data_9J1H
# 
_entry.id   9J1H 
# 
_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   9J1H         pdb_00009j1h 10.2210/pdb9j1h/pdb 
WWPDB D_1300049946 ?            ?                   
# 
_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                        9J1H 
_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 0000-0002-7563-0037 
'Wang, J.'   2 0000-0003-2585-5614 
'Yan, W.P.'  3 0000-0002-0210-9734 
# 
_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 'COBALT (II) ION'       58.933    2   ?          ? ? ? 
3 non-polymer syn '2-OXOGLUTARIC ACID'    146.098   2   ?          ? ? ? 
4 non-polymer syn GLYCEROL                92.094    1   ?          ? ? ? 
5 non-polymer syn 'SULFATE ION'           96.063    1   ?          ? ? ? 
6 water       nat water                   18.015    420 ?          ? ? ? 
# 
_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 'COBALT (II) ION'    CO  
3 '2-OXOGLUTARIC ACID' AKG 
4 GLYCEROL             GOL 
5 'SULFATE ION'        SO4 
6 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 
AKG non-polymer         . '2-OXOGLUTARIC ACID'    ?                               'C5 H6 O5'       146.098 
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 
GLN 'L-peptide linking' y GLUTAMINE               ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE               ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE           ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ?                               'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'           ?                               'O4 S -2'        96.063  
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  ?   ?   ?   B . n 
B 1 71  HIS 71  71  ?   ?   ?   B . n 
B 1 72  PHE 72  72  ?   ?   ?   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 ?   ?   ?   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 AKG ? ? AKG ? ? '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 CO  1   401 400 CO  CO  A . 
D 3 AKG 1   402 404 AKG AKG A . 
E 4 GOL 1   403 406 GOL GOL A . 
F 5 SO4 1   501 501 SO4 SO4 B . 
G 2 CO  1   502 400 CO  CO  B . 
H 3 AKG 1   503 404 AKG AKG B . 
I 6 HOH 1   501 386 HOH HOH A . 
I 6 HOH 2   502 34  HOH HOH A . 
I 6 HOH 3   503 420 HOH HOH A . 
I 6 HOH 4   504 117 HOH HOH A . 
I 6 HOH 5   505 52  HOH HOH A . 
I 6 HOH 6   506 176 HOH HOH A . 
I 6 HOH 7   507 333 HOH HOH A . 
I 6 HOH 8   508 102 HOH HOH A . 
I 6 HOH 9   509 46  HOH HOH A . 
I 6 HOH 10  510 44  HOH HOH A . 
I 6 HOH 11  511 96  HOH HOH A . 
I 6 HOH 12  512 152 HOH HOH A . 
I 6 HOH 13  513 30  HOH HOH A . 
I 6 HOH 14  514 366 HOH HOH A . 
I 6 HOH 15  515 363 HOH HOH A . 
I 6 HOH 16  516 104 HOH HOH A . 
I 6 HOH 17  517 260 HOH HOH A . 
I 6 HOH 18  518 202 HOH HOH A . 
I 6 HOH 19  519 127 HOH HOH A . 
I 6 HOH 20  520 2   HOH HOH A . 
I 6 HOH 21  521 256 HOH HOH A . 
I 6 HOH 22  522 239 HOH HOH A . 
I 6 HOH 23  523 403 HOH HOH A . 
I 6 HOH 24  524 45  HOH HOH A . 
I 6 HOH 25  525 264 HOH HOH A . 
I 6 HOH 26  526 11  HOH HOH A . 
I 6 HOH 27  527 73  HOH HOH A . 
I 6 HOH 28  528 399 HOH HOH A . 
I 6 HOH 29  529 348 HOH HOH A . 
I 6 HOH 30  530 336 HOH HOH A . 
I 6 HOH 31  531 114 HOH HOH A . 
I 6 HOH 32  532 115 HOH HOH A . 
I 6 HOH 33  533 32  HOH HOH A . 
I 6 HOH 34  534 268 HOH HOH A . 
I 6 HOH 35  535 120 HOH HOH A . 
I 6 HOH 36  536 83  HOH HOH A . 
I 6 HOH 37  537 312 HOH HOH A . 
I 6 HOH 38  538 413 HOH HOH A . 
I 6 HOH 39  539 233 HOH HOH A . 
I 6 HOH 40  540 19  HOH HOH A . 
I 6 HOH 41  541 210 HOH HOH A . 
I 6 HOH 42  542 188 HOH HOH A . 
I 6 HOH 43  543 356 HOH HOH A . 
I 6 HOH 44  544 3   HOH HOH A . 
I 6 HOH 45  545 28  HOH HOH A . 
I 6 HOH 46  546 107 HOH HOH A . 
I 6 HOH 47  547 307 HOH HOH A . 
I 6 HOH 48  548 374 HOH HOH A . 
I 6 HOH 49  549 116 HOH HOH A . 
I 6 HOH 50  550 308 HOH HOH A . 
I 6 HOH 51  551 382 HOH HOH A . 
I 6 HOH 52  552 355 HOH HOH A . 
I 6 HOH 53  553 290 HOH HOH A . 
I 6 HOH 54  554 251 HOH HOH A . 
I 6 HOH 55  555 141 HOH HOH A . 
I 6 HOH 56  556 109 HOH HOH A . 
I 6 HOH 57  557 119 HOH HOH A . 
I 6 HOH 58  558 55  HOH HOH A . 
I 6 HOH 59  559 171 HOH HOH A . 
I 6 HOH 60  560 320 HOH HOH A . 
I 6 HOH 61  561 319 HOH HOH A . 
I 6 HOH 62  562 4   HOH HOH A . 
I 6 HOH 63  563 237 HOH HOH A . 
I 6 HOH 64  564 112 HOH HOH A . 
I 6 HOH 65  565 108 HOH HOH A . 
I 6 HOH 66  566 50  HOH HOH A . 
I 6 HOH 67  567 88  HOH HOH A . 
I 6 HOH 68  568 225 HOH HOH A . 
I 6 HOH 69  569 398 HOH HOH A . 
I 6 HOH 70  570 118 HOH HOH A . 
I 6 HOH 71  571 354 HOH HOH A . 
I 6 HOH 72  572 384 HOH HOH A . 
I 6 HOH 73  573 318 HOH HOH A . 
I 6 HOH 74  574 48  HOH HOH A . 
I 6 HOH 75  575 138 HOH HOH A . 
I 6 HOH 76  576 122 HOH HOH A . 
I 6 HOH 77  577 376 HOH HOH A . 
I 6 HOH 78  578 77  HOH HOH A . 
I 6 HOH 79  579 367 HOH HOH A . 
I 6 HOH 80  580 103 HOH HOH A . 
I 6 HOH 81  581 95  HOH HOH A . 
I 6 HOH 82  582 379 HOH HOH A . 
I 6 HOH 83  583 27  HOH HOH A . 
I 6 HOH 84  584 38  HOH HOH A . 
I 6 HOH 85  585 238 HOH HOH A . 
I 6 HOH 86  586 69  HOH HOH A . 
I 6 HOH 87  587 41  HOH HOH A . 
I 6 HOH 88  588 241 HOH HOH A . 
I 6 HOH 89  589 351 HOH HOH A . 
I 6 HOH 90  590 12  HOH HOH A . 
I 6 HOH 91  591 8   HOH HOH A . 
I 6 HOH 92  592 7   HOH HOH A . 
I 6 HOH 93  593 31  HOH HOH A . 
I 6 HOH 94  594 406 HOH HOH A . 
I 6 HOH 95  595 168 HOH HOH A . 
I 6 HOH 96  596 266 HOH HOH A . 
I 6 HOH 97  597 26  HOH HOH A . 
I 6 HOH 98  598 25  HOH HOH A . 
I 6 HOH 99  599 6   HOH HOH A . 
I 6 HOH 100 600 282 HOH HOH A . 
I 6 HOH 101 601 347 HOH HOH A . 
I 6 HOH 102 602 409 HOH HOH A . 
I 6 HOH 103 603 371 HOH HOH A . 
I 6 HOH 104 604 332 HOH HOH A . 
I 6 HOH 105 605 58  HOH HOH A . 
I 6 HOH 106 606 72  HOH HOH A . 
I 6 HOH 107 607 42  HOH HOH A . 
I 6 HOH 108 608 305 HOH HOH A . 
I 6 HOH 109 609 67  HOH HOH A . 
I 6 HOH 110 610 234 HOH HOH A . 
I 6 HOH 111 611 184 HOH HOH A . 
I 6 HOH 112 612 49  HOH HOH A . 
I 6 HOH 113 613 231 HOH HOH A . 
I 6 HOH 114 614 144 HOH HOH A . 
I 6 HOH 115 615 35  HOH HOH A . 
I 6 HOH 116 616 223 HOH HOH A . 
I 6 HOH 117 617 212 HOH HOH A . 
I 6 HOH 118 618 56  HOH HOH A . 
I 6 HOH 119 619 313 HOH HOH A . 
I 6 HOH 120 620 229 HOH HOH A . 
I 6 HOH 121 621 163 HOH HOH A . 
I 6 HOH 122 622 60  HOH HOH A . 
I 6 HOH 123 623 133 HOH HOH A . 
I 6 HOH 124 624 408 HOH HOH A . 
I 6 HOH 125 625 331 HOH HOH A . 
I 6 HOH 126 626 227 HOH HOH A . 
I 6 HOH 127 627 416 HOH HOH A . 
I 6 HOH 128 628 353 HOH HOH A . 
I 6 HOH 129 629 68  HOH HOH A . 
I 6 HOH 130 630 213 HOH HOH A . 
I 6 HOH 131 631 259 HOH HOH A . 
I 6 HOH 132 632 196 HOH HOH A . 
I 6 HOH 133 633 209 HOH HOH A . 
I 6 HOH 134 634 387 HOH HOH A . 
I 6 HOH 135 635 417 HOH HOH A . 
I 6 HOH 136 636 314 HOH HOH A . 
I 6 HOH 137 637 244 HOH HOH A . 
I 6 HOH 138 638 158 HOH HOH A . 
I 6 HOH 139 639 195 HOH HOH A . 
I 6 HOH 140 640 177 HOH HOH A . 
I 6 HOH 141 641 190 HOH HOH A . 
I 6 HOH 142 642 222 HOH HOH A . 
I 6 HOH 143 643 301 HOH HOH A . 
I 6 HOH 144 644 359 HOH HOH A . 
I 6 HOH 145 645 101 HOH HOH A . 
I 6 HOH 146 646 142 HOH HOH A . 
I 6 HOH 147 647 57  HOH HOH A . 
I 6 HOH 148 648 283 HOH HOH A . 
I 6 HOH 149 649 179 HOH HOH A . 
I 6 HOH 150 650 373 HOH HOH A . 
I 6 HOH 151 651 110 HOH HOH A . 
I 6 HOH 152 652 224 HOH HOH A . 
I 6 HOH 153 653 352 HOH HOH A . 
I 6 HOH 154 654 300 HOH HOH A . 
I 6 HOH 155 655 325 HOH HOH A . 
I 6 HOH 156 656 235 HOH HOH A . 
I 6 HOH 157 657 230 HOH HOH A . 
I 6 HOH 158 658 343 HOH HOH A . 
I 6 HOH 159 659 199 HOH HOH A . 
I 6 HOH 160 660 381 HOH HOH A . 
I 6 HOH 161 661 279 HOH HOH A . 
I 6 HOH 162 662 322 HOH HOH A . 
I 6 HOH 163 663 167 HOH HOH A . 
I 6 HOH 164 664 84  HOH HOH A . 
I 6 HOH 165 665 414 HOH HOH A . 
I 6 HOH 166 666 124 HOH HOH A . 
I 6 HOH 167 667 277 HOH HOH A . 
I 6 HOH 168 668 339 HOH HOH A . 
I 6 HOH 169 669 270 HOH HOH A . 
I 6 HOH 170 670 375 HOH HOH A . 
I 6 HOH 171 671 147 HOH HOH A . 
I 6 HOH 172 672 161 HOH HOH A . 
I 6 HOH 173 673 326 HOH HOH A . 
I 6 HOH 174 674 276 HOH HOH A . 
I 6 HOH 175 675 295 HOH HOH A . 
I 6 HOH 176 676 76  HOH HOH A . 
I 6 HOH 177 677 178 HOH HOH A . 
I 6 HOH 178 678 153 HOH HOH A . 
I 6 HOH 179 679 208 HOH HOH A . 
I 6 HOH 180 680 383 HOH HOH A . 
I 6 HOH 181 681 149 HOH HOH A . 
I 6 HOH 182 682 78  HOH HOH A . 
I 6 HOH 183 683 342 HOH HOH A . 
I 6 HOH 184 684 389 HOH HOH A . 
I 6 HOH 185 685 294 HOH HOH A . 
I 6 HOH 186 686 89  HOH HOH A . 
I 6 HOH 187 687 105 HOH HOH A . 
I 6 HOH 188 688 402 HOH HOH A . 
I 6 HOH 189 689 338 HOH HOH A . 
I 6 HOH 190 690 180 HOH HOH A . 
I 6 HOH 191 691 368 HOH HOH A . 
I 6 HOH 192 692 183 HOH HOH A . 
I 6 HOH 193 693 186 HOH HOH A . 
I 6 HOH 194 694 123 HOH HOH A . 
I 6 HOH 195 695 247 HOH HOH A . 
I 6 HOH 196 696 302 HOH HOH A . 
I 6 HOH 197 697 273 HOH HOH A . 
I 6 HOH 198 698 397 HOH HOH A . 
I 6 HOH 199 699 206 HOH HOH A . 
I 6 HOH 200 700 165 HOH HOH A . 
I 6 HOH 201 701 200 HOH HOH A . 
I 6 HOH 202 702 385 HOH HOH A . 
I 6 HOH 203 703 341 HOH HOH A . 
I 6 HOH 204 704 253 HOH HOH A . 
I 6 HOH 205 705 380 HOH HOH A . 
I 6 HOH 206 706 236 HOH HOH A . 
I 6 HOH 207 707 261 HOH HOH A . 
I 6 HOH 208 708 140 HOH HOH A . 
I 6 HOH 209 709 169 HOH HOH A . 
I 6 HOH 210 710 192 HOH HOH A . 
I 6 HOH 211 711 150 HOH HOH A . 
I 6 HOH 212 712 87  HOH HOH A . 
I 6 HOH 213 713 293 HOH HOH A . 
I 6 HOH 214 714 211 HOH HOH A . 
I 6 HOH 215 715 254 HOH HOH A . 
I 6 HOH 216 716 201 HOH HOH A . 
I 6 HOH 217 717 280 HOH HOH A . 
I 6 HOH 218 718 263 HOH HOH A . 
I 6 HOH 219 719 306 HOH HOH A . 
I 6 HOH 220 720 404 HOH HOH A . 
I 6 HOH 221 721 392 HOH HOH A . 
I 6 HOH 222 722 365 HOH HOH A . 
I 6 HOH 223 723 143 HOH HOH A . 
I 6 HOH 224 724 267 HOH HOH A . 
I 6 HOH 225 725 198 HOH HOH A . 
I 6 HOH 226 726 310 HOH HOH A . 
I 6 HOH 227 727 297 HOH HOH A . 
I 6 HOH 228 728 291 HOH HOH A . 
I 6 HOH 229 729 296 HOH HOH A . 
J 6 HOH 1   601 216 HOH HOH B . 
J 6 HOH 2   602 309 HOH HOH B . 
J 6 HOH 3   603 75  HOH HOH B . 
J 6 HOH 4   604 269 HOH HOH B . 
J 6 HOH 5   605 337 HOH HOH B . 
J 6 HOH 6   606 21  HOH HOH B . 
J 6 HOH 7   607 10  HOH HOH B . 
J 6 HOH 8   608 344 HOH HOH B . 
J 6 HOH 9   609 54  HOH HOH B . 
J 6 HOH 10  610 126 HOH HOH B . 
J 6 HOH 11  611 93  HOH HOH B . 
J 6 HOH 12  612 250 HOH HOH B . 
J 6 HOH 13  613 62  HOH HOH B . 
J 6 HOH 14  614 185 HOH HOH B . 
J 6 HOH 15  615 65  HOH HOH B . 
J 6 HOH 16  616 125 HOH HOH B . 
J 6 HOH 17  617 419 HOH HOH B . 
J 6 HOH 18  618 9   HOH HOH B . 
J 6 HOH 19  619 175 HOH HOH B . 
J 6 HOH 20  620 372 HOH HOH B . 
J 6 HOH 21  621 33  HOH HOH B . 
J 6 HOH 22  622 162 HOH HOH B . 
J 6 HOH 23  623 29  HOH HOH B . 
J 6 HOH 24  624 316 HOH HOH B . 
J 6 HOH 25  625 79  HOH HOH B . 
J 6 HOH 26  626 418 HOH HOH B . 
J 6 HOH 27  627 401 HOH HOH B . 
J 6 HOH 28  628 405 HOH HOH B . 
J 6 HOH 29  629 220 HOH HOH B . 
J 6 HOH 30  630 17  HOH HOH B . 
J 6 HOH 31  631 40  HOH HOH B . 
J 6 HOH 32  632 346 HOH HOH B . 
J 6 HOH 33  633 189 HOH HOH B . 
J 6 HOH 34  634 47  HOH HOH B . 
J 6 HOH 35  635 146 HOH HOH B . 
J 6 HOH 36  636 98  HOH HOH B . 
J 6 HOH 37  637 335 HOH HOH B . 
J 6 HOH 38  638 51  HOH HOH B . 
J 6 HOH 39  639 207 HOH HOH B . 
J 6 HOH 40  640 36  HOH HOH B . 
J 6 HOH 41  641 63  HOH HOH B . 
J 6 HOH 42  642 59  HOH HOH B . 
J 6 HOH 43  643 82  HOH HOH B . 
J 6 HOH 44  644 134 HOH HOH B . 
J 6 HOH 45  645 412 HOH HOH B . 
J 6 HOH 46  646 53  HOH HOH B . 
J 6 HOH 47  647 173 HOH HOH B . 
J 6 HOH 48  648 362 HOH HOH B . 
J 6 HOH 49  649 151 HOH HOH B . 
J 6 HOH 50  650 74  HOH HOH B . 
J 6 HOH 51  651 194 HOH HOH B . 
J 6 HOH 52  652 410 HOH HOH B . 
J 6 HOH 53  653 70  HOH HOH B . 
J 6 HOH 54  654 131 HOH HOH B . 
J 6 HOH 55  655 378 HOH HOH B . 
J 6 HOH 56  656 205 HOH HOH B . 
J 6 HOH 57  657 317 HOH HOH B . 
J 6 HOH 58  658 90  HOH HOH B . 
J 6 HOH 59  659 121 HOH HOH B . 
J 6 HOH 60  660 80  HOH HOH B . 
J 6 HOH 61  661 154 HOH HOH B . 
J 6 HOH 62  662 155 HOH HOH B . 
J 6 HOH 63  663 288 HOH HOH B . 
J 6 HOH 64  664 15  HOH HOH B . 
J 6 HOH 65  665 255 HOH HOH B . 
J 6 HOH 66  666 85  HOH HOH B . 
J 6 HOH 67  667 100 HOH HOH B . 
J 6 HOH 68  668 257 HOH HOH B . 
J 6 HOH 69  669 258 HOH HOH B . 
J 6 HOH 70  670 97  HOH HOH B . 
J 6 HOH 71  671 1   HOH HOH B . 
J 6 HOH 72  672 157 HOH HOH B . 
J 6 HOH 73  673 203 HOH HOH B . 
J 6 HOH 74  674 160 HOH HOH B . 
J 6 HOH 75  675 5   HOH HOH B . 
J 6 HOH 76  676 43  HOH HOH B . 
J 6 HOH 77  677 156 HOH HOH B . 
J 6 HOH 78  678 334 HOH HOH B . 
J 6 HOH 79  679 358 HOH HOH B . 
J 6 HOH 80  680 369 HOH HOH B . 
J 6 HOH 81  681 18  HOH HOH B . 
J 6 HOH 82  682 284 HOH HOH B . 
J 6 HOH 83  683 37  HOH HOH B . 
J 6 HOH 84  684 39  HOH HOH B . 
J 6 HOH 85  685 311 HOH HOH B . 
J 6 HOH 86  686 248 HOH HOH B . 
J 6 HOH 87  687 20  HOH HOH B . 
J 6 HOH 88  688 193 HOH HOH B . 
J 6 HOH 89  689 132 HOH HOH B . 
J 6 HOH 90  690 61  HOH HOH B . 
J 6 HOH 91  691 327 HOH HOH B . 
J 6 HOH 92  692 99  HOH HOH B . 
J 6 HOH 93  693 249 HOH HOH B . 
J 6 HOH 94  694 135 HOH HOH B . 
J 6 HOH 95  695 13  HOH HOH B . 
J 6 HOH 96  696 221 HOH HOH B . 
J 6 HOH 97  697 170 HOH HOH B . 
J 6 HOH 98  698 23  HOH HOH B . 
J 6 HOH 99  699 148 HOH HOH B . 
J 6 HOH 100 700 242 HOH HOH B . 
J 6 HOH 101 701 304 HOH HOH B . 
J 6 HOH 102 702 22  HOH HOH B . 
J 6 HOH 103 703 14  HOH HOH B . 
J 6 HOH 104 704 240 HOH HOH B . 
J 6 HOH 105 705 272 HOH HOH B . 
J 6 HOH 106 706 81  HOH HOH B . 
J 6 HOH 107 707 64  HOH HOH B . 
J 6 HOH 108 708 16  HOH HOH B . 
J 6 HOH 109 709 285 HOH HOH B . 
J 6 HOH 110 710 245 HOH HOH B . 
J 6 HOH 111 711 91  HOH HOH B . 
J 6 HOH 112 712 214 HOH HOH B . 
J 6 HOH 113 713 92  HOH HOH B . 
J 6 HOH 114 714 271 HOH HOH B . 
J 6 HOH 115 715 299 HOH HOH B . 
J 6 HOH 116 716 94  HOH HOH B . 
J 6 HOH 117 717 71  HOH HOH B . 
J 6 HOH 118 718 328 HOH HOH B . 
J 6 HOH 119 719 281 HOH HOH B . 
J 6 HOH 120 720 130 HOH HOH B . 
J 6 HOH 121 721 361 HOH HOH B . 
J 6 HOH 122 722 66  HOH HOH B . 
J 6 HOH 123 723 86  HOH HOH B . 
J 6 HOH 124 724 287 HOH HOH B . 
J 6 HOH 125 725 24  HOH HOH B . 
J 6 HOH 126 726 226 HOH HOH B . 
J 6 HOH 127 727 323 HOH HOH B . 
J 6 HOH 128 728 215 HOH HOH B . 
J 6 HOH 129 729 136 HOH HOH B . 
J 6 HOH 130 730 324 HOH HOH B . 
J 6 HOH 131 731 292 HOH HOH B . 
J 6 HOH 132 732 218 HOH HOH B . 
J 6 HOH 133 733 166 HOH HOH B . 
J 6 HOH 134 734 172 HOH HOH B . 
J 6 HOH 135 735 191 HOH HOH B . 
J 6 HOH 136 736 360 HOH HOH B . 
J 6 HOH 137 737 289 HOH HOH B . 
J 6 HOH 138 738 217 HOH HOH B . 
J 6 HOH 139 739 159 HOH HOH B . 
J 6 HOH 140 740 111 HOH HOH B . 
J 6 HOH 141 741 128 HOH HOH B . 
J 6 HOH 142 742 286 HOH HOH B . 
J 6 HOH 143 743 252 HOH HOH B . 
J 6 HOH 144 744 395 HOH HOH B . 
J 6 HOH 145 745 321 HOH HOH B . 
J 6 HOH 146 746 391 HOH HOH B . 
J 6 HOH 147 747 139 HOH HOH B . 
J 6 HOH 148 748 303 HOH HOH B . 
J 6 HOH 149 749 370 HOH HOH B . 
J 6 HOH 150 750 394 HOH HOH B . 
J 6 HOH 151 751 415 HOH HOH B . 
J 6 HOH 152 752 275 HOH HOH B . 
J 6 HOH 153 753 174 HOH HOH B . 
J 6 HOH 154 754 411 HOH HOH B . 
J 6 HOH 155 755 350 HOH HOH B . 
J 6 HOH 156 756 228 HOH HOH B . 
J 6 HOH 157 757 329 HOH HOH B . 
J 6 HOH 158 758 278 HOH HOH B . 
J 6 HOH 159 759 164 HOH HOH B . 
J 6 HOH 160 760 187 HOH HOH B . 
J 6 HOH 161 761 393 HOH HOH B . 
J 6 HOH 162 762 129 HOH HOH B . 
J 6 HOH 163 763 232 HOH HOH B . 
J 6 HOH 164 764 407 HOH HOH B . 
J 6 HOH 165 765 298 HOH HOH B . 
J 6 HOH 166 766 137 HOH HOH B . 
J 6 HOH 167 767 219 HOH HOH B . 
J 6 HOH 168 768 246 HOH HOH B . 
J 6 HOH 169 769 345 HOH HOH B . 
J 6 HOH 170 770 388 HOH HOH B . 
J 6 HOH 171 771 340 HOH HOH B . 
J 6 HOH 172 772 145 HOH HOH B . 
J 6 HOH 173 773 357 HOH HOH B . 
J 6 HOH 174 774 349 HOH HOH B . 
J 6 HOH 175 775 390 HOH HOH B . 
J 6 HOH 176 776 377 HOH HOH B . 
J 6 HOH 177 777 315 HOH HOH B . 
J 6 HOH 178 778 262 HOH HOH B . 
J 6 HOH 179 779 421 HOH HOH B . 
J 6 HOH 180 780 181 HOH HOH B . 
J 6 HOH 181 781 113 HOH HOH B . 
J 6 HOH 182 782 204 HOH HOH B . 
J 6 HOH 183 783 396 HOH HOH B . 
J 6 HOH 184 784 197 HOH HOH B . 
J 6 HOH 185 785 364 HOH HOH B . 
J 6 HOH 186 786 182 HOH HOH B . 
J 6 HOH 187 787 400 HOH HOH B . 
J 6 HOH 188 788 274 HOH HOH B . 
J 6 HOH 189 789 243 HOH HOH B . 
J 6 HOH 190 790 106 HOH HOH B . 
J 6 HOH 191 791 265 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                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J1H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.032 
_cell.length_a_esd                 ? 
_cell.length_b                     62.077 
_cell.length_b_esd                 ? 
_cell.length_c                     151.020 
_cell.length_c_esd                 ? 
_cell.volume                       581541.845 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9J1H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J1H 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.58 
_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              6.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;100 mM Bis-Tris pH 6.4
50 mM CoCl2
1.8 M ammonium sulfate
;
_exptl_crystal_grow.pdbx_pH_range   6.0-7.0 
_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         2022-12-11 
_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                          ? 
_reflns.entry_id                                       9J1H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               47.95 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     40043 
_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                           99.04 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.28 
_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                                0.129 
_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                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.118 
_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                                    2.00 
_reflns_shell.d_res_low                                     2.07 
_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                             3641 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.5454 
_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                                  0.846 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.4696 
_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                               31.08 
_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                                 9J1H 
_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                            2.00 
_refine.ls_d_res_low                             47.95 
_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                     40043 
_refine.ls_number_reflns_R_free                  2009 
_refine.ls_number_reflns_R_work                  38034 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.91 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1815 
_refine.ls_R_factor_R_free                       0.1935 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1721 
_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                          44.63 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_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                 21.3399 
_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                            ? 
_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                       2.00 
_refine_hist.d_res_low                        47.95 
_refine_hist.number_atoms_solvent             420 
_refine_hist.number_atoms_total               4919 
_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        4466 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.0070  ? 4599 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9411  ? 6261 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0515  ? 699  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0160  ? 827  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.0789 ? 1757 ? 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' 2.00 2.05  . . 126 2376 84.46 . . . . 0.2648 . . . . . . . . . . . 0.2900 
'X-RAY DIFFRACTION' 2.05 2.10  . . 137 2608 91.57 . . . . 0.2436 . . . . . . . . . . . 0.2919 
'X-RAY DIFFRACTION' 2.10 2.16  . . 141 2674 94.59 . . . . 0.2339 . . . . . . . . . . . 0.2767 
'X-RAY DIFFRACTION' 2.16 2.23  . . 145 2757 95.00 . . . . 0.2290 . . . . . . . . . . . 0.2432 
'X-RAY DIFFRACTION' 2.23 2.31  . . 142 2703 94.98 . . . . 0.2342 . . . . . . . . . . . 0.2774 
'X-RAY DIFFRACTION' 2.31 2.40  . . 143 2710 94.95 . . . . 0.2340 . . . . . . . . . . . 0.2249 
'X-RAY DIFFRACTION' 2.40 2.51  . . 143 2718 94.97 . . . . 0.2221 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 2.51 2.65  . . 142 2711 94.99 . . . . 0.2150 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 2.65 2.81  . . 146 2770 94.96 . . . . 0.2084 . . . . . . . . . . . 0.2434 
'X-RAY DIFFRACTION' 2.81 3.03  . . 144 2728 94.92 . . . . 0.1948 . . . . . . . . . . . 0.2227 
'X-RAY DIFFRACTION' 3.03 3.33  . . 144 2753 95.00 . . . . 0.1657 . . . . . . . . . . . 0.1992 
'X-RAY DIFFRACTION' 3.33 3.82  . . 147 2778 94.91 . . . . 0.1472 . . . . . . . . . . . 0.1653 
'X-RAY DIFFRACTION' 3.82 4.81  . . 148 2815 94.91 . . . . 0.1287 . . . . . . . . . . . 0.1460 
'X-RAY DIFFRACTION' 4.81 47.95 . . 155 2939 94.84 . . . . 0.1618 . . . . . . . . . . . 0.1811 
# 
_struct.entry_id                     9J1H 
_struct.title                        'The binary complex structure of F2Y224-FtmOx1 mutant with alpha-ketoglutarate' 
_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        9J1H 
_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 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
# 
_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 9J1H A 1 ? 291 ? Q4WAW9 1 ? 291 ? 1 291 
2 1 9J1H 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 9J1H LEU A 292 ? UNP Q4WAW9 ? ? 'expression tag' 292 1  
1 9J1H GLU A 293 ? UNP Q4WAW9 ? ? 'expression tag' 293 2  
1 9J1H VAL A 294 ? UNP Q4WAW9 ? ? 'expression tag' 294 3  
1 9J1H ASP A 295 ? UNP Q4WAW9 ? ? 'expression tag' 295 4  
1 9J1H LEU A 296 ? UNP Q4WAW9 ? ? 'expression tag' 296 5  
1 9J1H GLN A 297 ? UNP Q4WAW9 ? ? 'expression tag' 297 6  
1 9J1H GLY A 298 ? UNP Q4WAW9 ? ? 'expression tag' 298 7  
1 9J1H ASP A 299 ? UNP Q4WAW9 ? ? 'expression tag' 299 8  
1 9J1H HIS A 300 ? UNP Q4WAW9 ? ? 'expression tag' 300 9  
1 9J1H GLY A 301 ? UNP Q4WAW9 ? ? 'expression tag' 301 10 
1 9J1H LEU A 302 ? UNP Q4WAW9 ? ? 'expression tag' 302 11 
1 9J1H SER A 303 ? UNP Q4WAW9 ? ? 'expression tag' 303 12 
1 9J1H ALA A 304 ? UNP Q4WAW9 ? ? 'expression tag' 304 13 
1 9J1H TRP A 305 ? UNP Q4WAW9 ? ? 'expression tag' 305 14 
1 9J1H SER A 306 ? UNP Q4WAW9 ? ? 'expression tag' 306 15 
1 9J1H HIS A 307 ? UNP Q4WAW9 ? ? 'expression tag' 307 16 
1 9J1H PRO A 308 ? UNP Q4WAW9 ? ? 'expression tag' 308 17 
1 9J1H GLN A 309 ? UNP Q4WAW9 ? ? 'expression tag' 309 18 
1 9J1H PHE A 310 ? UNP Q4WAW9 ? ? 'expression tag' 310 19 
1 9J1H GLU A 311 ? UNP Q4WAW9 ? ? 'expression tag' 311 20 
1 9J1H LYS A 312 ? UNP Q4WAW9 ? ? 'expression tag' 312 21 
2 9J1H LEU B 292 ? UNP Q4WAW9 ? ? 'expression tag' 292 22 
2 9J1H GLU B 293 ? UNP Q4WAW9 ? ? 'expression tag' 293 23 
2 9J1H VAL B 294 ? UNP Q4WAW9 ? ? 'expression tag' 294 24 
2 9J1H ASP B 295 ? UNP Q4WAW9 ? ? 'expression tag' 295 25 
2 9J1H LEU B 296 ? UNP Q4WAW9 ? ? 'expression tag' 296 26 
2 9J1H GLN B 297 ? UNP Q4WAW9 ? ? 'expression tag' 297 27 
2 9J1H GLY B 298 ? UNP Q4WAW9 ? ? 'expression tag' 298 28 
2 9J1H ASP B 299 ? UNP Q4WAW9 ? ? 'expression tag' 299 29 
2 9J1H HIS B 300 ? UNP Q4WAW9 ? ? 'expression tag' 300 30 
2 9J1H GLY B 301 ? UNP Q4WAW9 ? ? 'expression tag' 301 31 
2 9J1H LEU B 302 ? UNP Q4WAW9 ? ? 'expression tag' 302 32 
2 9J1H SER B 303 ? UNP Q4WAW9 ? ? 'expression tag' 303 33 
2 9J1H ALA B 304 ? UNP Q4WAW9 ? ? 'expression tag' 304 34 
2 9J1H TRP B 305 ? UNP Q4WAW9 ? ? 'expression tag' 305 35 
2 9J1H SER B 306 ? UNP Q4WAW9 ? ? 'expression tag' 306 36 
2 9J1H HIS B 307 ? UNP Q4WAW9 ? ? 'expression tag' 307 37 
2 9J1H PRO B 308 ? UNP Q4WAW9 ? ? 'expression tag' 308 38 
2 9J1H GLN B 309 ? UNP Q4WAW9 ? ? 'expression tag' 309 39 
2 9J1H PHE B 310 ? UNP Q4WAW9 ? ? 'expression tag' 310 40 
2 9J1H GLU B 311 ? UNP Q4WAW9 ? ? 'expression tag' 311 41 
2 9J1H 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)' 6340  ? 
1 MORE         -72   ? 
1 'SSA (A^2)'  22710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   '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  ? CYS A 82  ? ASN A 77  CYS A 82  1 ? 6  
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 ? MET A 247 ? PRO A 240 MET A 247 1 ? 8  
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 ASN B 77  ? THR B 81  ? ASN B 77  THR B 81  5 ? 5  
HELX_P HELX_P16 AB7 CYS B 82  ? THR B 88  ? CYS B 82  THR B 88  1 ? 7  
HELX_P HELX_P17 AB8 VAL B 89  ? ILE B 91  ? VAL B 89  ILE B 91  5 ? 3  
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 ? SER B 246 ? PRO B 240 SER B 246 1 ? 7  
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 ? ? ? ? ? ? ? 1.322 ? ? 
covale2  covale both ? A F2Y 224 C   ? ? ? 1_555 A PHE 225 N  ? ? A F2Y 224 A PHE 225 1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale3  covale both ? B ALA 223 C   ? ? ? 1_555 B F2Y 224 N  ? ? B ALA 223 B F2Y 224 1_555 ? ? ? ? ? ? ? 1.322 ? ? 
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 CO  .   CO ? ? A HIS 129 A CO  401 1_555 ? ? ? ? ? ? ? 1.982 ? ? 
metalc2  metalc ?    ? A ASP 131 OD1 ? ? ? 1_555 C CO  .   CO ? ? A ASP 131 A CO  401 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc3  metalc ?    ? A HIS 205 NE2 ? ? ? 1_555 C CO  .   CO ? ? A HIS 205 A CO  401 1_555 ? ? ? ? ? ? ? 2.692 ? ? 
metalc4  metalc ?    ? C CO  .   CO  ? ? ? 1_555 D AKG .   O5 ? ? A CO  401 A AKG 402 1_555 ? ? ? ? ? ? ? 2.229 ? ? 
metalc5  metalc ?    ? C CO  .   CO  ? ? ? 1_555 D AKG .   O2 ? ? A CO  401 A AKG 402 1_555 ? ? ? ? ? ? ? 1.863 ? ? 
metalc6  metalc ?    ? C CO  .   CO  ? ? ? 1_555 I HOH .   O  ? ? A CO  401 A HOH 503 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc7  metalc ?    ? B HIS 129 NE2 ? ? ? 1_555 G CO  .   CO ? ? B HIS 129 B CO  502 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc8  metalc ?    ? B ASP 131 OD1 ? ? ? 1_555 G CO  .   CO ? ? B ASP 131 B CO  502 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc9  metalc ?    ? B HIS 205 NE2 ? ? ? 1_555 G CO  .   CO ? ? B HIS 205 B CO  502 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc10 metalc ?    ? G CO  .   CO  ? ? ? 1_555 H AKG .   O1 ? ? B CO  502 B AKG 503 1_555 ? ? ? ? ? ? ? 2.679 ? ? 
metalc11 metalc ?    ? G CO  .   CO  ? ? ? 1_555 H AKG .   O5 ? ? B CO  502 B AKG 503 1_555 ? ? ? ? ? ? ? 2.499 ? ? 
metalc12 metalc ?    ? G CO  .   CO  ? ? ? 1_555 J HOH .   O  ? ? B CO  502 B HOH 617 1_555 ? ? ? ? ? ? ? 1.889 ? ? 
# 
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 CO ? C CO . ? A CO 401 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 89.5  ? 
2  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 NE2 ? A HIS 205 ? A HIS 205 ? 1_555 92.1  ? 
3  OD1 ? A ASP 131 ? A ASP 131 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 NE2 ? A HIS 205 ? A HIS 205 ? 1_555 79.5  ? 
4  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O5  ? D AKG .   ? A AKG 402 ? 1_555 107.5 ? 
5  OD1 ? A ASP 131 ? A ASP 131 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O5  ? D AKG .   ? A AKG 402 ? 1_555 160.9 ? 
6  NE2 ? A HIS 205 ? A HIS 205 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O5  ? D AKG .   ? A AKG 402 ? 1_555 91.1  ? 
7  NE2 ? A HIS 129 ? A HIS 129 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O2  ? D AKG .   ? A AKG 402 ? 1_555 88.6  ? 
8  OD1 ? A ASP 131 ? A ASP 131 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O2  ? D AKG .   ? A AKG 402 ? 1_555 108.1 ? 
9  NE2 ? A HIS 205 ? A HIS 205 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O2  ? D AKG .   ? A AKG 402 ? 1_555 172.4 ? 
10 O5  ? D AKG .   ? A AKG 402 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O2  ? D AKG .   ? A AKG 402 ? 1_555 81.5  ? 
11 NE2 ? A HIS 129 ? A HIS 129 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O   ? I HOH .   ? A HOH 503 ? 1_555 173.0 ? 
12 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O   ? I HOH .   ? A HOH 503 ? 1_555 96.0  ? 
13 NE2 ? A HIS 205 ? A HIS 205 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O   ? I HOH .   ? A HOH 503 ? 1_555 84.7  ? 
14 O5  ? D AKG .   ? A AKG 402 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O   ? I HOH .   ? A HOH 503 ? 1_555 66.4  ? 
15 O2  ? D AKG .   ? A AKG 402 ? 1_555 CO ? C CO . ? A CO 401 ? 1_555 O   ? I HOH .   ? A HOH 503 ? 1_555 93.7  ? 
16 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 75.9  ? 
17 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 96.4  ? 
18 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 97.8  ? 
19 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O1  ? H AKG .   ? B AKG 503 ? 1_555 82.1  ? 
20 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O1  ? H AKG .   ? B AKG 503 ? 1_555 100.5 ? 
21 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O1  ? H AKG .   ? B AKG 503 ? 1_555 160.7 ? 
22 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O5  ? H AKG .   ? B AKG 503 ? 1_555 110.5 ? 
23 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O5  ? H AKG .   ? B AKG 503 ? 1_555 162.3 ? 
24 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O5  ? H AKG .   ? B AKG 503 ? 1_555 97.8  ? 
25 O1  ? H AKG .   ? B AKG 503 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O5  ? H AKG .   ? B AKG 503 ? 1_555 65.2  ? 
26 NE2 ? B HIS 129 ? B HIS 129 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O   ? J HOH .   ? B HOH 617 ? 1_555 163.9 ? 
27 OD1 ? B ASP 131 ? B ASP 131 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O   ? J HOH .   ? B HOH 617 ? 1_555 89.3  ? 
28 NE2 ? B HIS 205 ? B HIS 205 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O   ? J HOH .   ? B HOH 617 ? 1_555 91.9  ? 
29 O1  ? H AKG .   ? B AKG 503 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O   ? J HOH .   ? B HOH 617 ? 1_555 94.5  ? 
30 O5  ? H AKG .   ? B AKG 503 ? 1_555 CO ? G CO . ? B CO 502 ? 1_555 O   ? J HOH .   ? B HOH 617 ? 1_555 81.8  ? 
# 
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 12.43 
2 ASP 264 B . ? ASP 264 B PRO 265 B ? PRO 265 B 1 14.46 
# 
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 ? VAL A 199 ? VAL A 196 VAL A 199 
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 ? LEU A 188 ? VAL A 187 LEU A 188 
AA2 2 GLU A 167 ? VAL A 168 ? GLU A 167 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  ? ALA B 13  ? ARG B 11  ALA B 13  
AA4 2 ALA B 30  ? LYS B 34  ? ALA B 30  LYS B 34  
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 ILE A 32  ? O ILE A 32  
AA1 2 3 N PHE A 31  ? N PHE A 31  O ILE A 198 ? O ILE A 198 
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 F2Y A 224 ? O F2Y A 224 N SER A 112 ? N SER A 112 
AA1 6 7 O GLU A 118 ? O GLU A 118 N LYS A 73  ? N LYS A 73  
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 VAL B 152 ? N VAL B 152 O ALA B 223 ? O ALA B 223 
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                   9J1H 
_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 ASN A 77  ? ? 32.96   67.63  
2  1 THR A 88  ? ? -137.07 -55.38 
3  1 ASP A 131 ? ? -81.44  34.33  
4  1 ASP A 132 ? ? -107.21 42.12  
5  1 ALA A 206 ? ? -174.93 149.47 
6  1 LYS B 59  ? ? -78.06  32.89  
7  1 ASN B 77  ? ? 34.01   67.04  
8  1 THR B 88  ? ? -131.88 -59.76 
9  1 ALA B 189 ? ? -112.31 63.67  
10 1 ASN B 210 ? ? -166.71 78.60  
11 1 VAL B 268 ? ? -108.83 -60.06 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 62  ? ? 0.099 'SIDE CHAIN' 
2 1 ARG A 183 ? ? 0.084 'SIDE CHAIN' 
3 1 ARG B 47  ? ? 0.191 'SIDE CHAIN' 
# 
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+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 36.878291173   -11.4470632117 7.79701308199 0.254904095099  ? 0.0564684330329  ? 0.0143235647532  
? 0.12034451513  ? -0.0314411351162  ? 0.324918679768 ? 2.59674850239  ? 0.602113343528   ? 0.480570659541   ? 2.12954597108  ? 
0.0928122193711  ? 1.63886394913  ? -0.0798169552764 ? 0.121543506418   ? -0.162427662791   ? -0.317230553981  ? 0.0381991216015   
? -0.182411707084  ? 0.163938555742   ? 0.0581450321255  ? 0.0432285802929   ? 
2  'X-RAY DIFFRACTION' ? refined 39.8253371756  -1.43451122787 20.6131661057 0.133542866846  ? -0.0320500007727 ? -0.0111108421176 
? 0.16371125712  ? 0.0180066424686   ? 0.334034579055 ? 0.498108964797 ? -0.611061931423  ? -0.593703311148  ? 1.67279659752  ? 
-1.63304218123   ? 6.71564117096  ? 0.0378076644469  ? -0.0803001204851 ? -0.0652506718434  ? 0.0430980889741  ? -0.0287711445982  
? -0.132663012764  ? -0.055806548604  ? 0.163774778316   ? -0.015211615828   ? 
3  'X-RAY DIFFRACTION' ? refined 28.4085774567  -9.9246778057  15.307275557  0.223016105626  ? -0.0196156738479 ? -0.0459355930629 
? 0.140936015324 ? 0.0128652236722   ? 0.369513597655 ? 0.672285332841 ? 0.400713363789   ? -0.14543971392   ? 2.23020822882  ? 
-0.265145069227  ? 0.986772364703 ? 0.0238190931006  ? -0.0864740365391 ? -0.238238940546   ? -0.121777526476  ? 0.0134572327368   
? -0.0290520166878 ? 0.206884230271   ? -0.0099913933888 ? -0.0498480778449  ? 
4  'X-RAY DIFFRACTION' ? refined 23.6146811489  -23.3110521452 21.4303853957 0.495979450761  ? 0.0141700946235  ? -0.0359465136668 
? 0.171679288172 ? 0.0770466960997   ? 0.370687895213 ? 2.56421280759  ? 2.94970713294    ? -0.700656701004  ? 3.64590001242  ? 
-0.550307918016  ? 1.80454417555  ? 0.162482400964   ? -0.44659214227   ? 0.0639632787941   ? 0.239135895755   ? 0.131224495225    
? -0.0871334165324 ? 0.320046748356   ? 0.00127115023304 ? -0.252810023715   ? 
5  'X-RAY DIFFRACTION' ? refined 31.6489422538  -15.1127182699 12.9740897892 0.309861222116  ? 0.019633819123   ? -0.0424671461593 
? 0.123219879065 ? -0.0361264066419  ? 0.393667316037 ? 1.62974384937  ? 0.626321059869   ? -0.0853416646997 ? 2.50076321705  ? 
-0.945672544513  ? 1.63527255279  ? -0.090830889406  ? 0.210490759991   ? -0.00785866403149 ? -0.0122229288505 ? 0.0299202384897   
? -0.352647256878  ? 0.340324478831   ? 0.0934301195638  ? 0.0412997584919   ? 
6  'X-RAY DIFFRACTION' ? refined 32.6658376869  3.17892751975  13.349849299  0.149075241953  ? -0.0367462219662 ? -0.0248905071949 
? 0.132732855771 ? -0.00989091590099 ? 0.271479357438 ? 0.66403739209  ? -0.927640687295  ? -0.0638418052647 ? 2.323106666    ? 
-0.326819230897  ? 1.35207775746  ? 0.123292799658   ? -0.020750807306  ? -0.188544419064   ? -0.169176913685  ? -0.00877647621652 
? -0.0413874879824 ? 0.0728977662086  ? 0.00244112339301 ? -0.111447247668   ? 
7  'X-RAY DIFFRACTION' ? refined 27.815404703   18.678163944   7.91972525649 0.204689964916  ? -0.0117900984138 ? -0.0227015709725 
? 0.135914052733 ? 0.0414651040566   ? 0.340307529757 ? 2.65612252542  ? -0.0473609199751 ? -1.82045790462   ? 2.47453648281  ? 
-0.0452349993302 ? 3.89987901641  ? 0.216337339951   ? 0.017056215355   ? 0.514661800208    ? -0.196027962107  ? -0.110605349041   
? -0.118081159955  ? -0.388958667749  ? 0.0985537867997  ? -0.111778070686   ? 
8  'X-RAY DIFFRACTION' ? refined 3.22783216925  20.4822267127  31.4520576591 0.18662387594   ? 0.0422994538265  ? 0.0512316516706  
? 0.306267346456 ? 0.0144257481338   ? 0.344894000423 ? 3.1608487099   ? 0.54118673193    ? -0.261731416564  ? 1.72399353928  ? 
0.176602662544   ? 1.08080572679  ? 0.0433443572568  ? -0.493320904845  ? 0.193044617822    ? 0.263643284256   ? -0.0148621016145  
? 0.460281729613   ? -0.108318204113  ? -0.224522139267  ? -0.00717175050323 ? 
9  'X-RAY DIFFRACTION' ? refined 15.9703063796  26.494901028   5.87778172001 0.770342204342  ? 0.106894722628   ? -0.135614606567  
? 0.479015554004 ? -0.0809869003674  ? 0.452483082571 ? 0.404709813233 ? -0.0733584359863 ? -0.359185053154  ? 4.67505381857  ? 
2.22536309261    ? 1.31658634758  ? 0.591238885839   ? 0.325829384257   ? 0.527985441415    ? 0.320919366062   ? -0.675489685708   
? 0.332179796904   ? -0.595255481677  ? -0.549413399529  ? 0.0871014433659   ? 
10 'X-RAY DIFFRACTION' ? refined 6.94234803901  28.7981377625  7.41240724281 1.01819828497   ? -0.155047268868  ? 0.460056793129   
? 0.574181125578 ? -0.194189905679   ? 0.62783971975  ? 4.12132416161  ? 1.616866332      ? 1.81349263084    ? 0.662512758197 ? 
0.970510853559   ? 3.16720064289  ? 0.0405713456291  ? 0.816457330972   ? -0.24930662287    ? -0.542953149464  ? -0.0551479501332  
? -0.110036821254  ? 0.104805934127   ? 0.527764827676   ? 0.0451532008543   ? 
11 'X-RAY DIFFRACTION' ? refined 13.9032748571  18.4280758224  26.6147130309 0.0819665410219 ? -0.0105584333345 ? -0.0064189471673 
? 0.203222386905 ? -0.00691891730579 ? 0.265178750331 ? 1.94163714118  ? -0.932542195152  ? -0.0607784178403 ? 2.31386009017  ? 
-0.565569628431  ? 1.94366301312  ? -0.0182687997723 ? -0.251760745917  ? 0.00612376633481  ? 0.0139102019861  ? 0.0843187155816   
? 0.0605119815619  ? -0.0340062890619 ? -0.124424203206  ? -0.0719300695002  ? 
12 'X-RAY DIFFRACTION' ? refined 0.294159289771 12.7730510721  20.2551722431 0.154578934812  ? -0.0228440335711 ? -0.0151043705803 
? 0.287324927354 ? 0.0768112104583   ? 0.408047281316 ? 2.24283336632  ? 0.225256870795   ? 0.107573888874   ? 0.407088994805 ? 
-0.162056230539  ? 0.762571193186 ? 0.0174427408928  ? 0.110982613735   ? -0.085606114808   ? -0.0997193310758 ? 0.0479127761933   
? 0.155208426536   ? 0.00644534598886 ? -0.229998782006  ? -0.0497818831264  ? 
13 'X-RAY DIFFRACTION' ? refined -6.35828517477 32.3410945163  14.3632096554 0.36211358617   ? 0.21431526983    ? 0.122296357388   
? 0.773607911468 ? 0.521068107241    ? 0.984349227409 ? 5.13519575772  ? -3.17103257259   ? 2.2055427951     ? 5.65829022849  ? 
-0.111263281667  ? 2.1904182412   ? -0.0214224170458 ? 0.0959938408609  ? 0.452281501383    ? -0.465364560956  ? -0.408802478832   
? 0.415076904563   ? -0.25464896112   ? -0.157843193773  ? 0.257470208559    ? 
14 'X-RAY DIFFRACTION' ? refined 25.0328046618  14.4489700167  26.6432644765 0.12529134167   ? -0.0182072420765 ? 0.00394396734405 
? 0.20297817801  ? -0.00576006007373 ? 0.263128209487 ? 1.62294204856  ? -0.959552099889  ? 0.351722030656   ? 2.00189094356  ? 
-0.153522119822  ? 0.858111879808 ? -0.0429070434601 ? -0.297636831874  ? 0.0162363758701   ? 0.0295287175851  ? 0.114623987597    
? -0.0407920733184 ? -0.0586109045506 ? 0.049071277361   ? -0.0674519972177  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 6   ? A 53  A 58  ? ? '(chain A and resid 6:58)'    
2  'X-RAY DIFFRACTION' 2  A 54  A 59  ? A 88  A 93  ? ? '(chain A and resid 59:93)'   
3  'X-RAY DIFFRACTION' 3  A 89  A 94  ? A 169 A 174 ? ? '(chain A and resid 94:174)'  
4  'X-RAY DIFFRACTION' 4  A 170 A 175 ? A 183 A 188 ? ? '(chain A and resid 175:188)' 
5  'X-RAY DIFFRACTION' 5  A 184 A 189 ? A 204 A 209 ? ? '(chain A and resid 189:209)' 
6  'X-RAY DIFFRACTION' 6  A 205 A 210 ? A 263 A 268 ? ? '(chain A and resid 210:268)' 
7  'X-RAY DIFFRACTION' 7  A 264 A 269 ? A 284 A 289 ? ? '(chain A and resid 269:289)' 
8  'X-RAY DIFFRACTION' 8  F 1   B 6   ? F 49  B 54  ? ? '(chain B and resid 6:54)'    
9  'X-RAY DIFFRACTION' 9  F 50  B 55  ? F 63  B 68  ? ? '(chain B and resid 55:68)'   
10 'X-RAY DIFFRACTION' 10 F 64  B 69  ? F 65  B 73  ? ? '(chain B and resid 69:73)'   
11 'X-RAY DIFFRACTION' 11 F 66  B 74  ? F 112 B 120 ? ? '(chain B and resid 74:120)'  
12 'X-RAY DIFFRACTION' 12 F 113 B 121 ? F 200 B 208 ? ? '(chain B and resid 121:208)' 
13 'X-RAY DIFFRACTION' 13 F 201 B 209 ? F 208 B 216 ? ? '(chain B and resid 209:216)' 
14 'X-RAY DIFFRACTION' 14 F 209 B 217 ? F 281 B 289 ? ? '(chain B and resid 217:289)' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 725 ? 5.81 . 
2 1 O ? A HOH 726 ? 6.26 . 
3 1 O ? A HOH 727 ? 6.68 . 
4 1 O ? A HOH 728 ? 7.11 . 
5 1 O ? A HOH 729 ? 7.15 . 
6 1 O ? B HOH 790 ? 5.85 . 
7 1 O ? B HOH 791 ? 6.39 . 
# 
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 PRO 70  ? B PRO 70  
35 1 Y 1 B HIS 71  ? B HIS 71  
36 1 Y 1 B PHE 72  ? B PHE 72  
37 1 Y 1 B PRO 290 ? B PRO 290 
38 1 Y 1 B ALA 291 ? B ALA 291 
39 1 Y 1 B LEU 292 ? B LEU 292 
40 1 Y 1 B GLU 293 ? B GLU 293 
41 1 Y 1 B VAL 294 ? B VAL 294 
42 1 Y 1 B ASP 295 ? B ASP 295 
43 1 Y 1 B LEU 296 ? B LEU 296 
44 1 Y 1 B GLN 297 ? B GLN 297 
45 1 Y 1 B GLY 298 ? B GLY 298 
46 1 Y 1 B ASP 299 ? B ASP 299 
47 1 Y 1 B HIS 300 ? B HIS 300 
48 1 Y 1 B GLY 301 ? B GLY 301 
49 1 Y 1 B LEU 302 ? B LEU 302 
50 1 Y 1 B SER 303 ? B SER 303 
51 1 Y 1 B ALA 304 ? B ALA 304 
52 1 Y 1 B TRP 305 ? B TRP 305 
53 1 Y 1 B SER 306 ? B SER 306 
54 1 Y 1 B HIS 307 ? B HIS 307 
55 1 Y 1 B PRO 308 ? B PRO 308 
56 1 Y 1 B GLN 309 ? B GLN 309 
57 1 Y 1 B PHE 310 ? B PHE 310 
58 1 Y 1 B GLU 311 ? B GLU 311 
59 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 
AKG C1   C  N N 1   
AKG O1   O  N N 2   
AKG O2   O  N N 3   
AKG C2   C  N N 4   
AKG O5   O  N N 5   
AKG C3   C  N N 6   
AKG C4   C  N N 7   
AKG C5   C  N N 8   
AKG O3   O  N N 9   
AKG O4   O  N N 10  
AKG HO2  H  N N 11  
AKG H31  H  N N 12  
AKG H32  H  N N 13  
AKG H41  H  N N 14  
AKG H42  H  N N 15  
AKG HO4  H  N N 16  
ALA N    N  N N 17  
ALA CA   C  N S 18  
ALA C    C  N N 19  
ALA O    O  N N 20  
ALA CB   C  N N 21  
ALA OXT  O  N N 22  
ALA H    H  N N 23  
ALA H2   H  N N 24  
ALA HA   H  N N 25  
ALA HB1  H  N N 26  
ALA HB2  H  N N 27  
ALA HB3  H  N N 28  
ALA HXT  H  N N 29  
ARG N    N  N N 30  
ARG CA   C  N S 31  
ARG C    C  N N 32  
ARG O    O  N N 33  
ARG CB   C  N N 34  
ARG CG   C  N N 35  
ARG CD   C  N N 36  
ARG NE   N  N N 37  
ARG CZ   C  N N 38  
ARG NH1  N  N N 39  
ARG NH2  N  N N 40  
ARG OXT  O  N N 41  
ARG H    H  N N 42  
ARG H2   H  N N 43  
ARG HA   H  N N 44  
ARG HB2  H  N N 45  
ARG HB3  H  N N 46  
ARG HG2  H  N N 47  
ARG HG3  H  N N 48  
ARG HD2  H  N N 49  
ARG HD3  H  N N 50  
ARG HE   H  N N 51  
ARG HH11 H  N N 52  
ARG HH12 H  N N 53  
ARG HH21 H  N N 54  
ARG HH22 H  N N 55  
ARG HXT  H  N N 56  
ASN N    N  N N 57  
ASN CA   C  N S 58  
ASN C    C  N N 59  
ASN O    O  N N 60  
ASN CB   C  N N 61  
ASN CG   C  N N 62  
ASN OD1  O  N N 63  
ASN ND2  N  N N 64  
ASN OXT  O  N N 65  
ASN H    H  N N 66  
ASN H2   H  N N 67  
ASN HA   H  N N 68  
ASN HB2  H  N N 69  
ASN HB3  H  N N 70  
ASN HD21 H  N N 71  
ASN HD22 H  N N 72  
ASN HXT  H  N N 73  
ASP N    N  N N 74  
ASP CA   C  N S 75  
ASP C    C  N N 76  
ASP O    O  N N 77  
ASP CB   C  N N 78  
ASP CG   C  N N 79  
ASP OD1  O  N N 80  
ASP OD2  O  N N 81  
ASP OXT  O  N N 82  
ASP H    H  N N 83  
ASP H2   H  N N 84  
ASP HA   H  N N 85  
ASP HB2  H  N N 86  
ASP HB3  H  N N 87  
ASP HD2  H  N N 88  
ASP HXT  H  N N 89  
CO  CO   CO N N 90  
CYS N    N  N N 91  
CYS CA   C  N R 92  
CYS C    C  N N 93  
CYS O    O  N N 94  
CYS CB   C  N N 95  
CYS SG   S  N N 96  
CYS OXT  O  N N 97  
CYS H    H  N N 98  
CYS H2   H  N N 99  
CYS HA   H  N N 100 
CYS HB2  H  N N 101 
CYS HB3  H  N N 102 
CYS HG   H  N N 103 
CYS HXT  H  N N 104 
F2Y OXT  O  N N 105 
F2Y C    C  N N 106 
F2Y O    O  N N 107 
F2Y CA   C  N S 108 
F2Y N    N  N N 109 
F2Y CB   C  N N 110 
F2Y CG   C  Y N 111 
F2Y CD1  C  Y N 112 
F2Y CE1  C  Y N 113 
F2Y F1   F  N N 114 
F2Y CD2  C  Y N 115 
F2Y CE2  C  Y N 116 
F2Y F2   F  N N 117 
F2Y CZ   C  Y N 118 
F2Y OH   O  N N 119 
F2Y HXT  H  N N 120 
F2Y HA   H  N N 121 
F2Y H    H  N N 122 
F2Y H2   H  N N 123 
F2Y H6   H  N N 124 
F2Y H7   H  N N 125 
F2Y H8   H  N N 126 
F2Y H9   H  N N 127 
F2Y H10  H  N N 128 
GLN N    N  N N 129 
GLN CA   C  N S 130 
GLN C    C  N N 131 
GLN O    O  N N 132 
GLN CB   C  N N 133 
GLN CG   C  N N 134 
GLN CD   C  N N 135 
GLN OE1  O  N N 136 
GLN NE2  N  N N 137 
GLN OXT  O  N N 138 
GLN H    H  N N 139 
GLN H2   H  N N 140 
GLN HA   H  N N 141 
GLN HB2  H  N N 142 
GLN HB3  H  N N 143 
GLN HG2  H  N N 144 
GLN HG3  H  N N 145 
GLN HE21 H  N N 146 
GLN HE22 H  N N 147 
GLN HXT  H  N N 148 
GLU N    N  N N 149 
GLU CA   C  N S 150 
GLU C    C  N N 151 
GLU O    O  N N 152 
GLU CB   C  N N 153 
GLU CG   C  N N 154 
GLU CD   C  N N 155 
GLU OE1  O  N N 156 
GLU OE2  O  N N 157 
GLU OXT  O  N N 158 
GLU H    H  N N 159 
GLU H2   H  N N 160 
GLU HA   H  N N 161 
GLU HB2  H  N N 162 
GLU HB3  H  N N 163 
GLU HG2  H  N N 164 
GLU HG3  H  N N 165 
GLU HE2  H  N N 166 
GLU HXT  H  N N 167 
GLY N    N  N N 168 
GLY CA   C  N N 169 
GLY C    C  N N 170 
GLY O    O  N N 171 
GLY OXT  O  N N 172 
GLY H    H  N N 173 
GLY H2   H  N N 174 
GLY HA2  H  N N 175 
GLY HA3  H  N N 176 
GLY HXT  H  N N 177 
GOL C1   C  N N 178 
GOL O1   O  N N 179 
GOL C2   C  N N 180 
GOL O2   O  N N 181 
GOL C3   C  N N 182 
GOL O3   O  N N 183 
GOL H11  H  N N 184 
GOL H12  H  N N 185 
GOL HO1  H  N N 186 
GOL H2   H  N N 187 
GOL HO2  H  N N 188 
GOL H31  H  N N 189 
GOL H32  H  N N 190 
GOL HO3  H  N N 191 
HIS N    N  N N 192 
HIS CA   C  N S 193 
HIS C    C  N N 194 
HIS O    O  N N 195 
HIS CB   C  N N 196 
HIS CG   C  Y N 197 
HIS ND1  N  Y N 198 
HIS CD2  C  Y N 199 
HIS CE1  C  Y N 200 
HIS NE2  N  Y N 201 
HIS OXT  O  N N 202 
HIS H    H  N N 203 
HIS H2   H  N N 204 
HIS HA   H  N N 205 
HIS HB2  H  N N 206 
HIS HB3  H  N N 207 
HIS HD1  H  N N 208 
HIS HD2  H  N N 209 
HIS HE1  H  N N 210 
HIS HE2  H  N N 211 
HIS HXT  H  N N 212 
HOH O    O  N N 213 
HOH H1   H  N N 214 
HOH H2   H  N N 215 
ILE N    N  N N 216 
ILE CA   C  N S 217 
ILE C    C  N N 218 
ILE O    O  N N 219 
ILE CB   C  N S 220 
ILE CG1  C  N N 221 
ILE CG2  C  N N 222 
ILE CD1  C  N N 223 
ILE OXT  O  N N 224 
ILE H    H  N N 225 
ILE H2   H  N N 226 
ILE HA   H  N N 227 
ILE HB   H  N N 228 
ILE HG12 H  N N 229 
ILE HG13 H  N N 230 
ILE HG21 H  N N 231 
ILE HG22 H  N N 232 
ILE HG23 H  N N 233 
ILE HD11 H  N N 234 
ILE HD12 H  N N 235 
ILE HD13 H  N N 236 
ILE HXT  H  N N 237 
LEU N    N  N N 238 
LEU CA   C  N S 239 
LEU C    C  N N 240 
LEU O    O  N N 241 
LEU CB   C  N N 242 
LEU CG   C  N N 243 
LEU CD1  C  N N 244 
LEU CD2  C  N N 245 
LEU OXT  O  N N 246 
LEU H    H  N N 247 
LEU H2   H  N N 248 
LEU HA   H  N N 249 
LEU HB2  H  N N 250 
LEU HB3  H  N N 251 
LEU HG   H  N N 252 
LEU HD11 H  N N 253 
LEU HD12 H  N N 254 
LEU HD13 H  N N 255 
LEU HD21 H  N N 256 
LEU HD22 H  N N 257 
LEU HD23 H  N N 258 
LEU HXT  H  N N 259 
LYS N    N  N N 260 
LYS CA   C  N S 261 
LYS C    C  N N 262 
LYS O    O  N N 263 
LYS CB   C  N N 264 
LYS CG   C  N N 265 
LYS CD   C  N N 266 
LYS CE   C  N N 267 
LYS NZ   N  N N 268 
LYS OXT  O  N N 269 
LYS H    H  N N 270 
LYS H2   H  N N 271 
LYS HA   H  N N 272 
LYS HB2  H  N N 273 
LYS HB3  H  N N 274 
LYS HG2  H  N N 275 
LYS HG3  H  N N 276 
LYS HD2  H  N N 277 
LYS HD3  H  N N 278 
LYS HE2  H  N N 279 
LYS HE3  H  N N 280 
LYS HZ1  H  N N 281 
LYS HZ2  H  N N 282 
LYS HZ3  H  N N 283 
LYS HXT  H  N N 284 
MET N    N  N N 285 
MET CA   C  N S 286 
MET C    C  N N 287 
MET O    O  N N 288 
MET CB   C  N N 289 
MET CG   C  N N 290 
MET SD   S  N N 291 
MET CE   C  N N 292 
MET OXT  O  N N 293 
MET H    H  N N 294 
MET H2   H  N N 295 
MET HA   H  N N 296 
MET HB2  H  N N 297 
MET HB3  H  N N 298 
MET HG2  H  N N 299 
MET HG3  H  N N 300 
MET HE1  H  N N 301 
MET HE2  H  N N 302 
MET HE3  H  N N 303 
MET HXT  H  N N 304 
PHE N    N  N N 305 
PHE CA   C  N S 306 
PHE C    C  N N 307 
PHE O    O  N N 308 
PHE CB   C  N N 309 
PHE CG   C  Y N 310 
PHE CD1  C  Y N 311 
PHE CD2  C  Y N 312 
PHE CE1  C  Y N 313 
PHE CE2  C  Y N 314 
PHE CZ   C  Y N 315 
PHE OXT  O  N N 316 
PHE H    H  N N 317 
PHE H2   H  N N 318 
PHE HA   H  N N 319 
PHE HB2  H  N N 320 
PHE HB3  H  N N 321 
PHE HD1  H  N N 322 
PHE HD2  H  N N 323 
PHE HE1  H  N N 324 
PHE HE2  H  N N 325 
PHE HZ   H  N N 326 
PHE HXT  H  N N 327 
PRO N    N  N N 328 
PRO CA   C  N S 329 
PRO C    C  N N 330 
PRO O    O  N N 331 
PRO CB   C  N N 332 
PRO CG   C  N N 333 
PRO CD   C  N N 334 
PRO OXT  O  N N 335 
PRO H    H  N N 336 
PRO HA   H  N N 337 
PRO HB2  H  N N 338 
PRO HB3  H  N N 339 
PRO HG2  H  N N 340 
PRO HG3  H  N N 341 
PRO HD2  H  N N 342 
PRO HD3  H  N N 343 
PRO HXT  H  N N 344 
SER N    N  N N 345 
SER CA   C  N S 346 
SER C    C  N N 347 
SER O    O  N N 348 
SER CB   C  N N 349 
SER OG   O  N N 350 
SER OXT  O  N N 351 
SER H    H  N N 352 
SER H2   H  N N 353 
SER HA   H  N N 354 
SER HB2  H  N N 355 
SER HB3  H  N N 356 
SER HG   H  N N 357 
SER HXT  H  N N 358 
SO4 S    S  N N 359 
SO4 O1   O  N N 360 
SO4 O2   O  N N 361 
SO4 O3   O  N N 362 
SO4 O4   O  N N 363 
THR N    N  N N 364 
THR CA   C  N S 365 
THR C    C  N N 366 
THR O    O  N N 367 
THR CB   C  N R 368 
THR OG1  O  N N 369 
THR CG2  C  N N 370 
THR OXT  O  N N 371 
THR H    H  N N 372 
THR H2   H  N N 373 
THR HA   H  N N 374 
THR HB   H  N N 375 
THR HG1  H  N N 376 
THR HG21 H  N N 377 
THR HG22 H  N N 378 
THR HG23 H  N N 379 
THR HXT  H  N N 380 
TRP N    N  N N 381 
TRP CA   C  N S 382 
TRP C    C  N N 383 
TRP O    O  N N 384 
TRP CB   C  N N 385 
TRP CG   C  Y N 386 
TRP CD1  C  Y N 387 
TRP CD2  C  Y N 388 
TRP NE1  N  Y N 389 
TRP CE2  C  Y N 390 
TRP CE3  C  Y N 391 
TRP CZ2  C  Y N 392 
TRP CZ3  C  Y N 393 
TRP CH2  C  Y N 394 
TRP OXT  O  N N 395 
TRP H    H  N N 396 
TRP H2   H  N N 397 
TRP HA   H  N N 398 
TRP HB2  H  N N 399 
TRP HB3  H  N N 400 
TRP HD1  H  N N 401 
TRP HE1  H  N N 402 
TRP HE3  H  N N 403 
TRP HZ2  H  N N 404 
TRP HZ3  H  N N 405 
TRP HH2  H  N N 406 
TRP HXT  H  N N 407 
TYR N    N  N N 408 
TYR CA   C  N S 409 
TYR C    C  N N 410 
TYR O    O  N N 411 
TYR CB   C  N N 412 
TYR CG   C  Y N 413 
TYR CD1  C  Y N 414 
TYR CD2  C  Y N 415 
TYR CE1  C  Y N 416 
TYR CE2  C  Y N 417 
TYR CZ   C  Y N 418 
TYR OH   O  N N 419 
TYR OXT  O  N N 420 
TYR H    H  N N 421 
TYR H2   H  N N 422 
TYR HA   H  N N 423 
TYR HB2  H  N N 424 
TYR HB3  H  N N 425 
TYR HD1  H  N N 426 
TYR HD2  H  N N 427 
TYR HE1  H  N N 428 
TYR HE2  H  N N 429 
TYR HH   H  N N 430 
TYR HXT  H  N N 431 
VAL N    N  N N 432 
VAL CA   C  N S 433 
VAL C    C  N N 434 
VAL O    O  N N 435 
VAL CB   C  N N 436 
VAL CG1  C  N N 437 
VAL CG2  C  N N 438 
VAL OXT  O  N N 439 
VAL H    H  N N 440 
VAL H2   H  N N 441 
VAL HA   H  N N 442 
VAL HB   H  N N 443 
VAL HG11 H  N N 444 
VAL HG12 H  N N 445 
VAL HG13 H  N N 446 
VAL HG21 H  N N 447 
VAL HG22 H  N N 448 
VAL HG23 H  N N 449 
VAL HXT  H  N N 450 
# 
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 
AKG C1  O1   doub N N 1   
AKG C1  O2   sing N N 2   
AKG C1  C2   sing N N 3   
AKG O2  HO2  sing N N 4   
AKG C2  O5   doub N N 5   
AKG C2  C3   sing N N 6   
AKG C3  C4   sing N N 7   
AKG C3  H31  sing N N 8   
AKG C3  H32  sing N N 9   
AKG C4  C5   sing N N 10  
AKG C4  H41  sing N N 11  
AKG C4  H42  sing N N 12  
AKG C5  O3   doub N N 13  
AKG C5  O4   sing N N 14  
AKG O4  HO4  sing N N 15  
ALA N   CA   sing N N 16  
ALA N   H    sing N N 17  
ALA N   H2   sing N N 18  
ALA CA  C    sing N N 19  
ALA CA  CB   sing N N 20  
ALA CA  HA   sing N N 21  
ALA C   O    doub N N 22  
ALA C   OXT  sing N N 23  
ALA CB  HB1  sing N N 24  
ALA CB  HB2  sing N N 25  
ALA CB  HB3  sing N N 26  
ALA OXT HXT  sing N N 27  
ARG N   CA   sing N N 28  
ARG N   H    sing N N 29  
ARG N   H2   sing N N 30  
ARG CA  C    sing N N 31  
ARG CA  CB   sing N N 32  
ARG CA  HA   sing N N 33  
ARG C   O    doub N N 34  
ARG C   OXT  sing N N 35  
ARG CB  CG   sing N N 36  
ARG CB  HB2  sing N N 37  
ARG CB  HB3  sing N N 38  
ARG CG  CD   sing N N 39  
ARG CG  HG2  sing N N 40  
ARG CG  HG3  sing N N 41  
ARG CD  NE   sing N N 42  
ARG CD  HD2  sing N N 43  
ARG CD  HD3  sing N N 44  
ARG NE  CZ   sing N N 45  
ARG NE  HE   sing N N 46  
ARG CZ  NH1  sing N N 47  
ARG CZ  NH2  doub N N 48  
ARG NH1 HH11 sing N N 49  
ARG NH1 HH12 sing N N 50  
ARG NH2 HH21 sing N N 51  
ARG NH2 HH22 sing N N 52  
ARG OXT HXT  sing N N 53  
ASN N   CA   sing N N 54  
ASN N   H    sing N N 55  
ASN N   H2   sing N N 56  
ASN CA  C    sing N N 57  
ASN CA  CB   sing N N 58  
ASN CA  HA   sing N N 59  
ASN C   O    doub N N 60  
ASN C   OXT  sing N N 61  
ASN CB  CG   sing N N 62  
ASN CB  HB2  sing N N 63  
ASN CB  HB3  sing N N 64  
ASN CG  OD1  doub N N 65  
ASN CG  ND2  sing N N 66  
ASN ND2 HD21 sing N N 67  
ASN ND2 HD22 sing N N 68  
ASN OXT HXT  sing N N 69  
ASP N   CA   sing N N 70  
ASP N   H    sing N N 71  
ASP N   H2   sing N N 72  
ASP CA  C    sing N N 73  
ASP CA  CB   sing N N 74  
ASP CA  HA   sing N N 75  
ASP C   O    doub N N 76  
ASP C   OXT  sing N N 77  
ASP CB  CG   sing N N 78  
ASP CB  HB2  sing N N 79  
ASP CB  HB3  sing N N 80  
ASP CG  OD1  doub N N 81  
ASP CG  OD2  sing N N 82  
ASP OD2 HD2  sing N N 83  
ASP OXT HXT  sing N N 84  
CYS N   CA   sing N N 85  
CYS N   H    sing N N 86  
CYS N   H2   sing N N 87  
CYS CA  C    sing N N 88  
CYS CA  CB   sing N N 89  
CYS CA  HA   sing N N 90  
CYS C   O    doub N N 91  
CYS C   OXT  sing N N 92  
CYS CB  SG   sing N N 93  
CYS CB  HB2  sing N N 94  
CYS CB  HB3  sing N N 95  
CYS SG  HG   sing N N 96  
CYS OXT HXT  sing N N 97  
F2Y F1  CE1  sing N N 98  
F2Y OH  CZ   sing N N 99  
F2Y CE1 CZ   doub Y N 100 
F2Y CE1 CD1  sing Y N 101 
F2Y CZ  CE2  sing Y N 102 
F2Y CD1 CG   doub Y N 103 
F2Y CE2 F2   sing N N 104 
F2Y CE2 CD2  doub Y N 105 
F2Y N   CA   sing N N 106 
F2Y CG  CD2  sing Y N 107 
F2Y CG  CB   sing N N 108 
F2Y CB  CA   sing N N 109 
F2Y CA  C    sing N N 110 
F2Y O   C    doub N N 111 
F2Y C   OXT  sing N N 112 
F2Y OXT HXT  sing N N 113 
F2Y CA  HA   sing N N 114 
F2Y N   H    sing N N 115 
F2Y N   H2   sing N N 116 
F2Y CB  H6   sing N N 117 
F2Y CB  H7   sing N N 118 
F2Y CD1 H8   sing N N 119 
F2Y CD2 H9   sing N N 120 
F2Y OH  H10  sing N N 121 
GLN N   CA   sing N N 122 
GLN N   H    sing N N 123 
GLN N   H2   sing N N 124 
GLN CA  C    sing N N 125 
GLN CA  CB   sing N N 126 
GLN CA  HA   sing N N 127 
GLN C   O    doub N N 128 
GLN C   OXT  sing N N 129 
GLN CB  CG   sing N N 130 
GLN CB  HB2  sing N N 131 
GLN CB  HB3  sing N N 132 
GLN CG  CD   sing N N 133 
GLN CG  HG2  sing N N 134 
GLN CG  HG3  sing N N 135 
GLN CD  OE1  doub N N 136 
GLN CD  NE2  sing N N 137 
GLN NE2 HE21 sing N N 138 
GLN NE2 HE22 sing N N 139 
GLN OXT HXT  sing N N 140 
GLU N   CA   sing N N 141 
GLU N   H    sing N N 142 
GLU N   H2   sing N N 143 
GLU CA  C    sing N N 144 
GLU CA  CB   sing N N 145 
GLU CA  HA   sing N N 146 
GLU C   O    doub N N 147 
GLU C   OXT  sing N N 148 
GLU CB  CG   sing N N 149 
GLU CB  HB2  sing N N 150 
GLU CB  HB3  sing N N 151 
GLU CG  CD   sing N N 152 
GLU CG  HG2  sing N N 153 
GLU CG  HG3  sing N N 154 
GLU CD  OE1  doub N N 155 
GLU CD  OE2  sing N N 156 
GLU OE2 HE2  sing N N 157 
GLU OXT HXT  sing N N 158 
GLY N   CA   sing N N 159 
GLY N   H    sing N N 160 
GLY N   H2   sing N N 161 
GLY CA  C    sing N N 162 
GLY CA  HA2  sing N N 163 
GLY CA  HA3  sing N N 164 
GLY C   O    doub N N 165 
GLY C   OXT  sing N N 166 
GLY OXT HXT  sing N N 167 
GOL C1  O1   sing N N 168 
GOL C1  C2   sing N N 169 
GOL C1  H11  sing N N 170 
GOL C1  H12  sing N N 171 
GOL O1  HO1  sing N N 172 
GOL C2  O2   sing N N 173 
GOL C2  C3   sing N N 174 
GOL C2  H2   sing N N 175 
GOL O2  HO2  sing N N 176 
GOL C3  O3   sing N N 177 
GOL C3  H31  sing N N 178 
GOL C3  H32  sing N N 179 
GOL O3  HO3  sing N N 180 
HIS N   CA   sing N N 181 
HIS N   H    sing N N 182 
HIS N   H2   sing N N 183 
HIS CA  C    sing N N 184 
HIS CA  CB   sing N N 185 
HIS CA  HA   sing N N 186 
HIS C   O    doub N N 187 
HIS C   OXT  sing N N 188 
HIS CB  CG   sing N N 189 
HIS CB  HB2  sing N N 190 
HIS CB  HB3  sing N N 191 
HIS CG  ND1  sing Y N 192 
HIS CG  CD2  doub Y N 193 
HIS ND1 CE1  doub Y N 194 
HIS ND1 HD1  sing N N 195 
HIS CD2 NE2  sing Y N 196 
HIS CD2 HD2  sing N N 197 
HIS CE1 NE2  sing Y N 198 
HIS CE1 HE1  sing N N 199 
HIS NE2 HE2  sing N N 200 
HIS OXT HXT  sing N N 201 
HOH O   H1   sing N N 202 
HOH O   H2   sing N N 203 
ILE N   CA   sing N N 204 
ILE N   H    sing N N 205 
ILE N   H2   sing N N 206 
ILE CA  C    sing N N 207 
ILE CA  CB   sing N N 208 
ILE CA  HA   sing N N 209 
ILE C   O    doub N N 210 
ILE C   OXT  sing N N 211 
ILE CB  CG1  sing N N 212 
ILE CB  CG2  sing N N 213 
ILE CB  HB   sing N N 214 
ILE CG1 CD1  sing N N 215 
ILE CG1 HG12 sing N N 216 
ILE CG1 HG13 sing N N 217 
ILE CG2 HG21 sing N N 218 
ILE CG2 HG22 sing N N 219 
ILE CG2 HG23 sing N N 220 
ILE CD1 HD11 sing N N 221 
ILE CD1 HD12 sing N N 222 
ILE CD1 HD13 sing N N 223 
ILE OXT HXT  sing N N 224 
LEU N   CA   sing N N 225 
LEU N   H    sing N N 226 
LEU N   H2   sing N N 227 
LEU CA  C    sing N N 228 
LEU CA  CB   sing N N 229 
LEU CA  HA   sing N N 230 
LEU C   O    doub N N 231 
LEU C   OXT  sing N N 232 
LEU CB  CG   sing N N 233 
LEU CB  HB2  sing N N 234 
LEU CB  HB3  sing N N 235 
LEU CG  CD1  sing N N 236 
LEU CG  CD2  sing N N 237 
LEU CG  HG   sing N N 238 
LEU CD1 HD11 sing N N 239 
LEU CD1 HD12 sing N N 240 
LEU CD1 HD13 sing N N 241 
LEU CD2 HD21 sing N N 242 
LEU CD2 HD22 sing N N 243 
LEU CD2 HD23 sing N N 244 
LEU OXT HXT  sing N N 245 
LYS N   CA   sing N N 246 
LYS N   H    sing N N 247 
LYS N   H2   sing N N 248 
LYS CA  C    sing N N 249 
LYS CA  CB   sing N N 250 
LYS CA  HA   sing N N 251 
LYS C   O    doub N N 252 
LYS C   OXT  sing N N 253 
LYS CB  CG   sing N N 254 
LYS CB  HB2  sing N N 255 
LYS CB  HB3  sing N N 256 
LYS CG  CD   sing N N 257 
LYS CG  HG2  sing N N 258 
LYS CG  HG3  sing N N 259 
LYS CD  CE   sing N N 260 
LYS CD  HD2  sing N N 261 
LYS CD  HD3  sing N N 262 
LYS CE  NZ   sing N N 263 
LYS CE  HE2  sing N N 264 
LYS CE  HE3  sing N N 265 
LYS NZ  HZ1  sing N N 266 
LYS NZ  HZ2  sing N N 267 
LYS NZ  HZ3  sing N N 268 
LYS OXT HXT  sing N N 269 
MET N   CA   sing N N 270 
MET N   H    sing N N 271 
MET N   H2   sing N N 272 
MET CA  C    sing N N 273 
MET CA  CB   sing N N 274 
MET CA  HA   sing N N 275 
MET C   O    doub N N 276 
MET C   OXT  sing N N 277 
MET CB  CG   sing N N 278 
MET CB  HB2  sing N N 279 
MET CB  HB3  sing N N 280 
MET CG  SD   sing N N 281 
MET CG  HG2  sing N N 282 
MET CG  HG3  sing N N 283 
MET SD  CE   sing N N 284 
MET CE  HE1  sing N N 285 
MET CE  HE2  sing N N 286 
MET CE  HE3  sing N N 287 
MET OXT HXT  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
SO4 S   O1   doub N N 342 
SO4 S   O2   doub N N 343 
SO4 S   O3   sing N N 344 
SO4 S   O4   sing N N 345 
THR N   CA   sing N N 346 
THR N   H    sing N N 347 
THR N   H2   sing N N 348 
THR CA  C    sing N N 349 
THR CA  CB   sing N N 350 
THR CA  HA   sing N N 351 
THR C   O    doub N N 352 
THR C   OXT  sing N N 353 
THR CB  OG1  sing N N 354 
THR CB  CG2  sing N N 355 
THR CB  HB   sing N N 356 
THR OG1 HG1  sing N N 357 
THR CG2 HG21 sing N N 358 
THR CG2 HG22 sing N N 359 
THR CG2 HG23 sing N N 360 
THR OXT HXT  sing N N 361 
TRP N   CA   sing N N 362 
TRP N   H    sing N N 363 
TRP N   H2   sing N N 364 
TRP CA  C    sing N N 365 
TRP CA  CB   sing N N 366 
TRP CA  HA   sing N N 367 
TRP C   O    doub N N 368 
TRP C   OXT  sing N N 369 
TRP CB  CG   sing N N 370 
TRP CB  HB2  sing N N 371 
TRP CB  HB3  sing N N 372 
TRP CG  CD1  doub Y N 373 
TRP CG  CD2  sing Y N 374 
TRP CD1 NE1  sing Y N 375 
TRP CD1 HD1  sing N N 376 
TRP CD2 CE2  doub Y N 377 
TRP CD2 CE3  sing Y N 378 
TRP NE1 CE2  sing Y N 379 
TRP NE1 HE1  sing N N 380 
TRP CE2 CZ2  sing Y N 381 
TRP CE3 CZ3  doub Y N 382 
TRP CE3 HE3  sing N N 383 
TRP CZ2 CH2  doub Y N 384 
TRP CZ2 HZ2  sing N N 385 
TRP CZ3 CH2  sing Y N 386 
TRP CZ3 HZ3  sing N N 387 
TRP CH2 HH2  sing N N 388 
TRP OXT HXT  sing N N 389 
TYR N   CA   sing N N 390 
TYR N   H    sing N N 391 
TYR N   H2   sing N N 392 
TYR CA  C    sing N N 393 
TYR CA  CB   sing N N 394 
TYR CA  HA   sing N N 395 
TYR C   O    doub N N 396 
TYR C   OXT  sing N N 397 
TYR CB  CG   sing N N 398 
TYR CB  HB2  sing N N 399 
TYR CB  HB3  sing N N 400 
TYR CG  CD1  doub Y N 401 
TYR CG  CD2  sing Y N 402 
TYR CD1 CE1  sing Y N 403 
TYR CD1 HD1  sing N N 404 
TYR CD2 CE2  doub Y N 405 
TYR CD2 HD2  sing N N 406 
TYR CE1 CZ   doub Y N 407 
TYR CE1 HE1  sing N N 408 
TYR CE2 CZ   sing Y N 409 
TYR CE2 HE2  sing N N 410 
TYR CZ  OH   sing N N 411 
TYR OH  HH   sing N N 412 
TYR OXT HXT  sing N N 413 
VAL N   CA   sing N N 414 
VAL N   H    sing N N 415 
VAL N   H2   sing N N 416 
VAL CA  C    sing N N 417 
VAL CA  CB   sing N N 418 
VAL CA  HA   sing N N 419 
VAL C   O    doub N N 420 
VAL C   OXT  sing N N 421 
VAL CB  CG1  sing N N 422 
VAL CB  CG2  sing N N 423 
VAL CB  HB   sing N N 424 
VAL CG1 HG11 sing N N 425 
VAL CG1 HG12 sing N N 426 
VAL CG1 HG13 sing N N 427 
VAL CG2 HG21 sing N N 428 
VAL CG2 HG22 sing N N 429 
VAL CG2 HG23 sing N N 430 
VAL OXT HXT  sing N N 431 
# 
_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   4Y5T 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9J1H 
_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]   0.016121 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016109 
_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]   0.006622 
_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.
;
? 
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   ? 27.16000  -32.88200 10.18900 1.000 43.56103 ? 6   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 6   ? 26.80400  -31.55000 10.69400 1.000 41.62012 ? 6   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 6   ? 27.18200  -30.40400 9.73700  1.000 40.88599 ? 6   LYS A C   1 
ATOM   4    O  O   . LYS A 1 6   ? 28.31500  -30.33600 9.25300  1.000 43.71674 ? 6   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 6   ? 27.46000  -31.31100 12.05400 1.000 40.88202 ? 6   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 6   ? 27.23000  -29.90900 12.57300 1.000 41.82199 ? 6   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 6   ? 27.59400  -29.75700 14.03600 1.000 43.18760 ? 6   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 6   ? 29.07600  -29.96500 14.28100 1.000 43.06952 ? 6   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 6   ? 29.40400  -29.52300 15.65700 1.000 41.26414 ? 6   LYS A NZ  1 
ATOM   10   N  N   . PRO A 1 7   ? 26.23600  -29.50000 9.47300  1.000 38.82973 ? 7   PRO A N   1 
ATOM   11   C  CA  . PRO A 1 7   ? 26.49500  -28.41400 8.51000  1.000 37.18120 ? 7   PRO A CA  1 
ATOM   12   C  C   . PRO A 1 7   ? 27.45100  -27.35300 9.05700  1.000 35.28370 ? 7   PRO A C   1 
ATOM   13   O  O   . PRO A 1 7   ? 27.39000  -26.97800 10.22800 1.000 34.82581 ? 7   PRO A O   1 
ATOM   14   C  CB  . PRO A 1 7   ? 25.09900  -27.82300 8.25700  1.000 36.75803 ? 7   PRO A CB  1 
ATOM   15   C  CG  . PRO A 1 7   ? 24.11900  -28.82500 8.82700  1.000 38.38537 ? 7   PRO A CG  1 
ATOM   16   C  CD  . PRO A 1 7   ? 24.83600  -29.52200 9.93000  1.000 38.02176 ? 7   PRO A CD  1 
ATOM   17   N  N   . GLN A 1 8   ? 28.31700  -26.84500 8.18600  1.000 32.08804 ? 8   GLN A N   1 
ATOM   18   C  CA  . GLN A 1 8   ? 29.34200  -25.87200 8.54700  1.000 31.88445 ? 8   GLN A CA  1 
ATOM   19   C  C   . GLN A 1 8   ? 29.01900  -24.49700 7.96700  1.000 30.76230 ? 8   GLN A C   1 
ATOM   20   O  O   . GLN A 1 8   ? 28.10500  -24.32700 7.15600  1.000 31.89594 ? 8   GLN A O   1 
ATOM   21   C  CB  . GLN A 1 8   ? 30.71900  -26.32100 8.04700  1.000 31.75233 ? 8   GLN A CB  1 
ATOM   22   C  CG  . GLN A 1 8   ? 31.23700  -27.61500 8.63000  1.000 32.33177 ? 8   GLN A CG  1 
ATOM   23   C  CD  . GLN A 1 8   ? 31.69600  -27.46000 10.05200 1.000 32.35488 ? 8   GLN A CD  1 
ATOM   24   O  OE1 . GLN A 1 8   ? 32.63600  -26.71500 10.34500 1.000 31.76964 ? 8   GLN A OE1 1 
ATOM   25   N  NE2 . GLN A 1 8   ? 31.03000  -28.16000 10.95700 1.000 34.80956 ? 8   GLN A NE2 1 
ATOM   26   N  N   . LEU A 1 9   ? 29.80400  -23.50900 8.38300  1.000 30.58140 ? 9   LEU A N   1 
ATOM   27   C  CA  . LEU A 1 9   ? 29.72000  -22.18400 7.78100  1.000 31.08215 ? 9   LEU A CA  1 
ATOM   28   C  C   . LEU A 1 9   ? 30.18800  -22.23700 6.33600  1.000 30.40726 ? 9   LEU A C   1 
ATOM   29   O  O   . LEU A 1 9   ? 31.14400  -22.94400 6.00600  1.000 31.04786 ? 9   LEU A O   1 
ATOM   30   C  CB  . LEU A 1 9   ? 30.57900  -21.18100 8.55100  1.000 28.83923 ? 9   LEU A CB  1 
ATOM   31   C  CG  . LEU A 1 9   ? 30.20700  -20.81200 9.97600  1.000 28.32312 ? 9   LEU A CG  1 
ATOM   32   C  CD1 . LEU A 1 9   ? 31.47700  -20.59800 10.78800 1.000 28.03730 ? 9   LEU A CD1 1 
ATOM   33   C  CD2 . LEU A 1 9   ? 29.36900  -19.56100 9.95600  1.000 27.09048 ? 9   LEU A CD2 1 
ATOM   34   N  N   . GLN A 1 10  ? 29.52900  -21.46300 5.47700  1.000 29.10950 ? 10  GLN A N   1 
ATOM   35   C  CA  . GLN A 1 10  ? 29.86500  -21.43100 4.05800  1.000 29.94380 ? 10  GLN A CA  1 
ATOM   36   C  C   . GLN A 1 10  ? 30.99000  -20.43000 3.82600  1.000 29.78001 ? 10  GLN A C   1 
ATOM   37   O  O   . GLN A 1 10  ? 30.85200  -19.24900 4.15300  1.000 29.94707 ? 10  GLN A O   1 
ATOM   38   C  CB  . GLN A 1 10  ? 28.65100  -21.06500 3.20500  1.000 29.50975 ? 10  GLN A CB  1 
ATOM   39   C  CG  . GLN A 1 10  ? 27.43900  -21.97000 3.40300  1.000 30.08676 ? 10  GLN A CG  1 
ATOM   40   C  CD  . GLN A 1 10  ? 27.71900  -23.41600 3.06300  1.000 29.48450 ? 10  GLN A CD  1 
ATOM   41   O  OE1 . GLN A 1 10  ? 28.41000  -23.71400 2.10000  1.000 29.55839 ? 10  GLN A OE1 1 
ATOM   42   N  NE2 . GLN A 1 10  ? 27.19200  -24.32000 3.86600  1.000 30.68642 ? 10  GLN A NE2 1 
ATOM   43   N  N   . ARG A 1 11  ? 32.10000  -20.90500 3.26900  1.000 29.82552 ? 11  ARG A N   1 
ATOM   44   C  CA  . ARG A 1 11  ? 33.16500  -20.03100 2.79700  1.000 29.83334 ? 11  ARG A CA  1 
ATOM   45   C  C   . ARG A 1 11  ? 32.87900  -19.62200 1.35900  1.000 30.09378 ? 11  ARG A C   1 
ATOM   46   O  O   . ARG A 1 11  ? 32.62500  -20.47200 0.50000  1.000 30.65486 ? 11  ARG A O   1 
ATOM   47   C  CB  . ARG A 1 11  ? 34.52800  -20.71800 2.88500  1.000 29.46482 ? 11  ARG A CB  1 
ATOM   48   C  CG  . ARG A 1 11  ? 35.18300  -20.67100 4.25200  1.000 30.60837 ? 11  ARG A CG  1 
ATOM   49   C  CD  . ARG A 1 11  ? 34.70100  -21.78100 5.15900  1.000 30.43302 ? 11  ARG A CD  1 
ATOM   50   N  NE  . ARG A 1 11  ? 35.54500  -21.90700 6.33900  1.000 30.94478 ? 11  ARG A NE  1 
ATOM   51   C  CZ  . ARG A 1 11  ? 35.19900  -22.56100 7.43700  1.000 30.68067 ? 11  ARG A CZ  1 
ATOM   52   N  NH1 . ARG A 1 11  ? 34.02000  -23.14900 7.54900  1.000 30.19781 ? 11  ARG A NH1 1 
ATOM   53   N  NH2 . ARG A 1 11  ? 36.05500  -22.62700 8.44700  1.000 31.16426 ? 11  ARG A NH2 1 
ATOM   54   N  N   . LEU A 1 12  ? 32.91400  -18.32400 1.09900  1.000 29.86158 ? 12  LEU A N   1 
ATOM   55   C  CA  . LEU A 1 12  ? 32.65100  -17.80100 -0.22900 1.000 30.24041 ? 12  LEU A CA  1 
ATOM   56   C  C   . LEU A 1 12  ? 33.91700  -17.15400 -0.76500 1.000 30.27004 ? 12  LEU A C   1 
ATOM   57   O  O   . LEU A 1 12  ? 34.88100  -16.92800 -0.03100 1.000 31.36085 ? 12  LEU A O   1 
ATOM   58   C  CB  . LEU A 1 12  ? 31.49100  -16.79500 -0.20600 1.000 30.77786 ? 12  LEU A CB  1 
ATOM   59   C  CG  . LEU A 1 12  ? 30.08300  -17.27700 0.16300  1.000 31.02695 ? 12  LEU A CG  1 
ATOM   60   C  CD1 . LEU A 1 12  ? 29.09500  -16.13300 0.27700  1.000 30.73120 ? 12  LEU A CD1 1 
ATOM   61   C  CD2 . LEU A 1 12  ? 29.61100  -18.26500 -0.87400 1.000 32.45513 ? 12  LEU A CD2 1 
ATOM   62   N  N   . ALA A 1 13  ? 33.91200  -16.87200 -2.06200 1.000 33.97036 ? 13  ALA A N   1 
ATOM   63   C  CA  . ALA A 1 13  ? 34.95600  -16.05300 -2.64600 1.000 35.58753 ? 13  ALA A CA  1 
ATOM   64   C  C   . ALA A 1 13  ? 34.69100  -14.59900 -2.30100 1.000 37.75218 ? 13  ALA A C   1 
ATOM   65   O  O   . ALA A 1 13  ? 33.55400  -14.20600 -2.03800 1.000 37.51131 ? 13  ALA A O   1 
ATOM   66   C  CB  . ALA A 1 13  ? 35.00800  -16.23800 -4.15800 1.000 37.66310 ? 13  ALA A CB  1 
ATOM   67   N  N   . ALA A 1 14  ? 35.75600  -13.79900 -2.27200 1.000 37.66211 ? 14  ALA A N   1 
ATOM   68   C  CA  . ALA A 1 14  ? 35.56400  -12.37500 -2.02200 1.000 37.52047 ? 14  ALA A CA  1 
ATOM   69   C  C   . ALA A 1 14  ? 34.70700  -11.74900 -3.11100 1.000 38.54298 ? 14  ALA A C   1 
ATOM   70   O  O   . ALA A 1 14  ? 33.91800  -10.83800 -2.83600 1.000 39.15820 ? 14  ALA A O   1 
ATOM   71   C  CB  . ALA A 1 14  ? 36.91100  -11.65900 -1.91400 1.000 36.64346 ? 14  ALA A CB  1 
ATOM   72   N  N   . ASP A 1 15  ? 34.82000  -12.25100 -4.34400 1.000 37.66714 ? 15  ASP A N   1 
ATOM   73   C  CA  . ASP A 1 15  ? 34.04000  -11.77500 -5.48100 1.000 37.10589 ? 15  ASP A CA  1 
ATOM   74   C  C   . ASP A 1 15  ? 32.64800  -12.39000 -5.55200 1.000 35.03316 ? 15  ASP A C   1 
ATOM   75   O  O   . ASP A 1 15  ? 31.98400  -12.24500 -6.58000 1.000 35.67068 ? 15  ASP A O   1 
ATOM   76   C  CB  . ASP A 1 15  ? 34.80500  -12.02300 -6.79800 1.000 38.29372 ? 15  ASP A CB  1 
ATOM   77   C  CG  . ASP A 1 15  ? 35.06600  -13.51900 -7.10000 1.000 40.90323 ? 15  ASP A CG  1 
ATOM   78   O  OD1 . ASP A 1 15  ? 34.30500  -14.40000 -6.65000 1.000 39.83970 ? 15  ASP A OD1 1 
ATOM   79   O  OD2 . ASP A 1 15  ? 36.04600  -13.82000 -7.82300 1.000 44.49986 ? 15  ASP A OD2 1 
ATOM   80   N  N   . ALA A 1 16  ? 32.19000  -13.06700 -4.50400 1.000 37.19570 ? 16  ALA A N   1 
ATOM   81   C  CA  . ALA A 1 16  ? 30.90700  -13.75200 -4.57200 1.000 37.20690 ? 16  ALA A CA  1 
ATOM   82   C  C   . ALA A 1 16  ? 29.75600  -12.75900 -4.70800 1.000 36.51681 ? 16  ALA A C   1 
ATOM   83   O  O   . ALA A 1 16  ? 29.83300  -11.61000 -4.26300 1.000 35.75835 ? 16  ALA A O   1 
ATOM   84   C  CB  . ALA A 1 16  ? 30.69600  -14.62900 -3.33600 1.000 35.81718 ? 16  ALA A CB  1 
ATOM   85   N  N   . ASP A 1 17  ? 28.69000  -13.21300 -5.36500 1.000 33.65012 ? 17  ASP A N   1 
ATOM   86   C  CA  . ASP A 1 17  ? 27.44600  -12.45900 -5.42600 1.000 33.62873 ? 17  ASP A CA  1 
ATOM   87   C  C   . ASP A 1 17  ? 27.01200  -12.06800 -4.02200 1.000 33.63837 ? 17  ASP A C   1 
ATOM   88   O  O   . ASP A 1 17  ? 27.18200  -12.83500 -3.07400 1.000 35.07268 ? 17  ASP A O   1 
ATOM   89   C  CB  . ASP A 1 17  ? 26.37300  -13.31300 -6.10800 1.000 33.73582 ? 17  ASP A CB  1 
ATOM   90   C  CG  . ASP A 1 17  ? 24.98100  -12.72800 -5.98600 1.000 35.67012 ? 17  ASP A CG  1 
ATOM   91   O  OD1 . ASP A 1 17  ? 24.84900  -11.51600 -5.71400 1.000 35.90063 ? 17  ASP A OD1 1 
ATOM   92   O  OD2 . ASP A 1 17  ? 24.00800  -13.49200 -6.16700 1.000 36.11540 ? 17  ASP A OD2 1 
ATOM   93   N  N   . VAL A 1 18  ? 26.45600  -10.86600 -3.87900 1.000 35.88129 ? 18  VAL A N   1 
ATOM   94   C  CA  . VAL A 1 18  ? 26.07500  -10.45800 -2.53000 1.000 35.95069 ? 18  VAL A CA  1 
ATOM   95   C  C   . VAL A 1 18  ? 24.72100  -11.03900 -2.15000 1.000 34.98092 ? 18  VAL A C   1 
ATOM   96   O  O   . VAL A 1 18  ? 24.45100  -11.24700 -0.96400 1.000 33.28736 ? 18  VAL A O   1 
ATOM   97   C  CB  . VAL A 1 18  ? 26.09700  -8.92800  -2.37700 1.000 34.60843 ? 18  VAL A CB  1 
ATOM   98   C  CG1 . VAL A 1 18  ? 24.96900  -8.29300  -3.15900 1.000 35.76679 ? 18  VAL A CG1 1 
ATOM   99   C  CG2 . VAL A 1 18  ? 26.00400  -8.55400  -0.90300 1.000 31.94941 ? 18  VAL A CG2 1 
ATOM   100  N  N   . ASP A 1 19  ? 23.89600  -11.35500 -3.14300 1.000 34.27603 ? 19  ASP A N   1 
ATOM   101  C  CA  . ASP A 1 19  ? 22.60200  -12.02300 -2.85500 1.000 34.88513 ? 19  ASP A CA  1 
ATOM   102  C  C   . ASP A 1 19  ? 22.93300  -13.33200 -2.13600 1.000 33.86917 ? 19  ASP A C   1 
ATOM   103  O  O   . ASP A 1 19  ? 22.29400  -13.61600 -1.11700 1.000 33.33893 ? 19  ASP A O   1 
ATOM   104  C  CB  . ASP A 1 19  ? 21.78800  -12.15000 -4.13200 1.000 35.81223 ? 19  ASP A CB  1 
ATOM   105  C  CG  . ASP A 1 19  ? 21.80100  -10.93000 -5.03800 1.000 39.04613 ? 19  ASP A CG  1 
ATOM   106  O  OD1 . ASP A 1 19  ? 21.49000  -9.82900  -4.54400 1.000 43.76784 ? 19  ASP A OD1 1 
ATOM   107  O  OD2 . ASP A 1 19  ? 22.10200  -11.09600 -6.23100 1.000 42.51086 ? 19  ASP A OD2 1 
ATOM   108  N  N   . ARG A 1 20  ? 23.89400  -14.08100 -2.66800 1.000 34.73087 ? 20  ARG A N   1 
ATOM   109  C  CA  . ARG A 1 20  ? 24.39100  -15.29000 -2.02700 1.000 34.48944 ? 20  ARG A CA  1 
ATOM   110  C  C   . ARG A 1 20  ? 24.77700  -15.02200 -0.57100 1.000 32.96705 ? 20  ARG A C   1 
ATOM   111  O  O   . ARG A 1 20  ? 24.45400  -15.81100 0.32800  1.000 32.42440 ? 20  ARG A O   1 
ATOM   112  C  CB  . ARG A 1 20  ? 25.56700  -15.81900 -2.85900 1.000 35.37723 ? 20  ARG A CB  1 
ATOM   113  C  CG  . ARG A 1 20  ? 26.32500  -16.99300 -2.28800 1.000 37.15053 ? 20  ARG A CG  1 
ATOM   114  C  CD  . ARG A 1 20  ? 27.32600  -17.56100 -3.29900 1.000 39.28788 ? 20  ARG A CD  1 
ATOM   115  N  NE  . ARG A 1 20  ? 26.66700  -18.23000 -4.41600 1.000 41.14086 ? 20  ARG A NE  1 
ATOM   116  C  CZ  . ARG A 1 20  ? 26.09800  -19.43000 -4.35100 1.000 40.89163 ? 20  ARG A CZ  1 
ATOM   117  N  NH1 . ARG A 1 20  ? 26.06300  -20.12200 -3.22500 1.000 40.13351 ? 20  ARG A NH1 1 
ATOM   118  N  NH2 . ARG A 1 20  ? 25.54900  -19.94900 -5.44500 1.000 41.00946 ? 20  ARG A NH2 1 
ATOM   119  N  N   . MET A 1 21  ? 25.42800  -13.88700 -0.31300 1.000 34.09260 ? 21  MET A N   1 
ATOM   120  C  CA  . MET A 1 21  ? 25.81500  -13.54200 1.04900  1.000 31.19438 ? 21  MET A CA  1 
ATOM   121  C  C   . MET A 1 21  ? 24.59100  -13.27100 1.91200  1.000 31.02826 ? 21  MET A C   1 
ATOM   122  O  O   . MET A 1 21  ? 24.40100  -13.90300 2.95400  1.000 30.40275 ? 21  MET A O   1 
ATOM   123  C  CB  . MET A 1 21  ? 26.76000  -12.34100 1.02300  1.000 31.27375 ? 21  MET A CB  1 
ATOM   124  C  CG  . MET A 1 21  ? 28.05100  -12.63100 0.26300  1.000 31.76817 ? 21  MET A CG  1 
ATOM   125  S  SD  . MET A 1 21  ? 29.18400  -11.25300 0.17000  1.000 29.13469 ? 21  MET A SD  1 
ATOM   126  C  CE  . MET A 1 21  ? 30.31400  -11.84400 -1.06900 1.000 31.70858 ? 21  MET A CE  1 
ATOM   127  N  N   . CYS A 1 22  ? 23.73500  -12.34500 1.48100  1.000 31.92958 ? 22  CYS A N   1 
ATOM   128  C  CA  . CYS A 1 22  ? 22.51100  -12.06400 2.22400  1.000 31.37674 ? 22  CYS A CA  1 
ATOM   129  C  C   . CYS A 1 22  ? 21.69200  -13.32600 2.45300  1.000 32.06833 ? 22  CYS A C   1 
ATOM   130  O  O   . CYS A 1 22  ? 21.07500  -13.49100 3.51100  1.000 32.69809 ? 22  CYS A O   1 
ATOM   131  C  CB  . CYS A 1 22  ? 21.68000  -11.02100 1.47900  1.000 32.35928 ? 22  CYS A CB  1 
ATOM   132  S  SG  . CYS A 1 22  ? 22.38900  -9.37200  1.48900  1.000 35.09065 ? 22  CYS A SG  1 
ATOM   133  N  N   . ARG A 1 23  ? 21.66900  -14.22500 1.46300  1.000 31.91769 ? 23  ARG A N   1 
ATOM   134  C  CA  . ARG A 1 23  ? 20.91000  -15.46700 1.58700  1.000 31.92809 ? 23  ARG A CA  1 
ATOM   135  C  C   . ARG A 1 23  ? 21.40600  -16.29500 2.75900  1.000 30.71033 ? 23  ARG A C   1 
ATOM   136  O  O   . ARG A 1 23  ? 20.61000  -16.81500 3.54500  1.000 30.93503 ? 23  ARG A O   1 
ATOM   137  C  CB  . ARG A 1 23  ? 21.01000  -16.28200 0.29800  1.000 33.71161 ? 23  ARG A CB  1 
ATOM   138  C  CG  . ARG A 1 23  ? 19.84100  -16.14100 -0.65100 1.000 34.41193 ? 23  ARG A CG  1 
ATOM   139  C  CD  . ARG A 1 23  ? 19.87400  -17.24700 -1.69100 1.000 35.83008 ? 23  ARG A CD  1 
ATOM   140  N  NE  . ARG A 1 23  ? 20.99600  -17.11900 -2.61400 1.000 36.84710 ? 23  ARG A NE  1 
ATOM   141  C  CZ  . ARG A 1 23  ? 22.04300  -17.93500 -2.66500 1.000 37.92126 ? 23  ARG A CZ  1 
ATOM   142  N  NH1 . ARG A 1 23  ? 22.18400  -18.94600 -1.81700 1.000 36.59221 ? 23  ARG A NH1 1 
ATOM   143  N  NH2 . ARG A 1 23  ? 22.96000  -17.74800 -3.61000 1.000 38.58932 ? 23  ARG A NH2 1 
ATOM   144  N  N   . LEU A 1 24  ? 22.72800  -16.44200 2.87600  1.000 31.72134 ? 24  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 24  ? 23.29900  -17.23600 3.95700  1.000 30.19885 ? 24  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 24  ? 23.11600  -16.55900 5.31100  1.000 30.58474 ? 24  LEU A C   1 
ATOM   147  O  O   . LEU A 1 24  ? 23.04300  -17.24300 6.33600  1.000 31.02782 ? 24  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 24  ? 24.77800  -17.50600 3.67700  1.000 30.22488 ? 24  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 24  ? 25.08000  -18.25800 2.37000  1.000 31.22002 ? 24  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 24  ? 26.57200  -18.32200 2.05700  1.000 29.35357 ? 24  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 24  ? 24.48900  -19.65000 2.41700  1.000 31.00961 ? 24  LEU A CD2 1 
ATOM   152  N  N   . LEU A 1 25  ? 23.05300  -15.22600 5.34500  1.000 31.18151 ? 25  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 25  ? 22.68300  -14.55300 6.58300  1.000 30.46015 ? 25  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 25  ? 21.22200  -14.77800 6.91900  1.000 30.36638 ? 25  LEU A C   1 
ATOM   155  O  O   . LEU A 1 25  ? 20.85400  -14.71200 8.08900  1.000 31.27406 ? 25  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 25  ? 22.96200  -13.05400 6.49400  1.000 30.33203 ? 25  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 25  ? 24.41800  -12.59100 6.46900  1.000 28.18193 ? 25  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 25  ? 24.50500  -11.07500 6.30100  1.000 26.52821 ? 25  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 25  ? 25.12100  -13.03000 7.72500  1.000 27.35296 ? 25  LEU A CD2 1 
ATOM   160  N  N   . GLU A 1 26  ? 20.38400  -15.05800 5.92400  1.000 30.70604 ? 26  GLU A N   1 
ATOM   161  C  CA  . GLU A 1 26  ? 18.97000  -15.29000 6.19600  1.000 31.28783 ? 26  GLU A CA  1 
ATOM   162  C  C   . GLU A 1 26  ? 18.73800  -16.65500 6.83800  1.000 30.90382 ? 26  GLU A C   1 
ATOM   163  O  O   . GLU A 1 26  ? 18.01700  -16.75600 7.83500  1.000 31.25423 ? 26  GLU A O   1 
ATOM   164  C  CB  . GLU A 1 26  ? 18.15700  -15.15400 4.90700  1.000 32.64484 ? 26  GLU A CB  1 
ATOM   165  C  CG  . GLU A 1 26  ? 17.97200  -13.72400 4.43500  1.000 35.75009 ? 26  GLU A CG  1 
ATOM   166  C  CD  . GLU A 1 26  ? 16.87200  -12.97900 5.18700  1.000 41.09401 ? 26  GLU A CD  1 
ATOM   167  O  OE1 . GLU A 1 26  ? 16.09200  -13.63000 5.92400  1.000 42.10235 ? 26  GLU A OE1 1 
ATOM   168  O  OE2 . GLU A 1 26  ? 16.78700  -11.73600 5.03000  1.000 41.92814 ? 26  GLU A OE2 1 
ATOM   169  N  N   . GLU A 1 27  ? 19.33100  -17.72200 6.28300  1.000 31.61285 ? 27  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 27  ? 19.08800  -19.07200 6.79700  1.000 33.94104 ? 27  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 27  ? 20.14700  -19.54900 7.78100  1.000 33.36561 ? 27  GLU A C   1 
ATOM   172  O  O   . GLU A 1 27  ? 19.80700  -20.14600 8.80600  1.000 34.95735 ? 27  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 27  ? 18.98300  -20.11600 5.67400  1.000 36.60569 ? 27  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 27  ? 18.74600  -21.53500 6.25900  1.000 40.39504 ? 27  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 27  ? 18.53100  -22.61700 5.22700  1.000 46.22538 ? 27  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 27  ? 19.48000  -22.93700 4.47600  1.000 45.89549 ? 27  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 27  ? 17.40700  -23.15900 5.18200  1.000 49.94102 ? 27  GLU A OE2 1 
ATOM   178  N  N   . ASP A 1 28  ? 21.42400  -19.35400 7.47300  1.000 31.65715 ? 28  ASP A N   1 
ATOM   179  C  CA  . ASP A 1 28  ? 22.45100  -19.82400 8.38500  1.000 30.39231 ? 28  ASP A CA  1 
ATOM   180  C  C   . ASP A 1 28  ? 22.80500  -18.78500 9.42800  1.000 28.93426 ? 28  ASP A C   1 
ATOM   181  O  O   . ASP A 1 28  ? 23.20200  -19.15000 10.53500 1.000 29.30207 ? 28  ASP A O   1 
ATOM   182  C  CB  . ASP A 1 28  ? 23.69400  -20.25500 7.60900  1.000 30.95799 ? 28  ASP A CB  1 
ATOM   183  C  CG  . ASP A 1 28  ? 23.51100  -21.60700 6.92400  1.000 34.31867 ? 28  ASP A CG  1 
ATOM   184  O  OD1 . ASP A 1 28  ? 22.37900  -22.14200 6.96200  1.000 34.90654 ? 28  ASP A OD1 1 
ATOM   185  O  OD2 . ASP A 1 28  ? 24.49400  -22.13600 6.35800  1.000 33.57260 ? 28  ASP A OD2 1 
ATOM   186  N  N   . GLY A 1 29  ? 22.62300  -17.50500 9.11600  1.000 29.49517 ? 29  GLY A N   1 
ATOM   187  C  CA  . GLY A 1 29  ? 22.93800  -16.43600 10.02800 1.000 28.26018 ? 29  GLY A CA  1 
ATOM   188  C  C   . GLY A 1 29  ? 24.36700  -15.95500 9.97600  1.000 26.16143 ? 29  GLY A C   1 
ATOM   189  O  O   . GLY A 1 29  ? 24.68700  -14.95500 10.62300 1.000 25.35465 ? 29  GLY A O   1 
ATOM   190  N  N   . ALA A 1 30  ? 25.23400  -16.62400 9.22600  1.000 27.41883 ? 30  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 30  ? 26.63800  -16.25200 9.16600  1.000 25.88262 ? 30  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 30  ? 27.27300  -16.90400 7.95100  1.000 26.34632 ? 30  ALA A C   1 
ATOM   193  O  O   . ALA A 1 30  ? 26.72000  -17.83500 7.36300  1.000 26.56033 ? 30  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 30  ? 27.38600  -16.66200 10.43800 1.000 25.07370 ? 30  ALA A CB  1 
ATOM   195  N  N   . PHE A 1 31  ? 28.44800  -16.40300 7.58500  1.000 26.52958 ? 31  PHE A N   1 
ATOM   196  C  CA  . PHE A 1 31  ? 29.25600  -17.00800 6.53500  1.000 26.18108 ? 31  PHE A CA  1 
ATOM   197  C  C   . PHE A 1 31  ? 30.64200  -16.38100 6.59500  1.000 27.43329 ? 31  PHE A C   1 
ATOM   198  O  O   . PHE A 1 31  ? 30.87200  -15.39100 7.29600  1.000 26.84508 ? 31  PHE A O   1 
ATOM   199  C  CB  . PHE A 1 31  ? 28.63500  -16.81900 5.15100  1.000 26.74842 ? 31  PHE A CB  1 
ATOM   200  C  CG  . PHE A 1 31  ? 28.55800  -15.38900 4.72400  1.000 26.67691 ? 31  PHE A CG  1 
ATOM   201  C  CD1 . PHE A 1 31  ? 27.50000  -14.59400 5.11300  1.000 26.10945 ? 31  PHE A CD1 1 
ATOM   202  C  CD2 . PHE A 1 31  ? 29.54700  -14.83800 3.93900  1.000 27.75600 ? 31  PHE A CD2 1 
ATOM   203  C  CE1 . PHE A 1 31  ? 27.43500  -13.27900 4.73000  1.000 26.32925 ? 31  PHE A CE1 1 
ATOM   204  C  CE2 . PHE A 1 31  ? 29.48400  -13.52100 3.55700  1.000 28.01767 ? 31  PHE A CE2 1 
ATOM   205  C  CZ  . PHE A 1 31  ? 28.42800  -12.74100 3.95600  1.000 26.54808 ? 31  PHE A CZ  1 
ATOM   206  N  N   . ILE A 1 32  ? 31.55900  -16.96600 5.83100  1.000 28.07271 ? 32  ILE A N   1 
ATOM   207  C  CA  . ILE A 1 32  ? 32.94500  -16.52800 5.76600  1.000 28.93777 ? 32  ILE A CA  1 
ATOM   208  C  C   . ILE A 1 32  ? 33.25500  -16.10700 4.34100  1.000 29.38489 ? 32  ILE A C   1 
ATOM   209  O  O   . ILE A 1 32  ? 32.84100  -16.77100 3.38700  1.000 29.39854 ? 32  ILE A O   1 
ATOM   210  C  CB  . ILE A 1 32  ? 33.90800  -17.64000 6.23100  1.000 28.81040 ? 32  ILE A CB  1 
ATOM   211  C  CG1 . ILE A 1 32  ? 33.79300  -17.83100 7.74300  1.000 27.74882 ? 32  ILE A CG1 1 
ATOM   212  C  CG2 . ILE A 1 32  ? 35.33200  -17.32600 5.81900  1.000 29.92734 ? 32  ILE A CG2 1 
ATOM   213  C  CD1 . ILE A 1 32  ? 34.44500  -19.06000 8.26000  1.000 28.08842 ? 32  ILE A CD1 1 
ATOM   214  N  N   . LEU A 1 33  ? 33.95500  -14.98500 4.20100  1.000 29.07944 ? 33  LEU A N   1 
ATOM   215  C  CA  . LEU A 1 33  ? 34.59600  -14.61500 2.94900  1.000 29.06568 ? 33  LEU A CA  1 
ATOM   216  C  C   . LEU A 1 33  ? 36.06200  -15.01300 3.02100  1.000 30.02184 ? 33  LEU A C   1 
ATOM   217  O  O   . LEU A 1 33  ? 36.71900  -14.79200 4.04000  1.000 30.34256 ? 33  LEU A O   1 
ATOM   218  C  CB  . LEU A 1 33  ? 34.46100  -13.11900 2.67900  1.000 30.76834 ? 33  LEU A CB  1 
ATOM   219  C  CG  . LEU A 1 33  ? 33.06600  -12.64400 2.28400  1.000 30.30905 ? 33  LEU A CG  1 
ATOM   220  C  CD1 . LEU A 1 33  ? 33.14900  -11.27100 1.67000  1.000 30.44876 ? 33  LEU A CD1 1 
ATOM   221  C  CD2 . LEU A 1 33  ? 32.44100  -13.61700 1.30400  1.000 30.39741 ? 33  LEU A CD2 1 
ATOM   222  N  N   . LYS A 1 34  ? 36.56700  -15.61600 1.95200  1.000 31.93308 ? 34  LYS A N   1 
ATOM   223  C  CA  . LYS A 1 34  ? 37.96000  -16.02700 1.90000  1.000 32.02661 ? 34  LYS A CA  1 
ATOM   224  C  C   . LYS A 1 34  ? 38.78900  -14.94200 1.22800  1.000 33.39644 ? 34  LYS A C   1 
ATOM   225  O  O   . LYS A 1 34  ? 38.45000  -14.48400 0.13300  1.000 34.45680 ? 34  LYS A O   1 
ATOM   226  C  CB  . LYS A 1 34  ? 38.11200  -17.35100 1.15100  1.000 31.26736 ? 34  LYS A CB  1 
ATOM   227  C  CG  . LYS A 1 34  ? 37.45100  -18.53100 1.83600  1.000 30.99556 ? 34  LYS A CG  1 
ATOM   228  C  CD  . LYS A 1 34  ? 37.95900  -18.72600 3.26000  1.000 31.76338 ? 34  LYS A CD  1 
ATOM   229  C  CE  . LYS A 1 34  ? 39.32200  -19.39800 3.30500  1.000 35.31417 ? 34  LYS A CE  1 
ATOM   230  N  NZ  . LYS A 1 34  ? 39.70100  -19.80800 4.68800  1.000 36.45317 ? 34  LYS A NZ  1 
ATOM   231  N  N   . GLY A 1 35  ? 39.86000  -14.52300 1.89400  1.000 31.85312 ? 35  GLY A N   1 
ATOM   232  C  CA  . GLY A 1 35  ? 40.83300  -13.63300 1.27500  1.000 31.08923 ? 35  GLY A CA  1 
ATOM   233  C  C   . GLY A 1 35  ? 40.30200  -12.26800 0.89500  1.000 31.65194 ? 35  GLY A C   1 
ATOM   234  O  O   . GLY A 1 35  ? 40.67600  -11.72600 -0.15500 1.000 30.38283 ? 35  GLY A O   1 
ATOM   235  N  N   . LEU A 1 36  ? 39.43100  -11.69800 1.72700  1.000 31.85721 ? 36  LEU A N   1 
ATOM   236  C  CA  . LEU A 1 36  ? 38.97900  -10.33000 1.50700  1.000 31.92987 ? 36  LEU A CA  1 
ATOM   237  C  C   . LEU A 1 36  ? 40.14700  -9.35400  1.55000  1.000 31.12744 ? 36  LEU A C   1 
ATOM   238  O  O   . LEU A 1 36  ? 40.43300  -8.65800  0.57000  1.000 30.50354 ? 36  LEU A O   1 
ATOM   239  C  CB  . LEU A 1 36  ? 37.93600  -9.95600  2.55400  1.000 30.53639 ? 36  LEU A CB  1 
ATOM   240  C  CG  . LEU A 1 36  ? 37.46300  -8.52000  2.41700  1.000 28.76395 ? 36  LEU A CG  1 
ATOM   241  C  CD1 . LEU A 1 36  ? 36.90300  -8.32200  1.02500  1.000 30.57310 ? 36  LEU A CD1 1 
ATOM   242  C  CD2 . LEU A 1 36  ? 36.42900  -8.23000  3.44400  1.000 27.44785 ? 36  LEU A CD2 1 
ATOM   243  N  N   . LEU A 1 37  ? 40.82600  -9.28900  2.68100  1.000 29.77582 ? 37  LEU A N   1 
ATOM   244  C  CA  . LEU A 1 37  ? 41.91600  -8.34700  2.85700  1.000 30.55777 ? 37  LEU A CA  1 
ATOM   245  C  C   . LEU A 1 37  ? 43.22300  -8.94200  2.34600  1.000 32.33802 ? 37  LEU A C   1 
ATOM   246  O  O   . LEU A 1 37  ? 43.48900  -10.13200 2.55500  1.000 32.71064 ? 37  LEU A O   1 
ATOM   247  C  CB  . LEU A 1 37  ? 42.07700  -7.98300  4.32400  1.000 29.75797 ? 37  LEU A CB  1 
ATOM   248  C  CG  . LEU A 1 37  ? 40.85300  -7.36100  4.97000  1.000 28.64444 ? 37  LEU A CG  1 
ATOM   249  C  CD1 . LEU A 1 37  ? 41.16600  -7.20200  6.42700  1.000 26.20274 ? 37  LEU A CD1 1 
ATOM   250  C  CD2 . LEU A 1 37  ? 40.50500  -6.01400  4.33000  1.000 26.34000 ? 37  LEU A CD2 1 
ATOM   251  N  N   . PRO A 1 38  ? 44.04600  -8.12700  1.69000  1.000 31.72407 ? 38  PRO A N   1 
ATOM   252  C  CA  . PRO A 1 38  ? 45.38400  -8.58000  1.29300  1.000 33.12935 ? 38  PRO A CA  1 
ATOM   253  C  C   . PRO A 1 38  ? 46.22800  -8.88800  2.51900  1.000 33.90058 ? 38  PRO A C   1 
ATOM   254  O  O   . PRO A 1 38  ? 45.88500  -8.53000  3.64600  1.000 34.75029 ? 38  PRO A O   1 
ATOM   255  C  CB  . PRO A 1 38  ? 45.94400  -7.38600  0.51000  1.000 32.79910 ? 38  PRO A CB  1 
ATOM   256  C  CG  . PRO A 1 38  ? 44.75300  -6.54400  0.17000  1.000 31.37556 ? 38  PRO A CG  1 
ATOM   257  C  CD  . PRO A 1 38  ? 43.78100  -6.74400  1.27400  1.000 29.89454 ? 38  PRO A CD  1 
ATOM   258  N  N   . PHE A 1 39  ? 47.35900  -9.56500  2.30100  1.000 33.21249 ? 39  PHE A N   1 
ATOM   259  C  CA  . PHE A 1 39  ? 48.24400  -9.80000  3.43600  1.000 34.47658 ? 39  PHE A CA  1 
ATOM   260  C  C   . PHE A 1 39  ? 48.95000  -8.52200  3.86200  1.000 35.29572 ? 39  PHE A C   1 
ATOM   261  O  O   . PHE A 1 39  ? 49.21400  -8.33800  5.05400  1.000 35.10861 ? 39  PHE A O   1 
ATOM   262  C  CB  . PHE A 1 39  ? 49.27500  -10.88500 3.13500  1.000 35.56320 ? 39  PHE A CB  1 
ATOM   263  C  CG  . PHE A 1 39  ? 50.22500  -11.12900 4.27800  1.000 36.80398 ? 39  PHE A CG  1 
ATOM   264  C  CD1 . PHE A 1 39  ? 49.87000  -11.96100 5.32600  1.000 37.83523 ? 39  PHE A CD1 1 
ATOM   265  C  CD2 . PHE A 1 39  ? 51.45300  -10.49500 4.32700  1.000 38.17936 ? 39  PHE A CD2 1 
ATOM   266  C  CE1 . PHE A 1 39  ? 50.72600  -12.16900 6.38700  1.000 37.09874 ? 39  PHE A CE1 1 
ATOM   267  C  CE2 . PHE A 1 39  ? 52.31100  -10.70000 5.38800  1.000 38.76467 ? 39  PHE A CE2 1 
ATOM   268  C  CZ  . PHE A 1 39  ? 51.94200  -11.53300 6.41900  1.000 38.42054 ? 39  PHE A CZ  1 
ATOM   269  N  N   . ASP A 1 40  ? 49.25000  -7.63000  2.91400  1.000 34.71450 ? 40  ASP A N   1 
ATOM   270  C  CA  . ASP A 1 40  ? 49.92300  -6.34000  3.25000  1.000 34.50495 ? 40  ASP A CA  1 
ATOM   271  C  C   . ASP A 1 40  ? 49.00300  -5.49400  4.13500  1.000 33.86732 ? 40  ASP A C   1 
ATOM   272  O  O   . ASP A 1 40  ? 49.51700  -4.78600  5.00500  1.000 33.61741 ? 40  ASP A O   1 
ATOM   273  C  CB  . ASP A 1 40  ? 50.38400  -5.55800  2.03300  1.000 36.00203 ? 40  ASP A CB  1 
ATOM   274  C  CG  . ASP A 1 40  ? 49.32900  -4.75800  1.28500  1.000 37.17234 ? 40  ASP A CG  1 
ATOM   275  O  OD1 . ASP A 1 40  ? 48.37600  -5.37200  0.78600  1.000 38.69318 ? 40  ASP A OD1 1 
ATOM   276  O  OD2 . ASP A 1 40  ? 49.48400  -3.52600  1.19300  1.000 37.59003 ? 40  ASP A OD2 1 
ATOM   277  N  N   . VAL A 1 41  ? 47.69000  -5.61000  3.93400  1.000 35.75493 ? 41  VAL A N   1 
ATOM   278  C  CA  . VAL A 1 41  ? 46.76000  -4.88100  4.78800  1.000 34.38381 ? 41  VAL A CA  1 
ATOM   279  C  C   . VAL A 1 41  ? 46.74200  -5.48200  6.19100  1.000 34.23537 ? 41  VAL A C   1 
ATOM   280  O  O   . VAL A 1 41  ? 46.69000  -4.75300  7.19400  1.000 33.15351 ? 41  VAL A O   1 
ATOM   281  C  CB  . VAL A 1 41  ? 45.36300  -4.85800  4.13600  1.000 32.61117 ? 41  VAL A CB  1 
ATOM   282  C  CG1 . VAL A 1 41  ? 44.30700  -4.35500  5.10000  1.000 31.30435 ? 41  VAL A CG1 1 
ATOM   283  C  CG2 . VAL A 1 41  ? 45.38700  -3.97600  2.89700  1.000 33.03960 ? 41  VAL A CG2 1 
ATOM   284  N  N   . VAL A 1 42  ? 46.82200  -6.81800  6.28500  1.000 32.46787 ? 42  VAL A N   1 
ATOM   285  C  CA  . VAL A 1 42  ? 46.79900  -7.50500  7.57800  1.000 31.59999 ? 42  VAL A CA  1 
ATOM   286  C  C   . VAL A 1 42  ? 48.05000  -7.18900  8.38900  1.000 30.77091 ? 42  VAL A C   1 
ATOM   287  O  O   . VAL A 1 42  ? 47.97200  -6.90600  9.58700  1.000 30.35800 ? 42  VAL A O   1 
ATOM   288  C  CB  . VAL A 1 42  ? 46.63800  -9.02500  7.38500  1.000 31.93019 ? 42  VAL A CB  1 
ATOM   289  C  CG1 . VAL A 1 42  ? 46.73400  -9.74300  8.72600  1.000 32.00038 ? 42  VAL A CG1 1 
ATOM   290  C  CG2 . VAL A 1 42  ? 45.31700  -9.35700  6.69200  1.000 30.85355 ? 42  VAL A CG2 1 
ATOM   291  N  N   . GLU A 1 43  ? 49.22100  -7.23200  7.76100  1.000 31.87865 ? 43  GLU A N   1 
ATOM   292  C  CA  . GLU A 1 43  ? 50.45400  -7.13200  8.53300  1.000 32.33453 ? 43  GLU A CA  1 
ATOM   293  C  C   . GLU A 1 43  ? 50.64600  -5.73400  9.13000  1.000 30.19581 ? 43  GLU A C   1 
ATOM   294  O  O   . GLU A 1 43  ? 51.12700  -5.60400  10.25700 1.000 29.99100 ? 43  GLU A O   1 
ATOM   295  C  CB  . GLU A 1 43  ? 51.64200  -7.54300  7.66100  1.000 35.92032 ? 43  GLU A CB  1 
ATOM   296  C  CG  . GLU A 1 43  ? 52.64400  -8.47500  8.36500  1.000 38.68648 ? 43  GLU A CG  1 
ATOM   297  C  CD  . GLU A 1 43  ? 53.87400  -8.78100  7.51500  1.000 41.02388 ? 43  GLU A CD  1 
ATOM   298  O  OE1 . GLU A 1 43  ? 54.06800  -8.10400  6.48100  1.000 39.72550 ? 43  GLU A OE1 1 
ATOM   299  O  OE2 . GLU A 1 43  ? 54.63600  -9.70700  7.88100  1.000 42.76323 ? 43  GLU A OE2 1 
ATOM   300  N  N   . SER A 1 44  ? 50.27000  -4.67400  8.41300  1.000 30.45429 ? 44  SER A N   1 
ATOM   301  C  CA  . SER A 1 44  ? 50.43300  -3.33900  8.98400  1.000 29.27262 ? 44  SER A CA  1 
ATOM   302  C  C   . SER A 1 44  ? 49.36900  -3.02800  10.03200 1.000 28.66225 ? 44  SER A C   1 
ATOM   303  O  O   . SER A 1 44  ? 49.65000  -2.31400  11.00000 1.000 27.77796 ? 44  SER A O   1 
ATOM   304  C  CB  . SER A 1 44  ? 50.41900  -2.27700  7.88300  1.000 30.26915 ? 44  SER A CB  1 
ATOM   305  O  OG  . SER A 1 44  ? 49.24500  -2.35800  7.10100  1.000 32.14992 ? 44  SER A OG  1 
ATOM   306  N  N   . PHE A 1 45  ? 48.18600  -3.60700  9.90300  1.000 28.51537 ? 45  PHE A N   1 
ATOM   307  C  CA  . PHE A 1 45  ? 47.16800  -3.44500  10.96700 1.000 27.92590 ? 45  PHE A CA  1 
ATOM   308  C  C   . PHE A 1 45  ? 47.73500  -3.99500  12.24400 1.000 28.52208 ? 45  PHE A C   1 
ATOM   309  O  O   . PHE A 1 45  ? 47.66800  -3.33800  13.26500 1.000 29.48643 ? 45  PHE A O   1 
ATOM   310  C  CB  . PHE A 1 45  ? 45.87300  -4.12800  10.54100 1.000 27.21817 ? 45  PHE A CB  1 
ATOM   311  C  CG  . PHE A 1 45  ? 44.61600  -3.82200  11.34500 1.000 27.05290 ? 45  PHE A CG  1 
ATOM   312  C  CD1 . PHE A 1 45  ? 44.64000  -2.94200  12.41700 1.000 26.06834 ? 45  PHE A CD1 1 
ATOM   313  C  CD2 . PHE A 1 45  ? 43.40500  -4.41600  11.01200 1.000 25.94808 ? 45  PHE A CD2 1 
ATOM   314  C  CE1 . PHE A 1 45  ? 43.49200  -2.68000  13.14000 1.000 26.03349 ? 45  PHE A CE1 1 
ATOM   315  C  CE2 . PHE A 1 45  ? 42.26000  -4.14500  11.73500 1.000 23.59855 ? 45  PHE A CE2 1 
ATOM   316  C  CZ  . PHE A 1 45  ? 42.30800  -3.27800  12.79600 1.000 25.08201 ? 45  PHE A CZ  1 
ATOM   317  N  N   . ASN A 1 46  ? 48.33100  -5.18400  12.16000 1.000 28.86347 ? 46  ASN A N   1 
ATOM   318  C  CA  . ASN A 1 46  ? 48.94200  -5.78800  13.34400 1.000 28.70864 ? 46  ASN A CA  1 
ATOM   319  C  C   . ASN A 1 46  ? 50.09000  -4.93800  13.88500 1.000 28.44087 ? 46  ASN A C   1 
ATOM   320  O  O   . ASN A 1 46  ? 50.26300  -4.81800  15.10200 1.000 28.02308 ? 46  ASN A O   1 
ATOM   321  C  CB  . ASN A 1 46  ? 49.43900  -7.19700  13.01200 1.000 29.03516 ? 46  ASN A CB  1 
ATOM   322  C  CG  . ASN A 1 46  ? 48.34700  -8.22800  13.07900 1.000 29.77847 ? 46  ASN A CG  1 
ATOM   323  O  OD1 . ASN A 1 46  ? 47.48500  -8.16900  13.94500 1.000 30.23649 ? 46  ASN A OD1 1 
ATOM   324  N  ND2 . ASN A 1 46  ? 48.37900  -9.18600  12.16700 1.000 31.11967 ? 46  ASN A ND2 1 
ATOM   325  N  N   . ARG A 1 47  ? 50.90000  -4.36400  12.99600 1.000 28.96512 ? 47  ARG A N   1 
ATOM   326  C  CA  . ARG A 1 47  ? 51.95700  -3.44700  13.41700 1.000 29.51612 ? 47  ARG A CA  1 
ATOM   327  C  C   . ARG A 1 47  ? 51.38700  -2.27600  14.21500 1.000 28.42510 ? 47  ARG A C   1 
ATOM   328  O  O   . ARG A 1 47  ? 51.87500  -1.95500  15.30400 1.000 27.96321 ? 47  ARG A O   1 
ATOM   329  C  CB  . ARG A 1 47  ? 52.70700  -2.94900  12.18300 1.000 30.96137 ? 47  ARG A CB  1 
ATOM   330  C  CG  . ARG A 1 47  ? 53.99400  -2.21700  12.45200 1.000 31.76365 ? 47  ARG A CG  1 
ATOM   331  C  CD  . ARG A 1 47  ? 54.97600  -2.61500  11.39000 1.000 33.53827 ? 47  ARG A CD  1 
ATOM   332  N  NE  . ARG A 1 47  ? 54.36000  -2.49100  10.07800 1.000 32.52041 ? 47  ARG A NE  1 
ATOM   333  C  CZ  . ARG A 1 47  ? 54.56400  -3.32600  9.07000  1.000 33.89047 ? 47  ARG A CZ  1 
ATOM   334  N  NH1 . ARG A 1 47  ? 55.33700  -4.39000  9.19900  1.000 37.13124 ? 47  ARG A NH1 1 
ATOM   335  N  NH2 . ARG A 1 47  ? 53.98000  -3.08300  7.90100  1.000 33.38573 ? 47  ARG A NH2 1 
ATOM   336  N  N   . GLU A 1 48  ? 50.35000  -1.62500  13.67900 1.000 28.30131 ? 48  GLU A N   1 
ATOM   337  C  CA  . GLU A 1 48  ? 49.71000  -0.51900  14.38500 1.000 27.66851 ? 48  GLU A CA  1 
ATOM   338  C  C   . GLU A 1 48  ? 49.12800  -0.97400  15.71800 1.000 28.98588 ? 48  GLU A C   1 
ATOM   339  O  O   . GLU A 1 48  ? 49.26300  -0.27700  16.73100 1.000 30.09733 ? 48  GLU A O   1 
ATOM   340  C  CB  . GLU A 1 48  ? 48.63200  0.09500   13.49800 1.000 25.42501 ? 48  GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 48  ? 49.21400  0.74300   12.26900 1.000 26.22695 ? 48  GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 48  ? 48.23200  0.83900   11.13000 1.000 25.56780 ? 48  GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 48  ? 47.02400  0.65100   11.38300 1.000 25.39620 ? 48  GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 48  ? 48.66800  1.09900   9.98300  1.000 25.23332 ? 48  GLU A OE2 1 
ATOM   345  N  N   . LEU A 1 49  ? 48.49000  -2.14700  15.74300 1.000 27.35309 ? 49  LEU A N   1 
ATOM   346  C  CA  . LEU A 1 49  ? 47.99200  -2.69600  16.99900 1.000 28.41966 ? 49  LEU A CA  1 
ATOM   347  C  C   . LEU A 1 49  ? 49.13200  -2.99000  17.97200 1.000 29.95556 ? 49  LEU A C   1 
ATOM   348  O  O   . LEU A 1 49  ? 48.99800  -2.77600  19.18300 1.000 30.13101 ? 49  LEU A O   1 
ATOM   349  C  CB  . LEU A 1 49  ? 47.19100  -3.95800  16.71000 1.000 28.41840 ? 49  LEU A CB  1 
ATOM   350  C  CG  . LEU A 1 49  ? 45.99900  -3.69300  15.80000 1.000 28.10261 ? 49  LEU A CG  1 
ATOM   351  C  CD1 . LEU A 1 49  ? 45.53000  -4.99100  15.19800 1.000 27.69998 ? 49  LEU A CD1 1 
ATOM   352  C  CD2 . LEU A 1 49  ? 44.89100  -3.02100  16.57000 1.000 25.73566 ? 49  LEU A CD2 1 
ATOM   353  N  N   . ASP A 1 50  ? 50.25800  -3.49600  17.45600 1.000 29.92589 ? 50  ASP A N   1 
ATOM   354  C  CA  . ASP A 1 50  ? 51.44200  -3.69900  18.28800 1.000 30.00837 ? 50  ASP A CA  1 
ATOM   355  C  C   . ASP A 1 50  ? 51.87400  -2.39000  18.94200 1.000 30.60373 ? 50  ASP A C   1 
ATOM   356  O  O   . ASP A 1 50  ? 52.19100  -2.35200  20.13700 1.000 32.34727 ? 50  ASP A O   1 
ATOM   357  C  CB  . ASP A 1 50  ? 52.59500  -4.27100  17.45100 1.000 29.64578 ? 50  ASP A CB  1 
ATOM   358  C  CG  . ASP A 1 50  ? 52.36900  -5.71800  17.00300 1.000 29.44062 ? 50  ASP A CG  1 
ATOM   359  O  OD1 . ASP A 1 50  ? 51.49400  -6.41300  17.56000 1.000 28.31356 ? 50  ASP A OD1 1 
ATOM   360  O  OD2 . ASP A 1 50  ? 53.10300  -6.15700  16.08700 1.000 28.00680 ? 50  ASP A OD2 1 
ATOM   361  N  N   . VAL A 1 51  ? 51.91400  -1.30800  18.15800 1.000 29.96794 ? 51  VAL A N   1 
ATOM   362  C  CA  . VAL A 1 51  ? 52.24600  0.01000   18.69500 1.000 30.04440 ? 51  VAL A CA  1 
ATOM   363  C  C   . VAL A 1 51  ? 51.32800  0.35700   19.85300 1.000 32.12908 ? 51  VAL A C   1 
ATOM   364  O  O   . VAL A 1 51  ? 51.76200  0.92600   20.85800 1.000 34.98152 ? 51  VAL A O   1 
ATOM   365  C  CB  . VAL A 1 51  ? 52.17200  1.06700   17.58200 1.000 29.60588 ? 51  VAL A CB  1 
ATOM   366  C  CG1 . VAL A 1 51  ? 52.33000  2.45800   18.17100 1.000 31.99032 ? 51  VAL A CG1 1 
ATOM   367  C  CG2 . VAL A 1 51  ? 53.24000  0.80200   16.54900 1.000 29.64027 ? 51  VAL A CG2 1 
ATOM   368  N  N   . GLN A 1 52  ? 50.04800  -0.00300  19.74100 1.000 31.96881 ? 52  GLN A N   1 
ATOM   369  C  CA  . GLN A 1 52  ? 49.09400  0.26100   20.81000 1.000 32.35135 ? 52  GLN A CA  1 
ATOM   370  C  C   . GLN A 1 52  ? 49.18100  -0.76700  21.92400 1.000 34.16582 ? 52  GLN A C   1 
ATOM   371  O  O   . GLN A 1 52  ? 48.96100  -0.43000  23.09300 1.000 35.71373 ? 52  GLN A O   1 
ATOM   372  C  CB  . GLN A 1 52  ? 47.68000  0.29300   20.24700 1.000 30.88148 ? 52  GLN A CB  1 
ATOM   373  C  CG  . GLN A 1 52  ? 47.43400  1.44400   19.31000 1.000 29.68010 ? 52  GLN A CG  1 
ATOM   374  C  CD  . GLN A 1 52  ? 47.55200  2.74800   20.02500 1.000 29.70018 ? 52  GLN A CD  1 
ATOM   375  O  OE1 . GLN A 1 52  ? 47.03800  2.89700   21.12800 1.000 31.00887 ? 52  GLN A OE1 1 
ATOM   376  N  NE2 . GLN A 1 52  ? 48.24800  3.69800   19.42400 1.000 31.27920 ? 52  GLN A NE2 1 
ATOM   377  N  N   . MET A 1 53  ? 49.47900  -2.02000  21.58300 1.000 33.42566 ? 53  MET A N   1 
ATOM   378  C  CA  . MET A 1 53  ? 49.64400  -3.03800  22.61400 1.000 34.41173 ? 53  MET A CA  1 
ATOM   379  C  C   . MET A 1 53  ? 50.85300  -2.75300  23.49100 1.000 37.26610 ? 53  MET A C   1 
ATOM   380  O  O   . MET A 1 53  ? 50.88200  -3.16000  24.65700 1.000 39.71378 ? 53  MET A O   1 
ATOM   381  C  CB  . MET A 1 53  ? 49.77000  -4.42100  21.97500 1.000 32.78213 ? 53  MET A CB  1 
ATOM   382  C  CG  . MET A 1 53  ? 48.45600  -4.98900  21.51800 1.000 31.58778 ? 53  MET A CG  1 
ATOM   383  S  SD  . MET A 1 53  ? 47.34800  -5.16200  22.91500 1.000 33.89190 ? 53  MET A SD  1 
ATOM   384  C  CE  . MET A 1 53  ? 47.98200  -6.64100  23.67300 1.000 31.81529 ? 53  MET A CE  1 
ATOM   385  N  N   . ALA A 1 54  ? 51.85400  -2.05400  22.95600 1.000 36.23752 ? 54  ALA A N   1 
ATOM   386  C  CA  . ALA A 1 54  ? 53.05600  -1.77000  23.72700 1.000 38.34663 ? 54  ALA A CA  1 
ATOM   387  C  C   . ALA A 1 54  ? 52.79200  -0.81800  24.88200 1.000 40.64147 ? 54  ALA A C   1 
ATOM   388  O  O   . ALA A 1 54  ? 53.57600  -0.79300  25.83500 1.000 42.47935 ? 54  ALA A O   1 
ATOM   389  C  CB  . ALA A 1 54  ? 54.14300  -1.18800  22.82100 1.000 37.49612 ? 54  ALA A CB  1 
ATOM   390  N  N   . ILE A 1 55  ? 51.71500  -0.04000  24.82000 1.000 44.09486 ? 55  ILE A N   1 
ATOM   391  C  CA  . ILE A 1 55  ? 51.42900  0.98100   25.82500 1.000 45.91601 ? 55  ILE A CA  1 
ATOM   392  C  C   . ILE A 1 55  ? 50.92400  0.30600   27.09500 1.000 48.01541 ? 55  ILE A C   1 
ATOM   393  O  O   . ILE A 1 55  ? 49.89500  -0.38600  27.05000 1.000 48.08244 ? 55  ILE A O   1 
ATOM   394  C  CB  . ILE A 1 55  ? 50.39500  2.00400   25.31900 1.000 46.38537 ? 55  ILE A CB  1 
ATOM   395  C  CG1 . ILE A 1 55  ? 50.63600  2.37700   23.85500 1.000 41.63791 ? 55  ILE A CG1 1 
ATOM   396  C  CG2 . ILE A 1 55  ? 50.44500  3.26000   26.16900 1.000 48.12438 ? 55  ILE A CG2 1 
ATOM   397  C  CD1 . ILE A 1 55  ? 51.69600  3.42800   23.65700 1.000 42.41335 ? 55  ILE A CD1 1 
ATOM   398  N  N   . PRO A 1 56  ? 51.59300  0.46700   28.23500 1.000 48.85616 ? 56  PRO A N   1 
ATOM   399  C  CA  . PRO A 1 56  ? 51.00300  0.02400   29.50200 1.000 51.49553 ? 56  PRO A CA  1 
ATOM   400  C  C   . PRO A 1 56  ? 49.63000  0.64900   29.68100 1.000 53.07706 ? 56  PRO A C   1 
ATOM   401  O  O   . PRO A 1 56  ? 49.44600  1.84900   29.42600 1.000 53.11924 ? 56  PRO A O   1 
ATOM   402  C  CB  . PRO A 1 56  ? 52.00700  0.51100   30.56100 1.000 49.76852 ? 56  PRO A CB  1 
ATOM   403  C  CG  . PRO A 1 56  ? 52.91200  1.46400   29.85600 1.000 48.20871 ? 56  PRO A CG  1 
ATOM   404  C  CD  . PRO A 1 56  ? 52.92300  1.06800   28.42300 1.000 47.04879 ? 56  PRO A CD  1 
ATOM   405  N  N   . PRO A 1 57  ? 48.63300  -0.13800  30.07600 1.000 54.63868 ? 57  PRO A N   1 
ATOM   406  C  CA  . PRO A 1 57  ? 47.22300  0.22400   29.77900 1.000 56.77654 ? 57  PRO A CA  1 
ATOM   407  C  C   . PRO A 1 57  ? 46.59100  1.21500   30.76100 1.000 60.24104 ? 57  PRO A C   1 
ATOM   408  O  O   . PRO A 1 57  ? 46.07300  2.24800   30.31100 1.000 58.30861 ? 57  PRO A O   1 
ATOM   409  C  CB  . PRO A 1 57  ? 46.48200  -1.12000  29.82400 1.000 53.49545 ? 57  PRO A CB  1 
ATOM   410  C  CG  . PRO A 1 57  ? 47.56300  -2.19200  29.88500 1.000 52.60882 ? 57  PRO A CG  1 
ATOM   411  C  CD  . PRO A 1 57  ? 48.78700  -1.55300  30.45400 1.000 54.44155 ? 57  PRO A CD  1 
ATOM   412  N  N   . PRO A 1 58  ? 46.55000  0.94200   32.10000 1.000 65.90112 ? 58  PRO A N   1 
ATOM   413  C  CA  . PRO A 1 58  ? 45.78400  1.85600   32.95500 1.000 65.06653 ? 58  PRO A CA  1 
ATOM   414  C  C   . PRO A 1 58  ? 46.53800  2.49700   34.12100 1.000 75.30726 ? 58  PRO A C   1 
ATOM   415  O  O   . PRO A 1 58  ? 47.10800  1.81700   34.98200 1.000 76.41418 ? 58  PRO A O   1 
ATOM   416  C  CB  . PRO A 1 58  ? 44.69600  0.94400   33.50700 1.000 65.11627 ? 58  PRO A CB  1 
ATOM   417  C  CG  . PRO A 1 58  ? 45.42300  -0.41800  33.62900 1.000 65.83293 ? 58  PRO A CG  1 
ATOM   418  C  CD  . PRO A 1 58  ? 46.74800  -0.30200  32.85800 1.000 66.23878 ? 58  PRO A CD  1 
ATOM   419  N  N   . LYS A 1 59  ? 46.49700  3.81600   34.18100 1.000 86.67198 ? 59  LYS A N   1 
ATOM   420  C  CA  . LYS A 1 59  ? 46.66300  4.49500   35.45200 1.000 88.07090 ? 59  LYS A CA  1 
ATOM   421  C  C   . LYS A 1 59  ? 45.32300  4.69100   36.15000 1.000 87.38718 ? 59  LYS A C   1 
ATOM   422  O  O   . LYS A 1 59  ? 45.24600  5.45000   37.12100 1.000 90.90276 ? 59  LYS A O   1 
ATOM   423  C  CB  . LYS A 1 59  ? 47.37300  5.83900   35.25400 1.000 91.32266 ? 59  LYS A CB  1 
ATOM   424  C  CG  . LYS A 1 59  ? 48.81200  5.73000   34.75000 1.000 93.33512 ? 59  LYS A CG  1 
ATOM   425  C  CD  . LYS A 1 59  ? 49.77000  5.28600   35.84300 1.000 90.52302 ? 59  LYS A CD  1 
ATOM   426  C  CE  . LYS A 1 59  ? 51.20600  5.30500   35.34500 1.000 90.81730 ? 59  LYS A CE  1 
ATOM   427  N  NZ  . LYS A 1 59  ? 52.19100  5.19900   36.45800 1.000 90.95297 ? 59  LYS A NZ  1 
ATOM   428  N  N   . GLY A 1 60  ? 44.26900  4.02200   35.67200 1.000 68.25473 ? 60  GLY A N   1 
ATOM   429  C  CA  . GLY A 1 60  ? 42.95500  4.15700   36.26800 1.000 57.47987 ? 60  GLY A CA  1 
ATOM   430  C  C   . GLY A 1 60  ? 41.84400  3.32500   35.65700 1.000 47.27062 ? 60  GLY A C   1 
ATOM   431  O  O   . GLY A 1 60  ? 41.98900  2.12000   35.45100 1.000 47.76499 ? 60  GLY A O   1 
ATOM   432  N  N   . GLU A 1 61  ? 40.72600  3.97700   35.36400 1.000 37.07438 ? 61  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 61  ? 39.50200  3.29700   34.97000 1.000 33.60160 ? 61  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 61  ? 39.54800  2.82500   33.52100 1.000 31.64197 ? 61  GLU A C   1 
ATOM   435  O  O   . GLU A 1 61  ? 39.95200  3.56400   32.62300 1.000 31.67852 ? 61  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 61  ? 38.31900  4.23700   35.16200 1.000 31.95492 ? 61  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 61  ? 37.01300  3.69800   34.70800 1.000 30.15453 ? 61  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 61  ? 35.87600  4.58500   35.13400 1.000 31.67571 ? 61  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 61  ? 35.97400  5.81800   34.94900 1.000 32.42325 ? 61  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 61  ? 34.89100  4.05000   35.67800 1.000 33.08908 ? 61  GLU A OE2 1 
ATOM   441  N  N   . ARG A 1 62  ? 39.12200  1.57900   33.29400 1.000 30.43489 ? 62  ARG A N   1 
ATOM   442  C  CA  . ARG A 1 62  ? 39.00600  0.98400   31.93800 1.000 29.15594 ? 62  ARG A CA  1 
ATOM   443  C  C   . ARG A 1 62  ? 37.56000  0.47300   31.85900 1.000 28.02004 ? 62  ARG A C   1 
ATOM   444  O  O   . ARG A 1 62  ? 37.31000  -0.62100  32.35000 1.000 28.66073 ? 62  ARG A O   1 
ATOM   445  C  CB  . ARG A 1 62  ? 40.08100  -0.08600  31.77700 1.000 30.07465 ? 62  ARG A CB  1 
ATOM   446  C  CG  . ARG A 1 62  ? 41.50000  0.33600   32.11800 1.000 34.18017 ? 62  ARG A CG  1 
ATOM   447  C  CD  . ARG A 1 62  ? 42.33300  -0.92200  32.18500 1.000 38.16944 ? 62  ARG A CD  1 
ATOM   448  N  NE  . ARG A 1 62  ? 42.36600  -1.57400  30.87600 1.000 38.97455 ? 62  ARG A NE  1 
ATOM   449  C  CZ  . ARG A 1 62  ? 42.93200  -2.74400  30.64200 1.000 39.67628 ? 62  ARG A CZ  1 
ATOM   450  N  NH1 . ARG A 1 62  ? 43.14000  -3.58200  31.63900 1.000 40.25435 ? 62  ARG A NH1 1 
ATOM   451  N  NH2 . ARG A 1 62  ? 43.26600  -3.07500  29.41100 1.000 36.37355 ? 62  ARG A NH2 1 
ATOM   452  N  N   . LEU A 1 63  ? 36.65600  1.20600   31.21400 1.000 27.78505 ? 63  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 63  ? 35.22100  0.93500   31.32200 1.000 28.21076 ? 63  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 63  ? 34.86800  -0.49500  30.91100 1.000 27.25516 ? 63  LEU A C   1 
ATOM   455  O  O   . LEU A 1 63  ? 34.18800  -1.21200  31.65100 1.000 27.30884 ? 63  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 63  ? 34.44000  1.94400   30.48000 1.000 25.92269 ? 63  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 63  ? 34.53000  3.40400   30.90800 1.000 26.55363 ? 63  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 63  ? 33.75000  4.28500   29.95200 1.000 25.57961 ? 63  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 63  ? 34.02200  3.57600   32.30800 1.000 27.37608 ? 63  LEU A CD2 1 
ATOM   460  N  N   . LEU A 1 64  ? 35.29800  -0.91900  29.72500 1.000 26.34446 ? 64  LEU A N   1 
ATOM   461  C  CA  . LEU A 1 64  ? 34.97500  -2.26100  29.25400 1.000 26.65358 ? 64  LEU A CA  1 
ATOM   462  C  C   . LEU A 1 64  ? 35.88400  -3.31200  29.88700 1.000 27.59954 ? 64  LEU A C   1 
ATOM   463  O  O   . LEU A 1 64  ? 35.40700  -4.34900  30.36300 1.000 27.61462 ? 64  LEU A O   1 
ATOM   464  C  CB  . LEU A 1 64  ? 35.06400  -2.31300  27.72300 1.000 24.69536 ? 64  LEU A CB  1 
ATOM   465  C  CG  . LEU A 1 64  ? 34.76400  -3.64400  27.02300 1.000 24.65635 ? 64  LEU A CG  1 
ATOM   466  C  CD1 . LEU A 1 64  ? 34.10800  -3.42500  25.67600 1.000 25.67406 ? 64  LEU A CD1 1 
ATOM   467  C  CD2 . LEU A 1 64  ? 36.01900  -4.46500  26.83900 1.000 24.52971 ? 64  LEU A CD2 1 
ATOM   468  N  N   . ALA A 1 65  ? 37.19800  -3.05400  29.90000 1.000 27.64310 ? 65  ALA A N   1 
ATOM   469  C  CA  . ALA A 1 65  ? 38.16300  -4.06100  30.32800 1.000 27.00369 ? 65  ALA A CA  1 
ATOM   470  C  C   . ALA A 1 65  ? 37.97800  -4.42700  31.79300 1.000 26.40639 ? 65  ALA A C   1 
ATOM   471  O  O   . ALA A 1 65  ? 38.16700  -5.58500  32.16900 1.000 26.04035 ? 65  ALA A O   1 
ATOM   472  C  CB  . ALA A 1 65  ? 39.58500  -3.57000  30.06300 1.000 29.18933 ? 65  ALA A CB  1 
ATOM   473  N  N   . ASP A 1 66  ? 37.60600  -3.45900  32.63500 1.000 26.29170 ? 66  ASP A N   1 
ATOM   474  C  CA  . ASP A 1 66  ? 37.27100  -3.75900  34.02500 1.000 27.02073 ? 66  ASP A CA  1 
ATOM   475  C  C   . ASP A 1 66  ? 36.02300  -4.63200  34.16000 1.000 27.51053 ? 66  ASP A C   1 
ATOM   476  O  O   . ASP A 1 66  ? 35.81800  -5.24200  35.21400 1.000 28.55257 ? 66  ASP A O   1 
ATOM   477  C  CB  . ASP A 1 66  ? 37.05000  -2.46800  34.81800 1.000 28.43103 ? 66  ASP A CB  1 
ATOM   478  C  CG  . ASP A 1 66  ? 38.29100  -1.59200  34.89700 1.000 28.96900 ? 66  ASP A CG  1 
ATOM   479  O  OD1 . ASP A 1 66  ? 39.39700  -2.10800  34.67600 1.000 30.00281 ? 66  ASP A OD1 1 
ATOM   480  O  OD2 . ASP A 1 66  ? 38.15600  -0.38100  35.19000 1.000 30.45802 ? 66  ASP A OD2 1 
ATOM   481  N  N   . LYS A 1 67  ? 35.18600  -4.71200  33.12900 1.000 26.88604 ? 67  LYS A N   1 
ATOM   482  C  CA  . LYS A 1 67  ? 33.90000  -5.39500  33.21100 1.000 26.44583 ? 67  LYS A CA  1 
ATOM   483  C  C   . LYS A 1 67  ? 33.95900  -6.87500  32.84500 1.000 26.59499 ? 67  LYS A C   1 
ATOM   484  O  O   . LYS A 1 67  ? 32.94400  -7.56900  32.97600 1.000 25.47477 ? 67  LYS A O   1 
ATOM   485  C  CB  . LYS A 1 67  ? 32.88000  -4.70000  32.30100 1.000 25.96960 ? 67  LYS A CB  1 
ATOM   486  C  CG  . LYS A 1 67  ? 31.75900  -4.00600  33.03500 1.000 27.56282 ? 67  LYS A CG  1 
ATOM   487  C  CD  . LYS A 1 67  ? 32.28600  -2.95100  33.98500 1.000 28.79581 ? 67  LYS A CD  1 
ATOM   488  C  CE  . LYS A 1 67  ? 31.15100  -2.21400  34.70600 1.000 31.79654 ? 67  LYS A CE  1 
ATOM   489  N  NZ  . LYS A 1 67  ? 31.63200  -1.09500  35.56200 1.000 33.06751 ? 67  LYS A NZ  1 
ATOM   490  N  N   . TYR A 1 68  ? 35.10100  -7.37600  32.39100 1.000 26.30602 ? 68  TYR A N   1 
ATOM   491  C  CA  . TYR A 1 68  ? 35.20000  -8.75200  31.93100 1.000 27.27788 ? 68  TYR A CA  1 
ATOM   492  C  C   . TYR A 1 68  ? 36.43000  -9.41400  32.53100 1.000 27.66418 ? 68  TYR A C   1 
ATOM   493  O  O   . TYR A 1 68  ? 37.42400  -8.74300  32.83000 1.000 25.96113 ? 68  TYR A O   1 
ATOM   494  C  CB  . TYR A 1 68  ? 35.26400  -8.82200  30.39400 1.000 26.55984 ? 68  TYR A CB  1 
ATOM   495  C  CG  . TYR A 1 68  ? 33.98800  -8.38300  29.68700 1.000 25.46392 ? 68  TYR A CG  1 
ATOM   496  C  CD1 . TYR A 1 68  ? 33.75400  -7.03000  29.47000 1.000 25.79872 ? 68  TYR A CD1 1 
ATOM   497  C  CD2 . TYR A 1 68  ? 33.05800  -9.32400  29.25300 1.000 25.40143 ? 68  TYR A CD2 1 
ATOM   498  C  CE1 . TYR A 1 68  ? 32.60500  -6.64100  28.84000 1.000 25.57719 ? 68  TYR A CE1 1 
ATOM   499  C  CE2 . TYR A 1 68  ? 31.91700  -8.90000  28.62700 1.000 25.58012 ? 68  TYR A CE2 1 
ATOM   500  C  CZ  . TYR A 1 68  ? 31.66700  -7.55800  28.40800 1.000 26.66931 ? 68  TYR A CZ  1 
ATOM   501  O  OH  . TYR A 1 68  ? 30.55000  -7.13900  27.79700 1.000 30.08835 ? 68  TYR A OH  1 
ATOM   502  N  N   . PRO A 1 69  ? 36.38800  -10.73000 32.72600 1.000 28.23164 ? 69  PRO A N   1 
ATOM   503  C  CA  . PRO A 1 69  ? 37.48600  -11.41600 33.40800 1.000 28.26791 ? 69  PRO A CA  1 
ATOM   504  C  C   . PRO A 1 69  ? 38.78700  -11.25700 32.64800 1.000 28.54939 ? 69  PRO A C   1 
ATOM   505  O  O   . PRO A 1 69  ? 38.79000  -10.86800 31.47100 1.000 28.53635 ? 69  PRO A O   1 
ATOM   506  C  CB  . PRO A 1 69  ? 37.02500  -12.88100 33.43500 1.000 29.08850 ? 69  PRO A CB  1 
ATOM   507  C  CG  . PRO A 1 69  ? 36.01700  -12.97400 32.35600 1.000 29.90826 ? 69  PRO A CG  1 
ATOM   508  C  CD  . PRO A 1 69  ? 35.32100  -11.66100 32.33600 1.000 27.58770 ? 69  PRO A CD  1 
ATOM   509  N  N   . PRO A 1 70  ? 39.90600  -11.54000 33.29000 1.000 28.91977 ? 70  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 70  ? 41.20600  -11.37900 32.63100 1.000 28.17395 ? 70  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 70  ? 41.52200  -12.46100 31.60400 1.000 30.84798 ? 70  PRO A C   1 
ATOM   512  O  O   . PRO A 1 70  ? 42.53300  -13.15700 31.73100 1.000 33.60408 ? 70  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 70  ? 42.17600  -11.44400 33.81100 1.000 28.05781 ? 70  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 70  ? 41.47400  -12.32300 34.80700 1.000 27.26174 ? 70  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 70  ? 40.04400  -11.93200 34.70500 1.000 28.18933 ? 70  PRO A CD  1 
ATOM   516  N  N   . HIS A 1 71  ? 40.68900  -12.61400 30.57700 1.000 31.27860 ? 71  HIS A N   1 
ATOM   517  C  CA  . HIS A 1 71  ? 40.83000  -13.71300 29.62900 1.000 32.76901 ? 71  HIS A CA  1 
ATOM   518  C  C   . HIS A 1 71  ? 41.21700  -13.24600 28.23800 1.000 33.19777 ? 71  HIS A C   1 
ATOM   519  O  O   . HIS A 1 71  ? 41.17400  -14.04300 27.29700 1.000 35.42635 ? 71  HIS A O   1 
ATOM   520  C  CB  . HIS A 1 71  ? 39.53700  -14.53000 29.55400 1.000 34.22274 ? 71  HIS A CB  1 
ATOM   521  C  CG  . HIS A 1 71  ? 39.21100  -15.26400 30.81900 1.000 34.19455 ? 71  HIS A CG  1 
ATOM   522  N  ND1 . HIS A 1 71  ? 37.94400  -15.71400 31.11300 1.000 31.28442 ? 71  HIS A ND1 1 
ATOM   523  C  CD2 . HIS A 1 71  ? 39.98800  -15.61700 31.86900 1.000 34.23733 ? 71  HIS A CD2 1 
ATOM   524  C  CE1 . HIS A 1 71  ? 37.95300  -16.31000 32.29000 1.000 32.41295 ? 71  HIS A CE1 1 
ATOM   525  N  NE2 . HIS A 1 71  ? 39.18400  -16.27100 32.76700 1.000 33.74292 ? 71  HIS A NE2 1 
ATOM   526  N  N   . PHE A 1 72  ? 41.58000  -11.98100 28.08100 1.000 30.65951 ? 72  PHE A N   1 
ATOM   527  C  CA  . PHE A 1 72  ? 41.98200  -11.45100 26.79100 1.000 30.67888 ? 72  PHE A CA  1 
ATOM   528  C  C   . PHE A 1 72  ? 42.60200  -10.09400 27.04200 1.000 29.63508 ? 72  PHE A C   1 
ATOM   529  O  O   . PHE A 1 72  ? 42.45100  -9.51500  28.11800 1.000 29.10816 ? 72  PHE A O   1 
ATOM   530  C  CB  . PHE A 1 72  ? 40.79500  -11.33400 25.81700 1.000 31.69472 ? 72  PHE A CB  1 
ATOM   531  C  CG  . PHE A 1 72  ? 39.51200  -10.86400 26.46900 1.000 30.52276 ? 72  PHE A CG  1 
ATOM   532  C  CD1 . PHE A 1 72  ? 39.30700  -9.52400  26.75300 1.000 30.30147 ? 72  PHE A CD1 1 
ATOM   533  C  CD2 . PHE A 1 72  ? 38.51400  -11.77100 26.79900 1.000 31.01830 ? 72  PHE A CD2 1 
ATOM   534  C  CE1 . PHE A 1 72  ? 38.14000  -9.10100  27.35500 1.000 28.58637 ? 72  PHE A CE1 1 
ATOM   535  C  CE2 . PHE A 1 72  ? 37.34400  -11.35600 27.39800 1.000 29.45052 ? 72  PHE A CE2 1 
ATOM   536  C  CZ  . PHE A 1 72  ? 37.16200  -10.01900 27.67900 1.000 29.26180 ? 72  PHE A CZ  1 
ATOM   537  N  N   . LYS A 1 73  ? 43.31000  -9.60600  26.03900 1.000 29.90650 ? 73  LYS A N   1 
ATOM   538  C  CA  . LYS A 1 73  ? 43.79600  -8.23900  25.99000 1.000 29.71236 ? 73  LYS A CA  1 
ATOM   539  C  C   . LYS A 1 73  ? 42.95900  -7.46100  24.98400 1.000 27.15476 ? 73  LYS A C   1 
ATOM   540  O  O   . LYS A 1 73  ? 42.46900  -8.02200  24.00100 1.000 26.05837 ? 73  LYS A O   1 
ATOM   541  C  CB  . LYS A 1 73  ? 45.27800  -8.18600  25.60000 1.000 30.10555 ? 73  LYS A CB  1 
ATOM   542  C  CG  . LYS A 1 73  ? 46.23700  -8.82500  26.59900 1.000 32.11779 ? 73  LYS A CG  1 
ATOM   543  C  CD  . LYS A 1 73  ? 46.36600  -7.98500  27.85200 1.000 34.24314 ? 73  LYS A CD  1 
ATOM   544  C  CE  . LYS A 1 73  ? 46.95000  -6.61200  27.53000 1.000 37.14837 ? 73  LYS A CE  1 
ATOM   545  N  NZ  . LYS A 1 73  ? 46.70900  -5.58300  28.60400 1.000 41.18839 ? 73  LYS A NZ  1 
ATOM   546  N  N   . TYR A 1 74  ? 42.82100  -6.15600  25.22400 1.000 26.60390 ? 74  TYR A N   1 
ATOM   547  C  CA  . TYR A 1 74  ? 41.81200  -5.32600  24.57100 1.000 24.16270 ? 74  TYR A CA  1 
ATOM   548  C  C   . TYR A 1 74  ? 42.40700  -4.00100  24.11900 1.000 24.30764 ? 74  TYR A C   1 
ATOM   549  O  O   . TYR A 1 74  ? 42.99000  -3.27700  24.93000 1.000 26.09733 ? 74  TYR A O   1 
ATOM   550  C  CB  . TYR A 1 74  ? 40.65500  -5.07300  25.54100 1.000 24.56544 ? 74  TYR A CB  1 
ATOM   551  C  CG  . TYR A 1 74  ? 39.57300  -4.08800  25.11900 1.000 23.55433 ? 74  TYR A CG  1 
ATOM   552  C  CD1 . TYR A 1 74  ? 38.60900  -4.45900  24.18600 1.000 23.65626 ? 74  TYR A CD1 1 
ATOM   553  C  CD2 . TYR A 1 74  ? 39.51200  -2.82500  25.70400 1.000 24.14443 ? 74  TYR A CD2 1 
ATOM   554  C  CE1 . TYR A 1 74  ? 37.62900  -3.56500  23.83400 1.000 22.24544 ? 74  TYR A CE1 1 
ATOM   555  C  CE2 . TYR A 1 74  ? 38.51800  -1.95800  25.32500 1.000 24.20467 ? 74  TYR A CE2 1 
ATOM   556  C  CZ  . TYR A 1 74  ? 37.55500  -2.29900  24.38900 1.000 23.17794 ? 74  TYR A CZ  1 
ATOM   557  O  OH  . TYR A 1 74  ? 36.58800  -1.43300  24.02200 1.000 24.53052 ? 74  TYR A OH  1 
ATOM   558  N  N   . VAL A 1 75  ? 42.23500  -3.67700  22.83900 1.000 23.95254 ? 75  VAL A N   1 
ATOM   559  C  CA  . VAL A 1 75  ? 42.57400  -2.36100  22.29700 1.000 24.90735 ? 75  VAL A CA  1 
ATOM   560  C  C   . VAL A 1 75  ? 41.30000  -1.68200  21.80600 1.000 23.51265 ? 75  VAL A C   1 
ATOM   561  O  O   . VAL A 1 75  ? 40.71700  -2.11500  20.80300 1.000 23.01081 ? 75  VAL A O   1 
ATOM   562  C  CB  . VAL A 1 75  ? 43.60000  -2.45300  21.15700 1.000 24.12818 ? 75  VAL A CB  1 
ATOM   563  C  CG1 . VAL A 1 75  ? 43.71200  -1.10900  20.48000 1.000 24.85230 ? 75  VAL A CG1 1 
ATOM   564  C  CG2 . VAL A 1 75  ? 44.96700  -2.86600  21.67800 1.000 25.06021 ? 75  VAL A CG2 1 
ATOM   565  N  N   . PRO A 1 76  ? 40.83900  -0.62200  22.45700 1.000 22.75883 ? 76  PRO A N   1 
ATOM   566  C  CA  . PRO A 1 76  ? 39.56500  -0.00800  22.07200 1.000 23.18231 ? 76  PRO A CA  1 
ATOM   567  C  C   . PRO A 1 76  ? 39.70100  0.91500   20.87200 1.000 23.12298 ? 76  PRO A C   1 
ATOM   568  O  O   . PRO A 1 76  ? 40.78800  1.37700   20.52700 1.000 23.99444 ? 76  PRO A O   1 
ATOM   569  C  CB  . PRO A 1 76  ? 39.17600  0.78500   23.32100 1.000 23.68942 ? 76  PRO A CB  1 
ATOM   570  C  CG  . PRO A 1 76  ? 40.49400  1.15600   23.91200 1.000 23.99731 ? 76  PRO A CG  1 
ATOM   571  C  CD  . PRO A 1 76  ? 41.40500  -0.00800  23.66900 1.000 23.67706 ? 76  PRO A CD  1 
ATOM   572  N  N   . ASN A 1 77  ? 38.54900  1.18800   20.24800 1.000 22.53515 ? 77  ASN A N   1 
ATOM   573  C  CA  . ASN A 1 77  ? 38.36200  2.10900   19.12400 1.000 21.67064 ? 77  ASN A CA  1 
ATOM   574  C  C   . ASN A 1 77  ? 39.54900  2.18600   18.17100 1.000 21.92734 ? 77  ASN A C   1 
ATOM   575  O  O   . ASN A 1 77  ? 40.19700  3.23000   18.06600 1.000 22.26838 ? 77  ASN A O   1 
ATOM   576  C  CB  . ASN A 1 77  ? 37.99900  3.52300   19.63000 1.000 21.30126 ? 77  ASN A CB  1 
ATOM   577  C  CG  . ASN A 1 77  ? 38.80300  3.96800   20.85400 1.000 22.20349 ? 77  ASN A CG  1 
ATOM   578  O  OD1 . ASN A 1 77  ? 38.33300  3.87400   21.97900 1.000 22.65861 ? 77  ASN A OD1 1 
ATOM   579  N  ND2 . ASN A 1 77  ? 40.00100  4.49600   20.62600 1.000 23.10395 ? 77  ASN A ND2 1 
ATOM   580  N  N   . VAL A 1 78  ? 39.82000  1.09900   17.44400 1.000 21.34318 ? 78  VAL A N   1 
ATOM   581  C  CA  . VAL A 1 78  ? 40.99800  1.05000   16.58900 1.000 21.65357 ? 78  VAL A CA  1 
ATOM   582  C  C   . VAL A 1 78  ? 40.93100  2.01400   15.41100 1.000 22.89272 ? 78  VAL A C   1 
ATOM   583  O  O   . VAL A 1 78  ? 41.96200  2.26300   14.78100 1.000 23.02364 ? 78  VAL A O   1 
ATOM   584  C  CB  . VAL A 1 78  ? 41.25600  -0.38300  16.07700 1.000 21.83345 ? 78  VAL A CB  1 
ATOM   585  C  CG1 . VAL A 1 78  ? 41.83900  -1.24200  17.18500 1.000 22.58522 ? 78  VAL A CG1 1 
ATOM   586  C  CG2 . VAL A 1 78  ? 39.98300  -1.01000  15.54300 1.000 21.91346 ? 78  VAL A CG2 1 
ATOM   587  N  N   . ALA A 1 79  ? 39.76100  2.58900   15.10500 1.000 22.82722 ? 79  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 79  ? 39.68800  3.57100   14.02300 1.000 21.57980 ? 79  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 79  ? 40.51100  4.81700   14.32900 1.000 22.22302 ? 79  ALA A C   1 
ATOM   590  O  O   . ALA A 1 79  ? 41.03800  5.44900   13.40600 1.000 22.65250 ? 79  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 79  ? 38.23800  3.96400   13.75000 1.000 21.13353 ? 79  ALA A CB  1 
ATOM   592  N  N   . THR A 1 80  ? 40.63800  5.19200   15.60200 1.000 22.30651 ? 80  THR A N   1 
ATOM   593  C  CA  . THR A 1 80  ? 41.35600  6.41800   15.93100 1.000 23.00208 ? 80  THR A CA  1 
ATOM   594  C  C   . THR A 1 80  ? 42.86300  6.22200   16.04800 1.000 24.05288 ? 80  THR A C   1 
ATOM   595  O  O   . THR A 1 80  ? 43.59900  7.20400   15.92100 1.000 23.76672 ? 80  THR A O   1 
ATOM   596  C  CB  . THR A 1 80  ? 40.84000  7.05100   17.23600 1.000 22.56746 ? 80  THR A CB  1 
ATOM   597  O  OG1 . THR A 1 80  ? 41.20800  6.22900   18.34500 1.000 23.12756 ? 80  THR A OG1 1 
ATOM   598  C  CG2 . THR A 1 80  ? 39.32400  7.22300   17.21900 1.000 22.28087 ? 80  THR A CG2 1 
ATOM   599  N  N   . THR A 1 81  ? 43.34900  4.99300   16.27300 1.000 24.06681 ? 81  THR A N   1 
ATOM   600  C  CA  . THR A 1 81  ? 44.78100  4.76500   16.44800 1.000 24.02591 ? 81  THR A CA  1 
ATOM   601  C  C   . THR A 1 81  ? 45.42800  3.94000   15.34300 1.000 24.09858 ? 81  THR A C   1 
ATOM   602  O  O   . THR A 1 81  ? 46.66100  3.90900   15.26800 1.000 25.55501 ? 81  THR A O   1 
ATOM   603  C  CB  . THR A 1 81  ? 45.07400  4.09100   17.80600 1.000 24.40715 ? 81  THR A CB  1 
ATOM   604  O  OG1 . THR A 1 81  ? 44.27700  2.91000   17.96800 1.000 24.52937 ? 81  THR A OG1 1 
ATOM   605  C  CG2 . THR A 1 81  ? 44.78500  5.03900   18.95200 1.000 25.69126 ? 81  THR A CG2 1 
ATOM   606  N  N   . CYS A 1 82  ? 44.65400  3.27700   14.48700 1.000 24.80599 ? 82  CYS A N   1 
ATOM   607  C  CA  . CYS A 1 82  ? 45.21200  2.37900   13.47700 1.000 24.56055 ? 82  CYS A CA  1 
ATOM   608  C  C   . CYS A 1 82  ? 44.88100  2.89100   12.08500 1.000 24.45260 ? 82  CYS A C   1 
ATOM   609  O  O   . CYS A 1 82  ? 43.74200  2.73600   11.61600 1.000 23.81674 ? 82  CYS A O   1 
ATOM   610  C  CB  . CYS A 1 82  ? 44.69600  0.95700   13.67700 1.000 23.87062 ? 82  CYS A CB  1 
ATOM   611  S  SG  . CYS A 1 82  ? 45.12100  0.31800   15.30300 1.000 24.91857 ? 82  CYS A SG  1 
ATOM   612  N  N   . PRO A 1 83  ? 45.83600  3.50400   11.39100 1.000 24.39260 ? 83  PRO A N   1 
ATOM   613  C  CA  . PRO A 1 83  ? 45.54200  4.04300   10.05500 1.000 24.24059 ? 83  PRO A CA  1 
ATOM   614  C  C   . PRO A 1 83  ? 45.04500  3.01800   9.04700  1.000 24.04543 ? 83  PRO A C   1 
ATOM   615  O  O   . PRO A 1 83  ? 44.21500  3.36600   8.20000  1.000 24.01790 ? 83  PRO A O   1 
ATOM   616  C  CB  . PRO A 1 83  ? 46.88500  4.64600   9.63600  1.000 25.07285 ? 83  PRO A CB  1 
ATOM   617  C  CG  . PRO A 1 83  ? 47.51300  5.05700   10.93900 1.000 26.24293 ? 83  PRO A CG  1 
ATOM   618  C  CD  . PRO A 1 83  ? 47.13000  3.98100   11.91300 1.000 24.75534 ? 83  PRO A CD  1 
ATOM   619  N  N   . THR A 1 84  ? 45.51100  1.76900   9.10200  1.000 24.61932 ? 84  THR A N   1 
ATOM   620  C  CA  . THR A 1 84  ? 45.04900  0.77500   8.13600  1.000 24.23155 ? 84  THR A CA  1 
ATOM   621  C  C   . THR A 1 84  ? 43.55700  0.50300   8.27900  1.000 23.57783 ? 84  THR A C   1 
ATOM   622  O  O   . THR A 1 84  ? 42.84100  0.39600   7.27700  1.000 24.03462 ? 84  THR A O   1 
ATOM   623  C  CB  . THR A 1 84  ? 45.83600  -0.52100  8.28700  1.000 24.88947 ? 84  THR A CB  1 
ATOM   624  O  OG1 . THR A 1 84  ? 47.22400  -0.24600  8.08600  1.000 25.73301 ? 84  THR A OG1 1 
ATOM   625  C  CG2 . THR A 1 84  ? 45.37700  -1.53200  7.26600  1.000 24.95045 ? 84  THR A CG2 1 
ATOM   626  N  N   . PHE A 1 85  ? 43.06300  0.38500   9.51000  1.000 23.94980 ? 85  PHE A N   1 
ATOM   627  C  CA  . PHE A 1 85  ? 41.62700  0.18800   9.68100  1.000 22.99568 ? 85  PHE A CA  1 
ATOM   628  C  C   . PHE A 1 85  ? 40.85500  1.38900   9.16400  1.000 22.82151 ? 85  PHE A C   1 
ATOM   629  O  O   . PHE A 1 85  ? 39.89400  1.24500   8.40600  1.000 23.37526 ? 85  PHE A O   1 
ATOM   630  C  CB  . PHE A 1 85  ? 41.28400  -0.07100  11.14900 1.000 22.47418 ? 85  PHE A CB  1 
ATOM   631  C  CG  . PHE A 1 85  ? 39.83700  -0.43300  11.37100 1.000 21.85063 ? 85  PHE A CG  1 
ATOM   632  C  CD1 . PHE A 1 85  ? 38.88500  0.54700   11.58000 1.000 21.28528 ? 85  PHE A CD1 1 
ATOM   633  C  CD2 . PHE A 1 85  ? 39.43400  -1.74500  11.34900 1.000 20.85129 ? 85  PHE A CD2 1 
ATOM   634  C  CE1 . PHE A 1 85  ? 37.57400  0.21500   11.76600 1.000 20.75294 ? 85  PHE A CE1 1 
ATOM   635  C  CE2 . PHE A 1 85  ? 38.13100  -2.07000  11.53700 1.000 20.63960 ? 85  PHE A CE2 1 
ATOM   636  C  CZ  . PHE A 1 85  ? 37.20000  -1.09800  11.74500 1.000 19.74037 ? 85  PHE A CZ  1 
ATOM   637  N  N   . ARG A 1 86  ? 41.28000  2.58600   9.56100  1.000 22.84139 ? 86  ARG A N   1 
ATOM   638  C  CA  . ARG A 1 86  ? 40.53100  3.80000   9.27300  1.000 23.57170 ? 86  ARG A CA  1 
ATOM   639  C  C   . ARG A 1 86  ? 40.43200  4.05000   7.77900  1.000 23.42807 ? 86  ARG A C   1 
ATOM   640  O  O   . ARG A 1 86  ? 39.36000  4.38400   7.26400  1.000 23.48618 ? 86  ARG A O   1 
ATOM   641  C  CB  . ARG A 1 86  ? 41.22100  4.96700   9.97400  1.000 24.85927 ? 86  ARG A CB  1 
ATOM   642  C  CG  . ARG A 1 86  ? 40.52300  6.26900   9.90400  1.000 24.65442 ? 86  ARG A CG  1 
ATOM   643  C  CD  . ARG A 1 86  ? 41.17600  7.25100   10.84500 1.000 24.15758 ? 86  ARG A CD  1 
ATOM   644  N  NE  . ARG A 1 86  ? 42.47500  7.68100   10.36100 1.000 25.02793 ? 86  ARG A NE  1 
ATOM   645  C  CZ  . ARG A 1 86  ? 43.59000  7.61900   11.06700 1.000 24.28490 ? 86  ARG A CZ  1 
ATOM   646  N  NH1 . ARG A 1 86  ? 43.59900  7.15700   12.29900 1.000 24.99836 ? 86  ARG A NH1 1 
ATOM   647  N  NH2 . ARG A 1 86  ? 44.72400  8.03000   10.52200 1.000 25.35604 ? 86  ARG A NH2 1 
ATOM   648  N  N   . ASN A 1 87  ? 41.54100  3.87700   7.07100  1.000 23.39616 ? 87  ASN A N   1 
ATOM   649  C  CA  . ASN A 1 87  ? 41.69000  4.30100   5.69300  1.000 23.96670 ? 87  ASN A CA  1 
ATOM   650  C  C   . ASN A 1 87  ? 41.54800  3.17900   4.69200  1.000 24.60125 ? 87  ASN A C   1 
ATOM   651  O  O   . ASN A 1 87  ? 41.53400  3.45500   3.49000  1.000 25.55633 ? 87  ASN A O   1 
ATOM   652  C  CB  . ASN A 1 87  ? 43.05900  4.94100   5.48800  1.000 23.82756 ? 87  ASN A CB  1 
ATOM   653  C  CG  . ASN A 1 87  ? 43.20000  6.24300   6.22900  1.000 26.03855 ? 87  ASN A CG  1 
ATOM   654  O  OD1 . ASN A 1 87  ? 42.26000  7.04400   6.29500  1.000 26.94355 ? 87  ASN A OD1 1 
ATOM   655  N  ND2 . ASN A 1 87  ? 44.37900  6.46800   6.80000  1.000 26.52306 ? 87  ASN A ND2 1 
ATOM   656  N  N   . THR A 1 88  ? 41.47400  1.93100   5.14200  1.000 24.13408 ? 88  THR A N   1 
ATOM   657  C  CA  . THR A 1 88  ? 41.41400  0.83300   4.19500  1.000 23.48488 ? 88  THR A CA  1 
ATOM   658  C  C   . THR A 1 88  ? 40.38800  -0.19900  4.61900  1.000 23.44754 ? 88  THR A C   1 
ATOM   659  O  O   . THR A 1 88  ? 39.48900  -0.52600  3.84600  1.000 25.16208 ? 88  THR A O   1 
ATOM   660  C  CB  . THR A 1 88  ? 42.79300  0.20200   4.02700  1.000 24.14463 ? 88  THR A CB  1 
ATOM   661  O  OG1 . THR A 1 88  ? 43.65300  1.13700   3.36000  1.000 24.71538 ? 88  THR A OG1 1 
ATOM   662  C  CG2 . THR A 1 88  ? 42.70400  -1.07100  3.19300  1.000 23.80481 ? 88  THR A CG2 1 
ATOM   663  N  N   . VAL A 1 89  ? 40.49500  -0.73000  5.83000  1.000 23.62857 ? 89  VAL A N   1 
ATOM   664  C  CA  . VAL A 1 89  ? 39.58500  -1.80300  6.20600  1.000 23.84269 ? 89  VAL A CA  1 
ATOM   665  C  C   . VAL A 1 89  ? 38.17000  -1.26300  6.35200  1.000 23.34644 ? 89  VAL A C   1 
ATOM   666  O  O   . VAL A 1 89  ? 37.21700  -1.83800  5.82000  1.000 21.78438 ? 89  VAL A O   1 
ATOM   667  C  CB  . VAL A 1 89  ? 40.06300  -2.50600  7.48600  1.000 23.77986 ? 89  VAL A CB  1 
ATOM   668  C  CG1 . VAL A 1 89  ? 39.06800  -3.56400  7.88000  1.000 24.34595 ? 89  VAL A CG1 1 
ATOM   669  C  CG2 . VAL A 1 89  ? 41.41900  -3.14800  7.26900  1.000 23.68348 ? 89  VAL A CG2 1 
ATOM   670  N  N   . LEU A 1 90  ? 38.02500  -0.11800  7.02700  1.000 22.79111 ? 90  LEU A N   1 
ATOM   671  C  CA  . LEU A 1 90  ? 36.70200  0.42400   7.33800  1.000 22.68202 ? 90  LEU A CA  1 
ATOM   672  C  C   . LEU A 1 90  ? 35.91100  0.77700   6.08500  1.000 22.74787 ? 90  LEU A C   1 
ATOM   673  O  O   . LEU A 1 90  ? 34.67700  0.72600   6.09900  1.000 22.78565 ? 90  LEU A O   1 
ATOM   674  C  CB  . LEU A 1 90  ? 36.84300  1.65200   8.24200  1.000 22.03550 ? 90  LEU A CB  1 
ATOM   675  C  CG  . LEU A 1 90  ? 35.61500  2.46100   8.67100  1.000 21.11970 ? 90  LEU A CG  1 
ATOM   676  C  CD1 . LEU A 1 90  ? 34.67700  1.64600   9.55600  1.000 20.91215 ? 90  LEU A CD1 1 
ATOM   677  C  CD2 . LEU A 1 90  ? 36.07100  3.68900   9.40200  1.000 20.94250 ? 90  LEU A CD2 1 
ATOM   678  N  N   . ILE A 1 91  ? 36.58700  1.12100   4.99600  1.000 23.39276 ? 91  ILE A N   1 
ATOM   679  C  CA  . ILE A 1 91  ? 35.91500  1.50300   3.76200  1.000 23.96156 ? 91  ILE A CA  1 
ATOM   680  C  C   . ILE A 1 91  ? 36.03100  0.40900   2.70000  1.000 25.28017 ? 91  ILE A C   1 
ATOM   681  O  O   . ILE A 1 91  ? 35.87600  0.68100   1.51000  1.000 27.96791 ? 91  ILE A O   1 
ATOM   682  C  CB  . ILE A 1 91  ? 36.43200  2.85400   3.23700  1.000 26.99438 ? 91  ILE A CB  1 
ATOM   683  C  CG1 . ILE A 1 91  ? 37.94700  2.83000   3.07300  1.000 27.61225 ? 91  ILE A CG1 1 
ATOM   684  C  CG2 . ILE A 1 91  ? 36.02900  3.97800   4.16900  1.000 24.79665 ? 91  ILE A CG2 1 
ATOM   685  C  CD1 . ILE A 1 91  ? 38.51800  4.17100   2.71800  1.000 31.97702 ? 91  ILE A CD1 1 
ATOM   686  N  N   . ASN A 1 92  ? 36.28700  -0.82700  3.11000  1.000 24.87966 ? 92  ASN A N   1 
ATOM   687  C  CA  . ASN A 1 92  ? 36.37800  -1.91600  2.15200  1.000 24.53567 ? 92  ASN A CA  1 
ATOM   688  C  C   . ASN A 1 92  ? 35.04800  -2.07900  1.42000  1.000 25.51687 ? 92  ASN A C   1 
ATOM   689  O  O   . ASN A 1 92  ? 34.00300  -2.23400  2.06200  1.000 25.75501 ? 92  ASN A O   1 
ATOM   690  C  CB  . ASN A 1 92  ? 36.75900  -3.22100  2.83300  1.000 23.95279 ? 92  ASN A CB  1 
ATOM   691  C  CG  . ASN A 1 92  ? 36.90600  -4.35200  1.84500  1.000 24.95095 ? 92  ASN A CG  1 
ATOM   692  O  OD1 . ASN A 1 92  ? 35.92800  -5.00700  1.48400  1.000 25.95682 ? 92  ASN A OD1 1 
ATOM   693  N  ND2 . ASN A 1 92  ? 38.12400  -4.57000  1.37700  1.000 25.15652 ? 92  ASN A ND2 1 
ATOM   694  N  N   . PRO A 1 93  ? 35.04700  -2.06300  0.09000  1.000 26.37192 ? 93  PRO A N   1 
ATOM   695  C  CA  . PRO A 1 93  ? 33.77300  -2.03400  -0.64100 1.000 26.21886 ? 93  PRO A CA  1 
ATOM   696  C  C   . PRO A 1 93  ? 32.95800  -3.30400  -0.51500 1.000 26.05015 ? 93  PRO A C   1 
ATOM   697  O  O   . PRO A 1 93  ? 31.72700  -3.23300  -0.55800 1.000 27.19554 ? 93  PRO A O   1 
ATOM   698  C  CB  . PRO A 1 93  ? 34.21500  -1.79600  -2.08600 1.000 27.35933 ? 93  PRO A CB  1 
ATOM   699  C  CG  . PRO A 1 93  ? 35.59500  -1.19400  -1.96700 1.000 29.95335 ? 93  PRO A CG  1 
ATOM   700  C  CD  . PRO A 1 93  ? 36.20500  -1.85300  -0.78900 1.000 27.06864 ? 93  PRO A CD  1 
ATOM   701  N  N   . VAL A 1 94  ? 33.59700  -4.46600  -0.38500 1.000 25.55409 ? 94  VAL A N   1 
ATOM   702  C  CA  . VAL A 1 94  ? 32.84000  -5.70300  -0.22300 1.000 26.01353 ? 94  VAL A CA  1 
ATOM   703  C  C   . VAL A 1 94  ? 32.08100  -5.68900  1.10000  1.000 25.89788 ? 94  VAL A C   1 
ATOM   704  O  O   . VAL A 1 94  ? 30.91700  -6.10300  1.17500  1.000 25.47194 ? 94  VAL A O   1 
ATOM   705  C  CB  . VAL A 1 94  ? 33.77900  -6.91900  -0.33400 1.000 26.50172 ? 94  VAL A CB  1 
ATOM   706  C  CG1 . VAL A 1 94  ? 33.05100  -8.18400  0.03800  1.000 26.72594 ? 94  VAL A CG1 1 
ATOM   707  C  CG2 . VAL A 1 94  ? 34.33300  -7.04700  -1.74600 1.000 26.29773 ? 94  VAL A CG2 1 
ATOM   708  N  N   . ILE A 1 95  ? 32.72700  -5.20900  2.16000  1.000 25.93049 ? 95  ILE A N   1 
ATOM   709  C  CA  . ILE A 1 95  ? 32.04000  -5.02000  3.43100  1.000 25.06092 ? 95  ILE A CA  1 
ATOM   710  C  C   . ILE A 1 95  ? 30.84400  -4.09400  3.25400  1.000 24.54238 ? 95  ILE A C   1 
ATOM   711  O  O   . ILE A 1 95  ? 29.77700  -4.32100  3.82900  1.000 25.02990 ? 95  ILE A O   1 
ATOM   712  C  CB  . ILE A 1 95  ? 33.02100  -4.48000  4.49200  1.000 24.65199 ? 95  ILE A CB  1 
ATOM   713  C  CG1 . ILE A 1 95  ? 34.17200  -5.46700  4.76100  1.000 24.56057 ? 95  ILE A CG1 1 
ATOM   714  C  CG2 . ILE A 1 95  ? 32.28300  -4.13300  5.77400  1.000 23.80040 ? 95  ILE A CG2 1 
ATOM   715  C  CD1 . ILE A 1 95  ? 33.74900  -6.82500  5.30700  1.000 25.74125 ? 95  ILE A CD1 1 
ATOM   716  N  N   . HIS A 1 96  ? 30.99000  -3.04600  2.45200  1.000 24.63593 ? 96  HIS A N   1 
ATOM   717  C  CA  . HIS A 1 96  ? 29.89500  -2.10200  2.34000  1.000 25.23836 ? 96  HIS A CA  1 
ATOM   718  C  C   . HIS A 1 96  ? 28.81200  -2.57800  1.39200  1.000 26.52283 ? 96  HIS A C   1 
ATOM   719  O  O   . HIS A 1 96  ? 27.64100  -2.24300  1.59200  1.000 27.23051 ? 96  HIS A O   1 
ATOM   720  C  CB  . HIS A 1 96  ? 30.43200  -0.74400  1.93600  1.000 25.17692 ? 96  HIS A CB  1 
ATOM   721  C  CG  . HIS A 1 96  ? 31.13000  -0.06200  3.05600  1.000 24.05280 ? 96  HIS A CG  1 
ATOM   722  N  ND1 . HIS A 1 96  ? 30.46100  0.69600   3.98800  1.000 23.26703 ? 96  HIS A ND1 1 
ATOM   723  C  CD2 . HIS A 1 96  ? 32.42000  -0.10100  3.45500  1.000 23.67219 ? 96  HIS A CD2 1 
ATOM   724  C  CE1 . HIS A 1 96  ? 31.32200  1.13400   4.88800  1.000 22.91264 ? 96  HIS A CE1 1 
ATOM   725  N  NE2 . HIS A 1 96  ? 32.51800  0.66600   4.58700  1.000 21.98170 ? 96  HIS A NE2 1 
ATOM   726  N  N   . ALA A 1 97  ? 29.16200  -3.36800  0.38100  1.000 26.10906 ? 97  ALA A N   1 
ATOM   727  C  CA  . ALA A 1 97  ? 28.12200  -3.95600  -0.44700 1.000 25.51147 ? 97  ALA A CA  1 
ATOM   728  C  C   . ALA A 1 97  ? 27.22100  -4.84400  0.39400  1.000 26.84561 ? 97  ALA A C   1 
ATOM   729  O  O   . ALA A 1 97  ? 25.99200  -4.80200  0.25900  1.000 26.59332 ? 97  ALA A O   1 
ATOM   730  C  CB  . ALA A 1 97  ? 28.74400  -4.73400  -1.60000 1.000 24.43671 ? 97  ALA A CB  1 
ATOM   731  N  N   . ILE A 1 98  ? 27.82000  -5.63100  1.29500  1.000 26.38566 ? 98  ILE A N   1 
ATOM   732  C  CA  . ILE A 1 98  ? 27.04700  -6.48900  2.19300  1.000 25.95259 ? 98  ILE A CA  1 
ATOM   733  C  C   . ILE A 1 98  ? 26.15700  -5.64900  3.10100  1.000 26.43979 ? 98  ILE A C   1 
ATOM   734  O  O   . ILE A 1 98  ? 24.96700  -5.93900  3.27100  1.000 26.36739 ? 98  ILE A O   1 
ATOM   735  C  CB  . ILE A 1 98  ? 27.98800  -7.38300  3.02400  1.000 24.74642 ? 98  ILE A CB  1 
ATOM   736  C  CG1 . ILE A 1 98  ? 28.66500  -8.44800  2.16800  1.000 27.05874 ? 98  ILE A CG1 1 
ATOM   737  C  CG2 . ILE A 1 98  ? 27.23000  -8.02700  4.16800  1.000 23.83985 ? 98  ILE A CG2 1 
ATOM   738  C  CD1 . ILE A 1 98  ? 29.77000  -9.19500  2.90600  1.000 25.76922 ? 98  ILE A CD1 1 
ATOM   739  N  N   . CYS A 1 99  ? 26.73000  -4.59900  3.71300  1.000 26.92113 ? 99  CYS A N   1 
ATOM   740  C  CA  . CYS A 1 99  ? 25.98000  -3.75200  4.64200  1.000 25.29154 ? 99  CYS A CA  1 
ATOM   741  C  C   . CYS A 1 99  ? 24.83600  -3.03300  3.94300  1.000 25.63258 ? 99  CYS A C   1 
ATOM   742  O  O   . CYS A 1 99  ? 23.71500  -2.98500  4.46400  1.000 26.19866 ? 99  CYS A O   1 
ATOM   743  C  CB  . CYS A 1 99  ? 26.90300  -2.72800  5.30700  1.000 24.70869 ? 99  CYS A CB  1 
ATOM   744  S  SG  . CYS A 1 99  ? 28.07000  -3.34500  6.55500  1.000 22.54137 ? 99  CYS A SG  1 
ATOM   745  N  N   . GLU A 1 100 ? 25.09700  -2.46400  2.76500  1.000 26.51368 ? 100 GLU A N   1 
ATOM   746  C  CA  . GLU A 1 100 ? 24.05500  -1.71900  2.07300  1.000 26.38144 ? 100 GLU A CA  1 
ATOM   747  C  C   . GLU A 1 100 ? 22.89600  -2.63200  1.69400  1.000 27.31011 ? 100 GLU A C   1 
ATOM   748  O  O   . GLU A 1 100 ? 21.73100  -2.23100  1.77100  1.000 27.76377 ? 100 GLU A O   1 
ATOM   749  C  CB  . GLU A 1 100 ? 24.65200  -0.99700  0.85800  1.000 28.11812 ? 100 GLU A CB  1 
ATOM   750  C  CG  . GLU A 1 100 ? 25.22800  0.40700   1.21100  1.000 29.23870 ? 100 GLU A CG  1 
ATOM   751  C  CD  . GLU A 1 100 ? 26.42200  0.87200   0.34000  1.000 32.25425 ? 100 GLU A CD  1 
ATOM   752  O  OE1 . GLU A 1 100 ? 26.64800  0.30700   -0.75100 1.000 35.21398 ? 100 GLU A OE1 1 
ATOM   753  O  OE2 . GLU A 1 100 ? 27.14300  1.81500   0.75300  1.000 31.46655 ? 100 GLU A OE2 1 
ATOM   754  N  N   . ALA A 1 101 ? 23.18900  -3.88200  1.33500  1.000 27.66446 ? 101 ALA A N   1 
ATOM   755  C  CA  . ALA A 1 101 ? 22.12300  -4.83600  1.04400  1.000 27.46570 ? 101 ALA A CA  1 
ATOM   756  C  C   . ALA A 1 101 ? 21.41700  -5.28500  2.31500  1.000 27.88507 ? 101 ALA A C   1 
ATOM   757  O  O   . ALA A 1 101 ? 20.18900  -5.40700  2.34100  1.000 29.31072 ? 101 ALA A O   1 
ATOM   758  C  CB  . ALA A 1 101 ? 22.69100  -6.04300  0.30600  1.000 27.73332 ? 101 ALA A CB  1 
ATOM   759  N  N   . TYR A 1 102 ? 22.17900  -5.53400  3.37800  1.000 27.65699 ? 102 TYR A N   1 
ATOM   760  C  CA  . TYR A 1 102 ? 21.60500  -6.03400  4.62100  1.000 27.40180 ? 102 TYR A CA  1 
ATOM   761  C  C   . TYR A 1 102 ? 20.79500  -4.96100  5.33800  1.000 27.19243 ? 102 TYR A C   1 
ATOM   762  O  O   . TYR A 1 102 ? 19.73200  -5.24900  5.89700  1.000 27.91926 ? 102 TYR A O   1 
ATOM   763  C  CB  . TYR A 1 102 ? 22.73000  -6.56000  5.50600  1.000 26.63331 ? 102 TYR A CB  1 
ATOM   764  C  CG  . TYR A 1 102 ? 22.35200  -7.04400  6.89900  1.000 26.21581 ? 102 TYR A CG  1 
ATOM   765  C  CD1 . TYR A 1 102 ? 21.89400  -8.34200  7.09100  1.000 26.35964 ? 102 TYR A CD1 1 
ATOM   766  C  CD2 . TYR A 1 102 ? 22.50600  -6.19800  7.99500  1.000 25.66758 ? 102 TYR A CD2 1 
ATOM   767  C  CE1 . TYR A 1 102 ? 21.57900  -8.76000  8.35500  1.000 25.68858 ? 102 TYR A CE1 1 
ATOM   768  C  CE2 . TYR A 1 102 ? 22.17800  -6.65100  9.24500  1.000 24.72588 ? 102 TYR A CE2 1 
ATOM   769  C  CZ  . TYR A 1 102 ? 21.71400  -7.93700  9.45900  1.000 25.69012 ? 102 TYR A CZ  1 
ATOM   770  O  OH  . TYR A 1 102 ? 21.39600  -8.36600  10.69600 1.000 26.43659 ? 102 TYR A OH  1 
ATOM   771  N  N   . PHE A 1 103 ? 21.26900  -3.71700  5.32900  1.000 27.45307 ? 103 PHE A N   1 
ATOM   772  C  CA  . PHE A 1 103 ? 20.55000  -2.62300  5.96600  1.000 28.26991 ? 103 PHE A CA  1 
ATOM   773  C  C   . PHE A 1 103 ? 19.58800  -1.91300  5.01300  1.000 29.02505 ? 103 PHE A C   1 
ATOM   774  O  O   . PHE A 1 103 ? 19.17300  -0.78500  5.29100  1.000 29.32892 ? 103 PHE A O   1 
ATOM   775  C  CB  . PHE A 1 103 ? 21.53800  -1.62700  6.56500  1.000 25.77695 ? 103 PHE A CB  1 
ATOM   776  C  CG  . PHE A 1 103 ? 22.25800  -2.14400  7.78100  1.000 24.71665 ? 103 PHE A CG  1 
ATOM   777  C  CD1 . PHE A 1 103 ? 21.55700  -2.48800  8.92300  1.000 23.98529 ? 103 PHE A CD1 1 
ATOM   778  C  CD2 . PHE A 1 103 ? 23.63700  -2.25800  7.79000  1.000 23.45262 ? 103 PHE A CD2 1 
ATOM   779  C  CE1 . PHE A 1 103 ? 22.21200  -2.95000  10.03900 1.000 22.78424 ? 103 PHE A CE1 1 
ATOM   780  C  CE2 . PHE A 1 103 ? 24.29600  -2.71200  8.90900  1.000 22.04419 ? 103 PHE A CE2 1 
ATOM   781  C  CZ  . PHE A 1 103 ? 23.58100  -3.05700  10.03300 1.000 22.59837 ? 103 PHE A CZ  1 
ATOM   782  N  N   . GLN A 1 104 ? 19.21900  -2.56300  3.90900  1.000 31.52894 ? 104 GLN A N   1 
ATOM   783  C  CA  . GLN A 1 104 ? 18.35700  -1.95100  2.90600  1.000 31.88485 ? 104 GLN A CA  1 
ATOM   784  C  C   . GLN A 1 104 ? 17.09600  -1.36800  3.53600  1.000 33.59102 ? 104 GLN A C   1 
ATOM   785  O  O   . GLN A 1 104 ? 16.73300  -0.21600  3.27800  1.000 35.62878 ? 104 GLN A O   1 
ATOM   786  C  CB  . GLN A 1 104 ? 18.00900  -2.99700  1.84600  1.000 32.29674 ? 104 GLN A CB  1 
ATOM   787  C  CG  . GLN A 1 104 ? 18.14800  -2.52400  0.41200  1.000 36.65304 ? 104 GLN A CG  1 
ATOM   788  C  CD  . GLN A 1 104 ? 16.85100  -1.96100  -0.13900 1.000 44.84161 ? 104 GLN A CD  1 
ATOM   789  O  OE1 . GLN A 1 104 ? 15.81100  -2.02400  0.51700  1.000 45.18520 ? 104 GLN A OE1 1 
ATOM   790  N  NE2 . GLN A 1 104 ? 16.90300  -1.41300  -1.35200 1.000 46.24303 ? 104 GLN A NE2 1 
ATOM   791  N  N   . ARG A 1 105 ? 16.43900  -2.14400  4.40000  1.000 32.39270 ? 105 ARG A N   1 
ATOM   792  C  CA  . ARG A 1 105 ? 15.17100  -1.75100  5.01100  1.000 30.62804 ? 105 ARG A CA  1 
ATOM   793  C  C   . ARG A 1 105 ? 15.31300  -0.71200  6.11300  1.000 28.88645 ? 105 ARG A C   1 
ATOM   794  O  O   . ARG A 1 105 ? 14.35800  0.02400   6.36700  1.000 28.72372 ? 105 ARG A O   1 
ATOM   795  C  CB  . ARG A 1 105 ? 14.46200  -2.97700  5.58900  1.000 31.03152 ? 105 ARG A CB  1 
ATOM   796  C  CG  . ARG A 1 105 ? 14.03700  -3.99300  4.54200  1.000 33.32300 ? 105 ARG A CG  1 
ATOM   797  C  CD  . ARG A 1 105 ? 13.56100  -5.29400  5.17700  1.000 35.02993 ? 105 ARG A CD  1 
ATOM   798  N  NE  . ARG A 1 105 ? 12.39000  -5.09600  6.02400  1.000 34.12980 ? 105 ARG A NE  1 
ATOM   799  C  CZ  . ARG A 1 105 ? 11.86600  -6.03100  6.80400  1.000 33.26992 ? 105 ARG A CZ  1 
ATOM   800  N  NH1 . ARG A 1 105 ? 12.37800  -7.25100  6.86300  1.000 35.32739 ? 105 ARG A NH1 1 
ATOM   801  N  NH2 . ARG A 1 105 ? 10.80200  -5.73500  7.54700  1.000 34.40999 ? 105 ARG A NH2 1 
ATOM   802  N  N   . THR A 1 106 ? 16.45700  -0.63300  6.78600  1.000 28.23326 ? 106 THR A N   1 
ATOM   803  C  CA  . THR A 1 106 ? 16.60100  0.31700   7.88000  1.000 27.55160 ? 106 THR A CA  1 
ATOM   804  C  C   . THR A 1 106 ? 17.22600  1.63800   7.45300  1.000 26.91811 ? 106 THR A C   1 
ATOM   805  O  O   . THR A 1 106 ? 17.17700  2.60100   8.22200  1.000 26.09532 ? 106 THR A O   1 
ATOM   806  C  CB  . THR A 1 106 ? 17.42800  -0.29300  9.01800  1.000 26.83768 ? 106 THR A CB  1 
ATOM   807  O  OG1 . THR A 1 106 ? 17.20400  0.44300   10.22800 1.000 27.10371 ? 106 THR A OG1 1 
ATOM   808  C  CG2 . THR A 1 106 ? 18.89800  -0.24700  8.68600  1.000 25.52644 ? 106 THR A CG2 1 
ATOM   809  N  N   . GLY A 1 107 ? 17.79100  1.71900   6.25000  1.000 26.24100 ? 107 GLY A N   1 
ATOM   810  C  CA  . GLY A 1 107 ? 18.46800  2.92600   5.83300  1.000 24.95600 ? 107 GLY A CA  1 
ATOM   811  C  C   . GLY A 1 107 ? 19.92900  2.91200   6.23900  1.000 24.77747 ? 107 GLY A C   1 
ATOM   812  O  O   . GLY A 1 107 ? 20.56800  1.85200   6.24200  1.000 24.66882 ? 107 GLY A O   1 
ATOM   813  N  N   . ASP A 1 108 ? 20.45700  4.07600   6.60700  1.000 23.46589 ? 108 ASP A N   1 
ATOM   814  C  CA  . ASP A 1 108 ? 21.88700  4.22600   6.83800  1.000 22.53865 ? 108 ASP A CA  1 
ATOM   815  C  C   . ASP A 1 108 ? 22.35000  3.44700   8.06600  1.000 21.34960 ? 108 ASP A C   1 
ATOM   816  O  O   . ASP A 1 108 ? 21.64000  3.32000   9.06100  1.000 20.88357 ? 108 ASP A O   1 
ATOM   817  C  CB  . ASP A 1 108 ? 22.24700  5.70500   7.01000  1.000 22.77205 ? 108 ASP A CB  1 
ATOM   818  C  CG  . ASP A 1 108 ? 22.11400  6.49900   5.72400  1.000 23.27139 ? 108 ASP A CG  1 
ATOM   819  O  OD1 . ASP A 1 108 ? 21.94200  5.88000   4.65900  1.000 23.71965 ? 108 ASP A OD1 1 
ATOM   820  O  OD2 . ASP A 1 108 ? 22.18100  7.74300   5.77800  1.000 23.11281 ? 108 ASP A OD2 1 
ATOM   821  N  N   . TYR A 1 109 ? 23.57100  2.94400   7.98600  1.000 20.91187 ? 109 TYR A N   1 
ATOM   822  C  CA  . TYR A 1 109 ? 24.26100  2.26800   9.07200  1.000 20.28491 ? 109 TYR A CA  1 
ATOM   823  C  C   . TYR A 1 109 ? 25.56400  3.02000   9.32000  1.000 20.79283 ? 109 TYR A C   1 
ATOM   824  O  O   . TYR A 1 109 ? 26.05000  3.74300   8.44300  1.000 20.88573 ? 109 TYR A O   1 
ATOM   825  C  CB  . TYR A 1 109 ? 24.56000  0.80600   8.70600  1.000 20.48751 ? 109 TYR A CB  1 
ATOM   826  C  CG  . TYR A 1 109 ? 25.45300  0.72400   7.47700  1.000 20.95499 ? 109 TYR A CG  1 
ATOM   827  C  CD1 . TYR A 1 109 ? 24.89800  0.78000   6.20000  1.000 22.53345 ? 109 TYR A CD1 1 
ATOM   828  C  CD2 . TYR A 1 109 ? 26.83500  0.64200   7.61900  1.000 20.95803 ? 109 TYR A CD2 1 
ATOM   829  C  CE1 . TYR A 1 109 ? 25.72200  0.74100   5.10400  1.000 22.87483 ? 109 TYR A CE1 1 
ATOM   830  C  CE2 . TYR A 1 109 ? 27.62600  0.60400   6.50000  1.000 21.16769 ? 109 TYR A CE2 1 
ATOM   831  C  CZ  . TYR A 1 109 ? 27.10000  0.66100   5.22000  1.000 22.66951 ? 109 TYR A CZ  1 
ATOM   832  O  OH  . TYR A 1 109 ? 27.90500  0.62900   4.13900  1.000 23.23272 ? 109 TYR A OH  1 
ATOM   833  N  N   . TRP A 1 110 ? 26.12600  2.87400   10.51900 1.000 19.40264 ? 110 TRP A N   1 
ATOM   834  C  CA  . TRP A 1 110 ? 27.45200  3.40800   10.78800 1.000 18.88935 ? 110 TRP A CA  1 
ATOM   835  C  C   . TRP A 1 110 ? 28.14700  2.48100   11.77300 1.000 19.09755 ? 110 TRP A C   1 
ATOM   836  O  O   . TRP A 1 110 ? 27.59600  1.45600   12.17100 1.000 18.94618 ? 110 TRP A O   1 
ATOM   837  C  CB  . TRP A 1 110 ? 27.38900  4.86800   11.26300 1.000 19.02283 ? 110 TRP A CB  1 
ATOM   838  C  CG  . TRP A 1 110 ? 26.51200  5.18200   12.46500 1.000 19.06521 ? 110 TRP A CG  1 
ATOM   839  C  CD1 . TRP A 1 110 ? 25.95100  4.29900   13.35600 1.000 18.49645 ? 110 TRP A CD1 1 
ATOM   840  C  CD2 . TRP A 1 110 ? 26.10000  6.49000   12.88900 1.000 18.68535 ? 110 TRP A CD2 1 
ATOM   841  N  NE1 . TRP A 1 110 ? 25.22800  4.98200   14.31100 1.000 17.93277 ? 110 TRP A NE1 1 
ATOM   842  C  CE2 . TRP A 1 110 ? 25.30500  6.32600   14.04500 1.000 17.84151 ? 110 TRP A CE2 1 
ATOM   843  C  CE3 . TRP A 1 110 ? 26.33800  7.78600   12.40700 1.000 18.34841 ? 110 TRP A CE3 1 
ATOM   844  C  CZ2 . TRP A 1 110 ? 24.73500  7.41400   14.71900 1.000 18.75510 ? 110 TRP A CZ2 1 
ATOM   845  C  CZ3 . TRP A 1 110 ? 25.77700  8.85900   13.07600 1.000 18.02923 ? 110 TRP A CZ3 1 
ATOM   846  C  CH2 . TRP A 1 110 ? 24.98600  8.66800   14.22400 1.000 18.02050 ? 110 TRP A CH2 1 
ATOM   847  N  N   . LEU A 1 111 ? 29.37900  2.83200   12.14600 1.000 19.06057 ? 111 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 111 ? 30.21400  1.99000   13.00000 1.000 18.58030 ? 111 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 111 ? 29.91400  2.27100   14.46500 1.000 18.83293 ? 111 LEU A C   1 
ATOM   850  O  O   . LEU A 1 111 ? 30.15900  3.38300   14.94800 1.000 19.17480 ? 111 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 111 ? 31.69900  2.22600   12.72300 1.000 18.45550 ? 111 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 111 ? 32.64500  1.29500   13.47800 1.000 17.50118 ? 111 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 111 ? 32.56700  -0.08000  12.87000 1.000 18.67082 ? 111 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 111 ? 34.07800  1.81700   13.45600 1.000 17.86227 ? 111 LEU A CD2 1 
ATOM   855  N  N   . SER A 1 112 ? 29.40400  1.26500   15.18100 1.000 18.49805 ? 112 SER A N   1 
ATOM   856  C  CA  . SER A 1 112 ? 29.17200  1.45700   16.60900 1.000 18.60091 ? 112 SER A CA  1 
ATOM   857  C  C   . SER A 1 112 ? 30.44100  1.23200   17.42800 1.000 19.79163 ? 112 SER A C   1 
ATOM   858  O  O   . SER A 1 112 ? 30.63900  1.89700   18.45000 1.000 20.89197 ? 112 SER A O   1 
ATOM   859  C  CB  . SER A 1 112 ? 28.06000  0.53700   17.09700 1.000 19.50679 ? 112 SER A CB  1 
ATOM   860  O  OG  . SER A 1 112 ? 27.85000  0.71900   18.47900 1.000 17.96019 ? 112 SER A OG  1 
ATOM   861  N  N   . ALA A 1 113 ? 31.31300  0.32500   16.99900 1.000 19.18885 ? 113 ALA A N   1 
ATOM   862  C  CA  . ALA A 1 113 ? 32.57200  0.08000   17.68000 1.000 19.59711 ? 113 ALA A CA  1 
ATOM   863  C  C   . ALA A 1 113 ? 33.44100  -0.78800  16.79000 1.000 19.68917 ? 113 ALA A C   1 
ATOM   864  O  O   . ALA A 1 113 ? 32.93600  -1.52500  15.94300 1.000 19.53876 ? 113 ALA A O   1 
ATOM   865  C  CB  . ALA A 1 113 ? 32.35600  -0.60500  19.03100 1.000 20.51011 ? 113 ALA A CB  1 
ATOM   866  N  N   . ALA A 1 114 ? 34.74800  -0.68500  16.99000 1.000 19.70868 ? 114 ALA A N   1 
ATOM   867  C  CA  . ALA A 1 114 ? 35.70000  -1.60700  16.38700 1.000 20.24111 ? 114 ALA A CA  1 
ATOM   868  C  C   . ALA A 1 114 ? 36.91200  -1.66200  17.29800 1.000 20.77500 ? 114 ALA A C   1 
ATOM   869  O  O   . ALA A 1 114 ? 37.49700  -0.62400  17.60900 1.000 21.77369 ? 114 ALA A O   1 
ATOM   870  C  CB  . ALA A 1 114 ? 36.10100  -1.17600  14.98500 1.000 20.09833 ? 114 ALA A CB  1 
ATOM   871  N  N   . PHE A 1 115 ? 37.28100  -2.86500  17.72400 1.000 21.71517 ? 115 PHE A N   1 
ATOM   872  C  CA  . PHE A 1 115 ? 38.28600  -3.04900  18.75600 1.000 21.64016 ? 115 PHE A CA  1 
ATOM   873  C  C   . PHE A 1 115 ? 38.98700  -4.37800  18.53600 1.000 23.02086 ? 115 PHE A C   1 
ATOM   874  O  O   . PHE A 1 115 ? 38.47000  -5.27400  17.86600 1.000 24.76018 ? 115 PHE A O   1 
ATOM   875  C  CB  . PHE A 1 115 ? 37.66000  -3.02300  20.14700 1.000 21.31405 ? 115 PHE A CB  1 
ATOM   876  C  CG  . PHE A 1 115 ? 36.56000  -4.03600  20.32400 1.000 21.97387 ? 115 PHE A CG  1 
ATOM   877  C  CD1 . PHE A 1 115 ? 35.26600  -3.75800  19.90900 1.000 22.77637 ? 115 PHE A CD1 1 
ATOM   878  C  CD2 . PHE A 1 115 ? 36.82200  -5.26800  20.90500 1.000 23.27722 ? 115 PHE A CD2 1 
ATOM   879  C  CE1 . PHE A 1 115 ? 34.25300  -4.68500  20.06800 1.000 23.29416 ? 115 PHE A CE1 1 
ATOM   880  C  CE2 . PHE A 1 115 ? 35.81400  -6.20300  21.06800 1.000 25.10799 ? 115 PHE A CE2 1 
ATOM   881  C  CZ  . PHE A 1 115 ? 34.52700  -5.90800  20.64500 1.000 24.52552 ? 115 PHE A CZ  1 
ATOM   882  N  N   . LEU A 1 116 ? 40.15800  -4.50700  19.14200 1.000 23.86243 ? 116 LEU A N   1 
ATOM   883  C  CA  . LEU A 1 116 ? 40.94400  -5.72700  19.08100 1.000 23.32537 ? 116 LEU A CA  1 
ATOM   884  C  C   . LEU A 1 116 ? 40.68500  -6.58900  20.30900 1.000 23.84463 ? 116 LEU A C   1 
ATOM   885  O  O   . LEU A 1 116 ? 40.64200  -6.08300  21.43200 1.000 24.13245 ? 116 LEU A O   1 
ATOM   886  C  CB  . LEU A 1 116 ? 42.43100  -5.39400  19.00000 1.000 23.67612 ? 116 LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 116 ? 43.40200  -6.57300  19.01400 1.000 24.20244 ? 116 LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 116 ? 43.29100  -7.36900  17.72200 1.000 25.11395 ? 116 LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 116 ? 44.82600  -6.09800  19.24100 1.000 25.21651 ? 116 LEU A CD2 1 
ATOM   890  N  N   . ARG A 1 117 ? 40.51400  -7.89400  20.08700 1.000 25.81623 ? 117 ARG A N   1 
ATOM   891  C  CA  . ARG A 1 117 ? 40.63800  -8.91300  21.12700 1.000 27.19310 ? 117 ARG A CA  1 
ATOM   892  C  C   . ARG A 1 117 ? 41.87600  -9.76300  20.84200 1.000 26.70451 ? 117 ARG A C   1 
ATOM   893  O  O   . ARG A 1 117 ? 42.06300  -10.24000 19.71800 1.000 26.64958 ? 117 ARG A O   1 
ATOM   894  C  CB  . ARG A 1 117 ? 39.38600  -9.79500  21.19900 1.000 27.82123 ? 117 ARG A CB  1 
ATOM   895  C  CG  . ARG A 1 117 ? 38.36700  -9.38300  22.24700 1.000 28.01483 ? 117 ARG A CG  1 
ATOM   896  C  CD  . ARG A 1 117 ? 37.08100  -10.19900 22.14000 1.000 30.39817 ? 117 ARG A CD  1 
ATOM   897  N  NE  . ARG A 1 117 ? 37.29800  -11.59500 21.77800 1.000 30.41694 ? 117 ARG A NE  1 
ATOM   898  C  CZ  . ARG A 1 117 ? 37.33600  -12.61200 22.62900 1.000 30.47628 ? 117 ARG A CZ  1 
ATOM   899  N  NH1 . ARG A 1 117 ? 37.27400  -12.42900 23.93900 1.000 29.74596 ? 117 ARG A NH1 1 
ATOM   900  N  NH2 . ARG A 1 117 ? 37.43200  -13.84500 22.15100 1.000 31.12594 ? 117 ARG A NH2 1 
ATOM   901  N  N   . GLU A 1 118 ? 42.72900  -9.92600  21.85200 1.000 28.01296 ? 118 GLU A N   1 
ATOM   902  C  CA  . GLU A 1 118 ? 43.92900  -10.75000 21.75300 1.000 30.21021 ? 118 GLU A CA  1 
ATOM   903  C  C   . GLU A 1 118 ? 43.91200  -11.75200 22.89600 1.000 31.62225 ? 118 GLU A C   1 
ATOM   904  O  O   . GLU A 1 118 ? 44.14700  -11.38600 24.05100 1.000 32.36574 ? 118 GLU A O   1 
ATOM   905  C  CB  . GLU A 1 118 ? 45.19200  -9.90300  21.80100 1.000 29.44755 ? 118 GLU A CB  1 
ATOM   906  C  CG  . GLU A 1 118 ? 46.43400  -10.70700 21.55500 1.000 30.79983 ? 118 GLU A CG  1 
ATOM   907  C  CD  . GLU A 1 118 ? 47.68900  -9.90300  21.75400 1.000 31.47356 ? 118 GLU A CD  1 
ATOM   908  O  OE1 . GLU A 1 118 ? 48.08500  -9.67000  22.91700 1.000 32.33202 ? 118 GLU A OE1 1 
ATOM   909  O  OE2 . GLU A 1 118 ? 48.27900  -9.50400  20.73900 1.000 32.19611 ? 118 GLU A OE2 1 
ATOM   910  N  N   . ILE A 1 119 ? 43.65000  -13.01100 22.58400 1.000 31.63115 ? 119 ILE A N   1 
ATOM   911  C  CA  . ILE A 1 119 ? 43.28700  -13.99400 23.59700 1.000 35.23329 ? 119 ILE A CA  1 
ATOM   912  C  C   . ILE A 1 119 ? 44.48700  -14.88200 23.87200 1.000 38.85769 ? 119 ILE A C   1 
ATOM   913  O  O   . ILE A 1 119 ? 45.08400  -15.44200 22.94300 1.000 39.22661 ? 119 ILE A O   1 
ATOM   914  C  CB  . ILE A 1 119 ? 42.06900  -14.82300 23.15800 1.000 35.68734 ? 119 ILE A CB  1 
ATOM   915  C  CG1 . ILE A 1 119 ? 40.89000  -13.90900 22.83000 1.000 31.20630 ? 119 ILE A CG1 1 
ATOM   916  C  CG2 . ILE A 1 119 ? 41.67900  -15.80500 24.24100 1.000 38.54190 ? 119 ILE A CG2 1 
ATOM   917  C  CD1 . ILE A 1 119 ? 40.78000  -13.56200 21.36300 1.000 29.98009 ? 119 ILE A CD1 1 
ATOM   918  N  N   . GLU A 1 120 ? 44.82800  -14.99000 25.14100 1.000 46.15269 ? 120 GLU A N   1 
ATOM   919  C  CA  . GLU A 1 120 ? 46.07000  -15.70200 25.51100 1.000 48.42886 ? 120 GLU A CA  1 
ATOM   920  C  C   . GLU A 1 120 ? 45.82400  -17.19100 25.74800 1.000 50.24965 ? 120 GLU A C   1 
ATOM   921  O  O   . GLU A 1 120 ? 44.77400  -17.55800 26.24100 1.000 51.59926 ? 120 GLU A O   1 
ATOM   922  C  CB  . GLU A 1 120 ? 46.69400  -15.10700 26.77200 1.000 49.48834 ? 120 GLU A CB  1 
ATOM   923  C  CG  . GLU A 1 120 ? 48.20700  -14.98100 26.63400 1.000 49.56540 ? 120 GLU A CG  1 
ATOM   924  C  CD  . GLU A 1 120 ? 48.96500  -14.21100 27.69200 1.000 53.24001 ? 120 GLU A CD  1 
ATOM   925  O  OE1 . GLU A 1 120 ? 48.38900  -13.80300 28.71700 1.000 56.53444 ? 120 GLU A OE1 1 
ATOM   926  O  OE2 . GLU A 1 120 ? 50.16700  -14.03200 27.46600 1.000 56.68867 ? 120 GLU A OE2 1 
ATOM   927  N  N   . SER A 1 121 ? 46.83100  -17.98900 25.46400 1.000 49.11232 ? 121 SER A N   1 
ATOM   928  C  CA  . SER A 1 121 ? 46.72700  -19.43100 25.65000 1.000 47.19450 ? 121 SER A CA  1 
ATOM   929  C  C   . SER A 1 121 ? 46.28900  -19.74800 27.07100 1.000 47.41062 ? 121 SER A C   1 
ATOM   930  O  O   . SER A 1 121 ? 46.68600  -19.07800 28.02700 1.000 49.26364 ? 121 SER A O   1 
ATOM   931  C  CB  . SER A 1 121 ? 48.06100  -20.10100 25.34800 1.000 43.86207 ? 121 SER A CB  1 
ATOM   932  O  OG  . SER A 1 121 ? 49.06300  -19.57500 26.18800 1.000 49.61688 ? 121 SER A OG  1 
ATOM   933  N  N   . GLY A 1 122 ? 45.43600  -20.75700 27.19900 1.000 47.88514 ? 122 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 122 ? 44.88000  -21.11400 28.48300 1.000 49.48257 ? 122 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 122 ? 43.73600  -20.24800 28.95100 1.000 48.58699 ? 122 GLY A C   1 
ATOM   936  O  O   . GLY A 1 122 ? 43.27200  -20.42600 30.08200 1.000 48.21213 ? 122 GLY A O   1 
ATOM   937  N  N   . MET A 1 123 ? 43.28300  -19.30600 28.14600 1.000 50.51399 ? 123 MET A N   1 
ATOM   938  C  CA  . MET A 1 123 ? 42.06300  -18.63800 28.55400 1.000 48.33312 ? 123 MET A CA  1 
ATOM   939  C  C   . MET A 1 123 ? 40.87300  -19.51000 28.17900 1.000 49.48811 ? 123 MET A C   1 
ATOM   940  O  O   . MET A 1 123 ? 40.91400  -20.22100 27.17100 1.000 48.69010 ? 123 MET A O   1 
ATOM   941  C  CB  . MET A 1 123 ? 41.94300  -17.27200 27.90100 1.000 48.04712 ? 123 MET A CB  1 
ATOM   942  C  CG  . MET A 1 123 ? 43.07600  -16.31900 28.27000 1.000 47.82700 ? 123 MET A CG  1 
ATOM   943  S  SD  . MET A 1 123 ? 43.50900  -16.34900 30.02200 1.000 57.91276 ? 123 MET A SD  1 
ATOM   944  C  CE  . MET A 1 123 ? 45.22300  -16.89900 29.96900 1.000 50.66012 ? 123 MET A CE  1 
ATOM   945  N  N   . PRO A 1 124 ? 39.82100  -19.50600 28.99200 1.000 45.52263 ? 124 PRO A N   1 
ATOM   946  C  CA  . PRO A 1 124 ? 38.67600  -20.37200 28.72000 1.000 45.54761 ? 124 PRO A CA  1 
ATOM   947  C  C   . PRO A 1 124 ? 37.78600  -19.76600 27.64900 1.000 46.14335 ? 124 PRO A C   1 
ATOM   948  O  O   . PRO A 1 124 ? 37.87600  -18.58100 27.32400 1.000 45.75387 ? 124 PRO A O   1 
ATOM   949  C  CB  . PRO A 1 124 ? 37.95800  -20.43000 30.06900 1.000 44.63692 ? 124 PRO A CB  1 
ATOM   950  C  CG  . PRO A 1 124 ? 38.23000  -19.10200 30.66200 1.000 41.52753 ? 124 PRO A CG  1 
ATOM   951  C  CD  . PRO A 1 124 ? 39.61900  -18.71100 30.21600 1.000 43.19720 ? 124 PRO A CD  1 
ATOM   952  N  N   . ALA A 1 125 ? 36.91100  -20.60900 27.10500 1.000 48.04676 ? 125 ALA A N   1 
ATOM   953  C  CA  . ALA A 1 125 ? 36.02900  -20.17700 26.03000 1.000 46.74349 ? 125 ALA A CA  1 
ATOM   954  C  C   . ALA A 1 125 ? 35.06300  -19.10100 26.52000 1.000 46.63254 ? 125 ALA A C   1 
ATOM   955  O  O   . ALA A 1 125 ? 34.70700  -19.03800 27.70100 1.000 46.96641 ? 125 ALA A O   1 
ATOM   956  C  CB  . ALA A 1 125 ? 35.25600  -21.37000 25.46200 1.000 43.88994 ? 125 ALA A CB  1 
ATOM   957  N  N   . GLN A 1 126 ? 34.66400  -18.23000 25.59800 1.000 40.42007 ? 126 GLN A N   1 
ATOM   958  C  CA  . GLN A 1 126 ? 33.62700  -17.25500 25.88500 1.000 38.51362 ? 126 GLN A CA  1 
ATOM   959  C  C   . GLN A 1 126 ? 32.27800  -17.96600 26.01300 1.000 38.38567 ? 126 GLN A C   1 
ATOM   960  O  O   . GLN A 1 126 ? 32.07400  -19.03600 25.43500 1.000 39.25321 ? 126 GLN A O   1 
ATOM   961  C  CB  . GLN A 1 126 ? 33.56500  -16.21400 24.76800 1.000 37.34924 ? 126 GLN A CB  1 
ATOM   962  C  CG  . GLN A 1 126 ? 33.44500  -14.76400 25.19800 1.000 35.14257 ? 126 GLN A CG  1 
ATOM   963  C  CD  . GLN A 1 126 ? 33.28900  -13.83600 24.01100 1.000 33.15668 ? 126 GLN A CD  1 
ATOM   964  O  OE1 . GLN A 1 126 ? 32.80000  -14.24300 22.95500 1.000 31.99892 ? 126 GLN A OE1 1 
ATOM   965  N  NE2 . GLN A 1 126 ? 33.71300  -12.58700 24.17200 1.000 32.56241 ? 126 GLN A NE2 1 
ATOM   966  N  N   . PRO A 1 127 ? 31.34300  -17.40400 26.77700 1.000 38.17468 ? 127 PRO A N   1 
ATOM   967  C  CA  . PRO A 1 127 ? 29.98200  -17.95200 26.80200 1.000 36.69896 ? 127 PRO A CA  1 
ATOM   968  C  C   . PRO A 1 127 ? 29.13800  -17.47600 25.63000 1.000 33.62406 ? 127 PRO A C   1 
ATOM   969  O  O   . PRO A 1 127 ? 29.25500  -16.34500 25.15700 1.000 34.32668 ? 127 PRO A O   1 
ATOM   970  C  CB  . PRO A 1 127 ? 29.41200  -17.42800 28.12400 1.000 35.17463 ? 127 PRO A CB  1 
ATOM   971  C  CG  . PRO A 1 127 ? 30.16300  -16.18900 28.37700 1.000 36.09071 ? 127 PRO A CG  1 
ATOM   972  C  CD  . PRO A 1 127 ? 31.55000  -16.40100 27.83500 1.000 37.87878 ? 127 PRO A CD  1 
ATOM   973  N  N   . PHE A 1 128 ? 28.26100  -18.37100 25.18000 1.000 34.00304 ? 128 PHE A N   1 
ATOM   974  C  CA  . PHE A 1 128 ? 27.40100  -18.13000 24.03100 1.000 32.09363 ? 128 PHE A CA  1 
ATOM   975  C  C   . PHE A 1 128 ? 26.48100  -16.94200 24.23700 1.000 32.44793 ? 128 PHE A C   1 
ATOM   976  O  O   . PHE A 1 128 ? 25.49300  -17.04500 24.96800 1.000 33.10202 ? 128 PHE A O   1 
ATOM   977  C  CB  . PHE A 1 128 ? 26.55400  -19.35800 23.74300 1.000 31.78933 ? 128 PHE A CB  1 
ATOM   978  C  CG  . PHE A 1 128 ? 27.31900  -20.48800 23.16500 1.000 32.59639 ? 128 PHE A CG  1 
ATOM   979  C  CD1 . PHE A 1 128 ? 27.82400  -20.40100 21.88100 1.000 32.04702 ? 128 PHE A CD1 1 
ATOM   980  C  CD2 . PHE A 1 128 ? 27.53300  -21.63500 23.89600 1.000 32.33482 ? 128 PHE A CD2 1 
ATOM   981  C  CE1 . PHE A 1 128 ? 28.53000  -21.43700 21.34200 1.000 32.41140 ? 128 PHE A CE1 1 
ATOM   982  C  CE2 . PHE A 1 128 ? 28.23200  -22.67700 23.35800 1.000 33.99445 ? 128 PHE A CE2 1 
ATOM   983  C  CZ  . PHE A 1 128 ? 28.72900  -22.58100 22.07800 1.000 33.34676 ? 128 PHE A CZ  1 
ATOM   984  N  N   . HIS A 1 129 ? 26.76500  -15.82900 23.57100 1.000 33.60209 ? 129 HIS A N   1 
ATOM   985  C  CA  . HIS A 1 129 ? 25.97100  -14.62300 23.71800 1.000 32.49236 ? 129 HIS A CA  1 
ATOM   986  C  C   . HIS A 1 129 ? 25.39900  -14.18800 22.37600 1.000 31.56037 ? 129 HIS A C   1 
ATOM   987  O  O   . HIS A 1 129 ? 25.82900  -14.62800 21.30500 1.000 31.22336 ? 129 HIS A O   1 
ATOM   988  C  CB  . HIS A 1 129 ? 26.81600  -13.49100 24.30000 1.000 31.15530 ? 129 HIS A CB  1 
ATOM   989  C  CG  . HIS A 1 129 ? 27.98400  -13.13500 23.44800 1.000 30.71224 ? 129 HIS A CG  1 
ATOM   990  N  ND1 . HIS A 1 129 ? 29.16500  -13.83600 23.47800 1.000 31.26934 ? 129 HIS A ND1 1 
ATOM   991  C  CD2 . HIS A 1 129 ? 28.14100  -12.17500 22.50900 1.000 32.49832 ? 129 HIS A CD2 1 
ATOM   992  C  CE1 . HIS A 1 129 ? 30.00800  -13.31400 22.60600 1.000 31.85720 ? 129 HIS A CE1 1 
ATOM   993  N  NE2 . HIS A 1 129 ? 29.41200  -12.30100 22.00600 1.000 31.69826 ? 129 HIS A NE2 1 
ATOM   994  N  N   . ARG A 1 130 ? 24.41200  -13.31600 22.45000 1.000 32.12955 ? 130 ARG A N   1 
ATOM   995  C  CA  . ARG A 1 130 ? 24.00700  -12.51700 21.31000 1.000 33.96591 ? 130 ARG A CA  1 
ATOM   996  C  C   . ARG A 1 130 ? 24.62300  -11.13000 21.45800 1.000 35.08826 ? 130 ARG A C   1 
ATOM   997  O  O   . ARG A 1 130 ? 24.83800  -10.64500 22.57100 1.000 36.24724 ? 130 ARG A O   1 
ATOM   998  C  CB  . ARG A 1 130 ? 22.47900  -12.44000 21.21400 1.000 34.08470 ? 130 ARG A CB  1 
ATOM   999  C  CG  . ARG A 1 130 ? 21.84600  -13.64600 20.57300 1.000 30.88844 ? 130 ARG A CG  1 
ATOM   1000 C  CD  . ARG A 1 130 ? 20.33800  -13.63500 20.73300 1.000 32.96261 ? 130 ARG A CD  1 
ATOM   1001 N  NE  . ARG A 1 130 ? 19.70000  -14.74500 20.03400 1.000 32.96293 ? 130 ARG A NE  1 
ATOM   1002 C  CZ  . ARG A 1 130 ? 18.41100  -15.05400 20.12700 1.000 33.61510 ? 130 ARG A CZ  1 
ATOM   1003 N  NH1 . ARG A 1 130 ? 17.59500  -14.39200 20.93100 1.000 34.14373 ? 130 ARG A NH1 1 
ATOM   1004 N  NH2 . ARG A 1 130 ? 17.92800  -16.04300 19.38400 1.000 32.50590 ? 130 ARG A NH2 1 
ATOM   1005 N  N   . ASP A 1 131 ? 24.94200  -10.49800 20.33300 1.000 32.76131 ? 131 ASP A N   1 
ATOM   1006 C  CA  . ASP A 1 131 ? 25.51200  -9.15800  20.41300 1.000 32.73611 ? 131 ASP A CA  1 
ATOM   1007 C  C   . ASP A 1 131 ? 24.43300  -8.09500  20.59900 1.000 36.80202 ? 131 ASP A C   1 
ATOM   1008 O  O   . ASP A 1 131 ? 24.57300  -6.98000  20.09500 1.000 36.57701 ? 131 ASP A O   1 
ATOM   1009 C  CB  . ASP A 1 131 ? 26.33000  -8.84500  19.16700 1.000 31.08075 ? 131 ASP A CB  1 
ATOM   1010 C  CG  . ASP A 1 131 ? 27.67700  -9.53400  19.16200 1.000 30.07942 ? 131 ASP A CG  1 
ATOM   1011 O  OD1 . ASP A 1 131 ? 28.06200  -10.16500 20.17700 1.000 31.35542 ? 131 ASP A OD1 1 
ATOM   1012 O  OD2 . ASP A 1 131 ? 28.36700  -9.43700  18.13400 1.000 28.88228 ? 131 ASP A OD2 1 
ATOM   1013 N  N   . ASP A 1 132 ? 23.36400  -8.42300  21.32600 1.000 49.07034 ? 132 ASP A N   1 
ATOM   1014 C  CA  . ASP A 1 132 ? 22.25500  -7.51300  21.59200 1.000 48.30583 ? 132 ASP A CA  1 
ATOM   1015 C  C   . ASP A 1 132 ? 22.27700  -7.03300  23.04200 1.000 49.28237 ? 132 ASP A C   1 
ATOM   1016 O  O   . ASP A 1 132 ? 21.24500  -6.95800  23.71000 1.000 51.06596 ? 132 ASP A O   1 
ATOM   1017 C  CB  . ASP A 1 132 ? 20.90300  -8.15000  21.22200 1.000 48.05957 ? 132 ASP A CB  1 
ATOM   1018 C  CG  . ASP A 1 132 ? 20.47000  -9.32600  22.12800 1.000 49.94734 ? 132 ASP A CG  1 
ATOM   1019 O  OD1 . ASP A 1 132 ? 21.09700  -9.60100  23.17200 1.000 52.72088 ? 132 ASP A OD1 1 
ATOM   1020 O  OD2 . ASP A 1 132 ? 19.46100  -9.99000  21.77800 1.000 50.12567 ? 132 ASP A OD2 1 
ATOM   1021 N  N   . ALA A 1 133 ? 23.46500  -6.70900  23.54800 1.000 38.37310 ? 133 ALA A N   1 
ATOM   1022 C  CA  . ALA A 1 133 ? 23.63100  -6.23100  24.91600 1.000 34.62490 ? 133 ALA A CA  1 
ATOM   1023 C  C   . ALA A 1 133 ? 23.99600  -4.75700  25.00000 1.000 30.57595 ? 133 ALA A C   1 
ATOM   1024 O  O   . ALA A 1 133 ? 23.56900  -4.08000  25.93400 1.000 30.24858 ? 133 ALA A O   1 
ATOM   1025 C  CB  . ALA A 1 133 ? 24.69700  -7.05900  25.64600 1.000 34.55609 ? 133 ALA A CB  1 
ATOM   1026 N  N   . THR A 1 134 ? 24.77800  -4.24100  24.04700 1.000 28.57708 ? 134 THR A N   1 
ATOM   1027 C  CA  . THR A 1 134 ? 25.08700  -2.81300  24.03300 1.000 27.14329 ? 134 THR A CA  1 
ATOM   1028 C  C   . THR A 1 134 ? 23.82000  -1.98300  23.85800 1.000 25.56433 ? 134 THR A C   1 
ATOM   1029 O  O   . THR A 1 134 ? 23.67000  -0.91700  24.46700 1.000 24.75017 ? 134 THR A O   1 
ATOM   1030 C  CB  . THR A 1 134 ? 26.09300  -2.51200  22.91900 1.000 27.19479 ? 134 THR A CB  1 
ATOM   1031 O  OG1 . THR A 1 134 ? 27.27600  -3.29800  23.12300 1.000 28.44127 ? 134 THR A OG1 1 
ATOM   1032 C  CG2 . THR A 1 134 ? 26.46000  -1.01800  22.90000 1.000 23.97604 ? 134 THR A CG2 1 
ATOM   1033 N  N   . HIS A 1 135 ? 22.89200  -2.46500  23.03300 1.000 27.36502 ? 135 HIS A N   1 
ATOM   1034 C  CA  . HIS A 1 135 ? 21.58200  -1.84700  22.84200 1.000 26.02123 ? 135 HIS A CA  1 
ATOM   1035 C  C   . HIS A 1 135 ? 20.51500  -2.87500  23.20400 1.000 27.54701 ? 135 HIS A C   1 
ATOM   1036 O  O   . HIS A 1 135 ? 19.99300  -3.57300  22.32200 1.000 27.31593 ? 135 HIS A O   1 
ATOM   1037 C  CB  . HIS A 1 135 ? 21.42300  -1.34100  21.40900 1.000 23.68167 ? 135 HIS A CB  1 
ATOM   1038 C  CG  . HIS A 1 135 ? 22.48900  -0.38100  20.98200 1.000 22.36073 ? 135 HIS A CG  1 
ATOM   1039 N  ND1 . HIS A 1 135 ? 23.69600  -0.79300  20.46100 1.000 23.33301 ? 135 HIS A ND1 1 
ATOM   1040 C  CD2 . HIS A 1 135 ? 22.53000  0.97200   20.99700 1.000 20.71758 ? 135 HIS A CD2 1 
ATOM   1041 C  CE1 . HIS A 1 135 ? 24.43200  0.26600   20.17300 1.000 22.15707 ? 135 HIS A CE1 1 
ATOM   1042 N  NE2 . HIS A 1 135 ? 23.74900  1.34900   20.49400 1.000 20.12616 ? 135 HIS A NE2 1 
ATOM   1043 N  N   . PRO A 1 136 ? 20.15200  -2.99500  24.48900 1.000 27.39633 ? 136 PRO A N   1 
ATOM   1044 C  CA  . PRO A 1 136 ? 19.23200  -4.07100  24.91000 1.000 29.13194 ? 136 PRO A CA  1 
ATOM   1045 C  C   . PRO A 1 136 ? 17.86300  -4.06200  24.23000 1.000 29.40793 ? 136 PRO A C   1 
ATOM   1046 O  O   . PRO A 1 136 ? 17.16000  -5.07800  24.29200 1.000 29.43046 ? 136 PRO A O   1 
ATOM   1047 C  CB  . PRO A 1 136 ? 19.09900  -3.83800  26.42000 1.000 29.14848 ? 136 PRO A CB  1 
ATOM   1048 C  CG  . PRO A 1 136 ? 20.37800  -3.15500  26.80300 1.000 29.25083 ? 136 PRO A CG  1 
ATOM   1049 C  CD  . PRO A 1 136 ? 20.72100  -2.27500  25.64300 1.000 27.76129 ? 136 PRO A CD  1 
ATOM   1050 N  N   . LEU A 1 137 ? 17.46200  -2.96500  23.57700 1.000 28.21913 ? 137 LEU A N   1 
ATOM   1051 C  CA  . LEU A 1 137 ? 16.19300  -2.94600  22.85600 1.000 27.61261 ? 137 LEU A CA  1 
ATOM   1052 C  C   . LEU A 1 137 ? 16.16700  -3.92300  21.68100 1.000 26.85760 ? 137 LEU A C   1 
ATOM   1053 O  O   . LEU A 1 137 ? 15.09200  -4.23600  21.17200 1.000 27.34475 ? 137 LEU A O   1 
ATOM   1054 C  CB  . LEU A 1 137 ? 15.88700  -1.51700  22.37700 1.000 27.27436 ? 137 LEU A CB  1 
ATOM   1055 C  CG  . LEU A 1 137 ? 16.75300  -0.81600  21.32700 1.000 25.68928 ? 137 LEU A CG  1 
ATOM   1056 C  CD1 . LEU A 1 137 ? 16.47300  -1.34200  19.92900 1.000 24.58435 ? 137 LEU A CD1 1 
ATOM   1057 C  CD2 . LEU A 1 137 ? 16.53400  0.69400   21.37600 1.000 23.61757 ? 137 LEU A CD2 1 
ATOM   1058 N  N   . MET A 1 138 ? 17.32100  -4.40500  21.23400 1.000 28.49342 ? 138 MET A N   1 
ATOM   1059 C  CA  . MET A 1 138 ? 17.36900  -5.32200  20.09900 1.000 29.25964 ? 138 MET A CA  1 
ATOM   1060 C  C   . MET A 1 138 ? 16.74100  -6.68000  20.39700 1.000 28.18171 ? 138 MET A C   1 
ATOM   1061 O  O   . MET A 1 138 ? 16.28400  -7.34400  19.46600 1.000 27.98346 ? 138 MET A O   1 
ATOM   1062 C  CB  . MET A 1 138 ? 18.81400  -5.52400  19.65600 1.000 30.13076 ? 138 MET A CB  1 
ATOM   1063 C  CG  . MET A 1 138 ? 19.25200  -4.60600  18.56000 1.000 27.47862 ? 138 MET A CG  1 
ATOM   1064 S  SD  . MET A 1 138 ? 21.04400  -4.62900  18.43400 1.000 32.75345 ? 138 MET A SD  1 
ATOM   1065 C  CE  . MET A 1 138 ? 21.33400  -6.37800  18.26700 1.000 29.63865 ? 138 MET A CE  1 
ATOM   1066 N  N   . HIS A 1 139 ? 16.76800  -7.13600  21.66100 1.000 29.78236 ? 139 HIS A N   1 
ATOM   1067 C  CA  . HIS A 1 139 ? 16.12600  -8.40000  22.03700 1.000 30.69397 ? 139 HIS A CA  1 
ATOM   1068 C  C   . HIS A 1 139 ? 14.67700  -8.41500  21.57900 1.000 29.97763 ? 139 HIS A C   1 
ATOM   1069 O  O   . HIS A 1 139 ? 14.16000  -9.46200  21.17800 1.000 29.21364 ? 139 HIS A O   1 
ATOM   1070 C  CB  . HIS A 1 139 ? 16.22700  -8.61300  23.57000 1.000 29.85743 ? 139 HIS A CB  1 
ATOM   1071 C  CG  . HIS A 1 139 ? 15.60600  -9.88900  24.09200 1.000 31.48461 ? 139 HIS A CG  1 
ATOM   1072 N  ND1 . HIS A 1 139 ? 15.96100  -11.14300 23.64200 1.000 31.89463 ? 139 HIS A ND1 1 
ATOM   1073 C  CD2 . HIS A 1 139 ? 14.68200  -10.09700 25.06700 1.000 31.33784 ? 139 HIS A CD2 1 
ATOM   1074 C  CE1 . HIS A 1 139 ? 15.26200  -12.06300 24.29000 1.000 31.43852 ? 139 HIS A CE1 1 
ATOM   1075 N  NE2 . HIS A 1 139 ? 14.47800  -11.45500 25.16300 1.000 33.29870 ? 139 HIS A NE2 1 
ATOM   1076 N  N   . TYR A 1 140 ? 14.03800  -7.24400  21.55200 1.000 28.96904 ? 140 TYR A N   1 
ATOM   1077 C  CA  . TYR A 1 140 ? 12.59500  -7.11600  21.41700 1.000 27.95707 ? 140 TYR A CA  1 
ATOM   1078 C  C   . TYR A 1 140 ? 12.11300  -6.92900  19.98400 1.000 28.51159 ? 140 TYR A C   1 
ATOM   1079 O  O   . TYR A 1 140 ? 10.90200  -6.97500  19.75500 1.000 30.95637 ? 140 TYR A O   1 
ATOM   1080 C  CB  . TYR A 1 140 ? 12.09900  -5.94000  22.26100 1.000 28.39362 ? 140 TYR A CB  1 
ATOM   1081 C  CG  . TYR A 1 140 ? 12.45500  -5.99600  23.74100 1.000 27.59217 ? 140 TYR A CG  1 
ATOM   1082 C  CD1 . TYR A 1 140 ? 11.62200  -6.65500  24.63800 1.000 29.59964 ? 140 TYR A CD1 1 
ATOM   1083 C  CD2 . TYR A 1 140 ? 13.60900  -5.37700  24.20900 1.000 28.60749 ? 140 TYR A CD2 1 
ATOM   1084 C  CE1 . TYR A 1 140 ? 11.95300  -6.68800  25.96700 1.000 29.77975 ? 140 TYR A CE1 1 
ATOM   1085 C  CE2 . TYR A 1 140 ? 13.90900  -5.43100  25.54500 1.000 29.25746 ? 140 TYR A CE2 1 
ATOM   1086 C  CZ  . TYR A 1 140 ? 13.09700  -6.08400  26.45600 1.000 29.58589 ? 140 TYR A CZ  1 
ATOM   1087 O  OH  . TYR A 1 140 ? 13.39700  -6.12800  27.76800 1.000 33.46011 ? 140 TYR A OH  1 
ATOM   1088 N  N   . GLN A 1 141 ? 12.99600  -6.69200  19.03100 1.000 29.98290 ? 141 GLN A N   1 
ATOM   1089 C  CA  . GLN A 1 141 ? 12.57600  -6.66000  17.63400 1.000 29.76478 ? 141 GLN A CA  1 
ATOM   1090 C  C   . GLN A 1 141 ? 12.16900  -8.06200  17.20100 1.000 30.35310 ? 141 GLN A C   1 
ATOM   1091 O  O   . GLN A 1 141 ? 12.89700  -9.02200  17.47400 1.000 28.99453 ? 141 GLN A O   1 
ATOM   1092 C  CB  . GLN A 1 141 ? 13.70100  -6.15400  16.73500 1.000 29.48723 ? 141 GLN A CB  1 
ATOM   1093 C  CG  . GLN A 1 141 ? 14.22500  -4.78000  17.09300 1.000 29.60341 ? 141 GLN A CG  1 
ATOM   1094 C  CD  . GLN A 1 141 ? 13.68700  -3.69400  16.17700 1.000 30.30423 ? 141 GLN A CD  1 
ATOM   1095 O  OE1 . GLN A 1 141 ? 13.84700  -3.76700  14.95700 1.000 31.87847 ? 141 GLN A OE1 1 
ATOM   1096 N  NE2 . GLN A 1 141 ? 13.04300  -2.67800  16.76200 1.000 28.50232 ? 141 GLN A NE2 1 
ATOM   1097 N  N   . PRO A 1 142 ? 11.01600  -8.22900  16.55800 1.000 31.89997 ? 142 PRO A N   1 
ATOM   1098 C  CA  . PRO A 1 142 ? 10.70500  -9.52400  15.94800 1.000 32.57670 ? 142 PRO A CA  1 
ATOM   1099 C  C   . PRO A 1 142 ? 11.78800  -9.90200  14.95700 1.000 33.05862 ? 142 PRO A C   1 
ATOM   1100 O  O   . PRO A 1 142 ? 12.40500  -9.04100  14.33000 1.000 33.30036 ? 142 PRO A O   1 
ATOM   1101 C  CB  . PRO A 1 142 ? 9.36800   -9.27500  15.24500 1.000 32.82907 ? 142 PRO A CB  1 
ATOM   1102 C  CG  . PRO A 1 142 ? 8.77100   -8.14000  15.97800 1.000 30.39370 ? 142 PRO A CG  1 
ATOM   1103 C  CD  . PRO A 1 142 ? 9.90200   -7.27700  16.43600 1.000 31.05734 ? 142 PRO A CD  1 
ATOM   1104 N  N   . LEU A 1 143 ? 12.02800  -11.20700 14.83100 1.000 32.09151 ? 143 LEU A N   1 
ATOM   1105 C  CA  . LEU A 1 143 ? 13.02500  -11.67700 13.87900 1.000 33.45447 ? 143 LEU A CA  1 
ATOM   1106 C  C   . LEU A 1 143 ? 12.83300  -11.03100 12.51600 1.000 34.47922 ? 143 LEU A C   1 
ATOM   1107 O  O   . LEU A 1 143 ? 13.80600  -10.69800 11.83200 1.000 35.59918 ? 143 LEU A O   1 
ATOM   1108 C  CB  . LEU A 1 143 ? 12.95700  -13.19600 13.74900 1.000 35.26078 ? 143 LEU A CB  1 
ATOM   1109 C  CG  . LEU A 1 143 ? 13.89000  -13.70600 12.65500 1.000 33.94074 ? 143 LEU A CG  1 
ATOM   1110 C  CD1 . LEU A 1 143 ? 15.32100  -13.34600 13.01400 1.000 32.82378 ? 143 LEU A CD1 1 
ATOM   1111 C  CD2 . LEU A 1 143 ? 13.74000  -15.18700 12.44900 1.000 32.87463 ? 143 LEU A CD2 1 
ATOM   1112 N  N   . GLU A 1 144 ? 11.58300  -10.80300 12.12000 1.000 35.87039 ? 144 GLU A N   1 
ATOM   1113 C  CA  . GLU A 1 144 ? 11.29400  -10.35500 10.73300 1.000 35.14398 ? 144 GLU A CA  1 
ATOM   1114 C  C   . GLU A 1 144 ? 11.47300  -8.84400  10.54100 1.000 36.00007 ? 144 GLU A C   1 
ATOM   1115 O  O   . GLU A 1 144 ? 11.60800  -8.41200  9.39200  1.000 36.50586 ? 144 GLU A O   1 
ATOM   1116 C  CB  . GLU A 1 144 ? 9.88700   -10.81000 10.35500 1.000 38.76525 ? 144 GLU A CB  1 
ATOM   1117 C  CG  . GLU A 1 144 ? 9.49200   -12.15000 10.97000 1.000 40.78444 ? 144 GLU A CG  1 
ATOM   1118 C  CD  . GLU A 1 144 ? 8.61700   -12.04100 12.20200 1.000 40.41066 ? 144 GLU A CD  1 
ATOM   1119 O  OE1 . GLU A 1 144 ? 7.48400   -11.55200 12.06900 1.000 43.87221 ? 144 GLU A OE1 1 
ATOM   1120 O  OE2 . GLU A 1 144 ? 9.06200   -12.43000 13.29200 1.000 40.77918 ? 144 GLU A OE2 1 
ATOM   1121 N  N   . ALA A 1 145 ? 11.51600  -8.10000  11.63600 1.000 36.37775 ? 145 ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 145 ? 11.69500  -6.65400  11.55200 1.000 34.14379 ? 145 ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 145 ? 13.01400  -6.30200  10.85000 1.000 32.17475 ? 145 ALA A C   1 
ATOM   1124 O  O   . ALA A 1 145 ? 13.92300  -7.13300  10.77300 1.000 32.77431 ? 145 ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 145 ? 11.65800  -6.05400  12.95800 1.000 32.05158 ? 145 ALA A CB  1 
ATOM   1126 N  N   . PRO A 1 146 ? 13.14300  -5.07800  10.32800 1.000 32.03671 ? 146 PRO A N   1 
ATOM   1127 C  CA  . PRO A 1 146 ? 14.39700  -4.68700  9.68400  1.000 30.82094 ? 146 PRO A CA  1 
ATOM   1128 C  C   . PRO A 1 146 ? 15.54500  -4.78000  10.66900 1.000 28.00514 ? 146 PRO A C   1 
ATOM   1129 O  O   . PRO A 1 146 ? 15.44700  -4.27500  11.79700 1.000 27.52486 ? 146 PRO A O   1 
ATOM   1130 C  CB  . PRO A 1 146 ? 14.14500  -3.23000  9.25700  1.000 30.44716 ? 146 PRO A CB  1 
ATOM   1131 C  CG  . PRO A 1 146 ? 12.68300  -3.05600  9.27600  1.000 31.21347 ? 146 PRO A CG  1 
ATOM   1132 C  CD  . PRO A 1 146 ? 12.19700  -3.94700  10.37100 1.000 32.40080 ? 146 PRO A CD  1 
ATOM   1133 N  N   . PRO A 1 147 ? 16.63100  -5.44700  10.30300 1.000 26.59915 ? 147 PRO A N   1 
ATOM   1134 C  CA  . PRO A 1 147 ? 17.75400  -5.57200  11.23200 1.000 26.28565 ? 147 PRO A CA  1 
ATOM   1135 C  C   . PRO A 1 147 ? 18.47200  -4.24600  11.40300 1.000 25.06597 ? 147 PRO A C   1 
ATOM   1136 O  O   . PRO A 1 147 ? 18.52300  -3.41200  10.49400 1.000 24.21163 ? 147 PRO A O   1 
ATOM   1137 C  CB  . PRO A 1 147 ? 18.65600  -6.61700  10.56900 1.000 25.78642 ? 147 PRO A CB  1 
ATOM   1138 C  CG  . PRO A 1 147 ? 18.31500  -6.53300  9.12300  1.000 27.05934 ? 147 PRO A CG  1 
ATOM   1139 C  CD  . PRO A 1 147 ? 16.84800  -6.20600  9.06300  1.000 27.46254 ? 147 PRO A CD  1 
ATOM   1140 N  N   . VAL A 1 148 ? 19.02500  -4.05900  12.59800 1.000 23.67578 ? 148 VAL A N   1 
ATOM   1141 C  CA  . VAL A 1 148 ? 19.68600  -2.81900  12.96700 1.000 23.35309 ? 148 VAL A CA  1 
ATOM   1142 C  C   . VAL A 1 148 ? 21.12400  -3.02700  13.41600 1.000 22.58079 ? 148 VAL A C   1 
ATOM   1143 O  O   . VAL A 1 148 ? 21.79000  -2.05000  13.75600 1.000 22.25096 ? 148 VAL A O   1 
ATOM   1144 C  CB  . VAL A 1 148 ? 18.89300  -2.07100  14.05900 1.000 22.57159 ? 148 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A 1 148 ? 17.53200  -1.61700  13.52700 1.000 23.52952 ? 148 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A 1 148 ? 18.72500  -2.95400  15.28200 1.000 22.62250 ? 148 VAL A CG2 1 
ATOM   1147 N  N   . SER A 1 149 ? 21.62800  -4.26800  13.43000 1.000 22.97367 ? 149 SER A N   1 
ATOM   1148 C  CA  . SER A 1 149 ? 22.99700  -4.53500  13.86600 1.000 23.79045 ? 149 SER A CA  1 
ATOM   1149 C  C   . SER A 1 149 ? 23.62000  -5.65200  13.04000 1.000 23.74294 ? 149 SER A C   1 
ATOM   1150 O  O   . SER A 1 149 ? 22.94200  -6.60400  12.65100 1.000 24.72217 ? 149 SER A O   1 
ATOM   1151 C  CB  . SER A 1 149 ? 23.07300  -4.92800  15.34200 1.000 23.29678 ? 149 SER A CB  1 
ATOM   1152 O  OG  . SER A 1 149 ? 24.41000  -4.81100  15.79400 1.000 22.64840 ? 149 SER A OG  1 
ATOM   1153 N  N   . LEU A 1 150 ? 24.92900  -5.53400  12.79600 1.000 22.96229 ? 150 LEU A N   1 
ATOM   1154 C  CA  . LEU A 1 150 ? 25.68600  -6.56200  12.08800 1.000 23.36148 ? 150 LEU A CA  1 
ATOM   1155 C  C   . LEU A 1 150 ? 27.08800  -6.63300  12.66600 1.000 22.98789 ? 150 LEU A C   1 
ATOM   1156 O  O   . LEU A 1 150 ? 27.72500  -5.59200  12.84900 1.000 21.66084 ? 150 LEU A O   1 
ATOM   1157 C  CB  . LEU A 1 150 ? 25.76300  -6.27600  10.58700 1.000 21.66799 ? 150 LEU A CB  1 
ATOM   1158 C  CG  . LEU A 1 150 ? 26.40000  -7.38400  9.74300  1.000 22.92251 ? 150 LEU A CG  1 
ATOM   1159 C  CD1 . LEU A 1 150 ? 25.51900  -8.63000  9.68700  1.000 22.19165 ? 150 LEU A CD1 1 
ATOM   1160 C  CD2 . LEU A 1 150 ? 26.68300  -6.87500  8.34300  1.000 23.26732 ? 150 LEU A CD2 1 
ATOM   1161 N  N   . SER A 1 151 ? 27.57300  -7.84900  12.92800 1.000 22.21308 ? 151 SER A N   1 
ATOM   1162 C  CA  . SER A 1 151 ? 28.89000  -8.05200  13.51500 1.000 22.93713 ? 151 SER A CA  1 
ATOM   1163 C  C   . SER A 1 151 ? 29.85000  -8.57400  12.46000 1.000 23.60649 ? 151 SER A C   1 
ATOM   1164 O  O   . SER A 1 151 ? 29.54900  -9.55500  11.77500 1.000 24.40731 ? 151 SER A O   1 
ATOM   1165 C  CB  . SER A 1 151 ? 28.81600  -9.02000  14.68700 1.000 23.72992 ? 151 SER A CB  1 
ATOM   1166 O  OG  . SER A 1 151 ? 27.86400  -8.56400  15.61900 1.000 25.25211 ? 151 SER A OG  1 
ATOM   1167 N  N   . VAL A 1 152 ? 31.00100  -7.92000  12.33100 1.000 23.23095 ? 152 VAL A N   1 
ATOM   1168 C  CA  . VAL A 1 152 ? 32.02700  -8.30400  11.37000 1.000 23.14382 ? 152 VAL A CA  1 
ATOM   1169 C  C   . VAL A 1 152 ? 33.28400  -8.64500  12.14700 1.000 23.55931 ? 152 VAL A C   1 
ATOM   1170 O  O   . VAL A 1 152 ? 33.81700  -7.80700  12.88400 1.000 22.70758 ? 152 VAL A O   1 
ATOM   1171 C  CB  . VAL A 1 152 ? 32.30600  -7.20200  10.34100 1.000 23.48286 ? 152 VAL A CB  1 
ATOM   1172 C  CG1 . VAL A 1 152 ? 33.46200  -7.61700  9.44000  1.000 23.30986 ? 152 VAL A CG1 1 
ATOM   1173 C  CG2 . VAL A 1 152 ? 31.05600  -6.90000  9.53000  1.000 22.46659 ? 152 VAL A CG2 1 
ATOM   1174 N  N   . ILE A 1 153 ? 33.76400  -9.86600  11.97000 1.000 23.86754 ? 153 ILE A N   1 
ATOM   1175 C  CA  . ILE A 1 153 ? 34.76600  -10.46000 12.83700 1.000 23.76630 ? 153 ILE A CA  1 
ATOM   1176 C  C   . ILE A 1 153 ? 36.00500  -10.71600 11.99500 1.000 24.47746 ? 153 ILE A C   1 
ATOM   1177 O  O   . ILE A 1 153 ? 35.95400  -11.47300 11.01800 1.000 25.06716 ? 153 ILE A O   1 
ATOM   1178 C  CB  . ILE A 1 153 ? 34.24200  -11.74800 13.49200 1.000 24.21438 ? 153 ILE A CB  1 
ATOM   1179 C  CG1 . ILE A 1 153 ? 33.12900  -11.42400 14.49800 1.000 24.89406 ? 153 ILE A CG1 1 
ATOM   1180 C  CG2 . ILE A 1 153 ? 35.34800  -12.49600 14.18000 1.000 24.34319 ? 153 ILE A CG2 1 
ATOM   1181 C  CD1 . ILE A 1 153 ? 31.76100  -11.20400 13.88600 1.000 24.45350 ? 153 ILE A CD1 1 
ATOM   1182 N  N   . PHE A 1 154 ? 37.10700  -10.06800 12.36200 1.000 25.91490 ? 154 PHE A N   1 
ATOM   1183 C  CA  . PHE A 1 154 ? 38.31200  -10.05300 11.54700 1.000 26.37787 ? 154 PHE A CA  1 
ATOM   1184 C  C   . PHE A 1 154 ? 39.37800  -10.94600 12.14200 1.000 27.64596 ? 154 PHE A C   1 
ATOM   1185 O  O   . PHE A 1 154 ? 39.91400  -10.62500 13.21200 1.000 27.39502 ? 154 PHE A O   1 
ATOM   1186 C  CB  . PHE A 1 154 ? 38.84900  -8.63300  11.42200 1.000 26.64967 ? 154 PHE A CB  1 
ATOM   1187 C  CG  . PHE A 1 154 ? 38.20600  -7.85300  10.34900 1.000 25.53799 ? 154 PHE A CG  1 
ATOM   1188 C  CD1 . PHE A 1 154 ? 38.52600  -8.09600  9.03200  1.000 25.58505 ? 154 PHE A CD1 1 
ATOM   1189 C  CD2 . PHE A 1 154 ? 37.27600  -6.88000  10.64900 1.000 24.09848 ? 154 PHE A CD2 1 
ATOM   1190 C  CE1 . PHE A 1 154 ? 37.93500  -7.37500  8.03000  1.000 26.72989 ? 154 PHE A CE1 1 
ATOM   1191 C  CE2 . PHE A 1 154 ? 36.68000  -6.15500  9.65000  1.000 24.57430 ? 154 PHE A CE2 1 
ATOM   1192 C  CZ  . PHE A 1 154 ? 37.00800  -6.40300  8.33700  1.000 24.45039 ? 154 PHE A CZ  1 
ATOM   1193 N  N   . PRO A 1 155 ? 39.73300  -12.05300 11.49300 1.000 29.07867 ? 155 PRO A N   1 
ATOM   1194 C  CA  . PRO A 1 155 ? 40.93300  -12.79800 11.90100 1.000 30.21649 ? 155 PRO A CA  1 
ATOM   1195 C  C   . PRO A 1 155 ? 42.19000  -12.01500 11.55000 1.000 29.68643 ? 155 PRO A C   1 
ATOM   1196 O  O   . PRO A 1 155 ? 42.43500  -11.70800 10.38300 1.000 30.44107 ? 155 PRO A O   1 
ATOM   1197 C  CB  . PRO A 1 155 ? 40.83200  -14.09700 11.09500 1.000 31.41946 ? 155 PRO A CB  1 
ATOM   1198 C  CG  . PRO A 1 155 ? 39.97600  -13.73000 9.90600  1.000 30.59283 ? 155 PRO A CG  1 
ATOM   1199 C  CD  . PRO A 1 155 ? 39.00600  -12.71200 10.39200 1.000 28.05590 ? 155 PRO A CD  1 
ATOM   1200 N  N   . LEU A 1 156 ? 42.97700  -11.67400 12.56800 1.000 28.53564 ? 156 LEU A N   1 
ATOM   1201 C  CA  . LEU A 1 156 ? 44.29600  -11.09700 12.34300 1.000 29.27321 ? 156 LEU A CA  1 
ATOM   1202 C  C   . LEU A 1 156 ? 45.40900  -12.12200 12.46900 1.000 31.44063 ? 156 LEU A C   1 
ATOM   1203 O  O   . LEU A 1 156 ? 46.54200  -11.84000 12.06500 1.000 33.83112 ? 156 LEU A O   1 
ATOM   1204 C  CB  . LEU A 1 156 ? 44.55200  -9.92500  13.30000 1.000 28.75455 ? 156 LEU A CB  1 
ATOM   1205 C  CG  . LEU A 1 156 ? 43.97700  -8.59500  12.79200 1.000 27.99923 ? 156 LEU A CG  1 
ATOM   1206 C  CD1 . LEU A 1 156 ? 43.85200  -7.60800  13.90800 1.000 26.79777 ? 156 LEU A CD1 1 
ATOM   1207 C  CD2 . LEU A 1 156 ? 44.83600  -8.01900  11.70000 1.000 29.03861 ? 156 LEU A CD2 1 
ATOM   1208 N  N   . THR A 1 157 ? 45.11500  -13.28200 13.02700 1.000 32.77760 ? 157 THR A N   1 
ATOM   1209 C  CA  . THR A 1 157 ? 45.91200  -14.48800 12.90100 1.000 34.02057 ? 157 THR A CA  1 
ATOM   1210 C  C   . THR A 1 157 ? 45.01300  -15.55000 12.27900 1.000 35.42756 ? 157 THR A C   1 
ATOM   1211 O  O   . THR A 1 157 ? 43.83100  -15.30900 12.03700 1.000 34.45943 ? 157 THR A O   1 
ATOM   1212 C  CB  . THR A 1 157 ? 46.44000  -14.93500 14.26200 1.000 33.59271 ? 157 THR A CB  1 
ATOM   1213 O  OG1 . THR A 1 157 ? 45.32700  -15.20900 15.11900 1.000 33.53953 ? 157 THR A OG1 1 
ATOM   1214 C  CG2 . THR A 1 157 ? 47.28600  -13.85100 14.88800 1.000 31.70570 ? 157 THR A CG2 1 
ATOM   1215 N  N   . GLU A 1 158 ? 45.55700  -16.73100 12.00800 1.000 35.98555 ? 158 GLU A N   1 
ATOM   1216 C  CA  . GLU A 1 158 ? 44.67300  -17.80600 11.58900 1.000 35.86227 ? 158 GLU A CA  1 
ATOM   1217 C  C   . GLU A 1 158 ? 43.85600  -18.28700 12.78400 1.000 35.17591 ? 158 GLU A C   1 
ATOM   1218 O  O   . GLU A 1 158 ? 44.30100  -18.22600 13.93200 1.000 33.90470 ? 158 GLU A O   1 
ATOM   1219 C  CB  . GLU A 1 158 ? 45.45300  -18.96100 10.97000 1.000 37.23614 ? 158 GLU A CB  1 
ATOM   1220 C  CG  . GLU A 1 158 ? 46.42300  -19.60200 11.91300 1.000 39.36399 ? 158 GLU A CG  1 
ATOM   1221 C  CD  . GLU A 1 158 ? 46.84500  -20.97600 11.45900 1.000 43.77087 ? 158 GLU A CD  1 
ATOM   1222 O  OE1 . GLU A 1 158 ? 46.21000  -21.51300 10.52100 1.000 44.27782 ? 158 GLU A OE1 1 
ATOM   1223 O  OE2 . GLU A 1 158 ? 47.81000  -21.51900 12.04500 1.000 44.01000 ? 158 GLU A OE2 1 
ATOM   1224 N  N   . PHE A 1 159 ? 42.62100  -18.70300 12.50700 1.000 37.15598 ? 159 PHE A N   1 
ATOM   1225 C  CA  . PHE A 1 159 ? 41.74200  -19.30400 13.50300 1.000 34.81291 ? 159 PHE A CA  1 
ATOM   1226 C  C   . PHE A 1 159 ? 41.77500  -20.81500 13.32200 1.000 35.14996 ? 159 PHE A C   1 
ATOM   1227 O  O   . PHE A 1 159 ? 41.66900  -21.31100 12.19700 1.000 35.50440 ? 159 PHE A O   1 
ATOM   1228 C  CB  . PHE A 1 159 ? 40.30400  -18.80400 13.36800 1.000 33.73743 ? 159 PHE A CB  1 
ATOM   1229 C  CG  . PHE A 1 159 ? 40.07700  -17.39500 13.84900 1.000 32.87542 ? 159 PHE A CG  1 
ATOM   1230 C  CD1 . PHE A 1 159 ? 41.11100  -16.62600 14.33900 1.000 31.85004 ? 159 PHE A CD1 1 
ATOM   1231 C  CD2 . PHE A 1 159 ? 38.80100  -16.84700 13.81500 1.000 31.68971 ? 159 PHE A CD2 1 
ATOM   1232 C  CE1 . PHE A 1 159 ? 40.87700  -15.34200 14.77000 1.000 31.25093 ? 159 PHE A CE1 1 
ATOM   1233 C  CE2 . PHE A 1 159 ? 38.56200  -15.56300 14.24300 1.000 29.86496 ? 159 PHE A CE2 1 
ATOM   1234 C  CZ  . PHE A 1 159 ? 39.59900  -14.80600 14.72000 1.000 29.55645 ? 159 PHE A CZ  1 
ATOM   1235 N  N   . THR A 1 160 ? 41.93800  -21.53900 14.42200 1.000 36.39742 ? 160 THR A N   1 
ATOM   1236 C  CA  . THR A 1 160 ? 42.08400  -22.98700 14.39000 1.000 36.37977 ? 160 THR A CA  1 
ATOM   1237 C  C   . THR A 1 160 ? 41.29800  -23.57800 15.55500 1.000 36.25762 ? 160 THR A C   1 
ATOM   1238 O  O   . THR A 1 160 ? 40.88800  -22.86200 16.47100 1.000 34.58059 ? 160 THR A O   1 
ATOM   1239 C  CB  . THR A 1 160 ? 43.56700  -23.39600 14.45900 1.000 36.78235 ? 160 THR A CB  1 
ATOM   1240 O  OG1 . THR A 1 160 ? 44.11800  -22.96200 15.70300 1.000 38.47052 ? 160 THR A OG1 1 
ATOM   1241 C  CG2 . THR A 1 160 ? 44.38100  -22.75400 13.32600 1.000 37.37992 ? 160 THR A CG2 1 
ATOM   1242 N  N   . GLU A 1 161 ? 41.08600  -24.90500 15.52200 1.000 36.19111 ? 161 GLU A N   1 
ATOM   1243 C  CA  . GLU A 1 161 ? 40.37800  -25.56900 16.62100 1.000 36.70453 ? 161 GLU A CA  1 
ATOM   1244 C  C   . GLU A 1 161 ? 41.11300  -25.38700 17.94000 1.000 36.99935 ? 161 GLU A C   1 
ATOM   1245 O  O   . GLU A 1 161 ? 40.48600  -25.32700 19.00300 1.000 38.27456 ? 161 GLU A O   1 
ATOM   1246 C  CB  . GLU A 1 161 ? 40.18600  -27.06800 16.33900 1.000 37.79781 ? 161 GLU A CB  1 
ATOM   1247 C  CG  . GLU A 1 161 ? 39.02800  -27.43700 15.37900 1.000 40.33175 ? 161 GLU A CG  1 
ATOM   1248 C  CD  . GLU A 1 161 ? 38.04800  -28.48900 15.94100 1.000 42.42992 ? 161 GLU A CD  1 
ATOM   1249 O  OE1 . GLU A 1 161 ? 38.30100  -29.03800 17.04000 1.000 42.20012 ? 161 GLU A OE1 1 
ATOM   1250 O  OE2 . GLU A 1 161 ? 37.01400  -28.76700 15.27900 1.000 42.02451 ? 161 GLU A OE2 1 
ATOM   1251 N  N   . GLU A 1 162 ? 42.43500  -25.25900 17.88400 1.000 36.55833 ? 162 GLU A N   1 
ATOM   1252 C  CA  . GLU A 1 162 ? 43.24900  -25.14800 19.08700 1.000 37.99461 ? 162 GLU A CA  1 
ATOM   1253 C  C   . GLU A 1 162 ? 43.20400  -23.74100 19.67100 1.000 37.34984 ? 162 GLU A C   1 
ATOM   1254 O  O   . GLU A 1 162 ? 43.02300  -23.57500 20.88100 1.000 38.04632 ? 162 GLU A O   1 
ATOM   1255 C  CB  . GLU A 1 162 ? 44.69000  -25.55500 18.76200 1.000 39.96331 ? 162 GLU A CB  1 
ATOM   1256 C  CG  . GLU A 1 162 ? 45.47900  -26.19000 19.90300 1.000 39.67363 ? 162 GLU A CG  1 
ATOM   1257 C  CD  . GLU A 1 162 ? 46.89900  -26.55800 19.48000 1.000 42.38223 ? 162 GLU A CD  1 
ATOM   1258 O  OE1 . GLU A 1 162 ? 47.27600  -26.19600 18.34100 1.000 44.16839 ? 162 GLU A OE1 1 
ATOM   1259 O  OE2 . GLU A 1 162 ? 47.63400  -27.20200 20.27400 1.000 42.61443 ? 162 GLU A OE2 1 
ATOM   1260 N  N   . ASN A 1 163 ? 43.37300  -22.71100 18.83000 1.000 36.62710 ? 163 ASN A N   1 
ATOM   1261 C  CA  . ASN A 1 163 ? 43.50000  -21.34800 19.33400 1.000 36.33710 ? 163 ASN A CA  1 
ATOM   1262 C  C   . ASN A 1 163 ? 42.16700  -20.72100 19.69000 1.000 35.08537 ? 163 ASN A C   1 
ATOM   1263 O  O   . ASN A 1 163 ? 42.15200  -19.62900 20.26400 1.000 33.99539 ? 163 ASN A O   1 
ATOM   1264 C  CB  . ASN A 1 163 ? 44.22800  -20.45000 18.32300 1.000 36.50827 ? 163 ASN A CB  1 
ATOM   1265 C  CG  . ASN A 1 163 ? 43.41200  -20.17100 17.05900 1.000 34.39935 ? 163 ASN A CG  1 
ATOM   1266 O  OD1 . ASN A 1 163 ? 42.21000  -20.43800 16.97900 1.000 33.79506 ? 163 ASN A OD1 1 
ATOM   1267 N  ND2 . ASN A 1 163 ? 44.08300  -19.61500 16.05900 1.000 34.02833 ? 163 ASN A ND2 1 
ATOM   1268 N  N   . GLY A 1 164 ? 41.06200  -21.36200 19.33200 1.000 36.25279 ? 164 GLY A N   1 
ATOM   1269 C  CA  . GLY A 1 164 ? 39.75400  -20.88400 19.72100 1.000 35.63960 ? 164 GLY A CA  1 
ATOM   1270 C  C   . GLY A 1 164 ? 38.98900  -20.13700 18.64700 1.000 33.56515 ? 164 GLY A C   1 
ATOM   1271 O  O   . GLY A 1 164 ? 38.36200  -19.11800 18.93900 1.000 32.95732 ? 164 GLY A O   1 
ATOM   1272 N  N   . ALA A 1 165 ? 39.03400  -20.62800 17.40800 1.000 32.06401 ? 165 ALA A N   1 
ATOM   1273 C  CA  . ALA A 1 165 ? 38.21000  -20.08500 16.33600 1.000 31.41709 ? 165 ALA A CA  1 
ATOM   1274 C  C   . ALA A 1 165 ? 36.78200  -19.86800 16.82100 1.000 31.89607 ? 165 ALA A C   1 
ATOM   1275 O  O   . ALA A 1 165 ? 36.23400  -20.68500 17.56400 1.000 32.06019 ? 165 ALA A O   1 
ATOM   1276 C  CB  . ALA A 1 165 ? 38.22000  -21.03800 15.13500 1.000 32.13896 ? 165 ALA A CB  1 
ATOM   1277 N  N   . THR A 1 166 ? 36.18500  -18.75100 16.40500 1.000 32.63216 ? 166 THR A N   1 
ATOM   1278 C  CA  . THR A 1 166 ? 34.87800  -18.35500 16.91900 1.000 31.33714 ? 166 THR A CA  1 
ATOM   1279 C  C   . THR A 1 166 ? 33.83500  -19.43100 16.65900 1.000 31.97555 ? 166 THR A C   1 
ATOM   1280 O  O   . THR A 1 166 ? 33.74100  -19.97600 15.55700 1.000 32.07344 ? 166 THR A O   1 
ATOM   1281 C  CB  . THR A 1 166 ? 34.44100  -17.03700 16.28900 1.000 30.40836 ? 166 THR A CB  1 
ATOM   1282 O  OG1 . THR A 1 166 ? 35.37200  -16.01300 16.65500 1.000 31.06672 ? 166 THR A OG1 1 
ATOM   1283 C  CG2 . THR A 1 166 ? 33.05100  -16.65300 16.76400 1.000 29.33128 ? 166 THR A CG2 1 
ATOM   1284 N  N   . GLU A 1 167 ? 33.08700  -19.71600 17.70700 1.000 31.47431 ? 167 GLU A N   1 
ATOM   1285 C  CA  . GLU A 1 167 ? 32.04700  -20.76400 17.64700 1.000 29.94390 ? 167 GLU A CA  1 
ATOM   1286 C  C   . GLU A 1 167 ? 30.70200  -20.13100 17.28800 1.000 30.01384 ? 167 GLU A C   1 
ATOM   1287 O  O   . GLU A 1 167 ? 30.23900  -19.28300 18.03600 1.000 29.38555 ? 167 GLU A O   1 
ATOM   1288 C  CB  . GLU A 1 167 ? 32.04700  -21.44200 19.01100 1.000 30.87449 ? 167 GLU A CB  1 
ATOM   1289 C  CG  . GLU A 1 167 ? 33.44500  -21.67500 19.57100 1.000 32.51800 ? 167 GLU A CG  1 
ATOM   1290 C  CD  . GLU A 1 167 ? 33.43000  -22.17100 20.99900 1.000 34.14091 ? 167 GLU A CD  1 
ATOM   1291 O  OE1 . GLU A 1 167 ? 32.33300  -22.44600 21.50600 1.000 35.67688 ? 167 GLU A OE1 1 
ATOM   1292 O  OE2 . GLU A 1 167 ? 34.50200  -22.24400 21.61900 1.000 35.34218 ? 167 GLU A OE2 1 
ATOM   1293 N  N   . VAL A 1 168 ? 30.13300  -20.56400 16.17700 1.000 30.93151 ? 168 VAL A N   1 
ATOM   1294 C  CA  . VAL A 1 168 ? 28.85200  -20.05200 15.69500 1.000 29.83372 ? 168 VAL A CA  1 
ATOM   1295 C  C   . VAL A 1 168 ? 27.84300  -21.18700 15.73800 1.000 29.87984 ? 168 VAL A C   1 
ATOM   1296 O  O   . VAL A 1 168 ? 28.13700  -22.29600 15.28100 1.000 30.55470 ? 168 VAL A O   1 
ATOM   1297 C  CB  . VAL A 1 168 ? 28.96600  -19.49100 14.26500 1.000 28.47428 ? 168 VAL A CB  1 
ATOM   1298 C  CG1 . VAL A 1 168 ? 27.62200  -18.94700 13.78300 1.000 27.98915 ? 168 VAL A CG1 1 
ATOM   1299 C  CG2 . VAL A 1 168 ? 30.06200  -18.43200 14.17400 1.000 27.88004 ? 168 VAL A CG2 1 
ATOM   1300 N  N   . ILE A 1 169 ? 26.66700  -20.91800 16.29200 1.000 29.44140 ? 169 ILE A N   1 
ATOM   1301 C  CA  . ILE A 1 169 ? 25.53800  -21.83600 16.22900 1.000 29.87288 ? 169 ILE A CA  1 
ATOM   1302 C  C   . ILE A 1 169 ? 24.65500  -21.36600 15.08400 1.000 29.58651 ? 169 ILE A C   1 
ATOM   1303 O  O   . ILE A 1 169 ? 24.01500  -20.31400 15.18000 1.000 30.61114 ? 169 ILE A O   1 
ATOM   1304 C  CB  . ILE A 1 169 ? 24.75800  -21.87500 17.54900 1.000 29.85593 ? 169 ILE A CB  1 
ATOM   1305 C  CG1 . ILE A 1 169 ? 25.69300  -22.15700 18.72600 1.000 32.18912 ? 169 ILE A CG1 1 
ATOM   1306 C  CG2 . ILE A 1 169 ? 23.66600  -22.90400 17.47800 1.000 30.23679 ? 169 ILE A CG2 1 
ATOM   1307 C  CD1 . ILE A 1 169 ? 24.98500  -22.23900 20.05400 1.000 32.24099 ? 169 ILE A CD1 1 
ATOM   1308 N  N   . LEU A 1 170 ? 24.62300  -22.13100 13.99500 1.000 29.11683 ? 170 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 170 ? 23.89200  -21.71100 12.80800 1.000 29.81280 ? 170 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 170 ? 22.39100  -21.69600 13.07800 1.000 30.32084 ? 170 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 170 ? 21.87900  -22.51000 13.84200 1.000 30.72541 ? 170 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 170 ? 24.21400  -22.63200 11.63000 1.000 29.90859 ? 170 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 170 ? 25.64200  -22.63500 11.06400 1.000 29.92092 ? 170 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 170 ? 25.69800  -23.42100 9.74900  1.000 30.95032 ? 170 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 170 ? 26.18300  -21.22100 10.88200 1.000 28.60579 ? 170 LEU A CD2 1 
ATOM   1316 N  N   . GLY A 1 171 ? 21.68700  -20.74100 12.46800 1.000 31.07155 ? 171 GLY A N   1 
ATOM   1317 C  CA  . GLY A 1 171 ? 20.25200  -20.63100 12.63100 1.000 31.26758 ? 171 GLY A CA  1 
ATOM   1318 C  C   . GLY A 1 171 ? 19.77600  -20.14400 13.98200 1.000 31.03271 ? 171 GLY A C   1 
ATOM   1319 O  O   . GLY A 1 171 ? 18.56200  -20.06800 14.19700 1.000 30.99342 ? 171 GLY A O   1 
ATOM   1320 N  N   . SER A 1 172 ? 20.68400  -19.77500 14.88900 1.000 30.31449 ? 172 SER A N   1 
ATOM   1321 C  CA  . SER A 1 172 ? 20.30000  -19.42800 16.25500 1.000 29.69924 ? 172 SER A CA  1 
ATOM   1322 C  C   . SER A 1 172 ? 19.54100  -18.10800 16.34800 1.000 30.69974 ? 172 SER A C   1 
ATOM   1323 O  O   . SER A 1 172 ? 18.90900  -17.84600 17.37900 1.000 31.71541 ? 172 SER A O   1 
ATOM   1324 C  CB  . SER A 1 172 ? 21.53600  -19.37400 17.15200 1.000 27.69879 ? 172 SER A CB  1 
ATOM   1325 O  OG  . SER A 1 172 ? 22.54600  -18.59300 16.55800 1.000 28.41897 ? 172 SER A OG  1 
ATOM   1326 N  N   . HIS A 1 173 ? 19.59000  -17.26700 15.31200 1.000 29.80011 ? 173 HIS A N   1 
ATOM   1327 C  CA  . HIS A 1 173 ? 18.78800  -16.05100 15.31700 1.000 29.28601 ? 173 HIS A CA  1 
ATOM   1328 C  C   . HIS A 1 173 ? 17.30000  -16.34900 15.26500 1.000 30.48266 ? 173 HIS A C   1 
ATOM   1329 O  O   . HIS A 1 173 ? 16.49000  -15.46500 15.55400 1.000 31.16150 ? 173 HIS A O   1 
ATOM   1330 C  CB  . HIS A 1 173 ? 19.18400  -15.14600 14.14900 1.000 30.02042 ? 173 HIS A CB  1 
ATOM   1331 C  CG  . HIS A 1 173 ? 18.99900  -15.77200 12.80700 1.000 29.78618 ? 173 HIS A CG  1 
ATOM   1332 N  ND1 . HIS A 1 173 ? 19.61000  -16.95200 12.44700 1.000 30.43156 ? 173 HIS A ND1 1 
ATOM   1333 C  CD2 . HIS A 1 173 ? 18.27200  -15.38200 11.73600 1.000 31.27877 ? 173 HIS A CD2 1 
ATOM   1334 C  CE1 . HIS A 1 173 ? 19.26600  -17.26100 11.21100 1.000 30.71002 ? 173 HIS A CE1 1 
ATOM   1335 N  NE2 . HIS A 1 173 ? 18.45300  -16.32600 10.75700 1.000 30.10304 ? 173 HIS A NE2 1 
ATOM   1336 N  N   . ARG A 1 174 ? 16.92000  -17.57200 14.91800 1.000 31.42210 ? 174 ARG A N   1 
ATOM   1337 C  CA  . ARG A 1 174 ? 15.51900  -17.94600 14.93100 1.000 31.18106 ? 174 ARG A CA  1 
ATOM   1338 C  C   . ARG A 1 174 ? 15.03400  -18.39500 16.30700 1.000 32.86775 ? 174 ARG A C   1 
ATOM   1339 O  O   . ARG A 1 174 ? 13.82000  -18.40700 16.54500 1.000 33.64630 ? 174 ARG A O   1 
ATOM   1340 C  CB  . ARG A 1 174 ? 15.27400  -19.03900 13.89000 1.000 31.61089 ? 174 ARG A CB  1 
ATOM   1341 C  CG  . ARG A 1 174 ? 15.14700  -18.48800 12.48500 1.000 30.84932 ? 174 ARG A CG  1 
ATOM   1342 C  CD  . ARG A 1 174 ? 14.86600  -19.58300 11.49000 1.000 31.97720 ? 174 ARG A CD  1 
ATOM   1343 N  NE  . ARG A 1 174 ? 16.05300  -20.39900 11.26800 1.000 34.61538 ? 174 ARG A NE  1 
ATOM   1344 C  CZ  . ARG A 1 174 ? 16.90400  -20.22400 10.26500 1.000 35.20208 ? 174 ARG A CZ  1 
ATOM   1345 N  NH1 . ARG A 1 174 ? 16.70300  -19.30100 9.34100  1.000 33.87475 ? 174 ARG A NH1 1 
ATOM   1346 N  NH2 . ARG A 1 174 ? 17.98300  -20.99800 10.18400 1.000 37.22217 ? 174 ARG A NH2 1 
ATOM   1347 N  N   . TRP A 1 175 ? 15.93900  -18.74700 17.22000 1.000 33.63764 ? 175 TRP A N   1 
ATOM   1348 C  CA  . TRP A 1 175 ? 15.51300  -19.17700 18.54700 1.000 35.09588 ? 175 TRP A CA  1 
ATOM   1349 C  C   . TRP A 1 175 ? 14.73000  -18.06900 19.23700 1.000 38.06065 ? 175 TRP A C   1 
ATOM   1350 O  O   . TRP A 1 175 ? 14.95700  -16.88000 19.00800 1.000 37.21452 ? 175 TRP A O   1 
ATOM   1351 C  CB  . TRP A 1 175 ? 16.70600  -19.56000 19.42700 1.000 33.58351 ? 175 TRP A CB  1 
ATOM   1352 C  CG  . TRP A 1 175 ? 17.55800  -20.65800 18.89400 1.000 32.19884 ? 175 TRP A CG  1 
ATOM   1353 C  CD1 . TRP A 1 175 ? 17.30200  -21.44200 17.81600 1.000 31.63453 ? 175 TRP A CD1 1 
ATOM   1354 C  CD2 . TRP A 1 175 ? 18.81700  -21.09000 19.41600 1.000 32.06821 ? 175 TRP A CD2 1 
ATOM   1355 N  NE1 . TRP A 1 175 ? 18.32300  -22.33500 17.62900 1.000 31.23634 ? 175 TRP A NE1 1 
ATOM   1356 C  CE2 . TRP A 1 175 ? 19.26500  -22.13800 18.60200 1.000 31.02166 ? 175 TRP A CE2 1 
ATOM   1357 C  CE3 . TRP A 1 175 ? 19.61100  -20.68500 20.49300 1.000 33.62656 ? 175 TRP A CE3 1 
ATOM   1358 C  CZ2 . TRP A 1 175 ? 20.46700  -22.79100 18.82700 1.000 32.06515 ? 175 TRP A CZ2 1 
ATOM   1359 C  CZ3 . TRP A 1 175 ? 20.80100  -21.33700 20.71900 1.000 31.38352 ? 175 TRP A CZ3 1 
ATOM   1360 C  CH2 . TRP A 1 175 ? 21.22200  -22.37200 19.88800 1.000 32.02865 ? 175 TRP A CH2 1 
ATOM   1361 N  N   . THR A 1 176 ? 13.79200  -18.47200 20.08900 1.000 42.95880 ? 176 THR A N   1 
ATOM   1362 C  CA  . THR A 1 176 ? 13.13900  -17.50300 20.95600 1.000 44.92049 ? 176 THR A CA  1 
ATOM   1363 C  C   . THR A 1 176 ? 14.14800  -16.88400 21.92000 1.000 45.63565 ? 176 THR A C   1 
ATOM   1364 O  O   . THR A 1 176 ? 14.21000  -15.65700 22.07000 1.000 47.79324 ? 176 THR A O   1 
ATOM   1365 C  CB  . THR A 1 176 ? 11.98500  -18.17000 21.71300 1.000 44.99812 ? 176 THR A CB  1 
ATOM   1366 O  OG1 . THR A 1 176 ? 12.48500  -19.25300 22.51000 1.000 47.53513 ? 176 THR A OG1 1 
ATOM   1367 C  CG2 . THR A 1 176 ? 10.95900  -18.71300 20.74200 1.000 43.77576 ? 176 THR A CG2 1 
ATOM   1368 N  N   . GLU A 1 177 ? 14.97100  -17.72100 22.55700 1.000 41.68514 ? 177 GLU A N   1 
ATOM   1369 C  CA  . GLU A 1 177 ? 15.86200  -17.30900 23.63300 1.000 39.55855 ? 177 GLU A CA  1 
ATOM   1370 C  C   . GLU A 1 177 ? 17.25000  -17.90200 23.41400 1.000 37.76045 ? 177 GLU A C   1 
ATOM   1371 O  O   . GLU A 1 177 ? 17.41100  -18.93000 22.75300 1.000 37.63273 ? 177 GLU A O   1 
ATOM   1372 C  CB  . GLU A 1 177 ? 15.31800  -17.74900 25.00500 1.000 43.26618 ? 177 GLU A CB  1 
ATOM   1373 C  CG  . GLU A 1 177 ? 13.81500  -17.52200 25.22500 1.000 47.00615 ? 177 GLU A CG  1 
ATOM   1374 C  CD  . GLU A 1 177 ? 13.17800  -18.54700 26.17900 1.000 50.70584 ? 177 GLU A CD  1 
ATOM   1375 O  OE1 . GLU A 1 177 ? 13.36100  -19.77200 25.96900 1.000 49.66026 ? 177 GLU A OE1 1 
ATOM   1376 O  OE2 . GLU A 1 177 ? 12.49300  -18.12400 27.14100 1.000 51.63499 ? 177 GLU A OE2 1 
ATOM   1377 N  N   . VAL A 1 178 ? 18.26100  -17.23300 23.97700 1.000 38.97730 ? 178 VAL A N   1 
ATOM   1378 C  CA  . VAL A 1 178 ? 19.63500  -17.73100 23.89600 1.000 36.04438 ? 178 VAL A CA  1 
ATOM   1379 C  C   . VAL A 1 178 ? 19.75700  -19.05500 24.63600 1.000 36.90625 ? 178 VAL A C   1 
ATOM   1380 O  O   . VAL A 1 178 ? 20.33100  -20.02700 24.12800 1.000 38.41646 ? 178 VAL A O   1 
ATOM   1381 C  CB  . VAL A 1 178 ? 20.61900  -16.69000 24.45800 1.000 34.53543 ? 178 VAL A CB  1 
ATOM   1382 C  CG1 . VAL A 1 178 ? 22.05800  -17.17400 24.31300 1.000 32.59277 ? 178 VAL A CG1 1 
ATOM   1383 C  CG2 . VAL A 1 178 ? 20.42500  -15.35600 23.78300 1.000 34.65452 ? 178 VAL A CG2 1 
ATOM   1384 N  N   . GLY A 1 179 ? 19.24100  -19.10000 25.86000 1.000 36.87662 ? 179 GLY A N   1 
ATOM   1385 C  CA  . GLY A 1 179 ? 19.10800  -20.35100 26.56800 1.000 37.52598 ? 179 GLY A CA  1 
ATOM   1386 C  C   . GLY A 1 179 ? 20.43000  -20.94900 27.01200 1.000 38.73446 ? 179 GLY A C   1 
ATOM   1387 O  O   . GLY A 1 179 ? 21.39400  -20.25300 27.34500 1.000 39.13887 ? 179 GLY A O   1 
ATOM   1388 N  N   . THR A 1 180 ? 20.46600  -22.28000 26.98700 1.000 37.84270 ? 180 THR A N   1 
ATOM   1389 C  CA  . THR A 1 180 ? 21.45300  -23.08700 27.69500 1.000 37.87938 ? 180 THR A CA  1 
ATOM   1390 C  C   . THR A 1 180 ? 22.22700  -23.94700 26.69800 1.000 38.09873 ? 180 THR A C   1 
ATOM   1391 O  O   . THR A 1 180 ? 22.09800  -25.17700 26.69800 1.000 37.19256 ? 180 THR A O   1 
ATOM   1392 C  CB  . THR A 1 180 ? 20.73700  -23.96200 28.72000 1.000 41.15910 ? 180 THR A CB  1 
ATOM   1393 O  OG1 . THR A 1 180 ? 20.09300  -25.04600 28.03700 1.000 42.62916 ? 180 THR A OG1 1 
ATOM   1394 C  CG2 . THR A 1 180 ? 19.65500  -23.16000 29.45600 1.000 40.22965 ? 180 THR A CG2 1 
ATOM   1395 N  N   . PRO A 1 181 ? 23.05300  -23.33900 25.84600 1.000 38.23535 ? 181 PRO A N   1 
ATOM   1396 C  CA  . PRO A 1 181 ? 23.55400  -24.05900 24.67100 1.000 35.82720 ? 181 PRO A CA  1 
ATOM   1397 C  C   . PRO A 1 181 ? 24.82300  -24.85300 24.93300 1.000 34.97974 ? 181 PRO A C   1 
ATOM   1398 O  O   . PRO A 1 181 ? 25.69500  -24.46600 25.71400 1.000 35.86714 ? 181 PRO A O   1 
ATOM   1399 C  CB  . PRO A 1 181 ? 23.81300  -22.92300 23.67400 1.000 34.92058 ? 181 PRO A CB  1 
ATOM   1400 C  CG  . PRO A 1 181 ? 24.19100  -21.77700 24.53100 1.000 35.42625 ? 181 PRO A CG  1 
ATOM   1401 C  CD  . PRO A 1 181 ? 23.58500  -21.96900 25.90400 1.000 38.48664 ? 181 PRO A CD  1 
ATOM   1402 N  N   . GLU A 1 182 ? 24.91000  -25.99100 24.25900 1.000 35.54782 ? 182 GLU A N   1 
ATOM   1403 C  CA  . GLU A 1 182 ? 26.04400  -26.88700 24.38500 1.000 35.87386 ? 182 GLU A CA  1 
ATOM   1404 C  C   . GLU A 1 182 ? 27.05100  -26.59500 23.28000 1.000 35.87307 ? 182 GLU A C   1 
ATOM   1405 O  O   . GLU A 1 182 ? 26.73500  -25.95400 22.27900 1.000 36.58473 ? 182 GLU A O   1 
ATOM   1406 C  CB  . GLU A 1 182 ? 25.57300  -28.34500 24.35500 1.000 34.82115 ? 182 GLU A CB  1 
ATOM   1407 C  CG  . GLU A 1 182 ? 24.74500  -28.71300 25.58600 1.000 33.39009 ? 182 GLU A CG  1 
ATOM   1408 C  CD  . GLU A 1 182 ? 24.14100  -30.10100 25.53400 1.000 33.96637 ? 182 GLU A CD  1 
ATOM   1409 O  OE1 . GLU A 1 182 ? 23.60400  -30.51000 24.48200 1.000 33.02450 ? 182 GLU A OE1 1 
ATOM   1410 O  OE2 . GLU A 1 182 ? 24.19300  -30.79400 26.56700 1.000 35.56005 ? 182 GLU A OE2 1 
ATOM   1411 N  N   . ARG A 1 183 ? 28.30500  -26.96500 23.49100 1.000 35.37582 ? 183 ARG A N   1 
ATOM   1412 C  CA  . ARG A 1 183 ? 29.38400  -26.57000 22.55400 1.000 34.99482 ? 183 ARG A CA  1 
ATOM   1413 C  C   . ARG A 1 183 ? 29.25000  -27.17500 21.15800 1.000 36.33705 ? 183 ARG A C   1 
ATOM   1414 O  O   . ARG A 1 183 ? 29.53300  -26.46100 20.19800 1.000 36.39600 ? 183 ARG A O   1 
ATOM   1415 C  CB  . ARG A 1 183 ? 30.74400  -26.88300 23.18100 1.000 33.96046 ? 183 ARG A CB  1 
ATOM   1416 C  CG  . ARG A 1 183 ? 31.07000  -25.97700 24.35100 1.000 34.61928 ? 183 ARG A CG  1 
ATOM   1417 C  CD  . ARG A 1 183 ? 31.33800  -24.59300 23.81600 1.000 34.36182 ? 183 ARG A CD  1 
ATOM   1418 N  NE  . ARG A 1 183 ? 31.07200  -23.59700 24.85300 1.000 36.69254 ? 183 ARG A NE  1 
ATOM   1419 C  CZ  . ARG A 1 183 ? 31.36500  -22.31600 24.74900 1.000 38.45890 ? 183 ARG A CZ  1 
ATOM   1420 N  NH1 . ARG A 1 183 ? 32.24000  -21.90900 23.85200 1.000 36.80826 ? 183 ARG A NH1 1 
ATOM   1421 N  NH2 . ARG A 1 183 ? 30.80200  -21.45300 25.56700 1.000 39.67249 ? 183 ARG A NH2 1 
ATOM   1422 N  N   . ASP A 1 184 ? 28.85500  -28.44200 21.05300 1.000 38.21385 ? 184 ASP A N   1 
ATOM   1423 C  CA  . ASP A 1 184 ? 28.84300  -29.06200 19.72600 1.000 37.84211 ? 184 ASP A CA  1 
ATOM   1424 C  C   . ASP A 1 184 ? 27.61100  -28.69500 18.90300 1.000 38.18571 ? 184 ASP A C   1 
ATOM   1425 O  O   . ASP A 1 184 ? 27.45500  -29.21600 17.79400 1.000 38.33164 ? 184 ASP A O   1 
ATOM   1426 C  CB  . ASP A 1 184 ? 28.97800  -30.59200 19.83500 1.000 38.24641 ? 184 ASP A CB  1 
ATOM   1427 C  CG  . ASP A 1 184 ? 27.76000  -31.25400 20.44100 1.000 37.54331 ? 184 ASP A CG  1 
ATOM   1428 O  OD1 . ASP A 1 184 ? 27.29400  -30.79100 21.50300 1.000 37.99893 ? 184 ASP A OD1 1 
ATOM   1429 O  OD2 . ASP A 1 184 ? 27.26700  -32.24000 19.84900 1.000 38.42670 ? 184 ASP A OD2 1 
ATOM   1430 N  N   . GLN A 1 185 ? 26.73400  -27.82500 19.42500 1.000 37.27045 ? 185 GLN A N   1 
ATOM   1431 C  CA  . GLN A 1 185 ? 25.72900  -27.16700 18.59400 1.000 36.09609 ? 185 GLN A CA  1 
ATOM   1432 C  C   . GLN A 1 185 ? 26.37600  -26.17000 17.64400 1.000 33.63001 ? 185 GLN A C   1 
ATOM   1433 O  O   . GLN A 1 185 ? 25.85300  -25.91700 16.55500 1.000 33.16301 ? 185 GLN A O   1 
ATOM   1434 C  CB  . GLN A 1 185 ? 24.69700  -26.44600 19.46800 1.000 34.71143 ? 185 GLN A CB  1 
ATOM   1435 C  CG  . GLN A 1 185 ? 23.91400  -27.34100 20.40900 1.000 34.18667 ? 185 GLN A CG  1 
ATOM   1436 C  CD  . GLN A 1 185 ? 22.88800  -26.58100 21.24400 1.000 34.50378 ? 185 GLN A CD  1 
ATOM   1437 O  OE1 . GLN A 1 185 ? 22.94300  -26.58600 22.47900 1.000 36.60338 ? 185 GLN A OE1 1 
ATOM   1438 N  NE2 . GLN A 1 185 ? 21.94300  -25.94000 20.57600 1.000 32.56893 ? 185 GLN A NE2 1 
ATOM   1439 N  N   . ALA A 1 186 ? 27.50300  -25.59700 18.04600 1.000 32.44374 ? 186 ALA A N   1 
ATOM   1440 C  CA  . ALA A 1 186 ? 28.20500  -24.60000 17.26300 1.000 30.96385 ? 186 ALA A CA  1 
ATOM   1441 C  C   . ALA A 1 186 ? 29.14100  -25.26500 16.27000 1.000 31.43698 ? 186 ALA A C   1 
ATOM   1442 O  O   . ALA A 1 186 ? 29.64200  -26.36800 16.50600 1.000 32.57377 ? 186 ALA A O   1 
ATOM   1443 C  CB  . ALA A 1 186 ? 29.00300  -23.66700 18.16900 1.000 30.60343 ? 186 ALA A CB  1 
ATOM   1444 N  N   . VAL A 1 187 ? 29.36800  -24.57600 15.15200 1.000 32.98493 ? 187 VAL A N   1 
ATOM   1445 C  CA  . VAL A 1 187 ? 30.39200  -24.93600 14.18200 1.000 32.79236 ? 187 VAL A CA  1 
ATOM   1446 C  C   . VAL A 1 187 ? 31.47000  -23.86700 14.23100 1.000 32.59062 ? 187 VAL A C   1 
ATOM   1447 O  O   . VAL A 1 187 ? 31.20600  -22.71400 14.58100 1.000 31.48975 ? 187 VAL A O   1 
ATOM   1448 C  CB  . VAL A 1 187 ? 29.81600  -25.08500 12.76200 1.000 32.87553 ? 187 VAL A CB  1 
ATOM   1449 C  CG1 . VAL A 1 187 ? 28.79700  -26.19500 12.74800 1.000 33.70957 ? 187 VAL A CG1 1 
ATOM   1450 C  CG2 . VAL A 1 187 ? 29.19000  -23.77700 12.29300 1.000 30.56002 ? 187 VAL A CG2 1 
ATOM   1451 N  N   . LEU A 1 188 ? 32.69400  -24.26000 13.89800 1.000 32.43744 ? 188 LEU A N   1 
ATOM   1452 C  CA  . LEU A 1 188 ? 33.85900  -23.40900 14.10100 1.000 31.78595 ? 188 LEU A CA  1 
ATOM   1453 C  C   . LEU A 1 188 ? 34.16500  -22.57800 12.86400 1.000 30.74956 ? 188 LEU A C   1 
ATOM   1454 O  O   . LEU A 1 188 ? 34.16000  -23.07800 11.73500 1.000 31.60128 ? 188 LEU A O   1 
ATOM   1455 C  CB  . LEU A 1 188 ? 35.08300  -24.24400 14.47700 1.000 32.56533 ? 188 LEU A CB  1 
ATOM   1456 C  CG  . LEU A 1 188 ? 35.35300  -24.30000 15.98000 1.000 33.09682 ? 188 LEU A CG  1 
ATOM   1457 C  CD1 . LEU A 1 188 ? 34.21500  -24.96400 16.70000 1.000 33.43835 ? 188 LEU A CD1 1 
ATOM   1458 C  CD2 . LEU A 1 188 ? 36.64300  -25.01900 16.26900 1.000 34.91545 ? 188 LEU A CD2 1 
ATOM   1459 N  N   . ALA A 1 189 ? 34.43200  -21.30000 13.08800 1.000 30.40057 ? 189 ALA A N   1 
ATOM   1460 C  CA  . ALA A 1 189 ? 34.92600  -20.42900 12.03000 1.000 30.35209 ? 189 ALA A CA  1 
ATOM   1461 C  C   . ALA A 1 189 ? 36.45300  -20.50100 12.01200 1.000 30.89023 ? 189 ALA A C   1 
ATOM   1462 O  O   . ALA A 1 189 ? 37.16100  -19.56200 12.35800 1.000 33.72043 ? 189 ALA A O   1 
ATOM   1463 C  CB  . ALA A 1 189 ? 34.42400  -19.00400 12.23500 1.000 29.15972 ? 189 ALA A CB  1 
ATOM   1464 N  N   . THR A 1 190 ? 36.95900  -21.66300 11.61900 1.000 32.33044 ? 190 THR A N   1 
ATOM   1465 C  CA  . THR A 1 190 ? 38.38900  -21.80500 11.39500 1.000 32.97249 ? 190 THR A CA  1 
ATOM   1466 C  C   . THR A 1 190 ? 38.77300  -21.01300 10.14900 1.000 34.00954 ? 190 THR A C   1 
ATOM   1467 O  O   . THR A 1 190 ? 38.24800  -21.25900 9.05800  1.000 34.18667 ? 190 THR A O   1 
ATOM   1468 C  CB  . THR A 1 190 ? 38.76900  -23.28000 11.25500 1.000 33.22863 ? 190 THR A CB  1 
ATOM   1469 O  OG1 . THR A 1 190 ? 37.86000  -23.93700 10.36400 1.000 33.74069 ? 190 THR A OG1 1 
ATOM   1470 C  CG2 . THR A 1 190 ? 38.72100  -23.96500 12.59500 1.000 32.14996 ? 190 THR A CG2 1 
ATOM   1471 N  N   . MET A 1 191 ? 39.67900  -20.05400 10.31500 1.000 34.47651 ? 191 MET A N   1 
ATOM   1472 C  CA  . MET A 1 191 ? 39.99400  -19.08400 9.27800  1.000 36.15678 ? 191 MET A CA  1 
ATOM   1473 C  C   . MET A 1 191 ? 41.48600  -18.79300 9.28000  1.000 38.13190 ? 191 MET A C   1 
ATOM   1474 O  O   . MET A 1 191 ? 42.19500  -19.07000 10.24700 1.000 37.54859 ? 191 MET A O   1 
ATOM   1475 C  CB  . MET A 1 191 ? 39.23300  -17.76400 9.47600  1.000 34.13489 ? 191 MET A CB  1 
ATOM   1476 C  CG  . MET A 1 191 ? 37.82300  -17.76100 8.94800  1.000 31.75545 ? 191 MET A CG  1 
ATOM   1477 S  SD  . MET A 1 191 ? 37.09600  -16.13600 9.12700  1.000 30.48879 ? 191 MET A SD  1 
ATOM   1478 C  CE  . MET A 1 191 ? 37.31600  -15.87300 10.87900 1.000 28.79148 ? 191 MET A CE  1 
ATOM   1479 N  N   . ASP A 1 192 ? 41.94200  -18.20400 8.18800  1.000 42.56974 ? 192 ASP A N   1 
ATOM   1480 C  CA  . ASP A 1 192 ? 43.30300  -17.73300 8.00700  1.000 42.50215 ? 192 ASP A CA  1 
ATOM   1481 C  C   . ASP A 1 192 ? 43.30500  -16.20600 7.94700  1.000 41.62385 ? 192 ASP A C   1 
ATOM   1482 O  O   . ASP A 1 192 ? 42.26700  -15.59300 7.67100  1.000 40.51078 ? 192 ASP A O   1 
ATOM   1483 C  CB  . ASP A 1 192 ? 43.89000  -18.33600 6.71900  1.000 44.31633 ? 192 ASP A CB  1 
ATOM   1484 C  CG  . ASP A 1 192 ? 43.84900  -19.87400 6.71400  1.000 45.41643 ? 192 ASP A CG  1 
ATOM   1485 O  OD1 . ASP A 1 192 ? 44.60100  -20.49100 7.49800  1.000 49.26564 ? 192 ASP A OD1 1 
ATOM   1486 O  OD2 . ASP A 1 192 ? 43.05300  -20.46900 5.94700  1.000 45.45322 ? 192 ASP A OD2 1 
ATOM   1487 N  N   . PRO A 1 193 ? 44.43600  -15.55200 8.23500  1.000 39.78351 ? 193 PRO A N   1 
ATOM   1488 C  CA  . PRO A 1 193 ? 44.45600  -14.08000 8.20100  1.000 37.43853 ? 193 PRO A CA  1 
ATOM   1489 C  C   . PRO A 1 193 ? 44.09700  -13.56500 6.81500  1.000 36.73483 ? 193 PRO A C   1 
ATOM   1490 O  O   . PRO A 1 193 ? 44.70800  -13.94400 5.81600  1.000 37.47894 ? 193 PRO A O   1 
ATOM   1491 C  CB  . PRO A 1 193 ? 45.90300  -13.73200 8.57600  1.000 36.19178 ? 193 PRO A CB  1 
ATOM   1492 C  CG  . PRO A 1 193 ? 46.41100  -14.90400 9.27900  1.000 36.47915 ? 193 PRO A CG  1 
ATOM   1493 C  CD  . PRO A 1 193 ? 45.73400  -16.09600 8.66500  1.000 39.68963 ? 193 PRO A CD  1 
ATOM   1494 N  N   . GLY A 1 194 ? 43.08300  -12.70000 6.76200  1.000 34.45624 ? 194 GLY A N   1 
ATOM   1495 C  CA  . GLY A 1 194 ? 42.56900  -12.14400 5.52200  1.000 33.18242 ? 194 GLY A CA  1 
ATOM   1496 C  C   . GLY A 1 194 ? 41.11600  -12.48800 5.27100  1.000 31.95816 ? 194 GLY A C   1 
ATOM   1497 O  O   . GLY A 1 194 ? 40.42400  -11.75400 4.56200  1.000 31.49008 ? 194 GLY A O   1 
ATOM   1498 N  N   . ASP A 1 195 ? 40.64600  -13.60200 5.82400  1.000 33.15474 ? 195 ASP A N   1 
ATOM   1499 C  CA  . ASP A 1 195 ? 39.24000  -13.95300 5.74800  1.000 31.90890 ? 195 ASP A CA  1 
ATOM   1500 C  C   . ASP A 1 195 ? 38.42400  -12.99900 6.61400  1.000 31.17649 ? 195 ASP A C   1 
ATOM   1501 O  O   . ASP A 1 195 ? 38.96000  -12.13600 7.31500  1.000 30.61064 ? 195 ASP A O   1 
ATOM   1502 C  CB  . ASP A 1 195 ? 39.02300  -15.39600 6.19200  1.000 32.50832 ? 195 ASP A CB  1 
ATOM   1503 C  CG  . ASP A 1 195 ? 39.88400  -16.38000 5.43100  1.000 33.66353 ? 195 ASP A CG  1 
ATOM   1504 O  OD1 . ASP A 1 195 ? 40.23200  -16.10200 4.26800  1.000 33.70690 ? 195 ASP A OD1 1 
ATOM   1505 O  OD2 . ASP A 1 195 ? 40.21300  -17.43500 6.00400  1.000 34.87062 ? 195 ASP A OD2 1 
ATOM   1506 N  N   . VAL A 1 196 ? 37.10400  -13.15100 6.55300  1.000 28.39415 ? 196 VAL A N   1 
ATOM   1507 C  CA  . VAL A 1 196 ? 36.18000  -12.34500 7.34900  1.000 26.93605 ? 196 VAL A CA  1 
ATOM   1508 C  C   . VAL A 1 196 ? 34.98100  -13.20900 7.72100  1.000 26.44372 ? 196 VAL A C   1 
ATOM   1509 O  O   . VAL A 1 196 ? 34.42600  -13.91300 6.87500  1.000 27.22651 ? 196 VAL A O   1 
ATOM   1510 C  CB  . VAL A 1 196 ? 35.71300  -11.07900 6.59900  1.000 26.32404 ? 196 VAL A CB  1 
ATOM   1511 C  CG1 . VAL A 1 196 ? 34.68400  -10.35900 7.40300  1.000 27.32647 ? 196 VAL A CG1 1 
ATOM   1512 C  CG2 . VAL A 1 196 ? 36.87000  -10.14500 6.34700  1.000 28.44943 ? 196 VAL A CG2 1 
ATOM   1513 N  N   . LEU A 1 197 ? 34.58900  -13.16100 8.99100  1.000 25.97301 ? 197 LEU A N   1 
ATOM   1514 C  CA  . LEU A 1 197 ? 33.36700  -13.79500 9.46400  1.000 26.07470 ? 197 LEU A CA  1 
ATOM   1515 C  C   . LEU A 1 197 ? 32.27700  -12.73500 9.58000  1.000 24.69741 ? 197 LEU A C   1 
ATOM   1516 O  O   . LEU A 1 197 ? 32.43700  -11.76000 10.31700 1.000 24.46164 ? 197 LEU A O   1 
ATOM   1517 C  CB  . LEU A 1 197 ? 33.60300  -14.46500 10.81400 1.000 25.86786 ? 197 LEU A CB  1 
ATOM   1518 C  CG  . LEU A 1 197 ? 32.38100  -15.09800 11.46500 1.000 26.24864 ? 197 LEU A CG  1 
ATOM   1519 C  CD1 . LEU A 1 197 ? 31.96200  -16.31500 10.68900 1.000 23.97768 ? 197 LEU A CD1 1 
ATOM   1520 C  CD2 . LEU A 1 197 ? 32.66300  -15.45700 12.89900 1.000 24.96435 ? 197 LEU A CD2 1 
ATOM   1521 N  N   . ILE A 1 198 ? 31.17900  -12.91100 8.85600  1.000 24.12598 ? 198 ILE A N   1 
ATOM   1522 C  CA  . ILE A 1 198 ? 30.05300  -11.99300 8.93200  1.000 23.98819 ? 198 ILE A CA  1 
ATOM   1523 C  C   . ILE A 1 198 ? 28.92200  -12.69500 9.65700  1.000 23.81662 ? 198 ILE A C   1 
ATOM   1524 O  O   . ILE A 1 198 ? 28.51700  -13.79400 9.26600  1.000 24.33613 ? 198 ILE A O   1 
ATOM   1525 C  CB  . ILE A 1 198 ? 29.60000  -11.51400 7.54700  1.000 24.21652 ? 198 ILE A CB  1 
ATOM   1526 C  CG1 . ILE A 1 198 ? 30.68800  -10.66900 6.88700  1.000 25.65430 ? 198 ILE A CG1 1 
ATOM   1527 C  CG2 . ILE A 1 198 ? 28.32700  -10.72000 7.67600  1.000 23.87847 ? 198 ILE A CG2 1 
ATOM   1528 C  CD1 . ILE A 1 198 ? 31.58800  -11.45600 5.96900  1.000 25.86693 ? 198 ILE A CD1 1 
ATOM   1529 N  N   . VAL A 1 199 ? 28.40800  -12.06200 10.70800 1.000 23.76438 ? 199 VAL A N   1 
ATOM   1530 C  CA  . VAL A 1 199 ? 27.46100  -12.69400 11.61500 1.000 24.00579 ? 199 VAL A CA  1 
ATOM   1531 C  C   . VAL A 1 199 ? 26.23100  -11.80000 11.75700 1.000 23.98190 ? 199 VAL A C   1 
ATOM   1532 O  O   . VAL A 1 199 ? 26.31500  -10.69200 12.30300 1.000 24.21560 ? 199 VAL A O   1 
ATOM   1533 C  CB  . VAL A 1 199 ? 28.09000  -12.99500 12.98100 1.000 22.72442 ? 199 VAL A CB  1 
ATOM   1534 C  CG1 . VAL A 1 199 ? 27.05900  -13.56800 13.92300 1.000 23.78564 ? 199 VAL A CG1 1 
ATOM   1535 C  CG2 . VAL A 1 199 ? 29.24500  -13.96300 12.81900 1.000 23.13081 ? 199 VAL A CG2 1 
ATOM   1536 N  N   . ARG A 1 200 ? 25.09500  -12.29200 11.26900 1.000 23.85911 ? 200 ARG A N   1 
ATOM   1537 C  CA  . ARG A 1 200 ? 23.81500  -11.61000 11.32800 1.000 23.19156 ? 200 ARG A CA  1 
ATOM   1538 C  C   . ARG A 1 200 ? 23.45000  -11.24700 12.76900 1.000 23.96026 ? 200 ARG A C   1 
ATOM   1539 O  O   . ARG A 1 200 ? 23.95400  -11.82100 13.73300 1.000 25.03468 ? 200 ARG A O   1 
ATOM   1540 C  CB  . ARG A 1 200 ? 22.74700  -12.51700 10.71800 1.000 24.54199 ? 200 ARG A CB  1 
ATOM   1541 C  CG  . ARG A 1 200 ? 21.44500  -11.86400 10.33800 1.000 26.04306 ? 200 ARG A CG  1 
ATOM   1542 C  CD  . ARG A 1 200 ? 20.29300  -12.85800 10.45400 1.000 26.79224 ? 200 ARG A CD  1 
ATOM   1543 N  NE  . ARG A 1 200 ? 19.06600  -12.31800 9.88600  1.000 28.18201 ? 200 ARG A NE  1 
ATOM   1544 C  CZ  . ARG A 1 200 ? 18.16200  -11.64100 10.57500 1.000 29.86606 ? 200 ARG A CZ  1 
ATOM   1545 N  NH1 . ARG A 1 200 ? 18.28400  -11.45200 11.88100 1.000 30.28264 ? 200 ARG A NH1 1 
ATOM   1546 N  NH2 . ARG A 1 200 ? 17.11000  -11.13700 9.94100  1.000 31.56528 ? 200 ARG A NH2 1 
ATOM   1547 N  N   . GLN A 1 201 ? 22.56200  -10.26700 12.90200 1.000 23.69335 ? 201 GLN A N   1 
ATOM   1548 C  CA  . GLN A 1 201 ? 21.95600  -9.94300  14.18600 1.000 25.33750 ? 201 GLN A CA  1 
ATOM   1549 C  C   . GLN A 1 201 ? 21.27200  -11.16900 14.78900 1.000 26.77772 ? 201 GLN A C   1 
ATOM   1550 O  O   . GLN A 1 201 ? 20.68200  -11.98400 14.07600 1.000 27.08554 ? 201 GLN A O   1 
ATOM   1551 C  CB  . GLN A 1 201 ? 20.94700  -8.81000  13.99300 1.000 25.42958 ? 201 GLN A CB  1 
ATOM   1552 C  CG  . GLN A 1 201 ? 20.09700  -8.46100  15.19300 1.000 26.81434 ? 201 GLN A CG  1 
ATOM   1553 C  CD  . GLN A 1 201 ? 19.17700  -7.29500  14.89500 1.000 25.63086 ? 201 GLN A CD  1 
ATOM   1554 O  OE1 . GLN A 1 201 ? 19.31700  -6.64200  13.86600 1.000 24.29550 ? 201 GLN A OE1 1 
ATOM   1555 N  NE2 . GLN A 1 201 ? 18.23800  -7.02700  15.79200 1.000 25.51513 ? 201 GLN A NE2 1 
ATOM   1556 N  N   . ARG A 1 202 ? 21.38200  -11.30700 16.11200 1.000 26.10242 ? 202 ARG A N   1 
ATOM   1557 C  CA  . ARG A 1 202 ? 20.71100  -12.30700 16.93900 1.000 26.98173 ? 202 ARG A CA  1 
ATOM   1558 C  C   . ARG A 1 202 ? 21.31000  -13.70600 16.84400 1.000 28.11150 ? 202 ARG A C   1 
ATOM   1559 O  O   . ARG A 1 202 ? 20.71700  -14.64900 17.38900 1.000 27.80542 ? 202 ARG A O   1 
ATOM   1560 C  CB  . ARG A 1 202 ? 19.22100  -12.39800 16.61500 1.000 27.17360 ? 202 ARG A CB  1 
ATOM   1561 C  CG  . ARG A 1 202 ? 18.36500  -12.66900 17.79300 1.000 28.16200 ? 202 ARG A CG  1 
ATOM   1562 C  CD  . ARG A 1 202 ? 16.92800  -12.55000 17.40700 1.000 29.65998 ? 202 ARG A CD  1 
ATOM   1563 N  NE  . ARG A 1 202 ? 16.29500  -11.48400 18.16600 1.000 31.00161 ? 202 ARG A NE  1 
ATOM   1564 C  CZ  . ARG A 1 202 ? 15.94100  -10.31000 17.66900 1.000 30.27429 ? 202 ARG A CZ  1 
ATOM   1565 N  NH1 . ARG A 1 202 ? 16.04700  -10.04100 16.38000 1.000 30.76569 ? 202 ARG A NH1 1 
ATOM   1566 N  NH2 . ARG A 1 202 ? 15.47700  -9.37800  18.49100 1.000 30.60718 ? 202 ARG A NH2 1 
ATOM   1567 N  N   . VAL A 1 203 ? 22.45800  -13.88500 16.19200 1.000 27.02507 ? 203 VAL A N   1 
ATOM   1568 C  CA  . VAL A 1 203 ? 23.10100  -15.19700 16.14700 1.000 26.81382 ? 203 VAL A CA  1 
ATOM   1569 C  C   . VAL A 1 203 ? 23.90000  -15.40900 17.42600 1.000 27.57969 ? 203 VAL A C   1 
ATOM   1570 O  O   . VAL A 1 203 ? 24.59200  -14.50100 17.90400 1.000 28.20446 ? 203 VAL A O   1 
ATOM   1571 C  CB  . VAL A 1 203 ? 23.99000  -15.32800 14.89700 1.000 26.14285 ? 203 VAL A CB  1 
ATOM   1572 C  CG1 . VAL A 1 203 ? 24.69200  -16.67400 14.88000 1.000 23.98943 ? 203 VAL A CG1 1 
ATOM   1573 C  CG2 . VAL A 1 203 ? 23.16200  -15.13900 13.63500 1.000 25.95961 ? 203 VAL A CG2 1 
ATOM   1574 N  N   . VAL A 1 204 ? 23.78800  -16.61700 17.99700 1.000 28.68774 ? 204 VAL A N   1 
ATOM   1575 C  CA  . VAL A 1 204 ? 24.44500  -16.98200 19.24600 1.000 28.18511 ? 204 VAL A CA  1 
ATOM   1576 C  C   . VAL A 1 204 ? 25.82200  -17.53700 18.92400 1.000 28.92424 ? 204 VAL A C   1 
ATOM   1577 O  O   . VAL A 1 204 ? 25.99500  -18.28600 17.96000 1.000 28.73286 ? 204 VAL A O   1 
ATOM   1578 C  CB  . VAL A 1 204 ? 23.58700  -17.99800 20.01900 1.000 28.57590 ? 204 VAL A CB  1 
ATOM   1579 C  CG1 . VAL A 1 204 ? 24.21500  -18.32400 21.33800 1.000 29.57259 ? 204 VAL A CG1 1 
ATOM   1580 C  CG2 . VAL A 1 204 ? 22.19400  -17.44500 20.23600 1.000 28.97921 ? 204 VAL A CG2 1 
ATOM   1581 N  N   . HIS A 1 205 ? 26.81100  -17.16700 19.71300 1.000 29.58010 ? 205 HIS A N   1 
ATOM   1582 C  CA  . HIS A 1 205 ? 28.19100  -17.41200 19.32300 1.000 29.43832 ? 205 HIS A CA  1 
ATOM   1583 C  C   . HIS A 1 205 ? 29.08100  -17.04400 20.50000 1.000 30.52660 ? 205 HIS A C   1 
ATOM   1584 O  O   . HIS A 1 205 ? 28.60700  -16.55900 21.53000 1.000 30.41907 ? 205 HIS A O   1 
ATOM   1585 C  CB  . HIS A 1 205 ? 28.55800  -16.59600 18.08700 1.000 28.84775 ? 205 HIS A CB  1 
ATOM   1586 C  CG  . HIS A 1 205 ? 28.48900  -15.12400 18.32200 1.000 29.66095 ? 205 HIS A CG  1 
ATOM   1587 N  ND1 . HIS A 1 205 ? 27.29700  -14.44700 18.42800 1.000 29.35083 ? 205 HIS A ND1 1 
ATOM   1588 C  CD2 . HIS A 1 205 ? 29.46100  -14.20700 18.52500 1.000 30.39042 ? 205 HIS A CD2 1 
ATOM   1589 C  CE1 . HIS A 1 205 ? 27.53600  -13.17200 18.66600 1.000 29.78084 ? 205 HIS A CE1 1 
ATOM   1590 N  NE2 . HIS A 1 205 ? 28.84200  -13.00000 18.72800 1.000 30.71229 ? 205 HIS A NE2 1 
ATOM   1591 N  N   . ALA A 1 206 ? 30.38400  -17.25600 20.32600 1.000 29.93690 ? 206 ALA A N   1 
ATOM   1592 C  CA  . ALA A 1 206 ? 31.35300  -17.03600 21.38800 1.000 30.60045 ? 206 ALA A CA  1 
ATOM   1593 C  C   . ALA A 1 206 ? 32.74900  -17.24800 20.82600 1.000 31.16191 ? 206 ALA A C   1 
ATOM   1594 O  O   . ALA A 1 206 ? 32.94400  -18.04700 19.90600 1.000 31.04061 ? 206 ALA A O   1 
ATOM   1595 C  CB  . ALA A 1 206 ? 31.11200  -17.97800 22.57800 1.000 30.72665 ? 206 ALA A CB  1 
ATOM   1596 N  N   . GLY A 1 207 ? 33.71400  -16.52400 21.39000 1.000 34.12130 ? 207 GLY A N   1 
ATOM   1597 C  CA  . GLY A 1 207 ? 35.10500  -16.79500 21.09600 1.000 33.85518 ? 207 GLY A CA  1 
ATOM   1598 C  C   . GLY A 1 207 ? 35.56300  -18.02200 21.86400 1.000 36.12325 ? 207 GLY A C   1 
ATOM   1599 O  O   . GLY A 1 207 ? 35.12900  -18.27700 22.98800 1.000 36.85909 ? 207 GLY A O   1 
ATOM   1600 N  N   . GLY A 1 208 ? 36.45800  -18.78800 21.23800 1.000 33.94711 ? 208 GLY A N   1 
ATOM   1601 C  CA  . GLY A 1 208 ? 36.89900  -20.02800 21.83400 1.000 36.46989 ? 208 GLY A CA  1 
ATOM   1602 C  C   . GLY A 1 208 ? 38.04000  -19.84400 22.80600 1.000 37.82715 ? 208 GLY A C   1 
ATOM   1603 O  O   . GLY A 1 208 ? 38.62500  -18.76800 22.92000 1.000 36.56162 ? 208 GLY A O   1 
ATOM   1604 N  N   . GLY A 1 209 ? 38.34900  -20.93000 23.51400 1.000 39.53283 ? 209 GLY A N   1 
ATOM   1605 C  CA  . GLY A 1 209 ? 39.49200  -20.93500 24.41300 1.000 40.93799 ? 209 GLY A CA  1 
ATOM   1606 C  C   . GLY A 1 209 ? 40.78500  -21.21500 23.66200 1.000 40.90775 ? 209 GLY A C   1 
ATOM   1607 O  O   . GLY A 1 209 ? 40.83800  -22.04700 22.75800 1.000 41.02581 ? 209 GLY A O   1 
ATOM   1608 N  N   . ASN A 1 210 ? 41.83800  -20.49700 24.03800 1.000 40.47746 ? 210 ASN A N   1 
ATOM   1609 C  CA  . ASN A 1 210 ? 43.12300  -20.67600 23.36900 1.000 40.55431 ? 210 ASN A CA  1 
ATOM   1610 C  C   . ASN A 1 210 ? 43.80400  -21.86300 24.02800 1.000 41.19749 ? 210 ASN A C   1 
ATOM   1611 O  O   . ASN A 1 210 ? 44.32700  -21.76200 25.13700 1.000 43.01889 ? 210 ASN A O   1 
ATOM   1612 C  CB  . ASN A 1 210 ? 43.97600  -19.41200 23.44200 1.000 41.72609 ? 210 ASN A CB  1 
ATOM   1613 C  CG  . ASN A 1 210 ? 45.12500  -19.41600 22.43100 1.000 41.33563 ? 210 ASN A CG  1 
ATOM   1614 O  OD1 . ASN A 1 210 ? 45.42400  -20.43800 21.82000 1.000 42.48004 ? 210 ASN A OD1 1 
ATOM   1615 N  ND2 . ASN A 1 210 ? 45.77600  -18.27400 22.26500 1.000 39.90817 ? 210 ASN A ND2 1 
ATOM   1616 N  N   . ARG A 1 211 ? 43.76900  -23.00700 23.35200 1.000 38.35157 ? 211 ARG A N   1 
ATOM   1617 C  CA  . ARG A 1 211 ? 44.38300  -24.22500 23.85700 1.000 39.45220 ? 211 ARG A CA  1 
ATOM   1618 C  C   . ARG A 1 211 ? 45.67100  -24.56800 23.11500 1.000 39.53009 ? 211 ARG A C   1 
ATOM   1619 O  O   . ARG A 1 211 ? 46.00100  -25.74400 22.94900 1.000 41.45993 ? 211 ARG A O   1 
ATOM   1620 C  CB  . ARG A 1 211 ? 43.38300  -25.38400 23.80100 1.000 38.45960 ? 211 ARG A CB  1 
ATOM   1621 C  CG  . ARG A 1 211 ? 42.23700  -25.23600 24.80200 1.000 38.03500 ? 211 ARG A CG  1 
ATOM   1622 C  CD  . ARG A 1 211 ? 41.39400  -26.49800 24.92300 1.000 39.13982 ? 211 ARG A CD  1 
ATOM   1623 N  NE  . ARG A 1 211 ? 40.67300  -26.80300 23.69600 1.000 39.09762 ? 211 ARG A NE  1 
ATOM   1624 C  CZ  . ARG A 1 211 ? 41.05000  -27.71800 22.81600 1.000 40.40143 ? 211 ARG A CZ  1 
ATOM   1625 N  NH1 . ARG A 1 211 ? 42.12500  -28.46400 23.01200 1.000 42.18482 ? 211 ARG A NH1 1 
ATOM   1626 N  NH2 . ARG A 1 211 ? 40.32900  -27.89300 21.71300 1.000 41.29588 ? 211 ARG A NH2 1 
ATOM   1627 N  N   . THR A 1 212 ? 46.41000  -23.56000 22.67200 1.000 42.88038 ? 212 THR A N   1 
ATOM   1628 C  CA  . THR A 1 212 ? 47.72900  -23.76400 22.10100 1.000 42.81133 ? 212 THR A CA  1 
ATOM   1629 C  C   . THR A 1 212 ? 48.79200  -23.69500 23.18700 1.000 45.01164 ? 212 THR A C   1 
ATOM   1630 O  O   . THR A 1 212 ? 48.57700  -23.14900 24.27200 1.000 45.43368 ? 212 THR A O   1 
ATOM   1631 C  CB  . THR A 1 212 ? 48.04100  -22.72500 21.02700 1.000 41.58910 ? 212 THR A CB  1 
ATOM   1632 O  OG1 . THR A 1 212 ? 48.01500  -21.41400 21.60600 1.000 41.44093 ? 212 THR A OG1 1 
ATOM   1633 C  CG2 . THR A 1 212 ? 47.03400  -22.81300 19.90600 1.000 41.93136 ? 212 THR A CG2 1 
ATOM   1634 N  N   . THR A 1 213 ? 49.95900  -24.25000 22.86400 1.000 40.82059 ? 213 THR A N   1 
ATOM   1635 C  CA  . THR A 1 213 ? 51.09800  -24.31400 23.76400 1.000 43.02788 ? 213 THR A CA  1 
ATOM   1636 C  C   . THR A 1 213 ? 52.27500  -23.45700 23.31800 1.000 45.27772 ? 213 THR A C   1 
ATOM   1637 O  O   . THR A 1 213 ? 53.09100  -23.06300 24.15500 1.000 45.84859 ? 213 THR A O   1 
ATOM   1638 C  CB  . THR A 1 213 ? 51.55900  -25.76700 23.90900 1.000 43.66663 ? 213 THR A CB  1 
ATOM   1639 O  OG1 . THR A 1 213 ? 51.62300  -26.36500 22.61300 1.000 46.73437 ? 213 THR A OG1 1 
ATOM   1640 C  CG2 . THR A 1 213 ? 50.57200  -26.55500 24.74800 1.000 45.37617 ? 213 THR A CG2 1 
ATOM   1641 N  N   . ALA A 1 214 ? 52.37900  -23.15700 22.02500 1.000 45.29187 ? 214 ALA A N   1 
ATOM   1642 C  CA  . ALA A 1 214 ? 53.42500  -22.29500 21.49600 1.000 43.60765 ? 214 ALA A CA  1 
ATOM   1643 C  C   . ALA A 1 214 ? 52.84600  -21.43300 20.38200 1.000 43.64822 ? 214 ALA A C   1 
ATOM   1644 O  O   . ALA A 1 214 ? 51.90100  -21.82900 19.69300 1.000 44.01913 ? 214 ALA A O   1 
ATOM   1645 C  CB  . ALA A 1 214 ? 54.61900  -23.10500 20.97200 1.000 44.73971 ? 214 ALA A CB  1 
ATOM   1646 N  N   . GLY A 1 215 ? 53.41100  -20.24600 20.22000 1.000 44.15779 ? 215 GLY A N   1 
ATOM   1647 C  CA  . GLY A 1 215 ? 53.03300  -19.34900 19.14800 1.000 41.28592 ? 215 GLY A CA  1 
ATOM   1648 C  C   . GLY A 1 215 ? 52.32900  -18.10300 19.66000 1.000 40.17631 ? 215 GLY A C   1 
ATOM   1649 O  O   . GLY A 1 215 ? 51.97500  -17.97700 20.83300 1.000 40.30296 ? 215 GLY A O   1 
ATOM   1650 N  N   . LYS A 1 216 ? 52.12000  -17.18200 18.72700 1.000 38.29096 ? 216 LYS A N   1 
ATOM   1651 C  CA  . LYS A 1 216 ? 51.54700  -15.89200 19.05100 1.000 37.06633 ? 216 LYS A CA  1 
ATOM   1652 C  C   . LYS A 1 216 ? 50.08200  -16.03900 19.46900 1.000 35.80271 ? 216 LYS A C   1 
ATOM   1653 O  O   . LYS A 1 216 ? 49.39200  -16.94900 19.00700 1.000 35.42352 ? 216 LYS A O   1 
ATOM   1654 C  CB  . LYS A 1 216 ? 51.67500  -14.96100 17.84800 1.000 39.28619 ? 216 LYS A CB  1 
ATOM   1655 C  CG  . LYS A 1 216 ? 53.03000  -14.25000 17.78400 1.000 39.83396 ? 216 LYS A CG  1 
ATOM   1656 C  CD  . LYS A 1 216 ? 53.24500  -13.46100 19.07800 1.000 40.21107 ? 216 LYS A CD  1 
ATOM   1657 C  CE  . LYS A 1 216 ? 54.70300  -13.31700 19.42800 1.000 44.14963 ? 216 LYS A CE  1 
ATOM   1658 N  NZ  . LYS A 1 216 ? 54.85200  -13.02100 20.87200 1.000 44.82149 ? 216 LYS A NZ  1 
ATOM   1659 N  N   . PRO A 1 217 ? 49.59200  -15.15900 20.35200 1.000 36.84091 ? 217 PRO A N   1 
ATOM   1660 C  CA  . PRO A 1 217 ? 48.18800  -15.23500 20.78600 1.000 34.76048 ? 217 PRO A CA  1 
ATOM   1661 C  C   . PRO A 1 217 ? 47.23500  -15.06400 19.61700 1.000 34.31318 ? 217 PRO A C   1 
ATOM   1662 O  O   . PRO A 1 217 ? 47.60300  -14.58000 18.54600 1.000 33.94856 ? 217 PRO A O   1 
ATOM   1663 C  CB  . PRO A 1 217 ? 48.04500  -14.06600 21.76700 1.000 34.33033 ? 217 PRO A CB  1 
ATOM   1664 C  CG  . PRO A 1 217 ? 49.41900  -13.72400 22.16400 1.000 35.81034 ? 217 PRO A CG  1 
ATOM   1665 C  CD  . PRO A 1 217 ? 50.31000  -14.05700 21.01200 1.000 36.31321 ? 217 PRO A CD  1 
ATOM   1666 N  N   . ARG A 1 218 ? 45.98400  -15.46200 19.83400 1.000 34.10214 ? 218 ARG A N   1 
ATOM   1667 C  CA  . ARG A 1 218 ? 44.96600  -15.22700 18.82400 1.000 33.63092 ? 218 ARG A CA  1 
ATOM   1668 C  C   . ARG A 1 218 ? 44.54600  -13.76500 18.87100 1.000 31.89770 ? 218 ARG A C   1 
ATOM   1669 O  O   . ARG A 1 218 ? 44.35200  -13.19400 19.95000 1.000 31.59785 ? 218 ARG A O   1 
ATOM   1670 C  CB  . ARG A 1 218 ? 43.75100  -16.13900 19.02500 1.000 33.43912 ? 218 ARG A CB  1 
ATOM   1671 C  CG  . ARG A 1 218 ? 42.79200  -16.12100 17.83300 1.000 31.83769 ? 218 ARG A CG  1 
ATOM   1672 C  CD  . ARG A 1 218 ? 41.63500  -17.08400 18.00000 1.000 32.72231 ? 218 ARG A CD  1 
ATOM   1673 N  NE  . ARG A 1 218 ? 40.73400  -16.69900 19.08000 1.000 33.12070 ? 218 ARG A NE  1 
ATOM   1674 C  CZ  . ARG A 1 218 ? 39.58800  -16.05000 18.91500 1.000 32.14176 ? 218 ARG A CZ  1 
ATOM   1675 N  NH1 . ARG A 1 218 ? 39.17400  -15.66800 17.72000 1.000 31.22956 ? 218 ARG A NH1 1 
ATOM   1676 N  NH2 . ARG A 1 218 ? 38.83400  -15.78500 19.97600 1.000 32.37206 ? 218 ARG A NH2 1 
ATOM   1677 N  N   . ARG A 1 219 ? 44.44300  -13.15300 17.69300 1.000 31.04749 ? 219 ARG A N   1 
ATOM   1678 C  CA  . ARG A 1 219 ? 43.95700  -11.78700 17.54300 1.000 29.63449 ? 219 ARG A CA  1 
ATOM   1679 C  C   . ARG A 1 219 ? 42.69500  -11.77800 16.70100 1.000 28.21986 ? 219 ARG A C   1 
ATOM   1680 O  O   . ARG A 1 219 ? 42.64600  -12.40800 15.64000 1.000 30.10045 ? 219 ARG A O   1 
ATOM   1681 C  CB  . ARG A 1 219 ? 44.99400  -10.88700 16.88400 1.000 28.91495 ? 219 ARG A CB  1 
ATOM   1682 C  CG  . ARG A 1 219 ? 45.84900  -10.14800 17.84400 1.000 28.57415 ? 219 ARG A CG  1 
ATOM   1683 C  CD  . ARG A 1 219 ? 46.77300  -9.24200  17.10500 1.000 27.96970 ? 219 ARG A CD  1 
ATOM   1684 N  NE  . ARG A 1 219 ? 47.85600  -8.79700  17.96600 1.000 30.22059 ? 219 ARG A NE  1 
ATOM   1685 C  CZ  . ARG A 1 219 ? 48.80400  -7.94800  17.59500 1.000 30.46369 ? 219 ARG A CZ  1 
ATOM   1686 N  NH1 . ARG A 1 219 ? 48.80700  -7.40200  16.39100 1.000 30.26412 ? 219 ARG A NH1 1 
ATOM   1687 N  NH2 . ARG A 1 219 ? 49.76800  -7.63600  18.45600 1.000 29.71465 ? 219 ARG A NH2 1 
ATOM   1688 N  N   . VAL A 1 220 ? 41.68900  -11.05200 17.16000 1.000 26.05954 ? 220 VAL A N   1 
ATOM   1689 C  CA  . VAL A 1 220 ? 40.48900  -10.83300 16.37100 1.000 27.29082 ? 220 VAL A CA  1 
ATOM   1690 C  C   . VAL A 1 220 ? 40.09600  -9.37300  16.53100 1.000 26.37935 ? 220 VAL A C   1 
ATOM   1691 O  O   . VAL A 1 220 ? 40.21700  -8.80800  17.62200 1.000 27.21374 ? 220 VAL A O   1 
ATOM   1692 C  CB  . VAL A 1 220 ? 39.35000  -11.80300 16.77500 1.000 27.20471 ? 220 VAL A CB  1 
ATOM   1693 C  CG1 . VAL A 1 220 ? 38.85000  -11.53900 18.17600 1.000 27.86725 ? 220 VAL A CG1 1 
ATOM   1694 C  CG2 . VAL A 1 220 ? 38.22300  -11.70500 15.82100 1.000 26.63436 ? 220 VAL A CG2 1 
ATOM   1695 N  N   . VAL A 1 221 ? 39.69400  -8.73900  15.43300 1.000 26.41205 ? 221 VAL A N   1 
ATOM   1696 C  CA  . VAL A 1 221 ? 39.12300  -7.39800  15.47000 1.000 25.18995 ? 221 VAL A CA  1 
ATOM   1697 C  C   . VAL A 1 221 ? 37.64600  -7.51500  15.13500 1.000 25.01861 ? 221 VAL A C   1 
ATOM   1698 O  O   . VAL A 1 221 ? 37.27200  -8.09900  14.10900 1.000 24.49716 ? 221 VAL A O   1 
ATOM   1699 C  CB  . VAL A 1 221 ? 39.84000  -6.42500  14.51600 1.000 25.35569 ? 221 VAL A CB  1 
ATOM   1700 C  CG1 . VAL A 1 221 ? 38.93200  -5.25500  14.18400 1.000 24.05106 ? 221 VAL A CG1 1 
ATOM   1701 C  CG2 . VAL A 1 221 ? 41.09300  -5.89300  15.15000 1.000 23.35061 ? 221 VAL A CG2 1 
ATOM   1702 N  N   . LEU A 1 222 ? 36.80900  -6.99100  16.01800 1.000 25.20857 ? 222 LEU A N   1 
ATOM   1703 C  CA  . LEU A 1 222 ? 35.36900  -7.00300  15.83900 1.000 24.19300 ? 222 LEU A CA  1 
ATOM   1704 C  C   . LEU A 1 222 ? 34.93100  -5.61000  15.42600 1.000 23.13927 ? 222 LEU A C   1 
ATOM   1705 O  O   . LEU A 1 222 ? 35.40500  -4.62200  15.98600 1.000 22.29978 ? 222 LEU A O   1 
ATOM   1706 C  CB  . LEU A 1 222 ? 34.65600  -7.43900  17.11900 1.000 24.23012 ? 222 LEU A CB  1 
ATOM   1707 C  CG  . LEU A 1 222 ? 35.01500  -8.84500  17.60200 1.000 24.77586 ? 222 LEU A CG  1 
ATOM   1708 C  CD1 . LEU A 1 222 ? 36.10100  -8.80500  18.65000 1.000 26.15055 ? 222 LEU A CD1 1 
ATOM   1709 C  CD2 . LEU A 1 222 ? 33.80400  -9.54100  18.13000 1.000 29.00830 ? 222 LEU A CD2 1 
ATOM   1710 N  N   . ALA A 1 223 ? 34.06600  -5.53900  14.41900 1.000 23.34633 ? 223 ALA A N   1 
ATOM   1711 C  CA  . ALA A 1 223 ? 33.50100  -4.27500  13.97500 1.000 22.21436 ? 223 ALA A CA  1 
ATOM   1712 C  C   . ALA A 1 223 ? 31.99700  -4.42500  13.97800 1.000 21.45724 ? 223 ALA A C   1 
ATOM   1713 O  O   . ALA A 1 223 ? 31.45600  -5.34800  13.38900 1.000 21.67923 ? 223 ALA A O   1 
ATOM   1714 C  CB  . ALA A 1 223 ? 34.00800  -3.89000  12.59200 1.000 21.09956 ? 223 ALA A CB  1 
HETATM 1715 C  C   . F2Y A 1 224 ? 29.25100  -2.41900  13.94000 1.000 20.06463 ? 224 F2Y A C   1 
HETATM 1716 O  O   . F2Y A 1 224 ? 29.34100  -1.23600  14.35900 1.000 19.55313 ? 224 F2Y A O   1 
HETATM 1717 C  CA  . F2Y A 1 224 ? 29.88100  -3.58300  14.74200 1.000 20.37859 ? 224 F2Y A CA  1 
HETATM 1718 N  N   . F2Y A 1 224 ? 31.32200  -3.53300  14.68200 1.000 20.94092 ? 224 F2Y A N   1 
HETATM 1719 C  CB  . F2Y A 1 224 ? 29.34000  -3.53800  16.17600 1.000 21.98215 ? 224 F2Y A CB  1 
HETATM 1720 C  CG  . F2Y A 1 224 ? 29.91800  -4.61800  17.03100 1.000 23.96192 ? 224 F2Y A CG  1 
HETATM 1721 C  CD1 . F2Y A 1 224 ? 30.39200  -5.80000  16.43300 1.000 23.93958 ? 224 F2Y A CD1 1 
HETATM 1722 C  CE1 . F2Y A 1 224 ? 30.94700  -6.81000  17.22300 1.000 24.40343 ? 224 F2Y A CE1 1 
HETATM 1723 F  F1  . F2Y A 1 224 ? 31.42900  -7.95100  16.68900 1.000 25.55044 ? 224 F2Y A F1  1 
HETATM 1724 C  CD2 . F2Y A 1 224 ? 29.99500  -4.48000  18.42100 1.000 24.44232 ? 224 F2Y A CD2 1 
HETATM 1725 C  CE2 . F2Y A 1 224 ? 30.54800  -5.50800  19.21800 1.000 26.49921 ? 224 F2Y A CE2 1 
HETATM 1726 F  F2  . F2Y A 1 224 ? 30.63700  -5.41400  20.56400 1.000 28.43456 ? 224 F2Y A F2  1 
HETATM 1727 C  CZ  . F2Y A 1 224 ? 31.02900  -6.67900  18.61800 1.000 26.29281 ? 224 F2Y A CZ  1 
HETATM 1728 O  OH  . F2Y A 1 224 ? 31.55500  -7.64500  19.44500 1.000 26.75991 ? 224 F2Y A OH  1 
ATOM   1729 N  N   . PHE A 1 225 ? 28.65900  -2.75700  12.80500 1.000 21.27465 ? 225 PHE A N   1 
ATOM   1730 C  CA  . PHE A 1 225 ? 27.88400  -1.80400  12.04300 1.000 19.86362 ? 225 PHE A CA  1 
ATOM   1731 C  C   . PHE A 1 225 ? 26.44900  -1.89200  12.48500 1.000 20.38252 ? 225 PHE A C   1 
ATOM   1732 O  O   . PHE A 1 225 ? 25.87800  -2.97300  12.52500 1.000 21.96346 ? 225 PHE A O   1 
ATOM   1733 C  CB  . PHE A 1 225 ? 28.01100  -2.07500  10.56200 1.000 19.63092 ? 225 PHE A CB  1 
ATOM   1734 C  CG  . PHE A 1 225 ? 29.38400  -1.84600  10.04000 1.000 19.21832 ? 225 PHE A CG  1 
ATOM   1735 C  CD1 . PHE A 1 225 ? 29.78500  -0.58600  9.65500  1.000 19.78581 ? 225 PHE A CD1 1 
ATOM   1736 C  CD2 . PHE A 1 225 ? 30.28000  -2.88700  9.95400  1.000 20.57161 ? 225 PHE A CD2 1 
ATOM   1737 C  CE1 . PHE A 1 225 ? 31.05300  -0.36700  9.18300  1.000 20.38422 ? 225 PHE A CE1 1 
ATOM   1738 C  CE2 . PHE A 1 225 ? 31.55300  -2.67600  9.48400  1.000 20.22052 ? 225 PHE A CE2 1 
ATOM   1739 C  CZ  . PHE A 1 225 ? 31.94100  -1.41400  9.09500  1.000 18.93322 ? 225 PHE A CZ  1 
ATOM   1740 N  N   . ASN A 1 226 ? 25.88000  -0.74800  12.84800 1.000 20.24510 ? 226 ASN A N   1 
ATOM   1741 C  CA  . ASN A 1 226 ? 24.51400  -0.66500  13.33100 1.000 20.43469 ? 226 ASN A CA  1 
ATOM   1742 C  C   . ASN A 1 226 ? 23.78200  0.44100   12.59500 1.000 20.37943 ? 226 ASN A C   1 
ATOM   1743 O  O   . ASN A 1 226 ? 24.39800  1.40100   12.12700 1.000 19.18621 ? 226 ASN A O   1 
ATOM   1744 C  CB  . ASN A 1 226 ? 24.45100  -0.37200  14.82600 1.000 21.22061 ? 226 ASN A CB  1 
ATOM   1745 C  CG  . ASN A 1 226 ? 24.99800  -1.49500  15.66800 1.000 20.71350 ? 226 ASN A CG  1 
ATOM   1746 O  OD1 . ASN A 1 226 ? 25.18100  -2.61700  15.19900 1.000 21.43676 ? 226 ASN A OD1 1 
ATOM   1747 N  ND2 . ASN A 1 226 ? 25.25200  -1.19800  16.93500 1.000 21.12303 ? 226 ASN A ND2 1 
ATOM   1748 N  N   . SER A 1 227 ? 22.45600  0.29500   12.50200 1.000 20.35127 ? 227 SER A N   1 
ATOM   1749 C  CA  . SER A 1 227 ? 21.62300  1.37100   11.98900 1.000 19.62923 ? 227 SER A CA  1 
ATOM   1750 C  C   . SER A 1 227 ? 22.03300  2.68400   12.63500 1.000 19.78295 ? 227 SER A C   1 
ATOM   1751 O  O   . SER A 1 227 ? 22.39200  2.72000   13.81300 1.000 19.81939 ? 227 SER A O   1 
ATOM   1752 C  CB  . SER A 1 227 ? 20.14400  1.08900   12.27600 1.000 20.56671 ? 227 SER A CB  1 
ATOM   1753 O  OG  . SER A 1 227 ? 19.33700  2.23400   12.03800 1.000 21.09580 ? 227 SER A OG  1 
ATOM   1754 N  N   . VAL A 1 228 ? 22.00500  3.76700   11.85300 1.000 19.92931 ? 228 VAL A N   1 
ATOM   1755 C  CA  . VAL A 1 228 ? 22.28900  5.07500   12.41900 1.000 19.07525 ? 228 VAL A CA  1 
ATOM   1756 C  C   . VAL A 1 228 ? 21.23300  5.49100   13.43100 1.000 19.51681 ? 228 VAL A C   1 
ATOM   1757 O  O   . VAL A 1 228 ? 21.40600  6.50900   14.09900 1.000 19.66218 ? 228 VAL A O   1 
ATOM   1758 C  CB  . VAL A 1 228 ? 22.44300  6.15400   11.31700 1.000 19.38158 ? 228 VAL A CB  1 
ATOM   1759 C  CG1 . VAL A 1 228 ? 23.62700  5.85000   10.41500 1.000 18.91895 ? 228 VAL A CG1 1 
ATOM   1760 C  CG2 . VAL A 1 228 ? 21.19500  6.26600   10.49000 1.000 20.93711 ? 228 VAL A CG2 1 
ATOM   1761 N  N   . GLN A 1 229 ? 20.15800  4.71400   13.59300 1.000 19.93844 ? 229 GLN A N   1 
ATOM   1762 C  CA  . GLN A 1 229 ? 19.20200  4.97600   14.66500 1.000 20.32853 ? 229 GLN A CA  1 
ATOM   1763 C  C   . GLN A 1 229 ? 19.76500  4.66800   16.04700 1.000 19.35461 ? 229 GLN A C   1 
ATOM   1764 O  O   . GLN A 1 229 ? 19.24000  5.17600   17.04400 1.000 18.62463 ? 229 GLN A O   1 
ATOM   1765 C  CB  . GLN A 1 229 ? 17.93600  4.14200   14.48400 1.000 21.29839 ? 229 GLN A CB  1 
ATOM   1766 C  CG  . GLN A 1 229 ? 17.17200  4.34400   13.19900 1.000 22.91075 ? 229 GLN A CG  1 
ATOM   1767 C  CD  . GLN A 1 229 ? 16.07700  3.33100   13.08200 1.000 23.90533 ? 229 GLN A CD  1 
ATOM   1768 O  OE1 . GLN A 1 229 ? 15.04500  3.46100   13.72000 1.000 24.69822 ? 229 GLN A OE1 1 
ATOM   1769 N  NE2 . GLN A 1 229 ? 16.31700  2.27700   12.31500 1.000 24.57432 ? 229 GLN A NE2 1 
ATOM   1770 N  N   . LEU A 1 230 ? 20.79500  3.83500   16.13600 1.000 18.97692 ? 230 LEU A N   1 
ATOM   1771 C  CA  . LEU A 1 230 ? 21.34500  3.39500   17.41000 1.000 18.56563 ? 230 LEU A CA  1 
ATOM   1772 C  C   . LEU A 1 230 ? 22.63300  4.14500   17.73700 1.000 19.20406 ? 230 LEU A C   1 
ATOM   1773 O  O   . LEU A 1 230 ? 23.51800  4.29000   16.88800 1.000 18.43097 ? 230 LEU A O   1 
ATOM   1774 C  CB  . LEU A 1 230 ? 21.61500  1.89200   17.38700 1.000 18.62790 ? 230 LEU A CB  1 
ATOM   1775 C  CG  . LEU A 1 230 ? 20.39900  1.02200   17.11600 1.000 19.22489 ? 230 LEU A CG  1 
ATOM   1776 C  CD1 . LEU A 1 230 ? 20.79000  -0.44200  17.13200 1.000 20.55960 ? 230 LEU A CD1 1 
ATOM   1777 C  CD2 . LEU A 1 230 ? 19.32700  1.31000   18.15500 1.000 19.92864 ? 230 LEU A CD2 1 
ATOM   1778 N  N   . THR A 1 231 ? 22.74200  4.58000   18.98600 1.000 18.83189 ? 231 THR A N   1 
ATOM   1779 C  CA  . THR A 1 231 ? 23.88200  5.37400   19.42000 1.000 18.57844 ? 231 THR A CA  1 
ATOM   1780 C  C   . THR A 1 231 ? 25.16400  4.54700   19.39300 1.000 19.12171 ? 231 THR A C   1 
ATOM   1781 O  O   . THR A 1 231 ? 25.18700  3.43800   19.92800 1.000 19.71542 ? 231 THR A O   1 
ATOM   1782 C  CB  . THR A 1 231 ? 23.62700  5.90300   20.82100 1.000 18.74980 ? 231 THR A CB  1 
ATOM   1783 O  OG1 . THR A 1 231 ? 22.48100  6.74900   20.80000 1.000 17.78478 ? 231 THR A OG1 1 
ATOM   1784 C  CG2 . THR A 1 231 ? 24.82500  6.69100   21.33100 1.000 18.60392 ? 231 THR A CG2 1 
ATOM   1785 N  N   . PRO A 1 232 ? 26.24400  5.04700   18.78500 1.000 18.75736 ? 232 PRO A N   1 
ATOM   1786 C  CA  . PRO A 1 232 ? 27.50800  4.29700   18.79500 1.000 19.34648 ? 232 PRO A CA  1 
ATOM   1787 C  C   . PRO A 1 232 ? 28.00900  4.06700   20.21600 1.000 19.58608 ? 232 PRO A C   1 
ATOM   1788 O  O   . PRO A 1 232 ? 27.88100  4.92500   21.09300 1.000 18.60403 ? 232 PRO A O   1 
ATOM   1789 C  CB  . PRO A 1 232 ? 28.46500  5.19300   17.99500 1.000 18.27813 ? 232 PRO A CB  1 
ATOM   1790 C  CG  . PRO A 1 232 ? 27.58100  6.05500   17.16700 1.000 18.83584 ? 232 PRO A CG  1 
ATOM   1791 C  CD  . PRO A 1 232 ? 26.33100  6.26800   17.96500 1.000 18.30592 ? 232 PRO A CD  1 
ATOM   1792 N  N   . PHE A 1 233 ? 28.55000  2.86900   20.44700 1.000 19.75796 ? 233 PHE A N   1 
ATOM   1793 C  CA  . PHE A 1 233 ? 29.20700  2.58000   21.71500 1.000 20.13529 ? 233 PHE A CA  1 
ATOM   1794 C  C   . PHE A 1 233 ? 30.42700  3.48700   21.90100 1.000 19.76234 ? 233 PHE A C   1 
ATOM   1795 O  O   . PHE A 1 233 ? 30.52800  4.23100   22.88400 1.000 19.95737 ? 233 PHE A O   1 
ATOM   1796 C  CB  . PHE A 1 233 ? 29.57400  1.08700   21.74800 1.000 20.98490 ? 233 PHE A CB  1 
ATOM   1797 C  CG  . PHE A 1 233 ? 30.32000  0.65600   22.97800 1.000 22.16052 ? 233 PHE A CG  1 
ATOM   1798 C  CD1 . PHE A 1 233 ? 29.70600  0.64200   24.21200 1.000 21.96615 ? 233 PHE A CD1 1 
ATOM   1799 C  CD2 . PHE A 1 233 ? 31.63500  0.23400   22.89000 1.000 22.02283 ? 233 PHE A CD2 1 
ATOM   1800 C  CE1 . PHE A 1 233 ? 30.38900  0.23300   25.33200 1.000 22.67326 ? 233 PHE A CE1 1 
ATOM   1801 C  CE2 . PHE A 1 233 ? 32.31800  -0.16700  24.01400 1.000 21.45453 ? 233 PHE A CE2 1 
ATOM   1802 C  CZ  . PHE A 1 233 ? 31.69400  -0.17000  25.23400 1.000 22.09224 ? 233 PHE A CZ  1 
ATOM   1803 N  N   . GLU A 1 234 ? 31.33900  3.47300   20.93300 1.000 20.09804 ? 234 GLU A N   1 
ATOM   1804 C  CA  . GLU A 1 234 ? 32.46700  4.38900   20.89900 1.000 19.45784 ? 234 GLU A CA  1 
ATOM   1805 C  C   . GLU A 1 234 ? 32.10200  5.63700   20.11000 1.000 19.35104 ? 234 GLU A C   1 
ATOM   1806 O  O   . GLU A 1 234 ? 31.51800  5.54200   19.03000 1.000 18.80418 ? 234 GLU A O   1 
ATOM   1807 C  CB  . GLU A 1 234 ? 33.66900  3.71200   20.24500 1.000 20.06940 ? 234 GLU A CB  1 
ATOM   1808 C  CG  . GLU A 1 234 ? 34.11800  2.46900   20.95000 1.000 19.54918 ? 234 GLU A CG  1 
ATOM   1809 C  CD  . GLU A 1 234 ? 35.12800  1.68500   20.15300 1.000 21.10740 ? 234 GLU A CD  1 
ATOM   1810 O  OE1 . GLU A 1 234 ? 35.17100  1.82700   18.90900 1.000 21.41621 ? 234 GLU A OE1 1 
ATOM   1811 O  OE2 . GLU A 1 234 ? 35.87900  0.91700   20.78500 1.000 21.98886 ? 234 GLU A OE2 1 
ATOM   1812 N  N   . THR A 1 235 ? 32.46100  6.80900   20.63900 1.000 19.98279 ? 235 THR A N   1 
ATOM   1813 C  CA  . THR A 1 235 ? 32.26500  8.06600   19.91900 1.000 20.40041 ? 235 THR A CA  1 
ATOM   1814 C  C   . THR A 1 235 ? 33.59400  8.60900   19.40600 1.000 20.52518 ? 235 THR A C   1 
ATOM   1815 O  O   . THR A 1 235 ? 34.54500  8.79800   20.17400 1.000 20.63582 ? 235 THR A O   1 
ATOM   1816 C  CB  . THR A 1 235 ? 31.55200  9.13500   20.75800 1.000 19.57644 ? 235 THR A CB  1 
ATOM   1817 O  OG1 . THR A 1 235 ? 31.41900  10.31600  19.96600 1.000 18.03163 ? 235 THR A OG1 1 
ATOM   1818 C  CG2 . THR A 1 235 ? 32.29400  9.47200   22.03700 1.000 19.79659 ? 235 THR A CG2 1 
ATOM   1819 N  N   . TYR A 1 236 ? 33.64500  8.86200   18.09800 1.000 20.83430 ? 236 TYR A N   1 
ATOM   1820 C  CA  . TYR A 1 236 ? 34.84300  9.30800   17.41000 1.000 20.02521 ? 236 TYR A CA  1 
ATOM   1821 C  C   . TYR A 1 236 ? 34.89600  10.82400  17.30100 1.000 19.76281 ? 236 TYR A C   1 
ATOM   1822 O  O   . TYR A 1 236 ? 35.71900  11.36400  16.56800 1.000 20.06743 ? 236 TYR A O   1 
ATOM   1823 C  CB  . TYR A 1 236 ? 34.92300  8.61200   16.04900 1.000 19.33326 ? 236 TYR A CB  1 
ATOM   1824 C  CG  . TYR A 1 236 ? 34.79300  7.10100   16.21600 1.000 20.19341 ? 236 TYR A CG  1 
ATOM   1825 C  CD1 . TYR A 1 236 ? 35.87200  6.36000   16.69900 1.000 21.02027 ? 236 TYR A CD1 1 
ATOM   1826 C  CD2 . TYR A 1 236 ? 33.59200  6.45300   15.92900 1.000 19.16602 ? 236 TYR A CD2 1 
ATOM   1827 C  CE1 . TYR A 1 236 ? 35.73800  5.00400   16.86500 1.000 20.55894 ? 236 TYR A CE1 1 
ATOM   1828 C  CE2 . TYR A 1 236 ? 33.49800  5.09100   16.10400 1.000 19.29490 ? 236 TYR A CE2 1 
ATOM   1829 C  CZ  . TYR A 1 236 ? 34.55900  4.33300   16.57600 1.000 19.85475 ? 236 TYR A CZ  1 
ATOM   1830 O  OH  . TYR A 1 236 ? 34.45900  2.99800   16.75600 1.000 19.40192 ? 236 TYR A OH  1 
ATOM   1831 N  N   . ARG A 1 237 ? 34.08800  11.51900  18.09200 1.000 20.43244 ? 237 ARG A N   1 
ATOM   1832 C  CA  . ARG A 1 237 ? 33.99100  12.96900  18.06100 1.000 20.93155 ? 237 ARG A CA  1 
ATOM   1833 C  C   . ARG A 1 237 ? 35.23400  13.66900  18.58000 1.000 21.69503 ? 237 ARG A C   1 
ATOM   1834 O  O   . ARG A 1 237 ? 35.29400  14.89800  18.50000 1.000 22.59548 ? 237 ARG A O   1 
ATOM   1835 C  CB  . ARG A 1 237 ? 32.78300  13.42600  18.88700 1.000 20.21999 ? 237 ARG A CB  1 
ATOM   1836 C  CG  . ARG A 1 237 ? 33.07200  13.54600  20.36600 1.000 19.74798 ? 237 ARG A CG  1 
ATOM   1837 C  CD  . ARG A 1 237 ? 31.92500  13.05400  21.19500 1.000 20.44564 ? 237 ARG A CD  1 
ATOM   1838 N  NE  . ARG A 1 237 ? 30.91200  14.06600  21.41300 1.000 20.46588 ? 237 ARG A NE  1 
ATOM   1839 C  CZ  . ARG A 1 237 ? 29.64900  13.80600  21.71500 1.000 20.79183 ? 237 ARG A CZ  1 
ATOM   1840 N  NH1 . ARG A 1 237 ? 29.18700  12.56700  21.77500 1.000 21.66326 ? 237 ARG A NH1 1 
ATOM   1841 N  NH2 . ARG A 1 237 ? 28.82400  14.81400  21.94800 1.000 21.81330 ? 237 ARG A NH2 1 
ATOM   1842 N  N   . THR A 1 238 ? 36.20800  12.95100  19.13600 1.000 21.56592 ? 238 THR A N   1 
ATOM   1843 C  CA  . THR A 1 238 ? 37.42100  13.60200  19.61000 1.000 21.67586 ? 238 THR A CA  1 
ATOM   1844 C  C   . THR A 1 238 ? 38.60300  13.36400  18.69300 1.000 22.08490 ? 238 THR A C   1 
ATOM   1845 O  O   . THR A 1 238 ? 39.73200  13.67600  19.07000 1.000 24.51356 ? 238 THR A O   1 
ATOM   1846 C  CB  . THR A 1 238 ? 37.78600  13.15900  21.02700 1.000 20.07005 ? 238 THR A CB  1 
ATOM   1847 O  OG1 . THR A 1 238 ? 38.21800  11.79300  21.01300 1.000 21.35991 ? 238 THR A OG1 1 
ATOM   1848 C  CG2 . THR A 1 238 ? 36.59800  13.33100  21.96300 1.000 21.64093 ? 238 THR A CG2 1 
ATOM   1849 N  N   . MET A 1 239 ? 38.37900  12.82600  17.50700 1.000 21.87604 ? 239 MET A N   1 
ATOM   1850 C  CA  . MET A 1 239 ? 39.46400  12.70800  16.55800 1.000 23.05255 ? 239 MET A CA  1 
ATOM   1851 C  C   . MET A 1 239 ? 39.91000  14.09600  16.10300 1.000 24.51239 ? 239 MET A C   1 
ATOM   1852 O  O   . MET A 1 239 ? 39.09400  15.01600  15.99500 1.000 24.60739 ? 239 MET A O   1 
ATOM   1853 C  CB  . MET A 1 239 ? 39.03800  11.87100  15.35900 1.000 22.68751 ? 239 MET A CB  1 
ATOM   1854 C  CG  . MET A 1 239 ? 38.83000  10.40200  15.69000 1.000 23.79807 ? 239 MET A CG  1 
ATOM   1855 S  SD  . MET A 1 239 ? 37.98300  9.48100   14.39700 1.000 24.79885 ? 239 MET A SD  1 
ATOM   1856 C  CE  . MET A 1 239 ? 38.96400  9.93400   12.97800 1.000 23.02122 ? 239 MET A CE  1 
ATOM   1857 N  N   . PRO A 1 240 ? 41.20700  14.28300  15.85800 1.000 26.21303 ? 240 PRO A N   1 
ATOM   1858 C  CA  . PRO A 1 240 ? 41.67800  15.57700  15.34200 1.000 27.94646 ? 240 PRO A CA  1 
ATOM   1859 C  C   . PRO A 1 240 ? 41.05900  15.90300  13.99000 1.000 27.12074 ? 240 PRO A C   1 
ATOM   1860 O  O   . PRO A 1 240 ? 40.75400  15.01200  13.19400 1.000 27.80702 ? 240 PRO A O   1 
ATOM   1861 C  CB  . PRO A 1 240 ? 43.19200  15.38200  15.22400 1.000 28.37630 ? 240 PRO A CB  1 
ATOM   1862 C  CG  . PRO A 1 240 ? 43.50900  14.28400  16.16300 1.000 28.50866 ? 240 PRO A CG  1 
ATOM   1863 C  CD  . PRO A 1 240 ? 42.31500  13.38100  16.20800 1.000 26.14137 ? 240 PRO A CD  1 
ATOM   1864 N  N   . ARG A 1 241 ? 40.88800  17.20600  13.72900 1.000 27.18203 ? 241 ARG A N   1 
ATOM   1865 C  CA  . ARG A 1 241 ? 40.28100  17.63600  12.47100 1.000 27.81069 ? 241 ARG A CA  1 
ATOM   1866 C  C   . ARG A 1 241 ? 41.14300  17.25600  11.27200 1.000 28.20880 ? 241 ARG A C   1 
ATOM   1867 O  O   . ARG A 1 241 ? 40.61400  16.86500  10.22600 1.000 29.08103 ? 241 ARG A O   1 
ATOM   1868 C  CB  . ARG A 1 241 ? 40.01600  19.14500  12.47100 1.000 29.06501 ? 241 ARG A CB  1 
ATOM   1869 C  CG  . ARG A 1 241 ? 39.59700  19.64100  11.09000 1.000 30.26206 ? 241 ARG A CG  1 
ATOM   1870 C  CD  . ARG A 1 241 ? 39.37400  21.13700  11.00400 1.000 31.38112 ? 241 ARG A CD  1 
ATOM   1871 N  NE  . ARG A 1 241 ? 38.05600  21.52400  11.49100 1.000 32.74507 ? 241 ARG A NE  1 
ATOM   1872 C  CZ  . ARG A 1 241 ? 36.92400  21.34900  10.82000 1.000 30.66590 ? 241 ARG A CZ  1 
ATOM   1873 N  NH1 . ARG A 1 241 ? 36.90600  20.76200  9.63600  1.000 29.95546 ? 241 ARG A NH1 1 
ATOM   1874 N  NH2 . ARG A 1 241 ? 35.78000  21.77000  11.35500 1.000 29.79819 ? 241 ARG A NH2 1 
ATOM   1875 N  N   . GLU A 1 242 ? 42.47200  17.37000  11.39000 1.000 28.98646 ? 242 GLU A N   1 
ATOM   1876 C  CA  . GLU A 1 242 ? 43.31500  16.89500  10.29600 1.000 28.85501 ? 242 GLU A CA  1 
ATOM   1877 C  C   . GLU A 1 242 ? 43.14300  15.39600  10.08800 1.000 27.76131 ? 242 GLU A C   1 
ATOM   1878 O  O   . GLU A 1 242 ? 43.18000  14.92700  8.94900  1.000 27.77243 ? 242 GLU A O   1 
ATOM   1879 C  CB  . GLU A 1 242 ? 44.78800  17.25500  10.52800 1.000 31.10252 ? 242 GLU A CB  1 
ATOM   1880 C  CG  . GLU A 1 242 ? 45.36100  16.91200  11.90100 1.000 34.21256 ? 242 GLU A CG  1 
ATOM   1881 C  CD  . GLU A 1 242 ? 45.35400  18.09500  12.86200 1.000 35.97353 ? 242 GLU A CD  1 
ATOM   1882 O  OE1 . GLU A 1 242 ? 44.34000  18.25900  13.57700 1.000 33.66471 ? 242 GLU A OE1 1 
ATOM   1883 O  OE2 . GLU A 1 242 ? 46.35100  18.86300  12.89000 1.000 38.12652 ? 242 GLU A OE2 1 
ATOM   1884 N  N   . MET A 1 243 ? 42.90000  14.63600  11.15800 1.000 28.33886 ? 243 MET A N   1 
ATOM   1885 C  CA  . MET A 1 243 ? 42.68800  13.19900  11.00500 1.000 27.82938 ? 243 MET A CA  1 
ATOM   1886 C  C   . MET A 1 243 ? 41.37000  12.90100  10.30100 1.000 27.22720 ? 243 MET A C   1 
ATOM   1887 O  O   . MET A 1 243 ? 41.32600  12.11300  9.35200  1.000 27.10158 ? 243 MET A O   1 
ATOM   1888 C  CB  . MET A 1 243 ? 42.72500  12.50400  12.36300 1.000 27.30152 ? 243 MET A CB  1 
ATOM   1889 C  CG  . MET A 1 243 ? 42.26500  11.06100  12.29100 1.000 26.31195 ? 243 MET A CG  1 
ATOM   1890 S  SD  . MET A 1 243 ? 42.48100  10.17400  13.81200 1.000 24.05933 ? 243 MET A SD  1 
ATOM   1891 C  CE  . MET A 1 243 ? 44.19300  10.56900  14.12000 1.000 25.13871 ? 243 MET A CE  1 
ATOM   1892 N  N   . VAL A 1 244 ? 40.28100  13.51200  10.75600 1.000 27.36540 ? 244 VAL A N   1 
ATOM   1893 C  CA  . VAL A 1 244 ? 38.98200  13.24000  10.15100 1.000 27.19538 ? 244 VAL A CA  1 
ATOM   1894 C  C   . VAL A 1 244 ? 38.93900  13.72500  8.70600  1.000 27.37432 ? 244 VAL A C   1 
ATOM   1895 O  O   . VAL A 1 244 ? 38.44400  13.02400  7.81400  1.000 26.00522 ? 244 VAL A O   1 
ATOM   1896 C  CB  . VAL A 1 244 ? 37.87500  13.87900  10.99900 1.000 25.86051 ? 244 VAL A CB  1 
ATOM   1897 C  CG1 . VAL A 1 244 ? 36.53600  13.68600  10.33600 1.000 24.50519 ? 244 VAL A CG1 1 
ATOM   1898 C  CG2 . VAL A 1 244 ? 37.87300  13.27300  12.36900 1.000 24.23348 ? 244 VAL A CG2 1 
ATOM   1899 N  N   . GLU A 1 245 ? 39.45700  14.92400  8.44600  1.000 28.32789 ? 245 GLU A N   1 
ATOM   1900 C  CA  . GLU A 1 245 ? 39.50900  15.42300  7.07700  1.000 27.98479 ? 245 GLU A CA  1 
ATOM   1901 C  C   . GLU A 1 245 ? 40.42600  14.57600  6.20400  1.000 27.45988 ? 245 GLU A C   1 
ATOM   1902 O  O   . GLU A 1 245 ? 40.28400  14.58400  4.97700  1.000 27.57243 ? 245 GLU A O   1 
ATOM   1903 C  CB  . GLU A 1 245 ? 39.92800  16.89700  7.08300  1.000 28.32455 ? 245 GLU A CB  1 
ATOM   1904 C  CG  . GLU A 1 245 ? 38.88600  17.79100  7.77100  1.000 28.68936 ? 245 GLU A CG  1 
ATOM   1905 C  CD  . GLU A 1 245 ? 39.23700  19.27400  7.80100  1.000 29.80284 ? 245 GLU A CD  1 
ATOM   1906 O  OE1 . GLU A 1 245 ? 40.43100  19.62500  7.86200  1.000 32.14234 ? 245 GLU A OE1 1 
ATOM   1907 O  OE2 . GLU A 1 245 ? 38.30500  20.09700  7.77200  1.000 29.66750 ? 245 GLU A OE2 1 
ATOM   1908 N  N   . SER A 1 246 ? 41.33000  13.80700  6.81100  1.000 27.12313 ? 246 SER A N   1 
ATOM   1909 C  CA  . SER A 1 246 ? 42.12100  12.85600  6.04100  1.000 28.19597 ? 246 SER A CA  1 
ATOM   1910 C  C   . SER A 1 246 ? 41.27600  11.69400  5.52700  1.000 27.36876 ? 246 SER A C   1 
ATOM   1911 O  O   . SER A 1 246 ? 41.62300  11.08300  4.51200  1.000 28.53077 ? 246 SER A O   1 
ATOM   1912 C  CB  . SER A 1 246 ? 43.27600  12.31900  6.88700  1.000 29.03362 ? 246 SER A CB  1 
ATOM   1913 O  OG  . SER A 1 246 ? 42.83000  11.26200  7.72300  1.000 28.75740 ? 246 SER A OG  1 
ATOM   1914 N  N   . MET A 1 247 ? 40.18500  11.36500  6.20400  1.000 26.96618 ? 247 MET A N   1 
ATOM   1915 C  CA  . MET A 1 247 ? 39.39900  10.20800  5.81200  1.000 26.63300 ? 247 MET A CA  1 
ATOM   1916 C  C   . MET A 1 247 ? 38.56200  10.51000  4.57100  1.000 26.88830 ? 247 MET A C   1 
ATOM   1917 O  O   . MET A 1 247 ? 38.41400  11.66200  4.15600  1.000 27.18428 ? 247 MET A O   1 
ATOM   1918 C  CB  . MET A 1 247 ? 38.51000  9.76600   6.96400  1.000 25.69874 ? 247 MET A CB  1 
ATOM   1919 C  CG  . MET A 1 247 ? 39.27700  9.50900   8.22100  1.000 24.59499 ? 247 MET A CG  1 
ATOM   1920 S  SD  . MET A 1 247 ? 38.25300  8.63100   9.36700  1.000 22.86141 ? 247 MET A SD  1 
ATOM   1921 C  CE  . MET A 1 247 ? 36.85100  9.71100   9.42900  1.000 24.25822 ? 247 MET A CE  1 
ATOM   1922 N  N   . THR A 1 248 ? 38.01700  9.44600   3.97300  1.000 26.50965 ? 248 THR A N   1 
ATOM   1923 C  CA  . THR A 1 248 ? 37.06600  9.55400   2.87500  1.000 27.11044 ? 248 THR A CA  1 
ATOM   1924 C  C   . THR A 1 248 ? 35.67600  9.89600   3.40500  1.000 25.20219 ? 248 THR A C   1 
ATOM   1925 O  O   . THR A 1 248 ? 35.37300  9.70900   4.58700  1.000 23.60114 ? 248 THR A O   1 
ATOM   1926 C  CB  . THR A 1 248 ? 36.98900  8.24700   2.06700  1.000 29.88503 ? 248 THR A CB  1 
ATOM   1927 O  OG1 . THR A 1 248 ? 36.58300  7.15700   2.91000  1.000 27.02315 ? 248 THR A OG1 1 
ATOM   1928 C  CG2 . THR A 1 248 ? 38.32000  7.91300   1.43200  1.000 33.47921 ? 248 THR A CG2 1 
ATOM   1929 N  N   . VAL A 1 249 ? 34.82200  10.39900  2.50600  1.000 24.85665 ? 249 VAL A N   1 
ATOM   1930 C  CA  . VAL A 1 249 ? 33.41600  10.63700  2.84600  1.000 24.76377 ? 249 VAL A CA  1 
ATOM   1931 C  C   . VAL A 1 249 ? 32.80600  9.41000   3.51600  1.000 23.07908 ? 249 VAL A C   1 
ATOM   1932 O  O   . VAL A 1 249 ? 32.19700  9.50100   4.59000  1.000 21.60842 ? 249 VAL A O   1 
ATOM   1933 C  CB  . VAL A 1 249 ? 32.62100  11.02900  1.59000  1.000 24.46607 ? 249 VAL A CB  1 
ATOM   1934 C  CG1 . VAL A 1 249 ? 31.13600  11.02900  1.88600  1.000 22.42000 ? 249 VAL A CG1 1 
ATOM   1935 C  CG2 . VAL A 1 249 ? 33.07100  12.37800  1.08500  1.000 25.60877 ? 249 VAL A CG2 1 
ATOM   1936 N  N   . LEU A 1 250 ? 32.95400  8.24400   2.88500  1.000 23.74214 ? 250 LEU A N   1 
ATOM   1937 C  CA  . LEU A 1 250 ? 32.44300  7.01500   3.47800  1.000 22.09642 ? 250 LEU A CA  1 
ATOM   1938 C  C   . LEU A 1 250 ? 33.01600  6.80600   4.87200  1.000 21.73939 ? 250 LEU A C   1 
ATOM   1939 O  O   . LEU A 1 250 ? 32.27300  6.55500   5.82400  1.000 20.64032 ? 250 LEU A O   1 
ATOM   1940 C  CB  . LEU A 1 250 ? 32.75100  5.82300   2.57300  1.000 24.02198 ? 250 LEU A CB  1 
ATOM   1941 C  CG  . LEU A 1 250 ? 32.26400  4.46900   3.09400  1.000 23.25949 ? 250 LEU A CG  1 
ATOM   1942 C  CD1 . LEU A 1 250 ? 30.75100  4.47000   3.28900  1.000 22.84258 ? 250 LEU A CD1 1 
ATOM   1943 C  CD2 . LEU A 1 250 ? 32.66300  3.36900   2.15100  1.000 25.04525 ? 250 LEU A CD2 1 
ATOM   1944 N  N   . GLY A 1 251 ? 34.33600  6.93400   5.01900  1.000 22.08097 ? 251 GLY A N   1 
ATOM   1945 C  CA  . GLY A 1 251 ? 34.94400  6.76500   6.33100  1.000 21.53518 ? 251 GLY A CA  1 
ATOM   1946 C  C   . GLY A 1 251 ? 34.40800  7.73700   7.36700  1.000 21.60594 ? 251 GLY A C   1 
ATOM   1947 O  O   . GLY A 1 251 ? 34.21600  7.37400   8.53100  1.000 19.86284 ? 251 GLY A O   1 
ATOM   1948 N  N   . GLN A 1 252 ? 34.15500  8.98400   6.95800  1.000 21.19365 ? 252 GLN A N   1 
ATOM   1949 C  CA  . GLN A 1 252 ? 33.62500  9.97400   7.88500  1.000 19.65961 ? 252 GLN A CA  1 
ATOM   1950 C  C   . GLN A 1 252 ? 32.16800  9.69400   8.22700  1.000 19.19962 ? 252 GLN A C   1 
ATOM   1951 O  O   . GLN A 1 252 ? 31.74200  9.91900   9.36100  1.000 18.85035 ? 252 GLN A O   1 
ATOM   1952 C  CB  . GLN A 1 252 ? 33.77200  11.37100  7.29400  1.000 22.02850 ? 252 GLN A CB  1 
ATOM   1953 C  CG  . GLN A 1 252 ? 35.20100  11.79200  6.99500  1.000 23.10015 ? 252 GLN A CG  1 
ATOM   1954 C  CD  . GLN A 1 252 ? 35.27600  13.15100  6.33000  1.000 23.75754 ? 252 GLN A CD  1 
ATOM   1955 O  OE1 . GLN A 1 252 ? 34.28300  13.65600  5.82600  1.000 22.98074 ? 252 GLN A OE1 1 
ATOM   1956 N  NE2 . GLN A 1 252 ? 36.46100  13.74900  6.32500  1.000 26.23039 ? 252 GLN A NE2 1 
ATOM   1957 N  N   . ARG A 1 253 ? 31.38100  9.22100   7.26300  1.000 19.22157 ? 253 ARG A N   1 
ATOM   1958 C  CA  . ARG A 1 253 ? 30.01600  8.82000   7.58600  1.000 19.27212 ? 253 ARG A CA  1 
ATOM   1959 C  C   . ARG A 1 253 ? 29.99800  7.66700   8.57900  1.000 17.94166 ? 253 ARG A C   1 
ATOM   1960 O  O   . ARG A 1 253 ? 29.10500  7.58900   9.42100  1.000 19.47201 ? 253 ARG A O   1 
ATOM   1961 C  CB  . ARG A 1 253 ? 29.25700  8.42100   6.32100  1.000 19.63045 ? 253 ARG A CB  1 
ATOM   1962 C  CG  . ARG A 1 253 ? 29.03400  9.52300   5.30600  1.000 20.50847 ? 253 ARG A CG  1 
ATOM   1963 C  CD  . ARG A 1 253 ? 28.45400  8.98100   4.00400  1.000 20.96251 ? 253 ARG A CD  1 
ATOM   1964 N  NE  . ARG A 1 253 ? 27.13000  8.39600   4.18200  1.000 22.97455 ? 253 ARG A NE  1 
ATOM   1965 C  CZ  . ARG A 1 253 ? 26.84700  7.09700   4.13600  1.000 21.91335 ? 253 ARG A CZ  1 
ATOM   1966 N  NH1 . ARG A 1 253 ? 27.77300  6.19000   3.86700  1.000 21.75642 ? 253 ARG A NH1 1 
ATOM   1967 N  NH2 . ARG A 1 253 ? 25.59900  6.69700   4.36800  1.000 22.19836 ? 253 ARG A NH2 1 
ATOM   1968 N  N   . MET A 1 254 ? 30.96700  6.75900   8.49000  1.000 19.56398 ? 254 MET A N   1 
ATOM   1969 C  CA  . MET A 1 254 ? 31.01100  5.63300   9.41800  1.000 19.75627 ? 254 MET A CA  1 
ATOM   1970 C  C   . MET A 1 254 ? 31.32000  6.09800   10.82700 1.000 18.84768 ? 254 MET A C   1 
ATOM   1971 O  O   . MET A 1 254 ? 30.78500  5.55400   11.79700 1.000 19.28702 ? 254 MET A O   1 
ATOM   1972 C  CB  . MET A 1 254 ? 32.04900  4.59000   8.97800  1.000 19.60847 ? 254 MET A CB  1 
ATOM   1973 C  CG  . MET A 1 254 ? 31.64600  3.69700   7.80100  1.000 20.55843 ? 254 MET A CG  1 
ATOM   1974 S  SD  . MET A 1 254 ? 30.00300  2.99600   7.94400  1.000 16.32922 ? 254 MET A SD  1 
ATOM   1975 C  CE  . MET A 1 254 ? 29.07800  3.99200   6.78400  1.000 20.40661 ? 254 MET A CE  1 
ATOM   1976 N  N   . LEU A 1 255 ? 32.17800  7.09700   10.96800 1.000 17.33731 ? 255 LEU A N   1 
ATOM   1977 C  CA  . LEU A 1 255 ? 32.64600  7.48000   12.28600 1.000 19.30881 ? 255 LEU A CA  1 
ATOM   1978 C  C   . LEU A 1 255 ? 31.83300  8.62500   12.90500 1.000 19.01736 ? 255 LEU A C   1 
ATOM   1979 O  O   . LEU A 1 255 ? 32.29100  9.25000   13.86400 1.000 18.92798 ? 255 LEU A O   1 
ATOM   1980 C  CB  . LEU A 1 255 ? 34.14000  7.80900   12.23200 1.000 19.39664 ? 255 LEU A CB  1 
ATOM   1981 C  CG  . LEU A 1 255 ? 35.07300  6.67300   11.76800 1.000 20.03109 ? 255 LEU A CG  1 
ATOM   1982 C  CD1 . LEU A 1 255 ? 36.50800  6.92000   12.21400 1.000 19.60033 ? 255 LEU A CD1 1 
ATOM   1983 C  CD2 . LEU A 1 255 ? 34.62000  5.30800   12.25300 1.000 19.81020 ? 255 LEU A CD2 1 
ATOM   1984 N  N   . GLY A 1 256 ? 30.62200  8.88400   12.41000 1.000 18.74792 ? 256 GLY A N   1 
ATOM   1985 C  CA  . GLY A 1 256 ? 29.69200  9.77200   13.07800 1.000 17.76781 ? 256 GLY A CA  1 
ATOM   1986 C  C   . GLY A 1 256 ? 29.80700  11.23800  12.71700 1.000 18.53165 ? 256 GLY A C   1 
ATOM   1987 O  O   . GLY A 1 256 ? 29.08600  12.05600  13.29000 1.000 16.98218 ? 256 GLY A O   1 
ATOM   1988 N  N   . TRP A 1 257 ? 30.66400  11.59600  11.77100 1.000 18.97648 ? 257 TRP A N   1 
ATOM   1989 C  CA  . TRP A 1 257 ? 30.93800  12.99500  11.48600 1.000 19.51679 ? 257 TRP A CA  1 
ATOM   1990 C  C   . TRP A 1 257 ? 30.01000  13.60500  10.44100 1.000 19.30715 ? 257 TRP A C   1 
ATOM   1991 O  O   . TRP A 1 257 ? 30.21300  14.76400  10.06700 1.000 20.61688 ? 257 TRP A O   1 
ATOM   1992 C  CB  . TRP A 1 257 ? 32.39600  13.15100  11.04200 1.000 18.73461 ? 257 TRP A CB  1 
ATOM   1993 C  CG  . TRP A 1 257 ? 33.35400  12.95700  12.17400 1.000 19.24595 ? 257 TRP A CG  1 
ATOM   1994 C  CD1 . TRP A 1 257 ? 33.77000  11.77200  12.70400 1.000 19.31269 ? 257 TRP A CD1 1 
ATOM   1995 C  CD2 . TRP A 1 257 ? 33.99400  13.98100  12.93500 1.000 20.04186 ? 257 TRP A CD2 1 
ATOM   1996 N  NE1 . TRP A 1 257 ? 34.64000  11.99900  13.73500 1.000 19.73080 ? 257 TRP A NE1 1 
ATOM   1997 C  CE2 . TRP A 1 257 ? 34.79200  13.34900  13.89700 1.000 20.00678 ? 257 TRP A CE2 1 
ATOM   1998 C  CE3 . TRP A 1 257 ? 33.97900  15.37900  12.88600 1.000 21.70681 ? 257 TRP A CE3 1 
ATOM   1999 C  CZ2 . TRP A 1 257 ? 35.56800  14.06100  14.80300 1.000 20.66571 ? 257 TRP A CZ2 1 
ATOM   2000 C  CZ3 . TRP A 1 257 ? 34.75600  16.08500  13.78600 1.000 21.49521 ? 257 TRP A CZ3 1 
ATOM   2001 C  CH2 . TRP A 1 257 ? 35.53700  15.42700  14.72800 1.000 21.44892 ? 257 TRP A CH2 1 
ATOM   2002 N  N   . ARG A 1 258 ? 29.00700  12.87600  9.95700  1.000 19.20240 ? 258 ARG A N   1 
ATOM   2003 C  CA  . ARG A 1 258 ? 28.13000  13.40900  8.92700  1.000 19.40502 ? 258 ARG A CA  1 
ATOM   2004 C  C   . ARG A 1 258 ? 26.68600  13.06800  9.24700  1.000 20.14207 ? 258 ARG A C   1 
ATOM   2005 O  O   . ARG A 1 258 ? 26.39400  12.04900  9.87600  1.000 20.62007 ? 258 ARG A O   1 
ATOM   2006 C  CB  . ARG A 1 258 ? 28.50000  12.89000  7.54000  1.000 19.68432 ? 258 ARG A CB  1 
ATOM   2007 C  CG  . ARG A 1 258 ? 29.80700  13.45500  7.07300  1.000 20.02243 ? 258 ARG A CG  1 
ATOM   2008 C  CD  . ARG A 1 258 ? 30.25400  12.92300  5.74000  1.000 21.49254 ? 258 ARG A CD  1 
ATOM   2009 N  NE  . ARG A 1 258 ? 31.46300  13.60800  5.29400  1.000 22.58407 ? 258 ARG A NE  1 
ATOM   2010 C  CZ  . ARG A 1 258 ? 31.51300  14.48100  4.29800  1.000 23.09100 ? 258 ARG A CZ  1 
ATOM   2011 N  NH1 . ARG A 1 258 ? 30.45900  14.72800  3.54200  1.000 23.54960 ? 258 ARG A NH1 1 
ATOM   2012 N  NH2 . ARG A 1 258 ? 32.64700  15.12900  4.06100  1.000 24.33334 ? 258 ARG A NH2 1 
ATOM   2013 N  N   . THR A 1 259 ? 25.78700  13.95300  8.82500  1.000 20.60190 ? 259 THR A N   1 
ATOM   2014 C  CA  . THR A 1 259 ? 24.35800  13.68700  8.93500  1.000 21.31374 ? 259 THR A CA  1 
ATOM   2015 C  C   . THR A 1 259 ? 24.00700  12.44400  8.12700  1.000 21.87519 ? 259 THR A C   1 
ATOM   2016 O  O   . THR A 1 259 ? 24.55400  12.21700  7.04400  1.000 22.17505 ? 259 THR A O   1 
ATOM   2017 C  CB  . THR A 1 259 ? 23.56300  14.90100  8.45000  1.000 20.72470 ? 259 THR A CB  1 
ATOM   2018 O  OG1 . THR A 1 259 ? 23.78000  15.98800  9.35000  1.000 20.64077 ? 259 THR A OG1 1 
ATOM   2019 C  CG2 . THR A 1 259 ? 22.07800  14.59900  8.39700  1.000 21.57598 ? 259 THR A CG2 1 
ATOM   2020 N  N   . MET A 1 260 ? 23.12400  11.60900  8.67200  1.000 21.68558 ? 260 MET A N   1 
ATOM   2021 C  CA  . MET A 1 260 ? 22.76300  10.35300  8.03100  1.000 21.32111 ? 260 MET A CA  1 
ATOM   2022 C  C   . MET A 1 260 ? 21.25300  10.30300  7.86500  1.000 22.83772 ? 260 MET A C   1 
ATOM   2023 O  O   . MET A 1 260 ? 20.52100  11.19900  8.28900  1.000 24.00886 ? 260 MET A O   1 
ATOM   2024 C  CB  . MET A 1 260 ? 23.27300  9.15000   8.82500  1.000 21.35550 ? 260 MET A CB  1 
ATOM   2025 C  CG  . MET A 1 260 ? 24.75700  9.23800   9.16500  1.000 21.18587 ? 260 MET A CG  1 
ATOM   2026 S  SD  . MET A 1 260 ? 25.86600  8.92500   7.77600  1.000 17.84497 ? 260 MET A SD  1 
ATOM   2027 C  CE  . MET A 1 260 ? 25.86700  7.13900   7.78600  1.000 19.86979 ? 260 MET A CE  1 
ATOM   2028 N  N   . LYS A 1 261 ? 20.77400  9.23500   7.23300  1.000 22.67948 ? 261 LYS A N   1 
ATOM   2029 C  CA  . LYS A 1 261 ? 19.37600  9.15200   6.83200  1.000 25.01391 ? 261 LYS A CA  1 
ATOM   2030 C  C   . LYS A 1 261 ? 18.83000  7.77200   7.18000  1.000 25.70696 ? 261 LYS A C   1 
ATOM   2031 O  O   . LYS A 1 261 ? 19.09000  6.78700   6.46700  1.000 25.30703 ? 261 LYS A O   1 
ATOM   2032 C  CB  . LYS A 1 261 ? 19.23400  9.45400   5.34100  1.000 25.38772 ? 261 LYS A CB  1 
ATOM   2033 C  CG  . LYS A 1 261 ? 17.83100  9.33500   4.78000  1.000 26.55917 ? 261 LYS A CG  1 
ATOM   2034 C  CD  . LYS A 1 261 ? 16.86900  10.28700  5.45800  1.000 28.15136 ? 261 LYS A CD  1 
ATOM   2035 C  CE  . LYS A 1 261 ? 15.52700  10.28400  4.73600  1.000 29.82559 ? 261 LYS A CE  1 
ATOM   2036 N  NZ  . LYS A 1 261 ? 14.95100  8.90300   4.59400  1.000 30.19529 ? 261 LYS A NZ  1 
ATOM   2037 N  N   . PRO A 1 262 ? 18.07100  7.65900   8.26100  1.000 25.41130 ? 262 PRO A N   1 
ATOM   2038 C  CA  . PRO A 1 262 ? 17.27200  6.45200   8.45500  1.000 26.81726 ? 262 PRO A CA  1 
ATOM   2039 C  C   . PRO A 1 262 ? 16.17700  6.39300   7.39900  1.000 29.03415 ? 262 PRO A C   1 
ATOM   2040 O  O   . PRO A 1 262 ? 15.76500  7.40800   6.82800  1.000 30.49248 ? 262 PRO A O   1 
ATOM   2041 C  CB  . PRO A 1 262 ? 16.69300  6.62000   9.86400  1.000 25.80693 ? 262 PRO A CB  1 
ATOM   2042 C  CG  . PRO A 1 262 ? 17.40300  7.79900   10.44800 1.000 24.66154 ? 262 PRO A CG  1 
ATOM   2043 C  CD  . PRO A 1 262 ? 17.81200  8.65500   9.30300  1.000 24.84525 ? 262 PRO A CD  1 
ATOM   2044 N  N   . SER A 1 263 ? 15.71900  5.17600   7.12000  1.000 28.81531 ? 263 SER A N   1 
ATOM   2045 C  CA  . SER A 1 263 ? 14.66200  5.00700   6.13500  1.000 28.62316 ? 263 SER A CA  1 
ATOM   2046 C  C   . SER A 1 263 ? 13.42300  5.82200   6.51500  1.000 30.82113 ? 263 SER A C   1 
ATOM   2047 O  O   . SER A 1 263 ? 13.21400  6.20300   7.67500  1.000 29.98192 ? 263 SER A O   1 
ATOM   2048 C  CB  . SER A 1 263 ? 14.27900  3.53700   6.00700  1.000 29.61366 ? 263 SER A CB  1 
ATOM   2049 O  OG  . SER A 1 263 ? 13.67800  3.08300   7.20000  1.000 30.13764 ? 263 SER A OG  1 
ATOM   2050 N  N   . ASP A 1 264 ? 12.59300  6.09300   5.51100  1.000 31.75444 ? 264 ASP A N   1 
ATOM   2051 C  CA  . ASP A 1 264 ? 11.30100  6.69200   5.78000  1.000 32.63018 ? 264 ASP A CA  1 
ATOM   2052 C  C   . ASP A 1 264 ? 10.52900  5.79200   6.75200  1.000 32.12001 ? 264 ASP A C   1 
ATOM   2053 O  O   . ASP A 1 264 ? 10.74500  4.57600   6.77800  1.000 32.17923 ? 264 ASP A O   1 
ATOM   2054 C  CB  . ASP A 1 264 ? 10.54000  6.88900   4.46700  1.000 33.82643 ? 264 ASP A CB  1 
ATOM   2055 C  CG  . ASP A 1 264 ? 11.25800  7.83400   3.50000  1.000 34.65979 ? 264 ASP A CG  1 
ATOM   2056 O  OD1 . ASP A 1 264 ? 12.24400  8.49500   3.89600  1.000 33.38387 ? 264 ASP A OD1 1 
ATOM   2057 O  OD2 . ASP A 1 264 ? 10.82700  7.90500   2.32800  1.000 35.85776 ? 264 ASP A OD2 1 
ATOM   2058 N  N   . PRO A 1 265 ? 9.62200   6.35600   7.58700  1.000 31.85781 ? 265 PRO A N   1 
ATOM   2059 C  CA  . PRO A 1 265 ? 9.03000   7.69700   7.60200  1.000 32.25646 ? 265 PRO A CA  1 
ATOM   2060 C  C   . PRO A 1 265 ? 9.92300   8.81400   8.11800  1.000 33.38071 ? 265 PRO A C   1 
ATOM   2061 O  O   . PRO A 1 265 ? 9.43100   9.93300   8.23300  1.000 33.96441 ? 265 PRO A O   1 
ATOM   2062 C  CB  . PRO A 1 265 ? 7.82500   7.50600   8.52900  1.000 31.08095 ? 265 PRO A CB  1 
ATOM   2063 C  CG  . PRO A 1 265 ? 8.31700   6.54300   9.53100  1.000 30.77799 ? 265 PRO A CG  1 
ATOM   2064 C  CD  . PRO A 1 265 ? 9.13600   5.56600   8.73400  1.000 31.79300 ? 265 PRO A CD  1 
ATOM   2065 N  N   . ASN A 1 266 ? 11.19500  8.58000   8.45300  1.000 32.50652 ? 266 ASN A N   1 
ATOM   2066 C  CA  . ASN A 1 266 ? 12.10500  9.68500   8.73300  1.000 30.61473 ? 266 ASN A CA  1 
ATOM   2067 C  C   . ASN A 1 266 ? 12.51200  10.27200  7.39900  1.000 31.60788 ? 266 ASN A C   1 
ATOM   2068 O  O   . ASN A 1 266 ? 13.35900  9.71800   6.69900  1.000 32.91037 ? 266 ASN A O   1 
ATOM   2069 C  CB  . ASN A 1 266 ? 13.32500  9.23500   9.51900  1.000 28.11686 ? 266 ASN A CB  1 
ATOM   2070 C  CG  . ASN A 1 266 ? 14.14100  10.40500  10.01400 1.000 27.43562 ? 266 ASN A CG  1 
ATOM   2071 O  OD1 . ASN A 1 266 ? 14.20900  11.44400  9.36700  1.000 27.69034 ? 266 ASN A OD1 1 
ATOM   2072 N  ND2 . ASN A 1 266 ? 14.76400  10.24600  11.17100 1.000 27.25387 ? 266 ASN A ND2 1 
ATOM   2073 N  N   . ILE A 1 267 ? 11.90800  11.40300  7.04700  1.000 32.02867 ? 267 ILE A N   1 
ATOM   2074 C  CA  . ILE A 1 267 ? 12.15700  12.06000  5.77000  1.000 32.86310 ? 267 ILE A CA  1 
ATOM   2075 C  C   . ILE A 1 267 ? 13.14200  13.21000  5.91100  1.000 31.63702 ? 267 ILE A C   1 
ATOM   2076 O  O   . ILE A 1 267 ? 13.39900  13.92700  4.93900  1.000 32.09835 ? 267 ILE A O   1 
ATOM   2077 C  CB  . ILE A 1 267 ? 10.84000  12.53800  5.13600  1.000 35.27240 ? 267 ILE A CB  1 
ATOM   2078 C  CG1 . ILE A 1 267 ? 9.97100   13.24800  6.18200  1.000 35.79893 ? 267 ILE A CG1 1 
ATOM   2079 C  CG2 . ILE A 1 267 ? 10.09700  11.36400  4.52900  1.000 34.59830 ? 267 ILE A CG2 1 
ATOM   2080 C  CD1 . ILE A 1 267 ? 8.59300   13.63900  5.67700  1.000 38.11551 ? 267 ILE A CD1 1 
ATOM   2081 N  N   . VAL A 1 268 ? 13.69900  13.40100  7.10200  1.000 32.55181 ? 268 VAL A N   1 
ATOM   2082 C  CA  . VAL A 1 268 ? 14.65000  14.47300  7.37700  1.000 31.59093 ? 268 VAL A CA  1 
ATOM   2083 C  C   . VAL A 1 268 ? 16.06000  13.92000  7.55900  1.000 29.95027 ? 268 VAL A C   1 
ATOM   2084 O  O   . VAL A 1 268 ? 16.99100  14.33100  6.87100  1.000 29.13437 ? 268 VAL A O   1 
ATOM   2085 C  CB  . VAL A 1 268 ? 14.21200  15.29900  8.60700  1.000 31.27106 ? 268 VAL A CB  1 
ATOM   2086 C  CG1 . VAL A 1 268 ? 15.17300  16.44600  8.84200  1.000 31.70882 ? 268 VAL A CG1 1 
ATOM   2087 C  CG2 . VAL A 1 268 ? 12.78700  15.79700  8.43200  1.000 32.94546 ? 268 VAL A CG2 1 
ATOM   2088 N  N   . GLY A 1 269 ? 16.23200  12.97700  8.47900  1.000 28.94467 ? 269 GLY A N   1 
ATOM   2089 C  CA  . GLY A 1 269 ? 17.54600  12.44800  8.78000  1.000 25.92393 ? 269 GLY A CA  1 
ATOM   2090 C  C   . GLY A 1 269 ? 17.80300  12.39600  10.27200 1.000 24.03682 ? 269 GLY A C   1 
ATOM   2091 O  O   . GLY A 1 269 ? 16.86500  12.32500  11.07000 1.000 23.82370 ? 269 GLY A O   1 
ATOM   2092 N  N   . ILE A 1 270 ? 19.07500  12.45600  10.65700 1.000 22.26756 ? 270 ILE A N   1 
ATOM   2093 C  CA  . ILE A 1 270 ? 19.49700  12.26800  12.03900 1.000 21.14575 ? 270 ILE A CA  1 
ATOM   2094 C  C   . ILE A 1 270 ? 20.93700  12.75900  12.11400 1.000 20.75867 ? 270 ILE A C   1 
ATOM   2095 O  O   . ILE A 1 270 ? 21.63300  12.80100  11.09500 1.000 22.45549 ? 270 ILE A O   1 
ATOM   2096 C  CB  . ILE A 1 270 ? 19.33500  10.78600  12.46800 1.000 21.19958 ? 270 ILE A CB  1 
ATOM   2097 C  CG1 . ILE A 1 270 ? 19.35300  10.63100  13.98300 1.000 19.72573 ? 270 ILE A CG1 1 
ATOM   2098 C  CG2 . ILE A 1 270 ? 20.39300  9.88200   11.85000 1.000 21.42819 ? 270 ILE A CG2 1 
ATOM   2099 C  CD1 . ILE A 1 270 ? 18.79000  9.32400   14.44200 1.000 19.66950 ? 270 ILE A CD1 1 
ATOM   2100 N  N   . ASN A 1 271 ? 21.38300  13.17500  13.29400 1.000 19.48836 ? 271 ASN A N   1 
ATOM   2101 C  CA  . ASN A 1 271 ? 22.73700  13.69300  13.48200 1.000 20.39246 ? 271 ASN A CA  1 
ATOM   2102 C  C   . ASN A 1 271 ? 22.92900  14.98600  12.68600 1.000 20.59157 ? 271 ASN A C   1 
ATOM   2103 O  O   . ASN A 1 271 ? 23.85200  15.11800  11.88000 1.000 20.40454 ? 271 ASN A O   1 
ATOM   2104 C  CB  . ASN A 1 271 ? 23.78600  12.63300  13.10400 1.000 20.56065 ? 271 ASN A CB  1 
ATOM   2105 C  CG  . ASN A 1 271 ? 25.12900  12.83200  13.80100 1.000 19.00820 ? 271 ASN A CG  1 
ATOM   2106 O  OD1 . ASN A 1 271 ? 25.20500  13.29200  14.93800 1.000 18.92791 ? 271 ASN A OD1 1 
ATOM   2107 N  ND2 . ASN A 1 271 ? 26.19400  12.46200  13.11300 1.000 18.58071 ? 271 ASN A ND2 1 
ATOM   2108 N  N   . LEU A 1 272 ? 22.02800  15.94300  12.90800 1.000 20.10726 ? 272 LEU A N   1 
ATOM   2109 C  CA  . LEU A 1 272 ? 22.06500  17.25200  12.26700 1.000 21.52984 ? 272 LEU A CA  1 
ATOM   2110 C  C   . LEU A 1 272 ? 22.01300  18.33400  13.34300 1.000 21.45031 ? 272 LEU A C   1 
ATOM   2111 O  O   . LEU A 1 272 ? 21.86000  18.04800  14.53200 1.000 22.07902 ? 272 LEU A O   1 
ATOM   2112 C  CB  . LEU A 1 272 ? 20.91300  17.40900  11.26300 1.000 22.08128 ? 272 LEU A CB  1 
ATOM   2113 C  CG  . LEU A 1 272 ? 19.55400  16.85800  11.69600 1.000 21.39245 ? 272 LEU A CG  1 
ATOM   2114 C  CD1 . LEU A 1 272 ? 18.83200  17.77600  12.66900 1.000 22.11583 ? 272 LEU A CD1 1 
ATOM   2115 C  CD2 . LEU A 1 272 ? 18.68400  16.59200  10.49200 1.000 24.14977 ? 272 LEU A CD2 1 
ATOM   2116 N  N   . ILE A 1 273 ? 22.14500  19.59300  12.93300 1.000 22.03122 ? 273 ILE A N   1 
ATOM   2117 C  CA  . ILE A 1 273 ? 22.12300  20.68800  13.89400 1.000 23.54426 ? 273 ILE A CA  1 
ATOM   2118 C  C   . ILE A 1 273 ? 21.88700  21.97300  13.12700 1.000 25.44532 ? 273 ILE A C   1 
ATOM   2119 O  O   . ILE A 1 273 ? 22.30600  22.11000  11.97800 1.000 26.34875 ? 273 ILE A O   1 
ATOM   2120 C  CB  . ILE A 1 273 ? 23.42700  20.74400  14.74000 1.000 23.05263 ? 273 ILE A CB  1 
ATOM   2121 C  CG1 . ILE A 1 273 ? 23.31800  21.77500  15.87200 1.000 23.70804 ? 273 ILE A CG1 1 
ATOM   2122 C  CG2 . ILE A 1 273 ? 24.63100  21.06000  13.87700 1.000 24.06022 ? 273 ILE A CG2 1 
ATOM   2123 C  CD1 . ILE A 1 273 ? 22.28700  21.43800  16.92300 1.000 22.42557 ? 273 ILE A CD1 1 
ATOM   2124 N  N   . ASP A 1 274 ? 21.19400  22.91300  13.76700 1.000 24.73819 ? 274 ASP A N   1 
ATOM   2125 C  CA  . ASP A 1 274 ? 20.87600  24.19900  13.15800 1.000 26.59064 ? 274 ASP A CA  1 
ATOM   2126 C  C   . ASP A 1 274 ? 20.08000  24.01100  11.87100 1.000 29.36178 ? 274 ASP A C   1 
ATOM   2127 O  O   . ASP A 1 274 ? 20.08700  24.87600  10.99600 1.000 31.13619 ? 274 ASP A O   1 
ATOM   2128 C  CB  . ASP A 1 274 ? 22.14600  25.02100  12.90500 1.000 26.43046 ? 274 ASP A CB  1 
ATOM   2129 C  CG  . ASP A 1 274 ? 22.86400  25.40300  14.18800 1.000 28.21970 ? 274 ASP A CG  1 
ATOM   2130 O  OD1 . ASP A 1 274 ? 22.19200  25.54300  15.23000 1.000 27.26038 ? 274 ASP A OD1 1 
ATOM   2131 O  OD2 . ASP A 1 274 ? 24.10300  25.57300  14.15500 1.000 30.99544 ? 274 ASP A OD2 1 
ATOM   2132 N  N   . ASP A 1 275 ? 19.40200  22.86300  11.75500 1.000 29.89401 ? 275 ASP A N   1 
ATOM   2133 C  CA  . ASP A 1 275 ? 18.62800  22.47600  10.57200 1.000 33.77809 ? 275 ASP A CA  1 
ATOM   2134 C  C   . ASP A 1 275 ? 19.50600  22.34200  9.32500  1.000 35.57769 ? 275 ASP A C   1 
ATOM   2135 O  O   . ASP A 1 275 ? 19.04400  22.54000  8.19500  1.000 39.06159 ? 275 ASP A O   1 
ATOM   2136 C  CB  . ASP A 1 275 ? 17.47900  23.45300  10.31700 1.000 38.52341 ? 275 ASP A CB  1 
ATOM   2137 C  CG  . ASP A 1 275 ? 16.36700  22.83700  9.51200  1.000 44.37908 ? 275 ASP A CG  1 
ATOM   2138 O  OD1 . ASP A 1 275 ? 16.23500  21.59200  9.54200  1.000 43.81562 ? 275 ASP A OD1 1 
ATOM   2139 O  OD2 . ASP A 1 275 ? 15.63300  23.59700  8.84800  1.000 50.48185 ? 275 ASP A OD2 1 
ATOM   2140 N  N   . LYS A 1 276 ? 20.78200  22.01500  9.52000  1.000 32.26633 ? 276 LYS A N   1 
ATOM   2141 C  CA  . LYS A 1 276 ? 21.72700  21.81300  8.43200  1.000 32.56576 ? 276 LYS A CA  1 
ATOM   2142 C  C   . LYS A 1 276 ? 22.47600  20.51300  8.65800  1.000 27.58231 ? 276 LYS A C   1 
ATOM   2143 O  O   . LYS A 1 276 ? 22.37700  19.88500  9.71000  1.000 25.65570 ? 276 LYS A O   1 
ATOM   2144 C  CB  . LYS A 1 276 ? 22.73100  22.96800  8.31600  1.000 31.88763 ? 276 LYS A CB  1 
ATOM   2145 C  CG  . LYS A 1 276 ? 22.15500  24.23800  7.75300  1.000 34.25164 ? 276 LYS A CG  1 
ATOM   2146 C  CD  . LYS A 1 276 ? 22.81400  25.43600  8.40300  1.000 34.30176 ? 276 LYS A CD  1 
ATOM   2147 C  CE  . LYS A 1 276 ? 22.54300  26.70100  7.63300  1.000 39.01968 ? 276 LYS A CE  1 
ATOM   2148 N  NZ  . LYS A 1 276 ? 21.09800  26.83200  7.31300  1.000 49.50385 ? 276 LYS A NZ  1 
ATOM   2149 N  N   . ARG A 1 277 ? 23.24300  20.12100  7.65700  1.000 27.25489 ? 277 ARG A N   1 
ATOM   2150 C  CA  . ARG A 1 277 ? 24.03700  18.91500  7.76800  1.000 26.08816 ? 277 ARG A CA  1 
ATOM   2151 C  C   . ARG A 1 277 ? 25.26000  19.17800  8.63600  1.000 24.86902 ? 277 ARG A C   1 
ATOM   2152 O  O   . ARG A 1 277 ? 25.87000  20.24600  8.57000  1.000 25.23548 ? 277 ARG A O   1 
ATOM   2153 C  CB  . ARG A 1 277 ? 24.44200  18.41300  6.38200  1.000 25.53982 ? 277 ARG A CB  1 
ATOM   2154 C  CG  . ARG A 1 277 ? 23.24800  18.01200  5.54100  1.000 27.71440 ? 277 ARG A CG  1 
ATOM   2155 C  CD  . ARG A 1 277 ? 23.64400  17.33700  4.26000  1.000 29.65861 ? 277 ARG A CD  1 
ATOM   2156 N  NE  . ARG A 1 277 ? 22.63500  17.50000  3.21900  1.000 31.61733 ? 277 ARG A NE  1 
ATOM   2157 C  CZ  . ARG A 1 277 ? 21.48500  16.83900  3.16200  1.000 32.11089 ? 277 ARG A CZ  1 
ATOM   2158 N  NH1 . ARG A 1 277 ? 21.12800  15.98100  4.10000  1.000 33.58032 ? 277 ARG A NH1 1 
ATOM   2159 N  NH2 . ARG A 1 277 ? 20.67100  17.04700  2.13400  1.000 33.24954 ? 277 ARG A NH2 1 
ATOM   2160 N  N   . LEU A 1 278 ? 25.60800  18.18800  9.46000  1.000 23.27203 ? 278 LEU A N   1 
ATOM   2161 C  CA  . LEU A 1 278 ? 26.72400  18.32300  10.39100 1.000 23.16115 ? 278 LEU A CA  1 
ATOM   2162 C  C   . LEU A 1 278 ? 28.01700  18.72200  9.68100  1.000 23.16287 ? 278 LEU A C   1 
ATOM   2163 O  O   . LEU A 1 278 ? 28.74900  19.60400  10.14100 1.000 23.11892 ? 278 LEU A O   1 
ATOM   2164 C  CB  . LEU A 1 278 ? 26.90700  17.00500  11.14800 1.000 20.90188 ? 278 LEU A CB  1 
ATOM   2165 C  CG  . LEU A 1 278 ? 28.12900  16.87000  12.04200 1.000 20.33633 ? 278 LEU A CG  1 
ATOM   2166 C  CD1 . LEU A 1 278 ? 28.16300  17.99500  13.05500 1.000 22.52804 ? 278 LEU A CD1 1 
ATOM   2167 C  CD2 . LEU A 1 278 ? 28.09900  15.53800  12.74500 1.000 19.42622 ? 278 LEU A CD2 1 
ATOM   2168 N  N   . GLU A 1 279 ? 28.32800  18.06300  8.56800  1.000 22.36410 ? 279 GLU A N   1 
ATOM   2169 C  CA  . GLU A 1 279 ? 29.56800  18.37700  7.87200  1.000 23.14208 ? 279 GLU A CA  1 
ATOM   2170 C  C   . GLU A 1 279 ? 29.54500  19.78500  7.27300  1.000 24.07463 ? 279 GLU A C   1 
ATOM   2171 O  O   . GLU A 1 279 ? 30.60200  20.41200  7.14800  1.000 24.68211 ? 279 GLU A O   1 
ATOM   2172 C  CB  . GLU A 1 279 ? 29.83900  17.32100  6.80300  1.000 22.72662 ? 279 GLU A CB  1 
ATOM   2173 C  CG  . GLU A 1 279 ? 28.75300  17.17300  5.74000  1.000 21.89728 ? 279 GLU A CG  1 
ATOM   2174 C  CD  . GLU A 1 279 ? 27.58700  16.28500  6.15800  1.000 22.93809 ? 279 GLU A CD  1 
ATOM   2175 O  OE1 . GLU A 1 279 ? 27.30000  16.17100  7.36400  1.000 22.29698 ? 279 GLU A OE1 1 
ATOM   2176 O  OE2 . GLU A 1 279 ? 26.94800  15.69700  5.26800  1.000 23.28387 ? 279 GLU A OE2 1 
ATOM   2177 N  N   . ASN A 1 280 ? 28.35900  20.29500  6.90700  1.000 24.33710 ? 280 ASN A N   1 
ATOM   2178 C  CA  . ASN A 1 280 ? 28.23200  21.68900  6.47100  1.000 24.76339 ? 280 ASN A CA  1 
ATOM   2179 C  C   . ASN A 1 280 ? 28.54900  22.64700  7.60600  1.000 24.27242 ? 280 ASN A C   1 
ATOM   2180 O  O   . ASN A 1 280 ? 29.36700  23.55600  7.45700  1.000 24.55033 ? 280 ASN A O   1 
ATOM   2181 C  CB  . ASN A 1 280 ? 26.81800  21.96500  5.95200  1.000 24.93379 ? 280 ASN A CB  1 
ATOM   2182 C  CG  . ASN A 1 280 ? 26.52500  21.26700  4.64600  1.000 27.80948 ? 280 ASN A CG  1 
ATOM   2183 O  OD1 . ASN A 1 280 ? 27.35100  20.52300  4.12300  1.000 28.45529 ? 280 ASN A OD1 1 
ATOM   2184 N  ND2 . ASN A 1 280 ? 25.33100  21.49400  4.11400  1.000 31.25923 ? 280 ASN A ND2 1 
ATOM   2185 N  N   . VAL A 1 281 ? 27.88100  22.47100  8.74400  1.000 23.93320 ? 281 VAL A N   1 
ATOM   2186 C  CA  . VAL A 1 281 ? 28.15800  23.26200  9.93300  1.000 23.94415 ? 281 VAL A CA  1 
ATOM   2187 C  C   . VAL A 1 281 ? 29.63500  23.21900  10.27600 1.000 25.06236 ? 281 VAL A C   1 
ATOM   2188 O  O   . VAL A 1 281 ? 30.19300  24.20700  10.76800 1.000 26.11198 ? 281 VAL A O   1 
ATOM   2189 C  CB  . VAL A 1 281 ? 27.28500  22.76200  11.10100 1.000 23.68608 ? 281 VAL A CB  1 
ATOM   2190 C  CG1 . VAL A 1 281 ? 27.64100  23.48900  12.37500 1.000 25.51315 ? 281 VAL A CG1 1 
ATOM   2191 C  CG2 . VAL A 1 281 ? 25.80700  22.95800  10.77500 1.000 25.08848 ? 281 VAL A CG2 1 
ATOM   2192 N  N   . LEU A 1 282 ? 30.30400  22.09600  10.00400 1.000 25.27151 ? 282 LEU A N   1 
ATOM   2193 C  CA  . LEU A 1 282 ? 31.70300  21.93300  10.38500 1.000 24.40744 ? 282 LEU A CA  1 
ATOM   2194 C  C   . LEU A 1 282 ? 32.68800  22.36500  9.30600  1.000 26.40085 ? 282 LEU A C   1 
ATOM   2195 O  O   . LEU A 1 282 ? 33.89100  22.40400  9.58300  1.000 28.67055 ? 282 LEU A O   1 
ATOM   2196 C  CB  . LEU A 1 282 ? 31.99300  20.47600  10.75700 1.000 25.12455 ? 282 LEU A CB  1 
ATOM   2197 C  CG  . LEU A 1 282 ? 31.33200  19.92500  12.01700 1.000 23.77624 ? 282 LEU A CG  1 
ATOM   2198 C  CD1 . LEU A 1 282 ? 31.72900  18.48400  12.21100 1.000 22.92317 ? 282 LEU A CD1 1 
ATOM   2199 C  CD2 . LEU A 1 282 ? 31.72300  20.74500  13.21300 1.000 23.78251 ? 282 LEU A CD2 1 
ATOM   2200 N  N   . GLN A 1 283 ? 32.22200  22.68900  8.10100  1.000 25.67395 ? 283 GLN A N   1 
ATOM   2201 C  CA  . GLN A 1 283 ? 33.10500  22.97600  6.97100  1.000 26.78521 ? 283 GLN A CA  1 
ATOM   2202 C  C   . GLN A 1 283 ? 34.14800  21.88000  6.81500  1.000 28.14086 ? 283 GLN A C   1 
ATOM   2203 O  O   . GLN A 1 283 ? 35.33700  22.13300  6.63600  1.000 28.55070 ? 283 GLN A O   1 
ATOM   2204 C  CB  . GLN A 1 283 ? 33.76500  24.33100  7.12000  1.000 30.13569 ? 283 GLN A CB  1 
ATOM   2205 C  CG  . GLN A 1 283 ? 32.95700  25.43100  6.52500  1.000 31.64532 ? 283 GLN A CG  1 
ATOM   2206 C  CD  . GLN A 1 283 ? 33.74400  26.70400  6.43200  1.000 34.07576 ? 283 GLN A CD  1 
ATOM   2207 O  OE1 . GLN A 1 283 ? 33.67300  27.54500  7.32600  1.000 36.90934 ? 283 GLN A OE1 1 
ATOM   2208 N  NE2 . GLN A 1 283 ? 34.51100  26.85700  5.35000  1.000 35.31146 ? 283 GLN A NE2 1 
ATOM   2209 N  N   . LEU A 1 284 ? 33.66800  20.64500  6.88700  1.000 27.73281 ? 284 LEU A N   1 
ATOM   2210 C  CA  . LEU A 1 284 ? 34.51600  19.47500  7.00300  1.000 27.52531 ? 284 LEU A CA  1 
ATOM   2211 C  C   . LEU A 1 284 ? 35.00700  19.05000  5.62900  1.000 27.36144 ? 284 LEU A C   1 
ATOM   2212 O  O   . LEU A 1 284 ? 34.21200  18.63400  4.78100  1.000 27.93994 ? 284 LEU A O   1 
ATOM   2213 C  CB  . LEU A 1 284 ? 33.72700  18.35700  7.66900  1.000 26.52957 ? 284 LEU A CB  1 
ATOM   2214 C  CG  . LEU A 1 284 ? 34.47500  17.12500  8.15300  1.000 26.45277 ? 284 LEU A CG  1 
ATOM   2215 C  CD1 . LEU A 1 284 ? 35.60900  17.51100  9.06200  1.000 26.51392 ? 284 LEU A CD1 1 
ATOM   2216 C  CD2 . LEU A 1 284 ? 33.48400  16.25100  8.88300  1.000 24.28986 ? 284 LEU A CD2 1 
ATOM   2217 N  N   . LYS A 1 285 ? 36.31500  19.14900  5.41200  1.000 27.26605 ? 285 LYS A N   1 
ATOM   2218 C  CA  . LYS A 1 285 ? 36.93200  18.55000  4.24000  1.000 27.98208 ? 285 LYS A CA  1 
ATOM   2219 C  C   . LYS A 1 285 ? 37.01800  17.03900  4.42300  1.000 27.22466 ? 285 LYS A C   1 
ATOM   2220 O  O   . LYS A 1 285 ? 37.06200  16.53300  5.54400  1.000 26.67395 ? 285 LYS A O   1 
ATOM   2221 C  CB  . LYS A 1 285 ? 38.33400  19.11800  4.00800  1.000 28.31693 ? 285 LYS A CB  1 
ATOM   2222 C  CG  . LYS A 1 285 ? 38.45600  20.63400  4.13200  1.000 31.47034 ? 285 LYS A CG  1 
ATOM   2223 C  CD  . LYS A 1 285 ? 39.92600  21.06900  4.09600  1.000 34.79348 ? 285 LYS A CD  1 
ATOM   2224 C  CE  . LYS A 1 285 ? 40.09500  22.57900  4.03900  1.000 36.11417 ? 285 LYS A CE  1 
ATOM   2225 N  NZ  . LYS A 1 285 ? 41.53100  22.98100  3.98700  1.000 37.77148 ? 285 LYS A NZ  1 
ATOM   2226 N  N   . ALA A 1 286 ? 37.04000  16.31800  3.30600  1.000 27.82079 ? 286 ALA A N   1 
ATOM   2227 C  CA  . ALA A 1 286 ? 37.26400  14.87900  3.31100  1.000 28.79112 ? 286 ALA A CA  1 
ATOM   2228 C  C   . ALA A 1 286 ? 38.24400  14.54600  2.20100  1.000 31.29483 ? 286 ALA A C   1 
ATOM   2229 O  O   . ALA A 1 286 ? 38.46100  15.34500  1.29000  1.000 32.06675 ? 286 ALA A O   1 
ATOM   2230 C  CB  . ALA A 1 286 ? 35.97300  14.08400  3.11500  1.000 28.03374 ? 286 ALA A CB  1 
ATOM   2231 N  N   . ALA A 1 287 ? 38.82000  13.34200  2.26400  1.000 28.94013 ? 287 ALA A N   1 
ATOM   2232 C  CA  . ALA A 1 287 ? 39.89400  12.99300  1.33600  1.000 31.20788 ? 287 ALA A CA  1 
ATOM   2233 C  C   . ALA A 1 287 ? 39.43600  12.89700  -0.12200 1.000 35.34412 ? 287 ALA A C   1 
ATOM   2234 O  O   . ALA A 1 287 ? 40.26600  13.04600  -1.02400 1.000 37.83819 ? 287 ALA A O   1 
ATOM   2235 C  CB  . ALA A 1 287 ? 40.55600  11.67200  1.74900  1.000 29.89797 ? 287 ALA A CB  1 
ATOM   2236 N  N   . ASP A 1 288 ? 38.15300  12.66100  -0.38800 1.000 36.34674 ? 288 ASP A N   1 
ATOM   2237 C  CA  . ASP A 1 288 ? 37.72300  12.40800  -1.75900 1.000 39.11874 ? 288 ASP A CA  1 
ATOM   2238 C  C   . ASP A 1 288 ? 36.51300  13.25200  -2.14200 1.000 37.19104 ? 288 ASP A C   1 
ATOM   2239 O  O   . ASP A 1 288 ? 35.63100  12.79700  -2.87100 1.000 38.42011 ? 288 ASP A O   1 
ATOM   2240 C  CB  . ASP A 1 288 ? 37.43800  10.91900  -1.97300 1.000 43.39441 ? 288 ASP A CB  1 
ATOM   2241 C  CG  . ASP A 1 288 ? 36.31500  10.38500  -1.09200 1.000 36.76969 ? 288 ASP A CG  1 
ATOM   2242 O  OD1 . ASP A 1 288 ? 36.11400  10.89500  0.02500  1.000 32.14288 ? 288 ASP A OD1 1 
ATOM   2243 O  OD2 . ASP A 1 288 ? 35.63000  9.43400   -1.52500 1.000 40.00441 ? 288 ASP A OD2 1 
ATOM   2244 N  N   . SER A 1 289 ? 36.45200  14.50100  -1.69600 1.000 33.90763 ? 289 SER A N   1 
ATOM   2245 C  CA  . SER A 1 289 ? 35.36700  15.36700  -2.16300 1.000 35.65854 ? 289 SER A CA  1 
ATOM   2246 C  C   . SER A 1 289 ? 35.81900  16.80200  -2.45200 1.000 35.33733 ? 289 SER A C   1 
ATOM   2247 O  O   . SER A 1 289 ? 36.78000  17.30000  -1.87100 1.000 35.65374 ? 289 SER A O   1 
ATOM   2248 C  CB  . SER A 1 289 ? 34.21000  15.36700  -1.15500 1.000 32.40629 ? 289 SER A CB  1 
ATOM   2249 O  OG  . SER A 1 289 ? 34.53300  16.09300  0.00800  1.000 31.68707 ? 289 SER A OG  1 
ATOM   2250 N  N   . LYS B 1 6   ? -16.53000 11.96700  26.56400 1.000 39.73030 ? 6   LYS B N   1 
ATOM   2251 C  CA  . LYS B 1 6   ? -15.25200 11.26700  26.41200 1.000 37.96315 ? 6   LYS B CA  1 
ATOM   2252 C  C   . LYS B 1 6   ? -14.29700 11.57900  27.55100 1.000 36.92955 ? 6   LYS B C   1 
ATOM   2253 O  O   . LYS B 1 6   ? -14.11100 12.73900  27.90000 1.000 36.65299 ? 6   LYS B O   1 
ATOM   2254 C  CB  . LYS B 1 6   ? -14.59300 11.63600  25.08800 1.000 36.72366 ? 6   LYS B CB  1 
ATOM   2255 C  CG  . LYS B 1 6   ? -15.24100 11.01500  23.86200 1.000 39.88005 ? 6   LYS B CG  1 
ATOM   2256 C  CD  . LYS B 1 6   ? -14.61300 11.53700  22.57500 1.000 39.03078 ? 6   LYS B CD  1 
ATOM   2257 C  CE  . LYS B 1 6   ? -13.10700 11.50500  22.66600 1.000 36.27505 ? 6   LYS B CE  1 
ATOM   2258 N  NZ  . LYS B 1 6   ? -12.64200 10.15100  23.06800 1.000 37.75583 ? 6   LYS B NZ  1 
ATOM   2259 N  N   . PRO B 1 7   ? -13.68500 10.54400  28.12200 1.000 37.20179 ? 7   PRO B N   1 
ATOM   2260 C  CA  . PRO B 1 7   ? -12.66800 10.75900  29.16300 1.000 36.15845 ? 7   PRO B CA  1 
ATOM   2261 C  C   . PRO B 1 7   ? -11.57300 11.70100  28.68700 1.000 34.21598 ? 7   PRO B C   1 
ATOM   2262 O  O   . PRO B 1 7   ? -10.96600 11.49900  27.63300 1.000 34.02122 ? 7   PRO B O   1 
ATOM   2263 C  CB  . PRO B 1 7   ? -12.12100 9.35100   29.42300 1.000 37.39677 ? 7   PRO B CB  1 
ATOM   2264 C  CG  . PRO B 1 7   ? -13.19700 8.43200   28.96300 1.000 39.61715 ? 7   PRO B CG  1 
ATOM   2265 C  CD  . PRO B 1 7   ? -13.89400 9.11800   27.82400 1.000 39.01388 ? 7   PRO B CD  1 
ATOM   2266 N  N   . GLN B 1 8   ? -11.32000 12.73700  29.47400 1.000 33.73415 ? 8   GLN B N   1 
ATOM   2267 C  CA  . GLN B 1 8   ? -10.40300 13.79600  29.08700 1.000 34.00222 ? 8   GLN B CA  1 
ATOM   2268 C  C   . GLN B 1 8   ? -9.03700  13.60500  29.74900 1.000 33.84431 ? 8   GLN B C   1 
ATOM   2269 O  O   . GLN B 1 8   ? -8.85700  12.79800  30.66700 1.000 34.95381 ? 8   GLN B O   1 
ATOM   2270 C  CB  . GLN B 1 8   ? -10.99200 15.16200  29.45000 1.000 34.01533 ? 8   GLN B CB  1 
ATOM   2271 C  CG  . GLN B 1 8   ? -12.41000 15.37900  28.96500 1.000 34.80707 ? 8   GLN B CG  1 
ATOM   2272 C  CD  . GLN B 1 8   ? -12.46600 15.75100  27.50900 1.000 34.45451 ? 8   GLN B CD  1 
ATOM   2273 O  OE1 . GLN B 1 8   ? -13.47800 15.54400  26.82400 1.000 37.55151 ? 8   GLN B OE1 1 
ATOM   2274 N  NE2 . GLN B 1 8   ? -11.37700 16.32400  27.02200 1.000 35.31067 ? 8   GLN B NE2 1 
ATOM   2275 N  N   . LEU B 1 9   ? -8.06600  14.37100  29.26400 1.000 32.49218 ? 9   LEU B N   1 
ATOM   2276 C  CA  . LEU B 1 9   ? -6.72400  14.33000  29.82800 1.000 32.49390 ? 9   LEU B CA  1 
ATOM   2277 C  C   . LEU B 1 9   ? -6.74300  14.76800  31.28900 1.000 32.53541 ? 9   LEU B C   1 
ATOM   2278 O  O   . LEU B 1 9   ? -7.23400  15.85300  31.61600 1.000 33.35866 ? 9   LEU B O   1 
ATOM   2279 C  CB  . LEU B 1 9   ? -5.79200  15.23100  29.01100 1.000 31.81627 ? 9   LEU B CB  1 
ATOM   2280 C  CG  . LEU B 1 9   ? -5.19700  14.74800  27.68600 1.000 30.08143 ? 9   LEU B CG  1 
ATOM   2281 C  CD1 . LEU B 1 9   ? -4.80900  15.93700  26.83600 1.000 28.99515 ? 9   LEU B CD1 1 
ATOM   2282 C  CD2 . LEU B 1 9   ? -3.98000  13.88900  27.94500 1.000 27.82450 ? 9   LEU B CD2 1 
ATOM   2283 N  N   . GLN B 1 10  ? -6.20700  13.92400  32.17200 1.000 32.83838 ? 10  GLN B N   1 
ATOM   2284 C  CA  . GLN B 1 10  ? -6.11200  14.28500  33.58100 1.000 33.22307 ? 10  GLN B CA  1 
ATOM   2285 C  C   . GLN B 1 10  ? -5.12200  15.42500  33.76300 1.000 32.31393 ? 10  GLN B C   1 
ATOM   2286 O  O   . GLN B 1 10  ? -4.07400  15.46200  33.11800 1.000 31.54143 ? 10  GLN B O   1 
ATOM   2287 C  CB  . GLN B 1 10  ? -5.68100  13.08600  34.42700 1.000 33.88412 ? 10  GLN B CB  1 
ATOM   2288 C  CG  . GLN B 1 10  ? -6.82500  12.21900  34.95000 1.000 34.64762 ? 10  GLN B CG  1 
ATOM   2289 C  CD  . GLN B 1 10  ? -7.11900  12.44100  36.43400 1.000 36.80463 ? 10  GLN B CD  1 
ATOM   2290 O  OE1 . GLN B 1 10  ? -7.22900  11.48600  37.20900 1.000 38.95644 ? 10  GLN B OE1 1 
ATOM   2291 N  NE2 . GLN B 1 10  ? -7.25900  13.70200  36.83100 1.000 34.92967 ? 10  GLN B NE2 1 
ATOM   2292 N  N   . ARG B 1 11  ? -5.46400  16.36100  34.64700 1.000 32.53416 ? 11  ARG B N   1 
ATOM   2293 C  CA  . ARG B 1 11  ? -4.62400  17.51100  34.97800 1.000 32.71019 ? 11  ARG B CA  1 
ATOM   2294 C  C   . ARG B 1 11  ? -4.08400  17.34800  36.39600 1.000 32.44349 ? 11  ARG B C   1 
ATOM   2295 O  O   . ARG B 1 11  ? -4.85900  17.19500  37.34600 1.000 33.14872 ? 11  ARG B O   1 
ATOM   2296 C  CB  . ARG B 1 11  ? -5.41100  18.81900  34.86400 1.000 33.24570 ? 11  ARG B CB  1 
ATOM   2297 C  CG  . ARG B 1 11  ? -5.48900  19.43500  33.47100 1.000 32.44595 ? 11  ARG B CG  1 
ATOM   2298 C  CD  . ARG B 1 11  ? -6.50800  18.75500  32.57300 1.000 32.25057 ? 11  ARG B CD  1 
ATOM   2299 N  NE  . ARG B 1 11  ? -6.71700  19.52000  31.34900 1.000 33.29077 ? 11  ARG B NE  1 
ATOM   2300 C  CZ  . ARG B 1 11  ? -7.30900  19.05500  30.25700 1.000 32.76991 ? 11  ARG B CZ  1 
ATOM   2301 N  NH1 . ARG B 1 11  ? -7.76500  17.81400  30.18900 1.000 31.59094 ? 11  ARG B NH1 1 
ATOM   2302 N  NH2 . ARG B 1 11  ? -7.44100  19.85300  29.20300 1.000 32.96258 ? 11  ARG B NH2 1 
ATOM   2303 N  N   . LEU B 1 12  ? -2.76600  17.39300  36.54400 1.000 35.55474 ? 12  LEU B N   1 
ATOM   2304 C  CA  . LEU B 1 12  ? -2.13400  17.21700  37.84100 1.000 37.58368 ? 12  LEU B CA  1 
ATOM   2305 C  C   . LEU B 1 12  ? -1.29400  18.43900  38.17100 1.000 38.43422 ? 12  LEU B C   1 
ATOM   2306 O  O   . LEU B 1 12  ? -0.80500  19.13300  37.27600 1.000 37.33815 ? 12  LEU B O   1 
ATOM   2307 C  CB  . LEU B 1 12  ? -1.25000  15.95300  37.88500 1.000 36.93847 ? 12  LEU B CB  1 
ATOM   2308 C  CG  . LEU B 1 12  ? -1.92600  14.60400  38.14600 1.000 35.15098 ? 12  LEU B CG  1 
ATOM   2309 C  CD1 . LEU B 1 12  ? -2.84000  14.24700  37.00100 1.000 34.95157 ? 12  LEU B CD1 1 
ATOM   2310 C  CD2 . LEU B 1 12  ? -0.89300  13.52000  38.35400 1.000 35.90637 ? 12  LEU B CD2 1 
ATOM   2311 N  N   . ALA B 1 13  ? -1.14200  18.70200  39.46600 1.000 38.92370 ? 13  ALA B N   1 
ATOM   2312 C  CA  . ALA B 1 13  ? -0.28800  19.78800  39.91100 1.000 40.40732 ? 13  ALA B CA  1 
ATOM   2313 C  C   . ALA B 1 13  ? 1.17400   19.38900  39.76300 1.000 42.11476 ? 13  ALA B C   1 
ATOM   2314 O  O   . ALA B 1 13  ? 1.51800   18.20400  39.72500 1.000 42.33368 ? 13  ALA B O   1 
ATOM   2315 C  CB  . ALA B 1 13  ? -0.59400  20.16400  41.36000 1.000 41.30522 ? 13  ALA B CB  1 
ATOM   2316 N  N   . ALA B 1 14  ? 2.04000   20.40100  39.67300 1.000 42.29442 ? 14  ALA B N   1 
ATOM   2317 C  CA  . ALA B 1 14  ? 3.44700   20.13400  39.39800 1.000 39.70718 ? 14  ALA B CA  1 
ATOM   2318 C  C   . ALA B 1 14  ? 4.05000   19.19600  40.42900 1.000 41.95928 ? 14  ALA B C   1 
ATOM   2319 O  O   . ALA B 1 14  ? 4.95000   18.41400  40.10000 1.000 40.96171 ? 14  ALA B O   1 
ATOM   2320 C  CB  . ALA B 1 14  ? 4.23300   21.44200  39.34700 1.000 37.61924 ? 14  ALA B CB  1 
ATOM   2321 N  N   . ASP B 1 15  ? 3.56600   19.24500  41.67300 1.000 43.29508 ? 15  ASP B N   1 
ATOM   2322 C  CA  . ASP B 1 15  ? 4.07700   18.39600  42.74100 1.000 42.73651 ? 15  ASP B CA  1 
ATOM   2323 C  C   . ASP B 1 15  ? 3.21500   17.16100  42.96400 1.000 44.36269 ? 15  ASP B C   1 
ATOM   2324 O  O   . ASP B 1 15  ? 3.19800   16.61000  44.06900 1.000 45.09139 ? 15  ASP B O   1 
ATOM   2325 C  CB  . ASP B 1 15  ? 4.22500   19.19400  44.03700 1.000 42.29035 ? 15  ASP B CB  1 
ATOM   2326 C  CG  . ASP B 1 15  ? 2.96500   19.95700  44.42400 1.000 45.57165 ? 15  ASP B CG  1 
ATOM   2327 O  OD1 . ASP B 1 15  ? 1.95500   19.89500  43.68500 1.000 45.47056 ? 15  ASP B OD1 1 
ATOM   2328 O  OD2 . ASP B 1 15  ? 2.99900   20.63300  45.48400 1.000 44.37223 ? 15  ASP B OD2 1 
ATOM   2329 N  N   . ALA B 1 16  ? 2.50400   16.71200  41.92900 1.000 50.32584 ? 16  ALA B N   1 
ATOM   2330 C  CA  . ALA B 1 16  ? 1.70200   15.50100  42.01900 1.000 49.22714 ? 16  ALA B CA  1 
ATOM   2331 C  C   . ALA B 1 16  ? 2.59900   14.27100  42.19900 1.000 48.91284 ? 16  ALA B C   1 
ATOM   2332 O  O   . ALA B 1 16  ? 3.82500   14.33900  42.09000 1.000 50.55174 ? 16  ALA B O   1 
ATOM   2333 C  CB  . ALA B 1 16  ? 0.82800   15.34900  40.77700 1.000 47.43557 ? 16  ALA B CB  1 
ATOM   2334 N  N   . ASP B 1 17  ? 1.97000   13.13200  42.47800 1.000 43.20949 ? 17  ASP B N   1 
ATOM   2335 C  CA  . ASP B 1 17  ? 2.70400   11.91500  42.80300 1.000 40.93959 ? 17  ASP B CA  1 
ATOM   2336 C  C   . ASP B 1 17  ? 3.19700   11.25900  41.52400 1.000 39.54981 ? 17  ASP B C   1 
ATOM   2337 O  O   . ASP B 1 17  ? 2.39300   10.88400  40.66800 1.000 39.38585 ? 17  ASP B O   1 
ATOM   2338 C  CB  . ASP B 1 17  ? 1.82000   10.95600  43.59300 1.000 40.40100 ? 17  ASP B CB  1 
ATOM   2339 C  CG  . ASP B 1 17  ? 2.62200   9.95500   44.39600 1.000 40.05930 ? 17  ASP B CG  1 
ATOM   2340 O  OD1 . ASP B 1 17  ? 3.85000   9.87400   44.20300 1.000 43.53767 ? 17  ASP B OD1 1 
ATOM   2341 O  OD2 . ASP B 1 17  ? 2.02400   9.25000   45.22600 1.000 41.28016 ? 17  ASP B OD2 1 
ATOM   2342 N  N   . VAL B 1 18  ? 4.51800   11.11200  41.40200 1.000 39.15792 ? 18  VAL B N   1 
ATOM   2343 C  CA  . VAL B 1 18  ? 5.10000   10.54700  40.18900 1.000 37.76426 ? 18  VAL B CA  1 
ATOM   2344 C  C   . VAL B 1 18  ? 4.63500   9.11300   39.98700 1.000 36.90411 ? 18  VAL B C   1 
ATOM   2345 O  O   . VAL B 1 18  ? 4.52500   8.64100   38.85000 1.000 36.63392 ? 18  VAL B O   1 
ATOM   2346 C  CB  . VAL B 1 18  ? 6.63500   10.65100  40.24300 1.000 36.68781 ? 18  VAL B CB  1 
ATOM   2347 C  CG1 . VAL B 1 18  ? 7.25800   9.93600   39.05400 1.000 33.52103 ? 18  VAL B CG1 1 
ATOM   2348 C  CG2 . VAL B 1 18  ? 7.05900   12.11200  40.28900 1.000 34.66250 ? 18  VAL B CG2 1 
ATOM   2349 N  N   . ASP B 1 19  ? 4.34700   8.40300   41.07800 1.000 37.64564 ? 19  ASP B N   1 
ATOM   2350 C  CA  . ASP B 1 19  ? 3.71500   7.09500   40.96100 1.000 37.53769 ? 19  ASP B CA  1 
ATOM   2351 C  C   . ASP B 1 19  ? 2.38700   7.20100   40.22700 1.000 37.81688 ? 19  ASP B C   1 
ATOM   2352 O  O   . ASP B 1 19  ? 2.06000   6.35000   39.39300 1.000 37.04889 ? 19  ASP B O   1 
ATOM   2353 C  CB  . ASP B 1 19  ? 3.50700   6.48000   42.34500 1.000 39.06887 ? 19  ASP B CB  1 
ATOM   2354 C  CG  . ASP B 1 19  ? 4.68300   5.63200   42.80700 1.000 41.17337 ? 19  ASP B CG  1 
ATOM   2355 O  OD1 . ASP B 1 19  ? 5.75700   5.65400   42.16500 1.000 44.31529 ? 19  ASP B OD1 1 
ATOM   2356 O  OD2 . ASP B 1 19  ? 4.52500   4.93000   43.82700 1.000 42.69243 ? 19  ASP B OD2 1 
ATOM   2357 N  N   . ARG B 1 20  ? 1.60700   8.24700   40.52300 1.000 37.93012 ? 20  ARG B N   1 
ATOM   2358 C  CA  . ARG B 1 20  ? 0.34600   8.45100   39.82500 1.000 35.30100 ? 20  ARG B CA  1 
ATOM   2359 C  C   . ARG B 1 20  ? 0.58500   8.80300   38.36500 1.000 34.92952 ? 20  ARG B C   1 
ATOM   2360 O  O   . ARG B 1 20  ? -0.12200  8.31300   37.47600 1.000 34.49579 ? 20  ARG B O   1 
ATOM   2361 C  CB  . ARG B 1 20  ? -0.47100  9.53900   40.51700 1.000 35.55945 ? 20  ARG B CB  1 
ATOM   2362 C  CG  . ARG B 1 20  ? -1.87400  9.63300   39.98000 1.000 36.34812 ? 20  ARG B CG  1 
ATOM   2363 C  CD  . ARG B 1 20  ? -2.63400  10.84700  40.50400 1.000 39.90833 ? 20  ARG B CD  1 
ATOM   2364 N  NE  . ARG B 1 20  ? -3.93400  10.99800  39.85100 1.000 39.19136 ? 20  ARG B NE  1 
ATOM   2365 C  CZ  . ARG B 1 20  ? -4.70000  12.07800  39.94000 1.000 38.88178 ? 20  ARG B CZ  1 
ATOM   2366 N  NH1 . ARG B 1 20  ? -4.33000  13.13300  40.64900 1.000 38.72076 ? 20  ARG B NH1 1 
ATOM   2367 N  NH2 . ARG B 1 20  ? -5.86600  12.10200  39.29700 1.000 38.45542 ? 20  ARG B NH2 1 
ATOM   2368 N  N   . MET B 1 21  ? 1.58700   9.64600   38.10000 1.000 36.62141 ? 21  MET B N   1 
ATOM   2369 C  CA  . MET B 1 21  ? 1.92200   10.00500  36.72600 1.000 34.47963 ? 21  MET B CA  1 
ATOM   2370 C  C   . MET B 1 21  ? 2.31900   8.78100   35.91300 1.000 34.49352 ? 21  MET B C   1 
ATOM   2371 O  O   . MET B 1 21  ? 1.97400   8.67400   34.73300 1.000 33.05392 ? 21  MET B O   1 
ATOM   2372 C  CB  . MET B 1 21  ? 3.04700   11.03500  36.71600 1.000 33.46957 ? 21  MET B CB  1 
ATOM   2373 C  CG  . MET B 1 21  ? 2.80800   12.22400  37.62100 1.000 34.88161 ? 21  MET B CG  1 
ATOM   2374 S  SD  . MET B 1 21  ? 3.95900   13.55000  37.25800 1.000 33.39002 ? 21  MET B SD  1 
ATOM   2375 C  CE  . MET B 1 21  ? 3.74700   14.57000  38.70900 1.000 37.25437 ? 21  MET B CE  1 
ATOM   2376 N  N   . CYS B 1 22  ? 3.04100   7.84400   36.52700 1.000 34.06179 ? 22  CYS B N   1 
ATOM   2377 C  CA  . CYS B 1 22  ? 3.42500   6.64200   35.79900 1.000 35.03141 ? 22  CYS B CA  1 
ATOM   2378 C  C   . CYS B 1 22  ? 2.21300   5.78000   35.45500 1.000 34.52924 ? 22  CYS B C   1 
ATOM   2379 O  O   . CYS B 1 22  ? 2.24300   5.04400   34.46300 1.000 34.55307 ? 22  CYS B O   1 
ATOM   2380 C  CB  . CYS B 1 22  ? 4.44700   5.84600   36.60500 1.000 35.37663 ? 22  CYS B CB  1 
ATOM   2381 S  SG  . CYS B 1 22  ? 5.92300   5.41100   35.65700 1.000 44.65154 ? 22  CYS B SG  1 
ATOM   2382 N  N   . ARG B 1 23  ? 1.14300   5.86100   36.25000 1.000 36.10504 ? 23  ARG B N   1 
ATOM   2383 C  CA  . ARG B 1 23  ? -0.07100  5.09900   35.97000 1.000 35.97922 ? 23  ARG B CA  1 
ATOM   2384 C  C   . ARG B 1 23  ? -0.91100  5.76300   34.88900 1.000 35.06129 ? 23  ARG B C   1 
ATOM   2385 O  O   . ARG B 1 23  ? -1.55600  5.07600   34.09400 1.000 35.13516 ? 23  ARG B O   1 
ATOM   2386 C  CB  . ARG B 1 23  ? -0.90400  4.93000   37.24700 1.000 36.31964 ? 23  ARG B CB  1 
ATOM   2387 C  CG  . ARG B 1 23  ? -0.33400  3.95500   38.27900 1.000 35.56837 ? 23  ARG B CG  1 
ATOM   2388 C  CD  . ARG B 1 23  ? -1.29100  3.75800   39.46200 1.000 37.88764 ? 23  ARG B CD  1 
ATOM   2389 N  NE  . ARG B 1 23  ? -1.45700  4.96100   40.27000 1.000 38.48574 ? 23  ARG B NE  1 
ATOM   2390 C  CZ  . ARG B 1 23  ? -0.81900  5.19000   41.40900 1.000 39.21453 ? 23  ARG B CZ  1 
ATOM   2391 N  NH1 . ARG B 1 23  ? 0.03300   4.30900   41.91100 1.000 40.15435 ? 23  ARG B NH1 1 
ATOM   2392 N  NH2 . ARG B 1 23  ? -1.04800  6.32400   42.06700 1.000 39.55215 ? 23  ARG B NH2 1 
ATOM   2393 N  N   . LEU B 1 24  ? -0.93300  7.09600   34.85700 1.000 32.44746 ? 24  LEU B N   1 
ATOM   2394 C  CA  . LEU B 1 24  ? -1.64500  7.79600   33.79400 1.000 31.47369 ? 24  LEU B CA  1 
ATOM   2395 C  C   . LEU B 1 24  ? -1.02800  7.51500   32.42900 1.000 31.41294 ? 24  LEU B C   1 
ATOM   2396 O  O   . LEU B 1 24  ? -1.75000  7.35900   31.43900 1.000 31.44576 ? 24  LEU B O   1 
ATOM   2397 C  CB  . LEU B 1 24  ? -1.64400  9.29700   34.06200 1.000 31.51102 ? 24  LEU B CB  1 
ATOM   2398 C  CG  . LEU B 1 24  ? -2.47000  9.83100   35.22400 1.000 33.29254 ? 24  LEU B CG  1 
ATOM   2399 C  CD1 . LEU B 1 24  ? -2.01200  11.23300  35.53400 1.000 32.82432 ? 24  LEU B CD1 1 
ATOM   2400 C  CD2 . LEU B 1 24  ? -3.95000  9.80700   34.87600 1.000 32.84142 ? 24  LEU B CD2 1 
ATOM   2401 N  N   . LEU B 1 25  ? 0.30600   7.47400   32.35100 1.000 31.34187 ? 25  LEU B N   1 
ATOM   2402 C  CA  . LEU B 1 25  ? 0.96400   7.22700   31.07200 1.000 30.19763 ? 25  LEU B CA  1 
ATOM   2403 C  C   . LEU B 1 25  ? 0.65600   5.83500   30.54900 1.000 30.01004 ? 25  LEU B C   1 
ATOM   2404 O  O   . LEU B 1 25  ? 0.52100   5.64100   29.34100 1.000 30.44153 ? 25  LEU B O   1 
ATOM   2405 C  CB  . LEU B 1 25  ? 2.47300   7.42100   31.20400 1.000 30.84586 ? 25  LEU B CB  1 
ATOM   2406 C  CG  . LEU B 1 25  ? 2.97700   8.85000   31.40500 1.000 28.27829 ? 25  LEU B CG  1 
ATOM   2407 C  CD1 . LEU B 1 25  ? 4.49700   8.87900   31.40200 1.000 28.05059 ? 25  LEU B CD1 1 
ATOM   2408 C  CD2 . LEU B 1 25  ? 2.42600   9.77000   30.33900 1.000 26.72288 ? 25  LEU B CD2 1 
ATOM   2409 N  N   . GLU B 1 26  ? 0.55300   4.84800   31.43600 1.000 30.73365 ? 26  GLU B N   1 
ATOM   2410 C  CA  . GLU B 1 26  ? 0.18800   3.51000   30.98500 1.000 30.85470 ? 26  GLU B CA  1 
ATOM   2411 C  C   . GLU B 1 26  ? -1.30800  3.40300   30.68200 1.000 31.82857 ? 26  GLU B C   1 
ATOM   2412 O  O   . GLU B 1 26  ? -1.69600  2.79600   29.67700 1.000 31.98656 ? 26  GLU B O   1 
ATOM   2413 C  CB  . GLU B 1 26  ? 0.60300   2.47100   32.03000 1.000 30.64627 ? 26  GLU B CB  1 
ATOM   2414 C  CG  . GLU B 1 26  ? 2.10700   2.38500   32.24800 1.000 32.22042 ? 26  GLU B CG  1 
ATOM   2415 C  CD  . GLU B 1 26  ? 2.89400   2.16900   30.95400 1.000 32.21803 ? 26  GLU B CD  1 
ATOM   2416 O  OE1 . GLU B 1 26  ? 2.79100   1.06700   30.35700 1.000 33.79745 ? 26  GLU B OE1 1 
ATOM   2417 O  OE2 . GLU B 1 26  ? 3.61600   3.11000   30.53700 1.000 31.70258 ? 26  GLU B OE2 1 
ATOM   2418 N  N   . GLU B 1 27  ? -2.16200  3.99300   31.52300 1.000 30.69770 ? 27  GLU B N   1 
ATOM   2419 C  CA  . GLU B 1 27  ? -3.60300  3.88500   31.31200 1.000 31.72886 ? 27  GLU B CA  1 
ATOM   2420 C  C   . GLU B 1 27  ? -4.05500  4.73500   30.13300 1.000 30.67723 ? 27  GLU B C   1 
ATOM   2421 O  O   . GLU B 1 27  ? -4.56000  4.21200   29.13400 1.000 31.53173 ? 27  GLU B O   1 
ATOM   2422 C  CB  . GLU B 1 27  ? -4.35200  4.28200   32.58400 1.000 32.98064 ? 27  GLU B CB  1 
ATOM   2423 C  CG  . GLU B 1 27  ? -4.14800  3.31400   33.74100 1.000 37.51247 ? 27  GLU B CG  1 
ATOM   2424 C  CD  . GLU B 1 27  ? -4.72400  3.82700   35.05300 1.000 41.27075 ? 27  GLU B CD  1 
ATOM   2425 O  OE1 . GLU B 1 27  ? -5.43900  4.85900   35.03200 1.000 42.90714 ? 27  GLU B OE1 1 
ATOM   2426 O  OE2 . GLU B 1 27  ? -4.45200  3.19700   36.10400 1.000 41.38502 ? 27  GLU B OE2 1 
ATOM   2427 N  N   . ASP B 1 28  ? -3.88600  6.05400   30.23400 1.000 31.16330 ? 28  ASP B N   1 
ATOM   2428 C  CA  . ASP B 1 28  ? -4.39800  6.98200   29.23500 1.000 29.54219 ? 28  ASP B CA  1 
ATOM   2429 C  C   . ASP B 1 28  ? -3.40700  7.23400   28.11500 1.000 29.46598 ? 28  ASP B C   1 
ATOM   2430 O  O   . ASP B 1 28  ? -3.81000  7.40000   26.96000 1.000 28.63870 ? 28  ASP B O   1 
ATOM   2431 C  CB  . ASP B 1 28  ? -4.76700  8.31100   29.89600 1.000 30.61286 ? 28  ASP B CB  1 
ATOM   2432 C  CG  . ASP B 1 28  ? -6.05200  8.23200   30.70500 1.000 32.55777 ? 28  ASP B CG  1 
ATOM   2433 O  OD1 . ASP B 1 28  ? -6.90500  7.37500   30.38900 1.000 32.80167 ? 28  ASP B OD1 1 
ATOM   2434 O  OD2 . ASP B 1 28  ? -6.20500  9.03300   31.65400 1.000 32.84827 ? 28  ASP B OD2 1 
ATOM   2435 N  N   . GLY B 1 29  ? -2.11600  7.26700   28.43800 1.000 29.13629 ? 29  GLY B N   1 
ATOM   2436 C  CA  . GLY B 1 29  ? -1.07700  7.52400   27.46800 1.000 28.32085 ? 29  GLY B CA  1 
ATOM   2437 C  C   . GLY B 1 29  ? -0.51900  8.92400   27.50100 1.000 27.19956 ? 29  GLY B C   1 
ATOM   2438 O  O   . GLY B 1 29  ? 0.38400   9.23100   26.71400 1.000 24.77483 ? 29  GLY B O   1 
ATOM   2439 N  N   . ALA B 1 30  ? -1.02200  9.77600   28.38800 1.000 26.98666 ? 30  ALA B N   1 
ATOM   2440 C  CA  . ALA B 1 30  ? -0.59800  11.16400  28.46800 1.000 26.57087 ? 30  ALA B CA  1 
ATOM   2441 C  C   . ALA B 1 30  ? -1.21000  11.76500  29.71900 1.000 27.34519 ? 30  ALA B C   1 
ATOM   2442 O  O   . ALA B 1 30  ? -2.22300  11.27800  30.22400 1.000 29.00899 ? 30  ALA B O   1 
ATOM   2443 C  CB  . ALA B 1 30  ? -1.01900  11.95600  27.22500 1.000 26.13327 ? 30  ALA B CB  1 
ATOM   2444 N  N   . PHE B 1 31  ? -0.58200  12.82400  30.22100 1.000 27.63998 ? 31  PHE B N   1 
ATOM   2445 C  CA  . PHE B 1 31  ? -1.18000  13.61200  31.28700 1.000 27.83991 ? 31  PHE B CA  1 
ATOM   2446 C  C   . PHE B 1 31  ? -0.64600  15.02900  31.19100 1.000 28.09909 ? 31  PHE B C   1 
ATOM   2447 O  O   . PHE B 1 31  ? 0.25600   15.32200  30.40600 1.000 27.81596 ? 31  PHE B O   1 
ATOM   2448 C  CB  . PHE B 1 31  ? -0.90600  13.02600  32.66700 1.000 28.68713 ? 31  PHE B CB  1 
ATOM   2449 C  CG  . PHE B 1 31  ? 0.51400   13.14700  33.10100 1.000 28.65112 ? 31  PHE B CG  1 
ATOM   2450 C  CD1 . PHE B 1 31  ? 1.43800   12.19400  32.74100 1.000 29.03269 ? 31  PHE B CD1 1 
ATOM   2451 C  CD2 . PHE B 1 31  ? 0.92300   14.20100  33.89200 1.000 29.94771 ? 31  PHE B CD2 1 
ATOM   2452 C  CE1 . PHE B 1 31  ? 2.74600   12.29500  33.14900 1.000 28.93946 ? 31  PHE B CE1 1 
ATOM   2453 C  CE2 . PHE B 1 31  ? 2.23600   14.30700  34.29900 1.000 29.87895 ? 31  PHE B CE2 1 
ATOM   2454 C  CZ  . PHE B 1 31  ? 3.14400   13.35600  33.92700 1.000 28.52035 ? 31  PHE B CZ  1 
ATOM   2455 N  N   . ILE B 1 32  ? -1.22000  15.90700  32.00700 1.000 28.43396 ? 32  ILE B N   1 
ATOM   2456 C  CA  . ILE B 1 32  ? -0.91700  17.33000  31.97700 1.000 29.61027 ? 32  ILE B CA  1 
ATOM   2457 C  C   . ILE B 1 32  ? -0.45800  17.76500  33.36400 1.000 31.10216 ? 32  ILE B C   1 
ATOM   2458 O  O   . ILE B 1 32  ? -1.12400  17.47400  34.36500 1.000 31.65210 ? 32  ILE B O   1 
ATOM   2459 C  CB  . ILE B 1 32  ? -2.13600  18.14700  31.50200 1.000 29.51202 ? 32  ILE B CB  1 
ATOM   2460 C  CG1 . ILE B 1 32  ? -2.41800  17.85200  30.01800 1.000 27.85330 ? 32  ILE B CG1 1 
ATOM   2461 C  CG2 . ILE B 1 32  ? -1.92500  19.63300  31.75900 1.000 29.29244 ? 32  ILE B CG2 1 
ATOM   2462 C  CD1 . ILE B 1 32  ? -3.59900  18.56800  29.43800 1.000 28.05786 ? 32  ILE B CD1 1 
ATOM   2463 N  N   . LEU B 1 33  ? 0.69500   18.42800  33.42100 1.000 30.98134 ? 33  LEU B N   1 
ATOM   2464 C  CA  . LEU B 1 33  ? 1.12800   19.14600  34.61000 1.000 31.76886 ? 33  LEU B CA  1 
ATOM   2465 C  C   . LEU B 1 33  ? 0.69500   20.59600  34.47100 1.000 32.31133 ? 33  LEU B C   1 
ATOM   2466 O  O   . LEU B 1 33  ? 0.98700   21.23800  33.46000 1.000 32.55101 ? 33  LEU B O   1 
ATOM   2467 C  CB  . LEU B 1 33  ? 2.64200   19.07100  34.77700 1.000 31.72531 ? 33  LEU B CB  1 
ATOM   2468 C  CG  . LEU B 1 33  ? 3.22800   17.70500  35.09800 1.000 31.47022 ? 33  LEU B CG  1 
ATOM   2469 C  CD1 . LEU B 1 33  ? 4.73200   17.80900  35.21200 1.000 31.82797 ? 33  LEU B CD1 1 
ATOM   2470 C  CD2 . LEU B 1 33  ? 2.62900   17.19700  36.38900 1.000 34.28671 ? 33  LEU B CD2 1 
ATOM   2471 N  N   . LYS B 1 34  ? -0.01600  21.10500  35.46700 1.000 32.98738 ? 34  LYS B N   1 
ATOM   2472 C  CA  . LYS B 1 34  ? -0.50300  22.47700  35.42700 1.000 32.45749 ? 34  LYS B CA  1 
ATOM   2473 C  C   . LYS B 1 34  ? 0.51600   23.37900  36.11000 1.000 33.37817 ? 34  LYS B C   1 
ATOM   2474 O  O   . LYS B 1 34  ? 0.89100   23.13600  37.26200 1.000 34.59429 ? 34  LYS B O   1 
ATOM   2475 C  CB  . LYS B 1 34  ? -1.86900  22.59400  36.09700 1.000 34.39813 ? 34  LYS B CB  1 
ATOM   2476 C  CG  . LYS B 1 34  ? -2.29100  24.03300  36.39800 1.000 38.36891 ? 34  LYS B CG  1 
ATOM   2477 C  CD  . LYS B 1 34  ? -2.63000  24.83200  35.14300 1.000 36.96334 ? 34  LYS B CD  1 
ATOM   2478 C  CE  . LYS B 1 34  ? -3.85000  24.26900  34.44100 1.000 37.07976 ? 34  LYS B CE  1 
ATOM   2479 N  NZ  . LYS B 1 34  ? -4.30700  25.15800  33.34700 1.000 36.69800 ? 34  LYS B NZ  1 
ATOM   2480 N  N   . GLY B 1 35  ? 0.97600   24.40300  35.39200 1.000 34.55541 ? 35  GLY B N   1 
ATOM   2481 C  CA  . GLY B 1 35  ? 1.88700   25.38000  35.95200 1.000 34.41788 ? 35  GLY B CA  1 
ATOM   2482 C  C   . GLY B 1 35  ? 3.18800   24.79800  36.46200 1.000 32.91448 ? 35  GLY B C   1 
ATOM   2483 O  O   . GLY B 1 35  ? 3.61900   25.09900  37.57600 1.000 33.86354 ? 35  GLY B O   1 
ATOM   2484 N  N   . LEU B 1 36  ? 3.83000   23.95600  35.66200 1.000 31.91530 ? 36  LEU B N   1 
ATOM   2485 C  CA  . LEU B 1 36  ? 5.14400   23.46600  36.05300 1.000 31.35195 ? 36  LEU B CA  1 
ATOM   2486 C  C   . LEU B 1 36  ? 6.16000   24.60000  36.11000 1.000 31.06744 ? 36  LEU B C   1 
ATOM   2487 O  O   . LEU B 1 36  ? 6.96100   24.67800  37.04700 1.000 30.25279 ? 36  LEU B O   1 
ATOM   2488 C  CB  . LEU B 1 36  ? 5.60900   22.38900  35.08400 1.000 29.74220 ? 36  LEU B CB  1 
ATOM   2489 C  CG  . LEU B 1 36  ? 6.95000   21.78300  35.47200 1.000 29.42970 ? 36  LEU B CG  1 
ATOM   2490 C  CD1 . LEU B 1 36  ? 6.73000   20.60200  36.38200 1.000 30.12000 ? 36  LEU B CD1 1 
ATOM   2491 C  CD2 . LEU B 1 36  ? 7.71400   21.38800  34.24400 1.000 28.53886 ? 36  LEU B CD2 1 
ATOM   2492 N  N   . LEU B 1 37  ? 6.13000   25.49500  35.12800 1.000 32.80619 ? 37  LEU B N   1 
ATOM   2493 C  CA  . LEU B 1 37  ? 7.13900   26.52600  34.97400 1.000 33.81719 ? 37  LEU B CA  1 
ATOM   2494 C  C   . LEU B 1 37  ? 6.54600   27.90100  35.22200 1.000 35.25989 ? 37  LEU B C   1 
ATOM   2495 O  O   . LEU B 1 37  ? 5.53900   28.25900  34.59700 1.000 34.24064 ? 37  LEU B O   1 
ATOM   2496 C  CB  . LEU B 1 37  ? 7.74300   26.47000  33.57000 1.000 32.34154 ? 37  LEU B CB  1 
ATOM   2497 C  CG  . LEU B 1 37  ? 8.43200   25.15600  33.23500 1.000 29.58748 ? 37  LEU B CG  1 
ATOM   2498 C  CD1 . LEU B 1 37  ? 8.67500   25.09600  31.74900 1.000 28.50854 ? 37  LEU B CD1 1 
ATOM   2499 C  CD2 . LEU B 1 37  ? 9.74100   25.04100  34.00100 1.000 28.68612 ? 37  LEU B CD2 1 
ATOM   2500 N  N   . PRO B 1 38  ? 7.15100   28.69900  36.10200 1.000 33.24204 ? 38  PRO B N   1 
ATOM   2501 C  CA  . PRO B 1 38  ? 6.62200   30.04000  36.37300 1.000 34.20980 ? 38  PRO B CA  1 
ATOM   2502 C  C   . PRO B 1 38  ? 6.64600   30.91500  35.13100 1.000 34.79172 ? 38  PRO B C   1 
ATOM   2503 O  O   . PRO B 1 38  ? 7.47000   30.73500  34.23300 1.000 34.56126 ? 38  PRO B O   1 
ATOM   2504 C  CB  . PRO B 1 38  ? 7.56300   30.58400  37.45800 1.000 36.01803 ? 38  PRO B CB  1 
ATOM   2505 C  CG  . PRO B 1 38  ? 8.79700   29.75100  37.36900 1.000 34.42687 ? 38  PRO B CG  1 
ATOM   2506 C  CD  . PRO B 1 38  ? 8.35300   28.39900  36.89800 1.000 32.93455 ? 38  PRO B CD  1 
ATOM   2507 N  N   . PHE B 1 39  ? 5.73600   31.89100  35.09800 1.000 35.42780 ? 39  PHE B N   1 
ATOM   2508 C  CA  . PHE B 1 39  ? 5.52400   32.65400  33.87400 1.000 35.82516 ? 39  PHE B CA  1 
ATOM   2509 C  C   . PHE B 1 39  ? 6.77000   33.41300  33.45000 1.000 35.53129 ? 39  PHE B C   1 
ATOM   2510 O  O   . PHE B 1 39  ? 7.00700   33.58200  32.25200 1.000 35.43627 ? 39  PHE B O   1 
ATOM   2511 C  CB  . PHE B 1 39  ? 4.35200   33.62000  34.03700 1.000 36.95220 ? 39  PHE B CB  1 
ATOM   2512 C  CG  . PHE B 1 39  ? 3.58500   33.83800  32.76900 1.000 37.34870 ? 39  PHE B CG  1 
ATOM   2513 C  CD1 . PHE B 1 39  ? 4.11400   34.61100  31.75100 1.000 38.52088 ? 39  PHE B CD1 1 
ATOM   2514 C  CD2 . PHE B 1 39  ? 2.35500   33.24600  32.57800 1.000 37.54627 ? 39  PHE B CD2 1 
ATOM   2515 C  CE1 . PHE B 1 39  ? 3.42600   34.80200  30.57000 1.000 37.83628 ? 39  PHE B CE1 1 
ATOM   2516 C  CE2 . PHE B 1 39  ? 1.65800   33.44100  31.40200 1.000 37.94790 ? 39  PHE B CE2 1 
ATOM   2517 C  CZ  . PHE B 1 39  ? 2.19900   34.21900  30.39600 1.000 37.37235 ? 39  PHE B CZ  1 
ATOM   2518 N  N   . ASP B 1 40  ? 7.58100   33.87100  34.40300 1.000 36.16354 ? 40  ASP B N   1 
ATOM   2519 C  CA  . ASP B 1 40  ? 8.77300   34.62400  34.03000 1.000 37.06354 ? 40  ASP B CA  1 
ATOM   2520 C  C   . ASP B 1 40  ? 9.83000   33.72800  33.39400 1.000 35.96939 ? 40  ASP B C   1 
ATOM   2521 O  O   . ASP B 1 40  ? 10.62600  34.19900  32.57600 1.000 34.81470 ? 40  ASP B O   1 
ATOM   2522 C  CB  . ASP B 1 40  ? 9.34300   35.37900  35.23700 1.000 41.92082 ? 40  ASP B CB  1 
ATOM   2523 C  CG  . ASP B 1 40  ? 9.29700   34.57300  36.52600 1.000 48.15949 ? 40  ASP B CG  1 
ATOM   2524 O  OD1 . ASP B 1 40  ? 8.26400   33.92000  36.80100 1.000 46.43106 ? 40  ASP B OD1 1 
ATOM   2525 O  OD2 . ASP B 1 40  ? 10.29700  34.61200  37.27900 1.000 54.41222 ? 40  ASP B OD2 1 
ATOM   2526 N  N   . VAL B 1 41  ? 9.86000   32.44200  33.74600 1.000 36.10713 ? 41  VAL B N   1 
ATOM   2527 C  CA  . VAL B 1 41  ? 10.65200  31.50500  32.95800 1.000 33.81520 ? 41  VAL B CA  1 
ATOM   2528 C  C   . VAL B 1 41  ? 10.04900  31.36600  31.56600 1.000 32.72134 ? 41  VAL B C   1 
ATOM   2529 O  O   . VAL B 1 41  ? 10.77200  31.31300  30.56100 1.000 32.57100 ? 41  VAL B O   1 
ATOM   2530 C  CB  . VAL B 1 41  ? 10.76500  30.15100  33.68500 1.000 32.40086 ? 41  VAL B CB  1 
ATOM   2531 C  CG1 . VAL B 1 41  ? 11.41400  29.10700  32.78900 1.000 30.99186 ? 41  VAL B CG1 1 
ATOM   2532 C  CG2 . VAL B 1 41  ? 11.57300  30.31400  34.95000 1.000 32.78430 ? 41  VAL B CG2 1 
ATOM   2533 N  N   . VAL B 1 42  ? 8.71500   31.34000  31.48200 1.000 34.08055 ? 42  VAL B N   1 
ATOM   2534 C  CA  . VAL B 1 42  ? 8.04900   31.31300  30.18400 1.000 34.38189 ? 42  VAL B CA  1 
ATOM   2535 C  C   . VAL B 1 42  ? 8.36700   32.58000  29.40600 1.000 32.51752 ? 42  VAL B C   1 
ATOM   2536 O  O   . VAL B 1 42  ? 8.65100   32.53400  28.20400 1.000 31.72073 ? 42  VAL B O   1 
ATOM   2537 C  CB  . VAL B 1 42  ? 6.52900   31.11600  30.35700 1.000 35.14115 ? 42  VAL B CB  1 
ATOM   2538 C  CG1 . VAL B 1 42  ? 5.79400   31.36700  29.04200 1.000 33.67234 ? 42  VAL B CG1 1 
ATOM   2539 C  CG2 . VAL B 1 42  ? 6.22600   29.70700  30.87100 1.000 33.09283 ? 42  VAL B CG2 1 
ATOM   2540 N  N   . GLU B 1 43  ? 8.35500   33.72500  30.07800 1.000 31.78138 ? 43  GLU B N   1 
ATOM   2541 C  CA  . GLU B 1 43  ? 8.61700   34.96500  29.36200 1.000 32.32060 ? 43  GLU B CA  1 
ATOM   2542 C  C   . GLU B 1 43  ? 10.07800  35.05700  28.93100 1.000 31.55306 ? 43  GLU B C   1 
ATOM   2543 O  O   . GLU B 1 43  ? 10.36800  35.51100  27.82400 1.000 30.80398 ? 43  GLU B O   1 
ATOM   2544 C  CB  . GLU B 1 43  ? 8.18800   36.16300  30.21400 1.000 34.70710 ? 43  GLU B CB  1 
ATOM   2545 C  CG  . GLU B 1 43  ? 9.24000   36.75500  31.13700 1.000 36.31317 ? 43  GLU B CG  1 
ATOM   2546 C  CD  . GLU B 1 43  ? 10.11500  37.78900  30.44600 1.000 38.93224 ? 43  GLU B CD  1 
ATOM   2547 O  OE1 . GLU B 1 43  ? 9.58800   38.54600  29.59300 1.000 39.61392 ? 43  GLU B OE1 1 
ATOM   2548 O  OE2 . GLU B 1 43  ? 11.33000  37.83400  30.75100 1.000 38.69466 ? 43  GLU B OE2 1 
ATOM   2549 N  N   . SER B 1 44  ? 11.01300  34.60700  29.77100 1.000 34.08741 ? 44  SER B N   1 
ATOM   2550 C  CA  . SER B 1 44  ? 12.41300  34.57700  29.35800 1.000 32.57790 ? 44  SER B CA  1 
ATOM   2551 C  C   . SER B 1 44  ? 12.58000  33.73300  28.10600 1.000 29.61846 ? 44  SER B C   1 
ATOM   2552 O  O   . SER B 1 44  ? 13.06900  34.20700  27.07600 1.000 29.21740 ? 44  SER B O   1 
ATOM   2553 C  CB  . SER B 1 44  ? 13.28900  34.03300  30.48400 1.000 32.35825 ? 44  SER B CB  1 
ATOM   2554 O  OG  . SER B 1 44  ? 13.39000  34.94800  31.55400 1.000 34.63387 ? 44  SER B OG  1 
ATOM   2555 N  N   . PHE B 1 45  ? 12.14600  32.49000  28.18000 1.000 28.83667 ? 45  PHE B N   1 
ATOM   2556 C  CA  . PHE B 1 45  ? 12.22300  31.59800  26.99600 1.000 27.47859 ? 45  PHE B CA  1 
ATOM   2557 C  C   . PHE B 1 45  ? 11.53600  32.26400  25.81000 1.000 29.07743 ? 45  PHE B C   1 
ATOM   2558 O  O   . PHE B 1 45  ? 12.08300  32.23100  24.71600 1.000 29.60860 ? 45  PHE B O   1 
ATOM   2559 C  CB  . PHE B 1 45  ? 11.64400  30.24000  27.39200 1.000 25.50350 ? 45  PHE B CB  1 
ATOM   2560 C  CG  . PHE B 1 45  ? 11.91800  29.10400  26.42200 1.000 25.75633 ? 45  PHE B CG  1 
ATOM   2561 C  CD1 . PHE B 1 45  ? 12.87000  29.23300  25.42100 1.000 24.70666 ? 45  PHE B CD1 1 
ATOM   2562 C  CD2 . PHE B 1 45  ? 11.26100  27.88900  26.55400 1.000 24.62811 ? 45  PHE B CD2 1 
ATOM   2563 C  CE1 . PHE B 1 45  ? 13.12300  28.19100  24.55100 1.000 24.23653 ? 45  PHE B CE1 1 
ATOM   2564 C  CE2 . PHE B 1 45  ? 11.52400  26.85200  25.68100 1.000 23.73755 ? 45  PHE B CE2 1 
ATOM   2565 C  CZ  . PHE B 1 45  ? 12.45400  27.00500  24.68600 1.000 23.69615 ? 45  PHE B CZ  1 
ATOM   2566 N  N   . ASN B 1 46  ? 10.37500  32.88000  26.03900 1.000 30.00604 ? 46  ASN B N   1 
ATOM   2567 C  CA  . ASN B 1 46  ? 9.63200   33.46800  24.92700 1.000 30.64524 ? 46  ASN B CA  1 
ATOM   2568 C  C   . ASN B 1 46  ? 10.39200  34.62500  24.27000 1.000 30.71571 ? 46  ASN B C   1 
ATOM   2569 O  O   . ASN B 1 46  ? 10.33300  34.79200  23.04900 1.000 29.90157 ? 46  ASN B O   1 
ATOM   2570 C  CB  . ASN B 1 46  ? 8.25700   33.92900  25.40500 1.000 32.07512 ? 46  ASN B CB  1 
ATOM   2571 C  CG  . ASN B 1 46  ? 7.14400   32.98800  24.99600 1.000 31.95858 ? 46  ASN B CG  1 
ATOM   2572 O  OD1 . ASN B 1 46  ? 7.15500   32.43300  23.90200 1.000 31.28423 ? 46  ASN B OD1 1 
ATOM   2573 N  ND2 . ASN B 1 46  ? 6.16600   32.81700  25.87200 1.000 32.49089 ? 46  ASN B ND2 1 
ATOM   2574 N  N   . ARG B 1 47  ? 11.12300  35.42200  25.03600 1.000 29.81851 ? 47  ARG B N   1 
ATOM   2575 C  CA  . ARG B 1 47  ? 11.89000  36.56300  24.47500 1.000 29.12468 ? 47  ARG B CA  1 
ATOM   2576 C  C   . ARG B 1 47  ? 13.19600  36.04800  23.82900 1.000 28.45884 ? 47  ARG B C   1 
ATOM   2577 O  O   . ARG B 1 47  ? 13.70900  36.71100  22.91800 1.000 28.40384 ? 47  ARG B O   1 
ATOM   2578 C  CB  . ARG B 1 47  ? 12.05800  37.62200  25.57500 1.000 31.03902 ? 47  ARG B CB  1 
ATOM   2579 C  CG  . ARG B 1 47  ? 10.78800  38.24600  26.13300 1.000 33.79086 ? 47  ARG B CG  1 
ATOM   2580 C  CD  . ARG B 1 47  ? 9.67000   38.33100  25.11300 1.000 34.16689 ? 47  ARG B CD  1 
ATOM   2581 N  NE  . ARG B 1 47  ? 8.52400   37.52400  25.54100 1.000 34.77300 ? 47  ARG B NE  1 
ATOM   2582 C  CZ  . ARG B 1 47  ? 7.40100   37.35800  24.86300 1.000 34.87412 ? 47  ARG B CZ  1 
ATOM   2583 N  NH1 . ARG B 1 47  ? 7.44100   37.15400  23.56300 1.000 33.37857 ? 47  ARG B NH1 1 
ATOM   2584 N  NH2 . ARG B 1 47  ? 6.24200   37.39300  25.49700 1.000 35.69102 ? 47  ARG B NH2 1 
ATOM   2585 N  N   . GLU B 1 48  ? 13.65900  34.86900  24.24800 1.000 28.67927 ? 48  GLU B N   1 
ATOM   2586 C  CA  . GLU B 1 48  ? 14.83900  34.29900  23.61800 1.000 28.63552 ? 48  GLU B CA  1 
ATOM   2587 C  C   . GLU B 1 48  ? 14.51000  33.66900  22.26900 1.000 30.00135 ? 48  GLU B C   1 
ATOM   2588 O  O   . GLU B 1 48  ? 15.38400  33.59300  21.39900 1.000 29.84258 ? 48  GLU B O   1 
ATOM   2589 C  CB  . GLU B 1 48  ? 15.48200  33.27700  24.55100 1.000 26.55506 ? 48  GLU B CB  1 
ATOM   2590 C  CG  . GLU B 1 48  ? 16.14300  33.91000  25.74700 1.000 27.16476 ? 48  GLU B CG  1 
ATOM   2591 C  CD  . GLU B 1 48  ? 16.41600  32.91500  26.85100 1.000 27.14851 ? 48  GLU B CD  1 
ATOM   2592 O  OE1 . GLU B 1 48  ? 16.19000  31.71500  26.61400 1.000 26.90048 ? 48  GLU B OE1 1 
ATOM   2593 O  OE2 . GLU B 1 48  ? 16.84100  33.32900  27.95400 1.000 27.70589 ? 48  GLU B OE2 1 
ATOM   2594 N  N   . LEU B 1 49  ? 13.26600  33.21800  22.07500 1.000 28.93679 ? 49  LEU B N   1 
ATOM   2595 C  CA  . LEU B 1 49  ? 12.85000  32.71700  20.77100 1.000 29.59157 ? 49  LEU B CA  1 
ATOM   2596 C  C   . LEU B 1 49  ? 12.53400  33.85000  19.79700 1.000 31.31543 ? 49  LEU B C   1 
ATOM   2597 O  O   . LEU B 1 49  ? 12.77300  33.71000  18.59200 1.000 32.82726 ? 49  LEU B O   1 
ATOM   2598 C  CB  . LEU B 1 49  ? 11.64700  31.79200  20.93100 1.000 29.52031 ? 49  LEU B CB  1 
ATOM   2599 C  CG  . LEU B 1 49  ? 11.96300  30.45200  21.58500 1.000 28.16365 ? 49  LEU B CG  1 
ATOM   2600 C  CD1 . LEU B 1 49  ? 10.70600  29.90900  22.21500 1.000 28.45098 ? 49  LEU B CD1 1 
ATOM   2601 C  CD2 . LEU B 1 49  ? 12.51000  29.48000  20.56800 1.000 24.61933 ? 49  LEU B CD2 1 
ATOM   2602 N  N   . ASP B 1 50  ? 12.00600  34.97200  20.29600 1.000 30.13646 ? 50  ASP B N   1 
ATOM   2603 C  CA  . ASP B 1 50  ? 11.84400  36.15300  19.45300 1.000 30.73468 ? 50  ASP B CA  1 
ATOM   2604 C  C   . ASP B 1 50  ? 13.17200  36.56600  18.83500 1.000 31.30968 ? 50  ASP B C   1 
ATOM   2605 O  O   . ASP B 1 50  ? 13.23600  36.90700  17.64800 1.000 32.26895 ? 50  ASP B O   1 
ATOM   2606 C  CB  . ASP B 1 50  ? 11.25600  37.31000  20.26600 1.000 31.08940 ? 50  ASP B CB  1 
ATOM   2607 C  CG  . ASP B 1 50  ? 9.74800   37.17700  20.49900 1.000 32.25306 ? 50  ASP B CG  1 
ATOM   2608 O  OD1 . ASP B 1 50  ? 9.06300   36.48500  19.71500 1.000 33.80549 ? 50  ASP B OD1 1 
ATOM   2609 O  OD2 . ASP B 1 50  ? 9.24600   37.78800  21.46300 1.000 32.01296 ? 50  ASP B OD2 1 
ATOM   2610 N  N   . VAL B 1 51  ? 14.24300  36.54800  19.63100 1.000 32.06405 ? 51  VAL B N   1 
ATOM   2611 C  CA  . VAL B 1 51  ? 15.57900  36.81200  19.10500 1.000 32.17170 ? 51  VAL B CA  1 
ATOM   2612 C  C   . VAL B 1 51  ? 15.89500  35.87900  17.94400 1.000 34.00817 ? 51  VAL B C   1 
ATOM   2613 O  O   . VAL B 1 51  ? 16.44900  36.29600  16.92400 1.000 37.21875 ? 51  VAL B O   1 
ATOM   2614 C  CB  . VAL B 1 51  ? 16.61700  36.68400  20.23200 1.000 31.73295 ? 51  VAL B CB  1 
ATOM   2615 C  CG1 . VAL B 1 51  ? 18.01100  36.54400  19.66400 1.000 33.30454 ? 51  VAL B CG1 1 
ATOM   2616 C  CG2 . VAL B 1 51  ? 16.53400  37.88100  21.12400 1.000 32.42426 ? 51  VAL B CG2 1 
ATOM   2617 N  N   . GLN B 1 52  ? 15.52700  34.60500  18.07000 1.000 32.74592 ? 52  GLN B N   1 
ATOM   2618 C  CA  . GLN B 1 52  ? 15.86000  33.64700  17.02300 1.000 33.85299 ? 52  GLN B CA  1 
ATOM   2619 C  C   . GLN B 1 52  ? 15.00500  33.85700  15.78800 1.000 35.78072 ? 52  GLN B C   1 
ATOM   2620 O  O   . GLN B 1 52  ? 15.48600  33.71800  14.65900 1.000 38.84775 ? 52  GLN B O   1 
ATOM   2621 C  CB  . GLN B 1 52  ? 15.69500  32.22400  17.53900 1.000 32.04385 ? 52  GLN B CB  1 
ATOM   2622 C  CG  . GLN B 1 52  ? 16.66000  31.87500  18.64600 1.000 31.27227 ? 52  GLN B CG  1 
ATOM   2623 C  CD  . GLN B 1 52  ? 18.06000  32.26700  18.28700 1.000 30.26156 ? 52  GLN B CD  1 
ATOM   2624 O  OE1 . GLN B 1 52  ? 18.72200  32.98700  19.02800 1.000 31.75685 ? 52  GLN B OE1 1 
ATOM   2625 N  NE2 . GLN B 1 52  ? 18.52000  31.80700  17.13700 1.000 31.10120 ? 52  GLN B NE2 1 
ATOM   2626 N  N   . MET B 1 53  ? 13.73600  34.18500  15.97500 1.000 34.56077 ? 53  MET B N   1 
ATOM   2627 C  CA  . MET B 1 53  ? 12.91000  34.45700  14.81500 1.000 34.68008 ? 53  MET B CA  1 
ATOM   2628 C  C   . MET B 1 53  ? 13.20600  35.81500  14.21100 1.000 37.61791 ? 53  MET B C   1 
ATOM   2629 O  O   . MET B 1 53  ? 12.65400  36.13800  13.15700 1.000 38.70845 ? 53  MET B O   1 
ATOM   2630 C  CB  . MET B 1 53  ? 11.44300  34.31800  15.20300 1.000 33.56015 ? 53  MET B CB  1 
ATOM   2631 C  CG  . MET B 1 53  ? 11.22900  33.04700  16.00000 1.000 33.07760 ? 53  MET B CG  1 
ATOM   2632 S  SD  . MET B 1 53  ? 9.55500   32.42200  16.01000 1.000 38.56624 ? 53  MET B SD  1 
ATOM   2633 C  CE  . MET B 1 53  ? 9.42000   31.72900  14.37100 1.000 39.64154 ? 53  MET B CE  1 
ATOM   2634 N  N   . ALA B 1 54  ? 14.08300  36.59600  14.83500 1.000 38.86320 ? 54  ALA B N   1 
ATOM   2635 C  CA  . ALA B 1 54  ? 14.60400  37.82100  14.24800 1.000 42.78728 ? 54  ALA B CA  1 
ATOM   2636 C  C   . ALA B 1 54  ? 15.90400  37.60300  13.48500 1.000 45.19976 ? 54  ALA B C   1 
ATOM   2637 O  O   . ALA B 1 54  ? 16.48200  38.56900  12.98500 1.000 44.72140 ? 54  ALA B O   1 
ATOM   2638 C  CB  . ALA B 1 54  ? 14.82600  38.87700  15.33400 1.000 39.93970 ? 54  ALA B CB  1 
ATOM   2639 N  N   . ILE B 1 55  ? 16.37800  36.36600  13.39500 1.000 55.64149 ? 55  ILE B N   1 
ATOM   2640 C  CA  . ILE B 1 55  ? 17.67900  36.07300  12.73700 1.000 54.32461 ? 55  ILE B CA  1 
ATOM   2641 C  C   . ILE B 1 55  ? 17.47700  36.17200  11.23200 1.000 54.43632 ? 55  ILE B C   1 
ATOM   2642 O  O   . ILE B 1 55  ? 16.39200  35.82900  10.76800 1.000 56.28185 ? 55  ILE B O   1 
ATOM   2643 C  CB  . ILE B 1 55  ? 18.22200  34.70100  13.15700 1.000 52.71774 ? 55  ILE B CB  1 
ATOM   2644 C  CG1 . ILE B 1 55  ? 18.84200  34.74100  14.54300 1.000 52.94910 ? 55  ILE B CG1 1 
ATOM   2645 C  CG2 . ILE B 1 55  ? 19.21600  34.15900  12.13200 1.000 56.84025 ? 55  ILE B CG2 1 
ATOM   2646 C  CD1 . ILE B 1 55  ? 19.85000  33.63500  14.77700 1.000 51.59240 ? 55  ILE B CD1 1 
ATOM   2647 N  N   . PRO B 1 56  ? 18.45000  36.69500  10.46900 1.000 56.70398 ? 56  PRO B N   1 
ATOM   2648 C  CA  . PRO B 1 56  ? 18.29300  36.76300  9.01700  1.000 58.54149 ? 56  PRO B CA  1 
ATOM   2649 C  C   . PRO B 1 56  ? 18.11500  35.37900  8.43200  1.000 61.66508 ? 56  PRO B C   1 
ATOM   2650 O  O   . PRO B 1 56  ? 18.62000  34.38100  8.98400  1.000 63.01436 ? 56  PRO B O   1 
ATOM   2651 C  CB  . PRO B 1 56  ? 19.60500  37.40900  8.54800  1.000 56.25885 ? 56  PRO B CB  1 
ATOM   2652 C  CG  . PRO B 1 56  ? 20.11400  38.15600  9.71900  1.000 56.02190 ? 56  PRO B CG  1 
ATOM   2653 C  CD  . PRO B 1 56  ? 19.68500  37.36500  10.92100 1.000 55.22378 ? 56  PRO B CD  1 
ATOM   2654 N  N   . PRO B 1 57  ? 17.38200  35.25800  7.33000  1.000 62.23024 ? 57  PRO B N   1 
ATOM   2655 C  CA  . PRO B 1 57  ? 17.26800  33.96100  6.64300  1.000 64.79110 ? 57  PRO B CA  1 
ATOM   2656 C  C   . PRO B 1 57  ? 18.62900  33.47100  6.18100  1.000 65.62486 ? 57  PRO B C   1 
ATOM   2657 O  O   . PRO B 1 57  ? 19.37200  34.21700  5.52600  1.000 66.25672 ? 57  PRO B O   1 
ATOM   2658 C  CB  . PRO B 1 57  ? 16.35800  34.27300  5.44600  1.000 65.89736 ? 57  PRO B CB  1 
ATOM   2659 C  CG  . PRO B 1 57  ? 15.59700  35.50500  5.85800  1.000 65.84881 ? 57  PRO B CG  1 
ATOM   2660 C  CD  . PRO B 1 57  ? 16.52800  36.29600  6.72200  1.000 61.36808 ? 57  PRO B CD  1 
ATOM   2661 N  N   . PRO B 1 58  ? 18.98500  32.22100  6.48000  1.000 67.84270 ? 58  PRO B N   1 
ATOM   2662 C  CA  . PRO B 1 58  ? 20.33600  31.74300  6.16200  1.000 68.46482 ? 58  PRO B CA  1 
ATOM   2663 C  C   . PRO B 1 58  ? 20.49400  31.41100  4.68700  1.000 69.93847 ? 58  PRO B C   1 
ATOM   2664 O  O   . PRO B 1 58  ? 19.63200  30.77700  4.07200  1.000 69.28726 ? 58  PRO B O   1 
ATOM   2665 C  CB  . PRO B 1 58  ? 20.46900  30.48400  7.02200  1.000 64.86672 ? 58  PRO B CB  1 
ATOM   2666 C  CG  . PRO B 1 58  ? 19.07500  29.95700  7.06400  1.000 65.17723 ? 58  PRO B CG  1 
ATOM   2667 C  CD  . PRO B 1 58  ? 18.14200  31.15100  7.03600  1.000 66.42645 ? 58  PRO B CD  1 
ATOM   2668 N  N   . LYS B 1 59  ? 21.63800  31.82700  4.13000  1.000 73.81262 ? 59  LYS B N   1 
ATOM   2669 C  CA  . LYS B 1 59  ? 21.95400  31.69000  2.70900  1.000 73.56212 ? 59  LYS B CA  1 
ATOM   2670 C  C   . LYS B 1 59  ? 22.39500  30.27200  2.31700  1.000 71.25422 ? 59  LYS B C   1 
ATOM   2671 O  O   . LYS B 1 59  ? 23.21600  30.11600  1.40800  1.000 72.20183 ? 59  LYS B O   1 
ATOM   2672 C  CB  . LYS B 1 59  ? 23.02800  32.70400  2.31300  1.000 75.28148 ? 59  LYS B CB  1 
ATOM   2673 N  N   . GLY B 1 60  ? 21.86600  29.23000  2.96500  1.000 66.14517 ? 60  GLY B N   1 
ATOM   2674 C  CA  . GLY B 1 60  ? 22.20600  27.87700  2.56600  1.000 61.02282 ? 60  GLY B CA  1 
ATOM   2675 C  C   . GLY B 1 60  ? 21.06600  26.88200  2.69200  1.000 56.58557 ? 60  GLY B C   1 
ATOM   2676 O  O   . GLY B 1 60  ? 19.90400  27.28300  2.81000  1.000 57.02087 ? 60  GLY B O   1 
ATOM   2677 N  N   . GLU B 1 61  ? 21.38400  25.58600  2.66900  1.000 51.38134 ? 61  GLU B N   1 
ATOM   2678 C  CA  . GLU B 1 61  ? 20.37100  24.54900  2.83400  1.000 50.16257 ? 61  GLU B CA  1 
ATOM   2679 C  C   . GLU B 1 61  ? 19.69700  24.65000  4.19700  1.000 49.90667 ? 61  GLU B C   1 
ATOM   2680 O  O   . GLU B 1 61  ? 20.28400  25.13000  5.16800  1.000 48.73871 ? 61  GLU B O   1 
ATOM   2681 C  CB  . GLU B 1 61  ? 21.00300  23.17100  2.69900  1.000 44.25403 ? 61  GLU B CB  1 
ATOM   2682 C  CG  . GLU B 1 61  ? 22.14500  22.97500  3.66300  1.000 41.43841 ? 61  GLU B CG  1 
ATOM   2683 C  CD  . GLU B 1 61  ? 22.27800  21.54300  4.14800  1.000 36.54603 ? 61  GLU B CD  1 
ATOM   2684 O  OE1 . GLU B 1 61  ? 21.97800  20.60700  3.37100  1.000 35.67345 ? 61  GLU B OE1 1 
ATOM   2685 O  OE2 . GLU B 1 61  ? 22.68900  21.35900  5.31200  1.000 36.43106 ? 61  GLU B OE2 1 
ATOM   2686 N  N   . ARG B 1 62  ? 18.45500  24.17100  4.27000  1.000 54.17623 ? 62  ARG B N   1 
ATOM   2687 C  CA  . ARG B 1 62  ? 17.72600  24.08900  5.53800  1.000 54.58986 ? 62  ARG B CA  1 
ATOM   2688 C  C   . ARG B 1 62  ? 16.87100  22.83000  5.50200  1.000 54.61500 ? 62  ARG B C   1 
ATOM   2689 O  O   . ARG B 1 62  ? 15.85600  22.80000  4.80400  1.000 58.39359 ? 62  ARG B O   1 
ATOM   2690 C  CB  . ARG B 1 62  ? 16.85900  25.32100  5.77700  1.000 58.94133 ? 62  ARG B CB  1 
ATOM   2691 C  CG  . ARG B 1 62  ? 17.60100  26.53100  6.29200  1.000 62.38439 ? 62  ARG B CG  1 
ATOM   2692 C  CD  . ARG B 1 62  ? 16.66100  27.44100  7.06400  1.000 68.10940 ? 62  ARG B CD  1 
ATOM   2693 N  NE  . ARG B 1 62  ? 16.25000  26.86100  8.34000  1.000 66.20936 ? 62  ARG B NE  1 
ATOM   2694 C  CZ  . ARG B 1 62  ? 16.55700  27.35300  9.53500  1.000 64.90756 ? 62  ARG B CZ  1 
ATOM   2695 N  NH1 . ARG B 1 62  ? 17.29600  28.44100  9.66700  1.000 70.66139 ? 62  ARG B NH1 1 
ATOM   2696 N  NH2 . ARG B 1 62  ? 16.10000  26.74300  10.62600 1.000 59.66270 ? 62  ARG B NH2 1 
ATOM   2697 N  N   . LEU B 1 63  ? 17.26200  21.80900  6.27200  1.000 48.72582 ? 63  LEU B N   1 
ATOM   2698 C  CA  . LEU B 1 63  ? 16.76600  20.45100  6.04700  1.000 47.16822 ? 63  LEU B CA  1 
ATOM   2699 C  C   . LEU B 1 63  ? 15.24800  20.37400  6.12200  1.000 49.58878 ? 63  LEU B C   1 
ATOM   2700 O  O   . LEU B 1 63  ? 14.58800  19.96200  5.16300  1.000 50.90751 ? 63  LEU B O   1 
ATOM   2701 C  CB  . LEU B 1 63  ? 17.41500  19.49100  7.04400  1.000 40.85566 ? 63  LEU B CB  1 
ATOM   2702 C  CG  . LEU B 1 63  ? 18.90000  19.34100  6.71300  1.000 36.38145 ? 63  LEU B CG  1 
ATOM   2703 C  CD1 . LEU B 1 63  ? 19.60800  18.41700  7.67400  1.000 35.68892 ? 63  LEU B CD1 1 
ATOM   2704 C  CD2 . LEU B 1 63  ? 19.01900  18.84000  5.29900  1.000 35.60419 ? 63  LEU B CD2 1 
ATOM   2705 N  N   . LEU B 1 64  ? 14.67700  20.77100  7.25100  1.000 48.96285 ? 64  LEU B N   1 
ATOM   2706 C  CA  . LEU B 1 64  ? 13.22900  20.83300  7.38200  1.000 51.70768 ? 64  LEU B CA  1 
ATOM   2707 C  C   . LEU B 1 64  ? 12.64200  22.17400  6.93400  1.000 55.68180 ? 64  LEU B C   1 
ATOM   2708 O  O   . LEU B 1 64  ? 11.43000  22.25900  6.70800  1.000 58.29959 ? 64  LEU B O   1 
ATOM   2709 C  CB  . LEU B 1 64  ? 12.82900  20.53900  8.83400  1.000 46.11180 ? 64  LEU B CB  1 
ATOM   2710 C  CG  . LEU B 1 64  ? 11.36100  20.19100  9.11200  1.000 48.08385 ? 64  LEU B CG  1 
ATOM   2711 C  CD1 . LEU B 1 64  ? 10.98300  18.88700  8.45400  1.000 50.02714 ? 64  LEU B CD1 1 
ATOM   2712 C  CD2 . LEU B 1 64  ? 11.08100  20.12800  10.59900 1.000 45.75100 ? 64  LEU B CD2 1 
ATOM   2713 N  N   . ALA B 1 65  ? 13.46200  23.21300  6.77700  1.000 59.11060 ? 65  ALA B N   1 
ATOM   2714 C  CA  . ALA B 1 65  ? 12.95800  24.54400  6.45800  1.000 64.32849 ? 65  ALA B CA  1 
ATOM   2715 C  C   . ALA B 1 65  ? 13.10500  24.91600  4.98700  1.000 66.04562 ? 65  ALA B C   1 
ATOM   2716 O  O   . ALA B 1 65  ? 12.20400  25.54800  4.42700  1.000 70.20867 ? 65  ALA B O   1 
ATOM   2717 C  CB  . ALA B 1 65  ? 13.65100  25.59000  7.32500  1.000 65.09400 ? 65  ALA B CB  1 
ATOM   2718 N  N   . ASP B 1 66  ? 14.20500  24.54400  4.33100  1.000 61.36309 ? 66  ASP B N   1 
ATOM   2719 C  CA  . ASP B 1 66  ? 14.10800  24.62900  2.87200  1.000 61.57908 ? 66  ASP B CA  1 
ATOM   2720 C  C   . ASP B 1 66  ? 13.24000  23.53300  2.30600  1.000 62.28083 ? 66  ASP B C   1 
ATOM   2721 O  O   . ASP B 1 66  ? 13.16500  23.36000  1.07800  1.000 64.92565 ? 66  ASP B O   1 
ATOM   2722 C  CB  . ASP B 1 66  ? 15.48900  24.58600  2.21400  1.000 60.30535 ? 66  ASP B CB  1 
ATOM   2723 C  CG  . ASP B 1 66  ? 16.17900  25.93600  2.21300  1.000 59.32881 ? 66  ASP B CG  1 
ATOM   2724 O  OD1 . ASP B 1 66  ? 15.49300  26.95000  2.45900  1.000 59.75919 ? 66  ASP B OD1 1 
ATOM   2725 O  OD2 . ASP B 1 66  ? 17.40500  25.97900  1.96200  1.000 57.36818 ? 66  ASP B OD2 1 
ATOM   2726 N  N   . LYS B 1 67  ? 12.58700  22.77700  3.19200  1.000 62.94780 ? 67  LYS B N   1 
ATOM   2727 C  CA  . LYS B 1 67  ? 11.58000  21.81300  2.77600  1.000 62.76432 ? 67  LYS B CA  1 
ATOM   2728 C  C   . LYS B 1 67  ? 10.23300  22.47800  2.49400  1.000 66.92017 ? 67  LYS B C   1 
ATOM   2729 O  O   . LYS B 1 67  ? 9.45300   21.96100  1.68500  1.000 60.71382 ? 67  LYS B O   1 
ATOM   2730 C  CB  . LYS B 1 67  ? 11.44400  20.72300  3.84600  1.000 59.68549 ? 67  LYS B CB  1 
ATOM   2731 C  CG  . LYS B 1 67  ? 10.40800  19.64400  3.54800  1.000 56.02039 ? 67  LYS B CG  1 
ATOM   2732 C  CD  . LYS B 1 67  ? 10.77400  18.30800  4.20000  1.000 54.77662 ? 67  LYS B CD  1 
ATOM   2733 C  CE  . LYS B 1 67  ? 9.81700   17.91900  5.32500  1.000 53.30210 ? 67  LYS B CE  1 
ATOM   2734 N  NZ  . LYS B 1 67  ? 8.41200   17.69800  4.88000  1.000 50.75600 ? 67  LYS B NZ  1 
ATOM   2735 N  N   . TYR B 1 68  ? 9.95400   23.62100  3.11600  1.000 73.28877 ? 68  TYR B N   1 
ATOM   2736 C  CA  . TYR B 1 68  ? 8.65000   24.26800  3.07700  1.000 76.93136 ? 68  TYR B CA  1 
ATOM   2737 C  C   . TYR B 1 68  ? 8.74300   25.69500  2.56900  1.000 79.66348 ? 68  TYR B C   1 
ATOM   2738 O  O   . TYR B 1 68  ? 9.83300   26.26800  2.46900  1.000 79.17159 ? 68  TYR B O   1 
ATOM   2739 C  CB  . TYR B 1 68  ? 8.01000   24.26900  4.47800  1.000 79.95803 ? 68  TYR B CB  1 
ATOM   2740 C  CG  . TYR B 1 68  ? 7.59500   22.89400  4.98000  1.000 74.02008 ? 68  TYR B CG  1 
ATOM   2741 C  CD1 . TYR B 1 68  ? 8.55700   22.03600  5.50900  1.000 69.66375 ? 68  TYR B CD1 1 
ATOM   2742 C  CD2 . TYR B 1 68  ? 6.26300   22.48700  4.91500  1.000 71.13675 ? 68  TYR B CD2 1 
ATOM   2743 C  CE1 . TYR B 1 68  ? 8.17800   20.79700  5.95400  1.000 66.69708 ? 68  TYR B CE1 1 
ATOM   2744 C  CE2 . TYR B 1 68  ? 5.92200   21.23900  5.37200  1.000 65.93996 ? 68  TYR B CE2 1 
ATOM   2745 C  CZ  . TYR B 1 68  ? 6.86300   20.36700  5.89800  1.000 63.74419 ? 68  TYR B CZ  1 
ATOM   2746 O  OH  . TYR B 1 68  ? 6.53500   19.14200  6.34900  1.000 60.42267 ? 68  TYR B OH  1 
ATOM   2747 N  N   . PRO B 1 69  ? 7.60800   26.28200  2.19000  1.000 81.63536 ? 69  PRO B N   1 
ATOM   2748 C  CA  . PRO B 1 69  ? 7.54100   27.73600  1.93300  1.000 82.92409 ? 69  PRO B CA  1 
ATOM   2749 C  C   . PRO B 1 69  ? 7.65800   28.53700  3.22200  1.000 86.48763 ? 69  PRO B C   1 
ATOM   2750 O  O   . PRO B 1 69  ? 7.67700   27.95500  4.31900  1.000 89.16099 ? 69  PRO B O   1 
ATOM   2751 C  CB  . PRO B 1 69  ? 6.15600   27.90400  1.28500  1.000 80.78186 ? 69  PRO B CB  1 
ATOM   2752 C  CG  . PRO B 1 69  ? 5.86600   26.56000  0.66100  1.000 82.13396 ? 69  PRO B CG  1 
ATOM   2753 C  CD  . PRO B 1 69  ? 6.45800   25.56100  1.60900  1.000 81.55084 ? 69  PRO B CD  1 
ATOM   2754 N  N   . LYS B 1 73  ? 7.06300   28.33300  10.32100 1.000 55.37325 ? 73  LYS B N   1 
ATOM   2755 C  CA  . LYS B 1 73  ? 7.61600   28.96700  11.50600 1.000 54.22563 ? 73  LYS B CA  1 
ATOM   2756 C  C   . LYS B 1 73  ? 8.31800   27.89500  12.32500 1.000 54.33456 ? 73  LYS B C   1 
ATOM   2757 O  O   . LYS B 1 73  ? 7.67200   26.97700  12.83400 1.000 54.09344 ? 73  LYS B O   1 
ATOM   2758 C  CB  . LYS B 1 73  ? 6.53200   29.67100  12.30800 1.000 52.76550 ? 73  LYS B CB  1 
ATOM   2759 C  CG  . LYS B 1 73  ? 5.92800   30.87100  11.59700 1.000 52.93628 ? 73  LYS B CG  1 
ATOM   2760 C  CD  . LYS B 1 73  ? 6.96400   31.93200  11.25100 1.000 53.58071 ? 73  LYS B CD  1 
ATOM   2761 C  CE  . LYS B 1 73  ? 6.30200   33.22900  10.80500 1.000 53.88425 ? 73  LYS B CE  1 
ATOM   2762 N  NZ  . LYS B 1 73  ? 5.36400   33.03600  9.66900  1.000 54.76153 ? 73  LYS B NZ  1 
ATOM   2763 N  N   . TYR B 1 74  ? 9.63900   28.02100  12.45000 1.000 41.30303 ? 74  TYR B N   1 
ATOM   2764 C  CA  . TYR B 1 74  ? 10.49100  26.93000  12.90400 1.000 36.26603 ? 74  TYR B CA  1 
ATOM   2765 C  C   . TYR B 1 74  ? 11.73800  27.48300  13.58300 1.000 32.70439 ? 74  TYR B C   1 
ATOM   2766 O  O   . TYR B 1 74  ? 12.43400  28.32700  13.01000 1.000 31.99390 ? 74  TYR B O   1 
ATOM   2767 C  CB  . TYR B 1 74  ? 10.89300  26.06000  11.71400 1.000 35.74048 ? 74  TYR B CB  1 
ATOM   2768 C  CG  . TYR B 1 74  ? 11.69200  24.82400  12.09300 1.000 34.16856 ? 74  TYR B CG  1 
ATOM   2769 C  CD1 . TYR B 1 74  ? 11.32700  24.09700  13.22400 1.000 32.42739 ? 74  TYR B CD1 1 
ATOM   2770 C  CD2 . TYR B 1 74  ? 12.79100  24.42600  11.33500 1.000 36.52368 ? 74  TYR B CD2 1 
ATOM   2771 C  CE1 . TYR B 1 74  ? 12.05100  22.98700  13.56900 1.000 32.03759 ? 74  TYR B CE1 1 
ATOM   2772 C  CE2 . TYR B 1 74  ? 13.49100  23.30700  11.71200 1.000 36.01803 ? 74  TYR B CE2 1 
ATOM   2773 C  CZ  . TYR B 1 74  ? 13.14500  22.56400  12.83100 1.000 32.61452 ? 74  TYR B CZ  1 
ATOM   2774 O  OH  . TYR B 1 74  ? 13.83800  21.46800  13.19900 1.000 32.28532 ? 74  TYR B OH  1 
ATOM   2775 N  N   . VAL B 1 75  ? 12.02800  26.99100  14.78700 1.000 31.31301 ? 75  VAL B N   1 
ATOM   2776 C  CA  . VAL B 1 75  ? 13.29200  27.27000  15.47100 1.000 30.36951 ? 75  VAL B CA  1 
ATOM   2777 C  C   . VAL B 1 75  ? 13.91400  25.94600  15.91000 1.000 28.20435 ? 75  VAL B C   1 
ATOM   2778 O  O   . VAL B 1 75  ? 13.42800  25.31300  16.85600 1.000 25.97461 ? 75  VAL B O   1 
ATOM   2779 C  CB  . VAL B 1 75  ? 13.09800  28.21900  16.66400 1.000 28.52789 ? 75  VAL B CB  1 
ATOM   2780 C  CG1 . VAL B 1 75  ? 14.40700  28.41500  17.38300 1.000 27.15466 ? 75  VAL B CG1 1 
ATOM   2781 C  CG2 . VAL B 1 75  ? 12.55400  29.56700  16.20200 1.000 29.05942 ? 75  VAL B CG2 1 
ATOM   2782 N  N   . PRO B 1 76  ? 14.96800  25.48200  15.25400 1.000 28.16073 ? 76  PRO B N   1 
ATOM   2783 C  CA  . PRO B 1 76  ? 15.52800  24.17100  15.58500 1.000 26.31374 ? 76  PRO B CA  1 
ATOM   2784 C  C   . PRO B 1 76  ? 16.42000  24.23700  16.81100 1.000 24.94221 ? 76  PRO B C   1 
ATOM   2785 O  O   . PRO B 1 76  ? 16.94500  25.28800  17.16800 1.000 25.86336 ? 76  PRO B O   1 
ATOM   2786 C  CB  . PRO B 1 76  ? 16.35100  23.82700  14.34500 1.000 27.23539 ? 76  PRO B CB  1 
ATOM   2787 C  CG  . PRO B 1 76  ? 16.80700  25.15000  13.87900 1.000 29.30823 ? 76  PRO B CG  1 
ATOM   2788 C  CD  . PRO B 1 76  ? 15.67200  26.10500  14.12200 1.000 28.75303 ? 76  PRO B CD  1 
ATOM   2789 N  N   . ASN B 1 77  ? 16.61600  23.06600  17.42100 1.000 23.64599 ? 77  ASN B N   1 
ATOM   2790 C  CA  . ASN B 1 77  ? 17.52600  22.85800  18.54600 1.000 23.24356 ? 77  ASN B CA  1 
ATOM   2791 C  C   . ASN B 1 77  ? 17.60900  24.06100  19.47900 1.000 23.52589 ? 77  ASN B C   1 
ATOM   2792 O  O   . ASN B 1 77  ? 18.66000  24.70200  19.57000 1.000 24.70229 ? 77  ASN B O   1 
ATOM   2793 C  CB  . ASN B 1 77  ? 18.92900  22.47600  18.04600 1.000 22.24969 ? 77  ASN B CB  1 
ATOM   2794 C  CG  . ASN B 1 77  ? 19.42700  23.35900  16.92000 1.000 23.79292 ? 77  ASN B CG  1 
ATOM   2795 O  OD1 . ASN B 1 77  ? 19.29700  23.01500  15.75100 1.000 24.09124 ? 77  ASN B OD1 1 
ATOM   2796 N  ND2 . ASN B 1 77  ? 20.02000  24.49200  17.26800 1.000 24.64615 ? 77  ASN B ND2 1 
ATOM   2797 N  N   . VAL B 1 78  ? 16.51600  24.37200  20.18200 1.000 22.59834 ? 78  VAL B N   1 
ATOM   2798 C  CA  . VAL B 1 78  ? 16.48000  25.60800  20.94800 1.000 22.96002 ? 78  VAL B CA  1 
ATOM   2799 C  C   . VAL B 1 78  ? 17.45000  25.56400  22.11900 1.000 23.73468 ? 78  VAL B C   1 
ATOM   2800 O  O   . VAL B 1 78  ? 17.79500  26.61200  22.66900 1.000 23.66990 ? 78  VAL B O   1 
ATOM   2801 C  CB  . VAL B 1 78  ? 15.05300  25.93900  21.43800 1.000 23.19210 ? 78  VAL B CB  1 
ATOM   2802 C  CG1 . VAL B 1 78  ? 14.08700  25.98200  20.27800 1.000 24.14031 ? 78  VAL B CG1 1 
ATOM   2803 C  CG2 . VAL B 1 78  ? 14.58300  24.95400  22.47900 1.000 22.54502 ? 78  VAL B CG2 1 
ATOM   2804 N  N   . ALA B 1 79  ? 17.93200  24.38100  22.50100 1.000 22.61708 ? 79  ALA B N   1 
ATOM   2805 C  CA  . ALA B 1 79  ? 18.87400  24.30700  23.61200 1.000 22.50850 ? 79  ALA B CA  1 
ATOM   2806 C  C   . ALA B 1 79  ? 20.14700  25.09800  23.33800 1.000 23.56014 ? 79  ALA B C   1 
ATOM   2807 O  O   . ALA B 1 79  ? 20.79000  25.57400  24.27900 1.000 24.70813 ? 79  ALA B O   1 
ATOM   2808 C  CB  . ALA B 1 79  ? 19.22000  22.85100  23.92200 1.000 21.99783 ? 79  ALA B CB  1 
ATOM   2809 N  N   . THR B 1 80  ? 20.53900  25.25400  22.07500 1.000 22.81652 ? 80  THR B N   1 
ATOM   2810 C  CA  . THR B 1 80  ? 21.81500  25.90500  21.81200 1.000 24.49658 ? 80  THR B CA  1 
ATOM   2811 C  C   . THR B 1 80  ? 21.70000  27.41700  21.69600 1.000 25.94305 ? 80  THR B C   1 
ATOM   2812 O  O   . THR B 1 80  ? 22.72600  28.10000  21.75700 1.000 27.12716 ? 80  THR B O   1 
ATOM   2813 C  CB  . THR B 1 80  ? 22.48700  25.35600  20.53800 1.000 25.00755 ? 80  THR B CB  1 
ATOM   2814 O  OG1 . THR B 1 80  ? 21.80200  25.83600  19.37700 1.000 25.93323 ? 80  THR B OG1 1 
ATOM   2815 C  CG2 . THR B 1 80  ? 22.50100  23.83500  20.52400 1.000 23.21184 ? 80  THR B CG2 1 
ATOM   2816 N  N   . THR B 1 81  ? 20.49300  27.96600  21.54300 1.000 25.82394 ? 81  THR B N   1 
ATOM   2817 C  CA  . THR B 1 81  ? 20.32800  29.40200  21.36300 1.000 25.75400 ? 81  THR B CA  1 
ATOM   2818 C  C   . THR B 1 81  ? 19.52900  30.08600  22.46200 1.000 26.39004 ? 81  THR B C   1 
ATOM   2819 O  O   . THR B 1 81  ? 19.51500  31.32200  22.50700 1.000 26.97815 ? 81  THR B O   1 
ATOM   2820 C  CB  . THR B 1 81  ? 19.65900  29.70900  20.01000 1.000 27.08164 ? 81  THR B CB  1 
ATOM   2821 O  OG1 . THR B 1 81  ? 18.38100  29.06400  19.93500 1.000 26.81630 ? 81  THR B OG1 1 
ATOM   2822 C  CG2 . THR B 1 81  ? 20.53100  29.24800  18.85300 1.000 26.92920 ? 81  THR B CG2 1 
ATOM   2823 N  N   . CYS B 1 82  ? 18.86000  29.33600  23.33700 1.000 26.47473 ? 82  CYS B N   1 
ATOM   2824 C  CA  . CYS B 1 82  ? 18.03800  29.91100  24.40100 1.000 25.32919 ? 82  CYS B CA  1 
ATOM   2825 C  C   . CYS B 1 82  ? 18.56800  29.42400  25.73600 1.000 25.63844 ? 82  CYS B C   1 
ATOM   2826 O  O   . CYS B 1 82  ? 18.26200  28.29400  26.15300 1.000 25.07379 ? 82  CYS B O   1 
ATOM   2827 C  CB  . CYS B 1 82  ? 16.57000  29.52900  24.23800 1.000 24.15659 ? 82  CYS B CB  1 
ATOM   2828 S  SG  . CYS B 1 82  ? 15.88800  29.93200  22.65000 1.000 26.00294 ? 82  CYS B SG  1 
ATOM   2829 N  N   . PRO B 1 83  ? 19.35500  30.23100  26.44300 1.000 26.10923 ? 83  PRO B N   1 
ATOM   2830 C  CA  . PRO B 1 83  ? 19.86500  29.79500  27.75200 1.000 26.44759 ? 83  PRO B CA  1 
ATOM   2831 C  C   . PRO B 1 83  ? 18.78000  29.41100  28.74600 1.000 25.34859 ? 83  PRO B C   1 
ATOM   2832 O  O   . PRO B 1 83  ? 19.04100  28.59400  29.63600 1.000 24.89344 ? 83  PRO B O   1 
ATOM   2833 C  CB  . PRO B 1 83  ? 20.66100  31.01500  28.23100 1.000 27.31488 ? 83  PRO B CB  1 
ATOM   2834 C  CG  . PRO B 1 83  ? 21.01700  31.74600  26.98800 1.000 28.37717 ? 83  PRO B CG  1 
ATOM   2835 C  CD  . PRO B 1 83  ? 19.86300  31.55700  26.06000 1.000 26.61848 ? 83  PRO B CD  1 
ATOM   2836 N  N   . THR B 1 84  ? 17.57600  29.98400  28.63300 1.000 26.44716 ? 84  THR B N   1 
ATOM   2837 C  CA  . THR B 1 84  ? 16.49200  29.64000  29.55000 1.000 25.60466 ? 84  THR B CA  1 
ATOM   2838 C  C   . THR B 1 84  ? 16.07500  28.18700  29.40800 1.000 24.02672 ? 84  THR B C   1 
ATOM   2839 O  O   . THR B 1 84  ? 15.75900  27.53100  30.40600 1.000 24.01949 ? 84  THR B O   1 
ATOM   2840 C  CB  . THR B 1 84  ? 15.29500  30.55000  29.31600 1.000 25.78269 ? 84  THR B CB  1 
ATOM   2841 O  OG1 . THR B 1 84  ? 15.68100  31.90100  29.57700 1.000 26.07348 ? 84  THR B OG1 1 
ATOM   2842 C  CG2 . THR B 1 84  ? 14.12100  30.14300  30.21200 1.000 27.24547 ? 84  THR B CG2 1 
ATOM   2843 N  N   . PHE B 1 85  ? 16.06400  27.66200  28.18200 1.000 24.70722 ? 85  PHE B N   1 
ATOM   2844 C  CA  . PHE B 1 85  ? 15.76000  26.24500  27.99900 1.000 24.20920 ? 85  PHE B CA  1 
ATOM   2845 C  C   . PHE B 1 85  ? 16.84500  25.36600  28.60800 1.000 23.17875 ? 85  PHE B C   1 
ATOM   2846 O  O   . PHE B 1 85  ? 16.57100  24.55700  29.49600 1.000 23.08615 ? 85  PHE B O   1 
ATOM   2847 C  CB  . PHE B 1 85  ? 15.56600  25.90400  26.51600 1.000 23.51560 ? 85  PHE B CB  1 
ATOM   2848 C  CG  . PHE B 1 85  ? 15.12800  24.48000  26.28500 1.000 22.14165 ? 85  PHE B CG  1 
ATOM   2849 C  CD1 . PHE B 1 85  ? 13.83500  24.09400  26.55200 1.000 22.03841 ? 85  PHE B CD1 1 
ATOM   2850 C  CD2 . PHE B 1 85  ? 16.01400  23.53100  25.82900 1.000 21.95857 ? 85  PHE B CD2 1 
ATOM   2851 C  CE1 . PHE B 1 85  ? 13.44000  22.79200  26.36500 1.000 21.88064 ? 85  PHE B CE1 1 
ATOM   2852 C  CE2 . PHE B 1 85  ? 15.61800  22.23500  25.64000 1.000 21.41998 ? 85  PHE B CE2 1 
ATOM   2853 C  CZ  . PHE B 1 85  ? 14.32900  21.86800  25.90700 1.000 21.51543 ? 85  PHE B CZ  1 
ATOM   2854 N  N   . ARG B 1 86  ? 18.09300  25.52400  28.16100 1.000 23.24132 ? 86  ARG B N   1 
ATOM   2855 C  CA  . ARG B 1 86  ? 19.11900  24.55700  28.53200 1.000 22.94447 ? 86  ARG B CA  1 
ATOM   2856 C  C   . ARG B 1 86  ? 19.54700  24.67900  29.98300 1.000 23.45078 ? 86  ARG B C   1 
ATOM   2857 O  O   . ARG B 1 86  ? 20.04700  23.70100  30.54400 1.000 26.26802 ? 86  ARG B O   1 
ATOM   2858 C  CB  . ARG B 1 86  ? 20.34200  24.68300  27.62000 1.000 24.01440 ? 86  ARG B CB  1 
ATOM   2859 C  CG  . ARG B 1 86  ? 21.18400  25.89900  27.85400 1.000 24.14389 ? 86  ARG B CG  1 
ATOM   2860 C  CD  . ARG B 1 86  ? 22.41200  25.88800  26.98300 1.000 24.69224 ? 86  ARG B CD  1 
ATOM   2861 N  NE  . ARG B 1 86  ? 22.92300  27.23800  26.82600 1.000 26.01740 ? 86  ARG B NE  1 
ATOM   2862 C  CZ  . ARG B 1 86  ? 22.57100  28.04300  25.84100 1.000 25.24379 ? 86  ARG B CZ  1 
ATOM   2863 N  NH1 . ARG B 1 86  ? 21.77900  27.63700  24.87300 1.000 27.34081 ? 86  ARG B NH1 1 
ATOM   2864 N  NH2 . ARG B 1 86  ? 23.01400  29.28800  25.83100 1.000 28.62862 ? 86  ARG B NH2 1 
ATOM   2865 N  N   . ASN B 1 87  ? 19.35500  25.83000  30.61800 1.000 23.72694 ? 87  ASN B N   1 
ATOM   2866 C  CA  . ASN B 1 87  ? 19.76800  25.99200  32.00200 1.000 23.04010 ? 87  ASN B CA  1 
ATOM   2867 C  C   . ASN B 1 87  ? 18.62200  26.02000  32.99800 1.000 23.82862 ? 87  ASN B C   1 
ATOM   2868 O  O   . ASN B 1 87  ? 18.88200  26.06800  34.20300 1.000 24.66850 ? 87  ASN B O   1 
ATOM   2869 C  CB  . ASN B 1 87  ? 20.59700  27.26600  32.15800 1.000 24.65208 ? 87  ASN B CB  1 
ATOM   2870 C  CG  . ASN B 1 87  ? 21.95100  27.13500  31.50500 1.000 27.15566 ? 87  ASN B CG  1 
ATOM   2871 O  OD1 . ASN B 1 87  ? 22.52900  26.04100  31.47800 1.000 26.79155 ? 87  ASN B OD1 1 
ATOM   2872 N  ND2 . ASN B 1 87  ? 22.45900  28.23400  30.95000 1.000 28.08983 ? 87  ASN B ND2 1 
ATOM   2873 N  N   . THR B 1 88  ? 17.37400  25.99500  32.54100 1.000 24.15284 ? 88  THR B N   1 
ATOM   2874 C  CA  . THR B 1 88  ? 16.25500  25.92400  33.46400 1.000 23.60243 ? 88  THR B CA  1 
ATOM   2875 C  C   . THR B 1 88  ? 15.28700  24.84800  33.02300 1.000 23.48326 ? 88  THR B C   1 
ATOM   2876 O  O   . THR B 1 88  ? 15.02400  23.89900  33.76600 1.000 25.75148 ? 88  THR B O   1 
ATOM   2877 C  CB  . THR B 1 88  ? 15.53400  27.26100  33.56400 1.000 24.03417 ? 88  THR B CB  1 
ATOM   2878 O  OG1 . THR B 1 88  ? 16.44800  28.25300  34.02800 1.000 25.78109 ? 88  THR B OG1 1 
ATOM   2879 C  CG2 . THR B 1 88  ? 14.39000  27.16600  34.54900 1.000 24.77875 ? 88  THR B CG2 1 
ATOM   2880 N  N   . VAL B 1 89  ? 14.74400  24.98400  31.81700 1.000 23.51050 ? 89  VAL B N   1 
ATOM   2881 C  CA  . VAL B 1 89  ? 13.63500  24.11700  31.45000 1.000 23.33016 ? 89  VAL B CA  1 
ATOM   2882 C  C   . VAL B 1 89  ? 14.12800  22.70200  31.19400 1.000 23.08777 ? 89  VAL B C   1 
ATOM   2883 O  O   . VAL B 1 89  ? 13.43400  21.73200  31.50900 1.000 21.74736 ? 89  VAL B O   1 
ATOM   2884 C  CB  . VAL B 1 89  ? 12.88100  24.69700  30.24300 1.000 22.92387 ? 89  VAL B CB  1 
ATOM   2885 C  CG1 . VAL B 1 89  ? 11.76000  23.76100  29.83200 1.000 23.63013 ? 89  VAL B CG1 1 
ATOM   2886 C  CG2 . VAL B 1 89  ? 12.33500  26.07900  30.57900 1.000 22.98994 ? 89  VAL B CG2 1 
ATOM   2887 N  N   . LEU B 1 90  ? 15.34800  22.56100  30.66900 1.000 22.30960 ? 90  LEU B N   1 
ATOM   2888 C  CA  . LEU B 1 90  ? 15.91400  21.24300  30.40600 1.000 22.44266 ? 90  LEU B CA  1 
ATOM   2889 C  C   . LEU B 1 90  ? 16.14300  20.44500  31.68700 1.000 22.27471 ? 90  LEU B C   1 
ATOM   2890 O  O   . LEU B 1 90  ? 16.10900  19.21300  31.65700 1.000 22.06504 ? 90  LEU B O   1 
ATOM   2891 C  CB  . LEU B 1 90  ? 17.22500  21.39400  29.62600 1.000 21.66477 ? 90  LEU B CB  1 
ATOM   2892 C  CG  . LEU B 1 90  ? 18.12100  20.18400  29.33500 1.000 21.60377 ? 90  LEU B CG  1 
ATOM   2893 C  CD1 . LEU B 1 90  ? 17.38500  19.09700  28.56600 1.000 21.43710 ? 90  LEU B CD1 1 
ATOM   2894 C  CD2 . LEU B 1 90  ? 19.33300  20.62800  28.55900 1.000 21.71707 ? 90  LEU B CD2 1 
ATOM   2895 N  N   . ILE B 1 91  ? 16.36800  21.10800  32.81500 1.000 22.44813 ? 91  ILE B N   1 
ATOM   2896 C  CA  . ILE B 1 91  ? 16.79500  20.42000  34.02600 1.000 23.28158 ? 91  ILE B CA  1 
ATOM   2897 C  C   . ILE B 1 91  ? 15.70800  20.43400  35.10100 1.000 23.72580 ? 91  ILE B C   1 
ATOM   2898 O  O   . ILE B 1 91  ? 16.00000  20.20100  36.26800 1.000 24.78526 ? 91  ILE B O   1 
ATOM   2899 C  CB  . ILE B 1 91  ? 18.11200  21.00000  34.56500 1.000 24.10334 ? 91  ILE B CB  1 
ATOM   2900 C  CG1 . ILE B 1 91  ? 17.96900  22.49800  34.81000 1.000 23.62023 ? 91  ILE B CG1 1 
ATOM   2901 C  CG2 . ILE B 1 91  ? 19.26200  20.71400  33.60700 1.000 23.84895 ? 91  ILE B CG2 1 
ATOM   2902 C  CD1 . ILE B 1 91  ? 19.11200  23.06700  35.55900 1.000 23.90968 ? 91  ILE B CD1 1 
ATOM   2903 N  N   . ASN B 1 92  ? 14.45900  20.69200  34.72000 1.000 24.57113 ? 92  ASN B N   1 
ATOM   2904 C  CA  . ASN B 1 92  ? 13.34100  20.72400  35.65100 1.000 25.03984 ? 92  ASN B CA  1 
ATOM   2905 C  C   . ASN B 1 92  ? 13.28800  19.43400  36.46500 1.000 24.59194 ? 92  ASN B C   1 
ATOM   2906 O  O   . ASN B 1 92  ? 13.19700  18.34700  35.88300 1.000 25.55680 ? 92  ASN B O   1 
ATOM   2907 C  CB  . ASN B 1 92  ? 12.02400  20.91800  34.91100 1.000 25.92625 ? 92  ASN B CB  1 
ATOM   2908 C  CG  . ASN B 1 92  ? 10.82700  20.90800  35.84400 1.000 26.86613 ? 92  ASN B CG  1 
ATOM   2909 O  OD1 . ASN B 1 92  ? 10.31500  19.85200  36.21500 1.000 26.50148 ? 92  ASN B OD1 1 
ATOM   2910 N  ND2 . ASN B 1 92  ? 10.37800  22.09300  36.22700 1.000 28.38834 ? 92  ASN B ND2 1 
ATOM   2911 N  N   . PRO B 1 93  ? 13.33500  19.51200  37.79200 1.000 24.65691 ? 93  PRO B N   1 
ATOM   2912 C  CA  . PRO B 1 93  ? 13.40500  18.28500  38.59000 1.000 25.14941 ? 93  PRO B CA  1 
ATOM   2913 C  C   . PRO B 1 93  ? 12.15900  17.42900  38.51000 1.000 26.25195 ? 93  PRO B C   1 
ATOM   2914 O  O   . PRO B 1 93  ? 12.25400  16.21700  38.73400 1.000 27.18181 ? 93  PRO B O   1 
ATOM   2915 C  CB  . PRO B 1 93  ? 13.63600  18.81100  40.01000 1.000 25.12625 ? 93  PRO B CB  1 
ATOM   2916 C  CG  . PRO B 1 93  ? 13.15000  20.21700  39.97400 1.000 25.46539 ? 93  PRO B CG  1 
ATOM   2917 C  CD  . PRO B 1 93  ? 13.47500  20.71900  38.61900 1.000 26.01933 ? 93  PRO B CD  1 
ATOM   2918 N  N   . VAL B 1 94  ? 10.99200  18.00900  38.21600 1.000 26.62937 ? 94  VAL B N   1 
ATOM   2919 C  CA  . VAL B 1 94  ? 9.78700   17.19600  38.06400 1.000 27.03422 ? 94  VAL B CA  1 
ATOM   2920 C  C   . VAL B 1 94  ? 9.89200   16.34200  36.80600 1.000 26.28813 ? 94  VAL B C   1 
ATOM   2921 O  O   . VAL B 1 94  ? 9.68900   15.12300  36.83500 1.000 27.08062 ? 94  VAL B O   1 
ATOM   2922 C  CB  . VAL B 1 94  ? 8.52800   18.08900  38.04400 1.000 27.91873 ? 94  VAL B CB  1 
ATOM   2923 C  CG1 . VAL B 1 94  ? 7.27600   17.25200  37.91100 1.000 28.12657 ? 94  VAL B CG1 1 
ATOM   2924 C  CG2 . VAL B 1 94  ? 8.44800   18.95300  39.28600 1.000 28.72027 ? 94  VAL B CG2 1 
ATOM   2925 N  N   . ILE B 1 95  ? 10.23600  16.97200  35.68700 1.000 26.09125 ? 95  ILE B N   1 
ATOM   2926 C  CA  . ILE B 1 95  ? 10.40200  16.24000  34.43700 1.000 25.10511 ? 95  ILE B CA  1 
ATOM   2927 C  C   . ILE B 1 95  ? 11.36700  15.07800  34.62400 1.000 25.49113 ? 95  ILE B C   1 
ATOM   2928 O  O   . ILE B 1 95  ? 11.08800  13.95000  34.21300 1.000 25.62521 ? 95  ILE B O   1 
ATOM   2929 C  CB  . ILE B 1 95  ? 10.87600  17.18600  33.32100 1.000 25.33174 ? 95  ILE B CB  1 
ATOM   2930 C  CG1 . ILE B 1 95  ? 9.92700   18.38500  33.16500 1.000 26.29942 ? 95  ILE B CG1 1 
ATOM   2931 C  CG2 . ILE B 1 95  ? 11.04600  16.41700  32.01800 1.000 24.85130 ? 95  ILE B CG2 1 
ATOM   2932 C  CD1 . ILE B 1 95  ? 8.46200   18.02300  32.91000 1.000 26.80621 ? 95  ILE B CD1 1 
ATOM   2933 N  N   . HIS B 1 96  ? 12.51600  15.33100  35.25000 1.000 25.93802 ? 96  HIS B N   1 
ATOM   2934 C  CA  . HIS B 1 96  ? 13.46600  14.24400  35.43600 1.000 25.74909 ? 96  HIS B CA  1 
ATOM   2935 C  C   . HIS B 1 96  ? 12.94500  13.21100  36.41300 1.000 26.26506 ? 96  HIS B C   1 
ATOM   2936 O  O   . HIS B 1 96  ? 13.25100  12.02200  36.27800 1.000 26.01073 ? 96  HIS B O   1 
ATOM   2937 C  CB  . HIS B 1 96  ? 14.81200  14.81300  35.84400 1.000 24.91688 ? 96  HIS B CB  1 
ATOM   2938 C  CG  . HIS B 1 96  ? 15.45700  15.53900  34.72100 1.000 23.75160 ? 96  HIS B CG  1 
ATOM   2939 N  ND1 . HIS B 1 96  ? 16.04700  14.88100  33.66800 1.000 24.03593 ? 96  HIS B ND1 1 
ATOM   2940 C  CD2 . HIS B 1 96  ? 15.48100  16.85100  34.40700 1.000 23.46103 ? 96  HIS B CD2 1 
ATOM   2941 C  CE1 . HIS B 1 96  ? 16.46300  15.76500  32.78100 1.000 22.94578 ? 96  HIS B CE1 1 
ATOM   2942 N  NE2 . HIS B 1 96  ? 16.12900  16.96700  33.20500 1.000 23.06792 ? 96  HIS B NE2 1 
ATOM   2943 N  N   . ALA B 1 97  ? 12.11300  13.62600  37.36200 1.000 26.46633 ? 97  ALA B N   1 
ATOM   2944 C  CA  . ALA B 1 97  ? 11.43500  12.63700  38.18000 1.000 26.57666 ? 97  ALA B CA  1 
ATOM   2945 C  C   . ALA B 1 97  ? 10.57000  11.74300  37.30800 1.000 26.75035 ? 97  ALA B C   1 
ATOM   2946 O  O   . ALA B 1 97  ? 10.54000  10.52300  37.49300 1.000 26.93422 ? 97  ALA B O   1 
ATOM   2947 C  CB  . ALA B 1 97  ? 10.60900  13.32200  39.26100 1.000 26.23469 ? 97  ALA B CB  1 
ATOM   2948 N  N   . ILE B 1 98  ? 9.90200   12.32500  36.31300 1.000 26.80651 ? 98  ILE B N   1 
ATOM   2949 C  CA  . ILE B 1 98  ? 9.01700   11.53200  35.46700 1.000 26.04978 ? 98  ILE B CA  1 
ATOM   2950 C  C   . ILE B 1 98  ? 9.82200   10.62000  34.54500 1.000 25.91822 ? 98  ILE B C   1 
ATOM   2951 O  O   . ILE B 1 98  ? 9.45400   9.45900   34.33200 1.000 25.77704 ? 98  ILE B O   1 
ATOM   2952 C  CB  . ILE B 1 98  ? 8.06600   12.45500  34.68400 1.000 25.77410 ? 98  ILE B CB  1 
ATOM   2953 C  CG1 . ILE B 1 98  ? 7.24000   13.30700  35.65600 1.000 27.64671 ? 98  ILE B CG1 1 
ATOM   2954 C  CG2 . ILE B 1 98  ? 7.13700   11.63400  33.82400 1.000 26.77098 ? 98  ILE B CG2 1 
ATOM   2955 C  CD1 . ILE B 1 98  ? 6.70200   14.60000  35.06300 1.000 27.78491 ? 98  ILE B CD1 1 
ATOM   2956 N  N   . CYS B 1 99  ? 10.94900  11.11500  34.01000 1.000 26.15460 ? 99  CYS B N   1 
ATOM   2957 C  CA  . CYS B 1 99  ? 11.75400  10.31500  33.08700 1.000 24.91253 ? 99  CYS B CA  1 
ATOM   2958 C  C   . CYS B 1 99  ? 12.40100  9.12100   33.78600 1.000 25.41888 ? 99  CYS B C   1 
ATOM   2959 O  O   . CYS B 1 99  ? 12.44400  8.02000   33.22800 1.000 25.67165 ? 99  CYS B O   1 
ATOM   2960 C  CB  . CYS B 1 99  ? 12.82400  11.18200  32.42400 1.000 24.44974 ? 99  CYS B CB  1 
ATOM   2961 S  SG  . CYS B 1 99  ? 12.24600  12.42700  31.25100 1.000 24.07785 ? 99  CYS B SG  1 
ATOM   2962 N  N   . GLU B 1 100 ? 12.90600  9.31700   35.00600 1.000 25.35126 ? 100 GLU B N   1 
ATOM   2963 C  CA  . GLU B 1 100 ? 13.56300  8.22500   35.71700 1.000 25.56583 ? 100 GLU B CA  1 
ATOM   2964 C  C   . GLU B 1 100 ? 12.59600  7.09000   36.03000 1.000 25.75431 ? 100 GLU B C   1 
ATOM   2965 O  O   . GLU B 1 100 ? 12.93600  5.91600   35.86500 1.000 25.76878 ? 100 GLU B O   1 
ATOM   2966 C  CB  . GLU B 1 100 ? 14.20200  8.74700   37.00000 1.000 26.08612 ? 100 GLU B CB  1 
ATOM   2967 C  CG  . GLU B 1 100 ? 15.65300  9.11300   36.84200 1.000 27.99365 ? 100 GLU B CG  1 
ATOM   2968 C  CD  . GLU B 1 100 ? 16.19100  9.84800   38.05200 1.000 32.25311 ? 100 GLU B CD  1 
ATOM   2969 O  OE1 . GLU B 1 100 ? 15.46000  9.93100   39.06700 1.000 33.42263 ? 100 GLU B OE1 1 
ATOM   2970 O  OE2 . GLU B 1 100 ? 17.33400  10.35500  37.98900 1.000 34.70932 ? 100 GLU B OE2 1 
ATOM   2971 N  N   . ALA B 1 101 ? 11.39500  7.41500   36.49700 1.000 26.62049 ? 101 ALA B N   1 
ATOM   2972 C  CA  . ALA B 1 101 ? 10.38900  6.38000   36.70000 1.000 28.91527 ? 101 ALA B CA  1 
ATOM   2973 C  C   . ALA B 1 101 ? 9.92700   5.79800   35.37300 1.000 28.38861 ? 101 ALA B C   1 
ATOM   2974 O  O   . ALA B 1 101 ? 9.69500   4.59200   35.26500 1.000 31.22968 ? 101 ALA B O   1 
ATOM   2975 C  CB  . ALA B 1 101 ? 9.20200   6.94800   37.47600 1.000 29.75346 ? 101 ALA B CB  1 
ATOM   2976 N  N   . TYR B 1 102 ? 9.79300   6.63600   34.34900 1.000 27.48605 ? 102 TYR B N   1 
ATOM   2977 C  CA  . TYR B 1 102 ? 9.30700   6.15200   33.06100 1.000 26.76065 ? 102 TYR B CA  1 
ATOM   2978 C  C   . TYR B 1 102 ? 10.33300  5.25300   32.38300 1.000 27.27651 ? 102 TYR B C   1 
ATOM   2979 O  O   . TYR B 1 102 ? 9.98100   4.19200   31.85800 1.000 28.24931 ? 102 TYR B O   1 
ATOM   2980 C  CB  . TYR B 1 102 ? 8.94300   7.34100   32.17000 1.000 26.41934 ? 102 TYR B CB  1 
ATOM   2981 C  CG  . TYR B 1 102 ? 8.50700   7.00800   30.74900 1.000 25.30945 ? 102 TYR B CG  1 
ATOM   2982 C  CD1 . TYR B 1 102 ? 7.18800   6.65400   30.48200 1.000 24.75501 ? 102 TYR B CD1 1 
ATOM   2983 C  CD2 . TYR B 1 102 ? 9.42600   7.07700   29.70200 1.000 24.87813 ? 102 TYR B CD2 1 
ATOM   2984 C  CE1 . TYR B 1 102 ? 6.81900   6.36600   29.19300 1.000 25.17034 ? 102 TYR B CE1 1 
ATOM   2985 C  CE2 . TYR B 1 102 ? 9.01900   6.77900   28.42600 1.000 24.05927 ? 102 TYR B CE2 1 
ATOM   2986 C  CZ  . TYR B 1 102 ? 7.71200   6.42300   28.13700 1.000 24.50188 ? 102 TYR B CZ  1 
ATOM   2987 O  OH  . TYR B 1 102 ? 7.33200   6.14400   26.87600 1.000 24.48577 ? 102 TYR B OH  1 
ATOM   2988 N  N   . PHE B 1 103 ? 11.60600  5.64200   32.40700 1.000 26.57305 ? 103 PHE B N   1 
ATOM   2989 C  CA  . PHE B 1 103 ? 12.66400  4.91400   31.71900 1.000 27.04533 ? 103 PHE B CA  1 
ATOM   2990 C  C   . PHE B 1 103 ? 13.34600  3.85200   32.59000 1.000 27.84099 ? 103 PHE B C   1 
ATOM   2991 O  O   . PHE B 1 103 ? 14.41300  3.36200   32.21200 1.000 28.60555 ? 103 PHE B O   1 
ATOM   2992 C  CB  . PHE B 1 103 ? 13.73100  5.89200   31.21000 1.000 25.64659 ? 103 PHE B CB  1 
ATOM   2993 C  CG  . PHE B 1 103 ? 13.28200  6.78800   30.07800 1.000 24.59216 ? 103 PHE B CG  1 
ATOM   2994 C  CD1 . PHE B 1 103 ? 12.97800  6.26200   28.83600 1.000 24.02567 ? 103 PHE B CD1 1 
ATOM   2995 C  CD2 . PHE B 1 103 ? 13.22900  8.16800   30.24800 1.000 23.56573 ? 103 PHE B CD2 1 
ATOM   2996 C  CE1 . PHE B 1 103 ? 12.59000  7.09200   27.79100 1.000 22.98113 ? 103 PHE B CE1 1 
ATOM   2997 C  CE2 . PHE B 1 103 ? 12.85100  8.99800   29.21100 1.000 23.11154 ? 103 PHE B CE2 1 
ATOM   2998 C  CZ  . PHE B 1 103 ? 12.53100  8.45600   27.98100 1.000 22.32428 ? 103 PHE B CZ  1 
ATOM   2999 N  N   . GLN B 1 104 ? 12.76100  3.48200   33.73600 1.000 27.82568 ? 104 GLN B N   1 
ATOM   3000 C  CA  . GLN B 1 104 ? 13.45600  2.63100   34.70500 1.000 27.40959 ? 104 GLN B CA  1 
ATOM   3001 C  C   . GLN B 1 104 ? 13.85900  1.28300   34.11700 1.000 27.89837 ? 104 GLN B C   1 
ATOM   3002 O  O   . GLN B 1 104 ? 14.90100  0.73800   34.48900 1.000 28.32623 ? 104 GLN B O   1 
ATOM   3003 C  CB  . GLN B 1 104 ? 12.57800  2.41700   35.93500 1.000 28.90310 ? 104 GLN B CB  1 
ATOM   3004 C  CG  . GLN B 1 104 ? 11.20000  1.94600   35.56500 1.000 30.76431 ? 104 GLN B CG  1 
ATOM   3005 C  CD  . GLN B 1 104 ? 10.34200  1.58400   36.75100 1.000 37.06747 ? 104 GLN B CD  1 
ATOM   3006 O  OE1 . GLN B 1 104 ? 10.84800  1.28500   37.83100 1.000 41.96616 ? 104 GLN B OE1 1 
ATOM   3007 N  NE2 . GLN B 1 104 ? 9.02500   1.59500   36.55200 1.000 37.46992 ? 104 GLN B NE2 1 
ATOM   3008 N  N   . ARG B 1 105 ? 13.06200  0.72900   33.20300 1.000 29.37794 ? 105 ARG B N   1 
ATOM   3009 C  CA  . ARG B 1 105 ? 13.38100  -0.56600  32.60600 1.000 29.48380 ? 105 ARG B CA  1 
ATOM   3010 C  C   . ARG B 1 105 ? 14.40400  -0.47500  31.48500 1.000 28.43058 ? 105 ARG B C   1 
ATOM   3011 O  O   . ARG B 1 105 ? 15.01700  -1.48600  31.13400 1.000 29.56391 ? 105 ARG B O   1 
ATOM   3012 C  CB  . ARG B 1 105 ? 12.11900  -1.23700  32.06100 1.000 29.38224 ? 105 ARG B CB  1 
ATOM   3013 C  CG  . ARG B 1 105 ? 11.21200  -1.83200  33.12800 1.000 29.86718 ? 105 ARG B CG  1 
ATOM   3014 C  CD  . ARG B 1 105 ? 10.26100  -2.85300  32.52100 1.000 31.50917 ? 105 ARG B CD  1 
ATOM   3015 N  NE  . ARG B 1 105 ? 9.35100   -2.23100  31.57000 1.000 31.03754 ? 105 ARG B NE  1 
ATOM   3016 C  CZ  . ARG B 1 105 ? 8.89200   -2.82400  30.47900 1.000 31.77116 ? 105 ARG B CZ  1 
ATOM   3017 N  NH1 . ARG B 1 105 ? 9.24300   -4.06100  30.16500 1.000 33.06667 ? 105 ARG B NH1 1 
ATOM   3018 N  NH2 . ARG B 1 105 ? 8.06900   -2.15500  29.67900 1.000 34.15521 ? 105 ARG B NH2 1 
ATOM   3019 N  N   . THR B 1 106 ? 14.59500  0.69300   30.89500 1.000 27.35039 ? 106 THR B N   1 
ATOM   3020 C  CA  . THR B 1 106 ? 15.52600  0.80300   29.79000 1.000 26.33067 ? 106 THR B CA  1 
ATOM   3021 C  C   . THR B 1 106 ? 16.82200  1.50900   30.15700 1.000 26.79760 ? 106 THR B C   1 
ATOM   3022 O  O   . THR B 1 106 ? 17.80900  1.35800   29.43200 1.000 25.91546 ? 106 THR B O   1 
ATOM   3023 C  CB  . THR B 1 106 ? 14.85400  1.52200   28.61600 1.000 26.44997 ? 106 THR B CB  1 
ATOM   3024 O  OG1 . THR B 1 106 ? 15.77800  1.64100   27.52700 1.000 27.79683 ? 106 THR B OG1 1 
ATOM   3025 C  CG2 . THR B 1 106 ? 14.38100  2.88700   29.04200 1.000 26.94663 ? 106 THR B CG2 1 
ATOM   3026 N  N   . GLY B 1 107 ? 16.85100  2.24900   31.26700 1.000 27.41407 ? 107 GLY B N   1 
ATOM   3027 C  CA  . GLY B 1 107 ? 18.06400  2.90700   31.70800 1.000 27.88731 ? 107 GLY B CA  1 
ATOM   3028 C  C   . GLY B 1 107 ? 18.11100  4.40200   31.45800 1.000 27.07790 ? 107 GLY B C   1 
ATOM   3029 O  O   . GLY B 1 107 ? 17.09100  5.09600   31.56300 1.000 25.49630 ? 107 GLY B O   1 
ATOM   3030 N  N   . ASP B 1 108 ? 19.30700  4.90200   31.13400 1.000 24.88501 ? 108 ASP B N   1 
ATOM   3031 C  CA  . ASP B 1 108 ? 19.54500  6.33100   30.98900 1.000 23.16457 ? 108 ASP B CA  1 
ATOM   3032 C  C   . ASP B 1 108 ? 18.86900  6.88100   29.74100 1.000 20.94980 ? 108 ASP B C   1 
ATOM   3033 O  O   . ASP B 1 108 ? 18.65100  6.17900   28.75500 1.000 21.67070 ? 108 ASP B O   1 
ATOM   3034 C  CB  . ASP B 1 108 ? 21.04300  6.63200   30.91700 1.000 22.60430 ? 108 ASP B CB  1 
ATOM   3035 C  CG  . ASP B 1 108 ? 21.65600  6.86900   32.26800 1.000 22.31178 ? 108 ASP B CG  1 
ATOM   3036 O  OD1 . ASP B 1 108 ? 20.94000  6.77800   33.27900 1.000 23.67773 ? 108 ASP B OD1 1 
ATOM   3037 O  OD2 . ASP B 1 108 ? 22.86300  7.15200   32.31800 1.000 23.77753 ? 108 ASP B OD2 1 
ATOM   3038 N  N   . TYR B 1 109 ? 18.57800  8.17200   29.78900 1.000 20.19011 ? 109 TYR B N   1 
ATOM   3039 C  CA  . TYR B 1 109 ? 17.88400  8.88000   28.72600 1.000 20.22524 ? 109 TYR B CA  1 
ATOM   3040 C  C   . TYR B 1 109 ? 18.63400  10.17700  28.45300 1.000 20.63750 ? 109 TYR B C   1 
ATOM   3041 O  O   . TYR B 1 109 ? 19.43200  10.63500  29.27500 1.000 20.12340 ? 109 TYR B O   1 
ATOM   3042 C  CB  . TYR B 1 109 ? 16.41700  9.18200   29.12000 1.000 20.41202 ? 109 TYR B CB  1 
ATOM   3043 C  CG  . TYR B 1 109 ? 16.33100  9.94200   30.43500 1.000 22.18617 ? 109 TYR B CG  1 
ATOM   3044 C  CD1 . TYR B 1 109 ? 16.33600  9.24600   31.64300 1.000 22.60228 ? 109 TYR B CD1 1 
ATOM   3045 C  CD2 . TYR B 1 109 ? 16.28800  11.33500  30.44800 1.000 22.67004 ? 109 TYR B CD2 1 
ATOM   3046 C  CE1 . TYR B 1 109 ? 16.28400  9.94500   32.82300 1.000 23.42930 ? 109 TYR B CE1 1 
ATOM   3047 C  CE2 . TYR B 1 109 ? 16.23800  11.99700  31.65100 1.000 22.35000 ? 109 TYR B CE2 1 
ATOM   3048 C  CZ  . TYR B 1 109 ? 16.23800  11.33000  32.86500 1.000 23.01528 ? 109 TYR B CZ  1 
ATOM   3049 O  OH  . TYR B 1 109 ? 16.19100  11.99500  34.03800 1.000 24.92415 ? 109 TYR B OH  1 
ATOM   3050 N  N   . TRP B 1 110 ? 18.39600  10.75800  27.27700 1.000 19.72213 ? 110 TRP B N   1 
ATOM   3051 C  CA  . TRP B 1 110 ? 18.94500  12.06700  26.97000 1.000 19.64242 ? 110 TRP B CA  1 
ATOM   3052 C  C   . TRP B 1 110 ? 18.01500  12.77700  26.00000 1.000 19.51994 ? 110 TRP B C   1 
ATOM   3053 O  O   . TRP B 1 110 ? 17.00800  12.22600  25.55800 1.000 19.55608 ? 110 TRP B O   1 
ATOM   3054 C  CB  . TRP B 1 110 ? 20.38500  11.97700  26.44700 1.000 19.12742 ? 110 TRP B CB  1 
ATOM   3055 C  CG  . TRP B 1 110 ? 20.65700  11.06600  25.26700 1.000 19.33956 ? 110 TRP B CG  1 
ATOM   3056 C  CD1 . TRP B 1 110 ? 19.74600  10.45600  24.43400 1.000 19.17216 ? 110 TRP B CD1 1 
ATOM   3057 C  CD2 . TRP B 1 110 ? 21.95100  10.66300  24.80700 1.000 19.30356 ? 110 TRP B CD2 1 
ATOM   3058 N  NE1 . TRP B 1 110 ? 20.40600  9.71300   23.47700 1.000 18.95070 ? 110 TRP B NE1 1 
ATOM   3059 C  CE2 . TRP B 1 110 ? 21.75900  9.82000   23.69100 1.000 19.22321 ? 110 TRP B CE2 1 
ATOM   3060 C  CE3 . TRP B 1 110 ? 23.26100  10.93700  25.23500 1.000 19.85764 ? 110 TRP B CE3 1 
ATOM   3061 C  CZ2 . TRP B 1 110 ? 22.83200  9.23900   23.00000 1.000 20.22803 ? 110 TRP B CZ2 1 
ATOM   3062 C  CZ3 . TRP B 1 110 ? 24.32600  10.36500  24.54600 1.000 19.53241 ? 110 TRP B CZ3 1 
ATOM   3063 C  CH2 . TRP B 1 110 ? 24.10500  9.53100   23.43500 1.000 19.89653 ? 110 TRP B CH2 1 
ATOM   3064 N  N   . LEU B 1 111 ? 18.34600  14.02900  25.70300 1.000 19.31793 ? 111 LEU B N   1 
ATOM   3065 C  CA  . LEU B 1 111 ? 17.53500  14.85800  24.82700 1.000 19.41603 ? 111 LEU B CA  1 
ATOM   3066 C  C   . LEU B 1 111 ? 17.86000  14.52000  23.38900 1.000 19.99820 ? 111 LEU B C   1 
ATOM   3067 O  O   . LEU B 1 111 ? 18.99500  14.72100  22.94800 1.000 19.88070 ? 111 LEU B O   1 
ATOM   3068 C  CB  . LEU B 1 111 ? 17.80100  16.33700  25.08700 1.000 19.01565 ? 111 LEU B CB  1 
ATOM   3069 C  CG  . LEU B 1 111 ? 16.92200  17.26500  24.26000 1.000 18.76128 ? 111 LEU B CG  1 
ATOM   3070 C  CD1 . LEU B 1 111 ? 15.49800  17.05300  24.68200 1.000 19.40004 ? 111 LEU B CD1 1 
ATOM   3071 C  CD2 . LEU B 1 111 ? 17.33300  18.70800  24.45300 1.000 18.55740 ? 111 LEU B CD2 1 
ATOM   3072 N  N   . SER B 1 112 ? 16.87300  14.00600  22.65400 1.000 19.62860 ? 112 SER B N   1 
ATOM   3073 C  CA  . SER B 1 112 ? 17.06800  13.73900  21.23400 1.000 19.60688 ? 112 SER B CA  1 
ATOM   3074 C  C   . SER B 1 112 ? 16.76200  14.95700  20.36300 1.000 20.22722 ? 112 SER B C   1 
ATOM   3075 O  O   . SER B 1 112 ? 17.40000  15.13800  19.31700 1.000 20.05510 ? 112 SER B O   1 
ATOM   3076 C  CB  . SER B 1 112 ? 16.21000  12.55300  20.79600 1.000 19.08722 ? 112 SER B CB  1 
ATOM   3077 O  OG  . SER B 1 112 ? 16.44300  12.25400  19.44100 1.000 18.88767 ? 112 SER B OG  1 
ATOM   3078 N  N   . ALA B 1 113 ? 15.82800  15.81300  20.78100 1.000 19.45828 ? 113 ALA B N   1 
ATOM   3079 C  CA  . ALA B 1 113 ? 15.52800  17.03600  20.05700 1.000 20.02677 ? 113 ALA B CA  1 
ATOM   3080 C  C   . ALA B 1 113 ? 14.74600  17.96600  20.96900 1.000 20.99524 ? 113 ALA B C   1 
ATOM   3081 O  O   . ALA B 1 113 ? 14.04400  17.51500  21.87200 1.000 21.19457 ? 113 ALA B O   1 
ATOM   3082 C  CB  . ALA B 1 113 ? 14.72600  16.75000  18.78300 1.000 20.82928 ? 113 ALA B CB  1 
ATOM   3083 N  N   . ALA B 1 114 ? 14.89200  19.26800  20.73500 1.000 21.45603 ? 114 ALA B N   1 
ATOM   3084 C  CA  . ALA B 1 114 ? 13.98100  20.26400  21.29200 1.000 22.01316 ? 114 ALA B CA  1 
ATOM   3085 C  C   . ALA B 1 114 ? 13.97400  21.45900  20.35600 1.000 21.89207 ? 114 ALA B C   1 
ATOM   3086 O  O   . ALA B 1 114 ? 15.02200  22.07200  20.14300 1.000 22.09656 ? 114 ALA B O   1 
ATOM   3087 C  CB  . ALA B 1 114 ? 14.38400  20.68400  22.70200 1.000 21.45345 ? 114 ALA B CB  1 
ATOM   3088 N  N   . PHE B 1 115 ? 12.80100  21.77300  19.79800 1.000 23.32807 ? 115 PHE B N   1 
ATOM   3089 C  CA  . PHE B 1 115 ? 12.63300  22.79000  18.76500 1.000 23.82452 ? 115 PHE B CA  1 
ATOM   3090 C  C   . PHE B 1 115 ? 11.31400  23.51500  18.98900 1.000 25.38681 ? 115 PHE B C   1 
ATOM   3091 O  O   . PHE B 1 115 ? 10.49600  23.11500  19.81800 1.000 26.07956 ? 115 PHE B O   1 
ATOM   3092 C  CB  . PHE B 1 115 ? 12.66700  22.18800  17.35400 1.000 23.47733 ? 115 PHE B CB  1 
ATOM   3093 C  CG  . PHE B 1 115 ? 11.62200  21.13100  17.11300 1.000 25.36201 ? 115 PHE B CG  1 
ATOM   3094 C  CD1 . PHE B 1 115 ? 11.87000  19.80200  17.43600 1.000 25.58512 ? 115 PHE B CD1 1 
ATOM   3095 C  CD2 . PHE B 1 115 ? 10.39500  21.45800  16.55400 1.000 25.52982 ? 115 PHE B CD2 1 
ATOM   3096 C  CE1 . PHE B 1 115 ? 10.90700  18.82200  17.22200 1.000 24.87427 ? 115 PHE B CE1 1 
ATOM   3097 C  CE2 . PHE B 1 115 ? 9.43000   20.48300  16.33100 1.000 25.96002 ? 115 PHE B CE2 1 
ATOM   3098 C  CZ  . PHE B 1 115 ? 9.68700   19.16800  16.67000 1.000 26.34544 ? 115 PHE B CZ  1 
ATOM   3099 N  N   . LEU B 1 116 ? 11.09300  24.57800  18.22500 1.000 26.86710 ? 116 LEU B N   1 
ATOM   3100 C  CA  . LEU B 1 116 ? 9.91500   25.41800  18.38700 1.000 26.41236 ? 116 LEU B CA  1 
ATOM   3101 C  C   . LEU B 1 116 ? 9.05900   25.37300  17.12900 1.000 28.11497 ? 116 LEU B C   1 
ATOM   3102 O  O   . LEU B 1 116 ? 9.57700   25.46700  16.01400 1.000 30.08850 ? 116 LEU B O   1 
ATOM   3103 C  CB  . LEU B 1 116 ? 10.33500  26.85600  18.69900 1.000 26.74598 ? 116 LEU B CB  1 
ATOM   3104 C  CG  . LEU B 1 116 ? 9.35000   28.00600  18.94300 1.000 27.37993 ? 116 LEU B CG  1 
ATOM   3105 C  CD1 . LEU B 1 116 ? 9.00100   28.69700  17.65300 1.000 28.75392 ? 116 LEU B CD1 1 
ATOM   3106 C  CD2 . LEU B 1 116 ? 8.09100   27.57000  19.67700 1.000 28.03598 ? 116 LEU B CD2 1 
ATOM   3107 N  N   . ARG B 1 117 ? 7.74900   25.22400  17.31500 1.000 28.70401 ? 117 ARG B N   1 
ATOM   3108 C  CA  . ARG B 1 117 ? 6.75500   25.42200  16.26300 1.000 31.19743 ? 117 ARG B CA  1 
ATOM   3109 C  C   . ARG B 1 117 ? 5.88100   26.62200  16.61200 1.000 30.29348 ? 117 ARG B C   1 
ATOM   3110 O  O   . ARG B 1 117 ? 5.36800   26.71500  17.73200 1.000 30.09528 ? 117 ARG B O   1 
ATOM   3111 C  CB  . ARG B 1 117 ? 5.87900   24.18000  16.08100 1.000 32.65988 ? 117 ARG B CB  1 
ATOM   3112 C  CG  . ARG B 1 117 ? 5.05000   24.19600  14.80700 1.000 34.48959 ? 117 ARG B CG  1 
ATOM   3113 C  CD  . ARG B 1 117 ? 5.94000   24.54300  13.61200 1.000 38.04375 ? 117 ARG B CD  1 
ATOM   3114 N  NE  . ARG B 1 117 ? 5.54200   23.89600  12.36800 1.000 40.03175 ? 117 ARG B NE  1 
ATOM   3115 C  CZ  . ARG B 1 117 ? 4.95900   24.51100  11.35000 1.000 41.94799 ? 117 ARG B CZ  1 
ATOM   3116 N  NH1 . ARG B 1 117 ? 4.67400   25.80500  11.39100 1.000 44.26194 ? 117 ARG B NH1 1 
ATOM   3117 N  NH2 . ARG B 1 117 ? 4.66100   23.81100  10.25900 1.000 40.07899 ? 117 ARG B NH2 1 
ATOM   3118 N  N   . GLU B 1 118 ? 5.72300   27.54100  15.66100 1.000 34.23720 ? 118 GLU B N   1 
ATOM   3119 C  CA  . GLU B 1 118 ? 4.83800   28.68900  15.80700 1.000 34.97286 ? 118 GLU B CA  1 
ATOM   3120 C  C   . GLU B 1 118 ? 3.73900   28.57300  14.76500 1.000 36.19678 ? 118 GLU B C   1 
ATOM   3121 O  O   . GLU B 1 118 ? 4.02300   28.36800  13.57900 1.000 38.41369 ? 118 GLU B O   1 
ATOM   3122 C  CB  . GLU B 1 118 ? 5.59700   30.01200  15.64900 1.000 35.74254 ? 118 GLU B CB  1 
ATOM   3123 C  CG  . GLU B 1 118 ? 4.73800   31.24000  15.90400 1.000 36.56259 ? 118 GLU B CG  1 
ATOM   3124 C  CD  . GLU B 1 118 ? 5.46200   32.56000  15.66800 1.000 38.25601 ? 118 GLU B CD  1 
ATOM   3125 O  OE1 . GLU B 1 118 ? 5.66700   32.94700  14.49900 1.000 39.54298 ? 118 GLU B OE1 1 
ATOM   3126 O  OE2 . GLU B 1 118 ? 5.82000   33.22300  16.65900 1.000 37.44153 ? 118 GLU B OE2 1 
ATOM   3127 N  N   . ILE B 1 119 ? 2.48800   28.68400  15.20400 1.000 37.32230 ? 119 ILE B N   1 
ATOM   3128 C  CA  . ILE B 1 119 ? 1.33400   28.45200  14.34200 1.000 38.68174 ? 119 ILE B CA  1 
ATOM   3129 C  C   . ILE B 1 119 ? 0.49300   29.71900  14.33200 1.000 41.20962 ? 119 ILE B C   1 
ATOM   3130 O  O   . ILE B 1 119 ? -0.20700  30.01500  15.31000 1.000 41.14568 ? 119 ILE B O   1 
ATOM   3131 C  CB  . ILE B 1 119 ? 0.50300   27.25000  14.80000 1.000 39.58359 ? 119 ILE B CB  1 
ATOM   3132 C  CG1 . ILE B 1 119 ? 1.38000   26.00000  14.92100 1.000 37.72271 ? 119 ILE B CG1 1 
ATOM   3133 C  CG2 . ILE B 1 119 ? -0.63100  27.01100  13.84400 1.000 42.08999 ? 119 ILE B CG2 1 
ATOM   3134 C  CD1 . ILE B 1 119 ? 1.88000   25.73900  16.33300 1.000 35.67437 ? 119 ILE B CD1 1 
ATOM   3135 N  N   . GLU B 1 120 ? 0.55500   30.46100  13.22700 1.000 37.96745 ? 120 GLU B N   1 
ATOM   3136 C  CA  . GLU B 1 120 ? -0.16000  31.71600  13.06400 1.000 38.02034 ? 120 GLU B CA  1 
ATOM   3137 C  C   . GLU B 1 120 ? -1.63400  31.45300  12.76500 1.000 40.82565 ? 120 GLU B C   1 
ATOM   3138 O  O   . GLU B 1 120 ? -2.02600  30.34600  12.38200 1.000 40.43875 ? 120 GLU B O   1 
ATOM   3139 C  CB  . GLU B 1 120 ? 0.46700   32.54500  11.93800 1.000 37.31243 ? 120 GLU B CB  1 
ATOM   3140 C  CG  . GLU B 1 120 ? 2.00700   32.67200  11.99100 1.000 40.76989 ? 120 GLU B CG  1 
ATOM   3141 C  CD  . GLU B 1 120 ? 2.75000   31.57000  11.22800 1.000 42.07791 ? 120 GLU B CD  1 
ATOM   3142 O  OE1 . GLU B 1 120 ? 2.76200   30.40600  11.69400 1.000 40.87236 ? 120 GLU B OE1 1 
ATOM   3143 O  OE2 . GLU B 1 120 ? 3.33700   31.87400  10.16500 1.000 43.98477 ? 120 GLU B OE2 1 
ATOM   3144 N  N   . SER B 1 121 ? -2.45500  32.48900  12.94700 1.000 45.88499 ? 121 SER B N   1 
ATOM   3145 C  CA  . SER B 1 121 ? -3.87100  32.38300  12.61200 1.000 48.75442 ? 121 SER B CA  1 
ATOM   3146 C  C   . SER B 1 121 ? -4.03400  32.04200  11.13700 1.000 44.37727 ? 121 SER B C   1 
ATOM   3147 O  O   . SER B 1 121 ? -3.34000  32.58200  10.27600 1.000 42.56033 ? 121 SER B O   1 
ATOM   3148 C  CB  . SER B 1 121 ? -4.60400  33.68800  12.93800 1.000 56.10499 ? 121 SER B CB  1 
ATOM   3149 O  OG  . SER B 1 121 ? -4.90700  33.80200  14.31900 1.000 58.91782 ? 121 SER B OG  1 
ATOM   3150 N  N   . GLY B 1 122 ? -4.95000  31.13100  10.84400 1.000 44.99896 ? 122 GLY B N   1 
ATOM   3151 C  CA  . GLY B 1 122 ? -5.10900  30.63500  9.49600  1.000 40.99213 ? 122 GLY B CA  1 
ATOM   3152 C  C   . GLY B 1 122 ? -4.28400  29.41400  9.16100  1.000 39.79389 ? 122 GLY B C   1 
ATOM   3153 O  O   . GLY B 1 122 ? -4.33100  28.95400  8.01500  1.000 37.57494 ? 122 GLY B O   1 
ATOM   3154 N  N   . MET B 1 123 ? -3.53600  28.87100  10.11600 1.000 40.74085 ? 123 MET B N   1 
ATOM   3155 C  CA  . MET B 1 123 ? -2.81900  27.68000  9.69800  1.000 39.24683 ? 123 MET B CA  1 
ATOM   3156 C  C   . MET B 1 123 ? -3.67200  26.43600  9.91400  1.000 40.89372 ? 123 MET B C   1 
ATOM   3157 O  O   . MET B 1 123 ? -4.47100  26.37600  10.85600 1.000 42.39048 ? 123 MET B O   1 
ATOM   3158 C  CB  . MET B 1 123 ? -1.51000  27.54300  10.46700 1.000 40.44156 ? 123 MET B CB  1 
ATOM   3159 C  CG  . MET B 1 123 ? -0.45900  28.61900  10.15500 1.000 40.27785 ? 123 MET B CG  1 
ATOM   3160 S  SD  . MET B 1 123 ? 0.11100   28.67900  8.43600  1.000 40.19089 ? 123 MET B SD  1 
ATOM   3161 C  CE  . MET B 1 123 ? -0.68700  30.17200  7.83800  1.000 34.23781 ? 123 MET B CE  1 
ATOM   3162 N  N   . PRO B 1 124 ? -3.52400  25.44700  9.03600  1.000 37.08096 ? 124 PRO B N   1 
ATOM   3163 C  CA  . PRO B 1 124 ? -4.32000  24.22200  9.15900  1.000 36.92608 ? 124 PRO B CA  1 
ATOM   3164 C  C   . PRO B 1 124 ? -3.82000  23.33800  10.28800 1.000 38.54677 ? 124 PRO B C   1 
ATOM   3165 O  O   . PRO B 1 124 ? -2.67900  23.44200  10.73900 1.000 38.16110 ? 124 PRO B O   1 
ATOM   3166 C  CB  . PRO B 1 124 ? -4.12600  23.53400  7.80200  1.000 36.83842 ? 124 PRO B CB  1 
ATOM   3167 C  CG  . PRO B 1 124 ? -2.82300  24.03800  7.31300  1.000 36.50796 ? 124 PRO B CG  1 
ATOM   3168 C  CD  . PRO B 1 124 ? -2.74100  25.46800  7.78900  1.000 37.06441 ? 124 PRO B CD  1 
ATOM   3169 N  N   . ALA B 1 125 ? -4.70000  22.44500  10.73800 1.000 40.43951 ? 125 ALA B N   1 
ATOM   3170 C  CA  . ALA B 1 125 ? -4.30500  21.44900  11.72200 1.000 38.24779 ? 125 ALA B CA  1 
ATOM   3171 C  C   . ALA B 1 125 ? -3.29000  20.48200  11.11900 1.000 35.55965 ? 125 ALA B C   1 
ATOM   3172 O  O   . ALA B 1 125 ? -3.17300  20.33500  9.89800  1.000 33.48056 ? 125 ALA B O   1 
ATOM   3173 C  CB  . ALA B 1 125 ? -5.52300  20.67800  12.24000 1.000 37.76002 ? 125 ALA B CB  1 
ATOM   3174 N  N   . GLN B 1 126 ? -2.55000  19.82200  11.99900 1.000 33.39287 ? 126 GLN B N   1 
ATOM   3175 C  CA  . GLN B 1 126 ? -1.49700  18.83100  11.84600 1.000 31.36711 ? 126 GLN B CA  1 
ATOM   3176 C  C   . GLN B 1 126 ? -2.09600  17.42900  11.81000 1.000 31.06530 ? 126 GLN B C   1 
ATOM   3177 O  O   . GLN B 1 126 ? -3.03600  17.14300  12.55200 1.000 33.60702 ? 126 GLN B O   1 
ATOM   3178 C  CB  . GLN B 1 126 ? -0.50400  18.94000  12.99700 1.000 31.15498 ? 126 GLN B CB  1 
ATOM   3179 C  CG  . GLN B 1 126 ? 0.66300   17.99500  12.91900 1.000 31.02591 ? 126 GLN B CG  1 
ATOM   3180 C  CD  . GLN B 1 126 ? 1.71300   18.30200  13.94500 1.000 29.30168 ? 126 GLN B CD  1 
ATOM   3181 O  OE1 . GLN B 1 126 ? 1.47500   18.20500  15.14900 1.000 28.72396 ? 126 GLN B OE1 1 
ATOM   3182 N  NE2 . GLN B 1 126 ? 2.89300   18.67700  13.47500 1.000 31.47157 ? 126 GLN B NE2 1 
ATOM   3183 N  N   . PRO B 1 127 ? -1.60100  16.53500  10.96000 1.000 29.70293 ? 127 PRO B N   1 
ATOM   3184 C  CA  . PRO B 1 127 ? -2.16800  15.17600  10.90400 1.000 30.91336 ? 127 PRO B CA  1 
ATOM   3185 C  C   . PRO B 1 127 ? -1.85800  14.34200  12.14400 1.000 28.39306 ? 127 PRO B C   1 
ATOM   3186 O  O   . PRO B 1 127 ? -0.84500  14.53500  12.82100 1.000 28.42080 ? 127 PRO B O   1 
ATOM   3187 C  CB  . PRO B 1 127 ? -1.50900  14.56300  9.66000  1.000 29.30489 ? 127 PRO B CB  1 
ATOM   3188 C  CG  . PRO B 1 127 ? -0.99900  15.71900  8.87900  1.000 30.43534 ? 127 PRO B CG  1 
ATOM   3189 C  CD  . PRO B 1 127 ? -0.65200  16.78600  9.86600  1.000 29.99261 ? 127 PRO B CD  1 
ATOM   3190 N  N   . PHE B 1 128 ? -2.75400  13.39100  12.42200 1.000 29.40429 ? 128 PHE B N   1 
ATOM   3191 C  CA  . PHE B 1 128 ? -2.55000  12.45100  13.51800 1.000 29.45531 ? 128 PHE B CA  1 
ATOM   3192 C  C   . PHE B 1 128 ? -1.26000  11.66800  13.32900 1.000 28.86748 ? 128 PHE B C   1 
ATOM   3193 O  O   . PHE B 1 128 ? -0.93600  11.22500  12.22600 1.000 29.41665 ? 128 PHE B O   1 
ATOM   3194 C  CB  . PHE B 1 128 ? -3.72400  11.47700  13.62500 1.000 29.14039 ? 128 PHE B CB  1 
ATOM   3195 C  CG  . PHE B 1 128 ? -4.86200  11.99200  14.45000 1.000 29.44998 ? 128 PHE B CG  1 
ATOM   3196 C  CD1 . PHE B 1 128 ? -4.66500  12.35000  15.77600 1.000 28.91102 ? 128 PHE B CD1 1 
ATOM   3197 C  CD2 . PHE B 1 128 ? -6.12200  12.11500  13.90800 1.000 30.73291 ? 128 PHE B CD2 1 
ATOM   3198 C  CE1 . PHE B 1 128 ? -5.70600  12.82600  16.54300 1.000 28.60382 ? 128 PHE B CE1 1 
ATOM   3199 C  CE2 . PHE B 1 128 ? -7.16400  12.59100  14.66800 1.000 33.07630 ? 128 PHE B CE2 1 
ATOM   3200 C  CZ  . PHE B 1 128 ? -6.95300  12.94300  15.99300 1.000 31.65938 ? 128 PHE B CZ  1 
ATOM   3201 N  N   . HIS B 1 129 ? -0.53100  11.47300  14.41900 1.000 28.14960 ? 129 HIS B N   1 
ATOM   3202 C  CA  . HIS B 1 129 ? 0.74600   10.79200  14.31800 1.000 28.72113 ? 129 HIS B CA  1 
ATOM   3203 C  C   . HIS B 1 129 ? 1.15600   10.27000  15.68600 1.000 28.63477 ? 129 HIS B C   1 
ATOM   3204 O  O   . HIS B 1 129 ? 0.56400   10.59800  16.71800 1.000 27.82721 ? 129 HIS B O   1 
ATOM   3205 C  CB  . HIS B 1 129 ? 1.81800   11.73100  13.75700 1.000 27.43903 ? 129 HIS B CB  1 
ATOM   3206 C  CG  . HIS B 1 129 ? 2.31400   12.72900  14.75200 1.000 27.85501 ? 129 HIS B CG  1 
ATOM   3207 N  ND1 . HIS B 1 129 ? 1.60500   13.85800  15.09300 1.000 28.04751 ? 129 HIS B ND1 1 
ATOM   3208 C  CD2 . HIS B 1 129 ? 3.44400   12.75500  15.49600 1.000 29.01127 ? 129 HIS B CD2 1 
ATOM   3209 C  CE1 . HIS B 1 129 ? 2.28300   14.54300  15.99800 1.000 28.94761 ? 129 HIS B CE1 1 
ATOM   3210 N  NE2 . HIS B 1 129 ? 3.40300   13.89400  16.26100 1.000 27.78692 ? 129 HIS B NE2 1 
ATOM   3211 N  N   . ARG B 1 130 ? 2.17000   9.42600   15.66400 1.000 28.95578 ? 130 ARG B N   1 
ATOM   3212 C  CA  . ARG B 1 130 ? 3.01300   9.15500   16.81300 1.000 29.33096 ? 130 ARG B CA  1 
ATOM   3213 C  C   . ARG B 1 130 ? 4.38000   9.75900   16.53100 1.000 28.71875 ? 130 ARG B C   1 
ATOM   3214 O  O   . ARG B 1 130 ? 4.78600   9.89400   15.37400 1.000 30.69678 ? 130 ARG B O   1 
ATOM   3215 C  CB  . ARG B 1 130 ? 3.14000   7.65000   17.06300 1.000 29.32266 ? 130 ARG B CB  1 
ATOM   3216 C  CG  . ARG B 1 130 ? 1.83500   6.89900   16.97800 1.000 27.81828 ? 130 ARG B CG  1 
ATOM   3217 C  CD  . ARG B 1 130 ? 2.05400   5.42800   16.76600 1.000 28.63688 ? 130 ARG B CD  1 
ATOM   3218 N  NE  . ARG B 1 130 ? 1.01200   4.63800   17.40500 1.000 30.60660 ? 130 ARG B NE  1 
ATOM   3219 C  CZ  . ARG B 1 130 ? 0.88400   3.32700   17.27300 1.000 32.47913 ? 130 ARG B CZ  1 
ATOM   3220 N  NH1 . ARG B 1 130 ? 1.67300   2.63200   16.47200 1.000 34.27324 ? 130 ARG B NH1 1 
ATOM   3221 N  NH2 . ARG B 1 130 ? -0.05500  2.69500   17.96500 1.000 32.88344 ? 130 ARG B NH2 1 
ATOM   3222 N  N   . ASP B 1 131 ? 5.09500   10.13600  17.58400 1.000 28.42681 ? 131 ASP B N   1 
ATOM   3223 C  CA  . ASP B 1 131 ? 6.46700   10.60100  17.41300 1.000 27.56476 ? 131 ASP B CA  1 
ATOM   3224 C  C   . ASP B 1 131 ? 7.40900   9.40200   17.24400 1.000 29.04495 ? 131 ASP B C   1 
ATOM   3225 O  O   . ASP B 1 131 ? 8.30400   9.13800   18.04100 1.000 28.37904 ? 131 ASP B O   1 
ATOM   3226 C  CB  . ASP B 1 131 ? 6.84600   11.50100  18.57600 1.000 26.61724 ? 131 ASP B CB  1 
ATOM   3227 C  CG  . ASP B 1 131 ? 5.94400   12.71900  18.67200 1.000 26.95488 ? 131 ASP B CG  1 
ATOM   3228 O  OD1 . ASP B 1 131 ? 5.40300   13.16500  17.63600 1.000 27.44822 ? 131 ASP B OD1 1 
ATOM   3229 O  OD2 . ASP B 1 131 ? 5.76900   13.24500  19.78200 1.000 26.91247 ? 131 ASP B OD2 1 
ATOM   3230 N  N   . ASP B 1 132 ? 7.18300   8.67500   16.14600 1.000 29.54962 ? 132 ASP B N   1 
ATOM   3231 C  CA  . ASP B 1 132 ? 7.86800   7.43200   15.83000 1.000 29.11984 ? 132 ASP B CA  1 
ATOM   3232 C  C   . ASP B 1 132 ? 8.67200   7.49800   14.54000 1.000 29.04137 ? 132 ASP B C   1 
ATOM   3233 O  O   . ASP B 1 132 ? 9.33800   6.51900   14.19300 1.000 27.70422 ? 132 ASP B O   1 
ATOM   3234 C  CB  . ASP B 1 132 ? 6.85400   6.26700   15.73100 1.000 30.95575 ? 132 ASP B CB  1 
ATOM   3235 C  CG  . ASP B 1 132 ? 6.01000   6.28500   14.42700 1.000 31.93167 ? 132 ASP B CG  1 
ATOM   3236 O  OD1 . ASP B 1 132 ? 5.43100   7.33700   14.07400 1.000 30.38054 ? 132 ASP B OD1 1 
ATOM   3237 O  OD2 . ASP B 1 132 ? 5.91100   5.22400   13.76200 1.000 34.20401 ? 132 ASP B OD2 1 
ATOM   3238 N  N   . ALA B 1 133 ? 8.63600   8.61700   13.81900 1.000 30.04365 ? 133 ALA B N   1 
ATOM   3239 C  CA  . ALA B 1 133 ? 9.21700   8.64900   12.48500 1.000 29.76985 ? 133 ALA B CA  1 
ATOM   3240 C  C   . ALA B 1 133 ? 10.72800  8.84400   12.50600 1.000 28.17646 ? 133 ALA B C   1 
ATOM   3241 O  O   . ALA B 1 133 ? 11.41100  8.38800   11.58600 1.000 28.64134 ? 133 ALA B O   1 
ATOM   3242 C  CB  . ALA B 1 133 ? 8.55100   9.74700   11.65000 1.000 29.67844 ? 133 ALA B CB  1 
ATOM   3243 N  N   . THR B 1 134 ? 11.27900  9.50200   13.52800 1.000 27.62167 ? 134 THR B N   1 
ATOM   3244 C  CA  . THR B 1 134 ? 12.71100  9.78600   13.49900 1.000 27.07846 ? 134 THR B CA  1 
ATOM   3245 C  C   . THR B 1 134 ? 13.54000  8.51800   13.68500 1.000 25.53438 ? 134 THR B C   1 
ATOM   3246 O  O   . THR B 1 134 ? 14.57200  8.34000   13.02700 1.000 24.69564 ? 134 THR B O   1 
ATOM   3247 C  CB  . THR B 1 134 ? 13.07200  10.82800  14.55700 1.000 27.50484 ? 134 THR B CB  1 
ATOM   3248 O  OG1 . THR B 1 134 ? 12.31300  12.02500  14.32900 1.000 29.95106 ? 134 THR B OG1 1 
ATOM   3249 C  CG2 . THR B 1 134 ? 14.55800  11.15900  14.47000 1.000 24.77089 ? 134 THR B CG2 1 
ATOM   3250 N  N   . HIS B 1 135 ? 13.10900  7.62800   14.57900 1.000 26.67563 ? 135 HIS B N   1 
ATOM   3251 C  CA  . HIS B 1 135 ? 13.74200  6.32700   14.78900 1.000 27.05759 ? 135 HIS B CA  1 
ATOM   3252 C  C   . HIS B 1 135 ? 12.73700  5.23700   14.41800 1.000 27.66622 ? 135 HIS B C   1 
ATOM   3253 O  O   . HIS B 1 135 ? 12.06300  4.67600   15.29600 1.000 26.70285 ? 135 HIS B O   1 
ATOM   3254 C  CB  . HIS B 1 135 ? 14.22900  6.17100   16.23000 1.000 24.11751 ? 135 HIS B CB  1 
ATOM   3255 C  CG  . HIS B 1 135 ? 15.13900  7.26700   16.68600 1.000 22.81031 ? 135 HIS B CG  1 
ATOM   3256 N  ND1 . HIS B 1 135 ? 14.68300  8.52400   17.01900 1.000 22.20178 ? 135 HIS B ND1 1 
ATOM   3257 C  CD2 . HIS B 1 135 ? 16.47900  7.29000   16.87600 1.000 21.64641 ? 135 HIS B CD2 1 
ATOM   3258 C  CE1 . HIS B 1 135 ? 15.70400  9.27200   17.39300 1.000 21.74791 ? 135 HIS B CE1 1 
ATOM   3259 N  NE2 . HIS B 1 135 ? 16.80500  8.54700   17.31300 1.000 20.99247 ? 135 HIS B NE2 1 
ATOM   3260 N  N   . PRO B 1 136 ? 12.63100  4.89300   13.13000 1.000 26.15701 ? 136 PRO B N   1 
ATOM   3261 C  CA  . PRO B 1 136 ? 11.59600  3.94200   12.69100 1.000 27.48191 ? 136 PRO B CA  1 
ATOM   3262 C  C   . PRO B 1 136 ? 11.64900  2.56600   13.35100 1.000 29.63996 ? 136 PRO B C   1 
ATOM   3263 O  O   . PRO B 1 136 ? 10.66000  1.83300   13.25600 1.000 30.70796 ? 136 PRO B O   1 
ATOM   3264 C  CB  . PRO B 1 136 ? 11.84800  3.83400   11.18300 1.000 27.54747 ? 136 PRO B CB  1 
ATOM   3265 C  CG  . PRO B 1 136 ? 12.46300  5.14000   10.82600 1.000 28.36967 ? 136 PRO B CG  1 
ATOM   3266 C  CD  . PRO B 1 136 ? 13.35000  5.47900   11.98900 1.000 27.41950 ? 136 PRO B CD  1 
ATOM   3267 N  N   . LEU B 1 137 ? 12.74400  2.18500   14.01900 1.000 28.03109 ? 137 LEU B N   1 
ATOM   3268 C  CA  . LEU B 1 137 ? 12.77400  0.88600   14.68300 1.000 27.38883 ? 137 LEU B CA  1 
ATOM   3269 C  C   . LEU B 1 137 ? 11.77000  0.79400   15.82800 1.000 28.81352 ? 137 LEU B C   1 
ATOM   3270 O  O   . LEU B 1 137 ? 11.37600  -0.31100  16.20500 1.000 29.59383 ? 137 LEU B O   1 
ATOM   3271 C  CB  . LEU B 1 137 ? 14.19100  0.57700   15.18100 1.000 26.70148 ? 137 LEU B CB  1 
ATOM   3272 C  CG  . LEU B 1 137 ? 14.84200  1.39700   16.29200 1.000 25.20166 ? 137 LEU B CG  1 
ATOM   3273 C  CD1 . LEU B 1 137 ? 14.32000  1.02100   17.66700 1.000 24.95297 ? 137 LEU B CD1 1 
ATOM   3274 C  CD2 . LEU B 1 137 ? 16.34500  1.19900   16.22400 1.000 25.34145 ? 137 LEU B CD2 1 
ATOM   3275 N  N   . MET B 1 138 ? 11.36700  1.92600   16.40100 1.000 28.33169 ? 138 MET B N   1 
ATOM   3276 C  CA  . MET B 1 138 ? 10.29300  1.93700   17.39100 1.000 28.79060 ? 138 MET B CA  1 
ATOM   3277 C  C   . MET B 1 138 ? 8.97900   1.39300   16.82900 1.000 30.13828 ? 138 MET B C   1 
ATOM   3278 O  O   . MET B 1 138 ? 8.16600   0.85400   17.58800 1.000 30.33064 ? 138 MET B O   1 
ATOM   3279 C  CB  . MET B 1 138 ? 10.08100  3.36100   17.90600 1.000 27.84975 ? 138 MET B CB  1 
ATOM   3280 C  CG  . MET B 1 138 ? 11.34500  4.06500   18.37400 1.000 30.14494 ? 138 MET B CG  1 
ATOM   3281 S  SD  . MET B 1 138 ? 11.11600  5.85500   18.48700 1.000 33.37556 ? 138 MET B SD  1 
ATOM   3282 C  CE  . MET B 1 138 ? 9.38900   5.92800   18.94600 1.000 25.41993 ? 138 MET B CE  1 
ATOM   3283 N  N   . HIS B 1 139 ? 8.74500   1.55300   15.51500 1.000 31.55458 ? 139 HIS B N   1 
ATOM   3284 C  CA  . HIS B 1 139 ? 7.54400   1.03000   14.86100 1.000 32.79400 ? 139 HIS B CA  1 
ATOM   3285 C  C   . HIS B 1 139 ? 7.35600   -0.44300  15.16700 1.000 34.71558 ? 139 HIS B C   1 
ATOM   3286 O  O   . HIS B 1 139 ? 6.22500   -0.94400  15.16100 1.000 35.98664 ? 139 HIS B O   1 
ATOM   3287 C  CB  . HIS B 1 139 ? 7.64700   1.24900   13.34000 1.000 33.53846 ? 139 HIS B CB  1 
ATOM   3288 C  CG  . HIS B 1 139 ? 6.38300   0.99200   12.56900 1.000 35.88062 ? 139 HIS B CG  1 
ATOM   3289 N  ND1 . HIS B 1 139 ? 5.70800   1.99300   11.90200 1.000 38.72933 ? 139 HIS B ND1 1 
ATOM   3290 C  CD2 . HIS B 1 139 ? 5.70800   -0.15300  12.30400 1.000 37.90279 ? 139 HIS B CD2 1 
ATOM   3291 C  CE1 . HIS B 1 139 ? 4.65500   1.48100   11.28800 1.000 39.68926 ? 139 HIS B CE1 1 
ATOM   3292 N  NE2 . HIS B 1 139 ? 4.63200   0.18000   11.51500 1.000 40.19641 ? 139 HIS B NE2 1 
ATOM   3293 N  N   . TYR B 1 140 ? 8.45200   -1.14200  15.46900 1.000 33.10972 ? 140 TYR B N   1 
ATOM   3294 C  CA  . TYR B 1 140 ? 8.47000   -2.58700  15.62600 1.000 33.20498 ? 140 TYR B CA  1 
ATOM   3295 C  C   . TYR B 1 140 ? 8.77100   -3.03400  17.05300 1.000 32.63474 ? 140 TYR B C   1 
ATOM   3296 O  O   . TYR B 1 140 ? 8.94200   -4.23400  17.28900 1.000 33.81280 ? 140 TYR B O   1 
ATOM   3297 C  CB  . TYR B 1 140 ? 9.48000   -3.19700  14.65400 1.000 32.49767 ? 140 TYR B CB  1 
ATOM   3298 C  CG  . TYR B 1 140 ? 9.28400   -2.74600  13.21400 1.000 33.18260 ? 140 TYR B CG  1 
ATOM   3299 C  CD1 . TYR B 1 140 ? 8.32200   -3.35300  12.41000 1.000 35.00071 ? 140 TYR B CD1 1 
ATOM   3300 C  CD2 . TYR B 1 140 ? 10.06600  -1.71800  12.69700 1.000 33.13909 ? 140 TYR B CD2 1 
ATOM   3301 C  CE1 . TYR B 1 140 ? 8.16000   -2.92400  11.12000 1.000 35.65149 ? 140 TYR B CE1 1 
ATOM   3302 C  CE2 . TYR B 1 140 ? 9.87700   -1.31900  11.40000 1.000 33.42198 ? 140 TYR B CE2 1 
ATOM   3303 C  CZ  . TYR B 1 140 ? 8.92600   -1.90300  10.58300 1.000 34.20362 ? 140 TYR B CZ  1 
ATOM   3304 O  OH  . TYR B 1 140 ? 8.76400   -1.49800  9.30800  1.000 36.95456 ? 140 TYR B OH  1 
ATOM   3305 N  N   . GLN B 1 141 ? 8.81200   -2.11900  18.01400 1.000 30.53767 ? 141 GLN B N   1 
ATOM   3306 C  CA  . GLN B 1 141 ? 8.91800   -2.54700  19.40800 1.000 31.88729 ? 141 GLN B CA  1 
ATOM   3307 C  C   . GLN B 1 141 ? 7.53900   -2.93500  19.94300 1.000 34.04437 ? 141 GLN B C   1 
ATOM   3308 O  O   . GLN B 1 141 ? 6.58700   -2.15700  19.81100 1.000 35.27011 ? 141 GLN B O   1 
ATOM   3309 C  CB  . GLN B 1 141 ? 9.53000   -1.44100  20.26900 1.000 32.36316 ? 141 GLN B CB  1 
ATOM   3310 C  CG  . GLN B 1 141 ? 10.96400  -1.02800  19.85900 1.000 32.09610 ? 141 GLN B CG  1 
ATOM   3311 C  CD  . GLN B 1 141 ? 12.07700  -1.85100  20.53400 1.000 28.76595 ? 141 GLN B CD  1 
ATOM   3312 O  OE1 . GLN B 1 141 ? 12.76700  -2.64300  19.88900 1.000 27.48248 ? 141 GLN B OE1 1 
ATOM   3313 N  NE2 . GLN B 1 141 ? 12.26200  -1.63800  21.83300 1.000 28.50771 ? 141 GLN B NE2 1 
ATOM   3314 N  N   . PRO B 1 142 ? 7.38800   -4.11600  20.53800 1.000 34.67970 ? 142 PRO B N   1 
ATOM   3315 C  CA  . PRO B 1 142 ? 6.08300   -4.50900  21.07800 1.000 34.92144 ? 142 PRO B CA  1 
ATOM   3316 C  C   . PRO B 1 142 ? 5.70800   -3.67900  22.29400 1.000 34.73518 ? 142 PRO B C   1 
ATOM   3317 O  O   . PRO B 1 142 ? 6.55500   -3.10500  22.97900 1.000 34.35359 ? 142 PRO B O   1 
ATOM   3318 C  CB  . PRO B 1 142 ? 6.27800   -5.98200  21.45300 1.000 34.63760 ? 142 PRO B CB  1 
ATOM   3319 C  CG  . PRO B 1 142 ? 7.49400   -6.41200  20.69800 1.000 33.14517 ? 142 PRO B CG  1 
ATOM   3320 C  CD  . PRO B 1 142 ? 8.36400   -5.20900  20.63400 1.000 33.15536 ? 142 PRO B CD  1 
ATOM   3321 N  N   . LEU B 1 143 ? 4.40300   -3.64300  22.56300 1.000 33.65678 ? 143 LEU B N   1 
ATOM   3322 C  CA  . LEU B 1 143 ? 3.86700   -2.77200  23.60100 1.000 34.22351 ? 143 LEU B CA  1 
ATOM   3323 C  C   . LEU B 1 143 ? 4.51300   -3.02000  24.96100 1.000 34.91423 ? 143 LEU B C   1 
ATOM   3324 O  O   . LEU B 1 143 ? 4.69500   -2.07500  25.74400 1.000 34.89623 ? 143 LEU B O   1 
ATOM   3325 C  CB  . LEU B 1 143 ? 2.35600   -2.96100  23.68800 1.000 34.70213 ? 143 LEU B CB  1 
ATOM   3326 C  CG  . LEU B 1 143 ? 1.66800   -2.01500  24.66300 1.000 34.60202 ? 143 LEU B CG  1 
ATOM   3327 C  CD1 . LEU B 1 143 ? 1.97300   -0.57700  24.27500 1.000 33.07641 ? 143 LEU B CD1 1 
ATOM   3328 C  CD2 . LEU B 1 143 ? 0.18800   -2.27000  24.66100 1.000 33.41615 ? 143 LEU B CD2 1 
ATOM   3329 N  N   . GLU B 1 144 ? 4.87400   -4.27200  25.25600 1.000 34.86366 ? 144 GLU B N   1 
ATOM   3330 C  CA  . GLU B 1 144 ? 5.36600   -4.64900  26.57700 1.000 33.88323 ? 144 GLU B CA  1 
ATOM   3331 C  C   . GLU B 1 144 ? 6.83700   -4.32100  26.79300 1.000 34.32638 ? 144 GLU B C   1 
ATOM   3332 O  O   . GLU B 1 144 ? 7.29300   -4.33600  27.94200 1.000 33.25791 ? 144 GLU B O   1 
ATOM   3333 C  CB  . GLU B 1 144 ? 5.14700   -6.14700  26.81800 1.000 35.85189 ? 144 GLU B CB  1 
ATOM   3334 C  CG  . GLU B 1 144 ? 6.03800   -7.07300  26.00700 1.000 36.75482 ? 144 GLU B CG  1 
ATOM   3335 C  CD  . GLU B 1 144 ? 5.27200   -7.79600  24.92800 1.000 38.49690 ? 144 GLU B CD  1 
ATOM   3336 O  OE1 . GLU B 1 144 ? 4.40300   -7.15300  24.30600 1.000 39.01033 ? 144 GLU B OE1 1 
ATOM   3337 O  OE2 . GLU B 1 144 ? 5.52200   -9.00300  24.71200 1.000 40.67113 ? 144 GLU B OE2 1 
ATOM   3338 N  N   . ALA B 1 145 ? 7.57900   -4.01700  25.73100 1.000 33.70256 ? 145 ALA B N   1 
ATOM   3339 C  CA  . ALA B 1 145 ? 9.00000   -3.72900  25.85100 1.000 31.04159 ? 145 ALA B CA  1 
ATOM   3340 C  C   . ALA B 1 145 ? 9.22300   -2.42500  26.61800 1.000 29.83395 ? 145 ALA B C   1 
ATOM   3341 O  O   . ALA B 1 145 ? 8.36600   -1.53700  26.59900 1.000 30.34459 ? 145 ALA B O   1 
ATOM   3342 C  CB  . ALA B 1 145 ? 9.63300   -3.63500  24.46400 1.000 29.46159 ? 145 ALA B CB  1 
ATOM   3343 N  N   . PRO B 1 146 ? 10.35900  -2.29200  27.30700 1.000 30.57379 ? 146 PRO B N   1 
ATOM   3344 C  CA  . PRO B 1 146 ? 10.69200  -1.02500  27.97000 1.000 30.35711 ? 146 PRO B CA  1 
ATOM   3345 C  C   . PRO B 1 146 ? 10.57200  0.13900   27.00500 1.000 28.77160 ? 146 PRO B C   1 
ATOM   3346 O  O   . PRO B 1 146 ? 11.09100  0.07500   25.88000 1.000 29.17610 ? 146 PRO B O   1 
ATOM   3347 C  CB  . PRO B 1 146 ? 12.15100  -1.23100  28.40800 1.000 29.32309 ? 146 PRO B CB  1 
ATOM   3348 C  CG  . PRO B 1 146 ? 12.30000  -2.69100  28.55100 1.000 30.26070 ? 146 PRO B CG  1 
ATOM   3349 C  CD  . PRO B 1 146 ? 11.41800  -3.29900  27.49100 1.000 31.54756 ? 146 PRO B CD  1 
ATOM   3350 N  N   . PRO B 1 147 ? 9.86800   1.20200   27.38600 1.000 28.04656 ? 147 PRO B N   1 
ATOM   3351 C  CA  . PRO B 1 147 ? 9.73400   2.35300   26.48200 1.000 26.46595 ? 147 PRO B CA  1 
ATOM   3352 C  C   . PRO B 1 147 ? 11.06200  3.07300   26.29700 1.000 26.24223 ? 147 PRO B C   1 
ATOM   3353 O  O   . PRO B 1 147 ? 11.87200  3.17100   27.22200 1.000 25.85232 ? 147 PRO B O   1 
ATOM   3354 C  CB  . PRO B 1 147 ? 8.70200   3.24500   27.18200 1.000 25.98558 ? 147 PRO B CB  1 
ATOM   3355 C  CG  . PRO B 1 147 ? 8.70200   2.80400   28.60300 1.000 27.48500 ? 147 PRO B CG  1 
ATOM   3356 C  CD  . PRO B 1 147 ? 9.04100   1.33900   28.59400 1.000 28.49240 ? 147 PRO B CD  1 
ATOM   3357 N  N   . VAL B 1 148 ? 11.28000  3.57100   25.07900 1.000 25.21098 ? 148 VAL B N   1 
ATOM   3358 C  CA  . VAL B 1 148 ? 12.53400  4.21400   24.70900 1.000 24.28486 ? 148 VAL B CA  1 
ATOM   3359 C  C   . VAL B 1 148 ? 12.37400  5.69600   24.42200 1.000 22.15935 ? 148 VAL B C   1 
ATOM   3360 O  O   . VAL B 1 148 ? 13.38400  6.37200   24.19000 1.000 22.30620 ? 148 VAL B O   1 
ATOM   3361 C  CB  . VAL B 1 148 ? 13.19900  3.51100   23.50800 1.000 24.35558 ? 148 VAL B CB  1 
ATOM   3362 C  CG1 . VAL B 1 148 ? 13.75900  2.13000   23.90900 1.000 25.26710 ? 148 VAL B CG1 1 
ATOM   3363 C  CG2 . VAL B 1 148 ? 12.22900  3.41100   22.33300 1.000 24.62095 ? 148 VAL B CG2 1 
ATOM   3364 N  N   . SER B 1 149 ? 11.15200  6.23200   24.45700 1.000 22.92412 ? 149 SER B N   1 
ATOM   3365 C  CA  . SER B 1 149 ? 10.88900  7.59900   24.02300 1.000 22.28084 ? 149 SER B CA  1 
ATOM   3366 C  C   . SER B 1 149 ? 9.76000   8.20900   24.84400 1.000 22.36608 ? 149 SER B C   1 
ATOM   3367 O  O   . SER B 1 149 ? 8.78500   7.52600   25.16000 1.000 24.15576 ? 149 SER B O   1 
ATOM   3368 C  CB  . SER B 1 149 ? 10.51100  7.63700   22.54000 1.000 21.62989 ? 149 SER B CB  1 
ATOM   3369 O  OG  . SER B 1 149 ? 10.16500  8.94700   22.14800 1.000 22.65491 ? 149 SER B OG  1 
ATOM   3370 N  N   . LEU B 1 150 ? 9.88500   9.50000   25.16200 1.000 22.97920 ? 150 LEU B N   1 
ATOM   3371 C  CA  . LEU B 1 150 ? 8.85500   10.23600  25.89400 1.000 23.52375 ? 150 LEU B CA  1 
ATOM   3372 C  C   . LEU B 1 150 ? 8.75300   11.65500  25.35900 1.000 22.93662 ? 150 LEU B C   1 
ATOM   3373 O  O   . LEU B 1 150 ? 9.76600   12.35700  25.28100 1.000 22.35171 ? 150 LEU B O   1 
ATOM   3374 C  CB  . LEU B 1 150 ? 9.15800   10.27800  27.39500 1.000 23.62606 ? 150 LEU B CB  1 
ATOM   3375 C  CG  . LEU B 1 150 ? 8.19000   11.08700  28.26500 1.000 24.20128 ? 150 LEU B CG  1 
ATOM   3376 C  CD1 . LEU B 1 150 ? 6.81300   10.42300  28.32800 1.000 23.33055 ? 150 LEU B CD1 1 
ATOM   3377 C  CD2 . LEU B 1 150 ? 8.77400   11.26500  29.65100 1.000 23.49515 ? 150 LEU B CD2 1 
ATOM   3378 N  N   . SER B 1 151 ? 7.53500   12.07900  25.02100 1.000 22.64337 ? 151 SER B N   1 
ATOM   3379 C  CA  . SER B 1 151 ? 7.28400   13.40200  24.45600 1.000 23.70562 ? 151 SER B CA  1 
ATOM   3380 C  C   . SER B 1 151 ? 6.86600   14.36400  25.55900 1.000 23.57308 ? 151 SER B C   1 
ATOM   3381 O  O   . SER B 1 151 ? 6.00500   14.03600  26.37900 1.000 23.76406 ? 151 SER B O   1 
ATOM   3382 C  CB  . SER B 1 151 ? 6.19700   13.34100  23.38400 1.000 23.28379 ? 151 SER B CB  1 
ATOM   3383 O  OG  . SER B 1 151 ? 6.58300   12.50700  22.31600 1.000 24.21301 ? 151 SER B OG  1 
ATOM   3384 N  N   . VAL B 1 152 ? 7.46900   15.54900  25.56900 1.000 23.65811 ? 152 VAL B N   1 
ATOM   3385 C  CA  . VAL B 1 152 ? 7.22600   16.56600  26.58800 1.000 24.23445 ? 152 VAL B CA  1 
ATOM   3386 C  C   . VAL B 1 152 ? 6.89200   17.86000  25.86400 1.000 24.44324 ? 152 VAL B C   1 
ATOM   3387 O  O   . VAL B 1 152 ? 7.74400   18.42500  25.17400 1.000 23.28698 ? 152 VAL B O   1 
ATOM   3388 C  CB  . VAL B 1 152 ? 8.43800   16.77300  27.51500 1.000 23.23760 ? 152 VAL B CB  1 
ATOM   3389 C  CG1 . VAL B 1 152 ? 8.09300   17.74600  28.61900 1.000 23.73678 ? 152 VAL B CG1 1 
ATOM   3390 C  CG2 . VAL B 1 152 ? 8.94200   15.45400  28.08500 1.000 22.33120 ? 152 VAL B CG2 1 
ATOM   3391 N  N   . ILE B 1 153 ? 5.66500   18.33200  26.02400 1.000 25.06902 ? 153 ILE B N   1 
ATOM   3392 C  CA  . ILE B 1 153 ? 5.13600   19.40400  25.19500 1.000 25.70682 ? 153 ILE B CA  1 
ATOM   3393 C  C   . ILE B 1 153 ? 4.88600   20.61900  26.07700 1.000 26.35538 ? 153 ILE B C   1 
ATOM   3394 O  O   . ILE B 1 153 ? 4.16600   20.53300  27.08000 1.000 26.76246 ? 153 ILE B O   1 
ATOM   3395 C  CB  . ILE B 1 153 ? 3.87100   18.94800  24.45400 1.000 24.99231 ? 153 ILE B CB  1 
ATOM   3396 C  CG1 . ILE B 1 153 ? 4.21800   17.72800  23.59500 1.000 25.19097 ? 153 ILE B CG1 1 
ATOM   3397 C  CG2 . ILE B 1 153 ? 3.31900   20.05000  23.58700 1.000 25.28976 ? 153 ILE B CG2 1 
ATOM   3398 C  CD1 . ILE B 1 153 ? 3.13200   17.27200  22.64200 1.000 23.32609 ? 153 ILE B CD1 1 
ATOM   3399 N  N   . PHE B 1 154 ? 5.50200   21.74300  25.70900 1.000 25.40886 ? 154 PHE B N   1 
ATOM   3400 C  CA  . PHE B 1 154 ? 5.47600   22.97900  26.48600 1.000 25.77214 ? 154 PHE B CA  1 
ATOM   3401 C  C   . PHE B 1 154 ? 4.65200   24.03500  25.76400 1.000 26.48008 ? 154 PHE B C   1 
ATOM   3402 O  O   . PHE B 1 154 ? 5.13200   24.62900  24.78700 1.000 27.14878 ? 154 PHE B O   1 
ATOM   3403 C  CB  . PHE B 1 154 ? 6.89800   23.50600  26.71900 1.000 25.13292 ? 154 PHE B CB  1 
ATOM   3404 C  CG  . PHE B 1 154 ? 7.80100   22.56900  27.48400 1.000 24.95338 ? 154 PHE B CG  1 
ATOM   3405 C  CD1 . PHE B 1 154 ? 7.71800   22.47300  28.85400 1.000 25.18959 ? 154 PHE B CD1 1 
ATOM   3406 C  CD2 . PHE B 1 154 ? 8.77300   21.82600  26.82800 1.000 24.27557 ? 154 PHE B CD2 1 
ATOM   3407 C  CE1 . PHE B 1 154 ? 8.56700   21.63000  29.55000 1.000 24.90851 ? 154 PHE B CE1 1 
ATOM   3408 C  CE2 . PHE B 1 154 ? 9.61800   20.98600  27.51700 1.000 22.97456 ? 154 PHE B CE2 1 
ATOM   3409 C  CZ  . PHE B 1 154 ? 9.52000   20.89000  28.87500 1.000 23.68468 ? 154 PHE B CZ  1 
ATOM   3410 N  N   . PRO B 1 155 ? 3.42800   24.32600  26.20000 1.000 28.12029 ? 155 PRO B N   1 
ATOM   3411 C  CA  . PRO B 1 155 ? 2.70100   25.47400  25.63200 1.000 30.18148 ? 155 PRO B CA  1 
ATOM   3412 C  C   . PRO B 1 155 ? 3.37600   26.78100  26.02500 1.000 28.52477 ? 155 PRO B C   1 
ATOM   3413 O  O   . PRO B 1 155 ? 3.50000   27.08900  27.20800 1.000 28.94343 ? 155 PRO B O   1 
ATOM   3414 C  CB  . PRO B 1 155 ? 1.30300   25.34600  26.24800 1.000 30.09400 ? 155 PRO B CB  1 
ATOM   3415 C  CG  . PRO B 1 155 ? 1.51000   24.52800  27.48700 1.000 28.90117 ? 155 PRO B CG  1 
ATOM   3416 C  CD  . PRO B 1 155 ? 2.62000   23.58300  27.18000 1.000 27.83693 ? 155 PRO B CD  1 
ATOM   3417 N  N   . LEU B 1 156 ? 3.83200   27.54900  25.04200 1.000 28.69293 ? 156 LEU B N   1 
ATOM   3418 C  CA  . LEU B 1 156 ? 4.47300   28.87000  25.28700 1.000 30.31013 ? 156 LEU B CA  1 
ATOM   3419 C  C   . LEU B 1 156 ? 3.42000   29.98600  25.17900 1.000 31.91544 ? 156 LEU B C   1 
ATOM   3420 O  O   . LEU B 1 156 ? 3.71600   31.08500  25.65400 1.000 32.76694 ? 156 LEU B O   1 
ATOM   3421 C  CB  . LEU B 1 156 ? 5.70900   29.10800  24.41800 1.000 28.96363 ? 156 LEU B CB  1 
ATOM   3422 C  CG  . LEU B 1 156 ? 6.95800   28.32200  24.82700 1.000 28.20822 ? 156 LEU B CG  1 
ATOM   3423 C  CD1 . LEU B 1 156 ? 8.21100   29.14700  24.63600 1.000 27.74380 ? 156 LEU B CD1 1 
ATOM   3424 C  CD2 . LEU B 1 156 ? 6.86700   27.81300  26.24700 1.000 26.97582 ? 156 LEU B CD2 1 
ATOM   3425 N  N   . THR B 1 157 ? 2.29900   29.74200  24.51300 1.000 30.97561 ? 157 THR B N   1 
ATOM   3426 C  CA  . THR B 1 157 ? 1.14200   30.62400  24.54000 1.000 30.36582 ? 157 THR B CA  1 
ATOM   3427 C  C   . THR B 1 157 ? -0.06700  29.74300  24.83400 1.000 32.05064 ? 157 THR B C   1 
ATOM   3428 O  O   . THR B 1 157 ? 0.02400   28.51500  24.79900 1.000 31.76425 ? 157 THR B O   1 
ATOM   3429 C  CB  . THR B 1 157 ? 0.98000   31.39200  23.21900 1.000 30.67656 ? 157 THR B CB  1 
ATOM   3430 O  OG1 . THR B 1 157 ? 0.72100   30.47000  22.15900 1.000 33.56397 ? 157 THR B OG1 1 
ATOM   3431 C  CG2 . THR B 1 157 ? 2.24400   32.15400  22.87700 1.000 30.54493 ? 157 THR B CG2 1 
ATOM   3432 N  N   . GLU B 1 158 ? -1.20300  30.35500  25.15400 1.000 33.17829 ? 158 GLU B N   1 
ATOM   3433 C  CA  . GLU B 1 158 ? -2.38000  29.56400  25.49000 1.000 32.60804 ? 158 GLU B CA  1 
ATOM   3434 C  C   . GLU B 1 158 ? -2.70400  28.58400  24.36800 1.000 32.92934 ? 158 GLU B C   1 
ATOM   3435 O  O   . GLU B 1 158 ? -2.62200  28.92200  23.18400 1.000 32.47856 ? 158 GLU B O   1 
ATOM   3436 C  CB  . GLU B 1 158 ? -3.57400  30.47600  25.75800 1.000 33.17252 ? 158 GLU B CB  1 
ATOM   3437 C  CG  . GLU B 1 158 ? -3.83500  31.46400  24.63700 1.000 35.26132 ? 158 GLU B CG  1 
ATOM   3438 C  CD  . GLU B 1 158 ? -5.08500  32.29700  24.84000 1.000 36.05007 ? 158 GLU B CD  1 
ATOM   3439 O  OE1 . GLU B 1 158 ? -5.74000  32.16100  25.89300 1.000 37.43982 ? 158 GLU B OE1 1 
ATOM   3440 O  OE2 . GLU B 1 158 ? -5.41700  33.08800  23.93600 1.000 36.56802 ? 158 GLU B OE2 1 
ATOM   3441 N  N   . PHE B 1 159 ? -3.01300  27.34300  24.75400 1.000 33.90978 ? 159 PHE B N   1 
ATOM   3442 C  CA  . PHE B 1 159 ? -3.56900  26.34100  23.85300 1.000 32.17286 ? 159 PHE B CA  1 
ATOM   3443 C  C   . PHE B 1 159 ? -5.08200  26.36700  24.00600 1.000 33.17155 ? 159 PHE B C   1 
ATOM   3444 O  O   . PHE B 1 159 ? -5.60100  26.20200  25.11300 1.000 32.86435 ? 159 PHE B O   1 
ATOM   3445 C  CB  . PHE B 1 159 ? -3.04200  24.94300  24.16500 1.000 31.02754 ? 159 PHE B CB  1 
ATOM   3446 C  CG  . PHE B 1 159 ? -1.65900  24.67400  23.65400 1.000 30.53258 ? 159 PHE B CG  1 
ATOM   3447 C  CD1 . PHE B 1 159 ? -0.86900  25.69100  23.15500 1.000 30.60206 ? 159 PHE B CD1 1 
ATOM   3448 C  CD2 . PHE B 1 159 ? -1.15100  23.38400  23.66200 1.000 29.78768 ? 159 PHE B CD2 1 
ATOM   3449 C  CE1 . PHE B 1 159 ? 0.40700   25.42900  22.69100 1.000 30.12219 ? 159 PHE B CE1 1 
ATOM   3450 C  CE2 . PHE B 1 159 ? 0.13100   23.11900  23.20400 1.000 29.03463 ? 159 PHE B CE2 1 
ATOM   3451 C  CZ  . PHE B 1 159 ? 0.90600   24.14600  22.71600 1.000 28.78094 ? 159 PHE B CZ  1 
ATOM   3452 N  N   . THR B 1 160 ? -5.79200  26.59400  22.91100 1.000 35.36457 ? 160 THR B N   1 
ATOM   3453 C  CA  . THR B 1 160 ? -7.24300  26.63200  22.95700 1.000 36.68208 ? 160 THR B CA  1 
ATOM   3454 C  C   . THR B 1 160 ? -7.80800  25.76500  21.84300 1.000 37.38470 ? 160 THR B C   1 
ATOM   3455 O  O   . THR B 1 160 ? -7.10700  25.40100  20.89900 1.000 37.20425 ? 160 THR B O   1 
ATOM   3456 C  CB  . THR B 1 160 ? -7.78400  28.07100  22.82300 1.000 38.01177 ? 160 THR B CB  1 
ATOM   3457 O  OG1 . THR B 1 160 ? -7.52200  28.56200  21.50400 1.000 37.96057 ? 160 THR B OG1 1 
ATOM   3458 C  CG2 . THR B 1 160 ? -7.14000  29.00500  23.84600 1.000 35.75551 ? 160 THR B CG2 1 
ATOM   3459 N  N   . GLU B 1 161 ? -9.09800  25.44400  21.96300 1.000 37.66970 ? 161 GLU B N   1 
ATOM   3460 C  CA  . GLU B 1 161 ? -9.81700  24.82600  20.85300 1.000 39.83754 ? 161 GLU B CA  1 
ATOM   3461 C  C   . GLU B 1 161 ? -9.65700  25.65200  19.58800 1.000 40.01729 ? 161 GLU B C   1 
ATOM   3462 O  O   . GLU B 1 161 ? -9.50300  25.10800  18.48700 1.000 42.09508 ? 161 GLU B O   1 
ATOM   3463 C  CB  . GLU B 1 161 ? -11.30100 24.68000  21.20900 1.000 43.80604 ? 161 GLU B CB  1 
ATOM   3464 C  CG  . GLU B 1 161 ? -12.21700 24.23000  20.06400 1.000 47.03756 ? 161 GLU B CG  1 
ATOM   3465 C  CD  . GLU B 1 161 ? -13.71000 24.36000  20.39900 1.000 51.97969 ? 161 GLU B CD  1 
ATOM   3466 O  OE1 . GLU B 1 161 ? -14.06000 24.45300  21.60000 1.000 51.03321 ? 161 GLU B OE1 1 
ATOM   3467 O  OE2 . GLU B 1 161 ? -14.53600 24.37700  19.45500 1.000 57.84105 ? 161 GLU B OE2 1 
ATOM   3468 N  N   . GLU B 1 162 ? -9.64300  26.97400  19.74200 1.000 41.15851 ? 162 GLU B N   1 
ATOM   3469 C  CA  . GLU B 1 162 ? -9.68100  27.89400  18.61400 1.000 42.17652 ? 162 GLU B CA  1 
ATOM   3470 C  C   . GLU B 1 162 ? -8.31600  28.09600  17.97700 1.000 41.63881 ? 162 GLU B C   1 
ATOM   3471 O  O   . GLU B 1 162 ? -8.24400  28.39200  16.78000 1.000 44.14353 ? 162 GLU B O   1 
ATOM   3472 C  CB  . GLU B 1 162 ? -10.24300 29.24500  19.06400 1.000 43.46149 ? 162 GLU B CB  1 
ATOM   3473 C  CG  . GLU B 1 162 ? -11.51100 29.15800  19.91600 1.000 44.98607 ? 162 GLU B CG  1 
ATOM   3474 C  CD  . GLU B 1 162 ? -11.23000 28.91700  21.39700 1.000 43.36392 ? 162 GLU B CD  1 
ATOM   3475 O  OE1 . GLU B 1 162 ? -10.75600 29.84700  22.08200 1.000 43.90407 ? 162 GLU B OE1 1 
ATOM   3476 O  OE2 . GLU B 1 162 ? -11.48000 27.79100  21.87500 1.000 44.33144 ? 162 GLU B OE2 1 
ATOM   3477 N  N   . ASN B 1 163 ? -7.23100  27.96400  18.74500 1.000 43.90477 ? 163 ASN B N   1 
ATOM   3478 C  CA  . ASN B 1 163 ? -5.88800  28.19100  18.22500 1.000 43.05791 ? 163 ASN B CA  1 
ATOM   3479 C  C   . ASN B 1 163 ? -5.11300  26.89800  18.02300 1.000 41.89347 ? 163 ASN B C   1 
ATOM   3480 O  O   . ASN B 1 163 ? -3.90600  26.94200  17.79100 1.000 41.28642 ? 163 ASN B O   1 
ATOM   3481 C  CB  . ASN B 1 163 ? -5.11400  29.16100  19.12800 1.000 40.02978 ? 163 ASN B CB  1 
ATOM   3482 C  CG  . ASN B 1 163 ? -4.60500  28.52900  20.41000 1.000 37.57677 ? 163 ASN B CG  1 
ATOM   3483 O  OD1 . ASN B 1 163 ? -4.94900  27.39700  20.76800 1.000 37.06876 ? 163 ASN B OD1 1 
ATOM   3484 N  ND2 . ASN B 1 163 ? -3.77100  29.28100  21.12300 1.000 34.36992 ? 163 ASN B ND2 1 
ATOM   3485 N  N   . GLY B 1 164 ? -5.77600  25.75500  18.11200 1.000 41.32194 ? 164 GLY B N   1 
ATOM   3486 C  CA  . GLY B 1 164 ? -5.18900  24.49800  17.72200 1.000 40.31853 ? 164 GLY B CA  1 
ATOM   3487 C  C   . GLY B 1 164 ? -4.57200  23.66200  18.81800 1.000 37.35754 ? 164 GLY B C   1 
ATOM   3488 O  O   . GLY B 1 164 ? -3.65500  22.89200  18.52500 1.000 35.51465 ? 164 GLY B O   1 
ATOM   3489 N  N   . ALA B 1 165 ? -5.05000  23.78300  20.06100 1.000 35.40588 ? 165 ALA B N   1 
ATOM   3490 C  CA  . ALA B 1 165 ? -4.56700  22.98100  21.17700 1.000 32.61809 ? 165 ALA B CA  1 
ATOM   3491 C  C   . ALA B 1 165 ? -4.35400  21.53200  20.76000 1.000 31.88436 ? 165 ALA B C   1 
ATOM   3492 O  O   . ALA B 1 165 ? -5.15200  20.96200  20.01300 1.000 30.79866 ? 165 ALA B O   1 
ATOM   3493 C  CB  . ALA B 1 165 ? -5.56200  23.05100  22.34300 1.000 32.79108 ? 165 ALA B CB  1 
ATOM   3494 N  N   . THR B 1 166 ? -3.25200  20.94800  21.23700 1.000 30.33860 ? 166 THR B N   1 
ATOM   3495 C  CA  . THR B 1 166 ? -2.87200  19.59600  20.83700 1.000 29.21425 ? 166 THR B CA  1 
ATOM   3496 C  C   . THR B 1 166 ? -3.98800  18.60700  21.14600 1.000 28.25610 ? 166 THR B C   1 
ATOM   3497 O  O   . THR B 1 166 ? -4.61400  18.65900  22.20600 1.000 28.38890 ? 166 THR B O   1 
ATOM   3498 C  CB  . THR B 1 166 ? -1.58500  19.15500  21.54400 1.000 27.62488 ? 166 THR B CB  1 
ATOM   3499 O  OG1 . THR B 1 166 ? -0.67400  20.25700  21.63000 1.000 28.00205 ? 166 THR B OG1 1 
ATOM   3500 C  CG2 . THR B 1 166 ? -0.91800  18.02500  20.77400 1.000 26.53782 ? 166 THR B CG2 1 
ATOM   3501 N  N   . GLU B 1 167 ? -4.22800  17.70200  20.20400 1.000 27.98339 ? 167 GLU B N   1 
ATOM   3502 C  CA  . GLU B 1 167 ? -5.25900  16.68400  20.31100 1.000 28.08161 ? 167 GLU B CA  1 
ATOM   3503 C  C   . GLU B 1 167 ? -4.59400  15.33600  20.55400 1.000 28.50586 ? 167 GLU B C   1 
ATOM   3504 O  O   . GLU B 1 167 ? -3.72100  14.93100  19.78600 1.000 29.07224 ? 167 GLU B O   1 
ATOM   3505 C  CB  . GLU B 1 167 ? -6.11100  16.66400  19.04100 1.000 28.29164 ? 167 GLU B CB  1 
ATOM   3506 C  CG  . GLU B 1 167 ? -6.82700  17.99800  18.78900 1.000 29.25462 ? 167 GLU B CG  1 
ATOM   3507 C  CD  . GLU B 1 167 ? -7.30200  18.18700  17.36000 1.000 29.77897 ? 167 GLU B CD  1 
ATOM   3508 O  OE1 . GLU B 1 167 ? -7.69800  17.19700  16.71500 1.000 30.75949 ? 167 GLU B OE1 1 
ATOM   3509 O  OE2 . GLU B 1 167 ? -7.27700  19.33900  16.87500 1.000 31.72328 ? 167 GLU B OE2 1 
ATOM   3510 N  N   . VAL B 1 168 ? -4.99300  14.65300  21.62700 1.000 27.94732 ? 168 VAL B N   1 
ATOM   3511 C  CA  . VAL B 1 168 ? -4.40600  13.38000  22.03700 1.000 26.42410 ? 168 VAL B CA  1 
ATOM   3512 C  C   . VAL B 1 168 ? -5.50200  12.32300  22.07000 1.000 27.97695 ? 168 VAL B C   1 
ATOM   3513 O  O   . VAL B 1 168 ? -6.57200  12.55100  22.64700 1.000 29.11050 ? 168 VAL B O   1 
ATOM   3514 C  CB  . VAL B 1 168 ? -3.73000  13.49100  23.41400 1.000 26.29594 ? 168 VAL B CB  1 
ATOM   3515 C  CG1 . VAL B 1 168 ? -3.08200  12.17100  23.79300 1.000 28.12246 ? 168 VAL B CG1 1 
ATOM   3516 C  CG2 . VAL B 1 168 ? -2.71900  14.63100  23.43500 1.000 26.20483 ? 168 VAL B CG2 1 
ATOM   3517 N  N   . ILE B 1 169 ? -5.23800  11.17300  21.45300 1.000 27.75741 ? 169 ILE B N   1 
ATOM   3518 C  CA  . ILE B 1 169 ? -6.16800  10.05100  21.46300 1.000 27.97398 ? 169 ILE B CA  1 
ATOM   3519 C  C   . ILE B 1 169 ? -5.75800  9.15400   22.62400 1.000 29.11504 ? 169 ILE B C   1 
ATOM   3520 O  O   . ILE B 1 169 ? -4.76100  8.43400   22.54500 1.000 28.05490 ? 169 ILE B O   1 
ATOM   3521 C  CB  . ILE B 1 169 ? -6.16000  9.29900   20.13400 1.000 28.69116 ? 169 ILE B CB  1 
ATOM   3522 C  CG1 . ILE B 1 169 ? -6.48900  10.25300  18.98600 1.000 30.01083 ? 169 ILE B CG1 1 
ATOM   3523 C  CG2 . ILE B 1 169 ? -7.12500  8.13800   20.17700 1.000 28.07327 ? 169 ILE B CG2 1 
ATOM   3524 C  CD1 . ILE B 1 169 ? -6.52200  9.59000   17.64600 1.000 28.64682 ? 169 ILE B CD1 1 
ATOM   3525 N  N   . LEU B 1 170 ? -6.53600  9.19400   23.70500 1.000 29.78990 ? 170 LEU B N   1 
ATOM   3526 C  CA  . LEU B 1 170 ? -6.14800  8.52100   24.93700 1.000 29.91603 ? 170 LEU B CA  1 
ATOM   3527 C  C   . LEU B 1 170 ? -6.25800  7.01000   24.77900 1.000 29.30013 ? 170 LEU B C   1 
ATOM   3528 O  O   . LEU B 1 170 ? -7.20600  6.50100   24.18000 1.000 30.58869 ? 170 LEU B O   1 
ATOM   3529 C  CB  . LEU B 1 170 ? -7.01800  8.99800   26.10700 1.000 29.70119 ? 170 LEU B CB  1 
ATOM   3530 C  CG  . LEU B 1 170 ? -7.05000  10.50500  26.40800 1.000 29.62585 ? 170 LEU B CG  1 
ATOM   3531 C  CD1 . LEU B 1 170 ? -7.68000  10.77400  27.75800 1.000 32.05989 ? 170 LEU B CD1 1 
ATOM   3532 C  CD2 . LEU B 1 170 ? -5.67300  11.14000  26.34400 1.000 29.21988 ? 170 LEU B CD2 1 
ATOM   3533 N  N   . GLY B 1 171 ? -5.26900  6.29200   25.30600 1.000 29.01297 ? 171 GLY B N   1 
ATOM   3534 C  CA  . GLY B 1 171 ? -5.21600  4.85000   25.16700 1.000 28.78170 ? 171 GLY B CA  1 
ATOM   3535 C  C   . GLY B 1 171 ? -4.74300  4.33500   23.82400 1.000 28.99507 ? 171 GLY B C   1 
ATOM   3536 O  O   . GLY B 1 171 ? -4.76000  3.11800   23.61100 1.000 30.00995 ? 171 GLY B O   1 
ATOM   3537 N  N   . SER B 1 172 ? -4.30600  5.20700   22.91200 1.000 29.09654 ? 172 SER B N   1 
ATOM   3538 C  CA  . SER B 1 172 ? -3.95900  4.78300   21.55700 1.000 28.40366 ? 172 SER B CA  1 
ATOM   3539 C  C   . SER B 1 172 ? -2.56000  4.18600   21.44000 1.000 29.76267 ? 172 SER B C   1 
ATOM   3540 O  O   . SER B 1 172 ? -2.17300  3.78300   20.33900 1.000 30.60430 ? 172 SER B O   1 
ATOM   3541 C  CB  . SER B 1 172 ? -4.10400  5.94500   20.56800 1.000 26.85597 ? 172 SER B CB  1 
ATOM   3542 O  OG  . SER B 1 172 ? -3.35700  7.07100   20.96200 1.000 28.27826 ? 172 SER B OG  1 
ATOM   3543 N  N   . HIS B 1 173 ? -1.78800  4.11200   22.52500 1.000 29.24943 ? 173 HIS B N   1 
ATOM   3544 C  CA  . HIS B 1 173 ? -0.56800  3.31400   22.47200 1.000 29.55429 ? 173 HIS B CA  1 
ATOM   3545 C  C   . HIS B 1 173 ? -0.85900  1.82400   22.40500 1.000 31.06945 ? 173 HIS B C   1 
ATOM   3546 O  O   . HIS B 1 173 ? 0.06400   1.03400   22.18300 1.000 31.58619 ? 173 HIS B O   1 
ATOM   3547 C  CB  . HIS B 1 173 ? 0.31400   3.60800   23.67800 1.000 28.79906 ? 173 HIS B CB  1 
ATOM   3548 C  CG  . HIS B 1 173 ? -0.41800  3.55800   24.97600 1.000 29.76523 ? 173 HIS B CG  1 
ATOM   3549 N  ND1 . HIS B 1 173 ? -1.32300  4.52300   25.35100 1.000 30.36529 ? 173 HIS B ND1 1 
ATOM   3550 C  CD2 . HIS B 1 173 ? -0.38200  2.66200   25.98700 1.000 30.02346 ? 173 HIS B CD2 1 
ATOM   3551 C  CE1 . HIS B 1 173 ? -1.81200  4.22500   26.54100 1.000 30.50957 ? 173 HIS B CE1 1 
ATOM   3552 N  NE2 . HIS B 1 173 ? -1.25700  3.10000   26.94800 1.000 30.31892 ? 173 HIS B NE2 1 
ATOM   3553 N  N   . ARG B 1 174 ? -2.11100  1.42000   22.58400 1.000 31.52012 ? 174 ARG B N   1 
ATOM   3554 C  CA  . ARG B 1 174 ? -2.46000  0.01900   22.46000 1.000 30.53610 ? 174 ARG B CA  1 
ATOM   3555 C  C   . ARG B 1 174 ? -2.75000  -0.39700  21.02500 1.000 31.79518 ? 174 ARG B C   1 
ATOM   3556 O  O   . ARG B 1 174 ? -2.88800  -1.59700  20.76900 1.000 33.28786 ? 174 ARG B O   1 
ATOM   3557 C  CB  . ARG B 1 174 ? -3.65100  -0.29500  23.36100 1.000 31.59152 ? 174 ARG B CB  1 
ATOM   3558 C  CG  . ARG B 1 174 ? -3.25500  -0.45000  24.81300 1.000 32.09967 ? 174 ARG B CG  1 
ATOM   3559 C  CD  . ARG B 1 174 ? -4.44300  -0.87500  25.63100 1.000 36.15198 ? 174 ARG B CD  1 
ATOM   3560 N  NE  . ARG B 1 174 ? -5.35900  0.24000   25.82100 1.000 36.37989 ? 174 ARG B NE  1 
ATOM   3561 C  CZ  . ARG B 1 174 ? -5.39500  0.99200   26.91100 1.000 36.84088 ? 174 ARG B CZ  1 
ATOM   3562 N  NH1 . ARG B 1 174 ? -4.64900  0.71200   27.96600 1.000 36.85307 ? 174 ARG B NH1 1 
ATOM   3563 N  NH2 . ARG B 1 174 ? -6.19200  2.05700   26.94000 1.000 37.25212 ? 174 ARG B NH2 1 
ATOM   3564 N  N   . TRP B 1 175 ? -2.82700  0.54300   20.08500 1.000 32.62725 ? 175 TRP B N   1 
ATOM   3565 C  CA  . TRP B 1 175 ? -2.98500  0.18600   18.68000 1.000 34.53766 ? 175 TRP B CA  1 
ATOM   3566 C  C   . TRP B 1 175 ? -1.64400  -0.21300  18.08300 1.000 36.27339 ? 175 TRP B C   1 
ATOM   3567 O  O   . TRP B 1 175 ? -0.62900  0.45500   18.29600 1.000 35.85348 ? 175 TRP B O   1 
ATOM   3568 C  CB  . TRP B 1 175 ? -3.54200  1.34100   17.85300 1.000 34.04391 ? 175 TRP B CB  1 
ATOM   3569 C  CG  . TRP B 1 175 ? -4.69900  2.07800   18.41500 1.000 31.04149 ? 175 TRP B CG  1 
ATOM   3570 C  CD1 . TRP B 1 175 ? -5.44700  1.74900   19.50100 1.000 29.84393 ? 175 TRP B CD1 1 
ATOM   3571 C  CD2 . TRP B 1 175 ? -5.24000  3.29100   17.90300 1.000 31.21032 ? 175 TRP B CD2 1 
ATOM   3572 N  NE1 . TRP B 1 175 ? -6.42400  2.68900   19.69800 1.000 29.55206 ? 175 TRP B NE1 1 
ATOM   3573 C  CE2 . TRP B 1 175 ? -6.32000  3.64500   18.72400 1.000 29.70004 ? 175 TRP B CE2 1 
ATOM   3574 C  CE3 . TRP B 1 175 ? -4.91100  4.11700   16.82500 1.000 31.53681 ? 175 TRP B CE3 1 
ATOM   3575 C  CZ2 . TRP B 1 175 ? -7.07400  4.79000   18.50700 1.000 30.97711 ? 175 TRP B CZ2 1 
ATOM   3576 C  CZ3 . TRP B 1 175 ? -5.66500  5.24600   16.60200 1.000 29.92880 ? 175 TRP B CZ3 1 
ATOM   3577 C  CH2 . TRP B 1 175 ? -6.73000  5.57700   17.43900 1.000 29.53679 ? 175 TRP B CH2 1 
ATOM   3578 N  N   . THR B 1 176 ? -1.65500  -1.29400  17.30300 1.000 37.35655 ? 176 THR B N   1 
ATOM   3579 C  CA  . THR B 1 176 ? -0.45700  -1.68800  16.56600 1.000 38.90337 ? 176 THR B CA  1 
ATOM   3580 C  C   . THR B 1 176 ? -0.06700  -0.61800  15.54500 1.000 39.49400 ? 176 THR B C   1 
ATOM   3581 O  O   . THR B 1 176 ? 1.10700   -0.22700  15.45100 1.000 37.68851 ? 176 THR B O   1 
ATOM   3582 C  CB  . THR B 1 176 ? -0.68100  -3.04600  15.88700 1.000 38.67696 ? 176 THR B CB  1 
ATOM   3583 O  OG1 . THR B 1 176 ? -1.29300  -2.86200  14.60700 1.000 40.59908 ? 176 THR B OG1 1 
ATOM   3584 C  CG2 . THR B 1 176 ? -1.59600  -3.91800  16.72600 1.000 39.39002 ? 176 THR B CG2 1 
ATOM   3585 N  N   . GLU B 1 177 ? -1.04900  -0.12200  14.78400 1.000 39.75921 ? 177 GLU B N   1 
ATOM   3586 C  CA  . GLU B 1 177 ? -0.85900  0.87700   13.74200 1.000 38.18581 ? 177 GLU B CA  1 
ATOM   3587 C  C   . GLU B 1 177 ? -1.69400  2.11300   14.05300 1.000 37.64856 ? 177 GLU B C   1 
ATOM   3588 O  O   . GLU B 1 177 ? -2.65300  2.06500   14.82800 1.000 38.36530 ? 177 GLU B O   1 
ATOM   3589 C  CB  . GLU B 1 177 ? -1.25400  0.33800   12.35100 1.000 39.02237 ? 177 GLU B CB  1 
ATOM   3590 C  CG  . GLU B 1 177 ? -2.77000  0.43600   12.06800 1.000 41.86620 ? 177 GLU B CG  1 
ATOM   3591 C  CD  . GLU B 1 177 ? -3.19000  0.09900   10.62100 1.000 44.20477 ? 177 GLU B CD  1 
ATOM   3592 O  OE1 . GLU B 1 177 ? -2.58800  0.64000   9.65800  1.000 44.77343 ? 177 GLU B OE1 1 
ATOM   3593 O  OE2 . GLU B 1 177 ? -4.14700  -0.69800  10.45800 1.000 42.36114 ? 177 GLU B OE2 1 
ATOM   3594 N  N   . VAL B 1 178 ? -1.31600  3.22700   13.42400 1.000 37.63655 ? 178 VAL B N   1 
ATOM   3595 C  CA  . VAL B 1 178 ? -2.09800  4.45300   13.54000 1.000 34.71681 ? 178 VAL B CA  1 
ATOM   3596 C  C   . VAL B 1 178 ? -3.38800  4.33900   12.73700 1.000 36.99065 ? 178 VAL B C   1 
ATOM   3597 O  O   . VAL B 1 178 ? -4.48500  4.61200   13.24100 1.000 36.40789 ? 178 VAL B O   1 
ATOM   3598 C  CB  . VAL B 1 178 ? -1.26900  5.66800   13.08200 1.000 34.05546 ? 178 VAL B CB  1 
ATOM   3599 C  CG1 . VAL B 1 178 ? -2.12700  6.92200   13.09200 1.000 32.72426 ? 178 VAL B CG1 1 
ATOM   3600 C  CG2 . VAL B 1 178 ? -0.07100  5.85800   13.95600 1.000 31.59207 ? 178 VAL B CG2 1 
ATOM   3601 N  N   . GLY B 1 179 ? -3.27800  3.93700   11.47400 1.000 36.81335 ? 179 GLY B N   1 
ATOM   3602 C  CA  . GLY B 1 179 ? -4.41900  4.07100   10.59500 1.000 36.38484 ? 179 GLY B CA  1 
ATOM   3603 C  C   . GLY B 1 179 ? -4.71500  5.53900   10.35800 1.000 35.48200 ? 179 GLY B C   1 
ATOM   3604 O  O   . GLY B 1 179 ? -3.81000  6.36500   10.19700 1.000 34.36649 ? 179 GLY B O   1 
ATOM   3605 N  N   . THR B 1 180 ? -6.00300  5.87200   10.34000 1.000 35.19667 ? 180 THR B N   1 
ATOM   3606 C  CA  . THR B 1 180 ? -6.46700  7.23200   10.07300 1.000 34.21258 ? 180 THR B CA  1 
ATOM   3607 C  C   . THR B 1 180 ? -7.64300  7.52900   10.97900 1.000 34.33278 ? 180 THR B C   1 
ATOM   3608 O  O   . THR B 1 180 ? -8.80400  7.47000   10.55700 1.000 32.05076 ? 180 THR B O   1 
ATOM   3609 C  CB  . THR B 1 180 ? -6.88700  7.39200   8.61800  1.000 34.28688 ? 180 THR B CB  1 
ATOM   3610 O  OG1 . THR B 1 180 ? -7.89800  6.42600   8.34700  1.000 35.06823 ? 180 THR B OG1 1 
ATOM   3611 C  CG2 . THR B 1 180 ? -5.72300  7.15800   7.69200  1.000 34.71418 ? 180 THR B CG2 1 
ATOM   3612 N  N   . PRO B 1 181 ? -7.38500  7.82800   12.24600 1.000 34.80367 ? 181 PRO B N   1 
ATOM   3613 C  CA  . PRO B 1 181 ? -8.47500  8.22800   13.13200 1.000 33.65444 ? 181 PRO B CA  1 
ATOM   3614 C  C   . PRO B 1 181 ? -9.01900  9.58200   12.71700 1.000 35.13253 ? 181 PRO B C   1 
ATOM   3615 O  O   . PRO B 1 181 ? -8.36600  10.36100  12.02200 1.000 35.96452 ? 181 PRO B O   1 
ATOM   3616 C  CB  . PRO B 1 181 ? -7.81300  8.28700   14.50900 1.000 31.85555 ? 181 PRO B CB  1 
ATOM   3617 C  CG  . PRO B 1 181 ? -6.37900  8.47900   14.23200 1.000 30.89656 ? 181 PRO B CG  1 
ATOM   3618 C  CD  . PRO B 1 181 ? -6.09400  7.77200   12.94800 1.000 33.49837 ? 181 PRO B CD  1 
ATOM   3619 N  N   . GLU B 1 182 ? -10.24500 9.84800   13.14200 1.000 33.82372 ? 182 GLU B N   1 
ATOM   3620 C  CA  . GLU B 1 182 ? -10.89700 11.11600  12.86700 1.000 35.14738 ? 182 GLU B CA  1 
ATOM   3621 C  C   . GLU B 1 182 ? -10.68100 12.05700  14.04400 1.000 34.17554 ? 182 GLU B C   1 
ATOM   3622 O  O   . GLU B 1 182 ? -10.54500 11.61400  15.18400 1.000 34.10706 ? 182 GLU B O   1 
ATOM   3623 C  CB  . GLU B 1 182 ? -12.39300 10.90800  12.60200 1.000 38.00065 ? 182 GLU B CB  1 
ATOM   3624 C  CG  . GLU B 1 182 ? -13.10800 12.12000  11.98900 1.000 39.57932 ? 182 GLU B CG  1 
ATOM   3625 C  CD  . GLU B 1 182 ? -12.26600 12.83700  10.94000 1.000 40.03146 ? 182 GLU B CD  1 
ATOM   3626 O  OE1 . GLU B 1 182 ? -11.84000 12.18700  9.96100  1.000 41.26494 ? 182 GLU B OE1 1 
ATOM   3627 O  OE2 . GLU B 1 182 ? -12.02100 14.05000  11.10100 1.000 40.12108 ? 182 GLU B OE2 1 
ATOM   3628 N  N   . ARG B 1 183 ? -10.65200 13.36600  13.76000 1.000 36.07791 ? 183 ARG B N   1 
ATOM   3629 C  CA  . ARG B 1 183 ? -10.40300 14.36300  14.80100 1.000 35.54706 ? 183 ARG B CA  1 
ATOM   3630 C  C   . ARG B 1 183 ? -11.24000 14.14500  16.04800 1.000 34.68381 ? 183 ARG B C   1 
ATOM   3631 O  O   . ARG B 1 183 ? -10.86400 14.62400  17.12100 1.000 34.43401 ? 183 ARG B O   1 
ATOM   3632 C  CB  . ARG B 1 183 ? -10.69900 15.77700  14.30000 1.000 35.66800 ? 183 ARG B CB  1 
ATOM   3633 C  CG  . ARG B 1 183 ? -9.81500  16.27400  13.20400 1.000 35.35898 ? 183 ARG B CG  1 
ATOM   3634 C  CD  . ARG B 1 183 ? -8.40900  16.44000  13.65900 1.000 33.06722 ? 183 ARG B CD  1 
ATOM   3635 N  NE  . ARG B 1 183 ? -7.53000  16.41200  12.50300 1.000 34.54930 ? 183 ARG B NE  1 
ATOM   3636 C  CZ  . ARG B 1 183 ? -6.20800  16.43400  12.56400 1.000 32.82530 ? 183 ARG B CZ  1 
ATOM   3637 N  NH1 . ARG B 1 183 ? -5.57100  16.52500  13.71500 1.000 30.39268 ? 183 ARG B NH1 1 
ATOM   3638 N  NH2 . ARG B 1 183 ? -5.50900  16.36000  11.43700 1.000 33.97277 ? 183 ARG B NH2 1 
ATOM   3639 N  N   . ASP B 1 184 ? -12.36900 13.44800  15.92800 1.000 35.55969 ? 184 ASP B N   1 
ATOM   3640 C  CA  . ASP B 1 184 ? -13.37400 13.34400  16.97500 1.000 33.93201 ? 184 ASP B CA  1 
ATOM   3641 C  C   . ASP B 1 184 ? -13.10700 12.20700  17.96100 1.000 33.77318 ? 184 ASP B C   1 
ATOM   3642 O  O   . ASP B 1 184 ? -13.76200 12.14500  19.00800 1.000 33.40095 ? 184 ASP B O   1 
ATOM   3643 C  CB  . ASP B 1 184 ? -14.75000 13.19200  16.32100 1.000 34.28047 ? 184 ASP B CB  1 
ATOM   3644 C  CG  . ASP B 1 184 ? -14.94800 14.15700  15.14500 1.000 37.34815 ? 184 ASP B CG  1 
ATOM   3645 O  OD1 . ASP B 1 184 ? -15.18600 15.37100  15.37200 1.000 37.49707 ? 184 ASP B OD1 1 
ATOM   3646 O  OD2 . ASP B 1 184 ? -14.83800 13.70000  13.98500 1.000 38.11255 ? 184 ASP B OD2 1 
ATOM   3647 N  N   . GLN B 1 185 ? -12.14200 11.33000  17.66900 1.000 33.60128 ? 185 GLN B N   1 
ATOM   3648 C  CA  . GLN B 1 185 ? -11.69700 10.32600  18.62200 1.000 32.86029 ? 185 GLN B CA  1 
ATOM   3649 C  C   . GLN B 1 185 ? -10.71500 10.87600  19.64500 1.000 31.80796 ? 185 GLN B C   1 
ATOM   3650 O  O   . GLN B 1 185 ? -10.36700 10.15900  20.58800 1.000 31.01618 ? 185 GLN B O   1 
ATOM   3651 C  CB  . GLN B 1 185 ? -11.04400 9.15600   17.88500 1.000 32.72323 ? 185 GLN B CB  1 
ATOM   3652 C  CG  . GLN B 1 185 ? -11.70300 8.80400   16.56700 1.000 34.06729 ? 185 GLN B CG  1 
ATOM   3653 C  CD  . GLN B 1 185 ? -11.21700 7.48300   16.00100 1.000 34.64664 ? 185 GLN B CD  1 
ATOM   3654 O  OE1 . GLN B 1 185 ? -11.37400 7.21000   14.81100 1.000 36.19758 ? 185 GLN B OE1 1 
ATOM   3655 N  NE2 . GLN B 1 185 ? -10.63600 6.65100   16.85500 1.000 33.16647 ? 185 GLN B NE2 1 
ATOM   3656 N  N   . ALA B 1 186 ? -10.26000 12.11600  19.48300 1.000 33.74560 ? 186 ALA B N   1 
ATOM   3657 C  CA  . ALA B 1 186 ? -9.23300  12.71700  20.32000 1.000 32.75258 ? 186 ALA B CA  1 
ATOM   3658 C  C   . ALA B 1 186 ? -9.84700  13.71900  21.28800 1.000 32.74678 ? 186 ALA B C   1 
ATOM   3659 O  O   . ALA B 1 186 ? -11.00300 14.12800  21.14800 1.000 33.76994 ? 186 ALA B O   1 
ATOM   3660 C  CB  . ALA B 1 186 ? -8.16900  13.40400  19.46200 1.000 30.32140 ? 186 ALA B CB  1 
ATOM   3661 N  N   . VAL B 1 187 ? -9.04400  14.10400  22.28500 1.000 31.04355 ? 187 VAL B N   1 
ATOM   3662 C  CA  . VAL B 1 187 ? -9.37400  15.16900  23.22000 1.000 31.23100 ? 187 VAL B CA  1 
ATOM   3663 C  C   . VAL B 1 187 ? -8.29600  16.23700  23.13500 1.000 31.57796 ? 187 VAL B C   1 
ATOM   3664 O  O   . VAL B 1 187 ? -7.15600  15.97900  22.74100 1.000 30.42637 ? 187 VAL B O   1 
ATOM   3665 C  CB  . VAL B 1 187 ? -9.51500  14.66600  24.66400 1.000 32.41778 ? 187 VAL B CB  1 
ATOM   3666 C  CG1 . VAL B 1 187 ? -10.76700 13.84300  24.80100 1.000 33.42420 ? 187 VAL B CG1 1 
ATOM   3667 C  CG2 . VAL B 1 187 ? -8.27500  13.85700  25.07100 1.000 30.93742 ? 187 VAL B CG2 1 
ATOM   3668 N  N   . LEU B 1 188 ? -8.67700  17.45000  23.52400 1.000 31.12326 ? 188 LEU B N   1 
ATOM   3669 C  CA  . LEU B 1 188 ? -7.83800  18.63500  23.44200 1.000 30.22836 ? 188 LEU B CA  1 
ATOM   3670 C  C   . LEU B 1 188 ? -6.93300  18.74300  24.65600 1.000 30.07765 ? 188 LEU B C   1 
ATOM   3671 O  O   . LEU B 1 188 ? -7.27300  18.29800  25.75500 1.000 32.01801 ? 188 LEU B O   1 
ATOM   3672 C  CB  . LEU B 1 188 ? -8.69500  19.89900  23.35200 1.000 31.61377 ? 188 LEU B CB  1 
ATOM   3673 C  CG  . LEU B 1 188 ? -9.85900  19.90000  22.36900 1.000 30.32364 ? 188 LEU B CG  1 
ATOM   3674 C  CD1 . LEU B 1 188 ? -10.47800 21.27000  22.33900 1.000 34.99224 ? 188 LEU B CD1 1 
ATOM   3675 C  CD2 . LEU B 1 188 ? -9.36400  19.51300  20.99900 1.000 31.11640 ? 188 LEU B CD2 1 
ATOM   3676 N  N   . ALA B 1 189 ? -5.78800  19.38400  24.46000 1.000 29.88133 ? 189 ALA B N   1 
ATOM   3677 C  CA  . ALA B 1 189 ? -4.88300  19.63900  25.57300 1.000 31.07966 ? 189 ALA B CA  1 
ATOM   3678 C  C   . ALA B 1 189 ? -4.80600  21.13200  25.88000 1.000 30.34807 ? 189 ALA B C   1 
ATOM   3679 O  O   . ALA B 1 189 ? -3.74200  21.73500  25.74100 1.000 31.69909 ? 189 ALA B O   1 
ATOM   3680 C  CB  . ALA B 1 189 ? -3.49000  19.07700  25.26500 1.000 28.77338 ? 189 ALA B CB  1 
ATOM   3681 N  N   . THR B 1 190 ? -5.91800  21.74000  26.29500 1.000 31.16222 ? 190 THR B N   1 
ATOM   3682 C  CA  . THR B 1 190 ? -5.90100  23.15600  26.63900 1.000 32.15892 ? 190 THR B CA  1 
ATOM   3683 C  C   . THR B 1 190 ? -5.06300  23.37100  27.89100 1.000 32.25548 ? 190 THR B C   1 
ATOM   3684 O  O   . THR B 1 190 ? -5.15300  22.60800  28.85800 1.000 32.67721 ? 190 THR B O   1 
ATOM   3685 C  CB  . THR B 1 190 ? -7.32400  23.70100  26.85000 1.000 33.29108 ? 190 THR B CB  1 
ATOM   3686 O  OG1 . THR B 1 190 ? -8.00600  22.93300  27.85700 1.000 32.97955 ? 190 THR B OG1 1 
ATOM   3687 C  CG2 . THR B 1 190 ? -8.11500  23.67500  25.54000 1.000 31.25048 ? 190 THR B CG2 1 
ATOM   3688 N  N   . MET B 1 191 ? -4.23600  24.41600  27.86200 1.000 31.79135 ? 191 MET B N   1 
ATOM   3689 C  CA  . MET B 1 191 ? -3.21900  24.64700  28.87400 1.000 32.10731 ? 191 MET B CA  1 
ATOM   3690 C  C   . MET B 1 191 ? -2.91800  26.13600  28.93900 1.000 33.47927 ? 191 MET B C   1 
ATOM   3691 O  O   . MET B 1 191 ? -3.16200  26.88200  27.98900 1.000 32.17492 ? 191 MET B O   1 
ATOM   3692 C  CB  . MET B 1 191 ? -1.92200  23.87400  28.57000 1.000 31.05355 ? 191 MET B CB  1 
ATOM   3693 C  CG  . MET B 1 191 ? -2.05900  22.35400  28.56000 1.000 29.96124 ? 191 MET B CG  1 
ATOM   3694 S  SD  . MET B 1 191 ? -0.53700  21.47300  28.20500 1.000 28.72579 ? 191 MET B SD  1 
ATOM   3695 C  CE  . MET B 1 191 ? -0.37800  21.62700  26.43900 1.000 27.29447 ? 191 MET B CE  1 
ATOM   3696 N  N   . ASP B 1 192 ? -2.38000  26.56300  30.09100 1.000 33.30198 ? 192 ASP B N   1 
ATOM   3697 C  CA  . ASP B 1 192 ? -1.79800  27.87100  30.33900 1.000 32.60911 ? 192 ASP B CA  1 
ATOM   3698 C  C   . ASP B 1 192 ? -0.29600  27.81500  30.07000 1.000 32.43646 ? 192 ASP B C   1 
ATOM   3699 O  O   . ASP B 1 192 ? 0.32500   26.76100  30.24700 1.000 31.17337 ? 192 ASP B O   1 
ATOM   3700 C  CB  . ASP B 1 192 ? -2.03700  28.30100  31.78700 1.000 32.64859 ? 192 ASP B CB  1 
ATOM   3701 C  CG  . ASP B 1 192 ? -3.50300  28.51000  32.10800 1.000 34.95878 ? 192 ASP B CG  1 
ATOM   3702 O  OD1 . ASP B 1 192 ? -4.18200  29.23200  31.34600 1.000 35.56312 ? 192 ASP B OD1 1 
ATOM   3703 O  OD2 . ASP B 1 192 ? -3.97400  27.94600  33.12300 1.000 35.72168 ? 192 ASP B OD2 1 
ATOM   3704 N  N   . PRO B 1 193 ? 0.31600   28.91500  29.61900 1.000 33.39876 ? 193 PRO B N   1 
ATOM   3705 C  CA  . PRO B 1 193 ? 1.78100   28.95900  29.55500 1.000 31.08977 ? 193 PRO B CA  1 
ATOM   3706 C  C   . PRO B 1 193 ? 2.36800   28.64700  30.92200 1.000 32.04253 ? 193 PRO B C   1 
ATOM   3707 O  O   . PRO B 1 193 ? 1.87200   29.11200  31.95100 1.000 32.07699 ? 193 PRO B O   1 
ATOM   3708 C  CB  . PRO B 1 193 ? 2.07600   30.39600  29.11800 1.000 31.79067 ? 193 PRO B CB  1 
ATOM   3709 C  CG  . PRO B 1 193 ? 0.86700   30.81800  28.39000 1.000 32.34180 ? 193 PRO B CG  1 
ATOM   3710 C  CD  . PRO B 1 193 ? -0.29400  30.13900  29.07100 1.000 32.69166 ? 193 PRO B CD  1 
ATOM   3711 N  N   . GLY B 1 194 ? 3.41100   27.82000  30.93200 1.000 31.38388 ? 194 GLY B N   1 
ATOM   3712 C  CA  . GLY B 1 194 ? 3.93800   27.25400  32.14800 1.000 32.01657 ? 194 GLY B CA  1 
ATOM   3713 C  C   . GLY B 1 194 ? 3.46500   25.84300  32.43900 1.000 31.24411 ? 194 GLY B C   1 
ATOM   3714 O  O   . GLY B 1 194 ? 4.09400   25.15000  33.24400 1.000 32.01650 ? 194 GLY B O   1 
ATOM   3715 N  N   . ASP B 1 195 ? 2.36300   25.41500  31.83300 1.000 29.95945 ? 195 ASP B N   1 
ATOM   3716 C  CA  . ASP B 1 195 ? 1.93000   24.03500  31.92700 1.000 30.46518 ? 195 ASP B CA  1 
ATOM   3717 C  C   . ASP B 1 195 ? 2.77600   23.16000  31.01100 1.000 29.36405 ? 195 ASP B C   1 
ATOM   3718 O  O   . ASP B 1 195 ? 3.53100   23.64800  30.16800 1.000 29.67402 ? 195 ASP B O   1 
ATOM   3719 C  CB  . ASP B 1 195 ? 0.46400   23.89800  31.54100 1.000 30.41391 ? 195 ASP B CB  1 
ATOM   3720 C  CG  . ASP B 1 195 ? -0.43900  24.68400  32.43400 1.000 32.59957 ? 195 ASP B CG  1 
ATOM   3721 O  OD1 . ASP B 1 195 ? 0.06400   25.21800  33.44300 1.000 34.29988 ? 195 ASP B OD1 1 
ATOM   3722 O  OD2 . ASP B 1 195 ? -1.64500  24.76400  32.12600 1.000 32.20510 ? 195 ASP B OD2 1 
ATOM   3723 N  N   . VAL B 1 196 ? 2.64300   21.84600  31.18200 1.000 29.05485 ? 196 VAL B N   1 
ATOM   3724 C  CA  . VAL B 1 196 ? 3.33300   20.87000  30.34700 1.000 27.88906 ? 196 VAL B CA  1 
ATOM   3725 C  C   . VAL B 1 196 ? 2.38500   19.71600  30.04800 1.000 28.24619 ? 196 VAL B C   1 
ATOM   3726 O  O   . VAL B 1 196 ? 1.56000   19.34300  30.88700 1.000 29.39993 ? 196 VAL B O   1 
ATOM   3727 C  CB  . VAL B 1 196 ? 4.61600   20.33500  31.00900 1.000 26.88326 ? 196 VAL B CB  1 
ATOM   3728 C  CG1 . VAL B 1 196 ? 5.45000   19.63700  29.98200 1.000 26.24588 ? 196 VAL B CG1 1 
ATOM   3729 C  CG2 . VAL B 1 196 ? 5.41600   21.44900  31.61000 1.000 29.65616 ? 196 VAL B CG2 1 
ATOM   3730 N  N   . LEU B 1 197 ? 2.50800   19.15600  28.84500 1.000 26.28521 ? 197 LEU B N   1 
ATOM   3731 C  CA  . LEU B 1 197 ? 1.78600   17.96400  28.42700 1.000 25.26851 ? 197 LEU B CA  1 
ATOM   3732 C  C   . LEU B 1 197 ? 2.80300   16.87000  28.14500 1.000 25.48060 ? 197 LEU B C   1 
ATOM   3733 O  O   . LEU B 1 197 ? 3.67700   17.04100  27.29200 1.000 26.35123 ? 197 LEU B O   1 
ATOM   3734 C  CB  . LEU B 1 197 ? 0.94800   18.25200  27.18500 1.000 25.72494 ? 197 LEU B CB  1 
ATOM   3735 C  CG  . LEU B 1 197 ? 0.44800   17.06900  26.36800 1.000 25.07698 ? 197 LEU B CG  1 
ATOM   3736 C  CD1 . LEU B 1 197 ? -0.63000  16.31800  27.10600 1.000 25.37661 ? 197 LEU B CD1 1 
ATOM   3737 C  CD2 . LEU B 1 197 ? -0.06700  17.56200  25.04900 1.000 23.83131 ? 197 LEU B CD2 1 
ATOM   3738 N  N   . ILE B 1 198 ? 2.70000   15.76000  28.86000 1.000 24.59118 ? 198 ILE B N   1 
ATOM   3739 C  CA  . ILE B 1 198 ? 3.59500   14.62300  28.67600 1.000 24.76487 ? 198 ILE B CA  1 
ATOM   3740 C  C   . ILE B 1 198 ? 2.86300   13.56000  27.87600 1.000 23.85967 ? 198 ILE B C   1 
ATOM   3741 O  O   . ILE B 1 198 ? 1.69000   13.28500  28.13100 1.000 24.55642 ? 198 ILE B O   1 
ATOM   3742 C  CB  . ILE B 1 198 ? 4.06200   14.06000  30.02900 1.000 24.77248 ? 198 ILE B CB  1 
ATOM   3743 C  CG1 . ILE B 1 198 ? 4.41200   15.19400  30.98900 1.000 26.31021 ? 198 ILE B CG1 1 
ATOM   3744 C  CG2 . ILE B 1 198 ? 5.25900   13.16700  29.83700 1.000 25.02810 ? 198 ILE B CG2 1 
ATOM   3745 C  CD1 . ILE B 1 198 ? 5.57500   16.04300  30.53200 1.000 24.29228 ? 198 ILE B CD1 1 
ATOM   3746 N  N   . VAL B 1 199 ? 3.54900   12.94800  26.91700 1.000 23.58140 ? 199 VAL B N   1 
ATOM   3747 C  CA  . VAL B 1 199 ? 2.93500   11.97300  26.02700 1.000 23.39075 ? 199 VAL B CA  1 
ATOM   3748 C  C   . VAL B 1 199 ? 3.81500   10.73200  25.95400 1.000 23.98915 ? 199 VAL B C   1 
ATOM   3749 O  O   . VAL B 1 199 ? 5.01300   10.83100  25.66300 1.000 24.62127 ? 199 VAL B O   1 
ATOM   3750 C  CB  . VAL B 1 199 ? 2.69800   12.56200  24.62400 1.000 24.45414 ? 199 VAL B CB  1 
ATOM   3751 C  CG1 . VAL B 1 199 ? 2.08600   11.52400  23.70600 1.000 24.90055 ? 199 VAL B CG1 1 
ATOM   3752 C  CG2 . VAL B 1 199 ? 1.80800   13.79300  24.70200 1.000 23.53006 ? 199 VAL B CG2 1 
ATOM   3753 N  N   . ARG B 1 200 ? 3.20900   9.57000   26.21600 1.000 24.59020 ? 200 ARG B N   1 
ATOM   3754 C  CA  . ARG B 1 200 ? 3.88700   8.28100   26.20800 1.000 24.76949 ? 200 ARG B CA  1 
ATOM   3755 C  C   . ARG B 1 200 ? 4.20400   7.83600   24.78300 1.000 25.93692 ? 200 ARG B C   1 
ATOM   3756 O  O   . ARG B 1 200 ? 3.52300   8.21100   23.82600 1.000 25.60272 ? 200 ARG B O   1 
ATOM   3757 C  CB  . ARG B 1 200 ? 3.00900   7.22500   26.88000 1.000 25.54281 ? 200 ARG B CB  1 
ATOM   3758 C  CG  . ARG B 1 200 ? 3.66700   5.86900   27.05000 1.000 26.51485 ? 200 ARG B CG  1 
ATOM   3759 C  CD  . ARG B 1 200 ? 2.68200   4.73400   26.85300 1.000 27.60472 ? 200 ARG B CD  1 
ATOM   3760 N  NE  . ARG B 1 200 ? 3.28900   3.43100   27.10600 1.000 29.66883 ? 200 ARG B NE  1 
ATOM   3761 C  CZ  . ARG B 1 200 ? 3.88900   2.68700   26.18400 1.000 29.77122 ? 200 ARG B CZ  1 
ATOM   3762 N  NH1 . ARG B 1 200 ? 3.96600   3.07700   24.92200 1.000 26.38292 ? 200 ARG B NH1 1 
ATOM   3763 N  NH2 . ARG B 1 200 ? 4.42100   1.51900   26.53700 1.000 30.73672 ? 200 ARG B NH2 1 
ATOM   3764 N  N   . GLN B 1 201 ? 5.24500   7.01700   24.64600 1.000 24.99037 ? 201 GLN B N   1 
ATOM   3765 C  CA  . GLN B 1 201 ? 5.54300   6.41300   23.35500 1.000 25.28403 ? 201 GLN B CA  1 
ATOM   3766 C  C   . GLN B 1 201 ? 4.33100   5.65100   22.82800 1.000 26.18819 ? 201 GLN B C   1 
ATOM   3767 O  O   . GLN B 1 201 ? 3.62000   4.99400   23.59000 1.000 27.81724 ? 201 GLN B O   1 
ATOM   3768 C  CB  . GLN B 1 201 ? 6.73300   5.46900   23.47900 1.000 25.26150 ? 201 GLN B CB  1 
ATOM   3769 C  CG  . GLN B 1 201 ? 6.93800   4.60900   22.25600 1.000 26.61201 ? 201 GLN B CG  1 
ATOM   3770 C  CD  . GLN B 1 201 ? 8.09800   3.67600   22.40400 1.000 25.89395 ? 201 GLN B CD  1 
ATOM   3771 O  OE1 . GLN B 1 201 ? 8.97400   3.90100   23.23400 1.000 25.02204 ? 201 GLN B OE1 1 
ATOM   3772 N  NE2 . GLN B 1 201 ? 8.11800   2.61500   21.60200 1.000 26.90618 ? 201 GLN B NE2 1 
ATOM   3773 N  N   . ARG B 1 202 ? 4.09300   5.75500   21.51800 1.000 25.23794 ? 202 ARG B N   1 
ATOM   3774 C  CA  . ARG B 1 202 ? 3.04100   5.08400   20.74300 1.000 24.89303 ? 202 ARG B CA  1 
ATOM   3775 C  C   . ARG B 1 202 ? 1.67300   5.74600   20.85600 1.000 26.75302 ? 202 ARG B C   1 
ATOM   3776 O  O   . ARG B 1 202 ? 0.69800   5.15900   20.37000 1.000 26.66597 ? 202 ARG B O   1 
ATOM   3777 C  CB  . ARG B 1 202 ? 2.85300   3.60600   21.10700 1.000 26.87856 ? 202 ARG B CB  1 
ATOM   3778 C  CG  . ARG B 1 202 ? 4.01200   2.69100   20.79500 1.000 28.43867 ? 202 ARG B CG  1 
ATOM   3779 C  CD  . ARG B 1 202 ? 3.62400   1.23400   21.05600 1.000 30.83826 ? 202 ARG B CD  1 
ATOM   3780 N  NE  . ARG B 1 202 ? 2.64800   0.78300   20.07500 1.000 32.93125 ? 202 ARG B NE  1 
ATOM   3781 C  CZ  . ARG B 1 202 ? 2.94700   0.05500   19.00700 1.000 36.01250 ? 202 ARG B CZ  1 
ATOM   3782 N  NH1 . ARG B 1 202 ? 4.17000   -0.41000  18.81000 1.000 36.24007 ? 202 ARG B NH1 1 
ATOM   3783 N  NH2 . ARG B 1 202 ? 1.99500   -0.21100  18.11300 1.000 36.39455 ? 202 ARG B NH2 1 
ATOM   3784 N  N   . VAL B 1 203 ? 1.55600   6.93800   21.44700 1.000 28.12701 ? 203 VAL B N   1 
ATOM   3785 C  CA  . VAL B 1 203 ? 0.26000   7.59300   21.62800 1.000 26.83099 ? 203 VAL B CA  1 
ATOM   3786 C  C   . VAL B 1 203 ? -0.00200  8.55400   20.47100 1.000 27.40168 ? 203 VAL B C   1 
ATOM   3787 O  O   . VAL B 1 203 ? 0.81700   9.43300   20.17700 1.000 26.68326 ? 203 VAL B O   1 
ATOM   3788 C  CB  . VAL B 1 203 ? 0.19800   8.32300   22.97700 1.000 26.07207 ? 203 VAL B CB  1 
ATOM   3789 C  CG1 . VAL B 1 203 ? -1.06200  9.15600   23.06100 1.000 25.73752 ? 203 VAL B CG1 1 
ATOM   3790 C  CG2 . VAL B 1 203 ? 0.24300   7.30800   24.10600 1.000 26.97957 ? 203 VAL B CG2 1 
ATOM   3791 N  N   . VAL B 1 204 ? -1.15700  8.39700   19.82500 1.000 27.80267 ? 204 VAL B N   1 
ATOM   3792 C  CA  . VAL B 1 204 ? -1.46900  9.15100   18.61600 1.000 26.88170 ? 204 VAL B CA  1 
ATOM   3793 C  C   . VAL B 1 204 ? -1.94500  10.54600  18.99200 1.000 27.18672 ? 204 VAL B C   1 
ATOM   3794 O  O   . VAL B 1 204 ? -2.82200  10.71300  19.84600 1.000 27.79028 ? 204 VAL B O   1 
ATOM   3795 C  CB  . VAL B 1 204 ? -2.51500  8.40400   17.77400 1.000 26.45388 ? 204 VAL B CB  1 
ATOM   3796 C  CG1 . VAL B 1 204 ? -3.08500  9.30800   16.72400 1.000 26.79996 ? 204 VAL B CG1 1 
ATOM   3797 C  CG2 . VAL B 1 204 ? -1.87600  7.20400   17.12400 1.000 27.89808 ? 204 VAL B CG2 1 
ATOM   3798 N  N   . HIS B 1 205 ? -1.37500  11.55700  18.35100 1.000 26.65992 ? 205 HIS B N   1 
ATOM   3799 C  CA  . HIS B 1 205 ? -1.72000  12.92200  18.68900 1.000 26.92239 ? 205 HIS B CA  1 
ATOM   3800 C  C   . HIS B 1 205 ? -1.48300  13.79900  17.47300 1.000 27.61014 ? 205 HIS B C   1 
ATOM   3801 O  O   . HIS B 1 205 ? -0.84200  13.39100  16.50500 1.000 27.00798 ? 205 HIS B O   1 
ATOM   3802 C  CB  . HIS B 1 205 ? -0.90100  13.41200  19.87000 1.000 26.70408 ? 205 HIS B CB  1 
ATOM   3803 C  CG  . HIS B 1 205 ? 0.56200   13.41000  19.59700 1.000 27.90235 ? 205 HIS B CG  1 
ATOM   3804 N  ND1 . HIS B 1 205 ? 1.29200   12.24800  19.48700 1.000 27.50054 ? 205 HIS B ND1 1 
ATOM   3805 C  CD2 . HIS B 1 205 ? 1.42400   14.42100  19.35000 1.000 28.59516 ? 205 HIS B CD2 1 
ATOM   3806 C  CE1 . HIS B 1 205 ? 2.54700   12.54600  19.21000 1.000 28.22106 ? 205 HIS B CE1 1 
ATOM   3807 N  NE2 . HIS B 1 205 ? 2.65500   13.85800  19.12200 1.000 28.82468 ? 205 HIS B NE2 1 
ATOM   3808 N  N   . ALA B 1 206 ? -1.99900  15.02600  17.54300 1.000 29.05562 ? 206 ALA B N   1 
ATOM   3809 C  CA  . ALA B 1 206 ? -1.93800  15.95500  16.41900 1.000 28.68359 ? 206 ALA B CA  1 
ATOM   3810 C  C   . ALA B 1 206 ? -2.18700  17.36600  16.91900 1.000 29.29033 ? 206 ALA B C   1 
ATOM   3811 O  O   . ALA B 1 206 ? -3.18100  17.60900  17.60400 1.000 29.10002 ? 206 ALA B O   1 
ATOM   3812 C  CB  . ALA B 1 206 ? -2.97400  15.60700  15.35100 1.000 29.20637 ? 206 ALA B CB  1 
ATOM   3813 N  N   . GLY B 1 207 ? -1.28800  18.28600  16.57500 1.000 30.89000 ? 207 GLY B N   1 
ATOM   3814 C  CA  . GLY B 1 207 ? -1.58700  19.69600  16.72800 1.000 31.40756 ? 207 GLY B CA  1 
ATOM   3815 C  C   . GLY B 1 207 ? -2.82600  20.08900  15.95300 1.000 32.51437 ? 207 GLY B C   1 
ATOM   3816 O  O   . GLY B 1 207 ? -3.19500  19.45800  14.96700 1.000 32.01482 ? 207 GLY B O   1 
ATOM   3817 N  N   . GLY B 1 208 ? -3.48000  21.15000  16.41400 1.000 35.80754 ? 208 GLY B N   1 
ATOM   3818 C  CA  . GLY B 1 208 ? -4.73200  21.56800  15.82300 1.000 39.06535 ? 208 GLY B CA  1 
ATOM   3819 C  C   . GLY B 1 208 ? -4.67500  22.71300  14.84600 1.000 42.64604 ? 208 GLY B C   1 
ATOM   3820 O  O   . GLY B 1 208 ? -5.71400  23.07400  14.28900 1.000 43.77080 ? 208 GLY B O   1 
ATOM   3821 N  N   . GLY B 1 209 ? -3.50300  23.29000  14.60300 1.000 58.68593 ? 209 GLY B N   1 
ATOM   3822 C  CA  . GLY B 1 209 ? -3.42400  24.41500  13.69200 1.000 59.02460 ? 209 GLY B CA  1 
ATOM   3823 C  C   . GLY B 1 209 ? -3.79400  25.71200  14.37900 1.000 58.66914 ? 209 GLY B C   1 
ATOM   3824 O  O   . GLY B 1 209 ? -3.40700  25.91900  15.53200 1.000 57.86595 ? 209 GLY B O   1 
ATOM   3825 N  N   . ASN B 1 210 ? -4.53200  26.58800  13.69200 1.000 53.15536 ? 210 ASN B N   1 
ATOM   3826 C  CA  . ASN B 1 210 ? -4.97300  27.83800  14.29200 1.000 53.18012 ? 210 ASN B CA  1 
ATOM   3827 C  C   . ASN B 1 210 ? -6.04500  28.46800  13.42000 1.000 54.52367 ? 210 ASN B C   1 
ATOM   3828 O  O   . ASN B 1 210 ? -5.77900  29.41500  12.67800 1.000 55.18878 ? 210 ASN B O   1 
ATOM   3829 C  CB  . ASN B 1 210 ? -3.80100  28.80200  14.48600 1.000 52.76664 ? 210 ASN B CB  1 
ATOM   3830 C  CG  . ASN B 1 210 ? -4.17800  30.01600  15.30400 1.000 53.01430 ? 210 ASN B CG  1 
ATOM   3831 O  OD1 . ASN B 1 210 ? -5.32900  30.17300  15.69200 1.000 53.49152 ? 210 ASN B OD1 1 
ATOM   3832 N  ND2 . ASN B 1 210 ? -3.21000  30.87700  15.57800 1.000 53.06815 ? 210 ASN B ND2 1 
ATOM   3833 N  N   . ARG B 1 211 ? -7.27000  27.96000  13.52200 1.000 60.04947 ? 211 ARG B N   1 
ATOM   3834 C  CA  . ARG B 1 211 ? -8.35700  28.38600  12.64800 1.000 61.64312 ? 211 ARG B CA  1 
ATOM   3835 C  C   . ARG B 1 211 ? -8.74400  29.84800  12.86700 1.000 62.06566 ? 211 ARG B C   1 
ATOM   3836 O  O   . ARG B 1 211 ? -9.54800  30.38100  12.09700 1.000 63.55010 ? 211 ARG B O   1 
ATOM   3837 C  CB  . ARG B 1 211 ? -9.55400  27.44400  12.86600 1.000 63.57730 ? 211 ARG B CB  1 
ATOM   3838 C  CG  . ARG B 1 211 ? -10.79200 27.70300  12.02300 1.000 71.62298 ? 211 ARG B CG  1 
ATOM   3839 C  CD  . ARG B 1 211 ? -10.53900 27.56900  10.53600 1.000 71.37902 ? 211 ARG B CD  1 
ATOM   3840 N  NE  . ARG B 1 211 ? -11.79600 27.53400  9.79500  1.000 73.72203 ? 211 ARG B NE  1 
ATOM   3841 C  CZ  . ARG B 1 211 ? -12.46100 28.60500  9.37900  1.000 75.80411 ? 211 ARG B CZ  1 
ATOM   3842 N  NH1 . ARG B 1 211 ? -12.02900 29.83100  9.63400  1.000 75.40986 ? 211 ARG B NH1 1 
ATOM   3843 N  NH2 . ARG B 1 211 ? -13.58500 28.44300  8.68500  1.000 76.59305 ? 211 ARG B NH2 1 
ATOM   3844 N  N   . THR B 1 212 ? -8.16900  30.51400  13.87300 1.000 59.71274 ? 212 THR B N   1 
ATOM   3845 C  CA  . THR B 1 212 ? -8.49900  31.89700  14.18900 1.000 58.84588 ? 212 THR B CA  1 
ATOM   3846 C  C   . THR B 1 212 ? -8.19500  32.84100  13.03700 1.000 58.66329 ? 212 THR B C   1 
ATOM   3847 O  O   . THR B 1 212 ? -7.71300  32.43200  11.97800 1.000 58.28765 ? 212 THR B O   1 
ATOM   3848 C  CB  . THR B 1 212 ? -7.74700  32.38600  15.43800 1.000 57.88405 ? 212 THR B CB  1 
ATOM   3849 O  OG1 . THR B 1 212 ? -6.32700  32.30000  15.22600 1.000 56.17353 ? 212 THR B OG1 1 
ATOM   3850 C  CG2 . THR B 1 212 ? -8.13900  31.56600  16.65200 1.000 55.95087 ? 212 THR B CG2 1 
ATOM   3851 N  N   . THR B 1 213 ? -8.48800  34.11800  13.24300 1.000 63.01418 ? 213 THR B N   1 
ATOM   3852 C  CA  . THR B 1 213 ? -8.29200  35.14800  12.23400 1.000 65.66748 ? 213 THR B CA  1 
ATOM   3853 C  C   . THR B 1 213 ? -7.36100  36.24000  12.72500 1.000 67.10632 ? 213 THR B C   1 
ATOM   3854 O  O   . THR B 1 213 ? -6.41200  36.60400  12.01900 1.000 66.27819 ? 213 THR B O   1 
ATOM   3855 C  CB  . THR B 1 213 ? -9.64500  35.74900  11.82000 1.000 66.75430 ? 213 THR B CB  1 
ATOM   3856 O  OG1 . THR B 1 213 ? -10.32700 36.24900  12.98400 1.000 66.40763 ? 213 THR B OG1 1 
ATOM   3857 C  CG2 . THR B 1 213 ? -10.52600 34.70400  11.13200 1.000 64.81230 ? 213 THR B CG2 1 
ATOM   3858 N  N   . ALA B 1 214 ? -7.61200  36.77100  13.92200 1.000 69.26635 ? 214 ALA B N   1 
ATOM   3859 C  CA  . ALA B 1 214 ? -6.76900  37.81700  14.48000 1.000 72.24205 ? 214 ALA B CA  1 
ATOM   3860 C  C   . ALA B 1 214 ? -5.38100  37.26700  14.79900 1.000 72.89772 ? 214 ALA B C   1 
ATOM   3861 O  O   . ALA B 1 214 ? -5.20800  36.08800  15.12300 1.000 68.59049 ? 214 ALA B O   1 
ATOM   3862 C  CB  . ALA B 1 214 ? -7.40600  38.41900  15.73100 1.000 74.51941 ? 214 ALA B CB  1 
ATOM   3863 N  N   . GLY B 1 215 ? -4.38600  38.14200  14.70900 1.000 83.83085 ? 215 GLY B N   1 
ATOM   3864 C  CA  . GLY B 1 215 ? -3.00600  37.71200  14.76900 1.000 82.50572 ? 215 GLY B CA  1 
ATOM   3865 C  C   . GLY B 1 215 ? -2.50300  37.31800  16.14100 1.000 79.16805 ? 215 GLY B C   1 
ATOM   3866 O  O   . GLY B 1 215 ? -1.91400  38.13600  16.85400 1.000 84.09569 ? 215 GLY B O   1 
ATOM   3867 N  N   . LYS B 1 216 ? -2.71200  36.06000  16.52100 1.000 64.18030 ? 216 LYS B N   1 
ATOM   3868 C  CA  . LYS B 1 216 ? -2.12500  35.51400  17.74100 1.000 57.44185 ? 216 LYS B CA  1 
ATOM   3869 C  C   . LYS B 1 216 ? -1.61500  34.11600  17.42800 1.000 55.21087 ? 216 LYS B C   1 
ATOM   3870 O  O   . LYS B 1 216 ? -2.41000  33.16800  17.32100 1.000 54.26709 ? 216 LYS B O   1 
ATOM   3871 C  CB  . LYS B 1 216 ? -3.12800  35.50000  18.89000 1.000 59.33981 ? 216 LYS B CB  1 
ATOM   3872 C  CG  . LYS B 1 216 ? -3.55200  36.88800  19.34100 1.000 62.80000 ? 216 LYS B CG  1 
ATOM   3873 C  CD  . LYS B 1 216 ? -2.39200  37.65000  19.95400 1.000 60.51455 ? 216 LYS B CD  1 
ATOM   3874 C  CE  . LYS B 1 216 ? -2.18200  37.23900  21.39700 1.000 61.53262 ? 216 LYS B CE  1 
ATOM   3875 N  NZ  . LYS B 1 216 ? -3.42400  37.43200  22.19100 1.000 60.90760 ? 216 LYS B NZ  1 
ATOM   3876 N  N   . PRO B 1 217 ? -0.30700  33.95500  17.24800 1.000 47.57654 ? 217 PRO B N   1 
ATOM   3877 C  CA  . PRO B 1 217 ? 0.25000   32.63300  16.93200 1.000 42.15055 ? 217 PRO B CA  1 
ATOM   3878 C  C   . PRO B 1 217 ? 0.38800   31.75300  18.16500 1.000 38.99739 ? 217 PRO B C   1 
ATOM   3879 O  O   . PRO B 1 217 ? 0.77100   32.21200  19.24300 1.000 38.05854 ? 217 PRO B O   1 
ATOM   3880 C  CB  . PRO B 1 217 ? 1.62600   32.96600  16.34700 1.000 40.00857 ? 217 PRO B CB  1 
ATOM   3881 C  CG  . PRO B 1 217 ? 1.98700   34.26400  16.98800 1.000 41.23004 ? 217 PRO B CG  1 
ATOM   3882 C  CD  . PRO B 1 217 ? 0.70700   35.02000  17.17900 1.000 46.65532 ? 217 PRO B CD  1 
ATOM   3883 N  N   . ARG B 1 218 ? 0.07300   30.46800  17.99400 1.000 37.11788 ? 218 ARG B N   1 
ATOM   3884 C  CA  . ARG B 1 218 ? 0.27900   29.49000  19.05500 1.000 35.03408 ? 218 ARG B CA  1 
ATOM   3885 C  C   . ARG B 1 218 ? 1.72500   29.00900  19.03600 1.000 33.25354 ? 218 ARG B C   1 
ATOM   3886 O  O   . ARG B 1 218 ? 2.29500   28.75900  17.96800 1.000 32.76358 ? 218 ARG B O   1 
ATOM   3887 C  CB  . ARG B 1 218 ? -0.67900  28.30900  18.89700 1.000 34.77077 ? 218 ARG B CB  1 
ATOM   3888 C  CG  . ARG B 1 218 ? -0.48500  27.21200  19.93000 1.000 32.70373 ? 218 ARG B CG  1 
ATOM   3889 C  CD  . ARG B 1 218 ? -1.48300  26.08900  19.74500 1.000 33.02453 ? 218 ARG B CD  1 
ATOM   3890 N  NE  . ARG B 1 218 ? -1.49400  25.59700  18.37500 1.000 34.57756 ? 218 ARG B NE  1 
ATOM   3891 C  CZ  . ARG B 1 218 ? -0.88600  24.49400  17.96700 1.000 34.99733 ? 218 ARG B CZ  1 
ATOM   3892 N  NH1 . ARG B 1 218 ? -0.21000  23.72900  18.80400 1.000 32.88177 ? 218 ARG B NH1 1 
ATOM   3893 N  NH2 . ARG B 1 218 ? -0.96400  24.14500  16.68700 1.000 36.54882 ? 218 ARG B NH2 1 
ATOM   3894 N  N   . ARG B 1 219 ? 2.32100   28.90200  20.22500 1.000 30.61716 ? 219 ARG B N   1 
ATOM   3895 C  CA  . ARG B 1 219 ? 3.72700   28.54100  20.38500 1.000 29.83525 ? 219 ARG B CA  1 
ATOM   3896 C  C   . ARG B 1 219 ? 3.85500   27.28000  21.21800 1.000 28.89929 ? 219 ARG B C   1 
ATOM   3897 O  O   . ARG B 1 219 ? 3.33700   27.21700  22.33600 1.000 29.62928 ? 219 ARG B O   1 
ATOM   3898 C  CB  . ARG B 1 219 ? 4.52000   29.65200  21.06600 1.000 29.91946 ? 219 ARG B CB  1 
ATOM   3899 C  CG  . ARG B 1 219 ? 4.89200   30.80100  20.18600 1.000 30.33111 ? 219 ARG B CG  1 
ATOM   3900 C  CD  . ARG B 1 219 ? 5.93400   31.61800  20.88200 1.000 30.14957 ? 219 ARG B CD  1 
ATOM   3901 N  NE  . ARG B 1 219 ? 6.74500   32.35400  19.92700 1.000 32.99236 ? 219 ARG B NE  1 
ATOM   3902 C  CZ  . ARG B 1 219 ? 7.77000   33.12700  20.25600 1.000 31.80568 ? 219 ARG B CZ  1 
ATOM   3903 N  NH1 . ARG B 1 219 ? 8.15800   33.26100  21.51400 1.000 30.90345 ? 219 ARG B NH1 1 
ATOM   3904 N  NH2 . ARG B 1 219 ? 8.42100   33.78300  19.30100 1.000 31.92205 ? 219 ARG B NH2 1 
ATOM   3905 N  N   . VAL B 1 220 ? 4.58200   26.32200  20.66300 1.000 27.82151 ? 220 VAL B N   1 
ATOM   3906 C  CA  . VAL B 1 220 ? 4.81300   25.02900  21.36100 1.000 28.11825 ? 220 VAL B CA  1 
ATOM   3907 C  C   . VAL B 1 220 ? 6.29100   24.61200  21.22200 1.000 27.07844 ? 220 VAL B C   1 
ATOM   3908 O  O   . VAL B 1 220 ? 6.80300   24.60800  20.11400 1.000 27.68652 ? 220 VAL B O   1 
ATOM   3909 C  CB  . VAL B 1 220 ? 3.87200   23.91700  20.85200 1.000 27.99872 ? 220 VAL B CB  1 
ATOM   3910 C  CG1 . VAL B 1 220 ? 3.81800   23.84800  19.33300 1.000 29.96534 ? 220 VAL B CG1 1 
ATOM   3911 C  CG2 . VAL B 1 220 ? 4.21400   22.56400  21.45700 1.000 26.48560 ? 220 VAL B CG2 1 
ATOM   3912 N  N   . VAL B 1 221 ? 6.93300   24.32700  22.34000 1.000 27.31685 ? 221 VAL B N   1 
ATOM   3913 C  CA  . VAL B 1 221 ? 8.28700   23.78700  22.31200 1.000 25.87387 ? 221 VAL B CA  1 
ATOM   3914 C  C   . VAL B 1 221 ? 8.18100   22.29500  22.61400 1.000 24.90268 ? 221 VAL B C   1 
ATOM   3915 O  O   . VAL B 1 221 ? 7.60000   21.89900  23.63100 1.000 25.64189 ? 221 VAL B O   1 
ATOM   3916 C  CB  . VAL B 1 221 ? 9.21300   24.51800  23.30400 1.000 25.86212 ? 221 VAL B CB  1 
ATOM   3917 C  CG1 . VAL B 1 221 ? 10.55800  23.81400  23.41700 1.000 24.31195 ? 221 VAL B CG1 1 
ATOM   3918 C  CG2 . VAL B 1 221 ? 9.41600   25.96800  22.88800 1.000 24.12105 ? 221 VAL B CG2 1 
ATOM   3919 N  N   . LEU B 1 222 ? 8.71300   21.46800  21.71600 1.000 25.17110 ? 222 LEU B N   1 
ATOM   3920 C  CA  . LEU B 1 222 ? 8.56300   20.01600  21.76900 1.000 24.39221 ? 222 LEU B CA  1 
ATOM   3921 C  C   . LEU B 1 222 ? 9.90000   19.38100  22.11200 1.000 23.88615 ? 222 LEU B C   1 
ATOM   3922 O  O   . LEU B 1 222 ? 10.87200  19.55000  21.37500 1.000 23.62334 ? 222 LEU B O   1 
ATOM   3923 C  CB  . LEU B 1 222 ? 8.03600   19.47400  20.44100 1.000 24.00752 ? 222 LEU B CB  1 
ATOM   3924 C  CG  . LEU B 1 222 ? 6.65000   20.04200  20.12500 1.000 25.35600 ? 222 LEU B CG  1 
ATOM   3925 C  CD1 . LEU B 1 222 ? 6.67500   20.93800  18.89500 1.000 26.53995 ? 222 LEU B CD1 1 
ATOM   3926 C  CD2 . LEU B 1 222 ? 5.64500   18.94100  19.97400 1.000 25.92552 ? 222 LEU B CD2 1 
ATOM   3927 N  N   . ALA B 1 223 ? 9.94800   18.65500  23.22500 1.000 23.33941 ? 223 ALA B N   1 
ATOM   3928 C  CA  . ALA B 1 223 ? 11.18000  18.02200  23.65700 1.000 23.06401 ? 223 ALA B CA  1 
ATOM   3929 C  C   . ALA B 1 223 ? 11.00800  16.51400  23.67400 1.000 21.67802 ? 223 ALA B C   1 
ATOM   3930 O  O   . ALA B 1 223 ? 10.11900  15.98900  24.32600 1.000 21.59499 ? 223 ALA B O   1 
ATOM   3931 C  CB  . ALA B 1 223 ? 11.60100  18.53700  25.02700 1.000 22.26059 ? 223 ALA B CB  1 
HETATM 3932 C  C   . F2Y B 1 224 ? 13.04100  13.76400  23.68600 1.000 20.20348 ? 224 F2Y B C   1 
HETATM 3933 O  O   . F2Y B 1 224 ? 14.21700  13.91100  23.27200 1.000 20.28252 ? 224 F2Y B O   1 
HETATM 3934 C  CA  . F2Y B 1 224 ? 11.84700  14.38000  22.90700 1.000 21.14483 ? 224 F2Y B CA  1 
HETATM 3935 N  N   . F2Y B 1 224 ? 11.86100  15.82600  22.93400 1.000 21.81386 ? 224 F2Y B N   1 
HETATM 3936 C  CB  . F2Y B 1 224 ? 11.87300  13.81800  21.48500 1.000 22.14626 ? 224 F2Y B CB  1 
HETATM 3937 C  CG  . F2Y B 1 224 ? 10.77900  14.36800  20.63300 1.000 24.45152 ? 224 F2Y B CG  1 
HETATM 3938 C  CD1 . F2Y B 1 224 ? 9.54800   14.75900  21.18800 1.000 24.55089 ? 224 F2Y B CD1 1 
HETATM 3939 C  CE1 . F2Y B 1 224 ? 8.53800   15.27600  20.36200 1.000 24.90082 ? 224 F2Y B CE1 1 
HETATM 3940 F  F1  . F2Y B 1 224 ? 7.33700   15.68400  20.83900 1.000 25.76462 ? 224 F2Y B F1  1 
HETATM 3941 C  CD2 . F2Y B 1 224 ? 10.97400  14.49100  19.25900 1.000 26.17766 ? 224 F2Y B CD2 1 
HETATM 3942 C  CE2 . F2Y B 1 224 ? 9.96500   15.00100  18.42900 1.000 26.33695 ? 224 F2Y B CE2 1 
HETATM 3943 F  F2  . F2Y B 1 224 ? 10.18200  15.10800  17.10100 1.000 29.28693 ? 224 F2Y B F2  1 
HETATM 3944 C  CZ  . F2Y B 1 224 ? 8.73500   15.40400  18.98100 1.000 26.14865 ? 224 F2Y B CZ  1 
HETATM 3945 O  OH  . F2Y B 1 224 ? 7.76200   15.90900  18.15000 1.000 26.85094 ? 224 F2Y B OH  1 
ATOM   3946 N  N   . PHE B 1 225 ? 12.72800  13.11200  24.79200 1.000 20.43247 ? 225 PHE B N   1 
ATOM   3947 C  CA  . PHE B 1 225 ? 13.72300  12.44300  25.60100 1.000 20.34837 ? 225 PHE B CA  1 
ATOM   3948 C  C   . PHE B 1 225 ? 13.72200  10.96000  25.27500 1.000 20.33772 ? 225 PHE B C   1 
ATOM   3949 O  O   . PHE B 1 225 ? 12.71500  10.29300  25.46500 1.000 20.78453 ? 225 PHE B O   1 
ATOM   3950 C  CB  . PHE B 1 225 ? 13.43600  12.68000  27.07400 1.000 19.90116 ? 225 PHE B CB  1 
ATOM   3951 C  CG  . PHE B 1 225 ? 13.54100  14.11700  27.47900 1.000 19.41896 ? 225 PHE B CG  1 
ATOM   3952 C  CD1 . PHE B 1 225 ? 12.47200  14.97100  27.32500 1.000 20.33197 ? 225 PHE B CD1 1 
ATOM   3953 C  CD2 . PHE B 1 225 ? 14.70900  14.61300  28.01600 1.000 20.13621 ? 225 PHE B CD2 1 
ATOM   3954 C  CE1 . PHE B 1 225 ? 12.56600  16.28500  27.69900 1.000 19.66837 ? 225 PHE B CE1 1 
ATOM   3955 C  CE2 . PHE B 1 225 ? 14.81300  15.93300  28.38800 1.000 19.84216 ? 225 PHE B CE2 1 
ATOM   3956 C  CZ  . PHE B 1 225 ? 13.74300  16.76700  28.23000 1.000 18.88414 ? 225 PHE B CZ  1 
ATOM   3957 N  N   . ASN B 1 226 ? 14.83700  10.45000  24.75700 1.000 20.00128 ? 226 ASN B N   1 
ATOM   3958 C  CA  . ASN B 1 226 ? 14.92600  9.06900   24.30400 1.000 20.38178 ? 226 ASN B CA  1 
ATOM   3959 C  C   . ASN B 1 226 ? 15.89700  8.29400   25.17400 1.000 20.45594 ? 226 ASN B C   1 
ATOM   3960 O  O   . ASN B 1 226 ? 16.76100  8.87000   25.83600 1.000 19.10772 ? 226 ASN B O   1 
ATOM   3961 C  CB  . ASN B 1 226 ? 15.40500  8.96200   22.85100 1.000 20.41015 ? 226 ASN B CB  1 
ATOM   3962 C  CG  . ASN B 1 226 ? 14.33300  9.30300   21.83700 1.000 20.73530 ? 226 ASN B CG  1 
ATOM   3963 O  OD1 . ASN B 1 226 ? 13.14500  9.33300   22.14400 1.000 21.70484 ? 226 ASN B OD1 1 
ATOM   3964 N  ND2 . ASN B 1 226 ? 14.75800  9.54400   20.60600 1.000 21.31150 ? 226 ASN B ND2 1 
ATOM   3965 N  N   . SER B 1 227 ? 15.74900  6.97100   25.15300 1.000 19.79609 ? 227 SER B N   1 
ATOM   3966 C  CA  . SER B 1 227 ? 16.81300  6.11100   25.64200 1.000 20.22034 ? 227 SER B CA  1 
ATOM   3967 C  C   . SER B 1 227 ? 18.13500  6.54500   25.02500 1.000 19.70791 ? 227 SER B C   1 
ATOM   3968 O  O   . SER B 1 227 ? 18.18100  6.92400   23.85500 1.000 19.86425 ? 227 SER B O   1 
ATOM   3969 C  CB  . SER B 1 227 ? 16.51500  4.65100   25.28100 1.000 21.43594 ? 227 SER B CB  1 
ATOM   3970 O  OG  . SER B 1 227 ? 17.67600  3.83400   25.38900 1.000 21.87126 ? 227 SER B OG  1 
ATOM   3971 N  N   . VAL B 1 228 ? 19.21600  6.50300   25.81300 1.000 19.46267 ? 228 VAL B N   1 
ATOM   3972 C  CA  . VAL B 1 228 ? 20.53900  6.78800   25.26900 1.000 19.72520 ? 228 VAL B CA  1 
ATOM   3973 C  C   . VAL B 1 228 ? 20.96900  5.74800   24.24200 1.000 19.84536 ? 228 VAL B C   1 
ATOM   3974 O  O   . VAL B 1 228 ? 21.96500  5.95400   23.55200 1.000 19.61927 ? 228 VAL B O   1 
ATOM   3975 C  CB  . VAL B 1 228 ? 21.62300  6.90800   26.37500 1.000 19.69522 ? 228 VAL B CB  1 
ATOM   3976 C  CG1 . VAL B 1 228 ? 21.35300  8.07200   27.28200 1.000 19.35436 ? 228 VAL B CG1 1 
ATOM   3977 C  CG2 . VAL B 1 228 ? 21.72900  5.62800   27.18700 1.000 21.32036 ? 228 VAL B CG2 1 
ATOM   3978 N  N   . GLN B 1 229 ? 20.25000  4.62700   24.12300 1.000 19.81669 ? 229 GLN B N   1 
ATOM   3979 C  CA  . GLN B 1 229 ? 20.50600  3.71800   23.01300 1.000 19.89940 ? 229 GLN B CA  1 
ATOM   3980 C  C   . GLN B 1 229 ? 20.12900  4.32000   21.67200 1.000 18.88631 ? 229 GLN B C   1 
ATOM   3981 O  O   . GLN B 1 229 ? 20.58300  3.82200   20.64100 1.000 19.41836 ? 229 GLN B O   1 
ATOM   3982 C  CB  . GLN B 1 229 ? 19.72800  2.41600   23.16400 1.000 20.96945 ? 229 GLN B CB  1 
ATOM   3983 C  CG  . GLN B 1 229 ? 19.91200  1.69300   24.45400 1.000 22.10241 ? 229 GLN B CG  1 
ATOM   3984 C  CD  . GLN B 1 229 ? 18.94500  0.56600   24.57200 1.000 23.69620 ? 229 GLN B CD  1 
ATOM   3985 O  OE1 . GLN B 1 229 ? 18.98500  -0.37300  23.78600 1.000 24.17798 ? 229 GLN B OE1 1 
ATOM   3986 N  NE2 . GLN B 1 229 ? 18.02700  0.66700   25.52200 1.000 24.46932 ? 229 GLN B NE2 1 
ATOM   3987 N  N   . LEU B 1 230 ? 19.29600  5.35400   21.65700 1.000 19.51594 ? 230 LEU B N   1 
ATOM   3988 C  CA  . LEU B 1 230 ? 18.79900  5.94500   20.42100 1.000 19.54542 ? 230 LEU B CA  1 
ATOM   3989 C  C   . LEU B 1 230 ? 19.60800  7.19300   20.08500 1.000 19.63844 ? 230 LEU B C   1 
ATOM   3990 O  O   . LEU B 1 230 ? 19.72800  8.10800   20.90800 1.000 19.21757 ? 230 LEU B O   1 
ATOM   3991 C  CB  . LEU B 1 230 ? 17.30900  6.29000   20.52600 1.000 19.18544 ? 230 LEU B CB  1 
ATOM   3992 C  CG  . LEU B 1 230 ? 16.28800  5.15500   20.63100 1.000 19.31819 ? 230 LEU B CG  1 
ATOM   3993 C  CD1 . LEU B 1 230 ? 14.86400  5.68300   20.58700 1.000 20.75912 ? 230 LEU B CD1 1 
ATOM   3994 C  CD2 . LEU B 1 230 ? 16.49400  4.15400   19.53400 1.000 19.82704 ? 230 LEU B CD2 1 
ATOM   3995 N  N   . THR B 1 231 ? 20.14800  7.22100   18.87400 1.000 19.58006 ? 231 THR B N   1 
ATOM   3996 C  CA  . THR B 1 231 ? 20.91400  8.35700   18.40100 1.000 18.98937 ? 231 THR B CA  1 
ATOM   3997 C  C   . THR B 1 231 ? 20.11400  9.64300   18.57400 1.000 19.90946 ? 231 THR B C   1 
ATOM   3998 O  O   . THR B 1 231 ? 18.95400  9.69800   18.15900 1.000 20.97170 ? 231 THR B O   1 
ATOM   3999 C  CB  . THR B 1 231 ? 21.27400  8.15700   16.93400 1.000 18.74685 ? 231 THR B CB  1 
ATOM   4000 O  OG1 . THR B 1 231 ? 22.11300  7.01500   16.81500 1.000 17.63680 ? 231 THR B OG1 1 
ATOM   4001 C  CG2 . THR B 1 231 ? 22.00900  9.35400   16.39500 1.000 18.72909 ? 231 THR B CG2 1 
ATOM   4002 N  N   . PRO B 1 232 ? 20.67900  10.67400  19.20200 1.000 19.62736 ? 232 PRO B N   1 
ATOM   4003 C  CA  . PRO B 1 232 ? 20.01900  11.98500  19.22500 1.000 19.97551 ? 232 PRO B CA  1 
ATOM   4004 C  C   . PRO B 1 232 ? 19.83000  12.53700  17.81800 1.000 19.74369 ? 232 PRO B C   1 
ATOM   4005 O  O   . PRO B 1 232 ? 20.77000  12.58600  17.02200 1.000 18.85886 ? 232 PRO B O   1 
ATOM   4006 C  CB  . PRO B 1 232 ? 20.98500  12.85200  20.04200 1.000 19.98161 ? 232 PRO B CB  1 
ATOM   4007 C  CG  . PRO B 1 232 ? 21.74500  11.89100  20.88000 1.000 20.32503 ? 232 PRO B CG  1 
ATOM   4008 C  CD  . PRO B 1 232 ? 21.87200  10.64200  20.06300 1.000 20.50927 ? 232 PRO B CD  1 
ATOM   4009 N  N   . PHE B 1 233 ? 18.59600  12.95700  17.51700 1.000 19.82720 ? 233 PHE B N   1 
ATOM   4010 C  CA  . PHE B 1 233 ? 18.30900  13.53500  16.21000 1.000 19.37937 ? 233 PHE B CA  1 
ATOM   4011 C  C   . PHE B 1 233 ? 19.03900  14.86400  16.01600 1.000 20.04233 ? 233 PHE B C   1 
ATOM   4012 O  O   . PHE B 1 233 ? 19.53400  15.15500  14.91900 1.000 20.73958 ? 233 PHE B O   1 
ATOM   4013 C  CB  . PHE B 1 233 ? 16.80000  13.70100  16.04300 1.000 19.36733 ? 233 PHE B CB  1 
ATOM   4014 C  CG  . PHE B 1 233 ? 16.41100  14.53500  14.85800 1.000 21.20578 ? 233 PHE B CG  1 
ATOM   4015 C  CD1 . PHE B 1 233 ? 16.30800  13.97200  13.59900 1.000 22.21306 ? 233 PHE B CD1 1 
ATOM   4016 C  CD2 . PHE B 1 233 ? 16.14700  15.88600  15.00200 1.000 20.39351 ? 233 PHE B CD2 1 
ATOM   4017 C  CE1 . PHE B 1 233 ? 15.94500  14.73600  12.51100 1.000 22.96293 ? 233 PHE B CE1 1 
ATOM   4018 C  CE2 . PHE B 1 233 ? 15.79300  16.64900  13.91400 1.000 21.83778 ? 233 PHE B CE2 1 
ATOM   4019 C  CZ  . PHE B 1 233 ? 15.69000  16.07200  12.66700 1.000 23.20967 ? 233 PHE B CZ  1 
ATOM   4020 N  N   . GLU B 1 234 ? 19.11300  15.68300  17.06400 1.000 20.41453 ? 234 GLU B N   1 
ATOM   4021 C  CA  . GLU B 1 234 ? 19.92000  16.89600  17.06700 1.000 19.51400 ? 234 GLU B CA  1 
ATOM   4022 C  C   . GLU B 1 234 ? 21.24300  16.59200  17.75700 1.000 19.50368 ? 234 GLU B C   1 
ATOM   4023 O  O   . GLU B 1 234 ? 21.25300  16.16700  18.91500 1.000 19.33467 ? 234 GLU B O   1 
ATOM   4024 C  CB  . GLU B 1 234 ? 19.18800  18.02900  17.79000 1.000 20.29086 ? 234 GLU B CB  1 
ATOM   4025 C  CG  . GLU B 1 234 ? 18.04900  18.62500  16.98100 1.000 21.43972 ? 234 GLU B CG  1 
ATOM   4026 C  CD  . GLU B 1 234 ? 17.11600  19.51600  17.78600 1.000 22.24304 ? 234 GLU B CD  1 
ATOM   4027 O  OE1 . GLU B 1 234 ? 17.27100  19.62100  19.03100 1.000 22.59500 ? 234 GLU B OE1 1 
ATOM   4028 O  OE2 . GLU B 1 234 ? 16.21800  20.11600  17.14900 1.000 22.60215 ? 234 GLU B OE2 1 
ATOM   4029 N  N   . THR B 1 235 ? 22.35600  16.81000  17.06300 1.000 20.20864 ? 235 THR B N   1 
ATOM   4030 C  CA  . THR B 1 235 ? 23.66300  16.65200  17.69500 1.000 20.73198 ? 235 THR B CA  1 
ATOM   4031 C  C   . THR B 1 235 ? 24.10100  17.99700  18.27600 1.000 20.80642 ? 235 THR B C   1 
ATOM   4032 O  O   . THR B 1 235 ? 24.17800  18.99600  17.55300 1.000 21.25019 ? 235 THR B O   1 
ATOM   4033 C  CB  . THR B 1 235 ? 24.71500  16.08300  16.72900 1.000 20.36421 ? 235 THR B CB  1 
ATOM   4034 O  OG1 . THR B 1 235 ? 25.98400  16.02900  17.38700 1.000 20.47442 ? 235 THR B OG1 1 
ATOM   4035 C  CG2 . THR B 1 235 ? 24.85100  16.90000  15.45500 1.000 19.94518 ? 235 THR B CG2 1 
ATOM   4036 N  N   . TYR B 1 236 ? 24.36300  18.02200  19.58800 1.000 20.72196 ? 236 TYR B N   1 
ATOM   4037 C  CA  . TYR B 1 236 ? 24.78900  19.22300  20.29400 1.000 20.42509 ? 236 TYR B CA  1 
ATOM   4038 C  C   . TYR B 1 236 ? 26.30300  19.27300  20.47000 1.000 20.59807 ? 236 TYR B C   1 
ATOM   4039 O  O   . TYR B 1 236 ? 26.80700  19.99400  21.33000 1.000 21.24513 ? 236 TYR B O   1 
ATOM   4040 C  CB  . TYR B 1 236 ? 24.06600  19.32900  21.63900 1.000 19.78010 ? 236 TYR B CB  1 
ATOM   4041 C  CG  . TYR B 1 236 ? 22.54800  19.40700  21.51700 1.000 20.30402 ? 236 TYR B CG  1 
ATOM   4042 C  CD1 . TYR B 1 236 ? 21.92600  20.60100  21.15300 1.000 20.94592 ? 236 TYR B CD1 1 
ATOM   4043 C  CD2 . TYR B 1 236 ? 21.76200  18.28400  21.77900 1.000 20.06093 ? 236 TYR B CD2 1 
ATOM   4044 C  CE1 . TYR B 1 236 ? 20.55400  20.64400  21.04700 1.000 21.91006 ? 236 TYR B CE1 1 
ATOM   4045 C  CE2 . TYR B 1 236 ? 20.39400  18.36600  21.66200 1.000 19.15550 ? 236 TYR B CE2 1 
ATOM   4046 C  CZ  . TYR B 1 236 ? 19.75200  19.53800  21.29200 1.000 20.51699 ? 236 TYR B CZ  1 
ATOM   4047 O  OH  . TYR B 1 236 ? 18.40400  19.58600  21.18400 1.000 21.18503 ? 236 TYR B OH  1 
ATOM   4048 N  N   . ARG B 1 237 ? 27.04000  18.56500  19.62900 1.000 21.07245 ? 237 ARG B N   1 
ATOM   4049 C  CA  . ARG B 1 237 ? 28.48900  18.49100  19.74700 1.000 21.77376 ? 237 ARG B CA  1 
ATOM   4050 C  C   . ARG B 1 237 ? 29.20800  19.73900  19.25900 1.000 22.47184 ? 237 ARG B C   1 
ATOM   4051 O  O   . ARG B 1 237 ? 30.40100  19.87900  19.52900 1.000 23.19062 ? 237 ARG B O   1 
ATOM   4052 C  CB  . ARG B 1 237 ? 29.00500  17.28700  18.96600 1.000 20.82428 ? 237 ARG B CB  1 
ATOM   4053 C  CG  . ARG B 1 237 ? 29.03500  17.52300  17.48300 1.000 20.93964 ? 237 ARG B CG  1 
ATOM   4054 C  CD  . ARG B 1 237 ? 29.04600  16.22300  16.73600 1.000 20.41556 ? 237 ARG B CD  1 
ATOM   4055 N  NE  . ARG B 1 237 ? 30.39100  15.71800  16.52800 1.000 20.05092 ? 237 ARG B NE  1 
ATOM   4056 C  CZ  . ARG B 1 237 ? 30.66100  14.50200  16.07700 1.000 19.47716 ? 237 ARG B CZ  1 
ATOM   4057 N  NH1 . ARG B 1 237 ? 29.70400  13.62500  15.83600 1.000 19.60479 ? 237 ARG B NH1 1 
ATOM   4058 N  NH2 . ARG B 1 237 ? 31.92000  14.16200  15.85200 1.000 20.19332 ? 237 ARG B NH2 1 
ATOM   4059 N  N   . THR B 1 238 ? 28.54300  20.63300  18.53300 1.000 23.45106 ? 238 THR B N   1 
ATOM   4060 C  CA  . THR B 1 238 ? 29.20100  21.84600  18.06400 1.000 23.71582 ? 238 THR B CA  1 
ATOM   4061 C  C   . THR B 1 238 ? 29.05500  23.01400  19.03000 1.000 23.87333 ? 238 THR B C   1 
ATOM   4062 O  O   . THR B 1 238 ? 29.54700  24.10100  18.72900 1.000 25.35740 ? 238 THR B O   1 
ATOM   4063 C  CB  . THR B 1 238 ? 28.67400  22.26700  16.68600 1.000 22.24777 ? 238 THR B CB  1 
ATOM   4064 O  OG1 . THR B 1 238 ? 27.35300  22.81000  16.81100 1.000 22.42948 ? 238 THR B OG1 1 
ATOM   4065 C  CG2 . THR B 1 238 ? 28.68000  21.08900  15.73200 1.000 22.83753 ? 238 THR B CG2 1 
ATOM   4066 N  N   . MET B 1 239 ? 28.39800  22.82700  20.16900 1.000 22.76027 ? 239 MET B N   1 
ATOM   4067 C  CA  . MET B 1 239 ? 28.34600  23.89300  21.15400 1.000 24.36684 ? 239 MET B CA  1 
ATOM   4068 C  C   . MET B 1 239 ? 29.76800  24.27500  21.56700 1.000 25.38136 ? 239 MET B C   1 
ATOM   4069 O  O   . MET B 1 239 ? 30.66900  23.43000  21.58400 1.000 25.75536 ? 239 MET B O   1 
ATOM   4070 C  CB  . MET B 1 239 ? 27.54200  23.47300  22.38700 1.000 23.74247 ? 239 MET B CB  1 
ATOM   4071 C  CG  . MET B 1 239 ? 26.03700  23.35900  22.17900 1.000 24.48675 ? 239 MET B CG  1 
ATOM   4072 S  SD  . MET B 1 239 ? 25.14700  22.69100  23.61300 1.000 24.41677 ? 239 MET B SD  1 
ATOM   4073 C  CE  . MET B 1 239 ? 24.90600  24.16800  24.58400 1.000 23.82739 ? 239 MET B CE  1 
ATOM   4074 N  N   . PRO B 1 240 ? 30.00700  25.54600  21.86900 1.000 27.05605 ? 240 PRO B N   1 
ATOM   4075 C  CA  . PRO B 1 240 ? 31.31400  25.93400  22.40300 1.000 27.57101 ? 240 PRO B CA  1 
ATOM   4076 C  C   . PRO B 1 240 ? 31.53400  25.31400  23.77000 1.000 27.25692 ? 240 PRO B C   1 
ATOM   4077 O  O   . PRO B 1 240 ? 30.59300  25.12700  24.54600 1.000 26.56592 ? 240 PRO B O   1 
ATOM   4078 C  CB  . PRO B 1 240 ? 31.22300  27.46000  22.50000 1.000 28.01855 ? 240 PRO B CB  1 
ATOM   4079 C  CG  . PRO B 1 240 ? 30.06600  27.83700  21.64700 1.000 29.09417 ? 240 PRO B CG  1 
ATOM   4080 C  CD  . PRO B 1 240 ? 29.11300  26.69700  21.68700 1.000 27.40987 ? 240 PRO B CD  1 
ATOM   4081 N  N   . ARG B 1 241 ? 32.78200  24.97800  24.07300 1.000 26.95996 ? 241 ARG B N   1 
ATOM   4082 C  CA  . ARG B 1 241 ? 33.10000  24.40400  25.40000 1.000 27.79189 ? 241 ARG B CA  1 
ATOM   4083 C  C   . ARG B 1 241 ? 32.62700  25.37200  26.48700 1.000 28.11573 ? 241 ARG B C   1 
ATOM   4084 O  O   . ARG B 1 241 ? 32.07800  24.90900  27.48100 1.000 27.89033 ? 241 ARG B O   1 
ATOM   4085 C  CB  . ARG B 1 241 ? 34.58600  24.08900  25.62400 1.000 28.31419 ? 241 ARG B CB  1 
ATOM   4086 C  CG  . ARG B 1 241 ? 34.93900  23.93200  27.09400 1.000 28.46531 ? 241 ARG B CG  1 
ATOM   4087 C  CD  . ARG B 1 241 ? 36.41800  23.85900  27.40500 1.000 29.26814 ? 241 ARG B CD  1 
ATOM   4088 N  NE  . ARG B 1 241 ? 36.99100  22.60200  26.92100 1.000 32.14282 ? 241 ARG B NE  1 
ATOM   4089 C  CZ  . ARG B 1 241 ? 37.32400  21.60100  27.71200 1.000 30.56472 ? 241 ARG B CZ  1 
ATOM   4090 N  NH1 . ARG B 1 241 ? 37.20300  21.72800  29.01500 1.000 31.25473 ? 241 ARG B NH1 1 
ATOM   4091 N  NH2 . ARG B 1 241 ? 37.75800  20.47200  27.19800 1.000 30.94125 ? 241 ARG B NH2 1 
ATOM   4092 N  N   . GLU B 1 242 ? 32.82100  26.66700  26.26800 1.000 28.47867 ? 242 GLU B N   1 
ATOM   4093 C  CA  . GLU B 1 242 ? 32.49700  27.64300  27.29900 1.000 27.62321 ? 242 GLU B CA  1 
ATOM   4094 C  C   . GLU B 1 242 ? 31.00000  27.66500  27.58800 1.000 27.22091 ? 242 GLU B C   1 
ATOM   4095 O  O   . GLU B 1 242 ? 30.59200  27.79600  28.74200 1.000 27.53277 ? 242 GLU B O   1 
ATOM   4096 C  CB  . GLU B 1 242 ? 33.01100  29.01900  26.88000 1.000 29.41231 ? 242 GLU B CB  1 
ATOM   4097 C  CG  . GLU B 1 242 ? 34.52300  29.05800  26.56000 1.000 31.60796 ? 242 GLU B CG  1 
ATOM   4098 C  CD  . GLU B 1 242 ? 34.89000  28.40800  25.21700 1.000 30.70772 ? 242 GLU B CD  1 
ATOM   4099 O  OE1 . GLU B 1 242 ? 34.04900  28.40600  24.29900 1.000 30.18169 ? 242 GLU B OE1 1 
ATOM   4100 O  OE2 . GLU B 1 242 ? 36.01600  27.88900  25.08100 1.000 33.66609 ? 242 GLU B OE2 1 
ATOM   4101 N  N   . MET B 1 243 ? 30.16300  27.50800  26.56100 1.000 28.30373 ? 243 MET B N   1 
ATOM   4102 C  CA  . MET B 1 243 ? 28.72800  27.36900  26.80300 1.000 27.69777 ? 243 MET B CA  1 
ATOM   4103 C  C   . MET B 1 243 ? 28.39800  26.03100  27.45300 1.000 26.60188 ? 243 MET B C   1 
ATOM   4104 O  O   . MET B 1 243 ? 27.48700  25.94500  28.28000 1.000 27.79577 ? 243 MET B O   1 
ATOM   4105 C  CB  . MET B 1 243 ? 27.95500  27.52500  25.49400 1.000 27.75194 ? 243 MET B CB  1 
ATOM   4106 C  CG  . MET B 1 243 ? 26.44900  27.46100  25.64900 1.000 27.80829 ? 243 MET B CG  1 
ATOM   4107 S  SD  . MET B 1 243 ? 25.61000  27.52000  24.07200 1.000 28.76141 ? 243 MET B SD  1 
ATOM   4108 C  CE  . MET B 1 243 ? 25.96100  29.19300  23.58000 1.000 29.62887 ? 243 MET B CE  1 
ATOM   4109 N  N   . VAL B 1 244 ? 29.13300  24.98200  27.09900 1.000 27.89126 ? 244 VAL B N   1 
ATOM   4110 C  CA  . VAL B 1 244 ? 28.88500  23.65900  27.66000 1.000 26.63566 ? 244 VAL B CA  1 
ATOM   4111 C  C   . VAL B 1 244 ? 29.23600  23.61000  29.14600 1.000 26.41638 ? 244 VAL B C   1 
ATOM   4112 O  O   . VAL B 1 244 ? 28.49200  23.04400  29.95800 1.000 24.12421 ? 244 VAL B O   1 
ATOM   4113 C  CB  . VAL B 1 244 ? 29.67300  22.61700  26.85200 1.000 25.70270 ? 244 VAL B CB  1 
ATOM   4114 C  CG1 . VAL B 1 244 ? 29.71400  21.29600  27.58500 1.000 24.33053 ? 244 VAL B CG1 1 
ATOM   4115 C  CG2 . VAL B 1 244 ? 29.05400  22.45800  25.47700 1.000 25.02013 ? 244 VAL B CG2 1 
ATOM   4116 N  N   . GLU B 1 245 ? 30.36100  24.21400  29.53100 1.000 27.98255 ? 245 GLU B N   1 
ATOM   4117 C  CA  . GLU B 1 245 ? 30.87900  24.06800  30.88600 1.000 27.92470 ? 245 GLU B CA  1 
ATOM   4118 C  C   . GLU B 1 245 ? 30.14100  24.90000  31.92100 1.000 26.99078 ? 245 GLU B C   1 
ATOM   4119 O  O   . GLU B 1 245 ? 30.35600  24.69000  33.11300 1.000 28.53575 ? 245 GLU B O   1 
ATOM   4120 C  CB  . GLU B 1 245 ? 32.36700  24.40000  30.91000 1.000 27.08256 ? 245 GLU B CB  1 
ATOM   4121 C  CG  . GLU B 1 245 ? 33.18400  23.30100  30.26500 1.000 27.84363 ? 245 GLU B CG  1 
ATOM   4122 C  CD  . GLU B 1 245 ? 34.64100  23.36900  30.61400 1.000 28.24320 ? 245 GLU B CD  1 
ATOM   4123 O  OE1 . GLU B 1 245 ? 35.11300  24.46800  30.95900 1.000 30.36645 ? 245 GLU B OE1 1 
ATOM   4124 O  OE2 . GLU B 1 245 ? 35.31100  22.32100  30.55100 1.000 28.12310 ? 245 GLU B OE2 1 
ATOM   4125 N  N   . SER B 1 246 ? 29.27200  25.81800  31.51800 1.000 26.66608 ? 246 SER B N   1 
ATOM   4126 C  CA  . SER B 1 246 ? 28.43600  26.51700  32.48200 1.000 28.05372 ? 246 SER B CA  1 
ATOM   4127 C  C   . SER B 1 246 ? 27.06400  25.85500  32.65600 1.000 27.76422 ? 246 SER B C   1 
ATOM   4128 O  O   . SER B 1 246 ? 26.20000  26.40800  33.35100 1.000 28.48626 ? 246 SER B O   1 
ATOM   4129 C  CB  . SER B 1 246 ? 28.29800  28.00200  32.09500 1.000 27.05100 ? 246 SER B CB  1 
ATOM   4130 O  OG  . SER B 1 246 ? 27.61000  28.18600  30.87800 1.000 27.29562 ? 246 SER B OG  1 
ATOM   4131 N  N   . MET B 1 247 ? 26.85100  24.68400  32.05900 1.000 27.28482 ? 247 MET B N   1 
ATOM   4132 C  CA  . MET B 1 247 ? 25.67800  23.87600  32.36000 1.000 26.39051 ? 247 MET B CA  1 
ATOM   4133 C  C   . MET B 1 247 ? 25.95000  22.98400  33.56000 1.000 26.41477 ? 247 MET B C   1 
ATOM   4134 O  O   . MET B 1 247 ? 27.09600  22.76100  33.95100 1.000 27.30188 ? 247 MET B O   1 
ATOM   4135 C  CB  . MET B 1 247 ? 25.27900  23.00500  31.17000 1.000 25.50383 ? 247 MET B CB  1 
ATOM   4136 C  CG  . MET B 1 247 ? 24.87800  23.78000  29.95700 1.000 25.48205 ? 247 MET B CG  1 
ATOM   4137 S  SD  . MET B 1 247 ? 24.21000  22.68000  28.72500 1.000 25.29210 ? 247 MET B SD  1 
ATOM   4138 C  CE  . MET B 1 247 ? 25.54400  22.65300  27.59600 1.000 25.15824 ? 247 MET B CE  1 
ATOM   4139 N  N   . THR B 1 248 ? 24.87300  22.46800  34.14300 1.000 26.16975 ? 248 THR B N   1 
ATOM   4140 C  CA  . THR B 1 248 ? 25.00000  21.45500  35.17700 1.000 25.74273 ? 248 THR B CA  1 
ATOM   4141 C  C   . THR B 1 248 ? 25.39600  20.11700  34.55000 1.000 24.93329 ? 248 THR B C   1 
ATOM   4142 O  O   . THR B 1 248 ? 25.31500  19.93100  33.33500 1.000 24.29723 ? 248 THR B O   1 
ATOM   4143 C  CB  . THR B 1 248 ? 23.68600  21.31000  35.94200 1.000 25.39016 ? 248 THR B CB  1 
ATOM   4144 O  OG1 . THR B 1 248 ? 22.63500  20.98700  35.02400 1.000 24.17538 ? 248 THR B OG1 1 
ATOM   4145 C  CG2 . THR B 1 248 ? 23.33700  22.59200  36.64200 1.000 24.41502 ? 248 THR B CG2 1 
ATOM   4146 N  N   . VAL B 1 249 ? 25.81900  19.16800  35.39200 1.000 25.03219 ? 249 VAL B N   1 
ATOM   4147 C  CA  . VAL B 1 249 ? 26.10700  17.81800  34.90100 1.000 24.72399 ? 249 VAL B CA  1 
ATOM   4148 C  C   . VAL B 1 249 ? 24.87000  17.20400  34.24900 1.000 24.12205 ? 249 VAL B C   1 
ATOM   4149 O  O   . VAL B 1 249 ? 24.96800  16.48000  33.25300 1.000 23.17717 ? 249 VAL B O   1 
ATOM   4150 C  CB  . VAL B 1 249 ? 26.62900  16.92300  36.03800 1.000 25.42304 ? 249 VAL B CB  1 
ATOM   4151 C  CG1 . VAL B 1 249 ? 26.89900  15.51600  35.51900 1.000 24.47477 ? 249 VAL B CG1 1 
ATOM   4152 C  CG2 . VAL B 1 249 ? 27.86700  17.51600  36.65900 1.000 26.65931 ? 249 VAL B CG2 1 
ATOM   4153 N  N   . LEU B 1 250 ? 23.69200  17.47000  34.81100 1.000 23.29410 ? 250 LEU B N   1 
ATOM   4154 C  CA  . LEU B 1 250 ? 22.45800  16.93200  34.25500 1.000 21.48415 ? 250 LEU B CA  1 
ATOM   4155 C  C   . LEU B 1 250 ? 22.23300  17.41200  32.82500 1.000 22.17288 ? 250 LEU B C   1 
ATOM   4156 O  O   . LEU B 1 250 ? 21.86600  16.61800  31.95200 1.000 21.48930 ? 250 LEU B O   1 
ATOM   4157 C  CB  . LEU B 1 250 ? 21.28300  17.31400  35.15000 1.000 22.70554 ? 250 LEU B CB  1 
ATOM   4158 C  CG  . LEU B 1 250 ? 19.88700  16.84700  34.74500 1.000 21.61399 ? 250 LEU B CG  1 
ATOM   4159 C  CD1 . LEU B 1 250 ? 19.89800  15.36600  34.42100 1.000 22.09322 ? 250 LEU B CD1 1 
ATOM   4160 C  CD2 . LEU B 1 250 ? 18.90900  17.14500  35.86700 1.000 22.14621 ? 250 LEU B CD2 1 
ATOM   4161 N  N   . GLY B 1 251 ? 22.45400  18.70300  32.55900 1.000 22.79127 ? 251 GLY B N   1 
ATOM   4162 C  CA  . GLY B 1 251 ? 22.27500  19.21200  31.20600 1.000 21.40843 ? 251 GLY B CA  1 
ATOM   4163 C  C   . GLY B 1 251 ? 23.25000  18.62800  30.19500 1.000 21.26089 ? 251 GLY B C   1 
ATOM   4164 O  O   . GLY B 1 251 ? 22.87200  18.34000  29.05400 1.000 20.37152 ? 251 GLY B O   1 
ATOM   4165 N  N   . GLN B 1 252 ? 24.52300  18.48000  30.58400 1.000 22.00156 ? 252 GLN B N   1 
ATOM   4166 C  CA  . GLN B 1 252 ? 25.53500  17.96100  29.66700 1.000 20.62069 ? 252 GLN B CA  1 
ATOM   4167 C  C   . GLN B 1 252 ? 25.23300  16.52300  29.27600 1.000 20.06353 ? 252 GLN B C   1 
ATOM   4168 O  O   . GLN B 1 252 ? 25.50100  16.10700  28.14500 1.000 20.26120 ? 252 GLN B O   1 
ATOM   4169 C  CB  . GLN B 1 252 ? 26.92700  18.04900  30.30400 1.000 23.46703 ? 252 GLN B CB  1 
ATOM   4170 C  CG  . GLN B 1 252 ? 27.42500  19.46500  30.64900 1.000 23.77221 ? 252 GLN B CG  1 
ATOM   4171 C  CD  . GLN B 1 252 ? 28.80300  19.48000  31.32600 1.000 24.40873 ? 252 GLN B CD  1 
ATOM   4172 O  OE1 . GLN B 1 252 ? 29.37900  18.43600  31.60900 1.000 24.38983 ? 252 GLN B OE1 1 
ATOM   4173 N  NE2 . GLN B 1 252 ? 29.32300  20.67200  31.58800 1.000 25.87333 ? 252 GLN B NE2 1 
ATOM   4174 N  N   . ARG B 1 253 ? 24.68700  15.74000  30.20100 1.000 19.84905 ? 253 ARG B N   1 
ATOM   4175 C  CA  . ARG B 1 253 ? 24.31400  14.37700  29.85200 1.000 20.32009 ? 253 ARG B CA  1 
ATOM   4176 C  C   . ARG B 1 253 ? 23.13200  14.36600  28.89100 1.000 19.48347 ? 253 ARG B C   1 
ATOM   4177 O  O   . ARG B 1 253 ? 23.08100  13.53800  27.97400 1.000 19.65328 ? 253 ARG B O   1 
ATOM   4178 C  CB  . ARG B 1 253 ? 24.01600  13.58200  31.12100 1.000 20.95618 ? 253 ARG B CB  1 
ATOM   4179 C  CG  . ARG B 1 253 ? 25.22700  13.47100  32.04600 1.000 21.39200 ? 253 ARG B CG  1 
ATOM   4180 C  CD  . ARG B 1 253 ? 24.92900  12.80500  33.38600 1.000 23.13747 ? 253 ARG B CD  1 
ATOM   4181 N  NE  . ARG B 1 253 ? 24.57500  11.39900  33.24400 1.000 24.58891 ? 253 ARG B NE  1 
ATOM   4182 C  CZ  . ARG B 1 253 ? 23.34200  10.91800  33.34200 1.000 25.38256 ? 253 ARG B CZ  1 
ATOM   4183 N  NH1 . ARG B 1 253 ? 22.31500  11.70000  33.63500 1.000 26.88734 ? 253 ARG B NH1 1 
ATOM   4184 N  NH2 . ARG B 1 253 ? 23.13200  9.61900   33.13400 1.000 23.91577 ? 253 ARG B NH2 1 
ATOM   4185 N  N   . MET B 1 254 ? 22.18600  15.29400  29.06300 1.000 20.27051 ? 254 MET B N   1 
ATOM   4186 C  CA  . MET B 1 254 ? 21.07300  15.39100  28.12300 1.000 19.87236 ? 254 MET B CA  1 
ATOM   4187 C  C   . MET B 1 254 ? 21.56700  15.75100  26.73300 1.000 19.89666 ? 254 MET B C   1 
ATOM   4188 O  O   . MET B 1 254 ? 21.11900  15.17300  25.73900 1.000 20.21030 ? 254 MET B O   1 
ATOM   4189 C  CB  . MET B 1 254 ? 20.03800  16.42700  28.58600 1.000 19.82786 ? 254 MET B CB  1 
ATOM   4190 C  CG  . MET B 1 254 ? 19.25900  16.11300  29.87100 1.000 20.40274 ? 254 MET B CG  1 
ATOM   4191 S  SD  . MET B 1 254 ? 18.32500  14.57300  29.91300 1.000 17.45716 ? 254 MET B SD  1 
ATOM   4192 C  CE  . MET B 1 254 ? 19.36900  13.55100  30.94500 1.000 21.74434 ? 254 MET B CE  1 
ATOM   4193 N  N   . LEU B 1 255 ? 22.49000  16.70300  26.63600 1.000 18.71120 ? 255 LEU B N   1 
ATOM   4194 C  CA  . LEU B 1 255 ? 22.96500  17.13900  25.33200 1.000 20.11434 ? 255 LEU B CA  1 
ATOM   4195 C  C   . LEU B 1 255 ? 24.11200  16.28200  24.80100 1.000 19.76234 ? 255 LEU B C   1 
ATOM   4196 O  O   . LEU B 1 255 ? 24.78600  16.69400  23.85700 1.000 20.17957 ? 255 LEU B O   1 
ATOM   4197 C  CB  . LEU B 1 255 ? 23.36700  18.61600  25.37400 1.000 19.71003 ? 255 LEU B CB  1 
ATOM   4198 C  CG  . LEU B 1 255 ? 22.30100  19.58900  25.88400 1.000 21.21995 ? 255 LEU B CG  1 
ATOM   4199 C  CD1 . LEU B 1 255 ? 22.75600  21.02700  25.73100 1.000 21.34565 ? 255 LEU B CD1 1 
ATOM   4200 C  CD2 . LEU B 1 255 ? 20.97300  19.40000  25.18300 1.000 19.62470 ? 255 LEU B CD2 1 
ATOM   4201 N  N   . GLY B 1 256 ? 24.34000  15.09900  25.36900 1.000 19.51079 ? 256 GLY B N   1 
ATOM   4202 C  CA  . GLY B 1 256 ? 25.22100  14.13200  24.74300 1.000 19.38422 ? 256 GLY B CA  1 
ATOM   4203 C  C   . GLY B 1 256 ? 26.70000  14.31800  24.99600 1.000 20.67378 ? 256 GLY B C   1 
ATOM   4204 O  O   . GLY B 1 256 ? 27.52200  13.73700  24.28700 1.000 20.06273 ? 256 GLY B O   1 
ATOM   4205 N  N   . TRP B 1 257 ? 27.07500  15.09500  25.99900 1.000 20.91137 ? 257 TRP B N   1 
ATOM   4206 C  CA  . TRP B 1 257 ? 28.47500  15.38600  26.24100 1.000 20.81945 ? 257 TRP B CA  1 
ATOM   4207 C  C   . TRP B 1 257 ? 29.10700  14.47700  27.28000 1.000 21.23655 ? 257 TRP B C   1 
ATOM   4208 O  O   . TRP B 1 257 ? 30.27200  14.67900  27.62700 1.000 21.76631 ? 257 TRP B O   1 
ATOM   4209 C  CB  . TRP B 1 257 ? 28.63000  16.84100  26.65900 1.000 21.22237 ? 257 TRP B CB  1 
ATOM   4210 C  CG  . TRP B 1 257 ? 28.48300  17.77600  25.51500 1.000 21.69108 ? 257 TRP B CG  1 
ATOM   4211 C  CD1 . TRP B 1 257 ? 27.32400  18.26600  24.99800 1.000 20.65575 ? 257 TRP B CD1 1 
ATOM   4212 C  CD2 . TRP B 1 257 ? 29.54100  18.32900  24.72800 1.000 22.25263 ? 257 TRP B CD2 1 
ATOM   4213 N  NE1 . TRP B 1 257 ? 27.59600  19.10000  23.94800 1.000 20.86484 ? 257 TRP B NE1 1 
ATOM   4214 C  CE2 . TRP B 1 257 ? 28.95200  19.15400  23.76100 1.000 22.30679 ? 257 TRP B CE2 1 
ATOM   4215 C  CE3 . TRP B 1 257 ? 30.93300  18.21400  24.75800 1.000 23.55807 ? 257 TRP B CE3 1 
ATOM   4216 C  CZ2 . TRP B 1 257 ? 29.70300  19.85900  22.82800 1.000 22.17997 ? 257 TRP B CZ2 1 
ATOM   4217 C  CZ3 . TRP B 1 257 ? 31.67600  18.91600  23.83300 1.000 22.97917 ? 257 TRP B CZ3 1 
ATOM   4218 C  CH2 . TRP B 1 257 ? 31.05900  19.72700  22.88100 1.000 23.70951 ? 257 TRP B CH2 1 
ATOM   4219 N  N   . ARG B 1 258 ? 28.37500  13.48300  27.78200 1.000 21.24398 ? 258 ARG B N   1 
ATOM   4220 C  CA  . ARG B 1 258 ? 28.88800  12.57600  28.79700 1.000 20.65823 ? 258 ARG B CA  1 
ATOM   4221 C  C   . ARG B 1 258 ? 28.64000  11.13600  28.37600 1.000 20.63987 ? 258 ARG B C   1 
ATOM   4222 O  O   . ARG B 1 258 ? 27.86300  10.85600  27.46100 1.000 21.58768 ? 258 ARG B O   1 
ATOM   4223 C  CB  . ARG B 1 258 ? 28.25600  12.84400  30.16800 1.000 20.45136 ? 258 ARG B CB  1 
ATOM   4224 C  CG  . ARG B 1 258 ? 28.60000  14.19600  30.70500 1.000 21.10922 ? 258 ARG B CG  1 
ATOM   4225 C  CD  . ARG B 1 258 ? 28.59200  14.25400  32.21500 1.000 22.34415 ? 258 ARG B CD  1 
ATOM   4226 N  NE  . ARG B 1 258 ? 29.16800  15.50900  32.68600 1.000 23.99744 ? 258 ARG B NE  1 
ATOM   4227 C  CZ  . ARG B 1 258 ? 30.08700  15.60900  33.63900 1.000 23.83912 ? 258 ARG B CZ  1 
ATOM   4228 N  NH1 . ARG B 1 258 ? 30.49600  14.55400  34.31900 1.000 24.46269 ? 258 ARG B NH1 1 
ATOM   4229 N  NH2 . ARG B 1 258 ? 30.60000  16.80100  33.92200 1.000 24.01725 ? 258 ARG B NH2 1 
ATOM   4230 N  N   . THR B 1 259 ? 29.33600  10.22500  29.05600 1.000 20.73765 ? 259 THR B N   1 
ATOM   4231 C  CA  . THR B 1 259 ? 29.11900  8.79300   28.89700 1.000 21.64690 ? 259 THR B CA  1 
ATOM   4232 C  C   . THR B 1 259 ? 27.84300  8.40000   29.62600 1.000 21.65524 ? 259 THR B C   1 
ATOM   4233 O  O   . THR B 1 259 ? 27.51600  8.96700   30.66800 1.000 22.23937 ? 259 THR B O   1 
ATOM   4234 C  CB  . THR B 1 259 ? 30.32400  8.01700   29.43700 1.000 21.72474 ? 259 THR B CB  1 
ATOM   4235 O  OG1 . THR B 1 259 ? 31.41800  8.15900   28.52400 1.000 23.64570 ? 259 THR B OG1 1 
ATOM   4236 C  CG2 . THR B 1 259 ? 30.01800  6.54100   29.61500 1.000 21.25681 ? 259 THR B CG2 1 
ATOM   4237 N  N   . MET B 1 260 ? 27.09500  7.45900   29.05400 1.000 22.39491 ? 260 MET B N   1 
ATOM   4238 C  CA  . MET B 1 260 ? 25.76900  7.11500   29.55600 1.000 22.57186 ? 260 MET B CA  1 
ATOM   4239 C  C   . MET B 1 260 ? 25.63700  5.60200   29.67400 1.000 22.47408 ? 260 MET B C   1 
ATOM   4240 O  O   . MET B 1 260 ? 26.50600  4.83500   29.25500 1.000 22.47763 ? 260 MET B O   1 
ATOM   4241 C  CB  . MET B 1 260 ? 24.66800  7.68500   28.65200 1.000 21.64648 ? 260 MET B CB  1 
ATOM   4242 C  CG  . MET B 1 260 ? 24.81000  9.18100   28.39100 1.000 21.37670 ? 260 MET B CG  1 
ATOM   4243 S  SD  . MET B 1 260 ? 24.44300  10.17500  29.84200 1.000 19.70627 ? 260 MET B SD  1 
ATOM   4244 C  CE  . MET B 1 260 ? 22.65000  10.12700  29.81400 1.000 20.88259 ? 260 MET B CE  1 
ATOM   4245 N  N   . LYS B 1 261 ? 24.51700  5.16700   30.24200 1.000 23.37078 ? 261 LYS B N   1 
ATOM   4246 C  CA  . LYS B 1 261 ? 24.34800  3.76800   30.61900 1.000 24.89218 ? 261 LYS B CA  1 
ATOM   4247 C  C   . LYS B 1 261 ? 22.92100  3.29900   30.34000 1.000 24.75539 ? 261 LYS B C   1 
ATOM   4248 O  O   . LYS B 1 261 ? 21.99800  3.58100   31.12400 1.000 25.12621 ? 261 LYS B O   1 
ATOM   4249 C  CB  . LYS B 1 261 ? 24.72500  3.58700   32.09000 1.000 25.83684 ? 261 LYS B CB  1 
ATOM   4250 C  CG  . LYS B 1 261 ? 24.54200  2.18200   32.67600 1.000 27.27577 ? 261 LYS B CG  1 
ATOM   4251 C  CD  . LYS B 1 261 ? 25.59300  1.20200   32.20600 1.000 27.02756 ? 261 LYS B CD  1 
ATOM   4252 C  CE  . LYS B 1 261 ? 25.48300  -0.09900  32.97900 1.000 30.00484 ? 261 LYS B CE  1 
ATOM   4253 N  NZ  . LYS B 1 261 ? 24.17700  -0.80600  32.76700 1.000 30.22615 ? 261 LYS B NZ  1 
ATOM   4254 N  N   . PRO B 1 262 ? 22.70100  2.57300   29.24300 1.000 24.63826 ? 262 PRO B N   1 
ATOM   4255 C  CA  . PRO B 1 262 ? 21.48900  1.76000   29.14400 1.000 26.13207 ? 262 PRO B CA  1 
ATOM   4256 C  C   . PRO B 1 262 ? 21.43500  0.77000   30.30000 1.000 28.27252 ? 262 PRO B C   1 
ATOM   4257 O  O   . PRO B 1 262 ? 22.45700  0.42300   30.89800 1.000 29.12912 ? 262 PRO B O   1 
ATOM   4258 C  CB  . PRO B 1 262 ? 21.64800  1.04200   27.79700 1.000 25.40138 ? 262 PRO B CB  1 
ATOM   4259 C  CG  . PRO B 1 262 ? 22.63900  1.84000   27.04400 1.000 22.82297 ? 262 PRO B CG  1 
ATOM   4260 C  CD  . PRO B 1 262 ? 23.57300  2.39400   28.07500 1.000 24.44467 ? 262 PRO B CD  1 
ATOM   4261 N  N   . SER B 1 263 ? 20.22600  0.32200   30.63300 1.000 27.82041 ? 263 SER B N   1 
ATOM   4262 C  CA  . SER B 1 263 ? 20.10500  -0.67100  31.69100 1.000 28.14292 ? 263 SER B CA  1 
ATOM   4263 C  C   . SER B 1 263 ? 20.73300  -1.99300  31.24600 1.000 29.76796 ? 263 SER B C   1 
ATOM   4264 O  O   . SER B 1 263 ? 20.91300  -2.26300  30.05700 1.000 30.40387 ? 263 SER B O   1 
ATOM   4265 C  CB  . SER B 1 263 ? 18.63900  -0.87500  32.08300 1.000 29.34471 ? 263 SER B CB  1 
ATOM   4266 O  OG  . SER B 1 263 ? 18.23100  0.02900   33.10400 1.000 30.49288 ? 263 SER B OG  1 
ATOM   4267 N  N   . ASP B 1 264 ? 21.09000  -2.81800  32.22100 1.000 30.80874 ? 264 ASP B N   1 
ATOM   4268 C  CA  . ASP B 1 264 ? 21.66800  -4.11000  31.89200 1.000 31.43743 ? 264 ASP B CA  1 
ATOM   4269 C  C   . ASP B 1 264 ? 20.69900  -4.90800  31.01900 1.000 31.49067 ? 264 ASP B C   1 
ATOM   4270 O  O   . ASP B 1 264 ? 19.48100  -4.80100  31.18700 1.000 32.63266 ? 264 ASP B O   1 
ATOM   4271 C  CB  . ASP B 1 264 ? 22.00300  -4.85800  33.17500 1.000 34.04536 ? 264 ASP B CB  1 
ATOM   4272 C  CG  . ASP B 1 264 ? 22.96300  -4.07800  34.04400 1.000 35.99424 ? 264 ASP B CG  1 
ATOM   4273 O  OD1 . ASP B 1 264 ? 22.48400  -3.21600  34.81400 1.000 38.87198 ? 264 ASP B OD1 1 
ATOM   4274 O  OD2 . ASP B 1 264 ? 24.19300  -4.27200  33.90700 1.000 35.19635 ? 264 ASP B OD2 1 
ATOM   4275 N  N   . PRO B 1 265 ? 21.20400  -5.74100  30.07600 1.000 31.97857 ? 265 PRO B N   1 
ATOM   4276 C  CA  . PRO B 1 265 ? 22.57400  -6.25700  29.89100 1.000 30.73515 ? 265 PRO B CA  1 
ATOM   4277 C  C   . PRO B 1 265 ? 23.65100  -5.32200  29.32400 1.000 32.89849 ? 265 PRO B C   1 
ATOM   4278 O  O   . PRO B 1 265 ? 24.79600  -5.76700  29.22000 1.000 32.33478 ? 265 PRO B O   1 
ATOM   4279 C  CB  . PRO B 1 265 ? 22.35400  -7.43500  28.93100 1.000 29.33958 ? 265 PRO B CB  1 
ATOM   4280 C  CG  . PRO B 1 265 ? 21.20400  -7.02000  28.10600 1.000 31.10548 ? 265 PRO B CG  1 
ATOM   4281 C  CD  . PRO B 1 265 ? 20.29100  -6.29700  29.05900 1.000 31.23799 ? 265 PRO B CD  1 
ATOM   4282 N  N   . ASN B 1 266 ? 23.40800  -4.07500  28.93400 1.000 30.84514 ? 266 ASN B N   1 
ATOM   4283 C  CA  . ASN B 1 266 ? 24.54700  -3.20000  28.68100 1.000 29.36128 ? 266 ASN B CA  1 
ATOM   4284 C  C   . ASN B 1 266 ? 25.24400  -2.97500  30.00900 1.000 29.83175 ? 266 ASN B C   1 
ATOM   4285 O  O   . ASN B 1 266 ? 24.79600  -2.16900  30.82700 1.000 30.99116 ? 266 ASN B O   1 
ATOM   4286 C  CB  . ASN B 1 266 ? 24.11900  -1.87800  28.06400 1.000 27.38763 ? 266 ASN B CB  1 
ATOM   4287 C  CG  . ASN B 1 266 ? 25.28700  -0.94800  27.84800 1.000 26.85110 ? 266 ASN B CG  1 
ATOM   4288 O  OD1 . ASN B 1 266 ? 25.93900  -0.52700  28.80200 1.000 27.13085 ? 266 ASN B OD1 1 
ATOM   4289 N  ND2 . ASN B 1 266 ? 25.55900  -0.61500  26.59100 1.000 26.38851 ? 266 ASN B ND2 1 
ATOM   4290 N  N   . ILE B 1 267 ? 26.35000  -3.68800  30.22800 1.000 29.80653 ? 267 ILE B N   1 
ATOM   4291 C  CA  . ILE B 1 267 ? 27.05100  -3.65900  31.50800 1.000 29.88264 ? 267 ILE B CA  1 
ATOM   4292 C  C   . ILE B 1 267 ? 28.24700  -2.72400  31.50400 1.000 28.50656 ? 267 ILE B C   1 
ATOM   4293 O  O   . ILE B 1 267 ? 28.97200  -2.66400  32.50200 1.000 29.13997 ? 267 ILE B O   1 
ATOM   4294 C  CB  . ILE B 1 267 ? 27.51400  -5.06700  31.93600 1.000 29.18297 ? 267 ILE B CB  1 
ATOM   4295 C  CG1 . ILE B 1 267 ? 28.61700  -5.57300  31.00100 1.000 27.94089 ? 267 ILE B CG1 1 
ATOM   4296 C  CG2 . ILE B 1 267 ? 26.33900  -6.03400  32.01400 1.000 28.98128 ? 267 ILE B CG2 1 
ATOM   4297 C  CD1 . ILE B 1 267 ? 29.45800  -6.69500  31.60600 1.000 27.94076 ? 267 ILE B CD1 1 
ATOM   4298 N  N   . VAL B 1 268 ? 28.48400  -1.99900  30.42200 1.000 27.18211 ? 268 VAL B N   1 
ATOM   4299 C  CA  . VAL B 1 268 ? 29.62200  -1.09400  30.31900 1.000 26.50651 ? 268 VAL B CA  1 
ATOM   4300 C  C   . VAL B 1 268 ? 29.17300  0.36600   30.36100 1.000 27.24157 ? 268 VAL B C   1 
ATOM   4301 O  O   . VAL B 1 268 ? 29.55800  1.12000   31.25700 1.000 28.05453 ? 268 VAL B O   1 
ATOM   4302 C  CB  . VAL B 1 268 ? 30.45100  -1.39600  29.05000 1.000 25.75125 ? 268 VAL B CB  1 
ATOM   4303 C  CG1 . VAL B 1 268 ? 31.51500  -0.32300  28.81700 1.000 23.82372 ? 268 VAL B CG1 1 
ATOM   4304 C  CG2 . VAL B 1 268 ? 31.08400  -2.79100  29.15500 1.000 26.36276 ? 268 VAL B CG2 1 
ATOM   4305 N  N   . GLY B 1 269 ? 28.34500  0.77300   29.41500 1.000 25.91454 ? 269 GLY B N   1 
ATOM   4306 C  CA  . GLY B 1 269 ? 27.97100  2.15200   29.21900 1.000 24.16252 ? 269 GLY B CA  1 
ATOM   4307 C  C   . GLY B 1 269 ? 27.85700  2.43400   27.74000 1.000 22.51937 ? 269 GLY B C   1 
ATOM   4308 O  O   . GLY B 1 269 ? 27.88400  1.52800   26.91100 1.000 22.79036 ? 269 GLY B O   1 
ATOM   4309 N  N   . ILE B 1 270 ? 27.72500  3.70800   27.38800 1.000 21.33146 ? 270 ILE B N   1 
ATOM   4310 C  CA  . ILE B 1 270 ? 27.64300  4.10500   25.98700 1.000 21.40439 ? 270 ILE B CA  1 
ATOM   4311 C  C   . ILE B 1 270 ? 28.17700  5.52300   25.86600 1.000 20.95914 ? 270 ILE B C   1 
ATOM   4312 O  O   . ILE B 1 270 ? 28.23400  6.27000   26.84400 1.000 20.95244 ? 270 ILE B O   1 
ATOM   4313 C  CB  . ILE B 1 270 ? 26.19400  3.99200   25.44500 1.000 21.62955 ? 270 ILE B CB  1 
ATOM   4314 C  CG1 . ILE B 1 270 ? 26.19500  3.57900   23.98400 1.000 20.36947 ? 270 ILE B CG1 1 
ATOM   4315 C  CG2 . ILE B 1 270 ? 25.43000  5.30700   25.58400 1.000 21.90571 ? 270 ILE B CG2 1 
ATOM   4316 C  CD1 . ILE B 1 270 ? 24.88400  3.00400   23.52300 1.000 20.55981 ? 270 ILE B CD1 1 
ATOM   4317 N  N   . ASN B 1 271 ? 28.57900  5.89000   24.64700 1.000 20.29132 ? 271 ASN B N   1 
ATOM   4318 C  CA  . ASN B 1 271 ? 29.11700  7.21600   24.36300 1.000 20.49732 ? 271 ASN B CA  1 
ATOM   4319 C  C   . ASN B 1 271 ? 30.43900  7.39200   25.09600 1.000 19.69084 ? 271 ASN B C   1 
ATOM   4320 O  O   . ASN B 1 271 ? 30.57600  8.30300   25.91400 1.000 19.92913 ? 271 ASN B O   1 
ATOM   4321 C  CB  . ASN B 1 271 ? 28.11300  8.31900   24.76000 1.000 19.91607 ? 271 ASN B CB  1 
ATOM   4322 C  CG  . ASN B 1 271 ? 28.44200  9.68300   24.15100 1.000 19.75576 ? 271 ASN B CG  1 
ATOM   4323 O  OD1 . ASN B 1 271 ? 28.95800  9.76700   23.03300 1.000 20.43457 ? 271 ASN B OD1 1 
ATOM   4324 N  ND2 . ASN B 1 271 ? 28.14600  10.75900  24.89400 1.000 19.55182 ? 271 ASN B ND2 1 
ATOM   4325 N  N   . LEU B 1 272 ? 31.41800  6.53500   24.80900 1.000 19.33236 ? 272 LEU B N   1 
ATOM   4326 C  CA  . LEU B 1 272 ? 32.70300  6.55800   25.49200 1.000 19.98969 ? 272 LEU B CA  1 
ATOM   4327 C  C   . LEU B 1 272 ? 33.82200  6.43300   24.46000 1.000 21.48426 ? 272 LEU B C   1 
ATOM   4328 O  O   . LEU B 1 272 ? 33.58500  6.11400   23.29400 1.000 21.75437 ? 272 LEU B O   1 
ATOM   4329 C  CB  . LEU B 1 272 ? 32.76600  5.44100   26.54000 1.000 20.90725 ? 272 LEU B CB  1 
ATOM   4330 C  CG  . LEU B 1 272 ? 32.62600  4.04200   25.94300 1.000 21.06338 ? 272 LEU B CG  1 
ATOM   4331 C  CD1 . LEU B 1 272 ? 33.96500  3.33000   25.91800 1.000 22.68008 ? 272 LEU B CD1 1 
ATOM   4332 C  CD2 . LEU B 1 272 ? 31.59800  3.22800   26.69300 1.000 21.48532 ? 272 LEU B CD2 1 
ATOM   4333 N  N   . ILE B 1 273 ? 35.05900  6.70100   24.87500 1.000 20.76546 ? 273 ILE B N   1 
ATOM   4334 C  CA  . ILE B 1 273 ? 36.17800  6.65800   23.94100 1.000 22.99145 ? 273 ILE B CA  1 
ATOM   4335 C  C   . ILE B 1 273 ? 37.45400  6.49100   24.74300 1.000 22.49068 ? 273 ILE B C   1 
ATOM   4336 O  O   . ILE B 1 273 ? 37.54900  6.94000   25.88400 1.000 22.35824 ? 273 ILE B O   1 
ATOM   4337 C  CB  . ILE B 1 273 ? 36.21600  7.92500   23.04300 1.000 23.56341 ? 273 ILE B CB  1 
ATOM   4338 C  CG1 . ILE B 1 273 ? 37.23200  7.79200   21.89000 1.000 23.66243 ? 273 ILE B CG1 1 
ATOM   4339 C  CG2 . ILE B 1 273 ? 36.51600  9.16800   23.87300 1.000 23.88162 ? 273 ILE B CG2 1 
ATOM   4340 C  CD1 . ILE B 1 273 ? 36.84000  6.81300   20.79200 1.000 21.51670 ? 273 ILE B CD1 1 
ATOM   4341 N  N   . ASP B 1 274 ? 38.43900  5.83400   24.13600 1.000 23.14149 ? 274 ASP B N   1 
ATOM   4342 C  CA  . ASP B 1 274 ? 39.69200  5.50200   24.80400 1.000 23.29852 ? 274 ASP B CA  1 
ATOM   4343 C  C   . ASP B 1 274 ? 39.45000  4.66900   26.05600 1.000 23.63693 ? 274 ASP B C   1 
ATOM   4344 O  O   . ASP B 1 274 ? 40.21900  4.73700   27.01400 1.000 24.28177 ? 274 ASP B O   1 
ATOM   4345 C  CB  . ASP B 1 274 ? 40.48600  6.76300   25.13300 1.000 23.15319 ? 274 ASP B CB  1 
ATOM   4346 C  CG  . ASP B 1 274 ? 40.88200  7.51800   23.89900 1.000 25.88318 ? 274 ASP B CG  1 
ATOM   4347 O  OD1 . ASP B 1 274 ? 41.05000  6.85400   22.85200 1.000 25.29375 ? 274 ASP B OD1 1 
ATOM   4348 O  OD2 . ASP B 1 274 ? 41.02400  8.76000   23.96000 1.000 27.77351 ? 274 ASP B OD2 1 
ATOM   4349 N  N   . ASP B 1 275 ? 38.37500  3.87800   26.04300 1.000 23.21289 ? 275 ASP B N   1 
ATOM   4350 C  CA  . ASP B 1 275 ? 37.89300  3.12300   27.19900 1.000 22.58537 ? 275 ASP B CA  1 
ATOM   4351 C  C   . ASP B 1 275 ? 37.69300  4.02200   28.41500 1.000 24.24156 ? 275 ASP B C   1 
ATOM   4352 O  O   . ASP B 1 275 ? 37.69300  3.55400   29.55400 1.000 25.18288 ? 275 ASP B O   1 
ATOM   4353 C  CB  . ASP B 1 275 ? 38.83000  1.96100   27.53300 1.000 23.98438 ? 275 ASP B CB  1 
ATOM   4354 C  CG  . ASP B 1 275 ? 38.09100  0.75700   28.06200 1.000 25.01243 ? 275 ASP B CG  1 
ATOM   4355 O  OD1 . ASP B 1 275 ? 36.84000  0.76600   28.01000 1.000 25.67932 ? 275 ASP B OD1 1 
ATOM   4356 O  OD2 . ASP B 1 275 ? 38.75500  -0.19200  28.53000 1.000 25.94230 ? 275 ASP B OD2 1 
ATOM   4357 N  N   . LYS B 1 276 ? 37.52600  5.31900   28.18300 1.000 24.18532 ? 276 LYS B N   1 
ATOM   4358 C  CA  . LYS B 1 276 ? 37.31700  6.29600   29.23600 1.000 23.64252 ? 276 LYS B CA  1 
ATOM   4359 C  C   . LYS B 1 276 ? 35.98600  6.99800   29.02200 1.000 22.23178 ? 276 LYS B C   1 
ATOM   4360 O  O   . LYS B 1 276 ? 35.44500  7.03800   27.91700 1.000 21.50237 ? 276 LYS B O   1 
ATOM   4361 C  CB  . LYS B 1 276 ? 38.44900  7.33600   29.27000 1.000 24.69335 ? 276 LYS B CB  1 
ATOM   4362 C  CG  . LYS B 1 276 ? 39.77900  6.79400   29.76000 1.000 26.22867 ? 276 LYS B CG  1 
ATOM   4363 C  CD  . LYS B 1 276 ? 40.94300  7.15300   28.83100 1.000 27.69462 ? 276 LYS B CD  1 
ATOM   4364 C  CE  . LYS B 1 276 ? 41.17100  8.65400   28.71100 1.000 29.23623 ? 276 LYS B CE  1 
ATOM   4365 N  NZ  . LYS B 1 276 ? 42.37500  9.00000   27.86700 1.000 30.08743 ? 276 LYS B NZ  1 
ATOM   4366 N  N   . ARG B 1 277 ? 35.46900  7.55100   30.10900 1.000 22.67735 ? 277 ARG B N   1 
ATOM   4367 C  CA  . ARG B 1 277 ? 34.28700  8.38600   30.04800 1.000 22.81025 ? 277 ARG B CA  1 
ATOM   4368 C  C   . ARG B 1 277 ? 34.57700  9.62900   29.22200 1.000 23.45949 ? 277 ARG B C   1 
ATOM   4369 O  O   . ARG B 1 277 ? 35.62300  10.25800  29.38200 1.000 24.41226 ? 277 ARG B O   1 
ATOM   4370 C  CB  . ARG B 1 277 ? 33.86000  8.74200   31.46900 1.000 24.03801 ? 277 ARG B CB  1 
ATOM   4371 C  CG  . ARG B 1 277 ? 33.94300  7.51600   32.39300 1.000 25.58413 ? 277 ARG B CG  1 
ATOM   4372 C  CD  . ARG B 1 277 ? 33.57300  7.80200   33.83000 1.000 26.53164 ? 277 ARG B CD  1 
ATOM   4373 N  NE  . ARG B 1 277 ? 32.16400  8.13900   33.95800 1.000 27.53051 ? 277 ARG B NE  1 
ATOM   4374 C  CZ  . ARG B 1 277 ? 31.17200  7.26200   33.91100 1.000 26.67350 ? 277 ARG B CZ  1 
ATOM   4375 N  NH1 . ARG B 1 277 ? 31.39500  5.97000   33.74900 1.000 29.03620 ? 277 ARG B NH1 1 
ATOM   4376 N  NH2 . ARG B 1 277 ? 29.92300  7.69500   34.02400 1.000 24.94875 ? 277 ARG B NH2 1 
ATOM   4377 N  N   . LEU B 1 278 ? 33.65200  9.96900   28.32000 1.000 23.50088 ? 278 LEU B N   1 
ATOM   4378 C  CA  . LEU B 1 278 ? 33.87000  11.09000  27.40800 1.000 24.01181 ? 278 LEU B CA  1 
ATOM   4379 C  C   . LEU B 1 278 ? 34.17300  12.37900  28.16300 1.000 23.96258 ? 278 LEU B C   1 
ATOM   4380 O  O   . LEU B 1 278 ? 35.01200  13.17700  27.73400 1.000 23.39320 ? 278 LEU B O   1 
ATOM   4381 C  CB  . LEU B 1 278 ? 32.64600  11.27700  26.50900 1.000 22.85990 ? 278 LEU B CB  1 
ATOM   4382 C  CG  . LEU B 1 278 ? 32.71500  12.47900  25.56600 1.000 22.56749 ? 278 LEU B CG  1 
ATOM   4383 C  CD1 . LEU B 1 278 ? 33.77700  12.24400  24.48300 1.000 22.65342 ? 278 LEU B CD1 1 
ATOM   4384 C  CD2 . LEU B 1 278 ? 31.36100  12.78300  24.96100 1.000 21.49328 ? 278 LEU B CD2 1 
ATOM   4385 N  N   . GLU B 1 279 ? 33.50100  12.59800  29.29200 1.000 24.04525 ? 279 GLU B N   1 
ATOM   4386 C  CA  . GLU B 1 279 ? 33.73800  13.80500  30.06900 1.000 25.19179 ? 279 GLU B CA  1 
ATOM   4387 C  C   . GLU B 1 279 ? 35.13300  13.83400  30.68500 1.000 24.89219 ? 279 GLU B C   1 
ATOM   4388 O  O   . GLU B 1 279 ? 35.63500  14.92200  30.98900 1.000 26.48815 ? 279 GLU B O   1 
ATOM   4389 C  CB  . GLU B 1 279 ? 32.66100  13.95500  31.14800 1.000 23.72482 ? 279 GLU B CB  1 
ATOM   4390 C  CG  . GLU B 1 279 ? 32.64900  12.86700  32.21100 1.000 24.21474 ? 279 GLU B CG  1 
ATOM   4391 C  CD  . GLU B 1 279 ? 31.70400  11.72100  31.89600 1.000 24.26270 ? 279 GLU B CD  1 
ATOM   4392 O  OE1 . GLU B 1 279 ? 31.36200  11.51000  30.71500 1.000 23.37280 ? 279 GLU B OE1 1 
ATOM   4393 O  OE2 . GLU B 1 279 ? 31.29400  11.02500  32.83700 1.000 24.69941 ? 279 GLU B OE2 1 
ATOM   4394 N  N   . ASN B 1 280 ? 35.78200  12.67400  30.85100 1.000 25.62428 ? 280 ASN B N   1 
ATOM   4395 C  CA  . ASN B 1 280 ? 37.15700  12.61900  31.34600 1.000 24.53970 ? 280 ASN B CA  1 
ATOM   4396 C  C   . ASN B 1 280 ? 38.19500  12.71400  30.23100 1.000 25.26738 ? 280 ASN B C   1 
ATOM   4397 O  O   . ASN B 1 280 ? 39.28000  13.25000  30.45700 1.000 26.26045 ? 280 ASN B O   1 
ATOM   4398 C  CB  . ASN B 1 280 ? 37.37100  11.33700  32.15600 1.000 24.77408 ? 280 ASN B CB  1 
ATOM   4399 C  CG  . ASN B 1 280 ? 36.54600  11.30800  33.44600 1.000 27.80253 ? 280 ASN B CG  1 
ATOM   4400 O  OD1 . ASN B 1 280 ? 36.29400  12.34600  34.05300 1.000 29.51116 ? 280 ASN B OD1 1 
ATOM   4401 N  ND2 . ASN B 1 280 ? 36.12700  10.11600  33.86600 1.000 26.86392 ? 280 ASN B ND2 1 
ATOM   4402 N  N   . VAL B 1 281 ? 37.89300  12.21600  29.03200 1.000 25.33894 ? 281 VAL B N   1 
ATOM   4403 C  CA  . VAL B 1 281 ? 38.77200  12.45300  27.89100 1.000 26.49045 ? 281 VAL B CA  1 
ATOM   4404 C  C   . VAL B 1 281 ? 38.80000  13.93300  27.54800 1.000 26.99436 ? 281 VAL B C   1 
ATOM   4405 O  O   . VAL B 1 281 ? 39.84800  14.48700  27.20700 1.000 27.72915 ? 281 VAL B O   1 
ATOM   4406 C  CB  . VAL B 1 281 ? 38.33000  11.60800  26.68400 1.000 26.28996 ? 281 VAL B CB  1 
ATOM   4407 C  CG1 . VAL B 1 281 ? 39.16200  11.95400  25.48600 1.000 26.26926 ? 281 VAL B CG1 1 
ATOM   4408 C  CG2 . VAL B 1 281 ? 38.46800  10.13400  26.98900 1.000 26.62435 ? 281 VAL B CG2 1 
ATOM   4409 N  N   . LEU B 1 282 ? 37.64800  14.59500  27.62300 1.000 25.98449 ? 282 LEU B N   1 
ATOM   4410 C  CA  . LEU B 1 282 ? 37.56200  16.02200  27.35500 1.000 25.85224 ? 282 LEU B CA  1 
ATOM   4411 C  C   . LEU B 1 282 ? 37.91500  16.86300  28.56800 1.000 26.91666 ? 282 LEU B C   1 
ATOM   4412 O  O   . LEU B 1 282 ? 37.99200  18.08700  28.44100 1.000 28.20426 ? 282 LEU B O   1 
ATOM   4413 C  CB  . LEU B 1 282 ? 36.15000  16.40300  26.88900 1.000 25.16622 ? 282 LEU B CB  1 
ATOM   4414 C  CG  . LEU B 1 282 ? 35.59000  15.89900  25.55400 1.000 24.56159 ? 282 LEU B CG  1 
ATOM   4415 C  CD1 . LEU B 1 282 ? 34.10800  16.23900  25.46400 1.000 23.97533 ? 282 LEU B CD1 1 
ATOM   4416 C  CD2 . LEU B 1 282 ? 36.33800  16.48200  24.37700 1.000 22.90760 ? 282 LEU B CD2 1 
ATOM   4417 N  N   . GLN B 1 283 ? 38.11300  16.23500  29.72500 1.000 26.07490 ? 283 GLN B N   1 
ATOM   4418 C  CA  . GLN B 1 283 ? 38.33600  16.92000  30.99400 1.000 26.49778 ? 283 GLN B CA  1 
ATOM   4419 C  C   . GLN B 1 283 ? 37.33300  18.05600  31.16900 1.000 27.26806 ? 283 GLN B C   1 
ATOM   4420 O  O   . GLN B 1 283 ? 37.67800  19.23000  31.31400 1.000 27.47495 ? 283 GLN B O   1 
ATOM   4421 C  CB  . GLN B 1 283 ? 39.77700  17.41000  31.09900 1.000 28.17952 ? 283 GLN B CB  1 
ATOM   4422 C  CG  . GLN B 1 283 ? 40.79500  16.29000  30.99700 1.000 27.49478 ? 283 GLN B CG  1 
ATOM   4423 C  CD  . GLN B 1 283 ? 42.12800  16.77900  30.49000 1.000 31.17310 ? 283 GLN B CD  1 
ATOM   4424 O  OE1 . GLN B 1 283 ? 42.69500  16.22600  29.54300 1.000 34.03371 ? 283 GLN B OE1 1 
ATOM   4425 N  NE2 . GLN B 1 283 ? 42.64000  17.82700  31.11600 1.000 32.82224 ? 283 GLN B NE2 1 
ATOM   4426 N  N   . LEU B 1 284 ? 36.06300  17.66100  31.14600 1.000 27.44181 ? 284 LEU B N   1 
ATOM   4427 C  CA  . LEU B 1 284 ? 34.95100  18.59500  31.11700 1.000 26.40399 ? 284 LEU B CA  1 
ATOM   4428 C  C   . LEU B 1 284 ? 34.63500  19.09600  32.51800 1.000 26.77552 ? 284 LEU B C   1 
ATOM   4429 O  O   . LEU B 1 284 ? 34.43700  18.29900  33.44100 1.000 27.37473 ? 284 LEU B O   1 
ATOM   4430 C  CB  . LEU B 1 284 ? 33.73000  17.90900  30.51600 1.000 26.09362 ? 284 LEU B CB  1 
ATOM   4431 C  CG  . LEU B 1 284 ? 32.85400  18.65500  29.51500 1.000 25.40314 ? 284 LEU B CG  1 
ATOM   4432 C  CD1 . LEU B 1 284 ? 33.66500  19.07700  28.31800 1.000 26.15098 ? 284 LEU B CD1 1 
ATOM   4433 C  CD2 . LEU B 1 284 ? 31.72200  17.74800  29.08900 1.000 23.71942 ? 284 LEU B CD2 1 
ATOM   4434 N  N   . LYS B 1 285 ? 34.58800  20.41600  32.67000 1.000 28.17109 ? 285 LYS B N   1 
ATOM   4435 C  CA  . LYS B 1 285 ? 34.08000  21.04700  33.87800 1.000 28.70499 ? 285 LYS B CA  1 
ATOM   4436 C  C   . LYS B 1 285 ? 32.57600  21.26600  33.73700 1.000 28.78475 ? 285 LYS B C   1 
ATOM   4437 O  O   . LYS B 1 285 ? 32.04000  21.36300  32.62600 1.000 26.94388 ? 285 LYS B O   1 
ATOM   4438 C  CB  . LYS B 1 285 ? 34.79600  22.37800  34.14200 1.000 29.51211 ? 285 LYS B CB  1 
ATOM   4439 C  CG  . LYS B 1 285 ? 36.32600  22.25800  34.29400 1.000 31.58950 ? 285 LYS B CG  1 
ATOM   4440 C  CD  . LYS B 1 285 ? 37.01000  23.59900  34.61900 1.000 31.38970 ? 285 LYS B CD  1 
ATOM   4441 C  CE  . LYS B 1 285 ? 38.54100  23.49300  34.55400 1.000 30.71903 ? 285 LYS B CE  1 
ATOM   4442 N  NZ  . LYS B 1 285 ? 39.25100  24.75600  34.95300 1.000 32.16057 ? 285 LYS B NZ  1 
ATOM   4443 N  N   . ALA B 1 286 ? 31.89200  21.31600  34.87600 1.000 29.62868 ? 286 ALA B N   1 
ATOM   4444 C  CA  . ALA B 1 286 ? 30.45300  21.52800  34.90900 1.000 29.92731 ? 286 ALA B CA  1 
ATOM   4445 C  C   . ALA B 1 286 ? 30.13300  22.50500  36.02500 1.000 31.24601 ? 286 ALA B C   1 
ATOM   4446 O  O   . ALA B 1 286 ? 30.85800  22.58500  37.02200 1.000 32.09470 ? 286 ALA B O   1 
ATOM   4447 C  CB  . ALA B 1 286 ? 29.67500  20.22900  35.13500 1.000 28.52840 ? 286 ALA B CB  1 
ATOM   4448 N  N   . ALA B 1 287 ? 29.02600  23.23600  35.85200 1.000 29.43292 ? 287 ALA B N   1 
ATOM   4449 C  CA  . ALA B 1 287 ? 28.62400  24.23000  36.84600 1.000 29.49518 ? 287 ALA B CA  1 
ATOM   4450 C  C   . ALA B 1 287 ? 28.54900  23.63100  38.24800 1.000 29.53041 ? 287 ALA B C   1 
ATOM   4451 O  O   . ALA B 1 287 ? 28.83100  24.31800  39.23600 1.000 29.13695 ? 287 ALA B O   1 
ATOM   4452 C  CB  . ALA B 1 287 ? 27.28200  24.86200  36.45200 1.000 28.67374 ? 287 ALA B CB  1 
ATOM   4453 N  N   . ASP B 1 288 ? 28.20400  22.35300  38.35500 1.000 30.95380 ? 288 ASP B N   1 
ATOM   4454 C  CA  . ASP B 1 288 ? 28.15700  21.65300  39.62800 1.000 30.27618 ? 288 ASP B CA  1 
ATOM   4455 C  C   . ASP B 1 288 ? 29.14800  20.49400  39.66000 1.000 33.16303 ? 288 ASP B C   1 
ATOM   4456 O  O   . ASP B 1 288 ? 28.88300  19.44500  40.24800 1.000 34.56790 ? 288 ASP B O   1 
ATOM   4457 C  CB  . ASP B 1 288 ? 26.74100  21.17000  39.92300 1.000 28.52486 ? 288 ASP B CB  1 
ATOM   4458 C  CG  . ASP B 1 288 ? 26.10600  20.46400  38.75500 1.000 27.17545 ? 288 ASP B CG  1 
ATOM   4459 O  OD1 . ASP B 1 288 ? 26.67100  20.53000  37.66100 1.000 27.88540 ? 288 ASP B OD1 1 
ATOM   4460 O  OD2 . ASP B 1 288 ? 25.03900  19.84200  38.92400 1.000 27.24006 ? 288 ASP B OD2 1 
ATOM   4461 N  N   . SER B 1 289 ? 30.30500  20.71400  39.03400 1.000 40.63359 ? 289 SER B N   1 
ATOM   4462 C  CA  . SER B 1 289 ? 31.40500  19.71400  38.99100 1.000 41.19178 ? 289 SER B CA  1 
ATOM   4463 C  C   . SER B 1 289 ? 31.82200  19.29100  40.40700 1.000 45.99862 ? 289 SER B C   1 
ATOM   4464 O  O   . SER B 1 289 ? 31.70700  18.09900  40.70800 1.000 50.68502 ? 289 SER B O   1 
ATOM   4465 C  CB  . SER B 1 289 ? 32.58000  20.28500  38.24800 1.000 39.67727 ? 289 SER B CB  1 
ATOM   4466 O  OG  . SER B 1 289 ? 32.44200  20.16200  36.84700 1.000 40.23031 ? 289 SER B OG  1 
HETATM 4467 CO CO  . CO  C 2 .   ? 30.15400  -11.37000 20.42200 1.000 29.00016 ? 401 CO  A CO  1 
HETATM 4468 C  C1  . AKG D 3 .   ? 32.47800  -10.80900 21.71700 1.000 32.08264 ? 402 AKG A C1  1 
HETATM 4469 O  O1  . AKG D 3 .   ? 33.27200  -10.35300 22.53900 1.000 32.56328 ? 402 AKG A O1  1 
HETATM 4470 O  O2  . AKG D 3 .   ? 31.25400  -10.39400 21.56600 1.000 32.07103 ? 402 AKG A O2  1 
HETATM 4471 C  C2  . AKG D 3 .   ? 32.88200  -11.96000 20.77900 1.000 32.93435 ? 402 AKG A C2  1 
HETATM 4472 O  O5  . AKG D 3 .   ? 32.09600  -12.34200 19.92100 1.000 32.00993 ? 402 AKG A O5  1 
HETATM 4473 C  C3  . AKG D 3 .   ? 34.24400  -12.57600 20.98200 1.000 32.38834 ? 402 AKG A C3  1 
HETATM 4474 C  C4  . AKG D 3 .   ? 35.13300  -12.48800 19.75800 1.000 31.99484 ? 402 AKG A C4  1 
HETATM 4475 C  C5  . AKG D 3 .   ? 34.83300  -13.52900 18.73700 1.000 31.43710 ? 402 AKG A C5  1 
HETATM 4476 O  O3  . AKG D 3 .   ? 33.82600  -13.51300 18.06200 1.000 33.22784 ? 402 AKG A O3  1 
HETATM 4477 O  O4  . AKG D 3 .   ? 35.76500  -14.44400 18.64000 1.000 31.90775 ? 402 AKG A O4  1 
HETATM 4478 C  C1  . GOL E 4 .   ? 41.96900  -16.57200 34.41400 1.000 35.05036 ? 403 GOL A C1  1 
HETATM 4479 O  O1  . GOL E 4 .   ? 40.68400  -17.09300 34.60000 1.000 32.58656 ? 403 GOL A O1  1 
HETATM 4480 C  C2  . GOL E 4 .   ? 42.79100  -17.60900 33.61000 1.000 37.58034 ? 403 GOL A C2  1 
HETATM 4481 O  O2  . GOL E 4 .   ? 43.56800  -17.04200 32.63000 1.000 39.82660 ? 403 GOL A O2  1 
HETATM 4482 C  C3  . GOL E 4 .   ? 43.61600  -18.36100 34.65800 1.000 34.77673 ? 403 GOL A C3  1 
HETATM 4483 O  O3  . GOL E 4 .   ? 42.67700  -18.84400 35.54900 1.000 36.17785 ? 403 GOL A O3  1 
HETATM 4484 S  S   . SO4 F 5 .   ? 25.65600  11.61900  19.29200 1.000 36.74314 ? 501 SO4 B S   1 
HETATM 4485 O  O1  . SO4 F 5 .   ? 26.82000  11.99100  18.53600 1.000 31.16250 ? 501 SO4 B O1  1 
HETATM 4486 O  O2  . SO4 F 5 .   ? 24.67500  12.64700  19.18400 1.000 26.44861 ? 501 SO4 B O2  1 
HETATM 4487 O  O3  . SO4 F 5 .   ? 26.01700  11.44000  20.67000 1.000 26.97444 ? 501 SO4 B O3  1 
HETATM 4488 O  O4  . SO4 F 5 .   ? 25.13800  10.39100  18.78200 1.000 28.79333 ? 501 SO4 B O4  1 
HETATM 4489 CO CO  . CO  G 2 .   ? 3.95900   14.80200  17.84900 1.000 27.44002 ? 502 CO  B CO  1 
HETATM 4490 C  C1  . AKG H 3 .   ? 4.57900   17.69700  16.29800 1.000 28.91728 ? 503 AKG B C1  1 
HETATM 4491 O  O1  . AKG H 3 .   ? 4.93300   16.54900  16.06700 1.000 29.72383 ? 503 AKG B O1  1 
HETATM 4492 O  O2  . AKG H 3 .   ? 5.07500   18.75700  15.70700 1.000 29.91573 ? 503 AKG B O2  1 
HETATM 4493 C  C2  . AKG H 3 .   ? 3.47700   17.99500  17.33300 1.000 29.40890 ? 503 AKG B C2  1 
HETATM 4494 O  O5  . AKG H 3 .   ? 2.94400   17.08300  17.95500 1.000 29.09473 ? 503 AKG B O5  1 
HETATM 4495 C  C3  . AKG H 3 .   ? 3.10200   19.43700  17.52600 1.000 29.05134 ? 503 AKG B C3  1 
HETATM 4496 C  C4  . AKG H 3 .   ? 1.74400   19.61400  18.17600 1.000 28.02944 ? 503 AKG B C4  1 
HETATM 4497 C  C5  . AKG H 3 .   ? 1.36000   21.05300  18.35200 1.000 27.31015 ? 503 AKG B C5  1 
HETATM 4498 O  O3  . AKG H 3 .   ? 0.80100   21.47000  19.34700 1.000 29.09658 ? 503 AKG B O3  1 
HETATM 4499 O  O4  . AKG H 3 .   ? 1.68400   21.80200  17.33600 1.000 26.92437 ? 503 AKG B O4  1 
HETATM 4500 O  O   . HOH I 6 .   ? 53.68400  -1.78200  27.87500 1.000 42.60107 ? 501 HOH A O   1 
HETATM 4501 O  O   . HOH I 6 .   ? 33.03600  -23.94500 9.88800  1.000 31.14137 ? 502 HOH A O   1 
HETATM 4502 O  O   . HOH I 6 .   ? 31.01700  -10.63800 18.75300 1.000 29.50758 ? 503 HOH A O   1 
HETATM 4503 O  O   . HOH I 6 .   ? 40.93300  -17.88900 21.23600 1.000 34.31365 ? 504 HOH A O   1 
HETATM 4504 O  O   . HOH I 6 .   ? 30.27500  10.16600  17.92800 1.000 22.29929 ? 505 HOH A O   1 
HETATM 4505 O  O   . HOH I 6 .   ? 45.22600  -12.37600 25.88400 1.000 35.91299 ? 506 HOH A O   1 
HETATM 4506 O  O   . HOH I 6 .   ? 48.50300  19.74600  13.21700 1.000 37.72324 ? 507 HOH A O   1 
HETATM 4507 O  O   . HOH I 6 .   ? 34.27800  -16.30600 -8.09100 1.000 41.38700 ? 508 HOH A O   1 
HETATM 4508 O  O   . HOH I 6 .   ? 36.80100  10.34200  19.74400 1.000 22.06664 ? 509 HOH A O   1 
HETATM 4509 O  O   . HOH I 6 .   ? 43.17300  2.39800   20.03700 1.000 23.81860 ? 510 HOH A O   1 
HETATM 4510 O  O   . HOH I 6 .   ? 37.41900  -15.74500 -7.37000 1.000 39.73417 ? 511 HOH A O   1 
HETATM 4511 O  O   . HOH I 6 .   ? 43.11500  8.87400   7.90600  1.000 26.66325 ? 512 HOH A O   1 
HETATM 4512 O  O   . HOH I 6 .   ? 14.11400  -2.54200  12.82900 1.000 26.24757 ? 513 HOH A O   1 
HETATM 4513 O  O   . HOH I 6 .   ? 7.11200   10.62200  8.32000  1.000 31.73249 ? 514 HOH A O   1 
HETATM 4514 O  O   . HOH I 6 .   ? 25.86900  -24.36400 5.90900  1.000 30.32686 ? 515 HOH A O   1 
HETATM 4515 O  O   . HOH I 6 .   ? 37.08400  -26.23700 10.57400 1.000 30.36040 ? 516 HOH A O   1 
HETATM 4516 O  O   . HOH I 6 .   ? 26.42800  -30.99800 27.52800 1.000 34.77552 ? 517 HOH A O   1 
HETATM 4517 O  O   . HOH I 6 .   ? 49.02300  -2.17700  3.18700  1.000 34.97324 ? 518 HOH A O   1 
HETATM 4518 O  O   . HOH I 6 .   ? 27.98200  -1.35400  19.78300 1.000 23.12827 ? 519 HOH A O   1 
HETATM 4519 O  O   . HOH I 6 .   ? 18.88000  3.38300   9.80800  1.000 22.35628 ? 520 HOH A O   1 
HETATM 4520 O  O   . HOH I 6 .   ? 35.55200  0.75000   23.58700 1.000 24.68970 ? 521 HOH A O   1 
HETATM 4521 O  O   . HOH I 6 .   ? 25.98100  -9.68200  24.52500 1.000 33.13305 ? 522 HOH A O   1 
HETATM 4522 O  O   . HOH I 6 .   ? 38.30800  -21.47500 5.84400  1.000 33.95335 ? 523 HOH A O   1 
HETATM 4523 O  O   . HOH I 6 .   ? 31.62900  -10.05800 -3.31300 1.000 32.43290 ? 524 HOH A O   1 
HETATM 4524 O  O   . HOH I 6 .   ? 44.70100  -4.36500  27.85100 1.000 34.62664 ? 525 HOH A O   1 
HETATM 4525 O  O   . HOH I 6 .   ? 26.52900  15.72500  22.06800 1.000 21.63204 ? 526 HOH A O   1 
HETATM 4526 O  O   . HOH I 6 .   ? 41.28500  -10.78800 8.39500  1.000 29.33236 ? 527 HOH A O   1 
HETATM 4527 O  O   . HOH I 6 .   ? 37.07000  -12.63000 1.01900  1.000 36.92693 ? 528 HOH A O   1 
HETATM 4528 O  O   . HOH I 6 .   ? 46.66700  -3.52200  27.22500 1.000 40.31751 ? 529 HOH A O   1 
HETATM 4529 O  O   . HOH I 6 .   ? 33.60500  -8.54700  24.20700 1.000 29.90467 ? 530 HOH A O   1 
HETATM 4530 O  O   . HOH I 6 .   ? 42.52800  -21.27200 36.08900 1.000 34.10716 ? 531 HOH A O   1 
HETATM 4531 O  O   . HOH I 6 .   ? 22.42200  9.43400   3.95800  1.000 23.24441 ? 532 HOH A O   1 
HETATM 4532 O  O   . HOH I 6 .   ? 36.60500  3.09000   23.62700 1.000 22.17298 ? 533 HOH A O   1 
HETATM 4533 O  O   . HOH I 6 .   ? 42.70300  -2.04900  27.11200 1.000 28.14012 ? 534 HOH A O   1 
HETATM 4534 O  O   . HOH I 6 .   ? 13.14500  4.92400   3.34500  1.000 33.40310 ? 535 HOH A O   1 
HETATM 4535 O  O   . HOH I 6 .   ? 33.40600  -0.07100  34.05800 1.000 29.19299 ? 536 HOH A O   1 
HETATM 4536 O  O   . HOH I 6 .   ? 29.02000  -20.88000 27.29600 1.000 36.89337 ? 537 HOH A O   1 
HETATM 4537 O  O   . HOH I 6 .   ? 42.47700  19.26500  6.38400  1.000 31.72697 ? 538 HOH A O   1 
HETATM 4538 O  O   . HOH I 6 .   ? 33.61200  -27.08300 12.68900 1.000 32.09397 ? 539 HOH A O   1 
HETATM 4539 O  O   . HOH I 6 .   ? 25.40000  4.13000   5.97400  1.000 21.13743 ? 540 HOH A O   1 
HETATM 4540 O  O   . HOH I 6 .   ? 44.82100  -13.20400 32.92800 1.000 31.56628 ? 541 HOH A O   1 
HETATM 4541 O  O   . HOH I 6 .   ? 16.22900  -21.23200 22.96100 1.000 34.62602 ? 542 HOH A O   1 
HETATM 4542 O  O   . HOH I 6 .   ? 26.13300  -33.03900 7.80400  1.000 36.49126 ? 543 HOH A O   1 
HETATM 4543 O  O   . HOH I 6 .   ? 28.03200  10.11000  10.47000 1.000 18.35124 ? 544 HOH A O   1 
HETATM 4544 O  O   . HOH I 6 .   ? 15.69500  -5.50300  14.33700 1.000 25.79308 ? 545 HOH A O   1 
HETATM 4545 O  O   . HOH I 6 .   ? 41.64700  7.79000   3.86900  1.000 26.02765 ? 546 HOH A O   1 
HETATM 4546 O  O   . HOH I 6 .   ? 20.77200  -25.20400 4.31300  1.000 49.89741 ? 547 HOH A O   1 
HETATM 4547 O  O   . HOH I 6 .   ? 36.33300  7.56200   36.86700 1.000 33.45575 ? 548 HOH A O   1 
HETATM 4548 O  O   . HOH I 6 .   ? 30.73800  16.58300  22.18800 1.000 23.19165 ? 549 HOH A O   1 
HETATM 4549 O  O   . HOH I 6 .   ? 35.91800  20.26900  13.50700 1.000 30.56640 ? 550 HOH A O   1 
HETATM 4550 O  O   . HOH I 6 .   ? 36.79300  19.50200  -3.32600 1.000 39.13604 ? 551 HOH A O   1 
HETATM 4551 O  O   . HOH I 6 .   ? 18.47500  -23.96000 15.54300 1.000 39.12785 ? 552 HOH A O   1 
HETATM 4552 O  O   . HOH I 6 .   ? 47.37600  -3.54500  -0.87300 1.000 38.57157 ? 553 HOH A O   1 
HETATM 4553 O  O   . HOH I 6 .   ? 37.99500  -27.85100 22.99600 1.000 40.12231 ? 554 HOH A O   1 
HETATM 4554 O  O   . HOH I 6 .   ? 17.52500  -3.20900  8.02700  1.000 26.10414 ? 555 HOH A O   1 
HETATM 4555 O  O   . HOH I 6 .   ? 25.31300  10.25500  4.80400  1.000 21.16209 ? 556 HOH A O   1 
HETATM 4556 O  O   . HOH I 6 .   ? 27.25100  -9.21500  -5.83000 1.000 32.24813 ? 557 HOH A O   1 
HETATM 4557 O  O   . HOH I 6 .   ? 26.47200  -5.39600  19.04600 1.000 27.63295 ? 558 HOH A O   1 
HETATM 4558 O  O   . HOH I 6 .   ? 23.63100  -29.91200 29.04300 1.000 34.74881 ? 559 HOH A O   1 
HETATM 4559 O  O   . HOH I 6 .   ? 39.42000  -1.36800  1.29200  1.000 27.68354 ? 560 HOH A O   1 
HETATM 4560 O  O   . HOH I 6 .   ? 24.859    -32.876   28.140   1.000 30.61461 ? 561 HOH A O   1 
HETATM 4561 O  O   . HOH I 6 .   ? 31.96600  11.32300  15.56000 1.000 18.47918 ? 562 HOH A O   1 
HETATM 4562 O  O   . HOH I 6 .   ? 25.97200  -21.33000 -0.81200 1.000 34.54424 ? 563 HOH A O   1 
HETATM 4563 O  O   . HOH I 6 .   ? 39.88300  -24.19400 21.38100 1.000 35.65773 ? 564 HOH A O   1 
HETATM 4564 O  O   . HOH I 6 .   ? 42.78700  -22.36500 9.97400  1.000 37.13592 ? 565 HOH A O   1 
HETATM 4565 O  O   . HOH I 6 .   ? 25.50400  -24.78300 14.12700 1.000 29.77412 ? 566 HOH A O   1 
HETATM 4566 O  O   . HOH I 6 .   ? 14.19200  -9.47500  9.45000  1.000 32.12110 ? 567 HOH A O   1 
HETATM 4567 O  O   . HOH I 6 .   ? 57.07100  -14.53500 21.20600 1.000 40.05274 ? 568 HOH A O   1 
HETATM 4568 O  O   . HOH I 6 .   ? 40.71800  -19.70600 33.81500 1.000 36.41615 ? 569 HOH A O   1 
HETATM 4569 O  O   . HOH I 6 .   ? 48.32400  -11.42400 24.99900 1.000 34.71924 ? 570 HOH A O   1 
HETATM 4570 O  O   . HOH I 6 .   ? 44.99700  1.87400   22.63800 1.000 27.41824 ? 571 HOH A O   1 
HETATM 4571 O  O   . HOH I 6 .   ? 14.87600  -12.06000 20.68600 1.000 30.96691 ? 572 HOH A O   1 
HETATM 4572 O  O   . HOH I 6 .   ? 13.03000  -21.10300 19.96900 1.000 36.89365 ? 573 HOH A O   1 
HETATM 4573 O  O   . HOH I 6 .   ? 49.05800  2.75500   15.94800 1.000 29.02675 ? 574 HOH A O   1 
HETATM 4574 O  O   . HOH I 6 .   ? 39.33000  22.54900  7.02700  1.000 30.88180 ? 575 HOH A O   1 
HETATM 4575 O  O   . HOH I 6 .   ? 20.43300  -27.67600 28.81700 1.000 34.93225 ? 576 HOH A O   1 
HETATM 4576 O  O   . HOH I 6 .   ? 9.59200   -9.15800  20.83900 1.000 30.52831 ? 577 HOH A O   1 
HETATM 4577 O  O   . HOH I 6 .   ? 16.41900  -9.63200  13.65000 1.000 28.06755 ? 578 HOH A O   1 
HETATM 4578 O  O   . HOH I 6 .   ? 26.77000  3.66100   2.81000  1.000 26.17458 ? 579 HOH A O   1 
HETATM 4579 O  O   . HOH I 6 .   ? 24.58300  -32.85800 19.39900 1.000 31.06511 ? 580 HOH A O   1 
HETATM 4580 O  O   . HOH I 6 .   ? 33.18700  17.37800  2.09500  1.000 27.90709 ? 581 HOH A O   1 
HETATM 4581 O  O   . HOH I 6 .   ? 37.991    -6.461    36.499   1.000 28.10072 ? 582 HOH A O   1 
HETATM 4582 O  O   . HOH I 6 .   ? 37.14100  1.91500   15.87100 1.000 21.89844 ? 583 HOH A O   1 
HETATM 4583 O  O   . HOH I 6 .   ? 22.16600  -9.56300  18.17700 1.000 30.25473 ? 584 HOH A O   1 
HETATM 4584 O  O   . HOH I 6 .   ? 18.72400  -22.32700 23.81700 1.000 36.34368 ? 585 HOH A O   1 
HETATM 4585 O  O   . HOH I 6 .   ? 41.71100  -26.15400 13.06800 1.000 32.01155 ? 586 HOH A O   1 
HETATM 4586 O  O   . HOH I 6 .   ? 26.86900  -20.60300 6.59700  1.000 29.50605 ? 587 HOH A O   1 
HETATM 4587 O  O   . HOH I 6 .   ? 34.43000  2.48400   -0.13700 1.000 33.98236 ? 588 HOH A O   1 
HETATM 4588 O  O   . HOH I 6 .   ? 38.21600  -14.86900 -3.19900 1.000 37.07917 ? 589 HOH A O   1 
HETATM 4589 O  O   . HOH I 6 .   ? 25.33000  -10.12900 15.55700 1.000 22.48271 ? 590 HOH A O   1 
HETATM 4590 O  O   . HOH I 6 .   ? 30.16400  6.19600   14.51500 1.000 18.21835 ? 591 HOH A O   1 
HETATM 4591 O  O   . HOH I 6 .   ? 25.27900  2.03600   17.01800 1.000 18.59111 ? 592 HOH A O   1 
HETATM 4592 O  O   . HOH I 6 .   ? 14.50700  0.03900   11.10900 1.000 25.49820 ? 593 HOH A O   1 
HETATM 4593 O  O   . HOH I 6 .   ? 26.37400  -35.23100 8.74000  1.000 36.36233 ? 594 HOH A O   1 
HETATM 4594 O  O   . HOH I 6 .   ? 14.39300  -14.18200 17.04100 1.000 28.50823 ? 595 HOH A O   1 
HETATM 4595 O  O   . HOH I 6 .   ? 35.79900  19.80400  -0.85200 1.000 33.15282 ? 596 HOH A O   1 
HETATM 4596 O  O   . HOH I 6 .   ? 26.93300  -5.98400  16.57800 1.000 24.08455 ? 597 HOH A O   1 
HETATM 4597 O  O   . HOH I 6 .   ? 25.81600  -2.99000  19.13800 1.000 23.47876 ? 598 HOH A O   1 
HETATM 4598 O  O   . HOH I 6 .   ? 30.79300  7.53400   17.05700 1.000 19.48285 ? 599 HOH A O   1 
HETATM 4599 O  O   . HOH I 6 .   ? 40.27800  -3.10000  2.63800  1.000 26.96315 ? 600 HOH A O   1 
HETATM 4600 O  O   . HOH I 6 .   ? 42.95600  -5.84700  28.61200 1.000 31.91319 ? 601 HOH A O   1 
HETATM 4601 O  O   . HOH I 6 .   ? 48.76600  4.64700   29.02800 1.000 51.05968 ? 602 HOH A O   1 
HETATM 4602 O  O   . HOH I 6 .   ? 19.55700  -8.55300  25.46900 1.000 35.43635 ? 603 HOH A O   1 
HETATM 4603 O  O   . HOH I 6 .   ? 40.55900  6.50600   36.80500 1.000 38.07413 ? 604 HOH A O   1 
HETATM 4604 O  O   . HOH I 6 .   ? 16.88600  -5.26300  5.24000  1.000 31.43865 ? 605 HOH A O   1 
HETATM 4605 O  O   . HOH I 6 .   ? 25.38400  -26.30800 12.24900 1.000 32.43944 ? 606 HOH A O   1 
HETATM 4606 O  O   . HOH I 6 .   ? 34.21400  7.59400   0.27800  1.000 27.35271 ? 607 HOH A O   1 
HETATM 4607 O  O   . HOH I 6 .   ? 28.55100  18.69900  2.15000  1.000 31.43746 ? 608 HOH A O   1 
HETATM 4608 O  O   . HOH I 6 .   ? 29.67400  -2.51700  21.60600 1.000 21.26391 ? 609 HOH A O   1 
HETATM 4609 O  O   . HOH I 6 .   ? 25.35800  27.05600  11.92500 1.000 31.52404 ? 610 HOH A O   1 
HETATM 4610 O  O   . HOH I 6 .   ? 41.93800  -22.99400 27.07000 1.000 41.01382 ? 611 HOH A O   1 
HETATM 4611 O  O   . HOH I 6 .   ? 24.66300  -11.56300 17.56500 1.000 27.59875 ? 612 HOH A O   1 
HETATM 4612 O  O   . HOH I 6 .   ? 30.47500  -25.29200 3.51400  1.000 32.28490 ? 613 HOH A O   1 
HETATM 4613 O  O   . HOH I 6 .   ? 18.34400  5.96500   3.72200  1.000 29.66104 ? 614 HOH A O   1 
HETATM 4614 O  O   . HOH I 6 .   ? 37.35300  16.93200  17.79300 1.000 24.68671 ? 615 HOH A O   1 
HETATM 4615 O  O   . HOH I 6 .   ? 17.30700  -7.26300  26.32700 1.000 31.83962 ? 616 HOH A O   1 
HETATM 4616 O  O   . HOH I 6 .   ? 32.23200  -23.84700 2.66900  1.000 29.65199 ? 617 HOH A O   1 
HETATM 4617 O  O   . HOH I 6 .   ? 24.12900  14.45100  5.07700  1.000 23.31146 ? 618 HOH A O   1 
HETATM 4618 O  O   . HOH I 6 .   ? 38.53900  6.88100   5.45400  1.000 26.45716 ? 619 HOH A O   1 
HETATM 4619 O  O   . HOH I 6 .   ? 49.99300  -16.90000 22.83500 1.000 38.40070 ? 620 HOH A O   1 
HETATM 4620 O  O   . HOH I 6 .   ? 50.43800  -11.10300 19.32300 1.000 32.79556 ? 621 HOH A O   1 
HETATM 4621 O  O   . HOH I 6 .   ? 31.06700  -0.39100  -1.45400 1.000 28.00062 ? 622 HOH A O   1 
HETATM 4622 O  O   . HOH I 6 .   ? 42.41600  15.64600  3.06300  1.000 29.88109 ? 623 HOH A O   1 
HETATM 4623 O  O   . HOH I 6 .   ? 41.08700  6.40900   32.68700 1.000 31.67474 ? 624 HOH A O   1 
HETATM 4624 O  O   . HOH I 6 .   ? 37.02800  -23.58300 27.90600 1.000 40.48511 ? 625 HOH A O   1 
HETATM 4625 O  O   . HOH I 6 .   ? 11.45800  -0.21800  5.35100  1.000 30.37678 ? 626 HOH A O   1 
HETATM 4626 O  O   . HOH I 6 .   ? 47.32900  5.83800   22.03900 1.000 32.05988 ? 627 HOH A O   1 
HETATM 4627 O  O   . HOH I 6 .   ? 54.19400  -12.48600 9.16500  1.000 39.19342 ? 628 HOH A O   1 
HETATM 4628 O  O   . HOH I 6 .   ? 18.59000  -8.12200  5.76900  1.000 31.73402 ? 629 HOH A O   1 
HETATM 4629 O  O   . HOH I 6 .   ? 18.53100  -10.08200 6.98300  1.000 33.35204 ? 630 HOH A O   1 
HETATM 4630 O  O   . HOH I 6 .   ? 38.16600  -24.03500 23.24100 1.000 37.49026 ? 631 HOH A O   1 
HETATM 4631 O  O   . HOH I 6 .   ? 51.41600  -11.33300 28.43000 1.000 44.11856 ? 632 HOH A O   1 
HETATM 4632 O  O   . HOH I 6 .   ? 34.30900  17.04700  20.54800 1.000 24.62468 ? 633 HOH A O   1 
HETATM 4633 O  O   . HOH I 6 .   ? 41.54200  3.54600   29.92300 1.000 31.82884 ? 634 HOH A O   1 
HETATM 4634 O  O   . HOH I 6 .   ? 25.04200  16.50700  1.47400  1.000 32.85179 ? 635 HOH A O   1 
HETATM 4635 O  O   . HOH I 6 .   ? 27.92000  13.04700  2.74900  1.000 23.23487 ? 636 HOH A O   1 
HETATM 4636 O  O   . HOH I 6 .   ? 20.75100  -11.98100 25.20400 1.000 37.83579 ? 637 HOH A O   1 
HETATM 4637 O  O   . HOH I 6 .   ? 5.13600   -13.59700 11.59200 1.000 46.03038 ? 638 HOH A O   1 
HETATM 4638 O  O   . HOH I 6 .   ? 35.18500  0.66500   35.36300 1.000 29.73983 ? 639 HOH A O   1 
HETATM 4639 O  O   . HOH I 6 .   ? 29.420    -29.547   24.965   1.000 35.97229 ? 640 HOH A O   1 
HETATM 4640 O  O   . HOH I 6 .   ? 29.76400  1.94200   -1.04800 1.000 31.48542 ? 641 HOH A O   1 
HETATM 4641 O  O   . HOH I 6 .   ? 35.92800  -24.17900 23.70600 1.000 39.46806 ? 642 HOH A O   1 
HETATM 4642 O  O   . HOH I 6 .   ? 40.95000  -22.73700 4.85800  1.000 43.09834 ? 643 HOH A O   1 
HETATM 4643 O  O   . HOH I 6 .   ? 29.88400  -33.44100 11.75100 1.000 42.67431 ? 644 HOH A O   1 
HETATM 4644 O  O   . HOH I 6 .   ? 32.15500  -29.11800 13.78800 1.000 40.19417 ? 645 HOH A O   1 
HETATM 4645 O  O   . HOH I 6 .   ? 32.17300  -18.99900 -3.69600 1.000 27.87887 ? 646 HOH A O   1 
HETATM 4646 O  O   . HOH I 6 .   ? 13.13000  0.43800   9.29700  1.000 28.22435 ? 647 HOH A O   1 
HETATM 4647 O  O   . HOH I 6 .   ? 43.05600  -17.13500 3.14500  1.000 39.12795 ? 648 HOH A O   1 
HETATM 4648 O  O   . HOH I 6 .   ? 20.09300  -10.95400 5.21800  1.000 33.66108 ? 649 HOH A O   1 
HETATM 4649 O  O   . HOH I 6 .   ? 41.61600  6.27000   1.94400  1.000 32.10509 ? 650 HOH A O   1 
HETATM 4650 O  O   . HOH I 6 .   ? 16.18000  15.71800  4.08200  1.000 34.83234 ? 651 HOH A O   1 
HETATM 4651 O  O   . HOH I 6 .   ? 27.17200  16.24700  2.10400  1.000 27.92897 ? 652 HOH A O   1 
HETATM 4652 O  O   . HOH I 6 .   ? 37.26200  23.75300  4.61300  1.000 36.02300 ? 653 HOH A O   1 
HETATM 4653 O  O   . HOH I 6 .   ? 29.13300  -0.64700  -2.62500 1.000 32.39753 ? 654 HOH A O   1 
HETATM 4654 O  O   . HOH I 6 .   ? 45.89300  11.09800  8.84300  1.000 32.99813 ? 655 HOH A O   1 
HETATM 4655 O  O   . HOH I 6 .   ? 23.02100  -12.00600 25.10000 1.000 35.88264 ? 656 HOH A O   1 
HETATM 4656 O  O   . HOH I 6 .   ? 27.57700  -32.55900 16.58100 1.000 42.12995 ? 657 HOH A O   1 
HETATM 4657 O  O   . HOH I 6 .   ? 43.69300  16.56400  6.11100  1.000 32.55578 ? 658 HOH A O   1 
HETATM 4658 O  O   . HOH I 6 .   ? 53.93300  7.96100   37.04700 1.000 51.34591 ? 659 HOH A O   1 
HETATM 4659 O  O   . HOH I 6 .   ? 49.28900  -12.60000 10.35500 1.000 30.44256 ? 660 HOH A O   1 
HETATM 4660 O  O   . HOH I 6 .   ? 28.89000  -7.75000  22.31000 1.000 30.83267 ? 661 HOH A O   1 
HETATM 4661 O  O   . HOH I 6 .   ? 27.67900  -8.68900  28.54300 1.000 28.44928 ? 662 HOH A O   1 
HETATM 4662 O  O   . HOH I 6 .   ? 23.25600  16.38400  0.11300  1.000 31.47502 ? 663 HOH A O   1 
HETATM 4663 O  O   . HOH I 6 .   ? 19.79500  27.86700  14.91100 1.000 31.58118 ? 664 HOH A O   1 
HETATM 4664 O  O   . HOH I 6 .   ? 44.73000  -13.14200 28.02700 1.000 39.54398 ? 665 HOH A O   1 
HETATM 4665 O  O   . HOH I 6 .   ? 47.44400  8.40600   12.46500 1.000 32.57188 ? 666 HOH A O   1 
HETATM 4666 O  O   . HOH I 6 .   ? 29.62000  7.36400   1.31000  1.000 23.56973 ? 667 HOH A O   1 
HETATM 4667 O  O   . HOH I 6 .   ? 55.53900  -3.25300  27.09900 1.000 39.07249 ? 668 HOH A O   1 
HETATM 4668 O  O   . HOH I 6 .   ? 14.21100  -12.77000 8.61400  1.000 35.16861 ? 669 HOH A O   1 
HETATM 4669 O  O   . HOH I 6 .   ? 43.61000  -26.92400 14.40900 1.000 36.37661 ? 670 HOH A O   1 
HETATM 4670 O  O   . HOH I 6 .   ? 49.62400  -12.03200 17.47100 1.000 31.99646 ? 671 HOH A O   1 
HETATM 4671 O  O   . HOH I 6 .   ? 18.39000  -9.08100  3.56600  1.000 36.12268 ? 672 HOH A O   1 
HETATM 4672 O  O   . HOH I 6 .   ? 46.97800  -1.71700  25.58500 1.000 37.60752 ? 673 HOH A O   1 
HETATM 4673 O  O   . HOH I 6 .   ? 17.56400  -24.10500 25.90800 1.000 37.85751 ? 674 HOH A O   1 
HETATM 4674 O  O   . HOH I 6 .   ? 28.35500  -3.94400  26.32700 1.000 26.28049 ? 675 HOH A O   1 
HETATM 4675 O  O   . HOH I 6 .   ? 23.68700  -8.31000  17.03200 1.000 27.56771 ? 676 HOH A O   1 
HETATM 4676 O  O   . HOH I 6 .   ? 52.05700  0.53900   9.40200  1.000 31.76753 ? 677 HOH A O   1 
HETATM 4677 O  O   . HOH I 6 .   ? 38.838    -15.520   37.123   1.000 28.49793 ? 678 HOH A O   1 
HETATM 4678 O  O   . HOH I 6 .   ? 15.95700  7.79500   1.40600  1.000 34.21144 ? 679 HOH A O   1 
HETATM 4679 O  O   . HOH I 6 .   ? 21.670    -26.483   17.104   1.000 35.47676 ? 680 HOH A O   1 
HETATM 4680 O  O   . HOH I 6 .   ? 31.99000  7.77300   -0.50700 1.000 28.72358 ? 681 HOH A O   1 
HETATM 4681 O  O   . HOH I 6 .   ? 39.83000  -23.85700 7.14700  1.000 35.56088 ? 682 HOH A O   1 
HETATM 4682 O  O   . HOH I 6 .   ? 37.63200  -27.90500 25.27900 1.000 38.04957 ? 683 HOH A O   1 
HETATM 4683 O  O   . HOH I 6 .   ? 39.13000  25.64400  3.64900  1.000 42.04568 ? 684 HOH A O   1 
HETATM 4684 O  O   . HOH I 6 .   ? 30.21000  -4.20400  25.03400 1.000 27.20019 ? 685 HOH A O   1 
HETATM 4685 O  O   . HOH I 6 .   ? 33.39100  17.91100  17.70300 1.000 27.07663 ? 686 HOH A O   1 
HETATM 4686 O  O   . HOH I 6 .   ? 15.31900  5.82500   2.59400  1.000 33.08197 ? 687 HOH A O   1 
HETATM 4687 O  O   . HOH I 6 .   ? 22.83200  2.48700   3.39800  1.000 26.41359 ? 688 HOH A O   1 
HETATM 4688 O  O   . HOH I 6 .   ? 38.53100  -13.27100 -5.11900 1.000 39.69756 ? 689 HOH A O   1 
HETATM 4689 O  O   . HOH I 6 .   ? 17.69800  14.78200  2.37800  1.000 35.92234 ? 690 HOH A O   1 
HETATM 4690 O  O   . HOH I 6 .   ? 49.71400  18.25200  11.34700 1.000 41.69353 ? 691 HOH A O   1 
HETATM 4691 O  O   . HOH I 6 .   ? 18.24000  12.81200  3.65300  1.000 32.44971 ? 692 HOH A O   1 
HETATM 4692 O  O   . HOH I 6 .   ? 42.34300  -24.83800 10.78500 1.000 34.01951 ? 693 HOH A O   1 
HETATM 4693 O  O   . HOH I 6 .   ? 21.94100  29.42100  15.69200 1.000 31.14592 ? 694 HOH A O   1 
HETATM 4694 O  O   . HOH I 6 .   ? 38.64800  -24.05300 5.17300  1.000 36.16850 ? 695 HOH A O   1 
HETATM 4695 O  O   . HOH I 6 .   ? 11.73000  -12.99500 18.48500 1.000 34.49532 ? 696 HOH A O   1 
HETATM 4696 O  O   . HOH I 6 .   ? 37.378    -15.351   -11.442  1.000 46.35747 ? 697 HOH A O   1 
HETATM 4697 O  O   . HOH I 6 .   ? 36.37600  -25.78800 5.12800  1.000 34.28259 ? 698 HOH A O   1 
HETATM 4698 O  O   . HOH I 6 .   ? 17.00800  -11.94000 28.42500 1.000 33.61325 ? 699 HOH A O   1 
HETATM 4699 O  O   . HOH I 6 .   ? 16.75300  -7.38600  3.66600  1.000 36.27958 ? 700 HOH A O   1 
HETATM 4700 O  O   . HOH I 6 .   ? 36.968    -16.686   36.516   1.000 30.43545 ? 701 HOH A O   1 
HETATM 4701 O  O   . HOH I 6 .   ? 28.32300  5.24900   -1.42300 1.000 33.02968 ? 702 HOH A O   1 
HETATM 4702 O  O   . HOH I 6 .   ? 35.03700  -24.69100 26.03300 1.000 38.43642 ? 703 HOH A O   1 
HETATM 4703 O  O   . HOH I 6 .   ? 31.385    -28.624   26.007   1.000 37.39775 ? 704 HOH A O   1 
HETATM 4704 O  O   . HOH I 6 .   ? 42.37400  -9.55300  -3.52500 1.000 43.47892 ? 705 HOH A O   1 
HETATM 4705 O  O   . HOH I 6 .   ? 31.33700  10.41400  -2.08300 1.000 29.63973 ? 706 HOH A O   1 
HETATM 4706 O  O   . HOH I 6 .   ? 16.25200  -15.00500 27.27700 1.000 38.46090 ? 707 HOH A O   1 
HETATM 4707 O  O   . HOH I 6 .   ? 41.085    -8.211    36.104   1.000 28.77542 ? 708 HOH A O   1 
HETATM 4708 O  O   . HOH I 6 .   ? 40.915    -5.493    37.285   1.000 27.71939 ? 709 HOH A O   1 
HETATM 4709 O  O   . HOH I 6 .   ? 36.04900  22.08700  15.89200 1.000 39.25545 ? 710 HOH A O   1 
HETATM 4710 O  O   . HOH I 6 .   ? 31.81500  -32.51900 12.46100 1.000 42.27587 ? 711 HOH A O   1 
HETATM 4711 O  O   . HOH I 6 .   ? 31.96600  -3.07700  22.49600 1.000 24.26953 ? 712 HOH A O   1 
HETATM 4712 O  O   . HOH I 6 .   ? 36.69200  19.12300  15.36100 1.000 31.57245 ? 713 HOH A O   1 
HETATM 4713 O  O   . HOH I 6 .   ? 32.47900  1.93400   -1.62200 1.000 31.45898 ? 714 HOH A O   1 
HETATM 4714 O  O   . HOH I 6 .   ? 25.13600  15.03300  -0.18300 1.000 35.08717 ? 715 HOH A O   1 
HETATM 4715 O  O   . HOH I 6 .   ? 18.08500  -9.96500  28.25800 1.000 35.09328 ? 716 HOH A O   1 
HETATM 4716 O  O   . HOH I 6 .   ? 28.68200  -6.39100  -4.94000 1.000 29.43633 ? 717 HOH A O   1 
HETATM 4717 O  O   . HOH I 6 .   ? 34.55000  19.56700  16.49100 1.000 28.77051 ? 718 HOH A O   1 
HETATM 4718 O  O   . HOH I 6 .   ? 36.268    27.501    11.765   1.000 46.83065 ? 719 HOH A O   1 
HETATM 4719 O  O   . HOH I 6 .   ? 45.915    -4.029    36.069   1.000 50.38763 ? 720 HOH A O   1 
HETATM 4720 O  O   . HOH I 6 .   ? 43.96300  9.14100   33.52500 1.000 33.75557 ? 721 HOH A O   1 
HETATM 4721 O  O   . HOH I 6 .   ? 41.02100  -10.14000 -5.32000 1.000 45.78903 ? 722 HOH A O   1 
HETATM 4722 O  O   . HOH I 6 .   ? 31.06300  5.29800   -1.47700 1.000 29.81562 ? 723 HOH A O   1 
HETATM 4723 O  O   . HOH I 6 .   ? 35.09700  22.55400  -0.07800 1.000 33.46976 ? 724 HOH A O   1 
HETATM 4724 O  O   . HOH I 6 .   ? 36.67500  -34.45100 14.10700 1.000 47.61545 ? 725 HOH A O   1 
HETATM 4725 O  O   . HOH I 6 .   ? 29.33000  5.95100   -3.40900 1.000 29.37201 ? 726 HOH A O   1 
HETATM 4726 O  O   . HOH I 6 .   ? 44.82800  16.61100  22.23800 1.000 45.67173 ? 727 HOH A O   1 
HETATM 4727 O  O   . HOH I 6 .   ? 34.81900  24.12900  -1.93700 1.000 37.63333 ? 728 HOH A O   1 
HETATM 4728 O  O   . HOH I 6 .   ? 43.32600  18.93100  22.32500 1.000 44.39589 ? 729 HOH A O   1 
HETATM 4729 O  O   . HOH J 6 .   ? -10.86700 10.72500  25.43500 1.000 33.27505 ? 601 HOH B O   1 
HETATM 4730 O  O   . HOH J 6 .   ? 27.23100  12.87800  16.41800 1.000 18.91694 ? 602 HOH B O   1 
HETATM 4731 O  O   . HOH J 6 .   ? 7.89600   8.88200   21.58700 1.000 25.96579 ? 603 HOH B O   1 
HETATM 4732 O  O   . HOH J 6 .   ? 24.18500  26.90500  34.43700 1.000 28.36780 ? 604 HOH B O   1 
HETATM 4733 O  O   . HOH J 6 .   ? 37.73600  26.49200  25.84800 1.000 32.20330 ? 605 HOH B O   1 
HETATM 4734 O  O   . HOH J 6 .   ? 23.52700  18.48200  37.73600 1.000 23.54105 ? 606 HOH B O   1 
HETATM 4735 O  O   . HOH J 6 .   ? 16.97600  21.90700  21.45000 1.000 22.15326 ? 607 HOH B O   1 
HETATM 4736 O  O   . HOH J 6 .   ? -1.04400  -4.40500  12.83500 1.000 37.77944 ? 608 HOH B O   1 
HETATM 4737 O  O   . HOH J 6 .   ? 25.52600  14.63900  20.13400 1.000 22.57075 ? 609 HOH B O   1 
HETATM 4738 O  O   . HOH J 6 .   ? -12.29800 5.84200   13.11600 1.000 30.62572 ? 610 HOH B O   1 
HETATM 4739 O  O   . HOH J 6 .   ? -2.64500  14.06500  42.02500 1.000 34.73654 ? 611 HOH B O   1 
HETATM 4740 O  O   . HOH J 6 .   ? 20.58300  19.87300  1.60000  1.000 35.36550 ? 612 HOH B O   1 
HETATM 4741 O  O   . HOH J 6 .   ? -6.80700  21.35200  18.04700 1.000 30.22257 ? 613 HOH B O   1 
HETATM 4742 O  O   . HOH J 6 .   ? 2.61400   -6.72000  22.79400 1.000 37.89409 ? 614 HOH B O   1 
HETATM 4743 O  O   . HOH J 6 .   ? 5.06700   25.44600  29.79700 1.000 29.25740 ? 615 HOH B O   1 
HETATM 4744 O  O   . HOH J 6 .   ? 28.37700  17.14200  40.70200 1.000 31.40806 ? 616 HOH B O   1 
HETATM 4745 O  O   . HOH J 6 .   ? 4.97300   15.48000  19.29100 1.000 27.93691 ? 617 HOH B O   1 
HETATM 4746 O  O   . HOH J 6 .   ? 23.22000  12.53100  17.07700 1.000 19.62176 ? 618 HOH B O   1 
HETATM 4747 O  O   . HOH J 6 .   ? 29.17100  9.79900   32.78200 1.000 23.24041 ? 619 HOH B O   1 
HETATM 4748 O  O   . HOH J 6 .   ? 14.60100  36.72400  9.35000  1.000 54.22949 ? 620 HOH B O   1 
HETATM 4749 O  O   . HOH J 6 .   ? 5.74100   10.20000  22.22600 1.000 23.50687 ? 621 HOH B O   1 
HETATM 4750 O  O   . HOH J 6 .   ? -5.15300  22.28100  31.29600 1.000 30.20791 ? 622 HOH B O   1 
HETATM 4751 O  O   . HOH J 6 .   ? 16.55500  6.32300   33.63200 1.000 22.63956 ? 623 HOH B O   1 
HETATM 4752 O  O   . HOH J 6 .   ? 17.86400  19.63400  37.78700 1.000 24.00060 ? 624 HOH B O   1 
HETATM 4753 O  O   . HOH J 6 .   ? 14.37000  19.47900  15.63300 1.000 23.91254 ? 625 HOH B O   1 
HETATM 4754 O  O   . HOH J 6 .   ? -8.14800  20.71500  26.62400 1.000 35.27935 ? 626 HOH B O   1 
HETATM 4755 O  O   . HOH J 6 .   ? -13.70300 16.07700  24.41600 1.000 37.66187 ? 627 HOH B O   1 
HETATM 4756 O  O   . HOH J 6 .   ? 42.45700  4.89300   22.28800 1.000 26.02451 ? 628 HOH B O   1 
HETATM 4757 O  O   . HOH J 6 .   ? -17.13600 12.50400  28.90900 1.000 35.50693 ? 629 HOH B O   1 
HETATM 4758 O  O   . HOH J 6 .   ? 21.77400  14.72200  23.37900 1.000 20.32173 ? 630 HOH B O   1 
HETATM 4759 O  O   . HOH J 6 .   ? 12.61900  9.70300   17.76200 1.000 25.77053 ? 631 HOH B O   1 
HETATM 4760 O  O   . HOH J 6 .   ? 18.25700  28.32100  1.25500  1.000 55.49392 ? 632 HOH B O   1 
HETATM 4761 O  O   . HOH J 6 .   ? 44.60500  8.50600   28.86900 1.000 39.03298 ? 633 HOH B O   1 
HETATM 4762 O  O   . HOH J 6 .   ? 17.86200  33.28200  21.42100 1.000 26.09898 ? 634 HOH B O   1 
HETATM 4763 O  O   . HOH J 6 .   ? -9.62800  6.94700   23.75800 1.000 31.17641 ? 635 HOH B O   1 
HETATM 4764 O  O   . HOH J 6 .   ? -11.24700 8.01500   21.56400 1.000 29.58805 ? 636 HOH B O   1 
HETATM 4765 O  O   . HOH J 6 .   ? 8.86500   1.01200   9.15800  1.000 33.04694 ? 637 HOH B O   1 
HETATM 4766 O  O   . HOH J 6 .   ? 32.16400  21.86200  20.29600 1.000 22.81702 ? 638 HOH B O   1 
HETATM 4767 O  O   . HOH J 6 .   ? -4.36500  39.64100  21.41900 1.000 54.63288 ? 639 HOH B O   1 
HETATM 4768 O  O   . HOH J 6 .   ? 25.41300  21.93800  18.19900 1.000 23.15532 ? 640 HOH B O   1 
HETATM 4769 O  O   . HOH J 6 .   ? 7.33600   15.93700  15.50000 1.000 29.20370 ? 641 HOH B O   1 
HETATM 4770 O  O   . HOH J 6 .   ? 41.25200  -0.59000  28.25200 1.000 27.29014 ? 642 HOH B O   1 
HETATM 4771 O  O   . HOH J 6 .   ? -0.66300  22.81900  14.52700 1.000 32.59040 ? 643 HOH B O   1 
HETATM 4772 O  O   . HOH J 6 .   ? -6.87100  25.32600  14.66500 1.000 48.95180 ? 644 HOH B O   1 
HETATM 4773 O  O   . HOH J 6 .   ? 18.82700  27.88100  11.64300 1.000 42.50539 ? 645 HOH B O   1 
HETATM 4774 O  O   . HOH J 6 .   ? -4.67800  11.95500  31.57700 1.000 30.05473 ? 646 HOH B O   1 
HETATM 4775 O  O   . HOH J 6 .   ? 30.34200  1.44100   33.70900 1.000 32.08591 ? 647 HOH B O   1 
HETATM 4776 O  O   . HOH J 6 .   ? 7.35000   5.81800   40.12400 1.000 38.35671 ? 648 HOH B O   1 
HETATM 4777 O  O   . HOH J 6 .   ? 18.91000  6.96900   34.90100 1.000 26.54972 ? 649 HOH B O   1 
HETATM 4778 O  O   . HOH J 6 .   ? 6.35700   16.48400  41.14300 1.000 39.79271 ? 650 HOH B O   1 
HETATM 4779 O  O   . HOH J 6 .   ? -1.34900  7.76300   44.22100 1.000 37.64195 ? 651 HOH B O   1 
HETATM 4780 O  O   . HOH J 6 .   ? 40.91500  11.21500  30.37300 1.000 30.66885 ? 652 HOH B O   1 
HETATM 4781 O  O   . HOH J 6 .   ? 10.98500  1.76800   31.99600 1.000 28.93798 ? 653 HOH B O   1 
HETATM 4782 O  O   . HOH J 6 .   ? 23.68000  26.11800  17.56400 1.000 26.52367 ? 654 HOH B O   1 
HETATM 4783 O  O   . HOH J 6 .   ? -8.47300  23.74800  30.31100 1.000 31.58836 ? 655 HOH B O   1 
HETATM 4784 O  O   . HOH J 6 .   ? -1.27400  3.52200   9.82400  1.000 37.83373 ? 656 HOH B O   1 
HETATM 4785 O  O   . HOH J 6 .   ? 1.92300   21.98000  14.72300 1.000 32.40615 ? 657 HOH B O   1 
HETATM 4786 O  O   . HOH J 6 .   ? 26.65800  25.20400  15.95800 1.000 27.56874 ? 658 HOH B O   1 
HETATM 4787 O  O   . HOH J 6 .   ? 18.61700  27.32900  17.39500 1.000 27.25237 ? 659 HOH B O   1 
HETATM 4788 O  O   . HOH J 6 .   ? 17.51600  12.42000  36.34100 1.000 30.04114 ? 660 HOH B O   1 
HETATM 4789 O  O   . HOH J 6 .   ? 6.28200   35.44700  15.16200 1.000 36.60393 ? 661 HOH B O   1 
HETATM 4790 O  O   . HOH J 6 .   ? 18.38600  -2.59200  29.28800 1.000 30.29244 ? 662 HOH B O   1 
HETATM 4791 O  O   . HOH J 6 .   ? 25.31900  27.23800  29.13200 1.000 27.20710 ? 663 HOH B O   1 
HETATM 4792 O  O   . HOH J 6 .   ? 18.73500  3.36400   27.79000 1.000 22.48208 ? 664 HOH B O   1 
HETATM 4793 O  O   . HOH J 6 .   ? 20.80100  -1.26500  35.54300 1.000 32.85363 ? 665 HOH B O   1 
HETATM 4794 O  O   . HOH J 6 .   ? -8.86200  10.15500  31.10900 1.000 33.30310 ? 666 HOH B O   1 
HETATM 4795 O  O   . HOH J 6 .   ? 7.69400   2.77800   31.71500 1.000 30.57627 ? 667 HOH B O   1 
HETATM 4796 O  O   . HOH J 6 .   ? 14.20600  14.82800  39.96900 1.000 24.27691 ? 668 HOH B O   1 
HETATM 4797 O  O   . HOH J 6 .   ? 15.86700  30.86700  34.34400 1.000 24.85308 ? 669 HOH B O   1 
HETATM 4798 O  O   . HOH J 6 .   ? 34.85800  15.79600  34.36200 1.000 26.84019 ? 670 HOH B O   1 
HETATM 4799 O  O   . HOH J 6 .   ? 25.59100  12.65500  27.51000 1.000 18.48646 ? 671 HOH B O   1 
HETATM 4800 O  O   . HOH J 6 .   ? 7.20300   22.28300  10.97500 1.000 37.75075 ? 672 HOH B O   1 
HETATM 4801 O  O   . HOH J 6 .   ? 27.62500  -2.83900  34.84700 1.000 32.22588 ? 673 HOH B O   1 
HETATM 4802 O  O   . HOH J 6 .   ? 16.10700  20.25700  12.33100 1.000 27.09079 ? 674 HOH B O   1 
HETATM 4803 O  O   . HOH J 6 .   ? 17.55200  9.71800   20.66300 1.000 20.36796 ? 675 HOH B O   1 
HETATM 4804 O  O   . HOH J 6 .   ? 19.78900  9.39700   31.89600 1.000 22.08407 ? 676 HOH B O   1 
HETATM 4805 O  O   . HOH J 6 .   ? 34.83500  26.74300  29.46700 1.000 30.16782 ? 677 HOH B O   1 
HETATM 4806 O  O   . HOH J 6 .   ? -3.85600  32.01500  21.03100 1.000 34.15737 ? 678 HOH B O   1 
HETATM 4807 O  O   . HOH J 6 .   ? -15.54000 14.72500  25.22000 1.000 39.75546 ? 679 HOH B O   1 
HETATM 4808 O  O   . HOH J 6 .   ? -7.58900  14.57400  10.44300 1.000 35.67409 ? 680 HOH B O   1 
HETATM 4809 O  O   . HOH J 6 .   ? 10.24000  -0.09100  22.97800 1.000 25.97275 ? 681 HOH B O   1 
HETATM 4810 O  O   . HOH J 6 .   ? 12.65900  24.48800  35.17600 1.000 30.35637 ? 682 HOH B O   1 
HETATM 4811 O  O   . HOH J 6 .   ? -8.68800  16.75300  27.73900 1.000 32.77427 ? 683 HOH B O   1 
HETATM 4812 O  O   . HOH J 6 .   ? 3.61600   9.74700   20.27700 1.000 26.40513 ? 684 HOH B O   1 
HETATM 4813 O  O   . HOH J 6 .   ? 22.10600  23.48100  32.57900 1.000 24.86108 ? 685 HOH B O   1 
HETATM 4814 O  O   . HOH J 6 .   ? -9.37600  12.93000  33.43900 1.000 33.03967 ? 686 HOH B O   1 
HETATM 4815 O  O   . HOH J 6 .   ? 18.88600  20.75000  14.10700 1.000 23.64380 ? 687 HOH B O   1 
HETATM 4816 O  O   . HOH J 6 .   ? -8.90200  12.68400  10.48600 1.000 34.76660 ? 688 HOH B O   1 
HETATM 4817 O  O   . HOH J 6 .   ? -7.37900  2.20700   24.20700 1.000 37.69790 ? 689 HOH B O   1 
HETATM 4818 O  O   . HOH J 6 .   ? 9.55100   11.70100  21.80900 1.000 23.96410 ? 690 HOH B O   1 
HETATM 4819 O  O   . HOH J 6 .   ? 9.58000   10.61000  15.61700 1.000 31.55471 ? 691 HOH B O   1 
HETATM 4820 O  O   . HOH J 6 .   ? 15.72100  5.36400   35.67400 1.000 26.76068 ? 692 HOH B O   1 
HETATM 4821 O  O   . HOH J 6 .   ? 9.65100   23.12500  38.80200 1.000 32.42772 ? 693 HOH B O   1 
HETATM 4822 O  O   . HOH J 6 .   ? 24.07700  20.60000  1.40900  1.000 34.55382 ? 694 HOH B O   1 
HETATM 4823 O  O   . HOH J 6 .   ? 22.90800  15.48500  21.16300 1.000 21.61267 ? 695 HOH B O   1 
HETATM 4824 O  O   . HOH J 6 .   ? -0.05100  23.54500  11.92000 1.000 34.39738 ? 696 HOH B O   1 
HETATM 4825 O  O   . HOH J 6 .   ? 11.75400  9.34300   39.82900 1.000 26.76670 ? 697 HOH B O   1 
HETATM 4826 O  O   . HOH J 6 .   ? 13.04600  -1.70900  24.61500 1.000 26.76456 ? 698 HOH B O   1 
HETATM 4827 O  O   . HOH J 6 .   ? 21.07100  3.04200   33.81800 1.000 28.86367 ? 699 HOH B O   1 
HETATM 4828 O  O   . HOH J 6 .   ? 25.52400  -2.58600  35.86400 1.000 39.36062 ? 700 HOH B O   1 
HETATM 4829 O  O   . HOH J 6 .   ? 6.27000   36.57100  20.57400 1.000 35.15070 ? 701 HOH B O   1 
HETATM 4830 O  O   . HOH J 6 .   ? 21.01300  20.04800  37.27900 1.000 19.71459 ? 702 HOH B O   1 
HETATM 4831 O  O   . HOH J 6 .   ? 28.04900  8.19800   20.68100 1.000 18.89142 ? 703 HOH B O   1 
HETATM 4832 O  O   . HOH J 6 .   ? 10.80500  12.50500  16.84400 1.000 29.26072 ? 704 HOH B O   1 
HETATM 4833 O  O   . HOH J 6 .   ? -4.63200  8.28300   40.85400 1.000 39.69436 ? 705 HOH B O   1 
HETATM 4834 O  O   . HOH J 6 .   ? 21.49400  32.95100  17.93100 1.000 30.65219 ? 706 HOH B O   1 
HETATM 4835 O  O   . HOH J 6 .   ? -19.28900 13.10700  26.65000 1.000 31.74746 ? 707 HOH B O   1 
HETATM 4836 O  O   . HOH J 6 .   ? 6.04700   6.46700   19.35100 1.000 26.74717 ? 708 HOH B O   1 
HETATM 4837 O  O   . HOH J 6 .   ? 19.68600  10.31100  34.08300 1.000 27.16241 ? 709 HOH B O   1 
HETATM 4838 O  O   . HOH J 6 .   ? -9.60900  16.15500  33.44100 1.000 31.78753 ? 710 HOH B O   1 
HETATM 4839 O  O   . HOH J 6 .   ? -7.40900  22.10400  9.42300  1.000 34.81616 ? 711 HOH B O   1 
HETATM 4840 O  O   . HOH J 6 .   ? -13.42100 26.96800  18.33100 1.000 47.59740 ? 712 HOH B O   1 
HETATM 4841 O  O   . HOH J 6 .   ? 4.52300   21.37700  13.73200 1.000 32.56782 ? 713 HOH B O   1 
HETATM 4842 O  O   . HOH J 6 .   ? 8.32700   -3.92600  7.51700  1.000 31.62174 ? 714 HOH B O   1 
HETATM 4843 O  O   . HOH J 6 .   ? 5.24100   34.92900  27.88100 1.000 32.77642 ? 715 HOH B O   1 
HETATM 4844 O  O   . HOH J 6 .   ? -0.88900  13.08400  43.58600 1.000 34.68523 ? 716 HOH B O   1 
HETATM 4845 O  O   . HOH J 6 .   ? 16.11300  -2.56800  28.47500 1.000 28.58834 ? 717 HOH B O   1 
HETATM 4846 O  O   . HOH J 6 .   ? 42.33700  13.19300  30.14100 1.000 32.81552 ? 718 HOH B O   1 
HETATM 4847 O  O   . HOH J 6 .   ? 3.02600   8.60600   12.63400 1.000 29.59095 ? 719 HOH B O   1 
HETATM 4848 O  O   . HOH J 6 .   ? 32.11900  17.58200  20.66200 1.000 21.81969 ? 720 HOH B O   1 
HETATM 4849 O  O   . HOH J 6 .   ? 38.72000  22.96700  31.40400 1.000 30.73581 ? 721 HOH B O   1 
HETATM 4850 O  O   . HOH J 6 .   ? 15.60900  -1.25800  25.73100 1.000 25.32518 ? 722 HOH B O   1 
HETATM 4851 O  O   . HOH J 6 .   ? -9.23900  10.69400  23.45200 1.000 30.10714 ? 723 HOH B O   1 
HETATM 4852 O  O   . HOH J 6 .   ? 31.95700  30.64900  23.74900 1.000 28.95523 ? 724 HOH B O   1 
HETATM 4853 O  O   . HOH J 6 .   ? 37.59600  7.74200   32.44300 1.000 26.08775 ? 725 HOH B O   1 
HETATM 4854 O  O   . HOH J 6 .   ? 13.58200  12.69100  18.20100 1.000 24.82893 ? 726 HOH B O   1 
HETATM 4855 O  O   . HOH J 6 .   ? 17.30000  2.25700   35.86200 1.000 29.16227 ? 727 HOH B O   1 
HETATM 4856 O  O   . HOH J 6 .   ? 7.95600   36.03700  16.78000 1.000 34.48741 ? 728 HOH B O   1 
HETATM 4857 O  O   . HOH J 6 .   ? 22.27600  0.34600   35.03400 1.000 31.64743 ? 729 HOH B O   1 
HETATM 4858 O  O   . HOH J 6 .   ? 30.52100  30.57400  25.81100 1.000 31.96265 ? 730 HOH B O   1 
HETATM 4859 O  O   . HOH J 6 .   ? 19.71400  9.26500   36.18600 1.000 31.67847 ? 731 HOH B O   1 
HETATM 4860 O  O   . HOH J 6 .   ? 0.93000   -0.38500  28.18600 1.000 31.65582 ? 732 HOH B O   1 
HETATM 4861 O  O   . HOH J 6 .   ? 29.13900  3.81900   32.94900 1.000 27.25624 ? 733 HOH B O   1 
HETATM 4862 O  O   . HOH J 6 .   ? 1.74100   25.49600  10.04900 1.000 39.96376 ? 734 HOH B O   1 
HETATM 4863 O  O   . HOH J 6 .   ? 32.15500  19.85300  16.78400 1.000 25.59571 ? 735 HOH B O   1 
HETATM 4864 O  O   . HOH J 6 .   ? -5.06200  12.33100  10.35000 1.000 28.03524 ? 736 HOH B O   1 
HETATM 4865 O  O   . HOH J 6 .   ? 4.98100   2.81600   16.55400 1.000 32.68657 ? 737 HOH B O   1 
HETATM 4866 O  O   . HOH J 6 .   ? 10.43500  11.24000  19.48800 1.000 28.36587 ? 738 HOH B O   1 
HETATM 4867 O  O   . HOH J 6 .   ? 19.62600  4.24500   35.05500 1.000 29.69039 ? 739 HOH B O   1 
HETATM 4868 O  O   . HOH J 6 .   ? 5.29700   4.59300   33.07400 1.000 33.08283 ? 740 HOH B O   1 
HETATM 4869 O  O   . HOH J 6 .   ? -8.03600  8.20900   34.41500 1.000 38.25357 ? 741 HOH B O   1 
HETATM 4870 O  O   . HOH J 6 .   ? 28.738    30.656    28.408   1.000 29.68189 ? 742 HOH B O   1 
HETATM 4871 O  O   . HOH J 6 .   ? -9.084    4.139     15.080   1.000 31.98512 ? 743 HOH B O   1 
HETATM 4872 O  O   . HOH J 6 .   ? 6.73100   19.43900  12.75600 1.000 30.66140 ? 744 HOH B O   1 
HETATM 4873 O  O   . HOH J 6 .   ? 28.12700  11.92600  34.24000 1.000 25.39743 ? 745 HOH B O   1 
HETATM 4874 O  O   . HOH J 6 .   ? 25.89400  25.65400  18.37700 1.000 27.98803 ? 746 HOH B O   1 
HETATM 4875 O  O   . HOH J 6 .   ? 6.15100   3.61200   18.78600 1.000 25.34633 ? 747 HOH B O   1 
HETATM 4876 O  O   . HOH J 6 .   ? 3.62300   -11.40800 26.64000 1.000 42.34199 ? 748 HOH B O   1 
HETATM 4877 O  O   . HOH J 6 .   ? 17.59700  21.77100  39.12500 1.000 26.65506 ? 749 HOH B O   1 
HETATM 4878 O  O   . HOH J 6 .   ? 10.07900  3.89100   40.26800 1.000 38.01662 ? 750 HOH B O   1 
HETATM 4879 O  O   . HOH J 6 .   ? 39.91500  14.42400  33.90900 1.000 33.74783 ? 751 HOH B O   1 
HETATM 4880 O  O   . HOH J 6 .   ? 12.89900  28.47700  8.17100  1.000 59.79288 ? 752 HOH B O   1 
HETATM 4881 O  O   . HOH J 6 .   ? -11.436   3.489     14.418   1.000 26.97486 ? 753 HOH B O   1 
HETATM 4882 O  O   . HOH J 6 .   ? 40.73300  10.51100  32.56600 1.000 32.95210 ? 754 HOH B O   1 
HETATM 4883 O  O   . HOH J 6 .   ? 14.50200  23.67600  37.48400 1.000 29.55966 ? 755 HOH B O   1 
HETATM 4884 O  O   . HOH J 6 .   ? 5.54400   12.07000  12.39800 1.000 30.00242 ? 756 HOH B O   1 
HETATM 4885 O  O   . HOH J 6 .   ? -12.26500 12.81100  33.11700 1.000 37.39498 ? 757 HOH B O   1 
HETATM 4886 O  O   . HOH J 6 .   ? 22.51100  14.02500  36.69300 1.000 28.31927 ? 758 HOH B O   1 
HETATM 4887 O  O   . HOH J 6 .   ? 0.43900   24.17600  8.58700  1.000 37.09295 ? 759 HOH B O   1 
HETATM 4888 O  O   . HOH J 6 .   ? 43.24600  8.96500   20.42600 1.000 30.09958 ? 760 HOH B O   1 
HETATM 4889 O  O   . HOH J 6 .   ? -9.10700  14.87900  8.61800  1.000 38.89290 ? 761 HOH B O   1 
HETATM 4890 O  O   . HOH J 6 .   ? -8.56200  23.13600  11.07000 1.000 36.15564 ? 762 HOH B O   1 
HETATM 4891 O  O   . HOH J 6 .   ? -10.85000 6.98500   25.66300 1.000 35.41512 ? 763 HOH B O   1 
HETATM 4892 O  O   . HOH J 6 .   ? 9.55300   6.55100   41.31000 1.000 36.56200 ? 764 HOH B O   1 
HETATM 4893 O  O   . HOH J 6 .   ? 5.00900   -9.62200  28.63300 1.000 41.82753 ? 765 HOH B O   1 
HETATM 4894 O  O   . HOH J 6 .   ? 41.63300  19.48400  26.58300 1.000 36.00803 ? 766 HOH B O   1 
HETATM 4895 O  O   . HOH J 6 .   ? -16.667   10.800    30.857   1.000 38.07266 ? 767 HOH B O   1 
HETATM 4896 O  O   . HOH J 6 .   ? 16.61100  6.25500   37.74000 1.000 29.50154 ? 768 HOH B O   1 
HETATM 4897 O  O   . HOH J 6 .   ? 33.62100  24.00500  18.79700 1.000 31.52089 ? 769 HOH B O   1 
HETATM 4898 O  O   . HOH J 6 .   ? 25.27500  12.67200  37.09800 1.000 30.80776 ? 770 HOH B O   1 
HETATM 4899 O  O   . HOH J 6 .   ? 23.93400  26.52900  36.80700 1.000 31.73426 ? 771 HOH B O   1 
HETATM 4900 O  O   . HOH J 6 .   ? 44.99700  7.44700   21.48800 1.000 31.63024 ? 772 HOH B O   1 
HETATM 4901 O  O   . HOH J 6 .   ? 39.88200  8.21500   33.23600 1.000 30.11993 ? 773 HOH B O   1 
HETATM 4902 O  O   . HOH J 6 .   ? -15.101   15.253    21.751   1.000 42.59035 ? 774 HOH B O   1 
HETATM 4903 O  O   . HOH J 6 .   ? 4.45300   10.32600  11.06400 1.000 29.54973 ? 775 HOH B O   1 
HETATM 4904 O  O   . HOH J 6 .   ? -13.31600 10.56900  32.68000 1.000 39.65962 ? 776 HOH B O   1 
HETATM 4905 O  O   . HOH J 6 .   ? 4.36500   37.10900  14.73000 1.000 36.26775 ? 777 HOH B O   1 
HETATM 4906 O  O   . HOH J 6 .   ? 45.09900  18.76500  26.75300 1.000 39.38476 ? 778 HOH B O   1 
HETATM 4907 O  O   . HOH J 6 .   ? 37.62900  24.73500  22.25500 1.000 41.02876 ? 779 HOH B O   1 
HETATM 4908 O  O   . HOH J 6 .   ? 23.13200  22.21100  -0.76700 1.000 37.00895 ? 780 HOH B O   1 
HETATM 4909 O  O   . HOH J 6 .   ? 43.73200  17.85600  25.20000 1.000 42.15847 ? 781 HOH B O   1 
HETATM 4910 O  O   . HOH J 6 .   ? 7.345     19.285    46.866   1.000 43.11968 ? 782 HOH B O   1 
HETATM 4911 O  O   . HOH J 6 .   ? 42.62100  11.52600  33.58900 1.000 39.42660 ? 783 HOH B O   1 
HETATM 4912 O  O   . HOH J 6 .   ? -9.37900  20.98000  10.89700 1.000 38.92085 ? 784 HOH B O   1 
HETATM 4913 O  O   . HOH J 6 .   ? 16.33300  24.61300  38.44600 1.000 30.75712 ? 785 HOH B O   1 
HETATM 4914 O  O   . HOH J 6 .   ? 22.85100  2.40000   36.27500 1.000 34.27941 ? 786 HOH B O   1 
HETATM 4915 O  O   . HOH J 6 .   ? 16.73900  21.63600  41.21100 1.000 30.72223 ? 787 HOH B O   1 
HETATM 4916 O  O   . HOH J 6 .   ? -10.77200 23.17300  32.26200 1.000 41.01586 ? 788 HOH B O   1 
HETATM 4917 O  O   . HOH J 6 .   ? -18.867   22.170    21.941   1.000 45.23123 ? 789 HOH B O   1 
HETATM 4918 O  O   . HOH J 6 .   ? 42.87900  19.82700  24.44400 1.000 42.80998 ? 790 HOH B O   1 
HETATM 4919 O  O   . HOH J 6 .   ? 39.86500  20.58300  21.16700 1.000 49.13508 ? 791 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   ? 0.64561 0.24806 0.76146 -0.05267 -0.04540 -0.00647 6   LYS A N   
2    C CA  . LYS A 6   ? 0.61062 0.24238 0.72837 -0.05412 -0.04536 0.00046  6   LYS A CA  
3    C C   . LYS A 6   ? 0.60118 0.24454 0.70777 -0.04395 -0.04113 -0.01593 6   LYS A C   
4    O O   . LYS A 6   ? 0.64143 0.27874 0.74086 -0.02950 -0.03520 -0.02462 6   LYS A O   
5    C CB  . LYS A 6   ? 0.59510 0.23769 0.72054 -0.04842 -0.04451 0.02021  6   LYS A CB  
6    C CG  . LYS A 6   ? 0.59687 0.26802 0.72415 -0.04831 -0.04348 0.02591  6   LYS A CG  
7    C CD  . LYS A 6   ? 0.60823 0.29073 0.74198 -0.04799 -0.04407 0.04776  6   LYS A CD  
8    C CE  . LYS A 6   ? 0.60952 0.28482 0.74210 -0.03102 -0.04199 0.04949  6   LYS A CE  
9    N NZ  . LYS A 6   ? 0.58013 0.27138 0.71634 -0.03069 -0.04371 0.06959  6   LYS A NZ  
10   N N   . PRO A 7   ? 0.56941 0.23054 0.67540 -0.05195 -0.04441 -0.01942 7   PRO A N   
11   C CA  . PRO A 7   ? 0.54927 0.22012 0.64333 -0.04376 -0.04186 -0.03424 7   PRO A CA  
12   C C   . PRO A 7   ? 0.51935 0.20659 0.61467 -0.02996 -0.03618 -0.02876 7   PRO A C   
13   O O   . PRO A 7   ? 0.50496 0.20885 0.60941 -0.03074 -0.03614 -0.01340 7   PRO A O   
14   C CB  . PRO A 7   ? 0.53764 0.22518 0.63381 -0.05726 -0.04932 -0.03630 7   PRO A CB  
15   C CG  . PRO A 7   ? 0.55591 0.23713 0.66543 -0.07403 -0.05525 -0.02650 7   PRO A CG  
16   C CD  . PRO A 7   ? 0.55182 0.22437 0.66846 -0.07007 -0.05119 -0.01084 7   PRO A CD  
17   N N   . GLN A 8   ? 0.48321 0.16991 0.56608 -0.01820 -0.03022 -0.04124 8   GLN A N   
18   C CA  . GLN A 8   ? 0.47542 0.17725 0.55880 -0.00502 -0.02412 -0.03791 8   GLN A CA  
19   C C   . GLN A 8   ? 0.45787 0.17993 0.53103 -0.00400 -0.02364 -0.04433 8   GLN A C   
20   O O   . GLN A 8   ? 0.47480 0.19884 0.53826 -0.01200 -0.02814 -0.05224 8   GLN A O   
21   C CB  . GLN A 8   ? 0.47956 0.17052 0.55636 0.00761  -0.01617 -0.04484 8   GLN A CB  
22   C CG  . GLN A 8   ? 0.48944 0.16421 0.57481 0.00979  -0.01660 -0.03767 8   GLN A CG  
23   C CD  . GLN A 8   ? 0.48123 0.16782 0.58029 0.01357  -0.01834 -0.01960 8   GLN A CD  
24   O OE1 . GLN A 8   ? 0.46828 0.16947 0.56935 0.02388  -0.01449 -0.01731 8   GLN A OE1 
25   N NE2 . GLN A 8   ? 0.51127 0.19205 0.61929 0.00404  -0.02459 -0.00602 8   GLN A NE2 
26   N N   . LEU A 9   ? 0.44962 0.18890 0.52344 0.00586  -0.01864 -0.03988 9   LEU A N   
27   C CA  . LEU A 9   ? 0.45374 0.21111 0.51613 0.00851  -0.01725 -0.04500 9   LEU A CA  
28   C C   . LEU A 9   ? 0.45531 0.19801 0.50201 0.01142  -0.01365 -0.06025 9   LEU A C   
29   O O   . LEU A 9   ? 0.46900 0.19382 0.51686 0.01784  -0.00773 -0.06693 9   LEU A O   
30   C CB  . LEU A 9   ? 0.41741 0.19308 0.48527 0.01795  -0.01273 -0.03754 9   LEU A CB  
31   C CG  . LEU A 9   ? 0.40075 0.19616 0.47923 0.01591  -0.01509 -0.02417 9   LEU A CG  
32   C CD1 . LEU A 9   ? 0.39313 0.19289 0.47927 0.02568  -0.01111 -0.01760 9   LEU A CD1 
33   C CD2 . LEU A 9   ? 0.37866 0.19688 0.45377 0.01337  -0.01754 -0.02477 9   LEU A CD2 
34   N N   . GLN A 10  ? 0.44086 0.19219 0.47299 0.00697  -0.01716 -0.06571 10  GLN A N   
35   C CA  . GLN A 10  ? 0.46207 0.20182 0.47384 0.00752  -0.01422 -0.07950 10  GLN A CA  
36   C C   . GLN A 10  ? 0.45854 0.20794 0.46503 0.01714  -0.00554 -0.07927 10  GLN A C   
37   O O   . GLN A 10  ? 0.45381 0.22229 0.46175 0.01851  -0.00752 -0.07129 10  GLN A O   
38   C CB  . GLN A 10  ? 0.45996 0.20435 0.45693 -0.00261 -0.02394 -0.08369 10  GLN A CB  
39   C CG  . GLN A 10  ? 0.46674 0.20521 0.47120 -0.01410 -0.03347 -0.08373 10  GLN A CG  
40   C CD  . GLN A 10  ? 0.46896 0.17904 0.47227 -0.01666 -0.03156 -0.09399 10  GLN A CD  
41   O OE1 . GLN A 10  ? 0.48041 0.17468 0.46799 -0.01327 -0.02600 -0.10737 10  GLN A OE1 
42   N NE2 . GLN A 10  ? 0.48074 0.18402 0.50118 -0.02288 -0.03566 -0.08791 10  GLN A NE2 
43   N N   . ARG A 11  ? 0.46480 0.20123 0.46720 0.02363  0.00433  -0.08856 11  ARG A N   
44   C CA  . ARG A 11  ? 0.46425 0.20952 0.45976 0.03057  0.01382  -0.09032 11  ARG A CA  
45   C C   . ARG A 11  ? 0.47803 0.22056 0.44483 0.02457  0.01410  -0.09985 11  ARG A C   
46   O O   . ARG A 11  ? 0.49553 0.22143 0.44779 0.02002  0.01424  -0.11282 11  ARG A O   
47   C CB  . ARG A 11  ? 0.45841 0.19495 0.46617 0.04072  0.02550  -0.09604 11  ARG A CB  
48   C CG  . ARG A 11  ? 0.46092 0.21015 0.49191 0.04804  0.02481  -0.08195 11  ARG A CG  
49   C CD  . ARG A 11  ? 0.45783 0.19895 0.49954 0.04578  0.01750  -0.07472 11  ARG A CD  
50   N NE  . ARG A 11  ? 0.45494 0.20670 0.51411 0.05282  0.01762  -0.06266 11  ARG A NE  
51   C CZ  . ARG A 11  ? 0.44853 0.19807 0.51913 0.05071  0.01134  -0.05193 11  ARG A CZ  
52   N NH1 . ARG A 11  ? 0.44667 0.18498 0.51573 0.04148  0.00500  -0.05090 11  ARG A NH1 
53   N NH2 . ARG A 11  ? 0.44685 0.20585 0.53140 0.05705  0.01095  -0.04179 11  ARG A NH2 
54   N N   . LEU A 12  ? 0.47304 0.23078 0.43078 0.02396  0.01335  -0.09327 12  LEU A N   
55   C CA  . LEU A 12  ? 0.48798 0.24454 0.41648 0.01749  0.01213  -0.09861 12  LEU A CA  
56   C C   . LEU A 12  ? 0.48923 0.25141 0.40948 0.02214  0.02551  -0.09977 12  LEU A C   
57   O O   . LEU A 12  ? 0.49371 0.26382 0.43404 0.03021  0.03344  -0.09496 12  LEU A O   
58   C CB  . LEU A 12  ? 0.49226 0.26062 0.41654 0.01135  -0.00218 -0.08835 12  LEU A CB  
59   C CG  . LEU A 12  ? 0.49303 0.26087 0.42498 0.00473  -0.01598 -0.08705 12  LEU A CG  
60   C CD1 . LEU A 12  ? 0.48314 0.26679 0.41771 0.00170  -0.02859 -0.07668 12  LEU A CD1 
61   C CD2 . LEU A 12  ? 0.52346 0.27465 0.43504 -0.00336 -0.01930 -0.10036 12  LEU A CD2 
62   N N   . ALA A 13  ? 0.54722 0.30625 0.43725 0.01597  0.02777  -0.10591 13  ALA A N   
63   C CA  . ALA A 13  ? 0.56850 0.33596 0.44770 0.01732  0.03963  -0.10411 13  ALA A CA  
64   C C   . ALA A 13  ? 0.58997 0.37124 0.47320 0.01575  0.03129  -0.08714 13  ALA A C   
65   O O   . ALA A 13  ? 0.58583 0.36900 0.47043 0.01208  0.01599  -0.07981 13  ALA A O   
66   C CB  . ALA A 13  ? 0.60982 0.36971 0.45150 0.00968  0.04508  -0.11560 13  ALA A CB  
67   N N   . ALA A 14  ? 0.58382 0.37507 0.47210 0.01878  0.04143  -0.08135 14  ALA A N   
68   C CA  . ALA A 14  ? 0.57752 0.37880 0.46928 0.01683  0.03348  -0.06603 14  ALA A CA  
69   C C   . ALA A 14  ? 0.60198 0.39927 0.46321 0.00710  0.02291  -0.06143 14  ALA A C   
70   O O   . ALA A 14  ? 0.60688 0.40787 0.47308 0.00558  0.00878  -0.05008 14  ALA A O   
71   C CB  . ALA A 14  ? 0.55969 0.37126 0.46133 0.01977  0.04645  -0.06111 14  ALA A CB  
72   N N   . ASP A 15  ? 0.60392 0.39366 0.43360 0.00066  0.02882  -0.07070 15  ASP A N   
73   C CA  . ASP A 15  ? 0.60960 0.39497 0.40528 -0.00977 0.01794  -0.06657 15  ASP A CA  
74   C C   . ASP A 15  ? 0.58736 0.36566 0.37809 -0.01341 0.00106  -0.07106 15  ASP A C   
75   O O   . ASP A 15  ? 0.60701 0.38085 0.36747 -0.02253 -0.00884 -0.07046 15  ASP A O   
76   C CB  . ASP A 15  ? 0.63764 0.41980 0.39755 -0.01652 0.03243  -0.07521 15  ASP A CB  
77   C CG  . ASP A 15  ? 0.67596 0.44903 0.42915 -0.01460 0.04373  -0.09718 15  ASP A CG  
78   O OD1 . ASP A 15  ? 0.66145 0.42627 0.42601 -0.01243 0.03498  -0.10482 15  ASP A OD1 
79   O OD2 . ASP A 15  ? 0.72665 0.50067 0.46347 -0.01562 0.06207  -0.10747 15  ASP A OD2 
80   N N   . ALA A 16  ? 0.60538 0.38345 0.42445 -0.00764 -0.00296 -0.07472 16  ALA A N   
81   C CA  . ALA A 16  ? 0.60808 0.38063 0.42498 -0.01243 -0.01755 -0.07975 16  ALA A CA  
82   C C   . ALA A 16  ? 0.59742 0.37705 0.41301 -0.01676 -0.03727 -0.06681 16  ALA A C   
83   O O   . ALA A 16  ? 0.58033 0.36886 0.40947 -0.01293 -0.04067 -0.05360 16  ALA A O   
84   C CB  . ALA A 16  ? 0.57980 0.35195 0.42913 -0.00635 -0.01679 -0.08372 16  ALA A CB  
85   N N   . ASP A 17  ? 0.56778 0.34292 0.36785 -0.02482 -0.05106 -0.07139 17  ASP A N   
86   C CA  . ASP A 17  ? 0.56307 0.34628 0.36839 -0.02808 -0.07199 -0.06046 17  ASP A CA  
87   C C   . ASP A 17  ? 0.54511 0.34080 0.39220 -0.01978 -0.07554 -0.05313 17  ASP A C   
88   O O   . ASP A 17  ? 0.55588 0.35222 0.42450 -0.01546 -0.06732 -0.05907 17  ASP A O   
89   C CB  . ASP A 17  ? 0.57109 0.34912 0.36160 -0.03766 -0.08557 -0.06943 17  ASP A CB  
90   C CG  . ASP A 17  ? 0.58653 0.37621 0.39257 -0.03989 -0.10790 -0.05960 17  ASP A CG  
91   O OD1 . ASP A 17  ? 0.58201 0.38104 0.40101 -0.03487 -0.11436 -0.04550 17  ASP A OD1 
92   O OD2 . ASP A 17  ? 0.59172 0.38131 0.39919 -0.04669 -0.11936 -0.06659 17  ASP A OD2 
93   N N   . VAL A 18  ? 0.56656 0.37186 0.42491 -0.01753 -0.08785 -0.04020 18  VAL A N   
94   C CA  . VAL A 18  ? 0.55018 0.36852 0.44726 -0.00928 -0.08940 -0.03559 18  VAL A CA  
95   C C   . VAL A 18  ? 0.52867 0.35597 0.44448 -0.01207 -0.10154 -0.03901 18  VAL A C   
96   O O   . VAL A 18  ? 0.49404 0.33159 0.43914 -0.00735 -0.09804 -0.03997 18  VAL A O   
97   C CB  . VAL A 18  ? 0.52767 0.35217 0.43512 -0.00397 -0.09587 -0.02245 18  VAL A CB  
98   C CG1 . VAL A 18  ? 0.54328 0.37052 0.44517 -0.00801 -0.11692 -0.01476 18  VAL A CG1 
99   C CG2 . VAL A 18  ? 0.47739 0.31439 0.42215 0.00531  -0.09242 -0.02130 18  VAL A CG2 
100  N N   . ASP A 19  ? 0.52654 0.35096 0.42483 -0.02079 -0.11527 -0.04113 19  ASP A N   
101  C CA  . ASP A 19  ? 0.52478 0.35875 0.44195 -0.02545 -0.12693 -0.04523 19  ASP A CA  
102  C C   . ASP A 19  ? 0.51093 0.33929 0.43666 -0.02654 -0.11347 -0.05548 19  ASP A C   
103  O O   . ASP A 19  ? 0.49013 0.33084 0.44575 -0.02528 -0.11403 -0.05501 19  ASP A O   
104  C CB  . ASP A 19  ? 0.54534 0.37610 0.43927 -0.03565 -0.14477 -0.04615 19  ASP A CB  
105  C CG  . ASP A 19  ? 0.59287 0.42276 0.46794 -0.03546 -0.15640 -0.03445 19  ASP A CG  
106  O OD1 . ASP A 19  ? 0.64097 0.48199 0.54001 -0.02768 -0.16296 -0.02363 19  ASP A OD1 
107  O OD2 . ASP A 19  ? 0.65378 0.47140 0.49004 -0.04343 -0.15910 -0.03636 19  ASP A OD2 
108  N N   . ARG A 20  ? 0.53612 0.34671 0.43679 -0.02885 -0.10181 -0.06411 20  ARG A N   
109  C CA  . ARG A 20  ? 0.53337 0.33480 0.44227 -0.02826 -0.08885 -0.07293 20  ARG A CA  
110  C C   . ARG A 20  ? 0.50046 0.31245 0.43969 -0.01896 -0.07931 -0.06637 20  ARG A C   
111  O O   . ARG A 20  ? 0.48605 0.30045 0.44548 -0.01994 -0.07691 -0.06780 20  ARG A O   
112  C CB  . ARG A 20  ? 0.56083 0.34334 0.44000 -0.02870 -0.07616 -0.08272 20  ARG A CB  
113  C CG  . ARG A 20  ? 0.58455 0.35467 0.47234 -0.02555 -0.06188 -0.09173 20  ARG A CG  
114  C CD  . ARG A 20  ? 0.62721 0.37970 0.48585 -0.02632 -0.05042 -0.10469 20  ARG A CD  
115  N NE  . ARG A 20  ? 0.66307 0.40404 0.49606 -0.03730 -0.05944 -0.11652 20  ARG A NE  
116  C CZ  . ARG A 20  ? 0.66195 0.39120 0.50055 -0.04343 -0.06383 -0.12684 20  ARG A CZ  
117  N NH1 . ARG A 20  ? 0.64302 0.37020 0.51168 -0.04013 -0.06024 -0.12508 20  ARG A NH1 
118  N NH2 . ARG A 20  ? 0.67567 0.39440 0.48810 -0.05412 -0.07275 -0.13876 20  ARG A NH2 
119  N N   . MET A 21  ? 0.51153 0.33014 0.45369 -0.01101 -0.07477 -0.05853 21  MET A N   
120  C CA  . MET A 21  ? 0.46261 0.29185 0.43078 -0.00270 -0.06683 -0.05323 21  MET A CA  
121  C C   . MET A 21  ? 0.44522 0.29316 0.44056 -0.00288 -0.07590 -0.04894 21  MET A C   
122  O O   . MET A 21  ? 0.42913 0.28314 0.44290 -0.00287 -0.07117 -0.04937 21  MET A O   
123  C CB  . MET A 21  ? 0.46426 0.29530 0.42870 0.00436  -0.06145 -0.04693 21  MET A CB  
124  C CG  . MET A 21  ? 0.48311 0.29971 0.42423 0.00445  -0.04947 -0.05137 21  MET A CG  
125  S SD  . MET A 21  ? 0.44996 0.26935 0.38768 0.01006  -0.04279 -0.04307 21  MET A SD  
126  C CE  . MET A 21  ? 0.49782 0.30288 0.40409 0.00627  -0.03001 -0.05076 21  MET A CE  
127  N N   . CYS A 22  ? 0.45214 0.31015 0.45089 -0.00327 -0.08903 -0.04445 22  CYS A N   
128  C CA  . CYS A 22  ? 0.42862 0.30733 0.45622 -0.00285 -0.09729 -0.04198 22  CYS A CA  
129  C C   . CYS A 22  ? 0.43353 0.31514 0.46978 -0.01180 -0.09928 -0.04688 22  CYS A C   
130  O O   . CYS A 22  ? 0.42745 0.32571 0.48922 -0.01180 -0.09723 -0.04571 22  CYS A O   
131  C CB  . CYS A 22  ? 0.43782 0.32434 0.46735 -0.00223 -0.11361 -0.03709 22  CYS A CB  
132  S SG  . CYS A 22  ? 0.47257 0.35821 0.50250 0.00829  -0.11339 -0.02901 22  CYS A SG  
133  N N   . ARG A 23  ? 0.44417 0.30971 0.45884 -0.02043 -0.10303 -0.05280 23  ARG A N   
134  C CA  . ARG A 23  ? 0.44203 0.30673 0.46436 -0.03059 -0.10610 -0.05790 23  ARG A CA  
135  C C   . ARG A 23  ? 0.42334 0.28517 0.45834 -0.02958 -0.09243 -0.05774 23  ARG A C   
136  O O   . ARG A 23  ? 0.41490 0.28891 0.47158 -0.03501 -0.09327 -0.05592 23  ARG A O   
137  C CB  . ARG A 23  ? 0.48134 0.32493 0.47461 -0.03942 -0.11121 -0.06665 23  ARG A CB  
138  C CG  . ARG A 23  ? 0.48932 0.33978 0.47839 -0.04806 -0.13022 -0.06783 23  ARG A CG  
139  C CD  . ARG A 23  ? 0.52331 0.35248 0.48560 -0.05897 -0.13403 -0.07933 23  ARG A CD  
140  N NE  . ARG A 23  ? 0.55462 0.36448 0.48092 -0.05620 -0.12704 -0.08426 23  ARG A NE  
141  C CZ  . ARG A 23  ? 0.57977 0.36935 0.49171 -0.05475 -0.11243 -0.09310 23  ARG A CZ  
142  N NH1 . ARG A 23  ? 0.55932 0.34194 0.48908 -0.05518 -0.10407 -0.09657 23  ARG A NH1 
143  N NH2 . ARG A 23  ? 0.60351 0.37972 0.48299 -0.05309 -0.10621 -0.09835 23  ARG A NH2 
144  N N   . LEU A 24  ? 0.44557 0.29205 0.46765 -0.02325 -0.08009 -0.05882 24  LEU A N   
145  C CA  . LEU A 24  ? 0.42417 0.26611 0.45714 -0.02164 -0.06880 -0.05714 24  LEU A CA  
146  C C   . LEU A 24  ? 0.41391 0.27828 0.46989 -0.01627 -0.06482 -0.04899 24  LEU A C   
147  O O   . LEU A 24  ? 0.41399 0.28185 0.48307 -0.01886 -0.05955 -0.04537 24  LEU A O   
148  C CB  . LEU A 24  ? 0.43671 0.25877 0.45293 -0.01514 -0.05778 -0.06071 24  LEU A CB  
149  C CG  . LEU A 24  ? 0.46504 0.26436 0.45682 -0.01985 -0.05856 -0.07164 24  LEU A CG  
150  C CD1 . LEU A 24  ? 0.45076 0.23576 0.42879 -0.01183 -0.04595 -0.07591 24  LEU A CD1 
151  C CD2 . LEU A 24  ? 0.46491 0.25165 0.46167 -0.02944 -0.06188 -0.07698 24  LEU A CD2 
152  N N   . LEU A 25  ? 0.41525 0.29400 0.47550 -0.00917 -0.06731 -0.04610 25  LEU A N   
153  C CA  . LEU A 25  ? 0.39100 0.29272 0.47363 -0.00474 -0.06448 -0.04138 25  LEU A CA  
154  C C   . LEU A 25  ? 0.37630 0.29798 0.47950 -0.01212 -0.07104 -0.04102 25  LEU A C   
155  O O   . LEU A 25  ? 0.37547 0.31590 0.49690 -0.01187 -0.06563 -0.03820 25  LEU A O   
156  C CB  . LEU A 25  ? 0.38628 0.29583 0.47037 0.00494  -0.06630 -0.03991 25  LEU A CB  
157  C CG  . LEU A 25  ? 0.36773 0.26461 0.43845 0.01249  -0.05826 -0.03885 25  LEU A CG  
158  C CD1 . LEU A 25  ? 0.34341 0.24688 0.41766 0.01994  -0.06247 -0.03680 25  LEU A CD1 
159  C CD2 . LEU A 25  ? 0.35396 0.25351 0.43181 0.01503  -0.04756 -0.03682 25  LEU A CD2 
160  N N   . GLU A 26  ? 0.38214 0.30180 0.48275 -0.01943 -0.08241 -0.04405 26  GLU A N   
161  C CA  . GLU A 26  ? 0.37458 0.31579 0.49842 -0.02729 -0.08927 -0.04380 26  GLU A CA  
162  C C   . GLU A 26  ? 0.36862 0.30695 0.49864 -0.03824 -0.08369 -0.04252 26  GLU A C   
163  O O   . GLU A 26  ? 0.35815 0.31891 0.51046 -0.04207 -0.07984 -0.03909 26  GLU A O   
164  C CB  . GLU A 26  ? 0.39336 0.33392 0.51307 -0.03237 -0.10546 -0.04692 26  GLU A CB  
165  C CG  . GLU A 26  ? 0.42833 0.37870 0.55131 -0.02289 -0.11420 -0.04513 26  GLU A CG  
166  C CD  . GLU A 26  ? 0.47335 0.45614 0.63189 -0.01908 -0.11751 -0.04370 26  GLU A CD  
167  O OE1 . GLU A 26  ? 0.47310 0.47372 0.65288 -0.02625 -0.11410 -0.04429 26  GLU A OE1 
168  O OE2 . GLU A 26  ? 0.47879 0.46924 0.64505 -0.00904 -0.12326 -0.04210 26  GLU A OE2 
169  N N   . GLU A 27  ? 0.39312 0.30384 0.50419 -0.04374 -0.08285 -0.04532 27  GLU A N   
170  C CA  . GLU A 27  ? 0.42295 0.32616 0.54050 -0.05504 -0.07965 -0.04337 27  GLU A CA  
171  C C   . GLU A 27  ? 0.42064 0.31256 0.53454 -0.05086 -0.06702 -0.03780 27  GLU A C   
172  O O   . GLU A 27  ? 0.43346 0.33377 0.56099 -0.05757 -0.06229 -0.03077 27  GLU A O   
173  C CB  . GLU A 27  ? 0.46998 0.34791 0.57296 -0.06482 -0.08751 -0.05085 27  GLU A CB  
174  C CG  . GLU A 27  ? 0.51861 0.38539 0.63082 -0.07703 -0.08476 -0.04796 27  GLU A CG  
175  C CD  . GLU A 27  ? 0.60468 0.44592 0.70575 -0.08797 -0.09320 -0.05709 27  GLU A CD  
176  O OE1 . GLU A 27  ? 0.61723 0.43094 0.69564 -0.08309 -0.09124 -0.06515 27  GLU A OE1 
177  O OE2 . GLU A 27  ? 0.64395 0.49357 0.76001 -0.10192 -0.10138 -0.05708 27  GLU A OE2 
178  N N   . ASP A 28  ? 0.41116 0.28448 0.50719 -0.04090 -0.06193 -0.04003 28  ASP A N   
179  C CA  . ASP A 28  ? 0.39884 0.26221 0.49372 -0.03646 -0.05193 -0.03426 28  ASP A CA  
180  C C   . ASP A 28  ? 0.37098 0.25542 0.47297 -0.02744 -0.04550 -0.02845 28  ASP A C   
181  O O   . ASP A 28  ? 0.37322 0.26012 0.48001 -0.02732 -0.03907 -0.02089 28  ASP A O   
182  C CB  . ASP A 28  ? 0.42182 0.25623 0.49821 -0.03037 -0.04879 -0.04022 28  ASP A CB  
183  C CG  . ASP A 28  ? 0.47466 0.28373 0.54557 -0.03958 -0.05259 -0.04631 28  ASP A CG  
184  O OD1 . ASP A 28  ? 0.47716 0.29117 0.55796 -0.05178 -0.05921 -0.04545 28  ASP A OD1 
185  O OD2 . ASP A 28  ? 0.47746 0.26224 0.53591 -0.03479 -0.04873 -0.05279 28  ASP A OD2 
186  N N   . GLY A 29  ? 0.37287 0.27215 0.47567 -0.02059 -0.04816 -0.03163 29  GLY A N   
187  C CA  . GLY A 29  ? 0.34883 0.26644 0.45848 -0.01190 -0.04293 -0.02874 29  GLY A CA  
188  C C   . GLY A 29  ? 0.33046 0.23570 0.42785 -0.00150 -0.03783 -0.02897 29  GLY A C   
189  O O   . GLY A 29  ? 0.31421 0.23286 0.41629 0.00573  -0.03480 -0.02802 29  GLY A O   
190  N N   . ALA A 30  ? 0.35915 0.24015 0.44249 -0.00067 -0.03651 -0.03128 30  ALA A N   
191  C CA  . ALA A 30  ? 0.34575 0.21708 0.42059 0.00860  -0.03065 -0.03149 30  ALA A CA  
192  C C   . ALA A 30  ? 0.36472 0.21207 0.42424 0.00850  -0.02985 -0.03770 30  ALA A C   
193  O O   . ALA A 30  ? 0.37285 0.20819 0.42812 0.00109  -0.03349 -0.04163 30  ALA A O   
194  C CB  . ALA A 30  ? 0.33263 0.20596 0.41410 0.01132  -0.02443 -0.02459 30  ALA A CB  
195  N N   . PHE A 31  ? 0.37167 0.21296 0.42337 0.01628  -0.02455 -0.03945 31  PHE A N   
196  C CA  . PHE A 31  ? 0.37871 0.19961 0.41645 0.01755  -0.02036 -0.04649 31  PHE A CA  
197  C C   . PHE A 31  ? 0.39441 0.21635 0.43158 0.02661  -0.01239 -0.04560 31  PHE A C   
198  O O   . PHE A 31  ? 0.37934 0.21610 0.42455 0.03076  -0.01217 -0.04015 31  PHE A O   
199  C CB  . PHE A 31  ? 0.39368 0.20850 0.41414 0.01219  -0.02602 -0.05351 31  PHE A CB  
200  C CG  . PHE A 31  ? 0.39083 0.21718 0.40560 0.01472  -0.02932 -0.05106 31  PHE A CG  
201  C CD1 . PHE A 31  ? 0.37451 0.21768 0.39985 0.01319  -0.03778 -0.04652 31  PHE A CD1 
202  C CD2 . PHE A 31  ? 0.41117 0.23164 0.41179 0.01856  -0.02373 -0.05305 31  PHE A CD2 
203  C CE1 . PHE A 31  ? 0.37567 0.22653 0.39819 0.01627  -0.04207 -0.04371 31  PHE A CE1 
204  C CE2 . PHE A 31  ? 0.41337 0.24200 0.40918 0.01990  -0.02764 -0.04881 31  PHE A CE2 
205  C CZ  . PHE A 31  ? 0.38642 0.22876 0.39353 0.01917  -0.03757 -0.04398 31  PHE A CZ  
206  N N   . ILE A 32  ? 0.41044 0.21709 0.43910 0.02932  -0.00559 -0.05221 32  ILE A N   
207  C CA  . ILE A 32  ? 0.42032 0.22850 0.45068 0.03719  0.00328  -0.05242 32  ILE A CA  
208  C C   . ILE A 32  ? 0.43459 0.23706 0.44484 0.03580  0.00727  -0.05968 32  ILE A C   
209  O O   . ILE A 32  ? 0.44421 0.23373 0.43907 0.03088  0.00651  -0.06810 32  ILE A O   
210  C CB  . ILE A 32  ? 0.41801 0.21608 0.46057 0.04295  0.00966  -0.05357 32  ILE A CB  
211  C CG1 . ILE A 32  ? 0.39579 0.20245 0.45609 0.04423  0.00549  -0.04295 32  ILE A CG1 
212  C CG2 . ILE A 32  ? 0.43111 0.23051 0.47548 0.05047  0.01987  -0.05699 32  ILE A CG2 
213  C CD1 . ILE A 32  ? 0.40004 0.19448 0.47271 0.04831  0.00763  -0.04125 32  ILE A CD1 
214  N N   . LEU A 33  ? 0.42785 0.24005 0.43698 0.03891  0.01106  -0.05618 33  LEU A N   
215  C CA  . LEU A 33  ? 0.43511 0.24324 0.42602 0.03781  0.01821  -0.06125 33  LEU A CA  
216  C C   . LEU A 33  ? 0.44397 0.25177 0.44495 0.04488  0.03138  -0.06494 33  LEU A C   
217  O O   . LEU A 33  ? 0.43791 0.25520 0.45977 0.05067  0.03279  -0.05895 33  LEU A O   
218  C CB  . LEU A 33  ? 0.45549 0.27361 0.43996 0.03549  0.01403  -0.05371 33  LEU A CB  
219  C CG  . LEU A 33  ? 0.45329 0.27157 0.42675 0.02913  0.00080  -0.05094 33  LEU A CG  
220  C CD1 . LEU A 33  ? 0.45703 0.27957 0.42032 0.02693  -0.00223 -0.04410 33  LEU A CD1 
221  C CD2 . LEU A 33  ? 0.46522 0.27072 0.41903 0.02294  -0.00150 -0.05972 33  LEU A CD2 
222  N N   . LYS A 34  ? 0.47608 0.27419 0.46304 0.04447  0.04083  -0.07563 34  LYS A N   
223  C CA  . LYS A 34  ? 0.47275 0.27235 0.47177 0.05193  0.05467  -0.08110 34  LYS A CA  
224  C C   . LYS A 34  ? 0.48889 0.30018 0.47984 0.05038  0.06360  -0.07891 34  LYS A C   
225  O O   . LYS A 34  ? 0.51207 0.32080 0.47633 0.04294  0.06446  -0.08091 34  LYS A O   
226  C CB  . LYS A 34  ? 0.47121 0.25424 0.46257 0.05335  0.06203  -0.09638 34  LYS A CB  
227  C CG  . LYS A 34  ? 0.46861 0.23751 0.47157 0.05461  0.05399  -0.09797 34  LYS A CG  
228  C CD  . LYS A 34  ? 0.46554 0.24324 0.49809 0.06203  0.05024  -0.08684 34  LYS A CD  
229  C CE  . LYS A 34  ? 0.50366 0.28717 0.55095 0.07095  0.05760  -0.08958 34  LYS A CE  
230  N NZ  . LYS A 34  ? 0.50825 0.29973 0.57707 0.07589  0.04978  -0.07697 34  LYS A NZ  
231  N N   . GLY A 35  ? 0.45736 0.28178 0.47114 0.05631  0.06925  -0.07371 35  GLY A N   
232  C CA  . GLY A 35  ? 0.44474 0.28098 0.45552 0.05444  0.08002  -0.07205 35  GLY A CA  
233  C C   . GLY A 35  ? 0.45632 0.29640 0.44991 0.04571  0.07318  -0.06210 35  GLY A C   
234  O O   . GLY A 35  ? 0.44568 0.28805 0.42068 0.03964  0.08121  -0.06221 35  GLY A O   
235  N N   . LEU A 36  ? 0.45664 0.29745 0.45634 0.04487  0.05862  -0.05335 36  LEU A N   
236  C CA  . LEU A 36  ? 0.45976 0.30357 0.44986 0.03856  0.05078  -0.04342 36  LEU A CA  
237  C C   . LEU A 36  ? 0.44199 0.29731 0.44340 0.03776  0.05827  -0.03722 36  LEU A C   
238  O O   . LEU A 36  ? 0.43964 0.29513 0.42422 0.03072  0.06321  -0.03347 36  LEU A O   
239  C CB  . LEU A 36  ? 0.43803 0.28288 0.43933 0.04005  0.03559  -0.03771 36  LEU A CB  
240  C CG  . LEU A 36  ? 0.41649 0.26317 0.41324 0.03553  0.02643  -0.02833 36  LEU A CG  
241  C CD1 . LEU A 36  ? 0.45227 0.28989 0.41949 0.02787  0.02420  -0.02729 36  LEU A CD1 
242  C CD2 . LEU A 36  ? 0.39457 0.24404 0.40429 0.03820  0.01348  -0.02577 36  LEU A CD2 
243  N N   . LEU A 37  ? 0.41222 0.27755 0.44158 0.04380  0.05853  -0.03530 37  LEU A N   
244  C CA  . LEU A 37  ? 0.41308 0.29051 0.45747 0.04234  0.06374  -0.02945 37  LEU A CA  
245  C C   . LEU A 37  ? 0.43016 0.31613 0.48241 0.04449  0.08096  -0.03555 37  LEU A C   
246  O O   . LEU A 37  ? 0.43203 0.31722 0.49361 0.05188  0.08603  -0.04398 37  LEU A O   
247  C CB  . LEU A 37  ? 0.39133 0.27725 0.46209 0.04720  0.05508  -0.02555 37  LEU A CB  
248  C CG  . LEU A 37  ? 0.37996 0.26087 0.44752 0.04629  0.03986  -0.02154 37  LEU A CG  
249  C CD1 . LEU A 37  ? 0.33778 0.22870 0.42911 0.05116  0.03405  -0.02040 37  LEU A CD1 
250  C CD2 . LEU A 37  ? 0.35613 0.23249 0.41218 0.03904  0.03486  -0.01442 37  LEU A CD2 
251  N N   . PRO A 38  ? 0.42010 0.31449 0.47078 0.03810  0.09015  -0.03124 38  PRO A N   
252  C CA  . PRO A 38  ? 0.42890 0.33676 0.49310 0.04027  0.10800  -0.03716 38  PRO A CA  
253  C C   . PRO A 38  ? 0.42160 0.34263 0.52384 0.04933  0.10672  -0.03775 38  PRO A C   
254  O O   . PRO A 38  ? 0.42806 0.34908 0.54321 0.05162  0.09275  -0.03221 38  PRO A O   
255  C CB  . PRO A 38  ? 0.42504 0.34037 0.48081 0.02896  0.11516  -0.02859 38  PRO A CB  
256  C CG  . PRO A 38  ? 0.42095 0.32104 0.45014 0.02120  0.10149  -0.01973 38  PRO A CG  
257  C CD  . PRO A 38  ? 0.40190 0.29396 0.44000 0.02824  0.08460  -0.02013 38  PRO A CD  
258  N N   . PHE A 39  ? 0.40249 0.33608 0.52335 0.05470  0.12137  -0.04500 39  PHE A N   
259  C CA  . PHE A 39  ? 0.40090 0.34899 0.56006 0.06305  0.11861  -0.04395 39  PHE A CA  
260  C C   . PHE A 39  ? 0.40017 0.36391 0.57701 0.05644  0.11594  -0.03423 39  PHE A C   
261  O O   . PHE A 39  ? 0.38745 0.35862 0.58790 0.06023  0.10482  -0.03003 39  PHE A O   
262  C CB  . PHE A 39  ? 0.40417 0.36257 0.58450 0.07228  0.13377  -0.05458 39  PHE A CB  
263  C CG  . PHE A 39  ? 0.40059 0.37523 0.62257 0.08120  0.12912  -0.05209 39  PHE A CG  
264  C CD1 . PHE A 39  ? 0.41254 0.37900 0.64602 0.09056  0.11604  -0.05140 39  PHE A CD1 
265  C CD2 . PHE A 39  ? 0.40084 0.39954 0.65026 0.07901  0.13651  -0.04903 39  PHE A CD2 
266  C CE1 . PHE A 39  ? 0.38859 0.37041 0.65058 0.09530  0.10644  -0.04606 39  PHE A CE1 
267  C CE2 . PHE A 39  ? 0.38995 0.40477 0.67816 0.08677  0.12989  -0.04621 39  PHE A CE2 
268  C CZ  . PHE A 39  ? 0.38771 0.39326 0.67884 0.09443  0.11341  -0.04417 39  PHE A CZ  
269  N N   . ASP A 40  ? 0.39539 0.36359 0.56001 0.04555  0.12525  -0.03020 40  ASP A N   
270  C CA  . ASP A 40  ? 0.38273 0.36374 0.56456 0.03712  0.12248  -0.02029 40  ASP A CA  
271  C C   . ASP A 40  ? 0.38068 0.34916 0.55696 0.03464  0.10215  -0.01296 40  ASP A C   
272  O O   . ASP A 40  ? 0.36656 0.34468 0.56606 0.03294  0.09444  -0.00842 40  ASP A O   
273  C CB  . ASP A 40  ? 0.40436 0.39089 0.57266 0.02429  0.13642  -0.01542 40  ASP A CB  
274  C CG  . ASP A 40  ? 0.43829 0.40516 0.56892 0.01387  0.13023  -0.00758 40  ASP A CG  
275  O OD1 . ASP A 40  ? 0.47208 0.42349 0.57460 0.01636  0.12848  -0.01235 40  ASP A OD1 
276  O OD2 . ASP A 40  ? 0.44343 0.41030 0.57451 0.00304  0.12640  0.00363  40  ASP A OD2 
277  N N   . VAL A 41  ? 0.42055 0.36937 0.56860 0.03480  0.09387  -0.01326 41  VAL A N   
278  C CA  . VAL A 41  ? 0.40757 0.34619 0.55267 0.03410  0.07589  -0.00854 41  VAL A CA  
279  C C   . VAL A 41  ? 0.39728 0.34118 0.56233 0.04363  0.06638  -0.01222 41  VAL A C   
280  O O   . VAL A 41  ? 0.37859 0.32538 0.55572 0.04289  0.05478  -0.00936 41  VAL A O   
281  C CB  . VAL A 41  ? 0.40239 0.32165 0.51504 0.03174  0.06994  -0.00780 41  VAL A CB  
282  C CG1 . VAL A 41  ? 0.38844 0.29938 0.50161 0.03397  0.05262  -0.00599 41  VAL A CG1 
283  C CG2 . VAL A 41  ? 0.41631 0.33013 0.50892 0.02046  0.07516  -0.00041 41  VAL A CG2 
284  N N   . VAL A 42  ? 0.37346 0.31824 0.54192 0.05226  0.07102  -0.01859 42  VAL A N   
285  C CA  . VAL A 42  ? 0.35571 0.30432 0.54063 0.06068  0.06168  -0.01988 42  VAL A CA  
286  C C   . VAL A 42  ? 0.32816 0.29619 0.54480 0.06208  0.06013  -0.01741 42  VAL A C   
287  O O   . VAL A 42  ? 0.31819 0.29061 0.54466 0.06330  0.04744  -0.01496 42  VAL A O   
288  C CB  . VAL A 42  ? 0.36292 0.30498 0.54530 0.06900  0.06677  -0.02607 42  VAL A CB  
289  C CG1 . VAL A 42  ? 0.35646 0.30258 0.55683 0.07680  0.05672  -0.02447 42  VAL A CG1 
290  C CG2 . VAL A 42  ? 0.36582 0.28895 0.51752 0.06659  0.06562  -0.02895 42  VAL A CG2 
291  N N   . GLU A 43  ? 0.33208 0.31375 0.56542 0.06143  0.07297  -0.01852 43  GLU A N   
292  C CA  . GLU A 43  ? 0.31922 0.32197 0.58738 0.06385  0.07103  -0.01671 43  GLU A CA  
293  C C   . GLU A 43  ? 0.28761 0.29644 0.56326 0.05485  0.06114  -0.01122 43  GLU A C   
294  O O   . GLU A 43  ? 0.27430 0.29462 0.57060 0.05680  0.05025  -0.00972 43  GLU A O   
295  C CB  . GLU A 43  ? 0.35295 0.37153 0.64033 0.06556  0.08883  -0.02034 43  GLU A CB  
296  C CG  . GLU A 43  ? 0.37034 0.40587 0.69370 0.07678  0.08804  -0.02245 43  GLU A CG  
297  C CD  . GLU A 43  ? 0.38515 0.44044 0.73313 0.07893  0.10688  -0.02739 43  GLU A CD  
298  O OE1 . GLU A 43  ? 0.37093 0.42996 0.70849 0.06926  0.12046  -0.02767 43  GLU A OE1 
299  O OE2 . GLU A 43  ? 0.39544 0.46161 0.76775 0.08864  0.10648  -0.03014 43  GLU A OE2 
300  N N   . SER A 44  ? 0.29938 0.29947 0.55828 0.04467  0.06342  -0.00811 44  SER A N   
301  C CA  . SER A 44  ? 0.28075 0.28315 0.54833 0.03621  0.05322  -0.00384 44  SER A CA  
302  C C   . SER A 44  ? 0.28094 0.27128 0.53682 0.03840  0.03646  -0.00528 44  SER A C   
303  O O   . SER A 44  ? 0.26312 0.25955 0.53277 0.03567  0.02540  -0.00540 44  SER A O   
304  C CB  . SER A 44  ? 0.29974 0.29498 0.55537 0.02424  0.06018  0.00165  44  SER A CB  
305  O OG  . SER A 44  ? 0.34116 0.31630 0.56410 0.02382  0.06125  0.00216  44  SER A OG  
306  N N   . PHE A 45  ? 0.29197 0.26735 0.52413 0.04322  0.03470  -0.00749 45  PHE A N   
307  C CA  . PHE A 45  ? 0.28998 0.25796 0.51312 0.04601  0.02069  -0.00989 45  PHE A CA  
308  C C   . PHE A 45  ? 0.28691 0.26908 0.52772 0.05133  0.01340  -0.01123 45  PHE A C   
309  O O   . PHE A 45  ? 0.29635 0.28223 0.54177 0.04937  0.00218  -0.01283 45  PHE A O   
310  C CB  . PHE A 45  ? 0.29431 0.24727 0.49259 0.04982  0.02157  -0.01161 45  PHE A CB  
311  C CG  . PHE A 45  ? 0.29874 0.24390 0.48524 0.05115  0.01002  -0.01417 45  PHE A CG  
312  C CD1 . PHE A 45  ? 0.28165 0.23179 0.47704 0.04946  -0.00021 -0.01638 45  PHE A CD1 
313  C CD2 . PHE A 45  ? 0.29483 0.22891 0.46217 0.05373  0.00992  -0.01554 45  PHE A CD2 
314  C CE1 . PHE A 45  ? 0.28613 0.23149 0.47154 0.05117  -0.00859 -0.02062 45  PHE A CE1 
315  C CE2 . PHE A 45  ? 0.26878 0.19930 0.42855 0.05491  0.00094  -0.01839 45  PHE A CE2 
316  C CZ  . PHE A 45  ? 0.28251 0.21919 0.45131 0.05403  -0.00748 -0.02128 45  PHE A CZ  
317  N N   . ASN A 46  ? 0.28528 0.27513 0.53627 0.05798  0.01945  -0.01076 46  ASN A N   
318  C CA  . ASN A 46  ? 0.27276 0.27619 0.54184 0.06343  0.01105  -0.00967 46  ASN A CA  
319  C C   . ASN A 46  ? 0.25515 0.27619 0.54929 0.05855  0.00562  -0.00853 46  ASN A C   
320  O O   . ASN A 46  ? 0.24467 0.27432 0.54576 0.05886  -0.00734 -0.00832 46  ASN A O   
321  C CB  . ASN A 46  ? 0.27234 0.27891 0.55195 0.07229  0.01870  -0.00906 46  ASN A CB  
322  C CG  . ASN A 46  ? 0.29372 0.28463 0.55309 0.07755  0.01753  -0.00961 46  ASN A CG  
323  O OD1 . ASN A 46  ? 0.30571 0.29165 0.55149 0.07666  0.00733  -0.00850 46  ASN A OD1 
324  N ND2 . ASN A 46  ? 0.31461 0.29842 0.56937 0.08145  0.02817  -0.01196 46  ASN A ND2 
325  N N   . ARG A 47  ? 0.25512 0.28276 0.56266 0.05302  0.01532  -0.00762 47  ARG A N   
326  C CA  . ARG A 47  ? 0.24828 0.29227 0.58093 0.04603  0.01028  -0.00643 47  ARG A CA  
327  C C   . ARG A 47  ? 0.24032 0.27655 0.56316 0.03916  -0.00338 -0.00888 47  ARG A C   
328  O O   . ARG A 47  ? 0.22601 0.27388 0.56258 0.03742  -0.01579 -0.01037 47  ARG A O   
329  C CB  . ARG A 47  ? 0.26099 0.31070 0.60470 0.03891  0.02502  -0.00418 47  ARG A CB  
330  C CG  . ARG A 47  ? 0.25328 0.32398 0.62962 0.03136  0.02290  -0.00217 47  ARG A CG  
331  C CD  . ARG A 47  ? 0.26412 0.35054 0.65964 0.03101  0.04111  -0.00048 47  ARG A CD  
332  N NE  . ARG A 47  ? 0.26536 0.33586 0.63441 0.02710  0.05544  0.00050  47  ARG A NE  
333  C CZ  . ARG A 47  ? 0.28253 0.35648 0.64867 0.03160  0.07268  -0.00142 47  ARG A CZ  
334  N NH1 . ARG A 47  ? 0.30965 0.40101 0.70015 0.04180  0.07852  -0.00504 47  ARG A NH1 
335  N NH2 . ARG A 47  ? 0.29032 0.34966 0.62853 0.02589  0.08376  -0.00007 47  ARG A NH2 
336  N N   . GLU A 48  ? 0.25304 0.26964 0.55265 0.03546  -0.00182 -0.01005 48  GLU A N   
337  C CA  . GLU A 48  ? 0.25093 0.25803 0.54231 0.03063  -0.01392 -0.01439 48  GLU A CA  
338  C C   . GLU A 48  ? 0.26969 0.27940 0.55224 0.03654  -0.02543 -0.01932 48  GLU A C   
339  O O   . GLU A 48  ? 0.28058 0.29499 0.56799 0.03301  -0.03705 -0.02441 48  GLU A O   
340  C CB  . GLU A 48  ? 0.23687 0.22234 0.50682 0.02797  -0.01028 -0.01390 48  GLU A CB  
341  C CG  . GLU A 48  ? 0.24614 0.22848 0.52188 0.01941  -0.00074 -0.00746 48  GLU A CG  
342  C CD  . GLU A 48  ? 0.25221 0.21558 0.50368 0.01874  0.00534  -0.00393 48  GLU A CD  
343  O OE1 . GLU A 48  ? 0.25990 0.21161 0.49343 0.02435  -0.00016 -0.00759 48  GLU A OE1 
344  O OE2 . GLU A 48  ? 0.24897 0.21057 0.49921 0.01200  0.01550  0.00283  48  GLU A OE2 
345  N N   . LEU A 49  ? 0.25459 0.26138 0.52333 0.04456  -0.02230 -0.01803 49  LEU A N   
346  C CA  . LEU A 49  ? 0.26975 0.28077 0.52930 0.04894  -0.03202 -0.02032 49  LEU A CA  
347  C C   . LEU A 49  ? 0.27616 0.30672 0.55529 0.04930  -0.04079 -0.01820 49  LEU A C   
348  O O   . LEU A 49  ? 0.27803 0.31489 0.55192 0.04791  -0.05264 -0.02160 49  LEU A O   
349  C CB  . LEU A 49  ? 0.27745 0.28083 0.52149 0.05598  -0.02624 -0.01731 49  LEU A CB  
350  C CG  . LEU A 49  ? 0.28579 0.27155 0.51043 0.05527  -0.01986 -0.01946 49  LEU A CG  
351  C CD1 . LEU A 49  ? 0.28629 0.26510 0.50109 0.06079  -0.01232 -0.01624 49  LEU A CD1 
352  C CD2 . LEU A 49  ? 0.26212 0.24313 0.47259 0.05390  -0.02763 -0.02573 49  LEU A CD2 
353  N N   . ASP A 50  ? 0.26447 0.30614 0.56643 0.05125  -0.03519 -0.01293 50  ASP A N   
354  C CA  . ASP A 50  ? 0.25050 0.31294 0.57674 0.05158  -0.04466 -0.01015 50  ASP A CA  
355  C C   . ASP A 50  ? 0.25290 0.32250 0.58741 0.04206  -0.05540 -0.01541 50  ASP A C   
356  O O   . ASP A 50  ? 0.27012 0.35144 0.60749 0.04079  -0.06962 -0.01661 50  ASP A O   
357  C CB  . ASP A 50  ? 0.23232 0.30704 0.58704 0.05507  -0.03467 -0.00536 50  ASP A CB  
358  C CG  . ASP A 50  ? 0.23259 0.30184 0.58418 0.06584  -0.02649 -0.00162 50  ASP A CG  
359  O OD1 . ASP A 50  ? 0.22842 0.28758 0.55980 0.07030  -0.03168 -0.00019 50  ASP A OD1 
360  O OD2 . ASP A 50  ? 0.20593 0.28153 0.57667 0.06937  -0.01433 -0.00065 50  ASP A OD2 
361  N N   . VAL A 51  ? 0.24623 0.30813 0.58428 0.03453  -0.04943 -0.01826 51  VAL A N   
362  C CA  . VAL A 51  ? 0.24384 0.30778 0.58993 0.02459  -0.05955 -0.02428 51  VAL A CA  
363  C C   . VAL A 51  ? 0.28008 0.33716 0.60352 0.02461  -0.07155 -0.03291 51  VAL A C   
364  O O   . VAL A 51  ? 0.31115 0.37748 0.64051 0.01933  -0.08474 -0.03876 51  VAL A O   
365  C CB  . VAL A 51  ? 0.24206 0.29232 0.59050 0.01673  -0.05081 -0.02425 51  VAL A CB  
366  C CG1 . VAL A 51  ? 0.27140 0.31785 0.62624 0.00658  -0.06238 -0.03161 51  VAL A CG1 
367  C CG2 . VAL A 51  ? 0.23061 0.29292 0.60266 0.01452  -0.03844 -0.01643 51  VAL A CG2 
368  N N   . GLN A 52  ? 0.29163 0.33405 0.58899 0.03019  -0.06692 -0.03463 52  GLN A N   
369  C CA  . GLN A 52  ? 0.30508 0.34344 0.58069 0.03068  -0.07548 -0.04363 52  GLN A CA  
370  C C   . GLN A 52  ? 0.32592 0.37861 0.59361 0.03473  -0.08323 -0.04052 52  GLN A C   
371  O O   . GLN A 52  ? 0.34750 0.40600 0.60346 0.03189  -0.09381 -0.04803 52  GLN A O   
372  C CB  . GLN A 52  ? 0.29967 0.31965 0.55404 0.03457  -0.06741 -0.04628 52  GLN A CB  
373  C CG  . GLN A 52  ? 0.28848 0.29209 0.54713 0.03022  -0.06330 -0.04917 52  GLN A CG  
374  C CD  . GLN A 52  ? 0.28779 0.28882 0.55186 0.02383  -0.07364 -0.06043 52  GLN A CD  
375  O OE1 . GLN A 52  ? 0.30719 0.31166 0.55934 0.02491  -0.08105 -0.07062 52  GLN A OE1 
376  N NE2 . GLN A 52  ? 0.30383 0.29896 0.58567 0.01634  -0.07401 -0.05917 52  GLN A NE2 
377  N N   . MET A 53  ? 0.31321 0.37078 0.58603 0.04113  -0.07828 -0.02965 53  MET A N   
378  C CA  . MET A 53  ? 0.32348 0.39312 0.59089 0.04471  -0.08716 -0.02359 53  MET A CA  
379  C C   . MET A 53  ? 0.34717 0.43625 0.63253 0.04030  -0.10157 -0.02311 53  MET A C   
380  O O   . MET A 53  ? 0.37838 0.47768 0.65288 0.03991  -0.11369 -0.02100 53  MET A O   
381  C CB  . MET A 53  ? 0.30139 0.36910 0.57508 0.05309  -0.07929 -0.01229 53  MET A CB  
382  C CG  . MET A 53  ? 0.29953 0.35054 0.55012 0.05691  -0.06973 -0.01195 53  MET A CG  
383  S SD  . MET A 53  ? 0.33841 0.39089 0.55843 0.05480  -0.07833 -0.01422 53  MET A SD  
384  C CE  . MET A 53  ? 0.30720 0.36971 0.53192 0.05935  -0.08716 0.00073  53  MET A CE  
385  N N   . ALA A 54  ? 0.32306 0.41840 0.63540 0.03590  -0.10102 -0.02439 54  ALA A N   
386  C CA  . ALA A 54  ? 0.33585 0.45160 0.66955 0.03090  -0.11552 -0.02394 54  ALA A CA  
387  C C   . ALA A 54  ? 0.36983 0.48733 0.68703 0.02270  -0.12931 -0.03569 54  ALA A C   
388  O O   . ALA A 54  ? 0.38461 0.51964 0.70978 0.01875  -0.14496 -0.03532 54  ALA A O   
389  C CB  . ALA A 54  ? 0.31116 0.43413 0.67940 0.02648  -0.11005 -0.02290 54  ALA A CB  
390  N N   . ILE A 55  ? 0.42660 0.52692 0.72187 0.02033  -0.12439 -0.04682 55  ILE A N   
391  C CA  . ILE A 55  ? 0.45460 0.55454 0.73546 0.01295  -0.13542 -0.06173 55  ILE A CA  
392  C C   . ILE A 55  ? 0.48754 0.59656 0.74027 0.01463  -0.14404 -0.06207 55  ILE A C   
393  O O   . ILE A 55  ? 0.49809 0.59968 0.72914 0.02054  -0.13570 -0.05882 55  ILE A O   
394  C CB  . ILE A 55  ? 0.47158 0.54968 0.74118 0.01170  -0.12689 -0.07397 55  ILE A CB  
395  C CG1 . ILE A 55  ? 0.40867 0.47449 0.69889 0.01138  -0.11512 -0.06836 55  ILE A CG1 
396  C CG2 . ILE A 55  ? 0.49512 0.57200 0.76138 0.00329  -0.13837 -0.09136 55  ILE A CG2 
397  C CD1 . ILE A 55  ? 0.40866 0.47712 0.72574 0.00145  -0.12099 -0.07149 55  ILE A CD1 
398  N N   . PRO A 56  ? 0.49327 0.61876 0.74429 0.00859  -0.16077 -0.06526 56  PRO A N   
399  C CA  . PRO A 56  ? 0.53518 0.66847 0.75294 0.00777  -0.16878 -0.06737 56  PRO A CA  
400  C C   . PRO A 56  ? 0.56901 0.68859 0.75908 0.00755  -0.15991 -0.08321 56  PRO A C   
401  O O   . PRO A 56  ? 0.57129 0.67992 0.76708 0.00404  -0.15787 -0.09880 56  PRO A O   
402  C CB  . PRO A 56  ? 0.50587 0.65712 0.72799 -0.00127 -0.18903 -0.07278 56  PRO A CB  
403  C CG  . PRO A 56  ? 0.47509 0.62456 0.73206 -0.00622 -0.19024 -0.07794 56  PRO A CG  
404  C CD  . PRO A 56  ? 0.45655 0.59564 0.73545 0.00103  -0.17362 -0.06684 56  PRO A CD  
405  N N   . PRO A 57  ? 0.59796 0.71750 0.76057 0.01140  -0.15413 -0.07930 57  PRO A N   
406  C CA  . PRO A 57  ? 0.63530 0.74080 0.78115 0.01459  -0.14010 -0.09033 57  PRO A CA  
407  C C   . PRO A 57  ? 0.68571 0.79343 0.80975 0.00946  -0.14320 -0.11266 57  PRO A C   
408  O O   . PRO A 57  ? 0.66369 0.75749 0.79428 0.01041  -0.13710 -0.12790 57  PRO A O   
409  C CB  . PRO A 57  ? 0.59900 0.70627 0.72731 0.01962  -0.13283 -0.07574 57  PRO A CB  
410  C CG  . PRO A 57  ? 0.58028 0.69737 0.72125 0.02089  -0.14180 -0.05572 57  PRO A CG  
411  C CD  . PRO A 57  ? 0.59487 0.72453 0.74914 0.01464  -0.15776 -0.06011 57  PRO A CD  
412  N N   . PRO A 58  ? 0.76096 0.88527 0.85772 0.00420  -0.15209 -0.11585 58  PRO A N   
413  C CA  . PRO A 58  ? 0.75737 0.88351 0.83135 0.00037  -0.15117 -0.13991 58  PRO A CA  
414  C C   . PRO A 58  ? 0.88646 1.02556 0.94931 -0.00924 -0.16784 -0.15329 58  PRO A C   
415  O O   . PRO A 58  ? 0.89991 1.05626 0.94722 -0.01437 -0.17988 -0.14294 58  PRO A O   
416  C CB  . PRO A 58  ? 0.76530 0.90024 0.80858 0.00194  -0.14220 -0.13448 58  PRO A CB  
417  C CG  . PRO A 58  ? 0.77142 0.91594 0.81399 0.00144  -0.15006 -0.10745 58  PRO A CG  
418  C CD  . PRO A 58  ? 0.76618 0.90599 0.84460 0.00279  -0.15873 -0.09838 58  PRO A CD  
419  N N   . LYS A 59  ? 1.09306 1.09941 1.10067 -0.16463 -0.11508 0.01655  59  LYS A N   
420  C CA  . LYS A 59  ? 1.13929 1.11035 1.09665 -0.18124 -0.12765 0.01264  59  LYS A CA  
421  C C   . LYS A 59  ? 1.16657 1.07131 1.08244 -0.15663 -0.11742 0.00761  59  LYS A C   
422  O O   . LYS A 59  ? 1.24698 1.10110 1.10581 -0.16688 -0.12453 0.00299  59  LYS A O   
423  C CB  . LYS A 59  ? 1.20309 1.14689 1.11987 -0.22384 -0.13861 0.00877  59  LYS A CB  
424  C CG  . LYS A 59  ? 1.19035 1.20961 1.14635 -0.24943 -0.14845 0.01677  59  LYS A CG  
425  C CD  . LYS A 59  ? 1.13476 1.20508 1.09962 -0.25644 -0.16324 0.02282  59  LYS A CD  
426  C CE  . LYS A 59  ? 1.10388 1.24517 1.10159 -0.26975 -0.16423 0.03277  59  LYS A CE  
427  N NZ  . LYS A 59  ? 1.09359 1.27526 1.08694 -0.28265 -0.17881 0.03870  59  LYS A NZ  
428  N N   . GLY A 60  ? 0.91577 0.82107 0.85653 -0.12501 -0.10093 0.00955  60  GLY A N   
429  C CA  . GLY A 60  ? 0.80644 0.66296 0.71457 -0.09966 -0.08945 0.00838  60  GLY A CA  
430  C C   . GLY A 60  ? 0.66002 0.53275 0.60330 -0.07069 -0.07306 0.01294  60  GLY A C   
431  O O   . GLY A 60  ? 0.63535 0.55432 0.62518 -0.06182 -0.07190 0.01763  60  GLY A O   
432  N N   . GLU A 61  ? 0.55312 0.38633 0.46920 -0.05605 -0.06027 0.01247  61  GLU A N   
433  C CA  . GLU A 61  ? 0.49523 0.34438 0.43710 -0.03042 -0.04571 0.01850  61  GLU A CA  
434  C C   . GLU A 61  ? 0.44345 0.32792 0.43088 -0.03369 -0.04185 0.01922  61  GLU A C   
435  O O   . GLU A 61  ? 0.44906 0.32394 0.43064 -0.04648 -0.04267 0.01522  61  GLU A O   
436  C CB  . GLU A 61  ? 0.50563 0.30811 0.40040 -0.01084 -0.03315 0.02034  61  GLU A CB  
437  C CG  . GLU A 61  ? 0.46610 0.29339 0.38624 0.01278  -0.01876 0.02884  61  GLU A CG  
438  C CD  . GLU A 61  ? 0.51440 0.30375 0.38538 0.03832  -0.00551 0.03422  61  GLU A CD  
439  O OE1 . GLU A 61  ? 0.55790 0.29633 0.37771 0.03837  -0.00329 0.02977  61  GLU A OE1 
440  O OE2 . GLU A 61  ? 0.52303 0.33185 0.40235 0.05922  0.00360  0.04408  61  GLU A OE2 
441  N N   . ARG A 62  ? 0.40276 0.32315 0.43048 -0.02292 -0.03735 0.02447  62  ARG A N   
442  C CA  . ARG A 62  ? 0.36468 0.31307 0.43004 -0.02374 -0.03307 0.02550  62  ARG A CA  
443  C C   . ARG A 62  ? 0.34531 0.30066 0.41866 -0.00719 -0.02209 0.03218  62  ARG A C   
444  O O   . ARG A 62  ? 0.34272 0.31428 0.43198 -0.00278 -0.02133 0.03693  62  ARG A O   
445  C CB  . ARG A 62  ? 0.35464 0.33601 0.45205 -0.03078 -0.04015 0.02607  62  ARG A CB  
446  C CG  . ARG A 62  ? 0.40548 0.39538 0.49782 -0.04681 -0.05208 0.02339  62  ARG A CG  
447  C CD  . ARG A 62  ? 0.43372 0.46125 0.55530 -0.04262 -0.05585 0.02792  62  ARG A CD  
448  N NE  . ARG A 62  ? 0.42932 0.47394 0.57760 -0.03843 -0.04974 0.02940  62  ARG A NE  
449  C CZ  . ARG A 62  ? 0.42405 0.49213 0.59134 -0.02907 -0.04884 0.03406  62  ARG A CZ  
450  N NH1 . ARG A 62  ? 0.43046 0.50440 0.59462 -0.01866 -0.05073 0.03826  62  ARG A NH1 
451  N NH2 . ARG A 62  ? 0.37246 0.45324 0.55633 -0.02743 -0.04485 0.03498  62  ARG A NH2 
452  N N   . LEU A 63  ? 0.34886 0.29560 0.41125 0.00086  -0.01378 0.03380  63  LEU A N   
453  C CA  . LEU A 63  ? 0.34850 0.30941 0.41397 0.01682  -0.00366 0.04314  63  LEU A CA  
454  C C   . LEU A 63  ? 0.31208 0.30788 0.41561 0.01104  -0.00377 0.04781  63  LEU A C   
455  O O   . LEU A 63  ? 0.30715 0.31536 0.41510 0.01573  -0.00036 0.05557  63  LEU A O   
456  C CB  . LEU A 63  ? 0.32684 0.28121 0.37689 0.02782  0.00484  0.04520  63  LEU A CB  
457  C CG  . LEU A 63  ? 0.36864 0.27475 0.36552 0.03757  0.00848  0.04230  63  LEU A CG  
458  C CD1 . LEU A 63  ? 0.36377 0.26390 0.34424 0.05255  0.01868  0.04564  63  LEU A CD1 
459  C CD2 . LEU A 63  ? 0.39545 0.28362 0.36110 0.05380  0.01295  0.04806  63  LEU A CD2 
460  N N   . LEU A 64  ? 0.28935 0.29654 0.41508 0.00020  -0.00703 0.04369  64  LEU A N   
461  C CA  . LEU A 64  ? 0.27857 0.30580 0.42834 -0.00717 -0.00733 0.04720  64  LEU A CA  
462  C C   . LEU A 64  ? 0.29124 0.31247 0.44495 -0.01142 -0.01233 0.04568  64  LEU A C   
463  O O   . LEU A 64  ? 0.28953 0.31401 0.44569 -0.01283 -0.01037 0.05139  64  LEU A O   
464  C CB  . LEU A 64  ? 0.24673 0.28130 0.41029 -0.01434 -0.00824 0.04346  64  LEU A CB  
465  C CG  . LEU A 64  ? 0.23834 0.28227 0.41621 -0.02478 -0.00946 0.04557  64  LEU A CG  
466  C CD1 . LEU A 64  ? 0.24442 0.30150 0.42958 -0.02896 -0.00848 0.04571  64  LEU A CD1 
467  C CD2 . LEU A 64  ? 0.24094 0.27052 0.42055 -0.02810 -0.01363 0.04043  64  LEU A CD2 
468  N N   . ALA A 65  ? 0.29452 0.30892 0.44687 -0.01345 -0.01837 0.03944  65  ALA A N   
469  C CA  . ALA A 65  ? 0.28459 0.30030 0.44113 -0.01293 -0.02245 0.03964  65  ALA A CA  
470  C C   . ALA A 65  ? 0.28314 0.29285 0.42734 -0.00641 -0.02243 0.04391  65  ALA A C   
471  O O   . ALA A 65  ? 0.27942 0.28659 0.42340 -0.00302 -0.02163 0.04738  65  ALA A O   
472  C CB  . ALA A 65  ? 0.30847 0.33178 0.46881 -0.01634 -0.02907 0.03510  65  ALA A CB  
473  N N   . ASP A 66  ? 0.28991 0.29148 0.41758 -0.00269 -0.02230 0.04407  66  ASP A N   
474  C CA  . ASP A 66  ? 0.30654 0.30061 0.41951 0.00551  -0.02086 0.04894  66  ASP A CA  
475  C C   . ASP A 66  ? 0.30915 0.30886 0.42727 0.00780  -0.01212 0.05776  66  ASP A C   
476  O O   . ASP A 66  ? 0.32701 0.32170 0.43615 0.01340  -0.00982 0.06315  66  ASP A O   
477  C CB  . ASP A 66  ? 0.33946 0.31594 0.42485 0.01106  -0.02117 0.04755  66  ASP A CB  
478  C CG  . ASP A 66  ? 0.35410 0.32042 0.42618 0.00209  -0.03169 0.03951  66  ASP A CG  
479  O OD1 . ASP A 66  ? 0.35619 0.33941 0.44438 -0.00512 -0.03913 0.03742  66  ASP A OD1 
480  O OD2 . ASP A 66  ? 0.39165 0.33247 0.43314 0.00210  -0.03213 0.03646  66  ASP A OD2 
481  N N   . LYS A 67  ? 0.29272 0.30481 0.42402 0.00165  -0.00768 0.06025  67  LYS A N   
482  C CA  . LYS A 67  ? 0.28078 0.30674 0.41730 -0.00191 -0.00057 0.07055  67  LYS A CA  
483  C C   . LYS A 67  ? 0.28319 0.30287 0.42443 -0.01471 -0.00104 0.07234  67  LYS A C   
484  O O   . LYS A 67  ? 0.26571 0.29442 0.40780 -0.02405 0.00370  0.08158  67  LYS A O   
485  C CB  . LYS A 67  ? 0.26413 0.31273 0.40987 -0.00322 0.00350  0.07430  67  LYS A CB  
486  C CG  . LYS A 67  ? 0.28178 0.34688 0.41860 0.01063  0.01197  0.08509  67  LYS A CG  
487  C CD  . LYS A 67  ? 0.31521 0.35390 0.42500 0.02780  0.01223  0.08081  67  LYS A CD  
488  C CE  . LYS A 67  ? 0.35585 0.40458 0.44770 0.04819  0.02323  0.09279  67  LYS A CE  
489  N NZ  . LYS A 67  ? 0.39797 0.40782 0.45062 0.06489  0.02359  0.08766  67  LYS A NZ  
490  N N   . TYR A 68  ? 0.28543 0.28876 0.42533 -0.01542 -0.00589 0.06512  68  TYR A N   
491  C CA  . TYR A 68  ? 0.30657 0.29111 0.43875 -0.02416 -0.00488 0.06639  68  TYR A CA  
492  C C   . TYR A 68  ? 0.32290 0.28716 0.44106 -0.01144 -0.00632 0.06439  68  TYR A C   
493  O O   . TYR A 68  ? 0.29652 0.27040 0.41948 -0.00040 -0.01107 0.06004  68  TYR A O   
494  C CB  . TYR A 68  ? 0.29558 0.27920 0.43437 -0.03372 -0.00708 0.06145  68  TYR A CB  
495  C CG  . TYR A 68  ? 0.26980 0.27696 0.42076 -0.04694 -0.00613 0.06511  68  TYR A CG  
496  C CD1 . TYR A 68  ? 0.26169 0.29269 0.42585 -0.03962 -0.00624 0.06357  68  TYR A CD1 
497  C CD2 . TYR A 68  ? 0.27205 0.27643 0.41665 -0.06686 -0.00530 0.07092  68  TYR A CD2 
498  C CE1 . TYR A 68  ? 0.24666 0.30448 0.42068 -0.04670 -0.00454 0.06888  68  TYR A CE1 
499  C CE2 . TYR A 68  ? 0.25868 0.29613 0.41712 -0.07880 -0.00568 0.07618  68  TYR A CE2 
500  C CZ  . TYR A 68  ? 0.25688 0.32466 0.43177 -0.06628 -0.00481 0.07581  68  TYR A CZ  
501  O OH  . TYR A 68  ? 0.28360 0.38881 0.47081 -0.07313 -0.00429 0.08284  68  TYR A OH  
502  N N   . PRO A 69  ? 0.34643 0.28266 0.44359 -0.01319 -0.00226 0.06858  69  PRO A N   
503  C CA  . PRO A 69  ? 0.35905 0.27694 0.43806 0.00458  -0.00171 0.06921  69  PRO A CA  
504  C C   . PRO A 69  ? 0.35838 0.28347 0.44289 0.01674  -0.00548 0.06408  69  PRO A C   
505  O O   . PRO A 69  ? 0.35168 0.28420 0.44837 0.00939  -0.00716 0.05964  69  PRO A O   
506  C CB  . PRO A 69  ? 0.39443 0.26975 0.44105 -0.00207 0.00531  0.07474  69  PRO A CB  
507  C CG  . PRO A 69  ? 0.40455 0.27723 0.45460 -0.02648 0.00536  0.07439  69  PRO A CG  
508  C CD  . PRO A 69  ? 0.34874 0.26686 0.43261 -0.03276 0.00199  0.07392  69  PRO A CD  
509  N N   . PRO A 70  ? 0.36476 0.29296 0.44111 0.03627  -0.00659 0.06603  70  PRO A N   
510  C CA  . PRO A 70  ? 0.34598 0.29383 0.43067 0.04940  -0.00960 0.06458  70  PRO A CA  
511  C C   . PRO A 70  ? 0.39785 0.31473 0.45950 0.05844  -0.00250 0.06629  70  PRO A C   
512  O O   . PRO A 70  ? 0.43983 0.35296 0.48401 0.08244  0.00109  0.07159  70  PRO A O   
513  C CB  . PRO A 70  ? 0.33945 0.30637 0.42025 0.06795  -0.01302 0.06915  70  PRO A CB  
514  C CG  . PRO A 70  ? 0.34979 0.28219 0.40384 0.07151  -0.00690 0.07369  70  PRO A CG  
515  C CD  . PRO A 70  ? 0.36263 0.28470 0.42374 0.04825  -0.00545 0.07115  70  PRO A CD  
516  N N   . HIS A 71  ? 0.41244 0.30652 0.46949 0.04158  -0.00022 0.06274  71  HIS A N   
517  C CA  . HIS A 71  ? 0.45766 0.30718 0.48023 0.04747  0.00661  0.06367  71  HIS A CA  
518  C C   . HIS A 71  ? 0.45438 0.31661 0.49037 0.04695  0.00530  0.05935  71  HIS A C   
519  O O   . HIS A 71  ? 0.50692 0.32766 0.51146 0.04877  0.01039  0.05884  71  HIS A O   
520  C CB  . HIS A 71  ? 0.50164 0.30358 0.49509 0.02489  0.00994  0.06405  71  HIS A CB  
521  C CG  . HIS A 71  ? 0.51759 0.29485 0.48680 0.02687  0.01424  0.07003  71  HIS A CG  
522  N ND1 . HIS A 71  ? 0.49339 0.24695 0.44833 0.00090  0.01581  0.07266  71  HIS A ND1 
523  C CD2 . HIS A 71  ? 0.52270 0.29877 0.47940 0.05151  0.01742  0.07507  71  HIS A CD2 
524  C CE1 . HIS A 71  ? 0.52127 0.25549 0.45478 0.00942  0.02074  0.07864  71  HIS A CE1 
525  N NE2 . HIS A 71  ? 0.53457 0.28002 0.46748 0.04138  0.02171  0.07972  71  HIS A NE2 
526  N N   . PHE A 72  ? 0.39222 0.30457 0.46813 0.04367  -0.00104 0.05629  72  PHE A N   
527  C CA  . PHE A 72  ? 0.38290 0.30993 0.47283 0.04316  -0.00161 0.05295  72  PHE A CA  
528  C C   . PHE A 72  ? 0.33925 0.31994 0.46681 0.04060  -0.00838 0.05173  72  PHE A C   
529  O O   . PHE A 72  ? 0.32279 0.32130 0.46188 0.03482  -0.01346 0.05158  72  PHE A O   
530  C CB  . PHE A 72  ? 0.40331 0.30990 0.49105 0.02074  -0.00247 0.04722  72  PHE A CB  
531  C CG  . PHE A 72  ? 0.38159 0.29625 0.48188 -0.00036 -0.00632 0.04602  72  PHE A CG  
532  C CD1 . PHE A 72  ? 0.35598 0.30837 0.48698 -0.00655 -0.01094 0.04366  72  PHE A CD1 
533  C CD2 . PHE A 72  ? 0.40643 0.28921 0.48291 -0.01342 -0.00428 0.04870  72  PHE A CD2 
534  C CE1 . PHE A 72  ? 0.32905 0.28990 0.46720 -0.01930 -0.01211 0.04488  72  PHE A CE1 
535  C CE2 . PHE A 72  ? 0.37638 0.27613 0.46648 -0.03040 -0.00640 0.05074  72  PHE A CE2 
536  C CZ  . PHE A 72  ? 0.35009 0.29037 0.47136 -0.03028 -0.00965 0.04927  72  PHE A CZ  
537  N N   . LYS A 73  ? 0.33112 0.33284 0.47235 0.04395  -0.00812 0.05124  73  LYS A N   
538  C CA  . LYS A 73  ? 0.30434 0.34876 0.47584 0.03393  -0.01437 0.04934  73  LYS A CA  
539  C C   . LYS A 73  ? 0.27220 0.30781 0.45175 0.01718  -0.01463 0.04226  73  LYS A C   
540  O O   . LYS A 73  ? 0.27134 0.28071 0.43805 0.01761  -0.01023 0.04035  73  LYS A O   
541  C CB  . LYS A 73  ? 0.29273 0.37571 0.47544 0.04864  -0.01331 0.05652  73  LYS A CB  
542  C CG  . LYS A 73  ? 0.31196 0.41839 0.48998 0.06839  -0.01371 0.06598  73  LYS A CG  
543  C CD  . LYS A 73  ? 0.32448 0.45949 0.51711 0.05432  -0.02437 0.06510  73  LYS A CD  
544  C CE  . LYS A 73  ? 0.33953 0.51484 0.55710 0.03410  -0.03197 0.06378  73  LYS A CE  
545  N NZ  . LYS A 73  ? 0.38866 0.56840 0.60791 0.01275  -0.04272 0.05882  73  LYS A NZ  
546  N N   . TYR A 74  ? 0.25375 0.30803 0.44904 0.00313  -0.01982 0.03866  74  TYR A N   
547  C CA  . TYR A 74  ? 0.22540 0.26930 0.42337 -0.00986 -0.01951 0.03289  74  TYR A CA  
548  C C   . TYR A 74  ? 0.21732 0.27978 0.42648 -0.01834 -0.02172 0.03068  74  TYR A C   
549  O O   . TYR A 74  ? 0.23435 0.31153 0.44570 -0.02484 -0.02696 0.03130  74  TYR A O   
550  C CB  . TYR A 74  ? 0.23604 0.26939 0.42795 -0.01628 -0.02097 0.03185  74  TYR A CB  
551  C CG  . TYR A 74  ? 0.22434 0.25403 0.41659 -0.02432 -0.01978 0.02871  74  TYR A CG  
552  C CD1 . TYR A 74  ? 0.22828 0.25095 0.41959 -0.02741 -0.01689 0.02841  74  TYR A CD1 
553  C CD2 . TYR A 74  ? 0.23287 0.26400 0.42051 -0.02768 -0.02154 0.02699  74  TYR A CD2 
554  C CE1 . TYR A 74  ? 0.20884 0.23592 0.40046 -0.03045 -0.01528 0.02782  74  TYR A CE1 
555  C CE2 . TYR A 74  ? 0.23777 0.26282 0.41908 -0.02851 -0.01816 0.02590  74  TYR A CE2 
556  C CZ  . TYR A 74  ? 0.22231 0.25015 0.40819 -0.02826 -0.01472 0.02704  74  TYR A CZ  
557  O OH  . TYR A 74  ? 0.24097 0.27034 0.42074 -0.02520 -0.01094 0.02804  74  TYR A OH  
558  N N   . VAL A 75  ? 0.21351 0.27143 0.42515 -0.02036 -0.01812 0.02814  75  VAL A N   
559  C CA  . VAL A 75  ? 0.22153 0.28732 0.43752 -0.03032 -0.01848 0.02576  75  VAL A CA  
560  C C   . VAL A 75  ? 0.21367 0.25904 0.42066 -0.03398 -0.01583 0.02109  75  VAL A C   
561  O O   . VAL A 75  ? 0.21000 0.24769 0.41662 -0.03001 -0.01245 0.01998  75  VAL A O   
562  C CB  . VAL A 75  ? 0.20280 0.28545 0.42852 -0.02645 -0.01488 0.02884  75  VAL A CB  
563  C CG1 . VAL A 75  ? 0.21228 0.29440 0.43760 -0.03893 -0.01380 0.02613  75  VAL A CG1 
564  C CG2 . VAL A 75  ? 0.19964 0.31635 0.43618 -0.02138 -0.01709 0.03669  75  VAL A CG2 
565  N N   . PRO A 76  ? 0.21130 0.24680 0.40664 -0.03976 -0.01700 0.01910  76  PRO A N   
566  C CA  . PRO A 76  ? 0.22536 0.24616 0.40931 -0.03660 -0.01277 0.01743  76  PRO A CA  
567  C C   . PRO A 76  ? 0.22895 0.24227 0.40735 -0.03843 -0.00865 0.01494  76  PRO A C   
568  O O   . PRO A 76  ? 0.23857 0.25459 0.41852 -0.04637 -0.00917 0.01432  76  PRO A O   
569  C CB  . PRO A 76  ? 0.24274 0.24994 0.40741 -0.03681 -0.01369 0.01764  76  PRO A CB  
570  C CG  . PRO A 76  ? 0.24706 0.25588 0.40885 -0.04810 -0.01950 0.01657  76  PRO A CG  
571  C CD  . PRO A 76  ? 0.22596 0.26136 0.41230 -0.04728 -0.02223 0.01931  76  PRO A CD  
572  N N   . ASN A 77  ? 0.22571 0.23333 0.39720 -0.03107 -0.00431 0.01495  77  ASN A N   
573  C CA  . ASN A 77  ? 0.22200 0.21890 0.38248 -0.02813 0.00106  0.01324  77  ASN A CA  
574  C C   . ASN A 77  ? 0.22211 0.22073 0.39030 -0.03487 0.00188  0.01149  77  ASN A C   
575  O O   . ASN A 77  ? 0.23564 0.22047 0.38999 -0.04250 0.00409  0.01043  77  ASN A O   
576  C CB  . ASN A 77  ? 0.23672 0.20721 0.36542 -0.02461 0.00553  0.01301  77  ASN A CB  
577  C CG  . ASN A 77  ? 0.25802 0.21316 0.37246 -0.03558 0.00143  0.01172  77  ASN A CG  
578  O OD1 . ASN A 77  ? 0.26794 0.21930 0.37368 -0.03110 -0.00008 0.01343  77  ASN A OD1 
579  N ND2 . ASN A 77  ? 0.27341 0.22109 0.38335 -0.05133 -0.00060 0.00959  77  ASN A ND2 
580  N N   . VAL A 78  ? 0.20445 0.21681 0.38969 -0.03226 0.00096  0.01206  78  VAL A N   
581  C CA  . VAL A 78  ? 0.20334 0.22278 0.39661 -0.03441 0.00329  0.01290  78  VAL A CA  
582  C C   . VAL A 78  ? 0.22670 0.23397 0.40914 -0.03360 0.00945  0.01134  78  VAL A C   
583  O O   . VAL A 78  ? 0.22467 0.23842 0.41170 -0.03765 0.01272  0.01335  78  VAL A O   
584  C CB  . VAL A 78  ? 0.19965 0.22701 0.40291 -0.02633 0.00282  0.01454  78  VAL A CB  
585  C CG1 . VAL A 78  ? 0.20271 0.24174 0.41368 -0.02563 -0.00108 0.01786  78  VAL A CG1 
586  C CG2 . VAL A 78  ? 0.20694 0.22294 0.40274 -0.02209 0.00166  0.01217  78  VAL A CG2 
587  N N   . ALA A 79  ? 0.23567 0.22869 0.40298 -0.02708 0.01198  0.00942  79  ALA A N   
588  C CA  . ALA A 79  ? 0.23029 0.20775 0.38189 -0.02356 0.01890  0.00841  79  ALA A CA  
589  C C   . ALA A 79  ? 0.25091 0.20907 0.38439 -0.03545 0.02248  0.00855  79  ALA A C   
590  O O   . ALA A 79  ? 0.26260 0.21062 0.38747 -0.03862 0.02840  0.00895  79  ALA A O   
591  C CB  . ALA A 79  ? 0.23181 0.20295 0.36822 -0.01038 0.02127  0.00848  79  ALA A CB  
592  N N   . THR A 80  ? 0.25828 0.20778 0.38149 -0.04427 0.01882  0.00844  80  THR A N   
593  C CA  . THR A 80  ? 0.28530 0.20764 0.38103 -0.06084 0.02067  0.00810  80  THR A CA  
594  C C   . THR A 80  ? 0.28346 0.23141 0.39902 -0.08207 0.01604  0.01139  80  THR A C   
595  O O   . THR A 80  ? 0.29200 0.22334 0.38769 -0.10142 0.01782  0.01249  80  THR A O   
596  C CB  . THR A 80  ? 0.29998 0.19303 0.36445 -0.06197 0.01870  0.00656  80  THR A CB  
597  O OG1 . THR A 80  ? 0.29139 0.20968 0.37767 -0.06868 0.00955  0.00742  80  THR A OG1 
598  C CG2 . THR A 80  ? 0.30701 0.18595 0.35362 -0.03687 0.02452  0.00689  80  THR A CG2 
599  N N   . THR A 81  ? 0.25835 0.24688 0.40920 -0.07898 0.01073  0.01443  81  THR A N   
600  C CA  . THR A 81  ? 0.23890 0.26355 0.41042 -0.09444 0.00687  0.02070  81  THR A CA  
601  C C   . THR A 81  ? 0.21996 0.27753 0.41814 -0.08336 0.01183  0.02637  81  THR A C   
602  O O   . THR A 81  ? 0.22071 0.31476 0.43550 -0.09383 0.01142  0.03456  81  THR A O   
603  C CB  . THR A 81  ? 0.23211 0.27905 0.41620 -0.09742 -0.00255 0.02243  81  THR A CB  
604  O OG1 . THR A 81  ? 0.22851 0.27883 0.42466 -0.07606 -0.00285 0.02073  81  THR A OG1 
605  C CG2 . THR A 81  ? 0.26935 0.28443 0.42237 -0.11258 -0.00790 0.01835  81  THR A CG2 
606  N N   . CYS A 82  ? 0.23165 0.27916 0.43171 -0.06272 0.01644  0.02346  82  CYS A N   
607  C CA  . CYS A 82  ? 0.21610 0.28492 0.43217 -0.04840 0.02154  0.02839  82  CYS A CA  
608  C C   . CYS A 82  ? 0.22553 0.27420 0.42936 -0.04251 0.02971  0.02636  82  CYS A C   
609  O O   . CYS A 82  ? 0.22973 0.25390 0.42131 -0.03136 0.03015  0.02019  82  CYS A O   
610  C CB  . CYS A 82  ? 0.20592 0.27417 0.42688 -0.03064 0.01878  0.02693  82  CYS A CB  
611  S SG  . CYS A 82  ? 0.20805 0.29827 0.44047 -0.03411 0.01063  0.03025  82  CYS A SG  
612  N N   . PRO A 83  ? 0.21949 0.28126 0.42606 -0.05039 0.03613  0.03249  83  PRO A N   
613  C CA  . PRO A 83  ? 0.22978 0.26954 0.42170 -0.04383 0.04488  0.03088  83  PRO A CA  
614  C C   . PRO A 83  ? 0.22976 0.26279 0.42107 -0.01972 0.04776  0.02879  83  PRO A C   
615  O O   . PRO A 83  ? 0.24402 0.25053 0.41802 -0.01217 0.05080  0.02361  83  PRO A O   
616  C CB  . PRO A 83  ? 0.22876 0.29477 0.42912 -0.05831 0.05121  0.04100  83  PRO A CB  
617  C CG  . PRO A 83  ? 0.23484 0.32054 0.44173 -0.08317 0.04320  0.04429  83  PRO A CG  
618  C CD  . PRO A 83  ? 0.20845 0.30449 0.42765 -0.07124 0.03475  0.04139  83  PRO A CD  
619  N N   . THR A 84  ? 0.22654 0.27876 0.43012 -0.00674 0.04689  0.03293  84  THR A N   
620  C CA  . THR A 84  ? 0.23200 0.26551 0.42317 0.01382  0.04914  0.03030  84  THR A CA  
621  C C   . THR A 84  ? 0.23786 0.24306 0.41493 0.01385  0.04121  0.02034  84  THR A C   
622  O O   . THR A 84  ? 0.25602 0.24039 0.41680 0.02151  0.04189  0.01601  84  THR A O   
623  C CB  . THR A 84  ? 0.23368 0.28266 0.42934 0.02975  0.05092  0.03724  84  THR A CB  
624  O OG1 . THR A 84  ? 0.22590 0.31401 0.43782 0.03192  0.05918  0.04977  84  THR A OG1 
625  C CG2 . THR A 84  ? 0.25398 0.26993 0.42409 0.04922  0.05332  0.03388  84  THR A CG2 
626  N N   . PHE A 85  ? 0.23952 0.24789 0.42257 0.00493  0.03340  0.01783  85  PHE A N   
627  C CA  . PHE A 85  ? 0.23623 0.22835 0.40916 0.00353  0.02653  0.01135  85  PHE A CA  
628  C C   . PHE A 85  ? 0.24071 0.22325 0.40315 0.00234  0.02895  0.00847  85  PHE A C   
629  O O   . PHE A 85  ? 0.25450 0.22823 0.40543 0.00810  0.02702  0.00546  85  PHE A O   
630  C CB  . PHE A 85  ? 0.22426 0.22417 0.40549 -0.00457 0.01960  0.01105  85  PHE A CB  
631  C CG  . PHE A 85  ? 0.22113 0.21396 0.39513 -0.00658 0.01305  0.00750  85  PHE A CG  
632  C CD1 . PHE A 85  ? 0.21473 0.20939 0.38463 -0.00829 0.01277  0.00653  85  PHE A CD1 
633  C CD2 . PHE A 85  ? 0.21354 0.19790 0.38081 -0.00661 0.00795  0.00670  85  PHE A CD2 
634  C CE1 . PHE A 85  ? 0.20677 0.20789 0.37386 -0.00939 0.00732  0.00654  85  PHE A CE1 
635  C CE2 . PHE A 85  ? 0.21217 0.19750 0.37454 -0.01360 0.00129  0.00547  85  PHE A CE2 
636  C CZ  . PHE A 85  ? 0.19461 0.19471 0.36072 -0.01475 0.00082  0.00624  85  PHE A CZ  
637  N N   . ARG A 86  ? 0.24138 0.22363 0.40286 -0.00531 0.03315  0.01002  86  ARG A N   
638  C CA  . ARG A 86  ? 0.26309 0.22748 0.40505 -0.00342 0.03714  0.00808  86  ARG A CA  
639  C C   . ARG A 86  ? 0.26880 0.22258 0.39878 0.00705  0.04349  0.00762  86  ARG A C   
640  O O   . ARG A 86  ? 0.27710 0.22288 0.39239 0.01695  0.04367  0.00572  86  ARG A O   
641  C CB  . ARG A 86  ? 0.28598 0.23988 0.41868 -0.01685 0.04092  0.00985  86  ARG A CB  
642  C CG  . ARG A 86  ? 0.30427 0.22745 0.40504 -0.01332 0.04668  0.00843  86  ARG A CG  
643  C CD  . ARG A 86  ? 0.31058 0.21377 0.39353 -0.03117 0.04791  0.00929  86  ARG A CD  
644  N NE  . ARG A 86  ? 0.32083 0.22500 0.40511 -0.04820 0.05234  0.01283  86  ARG A NE  
645  C CZ  . ARG A 86  ? 0.30037 0.22372 0.39862 -0.06976 0.04783  0.01643  86  ARG A CZ  
646  N NH1 . ARG A 86  ? 0.30099 0.23831 0.41053 -0.07555 0.03883  0.01570  86  ARG A NH1 
647  N NH2 . ARG A 86  ? 0.30964 0.24281 0.41096 -0.08618 0.05241  0.02218  86  ARG A NH2 
648  N N   . ASN A 87  ? 0.26504 0.22293 0.40098 0.00689  0.04909  0.01079  87  ASN A N   
649  C CA  . ASN A 87  ? 0.28087 0.22639 0.40336 0.01595  0.05746  0.01158  87  ASN A CA  
650  C C   . ASN A 87  ? 0.28947 0.23480 0.41046 0.02944  0.05577  0.01029  87  ASN A C   
651  O O   . ASN A 87  ? 0.31042 0.24346 0.41714 0.03939  0.06191  0.01033  87  ASN A O   
652  C CB  . ASN A 87  ? 0.27582 0.22704 0.40248 0.00633  0.06666  0.01817  87  ASN A CB  
653  C CG  . ASN A 87  ? 0.31299 0.24981 0.42655 -0.01094 0.06900  0.01880  87  ASN A CG  
654  O OD1 . ASN A 87  ? 0.34218 0.25103 0.43052 -0.00679 0.07023  0.01478  87  ASN A OD1 
655  N ND2 . ASN A 87  ? 0.30887 0.26398 0.43490 -0.03009 0.06967  0.02485  87  ASN A ND2 
656  N N   . THR A 88  ? 0.27857 0.23083 0.40758 0.03001  0.04820  0.00924  88  THR A N   
657  C CA  . THR A 88  ? 0.27916 0.21846 0.39470 0.04151  0.04692  0.00779  88  THR A CA  
658  C C   . THR A 88  ? 0.28317 0.21578 0.39195 0.03670  0.03470  0.00296  88  THR A C   
659  O O   . THR A 88  ? 0.31520 0.23504 0.40580 0.03807  0.02897  -0.00110 88  THR A O   
660  C CB  . THR A 88  ? 0.28379 0.22949 0.40411 0.05032  0.05460  0.01463  88  THR A CB  
661  O OG1 . THR A 88  ? 0.28663 0.24145 0.41100 0.05307  0.06627  0.02060  88  THR A OG1 
662  C CG2 . THR A 88  ? 0.29680 0.21635 0.39132 0.06479  0.05359  0.01288  88  THR A CG2 
663  N N   . VAL A 89  ? 0.27818 0.22009 0.39950 0.02898  0.03003  0.00398  89  VAL A N   
664  C CA  . VAL A 89  ? 0.28740 0.21974 0.39877 0.02175  0.01936  0.00060  89  VAL A CA  
665  C C   . VAL A 89  ? 0.27596 0.22155 0.38955 0.01278  0.01187  -0.00165 89  VAL A C   
666  O O   . VAL A 89  ? 0.26304 0.20316 0.36151 0.00714  0.00351  -0.00407 89  VAL A O   
667  C CB  . VAL A 89  ? 0.28138 0.21893 0.40321 0.01764  0.01753  0.00316  89  VAL A CB  
668  C CG1 . VAL A 89  ? 0.29778 0.22162 0.40563 0.00675  0.00726  0.00031  89  VAL A CG1 
669  C CG2 . VAL A 89  ? 0.28438 0.21469 0.40079 0.03198  0.02566  0.00801  89  VAL A CG2 
670  N N   . LEU A 90  ? 0.25812 0.22147 0.38637 0.01200  0.01514  0.00027  90  LEU A N   
671  C CA  . LEU A 90  ? 0.25061 0.23144 0.37977 0.00962  0.01047  0.00114  90  LEU A CA  
672  C C   . LEU A 90  ? 0.25558 0.23854 0.37019 0.01684  0.00947  0.00049  90  LEU A C   
673  O O   . LEU A 90  ? 0.24894 0.25414 0.36267 0.01412  0.00227  0.00272  90  LEU A O   
674  C CB  . LEU A 90  ? 0.23854 0.22486 0.37385 0.01228  0.01691  0.00358  90  LEU A CB  
675  C CG  . LEU A 90  ? 0.22350 0.22516 0.35380 0.01829  0.01683  0.00698  90  LEU A CG  
676  C CD1 . LEU A 90  ? 0.20906 0.23497 0.35054 0.01005  0.00782  0.00995  90  LEU A CD1 
677  C CD2 . LEU A 90  ? 0.22910 0.21580 0.35083 0.02219  0.02542  0.00814  90  LEU A CD2 
678  N N   . ILE A 91  ? 0.27336 0.23858 0.37688 0.02633  0.01653  -0.00112 91  ILE A N   
679  C CA  . ILE A 91  ? 0.28603 0.25133 0.37307 0.03547  0.01616  -0.00172 91  ILE A CA  
680  C C   . ILE A 91  ? 0.31469 0.26143 0.38441 0.03339  0.01033  -0.00550 91  ILE A C   
681  O O   . ILE A 91  ? 0.35724 0.29556 0.40985 0.04275  0.01187  -0.00672 91  ILE A O   
682  C CB  . ILE A 91  ? 0.33125 0.28446 0.40995 0.04930  0.02957  -0.00027 91  ILE A CB  
683  C CG1 . ILE A 91  ? 0.34412 0.27872 0.42630 0.04876  0.03881  -0.00017 91  ILE A CG1 
684  C CG2 . ILE A 91  ? 0.30064 0.26113 0.38039 0.05270  0.03452  0.00316  91  ILE A CG2 
685  C CD1 . ILE A 91  ? 0.40688 0.32830 0.47980 0.05510  0.05197  0.00236  91  ILE A CD1 
686  N N   . ASN A 92  ? 0.31462 0.24886 0.38184 0.02254  0.00413  -0.00729 92  ASN A N   
687  C CA  . ASN A 92  ? 0.33023 0.23372 0.36829 0.02091  -0.00103 -0.01111 92  ASN A CA  
688  C C   . ASN A 92  ? 0.34451 0.25858 0.36644 0.01117  -0.01409 -0.01274 92  ASN A C   
689  O O   . ASN A 92  ? 0.33417 0.27773 0.36667 -0.00441 -0.02443 -0.01034 92  ASN A O   
690  C CB  . ASN A 92  ? 0.33356 0.21429 0.36224 0.01148  -0.00494 -0.01208 92  ASN A CB  
691  C CG  . ASN A 92  ? 0.37632 0.21043 0.36128 0.01193  -0.00865 -0.01609 92  ASN A CG  
692  O OD1 . ASN A 92  ? 0.40087 0.22388 0.36149 -0.00563 -0.02214 -0.01932 92  ASN A OD1 
693  N ND2 . ASN A 92  ? 0.39265 0.19945 0.36373 0.03170  0.00337  -0.01486 92  ASN A ND2 
694  N N   . PRO A 93  ? 0.37011 0.26535 0.36655 0.01939  -0.01431 -0.01553 93  PRO A N   
695  C CA  . PRO A 93  ? 0.36574 0.28128 0.34918 0.01063  -0.02750 -0.01575 93  PRO A CA  
696  C C   . PRO A 93  ? 0.37203 0.28192 0.33583 -0.01796 -0.04559 -0.01766 93  PRO A C   
697  O O   . PRO A 93  ? 0.37108 0.32226 0.33996 -0.03296 -0.05858 -0.01407 93  PRO A O   
698  C CB  . PRO A 93  ? 0.39885 0.28582 0.35486 0.02775  -0.02203 -0.01893 93  PRO A CB  
699  C CG  . PRO A 93  ? 0.43327 0.30347 0.40135 0.04807  -0.00260 -0.01737 93  PRO A CG  
700  C CD  . PRO A 93  ? 0.39401 0.25817 0.37630 0.03954  -0.00105 -0.01656 93  PRO A CD  
701  N N   . VAL A 94  ? 0.43548 0.16583 0.36962 -0.02529 0.02276  -0.05669 94  VAL A N   
702  C CA  . VAL A 94  ? 0.44323 0.16778 0.37739 -0.02667 0.01389  -0.05622 94  VAL A CA  
703  C C   . VAL A 94  ? 0.42355 0.17547 0.38498 -0.02548 0.00123  -0.04950 94  VAL A C   
704  O O   . VAL A 94  ? 0.41975 0.16996 0.37811 -0.02934 -0.01200 -0.04707 94  VAL A O   
705  C CB  . VAL A 94  ? 0.45152 0.16557 0.38986 -0.02272 0.02704  -0.06048 94  VAL A CB  
706  C CG1 . VAL A 94  ? 0.45400 0.16480 0.39667 -0.02377 0.01792  -0.05919 94  VAL A CG1 
707  C CG2 . VAL A 94  ? 0.47046 0.15216 0.37658 -0.02493 0.04001  -0.06784 94  VAL A CG2 
708  N N   . ILE A 95  ? 0.40683 0.18360 0.39481 -0.02071 0.00528  -0.04637 95  ILE A N   
709  C CA  . ILE A 95  ? 0.38028 0.18141 0.39051 -0.02001 -0.00515 -0.04019 95  ILE A CA  
710  C C   . ILE A 95  ? 0.37609 0.17901 0.37740 -0.02414 -0.01671 -0.03755 95  ILE A C   
711  O O   . ILE A 95  ? 0.37624 0.18831 0.38648 -0.02589 -0.02764 -0.03346 95  ILE A O   
712  C CB  . ILE A 95  ? 0.35927 0.18335 0.39404 -0.01524 0.00114  -0.03783 95  ILE A CB  
713  C CG1 . ILE A 95  ? 0.35309 0.17796 0.40214 -0.01043 0.01078  -0.03907 95  ILE A CG1 
714  C CG2 . ILE A 95  ? 0.33534 0.18138 0.38759 -0.01530 -0.00866 -0.03193 95  ILE A CG2 
715  C CD1 . ILE A 95  ? 0.36544 0.18968 0.42293 -0.00948 0.00538  -0.03672 95  ILE A CD1 
716  N N   . HIS A 96  ? 0.38583 0.17977 0.37045 -0.02568 -0.01418 -0.03945 96  HIS A N   
717  C CA  . HIS A 96  ? 0.39430 0.19108 0.37357 -0.02851 -0.02538 -0.03609 96  HIS A CA  
718  C C   . HIS A 96  ? 0.42374 0.20137 0.38264 -0.03391 -0.03670 -0.03631 96  HIS A C   
719  O O   . HIS A 96  ? 0.42838 0.21346 0.39280 -0.03594 -0.04934 -0.03191 96  HIS A O   
720  C CB  . HIS A 96  ? 0.39721 0.19200 0.36741 -0.02807 -0.01944 -0.03704 96  HIS A CB  
721  C CG  . HIS A 96  ? 0.36778 0.18524 0.36088 -0.02420 -0.01338 -0.03529 96  HIS A CG  
722  N ND1 . HIS A 96  ? 0.34685 0.18239 0.35480 -0.02330 -0.02016 -0.03089 96  HIS A ND1 
723  C CD2 . HIS A 96  ? 0.35650 0.18156 0.36137 -0.02127 -0.00174 -0.03720 96  HIS A CD2 
724  C CE1 . HIS A 96  ? 0.33175 0.18297 0.35585 -0.02066 -0.01329 -0.03058 96  HIS A CE1 
725  N NE2 . HIS A 96  ? 0.32168 0.16798 0.34555 -0.01951 -0.00295 -0.03402 96  HIS A NE2 
726  N N   . ALA A 97  ? 0.43435 0.18718 0.37050 -0.03649 -0.03257 -0.04127 97  ALA A N   
727  C CA  . ALA A 97  ? 0.43975 0.17347 0.35609 -0.04274 -0.04502 -0.04151 97  ALA A CA  
728  C C   . ALA A 97  ? 0.44501 0.19255 0.38245 -0.04373 -0.05513 -0.03770 97  ALA A C   
729  O O   . ALA A 97  ? 0.44148 0.18992 0.37903 -0.04817 -0.06993 -0.03405 97  ALA A O   
730  C CB  . ALA A 97  ? 0.44661 0.14894 0.33294 -0.04551 -0.03692 -0.04836 97  ALA A CB  
731  N N   . ILE A 98  ? 0.42879 0.18790 0.38585 -0.03967 -0.04743 -0.03789 98  ILE A N   
732  C CA  . ILE A 98  ? 0.41221 0.18434 0.38953 -0.04059 -0.05525 -0.03388 98  ILE A CA  
733  C C   . ILE A 98  ? 0.40288 0.19992 0.40179 -0.03999 -0.06343 -0.02747 98  ILE A C   
734  O O   . ILE A 98  ? 0.39777 0.19963 0.40445 -0.04395 -0.07508 -0.02371 98  ILE A O   
735  C CB  . ILE A 98  ? 0.38924 0.16838 0.38262 -0.03560 -0.04484 -0.03459 98  ILE A CB  
736  C CG1 . ILE A 98  ? 0.43333 0.18658 0.40821 -0.03611 -0.03717 -0.04067 98  ILE A CG1 
737  C CG2 . ILE A 98  ? 0.36453 0.16061 0.38066 -0.03612 -0.05193 -0.02913 98  ILE A CG2 
738  C CD1 . ILE A 98  ? 0.40895 0.16890 0.40126 -0.02964 -0.02567 -0.04111 98  ILE A CD1 
739  N N   . CYS A 99  ? 0.40009 0.21300 0.40980 -0.03521 -0.05673 -0.02625 99  CYS A N   
740  C CA  . CYS A 99  ? 0.36552 0.20060 0.39484 -0.03393 -0.06184 -0.02086 99  CYS A CA  
741  C C   . CYS A 99  ? 0.37367 0.20451 0.39574 -0.03743 -0.07347 -0.01851 99  CYS A C   
742  O O   . CYS A 99  ? 0.37098 0.21484 0.40961 -0.03873 -0.08201 -0.01369 99  CYS A O   
743  C CB  . CYS A 99  ? 0.35100 0.19933 0.38849 -0.02897 -0.05223 -0.02101 99  CYS A CB  
744  S SG  . CYS A 99  ? 0.31294 0.17510 0.36842 -0.02448 -0.04215 -0.02089 99  CYS A SG  
745  N N   . GLU A 100 ? 0.39895 0.21144 0.39701 -0.03899 -0.07384 -0.02140 100 GLU A N   
746  C CA  . GLU A 100 ? 0.40145 0.20893 0.39200 -0.04199 -0.08626 -0.01831 100 GLU A CA  
747  C C   . GLU A 100 ? 0.41522 0.21666 0.40578 -0.04799 -0.10047 -0.01614 100 GLU A C   
748  O O   . GLU A 100 ? 0.41358 0.22447 0.41685 -0.04955 -0.11241 -0.01088 100 GLU A O   
749  C CB  . GLU A 100 ? 0.44074 0.22625 0.40137 -0.04308 -0.08346 -0.02169 100 GLU A CB  
750  C CG  . GLU A 100 ? 0.45012 0.24545 0.41537 -0.03830 -0.07538 -0.02095 100 GLU A CG  
751  C CD  . GLU A 100 ? 0.50315 0.27950 0.44286 -0.03834 -0.06408 -0.02591 100 GLU A CD  
752  O OE1 . GLU A 100 ? 0.55769 0.30951 0.47077 -0.04235 -0.06379 -0.02964 100 GLU A OE1 
753  O OE2 . GLU A 100 ? 0.48826 0.27336 0.43396 -0.03481 -0.05479 -0.02622 100 GLU A OE2 
754  N N   . ALA A 101 ? 0.42858 0.21505 0.40749 -0.05138 -0.09919 -0.01994 101 ALA A N   
755  C CA  . ALA A 101 ? 0.42786 0.20825 0.40746 -0.05809 -0.11267 -0.01814 101 ALA A CA  
756  C C   . ALA A 101 ? 0.41365 0.21897 0.42688 -0.05722 -0.11476 -0.01315 101 ALA A C   
757  O O   . ALA A 101 ? 0.42496 0.23740 0.45131 -0.06154 -0.12766 -0.00848 101 ALA A O   
758  C CB  . ALA A 101 ? 0.44798 0.20239 0.40337 -0.06202 -0.10926 -0.02429 101 ALA A CB  
759  N N   . TYR A 102 ? 0.40158 0.22004 0.42922 -0.05202 -0.10226 -0.01370 102 TYR A N   
760  C CA  . TYR A 102 ? 0.38220 0.22124 0.43771 -0.05158 -0.10249 -0.00912 102 TYR A CA  
761  C C   . TYR A 102 ? 0.36466 0.22618 0.44235 -0.04915 -0.10523 -0.00358 102 TYR A C   
762  O O   . TYR A 102 ? 0.36255 0.23723 0.46103 -0.05169 -0.11121 0.00122  102 TYR A O   
763  C CB  . TYR A 102 ? 0.36903 0.21294 0.42997 -0.04678 -0.08924 -0.01094 102 TYR A CB  
764  C CG  . TYR A 102 ? 0.34908 0.21220 0.43481 -0.04589 -0.08725 -0.00617 102 TYR A CG  
765  C CD1 . TYR A 102 ? 0.35075 0.20946 0.44133 -0.05026 -0.09093 -0.00484 102 TYR A CD1 
766  C CD2 . TYR A 102 ? 0.33041 0.21330 0.43155 -0.04115 -0.08106 -0.00330 102 TYR A CD2 
767  C CE1 . TYR A 102 ? 0.33032 0.20469 0.44104 -0.04980 -0.08823 -0.00018 102 TYR A CE1 
768  C CE2 . TYR A 102 ? 0.30762 0.20484 0.42701 -0.04097 -0.07857 0.00095  102 TYR A CE2 
769  C CZ  . TYR A 102 ? 0.31933 0.21282 0.44396 -0.04521 -0.08185 0.00284  102 TYR A CZ  
770  O OH  . TYR A 102 ? 0.31925 0.22534 0.45989 -0.04543 -0.07870 0.00742  102 TYR A OH  
771  N N   . PHE A 103 ? 0.36780 0.23331 0.44197 -0.04435 -0.10010 -0.00421 103 PHE A N   
772  C CA  . PHE A 103 ? 0.36552 0.24966 0.45895 -0.04134 -0.10132 0.00042  103 PHE A CA  
773  C C   . PHE A 103 ? 0.37777 0.25696 0.46808 -0.04358 -0.11412 0.00317  103 PHE A C   
774  O O   . PHE A 103 ? 0.37413 0.26437 0.47587 -0.03985 -0.11424 0.00627  103 PHE A O   
775  C CB  . PHE A 103 ? 0.33199 0.22295 0.42447 -0.03523 -0.08926 -0.00140 103 PHE A CB  
776  C CG  . PHE A 103 ? 0.31180 0.21320 0.41412 -0.03278 -0.07894 -0.00191 103 PHE A CG  
777  C CD1 . PHE A 103 ? 0.29025 0.20755 0.41354 -0.03299 -0.07828 0.00227  103 PHE A CD1 
778  C CD2 . PHE A 103 ? 0.30165 0.19680 0.39265 -0.03039 -0.06993 -0.00610 103 PHE A CD2 
779  C CE1 . PHE A 103 ? 0.27058 0.19530 0.39982 -0.03123 -0.07001 0.00245  103 PHE A CE1 
780  C CE2 . PHE A 103 ? 0.27741 0.18214 0.37803 -0.02821 -0.06255 -0.00564 103 PHE A CE2 
781  C CZ  . PHE A 103 ? 0.27401 0.19260 0.39203 -0.02878 -0.06315 -0.00128 103 PHE A CZ  
782  N N   . GLN A 104 ? 0.42053 0.28224 0.49519 -0.04972 -0.12538 0.00228  104 GLN A N   
783  C CA  . GLN A 104 ? 0.42962 0.28377 0.49809 -0.05264 -0.13997 0.00534  104 GLN A CA  
784  C C   . GLN A 104 ? 0.43271 0.30957 0.53403 -0.05095 -0.14659 0.01253  104 GLN A C   
785  O O   . GLN A 104 ? 0.45636 0.33630 0.56107 -0.04767 -0.15064 0.01563  104 GLN A O   
786  C CB  . GLN A 104 ? 0.44809 0.28137 0.49766 -0.06116 -0.15237 0.00376  104 GLN A CB  
787  C CG  . GLN A 104 ? 0.52273 0.33063 0.53929 -0.06440 -0.16103 0.00194  104 GLN A CG  
788  C CD  . GLN A 104 ? 0.62257 0.43330 0.64790 -0.06759 -0.18023 0.00870  104 GLN A CD  
789  O OE1 . GLN A 104 ? 0.60862 0.44099 0.66722 -0.06771 -0.18683 0.01450  104 GLN A OE1 
790  N NE2 . GLN A 104 ? 0.65752 0.44602 0.65348 -0.07030 -0.18927 0.00840  104 GLN A NE2 
791  N N   . ARG A 105 ? 0.40382 0.29650 0.53045 -0.05282 -0.14640 0.01538  105 ARG A N   
792  C CA  . ARG A 105 ? 0.36269 0.27736 0.52368 -0.05182 -0.15130 0.02226  105 ARG A CA  
793  C C   . ARG A 105 ? 0.32899 0.26144 0.50712 -0.04366 -0.13792 0.02357  105 ARG A C   
794  O O   . ARG A 105 ? 0.31412 0.26095 0.51630 -0.04094 -0.14118 0.02880  105 ARG A O   
795  C CB  . ARG A 105 ? 0.35778 0.28214 0.53913 -0.05736 -0.15360 0.02469  105 ARG A CB  
796  C CG  . ARG A 105 ? 0.39636 0.30440 0.56537 -0.06672 -0.16915 0.02430  105 ARG A CG  
797  C CD  . ARG A 105 ? 0.41013 0.32505 0.59580 -0.07252 -0.16882 0.02572  105 ARG A CD  
798  N NE  . ARG A 105 ? 0.37702 0.31756 0.60219 -0.07223 -0.16934 0.03264  105 ARG A NE  
799  C CZ  . ARG A 105 ? 0.35595 0.30716 0.60099 -0.07613 -0.16595 0.03520  105 ARG A CZ  
800  N NH1 . ARG A 105 ? 0.39162 0.33027 0.62039 -0.07999 -0.16244 0.03177  105 ARG A NH1 
801  N NH2 . ARG A 105 ? 0.35147 0.32562 0.63033 -0.07426 -0.16321 0.04149  105 ARG A NH2 
802  N N   . THR A 106 ? 0.32461 0.25619 0.49193 -0.03981 -0.12317 0.01910  106 THR A N   
803  C CA  . THR A 106 ? 0.30661 0.25287 0.48735 -0.03322 -0.11079 0.01988  106 THR A CA  
804  C C   . THR A 106 ? 0.30612 0.24493 0.47171 -0.02829 -0.10778 0.01781  106 THR A C   
805  O O   . THR A 106 ? 0.28862 0.23773 0.46515 -0.02304 -0.09944 0.01875  106 THR A O   
806  C CB  . THR A 106 ? 0.29626 0.24734 0.47611 -0.03238 -0.09747 0.01716  106 THR A CB  
807  O OG1 . THR A 106 ? 0.28893 0.25544 0.48545 -0.02784 -0.08707 0.01904  106 THR A OG1 
808  C CG2 . THR A 106 ? 0.29304 0.23019 0.44666 -0.03100 -0.09149 0.01134  106 THR A CG2 
809  N N   . GLY A 107 ? 0.31261 0.23224 0.45218 -0.03023 -0.11371 0.01495  107 GLY A N   
810  C CA  . GLY A 107 ? 0.30472 0.21551 0.42798 -0.02633 -0.10977 0.01295  107 GLY A CA  
811  C C   . GLY A 107 ? 0.30907 0.21541 0.41695 -0.02473 -0.09603 0.00715  107 GLY A C   
812  O O   . GLY A 107 ? 0.31220 0.21334 0.41176 -0.02752 -0.09316 0.00393  107 GLY A O   
813  N N   . ASP A 108 ? 0.29245 0.20097 0.39818 -0.02028 -0.08769 0.00603  108 ASP A N   
814  C CA  . ASP A 108 ? 0.28716 0.19078 0.37842 -0.01933 -0.07624 0.00088  108 ASP A CA  
815  C C   . ASP A 108 ? 0.26425 0.18014 0.36679 -0.01915 -0.06804 -0.00032 108 ASP A C   
816  O O   . ASP A 108 ? 0.24723 0.17738 0.36887 -0.01818 -0.06684 0.00267  108 ASP A O   
817  C CB  . ASP A 108 ? 0.29129 0.19470 0.37924 -0.01548 -0.07012 0.00036  108 ASP A CB  
818  C CG  . ASP A 108 ? 0.30880 0.19587 0.37954 -0.01578 -0.07683 0.00118  108 ASP A CG  
819  O OD1 . ASP A 108 ? 0.32347 0.19734 0.38043 -0.01951 -0.08543 0.00124  108 ASP A OD1 
820  O OD2 . ASP A 108 ? 0.30781 0.19341 0.37696 -0.01264 -0.07365 0.00182  108 ASP A OD2 
821  N N   . TYR A 109 ? 0.26488 0.17437 0.35530 -0.02003 -0.06198 -0.00445 109 TYR A N   
822  C CA  . TYR A 109 ? 0.25131 0.17001 0.34941 -0.01960 -0.05477 -0.00544 109 TYR A CA  
823  C C   . TYR A 109 ? 0.26050 0.17845 0.35109 -0.01780 -0.04578 -0.00881 109 TYR A C   
824  O O   . TYR A 109 ? 0.26980 0.17710 0.34667 -0.01772 -0.04446 -0.01115 109 TYR A O   
825  C CB  . TYR A 109 ? 0.25769 0.16931 0.35143 -0.02227 -0.05680 -0.00674 109 TYR A CB  
826  C CG  . TYR A 109 ? 0.27639 0.17028 0.34952 -0.02321 -0.05523 -0.01115 109 TYR A CG  
827  C CD1 . TYR A 109 ? 0.30632 0.18505 0.36480 -0.02587 -0.06287 -0.01152 109 TYR A CD1 
828  C CD2 . TYR A 109 ? 0.27848 0.17069 0.34714 -0.02166 -0.04596 -0.01461 109 TYR A CD2 
829  C CE1 . TYR A 109 ? 0.32409 0.18438 0.36067 -0.02710 -0.05965 -0.01579 109 TYR A CE1 
830  C CE2 . TYR A 109 ? 0.29253 0.16838 0.34337 -0.02245 -0.04233 -0.01871 109 TYR A CE2 
831  C CZ  . TYR A 109 ? 0.32342 0.18187 0.35605 -0.02526 -0.04823 -0.01967 109 TYR A CZ  
832  O OH  . TYR A 109 ? 0.34354 0.18360 0.35560 -0.02643 -0.04293 -0.02398 109 TYR A OH  
833  N N   . TRP A 110 ? 0.23648 0.16513 0.33560 -0.01694 -0.04000 -0.00874 110 TRP A N   
834  C CA  . TRP A 110 ? 0.23149 0.16044 0.32578 -0.01627 -0.03285 -0.01170 110 TRP A CA  
835  C C   . TRP A 110 ? 0.22880 0.16570 0.33112 -0.01644 -0.03037 -0.01108 110 TRP A C   
836  O O   . TRP A 110 ? 0.22347 0.16365 0.33274 -0.01704 -0.03354 -0.00855 110 TRP A O   
837  C CB  . TRP A 110 ? 0.23207 0.16458 0.32613 -0.01513 -0.02947 -0.01187 110 TRP A CB  
838  C CG  . TRP A 110 ? 0.22544 0.16852 0.33043 -0.01422 -0.02890 -0.00906 110 TRP A CG  
839  C CD1 . TRP A 110 ? 0.21202 0.16344 0.32732 -0.01477 -0.02986 -0.00623 110 TRP A CD1 
840  C CD2 . TRP A 110 ? 0.22004 0.16447 0.32545 -0.01267 -0.02575 -0.00900 110 TRP A CD2 
841  N NE1 . TRP A 110 ? 0.20062 0.15851 0.32223 -0.01379 -0.02659 -0.00461 110 TRP A NE1 
842  C CE2 . TRP A 110 ? 0.20277 0.15637 0.31876 -0.01220 -0.02396 -0.00647 110 TRP A CE2 
843  C CE3 . TRP A 110 ? 0.22092 0.15822 0.31801 -0.01169 -0.02347 -0.01087 110 TRP A CE3 
844  C CZ2 . TRP A 110 ? 0.21283 0.16833 0.33145 -0.01037 -0.01921 -0.00623 110 TRP A CZ2 
845  C CZ3 . TRP A 110 ? 0.21522 0.15444 0.31537 -0.00981 -0.01985 -0.01038 110 TRP A CZ3 
846  C CH2 . TRP A 110 ? 0.20855 0.15669 0.31945 -0.00896 -0.01736 -0.00833 110 TRP A CH2 
847  N N   . LEU A 111 ? 0.22760 0.16719 0.32943 -0.01622 -0.02530 -0.01298 111 LEU A N   
848  C CA  . LEU A 111 ? 0.21663 0.16304 0.32630 -0.01616 -0.02420 -0.01188 111 LEU A CA  
849  C C   . LEU A 111 ? 0.21465 0.17118 0.32973 -0.01695 -0.02459 -0.00906 111 LEU A C   
850  O O   . LEU A 111 ? 0.21904 0.17818 0.33133 -0.01766 -0.02203 -0.01015 111 LEU A O   
851  C CB  . LEU A 111 ? 0.21531 0.16107 0.32485 -0.01590 -0.01942 -0.01464 111 LEU A CB  
852  C CG  . LEU A 111 ? 0.19730 0.15006 0.31761 -0.01519 -0.01954 -0.01282 111 LEU A CG  
853  C CD1 . LEU A 111 ? 0.21382 0.15989 0.33570 -0.01359 -0.02042 -0.01255 111 LEU A CD1 
854  C CD2 . LEU A 111 ? 0.19905 0.15550 0.32413 -0.01538 -0.01522 -0.01476 111 LEU A CD2 
855  N N   . SER A 112 ? 0.20720 0.16754 0.32810 -0.01732 -0.02726 -0.00557 112 SER A N   
856  C CA  . SER A 112 ? 0.20555 0.17299 0.32822 -0.01867 -0.02667 -0.00283 112 SER A CA  
857  C C   . SER A 112 ? 0.21890 0.19035 0.34274 -0.01948 -0.02715 -0.00194 112 SER A C   
858  O O   . SER A 112 ? 0.23300 0.20778 0.35302 -0.02141 -0.02635 -0.00140 112 SER A O   
859  C CB  . SER A 112 ? 0.21481 0.18395 0.34240 -0.01945 -0.02858 0.00109  112 SER A CB  
860  O OG  . SER A 112 ? 0.19414 0.16783 0.32043 -0.02114 -0.02656 0.00364  112 SER A OG  
861  N N   . ALA A 113 ? 0.20985 0.18031 0.33892 -0.01811 -0.02866 -0.00173 113 ALA A N   
862  C CA  . ALA A 113 ? 0.21164 0.18710 0.34586 -0.01832 -0.03036 -0.00016 113 ALA A CA  
863  C C   . ALA A 113 ? 0.21101 0.18388 0.35321 -0.01541 -0.02968 -0.00107 113 ALA A C   
864  O O   . ALA A 113 ? 0.21176 0.17753 0.35310 -0.01387 -0.02893 -0.00195 113 ALA A O   
865  C CB  . ALA A 113 ? 0.22210 0.20071 0.35649 -0.01989 -0.03437 0.00510  113 ALA A CB  
866  N N   . ALA A 114 ? 0.20677 0.18494 0.35713 -0.01492 -0.02976 -0.00093 114 ALA A N   
867  C CA  . ALA A 114 ? 0.21003 0.18720 0.37185 -0.01144 -0.02820 -0.00093 114 ALA A CA  
868  C C   . ALA A 114 ? 0.20915 0.19643 0.38378 -0.01153 -0.03220 0.00257  114 ALA A C   
869  O O   . ALA A 114 ? 0.21950 0.21285 0.39495 -0.01429 -0.03246 0.00145  114 ALA A O   
870  C CB  . ALA A 114 ? 0.21081 0.18185 0.37099 -0.01017 -0.02080 -0.00642 114 ALA A CB  
871  N N   . PHE A 115 ? 0.21731 0.20574 0.40204 -0.00881 -0.03611 0.00711  115 PHE A N   
872  C CA  . PHE A 115 ? 0.20915 0.20701 0.40606 -0.00904 -0.04300 0.01226  115 PHE A CA  
873  C C   . PHE A 115 ? 0.22123 0.21857 0.43489 -0.00350 -0.04357 0.01549  115 PHE A C   
874  O O   . PHE A 115 ? 0.24720 0.23498 0.45860 -0.00041 -0.03975 0.01439  115 PHE A O   
875  C CB  . PHE A 115 ? 0.20856 0.20714 0.39414 -0.01303 -0.05075 0.01709  115 PHE A CB  
876  C CG  . PHE A 115 ? 0.22217 0.21270 0.40004 -0.01218 -0.05139 0.01980  115 PHE A CG  
877  C CD1 . PHE A 115 ? 0.23858 0.22296 0.40385 -0.01371 -0.04682 0.01659  115 PHE A CD1 
878  C CD2 . PHE A 115 ? 0.23686 0.22602 0.42154 -0.01000 -0.05694 0.02605  115 PHE A CD2 
879  C CE1 . PHE A 115 ? 0.24882 0.22684 0.40942 -0.01378 -0.04746 0.01927  115 PHE A CE1 
880  C CE2 . PHE A 115 ? 0.26513 0.24611 0.44275 -0.01000 -0.05713 0.02867  115 PHE A CE2 
881  C CZ  . PHE A 115 ? 0.26330 0.23920 0.42936 -0.01224 -0.05219 0.02511  115 PHE A CZ  
882  N N   . LEU A 116 ? 0.22288 0.23003 0.45375 -0.00243 -0.04904 0.01980  116 LEU A N   
883  C CA  . LEU A 116 ? 0.20917 0.21728 0.45981 0.00362  -0.05040 0.02401  116 LEU A CA  
884  C C   . LEU A 116 ? 0.21696 0.22388 0.46515 0.00333  -0.06132 0.03219  116 LEU A C   
885  O O   . LEU A 116 ? 0.22173 0.23323 0.46196 -0.00168 -0.07012 0.03603  116 LEU A O   
886  C CB  . LEU A 116 ? 0.20102 0.22196 0.47661 0.00545  -0.05053 0.02493  116 LEU A CB  
887  C CG  . LEU A 116 ? 0.19777 0.22221 0.49960 0.01262  -0.05217 0.03011  116 LEU A CG  
888  C CD1 . LEU A 116 ? 0.21226 0.22503 0.51692 0.01881  -0.03925 0.02520  116 LEU A CD1 
889  C CD2 . LEU A 116 ? 0.19601 0.23699 0.52511 0.01296  -0.05542 0.03270  116 LEU A CD2 
890  N N   . ARG A 117 ? 0.24311 0.24174 0.49605 0.00830  -0.06039 0.03478  117 ARG A N   
891  C CA  . ARG A 117 ? 0.25965 0.25685 0.51671 0.00980  -0.07040 0.04372  117 ARG A CA  
892  C C   . ARG A 117 ? 0.24279 0.24384 0.52802 0.01759  -0.07065 0.04718  117 ARG A C   
893  O O   . ARG A 117 ? 0.24104 0.23633 0.53519 0.02295  -0.06022 0.04248  117 ARG A O   
894  C CB  . ARG A 117 ? 0.27784 0.26105 0.51819 0.00906  -0.06941 0.04486  117 ARG A CB  
895  C CG  . ARG A 117 ? 0.28835 0.26954 0.50655 0.00193  -0.07462 0.04752  117 ARG A CG  
896  C CD  . ARG A 117 ? 0.32718 0.29574 0.53207 0.00073  -0.07155 0.04781  117 ARG A CD  
897  N NE  . ARG A 117 ? 0.32694 0.28663 0.54213 0.00621  -0.07118 0.05070  117 ARG A NE  
898  C CZ  . ARG A 117 ? 0.32945 0.28338 0.54513 0.00709  -0.07809 0.05897  117 ARG A CZ  
899  N NH1 . ARG A 117 ? 0.32269 0.27883 0.52870 0.00275  -0.08669 0.06579  117 ARG A NH1 
900  N NH2 . ARG A 117 ? 0.33833 0.28197 0.56235 0.01216  -0.07610 0.06042  117 ARG A NH2 
901  N N   . GLU A 118 ? 0.25173 0.26184 0.55080 0.01812  -0.08249 0.05541  118 GLU A N   
902  C CA  . GLU A 118 ? 0.26745 0.28306 0.59733 0.02605  -0.08464 0.06049  118 GLU A CA  
903  C C   . GLU A 118 ? 0.28699 0.29805 0.61647 0.02727  -0.09796 0.07132  118 GLU A C   
904  O O   . GLU A 118 ? 0.29583 0.31306 0.62087 0.02241  -0.11157 0.07793  118 GLU A O   
905  C CB  . GLU A 118 ? 0.24382 0.27754 0.59752 0.02575  -0.08759 0.06098  118 GLU A CB  
906  C CG  . GLU A 118 ? 0.24618 0.28731 0.63676 0.03480  -0.08756 0.06568  118 GLU A CG  
907  C CD  . GLU A 118 ? 0.23901 0.30023 0.65662 0.03360  -0.09266 0.06772  118 GLU A CD  
908  O OE1 . GLU A 118 ? 0.24592 0.31597 0.66658 0.02935  -0.10959 0.07563  118 GLU A OE1 
909  O OE2 . GLU A 118 ? 0.24031 0.30764 0.67535 0.03629  -0.07972 0.06145  118 GLU A OE2 
910  N N   . ILE A 119 ? 0.29034 0.28885 0.62265 0.03328  -0.09439 0.07327  119 ILE A N   
911  C CA  . ILE A 119 ? 0.34205 0.33098 0.66567 0.03324  -0.10514 0.08283  119 ILE A CA  
912  C C   . ILE A 119 ? 0.37623 0.36957 0.73062 0.04179  -0.11260 0.09164  119 ILE A C   
913  O O   . ILE A 119 ? 0.37342 0.36604 0.75097 0.05037  -0.10311 0.08888  119 ILE A O   
914  C CB  . ILE A 119 ? 0.36051 0.33070 0.66474 0.03307  -0.09719 0.07981  119 ILE A CB  
915  C CG1 . ILE A 119 ? 0.31317 0.28101 0.59152 0.02518  -0.09020 0.07149  119 ILE A CG1 
916  C CG2 . ILE A 119 ? 0.40366 0.36309 0.69767 0.03213  -0.10765 0.09005  119 ILE A CG2 
917  C CD1 . ILE A 119 ? 0.29727 0.26345 0.57838 0.02730  -0.07595 0.06059  119 ILE A CD1 
918  N N   . GLU A 120 ? 0.46762 0.46451 0.82147 0.03937  -0.12934 0.10223  120 GLU A N   
919  C CA  . GLU A 120 ? 0.48421 0.48806 0.86781 0.04638  -0.13844 0.11116  120 GLU A CA  
920  C C   . GLU A 120 ? 0.51436 0.50181 0.89309 0.05085  -0.13888 0.11673  120 GLU A C   
921  O O   . GLU A 120 ? 0.54479 0.51734 0.89841 0.04716  -0.14231 0.12000  120 GLU A O   
922  C CB  . GLU A 120 ? 0.49465 0.50954 0.87614 0.03976  -0.15645 0.11898  120 GLU A CB  
923  C CG  . GLU A 120 ? 0.47921 0.51113 0.89292 0.04298  -0.15783 0.11981  120 GLU A CG  
924  C CD  . GLU A 120 ? 0.52143 0.56550 0.93594 0.03563  -0.17452 0.12562  120 GLU A CD  
925  O OE1 . GLU A 120 ? 0.57422 0.61258 0.96125 0.02739  -0.18721 0.13001  120 GLU A OE1 
926  O OE2 . GLU A 120 ? 0.55101 0.60931 0.99359 0.03796  -0.17425 0.12564  120 GLU A OE2 
927  N N   . SER A 121 ? 0.49075 0.48153 0.89376 0.05819  -0.13585 0.11829  121 SER A N   
928  C CA  . SER A 121 ? 0.47209 0.44793 0.87315 0.06320  -0.13595 0.12340  121 SER A CA  
929  C C   . SER A 121 ? 0.48493 0.45266 0.86380 0.05737  -0.15274 0.13417  121 SER A C   
930  O O   . SER A 121 ? 0.50633 0.48362 0.88185 0.05168  -0.16685 0.13989  121 SER A O   
931  C CB  . SER A 121 ? 0.41657 0.40033 0.84965 0.07167  -0.13313 0.12523  121 SER A CB  
932  O OG  . SER A 121 ? 0.47913 0.47951 0.92658 0.06908  -0.14709 0.13195  121 SER A OG  
933  N N   . GLY A 122 ? 0.50330 0.45167 0.86445 0.05793  -0.15069 0.13661  122 GLY A N   
934  C CA  . GLY A 122 ? 0.53563 0.47277 0.87172 0.05187  -0.16407 0.14645  122 GLY A CA  
935  C C   . GLY A 122 ? 0.53594 0.46800 0.84214 0.04209  -0.16700 0.14606  122 GLY A C   
936  O O   . GLY A 122 ? 0.54256 0.46460 0.82468 0.03581  -0.17758 0.15437  122 GLY A O   
937  N N   . MET A 123 ? 0.55849 0.49625 0.86456 0.04046  -0.15782 0.13704  123 MET A N   
938  C CA  . MET A 123 ? 0.54374 0.47489 0.81780 0.03062  -0.15692 0.13505  123 MET A CA  
939  C C   . MET A 123 ? 0.57006 0.48258 0.82769 0.02959  -0.14653 0.13251  123 MET A C   
940  O O   . MET A 123 ? 0.55694 0.46361 0.82945 0.03655  -0.13696 0.12812  123 MET A O   
941  C CB  . MET A 123 ? 0.53591 0.48121 0.80845 0.02656  -0.14806 0.12329  123 MET A CB  
942  C CG  . MET A 123 ? 0.52188 0.48561 0.80972 0.02588  -0.15805 0.12514  123 MET A CG  
943  S SD  . MET A 123 ? 0.65488 0.61645 0.92909 0.02010  -0.18098 0.13957  123 MET A SD  
944  C CE  . MET A 123 ? 0.54520 0.52046 0.85919 0.02876  -0.18913 0.14502  123 MET A CE  
945  N N   . PRO A 124 ? 0.53355 0.43548 0.76062 0.02065  -0.14804 0.13540  124 PRO A N   
946  C CA  . PRO A 124 ? 0.54425 0.42898 0.75737 0.01858  -0.13922 0.13409  124 PRO A CA  
947  C C   . PRO A 124 ? 0.55222 0.44042 0.76059 0.01548  -0.12446 0.12092  124 PRO A C   
948  O O   . PRO A 124 ? 0.54238 0.44461 0.75145 0.01331  -0.12118 0.11357  124 PRO A O   
949  C CB  . PRO A 124 ? 0.54610 0.42049 0.72941 0.00940  -0.14603 0.14242  124 PRO A CB  
950  C CG  . PRO A 124 ? 0.50542 0.39318 0.67926 0.00385  -0.15127 0.14092  124 PRO A CG  
951  C CD  . PRO A 124 ? 0.51142 0.41541 0.71446 0.01142  -0.15719 0.13993  124 PRO A CD  
952  N N   . ALA A 125 ? 0.58276 0.45693 0.78588 0.01489  -0.11638 0.11844  125 ALA A N   
953  C CA  . ALA A 125 ? 0.56715 0.44261 0.76628 0.01189  -0.10407 0.10682  125 ALA A CA  
954  C C   . ALA A 125 ? 0.57011 0.45252 0.74920 0.00232  -0.10185 0.10391  125 ALA A C   
955  O O   . ALA A 125 ? 0.58095 0.46018 0.74339 -0.00350 -0.10705 0.11098  125 ALA A O   
956  C CB  . ALA A 125 ? 0.53797 0.39538 0.73426 0.01178  -0.09803 0.10585  125 ALA A CB  
957  N N   . GLN A 126 ? 0.48824 0.37909 0.66844 0.00094  -0.09363 0.09347  126 GLN A N   
958  C CA  . GLN A 126 ? 0.46765 0.36406 0.63163 -0.00715 -0.08952 0.08980  126 GLN A CA  
959  C C   . GLN A 126 ? 0.47385 0.35843 0.62620 -0.01315 -0.08499 0.09136  126 GLN A C   
960  O O   . GLN A 126 ? 0.48686 0.35993 0.64465 -0.01119 -0.08310 0.09148  126 GLN A O   
961  C CB  . GLN A 126 ? 0.44741 0.35445 0.61724 -0.00629 -0.08251 0.07885  126 GLN A CB  
962  C CG  . GLN A 126 ? 0.41823 0.33765 0.57938 -0.01058 -0.08208 0.07585  126 GLN A CG  
963  C CD  . GLN A 126 ? 0.38885 0.31597 0.55499 -0.00968 -0.07494 0.06556  126 GLN A CD  
964  O OE1 . GLN A 126 ? 0.37485 0.29639 0.54458 -0.00858 -0.06957 0.06055  126 GLN A OE1 
965  N NE2 . GLN A 126 ? 0.37805 0.31634 0.54283 -0.01063 -0.07537 0.06252  126 GLN A NE2 
966  N N   . PRO A 127 ? 0.47576 0.36220 0.61251 -0.02078 -0.08258 0.09259  127 PRO A N   
967  C CA  . PRO A 127 ? 0.46226 0.34040 0.59174 -0.02712 -0.07665 0.09325  127 PRO A CA  
968  C C   . PRO A 127 ? 0.41928 0.30317 0.55511 -0.02867 -0.06933 0.08371  127 PRO A C   
969  O O   . PRO A 127 ? 0.42341 0.31901 0.56183 -0.02754 -0.06709 0.07703  127 PRO A O   
970  C CB  . PRO A 127 ? 0.44885 0.32750 0.56013 -0.03419 -0.07568 0.09827  127 PRO A CB  
971  C CG  . PRO A 127 ? 0.45733 0.34773 0.56622 -0.03251 -0.07846 0.09541  127 PRO A CG  
972  C CD  . PRO A 127 ? 0.47382 0.36742 0.59798 -0.02429 -0.08566 0.09507  127 PRO A CD  
973  N N   . PHE A 128 ? 0.42663 0.30102 0.56432 -0.03187 -0.06639 0.08364  128 PHE A N   
974  C CA  . PHE A 128 ? 0.39954 0.27671 0.54316 -0.03416 -0.06170 0.07572  128 PHE A CA  
975  C C   . PHE A 128 ? 0.40078 0.29068 0.54142 -0.03905 -0.05691 0.07273  128 PHE A C   
976  O O   . PHE A 128 ? 0.41079 0.30018 0.54675 -0.04544 -0.05332 0.07678  128 PHE A O   
977  C CB  . PHE A 128 ? 0.39975 0.26350 0.54460 -0.03864 -0.06077 0.07771  128 PHE A CB  
978  C CG  . PHE A 128 ? 0.41336 0.26266 0.56249 -0.03344 -0.06380 0.07798  128 PHE A CG  
979  C CD1 . PHE A 128 ? 0.40490 0.25254 0.56020 -0.02850 -0.06311 0.06992  128 PHE A CD1 
980  C CD2 . PHE A 128 ? 0.41565 0.25133 0.56160 -0.03340 -0.06656 0.08631  128 PHE A CD2 
981  C CE1 . PHE A 128 ? 0.41323 0.24601 0.57224 -0.02328 -0.06401 0.06961  128 PHE A CE1 
982  C CE2 . PHE A 128 ? 0.43982 0.26106 0.59076 -0.02786 -0.06853 0.08650  128 PHE A CE2 
983  C CZ  . PHE A 128 ? 0.42979 0.24958 0.58766 -0.02265 -0.06669 0.07784  128 PHE A CZ  
984  N N   . HIS A 129 ? 0.41072 0.31125 0.55476 -0.03607 -0.05588 0.06572  129 HIS A N   
985  C CA  . HIS A 129 ? 0.39335 0.30548 0.53573 -0.03943 -0.05123 0.06265  129 HIS A CA  
986  C C   . HIS A 129 ? 0.37756 0.29366 0.52793 -0.03941 -0.04992 0.05509  129 HIS A C   
987  O O   . HIS A 129 ? 0.37411 0.28403 0.52820 -0.03637 -0.05241 0.05108  129 HIS A O   
988  C CB  . HIS A 129 ? 0.37561 0.29617 0.51198 -0.03662 -0.05176 0.06182  129 HIS A CB  
989  C CG  . HIS A 129 ? 0.36708 0.29057 0.50927 -0.03024 -0.05488 0.05682  129 HIS A CG  
990  N ND1 . HIS A 129 ? 0.37465 0.29306 0.52038 -0.02539 -0.05982 0.05955  129 HIS A ND1 
991  C CD2 . HIS A 129 ? 0.38608 0.31653 0.53218 -0.02791 -0.05305 0.04951  129 HIS A CD2 
992  C CE1 . HIS A 129 ? 0.37827 0.30127 0.53089 -0.02047 -0.05985 0.05385  129 HIS A CE1 
993  N NE2 . HIS A 129 ? 0.37447 0.30405 0.52587 -0.02222 -0.05580 0.04768  129 HIS A NE2 
994  N N   . ARG A 130 ? 0.38110 0.30636 0.53331 -0.04285 -0.04582 0.05339  130 ARG A N   
995  C CA  . ARG A 130 ? 0.40038 0.33163 0.55854 -0.04205 -0.04567 0.04666  130 ARG A CA  
996  C C   . ARG A 130 ? 0.41293 0.35323 0.56703 -0.03839 -0.04378 0.04324  130 ARG A C   
997  O O   . ARG A 130 ? 0.42858 0.37253 0.57611 -0.03883 -0.04118 0.04614  130 ARG A O   
998  C CB  . ARG A 130 ? 0.39740 0.33357 0.56409 -0.04779 -0.04316 0.04742  130 ARG A CB  
999  C CG  . ARG A 130 ? 0.35789 0.28523 0.53049 -0.05198 -0.04680 0.04838  130 ARG A CG  
1000 C CD  . ARG A 130 ? 0.37796 0.31219 0.56228 -0.05855 -0.04431 0.05088  130 ARG A CD  
1001 N NE  . ARG A 130 ? 0.37870 0.30445 0.56929 -0.06377 -0.04916 0.05141  130 ARG A NE  
1002 C CZ  . ARG A 130 ? 0.38115 0.31139 0.58469 -0.07074 -0.04836 0.05448  130 ARG A CZ  
1003 N NH1 . ARG A 130 ? 0.38052 0.32364 0.59315 -0.07281 -0.04130 0.05759  130 ARG A NH1 
1004 N NH2 . ARG A 130 ? 0.36864 0.28979 0.57665 -0.07601 -0.05434 0.05425  130 ARG A NH2 
1005 N N   . ASP A 131 ? 0.38229 0.32427 0.53822 -0.03529 -0.04512 0.03704  131 ASP A N   
1006 C CA  . ASP A 131 ? 0.38065 0.33026 0.53292 -0.03236 -0.04313 0.03367  131 ASP A CA  
1007 C C   . ASP A 131 ? 0.42858 0.38659 0.58314 -0.03457 -0.03891 0.03268  131 ASP A C   
1008 O O   . ASP A 131 ? 0.42453 0.38689 0.57834 -0.03236 -0.03788 0.02828  131 ASP A O   
1009 C CB  . ASP A 131 ? 0.36058 0.30757 0.51277 -0.02831 -0.04497 0.02774  131 ASP A CB  
1010 C CG  . ASP A 131 ? 0.34983 0.29142 0.50163 -0.02445 -0.04690 0.02835  131 ASP A CG  
1011 O OD1 . ASP A 131 ? 0.36654 0.30705 0.51778 -0.02452 -0.04840 0.03382  131 ASP A OD1 
1012 O OD2 . ASP A 131 ? 0.33574 0.27365 0.48801 -0.02121 -0.04668 0.02362  131 ASP A OD2 
1013 N N   . ASP A 132 ? 0.58212 0.54203 0.74030 -0.03875 -0.03567 0.03693  132 ASP A N   
1014 C CA  . ASP A 132 ? 0.56779 0.53597 0.73163 -0.04046 -0.03005 0.03670  132 ASP A CA  
1015 C C   . ASP A 132 ? 0.58265 0.55240 0.73746 -0.04178 -0.02305 0.03954  132 ASP A C   
1016 O O   . ASP A 132 ? 0.60284 0.57568 0.76176 -0.04496 -0.01622 0.04230  132 ASP A O   
1017 C CB  . ASP A 132 ? 0.55936 0.52947 0.73721 -0.04462 -0.03034 0.03900  132 ASP A CB  
1018 C CG  . ASP A 132 ? 0.58447 0.55037 0.76293 -0.04947 -0.02795 0.04521  132 ASP A CG  
1019 O OD1 . ASP A 132 ? 0.62513 0.58628 0.79174 -0.04969 -0.02555 0.04844  132 ASP A OD1 
1020 O OD2 . ASP A 132 ? 0.58231 0.54905 0.77318 -0.05370 -0.02907 0.04725  132 ASP A OD2 
1021 N N   . ALA A 133 ? 0.44968 0.41657 0.59175 -0.03979 -0.02454 0.03893  133 ALA A N   
1022 C CA  . ALA A 133 ? 0.40728 0.37253 0.53578 -0.04179 -0.01947 0.04123  133 ALA A CA  
1023 C C   . ALA A 133 ? 0.35709 0.32568 0.47898 -0.03978 -0.01652 0.03638  133 ALA A C   
1024 O O   . ALA A 133 ? 0.35616 0.32382 0.46932 -0.04187 -0.00906 0.03666  133 ALA A O   
1025 C CB  . ALA A 133 ? 0.41261 0.37044 0.52992 -0.04245 -0.02510 0.04565  133 ALA A CB  
1026 N N   . THR A 134 ? 0.33005 0.30098 0.45477 -0.03607 -0.02131 0.03178  134 THR A N   
1027 C CA  . THR A 134 ? 0.31299 0.28624 0.43209 -0.03455 -0.01842 0.02705  134 THR A CA  
1028 C C   . THR A 134 ? 0.28935 0.26661 0.41537 -0.03416 -0.01087 0.02512  134 THR A C   
1029 O O   . THR A 134 ? 0.28182 0.25840 0.40017 -0.03437 -0.00445 0.02306  134 THR A O   
1030 C CB  . THR A 134 ? 0.31209 0.28661 0.43458 -0.03105 -0.02413 0.02287  134 THR A CB  
1031 O OG1 . THR A 134 ? 0.32955 0.30158 0.44950 -0.03074 -0.03035 0.02511  134 THR A OG1 
1032 C CG2 . THR A 134 ? 0.27300 0.24881 0.38917 -0.03009 -0.02121 0.01814  134 THR A CG2 
1033 N N   . HIS A 135 ? 0.30592 0.28680 0.44703 -0.03366 -0.01185 0.02589  135 HIS A N   
1034 C CA  . HIS A 135 ? 0.28299 0.26947 0.43623 -0.03312 -0.00593 0.02551  135 HIS A CA  
1035 C C   . HIS A 135 ? 0.29795 0.28662 0.46209 -0.03663 -0.00336 0.03054  135 HIS A C   
1036 O O   . HIS A 135 ? 0.28976 0.28086 0.46726 -0.03731 -0.00896 0.03166  135 HIS A O   
1037 C CB  . HIS A 135 ? 0.24918 0.23850 0.41212 -0.02984 -0.01127 0.02214  135 HIS A CB  
1038 C CG  . HIS A 135 ? 0.23696 0.22327 0.38938 -0.02699 -0.01319 0.01744  135 HIS A CG  
1039 N ND1 . HIS A 135 ? 0.25291 0.23514 0.39850 -0.02640 -0.01941 0.01578  135 HIS A ND1 
1040 C CD2 . HIS A 135 ? 0.21742 0.20380 0.36595 -0.02471 -0.00897 0.01413  135 HIS A CD2 
1041 C CE1 . HIS A 135 ? 0.24081 0.22166 0.37940 -0.02442 -0.01892 0.01179  135 HIS A CE1 
1042 N NE2 . HIS A 135 ? 0.21430 0.19694 0.35346 -0.02354 -0.01302 0.01070  135 HIS A NE2 
1043 N N   . PRO A 136 ? 0.29886 0.28551 0.45656 -0.03967 0.00527  0.03365  136 PRO A N   
1044 C CA  . PRO A 136 ? 0.31747 0.30503 0.48439 -0.04395 0.00852  0.03900  136 PRO A CA  
1045 C C   . PRO A 136 ? 0.30930 0.30663 0.50143 -0.04414 0.01020  0.03998  136 PRO A C   
1046 O O   . PRO A 136 ? 0.30542 0.30425 0.50855 -0.04824 0.01019  0.04425  136 PRO A O   
1047 C CB  . PRO A 136 ? 0.32447 0.30659 0.47645 -0.04686 0.01989  0.04116  136 PRO A CB  
1048 C CG  . PRO A 136 ? 0.33531 0.31063 0.46546 -0.04529 0.01702  0.03797  136 PRO A CG  
1049 C CD  . PRO A 136 ? 0.31211 0.29276 0.44993 -0.04036 0.01161  0.03259  136 PRO A CD  
1050 N N   . LEU A 137 ? 0.28862 0.29242 0.49116 -0.04011 0.01085  0.03666  137 LEU A N   
1051 C CA  . LEU A 137 ? 0.26878 0.28273 0.49764 -0.04009 0.00983  0.03832  137 LEU A CA  
1052 C C   . LEU A 137 ? 0.25654 0.27025 0.49367 -0.04219 -0.00358 0.03915  137 LEU A C   
1053 O O   . LEU A 137 ? 0.25298 0.27420 0.51179 -0.04437 -0.00647 0.04177  137 LEU A O   
1054 C CB  . LEU A 137 ? 0.26022 0.27933 0.49676 -0.03458 0.01186  0.03501  137 LEU A CB  
1055 C CG  . LEU A 137 ? 0.24461 0.25976 0.47170 -0.03048 0.00256  0.03035  137 LEU A CG  
1056 C CD1 . LEU A 137 ? 0.22624 0.24315 0.46470 -0.03117 -0.01064 0.03089  137 LEU A CD1 
1057 C CD2 . LEU A 137 ? 0.21710 0.23418 0.44608 -0.02537 0.00907  0.02757  137 LEU A CD2 
1058 N N   . MET A 138 ? 0.28569 0.29044 0.50649 -0.04179 -0.01169 0.03692  138 MET A N   
1059 C CA  . MET A 138 ? 0.29538 0.29634 0.52002 -0.04378 -0.02325 0.03674  138 MET A CA  
1060 C C   . MET A 138 ? 0.27921 0.27916 0.51241 -0.04982 -0.02397 0.04150  138 MET A C   
1061 O O   . MET A 138 ? 0.27400 0.27280 0.51645 -0.05281 -0.03267 0.04191  138 MET A O   
1062 C CB  . MET A 138 ? 0.31620 0.30694 0.52169 -0.04137 -0.02889 0.03309  138 MET A CB  
1063 C CG  . MET A 138 ? 0.28443 0.27384 0.48580 -0.03735 -0.03384 0.02822  138 MET A CG  
1064 S SD  . MET A 138 ? 0.36120 0.34118 0.54209 -0.03419 -0.03547 0.02430  138 MET A SD  
1065 C CE  . MET A 138 ? 0.32526 0.29633 0.50455 -0.03738 -0.04060 0.02653  138 MET A CE  
1066 N N   . HIS A 139 ? 0.30196 0.30008 0.52955 -0.05229 -0.01555 0.04511  139 HIS A N   
1067 C CA  . HIS A 139 ? 0.31151 0.30782 0.54690 -0.05859 -0.01480 0.05025  139 HIS A CA  
1068 C C   . HIS A 139 ? 0.28979 0.29716 0.55206 -0.06210 -0.01525 0.05252  139 HIS A C   
1069 O O   . HIS A 139 ? 0.27739 0.28305 0.54955 -0.06764 -0.02100 0.05512  139 HIS A O   
1070 C CB  . HIS A 139 ? 0.30583 0.29855 0.53007 -0.06075 -0.00355 0.05422  139 HIS A CB  
1071 C CG  . HIS A 139 ? 0.32578 0.31491 0.55558 -0.06764 -0.00108 0.06014  139 HIS A CG  
1072 N ND1 . HIS A 139 ? 0.33523 0.31489 0.56173 -0.07049 -0.00983 0.06164  139 HIS A ND1 
1073 C CD2 . HIS A 139 ? 0.32041 0.31264 0.55765 -0.07242 0.01037  0.06497  139 HIS A CD2 
1074 C CE1 . HIS A 139 ? 0.32838 0.30567 0.56047 -0.07699 -0.00490 0.06732  139 HIS A CE1 
1075 N NE2 . HIS A 139 ? 0.34708 0.33225 0.58587 -0.07847 0.00764  0.06955  139 HIS A NE2 
1076 N N   . TYR A 140 ? 0.26897 0.28741 0.54432 -0.05884 -0.01035 0.05151  140 TYR A N   
1077 C CA  . TYR A 140 ? 0.24172 0.27360 0.54692 -0.06149 -0.00798 0.05489  140 TYR A CA  
1078 C C   . TYR A 140 ? 0.24181 0.27877 0.56272 -0.06124 -0.02192 0.05366  140 TYR A C   
1079 O O   . TYR A 140 ? 0.25953 0.30829 0.60838 -0.06430 -0.02320 0.05726  140 TYR A O   
1080 C CB  . TYR A 140 ? 0.24177 0.28241 0.55465 -0.05750 0.00651  0.05505  140 TYR A CB  
1081 C CG  . TYR A 140 ? 0.23982 0.27382 0.53474 -0.05850 0.02127  0.05625  140 TYR A CG  
1082 C CD1 . TYR A 140 ? 0.26093 0.29751 0.56622 -0.06418 0.03218  0.06142  140 TYR A CD1 
1083 C CD2 . TYR A 140 ? 0.26510 0.28953 0.53232 -0.05447 0.02374  0.05242  140 TYR A CD2 
1084 C CE1 . TYR A 140 ? 0.27300 0.30073 0.55777 -0.06562 0.04528  0.06263  140 TYR A CE1 
1085 C CE2 . TYR A 140 ? 0.28215 0.29880 0.53070 -0.05630 0.03547  0.05382  140 TYR A CE2 
1086 C CZ  . TYR A 140 ? 0.28402 0.30107 0.53904 -0.06185 0.04656  0.05892  140 TYR A CZ  
1087 O OH  . TYR A 140 ? 0.34403 0.35069 0.57662 -0.06422 0.05798  0.06044  140 TYR A OH  
1088 N N   . GLN A 141 ? 0.26884 0.29720 0.57317 -0.05799 -0.03219 0.04904  141 GLN A N   
1089 C CA  . GLN A 141 ? 0.26272 0.29174 0.57647 -0.05912 -0.04668 0.04812  141 GLN A CA  
1090 C C   . GLN A 141 ? 0.27000 0.29403 0.58925 -0.06729 -0.05551 0.05047  141 GLN A C   
1091 O O   . GLN A 141 ? 0.26241 0.27456 0.56469 -0.06960 -0.05480 0.04980  141 GLN A O   
1092 C CB  . GLN A 141 ? 0.27076 0.28847 0.56116 -0.05444 -0.05387 0.04240  141 GLN A CB  
1093 C CG  . GLN A 141 ? 0.27405 0.29432 0.55642 -0.04707 -0.04611 0.03959  141 GLN A CG  
1094 C CD  . GLN A 141 ? 0.27766 0.30314 0.57062 -0.04357 -0.05253 0.03901  141 GLN A CD  
1095 O OE1 . GLN A 141 ? 0.30239 0.32039 0.58846 -0.04444 -0.06495 0.03717  141 GLN A OE1 
1096 N NE2 . GLN A 141 ? 0.24590 0.28258 0.55448 -0.03955 -0.04381 0.04070  141 GLN A NE2 
1097 N N   . PRO A 142 ? 0.27878 0.31115 0.62212 -0.07201 -0.06418 0.05356  142 PRO A N   
1098 C CA  . PRO A 142 ? 0.28978 0.31419 0.63379 -0.08018 -0.07493 0.05467  142 PRO A CA  
1099 C C   . PRO A 142 ? 0.31181 0.31664 0.62762 -0.07993 -0.08499 0.04913  142 PRO A C   
1100 O O   . PRO A 142 ? 0.32088 0.32149 0.62289 -0.07416 -0.08807 0.04504  142 PRO A O   
1101 C CB  . PRO A 142 ? 0.28206 0.31788 0.64742 -0.08105 -0.08349 0.05746  142 PRO A CB  
1102 C CG  . PRO A 142 ? 0.23766 0.29130 0.62586 -0.07598 -0.07262 0.06028  142 PRO A CG  
1103 C CD  . PRO A 142 ? 0.25273 0.30233 0.62498 -0.07005 -0.06419 0.05662  142 PRO A CD  
1104 N N   . LEU A 143 ? 0.30791 0.29948 0.61194 -0.08505 -0.08823 0.04869  143 LEU A N   
1105 C CA  . LEU A 143 ? 0.34069 0.31183 0.61860 -0.08501 -0.09616 0.04319  143 LEU A CA  
1106 C C   . LEU A 143 ? 0.35673 0.32428 0.62905 -0.08417 -0.10845 0.04005  143 LEU A C   
1107 O O   . LEU A 143 ? 0.38234 0.33675 0.63351 -0.08094 -0.11107 0.03488  143 LEU A O   
1108 C CB  . LEU A 143 ? 0.37097 0.32903 0.63975 -0.09073 -0.09907 0.04338  143 LEU A CB  
1109 C CG  . LEU A 143 ? 0.37078 0.30630 0.61252 -0.09050 -0.10629 0.03719  143 LEU A CG  
1110 C CD1 . LEU A 143 ? 0.36416 0.29213 0.59086 -0.08393 -0.09877 0.03399  143 LEU A CD1 
1111 C CD2 . LEU A 143 ? 0.36480 0.28647 0.59781 -0.09623 -0.10917 0.03701  143 LEU A CD2 
1112 N N   . GLU A 144 ? 0.36460 0.34346 0.65486 -0.08644 -0.11551 0.04347  144 GLU A N   
1113 C CA  . GLU A 144 ? 0.36002 0.33257 0.64273 -0.08699 -0.12990 0.04162  144 GLU A CA  
1114 C C   . GLU A 144 ? 0.36694 0.34687 0.65403 -0.08081 -0.13014 0.04107  144 GLU A C   
1115 O O   . GLU A 144 ? 0.38154 0.35108 0.65443 -0.08070 -0.14112 0.03862  144 GLU A O   
1116 C CB  . GLU A 144 ? 0.39750 0.37773 0.69767 -0.09230 -0.13904 0.04626  144 GLU A CB  
1117 C CG  . GLU A 144 ? 0.42142 0.40121 0.72699 -0.09822 -0.13484 0.04839  144 GLU A CG  
1118 C CD  . GLU A 144 ? 0.39955 0.40057 0.73531 -0.09794 -0.12388 0.05429  144 GLU A CD  
1119 O OE1 . GLU A 144 ? 0.43050 0.44642 0.79002 -0.09795 -0.12772 0.05855  144 GLU A OE1 
1120 O OE2 . GLU A 144 ? 0.40415 0.40594 0.73933 -0.09763 -0.11121 0.05488  144 GLU A OE2 
1121 N N   . ALA A 145 ? 0.36114 0.35630 0.66475 -0.07624 -0.11795 0.04310  145 ALA A N   
1122 C CA  . ALA A 145 ? 0.33038 0.33205 0.63488 -0.06853 -0.11532 0.04227  145 ALA A CA  
1123 C C   . ALA A 145 ? 0.32282 0.30642 0.59326 -0.06425 -0.11603 0.03579  145 ALA A C   
1124 O O   . ALA A 145 ? 0.34234 0.31135 0.59158 -0.06571 -0.11400 0.03197  145 ALA A O   
1125 C CB  . ALA A 145 ? 0.29433 0.31114 0.61235 -0.06296 -0.09816 0.04429  145 ALA A CB  
1126 N N   . PRO A 146 ? 0.32254 0.30644 0.58827 -0.05885 -0.11826 0.03468  146 PRO A N   
1127 C CA  . PRO A 146 ? 0.32307 0.29032 0.55766 -0.05514 -0.11726 0.02874  146 PRO A CA  
1128 C C   . PRO A 146 ? 0.29138 0.25793 0.51476 -0.05082 -0.10237 0.02567  146 PRO A C   
1129 O O   . PRO A 146 ? 0.27659 0.25661 0.51262 -0.04709 -0.09168 0.02765  146 PRO A O   
1130 C CB  . PRO A 146 ? 0.31573 0.28749 0.55363 -0.04980 -0.11992 0.02973  146 PRO A CB  
1131 C CG  . PRO A 146 ? 0.30987 0.29701 0.57909 -0.05191 -0.12765 0.03616  146 PRO A CG  
1132 C CD  . PRO A 146 ? 0.31405 0.31346 0.60357 -0.05522 -0.12007 0.03900  146 PRO A CD  
1133 N N   . PRO A 147 ? 0.28662 0.23723 0.48680 -0.05143 -0.10128 0.02105  147 PRO A N   
1134 C CA  . PRO A 147 ? 0.28541 0.23611 0.47722 -0.04740 -0.08895 0.01894  147 PRO A CA  
1135 C C   . PRO A 147 ? 0.27134 0.22512 0.45593 -0.04085 -0.08210 0.01661  147 PRO A C   
1136 O O   . PRO A 147 ? 0.26512 0.21344 0.44137 -0.03923 -0.08663 0.01475  147 PRO A O   
1137 C CB  . PRO A 147 ? 0.29205 0.22409 0.46362 -0.04948 -0.09095 0.01477  147 PRO A CB  
1138 C CG  . PRO A 147 ? 0.31636 0.23527 0.47650 -0.05284 -0.10233 0.01263  147 PRO A CG  
1139 C CD  . PRO A 147 ? 0.31033 0.24140 0.49172 -0.05622 -0.11117 0.01779  147 PRO A CD  
1140 N N   . VAL A 148 ? 0.25056 0.21187 0.43714 -0.03769 -0.07149 0.01696  148 VAL A N   
1141 C CA  . VAL A 148 ? 0.24719 0.21205 0.42807 -0.03240 -0.06437 0.01492  148 VAL A CA  
1142 C C   . VAL A 148 ? 0.24374 0.20354 0.41069 -0.03024 -0.05789 0.01191  148 VAL A C   
1143 O O   . VAL A 148 ? 0.24063 0.20272 0.40209 -0.02678 -0.05233 0.00999  148 VAL A O   
1144 C CB  . VAL A 148 ? 0.22695 0.20640 0.42427 -0.03063 -0.05765 0.01833  148 VAL A CB  
1145 C CG1 . VAL A 148 ? 0.23099 0.21717 0.44585 -0.03125 -0.06390 0.02151  148 VAL A CG1 
1146 C CG2 . VAL A 148 ? 0.22332 0.20841 0.42782 -0.03308 -0.05165 0.02144  148 VAL A CG2 
1147 N N   . SER A 149 ? 0.25258 0.20544 0.41488 -0.03223 -0.05879 0.01167  149 SER A N   
1148 C CA  . SER A 149 ? 0.26719 0.21648 0.42026 -0.02973 -0.05356 0.00973  149 SER A CA  
1149 C C   . SER A 149 ? 0.27415 0.20960 0.41837 -0.03068 -0.05650 0.00730  149 SER A C   
1150 O O   . SER A 149 ? 0.28782 0.21735 0.43416 -0.03448 -0.06165 0.00845  149 SER A O   
1151 C CB  . SER A 149 ? 0.25628 0.21341 0.41548 -0.03000 -0.04856 0.01362  149 SER A CB  
1152 O OG  . SER A 149 ? 0.25093 0.20697 0.40263 -0.02709 -0.04479 0.01216  149 SER A OG  
1153 N N   . LEU A 150 ? 0.26913 0.19912 0.40422 -0.02735 -0.05257 0.00386  150 LEU A N   
1154 C CA  . LEU A 150 ? 0.28139 0.19758 0.40866 -0.02702 -0.05254 0.00111  150 LEU A CA  
1155 C C   . LEU A 150 ? 0.27554 0.19416 0.40374 -0.02277 -0.04649 0.00062  150 LEU A C   
1156 O O   . LEU A 150 ? 0.25682 0.18190 0.38429 -0.02040 -0.04289 -0.00073 150 LEU A O   
1157 C CB  . LEU A 150 ? 0.26925 0.17155 0.38249 -0.02774 -0.05449 -0.00388 150 LEU A CB  
1158 C CG  . LEU A 150 ? 0.29464 0.17902 0.39729 -0.02794 -0.05329 -0.00752 150 LEU A CG  
1159 C CD1 . LEU A 150 ? 0.28724 0.16429 0.39164 -0.03253 -0.05939 -0.00559 150 LEU A CD1 
1160 C CD2 . LEU A 150 ? 0.30995 0.17945 0.39465 -0.02842 -0.05274 -0.01288 150 LEU A CD2 
1161 N N   . SER A 151 ? 0.26673 0.17984 0.39743 -0.02195 -0.04591 0.00197  151 SER A N   
1162 C CA  . SER A 151 ? 0.27334 0.18955 0.40862 -0.01767 -0.04175 0.00272  151 SER A CA  
1163 C C   . SER A 151 ? 0.28791 0.19087 0.41816 -0.01473 -0.03775 -0.00192 151 SER A C   
1164 O O   . SER A 151 ? 0.30461 0.19341 0.42935 -0.01606 -0.03878 -0.00353 151 SER A O   
1165 C CB  . SER A 151 ? 0.27969 0.19918 0.42275 -0.01799 -0.04368 0.00864  151 SER A CB  
1166 O OG  . SER A 151 ? 0.29467 0.22427 0.44052 -0.02120 -0.04549 0.01254  151 SER A OG  
1167 N N   . VAL A 152 ? 0.28126 0.18801 0.41340 -0.01112 -0.03251 -0.00424 152 VAL A N   
1168 C CA  . VAL A 152 ? 0.28490 0.18020 0.41427 -0.00778 -0.02598 -0.00879 152 VAL A CA  
1169 C C   . VAL A 152 ? 0.28217 0.18586 0.42712 -0.00289 -0.02306 -0.00593 152 VAL A C   
1170 O O   . VAL A 152 ? 0.26397 0.18200 0.41682 -0.00215 -0.02340 -0.00389 152 VAL A O   
1171 C CB  . VAL A 152 ? 0.29407 0.18529 0.41288 -0.00821 -0.02126 -0.01418 152 VAL A CB  
1172 C CG1 . VAL A 152 ? 0.29642 0.17589 0.41336 -0.00462 -0.01197 -0.01879 152 VAL A CG1 
1173 C CG2 . VAL A 152 ? 0.28947 0.17130 0.39286 -0.01296 -0.02614 -0.01614 152 VAL A CG2 
1174 N N   . ILE A 153 ? 0.28777 0.18177 0.43732 0.00033  -0.02071 -0.00568 153 ILE A N   
1175 C CA  . ILE A 153 ? 0.27821 0.17965 0.44514 0.00518  -0.02062 -0.00100 153 ILE A CA  
1176 C C   . ILE A 153 ? 0.28718 0.18195 0.46090 0.01066  -0.01103 -0.00512 153 ILE A C   
1177 O O   . ILE A 153 ? 0.30348 0.18013 0.46882 0.01172  -0.00553 -0.00951 153 ILE A O   
1178 C CB  . ILE A 153 ? 0.28500 0.18072 0.45432 0.00496  -0.02596 0.00415  153 ILE A CB  
1179 C CG1 . ILE A 153 ? 0.29188 0.19662 0.45737 -0.00038 -0.03368 0.00898  153 ILE A CG1 
1180 C CG2 . ILE A 153 ? 0.27960 0.17906 0.46627 0.01091  -0.02595 0.00905  153 ILE A CG2 
1181 C CD1 . ILE A 153 ? 0.29287 0.19126 0.44499 -0.00613 -0.03558 0.00606  153 ILE A CD1 
1182 N N   . PHE A 154 ? 0.29574 0.20447 0.48444 0.01367  -0.00855 -0.00391 154 PHE A N   
1183 C CA  . PHE A 154 ? 0.29956 0.20516 0.49752 0.01844  0.00234  -0.00801 154 PHE A CA  
1184 C C   . PHE A 154 ? 0.30562 0.21684 0.52796 0.02519  0.00283  -0.00315 154 PHE A C   
1185 O O   . PHE A 154 ? 0.29114 0.21995 0.52980 0.02595  -0.00394 0.00283  154 PHE A O   
1186 C CB  . PHE A 154 ? 0.29819 0.21587 0.49850 0.01661  0.00553  -0.01020 154 PHE A CB  
1187 C CG  . PHE A 154 ? 0.29525 0.20193 0.47315 0.01230  0.00991  -0.01653 154 PHE A CG  
1188 C CD1 . PHE A 154 ? 0.30498 0.19427 0.47287 0.01364  0.02109  -0.02290 154 PHE A CD1 
1189 C CD2 . PHE A 154 ? 0.27922 0.19135 0.44506 0.00698  0.00308  -0.01593 154 PHE A CD2 
1190 C CE1 . PHE A 154 ? 0.33130 0.20846 0.47586 0.00920  0.02388  -0.02809 154 PHE A CE1 
1191 C CE2 . PHE A 154 ? 0.29542 0.19696 0.44134 0.00338  0.00583  -0.02087 154 PHE A CE2 
1192 C CZ  . PHE A 154 ? 0.30362 0.18741 0.43797 0.00421  0.01546  -0.02671 154 PHE A CZ  
1193 N N   . PRO A 155 ? 0.32779 0.22381 0.55326 0.03019  0.01028  -0.00532 155 PRO A N   
1194 C CA  . PRO A 155 ? 0.33110 0.23294 0.58406 0.03814  0.01280  -0.00100 155 PRO A CA  
1195 C C   . PRO A 155 ? 0.31415 0.22808 0.58572 0.04123  0.02169  -0.00312 155 PRO A C   
1196 O O   . PRO A 155 ? 0.32994 0.23343 0.59325 0.04136  0.03463  -0.01057 155 PRO A O   
1197 C CB  . PRO A 155 ? 0.35633 0.23443 0.60303 0.04214  0.02081  -0.00458 155 PRO A CB  
1198 C CG  . PRO A 155 ? 0.36184 0.22215 0.57840 0.03627  0.02648  -0.01317 155 PRO A CG  
1199 C CD  . PRO A 155 ? 0.33032 0.20181 0.53386 0.02858  0.01590  -0.01153 155 PRO A CD  
1200 N N   . LEU A 156 ? 0.28438 0.21968 0.58017 0.04293  0.01444  0.00363  156 LEU A N   
1201 C CA  . LEU A 156 ? 0.28089 0.22981 0.60155 0.04626  0.02207  0.00299  156 LEU A CA  
1202 C C   . LEU A 156 ? 0.29673 0.24854 0.64933 0.05577  0.02607  0.00716  156 LEU A C   
1203 O O   . LEU A 156 ? 0.31604 0.27677 0.69261 0.05974  0.03587  0.00587  156 LEU A O   
1204 C CB  . LEU A 156 ? 0.26421 0.23546 0.59286 0.04117  0.01141  0.00732  156 LEU A CB  
1205 C CG  . LEU A 156 ? 0.26261 0.23281 0.56843 0.03360  0.01445  0.00118  156 LEU A CG  
1206 C CD1 . LEU A 156 ? 0.24190 0.22875 0.54755 0.02770  0.00170  0.00558  156 LEU A CD1 
1207 C CD2 . LEU A 156 ? 0.27352 0.24296 0.58686 0.03478  0.02989  -0.00497 156 LEU A CD2 
1208 N N   . THR A 157 ? 0.31527 0.25997 0.67015 0.05950  0.01899  0.01247  157 THR A N   
1209 C CA  . THR A 157 ? 0.32491 0.26386 0.70386 0.06944  0.02495  0.01514  157 THR A CA  
1210 C C   . THR A 157 ? 0.36003 0.27132 0.71474 0.07017  0.03008  0.01084  157 THR A C   
1211 O O   . THR A 157 ? 0.36197 0.26225 0.68508 0.06267  0.02716  0.00686  157 THR A O   
1212 C CB  . THR A 157 ? 0.30553 0.26053 0.71030 0.07312  0.00943  0.02700  157 THR A CB  
1213 O OG1 . THR A 157 ? 0.31421 0.26388 0.69626 0.06767  -0.00477 0.03156  157 THR A OG1 
1214 C CG2 . THR A 157 ? 0.26561 0.24697 0.69209 0.07076  0.00246  0.03109  157 THR A CG2 
1215 N N   . GLU A 158 ? 0.36668 0.26805 0.73256 0.07754  0.03718  0.01155  158 GLU A N   
1216 C CA  . GLU A 158 ? 0.38208 0.25809 0.72243 0.07666  0.03917  0.00845  158 GLU A CA  
1217 C C   . GLU A 158 ? 0.37462 0.25144 0.71046 0.07411  0.02161  0.01703  158 GLU A C   
1218 O O   . GLU A 158 ? 0.34583 0.24074 0.70165 0.07586  0.00956  0.02651  158 GLU A O   
1219 C CB  . GLU A 158 ? 0.40081 0.26582 0.74818 0.08382  0.05163  0.00648  158 GLU A CB  
1220 C CG  . GLU A 158 ? 0.41189 0.29286 0.79090 0.09066  0.04498  0.01632  158 GLU A CG  
1221 C CD  . GLU A 158 ? 0.47246 0.33748 0.85315 0.09736  0.05428  0.01529  158 GLU A CD  
1222 O OE1 . GLU A 158 ? 0.49652 0.33612 0.84972 0.09577  0.06362  0.00731  158 GLU A OE1 
1223 O OE2 . GLU A 158 ? 0.46206 0.33925 0.87087 0.10389  0.05153  0.02255  158 GLU A OE2 
1224 N N   . PHE A 159 ? 0.41577 0.27262 0.72337 0.06872  0.01974  0.01374  159 PHE A N   
1225 C CA  . PHE A 159 ? 0.38980 0.24328 0.68965 0.06540  0.00571  0.02116  159 PHE A CA  
1226 C C   . PHE A 159 ? 0.40148 0.23720 0.69687 0.06938  0.00933  0.02183  159 PHE A C   
1227 O O   . PHE A 159 ? 0.41753 0.23377 0.69770 0.06982  0.02118  0.01346  159 PHE A O   
1228 C CB  . PHE A 159 ? 0.38834 0.23612 0.65741 0.05453  0.00066  0.01744  159 PHE A CB  
1229 C CG  . PHE A 159 ? 0.37147 0.24065 0.63700 0.04831  -0.00596 0.01829  159 PHE A CG  
1230 C CD1 . PHE A 159 ? 0.34422 0.23470 0.63123 0.05144  -0.00758 0.02168  159 PHE A CD1 
1231 C CD2 . PHE A 159 ? 0.36507 0.23249 0.60650 0.03912  -0.01074 0.01581  159 PHE A CD2 
1232 C CE1 . PHE A 159 ? 0.33291 0.24016 0.61432 0.04524  -0.01328 0.02190  159 PHE A CE1 
1233 C CE2 . PHE A 159 ? 0.33739 0.22228 0.57506 0.03393  -0.01572 0.01627  159 PHE A CE2 
1234 C CZ  . PHE A 159 ? 0.32104 0.22481 0.57716 0.03683  -0.01678 0.01903  159 PHE A CZ  
1235 N N   . THR A 160 ? 0.41177 0.25268 0.71848 0.07202  -0.00098 0.03178  160 THR A N   
1236 C CA  . THR A 160 ? 0.41720 0.24231 0.72275 0.07671  0.00160  0.03370  160 THR A CA  
1237 C C   . THR A 160 ? 0.41902 0.24129 0.71732 0.07280  -0.01261 0.04297  160 THR A C   
1238 O O   . THR A 160 ? 0.39333 0.22875 0.69182 0.06784  -0.02414 0.04887  160 THR A O   
1239 C CB  . THR A 160 ? 0.40928 0.24476 0.74352 0.08681  0.00663  0.03701  160 THR A CB  
1240 O OG1 . THR A 160 ? 0.41574 0.27450 0.77147 0.08788  -0.00676 0.04748  160 THR A OG1 
1241 C CG2 . THR A 160 ? 0.41280 0.25219 0.75528 0.08998  0.02218  0.02819  160 THR A CG2 
1242 N N   . GLU A 161 ? 0.42707 0.23055 0.71748 0.07480  -0.01120 0.04427  161 GLU A N   
1243 C CA  . GLU A 161 ? 0.43762 0.23648 0.72051 0.07101  -0.02337 0.05343  161 GLU A CA  
1244 C C   . GLU A 161 ? 0.42810 0.24668 0.73102 0.07433  -0.03541 0.06518  161 GLU A C   
1245 O O   . GLU A 161 ? 0.44587 0.26730 0.74109 0.06879  -0.04732 0.07311  161 GLU A O   
1246 C CB  . GLU A 161 ? 0.46288 0.23749 0.73577 0.07348  -0.01901 0.05292  161 GLU A CB  
1247 C CG  . GLU A 161 ? 0.51222 0.26308 0.75712 0.06609  -0.01294 0.04388  161 GLU A CG  
1248 C CD  . GLU A 161 ? 0.54964 0.28366 0.77885 0.06055  -0.01942 0.04889  161 GLU A CD  
1249 O OE1 . GLU A 161 ? 0.54240 0.28037 0.78064 0.06328  -0.02741 0.05929  161 GLU A OE1 
1250 O OE2 . GLU A 161 ? 0.55774 0.27411 0.76489 0.05279  -0.01686 0.04260  161 GLU A OE2 
1251 N N   . GLU A 162 ? 0.40968 0.24190 0.73747 0.08253  -0.03259 0.06646  162 GLU A N   
1252 C CA  . GLU A 162 ? 0.41519 0.26570 0.76273 0.08549  -0.04510 0.07765  162 GLU A CA  
1253 C C   . GLU A 162 ? 0.39923 0.27029 0.74961 0.07993  -0.05397 0.07995  162 GLU A C   
1254 O O   . GLU A 162 ? 0.40677 0.28479 0.75403 0.07609  -0.06822 0.08931  162 GLU A O   
1255 C CB  . GLU A 162 ? 0.42834 0.28637 0.80371 0.09573  -0.03874 0.07809  162 GLU A CB  
1256 C CG  . GLU A 162 ? 0.41617 0.28218 0.80907 0.10043  -0.05098 0.09031  162 GLU A CG  
1257 C CD  . GLU A 162 ? 0.43764 0.31186 0.86084 0.11046  -0.04354 0.09020  162 GLU A CD  
1258 O OE1 . GLU A 162 ? 0.45768 0.33284 0.88768 0.11308  -0.02847 0.08065  162 GLU A OE1 
1259 O OE2 . GLU A 162 ? 0.43339 0.31254 0.87322 0.11545  -0.05240 0.09974  162 GLU A OE2 
1260 N N   . ASN A 163 ? 0.38597 0.26539 0.74031 0.07917  -0.04553 0.07149  163 ASN A N   
1261 C CA  . ASN A 163 ? 0.37384 0.27322 0.73358 0.07488  -0.05320 0.07334  163 ASN A CA  
1262 C C   . ASN A 163 ? 0.36765 0.26233 0.70310 0.06566  -0.05927 0.07312  163 ASN A C   
1263 O O   . ASN A 163 ? 0.34897 0.25866 0.68403 0.06114  -0.06679 0.07528  163 ASN A O   
1264 C CB  . ASN A 163 ? 0.36773 0.27779 0.74163 0.07747  -0.04146 0.06474  163 ASN A CB  
1265 C CG  . ASN A 163 ? 0.35267 0.24749 0.70687 0.07447  -0.02815 0.05291  163 ASN A CG  
1266 O OD1 . ASN A 163 ? 0.35820 0.23734 0.68852 0.06900  -0.02946 0.05097  163 ASN A OD1 
1267 N ND2 . ASN A 163 ? 0.34332 0.24253 0.70707 0.07730  -0.01536 0.04506  163 ASN A ND2 
1268 N N   . GLY A 164 ? 0.39610 0.27104 0.71029 0.06193  -0.05547 0.06990  164 GLY A N   
1269 C CA  . GLY A 164 ? 0.39734 0.26983 0.68697 0.05174  -0.06031 0.06964  164 GLY A CA  
1270 C C   . GLY A 164 ? 0.37732 0.24772 0.65029 0.04598  -0.05085 0.05792  164 GLY A C   
1271 O O   . GLY A 164 ? 0.37033 0.25150 0.63040 0.03852  -0.05392 0.05633  164 GLY A O   
1272 N N   . ALA A 165 ? 0.36368 0.21889 0.63572 0.04934  -0.03948 0.04983  165 ALA A N   
1273 C CA  . ALA A 165 ? 0.36420 0.21273 0.61678 0.04327  -0.03197 0.03934  165 ALA A CA  
1274 C C   . ALA A 165 ? 0.37741 0.22543 0.60907 0.03300  -0.03885 0.04073  165 ALA A C   
1275 O O   . ALA A 165 ? 0.38342 0.22398 0.61075 0.03069  -0.04495 0.04736  165 ALA A O   
1276 C CB  . ALA A 165 ? 0.38302 0.20735 0.63076 0.04673  -0.02118 0.03224  165 ALA A CB  
1277 N N   . THR A 166 ? 0.38803 0.24399 0.60786 0.02695  -0.03736 0.03482  166 THR A N   
1278 C CA  . THR A 166 ? 0.37552 0.23512 0.58003 0.01782  -0.04318 0.03641  166 THR A CA  
1279 C C   . THR A 166 ? 0.39375 0.23450 0.58668 0.01334  -0.04361 0.03622  166 THR A C   
1280 O O   . THR A 166 ? 0.40254 0.22650 0.58960 0.01395  -0.03785 0.02970  166 THR A O   
1281 C CB  . THR A 166 ? 0.36382 0.23234 0.55922 0.01336  -0.04037 0.02933  166 THR A CB  
1282 O OG1 . THR A 166 ? 0.36285 0.24890 0.56864 0.01635  -0.04062 0.03011  166 THR A OG1 
1283 C CG2 . THR A 166 ? 0.35309 0.22544 0.53593 0.00473  -0.04524 0.03092  166 THR A CG2 
1284 N N   . GLU A 167 ? 0.38804 0.23088 0.57695 0.00834  -0.05020 0.04346  167 GLU A N   
1285 C CA  . GLU A 167 ? 0.37723 0.20353 0.55697 0.00283  -0.05144 0.04478  167 GLU A CA  
1286 C C   . GLU A 167 ? 0.38073 0.21061 0.54905 -0.00639 -0.05200 0.04063  167 GLU A C   
1287 O O   . GLU A 167 ? 0.36798 0.21323 0.53531 -0.01016 -0.05465 0.04358  167 GLU A O   
1288 C CB  . GLU A 167 ? 0.38813 0.21421 0.57075 0.00257  -0.05746 0.05573  167 GLU A CB  
1289 C CG  . GLU A 167 ? 0.40299 0.23278 0.59977 0.01180  -0.05973 0.06142  167 GLU A CG  
1290 C CD  . GLU A 167 ? 0.42365 0.25368 0.61987 0.01066  -0.06752 0.07309  167 GLU A CD  
1291 O OE1 . GLU A 167 ? 0.44867 0.27382 0.63307 0.00280  -0.06917 0.07635  167 GLU A OE1 
1292 O OE2 . GLU A 167 ? 0.43334 0.26866 0.64084 0.01714  -0.07215 0.07925  167 GLU A OE2 
1293 N N   . VAL A 168 ? 0.40003 0.21497 0.56025 -0.00969 -0.04971 0.03414  168 VAL A N   
1294 C CA  . VAL A 168 ? 0.38822 0.20548 0.53984 -0.01836 -0.05168 0.03041  168 VAL A CA  
1295 C C   . VAL A 168 ? 0.39516 0.19772 0.54241 -0.02540 -0.05469 0.03286  168 VAL A C   
1296 O O   . VAL A 168 ? 0.41144 0.19389 0.55561 -0.02377 -0.05315 0.03146  168 VAL A O   
1297 C CB  . VAL A 168 ? 0.37564 0.18711 0.51914 -0.01801 -0.04833 0.02062  168 VAL A CB  
1298 C CG1 . VAL A 168 ? 0.37094 0.18540 0.50712 -0.02688 -0.05256 0.01791  168 VAL A CG1 
1299 C CG2 . VAL A 168 ? 0.36211 0.18651 0.51070 -0.01113 -0.04413 0.01817  168 VAL A CG2 
1300 N N   . ILE A 169 ? 0.38626 0.19828 0.53411 -0.03325 -0.05821 0.03650  169 ILE A N   
1301 C CA  . ILE A 169 ? 0.39636 0.19692 0.54175 -0.04191 -0.06122 0.03829  169 ILE A CA  
1302 C C   . ILE A 169 ? 0.39476 0.19427 0.53513 -0.04822 -0.06393 0.03134  169 ILE A C   
1303 O O   . ILE A 169 ? 0.40071 0.21739 0.54498 -0.05110 -0.06541 0.03124  169 ILE A O   
1304 C CB  . ILE A 169 ? 0.39062 0.20211 0.54166 -0.04717 -0.06248 0.04709  169 ILE A CB  
1305 C CG1 . ILE A 169 ? 0.41900 0.23200 0.57204 -0.04098 -0.06134 0.05450  169 ILE A CG1 
1306 C CG2 . ILE A 169 ? 0.39971 0.19886 0.55029 -0.05639 -0.06491 0.04928  169 ILE A CG2 
1307 C CD1 . ILE A 169 ? 0.41704 0.23698 0.57100 -0.04650 -0.06153 0.06329  169 ILE A CD1 
1308 N N   . LEU A 170 ? 0.39911 0.17722 0.52998 -0.05039 -0.06488 0.02562  170 LEU A N   
1309 C CA  . LEU A 170 ? 0.41185 0.18732 0.53358 -0.05610 -0.06848 0.01874  170 LEU A CA  
1310 C C   . LEU A 170 ? 0.41266 0.19873 0.54066 -0.06608 -0.07433 0.02235  170 LEU A C   
1311 O O   . LEU A 170 ? 0.41610 0.20192 0.54940 -0.07000 -0.07443 0.02802  170 LEU A O   
1312 C CB  . LEU A 170 ? 0.42718 0.17798 0.53123 -0.05601 -0.06636 0.01146  170 LEU A CB  
1313 C CG  . LEU A 170 ? 0.43377 0.17214 0.53094 -0.04635 -0.05868 0.00610  170 LEU A CG  
1314 C CD1 . LEU A 170 ? 0.46258 0.17481 0.53859 -0.04855 -0.05588 -0.00216 170 LEU A CD1 
1315 C CD2 . LEU A 170 ? 0.41128 0.16296 0.51264 -0.04176 -0.05740 0.00373  170 LEU A CD2 
1316 N N   . GLY A 171 ? 0.41863 0.21464 0.54731 -0.06991 -0.07894 0.01949  171 GLY A N   
1317 C CA  . GLY A 171 ? 0.41371 0.22220 0.55211 -0.07853 -0.08447 0.02284  171 GLY A CA  
1318 C C   . GLY A 171 ? 0.39774 0.22664 0.55472 -0.07947 -0.08209 0.03077  171 GLY A C   
1319 O O   . GLY A 171 ? 0.38957 0.23025 0.55778 -0.08620 -0.08489 0.03400  171 GLY A O   
1320 N N   . SER A 172 ? 0.38584 0.22059 0.54539 -0.07249 -0.07618 0.03383  172 SER A N   
1321 C CA  . SER A 172 ? 0.36857 0.22054 0.53932 -0.07298 -0.07189 0.04113  172 SER A CA  
1322 C C   . SER A 172 ? 0.37087 0.24390 0.55168 -0.07407 -0.07170 0.04115  172 SER A C   
1323 O O   . SER A 172 ? 0.37594 0.26216 0.56694 -0.07650 -0.06755 0.04676  172 SER A O   
1324 C CB  . SER A 172 ? 0.34454 0.19746 0.51043 -0.06455 -0.06636 0.04384  172 SER A CB  
1325 O OG  . SER A 172 ? 0.35515 0.20971 0.51494 -0.05692 -0.06539 0.03819  172 SER A OG  
1326 N N   . HIS A 173 ? 0.35987 0.23505 0.53735 -0.07220 -0.07533 0.03519  173 HIS A N   
1327 C CA  . HIS A 173 ? 0.34357 0.23721 0.53196 -0.07313 -0.07596 0.03554  173 HIS A CA  
1328 C C   . HIS A 173 ? 0.35131 0.25109 0.55581 -0.08234 -0.08060 0.03903  173 HIS A C   
1329 O O   . HIS A 173 ? 0.34919 0.26646 0.56834 -0.08322 -0.07944 0.04128  173 HIS A O   
1330 C CB  . HIS A 173 ? 0.35648 0.24820 0.53596 -0.06940 -0.07972 0.02890  173 HIS A CB  
1331 C CG  . HIS A 173 ? 0.36276 0.23665 0.53232 -0.07401 -0.08803 0.02422  173 HIS A CG  
1332 N ND1 . HIS A 173 ? 0.38207 0.23505 0.53914 -0.07460 -0.08813 0.02184  173 HIS A ND1 
1333 C CD2 . HIS A 173 ? 0.38259 0.25462 0.55124 -0.07849 -0.09685 0.02150  173 HIS A CD2 
1334 C CE1 . HIS A 173 ? 0.39396 0.23331 0.53957 -0.07895 -0.09514 0.01708  173 HIS A CE1 
1335 N NE2 . HIS A 173 ? 0.38045 0.23129 0.53204 -0.08148 -0.10118 0.01705  173 HIS A NE2 
1336 N N   . ARG A 174 ? 0.36829 0.25494 0.57067 -0.08862 -0.08502 0.03945  174 ARG A N   
1337 C CA  . ARG A 174 ? 0.35776 0.25326 0.57372 -0.09606 -0.08805 0.04268  174 ARG A CA  
1338 C C   . ARG A 174 ? 0.37229 0.27585 0.60069 -0.09924 -0.07998 0.05003  174 ARG A C   
1339 O O   . ARG A 174 ? 0.37234 0.28869 0.61738 -0.10459 -0.07967 0.05353  174 ARG A O   
1340 C CB  . ARG A 174 ? 0.37281 0.25146 0.57680 -0.10094 -0.09566 0.03901  174 ARG A CB  
1341 C CG  . ARG A 174 ? 0.36743 0.24203 0.56267 -0.10106 -0.10492 0.03317  174 ARG A CG  
1342 C CD  . ARG A 174 ? 0.39252 0.24882 0.57364 -0.10694 -0.11206 0.02956  174 ARG A CD  
1343 N NE  . ARG A 174 ? 0.44058 0.27407 0.60057 -0.10358 -0.10789 0.02523  174 ARG A NE  
1344 C CZ  . ARG A 174 ? 0.46008 0.27772 0.59972 -0.09989 -0.10901 0.01838  174 ARG A CZ  
1345 N NH1 . ARG A 174 ? 0.44422 0.26426 0.57861 -0.09989 -0.11530 0.01507  174 ARG A NH1 
1346 N NH2 . ARG A 174 ? 0.49732 0.29547 0.62148 -0.09591 -0.10310 0.01502  174 ARG A NH2 
1347 N N   . TRP A 175 ? 0.49289 0.25003 0.53516 -0.02108 -0.00168 0.13927  175 TRP A N   
1348 C CA  . TRP A 175 ? 0.51128 0.26532 0.55688 -0.01869 0.00729  0.14142  175 TRP A CA  
1349 C C   . TRP A 175 ? 0.52545 0.29379 0.62689 -0.01349 0.02578  0.14447  175 TRP A C   
1350 O O   . TRP A 175 ? 0.50209 0.27638 0.63552 -0.00764 0.03309  0.13892  175 TRP A O   
1351 C CB  . TRP A 175 ? 0.50866 0.24120 0.52617 -0.01337 0.01054  0.12940  175 TRP A CB  
1352 C CG  . TRP A 175 ? 0.51060 0.22914 0.48366 -0.01486 -0.00202 0.12516  175 TRP A CG  
1353 C CD1 . TRP A 175 ? 0.50567 0.23131 0.46499 -0.02007 -0.00693 0.12917  175 TRP A CD1 
1354 C CD2 . TRP A 175 ? 0.52166 0.22466 0.47213 -0.00959 -0.00615 0.11486  175 TRP A CD2 
1355 N NE1 . TRP A 175 ? 0.50822 0.22907 0.44954 -0.01800 -0.01114 0.12235  175 TRP A NE1 
1356 C CE2 . TRP A 175 ? 0.51177 0.22001 0.44690 -0.01104 -0.01287 0.11351  175 TRP A CE2 
1357 C CE3 . TRP A 175 ? 0.54291 0.24814 0.48661 -0.00285 -0.00005 0.09754  175 TRP A CE3 
1358 C CZ2 . TRP A 175 ? 0.53548 0.23242 0.45043 -0.00635 -0.01956 0.10342  175 TRP A CZ2 
1359 C CZ3 . TRP A 175 ? 0.52615 0.22200 0.44428 0.00136  -0.00913 0.08873  175 TRP A CZ3 
1360 C CH2 . TRP A 175 ? 0.54456 0.22541 0.44698 0.00047  -0.02069 0.09470  175 TRP A CH2 
1361 N N   . THR A 176 ? 0.58194 0.35440 0.69589 -0.01613 0.03679  0.15222  176 THR A N   
1362 C CA  . THR A 176 ? 0.58699 0.36843 0.75135 -0.01122 0.06415  0.14800  176 THR A CA  
1363 C C   . THR A 176 ? 0.60493 0.37900 0.75002 -0.00578 0.08098  0.11800  176 THR A C   
1364 O O   . THR A 176 ? 0.61867 0.39617 0.80109 0.00028  0.09893  0.10738  176 THR A O   
1365 C CB  . THR A 176 ? 0.58269 0.37526 0.75178 -0.01803 0.07372  0.15426  176 THR A CB  
1366 O OG1 . THR A 176 ? 0.63989 0.42031 0.74592 -0.02382 0.06954  0.14294  176 THR A OG1 
1367 C CG2 . THR A 176 ? 0.55642 0.36435 0.74251 -0.02479 0.05471  0.18028  176 THR A CG2 
1368 N N   . GLU A 177 ? 0.57775 0.34088 0.66521 -0.00914 0.07417  0.10549  177 GLU A N   
1369 C CA  . GLU A 177 ? 0.56089 0.31917 0.62298 -0.00921 0.08718  0.07964  177 GLU A CA  
1370 C C   . GLU A 177 ? 0.55722 0.30333 0.57418 -0.00737 0.06635  0.07429  177 GLU A C   
1371 O O   . GLU A 177 ? 0.56523 0.30376 0.56089 -0.00779 0.04579  0.08779  177 GLU A O   
1372 C CB  . GLU A 177 ? 0.61447 0.37512 0.65434 -0.01963 0.10267  0.07044  177 GLU A CB  
1373 C CG  . GLU A 177 ? 0.64280 0.41660 0.72663 -0.02298 0.12298  0.07800  177 GLU A CG  
1374 C CD  . GLU A 177 ? 0.70079 0.47487 0.75093 -0.03627 0.12687  0.07868  177 GLU A CD  
1375 O OE1 . GLU A 177 ? 0.70355 0.47007 0.71324 -0.03985 0.10300  0.09145  177 GLU A OE1 
1376 O OE2 . GLU A 177 ? 0.70604 0.48596 0.76990 -0.04445 0.15565  0.06557  177 GLU A OE2 
1377 N N   . VAL A 178 ? 0.57725 0.32136 0.58235 -0.00622 0.07331  0.05394  178 VAL A N   
1378 C CA  . VAL A 178 ? 0.55429 0.29079 0.52445 -0.00408 0.05497  0.04815  178 VAL A CA  
1379 C C   . VAL A 178 ? 0.58116 0.31244 0.50867 -0.01027 0.04178  0.05314  178 VAL A C   
1380 O O   . VAL A 178 ? 0.60933 0.33196 0.51836 -0.00673 0.02171  0.06202  178 VAL A O   
1381 C CB  . VAL A 178 ? 0.53519 0.27387 0.50312 -0.00445 0.06544  0.02621  178 VAL A CB  
1382 C CG1 . VAL A 178 ? 0.52056 0.25567 0.46215 -0.00147 0.04555  0.02213  178 VAL A CG1 
1383 C CG2 . VAL A 178 ? 0.52154 0.26251 0.53266 0.00113  0.08004  0.02183  178 VAL A CG2 
1384 N N   . GLY A 179 ? 0.58515 0.31956 0.49643 -0.02101 0.05425  0.04688  179 GLY A N   
1385 C CA  . GLY A 179 ? 0.60848 0.33692 0.48042 -0.02962 0.04210  0.05523  179 GLY A CA  
1386 C C   . GLY A 179 ? 0.63733 0.35993 0.47447 -0.03041 0.02170  0.05306  179 GLY A C   
1387 O O   . GLY A 179 ? 0.64188 0.36884 0.47638 -0.03089 0.02265  0.03942  179 GLY A O   
1388 N N   . THR A 180 ? 0.63726 0.34988 0.45071 -0.03072 0.00230  0.06832  180 THR A N   
1389 C CA  . THR A 180 ? 0.65052 0.35735 0.43138 -0.03435 -0.01827 0.07196  180 THR A CA  
1390 C C   . THR A 180 ? 0.65409 0.35046 0.44303 -0.01992 -0.03818 0.08260  180 THR A C   
1391 O O   . THR A 180 ? 0.65275 0.33578 0.42462 -0.02019 -0.05217 0.09724  180 THR A O   
1392 C CB  . THR A 180 ? 0.70615 0.40668 0.45103 -0.05011 -0.02139 0.08117  180 THR A CB  
1393 O OG1 . THR A 180 ? 0.72886 0.41755 0.47331 -0.04530 -0.02995 0.09814  180 THR A OG1 
1394 C CG2 . THR A 180 ? 0.69185 0.40059 0.43610 -0.06481 0.00607  0.06953  180 THR A CG2 
1395 N N   . PRO A 181 ? 0.64607 0.34614 0.46055 -0.00846 -0.03790 0.07442  181 PRO A N   
1396 C CA  . PRO A 181 ? 0.61562 0.30339 0.44227 0.00317  -0.04842 0.08142  181 PRO A CA  
1397 C C   . PRO A 181 ? 0.60798 0.29094 0.43016 0.00949  -0.06733 0.08486  181 PRO A C   
1398 O O   . PRO A 181 ? 0.61577 0.31074 0.43628 0.00787  -0.07399 0.07895  181 PRO A O   
1399 C CB  . PRO A 181 ? 0.59217 0.28664 0.44801 0.00922  -0.03679 0.06976  181 PRO A CB  
1400 C CG  . PRO A 181 ? 0.59254 0.30275 0.45074 0.00522  -0.02821 0.05511  181 PRO A CG  
1401 C CD  . PRO A 181 ? 0.63912 0.35256 0.47064 -0.00769 -0.02601 0.05701  181 PRO A CD  
1402 N N   . GLU A 182 ? 0.62113 0.28587 0.44366 0.01564  -0.07576 0.09541  182 GLU A N   
1403 C CA  . GLU A 182 ? 0.62579 0.28299 0.45426 0.02419  -0.09233 0.10115  182 GLU A CA  
1404 C C   . GLU A 182 ? 0.61548 0.27222 0.47531 0.03579  -0.08757 0.08994  182 GLU A C   
1405 O O   . GLU A 182 ? 0.62185 0.27746 0.49074 0.03512  -0.07339 0.08108  182 GLU A O   
1406 C CB  . GLU A 182 ? 0.62534 0.25979 0.43792 0.02349  -0.10088 0.11760  182 GLU A CB  
1407 C CG  . GLU A 182 ? 0.61871 0.25271 0.39725 0.01018  -0.10813 0.12940  182 GLU A CG  
1408 C CD  . GLU A 182 ? 0.62682 0.26160 0.40215 0.00731  -0.10746 0.13713  182 GLU A CD  
1409 O OE1 . GLU A 182 ? 0.60982 0.24667 0.39829 0.00874  -0.09407 0.13286  182 GLU A OE1 
1410 O OE2 . GLU A 182 ? 0.65351 0.28670 0.41091 0.00136  -0.12103 0.14793  182 GLU A OE2 
1411 N N   . ARG A 183 ? 0.60173 0.26174 0.48065 0.04492  -0.09953 0.09035  183 ARG A N   
1412 C CA  . ARG A 183 ? 0.58456 0.24829 0.49679 0.05475  -0.09275 0.07668  183 ARG A CA  
1413 C C   . ARG A 183 ? 0.60729 0.24632 0.52704 0.05782  -0.08033 0.07344  183 ARG A C   
1414 O O   . ARG A 183 ? 0.60322 0.24395 0.53571 0.05725  -0.06702 0.05935  183 ARG A O   
1415 C CB  . ARG A 183 ? 0.55882 0.23495 0.49658 0.06360  -0.10929 0.08011  183 ARG A CB  
1416 C CG  . ARG A 183 ? 0.56091 0.26405 0.49041 0.05555  -0.11906 0.07848  183 ARG A CG  
1417 C CD  . ARG A 183 ? 0.54916 0.26705 0.48938 0.05393  -0.10322 0.05815  183 ARG A CD  
1418 N NE  . ARG A 183 ? 0.58024 0.31575 0.49816 0.04054  -0.10340 0.05362  183 ARG A NE  
1419 C CZ  . ARG A 183 ? 0.59590 0.34581 0.51956 0.03648  -0.09210 0.03706  183 ARG A CZ  
1420 N NH1 . ARG A 183 ? 0.56346 0.31840 0.51668 0.04485  -0.08622 0.02545  183 ARG A NH1 
1421 N NH2 . ARG A 183 ? 0.61671 0.37442 0.51625 0.02268  -0.08506 0.03116  183 ARG A NH2 
1422 N N   . ASP A 184 ? 0.63607 0.26571 0.55017 0.05658  -0.07952 0.08322  184 ASP A N   
1423 C CA  . ASP A 184 ? 0.63079 0.25144 0.55560 0.05419  -0.06123 0.07597  184 ASP A CA  
1424 C C   . ASP A 184 ? 0.64036 0.26388 0.54665 0.03937  -0.04880 0.07391  184 ASP A C   
1425 O O   . ASP A 184 ? 0.64414 0.25952 0.55276 0.03228  -0.03669 0.06959  184 ASP A O   
1426 C CB  . ASP A 184 ? 0.63812 0.24664 0.56843 0.05818  -0.06241 0.08538  184 ASP A CB  
1427 C CG  . ASP A 184 ? 0.63861 0.24762 0.54025 0.04916  -0.06809 0.09893  184 ASP A CG  
1428 O OD1 . ASP A 184 ? 0.64723 0.26625 0.53031 0.04595  -0.08075 0.10645  184 ASP A OD1 
1429 O OD2 . ASP A 184 ? 0.65499 0.25302 0.55203 0.04369  -0.05900 0.10098  184 ASP A OD2 
1430 N N   . GLN A 185 ? 0.63042 0.26497 0.52072 0.03355  -0.05224 0.07772  185 GLN A N   
1431 C CA  . GLN A 185 ? 0.61435 0.25724 0.49989 0.02171  -0.04198 0.07622  185 GLN A CA  
1432 C C   . GLN A 185 ? 0.57757 0.22181 0.47841 0.02091  -0.03353 0.06322  185 GLN A C   
1433 O O   . GLN A 185 ? 0.57048 0.21816 0.47141 0.00965  -0.02558 0.06206  185 GLN A O   
1434 C CB  . GLN A 185 ? 0.59748 0.25038 0.47102 0.01775  -0.04530 0.08353  185 GLN A CB  
1435 C CG  . GLN A 185 ? 0.59713 0.24978 0.45203 0.01462  -0.05203 0.09565  185 GLN A CG  
1436 C CD  . GLN A 185 ? 0.60301 0.26142 0.44655 0.00873  -0.05125 0.10124  185 GLN A CD  
1437 O OE1 . GLN A 185 ? 0.63844 0.28942 0.46289 0.00853  -0.05926 0.10569  185 GLN A OE1 
1438 N NE2 . GLN A 185 ? 0.57093 0.24059 0.42596 0.00221  -0.04162 0.10244  185 GLN A NE2 
1439 N N   . ALA A 186 ? 0.55903 0.20154 0.47214 0.03130  -0.03687 0.05405  186 ALA A N   
1440 C CA  . ALA A 186 ? 0.53463 0.17951 0.46234 0.03047  -0.02858 0.03984  186 ALA A CA  
1441 C C   . ALA A 186 ? 0.53888 0.17424 0.48134 0.03043  -0.01946 0.02973  186 ALA A C   
1442 O O   . ALA A 186 ? 0.55377 0.17992 0.50396 0.03791  -0.02141 0.03194  186 ALA A O   
1443 C CB  . ALA A 186 ? 0.52429 0.17713 0.46136 0.04025  -0.03540 0.03208  186 ALA A CB  
1444 N N   . VAL A 187 ? 0.55606 0.19303 0.50419 0.02084  -0.00905 0.01875  187 VAL A N   
1445 C CA  . VAL A 187 ? 0.55097 0.17988 0.51511 0.01849  0.00083  0.00398  187 VAL A CA  
1446 C C   . VAL A 187 ? 0.53951 0.17667 0.52212 0.02458  0.00317  -0.01115 187 VAL A C   
1447 O O   . VAL A 187 ? 0.52390 0.17105 0.50152 0.02396  0.00086  -0.01079 187 VAL A O   
1448 C CB  . VAL A 187 ? 0.55934 0.18297 0.50681 -0.00187 0.00837  0.00278  187 VAL A CB  
1449 C CG1 . VAL A 187 ? 0.57862 0.19441 0.50777 -0.00792 0.00619  0.01650  187 VAL A CG1 
1450 C CG2 . VAL A 187 ? 0.52897 0.16469 0.46748 -0.01333 0.00789  0.00569  187 VAL A CG2 
1451 N N   . LEU A 188 ? 0.53431 0.16534 0.53283 0.03107  0.00636  -0.02503 188 LEU A N   
1452 C CA  . LEU A 188 ? 0.51635 0.15959 0.53179 0.03904  0.01145  -0.03834 188 LEU A CA  
1453 C C   . LEU A 188 ? 0.50268 0.15242 0.51325 0.02345  0.02238  -0.05217 188 LEU A C   
1454 O O   . LEU A 188 ? 0.51917 0.16058 0.52096 0.01075  0.03137  -0.05678 188 LEU A O   
1455 C CB  . LEU A 188 ? 0.51249 0.16116 0.56369 0.05454  0.01336  -0.04274 188 LEU A CB  
1456 C CG  . LEU A 188 ? 0.50456 0.16936 0.58361 0.07137  -0.00605 -0.03183 188 LEU A CG  
1457 C CD1 . LEU A 188 ? 0.52147 0.17396 0.57507 0.07222  -0.01986 -0.01197 188 LEU A CD1 
1458 C CD2 . LEU A 188 ? 0.50836 0.18451 0.63376 0.08609  -0.00848 -0.03370 188 LEU A CD2 
1459 N N   . ALA A 189 ? 0.45394 0.18979 0.51135 0.05439  -0.01984 -0.05346 189 ALA A N   
1460 C CA  . ALA A 189 ? 0.44153 0.19693 0.51478 0.05505  -0.01281 -0.05355 189 ALA A CA  
1461 C C   . ALA A 189 ? 0.43491 0.20015 0.53863 0.06884  -0.00853 -0.04959 189 ALA A C   
1462 O O   . ALA A 189 ? 0.45490 0.24106 0.58526 0.07138  -0.01503 -0.04219 189 ALA A O   
1463 C CB  . ALA A 189 ? 0.41729 0.19297 0.49767 0.04670  -0.02141 -0.04834 189 ALA A CB  
1464 N N   . THR A 190 ? 0.45958 0.20851 0.56032 0.07782  0.00266  -0.05426 190 THR A N   
1465 C CA  . THR A 190 ? 0.45361 0.21339 0.58580 0.09204  0.01070  -0.05030 190 THR A CA  
1466 C C   . THR A 190 ? 0.45673 0.23796 0.59751 0.09040  0.02359  -0.05074 190 THR A C   
1467 O O   . THR A 190 ? 0.47043 0.24300 0.58551 0.08470  0.03627  -0.05895 190 THR A O   
1468 C CB  . THR A 190 ? 0.46781 0.20471 0.59002 0.10206  0.02133  -0.05476 190 THR A CB  
1469 O OG1 . THR A 190 ? 0.49412 0.20652 0.58136 0.09518  0.03254  -0.06718 190 THR A OG1 
1470 C CG2 . THR A 190 ? 0.45990 0.18714 0.57452 0.10337  0.00777  -0.04807 190 THR A CG2 
1471 N N   . MET A 191 ? 0.44195 0.25061 0.61739 0.09401  0.01954  -0.04129 191 MET A N   
1472 C CA  . MET A 191 ? 0.45200 0.28412 0.63767 0.09029  0.02883  -0.03896 191 MET A CA  
1473 C C   . MET A 191 ? 0.45452 0.30992 0.68441 0.10182  0.03317  -0.02970 191 MET A C   
1474 O O   . MET A 191 ? 0.43796 0.29549 0.69323 0.11036  0.02344  -0.02306 191 MET A O   
1475 C CB  . MET A 191 ? 0.42309 0.26908 0.60480 0.07672  0.01566  -0.03482 191 MET A CB  
1476 C CG  . MET A 191 ? 0.40959 0.24325 0.55372 0.06408  0.01651  -0.04170 191 MET A CG  
1477 S SD  . MET A 191 ? 0.38578 0.23835 0.53431 0.05144  0.00343  -0.03473 191 MET A SD  
1478 C CE  . MET A 191 ? 0.35931 0.20963 0.52501 0.05481  -0.01575 -0.02983 191 MET A CE  
1479 N N   . ASP A 192 ? 0.50127 0.37545 0.74073 0.10101  0.04714  -0.02797 192 ASP A N   
1480 C CA  . ASP A 192 ? 0.47652 0.37831 0.76006 0.10950  0.05309  -0.01772 192 ASP A CA  
1481 C C   . ASP A 192 ? 0.45193 0.37927 0.75032 0.09832  0.04324  -0.00897 192 ASP A C   
1482 O O   . ASP A 192 ? 0.44815 0.37132 0.71976 0.08564  0.03857  -0.01227 192 ASP A O   
1483 C CB  . ASP A 192 ? 0.49996 0.40173 0.78214 0.11814  0.08099  -0.02263 192 ASP A CB  
1484 C CG  . ASP A 192 ? 0.52995 0.40117 0.79450 0.12936  0.09246  -0.03286 192 ASP A CG  
1485 O OD1 . ASP A 192 ? 0.56957 0.43972 0.86257 0.14244  0.08871  -0.02765 192 ASP A OD1 
1486 O OD2 . ASP A 192 ? 0.55262 0.39971 0.77468 0.12441  0.10397  -0.04552 192 ASP A OD2 
1487 N N   . PRO A 193 ? 0.40514 0.35883 0.74762 0.10223  0.03878  0.00318  193 PRO A N   
1488 C CA  . PRO A 193 ? 0.36350 0.33871 0.72028 0.09076  0.02875  0.01163  193 PRO A CA  
1489 C C   . PRO A 193 ? 0.35790 0.34030 0.69755 0.08357  0.04510  0.00969  193 PRO A C   
1490 O O   . PRO A 193 ? 0.36303 0.35303 0.70797 0.08998  0.06653  0.00930  193 PRO A O   
1491 C CB  . PRO A 193 ? 0.32121 0.32326 0.73065 0.09750  0.02496  0.02512  193 PRO A CB  
1492 C CG  . PRO A 193 ? 0.32424 0.31631 0.74548 0.11078  0.02339  0.02479  193 PRO A CG  
1493 C CD  . PRO A 193 ? 0.38634 0.35159 0.77010 0.11655  0.04072  0.01112  193 PRO A CD  
1494 N N   . GLY A 194 ? 0.33725 0.31648 0.65545 0.07027  0.03527  0.00890  194 GLY A N   
1495 C CA  . GLY A 194 ? 0.32593 0.31053 0.62432 0.06122  0.04653  0.00863  194 GLY A CA  
1496 C C   . GLY A 194 ? 0.33316 0.29521 0.58590 0.05319  0.04473  -0.00112 194 GLY A C   
1497 O O   . GLY A 194 ? 0.33100 0.29750 0.56798 0.04237  0.04493  0.00116  194 GLY A O   
1498 N N   . ASP A 195 ? 0.36277 0.30140 0.59556 0.05783  0.04255  -0.01064 195 ASP A N   
1499 C CA  . ASP A 195 ? 0.36704 0.28510 0.56025 0.04927  0.03824  -0.01869 195 ASP A CA  
1500 C C   . ASP A 195 ? 0.35637 0.27637 0.55182 0.04094  0.01878  -0.01427 195 ASP A C   
1501 O O   . ASP A 195 ? 0.33547 0.26847 0.55912 0.04168  0.00830  -0.00671 195 ASP A O   
1502 C CB  . ASP A 195 ? 0.38953 0.28164 0.56400 0.05622  0.04067  -0.02889 195 ASP A CB  
1503 C CG  . ASP A 195 ? 0.40617 0.29268 0.58021 0.06671  0.06126  -0.03415 195 ASP A CG  
1504 O OD1 . ASP A 195 ? 0.40423 0.30133 0.57515 0.06495  0.07661  -0.03340 195 ASP A OD1 
1505 O OD2 . ASP A 195 ? 0.42601 0.29648 0.60243 0.07701  0.06284  -0.03876 195 ASP A OD2 
1506 N N   . VAL A 196 ? 0.33571 0.24201 0.50112 0.03253  0.01432  -0.01899 196 VAL A N   
1507 C CA  . VAL A 196 ? 0.31761 0.22322 0.48262 0.02564  -0.00118 -0.01582 196 VAL A CA  
1508 C C   . VAL A 196 ? 0.32828 0.21273 0.46373 0.02213  -0.00477 -0.02339 196 VAL A C   
1509 O O   . VAL A 196 ? 0.34974 0.22521 0.45953 0.01763  0.00307  -0.02852 196 VAL A O   
1510 C CB  . VAL A 196 ? 0.30355 0.22501 0.47163 0.01597  -0.00251 -0.00783 196 VAL A CB  
1511 C CG1 . VAL A 196 ? 0.31782 0.23559 0.48487 0.01062  -0.01586 -0.00558 196 VAL A CG1 
1512 C CG2 . VAL A 196 ? 0.31321 0.25528 0.51245 0.01810  -0.00047 0.00096  196 VAL A CG2 
1513 N N   . LEU A 197 ? 0.32445 0.20022 0.46218 0.02321  -0.01661 -0.02395 197 LEU A N   
1514 C CA  . LEU A 197 ? 0.33957 0.19817 0.45298 0.01867  -0.02088 -0.02890 197 LEU A CA  
1515 C C   . LEU A 197 ? 0.31970 0.18571 0.43298 0.01022  -0.02794 -0.02384 197 LEU A C   
1516 O O   . LEU A 197 ? 0.30898 0.18099 0.43946 0.01142  -0.03540 -0.01961 197 LEU A O   
1517 C CB  . LEU A 197 ? 0.34177 0.18519 0.45590 0.02536  -0.02788 -0.03203 197 LEU A CB  
1518 C CG  . LEU A 197 ? 0.36011 0.18609 0.45113 0.02066  -0.03223 -0.03593 197 LEU A CG  
1519 C CD1 . LEU A 197 ? 0.34381 0.15604 0.41119 0.01796  -0.02394 -0.04215 197 LEU A CD1 
1520 C CD2 . LEU A 197 ? 0.34728 0.16081 0.44044 0.02625  -0.04071 -0.03658 197 LEU A CD2 
1521 N N   . ILE A 198 ? 0.31900 0.18400 0.41368 0.00153  -0.02583 -0.02390 198 ILE A N   
1522 C CA  . ILE A 198 ? 0.31376 0.18664 0.41104 -0.00562 -0.03182 -0.01773 198 ILE A CA  
1523 C C   . ILE A 198 ? 0.32151 0.18062 0.40280 -0.00871 -0.03541 -0.02115 198 ILE A C   
1524 O O   . ILE A 198 ? 0.33868 0.18694 0.39904 -0.01272 -0.03235 -0.02591 198 ILE A O   
1525 C CB  . ILE A 198 ? 0.31355 0.20019 0.40638 -0.01448 -0.02877 -0.01154 198 ILE A CB  
1526 C CG1 . ILE A 198 ? 0.32077 0.22259 0.43138 -0.01207 -0.02485 -0.00623 198 ILE A CG1 
1527 C CG2 . ILE A 198 ? 0.30518 0.19932 0.40278 -0.02098 -0.03534 -0.00404 198 ILE A CG2 
1528 C CD1 . ILE A 198 ? 0.32757 0.22775 0.42751 -0.01016 -0.01385 -0.01088 198 ILE A CD1 
1529 N N   . VAL A 199 ? 0.31815 0.17646 0.40833 -0.00736 -0.04111 -0.01887 199 VAL A N   
1530 C CA  . VAL A 199 ? 0.32977 0.17513 0.40721 -0.00891 -0.04329 -0.02166 199 VAL A CA  
1531 C C   . VAL A 199 ? 0.32363 0.17852 0.40905 -0.01365 -0.04524 -0.01487 199 VAL A C   
1532 O O   . VAL A 199 ? 0.31986 0.17920 0.42103 -0.00997 -0.04717 -0.01190 199 VAL A O   
1533 C CB  . VAL A 199 ? 0.31847 0.14940 0.39556 -0.00118 -0.04657 -0.02644 199 VAL A CB  
1534 C CG1 . VAL A 199 ? 0.34091 0.15908 0.40376 -0.00357 -0.04768 -0.02811 199 VAL A CG1 
1535 C CG2 . VAL A 199 ? 0.32775 0.15034 0.40078 0.00442  -0.04456 -0.03133 199 VAL A CG2 
1536 N N   . ARG A 200 ? 0.32459 0.18190 0.40005 -0.02193 -0.04474 -0.01217 200 ARG A N   
1537 C CA  . ARG A 200 ? 0.30895 0.17750 0.39473 -0.02649 -0.04598 -0.00401 200 ARG A CA  
1538 C C   . ARG A 200 ? 0.31950 0.18003 0.41085 -0.02049 -0.04511 -0.00548 200 ARG A C   
1539 O O   . ARG A 200 ? 0.34213 0.18645 0.42262 -0.01572 -0.04499 -0.01273 200 ARG A O   
1540 C CB  . ARG A 200 ? 0.33016 0.20012 0.40221 -0.03732 -0.04694 -0.00155 200 ARG A CB  
1541 C CG  . ARG A 200 ? 0.33838 0.22639 0.42474 -0.04417 -0.04932 0.01017  200 ARG A CG  
1542 C CD  . ARG A 200 ? 0.35237 0.23770 0.42791 -0.05336 -0.05073 0.01176  200 ARG A CD  
1543 N NE  . ARG A 200 ? 0.35757 0.26390 0.44932 -0.06144 -0.05446 0.02513  200 ARG A NE  
1544 C CZ  . ARG A 200 ? 0.36804 0.28482 0.48192 -0.05807 -0.05221 0.03293  200 ARG A CZ  
1545 N NH1 . ARG A 200 ? 0.37577 0.28164 0.49319 -0.04799 -0.04574 0.02744  200 ARG A NH1 
1546 N NH2 . ARG A 200 ? 0.37609 0.31448 0.50877 -0.06495 -0.05626 0.04699  200 ARG A NH2 
1547 N N   . GLN A 201 ? 0.30692 0.17838 0.41494 -0.02064 -0.04407 0.00198  201 GLN A N   
1548 C CA  . GLN A 201 ? 0.32938 0.19303 0.44030 -0.01591 -0.04041 0.00081  201 GLN A CA  
1549 C C   . GLN A 201 ? 0.35670 0.21043 0.45030 -0.01961 -0.03839 -0.00207 201 GLN A C   
1550 O O   . GLN A 201 ? 0.36084 0.22007 0.44821 -0.02803 -0.03987 0.00111  201 GLN A O   
1551 C CB  . GLN A 201 ? 0.31771 0.19671 0.45179 -0.01569 -0.03772 0.01086  201 GLN A CB  
1552 C CG  . GLN A 201 ? 0.33593 0.20857 0.47432 -0.01082 -0.03058 0.01059  201 GLN A CG  
1553 C CD  . GLN A 201 ? 0.30649 0.19491 0.47245 -0.00877 -0.02686 0.02143  201 GLN A CD  
1554 O OE1 . GLN A 201 ? 0.27978 0.18225 0.46109 -0.01069 -0.03124 0.02912  201 GLN A OE1 
1555 N NE2 . GLN A 201 ? 0.30353 0.18953 0.47639 -0.00448 -0.01801 0.02282  201 GLN A NE2 
1556 N N   . ARG A 202 ? 0.35685 0.19434 0.44058 -0.01439 -0.03560 -0.00796 202 ARG A N   
1557 C CA  . ARG A 202 ? 0.37697 0.20338 0.44483 -0.01706 -0.03243 -0.00973 202 ARG A CA  
1558 C C   . ARG A 202 ? 0.40284 0.21548 0.44979 -0.02014 -0.03646 -0.01519 202 ARG A C   
1559 O O   . ARG A 202 ? 0.40660 0.20983 0.44005 -0.02409 -0.03458 -0.01540 202 ARG A O   
1560 C CB  . ARG A 202 ? 0.37076 0.21234 0.44937 -0.02388 -0.02845 -0.00055 202 ARG A CB  
1561 C CG  . ARG A 202 ? 0.38754 0.22191 0.46057 -0.02322 -0.02091 -0.00005 202 ARG A CG  
1562 C CD  . ARG A 202 ? 0.39338 0.24801 0.48555 -0.02910 -0.01676 0.01125  202 ARG A CD  
1563 N NE  . ARG A 202 ? 0.40339 0.26257 0.51196 -0.02146 -0.00660 0.01441  202 ARG A NE  
1564 C CZ  . ARG A 202 ? 0.37991 0.25535 0.51502 -0.01757 -0.00462 0.02144  202 ARG A CZ  
1565 N NH1 . ARG A 202 ? 0.37610 0.26790 0.52495 -0.02207 -0.01295 0.02800  202 ARG A NH1 
1566 N NH2 . ARG A 202 ? 0.38088 0.25439 0.52767 -0.00888 0.00651  0.02197  202 ARG A NH2 
1567 N N   . VAL A 203 ? 0.39053 0.20099 0.43531 -0.01812 -0.04091 -0.01912 203 VAL A N   
1568 C CA  . VAL A 203 ? 0.39900 0.19398 0.42583 -0.01877 -0.04319 -0.02464 203 VAL A CA  
1569 C C   . VAL A 203 ? 0.41772 0.19505 0.43513 -0.01148 -0.04537 -0.02948 203 VAL A C   
1570 O O   . VAL A 203 ? 0.42229 0.20190 0.44745 -0.00543 -0.04706 -0.03048 203 VAL A O   
1571 C CB  . VAL A 203 ? 0.38793 0.18813 0.41725 -0.01873 -0.04470 -0.02655 203 VAL A CB  
1572 C CG1 . VAL A 203 ? 0.37236 0.15424 0.38489 -0.01733 -0.04508 -0.03276 203 VAL A CG1 
1573 C CG2 . VAL A 203 ? 0.37877 0.19504 0.41254 -0.02792 -0.04407 -0.02104 203 VAL A CG2 
1574 N N   . VAL A 204 ? 0.44319 0.20421 0.44260 -0.01313 -0.04555 -0.03142 204 VAL A N   
1575 C CA  . VAL A 204 ? 0.44342 0.19603 0.43146 -0.00769 -0.04584 -0.03299 204 VAL A CA  
1576 C C   . VAL A 204 ? 0.45221 0.20524 0.44154 -0.00213 -0.04830 -0.03506 204 VAL A C   
1577 O O   . VAL A 204 ? 0.45086 0.20176 0.43910 -0.00356 -0.04698 -0.03671 204 VAL A O   
1578 C CB  . VAL A 204 ? 0.45905 0.19707 0.42963 -0.01258 -0.04394 -0.03174 204 VAL A CB  
1579 C CG1 . VAL A 204 ? 0.47907 0.20710 0.43745 -0.00804 -0.04610 -0.03217 204 VAL A CG1 
1580 C CG2 . VAL A 204 ? 0.46326 0.20184 0.43598 -0.01825 -0.04014 -0.02833 204 VAL A CG2 
1581 N N   . HIS A 205 ? 0.45949 0.21326 0.45115 0.00380  -0.05224 -0.03497 205 HIS A N   
1582 C CA  . HIS A 205 ? 0.45370 0.21045 0.45438 0.00981  -0.05552 -0.03542 205 HIS A CA  
1583 C C   . HIS A 205 ? 0.46811 0.22262 0.46914 0.01398  -0.06318 -0.03394 205 HIS A C   
1584 O O   . HIS A 205 ? 0.47176 0.22102 0.46300 0.01179  -0.06499 -0.03382 205 HIS A O   
1585 C CB  . HIS A 205 ? 0.43595 0.20596 0.45417 0.01072  -0.05446 -0.03596 205 HIS A CB  
1586 C CG  . HIS A 205 ? 0.43899 0.21956 0.46843 0.01045  -0.05672 -0.03445 205 HIS A CG  
1587 N ND1 . HIS A 205 ? 0.43492 0.21721 0.46306 0.00606  -0.05374 -0.03364 205 HIS A ND1 
1588 C CD2 . HIS A 205 ? 0.44117 0.22941 0.48412 0.01391  -0.06180 -0.03339 205 HIS A CD2 
1589 C CE1 . HIS A 205 ? 0.43432 0.22390 0.47332 0.00754  -0.05560 -0.03273 205 HIS A CE1 
1590 N NE2 . HIS A 205 ? 0.44222 0.23540 0.48931 0.01145  -0.06100 -0.03270 205 HIS A NE2 
1591 N N   . ALA A 206 ? 0.45603 0.21286 0.46857 0.01977  -0.06817 -0.03287 206 ALA A N   
1592 C CA  . ALA A 206 ? 0.46498 0.21817 0.47954 0.02293  -0.07908 -0.03046 206 ALA A CA  
1593 C C   . ALA A 206 ? 0.46281 0.22256 0.49864 0.02977  -0.08321 -0.02831 206 ALA A C   
1594 O O   . ALA A 206 ? 0.45955 0.21931 0.50054 0.03329  -0.07621 -0.02918 206 ALA A O   
1595 C CB  . ALA A 206 ? 0.47921 0.21494 0.47332 0.02202  -0.08330 -0.02880 206 ALA A CB  
1596 N N   . GLY A 207 ? 0.49473 0.25856 0.54317 0.03144  -0.09454 -0.02560 207 GLY A N   
1597 C CA  . GLY A 207 ? 0.48126 0.25138 0.55371 0.03841  -0.10029 -0.02153 207 GLY A CA  
1598 C C   . GLY A 207 ? 0.51641 0.27353 0.58258 0.04269  -0.10628 -0.01759 207 GLY A C   
1599 O O   . GLY A 207 ? 0.53752 0.28047 0.58248 0.03905  -0.11311 -0.01671 207 GLY A O   
1600 N N   . GLY A 208 ? 0.48118 0.24238 0.56627 0.05098  -0.10296 -0.01472 208 GLY A N   
1601 C CA  . GLY A 208 ? 0.51811 0.26738 0.60020 0.05630  -0.10677 -0.01003 208 GLY A CA  
1602 C C   . GLY A 208 ? 0.52912 0.28087 0.62727 0.05883  -0.12491 -0.00144 208 GLY A C   
1603 O O   . GLY A 208 ? 0.50355 0.26713 0.61849 0.05665  -0.13451 0.00076  208 GLY A O   
1604 N N   . GLY A 209 ? 0.55637 0.29609 0.64961 0.06269  -0.13059 0.00436  209 GLY A N   
1605 C CA  . GLY A 209 ? 0.56756 0.31010 0.67779 0.06523  -0.14918 0.01482  209 GLY A CA  
1606 C C   . GLY A 209 ? 0.54768 0.30902 0.69761 0.07590  -0.14525 0.02106  209 GLY A C   
1607 O O   . GLY A 209 ? 0.54711 0.30833 0.70335 0.08411  -0.12859 0.01874  209 GLY A O   
1608 N N   . ASN A 210 ? 0.55315 0.34845 0.63636 0.06818  -0.06914 0.05301  210 ASN A N   
1609 C CA  . ASN A 210 ? 0.55078 0.35265 0.63745 0.07981  -0.07097 0.04690  210 ASN A CA  
1610 C C   . ASN A 210 ? 0.56889 0.35362 0.64281 0.09434  -0.07230 0.05202  210 ASN A C   
1611 O O   . ASN A 210 ? 0.59016 0.38296 0.66140 0.10306  -0.07564 0.05623  210 ASN A O   
1612 C CB  . ASN A 210 ? 0.54950 0.38439 0.65151 0.08243  -0.07354 0.04220  210 ASN A CB  
1613 C CG  . ASN A 210 ? 0.53813 0.38281 0.64962 0.09111  -0.07257 0.03564  210 ASN A CG  
1614 O OD1 . ASN A 210 ? 0.56163 0.38753 0.66489 0.09847  -0.07046 0.03498  210 ASN A OD1 
1615 N ND2 . ASN A 210 ? 0.50490 0.37788 0.63355 0.09068  -0.07338 0.03126  210 ASN A ND2 
1616 N N   . ARG A 211 ? 0.54495 0.30350 0.60873 0.09750  -0.07032 0.05154  211 ARG A N   
1617 C CA  . ARG A 211 ? 0.57045 0.30860 0.61995 0.11190  -0.07081 0.05635  211 ARG A CA  
1618 C C   . ARG A 211 ? 0.56936 0.31152 0.62109 0.12667  -0.07112 0.05107  211 ARG A C   
1619 O O   . ARG A 211 ? 0.60678 0.32401 0.64450 0.13687  -0.06996 0.05275  211 ARG A O   
1620 C CB  . ARG A 211 ? 0.57530 0.27636 0.60964 0.10561  -0.06792 0.06119  211 ARG A CB  
1621 C CG  . ARG A 211 ? 0.57222 0.26827 0.60467 0.09473  -0.06568 0.06968  211 ARG A CG  
1622 C CD  . ARG A 211 ? 0.60286 0.26173 0.62255 0.09010  -0.06217 0.07638  211 ARG A CD  
1623 N NE  . ARG A 211 ? 0.60614 0.24984 0.62955 0.07778  -0.06275 0.07062  211 ARG A NE  
1624 C CZ  . ARG A 211 ? 0.63327 0.25543 0.64638 0.08291  -0.06363 0.06552  211 ARG A CZ  
1625 N NH1 . ARG A 211 ? 0.66288 0.27679 0.66315 0.10000  -0.06266 0.06626  211 ARG A NH1 
1626 N NH2 . ARG A 211 ? 0.64722 0.25999 0.66184 0.07062  -0.06411 0.05892  211 ARG A NH2 
1627 N N   . THR A 212 ? 0.59571 0.36833 0.66523 0.12840  -0.07177 0.04527  212 THR A N   
1628 C CA  . THR A 212 ? 0.58933 0.37157 0.66574 0.14365  -0.07070 0.04179  212 THR A CA  
1629 C C   . THR A 212 ? 0.60821 0.40963 0.69239 0.15743  -0.07629 0.04542  212 THR A C   
1630 O O   . THR A 212 ? 0.60907 0.42200 0.69520 0.15398  -0.08161 0.04863  212 THR A O   
1631 C CB  . THR A 212 ? 0.56029 0.36564 0.65427 0.13903  -0.06719 0.03453  212 THR A CB  
1632 O OG1 . THR A 212 ? 0.54239 0.37835 0.65382 0.13087  -0.07057 0.03391  212 THR A OG1 
1633 C CG2 . THR A 212 ? 0.57486 0.35972 0.65862 0.12743  -0.06327 0.03025  212 THR A CG2 
1634 N N   . THR A 213 ? 0.55286 0.35719 0.64094 0.17413  -0.07538 0.04473  213 THR A N   
1635 C CA  . THR A 213 ? 0.57163 0.39422 0.66902 0.18969  -0.08188 0.04767  213 THR A CA  
1636 C C   . THR A 213 ? 0.57746 0.43752 0.70537 0.19526  -0.08225 0.04328  213 THR A C   
1637 O O   . THR A 213 ? 0.57136 0.45585 0.71483 0.20275  -0.09061 0.04442  213 THR A O   
1638 C CB  . THR A 213 ? 0.59485 0.39066 0.67363 0.20702  -0.08094 0.05210  213 THR A CB  
1639 O OG1 . THR A 213 ? 0.64178 0.41976 0.71416 0.21004  -0.07243 0.04871  213 THR A OG1 
1640 C CG2 . THR A 213 ? 0.63649 0.39926 0.68834 0.20330  -0.08213 0.05850  213 THR A CG2 
1641 N N   . ALA A 214 ? 0.57322 0.43756 0.71011 0.19197  -0.07355 0.03849  214 ALA A N   
1642 C CA  . ALA A 214 ? 0.52997 0.42916 0.69776 0.19573  -0.07098 0.03521  214 ALA A CA  
1643 C C   . ALA A 214 ? 0.52780 0.43040 0.70024 0.18154  -0.06283 0.03003  214 ALA A C   
1644 O O   . ALA A 214 ? 0.54913 0.42365 0.69974 0.17460  -0.05794 0.02834  214 ALA A O   
1645 C CB  . ALA A 214 ? 0.54185 0.44203 0.71602 0.21604  -0.06559 0.03664  214 ALA A CB  
1646 N N   . GLY A 215 ? 0.51346 0.44981 0.71452 0.17724  -0.06216 0.02749  215 GLY A N   
1647 C CA  . GLY A 215 ? 0.47321 0.41515 0.68031 0.16602  -0.05355 0.02303  215 GLY A CA  
1648 C C   . GLY A 215 ? 0.45154 0.40870 0.66627 0.14850  -0.05911 0.02103  215 GLY A C   
1649 O O   . GLY A 215 ? 0.45374 0.41288 0.66470 0.14424  -0.06923 0.02302  215 GLY A O   
1650 N N   . LYS A 216 ? 0.42216 0.38770 0.64503 0.13951  -0.05143 0.01724  216 LYS A N   
1651 C CA  . LYS A 216 ? 0.39861 0.37959 0.63015 0.12384  -0.05494 0.01500  216 LYS A CA  
1652 C C   . LYS A 216 ? 0.39860 0.35686 0.60488 0.11224  -0.05933 0.01544  216 LYS A C   
1653 O O   . LYS A 216 ? 0.41065 0.34057 0.59471 0.11285  -0.05652 0.01584  216 LYS A O   
1654 C CB  . LYS A 216 ? 0.41922 0.41081 0.66267 0.11866  -0.04403 0.01142  216 LYS A CB  
1655 C CG  . LYS A 216 ? 0.40312 0.42821 0.68217 0.12394  -0.04112 0.01173  216 LYS A CG  
1656 C CD  . LYS A 216 ? 0.39413 0.44254 0.69116 0.11737  -0.05434 0.01180  216 LYS A CD  
1657 C CE  . LYS A 216 ? 0.42248 0.50078 0.75422 0.12676  -0.05765 0.01326  216 LYS A CE  
1658 N NZ  . LYS A 216 ? 0.42444 0.51544 0.76314 0.12461  -0.07483 0.01327  216 LYS A NZ  
1659 N N   . PRO A 217 ? 0.40670 0.37645 0.61664 0.10182  -0.06623 0.01560  217 PRO A N   
1660 C CA  . PRO A 217 ? 0.39361 0.34442 0.58272 0.09117  -0.06880 0.01723  217 PRO A CA  
1661 C C   . PRO A 217 ? 0.39586 0.33270 0.57518 0.08182  -0.06149 0.01408  217 PRO A C   
1662 O O   . PRO A 217 ? 0.38615 0.33009 0.57365 0.08199  -0.05456 0.01018  217 PRO A O   
1663 C CB  . PRO A 217 ? 0.37886 0.34881 0.57673 0.08334  -0.07554 0.01716  217 PRO A CB  
1664 C CG  . PRO A 217 ? 0.38192 0.37650 0.60220 0.09175  -0.08060 0.01618  217 PRO A CG  
1665 C CD  . PRO A 217 ? 0.38208 0.38193 0.61572 0.09973  -0.07216 0.01442  217 PRO A CD  
1666 N N   . ARG A 218 ? 0.40579 0.32225 0.56768 0.07393  -0.06310 0.01615  218 ARG A N   
1667 C CA  . ARG A 218 ? 0.40652 0.31100 0.56029 0.06404  -0.05897 0.01291  218 ARG A CA  
1668 C C   . ARG A 218 ? 0.37486 0.29868 0.53843 0.05317  -0.05849 0.01084  218 ARG A C   
1669 O O   . ARG A 218 ? 0.36604 0.30113 0.53341 0.04914  -0.06289 0.01357  218 ARG A O   
1670 C CB  . ARG A 218 ? 0.41863 0.29661 0.55530 0.05827  -0.06140 0.01612  218 ARG A CB  
1671 C CG  . ARG A 218 ? 0.40614 0.26893 0.53461 0.04996  -0.05931 0.01185  218 ARG A CG  
1672 C CD  . ARG A 218 ? 0.42996 0.26713 0.54620 0.04345  -0.06268 0.01501  218 ARG A CD  
1673 N NE  . ARG A 218 ? 0.43151 0.27522 0.55171 0.03410  -0.06459 0.02085  218 ARG A NE  
1674 C CZ  . ARG A 218 ? 0.41699 0.26380 0.54046 0.02187  -0.06486 0.02073  218 ARG A CZ  
1675 N NH1 . ARG A 218 ? 0.40652 0.25075 0.52931 0.01695  -0.06479 0.01453  218 ARG A NH1 
1676 N NH2 . ARG A 218 ? 0.41726 0.26908 0.54365 0.01559  -0.06495 0.02733  218 ARG A NH2 
1677 N N   . ARG A 219 ? 0.36287 0.28861 0.52818 0.04976  -0.05286 0.00602  219 ARG A N   
1678 C CA  . ARG A 219 ? 0.33807 0.27812 0.50979 0.03967  -0.05129 0.00378  219 ARG A CA  
1679 C C   . ARG A 219 ? 0.33002 0.25359 0.48863 0.03151  -0.05011 0.00162  219 ARG A C   
1680 O O   . ARG A 219 ? 0.36301 0.26934 0.51133 0.03531  -0.04765 -0.00142 219 ARG A O   
1681 C CB  . ARG A 219 ? 0.31763 0.27637 0.50464 0.04297  -0.04510 0.00033  219 ARG A CB  
1682 C CG  . ARG A 219 ? 0.29889 0.28201 0.50478 0.04357  -0.04858 0.00149  219 ARG A CG  
1683 C CD  . ARG A 219 ? 0.27935 0.28014 0.50323 0.04486  -0.04137 -0.00138 219 ARG A CD  
1684 N NE  . ARG A 219 ? 0.29265 0.31666 0.53894 0.04749  -0.04618 -0.00052 219 ARG A NE  
1685 C CZ  . ARG A 219 ? 0.28138 0.32548 0.55061 0.04762  -0.04134 -0.00206 219 ARG A CZ  
1686 N NH1 . ARG A 219 ? 0.27872 0.32182 0.54936 0.04593  -0.02981 -0.00394 219 ARG A NH1 
1687 N NH2 . ARG A 219 ? 0.25755 0.32251 0.54896 0.04963  -0.04847 -0.00152 219 ARG A NH2 
1688 N N   . VAL A 220 ? 0.30108 0.22947 0.45959 0.02118  -0.05235 0.00300  220 VAL A N   
1689 C CA  . VAL A 220 ? 0.32295 0.24073 0.47324 0.01304  -0.05216 0.00080  220 VAL A CA  
1690 C C   . VAL A 220 ? 0.30351 0.23855 0.46023 0.00560  -0.05044 0.00012  220 VAL A C   
1691 O O   . VAL A 220 ? 0.30735 0.25600 0.47064 0.00375  -0.05199 0.00325  220 VAL A O   
1692 C CB  . VAL A 220 ? 0.33035 0.23030 0.47301 0.00778  -0.05718 0.00478  220 VAL A CB  
1693 C CG1 . VAL A 220 ? 0.33430 0.24309 0.48144 0.00310  -0.05898 0.01142  220 VAL A CG1 
1694 C CG2 . VAL A 220 ? 0.32877 0.21766 0.46556 0.00040  -0.05883 0.00162  220 VAL A CG2 
1695 N N   . VAL A 221 ? 0.30598 0.23889 0.45867 0.00265  -0.04735 -0.00426 221 VAL A N   
1696 C CA  . VAL A 221 ? 0.28541 0.23058 0.44111 -0.00449 -0.04563 -0.00485 221 VAL A CA  
1697 C C   . VAL A 221 ? 0.28930 0.22365 0.43764 -0.01175 -0.04923 -0.00448 221 VAL A C   
1698 O O   . VAL A 221 ? 0.29104 0.20933 0.43041 -0.01078 -0.05106 -0.00794 221 VAL A O   
1699 C CB  . VAL A 221 ? 0.28431 0.23695 0.44215 -0.00175 -0.03851 -0.00945 221 VAL A CB  
1700 C CG1 . VAL A 221 ? 0.26770 0.22409 0.42205 -0.00876 -0.03706 -0.01077 221 VAL A CG1 
1701 C CG2 . VAL A 221 ? 0.24795 0.21873 0.42054 0.00142  -0.03587 -0.00866 221 VAL A CG2 
1702 N N   . LEU A 222 ? 0.28769 0.23021 0.43991 -0.01840 -0.05074 -0.00018 222 LEU A N   
1703 C CA  . LEU A 222 ? 0.27720 0.21417 0.42786 -0.02570 -0.05381 0.00149  222 LEU A CA  
1704 C C   . LEU A 222 ? 0.26060 0.20779 0.41079 -0.02897 -0.05087 -0.00080 222 LEU A C   
1705 O O   . LEU A 222 ? 0.24460 0.20501 0.39768 -0.02856 -0.04707 -0.00016 222 LEU A O   
1706 C CB  . LEU A 222 ? 0.27567 0.21375 0.43122 -0.02970 -0.05551 0.00947  222 LEU A CB  
1707 C CG  . LEU A 222 ? 0.28710 0.21271 0.44157 -0.02630 -0.05793 0.01274  222 LEU A CG  
1708 C CD1 . LEU A 222 ? 0.30178 0.23524 0.45658 -0.01977 -0.05636 0.01523  222 LEU A CD1 
1709 C CD2 . LEU A 222 ? 0.34202 0.25976 0.50040 -0.03271 -0.05986 0.01952  222 LEU A CD2 
1710 N N   . ALA A 223 ? 0.26733 0.20685 0.41287 -0.03168 -0.05345 -0.00390 223 ALA A N   
1711 C CA  . ALA A 223 ? 0.25120 0.19826 0.39458 -0.03409 -0.05117 -0.00569 223 ALA A CA  
1712 C C   . ALA A 223 ? 0.24072 0.18624 0.38831 -0.04057 -0.05661 -0.00281 223 ALA A C   
1713 O O   . ALA A 223 ? 0.24796 0.18079 0.39496 -0.04225 -0.06337 -0.00442 223 ALA A O   
1714 C CB  . ALA A 223 ? 0.24326 0.18279 0.37563 -0.02892 -0.04860 -0.01273 223 ALA A CB  
1715 C C   . F2Y A 224 ? 0.21353 0.17886 0.36998 -0.04972 -0.05757 0.00241  224 F2Y A C   
1716 O O   . F2Y A 224 ? 0.20458 0.18018 0.35817 -0.04845 -0.05121 0.00383  224 F2Y A O   
1717 C CA  . F2Y A 224 ? 0.21760 0.17815 0.37855 -0.04985 -0.05777 0.00568  224 F2Y A CA  
1718 N N   . F2Y A 224 ? 0.22816 0.18646 0.38104 -0.04410 -0.05391 0.00172  224 F2Y A N   
1719 C CB  . F2Y A 224 ? 0.23144 0.20181 0.40197 -0.05284 -0.05396 0.01514  224 F2Y A CB  
1720 C CG  . F2Y A 224 ? 0.25781 0.22234 0.43029 -0.05183 -0.05371 0.01912  224 F2Y A CG  
1721 C CD1 . F2Y A 224 ? 0.26284 0.21326 0.43350 -0.05085 -0.05878 0.01540  224 F2Y A CD1 
1722 C CE1 . F2Y A 224 ? 0.27079 0.21455 0.44188 -0.04885 -0.05835 0.01931  224 F2Y A CE1 
1723 F F1  . F2Y A 224 ? 0.29151 0.22010 0.45919 -0.04693 -0.06269 0.01598  224 F2Y A F1  
1724 C CD2 . F2Y A 224 ? 0.26163 0.23218 0.43489 -0.05056 -0.04856 0.02650  224 F2Y A CD2 
1725 C CE2 . F2Y A 224 ? 0.29031 0.25362 0.46292 -0.04822 -0.04860 0.03039  224 F2Y A CE2 
1726 F F2  . F2Y A 224 ? 0.31487 0.28107 0.48444 -0.04540 -0.04418 0.03745  224 F2Y A F2  
1727 C CZ  . F2Y A 224 ? 0.29210 0.24252 0.46439 -0.04749 -0.05338 0.02693  224 F2Y A CZ  
1728 O OH  . F2Y A 224 ? 0.30118 0.24396 0.47162 -0.04425 -0.05298 0.03128  224 F2Y A OH  
1729 N N   . PHE A 225 ? 0.23281 0.18880 0.38673 -0.05033 -0.06511 -0.00227 225 PHE A N   
1730 C CA  . PHE A 225 ? 0.21524 0.17442 0.36507 -0.04969 -0.06690 -0.00483 225 PHE A CA  
1731 C C   . PHE A 225 ? 0.21284 0.18161 0.38000 -0.05584 -0.07135 0.00140  225 PHE A C   
1732 O O   . PHE A 225 ? 0.23092 0.19560 0.40799 -0.05982 -0.07774 0.00339  225 PHE A O   
1733 C CB  . PHE A 225 ? 0.22263 0.16525 0.35801 -0.04547 -0.07365 -0.01352 225 PHE A CB  
1734 C CG  . PHE A 225 ? 0.22565 0.15991 0.34464 -0.03818 -0.06658 -0.01859 225 PHE A CG  
1735 C CD1 . PHE A 225 ? 0.23530 0.17296 0.34352 -0.03367 -0.05862 -0.02058 225 PHE A CD1 
1736 C CD2 . PHE A 225 ? 0.24764 0.17072 0.36326 -0.03560 -0.06694 -0.02064 225 PHE A CD2 
1737 C CE1 . PHE A 225 ? 0.24874 0.18005 0.34573 -0.02745 -0.05062 -0.02408 225 PHE A CE1 
1738 C CE2 . PHE A 225 ? 0.24895 0.16649 0.35285 -0.02833 -0.05911 -0.02424 225 PHE A CE2 
1739 C CZ  . PHE A 225 ? 0.23372 0.15603 0.32962 -0.02461 -0.05065 -0.02573 225 PHE A CZ  
1740 N N   . ASN A 226 ? 0.20597 0.18795 0.37530 -0.05534 -0.06618 0.00511  226 ASN A N   
1741 C CA  . ASN A 226 ? 0.19815 0.19248 0.38580 -0.05983 -0.06786 0.01243  226 ASN A CA  
1742 C C   . ASN A 226 ? 0.19701 0.19692 0.38039 -0.05676 -0.06955 0.01008  226 ASN A C   
1743 O O   . ASN A 226 ? 0.18922 0.18560 0.35417 -0.05105 -0.06497 0.00521  226 ASN A O   
1744 C CB  . ASN A 226 ? 0.20194 0.20772 0.39663 -0.06054 -0.05755 0.02205  226 ASN A CB  
1745 C CG  . ASN A 226 ? 0.19631 0.19671 0.39399 -0.06214 -0.05564 0.02579  226 ASN A CG  
1746 O OD1 . ASN A 226 ? 0.20915 0.19899 0.40635 -0.06321 -0.06164 0.02252  226 ASN A OD1 
1747 N ND2 . ASN A 226 ? 0.19960 0.20560 0.39738 -0.06104 -0.04715 0.03270  226 ASN A ND2 
1748 N N   . SER A 227 ? 0.18749 0.19631 0.38945 -0.06049 -0.07598 0.01407  227 SER A N   
1749 C CA  . SER A 227 ? 0.17596 0.19309 0.37677 -0.05683 -0.07727 0.01367  227 SER A CA  
1750 C C   . SER A 227 ? 0.18039 0.20357 0.36770 -0.05139 -0.06382 0.01649  227 SER A C   
1751 O O   . SER A 227 ? 0.17862 0.20644 0.36798 -0.05227 -0.05450 0.02256  227 SER A O   
1752 C CB  . SER A 227 ? 0.17371 0.20573 0.40201 -0.06136 -0.08187 0.02122  227 SER A CB  
1753 O OG  . SER A 227 ? 0.17578 0.21957 0.40619 -0.05711 -0.08118 0.02298  227 SER A OG  
1754 N N   . VAL A 228 ? 0.18846 0.20911 0.35965 -0.04524 -0.06326 0.01175  228 VAL A N   
1755 C CA  . VAL A 228 ? 0.18062 0.20521 0.33895 -0.04046 -0.05130 0.01424  228 VAL A CA  
1756 C C   . VAL A 228 ? 0.17582 0.21648 0.34925 -0.04060 -0.04577 0.02439  228 VAL A C   
1757 O O   . VAL A 228 ? 0.18065 0.22334 0.34308 -0.03655 -0.03564 0.02738  228 VAL A O   
1758 C CB  . VAL A 228 ? 0.19447 0.21067 0.33128 -0.03345 -0.05106 0.00755  228 VAL A CB  
1759 C CG1 . VAL A 228 ? 0.20009 0.19927 0.31947 -0.03171 -0.05239 -0.00114 228 VAL A CG1 
1760 C CG2 . VAL A 228 ? 0.21041 0.23115 0.35396 -0.03108 -0.06089 0.00705  228 VAL A CG2 
1761 N N   . GLN A 229 ? 0.16913 0.22048 0.36795 -0.04507 -0.05162 0.03017  229 GLN A N   
1762 C CA  . GLN A 229 ? 0.16320 0.23030 0.37890 -0.04481 -0.04380 0.04168  229 GLN A CA  
1763 C C   . GLN A 229 ? 0.15172 0.21775 0.36591 -0.04609 -0.03331 0.04822  229 GLN A C   
1764 O O   . GLN A 229 ? 0.13869 0.21308 0.35589 -0.04273 -0.02315 0.05731  229 GLN A O   
1765 C CB  . GLN A 229 ? 0.16042 0.24026 0.40856 -0.05029 -0.05226 0.04705  229 GLN A CB  
1766 C CG  . GLN A 229 ? 0.17798 0.26071 0.43182 -0.04895 -0.06548 0.04141  229 GLN A CG  
1767 C CD  . GLN A 229 ? 0.17671 0.26928 0.46231 -0.05570 -0.07497 0.04556  229 GLN A CD  
1768 O OE1 . GLN A 229 ? 0.17543 0.28326 0.47973 -0.05501 -0.06874 0.05522  229 GLN A OE1 
1769 N NE2 . GLN A 229 ? 0.19156 0.26960 0.47255 -0.05953 -0.08646 0.03758  229 GLN A NE2 
1770 N N   . LEU A 230 ? 0.15251 0.20759 0.36094 -0.04964 -0.03556 0.04410  230 LEU A N   
1771 C CA  . LEU A 230 ? 0.14872 0.20135 0.35534 -0.05029 -0.02783 0.04990  230 LEU A CA  
1772 C C   . LEU A 230 ? 0.16851 0.21164 0.34952 -0.04593 -0.02274 0.04450  230 LEU A C   
1773 O O   . LEU A 230 ? 0.16546 0.20021 0.33463 -0.04572 -0.02702 0.03511  230 LEU A O   
1774 C CB  . LEU A 230 ? 0.14727 0.19415 0.36635 -0.05677 -0.03412 0.04979  230 LEU A CB  
1775 C CG  . LEU A 230 ? 0.14419 0.19795 0.38832 -0.06188 -0.03987 0.05447  230 LEU A CG  
1776 C CD1 . LEU A 230 ? 0.16482 0.20699 0.40936 -0.06518 -0.04436 0.05251  230 LEU A CD1 
1777 C CD2 . LEU A 230 ? 0.14361 0.21104 0.40254 -0.06036 -0.02964 0.06737  230 LEU A CD2 
1778 N N   . THR A 231 ? 0.16626 0.20995 0.33932 -0.04231 -0.01368 0.05075  231 THR A N   
1779 C CA  . THR A 231 ? 0.17335 0.20853 0.32401 -0.03861 -0.01012 0.04593  231 THR A CA  
1780 C C   . THR A 231 ? 0.18385 0.21096 0.33173 -0.04138 -0.01492 0.04029  231 THR A C   
1781 O O   . THR A 231 ? 0.18867 0.21485 0.34558 -0.04355 -0.01612 0.04463  231 THR A O   
1782 C CB  . THR A 231 ? 0.17870 0.21375 0.31996 -0.03334 -0.00104 0.05397  231 THR A CB  
1783 O OG1 . THR A 231 ? 0.16347 0.20591 0.30636 -0.02933 0.00452  0.05922  231 THR A OG1 
1784 C CG2 . THR A 231 ? 0.18775 0.21263 0.30648 -0.03024 0.00011  0.04824  231 THR A CG2 
1785 N N   . PRO A 232 ? 0.18504 0.20618 0.32147 -0.04096 -0.01693 0.03132  232 PRO A N   
1786 C CA  . PRO A 232 ? 0.19469 0.21000 0.33039 -0.04248 -0.02066 0.02661  232 PRO A CA  
1787 C C   . PRO A 232 ? 0.19997 0.21334 0.33088 -0.04045 -0.01858 0.03102  232 PRO A C   
1788 O O   . PRO A 232 ? 0.19140 0.20417 0.31129 -0.03695 -0.01408 0.03396  232 PRO A O   
1789 C CB  . PRO A 232 ? 0.18594 0.19724 0.31130 -0.04154 -0.02020 0.01796  232 PRO A CB  
1790 C CG  . PRO A 232 ? 0.19370 0.20649 0.31549 -0.04028 -0.01847 0.01714  232 PRO A CG  
1791 C CD  . PRO A 232 ? 0.18355 0.20298 0.30901 -0.03886 -0.01531 0.02562  232 PRO A CD  
1792 N N   . PHE A 233 ? 0.20109 0.21144 0.33819 -0.04167 -0.02229 0.03153  233 PHE A N   
1793 C CA  . PHE A 233 ? 0.20940 0.21598 0.33966 -0.03851 -0.02194 0.03458  233 PHE A CA  
1794 C C   . PHE A 233 ? 0.20895 0.21369 0.32824 -0.03652 -0.02353 0.02766  233 PHE A C   
1795 O O   . PHE A 233 ? 0.21648 0.21854 0.32326 -0.03304 -0.02189 0.02928  233 PHE A O   
1796 C CB  . PHE A 233 ? 0.21851 0.22124 0.35758 -0.03976 -0.02599 0.03593  233 PHE A CB  
1797 C CG  . PHE A 233 ? 0.23773 0.23535 0.36892 -0.03534 -0.02686 0.03876  233 PHE A CG  
1798 C CD1 . PHE A 233 ? 0.23883 0.23336 0.36243 -0.03146 -0.02209 0.04762  233 PHE A CD1 
1799 C CD2 . PHE A 233 ? 0.23679 0.23220 0.36777 -0.03393 -0.03228 0.03298  233 PHE A CD2 
1800 C CE1 . PHE A 233 ? 0.25376 0.24113 0.36659 -0.02593 -0.02371 0.05004  233 PHE A CE1 
1801 C CE2 . PHE A 233 ? 0.23368 0.22442 0.35708 -0.02891 -0.03470 0.03531  233 PHE A CE2 
1802 C CZ  . PHE A 233 ? 0.24695 0.23266 0.35979 -0.02474 -0.03093 0.04357  233 PHE A CZ  
1803 N N   . GLU A 234 ? 0.21144 0.21680 0.33539 -0.03856 -0.02653 0.01998  234 GLU A N   
1804 C CA  . GLU A 234 ? 0.20485 0.21036 0.32410 -0.03828 -0.02737 0.01346  234 GLU A CA  
1805 C C   . GLU A 234 ? 0.20512 0.21089 0.31924 -0.03961 -0.02298 0.01028  234 GLU A C   
1806 O O   . GLU A 234 ? 0.19692 0.20316 0.31439 -0.04078 -0.02138 0.00937  234 GLU A O   
1807 C CB  . GLU A 234 ? 0.20898 0.21560 0.33797 -0.03893 -0.03068 0.00815  234 GLU A CB  
1808 C CG  . GLU A 234 ? 0.20140 0.20673 0.33465 -0.03663 -0.03521 0.01090  234 GLU A CG  
1809 C CD  . GLU A 234 ? 0.21759 0.22362 0.36077 -0.03611 -0.03731 0.00649  234 GLU A CD  
1810 O OE1 . GLU A 234 ? 0.22070 0.22624 0.36678 -0.03743 -0.03448 0.00254  234 GLU A OE1 
1811 O OE2 . GLU A 234 ? 0.22769 0.23365 0.37413 -0.03314 -0.04149 0.00729  234 GLU A OE2 
1812 N N   . THR A 235 ? 0.21705 0.22067 0.32153 -0.03901 -0.02178 0.00825  235 THR A N   
1813 C CA  . THR A 235 ? 0.22521 0.22674 0.32317 -0.03997 -0.01708 0.00500  235 THR A CA  
1814 C C   . THR A 235 ? 0.22548 0.22653 0.32785 -0.04267 -0.01719 -0.00189 235 THR A C   
1815 O O   . THR A 235 ? 0.22631 0.22745 0.33031 -0.04354 -0.02130 -0.00417 235 THR A O   
1816 C CB  . THR A 235 ? 0.22145 0.21834 0.30402 -0.03729 -0.01409 0.00804  235 THR A CB  
1817 O OG1 . THR A 235 ? 0.20528 0.19867 0.28116 -0.03795 -0.00936 0.00470  235 THR A OG1 
1818 C CG2 . THR A 235 ? 0.22880 0.22063 0.30275 -0.03596 -0.01830 0.00702  235 THR A CG2 
1819 N N   . TYR A 236 ? 0.22893 0.22911 0.33357 -0.04360 -0.01268 -0.00492 236 TYR A N   
1820 C CA  . TYR A 236 ? 0.21660 0.21649 0.32778 -0.04580 -0.00984 -0.01009 236 TYR A CA  
1821 C C   . TYR A 236 ? 0.21835 0.21226 0.32029 -0.04742 -0.00476 -0.01221 236 TYR A C   
1822 O O   . TYR A 236 ? 0.22112 0.21335 0.32800 -0.04949 0.00019  -0.01556 236 TYR A O   
1823 C CB  . TYR A 236 ? 0.20649 0.20564 0.32244 -0.04421 -0.00673 -0.01156 236 TYR A CB  
1824 C CG  . TYR A 236 ? 0.21395 0.21615 0.33716 -0.04275 -0.01242 -0.00951 236 TYR A CG  
1825 C CD1 . TYR A 236 ? 0.21897 0.22590 0.35380 -0.04283 -0.01607 -0.01030 236 TYR A CD1 
1826 C CD2 . TYR A 236 ? 0.20288 0.20303 0.32232 -0.04142 -0.01460 -0.00666 236 TYR A CD2 
1827 C CE1 . TYR A 236 ? 0.21150 0.21878 0.35086 -0.04104 -0.02073 -0.00817 236 TYR A CE1 
1828 C CE2 . TYR A 236 ? 0.20197 0.20281 0.32833 -0.04096 -0.01968 -0.00473 236 TYR A CE2 
1829 C CZ  . TYR A 236 ? 0.20539 0.20870 0.34031 -0.04046 -0.02241 -0.00535 236 TYR A CZ  
1830 O OH  . TYR A 236 ? 0.19854 0.20028 0.33837 -0.03949 -0.02692 -0.00320 236 TYR A OH  
1831 N N   . ARG A 237 ? 0.23271 0.22236 0.32127 -0.04619 -0.00528 -0.00987 237 ARG A N   
1832 C CA  . ARG A 237 ? 0.24603 0.22703 0.32224 -0.04693 -0.00063 -0.01155 237 ARG A CA  
1833 C C   . ARG A 237 ? 0.25490 0.23331 0.33610 -0.05175 -0.00310 -0.01598 237 ARG A C   
1834 O O   . ARG A 237 ? 0.27242 0.24165 0.34445 -0.05348 0.00076  -0.01798 237 ARG A O   
1835 C CB  . ARG A 237 ? 0.24408 0.22052 0.30367 -0.04280 -0.00058 -0.00728 237 ARG A CB  
1836 C CG  . ARG A 237 ? 0.24132 0.21446 0.29455 -0.04237 -0.00663 -0.00689 237 ARG A CG  
1837 C CD  . ARG A 237 ? 0.25272 0.22676 0.29736 -0.03672 -0.00691 -0.00012 237 ARG A CD  
1838 N NE  . ARG A 237 ? 0.26160 0.22783 0.28819 -0.03209 -0.00130 0.00285  237 ARG A NE  
1839 C CZ  . ARG A 237 ? 0.26631 0.23540 0.28829 -0.02656 0.00239  0.01003  237 ARG A CZ  
1840 N NH1 . ARG A 237 ? 0.26973 0.24876 0.30462 -0.02610 0.00107  0.01498  237 ARG A NH1 
1841 N NH2 . ARG A 237 ? 0.28729 0.24899 0.29253 -0.02131 0.00804  0.01272  237 ARG A NH2 
1842 N N   . THR A 238 ? 0.24602 0.23166 0.34173 -0.05393 -0.01012 -0.01758 238 THR A N   
1843 C CA  . THR A 238 ? 0.24463 0.22964 0.34931 -0.05914 -0.01444 -0.02216 238 THR A CA  
1844 C C   . THR A 238 ? 0.23937 0.23263 0.36713 -0.06300 -0.01078 -0.02459 238 THR A C   
1845 O O   . THR A 238 ? 0.26373 0.26088 0.40679 -0.06788 -0.01540 -0.02795 238 THR A O   
1846 C CB  . THR A 238 ? 0.22383 0.21048 0.32827 -0.05815 -0.02651 -0.02268 238 THR A CB  
1847 O OG1 . THR A 238 ? 0.23142 0.22924 0.35092 -0.05634 -0.03036 -0.02128 238 THR A OG1 
1848 C CG2 . THR A 238 ? 0.25501 0.23227 0.33497 -0.05258 -0.02801 -0.01898 238 THR A CG2 
1849 N N   . MET A 239 ? 0.23494 0.23051 0.36573 -0.06043 -0.00280 -0.02289 239 MET A N   
1850 C CA  . MET A 239 ? 0.24178 0.24272 0.39139 -0.06244 0.00366  -0.02434 239 MET A CA  
1851 C C   . MET A 239 ? 0.26233 0.25613 0.41290 -0.06734 0.01166  -0.02618 239 MET A C   
1852 O O   . MET A 239 ? 0.27390 0.25596 0.40511 -0.06683 0.01558  -0.02584 239 MET A O   
1853 C CB  . MET A 239 ? 0.23851 0.23874 0.38477 -0.05693 0.01051  -0.02237 239 MET A CB  
1854 C CG  . MET A 239 ? 0.24924 0.25590 0.39908 -0.05316 0.00320  -0.02076 239 MET A CG  
1855 S SD  . MET A 239 ? 0.26739 0.26811 0.40675 -0.04684 0.00784  -0.01929 239 MET A SD  
1856 C CE  . MET A 239 ? 0.24430 0.24110 0.38929 -0.04537 0.02103  -0.02089 239 MET A CE  
1857 N N   . PRO A 240 ? 0.27374 0.27438 0.44785 -0.07209 0.01453  -0.02769 240 PRO A N   
1858 C CA  . PRO A 240 ? 0.29697 0.29007 0.47479 -0.07757 0.02392  -0.02861 240 PRO A CA  
1859 C C   . PRO A 240 ? 0.29582 0.27752 0.45712 -0.07265 0.03865  -0.02611 240 PRO A C   
1860 O O   . PRO A 240 ? 0.30558 0.28859 0.46237 -0.06585 0.04283  -0.02424 240 PRO A O   
1861 C CB  . PRO A 240 ? 0.28776 0.29441 0.49601 -0.08103 0.02470  -0.02869 240 PRO A CB  
1862 C CG  . PRO A 240 ? 0.28181 0.30144 0.49995 -0.07907 0.01090  -0.02951 240 PRO A CG  
1863 C CD  . PRO A 240 ? 0.25903 0.27504 0.45919 -0.07304 0.00835  -0.02832 240 PRO A CD  
1864 N N   . ARG A 241 ? 0.30464 0.27300 0.45516 -0.07563 0.04597  -0.02637 241 ARG A N   
1865 C CA  . ARG A 241 ? 0.32348 0.27843 0.45477 -0.06986 0.05967  -0.02398 241 ARG A CA  
1866 C C   . ARG A 241 ? 0.32312 0.28048 0.46820 -0.06738 0.07277  -0.02174 241 ARG A C   
1867 O O   . ARG A 241 ? 0.34210 0.29203 0.47082 -0.05876 0.08010  -0.01996 241 ARG A O   
1868 C CB  . ARG A 241 ? 0.34970 0.28819 0.46645 -0.07325 0.06553  -0.02437 241 ARG A CB  
1869 C CG  . ARG A 241 ? 0.37606 0.29960 0.47415 -0.06669 0.08104  -0.02157 241 ARG A CG  
1870 C CD  . ARG A 241 ? 0.40156 0.30664 0.48414 -0.06924 0.08847  -0.02139 241 ARG A CD  
1871 N NE  . ARG A 241 ? 0.43076 0.32724 0.48617 -0.06447 0.08194  -0.02190 241 ARG A NE  
1872 C CZ  . ARG A 241 ? 0.41415 0.30462 0.44640 -0.05436 0.08426  -0.02001 241 ARG A CZ  
1873 N NH1 . ARG A 241 ? 0.40654 0.29617 0.43546 -0.04751 0.09148  -0.01831 241 ARG A NH1 
1874 N NH2 . ARG A 241 ? 0.41188 0.29666 0.42366 -0.05036 0.07874  -0.01984 241 ARG A NH2 
1875 N N   . GLU A 242 ? 0.31974 0.28686 0.49476 -0.07413 0.07590  -0.02165 242 GLU A N   
1876 C CA  . GLU A 242 ? 0.31202 0.28282 0.50152 -0.07021 0.08966  -0.01845 242 GLU A CA  
1877 C C   . GLU A 242 ? 0.29591 0.27489 0.48401 -0.06195 0.08471  -0.01823 242 GLU A C   
1878 O O   . GLU A 242 ? 0.30089 0.27356 0.48077 -0.05351 0.09584  -0.01590 242 GLU A O   
1879 C CB  . GLU A 242 ? 0.32570 0.30923 0.54682 -0.07632 0.09117  -0.01747 242 GLU A CB  
1880 C CG  . GLU A 242 ? 0.35348 0.35412 0.59232 -0.08131 0.07177  -0.02042 242 GLU A CG  
1881 C CD  . GLU A 242 ? 0.37917 0.37465 0.61301 -0.08912 0.06183  -0.02311 242 GLU A CD  
1882 O OE1 . GLU A 242 ? 0.35953 0.34677 0.57281 -0.08976 0.05266  -0.02583 242 GLU A OE1 
1883 O OE2 . GLU A 242 ? 0.39982 0.39841 0.65040 -0.09457 0.06367  -0.02237 242 GLU A OE2 
1884 N N   . MET A 243 ? 0.29812 0.28804 0.49059 -0.06337 0.06831  -0.02058 243 MET A N   
1885 C CA  . MET A 243 ? 0.29059 0.28605 0.48075 -0.05603 0.06321  -0.02029 243 MET A CA  
1886 C C   . MET A 243 ? 0.29815 0.27952 0.45683 -0.04807 0.06393  -0.02012 243 MET A C   
1887 O O   . MET A 243 ? 0.30077 0.27709 0.45188 -0.04010 0.06909  -0.01929 243 MET A O   
1888 C CB  . MET A 243 ? 0.27594 0.28445 0.47694 -0.05926 0.04621  -0.02216 243 MET A CB  
1889 C CG  . MET A 243 ? 0.26505 0.27562 0.45906 -0.05210 0.04016  -0.02168 243 MET A CG  
1890 S SD  . MET A 243 ? 0.22761 0.25192 0.43461 -0.05435 0.02278  -0.02270 243 MET A SD  
1891 C CE  . MET A 243 ? 0.22417 0.26387 0.46712 -0.06008 0.02395  -0.02339 243 MET A CE  
1892 N N   . VAL A 244 ? 0.30840 0.28288 0.44848 -0.04954 0.05815  -0.02098 244 VAL A N   
1893 C CA  . VAL A 244 ? 0.31847 0.28225 0.43259 -0.04241 0.05686  -0.02076 244 VAL A CA  
1894 C C   . VAL A 244 ? 0.33128 0.27964 0.42917 -0.03581 0.07079  -0.01980 244 VAL A C   
1895 O O   . VAL A 244 ? 0.32156 0.26201 0.40451 -0.02758 0.07129  -0.02006 244 VAL A O   
1896 C CB  . VAL A 244 ? 0.30681 0.26831 0.40746 -0.04484 0.04905  -0.02095 244 VAL A CB  
1897 C CG1 . VAL A 244 ? 0.30009 0.25280 0.37820 -0.03773 0.04763  -0.02035 244 VAL A CG1 
1898 C CG2 . VAL A 244 ? 0.27826 0.25203 0.39047 -0.04897 0.03625  -0.02126 244 VAL A CG2 
1899 N N   . GLU A 245 ? 0.34514 0.28695 0.44424 -0.03892 0.08204  -0.01871 245 GLU A N   
1900 C CA  . GLU A 245 ? 0.35196 0.27704 0.43429 -0.03173 0.09732  -0.01690 245 GLU A CA  
1901 C C   . GLU A 245 ? 0.34233 0.26783 0.43319 -0.02578 0.10647  -0.01544 245 GLU A C   
1902 O O   . GLU A 245 ? 0.35605 0.26530 0.42628 -0.01601 0.11699  -0.01421 245 GLU A O   
1903 C CB  . GLU A 245 ? 0.35828 0.27563 0.44230 -0.03738 0.10826  -0.01532 245 GLU A CB  
1904 C CG  . GLU A 245 ? 0.37029 0.28182 0.43795 -0.04019 0.10085  -0.01664 245 GLU A CG  
1905 C CD  . GLU A 245 ? 0.38864 0.28892 0.45482 -0.04577 0.11087  -0.01550 245 GLU A CD  
1906 O OE1 . GLU A 245 ? 0.40910 0.31342 0.49874 -0.05301 0.11847  -0.01442 245 GLU A OE1 
1907 O OE2 . GLU A 245 ? 0.39915 0.28641 0.44167 -0.04297 0.11100  -0.01549 245 GLU A OE2 
1908 N N   . SER A 246 ? 0.32319 0.26570 0.44166 -0.02996 0.10229  -0.01550 246 SER A N   
1909 C CA  . SER A 246 ? 0.33419 0.27747 0.45966 -0.02262 0.11007  -0.01394 246 SER A CA  
1910 C C   . SER A 246 ? 0.33413 0.26871 0.43705 -0.01302 0.10212  -0.01615 246 SER A C   
1911 O O   . SER A 246 ? 0.35528 0.27989 0.44886 -0.00316 0.11067  -0.01526 246 SER A O   
1912 C CB  . SER A 246 ? 0.32546 0.29038 0.48730 -0.02890 0.10623  -0.01340 246 SER A CB  
1913 O OG  . SER A 246 ? 0.31822 0.29248 0.48195 -0.02950 0.08915  -0.01604 246 SER A OG  
1914 N N   . MET A 247 ? 0.33104 0.26823 0.42532 -0.01549 0.08618  -0.01880 247 MET A N   
1915 C CA  . MET A 247 ? 0.33452 0.26484 0.41257 -0.00846 0.07675  -0.02102 247 MET A CA  
1916 C C   . MET A 247 ? 0.35582 0.26447 0.40135 0.00106  0.08085  -0.02205 247 MET A C   
1917 O O   . MET A 247 ? 0.36654 0.26605 0.40028 0.00198  0.08991  -0.02078 247 MET A O   
1918 C CB  . MET A 247 ? 0.31748 0.25857 0.40038 -0.01467 0.05963  -0.02237 247 MET A CB  
1919 C CG  . MET A 247 ? 0.28823 0.24790 0.39837 -0.02258 0.05439  -0.02158 247 MET A CG  
1920 S SD  . MET A 247 ? 0.26328 0.23094 0.37440 -0.02612 0.03654  -0.02209 247 MET A SD  
1921 C CE  . MET A 247 ? 0.28956 0.25053 0.38161 -0.02745 0.03437  -0.02185 247 MET A CE  
1922 N N   . THR A 248 ? 0.35950 0.25832 0.38942 0.00858  0.07323  -0.02463 248 THR A N   
1923 C CA  . THR A 248 ? 0.38471 0.26280 0.38256 0.01806  0.07161  -0.02688 248 THR A CA  
1924 C C   . THR A 248 ? 0.36086 0.24324 0.35347 0.01362  0.05799  -0.02812 248 THR A C   
1925 O O   . THR A 248 ? 0.32857 0.22810 0.34007 0.00451  0.04856  -0.02742 248 THR A O   
1926 C CB  . THR A 248 ? 0.42934 0.29373 0.41242 0.02746  0.06605  -0.03005 248 THR A CB  
1927 O OG1 . THR A 248 ? 0.38420 0.26050 0.38205 0.02139  0.05016  -0.03173 248 THR A OG1 
1928 C CG2 . THR A 248 ? 0.47642 0.33436 0.46128 0.03463  0.08146  -0.02814 248 THR A CG2 
1929 N N   . VAL A 249 ? 0.37085 0.23687 0.33672 0.02135  0.05741  -0.02957 249 VAL A N   
1930 C CA  . VAL A 249 ? 0.37007 0.23999 0.33085 0.01928  0.04410  -0.03052 249 VAL A CA  
1931 C C   . VAL A 249 ? 0.33992 0.22154 0.31544 0.01413  0.02745  -0.03200 249 VAL A C   
1932 O O   . VAL A 249 ? 0.31068 0.20835 0.30199 0.00615  0.02011  -0.03002 249 VAL A O   
1933 C CB  . VAL A 249 ? 0.38407 0.23286 0.31267 0.03094  0.04300  -0.03282 249 VAL A CB  
1934 C CG1 . VAL A 249 ? 0.35630 0.21157 0.28398 0.02948  0.02687  -0.03392 249 VAL A CG1 
1935 C CG2 . VAL A 249 ? 0.40728 0.24453 0.32121 0.03531  0.06002  -0.03016 249 VAL A CG2 
1936 N N   . LEU A 250 ? 0.35374 0.22549 0.32287 0.01920  0.02201  -0.03514 250 LEU A N   
1937 C CA  . LEU A 250 ? 0.32531 0.20560 0.30865 0.01397  0.00702  -0.03629 250 LEU A CA  
1938 C C   . LEU A 250 ? 0.30449 0.20551 0.31600 0.00377  0.00824  -0.03270 250 LEU A C   
1939 O O   . LEU A 250 ? 0.28143 0.19567 0.30714 -0.00329 -0.00116 -0.03081 250 LEU A O   
1940 C CB  . LEU A 250 ? 0.35978 0.22279 0.33015 0.02146  0.00293  -0.04045 250 LEU A CB  
1941 C CG  . LEU A 250 ? 0.34403 0.21196 0.32776 0.01611  -0.01241 -0.04183 250 LEU A CG  
1942 C CD1 . LEU A 250 ? 0.33600 0.20909 0.32282 0.01191  -0.02760 -0.04234 250 LEU A CD1 
1943 C CD2 . LEU A 250 ? 0.37917 0.22610 0.34634 0.02453  -0.01544 -0.04639 250 LEU A CD2 
1944 N N   . GLY A 251 ? 0.30492 0.20900 0.32506 0.00344  0.01998  -0.03133 251 GLY A N   
1945 C CA  . GLY A 251 ? 0.28332 0.20609 0.32883 -0.00518 0.01966  -0.02852 251 GLY A CA  
1946 C C   . GLY A 251 ? 0.27733 0.21270 0.33090 -0.01252 0.01819  -0.02584 251 GLY A C   
1947 O O   . GLY A 251 ? 0.24597 0.19423 0.31450 -0.01882 0.01127  -0.02382 251 GLY A O   
1948 N N   . GLN A 252 ? 0.27815 0.20773 0.31939 -0.01071 0.02523  -0.02553 252 GLN A N   
1949 C CA  . GLN A 252 ? 0.25457 0.19283 0.29958 -0.01622 0.02454  -0.02315 252 GLN A CA  
1950 C C   . GLN A 252 ? 0.24817 0.19050 0.29082 -0.01670 0.01316  -0.02207 252 GLN A C   
1951 O O   . GLN A 252 ? 0.23696 0.19034 0.28892 -0.02180 0.00973  -0.01915 252 GLN A O   
1952 C CB  . GLN A 252 ? 0.29252 0.22092 0.32354 -0.01347 0.03591  -0.02295 252 GLN A CB  
1953 C CG  . GLN A 252 ? 0.30489 0.23050 0.34231 -0.01415 0.04907  -0.02276 252 GLN A CG  
1954 C CD  . GLN A 252 ? 0.32252 0.23541 0.34474 -0.01128 0.06137  -0.02191 252 GLN A CD  
1955 O OE1 . GLN A 252 ? 0.32268 0.22573 0.32475 -0.00603 0.06014  -0.02211 252 GLN A OE1 
1956 N NE2 . GLN A 252 ? 0.35019 0.26322 0.38323 -0.01465 0.07329  -0.02063 252 GLN A NE2 
1957 N N   . ARG A 253 ? 0.25559 0.18871 0.28604 -0.01100 0.00713  -0.02419 253 ARG A N   
1958 C CA  . ARG A 253 ? 0.25268 0.19232 0.28726 -0.01242 -0.00465 -0.02276 253 ARG A CA  
1959 C C   . ARG A 253 ? 0.22538 0.17649 0.27984 -0.01882 -0.01207 -0.02062 253 ARG A C   
1960 O O   . ARG A 253 ? 0.23770 0.19964 0.30251 -0.02263 -0.01732 -0.01673 253 ARG A O   
1961 C CB  . ARG A 253 ? 0.26648 0.19336 0.28603 -0.00545 -0.01235 -0.02644 253 ARG A CB  
1962 C CG  . ARG A 253 ? 0.28977 0.20339 0.28607 0.00276  -0.00665 -0.02813 253 ARG A CG  
1963 C CD  . ARG A 253 ? 0.30679 0.20452 0.28517 0.01107  -0.01594 -0.03289 253 ARG A CD  
1964 N NE  . ARG A 253 ? 0.32597 0.23208 0.31488 0.00864  -0.03195 -0.03279 253 ARG A NE  
1965 C CZ  . ARG A 253 ? 0.30928 0.21531 0.30802 0.00567  -0.04432 -0.03492 253 ARG A CZ  
1966 N NH1 . ARG A 253 ? 0.31150 0.20770 0.30744 0.00617  -0.04311 -0.03782 253 ARG A NH1 
1967 N NH2 . ARG A 253 ? 0.30489 0.22081 0.31774 0.00215  -0.05794 -0.03377 253 ARG A NH2 
1968 N N   . MET A 254 ? 0.24524 0.19340 0.30471 -0.01916 -0.01161 -0.02245 254 MET A N   
1969 C CA  . MET A 254 ? 0.23923 0.19593 0.31548 -0.02431 -0.01811 -0.02020 254 MET A CA  
1970 C C   . MET A 254 ? 0.21942 0.18928 0.30743 -0.02955 -0.01469 -0.01598 254 MET A C   
1971 O O   . MET A 254 ? 0.21869 0.19669 0.31744 -0.03336 -0.01993 -0.01203 254 MET A O   
1972 C CB  . MET A 254 ? 0.23958 0.18880 0.31664 -0.02190 -0.01774 -0.02311 254 MET A CB  
1973 C CG  . MET A 254 ? 0.26075 0.19440 0.32598 -0.01686 -0.02488 -0.02736 254 MET A CG  
1974 S SD  . MET A 254 ? 0.20434 0.13997 0.27612 -0.02106 -0.04012 -0.02627 254 MET A SD  
1975 C CE  . MET A 254 ? 0.26507 0.19218 0.31811 -0.01507 -0.04223 -0.02941 254 MET A CE  
1976 N N   . LEU A 255 ? 0.20087 0.17147 0.28640 -0.02959 -0.00604 -0.01663 255 LEU A N   
1977 C CA  . LEU A 255 ? 0.21949 0.19976 0.31440 -0.03406 -0.00468 -0.01399 255 LEU A CA  
1978 C C   . LEU A 255 ? 0.21699 0.19995 0.30563 -0.03508 -0.00297 -0.01125 255 LEU A C   
1979 O O   . LEU A 255 ? 0.21397 0.20057 0.30464 -0.03770 -0.00097 -0.01022 255 LEU A O   
1980 C CB  . LEU A 255 ? 0.21871 0.19927 0.31900 -0.03468 0.00185  -0.01637 255 LEU A CB  
1981 C CG  . LEU A 255 ? 0.22457 0.20389 0.33263 -0.03246 0.00152  -0.01820 255 LEU A CG  
1982 C CD1 . LEU A 255 ? 0.21223 0.19855 0.33395 -0.03444 0.00593  -0.01879 255 LEU A CD1 
1983 C CD2 . LEU A 255 ? 0.21913 0.20057 0.33300 -0.03294 -0.00764 -0.01650 255 LEU A CD2 
1984 N N   . GLY A 256 ? 0.21690 0.19768 0.29776 -0.03246 -0.00462 -0.01009 256 GLY A N   
1985 C CA  . GLY A 256 ? 0.20479 0.18926 0.28105 -0.03213 -0.00338 -0.00629 256 GLY A CA  
1986 C C   . GLY A 256 ? 0.22167 0.19889 0.28356 -0.02975 0.00429  -0.00783 256 GLY A C   
1987 O O   . GLY A 256 ? 0.20368 0.18215 0.25942 -0.02846 0.00612  -0.00476 256 GLY A O   
1988 N N   . TRP A 257 ? 0.23235 0.20077 0.28790 -0.02842 0.00985  -0.01192 257 TRP A N   
1989 C CA  . TRP A 257 ? 0.24636 0.20604 0.28915 -0.02706 0.01855  -0.01297 257 TRP A CA  
1990 C C   . TRP A 257 ? 0.25227 0.20314 0.27818 -0.02025 0.02062  -0.01315 257 TRP A C   
1991 O O   . TRP A 257 ? 0.27661 0.21741 0.28933 -0.01811 0.02881  -0.01379 257 TRP A O   
1992 C CB  . TRP A 257 ? 0.23683 0.19153 0.28347 -0.02920 0.02563  -0.01606 257 TRP A CB  
1993 C CG  . TRP A 257 ? 0.23523 0.19841 0.29762 -0.03565 0.02359  -0.01610 257 TRP A CG  
1994 C CD1 . TRP A 257 ? 0.22815 0.20044 0.30520 -0.03783 0.01707  -0.01591 257 TRP A CD1 
1995 C CD2 . TRP A 257 ? 0.24520 0.20716 0.30914 -0.04028 0.02666  -0.01666 257 TRP A CD2 
1996 N NE1 . TRP A 257 ? 0.22819 0.20586 0.31563 -0.04277 0.01555  -0.01631 257 TRP A NE1 
1997 C CE2 . TRP A 257 ? 0.23623 0.20763 0.31631 -0.04478 0.02067  -0.01712 257 TRP A CE2 
1998 C CE3 . TRP A 257 ? 0.27342 0.22556 0.32578 -0.04089 0.03329  -0.01708 257 TRP A CE3 
1999 C CZ2 . TRP A 257 ? 0.24258 0.21445 0.32817 -0.05001 0.01950  -0.01857 257 TRP A CZ2 
2000 C CZ3 . TRP A 257 ? 0.26902 0.22060 0.32709 -0.04690 0.03285  -0.01847 257 TRP A CZ3 
2001 C CH2 . TRP A 257 ? 0.25950 0.22115 0.33431 -0.05146 0.02527  -0.01949 257 TRP A CH2 
2002 N N   . ARG A 258 ? 0.25001 0.20353 0.27606 -0.01672 0.01288  -0.01265 258 ARG A N   
2003 C CA  . ARG A 258 ? 0.26068 0.20594 0.27068 -0.00924 0.01262  -0.01335 258 ARG A CA  
2004 C C   . ARG A 258 ? 0.26402 0.22010 0.28119 -0.00786 0.00335  -0.00995 258 ARG A C   
2005 O O   . ARG A 258 ? 0.26053 0.22788 0.29506 -0.01234 -0.00373 -0.00789 258 ARG A O   
2006 C CB  . ARG A 258 ? 0.27171 0.20463 0.27158 -0.00418 0.01199  -0.01775 258 ARG A CB  
2007 C CG  . ARG A 258 ? 0.28252 0.20398 0.27426 -0.00365 0.02436  -0.01963 258 ARG A CG  
2008 C CD  . ARG A 258 ? 0.30999 0.21728 0.28935 0.00297  0.02608  -0.02316 258 ARG A CD  
2009 N NE  . ARG A 258 ? 0.32946 0.22625 0.30239 0.00402  0.04091  -0.02331 258 ARG A NE  
2010 C CZ  . ARG A 258 ? 0.34896 0.22857 0.29981 0.01164  0.05046  -0.02351 258 ARG A CZ  
2011 N NH1 . ARG A 258 ? 0.36495 0.23464 0.29519 0.02029  0.04544  -0.02450 258 ARG A NH1 
2012 N NH2 . ARG A 258 ? 0.36737 0.23954 0.31764 0.01075  0.06541  -0.02234 258 ARG A NH2 
2013 N N   . THR A 259 ? 0.27510 0.22784 0.27984 -0.00137 0.00417  -0.00877 259 THR A N   
2014 C CA  . THR A 259 ? 0.27731 0.24149 0.29103 0.00113  -0.00463 -0.00530 259 THR A CA  
2015 C C   . THR A 259 ? 0.28148 0.24648 0.30319 0.00107  -0.01690 -0.00842 259 THR A C   
2016 O O   . THR A 259 ? 0.29450 0.24536 0.30268 0.00453  -0.01798 -0.01389 259 THR A O   
2017 C CB  . THR A 259 ? 0.27722 0.23602 0.27420 0.00988  -0.00161 -0.00412 259 THR A CB  
2018 O OG1 . THR A 259 ? 0.27885 0.23627 0.26913 0.00948  0.00877  -0.00090 259 THR A OG1 
2019 C CG2 . THR A 259 ? 0.27938 0.25172 0.28870 0.01332  -0.01173 -0.00065 259 THR A CG2 
2020 N N   . MET A 260 ? 0.26684 0.24688 0.31024 -0.00283 -0.02575 -0.00474 260 MET A N   
2021 C CA  . MET A 260 ? 0.25866 0.23901 0.31243 -0.00464 -0.03893 -0.00774 260 MET A CA  
2022 C C   . MET A 260 ? 0.26956 0.26176 0.33641 -0.00241 -0.04923 -0.00469 260 MET A C   
2023 O O   . MET A 260 ? 0.28085 0.28212 0.34926 0.00115  -0.04488 0.00038  260 MET A O   
2024 C CB  . MET A 260 ? 0.25095 0.23734 0.32312 -0.01334 -0.04074 -0.00628 260 MET A CB  
2025 C CG  . MET A 260 ? 0.25408 0.23286 0.31803 -0.01554 -0.03084 -0.00833 260 MET A CG  
2026 S SD  . MET A 260 ? 0.22504 0.18338 0.26961 -0.01107 -0.03033 -0.01663 260 MET A SD  
2027 C CE  . MET A 260 ? 0.24516 0.20422 0.30559 -0.01624 -0.04207 -0.01819 260 MET A CE  
2028 N N   . LYS A 261 ? 0.26418 0.25612 0.34142 -0.00432 -0.06357 -0.00785 261 LYS A N   
2029 C CA  . LYS A 261 ? 0.28575 0.28797 0.37669 -0.00205 -0.07633 -0.00645 261 LYS A CA  
2030 C C   . LYS A 261 ? 0.28078 0.29392 0.40205 -0.01134 -0.08789 -0.00442 261 LYS A C   
2031 O O   . LYS A 261 ? 0.28043 0.28167 0.39945 -0.01357 -0.09901 -0.01087 261 LYS A O   
2032 C CB  . LYS A 261 ? 0.30420 0.28945 0.37097 0.00746  -0.08549 -0.01436 261 LYS A CB  
2033 C CG  . LYS A 261 ? 0.31143 0.30604 0.39166 0.01061  -0.10218 -0.01451 261 LYS A CG  
2034 C CD  . LYS A 261 ? 0.32037 0.33496 0.41429 0.01357  -0.09654 -0.00614 261 LYS A CD  
2035 C CE  . LYS A 261 ? 0.33440 0.35819 0.44064 0.01861  -0.11386 -0.00691 261 LYS A CE  
2036 N NZ  . LYS A 261 ? 0.32666 0.35834 0.46228 0.00961  -0.13198 -0.00856 261 LYS A NZ  
2037 N N   . PRO A 262 ? 0.26089 0.29477 0.40986 -0.01648 -0.08493 0.00478  262 PRO A N   
2038 C CA  . PRO A 262 ? 0.26409 0.30951 0.44534 -0.02486 -0.09679 0.00775  262 PRO A CA  
2039 C C   . PRO A 262 ? 0.28841 0.33684 0.47791 -0.02171 -0.11449 0.00403  262 PRO A C   
2040 O O   . PRO A 262 ? 0.31150 0.35980 0.48728 -0.01238 -0.11527 0.00257  262 PRO A O   
2041 C CB  . PRO A 262 ? 0.23611 0.30267 0.44176 -0.02842 -0.08556 0.02003  262 PRO A CB  
2042 C CG  . PRO A 262 ? 0.23102 0.29318 0.41282 -0.02240 -0.06880 0.02181  262 PRO A CG  
2043 C CD  . PRO A 262 ? 0.24862 0.29512 0.40027 -0.01397 -0.07069 0.01327  262 PRO A CD  
2044 N N   . SER A 263 ? 0.27796 0.32757 0.48932 -0.02940 -0.12989 0.00209  263 SER A N   
2045 C CA  . SER A 263 ? 0.27094 0.32338 0.49322 -0.02751 -0.15010 -0.00220 263 SER A CA  
2046 C C   . SER A 263 ? 0.28232 0.36048 0.52826 -0.02418 -0.14857 0.00652  263 SER A C   
2047 O O   . SER A 263 ? 0.26060 0.35618 0.52240 -0.02587 -0.13291 0.01733  263 SER A O   
2048 C CB  . SER A 263 ? 0.27651 0.32697 0.52170 -0.03792 -0.16407 -0.00389 263 SER A CB  
2049 O OG  . SER A 263 ? 0.26716 0.33607 0.54186 -0.04563 -0.15243 0.00782  263 SER A OG  
2050 N N   . ASP A 264 ? 0.29345 0.37291 0.54016 -0.01811 -0.16531 0.00171  264 ASP A N   
2051 C CA  . ASP A 264 ? 0.28609 0.39222 0.56149 -0.01511 -0.16715 0.00994  264 ASP A CA  
2052 C C   . ASP A 264 ? 0.26190 0.38523 0.57328 -0.02657 -0.15966 0.01972  264 ASP A C   
2053 O O   . ASP A 264 ? 0.26497 0.37740 0.58029 -0.03581 -0.16273 0.01720  264 ASP A O   
2054 C CB  . ASP A 264 ? 0.30611 0.40653 0.57261 -0.00727 -0.18666 0.00182  264 ASP A CB  
2055 C CG  . ASP A 264 ? 0.34065 0.41716 0.55910 0.00688  -0.18759 -0.00723 264 ASP A CG  
2056 O OD1 . ASP A 264 ? 0.33766 0.40290 0.52788 0.01056  -0.16736 -0.00600 264 ASP A OD1 
2057 O OD2 . ASP A 264 ? 0.36351 0.42983 0.56909 0.01456  -0.20670 -0.01556 264 ASP A OD2 
2058 N N   . PRO A 265 ? 0.24213 0.39044 0.57788 -0.02484 -0.14854 0.03146  265 PRO A N   
2059 C CA  . PRO A 265 ? 0.24126 0.40579 0.57855 -0.01305 -0.14471 0.03658  265 PRO A CA  
2060 C C   . PRO A 265 ? 0.26699 0.42498 0.57634 -0.00462 -0.12737 0.03915  265 PRO A C   
2061 O O   . PRO A 265 ? 0.27341 0.44018 0.57690 0.00607  -0.11962 0.04390  265 PRO A O   
2062 C CB  . PRO A 265 ? 0.20629 0.39550 0.57915 -0.01692 -0.13467 0.04903  265 PRO A CB  
2063 C CG  . PRO A 265 ? 0.20145 0.38608 0.58189 -0.02779 -0.12298 0.05397  265 PRO A CG  
2064 C CD  . PRO A 265 ? 0.22800 0.38852 0.59147 -0.03430 -0.13646 0.04196  265 PRO A CD  
2065 N N   . ASN A 266 ? 0.27112 0.40932 0.55466 -0.00842 -0.11715 0.03545  266 ASN A N   
2066 C CA  . ASN A 266 ? 0.26501 0.38844 0.50977 -0.00029 -0.09981 0.03445  266 ASN A CA  
2067 C C   . ASN A 266 ? 0.29657 0.39885 0.50553 0.00879  -0.10839 0.02302  266 ASN A C   
2068 O O   . ASN A 266 ? 0.32634 0.40811 0.51600 0.00630  -0.11513 0.01356  266 ASN A O   
2069 C CB  . ASN A 266 ? 0.24160 0.35266 0.47405 -0.00732 -0.08760 0.03428  266 ASN A CB  
2070 C CG  . ASN A 266 ? 0.24757 0.34734 0.44752 -0.00034 -0.06976 0.03488  266 ASN A CG  
2071 O OD1 . ASN A 266 ? 0.26237 0.35265 0.43709 0.00923  -0.06841 0.03084  266 ASN A OD1 
2072 N ND2 . ASN A 266 ? 0.24552 0.34480 0.44520 -0.00494 -0.05653 0.03988  266 ASN A ND2 
2073 N N   . ILE A 267 ? 0.30417 0.41014 0.50264 0.02054  -0.10712 0.02443  267 ILE A N   
2074 C CA  . ILE A 267 ? 0.33338 0.41880 0.49647 0.03134  -0.11443 0.01490  267 ILE A CA  
2075 C C   . ILE A 267 ? 0.33744 0.40373 0.46089 0.03842  -0.09577 0.01384  267 ILE A C   
2076 O O   . ILE A 267 ? 0.36041 0.40787 0.45131 0.04857  -0.09736 0.00757  267 ILE A O   
2077 C CB  . ILE A 267 ? 0.35509 0.45455 0.53054 0.04086  -0.12766 0.01626  267 ILE A CB  
2078 C CG1 . ILE A 267 ? 0.34551 0.47044 0.54425 0.04432  -0.11493 0.02911  267 ILE A CG1 
2079 C CG2 . ILE A 267 ? 0.33317 0.44224 0.53916 0.03418  -0.15197 0.01242  267 ILE A CG2 
2080 C CD1 . ILE A 267 ? 0.36153 0.50591 0.58078 0.05338  -0.12785 0.03213  267 ILE A CD1 
2081 N N   . VAL A 268 ? 0.34748 0.41683 0.47251 0.03342  -0.07843 0.01987  268 VAL A N   
2082 C CA  . VAL A 268 ? 0.35222 0.40421 0.44388 0.03810  -0.06124 0.01912  268 VAL A CA  
2083 C C   . VAL A 268 ? 0.34063 0.37705 0.42030 0.02959  -0.05563 0.01414  268 VAL A C   
2084 O O   . VAL A 268 ? 0.34732 0.36216 0.39749 0.03292  -0.05183 0.00746  268 VAL A O   
2085 C CB  . VAL A 268 ? 0.34177 0.40649 0.43990 0.04107  -0.04622 0.02932  268 VAL A CB  
2086 C CG1 . VAL A 268 ? 0.36584 0.41013 0.42882 0.04546  -0.03059 0.02755  268 VAL A CG1 
2087 C CG2 . VAL A 268 ? 0.35191 0.43449 0.46537 0.05038  -0.05124 0.03519  268 VAL A CG2 
2088 N N   . GLY A 269 ? 0.28551 0.37149 0.44277 -0.00313 -0.07349 0.00166  269 GLY A N   
2089 C CA  . GLY A 269 ? 0.26384 0.31926 0.40190 -0.00917 -0.06725 0.00145  269 GLY A CA  
2090 C C   . GLY A 269 ? 0.24273 0.28630 0.38427 -0.01256 -0.05813 -0.00359 269 GLY A C   
2091 O O   . GLY A 269 ? 0.23134 0.28817 0.38568 -0.01543 -0.05465 -0.00989 269 GLY A O   
2092 N N   . ILE A 270 ? 0.23130 0.25314 0.36162 -0.01210 -0.05422 -0.00070 270 ILE A N   
2093 C CA  . ILE A 270 ? 0.22119 0.23361 0.34864 -0.01578 -0.04742 -0.00491 270 ILE A CA  
2094 C C   . ILE A 270 ? 0.22313 0.22150 0.34411 -0.01280 -0.04718 0.00002  270 ILE A C   
2095 O O   . ILE A 270 ? 0.24806 0.24132 0.36382 -0.01023 -0.04971 0.00643  270 ILE A O   
2096 C CB  . ILE A 270 ? 0.22733 0.23574 0.34242 -0.02537 -0.04224 -0.00898 270 ILE A CB  
2097 C CG1 . ILE A 270 ? 0.21122 0.21509 0.32318 -0.02770 -0.03503 -0.01267 270 ILE A CG1 
2098 C CG2 . ILE A 270 ? 0.24160 0.23425 0.33832 -0.02646 -0.04115 -0.00414 270 ILE A CG2 
2099 C CD1 . ILE A 270 ? 0.21518 0.21468 0.31749 -0.03668 -0.02699 -0.01616 270 ILE A CD1 
2100 N N   . ASN A 271 ? 0.20811 0.20274 0.32962 -0.01408 -0.04393 -0.00363 271 ASN A N   
2101 C CA  . ASN A 271 ? 0.22243 0.21088 0.34150 -0.01434 -0.04444 -0.00126 271 ASN A CA  
2102 C C   . ASN A 271 ? 0.22379 0.20619 0.35240 -0.01049 -0.04488 0.00204  271 ASN A C   
2103 O O   . ASN A 271 ? 0.22346 0.20158 0.35023 -0.00986 -0.04557 0.00852  271 ASN A O   
2104 C CB  . ASN A 271 ? 0.22889 0.21577 0.33655 -0.01450 -0.04502 0.00513  271 ASN A CB  
2105 C CG  . ASN A 271 ? 0.20795 0.19936 0.31491 -0.01593 -0.04573 0.00610  271 ASN A CG  
2106 O OD1 . ASN A 271 ? 0.20506 0.20135 0.31277 -0.01963 -0.04612 -0.00026 271 ASN A OD1 
2107 N ND2 . ASN A 271 ? 0.20262 0.19537 0.30800 -0.01329 -0.04579 0.01352  271 ASN A ND2 
2108 N N   . LEU A 272 ? 0.21512 0.19537 0.35350 -0.00674 -0.04227 -0.00151 272 LEU A N   
2109 C CA  . LEU A 272 ? 0.23466 0.20299 0.38039 -0.00079 -0.03940 0.00279  272 LEU A CA  
2110 C C   . LEU A 272 ? 0.23600 0.19245 0.38657 -0.00323 -0.03188 -0.00652 272 LEU A C   
2111 O O   . LEU A 272 ? 0.24346 0.20458 0.39086 -0.00898 -0.03033 -0.01628 272 LEU A O   
2112 C CB  . LEU A 272 ? 0.23728 0.21270 0.38900 0.01060  -0.04211 0.01003  272 LEU A CB  
2113 C CG  . LEU A 272 ? 0.21957 0.21420 0.37905 0.01246  -0.04374 0.00491  272 LEU A CG  
2114 C CD1 . LEU A 272 ? 0.22604 0.21723 0.39704 0.01731  -0.03573 -0.00153 272 LEU A CD1 
2115 C CD2 . LEU A 272 ? 0.24723 0.25978 0.41057 0.01987  -0.05104 0.01223  272 LEU A CD2 
2116 N N   . ILE A 273 ? 0.24809 0.18564 0.40335 0.00090  -0.02539 -0.00376 273 ILE A N   
2117 C CA  . ILE A 273 ? 0.27270 0.19200 0.42988 -0.00278 -0.01533 -0.01452 273 ILE A CA  
2118 C C   . ILE A 273 ? 0.30345 0.19772 0.46563 0.00758  -0.00588 -0.00695 273 ILE A C   
2119 O O   . ILE A 273 ? 0.31717 0.20599 0.47798 0.01183  -0.00718 0.00552  273 ILE A O   
2120 C CB  . ILE A 273 ? 0.26932 0.18681 0.41977 -0.02043 -0.01531 -0.02523 273 ILE A CB  
2121 C CG1 . ILE A 273 ? 0.28456 0.18373 0.43251 -0.02767 -0.00496 -0.04083 273 ILE A CG1 
2122 C CG2 . ILE A 273 ? 0.28378 0.19477 0.43562 -0.02635 -0.01514 -0.01847 273 ILE A CG2 
2123 C CD1 . ILE A 273 ? 0.26692 0.17376 0.41139 -0.02418 -0.00306 -0.04956 273 ILE A CD1 
2124 N N   . ASP A 274 ? 0.29917 0.17569 0.46508 0.01312  0.00556  -0.01368 274 ASP A N   
2125 C CA  . ASP A 274 ? 0.33152 0.17804 0.50077 0.02630  0.01821  -0.00550 274 ASP A CA  
2126 C C   . ASP A 274 ? 0.36003 0.22060 0.53499 0.04697  0.01174  0.01399  274 ASP A C   
2127 O O   . ASP A 274 ? 0.39031 0.22897 0.56375 0.05925  0.01896  0.02732  274 ASP A O   
2128 C CB  . ASP A 274 ? 0.34180 0.15810 0.50434 0.01327  0.02694  -0.00670 274 ASP A CB  
2129 C CG  . ASP A 274 ? 0.37032 0.17436 0.52754 -0.00834 0.03357  -0.02811 274 ASP A CG  
2130 O OD1 . ASP A 274 ? 0.35936 0.16126 0.51515 -0.00777 0.03851  -0.04080 274 ASP A OD1 
2131 O OD2 . ASP A 274 ? 0.40811 0.20709 0.56249 -0.02658 0.03405  -0.03287 274 ASP A OD2 
2132 N N   . ASP A 275 ? 0.35294 0.25023 0.53266 0.04983  -0.00158 0.01552  275 ASP A N   
2133 C CA  . ASP A 275 ? 0.39281 0.31366 0.57695 0.06521  -0.01155 0.03070  275 ASP A CA  
2134 C C   . ASP A 275 ? 0.42184 0.33660 0.59335 0.06380  -0.01684 0.04306  275 ASP A C   
2135 O O   . ASP A 275 ? 0.46442 0.38574 0.63400 0.07923  -0.02103 0.05842  275 ASP A O   
2136 C CB  . ASP A 275 ? 0.44978 0.36795 0.64598 0.08920  -0.00433 0.04041  275 ASP A CB  
2137 C CG  . ASP A 275 ? 0.50655 0.46676 0.71289 0.10287  -0.01788 0.05054  275 ASP A CG  
2138 O OD1 . ASP A 275 ? 0.48929 0.47966 0.69585 0.09032  -0.03002 0.04378  275 ASP A OD1 
2139 O OD2 . ASP A 275 ? 0.58042 0.54370 0.79396 0.12598  -0.01594 0.06530  275 ASP A OD2 
2140 N N   . LYS A 276 ? 0.38622 0.29099 0.54876 0.04620  -0.01640 0.03702  276 LYS A N   
2141 C CA  . LYS A 276 ? 0.39545 0.29524 0.54666 0.04306  -0.01893 0.04712  276 LYS A CA  
2142 C C   . LYS A 276 ? 0.32792 0.24597 0.47412 0.02804  -0.02722 0.03971  276 LYS A C   
2143 O O   . LYS A 276 ? 0.29831 0.22835 0.44814 0.01962  -0.03001 0.02772  276 LYS A O   
2144 C CB  . LYS A 276 ? 0.39971 0.26425 0.54762 0.03808  -0.00480 0.04986  276 LYS A CB  
2145 C CG  . LYS A 276 ? 0.43890 0.27653 0.58598 0.05591  0.00641  0.06277  276 LYS A CG  
2146 C CD  . LYS A 276 ? 0.45235 0.25034 0.60062 0.04616  0.02474  0.05519  276 LYS A CD  
2147 C CE  . LYS A 276 ? 0.52602 0.29634 0.66021 0.06062  0.03760  0.06816  276 LYS A CE  
2148 N NZ  . LYS A 276 ? 0.65367 0.43768 0.78957 0.08623  0.03288  0.07851  276 LYS A NZ  
2149 N N   . ARG A 277 ? 0.32718 0.24516 0.46322 0.02630  -0.02935 0.04810  277 ARG A N   
2150 C CA  . ARG A 277 ? 0.30963 0.24123 0.44037 0.01539  -0.03437 0.04329  277 ARG A CA  
2151 C C   . ARG A 277 ? 0.29426 0.21983 0.43083 0.00196  -0.02858 0.03550  277 ARG A C   
2152 O O   . ARG A 277 ? 0.30365 0.21112 0.44406 -0.00191 -0.01954 0.03686  277 ARG A O   
2153 C CB  . ARG A 277 ? 0.30689 0.23981 0.42370 0.01902  -0.03645 0.05417  277 ARG A CB  
2154 C CG  . ARG A 277 ? 0.33261 0.27888 0.44154 0.02937  -0.04518 0.05941  277 ARG A CG  
2155 C CD  . ARG A 277 ? 0.36291 0.31120 0.45277 0.03033  -0.04763 0.06653  277 ARG A CD  
2156 N NE  . ARG A 277 ? 0.38766 0.34600 0.46766 0.04189  -0.05511 0.07505  277 ARG A NE  
2157 C CZ  . ARG A 277 ? 0.38550 0.36820 0.46636 0.04272  -0.06601 0.06970  277 ARG A CZ  
2158 N NH1 . ARG A 277 ? 0.39710 0.39142 0.48738 0.03276  -0.06849 0.05631  277 ARG A NH1 
2159 N NH2 . ARG A 277 ? 0.39801 0.39557 0.46975 0.05337  -0.07437 0.07835  277 ARG A NH2 
2160 N N   . LEU A 278 ? 0.26856 0.21035 0.40532 -0.00554 -0.03349 0.02742  278 LEU A N   
2161 C CA  . LEU A 278 ? 0.26363 0.21000 0.40639 -0.01772 -0.03141 0.01962  278 LEU A CA  
2162 C C   . LEU A 278 ? 0.26359 0.20652 0.40997 -0.02330 -0.02566 0.02560  278 LEU A C   
2163 O O   . LEU A 278 ? 0.26161 0.19989 0.41692 -0.03452 -0.02001 0.01971  278 LEU A O   
2164 C CB  . LEU A 278 ? 0.22985 0.19596 0.36837 -0.01979 -0.03805 0.01547  278 LEU A CB  
2165 C CG  . LEU A 278 ? 0.21596 0.19737 0.35936 -0.02930 -0.03933 0.01025  278 LEU A CG  
2166 C CD1 . LEU A 278 ? 0.24325 0.22015 0.39257 -0.03969 -0.03697 -0.00189 278 LEU A CD1 
2167 C CD2 . LEU A 278 ? 0.20211 0.19869 0.33730 -0.02607 -0.04466 0.00995  278 LEU A CD2 
2168 N N   . GLU A 279 ? 0.25496 0.20061 0.39416 -0.01731 -0.02577 0.03600  279 GLU A N   
2169 C CA  . GLU A 279 ? 0.26378 0.20827 0.40724 -0.02228 -0.01818 0.04228  279 GLU A CA  
2170 C C   . GLU A 279 ? 0.28366 0.20267 0.42839 -0.02360 -0.00772 0.04733  279 GLU A C   
2171 O O   . GLU A 279 ? 0.28938 0.20517 0.44326 -0.03425 0.00141  0.04769  279 GLU A O   
2172 C CB  . GLU A 279 ? 0.26066 0.21049 0.39235 -0.01435 -0.01836 0.05165  279 GLU A CB  
2173 C CG  . GLU A 279 ? 0.26014 0.19767 0.37419 -0.00317 -0.02069 0.05885  279 GLU A CG  
2174 C CD  . GLU A 279 ? 0.27277 0.21845 0.38032 0.00098  -0.03050 0.05284  279 GLU A CD  
2175 O OE1 . GLU A 279 ? 0.25925 0.21241 0.37552 -0.00311 -0.03418 0.04382  279 GLU A OE1 
2176 O OE2 . GLU A 279 ? 0.28230 0.22751 0.37487 0.00697  -0.03392 0.05647  279 GLU A OE2 
2177 N N   . ASN A 280 ? 0.29553 0.19708 0.43208 -0.01260 -0.00779 0.05194  280 ASN A N   
2178 C CA  . ASN A 280 ? 0.31109 0.18282 0.44699 -0.01056 0.00416  0.05825  280 ASN A CA  
2179 C C   . ASN A 280 ? 0.30475 0.16436 0.45314 -0.02457 0.01165  0.04493  280 ASN A C   
2180 O O   . ASN A 280 ? 0.31277 0.15409 0.46594 -0.03580 0.02464  0.04488  280 ASN A O   
2181 C CB  . ASN A 280 ? 0.31976 0.18156 0.44605 0.00807  0.00107  0.06707  280 ASN A CB  
2182 C CG  . ASN A 280 ? 0.35863 0.22934 0.46866 0.01996  -0.00512 0.08020  280 ASN A CG  
2183 O OD1 . ASN A 280 ? 0.36572 0.24574 0.46971 0.01494  -0.00542 0.08220  280 ASN A OD1 
2184 N ND2 . ASN A 280 ? 0.40501 0.27518 0.50752 0.03628  -0.01001 0.08878  280 ASN A ND2 
2185 N N   . VAL A 281 ? 0.29640 0.16443 0.44853 -0.02548 0.00503  0.03253  281 VAL A N   
2186 C CA  . VAL A 281 ? 0.29711 0.15577 0.45689 -0.04042 0.01107  0.01643  281 VAL A CA  
2187 C C   . VAL A 281 ? 0.30263 0.17739 0.47224 -0.06113 0.01213  0.00855  281 VAL A C   
2188 O O   . VAL A 281 ? 0.31880 0.17886 0.49448 -0.07802 0.02208  -0.00232 281 VAL A O   
2189 C CB  . VAL A 281 ? 0.28944 0.16212 0.44840 -0.03783 0.00225  0.00478  281 VAL A CB  
2190 C CG1 . VAL A 281 ? 0.31396 0.17929 0.47613 -0.05490 0.00768  -0.01400 281 VAL A CG1 
2191 C CG2 . VAL A 281 ? 0.31246 0.17329 0.46749 -0.01818 0.00302  0.01194  281 VAL A CG2 
2192 N N   . LEU A 282 ? 0.29412 0.19980 0.46628 -0.06052 0.00308  0.01350  282 LEU A N   
2193 C CA  . LEU A 282 ? 0.26991 0.20183 0.45564 -0.07737 0.00217  0.00718  282 LEU A CA  
2194 C C   . LEU A 282 ? 0.29466 0.22076 0.48770 -0.08336 0.01396  0.01666  282 LEU A C   
2195 O O   . LEU A 282 ? 0.30984 0.26032 0.51919 -0.09936 0.01528  0.01095  282 LEU A O   
2196 C CB  . LEU A 282 ? 0.26643 0.23568 0.45251 -0.07123 -0.01147 0.00865  282 LEU A CB  
2197 C CG  . LEU A 282 ? 0.24737 0.22897 0.42705 -0.06919 -0.02224 -0.00127 282 LEU A CG  
2198 C CD1 . LEU A 282 ? 0.22704 0.23899 0.40495 -0.06111 -0.03186 0.00426  282 LEU A CD1 
2199 C CD2 . LEU A 282 ? 0.24366 0.23059 0.42938 -0.08762 -0.02211 -0.01855 282 LEU A CD2 
2200 N N   . GLN A 283 ? 0.29866 0.19655 0.48029 -0.07105 0.02261  0.03127  283 GLN A N   
2201 C CA  . GLN A 283 ? 0.31424 0.20527 0.49821 -0.07434 0.03528  0.04287  283 GLN A CA  
2202 C C   . GLN A 283 ? 0.31480 0.24530 0.50912 -0.07599 0.02997  0.04515  283 GLN A C   
2203 O O   . GLN A 283 ? 0.30978 0.25449 0.52053 -0.08972 0.03870  0.04476  283 GLN A O   
2204 C CB  . GLN A 283 ? 0.36048 0.22940 0.55514 -0.09471 0.05199  0.03640  283 GLN A CB  
2205 C CG  . GLN A 283 ? 0.40199 0.22424 0.57614 -0.08439 0.06420  0.04422  283 GLN A CG  
2206 C CD  . GLN A 283 ? 0.44001 0.24259 0.61212 -0.10070 0.08057  0.03913  283 GLN A CD  
2207 O OE1 . GLN A 283 ? 0.48021 0.27060 0.65158 -0.11227 0.08358  0.02426  283 GLN A OE1 
2208 N NE2 . GLN A 283 ? 0.45763 0.25628 0.62776 -0.10222 0.09197  0.05118  283 GLN A NE2 
2209 N N   . LEU A 284 ? 0.30692 0.25463 0.49217 -0.06146 0.01708  0.04764  284 LEU A N   
2210 C CA  . LEU A 284 ? 0.28956 0.27312 0.48316 -0.05926 0.01151  0.04884  284 LEU A CA  
2211 C C   . LEU A 284 ? 0.29113 0.27105 0.47743 -0.05058 0.02118  0.06292  284 LEU A C   
2212 O O   . LEU A 284 ? 0.31226 0.27336 0.47597 -0.03655 0.02054  0.07109  284 LEU A O   
2213 C CB  . LEU A 284 ? 0.27695 0.27105 0.46000 -0.04771 -0.00257 0.04562  284 LEU A CB  
2214 C CG  . LEU A 284 ? 0.26227 0.29051 0.45231 -0.04319 -0.00881 0.04609  284 LEU A CG  
2215 C CD1 . LEU A 284 ? 0.24379 0.30533 0.45829 -0.05777 -0.01076 0.03835  284 LEU A CD1 
2216 C CD2 . LEU A 284 ? 0.23999 0.26704 0.41587 -0.03401 -0.01956 0.04246  284 LEU A CD2 
2217 N N   . LYS A 285 ? 0.27665 0.27735 0.48199 -0.05971 0.03034  0.06489  285 LYS A N   
2218 C CA  . LYS A 285 ? 0.28659 0.29017 0.48643 -0.05068 0.04066  0.07715  285 LYS A CA  
2219 C C   . LYS A 285 ? 0.27115 0.29668 0.46658 -0.03613 0.03265  0.07853  285 LYS A C   
2220 O O   . LYS A 285 ? 0.25282 0.30205 0.45862 -0.03619 0.02108  0.07132  285 LYS A O   
2221 C CB  . LYS A 285 ? 0.27545 0.29891 0.50156 -0.06539 0.05490  0.07857  285 LYS A CB  
2222 C CG  . LYS A 285 ? 0.31861 0.32248 0.55464 -0.08563 0.06483  0.07357  285 LYS A CG  
2223 C CD  . LYS A 285 ? 0.34000 0.37368 0.60831 -0.10478 0.07786  0.07158  285 LYS A CD  
2224 C CE  . LYS A 285 ? 0.36377 0.36949 0.63891 -0.12735 0.09315  0.06698  285 LYS A CE  
2225 N NZ  . LYS A 285 ? 0.36505 0.40299 0.66711 -0.14717 0.10442  0.06234  285 LYS A NZ  
2226 N N   . ALA A 286 ? 0.28866 0.30298 0.46543 -0.02331 0.04041  0.08804  286 ALA A N   
2227 C CA  . ALA A 286 ? 0.29848 0.32631 0.46914 -0.00926 0.03884  0.09013  286 ALA A CA  
2228 C C   . ALA A 286 ? 0.32912 0.36052 0.49942 -0.00346 0.05621  0.09963  286 ALA A C   
2229 O O   . ALA A 286 ? 0.34526 0.36192 0.51121 -0.00899 0.06818  0.10531  286 ALA A O   
2230 C CB  . ALA A 286 ? 0.30768 0.31051 0.44696 0.00130  0.03073  0.08836  286 ALA A CB  
2231 N N   . ALA A 287 ? 0.29291 0.34105 0.46563 0.00930  0.05969  0.10233  287 ALA A N   
2232 C CA  . ALA A 287 ? 0.31713 0.37405 0.49458 0.01610  0.07851  0.11089  287 ALA A CA  
2233 C C   . ALA A 287 ? 0.39460 0.41343 0.53489 0.02140  0.09036  0.11582  287 ALA A C   
2234 O O   . ALA A 287 ? 0.42496 0.44562 0.56711 0.02247  0.10844  0.12306  287 ALA A O   
2235 C CB  . ALA A 287 ? 0.28989 0.36976 0.47634 0.03268  0.08131  0.11378  287 ALA A CB  
2236 N N   . ASP A 288 ? 0.42889 0.41661 0.53551 0.02414  0.08092  0.11194  288 ASP A N   
2237 C CA  . ASP A 288 ? 0.48719 0.44422 0.55492 0.02978  0.08996  0.11546  288 ASP A CA  
2238 C C   . ASP A 288 ? 0.47790 0.41179 0.52340 0.02437  0.07945  0.11527  288 ASP A C   
2239 O O   . ASP A 288 ? 0.51211 0.42529 0.52239 0.02910  0.07569  0.11351  288 ASP A O   
2240 C CB  . ASP A 288 ? 0.55408 0.49815 0.59657 0.04154  0.09206  0.11078  288 ASP A CB  
2241 C CG  . ASP A 288 ? 0.47434 0.41271 0.51003 0.04072  0.07410  0.10139  288 ASP A CG  
2242 O OD1 . ASP A 288 ? 0.40205 0.35711 0.46212 0.03477  0.06119  0.09876  288 ASP A OD1 
2243 O OD2 . ASP A 288 ? 0.53304 0.44935 0.53760 0.04466  0.07430  0.09554  288 ASP A OD2 
2244 N N   . SER A 289 ? 0.42870 0.36607 0.49356 0.01470  0.07538  0.11706  289 SER A N   
2245 C CA  . SER A 289 ? 0.46564 0.37979 0.50943 0.01388  0.06864  0.12043  289 SER A CA  
2246 C C   . SER A 289 ? 0.46122 0.36592 0.51552 0.00603  0.07996  0.12941  289 SER A C   
2247 O O   . SER A 289 ? 0.44929 0.36970 0.53569 -0.00462 0.08759  0.12807  289 SER A O   
2248 C CB  . SER A 289 ? 0.42213 0.33853 0.47063 0.01276  0.04895  0.11137  289 SER A CB  
2249 O OG  . SER A 289 ? 0.39776 0.32739 0.47882 0.00312  0.04577  0.10680  289 SER A OG  
2250 N N   . LYS B 6   ? 0.19982 0.54228 0.76748 -0.00549 0.05255  0.04050  6   LYS B N   
2251 C CA  . LYS B 6   ? 0.19229 0.51446 0.73568 -0.01111 0.04983  0.04441  6   LYS B CA  
2252 C C   . LYS B 6   ? 0.19042 0.50136 0.71137 -0.00761 0.06366  0.04829  6   LYS B C   
2253 O O   . LYS B 6   ? 0.18888 0.50022 0.70354 0.00257  0.06663  0.04566  6   LYS B O   
2254 C CB  . LYS B 6   ? 0.18330 0.49647 0.71556 -0.00803 0.03017  0.04248  6   LYS B CB  
2255 C CG  . LYS B 6   ? 0.21506 0.53786 0.76234 -0.01496 0.01528  0.03880  6   LYS B CG  
2256 C CD  . LYS B 6   ? 0.21072 0.52807 0.74420 -0.01148 -0.00360 0.03720  6   LYS B CD  
2257 C CE  . LYS B 6   ? 0.19257 0.48798 0.69774 -0.01106 -0.00298 0.03962  6   LYS B CE  
2258 N NZ  . LYS B 6   ? 0.21601 0.50112 0.71741 -0.02194 0.00498  0.04043  6   LYS B NZ  
2259 N N   . PRO B 7   ? 0.20111 0.50202 0.71037 -0.01611 0.07184  0.05462  7   PRO B N   
2260 C CA  . PRO B 7   ? 0.19915 0.49044 0.68427 -0.01367 0.08358  0.05976  7   PRO B CA  
2261 C C   . PRO B 7   ? 0.18509 0.46388 0.65108 -0.00481 0.07399  0.05739  7   PRO B C   
2262 O O   . PRO B 7   ? 0.18824 0.45593 0.64848 -0.00593 0.05924  0.05688  7   PRO B O   
2263 C CB  . PRO B 7   ? 0.22127 0.50068 0.69896 -0.02466 0.08733  0.06873  7   PRO B CB  
2264 C CG  . PRO B 7   ? 0.23841 0.52582 0.74104 -0.03332 0.08484  0.06726  7   PRO B CG  
2265 C CD  . PRO B 7   ? 0.22210 0.51971 0.74054 -0.02837 0.07030  0.05765  7   PRO B CD  
2266 N N   . GLN B 8   ? 0.18150 0.46268 0.63756 0.00353  0.08305  0.05496  8   GLN B N   
2267 C CA  . GLN B 8   ? 0.19354 0.46383 0.63455 0.01280  0.07511  0.05163  8   GLN B CA  
2268 C C   . GLN B 8   ? 0.20443 0.46259 0.61891 0.01168  0.08128  0.05701  8   GLN B C   
2269 O O   . GLN B 8   ? 0.22063 0.48040 0.62706 0.00493  0.09333  0.06408  8   GLN B O   
2270 C CB  . GLN B 8   ? 0.18785 0.46709 0.63749 0.02353  0.08022  0.04343  8   GLN B CB  
2271 C CG  . GLN B 8   ? 0.18351 0.47751 0.66149 0.02534  0.07588  0.03943  8   GLN B CG  
2272 C CD  . GLN B 8   ? 0.17866 0.46766 0.66279 0.02887  0.05512  0.03929  8   GLN B CD  
2273 O OE1 . GLN B 8   ? 0.20708 0.50766 0.71205 0.02714  0.04713  0.03872  8   GLN B OE1 
2274 N NE2 . GLN B 8   ? 0.20106 0.47419 0.66640 0.03352  0.04623  0.04013  8   GLN B NE2 
2275 N N   . LEU B 9   ? 0.19589 0.44219 0.59647 0.01830  0.07242  0.05472  9   LEU B N   
2276 C CA  . LEU B 9   ? 0.21046 0.44329 0.58087 0.01814  0.07574  0.05807  9   LEU B CA  
2277 C C   . LEU B 9   ? 0.21283 0.45327 0.57010 0.02017  0.09361  0.05603  9   LEU B C   
2278 O O   . LEU B 9   ? 0.21741 0.46650 0.58356 0.02779  0.09997  0.04692  9   LEU B O   
2279 C CB  . LEU B 9   ? 0.21336 0.42919 0.56632 0.02484  0.06184  0.05314  9   LEU B CB  
2280 C CG  . LEU B 9   ? 0.19709 0.40039 0.54548 0.02132  0.04467  0.05526  9   LEU B CG  
2281 C CD1 . LEU B 9   ? 0.18815 0.38292 0.53062 0.02916  0.03302  0.05055  9   LEU B CD1 
2282 C CD2 . LEU B 9   ? 0.18251 0.37015 0.50455 0.01549  0.04452  0.06004  9   LEU B CD2 
2283 N N   . GLN B 10  ? 0.22437 0.46231 0.56103 0.01326  0.10175  0.06441  10  GLN B N   
2284 C CA  . GLN B 10  ? 0.23261 0.47943 0.55029 0.01369  0.11799  0.06295  10  GLN B CA  
2285 C C   . GLN B 10  ? 0.23383 0.46910 0.52486 0.02103  0.11440  0.05312  10  GLN B C   
2286 O O   . GLN B 10  ? 0.23555 0.45239 0.51049 0.02222  0.10091  0.05403  10  GLN B O   
2287 C CB  . GLN B 10  ? 0.24700 0.49368 0.54676 0.00431  0.12505  0.07750  10  GLN B CB  
2288 C CG  . GLN B 10  ? 0.24291 0.50806 0.56548 -0.00358 0.13885  0.08615  10  GLN B CG  
2289 C CD  . GLN B 10  ? 0.26925 0.55262 0.57654 -0.00577 0.15888  0.08702  10  GLN B CD  
2290 O OE1 . GLN B 10  ? 0.29652 0.58640 0.59725 -0.01459 0.16855  0.10125  10  GLN B OE1 
2291 N NE2 . GLN B 10  ? 0.24474 0.53615 0.54627 0.00179  0.16530  0.07141  10  GLN B NE2 
2292 N N   . ARG B 11  ? 0.23370 0.48057 0.52188 0.02542  0.12742  0.04239  11  ARG B N   
2293 C CA  . ARG B 11  ? 0.24635 0.48433 0.51216 0.03153  0.12673  0.03034  11  ARG B CA  
2294 C C   . ARG B 11  ? 0.25114 0.49721 0.48436 0.02653  0.13911  0.03075  11  ARG B C   
2295 O O   . ARG B 11  ? 0.25232 0.51852 0.48866 0.02322  0.15580  0.02995  11  ARG B O   
2296 C CB  . ARG B 11  ? 0.24284 0.48727 0.53307 0.04086  0.13184  0.01475  11  ARG B CB  
2297 C CG  . ARG B 11  ? 0.22981 0.46132 0.54167 0.04817  0.11572  0.01303  11  ARG B CG  
2298 C CD  . ARG B 11  ? 0.21352 0.45381 0.55805 0.04662  0.10942  0.02146  11  ARG B CD  
2299 N NE  . ARG B 11  ? 0.22218 0.45501 0.58771 0.05433  0.09502  0.01941  11  ARG B NE  
2300 C CZ  . ARG B 11  ? 0.20675 0.44339 0.59497 0.05317  0.08292  0.02649  11  ARG B CZ  
2301 N NH1 . ARG B 11  ? 0.18740 0.43220 0.58071 0.04414  0.08306  0.03412  11  ARG B NH1 
2302 N NH2 . ARG B 11  ? 0.20920 0.43700 0.60623 0.05951  0.06829  0.02532  11  ARG B NH2 
2303 N N   . LEU B 12  ? 0.30541 0.53801 0.50749 0.02559  0.13104  0.03200  12  LEU B N   
2304 C CA  . LEU B 12  ? 0.33943 0.58078 0.50780 0.02048  0.13948  0.03378  12  LEU B CA  
2305 C C   . LEU B 12  ? 0.35889 0.59436 0.50708 0.02499  0.13798  0.01683  12  LEU B C   
2306 O O   . LEU B 12  ? 0.34864 0.56669 0.50336 0.03070  0.12636  0.00976  12  LEU B O   
2307 C CB  . LEU B 12  ? 0.34008 0.57375 0.48967 0.01376  0.13089  0.05342  12  LEU B CB  
2308 C CG  . LEU B 12  ? 0.31074 0.55392 0.47092 0.00613  0.13737  0.07206  12  LEU B CG  
2309 C CD1 . LEU B 12  ? 0.29706 0.53603 0.49491 0.00711  0.13303  0.07362  12  LEU B CD1 
2310 C CD2 . LEU B 12  ? 0.32985 0.56422 0.47020 0.00080  0.12933  0.09047  12  LEU B CD2 
2311 N N   . ALA B 13  ? 0.36805 0.61915 0.49172 0.02155  0.15020  0.01011  13  ALA B N   
2312 C CA  . ALA B 13  ? 0.39505 0.64255 0.49769 0.02390  0.14931  -0.00737 13  ALA B CA  
2313 C C   . ALA B 13  ? 0.42987 0.66390 0.50640 0.02114  0.13376  0.00185  13  ALA B C   
2314 O O   . ALA B 13  ? 0.43571 0.66862 0.50415 0.01638  0.12765  0.02192  13  ALA B O   
2315 C CB  . ALA B 13  ? 0.40494 0.67654 0.48793 0.01984  0.16745  -0.01940 13  ALA B CB  
2316 N N   . ALA B 14  ? 0.43893 0.66252 0.50554 0.02423  0.12766  -0.01334 14  ALA B N   
2317 C CA  . ALA B 14  ? 0.41696 0.62750 0.46423 0.02238  0.11225  -0.00645 14  ALA B CA  
2318 C C   . ALA B 14  ? 0.45084 0.67575 0.46767 0.01497  0.11225  0.00744  14  ALA B C   
2319 O O   . ALA B 14  ? 0.44372 0.65977 0.45286 0.01322  0.09957  0.02249  14  ALA B O   
2320 C CB  . ALA B 14  ? 0.39578 0.59661 0.43697 0.02537  0.10844  -0.02680 14  ALA B CB  
2321 N N   . ASP B 15  ? 0.46563 0.71369 0.46569 0.01054  0.12643  0.00333  15  ASP B N   
2322 C CA  . ASP B 15  ? 0.46334 0.72830 0.43216 0.00302  0.12673  0.01851  15  ASP B CA  
2323 C C   . ASP B 15  ? 0.47826 0.75309 0.45423 -0.00121 0.13426  0.04102  15  ASP B C   
2324 O O   . ASP B 15  ? 0.48879 0.78389 0.44059 -0.00804 0.14122  0.05223  15  ASP B O   
2325 C CB  . ASP B 15  ? 0.46006 0.74702 0.39976 -0.00114 0.13693  0.00061  15  ASP B CB  
2326 C CG  . ASP B 15  ? 0.49297 0.79296 0.44559 0.00013  0.15669  -0.01871 15  ASP B CG  
2327 O OD1 . ASP B 15  ? 0.48308 0.77565 0.46894 0.00480  0.16169  -0.01723 15  ASP B OD1 
2328 O OD2 . ASP B 15  ? 0.47885 0.79811 0.40898 -0.00372 0.16723  -0.03666 15  ASP B OD2 
2329 N N   . ALA B 16  ? 0.54723 0.80887 0.55605 0.00200  0.13275  0.04830  16  ALA B N   
2330 C CA  . ALA B 16  ? 0.52702 0.79541 0.54797 -0.00265 0.13907  0.06937  16  ALA B CA  
2331 C C   . ALA B 16  ? 0.52930 0.79324 0.53593 -0.00714 0.12850  0.09467  16  ALA B C   
2332 O O   . ALA B 16  ? 0.55820 0.81288 0.54965 -0.00561 0.11494  0.09558  16  ALA B O   
2333 C CB  . ALA B 16  ? 0.49549 0.75068 0.55617 0.00147  0.13738  0.06888  16  ALA B CB  
2334 N N   . ASP B 17  ? 0.45211 0.72282 0.46683 -0.01270 0.13511  0.11579  17  ASP B N   
2335 C CA  . ASP B 17  ? 0.42784 0.69590 0.43178 -0.01710 0.12727  0.14235  17  ASP B CA  
2336 C C   . ASP B 17  ? 0.41051 0.65236 0.43984 -0.01344 0.11237  0.14928  17  ASP B C   
2337 O O   . ASP B 17  ? 0.40111 0.63380 0.46157 -0.01310 0.11431  0.14944  17  ASP B O   
2338 C CB  . ASP B 17  ? 0.41522 0.69937 0.42047 -0.02512 0.14117  0.16324  17  ASP B CB  
2339 C CG  . ASP B 17  ? 0.41655 0.70557 0.39995 -0.03024 0.13564  0.19098  17  ASP B CG  
2340 O OD1 . ASP B 17  ? 0.46763 0.74568 0.44093 -0.02682 0.11966  0.19471  17  ASP B OD1 
2341 O OD2 . ASP B 17  ? 0.43005 0.73047 0.40793 -0.03721 0.14532  0.20718  17  ASP B OD2 
2342 N N   . VAL B 18  ? 0.41312 0.64484 0.42985 -0.01118 0.09772  0.15403  18  VAL B N   
2343 C CA  . VAL B 18  ? 0.39582 0.60374 0.43531 -0.00771 0.08432  0.15766  18  VAL B CA  
2344 C C   . VAL B 18  ? 0.37923 0.58071 0.44224 -0.01194 0.08621  0.17980  18  VAL B C   
2345 O O   . VAL B 18  ? 0.37232 0.55633 0.46327 -0.01053 0.08072  0.17821  18  VAL B O   
2346 C CB  . VAL B 18  ? 0.39001 0.59190 0.41206 -0.00481 0.06978  0.15884  18  VAL B CB  
2347 C CG1 . VAL B 18  ? 0.34936 0.52852 0.39577 -0.00186 0.05781  0.16342  18  VAL B CG1 
2348 C CG2 . VAL B 18  ? 0.36906 0.57456 0.37340 -0.00132 0.06799  0.13438  18  VAL B CG2 
2349 N N   . ASP B 19  ? 0.38738 0.60323 0.43975 -0.01790 0.09435  0.20047  19  ASP B N   
2350 C CA  . ASP B 19  ? 0.37930 0.58967 0.45729 -0.02310 0.09912  0.22138  19  ASP B CA  
2351 C C   . ASP B 19  ? 0.37357 0.58251 0.48079 -0.02455 0.10827  0.20948  19  ASP B C   
2352 O O   . ASP B 19  ? 0.35809 0.55272 0.49688 -0.02632 0.10586  0.21476  19  ASP B O   
2353 C CB  . ASP B 19  ? 0.39875 0.62797 0.45772 -0.03011 0.10858  0.24589  19  ASP B CB  
2354 C CG  . ASP B 19  ? 0.43142 0.65298 0.48000 -0.02917 0.09518  0.26607  19  ASP B CG  
2355 O OD1 . ASP B 19  ? 0.47399 0.68294 0.52685 -0.02392 0.08216  0.26547  19  ASP B OD1 
2356 O OD2 . ASP B 19  ? 0.45208 0.68022 0.48981 -0.03344 0.09734  0.28179  19  ASP B OD2 
2357 N N   . ARG B 20  ? 0.37245 0.59709 0.47164 -0.02383 0.11865  0.19231  20  ARG B N   
2358 C CA  . ARG B 20  ? 0.32881 0.55473 0.45773 -0.02414 0.12614  0.18030  20  ARG B CA  
2359 C C   . ARG B 20  ? 0.32394 0.53058 0.47264 -0.01808 0.11311  0.16421  20  ARG B C   
2360 O O   . ARG B 20  ? 0.31025 0.51017 0.49026 -0.01982 0.11230  0.16311  20  ARG B O   
2361 C CB  . ARG B 20  ? 0.32853 0.57624 0.44633 -0.02357 0.14034  0.16501  20  ARG B CB  
2362 C CG  . ARG B 20  ? 0.32525 0.57903 0.47678 -0.02441 0.14957  0.15642  20  ARG B CG  
2363 C CD  . ARG B 20  ? 0.36550 0.63885 0.51198 -0.02158 0.16277  0.13716  20  ARG B CD  
2364 N NE  . ARG B 20  ? 0.34207 0.62103 0.52599 -0.02074 0.16905  0.12810  20  ARG B NE  
2365 C CZ  . ARG B 20  ? 0.33073 0.62290 0.52369 -0.01601 0.17816  0.10897  20  ARG B CZ  
2366 N NH1 . ARG B 20  ? 0.33453 0.63462 0.50207 -0.01214 0.18333  0.09463  20  ARG B NH1 
2367 N NH2 . ARG B 20  ? 0.31075 0.60883 0.54155 -0.01515 0.18192  0.10332  20  ARG B NH2 
2368 N N   . MET B 21  ? 0.35407 0.55292 0.48446 -0.01180 0.10277  0.15172  21  MET B N   
2369 C CA  . MET B 21  ? 0.32788 0.50920 0.47299 -0.00670 0.09047  0.13806  21  MET B CA  
2370 C C   . MET B 21  ? 0.32712 0.49153 0.49195 -0.00921 0.08159  0.14906  21  MET B C   
2371 O O   . MET B 21  ? 0.30440 0.45932 0.49217 -0.00872 0.07624  0.14070  21  MET B O   
2372 C CB  . MET B 21  ? 0.32485 0.50109 0.44575 -0.00094 0.08202  0.12566  21  MET B CB  
2373 C CG  . MET B 21  ? 0.34428 0.53627 0.44480 0.00097  0.09095  0.11318  21  MET B CG  
2374 S SD  . MET B 21  ? 0.33453 0.51666 0.41749 0.00740  0.08051  0.09421  21  MET B SD  
2375 C CE  . MET B 21  ? 0.38503 0.58875 0.44172 0.00673  0.09330  0.08292  21  MET B CE  
2376 N N   . CYS B 22  ? 0.32525 0.48648 0.48246 -0.01199 0.07980  0.16760  22  CYS B N   
2377 C CA  . CYS B 22  ? 0.33560 0.47977 0.51566 -0.01410 0.07265  0.17718  22  CYS B CA  
2378 C C   . CYS B 22  ? 0.31846 0.46295 0.53055 -0.02054 0.08010  0.18252  22  CYS B C   
2379 O O   . CYS B 22  ? 0.31506 0.44527 0.55253 -0.02235 0.07431  0.18044  22  CYS B O   
2380 C CB  . CYS B 22  ? 0.34488 0.48609 0.51319 -0.01475 0.06906  0.19779  22  CYS B CB  
2381 S SG  . CYS B 22  ? 0.46676 0.58631 0.64348 -0.01001 0.05324  0.19512  22  CYS B SG  
2382 N N   . ARG B 23  ? 0.33256 0.49428 0.54498 -0.02470 0.09341  0.18788  23  ARG B N   
2383 C CA  . ARG B 23  ? 0.31916 0.48380 0.56409 -0.03167 0.10139  0.19227  23  ARG B CA  
2384 C C   . ARG B 23  ? 0.30032 0.46738 0.56447 -0.02978 0.09912  0.17115  23  ARG B C   
2385 O O   . ARG B 23  ? 0.29235 0.45497 0.58766 -0.03456 0.09797  0.16931  23  ARG B O   
2386 C CB  . ARG B 23  ? 0.31883 0.50329 0.55786 -0.03751 0.11776  0.20658  23  ARG B CB  
2387 C CG  . ARG B 23  ? 0.31629 0.49587 0.53928 -0.04046 0.11776  0.22888  23  ARG B CG  
2388 C CD  . ARG B 23  ? 0.34360 0.53937 0.55658 -0.04619 0.13145  0.23709  23  ARG B CD  
2389 N NE  . ARG B 23  ? 0.35313 0.57146 0.53769 -0.04452 0.14074  0.22904  23  ARG B NE  
2390 C CZ  . ARG B 23  ? 0.37088 0.59962 0.51947 -0.04452 0.14239  0.23792  23  ARG B CZ  
2391 N NH1 . ARG B 23  ? 0.38970 0.60917 0.52681 -0.04548 0.13446  0.25737  23  ARG B NH1 
2392 N NH2 . ARG B 23  ? 0.37615 0.62578 0.50088 -0.04332 0.15167  0.22567  23  ARG B NH2 
2393 N N   . LEU B 24  ? 0.27020 0.44498 0.51767 -0.02313 0.09816  0.15538  24  LEU B N   
2394 C CA  . LEU B 24  ? 0.25120 0.42799 0.51667 -0.02008 0.09382  0.13744  24  LEU B CA  
2395 C C   . LEU B 24  ? 0.25313 0.41199 0.52843 -0.01900 0.07888  0.12993  24  LEU B C   
2396 O O   . LEU B 24  ? 0.24499 0.40465 0.54516 -0.02122 0.07482  0.12195  24  LEU B O   
2397 C CB  . LEU B 24  ? 0.25510 0.44058 0.50160 -0.01239 0.09537  0.12349  24  LEU B CB  
2398 C CG  . LEU B 24  ? 0.27254 0.47916 0.51327 -0.01278 0.11137  0.12333  24  LEU B CG  
2399 C CD1 . LEU B 24  ? 0.27357 0.48267 0.49094 -0.00503 0.11098  0.10904  24  LEU B CD1 
2400 C CD2 . LEU B 24  ? 0.25099 0.47142 0.52541 -0.01501 0.11847  0.11877  24  LEU B CD2 
2401 N N   . LEU B 25  ? 0.26339 0.40810 0.51935 -0.01592 0.07058  0.13143  25  LEU B N   
2402 C CA  . LEU B 25  ? 0.25160 0.38064 0.51513 -0.01524 0.05798  0.12300  25  LEU B CA  
2403 C C   . LEU B 25  ? 0.24201 0.36365 0.53458 -0.02278 0.05754  0.12848  25  LEU B C   
2404 O O   . LEU B 25  ? 0.24399 0.36017 0.55248 -0.02475 0.05001  0.11714  25  LEU B O   
2405 C CB  . LEU B 25  ? 0.27170 0.38909 0.51121 -0.01071 0.05091  0.12399  25  LEU B CB  
2406 C CG  . LEU B 25  ? 0.24683 0.36758 0.46003 -0.00377 0.04845  0.11404  25  LEU B CG  
2407 C CD1 . LEU B 25  ? 0.25376 0.36318 0.44885 -0.00072 0.04051  0.11472  25  LEU B CD1 
2408 C CD2 . LEU B 25  ? 0.22429 0.34620 0.44485 -0.00097 0.04366  0.09855  25  LEU B CD2 
2409 N N   . GLU B 26  ? 0.24874 0.37024 0.54876 -0.02768 0.06557  0.14577  26  GLU B N   
2410 C CA  . GLU B 26  ? 0.24225 0.35553 0.57456 -0.03557 0.06649  0.15085  26  GLU B CA  
2411 C C   . GLU B 26  ? 0.24168 0.36787 0.59979 -0.04154 0.07206  0.14549  26  GLU B C   
2412 O O   . GLU B 26  ? 0.23946 0.35836 0.61752 -0.04540 0.06606  0.13450  26  GLU B O   
2413 C CB  . GLU B 26  ? 0.24103 0.34822 0.57517 -0.03878 0.07286  0.17381  26  GLU B CB  
2414 C CG  . GLU B 26  ? 0.27160 0.36600 0.58663 -0.03299 0.06539  0.17987  26  GLU B CG  
2415 C CD  . GLU B 26  ? 0.27348 0.35173 0.59893 -0.03110 0.05429  0.16461  26  GLU B CD  
2416 O OE1 . GLU B 26  ? 0.28729 0.35383 0.64303 -0.03650 0.05387  0.16431  26  GLU B OE1 
2417 O OE2 . GLU B 26  ? 0.27434 0.35200 0.57821 -0.02478 0.04682  0.15216  26  GLU B OE2 
2418 N N   . GLU B 27  ? 0.22362 0.36737 0.57538 -0.04099 0.08189  0.14917  27  GLU B N   
2419 C CA  . GLU B 27  ? 0.22672 0.38099 0.59785 -0.04492 0.08574  0.14200  27  GLU B CA  
2420 C C   . GLU B 27  ? 0.20794 0.36931 0.58834 -0.04194 0.07671  0.12322  27  GLU B C   
2421 O O   . GLU B 27  ? 0.21384 0.37134 0.61288 -0.04612 0.06947  0.11332  27  GLU B O   
2422 C CB  . GLU B 27  ? 0.23979 0.41163 0.60169 -0.04511 0.09985  0.15024  27  GLU B CB  
2423 C CG  . GLU B 27  ? 0.30167 0.46871 0.65492 -0.04960 0.10833  0.17002  27  GLU B CG  
2424 C CD  . GLU B 27  ? 0.34832 0.53477 0.68501 -0.05006 0.12265  0.17709  27  GLU B CD  
2425 O OE1 . GLU B 27  ? 0.36300 0.56634 0.70093 -0.04701 0.12726  0.16482  27  GLU B OE1 
2426 O OE2 . GLU B 27  ? 0.35497 0.54009 0.67738 -0.05324 0.12901  0.19437  27  GLU B OE2 
2427 N N   . ASP B 28  ? 0.21499 0.38722 0.58185 -0.03453 0.07656  0.11805  28  ASP B N   
2428 C CA  . ASP B 28  ? 0.18953 0.36942 0.56352 -0.03012 0.06771  0.10258  28  ASP B CA  
2429 C C   . ASP B 28  ? 0.19802 0.36287 0.55868 -0.02679 0.05273  0.09302  28  ASP B C   
2430 O O   . ASP B 28  ? 0.18197 0.35038 0.55579 -0.02772 0.04281  0.08250  28  ASP B O   
2431 C CB  . ASP B 28  ? 0.20293 0.39613 0.56409 -0.02198 0.07390  0.09898  28  ASP B CB  
2432 C CG  . ASP B 28  ? 0.21614 0.42753 0.59338 -0.02493 0.08750  0.10218  28  ASP B CG  
2433 O OD1 . ASP B 28  ? 0.21254 0.42468 0.60909 -0.03179 0.08690  0.10182  28  ASP B OD1 
2434 O OD2 . ASP B 28  ? 0.21934 0.44264 0.58611 -0.02034 0.09845  0.10275  28  ASP B OD2 
2435 N N   . GLY B 29  ? 0.20744 0.35750 0.54211 -0.02338 0.05087  0.09677  29  GLY B N   
2436 C CA  . GLY B 29  ? 0.20628 0.34277 0.52701 -0.02047 0.03868  0.08812  29  GLY B CA  
2437 C C   . GLY B 29  ? 0.20086 0.33664 0.49596 -0.01157 0.03498  0.08241  29  GLY B C   
2438 O O   . GLY B 29  ? 0.17800 0.30318 0.46015 -0.00936 0.02568  0.07585  29  GLY B O   
2439 N N   . ALA B 30  ? 0.19659 0.34338 0.48539 -0.00695 0.04291  0.08390  30  ALA B N   
2440 C CA  . ALA B 30  ? 0.19826 0.34414 0.46717 0.00124  0.04061  0.07710  30  ALA B CA  
2441 C C   . ALA B 30  ? 0.20478 0.36390 0.47031 0.00427  0.05339  0.07895  30  ALA B C   
2442 O O   . ALA B 30  ? 0.21565 0.38781 0.49875 0.00048  0.06271  0.08373  30  ALA B O   
2443 C CB  . ALA B 30  ? 0.18894 0.33678 0.46722 0.00444  0.03038  0.06749  30  ALA B CB  
2444 N N   . PHE B 31  ? 0.21672 0.37321 0.46027 0.01039  0.05461  0.07401  31  PHE B N   
2445 C CA  . PHE B 31  ? 0.21577 0.38572 0.45630 0.01385  0.06677  0.07075  31  PHE B CA  
2446 C C   . PHE B 31  ? 0.22565 0.38967 0.45231 0.02149  0.06333  0.05948  31  PHE B C   
2447 O O   . PHE B 31  ? 0.23009 0.37985 0.44694 0.02327  0.05224  0.05670  31  PHE B O   
2448 C CB  . PHE B 31  ? 0.23002 0.40619 0.45377 0.00972  0.07790  0.08003  31  PHE B CB  
2449 C CG  . PHE B 31  ? 0.24306 0.40882 0.43673 0.01073  0.07349  0.08160  31  PHE B CG  
2450 C CD1 . PHE B 31  ? 0.25372 0.40671 0.44267 0.00746  0.06516  0.09042  31  PHE B CD1 
2451 C CD2 . PHE B 31  ? 0.26518 0.43501 0.43769 0.01474  0.07792  0.07322  31  PHE B CD2 
2452 C CE1 . PHE B 31  ? 0.26316 0.40878 0.42763 0.00869  0.06051  0.09223  31  PHE B CE1 
2453 C CE2 . PHE B 31  ? 0.27548 0.43805 0.42174 0.01498  0.07288  0.07416  31  PHE B CE2 
2454 C CZ  . PHE B 31  ? 0.26330 0.41442 0.40593 0.01221  0.06385  0.08436  31  PHE B CZ  
2455 N N   . ILE B 32  ? 0.22581 0.40115 0.45341 0.02553  0.07406  0.05236  32  ILE B N   
2456 C CA  . ILE B 32  ? 0.24447 0.41471 0.46587 0.03292  0.07293  0.04005  32  ILE B CA  
2457 C C   . ILE B 32  ? 0.26925 0.44534 0.46714 0.03281  0.08412  0.03457  32  ILE B C   
2458 O O   . ILE B 32  ? 0.27057 0.46305 0.46902 0.03009  0.09752  0.03583  32  ILE B O   
2459 C CB  . ILE B 32  ? 0.23043 0.40896 0.48193 0.03911  0.07462  0.03316  32  ILE B CB  
2460 C CG1 . ILE B 32  ? 0.20506 0.37822 0.47502 0.03903  0.06011  0.03805  32  ILE B CG1 
2461 C CG2 . ILE B 32  ? 0.23014 0.40410 0.47874 0.04688  0.07742  0.02014  32  ILE B CG2 
2462 C CD1 . ILE B 32  ? 0.19390 0.37666 0.49551 0.04521  0.05848  0.03432  32  ILE B CD1 
2463 N N   . LEU B 33  ? 0.27876 0.44300 0.45539 0.03474  0.07870  0.02839  33  LEU B N   
2464 C CA  . LEU B 33  ? 0.29369 0.46387 0.44951 0.03524  0.08767  0.01830  33  LEU B CA  
2465 C C   . LEU B 33  ? 0.29642 0.46460 0.46666 0.04262  0.09134  0.00196  33  LEU B C   
2466 O O   . LEU B 33  ? 0.30135 0.45447 0.48098 0.04699  0.08119  -0.00065 33  LEU B O   
2467 C CB  . LEU B 33  ? 0.30598 0.46569 0.43375 0.03267  0.07932  0.01963  33  LEU B CB  
2468 C CG  . LEU B 33  ? 0.30695 0.46851 0.42027 0.02633  0.07598  0.03580  33  LEU B CG  
2469 C CD1 . LEU B 33  ? 0.32223 0.47473 0.41236 0.02526  0.06689  0.03523  33  LEU B CD1 
2470 C CD2 . LEU B 33  ? 0.33894 0.52029 0.44351 0.02201  0.08937  0.04117  33  LEU B CD2 
2471 N N   . LYS B 34  ? 0.29879 0.48227 0.47231 0.04390  0.10637  -0.00865 34  LYS B N   
2472 C CA  . LYS B 34  ? 0.28633 0.46821 0.47870 0.05155  0.11184  -0.02549 34  LYS B CA  
2473 C C   . LYS B 34  ? 0.30766 0.48354 0.47702 0.05130  0.11387  -0.04041 34  LYS B C   
2474 O O   . LYS B 34  ? 0.32756 0.51581 0.47106 0.04573  0.12188  -0.04433 34  LYS B O   
2475 C CB  . LYS B 34  ? 0.29697 0.49963 0.51037 0.05342  0.12847  -0.03208 34  LYS B CB  
2476 C CG  . LYS B 34  ? 0.34106 0.54431 0.57247 0.06117  0.13799  -0.05298 34  LYS B CG  
2477 C CD  . LYS B 34  ? 0.31739 0.50540 0.58165 0.07037  0.12743  -0.05291 34  LYS B CD  
2478 C CE  . LYS B 34  ? 0.30471 0.50300 0.60115 0.07279  0.12524  -0.04151 34  LYS B CE  
2479 N NZ  . LYS B 34  ? 0.29211 0.48006 0.62218 0.08247  0.11579  -0.04156 34  LYS B NZ  
2480 N N   . GLY B 35  ? 0.32554 0.48325 0.50416 0.05656  0.10612  -0.04798 35  GLY B N   
2481 C CA  . GLY B 35  ? 0.33137 0.48205 0.49430 0.05620  0.10805  -0.06438 35  GLY B CA  
2482 C C   . GLY B 35  ? 0.32436 0.47531 0.45093 0.04838  0.10222  -0.06044 35  GLY B C   
2483 O O   . GLY B 35  ? 0.33998 0.50107 0.44560 0.04453  0.10962  -0.07303 35  GLY B O   
2484 N N   . LEU B 36  ? 0.31722 0.45865 0.43676 0.04586  0.08879  -0.04366 36  LEU B N   
2485 C CA  . LEU B 36  ? 0.32019 0.46085 0.41020 0.03970  0.08177  -0.03964 36  LEU B CA  
2486 C C   . LEU B 36  ? 0.32286 0.45228 0.40528 0.03981  0.07831  -0.05506 36  LEU B C   
2487 O O   . LEU B 36  ? 0.31771 0.45544 0.37632 0.03493  0.07941  -0.06260 36  LEU B O   
2488 C CB  . LEU B 36  ? 0.30293 0.43438 0.39276 0.03782  0.06898  -0.02070 36  LEU B CB  
2489 C CG  . LEU B 36  ? 0.30741 0.43922 0.37156 0.03241  0.06143  -0.01490 36  LEU B CG  
2490 C CD1 . LEU B 36  ? 0.31502 0.46378 0.36562 0.02788  0.06593  -0.00246 36  LEU B CD1 
2491 C CD2 . LEU B 36  ? 0.29992 0.41540 0.36902 0.03238  0.04828  -0.00562 36  LEU B CD2 
2492 N N   . LEU B 37  ? 0.34397 0.45548 0.44704 0.04481  0.07391  -0.05941 37  LEU B N   
2493 C CA  . LEU B 37  ? 0.36252 0.45982 0.46257 0.04423  0.06956  -0.07134 37  LEU B CA  
2494 C C   . LEU B 37  ? 0.37563 0.46817 0.49592 0.04926  0.07930  -0.09036 37  LEU B C   
2495 O O   . LEU B 37  ? 0.35528 0.44259 0.50311 0.05610  0.08161  -0.08775 37  LEU B O   
2496 C CB  . LEU B 37  ? 0.34767 0.42603 0.45513 0.04494  0.05636  -0.05923 37  LEU B CB  
2497 C CG  . LEU B 37  ? 0.31729 0.39826 0.40863 0.04027  0.04702  -0.04295 37  LEU B CG  
2498 C CD1 . LEU B 37  ? 0.30518 0.37028 0.40773 0.04147  0.03676  -0.03225 37  LEU B CD1 
2499 C CD2 . LEU B 37  ? 0.31238 0.39804 0.37952 0.03438  0.04390  -0.04806 37  LEU B CD2 
2500 N N   . PRO B 38  ? 0.35296 0.44739 0.46269 0.04612  0.08467  -0.11010 38  PRO B N   
2501 C CA  . PRO B 38  ? 0.35971 0.44810 0.49200 0.05081  0.09514  -0.13099 38  PRO B CA  
2502 C C   . PRO B 38  ? 0.36608 0.42905 0.52679 0.05663  0.08846  -0.12696 38  PRO B C   
2503 O O   . PRO B 38  ? 0.36934 0.41892 0.52491 0.05440  0.07613  -0.11417 38  PRO B O   
2504 C CB  . PRO B 38  ? 0.38765 0.48233 0.49854 0.04379  0.09902  -0.15244 38  PRO B CB  
2505 C CG  . PRO B 38  ? 0.37610 0.47289 0.45907 0.03671  0.08612  -0.13980 38  PRO B CG  
2506 C CD  . PRO B 38  ? 0.35655 0.45984 0.43497 0.03792  0.08095  -0.11486 38  PRO B CD  
2507 N N   . PHE B 39  ? 0.36568 0.42273 0.55768 0.06412  0.09725  -0.13785 39  PHE B N   
2508 C CA  . PHE B 39  ? 0.36799 0.40262 0.59059 0.07098  0.09064  -0.12906 39  PHE B CA  
2509 C C   . PHE B 39  ? 0.37232 0.38606 0.59165 0.06683  0.08353  -0.13252 39  PHE B C   
2510 O O   . PHE B 39  ? 0.37326 0.37026 0.60289 0.06860  0.07318  -0.11626 39  PHE B O   
2511 C CB  . PHE B 39  ? 0.37031 0.40282 0.63088 0.08052  0.10192  -0.14113 39  PHE B CB  
2512 C CG  . PHE B 39  ? 0.36858 0.38952 0.66099 0.08939  0.09404  -0.12234 39  PHE B CG  
2513 C CD1 . PHE B 39  ? 0.38688 0.38362 0.69312 0.09123  0.08441  -0.11351 39  PHE B CD1 
2514 C CD2 . PHE B 39  ? 0.36097 0.39678 0.66883 0.09508  0.09557  -0.11221 39  PHE B CD2 
2515 C CE1 . PHE B 39  ? 0.37228 0.36063 0.70470 0.09874  0.07561  -0.09393 39  PHE B CE1 
2516 C CE2 . PHE B 39  ? 0.35914 0.38714 0.69557 0.10279  0.08640  -0.09443 39  PHE B CE2 
2517 C CZ  . PHE B 39  ? 0.35715 0.36172 0.70111 0.10357  0.07517  -0.08388 39  PHE B CZ  
2518 N N   . ASP B 40  ? 0.38446 0.40036 0.58923 0.06045  0.08889  -0.15342 40  ASP B N   
2519 C CA  . ASP B 40  ? 0.40225 0.39902 0.60697 0.05556  0.08282  -0.15799 40  ASP B CA  
2520 C C   . ASP B 40  ? 0.39691 0.39334 0.57642 0.04898  0.06926  -0.13970 40  ASP B C   
2521 O O   . ASP B 40  ? 0.38642 0.36484 0.57154 0.04652  0.06205  -0.13373 40  ASP B O   
2522 C CB  . ASP B 40  ? 0.46460 0.46561 0.66259 0.04967  0.09191  -0.18779 40  ASP B CB  
2523 C CG  . ASP B 40  ? 0.54429 0.57440 0.71115 0.04444  0.09778  -0.19800 40  ASP B CG  
2524 O OD1 . ASP B 40  ? 0.51749 0.56319 0.68349 0.04872  0.10361  -0.19202 40  ASP B OD1 
2525 O OD2 . ASP B 40  ? 0.62839 0.66693 0.77209 0.03555  0.09646  -0.21168 40  ASP B OD2 
2526 N N   . VAL B 41  ? 0.40075 0.41666 0.55449 0.04595  0.06634  -0.13045 41  VAL B N   
2527 C CA  . VAL B 41  ? 0.37766 0.39222 0.51494 0.04189  0.05394  -0.11095 41  VAL B CA  
2528 C C   . VAL B 41  ? 0.36193 0.36445 0.51688 0.04744  0.04764  -0.09078 41  VAL B C   
2529 O O   . VAL B 41  ? 0.36455 0.35533 0.51767 0.04476  0.03862  -0.07901 41  VAL B O   
2530 C CB  . VAL B 41  ? 0.36136 0.39839 0.47133 0.03804  0.05270  -0.10502 41  VAL B CB  
2531 C CG1 . VAL B 41  ? 0.34777 0.38271 0.44707 0.03539  0.04100  -0.08482 41  VAL B CG1 
2532 C CG2 . VAL B 41  ? 0.36887 0.41879 0.45799 0.03130  0.05572  -0.12258 41  VAL B CG2 
2533 N N   . VAL B 42  ? 0.37169 0.37868 0.54454 0.05481  0.05241  -0.08712 42  VAL B N   
2534 C CA  . VAL B 42  ? 0.37228 0.37030 0.56378 0.06022  0.04555  -0.06890 42  VAL B CA  
2535 C C   . VAL B 42  ? 0.34958 0.32480 0.56113 0.06232  0.04277  -0.06834 42  VAL B C   
2536 O O   . VAL B 42  ? 0.34247 0.30746 0.55531 0.06149  0.03319  -0.05169 42  VAL B O   
2537 C CB  . VAL B 42  ? 0.37156 0.38140 0.58224 0.06782  0.05146  -0.06700 42  VAL B CB  
2538 C CG1 . VAL B 42  ? 0.34786 0.34881 0.58272 0.07416  0.04358  -0.05013 42  VAL B CG1 
2539 C CG2 . VAL B 42  ? 0.34501 0.37586 0.53651 0.06454  0.05264  -0.06157 42  VAL B CG2 
2540 N N   . GLU B 43  ? 0.33774 0.30478 0.56503 0.06430  0.05154  -0.08665 43  GLU B N   
2541 C CA  . GLU B 43  ? 0.34472 0.28798 0.59534 0.06638  0.04965  -0.08501 43  GLU B CA  
2542 C C   . GLU B 43  ? 0.34437 0.27659 0.57791 0.05711  0.04305  -0.08215 43  GLU B C   
2543 O O   . GLU B 43  ? 0.33711 0.25307 0.58022 0.05683  0.03647  -0.06752 43  GLU B O   
2544 C CB  . GLU B 43  ? 0.36863 0.30493 0.64515 0.07098  0.06193  -0.10744 43  GLU B CB  
2545 C CG  . GLU B 43  ? 0.39358 0.32596 0.66019 0.06310  0.06796  -0.13117 43  GLU B CG  
2546 C CD  . GLU B 43  ? 0.43052 0.33715 0.71157 0.05973  0.06422  -0.12927 43  GLU B CD  
2547 O OE1 . GLU B 43  ? 0.43542 0.32500 0.74473 0.06595  0.06209  -0.11643 43  GLU B OE1 
2548 O OE2 . GLU B 43  ? 0.43388 0.33928 0.69707 0.04999  0.06262  -0.13850 43  GLU B OE2 
2549 N N   . SER B 44  ? 0.38139 0.32400 0.58977 0.04916  0.04439  -0.09470 44  SER B N   
2550 C CA  . SER B 44  ? 0.36951 0.30513 0.56318 0.04027  0.03785  -0.09167 44  SER B CA  
2551 C C   . SER B 44  ? 0.33538 0.27093 0.51905 0.03915  0.02772  -0.06767 44  SER B C   
2552 O O   . SER B 44  ? 0.33316 0.25362 0.52334 0.03677  0.02300  -0.05659 44  SER B O   
2553 C CB  . SER B 44  ? 0.36970 0.32181 0.53796 0.03284  0.03907  -0.10667 44  SER B CB  
2554 O OG  . SER B 44  ? 0.39634 0.34790 0.57169 0.03121  0.04772  -0.13141 44  SER B OG  
2555 N N   . PHE B 45  ? 0.32482 0.27745 0.49339 0.04036  0.02507  -0.05985 45  PHE B N   
2556 C CA  . PHE B 45  ? 0.31002 0.26434 0.46971 0.03898  0.01609  -0.03965 45  PHE B CA  
2557 C C   . PHE B 45  ? 0.32804 0.26912 0.50765 0.04380  0.01244  -0.02522 45  PHE B C   
2558 O O   . PHE B 45  ? 0.33875 0.27277 0.51348 0.03981  0.00598  -0.01229 45  PHE B O   
2559 C CB  . PHE B 45  ? 0.28283 0.25655 0.42964 0.04032  0.01554  -0.03576 45  PHE B CB  
2560 C CG  . PHE B 45  ? 0.28855 0.26699 0.42309 0.03703  0.00741  -0.02041 45  PHE B CG  
2561 C CD1 . PHE B 45  ? 0.28009 0.24909 0.40957 0.03179  0.00187  -0.01339 45  PHE B CD1 
2562 C CD2 . PHE B 45  ? 0.27137 0.26429 0.40009 0.03834  0.00646  -0.01452 45  PHE B CD2 
2563 C CE1 . PHE B 45  ? 0.27586 0.25038 0.39464 0.02841  -0.00414 -0.00243 45  PHE B CE1 
2564 C CE2 . PHE B 45  ? 0.26182 0.25838 0.38173 0.03491  -0.00016 -0.00336 45  PHE B CE2 
2565 C CZ  . PHE B 45  ? 0.26598 0.25376 0.38060 0.03009  -0.00526 0.00169  45  PHE B CZ  
2566 N N   . ASN B 46  ? 0.33293 0.27193 0.53524 0.05214  0.01668  -0.02735 46  ASN B N   
2567 C CA  . ASN B 46  ? 0.33739 0.26627 0.56071 0.05782  0.01152  -0.01106 46  ASN B CA  
2568 C C   . ASN B 46  ? 0.34226 0.24919 0.57561 0.05494  0.00997  -0.00637 46  ASN B C   
2569 O O   . ASN B 46  ? 0.33317 0.23330 0.56965 0.05474  0.00230  0.01295  46  ASN B O   
2570 C CB  . ASN B 46  ? 0.34537 0.27748 0.59586 0.06818  0.01699  -0.01565 46  ASN B CB  
2571 C CG  . ASN B 46  ? 0.33770 0.28670 0.58988 0.07254  0.01210  -0.00359 46  ASN B CG  
2572 O OD1 . ASN B 46  ? 0.33115 0.28287 0.57463 0.07013  0.00210  0.01345  46  ASN B OD1 
2573 N ND2 . ASN B 46  ? 0.33626 0.29786 0.60039 0.07829  0.01969  -0.01346 46  ASN B ND2 
2574 N N   . ARG B 47  ? 0.33283 0.22933 0.57081 0.05173  0.01703  -0.02328 47  ARG B N   
2575 C CA  . ARG B 47  ? 0.32729 0.20147 0.57784 0.04784  0.01684  -0.01966 47  ARG B CA  
2576 C C   . ARG B 47  ? 0.32690 0.20194 0.55246 0.03690  0.01165  -0.01227 47  ARG B C   
2577 O O   . ARG B 47  ? 0.32920 0.18908 0.56094 0.03297  0.00908  0.00009  47  ARG B O   
2578 C CB  . ARG B 47  ? 0.34883 0.21230 0.61821 0.04846  0.02708  -0.04327 47  ARG B CB  
2579 C CG  . ARG B 47  ? 0.37455 0.23586 0.67349 0.05951  0.03391  -0.05183 47  ARG B CG  
2580 C CD  . ARG B 47  ? 0.37402 0.23380 0.69037 0.06823  0.02724  -0.02841 47  ARG B CD  
2581 N NE  . ARG B 47  ? 0.37468 0.25407 0.69246 0.07594  0.02858  -0.03052 47  ARG B NE  
2582 C CZ  . ARG B 47  ? 0.36990 0.25737 0.69780 0.08241  0.02247  -0.01342 47  ARG B CZ  
2583 N NH1 . ARG B 47  ? 0.35364 0.23895 0.67564 0.08098  0.01090  0.01086  47  ARG B NH1 
2584 N NH2 . ARG B 47  ? 0.37126 0.27077 0.71407 0.08932  0.02811  -0.02154 47  ARG B NH2 
2585 N N   . GLU B 48  ? 0.33225 0.22525 0.53218 0.03253  0.01035  -0.01807 48  GLU B N   
2586 C CA  . GLU B 48  ? 0.33750 0.23335 0.51717 0.02325  0.00597  -0.01172 48  GLU B CA  
2587 C C   . GLU B 48  ? 0.35633 0.25609 0.52750 0.02317  -0.00161 0.00995  48  GLU B C   
2588 O O   . GLU B 48  ? 0.35870 0.25552 0.51966 0.01571  -0.00430 0.01863  48  GLU B O   
2589 C CB  . GLU B 48  ? 0.31218 0.22549 0.47130 0.01930  0.00679  -0.02490 48  GLU B CB  
2590 C CG  . GLU B 48  ? 0.31937 0.23109 0.48168 0.01598  0.01258  -0.04622 48  GLU B CG  
2591 C CD  . GLU B 48  ? 0.31863 0.25082 0.46207 0.01458  0.01275  -0.05761 48  GLU B CD  
2592 O OE1 . GLU B 48  ? 0.31578 0.26075 0.44557 0.01589  0.00867  -0.04773 48  GLU B OE1 
2593 O OE2 . GLU B 48  ? 0.32468 0.26062 0.46739 0.01189  0.01676  -0.07613 48  GLU B OE2 
2594 N N   . LEU B 49  ? 0.33865 0.24669 0.51412 0.03063  -0.00477 0.01783  49  LEU B N   
2595 C CA  . LEU B 49  ? 0.34750 0.26052 0.51633 0.03023  -0.01281 0.03730  49  LEU B CA  
2596 C C   . LEU B 49  ? 0.36897 0.26677 0.55410 0.03217  -0.01625 0.05394  49  LEU B C   
2597 O O   . LEU B 49  ? 0.39145 0.29007 0.56576 0.02728  -0.02225 0.07018  49  LEU B O   
2598 C CB  . LEU B 49  ? 0.34104 0.27034 0.51026 0.03651  -0.01563 0.03906  49  LEU B CB  
2599 C CG  . LEU B 49  ? 0.32473 0.26979 0.47557 0.03336  -0.01407 0.02921  49  LEU B CG  
2600 C CD1 . LEU B 49  ? 0.32143 0.27888 0.48069 0.04044  -0.01277 0.02643  49  LEU B CD1 
2601 C CD2 . LEU B 49  ? 0.28357 0.23610 0.41574 0.02641  -0.01978 0.03776  49  LEU B CD2 
2602 N N   . ASP B 50  ? 0.34972 0.23405 0.56128 0.03904  -0.01226 0.05038  50  ASP B N   
2603 C CA  . ASP B 50  ? 0.35680 0.22335 0.58763 0.04085  -0.01503 0.06713  50  ASP B CA  
2604 C C   . ASP B 50  ? 0.37160 0.22657 0.59145 0.02987  -0.01406 0.07273  50  ASP B C   
2605 O O   . ASP B 50  ? 0.38618 0.23575 0.60414 0.02688  -0.01960 0.09417  50  ASP B O   
2606 C CB  . ASP B 50  ? 0.35497 0.20657 0.61972 0.04950  -0.00850 0.05752  50  ASP B CB  
2607 C CG  . ASP B 50  ? 0.36008 0.22160 0.64379 0.06154  -0.01038 0.05928  50  ASP B CG  
2608 O OD1 . ASP B 50  ? 0.37752 0.25312 0.65381 0.06362  -0.01937 0.07496  50  ASP B OD1 
2609 O OD2 . ASP B 50  ? 0.35147 0.21075 0.65413 0.06703  -0.00237 0.04306  50  ASP B OD2 
2610 N N   . VAL B 51  ? 0.38429 0.23702 0.59698 0.02328  -0.00711 0.05406  51  VAL B N   
2611 C CA  . VAL B 51  ? 0.39152 0.23677 0.59409 0.01182  -0.00536 0.05720  51  VAL B CA  
2612 C C   . VAL B 51  ? 0.41892 0.27776 0.59548 0.00549  -0.01131 0.07222  51  VAL B C   
2613 O O   . VAL B 51  ? 0.46335 0.31536 0.63543 -0.00161 -0.01231 0.08754  51  VAL B O   
2614 C CB  . VAL B 51  ? 0.38681 0.23449 0.58441 0.00611  0.00132  0.03287  51  VAL B CB  
2615 C CG1 . VAL B 51  ? 0.41129 0.25951 0.59462 -0.00609 0.00229  0.03522  51  VAL B CG1 
2616 C CG2 . VAL B 51  ? 0.39235 0.22319 0.61644 0.00894  0.00798  0.01864  51  VAL B CG2 
2617 N N   . GLN B 52  ? 0.40198 0.28048 0.56173 0.00749  -0.01464 0.06784  52  GLN B N   
2618 C CA  . GLN B 52  ? 0.41931 0.31160 0.55535 0.00093  -0.01914 0.07770  52  GLN B CA  
2619 C C   . GLN B 52  ? 0.44350 0.33689 0.57911 0.00283  -0.02695 0.10053  52  GLN B C   
2620 O O   . GLN B 52  ? 0.48641 0.38379 0.60583 -0.00521 -0.02933 0.11319  52  GLN B O   
2621 C CB  . GLN B 52  ? 0.39468 0.30595 0.51689 0.00246  -0.02016 0.06591  52  GLN B CB  
2622 C CG  . GLN B 52  ? 0.38518 0.29913 0.50390 -0.00048 -0.01431 0.04650  52  GLN B CG  
2623 C CD  . GLN B 52  ? 0.37587 0.28390 0.49003 -0.01044 -0.01056 0.04521  52  GLN B CD  
2624 O OE1 . GLN B 52  ? 0.39448 0.29351 0.51862 -0.01257 -0.00582 0.03443  52  GLN B OE1 
2625 N NE2 . GLN B 52  ? 0.38922 0.30354 0.48894 -0.01734 -0.01216 0.05513  52  GLN B NE2 
2626 N N   . MET B 53  ? 0.42262 0.31464 0.57589 0.01312  -0.03111 0.10606  53  MET B N   
2627 C CA  . MET B 53  ? 0.42267 0.31722 0.57780 0.01535  -0.04034 0.12933  53  MET B CA  
2628 C C   . MET B 53  ? 0.46208 0.33693 0.63030 0.01348  -0.04023 0.14674  53  MET B C   
2629 O O   . MET B 53  ? 0.47530 0.35194 0.64351 0.01421  -0.04866 0.16984  53  MET B O   
2630 C CB  . MET B 53  ? 0.40001 0.30197 0.57316 0.02729  -0.04534 0.12986  53  MET B CB  
2631 C CG  . MET B 53  ? 0.39165 0.31020 0.55495 0.02848  -0.04305 0.11150  53  MET B CG  
2632 S SD  . MET B 53  ? 0.45121 0.38751 0.62662 0.03807  -0.05062 0.11539  53  MET B SD  
2633 C CE  . MET B 53  ? 0.46691 0.41970 0.61958 0.03062  -0.06267 0.13359  53  MET B CE  
2634 N N   . ALA B 54  ? 0.48009 0.33710 0.65944 0.01034  -0.03131 0.13689  54  ALA B N   
2635 C CA  . ALA B 54  ? 0.53262 0.36949 0.72360 0.00573  -0.02940 0.15266  54  ALA B CA  
2636 C C   . ALA B 54  ? 0.57036 0.41015 0.73688 -0.00872 -0.02603 0.15723  54  ALA B C   
2637 O O   . ALA B 54  ? 0.56706 0.39160 0.74055 -0.01474 -0.02288 0.16972  54  ALA B O   
2638 C CB  . ALA B 54  ? 0.49388 0.31141 0.71224 0.00920  -0.02055 0.13619  54  ALA B CB  
2639 N N   . ILE B 55  ? 1.07861 0.39340 0.64211 0.02473  0.00040  -0.09849 55  ILE B N   
2640 C CA  . ILE B 55  ? 1.06092 0.37777 0.62540 0.02458  -0.01769 -0.07920 55  ILE B CA  
2641 C C   . ILE B 55  ? 1.04106 0.39696 0.63032 0.06025  -0.01990 -0.06502 55  ILE B C   
2642 O O   . ILE B 55  ? 1.04708 0.43968 0.65169 0.07926  -0.01879 -0.07360 55  ILE B O   
2643 C CB  . ILE B 55  ? 1.04388 0.36519 0.59396 -0.00039 -0.03819 -0.08473 55  ILE B CB  
2644 C CG1 . ILE B 55  ? 1.07608 0.34340 0.59235 -0.03421 -0.04204 -0.09341 55  ILE B CG1 
2645 C CG2 . ILE B 55  ? 1.08298 0.42818 0.64851 0.00781  -0.05641 -0.06822 55  ILE B CG2 
2646 C CD1 . ILE B 55  ? 1.06548 0.32675 0.56805 -0.05458 -0.06880 -0.09278 55  ILE B CD1 
2647 N N   . PRO B 56  ? 1.07240 0.41723 0.66486 0.07036  -0.02136 -0.04537 56  PRO B N   
2648 C CA  . PRO B 56  ? 1.08233 0.45459 0.68739 0.10389  -0.02297 -0.03113 56  PRO B CA  
2649 C C   . PRO B 56  ? 1.10310 0.52205 0.71785 0.10707  -0.04096 -0.03369 56  PRO B C   
2650 O O   . PRO B 56  ? 1.11961 0.54381 0.73084 0.08105  -0.05397 -0.03988 56  PRO B O   
2651 C CB  . PRO B 56  ? 1.06483 0.40662 0.66614 0.10239  -0.01847 -0.01244 56  PRO B CB  
2652 C CG  . PRO B 56  ? 1.07959 0.37715 0.67183 0.07758  -0.00940 -0.01793 56  PRO B CG  
2653 C CD  . PRO B 56  ? 1.07109 0.37229 0.65487 0.05211  -0.01860 -0.03734 56  PRO B CD  
2654 N N   . PRO B 57  ? 1.09585 0.54754 0.72108 0.13923  -0.04398 -0.03014 57  PRO B N   
2655 C CA  . PRO B 57  ? 1.10987 0.60677 0.74512 0.14426  -0.06126 -0.03130 57  PRO B CA  
2656 C C   . PRO B 57  ? 1.12322 0.61535 0.75487 0.13234  -0.07032 -0.01596 57  PRO B C   
2657 O O   . PRO B 57  ? 1.14139 0.60894 0.76713 0.14233  -0.06228 0.00092  57  PRO B O   
2658 C CB  . PRO B 57  ? 1.11351 0.63384 0.75645 0.18605  -0.06249 -0.02765 57  PRO B CB  
2659 C CG  . PRO B 57  ? 1.12095 0.61727 0.76374 0.19898  -0.04732 -0.03422 57  PRO B CG  
2660 C CD  . PRO B 57  ? 1.08568 0.53294 0.71309 0.17366  -0.03376 -0.02747 57  PRO B CD  
2661 N N   . PRO B 58  ? 1.14286 0.65624 0.77862 0.11111  -0.08571 -0.02251 58  PRO B N   
2662 C CA  . PRO B 58  ? 1.15155 0.65982 0.78998 0.09707  -0.09524 -0.01151 58  PRO B CA  
2663 C C   . PRO B 58  ? 1.15940 0.69360 0.80435 0.12147  -0.09883 0.00246  58  PRO B C   
2664 O O   . PRO B 58  ? 1.13703 0.70912 0.78646 0.13999  -0.10648 -0.00114 58  PRO B O   
2665 C CB  . PRO B 58  ? 1.10210 0.62312 0.73942 0.06893  -0.11241 -0.02555 58  PRO B CB  
2666 C CG  . PRO B 58  ? 1.09442 0.64844 0.73358 0.07938  -0.11223 -0.03936 58  PRO B CG  
2667 C CD  . PRO B 58  ? 1.11362 0.65706 0.75322 0.10046  -0.09434 -0.04141 58  PRO B CD  
2668 N N   . LYS B 59  ? 1.21583 0.72718 0.86153 0.12004  -0.09240 0.01688  59  LYS B N   
2669 C CA  . LYS B 59  ? 1.20973 0.73125 0.85405 0.14131  -0.09014 0.03188  59  LYS B CA  
2670 C C   . LYS B 59  ? 1.16353 0.72200 0.82181 0.13160  -0.10793 0.03003  59  LYS B C   
2671 O O   . LYS B 59  ? 1.17520 0.73136 0.83679 0.13490  -0.10437 0.04113  59  LYS B O   
2672 C CB  . LYS B 59  ? 1.24779 0.72504 0.88753 0.14000  -0.07062 0.04549  59  LYS B CB  
2673 N N   . GLY B 60  ? 1.08603 0.67591 0.75128 0.11922  -0.12494 0.01562  60  GLY B N   
2674 C CA  . GLY B 60  ? 1.00551 0.63048 0.68260 0.11187  -0.14195 0.01380  60  GLY B CA  
2675 C C   . GLY B 60  ? 0.93484 0.60159 0.61357 0.11667  -0.15470 0.00084  60  GLY B C   
2676 O O   . GLY B 60  ? 0.93942 0.61333 0.61379 0.13246  -0.14905 -0.00634 60  GLY B O   
2677 N N   . GLU B 61  ? 0.85662 0.55098 0.54465 0.10299  -0.17115 -0.00410 61  GLU B N   
2678 C CA  . GLU B 61  ? 0.82749 0.56021 0.51825 0.10372  -0.18158 -0.01827 61  GLU B CA  
2679 C C   . GLU B 61  ? 0.83286 0.54971 0.51366 0.08588  -0.17799 -0.03548 61  GLU B C   
2680 O O   . GLU B 61  ? 0.83507 0.51211 0.50467 0.06487  -0.17542 -0.03703 61  GLU B O   
2681 C CB  . GLU B 61  ? 0.74189 0.49828 0.44128 0.08795  -0.19923 -0.02015 61  GLU B CB  
2682 C CG  . GLU B 61  ? 0.71749 0.44240 0.41458 0.05666  -0.20826 -0.02284 61  GLU B CG  
2683 C CD  . GLU B 61  ? 0.65056 0.39166 0.34637 0.03638  -0.22793 -0.03393 61  GLU B CD  
2684 O OE1 . GLU B 61  ? 0.62276 0.40427 0.32840 0.04594  -0.23497 -0.03379 61  GLU B OE1 
2685 O OE2 . GLU B 61  ? 0.66438 0.37391 0.34592 0.01130  -0.23713 -0.04299 61  GLU B OE2 
2686 N N   . ARG B 62  ? 0.87550 0.62224 0.56071 0.09360  -0.17713 -0.05036 62  ARG B N   
2687 C CA  . ARG B 62  ? 0.88899 0.62140 0.56377 0.07430  -0.17011 -0.06997 62  ARG B CA  
2688 C C   . ARG B 62  ? 0.87303 0.64561 0.55648 0.07165  -0.17558 -0.08677 62  ARG B C   
2689 O O   . ARG B 62  ? 0.90141 0.71172 0.60556 0.09590  -0.17238 -0.09417 62  ARG B O   
2690 C CB  . ARG B 62  ? 0.94825 0.66644 0.62481 0.08898  -0.15200 -0.07538 62  ARG B CB  
2691 C CG  . ARG B 62  ? 1.01331 0.68162 0.67539 0.08158  -0.14295 -0.06480 62  ARG B CG  
2692 C CD  . ARG B 62  ? 1.09352 0.74221 0.75212 0.08277  -0.12489 -0.07793 62  ARG B CD  
2693 N NE  . ARG B 62  ? 1.07965 0.71323 0.72277 0.05353  -0.12058 -0.09808 62  ARG B NE  
2694 C CZ  . ARG B 62  ? 1.08804 0.67224 0.70591 0.02938  -0.11281 -0.10275 62  ARG B CZ  
2695 N NH1 . ARG B 62  ? 1.17502 0.72390 0.78589 0.02989  -0.10901 -0.08975 62  ARG B NH1 
2696 N NH2 . ARG B 62  ? 1.03478 0.60100 0.63114 0.00373  -0.10749 -0.12179 62  ARG B NH2 
2697 N N   . LEU B 63  ? 0.80756 0.56920 0.47460 0.04280  -0.18441 -0.09439 63  LEU B N   
2698 C CA  . LEU B 63  ? 0.77282 0.57221 0.44715 0.03906  -0.19200 -0.10615 63  LEU B CA  
2699 C C   . LEU B 63  ? 0.78878 0.61601 0.47935 0.04858  -0.17693 -0.12827 63  LEU B C   
2700 O O   . LEU B 63  ? 0.77976 0.65635 0.49815 0.07096  -0.18054 -0.13276 63  LEU B O   
2701 C CB  . LEU B 63  ? 0.70827 0.48258 0.36148 0.00499  -0.19776 -0.10902 63  LEU B CB  
2702 C CG  . LEU B 63  ? 0.64826 0.41917 0.31490 0.00055  -0.20817 -0.08690 63  LEU B CG  
2703 C CD1 . LEU B 63  ? 0.63959 0.40266 0.31376 -0.02476 -0.20165 -0.08267 63  LEU B CD1 
2704 C CD2 . LEU B 63  ? 0.61178 0.43234 0.30868 0.02106  -0.21383 -0.07671 63  LEU B CD2 
2705 N N   . LEU B 64  ? 0.79649 0.59193 0.47195 0.03181  -0.15975 -0.14428 64  LEU B N   
2706 C CA  . LEU B 64  ? 0.81562 0.63532 0.51372 0.03979  -0.14155 -0.16905 64  LEU B CA  
2707 C C   . LEU B 64  ? 0.85539 0.68238 0.57789 0.06906  -0.13218 -0.16787 64  LEU B C   
2708 O O   . LEU B 64  ? 0.86687 0.72647 0.62178 0.08522  -0.12241 -0.18849 64  LEU B O   
2709 C CB  . LEU B 64  ? 0.76850 0.54689 0.43665 0.00538  -0.12340 -0.19011 64  LEU B CB  
2710 C CG  . LEU B 64  ? 0.77724 0.58035 0.46938 0.00353  -0.10110 -0.22249 64  LEU B CG  
2711 C CD1 . LEU B 64  ? 0.77794 0.63093 0.49193 0.00717  -0.10927 -0.23243 64  LEU B CD1 
2712 C CD2 . LEU B 64  ? 0.77969 0.52637 0.43227 -0.03209 -0.07811 -0.24092 64  LEU B CD2 
2713 N N   . ALA B 65  ? 0.91285 0.71018 0.62290 0.07711  -0.13536 -0.14595 65  ALA B N   
2714 C CA  . ALA B 65  ? 0.97510 0.76873 0.70036 0.10324  -0.12573 -0.14399 65  ALA B CA  
2715 C C   . ALA B 65  ? 0.98271 0.80298 0.72374 0.14100  -0.13903 -0.12604 65  ALA B C   
2716 O O   . ALA B 65  ? 1.02179 0.86077 0.78505 0.17119  -0.13661 -0.13324 65  ALA B O   
2717 C CB  . ALA B 65  ? 1.01323 0.74911 0.71094 0.08739  -0.11592 -0.13386 65  ALA B CB  
2718 N N   . ASP B 66  ? 0.92783 0.74712 0.65657 0.14092  -0.15316 -0.10416 66  ASP B N   
2719 C CA  . ASP B 66  ? 0.91699 0.76508 0.65765 0.17679  -0.16448 -0.09214 66  ASP B CA  
2720 C C   . ASP B 66  ? 0.89945 0.80201 0.66493 0.18832  -0.17492 -0.10858 66  ASP B C   
2721 O O   . ASP B 66  ? 0.92202 0.85058 0.69428 0.21656  -0.18794 -0.10024 66  ASP B O   
2722 C CB  . ASP B 66  ? 0.91235 0.74366 0.63532 0.17495  -0.17270 -0.06562 66  ASP B CB  
2723 C CG  . ASP B 66  ? 0.92149 0.70554 0.62720 0.17999  -0.16198 -0.04788 66  ASP B CG  
2724 O OD1 . ASP B 66  ? 0.93186 0.70046 0.63826 0.19343  -0.15115 -0.05320 66  ASP B OD1 
2725 O OD2 . ASP B 66  ? 0.90762 0.67018 0.60193 0.17022  -0.16343 -0.03025 66  ASP B OD2 
2726 N N   . LYS B 67  ? 0.89954 0.81617 0.67602 0.16596  -0.16826 -0.13281 67  LYS B N   
2727 C CA  . LYS B 67  ? 0.86948 0.83875 0.67653 0.17580  -0.17382 -0.15465 67  LYS B CA  
2728 C C   . LYS B 67  ? 0.90268 0.89575 0.74423 0.20548  -0.16920 -0.17567 67  LYS B C   
2729 O O   . LYS B 67  ? 0.79816 0.83836 0.67032 0.22881  -0.18060 -0.18953 67  LYS B O   
2730 C CB  . LYS B 67  ? 0.83235 0.80103 0.63440 0.13806  -0.16512 -0.17350 67  LYS B CB  
2731 C CG  . LYS B 67  ? 0.75726 0.77855 0.59271 0.14237  -0.16643 -0.19963 67  LYS B CG  
2732 C CD  . LYS B 67  ? 0.74912 0.76626 0.56588 0.10688  -0.16523 -0.20583 67  LYS B CD  
2733 C CE  . LYS B 67  ? 0.73125 0.74107 0.55291 0.08144  -0.14137 -0.23836 67  LYS B CE  
2734 N NZ  . LYS B 67  ? 0.66350 0.72657 0.53843 0.10063  -0.13430 -0.26929 67  LYS B NZ  
2735 N N   . TYR B 68  ? 0.99444 0.95624 0.83395 0.20653  -0.15457 -0.17943 68  TYR B N   
2736 C CA  . TYR B 68  ? 1.02189 1.00269 0.89846 0.23037  -0.14830 -0.20424 68  TYR B CA  
2737 C C   . TYR B 68  ? 1.06854 1.02241 0.93589 0.26131  -0.15152 -0.18778 68  TYR B C   
2738 O O   . TYR B 68  ? 1.08810 1.00174 0.91831 0.25764  -0.15187 -0.15849 68  TYR B O   
2739 C CB  . TYR B 68  ? 1.06162 1.02835 0.94806 0.19935  -0.12222 -0.23183 68  TYR B CB  
2740 C CG  . TYR B 68  ? 0.97383 0.96613 0.87247 0.17189  -0.11469 -0.25566 68  TYR B CG  
2741 C CD1 . TYR B 68  ? 0.93980 0.90834 0.79876 0.13773  -0.11503 -0.24238 68  TYR B CD1 
2742 C CD2 . TYR B 68  ? 0.90511 0.94238 0.85539 0.18093  -0.10755 -0.29245 68  TYR B CD2 
2743 C CE1 . TYR B 68  ? 0.89498 0.88037 0.75884 0.11337  -0.10744 -0.26337 68  TYR B CE1 
2744 C CE2 . TYR B 68  ? 0.83041 0.88622 0.78879 0.15405  -0.09725 -0.31412 68  TYR B CE2 
2745 C CZ  . TYR B 68  ? 0.82729 0.85549 0.73921 0.11981  -0.09650 -0.29910 68  TYR B CZ  
2746 O OH  . TYR B 68  ? 0.78086 0.82069 0.69424 0.09354  -0.08574 -0.31967 68  TYR B OH  
2747 N N   . PRO B 69  ? 1.28212 0.95378 0.86587 -0.12103 0.42978  -0.24099 69  PRO B N   
2748 C CA  . PRO B 69  ? 1.30509 0.98060 0.86505 -0.13969 0.43485  -0.21822 69  PRO B CA  
2749 C C   . PRO B 69  ? 1.35370 1.00425 0.92819 -0.14682 0.43587  -0.19864 69  PRO B C   
2750 O O   . PRO B 69  ? 1.38501 1.01662 0.98607 -0.13909 0.43277  -0.20186 69  PRO B O   
2751 C CB  . PRO B 69  ? 1.29347 0.94808 0.82780 -0.14622 0.42841  -0.21821 69  PRO B CB  
2752 C CG  . PRO B 69  ? 1.30579 0.96986 0.84506 -0.13223 0.42266  -0.24377 69  PRO B CG  
2753 C CD  . PRO B 69  ? 1.28954 0.94556 0.86347 -0.11698 0.42047  -0.25480 69  PRO B CD  
2754 N N   . LYS B 73  ? 0.95275 0.50597 0.64522 -0.15852 0.42453  -0.16959 73  LYS B N   
2755 C CA  . LYS B 73  ? 0.93013 0.48863 0.64157 -0.16689 0.42749  -0.15867 73  LYS B CA  
2756 C C   . LYS B 73  ? 0.92501 0.48525 0.65421 -0.16200 0.43078  -0.16256 73  LYS B C   
2757 O O   . LYS B 73  ? 0.92687 0.46903 0.65940 -0.16306 0.42730  -0.16951 73  LYS B O   
2758 C CB  . LYS B 73  ? 0.91412 0.45952 0.63121 -0.17926 0.42210  -0.15551 73  LYS B CB  
2759 C CG  . LYS B 73  ? 0.92391 0.46328 0.62414 -0.18330 0.42127  -0.15232 73  LYS B CG  
2760 C CD  . LYS B 73  ? 0.92950 0.48139 0.62493 -0.18552 0.42609  -0.14072 73  LYS B CD  
2761 C CE  . LYS B 73  ? 0.94377 0.48138 0.62221 -0.19360 0.42700  -0.13537 73  LYS B CE  
2762 N NZ  . LYS B 73  ? 0.96901 0.49288 0.61880 -0.19092 0.42728  -0.14163 73  LYS B NZ  
2763 N N   . TYR B 74  ? 0.49709 0.49046 0.58177 0.06077  -0.00757 0.03073  74  TYR B N   
2764 C CA  . TYR B 74  ? 0.43099 0.42782 0.51914 0.05006  -0.00651 0.02434  74  TYR B CA  
2765 C C   . TYR B 74  ? 0.38528 0.37368 0.48366 0.04423  0.00642  0.02332  74  TYR B C   
2766 O O   . TYR B 74  ? 0.38361 0.35597 0.47604 0.04769  0.01631  0.02951  74  TYR B O   
2767 C CB  . TYR B 74  ? 0.43484 0.42294 0.50020 0.05217  -0.00934 0.02554  74  TYR B CB  
2768 C CG  . TYR B 74  ? 0.41338 0.40403 0.48084 0.04311  -0.00894 0.01925  74  TYR B CG  
2769 C CD1 . TYR B 74  ? 0.37993 0.38647 0.46570 0.03435  -0.01485 0.01288  74  TYR B CD1 
2770 C CD2 . TYR B 74  ? 0.45308 0.43035 0.50430 0.04481  -0.00141 0.02099  74  TYR B CD2 
2771 C CE1 . TYR B 74  ? 0.37424 0.38163 0.46141 0.02737  -0.01424 0.00836  74  TYR B CE1 
2772 C CE2 . TYR B 74  ? 0.44495 0.42458 0.49899 0.03817  -0.00088 0.01564  74  TYR B CE2 
2773 C CZ  . TYR B 74  ? 0.39116 0.38506 0.46298 0.02928  -0.00766 0.00928  74  TYR B CZ  
2774 O OH  . TYR B 74  ? 0.38599 0.38074 0.45997 0.02391  -0.00686 0.00521  74  TYR B OH  
2775 N N   . VAL B 75  ? 0.35867 0.35823 0.47285 0.03527  0.00595  0.01615  75  VAL B N   
2776 C CA  . VAL B 75  ? 0.34469 0.33964 0.46957 0.02818  0.01490  0.01353  75  VAL B CA  
2777 C C   . VAL B 75  ? 0.31297 0.31765 0.44101 0.02061  0.01252  0.00879  75  VAL B C   
2778 O O   . VAL B 75  ? 0.27722 0.29593 0.41377 0.01664  0.00639  0.00364  75  VAL B O   
2779 C CB  . VAL B 75  ? 0.31575 0.31253 0.45566 0.02658  0.01659  0.00884  75  VAL B CB  
2780 C CG1 . VAL B 75  ? 0.29552 0.28912 0.44711 0.01804  0.02248  0.00466  75  VAL B CG1 
2781 C CG2 . VAL B 75  ? 0.32813 0.31138 0.46462 0.03521  0.02013  0.01399  75  VAL B CG2 
2782 N N   . PRO B 76  ? 0.31700 0.31468 0.43829 0.01957  0.01812  0.01140  76  PRO B N   
2783 C CA  . PRO B 76  ? 0.29061 0.29582 0.41337 0.01449  0.01595  0.00760  76  PRO B CA  
2784 C C   . PRO B 76  ? 0.26415 0.27776 0.40578 0.00696  0.01913  0.00351  76  PRO B C   
2785 O O   . PRO B 76  ? 0.27333 0.28356 0.42580 0.00477  0.02452  0.00366  76  PRO B O   
2786 C CB  . PRO B 76  ? 0.31146 0.30474 0.41863 0.01909  0.02278  0.01274  76  PRO B CB  
2787 C CG  . PRO B 76  ? 0.34059 0.32350 0.44949 0.02199  0.03289  0.01952  76  PRO B CG  
2788 C CD  . PRO B 76  ? 0.33309 0.31532 0.44408 0.02457  0.02793  0.01933  76  PRO B CD  
2789 N N   . ASN B 77  ? 0.24338 0.26682 0.38825 0.00309  0.01500  -0.00010 77  ASN B N   
2790 C CA  . ASN B 77  ? 0.22997 0.26325 0.38992 -0.00285 0.01623  -0.00362 77  ASN B CA  
2791 C C   . ASN B 77  ? 0.22845 0.26412 0.40130 -0.00590 0.01689  -0.00737 77  ASN B C   
2792 O O   . ASN B 77  ? 0.24062 0.27373 0.42423 -0.00935 0.02198  -0.00721 77  ASN B O   
2793 C CB  . ASN B 77  ? 0.21742 0.24818 0.37979 -0.00322 0.02369  -0.00026 77  ASN B CB  
2794 C CG  . ASN B 77  ? 0.24232 0.26074 0.40096 0.00020  0.03320  0.00619  77  ASN B CG  
2795 O OD1 . ASN B 77  ? 0.25521 0.26378 0.39637 0.00665  0.03621  0.01060  77  ASN B OD1 
2796 N ND2 . ASN B 77  ? 0.24812 0.26590 0.42242 -0.00400 0.03797  0.00690  77  ASN B ND2 
2797 N N   . VAL B 78  ? 0.21518 0.25561 0.38784 -0.00456 0.01180  -0.01093 78  VAL B N   
2798 C CA  . VAL B 78  ? 0.21819 0.25593 0.39826 -0.00520 0.01257  -0.01561 78  VAL B CA  
2799 C C   . VAL B 78  ? 0.22177 0.26729 0.41275 -0.01112 0.01086  -0.02190 78  VAL B C   
2800 O O   . VAL B 78  ? 0.22051 0.26050 0.41834 -0.01335 0.01104  -0.02719 78  VAL B O   
2801 C CB  . VAL B 78  ? 0.22100 0.26289 0.39730 0.00005  0.00890  -0.01763 78  VAL B CB  
2802 C CG1 . VAL B 78  ? 0.23756 0.27458 0.40508 0.00606  0.00838  -0.01129 78  VAL B CG1 
2803 C CG2 . VAL B 78  ? 0.20686 0.26539 0.38436 -0.00098 0.00416  -0.02018 78  VAL B CG2 
2804 N N   . ALA B 79  ? 0.20327 0.26034 0.39573 -0.01347 0.00838  -0.02167 79  ALA B N   
2805 C CA  . ALA B 79  ? 0.19554 0.26197 0.39771 -0.01796 0.00525  -0.02708 79  ALA B CA  
2806 C C   . ALA B 79  ? 0.20589 0.26720 0.42209 -0.02332 0.00844  -0.02758 79  ALA B C   
2807 O O   . ALA B 79  ? 0.21561 0.28147 0.44172 -0.02782 0.00395  -0.03444 79  ALA B O   
2808 C CB  . ALA B 79  ? 0.18537 0.26383 0.38662 -0.01811 0.00292  -0.02447 79  ALA B CB  
2809 N N   . THR B 80  ? 0.19897 0.25133 0.41662 -0.02300 0.01596  -0.02021 80  THR B N   
2810 C CA  . THR B 80  ? 0.21498 0.26544 0.45034 -0.02888 0.02065  -0.01830 80  THR B CA  
2811 C C   . THR B 80  ? 0.23648 0.27158 0.47766 -0.03167 0.02300  -0.02013 80  THR B C   
2812 O O   . THR B 80  ? 0.24553 0.27928 0.50590 -0.03906 0.02496  -0.02026 80  THR B O   
2813 C CB  . THR B 80  ? 0.22194 0.27083 0.45740 -0.02644 0.03022  -0.00793 80  THR B CB  
2814 O OG1 . THR B 80  ? 0.24362 0.27655 0.46518 -0.02104 0.03666  -0.00181 80  THR B OG1 
2815 C CG2 . THR B 80  ? 0.19897 0.25756 0.42541 -0.02218 0.02837  -0.00636 80  THR B CG2 
2816 N N   . THR B 81  ? 0.24345 0.26702 0.47072 -0.02609 0.02273  -0.02116 81  THR B N   
2817 C CA  . THR B 81  ? 0.24740 0.25274 0.47840 -0.02697 0.02586  -0.02196 81  THR B CA  
2818 C C   . THR B 81  ? 0.25868 0.25932 0.48469 -0.02503 0.01899  -0.03296 81  THR B C   
2819 O O   . THR B 81  ? 0.27051 0.25367 0.50087 -0.02634 0.02054  -0.03590 81  THR B O   
2820 C CB  . THR B 81  ? 0.27300 0.26461 0.49137 -0.01943 0.03375  -0.01152 81  THR B CB  
2821 O OG1 . THR B 81  ? 0.27372 0.27065 0.47452 -0.01113 0.02946  -0.01160 81  THR B OG1 
2822 C CG2 . THR B 81  ? 0.27018 0.26226 0.49074 -0.01982 0.04273  -0.00050 81  THR B CG2 
2823 N N   . CYS B 82  ? 0.25844 0.27261 0.47487 -0.02118 0.01251  -0.03851 82  CYS B N   
2824 C CA  . CYS B 82  ? 0.24752 0.25873 0.45615 -0.01671 0.00775  -0.04829 82  CYS B CA  
2825 C C   . CYS B 82  ? 0.24628 0.27131 0.45655 -0.02029 -0.00027 -0.05771 82  CYS B C   
2826 O O   . CYS B 82  ? 0.23567 0.27754 0.43948 -0.01752 -0.00263 -0.05592 82  CYS B O   
2827 C CB  . CYS B 82  ? 0.23561 0.25183 0.43040 -0.00663 0.00882  -0.04436 82  CYS B CB  
2828 S SG  . CYS B 82  ? 0.26475 0.26844 0.45480 -0.00071 0.01552  -0.03279 82  CYS B SG  
2829 N N   . PRO B 83  ? 0.25191 0.26983 0.47030 -0.02636 -0.00535 -0.06768 83  PRO B N   
2830 C CA  . PRO B 83  ? 0.25209 0.28360 0.46920 -0.02854 -0.01492 -0.07734 83  PRO B CA  
2831 C C   . PRO B 83  ? 0.24230 0.28150 0.43934 -0.01843 -0.01716 -0.08190 83  PRO B C   
2832 O O   . PRO B 83  ? 0.23276 0.28812 0.42496 -0.01770 -0.02275 -0.08439 83  PRO B O   
2833 C CB  . PRO B 83  ? 0.26455 0.28127 0.49202 -0.03622 -0.02105 -0.08898 83  PRO B CB  
2834 C CG  . PRO B 83  ? 0.27821 0.27917 0.52082 -0.04179 -0.01297 -0.08088 83  PRO B CG  
2835 C CD  . PRO B 83  ? 0.26169 0.25820 0.49148 -0.03211 -0.00339 -0.07027 83  PRO B CD  
2836 N N   . THR B 84  ? 0.26332 0.29237 0.44918 -0.00971 -0.01223 -0.08191 84  THR B N   
2837 C CA  . THR B 84  ? 0.25505 0.29363 0.42418 0.00085  -0.01198 -0.08430 84  THR B CA  
2838 C C   . THR B 84  ? 0.22831 0.28810 0.39650 0.00246  -0.00977 -0.07322 84  THR B C   
2839 O O   . THR B 84  ? 0.22683 0.30042 0.38538 0.00713  -0.01141 -0.07432 84  THR B O   
2840 C CB  . THR B 84  ? 0.26420 0.28963 0.42580 0.01061  -0.00593 -0.08454 84  THR B CB  
2841 O OG1 . THR B 84  ? 0.27600 0.27798 0.43669 0.00961  -0.00830 -0.09610 84  THR B OG1 
2842 C CG2 . THR B 84  ? 0.28292 0.32200 0.43028 0.02244  -0.00332 -0.08454 84  THR B CG2 
2843 N N   . PHE B 85  ? 0.23365 0.29471 0.41040 -0.00095 -0.00594 -0.06242 85  PHE B N   
2844 C CA  . PHE B 85  ? 0.22195 0.29937 0.39852 -0.00090 -0.00514 -0.05309 85  PHE B CA  
2845 C C   . PHE B 85  ? 0.20430 0.29272 0.38367 -0.00589 -0.00993 -0.05407 85  PHE B C   
2846 O O   . PHE B 85  ? 0.20102 0.30257 0.37358 -0.00265 -0.01147 -0.05286 85  PHE B O   
2847 C CB  . PHE B 85  ? 0.21289 0.28602 0.39458 -0.00280 -0.00147 -0.04339 85  PHE B CB  
2848 C CG  . PHE B 85  ? 0.19155 0.27743 0.37230 -0.00298 -0.00176 -0.03527 85  PHE B CG  
2849 C CD1 . PHE B 85  ? 0.18806 0.28348 0.36582 0.00191  -0.00098 -0.03141 85  PHE B CD1 
2850 C CD2 . PHE B 85  ? 0.18733 0.27531 0.37169 -0.00798 -0.00257 -0.03139 85  PHE B CD2 
2851 C CE1 . PHE B 85  ? 0.18225 0.28749 0.36163 -0.00004 -0.00200 -0.02417 85  PHE B CE1 
2852 C CE2 . PHE B 85  ? 0.17855 0.27402 0.36129 -0.00829 -0.00331 -0.02499 85  PHE B CE2 
2853 C CZ  . PHE B 85  ? 0.17781 0.28113 0.35855 -0.00524 -0.00353 -0.02155 85  PHE B CZ  
2854 N N   . ARG B 86  ? 0.20278 0.28703 0.39325 -0.01311 -0.01176 -0.05512 86  ARG B N   
2855 C CA  . ARG B 86  ? 0.19293 0.28995 0.38890 -0.01673 -0.01575 -0.05344 86  ARG B CA  
2856 C C   . ARG B 86  ? 0.19835 0.30353 0.38914 -0.01563 -0.02375 -0.06258 86  ARG B C   
2857 O O   . ARG B 86  ? 0.22969 0.34852 0.41986 -0.01506 -0.02733 -0.05984 86  ARG B O   
2858 C CB  . ARG B 86  ? 0.20222 0.29577 0.41445 -0.02379 -0.01427 -0.05057 86  ARG B CB  
2859 C CG  . ARG B 86  ? 0.20236 0.28872 0.42628 -0.02993 -0.01797 -0.05890 86  ARG B CG  
2860 C CD  . ARG B 86  ? 0.20227 0.28984 0.44608 -0.03688 -0.01477 -0.05329 86  ARG B CD  
2861 N NE  . ARG B 86  ? 0.21876 0.29377 0.47601 -0.04380 -0.01516 -0.05842 86  ARG B NE  
2862 C CZ  . ARG B 86  ? 0.21436 0.27212 0.47267 -0.04409 -0.00713 -0.05413 86  ARG B CZ  
2863 N NH1 . ARG B 86  ? 0.24642 0.29927 0.49314 -0.03777 0.00081  -0.04514 86  ARG B NH1 
2864 N NH2 . ARG B 86  ? 0.25754 0.30175 0.52847 -0.05080 -0.00781 -0.05893 86  ARG B NH2 
2865 N N   . ASN B 87  ? 0.20689 0.30286 0.39177 -0.01420 -0.02708 -0.07353 87  ASN B N   
2866 C CA  . ASN B 87  ? 0.19927 0.30113 0.37503 -0.01219 -0.03627 -0.08409 87  ASN B CA  
2867 C C   . ASN B 87  ? 0.21614 0.31974 0.36949 -0.00117 -0.03459 -0.08739 87  ASN B C   
2868 O O   . ASN B 87  ? 0.22955 0.33813 0.36961 0.00292  -0.04181 -0.09582 87  ASN B O   
2869 C CB  . ASN B 87  ? 0.22109 0.31010 0.40548 -0.01901 -0.04364 -0.09681 87  ASN B CB  
2870 C CG  . ASN B 87  ? 0.24281 0.33692 0.45206 -0.02993 -0.04645 -0.09332 87  ASN B CG  
2871 O OD1 . ASN B 87  ? 0.23049 0.34147 0.44600 -0.03051 -0.04735 -0.08574 87  ASN B OD1 
2872 N ND2 . ASN B 87  ? 0.25435 0.33380 0.47914 -0.03809 -0.04663 -0.09755 87  ASN B ND2 
2873 N N   . THR B 88  ? 0.22264 0.32360 0.37145 0.00448  -0.02539 -0.08069 88  THR B N   
2874 C CA  . THR B 88  ? 0.21981 0.32642 0.35056 0.01575  -0.02144 -0.08108 88  THR B CA  
2875 C C   . THR B 88  ? 0.21301 0.33206 0.34719 0.01815  -0.01334 -0.06613 88  THR B C   
2876 O O   . THR B 88  ? 0.23942 0.37273 0.36629 0.02225  -0.01184 -0.05998 88  THR B O   
2877 C CB  . THR B 88  ? 0.23334 0.32390 0.35595 0.02220  -0.01857 -0.09009 88  THR B CB  
2878 O OG1 . THR B 88  ? 0.26129 0.33743 0.38084 0.01875  -0.02752 -0.10535 88  THR B OG1 
2879 C CG2 . THR B 88  ? 0.24623 0.34492 0.35033 0.03575  -0.01261 -0.08958 88  THR B CG2 
2880 N N   . VAL B 89  ? 0.21155 0.32488 0.35686 0.01553  -0.00859 -0.05988 89  VAL B N   
2881 C CA  . VAL B 89  ? 0.20427 0.32879 0.35337 0.01787  -0.00254 -0.04759 89  VAL B CA  
2882 C C   . VAL B 89  ? 0.19616 0.32952 0.35156 0.01164  -0.00419 -0.03866 89  VAL B C   
2883 O O   . VAL B 89  ? 0.17519 0.32049 0.33062 0.01348  -0.00089 -0.02957 89  VAL B O   
2884 C CB  . VAL B 89  ? 0.19909 0.31535 0.35656 0.01791  0.00087  -0.04427 89  VAL B CB  
2885 C CG1 . VAL B 89  ? 0.20128 0.33077 0.36579 0.01863  0.00443  -0.03226 89  VAL B CG1 
2886 C CG2 . VAL B 89  ? 0.20559 0.31183 0.35610 0.02616  0.00345  -0.05237 89  VAL B CG2 
2887 N N   . LEU B 90  ? 0.18619 0.31363 0.34785 0.00463  -0.00864 -0.04063 90  LEU B N   
2888 C CA  . LEU B 90  ? 0.18425 0.31759 0.35089 0.00037  -0.00979 -0.03286 90  LEU B CA  
2889 C C   . LEU B 90  ? 0.18068 0.32647 0.33918 0.00406  -0.01154 -0.03070 90  LEU B C   
2890 O O   . LEU B 90  ? 0.17554 0.32683 0.33601 0.00307  -0.01022 -0.02139 90  LEU B O   
2891 C CB  . LEU B 90  ? 0.17384 0.29974 0.34959 -0.00584 -0.01269 -0.03540 90  LEU B CB  
2892 C CG  . LEU B 90  ? 0.16987 0.29995 0.35102 -0.00873 -0.01377 -0.02915 90  LEU B CG  
2893 C CD1 . LEU B 90  ? 0.16857 0.29639 0.34956 -0.00917 -0.01020 -0.01986 90  LEU B CD1 
2894 C CD2 . LEU B 90  ? 0.16959 0.29388 0.36168 -0.01342 -0.01447 -0.03171 90  LEU B CD2 
2895 N N   . ILE B 91  ? 0.18555 0.33423 0.33315 0.00897  -0.01473 -0.03907 91  ILE B N   
2896 C CA  . ILE B 91  ? 0.19591 0.35585 0.33284 0.01355  -0.01785 -0.03754 91  ILE B CA  
2897 C C   . ILE B 91  ? 0.20428 0.37186 0.32533 0.02328  -0.01240 -0.03530 91  ILE B C   
2898 O O   . ILE B 91  ? 0.22017 0.39539 0.32617 0.02980  -0.01496 -0.03643 91  ILE B O   
2899 C CB  . ILE B 91  ? 0.20710 0.36663 0.34209 0.01217  -0.02803 -0.04886 91  ILE B CB  
2900 C CG1 . ILE B 91  ? 0.20655 0.35546 0.33545 0.01346  -0.03086 -0.06300 91  ILE B CG1 
2901 C CG2 . ILE B 91  ? 0.19836 0.35593 0.35186 0.00363  -0.03139 -0.04715 91  ILE B CG2 
2902 C CD1 . ILE B 91  ? 0.21130 0.36036 0.33680 0.01206  -0.04276 -0.07548 91  ILE B CD1 
2903 N N   . ASN B 92  ? 0.21413 0.38113 0.33833 0.02534  -0.00461 -0.03129 92  ASN B N   
2904 C CA  . ASN B 92  ? 0.22079 0.39726 0.33335 0.03539  0.00318  -0.02725 92  ASN B CA  
2905 C C   . ASN B 92  ? 0.21267 0.40217 0.31953 0.03842  0.00655  -0.01484 92  ASN B C   
2906 O O   . ASN B 92  ? 0.21957 0.41151 0.33995 0.03179  0.00829  -0.00331 92  ASN B O   
2907 C CB  . ASN B 92  ? 0.22730 0.40556 0.35222 0.03544  0.01092  -0.02091 92  ASN B CB  
2908 C CG  . ASN B 92  ? 0.23730 0.42897 0.35452 0.04636  0.02108  -0.01443 92  ASN B CG  
2909 O OD1 . ASN B 92  ? 0.22695 0.43179 0.34819 0.04674  0.02709  -0.00077 92  ASN B OD1 
2910 N ND2 . ASN B 92  ? 0.26150 0.44906 0.36807 0.05579  0.02400  -0.02363 92  ASN B ND2 
2911 N N   . PRO B 93  ? 0.21837 0.41453 0.30395 0.04887  0.00759  -0.01668 93  PRO B N   
2912 C CA  . PRO B 93  ? 0.22333 0.43059 0.30164 0.05262  0.01091  -0.00351 93  PRO B CA  
2913 C C   . PRO B 93  ? 0.23020 0.44747 0.31979 0.05256  0.02345  0.01419  93  PRO B C   
2914 O O   . PRO B 93  ? 0.23930 0.46152 0.33196 0.05082  0.02610  0.02776  93  PRO B O   
2915 C CB  . PRO B 93  ? 0.23171 0.44260 0.28037 0.06597  0.00920  -0.01133 93  PRO B CB  
2916 C CG  . PRO B 93  ? 0.24082 0.44374 0.28300 0.07048  0.00996  -0.02538 93  PRO B CG  
2917 C CD  . PRO B 93  ? 0.24433 0.43538 0.30891 0.05806  0.00435  -0.03190 93  PRO B CD  
2918 N N   . VAL B 94  ? 0.23113 0.45192 0.32874 0.05445  0.03117  0.01523  94  VAL B N   
2919 C CA  . VAL B 94  ? 0.22643 0.45947 0.34127 0.05232  0.04202  0.03263  94  VAL B CA  
2920 C C   . VAL B 94  ? 0.21103 0.43779 0.35001 0.03753  0.03707  0.03849  94  VAL B C   
2921 O O   . VAL B 94  ? 0.21652 0.44710 0.36532 0.03254  0.04040  0.05259  94  VAL B O   
2922 C CB  . VAL B 94  ? 0.23320 0.47438 0.35321 0.05904  0.05077  0.03214  94  VAL B CB  
2923 C CG1 . VAL B 94  ? 0.22268 0.48043 0.36557 0.05582  0.06136  0.05098  94  VAL B CG1 
2924 C CG2 . VAL B 94  ? 0.25178 0.49571 0.34374 0.07560  0.05606  0.02462  94  VAL B CG2 
2925 N N   . ILE B 95  ? 0.20980 0.42473 0.35682 0.03090  0.02916  0.02762  95  ILE B N   
2926 C CA  . ILE B 95  ? 0.19427 0.40064 0.35897 0.01865  0.02380  0.03092  95  ILE B CA  
2927 C C   . ILE B 95  ? 0.20203 0.40316 0.36336 0.01520  0.02055  0.03619  95  ILE B C   
2928 O O   . ILE B 95  ? 0.20032 0.39941 0.37391 0.00824  0.02150  0.04667  95  ILE B O   
2929 C CB  . ILE B 95  ? 0.20069 0.39378 0.36802 0.01475  0.01642  0.01797  95  ILE B CB  
2930 C CG1 . ILE B 95  ? 0.21103 0.40762 0.38060 0.02002  0.01984  0.01329  95  ILE B CG1 
2931 C CG2 . ILE B 95  ? 0.19342 0.37663 0.37418 0.00420  0.01136  0.02095  95  ILE B CG2 
2932 C CD1 . ILE B 95  ? 0.20707 0.41726 0.39418 0.01896  0.02570  0.02477  95  ILE B CD1 
2933 N N   . HIS B 96  ? 0.21390 0.41232 0.35931 0.02020  0.01593  0.02888  96  HIS B N   
2934 C CA  . HIS B 96  ? 0.21351 0.40837 0.35647 0.01878  0.01273  0.03460  96  HIS B CA  
2935 C C   . HIS B 96  ? 0.21840 0.42217 0.35738 0.02310  0.02059  0.05044  96  HIS B C   
2936 O O   . HIS B 96  ? 0.21520 0.41359 0.35950 0.01950  0.02067  0.06031  96  HIS B O   
2937 C CB  . HIS B 96  ? 0.20770 0.40083 0.33820 0.02289  0.00447  0.02315  96  HIS B CB  
2938 C CG  . HIS B 96  ? 0.19331 0.37612 0.33302 0.01635  -0.00194 0.01160  96  HIS B CG  
2939 N ND1 . HIS B 96  ? 0.19618 0.36971 0.34736 0.00959  -0.00446 0.01372  96  HIS B ND1 
2940 C CD2 . HIS B 96  ? 0.19108 0.36985 0.33048 0.01586  -0.00459 -0.00071 96  HIS B CD2 
2941 C CE1 . HIS B 96  ? 0.18291 0.34902 0.33991 0.00560  -0.00790 0.00389  96  HIS B CE1 
2942 N NE2 . HIS B 96  ? 0.18558 0.35423 0.33666 0.00866  -0.00822 -0.00460 96  HIS B NE2 
2943 N N   . ALA B 97  ? 0.21982 0.43600 0.34977 0.03131  0.02853  0.05411  97  ALA B N   
2944 C CA  . ALA B 97  ? 0.21822 0.44370 0.34787 0.03473  0.03887  0.07228  97  ALA B CA  
2945 C C   . ALA B 97  ? 0.21247 0.43538 0.36854 0.02280  0.04253  0.08397  97  ALA B C   
2946 O O   . ALA B 97  ? 0.21376 0.43388 0.37574 0.01952  0.04609  0.09819  97  ALA B O   
2947 C CB  . ALA B 97  ? 0.21363 0.45382 0.32935 0.04680  0.04877  0.07440  97  ALA B CB  
2948 N N   . ILE B 98  ? 0.20809 0.43021 0.38022 0.01597  0.04035  0.07770  98  ILE B N   
2949 C CA  . ILE B 98  ? 0.19046 0.41115 0.38816 0.00411  0.04127  0.08714  98  ILE B CA  
2950 C C   . ILE B 98  ? 0.19384 0.39470 0.39624 -0.00517 0.03248  0.08535  98  ILE B C   
2951 O O   . ILE B 98  ? 0.18938 0.38460 0.40542 -0.01309 0.03381  0.09671  98  ILE B O   
2952 C CB  . ILE B 98  ? 0.18004 0.40726 0.39199 0.00124  0.04008  0.08090  98  ILE B CB  
2953 C CG1 . ILE B 98  ? 0.19900 0.44556 0.40589 0.01272  0.05070  0.08362  98  ILE B CG1 
2954 C CG2 . ILE B 98  ? 0.18348 0.41100 0.42270 -0.01153 0.03840  0.08978  98  ILE B CG2 
2955 C CD1 . ILE B 98  ? 0.19819 0.44823 0.40928 0.01556  0.04865  0.07273  98  ILE B CD1 
2956 N N   . CYS B 99  ? 0.20433 0.39363 0.39579 -0.00394 0.02404  0.07148  99  CYS B N   
2957 C CA  . CYS B 99  ? 0.19394 0.36449 0.38813 -0.01037 0.01711  0.06916  99  CYS B CA  
2958 C C   . CYS B 99  ? 0.20414 0.36933 0.39233 -0.00762 0.01951  0.07982  99  CYS B C   
2959 O O   . CYS B 99  ? 0.20962 0.36000 0.40579 -0.01409 0.01798  0.08548  99  CYS B O   
2960 C CB  . CYS B 99  ? 0.19349 0.35632 0.37917 -0.00844 0.00994  0.05387  99  CYS B CB  
2961 S SG  . CYS B 99  ? 0.18710 0.34834 0.37940 -0.01225 0.00615  0.04223  99  CYS B SG  
2962 N N   . GLU B 100 ? 0.20501 0.38057 0.37765 0.00275  0.02268  0.08244  100 GLU B N   
2963 C CA  . GLU B 100 ? 0.21167 0.38301 0.37670 0.00752  0.02466  0.09360  100 GLU B CA  
2964 C C   . GLU B 100 ? 0.21084 0.38058 0.38712 0.00296  0.03321  0.11198  100 GLU B C   
2965 O O   . GLU B 100 ? 0.21478 0.36960 0.39472 0.00023  0.03315  0.12054  100 GLU B O   
2966 C CB  . GLU B 100 ? 0.22081 0.40558 0.36476 0.02051  0.02501  0.09238  100 GLU B CB  
2967 C CG  . GLU B 100 ? 0.24879 0.43049 0.38435 0.02453  0.01505  0.08042  100 GLU B CG  
2968 C CD  . GLU B 100 ? 0.30476 0.50068 0.42004 0.03602  0.01213  0.07543  100 GLU B CD  
2969 O OE1 . GLU B 100 ? 0.32007 0.52631 0.42353 0.04286  0.01928  0.08274  100 GLU B OE1 
2970 O OE2 . GLU B 100 ? 0.33678 0.53395 0.44806 0.03837  0.00259  0.06410  100 GLU B OE2 
2971 N N   . ALA B 101 ? 0.21454 0.39923 0.39769 0.00238  0.04132  0.11898  101 ALA B N   
2972 C CA  . ALA B 101 ? 0.23780 0.42274 0.43811 -0.00440 0.04993  0.13744  101 ALA B CA  
2973 C C   . ALA B 101 ? 0.22869 0.39797 0.45197 -0.01984 0.04353  0.13519  101 ALA B C   
2974 O O   . ALA B 101 ? 0.26498 0.42131 0.50029 -0.02735 0.04537  0.14710  101 ALA B O   
2975 C CB  . ALA B 101 ? 0.23908 0.44731 0.44410 -0.00059 0.06117  0.14576  101 ALA B CB  
2976 N N   . TYR B 102 ? 0.21588 0.38434 0.44412 -0.02442 0.03545  0.11984  102 TYR B N   
2977 C CA  . TYR B 102 ? 0.20539 0.35944 0.45196 -0.03798 0.02770  0.11621  102 TYR B CA  
2978 C C   . TYR B 102 ? 0.22352 0.35024 0.46263 -0.04017 0.02077  0.11185  102 TYR B C   
2979 O O   . TYR B 102 ? 0.23736 0.34704 0.48895 -0.05008 0.01803  0.11698  102 TYR B O   
2980 C CB  . TYR B 102 ? 0.19783 0.35840 0.44759 -0.03965 0.02113  0.10170  102 TYR B CB  
2981 C CG  . TYR B 102 ? 0.18405 0.33015 0.44744 -0.05167 0.01067  0.09512  102 TYR B CG  
2982 C CD1 . TYR B 102 ? 0.16932 0.31971 0.45155 -0.06083 0.00930  0.10059  102 TYR B CD1 
2983 C CD2 . TYR B 102 ? 0.18963 0.31550 0.44013 -0.05138 0.00179  0.08154  102 TYR B CD2 
2984 C CE1 . TYR B 102 ? 0.17870 0.31293 0.46473 -0.06946 -0.00248 0.09147  102 TYR B CE1 
2985 C CE2 . TYR B 102 ? 0.18148 0.29317 0.43949 -0.06055 -0.00810 0.07494  102 TYR B CE2 
2986 C CZ  . TYR B 102 ? 0.17954 0.29548 0.45594 -0.07028 -0.01151 0.07943  102 TYR B CZ  
2987 O OH  . TYR B 102 ? 0.18442 0.28456 0.46137 -0.07741 -0.02315 0.07049  102 TYR B OH  
2988 N N   . PHE B 103 ? 0.22258 0.34463 0.44245 -0.03079 0.01798  0.10262  103 PHE B N   
2989 C CA  . PHE B 103 ? 0.23893 0.33735 0.45132 -0.03018 0.01255  0.09772  103 PHE B CA  
2990 C C   . PHE B 103 ? 0.25393 0.34475 0.45915 -0.02366 0.01749  0.11032  103 PHE B C   
2991 O O   . PHE B 103 ? 0.27179 0.34656 0.46853 -0.01904 0.01427  0.10660  103 PHE B O   
2992 C CB  . PHE B 103 ? 0.22512 0.32455 0.42478 -0.02353 0.00748  0.08239  103 PHE B CB  
2993 C CG  . PHE B 103 ? 0.21050 0.30948 0.41441 -0.02902 0.00191  0.06988  103 PHE B CG  
2994 C CD1 . PHE B 103 ? 0.20816 0.28787 0.41683 -0.03686 -0.00407 0.06524  103 PHE B CD1 
2995 C CD2 . PHE B 103 ? 0.19303 0.30875 0.39361 -0.02517 0.00210  0.06224  103 PHE B CD2 
2996 C CE1 . PHE B 103 ? 0.19467 0.27417 0.40433 -0.04020 -0.00962 0.05456  103 PHE B CE1 
2997 C CE2 . PHE B 103 ? 0.18686 0.30101 0.39026 -0.02880 -0.00247 0.05227  103 PHE B CE2 
2998 C CZ  . PHE B 103 ? 0.18120 0.27825 0.38877 -0.03595 -0.00828 0.04902  103 PHE B CZ  
2999 N N   . GLN B 104 ? 0.24897 0.35119 0.45709 -0.02192 0.02608  0.12616  104 GLN B N   
3000 C CA  . GLN B 104 ? 0.24865 0.34662 0.44616 -0.01271 0.03132  0.13932  104 GLN B CA  
3001 C C   . GLN B 104 ? 0.26360 0.33157 0.46485 -0.01635 0.02930  0.14389  104 GLN B C   
3002 O O   . GLN B 104 ? 0.27571 0.33557 0.46498 -0.00618 0.02977  0.14801  104 GLN B O   
3003 C CB  . GLN B 104 ? 0.26134 0.37511 0.46174 -0.01085 0.04258  0.15760  104 GLN B CB  
3004 C CG  . GLN B 104 ? 0.27747 0.38868 0.50275 -0.02545 0.04626  0.16620  104 GLN B CG  
3005 C CD  . GLN B 104 ? 0.35023 0.47647 0.58169 -0.02382 0.05997  0.18767  104 GLN B CD  
3006 O OE1 . GLN B 104 ? 0.41655 0.54679 0.63119 -0.01170 0.06707  0.19933  104 GLN B OE1 
3007 N NE2 . GLN B 104 ? 0.34381 0.47971 0.60017 -0.03554 0.06401  0.19407  104 GLN B NE2 
3008 N N   . ARG B 105 ? 0.28275 0.33337 0.50011 -0.03007 0.02625  0.14274  105 ARG B N   
3009 C CA  . ARG B 105 ? 0.29448 0.31188 0.51389 -0.03380 0.02370  0.14533  105 ARG B CA  
3010 C C   . ARG B 105 ? 0.29093 0.29060 0.49870 -0.02956 0.01552  0.12828  105 ARG B C   
3011 O O   . ARG B 105 ? 0.31607 0.28846 0.51876 -0.02664 0.01466  0.12960  105 ARG B O   
3012 C CB  . ARG B 105 ? 0.29044 0.29410 0.53185 -0.05114 0.02176  0.14960  105 ARG B CB  
3013 C CG  . ARG B 105 ? 0.28854 0.30088 0.54539 -0.05607 0.03226  0.17174  105 ARG B CG  
3014 C CD  . ARG B 105 ? 0.30899 0.29864 0.58957 -0.07399 0.02885  0.17682  105 ARG B CD  
3015 N NE  . ARG B 105 ? 0.29596 0.29425 0.58907 -0.08540 0.01897  0.16215  105 ARG B NE  
3016 C CZ  . ARG B 105 ? 0.31123 0.28678 0.60915 -0.09624 0.00741  0.15004  105 ARG B CZ  
3017 N NH1 . ARG B 105 ? 0.34090 0.28161 0.63388 -0.09865 0.00467  0.15011  105 ARG B NH1 
3018 N NH2 . ARG B 105 ? 0.33494 0.32240 0.64040 -0.10360 -0.00179 0.13725  105 ARG B NH2 
3019 N N   . THR B 106 ? 0.27425 0.28734 0.47760 -0.02846 0.01056  0.11310  106 THR B N   
3020 C CA  . THR B 106 ? 0.27000 0.26746 0.46299 -0.02416 0.00479  0.09855  106 THR B CA  
3021 C C   . THR B 106 ? 0.27452 0.28777 0.45590 -0.01056 0.00605  0.09428  106 THR B C   
3022 O O   . THR B 106 ? 0.27009 0.27062 0.44396 -0.00418 0.00416  0.08672  106 THR B O   
3023 C CB  . THR B 106 ? 0.27058 0.26697 0.46743 -0.03330 -0.00230 0.08458  106 THR B CB  
3024 O OG1 . THR B 106 ? 0.29693 0.27802 0.48119 -0.02763 -0.00613 0.07159  106 THR B OG1 
3025 C CG2 . THR B 106 ? 0.26526 0.29255 0.46605 -0.03368 -0.00128 0.08201  106 THR B CG2 
3026 N N   . GLY B 107 ? 0.27372 0.31415 0.45374 -0.00570 0.00907  0.09894  107 GLY B N   
3027 C CA  . GLY B 107 ? 0.27721 0.33380 0.44858 0.00580  0.00811  0.09473  107 GLY B CA  
3028 C C   . GLY B 107 ? 0.26072 0.33607 0.43205 0.00451  0.00472  0.08168  107 GLY B C   
3029 O O   . GLY B 107 ? 0.23589 0.32153 0.41132 -0.00192 0.00515  0.07984  107 GLY B O   
3030 N N   . ASP B 108 ? 0.23239 0.31237 0.40076 0.01095  0.00189  0.07345  108 ASP B N   
3031 C CA  . ASP B 108 ? 0.20476 0.30137 0.37402 0.01023  -0.00115 0.06200  108 ASP B CA  
3032 C C   . ASP B 108 ? 0.17879 0.26570 0.35150 0.00174  -0.00229 0.05270  108 ASP B C   
3033 O O   . ASP B 108 ? 0.19481 0.26115 0.36743 -0.00168 -0.00244 0.05179  108 ASP B O   
3034 C CB  . ASP B 108 ? 0.19487 0.29916 0.36483 0.01806  -0.00359 0.05735  108 ASP B CB  
3035 C CG  . ASP B 108 ? 0.18527 0.31051 0.35197 0.02566  -0.00639 0.06114  108 ASP B CG  
3036 O OD1 . ASP B 108 ? 0.20241 0.33468 0.36255 0.02641  -0.00517 0.06774  108 ASP B OD1 
3037 O OD2 . ASP B 108 ? 0.19897 0.33466 0.36980 0.03129  -0.00996 0.05773  108 ASP B OD2 
3038 N N   . TYR B 109 ? 0.16412 0.26489 0.33812 -0.00063 -0.00376 0.04523  109 TYR B N   
3039 C CA  . TYR B 109 ? 0.16570 0.26068 0.34209 -0.00718 -0.00508 0.03733  109 TYR B CA  
3040 C C   . TYR B 109 ? 0.16783 0.27171 0.34459 -0.00514 -0.00634 0.02780  109 TYR B C   
3041 O O   . TYR B 109 ? 0.15666 0.27427 0.33367 -0.00063 -0.00738 0.02668  109 TYR B O   
3042 C CB  . TYR B 109 ? 0.16413 0.26687 0.34457 -0.01276 -0.00437 0.04027  109 TYR B CB  
3043 C CG  . TYR B 109 ? 0.18066 0.30388 0.35844 -0.00824 -0.00250 0.04153  109 TYR B CG  
3044 C CD1 . TYR B 109 ? 0.18476 0.31518 0.35885 -0.00378 0.00055  0.05177  109 TYR B CD1 
3045 C CD2 . TYR B 109 ? 0.18400 0.31676 0.36060 -0.00740 -0.00374 0.03236  109 TYR B CD2 
3046 C CE1 . TYR B 109 ? 0.19191 0.33951 0.35879 0.00206  0.00184  0.05175  109 TYR B CE1 
3047 C CE2 . TYR B 109 ? 0.17684 0.32486 0.34750 -0.00222 -0.00276 0.03171  109 TYR B CE2 
3048 C CZ  . TYR B 109 ? 0.18465 0.34088 0.34895 0.00305  -0.00020 0.04082  109 TYR B CZ  
3049 O OH  . TYR B 109 ? 0.20768 0.37770 0.36163 0.00973  0.00040  0.03915  109 TYR B OH  
3050 N N   . TRP B 110 ? 0.15905 0.25433 0.33597 -0.00859 -0.00683 0.02120  110 TRP B N   
3051 C CA  . TRP B 110 ? 0.15520 0.25698 0.33414 -0.00797 -0.00692 0.01356  110 TRP B CA  
3052 C C   . TRP B 110 ? 0.15645 0.25122 0.33400 -0.01214 -0.00739 0.00919  110 TRP B C   
3053 O O   . TRP B 110 ? 0.16009 0.24688 0.33608 -0.01560 -0.00898 0.01137  110 TRP B O   
3054 C CB  . TRP B 110 ? 0.14875 0.24794 0.33007 -0.00378 -0.00512 0.01212  110 TRP B CB  
3055 C CG  . TRP B 110 ? 0.15948 0.23991 0.33542 -0.00163 -0.00245 0.01335  110 TRP B CG  
3056 C CD1 . TRP B 110 ? 0.16591 0.22873 0.33382 -0.00444 -0.00355 0.01309  110 TRP B CD1 
3057 C CD2 . TRP B 110 ? 0.15947 0.23688 0.33709 0.00474  0.00139  0.01442  110 TRP B CD2 
3058 N NE1 . TRP B 110 ? 0.17109 0.21717 0.33177 0.00040  -0.00080 0.01260  110 TRP B NE1 
3059 C CE2 . TRP B 110 ? 0.16946 0.22472 0.33621 0.00681  0.00347  0.01412  110 TRP B CE2 
3060 C CE3 . TRP B 110 ? 0.15791 0.25032 0.34627 0.00923  0.00288  0.01552  110 TRP B CE3 
3061 C CZ2 . TRP B 110 ? 0.18606 0.23252 0.34999 0.01495  0.00894  0.01519  110 TRP B CZ2 
3062 C CZ3 . TRP B 110 ? 0.15497 0.24214 0.34503 0.01642  0.00828  0.01791  110 TRP B CZ3 
3063 C CH2 . TRP B 110 ? 0.17183 0.23559 0.34856 0.02005  0.01226  0.01783  110 TRP B CH2 
3064 N N   . LEU B 111 ? 0.15213 0.25035 0.33151 -0.01195 -0.00669 0.00339  111 LEU B N   
3065 C CA  . LEU B 111 ? 0.15601 0.24835 0.33336 -0.01408 -0.00693 0.00001  111 LEU B CA  
3066 C C   . LEU B 111 ? 0.17096 0.24712 0.34175 -0.01309 -0.00568 -0.00063 111 LEU B C   
3067 O O   . LEU B 111 ? 0.17025 0.24366 0.34147 -0.01024 -0.00181 -0.00152 111 LEU B O   
3068 C CB  . LEU B 111 ? 0.14749 0.24644 0.32858 -0.01369 -0.00595 -0.00523 111 LEU B CB  
3069 C CG  . LEU B 111 ? 0.14714 0.23987 0.32583 -0.01426 -0.00575 -0.00744 111 LEU B CG  
3070 C CD1 . LEU B 111 ? 0.15305 0.25190 0.33217 -0.01511 -0.00816 -0.00507 111 LEU B CD1 
3071 C CD2 . LEU B 111 ? 0.14273 0.23713 0.32523 -0.01381 -0.00407 -0.01245 111 LEU B CD2 
3072 N N   . SER B 112 ? 0.17162 0.23774 0.33644 -0.01508 -0.00907 -0.00011 112 SER B N   
3073 C CA  . SER B 112 ? 0.18102 0.22972 0.33423 -0.01278 -0.00898 -0.00213 112 SER B CA  
3074 C C   . SER B 112 ? 0.19122 0.23741 0.33990 -0.01133 -0.00825 -0.00467 112 SER B C   
3075 O O   . SER B 112 ? 0.19607 0.23103 0.33491 -0.00695 -0.00437 -0.00549 112 SER B O   
3076 C CB  . SER B 112 ? 0.18049 0.21699 0.32776 -0.01578 -0.01530 -0.00177 112 SER B CB  
3077 O OG  . SER B 112 ? 0.18958 0.20706 0.32100 -0.01210 -0.01609 -0.00531 112 SER B OG  
3078 N N   . ALA B 113 ? 0.17604 0.23222 0.33107 -0.01353 -0.01065 -0.00496 113 ALA B N   
3079 C CA  . ALA B 113 ? 0.18536 0.23877 0.33680 -0.01107 -0.00956 -0.00624 113 ALA B CA  
3080 C C   . ALA B 113 ? 0.18977 0.25665 0.35131 -0.01211 -0.01029 -0.00656 113 ALA B C   
3081 O O   . ALA B 113 ? 0.18626 0.26407 0.35497 -0.01462 -0.01295 -0.00514 113 ALA B O   
3082 C CB  . ALA B 113 ? 0.20364 0.24530 0.34248 -0.00961 -0.01519 -0.00667 113 ALA B CB  
3083 N N   . ALA B 114 ? 0.19623 0.26111 0.35789 -0.00943 -0.00680 -0.00785 114 ALA B N   
3084 C CA  . ALA B 114 ? 0.19879 0.27149 0.36612 -0.00793 -0.00742 -0.00873 114 ALA B CA  
3085 C C   . ALA B 114 ? 0.20252 0.26455 0.36472 -0.00380 -0.00468 -0.00841 114 ALA B C   
3086 O O   . ALA B 114 ? 0.20767 0.26199 0.36991 -0.00373 0.00086  -0.00903 114 ALA B O   
3087 C CB  . ALA B 114 ? 0.18595 0.26831 0.36087 -0.00876 -0.00505 -0.01190 114 ALA B CB  
3088 N N   . PHE B 115 ? 0.22149 0.28393 0.38094 -0.00033 -0.00854 -0.00637 115 PHE B N   
3089 C CA  . PHE B 115 ? 0.23404 0.28533 0.38585 0.00531  -0.00676 -0.00411 115 PHE B CA  
3090 C C   . PHE B 115 ? 0.24941 0.30872 0.40645 0.01001  -0.00975 -0.00293 115 PHE B C   
3091 O O   . PHE B 115 ? 0.24991 0.32443 0.41657 0.00865  -0.01298 -0.00329 115 PHE B O   
3092 C CB  . PHE B 115 ? 0.23830 0.27880 0.37493 0.00755  -0.00988 -0.00151 115 PHE B CB  
3093 C CG  . PHE B 115 ? 0.26034 0.30758 0.39573 0.00569  -0.02043 -0.00175 115 PHE B CG  
3094 C CD1 . PHE B 115 ? 0.26205 0.31111 0.39896 -0.00020 -0.02353 -0.00372 115 PHE B CD1 
3095 C CD2 . PHE B 115 ? 0.26137 0.31292 0.39572 0.00962  -0.02788 0.00037  115 PHE B CD2 
3096 C CE1 . PHE B 115 ? 0.25110 0.30445 0.38956 -0.00376 -0.03386 -0.00402 115 PHE B CE1 
3097 C CE2 . PHE B 115 ? 0.26329 0.32250 0.40057 0.00610  -0.03924 -0.00006 115 PHE B CE2 
3098 C CZ  . PHE B 115 ? 0.26733 0.32653 0.40714 -0.00140 -0.04220 -0.00248 115 PHE B CZ  
3099 N N   . LEU B 116 ? 0.27341 0.32287 0.42454 0.01656  -0.00775 -0.00017 116 LEU B N   
3100 C CA  . LEU B 116 ? 0.26382 0.31964 0.42009 0.02340  -0.00940 0.00166  116 LEU B CA  
3101 C C   . LEU B 116 ? 0.28848 0.34331 0.43645 0.02920  -0.01646 0.00687  116 LEU B C   
3102 O O   . LEU B 116 ? 0.32337 0.36347 0.45639 0.03175  -0.01566 0.00953  116 LEU B O   
3103 C CB  . LEU B 116 ? 0.27191 0.31535 0.42897 0.02766  -0.00135 0.00044  116 LEU B CB  
3104 C CG  . LEU B 116 ? 0.27853 0.32240 0.43938 0.03709  0.00004  0.00168  116 LEU B CG  
3105 C CD1 . LEU B 116 ? 0.30308 0.33506 0.45438 0.04536  -0.00033 0.00880  116 LEU B CD1 
3106 C CD2 . LEU B 116 ? 0.27577 0.34223 0.44723 0.03968  -0.00441 0.00177  116 LEU B CD2 
3107 N N   . ARG B 117 ? 0.28697 0.35885 0.44481 0.03184  -0.02341 0.00879  117 ARG B N   
3108 C CA  . ARG B 117 ? 0.31898 0.39387 0.47251 0.03897  -0.03185 0.01375  117 ARG B CA  
3109 C C   . ARG B 117 ? 0.30225 0.38379 0.46498 0.04912  -0.02891 0.01719  117 ARG B C   
3110 O O   . ARG B 117 ? 0.28956 0.38600 0.46792 0.04919  -0.02589 0.01588  117 ARG B O   
3111 C CB  . ARG B 117 ? 0.32922 0.42100 0.49071 0.03324  -0.04460 0.01376  117 ARG B CB  
3112 C CG  . ARG B 117 ? 0.35465 0.44771 0.50809 0.03917  -0.05685 0.01727  117 ARG B CG  
3113 C CD  . ARG B 117 ? 0.41725 0.48535 0.54289 0.04466  -0.05443 0.01794  117 ARG B CD  
3114 N NE  . ARG B 117 ? 0.44892 0.51365 0.55845 0.04642  -0.06828 0.01765  117 ARG B NE  
3115 C CZ  . ARG B 117 ? 0.47826 0.54050 0.57507 0.05723  -0.07509 0.02238  117 ARG B CZ  
3116 N NH1 . ARG B 117 ? 0.50672 0.56874 0.60630 0.06770  -0.06850 0.02896  117 ARG B NH1 
3117 N NH2 . ARG B 117 ? 0.46181 0.52005 0.54096 0.05837  -0.08939 0.02020  117 ARG B NH2 
3118 N N   . GLU B 118 ? 0.35992 0.42950 0.51144 0.05911  -0.02882 0.02217  118 GLU B N   
3119 C CA  . GLU B 118 ? 0.36556 0.43919 0.52407 0.07118  -0.02666 0.02658  118 GLU B CA  
3120 C C   . GLU B 118 ? 0.37765 0.46282 0.53484 0.07870  -0.03908 0.03304  118 GLU B C   
3121 O O   . GLU B 118 ? 0.41580 0.48939 0.55436 0.08018  -0.04472 0.03541  118 GLU B O   
3122 C CB  . GLU B 118 ? 0.38764 0.43508 0.53534 0.07768  -0.01538 0.02808  118 GLU B CB  
3123 C CG  . GLU B 118 ? 0.39590 0.44329 0.55002 0.09127  -0.01176 0.03191  118 GLU B CG  
3124 C CD  . GLU B 118 ? 0.43081 0.44815 0.57459 0.09715  -0.00108 0.03404  118 GLU B CD  
3125 O OE1 . GLU B 118 ? 0.45699 0.45921 0.58625 0.10273  -0.00097 0.04179  118 GLU B OE1 
3126 O OE2 . GLU B 118 ? 0.42177 0.42949 0.57135 0.09637  0.00714  0.02808  118 GLU B OE2 
3127 N N   . ILE B 119 ? 0.37740 0.48658 0.55410 0.08409  -0.04360 0.03603  119 ILE B N   
3128 C CA  . ILE B 119 ? 0.38690 0.51403 0.56880 0.08978  -0.05818 0.04183  119 ILE B CA  
3129 C C   . ILE B 119 ? 0.41509 0.54698 0.60370 0.10662  -0.05498 0.04900  119 ILE B C   
3130 O O   . ILE B 119 ? 0.40128 0.55115 0.61093 0.11079  -0.04984 0.04990  119 ILE B O   
3131 C CB  . ILE B 119 ? 0.38046 0.53753 0.58601 0.07970  -0.06846 0.04055  119 ILE B CB  
3132 C CG1 . ILE B 119 ? 0.36188 0.51079 0.56062 0.06378  -0.07008 0.03347  119 ILE B CG1 
3133 C CG2 . ILE B 119 ? 0.40364 0.57941 0.61619 0.08408  -0.08606 0.04568  119 ILE B CG2 
3134 C CD1 . ILE B 119 ? 0.33127 0.48314 0.54106 0.05621  -0.05791 0.02948  119 ILE B CD1 
3135 N N   . GLU B 120 ? 0.38587 0.50123 0.55549 0.11773  -0.05713 0.05486  120 GLU B N   
3136 C CA  . GLU B 120 ? 0.38580 0.50069 0.55811 0.13569  -0.05394 0.06295  120 GLU B CA  
3137 C C   . GLU B 120 ? 0.40331 0.55246 0.59542 0.14273  -0.06884 0.06901  120 GLU B C   
3138 O O   . GLU B 120 ? 0.38987 0.55801 0.58861 0.13332  -0.08392 0.06719  120 GLU B O   
3139 C CB  . GLU B 120 ? 0.39654 0.48071 0.54045 0.14515  -0.05066 0.06902  120 GLU B CB  
3140 C CG  . GLU B 120 ? 0.45695 0.50919 0.58293 0.13621  -0.03760 0.06458  120 GLU B CG  
3141 C CD  . GLU B 120 ? 0.48110 0.52802 0.58965 0.12527  -0.04407 0.06124  120 GLU B CD  
3142 O OE1 . GLU B 120 ? 0.45727 0.51985 0.57585 0.11227  -0.05024 0.05362  120 GLU B OE1 
3143 O OE2 . GLU B 120 ? 0.52060 0.54624 0.60438 0.13059  -0.04187 0.06680  120 GLU B OE2 
3144 N N   . SER B 121 ? 0.41579 0.53215 0.79549 0.05532  -0.03364 0.20793  121 SER B N   
3145 C CA  . SER B 121 ? 0.44307 0.57675 0.83262 0.05982  -0.03752 0.21438  121 SER B CA  
3146 C C   . SER B 121 ? 0.38373 0.53851 0.76389 0.05513  -0.04449 0.23001  121 SER B C   
3147 O O   . SER B 121 ? 0.36187 0.51608 0.73915 0.05181  -0.04664 0.24198  121 SER B O   
3148 C CB  . SER B 121 ? 0.53231 0.65598 0.94344 0.06693  -0.03580 0.21662  121 SER B CB  
3149 O OG  . SER B 121 ? 0.56833 0.68117 0.98911 0.07239  -0.03005 0.20054  121 SER B OG  
3150 N N   . GLY B 122 ? 0.38752 0.56166 0.76058 0.05344  -0.04746 0.22830  122 GLY B N   
3151 C CA  . GLY B 122 ? 0.33310 0.53004 0.69438 0.04784  -0.05393 0.23958  122 GLY B CA  
3152 C C   . GLY B 122 ? 0.32518 0.52706 0.65974 0.03824  -0.05336 0.22967  122 GLY B C   
3153 O O   . GLY B 122 ? 0.29413 0.51624 0.61730 0.03290  -0.05842 0.23681  122 GLY B O   
3154 N N   . MET B 123 ? 0.34588 0.53126 0.67083 0.03596  -0.04744 0.21330  123 MET B N   
3155 C CA  . MET B 123 ? 0.33258 0.52416 0.63446 0.02738  -0.04744 0.20480  123 MET B CA  
3156 C C   . MET B 123 ? 0.35175 0.55483 0.64720 0.02465  -0.04850 0.19401  123 MET B C   
3157 O O   . MET B 123 ? 0.36857 0.56771 0.67437 0.02882  -0.04639 0.18796  123 MET B O   
3158 C CB  . MET B 123 ? 0.35741 0.52859 0.65059 0.02504  -0.04136 0.19363  123 MET B CB  
3159 C CG  . MET B 123 ? 0.35774 0.51822 0.65442 0.02546  -0.04044 0.20341  123 MET B CG  
3160 S SD  . MET B 123 ? 0.35392 0.53414 0.63901 0.01952  -0.04577 0.21882  123 MET B SD  
3161 C CE  . MET B 123 ? 0.26872 0.45479 0.57737 0.02599  -0.05072 0.24183  123 MET B CE  
3162 N N   . PRO B 124 ? 0.30372 0.52208 0.58311 0.01747  -0.05177 0.19137  124 PRO B N   
3163 C CA  . PRO B 124 ? 0.29976 0.52903 0.57424 0.01383  -0.05340 0.18116  124 PRO B CA  
3164 C C   . PRO B 124 ? 0.32764 0.54098 0.59598 0.01161  -0.04782 0.16469  124 PRO B C   
3165 O O   . PRO B 124 ? 0.33008 0.52726 0.59262 0.01102  -0.04328 0.15984  124 PRO B O   
3166 C CB  . PRO B 124 ? 0.29689 0.54642 0.55638 0.00653  -0.05845 0.18253  124 PRO B CB  
3167 C CG  . PRO B 124 ? 0.29750 0.54109 0.54855 0.00504  -0.05674 0.18716  124 PRO B CG  
3168 C CD  . PRO B 124 ? 0.30392 0.53354 0.57081 0.01238  -0.05474 0.19869  124 PRO B CD  
3169 N N   . ALA B 125 ? 0.34888 0.56833 0.61931 0.01000  -0.04849 0.15700  125 ALA B N   
3170 C CA  . ALA B 125 ? 0.32678 0.53464 0.59181 0.00684  -0.04413 0.14297  125 ALA B CA  
3171 C C   . ALA B 125 ? 0.29834 0.50585 0.54691 -0.00039 -0.04443 0.13527  125 ALA B C   
3172 O O   . ALA B 125 ? 0.27009 0.49132 0.51070 -0.00400 -0.04867 0.13855  125 ALA B O   
3173 C CB  . ALA B 125 ? 0.31522 0.53206 0.58743 0.00587  -0.04542 0.13830  125 ALA B CB  
3174 N N   . GLN B 126 ? 0.27720 0.47027 0.52131 -0.00234 -0.03978 0.12487  126 GLN B N   
3175 C CA  . GLN B 126 ? 0.25745 0.44505 0.48931 -0.00794 -0.03828 0.11516  126 GLN B CA  
3176 C C   . GLN B 126 ? 0.25137 0.44640 0.48257 -0.01351 -0.04078 0.10610  126 GLN B C   
3177 O O   . GLN B 126 ? 0.27996 0.47642 0.52053 -0.01283 -0.04085 0.10518  126 GLN B O   
3178 C CB  . GLN B 126 ? 0.26142 0.42963 0.49270 -0.00626 -0.03204 0.11034  126 GLN B CB  
3179 C CG  . GLN B 126 ? 0.26553 0.42713 0.48619 -0.01100 -0.03007 0.10129  126 GLN B CG  
3180 C CD  . GLN B 126 ? 0.24953 0.39427 0.46953 -0.00910 -0.02441 0.09887  126 GLN B CD  
3181 O OE1 . GLN B 126 ? 0.24244 0.38012 0.46883 -0.00751 -0.02147 0.09618  126 GLN B OE1 
3182 N NE2 . GLN B 126 ? 0.28115 0.42131 0.49332 -0.00962 -0.02288 0.09995  126 GLN B NE2 
3183 N N   . PRO B 127 ? 0.23548 0.43610 0.45700 -0.01919 -0.04284 0.09900  127 PRO B N   
3184 C CA  . PRO B 127 ? 0.24833 0.45474 0.47149 -0.02495 -0.04554 0.08940  127 PRO B CA  
3185 C C   . PRO B 127 ? 0.22001 0.41098 0.44781 -0.02611 -0.04151 0.08200  127 PRO B C   
3186 O O   . PRO B 127 ? 0.22609 0.40252 0.45126 -0.02403 -0.03663 0.08090  127 PRO B O   
3187 C CB  . PRO B 127 ? 0.22887 0.44406 0.44052 -0.03001 -0.04797 0.08234  127 PRO B CB  
3188 C CG  . PRO B 127 ? 0.24347 0.46482 0.44811 -0.02703 -0.04813 0.09194  127 PRO B CG  
3189 C CD  . PRO B 127 ? 0.24133 0.44696 0.45130 -0.02074 -0.04352 0.10001  127 PRO B CD  
3190 N N   . PHE B 128 ? 0.22868 0.42441 0.46414 -0.02998 -0.04395 0.07767  128 PHE B N   
3191 C CA  . PHE B 128 ? 0.23128 0.41521 0.47268 -0.03224 -0.04105 0.07201  128 PHE B CA  
3192 C C   . PHE B 128 ? 0.22958 0.40292 0.46433 -0.03511 -0.03910 0.06308  128 PHE B C   
3193 O O   . PHE B 128 ? 0.23668 0.41608 0.46493 -0.03841 -0.04178 0.05657  128 PHE B O   
3194 C CB  . PHE B 128 ? 0.22102 0.41368 0.47250 -0.03728 -0.04496 0.06926  128 PHE B CB  
3195 C CG  . PHE B 128 ? 0.21950 0.41822 0.48125 -0.03422 -0.04455 0.07722  128 PHE B CG  
3196 C CD1 . PHE B 128 ? 0.21431 0.40378 0.48039 -0.03038 -0.03921 0.08062  128 PHE B CD1 
3197 C CD2 . PHE B 128 ? 0.22831 0.44382 0.49558 -0.03520 -0.04940 0.08085  128 PHE B CD2 
3198 C CE1 . PHE B 128 ? 0.20469 0.40171 0.48042 -0.02726 -0.03829 0.08666  128 PHE B CE1 
3199 C CE2 . PHE B 128 ? 0.25225 0.47457 0.52993 -0.03187 -0.04865 0.08781  128 PHE B CE2 
3200 C CZ  . PHE B 128 ? 0.23598 0.44902 0.51792 -0.02775 -0.04284 0.09027  128 PHE B CZ  
3201 N N   . HIS B 129 ? 0.22450 0.38362 0.46144 -0.03383 -0.03441 0.06242  129 HIS B N   
3202 C CA  . HIS B 129 ? 0.23673 0.38560 0.46894 -0.03560 -0.03221 0.05497  129 HIS B CA  
3203 C C   . HIS B 129 ? 0.23737 0.37395 0.47667 -0.03559 -0.02842 0.05531  129 HIS B C   
3204 O O   . HIS B 129 ? 0.22500 0.36170 0.47061 -0.03385 -0.02684 0.06144  129 HIS B O   
3205 C CB  . HIS B 129 ? 0.22509 0.37181 0.44566 -0.03213 -0.02983 0.05683  129 HIS B CB  
3206 C CG  . HIS B 129 ? 0.23362 0.37089 0.45385 -0.02722 -0.02516 0.06378  129 HIS B CG  
3207 N ND1 . HIS B 129 ? 0.23399 0.37451 0.45718 -0.02309 -0.02489 0.07210  129 HIS B ND1 
3208 C CD2 . HIS B 129 ? 0.25291 0.37818 0.47121 -0.02589 -0.02067 0.06284  129 HIS B CD2 
3209 C CE1 . HIS B 129 ? 0.24883 0.37931 0.47173 -0.01967 -0.02036 0.07482  129 HIS B CE1 
3210 N NE2 . HIS B 129 ? 0.23822 0.35996 0.45760 -0.02156 -0.01787 0.06967  129 HIS B NE2 
3211 N N   . ARG B 130 ? 0.24454 0.37232 0.48333 -0.03757 -0.02705 0.04864  130 ARG B N   
3212 C CA  . ARG B 130 ? 0.25203 0.36817 0.49425 -0.03655 -0.02285 0.05018  130 ARG B CA  
3213 C C   . ARG B 130 ? 0.24977 0.35991 0.48150 -0.03344 -0.01947 0.04904  130 ARG B C   
3214 O O   . ARG B 130 ? 0.27616 0.39025 0.49993 -0.03358 -0.02062 0.04453  130 ARG B O   
3215 C CB  . ARG B 130 ? 0.25020 0.36067 0.50326 -0.04111 -0.02409 0.04462  130 ARG B CB  
3216 C CG  . ARG B 130 ? 0.22528 0.34260 0.48909 -0.04575 -0.02853 0.04381  130 ARG B CG  
3217 C CD  . ARG B 130 ? 0.23411 0.34532 0.50864 -0.05068 -0.03072 0.03569  130 ARG B CD  
3218 N NE  . ARG B 130 ? 0.25332 0.36673 0.54287 -0.05528 -0.03337 0.03923  130 ARG B NE  
3219 C CZ  . ARG B 130 ? 0.27406 0.38278 0.57721 -0.06059 -0.03630 0.03336  130 ARG B CZ  
3220 N NH1 . ARG B 130 ? 0.29881 0.40080 0.60262 -0.06163 -0.03701 0.02186  130 ARG B NH1 
3221 N NH2 . ARG B 130 ? 0.27352 0.38474 0.59116 -0.06502 -0.03850 0.03897  130 ARG B NH2 
3222 N N   . ASP B 131 ? 0.24865 0.35119 0.48025 -0.03100 -0.01532 0.05325  131 ASP B N   
3223 C CA  . ASP B 131 ? 0.24250 0.33913 0.46571 -0.02875 -0.01209 0.05217  131 ASP B CA  
3224 C C   . ASP B 131 ? 0.26220 0.35285 0.48853 -0.03084 -0.01159 0.04502  131 ASP B C   
3225 O O   . ASP B 131 ? 0.25531 0.33874 0.48422 -0.03015 -0.00866 0.04612  131 ASP B O   
3226 C CB  . ASP B 131 ? 0.23228 0.32449 0.45456 -0.02575 -0.00822 0.05852  131 ASP B CB  
3227 C CG  . ASP B 131 ? 0.23520 0.33259 0.45638 -0.02292 -0.00851 0.06407  131 ASP B CG  
3228 O OD1 . ASP B 131 ? 0.24045 0.34414 0.45832 -0.02240 -0.01126 0.06469  131 ASP B OD1 
3229 O OD2 . ASP B 131 ? 0.23398 0.33029 0.45829 -0.02108 -0.00600 0.06773  131 ASP B OD2 
3230 N N   . ASP B 132 ? 0.26704 0.36193 0.49378 -0.03336 -0.01466 0.03709  132 ASP B N   
3231 C CA  . ASP B 132 ? 0.26129 0.35128 0.49385 -0.03530 -0.01479 0.02794  132 ASP B CA  
3232 C C   . ASP B 132 ? 0.26186 0.35667 0.48491 -0.03474 -0.01435 0.01963  132 ASP B C   
3233 O O   . ASP B 132 ? 0.24444 0.33587 0.47233 -0.03559 -0.01391 0.01028  132 ASP B O   
3234 C CB  . ASP B 132 ? 0.28005 0.37109 0.52504 -0.03969 -0.01893 0.02306  132 ASP B CB  
3235 C CG  . ASP B 132 ? 0.29000 0.39294 0.53032 -0.04218 -0.02314 0.01651  132 ASP B CG  
3236 O OD1 . ASP B 132 ? 0.27023 0.38234 0.50175 -0.04084 -0.02411 0.02214  132 ASP B OD1 
3237 O OD2 . ASP B 132 ? 0.31641 0.42013 0.56306 -0.04561 -0.02572 0.00556  132 ASP B OD2 
3238 N N   . ALA B 133 ? 0.27574 0.37930 0.48649 -0.03327 -0.01439 0.02299  133 ALA B N   
3239 C CA  . ALA B 133 ? 0.27226 0.38518 0.47368 -0.03365 -0.01453 0.01565  133 ALA B CA  
3240 C C   . ALA B 133 ? 0.25513 0.36385 0.45159 -0.03117 -0.00998 0.01468  133 ALA B C   
3241 O O   . ALA B 133 ? 0.26023 0.37498 0.45303 -0.03164 -0.00924 0.00531  133 ALA B O   
3242 C CB  . ALA B 133 ? 0.26996 0.39632 0.46136 -0.03356 -0.01689 0.02165  133 ALA B CB  
3243 N N   . THR B 134 ? 0.25100 0.35099 0.44751 -0.02871 -0.00684 0.02338  134 THR B N   
3244 C CA  . THR B 134 ? 0.24651 0.34432 0.43802 -0.02674 -0.00279 0.02324  134 THR B CA  
3245 C C   . THR B 134 ? 0.22613 0.31779 0.42627 -0.02659 -0.00110 0.01431  134 THR B C   
3246 O O   . THR B 134 ? 0.21546 0.31102 0.41184 -0.02561 0.00124  0.00821  134 THR B O   
3247 C CB  . THR B 134 ? 0.25473 0.34557 0.44475 -0.02474 -0.00022 0.03395  134 THR B CB  
3248 O OG1 . THR B 134 ? 0.28597 0.38167 0.47036 -0.02431 -0.00176 0.04167  134 THR B OG1 
3249 C CG2 . THR B 134 ? 0.22206 0.31206 0.40706 -0.02336 0.00364  0.03409  134 THR B CG2 
3250 N N   . HIS B 135 ? 0.23925 0.32208 0.45222 -0.02742 -0.00220 0.01403  135 HIS B N   
3251 C CA  . HIS B 135 ? 0.24230 0.31819 0.46757 -0.02724 -0.00137 0.00654  135 HIS B CA  
3252 C C   . HIS B 135 ? 0.24661 0.32230 0.48228 -0.03033 -0.00536 -0.00157 135 HIS B C   
3253 O O   . HIS B 135 ? 0.23267 0.30162 0.48029 -0.03202 -0.00721 0.00273  135 HIS B O   
3254 C CB  . HIS B 135 ? 0.20545 0.27152 0.43938 -0.02602 0.00060  0.01503  135 HIS B CB  
3255 C CG  . HIS B 135 ? 0.19188 0.25841 0.41640 -0.02380 0.00407  0.02260  135 HIS B CG  
3256 N ND1 . HIS B 135 ? 0.18635 0.25534 0.40188 -0.02377 0.00418  0.03093  135 HIS B ND1 
3257 C CD2 . HIS B 135 ? 0.17780 0.24271 0.40195 -0.02169 0.00744  0.02276  135 HIS B CD2 
3258 C CE1 . HIS B 135 ? 0.18270 0.25086 0.39276 -0.02221 0.00732  0.03537  135 HIS B CE1 
3259 N NE2 . HIS B 135 ? 0.17222 0.23859 0.38681 -0.02110 0.00929  0.03093  135 HIS B NE2 
3260 N N   . PRO B 136 ? 0.22587 0.31013 0.45785 -0.03160 -0.00680 -0.01355 136 PRO B N   
3261 C CA  . PRO B 136 ? 0.23910 0.32466 0.48043 -0.03538 -0.01113 -0.02241 136 PRO B CA  
3262 C C   . PRO B 136 ? 0.26382 0.33641 0.52595 -0.03638 -0.01193 -0.02668 136 PRO B C   
3263 O O   . PRO B 136 ? 0.27427 0.34583 0.54666 -0.04024 -0.01591 -0.03103 136 PRO B O   
3264 C CB  . PRO B 136 ? 0.23842 0.33730 0.47096 -0.03608 -0.01145 -0.03629 136 PRO B CB  
3265 C CG  . PRO B 136 ? 0.25161 0.35964 0.46667 -0.03363 -0.00866 -0.02890 136 PRO B CG  
3266 C CD  . PRO B 136 ? 0.24261 0.33871 0.46050 -0.03032 -0.00484 -0.01878 136 PRO B CD  
3267 N N   . LEU B 137 ? 0.24394 0.30708 0.51403 -0.03331 -0.00864 -0.02473 137 LEU B N   
3268 C CA  . LEU B 137 ? 0.23251 0.28332 0.52482 -0.03419 -0.00980 -0.02641 137 LEU B CA  
3269 C C   . LEU B 137 ? 0.24920 0.29517 0.55042 -0.03716 -0.01241 -0.01342 137 LEU B C   
3270 O O   . LEU B 137 ? 0.25527 0.29334 0.57581 -0.03977 -0.01495 -0.01447 137 LEU B O   
3271 C CB  . LEU B 137 ? 0.22390 0.26754 0.52309 -0.02982 -0.00580 -0.02501 137 LEU B CB  
3272 C CG  . LEU B 137 ? 0.20740 0.24955 0.50060 -0.02729 -0.00279 -0.00964 137 LEU B CG  
3273 C CD1 . LEU B 137 ? 0.20215 0.23740 0.50855 -0.02920 -0.00449 0.00349  137 LEU B CD1 
3274 C CD2 . LEU B 137 ? 0.20896 0.24927 0.50464 -0.02288 0.00119  -0.01305 137 LEU B CD2 
3275 N N   . MET B 138 ? 0.24554 0.29659 0.53435 -0.03683 -0.01171 -0.00122 138 MET B N   
3276 C CA  . MET B 138 ? 0.24933 0.29984 0.54474 -0.03970 -0.01394 0.00999  138 MET B CA  
3277 C C   . MET B 138 ? 0.26309 0.31700 0.56503 -0.04447 -0.01872 0.00428  138 MET B C   
3278 O O   . MET B 138 ? 0.26194 0.31347 0.57701 -0.04784 -0.02109 0.01100  138 MET B O   
3279 C CB  . MET B 138 ? 0.24041 0.29747 0.52028 -0.03790 -0.01202 0.02075  138 MET B CB  
3280 C CG  . MET B 138 ? 0.27283 0.32811 0.54443 -0.03388 -0.00758 0.02554  138 MET B CG  
3281 S SD  . MET B 138 ? 0.31755 0.38043 0.57013 -0.03182 -0.00572 0.03303  138 MET B SD  
3282 C CE  . MET B 138 ? 0.21352 0.28141 0.47091 -0.03477 -0.00908 0.03872  138 MET B CE  
3283 N N   . HIS B 139 ? 0.28154 0.34306 0.57432 -0.04525 -0.02028 -0.00738 139 HIS B N   
3284 C CA  . HIS B 139 ? 0.29362 0.36040 0.59200 -0.05025 -0.02519 -0.01448 139 HIS B CA  
3285 C C   . HIS B 139 ? 0.31361 0.36989 0.63553 -0.05393 -0.02774 -0.01936 139 HIS B C   
3286 O O   . HIS B 139 ? 0.32582 0.38392 0.65758 -0.05905 -0.03201 -0.01984 139 HIS B O   
3287 C CB  . HIS B 139 ? 0.30358 0.38133 0.58940 -0.05043 -0.02609 -0.02842 139 HIS B CB  
3288 C CG  . HIS B 139 ? 0.32950 0.41727 0.61654 -0.05565 -0.03134 -0.03513 139 HIS B CG  
3289 N ND1 . HIS B 139 ? 0.36571 0.46876 0.63706 -0.05600 -0.03303 -0.03234 139 HIS B ND1 
3290 C CD2 . HIS B 139 ? 0.35061 0.43614 0.65338 -0.06094 -0.03553 -0.04483 139 HIS B CD2 
3291 C CE1 . HIS B 139 ? 0.37350 0.48454 0.64997 -0.06128 -0.03807 -0.03962 139 HIS B CE1 
3292 N NE2 . HIS B 139 ? 0.37718 0.47757 0.67252 -0.06463 -0.03968 -0.04788 139 HIS B NE2 
3293 N N   . TYR B 140 ? 0.29332 0.33859 0.62610 -0.05142 -0.02531 -0.02204 140 TYR B N   
3294 C CA  . TYR B 140 ? 0.29009 0.32373 0.64782 -0.05415 -0.02757 -0.02801 140 TYR B CA  
3295 C C   . TYR B 140 ? 0.28088 0.30444 0.65465 -0.05363 -0.02660 -0.01264 140 TYR B C   
3296 O O   . TYR B 140 ? 0.29173 0.30419 0.68882 -0.05524 -0.02824 -0.01501 140 TYR B O   
3297 C CB  . TYR B 140 ? 0.28117 0.31122 0.64238 -0.05150 -0.02597 -0.04594 140 TYR B CB  
3298 C CG  . TYR B 140 ? 0.29102 0.33478 0.63499 -0.05216 -0.02662 -0.06112 140 TYR B CG  
3299 C CD1 . TYR B 140 ? 0.31046 0.35883 0.66058 -0.05774 -0.03133 -0.07383 140 TYR B CD1 
3300 C CD2 . TYR B 140 ? 0.29448 0.34786 0.61680 -0.04773 -0.02273 -0.06169 140 TYR B CD2 
3301 C CE1 . TYR B 140 ? 0.31898 0.38299 0.65262 -0.05863 -0.03207 -0.08668 140 TYR B CE1 
3302 C CE2 . TYR B 140 ? 0.29813 0.36654 0.60521 -0.04878 -0.02353 -0.07363 140 TYR B CE2 
3303 C CZ  . TYR B 140 ? 0.30429 0.37928 0.61601 -0.05415 -0.02820 -0.08631 140 TYR B CZ  
3304 O OH  . TYR B 140 ? 0.33843 0.43130 0.63438 -0.05545 -0.02913 -0.09745 140 TYR B OH  
3305 N N   . GLN B 141 ? 0.25638 0.28437 0.61954 -0.05170 -0.02422 0.00309  141 GLN B N   
3306 C CA  . GLN B 141 ? 0.27029 0.29304 0.64824 -0.05240 -0.02390 0.01880  141 GLN B CA  
3307 C C   . GLN B 141 ? 0.29278 0.31854 0.68221 -0.05855 -0.02789 0.02695  141 GLN B C   
3308 O O   . GLN B 141 ? 0.30910 0.34519 0.68582 -0.06014 -0.02880 0.02894  141 GLN B O   
3309 C CB  . GLN B 141 ? 0.27963 0.30792 0.64210 -0.04837 -0.01970 0.03109  141 GLN B CB  
3310 C CG  . GLN B 141 ? 0.28043 0.30659 0.63249 -0.04267 -0.01562 0.02516  141 GLN B CG  
3311 C CD  . GLN B 141 ? 0.23557 0.25312 0.60428 -0.04035 -0.01416 0.02983  141 GLN B CD  
3312 O OE1 . GLN B 141 ? 0.21823 0.22826 0.59771 -0.03845 -0.01401 0.01895  141 GLN B OE1 
3313 N NE2 . GLN B 141 ? 0.23066 0.25089 0.60161 -0.04029 -0.01302 0.04584  141 GLN B NE2 
3314 N N   . PRO B 142 ? 0.29517 0.31287 0.70962 -0.06212 -0.03041 0.03245  142 PRO B N   
3315 C CA  . PRO B 142 ? 0.29277 0.31471 0.71938 -0.06864 -0.03419 0.04154  142 PRO B CA  
3316 C C   . PRO B 142 ? 0.29109 0.32413 0.70455 -0.06716 -0.03188 0.05904  142 PRO B C   
3317 O O   . PRO B 142 ? 0.28827 0.32345 0.69357 -0.06309 -0.02810 0.06673  142 PRO B O   
3318 C CB  . PRO B 142 ? 0.28658 0.29535 0.73414 -0.06855 -0.03637 0.04361  142 PRO B CB  
3319 C CG  . PRO B 142 ? 0.26816 0.26593 0.72528 -0.06578 -0.03507 0.02994  142 PRO B CG  
3320 C CD  . PRO B 142 ? 0.27341 0.27774 0.70861 -0.06059 -0.03030 0.02992  142 PRO B CD  
3321 N N   . LEU B 143 ? 0.27550 0.31646 0.68684 -0.07051 -0.03420 0.06435  143 LEU B N   
3322 C CA  . LEU B 143 ? 0.28290 0.33671 0.68073 -0.06919 -0.03193 0.07782  143 LEU B CA  
3323 C C   . LEU B 143 ? 0.29169 0.34512 0.68977 -0.06592 -0.02965 0.09186  143 LEU B C   
3324 O O   . LEU B 143 ? 0.29289 0.35595 0.67706 -0.06319 -0.02622 0.09945  143 LEU B O   
3325 C CB  . LEU B 143 ? 0.28568 0.34739 0.68545 -0.07355 -0.03506 0.08098  143 LEU B CB  
3326 C CG  . LEU B 143 ? 0.28383 0.36059 0.67030 -0.07219 -0.03255 0.09241  143 LEU B CG  
3327 C CD1 . LEU B 143 ? 0.26710 0.35124 0.63841 -0.06888 -0.02935 0.08813  143 LEU B CD1 
3328 C CD2 . LEU B 143 ? 0.26485 0.34973 0.65508 -0.07660 -0.03563 0.09471  143 LEU B CD2 
3329 N N   . GLU B 144 ? 0.28885 0.33239 0.70342 -0.06606 -0.03176 0.09519  144 GLU B N   
3330 C CA  . GLU B 144 ? 0.27464 0.32056 0.69220 -0.06353 -0.03087 0.11025  144 GLU B CA  
3331 C C   . GLU B 144 ? 0.28250 0.32539 0.69636 -0.05871 -0.02757 0.11095  144 GLU B C   
3332 O O   . GLU B 144 ? 0.26755 0.31660 0.67950 -0.05649 -0.02646 0.12371  144 GLU B O   
3333 C CB  . GLU B 144 ? 0.29491 0.33277 0.73453 -0.06531 -0.03502 0.11515  144 GLU B CB  
3334 C CG  . GLU B 144 ? 0.30588 0.32744 0.76319 -0.06378 -0.03634 0.10478  144 GLU B CG  
3335 C CD  . GLU B 144 ? 0.32676 0.33975 0.79619 -0.06810 -0.04004 0.09160  144 GLU B CD  
3336 O OE1 . GLU B 144 ? 0.33491 0.35386 0.79345 -0.07157 -0.04045 0.08436  144 GLU B OE1 
3337 O OE2 . GLU B 144 ? 0.35113 0.35251 0.84168 -0.06804 -0.04271 0.08838  144 GLU B OE2 
3338 N N   . ALA B 145 ? 0.27747 0.31279 0.69028 -0.05739 -0.02609 0.09771  145 ALA B N   
3339 C CA  . ALA B 145 ? 0.24549 0.27799 0.65595 -0.05310 -0.02285 0.09774  145 ALA B CA  
3340 C C   . ALA B 145 ? 0.23278 0.27811 0.62266 -0.05114 -0.01904 0.10494  145 ALA B C   
3341 O O   . ALA B 145 ? 0.24058 0.29497 0.61741 -0.05264 -0.01828 0.10424  145 ALA B O   
3342 C CB  . ALA B 145 ? 0.22738 0.25100 0.64102 -0.05283 -0.02197 0.08082  145 ALA B CB  
3343 N N   . PRO B 146 ? 0.24235 0.28926 0.63005 -0.04770 -0.01672 0.11148  146 PRO B N   
3344 C CA  . PRO B 146 ? 0.24221 0.30072 0.61050 -0.04597 -0.01301 0.11579  146 PRO B CA  
3345 C C   . PRO B 146 ? 0.22584 0.28569 0.58166 -0.04612 -0.01065 0.10465  146 PRO B C   
3346 O O   . PRO B 146 ? 0.23281 0.28419 0.59155 -0.04527 -0.01037 0.09350  146 PRO B O   
3347 C CB  . PRO B 146 ? 0.22854 0.28510 0.60049 -0.04257 -0.01140 0.12021  146 PRO B CB  
3348 C CG  . PRO B 146 ? 0.23589 0.28429 0.62958 -0.04232 -0.01484 0.12500  146 PRO B CG  
3349 C CD  . PRO B 146 ? 0.25192 0.29053 0.65622 -0.04513 -0.01753 0.11472  146 PRO B CD  
3350 N N   . PRO B 147 ? 0.21791 0.28868 0.55905 -0.04644 -0.00909 0.10658  147 PRO B N   
3351 C CA  . PRO B 147 ? 0.20194 0.27382 0.52983 -0.04514 -0.00731 0.09681  147 PRO B CA  
3352 C C   . PRO B 147 ? 0.20432 0.27307 0.51969 -0.04073 -0.00403 0.09257  147 PRO B C   
3353 O O   . PRO B 147 ? 0.19788 0.27095 0.51344 -0.04006 -0.00208 0.09995  147 PRO B O   
3354 C CB  . PRO B 147 ? 0.19416 0.27940 0.51378 -0.04618 -0.00625 0.10204  147 PRO B CB  
3355 C CG  . PRO B 147 ? 0.21097 0.30263 0.53070 -0.04632 -0.00619 0.11320  147 PRO B CG  
3356 C CD  . PRO B 147 ? 0.22161 0.30391 0.55707 -0.04734 -0.00929 0.11663  147 PRO B CD  
3357 N N   . VAL B 148 ? 0.19678 0.25965 0.50147 -0.03817 -0.00362 0.08108  148 VAL B N   
3358 C CA  . VAL B 148 ? 0.18975 0.24962 0.48335 -0.03442 -0.00071 0.07644  148 VAL B CA  
3359 C C   . VAL B 148 ? 0.16753 0.23165 0.44278 -0.03246 0.00129  0.07345  148 VAL B C   
3360 O O   . VAL B 148 ? 0.17303 0.23575 0.43875 -0.02994 0.00376  0.07087  148 VAL B O   
3361 C CB  . VAL B 148 ? 0.19229 0.24296 0.49015 -0.03286 -0.00140 0.06599  148 VAL B CB  
3362 C CG1 . VAL B 148 ? 0.19909 0.24379 0.51715 -0.03344 -0.00256 0.06923  148 VAL B CG1 
3363 C CG2 . VAL B 148 ? 0.19674 0.24618 0.49256 -0.03418 -0.00400 0.05655  148 VAL B CG2 
3364 N N   . SER B 149 ? 0.17666 0.24616 0.44819 -0.03351 0.00028  0.07435  149 SER B N   
3365 C CA  . SER B 149 ? 0.17242 0.24457 0.42958 -0.03127 0.00161  0.07128  149 SER B CA  
3366 C C   . SER B 149 ? 0.17075 0.25164 0.42741 -0.03190 0.00183  0.07641  149 SER B C   
3367 O O   . SER B 149 ? 0.18889 0.27397 0.45495 -0.03454 -0.00026 0.07973  149 SER B O   
3368 C CB  . SER B 149 ? 0.16656 0.23590 0.41938 -0.03080 -0.00053 0.06313  149 SER B CB  
3369 O OG  . SER B 149 ? 0.18229 0.25491 0.42358 -0.02872 0.00024  0.06252  149 SER B OG  
3370 N N   . LEU B 150 ? 0.18080 0.26473 0.42758 -0.02950 0.00441  0.07656  150 LEU B N   
3371 C CA  . LEU B 150 ? 0.18495 0.27773 0.43111 -0.02905 0.00530  0.07939  150 LEU B CA  
3372 C C   . LEU B 150 ? 0.18124 0.27245 0.41780 -0.02558 0.00651  0.07563  150 LEU B C   
3373 O O   . LEU B 150 ? 0.17767 0.26431 0.40728 -0.02401 0.00854  0.07378  150 LEU B O   
3374 C CB  . LEU B 150 ? 0.18278 0.28391 0.43099 -0.03013 0.00788  0.08479  150 LEU B CB  
3375 C CG  . LEU B 150 ? 0.18646 0.29917 0.43391 -0.02934 0.00969  0.08611  150 LEU B CG  
3376 C CD1 . LEU B 150 ? 0.16996 0.29013 0.42636 -0.03138 0.00746  0.08960  150 LEU B CD1 
3377 C CD2 . LEU B 150 ? 0.17460 0.29695 0.42115 -0.03043 0.01263  0.08944  150 LEU B CD2 
3378 N N   . SER B 151 ? 0.17575 0.27117 0.41342 -0.02448 0.00513  0.07532  151 SER B N   
3379 C CA  . SER B 151 ? 0.19166 0.28572 0.42333 -0.02089 0.00566  0.07325  151 SER B CA  
3380 C C   . SER B 151 ? 0.18756 0.28788 0.42023 -0.01870 0.00866  0.07393  151 SER B C   
3381 O O   . SER B 151 ? 0.18477 0.29467 0.42349 -0.01960 0.00903  0.07608  151 SER B O   
3382 C CB  . SER B 151 ? 0.18496 0.28132 0.41839 -0.02054 0.00212  0.07280  151 SER B CB  
3383 O OG  . SER B 151 ? 0.19862 0.29075 0.43061 -0.02267 -0.00053 0.07010  151 SER B OG  
3384 N N   . VAL B 152 ? 0.19188 0.28756 0.41947 -0.01603 0.01084  0.07168  152 VAL B N   
3385 C CA  . VAL B 152 ? 0.19712 0.29758 0.42609 -0.01371 0.01403  0.06975  152 VAL B CA  
3386 C C   . VAL B 152 ? 0.20154 0.29671 0.43048 -0.00955 0.01379  0.06830  152 VAL B C   
3387 O O   . VAL B 152 ? 0.19143 0.27756 0.41581 -0.00904 0.01359  0.06802  152 VAL B O   
3388 C CB  . VAL B 152 ? 0.18599 0.28582 0.41112 -0.01516 0.01704  0.06787  152 VAL B CB  
3389 C CG1 . VAL B 152 ? 0.18921 0.29629 0.41639 -0.01322 0.02035  0.06386  152 VAL B CG1 
3390 C CG2 . VAL B 152 ? 0.17268 0.27700 0.39880 -0.01919 0.01669  0.07136  152 VAL B CG2 
3391 N N   . ILE B 153 ? 0.20525 0.30680 0.44046 -0.00655 0.01378  0.06820  153 ILE B N   
3392 C CA  . ILE B 153 ? 0.21369 0.31119 0.45186 -0.00229 0.01254  0.06894  153 ILE B CA  
3393 C C   . ILE B 153 ? 0.21962 0.31826 0.46351 0.00175  0.01602  0.06448  153 ILE B C   
3394 O O   . ILE B 153 ? 0.21962 0.32892 0.46831 0.00263  0.01824  0.06174  153 ILE B O   
3395 C CB  . ILE B 153 ? 0.20092 0.30511 0.44356 -0.00165 0.00900  0.07265  153 ILE B CB  
3396 C CG1 . ILE B 153 ? 0.20568 0.30834 0.44312 -0.00612 0.00568  0.07463  153 ILE B CG1 
3397 C CG2 . ILE B 153 ? 0.20411 0.30588 0.45090 0.00290  0.00729  0.07520  153 ILE B CG2 
3398 C CD1 . ILE B 153 ? 0.17894 0.28783 0.41952 -0.00653 0.00141  0.07743  153 ILE B CD1 
3399 N N   . PHE B 154 ? 0.21096 0.29933 0.45513 0.00396  0.01659  0.06344  154 PHE B N   
3400 C CA  . PHE B 154 ? 0.21402 0.30036 0.46484 0.00756  0.01988  0.05747  154 PHE B CA  
3401 C C   . PHE B 154 ? 0.22098 0.30333 0.48182 0.01315  0.01838  0.06005  154 PHE B C   
3402 O O   . PHE B 154 ? 0.23279 0.30511 0.49363 0.01365  0.01626  0.06481  154 PHE B O   
3403 C CB  . PHE B 154 ? 0.21071 0.28740 0.45683 0.00526  0.02160  0.05421  154 PHE B CB  
3404 C CG  . PHE B 154 ? 0.20974 0.29105 0.44733 0.00014  0.02305  0.05228  154 PHE B CG  
3405 C CD1 . PHE B 154 ? 0.20897 0.30079 0.44732 -0.00072 0.02630  0.04625  154 PHE B CD1 
3406 C CD2 . PHE B 154 ? 0.20548 0.28190 0.43498 -0.00365 0.02124  0.05664  154 PHE B CD2 
3407 C CE1 . PHE B 154 ? 0.20581 0.30330 0.43730 -0.00546 0.02720  0.04631  154 PHE B CE1 
3408 C CE2 . PHE B 154 ? 0.18952 0.27009 0.41332 -0.00776 0.02237  0.05584  154 PHE B CE2 
3409 C CZ  . PHE B 154 ? 0.19466 0.28567 0.41958 -0.00877 0.02512  0.05148  154 PHE B CZ  
3410 N N   . PRO B 155 ? 0.23568 0.32656 0.50621 0.01754  0.01939  0.05790  155 PRO B N   
3411 C CA  . PRO B 155 ? 0.25905 0.34567 0.54204 0.02378  0.01829  0.06021  155 PRO B CA  
3412 C C   . PRO B 155 ? 0.23969 0.31467 0.52946 0.02626  0.02091  0.05436  155 PRO B C   
3413 O O   . PRO B 155 ? 0.24313 0.32115 0.53544 0.02687  0.02508  0.04413  155 PRO B O   
3414 C CB  . PRO B 155 ? 0.25022 0.35110 0.54211 0.02769  0.01967  0.05753  155 PRO B CB  
3415 C CG  . PRO B 155 ? 0.23386 0.34517 0.51908 0.02377  0.02310  0.05105  155 PRO B CG  
3416 C CD  . PRO B 155 ? 0.22658 0.33284 0.49825 0.01702  0.02139  0.05455  155 PRO B CD  
3417 N N   . LEU B 156 ? 0.24479 0.30749 0.53792 0.02718  0.01839  0.06076  156 LEU B N   
3418 C CA  . LEU B 156 ? 0.26655 0.31604 0.56905 0.02917  0.02020  0.05642  156 LEU B CA  
3419 C C   . LEU B 156 ? 0.28109 0.32830 0.60325 0.03708  0.02009  0.05673  156 LEU B C   
3420 O O   . LEU B 156 ? 0.29126 0.32868 0.62506 0.03969  0.02235  0.04994  156 LEU B O   
3421 C CB  . LEU B 156 ? 0.25547 0.29311 0.55191 0.02493  0.01796  0.06340  156 LEU B CB  
3422 C CG  . LEU B 156 ? 0.25100 0.28877 0.53201 0.01808  0.01941  0.05970  156 LEU B CG  
3423 C CD1 . LEU B 156 ? 0.24911 0.27392 0.53111 0.01531  0.01964  0.06014  156 LEU B CD1 
3424 C CD2 . LEU B 156 ? 0.23342 0.28052 0.51102 0.01704  0.02331  0.04841  156 LEU B CD2 
3425 N N   . THR B 157 ? 0.26494 0.32023 0.59177 0.04056  0.01722  0.06462  157 THR B N   
3426 C CA  . THR B 157 ? 0.25018 0.30707 0.59651 0.04874  0.01738  0.06464  157 THR B CA  
3427 C C   . THR B 157 ? 0.26597 0.34093 0.61088 0.05028  0.01760  0.06384  157 THR B C   
3428 O O   . THR B 157 ? 0.26442 0.34810 0.59438 0.04471  0.01663  0.06554  157 THR B O   
3429 C CB  . THR B 157 ? 0.25323 0.30241 0.60993 0.05169  0.01257  0.07883  157 THR B CB  
3430 O OG1 . THR B 157 ? 0.29049 0.34898 0.63580 0.04832  0.00795  0.09038  157 THR B OG1 
3431 C CG2 . THR B 157 ? 0.25692 0.28946 0.61419 0.04873  0.01208  0.08148  157 THR B CG2 
3432 N N   . GLU B 158 ? 0.27262 0.35353 0.63447 0.05782  0.01896  0.06105  158 GLU B N   
3433 C CA  . GLU B 158 ? 0.25914 0.35880 0.62102 0.05916  0.01943  0.06031  158 GLU B CA  
3434 C C   . GLU B 158 ? 0.26413 0.37075 0.61629 0.05507  0.01381  0.07313  158 GLU B C   
3435 O O   . GLU B 158 ? 0.25970 0.36042 0.61392 0.05553  0.00917  0.08421  158 GLU B O   
3436 C CB  . GLU B 158 ? 0.25718 0.36219 0.64104 0.06878  0.02109  0.05745  158 GLU B CB  
3437 C CG  . GLU B 158 ? 0.28184 0.37687 0.68106 0.07424  0.01681  0.06884  158 GLU B CG  
3438 C CD  . GLU B 158 ? 0.28182 0.38305 0.70488 0.08447  0.01806  0.06725  158 GLU B CD  
3439 O OE1 . GLU B 158 ? 0.29377 0.40746 0.72131 0.08756  0.02286  0.05567  158 GLU B OE1 
3440 O OE2 . GLU B 158 ? 0.28544 0.38045 0.72353 0.08953  0.01423  0.07823  158 GLU B OE2 
3441 N N   . PHE B 159 ? 0.27569 0.39555 0.61718 0.05035  0.01415  0.07145  159 PHE B N   
3442 C CA  . PHE B 159 ? 0.25264 0.38208 0.58770 0.04667  0.00915  0.08082  159 PHE B CA  
3443 C C   . PHE B 159 ? 0.25556 0.40100 0.60381 0.05179  0.00890  0.08219  159 PHE B C   
3444 O O   . PHE B 159 ? 0.24679 0.40279 0.59912 0.05330  0.01323  0.07432  159 PHE B O   
3445 C CB  . PHE B 159 ? 0.24221 0.37582 0.56087 0.03830  0.00930  0.07864  159 PHE B CB  
3446 C CG  . PHE B 159 ? 0.24478 0.36544 0.54988 0.03278  0.00801  0.08014  159 PHE B CG  
3447 C CD1 . PHE B 159 ? 0.24974 0.35636 0.55664 0.03473  0.00766  0.08222  159 PHE B CD1 
3448 C CD2 . PHE B 159 ? 0.23895 0.36193 0.53092 0.02559  0.00710  0.07988  159 PHE B CD2 
3449 C CE1 . PHE B 159 ? 0.25104 0.34782 0.54565 0.02953  0.00674  0.08375  159 PHE B CE1 
3450 C CE2 . PHE B 159 ? 0.23683 0.34908 0.51727 0.02106  0.00628  0.08065  159 PHE B CE2 
3451 C CZ  . PHE B 159 ? 0.23745 0.33744 0.51865 0.02300  0.00621  0.08254  159 PHE B CZ  
3452 N N   . THR B 160 ? 0.27971 0.42900 0.63498 0.05442  0.00389  0.09247  160 THR B N   
3453 C CA  . THR B 160 ? 0.28645 0.45206 0.65524 0.05937  0.00308  0.09500  160 THR B CA  
3454 C C   . THR B 160 ? 0.29359 0.46994 0.65693 0.05483  -0.00345 0.10518  160 THR B C   
3455 O O   . THR B 160 ? 0.29728 0.46745 0.64886 0.04954  -0.00746 0.11062  160 THR B O   
3456 C CB  . THR B 160 ? 0.29750 0.45950 0.68728 0.06959  0.00360  0.09716  160 THR B CB  
3457 O OG1 . THR B 160 ? 0.29887 0.45328 0.69018 0.07001  -0.00202 0.10954  160 THR B OG1 
3458 C CG2 . THR B 160 ? 0.27093 0.42044 0.66718 0.07376  0.00977  0.08544  160 THR B CG2 
3459 N N   . GLU B 161 ? 0.28825 0.48232 0.66070 0.05682  -0.00443 0.10704  161 GLU B N   
3460 C CA  . GLU B 161 ? 0.31206 0.51835 0.68324 0.05354  -0.01117 0.11676  161 GLU B CA  
3461 C C   . GLU B 161 ? 0.31487 0.51581 0.68980 0.05651  -0.01614 0.12745  161 GLU B C   
3462 O O   . GLU B 161 ? 0.34322 0.54781 0.70839 0.05092  -0.02179 0.13430  161 GLU B O   
3463 C CB  . GLU B 161 ? 0.35095 0.57750 0.73597 0.05708  -0.01117 0.11782  161 GLU B CB  
3464 C CG  . GLU B 161 ? 0.38600 0.62780 0.77341 0.05474  -0.01851 0.12814  161 GLU B CG  
3465 C CD  . GLU B 161 ? 0.43765 0.69778 0.83957 0.05955  -0.01821 0.12941  161 GLU B CD  
3466 O OE1 . GLU B 161 ? 0.42251 0.68652 0.83000 0.06271  -0.01213 0.12121  161 GLU B OE1 
3467 O OE2 . GLU B 161 ? 0.50816 0.77774 0.91180 0.05941  -0.02380 0.13743  161 GLU B OE2 
3468 N N   . GLU B 162 ? 0.32726 0.51981 0.71677 0.06504  -0.01404 0.12878  162 GLU B N   
3469 C CA  . GLU B 162 ? 0.33816 0.52792 0.73643 0.06909  -0.01884 0.14142  162 GLU B CA  
3470 C C   . GLU B 162 ? 0.34077 0.51473 0.72659 0.06466  -0.02013 0.14464  162 GLU B C   
3471 O O   . GLU B 162 ? 0.37166 0.54827 0.75733 0.06395  -0.02562 0.15710  162 GLU B O   
3472 C CB  . GLU B 162 ? 0.34790 0.53370 0.76974 0.08023  -0.01604 0.14161  162 GLU B CB  
3473 C CG  . GLU B 162 ? 0.36003 0.55868 0.79055 0.08457  -0.01272 0.13439  162 GLU B CG  
3474 C CD  . GLU B 162 ? 0.33944 0.53729 0.77090 0.08534  -0.00516 0.11920  162 GLU B CD  
3475 O OE1 . GLU B 162 ? 0.34776 0.53247 0.78793 0.09072  -0.00029 0.11130  162 GLU B OE1 
3476 O OE2 . GLU B 162 ? 0.35081 0.56095 0.77263 0.07961  -0.00413 0.11472  162 GLU B OE2 
3477 N N   . ASN B 163 ? 0.37764 0.53715 0.75339 0.06157  -0.01524 0.13436  163 ASN B N   
3478 C CA  . ASN B 163 ? 0.37542 0.52029 0.74030 0.05749  -0.01587 0.13687  163 ASN B CA  
3479 C C   . ASN B 163 ? 0.36782 0.51359 0.71035 0.04783  -0.01658 0.13284  163 ASN B C   
3480 O O   . ASN B 163 ? 0.36746 0.50171 0.69953 0.04400  -0.01593 0.13236  163 ASN B O   
3481 C CB  . ASN B 163 ? 0.34066 0.46750 0.71278 0.06133  -0.01034 0.12914  163 ASN B CB  
3482 C CG  . ASN B 163 ? 0.31406 0.43735 0.67634 0.05798  -0.00451 0.11418  163 ASN B CG  
3483 O OD1 . ASN B 163 ? 0.30713 0.44135 0.65997 0.05371  -0.00408 0.10981  163 ASN B OD1 
3484 N ND2 . ASN B 163 ? 0.27728 0.38581 0.64281 0.05961  -0.00017 0.10671  163 ASN B ND2 
3485 N N   . GLY B 164 ? 0.35812 0.51723 0.69469 0.04388  -0.01787 0.12989  164 GLY B N   
3486 C CA  . GLY B 164 ? 0.35074 0.51180 0.66938 0.03509  -0.01966 0.12720  164 GLY B CA  
3487 C C   . GLY B 164 ? 0.31823 0.47326 0.62793 0.03086  -0.01494 0.11598  164 GLY B C   
3488 O O   . GLY B 164 ? 0.30112 0.45132 0.59695 0.02458  -0.01547 0.11352  164 GLY B O   
3489 N N   . ALA B 165 ? 0.29020 0.44705 0.60801 0.03419  -0.01036 0.10943  165 ALA B N   
3490 C CA  . ALA B 165 ? 0.25800 0.41283 0.56850 0.03007  -0.00608 0.10038  165 ALA B CA  
3491 C C   . ALA B 165 ? 0.25132 0.41022 0.54992 0.02176  -0.00908 0.10027  165 ALA B C   
3492 O O   . ALA B 165 ? 0.23354 0.40340 0.53327 0.01951  -0.01370 0.10453  165 ALA B O   
3493 C CB  . ALA B 165 ? 0.25285 0.41866 0.57440 0.03385  -0.00229 0.09564  165 ALA B CB  
3494 N N   . THR B 166 ? 0.23814 0.38818 0.52641 0.01720  -0.00658 0.09507  166 THR B N   
3495 C CA  . THR B 166 ? 0.22685 0.37775 0.50541 0.00971  -0.00914 0.09410  166 THR B CA  
3496 C C   . THR B 166 ? 0.20830 0.37292 0.49238 0.00667  -0.01077 0.09418  166 THR B C   
3497 O O   . THR B 166 ? 0.20507 0.37695 0.49663 0.00857  -0.00759 0.09257  166 THR B O   
3498 C CB  . THR B 166 ? 0.21310 0.35349 0.48303 0.00631  -0.00554 0.08881  166 THR B CB  
3499 O OG1 . THR B 166 ? 0.22234 0.35134 0.49027 0.00978  -0.00286 0.08796  166 THR B OG1 
3500 C CG2 . THR B 166 ? 0.20349 0.34081 0.46401 -0.00004 -0.00854 0.08811  166 THR B CG2 
3501 N N   . GLU B 167 ? 0.20440 0.37370 0.48514 0.00156  -0.01573 0.09569  167 GLU B N   
3502 C CA  . GLU B 167 ? 0.19952 0.38132 0.48614 -0.00267 -0.01834 0.09609  167 GLU B CA  
3503 C C   . GLU B 167 ? 0.20836 0.38490 0.48983 -0.00995 -0.01846 0.09203  167 GLU B C   
3504 O O   . GLU B 167 ? 0.22107 0.38948 0.49406 -0.01301 -0.02027 0.08956  167 GLU B O   
3505 C CB  . GLU B 167 ? 0.19794 0.39026 0.48675 -0.00344 -0.02447 0.10017  167 GLU B CB  
3506 C CG  . GLU B 167 ? 0.20549 0.40387 0.50219 0.00428  -0.02480 0.10605  167 GLU B CG  
3507 C CD  . GLU B 167 ? 0.20929 0.41677 0.50540 0.00387  -0.03108 0.11171  167 GLU B CD  
3508 O OE1 . GLU B 167 ? 0.21954 0.43583 0.51335 -0.00242 -0.03569 0.11053  167 GLU B OE1 
3509 O OE2 . GLU B 167 ? 0.23336 0.43990 0.53208 0.00964  -0.03160 0.11757  167 GLU B OE2 
3510 N N   . VAL B 168 ? 0.19741 0.37943 0.48504 -0.01254 -0.01642 0.09175  168 VAL B N   
3511 C CA  . VAL B 168 ? 0.18019 0.35737 0.46644 -0.01910 -0.01634 0.08962  168 VAL B CA  
3512 C C   . VAL B 168 ? 0.19272 0.38155 0.48872 -0.02468 -0.01981 0.09169  168 VAL B C   
3513 O O   . VAL B 168 ? 0.19977 0.40192 0.50438 -0.02319 -0.01897 0.09514  168 VAL B O   
3514 C CB  . VAL B 168 ? 0.17995 0.35376 0.46541 -0.01805 -0.01066 0.08916  168 VAL B CB  
3515 C CG1 . VAL B 168 ? 0.20465 0.37353 0.49034 -0.02457 -0.01104 0.08887  168 VAL B CG1 
3516 C CG2 . VAL B 168 ? 0.18507 0.34818 0.46241 -0.01276 -0.00729 0.08669  168 VAL B CG2 
3517 N N   . ILE B 169 ? 0.19154 0.37581 0.48731 -0.03114 -0.02363 0.08909  169 ILE B N   
3518 C CA  . ILE B 169 ? 0.18775 0.38092 0.49421 -0.03776 -0.02738 0.09047  169 ILE B CA  
3519 C C   . ILE B 169 ? 0.20139 0.39137 0.51348 -0.04184 -0.02477 0.09270  169 ILE B C   
3520 O O   . ILE B 169 ? 0.19282 0.37051 0.50262 -0.04482 -0.02492 0.08980  169 ILE B O   
3521 C CB  . ILE B 169 ? 0.19814 0.38876 0.50324 -0.04281 -0.03326 0.08522  169 ILE B CB  
3522 C CG1 . ILE B 169 ? 0.21514 0.41151 0.51362 -0.03880 -0.03589 0.08468  169 ILE B CG1 
3523 C CG2 . ILE B 169 ? 0.18323 0.38225 0.50118 -0.05033 -0.03738 0.08602  169 ILE B CG2 
3524 C CD1 . ILE B 169 ? 0.19820 0.39624 0.49400 -0.04389 -0.04167 0.07877  169 ILE B CD1 
3525 N N   . LEU B 170 ? 0.20295 0.40565 0.52327 -0.04188 -0.02237 0.09846  170 LEU B N   
3526 C CA  . LEU B 170 ? 0.20272 0.40603 0.52792 -0.04518 -0.01935 0.10278  170 LEU B CA  
3527 C C   . LEU B 170 ? 0.19400 0.39250 0.52677 -0.05334 -0.02348 0.10373  170 LEU B C   
3528 O O   . LEU B 170 ? 0.20660 0.41020 0.54543 -0.05719 -0.02789 0.10320  170 LEU B O   
3529 C CB  . LEU B 170 ? 0.19431 0.41290 0.52130 -0.04250 -0.01533 0.10729  170 LEU B CB  
3530 C CG  . LEU B 170 ? 0.19189 0.41751 0.51624 -0.03420 -0.01084 0.10577  170 LEU B CG  
3531 C CD1 . LEU B 170 ? 0.21825 0.45753 0.54235 -0.03222 -0.00600 0.10795  170 LEU B CD1 
3532 C CD2 . LEU B 170 ? 0.19614 0.40578 0.50831 -0.03017 -0.00810 0.10092  170 LEU B CD2 
3533 N N   . GLY B 171 ? 0.19451 0.38178 0.52607 -0.05557 -0.02212 0.10457  171 GLY B N   
3534 C CA  . GLY B 171 ? 0.19209 0.37062 0.53086 -0.06216 -0.02578 0.10477  171 GLY B CA  
3535 C C   . GLY B 171 ? 0.19667 0.36496 0.54005 -0.06537 -0.03039 0.09685  171 GLY B C   
3536 O O   . GLY B 171 ? 0.20938 0.36989 0.56098 -0.07085 -0.03374 0.09521  171 GLY B O   
3537 N N   . SER B 172 ? 0.20231 0.36760 0.53563 -0.06095 -0.03031 0.09030  172 SER B N   
3538 C CA  . SER B 172 ? 0.19754 0.35383 0.52784 -0.06278 -0.03432 0.08042  172 SER B CA  
3539 C C   . SER B 172 ? 0.22077 0.36080 0.54928 -0.06296 -0.03318 0.07551  172 SER B C   
3540 O O   . SER B 172 ? 0.23447 0.36770 0.56066 -0.06433 -0.03593 0.06593  172 SER B O   
3541 C CB  . SER B 172 ? 0.18108 0.34150 0.49783 -0.05757 -0.03477 0.07605  172 SER B CB  
3542 O OG  . SER B 172 ? 0.20410 0.36099 0.50936 -0.05064 -0.02983 0.07796  172 SER B OG  
3543 N N   . HIS B 173 ? 0.21541 0.35075 0.54518 -0.06159 -0.02921 0.08145  173 HIS B N   
3544 C CA  . HIS B 173 ? 0.22305 0.34405 0.55582 -0.06256 -0.02881 0.07800  173 HIS B CA  
3545 C C   . HIS B 173 ? 0.23753 0.35375 0.58922 -0.06968 -0.03297 0.07749  173 HIS B C   
3546 O O   . HIS B 173 ? 0.24639 0.34993 0.60381 -0.07057 -0.03339 0.07293  173 HIS B O   
3547 C CB  . HIS B 173 ? 0.21493 0.33424 0.54507 -0.05961 -0.02395 0.08556  173 HIS B CB  
3548 C CG  . HIS B 173 ? 0.22143 0.35219 0.55733 -0.06116 -0.02246 0.09664  173 HIS B CG  
3549 N ND1 . HIS B 173 ? 0.22629 0.37081 0.55665 -0.05871 -0.02070 0.09978  173 HIS B ND1 
3550 C CD2 . HIS B 173 ? 0.22414 0.35262 0.56399 -0.06294 -0.02218 0.10389  173 HIS B CD2 
3551 C CE1 . HIS B 173 ? 0.22595 0.37708 0.55620 -0.05938 -0.01911 0.10754  173 HIS B CE1 
3552 N NE2 . HIS B 173 ? 0.22476 0.36681 0.56041 -0.06211 -0.02018 0.11087  173 HIS B NE2 
3553 N N   . ARG B 174 ? 0.23699 0.36228 0.59835 -0.07433 -0.03595 0.08161  174 ARG B N   
3554 C CA  . ARG B 174 ? 0.22277 0.34034 0.59712 -0.07997 -0.03986 0.07969  174 ARG B CA  
3555 C C   . ARG B 174 ? 0.23680 0.35314 0.61813 -0.08455 -0.04516 0.06665  174 ARG B C   
3556 O O   . ARG B 174 ? 0.25460 0.36223 0.64796 -0.08929 -0.04851 0.06197  174 ARG B O   
3557 C CB  . ARG B 174 ? 0.23226 0.35861 0.60947 -0.08218 -0.04025 0.08962  174 ARG B CB  
3558 C CG  . ARG B 174 ? 0.23972 0.36530 0.61462 -0.07968 -0.03640 0.10141  174 ARG B CG  
3559 C CD  . ARG B 174 ? 0.28628 0.42181 0.66552 -0.08267 -0.03723 0.11074  174 ARG B CD  
3560 N NE  . ARG B 174 ? 0.28649 0.43891 0.65687 -0.08042 -0.03521 0.11287  174 ARG B NE  
3561 C CZ  . ARG B 174 ? 0.29182 0.45463 0.65333 -0.07646 -0.03059 0.12015  174 ARG B CZ  
3562 N NH1 . ARG B 174 ? 0.29354 0.45366 0.65305 -0.07512 -0.02797 0.12723  174 ARG B NH1 
3563 N NH2 . ARG B 174 ? 0.29436 0.47158 0.64947 -0.07363 -0.02870 0.11989  174 ARG B NH2 
3564 N N   . TRP B 175 ? 0.25016 0.37258 0.61695 -0.08121 -0.04538 0.05938  175 TRP B N   
3565 C CA  . TRP B 175 ? 0.27508 0.39673 0.64046 -0.08394 -0.04978 0.04525  175 TRP B CA  
3566 C C   . TRP B 175 ? 0.30291 0.41043 0.66489 -0.08180 -0.04848 0.03427  175 TRP B C   
3567 O O   . TRP B 175 ? 0.30324 0.40599 0.65303 -0.07564 -0.04392 0.03590  175 TRP B O   
3568 C CB  . TRP B 175 ? 0.26995 0.40483 0.61874 -0.08058 -0.05051 0.04270  175 TRP B CB  
3569 C CG  . TRP B 175 ? 0.22702 0.37674 0.57567 -0.07976 -0.05041 0.05338  175 TRP B CG  
3570 C CD1 . TRP B 175 ? 0.20564 0.36093 0.56736 -0.08283 -0.05014 0.06400  175 TRP B CD1 
3571 C CD2 . TRP B 175 ? 0.22930 0.39154 0.56501 -0.07526 -0.05043 0.05476  175 TRP B CD2 
3572 N NE1 . TRP B 175 ? 0.19821 0.36908 0.55556 -0.08013 -0.04963 0.07059  175 TRP B NE1 
3573 C CE2 . TRP B 175 ? 0.20392 0.37839 0.54616 -0.07527 -0.04996 0.06520  175 TRP B CE2 
3574 C CE3 . TRP B 175 ? 0.23758 0.40288 0.55780 -0.07118 -0.05082 0.04896  175 TRP B CE3 
3575 C CZ2 . TRP B 175 ? 0.21797 0.40605 0.55297 -0.07070 -0.04983 0.06926  175 TRP B CZ2 
3576 C CZ3 . TRP B 175 ? 0.21505 0.39379 0.52831 -0.06718 -0.05113 0.05448  175 TRP B CZ3 
3577 C CH2 . TRP B 175 ? 0.20397 0.39317 0.52512 -0.06662 -0.05061 0.06415  175 TRP B CH2 
3578 N N   . THR B 176 ? 0.31477 0.41647 0.68814 -0.08699 -0.05252 0.02211  176 THR B N   
3579 C CA  . THR B 176 ? 0.33896 0.42965 0.70954 -0.08479 -0.05137 0.00890  176 THR B CA  
3580 C C   . THR B 176 ? 0.35147 0.45039 0.69873 -0.07981 -0.04984 0.00174  176 THR B C   
3581 O O   . THR B 176 ? 0.33398 0.42706 0.67095 -0.07438 -0.04574 -0.00041 176 THR B O   
3582 C CB  . THR B 176 ? 0.33208 0.41648 0.72099 -0.09162 -0.05624 -0.00479 176 THR B CB  
3583 O OG1 . THR B 176 ? 0.35533 0.45185 0.73540 -0.09429 -0.06005 -0.01756 176 THR B OG1 
3584 C CG2 . THR B 176 ? 0.33411 0.41649 0.74603 -0.09852 -0.05955 0.00437  176 THR B CG2 
3585 N N   . GLU B 177 ? 0.35244 0.46631 0.69192 -0.08180 -0.05327 -0.00073 177 GLU B N   
3586 C CA  . GLU B 177 ? 0.33563 0.46053 0.65473 -0.07812 -0.05288 -0.00559 177 GLU B CA  
3587 C C   . GLU B 177 ? 0.32780 0.46524 0.63743 -0.07516 -0.05253 0.00739  177 GLU B C   
3588 O O   . GLU B 177 ? 0.33244 0.47364 0.65163 -0.07728 -0.05372 0.01664  177 GLU B O   
3589 C CB  . GLU B 177 ? 0.34316 0.47772 0.66179 -0.08328 -0.05797 -0.02159 177 GLU B CB  
3590 C CG  . GLU B 177 ? 0.37275 0.52323 0.69474 -0.08838 -0.06348 -0.01884 177 GLU B CG  
3591 C CD  . GLU B 177 ? 0.39888 0.56369 0.71702 -0.09352 -0.06881 -0.03432 177 GLU B CD  
3592 O OE1 . GLU B 177 ? 0.40877 0.58193 0.71048 -0.09063 -0.06788 -0.04102 177 GLU B OE1 
3593 O OE2 . GLU B 177 ? 0.36944 0.53888 0.70122 -0.10094 -0.07408 -0.03939 177 GLU B OE2 
3594 N N   . VAL B 178 ? 0.33119 0.47577 0.62306 -0.07016 -0.05084 0.00813  178 VAL B N   
3595 C CA  . VAL B 178 ? 0.29278 0.44940 0.57691 -0.06676 -0.05089 0.01926  178 VAL B CA  
3596 C C   . VAL B 178 ? 0.31506 0.48858 0.60184 -0.07149 -0.05701 0.01679  178 VAL B C   
3597 O O   . VAL B 178 ? 0.30285 0.48438 0.59610 -0.07209 -0.05855 0.02557  178 VAL B O   
3598 C CB  . VAL B 178 ? 0.28962 0.44798 0.55635 -0.06035 -0.04762 0.02186  178 VAL B CB  
3599 C CG1 . VAL B 178 ? 0.27044 0.44095 0.53198 -0.05671 -0.04827 0.03287  178 VAL B CG1 
3600 C CG2 . VAL B 178 ? 0.26415 0.40741 0.52879 -0.05599 -0.04178 0.02521  178 VAL B CG2 
3601 N N   . GLY B 179 ? 0.31190 0.49302 0.59381 -0.07501 -0.06056 0.00444  179 GLY B N   
3602 C CA  . GLY B 179 ? 0.30025 0.50114 0.58107 -0.07887 -0.06644 0.00297  179 GLY B CA  
3603 C C   . GLY B 179 ? 0.28871 0.50207 0.55738 -0.07295 -0.06583 0.01483  179 GLY B C   
3604 O O   . GLY B 179 ? 0.27973 0.48982 0.53622 -0.06735 -0.06209 0.01798  179 GLY B O   
3605 N N   . THR B 180 ? 0.27859 0.50651 0.55221 -0.07421 -0.06965 0.02200  180 THR B N   
3606 C CA  . THR B 180 ? 0.26428 0.50545 0.53019 -0.06863 -0.06998 0.03389  180 THR B CA  
3607 C C   . THR B 180 ? 0.26037 0.50604 0.53807 -0.06733 -0.07037 0.04478  180 THR B C   
3608 O O   . THR B 180 ? 0.22390 0.48674 0.50714 -0.07064 -0.07559 0.04662  180 THR B O   
3609 C CB  . THR B 180 ? 0.26058 0.52367 0.51849 -0.07178 -0.07583 0.02996  180 THR B CB  
3610 O OG1 . THR B 180 ? 0.26358 0.53703 0.53183 -0.07972 -0.08159 0.02299  180 THR B OG1 
3611 C CG2 . THR B 180 ? 0.27048 0.53264 0.51586 -0.07284 -0.07496 0.01895  180 THR B CG2 
3612 N N   . PRO B 181 ? 0.26929 0.50167 0.55141 -0.06278 -0.06490 0.05176  181 PRO B N   
3613 C CA  . PRO B 181 ? 0.24900 0.48808 0.54164 -0.06063 -0.06440 0.06197  181 PRO B CA  
3614 C C   . PRO B 181 ? 0.26473 0.51707 0.55308 -0.05419 -0.06520 0.07142  181 PRO B C   
3615 O O   . PRO B 181 ? 0.27903 0.53134 0.55612 -0.05025 -0.06467 0.07267  181 PRO B O   
3616 C CB  . PRO B 181 ? 0.23081 0.45336 0.52619 -0.05699 -0.05773 0.06558  181 PRO B CB  
3617 C CG  . PRO B 181 ? 0.22722 0.43611 0.51060 -0.05432 -0.05447 0.06091  181 PRO B CG  
3618 C CD  . PRO B 181 ? 0.26065 0.47329 0.53884 -0.05972 -0.05892 0.05013  181 PRO B CD  
3619 N N   . GLU B 182 ? 0.24052 0.50515 0.53948 -0.05321 -0.06661 0.07877  182 GLU B N   
3620 C CA  . GLU B 182 ? 0.25292 0.53040 0.55213 -0.04642 -0.06741 0.08879  182 GLU B CA  
3621 C C   . GLU B 182 ? 0.24290 0.51057 0.54505 -0.03795 -0.06062 0.09568  182 GLU B C   
3622 O O   . GLU B 182 ? 0.24327 0.50195 0.55069 -0.03862 -0.05646 0.09438  182 GLU B O   
3623 C CB  . GLU B 182 ? 0.27826 0.57701 0.58858 -0.04967 -0.07296 0.09248  182 GLU B CB  
3624 C CG  . GLU B 182 ? 0.29233 0.60781 0.60369 -0.04338 -0.07558 0.10276  182 GLU B CG  
3625 C CD  . GLU B 182 ? 0.30277 0.61759 0.60066 -0.04052 -0.07662 0.10404  182 GLU B CD  
3626 O OE1 . GLU B 182 ? 0.32017 0.63885 0.60886 -0.04693 -0.08039 0.09623  182 GLU B OE1 
3627 O OE2 . GLU B 182 ? 0.30539 0.61637 0.60265 -0.03202 -0.07355 0.11265  182 GLU B OE2 
3628 N N   . ARG B 183 ? 0.26695 0.53732 0.56653 -0.03017 -0.05967 0.10311  183 ARG B N   
3629 C CA  . ARG B 183 ? 0.26232 0.52311 0.56520 -0.02182 -0.05327 0.10791  183 ARG B CA  
3630 C C   . ARG B 183 ? 0.24578 0.51085 0.56120 -0.02099 -0.05029 0.10931  183 ARG B C   
3631 O O   . ARG B 183 ? 0.24513 0.50101 0.56220 -0.01613 -0.04417 0.10960  183 ARG B O   
3632 C CB  . ARG B 183 ? 0.26099 0.52829 0.56594 -0.01377 -0.05404 0.11706  183 ARG B CB  
3633 C CG  . ARG B 183 ? 0.26207 0.52600 0.55542 -0.01320 -0.05593 0.11868  183 ARG B CG  
3634 C CD  . ARG B 183 ? 0.24286 0.48633 0.52722 -0.01181 -0.05046 0.11442  183 ARG B CD  
3635 N NE  . ARG B 183 ? 0.26604 0.50902 0.53766 -0.01467 -0.05295 0.11327  183 ARG B NE  
3636 C CZ  . ARG B 183 ? 0.25244 0.48053 0.51425 -0.01489 -0.04936 0.10924  183 ARG B CZ  
3637 N NH1 . ARG B 183 ? 0.22671 0.43851 0.48957 -0.01244 -0.04342 0.10628  183 ARG B NH1 
3638 N NH2 . ARG B 183 ? 0.26950 0.50120 0.52012 -0.01785 -0.05182 0.10816  183 ARG B NH2 
3639 N N   . ASP B 184 ? 0.24872 0.52929 0.57309 -0.02596 -0.05448 0.11008  184 ASP B N   
3640 C CA  . ASP B 184 ? 0.22034 0.51082 0.55810 -0.02503 -0.05227 0.11336  184 ASP B CA  
3641 C C   . ASP B 184 ? 0.21981 0.50336 0.56005 -0.03144 -0.04957 0.10912  184 ASP B C   
3642 O O   . ASP B 184 ? 0.20916 0.50055 0.55937 -0.03061 -0.04642 0.11223  184 ASP B O   
3643 C CB  . ASP B 184 ? 0.21416 0.52680 0.56154 -0.02752 -0.05849 0.11764  184 ASP B CB  
3644 C CG  . ASP B 184 ? 0.25115 0.57230 0.59561 -0.02269 -0.06264 0.12294  184 ASP B CG  
3645 O OD1 . ASP B 184 ? 0.25057 0.57384 0.60031 -0.01320 -0.06000 0.12952  184 ASP B OD1 
3646 O OD2 . ASP B 184 ? 0.26146 0.58770 0.59893 -0.02847 -0.06859 0.12048  184 ASP B OD2 
3647 N N   . GLN B 185 ? 0.22481 0.49479 0.55709 -0.03750 -0.05053 0.10262  185 GLN B N   
3648 C CA  . GLN B 185 ? 0.21744 0.47837 0.55273 -0.04272 -0.04773 0.10001  185 GLN B CA  
3649 C C   . GLN B 185 ? 0.21026 0.45818 0.54012 -0.03719 -0.04056 0.10033  185 GLN B C   
3650 O O   . GLN B 185 ? 0.20087 0.44369 0.53391 -0.04069 -0.03775 0.10020  185 GLN B O   
3651 C CB  . GLN B 185 ? 0.22026 0.47151 0.55157 -0.05086 -0.05168 0.09235  185 GLN B CB  
3652 C CG  . GLN B 185 ? 0.23329 0.49595 0.56517 -0.05579 -0.05906 0.08903  185 GLN B CG  
3653 C CD  . GLN B 185 ? 0.24331 0.49792 0.57518 -0.06470 -0.06276 0.07949  185 GLN B CD  
3654 O OE1 . GLN B 185 ? 0.26193 0.52310 0.59030 -0.06864 -0.06822 0.07348  185 GLN B OE1 
3655 N NE2 . GLN B 185 ? 0.22730 0.46877 0.56411 -0.06795 -0.05990 0.07790  185 GLN B NE2 
3656 N N   . ALA B 186 ? 0.23877 0.48193 0.56148 -0.02912 -0.03785 0.10119  186 ALA B N   
3657 C CA  . ALA B 186 ? 0.23249 0.46282 0.54914 -0.02420 -0.03154 0.10009  186 ALA B CA  
3658 C C   . ALA B 186 ? 0.22725 0.46609 0.55089 -0.01693 -0.02678 0.10361  186 ALA B C   
3659 O O   . ALA B 186 ? 0.23231 0.48591 0.56488 -0.01416 -0.02836 0.10738  186 ALA B O   
3660 C CB  . ALA B 186 ? 0.20995 0.42760 0.51453 -0.02084 -0.03169 0.09774  186 ALA B CB  
3661 N N   . VAL B 187 ? 0.20973 0.44007 0.52972 -0.01384 -0.02084 0.10163  187 VAL B N   
3662 C CA  . VAL B 187 ? 0.20844 0.44465 0.53355 -0.00631 -0.01544 0.10203  187 VAL B CA  
3663 C C   . VAL B 187 ? 0.22058 0.44157 0.53767 -0.00048 -0.01242 0.09896  187 VAL B C   
3664 O O   . VAL B 187 ? 0.21417 0.42086 0.52104 -0.00319 -0.01302 0.09671  187 VAL B O   
3665 C CB  . VAL B 187 ? 0.21918 0.46377 0.54877 -0.00862 -0.01076 0.10193  187 VAL B CB  
3666 C CG1 . VAL B 187 ? 0.22230 0.48483 0.56283 -0.01340 -0.01338 0.10642  187 VAL B CG1 
3667 C CG2 . VAL B 187 ? 0.20749 0.43932 0.52867 -0.01412 -0.00951 0.09997  187 VAL B CG2 
3668 N N   . LEU B 188 ? 0.21157 0.43611 0.53486 0.00762  -0.00906 0.09863  188 LEU B N   
3669 C CA  . LEU B 188 ? 0.20599 0.41700 0.52555 0.01374  -0.00643 0.09617  188 LEU B CA  
3670 C C   . LEU B 188 ? 0.20778 0.41234 0.52270 0.01377  -0.00043 0.09027  188 LEU B C   
3671 O O   . LEU B 188 ? 0.22764 0.44307 0.54583 0.01209  0.00292  0.08853  188 LEU B O   
3672 C CB  . LEU B 188 ? 0.21743 0.43472 0.54903 0.02272  -0.00560 0.09791  188 LEU B CB  
3673 C CG  . LEU B 188 ? 0.19428 0.42388 0.53400 0.02380  -0.01115 0.10480  188 LEU B CG  
3674 C CD1 . LEU B 188 ? 0.24802 0.48068 0.60085 0.03381  -0.00978 0.10677  188 LEU B CD1 
3675 C CD2 . LEU B 188 ? 0.20973 0.43264 0.53991 0.01912  -0.01720 0.10862  188 LEU B CD2 
3676 N N   . ALA B 189 ? 0.21301 0.40168 0.52067 0.01555  0.00089  0.08769  189 ALA B N   
3677 C CA  . ALA B 189 ? 0.23148 0.41453 0.53488 0.01584  0.00634  0.08161  189 ALA B CA  
3678 C C   . ALA B 189 ? 0.22180 0.39990 0.53139 0.02382  0.00993  0.07729  189 ALA B C   
3679 O O   . ALA B 189 ? 0.24553 0.40909 0.54981 0.02464  0.01096  0.07486  189 ALA B O   
3680 C CB  . ALA B 189 ? 0.21123 0.38006 0.50196 0.01049  0.00538  0.08104  189 ALA B CB  
3681 N N   . THR B 190 ? 0.22393 0.41399 0.54611 0.02973  0.01189  0.07599  190 THR B N   
3682 C CA  . THR B 190 ? 0.23524 0.42026 0.56640 0.03780  0.01551  0.07050  190 THR B CA  
3683 C C   . THR B 190 ? 0.23866 0.42167 0.56523 0.03702  0.02132  0.06080  190 THR B C   
3684 O O   . THR B 190 ? 0.24096 0.43680 0.56383 0.03305  0.02402  0.05817  190 THR B O   
3685 C CB  . THR B 190 ? 0.23914 0.43916 0.58661 0.04487  0.01667  0.07034  190 THR B CB  
3686 O OG1 . THR B 190 ? 0.22828 0.44781 0.57698 0.04232  0.01963  0.06780  190 THR B OG1 
3687 C CG2 . THR B 190 ? 0.21066 0.41296 0.56375 0.04624  0.01043  0.08052  190 THR B CG2 
3688 N N   . MET B 191 ? 0.23757 0.40547 0.56488 0.04031  0.02295  0.05610  191 MET B N   
3689 C CA  . MET B 191 ? 0.24498 0.40876 0.56619 0.03845  0.02750  0.04688  191 MET B CA  
3690 C C   . MET B 191 ? 0.26314 0.41472 0.59420 0.04503  0.02983  0.03993  191 MET B C   
3691 O O   . MET B 191 ? 0.24701 0.38860 0.58688 0.04963  0.02691  0.04514  191 MET B O   
3692 C CB  . MET B 191 ? 0.24042 0.39345 0.54602 0.03080  0.02540  0.05023  191 MET B CB  
3693 C CG  . MET B 191 ? 0.22616 0.38865 0.52358 0.02384  0.02313  0.05626  191 MET B CG  
3694 S SD  . MET B 191 ? 0.21984 0.36962 0.50199 0.01615  0.02100  0.05928  191 MET B SD  
3695 C CE  . MET B 191 ? 0.20699 0.34284 0.48723 0.01667  0.01527  0.06667  191 MET B CE  
3696 N N   . ASP B 192 ? 0.26052 0.41389 0.59091 0.04511  0.03497  0.02818  192 ASP B N   
3697 C CA  . ASP B 192 ? 0.25351 0.39377 0.59172 0.04928  0.03754  0.01898  192 ASP B CA  
3698 C C   . ASP B 192 ? 0.26073 0.38494 0.58676 0.04327  0.03607  0.02024  192 ASP B C   
3699 O O   . ASP B 192 ? 0.24825 0.37653 0.55967 0.03624  0.03535  0.02332  192 ASP B O   
3700 C CB  . ASP B 192 ? 0.24762 0.40174 0.59114 0.05184  0.04402  0.00363  192 ASP B CB  
3701 C CG  . ASP B 192 ? 0.26654 0.43757 0.62417 0.05878  0.04635  0.00074  192 ASP B CG  
3702 O OD1 . ASP B 192 ? 0.27172 0.43549 0.64403 0.06573  0.04438  0.00457  192 ASP B OD1 
3703 O OD2 . ASP B 192 ? 0.26987 0.46291 0.62448 0.05722  0.05011  -0.00452 192 ASP B OD2 
3704 N N   . PRO B 193 ? 0.27664 0.38273 0.60963 0.04578  0.03542  0.01878  193 PRO B N   
3705 C CA  . PRO B 193 ? 0.25522 0.34826 0.57779 0.03997  0.03491  0.01813  193 PRO B CA  
3706 C C   . PRO B 193 ? 0.26659 0.36999 0.58090 0.03579  0.03933  0.00652  193 PRO B C   
3707 O O   . PRO B 193 ? 0.26095 0.37509 0.58275 0.03912  0.04374  -0.00551 193 PRO B O   
3708 C CB  . PRO B 193 ? 0.26533 0.34031 0.60226 0.04447  0.03450  0.01623  193 PRO B CB  
3709 C CG  . PRO B 193 ? 0.26721 0.34286 0.61878 0.05162  0.03232  0.02317  193 PRO B CG  
3710 C CD  . PRO B 193 ? 0.26449 0.36111 0.61653 0.05380  0.03462  0.01951  193 PRO B CD  
3711 N N   . GLY B 194 ? 0.26371 0.36599 0.56274 0.02849  0.03815  0.01029  194 GLY B N   
3712 C CA  . GLY B 194 ? 0.27042 0.38612 0.55995 0.02356  0.04135  0.00312  194 GLY B CA  
3713 C C   . GLY B 194 ? 0.25775 0.39060 0.53879 0.01996  0.04080  0.00977  194 GLY B C   
3714 O O   . GLY B 194 ? 0.26735 0.41027 0.53886 0.01451  0.04215  0.00849  194 GLY B O   
3715 N N   . ASP B 195 ? 0.23851 0.37574 0.52407 0.02263  0.03867  0.01722  195 ASP B N   
3716 C CA  . ASP B 195 ? 0.24254 0.39321 0.52178 0.01849  0.03722  0.02507  195 ASP B CA  
3717 C C   . ASP B 195 ? 0.23574 0.37495 0.50500 0.01327  0.03291  0.03475  195 ASP B C   
3718 O O   . ASP B 195 ? 0.24588 0.36836 0.51324 0.01348  0.03090  0.03651  195 ASP B O   
3719 C CB  . ASP B 195 ? 0.23591 0.39532 0.52436 0.02268  0.03607  0.02930  195 ASP B CB  
3720 C CG  . ASP B 195 ? 0.25543 0.42833 0.55487 0.02841  0.04067  0.01955  195 ASP B CG  
3721 O OD1 . ASP B 195 ? 0.27568 0.45318 0.57438 0.02836  0.04491  0.00865  195 ASP B OD1 
3722 O OD2 . ASP B 195 ? 0.24482 0.42489 0.55394 0.03292  0.04006  0.02220  195 ASP B OD2 
3723 N N   . VAL B 196 ? 0.23029 0.37938 0.49428 0.00849  0.03157  0.04107  196 VAL B N   
3724 C CA  . VAL B 196 ? 0.22109 0.36108 0.47748 0.00383  0.02766  0.04911  196 VAL B CA  
3725 C C   . VAL B 196 ? 0.22181 0.37088 0.48054 0.00173  0.02493  0.05640  196 VAL B C   
3726 O O   . VAL B 196 ? 0.22944 0.39510 0.49252 0.00126  0.02669  0.05647  196 VAL B O   
3727 C CB  . VAL B 196 ? 0.21114 0.35132 0.45898 -0.00144 0.02881  0.04861  196 VAL B CB  
3728 C CG1 . VAL B 196 ? 0.20937 0.33670 0.45115 -0.00454 0.02521  0.05475  196 VAL B CG1 
3729 C CG2 . VAL B 196 ? 0.24795 0.38424 0.49461 -0.00021 0.03199  0.03989  196 VAL B CG2 
3730 N N   . LEU B 197 ? 0.20107 0.34037 0.45728 0.00011  0.02061  0.06218  197 LEU B N   
3731 C CA  . LEU B 197 ? 0.18546 0.33079 0.44384 -0.00309 0.01726  0.06835  197 LEU B CA  
3732 C C   . LEU B 197 ? 0.19260 0.33091 0.44464 -0.00850 0.01526  0.07150  197 LEU B C   
3733 O O   . LEU B 197 ? 0.20982 0.33519 0.45621 -0.00853 0.01381  0.07106  197 LEU B O   
3734 C CB  . LEU B 197 ? 0.19106 0.33300 0.45336 -0.00020 0.01361  0.07099  197 LEU B CB  
3735 C CG  . LEU B 197 ? 0.18191 0.32594 0.44496 -0.00423 0.00898  0.07611  197 LEU B CG  
3736 C CD1 . LEU B 197 ? 0.17795 0.33776 0.44848 -0.00643 0.00917  0.07865  197 LEU B CD1 
3737 C CD2 . LEU B 197 ? 0.16696 0.30720 0.43132 -0.00145 0.00530  0.07811  197 LEU B CD2 
3738 N N   . ILE B 198 ? 0.17756 0.32506 0.43173 -0.01294 0.01526  0.07508  198 ILE B N   
3739 C CA  . ILE B 198 ? 0.18269 0.32407 0.43420 -0.01771 0.01333  0.07845  198 ILE B CA  
3740 C C   . ILE B 198 ? 0.16945 0.31074 0.42637 -0.02057 0.00901  0.08228  198 ILE B C   
3741 O O   . ILE B 198 ? 0.17215 0.32466 0.43622 -0.02128 0.00827  0.08493  198 ILE B O   
3742 C CB  . ILE B 198 ? 0.17912 0.33074 0.43139 -0.02114 0.01579  0.08125  198 ILE B CB  
3743 C CG1 . ILE B 198 ? 0.19792 0.35547 0.44628 -0.01851 0.02026  0.07584  198 ILE B CG1 
3744 C CG2 . ILE B 198 ? 0.18609 0.32884 0.43603 -0.02459 0.01432  0.08404  198 ILE B CG2 
3745 C CD1 . ILE B 198 ? 0.17956 0.32278 0.42065 -0.01649 0.02102  0.07077  198 ILE B CD1 
3746 N N   . VAL B 199 ? 0.17068 0.30045 0.42485 -0.02244 0.00622  0.08190  199 VAL B N   
3747 C CA  . VAL B 199 ? 0.16695 0.29561 0.42618 -0.02539 0.00185  0.08314  199 VAL B CA  
3748 C C   . VAL B 199 ? 0.17613 0.29782 0.43753 -0.02954 0.00044  0.08411  199 VAL B C   
3749 O O   . VAL B 199 ? 0.18932 0.30163 0.44454 -0.02871 0.00139  0.08153  199 VAL B O   
3750 C CB  . VAL B 199 ? 0.18376 0.30685 0.43853 -0.02284 -0.00073 0.07980  199 VAL B CB  
3751 C CG1 . VAL B 199 ? 0.18758 0.31137 0.44716 -0.02656 -0.00545 0.07946  199 VAL B CG1 
3752 C CG2 . VAL B 199 ? 0.16964 0.29918 0.42521 -0.01811 0.00042  0.07997  199 VAL B CG2 
3753 N N   . ARG B 200 ? 0.17870 0.30519 0.45042 -0.03396 -0.00185 0.08810  200 ARG B N   
3754 C CA  . ARG B 200 ? 0.18097 0.30089 0.45927 -0.03792 -0.00357 0.08975  200 ARG B CA  
3755 C C   . ARG B 200 ? 0.19991 0.30878 0.47680 -0.03834 -0.00674 0.08289  200 ARG B C   
3756 O O   . ARG B 200 ? 0.19636 0.30633 0.47010 -0.03745 -0.00891 0.07888  200 ARG B O   
3757 C CB  . ARG B 200 ? 0.18322 0.31187 0.47542 -0.04289 -0.00547 0.09681  200 ARG B CB  
3758 C CG  . ARG B 200 ? 0.19418 0.31614 0.49711 -0.04699 -0.00728 0.10034  200 ARG B CG  
3759 C CD  . ARG B 200 ? 0.20313 0.32628 0.51945 -0.05197 -0.01146 0.10293  200 ARG B CD  
3760 N NE  . ARG B 200 ? 0.22988 0.34327 0.55413 -0.05427 -0.01326 0.10585  200 ARG B NE  
3761 C CZ  . ARG B 200 ? 0.23254 0.33363 0.56500 -0.05570 -0.01563 0.09987  200 ARG B CZ  
3762 N NH1 . ARG B 200 ? 0.19301 0.28908 0.52034 -0.05442 -0.01664 0.08933  200 ARG B NH1 
3763 N NH2 . ARG B 200 ? 0.24452 0.33706 0.58628 -0.05690 -0.01706 0.10332  200 ARG B NH2 
3764 N N   . GLN B 201 ? 0.18995 0.28978 0.46978 -0.03966 -0.00702 0.08147  201 GLN B N   
3765 C CA  . GLN B 201 ? 0.19636 0.28757 0.47675 -0.04049 -0.00981 0.07360  201 GLN B CA  
3766 C C   . GLN B 201 ? 0.20347 0.29803 0.49353 -0.04450 -0.01419 0.07197  201 GLN B C   
3767 O O   . GLN B 201 ? 0.21848 0.31803 0.52042 -0.04807 -0.01539 0.07833  201 GLN B O   
3768 C CB  . GLN B 201 ? 0.19700 0.27915 0.48367 -0.04131 -0.00934 0.07277  201 GLN B CB  
3769 C CG  . GLN B 201 ? 0.21517 0.28971 0.50626 -0.04267 -0.01219 0.06333  201 GLN B CG  
3770 C CD  . GLN B 201 ? 0.20618 0.27172 0.50595 -0.04264 -0.01148 0.06216  201 GLN B CD  
3771 O OE1 . GLN B 201 ? 0.19583 0.26082 0.49407 -0.04076 -0.00855 0.06794  201 GLN B OE1 
3772 N NE2 . GLN B 201 ? 0.21776 0.27680 0.52775 -0.04466 -0.01422 0.05417  201 GLN B NE2 
3773 N N   . ARG B 202 ? 0.19346 0.28700 0.47847 -0.04436 -0.01671 0.06382  202 ARG B N   
3774 C CA  . ARG B 202 ? 0.18542 0.28262 0.47778 -0.04844 -0.02143 0.05955  202 ARG B CA  
3775 C C   . ARG B 202 ? 0.20513 0.31452 0.49684 -0.04853 -0.02276 0.06409  202 ARG B C   
3776 O O   . ARG B 202 ? 0.19980 0.31420 0.49918 -0.05262 -0.02691 0.06194  202 ARG B O   
3777 C CB  . ARG B 202 ? 0.20597 0.29881 0.51648 -0.05387 -0.02399 0.06031  202 ARG B CB  
3778 C CG  . ARG B 202 ? 0.22790 0.30848 0.54416 -0.05420 -0.02384 0.05405  202 ARG B CG  
3779 C CD  . ARG B 202 ? 0.25275 0.32859 0.59037 -0.05992 -0.02725 0.05486  202 ARG B CD  
3780 N NE  . ARG B 202 ? 0.27663 0.35558 0.61902 -0.06416 -0.03194 0.04651  202 ARG B NE  
3781 C CZ  . ARG B 202 ? 0.31636 0.38902 0.66293 -0.06585 -0.03438 0.03324  202 ARG B CZ  
3782 N NH1 . ARG B 202 ? 0.32200 0.38400 0.67096 -0.06347 -0.03250 0.02712  202 ARG B NH1 
3783 N NH2 . ARG B 202 ? 0.31849 0.39707 0.66726 -0.07001 -0.03878 0.02526  202 ARG B NH2 
3784 N N   . VAL B 203 ? 0.22335 0.33803 0.50732 -0.04418 -0.01953 0.06949  203 VAL B N   
3785 C CA  . VAL B 203 ? 0.20244 0.32928 0.48773 -0.04331 -0.02030 0.07376  203 VAL B CA  
3786 C C   . VAL B 203 ? 0.21187 0.34197 0.48730 -0.04002 -0.02183 0.07021  203 VAL B C   
3787 O O   . VAL B 203 ? 0.20790 0.33318 0.47277 -0.03582 -0.01949 0.06897  203 VAL B O   
3788 C CB  . VAL B 203 ? 0.19117 0.32337 0.47608 -0.04026 -0.01580 0.08072  203 VAL B CB  
3789 C CG1 . VAL B 203 ? 0.18236 0.32712 0.46842 -0.03785 -0.01599 0.08360  203 VAL B CG1 
3790 C CG2 . VAL B 203 ? 0.19844 0.33230 0.49436 -0.04450 -0.01507 0.08645  203 VAL B CG2 
3791 N N   . VAL B 204 ? 0.21238 0.35188 0.49212 -0.04226 -0.02601 0.06963  204 VAL B N   
3792 C CA  . VAL B 204 ? 0.20147 0.34661 0.47330 -0.04007 -0.02854 0.06734  204 VAL B CA  
3793 C C   . VAL B 204 ? 0.20425 0.35541 0.47331 -0.03402 -0.02621 0.07372  204 VAL B C   
3794 O O   . VAL B 204 ? 0.20683 0.36549 0.48358 -0.03322 -0.02517 0.07857  204 VAL B O   
3795 C CB  . VAL B 204 ? 0.19078 0.34538 0.46897 -0.04528 -0.03438 0.06406  204 VAL B CB  
3796 C CG1 . VAL B 204 ? 0.19381 0.35914 0.46533 -0.04278 -0.03717 0.06491  204 VAL B CG1 
3797 C CG2 . VAL B 204 ? 0.21099 0.35834 0.49067 -0.05035 -0.03667 0.05482  204 VAL B CG2 
3798 N N   . HIS B 205 ? 0.20171 0.35023 0.46101 -0.02973 -0.02531 0.07375  205 HIS B N   
3799 C CA  . HIS B 205 ? 0.20415 0.35584 0.46294 -0.02357 -0.02303 0.07931  205 HIS B CA  
3800 C C   . HIS B 205 ? 0.21498 0.36809 0.46599 -0.02085 -0.02500 0.08054  205 HIS B C   
3801 O O   . HIS B 205 ? 0.21030 0.36181 0.45408 -0.02357 -0.02701 0.07657  205 HIS B O   
3802 C CB  . HIS B 205 ? 0.20479 0.34774 0.46210 -0.02048 -0.01735 0.08008  205 HIS B CB  
3803 C CG  . HIS B 205 ? 0.22694 0.35816 0.47506 -0.02068 -0.01553 0.07682  205 HIS B CG  
3804 N ND1 . HIS B 205 ? 0.22414 0.34957 0.47119 -0.02512 -0.01607 0.07238  205 HIS B ND1 
3805 C CD2 . HIS B 205 ? 0.24031 0.36505 0.48113 -0.01707 -0.01336 0.07749  205 HIS B CD2 
3806 C CE1 . HIS B 205 ? 0.23884 0.35577 0.47766 -0.02389 -0.01401 0.07027  205 HIS B CE1 
3807 N NE2 . HIS B 205 ? 0.24804 0.36456 0.48261 -0.01942 -0.01241 0.07357  205 HIS B NE2 
3808 N N   . ALA B 206 ? 0.23111 0.38819 0.48468 -0.01531 -0.02429 0.08635  206 ALA B N   
3809 C CA  . ALA B 206 ? 0.22677 0.38734 0.47573 -0.01254 -0.02666 0.09060  206 ALA B CA  
3810 C C   . ALA B 206 ? 0.23320 0.39193 0.48777 -0.00549 -0.02403 0.09660  206 ALA B C   
3811 O O   . ALA B 206 ? 0.22549 0.39023 0.48994 -0.00269 -0.02330 0.09852  206 ALA B O   
3812 C CB  . ALA B 206 ? 0.22763 0.40357 0.47851 -0.01519 -0.03273 0.09225  206 ALA B CB  
3813 N N   . GLY B 207 ? 0.25777 0.40862 0.50730 -0.00270 -0.02254 0.09922  207 GLY B N   
3814 C CA  . GLY B 207 ? 0.26232 0.41174 0.51928 0.00390  -0.02135 0.10556  207 GLY B CA  
3815 C C   . GLY B 207 ? 0.26913 0.43267 0.53360 0.00622  -0.02607 0.11288  207 GLY B C   
3816 O O   . GLY B 207 ? 0.26044 0.43515 0.52082 0.00222  -0.03087 0.11401  207 GLY B O   
3817 N N   . GLY B 208 ? 0.30670 0.47063 0.58319 0.01288  -0.02472 0.11741  208 GLY B N   
3818 C CA  . GLY B 208 ? 0.33992 0.51801 0.62638 0.01608  -0.02894 0.12512  208 GLY B CA  
3819 C C   . GLY B 208 ? 0.38350 0.56319 0.67366 0.02000  -0.03186 0.13599  208 GLY B C   
3820 O O   . GLY B 208 ? 0.39028 0.58328 0.68953 0.02281  -0.03592 0.14393  208 GLY B O   
3821 N N   . GLY B 209 ? 0.46361 0.83247 0.93372 0.14327  0.16217  0.46745  209 GLY B N   
3822 C CA  . GLY B 209 ? 0.46775 0.84516 0.92975 0.15104  0.16573  0.47101  209 GLY B CA  
3823 C C   . GLY B 209 ? 0.46463 0.83472 0.92980 0.14506  0.16342  0.46687  209 GLY B C   
3824 O O   . GLY B 209 ? 0.46172 0.81928 0.91764 0.13884  0.16088  0.45799  209 GLY B O   
3825 N N   . ASN B 210 ? 0.39022 0.76436 0.86507 0.15089  0.16014  0.47129  210 ASN B N   
3826 C CA  . ASN B 210 ? 0.38767 0.75899 0.87395 0.14676  0.15940  0.47227  210 ASN B CA  
3827 C C   . ASN B 210 ? 0.40438 0.76971 0.89756 0.15817  0.14098  0.46052  210 ASN B C   
3828 O O   . ASN B 210 ? 0.41822 0.77881 0.89989 0.16513  0.13691  0.46267  210 ASN B O   
3829 C CB  . ASN B 210 ? 0.38538 0.75666 0.86286 0.14404  0.16363  0.47166  210 ASN B CB  
3830 C CG  . ASN B 210 ? 0.38439 0.75173 0.87818 0.14044  0.16167  0.47468  210 ASN B CG  
3831 O OD1 . ASN B 210 ? 0.38710 0.75211 0.89323 0.14329  0.15567  0.47013  210 ASN B OD1 
3832 N ND2 . ASN B 210 ? 0.38424 0.75014 0.88196 0.13746  0.16089  0.47427  210 ASN B ND2 
3833 N N   . ARG B 211 ? 0.46657 0.83203 0.98301 0.16045  0.12866  0.44848  211 ARG B N   
3834 C CA  . ARG B 211 ? 0.48511 0.84458 1.01247 0.17344  0.10611  0.43362  211 ARG B CA  
3835 C C   . ARG B 211 ? 0.48847 0.84593 1.02381 0.17519  0.10218  0.43086  211 ARG B C   
3836 O O   . ARG B 211 ? 0.50864 0.85756 1.04841 0.18764  0.08173  0.41953  211 ARG B O   
3837 C CB  . ARG B 211 ? 0.49334 0.86055 1.06175 0.17229  0.09486  0.42022  211 ARG B CB  
3838 C CG  . ARG B 211 ? 0.58930 0.95192 1.18013 0.18629  0.06662  0.40057  211 ARG B CG  
3839 C CD  . ARG B 211 ? 0.60646 0.94718 1.15843 0.20744  0.04383  0.39439  211 ARG B CD  
3840 N NE  . ARG B 211 ? 0.63047 0.96369 1.20695 0.22321  0.01035  0.37211  211 ARG B NE  
3841 C CZ  . ARG B 211 ? 0.65958 0.98480 1.23583 0.23442  -0.00577 0.36319  211 ARG B CZ  
3842 N NH1 . ARG B 211 ? 0.66207 0.98482 1.21834 0.23069  0.00792  0.37522  211 ARG B NH1 
3843 N NH2 . ARG B 211 ? 0.66416 0.98200 1.26402 0.25068  -0.03976 0.34050  211 ARG B NH2 
3844 N N   . THR B 212 ? 0.45699 0.81862 0.99320 0.16580  0.11687  0.43908  212 THR B N   
3845 C CA  . THR B 212 ? 0.44308 0.80149 0.99131 0.16918  0.10957  0.43348  212 THR B CA  
3846 C C   . THR B 212 ? 0.45185 0.79364 0.98344 0.17750  0.09724  0.43880  212 THR B C   
3847 O O   . THR B 212 ? 0.45849 0.79304 0.96313 0.18299  0.09681  0.44658  212 THR B O   
3848 C CB  . THR B 212 ? 0.42950 0.79135 0.97848 0.16160  0.12225  0.43907  212 THR B CB  
3849 O OG1 . THR B 212 ? 0.41548 0.77330 0.94556 0.15421  0.13310  0.45634  212 THR B OG1 
3850 C CG2 . THR B 212 ? 0.39835 0.77304 0.95449 0.15824  0.13369  0.43403  212 THR B CG2 
3851 N N   . THR B 213 ? 0.50500 0.83906 1.05020 0.18103  0.08627  0.43414  213 THR B N   
3852 C CA  . THR B 213 ? 0.54994 0.86337 1.08176 0.18852  0.07280  0.44164  213 THR B CA  
3853 C C   . THR B 213 ? 0.56681 0.87367 1.10925 0.18027  0.07607  0.45322  213 THR B C   
3854 O O   . THR B 213 ? 0.56322 0.86209 1.09295 0.17726  0.08130  0.47210  213 THR B O   
3855 C CB  . THR B 213 ? 0.56294 0.86613 1.10729 0.20301  0.04721  0.42366  213 THR B CB  
3856 O OG1 . THR B 213 ? 0.54265 0.85816 1.12237 0.20257  0.04387  0.40646  213 THR B OG1 
3857 C CG2 . THR B 213 ? 0.53868 0.84517 1.07871 0.21297  0.03702  0.41115  213 THR B CG2 
3858 N N   . ALA B 214 ? 0.58403 0.89534 1.15244 0.17870  0.07187  0.44082  214 ALA B N   
3859 C CA  . ALA B 214 ? 0.61952 0.92079 1.20456 0.17330  0.06713  0.44686  214 ALA B CA  
3860 C C   . ALA B 214 ? 0.62604 0.93671 1.20703 0.15973  0.08665  0.46351  214 ALA B C   
3861 O O   . ALA B 214 ? 0.57068 0.89749 1.13796 0.15573  0.10365  0.46392  214 ALA B O   
3862 C CB  . ALA B 214 ? 0.63920 0.94427 1.24792 0.18197  0.05478  0.42294  214 ALA B CB  
3863 N N   . GLY B 215 ? 0.76212 1.06232 1.36075 0.15253  0.08226  0.47736  215 GLY B N   
3864 C CA  . GLY B 215 ? 0.73932 1.05207 1.34345 0.14039  0.09927  0.49428  215 GLY B CA  
3865 C C   . GLY B 215 ? 0.69229 1.01152 1.30421 0.13644  0.10207  0.48524  215 GLY B C   
3866 O O   . GLY B 215 ? 0.74944 1.05730 1.38851 0.13420  0.08751  0.48270  215 GLY B O   
3867 N N   . LYS B 216 ? 0.50551 0.83978 1.09327 0.13716  0.11773  0.48002  216 LYS B N   
3868 C CA  . LYS B 216 ? 0.41926 0.75893 1.00433 0.13525  0.12270  0.47488  216 LYS B CA  
3869 C C   . LYS B 216 ? 0.39268 0.74831 0.95677 0.12841  0.14504  0.48586  216 LYS B C   
3870 O O   . LYS B 216 ? 0.38694 0.74675 0.92821 0.13167  0.15286  0.48227  216 LYS B O   
3871 C CB  . LYS B 216 ? 0.44482 0.78665 1.02318 0.14892  0.11542  0.45233  216 LYS B CB  
3872 C CG  . LYS B 216 ? 0.48427 0.81496 1.08688 0.16079  0.09068  0.43467  216 LYS B CG  
3873 C CD  . LYS B 216 ? 0.45193 0.76961 1.07774 0.15935  0.07410  0.43359  216 LYS B CD  
3874 C CE  . LYS B 216 ? 0.46468 0.79318 1.08009 0.17253  0.07288  0.41654  216 LYS B CE  
3875 N NZ  . LYS B 216 ? 0.45444 0.79707 1.06269 0.19540  0.06905  0.39189  216 LYS B NZ  
3876 N N   . PRO B 217 ? 0.54659 0.47736 0.78374 0.08941  -0.07576 -0.02393 217 PRO B N   
3877 C CA  . PRO B 217 ? 0.47780 0.41312 0.71060 0.08006  -0.07673 -0.01948 217 PRO B CA  
3878 C C   . PRO B 217 ? 0.42441 0.38628 0.67103 0.07587  -0.06529 -0.01893 217 PRO B C   
3879 O O   . PRO B 217 ? 0.41085 0.38027 0.65493 0.07723  -0.05407 -0.02317 217 PRO B O   
3880 C CB  . PRO B 217 ? 0.46924 0.38013 0.67077 0.07415  -0.07506 -0.01991 217 PRO B CB  
3881 C CG  . PRO B 217 ? 0.48950 0.39246 0.68460 0.07756  -0.06782 -0.02555 217 PRO B CG  
3882 C CD  . PRO B 217 ? 0.55057 0.45853 0.76359 0.08840  -0.07186 -0.02781 217 PRO B CD  
3883 N N   . ARG B 218 ? 0.39148 0.36653 0.65229 0.07127  -0.06892 -0.01366 218 ARG B N   
3884 C CA  . ARG B 218 ? 0.35346 0.35177 0.62590 0.06651  -0.05834 -0.01095 218 ARG B CA  
3885 C C   . ARG B 218 ? 0.34204 0.33110 0.59035 0.05771  -0.05390 -0.01146 218 ARG B C   
3886 O O   . ARG B 218 ? 0.34753 0.31808 0.57926 0.05347  -0.06169 -0.01066 218 ARG B O   
3887 C CB  . ARG B 218 ? 0.33453 0.35035 0.63626 0.06480  -0.06431 -0.00435 218 ARG B CB  
3888 C CG  . ARG B 218 ? 0.29637 0.33514 0.61108 0.05962  -0.05335 0.00068  218 ARG B CG  
3889 C CD  . ARG B 218 ? 0.28378 0.33887 0.63213 0.05741  -0.05978 0.00801  218 ARG B CD  
3890 N NE  . ARG B 218 ? 0.31078 0.34802 0.65499 0.05380  -0.07719 0.00763  218 ARG B NE  
3891 C CZ  . ARG B 218 ? 0.31982 0.35186 0.65805 0.04605  -0.08176 0.00969  218 ARG B CZ  
3892 N NH1 . ARG B 218 ? 0.28955 0.33300 0.62681 0.04026  -0.07048 0.01318  218 ARG B NH1 
3893 N NH2 . ARG B 218 ? 0.34745 0.36180 0.67945 0.04512  -0.09860 0.00791  218 ARG B NH2 
3894 N N   . ARG B 219 ? 0.30521 0.30727 0.55083 0.05609  -0.04132 -0.01295 219 ARG B N   
3895 C CA  . ARG B 219 ? 0.30429 0.29999 0.52933 0.04856  -0.03630 -0.01421 219 ARG B CA  
3896 C C   . ARG B 219 ? 0.28170 0.29878 0.51756 0.04435  -0.02948 -0.00931 219 ARG B C   
3897 O O   . ARG B 219 ? 0.27962 0.31712 0.52904 0.04878  -0.02081 -0.00810 219 ARG B O   
3898 C CB  . ARG B 219 ? 0.31306 0.30170 0.52204 0.05060  -0.02903 -0.02170 219 ARG B CB  
3899 C CG  . ARG B 219 ? 0.33220 0.29484 0.52541 0.05152  -0.03455 -0.02550 219 ARG B CG  
3900 C CD  . ARG B 219 ? 0.33662 0.29269 0.51624 0.05046  -0.02791 -0.03254 219 ARG B CD  
3901 N NE  . ARG B 219 ? 0.38672 0.31693 0.54991 0.04685  -0.03163 -0.03328 219 ARG B NE  
3902 C CZ  . ARG B 219 ? 0.37860 0.29826 0.53161 0.04416  -0.02789 -0.03869 219 ARG B CZ  
3903 N NH1 . ARG B 219 ? 0.36259 0.29425 0.51736 0.04512  -0.02190 -0.04544 219 ARG B NH1 
3904 N NH2 . ARG B 219 ? 0.39181 0.28811 0.53298 0.04084  -0.03046 -0.03707 219 ARG B NH2 
3905 N N   . VAL B 220 ? 0.27261 0.28379 0.50070 0.03670  -0.03286 -0.00633 220 VAL B N   
3906 C CA  . VAL B 220 ? 0.26743 0.29613 0.50481 0.03198  -0.02734 -0.00085 220 VAL B CA  
3907 C C   . VAL B 220 ? 0.26472 0.28358 0.48057 0.02508  -0.02544 -0.00251 220 VAL B C   
3908 O O   . VAL B 220 ? 0.28317 0.28340 0.48539 0.02199  -0.03250 -0.00369 220 VAL B O   
3909 C CB  . VAL B 220 ? 0.25539 0.29187 0.51656 0.02998  -0.03521 0.00628  220 VAL B CB  
3910 C CG1 . VAL B 220 ? 0.28990 0.30518 0.54347 0.02847  -0.04982 0.00480  220 VAL B CG1 
3911 C CG2 . VAL B 220 ? 0.22857 0.27923 0.49853 0.02434  -0.03025 0.01268  220 VAL B CG2 
3912 N N   . VAL B 221 ? 0.26463 0.29610 0.47719 0.02397  -0.01586 -0.00258 221 VAL B N   
3913 C CA  . VAL B 221 ? 0.25342 0.27936 0.45031 0.01765  -0.01408 -0.00342 221 VAL B CA  
3914 C C   . VAL B 221 ? 0.23226 0.27200 0.44193 0.01398  -0.01314 0.00433  221 VAL B C   
3915 O O   . VAL B 221 ? 0.23039 0.28951 0.45438 0.01670  -0.00652 0.00913  221 VAL B O   
3916 C CB  . VAL B 221 ? 0.25704 0.28524 0.44036 0.01900  -0.00626 -0.00985 221 VAL B CB  
3917 C CG1 . VAL B 221 ? 0.24154 0.26854 0.41367 0.01276  -0.00429 -0.00986 221 VAL B CG1 
3918 C CG2 . VAL B 221 ? 0.24433 0.25547 0.41668 0.02135  -0.00846 -0.01737 221 VAL B CG2 
3919 N N   . LEU B 222 ? 0.24084 0.27005 0.44550 0.00850  -0.01946 0.00603  222 LEU B N   
3920 C CA  . LEU B 222 ? 0.22356 0.26142 0.44182 0.00472  -0.02135 0.01308  222 LEU B CA  
3921 C C   . LEU B 222 ? 0.22162 0.25941 0.42653 0.00050  -0.01695 0.01284  222 LEU B C   
3922 O O   . LEU B 222 ? 0.22923 0.25186 0.41649 -0.00195 -0.01949 0.00841  222 LEU B O   
3923 C CB  . LEU B 222 ? 0.22099 0.24603 0.44516 0.00312  -0.03424 0.01413  222 LEU B CB  
3924 C CG  . LEU B 222 ? 0.23194 0.25868 0.47280 0.00767  -0.04009 0.01461  222 LEU B CG  
3925 C CD1 . LEU B 222 ? 0.25990 0.26473 0.48376 0.01036  -0.04880 0.00871  222 LEU B CD1 
3926 C CD2 . LEU B 222 ? 0.22670 0.26251 0.49584 0.00595  -0.04724 0.02111  222 LEU B CD2 
3927 N N   . ALA B 223 ? 0.20602 0.26108 0.41969 0.00027  -0.00990 0.01830  223 ALA B N   
3928 C CA  . ALA B 223 ? 0.20572 0.26235 0.40825 -0.00284 -0.00615 0.01843  223 ALA B CA  
3929 C C   . ALA B 223 ? 0.18133 0.24392 0.39841 -0.00625 -0.00838 0.02692  223 ALA B C   
3930 O O   . ALA B 223 ? 0.16895 0.24608 0.40548 -0.00507 -0.00516 0.03500  223 ALA B O   
3931 C CB  . ALA B 223 ? 0.19366 0.26331 0.38883 0.00098  0.00354  0.01662  223 ALA B CB  
3932 C C   . F2Y B 224 ? 0.16540 0.22494 0.37730 -0.01452 -0.01077 0.03387  224 F2Y B C   
3933 O O   . F2Y B 224 ? 0.17544 0.22536 0.36985 -0.01566 -0.01142 0.02771  224 F2Y B O   
3934 C CA  . F2Y B 224 ? 0.17628 0.22981 0.39732 -0.01337 -0.01680 0.03224  224 F2Y B CA  
3935 N N   . F2Y B 224 ? 0.18979 0.24066 0.39838 -0.01018 -0.01359 0.02539  224 F2Y B N   
3936 C CB  . F2Y B 224 ? 0.19556 0.23096 0.41493 -0.01561 -0.02870 0.02932  224 F2Y B CB  
3937 C CG  . F2Y B 224 ? 0.22499 0.25271 0.45134 -0.01378 -0.03691 0.02706  224 F2Y B CG  
3938 C CD1 . F2Y B 224 ? 0.21523 0.25597 0.46162 -0.01181 -0.03484 0.03138  224 F2Y B CD1 
3939 C CE1 . F2Y B 224 ? 0.21945 0.25308 0.47358 -0.00962 -0.04377 0.02892  224 F2Y B CE1 
3940 F F1  . F2Y B 224 ? 0.21891 0.26566 0.49437 -0.00713 -0.04186 0.03284  224 F2Y B F1  
3941 C CD2 . F2Y B 224 ? 0.25825 0.26581 0.47057 -0.01296 -0.04672 0.02083  224 F2Y B CD2 
3942 C CE2 . F2Y B 224 ? 0.26149 0.26074 0.47846 -0.01023 -0.05596 0.01849  224 F2Y B CE2 
3943 F F2  . F2Y B 224 ? 0.31148 0.29032 0.51096 -0.00794 -0.06544 0.01277  224 F2Y B F2  
3944 C CZ  . F2Y B 224 ? 0.24733 0.25978 0.48642 -0.00881 -0.05510 0.02233  224 F2Y B CZ  
3945 O OH  . F2Y B 224 ? 0.25704 0.26148 0.50170 -0.00565 -0.06525 0.01973  224 F2Y B OH  
3946 N N   . PHE B 225 ? 0.15883 0.23445 0.38307 -0.01366 -0.00464 0.04269  225 PHE B N   
3947 C CA  . PHE B 225 ? 0.15794 0.24014 0.37506 -0.01373 0.00021  0.04567  225 PHE B CA  
3948 C C   . PHE B 225 ? 0.15439 0.23332 0.38503 -0.01739 -0.00499 0.05286  225 PHE B C   
3949 O O   . PHE B 225 ? 0.15047 0.23595 0.40330 -0.01842 -0.00549 0.06214  225 PHE B O   
3950 C CB  . PHE B 225 ? 0.14568 0.24661 0.36387 -0.00880 0.01070  0.05135  225 PHE B CB  
3951 C CG  . PHE B 225 ? 0.14378 0.24678 0.34727 -0.00424 0.01485  0.04263  225 PHE B CG  
3952 C CD1 . PHE B 225 ? 0.15251 0.25691 0.36311 -0.00164 0.01559  0.04119  225 PHE B CD1 
3953 C CD2 . PHE B 225 ? 0.15920 0.26237 0.34352 -0.00233 0.01702  0.03541  225 PHE B CD2 
3954 C CE1 . PHE B 225 ? 0.14833 0.25304 0.34593 0.00301  0.01871  0.03265  225 PHE B CE1 
3955 C CE2 . PHE B 225 ? 0.15932 0.26274 0.33185 0.00174  0.01930  0.02647  225 PHE B CE2 
3956 C CZ  . PHE B 225 ? 0.14515 0.24872 0.32364 0.00453  0.02030  0.02504  225 PHE B CZ  
3957 N N   . ASN B 226 ? 0.15740 0.22590 0.37665 -0.01925 -0.00902 0.04859  226 ASN B N   
3958 C CA  . ASN B 226 ? 0.16085 0.22260 0.39097 -0.02206 -0.01563 0.05319  226 ASN B CA  
3959 C C   . ASN B 226 ? 0.16084 0.22967 0.38672 -0.02136 -0.01091 0.05788  226 ASN B C   
3960 O O   . ASN B 226 ? 0.14684 0.22204 0.35712 -0.01889 -0.00490 0.05432  226 ASN B O   
3961 C CB  . ASN B 226 ? 0.17126 0.21312 0.39112 -0.02317 -0.02520 0.04417  226 ASN B CB  
3962 C CG  . ASN B 226 ? 0.17633 0.20824 0.40327 -0.02346 -0.03371 0.04113  226 ASN B CG  
3963 O OD1 . ASN B 226 ? 0.17947 0.21930 0.42592 -0.02405 -0.03429 0.04686  226 ASN B OD1 
3964 N ND2 . ASN B 226 ? 0.19465 0.20931 0.40578 -0.02234 -0.04035 0.03241  226 ASN B ND2 
3965 N N   . SER B 227 ? 0.14813 0.21491 0.38912 -0.02335 -0.01490 0.06562  227 SER B N   
3966 C CA  . SER B 227 ? 0.15486 0.22299 0.39043 -0.02252 -0.01341 0.06854  227 SER B CA  
3967 C C   . SER B 227 ? 0.15856 0.21767 0.37258 -0.02147 -0.01511 0.05667  227 SER B C   
3968 O O   . SER B 227 ? 0.16721 0.21298 0.37456 -0.02227 -0.02058 0.04817  227 SER B O   
3969 C CB  . SER B 227 ? 0.16651 0.22683 0.42113 -0.02523 -0.02079 0.07557  227 SER B CB  
3970 O OG  . SER B 227 ? 0.17587 0.23222 0.42292 -0.02400 -0.02195 0.07528  227 SER B OG  
3971 N N   . VAL B 228 ? 0.15640 0.22321 0.35988 -0.01913 -0.01026 0.05653  228 VAL B N   
3972 C CA  . VAL B 228 ? 0.16703 0.22724 0.35519 -0.01844 -0.01136 0.04666  228 VAL B CA  
3973 C C   . VAL B 228 ? 0.17262 0.21849 0.36292 -0.01898 -0.01845 0.04472  228 VAL B C   
3974 O O   . VAL B 228 ? 0.17594 0.21483 0.35467 -0.01794 -0.01895 0.03670  228 VAL B O   
3975 C CB  . VAL B 228 ? 0.16541 0.23796 0.34496 -0.01552 -0.00634 0.04661  228 VAL B CB  
3976 C CG1 . VAL B 228 ? 0.15942 0.24358 0.33238 -0.01357 -0.00065 0.04500  228 VAL B CG1 
3977 C CG2 . VAL B 228 ? 0.18130 0.25977 0.36901 -0.01374 -0.00638 0.05718  228 VAL B CG2 
3978 N N   . GLN B 229 ? 0.16865 0.20979 0.37450 -0.02017 -0.02385 0.05187  229 GLN B N   
3979 C CA  . GLN B 229 ? 0.17485 0.19933 0.38190 -0.01981 -0.03255 0.04784  229 GLN B CA  
3980 C C   . GLN B 229 ? 0.16955 0.17971 0.36833 -0.01969 -0.03798 0.03864  229 GLN B C   
3981 O O   . GLN B 229 ? 0.18362 0.17906 0.37512 -0.01730 -0.04408 0.03227  229 GLN B O   
3982 C CB  . GLN B 229 ? 0.18242 0.20332 0.41100 -0.02157 -0.03889 0.05705  229 GLN B CB  
3983 C CG  . GLN B 229 ? 0.18943 0.22271 0.42765 -0.02127 -0.03376 0.06892  229 GLN B CG  
3984 C CD  . GLN B 229 ? 0.20240 0.23210 0.46585 -0.02413 -0.03912 0.07963  229 GLN B CD  
3985 O OE1 . GLN B 229 ? 0.21106 0.22550 0.48210 -0.02450 -0.04900 0.07704  229 GLN B OE1 
3986 N NE2 . GLN B 229 ? 0.20287 0.24616 0.48069 -0.02590 -0.03275 0.09164  229 GLN B NE2 
3987 N N   . LEU B 230 ? 0.17642 0.18997 0.37513 -0.02111 -0.03612 0.03790  230 LEU B N   
3988 C CA  . LEU B 230 ? 0.18400 0.18370 0.37493 -0.02034 -0.04204 0.03045  230 LEU B CA  
3989 C C   . LEU B 230 ? 0.19242 0.19118 0.36257 -0.01876 -0.03533 0.02310  230 LEU B C   
3990 O O   . LEU B 230 ? 0.18362 0.19464 0.35192 -0.01982 -0.02749 0.02411  230 LEU B O   
3991 C CB  . LEU B 230 ? 0.17318 0.17616 0.37963 -0.02253 -0.04530 0.03453  230 LEU B CB  
3992 C CG  . LEU B 230 ? 0.16649 0.16869 0.39882 -0.02498 -0.05339 0.04196  230 LEU B CG  
3993 C CD1 . LEU B 230 ? 0.17813 0.18420 0.42643 -0.02672 -0.05639 0.04470  230 LEU B CD1 
3994 C CD2 . LEU B 230 ? 0.17966 0.16291 0.41077 -0.02340 -0.06565 0.03641  230 LEU B CD2 
3995 N N   . THR B 231 ? 0.20182 0.18544 0.35670 -0.01572 -0.03845 0.01592  231 THR B N   
3996 C CA  . THR B 231 ? 0.20121 0.18208 0.33822 -0.01435 -0.03166 0.01035  231 THR B CA  
3997 C C   . THR B 231 ? 0.21179 0.19601 0.34867 -0.01609 -0.02931 0.01038  231 THR B C   
3998 O O   . THR B 231 ? 0.22555 0.20377 0.36751 -0.01585 -0.03627 0.01091  231 THR B O   
3999 C CB  . THR B 231 ? 0.20995 0.17213 0.33021 -0.00946 -0.03583 0.00423  231 THR B CB  
4000 O OG1 . THR B 231 ? 0.19691 0.15647 0.31674 -0.00683 -0.03708 0.00335  231 THR B OG1 
4001 C CG2 . THR B 231 ? 0.21644 0.17541 0.31977 -0.00811 -0.02742 0.00065  231 THR B CG2 
4002 N N   . PRO B 232 ? 0.20640 0.19998 0.33938 -0.01760 -0.02068 0.00941  232 PRO B N   
4003 C CA  . PRO B 232 ? 0.21154 0.20521 0.34223 -0.01829 -0.01868 0.00804  232 PRO B CA  
4004 C C   . PRO B 232 ? 0.21930 0.19511 0.33576 -0.01569 -0.02184 0.00416  232 PRO B C   
4005 O O   . PRO B 232 ? 0.21562 0.18247 0.31847 -0.01372 -0.01894 0.00136  232 PRO B O   
4006 C CB  . PRO B 232 ? 0.20902 0.21313 0.33706 -0.01992 -0.01002 0.00601  232 PRO B CB  
4007 C CG  . PRO B 232 ? 0.20760 0.22279 0.34187 -0.02030 -0.00850 0.00843  232 PRO B CG  
4008 C CD  . PRO B 232 ? 0.21342 0.21892 0.34692 -0.01858 -0.01378 0.00945  232 PRO B CD  
4009 N N   . PHE B 233 ? 0.22088 0.19196 0.34050 -0.01489 -0.02748 0.00458  233 PHE B N   
4010 C CA  . PHE B 233 ? 0.22612 0.17963 0.33058 -0.01128 -0.03157 0.00137  233 PHE B CA  
4011 C C   . PHE B 233 ? 0.23988 0.19007 0.33156 -0.01144 -0.02265 -0.00044 233 PHE B C   
4012 O O   . PHE B 233 ? 0.25925 0.19522 0.33354 -0.00813 -0.02129 -0.00198 233 PHE B O   
4013 C CB  . PHE B 233 ? 0.22362 0.17469 0.33756 -0.01029 -0.04053 0.00231  233 PHE B CB  
4014 C CG  . PHE B 233 ? 0.25789 0.19206 0.35577 -0.00593 -0.04481 -0.00063 233 PHE B CG  
4015 C CD1 . PHE B 233 ? 0.28100 0.19787 0.36513 -0.00075 -0.05395 -0.00355 233 PHE B CD1 
4016 C CD2 . PHE B 233 ? 0.24843 0.18286 0.34357 -0.00604 -0.04028 -0.00067 233 PHE B CD2 
4017 C CE1 . PHE B 233 ? 0.30179 0.20243 0.36827 0.00461  -0.05819 -0.00564 233 PHE B CE1 
4018 C CE2 . PHE B 233 ? 0.27736 0.19535 0.35702 -0.00146 -0.04423 -0.00225 233 PHE B CE2 
4019 C CZ  . PHE B 233 ? 0.30535 0.20664 0.36987 0.00406  -0.05304 -0.00434 233 PHE B CZ  
4020 N N   . GLU B 234 ? 0.23770 0.20020 0.33776 -0.01473 -0.01651 -0.00008 234 GLU B N   
4021 C CA  . GLU B 234 ? 0.22922 0.18990 0.32232 -0.01613 -0.00844 -0.00197 234 GLU B CA  
4022 C C   . GLU B 234 ? 0.22409 0.19574 0.32123 -0.01901 -0.00178 -0.00268 234 GLU B C   
4023 O O   . GLU B 234 ? 0.21330 0.19972 0.32160 -0.02069 -0.00169 -0.00220 234 GLU B O   
4024 C CB  . GLU B 234 ? 0.23499 0.20089 0.33508 -0.01707 -0.00763 -0.00294 234 GLU B CB  
4025 C CG  . GLU B 234 ? 0.25529 0.20877 0.35056 -0.01377 -0.01334 -0.00262 234 GLU B CG  
4026 C CD  . GLU B 234 ? 0.25972 0.22038 0.36503 -0.01347 -0.01364 -0.00350 234 GLU B CD  
4027 O OE1 . GLU B 234 ? 0.25601 0.23166 0.37084 -0.01518 -0.00955 -0.00452 234 GLU B OE1 
4028 O OE2 . GLU B 234 ? 0.26854 0.21929 0.37095 -0.01042 -0.01832 -0.00342 234 GLU B OE2 
4029 N N   . THR B 235 ? 0.23808 0.20314 0.32661 -0.01897 0.00400  -0.00326 235 THR B N   
4030 C CA  . THR B 235 ? 0.23869 0.21497 0.33406 -0.02179 0.01004  -0.00429 235 THR B CA  
4031 C C   . THR B 235 ? 0.23619 0.21667 0.33769 -0.02552 0.01489  -0.00671 235 THR B C   
4032 O O   . THR B 235 ? 0.24746 0.21676 0.34319 -0.02584 0.01845  -0.00624 235 THR B O   
4033 C CB  . THR B 235 ? 0.23892 0.20876 0.32606 -0.01956 0.01454  -0.00337 235 THR B CB  
4034 O OG1 . THR B 235 ? 0.23267 0.21507 0.33019 -0.02249 0.02014  -0.00443 235 THR B OG1 
4035 C CG2 . THR B 235 ? 0.24373 0.19750 0.31660 -0.01721 0.01939  -0.00181 235 THR B CG2 
4036 N N   . TYR B 236 ? 0.22635 0.22193 0.33907 -0.02773 0.01434  -0.00930 236 TYR B N   
4037 C CA  . TYR B 236 ? 0.21873 0.21872 0.33862 -0.03074 0.01652  -0.01356 236 TYR B CA  
4038 C C   . TYR B 236 ? 0.21587 0.22249 0.34427 -0.03390 0.02082  -0.01545 236 TYR B C   
4039 O O   . TYR B 236 ? 0.21842 0.23237 0.35643 -0.03642 0.02021  -0.02031 236 TYR B O   
4040 C CB  . TYR B 236 ? 0.20506 0.21665 0.32984 -0.02945 0.01232  -0.01635 236 TYR B CB  
4041 C CG  . TYR B 236 ? 0.21448 0.22160 0.33538 -0.02642 0.00897  -0.01417 236 TYR B CG  
4042 C CD1 . TYR B 236 ? 0.22684 0.22389 0.34512 -0.02600 0.00886  -0.01594 236 TYR B CD1 
4043 C CD2 . TYR B 236 ? 0.20883 0.22210 0.33129 -0.02407 0.00578  -0.00994 236 TYR B CD2 
4044 C CE1 . TYR B 236 ? 0.24030 0.23473 0.35746 -0.02280 0.00539  -0.01401 236 TYR B CE1 
4045 C CE2 . TYR B 236 ? 0.19792 0.20865 0.32126 -0.02168 0.00267  -0.00766 236 TYR B CE2 
4046 C CZ  . TYR B 236 ? 0.21899 0.22085 0.33971 -0.02072 0.00224  -0.00988 236 TYR B CZ  
4047 O OH  . TYR B 236 ? 0.22676 0.22751 0.35067 -0.01792 -0.00128 -0.00765 236 TYR B OH  
4048 N N   . ARG B 237 ? 0.22372 0.22744 0.34949 -0.03328 0.02480  -0.01222 237 ARG B N   
4049 C CA  . ARG B 237 ? 0.22623 0.23810 0.36298 -0.03579 0.02938  -0.01324 237 ARG B CA  
4050 C C   . ARG B 237 ? 0.23456 0.24068 0.37859 -0.03989 0.03590  -0.01322 237 ARG B C   
4051 O O   . ARG B 237 ? 0.23572 0.25069 0.39473 -0.04309 0.03903  -0.01468 237 ARG B O   
4052 C CB  . ARG B 237 ? 0.21640 0.22703 0.34780 -0.03244 0.03236  -0.00961 237 ARG B CB  
4053 C CG  . ARG B 237 ? 0.22717 0.22221 0.34623 -0.03011 0.03895  -0.00544 237 ARG B CG  
4054 C CD  . ARG B 237 ? 0.22587 0.21631 0.33352 -0.02427 0.03853  -0.00339 237 ARG B CD  
4055 N NE  . ARG B 237 ? 0.21649 0.21418 0.33117 -0.02330 0.04534  -0.00265 237 ARG B NE  
4056 C CZ  . ARG B 237 ? 0.21180 0.20832 0.31992 -0.01778 0.04501  -0.00217 237 ARG B CZ  
4057 N NH1 . ARG B 237 ? 0.22021 0.20847 0.31621 -0.01353 0.03711  -0.00265 237 ARG B NH1 
4058 N NH2 . ARG B 237 ? 0.21598 0.21963 0.33165 -0.01631 0.05243  -0.00141 237 ARG B NH2 
4059 N N   . THR B 238 ? 0.25457 0.24614 0.39032 -0.03988 0.03793  -0.01098 238 THR B N   
4060 C CA  . THR B 238 ? 0.25742 0.24216 0.40151 -0.04407 0.04468  -0.00937 238 THR B CA  
4061 C C   . THR B 238 ? 0.25455 0.24138 0.41115 -0.04821 0.03986  -0.01554 238 THR B C   
4062 O O   . THR B 238 ? 0.27221 0.25236 0.43890 -0.05245 0.04420  -0.01451 238 THR B O   
4063 C CB  . THR B 238 ? 0.25066 0.21649 0.37816 -0.04111 0.05007  -0.00264 238 THR B CB  
4064 O OG1 . THR B 238 ? 0.25886 0.21595 0.37741 -0.03933 0.04350  -0.00431 238 THR B OG1 
4065 C CG2 . THR B 238 ? 0.26493 0.22668 0.37611 -0.03506 0.05276  0.00164  238 THR B CG2 
4066 N N   . MET B 239 ? 0.23780 0.23303 0.39396 -0.04654 0.03133  -0.02166 239 MET B N   
4067 C CA  . MET B 239 ? 0.25395 0.25144 0.42043 -0.04885 0.02612  -0.02923 239 MET B CA  
4068 C C   . MET B 239 ? 0.25704 0.26269 0.44464 -0.05427 0.02678  -0.03305 239 MET B C   
4069 O O   . MET B 239 ? 0.25605 0.27229 0.45024 -0.05486 0.02882  -0.03160 239 MET B O   
4070 C CB  . MET B 239 ? 0.24441 0.25225 0.40545 -0.04444 0.01817  -0.03476 239 MET B CB  
4071 C CG  . MET B 239 ? 0.26083 0.26212 0.40743 -0.03971 0.01652  -0.03207 239 MET B CG  
4072 S SD  . MET B 239 ? 0.25647 0.27273 0.39852 -0.03394 0.01038  -0.03554 239 MET B SD  
4073 C CE  . MET B 239 ? 0.24813 0.26308 0.39412 -0.03266 0.00599  -0.04557 239 MET B CE  
4074 N N   . PRO B 240 ? 0.27565 0.27617 0.47618 -0.05826 0.02455  -0.03803 240 PRO B N   
4075 C CA  . PRO B 240 ? 0.27119 0.28048 0.49591 -0.06370 0.02247  -0.04321 240 PRO B CA  
4076 C C   . PRO B 240 ? 0.26111 0.28698 0.48755 -0.06058 0.01267  -0.05209 240 PRO B C   
4077 O O   . PRO B 240 ? 0.25654 0.28464 0.46820 -0.05489 0.00660  -0.05643 240 PRO B O   
4078 C CB  . PRO B 240 ? 0.27707 0.27429 0.51321 -0.06769 0.01974  -0.04774 240 PRO B CB  
4079 C CG  . PRO B 240 ? 0.30226 0.28295 0.52024 -0.06487 0.02417  -0.04144 240 PRO B CG  
4080 C CD  . PRO B 240 ? 0.28675 0.27230 0.48240 -0.05794 0.02319  -0.03920 240 PRO B CD  
4081 N N   . ARG B 241 ? 0.24721 0.28533 0.49181 -0.06358 0.01144  -0.05418 241 ARG B N   
4082 C CA  . ARG B 241 ? 0.25214 0.30587 0.49796 -0.05980 0.00104  -0.06266 241 ARG B CA  
4083 C C   . ARG B 241 ? 0.25761 0.30879 0.50187 -0.05756 -0.00981 -0.07438 241 ARG B C   
4084 O O   . ARG B 241 ? 0.25739 0.31580 0.48652 -0.05046 -0.01635 -0.07909 241 ARG B O   
4085 C CB  . ARG B 241 ? 0.24630 0.31354 0.51596 -0.06340 -0.00086 -0.06478 241 ARG B CB  
4086 C CG  . ARG B 241 ? 0.24289 0.32313 0.51553 -0.05947 -0.01471 -0.07613 241 ARG B CG  
4087 C CD  . ARG B 241 ? 0.23941 0.33261 0.54003 -0.06329 -0.01962 -0.08042 241 ARG B CD  
4088 N NE  . ARG B 241 ? 0.27206 0.37522 0.57400 -0.06203 -0.01269 -0.07204 241 ARG B NE  
4089 C CZ  . ARG B 241 ? 0.24902 0.36559 0.54670 -0.05641 -0.01939 -0.07433 241 ARG B CZ  
4090 N NH1 . ARG B 241 ? 0.25797 0.38023 0.54934 -0.05138 -0.03282 -0.08438 241 ARG B NH1 
4091 N NH2 . ARG B 241 ? 0.25144 0.37477 0.54942 -0.05477 -0.01273 -0.06652 241 ARG B NH2 
4092 N N   . GLU B 242 ? 0.26090 0.30129 0.51988 -0.06286 -0.01098 -0.07830 242 GLU B N   
4093 C CA  . GLU B 242 ? 0.25116 0.28793 0.51047 -0.06026 -0.02251 -0.09131 242 GLU B CA  
4094 C C   . GLU B 242 ? 0.25693 0.28781 0.48953 -0.05231 -0.02265 -0.09179 242 GLU B C   
4095 O O   . GLU B 242 ? 0.26281 0.29824 0.48508 -0.04521 -0.03156 -0.10163 242 GLU B O   
4096 C CB  . GLU B 242 ? 0.27003 0.29420 0.55330 -0.06828 -0.02335 -0.09429 242 GLU B CB  
4097 C CG  . GLU B 242 ? 0.28709 0.31772 0.59615 -0.07472 -0.02140 -0.09068 242 GLU B CG  
4098 C CD  . GLU B 242 ? 0.27513 0.30601 0.58561 -0.07830 -0.00569 -0.07485 242 GLU B CD  
4099 O OE1 . GLU B 242 ? 0.27643 0.29615 0.57418 -0.07860 0.00371  -0.06665 242 GLU B OE1 
4100 O OE2 . GLU B 242 ? 0.30462 0.34649 0.62805 -0.07987 -0.00307 -0.07104 242 GLU B OE2 
4101 N N   . MET B 243 ? 0.27766 0.29914 0.49861 -0.05247 -0.01291 -0.08120 243 MET B N   
4102 C CA  . MET B 243 ? 0.27832 0.29701 0.47706 -0.04489 -0.01266 -0.08038 243 MET B CA  
4103 C C   . MET B 243 ? 0.26424 0.29794 0.44857 -0.03846 -0.01314 -0.07783 243 MET B C   
4104 O O   . MET B 243 ? 0.28271 0.32049 0.45291 -0.03083 -0.01613 -0.08110 243 MET B O   
4105 C CB  . MET B 243 ? 0.28598 0.29067 0.47780 -0.04661 -0.00383 -0.06996 243 MET B CB  
4106 C CG  . MET B 243 ? 0.29369 0.29554 0.46737 -0.03938 -0.00390 -0.06880 243 MET B CG  
4107 S SD  . MET B 243 ? 0.31377 0.29976 0.47927 -0.04063 0.00412  -0.05694 243 MET B SD  
4108 C CE  . MET B 243 ? 0.32666 0.29426 0.50484 -0.04575 0.00406  -0.05984 243 MET B CE  
4109 N N   . VAL B 244 ? 0.27647 0.31841 0.46486 -0.04097 -0.00965 -0.07145 244 VAL B N   
4110 C CA  . VAL B 244 ? 0.26017 0.31500 0.43687 -0.03539 -0.01001 -0.06770 244 VAL B CA  
4111 C C   . VAL B 244 ? 0.25400 0.32113 0.42857 -0.02974 -0.01931 -0.07719 244 VAL B C   
4112 O O   . VAL B 244 ? 0.22766 0.30214 0.38682 -0.02204 -0.02050 -0.07629 244 VAL B O   
4113 C CB  . VAL B 244 ? 0.24503 0.30373 0.42782 -0.03913 -0.00450 -0.05940 244 VAL B CB  
4114 C CG1 . VAL B 244 ? 0.22561 0.29794 0.40089 -0.03391 -0.00679 -0.05684 244 VAL B CG1 
4115 C CG2 . VAL B 244 ? 0.24253 0.28899 0.41913 -0.04119 0.00394  -0.04992 244 VAL B CG2 
4116 N N   . GLU B 245 ? 0.26784 0.33730 0.45807 -0.03294 -0.02622 -0.08617 245 GLU B N   
4117 C CA  . GLU B 245 ? 0.26390 0.34517 0.45194 -0.02699 -0.03685 -0.09575 245 GLU B CA  
4118 C C   . GLU B 245 ? 0.25744 0.33601 0.43208 -0.01904 -0.04395 -0.10637 245 GLU B C   
4119 O O   . GLU B 245 ? 0.27693 0.36491 0.44239 -0.01116 -0.05241 -0.11376 245 GLU B O   
4120 C CB  . GLU B 245 ? 0.24372 0.32894 0.45635 -0.03317 -0.04339 -0.10232 245 GLU B CB  
4121 C CG  . GLU B 245 ? 0.24729 0.34077 0.46987 -0.03714 -0.03753 -0.09292 245 GLU B CG  
4122 C CD  . GLU B 245 ? 0.24126 0.34435 0.48750 -0.04054 -0.04550 -0.09963 245 GLU B CD  
4123 O OE1 . GLU B 245 ? 0.26408 0.36373 0.52599 -0.04359 -0.05393 -0.11033 245 GLU B OE1 
4124 O OE2 . GLU B 245 ? 0.23462 0.34855 0.48539 -0.03999 -0.04408 -0.09453 245 GLU B OE2 
4125 N N   . SER B 246 ? 0.25857 0.32444 0.43018 -0.01956 -0.04090 -0.10742 246 SER B N   
4126 C CA  . SER B 246 ? 0.28194 0.34559 0.43838 -0.01012 -0.04614 -0.11687 246 SER B CA  
4127 C C   . SER B 246 ? 0.28379 0.35176 0.41936 -0.00223 -0.03816 -0.10812 246 SER B C   
4128 O O   . SER B 246 ? 0.29783 0.36442 0.42010 0.00653  -0.03962 -0.11397 246 SER B O   
4129 C CB  . SER B 246 ? 0.27122 0.31841 0.43818 -0.01396 -0.04901 -0.12482 246 SER B CB  
4130 O OG  . SER B 246 ? 0.27725 0.31344 0.44641 -0.01926 -0.03902 -0.11455 246 SER B OG  
4131 N N   . MET B 247 ? 0.27647 0.34982 0.41041 -0.00476 -0.03000 -0.09451 247 MET B N   
4132 C CA  . MET B 247 ? 0.26799 0.34827 0.38645 0.00234  -0.02353 -0.08550 247 MET B CA  
4133 C C   . MET B 247 ? 0.26719 0.36250 0.37395 0.01053  -0.02646 -0.08520 247 MET B C   
4134 O O   . MET B 247 ? 0.27512 0.37570 0.38653 0.00959  -0.03330 -0.09012 247 MET B O   
4135 C CB  . MET B 247 ? 0.25611 0.33373 0.37918 -0.00380 -0.01505 -0.07153 247 MET B CB  
4136 C CG  . MET B 247 ? 0.25846 0.32101 0.38873 -0.01001 -0.01163 -0.06996 247 MET B CG  
4137 S SD  . MET B 247 ? 0.25700 0.31665 0.38734 -0.01374 -0.00388 -0.05510 247 MET B SD  
4138 C CE  . MET B 247 ? 0.25374 0.30597 0.39619 -0.02315 -0.00286 -0.05386 247 MET B CE  
4139 N N   . THR B 248 ? 0.26649 0.36902 0.35883 0.01898  -0.02096 -0.07854 248 THR B N   
4140 C CA  . THR B 248 ? 0.26059 0.37699 0.34053 0.02705  -0.02115 -0.07397 248 THR B CA  
4141 C C   . THR B 248 ? 0.24625 0.36657 0.33453 0.02071  -0.01741 -0.06139 248 THR B C   
4142 O O   . THR B 248 ? 0.23666 0.34941 0.33711 0.01173  -0.01338 -0.05557 248 THR B O   
4143 C CB  . THR B 248 ? 0.25909 0.38236 0.32325 0.03797  -0.01415 -0.06844 248 THR B CB  
4144 O OG1 . THR B 248 ? 0.24202 0.36206 0.31448 0.03313  -0.00511 -0.05693 248 THR B OG1 
4145 C CG2 . THR B 248 ? 0.25148 0.37108 0.30510 0.04639  -0.01812 -0.08202 248 THR B CG2 
4146 N N   . VAL B 249 ? 0.24651 0.37793 0.32667 0.02651  -0.01914 -0.05730 249 VAL B N   
4147 C CA  . VAL B 249 ? 0.23912 0.37400 0.32627 0.02206  -0.01572 -0.04500 249 VAL B CA  
4148 C C   . VAL B 249 ? 0.23132 0.36392 0.32129 0.01984  -0.00616 -0.03174 249 VAL B C   
4149 O O   . VAL B 249 ? 0.21724 0.34523 0.31816 0.01256  -0.00381 -0.02450 249 VAL B O   
4150 C CB  . VAL B 249 ? 0.24771 0.39448 0.32377 0.03043  -0.01910 -0.04180 249 VAL B CB  
4151 C CG1 . VAL B 249 ? 0.23223 0.38108 0.31662 0.02612  -0.01588 -0.02903 249 VAL B CG1 
4152 C CG2 . VAL B 249 ? 0.26290 0.41200 0.33803 0.03282  -0.03081 -0.05593 249 VAL B CG2 
4153 N N   . LEU B 250 ? 0.22270 0.35877 0.30360 0.02675  -0.00098 -0.02876 250 LEU B N   
4154 C CA  . LEU B 250 ? 0.19790 0.33320 0.28520 0.02478  0.00717  -0.01643 250 LEU B CA  
4155 C C   . LEU B 250 ? 0.20680 0.32882 0.30685 0.01523  0.00712  -0.01832 250 LEU B C   
4156 O O   . LEU B 250 ? 0.19625 0.31442 0.30583 0.00982  0.00959  -0.00928 250 LEU B O   
4157 C CB  . LEU B 250 ? 0.21422 0.35697 0.29151 0.03463  0.01321  -0.01408 250 LEU B CB  
4158 C CG  . LEU B 250 ? 0.19648 0.34123 0.28352 0.03372  0.02174  -0.00128 250 LEU B CG  
4159 C CD1 . LEU B 250 ? 0.19831 0.34570 0.29543 0.02919  0.02391  0.01285  250 LEU B CD1 
4160 C CD2 . LEU B 250 ? 0.20309 0.35895 0.27941 0.04560  0.02906  0.00174  250 LEU B CD2 
4161 N N   . GLY B 251 ? 0.21740 0.33122 0.31734 0.01356  0.00372  -0.02999 251 GLY B N   
4162 C CA  . GLY B 251 ? 0.20117 0.30141 0.31085 0.00552  0.00402  -0.03094 251 GLY B CA  
4163 C C   . GLY B 251 ? 0.19856 0.29266 0.31659 -0.00268 0.00244  -0.02881 251 GLY B C   
4164 O O   . GLY B 251 ? 0.18835 0.27377 0.31191 -0.00756 0.00450  -0.02343 251 GLY B O   
4165 N N   . GLN B 252 ? 0.20622 0.30464 0.32510 -0.00343 -0.00163 -0.03363 252 GLN B N   
4166 C CA  . GLN B 252 ? 0.18721 0.28134 0.31494 -0.01014 -0.00214 -0.03199 252 GLN B CA  
4167 C C   . GLN B 252 ? 0.17919 0.27508 0.30806 -0.01047 0.00061  -0.02074 252 GLN B C   
4168 O O   . GLN B 252 ? 0.18262 0.27047 0.31674 -0.01529 0.00198  -0.01766 252 GLN B O   
4169 C CB  . GLN B 252 ? 0.21977 0.32088 0.35099 -0.00994 -0.00762 -0.03930 252 GLN B CB  
4170 C CG  . GLN B 252 ? 0.22356 0.32171 0.35796 -0.01068 -0.01259 -0.05191 252 GLN B CG  
4171 C CD  . GLN B 252 ? 0.22672 0.33297 0.36773 -0.01035 -0.02005 -0.05959 252 GLN B CD  
4172 O OE1 . GLN B 252 ? 0.22344 0.33835 0.36491 -0.00862 -0.02129 -0.05537 252 GLN B OE1 
4173 N NE2 . GLN B 252 ? 0.24411 0.34713 0.39182 -0.01186 -0.02599 -0.07113 252 GLN B NE2 
4174 N N   . ARG B 253 ? 0.17488 0.28060 0.29870 -0.00481 0.00149  -0.01430 253 ARG B N   
4175 C CA  . ARG B 253 ? 0.17943 0.28552 0.30713 -0.00551 0.00346  -0.00314 253 ARG B CA  
4176 C C   . ARG B 253 ? 0.17039 0.26732 0.30256 -0.00840 0.00593  0.00174  253 ARG B C   
4177 O O   . ARG B 253 ? 0.17307 0.26297 0.31069 -0.01173 0.00531  0.00667  253 ARG B O   
4178 C CB  . ARG B 253 ? 0.18500 0.30372 0.30751 0.00131  0.00463  0.00417  253 ARG B CB  
4179 C CG  . ARG B 253 ? 0.18958 0.31682 0.30640 0.00525  0.00032  -0.00056 253 ARG B CG  
4180 C CD  . ARG B 253 ? 0.21090 0.35011 0.31811 0.01394  0.00174  0.00691  253 ARG B CD  
4181 N NE  . ARG B 253 ? 0.22697 0.36701 0.34029 0.01338  0.00461  0.02070  253 ARG B NE  
4182 C CZ  . ARG B 253 ? 0.23534 0.37700 0.35208 0.01452  0.01048  0.03196  253 ARG B CZ  
4183 N NH1 . ARG B 253 ? 0.25463 0.39890 0.36807 0.01732  0.01503  0.03158  253 ARG B NH1 
4184 N NH2 . ARG B 253 ? 0.21408 0.35470 0.33991 0.01285  0.01163  0.04393  253 ARG B NH2 
4185 N N   . MET B 254 ? 0.18131 0.27758 0.31129 -0.00648 0.00775  -0.00045 254 MET B N   
4186 C CA  . MET B 254 ? 0.17736 0.26493 0.31277 -0.00886 0.00865  0.00316  254 MET B CA  
4187 C C   . MET B 254 ? 0.18245 0.25513 0.31840 -0.01432 0.00651  -0.00117 254 MET B C   
4188 O O   . MET B 254 ? 0.18810 0.25221 0.32759 -0.01657 0.00508  0.00317  254 MET B O   
4189 C CB  . MET B 254 ? 0.17661 0.26666 0.31010 -0.00490 0.01097  0.00070  254 MET B CB  
4190 C CG  . MET B 254 ? 0.17933 0.28421 0.31166 0.00215  0.01541  0.00678  254 MET B CG  
4191 S SD  . MET B 254 ? 0.13548 0.24721 0.28061 0.00195  0.01843  0.02271  254 MET B SD  
4192 C CE  . MET B 254 ? 0.18867 0.31037 0.32714 0.00499  0.01901  0.02718  254 MET B CE  
4193 N N   . LEU B 255 ? 0.16975 0.23877 0.30242 -0.01606 0.00611  -0.00951 255 LEU B N   
4194 C CA  . LEU B 255 ? 0.19217 0.24732 0.32476 -0.02055 0.00616  -0.01208 255 LEU B CA  
4195 C C   . LEU B 255 ? 0.18753 0.24155 0.32180 -0.02291 0.00632  -0.01073 255 LEU B C   
4196 O O   . LEU B 255 ? 0.19604 0.24088 0.32982 -0.02583 0.00808  -0.01300 255 LEU B O   
4197 C CB  . LEU B 255 ? 0.18887 0.23934 0.32067 -0.02194 0.00652  -0.02025 255 LEU B CB  
4198 C CG  . LEU B 255 ? 0.20878 0.25906 0.33842 -0.01858 0.00618  -0.02319 255 LEU B CG  
4199 C CD1 . LEU B 255 ? 0.21295 0.25480 0.34329 -0.02060 0.00563  -0.03127 255 LEU B CD1 
4200 C CD2 . LEU B 255 ? 0.19068 0.23467 0.32030 -0.01748 0.00638  -0.01740 255 LEU B CD2 
4201 N N   . GLY B 256 ? 0.18065 0.24361 0.31707 -0.02110 0.00521  -0.00640 256 GLY B N   
4202 C CA  . GLY B 256 ? 0.17926 0.23972 0.31754 -0.02220 0.00507  -0.00439 256 GLY B CA  
4203 C C   . GLY B 256 ? 0.19238 0.25875 0.33438 -0.02333 0.00581  -0.00923 256 GLY B C   
4204 O O   . GLY B 256 ? 0.18494 0.24824 0.32912 -0.02408 0.00710  -0.00850 256 GLY B O   
4205 N N   . TRP B 257 ? 0.19193 0.26702 0.33558 -0.02283 0.00449  -0.01465 257 TRP B N   
4206 C CA  . TRP B 257 ? 0.18631 0.26740 0.33733 -0.02441 0.00364  -0.02022 257 TRP B CA  
4207 C C   . TRP B 257 ? 0.18657 0.28087 0.33945 -0.02068 -0.00019 -0.01932 257 TRP B C   
4208 O O   . TRP B 257 ? 0.18830 0.28963 0.34909 -0.02131 -0.00261 -0.02448 257 TRP B O   
4209 C CB  . TRP B 257 ? 0.19058 0.27155 0.34423 -0.02614 0.00222  -0.02840 257 TRP B CB  
4210 C CG  . TRP B 257 ? 0.20052 0.26801 0.35563 -0.03054 0.00639  -0.02916 257 TRP B CG  
4211 C CD1 . TRP B 257 ? 0.19333 0.25038 0.34112 -0.03034 0.00802  -0.02718 257 TRP B CD1 
4212 C CD2 . TRP B 257 ? 0.20579 0.26884 0.37087 -0.03530 0.00994  -0.03101 257 TRP B CD2 
4213 N NE1 . TRP B 257 ? 0.19914 0.24435 0.34928 -0.03424 0.01188  -0.02769 257 TRP B NE1 
4214 C CE2 . TRP B 257 ? 0.21262 0.26138 0.37356 -0.03749 0.01396  -0.02943 257 TRP B CE2 
4215 C CE3 . TRP B 257 ? 0.21533 0.28581 0.39396 -0.03766 0.01044  -0.03320 257 TRP B CE3 
4216 C CZ2 . TRP B 257 ? 0.21112 0.25215 0.37948 -0.04184 0.01956  -0.02883 257 TRP B CZ2 
4217 C CZ3 . TRP B 257 ? 0.20668 0.27089 0.39553 -0.04248 0.01630  -0.03287 257 TRP B CZ3 
4218 C CH2 . TRP B 257 ? 0.22287 0.27217 0.40582 -0.04448 0.02133  -0.03016 257 TRP B CH2 
4219 N N   . ARG B 258 ? 0.18734 0.28520 0.33464 -0.01674 -0.00102 -0.01233 258 ARG B N   
4220 C CA  . ARG B 258 ? 0.17617 0.28548 0.32326 -0.01220 -0.00444 -0.00969 258 ARG B CA  
4221 C C   . ARG B 258 ? 0.17656 0.28280 0.32486 -0.01120 -0.00357 -0.00043 258 ARG B C   
4222 O O   . ARG B 258 ? 0.19204 0.28800 0.34019 -0.01335 -0.00136 0.00353  258 ARG B O   
4223 C CB  . ARG B 258 ? 0.17362 0.29180 0.31165 -0.00659 -0.00634 -0.00950 258 ARG B CB  
4224 C CG  . ARG B 258 ? 0.18165 0.30237 0.31803 -0.00620 -0.00941 -0.02043 258 ARG B CG  
4225 C CD  . ARG B 258 ? 0.19704 0.32894 0.32299 0.00185  -0.01370 -0.02264 258 ARG B CD  
4226 N NE  . ARG B 258 ? 0.21744 0.35060 0.34375 0.00231  -0.01939 -0.03563 258 ARG B NE  
4227 C CZ  . ARG B 258 ? 0.21306 0.35484 0.33788 0.00685  -0.02741 -0.04273 258 ARG B CZ  
4228 N NH1 . ARG B 258 ? 0.21959 0.37020 0.33968 0.01241  -0.03012 -0.03745 258 ARG B NH1 
4229 N NH2 . ARG B 258 ? 0.21435 0.35513 0.34306 0.00610  -0.03384 -0.05560 258 ARG B NH2 
4230 N N   . THR B 259 ? 0.17449 0.28900 0.32444 -0.00748 -0.00653 0.00243  259 THR B N   
4231 C CA  . THR B 259 ? 0.18619 0.29818 0.33811 -0.00562 -0.00685 0.01161  259 THR B CA  
4232 C C   . THR B 259 ? 0.18709 0.30124 0.33447 -0.00298 -0.00563 0.02070  259 THR B C   
4233 O O   . THR B 259 ? 0.19401 0.31664 0.33434 0.00048  -0.00519 0.02032  259 THR B O   
4234 C CB  . THR B 259 ? 0.18318 0.30335 0.33892 -0.00187 -0.01061 0.01188  259 THR B CB  
4235 O OG1 . THR B 259 ? 0.20568 0.32322 0.36953 -0.00448 -0.01007 0.00556  259 THR B OG1 
4236 C CG2 . THR B 259 ? 0.17741 0.29578 0.33447 0.00131  -0.01174 0.02249  259 THR B CG2 
4237 N N   . MET B 260 ? 0.19748 0.30374 0.34969 -0.00427 -0.00502 0.02869  260 MET B N   
4238 C CA  . MET B 260 ? 0.19884 0.30669 0.35210 -0.00317 -0.00277 0.03850  260 MET B CA  
4239 C C   . MET B 260 ? 0.19571 0.30159 0.35661 -0.00179 -0.00439 0.04954  260 MET B C   
4240 O O   . MET B 260 ? 0.19612 0.29758 0.36035 -0.00147 -0.00776 0.04852  260 MET B O   
4241 C CB  . MET B 260 ? 0.18916 0.28790 0.34541 -0.00741 -0.00130 0.03720  260 MET B CB  
4242 C CG  . MET B 260 ? 0.18825 0.28604 0.33794 -0.00904 0.00007  0.02663  260 MET B CG  
4243 S SD  . MET B 260 ? 0.16552 0.27670 0.30653 -0.00419 0.00289  0.02505  260 MET B SD  
4244 C CE  . MET B 260 ? 0.17881 0.28927 0.32536 -0.00422 0.00687  0.03389  260 MET B CE  
4245 N N   . LYS B 261 ? 0.20452 0.31357 0.36990 -0.00079 -0.00158 0.06070  261 LYS B N   
4246 C CA  . LYS B 261 ? 0.22105 0.32966 0.39509 0.00086  -0.00240 0.07342  261 LYS B CA  
4247 C C   . LYS B 261 ? 0.21600 0.32010 0.40449 -0.00255 -0.00082 0.08337  261 LYS B C   
4248 O O   . LYS B 261 ? 0.21721 0.33056 0.40691 -0.00081 0.00518  0.09131  261 LYS B O   
4249 C CB  . LYS B 261 ? 0.23163 0.35364 0.39642 0.00792  0.00028  0.08022  261 LYS B CB  
4250 C CG  . LYS B 261 ? 0.24712 0.36960 0.41964 0.01066  0.00077  0.09596  261 LYS B CG  
4251 C CD  . LYS B 261 ? 0.24500 0.35967 0.42225 0.01080  -0.00578 0.09440  261 LYS B CD  
4252 C CE  . LYS B 261 ? 0.28040 0.39603 0.46362 0.01465  -0.00528 0.11060  261 LYS B CE  
4253 N NZ  . LYS B 261 ? 0.27926 0.38890 0.48030 0.01036  -0.00269 0.12368  261 LYS B NZ  
4254 N N   . PRO B 262 ? 0.21511 0.30539 0.41564 -0.00679 -0.00636 0.08304  262 PRO B N   
4255 C CA  . PRO B 262 ? 0.22899 0.31532 0.44859 -0.00975 -0.00706 0.09466  262 PRO B CA  
4256 C C   . PRO B 262 ? 0.25137 0.34553 0.47733 -0.00646 -0.00339 0.11042  262 PRO B C   
4257 O O   . PRO B 262 ? 0.26425 0.36219 0.48033 -0.00190 -0.00345 0.11116  262 PRO B O   
4258 C CB  . PRO B 262 ? 0.22306 0.29132 0.45075 -0.01304 -0.01635 0.08875  262 PRO B CB  
4259 C CG  . PRO B 262 ? 0.19741 0.26114 0.40863 -0.01220 -0.01783 0.07369  262 PRO B CG  
4260 C CD  . PRO B 262 ? 0.21774 0.29538 0.41566 -0.00821 -0.01246 0.07233  262 PRO B CD  
4261 N N   . SER B 263 ? 0.23877 0.33588 0.48240 -0.00846 0.00009  0.12395  263 SER B N   
4262 C CA  . SER B 263 ? 0.23819 0.34172 0.48940 -0.00538 0.00479  0.14150  263 SER B CA  
4263 C C   . SER B 263 ? 0.25998 0.35005 0.52101 -0.00654 -0.00347 0.14397  263 SER B C   
4264 O O   . SER B 263 ? 0.27098 0.34618 0.53805 -0.01034 -0.01266 0.13397  263 SER B O   
4265 C CB  . SER B 263 ? 0.24412 0.35426 0.51658 -0.00785 0.01149  0.15688  263 SER B CB  
4266 O OG  . SER B 263 ? 0.25715 0.38421 0.51723 -0.00250 0.02276  0.16101  263 SER B OG  
4267 N N   . ASP B 264 ? 0.27169 0.36641 0.53249 -0.00204 -0.00024 0.15724  264 ASP B N   
4268 C CA  . ASP B 264 ? 0.28059 0.36224 0.55164 -0.00232 -0.00797 0.16064  264 ASP B CA  
4269 C C   . ASP B 264 ? 0.27637 0.34393 0.57620 -0.00968 -0.01442 0.16493  264 ASP B C   
4270 O O   . ASP B 264 ? 0.28350 0.35598 0.60042 -0.01364 -0.00986 0.17451  264 ASP B O   
4271 C CB  . ASP B 264 ? 0.31220 0.40140 0.57997 0.00398  -0.00260 0.17736  264 ASP B CB  
4272 C CG  . ASP B 264 ? 0.34201 0.44450 0.58110 0.01214  0.00128  0.17169  264 ASP B CG  
4273 O OD1 . ASP B 264 ? 0.37765 0.49397 0.60534 0.01525  0.00991  0.17455  264 ASP B OD1 
4274 O OD2 . ASP B 264 ? 0.33653 0.43557 0.56520 0.01568  -0.00503 0.16289  264 ASP B OD2 
4275 N N   . PRO B 265 ? 0.28605 0.33583 0.59316 -0.01113 -0.02570 0.15767  265 PRO B N   
4276 C CA  . PRO B 265 ? 0.27682 0.31935 0.57163 -0.00609 -0.03130 0.15020  265 PRO B CA  
4277 C C   . PRO B 265 ? 0.31159 0.35569 0.58272 -0.00304 -0.03260 0.13098  265 PRO B C   
4278 O O   . PRO B 265 ? 0.30826 0.34844 0.57188 0.00157  -0.03635 0.12574  265 PRO B O   
4279 C CB  . PRO B 265 ? 0.25922 0.28058 0.57497 -0.00931 -0.04299 0.14914  265 PRO B CB  
4280 C CG  . PRO B 265 ? 0.27908 0.29506 0.60772 -0.01585 -0.04655 0.14446  265 PRO B CG  
4281 C CD  . PRO B 265 ? 0.27351 0.30797 0.60542 -0.01779 -0.03484 0.15646  265 PRO B CD  
4282 N N   . ASN B 266 ? 0.28737 0.33676 0.54785 -0.00509 -0.02966 0.12052  266 ASN B N   
4283 C CA  . ASN B 266 ? 0.27404 0.32781 0.51375 -0.00183 -0.02879 0.10592  266 ASN B CA  
4284 C C   . ASN B 266 ? 0.27866 0.34853 0.50628 0.00371  -0.02297 0.11150  266 ASN B C   
4285 O O   . ASN B 266 ? 0.29143 0.37439 0.51170 0.00446  -0.01611 0.11524  266 ASN B O   
4286 C CB  . ASN B 266 ? 0.25118 0.30675 0.48267 -0.00512 -0.02649 0.09511  266 ASN B CB  
4287 C CG  . ASN B 266 ? 0.24874 0.30918 0.46230 -0.00252 -0.02477 0.08172  266 ASN B CG  
4288 O OD1 . ASN B 266 ? 0.25102 0.32476 0.45507 0.00098  -0.02073 0.08247  266 ASN B OD1 
4289 N ND2 . ASN B 266 ? 0.24793 0.29753 0.45718 -0.00383 -0.02802 0.06958  266 ASN B ND2 
4290 N N   . ILE B 267 ? 0.27968 0.34833 0.50450 0.00865  -0.02641 0.11144  267 ILE B N   
4291 C CA  . ILE B 267 ? 0.27971 0.36218 0.49351 0.01519  -0.02333 0.11732  267 ILE B CA  
4292 C C   . ILE B 267 ? 0.26434 0.35550 0.46328 0.01824  -0.02395 0.10289  267 ILE B C   
4293 O O   . ILE B 267 ? 0.27183 0.37408 0.46128 0.02436  -0.02385 0.10499  267 ILE B O   
4294 C CB  . ILE B 267 ? 0.27007 0.34713 0.49161 0.01969  -0.02727 0.12838  267 ILE B CB  
4295 C CG1 . ILE B 267 ? 0.25698 0.32374 0.48090 0.02149  -0.03469 0.11684  267 ILE B CG1 
4296 C CG2 . ILE B 267 ? 0.26417 0.33250 0.50448 0.01608  -0.02668 0.14442  267 ILE B CG2 
4297 C CD1 . ILE B 267 ? 0.25654 0.32204 0.48304 0.02841  -0.03875 0.12463  267 ILE B CD1 
4298 N N   . VAL B 268 ? 0.24967 0.33605 0.44707 0.01448  -0.02491 0.08878  268 VAL B N   
4299 C CA  . VAL B 268 ? 0.24158 0.33586 0.42969 0.01620  -0.02499 0.07567  268 VAL B CA  
4300 C C   . VAL B 268 ? 0.25142 0.35244 0.43119 0.01279  -0.02052 0.06882  268 VAL B C   
4301 O O   . VAL B 268 ? 0.26056 0.37419 0.43119 0.01569  -0.01935 0.06625  268 VAL B O   
4302 C CB  . VAL B 268 ? 0.23387 0.31793 0.42662 0.01588  -0.02822 0.06546  268 VAL B CB  
4303 C CG1 . VAL B 268 ? 0.20839 0.30113 0.39567 0.01610  -0.02648 0.05274  268 VAL B CG1 
4304 C CG2 . VAL B 268 ? 0.24091 0.31969 0.44107 0.02104  -0.03321 0.07091  268 VAL B CG2 
4305 N N   . GLY B 269 ? 0.23670 0.32865 0.41927 0.00733  -0.01905 0.06544  269 GLY B N   
4306 C CA  . GLY B 269 ? 0.21564 0.31093 0.39149 0.00404  -0.01546 0.05781  269 GLY B CA  
4307 C C   . GLY B 269 ? 0.19861 0.28076 0.37627 -0.00013 -0.01625 0.04951  269 GLY B C   
4308 O O   . GLY B 269 ? 0.20415 0.27430 0.38748 -0.00008 -0.01983 0.04993  269 GLY B O   
4309 N N   . ILE B 270 ? 0.18522 0.26846 0.35682 -0.00294 -0.01327 0.04168  270 ILE B N   
4310 C CA  . ILE B 270 ? 0.19089 0.26156 0.36082 -0.00583 -0.01328 0.03424  270 ILE B CA  
4311 C C   . ILE B 270 ? 0.18575 0.26137 0.34923 -0.00755 -0.00937 0.02534  270 ILE B C   
4312 O O   . ILE B 270 ? 0.18272 0.26971 0.34367 -0.00728 -0.00782 0.02456  270 ILE B O   
4313 C CB  . ILE B 270 ? 0.19596 0.25655 0.36931 -0.00873 -0.01502 0.03810  270 ILE B CB  
4314 C CG1 . ILE B 270 ? 0.18602 0.22965 0.35828 -0.00879 -0.01886 0.03300  270 ILE B CG1 
4315 C CG2 . ILE B 270 ? 0.19968 0.26409 0.36855 -0.01136 -0.01146 0.03569  270 ILE B CG2 
4316 C CD1 . ILE B 270 ? 0.18944 0.22229 0.36946 -0.01063 -0.02435 0.03745  270 ILE B CD1 
4317 N N   . ASN B 271 ? 0.18141 0.24759 0.34198 -0.00873 -0.00787 0.01869  271 ASN B N   
4318 C CA  . ASN B 271 ? 0.18435 0.25303 0.34143 -0.01102 -0.00354 0.01136  271 ASN B CA  
4319 C C   . ASN B 271 ? 0.16798 0.25000 0.33019 -0.00971 -0.00293 0.00808  271 ASN B C   
4320 O O   . ASN B 271 ? 0.16776 0.25924 0.33021 -0.01089 -0.00278 0.00510  271 ASN B O   
4321 C CB  . ASN B 271 ? 0.17765 0.24794 0.33114 -0.01381 -0.00236 0.01101  271 ASN B CB  
4322 C CG  . ASN B 271 ? 0.17776 0.24481 0.32806 -0.01673 0.00160  0.00403  271 ASN B CG  
4323 O OD1 . ASN B 271 ? 0.18989 0.24834 0.33819 -0.01705 0.00435  0.00136  271 ASN B OD1 
4324 N ND2 . ASN B 271 ? 0.17336 0.24674 0.32278 -0.01820 0.00224  0.00140  271 ASN B ND2 
4325 N N   . LEU B 272 ? 0.16160 0.24430 0.32863 -0.00671 -0.00347 0.00784  272 LEU B N   
4326 C CA  . LEU B 272 ? 0.16279 0.25898 0.33775 -0.00487 -0.00427 0.00497  272 LEU B CA  
4327 C C   . LEU B 272 ? 0.18049 0.27452 0.36130 -0.00375 -0.00007 0.00094  272 LEU B C   
4328 O O   . LEU B 272 ? 0.18996 0.27119 0.36542 -0.00278 0.00293  0.00103  272 LEU B O   
4329 C CB  . LEU B 272 ? 0.17155 0.27445 0.34838 -0.00034 -0.00972 0.01102  272 LEU B CB  
4330 C CG  . LEU B 272 ? 0.17658 0.26917 0.35456 0.00284  -0.01150 0.01599  272 LEU B CG  
4331 C CD1 . LEU B 272 ? 0.19254 0.29060 0.37861 0.00747  -0.01274 0.01415  272 LEU B CD1 
4332 C CD2 . LEU B 272 ? 0.18311 0.27380 0.35944 0.00401  -0.01520 0.02547  272 LEU B CD2 
4333 N N   . ILE B 273 ? 0.16334 0.27024 0.35542 -0.00317 0.00015  -0.00283 273 ILE B N   
4334 C CA  . ILE B 273 ? 0.18839 0.29606 0.38911 -0.00187 0.00598  -0.00587 273 ILE B CA  
4335 C C   . ILE B 273 ? 0.17113 0.29559 0.38782 0.00030  0.00270  -0.00823 273 ILE B C   
4336 O O   . ILE B 273 ? 0.16470 0.29973 0.38509 -0.00088 -0.00326 -0.01003 273 ILE B O   
4337 C CB  . ILE B 273 ? 0.19725 0.30025 0.39780 -0.00670 0.01400  -0.00903 273 ILE B CB  
4338 C CG1 . ILE B 273 ? 0.19678 0.29868 0.40360 -0.00412 0.02286  -0.00994 273 ILE B CG1 
4339 C CG2 . ILE B 273 ? 0.19438 0.30836 0.40465 -0.01190 0.01231  -0.01315 273 ILE B CG2 
4340 C CD1 . ILE B 273 ? 0.17936 0.26601 0.37217 0.00176  0.02522  -0.00787 273 ILE B CD1 
4341 N N   . ASP B 274 ? 0.17555 0.30240 0.40132 0.00448  0.00612  -0.00872 274 ASP B N   
4342 C CA  . ASP B 274 ? 0.16633 0.30932 0.40959 0.00770  0.00239  -0.01069 274 ASP B CA  
4343 C C   . ASP B 274 ? 0.17044 0.31791 0.40974 0.01177  -0.00816 -0.00743 274 ASP B C   
4344 O O   . ASP B 274 ? 0.17024 0.33202 0.42033 0.01354  -0.01462 -0.00969 274 ASP B O   
4345 C CB  . ASP B 274 ? 0.15436 0.31074 0.41461 0.00246  0.00325  -0.01614 274 ASP B CB  
4346 C CG  . ASP B 274 ? 0.18769 0.34080 0.45496 -0.00104 0.01520  -0.01724 274 ASP B CG  
4347 O OD1 . ASP B 274 ? 0.18404 0.32986 0.44714 0.00341  0.02269  -0.01485 274 ASP B OD1 
4348 O OD2 . ASP B 274 ? 0.20736 0.36428 0.48363 -0.00754 0.01724  -0.02025 274 ASP B OD2 
4349 N N   . ASP B 275 ? 0.17420 0.30916 0.39862 0.01357  -0.01017 -0.00165 275 ASP B N   
4350 C CA  . ASP B 275 ? 0.16767 0.30448 0.38599 0.01702  -0.01823 0.00424  275 ASP B CA  
4351 C C   . ASP B 275 ? 0.18619 0.33351 0.40137 0.01504  -0.02284 0.00266  275 ASP B C   
4352 O O   . ASP B 275 ? 0.19714 0.35101 0.40868 0.01959  -0.02960 0.00646  275 ASP B O   
4353 C CB  . ASP B 275 ? 0.18050 0.32301 0.40779 0.02433  -0.02297 0.00633  275 ASP B CB  
4354 C CG  . ASP B 275 ? 0.19896 0.33349 0.41791 0.02844  -0.02802 0.01550  275 ASP B CG  
4355 O OD1 . ASP B 275 ? 0.21438 0.33866 0.42266 0.02521  -0.02687 0.02027  275 ASP B OD1 
4356 O OD2 . ASP B 275 ? 0.20742 0.34603 0.43224 0.03487  -0.03312 0.01850  275 ASP B OD2 
4357 N N   . LYS B 276 ? 0.18517 0.33327 0.40050 0.00917  -0.01940 -0.00299 276 LYS B N   
4358 C CA  . LYS B 276 ? 0.17688 0.33300 0.38843 0.00773  -0.02401 -0.00663 276 LYS B CA  
4359 C C   . LYS B 276 ? 0.16663 0.31285 0.36522 0.00338  -0.01998 -0.00534 276 LYS B C   
4360 O O   . LYS B 276 ? 0.16218 0.29662 0.35819 0.00000  -0.01366 -0.00389 276 LYS B O   
4361 C CB  . LYS B 276 ? 0.18105 0.34808 0.40911 0.00469  -0.02540 -0.01606 276 LYS B CB  
4362 C CG  . LYS B 276 ? 0.19083 0.37139 0.43435 0.00947  -0.03178 -0.01840 276 LYS B CG  
4363 C CD  . LYS B 276 ? 0.19989 0.38597 0.46640 0.00619  -0.02632 -0.02311 276 LYS B CD  
4364 C CE  . LYS B 276 ? 0.21460 0.40391 0.49234 -0.00122 -0.02483 -0.03040 276 LYS B CE  
4365 N NZ  . LYS B 276 ? 0.21411 0.41086 0.51822 -0.00448 -0.01836 -0.03317 276 LYS B NZ  
4366 N N   . ARG B 277 ? 0.17358 0.32482 0.36324 0.00463  -0.02417 -0.00622 277 ARG B N   
4367 C CA  . ARG B 277 ? 0.18098 0.32540 0.36030 0.00125  -0.02079 -0.00634 277 ARG B CA  
4368 C C   . ARG B 277 ? 0.18780 0.32869 0.37487 -0.00527 -0.01695 -0.01421 277 ARG B C   
4369 O O   . ARG B 277 ? 0.19316 0.34191 0.39249 -0.00671 -0.01971 -0.02152 277 ARG B O   
4370 C CB  . ARG B 277 ? 0.19772 0.34998 0.36563 0.00595  -0.02597 -0.00678 277 ARG B CB  
4371 C CG  . ARG B 277 ? 0.21736 0.37543 0.37929 0.01357  -0.03008 0.00147  277 ARG B CG  
4372 C CD  . ARG B 277 ? 0.23169 0.39773 0.37866 0.02046  -0.03446 0.00196  277 ARG B CD  
4373 N NE  . ARG B 277 ? 0.24982 0.41094 0.38528 0.02003  -0.02859 0.00688  277 ARG B NE  
4374 C CZ  . ARG B 277 ? 0.24178 0.39829 0.37340 0.02094  -0.02342 0.01936  277 ARG B CZ  
4375 N NH1 . ARG B 277 ? 0.27068 0.42502 0.40754 0.02237  -0.02379 0.02827  277 ARG B NH1 
4376 N NH2 . ARG B 277 ? 0.22316 0.37709 0.34769 0.02040  -0.01801 0.02300  277 ARG B NH2 
4377 N N   . LEU B 278 ? 0.19425 0.32302 0.37566 -0.00914 -0.01091 -0.01217 278 LEU B N   
4378 C CA  . LEU B 278 ? 0.20064 0.32368 0.38802 -0.01493 -0.00603 -0.01750 278 LEU B CA  
4379 C C   . LEU B 278 ? 0.19626 0.32583 0.38838 -0.01697 -0.01001 -0.02579 278 LEU B C   
4380 O O   . LEU B 278 ? 0.18403 0.31489 0.38992 -0.02132 -0.00843 -0.03112 278 LEU B O   
4381 C CB  . LEU B 278 ? 0.19429 0.30295 0.37132 -0.01724 -0.00093 -0.01379 278 LEU B CB  
4382 C CG  . LEU B 278 ? 0.19229 0.29294 0.37223 -0.02243 0.00448  -0.01770 278 LEU B CG  
4383 C CD1 . LEU B 278 ? 0.19101 0.28974 0.37998 -0.02341 0.01037  -0.01746 278 LEU B CD1 
4384 C CD2 . LEU B 278 ? 0.18702 0.27465 0.35498 -0.02350 0.00691  -0.01474 278 LEU B CD2 
4385 N N   . GLU B 279 ? 0.19957 0.33303 0.38102 -0.01343 -0.01512 -0.02689 279 GLU B N   
4386 C CA  . GLU B 279 ? 0.21177 0.34990 0.39550 -0.01388 -0.02063 -0.03638 279 GLU B CA  
4387 C C   . GLU B 279 ? 0.19922 0.34946 0.39712 -0.01268 -0.02837 -0.04316 279 GLU B C   
4388 O O   . GLU B 279 ? 0.21541 0.36804 0.42298 -0.01523 -0.03333 -0.05262 279 GLU B O   
4389 C CB  . GLU B 279 ? 0.19864 0.33821 0.36459 -0.00813 -0.02360 -0.03591 279 GLU B CB  
4390 C CG  . GLU B 279 ? 0.20506 0.35381 0.36118 -0.00005 -0.02773 -0.03051 279 GLU B CG  
4391 C CD  . GLU B 279 ? 0.20966 0.35385 0.35837 0.00139  -0.02173 -0.01780 279 GLU B CD  
4392 O OE1 . GLU B 279 ? 0.19998 0.33452 0.35356 -0.00375 -0.01597 -0.01397 279 GLU B OE1 
4393 O OE2 . GLU B 279 ? 0.21684 0.36665 0.35497 0.00808  -0.02312 -0.01141 279 GLU B OE2 
4394 N N   . ASN B 280 ? 0.20493 0.36238 0.40630 -0.00887 -0.03033 -0.03886 280 ASN B N   
4395 C CA  . ASN B 280 ? 0.18163 0.35142 0.39935 -0.00744 -0.03815 -0.04493 280 ASN B CA  
4396 C C   . ASN B 280 ? 0.18268 0.35351 0.42385 -0.01347 -0.03250 -0.04564 280 ASN B C   
4397 O O   . ASN B 280 ? 0.18537 0.36539 0.44702 -0.01558 -0.03787 -0.05291 280 ASN B O   
4398 C CB  . ASN B 280 ? 0.18457 0.36213 0.39461 0.00089  -0.04361 -0.03968 280 ASN B CB  
4399 C CG  . ASN B 280 ? 0.22976 0.40921 0.41740 0.00844  -0.04929 -0.03882 280 ASN B CG  
4400 O OD1 . ASN B 280 ? 0.25320 0.43305 0.43504 0.00911  -0.05389 -0.04685 280 ASN B OD1 
4401 N ND2 . ASN B 280 ? 0.22184 0.40199 0.39688 0.01473  -0.04857 -0.02872 280 ASN B ND2 
4402 N N   . VAL B 281 ? 0.18723 0.34906 0.42647 -0.01572 -0.02187 -0.03835 281 VAL B N   
4403 C CA  . VAL B 281 ? 0.19550 0.35716 0.45386 -0.02057 -0.01390 -0.03832 281 VAL B CA  
4404 C C   . VAL B 281 ? 0.19994 0.35748 0.46824 -0.02790 -0.01121 -0.04342 281 VAL B C   
4405 O O   . VAL B 281 ? 0.19917 0.36297 0.49144 -0.03229 -0.00920 -0.04643 281 VAL B O   
4406 C CB  . VAL B 281 ? 0.19989 0.35055 0.44845 -0.01943 -0.00376 -0.03014 281 VAL B CB  
4407 C CG1 . VAL B 281 ? 0.19466 0.34446 0.45899 -0.02303 0.00634  -0.02951 281 VAL B CG1 
4408 C CG2 . VAL B 281 ? 0.20460 0.35881 0.44819 -0.01249 -0.00708 -0.02553 281 VAL B CG2 
4409 N N   . LEU B 282 ? 0.19607 0.34305 0.44817 -0.02931 -0.01085 -0.04387 282 LEU B N   
4410 C CA  . LEU B 282 ? 0.19378 0.33468 0.45381 -0.03572 -0.00918 -0.04859 282 LEU B CA  
4411 C C   . LEU B 282 ? 0.20185 0.35035 0.47051 -0.03587 -0.02141 -0.05919 282 LEU B C   
4412 O O   . LEU B 282 ? 0.21612 0.35985 0.49565 -0.04140 -0.02193 -0.06445 282 LEU B O   
4413 C CB  . LEU B 282 ? 0.19703 0.32274 0.43643 -0.03631 -0.00421 -0.04507 282 LEU B CB  
4414 C CG  . LEU B 282 ? 0.19696 0.31063 0.42564 -0.03653 0.00654  -0.03632 282 LEU B CG  
4415 C CD1 . LEU B 282 ? 0.20009 0.30164 0.40923 -0.03583 0.00705  -0.03448 282 LEU B CD1 
4416 C CD2 . LEU B 282 ? 0.17272 0.28205 0.41561 -0.04155 0.01621  -0.03424 282 LEU B CD2 
4417 N N   . GLN B 283 ? 0.18958 0.34850 0.45265 -0.02927 -0.03172 -0.06245 283 GLN B N   
4418 C CA  . GLN B 283 ? 0.19231 0.35752 0.45696 -0.02658 -0.04540 -0.07353 283 GLN B CA  
4419 C C   . GLN B 283 ? 0.20981 0.36387 0.46238 -0.02790 -0.04599 -0.07830 283 GLN B C   
4420 O O   . GLN B 283 ? 0.20845 0.36029 0.47519 -0.03219 -0.05131 -0.08739 283 GLN B O   
4421 C CB  . GLN B 283 ? 0.19951 0.37502 0.49616 -0.03084 -0.05224 -0.08124 283 GLN B CB  
4422 C CG  . GLN B 283 ? 0.18219 0.37027 0.49221 -0.02833 -0.05226 -0.07711 283 GLN B CG  
4423 C CD  . GLN B 283 ? 0.21751 0.40954 0.55738 -0.03449 -0.05043 -0.07851 283 GLN B CD  
4424 O OE1 . GLN B 283 ? 0.25049 0.44335 0.59929 -0.03612 -0.03948 -0.07038 283 GLN B OE1 
4425 N NE2 . GLN B 283 ? 0.23532 0.42636 0.58542 -0.03672 -0.06023 -0.08763 283 GLN B NE2 
4426 N N   . LEU B 284 ? 0.22267 0.36959 0.45041 -0.02397 -0.04061 -0.07178 284 LEU B N   
4427 C CA  . LEU B 284 ? 0.21740 0.35313 0.43271 -0.02459 -0.03851 -0.07396 284 LEU B CA  
4428 C C   . LEU B 284 ? 0.22520 0.36463 0.42752 -0.01715 -0.04963 -0.08369 284 LEU B C   
4429 O O   . LEU B 284 ? 0.23546 0.38275 0.42191 -0.00858 -0.05372 -0.08188 284 LEU B O   
4430 C CB  . LEU B 284 ? 0.22201 0.35020 0.41923 -0.02304 -0.02870 -0.06283 284 LEU B CB  
4431 C CG  . LEU B 284 ? 0.21903 0.33286 0.41332 -0.02786 -0.02068 -0.06001 284 LEU B CG  
4432 C CD1 . LEU B 284 ? 0.22410 0.33251 0.43701 -0.03587 -0.01461 -0.05864 284 LEU B CD1 
4433 C CD2 . LEU B 284 ? 0.20459 0.31377 0.38287 -0.02507 -0.01412 -0.04966 284 LEU B CD2 
4434 N N   . LYS B 285 ? 0.24309 0.37600 0.45128 -0.01965 -0.05438 -0.09377 285 LYS B N   
4435 C CA  . LYS B 285 ? 0.25524 0.38811 0.44731 -0.01147 -0.06388 -0.10402 285 LYS B CA  
4436 C C   . LYS B 285 ? 0.26605 0.39003 0.43761 -0.00831 -0.05572 -0.09909 285 LYS B C   
4437 O O   . LYS B 285 ? 0.24458 0.35947 0.41970 -0.01458 -0.04549 -0.09138 285 LYS B O   
4438 C CB  . LYS B 285 ? 0.26059 0.38970 0.47104 -0.01522 -0.07482 -0.11887 285 LYS B CB  
4439 C CG  . LYS B 285 ? 0.27478 0.41397 0.51151 -0.01900 -0.08421 -0.12460 285 LYS B CG  
4440 C CD  . LYS B 285 ? 0.26633 0.40143 0.52490 -0.02307 -0.09699 -0.14006 285 LYS B CD  
4441 C CE  . LYS B 285 ? 0.24296 0.38882 0.53540 -0.02900 -0.10466 -0.14390 285 LYS B CE  
4442 N NZ  . LYS B 285 ? 0.25936 0.39608 0.56651 -0.03099 -0.11484 -0.15451 285 LYS B NZ  
4443 N N   . ALA B 286 ? 0.28300 0.41020 0.43256 0.00245  -0.06022 -0.10328 286 ALA B N   
4444 C CA  . ALA B 286 ? 0.29473 0.41619 0.42618 0.00703  -0.05276 -0.09904 286 ALA B CA  
4445 C C   . ALA B 286 ? 0.31645 0.43654 0.43422 0.01632  -0.06146 -0.11259 286 ALA B C   
4446 O O   . ALA B 286 ? 0.32646 0.45289 0.44010 0.02272  -0.07321 -0.12266 286 ALA B O   
4447 C CB  . ALA B 286 ? 0.27998 0.40880 0.39517 0.01292  -0.04481 -0.08519 286 ALA B CB  
4448 N N   . ALA B 287 ? 0.29895 0.41043 0.40893 0.01807  -0.05624 -0.11325 287 ALA B N   
4449 C CA  . ALA B 287 ? 0.30546 0.41393 0.40130 0.02802  -0.06366 -0.12682 287 ALA B CA  
4450 C C   . ALA B 287 ? 0.31010 0.43056 0.38136 0.04267  -0.06808 -0.12875 287 ALA B C   
4451 O O   . ALA B 287 ? 0.30878 0.42877 0.36952 0.05171  -0.07970 -0.14368 287 ALA B O   
4452 C CB  . ALA B 287 ? 0.30017 0.39979 0.38951 0.02945  -0.05498 -0.12415 287 ALA B CB  
4453 N N   . ASP B 288 ? 0.32802 0.45843 0.38965 0.04570  -0.05963 -0.11392 288 ASP B N   
4454 C CA  . ASP B 288 ? 0.32352 0.46543 0.36141 0.05965  -0.06198 -0.11226 288 ASP B CA  
4455 C C   . ASP B 288 ? 0.35511 0.50578 0.39915 0.05714  -0.06515 -0.10534 288 ASP B C   
4456 O O   . ASP B 288 ? 0.37495 0.53474 0.40373 0.06489  -0.06060 -0.09425 288 ASP B O   
4457 C CB  . ASP B 288 ? 0.30584 0.45237 0.32560 0.06785  -0.04831 -0.09938 288 ASP B CB  
4458 C CG  . ASP B 288 ? 0.28435 0.42923 0.31897 0.05723  -0.03561 -0.08300 288 ASP B CG  
4459 O OD1 . ASP B 288 ? 0.28862 0.42667 0.34422 0.04441  -0.03670 -0.08301 288 ASP B OD1 
4460 O OD2 . ASP B 288 ? 0.28626 0.43663 0.31210 0.06210  -0.02461 -0.07004 288 ASP B OD2 
4461 N N   . SER B 289 ? 0.44273 0.59061 0.51055 0.04661  -0.07272 -0.11160 289 SER B N   
4462 C CA  . SER B 289 ? 0.44357 0.59979 0.52174 0.04380  -0.07701 -0.10698 289 SER B CA  
4463 C C   . SER B 289 ? 0.50818 0.67419 0.56537 0.05809  -0.08743 -0.11148 289 SER B C   
4464 O O   . SER B 289 ? 0.56853 0.74222 0.61505 0.06307  -0.08249 -0.09854 289 SER B O   
4465 C CB  . SER B 289 ? 0.41566 0.56828 0.52361 0.03199  -0.08419 -0.11561 289 SER B CB  
4466 O OG  . SER B 289 ? 0.41865 0.56498 0.54495 0.01945  -0.07288 -0.10624 289 SER B OG  
# 
