579 C CG1 . VAL A 204 ? 0.46872 0.45384 0.31889 -0.01037 0.02081  -0.02943 204 VAL A CG1 
1580 C CG2 . VAL A 204 ? 0.47596 0.47223 0.33265 0.00000  0.02195  -0.02052 204 VAL A CG2 
1581 N N   . HIS A 205 ? 0.45174 0.45101 0.32557 -0.00477 0.03242  -0.04604 205 HIS A N   
1582 C CA  . HIS A 205 ? 0.47857 0.47963 0.35760 -0.00284 0.03571  -0.05685 205 HIS A CA  
1583 C C   . HIS A 205 ? 0.50982 0.50440 0.39672 0.00018  0.02379  -0.05807 205 HIS A C   
1584 O O   . HIS A 205 ? 0.47954 0.47107 0.36774 -0.00297 0.01308  -0.04780 205 HIS A O   
1585 C CB  . HIS A 205 ? 0.46133 0.47413 0.35153 -0.00240 0.04175  -0.05840 205 HIS A CB  
1586 C CG  . HIS A 205 ? 0.49057 0.50917 0.39342 -0.00180 0.03548  -0.05112 205 HIS A CG  
1587 N ND1 . HIS A 205 ? 0.48696 0.50909 0.38661 -0.00250 0.03480  -0.04316 205 HIS A ND1 
1588 C CD2 . HIS A 205 ? 0.46896 0.49226 0.38687 -0.00094 0.02835  -0.05040 205 HIS A CD2 
1589 C CE1 . HIS A 205 ? 0.53581 0.56895 0.44659 -0.00368 0.02960  -0.03795 205 HIS A CE1 
1590 N NE2 . HIS A 205 ? 0.53352 0.56552 0.45506 -0.00433 0.02460  -0.04081 205 HIS A NE2 
1591 N N   . ALA A 206 ? 0.48558 0.47927 0.37802 0.00621  0.02411  -0.07037 206 ALA A N   
1592 C CA  . ALA A 206 ? 0.53905 0.51859 0.43749 0.01080  0.00874  -0.07343 206 ALA A CA  
1593 C C   . ALA A 206 ? 0.59624 0.58129 0.50910 0.02157  0.00996  -0.08739 206 ALA A C   
1594 O O   . ALA A 206 ? 0.54458 0.54387 0.45580 0.02645  0.02355  -0.09952 206 ALA A O   
1595 C CB  . ALA A 206 ? 0.55321 0.51265 0.43308 0.01031  0.00113  -0.07747 206 ALA A CB  
1596 N N   . GLY A 207 ? 0.65481 0.60564 0.47955 0.00612  0.03056  -0.21505 207 GLY A N   
1597 C CA  . GLY A 207 ? 0.64016 0.59055 0.47065 0.01510  0.04578  -0.22401 207 GLY A CA  
1598 C C   . GLY A 207 ? 0.68846 0.63194 0.48662 0.02204  0.04874  -0.24443 207 GLY A C   
1599 O O   . GLY A 207 ? 0.70536 0.63479 0.48843 0.01967  0.03508  -0.25837 207 GLY A O   
1600 N N   . GLY A 208 ? 0.71609 0.67137 0.50397 0.03049  0.06695  -0.24722 208 GLY A N   
1601 C CA  . GLY A 208 ? 0.75947 0.71078 0.51262 0.03821  0.07257  -0.26616 208 GLY A CA  
1602 C C   . GLY A 208 ? 0.77130 0.70167 0.52847 0.04710  0.07020  -0.28930 208 GLY A C   
1603 O O   . GLY A 208 ? 0.80511 0.72651 0.53221 0.05326  0.07208  -0.30266 208 GLY A O   
1604 N N   . GLY A 209 ? 0.77675 0.69416 0.56836 0.04740  0.06531  -0.28859 209 GLY A N   
1605 C CA  . GLY A 209 ? 0.84473 0.73646 0.63960 0.05658  0.06433  -0.30486 209 GLY A CA  
1606 C C   . GLY A 209 ? 0.84354 0.74566 0.63974 0.07301  0.08346  -0.30708 209 GLY A C   
1607 O O   . GLY A 209 ? 0.83424 0.76065 0.65251 0.07701  0.09545  -0.29676 209 GLY A O   
1608 N N   . ASN A 210 ? 0.92366 0.80906 0.69667 0.08228  0.08646  -0.32091 210 ASN A N   
1609 C CA  . ASN A 210 ? 0.93421 0.82988 0.70653 0.09916  0.10479  -0.32494 210 ASN A CA  
1610 C C   . ASN A 210 ? 0.97770 0.85050 0.71654 0.10608  0.10590  -0.34207 210 ASN A C   
1611 O O   . ASN A 210 ? 1.02271 0.86271 0.76345 0.11062  0.09949  -0.35280 210 ASN A O   
1612 C CB  . ASN A 210 ? 0.91639 0.80652 0.72497 0.10992  0.10777  -0.32190 210 ASN A CB  
1613 C CG  . ASN A 210 ? 0.88505 0.79743 0.70157 0.12738  0.12685  -0.32259 210 ASN A CG  
1614 O OD1 . ASN A 210 ? 0.89191 0.81419 0.68412 0.13313  0.13847  -0.32962 210 ASN A OD1 
1615 N ND2 . ASN A 210 ? 0.79726 0.71854 0.64831 0.13602  0.13002  -0.31504 210 ASN A ND2 
1616 N N   . ARG A 211 ? 1.05983 0.94770 0.76629 0.10647  0.11502  -0.34437 211 ARG A N   
1617 C CA  . ARG A 211 ? 1.10741 0.97471 0.77775 0.11170  0.11670  -0.36105 211 ARG A CA  
1618 C C   . ARG A 211 ? 1.12666 0.99298 0.80092 0.13023  0.13409  -0.37030 211 ARG A C   
1619 O O   . ARG A 211 ? 1.16111 1.00960 0.80597 0.13563  0.13762  -0.38570 211 ARG A O   
1620 C CB  . ARG A 211 ? 1.16213 1.04460 0.79273 0.10555  0.12079  -0.35894 211 ARG A CB  
1621 C CG  . ARG A 211 ? 1.22213 1.11485 0.84813 0.08967  0.10728  -0.34602 211 ARG A CG  
1622 C CD  . ARG A 211 ? 1.28662 1.18667 0.86548 0.08512  0.10992  -0.34425 211 ARG A CD  
1623 N NE  . ARG A 211 ? 1.20571 1.13313 0.77430 0.09063  0.13352  -0.33483 211 ARG A NE  
1624 C CZ  . ARG A 211 ? 1.18221 1.11111 0.73097 0.10107  0.15086  -0.34357 211 ARG A CZ  
1625 N NH1 . ARG A 211 ? 1.20287 1.10611 0.73828 0.10819  0.14792  -0.36294 211 ARG A NH1 
1626 N NH2 . ARG A 211 ? 1.25235 1.20927 0.79511 0.10349  0.17243  -0.33264 211 ARG A NH2 
1627 N N   . THR A 212 ? 1.05233 0.93840 0.76181 0.14028  0.14478  -0.36201 212 THR A N   
1628 C CA  . THR A 212 ? 1.07123 0.96029 0.78664 0.15927  0.16102  -0.37062 212 THR A CA  
1629 C C   . THR A 212 ? 1.12307 0.96738 0.83817 0.16690  0.15230  -0.38549 212 THR A C   
1630 O O   . THR A 212 ? 1.12719 0.94132 0.84642 0.15704  0.13451  -0.38593 212 THR A O   
1631 C CB  . THR A 212 ? 1.01499 0.93987 0.77084 0.16793  0.17280  -0.35745 212 THR A CB  
1632 O OG1 . THR A 212 ? 0.96285 0.87556 0.75036 0.16537  0.15930  -0.34949 212 THR A OG1 
1633 C CG2 . THR A 212 ? 0.92119 0.88959 0.67686 0.15827  0.18353  -0.34285 212 THR A CG2 
1634 N N   . THR A 213 ? 1.15560 0.99539 0.86520 0.18384  0.16590  -0.39790 213 THR A N   
1635 C CA  . THR A 213 ? 1.23513 1.03167 0.94357 0.19279  0.16068  -0.41255 213 THR A CA  
1636 C C   . THR A 213 ? 1.25362 1.05242 0.99901 0.20997  0.16620  -0.40785 213 THR A C   
1637 O O   . THR A 213 ? 1.28100 1.04126 1.03496 0.21237  0.15625  -0.41147 213 THR A O   
1638 C CB  . THR A 213 ? 1.21666 1.00010 0.89079 0.20089  0.17082  -0.43273 213 THR A CB  
1639 O OG1 . THR A 213 ? 1.17123 0.99217 0.85235 0.21656  0.19287  -0.43211 213 THR A OG1 
1640 C CG2 . THR A 213 ? 1.24105 1.01996 0.87554 0.18437  0.16364  -0.43774 213 THR A CG2 
1641 N N   . ALA A 214 ? 1.23047 1.07362 0.99739 0.22126  0.18171  -0.39951 214 ALA A N   
1642 C CA  . ALA A 214 ? 1.18039 1.03548 0.98560 0.23760  0.18601  -0.39272 214 ALA A CA  
1643 C C   . ALA A 214 ? 1.15583 1.05757 0.99010 0.23136  0.18821  -0.37284 214 ALA A C   
1644 O O   . ALA A 214 ? 1.12702 1.04979 0.95052 0.21516  0.18806  -0.36515 214 ALA A O   
1645 C CB  . ALA A 214 ? 1.18890 1.05607 0.99612 0.25978  0.20365  -0.40504 214 ALA A CB  
1646 N N   . GLY A 215 ? 1.16225 1.07925 1.03292 0.24410  0.18969  -0.36464 215 GLY A N   
1647 C CA  . GLY A 215 ? 1.07905 1.04047 0.98080 0.23894  0.19149  -0.34692 215 GLY A CA  
1648 C C   . GLY A 215 ? 0.97565 0.91826 0.89783 0.23299  0.17450  -0.33490 215 GLY A C   
1649 O O   . GLY A 215 ? 0.98639 0.88272 0.89483 0.22663  0.16071  -0.33820 215 GLY A O   
1650 N N   . LYS A 216 ? 0.88691 0.86693 0.84295 0.23434  0.17602  -0.32071 216 LYS A N   
1651 C CA  . LYS A 216 ? 0.94418 0.91249 0.92010 0.22818  0.16143  -0.30777 216 LYS A CA  
1652 C C   . LYS A 216 ? 0.90620 0.87001 0.86888 0.20398  0.15296  -0.30177 216 LYS A C   
1653 O O   . LYS A 216 ? 0.88777 0.87306 0.83383 0.19251  0.16023  -0.30307 216 LYS A O   
1654 C CB  . LYS A 216 ? 0.92618 0.93915 0.94074 0.23536  0.16512  -0.29511 216 LYS A CB  
1655 C CG  . LYS A 216 ? 0.92342 0.93102 0.95861 0.25973  0.16486  -0.29681 216 LYS A CG  
1656 C CD  . LYS A 216 ? 0.91985 0.97788 0.99358 0.26508  0.16709  -0.28457 216 LYS A CD  
1657 C CE  . LYS A 216 ? 0.85058 0.90527 0.94509 0.29059  0.16503  -0.28595 216 LYS A CE  
1658 N NZ  . LYS A 216 ? 0.89100 0.94366 0.97668 0.30813  0.17700  -0.30170 216 LYS A NZ  
1659 N N   . PRO A 217 ? 0.89930 0.83501 0.86853 0.19583  0.13794  -0.29468 217 PRO A N   
1660 C CA  . PRO A 217 ? 0.81793 0.74778 0.77619 0.17315  0.12914  -0.29038 217 PRO A CA  
1661 C C   . PRO A 217 ? 0.79503 0.77285 0.76573 0.16152  0.13621  -0.27960 217 PRO A C   
1662 O O   . PRO A 217 ? 0.76508 0.77821 0.76201 0.16805  0.14343  -0.27141 217 PRO A O   
1663 C CB  . PRO A 217 ? 0.84563 0.74109 0.81669 0.16935  0.11415  -0.28296 217 PRO A CB  
1664 C CG  . PRO A 217 ? 0.90389 0.76994 0.87727 0.18888  0.11378  -0.28757 217 PRO A CG  
1665 C CD  . PRO A 217 ? 0.92787 0.83143 0.91162 0.20689  0.12850  -0.29073 217 PRO A CD  
1666 N N   . ARG A 218 ? 0.77365 0.75178 0.72460 0.14330  0.13357  -0.27947 218 ARG A N   
1667 C CA  . ARG A 218 ? 0.72129 0.73563 0.68060 0.12878  0.13876  -0.26783 218 ARG A CA  
1668 C C   . ARG A 218 ? 0.68731 0.69760 0.67240 0.12085  0.12829  -0.25450 218 ARG A C   
1669 O O   . ARG A 218 ? 0.70573 0.68021 0.68890 0.11587  0.11425  -0.25304 218 ARG A O   
1670 C CB  . ARG A 218 ? 0.74609 0.75723 0.67237 0.11295  0.13790  -0.27055 218 ARG A CB  
1671 C CG  . ARG A 218 ? 0.72414 0.76354 0.65304 0.09553  0.14161  -0.25359 218 ARG A CG  
1672 C CD  . ARG A 218 ? 0.73720 0.77469 0.62783 0.08338  0.14237  -0.25447 218 ARG A CD  
1673 N NE  . ARG A 218 ? 0.75357 0.75609 0.62554 0.07655  0.12463  -0.25946 218 ARG A NE  
1674 C CZ  . ARG A 218 ? 0.75367 0.74383 0.63387 0.06334  0.10970  -0.24589 218 ARG A CZ  
1675 N NH1 . ARG A 218 ? 0.72335 0.72823 0.62755 0.05620  0.10957  -0.22673 218 ARG A NH1 
1676 N NH2 . ARG A 218 ? 0.74324 0.70730 0.60770 0.05711  0.09452  -0.25275 218 ARG A NH2 
1677 N N   . ARG A 219 ? 0.63142 0.67669 0.63913 0.11713  0.13388  -0.23984 219 ARG A N   
1678 C CA  . ARG A 219 ? 0.63896 0.68157 0.67108 0.11190  0.12363  -0.22282 219 ARG A CA  
1679 C C   . ARG A 219 ? 0.55112 0.61248 0.58285 0.09084  0.12297  -0.20522 219 ARG A C   
1680 O O   . ARG A 219 ? 0.55295 0.64606 0.58214 0.08536  0.13498  -0.20294 219 ARG A O   
1681 C CB  . ARG A 219 ? 0.62999 0.69511 0.69206 0.13021  0.12834  -0.22318 219 ARG A CB  
1682 C CG  . ARG A 219 ? 0.60157 0.66702 0.68688 0.12745  0.11834  -0.20680 219 ARG A CG  
1683 C CD  . ARG A 219 ? 0.63277 0.72367 0.74628 0.14834  0.12190  -0.20927 219 ARG A CD  
1684 N NE  . ARG A 219 ? 0.63407 0.69088 0.74828 0.16940  0.11517  -0.21768 219 ARG A NE  
1685 C CZ  . ARG A 219 ? 0.64923 0.71142 0.78440 0.18710  0.11054  -0.21351 219 ARG A CZ  
1686 N NH1 . ARG A 219 ? 0.56068 0.66610 0.72221 0.18772  0.11182  -0.20503 219 ARG A NH1 
1687 N NH2 . ARG A 219 ? 0.71297 0.73423 0.84006 0.20297  0.10355  -0.21608 219 ARG A NH2 
1688 N N   . VAL A 220 ? 0.55128 0.59191 0.58434 0.07885  0.10981  -0.19301 220 VAL A N   
1689 C CA  . VAL A 220 ? 0.50726 0.55964 0.53711 0.06042  0.10786  -0.17727 220 VAL A CA  
1690 C C   . VAL A 220 ? 0.54377 0.58479 0.59062 0.05499  0.09620  -0.16326 220 VAL A C   
1691 O O   . VAL A 220 ? 0.51925 0.53172 0.56746 0.05765  0.08663  -0.16474 220 VAL A O   
1692 C CB  . VAL A 220 ? 0.49925 0.53730 0.49817 0.04902  0.10468  -0.17965 220 VAL A CB  
1693 C CG1 . VAL A 220 ? 0.52542 0.52816 0.51660 0.04906  0.09157  -0.18663 220 VAL A CG1 
1694 C CG2 . VAL A 220 ? 0.49557 0.54222 0.48961 0.03280  0.10231  -0.16327 220 VAL A CG2 
1695 N N   . VAL A 221 ? 0.45347 0.51597 0.51163 0.04615  0.09763  -0.14978 221 VAL A N   
1696 C CA  . VAL A 221 ? 0.45652 0.51076 0.52659 0.03966  0.08761  -0.13616 221 VAL A CA  
1697 C C   . VAL A 221 ? 0.48352 0.53290 0.53781 0.02315  0.08385  -0.12678 221 VAL A C   
1698 O O   . VAL A 221 ? 0.42584 0.49206 0.47130 0.01503  0.09088  -0.12312 221 VAL A O   
1699 C CB  . VAL A 221 ? 0.42731 0.50746 0.52173 0.04320  0.08987  -0.12918 221 VAL A CB  
1700 C CG1 . VAL A 221 ? 0.37381 0.44689 0.47355 0.03344  0.08061  -0.11490 221 VAL A CG1 
1701 C CG2 . VAL A 221 ? 0.45912 0.53789 0.56934 0.06223  0.08913  -0.13647 221 VAL A CG2 
1702 N N   . LEU A 222 ? 0.44112 0.46728 0.49177 0.01845  0.07317  -0.12271 222 LEU A N   
1703 C CA  . LEU A 222 ? 0.45331 0.47374 0.49027 0.00610  0.06779  -0.11484 222 LEU A CA  
1704 C C   . LEU A 222 ? 0.41453 0.43402 0.46471 0.00125  0.06193  -0.10185 222 LEU A C   
1705 O O   . LEU A 222 ? 0.44241 0.45010 0.50442 0.00498  0.05662  -0.10037 222 LEU A O   
1706 C CB  . LEU A 222 ? 0.43641 0.43617 0.45989 0.00434  0.05999  -0.12210 222 LEU A CB  
1707 C CG  . LEU A 222 ? 0.54024 0.53673 0.54596 0.00899  0.06373  -0.13695 222 LEU A CG  
1708 C CD1 . LEU A 222 ? 0.58223 0.55966 0.59451 0.01717  0.06085  -0.14905 222 LEU A CD1 
1709 C CD2 . LEU A 222 ? 0.57365 0.56465 0.55607 0.00145  0.05753  -0.13799 222 LEU A CD2 
1710 N N   . ALA A 223 ? 0.38004 0.40925 0.42557 -0.00720 0.06326  -0.09259 223 ALA A N   
1711 C CA  . ALA A 223 ? 0.39741 0.42379 0.45077 -0.01208 0.05750  -0.08148 223 ALA A CA  
1712 C C   . ALA A 223 ? 0.42899 0.44475 0.46619 -0.01956 0.05195  -0.07611 223 ALA A C   
1713 O O   . ALA A 223 ? 0.42787 0.44588 0.44792 -0.02451 0.05504  -0.07455 223 ALA A O   
1714 C CB  . ALA A 223 ? 0.31369 0.35871 0.37719 -0.01509 0.06236  -0.07578 223 ALA A CB  
1715 C C   . F2Y A 224 ? 0.38415 0.38087 0.41987 -0.02690 0.03596  -0.05790 224 F2Y A C   
1716 O O   . F2Y A 224 ? 0.36511 0.36081 0.41496 -0.02482 0.03441  -0.05543 224 F2Y A O   
1717 C CA  . F2Y A 224 ? 0.38411 0.38128 0.41533 -0.02405 0.03776  -0.06820 224 F2Y A CA  
1718 N N   . F2Y A 224 ? 0.35067 0.35509 0.39294 -0.01969 0.04411  -0.07297 224 F2Y A N   
1719 C CB  . F2Y A 224 ? 0.43125 0.42010 0.46612 -0.02295 0.03057  -0.07328 224 F2Y A CB  
1720 C CG  . F2Y A 224 ? 0.45807 0.44433 0.48600 -0.02101 0.03078  -0.08498 224 F2Y A CG  
1721 C CD1 . F2Y A 224 ? 0.48416 0.47555 0.49569 -0.02018 0.03634  -0.08878 224 F2Y A CD1 
1722 C CE1 . F2Y A 224 ? 0.56028 0.54868 0.56171 -0.01738 0.03691  -0.10112 224 F2Y A CE1 
1723 F F1  . F2Y A 224 ? 0.49716 0.49144 0.48031 -0.01627 0.04383  -0.10496 224 F2Y A F1  
1724 C CD2 . F2Y A 224 ? 0.47939 0.45733 0.51523 -0.02094 0.02629  -0.09277 224 F2Y A CD2 
1725 C CE2 . F2Y A 224 ? 0.48613 0.45901 0.51314 -0.01932 0.02586  -0.10558 224 F2Y A CE2 
1726 F F2  . F2Y A 224 ? 0.54166 0.50359 0.57628 -0.02132 0.02115  -0.11379 224 F2Y A F2  
1727 C CZ  . F2Y A 224 ? 0.55370 0.53187 0.56243 -0.01657 0.03089  -0.11040 224 F2Y A CZ  
1728 O OH  . F2Y A 224 ? 0.59069 0.56300 0.58807 -0.01405 0.03051  -0.12437 224 F2Y A OH  
1729 N N   . PHE A 225 ? 0.38032 0.37542 0.40190 -0.03145 0.03654  -0.05218 225 PHE A N   
1730 C CA  . PHE A 225 ? 0.36910 0.35960 0.39090 -0.03416 0.03423  -0.04410 225 PHE A CA  
1731 C C   . PHE A 225 ? 0.40629 0.38576 0.41792 -0.03217 0.02682  -0.04105 225 PHE A C   
1732 O O   . PHE A 225 ? 0.41337 0.38728 0.40782 -0.03207 0.02455  -0.04092 225 PHE A O   
1733 C CB  . PHE A 225 ? 0.38508 0.37792 0.39839 -0.04152 0.03980  -0.03978 225 PHE A CB  
1734 C CG  . PHE A 225 ? 0.39503 0.40474 0.42431 -0.04304 0.04605  -0.04242 225 PHE A CG  
1735 C CD1 . PHE A 225 ? 0.36047 0.37505 0.40407 -0.04286 0.04382  -0.04016 225 PHE A CD1 
1736 C CD2 . PHE A 225 ? 0.38436 0.40688 0.41387 -0.04349 0.05385  -0.04774 225 PHE A CD2 
1737 C CE1 . PHE A 225 ? 0.35678 0.38998 0.41634 -0.04275 0.04767  -0.04289 225 PHE A CE1 
1738 C CE2 . PHE A 225 ? 0.37365 0.41608 0.42096 -0.04291 0.05932  -0.05099 225 PHE A CE2 
1739 C CZ  . PHE A 225 ? 0.34761 0.39619 0.41079 -0.04241 0.05553  -0.04845 225 PHE A CZ  
1740 N N   . ASN A 226 ? 0.35632 0.33375 0.37781 -0.02948 0.02310  -0.03863 226 ASN A N   
1741 C CA  . ASN A 226 ? 0.33969 0.31202 0.35707 -0.02541 0.01648  -0.03722 226 ASN A CA  
1742 C C   . ASN A 226 ? 0.31364 0.27747 0.32630 -0.02448 0.01522  -0.03112 226 ASN A C   
1743 O O   . ASN A 226 ? 0.32891 0.29294 0.34689 -0.02713 0.01839  -0.02905 226 ASN A O   
1744 C CB  . ASN A 226 ? 0.32036 0.30007 0.35517 -0.02280 0.01420  -0.04144 226 ASN A CB  
1745 C CG  . ASN A 226 ? 0.37201 0.35610 0.40863 -0.02353 0.01261  -0.04915 226 ASN A CG  
1746 O OD1 . ASN A 226 ? 0.42827 0.41063 0.45045 -0.02410 0.01242  -0.05161 226 ASN A OD1 
1747 N ND2 . ASN A 226 ? 0.32135 0.30977 0.37379 -0.02429 0.01167  -0.05323 226 ASN A ND2 
1748 N N   . SER A 227 ? 0.32505 0.28163 0.32779 -0.01929 0.00955  -0.02924 227 SER A N   
1749 C CA  . SER A 227 ? 0.34687 0.29541 0.34749 -0.01517 0.00773  -0.02578 227 SER A CA  
1750 C C   . SER A 227 ? 0.31881 0.27746 0.33798 -0.01437 0.01062  -0.02714 227 SER A C   
1751 O O   . SER A 227 ? 0.28988 0.26065 0.32413 -0.01422 0.01143  -0.03045 227 SER A O   
1752 C CB  . SER A 227 ? 0.34344 0.28819 0.33675 -0.00575 0.00053  -0.02558 227 SER A CB  
1753 O OG  . SER A 227 ? 0.31422 0.25677 0.31134 0.00100  -0.00035 -0.02482 227 SER A OG  
1754 N N   . VAL A 228 ? 0.28954 0.24112 0.30539 -0.01456 0.01213  -0.02453 228 VAL A N   
1755 C CA  . VAL A 228 ? 0.28597 0.24491 0.31402 -0.01290 0.01497  -0.02465 228 VAL A CA  
1756 C C   . VAL A 228 ? 0.30745 0.27422 0.34369 -0.00593 0.01438  -0.02600 228 VAL A C   
1757 O O   . VAL A 228 ? 0.27383 0.24802 0.32010 -0.00543 0.01840  -0.02554 228 VAL A O   
1758 C CB  . VAL A 228 ? 0.31424 0.26373 0.33350 -0.01420 0.01547  -0.02267 228 VAL A CB  
1759 C CG1 . VAL A 228 ? 0.30943 0.25801 0.32634 -0.02252 0.01625  -0.02220 228 VAL A CG1 
1760 C CG2 . VAL A 228 ? 0.29423 0.22797 0.29762 -0.00907 0.01215  -0.02231 228 VAL A CG2 
1761 N N   . GLN A 229 ? 0.28896 0.25557 0.32113 -0.00031 0.00959  -0.02742 229 GLN A N   
1762 C CA  . GLN A 229 ? 0.29174 0.27361 0.33747 0.00596  0.00850  -0.03022 229 GLN A CA  
1763 C C   . GLN A 229 ? 0.29879 0.29682 0.36347 -0.00021 0.01036  -0.03328 229 GLN A C   
1764 O O   . GLN A 229 ? 0.23907 0.25292 0.32014 0.00080  0.01241  -0.03528 229 GLN A O   
1765 C CB  . GLN A 229 ? 0.29294 0.27267 0.33033 0.01466  0.00066  -0.03147 229 GLN A CB  
1766 C CG  . GLN A 229 ? 0.34010 0.29862 0.35677 0.02206  -0.00186 -0.02861 229 GLN A CG  
1767 C CD  . GLN A 229 ? 0.35525 0.30863 0.36126 0.03285  -0.01079 -0.02875 229 GLN A CD  
1768 O OE1 . GLN A 229 ? 0.30185 0.27137 0.31976 0.04337  -0.01437 -0.03214 229 GLN A OE1 
1769 N NE2 . GLN A 229 ? 0.35899 0.29127 0.34265 0.03035  -0.01432 -0.02480 229 GLN A NE2 
1770 N N   . LEU A 230 ? 0.25931 0.25340 0.32203 -0.00691 0.01025  -0.03424 230 LEU A N   
1771 C CA  . LEU A 230 ? 0.29145 0.29497 0.36815 -0.01272 0.01068  -0.03869 230 LEU A CA  
1772 C C   . LEU A 230 ? 0.27794 0.27751 0.36131 -0.01821 0.01748  -0.03663 230 LEU A C   
1773 O O   . LEU A 230 ? 0.24932 0.23966 0.32409 -0.01879 0.01951  -0.03388 230 LEU A O   
1774 C CB  . LEU A 230 ? 0.28319 0.28317 0.35039 -0.01443 0.00610  -0.04248 230 LEU A CB  
1775 C CG  . LEU A 230 ? 0.31818 0.32136 0.37666 -0.00845 -0.00245 -0.04449 230 LEU A CG  
1776 C CD1 . LEU A 230 ? 0.32485 0.32436 0.37096 -0.01079 -0.00610 -0.04840 230 LEU A CD1 
1777 C CD2 . LEU A 230 ? 0.29235 0.31462 0.37004 -0.00613 -0.00618 -0.04873 230 LEU A CD2 
1778 N N   . THR A 231 ? 0.28669 0.29335 0.38541 -0.02247 0.02050  -0.03802 231 THR A N   
1779 C CA  . THR A 231 ? 0.27158 0.27079 0.37420 -0.02640 0.02679  -0.03441 231 THR A CA  
1780 C C   . THR A 231 ? 0.26690 0.25624 0.36618 -0.02837 0.02613  -0.03714 231 THR A C   
1781 O O   . THR A 231 ? 0.29033 0.28115 0.39232 -0.03104 0.02285  -0.04390 231 THR A O   
1782 C CB  . THR A 231 ? 0.26281 0.26932 0.38131 -0.03259 0.03094  -0.03482 231 THR A CB  
1783 O OG1 . THR A 231 ? 0.27562 0.29594 0.39913 -0.02946 0.03293  -0.03316 231 THR A OG1 
1784 C CG2 . THR A 231 ? 0.24137 0.23430 0.35931 -0.03625 0.03741  -0.02932 231 THR A CG2 
1785 N N   . PRO A 232 ? 0.26164 0.24228 0.35524 -0.02615 0.02873  -0.03303 232 PRO A N   
1786 C CA  . PRO A 232 ? 0.31187 0.28609 0.40421 -0.02555 0.02862  -0.03657 232 PRO A CA  
1787 C C   . PRO A 232 ? 0.31836 0.28440 0.41911 -0.02947 0.03017  -0.04014 232 PRO A C   
1788 O O   . PRO A 232 ? 0.32323 0.28369 0.42938 -0.03268 0.03360  -0.03574 232 PRO A O   
1789 C CB  . PRO A 232 ? 0.31976 0.29059 0.40751 -0.02110 0.03015  -0.03093 232 PRO A CB  
1790 C CG  . PRO A 232 ? 0.30148 0.27676 0.38268 -0.02020 0.02931  -0.02635 232 PRO A CG  
1791 C CD  . PRO A 232 ? 0.26768 0.24642 0.35425 -0.02252 0.03048  -0.02633 232 PRO A CD  
1792 N N   . PHE A 233 ? 0.31632 0.28024 0.41633 -0.03005 0.02806  -0.04846 233 PHE A N   
1793 C CA  . PHE A 233 ? 0.35680 0.30824 0.46242 -0.03384 0.02879  -0.05390 233 PHE A CA  
1794 C C   . PHE A 233 ? 0.35567 0.29090 0.46076 -0.02973 0.03266  -0.04841 233 PHE A C   
1795 O O   . PHE A 233 ? 0.38120 0.30311 0.49037 -0.03453 0.03532  -0.04513 233 PHE A O   
1796 C CB  . PHE A 233 ? 0.34719 0.29820 0.44764 -0.03285 0.02580  -0.06501 233 PHE A CB  
1797 C CG  . PHE A 233 ? 0.37787 0.31186 0.48126 -0.03590 0.02590  -0.07303 233 PHE A CG  
1798 C CD1 . PHE A 233 ? 0.39211 0.32367 0.50370 -0.04621 0.02334  -0.07790 233 PHE A CD1 
1799 C CD2 . PHE A 233 ? 0.36254 0.28353 0.46109 -0.02844 0.02823  -0.07687 233 PHE A CD2 
1800 C CE1 . PHE A 233 ? 0.40794 0.31989 0.52087 -0.05085 0.02297  -0.08630 233 PHE A CE1 
1801 C CE2 . PHE A 233 ? 0.39693 0.29714 0.49562 -0.03016 0.02803  -0.08526 233 PHE A CE2 
1802 C CZ  . PHE A 233 ? 0.41729 0.31065 0.52211 -0.04233 0.02530  -0.09000 233 PHE A CZ  
1803 N N   . GLU A 234 ? 0.35783 0.29469 0.45782 -0.02098 0.03292  -0.04676 234 GLU A N   
1804 C CA  . GLU A 234 ? 0.38054 0.30581 0.47917 -0.01356 0.03446  -0.04091 234 GLU A CA  
1805 C C   . GLU A 234 ? 0.36269 0.29502 0.45814 -0.01195 0.03455  -0.03070 234 GLU A C   
1806 O O   . GLU A 234 ? 0.35914 0.30698 0.45255 -0.01149 0.03294  -0.03050 234 GLU A O   
1807 C CB  . GLU A 234 ? 0.38529 0.31439 0.48334 -0.00381 0.03391  -0.04659 234 GLU A CB  
1808 C CG  . GLU A 234 ? 0.44052 0.35878 0.53854 -0.00273 0.03445  -0.05793 234 GLU A CG  
1809 C CD  . GLU A 234 ? 0.47704 0.40710 0.57456 0.00617  0.03577  -0.06614 234 GLU A CD  
1810 O OE1 . GLU A 234 ? 0.44409 0.39473 0.54297 0.00848  0.03646  -0.06360 234 GLU A OE1 
1811 O OE2 . GLU A 234 ? 0.46927 0.38764 0.56500 0.01021  0.03675  -0.07597 234 GLU A OE2 
1812 N N   . THR A 235 ? 0.37007 0.28876 0.46262 -0.01153 0.03658  -0.02232 235 THR A N   
1813 C CA  . THR A 235 ? 0.37473 0.29792 0.46045 -0.00840 0.03633  -0.01324 235 THR A CA  
1814 C C   . THR A 235 ? 0.39563 0.31439 0.47711 0.00306  0.03292  -0.00986 235 THR A C   
1815 O O   . THR A 235 ? 0.40643 0.30662 0.48614 0.00838  0.03315  -0.00802 235 THR A O   
1816 C CB  . THR A 235 ? 0.39668 0.31036 0.47869 -0.01453 0.04136  -0.00516 235 THR A CB  
1817 O OG1 . THR A 235 ? 0.41237 0.32884 0.48367 -0.00973 0.04091  0.00290  235 THR A OG1 
1818 C CG2 . THR A 235 ? 0.37081 0.25971 0.45140 -0.01622 0.04454  -0.00175 235 THR A CG2 
1819 N N   . TYR A 236 ? 0.34349 0.27885 0.42354 0.00702  0.02905  -0.00951 236 TYR A N   
1820 C CA  . TYR A 236 ? 0.35536 0.29528 0.43506 0.01801  0.02395  -0.00791 236 TYR A CA  
1821 C C   . TYR A 236 ? 0.38474 0.31807 0.45201 0.02231  0.02125  0.00207  236 TYR A C   
1822 O O   . TYR A 236 ? 0.37981 0.32169 0.44583 0.03113  0.01477  0.00350  236 TYR A O   
1823 C CB  . TYR A 236 ? 0.35316 0.31773 0.44063 0.01755  0.02116  -0.01475 236 TYR A CB  
1824 C CG  . TYR A 236 ? 0.41879 0.38816 0.51462 0.01514  0.02462  -0.02397 236 TYR A CG  
1825 C CD1 . TYR A 236 ? 0.44465 0.41292 0.54728 0.02441  0.02483  -0.02903 236 TYR A CD1 
1826 C CD2 . TYR A 236 ? 0.42133 0.39471 0.51590 0.00531  0.02733  -0.02767 236 TYR A CD2 
1827 C CE1 . TYR A 236 ? 0.47044 0.44242 0.57741 0.02266  0.02861  -0.03828 236 TYR A CE1 
1828 C CE2 . TYR A 236 ? 0.44751 0.42412 0.54558 0.00380  0.02998  -0.03582 236 TYR A CE2 
1829 C CZ  . TYR A 236 ? 0.45812 0.43427 0.56183 0.01183  0.03119  -0.04167 236 TYR A CZ  
1830 O OH  . TYR A 236 ? 0.52468 0.50375 0.62872 0.01055  0.03439  -0.05062 236 TYR A OH  
1831 N N   . ARG A 237 ? 0.40006 0.31936 0.45804 0.01646  0.02624  0.00877  237 ARG A N   
1832 C CA  . ARG A 237 ? 0.40919 0.32205 0.45108 0.01918  0.02561  0.01839  237 ARG A CA  
1833 C C   . ARG A 237 ? 0.43002 0.32409 0.46110 0.03010  0.02244  0.02686  237 ARG A C   
1834 O O   . ARG A 237 ? 0.45352 0.34293 0.46785 0.03462  0.02010  0.03508  237 ARG A O   
1835 C CB  . ARG A 237 ? 0.42038 0.32655 0.45693 0.00923  0.03431  0.02259  237 ARG A CB  
1836 C CG  . ARG A 237 ? 0.40630 0.29237 0.44510 0.00361  0.04128  0.02609  237 ARG A CG  
1837 C CD  . ARG A 237 ? 0.41117 0.30262 0.45446 -0.00880 0.05001  0.02599  237 ARG A CD  
1838 N NE  . ARG A 237 ? 0.52085 0.40584 0.54840 -0.00996 0.05623  0.03641  237 ARG A NE  
1839 C CZ  . ARG A 237 ? 0.46734 0.36166 0.49691 -0.01827 0.06479  0.03736  237 ARG A CZ  
1840 N NH1 . ARG A 237 ? 0.44684 0.35855 0.49421 -0.02502 0.06627  0.02850  237 ARG A NH1 
1841 N NH2 . ARG A 237 ? 0.49342 0.38070 0.50619 -0.01882 0.07206  0.04739  237 ARG A NH2 
1842 N N   . THR A 238 ? 0.45569 0.33658 0.49305 0.03560  0.02194  0.02512  238 THR A N   
1843 C CA  . THR A 238 ? 0.48573 0.34538 0.51115 0.04876  0.01771  0.03349  238 THR A CA  
1844 C C   . THR A 238 ? 0.48322 0.35986 0.51681 0.06410  0.00735  0.02854  238 THR A C   
1845 O O   . THR A 238 ? 0.52442 0.38557 0.55046 0.07876  0.00190  0.03402  238 THR A O   
1846 C CB  . THR A 238 ? 0.50247 0.33050 0.52664 0.04724  0.02322  0.03541  238 THR A CB  
1847 O OG1 . THR A 238 ? 0.51952 0.35441 0.56103 0.04961  0.02222  0.02282  238 THR A OG1 
1848 C CG2 . THR A 238 ? 0.52627 0.34264 0.54720 0.02968  0.03385  0.03921  238 THR A CG2 
1849 N N   . MET A 239 ? 0.44631 0.35428 0.49554 0.06115  0.00475  0.01846  239 MET A N   
1850 C CA  . MET A 239 ? 0.48722 0.41870 0.54679 0.07350  -0.00467 0.01376  239 MET A CA  
1851 C C   . MET A 239 ? 0.47050 0.40204 0.51449 0.08252  -0.01392 0.02255  239 MET A C   
1852 O O   . MET A 239 ? 0.47126 0.39882 0.49999 0.07463  -0.01261 0.02800  239 MET A O   
1853 C CB  . MET A 239 ? 0.43791 0.40212 0.51405 0.06419  -0.00437 0.00318  239 MET A CB  
1854 C CG  . MET A 239 ? 0.46047 0.42900 0.55100 0.05971  0.00251  -0.00626 239 MET A CG  
1855 S SD  . MET A 239 ? 0.55225 0.55453 0.65632 0.04737  0.00390  -0.01567 239 MET A SD  
1856 C CE  . MET A 239 ? 0.38134 0.41262 0.49530 0.05723  -0.00696 -0.01682 239 MET A CE  
1857 N N   . PRO A 240 ? 0.52194 0.45804 0.56810 0.10035  -0.02373 0.02372  240 PRO A N   
1858 C CA  . PRO A 240 ? 0.51949 0.45873 0.54972 0.11012  -0.03507 0.03129  240 PRO A CA  
1859 C C   . PRO A 240 ? 0.52555 0.49888 0.56309 0.10161  -0.04095 0.02423  240 PRO A C   
1860 O O   . PRO A 240 ? 0.48164 0.48147 0.54141 0.09315  -0.03900 0.01318  240 PRO A O   
1861 C CB  . PRO A 240 ? 0.52713 0.46948 0.56449 0.13271  -0.04526 0.03126  240 PRO A CB  
1862 C CG  . PRO A 240 ? 0.53589 0.46307 0.58510 0.13489  -0.03672 0.02650  240 PRO A CG  
1863 C CD  . PRO A 240 ? 0.46243 0.39910 0.52369 0.11427  -0.02520 0.01808  240 PRO A CD  
1864 N N   . ARG A 241 ? 0.52652 0.49651 0.54247 0.10338  -0.04800 0.03081  241 ARG A N   
1865 C CA  . ARG A 241 ? 0.52928 0.52558 0.54767 0.09422  -0.05420 0.02370  241 ARG A CA  
1866 C C   . ARG A 241 ? 0.52891 0.56416 0.57432 0.09901  -0.06505 0.01303  241 ARG A C   
1867 O O   . ARG A 241 ? 0.52878 0.58796 0.58943 0.08533  -0.06449 0.00323  241 ARG A O   
1868 C CB  . ARG A 241 ? 0.55025 0.53439 0.53728 0.09812  -0.06108 0.03197  241 ARG A CB  
1869 C CG  . ARG A 241 ? 0.56699 0.57221 0.55166 0.08829  -0.06787 0.02378  241 ARG A CG  
1870 C CD  . ARG A 241 ? 0.65174 0.64157 0.60059 0.09316  -0.07354 0.03154  241 ARG A CD  
1871 N NE  . ARG A 241 ? 0.65213 0.65660 0.59528 0.08278  -0.07913 0.02227  241 ARG A NE  
1872 C CZ  . ARG A 241 ? 0.62536 0.61936 0.55857 0.06972  -0.06888 0.01954  241 ARG A CZ  
1873 N NH1 . ARG A 241 ? 0.66134 0.63434 0.59029 0.06503  -0.05271 0.02564  241 ARG A NH1 
1874 N NH2 . ARG A 241 ? 0.58165 0.58691 0.51007 0.06131  -0.07548 0.00962  241 ARG A NH2 
1875 N N   . GLU A 242 ? 0.50470 0.54703 0.55680 0.11835  -0.07473 0.01482  242 GLU A N   
1876 C CA  . GLU A 242 ? 0.54329 0.62882 0.62602 0.12369  -0.08419 0.00381  242 GLU A CA  
1877 C C   . GLU A 242 ? 0.46086 0.56372 0.57158 0.11230  -0.07224 -0.00645 242 GLU A C   
1878 O O   . GLU A 242 ? 0.44118 0.57928 0.57362 0.10168  -0.07396 -0.01657 242 GLU A O   
1879 C CB  . GLU A 242 ? 0.54876 0.63792 0.63546 0.14991  -0.09563 0.00730  242 GLU A CB  
1880 C CG  . GLU A 242 ? 0.70584 0.75975 0.75669 0.16450  -0.10294 0.02213  242 GLU A CG  
1881 C CD  . GLU A 242 ? 0.79933 0.80522 0.83249 0.16837  -0.09036 0.03270  242 GLU A CD  
1882 O OE1 . GLU A 242 ? 0.79824 0.79915 0.84536 0.18175  -0.08859 0.03080  242 GLU A OE1 
1883 O OE2 . GLU A 242 ? 0.72329 0.69738 0.72942 0.15748  -0.08191 0.04194  242 GLU A OE2 
1884 N N   . MET A 243 ? 0.45757 0.53525 0.56665 0.11348  -0.06005 -0.00405 243 MET A N   
1885 C CA  . MET A 243 ? 0.42976 0.52000 0.55943 0.10272  -0.04825 -0.01332 243 MET A CA  
1886 C C   . MET A 243 ? 0.44119 0.53472 0.56793 0.07945  -0.04158 -0.01642 243 MET A C   
1887 O O   . MET A 243 ? 0.43347 0.55350 0.57921 0.06874  -0.03792 -0.02522 243 MET A O   
1888 C CB  . MET A 243 ? 0.46514 0.52350 0.58900 0.10814  -0.03811 -0.01061 243 MET A CB  
1889 C CG  . MET A 243 ? 0.47098 0.54198 0.61346 0.10023  -0.02683 -0.02095 243 MET A CG  
1890 S SD  . MET A 243 ? 0.53932 0.57208 0.67401 0.10683  -0.01709 -0.02036 243 MET A SD  
1891 C CE  . MET A 243 ? 0.43310 0.46834 0.57643 0.13623  -0.02586 -0.02128 243 MET A CE  
1892 N N   . VAL A 244 ? 0.41816 0.48437 0.52048 0.07179  -0.03925 -0.00913 244 VAL A N   
1893 C CA  . VAL A 244 ? 0.42698 0.49357 0.52525 0.05262  -0.03357 -0.01232 244 VAL A CA  
1894 C C   . VAL A 244 ? 0.39732 0.49195 0.50340 0.04496  -0.04249 -0.01877 244 VAL A C   
1895 O O   . VAL A 244 ? 0.37098 0.47846 0.48713 0.03019  -0.03809 -0.02535 244 VAL A O   
1896 C CB  . VAL A 244 ? 0.44111 0.47643 0.51332 0.04832  -0.02915 -0.00420 244 VAL A CB  
1897 C CG1 . VAL A 244 ? 0.38513 0.42147 0.45241 0.03203  -0.02547 -0.00827 244 VAL A CG1 
1898 C CG2 . VAL A 244 ? 0.44451 0.45526 0.51343 0.05040  -0.01912 0.00033  244 VAL A CG2 
1899 N N   . GLU A 245 ? 0.41950 0.52296 0.51994 0.05426  -0.05565 -0.01703 245 GLU A N   
1900 C CA  . GLU A 245 ? 0.41269 0.54133 0.51882 0.04535  -0.06586 -0.02415 245 GLU A CA  
1901 C C   . GLU A 245 ? 0.40074 0.57135 0.54061 0.04404  -0.06946 -0.03362 245 GLU A C   
1902 O O   . GLU A 245 ? 0.38712 0.58179 0.53704 0.03183  -0.07611 -0.04112 245 GLU A O   
1903 C CB  . GLU A 245 ? 0.43145 0.55505 0.51665 0.05560  -0.07992 -0.01967 245 GLU A CB  
1904 C CG  . GLU A 245 ? 0.47390 0.56065 0.52480 0.05322  -0.07478 -0.01175 245 GLU A CG  
1905 C CD  . GLU A 245 ? 0.56096 0.64246 0.58620 0.06218  -0.08796 -0.00781 245 GLU A CD  
1906 O OE1 . GLU A 245 ? 0.58477 0.67911 0.61267 0.07771  -0.10032 -0.00552 245 GLU A OE1 
1907 O OE2 . GLU A 245 ? 0.56131 0.62567 0.56215 0.05498  -0.08626 -0.00733 245 GLU A OE2 
1908 N N   . SER A 246 ? 0.36469 0.54504 0.52262 0.05558  -0.06460 -0.03427 246 SER A N   
1909 C CA  . SER A 246 ? 0.35085 0.57307 0.54248 0.05302  -0.06357 -0.04402 246 SER A CA  
1910 C C   . SER A 246 ? 0.34053 0.56473 0.53969 0.03286  -0.04890 -0.04862 246 SER A C   
1911 O O   . SER A 246 ? 0.32556 0.58534 0.55033 0.02444  -0.04620 -0.05665 246 SER A O   
1912 C CB  . SER A 246 ? 0.35879 0.59018 0.56551 0.07536  -0.06322 -0.04420 246 SER A CB  
1913 O OG  . SER A 246 ? 0.41478 0.62080 0.61574 0.07514  -0.04845 -0.04235 246 SER A OG  
1914 N N   . MET A 247 ? 0.34576 0.53411 0.52318 0.02499  -0.03942 -0.04352 247 MET A N   
1915 C CA  . MET A 247 ? 0.35092 0.53744 0.53106 0.00802  -0.02667 -0.04661 247 MET A CA  
1916 C C   . MET A 247 ? 0.34770 0.53548 0.52193 -0.01236 -0.02897 -0.04905 247 MET A C   
1917 O O   . MET A 247 ? 0.33483 0.51744 0.49772 -0.01351 -0.03958 -0.04834 247 MET A O   
1918 C CB  . MET A 247 ? 0.32693 0.47672 0.48768 0.00928  -0.01711 -0.04094 247 MET A CB  
1919 C CG  . MET A 247 ? 0.35995 0.50135 0.52360 0.02672  -0.01425 -0.03917 247 MET A CG  
1920 S SD  . MET A 247 ? 0.39397 0.49861 0.53941 0.02228  -0.00297 -0.03535 247 MET A SD  
1921 C CE  . MET A 247 ? 0.35340 0.42915 0.47372 0.02077  -0.00821 -0.02644 247 MET A CE  
1922 N N   . THR A 248 ? 0.31402 0.50537 0.49295 -0.02842 -0.01874 -0.05193 248 THR A N   
1923 C CA  . THR A 248 ? 0.31407 0.49691 0.48315 -0.04858 -0.01918 -0.05334 248 THR A CA  
1924 C C   . THR A 248 ? 0.31674 0.45710 0.45561 -0.04914 -0.01760 -0.04742 248 THR A C   
1925 O O   . THR A 248 ? 0.28462 0.40587 0.41354 -0.03752 -0.01363 -0.04243 248 THR A O   
1926 C CB  . THR A 248 ? 0.31058 0.50710 0.49106 -0.06531 -0.00763 -0.05650 248 THR A CB  
1927 O OG1 . THR A 248 ? 0.27637 0.45560 0.44817 -0.06044 0.00395  -0.05291 248 THR A OG1 
1928 C CG2 . THR A 248 ? 0.29775 0.54196 0.51122 -0.06583 -0.00770 -0.06339 248 THR A CG2 
1929 N N   . VAL A 249 ? 0.33344 0.45956 0.45860 -0.06322 -0.02064 -0.04882 249 VAL A N   
1930 C CA  . VAL A 249 ? 0.35761 0.44595 0.45567 -0.06328 -0.01839 -0.04452 249 VAL A CA  
1931 C C   . VAL A 249 ? 0.32670 0.40097 0.42056 -0.06273 -0.00670 -0.04059 249 VAL A C   
1932 O O   . VAL A 249 ? 0.34012 0.39511 0.42222 -0.05275 -0.00414 -0.03622 249 VAL A O   
1933 C CB  . VAL A 249 ? 0.38669 0.46040 0.47108 -0.07896 -0.02263 -0.04817 249 VAL A CB  
1934 C CG1 . VAL A 249 ? 0.37805 0.41398 0.43673 -0.07840 -0.01809 -0.04442 249 VAL A CG1 
1935 C CG2 . VAL A 249 ? 0.39483 0.47632 0.47631 -0.07704 -0.03621 -0.05271 249 VAL A CG2 
1936 N N   . LEU A 250 ? 0.30815 0.39358 0.41152 -0.07403 0.00060  -0.04233 250 LEU A N   
1937 C CA  . LEU A 250 ? 0.30300 0.37680 0.40031 -0.07342 0.01074  -0.03923 250 LEU A CA  
1938 C C   . LEU A 250 ? 0.31122 0.38946 0.41548 -0.05694 0.01297  -0.03808 250 LEU A C   
1939 O O   . LEU A 250 ? 0.33057 0.38893 0.42302 -0.05128 0.01613  -0.03496 250 LEU A O   
1940 C CB  . LEU A 250 ? 0.35218 0.44178 0.45848 -0.08804 0.01895  -0.04122 250 LEU A CB  
1941 C CG  . LEU A 250 ? 0.36830 0.45019 0.46732 -0.08723 0.02952  -0.03876 250 LEU A CG  
1942 C CD1 . LEU A 250 ? 0.34144 0.38706 0.41422 -0.08731 0.02915  -0.03371 250 LEU A CD1 
1943 C CD2 . LEU A 250 ? 0.34548 0.44716 0.45331 -0.10184 0.03905  -0.04050 250 LEU A CD2 
1944 N N   . GLY A 251 ? 0.28834 0.39163 0.41176 -0.04864 0.01044  -0.04098 251 GLY A N   
1945 C CA  . GLY A 251 ? 0.30448 0.40595 0.43207 -0.03269 0.01194  -0.03997 251 GLY A CA  
1946 C C   . GLY A 251 ? 0.30482 0.38078 0.41685 -0.02411 0.00781  -0.03458 251 GLY A C   
1947 O O   . GLY A 251 ? 0.31515 0.37547 0.42132 -0.01864 0.01214  -0.03248 251 GLY A O   
1948 N N   . GLN A 252 ? 0.31952 0.39197 0.42429 -0.02390 -0.00027 -0.03284 252 GLN A N   
1949 C CA  . GLN A 252 ? 0.34880 0.39900 0.43717 -0.01677 -0.00253 -0.02744 252 GLN A CA  
1950 C C   . GLN A 252 ? 0.30611 0.33475 0.38073 -0.02177 0.00339  -0.02549 252 GLN A C   
1951 O O   . GLN A 252 ? 0.30737 0.32214 0.37580 -0.01571 0.00626  -0.02172 252 GLN A O   
1952 C CB  . GLN A 252 ? 0.31242 0.36377 0.39214 -0.01664 -0.01195 -0.02729 252 GLN A CB  
1953 C CG  . GLN A 252 ? 0.31348 0.38704 0.40584 -0.00830 -0.02052 -0.02863 252 GLN A CG  
1954 C CD  . GLN A 252 ? 0.34555 0.42153 0.42731 -0.00879 -0.03170 -0.02971 252 GLN A CD  
1955 O OE1 . GLN A 252 ? 0.38605 0.44732 0.45162 -0.01690 -0.03238 -0.03089 252 GLN A OE1 
1956 N NE2 . GLN A 252 ? 0.31883 0.41243 0.40814 0.00129  -0.04129 -0.02989 252 GLN A NE2 
1957 N N   . ARG A 253 ? 0.32767 0.35345 0.39766 -0.03286 0.00507  -0.02788 253 ARG A N   
1958 C CA  . ARG A 253 ? 0.33609 0.34246 0.39308 -0.03541 0.00924  -0.02623 253 ARG A CA  
1959 C C   . ARG A 253 ? 0.30279 0.30892 0.36518 -0.03223 0.01530  -0.02592 253 ARG A C   
1960 O O   . ARG A 253 ? 0.29737 0.29180 0.35421 -0.02807 0.01709  -0.02397 253 ARG A O   
1961 C CB  . ARG A 253 ? 0.32639 0.32595 0.37477 -0.04737 0.00906  -0.02805 253 ARG A CB  
1962 C CG  . ARG A 253 ? 0.35040 0.34317 0.38897 -0.05100 0.00229  -0.02981 253 ARG A CG  
1963 C CD  . ARG A 253 ? 0.35376 0.33624 0.38353 -0.06507 0.00164  -0.03209 253 ARG A CD  
1964 N NE  . ARG A 253 ? 0.41449 0.37096 0.42649 -0.06439 0.00433  -0.02977 253 ARG A NE  
1965 C CZ  . ARG A 253 ? 0.47431 0.42455 0.48295 -0.06852 0.00956  -0.02730 253 ARG A CZ  
1966 N NH1 . ARG A 253 ? 0.44504 0.41234 0.46545 -0.07600 0.01421  -0.02737 253 ARG A NH1 
1967 N NH2 . ARG A 253 ? 0.44007 0.36739 0.43225 -0.06406 0.01006  -0.02492 253 ARG A NH2 
1968 N N   . MET A 254 ? 0.31793 0.33877 0.39173 -0.03418 0.01854  -0.02884 254 MET A N   
1969 C CA  . MET A 254 ? 0.29454 0.31425 0.37099 -0.03107 0.02375  -0.03033 254 MET A CA  
1970 C C   . MET A 254 ? 0.28130 0.29497 0.36172 -0.02130 0.02324  -0.02915 254 MET A C   
1971 O O   . MET A 254 ? 0.28944 0.29478 0.36773 -0.02004 0.02577  -0.03003 254 MET A O   
1972 C CB  . MET A 254 ? 0.29841 0.33672 0.38579 -0.03330 0.02831  -0.03475 254 MET A CB  
1973 C CG  . MET A 254 ? 0.32154 0.36374 0.40330 -0.04581 0.03169  -0.03503 254 MET A CG  
1974 S SD  . MET A 254 ? 0.32726 0.34494 0.38659 -0.05007 0.03320  -0.03177 254 MET A SD  
1975 C CE  . MET A 254 ? 0.34325 0.34569 0.39082 -0.05683 0.02761  -0.02808 254 MET A CE  
1976 N N   . LEU A 255 ? 0.28332 0.29972 0.36810 -0.01500 0.01953  -0.02694 255 LEU A N   
1977 C CA  . LEU A 255 ? 0.29783 0.30513 0.38456 -0.00644 0.01978  -0.02449 255 LEU A CA  
1978 C C   . LEU A 255 ? 0.29122 0.28428 0.36743 -0.00569 0.01895  -0.01862 255 LEU A C   
1979 O O   . LEU A 255 ? 0.31706 0.30104 0.39221 0.00010  0.01924  -0.01447 255 LEU A O   
1980 C CB  . LEU A 255 ? 0.31730 0.33465 0.41354 0.00259  0.01653  -0.02485 255 LEU A CB  
1981 C CG  . LEU A 255 ? 0.31283 0.34831 0.42261 0.00420  0.01909  -0.03172 255 LEU A CG  
1982 C CD1 . LEU A 255 ? 0.30028 0.34505 0.42061 0.01702  0.01525  -0.03234 255 LEU A CD1 
1983 C CD2 . LEU A 255 ? 0.31261 0.34106 0.42168 0.00245  0.02558  -0.03630 255 LEU A CD2 
1984 N N   . GLY A 256 ? 0.27459 0.26416 0.34185 -0.01104 0.01878  -0.01807 256 GLY A N   
1985 C CA  . GLY A 256 ? 0.30678 0.28587 0.36532 -0.00985 0.02026  -0.01394 256 GLY A CA  
1986 C C   . GLY A 256 ? 0.32815 0.30460 0.37691 -0.00593 0.01719  -0.00975 256 GLY A C   
1987 O O   . GLY A 256 ? 0.32956 0.29816 0.37037 -0.00420 0.02037  -0.00575 256 GLY A O   
1988 N N   . TRP A 257 ? 0.32317 0.30788 0.37196 -0.00482 0.01114  -0.01102 257 TRP A N   
1989 C CA  . TRP A 257 ? 0.34524 0.32821 0.38265 -0.00013 0.00618  -0.00770 257 TRP A CA  
1990 C C   . TRP A 257 ? 0.34909 0.32949 0.37348 -0.00432 0.00305  -0.01071 257 TRP A C   
1991 O O   . TRP A 257 ? 0.35108 0.33041 0.36335 -0.00092 -0.00220 -0.00965 257 TRP A O   
1992 C CB  . TRP A 257 ? 0.32623 0.32194 0.37165 0.00498  -0.00090 -0.00832 257 TRP A CB  
1993 C CG  . TRP A 257 ? 0.37893 0.36908 0.42928 0.01344  0.00110  -0.00371 257 TRP A CG  
1994 C CD1 . TRP A 257 ? 0.36439 0.35677 0.42870 0.01464  0.00469  -0.00631 257 TRP A CD1 
1995 C CD2 . TRP A 257 ? 0.41690 0.39381 0.45482 0.02189  0.00008  0.00448  257 TRP A CD2 
1996 N NE1 . TRP A 257 ? 0.39158 0.37102 0.45391 0.02344  0.00542  -0.00092 257 TRP A NE1 
1997 C CE2 . TRP A 257 ? 0.39097 0.36000 0.43679 0.02764  0.00282  0.00673  257 TRP A CE2 
1998 C CE3 . TRP A 257 ? 0.44296 0.41169 0.46106 0.02518  -0.00245 0.01024  257 TRP A CE3 
1999 C CZ2 . TRP A 257 ? 0.42563 0.37632 0.46016 0.03602  0.00287  0.01569  257 TRP A CZ2 
2000 C CZ3 . TRP A 257 ? 0.52020 0.47323 0.52612 0.03355  -0.00182 0.01977  257 TRP A CZ3 
2001 C CH2 . TRP A 257 ? 0.49133 0.43416 0.50554 0.03858  0.00077  0.02300  257 TRP A CH2 
2002 N N   . ARG A 258 ? 0.30549 0.28240 0.32957 -0.01072 0.00552  -0.01458 258 ARG A N   
2003 C CA  . ARG A 258 ? 0.31739 0.28659 0.32759 -0.01430 0.00243  -0.01829 258 ARG A CA  
2004 C C   . ARG A 258 ? 0.35720 0.31480 0.36118 -0.01371 0.00798  -0.01870 258 ARG A C   
2005 O O   . ARG A 258 ? 0.34305 0.30212 0.35628 -0.01369 0.01268  -0.01754 258 ARG A O   
2006 C CB  . ARG A 258 ? 0.34106 0.31646 0.35592 -0.02365 -0.00272 -0.02348 258 ARG A CB  
2007 C CG  . ARG A 258 ? 0.38121 0.37334 0.40404 -0.02334 -0.00990 -0.02467 258 ARG A CG  
2008 C CD  . ARG A 258 ? 0.39192 0.39334 0.41990 -0.03492 -0.01540 -0.03078 258 ARG A CD  
2009 N NE  . ARG A 258 ? 0.34508 0.36536 0.38029 -0.03239 -0.02434 -0.03268 258 ARG A NE  
2010 C CZ  . ARG A 258 ? 0.40355 0.42566 0.43061 -0.03686 -0.03360 -0.03763 258 ARG A CZ  
2011 N NH1 . ARG A 258 ? 0.41463 0.41909 0.42672 -0.04594 -0.03451 -0.04203 258 ARG A NH1 
2012 N NH2 . ARG A 258 ? 0.37605 0.41678 0.40889 -0.03128 -0.04317 -0.03870 258 ARG A NH2 
2013 N N   . THR A 259 ? 0.33176 0.27833 0.31950 -0.01221 0.00651  -0.02139 259 THR A N   
2014 C CA  . THR A 259 ? 0.38169 0.31760 0.36306 -0.00947 0.01022  -0.02311 259 THR A CA  
2015 C C   . THR A 259 ? 0.37988 0.30914 0.36280 -0.01608 0.00810  -0.02543 259 THR A C   
2016 O O   . THR A 259 ? 0.34534 0.27284 0.32662 -0.02438 0.00355  -0.02768 259 THR A O   
2017 C CB  . THR A 259 ? 0.40662 0.33067 0.36810 -0.00458 0.00902  -0.02671 259 THR A CB  
2018 O OG1 . THR A 259 ? 0.37915 0.30937 0.33689 0.00183  0.01333  -0.02306 259 THR A OG1 
2019 C CG2 . THR A 259 ? 0.38459 0.29593 0.33856 0.00033  0.01137  -0.02998 259 THR A CG2 
2020 N N   . MET A 260 ? 0.35252 0.27918 0.33857 -0.01294 0.01139  -0.02459 260 MET A N   
2021 C CA  . MET A 260 ? 0.34758 0.26654 0.33206 -0.01807 0.00994  -0.02489 260 MET A CA  
2022 C C   . MET A 260 ? 0.40232 0.30470 0.37392 -0.01091 0.00922  -0.02629 260 MET A C   
2023 O O   . MET A 260 ? 0.37396 0.27584 0.34222 -0.00148 0.01096  -0.02785 260 MET A O   
2024 C CB  . MET A 260 ? 0.32803 0.26034 0.32747 -0.01978 0.01272  -0.02267 260 MET A CB  
2025 C CG  . MET A 260 ? 0.33206 0.28017 0.34515 -0.02256 0.01388  -0.02170 260 MET A CG  
2026 S SD  . MET A 260 ? 0.35635 0.30831 0.37016 -0.03336 0.01082  -0.02348 260 MET A SD  
2027 C CE  . MET A 260 ? 0.38179 0.33769 0.40079 -0.03814 0.01470  -0.02307 260 MET A CE  
2028 N N   . LYS A 261 ? 0.41257 0.30145 0.37615 -0.01455 0.00709  -0.02543 261 LYS A N   
2029 C CA  . LYS A 261 ? 0.42686 0.29391 0.37406 -0.00686 0.00453  -0.02633 261 LYS A CA  
2030 C C   . LYS A 261 ? 0.41431 0.28062 0.36191 -0.00414 0.00365  -0.02310 261 LYS A C   
2031 O O   . LYS A 261 ? 0.40878 0.26512 0.34851 -0.01307 0.00289  -0.02009 261 LYS A O   
2032 C CB  . LYS A 261 ? 0.44965 0.28965 0.37706 -0.01428 0.00091  -0.02811 261 LYS A CB  
2033 C CG  . LYS A 261 ? 0.50351 0.31280 0.40955 -0.00554 -0.00243 -0.02898 261 LYS A CG  
2034 C CD  . LYS A 261 ? 0.52693 0.33697 0.43087 0.01142  -0.00191 -0.03375 261 LYS A CD  
2035 C CE  . LYS A 261 ? 0.52436 0.29945 0.40450 0.02158  -0.00606 -0.03628 261 LYS A CE  
2036 N NZ  . LYS A 261 ? 0.57712 0.34249 0.45253 0.02700  -0.00893 -0.03078 261 LYS A NZ  
2037 N N   . PRO A 262 ? 0.39294 0.27036 0.34860 0.00769  0.00361  -0.02379 262 PRO A N   
2038 C CA  . PRO A 262 ? 0.42242 0.29387 0.37209 0.01349  -0.00036 -0.02169 262 PRO A CA  
2039 C C   . PRO A 262 ? 0.47421 0.31239 0.39865 0.01927  -0.00493 -0.02079 262 PRO A C   
2040 O O   . PRO A 262 ? 0.45582 0.27790 0.36997 0.02093  -0.00491 -0.02365 262 PRO A O   
2041 C CB  . PRO A 262 ? 0.40941 0.30454 0.37698 0.02508  -0.00014 -0.02442 262 PRO A CB  
2042 C CG  . PRO A 262 ? 0.37237 0.28517 0.35520 0.02238  0.00623  -0.02649 262 PRO A CG  
2043 C CD  . PRO A 262 ? 0.39068 0.28508 0.35871 0.01697  0.00682  -0.02671 262 PRO A CD  
2044 N N   . SER A 263 ? 0.47487 0.29984 0.38650 0.02265  -0.00937 -0.01685 263 SER A N   
2045 C CA  . SER A 263 ? 0.52350 0.31045 0.40736 0.02802  -0.01405 -0.01440 263 SER A CA  
2046 C C   . SER A 263 ? 0.55494 0.33765 0.43748 0.04797  -0.01726 -0.01925 263 SER A C   
2047 O O   . SER A 263 ? 0.50785 0.32114 0.41220 0.05754  -0.01580 -0.02347 263 SER A O   
2048 C CB  . SER A 263 ? 0.58941 0.36211 0.45656 0.02879  -0.01836 -0.00759 263 SER A CB  
2049 O OG  . SER A 263 ? 0.61536 0.41151 0.49523 0.04261  -0.02287 -0.00901 263 SER A OG  
2050 N N   . ASP A 264 ? 0.56793 0.31165 0.42454 0.05371  -0.02085 -0.01914 264 ASP A N   
2051 C CA  . ASP A 264 ? 0.58335 0.31823 0.43437 0.07656  -0.02484 -0.02376 264 ASP A CA  
2052 C C   . ASP A 264 ? 0.62468 0.38092 0.48663 0.09171  -0.03022 -0.02196 264 ASP A C   
2053 O O   . ASP A 264 ? 0.58886 0.34261 0.44460 0.08588  -0.03367 -0.01541 264 ASP A O   
2054 C CB  . ASP A 264 ? 0.68900 0.37050 0.50537 0.08076  -0.02950 -0.02263 264 ASP A CB  
2055 C CG  . ASP A 264 ? 0.76213 0.42322 0.56832 0.06707  -0.02582 -0.02739 264 ASP A CG  
2056 O OD1 . ASP A 264 ? 0.75220 0.44095 0.57699 0.05496  -0.02026 -0.03070 264 ASP A OD1 
2057 O OD2 . ASP A 264 ? 0.83598 0.45100 0.61381 0.06872  -0.02946 -0.02809 264 ASP A OD2 
2058 N N   . PRO A 265 ? 0.58080 0.36008 0.45891 0.11108  -0.03120 -0.02814 265 PRO A N   
2059 C CA  . PRO A 265 ? 0.55452 0.33456 0.43521 0.12316  -0.02712 -0.03625 265 PRO A CA  
2060 C C   . PRO A 265 ? 0.53698 0.35019 0.44096 0.11274  -0.01687 -0.04067 265 PRO A C   
2061 O O   . PRO A 265 ? 0.50805 0.32921 0.41608 0.12366  -0.01217 -0.04745 265 PRO A O   
2062 C CB  . PRO A 265 ? 0.54564 0.34249 0.43625 0.14920  -0.03277 -0.03984 265 PRO A CB  
2063 C CG  . PRO A 265 ? 0.53619 0.36833 0.44900 0.14392  -0.03574 -0.03648 265 PRO A CG  
2064 C CD  . PRO A 265 ? 0.55636 0.36471 0.45106 0.12380  -0.03724 -0.02800 265 PRO A CD  
2065 N N   . ASN A 266 ? 0.49699 0.32949 0.41513 0.09353  -0.01280 -0.03715 266 ASN A N   
2066 C CA  . ASN A 266 ? 0.49319 0.34354 0.42338 0.08365  -0.00412 -0.03986 266 ASN A CA  
2067 C C   . ASN A 266 ? 0.55880 0.37552 0.46486 0.07564  -0.00422 -0.04112 266 ASN A C   
2068 O O   . ASN A 266 ? 0.59281 0.39353 0.48964 0.05994  -0.00637 -0.03685 266 ASN A O   
2069 C CB  . ASN A 266 ? 0.43981 0.31635 0.39027 0.06740  -0.00076 -0.03587 266 ASN A CB  
2070 C CG  . ASN A 266 ? 0.44440 0.33433 0.40319 0.05813  0.00704  -0.03699 266 ASN A CG  
2071 O OD1 . ASN A 266 ? 0.45949 0.33063 0.40228 0.05450  0.00772  -0.03873 266 ASN A OD1 
2072 N ND2 . ASN A 266 ? 0.39416 0.31491 0.37636 0.05411  0.01228  -0.03604 266 ASN A ND2 
2073 N N   . ILE A 267 ? 0.53779 0.34545 0.43404 0.08554  -0.00165 -0.04786 267 ILE A N   
2074 C CA  . ILE A 267 ? 0.62318 0.39659 0.49463 0.07806  -0.00357 -0.05102 267 ILE A CA  
2075 C C   . ILE A 267 ? 0.56952 0.35767 0.44531 0.06769  0.00167  -0.05379 267 ILE A C   
2076 O O   . ILE A 267 ? 0.59357 0.35758 0.45030 0.06063  -0.00095 -0.05791 267 ILE A O   
2077 C CB  . ILE A 267 ? 0.67472 0.41567 0.52279 0.09618  -0.00661 -0.05807 267 ILE A CB  
2078 C CG1 . ILE A 267 ? 0.64826 0.41485 0.50733 0.11513  0.00012  -0.06517 267 ILE A CG1 
2079 C CG2 . ILE A 267 ? 0.67679 0.38999 0.51150 0.10486  -0.01441 -0.05368 267 ILE A CG2 
2080 C CD1 . ILE A 267 ? 0.78937 0.52397 0.62322 0.13229  -0.00117 -0.07481 267 ILE A CD1 
2081 N N   . VAL A 268 ? 0.48238 0.30735 0.38101 0.06592  0.00816  -0.05151 268 VAL A N   
2082 C CA  . VAL A 268 ? 0.48378 0.32157 0.38406 0.05791  0.01265  -0.05235 268 VAL A CA  
2083 C C   . VAL A 268 ? 0.50185 0.35364 0.41594 0.04072  0.01184  -0.04577 268 VAL A C   
2084 O O   . VAL A 268 ? 0.47427 0.32277 0.38219 0.03064  0.01000  -0.04624 268 VAL A O   
2085 C CB  . VAL A 268 ? 0.52208 0.38749 0.43413 0.06893  0.02218  -0.05405 268 VAL A CB  
2086 C CG1 . VAL A 268 ? 0.48536 0.36027 0.39384 0.06123  0.02665  -0.05317 268 VAL A CG1 
2087 C CG2 . VAL A 268 ? 0.55453 0.40911 0.45404 0.08791  0.02382  -0.06198 268 VAL A CG2 
2088 N N   . GLY A 269 ? 0.43319 0.30196 0.36612 0.03844  0.01266  -0.04058 269 GLY A N   
2089 C CA  . GLY A 269 ? 0.34963 0.23368 0.29695 0.02534  0.01323  -0.03550 269 GLY A CA  
2090 C C   . GLY A 269 ? 0.37383 0.28606 0.34316 0.02746  0.01936  -0.03267 269 GLY A C   
2091 O O   . GLY A 269 ? 0.37150 0.29498 0.34853 0.03757  0.02269  -0.03436 269 GLY A O   
2092 N N   . ILE A 270 ? 0.37790 0.30183 0.35812 0.01779  0.02086  -0.02883 270 ILE A N   
2093 C CA  . ILE A 270 ? 0.37084 0.31623 0.37078 0.01651  0.02631  -0.02580 270 ILE A CA  
2094 C C   . ILE A 270 ? 0.36398 0.31244 0.36552 0.00909  0.02763  -0.02214 270 ILE A C   
2095 O O   . ILE A 270 ? 0.37696 0.31668 0.37053 0.00398  0.02276  -0.02235 270 ILE A O   
2096 C CB  . ILE A 270 ? 0.33046 0.28251 0.34307 0.01441  0.02351  -0.02549 270 ILE A CB  
2097 C CG1 . ILE A 270 ? 0.34746 0.32100 0.38023 0.01537  0.02848  -0.02525 270 ILE A CG1 
2098 C CG2 . ILE A 270 ? 0.30271 0.25175 0.31704 0.00429  0.02058  -0.02342 270 ILE A CG2 
2099 C CD1 . ILE A 270 ? 0.36847 0.34919 0.41087 0.01639  0.02363  -0.02731 270 ILE A CD1 
2100 N N   . ASN A 271 ? 0.33685 0.29770 0.34851 0.00865  0.03415  -0.01865 271 ASN A N   
2101 C CA  . ASN A 271 ? 0.35895 0.32011 0.37045 0.00414  0.03507  -0.01391 271 ASN A CA  
2102 C C   . ASN A 271 ? 0.37739 0.32996 0.36933 0.00704  0.03324  -0.01399 271 ASN A C   
2103 O O   . ASN A 271 ? 0.37150 0.31987 0.35807 0.00403  0.02707  -0.01373 271 ASN A O   
2104 C CB  . ASN A 271 ? 0.34597 0.30668 0.36544 -0.00197 0.02983  -0.01367 271 ASN A CB  
2105 C CG  . ASN A 271 ? 0.37715 0.34014 0.40229 -0.00410 0.03124  -0.00890 271 ASN A CG  
2106 O OD1 . ASN A 271 ? 0.36227 0.32731 0.39193 -0.00405 0.03736  -0.00483 271 ASN A OD1 
2107 N ND2 . ASN A 271 ? 0.32772 0.29023 0.35330 -0.00609 0.02574  -0.00939 271 ASN A ND2 
2108 N N   . LEU A 272 ? 0.38486 0.33688 0.36639 0.01342  0.03837  -0.01545 272 LEU A N   
2109 C CA  . LEU A 272 ? 0.42722 0.37101 0.38685 0.01718  0.03740  -0.01648 272 LEU A CA  
2110 C C   . LEU A 272 ? 0.39263 0.34328 0.34747 0.02048  0.04796  -0.01127 272 LEU A C   
2111 O O   . LEU A 272 ? 0.36960 0.33160 0.34005 0.01863  0.05631  -0.00748 272 LEU A O   
2112 C CB  . LEU A 272 ? 0.41483 0.34665 0.35953 0.02268  0.03403  -0.02479 272 LEU A CB  
2113 C CG  . LEU A 272 ? 0.46543 0.40259 0.41785 0.03007  0.03989  -0.02797 272 LEU A CG  
2114 C CD1 . LEU A 272 ? 0.52079 0.45453 0.45564 0.04045  0.04543  -0.03291 272 LEU A CD1 
2115 C CD2 . LEU A 272 ? 0.42999 0.35740 0.38612 0.02981  0.03273  -0.03178 272 LEU A CD2 
2116 N N   . ILE A 273 ? 0.40951 0.35306 0.34138 0.02427  0.04757  -0.01112 273 ILE A N   
2117 C CA  . ILE A 273 ? 0.43162 0.37909 0.35264 0.02705  0.05835  -0.00500 273 ILE A CA  
2118 C C   . ILE A 273 ? 0.45737 0.39567 0.34856 0.03432  0.05708  -0.01014 273 ILE A C   
2119 O O   . ILE A 273 ? 0.44320 0.37078 0.32176 0.03430  0.04513  -0.01553 273 ILE A O   
2120 C CB  . ILE A 273 ? 0.44397 0.38975 0.36623 0.02217  0.05846  0.00582  273 ILE A CB  
2121 C CG1 . ILE A 273 ? 0.53851 0.48574 0.44834 0.02319  0.07202  0.01424  273 ILE A CG1 
2122 C CG2 . ILE A 273 ? 0.48662 0.42316 0.39366 0.02343  0.04556  0.00560  273 ILE A CG2 
2123 C CD1 . ILE A 273 ? 0.48827 0.45062 0.41887 0.01954  0.08605  0.01501  273 ILE A CD1 
2124 N N   . ASP A 274 ? 0.42579 0.36958 0.30604 0.03987  0.06990  -0.00932 274 ASP A N   
2125 C CA  . ASP A 274 ? 0.49684 0.43223 0.34543 0.04813  0.07101  -0.01494 274 ASP A CA  
2126 C C   . ASP A 274 ? 0.48967 0.41347 0.33122 0.05324  0.06193  -0.02852 274 ASP A C   
2127 O O   . ASP A 274 ? 0.52075 0.43053 0.33562 0.05680  0.05486  -0.03533 274 ASP A O   
2128 C CB  . ASP A 274 ? 0.55152 0.47689 0.37513 0.04721  0.06401  -0.00930 274 ASP A CB  
2129 C CG  . ASP A 274 ? 0.58180 0.51152 0.40602 0.04340  0.07322  0.00555  274 ASP A CG  
2130 O OD1 . ASP A 274 ? 0.59967 0.53994 0.43173 0.04241  0.08948  0.01015  274 ASP A OD1 
2131 O OD2 . ASP A 274 ? 0.61822 0.54063 0.43537 0.04139  0.06420  0.01262  274 ASP A OD2 
2132 N N   . ASP A 275 ? 0.38274 0.41055 0.42188 0.09126  0.01030  -0.03715 275 ASP A N   
2133 C CA  . ASP A 275 ? 0.39481 0.40291 0.45947 0.09035  0.01331  -0.04477 275 ASP A CA  
2134 C C   . ASP A 275 ? 0.39912 0.40146 0.46726 0.07959  0.00588  -0.05724 275 ASP A C   
2135 O O   . ASP A 275 ? 0.41920 0.40509 0.50423 0.07582  0.01157  -0.07442 275 ASP A O   
2136 C CB  . ASP A 275 ? 0.42066 0.42007 0.49010 0.09778  0.02463  -0.06162 275 ASP A CB  
2137 C CG  . ASP A 275 ? 0.49571 0.46963 0.59229 0.10136  0.03473  -0.06154 275 ASP A CG  
2138 O OD1 . ASP A 275 ? 0.49729 0.46213 0.60777 0.10162  0.03376  -0.04398 275 ASP A OD1 
2139 O OD2 . ASP A 275 ? 0.46435 0.42472 0.56617 0.10539  0.04567  -0.07848 275 ASP A OD2 
2140 N N   . LYS A 276 ? 0.38233 0.39844 0.43623 0.07414  -0.00489 -0.04977 276 LYS A N   
2141 C CA  . LYS A 276 ? 0.38352 0.40162 0.44269 0.06414  -0.01302 -0.06127 276 LYS A CA  
2142 C C   . LYS A 276 ? 0.38084 0.39655 0.44445 0.05908  -0.01850 -0.03841 276 LYS A C   
2143 O O   . LYS A 276 ? 0.35341 0.37199 0.40848 0.06299  -0.01848 -0.01598 276 LYS A O   
2144 C CB  . LYS A 276 ? 0.39237 0.43601 0.42525 0.06574  -0.02223 -0.07909 276 LYS A CB  
2145 C CG  . LYS A 276 ? 0.44318 0.49157 0.46730 0.07164  -0.01784 -0.10452 276 LYS A CG  
2146 C CD  . LYS A 276 ? 0.56157 0.63691 0.56920 0.07216  -0.02891 -0.13072 276 LYS A CD  
2147 C CE  . LYS A 276 ? 0.55141 0.64875 0.52433 0.08153  -0.03776 -0.11559 276 LYS A CE  
2148 N NZ  . LYS A 276 ? 0.60599 0.73601 0.56788 0.08338  -0.05208 -0.13838 276 LYS A NZ  
2149 N N   . ARG A 277 ? 0.36646 0.37854 0.44458 0.04923  -0.02231 -0.04689 277 ARG A N   
2150 C CA  . ARG A 277 ? 0.35711 0.36740 0.43758 0.04413  -0.02754 -0.02738 277 ARG A CA  
2151 C C   . ARG A 277 ? 0.37106 0.40532 0.42208 0.04667  -0.03761 -0.01918 277 ARG A C   
2152 O O   . ARG A 277 ? 0.33756 0.39277 0.37175 0.04948  -0.04363 -0.03596 277 ARG A O   
2153 C CB  . ARG A 277 ? 0.36101 0.36184 0.46670 0.03224  -0.02632 -0.04112 277 ARG A CB  
2154 C CG  . ARG A 277 ? 0.40486 0.37285 0.53869 0.03014  -0.01029 -0.04666 277 ARG A CG  
2155 C CD  . ARG A 277 ? 0.46303 0.41871 0.62354 0.01600  -0.00450 -0.06056 277 ARG A CD  
2156 N NE  . ARG A 277 ? 0.57205 0.49303 0.75797 0.01329  0.01609  -0.07268 277 ARG A NE  
2157 C CZ  . ARG A 277 ? 0.66649 0.55122 0.86064 0.02169  0.03171  -0.05068 277 ARG A CZ  
2158 N NH1 . ARG A 277 ? 0.62661 0.50932 0.80774 0.03209  0.02663  -0.01780 277 ARG A NH1 
2159 N NH2 . ARG A 277 ? 0.63597 0.48568 0.85024 0.02122  0.05421  -0.06244 277 ARG A NH2 
2160 N N   . LEU A 278 ? 0.35387 0.38471 0.39700 0.04728  -0.03814 0.00665  278 LEU A N   
2161 C CA  . LEU A 278 ? 0.36204 0.40829 0.37573 0.05035  -0.04244 0.01772  278 LEU A CA  
2162 C C   . LEU A 278 ? 0.36988 0.43296 0.37653 0.04878  -0.05174 0.00638  278 LEU A C   
2163 O O   . LEU A 278 ? 0.38404 0.46558 0.36208 0.05776  -0.05457 0.00210  278 LEU A O   
2164 C CB  . LEU A 278 ? 0.32373 0.36121 0.33602 0.04766  -0.04050 0.04379  278 LEU A CB  
2165 C CG  . LEU A 278 ? 0.35394 0.39976 0.33729 0.04912  -0.04061 0.05756  278 LEU A CG  
2166 C CD1 . LEU A 278 ? 0.31773 0.37159 0.27319 0.05765  -0.03250 0.05508  278 LEU A CD1 
2167 C CD2 . LEU A 278 ? 0.32516 0.36121 0.31238 0.04387  -0.03813 0.07914  278 LEU A CD2 
2168 N N   . GLU A 279 ? 0.33522 0.39348 0.36760 0.03914  -0.05518 0.00093  279 GLU A N   
2169 C CA  . GLU A 279 ? 0.36140 0.44256 0.39367 0.03685  -0.06468 -0.01309 279 GLU A CA  
2170 C C   . GLU A 279 ? 0.37950 0.48609 0.40813 0.04108  -0.07013 -0.04519 279 GLU A C   
2171 O O   . GLU A 279 ? 0.40256 0.54036 0.41580 0.04754  -0.08009 -0.05588 279 GLU A O   
2172 C CB  . GLU A 279 ? 0.31393 0.38286 0.38029 0.02346  -0.06349 -0.01480 279 GLU A CB  
2173 C CG  . GLU A 279 ? 0.34158 0.38908 0.44156 0.01473  -0.05369 -0.03165 279 GLU A CG  
2174 C CD  . GLU A 279 ? 0.33024 0.34264 0.43718 0.01713  -0.04220 -0.00895 279 GLU A CD  
2175 O OE1 . GLU A 279 ? 0.33732 0.34858 0.42333 0.02567  -0.04302 0.01219  279 GLU A OE1 
2176 O OE2 . GLU A 279 ? 0.38806 0.37477 0.52201 0.01137  -0.03075 -0.01348 279 GLU A OE2 
2177 N N   . ASN A 280 ? 0.37290 0.46904 0.41319 0.03974  -0.06382 -0.06110 280 ASN A N   
2178 C CA  . ASN A 280 ? 0.37124 0.49166 0.40560 0.04404  -0.06858 -0.09335 280 ASN A CA  
2179 C C   . ASN A 280 ? 0.38755 0.52274 0.37783 0.06255  -0.07009 -0.08731 280 ASN A C   
2180 O O   . ASN A 280 ? 0.40976 0.57620 0.38007 0.07276  -0.07863 -0.10709 280 ASN A O   
2181 C CB  . ASN A 280 ? 0.37735 0.47693 0.43905 0.03596  -0.05822 -0.11268 280 ASN A CB  
2182 C CG  . ASN A 280 ? 0.41251 0.50011 0.51636 0.01829  -0.05326 -0.12834 280 ASN A CG  
2183 O OD1 . ASN A 280 ? 0.43952 0.54547 0.55395 0.01123  -0.06079 -0.13430 280 ASN A OD1 
2184 N ND2 . ASN A 280 ? 0.41008 0.46558 0.53824 0.01191  -0.03802 -0.13477 280 ASN A ND2 
2185 N N   . VAL A 281 ? 0.42079 0.53508 0.39557 0.06792  -0.06044 -0.06146 281 VAL A N   
2186 C CA  . VAL A 281 ? 0.40676 0.52862 0.33945 0.08455  -0.05622 -0.05206 281 VAL A CA  
2187 C C   . VAL A 281 ? 0.45646 0.59654 0.36014 0.09447  -0.06216 -0.04060 281 VAL A C   
2188 O O   . VAL A 281 ? 0.44948 0.60841 0.31646 0.11251  -0.06313 -0.04547 281 VAL A O   
2189 C CB  . VAL A 281 ? 0.46174 0.55877 0.39254 0.08394  -0.04226 -0.02904 281 VAL A CB  
2190 C CG1 . VAL A 281 ? 0.46850 0.56782 0.35747 0.09855  -0.03241 -0.01691 281 VAL A CG1 
2191 C CG2 . VAL A 281 ? 0.41540 0.49957 0.36928 0.08031  -0.03599 -0.04137 281 VAL A CG2 
2192 N N   . LEU A 282 ? 0.38739 0.52148 0.30487 0.08531  -0.06511 -0.02453 282 LEU A N   
2193 C CA  . LEU A 282 ? 0.45573 0.60422 0.34693 0.09521  -0.06889 -0.01107 282 LEU A CA  
2194 C C   . LEU A 282 ? 0.43987 0.62463 0.33816 0.09826  -0.08477 -0.03360 282 LEU A C   
2195 O O   . LEU A 282 ? 0.43991 0.64317 0.31355 0.11132  -0.08895 -0.02446 282 LEU A O   
2196 C CB  . LEU A 282 ? 0.41553 0.54266 0.31686 0.08453  -0.06443 0.01575  282 LEU A CB  
2197 C CG  . LEU A 282 ? 0.41903 0.51884 0.31057 0.08212  -0.04926 0.03878  282 LEU A CG  
2198 C CD1 . LEU A 282 ? 0.46574 0.55011 0.37265 0.07012  -0.04853 0.05851  282 LEU A CD1 
2199 C CD2 . LEU A 282 ? 0.48847 0.58818 0.33461 0.09865  -0.03723 0.05025  282 LEU A CD2 
2200 N N   . GLN A 283 ? 0.41735 0.61366 0.34976 0.08671  -0.09205 -0.06378 283 GLN A N   
2201 C CA  . GLN A 283 ? 0.42639 0.66345 0.37410 0.08582  -0.10684 -0.09230 283 GLN A CA  
2202 C C   . GLN A 283 ? 0.42801 0.66963 0.38831 0.07998  -0.11100 -0.07742 283 GLN A C   
2203 O O   . GLN A 283 ? 0.37393 0.65261 0.32121 0.09196  -0.12165 -0.08271 283 GLN A O   
2204 C CB  . GLN A 283 ? 0.45872 0.73654 0.36675 0.11062  -0.11577 -0.10815 283 GLN A CB  
2205 C CG  . GLN A 283 ? 0.49240 0.76935 0.39125 0.11540  -0.11250 -0.12932 283 GLN A CG  
2206 C CD  . GLN A 283 ? 0.63848 0.94827 0.48531 0.14597  -0.11765 -0.13614 283 GLN A CD  
2207 O OE1 . GLN A 283 ? 0.61345 0.95661 0.45923 0.15188  -0.12746 -0.17050 283 GLN A OE1 
2208 N NE2 . GLN A 283 ? 0.73058 1.02674 0.53584 0.16513  -0.10728 -0.10257 283 GLN A NE2 
2209 N N   . LEU A 284 ? 0.37812 0.58204 0.36187 0.06374  -0.10191 -0.05741 284 LEU A N   
2210 C CA  . LEU A 284 ? 0.41696 0.61485 0.40973 0.05784  -0.10224 -0.03756 284 LEU A CA  
2211 C C   . LEU A 284 ? 0.39599 0.61681 0.43038 0.04390  -0.10967 -0.06324 284 LEU A C   
2212 O O   . LEU A 284 ? 0.38876 0.59371 0.46154 0.02626  -0.10398 -0.08037 284 LEU A O   
2213 C CB  . LEU A 284 ? 0.43100 0.58273 0.43376 0.04677  -0.08996 -0.01065 284 LEU A CB  
2214 C CG  . LEU A 284 ? 0.50196 0.63849 0.48643 0.04931  -0.08575 0.02233  284 LEU A CG  
2215 C CD1 . LEU A 284 ? 0.49432 0.64130 0.43084 0.06885  -0.08358 0.03532  284 LEU A CD1 
2216 C CD2 . LEU A 284 ? 0.42393 0.52174 0.41994 0.03943  -0.07545 0.04190  284 LEU A CD2 
2217 N N   . LYS A 285 ? 0.40242 0.65982 0.43015 0.05227  -0.11991 -0.06616 285 LYS A N   
2218 C CA  . LYS A 285 ? 0.39206 0.66895 0.46235 0.03714  -0.12420 -0.08405 285 LYS A CA  
2219 C C   . LYS A 285 ? 0.36480 0.60033 0.45045 0.02437  -0.11318 -0.05449 285 LYS A C   
2220 O O   . LYS A 285 ? 0.38040 0.58413 0.43805 0.03075  -0.10634 -0.02022 285 LYS A O   
2221 C CB  . LYS A 285 ? 0.37734 0.71223 0.43476 0.05350  -0.13938 -0.09538 285 LYS A CB  
2222 C CG  . LYS A 285 ? 0.43259 0.81796 0.47081 0.07098  -0.15276 -0.12618 285 LYS A CG  
2223 C CD  . LYS A 285 ? 0.46398 0.87656 0.47961 0.08932  -0.15321 -0.12137 285 LYS A CD  
2224 C CE  . LYS A 285 ? 0.50952 0.96237 0.51540 0.10322  -0.15823 -0.15233 285 LYS A CE  
2225 N NZ  . LYS A 285 ? 0.58726 1.07197 0.57667 0.12325  -0.15858 -0.14955 285 LYS A NZ  
2226 N N   . ALA A 286 ? 0.36213 0.59895 0.49329 0.00582  -0.11002 -0.06992 286 ALA A N   
2227 C CA  . ALA A 286 ? 0.37817 0.58006 0.52373 -0.00441 -0.09954 -0.04398 286 ALA A CA  
2228 C C   . ALA A 286 ? 0.39790 0.62928 0.58191 -0.01567 -0.10179 -0.06389 286 ALA A C   
2229 O O   . ALA A 286 ? 0.35446 0.62722 0.56637 -0.02212 -0.10843 -0.10332 286 ALA A O   
2230 C CB  . ALA A 286 ? 0.37917 0.52660 0.54357 -0.01759 -0.08295 -0.03462 286 ALA A CB  
2231 N N   . ALA A 287 ? 0.38387 0.59551 0.57090 -0.01873 -0.09552 -0.03819 287 ALA A N   
2232 C CA  . ALA A 287 ? 0.37065 0.61157 0.59338 -0.02820 -0.09650 -0.05394 287 ALA A CA  
2233 C C   . ALA A 287 ? 0.33989 0.57888 0.61958 -0.05237 -0.08535 -0.09013 287 ALA A C   
2234 O O   . ALA A 287 ? 0.33909 0.62397 0.65490 -0.06134 -0.08988 -0.12243 287 ALA A O   
2235 C CB  . ALA A 287 ? 0.32631 0.53567 0.54267 -0.02869 -0.08763 -0.01788 287 ALA A CB  
2236 N N   . ASP A 288 ? 0.39654 0.58437 0.68608 -0.06261 -0.06903 -0.08678 288 ASP A N   
2237 C CA  . ASP A 288 ? 0.42895 0.59733 0.77074 -0.08587 -0.04966 -0.11464 288 ASP A CA  
2238 C C   . ASP A 288 ? 0.44697 0.60485 0.79374 -0.08994 -0.04488 -0.13833 288 ASP A C   
2239 O O   . ASP A 288 ? 0.48458 0.59395 0.85355 -0.10179 -0.02210 -0.14048 288 ASP A O   
2240 C CB  . ASP A 288 ? 0.39250 0.49734 0.74301 -0.09266 -0.02658 -0.08389 288 ASP A CB  
2241 C CG  . ASP A 288 ? 0.39014 0.44844 0.69891 -0.07783 -0.02392 -0.04521 288 ASP A CG  
2242 O OD1 . ASP A 288 ? 0.40095 0.47876 0.67068 -0.06215 -0.04119 -0.03484 288 ASP A OD1 
2243 O OD2 . ASP A 288 ? 0.42575 0.42984 0.74039 -0.08055 -0.00363 -0.02622 288 ASP A OD2 
2244 N N   . SER A 289 ? 0.60902 0.80922 0.93268 -0.07812 -0.06407 -0.15514 289 SER A N   
2245 C CA  . SER A 289 ? 0.65284 0.84759 0.98291 -0.08258 -0.05969 -0.18199 289 SER A CA  
2246 C C   . SER A 289 ? 0.70387 0.96834 1.03906 -0.08071 -0.07874 -0.22660 289 SER A C   
2247 O O   . SER A 289 ? 0.70243 1.02195 1.02957 -0.07092 -0.09741 -0.23261 289 SER A O   
2248 C CB  . SER A 289 ? 0.63567 0.79564 0.92103 -0.06548 -0.06025 -0.15002 289 SER A CB  
2249 O OG  . SER A 289 ? 0.64746 0.84232 0.88779 -0.04434 -0.08101 -0.13658 289 SER A OG  
2250 N N   . LYS B 6   ? 0.49524 0.83228 0.81349 0.21808  -0.11598 0.00990  6   LYS B N   
2251 C CA  . LYS B 6   ? 0.57360 0.87852 0.86097 0.18476  -0.11348 0.01737  6   LYS B CA  
2252 C C   . LYS B 6   ? 0.57061 0.89890 0.84222 0.15769  -0.09082 0.00542  6   LYS B C   
2253 O O   . LYS B 6   ? 0.57091 0.91014 0.84509 0.16495  -0.07453 -0.01125 6   LYS B O   
2254 C CB  . LYS B 6   ? 0.59209 0.82724 0.86202 0.19131  -0.11828 0.01369  6   LYS B CB  
2255 C CG  . LYS B 6   ? 0.63992 0.83615 0.91969 0.20619  -0.14595 0.03218  6   LYS B CG  
2256 C CD  . LYS B 6   ? 0.60688 0.73903 0.86347 0.19499  -0.15177 0.03638  6   LYS B CD  
2257 C CE  . LYS B 6   ? 0.58259 0.72235 0.81423 0.15736  -0.14587 0.05049  6   LYS B CE  
2258 N NZ  . LYS B 6   ? 0.64624 0.81775 0.88414 0.14417  -0.16164 0.07790  6   LYS B NZ  
2259 N N   . PRO B 7   ? 0.48735 0.82420 0.74299 0.12693  -0.09088 0.01382  7   PRO B N   
2260 C CA  . PRO B 7   ? 0.43348 0.77755 0.67294 0.10135  -0.07271 0.00128  7   PRO B CA  
2261 C C   . PRO B 7   ? 0.43682 0.73240 0.65718 0.10281  -0.06056 -0.01101 7   PRO B C   
2262 O O   . PRO B 7   ? 0.41130 0.66221 0.61772 0.10626  -0.06744 -0.00647 7   PRO B O   
2263 C CB  . PRO B 7   ? 0.39611 0.74753 0.61928 0.07432  -0.07966 0.01038  7   PRO B CB  
2264 C CG  . PRO B 7   ? 0.41664 0.79480 0.65597 0.08326  -0.09917 0.02937  7   PRO B CG  
2265 C CD  . PRO B 7   ? 0.45278 0.80109 0.70646 0.11484  -0.10842 0.03452  7   PRO B CD  
2266 N N   . GLN B 8   ? 0.41646 0.72436 0.63774 0.09915  -0.04364 -0.02424 8   GLN B N   
2267 C CA  . GLN B 8   ? 0.40152 0.67199 0.60679 0.10142  -0.03146 -0.03548 8   GLN B CA  
2268 C C   . GLN B 8   ? 0.35393 0.60910 0.53929 0.07287  -0.02210 -0.03887 8   GLN B C   
2269 O O   . GLN B 8   ? 0.32689 0.60404 0.51238 0.05205  -0.02327 -0.03688 8   GLN B O   
2270 C CB  . GLN B 8   ? 0.32632 0.62451 0.54550 0.11753  -0.01921 -0.04595 8   GLN B CB  
2271 C CG  . GLN B 8   ? 0.42190 0.73404 0.66135 0.15238  -0.02773 -0.04840 8   GLN B CG  
2272 C CD  . GLN B 8   ? 0.40926 0.66343 0.63826 0.17118  -0.03987 -0.05066 8   GLN B CD  
2273 O OE1 . GLN B 8   ? 0.41728 0.63427 0.62788 0.17135  -0.03355 -0.05987 8   GLN B OE1 
2274 N NE2 . GLN B 8   ? 0.40725 0.65305 0.64896 0.18538  -0.05939 -0.04031 8   GLN B NE2 
2275 N N   . LEU B 9   ? 0.35220 0.56883 0.52091 0.07325  -0.01401 -0.04551 9   LEU B N   
2276 C CA  . LEU B 9   ? 0.34538 0.54609 0.49842 0.05068  -0.00463 -0.05009 9   LEU B CA  
2277 C C   . LEU B 9   ? 0.37727 0.60981 0.54174 0.03822  0.00571  -0.05370 9   LEU B C   
2278 O O   . LEU B 9   ? 0.30023 0.55830 0.47789 0.04975  0.01225  -0.05480 9   LEU B O   
2279 C CB  . LEU B 9   ? 0.36771 0.52485 0.50347 0.05564  0.00101  -0.05446 9   LEU B CB  
2280 C CG  . LEU B 9   ? 0.37461 0.49656 0.49728 0.06012  -0.00947 -0.04854 9   LEU B CG  
2281 C CD1 . LEU B 9   ? 0.34790 0.43415 0.46041 0.07177  -0.00660 -0.05330 9   LEU B CD1 
2282 C CD2 . LEU B 9   ? 0.34398 0.45988 0.45285 0.03971  -0.00957 -0.04656 9   LEU B CD2 
2283 N N   . GLN B 10  ? 0.31919 0.55219 0.47923 0.01435  0.00618  -0.05560 10  GLN B N   
2284 C CA  . GLN B 10  ? 0.32793 0.58501 0.50000 -0.00239 0.01266  -0.05615 10  GLN B CA  
2285 C C   . GLN B 10  ? 0.35598 0.58607 0.51907 -0.00617 0.02376  -0.05811 10  GLN B C   
2286 O O   . GLN B 10  ? 0.34153 0.52995 0.48654 -0.00719 0.02480  -0.06224 10  GLN B O   
2287 C CB  . GLN B 10  ? 0.32916 0.59310 0.50150 -0.02656 0.00517  -0.05947 10  GLN B CB  
2288 C CG  . GLN B 10  ? 0.32347 0.61935 0.50327 -0.02434 -0.00660 -0.05599 10  GLN B CG  
2289 C CD  . GLN B 10  ? 0.37105 0.68870 0.55648 -0.04926 -0.01426 -0.06031 10  GLN B CD  
2290 O OE1 . GLN B 10  ? 0.35668 0.67283 0.54859 -0.06795 -0.01148 -0.06342 10  GLN B OE1 
2291 N NE2 . GLN B 10  ? 0.35719 0.69501 0.54028 -0.05100 -0.02587 -0.05970 10  GLN B NE2 
2292 N N   . ARG B 11  ? 0.32561 0.58554 0.50229 -0.00798 0.03184  -0.05323 11  ARG B N   
2293 C CA  . ARG B 11  ? 0.31203 0.55808 0.48333 -0.01497 0.04169  -0.05052 11  ARG B CA  
2294 C C   . ARG B 11  ? 0.35164 0.60653 0.53434 -0.04456 0.03994  -0.04444 11  ARG B C   
2295 O O   . ARG B 11  ? 0.31621 0.61686 0.51913 -0.05476 0.03815  -0.03752 11  ARG B O   
2296 C CB  . ARG B 11  ? 0.33647 0.61736 0.51462 0.00244  0.05143  -0.04753 11  ARG B CB  
2297 C CG  . ARG B 11  ? 0.39267 0.65059 0.55607 0.02990  0.05315  -0.05598 11  ARG B CG  
2298 C CD  . ARG B 11  ? 0.41076 0.68077 0.58166 0.05346  0.04513  -0.06121 11  ARG B CD  
2299 N NE  . ARG B 11  ? 0.38097 0.62353 0.53908 0.07875  0.04417  -0.07027 11  ARG B NE  
2300 C CZ  . ARG B 11  ? 0.43813 0.66326 0.59675 0.09843  0.03272  -0.07440 11  ARG B CZ  
2301 N NH1 . ARG B 11  ? 0.34586 0.58262 0.51658 0.09718  0.02220  -0.06866 11  ARG B NH1 
2302 N NH2 . ARG B 11  ? 0.40938 0.60381 0.55642 0.11861  0.02980  -0.08346 11  ARG B NH2 
2303 N N   . LEU B 12  ? 0.34242 0.55414 0.51442 -0.05828 0.03897  -0.04644 12  LEU B N   
2304 C CA  . LEU B 12  ? 0.39232 0.59848 0.57516 -0.08654 0.03290  -0.04270 12  LEU B CA  
2305 C C   . LEU B 12  ? 0.41361 0.60358 0.59706 -0.09698 0.03855  -0.03124 12  LEU B C   
2306 O O   . LEU B 12  ? 0.37386 0.53568 0.54166 -0.08419 0.04477  -0.03247 12  LEU B O   
2307 C CB  . LEU B 12  ? 0.38925 0.55622 0.56132 -0.09378 0.02255  -0.05785 12  LEU B CB  
2308 C CG  . LEU B 12  ? 0.45329 0.64084 0.62820 -0.09725 0.01228  -0.06690 12  LEU B CG  
2309 C CD1 . LEU B 12  ? 0.41257 0.62988 0.58602 -0.07544 0.01415  -0.06484 12  LEU B CD1 
2310 C CD2 . LEU B 12  ? 0.45076 0.60018 0.60949 -0.10092 0.00464  -0.08452 12  LEU B CD2 
2311 N N   . ALA B 13  ? 0.38573 0.59536 0.58826 -0.12200 0.03487  -0.01767 13  ALA B N   
2312 C CA  . ALA B 13  ? 0.39702 0.58821 0.60256 -0.13722 0.03625  -0.00270 13  ALA B CA  
2313 C C   . ALA B 13  ? 0.50420 0.62864 0.70058 -0.14357 0.02699  -0.01310 13  ALA B C   
2314 O O   . ALA B 13  ? 0.50762 0.60814 0.69952 -0.14367 0.01795  -0.03150 13  ALA B O   
2315 C CB  . ALA B 13  ? 0.43876 0.66885 0.67006 -0.16642 0.03160  0.01835  13  ALA B CB  
2316 N N   . ALA B 14  ? 0.55890 0.65758 0.75335 -0.14856 0.02884  -0.00086 14  ALA B N   
2317 C CA  . ALA B 14  ? 0.56101 0.59725 0.74843 -0.14950 0.02083  -0.01026 14  ALA B CA  
2318 C C   . ALA B 14  ? 0.56883 0.57705 0.77020 -0.17101 0.00339  -0.01872 14  ALA B C   
2319 O O   . ALA B 14  ? 0.61327 0.57469 0.80687 -0.16509 -0.00421 -0.03829 14  ALA B O   
2320 C CB  . ALA B 14  ? 0.57867 0.59907 0.76626 -0.15339 0.02405  0.00973  14  ALA B CB  
2321 N N   . ASP B 15  ? 0.54803 0.58569 0.77034 -0.19574 -0.00398 -0.00553 15  ASP B N   
2322 C CA  . ASP B 15  ? 0.55024 0.56033 0.78681 -0.21899 -0.02360 -0.01437 15  ASP B CA  
2323 C C   . ASP B 15  ? 0.54702 0.57033 0.77727 -0.21376 -0.02846 -0.03971 15  ASP B C   
2324 O O   . ASP B 15  ? 0.55901 0.56852 0.80038 -0.23404 -0.04557 -0.04943 15  ASP B O   
2325 C CB  . ASP B 15  ? 0.61716 0.65495 0.88122 -0.25268 -0.03210 0.01424  15  ASP B CB  
2326 C CG  . ASP B 15  ? 0.60821 0.72411 0.88108 -0.25502 -0.02255 0.02625  15  ASP B CG  
2327 O OD1 . ASP B 15  ? 0.59786 0.75295 0.86265 -0.23653 -0.00459 0.03613  15  ASP B OD1 
2328 O OD2 . ASP B 15  ? 0.73262 0.87164 1.02074 -0.27391 -0.03380 0.02406  15  ASP B OD2 
2329 N N   . ALA B 16  ? 0.54256 0.59123 0.75556 -0.18843 -0.01590 -0.04979 16  ALA B N   
2330 C CA  . ALA B 16  ? 0.55702 0.62825 0.76522 -0.18479 -0.02070 -0.06766 16  ALA B CA  
2331 C C   . ALA B 16  ? 0.57597 0.60283 0.77341 -0.18563 -0.03365 -0.09608 16  ALA B C   
2332 O O   . ALA B 16  ? 0.56826 0.54617 0.75848 -0.17974 -0.03563 -0.10542 16  ALA B O   
2333 C CB  . ALA B 16  ? 0.52002 0.62010 0.71262 -0.15687 -0.00691 -0.06976 16  ALA B CB  
2334 N N   . ASP B 17  ? 0.51603 0.56508 0.71248 -0.19149 -0.04270 -0.11078 17  ASP B N   
2335 C CA  . ASP B 17  ? 0.55530 0.57238 0.74136 -0.19407 -0.05647 -0.14095 17  ASP B CA  
2336 C C   . ASP B 17  ? 0.57663 0.58161 0.73623 -0.16604 -0.04742 -0.15906 17  ASP B C   
2337 O O   . ASP B 17  ? 0.51038 0.54798 0.65885 -0.14942 -0.03633 -0.15271 17  ASP B O   
2338 C CB  . ASP B 17  ? 0.54564 0.59910 0.73751 -0.21029 -0.06918 -0.14948 17  ASP B CB  
2339 C CG  . ASP B 17  ? 0.66047 0.68416 0.84177 -0.21592 -0.08586 -0.18352 17  ASP B CG  
2340 O OD1 . ASP B 17  ? 0.75739 0.74632 0.95286 -0.23805 -0.10318 -0.19086 17  ASP B OD1 
2341 O OD2 . ASP B 17  ? 0.72347 0.75941 0.88219 -0.19834 -0.08272 -0.20311 17  ASP B OD2 
2342 N N   . VAL B 18  ? 0.61867 0.57745 0.76990 -0.16078 -0.05351 -0.18121 18  VAL B N   
2343 C CA  . VAL B 18  ? 0.64548 0.59783 0.77389 -0.13487 -0.04393 -0.19570 18  VAL B CA  
2344 C C   . VAL B 18  ? 0.64224 0.63085 0.75317 -0.12908 -0.04641 -0.21410 18  VAL B C   
2345 O O   . VAL B 18  ? 0.62100 0.63443 0.71637 -0.11196 -0.03568 -0.20956 18  VAL B O   
2346 C CB  . VAL B 18  ? 0.70004 0.59814 0.82712 -0.12771 -0.04915 -0.21419 18  VAL B CB  
2347 C CG1 . VAL B 18  ? 0.68632 0.58917 0.79044 -0.10240 -0.04103 -0.23368 18  VAL B CG1 
2348 C CG2 . VAL B 18  ? 0.67332 0.54332 0.81392 -0.12877 -0.04354 -0.18932 18  VAL B CG2 
2349 N N   . ASP B 19  ? 0.58883 0.58266 0.70215 -0.14497 -0.06210 -0.23332 19  ASP B N   
2350 C CA  . ASP B 19  ? 0.58803 0.62567 0.68491 -0.14247 -0.06548 -0.24704 19  ASP B CA  
2351 C C   . ASP B 19  ? 0.55840 0.64492 0.65696 -0.13862 -0.05619 -0.21905 19  ASP B C   
2352 O O   . ASP B 19  ? 0.52800 0.64401 0.60950 -0.12463 -0.05056 -0.21819 19  ASP B O   
2353 C CB  . ASP B 19  ? 0.67591 0.71578 0.77845 -0.16457 -0.08560 -0.26793 19  ASP B CB  
2354 C CG  . ASP B 19  ? 0.81800 0.80674 0.91671 -0.16483 -0.09829 -0.30284 19  ASP B CG  
2355 O OD1 . ASP B 19  ? 0.86179 0.81410 0.95684 -0.14756 -0.09064 -0.30760 19  ASP B OD1 
2356 O OD2 . ASP B 19  ? 0.86696 0.84994 0.96284 -0.17793 -0.11540 -0.31830 19  ASP B OD2 
2357 N N   . ARG B 20  ? 0.51950 0.61640 0.63995 -0.15036 -0.05524 -0.19497 20  ARG B N   
2358 C CA  . ARG B 20  ? 0.48286 0.62339 0.60838 -0.14295 -0.04722 -0.17045 20  ARG B CA  
2359 C C   . ARG B 20  ? 0.44248 0.57617 0.55497 -0.11896 -0.03270 -0.16004 20  ARG B C   
2360 O O   . ARG B 20  ? 0.41876 0.58167 0.52240 -0.10731 -0.03048 -0.15265 20  ARG B O   
2361 C CB  . ARG B 20  ? 0.48441 0.63818 0.63636 -0.15655 -0.04647 -0.14842 20  ARG B CB  
2362 C CG  . ARG B 20  ? 0.44513 0.64315 0.60471 -0.14402 -0.03790 -0.12605 20  ARG B CG  
2363 C CD  . ARG B 20  ? 0.44364 0.66269 0.62865 -0.15476 -0.03484 -0.10590 20  ARG B CD  
2364 N NE  . ARG B 20  ? 0.43969 0.70207 0.63272 -0.13806 -0.02702 -0.08913 20  ARG B NE  
2365 C CZ  . ARG B 20  ? 0.41638 0.70981 0.62993 -0.13944 -0.02071 -0.07144 20  ARG B CZ  
2366 N NH1 . ARG B 20  ? 0.36843 0.65780 0.59676 -0.16017 -0.02118 -0.06343 20  ARG B NH1 
2367 N NH2 . ARG B 20  ? 0.39076 0.72198 0.61098 -0.11905 -0.01461 -0.06108 20  ARG B NH2 
2368 N N   . MET B 21  ? 0.44498 0.53997 0.55744 -0.11274 -0.02463 -0.15739 21  MET B N   
2369 C CA  . MET B 21  ? 0.42272 0.50954 0.52351 -0.09235 -0.01254 -0.14773 21  MET B CA  
2370 C C   . MET B 21  ? 0.47837 0.57243 0.55758 -0.08118 -0.01297 -0.16050 21  MET B C   
2371 O O   . MET B 21  ? 0.42821 0.54192 0.49941 -0.06968 -0.00914 -0.14821 21  MET B O   
2372 C CB  . MET B 21  ? 0.46422 0.50975 0.56824 -0.08984 -0.00601 -0.14454 21  MET B CB  
2373 C CG  . MET B 21  ? 0.51618 0.56449 0.63978 -0.09980 -0.00320 -0.12537 21  MET B CG  
2374 S SD  . MET B 21  ? 0.52828 0.53467 0.65428 -0.09716 0.00396  -0.11612 21  MET B SD  
2375 C CE  . MET B 21  ? 0.55672 0.52613 0.69456 -0.11736 -0.01039 -0.12952 21  MET B CE  
2376 N N   . CYS B 22  ? 0.45888 0.53872 0.52923 -0.08457 -0.01876 -0.18522 22  CYS B N   
2377 C CA  . CYS B 22  ? 0.50262 0.60053 0.55176 -0.07507 -0.01907 -0.20003 22  CYS B CA  
2378 C C   . CYS B 22  ? 0.48251 0.63016 0.52502 -0.07741 -0.02392 -0.19147 22  CYS B C   
2379 O O   . CYS B 22  ? 0.46303 0.63343 0.49158 -0.06760 -0.02052 -0.18338 22  CYS B O   
2380 C CB  . CYS B 22  ? 0.58161 0.66082 0.62505 -0.07881 -0.02710 -0.23337 22  CYS B CB  
2381 S SG  . CYS B 22  ? 0.82082 0.92331 0.83764 -0.06353 -0.02497 -0.25804 22  CYS B SG  
2382 N N   . ARG B 23  ? 0.44915 0.61670 0.50307 -0.09160 -0.03323 -0.19044 23  ARG B N   
2383 C CA  . ARG B 23  ? 0.42684 0.64348 0.47679 -0.09347 -0.03950 -0.17996 23  ARG B CA  
2384 C C   . ARG B 23  ? 0.44442 0.67175 0.50324 -0.08273 -0.03409 -0.14934 23  ARG B C   
2385 O O   . ARG B 23  ? 0.42454 0.68134 0.47512 -0.07678 -0.03708 -0.13644 23  ARG B O   
2386 C CB  . ARG B 23  ? 0.48393 0.72191 0.54535 -0.11191 -0.05223 -0.18747 23  ARG B CB  
2387 C CG  . ARG B 23  ? 0.55208 0.80369 0.59622 -0.12041 -0.06294 -0.21753 23  ARG B CG  
2388 C CD  . ARG B 23  ? 0.57388 0.85543 0.62794 -0.13954 -0.07763 -0.22142 23  ARG B CD  
2389 N NE  . ARG B 23  ? 0.63182 0.87950 0.70410 -0.15606 -0.08419 -0.23205 23  ARG B NE  
2390 C CZ  . ARG B 23  ? 0.62806 0.84761 0.69403 -0.16554 -0.09435 -0.26387 23  ARG B CZ  
2391 N NH1 . ARG B 23  ? 0.71693 0.94172 0.75712 -0.15729 -0.09706 -0.29237 23  ARG B NH1 
2392 N NH2 . ARG B 23  ? 0.66844 0.85528 0.75517 -0.18360 -0.10301 -0.26711 23  ARG B NH2 
2393 N N   . LEU B 24  ? 0.40367 0.60781 0.47916 -0.07989 -0.02740 -0.13755 24  LEU B N   
2394 C CA  . LEU B 24  ? 0.43276 0.64036 0.51514 -0.06587 -0.02252 -0.11424 24  LEU B CA  
2395 C C   . LEU B 24  ? 0.41719 0.61456 0.48268 -0.05339 -0.01889 -0.10800 24  LEU B C   
2396 O O   . LEU B 24  ? 0.37661 0.58855 0.44246 -0.04479 -0.02257 -0.09002 24  LEU B O   
2397 C CB  . LEU B 24  ? 0.39615 0.58015 0.49356 -0.06348 -0.01404 -0.10780 24  LEU B CB  
2398 C CG  . LEU B 24  ? 0.40343 0.61516 0.52348 -0.06922 -0.01643 -0.09875 24  LEU B CG  
2399 C CD1 . LEU B 24  ? 0.35724 0.55213 0.48877 -0.06707 -0.00658 -0.09198 24  LEU B CD1 
2400 C CD2 . LEU B 24  ? 0.41757 0.66217 0.54374 -0.05678 -0.02133 -0.08406 24  LEU B CD2 
2401 N N   . LEU B 25  ? 0.39773 0.57015 0.45050 -0.05243 -0.01305 -0.12138 25  LEU B N   
2402 C CA  . LEU B 25  ? 0.42554 0.59356 0.46387 -0.04279 -0.00938 -0.11429 25  LEU B CA  
2403 C C   . LEU B 25  ? 0.43193 0.64046 0.45665 -0.04512 -0.01674 -0.11059 25  LEU B C   
2404 O O   . LEU B 25  ? 0.42117 0.63807 0.43983 -0.03977 -0.01803 -0.09215 25  LEU B O   
2405 C CB  . LEU B 25  ? 0.44966 0.58886 0.48014 -0.04021 -0.00164 -0.13048 25  LEU B CB  
2406 C CG  . LEU B 25  ? 0.40530 0.50499 0.44566 -0.03577 0.00609  -0.12589 25  LEU B CG  
2407 C CD1 . LEU B 25  ? 0.42467 0.49836 0.45931 -0.03276 0.01131  -0.14171 25  LEU B CD1 
2408 C CD2 . LEU B 25  ? 0.36389 0.45753 0.40481 -0.02613 0.00855  -0.10432 25  LEU B CD2 
2409 N N   . GLU B 26  ? 0.41653 0.65216 0.43593 -0.05460 -0.02300 -0.12666 26  GLU B N   
2410 C CA  . GLU B 26  ? 0.40134 0.68291 0.40523 -0.05748 -0.02982 -0.12218 26  GLU B CA  
2411 C C   . GLU B 26  ? 0.40634 0.71631 0.41987 -0.05931 -0.04023 -0.09686 26  GLU B C   
2412 O O   . GLU B 26  ? 0.42207 0.76231 0.42669 -0.05922 -0.04615 -0.07829 26  GLU B O   
2413 C CB  . GLU B 26  ? 0.44282 0.74550 0.43355 -0.06558 -0.03343 -0.15276 26  GLU B CB  
2414 C CG  . GLU B 26  ? 0.58746 0.86822 0.56679 -0.05897 -0.02487 -0.17788 26  GLU B CG  
2415 C CD  . GLU B 26  ? 0.58232 0.87585 0.54944 -0.04933 -0.01744 -0.16427 26  GLU B CD  
2416 O OE1 . GLU B 26  ? 0.60918 0.95262 0.56025 -0.05122 -0.02050 -0.15893 26  GLU B OE1 
2417 O OE2 . GLU B 26  ? 0.59398 0.85163 0.56792 -0.04149 -0.00925 -0.15708 26  GLU B OE2 
2418 N N   . GLU B 27  ? 0.41071 0.71387 0.44414 -0.06062 -0.04321 -0.09346 27  GLU B N   
2419 C CA  . GLU B 27  ? 0.39794 0.72947 0.44464 -0.05932 -0.05390 -0.07137 27  GLU B CA  
2420 C C   . GLU B 27  ? 0.39461 0.70250 0.45394 -0.04457 -0.05343 -0.04754 27  GLU B C   
2421 O O   . GLU B 27  ? 0.39929 0.72109 0.45776 -0.04035 -0.06268 -0.02489 27  GLU B O   
2422 C CB  . GLU B 27  ? 0.46037 0.80534 0.52409 -0.06764 -0.05790 -0.08068 27  GLU B CB  
2423 C CG  . GLU B 27  ? 0.50729 0.86438 0.55918 -0.08356 -0.06066 -0.10887 27  GLU B CG  
2424 C CD  . GLU B 27  ? 0.70702 1.08874 0.77540 -0.09668 -0.06974 -0.11375 27  GLU B CD  
2425 O OE1 . GLU B 27  ? 0.76480 1.17163 0.85133 -0.09281 -0.07535 -0.09305 27  GLU B OE1 
2426 O OE2 . GLU B 27  ? 0.70461 1.08070 0.76926 -0.11077 -0.07270 -0.13853 27  GLU B OE2 
2427 N N   . ASP B 28  ? 0.39389 0.66573 0.46466 -0.03710 -0.04415 -0.05244 28  ASP B N   
2428 C CA  . ASP B 28  ? 0.37048 0.61519 0.45137 -0.02153 -0.04309 -0.03728 28  ASP B CA  
2429 C C   . ASP B 28  ? 0.37792 0.59031 0.44465 -0.01768 -0.03776 -0.03440 28  ASP B C   
2430 O O   . ASP B 28  ? 0.38409 0.58187 0.45322 -0.00864 -0.04394 -0.01689 28  ASP B O   
2431 C CB  . ASP B 28  ? 0.37972 0.61043 0.47746 -0.01589 -0.03500 -0.04497 28  ASP B CB  
2432 C CG  . ASP B 28  ? 0.44142 0.70753 0.55997 -0.01450 -0.04155 -0.04014 28  ASP B CG  
2433 O OD1 . ASP B 28  ? 0.46214 0.76131 0.58156 -0.01907 -0.05304 -0.03217 28  ASP B OD1 
2434 O OD2 . ASP B 28  ? 0.48677 0.75312 0.62134 -0.00891 -0.03523 -0.04306 28  ASP B OD2 
2435 N N   . GLY B 29  ? 0.36692 0.56656 0.42085 -0.02407 -0.02795 -0.05109 29  GLY B N   
2436 C CA  . GLY B 29  ? 0.34053 0.51594 0.38289 -0.02076 -0.02270 -0.04817 29  GLY B CA  
2437 C C   . GLY B 29  ? 0.32782 0.46360 0.37564 -0.01306 -0.01370 -0.05242 29  GLY B C   
2438 O O   . GLY B 29  ? 0.34722 0.46271 0.38645 -0.01086 -0.00945 -0.05054 29  GLY B O   
2439 N N   . ALA B 30  ? 0.37957 0.50956 0.44140 -0.00966 -0.01077 -0.05697 30  ALA B N   
2440 C CA  . ALA B 30  ? 0.35493 0.45505 0.42096 -0.00257 -0.00229 -0.05968 30  ALA B CA  
2441 C C   . ALA B 30  ? 0.33831 0.44962 0.41946 -0.00438 0.00173  -0.06572 30  ALA B C   
2442 O O   . ALA B 30  ? 0.31714 0.45780 0.40898 -0.00666 -0.00410 -0.06368 30  ALA B O   
2443 C CB  . ALA B 30  ? 0.30128 0.38295 0.36864 0.01088  -0.00714 -0.04676 30  ALA B CB  
2444 N N   . PHE B 31  ? 0.32758 0.41985 0.41038 -0.00474 0.01110  -0.07076 31  PHE B N   
2445 C CA  . PHE B 31  ? 0.36627 0.47312 0.46440 -0.00687 0.01574  -0.07146 31  PHE B CA  
2446 C C   . PHE B 31  ? 0.39454 0.47890 0.49006 -0.00362 0.02530  -0.07124 31  PHE B C   
2447 O O   . PHE B 31  ? 0.39149 0.44761 0.47413 -0.00111 0.02760  -0.07210 31  PHE B O   
2448 C CB  . PHE B 31  ? 0.34864 0.47230 0.45447 -0.02497 0.01373  -0.07855 31  PHE B CB  
2449 C CG  . PHE B 31  ? 0.37788 0.47409 0.47637 -0.03631 0.01665  -0.08842 31  PHE B CG  
2450 C CD1 . PHE B 31  ? 0.34237 0.42795 0.42677 -0.03832 0.01320  -0.09855 31  PHE B CD1 
2451 C CD2 . PHE B 31  ? 0.38248 0.46637 0.48919 -0.04408 0.02211  -0.08691 31  PHE B CD2 
2452 C CE1 . PHE B 31  ? 0.44009 0.49937 0.51988 -0.04458 0.01495  -0.11050 31  PHE B CE1 
2453 C CE2 . PHE B 31  ? 0.38621 0.43991 0.48901 -0.05277 0.02225  -0.09495 31  PHE B CE2 
2454 C CZ  . PHE B 31  ? 0.40100 0.44045 0.49102 -0.05149 0.01850  -0.10853 31  PHE B CZ  
2455 N N   . ILE B 32  ? 0.38187 0.48536 0.49019 -0.00411 0.03061  -0.06847 32  ILE B N   
2456 C CA  . ILE B 32  ? 0.38188 0.47597 0.48825 -0.00112 0.03962  -0.06578 32  ILE B CA  
2457 C C   . ILE B 32  ? 0.38884 0.49111 0.50552 -0.02040 0.04335  -0.06256 32  ILE B C   
2458 O O   . ILE B 32  ? 0.38978 0.52201 0.52177 -0.03083 0.04081  -0.06032 32  ILE B O   
2459 C CB  . ILE B 32  ? 0.34243 0.45892 0.45423 0.01724  0.04264  -0.06409 32  ILE B CB  
2460 C CG1 . ILE B 32  ? 0.38564 0.47964 0.48684 0.03569  0.03612  -0.06677 32  ILE B CG1 
2461 C CG2 . ILE B 32  ? 0.33810 0.46189 0.44910 0.01682  0.05309  -0.06093 32  ILE B CG2 
2462 C CD1 . ILE B 32  ? 0.34299 0.45752 0.45290 0.05740  0.03411  -0.06947 32  ILE B CD1 
2463 N N   . LEU B 33  ? 0.37602 0.45180 0.48604 -0.02626 0.04751  -0.06034 33  LEU B N   
2464 C CA  . LEU B 33  ? 0.37131 0.45100 0.49255 -0.04444 0.04950  -0.05223 33  LEU B CA  
2465 C C   . LEU B 33  ? 0.36563 0.47086 0.48893 -0.03891 0.05860  -0.04151 33  LEU B C   
2466 O O   . LEU B 33  ? 0.37741 0.46772 0.48692 -0.02693 0.06325  -0.04154 33  LEU B O   
2467 C CB  . LEU B 33  ? 0.42274 0.45971 0.53781 -0.05277 0.04701  -0.05429 33  LEU B CB  
2468 C CG  . LEU B 33  ? 0.45626 0.47248 0.57049 -0.05966 0.03817  -0.06801 33  LEU B CG  
2469 C CD1 . LEU B 33  ? 0.46990 0.44487 0.57658 -0.05859 0.03696  -0.07307 33  LEU B CD1 
2470 C CD2 . LEU B 33  ? 0.41150 0.44189 0.54303 -0.07980 0.03090  -0.06756 33  LEU B CD2 
2471 N N   . LYS B 34  ? 0.36220 0.51061 0.50228 -0.04798 0.06085  -0.03263 34  LYS B N   
2472 C CA  . LYS B 34  ? 0.37094 0.55852 0.51300 -0.04050 0.07070  -0.02403 34  LYS B CA  
2473 C C   . LYS B 34  ? 0.40142 0.58449 0.54420 -0.05778 0.07410  -0.00779 34  LYS B C   
2474 O O   . LYS B 34  ? 0.40762 0.58381 0.56387 -0.08205 0.06812  0.00297  34  LYS B O   
2475 C CB  . LYS B 34  ? 0.35756 0.60457 0.51938 -0.04163 0.07234  -0.01985 34  LYS B CB  
2476 C CG  . LYS B 34  ? 0.47701 0.77405 0.63933 -0.02453 0.08344  -0.01769 34  LYS B CG  
2477 C CD  . LYS B 34  ? 0.49135 0.77932 0.64148 0.00827  0.08339  -0.03593 34  LYS B CD  
2478 C CE  . LYS B 34  ? 0.51734 0.84886 0.66398 0.02938  0.09376  -0.04015 34  LYS B CE  
2479 N NZ  . LYS B 34  ? 0.51009 0.83058 0.63901 0.02556  0.10059  -0.03521 34  LYS B NZ  
2480 N N   . GLY B 35  ? 0.41024 0.59533 0.53868 -0.04591 0.08166  -0.00561 35  GLY B N   
2481 C CA  . GLY B 35  ? 0.35327 0.54434 0.48222 -0.06154 0.08505  0.01376  35  GLY B CA  
2482 C C   . GLY B 35  ? 0.39610 0.53482 0.52723 -0.07934 0.07619  0.02115  35  GLY B C   
2483 O O   . GLY B 35  ? 0.41809 0.56226 0.56122 -0.10125 0.07355  0.04196  35  GLY B O   
2484 N N   . LEU B 36  ? 0.37536 0.46515 0.49671 -0.07022 0.07054  0.00538  36  LEU B N   
2485 C CA  . LEU B 36  ? 0.44505 0.48624 0.56923 -0.08196 0.06208  0.00827  36  LEU B CA  
2486 C C   . LEU B 36  ? 0.43155 0.46274 0.55014 -0.08514 0.06423  0.02514  36  LEU B C   
2487 O O   . LEU B 36  ? 0.45090 0.46561 0.58222 -0.10355 0.05740  0.04158  36  LEU B O   
2488 C CB  . LEU B 36  ? 0.40176 0.40479 0.51478 -0.06800 0.05797  -0.01254 36  LEU B CB  
2489 C CG  . LEU B 36  ? 0.46429 0.42032 0.58033 -0.07442 0.04991  -0.01388 36  LEU B CG  
2490 C CD1 . LEU B 36  ? 0.46696 0.41286 0.60286 -0.09570 0.03948  -0.01134 36  LEU B CD1 
2491 C CD2 . LEU B 36  ? 0.45565 0.38551 0.55902 -0.05858 0.04830  -0.03308 36  LEU B CD2 
2492 N N   . LEU B 37  ? 0.40808 0.44716 0.50825 -0.06795 0.07158  0.02185  37  LEU B N   
2493 C CA  . LEU B 37  ? 0.45232 0.48324 0.54439 -0.06960 0.07278  0.03671  37  LEU B CA  
2494 C C   . LEU B 37  ? 0.43290 0.51810 0.52334 -0.07479 0.08100  0.05349  37  LEU B C   
2495 O O   . LEU B 37  ? 0.41936 0.54111 0.50028 -0.06005 0.08902  0.04222  37  LEU B O   
2496 C CB  . LEU B 37  ? 0.44739 0.45521 0.51923 -0.04973 0.07401  0.02296  37  LEU B CB  
2497 C CG  . LEU B 37  ? 0.43639 0.40341 0.50804 -0.04262 0.06779  0.00633  37  LEU B CG  
2498 C CD1 . LEU B 37  ? 0.38298 0.33686 0.43631 -0.02631 0.06870  -0.00239 37  LEU B CD1 
2499 C CD2 . LEU B 37  ? 0.46861 0.40136 0.55437 -0.05471 0.05964  0.01353  37  LEU B CD2 
2500 N N   . PRO B 38  ? 0.42732 0.52214 0.52717 -0.09449 0.07869  0.08036  38  PRO B N   
2501 C CA  . PRO B 38  ? 0.45919 0.61603 0.55507 -0.09975 0.08765  0.09830  38  PRO B CA  
2502 C C   . PRO B 38  ? 0.46011 0.63032 0.52904 -0.07850 0.09523  0.08737  38  PRO B C   
2503 O O   . PRO B 38  ? 0.46628 0.59362 0.52229 -0.06659 0.09134  0.07593  38  PRO B O   
2504 C CB  . PRO B 38  ? 0.40817 0.56019 0.51918 -0.12697 0.07984  0.13308  38  PRO B CB  
2505 C CG  . PRO B 38  ? 0.49279 0.57150 0.60929 -0.12716 0.06735  0.12818  38  PRO B CG  
2506 C CD  . PRO B 38  ? 0.43204 0.48243 0.54714 -0.11209 0.06652  0.09606  38  PRO B CD  
2507 N N   . PHE B 39  ? 0.42640 0.66064 0.48722 -0.07365 0.10565  0.08979  39  PHE B N   
2508 C CA  . PHE B 39  ? 0.48082 0.73207 0.51466 -0.05184 0.11189  0.07388  39  PHE B CA  
2509 C C   . PHE B 39  ? 0.46345 0.69597 0.48341 -0.05726 0.10792  0.08890  39  PHE B C   
2510 O O   . PHE B 39  ? 0.51001 0.72648 0.50836 -0.04004 0.10727  0.07149  39  PHE B O   
2511 C CB  . PHE B 39  ? 0.49107 0.82229 0.51982 -0.04527 0.12398  0.07311  39  PHE B CB  
2512 C CG  . PHE B 39  ? 0.55703 0.90456 0.55792 -0.01831 0.12899  0.04747  39  PHE B CG  
2513 C CD1 . PHE B 39  ? 0.60050 0.90502 0.59221 0.00516  0.12423  0.01554  39  PHE B CD1 
2514 C CD2 . PHE B 39  ? 0.58272 0.98988 0.56639 -0.01724 0.13694  0.05534  39  PHE B CD2 
2515 C CE1 . PHE B 39  ? 0.58151 0.89427 0.54881 0.02919  0.12534  -0.00972 39  PHE B CE1 
2516 C CE2 . PHE B 39  ? 0.56641 0.98705 0.52302 0.00858  0.13976  0.02709  39  PHE B CE2 
2517 C CZ  . PHE B 39  ? 0.62368 0.99308 0.57285 0.03187  0.13297  -0.00639 39  PHE B CZ  
2518 N N   . ASP B 40  ? 0.42828 0.66171 0.46147 -0.08156 0.10328  0.12214  40  ASP B N   
2519 C CA  . ASP B 40  ? 0.50177 0.71712 0.52429 -0.08610 0.09780  0.13893  40  ASP B CA  
2520 C C   . ASP B 40  ? 0.51345 0.65741 0.53499 -0.07584 0.08866  0.12393  40  ASP B C   
2521 O O   . ASP B 40  ? 0.50809 0.63967 0.51236 -0.06676 0.08637  0.12081  40  ASP B O   
2522 C CB  . ASP B 40  ? 0.49132 0.71874 0.53225 -0.11498 0.09178  0.18124  40  ASP B CB  
2523 C CG  . ASP B 40  ? 0.63311 0.80215 0.70292 -0.12968 0.07908  0.18974  40  ASP B CG  
2524 O OD1 . ASP B 40  ? 0.56190 0.72221 0.64434 -0.12911 0.07955  0.17358  40  ASP B OD1 
2525 O OD2 . ASP B 40  ? 0.74349 0.87536 0.82361 -0.14090 0.06738  0.21173  40  ASP B OD2 
2526 N N   . VAL B 41  ? 0.51904 0.62105 0.55865 -0.07729 0.08327  0.11419  41  VAL B N   
2527 C CA  . VAL B 41  ? 0.47846 0.52301 0.51710 -0.06572 0.07633  0.09762  41  VAL B CA  
2528 C C   . VAL B 41  ? 0.47623 0.52152 0.49319 -0.04389 0.08050  0.06974  41  VAL B C   
2529 O O   . VAL B 41  ? 0.43859 0.45979 0.44407 -0.03500 0.07644  0.06405  41  VAL B O   
2530 C CB  . VAL B 41  ? 0.46653 0.47536 0.52680 -0.07135 0.07028  0.09031  41  VAL B CB  
2531 C CG1 . VAL B 41  ? 0.47124 0.43382 0.52809 -0.05633 0.06565  0.06903  41  VAL B CG1 
2532 C CG2 . VAL B 41  ? 0.47817 0.47204 0.56118 -0.09325 0.06113  0.11737  41  VAL B CG2 
2533 N N   . VAL B 42  ? 0.46056 0.53374 0.47358 -0.03531 0.08701  0.05314  42  VAL B N   
2534 C CA  . VAL B 42  ? 0.49712 0.56513 0.49269 -0.01466 0.08768  0.02671  42  VAL B CA  
2535 C C   . VAL B 42  ? 0.47536 0.55760 0.44762 -0.00750 0.08804  0.02573  42  VAL B C   
2536 O O   . VAL B 42  ? 0.42447 0.47832 0.38433 0.00210  0.08202  0.01345  42  VAL B O   
2537 C CB  . VAL B 42  ? 0.48018 0.57913 0.47872 -0.00511 0.09339  0.01108  42  VAL B CB  
2538 C CG1 . VAL B 42  ? 0.49776 0.59261 0.47787 0.01705  0.09179  -0.01435 42  VAL B CG1 
2539 C CG2 . VAL B 42  ? 0.44998 0.52879 0.46882 -0.01068 0.09032  0.00809  42  VAL B CG2 
2540 N N   . GLU B 43  ? 0.46601 0.59565 0.43208 -0.01422 0.09414  0.04049  43  GLU B N   
2541 C CA  . GLU B 43  ? 0.46119 0.61153 0.40189 -0.00695 0.09435  0.03685  43  GLU B CA  
2542 C C   . GLU B 43  ? 0.46407 0.58467 0.40158 -0.01529 0.08614  0.05358  43  GLU B C   
2543 O O   . GLU B 43  ? 0.48318 0.59498 0.40121 -0.00634 0.08127  0.04209  43  GLU B O   
2544 C CB  . GLU B 43  ? 0.53945 0.75954 0.47244 -0.01094 0.10413  0.04744  43  GLU B CB  
2545 C CG  . GLU B 43  ? 0.58906 0.84821 0.51940 0.00593  0.11250  0.02308  43  GLU B CG  
2546 C CD  . GLU B 43  ? 0.64479 0.87766 0.55835 0.03174  0.10750  -0.01458 43  GLU B CD  
2547 O OE1 . GLU B 43  ? 0.56810 0.74922 0.49106 0.03685  0.10013  -0.02625 43  GLU B OE1 
2548 O OE2 . GLU B 43  ? 0.70587 0.97139 0.59677 0.04660  0.10979  -0.03246 43  GLU B OE2 
2549 N N   . SER B 44  ? 0.43576 0.53933 0.39346 -0.03171 0.08272  0.07992  44  SER B N   
2550 C CA  . SER B 44  ? 0.47569 0.54660 0.43495 -0.03540 0.07368  0.09355  44  SER B CA  
2551 C C   . SER B 44  ? 0.46014 0.48784 0.41681 -0.02227 0.06800  0.07129  44  SER B C   
2552 O O   . SER B 44  ? 0.42190 0.43967 0.36710 -0.01826 0.06202  0.07094  44  SER B O   
2553 C CB  . SER B 44  ? 0.45298 0.50233 0.43894 -0.05120 0.06845  0.12048  44  SER B CB  
2554 O OG  . SER B 44  ? 0.60103 0.68975 0.59240 -0.06778 0.07123  0.14717  44  SER B OG  
2555 N N   . PHE B 45  ? 0.43253 0.43801 0.40087 -0.01739 0.06895  0.05520  45  PHE B N   
2556 C CA  . PHE B 45  ? 0.44074 0.41239 0.40762 -0.00716 0.06366  0.03726  45  PHE B CA  
2557 C C   . PHE B 45  ? 0.45284 0.43164 0.39652 0.00384  0.06123  0.01904  45  PHE B C   
2558 O O   . PHE B 45  ? 0.45116 0.41176 0.38775 0.00669  0.05372  0.01608  45  PHE B O   
2559 C CB  . PHE B 45  ? 0.45523 0.41167 0.43708 -0.00543 0.06538  0.02524  45  PHE B CB  
2560 C CG  . PHE B 45  ? 0.45811 0.38346 0.44332 0.00122  0.05991  0.01336  45  PHE B CG  
2561 C CD1 . PHE B 45  ? 0.45023 0.36135 0.43135 0.00340  0.05404  0.01730  45  PHE B CD1 
2562 C CD2 . PHE B 45  ? 0.42764 0.34490 0.42067 0.00433  0.06053  0.00016  45  PHE B CD2 
2563 C CE1 . PHE B 45  ? 0.45854 0.35126 0.44366 0.00810  0.04979  0.00896  45  PHE B CE1 
2564 C CE2 . PHE B 45  ? 0.42758 0.32522 0.42275 0.00890  0.05589  -0.00807 45  PHE B CE2 
2565 C CZ  . PHE B 45  ? 0.46318 0.35009 0.45474 0.01053  0.05098  -0.00332 45  PHE B CZ  
2566 N N   . ASN B 46  ? 0.45184 0.45847 0.38448 0.01038  0.06632  0.00622  46  ASN B N   
2567 C CA  . ASN B 46  ? 0.47357 0.48333 0.38411 0.02269  0.06163  -0.01474 46  ASN B CA  
2568 C C   . ASN B 46  ? 0.48140 0.49936 0.37407 0.01924  0.05641  -0.00743 46  ASN B C   
2569 O O   . ASN B 46  ? 0.47939 0.47807 0.35933 0.02420  0.04641  -0.02012 46  ASN B O   
2570 C CB  . ASN B 46  ? 0.46741 0.51243 0.37026 0.03350  0.06863  -0.03073 46  ASN B CB  
2571 C CG  . ASN B 46  ? 0.49674 0.52444 0.40972 0.04431  0.06710  -0.04883 46  ASN B CG  
2572 O OD1 . ASN B 46  ? 0.49685 0.48566 0.41304 0.04652  0.05785  -0.05552 46  ASN B OD1 
2573 N ND2 . ASN B 46  ? 0.45151 0.51217 0.37104 0.05014  0.07561  -0.05419 46  ASN B ND2 
2574 N N   . ARG B 47  ? 0.45504 0.50220 0.34720 0.00899  0.06120  0.01501  47  ARG B N   
2575 C CA  . ARG B 47  ? 0.49834 0.55863 0.37236 0.00542  0.05539  0.02333  47  ARG B CA  
2576 C C   . ARG B 47  ? 0.47628 0.50096 0.35896 0.00097  0.04542  0.03348  47  ARG B C   
2577 O O   . ARG B 47  ? 0.51370 0.53502 0.38066 0.00231  0.03627  0.02770  47  ARG B O   
2578 C CB  . ARG B 47  ? 0.50565 0.60993 0.37790 -0.00598 0.06166  0.04970  47  ARG B CB  
2579 C CG  . ARG B 47  ? 0.60606 0.76012 0.47024 -0.00284 0.07285  0.04324  47  ARG B CG  
2580 C CD  . ARG B 47  ? 0.67364 0.85708 0.50680 0.01246  0.07286  0.01367  47  ARG B CD  
2581 N NE  . ARG B 47  ? 0.65355 0.80135 0.48371 0.02938  0.06741  -0.02071 47  ARG B NE  
2582 C CZ  . ARG B 47  ? 0.65457 0.80084 0.49564 0.03988  0.07281  -0.03683 47  ARG B CZ  
2583 N NH1 . ARG B 47  ? 0.64060 0.81978 0.49722 0.03458  0.08453  -0.02324 47  ARG B NH1 
2584 N NH2 . ARG B 47  ? 0.59820 0.70985 0.43602 0.05487  0.06459  -0.06525 47  ARG B NH2 
2585 N N   . GLU B 48  ? 0.45037 0.45119 0.35829 -0.00390 0.04633  0.04753  48  GLU B N   
2586 C CA  . GLU B 48  ? 0.46057 0.43323 0.37907 -0.00437 0.03813  0.05391  48  GLU B CA  
2587 C C   . GLU B 48  ? 0.47788 0.43039 0.38864 0.00238  0.03130  0.03222  48  GLU B C   
2588 O O   . GLU B 48  ? 0.45759 0.40435 0.36300 0.00095  0.02198  0.03427  48  GLU B O   
2589 C CB  . GLU B 48  ? 0.45412 0.40551 0.40060 -0.00670 0.04063  0.06540  48  GLU B CB  
2590 C CG  . GLU B 48  ? 0.45919 0.42291 0.41708 -0.01620 0.04270  0.09131  48  GLU B CG  
2591 C CD  . GLU B 48  ? 0.51689 0.45749 0.50148 -0.01908 0.04435  0.09663  48  GLU B CD  
2592 O OE1 . GLU B 48  ? 0.48359 0.40141 0.47715 -0.01243 0.04479  0.07991  48  GLU B OE1 
2593 O OE2 . GLU B 48  ? 0.53631 0.48249 0.53283 -0.02931 0.04384  0.11834  48  GLU B OE2 
2594 N N   . LEU B 49  ? 0.48526 0.42844 0.39668 0.00843  0.03424  0.01363  49  LEU B N   
2595 C CA  . LEU B 49  ? 0.48655 0.40875 0.39216 0.01321  0.02536  -0.00392 49  LEU B CA  
2596 C C   . LEU B 49  ? 0.55108 0.47867 0.43230 0.01542  0.01587  -0.01655 49  LEU B C   
2597 O O   . LEU B 49  ? 0.55116 0.46097 0.42822 0.01291  0.00329  -0.02070 49  LEU B O   
2598 C CB  . LEU B 49  ? 0.47078 0.38465 0.38289 0.01986  0.02943  -0.01872 49  LEU B CB  
2599 C CG  . LEU B 49  ? 0.47545 0.38078 0.41022 0.01672  0.03565  -0.00959 49  LEU B CG  
2600 C CD1 . LEU B 49  ? 0.41864 0.32529 0.35903 0.02175  0.04062  -0.02126 49  LEU B CD1 
2601 C CD2 . LEU B 49  ? 0.44723 0.33386 0.39049 0.01458  0.02837  -0.00647 49  LEU B CD2 
2602 N N   . ASP B 50  ? 0.50290 0.45784 0.36779 0.01939  0.02094  -0.02308 50  ASP B N   
2603 C CA  . ASP B 50  ? 0.54403 0.50785 0.38262 0.02310  0.01168  -0.03919 50  ASP B CA  
2604 C C   . ASP B 50  ? 0.54154 0.50523 0.37420 0.01282  0.00149  -0.02511 50  ASP B C   
2605 O O   . ASP B 50  ? 0.55469 0.50414 0.37377 0.01200  -0.01317 -0.03819 50  ASP B O   
2606 C CB  . ASP B 50  ? 0.48815 0.49501 0.31033 0.02879  0.02154  -0.04503 50  ASP B CB  
2607 C CG  . ASP B 50  ? 0.57479 0.58724 0.39700 0.04332  0.02777  -0.06783 50  ASP B CG  
2608 O OD1 . ASP B 50  ? 0.65060 0.62902 0.48376 0.04925  0.02228  -0.07999 50  ASP B OD1 
2609 O OD2 . ASP B 50  ? 0.63077 0.68669 0.44284 0.04894  0.03800  -0.07202 50  ASP B OD2 
2610 N N   . VAL B 51  ? 0.50141 0.48026 0.34570 0.00468  0.00729  0.00216  51  VAL B N   
2611 C CA  . VAL B 51  ? 0.52271 0.50519 0.36643 -0.00392 -0.00212 0.01934  51  VAL B CA  
2612 C C   . VAL B 51  ? 0.54672 0.49989 0.40100 -0.00662 -0.01347 0.01637  51  VAL B C   
2613 O O   . VAL B 51  ? 0.49679 0.44965 0.34070 -0.01248 -0.02717 0.01524  51  VAL B O   
2614 C CB  . VAL B 51  ? 0.50910 0.50510 0.37138 -0.00930 0.00512  0.05010  51  VAL B CB  
2615 C CG1 . VAL B 51  ? 0.51138 0.51190 0.37773 -0.01551 -0.00520 0.06891  51  VAL B CG1 
2616 C CG2 . VAL B 51  ? 0.52565 0.55700 0.37680 -0.01126 0.01394  0.05878  51  VAL B CG2 
2617 N N   . GLN B 52  ? 0.49424 0.42674 0.36924 -0.00392 -0.00860 0.01618  52  GLN B N   
2618 C CA  . GLN B 52  ? 0.52073 0.43463 0.40749 -0.00799 -0.01807 0.01758  52  GLN B CA  
2619 C C   . GLN B 52  ? 0.54420 0.43941 0.41559 -0.00971 -0.03270 -0.00222 52  GLN B C   
2620 O O   . GLN B 52  ? 0.51444 0.40382 0.38577 -0.01879 -0.04704 0.00196  52  GLN B O   
2621 C CB  . GLN B 52  ? 0.49441 0.39707 0.40408 -0.00427 -0.00893 0.02073  52  GLN B CB  
2622 C CG  . GLN B 52  ? 0.45905 0.37214 0.38702 -0.00240 0.00108  0.03867  52  GLN B CG  
2623 C CD  . GLN B 52  ? 0.47859 0.40508 0.41235 -0.00612 -0.00551 0.05670  52  GLN B CD  
2624 O OE1 . GLN B 52  ? 0.49892 0.43939 0.43112 -0.00697 -0.00429 0.07047  52  GLN B OE1 
2625 N NE2 . GLN B 52  ? 0.43420 0.36059 0.37583 -0.00916 -0.01333 0.05917  52  GLN B NE2 
2626 N N   . MET B 53  ? 0.53309 0.41874 0.39320 -0.00108 -0.03094 -0.02341 53  MET B N   
2627 C CA  . MET B 53  ? 0.58632 0.44685 0.43382 -0.00026 -0.04766 -0.04432 53  MET B CA  
2628 C C   . MET B 53  ? 0.57530 0.44153 0.39882 -0.00387 -0.06124 -0.05442 53  MET B C   
2629 O O   . MET B 53  ? 0.66458 0.50507 0.48023 -0.00802 -0.08078 -0.06780 53  MET B O   
2630 C CB  . MET B 53  ? 0.56013 0.41075 0.40428 0.01392  -0.04259 -0.06565 53  MET B CB  
2631 C CG  . MET B 53  ? 0.65617 0.49382 0.52302 0.01481  -0.03638 -0.05821 53  MET B CG  
2632 S SD  . MET B 53  ? 0.79851 0.63591 0.66680 0.03182  -0.02678 -0.07730 53  MET B SD  
2633 C CE  . MET B 53  ? 0.75793 0.57149 0.60607 0.04278  -0.04606 -0.10805 53  MET B CE  
2634 N N   . ALA B 54  ? 0.60442 0.50358 0.41637 -0.00377 -0.05323 -0.04731 54  ALA B N   
2635 C CA  . ALA B 54  ? 0.62544 0.53788 0.41235 -0.00795 -0.06566 -0.05589 54  ALA B CA  
2636 C C   . ALA B 54  ? 0.64739 0.55863 0.44038 -0.02400 -0.08015 -0.03782 54  ALA B C   
2637 O O   . ALA B 54  ? 0.65568 0.57170 0.42842 -0.03025 -0.09565 -0.04694 54  ALA B O   
2638 C CB  . ALA B 54  ? 0.58305 0.53916 0.35621 -0.00415 -0.05188 -0.04919 54  ALA B CB  
2639 N N   . ILE B 55  ? 0.61727 0.52629 0.43732 -0.03008 -0.07581 -0.01398 55  ILE B N   
2640 C CA  . ILE B 55  ? 0.64040 0.55951 0.47027 -0.04381 -0.08719 0.00642  55  ILE B CA  
2641 C C   . ILE B 55  ? 0.71244 0.60544 0.53757 -0.05542 -0.11049 -0.00474 55  ILE B C   
2642 O O   . ILE B 55  ? 0.72650 0.59031 0.56060 -0.05491 -0.11434 -0.01275 55  ILE B O   
2643 C CB  . ILE B 55  ? 0.62821 0.55535 0.48932 -0.04335 -0.07556 0.03075  55  ILE B CB  
2644 C CG1 . ILE B 55  ? 0.57936 0.52858 0.44648 -0.03477 -0.05810 0.04472  55  ILE B CG1 
2645 C CG2 . ILE B 55  ? 0.66091 0.60098 0.53578 -0.05615 -0.08832 0.04959  55  ILE B CG2 
2646 C CD1 . ILE B 55  ? 0.56620 0.51506 0.46304 -0.02904 -0.04552 0.05979  55  ILE B CD1 
2647 N N   . PRO B 56  ? 0.75350 0.65533 0.56559 -0.06754 -0.12831 -0.00412 56  PRO B N   
2648 C CA  . PRO B 56  ? 0.81593 0.69022 0.62602 -0.08238 -0.15397 -0.01228 56  PRO B CA  
2649 C C   . PRO B 56  ? 0.89626 0.76828 0.73720 -0.09340 -0.15593 0.01138  56  PRO B C   
2650 O O   . PRO B 56  ? 0.88719 0.79008 0.74889 -0.09246 -0.14212 0.03607  56  PRO B O   
2651 C CB  . PRO B 56  ? 0.80580 0.70195 0.59936 -0.09483 -0.17010 -0.00971 56  PRO B CB  
2652 C CG  . PRO B 56  ? 0.76497 0.69393 0.54194 -0.08231 -0.15346 -0.01060 56  PRO B CG  
2653 C CD  . PRO B 56  ? 0.69795 0.63624 0.49687 -0.06990 -0.12770 0.00579  56  PRO B CD  
2654 N N   . PRO B 57  ? 0.94258 0.78078 0.78820 -0.10367 -0.17383 0.00527  57  PRO B N   
2655 C CA  . PRO B 57  ? 0.98136 0.82319 0.85567 -0.11414 -0.17401 0.02876  57  PRO B CA  
2656 C C   . PRO B 57  ? 1.01428 0.89368 0.90468 -0.13156 -0.18132 0.05668  57  PRO B C   
2657 O O   . PRO B 57  ? 0.96467 0.84761 0.84433 -0.14575 -0.20090 0.05614  57  PRO B O   
2658 C CB  . PRO B 57  ? 1.00275 0.79703 0.87464 -0.12402 -0.19745 0.01630  57  PRO B CB  
2659 C CG  . PRO B 57  ? 0.97147 0.73394 0.81457 -0.11038 -0.20396 -0.01971 57  PRO B CG  
2660 C CD  . PRO B 57  ? 0.97044 0.76583 0.79553 -0.10632 -0.19701 -0.02335 57  PRO B CD  
2661 N N   . PRO B 58  ? 0.90747 1.23802 0.88408 -0.10351 -0.04051 -0.18016 58  PRO B N   
2662 C CA  . PRO B 58  ? 0.91894 1.30060 0.92456 -0.10479 -0.06136 -0.19393 58  PRO B CA  
2663 C C   . PRO B 58  ? 0.92407 1.30829 0.96552 -0.12953 -0.02979 -0.25095 58  PRO B C   
2664 O O   . PRO B 58  ? 0.92096 1.25146 0.96808 -0.14181 0.01183  -0.27306 58  PRO B O   
2665 C CB  . PRO B 58  ? 0.91108 1.24675 0.93043 -0.07925 -0.07472 -0.15259 58  PRO B CB  
2666 C CG  . PRO B 58  ? 0.93857 1.22226 0.92771 -0.06333 -0.07313 -0.11228 58  PRO B CG  
2667 C CD  . PRO B 58  ? 0.93894 1.20083 0.91111 -0.07909 -0.04222 -0.13555 58  PRO B CD  
2668 N N   . LYS B 59  ? 0.79931 1.24797 0.87106 -0.13587 -0.04846 -0.27441 59  LYS B N   
2669 C CA  . LYS B 59  ? 0.79949 1.25427 0.91427 -0.16048 -0.01758 -0.33196 59  LYS B CA  
2670 C C   . LYS B 59  ? 0.70936 1.08846 0.85194 -0.15187 0.00476  -0.32370 59  LYS B C   
2671 O O   . LYS B 59  ? 0.73172 1.07669 0.90110 -0.17091 0.04759  -0.36292 59  LYS B O   
2672 C CB  . LYS B 59  ? 0.70744 1.27101 0.84969 -0.17231 -0.04661 -0.36634 59  LYS B CB  
2673 N N   . GLY B 60  ? 0.72229 1.07278 0.85868 -0.12515 -0.01919 -0.27461 60  GLY B N   
2674 C CA  . GLY B 60  ? 0.62860 0.91931 0.78840 -0.11878 -0.00150 -0.26865 60  GLY B CA  
2675 C C   . GLY B 60  ? 0.64569 0.84098 0.77797 -0.11108 0.02999  -0.24505 60  GLY B C   
2676 O O   . GLY B 60  ? 0.60390 0.77622 0.70472 -0.10837 0.03778  -0.23146 60  GLY B O   
2677 N N   . GLU B 61  ? 0.56055 0.70390 0.70641 -0.10720 0.04796  -0.24037 61  GLU B N   
2678 C CA  . GLU B 61  ? 0.57362 0.63178 0.69242 -0.09783 0.07579  -0.21561 61  GLU B CA  
2679 C C   . GLU B 61  ? 0.59171 0.63359 0.67279 -0.07502 0.05038  -0.16716 61  GLU B C   
2680 O O   . GLU B 61  ? 0.55236 0.62790 0.63386 -0.06264 0.01435  -0.14466 61  GLU B O   
2681 C CB  . GLU B 61  ? 0.58253 0.60232 0.71741 -0.09758 0.09183  -0.21666 61  GLU B CB  
2682 C CG  . GLU B 61  ? 0.60204 0.54676 0.70065 -0.08295 0.10810  -0.18130 61  GLU B CG  
2683 C CD  . GLU B 61  ? 0.67889 0.59279 0.78763 -0.08504 0.12249  -0.18337 61  GLU B CD  
2684 O OE1 . GLU B 61  ? 0.62410 0.56986 0.75428 -0.08118 0.09629  -0.18058 61  GLU B OE1 
2685 O OE2 . GLU B 61  ? 0.72309 0.57896 0.81945 -0.09048 0.16314  -0.18689 61  GLU B OE2 
2686 N N   . ARG B 62  ? 0.60561 0.59628 0.65964 -0.06895 0.07154  -0.15145 62  ARG B N   
2687 C CA  . ARG B 62  ? 0.54796 0.51613 0.57123 -0.04788 0.05365  -0.10912 62  ARG B CA  
2688 C C   . ARG B 62  ? 0.58906 0.48926 0.59398 -0.03823 0.07991  -0.09117 62  ARG B C   
2689 O O   . ARG B 62  ? 0.63828 0.50334 0.64075 -0.04149 0.11301  -0.09808 62  ARG B O   
2690 C CB  . ARG B 62  ? 0.60124 0.59026 0.61012 -0.04708 0.04638  -0.10467 62  ARG B CB  
2691 C CG  . ARG B 62  ? 0.62583 0.67998 0.63563 -0.04737 0.01027  -0.10141 62  ARG B CG  
2692 C CD  . ARG B 62  ? 0.77897 0.87311 0.78507 -0.06352 0.01601  -0.12709 62  ARG B CD  
2693 N NE  . ARG B 62  ? 0.81885 0.88068 0.80775 -0.06121 0.03489  -0.11981 62  ARG B NE  
2694 C CZ  . ARG B 62  ? 0.79988 0.86876 0.76788 -0.05086 0.01827  -0.09436 62  ARG B CZ  
2695 N NH1 . ARG B 62  ? 0.84182 0.94296 0.80016 -0.04076 -0.01562 -0.06964 62  ARG B NH1 
2696 N NH2 . ARG B 62  ? 0.81646 0.85759 0.77813 -0.05028 0.03935  -0.09351 62  ARG B NH2 
2697 N N   . LEU B 63  ? 0.56285 0.44683 0.55561 -0.02600 0.06622  -0.06743 63  LEU B N   
2698 C CA  . LEU B 63  ? 0.56190 0.39077 0.53399 -0.01938 0.08983  -0.05344 63  LEU B CA  
2699 C C   . LEU B 63  ? 0.62106 0.41416 0.56943 -0.00554 0.10467  -0.03093 63  LEU B C   
2700 O O   . LEU B 63  ? 0.64890 0.39864 0.59361 -0.00649 0.14112  -0.03243 63  LEU B O   
2701 C CB  . LEU B 63  ? 0.56425 0.39458 0.52584 -0.01096 0.06872  -0.03548 63  LEU B CB  
2702 C CG  . LEU B 63  ? 0.59496 0.44583 0.58630 -0.02329 0.06488  -0.05679 63  LEU B CG  
2703 C CD1 . LEU B 63  ? 0.49044 0.34578 0.47828 -0.01617 0.04563  -0.04143 63  LEU B CD1 
2704 C CD2 . LEU B 63  ? 0.58286 0.40080 0.58102 -0.03770 0.10316  -0.07997 63  LEU B CD2 
2705 N N   . LEU B 64  ? 0.58856 0.39825 0.52564 0.00836  0.07939  -0.00909 64  LEU B N   
2706 C CA  . LEU B 64  ? 0.64517 0.42741 0.56882 0.02363  0.09123  0.01203  64  LEU B CA  
2707 C C   . LEU B 64  ? 0.65594 0.43945 0.60010 0.01416  0.11324  -0.00773 64  LEU B C   
2708 O O   . LEU B 64  ? 0.68210 0.42560 0.63056 0.01848  0.14724  -0.00446 64  LEU B O   
2709 C CB  . LEU B 64  ? 0.63130 0.43436 0.54291 0.03999  0.05861  0.03710  64  LEU B CB  
2710 C CG  . LEU B 64  ? 0.66623 0.44779 0.57060 0.05887  0.06710  0.06004  64  LEU B CG  
2711 C CD1 . LEU B 64  ? 0.68872 0.43395 0.56788 0.07475  0.07914  0.08489  64  LEU B CD1 
2712 C CD2 . LEU B 64  ? 0.66795 0.48104 0.57499 0.06883  0.03797  0.07231  64  LEU B CD2 
2713 N N   . ALA B 65  ? 0.63035 0.46030 0.58787 0.00112  0.09647  -0.02794 65  ALA B N   
2714 C CA  . ALA B 65  ? 0.63193 0.47203 0.60436 -0.00958 0.11436  -0.04843 65  ALA B CA  
2715 C C   . ALA B 65  ? 0.67022 0.48735 0.66522 -0.02716 0.15829  -0.08086 65  ALA B C   
2716 O O   . ALA B 65  ? 0.61624 0.41507 0.62687 -0.03126 0.18909  -0.09206 65  ALA B O   
2717 C CB  . ALA B 65  ? 0.62268 0.52338 0.59634 -0.02147 0.08646  -0.06289 65  ALA B CB  
2718 N N   . ASP B 66  ? 0.62260 0.43904 0.62594 -0.03887 0.16599  -0.09898 66  ASP B N   
2719 C CA  . ASP B 66  ? 0.66397 0.46098 0.69536 -0.05911 0.21135  -0.13588 66  ASP B CA  
2720 C C   . ASP B 66  ? 0.72087 0.44373 0.75290 -0.04730 0.25644  -0.11722 66  ASP B C   
2721 O O   . ASP B 66  ? 0.76848 0.46581 0.82997 -0.06346 0.30387  -0.14669 66  ASP B O   
2722 C CB  . ASP B 66  ? 0.67761 0.49308 0.72275 -0.07405 0.20910  -0.16039 66  ASP B CB  
2723 C CG  . ASP B 66  ? 0.66488 0.55979 0.72448 -0.08958 0.17546  -0.18898 66  ASP B CG  
2724 O OD1 . ASP B 66  ? 0.63724 0.57219 0.69058 -0.09162 0.15706  -0.19165 66  ASP B OD1 
2725 O OD2 . ASP B 66  ? 0.67638 0.59531 0.75398 -0.09898 0.16794  -0.20754 66  ASP B OD2 
2726 N N   . LYS B 67  ? 0.74130 0.43176 0.74404 -0.01946 0.24425  -0.06939 67  LYS B N   
2727 C CA  . LYS B 67  ? 0.75834 0.38300 0.75840 -0.00191 0.28274  -0.04168 67  LYS B CA  
2728 C C   . LYS B 67  ? 0.75074 0.36409 0.77126 0.00701  0.29972  -0.03566 67  LYS B C   
2729 O O   . LYS B 67  ? 0.77541 0.33317 0.80653 0.02141  0.33914  -0.01516 67  LYS B O   
2730 C CB  . LYS B 67  ? 0.80193 0.40710 0.75996 0.02499  0.25964  0.00686  67  LYS B CB  
2731 C CG  . LYS B 67  ? 0.81153 0.42073 0.75098 0.01565  0.24994  0.00071  67  LYS B CG  
2732 C CD  . LYS B 67  ? 0.82146 0.43245 0.71881 0.03702  0.21777  0.03978  67  LYS B CD  
2733 C CE  . LYS B 67  ? 0.90797 0.48814 0.78140 0.03267  0.23573  0.04395  67  LYS B CE  
2734 N NZ  . LYS B 67  ? 0.94666 0.53856 0.84823 0.00388  0.24918  -0.00032 67  LYS B NZ  
2735 N N   . TYR B 68  ? 0.73387 0.39621 0.76192 -0.00048 0.27420  -0.05129 68  TYR B N   
2736 C CA  . TYR B 68  ? 0.73809 0.39495 0.78539 0.00836  0.28578  -0.04513 68  TYR B CA  
2737 C C   . TYR B 68  ? 0.71405 0.39997 0.79381 -0.02278 0.30880  -0.09765 68  TYR B C   
2738 O O   . TYR B 68  ? 0.70132 0.42891 0.78158 -0.04885 0.30043  -0.13541 68  TYR B O   
2739 C CB  . TYR B 68  ? 0.69970 0.38914 0.72378 0.02761  0.23664  -0.01513 68  TYR B CB  
2740 C CG  . TYR B 68  ? 0.80521 0.47212 0.79971 0.05671  0.21662  0.03179  68  TYR B CG  
2741 C CD1 . TYR B 68  ? 0.91324 0.52667 0.91175 0.07904  0.24691  0.06233  68  TYR B CD1 
2742 C CD2 . TYR B 68  ? 0.73511 0.43494 0.69950 0.06058  0.17160  0.04389  68  TYR B CD2 
2743 C CE1 . TYR B 68  ? 0.95218 0.55353 0.91704 0.10445  0.22731  0.10418  68  TYR B CE1 
2744 C CE2 . TYR B 68  ? 0.78095 0.46588 0.71802 0.08297  0.15657  0.07977  68  TYR B CE2 
2745 C CZ  . TYR B 68  ? 0.88284 0.52215 0.81527 0.10505  0.18164  0.11057  68  TYR B CZ  
2746 O OH  . TYR B 68  ? 0.95790 0.59149 0.85642 0.12660  0.16425  0.14595  68  TYR B OH  
2747 N N   . PRO B 69  ? 0.75185 0.42047 0.86200 -0.02142 0.33931  -0.10336 69  PRO B N   
2748 C CA  . PRO B 69  ? 0.76860 0.47058 0.90820 -0.05485 0.36364  -0.15888 69  PRO B CA  
2749 C C   . PRO B 69  ? 0.72054 0.49613 0.83202 -0.06821 0.31594  -0.17288 69  PRO B C   
2750 O O   . PRO B 69  ? 0.66865 0.46027 0.74783 -0.04825 0.27002  -0.13624 69  PRO B O   
2751 C CB  . PRO B 69  ? 0.75678 0.41995 0.93458 -0.04346 0.40254  -0.15115 69  PRO B CB  
2752 C CG  . PRO B 69  ? 0.79928 0.40006 0.97594 -0.00588 0.41117  -0.09570 69  PRO B CG  
2753 C CD  . PRO B 69  ? 0.75779 0.37607 0.88182 0.01049  0.35733  -0.06119 69  PRO B CD  
2754 N N   . PRO B 70  ? 0.73001 0.55330 0.85313 -0.10234 0.32759  -0.22579 70  PRO B N   
2755 C CA  . PRO B 70  ? 0.72018 0.61712 0.81002 -0.11448 0.28213  -0.23525 70  PRO B CA  
2756 C C   . PRO B 70  ? 0.73435 0.63918 0.80644 -0.09910 0.25969  -0.20636 70  PRO B C   
2757 O O   . PRO B 70  ? 0.74303 0.69441 0.78081 -0.09838 0.21697  -0.19425 70  PRO B O   
2758 C CB  . PRO B 70  ? 0.70146 0.64576 0.81062 -0.15492 0.30934  -0.30090 70  PRO B CB  
2759 C CG  . PRO B 70  ? 0.74024 0.63902 0.89394 -0.16611 0.36317  -0.32925 70  PRO B CG  
2760 C CD  . PRO B 70  ? 0.74507 0.56058 0.91222 -0.13258 0.38439  -0.28084 70  PRO B CD  
2761 N N   . HIS B 71  ? 0.71639 0.57755 0.81533 -0.08633 0.28921  -0.19473 71  HIS B N   
2762 C CA  . HIS B 71  ? 0.70875 0.57854 0.79847 -0.07247 0.27043  -0.17086 71  HIS B CA  
2763 C C   . HIS B 71  ? 0.70663 0.56357 0.77302 -0.03850 0.22829  -0.11644 71  HIS B C   
2764 O O   . HIS B 71  ? 0.72317 0.58955 0.78487 -0.02656 0.21083  -0.09699 71  HIS B O   
2765 C CB  . HIS B 71  ? 0.67525 0.50717 0.81226 -0.07000 0.31773  -0.17997 71  HIS B CB  
2766 C CG  . HIS B 71  ? 0.75614 0.52148 0.92528 -0.04254 0.34404  -0.15070 71  HIS B CG  
2767 N ND1 . HIS B 71  ? 0.82512 0.56538 0.98768 -0.00431 0.31906  -0.09680 71  HIS B ND1 
2768 C CD2 . HIS B 71  ? 0.77169 0.49194 0.97888 -0.04731 0.39445  -0.16633 71  HIS B CD2 
2769 C CE1 . HIS B 71  ? 0.87964 0.56423 1.06892 0.01549  0.34991  -0.07599 71  HIS B CE1 
2770 N NE2 . HIS B 71  ? 0.88248 0.54892 1.10064 -0.00947 0.39838  -0.11581 71  HIS B NE2 
2771 N N   . PHE B 72  ? 0.69916 0.53759 0.75314 -0.02582 0.21461  -0.09648 72  PHE B N   
2772 C CA  . PHE B 72  ? 0.68757 0.51937 0.71901 0.00169  0.17671  -0.05218 72  PHE B CA  
2773 C C   . PHE B 72  ? 0.61664 0.49656 0.62064 -0.00166 0.13500  -0.04545 72  PHE B C   
2774 O O   . PHE B 72  ? 0.58121 0.49920 0.56874 -0.02038 0.12131  -0.06413 72  PHE B O   
2775 C CB  . PHE B 72  ? 0.63174 0.44277 0.65187 0.00613  0.17433  -0.04384 72  PHE B CB  
2776 C CG  . PHE B 72  ? 0.66986 0.47163 0.66794 0.03165  0.14249  -0.00341 72  PHE B CG  
2777 C CD1 . PHE B 72  ? 0.69992 0.47418 0.70357 0.05899  0.14379  0.02943  72  PHE B CD1 
2778 C CD2 . PHE B 72  ? 0.65191 0.47541 0.62759 0.02793  0.11317  -0.00047 72  PHE B CD2 
2779 C CE1 . PHE B 72  ? 0.70648 0.48122 0.68794 0.07929  0.11449  0.06090  72  PHE B CE1 
2780 C CE2 . PHE B 72  ? 0.64483 0.46176 0.60258 0.04713  0.08847  0.02990  72  PHE B CE2 
2781 C CZ  . PHE B 72  ? 0.66139 0.45638 0.61923 0.07143  0.08866  0.05879  72  PHE B CZ  
2782 N N   . LYS B 73  ? 0.57535 0.45481 0.57759 0.01783  0.11545  -0.01738 73  LYS B N   
2783 C CA  . LYS B 73  ? 0.56632 0.48324 0.54929 0.01572  0.08395  -0.00883 73  LYS B CA  
2784 C C   . LYS B 73  ? 0.54009 0.45505 0.51098 0.03423  0.05252  0.02053  73  LYS B C   
2785 O O   . LYS B 73  ? 0.50715 0.40316 0.48754 0.05507  0.04844  0.04152  73  LYS B O   
2786 C CB  . LYS B 73  ? 0.55363 0.47554 0.55140 0.01786  0.09206  -0.00844 73  LYS B CB  
2787 C CG  . LYS B 73  ? 0.65321 0.57865 0.66562 -0.00390 0.12771  -0.04259 73  LYS B CG  
2788 C CD  . LYS B 73  ? 0.65927 0.62966 0.64217 -0.03166 0.12159  -0.06710 73  LYS B CD  
2789 C CE  . LYS B 73  ? 0.71721 0.69780 0.71327 -0.05765 0.15940  -0.10784 73  LYS B CE  
2790 N NZ  . LYS B 73  ? 0.76104 0.79511 0.72080 -0.08159 0.14905  -0.12456 73  LYS B NZ  
2791 N N   . TYR B 74  ? 0.48339 0.42210 0.43639 0.02652  0.03092  0.02062  74  TYR B N   
2792 C CA  . TYR B 74  ? 0.47817 0.41335 0.42473 0.03917  0.00777  0.04070  74  TYR B CA  
2793 C C   . TYR B 74  ? 0.46597 0.43428 0.40297 0.03119  -0.01457 0.04289  74  TYR B C   
2794 O O   . TYR B 74  ? 0.48264 0.47427 0.41322 0.01640  -0.01360 0.02743  74  TYR B O   
2795 C CB  . TYR B 74  ? 0.50203 0.41052 0.44700 0.04120  0.01860  0.03788  74  TYR B CB  
2796 C CG  . TYR B 74  ? 0.53456 0.44046 0.47116 0.04923  -0.00064 0.05200  74  TYR B CG  
2797 C CD1 . TYR B 74  ? 0.51395 0.41354 0.44821 0.06613  -0.01314 0.07221  74  TYR B CD1 
2798 C CD2 . TYR B 74  ? 0.50519 0.41944 0.44021 0.03827  -0.00446 0.04078  74  TYR B CD2 
2799 C CE1 . TYR B 74  ? 0.49300 0.39362 0.41980 0.06904  -0.02696 0.07869  74  TYR B CE1 
2800 C CE2 . TYR B 74  ? 0.52295 0.43363 0.45488 0.04338  -0.01737 0.04993  74  TYR B CE2 
2801 C CZ  . TYR B 74  ? 0.51243 0.41542 0.43835 0.05740  -0.02749 0.06776  74  TYR B CZ  
2802 O OH  . TYR B 74  ? 0.53947 0.44174 0.46221 0.05835  -0.03653 0.07077  74  TYR B OH  
2803 N N   . VAL B 75  ? 0.41963 0.39303 0.35926 0.04135  -0.03341 0.06168  75  VAL B N   
2804 C CA  . VAL B 75  ? 0.40726 0.40417 0.34582 0.03843  -0.05172 0.07016  75  VAL B CA  
2805 C C   . VAL B 75  ? 0.40752 0.39302 0.35594 0.04729  -0.06249 0.07920  75  VAL B C   
2806 O O   . VAL B 75  ? 0.38755 0.36553 0.34344 0.05644  -0.06601 0.08737  75  VAL B O   
2807 C CB  . VAL B 75  ? 0.42240 0.43620 0.36054 0.03845  -0.05659 0.08215  75  VAL B CB  
2808 C CG1 . VAL B 75  ? 0.40195 0.43523 0.34282 0.03903  -0.07203 0.09731  75  VAL B CG1 
2809 C CG2 . VAL B 75  ? 0.44558 0.47245 0.36963 0.02654  -0.04262 0.06977  75  VAL B CG2 
2810 N N   . PRO B 76  ? 0.39046 0.37800 0.34183 0.04335  -0.06650 0.07411  76  PRO B N   
2811 C CA  . PRO B 76  ? 0.40358 0.38049 0.36487 0.04834  -0.07249 0.07812  76  PRO B CA  
2812 C C   . PRO B 76  ? 0.36821 0.36028 0.34937 0.05105  -0.08454 0.09045  76  PRO B C   
2813 O O   . PRO B 76  ? 0.36894 0.38010 0.35471 0.04986  -0.08990 0.09959  76  PRO B O   
2814 C CB  . PRO B 76  ? 0.38975 0.36467 0.35329 0.04060  -0.06790 0.06464  76  PRO B CB  
2815 C CG  . PRO B 76  ? 0.39892 0.40382 0.36435 0.03297  -0.07237 0.05955  76  PRO B CG  
2816 C CD  . PRO B 76  ? 0.40436 0.41136 0.35432 0.03244  -0.06604 0.06121  76  PRO B CD  
2817 N N   . ASN B 77  ? 0.37311 0.34650 0.36175 -0.00888 -0.01092 -0.01426 77  ASN B N   
2818 C CA  . ASN B 77  ? 0.38320 0.35994 0.37225 -0.00790 -0.00595 -0.00827 77  ASN B CA  
2819 C C   . ASN B 77  ? 0.38618 0.35934 0.35937 -0.00166 -0.00228 -0.00557 77  ASN B C   
2820 O O   . ASN B 77  ? 0.37868 0.35126 0.34431 0.00244  -0.00556 -0.00387 77  ASN B O   
2821 C CB  . ASN B 77  ? 0.36804 0.35023 0.36537 -0.00903 -0.01101 -0.00717 77  ASN B CB  
2822 C CG  . ASN B 77  ? 0.40640 0.39025 0.40151 -0.00752 -0.02120 -0.01175 77  ASN B CG  
2823 O OD1 . ASN B 77  ? 0.43757 0.42417 0.44315 -0.01249 -0.02655 -0.01524 77  ASN B OD1 
2824 N ND2 . ASN B 77  ? 0.38978 0.37194 0.37145 -0.00098 -0.02427 -0.01145 77  ASN B ND2 
2825 N N   . VAL B 78  ? 0.40937 0.38122 0.37776 -0.00045 0.00491  -0.00440 78  VAL B N   
2826 C CA  . VAL B 78  ? 0.43283 0.40223 0.38502 0.00583  0.00953  -0.00151 78  VAL B CA  
2827 C C   . VAL B 78  ? 0.38807 0.35617 0.33829 0.00598  0.01446  0.00662  78  VAL B C   
2828 O O   . VAL B 78  ? 0.40524 0.37026 0.34039 0.01164  0.01724  0.01066  78  VAL B O   
2829 C CB  . VAL B 78  ? 0.40213 0.37351 0.35236 0.00731  0.01704  -0.00187 78  VAL B CB  
2830 C CG1 . VAL B 78  ? 0.43390 0.40221 0.38023 0.01026  0.01143  -0.01041 78  VAL B CG1 
2831 C CG2 . VAL B 78  ? 0.37396 0.35063 0.34046 0.00074  0.02304  0.00148  78  VAL B CG2 
2832 N N   . ALA B 79  ? 0.40393 0.37280 0.36749 0.00056  0.01543  0.00914  79  ALA B N   
2833 C CA  . ALA B 79  ? 0.41462 0.37866 0.37638 0.00071  0.01962  0.01633  79  ALA B CA  
2834 C C   . ALA B 79  ? 0.42961 0.38982 0.38039 0.00737  0.01405  0.01836  79  ALA B C   
2835 O O   . ALA B 79  ? 0.43563 0.38900 0.37852 0.01014  0.01806  0.02559  79  ALA B O   
2836 C CB  . ALA B 79  ? 0.39754 0.36188 0.37465 -0.00545 0.02050  0.01638  79  ALA B CB  
2837 N N   . THR B 80  ? 0.38154 0.34595 0.33221 0.00991  0.00452  0.01257  80  THR B N   
2838 C CA  . THR B 80  ? 0.40818 0.37169 0.34984 0.01683  -0.00217 0.01411  80  THR B CA  
2839 C C   . THR B 80  ? 0.46018 0.42071 0.38035 0.02452  -0.00387 0.01446  80  THR B C   
2840 O O   . THR B 80  ? 0.49551 0.45368 0.40402 0.03174  -0.00770 0.01814  80  THR B O   
2841 C CB  . THR B 80  ? 0.42246 0.39455 0.37600 0.01570  -0.01251 0.00798  80  THR B CB  
2842 O OG1 . THR B 80  ? 0.45592 0.43082 0.40837 0.01402  -0.01813 0.00047  80  THR B OG1 
2843 C CG2 . THR B 80  ? 0.41128 0.38754 0.38396 0.00939  -0.01015 0.00774  80  THR B CG2 
2844 N N   . THR B 81  ? 0.44953 0.41012 0.36288 0.02448  -0.00131 0.01061  81  THR B N   
2845 C CA  . THR B 81  ? 0.47129 0.42922 0.36189 0.03300  -0.00283 0.00944  81  THR B CA  
2846 C C   . THR B 81  ? 0.47178 0.42712 0.35099 0.03526  0.00984  0.01535  81  THR B C   
2847 O O   . THR B 81  ? 0.47134 0.42447 0.32864 0.04385  0.01074  0.01615  81  THR B O   
2848 C CB  . THR B 81  ? 0.47040 0.43016 0.35925 0.03351  -0.01235 -0.00222 81  THR B CB  
2849 O OG1 . THR B 81  ? 0.44766 0.40849 0.34971 0.02698  -0.00794 -0.00581 81  THR B OG1 
2850 C CG2 . THR B 81  ? 0.46760 0.43189 0.36662 0.03158  -0.02558 -0.00750 81  THR B CG2 
2851 N N   . CYS B 82  ? 0.44523 0.40220 0.33858 0.02814  0.01949  0.01934  82  CYS B N   
2852 C CA  . CYS B 82  ? 0.46866 0.42700 0.35626 0.02890  0.03209  0.02528  82  CYS B CA  
2853 C C   . CYS B 82  ? 0.46018 0.41518 0.35498 0.02365  0.04106  0.03642  82  CYS B C   
2854 O O   . CYS B 82  ? 0.45476 0.41238 0.36869 0.01488  0.04475  0.03689  82  CYS B O   
2855 C CB  . CYS B 82  ? 0.46313 0.42812 0.36248 0.02515  0.03480  0.01904  82  CYS B CB  
2856 S SG  . CYS B 82  ? 0.48609 0.44982 0.37647 0.03092  0.02343  0.00545  82  CYS B SG  
2857 N N   . PRO B 83  ? 0.44412 0.39204 0.32333 0.02885  0.04426  0.04556  83  PRO B N   
2858 C CA  . PRO B 83  ? 0.47791 0.41874 0.36362 0.02330  0.05247  0.05664  83  PRO B CA  
2859 C C   . PRO B 83  ? 0.47583 0.42238 0.37589 0.01457  0.06397  0.06053  83  PRO B C   
2860 O O   . PRO B 83  ? 0.46317 0.40463 0.37694 0.00620  0.06773  0.06551  83  PRO B O   
2861 C CB  . PRO B 83  ? 0.48861 0.42132 0.35010 0.03230  0.05598  0.06684  83  PRO B CB  
2862 C CG  . PRO B 83  ? 0.52736 0.46216 0.37197 0.04258  0.04505  0.05938  83  PRO B CG  
2863 C CD  . PRO B 83  ? 0.50030 0.44509 0.35390 0.04039  0.04013  0.04628  83  PRO B CD  
2864 N N   . THR B 84  ? 0.45499 0.41217 0.35242 0.01672  0.06940  0.05817  84  THR B N   
2865 C CA  . THR B 84  ? 0.48003 0.44645 0.39364 0.00884  0.08011  0.06204  84  THR B CA  
2866 C C   . THR B 84  ? 0.46088 0.43171 0.39862 -0.00039 0.07507  0.05466  84  THR B C   
2867 O O   . THR B 84  ? 0.44300 0.41601 0.39775 -0.00995 0.08031  0.05875  84  THR B O   
2868 C CB  . THR B 84  ? 0.51180 0.49040 0.41697 0.01553  0.08706  0.06061  84  THR B CB  
2869 O OG1 . THR B 84  ? 0.51623 0.49165 0.39867 0.02348  0.09476  0.06992  84  THR B OG1 
2870 C CG2 . THR B 84  ? 0.45723 0.45005 0.38426 0.00753  0.09633  0.06269  84  THR B CG2 
2871 N N   . PHE B 85  ? 0.44442 0.41631 0.38376 0.00202  0.06464  0.04396  85  PHE B N   
2872 C CA  . PHE B 85  ? 0.41918 0.39441 0.37860 -0.00567 0.05988  0.03790  85  PHE B CA  
2873 C C   . PHE B 85  ? 0.43138 0.39671 0.39777 -0.01130 0.05691  0.04051  85  PHE B C   
2874 O O   . PHE B 85  ? 0.41096 0.37720 0.39276 -0.01968 0.05914  0.04131  85  PHE B O   
2875 C CB  . PHE B 85  ? 0.42321 0.40049 0.38196 -0.00201 0.05029  0.02752  85  PHE B CB  
2876 C CG  . PHE B 85  ? 0.39585 0.37686 0.37265 -0.00872 0.04620  0.02240  85  PHE B CG  
2877 C CD1 . PHE B 85  ? 0.40794 0.39878 0.39573 -0.01111 0.04930  0.02013  85  PHE B CD1 
2878 C CD2 . PHE B 85  ? 0.38707 0.36267 0.36914 -0.01155 0.03950  0.02027  85  PHE B CD2 
2879 C CE1 . PHE B 85  ? 0.37557 0.36965 0.37768 -0.01630 0.04506  0.01590  85  PHE B CE1 
2880 C CE2 . PHE B 85  ? 0.41242 0.39162 0.40831 -0.01666 0.03642  0.01606  85  PHE B CE2 
2881 C CZ  . PHE B 85  ? 0.37762 0.36551 0.38270 -0.01909 0.03896  0.01402  85  PHE B CZ  
2882 N N   . ARG B 86  ? 0.42222 0.37807 0.37688 -0.00596 0.05147  0.04146  86  ARG B N   
2883 C CA  . ARG B 86  ? 0.45589 0.40192 0.41578 -0.00861 0.04781  0.04269  86  ARG B CA  
2884 C C   . ARG B 86  ? 0.46253 0.39967 0.42647 -0.01473 0.05564  0.05136  86  ARG B C   
2885 O O   . ARG B 86  ? 0.48264 0.41420 0.45830 -0.02091 0.05423  0.04978  86  ARG B O   
2886 C CB  . ARG B 86  ? 0.45701 0.39695 0.40306 0.00018  0.04090  0.04301  86  ARG B CB  
2887 C CG  . ARG B 86  ? 0.47492 0.40473 0.42439 0.00042  0.03746  0.04476  86  ARG B CG  
2888 C CD  . ARG B 86  ? 0.48672 0.41565 0.42566 0.01002  0.02907  0.04379  86  ARG B CD  
2889 N NE  . ARG B 86  ? 0.45463 0.37606 0.37430 0.01750  0.03134  0.05217  86  ARG B NE  
2890 C CZ  . ARG B 86  ? 0.49514 0.42146 0.39956 0.02433  0.02887  0.05153  86  ARG B CZ  
2891 N NH1 . ARG B 86  ? 0.43190 0.36922 0.33863 0.02415  0.02380  0.04237  86  ARG B NH1 
2892 N NH2 . ARG B 86  ? 0.51278 0.43127 0.39775 0.03193  0.03136  0.06028  86  ARG B NH2 
2893 N N   . ASN B 87  ? 0.45686 0.39203 0.41098 -0.01334 0.06412  0.06058  87  ASN B N   
2894 C CA  . ASN B 87  ? 0.46459 0.38864 0.42154 -0.01961 0.07189  0.07078  87  ASN B CA  
2895 C C   . ASN B 87  ? 0.46436 0.39810 0.43764 -0.03002 0.08041  0.07337  87  ASN B C   
2896 O O   . ASN B 87  ? 0.52096 0.44547 0.50231 -0.03847 0.08540  0.08013  87  ASN B O   
2897 C CB  . ASN B 87  ? 0.46380 0.37862 0.39998 -0.01231 0.07734  0.08219  87  ASN B CB  
2898 C CG  . ASN B 87  ? 0.50271 0.40656 0.42409 -0.00232 0.06870  0.08161  87  ASN B CG  
2899 O OD1 . ASN B 87  ? 0.51639 0.41266 0.44496 -0.00312 0.06183  0.07722  87  ASN B OD1 
2900 N ND2 . ASN B 87  ? 0.51986 0.42399 0.41999 0.00814  0.06877  0.08578  87  ASN B ND2 
2901 N N   . THR B 88  ? 0.43637 0.38815 0.41528 -0.02952 0.08201  0.06840  88  THR B N   
2902 C CA  . THR B 88  ? 0.46618 0.43128 0.46133 -0.03788 0.09062  0.07170  88  THR B CA  
2903 C C   . THR B 88  ? 0.45270 0.43271 0.46474 -0.04115 0.08544  0.06112  88  THR B C   
2904 O O   . THR B 88  ? 0.46070 0.44383 0.49147 -0.05118 0.08470  0.05948  88  THR B O   
2905 C CB  . THR B 88  ? 0.45401 0.42861 0.43768 -0.03191 0.10131  0.07948  88  THR B CB  
2906 O OG1 . THR B 88  ? 0.48570 0.44535 0.45211 -0.02862 0.10616  0.09058  88  THR B OG1 
2907 C CG2 . THR B 88  ? 0.41916 0.41106 0.42192 -0.04011 0.11132  0.08390  88  THR B CG2 
2908 N N   . VAL B 89  ? 0.43275 0.42067 0.43785 -0.03273 0.08100  0.05371  89  VAL B N   
2909 C CA  . VAL B 89  ? 0.39276 0.39350 0.41208 -0.03456 0.07642  0.04496  89  VAL B CA  
2910 C C   . VAL B 89  ? 0.41500 0.40863 0.44304 -0.03976 0.06724  0.03863  89  VAL B C   
2911 O O   . VAL B 89  ? 0.38285 0.38405 0.42727 -0.04665 0.06562  0.03539  89  VAL B O   
2912 C CB  . VAL B 89  ? 0.44549 0.45176 0.45372 -0.02413 0.07339  0.03875  89  VAL B CB  
2913 C CG1 . VAL B 89  ? 0.38504 0.40360 0.40730 -0.02516 0.06987  0.03157  89  VAL B CG1 
2914 C CG2 . VAL B 89  ? 0.40812 0.42007 0.40381 -0.01698 0.08253  0.04414  89  VAL B CG2 
2915 N N   . LEU B 90  ? 0.43006 0.41062 0.44707 -0.03572 0.06099  0.03655  90  LEU B N   
2916 C CA  . LEU B 90  ? 0.35627 0.33165 0.37938 -0.03833 0.05298  0.03017  90  LEU B CA  
2917 C C   . LEU B 90  ? 0.42875 0.39854 0.46353 -0.04753 0.05368  0.03119  90  LEU B C   
2918 O O   . LEU B 90  ? 0.44051 0.41100 0.48314 -0.05058 0.04806  0.02470  90  LEU B O   
2919 C CB  . LEU B 90  ? 0.39428 0.35842 0.40485 -0.03195 0.04761  0.02934  90  LEU B CB  
2920 C CG  . LEU B 90  ? 0.43386 0.39277 0.44855 -0.03256 0.04074  0.02390  90  LEU B CG  
2921 C CD1 . LEU B 90  ? 0.36841 0.33790 0.38988 -0.03262 0.03611  0.01675  90  LEU B CD1 
2922 C CD2 . LEU B 90  ? 0.38407 0.33433 0.38809 -0.02566 0.03692  0.02499  90  LEU B CD2 
2923 N N   . ILE B 91  ? 0.39528 0.35806 0.43038 -0.05203 0.06018  0.03914  91  ILE B N   
2924 C CA  . ILE B 91  ? 0.43905 0.39196 0.48438 -0.06139 0.05969  0.03954  91  ILE B CA  
2925 C C   . ILE B 91  ? 0.41139 0.37599 0.47376 -0.07153 0.06533  0.04273  91  ILE B C   
2926 O O   . ILE B 91  ? 0.42946 0.38508 0.50094 -0.08102 0.06644  0.04515  91  ILE B O   
2927 C CB  . ILE B 91  ? 0.45529 0.38640 0.48974 -0.06011 0.06130  0.04607  91  ILE B CB  
2928 C CG1 . ILE B 91  ? 0.44868 0.37866 0.47455 -0.05844 0.07071  0.05780  91  ILE B CG1 
2929 C CG2 . ILE B 91  ? 0.45616 0.37947 0.47797 -0.05012 0.05434  0.04153  91  ILE B CG2 
2930 C CD1 . ILE B 91  ? 0.51106 0.41792 0.52771 -0.05880 0.07366  0.06679  91  ILE B CD1 
2931 N N   . ASN B 92  ? 0.39250 0.37718 0.46026 -0.06955 0.06859  0.04249  92  ASN B N   
2932 C CA  . ASN B 92  ? 0.40944 0.41051 0.49654 -0.07834 0.07363  0.04504  92  ASN B CA  
2933 C C   . ASN B 92  ? 0.37772 0.37844 0.48154 -0.08862 0.06652  0.03841  92  ASN B C   
2934 O O   . ASN B 92  ? 0.37794 0.38117 0.48176 -0.08567 0.05781  0.02907  92  ASN B O   
2935 C CB  . ASN B 92  ? 0.37129 0.39462 0.46190 -0.07201 0.07541  0.04252  92  ASN B CB  
2936 C CG  . ASN B 92  ? 0.43416 0.47815 0.54611 -0.07967 0.08153  0.04608  92  ASN B CG  
2937 O OD1 . ASN B 92  ? 0.43625 0.49133 0.56563 -0.08581 0.07594  0.04036  92  ASN B OD1 
2938 N ND2 . ASN B 92  ? 0.38917 0.43960 0.50029 -0.07938 0.09316  0.05598  92  ASN B ND2 
2939 N N   . PRO B 93  ? 0.38682 0.38504 0.50504 -0.10087 0.06979  0.04291  93  PRO B N   
2940 C CA  . PRO B 93  ? 0.38469 0.37835 0.51621 -0.11069 0.06119  0.03509  93  PRO B CA  
2941 C C   . PRO B 93  ? 0.40889 0.42742 0.55807 -0.11345 0.05603  0.02793  93  PRO B C   
2942 O O   . PRO B 93  ? 0.38684 0.40285 0.54131 -0.11732 0.04611  0.01852  93  PRO B O   
2943 C CB  . PRO B 93  ? 0.38734 0.36935 0.52922 -0.12372 0.06676  0.04318  93  PRO B CB  
2944 C CG  . PRO B 93  ? 0.46359 0.45708 0.60597 -0.12258 0.07976  0.05574  93  PRO B CG  
2945 C CD  . PRO B 93  ? 0.37310 0.37177 0.49549 -0.10652 0.08151  0.05554  93  PRO B CD  
2946 N N   . VAL B 94  ? 0.36480 0.40716 0.52202 -0.11033 0.06218  0.03183  94  VAL B N   
2947 C CA  . VAL B 94  ? 0.32492 0.39145 0.49714 -0.10988 0.05666  0.02516  94  VAL B CA  
2948 C C   . VAL B 94  ? 0.35382 0.41727 0.51120 -0.09852 0.04827  0.01668  94  VAL B C   
2949 O O   . VAL B 94  ? 0.33836 0.40838 0.50209 -0.09956 0.03894  0.00856  94  VAL B O   
2950 C CB  . VAL B 94  ? 0.35715 0.44982 0.54131 -0.10753 0.06631  0.03187  94  VAL B CB  
2951 C CG1 . VAL B 94  ? 0.36247 0.48064 0.56184 -0.10486 0.05992  0.02505  94  VAL B CG1 
2952 C CG2 . VAL B 94  ? 0.36427 0.46147 0.56506 -0.12019 0.07597  0.04185  94  VAL B CG2 
2953 N N   . ILE B 95  ? 0.34739 0.40125 0.48490 -0.08774 0.05123  0.01871  95  ILE B N   
2954 C CA  . ILE B 95  ? 0.36349 0.41292 0.48782 -0.07836 0.04405  0.01197  95  ILE B CA  
2955 C C   . ILE B 95  ? 0.37656 0.41101 0.49674 -0.08166 0.03550  0.00529  95  ILE B C   
2956 O O   . ILE B 95  ? 0.35679 0.39536 0.47598 -0.07865 0.02799  -0.00151 95  ILE B O   
2957 C CB  . ILE B 95  ? 0.36336 0.40330 0.46862 -0.06837 0.04810  0.01529  95  ILE B CB  
2958 C CG1 . ILE B 95  ? 0.38154 0.43572 0.48767 -0.06294 0.05604  0.02013  95  ILE B CG1 
2959 C CG2 . ILE B 95  ? 0.33890 0.37270 0.43242 -0.06076 0.04078  0.00912  95  ILE B CG2 
2960 C CD1 . ILE B 95  ? 0.43810 0.51335 0.55660 -0.06003 0.05427  0.01676  95  ILE B CD1 
2961 N N   . HIS B 96  ? 0.36126 0.37752 0.47771 -0.08689 0.03682  0.00737  96  HIS B N   
2962 C CA  . HIS B 96  ? 0.38226 0.38221 0.49196 -0.08776 0.02952  0.00059  96  HIS B CA  
2963 C C   . HIS B 96  ? 0.37342 0.37782 0.49681 -0.09678 0.02241  -0.00638 96  HIS B C   
2964 O O   . HIS B 96  ? 0.39437 0.39307 0.51149 -0.09448 0.01459  -0.01464 96  HIS B O   
2965 C CB  . HIS B 96  ? 0.37237 0.34963 0.47198 -0.08822 0.03306  0.00506  96  HIS B CB  
2966 C CG  . HIS B 96  ? 0.40661 0.37873 0.49007 -0.07752 0.03596  0.00861  96  HIS B CG  
2967 N ND1 . HIS B 96  ? 0.38679 0.35360 0.45915 -0.06971 0.03105  0.00352  96  HIS B ND1 
2968 C CD2 . HIS B 96  ? 0.37434 0.34833 0.45152 -0.07320 0.04274  0.01625  96  HIS B CD2 
2969 C CE1 . HIS B 96  ? 0.42904 0.39457 0.49096 -0.06215 0.03396  0.00773  96  HIS B CE1 
2970 N NE2 . HIS B 96  ? 0.42611 0.39508 0.48936 -0.06366 0.04051  0.01492  96  HIS B NE2 
2971 N N   . ALA B 97  ? 0.36372 0.37984 0.50590 -0.10676 0.02478  -0.00343 97  ALA B N   
2972 C CA  . ALA B 97  ? 0.38398 0.40994 0.54180 -0.11520 0.01624  -0.01108 97  ALA B CA  
2973 C C   . ALA B 97  ? 0.36462 0.40826 0.52123 -0.10730 0.00946  -0.01730 97  ALA B C   
2974 O O   . ALA B 97  ? 0.38392 0.42627 0.53865 -0.10768 -0.00043 -0.02645 97  ALA B O   
2975 C CB  . ALA B 97  ? 0.35248 0.39354 0.53438 -0.12734 0.02076  -0.00559 97  ALA B CB  
2976 N N   . ILE B 98  ? 0.35893 0.41753 0.51459 -0.09915 0.01451  -0.01247 98  ILE B N   
2977 C CA  . ILE B 98  ? 0.32590 0.39829 0.47874 -0.09057 0.00860  -0.01693 98  ILE B CA  
2978 C C   . ILE B 98  ? 0.34935 0.40569 0.48161 -0.08301 0.00392  -0.02163 98  ILE B C   
2979 O O   . ILE B 98  ? 0.33974 0.39941 0.46884 -0.08071 -0.00446 -0.02836 98  ILE B O   
2980 C CB  . ILE B 98  ? 0.31633 0.40316 0.47023 -0.08246 0.01548  -0.01079 98  ILE B CB  
2981 C CG1 . ILE B 98  ? 0.35268 0.45945 0.52816 -0.08882 0.02110  -0.00599 98  ILE B CG1 
2982 C CG2 . ILE B 98  ? 0.32754 0.42323 0.47535 -0.07232 0.00958  -0.01439 98  ILE B CG2 
2983 C CD1 . ILE B 98  ? 0.35478 0.46883 0.52696 -0.08084 0.03103  0.00101  98  ILE B CD1 
2984 N N   . CYS B 99  ? 0.30537 0.34586 0.42346 -0.07847 0.00946  -0.01772 99  CYS B N   
2985 C CA  . CYS B 99  ? 0.38621 0.41428 0.48716 -0.07132 0.00643  -0.02104 99  CYS B CA  
2986 C C   . CYS B 99  ? 0.35717 0.37551 0.45501 -0.07477 -0.00071 -0.02906 99  CYS B C   
2987 O O   . CYS B 99  ? 0.35608 0.37526 0.44479 -0.06928 -0.00603 -0.03412 99  CYS B O   
2988 C CB  . CYS B 99  ? 0.34755 0.36142 0.43721 -0.06737 0.01268  -0.01592 99  CYS B CB  
2989 S SG  . CYS B 99  ? 0.39922 0.42132 0.48576 -0.06027 0.01859  -0.00941 99  CYS B SG  
2990 N N   . GLU B 100 ? 0.36774 0.37561 0.47200 -0.08360 -0.00082 -0.03030 100 GLU B N   
2991 C CA  . GLU B 100 ? 0.41278 0.40714 0.51163 -0.08605 -0.00801 -0.03926 100 GLU B CA  
2992 C C   . GLU B 100 ? 0.41998 0.42818 0.52445 -0.08785 -0.01768 -0.04739 100 GLU B C   
2993 O O   . GLU B 100 ? 0.43653 0.43852 0.52881 -0.08343 -0.02426 -0.05546 100 GLU B O   
2994 C CB  . GLU B 100 ? 0.43521 0.41264 0.54040 -0.09589 -0.00661 -0.03877 100 GLU B CB  
2995 C CG  . GLU B 100 ? 0.50015 0.45607 0.59173 -0.09084 -0.00097 -0.03474 100 GLU B CG  
2996 C CD  . GLU B 100 ? 0.61759 0.55606 0.71541 -0.10003 0.00232  -0.03080 100 GLU B CD  
2997 O OE1 . GLU B 100 ? 0.63226 0.57239 0.74502 -0.11180 -0.00095 -0.03315 100 GLU B OE1 
2998 O OE2 . GLU B 100 ? 0.69857 0.62178 0.78682 -0.09561 0.00802  -0.02481 100 GLU B OE2 
2999 N N   . ALA B 101 ? 0.38288 0.41134 0.50507 -0.09310 -0.01864 -0.04532 101 ALA B N   
3000 C CA  . ALA B 101 ? 0.38774 0.43246 0.51613 -0.09367 -0.02882 -0.05261 101 ALA B CA  
3001 C C   . ALA B 101 ? 0.38995 0.44302 0.50456 -0.08097 -0.03036 -0.05224 101 ALA B C   
3002 O O   . ALA B 101 ? 0.40365 0.45895 0.50962 -0.07704 -0.03899 -0.05952 101 ALA B O   
3003 C CB  . ALA B 101 ? 0.40085 0.46783 0.55445 -0.10199 -0.02889 -0.04964 101 ALA B CB  
3004 N N   . TYR B 102 ? 0.38588 0.44243 0.49731 -0.07442 -0.02217 -0.04370 102 TYR B N   
3005 C CA  . TYR B 102 ? 0.36496 0.42749 0.46466 -0.06336 -0.02283 -0.04180 102 TYR B CA  
3006 C C   . TYR B 102 ? 0.37347 0.42126 0.45282 -0.05715 -0.02384 -0.04482 102 TYR B C   
3007 O O   . TYR B 102 ? 0.36526 0.41776 0.43421 -0.05007 -0.02819 -0.04660 102 TYR B O   
3008 C CB  . TYR B 102 ? 0.33032 0.39572 0.43127 -0.05903 -0.01405 -0.03291 102 TYR B CB  
3009 C CG  . TYR B 102 ? 0.35028 0.41757 0.43976 -0.04863 -0.01347 -0.02950 102 TYR B CG  
3010 C CD1 . TYR B 102 ? 0.33881 0.42127 0.43221 -0.04362 -0.01799 -0.02921 102 TYR B CD1 
3011 C CD2 . TYR B 102 ? 0.33675 0.39080 0.41307 -0.04425 -0.00852 -0.02609 102 TYR B CD2 
3012 C CE1 . TYR B 102 ? 0.36376 0.44465 0.44640 -0.03462 -0.01711 -0.02509 102 TYR B CE1 
3013 C CE2 . TYR B 102 ? 0.30254 0.35742 0.37062 -0.03661 -0.00784 -0.02228 102 TYR B CE2 
3014 C CZ  . TYR B 102 ? 0.31533 0.38190 0.38559 -0.03171 -0.01183 -0.02140 102 TYR B CZ  
3015 O OH  . TYR B 102 ? 0.32555 0.38972 0.38714 -0.02449 -0.01095 -0.01679 102 TYR B OH  
3016 N N   . PHE B 103 ? 0.35758 0.38835 0.43075 -0.05870 -0.01921 -0.04454 103 PHE B N   
3017 C CA  . PHE B 103 ? 0.36510 0.38374 0.42076 -0.05184 -0.01806 -0.04624 103 PHE B CA  
3018 C C   . PHE B 103 ? 0.40442 0.41309 0.45236 -0.05295 -0.02471 -0.05642 103 PHE B C   
3019 O O   . PHE B 103 ? 0.39071 0.38748 0.42491 -0.04740 -0.02278 -0.05865 103 PHE B O   
3020 C CB  . PHE B 103 ? 0.31154 0.31881 0.36466 -0.05082 -0.00979 -0.04033 103 PHE B CB  
3021 C CG  . PHE B 103 ? 0.35362 0.36778 0.40761 -0.04676 -0.00422 -0.03199 103 PHE B CG  
3022 C CD1 . PHE B 103 ? 0.35776 0.37700 0.40353 -0.03978 -0.00411 -0.02970 103 PHE B CD1 
3023 C CD2 . PHE B 103 ? 0.34717 0.36107 0.40890 -0.04981 0.00092  -0.02649 103 PHE B CD2 
3024 C CE1 . PHE B 103 ? 0.32178 0.34416 0.36844 -0.03690 0.00006  -0.02295 103 PHE B CE1 
3025 C CE2 . PHE B 103 ? 0.30320 0.32118 0.36394 -0.04566 0.00491  -0.02058 103 PHE B CE2 
3026 C CZ  . PHE B 103 ? 0.31926 0.34064 0.37307 -0.03966 0.00399  -0.01926 103 PHE B CZ  
3027 N N   . GLN B 104 ? 0.39625 0.41040 0.45305 -0.05954 -0.03288 -0.06316 104 GLN B N   
3028 C CA  . GLN B 104 ? 0.42237 0.42452 0.47294 -0.06217 -0.04058 -0.07447 104 GLN B CA  
3029 C C   . GLN B 104 ? 0.45574 0.45396 0.48395 -0.05109 -0.04320 -0.07992 104 GLN B C   
3030 O O   . GLN B 104 ? 0.48721 0.46885 0.50344 -0.04862 -0.04430 -0.08699 104 GLN B O   
3031 C CB  . GLN B 104 ? 0.45391 0.46765 0.51952 -0.07111 -0.05053 -0.08079 104 GLN B CB  
3032 C CG  . GLN B 104 ? 0.55557 0.55490 0.61937 -0.07739 -0.05947 -0.09309 104 GLN B CG  
3033 C CD  . GLN B 104 ? 0.71012 0.72462 0.79213 -0.08730 -0.07028 -0.09913 104 GLN B CD  
3034 O OE1 . GLN B 104 ? 0.68359 0.71881 0.78376 -0.09094 -0.06861 -0.09228 104 GLN B OE1 
3035 N NE2 . GLN B 104 ? 0.74761 0.75288 0.82517 -0.09116 -0.08192 -0.11258 104 GLN B NE2 
3036 N N   . ARG B 105 ? 0.39647 0.40916 0.41794 -0.04359 -0.04372 -0.07635 105 ARG B N   
3037 C CA  . ARG B 105 ? 0.46867 0.47981 0.46815 -0.03273 -0.04507 -0.07984 105 ARG B CA  
3038 C C   . ARG B 105 ? 0.45636 0.46056 0.44536 -0.02528 -0.03432 -0.07300 105 ARG B C   
3039 O O   . ARG B 105 ? 0.49822 0.49760 0.46934 -0.01685 -0.03354 -0.07685 105 ARG B O   
3040 C CB  . ARG B 105 ? 0.43876 0.46733 0.43407 -0.02723 -0.04965 -0.07722 105 ARG B CB  
3041 C CG  . ARG B 105 ? 0.50644 0.54579 0.50952 -0.03188 -0.06248 -0.08539 105 ARG B CG  
3042 C CD  . ARG B 105 ? 0.50645 0.56455 0.51005 -0.02601 -0.06509 -0.07893 105 ARG B CD  
3043 N NE  . ARG B 105 ? 0.49689 0.55460 0.47647 -0.01378 -0.06377 -0.07653 105 ARG B NE  
3044 C CZ  . ARG B 105 ? 0.49472 0.56123 0.46929 -0.00641 -0.06062 -0.06651 105 ARG B CZ  
3045 N NH1 . ARG B 105 ? 0.48664 0.56267 0.47765 -0.00874 -0.05898 -0.05893 105 ARG B NH1 
3046 N NH2 . ARG B 105 ? 0.51865 0.58343 0.47051 0.00402  -0.05844 -0.06361 105 ARG B NH2 
3047 N N   . THR B 106 ? 0.42029 0.42528 0.41983 -0.02767 -0.02621 -0.06325 106 THR B N   
3048 C CA  . THR B 106 ? 0.41637 0.41706 0.40877 -0.02148 -0.01721 -0.05714 106 THR B CA  
3049 C C   . THR B 106 ? 0.40346 0.38899 0.39725 -0.02298 -0.01380 -0.05945 106 THR B C   
3050 O O   . THR B 106 ? 0.36788 0.34972 0.35376 -0.01616 -0.00807 -0.05758 106 THR B O   
3051 C CB  . THR B 106 ? 0.43342 0.44290 0.43423 -0.02193 -0.01133 -0.04577 106 THR B CB  
3052 O OG1 . THR B 106 ? 0.40796 0.41791 0.40095 -0.01542 -0.00437 -0.04011 106 THR B OG1 
3053 C CG2 . THR B 106 ? 0.39763 0.40294 0.41275 -0.02896 -0.00848 -0.04241 106 THR B CG2 
3054 N N   . GLY B 107 ? 0.39934 0.37646 0.40341 -0.03140 -0.01696 -0.06286 107 GLY B N   
3055 C CA  . GLY B 107 ? 0.39584 0.35611 0.40044 -0.03249 -0.01396 -0.06398 107 GLY B CA  
3056 C C   . GLY B 107 ? 0.40977 0.37059 0.42574 -0.03633 -0.00772 -0.05421 107 GLY B C   
3057 O O   . GLY B 107 ? 0.38521 0.35625 0.41223 -0.04199 -0.00758 -0.04937 107 GLY B O   
3058 N N   . ASP B 108 ? 0.39797 0.34880 0.41055 -0.03209 -0.00269 -0.05139 108 ASP B N   
3059 C CA  . ASP B 108 ? 0.35381 0.30334 0.37480 -0.03515 0.00212  -0.04295 108 ASP B CA  
3060 C C   . ASP B 108 ? 0.37025 0.33563 0.39529 -0.03388 0.00537  -0.03541 108 ASP B C   
3061 O O   . ASP B 108 ? 0.35876 0.33363 0.37899 -0.02875 0.00595  -0.03478 108 ASP B O   
3062 C CB  . ASP B 108 ? 0.39124 0.32778 0.40689 -0.02925 0.00568  -0.04155 108 ASP B CB  
3063 C CG  . ASP B 108 ? 0.44448 0.35976 0.45792 -0.03192 0.00313  -0.04695 108 ASP B CG  
3064 O OD1 . ASP B 108 ? 0.47189 0.38301 0.49068 -0.04070 -0.00123 -0.05103 108 ASP B OD1 
3065 O OD2 . ASP B 108 ? 0.42991 0.33250 0.43693 -0.02509 0.00514  -0.04722 108 ASP B OD2 
3066 N N   . TYR B 109 ? 0.34101 0.30768 0.37408 -0.03837 0.00788  -0.02941 109 TYR B N   
3067 C CA  . TYR B 109 ? 0.33645 0.31407 0.37283 -0.03728 0.01060  -0.02300 109 TYR B CA  
3068 C C   . TYR B 109 ? 0.33979 0.31129 0.37618 -0.03599 0.01431  -0.01768 109 TYR B C   
3069 O O   . TYR B 109 ? 0.33764 0.29700 0.37274 -0.03688 0.01510  -0.01771 109 TYR B O   
3070 C CB  . TYR B 109 ? 0.32773 0.31480 0.37251 -0.04263 0.00936  -0.02191 109 TYR B CB  
3071 C CG  . TYR B 109 ? 0.34821 0.32976 0.40028 -0.04949 0.01055  -0.02089 109 TYR B CG  
3072 C CD1 . TYR B 109 ? 0.34102 0.31712 0.39677 -0.05518 0.00694  -0.02624 109 TYR B CD1 
3073 C CD2 . TYR B 109 ? 0.33219 0.31343 0.38672 -0.05028 0.01528  -0.01448 109 TYR B CD2 
3074 C CE1 . TYR B 109 ? 0.36862 0.33924 0.43260 -0.06274 0.00888  -0.02389 109 TYR B CE1 
3075 C CE2 . TYR B 109 ? 0.38969 0.36617 0.45026 -0.05651 0.01780  -0.01193 109 TYR B CE2 
3076 C CZ  . TYR B 109 ? 0.38476 0.35573 0.45126 -0.06351 0.01508  -0.01591 109 TYR B CZ  
3077 O OH  . TYR B 109 ? 0.37520 0.34129 0.44931 -0.07096 0.01837  -0.01198 109 TYR B OH  
3078 N N   . TRP B 110 ? 0.28785 0.26648 0.32481 -0.03355 0.01597  -0.01320 110 TRP B N   
3079 C CA  . TRP B 110 ? 0.31494 0.28948 0.35119 -0.03235 0.01816  -0.00854 110 TRP B CA  
3080 C C   . TRP B 110 ? 0.29534 0.27839 0.33349 -0.03230 0.01849  -0.00550 110 TRP B C   
3081 O O   . TRP B 110 ? 0.27354 0.26413 0.31402 -0.03304 0.01739  -0.00643 110 TRP B O   
3082 C CB  . TRP B 110 ? 0.30256 0.27260 0.33473 -0.02640 0.01840  -0.00803 110 TRP B CB  
3083 C CG  . TRP B 110 ? 0.32632 0.30551 0.35879 -0.02227 0.01799  -0.00890 110 TRP B CG  
3084 C CD1 . TRP B 110 ? 0.28421 0.27326 0.31895 -0.02348 0.01761  -0.00851 110 TRP B CD1 
3085 C CD2 . TRP B 110 ? 0.33631 0.31599 0.36732 -0.01599 0.01870  -0.00936 110 TRP B CD2 
3086 N NE1 . TRP B 110 ? 0.30744 0.30314 0.34253 -0.01951 0.01865  -0.00796 110 TRP B NE1 
3087 C CE2 . TRP B 110 ? 0.28141 0.27317 0.31501 -0.01467 0.01948  -0.00874 110 TRP B CE2 
3088 C CE3 . TRP B 110 ? 0.29670 0.26791 0.32473 -0.01074 0.01909  -0.00969 110 TRP B CE3 
3089 C CZ2 . TRP B 110 ? 0.32082 0.31934 0.35577 -0.00882 0.02134  -0.00832 110 TRP B CZ2 
3090 C CZ3 . TRP B 110 ? 0.32209 0.29951 0.35084 -0.00357 0.02018  -0.01015 110 TRP B CZ3 
3091 C CH2 . TRP B 110 ? 0.34294 0.33525 0.37587 -0.00291 0.02163  -0.00946 110 TRP B CH2 
3092 N N   . LEU B 111 ? 0.30611 0.28660 0.34180 -0.03053 0.01951  -0.00211 111 LEU B N   
3093 C CA  . LEU B 111 ? 0.33324 0.31885 0.36870 -0.02999 0.01929  -0.00048 111 LEU B CA  
3094 C C   . LEU B 111 ? 0.30454 0.29467 0.34076 -0.02770 0.01661  -0.00087 111 LEU B C   
3095 O O   . LEU B 111 ? 0.34405 0.33355 0.37952 -0.02505 0.01541  -0.00013 111 LEU B O   
3096 C CB  . LEU B 111 ? 0.36286 0.34370 0.39310 -0.02853 0.02108  0.00278  111 LEU B CB  
3097 C CG  . LEU B 111 ? 0.30848 0.29301 0.33580 -0.02675 0.02065  0.00305  111 LEU B CG  
3098 C CD1 . LEU B 111 ? 0.31866 0.30865 0.35023 -0.02903 0.02317  0.00247  111 LEU B CD1 
3099 C CD2 . LEU B 111 ? 0.32064 0.30045 0.33886 -0.02315 0.02149  0.00592  111 LEU B CD2 
3100 N N   . SER B 112 ? 0.31001 0.30496 0.34869 -0.02873 0.01563  -0.00148 112 SER B N   
3101 C CA  . SER B 112 ? 0.30402 0.30210 0.34489 -0.02822 0.01344  -0.00078 112 SER B CA  
3102 C C   . SER B 112 ? 0.29218 0.28799 0.33112 -0.02757 0.01091  -0.00079 112 SER B C   
3103 O O   . SER B 112 ? 0.29974 0.29724 0.34105 -0.02749 0.00806  -0.00052 112 SER B O   
3104 C CB  . SER B 112 ? 0.30070 0.30215 0.34377 -0.02939 0.01338  -0.00037 112 SER B CB  
3105 O OG  . SER B 112 ? 0.29559 0.29923 0.34210 -0.03025 0.01210  0.00163  112 SER B OG  
3106 N N   . ALA B 113 ? 0.33064 0.32364 0.36557 -0.02680 0.01167  -0.00155 113 ALA B N   
3107 C CA  . ALA B 113 ? 0.30815 0.29757 0.33811 -0.02484 0.00912  -0.00293 113 ALA B CA  
3108 C C   . ALA B 113 ? 0.34985 0.33799 0.37410 -0.02245 0.01261  -0.00301 113 ALA B C   
3109 O O   . ALA B 113 ? 0.28300 0.27463 0.31071 -0.02339 0.01598  -0.00236 113 ALA B O   
3110 C CB  . ALA B 113 ? 0.32907 0.31658 0.36144 -0.02594 0.00585  -0.00431 113 ALA B CB  
3111 N N   . ALA B 114 ? 0.29575 0.28036 0.31142 -0.01906 0.01169  -0.00376 114 ALA B N   
3112 C CA  . ALA B 114 ? 0.33939 0.32378 0.34815 -0.01545 0.01572  -0.00375 114 ALA B CA  
3113 C C   . ALA B 114 ? 0.33437 0.31335 0.33206 -0.01067 0.01172  -0.00729 114 ALA B C   
3114 O O   . ALA B 114 ? 0.34857 0.32506 0.34051 -0.00938 0.00805  -0.00742 114 ALA B O   
3115 C CB  . ALA B 114 ? 0.34651 0.33231 0.35345 -0.01586 0.02155  0.00075  114 ALA B CB  
3116 N N   . PHE B 115 ? 0.34098 0.31784 0.33509 -0.00724 0.01172  -0.01073 115 PHE B N   
3117 C CA  . PHE B 115 ? 0.36886 0.33788 0.35243 -0.00299 0.00601  -0.01630 115 PHE B CA  
3118 C C   . PHE B 115 ? 0.38365 0.35098 0.35878 0.00409  0.00970  -0.01920 115 PHE B C   
3119 O O   . PHE B 115 ? 0.35319 0.32619 0.33492 0.00478  0.01508  -0.01733 115 PHE B O   
3120 C CB  . PHE B 115 ? 0.36800 0.33159 0.35864 -0.00739 -0.00169 -0.01956 115 PHE B CB  
3121 C CG  . PHE B 115 ? 0.38358 0.34668 0.38314 -0.00941 -0.00011 -0.01872 115 PHE B CG  
3122 C CD1 . PHE B 115 ? 0.37716 0.34734 0.38785 -0.01418 0.00278  -0.01395 115 PHE B CD1 
3123 C CD2 . PHE B 115 ? 0.42405 0.37835 0.41929 -0.00556 -0.00215 -0.02292 115 PHE B CD2 
3124 C CE1 . PHE B 115 ? 0.42972 0.39965 0.44652 -0.01499 0.00357  -0.01268 115 PHE B CE1 
3125 C CE2 . PHE B 115 ? 0.41637 0.36925 0.41867 -0.00623 -0.00112 -0.02119 115 PHE B CE2 
3126 C CZ  . PHE B 115 ? 0.39889 0.36028 0.41172 -0.01093 0.00168  -0.01572 115 PHE B CZ  
3127 N N   . LEU B 116 ? 0.37065 0.33103 0.33087 0.01018  0.00632  -0.02428 116 LEU B N   
3128 C CA  . LEU B 116 ? 0.39112 0.34844 0.34020 0.01905  0.00933  -0.02854 116 LEU B CA  
3129 C C   . LEU B 116 ? 0.43951 0.38473 0.38869 0.02015  0.00230  -0.03567 116 LEU B C   
3130 O O   . LEU B 116 ? 0.43359 0.36982 0.38359 0.01564  -0.00694 -0.03956 116 LEU B O   
3131 C CB  . LEU B 116 ? 0.40785 0.36246 0.33711 0.02639  0.00921  -0.03087 116 LEU B CB  
3132 C CG  . LEU B 116 ? 0.47201 0.42436 0.38404 0.03811  0.01350  -0.03538 116 LEU B CG  
3133 C CD1 . LEU B 116 ? 0.56511 0.50222 0.46862 0.04240  0.00423  -0.04636 116 LEU B CD1 
3134 C CD2 . LEU B 116 ? 0.52142 0.48542 0.44293 0.04007  0.02449  -0.03042 116 LEU B CD2 
3135 N N   . ARG B 117 ? 0.39946 0.34465 0.34908 0.02602  0.00665  -0.03695 117 ARG B N   
3136 C CA  . ARG B 117 ? 0.46072 0.39082 0.40442 0.03109  0.00114  -0.04454 117 ARG B CA  
3137 C C   . ARG B 117 ? 0.49146 0.42143 0.41999 0.04437  0.00659  -0.04901 117 ARG B C   
3138 O O   . ARG B 117 ? 0.44168 0.38714 0.37252 0.04835  0.01671  -0.04384 117 ARG B O   
3139 C CB  . ARG B 117 ? 0.48663 0.41508 0.44452 0.02794  0.00092  -0.04173 117 ARG B CB  
3140 C CG  . ARG B 117 ? 0.47484 0.40078 0.44539 0.01600  -0.00471 -0.03812 117 ARG B CG  
3141 C CD  . ARG B 117 ? 0.55014 0.45916 0.51583 0.01249  -0.01498 -0.04452 117 ARG B CD  
3142 N NE  . ARG B 117 ? 0.62250 0.51407 0.58637 0.01535  -0.01895 -0.04854 117 ARG B NE  
3143 C CZ  . ARG B 117 ? 0.62886 0.50452 0.57851 0.02329  -0.02308 -0.05759 117 ARG B CZ  
3144 N NH1 . ARG B 117 ? 0.64046 0.51611 0.57501 0.02934  -0.02424 -0.06406 117 ARG B NH1 
3145 N NH2 . ARG B 117 ? 0.66900 0.52692 0.61792 0.02603  -0.02627 -0.06029 117 ARG B NH2 
3146 N N   . GLU B 118 ? 0.48205 0.39483 0.39542 0.05113  -0.00004 -0.05881 118 GLU B N   
3147 C CA  . GLU B 118 ? 0.54148 0.45140 0.43849 0.06585  0.00459  -0.06482 118 GLU B CA  
3148 C C   . GLU B 118 ? 0.57218 0.46296 0.46729 0.07094  -0.00122 -0.07227 118 GLU B C   
3149 O O   . GLU B 118 ? 0.58012 0.45115 0.47153 0.06644  -0.01242 -0.07895 118 GLU B O   
3150 C CB  . GLU B 118 ? 0.56482 0.46960 0.43887 0.07227  0.00196  -0.07123 118 GLU B CB  
3151 C CG  . GLU B 118 ? 0.62917 0.54753 0.49098 0.08441  0.01432  -0.06898 118 GLU B CG  
3152 C CD  . GLU B 118 ? 0.69543 0.60861 0.53072 0.09264  0.01230  -0.07484 118 GLU B CD  
3153 O OE1 . GLU B 118 ? 0.77426 0.66802 0.59362 0.09716  0.00140  -0.08688 118 GLU B OE1 
3154 O OE2 . GLU B 118 ? 0.67171 0.59964 0.50136 0.09463  0.02142  -0.06724 118 GLU B OE2 
3155 N N   . ILE B 119 ? 0.57881 0.47527 0.47713 0.08035  0.00612  -0.07098 119 ILE B N   
3156 C CA  . ILE B 119 ? 0.57436 0.45208 0.47073 0.08724  0.00163  -0.07687 119 ILE B CA  
3157 C C   . ILE B 119 ? 0.62317 0.49248 0.49761 0.10488  0.00395  -0.08701 119 ILE B C   
3158 O O   . ILE B 119 ? 0.59489 0.48281 0.46697 0.11550  0.01521  -0.08451 119 ILE B O   
3159 C CB  . ILE B 119 ? 0.57280 0.46214 0.48784 0.08723  0.00687  -0.06865 119 ILE B CB  
3160 C CG1 . ILE B 119 ? 0.59165 0.48933 0.52535 0.07082  0.00481  -0.05933 119 ILE B CG1 
3161 C CG2 . ILE B 119 ? 0.58605 0.45306 0.49790 0.09496  0.00160  -0.07373 119 ILE B CG2 
3162 C CD1 . ILE B 119 ? 0.56464 0.48945 0.50908 0.06555  0.01325  -0.05090 119 ILE B CD1 
3163 N N   . GLU B 120 ? 0.62211 0.46366 0.48085 0.10797  -0.00663 -0.09866 120 GLU B N   
3164 C CA  . GLU B 120 ? 0.66440 0.49336 0.49822 0.12530  -0.00644 -0.11080 120 GLU B CA  
3165 C C   . GLU B 120 ? 0.64976 0.47153 0.48339 0.13984  -0.00242 -0.11344 120 GLU B C   
3166 O O   . GLU B 120 ? 0.69349 0.51145 0.54383 0.13534  -0.00391 -0.10783 120 GLU B O   
3167 C CB  . GLU B 120 ? 0.64601 0.44545 0.46311 0.12260  -0.02137 -0.12393 120 GLU B CB  
3168 C CG  . GLU B 120 ? 0.72314 0.52847 0.53821 0.11054  -0.02752 -0.12331 120 GLU B CG  
3169 C CD  . GLU B 120 ? 0.83288 0.63656 0.67086 0.09050  -0.03520 -0.11652 120 GLU B CD  
3170 O OE1 . GLU B 120 ? 0.77974 0.59181 0.63828 0.08443  -0.03008 -0.10626 120 GLU B OE1 
3171 O OE2 . GLU B 120 ? 0.88823 0.68318 0.72343 0.08143  -0.04655 -0.12165 120 GLU B OE2 
3172 N N   . SER B 121 ? 0.67105 0.49055 0.48396 0.15878  0.00262  -0.12220 121 SER B N   
3173 C CA  . SER B 121 ? 0.68172 0.48776 0.48927 0.17559  0.00406  -0.12827 121 SER B CA  
3174 C C   . SER B 121 ? 0.74138 0.51126 0.55000 0.16961  -0.00997 -0.13403 121 SER B C   
3175 O O   . SER B 121 ? 0.72364 0.47295 0.52655 0.15784  -0.02203 -0.13994 121 SER B O   
3176 C CB  . SER B 121 ? 0.68424 0.48441 0.46305 0.19662  0.00804  -0.14076 121 SER B CB  
3177 O OG  . SER B 121 ? 0.67929 0.51411 0.45866 0.20527  0.02399  -0.13377 121 SER B OG  
3178 N N   . GLY B 122 ? 0.71152 0.47414 0.52846 0.17763  -0.00847 -0.13165 122 GLY B N   
3179 C CA  . GLY B 122 ? 0.75214 0.47820 0.56903 0.17372  -0.02034 -0.13582 122 GLY B CA  
3180 C C   . GLY B 122 ? 0.79997 0.52572 0.63935 0.15259  -0.02537 -0.12407 122 GLY B C   
3181 O O   . GLY B 122 ? 0.84862 0.54427 0.68963 0.14777  -0.03432 -0.12526 122 GLY B O   
3182 N N   . MET B 123 ? 0.70624 0.46328 0.56230 0.14027  -0.01956 -0.11259 123 MET B N   
3183 C CA  . MET B 123 ? 0.75501 0.51274 0.63075 0.12150  -0.02362 -0.10180 123 MET B CA  
3184 C C   . MET B 123 ? 0.74807 0.51455 0.63861 0.12575  -0.01859 -0.09121 123 MET B C   
3185 O O   . MET B 123 ? 0.72706 0.51800 0.62167 0.13738  -0.00919 -0.08786 123 MET B O   
3186 C CB  . MET B 123 ? 0.75906 0.54406 0.64504 0.10717  -0.02043 -0.09487 123 MET B CB  
3187 C CG  . MET B 123 ? 0.86385 0.63677 0.75595 0.08816  -0.03021 -0.09408 123 MET B CG  
3188 S SD  . MET B 123 ? 1.09337 0.82598 0.96722 0.08868  -0.04436 -0.10995 123 MET B SD  
3189 C CE  . MET B 123 ? 0.98310 0.71128 0.87452 0.06374  -0.05373 -0.10432 123 MET B CE  
3190 N N   . PRO B 124 ? 0.76003 0.50809 0.65901 0.11671  -0.02471 -0.08540 124 PRO B N   
3191 C CA  . PRO B 124 ? 0.74467 0.50093 0.65597 0.12085  -0.02097 -0.07460 124 PRO B CA  
3192 C C   . PRO B 124 ? 0.65296 0.44334 0.58236 0.10942  -0.01538 -0.06278 124 PRO B C   
3193 O O   . PRO B 124 ? 0.60290 0.40596 0.53662 0.09619  -0.01513 -0.06164 124 PRO B O   
3194 C CB  . PRO B 124 ? 0.76023 0.48081 0.67094 0.11412  -0.02975 -0.07242 124 PRO B CB  
3195 C CG  . PRO B 124 ? 0.74715 0.45530 0.65650 0.09710  -0.03686 -0.07697 124 PRO B CG  
3196 C CD  . PRO B 124 ? 0.80987 0.52709 0.70651 0.10328  -0.03568 -0.08872 124 PRO B CD  
3197 N N   . ALA B 125 ? 0.58604 0.39062 0.52545 0.11558  -0.01157 -0.05439 125 ALA B N   
3198 C CA  . ALA B 125 ? 0.60730 0.44302 0.56288 0.10607  -0.00718 -0.04444 125 ALA B CA  
3199 C C   . ALA B 125 ? 0.58542 0.41190 0.54760 0.08920  -0.01189 -0.03664 125 ALA B C   
3200 O O   . ALA B 125 ? 0.64740 0.44535 0.60507 0.08671  -0.01764 -0.03555 125 ALA B O   
3201 C CB  . ALA B 125 ? 0.60366 0.45919 0.56800 0.11845  -0.00298 -0.03887 125 ALA B CB  
3202 N N   . GLN B 126 ? 0.56000 0.41060 0.53300 0.07766  -0.00890 -0.03099 126 GLN B N   
3203 C CA  . GLN B 126 ? 0.57864 0.42677 0.55883 0.06351  -0.01143 -0.02267 126 GLN B CA  
3204 C C   . GLN B 126 ? 0.54740 0.39276 0.53067 0.06856  -0.01212 -0.01387 126 GLN B C   
3205 O O   . GLN B 126 ? 0.56750 0.42588 0.55268 0.08104  -0.00981 -0.01299 126 GLN B O   
3206 C CB  . GLN B 126 ? 0.55639 0.43199 0.54633 0.05314  -0.00757 -0.01928 126 GLN B CB  
3207 C CG  . GLN B 126 ? 0.54003 0.41444 0.52843 0.04274  -0.00871 -0.02355 126 GLN B CG  
3208 C CD  . GLN B 126 ? 0.56958 0.46929 0.56683 0.03479  -0.00459 -0.01989 126 GLN B CD  
3209 O OE1 . GLN B 126 ? 0.52135 0.44109 0.52487 0.03852  -0.00036 -0.01690 126 GLN B OE1 
3210 N NE2 . GLN B 126 ? 0.59752 0.49637 0.59603 0.02391  -0.00635 -0.02037 126 GLN B NE2 
3211 N N   . PRO B 127 ? 0.60338 0.43467 0.58793 0.05903  -0.01498 -0.00641 127 PRO B N   
3212 C CA  . PRO B 127 ? 0.62038 0.45536 0.60746 0.06231  -0.01471 0.00403  127 PRO B CA  
3213 C C   . PRO B 127 ? 0.51201 0.38072 0.50812 0.05983  -0.01116 0.00737  127 PRO B C   
3214 O O   . PRO B 127 ? 0.45829 0.34253 0.45960 0.05059  -0.00890 0.00453  127 PRO B O   
3215 C CB  . PRO B 127 ? 0.60813 0.42269 0.59469 0.04991  -0.01697 0.01158  127 PRO B CB  
3216 C CG  . PRO B 127 ? 0.67755 0.47585 0.66271 0.04108  -0.01979 0.00389  127 PRO B CG  
3217 C CD  . PRO B 127 ? 0.60836 0.42474 0.59363 0.04403  -0.01798 -0.00622 127 PRO B CD  
3218 N N   . PHE B 128 ? 0.50124 0.38032 0.49879 0.06874  -0.01143 0.01305  128 PHE B N   
3219 C CA  . PHE B 128 ? 0.48791 0.39619 0.49351 0.06553  -0.00987 0.01619  128 PHE B CA  
3220 C C   . PHE B 128 ? 0.48021 0.38719 0.48585 0.05183  -0.00948 0.02232  128 PHE B C   
3221 O O   . PHE B 128 ? 0.50631 0.39253 0.50634 0.04835  -0.01059 0.02871  128 PHE B O   
3222 C CB  . PHE B 128 ? 0.46076 0.37941 0.46709 0.07828  -0.01207 0.02084  128 PHE B CB  
3223 C CG  . PHE B 128 ? 0.52077 0.45439 0.53254 0.09130  -0.01118 0.01479  128 PHE B CG  
3224 C CD1 . PHE B 128 ? 0.46784 0.42875 0.49045 0.08811  -0.00779 0.00934  128 PHE B CD1 
3225 C CD2 . PHE B 128 ? 0.51501 0.43574 0.52160 0.10713  -0.01318 0.01513  128 PHE B CD2 
3226 C CE1 . PHE B 128 ? 0.45798 0.43578 0.48757 0.09973  -0.00560 0.00482  128 PHE B CE1 
3227 C CE2 . PHE B 128 ? 0.58375 0.52159 0.59668 0.12031  -0.01140 0.00969  128 PHE B CE2 
3228 C CZ  . PHE B 128 ? 0.50923 0.47704 0.53439 0.11615  -0.00720 0.00478  128 PHE B CZ  
3229 N N   . HIS B 129 ? 0.43678 0.36544 0.44904 0.04405  -0.00740 0.02054  129 HIS B N   
3230 C CA  . HIS B 129 ? 0.46411 0.39332 0.47649 0.03214  -0.00617 0.02506  129 HIS B CA  
3231 C C   . HIS B 129 ? 0.44081 0.39537 0.45922 0.02832  -0.00490 0.02305  129 HIS B C   
3232 O O   . HIS B 129 ? 0.42693 0.39805 0.45121 0.03258  -0.00490 0.01817  129 HIS B O   
3233 C CB  . HIS B 129 ? 0.44697 0.36311 0.45997 0.02231  -0.00524 0.02198  129 HIS B CB  
3234 C CG  . HIS B 129 ? 0.45245 0.37798 0.46915 0.02122  -0.00399 0.01304  129 HIS B CG  
3235 N ND1 . HIS B 129 ? 0.49052 0.40993 0.50448 0.02927  -0.00451 0.00672  129 HIS B ND1 
3236 C CD2 . HIS B 129 ? 0.44245 0.38257 0.46400 0.01418  -0.00180 0.00995  129 HIS B CD2 
3237 C CE1 . HIS B 129 ? 0.47090 0.40149 0.48739 0.02678  -0.00225 0.00080  129 HIS B CE1 
3238 N NE2 . HIS B 129 ? 0.44086 0.38319 0.46219 0.01743  -0.00083 0.00290  129 HIS B NE2 
3239 N N   . ARG B 130 ? 0.45463 0.41161 0.47214 0.01992  -0.00353 0.02675  130 ARG B N   
3240 C CA  . ARG B 130 ? 0.45164 0.42705 0.47368 0.01434  -0.00227 0.02361  130 ARG B CA  
3241 C C   . ARG B 130 ? 0.41515 0.38683 0.43998 0.00469  0.00044  0.02104  130 ARG B C   
3242 O O   . ARG B 130 ? 0.45032 0.40736 0.47365 0.00077  0.00092  0.02353  130 ARG B O   
3243 C CB  . ARG B 130 ? 0.44321 0.42565 0.46003 0.01469  -0.00303 0.02903  130 ARG B CB  
3244 C CG  . ARG B 130 ? 0.41946 0.41006 0.43394 0.02486  -0.00723 0.03052  130 ARG B CG  
3245 C CD  . ARG B 130 ? 0.35561 0.35024 0.36077 0.02690  -0.00868 0.03650  130 ARG B CD  
3246 N NE  . ARG B 130 ? 0.39095 0.39991 0.39616 0.03578  -0.01436 0.03509  130 ARG B NE  
3247 C CZ  . ARG B 130 ? 0.49579 0.50851 0.49080 0.04188  -0.01779 0.04019  130 ARG B CZ  
3248 N NH1 . ARG B 130 ? 0.47209 0.47420 0.45478 0.04069  -0.01476 0.04841  130 ARG B NH1 
3249 N NH2 . ARG B 130 ? 0.47208 0.50106 0.46953 0.04948  -0.02440 0.03722  130 ARG B NH2 
3250 N N   . ASP B 131 ? 0.42173 0.40673 0.45138 0.00082  0.00169  0.01613  131 ASP B N   
3251 C CA  . ASP B 131 ? 0.39622 0.37981 0.42836 -0.00686 0.00381  0.01369  131 ASP B CA  
3252 C C   . ASP B 131 ? 0.43196 0.41901 0.46283 -0.01176 0.00542  0.01738  131 ASP B C   
3253 O O   . ASP B 131 ? 0.49013 0.48690 0.52254 -0.01428 0.00646  0.01470  131 ASP B O   
3254 C CB  . ASP B 131 ? 0.39706 0.39098 0.43384 -0.00779 0.00495  0.00777  131 ASP B CB  
3255 C CG  . ASP B 131 ? 0.44916 0.43947 0.48621 -0.00324 0.00521  0.00420  131 ASP B CG  
3256 O OD1 . ASP B 131 ? 0.41902 0.39594 0.45202 -0.00017 0.00374  0.00485  131 ASP B OD1 
3257 O OD2 . ASP B 131 ? 0.45348 0.45368 0.49438 -0.00265 0.00717  0.00090  131 ASP B OD2 
3258 N N   . ASP B 132 ? 0.39408 0.37238 0.42179 -0.01268 0.00606  0.02394  132 ASP B N   
3259 C CA  . ASP B 132 ? 0.41377 0.39671 0.43967 -0.01607 0.00901  0.02865  132 ASP B CA  
3260 C C   . ASP B 132 ? 0.41875 0.39377 0.44889 -0.02267 0.01119  0.03312  132 ASP B C   
3261 O O   . ASP B 132 ? 0.43475 0.41156 0.46356 -0.02474 0.01470  0.04006  132 ASP B O   
3262 C CB  . ASP B 132 ? 0.44107 0.42595 0.45857 -0.01056 0.00886  0.03450  132 ASP B CB  
3263 C CG  . ASP B 132 ? 0.52145 0.49228 0.53527 -0.00681 0.00752  0.04086  132 ASP B CG  
3264 O OD1 . ASP B 132 ? 0.49373 0.45173 0.51167 -0.00930 0.00672  0.04027  132 ASP B OD1 
3265 O OD2 . ASP B 132 ? 0.51399 0.48545 0.51961 -0.00063 0.00665  0.04619  132 ASP B OD2 
3266 N N   . ALA B 133 ? 0.39886 0.36631 0.43427 -0.02601 0.00913  0.02926  133 ALA B N   
3267 C CA  . ALA B 133 ? 0.41201 0.37175 0.45360 -0.03316 0.00932  0.03262  133 ALA B CA  
3268 C C   . ALA B 133 ? 0.36894 0.33896 0.41819 -0.03862 0.01046  0.03002  133 ALA B C   
3269 O O   . ALA B 133 ? 0.39700 0.36921 0.45333 -0.04460 0.01252  0.03506  133 ALA B O   
3270 C CB  . ALA B 133 ? 0.39866 0.34192 0.44042 -0.03327 0.00472  0.02915  133 ALA B CB  
3271 N N   . THR B 134 ? 0.34694 0.32387 0.39573 -0.03656 0.00944  0.02305  134 THR B N   
3272 C CA  . THR B 134 ? 0.32495 0.31008 0.38033 -0.04035 0.00983  0.02095  134 THR B CA  
3273 C C   . THR B 134 ? 0.32929 0.32650 0.38637 -0.04060 0.01486  0.02525  134 THR B C   
3274 O O   . THR B 134 ? 0.27853 0.28273 0.34395 -0.04455 0.01648  0.02760  134 THR B O   
3275 C CB  . THR B 134 ? 0.35429 0.34174 0.40692 -0.03736 0.00808  0.01384  134 THR B CB  
3276 O OG1 . THR B 134 ? 0.43482 0.41200 0.48401 -0.03564 0.00448  0.01000  134 THR B OG1 
3277 C CG2 . THR B 134 ? 0.33891 0.33307 0.39747 -0.04005 0.00747  0.01213  134 THR B CG2 
3278 N N   . HIS B 135 ? 0.32242 0.32311 0.37167 -0.03582 0.01710  0.02595  135 HIS B N   
3279 C CA  . HIS B 135 ? 0.33569 0.34630 0.38232 -0.03399 0.02187  0.02915  135 HIS B CA  
3280 C C   . HIS B 135 ? 0.31993 0.32731 0.35938 -0.03178 0.02366  0.03595  135 HIS B C   
3281 O O   . HIS B 135 ? 0.31170 0.31986 0.34193 -0.02643 0.02244  0.03424  135 HIS B O   
3282 C CB  . HIS B 135 ? 0.32560 0.34157 0.36684 -0.02968 0.02157  0.02262  135 HIS B CB  
3283 C CG  . HIS B 135 ? 0.32822 0.34554 0.37469 -0.03089 0.02027  0.01739  135 HIS B CG  
3284 N ND1 . HIS B 135 ? 0.29022 0.30169 0.33758 -0.03158 0.01663  0.01304  135 HIS B ND1 
3285 C CD2 . HIS B 135 ? 0.31392 0.33792 0.36396 -0.03033 0.02244  0.01637  135 HIS B CD2 
3286 C CE1 . HIS B 135 ? 0.29291 0.30641 0.34312 -0.03172 0.01639  0.01011  135 HIS B CE1 
3287 N NE2 . HIS B 135 ? 0.32855 0.34937 0.38088 -0.03075 0.01948  0.01184  135 HIS B NE2 
3288 N N   . PRO B 136 ? 0.33189 0.33549 0.37571 -0.03600 0.02612  0.04406  136 PRO B N   
3289 C CA  . PRO B 136 ? 0.32623 0.32363 0.36204 -0.03364 0.02793  0.05232  136 PRO B CA  
3290 C C   . PRO B 136 ? 0.35690 0.36312 0.38026 -0.02688 0.03138  0.05462  136 PRO B C   
3291 O O   . PRO B 136 ? 0.33831 0.33941 0.35148 -0.02204 0.03035  0.05874  136 PRO B O   
3292 C CB  . PRO B 136 ? 0.31276 0.30706 0.35802 -0.04130 0.03171  0.06153  136 PRO B CB  
3293 C CG  . PRO B 136 ? 0.36530 0.36168 0.42454 -0.04788 0.02891  0.05605  136 PRO B CG  
3294 C CD  . PRO B 136 ? 0.31202 0.31769 0.36924 -0.04352 0.02721  0.04650  136 PRO B CD  
3295 N N   . LEU B 137 ? 0.33170 0.35032 0.35417 -0.02520 0.03475  0.05140  137 LEU B N   
3296 C CA  . LEU B 137 ? 0.35056 0.37604 0.35845 -0.01776 0.03697  0.05171  137 LEU B CA  
3297 C C   . LEU B 137 ? 0.36395 0.38589 0.36266 -0.01240 0.02994  0.04538  137 LEU B C   
3298 O O   . LEU B 137 ? 0.37775 0.40201 0.36292 -0.00606 0.02948  0.04736  137 LEU B O   
3299 C CB  . LEU B 137 ? 0.32506 0.36191 0.33275 -0.01560 0.04057  0.04656  137 LEU B CB  
3300 C CG  . LEU B 137 ? 0.31918 0.35645 0.33109 -0.01559 0.03610  0.03497  137 LEU B CG  
3301 C CD1 . LEU B 137 ? 0.32597 0.36111 0.32712 -0.01078 0.03044  0.02705  137 LEU B CD1 
3302 C CD2 . LEU B 137 ? 0.28262 0.32910 0.29864 -0.01428 0.04091  0.03265  137 LEU B CD2 
3303 N N   . MET B 138 ? 0.31902 0.33685 0.32515 -0.01461 0.02447  0.03807  138 MET B N   
3304 C CA  . MET B 138 ? 0.37427 0.39173 0.37626 -0.01057 0.01807  0.03225  138 MET B CA  
3305 C C   . MET B 138 ? 0.37775 0.39027 0.37268 -0.00593 0.01601  0.03883  138 MET B C   
3306 O O   . MET B 138 ? 0.36173 0.37840 0.34999 -0.00030 0.01114  0.03592  138 MET B O   
3307 C CB  . MET B 138 ? 0.36127 0.37544 0.37387 -0.01414 0.01472  0.02584  138 MET B CB  
3308 C CG  . MET B 138 ? 0.34925 0.36778 0.36632 -0.01675 0.01486  0.01817  138 MET B CG  
3309 S SD  . MET B 138 ? 0.46081 0.47494 0.48798 -0.02035 0.01242  0.01323  138 MET B SD  
3310 C CE  . MET B 138 ? 0.40163 0.41743 0.42794 -0.01626 0.00788  0.01161  138 MET B CE  
3311 N N   . HIS B 139 ? 0.35488 0.35821 0.35168 -0.00821 0.01909  0.04779  139 HIS B N   
3312 C CA  . HIS B 139 ? 0.39253 0.38765 0.38187 -0.00324 0.01751  0.05544  139 HIS B CA  
3313 C C   . HIS B 139 ? 0.43078 0.43190 0.40437 0.00381  0.01862  0.06069  139 HIS B C   
3314 O O   . HIS B 139 ? 0.41863 0.41591 0.38349 0.01073  0.01511  0.06502  139 HIS B O   
3315 C CB  . HIS B 139 ? 0.42221 0.40389 0.41706 -0.00878 0.02120  0.06436  139 HIS B CB  
3316 C CG  . HIS B 139 ? 0.47295 0.44131 0.46060 -0.00387 0.01959  0.07276  139 HIS B CG  
3317 N ND1 . HIS B 139 ? 0.46204 0.42179 0.45105 0.00060  0.01371  0.06899  139 HIS B ND1 
3318 C CD2 . HIS B 139 ? 0.45745 0.41899 0.43590 -0.00188 0.02354  0.08541  139 HIS B CD2 
3319 C CE1 . HIS B 139 ? 0.46614 0.41316 0.44707 0.00564  0.01340  0.07848  139 HIS B CE1 
3320 N NE2 . HIS B 139 ? 0.49322 0.44044 0.46724 0.00389  0.01929  0.08900  139 HIS B NE2 
3321 N N   . TYR B 140 ? 0.38949 0.40002 0.35799 0.00353  0.02319  0.06021  140 TYR B N   
3322 C CA  . TYR B 140 ? 0.40947 0.42572 0.36007 0.01112  0.02491  0.06497  140 TYR B CA  
3323 C C   . TYR B 140 ? 0.42809 0.45488 0.37067 0.01630  0.01912  0.05340  140 TYR B C   
3324 O O   . TYR B 140 ? 0.43856 0.47040 0.36389 0.02384  0.01865  0.05505  140 TYR B O   
3325 C CB  . TYR B 140 ? 0.37740 0.39709 0.32532 0.00876  0.03536  0.07374  140 TYR B CB  
3326 C CG  . TYR B 140 ? 0.39656 0.40710 0.35675 0.00057  0.04115  0.08440  140 TYR B CG  
3327 C CD1 . TYR B 140 ? 0.40888 0.42002 0.38733 -0.00841 0.04247  0.08023  140 TYR B CD1 
3328 C CD2 . TYR B 140 ? 0.46520 0.46595 0.41841 0.00183  0.04449  0.09838  140 TYR B CD2 
3329 C CE1 . TYR B 140 ? 0.41611 0.41913 0.40666 -0.01670 0.04607  0.08866  140 TYR B CE1 
3330 C CE2 . TYR B 140 ? 0.45249 0.44335 0.41841 -0.00721 0.04904  0.10741  140 TYR B CE2 
3331 C CZ  . TYR B 140 ? 0.47576 0.46791 0.46115 -0.01701 0.04934  0.10206  140 TYR B CZ  
3332 O OH  . TYR B 140 ? 0.53123 0.51389 0.53000 -0.02669 0.05225  0.10978  140 TYR B OH  
3333 N N   . GLN B 141 ? 0.42590 0.45538 0.37974 0.01230  0.01470  0.04191  141 GLN B N   
3334 C CA  . GLN B 141 ? 0.40503 0.44232 0.35354 0.01556  0.00800  0.03057  141 GLN B CA  
3335 C C   . GLN B 141 ? 0.43912 0.47933 0.38151 0.02192  -0.00053 0.03002  141 GLN B C   
3336 O O   . GLN B 141 ? 0.47568 0.51239 0.42707 0.02149  -0.00326 0.03252  141 GLN B O   
3337 C CB  . GLN B 141 ? 0.40902 0.44665 0.37263 0.00884  0.00566  0.02050  141 GLN B CB  
3338 C CG  . GLN B 141 ? 0.39317 0.42979 0.36129 0.00456  0.01232  0.01925  141 GLN B CG  
3339 C CD  . GLN B 141 ? 0.47221 0.51301 0.43079 0.00776  0.01146  0.01068  141 GLN B CD  
3340 O OE1 . GLN B 141 ? 0.43896 0.48259 0.38596 0.01238  0.01687  0.01357  141 GLN B OE1 
3341 N NE2 . GLN B 141 ? 0.40225 0.44286 0.36576 0.00532  0.00507  0.00011  141 GLN B NE2 
3342 N N   . PRO B 142 ? 0.43861 0.48570 0.36573 0.02873  -0.00542 0.02621  142 PRO B N   
3343 C CA  . PRO B 142 ? 0.48300 0.53593 0.40593 0.03511  -0.01538 0.02437  142 PRO B CA  
3344 C C   . PRO B 142 ? 0.49667 0.55609 0.43691 0.03020  -0.02308 0.01322  142 PRO B C   
3345 O O   . PRO B 142 ? 0.43867 0.49809 0.38839 0.02301  -0.02208 0.00504  142 PRO B O   
3346 C CB  . PRO B 142 ? 0.50841 0.56753 0.40942 0.04303  -0.01902 0.02118  142 PRO B CB  
3347 C CG  . PRO B 142 ? 0.52947 0.58510 0.42213 0.04183  -0.00886 0.02334  142 PRO B CG  
3348 C CD  . PRO B 142 ? 0.47385 0.52443 0.38656 0.03170  -0.00278 0.02216  142 PRO B CD  
3349 N N   . LEU B 143 ? 0.51019 0.57595 0.45435 0.03483  -0.03071 0.01360  143 LEU B N   
3350 C CA  . LEU B 143 ? 0.50283 0.57785 0.46598 0.03041  -0.03715 0.00488  143 LEU B CA  
3351 C C   . LEU B 143 ? 0.50655 0.58917 0.47179 0.02556  -0.04319 -0.00802 143 LEU B C   
3352 O O   . LEU B 143 ? 0.50844 0.59296 0.49043 0.01712  -0.04321 -0.01454 143 LEU B O   
3353 C CB  . LEU B 143 ? 0.53271 0.61687 0.49833 0.03853  -0.04492 0.00756  143 LEU B CB  
3354 C CG  . LEU B 143 ? 0.50896 0.60897 0.49458 0.03518  -0.05276 -0.00164 143 LEU B CG  
3355 C CD1 . LEU B 143 ? 0.45941 0.55622 0.46436 0.02686  -0.04611 -0.00266 143 LEU B CD1 
3356 C CD2 . LEU B 143 ? 0.55348 0.66619 0.54065 0.04542  -0.06153 0.00083  143 LEU B CD2 
3357 N N   . GLU B 144 ? 0.47530 0.56096 0.42265 0.03094  -0.04839 -0.01183 144 GLU B N   
3358 C CA  . GLU B 144 ? 0.52104 0.61147 0.46837 0.02696  -0.05587 -0.02539 144 GLU B CA  
3359 C C   . GLU B 144 ? 0.52989 0.60924 0.47553 0.02079  -0.04874 -0.02995 144 GLU B C   
3360 O O   . GLU B 144 ? 0.50094 0.58037 0.44883 0.01617  -0.05444 -0.04165 144 GLU B O   
3361 C CB  . GLU B 144 ? 0.58233 0.67902 0.50808 0.03639  -0.06507 -0.02917 144 GLU B CB  
3362 C CG  . GLU B 144 ? 0.59245 0.68041 0.49227 0.04371  -0.05775 -0.02385 144 GLU B CG  
3363 C CD  . GLU B 144 ? 0.69519 0.78054 0.58385 0.05209  -0.05166 -0.00789 144 GLU B CD  
3364 O OE1 . GLU B 144 ? 0.68381 0.76955 0.58637 0.05128  -0.05089 -0.00051 144 GLU B OE1 
3365 O OE2 . GLU B 144 ? 0.67551 0.75748 0.54086 0.05978  -0.04715 -0.00249 144 GLU B OE2 
3366 N N   . ALA B 145 ? 0.45439 0.52419 0.39699 0.02063  -0.03710 -0.02131 145 ALA B N   
3367 C CA  . ALA B 145 ? 0.46866 0.52978 0.41172 0.01589  -0.03047 -0.02518 145 ALA B CA  
3368 C C   . ALA B 145 ? 0.43311 0.49234 0.39700 0.00576  -0.03161 -0.03135 145 ALA B C   
3369 O O   . ALA B 145 ? 0.44993 0.51409 0.42932 0.00213  -0.03331 -0.02904 145 ALA B O   
3370 C CB  . ALA B 145 ? 0.43454 0.48931 0.37470 0.01700  -0.01845 -0.01387 145 ALA B CB  
3371 N N   . PRO B 146 ? 0.42935 0.48110 0.39320 0.00187  -0.03023 -0.03874 146 PRO B N   
3372 C CA  . PRO B 146 ? 0.43630 0.48405 0.41854 -0.00769 -0.02980 -0.04247 146 PRO B CA  
3373 C C   . PRO B 146 ? 0.37583 0.42182 0.36961 -0.01051 -0.02171 -0.03295 146 PRO B C   
3374 O O   . PRO B 146 ? 0.34416 0.38569 0.33231 -0.00766 -0.01423 -0.02631 146 PRO B O   
3375 C CB  . PRO B 146 ? 0.42637 0.46275 0.40121 -0.00827 -0.02786 -0.04965 146 PRO B CB  
3376 C CG  . PRO B 146 ? 0.48343 0.52083 0.43647 0.00062  -0.03134 -0.05430 146 PRO B CG  
3377 C CD  . PRO B 146 ? 0.44300 0.48906 0.38855 0.00723  -0.02898 -0.04406 146 PRO B CD  
3378 N N   . PRO B 147 ? 0.38061 0.43098 0.39066 -0.01587 -0.02302 -0.03215 147 PRO B N   
3379 C CA  . PRO B 147 ? 0.33150 0.37939 0.34998 -0.01736 -0.01611 -0.02425 147 PRO B CA  
3380 C C   . PRO B 147 ? 0.32248 0.36007 0.34181 -0.02065 -0.00962 -0.02370 147 PRO B C   
3381 O O   . PRO B 147 ? 0.34078 0.37294 0.36040 -0.02393 -0.01050 -0.02972 147 PRO B O   
3382 C CB  . PRO B 147 ? 0.39053 0.44666 0.42512 -0.02163 -0.01896 -0.02540 147 PRO B CB  
3383 C CG  . PRO B 147 ? 0.42341 0.48555 0.46172 -0.02532 -0.02698 -0.03430 147 PRO B CG  
3384 C CD  . PRO B 147 ? 0.41943 0.48007 0.44028 -0.01934 -0.03130 -0.03772 147 PRO B CD  
3385 N N   . VAL B 148 ? 0.30993 0.34413 0.32935 -0.01937 -0.00376 -0.01652 148 VAL B N   
3386 C CA  . VAL B 148 ? 0.28414 0.31094 0.30471 -0.02130 0.00171  -0.01515 148 VAL B CA  
3387 C C   . VAL B 148 ? 0.29516 0.31973 0.32515 -0.02448 0.00444  -0.01151 148 VAL B C   
3388 O O   . VAL B 148 ? 0.29036 0.30977 0.32154 -0.02564 0.00802  -0.01000 148 VAL B O   
3389 C CB  . VAL B 148 ? 0.32676 0.35269 0.33866 -0.01708 0.00608  -0.01066 148 VAL B CB  
3390 C CG1 . VAL B 148 ? 0.30731 0.33450 0.30695 -0.01259 0.00456  -0.01539 148 VAL B CG1 
3391 C CG2 . VAL B 148 ? 0.30025 0.32834 0.31120 -0.01502 0.00743  -0.00274 148 VAL B CG2 
3392 N N   . SER B 149 ? 0.32438 0.35342 0.36054 -0.02494 0.00262  -0.01049 149 SER B N   
3393 C CA  . SER B 149 ? 0.29873 0.32532 0.34085 -0.02620 0.00540  -0.00757 149 SER B CA  
3394 C C   . SER B 149 ? 0.29421 0.32801 0.34476 -0.02700 0.00392  -0.00892 149 SER B C   
3395 O O   . SER B 149 ? 0.30342 0.34549 0.35583 -0.02469 0.00014  -0.00980 149 SER B O   
3396 C CB  . SER B 149 ? 0.34666 0.36964 0.38542 -0.02314 0.00682  -0.00219 149 SER B CB  
3397 O OG  . SER B 149 ? 0.42870 0.44639 0.47050 -0.02450 0.00908  -0.00098 149 SER B OG  
3398 N N   . LEU B 150 ? 0.27975 0.31177 0.33532 -0.02946 0.00713  -0.00852 150 LEU B N   
3399 C CA  . LEU B 150 ? 0.31476 0.35552 0.37938 -0.02992 0.00778  -0.00877 150 LEU B CA  
3400 C C   . LEU B 150 ? 0.34777 0.38400 0.41109 -0.02787 0.01211  -0.00617 150 LEU B C   
3401 O O   . LEU B 150 ? 0.33486 0.36262 0.39387 -0.02965 0.01451  -0.00544 150 LEU B O   
3402 C CB  . LEU B 150 ? 0.30717 0.35188 0.37975 -0.03648 0.00776  -0.01156 150 LEU B CB  
3403 C CG  . LEU B 150 ? 0.33722 0.39409 0.42259 -0.03872 0.00977  -0.01091 150 LEU B CG  
3404 C CD1 . LEU B 150 ? 0.32575 0.39743 0.41835 -0.03586 0.00471  -0.01262 150 LEU B CD1 
3405 C CD2 . LEU B 150 ? 0.30168 0.35722 0.39429 -0.04726 0.01127  -0.01198 150 LEU B CD2 
3406 N N   . SER B 151 ? 0.32183 0.43702 0.40955 0.02261  -0.02381 -0.06470 151 SER B N   
3407 C CA  . SER B 151 ? 0.31090 0.43441 0.40985 0.01365  -0.02302 -0.06068 151 SER B CA  
3408 C C   . SER B 151 ? 0.30219 0.40673 0.39805 0.01050  -0.02826 -0.05751 151 SER B C   
3409 O O   . SER B 151 ? 0.28954 0.38067 0.38414 0.00566  -0.02994 -0.05573 151 SER B O   
3410 C CB  . SER B 151 ? 0.32027 0.45064 0.42550 0.00187  -0.01730 -0.05774 151 SER B CB  
3411 O OG  . SER B 151 ? 0.35208 0.50225 0.46312 0.00100  -0.01060 -0.05646 151 SER B OG  
3412 N N   . VAL B 152 ? 0.29616 0.40307 0.39165 0.01332  -0.03084 -0.05530 152 VAL B N   
3413 C CA  . VAL B 152 ? 0.30361 0.39567 0.39418 0.01049  -0.03287 -0.04848 152 VAL B CA  
3414 C C   . VAL B 152 ? 0.31420 0.41864 0.40319 0.00703  -0.03023 -0.04724 152 VAL B C   
3415 O O   . VAL B 152 ? 0.33349 0.45159 0.42152 0.01157  -0.03377 -0.05007 152 VAL B O   
3416 C CB  . VAL B 152 ? 0.35810 0.43340 0.44072 0.01991  -0.03947 -0.04495 152 VAL B CB  
3417 C CG1 . VAL B 152 ? 0.34578 0.40429 0.42430 0.01318  -0.03937 -0.03332 152 VAL B CG1 
3418 C CG2 . VAL B 152 ? 0.34700 0.40688 0.42642 0.02691  -0.04395 -0.05160 152 VAL B CG2 
3419 N N   . ILE B 153 ? 0.29695 0.39870 0.38562 0.00048  -0.02503 -0.04447 153 ILE B N   
3420 C CA  . ILE B 153 ? 0.34058 0.45018 0.42314 -0.00090 -0.02221 -0.04775 153 ILE B CA  
3421 C C   . ILE B 153 ? 0.33459 0.44127 0.40509 0.00151  -0.01815 -0.03933 153 ILE B C   
3422 O O   . ILE B 153 ? 0.34556 0.44925 0.42164 -0.00174 -0.01186 -0.03160 153 ILE B O   
3423 C CB  . ILE B 153 ? 0.31662 0.42531 0.40556 -0.00598 -0.01764 -0.05276 153 ILE B CB  
3424 C CG1 . ILE B 153 ? 0.33981 0.45297 0.43747 -0.00939 -0.02002 -0.05742 153 ILE B CG1 
3425 C CG2 . ILE B 153 ? 0.32619 0.43451 0.40448 -0.00504 -0.01546 -0.05848 153 ILE B CG2 
3426 C CD1 . ILE B 153 ? 0.31709 0.42365 0.42003 -0.01282 -0.01637 -0.05671 153 ILE B CD1 
3427 N N   . PHE B 154 ? 0.32872 0.43984 0.38329 0.00722  -0.02189 -0.03950 154 PHE B N   
3428 C CA  . PHE B 154 ? 0.35772 0.46712 0.39423 0.01147  -0.01689 -0.02877 154 PHE B CA  
3429 C C   . PHE B 154 ? 0.35721 0.47353 0.37705 0.01489  -0.01236 -0.03692 154 PHE B C   
3430 O O   . PHE B 154 ? 0.33688 0.45735 0.34350 0.01845  -0.02142 -0.04767 154 PHE B O   
3431 C CB  . PHE B 154 ? 0.32427 0.43089 0.34644 0.01950  -0.02538 -0.02178 154 PHE B CB  
3432 C CG  . PHE B 154 ? 0.35316 0.44599 0.38600 0.02049  -0.03040 -0.01496 154 PHE B CG  
3433 C CD1 . PHE B 154 ? 0.37328 0.44753 0.40454 0.01729  -0.02653 0.00105  154 PHE B CD1 
3434 C CD2 . PHE B 154 ? 0.38774 0.48570 0.43171 0.02517  -0.03907 -0.02452 154 PHE B CD2 
3435 C CE1 . PHE B 154 ? 0.40382 0.45647 0.44117 0.01915  -0.03380 0.00450  154 PHE B CE1 
3436 C CE2 . PHE B 154 ? 0.34445 0.42638 0.39333 0.03077  -0.04376 -0.02116 154 PHE B CE2 
3437 C CZ  . PHE B 154 ? 0.35435 0.40960 0.39790 0.02820  -0.04253 -0.00810 154 PHE B CZ  
3438 N N   . PRO B 155 ? 0.37168 0.49045 0.39173 0.01513  0.00021  -0.03354 155 PRO B N   
3439 C CA  . PRO B 155 ? 0.38834 0.51105 0.38473 0.02388  0.00601  -0.04177 155 PRO B CA  
3440 C C   . PRO B 155 ? 0.39818 0.52515 0.36346 0.03247  0.00751  -0.03297 155 PRO B C   
3441 O O   . PRO B 155 ? 0.39153 0.52117 0.35662 0.03150  0.01559  -0.01299 155 PRO B O   
3442 C CB  . PRO B 155 ? 0.37093 0.50103 0.38086 0.02500  0.02129  -0.03672 155 PRO B CB  
3443 C CG  . PRO B 155 ? 0.34185 0.47556 0.37655 0.01518  0.02387  -0.01913 155 PRO B CG  
3444 C CD  . PRO B 155 ? 0.33005 0.45075 0.37285 0.00885  0.00879  -0.02311 155 PRO B CD  
3445 N N   . LEU B 156 ? 0.41527 0.54120 0.35275 0.04009  -0.00159 -0.04728 156 LEU B N   
3446 C CA  . LEU B 156 ? 0.42993 0.56029 0.32963 0.05134  -0.00169 -0.04025 156 LEU B CA  
3447 C C   . LEU B 156 ? 0.48139 0.61513 0.34754 0.06431  0.00937  -0.04867 156 LEU B C   
3448 O O   . LEU B 156 ? 0.46176 0.60110 0.29050 0.07584  0.01324  -0.04060 156 LEU B O   
3449 C CB  . LEU B 156 ? 0.40510 0.53566 0.29271 0.05341  -0.02392 -0.04979 156 LEU B CB  
3450 C CG  . LEU B 156 ? 0.46973 0.60018 0.38324 0.04786  -0.03225 -0.03808 156 LEU B CG  
3451 C CD1 . LEU B 156 ? 0.44379 0.58296 0.34652 0.05380  -0.05306 -0.04524 156 LEU B CD1 
3452 C CD2 . LEU B 156 ? 0.47438 0.59828 0.38489 0.04948  -0.02068 -0.01198 156 LEU B CD2 
3453 N N   . THR B 157 ? 0.45126 0.57995 0.32620 0.06520  0.01418  -0.06480 157 THR B N   
3454 C CA  . THR B 157 ? 0.52850 0.66143 0.38085 0.08033  0.03085  -0.07060 157 THR B CA  
3455 C C   . THR B 157 ? 0.50055 0.64112 0.39129 0.07646  0.04595  -0.06320 157 THR B C   
3456 O O   . THR B 157 ? 0.47715 0.61521 0.40548 0.06176  0.04044  -0.05714 157 THR B O   
3457 C CB  . THR B 157 ? 0.51777 0.63141 0.34114 0.08938  0.01859  -0.10139 157 THR B CB  
3458 O OG1 . THR B 157 ? 0.55907 0.65544 0.41467 0.07600  0.00663  -0.11419 157 THR B OG1 
3459 C CG2 . THR B 157 ? 0.49646 0.60631 0.28321 0.09251  -0.00055 -0.11081 157 THR B CG2 
3460 N N   . GLU B 158 ? 0.50554 0.65798 0.38555 0.09197  0.06461  -0.06440 158 GLU B N   
3461 C CA  . GLU B 158 ? 0.51122 0.67404 0.42829 0.09196  0.07611  -0.06074 158 GLU B CA  
3462 C C   . GLU B 158 ? 0.48451 0.62064 0.41891 0.08558  0.05986  -0.07913 158 GLU B C   
3463 O O   . GLU B 158 ? 0.51066 0.62060 0.42088 0.08936  0.04672  -0.10112 158 GLU B O   
3464 C CB  . GLU B 158 ? 0.48385 0.66473 0.38334 0.11560  0.09779  -0.06413 158 GLU B CB  
3465 C CG  . GLU B 158 ? 0.58469 0.73876 0.43880 0.13489  0.09088  -0.09422 158 GLU B CG  
3466 C CD  . GLU B 158 ? 0.73558 0.90708 0.56594 0.16418  0.11403  -0.09987 158 GLU B CD  
3467 O OE1 . GLU B 158 ? 0.74054 0.95283 0.59592 0.16844  0.13749  -0.07775 158 GLU B OE1 
3468 O OE2 . GLU B 158 ? 0.82001 0.96518 0.60697 0.18321  0.10838  -0.12721 158 GLU B OE2 
3469 N N   . PHE B 159 ? 0.39438 0.53616 0.36988 0.07421  0.05947  -0.06903 159 PHE B N   
3470 C CA  . PHE B 159 ? 0.46304 0.58451 0.45569 0.07209  0.05046  -0.08075 159 PHE B CA  
3471 C C   . PHE B 159 ? 0.43875 0.57389 0.44333 0.08931  0.06519  -0.08012 159 PHE B C   
3472 O O   . PHE B 159 ? 0.44014 0.60758 0.47288 0.08797  0.07658  -0.06238 159 PHE B O   
3473 C CB  . PHE B 159 ? 0.40553 0.52635 0.43070 0.05287  0.04047  -0.07036 159 PHE B CB  
3474 C CG  . PHE B 159 ? 0.42548 0.53106 0.44390 0.03940  0.02466  -0.07524 159 PHE B CG  
3475 C CD1 . PHE B 159 ? 0.42995 0.53243 0.42033 0.04138  0.01915  -0.08180 159 PHE B CD1 
3476 C CD2 . PHE B 159 ? 0.39579 0.49415 0.43632 0.02648  0.01527  -0.07296 159 PHE B CD2 
3477 C CE1 . PHE B 159 ? 0.43795 0.53437 0.42883 0.03019  0.00377  -0.08561 159 PHE B CE1 
3478 C CE2 . PHE B 159 ? 0.39607 0.48858 0.43526 0.01603  0.00319  -0.07638 159 PHE B CE2 
3479 C CZ  . PHE B 159 ? 0.40336 0.49667 0.42088 0.01770  -0.00295 -0.08272 159 PHE B CZ  
3480 N N   . THR B 160 ? 0.46753 0.57833 0.45262 0.10562  0.06390  -0.09951 160 THR B N   
3481 C CA  . THR B 160 ? 0.49324 0.61407 0.48723 0.12794  0.07690  -0.10163 160 THR B CA  
3482 C C   . THR B 160 ? 0.57254 0.65538 0.57234 0.13020  0.06427  -0.11333 160 THR B C   
3483 O O   . THR B 160 ? 0.52333 0.57209 0.51630 0.11396  0.04754  -0.12089 160 THR B O   
3484 C CB  . THR B 160 ? 0.54355 0.66658 0.49913 0.15450  0.09056  -0.11516 160 THR B CB  
3485 O OG1 . THR B 160 ? 0.55587 0.62786 0.47622 0.16119  0.07600  -0.14200 160 THR B OG1 
3486 C CG2 . THR B 160 ? 0.51069 0.65874 0.44513 0.15047  0.09938  -0.10508 160 THR B CG2 
3487 N N   . GLU B 161 ? 0.56058 0.65151 0.57469 0.15109  0.07298  -0.11278 161 GLU B N   
3488 C CA  . GLU B 161 ? 0.65117 0.70113 0.66662 0.15730  0.06174  -0.12164 161 GLU B CA  
3489 C C   . GLU B 161 ? 0.64509 0.63894 0.61941 0.16194  0.05136  -0.14639 161 GLU B C   
3490 O O   . GLU B 161 ? 0.68296 0.63381 0.65550 0.14834  0.03568  -0.15117 161 GLU B O   
3491 C CB  . GLU B 161 ? 0.62720 0.69670 0.66167 0.18565  0.07284  -0.11795 161 GLU B CB  
3492 C CG  . GLU B 161 ? 0.79483 0.81494 0.82507 0.19695  0.06109  -0.12595 161 GLU B CG  
3493 C CD  . GLU B 161 ? 0.91570 0.95371 0.96140 0.23207  0.07120  -0.12443 161 GLU B CD  
3494 O OE1 . GLU B 161 ? 0.92275 1.02334 0.99661 0.24163  0.08633  -0.11216 161 GLU B OE1 
3495 O OE2 . GLU B 161 ? 0.98099 0.97073 1.01254 0.25029  0.06375  -0.13457 161 GLU B OE2 
3496 N N   . GLU B 162 ? 0.62196 0.61565 0.56189 0.17938  0.05930  -0.16190 162 GLU B N   
3497 C CA  . GLU B 162 ? 0.67325 0.61046 0.57092 0.18630  0.04695  -0.18969 162 GLU B CA  
3498 C C   . GLU B 162 ? 0.63063 0.54967 0.51652 0.15606  0.02845  -0.19541 162 GLU B C   
3499 O O   . GLU B 162 ? 0.67748 0.54524 0.54809 0.14664  0.01049  -0.21241 162 GLU B O   
3500 C CB  . GLU B 162 ? 0.73246 0.67547 0.59091 0.21966  0.06123  -0.20723 162 GLU B CB  
3501 C CG  . GLU B 162 ? 0.83928 0.82474 0.71740 0.24966  0.08512  -0.19594 162 GLU B CG  
3502 C CD  . GLU B 162 ? 0.84684 0.90507 0.75801 0.24031  0.10265  -0.16807 162 GLU B CD  
3503 O OE1 . GLU B 162 ? 0.81549 0.88743 0.71468 0.22127  0.10112  -0.16224 162 GLU B OE1 
3504 O OE2 . GLU B 162 ? 0.85085 0.95074 0.80168 0.24994  0.11570  -0.15090 162 GLU B OE2 
3505 N N   . ASN B 163 ? 0.54858 0.50808 0.44288 0.14048  0.03142  -0.18119 163 ASN B N   
3506 C CA  . ASN B 163 ? 0.58559 0.53366 0.46643 0.11809  0.01385  -0.18850 163 ASN B CA  
3507 C C   . ASN B 163 ? 0.57263 0.52431 0.48963 0.08828  0.00298  -0.17329 163 ASN B C   
3508 O O   . ASN B 163 ? 0.55830 0.51150 0.47330 0.06966  -0.01037 -0.17569 163 ASN B O   
3509 C CB  . ASN B 163 ? 0.56088 0.54308 0.41851 0.12309  0.02078  -0.18511 163 ASN B CB  
3510 C CG  . ASN B 163 ? 0.55565 0.58322 0.44453 0.11020  0.03035  -0.15632 163 ASN B CG  
3511 O OD1 . ASN B 163 ? 0.48448 0.52133 0.41187 0.09795  0.03139  -0.14069 163 ASN B OD1 
3512 N ND2 . ASN B 163 ? 0.55693 0.60907 0.42476 0.11344  0.03591  -0.14966 163 ASN B ND2 
3513 N N   . GLY B 164 ? 0.54959 0.50571 0.49827 0.08553  0.00821  -0.15799 164 GLY B N   
3514 C CA  . GLY B 164 ? 0.49835 0.44888 0.47327 0.06101  -0.00195 -0.14728 164 GLY B CA  
3515 C C   . GLY B 164 ? 0.49091 0.48085 0.49431 0.05075  0.00376  -0.12543 164 GLY B C   
3516 O O   . GLY B 164 ? 0.43480 0.42814 0.45218 0.03136  -0.00430 -0.11906 164 GLY B O   
3517 N N   . ALA B 165 ? 0.44935 0.46957 0.46263 0.06339  0.01728  -0.11431 165 ALA B N   
3518 C CA  . ALA B 165 ? 0.40851 0.45931 0.44870 0.05274  0.01997  -0.09540 165 ALA B CA  
3519 C C   . ALA B 165 ? 0.40450 0.44292 0.46237 0.03929  0.01118  -0.08906 165 ALA B C   
3520 O O   . ALA B 165 ? 0.40619 0.42097 0.46464 0.04413  0.00883  -0.09136 165 ALA B O   
3521 C CB  . ALA B 165 ? 0.40204 0.48280 0.45860 0.06627  0.03342  -0.08453 165 ALA B CB  
3522 N N   . THR B 166 ? 0.37027 0.42311 0.43933 0.02444  0.00687  -0.08048 166 THR B N   
3523 C CA  . THR B 166 ? 0.35863 0.40422 0.43936 0.01277  0.00050  -0.07439 166 THR B CA  
3524 C C   . THR B 166 ? 0.34504 0.38809 0.43679 0.02025  0.00199  -0.06646 166 THR B C   
3525 O O   . THR B 166 ? 0.32412 0.38798 0.42776 0.02842  0.00611  -0.06035 166 THR B O   
3526 C CB  . THR B 166 ? 0.36702 0.43274 0.45656 0.00285  -0.00199 -0.06705 166 THR B CB  
3527 O OG1 . THR B 166 ? 0.32316 0.39605 0.40272 0.00075  -0.00354 -0.07192 166 THR B OG1 
3528 C CG2 . THR B 166 ? 0.34087 0.40122 0.43595 -0.00764 -0.00679 -0.06368 166 THR B CG2 
3529 N N   . GLU B 167 ? 0.37216 0.39110 0.46112 0.01673  -0.00211 -0.06505 167 GLU B N   
3530 C CA  . GLU B 167 ? 0.36472 0.37740 0.45935 0.02497  -0.00314 -0.05590 167 GLU B CA  
3531 C C   . GLU B 167 ? 0.36702 0.39200 0.46720 0.01509  -0.00681 -0.04555 167 GLU B C   
3532 O O   . GLU B 167 ? 0.37394 0.39325 0.46978 0.00215  -0.00768 -0.04435 167 GLU B O   
3533 C CB  . GLU B 167 ? 0.38800 0.35998 0.47069 0.02841  -0.00524 -0.05826 167 GLU B CB  
3534 C CG  . GLU B 167 ? 0.47314 0.42793 0.54397 0.04026  -0.00289 -0.07339 167 GLU B CG  
3535 C CD  . GLU B 167 ? 0.58882 0.49329 0.64411 0.03842  -0.00812 -0.08075 167 GLU B CD  
3536 O OE1 . GLU B 167 ? 0.62633 0.50819 0.68243 0.02660  -0.01216 -0.07039 167 GLU B OE1 
3537 O OE2 . GLU B 167 ? 0.65685 0.54218 0.69692 0.04892  -0.00812 -0.09701 167 GLU B OE2 
3538 N N   . VAL B 168 ? 0.31602 0.36040 0.42616 0.02168  -0.00931 -0.03899 168 VAL B N   
3539 C CA  . VAL B 168 ? 0.33759 0.39342 0.44803 0.01545  -0.01454 -0.03285 168 VAL B CA  
3540 C C   . VAL B 168 ? 0.37173 0.42592 0.48184 0.02582  -0.02072 -0.02440 168 VAL B C   
3541 O O   . VAL B 168 ? 0.35124 0.41561 0.47379 0.03774  -0.02249 -0.02349 168 VAL B O   
3542 C CB  . VAL B 168 ? 0.35474 0.43465 0.47598 0.01103  -0.01657 -0.03532 168 VAL B CB  
3543 C CG1 . VAL B 168 ? 0.34087 0.42524 0.45665 0.00657  -0.02366 -0.03327 168 VAL B CG1 
3544 C CG2 . VAL B 168 ? 0.35517 0.43644 0.47430 0.00464  -0.01126 -0.04166 168 VAL B CG2 
3545 N N   . ILE B 169 ? 0.33842 0.38288 0.43396 0.02311  -0.02351 -0.01721 169 ILE B N   
3546 C CA  . ILE B 169 ? 0.36529 0.40797 0.45405 0.03404  -0.03148 -0.00779 169 ILE B CA  
3547 C C   . ILE B 169 ? 0.36807 0.43226 0.45547 0.03208  -0.04086 -0.00967 169 ILE B C   
3548 O O   . ILE B 169 ? 0.39453 0.45684 0.46563 0.02594  -0.03940 -0.00983 169 ILE B O   
3549 C CB  . ILE B 169 ? 0.38231 0.39683 0.44968 0.03364  -0.02815 0.00399  169 ILE B CB  
3550 C CG1 . ILE B 169 ? 0.39061 0.37553 0.45885 0.03114  -0.02108 0.00289  169 ILE B CG1 
3551 C CG2 . ILE B 169 ? 0.38897 0.40032 0.44563 0.04893  -0.03788 0.01556  169 ILE B CG2 
3552 C CD1 . ILE B 169 ? 0.45035 0.40236 0.50072 0.02556  -0.01742 0.01726  169 ILE B CD1 
3553 N N   . LEU B 170 ? 0.37166 0.45695 0.47687 0.03760  -0.05087 -0.01176 170 LEU B N   
3554 C CA  . LEU B 170 ? 0.38644 0.48796 0.49253 0.03321  -0.06354 -0.01662 170 LEU B CA  
3555 C C   . LEU B 170 ? 0.40797 0.50173 0.48549 0.04014  -0.07291 -0.01183 170 LEU B C   
3556 O O   . LEU B 170 ? 0.39873 0.48421 0.46593 0.05146  -0.07491 -0.00139 170 LEU B O   
3557 C CB  . LEU B 170 ? 0.39958 0.52879 0.53762 0.03452  -0.07348 -0.01792 170 LEU B CB  
3558 C CG  . LEU B 170 ? 0.35189 0.49414 0.51676 0.03250  -0.06158 -0.01870 170 LEU B CG  
3559 C CD1 . LEU B 170 ? 0.40557 0.58381 0.60661 0.03131  -0.06985 -0.01696 170 LEU B CD1 
3560 C CD2 . LEU B 170 ? 0.37407 0.50629 0.53294 0.01990  -0.05118 -0.02449 170 LEU B CD2 
3561 N N   . GLY B 171 ? 0.40168 0.49568 0.46252 0.03551  -0.07856 -0.01935 171 GLY B N   
3562 C CA  . GLY B 171 ? 0.43602 0.52419 0.46256 0.04375  -0.08646 -0.01695 171 GLY B CA  
3563 C C   . GLY B 171 ? 0.44760 0.52051 0.44628 0.04562  -0.07010 -0.00697 171 GLY B C   
3564 O O   . GLY B 171 ? 0.48864 0.55862 0.45348 0.05325  -0.07257 -0.00364 171 GLY B O   
3565 N N   . SER B 172 ? 0.40190 0.46663 0.41325 0.03805  -0.05365 -0.00213 172 SER B N   
3566 C CA  . SER B 172 ? 0.44655 0.49785 0.43983 0.03600  -0.03880 0.01138  172 SER B CA  
3567 C C   . SER B 172 ? 0.42616 0.48635 0.40222 0.03265  -0.02875 0.00867  172 SER B C   
3568 O O   . SER B 172 ? 0.42077 0.47730 0.38176 0.03031  -0.01541 0.02237  172 SER B O   
3569 C CB  . SER B 172 ? 0.42587 0.46391 0.44021 0.02695  -0.02815 0.01480  172 SER B CB  
3570 O OG  . SER B 172 ? 0.39274 0.44100 0.42841 0.01789  -0.02474 0.00148  172 SER B OG  
3571 N N   . HIS B 173 ? 0.39988 0.47153 0.37864 0.03301  -0.03413 -0.00746 173 HIS B N   
3572 C CA  . HIS B 173 ? 0.41350 0.49435 0.37201 0.03667  -0.02575 -0.01179 173 HIS B CA  
3573 C C   . HIS B 173 ? 0.48658 0.56703 0.40402 0.05027  -0.02882 -0.00669 173 HIS B C   
3574 O O   . HIS B 173 ? 0.48434 0.57466 0.37948 0.05605  -0.01597 -0.00488 173 HIS B O   
3575 C CB  . HIS B 173 ? 0.40647 0.49118 0.37435 0.03696  -0.03331 -0.03104 173 HIS B CB  
3576 C CG  . HIS B 173 ? 0.43134 0.50944 0.39931 0.03978  -0.05505 -0.04209 173 HIS B CG  
3577 N ND1 . HIS B 173 ? 0.43524 0.51348 0.43076 0.03299  -0.06424 -0.04021 173 HIS B ND1 
3578 C CD2 . HIS B 173 ? 0.44687 0.51956 0.39283 0.04778  -0.07014 -0.05579 173 HIS B CD2 
3579 C CE1 . HIS B 173 ? 0.48359 0.56137 0.47932 0.03406  -0.08390 -0.05007 173 HIS B CE1 
3580 N NE2 . HIS B 173 ? 0.49556 0.56640 0.46018 0.04208  -0.08955 -0.06073 173 HIS B NE2 
3581 N N   . ARG B 174 ? 0.47632 0.54902 0.38253 0.05724  -0.04497 -0.00338 174 ARG B N   
3582 C CA  . ARG B 174 ? 0.51220 0.58340 0.37392 0.07169  -0.04951 0.00381  174 ARG B CA  
3583 C C   . ARG B 174 ? 0.58181 0.64576 0.42820 0.07200  -0.03408 0.03082  174 ARG B C   
3584 O O   . ARG B 174 ? 0.61267 0.67500 0.41740 0.08483  -0.03533 0.04142  174 ARG B O   
3585 C CB  . ARG B 174 ? 0.52414 0.59323 0.38019 0.07989  -0.07749 -0.00433 174 ARG B CB  
3586 C CG  . ARG B 174 ? 0.54424 0.61610 0.40661 0.07855  -0.09567 -0.03009 174 ARG B CG  
3587 C CD  . ARG B 174 ? 0.57049 0.64474 0.42767 0.08429  -0.12625 -0.03800 174 ARG B CD  
3588 N NE  . ARG B 174 ? 0.63334 0.71645 0.53496 0.07693  -0.13385 -0.03086 174 ARG B NE  
3589 C CZ  . ARG B 174 ? 0.55552 0.64594 0.50089 0.06351  -0.13829 -0.03986 174 ARG B CZ  
3590 N NH1 . ARG B 174 ? 0.52481 0.60953 0.47565 0.05467  -0.13923 -0.05591 174 ARG B NH1 
3591 N NH2 . ARG B 174 ? 0.52766 0.63083 0.51069 0.06062  -0.14070 -0.03133 174 ARG B NH2 
3592 N N   . TRP B 175 ? 0.53020 0.58666 0.40548 0.05819  -0.02055 0.04260  175 TRP B N   
3593 C CA  . TRP B 175 ? 0.56650 0.60820 0.42848 0.05550  -0.00750 0.06947  175 TRP B CA  
3594 C C   . TRP B 175 ? 0.63416 0.69050 0.47934 0.05079  0.01586  0.08124  175 TRP B C   
3595 O O   . TRP B 175 ? 0.57321 0.65092 0.43213 0.04599  0.02509  0.06849  175 TRP B O   
3596 C CB  . TRP B 175 ? 0.56504 0.58735 0.46203 0.04160  -0.00344 0.07595  175 TRP B CB  
3597 C CG  . TRP B 175 ? 0.59973 0.61076 0.51557 0.04838  -0.02138 0.06791  175 TRP B CG  
3598 C CD1 . TRP B 175 ? 0.55095 0.57133 0.46176 0.06264  -0.04149 0.05850  175 TRP B CD1 
3599 C CD2 . TRP B 175 ? 0.52056 0.51223 0.46490 0.04189  -0.02055 0.06813  175 TRP B CD2 
3600 N NE1 . TRP B 175 ? 0.51451 0.52861 0.45337 0.06574  -0.05078 0.05513  175 TRP B NE1 
3601 C CE2 . TRP B 175 ? 0.49068 0.48523 0.44697 0.05514  -0.03750 0.05998  175 TRP B CE2 
3602 C CE3 . TRP B 175 ? 0.53679 0.50959 0.49749 0.02633  -0.00807 0.07324  175 TRP B CE3 
3603 C CZ2 . TRP B 175 ? 0.47570 0.45600 0.45651 0.05712  -0.03926 0.05699  175 TRP B CZ2 
3604 C CZ3 . TRP B 175 ? 0.50773 0.45975 0.48868 0.02735  -0.01284 0.06770  175 TRP B CZ3 
3605 C CH2 . TRP B 175 ? 0.49848 0.45471 0.48764 0.04451  -0.02679 0.05985  175 TRP B CH2 
3606 N N   . THR B 176 ? 0.70414 0.75039 0.52107 0.05274  0.02641  0.10809  176 THR B N   
3607 C CA  . THR B 176 ? 0.70987 0.77494 0.51465 0.04617  0.05254  0.12522  176 THR B CA  
3608 C C   . THR B 176 ? 0.69506 0.76358 0.54609 0.02048  0.06761  0.13082  176 THR B C   
3609 O O   . THR B 176 ? 0.68067 0.78106 0.54994 0.01413  0.08085  0.12294  176 THR B O   
3610 C CB  . THR B 176 ? 0.74664 0.79760 0.50793 0.05355  0.06009  0.15657  176 THR B CB  
3611 O OG1 . THR B 176 ? 0.88350 0.89599 0.65766 0.04520  0.05324  0.17368  176 THR B OG1 
3612 C CG2 . THR B 176 ? 0.79554 0.84813 0.50744 0.08041  0.04245  0.14779  176 THR B CG2 
3613 N N   . GLU B 177 ? 0.74351 0.77909 0.61440 0.00698  0.06351  0.14216  177 GLU B N   
3614 C CA  . GLU B 177 ? 0.72917 0.76192 0.64222 -0.01865 0.07249  0.14444  177 GLU B CA  
3615 C C   . GLU B 177 ? 0.68713 0.69552 0.62719 -0.02083 0.05423  0.12461  177 GLU B C   
3616 O O   . GLU B 177 ? 0.69154 0.68692 0.62110 -0.00383 0.03739  0.11414  177 GLU B O   
3617 C CB  . GLU B 177 ? 0.78280 0.79284 0.69270 -0.03643 0.08709  0.17826  177 GLU B CB  
3618 C CG  . GLU B 177 ? 0.85564 0.81463 0.74180 -0.02768 0.07539  0.19424  177 GLU B CG  
3619 C CD  . GLU B 177 ? 1.05407 0.97840 0.94288 -0.04954 0.08766  0.22690  177 GLU B CD  
3620 O OE1 . GLU B 177 ? 1.10475 1.05423 1.00344 -0.06929 0.10893  0.24448  177 GLU B OE1 
3621 O OE2 . GLU B 177 ? 1.13165 1.00357 1.01444 -0.04699 0.07614  0.23560  177 GLU B OE2 
3622 N N   . VAL B 178 ? 0.64647 0.65298 0.62219 -0.04158 0.05755  0.11908  178 VAL B N   
3623 C CA  . VAL B 178 ? 0.61717 0.59705 0.61296 -0.04313 0.04287  0.10239  178 VAL B CA  
3624 C C   . VAL B 178 ? 0.65331 0.58253 0.63728 -0.04162 0.03739  0.11791  178 VAL B C   
3625 O O   . VAL B 178 ? 0.66310 0.57151 0.64474 -0.02615 0.02363  0.10771  178 VAL B O   
3626 C CB  . VAL B 178 ? 0.57757 0.56889 0.60909 -0.06403 0.04530  0.09001  178 VAL B CB  
3627 C CG1 . VAL B 178 ? 0.47328 0.43275 0.51754 -0.06411 0.03156  0.07369  178 VAL B CG1 
3628 C CG2 . VAL B 178 ? 0.51085 0.54881 0.55334 -0.05962 0.04766  0.07328  178 VAL B CG2 
3629 N N   . GLY B 179 ? 0.68245 0.59166 0.65923 -0.05644 0.04866  0.14438  179 GLY B N   
3630 C CA  . GLY B 179 ? 0.73515 0.58676 0.70178 -0.05686 0.04310  0.16001  179 GLY B CA  
3631 C C   . GLY B 179 ? 0.73433 0.55338 0.72602 -0.06650 0.03303  0.14146  179 GLY B C   
3632 O O   . GLY B 179 ? 0.73927 0.57730 0.75846 -0.08427 0.03427  0.12550  179 GLY B O   
3633 N N   . THR B 180 ? 0.75194 0.52147 0.73139 -0.05165 0.02196  0.14276  180 THR B N   
3634 C CA  . THR B 180 ? 0.77377 0.50459 0.76761 -0.05356 0.01162  0.12345  180 THR B CA  
3635 C C   . THR B 180 ? 0.73911 0.46723 0.72589 -0.02054 -0.00030 0.10752  180 THR B C   
3636 O O   . THR B 180 ? 0.76606 0.44776 0.73930 -0.00352 -0.00759 0.11375  180 THR B O   
3637 C CB  . THR B 180 ? 0.87165 0.53486 0.85910 -0.06859 0.01095  0.14181  180 THR B CB  
3638 O OG1 . THR B 180 ? 0.90528 0.53661 0.86291 -0.04876 0.00968  0.16684  180 THR B OG1 
3639 C CG2 . THR B 180 ? 0.82968 0.50247 0.83325 -0.10646 0.02339  0.15896  180 THR B CG2 
3640 N N   . PRO B 181 ? 0.73777 0.51602 0.73537 -0.01045 -0.00234 0.08820  181 PRO B N   
3641 C CA  . PRO B 181 ? 0.69722 0.48397 0.69404 0.01860  -0.01217 0.07668  181 PRO B CA  
3642 C C   . PRO B 181 ? 0.72550 0.47874 0.72990 0.02788  -0.01761 0.05953  181 PRO B C   
3643 O O   . PRO B 181 ? 0.72947 0.46421 0.74189 0.01088  -0.01607 0.04732  181 PRO B O   
3644 C CB  . PRO B 181 ? 0.60543 0.45096 0.61580 0.01849  -0.01163 0.06114  181 PRO B CB  
3645 C CG  . PRO B 181 ? 0.59182 0.45101 0.61385 -0.00719 -0.00317 0.05577  181 PRO B CG  
3646 C CD  . PRO B 181 ? 0.67290 0.50222 0.68597 -0.02503 0.00408  0.07736  181 PRO B CD  
3647 N N   . GLU B 182 ? 0.69304 0.44144 0.69444 0.05702  -0.02484 0.05755  182 GLU B N   
3648 C CA  . GLU B 182 ? 0.78037 0.50337 0.78665 0.07328  -0.02820 0.03940  182 GLU B CA  
3649 C C   . GLU B 182 ? 0.70779 0.47986 0.73365 0.07601  -0.02574 0.01652  182 GLU B C   
3650 O O   . GLU B 182 ? 0.62424 0.44803 0.66142 0.07484  -0.02516 0.01693  182 GLU B O   
3651 C CB  . GLU B 182 ? 0.78983 0.49136 0.78758 0.10707  -0.03559 0.04806  182 GLU B CB  
3652 C CG  . GLU B 182 ? 0.94143 0.59990 0.93647 0.12647  -0.03766 0.03169  182 GLU B CG  
3653 C CD  . GLU B 182 ? 1.07684 0.67131 1.05887 0.10390  -0.03730 0.02716  182 GLU B CD  
3654 O OE1 . GLU B 182 ? 1.16728 0.70698 1.13254 0.09806  -0.04037 0.04725  182 GLU B OE1 
3655 O OE2 . GLU B 182 ? 1.00514 0.60409 0.99353 0.09091  -0.03509 0.00453  182 GLU B OE2 
3656 N N   . ARG B 183 ? 0.68221 0.43404 0.70890 0.07948  -0.02477 -0.00336 183 ARG B N   
3657 C CA  . ARG B 183 ? 0.68411 0.47903 0.72460 0.08156  -0.02059 -0.02257 183 ARG B CA  
3658 C C   . ARG B 183 ? 0.63687 0.47959 0.69329 0.10454  -0.02013 -0.02096 183 ARG B C   
3659 O O   . ARG B 183 ? 0.58081 0.47258 0.65272 0.09760  -0.01714 -0.02482 183 ARG B O   
3660 C CB  . ARG B 183 ? 0.73494 0.49597 0.76549 0.08825  -0.02027 -0.04407 183 ARG B CB  
3661 C CG  . ARG B 183 ? 0.75529 0.47581 0.77581 0.06085  -0.02400 -0.04975 183 ARG B CG  
3662 C CD  . ARG B 183 ? 0.69757 0.46114 0.73004 0.03569  -0.02143 -0.05437 183 ARG B CD  
3663 N NE  . ARG B 183 ? 0.74899 0.48333 0.77976 0.00667  -0.02629 -0.05532 183 ARG B NE  
3664 C CZ  . ARG B 183 ? 0.71190 0.47670 0.75422 -0.01661 -0.02628 -0.05879 183 ARG B CZ  
3665 N NH1 . ARG B 183 ? 0.58715 0.40494 0.63871 -0.01356 -0.02184 -0.06244 183 ARG B NH1 
3666 N NH2 . ARG B 183 ? 0.69034 0.43170 0.73708 -0.04387 -0.03164 -0.05771 183 ARG B NH2 
3667 N N   . ASP B 184 ? 0.62427 0.45373 0.67936 0.13148  -0.02419 -0.01417 184 ASP B N   
3668 C CA  . ASP B 184 ? 0.59601 0.47635 0.67321 0.15369  -0.02495 -0.01309 184 ASP B CA  
3669 C C   . ASP B 184 ? 0.55698 0.48073 0.64616 0.14346  -0.03137 0.00010  184 ASP B C   
3670 O O   . ASP B 184 ? 0.59505 0.56654 0.70797 0.15580  -0.03449 0.00086  184 ASP B O   
3671 C CB  . ASP B 184 ? 0.66849 0.52554 0.74300 0.18850  -0.02914 -0.00920 184 ASP B CB  
3672 C CG  . ASP B 184 ? 0.80243 0.60734 0.85428 0.18972  -0.03795 0.00921  184 ASP B CG  
3673 O OD1 . ASP B 184 ? 0.79703 0.61961 0.84716 0.17894  -0.04400 0.02590  184 ASP B OD1 
3674 O OD2 . ASP B 184 ? 0.91401 0.65738 0.94681 0.20227  -0.03903 0.00732  184 ASP B OD2 
3675 N N   . GLN B 185 ? 0.55748 0.46783 0.63147 0.12150  -0.03355 0.00971  185 GLN B N   
3676 C CA  . GLN B 185 ? 0.52901 0.47863 0.60856 0.11126  -0.03925 0.01658  185 GLN B CA  
3677 C C   . GLN B 185 ? 0.49734 0.48369 0.59272 0.09397  -0.03440 0.00423  185 GLN B C   
3678 O O   . GLN B 185 ? 0.46296 0.48271 0.56670 0.08826  -0.04071 0.00582  185 GLN B O   
3679 C CB  . GLN B 185 ? 0.57544 0.50079 0.62955 0.09711  -0.04027 0.03106  185 GLN B CB  
3680 C CG  . GLN B 185 ? 0.63732 0.52259 0.67022 0.11145  -0.04524 0.04922  185 GLN B CG  
3681 C CD  . GLN B 185 ? 0.66325 0.52818 0.67049 0.09414  -0.04150 0.06598  185 GLN B CD  
3682 O OE1 . GLN B 185 ? 0.74347 0.56197 0.73624 0.08650  -0.03613 0.07644  185 GLN B OE1 
3683 N NE2 . GLN B 185 ? 0.59033 0.48966 0.59163 0.08764  -0.04391 0.06862  185 GLN B NE2 
3684 N N   . ALA B 186 ? 0.45018 0.42686 0.54648 0.08573  -0.02514 -0.00801 186 ALA B N   
3685 C CA  . ALA B 186 ? 0.41987 0.42563 0.52709 0.07085  -0.02047 -0.01759 186 ALA B CA  
3686 C C   . ALA B 186 ? 0.42198 0.46142 0.55117 0.08271  -0.01656 -0.02417 186 ALA B C   
3687 O O   . ALA B 186 ? 0.42073 0.45765 0.55497 0.10336  -0.01395 -0.02600 186 ALA B O   
3688 C CB  . ALA B 186 ? 0.40535 0.38665 0.50024 0.05552  -0.01419 -0.02614 186 ALA B CB  
3689 N N   . VAL B 187 ? 0.35379 0.42500 0.49613 0.07024  -0.01515 -0.02656 187 VAL B N   
3690 C CA  . VAL B 187 ? 0.36067 0.46480 0.52303 0.07536  -0.00762 -0.03014 187 VAL B CA  
3691 C C   . VAL B 187 ? 0.39723 0.49442 0.54745 0.06358  0.00073  -0.03847 187 VAL B C   
3692 O O   . VAL B 187 ? 0.32473 0.40244 0.45963 0.04904  -0.00202 -0.04086 187 VAL B O   
3693 C CB  . VAL B 187 ? 0.38254 0.52886 0.57284 0.06914  -0.01430 -0.02306 187 VAL B CB  
3694 C CG1 . VAL B 187 ? 0.38382 0.54336 0.58789 0.08335  -0.02525 -0.01580 187 VAL B CG1 
3695 C CG2 . VAL B 187 ? 0.33879 0.48037 0.52114 0.04845  -0.02167 -0.02299 187 VAL B CG2 
3696 N N   . LEU B 188 ? 0.32500 0.44307 0.48264 0.07115  0.01130  -0.04174 188 LEU B N   
3697 C CA  . LEU B 188 ? 0.37871 0.48908 0.51880 0.06574  0.01890  -0.04996 188 LEU B CA  
3698 C C   . LEU B 188 ? 0.34695 0.48578 0.49878 0.05185  0.02150  -0.04310 188 LEU B C   
3699 O O   . LEU B 188 ? 0.32719 0.50011 0.50393 0.05285  0.02540  -0.03401 188 LEU B O   
3700 C CB  . LEU B 188 ? 0.37260 0.48149 0.50225 0.08644  0.03032  -0.05887 188 LEU B CB  
3701 C CG  . LEU B 188 ? 0.42459 0.49372 0.53714 0.10249  0.02734  -0.06850 188 LEU B CG  
3702 C CD1 . LEU B 188 ? 0.50438 0.57140 0.60161 0.12631  0.03911  -0.08102 188 LEU B CD1 
3703 C CD2 . LEU B 188 ? 0.43057 0.45718 0.52233 0.08594  0.01757  -0.07453 188 LEU B CD2 
3704 N N   . ALA B 189 ? 0.33255 0.45735 0.46831 0.03878  0.01878  -0.04651 189 ALA B N   
3705 C CA  . ALA B 189 ? 0.33443 0.47628 0.47425 0.02808  0.02126  -0.04005 189 ALA B CA  
3706 C C   . ALA B 189 ? 0.37902 0.52900 0.50402 0.03640  0.03367  -0.04226 189 ALA B C   
3707 O O   . ALA B 189 ? 0.41253 0.55213 0.51664 0.03238  0.03281  -0.04620 189 ALA B O   
3708 C CB  . ALA B 189 ? 0.30718 0.43234 0.43666 0.01475  0.01185  -0.04203 189 ALA B CB  
3709 N N   . THR B 190 ? 0.36462 0.53653 0.49954 0.05053  0.04536  -0.03957 190 THR B N   
3710 C CA  . THR B 190 ? 0.37885 0.56509 0.49783 0.06111  0.06046  -0.03961 190 THR B CA  
3711 C C   . THR B 190 ? 0.37694 0.58393 0.50414 0.04679  0.06525  -0.02318 190 THR B C   
3712 O O   . THR B 190 ? 0.35174 0.57749 0.51053 0.03433  0.06285  -0.00989 190 THR B O   
3713 C CB  . THR B 190 ? 0.38902 0.60074 0.52034 0.08237  0.07447  -0.03922 190 THR B CB  
3714 O OG1 . THR B 190 ? 0.30630 0.55121 0.48032 0.07632  0.07381  -0.02485 190 THR B OG1 
3715 C CG2 . THR B 190 ? 0.40348 0.58354 0.51769 0.10092  0.07002  -0.05688 190 THR B CG2 
3716 N N   . MET B 191 ? 0.35761 0.55819 0.45491 0.04823  0.07005  -0.02391 191 MET B N   
3717 C CA  . MET B 191 ? 0.34979 0.55595 0.44737 0.03392  0.07057  -0.00785 191 MET B CA  
3718 C C   . MET B 191 ? 0.39025 0.60179 0.45322 0.04417  0.08282  -0.00498 191 MET B C   
3719 O O   . MET B 191 ? 0.40596 0.60713 0.43781 0.06009  0.08435  -0.02147 191 MET B O   
3720 C CB  . MET B 191 ? 0.35692 0.53486 0.44904 0.02091  0.05215  -0.01212 191 MET B CB  
3721 C CG  . MET B 191 ? 0.37525 0.54732 0.49489 0.00986  0.04005  -0.01225 191 MET B CG  
3722 S SD  . MET B 191 ? 0.35046 0.49494 0.45998 -0.00012 0.02285  -0.01711 191 MET B SD  
3723 C CE  . MET B 191 ? 0.33676 0.46548 0.42334 0.00827  0.01792  -0.03635 191 MET B CE  
3724 N N   . ASP B 192 ? 0.41307 0.63720 0.47864 0.03458  0.09016  0.01631  192 ASP B N   
3725 C CA  . ASP B 192 ? 0.39577 0.62111 0.42342 0.04211  0.09924  0.02382  192 ASP B CA  
3726 C C   . ASP B 192 ? 0.42236 0.61935 0.43235 0.03315  0.08209  0.02541  192 ASP B C   
3727 O O   . ASP B 192 ? 0.38002 0.56270 0.41366 0.01876  0.06876  0.02782  192 ASP B O   
3728 C CB  . ASP B 192 ? 0.43940 0.69826 0.48082 0.03784  0.12114  0.05155  192 ASP B CB  
3729 C CG  . ASP B 192 ? 0.55175 0.84890 0.60854 0.05255  0.14178  0.05069  192 ASP B CG  
3730 O OD1 . ASP B 192 ? 0.52346 0.81934 0.54727 0.07608  0.14807  0.03238  192 ASP B OD1 
3731 O OD2 . ASP B 192 ? 0.55920 0.88789 0.66197 0.04138  0.15040  0.06722  192 ASP B OD2 
3732 N N   . PRO B 193 ? 0.39320 0.58231 0.36018 0.04401  0.08085  0.02263  193 PRO B N   
3733 C CA  . PRO B 193 ? 0.42338 0.59135 0.37562 0.03875  0.06493  0.02743  193 PRO B CA  
3734 C C   . PRO B 193 ? 0.40223 0.56693 0.37637 0.02345  0.06791  0.05423  193 PRO B C   
3735 O O   . PRO B 193 ? 0.42680 0.60979 0.41090 0.01844  0.08588  0.07533  193 PRO B O   
3736 C CB  . PRO B 193 ? 0.47141 0.64124 0.37246 0.05505  0.06773  0.02655  193 PRO B CB  
3737 C CG  . PRO B 193 ? 0.49046 0.67246 0.37620 0.06976  0.07851  0.00894  193 PRO B CG  
3738 C CD  . PRO B 193 ? 0.49509 0.69584 0.42241 0.06409  0.09373  0.01560  193 PRO B CD  
3739 N N   . GLY B 194 ? 0.40726 0.54845 0.39053 0.01579  0.05028  0.05322  194 GLY B N   
3740 C CA  . GLY B 194 ? 0.43259 0.55989 0.43771 0.00074  0.04849  0.07327  194 GLY B CA  
3741 C C   . GLY B 194 ? 0.42622 0.55138 0.47239 -0.01281 0.04228  0.06606  194 GLY B C   
3742 O O   . GLY B 194 ? 0.41815 0.52164 0.47920 -0.02427 0.03287  0.07404  194 GLY B O   
3743 N N   . ASP B 195 ? 0.37280 0.51657 0.43430 -0.01027 0.04588  0.05084  195 ASP B N   
3744 C CA  . ASP B 195 ? 0.33337 0.47364 0.42696 -0.02002 0.03640  0.04231  195 ASP B CA  
3745 C C   . ASP B 195 ? 0.38463 0.50243 0.46971 -0.01602 0.01923  0.02492  195 ASP B C   
3746 O O   . ASP B 195 ? 0.36267 0.47449 0.42344 -0.00598 0.01481  0.01719  195 ASP B O   
3747 C CB  . ASP B 195 ? 0.35838 0.52380 0.46943 -0.01571 0.04438  0.03327  195 ASP B CB  
3748 C CG  . ASP B 195 ? 0.37207 0.57020 0.49983 -0.01780 0.06330  0.05029  195 ASP B CG  
3749 O OD1 . ASP B 195 ? 0.39577 0.59747 0.53043 -0.02941 0.06971  0.07200  195 ASP B OD1 
3750 O OD2 . ASP B 195 ? 0.34749 0.56850 0.48321 -0.00727 0.07232  0.04272  195 ASP B OD2 
3751 N N   . VAL B 196 ? 0.31865 0.42791 0.42465 -0.02358 0.00935  0.01878  196 VAL B N   
3752 C CA  . VAL B 196 ? 0.35431 0.44828 0.45465 -0.01905 -0.00350 0.00375  196 VAL B CA  
3753 C C   . VAL B 196 ? 0.33850 0.43820 0.45644 -0.02201 -0.00708 -0.00646 196 VAL B C   
3754 O O   . VAL B 196 ? 0.35296 0.45645 0.49101 -0.03099 -0.00879 -0.00131 196 VAL B O   
3755 C CB  . VAL B 196 ? 0.37474 0.44245 0.47062 -0.02057 -0.01442 0.00786  196 VAL B CB  
3756 C CG1 . VAL B 196 ? 0.36874 0.43005 0.45808 -0.01146 -0.02374 -0.00769 196 VAL B CG1 
3757 C CG2 . VAL B 196 ? 0.42094 0.47975 0.49767 -0.01651 -0.01166 0.02236  196 VAL B CG2 
3758 N N   . LEU B 197 ? 0.30718 0.40816 0.41813 -0.01542 -0.00928 -0.01957 197 LEU B N   
3759 C CA  . LEU B 197 ? 0.30842 0.41095 0.42927 -0.01616 -0.01299 -0.02734 197 LEU B CA  
3760 C C   . LEU B 197 ? 0.29565 0.38572 0.41055 -0.01443 -0.02211 -0.03439 197 LEU B C   
3761 O O   . LEU B 197 ? 0.29531 0.38432 0.39993 -0.00928 -0.02295 -0.03861 197 LEU B O   
3762 C CB  . LEU B 197 ? 0.26720 0.37660 0.38366 -0.01071 -0.00732 -0.03432 197 LEU B CB  
3763 C CG  . LEU B 197 ? 0.27961 0.38522 0.39930 -0.01006 -0.01105 -0.04035 197 LEU B CG  
3764 C CD1 . LEU B 197 ? 0.24832 0.35956 0.38317 -0.01161 -0.01419 -0.03613 197 LEU B CD1 
3765 C CD2 . LEU B 197 ? 0.26895 0.37141 0.38155 -0.00617 -0.00668 -0.04651 197 LEU B CD2 
3766 N N   . ILE B 198 ? 0.28397 0.36775 0.40520 -0.01739 -0.02934 -0.03619 198 ILE B N   
3767 C CA  . ILE B 198 ? 0.28682 0.35851 0.39804 -0.01257 -0.03700 -0.04406 198 ILE B CA  
3768 C C   . ILE B 198 ? 0.32658 0.40505 0.43576 -0.01019 -0.03692 -0.04890 198 ILE B C   
3769 O O   . ILE B 198 ? 0.31693 0.39923 0.43448 -0.01367 -0.04024 -0.04699 198 ILE B O   
3770 C CB  . ILE B 198 ? 0.35617 0.40797 0.46830 -0.01659 -0.04818 -0.04434 198 ILE B CB  
3771 C CG1 . ILE B 198 ? 0.37871 0.42009 0.49464 -0.02219 -0.04751 -0.03389 198 ILE B CG1 
3772 C CG2 . ILE B 198 ? 0.30966 0.34572 0.40457 -0.00609 -0.05523 -0.05544 198 ILE B CG2 
3773 C CD1 . ILE B 198 ? 0.36735 0.40093 0.46851 -0.01180 -0.04572 -0.03371 198 ILE B CD1 
3774 N N   . VAL B 199 ? 0.32028 0.40265 0.41964 -0.00415 -0.03327 -0.05328 199 VAL B N   
3775 C CA  . VAL B 199 ? 0.33086 0.41864 0.42558 -0.00270 -0.03045 -0.05355 199 VAL B CA  
3776 C C   . VAL B 199 ? 0.31336 0.40022 0.39299 0.00547  -0.03162 -0.05880 199 VAL B C   
3777 O O   . VAL B 199 ? 0.31835 0.41220 0.39577 0.01082  -0.02745 -0.06139 199 VAL B O   
3778 C CB  . VAL B 199 ? 0.33162 0.42748 0.43050 -0.00596 -0.02172 -0.05070 199 VAL B CB  
3779 C CG1 . VAL B 199 ? 0.33965 0.43422 0.43323 -0.00594 -0.01897 -0.04682 199 VAL B CG1 
3780 C CG2 . VAL B 199 ? 0.27336 0.36867 0.38068 -0.00933 -0.01987 -0.04870 199 VAL B CG2 
3781 N N   . ARG B 200 ? 0.30879 0.38994 0.37719 0.00856  -0.03761 -0.06070 200 ARG B N   
3782 C CA  . ARG B 200 ? 0.30545 0.38550 0.35203 0.01945  -0.03800 -0.06667 200 ARG B CA  
3783 C C   . ARG B 200 ? 0.32730 0.42539 0.37047 0.02156  -0.02342 -0.06020 200 ARG B C   
3784 O O   . ARG B 200 ? 0.31023 0.41371 0.36366 0.01296  -0.01714 -0.05107 200 ARG B O   
3785 C CB  . ARG B 200 ? 0.34706 0.41807 0.37940 0.02168  -0.04967 -0.06950 200 ARG B CB  
3786 C CG  . ARG B 200 ? 0.37872 0.44450 0.38003 0.03561  -0.05265 -0.07869 200 ARG B CG  
3787 C CD  . ARG B 200 ? 0.42317 0.48729 0.40590 0.03873  -0.06133 -0.07747 200 ARG B CD  
3788 N NE  . ARG B 200 ? 0.48783 0.54350 0.43428 0.05398  -0.06694 -0.08971 200 ARG B NE  
3789 C CZ  . ARG B 200 ? 0.48771 0.55511 0.41041 0.06712  -0.05197 -0.08800 200 ARG B CZ  
3790 N NH1 . ARG B 200 ? 0.39193 0.48054 0.32789 0.06317  -0.03168 -0.07323 200 ARG B NH1 
3791 N NH2 . ARG B 200 ? 0.56455 0.62310 0.44936 0.08430  -0.05754 -0.10164 200 ARG B NH2 
3792 N N   . GLN B 201 ? 0.31638 0.42339 0.34588 0.03320  -0.01777 -0.06477 201 GLN B N   
3793 C CA  . GLN B 201 ? 0.32887 0.45825 0.35461 0.03491  -0.00247 -0.05630 201 GLN B CA  
3794 C C   . GLN B 201 ? 0.32680 0.45088 0.34041 0.03030  -0.00083 -0.04566 201 GLN B C   
3795 O O   . GLN B 201 ? 0.34096 0.44919 0.33773 0.03480  -0.01240 -0.04927 201 GLN B O   
3796 C CB  . GLN B 201 ? 0.28691 0.42751 0.29281 0.05366  0.00330  -0.06399 201 GLN B CB  
3797 C CG  . GLN B 201 ? 0.33794 0.51035 0.34097 0.05659  0.02298  -0.05285 201 GLN B CG  
3798 C CD  . GLN B 201 ? 0.36414 0.55138 0.34561 0.08048  0.03056  -0.06234 201 GLN B CD  
3799 O OE1 . GLN B 201 ? 0.35368 0.52699 0.32937 0.09421  0.02098  -0.07799 201 GLN B OE1 
3800 N NE2 . GLN B 201 ? 0.33347 0.54760 0.30155 0.08673  0.04869  -0.05210 201 GLN B NE2 
3801 N N   . ARG B 202 ? 0.34702 0.48325 0.37053 0.02053  0.01179  -0.03180 202 ARG B N   
3802 C CA  . ARG B 202 ? 0.33797 0.46659 0.34938 0.01628  0.01600  -0.01700 202 ARG B CA  
3803 C C   . ARG B 202 ? 0.34630 0.45222 0.36457 0.01016  0.00528  -0.01440 202 ARG B C   
3804 O O   . ARG B 202 ? 0.35631 0.45122 0.36186 0.01057  0.00588  -0.00229 202 ARG B O   
3805 C CB  . ARG B 202 ? 0.37389 0.50154 0.34869 0.03119  0.01564  -0.01577 202 ARG B CB  
3806 C CG  . ARG B 202 ? 0.42361 0.57618 0.38462 0.03969  0.03233  -0.01188 202 ARG B CG  
3807 C CD  . ARG B 202 ? 0.47150 0.61833 0.38943 0.05852  0.02767  -0.01725 202 ARG B CD  
3808 N NE  . ARG B 202 ? 0.50605 0.63823 0.40356 0.05719  0.02376  -0.00290 202 ARG B NE  
3809 C CZ  . ARG B 202 ? 0.57117 0.71215 0.44994 0.05739  0.03970  0.01798  202 ARG B CZ  
3810 N NH1 . ARG B 202 ? 0.56141 0.73107 0.44542 0.05559  0.06249  0.02801  202 ARG B NH1 
3811 N NH2 . ARG B 202 ? 0.55654 0.67943 0.41179 0.05989  0.03277  0.03091  202 ARG B NH2 
3812 N N   . VAL B 203 ? 0.33814 0.43782 0.37437 0.00689  -0.00371 -0.02403 203 VAL B N   
3813 C CA  . VAL B 203 ? 0.35648 0.44114 0.40133 0.00422  -0.01104 -0.02150 203 VAL B CA  
3814 C C   . VAL B 203 ? 0.35583 0.43244 0.41342 -0.00620 -0.00333 -0.01429 203 VAL B C   
3815 O O   . VAL B 203 ? 0.34242 0.42645 0.41410 -0.01452 0.00121  -0.01838 203 VAL B O   
3816 C CB  . VAL B 203 ? 0.34846 0.43324 0.40750 0.00456  -0.02084 -0.03225 203 VAL B CB  
3817 C CG1 . VAL B 203 ? 0.30881 0.38650 0.38044 0.00401  -0.02450 -0.02903 203 VAL B CG1 
3818 C CG2 . VAL B 203 ? 0.33447 0.41969 0.38147 0.01173  -0.03218 -0.04009 203 VAL B CG2 
3819 N N   . VAL B 204 ? 0.35530 0.41423 0.40674 -0.00498 -0.00399 -0.00421 204 VAL B N   
3820 C CA  . VAL B 204 ? 0.34960 0.38981 0.40916 -0.01436 0.00079  0.00164  204 VAL B CA  
3821 C C   . VAL B 204 ? 0.38143 0.41473 0.45528 -0.01310 -0.00440 -0.00999 204 VAL B C   
3822 O O   . VAL B 204 ? 0.34696 0.38204 0.42291 -0.00250 -0.01088 -0.01363 204 VAL B O   
3823 C CB  . VAL B 204 ? 0.36077 0.37748 0.40487 -0.01011 0.00102  0.01751  204 VAL B CB  
3824 C CG1 . VAL B 204 ? 0.38256 0.36965 0.43365 -0.02100 0.00434  0.02264  204 VAL B CG1 
3825 C CG2 . VAL B 204 ? 0.38262 0.40940 0.40636 -0.00944 0.00818  0.03103  204 VAL B CG2 
3826 N N   . HIS B 205 ? 0.34789 0.37680 0.43177 -0.02376 -0.00169 -0.01569 205 HIS B N   
3827 C CA  . HIS B 205 ? 0.37362 0.39895 0.46482 -0.02105 -0.00515 -0.02808 205 HIS B CA  
3828 C C   . HIS B 205 ? 0.37005 0.37825 0.46451 -0.03315 -0.00491 -0.03277 205 HIS B C   
3829 O O   . HIS B 205 ? 0.38139 0.38682 0.47935 -0.04694 -0.00214 -0.02574 205 HIS B O   
3830 C CB  . HIS B 205 ? 0.32696 0.37747 0.42425 -0.01939 -0.00664 -0.03619 205 HIS B CB  
3831 C CG  . HIS B 205 ? 0.34650 0.41403 0.44831 -0.02824 -0.00436 -0.03726 205 HIS B CG  
3832 N ND1 . HIS B 205 ? 0.37850 0.45932 0.47669 -0.02789 -0.00074 -0.03084 205 HIS B ND1 
3833 C CD2 . HIS B 205 ? 0.34089 0.41722 0.45061 -0.03575 -0.00538 -0.04394 205 HIS B CD2 
3834 C CE1 . HIS B 205 ? 0.34408 0.44426 0.45139 -0.03375 0.00196  -0.03308 205 HIS B CE1 
3835 N NE2 . HIS B 205 ? 0.35501 0.45356 0.47081 -0.03920 -0.00218 -0.04076 205 HIS B NE2 
3836 N N   . ALA B 206 ? 0.39214 0.39051 0.48541 -0.02839 -0.00805 -0.04495 206 ALA B N   
3837 C CA  . ALA B 206 ? 0.37697 0.35629 0.46945 -0.03881 -0.01196 -0.05463 206 ALA B CA  
3838 C C   . ALA B 206 ? 0.42253 0.40795 0.50912 -0.03034 -0.01463 -0.06977 206 ALA B C   
3839 O O   . ALA B 206 ? 0.41629 0.40249 0.49732 -0.01405 -0.01153 -0.07177 206 ALA B O   
3840 C CB  . ALA B 206 ? 0.45058 0.38597 0.53470 -0.03873 -0.01373 -0.05226 206 ALA B CB  
3841 N N   . GLY B 207 ? 0.38787 0.38083 0.47594 -0.04080 -0.02023 -0.07925 207 GLY B N   
3842 C CA  . GLY B 207 ? 0.42047 0.40928 0.49408 -0.03234 -0.02403 -0.09448 207 GLY B CA  
3843 C C   . GLY B 207 ? 0.46904 0.41809 0.52671 -0.02317 -0.02533 -0.10419 207 GLY B C   
3844 O O   . GLY B 207 ? 0.48807 0.40480 0.54654 -0.03220 -0.02934 -0.10338 207 GLY B O   
3845 N N   . GLY B 208 ? 0.47091 0.42114 0.51325 -0.00411 -0.02107 -0.11257 208 GLY B N   
3846 C CA  . GLY B 208 ? 0.46623 0.38067 0.49236 0.01126  -0.02032 -0.12246 208 GLY B CA  
3847 C C   . GLY B 208 ? 0.54789 0.42802 0.55165 0.00901  -0.03113 -0.14414 208 GLY B C   
3848 O O   . GLY B 208 ? 0.61446 0.45883 0.59970 0.02527  -0.03116 -0.15589 208 GLY B O   
3849 N N   . GLY B 209 ? 0.52645 0.41544 0.53114 -0.00935 -0.04204 -0.15109 209 GLY B N   
3850 C CA  . GLY B 209 ? 0.58363 0.44262 0.56455 -0.01146 -0.05602 -0.17482 209 GLY B CA  
3851 C C   . GLY B 209 ? 0.62607 0.49587 0.57587 0.01309  -0.05107 -0.18826 209 GLY B C   
3852 O O   . GLY B 209 ? 0.55944 0.47147 0.51176 0.01985  -0.04183 -0.17798 209 GLY B O   
3853 N N   . ASN B 210 ? 0.56276 0.44439 0.64899 0.02344  -0.07010 -0.07874 210 ASN B N   
3854 C CA  . ASN B 210 ? 0.56496 0.47979 0.66944 0.02912  -0.07349 -0.09780 210 ASN B CA  
3855 C C   . ASN B 210 ? 0.58785 0.48234 0.70130 0.03743  -0.07963 -0.11253 210 ASN B C   
3856 O O   . ASN B 210 ? 0.59658 0.48162 0.71752 0.02803  -0.07659 -0.12102 210 ASN B O   
3857 C CB  . ASN B 210 ? 0.56988 0.51510 0.67894 0.01770  -0.06610 -0.10393 210 ASN B CB  
3858 C CG  . ASN B 210 ? 0.52845 0.50071 0.64157 0.02571  -0.06325 -0.11951 210 ASN B CG  
3859 O OD1 . ASN B 210 ? 0.47892 0.45087 0.60244 0.03617  -0.06569 -0.13073 210 ASN B OD1 
3860 N ND2 . ASN B 210 ? 0.49563 0.48804 0.59719 0.02280  -0.05644 -0.12076 210 ASN B ND2 
3861 N N   . ARG B 211 ? 0.57639 0.46708 0.69405 0.05602  -0.08949 -0.11995 211 ARG B N   
3862 C CA  . ARG B 211 ? 0.63633 0.50206 0.76030 0.06752  -0.09677 -0.13327 211 ARG B CA  
3863 C C   . ARG B 211 ? 0.56956 0.46887 0.71649 0.07142  -0.09533 -0.15754 211 ARG B C   
3864 O O   . ARG B 211 ? 0.55277 0.43721 0.70888 0.08351  -0.10215 -0.17224 211 ARG B O   
3865 C CB  . ARG B 211 ? 0.64738 0.48252 0.75869 0.09195  -0.11181 -0.12958 211 ARG B CB  
3866 C CG  . ARG B 211 ? 0.73820 0.52913 0.81211 0.09393  -0.11169 -0.10408 211 ARG B CG  
3867 C CD  . ARG B 211 ? 0.79288 0.54660 0.85444 0.07157  -0.09370 -0.09086 211 ARG B CD  
3868 N NE  . ARG B 211 ? 0.88888 0.61454 0.96144 0.06972  -0.09099 -0.10344 211 ARG B NE  
3869 C CZ  . ARG B 211 ? 0.87933 0.58106 0.95938 0.04801  -0.07482 -0.10363 211 ARG B CZ  
3870 N NH1 . ARG B 211 ? 0.82438 0.52712 0.90319 0.02654  -0.05909 -0.09183 211 ARG B NH1 
3871 N NH2 . ARG B 211 ? 0.88707 0.56613 0.98229 0.04747  -0.07397 -0.11998 211 ARG B NH2 
3872 N N   . THR B 212 ? 0.52688 0.46516 0.67803 0.06321  -0.08444 -0.16152 212 THR B N   
3873 C CA  . THR B 212 ? 0.49046 0.45115 0.65084 0.06657  -0.07713 -0.18242 212 THR B CA  
3874 C C   . THR B 212 ? 0.54290 0.49045 0.69740 0.06104  -0.07954 -0.19194 212 THR B C   
3875 O O   . THR B 212 ? 0.58282 0.51529 0.73193 0.04922  -0.08205 -0.18337 212 THR B O   
3876 C CB  . THR B 212 ? 0.48272 0.47493 0.63594 0.06114  -0.05994 -0.18114 212 THR B CB  
3877 O OG1 . THR B 212 ? 0.44958 0.44104 0.58055 0.04977  -0.05767 -0.16744 212 THR B OG1 
3878 C CG2 . THR B 212 ? 0.43551 0.44448 0.60536 0.06358  -0.05541 -0.17800 212 THR B CG2 
3879 N N   . THR B 213 ? 0.53506 0.49067 0.69512 0.06964  -0.07784 -0.21385 213 THR B N   
3880 C CA  . THR B 213 ? 0.50080 0.44649 0.65979 0.06780  -0.08333 -0.23057 213 THR B CA  
3881 C C   . THR B 213 ? 0.50149 0.47192 0.64104 0.07317  -0.07566 -0.24585 213 THR B C   
3882 O O   . THR B 213 ? 0.49181 0.45950 0.62935 0.07706  -0.08247 -0.26693 213 THR B O   
3883 C CB  . THR B 213 ? 0.60161 0.52209 0.77830 0.07777  -0.09162 -0.24573 213 THR B CB  
3884 O OG1 . THR B 213 ? 0.62822 0.56689 0.81396 0.09290  -0.08679 -0.25896 213 THR B OG1 
3885 C CG2 . THR B 213 ? 0.56847 0.44901 0.74875 0.07725  -0.09879 -0.22844 213 THR B CG2 
3886 N N   . ALA B 214 ? 0.50582 0.49549 0.62718 0.07507  -0.06050 -0.23665 214 ALA B N   
3887 C CA  . ALA B 214 ? 0.54131 0.54242 0.62932 0.08456  -0.04728 -0.24710 214 ALA B CA  
3888 C C   . ALA B 214 ? 0.55596 0.56069 0.61027 0.08409  -0.05163 -0.24013 214 ALA B C   
3889 O O   . ALA B 214 ? 0.59414 0.60027 0.60593 0.09738  -0.04254 -0.24657 214 ALA B O   
3890 C CB  . ALA B 214 ? 0.54061 0.55233 0.62598 0.08713  -0.02088 -0.24254 214 ALA B CB  
3891 N N   . GLY B 215 ? 0.45559 0.45947 0.52442 0.07182  -0.06435 -0.22805 215 GLY B N   
3892 C CA  . GLY B 215 ? 0.46552 0.47808 0.51149 0.07300  -0.07166 -0.22553 215 GLY B CA  
3893 C C   . GLY B 215 ? 0.52915 0.54515 0.54561 0.07426  -0.05672 -0.20317 215 GLY B C   
3894 O O   . GLY B 215 ? 0.54329 0.56221 0.52174 0.08621  -0.05908 -0.20427 215 GLY B O   
3895 N N   . LYS B 216 ? 0.45202 0.46617 0.48410 0.06474  -0.04283 -0.18521 216 LYS B N   
3896 C CA  . LYS B 216 ? 0.51078 0.52589 0.52158 0.06327  -0.02598 -0.16582 216 LYS B CA  
3897 C C   . LYS B 216 ? 0.50993 0.52840 0.54251 0.04938  -0.03487 -0.14893 216 LYS B C   
3898 O O   . LYS B 216 ? 0.46387 0.48000 0.52728 0.04091  -0.03758 -0.14397 216 LYS B O   
3899 C CB  . LYS B 216 ? 0.55238 0.56710 0.57112 0.06241  -0.00090 -0.16475 216 LYS B CB  
3900 C CG  . LYS B 216 ? 0.60041 0.60916 0.59640 0.07507  0.01637  -0.18126 216 LYS B CG  
3901 C CD  . LYS B 216 ? 0.73382 0.72575 0.67083 0.08507  0.04228  -0.17223 216 LYS B CD  
3902 C CE  . LYS B 216 ? 0.81138 0.80111 0.75544 0.07293  0.06398  -0.15326 216 LYS B CE  
3903 N NZ  . LYS B 216 ? 0.82033 0.82537 0.82094 0.05958  0.07969  -0.16078 216 LYS B NZ  
3904 N N   . PRO B 217 ? 0.48286 0.50523 0.49789 0.04963  -0.04039 -0.14117 217 PRO B N   
3905 C CA  . PRO B 217 ? 0.48789 0.51320 0.52388 0.03606  -0.04641 -0.12681 217 PRO B CA  
3906 C C   . PRO B 217 ? 0.48299 0.50726 0.51537 0.03129  -0.03147 -0.10806 217 PRO B C   
3907 O O   . PRO B 217 ? 0.54478 0.56618 0.55176 0.03761  -0.01473 -0.10349 217 PRO B O   
3908 C CB  . PRO B 217 ? 0.45827 0.49395 0.48240 0.04070  -0.05871 -0.13263 217 PRO B CB  
3909 C CG  . PRO B 217 ? 0.50858 0.54172 0.48721 0.06157  -0.05544 -0.14047 217 PRO B CG  
3910 C CD  . PRO B 217 ? 0.50548 0.53007 0.48279 0.06573  -0.04728 -0.15100 217 PRO B CD  
3911 N N   . ARG B 218 ? 0.45552 0.47773 0.51117 0.02069  -0.03594 -0.09812 218 ARG B N   
3912 C CA  . ARG B 218 ? 0.45453 0.47870 0.51105 0.01629  -0.02662 -0.08403 218 ARG B CA  
3913 C C   . ARG B 218 ? 0.43438 0.46200 0.47703 0.01302  -0.02754 -0.07246 218 ARG B C   
3914 O O   . ARG B 218 ? 0.44247 0.47084 0.49391 0.00749  -0.03784 -0.07207 218 ARG B O   
3915 C CB  . ARG B 218 ? 0.44081 0.45872 0.51974 0.01282  -0.03417 -0.08077 218 ARG B CB  
3916 C CG  . ARG B 218 ? 0.44097 0.46472 0.52475 0.01088  -0.02842 -0.07285 218 ARG B CG  
3917 C CD  . ARG B 218 ? 0.41819 0.43606 0.51866 0.01644  -0.04060 -0.07624 218 ARG B CD  
3918 N NE  . ARG B 218 ? 0.46215 0.45613 0.55178 0.01621  -0.05211 -0.06721 218 ARG B NE  
3919 C CZ  . ARG B 218 ? 0.48966 0.47227 0.56492 0.01091  -0.05228 -0.05218 218 ARG B CZ  
3920 N NH1 . ARG B 218 ? 0.43784 0.43380 0.50881 0.00702  -0.04624 -0.04523 218 ARG B NH1 
3921 N NH2 . ARG B 218 ? 0.46750 0.42110 0.53202 0.00892  -0.05508 -0.04449 218 ARG B NH2 
3922 N N   . ARG B 219 ? 0.42341 0.45140 0.44743 0.01591  -0.01409 -0.06465 219 ARG B N   
3923 C CA  . ARG B 219 ? 0.41185 0.44202 0.41925 0.01710  -0.01483 -0.05503 219 ARG B CA  
3924 C C   . ARG B 219 ? 0.43431 0.46413 0.45075 0.00895  -0.00725 -0.04274 219 ARG B C   
3925 O O   . ARG B 219 ? 0.39272 0.41955 0.41471 0.00711  0.00665  -0.04301 219 ARG B O   
3926 C CB  . ARG B 219 ? 0.44308 0.46423 0.40936 0.03242  -0.00563 -0.05540 219 ARG B CB  
3927 C CG  . ARG B 219 ? 0.51052 0.53243 0.45683 0.03949  -0.00984 -0.04788 219 ARG B CG  
3928 C CD  . ARG B 219 ? 0.51342 0.51654 0.40519 0.06228  -0.00341 -0.04758 219 ARG B CD  
3929 N NE  . ARG B 219 ? 0.54990 0.56057 0.42690 0.07889  -0.02334 -0.06504 219 ARG B NE  
3930 C CZ  . ARG B 219 ? 0.57821 0.57236 0.39936 0.10649  -0.02641 -0.06868 219 ARG B CZ  
3931 N NH1 . ARG B 219 ? 0.49473 0.45660 0.26456 0.12013  -0.00703 -0.05240 219 ARG B NH1 
3932 N NH2 . ARG B 219 ? 0.62208 0.62827 0.43517 0.12294  -0.04935 -0.09039 219 ARG B NH2 
3933 N N   . VAL B 220 ? 0.38470 0.41919 0.40636 0.00378  -0.01500 -0.03553 220 VAL B N   
3934 C CA  . VAL B 220 ? 0.39913 0.43305 0.42605 -0.00217 -0.01043 -0.02547 220 VAL B CA  
3935 C C   . VAL B 220 ? 0.36195 0.40074 0.37850 -0.00136 -0.01113 -0.01856 220 VAL B C   
3936 O O   . VAL B 220 ? 0.34196 0.38921 0.36283 -0.00086 -0.01998 -0.02335 220 VAL B O   
3937 C CB  . VAL B 220 ? 0.38349 0.41271 0.42682 -0.00773 -0.01893 -0.02413 220 VAL B CB  
3938 C CG1 . VAL B 220 ? 0.37128 0.39581 0.41788 -0.01337 -0.02532 -0.02198 220 VAL B CG1 
3939 C CG2 . VAL B 220 ? 0.39683 0.42584 0.44111 -0.00900 -0.01650 -0.01830 220 VAL B CG2 
3940 N N   . VAL B 221 ? 0.35501 0.39037 0.36326 -0.00100 -0.00141 -0.01109 221 VAL B N   
3941 C CA  . VAL B 221 ? 0.37812 0.41800 0.38067 -0.00023 -0.00215 -0.00468 221 VAL B CA  
3942 C C   . VAL B 221 ? 0.36177 0.40135 0.37600 -0.00888 -0.00133 0.00073  221 VAL B C   
3943 O O   . VAL B 221 ? 0.35209 0.38735 0.37171 -0.01057 0.00352  -0.00072 221 VAL B O   
3944 C CB  . VAL B 221 ? 0.39289 0.42185 0.36857 0.01082  0.00852  -0.00025 221 VAL B CB  
3945 C CG1 . VAL B 221 ? 0.35054 0.38237 0.32521 0.01079  0.00957  0.00614  221 VAL B CG1 
3946 C CG2 . VAL B 221 ? 0.39122 0.41855 0.34248 0.02734  0.00143  -0.00601 221 VAL B CG2 
3947 N N   . LEU B 222 ? 0.30024 0.34464 0.31969 -0.01346 -0.00544 0.00370  222 LEU B N   
3948 C CA  . LEU B 222 ? 0.32290 0.36152 0.34117 -0.01786 -0.00384 0.00986  222 LEU B CA  
3949 C C   . LEU B 222 ? 0.33602 0.38144 0.34951 -0.01664 0.00167  0.01354  222 LEU B C   
3950 O O   . LEU B 222 ? 0.31360 0.37062 0.33211 -0.01523 0.00136  0.01076  222 LEU B O   
3951 C CB  . LEU B 222 ? 0.34182 0.36997 0.36185 -0.02398 -0.00515 0.01243  222 LEU B CB  
3952 C CG  . LEU B 222 ? 0.42888 0.44607 0.45264 -0.02319 -0.01147 0.00830  222 LEU B CG  
3953 C CD1 . LEU B 222 ? 0.39626 0.41748 0.43509 -0.02929 -0.01113 0.00135  222 LEU B CD1 
3954 C CD2 . LEU B 222 ? 0.47556 0.46780 0.48357 -0.01972 -0.01437 0.01428  222 LEU B CD2 
3955 N N   . ALA B 223 ? 0.33863 0.37937 0.34634 -0.01550 0.00492  0.01578  223 ALA B N   
3956 C CA  . ALA B 223 ? 0.32639 0.37071 0.32899 -0.01375 0.01041  0.01855  223 ALA B CA  
3957 C C   . ALA B 223 ? 0.35904 0.39717 0.35406 -0.01568 0.01018  0.02108  223 ALA B C   
3958 O O   . ALA B 223 ? 0.35270 0.38366 0.34425 -0.01298 0.00441  0.01741  223 ALA B O   
3959 C CB  . ALA B 223 ? 0.32578 0.36443 0.32433 -0.00907 0.01755  0.01703  223 ALA B CB  
3960 C C   . F2Y B 224 ? 0.34454 0.38132 0.31630 -0.01375 0.02457  0.02607  224 F2Y B C   
3961 O O   . F2Y B 224 ? 0.35921 0.40964 0.34254 -0.01470 0.03112  0.02497  224 F2Y B O   
3962 C CA  . F2Y B 224 ? 0.35356 0.38267 0.32714 -0.01736 0.01979  0.02839  224 F2Y B CA  
3963 N N   . F2Y B 224 ? 0.33026 0.37145 0.32219 -0.01813 0.01623  0.02461  224 F2Y B N   
3964 C CB  . F2Y B 224 ? 0.38444 0.40277 0.35161 -0.02446 0.03133  0.03422  224 F2Y B CB  
3965 C CG  . F2Y B 224 ? 0.43839 0.44301 0.40658 -0.02809 0.02862  0.03617  224 F2Y B CG  
3966 C CD1 . F2Y B 224 ? 0.49303 0.48978 0.45451 -0.02040 0.01399  0.03451  224 F2Y B CD1 
3967 C CE1 . F2Y B 224 ? 0.55862 0.54092 0.52012 -0.02134 0.01025  0.03537  224 F2Y B CE1 
3968 F F1  . F2Y B 224 ? 0.46832 0.44715 0.42875 -0.01233 -0.00450 0.03031  224 F2Y B F1  
3969 C CD2 . F2Y B 224 ? 0.45459 0.45503 0.43596 -0.03942 0.04153  0.03616  224 F2Y B CD2 
3970 C CE2 . F2Y B 224 ? 0.46866 0.45185 0.45094 -0.04266 0.03967  0.03698  224 F2Y B CE2 
3971 F F2  . F2Y B 224 ? 0.54130 0.51907 0.54279 -0.05629 0.05527  0.03355  224 F2Y B F2  
3972 C CZ  . F2Y B 224 ? 0.54637 0.51892 0.51547 -0.03238 0.02311  0.03794  224 F2Y B CZ  
3973 O OH  . F2Y B 224 ? 0.58080 0.53494 0.55062 -0.03386 0.02105  0.03790  224 F2Y B OH  
3974 N N   . PHE B 225 ? 0.34651 0.37686 0.30814 -0.00802 0.01945  0.02158  225 PHE B N   
3975 C CA  . PHE B 225 ? 0.35814 0.39149 0.31599 -0.00442 0.02399  0.01771  225 PHE B CA  
3976 C C   . PHE B 225 ? 0.36517 0.38627 0.29445 -0.00020 0.02675  0.02042  225 PHE B C   
3977 O O   . PHE B 225 ? 0.39717 0.40260 0.30417 0.00656  0.01788  0.02019  225 PHE B O   
3978 C CB  . PHE B 225 ? 0.34324 0.37673 0.31254 -0.00174 0.01899  0.00610  225 PHE B CB  
3979 C CG  . PHE B 225 ? 0.39529 0.42960 0.38217 -0.00511 0.02495  0.00610  225 PHE B CG  
3980 C CD1 . PHE B 225 ? 0.38197 0.41309 0.36828 -0.00222 0.03460  0.00891  225 PHE B CD1 
3981 C CD2 . PHE B 225 ? 0.40270 0.43624 0.40038 -0.00817 0.02205  0.00369  225 PHE B CD2 
3982 C CE1 . PHE B 225 ? 0.43335 0.45371 0.42042 -0.00048 0.04223  0.01159  225 PHE B CE1 
3983 C CE2 . PHE B 225 ? 0.38804 0.41508 0.39174 -0.00952 0.03195  0.00507  225 PHE B CE2 
3984 C CZ  . PHE B 225 ? 0.43165 0.44858 0.42539 -0.00477 0.04263  0.01028  225 PHE B CZ  
3985 N N   . ASN B 226 ? 0.26363 0.38065 0.39723 0.06118  0.03482  0.01982  226 ASN B N   
3986 C CA  . ASN B 226 ? 0.27617 0.37145 0.41523 0.05620  0.02645  0.01822  226 ASN B CA  
3987 C C   . ASN B 226 ? 0.25754 0.35268 0.40450 0.03302  0.01864  0.02420  226 ASN B C   
3988 O O   . ASN B 226 ? 0.23126 0.32357 0.37263 0.02144  0.01687  0.02564  226 ASN B O   
3989 C CB  . ASN B 226 ? 0.28263 0.33385 0.40412 0.06015  0.02243  0.00545  226 ASN B CB  
3990 C CG  . ASN B 226 ? 0.32820 0.36494 0.43610 0.08266  0.02635  -0.00180 226 ASN B CG  
3991 O OD1 . ASN B 226 ? 0.34480 0.40551 0.45941 0.09949  0.03210  0.00180  226 ASN B OD1 
3992 N ND2 . ASN B 226 ? 0.32970 0.32645 0.41670 0.08331  0.02227  -0.01223 226 ASN B ND2 
3993 N N   . SER B 227 ? 0.25009 0.34443 0.40717 0.02698  0.01290  0.02708  227 SER B N   
3994 C CA  . SER B 227 ? 0.27637 0.35707 0.43468 0.00835  0.00438  0.02698  227 SER B CA  
3995 C C   . SER B 227 ? 0.24321 0.29363 0.38789 0.00550  0.00128  0.01619  227 SER B C   
3996 O O   . SER B 227 ? 0.27409 0.30587 0.40904 0.01455  0.00269  0.00708  227 SER B O   
3997 C CB  . SER B 227 ? 0.24264 0.31799 0.40737 0.00573  -0.00063 0.02650  227 SER B CB  
3998 O OG  . SER B 227 ? 0.24798 0.30748 0.41002 -0.00902 -0.00767 0.02231  227 SER B OG  
3999 N N   . VAL B 228 ? 0.22721 0.27176 0.36967 -0.00741 -0.00437 0.01769  228 VAL B N   
4000 C CA  . VAL B 228 ? 0.25039 0.26996 0.38249 -0.00865 -0.00895 0.00798  228 VAL B CA  
4001 C C   . VAL B 228 ? 0.26119 0.26698 0.39366 -0.00825 -0.01244 -0.00204 228 VAL B C   
4002 O O   . VAL B 228 ? 0.27461 0.26639 0.40028 -0.00710 -0.01536 -0.01079 228 VAL B O   
4003 C CB  . VAL B 228 ? 0.27502 0.28676 0.40271 -0.02042 -0.01666 0.01186  228 VAL B CB  
4004 C CG1 . VAL B 228 ? 0.24559 0.27278 0.36953 -0.02488 -0.01390 0.02353  228 VAL B CG1 
4005 C CG2 . VAL B 228 ? 0.23540 0.24668 0.36839 -0.03129 -0.02308 0.01450  228 VAL B CG2 
4006 N N   . GLN B 229 ? 0.25748 0.27059 0.39757 -0.00993 -0.01248 -0.00012 229 GLN B N   
4007 C CA  . GLN B 229 ? 0.29593 0.29938 0.43391 -0.01090 -0.01495 -0.00836 229 GLN B CA  
4008 C C   . GLN B 229 ? 0.26898 0.26038 0.39663 -0.00264 -0.01234 -0.01354 229 GLN B C   
4009 O O   . GLN B 229 ? 0.26722 0.24960 0.38896 -0.00669 -0.01554 -0.02082 229 GLN B O   
4010 C CB  . GLN B 229 ? 0.26916 0.28211 0.41495 -0.01575 -0.01648 -0.00327 229 GLN B CB  
4011 C CG  . GLN B 229 ? 0.27070 0.29414 0.42374 -0.02632 -0.02006 0.00248  229 GLN B CG  
4012 C CD  . GLN B 229 ? 0.28953 0.32499 0.44995 -0.03086 -0.02161 0.00923  229 GLN B CD  
4013 O OE1 . GLN B 229 ? 0.26933 0.29941 0.42712 -0.03421 -0.02401 0.00462  229 GLN B OE1 
4014 N NE2 . GLN B 229 ? 0.27790 0.33274 0.44727 -0.03173 -0.02068 0.02127  229 GLN B NE2 
4015 N N   . LEU B 230 ? 0.27534 0.26716 0.39867 0.00798  -0.00699 -0.01020 230 LEU B N   
4016 C CA  . LEU B 230 ? 0.28250 0.25618 0.39069 0.01643  -0.00556 -0.01563 230 LEU B CA  
4017 C C   . LEU B 230 ? 0.32682 0.29180 0.42349 0.01821  -0.00415 -0.02097 230 LEU B C   
4018 O O   . LEU B 230 ? 0.32498 0.30056 0.42369 0.02062  -0.00052 -0.01728 230 LEU B O   
4019 C CB  . LEU B 230 ? 0.29842 0.27492 0.40527 0.03094  -0.00089 -0.01106 230 LEU B CB  
4020 C CG  . LEU B 230 ? 0.29166 0.27836 0.41004 0.03116  -0.00330 -0.00395 230 LEU B CG  
4021 C CD1 . LEU B 230 ? 0.30135 0.29308 0.41839 0.05078  0.00124  -0.00040 230 LEU B CD1 
4022 C CD2 . LEU B 230 ? 0.32110 0.28853 0.43222 0.02156  -0.01097 -0.00731 230 LEU B CD2 
4023 N N   . THR B 231 ? 0.27377 0.22132 0.35740 0.01458  -0.00797 -0.02836 231 THR B N   
4024 C CA  . THR B 231 ? 0.30109 0.23979 0.37199 0.01476  -0.00823 -0.03332 231 THR B CA  
4025 C C   . THR B 231 ? 0.29978 0.23370 0.35887 0.02669  -0.00156 -0.03257 231 THR B C   
4026 O O   . THR B 231 ? 0.30760 0.22927 0.35627 0.03637  0.00092  -0.03387 231 THR B O   
4027 C CB  . THR B 231 ? 0.32969 0.25195 0.38616 0.00730  -0.01397 -0.03981 231 THR B CB  
4028 O OG1 . THR B 231 ? 0.33237 0.26695 0.40065 -0.00349 -0.01885 -0.04091 231 THR B OG1 
4029 C CG2 . THR B 231 ? 0.27877 0.19425 0.32174 0.00542  -0.01565 -0.04435 231 THR B CG2 
4030 N N   . PRO B 232 ? 0.30673 0.24877 0.36465 0.02708  0.00088  -0.03093 232 PRO B N   
4031 C CA  . PRO B 232 ? 0.31381 0.25409 0.35730 0.03767  0.00803  -0.03172 232 PRO B CA  
4032 C C   . PRO B 232 ? 0.34076 0.25223 0.35893 0.04098  0.00635  -0.04080 232 PRO B C   
4033 O O   . PRO B 232 ? 0.34321 0.24199 0.35360 0.03064  -0.00066 -0.04488 232 PRO B O   
4034 C CB  . PRO B 232 ? 0.34812 0.30037 0.39273 0.03167  0.00793  -0.02751 232 PRO B CB  
4035 C CG  . PRO B 232 ? 0.29894 0.26182 0.36311 0.02162  0.00175  -0.02193 232 PRO B CG  
4036 C CD  . PRO B 232 ? 0.25043 0.20265 0.31823 0.01856  -0.00345 -0.02802 232 PRO B CD  
4037 N N   . PHE B 233 ? 0.32806 0.22937 0.33230 0.05579  0.01200  -0.04402 233 PHE B N   
4038 C CA  . PHE B 233 ? 0.40476 0.27109 0.37794 0.05968  0.00956  -0.05334 233 PHE B CA  
4039 C C   . PHE B 233 ? 0.44483 0.30785 0.40221 0.05385  0.00981  -0.05676 233 PHE B C   
4040 O O   . PHE B 233 ? 0.42847 0.26839 0.36684 0.04375  0.00253  -0.06184 233 PHE B O   
4041 C CB  . PHE B 233 ? 0.38250 0.23897 0.34317 0.08185  0.01599  -0.05714 233 PHE B CB  
4042 C CG  . PHE B 233 ? 0.47572 0.28999 0.39773 0.08947  0.01381  -0.06830 233 PHE B CG  
4043 C CD1 . PHE B 233 ? 0.47795 0.25089 0.37879 0.08239  0.00280  -0.07230 233 PHE B CD1 
4044 C CD2 . PHE B 233 ? 0.46628 0.28126 0.36997 0.10320  0.02239  -0.07471 233 PHE B CD2 
4045 C CE1 . PHE B 233 ? 0.53073 0.25728 0.39004 0.08815  -0.00118 -0.08264 233 PHE B CE1 
4046 C CE2 . PHE B 233 ? 0.52645 0.29820 0.39020 0.11110  0.01999  -0.08648 233 PHE B CE2 
4047 C CZ  . PHE B 233 ? 0.55819 0.28238 0.39841 0.10350  0.00747  -0.09054 233 PHE B CZ  
4048 N N   . GLU B 234 ? 0.40839 0.29643 0.37260 0.05794  0.01727  -0.05273 234 GLU B N   
4049 C CA  . GLU B 234 ? 0.41059 0.30027 0.36204 0.05106  0.01707  -0.05335 234 GLU B CA  
4050 C C   . GLU B 234 ? 0.39776 0.30617 0.37082 0.03700  0.01092  -0.04498 234 GLU B C   
4051 O O   . GLU B 234 ? 0.40061 0.33099 0.39559 0.03647  0.01277  -0.03709 234 GLU B O   
4052 C CB  . GLU B 234 ? 0.37816 0.28488 0.32055 0.06307  0.02857  -0.05332 234 GLU B CB  
4053 C CG  . GLU B 234 ? 0.44209 0.32475 0.35563 0.08057  0.03410  -0.06511 234 GLU B CG  
4054 C CD  . GLU B 234 ? 0.49142 0.40080 0.40045 0.09830  0.04808  -0.06641 234 GLU B CD  
4055 O OE1 . GLU B 234 ? 0.42720 0.37871 0.35769 0.09500  0.05397  -0.05597 234 GLU B OE1 
4056 O OE2 . GLU B 234 ? 0.52296 0.41069 0.40440 0.11542  0.05268  -0.07832 234 GLU B OE2 
4057 N N   . THR B 235 ? 0.33716 0.23615 0.30298 0.02613  0.00253  -0.04663 235 THR B N   
4058 C CA  . THR B 235 ? 0.39554 0.30891 0.37873 0.01715  -0.00440 -0.03989 235 THR B CA  
4059 C C   . THR B 235 ? 0.44633 0.36463 0.41789 0.01380  -0.00458 -0.03549 235 THR B C   
4060 O O   . THR B 235 ? 0.42106 0.32768 0.36963 0.01279  -0.00438 -0.04015 235 THR B O   
4061 C CB  . THR B 235 ? 0.38794 0.29609 0.37622 0.00904  -0.01469 -0.04339 235 THR B CB  
4062 O OG1 . THR B 235 ? 0.40369 0.32351 0.40544 0.00506  -0.02191 -0.03829 235 THR B OG1 
4063 C CG2 . THR B 235 ? 0.40895 0.29976 0.37261 0.00380  -0.01856 -0.04989 235 THR B CG2 
4064 N N   . TYR B 236 ? 0.35350 0.28696 0.33771 0.01039  -0.00579 -0.02591 236 TYR B N   
4065 C CA  . TYR B 236 ? 0.42264 0.36109 0.39483 0.00455  -0.00726 -0.01906 236 TYR B CA  
4066 C C   . TYR B 236 ? 0.41819 0.34936 0.39289 -0.00293 -0.02143 -0.01522 236 TYR B C   
4067 O O   . TYR B 236 ? 0.41291 0.34571 0.37984 -0.00945 -0.02619 -0.00663 236 TYR B O   
4068 C CB  . TYR B 236 ? 0.34406 0.30344 0.32300 0.00285  -0.00085 -0.00890 236 TYR B CB  
4069 C CG  . TYR B 236 ? 0.36604 0.33850 0.34062 0.01408  0.01371  -0.01346 236 TYR B CG  
4070 C CD1 . TYR B 236 ? 0.44725 0.42335 0.39928 0.01851  0.02192  -0.01751 236 TYR B CD1 
4071 C CD2 . TYR B 236 ? 0.41484 0.39480 0.40636 0.02185  0.01835  -0.01470 236 TYR B CD2 
4072 C CE1 . TYR B 236 ? 0.45918 0.44658 0.40639 0.03340  0.03485  -0.02364 236 TYR B CE1 
4073 C CE2 . TYR B 236 ? 0.38931 0.38049 0.37673 0.03580  0.03018  -0.01924 236 TYR B CE2 
4074 C CZ  . TYR B 236 ? 0.45621 0.45130 0.42163 0.04348  0.03885  -0.02446 236 TYR B CZ  
4075 O OH  . TYR B 236 ? 0.55757 0.56359 0.51854 0.06164  0.05030  -0.03062 236 TYR B OH  
4076 N N   . ARG B 237 ? 0.39293 0.31765 0.37678 -0.00176 -0.02874 -0.02135 237 ARG B N   
4077 C CA  . ARG B 237 ? 0.43075 0.35336 0.42109 -0.00396 -0.04243 -0.01912 237 ARG B CA  
4078 C C   . ARG B 237 ? 0.42685 0.34521 0.39945 -0.00855 -0.04925 -0.01753 237 ARG B C   
4079 O O   . ARG B 237 ? 0.44457 0.36186 0.42111 -0.00869 -0.06177 -0.01342 237 ARG B O   
4080 C CB  . ARG B 237 ? 0.43527 0.36173 0.44095 -0.00073 -0.04642 -0.02709 237 ARG B CB  
4081 C CG  . ARG B 237 ? 0.41865 0.34361 0.41321 -0.00397 -0.04489 -0.03495 237 ARG B CG  
4082 C CD  . ARG B 237 ? 0.46914 0.40155 0.47824 -0.00375 -0.04517 -0.04124 237 ARG B CD  
4083 N NE  . ARG B 237 ? 0.48687 0.43467 0.50906 -0.00326 -0.05541 -0.04310 237 ARG B NE  
4084 C CZ  . ARG B 237 ? 0.47402 0.43655 0.51168 -0.00279 -0.05683 -0.04811 237 ARG B CZ  
4085 N NH1 . ARG B 237 ? 0.41930 0.37965 0.46074 -0.00472 -0.04990 -0.05062 237 ARG B NH1 
4086 N NH2 . ARG B 237 ? 0.43446 0.41689 0.48391 0.00037  -0.06563 -0.05054 237 ARG B NH2 
4087 N N   . THR B 238 ? 0.38495 0.29941 0.33666 -0.01133 -0.04246 -0.02098 238 THR B N   
4088 C CA  . THR B 238 ? 0.44028 0.35081 0.37257 -0.01776 -0.04924 -0.01888 238 THR B CA  
4089 C C   . THR B 238 ? 0.49392 0.40560 0.41160 -0.02269 -0.04739 -0.00943 238 THR B C   
4090 O O   . THR B 238 ? 0.49122 0.39972 0.38949 -0.02936 -0.05237 -0.00675 238 THR B O   
4091 C CB  . THR B 238 ? 0.48733 0.38889 0.39843 -0.02071 -0.04510 -0.02838 238 THR B CB  
4092 O OG1 . THR B 238 ? 0.47527 0.37095 0.37144 -0.01630 -0.03109 -0.03264 238 THR B OG1 
4093 C CG2 . THR B 238 ? 0.46172 0.36331 0.38422 -0.02059 -0.04827 -0.03594 238 THR B CG2 
4094 N N   . MET B 239 ? 0.47371 0.39244 0.39895 -0.02176 -0.04076 -0.00353 239 MET B N   
4095 C CA  . MET B 239 ? 0.48134 0.40594 0.39342 -0.03031 -0.04065 0.00802  239 MET B CA  
4096 C C   . MET B 239 ? 0.49024 0.40449 0.39959 -0.03714 -0.05876 0.01808  239 MET B C   
4097 O O   . MET B 239 ? 0.51994 0.42615 0.44634 -0.03254 -0.06983 0.01908  239 MET B O   
4098 C CB  . MET B 239 ? 0.47186 0.40960 0.39578 -0.03116 -0.03340 0.01484  239 MET B CB  
4099 C CG  . MET B 239 ? 0.49497 0.44874 0.41767 -0.02362 -0.01532 0.00788  239 MET B CG  
4100 S SD  . MET B 239 ? 0.60577 0.58462 0.54481 -0.02643 -0.00785 0.01824  239 MET B SD  
4101 C CE  . MET B 239 ? 0.47857 0.46453 0.40116 -0.04625 -0.01606 0.03624  239 MET B CE  
4102 N N   . PRO B 240 ? 0.54223 0.45556 0.42921 -0.04676 -0.06291 0.02521  240 PRO B N   
4103 C CA  . PRO B 240 ? 0.57855 0.47923 0.46099 -0.05299 -0.08217 0.03716  240 PRO B CA  
4104 C C   . PRO B 240 ? 0.55488 0.44770 0.44561 -0.05679 -0.08966 0.04865  240 PRO B C   
4105 O O   . PRO B 240 ? 0.55513 0.45923 0.44668 -0.06249 -0.07933 0.05283  240 PRO B O   
4106 C CB  . PRO B 240 ? 0.57889 0.48334 0.43218 -0.06573 -0.08172 0.04393  240 PRO B CB  
4107 C CG  . PRO B 240 ? 0.62483 0.53831 0.46797 -0.06156 -0.06562 0.02969  240 PRO B CG  
4108 C CD  . PRO B 240 ? 0.54835 0.46940 0.41062 -0.05092 -0.05153 0.02106  240 PRO B CD  
4109 N N   . ARG B 241 ? 0.59092 0.46399 0.48658 -0.05312 -0.10888 0.05363  241 ARG B N   
4110 C CA  . ARG B 241 ? 0.56623 0.42111 0.46387 -0.05691 -0.12015 0.06409  241 ARG B CA  
4111 C C   . ARG B 241 ? 0.57200 0.42857 0.44799 -0.07768 -0.11995 0.08059  241 ARG B C   
4112 O O   . ARG B 241 ? 0.55618 0.41281 0.43407 -0.08622 -0.11808 0.08768  241 ARG B O   
4113 C CB  . ARG B 241 ? 0.55097 0.37978 0.44953 -0.04759 -0.14322 0.06675  241 ARG B CB  
4114 C CG  . ARG B 241 ? 0.63750 0.43712 0.53503 -0.04789 -0.15767 0.07441  241 ARG B CG  
4115 C CD  . ARG B 241 ? 0.72368 0.49769 0.62364 -0.03102 -0.17964 0.07262  241 ARG B CD  
4116 N NE  . ARG B 241 ? 0.80758 0.54683 0.70310 -0.02890 -0.19369 0.07698  241 ARG B NE  
4117 C CZ  . ARG B 241 ? 0.78564 0.51850 0.69845 -0.01196 -0.19418 0.06448  241 ARG B CZ  
4118 N NH1 . ARG B 241 ? 0.72376 0.48508 0.66132 0.00433  -0.18256 0.04784  241 ARG B NH1 
4119 N NH2 . ARG B 241 ? 0.80773 0.50371 0.70989 -0.01307 -0.20749 0.06902  241 ARG B NH2 
4120 N N   . GLU B 242 ? 0.49587 0.49879 0.38800 0.07134  -0.08198 0.04174  242 GLU B N   
4121 C CA  . GLU B 242 ? 0.52780 0.50323 0.38618 0.07855  -0.06882 0.06004  242 GLU B CA  
4122 C C   . GLU B 242 ? 0.52563 0.48314 0.38719 0.05918  -0.05276 0.05518  242 GLU B C   
4123 O O   . GLU B 242 ? 0.51812 0.44852 0.37711 0.05657  -0.03526 0.07084  242 GLU B O   
4124 C CB  . GLU B 242 ? 0.58720 0.58188 0.40632 0.09508  -0.08096 0.06209  242 GLU B CB  
4125 C CG  . GLU B 242 ? 0.71388 0.74214 0.53475 0.11425  -0.10294 0.06112  242 GLU B CG  
4126 C CD  . GLU B 242 ? 0.73731 0.80938 0.58205 0.10128  -0.12290 0.03299  242 GLU B CD  
4127 O OE1 . GLU B 242 ? 0.81542 0.90825 0.63657 0.10055  -0.13617 0.01993  242 GLU B OE1 
4128 O OE2 . GLU B 242 ? 0.63564 0.71998 0.52133 0.09075  -0.12439 0.02359  242 GLU B OE2 
4129 N N   . MET B 243 ? 0.51068 0.48324 0.38004 0.04519  -0.05826 0.03360  243 MET B N   
4130 C CA  . MET B 243 ? 0.50829 0.46608 0.38185 0.03073  -0.04386 0.02849  243 MET B CA  
4131 C C   . MET B 243 ? 0.49372 0.43683 0.40084 0.01882  -0.03383 0.03134  243 MET B C   
4132 O O   . MET B 243 ? 0.48288 0.41028 0.39316 0.01317  -0.01848 0.04011  243 MET B O   
4133 C CB  . MET B 243 ? 0.49800 0.46801 0.36995 0.02047  -0.05238 0.00474  243 MET B CB  
4134 C CG  . MET B 243 ? 0.53065 0.48509 0.39719 0.01319  -0.03742 0.00085  243 MET B CG  
4135 S SD  . MET B 243 ? 0.63681 0.59166 0.49650 0.00266  -0.04519 -0.02681 243 MET B SD  
4136 C CE  . MET B 243 ? 0.54158 0.50878 0.35672 0.01525  -0.05890 -0.03462 243 MET B CE  
4137 N N   . VAL B 244 ? 0.47112 0.42278 0.40383 0.01478  -0.04246 0.02308  244 VAL B N   
4138 C CA  . VAL B 244 ? 0.49255 0.43106 0.45232 0.00482  -0.03483 0.02306  244 VAL B CA  
4139 C C   . VAL B 244 ? 0.47767 0.39152 0.43541 0.00918  -0.02404 0.04131  244 VAL B C   
4140 O O   . VAL B 244 ? 0.44873 0.34831 0.41860 -0.00187 -0.01326 0.04390  244 VAL B O   
4141 C CB  . VAL B 244 ? 0.48530 0.43878 0.46781 0.00375  -0.04449 0.01288  244 VAL B CB  
4142 C CG1 . VAL B 244 ? 0.40924 0.34691 0.41254 -0.00303 -0.03697 0.01299  244 VAL B CG1 
4143 C CG2 . VAL B 244 ? 0.44322 0.41707 0.43166 -0.00665 -0.05226 -0.00455 244 VAL B CG2 
4144 N N   . GLU B 245 ? 0.48475 0.39296 0.42715 0.02518  -0.02719 0.05442  245 GLU B N   
4145 C CA  . GLU B 245 ? 0.51039 0.38673 0.44963 0.02885  -0.01639 0.07257  245 GLU B CA  
4146 C C   . GLU B 245 ? 0.53356 0.39563 0.45772 0.02318  -0.00076 0.08719  245 GLU B C   
4147 O O   . GLU B 245 ? 0.55802 0.39316 0.48885 0.01583  0.01154  0.09931  245 GLU B O   
4148 C CB  . GLU B 245 ? 0.52609 0.39743 0.45084 0.05135  -0.02387 0.08395  245 GLU B CB  
4149 C CG  . GLU B 245 ? 0.53442 0.42055 0.48148 0.05719  -0.03529 0.07093  245 GLU B CG  
4150 C CD  . GLU B 245 ? 0.61257 0.48940 0.55033 0.08250  -0.04022 0.08323  245 GLU B CD  
4151 O OE1 . GLU B 245 ? 0.61810 0.49208 0.52822 0.09961  -0.04218 0.09932  245 GLU B OE1 
4152 O OE2 . GLU B 245 ? 0.64037 0.51191 0.59602 0.08787  -0.04159 0.07730  245 GLU B OE2 
4153 N N   . SER B 246 ? 0.51778 0.39769 0.42339 0.02482  0.00006  0.08486  246 SER B N   
4154 C CA  . SER B 246 ? 0.55460 0.42679 0.44792 0.02029  0.01780  0.09844  246 SER B CA  
4155 C C   . SER B 246 ? 0.52356 0.39900 0.44602 0.00090  0.02767  0.09093  246 SER B C   
4156 O O   . SER B 246 ? 0.55864 0.43059 0.48207 -0.00580 0.04441  0.10339  246 SER B O   
4157 C CB  . SER B 246 ? 0.53274 0.42258 0.39215 0.03162  0.01624  0.09673  246 SER B CB  
4158 O OG  . SER B 246 ? 0.56886 0.47789 0.43725 0.02471  0.00827  0.07341  246 SER B OG  
4159 N N   . MET B 247 ? 0.47087 0.35538 0.41760 -0.00753 0.01822  0.07234  247 MET B N   
4160 C CA  . MET B 247 ? 0.50336 0.39374 0.47651 -0.02272 0.02474  0.06525  247 MET B CA  
4161 C C   . MET B 247 ? 0.50412 0.37673 0.50113 -0.03488 0.02869  0.07040  247 MET B C   
4162 O O   . MET B 247 ? 0.53024 0.38195 0.52468 -0.03084 0.02454  0.07498  247 MET B O   
4163 C CB  . MET B 247 ? 0.47154 0.37581 0.45547 -0.02527 0.01351  0.04477  247 MET B CB  
4164 C CG  . MET B 247 ? 0.50247 0.41868 0.46435 -0.01701 0.00768  0.03524  247 MET B CG  
4165 S SD  . MET B 247 ? 0.49414 0.41789 0.47029 -0.02434 0.00088  0.01478  247 MET B SD  
4166 C CE  . MET B 247 ? 0.47894 0.40223 0.47224 -0.02763 -0.01135 0.00872  247 MET B CE  
4167 N N   . THR B 248 ? 0.45419 0.33610 0.47469 -0.04900 0.03566  0.06773  248 THR B N   
4168 C CA  . THR B 248 ? 0.49349 0.36287 0.53935 -0.06431 0.03644  0.06676  248 THR B CA  
4169 C C   . THR B 248 ? 0.46151 0.33097 0.51804 -0.06482 0.02209  0.04854  248 THR B C   
4170 O O   . THR B 248 ? 0.44588 0.32982 0.49661 -0.05711 0.01425  0.03778  248 THR B O   
4171 C CB  . THR B 248 ? 0.48964 0.37908 0.55989 -0.07915 0.04685  0.06911  248 THR B CB  
4172 O OG1 . THR B 248 ? 0.40700 0.32386 0.48507 -0.07575 0.04125  0.05537  248 THR B OG1 
4173 C CG2 . THR B 248 ? 0.43501 0.32972 0.49446 -0.07775 0.06461  0.08814  248 THR B CG2 
4174 N N   . VAL B 249 ? 0.47992 0.33089 0.55060 -0.07485 0.01967  0.04490  249 VAL B N   
4175 C CA  . VAL B 249 ? 0.46060 0.31142 0.53781 -0.07410 0.00782  0.02789  249 VAL B CA  
4176 C C   . VAL B 249 ? 0.41019 0.29058 0.49722 -0.07629 0.00379  0.01713  249 VAL B C   
4177 O O   . VAL B 249 ? 0.42921 0.31690 0.51030 -0.06869 -0.00338 0.00753  249 VAL B O   
4178 C CB  . VAL B 249 ? 0.47152 0.29738 0.56051 -0.08604 0.00611  0.02273  249 VAL B CB  
4179 C CG1 . VAL B 249 ? 0.46159 0.29017 0.55242 -0.08291 -0.00524 0.00421  249 VAL B CG1 
4180 C CG2 . VAL B 249 ? 0.46214 0.24937 0.53741 -0.08072 0.01094  0.03419  249 VAL B CG2 
4181 N N   . LEU B 250 ? 0.38819 0.28664 0.49099 -0.08597 0.00944  0.01991  250 LEU B N   
4182 C CA  . LEU B 250 ? 0.39868 0.32406 0.50948 -0.08409 0.00614  0.01177  250 LEU B CA  
4183 C C   . LEU B 250 ? 0.36408 0.29419 0.45513 -0.07012 0.00611  0.01068  250 LEU B C   
4184 O O   . LEU B 250 ? 0.35761 0.29146 0.44472 -0.06534 -0.00040 0.00135  250 LEU B O   
4185 C CB  . LEU B 250 ? 0.32534 0.27511 0.45772 -0.09309 0.01399  0.01751  250 LEU B CB  
4186 C CG  . LEU B 250 ? 0.34873 0.32813 0.49123 -0.08776 0.01041  0.01044  250 LEU B CG  
4187 C CD1 . LEU B 250 ? 0.32683 0.30486 0.47227 -0.08900 -0.00323 -0.00265 250 LEU B CD1 
4188 C CD2 . LEU B 250 ? 0.41040 0.42165 0.58033 -0.09584 0.01827  0.01650  250 LEU B CD2 
4189 N N   . GLY B 251 ? 0.39561 0.32274 0.47150 -0.06411 0.01329  0.01997  251 GLY B N   
4190 C CA  . GLY B 251 ? 0.37525 0.30432 0.43060 -0.05308 0.01140  0.01594  251 GLY B CA  
4191 C C   . GLY B 251 ? 0.39330 0.31366 0.44131 -0.04993 0.00100  0.00771  251 GLY B C   
4192 O O   . GLY B 251 ? 0.35035 0.27422 0.39311 -0.04755 -0.00313 -0.00113 251 GLY B O   
4193 N N   . GLN B 252 ? 0.37091 0.27935 0.41882 -0.04940 -0.00205 0.01128  252 GLN B N   
4194 C CA  . GLN B 252 ? 0.40195 0.30904 0.44786 -0.04495 -0.01054 0.00392  252 GLN B CA  
4195 C C   . GLN B 252 ? 0.36061 0.27182 0.41727 -0.04957 -0.01390 -0.00665 252 GLN B C   
4196 O O   . GLN B 252 ? 0.36086 0.27892 0.41510 -0.04805 -0.01745 -0.01337 252 GLN B O   
4197 C CB  . GLN B 252 ? 0.42449 0.31643 0.46927 -0.03997 -0.01179 0.01004  252 GLN B CB  
4198 C CG  . GLN B 252 ? 0.43599 0.32228 0.46456 -0.03183 -0.00886 0.02311  252 GLN B CG  
4199 C CD  . GLN B 252 ? 0.46970 0.33567 0.49430 -0.02319 -0.00969 0.03098  252 GLN B CD  
4200 O OE1 . GLN B 252 ? 0.45895 0.31065 0.49383 -0.02549 -0.01060 0.02591  252 GLN B OE1 
4201 N NE2 . GLN B 252 ? 0.47719 0.33986 0.48340 -0.01091 -0.00962 0.04309  252 GLN B NE2 
4202 N N   . ARG B 253 ? 0.33987 0.24807 0.40788 -0.05602 -0.01281 -0.00795 253 ARG B N   
4203 C CA  . ARG B 253 ? 0.35449 0.26773 0.42762 -0.05815 -0.01655 -0.01698 253 ARG B CA  
4204 C C   . ARG B 253 ? 0.37676 0.29984 0.44498 -0.05610 -0.01528 -0.01885 253 ARG B C   
4205 O O   . ARG B 253 ? 0.34677 0.27016 0.41060 -0.05461 -0.01704 -0.02388 253 ARG B O   
4206 C CB  . ARG B 253 ? 0.36518 0.27788 0.45074 -0.06589 -0.01805 -0.01922 253 ARG B CB  
4207 C CG  . ARG B 253 ? 0.37416 0.26703 0.46149 -0.06879 -0.01976 -0.02091 253 ARG B CG  
4208 C CD  . ARG B 253 ? 0.42435 0.31518 0.52511 -0.08085 -0.02290 -0.02619 253 ARG B CD  
4209 N NE  . ARG B 253 ? 0.43997 0.34033 0.53956 -0.08008 -0.03068 -0.03829 253 ARG B NE  
4210 C CZ  . ARG B 253 ? 0.49993 0.42311 0.60741 -0.08242 -0.03430 -0.04046 253 ARG B CZ  
4211 N NH1 . ARG B 253 ? 0.47843 0.41951 0.59962 -0.08634 -0.03010 -0.03264 253 ARG B NH1 
4212 N NH2 . ARG B 253 ? 0.47041 0.40032 0.57044 -0.07834 -0.04174 -0.04995 253 ARG B NH2 
4213 N N   . MET B 254 ? 0.37927 0.30796 0.44649 -0.05509 -0.01051 -0.01415 254 MET B N   
4214 C CA  . MET B 254 ? 0.34533 0.27646 0.40486 -0.05040 -0.00831 -0.01635 254 MET B CA  
4215 C C   . MET B 254 ? 0.33135 0.25359 0.37695 -0.04943 -0.00940 -0.02059 254 MET B C   
4216 O O   . MET B 254 ? 0.34035 0.25598 0.37939 -0.04866 -0.00877 -0.02429 254 MET B O   
4217 C CB  . MET B 254 ? 0.33109 0.27066 0.39117 -0.04646 -0.00129 -0.01119 254 MET B CB  
4218 C CG  . MET B 254 ? 0.36383 0.32087 0.44403 -0.04926 -0.00004 -0.00784 254 MET B CG  
4219 S SD  . MET B 254 ? 0.36085 0.32589 0.44674 -0.04566 -0.00718 -0.01349 254 MET B SD  
4220 C CE  . MET B 254 ? 0.36125 0.32751 0.46081 -0.05754 -0.01579 -0.01800 254 MET B CE  
4221 N N   . LEU B 255 ? 0.31188 0.23393 0.35308 -0.04988 -0.01145 -0.01984 255 LEU B N   
4222 C CA  . LEU B 255 ? 0.32665 0.24722 0.35822 -0.05117 -0.01477 -0.02564 255 LEU B CA  
4223 C C   . LEU B 255 ? 0.31821 0.24490 0.35879 -0.05487 -0.01924 -0.02907 255 LEU B C   
4224 O O   . LEU B 255 ? 0.34200 0.27622 0.38151 -0.05743 -0.02365 -0.03345 255 LEU B O   
4225 C CB  . LEU B 255 ? 0.33864 0.26197 0.35790 -0.04706 -0.01615 -0.02355 255 LEU B CB  
4226 C CG  . LEU B 255 ? 0.40940 0.32924 0.41773 -0.04184 -0.00853 -0.02006 255 LEU B CG  
4227 C CD1 . LEU B 255 ? 0.38563 0.30669 0.37300 -0.03618 -0.00936 -0.01973 255 LEU B CD1 
4228 C CD2 . LEU B 255 ? 0.32671 0.23784 0.33091 -0.04079 -0.00446 -0.02588 255 LEU B CD2 
4229 N N   . GLY B 256 ? 0.30766 0.23447 0.35728 -0.05495 -0.01827 -0.02827 256 GLY B N   
4230 C CA  . GLY B 256 ? 0.35277 0.28691 0.40936 -0.05668 -0.01915 -0.03166 256 GLY B CA  
4231 C C   . GLY B 256 ? 0.35832 0.30280 0.42199 -0.05130 -0.02286 -0.03098 256 GLY B C   
4232 O O   . GLY B 256 ? 0.35374 0.31169 0.42568 -0.05126 -0.02285 -0.03400 256 GLY B O   
4233 N N   . TRP B 257 ? 0.32656 0.26554 0.38730 -0.04555 -0.02473 -0.02578 257 TRP B N   
4234 C CA  . TRP B 257 ? 0.36847 0.31305 0.43195 -0.03626 -0.02833 -0.02292 257 TRP B CA  
4235 C C   . TRP B 257 ? 0.34925 0.28148 0.41648 -0.03026 -0.02639 -0.02280 257 TRP B C   
4236 O O   . TRP B 257 ? 0.36266 0.29398 0.43052 -0.01904 -0.02822 -0.01992 257 TRP B O   
4237 C CB  . TRP B 257 ? 0.36498 0.30514 0.41730 -0.03123 -0.03034 -0.01505 257 TRP B CB  
4238 C CG  . TRP B 257 ? 0.37550 0.33257 0.42174 -0.03256 -0.03603 -0.01872 257 TRP B CG  
4239 C CD1 . TRP B 257 ? 0.37601 0.33038 0.41217 -0.03960 -0.03502 -0.02274 257 TRP B CD1 
4240 C CD2 . TRP B 257 ? 0.40000 0.38021 0.45031 -0.02685 -0.04463 -0.02115 257 TRP B CD2 
4241 N NE1 . TRP B 257 ? 0.38105 0.35119 0.41233 -0.04067 -0.04314 -0.02913 257 TRP B NE1 
4242 C CE2 . TRP B 257 ? 0.40565 0.39579 0.44769 -0.03382 -0.05002 -0.02815 257 TRP B CE2 
4243 C CE3 . TRP B 257 ? 0.45709 0.45231 0.51762 -0.01515 -0.04882 -0.01890 257 TRP B CE3 
4244 C CZ2 . TRP B 257 ? 0.38695 0.40473 0.43259 -0.03243 -0.06132 -0.03379 257 TRP B CZ2 
4245 C CZ3 . TRP B 257 ? 0.42337 0.45041 0.48972 -0.01102 -0.05920 -0.02253 257 TRP B CZ3 
4246 C CH2 . TRP B 257 ? 0.37730 0.41692 0.43706 -0.02114 -0.06630 -0.03035 257 TRP B CH2 
4247 N N   . ARG B 258 ? 0.32241 0.24444 0.39015 -0.03587 -0.02358 -0.02679 258 ARG B N   
4248 C CA  . ARG B 258 ? 0.39360 0.29945 0.46117 -0.03221 -0.02307 -0.03025 258 ARG B CA  
4249 C C   . ARG B 258 ? 0.38586 0.29679 0.45247 -0.03376 -0.02168 -0.03882 258 ARG B C   
4250 O O   . ARG B 258 ? 0.37203 0.29294 0.43758 -0.03969 -0.02034 -0.03925 258 ARG B O   
4251 C CB  . ARG B 258 ? 0.37997 0.26622 0.44694 -0.03920 -0.02281 -0.02700 258 ARG B CB  
4252 C CG  . ARG B 258 ? 0.41874 0.29667 0.48253 -0.03701 -0.02115 -0.01548 258 ARG B CG  
4253 C CD  . ARG B 258 ? 0.44712 0.30170 0.51304 -0.04479 -0.01821 -0.01119 258 ARG B CD  
4254 N NE  . ARG B 258 ? 0.45529 0.29336 0.51325 -0.03845 -0.01469 0.00188  258 ARG B NE  
4255 C CZ  . ARG B 258 ? 0.47001 0.27664 0.52395 -0.03530 -0.01255 0.00560  258 ARG B CZ  
4256 N NH1 . ARG B 258 ? 0.51623 0.30320 0.57406 -0.04023 -0.01415 -0.00539 258 ARG B NH1 
4257 N NH2 . ARG B 258 ? 0.52164 0.31298 0.56399 -0.02594 -0.00885 0.02048  258 ARG B NH2 
4258 N N   . THR B 259 ? 0.34782 0.24822 0.41098 -0.02658 -0.02130 -0.04531 259 THR B N   
4259 C CA  . THR B 259 ? 0.36371 0.26594 0.41963 -0.02598 -0.01996 -0.05401 259 THR B CA  
4260 C C   . THR B 259 ? 0.38312 0.27783 0.43568 -0.03584 -0.02463 -0.05684 259 THR B C   
4261 O O   . THR B 259 ? 0.39993 0.28183 0.45744 -0.04224 -0.02811 -0.05575 259 THR B O   
4262 C CB  . THR B 259 ? 0.39365 0.28284 0.44268 -0.01367 -0.01853 -0.06252 259 THR B CB  
4263 O OG1 . THR B 259 ? 0.39832 0.30408 0.45432 -0.00168 -0.01385 -0.05925 259 THR B OG1 
4264 C CG2 . THR B 259 ? 0.37375 0.26271 0.40890 -0.01155 -0.01752 -0.07300 259 THR B CG2 
4265 N N   . MET B 260 ? 0.38224 0.28718 0.42720 -0.03677 -0.02428 -0.05926 260 MET B N   
4266 C CA  . MET B 260 ? 0.37598 0.28272 0.41906 -0.04301 -0.03017 -0.06093 260 MET B CA  
4267 C C   . MET B 260 ? 0.41964 0.32680 0.44622 -0.03793 -0.03328 -0.07058 260 MET B C   
4268 O O   . MET B 260 ? 0.43555 0.34124 0.45082 -0.02946 -0.02817 -0.07480 260 MET B O   
4269 C CB  . MET B 260 ? 0.34609 0.26437 0.39154 -0.04555 -0.02748 -0.05145 260 MET B CB  
4270 C CG  . MET B 260 ? 0.37217 0.29044 0.42801 -0.04903 -0.02453 -0.04390 260 MET B CG  
4271 S SD  . MET B 260 ? 0.38887 0.30237 0.45713 -0.05592 -0.02782 -0.04132 260 MET B SD  
4272 C CE  . MET B 260 ? 0.33281 0.26100 0.40381 -0.05696 -0.02776 -0.03683 260 MET B CE  
4273 N N   . LYS B 261 ? 0.38802 0.30105 0.41247 -0.04156 -0.04173 -0.07417 261 LYS B N   
4274 C CA  . LYS B 261 ? 0.43051 0.34491 0.43564 -0.03618 -0.04817 -0.08534 261 LYS B CA  
4275 C C   . LYS B 261 ? 0.44455 0.37623 0.44166 -0.03266 -0.05274 -0.08009 261 LYS B C   
4276 O O   . LYS B 261 ? 0.41236 0.35620 0.42265 -0.03829 -0.06201 -0.08051 261 LYS B O   
4277 C CB  . LYS B 261 ? 0.42484 0.32689 0.43362 -0.04367 -0.05884 -0.10064 261 LYS B CB  
4278 C CG  . LYS B 261 ? 0.48171 0.38482 0.46853 -0.03962 -0.06945 -0.11698 261 LYS B CG  
4279 C CD  . LYS B 261 ? 0.50400 0.39621 0.46373 -0.02511 -0.06172 -0.12355 261 LYS B CD  
4280 C CE  . LYS B 261 ? 0.58430 0.47249 0.51816 -0.02130 -0.07380 -0.14373 261 LYS B CE  
4281 N NZ  . LYS B 261 ? 0.57349 0.48751 0.49964 -0.02050 -0.08506 -0.14152 261 LYS B NZ  
4282 N N   . PRO B 262 ? 0.40801 0.34221 0.38446 -0.02252 -0.04537 -0.07348 262 PRO B N   
4283 C CA  . PRO B 262 ? 0.42483 0.37037 0.38334 -0.01403 -0.05129 -0.07019 262 PRO B CA  
4284 C C   . PRO B 262 ? 0.42166 0.37363 0.36690 -0.01173 -0.06643 -0.08686 262 PRO B C   
4285 O O   . PRO B 262 ? 0.47612 0.41692 0.41784 -0.01472 -0.06883 -0.10143 262 PRO B O   
4286 C CB  . PRO B 262 ? 0.42828 0.36787 0.36371 -0.00487 -0.03675 -0.05942 262 PRO B CB  
4287 C CG  . PRO B 262 ? 0.41583 0.34809 0.36693 -0.01173 -0.02411 -0.05573 262 PRO B CG  
4288 C CD  . PRO B 262 ? 0.42598 0.35459 0.39473 -0.01812 -0.03076 -0.06791 262 PRO B CD  
4289 N N   . SER B 263 ? 0.44812 0.41753 0.38364 -0.00480 -0.07750 -0.08560 263 SER B N   
4290 C CA  . SER B 263 ? 0.49443 0.47444 0.41560 -0.00300 -0.09507 -0.10351 263 SER B CA  
4291 C C   . SER B 263 ? 0.54180 0.50992 0.42361 0.00900  -0.09030 -0.11083 263 SER B C   
4292 O O   . SER B 263 ? 0.48336 0.44269 0.34712 0.01855  -0.07301 -0.09739 263 SER B O   
4293 C CB  . SER B 263 ? 0.52335 0.53199 0.44251 0.00513  -0.10972 -0.09967 263 SER B CB  
4294 O OG  . SER B 263 ? 0.59315 0.62005 0.55176 -0.00803 -0.11824 -0.10135 263 SER B OG  
4295 N N   . ASP B 264 ? 0.54702 0.51487 0.41618 0.00713  -0.10517 -0.13348 264 ASP B N   
4296 C CA  . ASP B 264 ? 0.58860 0.55124 0.41298 0.02233  -0.10479 -0.14318 264 ASP B CA  
4297 C C   . ASP B 264 ? 0.57284 0.55050 0.36858 0.04013  -0.10148 -0.12480 264 ASP B C   
4298 O O   . ASP B 264 ? 0.57881 0.57636 0.38520 0.04167  -0.11234 -0.11602 264 ASP B O   
4299 C CB  . ASP B 264 ? 0.61031 0.57488 0.42248 0.01771  -0.12768 -0.17235 264 ASP B CB  
4300 C CG  . ASP B 264 ? 0.76490 0.70830 0.60738 -0.00284 -0.13211 -0.18962 264 ASP B CG  
4301 O OD1 . ASP B 264 ? 0.71179 0.63515 0.57351 -0.00743 -0.11557 -0.18095 264 ASP B OD1 
4302 O OD2 . ASP B 264 ? 0.87208 0.81890 0.71823 -0.01468 -0.15306 -0.21191 264 ASP B OD2 
4303 N N   . PRO B 265 ? 0.60561 0.57467 0.36357 0.05536  -0.08614 -0.11797 265 PRO B N   
4304 C CA  . PRO B 265 ? 0.61263 0.56566 0.34961 0.06037  -0.07395 -0.13004 265 PRO B CA  
4305 C C   . PRO B 265 ? 0.58359 0.52318 0.34767 0.05289  -0.05237 -0.12189 265 PRO B C   
4306 O O   . PRO B 265 ? 0.60068 0.53168 0.34922 0.06055  -0.04033 -0.12979 265 PRO B O   
4307 C CB  . PRO B 265 ? 0.65457 0.61254 0.34041 0.08158  -0.06440 -0.11972 265 PRO B CB  
4308 C CG  . PRO B 265 ? 0.63922 0.60385 0.33071 0.08407  -0.05837 -0.09116 265 PRO B CG  
4309 C CD  . PRO B 265 ? 0.60851 0.58470 0.33753 0.07190  -0.07912 -0.09551 265 PRO B CD  
4310 N N   . ASN B 266 ? 0.53844 0.47800 0.34132 0.04004  -0.04737 -0.10785 266 ASN B N   
4311 C CA  . ASN B 266 ? 0.53617 0.46585 0.36683 0.03213  -0.03479 -0.10748 266 ASN B CA  
4312 C C   . ASN B 266 ? 0.61103 0.52766 0.45489 0.02434  -0.04887 -0.12947 266 ASN B C   
4313 O O   . ASN B 266 ? 0.63053 0.54833 0.49784 0.01127  -0.06293 -0.13250 266 ASN B O   
4314 C CB  . ASN B 266 ? 0.48768 0.42031 0.35136 0.02092  -0.02767 -0.08855 266 ASN B CB  
4315 C CG  . ASN B 266 ? 0.51664 0.44438 0.40724 0.01458  -0.01643 -0.08735 266 ASN B CG  
4316 O OD1 . ASN B 266 ? 0.59011 0.50837 0.48601 0.01518  -0.01972 -0.10155 266 ASN B OD1 
4317 N ND2 . ASN B 266 ? 0.48504 0.41804 0.39161 0.00913  -0.00397 -0.07078 266 ASN B ND2 
4318 N N   . ILE B 267 ? 0.59536 0.49796 0.42358 0.03257  -0.04410 -0.14477 267 ILE B N   
4319 C CA  . ILE B 267 ? 0.67829 0.55863 0.51459 0.02534  -0.05629 -0.16601 267 ILE B CA  
4320 C C   . ILE B 267 ? 0.67279 0.53760 0.53461 0.02351  -0.04513 -0.16248 267 ILE B C   
4321 O O   . ILE B 267 ? 0.73989 0.57836 0.60706 0.01884  -0.05204 -0.17743 267 ILE B O   
4322 C CB  . ILE B 267 ? 0.70893 0.57576 0.50487 0.03677  -0.06371 -0.19125 267 ILE B CB  
4323 C CG1 . ILE B 267 ? 0.77459 0.64302 0.54189 0.05844  -0.04318 -0.18933 267 ILE B CG1 
4324 C CG2 . ILE B 267 ? 0.69356 0.57770 0.46771 0.03609  -0.08204 -0.19743 267 ILE B CG2 
4325 C CD1 . ILE B 267 ? 0.87163 0.71696 0.64422 0.06658  -0.03262 -0.19974 267 ILE B CD1 
4326 N N   . VAL B 268 ? 0.63194 0.51135 0.50996 0.02637  -0.02908 -0.14303 268 VAL B N   
4327 C CA  . VAL B 268 ? 0.60701 0.47942 0.50754 0.02857  -0.01929 -0.13863 268 VAL B CA  
4328 C C   . VAL B 268 ? 0.59007 0.46826 0.52452 0.01369  -0.02153 -0.12313 268 VAL B C   
4329 O O   . VAL B 268 ? 0.58621 0.44756 0.53738 0.00879  -0.02529 -0.12474 268 VAL B O   
4330 C CB  . VAL B 268 ? 0.60636 0.49737 0.50162 0.04394  0.00052  -0.13111 268 VAL B CB  
4331 C CG1 . VAL B 268 ? 0.60299 0.49502 0.52499 0.04799  0.00804  -0.12593 268 VAL B CG1 
4332 C CG2 . VAL B 268 ? 0.66972 0.55414 0.52789 0.06182  0.00514  -0.14724 268 VAL B CG2 
4333 N N   . GLY B 269 ? 0.50868 0.40738 0.45008 0.00777  -0.01808 -0.10762 269 GLY B N   
4334 C CA  . GLY B 269 ? 0.49721 0.40110 0.46517 -0.00443 -0.01957 -0.09460 269 GLY B CA  
4335 C C   . GLY B 269 ? 0.45002 0.37243 0.42498 -0.00497 -0.00712 -0.07924 269 GLY B C   
4336 O O   . GLY B 269 ? 0.42825 0.36030 0.38748 0.00124  0.00242  -0.07579 269 GLY B O   
4337 N N   . ILE B 270 ? 0.40080 0.32685 0.39832 -0.01347 -0.00679 -0.07025 270 ILE B N   
4338 C CA  . ILE B 270 ? 0.39716 0.33792 0.40448 -0.01833 0.00293  -0.05825 270 ILE B CA  
4339 C C   . ILE B 270 ? 0.36847 0.31275 0.39865 -0.02349 0.00070  -0.05501 270 ILE B C   
4340 O O   . ILE B 270 ? 0.38259 0.31507 0.41814 -0.02457 -0.00757 -0.05777 270 ILE B O   
4341 C CB  . ILE B 270 ? 0.37613 0.31392 0.37420 -0.02418 0.00246  -0.04987 270 ILE B CB  
4342 C CG1 . ILE B 270 ? 0.38688 0.33246 0.38488 -0.02852 0.01592  -0.03923 270 ILE B CG1 
4343 C CG2 . ILE B 270 ? 0.38198 0.31331 0.39233 -0.03187 -0.00642 -0.04721 270 ILE B CG2 
4344 C CD1 . ILE B 270 ? 0.43811 0.37401 0.41522 -0.02740 0.01869  -0.03081 270 ILE B CD1 
4345 N N   . ASN B 271 ? 0.36196 0.32375 0.40526 -0.02732 0.00813  -0.04896 271 ASN B N   
4346 C CA  . ASN B 271 ? 0.36424 0.33478 0.42673 -0.03127 0.00435  -0.04643 271 ASN B CA  
4347 C C   . ASN B 271 ? 0.38245 0.35367 0.45106 -0.01868 0.00116  -0.05093 271 ASN B C   
4348 O O   . ASN B 271 ? 0.35057 0.30960 0.42162 -0.01759 -0.00625 -0.05000 271 ASN B O   
4349 C CB  . ASN B 271 ? 0.37418 0.33075 0.43583 -0.03968 -0.00323 -0.04325 271 ASN B CB  
4350 C CG  . ASN B 271 ? 0.36746 0.33420 0.44227 -0.04430 -0.00650 -0.04060 271 ASN B CG  
4351 O OD1 . ASN B 271 ? 0.36136 0.34727 0.44712 -0.04909 -0.00304 -0.03998 271 ASN B OD1 
4352 N ND2 . ASN B 271 ? 0.33550 0.29157 0.40913 -0.04369 -0.01313 -0.03913 271 ASN B ND2 
4353 N N   . LEU B 272 ? 0.38548 0.36930 0.45438 -0.00728 0.00857  -0.05478 272 LEU B N   
4354 C CA  . LEU B 272 ? 0.39299 0.37394 0.46449 0.00957  0.00746  -0.05939 272 LEU B CA  
4355 C C   . LEU B 272 ? 0.35069 0.36963 0.44128 0.01833  0.01545  -0.05742 272 LEU B C   
4356 O O   . LEU B 272 ? 0.34124 0.38702 0.44261 0.00833  0.02305  -0.05349 272 LEU B O   
4357 C CB  . LEU B 272 ? 0.37080 0.32532 0.42026 0.01951  0.00806  -0.06990 272 LEU B CB  
4358 C CG  . LEU B 272 ? 0.42674 0.38890 0.46000 0.02293  0.01733  -0.07469 272 LEU B CG  
4359 C CD1 . LEU B 272 ? 0.50089 0.46148 0.52447 0.04399  0.02436  -0.08446 272 LEU B CD1 
4360 C CD2 . LEU B 272 ? 0.44129 0.38114 0.45324 0.01471  0.01045  -0.07936 272 LEU B CD2 
4361 N N   . ILE B 273 ? 0.33739 0.35910 0.43362 0.03720  0.01429  -0.05947 273 ILE B N   
4362 C CA  . ILE B 273 ? 0.37342 0.43921 0.49309 0.04877  0.02032  -0.05739 273 ILE B CA  
4363 C C   . ILE B 273 ? 0.38579 0.44112 0.49855 0.07723  0.02320  -0.06291 273 ILE B C   
4364 O O   . ILE B 273 ? 0.42267 0.43677 0.51928 0.08545  0.01610  -0.06496 273 ILE B O   
4365 C CB  . ILE B 273 ? 0.35055 0.44363 0.49333 0.04114  0.01073  -0.05042 273 ILE B CB  
4366 C CG1 . ILE B 273 ? 0.36270 0.51203 0.53601 0.05189  0.01488  -0.04913 273 ILE B CG1 
4367 C CG2 . ILE B 273 ? 0.39084 0.45308 0.52269 0.04832  -0.00150 -0.04727 273 ILE B CG2 
4368 C CD1 . ILE B 273 ? 0.34234 0.52602 0.53017 0.03979  0.02983  -0.04944 273 ILE B CD1 
4369 N N   . ASP B 274 ? 0.38526 0.47651 0.51008 0.09229  0.03528  -0.06505 274 ASP B N   
4370 C CA  . ASP B 274 ? 0.41808 0.50248 0.53600 0.12413  0.04081  -0.07131 274 ASP B CA  
4371 C C   . ASP B 274 ? 0.45325 0.47929 0.53348 0.13083  0.04160  -0.08320 274 ASP B C   
4372 O O   . ASP B 274 ? 0.47960 0.47457 0.54625 0.15382  0.04096  -0.08939 274 ASP B O   
4373 C CB  . ASP B 274 ? 0.42556 0.51180 0.55564 0.14212  0.03076  -0.06543 274 ASP B CB  
4374 C CG  . ASP B 274 ? 0.47431 0.62408 0.64199 0.13702  0.02669  -0.05655 274 ASP B CG  
4375 O OD1 . ASP B 274 ? 0.48071 0.68162 0.67165 0.13075  0.03714  -0.05667 274 ASP B OD1 
4376 O OD2 . ASP B 274 ? 0.51556 0.66503 0.68902 0.13836  0.01309  -0.04957 274 ASP B OD2 
4377 N N   . ASP B 275 ? 0.44924 0.45880 0.51148 0.11126  0.04207  -0.08705 275 ASP B N   
4378 C CA  . ASP B 275 ? 0.52498 0.48330 0.55301 0.11186  0.03835  -0.10005 275 ASP B CA  
4379 C C   . ASP B 275 ? 0.57077 0.48202 0.59248 0.10758  0.02464  -0.10081 275 ASP B C   
4380 O O   . ASP B 275 ? 0.52858 0.39403 0.52651 0.11240  0.02122  -0.11338 275 ASP B O   
4381 C CB  . ASP B 275 ? 0.56362 0.51352 0.57055 0.13831  0.04962  -0.11390 275 ASP B CB  
4382 C CG  . ASP B 275 ? 0.65623 0.57098 0.62619 0.13313  0.04740  -0.12904 275 ASP B CG  
4383 O OD1 . ASP B 275 ? 0.66171 0.56970 0.62754 0.10938  0.03846  -0.12623 275 ASP B OD1 
4384 O OD2 . ASP B 275 ? 0.64268 0.53764 0.58683 0.15403  0.05366  -0.14453 275 ASP B OD2 
4385 N N   . LYS B 276 ? 0.50623 0.42767 0.54792 0.09729  0.01732  -0.08770 276 LYS B N   
4386 C CA  . LYS B 276 ? 0.50819 0.38992 0.54534 0.09191  0.00722  -0.08389 276 LYS B CA  
4387 C C   . LYS B 276 ? 0.47400 0.36224 0.51909 0.06511  -0.00005 -0.07550 276 LYS B C   
4388 O O   . LYS B 276 ? 0.43719 0.36086 0.49399 0.05378  0.00185  -0.07088 276 LYS B O   
4389 C CB  . LYS B 276 ? 0.50251 0.38837 0.55076 0.11224  0.00619  -0.07422 276 LYS B CB  
4390 C CG  . LYS B 276 ? 0.60768 0.48008 0.64648 0.14369  0.01348  -0.08189 276 LYS B CG  
4391 C CD  . LYS B 276 ? 0.65896 0.56017 0.71592 0.16766  0.01308  -0.07004 276 LYS B CD  
4392 C CE  . LYS B 276 ? 0.71063 0.58515 0.76505 0.16425  0.00320  -0.05626 276 LYS B CE  
4393 N NZ  . LYS B 276 ? 0.77065 0.68491 0.84312 0.18601  -0.00061 -0.04332 276 LYS B NZ  
4394 N N   . ARG B 277 ? 0.45502 0.30717 0.49354 0.05512  -0.00699 -0.07332 277 ARG B N   
4395 C CA  . ARG B 277 ? 0.45864 0.31866 0.50532 0.03407  -0.01234 -0.06428 277 ARG B CA  
4396 C C   . ARG B 277 ? 0.43200 0.32016 0.49339 0.03770  -0.01377 -0.05137 277 ARG B C   
4397 O O   . ARG B 277 ? 0.43788 0.32395 0.50096 0.05517  -0.01417 -0.04592 277 ARG B O   
4398 C CB  . ARG B 277 ? 0.49495 0.31497 0.53446 0.02210  -0.01712 -0.06390 277 ARG B CB  
4399 C CG  . ARG B 277 ? 0.60049 0.39523 0.62713 0.01473  -0.01942 -0.07957 277 ARG B CG  
4400 C CD  . ARG B 277 ? 0.64159 0.40203 0.66812 -0.00205 -0.02421 -0.07959 277 ARG B CD  
4401 N NE  . ARG B 277 ? 0.75546 0.48702 0.76905 -0.00683 -0.02833 -0.09809 277 ARG B NE  
4402 C CZ  . ARG B 277 ? 0.89628 0.60189 0.91224 -0.02592 -0.03383 -0.10342 277 ARG B CZ  
4403 N NH1 . ARG B 277 ? 0.90668 0.61386 0.93838 -0.04194 -0.03361 -0.08979 277 ARG B NH1 
4404 N NH2 . ARG B 277 ? 0.89673 0.57576 0.89913 -0.02976 -0.03936 -0.12374 277 ARG B NH2 
4405 N N   . LEU B 278 ? 0.42659 0.33971 0.49641 0.02219  -0.01543 -0.04721 278 LEU B N   
4406 C CA  . LEU B 278 ? 0.40137 0.34403 0.48352 0.02227  -0.01866 -0.03894 278 LEU B CA  
4407 C C   . LEU B 278 ? 0.39936 0.32444 0.47574 0.02836  -0.02374 -0.02902 278 LEU B C   
4408 O O   . LEU B 278 ? 0.36696 0.31132 0.44868 0.04140  -0.02754 -0.02308 278 LEU B O   
4409 C CB  . LEU B 278 ? 0.36087 0.31954 0.44702 0.00280  -0.01914 -0.03862 278 LEU B CB  
4410 C CG  . LEU B 278 ? 0.37760 0.35816 0.47117 -0.00238 -0.02462 -0.03326 278 LEU B CG  
4411 C CD1 . LEU B 278 ? 0.34313 0.36171 0.45377 0.00692  -0.02606 -0.03401 278 LEU B CD1 
4412 C CD2 . LEU B 278 ? 0.35424 0.33749 0.44648 -0.02093 -0.02366 -0.03483 278 LEU B CD2 
4413 N N   . GLU B 279 ? 0.39270 0.28385 0.45841 0.01937  -0.02365 -0.02620 279 GLU B N   
4414 C CA  . GLU B 279 ? 0.45658 0.32745 0.51390 0.02462  -0.02522 -0.01391 279 GLU B CA  
4415 C C   . GLU B 279 ? 0.49409 0.34257 0.54448 0.04693  -0.02409 -0.01030 279 GLU B C   
4416 O O   . GLU B 279 ? 0.49998 0.34177 0.54278 0.05912  -0.02597 0.00258  279 GLU B O   
4417 C CB  . GLU B 279 ? 0.46608 0.30912 0.51795 0.00738  -0.02268 -0.01086 279 GLU B CB  
4418 C CG  . GLU B 279 ? 0.48472 0.29728 0.53477 0.00052  -0.02053 -0.02066 279 GLU B CG  
4419 C CD  . GLU B 279 ? 0.49384 0.32418 0.54931 -0.01100 -0.02196 -0.03357 279 GLU B CD  
4420 O OE1 . GLU B 279 ? 0.41707 0.27826 0.47704 -0.00895 -0.02223 -0.03617 279 GLU B OE1 
4421 O OE2 . GLU B 279 ? 0.49799 0.31106 0.55284 -0.02268 -0.02301 -0.04063 279 GLU B OE2 
4422 N N   . ASN B 280 ? 0.48276 0.31873 0.53234 0.05539  -0.02076 -0.02116 280 ASN B N   
4423 C CA  . ASN B 280 ? 0.49147 0.30505 0.53314 0.08110  -0.01876 -0.01890 280 ASN B CA  
4424 C C   . ASN B 280 ? 0.51977 0.37919 0.57358 0.10290  -0.02149 -0.01529 280 ASN B C   
4425 O O   . ASN B 280 ? 0.49035 0.34305 0.53855 0.12558  -0.02354 -0.00464 280 ASN B O   
4426 C CB  . ASN B 280 ? 0.52721 0.31163 0.56083 0.08523  -0.01394 -0.03446 280 ASN B CB  
4427 C CG  . ASN B 280 ? 0.65124 0.38525 0.67329 0.06647  -0.01340 -0.03882 280 ASN B CG  
4428 O OD1 . ASN B 280 ? 0.63803 0.35135 0.65778 0.05496  -0.01378 -0.02673 280 ASN B OD1 
4429 N ND2 . ASN B 280 ? 0.66204 0.37827 0.67678 0.06280  -0.01235 -0.05649 280 ASN B ND2 
4430 N N   . VAL B 281 ? 0.48789 0.39490 0.55913 0.09692  -0.02123 -0.02346 281 VAL B N   
4431 C CA  . VAL B 281 ? 0.41746 0.37725 0.50755 0.11306  -0.02424 -0.02110 281 VAL B CA  
4432 C C   . VAL B 281 ? 0.43174 0.41109 0.52345 0.11237  -0.03456 -0.00934 281 VAL B C   
4433 O O   . VAL B 281 ? 0.42426 0.43005 0.52246 0.13455  -0.04052 -0.00277 281 VAL B O   
4434 C CB  . VAL B 281 ? 0.44378 0.44849 0.55358 0.09998  -0.01987 -0.03083 281 VAL B CB  
4435 C CG1 . VAL B 281 ? 0.37422 0.44113 0.51060 0.11019  -0.02369 -0.02863 281 VAL B CG1 
4436 C CG2 . VAL B 281 ? 0.47222 0.46035 0.57488 0.10622  -0.00906 -0.04198 281 VAL B CG2 
4437 N N   . LEU B 282 ? 0.42103 0.38921 0.50502 0.08931  -0.03717 -0.00686 282 LEU B N   
4438 C CA  . LEU B 282 ? 0.45306 0.43552 0.53159 0.08849  -0.04630 0.00272  282 LEU B CA  
4439 C C   . LEU B 282 ? 0.49489 0.43569 0.54941 0.10273  -0.04625 0.01793  282 LEU B C   
4440 O O   . LEU B 282 ? 0.50191 0.45456 0.54636 0.10831  -0.05363 0.02785  282 LEU B O   
4441 C CB  . LEU B 282 ? 0.37820 0.36451 0.45547 0.06081  -0.04705 -0.00128 282 LEU B CB  
4442 C CG  . LEU B 282 ? 0.41446 0.43866 0.51143 0.04381  -0.04763 -0.01303 282 LEU B CG  
4443 C CD1 . LEU B 282 ? 0.40729 0.42117 0.49606 0.02107  -0.04726 -0.01539 282 LEU B CD1 
4444 C CD2 . LEU B 282 ? 0.37721 0.45416 0.49291 0.05107  -0.05695 -0.01516 282 LEU B CD2 
4445 N N   . GLN B 283 ? 0.51309 0.40392 0.55621 0.10800  -0.03791 0.01981  283 GLN B N   
4446 C CA  . GLN B 283 ? 0.56975 0.41023 0.58946 0.11580  -0.03429 0.03559  283 GLN B CA  
4447 C C   . GLN B 283 ? 0.54355 0.38140 0.55291 0.09706  -0.03433 0.04452  283 GLN B C   
4448 O O   . GLN B 283 ? 0.57625 0.40968 0.56806 0.10818  -0.03654 0.06045  283 GLN B O   
4449 C CB  . GLN B 283 ? 0.56213 0.40282 0.57209 0.15042  -0.03850 0.04854  283 GLN B CB  
4450 C CG  . GLN B 283 ? 0.60714 0.46013 0.63016 0.17238  -0.03753 0.03875  283 GLN B CG  
4451 C CD  . GLN B 283 ? 0.74769 0.59516 0.76014 0.21092  -0.04062 0.05234  283 GLN B CD  
4452 O OE1 . GLN B 283 ? 0.78186 0.68162 0.80310 0.22738  -0.05151 0.05763  283 GLN B OE1 
4453 N NE2 . GLN B 283 ? 0.84485 0.62766 0.83754 0.22633  -0.03187 0.05784  283 GLN B NE2 
4454 N N   . LEU B 284 ? 0.50236 0.34474 0.52096 0.07081  -0.03136 0.03434  284 LEU B N   
4455 C CA  . LEU B 284 ? 0.56817 0.41421 0.58027 0.05331  -0.02986 0.03951  284 LEU B CA  
4456 C C   . LEU B 284 ? 0.57791 0.37804 0.57579 0.04721  -0.01992 0.05356  284 LEU B C   
4457 O O   . LEU B 284 ? 0.59413 0.36320 0.59776 0.03590  -0.01373 0.04898  284 LEU B O   
4458 C CB  . LEU B 284 ? 0.53831 0.40257 0.56582 0.03126  -0.02920 0.02449  284 LEU B CB  
4459 C CG  . LEU B 284 ? 0.57597 0.46659 0.60214 0.01969  -0.03187 0.02259  284 LEU B CG  
4460 C CD1 . LEU B 284 ? 0.54067 0.46405 0.56326 0.03258  -0.04209 0.02317  284 LEU B CD1 
4461 C CD2 . LEU B 284 ? 0.50731 0.41082 0.54834 0.00324  -0.03088 0.00816  284 LEU B CD2 
4462 N N   . LYS B 285 ? 0.59745 0.39744 0.57746 0.05189  -0.01846 0.06919  285 LYS B N   
4463 C CA  . LYS B 285 ? 0.61056 0.37227 0.57944 0.04150  -0.00576 0.08452  285 LYS B CA  
4464 C C   . LYS B 285 ? 0.57180 0.35449 0.54919 0.01935  -0.00154 0.07938  285 LYS B C   
4465 O O   . LYS B 285 ? 0.57081 0.39040 0.55328 0.01798  -0.00917 0.06771  285 LYS B O   
4466 C CB  . LYS B 285 ? 0.65151 0.39837 0.59155 0.06086  -0.00308 0.10785  285 LYS B CB  
4467 C CG  . LYS B 285 ? 0.68836 0.41632 0.61697 0.08935  -0.00792 0.11572  285 LYS B CG  
4468 C CD  . LYS B 285 ? 0.74666 0.44989 0.64226 0.10867  -0.00301 0.14282  285 LYS B CD  
4469 C CE  . LYS B 285 ? 0.79792 0.47190 0.68064 0.13937  -0.00560 0.15320  285 LYS B CE  
4470 N NZ  . LYS B 285 ? 0.87563 0.60073 0.75946 0.16601  -0.02318 0.14776  285 LYS B NZ  
4471 N N   . ALA B 286 ? 0.62117 0.38086 0.60113 0.00293  0.01070  0.08790  286 ALA B N   
4472 C CA  . ALA B 286 ? 0.60818 0.38908 0.59732 -0.01484 0.01695  0.08571  286 ALA B CA  
4473 C C   . ALA B 286 ? 0.66484 0.42534 0.64422 -0.02188 0.03307  0.10713  286 ALA B C   
4474 O O   . ALA B 286 ? 0.66407 0.38499 0.63726 -0.02185 0.04036  0.12060  286 ALA B O   
4475 C CB  . ALA B 286 ? 0.56457 0.35212 0.58116 -0.03368 0.01511  0.06827  286 ALA B CB  
4476 N N   . ALA B 287 ? 0.63292 0.41882 0.61066 -0.02798 0.04033  0.11044  287 ALA B N   
4477 C CA  . ALA B 287 ? 0.67277 0.44703 0.63958 -0.03309 0.05852  0.13276  287 ALA B CA  
4478 C C   . ALA B 287 ? 0.72184 0.46904 0.71221 -0.05595 0.06998  0.13889  287 ALA B C   
4479 O O   . ALA B 287 ? 0.71793 0.43451 0.69705 -0.05912 0.08456  0.16086  287 ALA B O   
4480 C CB  . ALA B 287 ? 0.59079 0.40146 0.55539 -0.03515 0.06541  0.13139  287 ALA B CB  
4481 N N   . ASP B 288 ? 0.68547 0.44227 0.70736 -0.07287 0.06339  0.11981  288 ASP B N   
4482 C CA  . ASP B 288 ? 0.76840 0.50588 0.81639 -0.09853 0.07144  0.12113  288 ASP B CA  
4483 C C   . ASP B 288 ? 0.79549 0.49873 0.85004 -0.10196 0.06024  0.10670  288 ASP B C   
4484 O O   . ASP B 288 ? 0.83213 0.52919 0.91239 -0.12466 0.05928  0.09601  288 ASP B O   
4485 C CB  . ASP B 288 ? 0.65548 0.43605 0.73591 -0.11716 0.07380  0.11137  288 ASP B CB  
4486 C CG  . ASP B 288 ? 0.62862 0.43877 0.71886 -0.11142 0.05664  0.08727  288 ASP B CG  
4487 O OD1 . ASP B 288 ? 0.58504 0.38584 0.65896 -0.09522 0.04414  0.07775  288 ASP B OD1 
4488 O OD2 . ASP B 288 ? 0.64033 0.48513 0.75551 -0.12263 0.05668  0.07922  288 ASP B OD2 
4489 N N   . SER B 289 ? 0.77526 0.45915 0.80691 -0.07872 0.05127  0.10496  289 SER B N   
4490 C CA  . SER B 289 ? 0.88006 0.52194 0.91033 -0.07660 0.04503  0.09551  289 SER B CA  
4491 C C   . SER B 289 ? 0.97304 0.56327 1.00788 -0.09636 0.05692  0.10546  289 SER B C   
4492 O O   . SER B 289 ? 0.96448 0.53621 1.01594 -0.11324 0.05167  0.08786  289 SER B O   
4493 C CB  . SER B 289 ? 0.86767 0.49591 0.87053 -0.04463 0.03884  0.10086  289 SER B CB  
4494 O OG  . SER B 289 ? 0.79411 0.46177 0.80068 -0.03191 0.02508  0.08356  289 SER B OG  
4495 N N   . PRO B 290 ? 1.13810 0.70099 1.15720 -0.09630 0.07312  0.13278  290 PRO B N   
4496 C CA  . PRO B 290 ? 1.10835 0.62383 1.12712 -0.11400 0.07942  0.13933  290 PRO B CA  
4497 C C   . PRO B 290 ? 1.15842 0.69514 1.21042 -0.15015 0.07687  0.12441  290 PRO B C   
4498 O O   . PRO B 290 ? 1.20896 0.72466 1.26724 -0.16088 0.06477  0.10495  290 PRO B O   
4499 C CB  . PRO B 290 ? 1.10894 0.61196 1.10445 -0.10706 0.09604  0.17182  290 PRO B CB  
4500 C CG  . PRO B 290 ? 1.08122 0.60160 1.05274 -0.07534 0.09679  0.18271  290 PRO B CG  
4501 C CD  . PRO B 290 ? 1.06999 0.65021 1.06438 -0.07810 0.08142  0.15592  290 PRO B CD  
# 
