data_9GO1
# 
_entry.id   9GO1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GO1         pdb_00009go1 10.2210/pdb9go1/pdb 
WWPDB D_1292140958 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GO1 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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              joerg.standfuss@psi.ch 
_pdbx_contact_author.name_first         Joerg 
_pdbx_contact_author.name_last          Standfuss 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8825-386X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mulder, M.'     1 0009-0003-2988-2780 
'Weinert, T.'    2 0000-0002-0339-3722 
'Skopintsev, P.' 3 ?                   
'Bruenle, S.'    4 ?                   
'Broser, M.'     5 ?                   
'Hegemann, P.'   6 ?                   
'Standfuss, J.'  7 ?                   
# 
_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            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                1282 
_citation.page_last                 1290 
_citation.title                     'Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c15402 
_citation.pdbx_database_id_PubMed   39680650 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mulder, M.'       1  ?                   
primary 'Hwang, S.'        2  0000-0003-4323-1450 
primary 'Broser, M.'       3  0000-0002-7133-4548 
primary 'Brunle, S.'       4  ?                   
primary 'Skopintsev, P.'   5  ?                   
primary 'Schattenberg, C.' 6  0009-0005-1509-0445 
primary 'Schnick, C.'      7  ?                   
primary 'Hartmann, S.'     8  ?                   
primary 'Church, J.'       9  0000-0001-5986-1305 
primary 'Schapiro, I.'     10 0000-0001-8536-6869 
primary 'Dworkowski, F.'   11 ?                   
primary 'Weinert, T.'      12 ?                   
primary 'Hegemann, P.'     13 0000-0003-3589-6452 
primary 'Sun, H.'          14 0000-0002-1655-0838 
primary 'Standfuss, J.'    15 ?                   
# 
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 'Archaeal-type opsin 1,Archaeal-type opsin 2'    37441.984 1  ? ? ? ? 
2 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 356.540   9  ? ? ? ? 
3 non-polymer syn RETINAL                                          284.436   1  ? ? ? ? 
4 water       nat water                                            18.015    13 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Channelopsin-1,Retinal binding protein,Sensory opsin B' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;STGSDATVPVATQDGPDYVFHRAHERMLFQTSYTLENNGSVICIPNNGQCFCLAWLKSNGTNAEKLAANILQWITFALSA
LCLMFYGYQTWKSTCGWEEIYVATIEMIKFIIEYFHEFDEPAVIYSSNGNKTVWLRYAEWLLTCPVILIHLSNLTGLAND
YNKRTMGLLVSDIGTIVWGTTAALSKGYVRVIFFLMGLCYGIYTFFNAAKVYIEAYHTVPKGRCRQVVTGMAWLFFVSWG
MFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTKLNIGGTEIEVETLVEDEA
EAGAVSSEDLYFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STGSDATVPVATQDGPDYVFHRAHERMLFQTSYTLENNGSVICIPNNGQCFCLAWLKSNGTNAEKLAANILQWITFALSA
LCLMFYGYQTWKSTCGWEEIYVATIEMIKFIIEYFHEFDEPAVIYSSNGNKTVWLRYAEWLLTCPVILIHLSNLTGLAND
YNKRTMGLLVSDIGTIVWGTTAALSKGYVRVIFFLMGLCYGIYTFFNAAKVYIEAYHTVPKGRCRQVVTGMAWLFFVSWG
MFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTKLNIGGTEIEVETLVEDEA
EAGAVSSEDLYFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' OLC 
3 RETINAL                                          RET 
4 water                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   THR n 
1 3   GLY n 
1 4   SER n 
1 5   ASP n 
1 6   ALA n 
1 7   THR n 
1 8   VAL n 
1 9   PRO n 
1 10  VAL n 
1 11  ALA n 
1 12  THR n 
1 13  GLN n 
1 14  ASP n 
1 15  GLY n 
1 16  PRO n 
1 17  ASP n 
1 18  TYR n 
1 19  VAL n 
1 20  PHE n 
1 21  HIS n 
1 22  ARG n 
1 23  ALA n 
1 24  HIS n 
1 25  GLU n 
1 26  ARG n 
1 27  MET n 
1 28  LEU n 
1 29  PHE n 
1 30  GLN n 
1 31  THR n 
1 32  SER n 
1 33  TYR n 
1 34  THR n 
1 35  LEU n 
1 36  GLU n 
1 37  ASN n 
1 38  ASN n 
1 39  GLY n 
1 40  SER n 
1 41  VAL n 
1 42  ILE n 
1 43  CYS n 
1 44  ILE n 
1 45  PRO n 
1 46  ASN n 
1 47  ASN n 
1 48  GLY n 
1 49  GLN n 
1 50  CYS n 
1 51  PHE n 
1 52  CYS n 
1 53  LEU n 
1 54  ALA n 
1 55  TRP n 
1 56  LEU n 
1 57  LYS n 
1 58  SER n 
1 59  ASN n 
1 60  GLY n 
1 61  THR n 
1 62  ASN n 
1 63  ALA n 
1 64  GLU n 
1 65  LYS n 
1 66  LEU n 
1 67  ALA n 
1 68  ALA n 
1 69  ASN n 
1 70  ILE n 
1 71  LEU n 
1 72  GLN n 
1 73  TRP n 
1 74  ILE n 
1 75  THR n 
1 76  PHE n 
1 77  ALA n 
1 78  LEU n 
1 79  SER n 
1 80  ALA n 
1 81  LEU n 
1 82  CYS n 
1 83  LEU n 
1 84  MET n 
1 85  PHE n 
1 86  TYR n 
1 87  GLY n 
1 88  TYR n 
1 89  GLN n 
1 90  THR n 
1 91  TRP n 
1 92  LYS n 
1 93  SER n 
1 94  THR n 
1 95  CYS n 
1 96  GLY n 
1 97  TRP n 
1 98  GLU n 
1 99  GLU n 
1 100 ILE n 
1 101 TYR n 
1 102 VAL n 
1 103 ALA n 
1 104 THR n 
1 105 ILE n 
1 106 GLU n 
1 107 MET n 
1 108 ILE n 
1 109 LYS n 
1 110 PHE n 
1 111 ILE n 
1 112 ILE n 
1 113 GLU n 
1 114 TYR n 
1 115 PHE n 
1 116 HIS n 
1 117 GLU n 
1 118 PHE n 
1 119 ASP n 
1 120 GLU n 
1 121 PRO n 
1 122 ALA n 
1 123 VAL n 
1 124 ILE n 
1 125 TYR n 
1 126 SER n 
1 127 SER n 
1 128 ASN n 
1 129 GLY n 
1 130 ASN n 
1 131 LYS n 
1 132 THR n 
1 133 VAL n 
1 134 TRP n 
1 135 LEU n 
1 136 ARG n 
1 137 TYR n 
1 138 ALA n 
1 139 GLU n 
1 140 TRP n 
1 141 LEU n 
1 142 LEU n 
1 143 THR n 
1 144 CYS n 
1 145 PRO n 
1 146 VAL n 
1 147 ILE n 
1 148 LEU n 
1 149 ILE n 
1 150 HIS n 
1 151 LEU n 
1 152 SER n 
1 153 ASN n 
1 154 LEU n 
1 155 THR n 
1 156 GLY n 
1 157 LEU n 
1 158 ALA n 
1 159 ASN n 
1 160 ASP n 
1 161 TYR n 
1 162 ASN n 
1 163 LYS n 
1 164 ARG n 
1 165 THR n 
1 166 MET n 
1 167 GLY n 
1 168 LEU n 
1 169 LEU n 
1 170 VAL n 
1 171 SER n 
1 172 ASP n 
1 173 ILE n 
1 174 GLY n 
1 175 THR n 
1 176 ILE n 
1 177 VAL n 
1 178 TRP n 
1 179 GLY n 
1 180 THR n 
1 181 THR n 
1 182 ALA n 
1 183 ALA n 
1 184 LEU n 
1 185 SER n 
1 186 LYS n 
1 187 GLY n 
1 188 TYR n 
1 189 VAL n 
1 190 ARG n 
1 191 VAL n 
1 192 ILE n 
1 193 PHE n 
1 194 PHE n 
1 195 LEU n 
1 196 MET n 
1 197 GLY n 
1 198 LEU n 
1 199 CYS n 
1 200 TYR n 
1 201 GLY n 
1 202 ILE n 
1 203 TYR n 
1 204 THR n 
1 205 PHE n 
1 206 PHE n 
1 207 ASN n 
1 208 ALA n 
1 209 ALA n 
1 210 LYS n 
1 211 VAL n 
1 212 TYR n 
1 213 ILE n 
1 214 GLU n 
1 215 ALA n 
1 216 TYR n 
1 217 HIS n 
1 218 THR n 
1 219 VAL n 
1 220 PRO n 
1 221 LYS n 
1 222 GLY n 
1 223 ARG n 
1 224 CYS n 
1 225 ARG n 
1 226 GLN n 
1 227 VAL n 
1 228 VAL n 
1 229 THR n 
1 230 GLY n 
1 231 MET n 
1 232 ALA n 
1 233 TRP n 
1 234 LEU n 
1 235 PHE n 
1 236 PHE n 
1 237 VAL n 
1 238 SER n 
1 239 TRP n 
1 240 GLY n 
1 241 MET n 
1 242 PHE n 
1 243 PRO n 
1 244 ILE n 
1 245 LEU n 
1 246 PHE n 
1 247 ILE n 
1 248 LEU n 
1 249 GLY n 
1 250 PRO n 
1 251 GLU n 
1 252 GLY n 
1 253 PHE n 
1 254 GLY n 
1 255 VAL n 
1 256 LEU n 
1 257 SER n 
1 258 VAL n 
1 259 TYR n 
1 260 GLY n 
1 261 SER n 
1 262 THR n 
1 263 VAL n 
1 264 GLY n 
1 265 HIS n 
1 266 THR n 
1 267 ILE n 
1 268 ILE n 
1 269 ASP n 
1 270 LEU n 
1 271 MET n 
1 272 SER n 
1 273 LYS n 
1 274 ASN n 
1 275 CYS n 
1 276 TRP n 
1 277 GLY n 
1 278 LEU n 
1 279 LEU n 
1 280 GLY n 
1 281 HIS n 
1 282 TYR n 
1 283 LEU n 
1 284 ARG n 
1 285 VAL n 
1 286 LEU n 
1 287 ILE n 
1 288 HIS n 
1 289 GLU n 
1 290 HIS n 
1 291 ILE n 
1 292 LEU n 
1 293 ILE n 
1 294 HIS n 
1 295 GLY n 
1 296 ASP n 
1 297 ILE n 
1 298 ARG n 
1 299 LYS n 
1 300 THR n 
1 301 THR n 
1 302 LYS n 
1 303 LEU n 
1 304 ASN n 
1 305 ILE n 
1 306 GLY n 
1 307 GLY n 
1 308 THR n 
1 309 GLU n 
1 310 ILE n 
1 311 GLU n 
1 312 VAL n 
1 313 GLU n 
1 314 THR n 
1 315 LEU n 
1 316 VAL n 
1 317 GLU n 
1 318 ASP n 
1 319 GLU n 
1 320 ALA n 
1 321 GLU n 
1 322 ALA n 
1 323 GLY n 
1 324 ALA n 
1 325 VAL n 
1 326 SER n 
1 327 SER n 
1 328 GLU n 
1 329 ASP n 
1 330 LEU n 
1 331 TYR n 
1 332 PHE n 
1 333 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   222 'Chlamydomonas smithii' ? acop1                                  ? ? ? ? ? ? 
'Chlamydomonas reinhardtii' 3055 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 223 333 'Chlamydomonas smithii' ? 'cop4, acop2, CSOB, CHLRE_02g085257v5' ? ? ? ? ? ? 
'Chlamydomonas reinhardtii' 3055 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                          ?                   'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                         ?                   'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ?                   'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ?                   'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                         ?                   'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                        ?                   'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                  ?                   'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                          ?                   'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                        ?                   'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                            ?                   'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                       ?                   'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                          ?                   'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                           ?                   'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                       ?                   'C5 H11 N O2 S'  149.211 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 1-Oleoyl-R-glycerol 'C21 H40 O4'     356.540 
PHE 'L-peptide linking' y PHENYLALANINE                                    ?                   'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                          ?                   'C5 H9 N O2'     115.130 
RET non-polymer         . RETINAL                                          ?                   'C20 H28 O'      284.436 
SER 'L-peptide linking' y SERINE                                           ?                   'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                        ?                   'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                       ?                   'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                         ?                   'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                           ?                   'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   24  ?   ?   ?   A . n 
A 1 2   THR 2   25  ?   ?   ?   A . n 
A 1 3   GLY 3   26  ?   ?   ?   A . n 
A 1 4   SER 4   27  ?   ?   ?   A . n 
A 1 5   ASP 5   28  ?   ?   ?   A . n 
A 1 6   ALA 6   29  ?   ?   ?   A . n 
A 1 7   THR 7   30  ?   ?   ?   A . n 
A 1 8   VAL 8   31  ?   ?   ?   A . n 
A 1 9   PRO 9   32  ?   ?   ?   A . n 
A 1 10  VAL 10  33  ?   ?   ?   A . n 
A 1 11  ALA 11  34  ?   ?   ?   A . n 
A 1 12  THR 12  35  ?   ?   ?   A . n 
A 1 13  GLN 13  36  ?   ?   ?   A . n 
A 1 14  ASP 14  37  ?   ?   ?   A . n 
A 1 15  GLY 15  38  ?   ?   ?   A . n 
A 1 16  PRO 16  39  ?   ?   ?   A . n 
A 1 17  ASP 17  40  ?   ?   ?   A . n 
A 1 18  TYR 18  41  ?   ?   ?   A . n 
A 1 19  VAL 19  42  ?   ?   ?   A . n 
A 1 20  PHE 20  43  ?   ?   ?   A . n 
A 1 21  HIS 21  44  ?   ?   ?   A . n 
A 1 22  ARG 22  45  ?   ?   ?   A . n 
A 1 23  ALA 23  46  ?   ?   ?   A . n 
A 1 24  HIS 24  47  ?   ?   ?   A . n 
A 1 25  GLU 25  48  ?   ?   ?   A . n 
A 1 26  ARG 26  49  ?   ?   ?   A . n 
A 1 27  MET 27  50  50  MET MET A . n 
A 1 28  LEU 28  51  51  LEU LEU A . n 
A 1 29  PHE 29  52  52  PHE PHE A . n 
A 1 30  GLN 30  53  53  GLN GLN A . n 
A 1 31  THR 31  54  54  THR THR A . n 
A 1 32  SER 32  55  55  SER SER A . n 
A 1 33  TYR 33  56  56  TYR TYR A . n 
A 1 34  THR 34  57  57  THR THR A . n 
A 1 35  LEU 35  58  58  LEU LEU A . n 
A 1 36  GLU 36  59  59  GLU GLU A . n 
A 1 37  ASN 37  60  60  ASN ASN A . n 
A 1 38  ASN 38  61  61  ASN ASN A . n 
A 1 39  GLY 39  62  62  GLY GLY A . n 
A 1 40  SER 40  63  63  SER SER A . n 
A 1 41  VAL 41  64  64  VAL VAL A . n 
A 1 42  ILE 42  65  65  ILE ILE A . n 
A 1 43  CYS 43  66  66  CYS CYS A . n 
A 1 44  ILE 44  67  67  ILE ILE A . n 
A 1 45  PRO 45  68  68  PRO PRO A . n 
A 1 46  ASN 46  69  69  ASN ASN A . n 
A 1 47  ASN 47  70  70  ASN ASN A . n 
A 1 48  GLY 48  71  71  GLY GLY A . n 
A 1 49  GLN 49  72  72  GLN GLN A . n 
A 1 50  CYS 50  73  73  CYS CYS A . n 
A 1 51  PHE 51  74  74  PHE PHE A . n 
A 1 52  CYS 52  75  75  CYS CYS A . n 
A 1 53  LEU 53  76  76  LEU LEU A . n 
A 1 54  ALA 54  77  77  ALA ALA A . n 
A 1 55  TRP 55  78  78  TRP TRP A . n 
A 1 56  LEU 56  79  79  LEU LEU A . n 
A 1 57  LYS 57  80  80  LYS LYS A . n 
A 1 58  SER 58  81  81  SER SER A . n 
A 1 59  ASN 59  82  82  ASN ASN A . n 
A 1 60  GLY 60  83  83  GLY GLY A . n 
A 1 61  THR 61  84  84  THR THR A . n 
A 1 62  ASN 62  85  85  ASN ASN A . n 
A 1 63  ALA 63  86  86  ALA ALA A . n 
A 1 64  GLU 64  87  87  GLU GLU A . n 
A 1 65  LYS 65  88  88  LYS LYS A . n 
A 1 66  LEU 66  89  89  LEU LEU A . n 
A 1 67  ALA 67  90  90  ALA ALA A . n 
A 1 68  ALA 68  91  91  ALA ALA A . n 
A 1 69  ASN 69  92  92  ASN ASN A . n 
A 1 70  ILE 70  93  93  ILE ILE A . n 
A 1 71  LEU 71  94  94  LEU LEU A . n 
A 1 72  GLN 72  95  95  GLN GLN A . n 
A 1 73  TRP 73  96  96  TRP TRP A . n 
A 1 74  ILE 74  97  97  ILE ILE A . n 
A 1 75  THR 75  98  98  THR THR A . n 
A 1 76  PHE 76  99  99  PHE PHE A . n 
A 1 77  ALA 77  100 100 ALA ALA A . n 
A 1 78  LEU 78  101 101 LEU LEU A . n 
A 1 79  SER 79  102 102 SER SER A . n 
A 1 80  ALA 80  103 103 ALA ALA A . n 
A 1 81  LEU 81  104 104 LEU LEU A . n 
A 1 82  CYS 82  105 105 CYS CYS A . n 
A 1 83  LEU 83  106 106 LEU LEU A . n 
A 1 84  MET 84  107 107 MET MET A . n 
A 1 85  PHE 85  108 108 PHE PHE A . n 
A 1 86  TYR 86  109 109 TYR TYR A . n 
A 1 87  GLY 87  110 110 GLY GLY A . n 
A 1 88  TYR 88  111 111 TYR TYR A . n 
A 1 89  GLN 89  112 ?   ?   ?   A . n 
A 1 90  THR 90  113 ?   ?   ?   A . n 
A 1 91  TRP 91  114 ?   ?   ?   A . n 
A 1 92  LYS 92  115 ?   ?   ?   A . n 
A 1 93  SER 93  116 ?   ?   ?   A . n 
A 1 94  THR 94  117 ?   ?   ?   A . n 
A 1 95  CYS 95  118 118 CYS CYS A . n 
A 1 96  GLY 96  119 119 GLY GLY A . n 
A 1 97  TRP 97  120 120 TRP TRP A . n 
A 1 98  GLU 98  121 121 GLU GLU A . n 
A 1 99  GLU 99  122 122 GLU GLU A . n 
A 1 100 ILE 100 123 123 ILE ILE A . n 
A 1 101 TYR 101 124 124 TYR TYR A . n 
A 1 102 VAL 102 125 125 VAL VAL A . n 
A 1 103 ALA 103 126 126 ALA ALA A . n 
A 1 104 THR 104 127 127 THR THR A . n 
A 1 105 ILE 105 128 128 ILE ILE A . n 
A 1 106 GLU 106 129 129 GLU GLU A . n 
A 1 107 MET 107 130 130 MET MET A . n 
A 1 108 ILE 108 131 131 ILE ILE A . n 
A 1 109 LYS 109 132 132 LYS LYS A . n 
A 1 110 PHE 110 133 133 PHE PHE A . n 
A 1 111 ILE 111 134 134 ILE ILE A . n 
A 1 112 ILE 112 135 135 ILE ILE A . n 
A 1 113 GLU 113 136 136 GLU GLU A . n 
A 1 114 TYR 114 137 137 TYR TYR A . n 
A 1 115 PHE 115 138 138 PHE PHE A . n 
A 1 116 HIS 116 139 139 HIS HIS A . n 
A 1 117 GLU 117 140 140 GLU GLU A . n 
A 1 118 PHE 118 141 141 PHE PHE A . n 
A 1 119 ASP 119 142 142 ASP ASP A . n 
A 1 120 GLU 120 143 143 GLU GLU A . n 
A 1 121 PRO 121 144 144 PRO PRO A . n 
A 1 122 ALA 122 145 145 ALA ALA A . n 
A 1 123 VAL 123 146 146 VAL VAL A . n 
A 1 124 ILE 124 147 147 ILE ILE A . n 
A 1 125 TYR 125 148 148 TYR TYR A . n 
A 1 126 SER 126 149 149 SER SER A . n 
A 1 127 SER 127 150 150 SER SER A . n 
A 1 128 ASN 128 151 151 ASN ASN A . n 
A 1 129 GLY 129 152 152 GLY GLY A . n 
A 1 130 ASN 130 153 153 ASN ASN A . n 
A 1 131 LYS 131 154 154 LYS LYS A . n 
A 1 132 THR 132 155 155 THR THR A . n 
A 1 133 VAL 133 156 156 VAL VAL A . n 
A 1 134 TRP 134 157 157 TRP TRP A . n 
A 1 135 LEU 135 158 158 LEU LEU A . n 
A 1 136 ARG 136 159 159 ARG ARG A . n 
A 1 137 TYR 137 160 160 TYR TYR A . n 
A 1 138 ALA 138 161 161 ALA ALA A . n 
A 1 139 GLU 139 162 162 GLU GLU A . n 
A 1 140 TRP 140 163 163 TRP TRP A . n 
A 1 141 LEU 141 164 164 LEU LEU A . n 
A 1 142 LEU 142 165 165 LEU LEU A . n 
A 1 143 THR 143 166 166 THR THR A . n 
A 1 144 CYS 144 167 167 CYS CYS A . n 
A 1 145 PRO 145 168 168 PRO PRO A . n 
A 1 146 VAL 146 169 169 VAL VAL A . n 
A 1 147 ILE 147 170 170 ILE ILE A . n 
A 1 148 LEU 148 171 171 LEU LEU A . n 
A 1 149 ILE 149 172 172 ILE ILE A . n 
A 1 150 HIS 150 173 173 HIS HIS A . n 
A 1 151 LEU 151 174 174 LEU LEU A . n 
A 1 152 SER 152 175 175 SER SER A . n 
A 1 153 ASN 153 176 176 ASN ASN A . n 
A 1 154 LEU 154 177 177 LEU LEU A . n 
A 1 155 THR 155 178 178 THR THR A . n 
A 1 156 GLY 156 179 179 GLY GLY A . n 
A 1 157 LEU 157 180 180 LEU LEU A . n 
A 1 158 ALA 158 181 181 ALA ALA A . n 
A 1 159 ASN 159 182 182 ASN ASN A . n 
A 1 160 ASP 160 183 183 ASP ASP A . n 
A 1 161 TYR 161 184 184 TYR TYR A . n 
A 1 162 ASN 162 185 185 ASN ASN A . n 
A 1 163 LYS 163 186 186 LYS LYS A . n 
A 1 164 ARG 164 187 187 ARG ARG A . n 
A 1 165 THR 165 188 188 THR THR A . n 
A 1 166 MET 166 189 189 MET MET A . n 
A 1 167 GLY 167 190 190 GLY GLY A . n 
A 1 168 LEU 168 191 191 LEU LEU A . n 
A 1 169 LEU 169 192 192 LEU LEU A . n 
A 1 170 VAL 170 193 193 VAL VAL A . n 
A 1 171 SER 171 194 194 SER SER A . n 
A 1 172 ASP 172 195 195 ASP ASP A . n 
A 1 173 ILE 173 196 196 ILE ILE A . n 
A 1 174 GLY 174 197 197 GLY GLY A . n 
A 1 175 THR 175 198 198 THR THR A . n 
A 1 176 ILE 176 199 199 ILE ILE A . n 
A 1 177 VAL 177 200 200 VAL VAL A . n 
A 1 178 TRP 178 201 201 TRP TRP A . n 
A 1 179 GLY 179 202 202 GLY GLY A . n 
A 1 180 THR 180 203 203 THR THR A . n 
A 1 181 THR 181 204 204 THR THR A . n 
A 1 182 ALA 182 205 205 ALA ALA A . n 
A 1 183 ALA 183 206 206 ALA ALA A . n 
A 1 184 LEU 184 207 207 LEU LEU A . n 
A 1 185 SER 185 208 208 SER SER A . n 
A 1 186 LYS 186 209 209 LYS LYS A . n 
A 1 187 GLY 187 210 210 GLY GLY A . n 
A 1 188 TYR 188 211 211 TYR TYR A . n 
A 1 189 VAL 189 212 212 VAL VAL A . n 
A 1 190 ARG 190 213 213 ARG ARG A . n 
A 1 191 VAL 191 214 214 VAL VAL A . n 
A 1 192 ILE 192 215 215 ILE ILE A . n 
A 1 193 PHE 193 216 216 PHE PHE A . n 
A 1 194 PHE 194 217 217 PHE PHE A . n 
A 1 195 LEU 195 218 218 LEU LEU A . n 
A 1 196 MET 196 219 219 MET MET A . n 
A 1 197 GLY 197 220 220 GLY GLY A . n 
A 1 198 LEU 198 221 221 LEU LEU A . n 
A 1 199 CYS 199 222 222 CYS CYS A . n 
A 1 200 TYR 200 223 223 TYR TYR A . n 
A 1 201 GLY 201 224 224 GLY GLY A . n 
A 1 202 ILE 202 225 225 ILE ILE A . n 
A 1 203 TYR 203 226 226 TYR TYR A . n 
A 1 204 THR 204 227 227 THR THR A . n 
A 1 205 PHE 205 228 228 PHE PHE A . n 
A 1 206 PHE 206 229 229 PHE PHE A . n 
A 1 207 ASN 207 230 230 ASN ASN A . n 
A 1 208 ALA 208 231 231 ALA ALA A . n 
A 1 209 ALA 209 232 232 ALA ALA A . n 
A 1 210 LYS 210 233 233 LYS LYS A . n 
A 1 211 VAL 211 234 234 VAL VAL A . n 
A 1 212 TYR 212 235 235 TYR TYR A . n 
A 1 213 ILE 213 236 236 ILE ILE A . n 
A 1 214 GLU 214 237 237 GLU GLU A . n 
A 1 215 ALA 215 238 238 ALA ALA A . n 
A 1 216 TYR 216 239 239 TYR TYR A . n 
A 1 217 HIS 217 240 240 HIS HIS A . n 
A 1 218 THR 218 241 241 THR THR A . n 
A 1 219 VAL 219 242 242 VAL VAL A . n 
A 1 220 PRO 220 243 243 PRO PRO A . n 
A 1 221 LYS 221 244 244 LYS LYS A . n 
A 1 222 GLY 222 245 245 GLY GLY A . n 
A 1 223 ARG 223 246 246 ARG ARG A . n 
A 1 224 CYS 224 247 247 CYS CYS A . n 
A 1 225 ARG 225 248 248 ARG ARG A . n 
A 1 226 GLN 226 249 249 GLN GLN A . n 
A 1 227 VAL 227 250 250 VAL VAL A . n 
A 1 228 VAL 228 251 251 VAL VAL A . n 
A 1 229 THR 229 252 252 THR THR A . n 
A 1 230 GLY 230 253 253 GLY GLY A . n 
A 1 231 MET 231 254 254 MET MET A . n 
A 1 232 ALA 232 255 255 ALA ALA A . n 
A 1 233 TRP 233 256 256 TRP TRP A . n 
A 1 234 LEU 234 257 257 LEU LEU A . n 
A 1 235 PHE 235 258 258 PHE PHE A . n 
A 1 236 PHE 236 259 259 PHE PHE A . n 
A 1 237 VAL 237 260 260 VAL VAL A . n 
A 1 238 SER 238 261 261 SER SER A . n 
A 1 239 TRP 239 262 262 TRP TRP A . n 
A 1 240 GLY 240 263 263 GLY GLY A . n 
A 1 241 MET 241 264 264 MET MET A . n 
A 1 242 PHE 242 265 265 PHE PHE A . n 
A 1 243 PRO 243 266 266 PRO PRO A . n 
A 1 244 ILE 244 267 267 ILE ILE A . n 
A 1 245 LEU 245 268 268 LEU LEU A . n 
A 1 246 PHE 246 269 269 PHE PHE A . n 
A 1 247 ILE 247 270 270 ILE ILE A . n 
A 1 248 LEU 248 271 271 LEU LEU A . n 
A 1 249 GLY 249 272 272 GLY GLY A . n 
A 1 250 PRO 250 273 273 PRO PRO A . n 
A 1 251 GLU 251 274 274 GLU GLU A . n 
A 1 252 GLY 252 275 275 GLY GLY A . n 
A 1 253 PHE 253 276 276 PHE PHE A . n 
A 1 254 GLY 254 277 277 GLY GLY A . n 
A 1 255 VAL 255 278 278 VAL VAL A . n 
A 1 256 LEU 256 279 279 LEU LEU A . n 
A 1 257 SER 257 280 280 SER SER A . n 
A 1 258 VAL 258 281 281 VAL VAL A . n 
A 1 259 TYR 259 282 282 TYR TYR A . n 
A 1 260 GLY 260 283 283 GLY GLY A . n 
A 1 261 SER 261 284 284 SER SER A . n 
A 1 262 THR 262 285 285 THR THR A . n 
A 1 263 VAL 263 286 286 VAL VAL A . n 
A 1 264 GLY 264 287 287 GLY GLY A . n 
A 1 265 HIS 265 288 288 HIS HIS A . n 
A 1 266 THR 266 289 289 THR THR A . n 
A 1 267 ILE 267 290 290 ILE ILE A . n 
A 1 268 ILE 268 291 291 ILE ILE A . n 
A 1 269 ASP 269 292 292 ASP ASP A . n 
A 1 270 LEU 270 293 293 LEU LEU A . n 
A 1 271 MET 271 294 294 MET MET A . n 
A 1 272 SER 272 295 295 SER SER A . n 
A 1 273 LYS 273 296 296 LYS LYR A A n 
A 1 274 ASN 274 297 297 ASN ASN A . n 
A 1 275 CYS 275 298 298 CYS CYS A . n 
A 1 276 TRP 276 299 299 TRP TRP A . n 
A 1 277 GLY 277 300 300 GLY GLY A . n 
A 1 278 LEU 278 301 301 LEU LEU A . n 
A 1 279 LEU 279 302 302 LEU LEU A . n 
A 1 280 GLY 280 303 303 GLY GLY A . n 
A 1 281 HIS 281 304 304 HIS HIS A . n 
A 1 282 TYR 282 305 305 TYR TYR A . n 
A 1 283 LEU 283 306 306 LEU LEU A . n 
A 1 284 ARG 284 307 307 ARG ARG A . n 
A 1 285 VAL 285 308 308 VAL VAL A . n 
A 1 286 LEU 286 309 309 LEU LEU A . n 
A 1 287 ILE 287 310 310 ILE ILE A . n 
A 1 288 HIS 288 311 311 HIS HIS A . n 
A 1 289 GLU 289 312 312 GLU GLU A . n 
A 1 290 HIS 290 313 313 HIS HIS A . n 
A 1 291 ILE 291 314 314 ILE ILE A . n 
A 1 292 LEU 292 315 315 LEU LEU A . n 
A 1 293 ILE 293 316 316 ILE ILE A . n 
A 1 294 HIS 294 317 317 HIS HIS A . n 
A 1 295 GLY 295 318 318 GLY GLY A . n 
A 1 296 ASP 296 319 319 ASP ASP A . n 
A 1 297 ILE 297 320 320 ILE ILE A . n 
A 1 298 ARG 298 321 321 ARG ARG A . n 
A 1 299 LYS 299 322 322 LYS LYS A . n 
A 1 300 THR 300 323 323 THR THR A . n 
A 1 301 THR 301 324 324 THR THR A . n 
A 1 302 LYS 302 325 325 LYS LYS A . n 
A 1 303 LEU 303 326 326 LEU LEU A . n 
A 1 304 ASN 304 327 327 ASN ASN A . n 
A 1 305 ILE 305 328 ?   ?   ?   A . n 
A 1 306 GLY 306 329 ?   ?   ?   A . n 
A 1 307 GLY 307 330 ?   ?   ?   A . n 
A 1 308 THR 308 331 331 THR THR A . n 
A 1 309 GLU 309 332 332 GLU GLU A . n 
A 1 310 ILE 310 333 333 ILE ILE A . n 
A 1 311 GLU 311 334 334 GLU GLU A . n 
A 1 312 VAL 312 335 335 VAL VAL A . n 
A 1 313 GLU 313 336 336 GLU GLU A . n 
A 1 314 THR 314 337 337 THR THR A . n 
A 1 315 LEU 315 338 338 LEU LEU A . n 
A 1 316 VAL 316 339 339 VAL VAL A . n 
A 1 317 GLU 317 340 340 GLU GLU A . n 
A 1 318 ASP 318 341 341 ASP ASP A . n 
A 1 319 GLU 319 342 342 GLU GLU A . n 
A 1 320 ALA 320 343 343 ALA ALA A . n 
A 1 321 GLU 321 344 344 GLU GLU A . n 
A 1 322 ALA 322 345 345 ALA ALA A . n 
A 1 323 GLY 323 346 346 GLY GLY A . n 
A 1 324 ALA 324 347 347 ALA ALA A . n 
A 1 325 VAL 325 348 348 VAL VAL A . n 
A 1 326 SER 326 349 349 SER SER A . n 
A 1 327 SER 327 350 350 SER SER A . n 
A 1 328 GLU 328 351 351 GLU GLU A . n 
A 1 329 ASP 329 352 352 ASP ASP A . n 
A 1 330 LEU 330 353 ?   ?   ?   A . n 
A 1 331 TYR 331 354 ?   ?   ?   A . n 
A 1 332 PHE 332 355 ?   ?   ?   A . n 
A 1 333 GLN 333 356 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        RET 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RET 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 OLC 1  401 402 OLC OLC A . 
C 2 OLC 1  402 403 OLC OLC A . 
D 2 OLC 1  403 404 OLC OLC A . 
E 2 OLC 1  404 405 OLC OLC A . 
F 2 OLC 1  405 406 OLC OLC A . 
G 2 OLC 1  406 407 OLC OLC A . 
H 2 OLC 1  407 408 OLC OLC A . 
I 2 OLC 1  408 409 OLC OLC A . 
J 2 OLC 1  409 410 OLC OLC A . 
K 3 RET 1  410 296 RET LYR A . 
L 4 HOH 1  501 7   HOH HOH A . 
L 4 HOH 2  502 6   HOH HOH A . 
L 4 HOH 3  503 8   HOH HOH A . 
L 4 HOH 4  504 1   HOH HOH A . 
L 4 HOH 5  505 2   HOH HOH A . 
L 4 HOH 6  506 3   HOH HOH A . 
L 4 HOH 7  507 4   HOH HOH A . 
L 4 HOH 8  508 9   HOH HOH A . 
L 4 HOH 9  509 12  HOH HOH A . 
L 4 HOH 10 510 5   HOH HOH A . 
L 4 HOH 11 511 13  HOH HOH A . 
L 4 HOH 12 512 10  HOH HOH A . 
L 4 HOH 13 513 11  HOH HOH A . 
# 
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 A MET 50  ? CG  ? A MET 27  CG  
2   1 Y 1 A MET 50  ? SD  ? A MET 27  SD  
3   1 Y 1 A MET 50  ? CE  ? A MET 27  CE  
4   1 Y 1 A LEU 51  ? CG  ? A LEU 28  CG  
5   1 Y 1 A LEU 51  ? CD1 ? A LEU 28  CD1 
6   1 Y 1 A LEU 51  ? CD2 ? A LEU 28  CD2 
7   1 Y 1 A CYS 118 ? SG  ? A CYS 95  SG  
8   1 Y 1 A LYS 186 ? CG  ? A LYS 163 CG  
9   1 Y 1 A LYS 186 ? CD  ? A LYS 163 CD  
10  1 Y 1 A LYS 186 ? CE  ? A LYS 163 CE  
11  1 Y 1 A LYS 186 ? NZ  ? A LYS 163 NZ  
12  1 Y 1 A LYS 244 ? CG  ? A LYS 221 CG  
13  1 Y 1 A LYS 244 ? CD  ? A LYS 221 CD  
14  1 Y 1 A LYS 244 ? CE  ? A LYS 221 CE  
15  1 Y 1 A LYS 244 ? NZ  ? A LYS 221 NZ  
16  1 Y 1 A LEU 326 ? CG  ? A LEU 303 CG  
17  1 Y 1 A LEU 326 ? CD1 ? A LEU 303 CD1 
18  1 Y 1 A LEU 326 ? CD2 ? A LEU 303 CD2 
19  1 Y 1 A ASN 327 ? CG  ? A ASN 304 CG  
20  1 Y 1 A ASN 327 ? OD1 ? A ASN 304 OD1 
21  1 Y 1 A ASN 327 ? ND2 ? A ASN 304 ND2 
22  1 Y 1 A THR 331 ? OG1 ? A THR 308 OG1 
23  1 Y 1 A THR 331 ? CG2 ? A THR 308 CG2 
24  1 Y 1 A GLU 332 ? CG  ? A GLU 309 CG  
25  1 Y 1 A GLU 332 ? CD  ? A GLU 309 CD  
26  1 Y 1 A GLU 332 ? OE1 ? A GLU 309 OE1 
27  1 Y 1 A GLU 332 ? OE2 ? A GLU 309 OE2 
28  1 Y 1 A GLU 342 ? CG  ? A GLU 319 CG  
29  1 Y 1 A GLU 342 ? CD  ? A GLU 319 CD  
30  1 Y 1 A GLU 342 ? OE1 ? A GLU 319 OE1 
31  1 Y 1 A GLU 342 ? OE2 ? A GLU 319 OE2 
32  1 N 1 A OLC 402 ? C18 ? C OLC 1   C18 
33  1 N 1 A OLC 402 ? C17 ? C OLC 1   C17 
34  1 N 1 A OLC 402 ? C24 ? C OLC 1   C24 
35  1 N 1 A OLC 402 ? C16 ? C OLC 1   C16 
36  1 N 1 A OLC 402 ? C15 ? C OLC 1   C15 
37  1 N 1 A OLC 402 ? C21 ? C OLC 1   C21 
38  1 N 1 A OLC 402 ? C22 ? C OLC 1   C22 
39  1 N 1 A OLC 402 ? O25 ? C OLC 1   O25 
40  1 N 1 A OLC 402 ? O23 ? C OLC 1   O23 
41  1 N 1 A OLC 403 ? C18 ? D OLC 1   C18 
42  1 N 1 A OLC 403 ? C10 ? D OLC 1   C10 
43  1 N 1 A OLC 403 ? C9  ? D OLC 1   C9  
44  1 N 1 A OLC 403 ? C17 ? D OLC 1   C17 
45  1 N 1 A OLC 403 ? C11 ? D OLC 1   C11 
46  1 N 1 A OLC 403 ? C8  ? D OLC 1   C8  
47  1 N 1 A OLC 403 ? C16 ? D OLC 1   C16 
48  1 N 1 A OLC 403 ? C12 ? D OLC 1   C12 
49  1 N 1 A OLC 403 ? C15 ? D OLC 1   C15 
50  1 N 1 A OLC 403 ? C13 ? D OLC 1   C13 
51  1 N 1 A OLC 403 ? C14 ? D OLC 1   C14 
52  1 N 1 A OLC 404 ? C18 ? E OLC 1   C18 
53  1 N 1 A OLC 404 ? C10 ? E OLC 1   C10 
54  1 N 1 A OLC 404 ? C17 ? E OLC 1   C17 
55  1 N 1 A OLC 404 ? C11 ? E OLC 1   C11 
56  1 N 1 A OLC 404 ? C16 ? E OLC 1   C16 
57  1 N 1 A OLC 404 ? C12 ? E OLC 1   C12 
58  1 N 1 A OLC 404 ? C15 ? E OLC 1   C15 
59  1 N 1 A OLC 404 ? C13 ? E OLC 1   C13 
60  1 N 1 A OLC 404 ? C14 ? E OLC 1   C14 
61  1 N 1 A OLC 405 ? C18 ? F OLC 1   C18 
62  1 N 1 A OLC 405 ? C17 ? F OLC 1   C17 
63  1 N 1 A OLC 405 ? C16 ? F OLC 1   C16 
64  1 N 1 A OLC 405 ? C12 ? F OLC 1   C12 
65  1 N 1 A OLC 405 ? C15 ? F OLC 1   C15 
66  1 N 1 A OLC 405 ? C13 ? F OLC 1   C13 
67  1 N 1 A OLC 405 ? C14 ? F OLC 1   C14 
68  1 N 1 A OLC 406 ? C18 ? G OLC 1   C18 
69  1 N 1 A OLC 406 ? C10 ? G OLC 1   C10 
70  1 N 1 A OLC 406 ? C9  ? G OLC 1   C9  
71  1 N 1 A OLC 406 ? C17 ? G OLC 1   C17 
72  1 N 1 A OLC 406 ? C11 ? G OLC 1   C11 
73  1 N 1 A OLC 406 ? C24 ? G OLC 1   C24 
74  1 N 1 A OLC 406 ? C16 ? G OLC 1   C16 
75  1 N 1 A OLC 406 ? C12 ? G OLC 1   C12 
76  1 N 1 A OLC 406 ? C15 ? G OLC 1   C15 
77  1 N 1 A OLC 406 ? C13 ? G OLC 1   C13 
78  1 N 1 A OLC 406 ? C14 ? G OLC 1   C14 
79  1 N 1 A OLC 406 ? C21 ? G OLC 1   C21 
80  1 N 1 A OLC 406 ? C22 ? G OLC 1   C22 
81  1 N 1 A OLC 406 ? O25 ? G OLC 1   O25 
82  1 N 1 A OLC 406 ? O23 ? G OLC 1   O23 
83  1 N 1 A OLC 407 ? C18 ? H OLC 1   C18 
84  1 N 1 A OLC 407 ? C10 ? H OLC 1   C10 
85  1 N 1 A OLC 407 ? C9  ? H OLC 1   C9  
86  1 N 1 A OLC 407 ? C17 ? H OLC 1   C17 
87  1 N 1 A OLC 407 ? C11 ? H OLC 1   C11 
88  1 N 1 A OLC 407 ? C24 ? H OLC 1   C24 
89  1 N 1 A OLC 407 ? C16 ? H OLC 1   C16 
90  1 N 1 A OLC 407 ? C12 ? H OLC 1   C12 
91  1 N 1 A OLC 407 ? C15 ? H OLC 1   C15 
92  1 N 1 A OLC 407 ? C13 ? H OLC 1   C13 
93  1 N 1 A OLC 407 ? C14 ? H OLC 1   C14 
94  1 N 1 A OLC 407 ? C21 ? H OLC 1   C21 
95  1 N 1 A OLC 407 ? C22 ? H OLC 1   C22 
96  1 N 1 A OLC 407 ? O25 ? H OLC 1   O25 
97  1 N 1 A OLC 407 ? O23 ? H OLC 1   O23 
98  1 N 1 A OLC 408 ? C18 ? I OLC 1   C18 
99  1 N 1 A OLC 408 ? C17 ? I OLC 1   C17 
100 1 N 1 A OLC 408 ? C11 ? I OLC 1   C11 
101 1 N 1 A OLC 408 ? C24 ? I OLC 1   C24 
102 1 N 1 A OLC 408 ? C16 ? I OLC 1   C16 
103 1 N 1 A OLC 408 ? C12 ? I OLC 1   C12 
104 1 N 1 A OLC 408 ? C15 ? I OLC 1   C15 
105 1 N 1 A OLC 408 ? C13 ? I OLC 1   C13 
106 1 N 1 A OLC 408 ? C14 ? I OLC 1   C14 
107 1 N 1 A OLC 408 ? C21 ? I OLC 1   C21 
108 1 N 1 A OLC 408 ? C1  ? I OLC 1   C1  
109 1 N 1 A OLC 408 ? C22 ? I OLC 1   C22 
110 1 N 1 A OLC 408 ? O19 ? I OLC 1   O19 
111 1 N 1 A OLC 408 ? O25 ? I OLC 1   O25 
112 1 N 1 A OLC 408 ? O23 ? I OLC 1   O23 
113 1 N 1 A OLC 408 ? O20 ? I OLC 1   O20 
114 1 N 1 A OLC 409 ? C18 ? J OLC 1   C18 
115 1 N 1 A OLC 409 ? C10 ? J OLC 1   C10 
116 1 N 1 A OLC 409 ? C17 ? J OLC 1   C17 
117 1 N 1 A OLC 409 ? C11 ? J OLC 1   C11 
118 1 N 1 A OLC 409 ? C24 ? J OLC 1   C24 
119 1 N 1 A OLC 409 ? C16 ? J OLC 1   C16 
120 1 N 1 A OLC 409 ? C12 ? J OLC 1   C12 
121 1 N 1 A OLC 409 ? C15 ? J OLC 1   C15 
122 1 N 1 A OLC 409 ? C13 ? J OLC 1   C13 
123 1 N 1 A OLC 409 ? C14 ? J OLC 1   C14 
124 1 N 1 A OLC 409 ? C21 ? J OLC 1   C21 
125 1 N 1 A OLC 409 ? C1  ? J OLC 1   C1  
126 1 N 1 A OLC 409 ? C22 ? J OLC 1   C22 
127 1 N 1 A OLC 409 ? O19 ? J OLC 1   O19 
128 1 N 1 A OLC 409 ? O25 ? J OLC 1   O25 
129 1 N 1 A OLC 409 ? O23 ? J OLC 1   O23 
130 1 N 1 A OLC 409 ? O20 ? J OLC 1   O20 
# 
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_4459 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.9.1     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.9.1.    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20_4459 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                     9GO1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.400 
_cell.length_a_esd                 ? 
_cell.length_b                     141.700 
_cell.length_b_esd                 ? 
_cell.length_c                     94.400 
_cell.length_c_esd                 ? 
_cell.volume                       821315.872 
_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                         9GO1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 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                   9GO1 
_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             2.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.82 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'100 mM sodium citrate (pH 6.0), 30% PEG500DME, 100 mM MgCl2, 100 mM NaCl, and 100 mM (NH4)2SO4.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-07-07 
_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                    Si-111 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GO1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.59 
_reflns.d_resolution_low                               70.85 
_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                                     8838 
_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                           67.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                415.94 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.7 
_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                                ? 
_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                                   ? 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   0.06 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.59 
_reflns_shell.d_res_low                                     2.69 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.05 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1288 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  0.849 
_reflns_shell.pdbx_R_split                                  0.87 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               57.64 
_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                                 9GO1 
_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                            2.59 
_refine.ls_d_res_low                             70.85 
_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                     8836 
_refine.ls_number_reflns_R_free                  884 
_refine.ls_number_reflns_R_work                  7952 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    66.86 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2171 
_refine.ls_R_factor_R_free                       0.2696 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2114 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_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                 32.8552 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2925 
_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                       2.59 
_refine_hist.d_res_low                        70.85 
_refine_hist.number_atoms_solvent             13 
_refine_hist.number_atoms_total               2460 
_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        2321 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         126 
_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' ? 0.0046  ? 2499 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9193  ? 3363 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0535  ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0035  ? 417  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.9305 ? 422  ? 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' 2.59 2.75  . . 25  245  12.62  . . . . 0.3251 . . . . . . . . . . . 0.3509 
'X-RAY DIFFRACTION' 2.75 2.96  . . 61  531  27.11  . . . . 0.2929 . . . . . . . . . . . 0.3137 
'X-RAY DIFFRACTION' 2.96 3.26  . . 126 1146 58.81  . . . . 0.2704 . . . . . . . . . . . 0.3630 
'X-RAY DIFFRACTION' 3.26 3.73  . . 219 1957 99.63  . . . . 0.2176 . . . . . . . . . . . 0.2880 
'X-RAY DIFFRACTION' 3.73 4.70  . . 222 1999 100.00 . . . . 0.1811 . . . . . . . . . . . 0.2463 
'X-RAY DIFFRACTION' 4.70 70.85 . . 231 2074 99.78  . . . . 0.2127 . . . . . . . . . . . 0.2563 
# 
_struct.entry_id                     9GO1 
_struct.title                        'C1C2 Channelrhodopsin - SMX Dark structure' 
_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        9GO1 
_struct_keywords.text            'channelrhodopsin, dark, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q93WP2_CHLRE Q93WP2 ? 1 
;STGSDATVPVATQDGPDYVFHRAHERMLFQTSYTLENNGSVICIPNNGQCFCLAWLKSNGTNAEKLAANILQWITFALSA
LCLMFYGYQTWKSTCGWEEIYVATIEMIKFIIEYFHEFDEPAVIYSSNGNKTVWLRYAEWLLTCPVILIHLSNLTGLAND
YNKRTMGLLVSDIGTIVWGTTAALSKGYVRVIFFLMGLCYGIYTFFNAAKVYIEAYHTVPKG
;
24  
2 UNP Q8RUT8_CHLRE Q8RUT8 ? 1 
;RCRQVVTGMAWLFFVSWGMFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTK
LNIGGTEIEVETLVEDEAEAGAV
;
207 
# 
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 9GO1 A 1   ? 222 ? Q93WP2 24  ? 245 ? 24  245 
2 2 9GO1 A 223 ? 325 ? Q8RUT8 207 ? 309 ? 246 348 
# 
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 
2 9GO1 SER A 326 ? UNP Q8RUT8 ? ? 'expression tag' 349 1 
2 9GO1 SER A 327 ? UNP Q8RUT8 ? ? 'expression tag' 350 2 
2 9GO1 GLU A 328 ? UNP Q8RUT8 ? ? 'expression tag' 351 3 
2 9GO1 ASP A 329 ? UNP Q8RUT8 ? ? 'expression tag' 352 4 
2 9GO1 LEU A 330 ? UNP Q8RUT8 ? ? 'expression tag' 353 5 
2 9GO1 TYR A 331 ? UNP Q8RUT8 ? ? 'expression tag' 354 6 
2 9GO1 PHE A 332 ? UNP Q8RUT8 ? ? 'expression tag' 355 7 
2 9GO1 GLN A 333 ? UNP Q8RUT8 ? ? 'expression tag' 356 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 6140  ? 
1 MORE         -54   ? 
1 'SSA (A^2)'  26280 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_555 -x,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 47.2000000000 
# 
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 LEU A 53  ? LYS A 57  ? LEU A 76  LYS A 80  5 ? 5  
HELX_P HELX_P2 AA2 THR A 61  ? GLY A 87  ? THR A 84  GLY A 110 1 ? 27 
HELX_P HELX_P3 AA3 GLY A 96  ? GLU A 117 ? GLY A 119 GLU A 140 1 ? 22 
HELX_P HELX_P4 AA4 VAL A 133 ? SER A 152 ? VAL A 156 SER A 175 1 ? 20 
HELX_P HELX_P5 AA5 ASN A 162 ? SER A 185 ? ASN A 185 SER A 208 1 ? 24 
HELX_P HELX_P6 AA6 LYS A 186 ? VAL A 219 ? LYS A 209 VAL A 242 1 ? 34 
HELX_P HELX_P7 AA7 GLY A 222 ? GLY A 249 ? GLY A 245 GLY A 272 1 ? 28 
HELX_P HELX_P8 AA8 SER A 257 ? LYS A 273 A SER A 280 LYS A 296 1 ? 17 
HELX_P HELX_P9 AA9 LYS A 273 A GLY A 295 ? LYS A 296 GLY A 318 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 43  SG ? ? ? 1_555 A CYS 43 SG  ? ? A CYS 66  A CYS 66  3_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf2 disulf ?   ? A CYS 50  SG ? ? ? 1_555 A CYS 52 SG  ? ? A CYS 73  A CYS 75  3_555 ? ? ? ? ? ? ? 2.030 ? ? 
covale1 covale one ? A LYS 273 NZ ? A ? 1_555 K RET .  C15 ? ? A LYS 296 A RET 410 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 RET K .  ? LYS A 273 ? RET A 410 ? 1_555 LYS A 296 A 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like   
2 CYS A 43 ? CYS A 43  ? CYS A 66  ? 1_555 CYS A 66  ? 3_555 SG  SG .   . .   None          'Disulfide bridge' 
3 CYS A 50 ? CYS A 52  ? CYS A 73  ? 1_555 CYS A 75  ? 3_555 SG  SG .   . .   None          'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           120 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            143 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    121 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     144 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       4.02 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? 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 THR A 34  ? GLU A 36  ? THR A 57  GLU A 59  
AA1 2 VAL A 41  ? CYS A 43  ? VAL A 64  CYS A 66  
AA2 1 ILE A 124 ? TYR A 125 ? ILE A 147 TYR A 148 
AA2 2 LYS A 131 ? THR A 132 ? LYS A 154 THR A 155 
AA3 1 ILE A 310 ? VAL A 316 ? ILE A 333 VAL A 339 
AA3 2 ILE A 297 ? ASN A 304 ? ILE A 320 ASN A 327 
AA3 3 ALA A 324 ? GLU A 328 ? ALA A 347 GLU A 351 
# 
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 GLU A 36  ? N GLU A 59  O VAL A 41  ? O VAL A 64  
AA2 1 2 N ILE A 124 ? N ILE A 147 O THR A 132 ? O THR A 155 
AA3 1 2 O ILE A 310 ? O ILE A 333 N LEU A 303 ? N LEU A 326 
AA3 2 3 N THR A 300 ? N THR A 323 O VAL A 325 ? O VAL A 348 
# 
_pdbx_entry_details.entry_id                   9GO1 
_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 HIS A 139 ? ? -142.60 37.29  
2 1 LYS A 296 A ? -113.44 -75.93 
3 1 ALA A 345 ? ? -155.30 29.11  
4 1 SER A 350 ? ? -167.79 113.83 
# 
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 4.66494612941   3.96880644946 19.5548052039 0.206530986825  ? 0.0259680647801  ? 0.14923886054    
? 0.201678731549  ? -0.0438415174395 ? 0.438380140248  ? 0.414046143198  ? -0.121361987521   ? 0.0711159607264 ? 0.0396207844912  
? -0.0153202508181  ? 0.0646154374888 ? -0.0953775559794 ? -0.103943142009 ? -0.222116556459  ? 0.0598712993808  ? 0.126896830545 
? 0.00594495305575 ? 0.0218828038238  ? 0.0207622362806   ? -0.0159619703557  ? 
2 'X-RAY DIFFRACTION' ? refined 22.2032841254   32.3999103778 13.9042612614 0.416848554632  ? -0.101572558576  ? 0.289923783233   
? 0.465604872682  ? -0.0916964093994 ? 0.751236754473  ? 0.307864394053  ? -0.00493532323901 ? 0.469176651999  ? 0.0870776264746  
? -0.0946694383858  ? 0.81169763727   ? -0.231199112677  ? -0.144660151221 ? -0.474638609318  ? -0.0344934215317 ? -0.19069660875 
? -0.093492344538  ? 0.174321356426   ? 0.111720919632    ? -0.205435002776   ? 
3 'X-RAY DIFFRACTION' ? refined 12.6192471696   30.2582669482 21.3631579343 0.0994598205196 ? -0.08955167255   ? -0.0304413614632 
? 0.296180734357  ? 0.0622234571988  ? 0.344091980285  ? 0.0119881202317 ? 0.0188235158049   ? 0.0407812760018 ? 0.0177908851283  
? 0.0389105832925   ? 0.104935530059  ? -0.114399303367  ? 0.0249490311941 ? 0.158483832297   ? -0.0154183593292 ? 
0.00247843219052 ? -0.30690044846   ? -0.186963010659  ? 0.234688311403    ? -0.617555991144   ? 
4 'X-RAY DIFFRACTION' ? refined -0.286529700545 42.1066883985 14.6957205411 0.0923872154042 ? -0.0828817966274 ? -0.0633732728013 
? 0.123063974202  ? -0.12076499347   ? -0.183191978267 ? 0.118135939003  ? -0.054438706371   ? 0.100456305241  ? 0.0631690466959  
? -0.118794076286   ? 0.205527808746  ? 0.0840392437555  ? 0.0893313006736 ? -0.0924219963378 ? -0.0639128411629 ? 0.0369584630988 
? 0.0765842526975  ? 0.135482701818   ? -0.00517602542485 ? 1.32195274429     ? 
5 'X-RAY DIFFRACTION' ? refined 11.3142246688   43.4004505441 8.44783994149 0.413476546255  ? -0.274114240075  ? 0.192620936912   
? 0.0657139826355 ? 0.0226622192759  ? 0.179430849352  ? 0.37309520194   ? -0.00804681440314 ? 0.14007495886   ? 0.00413521221081 
? -0.00364273600882 ? 0.0640810338307 ? 0.028187213273   ? 0.216424570715  ? 0.15041592725    ? -0.148424524117  ? 0.0249733759207 
? -0.0990786986945 ? -0.286864701808  ? 0.15420854104     ? 0.324390007382    ? 
6 'X-RAY DIFFRACTION' ? refined 3.99251682246   69.2532020911 6.93341810207 0.823107987316  ? -0.0049298209305 ? -0.076545095158  
? 0.455261949649  ? 0.032409887426   ? 0.801075418923  ? 0.0316625004733 ? -0.0137219116201  ? 0.0211707658814 ? 0.0318897203238  
? 0.0117123194996   ? 0.0232550115837 ? -0.143875500156  ? 0.169858848884  ? -0.0554056080174 ? -0.186273874109  ? 0.131628482737 
? 0.248153881094   ? -0.0510859348957 ? -0.328811426201   ? 0.000290799349329 ? 
# 
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 50  ? A 35  A 84  ? ? 
;chain 'A' and (resid 50 through 84 )
;
2 'X-RAY DIFFRACTION' 2 A 36  A 85  ? A 60  A 109 ? ? 
;chain 'A' and (resid 85 through 109 )
;
3 'X-RAY DIFFRACTION' 3 A 61  A 110 ? A 101 A 156 ? ? 
;chain 'A' and (resid 110 through 156 )
;
4 'X-RAY DIFFRACTION' 4 A 102 A 157 ? A 186 A 241 ? ? 
;chain 'A' and (resid 157 through 241 )
;
5 'X-RAY DIFFRACTION' 5 A 187 A 242 ? A 262 A 317 ? ? 
;chain 'A' and (resid 242 through 317 )
;
6 'X-RAY DIFFRACTION' 6 A 263 A 318 ? A 294 A 352 ? ? 
;chain 'A' and (resid 318 through 352 )
;
# 
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 SER 24  ? A SER 1   
2  1 Y 1 A THR 25  ? A THR 2   
3  1 Y 1 A GLY 26  ? A GLY 3   
4  1 Y 1 A SER 27  ? A SER 4   
5  1 Y 1 A ASP 28  ? A ASP 5   
6  1 Y 1 A ALA 29  ? A ALA 6   
7  1 Y 1 A THR 30  ? A THR 7   
8  1 Y 1 A VAL 31  ? A VAL 8   
9  1 Y 1 A PRO 32  ? A PRO 9   
10 1 Y 1 A VAL 33  ? A VAL 10  
11 1 Y 1 A ALA 34  ? A ALA 11  
12 1 Y 1 A THR 35  ? A THR 12  
13 1 Y 1 A GLN 36  ? A GLN 13  
14 1 Y 1 A ASP 37  ? A ASP 14  
15 1 Y 1 A GLY 38  ? A GLY 15  
16 1 Y 1 A PRO 39  ? A PRO 16  
17 1 Y 1 A ASP 40  ? A ASP 17  
18 1 Y 1 A TYR 41  ? A TYR 18  
19 1 Y 1 A VAL 42  ? A VAL 19  
20 1 Y 1 A PHE 43  ? A PHE 20  
21 1 Y 1 A HIS 44  ? A HIS 21  
22 1 Y 1 A ARG 45  ? A ARG 22  
23 1 Y 1 A ALA 46  ? A ALA 23  
24 1 Y 1 A HIS 47  ? A HIS 24  
25 1 Y 1 A GLU 48  ? A GLU 25  
26 1 Y 1 A ARG 49  ? A ARG 26  
27 1 Y 1 A GLN 112 ? A GLN 89  
28 1 Y 1 A THR 113 ? A THR 90  
29 1 Y 1 A TRP 114 ? A TRP 91  
30 1 Y 1 A LYS 115 ? A LYS 92  
31 1 Y 1 A SER 116 ? A SER 93  
32 1 Y 1 A THR 117 ? A THR 94  
33 1 Y 1 A ILE 328 ? A ILE 305 
34 1 Y 1 A GLY 329 ? A GLY 306 
35 1 Y 1 A GLY 330 ? A GLY 307 
36 1 Y 1 A LEU 353 ? A LEU 330 
37 1 Y 1 A TYR 354 ? A TYR 331 
38 1 Y 1 A PHE 355 ? A PHE 332 
39 1 Y 1 A GLN 356 ? A GLN 333 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
OLC C18  C N N 250 
OLC C10  C N N 251 
OLC C9   C N N 252 
OLC C17  C N N 253 
OLC C11  C N N 254 
OLC C8   C N N 255 
OLC C24  C N N 256 
OLC C16  C N N 257 
OLC C12  C N N 258 
OLC C7   C N N 259 
OLC C15  C N N 260 
OLC C13  C N N 261 
OLC C6   C N N 262 
OLC C14  C N N 263 
OLC C5   C N N 264 
OLC C4   C N N 265 
OLC C3   C N N 266 
OLC C2   C N N 267 
OLC C21  C N N 268 
OLC C1   C N N 269 
OLC C22  C N R 270 
OLC O19  O N N 271 
OLC O25  O N N 272 
OLC O23  O N N 273 
OLC O20  O N N 274 
OLC H18  H N N 275 
OLC H18A H N N 276 
OLC H18B H N N 277 
OLC H10  H N N 278 
OLC H9   H N N 279 
OLC H17  H N N 280 
OLC H17A H N N 281 
OLC H11  H N N 282 
OLC H11A H N N 283 
OLC H8   H N N 284 
OLC H8A  H N N 285 
OLC H24  H N N 286 
OLC H24A H N N 287 
OLC H16  H N N 288 
OLC H16A H N N 289 
OLC H12  H N N 290 
OLC H12A H N N 291 
OLC H7   H N N 292 
OLC H7A  H N N 293 
OLC H15  H N N 294 
OLC H15A H N N 295 
OLC H13  H N N 296 
OLC H13A H N N 297 
OLC H6   H N N 298 
OLC H6A  H N N 299 
OLC H14  H N N 300 
OLC H14A H N N 301 
OLC H5   H N N 302 
OLC H5A  H N N 303 
OLC H4   H N N 304 
OLC H4A  H N N 305 
OLC H3   H N N 306 
OLC H3A  H N N 307 
OLC H2   H N N 308 
OLC H2A  H N N 309 
OLC H21  H N N 310 
OLC H21A H N N 311 
OLC H22  H N N 312 
OLC HO25 H N N 313 
OLC HO23 H N N 314 
PHE N    N N N 315 
PHE CA   C N S 316 
PHE C    C N N 317 
PHE O    O N N 318 
PHE CB   C N N 319 
PHE CG   C Y N 320 
PHE CD1  C Y N 321 
PHE CD2  C Y N 322 
PHE CE1  C Y N 323 
PHE CE2  C Y N 324 
PHE CZ   C Y N 325 
PHE OXT  O N N 326 
PHE H    H N N 327 
PHE H2   H N N 328 
PHE HA   H N N 329 
PHE HB2  H N N 330 
PHE HB3  H N N 331 
PHE HD1  H N N 332 
PHE HD2  H N N 333 
PHE HE1  H N N 334 
PHE HE2  H N N 335 
PHE HZ   H N N 336 
PHE HXT  H N N 337 
PRO N    N N N 338 
PRO CA   C N S 339 
PRO C    C N N 340 
PRO O    O N N 341 
PRO CB   C N N 342 
PRO CG   C N N 343 
PRO CD   C N N 344 
PRO OXT  O N N 345 
PRO H    H N N 346 
PRO HA   H N N 347 
PRO HB2  H N N 348 
PRO HB3  H N N 349 
PRO HG2  H N N 350 
PRO HG3  H N N 351 
PRO HD2  H N N 352 
PRO HD3  H N N 353 
PRO HXT  H N N 354 
RET C1   C N N 355 
RET C2   C N N 356 
RET C3   C N N 357 
RET C4   C N N 358 
RET C5   C N N 359 
RET C6   C N N 360 
RET C7   C N N 361 
RET C8   C N N 362 
RET C9   C N N 363 
RET C10  C N N 364 
RET C11  C N N 365 
RET C12  C N N 366 
RET C13  C N N 367 
RET C14  C N N 368 
RET C15  C N N 369 
RET O1   O N N 370 
RET C16  C N N 371 
RET C17  C N N 372 
RET C18  C N N 373 
RET C19  C N N 374 
RET C20  C N N 375 
RET H21  H N N 376 
RET H22  H N N 377 
RET H31  H N N 378 
RET H32  H N N 379 
RET H41  H N N 380 
RET H42  H N N 381 
RET H7   H N N 382 
RET H8   H N N 383 
RET H10  H N N 384 
RET H11  H N N 385 
RET H12  H N N 386 
RET H14  H N N 387 
RET H15  H N N 388 
RET H161 H N N 389 
RET H162 H N N 390 
RET H163 H N N 391 
RET H171 H N N 392 
RET H172 H N N 393 
RET H173 H N N 394 
RET H181 H N N 395 
RET H182 H N N 396 
RET H183 H N N 397 
RET H191 H N N 398 
RET H192 H N N 399 
RET H193 H N N 400 
RET H201 H N N 401 
RET H202 H N N 402 
RET H203 H N N 403 
SER N    N N N 404 
SER CA   C N S 405 
SER C    C N N 406 
SER O    O N N 407 
SER CB   C N N 408 
SER OG   O N N 409 
SER OXT  O N N 410 
SER H    H N N 411 
SER H2   H N N 412 
SER HA   H N N 413 
SER HB2  H N N 414 
SER HB3  H N N 415 
SER HG   H N N 416 
SER HXT  H N N 417 
THR N    N N N 418 
THR CA   C N S 419 
THR C    C N N 420 
THR O    O N N 421 
THR CB   C N R 422 
THR OG1  O N N 423 
THR CG2  C N N 424 
THR OXT  O N N 425 
THR H    H N N 426 
THR H2   H N N 427 
THR HA   H N N 428 
THR HB   H N N 429 
THR HG1  H N N 430 
THR HG21 H N N 431 
THR HG22 H N N 432 
THR HG23 H N N 433 
THR HXT  H N N 434 
TRP N    N N N 435 
TRP CA   C N S 436 
TRP C    C N N 437 
TRP O    O N N 438 
TRP CB   C N N 439 
TRP CG   C Y N 440 
TRP CD1  C Y N 441 
TRP CD2  C Y N 442 
TRP NE1  N Y N 443 
TRP CE2  C Y N 444 
TRP CE3  C Y N 445 
TRP CZ2  C Y N 446 
TRP CZ3  C Y N 447 
TRP CH2  C Y N 448 
TRP OXT  O N N 449 
TRP H    H N N 450 
TRP H2   H N N 451 
TRP HA   H N N 452 
TRP HB2  H N N 453 
TRP HB3  H N N 454 
TRP HD1  H N N 455 
TRP HE1  H N N 456 
TRP HE3  H N N 457 
TRP HZ2  H N N 458 
TRP HZ3  H N N 459 
TRP HH2  H N N 460 
TRP HXT  H N N 461 
TYR N    N N N 462 
TYR CA   C N S 463 
TYR C    C N N 464 
TYR O    O N N 465 
TYR CB   C N N 466 
TYR CG   C Y N 467 
TYR CD1  C Y N 468 
TYR CD2  C Y N 469 
TYR CE1  C Y N 470 
TYR CE2  C Y N 471 
TYR CZ   C Y N 472 
TYR OH   O N N 473 
TYR OXT  O N N 474 
TYR H    H N N 475 
TYR H2   H N N 476 
TYR HA   H N N 477 
TYR HB2  H N N 478 
TYR HB3  H N N 479 
TYR HD1  H N N 480 
TYR HD2  H N N 481 
TYR HE1  H N N 482 
TYR HE2  H N N 483 
TYR HH   H N N 484 
TYR HXT  H N N 485 
VAL N    N N N 486 
VAL CA   C N S 487 
VAL C    C N N 488 
VAL O    O N N 489 
VAL CB   C N N 490 
VAL CG1  C N N 491 
VAL CG2  C N N 492 
VAL OXT  O N N 493 
VAL H    H N N 494 
VAL H2   H N N 495 
VAL HA   H N N 496 
VAL HB   H N N 497 
VAL HG11 H N N 498 
VAL HG12 H N N 499 
VAL HG13 H N N 500 
VAL HG21 H N N 501 
VAL HG22 H N N 502 
VAL HG23 H N N 503 
VAL HXT  H N N 504 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
OLC C18 C17  sing N N 237 
OLC C10 C9   doub N N 238 
OLC C10 C11  sing N N 239 
OLC C9  C8   sing N N 240 
OLC C17 C16  sing N Z 241 
OLC C11 C12  sing N N 242 
OLC C8  C7   sing N N 243 
OLC C24 C22  sing N N 244 
OLC C24 O25  sing N N 245 
OLC C16 C15  sing N N 246 
OLC C12 C13  sing N N 247 
OLC C7  C6   sing N N 248 
OLC C15 C14  sing N N 249 
OLC C13 C14  sing N N 250 
OLC C6  C5   sing N N 251 
OLC C5  C4   sing N N 252 
OLC C4  C3   sing N N 253 
OLC C3  C2   sing N N 254 
OLC C2  C1   sing N N 255 
OLC C21 C22  sing N N 256 
OLC C21 O20  sing N N 257 
OLC C1  O19  doub N N 258 
OLC C1  O20  sing N N 259 
OLC C22 O23  sing N N 260 
OLC C18 H18  sing N N 261 
OLC C18 H18A sing N N 262 
OLC C18 H18B sing N N 263 
OLC C10 H10  sing N N 264 
OLC C9  H9   sing N N 265 
OLC C17 H17  sing N N 266 
OLC C17 H17A sing N N 267 
OLC C11 H11  sing N N 268 
OLC C11 H11A sing N N 269 
OLC C8  H8   sing N N 270 
OLC C8  H8A  sing N N 271 
OLC C24 H24  sing N N 272 
OLC C24 H24A sing N N 273 
OLC C16 H16  sing N N 274 
OLC C16 H16A sing N N 275 
OLC C12 H12  sing N N 276 
OLC C12 H12A sing N N 277 
OLC C7  H7   sing N N 278 
OLC C7  H7A  sing N N 279 
OLC C15 H15  sing N N 280 
OLC C15 H15A sing N N 281 
OLC C13 H13  sing N N 282 
OLC C13 H13A sing N N 283 
OLC C6  H6   sing N N 284 
OLC C6  H6A  sing N N 285 
OLC C14 H14  sing N N 286 
OLC C14 H14A sing N N 287 
OLC C5  H5   sing N N 288 
OLC C5  H5A  sing N N 289 
OLC C4  H4   sing N N 290 
OLC C4  H4A  sing N N 291 
OLC C3  H3   sing N N 292 
OLC C3  H3A  sing N N 293 
OLC C2  H2   sing N N 294 
OLC C2  H2A  sing N N 295 
OLC C21 H21  sing N N 296 
OLC C21 H21A sing N N 297 
OLC C22 H22  sing N N 298 
OLC O25 HO25 sing N N 299 
OLC O23 HO23 sing N N 300 
PHE N   CA   sing N N 301 
PHE N   H    sing N N 302 
PHE N   H2   sing N N 303 
PHE CA  C    sing N N 304 
PHE CA  CB   sing N N 305 
PHE CA  HA   sing N N 306 
PHE C   O    doub N N 307 
PHE C   OXT  sing N N 308 
PHE CB  CG   sing N N 309 
PHE CB  HB2  sing N N 310 
PHE CB  HB3  sing N N 311 
PHE CG  CD1  doub Y N 312 
PHE CG  CD2  sing Y N 313 
PHE CD1 CE1  sing Y N 314 
PHE CD1 HD1  sing N N 315 
PHE CD2 CE2  doub Y N 316 
PHE CD2 HD2  sing N N 317 
PHE CE1 CZ   doub Y N 318 
PHE CE1 HE1  sing N N 319 
PHE CE2 CZ   sing Y N 320 
PHE CE2 HE2  sing N N 321 
PHE CZ  HZ   sing N N 322 
PHE OXT HXT  sing N N 323 
PRO N   CA   sing N N 324 
PRO N   CD   sing N N 325 
PRO N   H    sing N N 326 
PRO CA  C    sing N N 327 
PRO CA  CB   sing N N 328 
PRO CA  HA   sing N N 329 
PRO C   O    doub N N 330 
PRO C   OXT  sing N N 331 
PRO CB  CG   sing N N 332 
PRO CB  HB2  sing N N 333 
PRO CB  HB3  sing N N 334 
PRO CG  CD   sing N N 335 
PRO CG  HG2  sing N N 336 
PRO CG  HG3  sing N N 337 
PRO CD  HD2  sing N N 338 
PRO CD  HD3  sing N N 339 
PRO OXT HXT  sing N N 340 
RET C1  C2   sing N N 341 
RET C1  C6   sing N N 342 
RET C1  C16  sing N N 343 
RET C1  C17  sing N N 344 
RET C2  C3   sing N N 345 
RET C2  H21  sing N N 346 
RET C2  H22  sing N N 347 
RET C3  C4   sing N N 348 
RET C3  H31  sing N N 349 
RET C3  H32  sing N N 350 
RET C4  C5   sing N N 351 
RET C4  H41  sing N N 352 
RET C4  H42  sing N N 353 
RET C5  C6   doub N N 354 
RET C5  C18  sing N N 355 
RET C6  C7   sing N N 356 
RET C7  C8   doub N E 357 
RET C7  H7   sing N N 358 
RET C8  C9   sing N N 359 
RET C8  H8   sing N N 360 
RET C9  C10  doub N E 361 
RET C9  C19  sing N N 362 
RET C10 C11  sing N N 363 
RET C10 H10  sing N N 364 
RET C11 C12  doub N E 365 
RET C11 H11  sing N N 366 
RET C12 C13  sing N N 367 
RET C12 H12  sing N N 368 
RET C13 C14  doub N E 369 
RET C13 C20  sing N N 370 
RET C14 C15  sing N N 371 
RET C14 H14  sing N N 372 
RET C15 O1   doub N N 373 
RET C15 H15  sing N N 374 
RET C16 H161 sing N N 375 
RET C16 H162 sing N N 376 
RET C16 H163 sing N N 377 
RET C17 H171 sing N N 378 
RET C17 H172 sing N N 379 
RET C17 H173 sing N N 380 
RET C18 H181 sing N N 381 
RET C18 H182 sing N N 382 
RET C18 H183 sing N N 383 
RET C19 H191 sing N N 384 
RET C19 H192 sing N N 385 
RET C19 H193 sing N N 386 
RET C20 H201 sing N N 387 
RET C20 H202 sing N N 388 
RET C20 H203 sing N N 389 
SER N   CA   sing N N 390 
SER N   H    sing N N 391 
SER N   H2   sing N N 392 
SER CA  C    sing N N 393 
SER CA  CB   sing N N 394 
SER CA  HA   sing N N 395 
SER C   O    doub N N 396 
SER C   OXT  sing N N 397 
SER CB  OG   sing N N 398 
SER CB  HB2  sing N N 399 
SER CB  HB3  sing N N 400 
SER OG  HG   sing N N 401 
SER OXT HXT  sing N N 402 
THR N   CA   sing N N 403 
THR N   H    sing N N 404 
THR N   H2   sing N N 405 
THR CA  C    sing N N 406 
THR CA  CB   sing N N 407 
THR CA  HA   sing N N 408 
THR C   O    doub N N 409 
THR C   OXT  sing N N 410 
THR CB  OG1  sing N N 411 
THR CB  CG2  sing N N 412 
THR CB  HB   sing N N 413 
THR OG1 HG1  sing N N 414 
THR CG2 HG21 sing N N 415 
THR CG2 HG22 sing N N 416 
THR CG2 HG23 sing N N 417 
THR OXT HXT  sing N N 418 
TRP N   CA   sing N N 419 
TRP N   H    sing N N 420 
TRP N   H2   sing N N 421 
TRP CA  C    sing N N 422 
TRP CA  CB   sing N N 423 
TRP CA  HA   sing N N 424 
TRP C   O    doub N N 425 
TRP C   OXT  sing N N 426 
TRP CB  CG   sing N N 427 
TRP CB  HB2  sing N N 428 
TRP CB  HB3  sing N N 429 
TRP CG  CD1  doub Y N 430 
TRP CG  CD2  sing Y N 431 
TRP CD1 NE1  sing Y N 432 
TRP CD1 HD1  sing N N 433 
TRP CD2 CE2  doub Y N 434 
TRP CD2 CE3  sing Y N 435 
TRP NE1 CE2  sing Y N 436 
TRP NE1 HE1  sing N N 437 
TRP CE2 CZ2  sing Y N 438 
TRP CE3 CZ3  doub Y N 439 
TRP CE3 HE3  sing N N 440 
TRP CZ2 CH2  doub Y N 441 
TRP CZ2 HZ2  sing N N 442 
TRP CZ3 CH2  sing Y N 443 
TRP CZ3 HZ3  sing N N 444 
TRP CH2 HH2  sing N N 445 
TRP OXT HXT  sing N N 446 
TYR N   CA   sing N N 447 
TYR N   H    sing N N 448 
TYR N   H2   sing N N 449 
TYR CA  C    sing N N 450 
TYR CA  CB   sing N N 451 
TYR CA  HA   sing N N 452 
TYR C   O    doub N N 453 
TYR C   OXT  sing N N 454 
TYR CB  CG   sing N N 455 
TYR CB  HB2  sing N N 456 
TYR CB  HB3  sing N N 457 
TYR CG  CD1  doub Y N 458 
TYR CG  CD2  sing Y N 459 
TYR CD1 CE1  sing Y N 460 
TYR CD1 HD1  sing N N 461 
TYR CD2 CE2  doub Y N 462 
TYR CD2 HD2  sing N N 463 
TYR CE1 CZ   doub Y N 464 
TYR CE1 HE1  sing N N 465 
TYR CE2 CZ   sing Y N 466 
TYR CE2 HE2  sing N N 467 
TYR CZ  OH   sing N N 468 
TYR OH  HH   sing N N 469 
TYR OXT HXT  sing N N 470 
VAL N   CA   sing N N 471 
VAL N   H    sing N N 472 
VAL N   H2   sing N N 473 
VAL CA  C    sing N N 474 
VAL CA  CB   sing N N 475 
VAL CA  HA   sing N N 476 
VAL C   O    doub N N 477 
VAL C   OXT  sing N N 478 
VAL CB  CG1  sing N N 479 
VAL CB  CG2  sing N N 480 
VAL CB  HB   sing N N 481 
VAL CG1 HG11 sing N N 482 
VAL CG1 HG12 sing N N 483 
VAL CG1 HG13 sing N N 484 
VAL CG2 HG21 sing N N 485 
VAL CG2 HG22 sing N N 486 
VAL CG2 HG23 sing N N 487 
VAL OXT HXT  sing N N 488 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland      310030_197674   1 
'Swiss National Science Foundation' Switzerland      310030_207462   2 
Innosuisse                          'European Union' '42711.1 IP-LS' 3 
# 
_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   6C86 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_atom_sites.entry_id                    9GO1 
_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]   0.016287 
_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]   0.007057 
_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]   0.010593 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 27  ? 13.85693  11.09847  22.43722 1.000 53.34534  ? 50  MET A N   1 
ATOM   2    C CA  . MET A 1 27  ? 12.48980  11.50259  22.75245 1.000 81.01367  ? 50  MET A CA  1 
ATOM   3    C C   . MET A 1 27  ? 12.11855  11.14837  24.19332 1.000 91.55302  ? 50  MET A C   1 
ATOM   4    O O   . MET A 1 27  ? 12.57862  10.14017  24.73187 1.000 89.53643  ? 50  MET A O   1 
ATOM   5    C CB  . MET A 1 27  ? 11.50455  10.84727  21.78110 1.000 53.53992  ? 50  MET A CB  1 
ATOM   6    N N   . LEU A 1 28  ? 11.27336  11.97787  24.81036 1.000 79.25746  ? 51  LEU A N   1 
ATOM   7    C CA  . LEU A 1 28  ? 10.65052  11.66526  26.09180 1.000 64.26686  ? 51  LEU A CA  1 
ATOM   8    C C   . LEU A 1 28  ? 9.17853   11.28271  25.94403 1.000 64.34765  ? 51  LEU A C   1 
ATOM   9    O O   . LEU A 1 28  ? 8.38507   11.48038  26.86801 1.000 67.29752  ? 51  LEU A O   1 
ATOM   10   C CB  . LEU A 1 28  ? 10.79940  12.84043  27.05727 1.000 64.79637  ? 51  LEU A CB  1 
ATOM   11   N N   . PHE A 1 29  ? 8.80030   10.74113  24.78965 1.000 62.31708  ? 52  PHE A N   1 
ATOM   12   C CA  . PHE A 1 29  ? 7.61500   9.90693   24.65119 1.000 53.27886  ? 52  PHE A CA  1 
ATOM   13   C C   . PHE A 1 29  ? 8.02662   8.50370   24.22032 1.000 60.31122  ? 52  PHE A C   1 
ATOM   14   O O   . PHE A 1 29  ? 9.19220   8.23393   23.91569 1.000 49.04968  ? 52  PHE A O   1 
ATOM   15   C CB  . PHE A 1 29  ? 6.60446   10.50264  23.65360 1.000 41.95123  ? 52  PHE A CB  1 
ATOM   16   C CG  . PHE A 1 29  ? 7.22822   11.06671  22.40523 1.000 51.00768  ? 52  PHE A CG  1 
ATOM   17   C CD1 . PHE A 1 29  ? 7.69340   10.22753  21.40280 1.000 45.16627  ? 52  PHE A CD1 1 
ATOM   18   C CD2 . PHE A 1 29  ? 7.32910   12.43878  22.22536 1.000 43.67266  ? 52  PHE A CD2 1 
ATOM   19   C CE1 . PHE A 1 29  ? 8.26479   10.74601  20.25384 1.000 52.37607  ? 52  PHE A CE1 1 
ATOM   20   C CE2 . PHE A 1 29  ? 7.89596   12.96250  21.07783 1.000 49.33894  ? 52  PHE A CE2 1 
ATOM   21   C CZ  . PHE A 1 29  ? 8.36478   12.11367  20.08993 1.000 58.03319  ? 52  PHE A CZ  1 
ATOM   22   N N   . GLN A 1 30  ? 7.05010   7.60004   24.21432 1.000 57.48785  ? 53  GLN A N   1 
ATOM   23   C CA  . GLN A 1 30  ? 7.31969   6.21360   23.86489 1.000 46.64317  ? 53  GLN A CA  1 
ATOM   24   C C   . GLN A 1 30  ? 7.67011   6.09615   22.38580 1.000 62.41752  ? 53  GLN A C   1 
ATOM   25   O O   . GLN A 1 30  ? 6.94506   6.59362   21.51756 1.000 59.46811  ? 53  GLN A O   1 
ATOM   26   C CB  . GLN A 1 30  ? 6.10789   5.34445   24.19884 1.000 43.80030  ? 53  GLN A CB  1 
ATOM   27   C CG  . GLN A 1 30  ? 6.36023   3.85174   24.09418 1.000 48.49854  ? 53  GLN A CG  1 
ATOM   28   C CD  . GLN A 1 30  ? 7.56921   3.41074   24.89070 1.000 48.60422  ? 53  GLN A CD  1 
ATOM   29   O OE1 . GLN A 1 30  ? 7.65259   3.64394   26.09799 1.000 54.34998  ? 53  GLN A OE1 1 
ATOM   30   N NE2 . GLN A 1 30  ? 8.51246   2.75917   24.21904 1.000 45.38525  ? 53  GLN A NE2 1 
ATOM   31   N N   . THR A 1 31  ? 8.79427   5.43681   22.10456 1.000 57.29306  ? 54  THR A N   1 
ATOM   32   C CA  . THR A 1 31  ? 9.26115   5.21810   20.74510 1.000 48.60749  ? 54  THR A CA  1 
ATOM   33   C C   . THR A 1 31  ? 9.39083   3.75003   20.37296 1.000 66.13982  ? 54  THR A C   1 
ATOM   34   O O   . THR A 1 31  ? 9.47788   3.44164   19.17896 1.000 66.41487  ? 54  THR A O   1 
ATOM   35   C CB  . THR A 1 31  ? 10.61964  5.90359   20.52641 1.000 51.28903  ? 54  THR A CB  1 
ATOM   36   O OG1 . THR A 1 31  ? 11.56742  5.40252   21.47863 1.000 55.34911  ? 54  THR A OG1 1 
ATOM   37   C CG2 . THR A 1 31  ? 10.48998  7.40854   20.68467 1.000 46.58106  ? 54  THR A CG2 1 
ATOM   38   N N   . SER A 1 32  ? 9.41229   2.84587   21.34784 1.000 58.24840  ? 55  SER A N   1 
ATOM   39   C CA  . SER A 1 32  ? 9.50080   1.41347   21.10182 1.000 58.61916  ? 55  SER A CA  1 
ATOM   40   C C   . SER A 1 32  ? 8.12148   0.79120   21.27120 1.000 56.14878  ? 55  SER A C   1 
ATOM   41   O O   . SER A 1 32  ? 7.45809   1.00642   22.29210 1.000 49.59745  ? 55  SER A O   1 
ATOM   42   C CB  . SER A 1 32  ? 10.50780  0.75595   22.04795 1.000 54.16625  ? 55  SER A CB  1 
ATOM   43   O OG  . SER A 1 32  ? 9.95546   0.58086   23.34112 1.000 77.98906  ? 55  SER A OG  1 
ATOM   44   N N   . TYR A 1 33  ? 7.69426   0.02661   20.26907 1.000 57.06847  ? 56  TYR A N   1 
ATOM   45   C CA  . TYR A 1 33  ? 6.41720   -0.66916  20.31938 1.000 50.99630  ? 56  TYR A CA  1 
ATOM   46   C C   . TYR A 1 33  ? 6.49606   -1.92629  19.46462 1.000 44.50693  ? 56  TYR A C   1 
ATOM   47   O O   . TYR A 1 33  ? 7.41401   -2.09927  18.65963 1.000 74.63112  ? 56  TYR A O   1 
ATOM   48   C CB  . TYR A 1 33  ? 5.27711   0.24035   19.85387 1.000 39.26885  ? 56  TYR A CB  1 
ATOM   49   C CG  . TYR A 1 33  ? 5.42870   0.71116   18.42590 1.000 36.21062  ? 56  TYR A CG  1 
ATOM   50   C CD1 . TYR A 1 33  ? 6.23988   1.79600   18.11572 1.000 36.22567  ? 56  TYR A CD1 1 
ATOM   51   C CD2 . TYR A 1 33  ? 4.78175   0.05777   17.38503 1.000 46.64162  ? 56  TYR A CD2 1 
ATOM   52   C CE1 . TYR A 1 33  ? 6.38981   2.22836   16.80977 1.000 44.54042  ? 56  TYR A CE1 1 
ATOM   53   C CE2 . TYR A 1 33  ? 4.92722   0.48141   16.07557 1.000 59.30562  ? 56  TYR A CE2 1 
ATOM   54   C CZ  . TYR A 1 33  ? 5.73340   1.56554   15.79415 1.000 45.54609  ? 56  TYR A CZ  1 
ATOM   55   O OH  . TYR A 1 33  ? 5.87732   1.99077   14.49283 1.000 77.85153  ? 56  TYR A OH  1 
ATOM   56   N N   . THR A 1 34  ? 5.51173   -2.80596  19.64567 1.000 44.20978  ? 57  THR A N   1 
ATOM   57   C CA  . THR A 1 34  ? 5.32456   -3.97633  18.79832 1.000 46.29777  ? 57  THR A CA  1 
ATOM   58   C C   . THR A 1 34  ? 3.93357   -3.94390  18.18006 1.000 51.76932  ? 57  THR A C   1 
ATOM   59   O O   . THR A 1 34  ? 2.95244   -3.60215  18.84977 1.000 53.85582  ? 57  THR A O   1 
ATOM   60   C CB  . THR A 1 34  ? 5.50444   -5.28463  19.58732 1.000 53.34009  ? 57  THR A CB  1 
ATOM   61   O OG1 . THR A 1 34  ? 4.41254   -5.45305  20.50004 1.000 66.38747  ? 57  THR A OG1 1 
ATOM   62   C CG2 . THR A 1 34  ? 6.80740   -5.26031  20.37822 1.000 42.91532  ? 57  THR A CG2 1 
ATOM   63   N N   . LEU A 1 35  ? 3.85830   -4.27812  16.89412 1.000 56.27520  ? 58  LEU A N   1 
ATOM   64   C CA  . LEU A 1 35  ? 2.58672   -4.60440  16.26270 1.000 68.66924  ? 58  LEU A CA  1 
ATOM   65   C C   . LEU A 1 35  ? 2.21017   -6.04984  16.56668 1.000 66.48707  ? 58  LEU A C   1 
ATOM   66   O O   . LEU A 1 35  ? 3.04219   -6.95523  16.44630 1.000 80.71864  ? 58  LEU A O   1 
ATOM   67   C CB  . LEU A 1 35  ? 2.66961   -4.39446  14.74993 1.000 78.45747  ? 58  LEU A CB  1 
ATOM   68   C CG  . LEU A 1 35  ? 2.88173   -2.98292  14.19513 1.000 58.76322  ? 58  LEU A CG  1 
ATOM   69   C CD1 . LEU A 1 35  ? 2.31092   -2.85741  12.79299 1.000 60.81335  ? 58  LEU A CD1 1 
ATOM   70   C CD2 . LEU A 1 35  ? 2.26628   -1.95235  15.09458 1.000 51.14441  ? 58  LEU A CD2 1 
ATOM   71   N N   . GLU A 1 36  ? 0.95741   -6.26676  16.95909 1.000 54.25844  ? 59  GLU A N   1 
ATOM   72   C CA  . GLU A 1 36  ? 0.43451   -7.60650  17.17826 1.000 70.92756  ? 59  GLU A CA  1 
ATOM   73   C C   . GLU A 1 36  ? -0.83475  -7.79237  16.35686 1.000 71.24508  ? 59  GLU A C   1 
ATOM   74   O O   . GLU A 1 36  ? -1.39979  -6.83296  15.82271 1.000 68.79421  ? 59  GLU A O   1 
ATOM   75   C CB  . GLU A 1 36  ? 0.14943   -7.85908  18.66639 1.000 56.18567  ? 59  GLU A CB  1 
ATOM   76   C CG  . GLU A 1 36  ? 1.35881   -7.69146  19.57368 1.000 59.05589  ? 59  GLU A CG  1 
ATOM   77   C CD  . GLU A 1 36  ? 2.40456   -8.76967  19.36339 1.000 73.79708  ? 59  GLU A CD  1 
ATOM   78   O OE1 . GLU A 1 36  ? 2.03011   -9.90309  18.99214 1.000 76.29657  ? 59  GLU A OE1 1 
ATOM   79   O OE2 . GLU A 1 36  ? 3.60263   -8.48311  19.57132 1.000 73.79034  ? 59  GLU A OE2 1 
ATOM   80   N N   . ASN A 1 37  ? -1.28827  -9.04693  16.28338 1.000 65.40311  ? 60  ASN A N   1 
ATOM   81   C CA  . ASN A 1 37  ? -2.56490  -9.40511  15.66166 1.000 58.89911  ? 60  ASN A CA  1 
ATOM   82   C C   . ASN A 1 37  ? -2.69152  -8.80457  14.26156 1.000 78.27386  ? 60  ASN A C   1 
ATOM   83   O O   . ASN A 1 37  ? -3.68681  -8.15681  13.92528 1.000 79.64193  ? 60  ASN A O   1 
ATOM   84   C CB  . ASN A 1 37  ? -3.73687  -8.98111  16.54881 1.000 55.06513  ? 60  ASN A CB  1 
ATOM   85   C CG  . ASN A 1 37  ? -3.81768  -9.78644  17.83059 1.000 74.03166  ? 60  ASN A CG  1 
ATOM   86   O OD1 . ASN A 1 37  ? -2.92582  -10.57895 18.13465 1.000 83.40091  ? 60  ASN A OD1 1 
ATOM   87   N ND2 . ASN A 1 37  ? -4.88787  -9.58369  18.59335 1.000 65.81514  ? 60  ASN A ND2 1 
ATOM   88   N N   . ASN A 1 38  ? -1.65435  -9.01385  13.44283 1.000 67.23771  ? 61  ASN A N   1 
ATOM   89   C CA  . ASN A 1 38  ? -1.66080  -8.57934  12.04333 1.000 85.38305  ? 61  ASN A CA  1 
ATOM   90   C C   . ASN A 1 38  ? -1.74367  -7.05597  11.96714 1.000 89.72556  ? 61  ASN A C   1 
ATOM   91   O O   . ASN A 1 38  ? -2.48847  -6.48883  11.16370 1.000 81.94891  ? 61  ASN A O   1 
ATOM   92   C CB  . ASN A 1 38  ? -2.79325  -9.23807  11.24662 1.000 93.32421  ? 61  ASN A CB  1 
ATOM   93   C CG  . ASN A 1 38  ? -2.62816  -9.07437  9.74200  1.000 99.05169  ? 61  ASN A CG  1 
ATOM   94   O OD1 . ASN A 1 38  ? -1.53443  -8.79274  9.25134  1.000 111.36783 ? 61  ASN A OD1 1 
ATOM   95   N ND2 . ASN A 1 38  ? -3.72159  -9.24158  9.00492  1.000 93.15768  ? 61  ASN A ND2 1 
ATOM   96   N N   . GLY A 1 39  ? -0.97362  -6.38795  12.82390 1.000 83.32132  ? 62  GLY A N   1 
ATOM   97   C CA  . GLY A 1 39  ? -0.87897  -4.94580  12.78549 1.000 76.40401  ? 62  GLY A CA  1 
ATOM   98   C C   . GLY A 1 39  ? -2.05629  -4.21046  13.38099 1.000 68.05690  ? 62  GLY A C   1 
ATOM   99   O O   . GLY A 1 39  ? -2.17614  -2.99720  13.17164 1.000 67.28571  ? 62  GLY A O   1 
ATOM   100  N N   . SER A 1 40  ? -2.92803  -4.89815  14.12089 1.000 54.74123  ? 63  SER A N   1 
ATOM   101  C CA  . SER A 1 40  ? -4.12943  -4.27836  14.65548 1.000 53.60703  ? 63  SER A CA  1 
ATOM   102  C C   . SER A 1 40  ? -3.99327  -3.87566  16.12302 1.000 50.47799  ? 63  SER A C   1 
ATOM   103  O O   . SER A 1 40  ? -4.87464  -3.17279  16.63207 1.000 53.74524  ? 63  SER A O   1 
ATOM   104  C CB  . SER A 1 40  ? -5.33225  -5.22801  14.48822 1.000 52.02818  ? 63  SER A CB  1 
ATOM   105  O OG  . SER A 1 40  ? -5.17904  -6.40496  15.26508 1.000 61.57969  ? 63  SER A OG  1 
ATOM   106  N N   . VAL A 1 41  ? -2.92994  -4.30563  16.81503 1.000 39.97886  ? 64  VAL A N   1 
ATOM   107  C CA  . VAL A 1 41  ? -2.71802  -3.98331  18.22281 1.000 46.52619  ? 64  VAL A CA  1 
ATOM   108  C C   . VAL A 1 41  ? -1.28372  -3.49997  18.38676 1.000 46.77905  ? 64  VAL A C   1 
ATOM   109  O O   . VAL A 1 41  ? -0.35316  -4.09571  17.82239 1.000 56.93249  ? 64  VAL A O   1 
ATOM   110  C CB  . VAL A 1 41  ? -2.98233  -5.20171  19.12795 1.000 40.93839  ? 64  VAL A CB  1 
ATOM   111  C CG1 . VAL A 1 41  ? -2.65618  -4.87622  20.56296 1.000 46.42626  ? 64  VAL A CG1 1 
ATOM   112  C CG2 . VAL A 1 41  ? -4.40667  -5.68615  18.99538 1.000 51.24010  ? 64  VAL A CG2 1 
ATOM   113  N N   . ILE A 1 42  ? -1.11441  -2.40166  19.13213 1.000 38.23122  ? 65  ILE A N   1 
ATOM   114  C CA  . ILE A 1 42  ? 0.19801   -1.91140  19.52181 1.000 52.27048  ? 65  ILE A CA  1 
ATOM   115  C C   . ILE A 1 42  ? 0.34233   -2.07396  21.04246 1.000 50.33096  ? 65  ILE A C   1 
ATOM   116  O O   . ILE A 1 42  ? -0.55611  -1.69455  21.80630 1.000 53.59585  ? 65  ILE A O   1 
ATOM   117  C CB  . ILE A 1 42  ? 0.41041   -0.46728  19.04020 1.000 43.57906  ? 65  ILE A CB  1 
ATOM   118  C CG1 . ILE A 1 42  ? 0.31409   -0.38746  17.48440 1.000 48.61699  ? 65  ILE A CG1 1 
ATOM   119  C CG2 . ILE A 1 42  ? 1.76360   0.07977   19.59854 1.000 52.58862  ? 65  ILE A CG2 1 
ATOM   120  C CD1 . ILE A 1 42  ? 0.43237   1.03686   16.98587 1.000 50.77669  ? 65  ILE A CD1 1 
ATOM   121  N N   . CYS A 1 43  ? 1.45393   -2.66992  21.46086 1.000 39.74089  ? 66  CYS A N   1 
ATOM   122  C CA  . CYS A 1 43  ? 1.85214   -2.88251  22.84651 1.000 52.96909  ? 66  CYS A CA  1 
ATOM   123  C C   . CYS A 1 43  ? 3.11048   -2.09721  23.18624 1.000 46.95282  ? 66  CYS A C   1 
ATOM   124  O O   . CYS A 1 43  ? 4.04429   -2.03357  22.37965 1.000 49.83260  ? 66  CYS A O   1 
ATOM   125  C CB  . CYS A 1 43  ? 2.07216   -4.37090  23.09920 1.000 56.96109  ? 66  CYS A CB  1 
ATOM   126  S SG  . CYS A 1 43  ? 0.61491   -5.40836  22.78149 1.000 61.21789  ? 66  CYS A SG  1 
ATOM   127  N N   . ILE A 1 44  ? 3.13299   -1.52581  24.38978 1.000 38.99984  ? 67  ILE A N   1 
ATOM   128  C CA  . ILE A 1 44  ? 4.22836   -0.65851  24.81139 1.000 48.67546  ? 67  ILE A CA  1 
ATOM   129  C C   . ILE A 1 44  ? 4.60802   -1.04197  26.24161 1.000 36.00913  ? 67  ILE A C   1 
ATOM   130  O O   . ILE A 1 44  ? 3.81844   -1.63665  26.97363 1.000 34.18042  ? 67  ILE A O   1 
ATOM   131  C CB  . ILE A 1 44  ? 3.82847   0.83683   24.79552 1.000 63.98261  ? 67  ILE A CB  1 
ATOM   132  C CG1 . ILE A 1 44  ? 2.47924   1.07328   25.48267 1.000 49.12793  ? 67  ILE A CG1 1 
ATOM   133  C CG2 . ILE A 1 44  ? 3.69972   1.35600   23.37107 1.000 31.33561  ? 67  ILE A CG2 1 
ATOM   134  C CD1 . ILE A 1 44  ? 2.38597   2.44613   26.11603 1.000 42.26277  ? 67  ILE A CD1 1 
ATOM   135  N N   . PRO A 1 45  ? 5.84096   -0.71559  26.63100 1.000 36.46672  ? 68  PRO A N   1 
ATOM   136  C CA  . PRO A 1 45  ? 6.19513   -0.85340  28.04500 1.000 43.33088  ? 68  PRO A CA  1 
ATOM   137  C C   . PRO A 1 45  ? 5.28097   0.05544   28.85236 1.000 37.14274  ? 68  PRO A C   1 
ATOM   138  O O   . PRO A 1 45  ? 5.01917   1.20153   28.48189 1.000 48.17843  ? 68  PRO A O   1 
ATOM   139  C CB  . PRO A 1 45  ? 7.66332   -0.40357  28.09714 1.000 46.69266  ? 68  PRO A CB  1 
ATOM   140  C CG  . PRO A 1 45  ? 8.15246   -0.45724  26.70002 1.000 50.07737  ? 68  PRO A CG  1 
ATOM   141  C CD  . PRO A 1 45  ? 6.96522   -0.23368  25.81765 1.000 40.36813  ? 68  PRO A CD  1 
ATOM   142  N N   . ASN A 1 46  ? 4.78907   -0.47724  29.96970 1.000 35.96887  ? 69  ASN A N   1 
ATOM   143  C CA  . ASN A 1 46  ? 4.02275   0.29773   30.94657 1.000 26.01840  ? 69  ASN A CA  1 
ATOM   144  C C   . ASN A 1 46  ? 4.94980   1.09749   31.86127 1.000 40.09134  ? 69  ASN A C   1 
ATOM   145  O O   . ASN A 1 46  ? 5.07812   0.84391   33.06027 1.000 40.79457  ? 69  ASN A O   1 
ATOM   146  C CB  . ASN A 1 46  ? 3.11258   -0.61694  31.75148 1.000 36.67341  ? 69  ASN A CB  1 
ATOM   147  C CG  . ASN A 1 46  ? 2.06655   0.15159   32.53399 1.000 38.88437  ? 69  ASN A CG  1 
ATOM   148  O OD1 . ASN A 1 46  ? 2.05274   1.38438   32.52903 1.000 61.90174  ? 69  ASN A OD1 1 
ATOM   149  N ND2 . ASN A 1 46  ? 1.18322   -0.57230  33.21421 1.000 52.71733  ? 69  ASN A ND2 1 
ATOM   150  N N   . ASN A 1 47  ? 5.58577   2.10419   31.26401 1.000 48.62778  ? 70  ASN A N   1 
ATOM   151  C CA  . ASN A 1 47  ? 6.58390   2.92096   31.93963 1.000 41.85343  ? 70  ASN A CA  1 
ATOM   152  C C   . ASN A 1 47  ? 6.09253   4.34377   32.19072 1.000 48.92219  ? 70  ASN A C   1 
ATOM   153  O O   . ASN A 1 47  ? 6.89267   5.21574   32.54840 1.000 59.36943  ? 70  ASN A O   1 
ATOM   154  C CB  . ASN A 1 47  ? 7.88589   2.93491   31.13349 1.000 41.52327  ? 70  ASN A CB  1 
ATOM   155  C CG  . ASN A 1 47  ? 7.69260   3.43917   29.71292 1.000 46.58445  ? 70  ASN A CG  1 
ATOM   156  O OD1 . ASN A 1 47  ? 6.58151   3.78491   29.30458 1.000 58.75525  ? 70  ASN A OD1 1 
ATOM   157  N ND2 . ASN A 1 47  ? 8.77988   3.47532   28.94785 1.000 56.06460  ? 70  ASN A ND2 1 
ATOM   158  N N   . GLY A 1 48  ? 4.79290   4.59332   32.01328 1.000 38.78880  ? 71  GLY A N   1 
ATOM   159  C CA  . GLY A 1 48  ? 4.19378   5.89668   32.21240 1.000 45.20084  ? 71  GLY A CA  1 
ATOM   160  C C   . GLY A 1 48  ? 4.25202   6.85219   31.04089 1.000 54.73087  ? 71  GLY A C   1 
ATOM   161  O O   . GLY A 1 48  ? 3.57025   7.88499   31.07505 1.000 51.43865  ? 71  GLY A O   1 
ATOM   162  N N   . GLN A 1 49  ? 5.02013   6.53921   30.00139 1.000 40.52947  ? 72  GLN A N   1 
ATOM   163  C CA  . GLN A 1 49  ? 5.16746   7.44169   28.86570 1.000 37.88457  ? 72  GLN A CA  1 
ATOM   164  C C   . GLN A 1 49  ? 3.96592   7.35650   27.93002 1.000 37.14121  ? 72  GLN A C   1 
ATOM   165  O O   . GLN A 1 49  ? 3.35830   6.29540   27.75598 1.000 48.58548  ? 72  GLN A O   1 
ATOM   166  C CB  . GLN A 1 49  ? 6.45032   7.13764   28.09841 1.000 45.37887  ? 72  GLN A CB  1 
ATOM   167  C CG  . GLN A 1 49  ? 7.71286   7.43032   28.88915 1.000 51.11895  ? 72  GLN A CG  1 
ATOM   168  C CD  . GLN A 1 49  ? 8.96523   7.35385   28.03958 1.000 57.10397  ? 72  GLN A CD  1 
ATOM   169  O OE1 . GLN A 1 49  ? 8.90185   7.04754   26.84894 1.000 72.70910  ? 72  GLN A OE1 1 
ATOM   170  N NE2 . GLN A 1 49  ? 10.11429  7.61814   28.65109 1.000 88.01748  ? 72  GLN A NE2 1 
ATOM   171  N N   . CYS A 1 50  ? 3.63635   8.49363   27.31745 1.000 33.29177  ? 73  CYS A N   1 
ATOM   172  C CA  . CYS A 1 50  ? 2.62035   8.57738   26.28066 1.000 30.98246  ? 73  CYS A CA  1 
ATOM   173  C C   . CYS A 1 50  ? 3.16703   8.03166   24.95970 1.000 40.77204  ? 73  CYS A C   1 
ATOM   174  O O   . CYS A 1 50  ? 4.37940   8.02741   24.71008 1.000 46.38537  ? 73  CYS A O   1 
ATOM   175  C CB  . CYS A 1 50  ? 2.17253   10.02705  26.10651 1.000 28.44112  ? 73  CYS A CB  1 
ATOM   176  S SG  . CYS A 1 50  ? 1.64973   10.79835  27.66253 1.000 30.14081  ? 73  CYS A SG  1 
ATOM   177  N N   . PHE A 1 51  ? 2.25438   7.60357   24.08790 1.000 39.53796  ? 74  PHE A N   1 
ATOM   178  C CA  . PHE A 1 51  ? 2.62653   6.98651   22.82087 1.000 46.09113  ? 74  PHE A CA  1 
ATOM   179  C C   . PHE A 1 51  ? 1.66648   7.45042   21.73605 1.000 33.40237  ? 74  PHE A C   1 
ATOM   180  O O   . PHE A 1 51  ? 0.45917   7.58147   21.97391 1.000 38.44172  ? 74  PHE A O   1 
ATOM   181  C CB  . PHE A 1 51  ? 2.62965   5.45104   22.90262 1.000 48.24567  ? 74  PHE A CB  1 
ATOM   182  C CG  . PHE A 1 51  ? 2.72502   4.77030   21.55788 1.000 36.28843  ? 74  PHE A CG  1 
ATOM   183  C CD1 . PHE A 1 51  ? 3.95745   4.59001   20.94195 1.000 25.84082  ? 74  PHE A CD1 1 
ATOM   184  C CD2 . PHE A 1 51  ? 1.58818   4.29452   20.92330 1.000 28.26519  ? 74  PHE A CD2 1 
ATOM   185  C CE1 . PHE A 1 51  ? 4.04524   3.96615   19.71100 1.000 38.50628  ? 74  PHE A CE1 1 
ATOM   186  C CE2 . PHE A 1 51  ? 1.67016   3.66581   19.69918 1.000 30.66955  ? 74  PHE A CE2 1 
ATOM   187  C CZ  . PHE A 1 51  ? 2.89729   3.50121   19.09018 1.000 43.16167  ? 74  PHE A CZ  1 
ATOM   188  N N   . CYS A 1 52  ? 2.21698   7.70650   20.55020 1.000 31.61496  ? 75  CYS A N   1 
ATOM   189  C CA  . CYS A 1 52  ? 1.40956   7.94327   19.36562 1.000 29.28569  ? 75  CYS A CA  1 
ATOM   190  C C   . CYS A 1 52  ? 2.27920   7.82160   18.12437 1.000 34.95567  ? 75  CYS A C   1 
ATOM   191  O O   . CYS A 1 52  ? 3.41259   8.31504   18.09906 1.000 34.36144  ? 75  CYS A O   1 
ATOM   192  C CB  . CYS A 1 52  ? 0.75762   9.32676   19.39650 1.000 28.30285  ? 75  CYS A CB  1 
ATOM   193  S SG  . CYS A 1 52  ? -0.68726  9.48512   18.32468 1.000 36.81202  ? 75  CYS A SG  1 
ATOM   194  N N   . LEU A 1 53  ? 1.74605   7.14580   17.10543 1.000 36.09051  ? 76  LEU A N   1 
ATOM   195  C CA  . LEU A 1 53  ? 2.51090   6.93182   15.88382 1.000 42.76671  ? 76  LEU A CA  1 
ATOM   196  C C   . LEU A 1 53  ? 2.77568   8.26312   15.19274 1.000 49.33452  ? 76  LEU A C   1 
ATOM   197  O O   . LEU A 1 53  ? 3.86808   8.48367   14.65639 1.000 56.14757  ? 76  LEU A O   1 
ATOM   198  C CB  . LEU A 1 53  ? 1.75546   5.97252   14.96590 1.000 27.55249  ? 76  LEU A CB  1 
ATOM   199  C CG  . LEU A 1 53  ? 1.89725   4.48933   15.29750 1.000 28.02217  ? 76  LEU A CG  1 
ATOM   200  C CD1 . LEU A 1 53  ? 1.03677   3.65889   14.35684 1.000 44.57182  ? 76  LEU A CD1 1 
ATOM   201  C CD2 . LEU A 1 53  ? 3.35503   4.05583   15.22473 1.000 46.26897  ? 76  LEU A CD2 1 
ATOM   202  N N   . ALA A 1 54  ? 1.77106   9.14907   15.18029 1.000 39.02571  ? 77  ALA A N   1 
ATOM   203  C CA  . ALA A 1 54  ? 1.87734   10.41794  14.46698 1.000 43.85415  ? 77  ALA A CA  1 
ATOM   204  C C   . ALA A 1 54  ? 3.09542   11.20306  14.93024 1.000 45.34676  ? 77  ALA A C   1 
ATOM   205  O O   . ALA A 1 54  ? 3.72456   11.90819  14.13211 1.000 48.82642  ? 77  ALA A O   1 
ATOM   206  C CB  . ALA A 1 54  ? 0.60555   11.24316  14.65728 1.000 41.15807  ? 77  ALA A CB  1 
ATOM   207  N N   . TRP A 1 55  ? 3.43630   11.09669  16.21866 1.000 43.58561  ? 78  TRP A N   1 
ATOM   208  C CA  . TRP A 1 55  ? 4.57017   11.82934  16.76735 1.000 43.18473  ? 78  TRP A CA  1 
ATOM   209  C C   . TRP A 1 55  ? 5.89241   11.34052  16.19855 1.000 49.94496  ? 78  TRP A C   1 
ATOM   210  O O   . TRP A 1 55  ? 6.87726   12.08705  16.22805 1.000 56.92784  ? 78  TRP A O   1 
ATOM   211  C CB  . TRP A 1 55  ? 4.61051   11.72824  18.29491 1.000 29.24129  ? 78  TRP A CB  1 
ATOM   212  C CG  . TRP A 1 55  ? 3.41267   12.27504  18.99589 1.000 27.10612  ? 78  TRP A CG  1 
ATOM   213  C CD1 . TRP A 1 55  ? 2.54088   13.21570  18.52514 1.000 29.39987  ? 78  TRP A CD1 1 
ATOM   214  C CD2 . TRP A 1 55  ? 2.96912   11.93951  20.31535 1.000 29.54804  ? 78  TRP A CD2 1 
ATOM   215  N NE1 . TRP A 1 55  ? 1.57137   13.47552  19.46728 1.000 32.38405  ? 78  TRP A NE1 1 
ATOM   216  C CE2 . TRP A 1 55  ? 1.81228   12.70303  20.57498 1.000 35.54722  ? 78  TRP A CE2 1 
ATOM   217  C CE3 . TRP A 1 55  ? 3.43268   11.06008  21.29966 1.000 43.66441  ? 78  TRP A CE3 1 
ATOM   218  C CZ2 . TRP A 1 55  ? 1.11146   12.61350  21.78051 1.000 28.47059  ? 78  TRP A CZ2 1 
ATOM   219  C CZ3 . TRP A 1 55  ? 2.73546   10.97359  22.49784 1.000 41.34429  ? 78  TRP A CZ3 1 
ATOM   220  C CH2 . TRP A 1 55  ? 1.58865   11.74793  22.72672 1.000 26.34438  ? 78  TRP A CH2 1 
ATOM   221  N N   . LEU A 1 56  ? 5.94921   10.10937  15.69840 1.000 50.72788  ? 79  LEU A N   1 
ATOM   222  C CA  . LEU A 1 56  ? 7.22388   9.53542   15.30185 1.000 47.83731  ? 79  LEU A CA  1 
ATOM   223  C C   . LEU A 1 56  ? 7.53920   9.77466   13.83034 1.000 48.75274  ? 79  LEU A C   1 
ATOM   224  O O   . LEU A 1 56  ? 8.60118   9.34690   13.36824 1.000 72.71469  ? 79  LEU A O   1 
ATOM   225  C CB  . LEU A 1 56  ? 7.24452   8.03188   15.60376 1.000 45.76561  ? 79  LEU A CB  1 
ATOM   226  C CG  . LEU A 1 56  ? 6.81283   7.61888   17.01475 1.000 38.69721  ? 79  LEU A CG  1 
ATOM   227  C CD1 . LEU A 1 56  ? 6.47834   6.13724   17.05961 1.000 40.85744  ? 79  LEU A CD1 1 
ATOM   228  C CD2 . LEU A 1 56  ? 7.87287   7.97123   18.05408 1.000 42.41977  ? 79  LEU A CD2 1 
ATOM   229  N N   . LYS A 1 57  ? 6.62941   10.40272  13.08094 1.000 38.79379  ? 80  LYS A N   1 
ATOM   230  C CA  . LYS A 1 57  ? 6.92268   10.79048  11.70935 1.000 53.70873  ? 80  LYS A CA  1 
ATOM   231  C C   . LYS A 1 57  ? 8.20426   11.61285  11.69044 1.000 62.33540  ? 80  LYS A C   1 
ATOM   232  O O   . LYS A 1 57  ? 8.45344   12.40844  12.60082 1.000 53.85408  ? 80  LYS A O   1 
ATOM   233  C CB  . LYS A 1 57  ? 5.75616   11.57310  11.11024 1.000 47.21607  ? 80  LYS A CB  1 
ATOM   234  C CG  . LYS A 1 57  ? 4.57158   10.68077  10.77832 1.000 45.68329  ? 80  LYS A CG  1 
ATOM   235  C CD  . LYS A 1 57  ? 3.45190   11.43896  10.08747 1.000 48.47397  ? 80  LYS A CD  1 
ATOM   236  C CE  . LYS A 1 57  ? 3.01964   12.64757  10.89783 1.000 58.62604  ? 80  LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 57  ? 1.54174   12.66887  11.09271 1.000 65.68423  ? 80  LYS A NZ  1 
ATOM   238  N N   . SER A 1 58  ? 9.00987   11.44363  10.64324 1.000 56.24115  ? 81  SER A N   1 
ATOM   239  C CA  . SER A 1 58  ? 10.26834  12.17518  10.58488 1.000 52.61199  ? 81  SER A CA  1 
ATOM   240  C C   . SER A 1 58  ? 10.02494  13.67823  10.50099 1.000 67.32048  ? 81  SER A C   1 
ATOM   241  O O   . SER A 1 58  ? 9.02317   14.14496  9.95082  1.000 59.04746  ? 81  SER A O   1 
ATOM   242  C CB  . SER A 1 58  ? 11.10025  11.71526  9.38811  1.000 72.05736  ? 81  SER A CB  1 
ATOM   243  O OG  . SER A 1 58  ? 10.48896  12.08933  8.16370  1.000 86.69443  ? 81  SER A OG  1 
ATOM   244  N N   . ASN A 1 59  ? 10.96383  14.43507  11.06772 1.000 63.02714  ? 82  ASN A N   1 
ATOM   245  C CA  . ASN A 1 59  ? 10.99378  15.88511  10.94905 1.000 55.74064  ? 82  ASN A CA  1 
ATOM   246  C C   . ASN A 1 59  ? 11.61000  16.35282  9.63752  1.000 75.17526  ? 82  ASN A C   1 
ATOM   247  O O   . ASN A 1 59  ? 11.49799  17.53978  9.30978  1.000 68.22975  ? 82  ASN A O   1 
ATOM   248  C CB  . ASN A 1 59  ? 11.75753  16.49732  12.12764 1.000 75.37625  ? 82  ASN A CB  1 
ATOM   249  C CG  . ASN A 1 59  ? 11.08149  16.23628  13.46306 1.000 61.10157  ? 82  ASN A CG  1 
ATOM   250  O OD1 . ASN A 1 59  ? 9.85255   16.23415  13.56296 1.000 43.28180  ? 82  ASN A OD1 1 
ATOM   251  N ND2 . ASN A 1 59  ? 11.88637  16.01210  14.49933 1.000 52.06850  ? 82  ASN A ND2 1 
ATOM   252  N N   . GLY A 1 60  ? 12.24328  15.45786  8.88345  1.000 79.00616  ? 83  GLY A N   1 
ATOM   253  C CA  . GLY A 1 60  ? 12.74461  15.77067  7.56669  1.000 59.53717  ? 83  GLY A CA  1 
ATOM   254  C C   . GLY A 1 60  ? 14.10419  15.15015  7.32293  1.000 60.84339  ? 83  GLY A C   1 
ATOM   255  O O   . GLY A 1 60  ? 14.62826  14.39169  8.13763  1.000 59.60545  ? 83  GLY A O   1 
ATOM   256  N N   . THR A 1 61  ? 14.66891  15.50038  6.17100  1.000 72.26784  ? 84  THR A N   1 
ATOM   257  C CA  . THR A 1 61  ? 15.96029  15.01177  5.71073  1.000 85.09885  ? 84  THR A CA  1 
ATOM   258  C C   . THR A 1 61  ? 17.12681  15.62145  6.48780  1.000 80.17198  ? 84  THR A C   1 
ATOM   259  O O   . THR A 1 61  ? 16.99831  16.63434  7.18168  1.000 74.19585  ? 84  THR A O   1 
ATOM   260  C CB  . THR A 1 61  ? 16.13368  15.30303  4.21781  1.000 84.45317  ? 84  THR A CB  1 
ATOM   261  O OG1 . THR A 1 61  ? 16.58953  16.65108  4.03721  1.000 82.19809  ? 84  THR A OG1 1 
ATOM   262  C CG2 . THR A 1 61  ? 14.81316  15.11690  3.48410  1.000 49.69947  ? 84  THR A CG2 1 
ATOM   263  N N   . ASN A 1 62  ? 18.28278  14.95681  6.36850  1.000 96.44879  ? 85  ASN A N   1 
ATOM   264  C CA  . ASN A 1 62  ? 19.50809  15.43348  7.00394  1.000 89.44818  ? 85  ASN A CA  1 
ATOM   265  C C   . ASN A 1 62  ? 19.93676  16.76472  6.40333  1.000 83.82245  ? 85  ASN A C   1 
ATOM   266  O O   . ASN A 1 62  ? 20.52405  17.60268  7.09780  1.000 74.41622  ? 85  ASN A O   1 
ATOM   267  C CB  . ASN A 1 62  ? 20.62080  14.39277  6.85840  1.000 99.60164  ? 85  ASN A CB  1 
ATOM   268  C CG  . ASN A 1 62  ? 20.47329  13.23350  7.83124  1.000 112.14355 ? 85  ASN A CG  1 
ATOM   269  O OD1 . ASN A 1 62  ? 21.46377  12.63669  8.25549  1.000 139.44173 ? 85  ASN A OD1 1 
ATOM   270  N ND2 . ASN A 1 62  ? 19.23578  12.90929  8.18777  1.000 83.82945  ? 85  ASN A ND2 1 
ATOM   271  N N   . ALA A 1 63  ? 19.63986  16.97384  5.11775  1.000 90.56515  ? 86  ALA A N   1 
ATOM   272  C CA  . ALA A 1 63  ? 19.97754  18.22503  4.44691  1.000 89.36262  ? 86  ALA A CA  1 
ATOM   273  C C   . ALA A 1 63  ? 19.18586  19.36428  5.07015  1.000 91.62405  ? 86  ALA A C   1 
ATOM   274  O O   . ALA A 1 63  ? 19.72477  20.44851  5.32036  1.000 75.63104  ? 86  ALA A O   1 
ATOM   275  C CB  . ALA A 1 63  ? 19.70293  18.11765  2.94675  1.000 81.00003  ? 86  ALA A CB  1 
ATOM   276  N N   . GLU A 1 64  ? 17.89641  19.12874  5.30827  1.000 99.88535  ? 87  GLU A N   1 
ATOM   277  C CA  . GLU A 1 64  ? 17.05070  20.10365  5.98482  1.000 72.83776  ? 87  GLU A CA  1 
ATOM   278  C C   . GLU A 1 64  ? 17.59797  20.39359  7.37953  1.000 71.27329  ? 87  GLU A C   1 
ATOM   279  O O   . GLU A 1 64  ? 17.64218  21.55346  7.80681  1.000 68.77647  ? 87  GLU A O   1 
ATOM   280  C CB  . GLU A 1 64  ? 15.61612  19.58675  6.02349  1.000 56.44078  ? 87  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 64  ? 14.91262  19.70993  4.67796  1.000 50.03154  ? 87  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 64  ? 13.46420  19.27377  4.72334  1.000 64.79544  ? 87  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 64  ? 13.15245  18.33585  5.48831  1.000 65.62891  ? 87  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 64  ? 12.63845  19.86614  3.99539  1.000 74.27305  ? 87  GLU A OE2 1 
ATOM   285  N N   . LYS A 1 65  ? 18.01683  19.35174  8.10670  1.000 77.37684  ? 88  LYS A N   1 
ATOM   286  C CA  . LYS A 1 65  ? 18.55616  19.55349  9.44966  1.000 82.35956  ? 88  LYS A CA  1 
ATOM   287  C C   . LYS A 1 65  ? 19.81073  20.41207  9.39750  1.000 79.15440  ? 88  LYS A C   1 
ATOM   288  O O   . LYS A 1 65  ? 19.97728  21.33239  10.20553 1.000 83.15469  ? 88  LYS A O   1 
ATOM   289  C CB  . LYS A 1 65  ? 18.87573  18.20645  10.09995 1.000 89.94129  ? 88  LYS A CB  1 
ATOM   290  C CG  . LYS A 1 65  ? 19.47804  18.31226  11.50046 1.000 95.07487  ? 88  LYS A CG  1 
ATOM   291  C CD  . LYS A 1 65  ? 18.51485  18.58069  12.63404 1.000 94.45934  ? 88  LYS A CD  1 
ATOM   292  C CE  . LYS A 1 65  ? 19.02479  17.87063  13.88809 1.000 105.98512 ? 88  LYS A CE  1 
ATOM   293  N NZ  . LYS A 1 65  ? 19.05601  18.75471  15.08978 1.000 85.22842  ? 88  LYS A NZ  1 
ATOM   294  N N   . LEU A 1 66  ? 20.71556  20.11814  8.46208  1.000 92.04583  ? 89  LEU A N   1 
ATOM   295  C CA  . LEU A 1 66  ? 21.96764  20.86284  8.40524  1.000 108.46606 ? 89  LEU A CA  1 
ATOM   296  C C   . LEU A 1 66  ? 21.67180  22.33513  8.14421  1.000 90.13007  ? 89  LEU A C   1 
ATOM   297  O O   . LEU A 1 66  ? 22.21014  23.22310  8.81520  1.000 90.87941  ? 89  LEU A O   1 
ATOM   298  C CB  . LEU A 1 66  ? 22.88108  20.27147  7.32903  1.000 98.76744  ? 89  LEU A CB  1 
ATOM   299  C CG  . LEU A 1 66  ? 24.32316  20.77491  7.27675  1.000 81.63559  ? 89  LEU A CG  1 
ATOM   300  C CD1 . LEU A 1 66  ? 25.07457  20.34357  8.52631  1.000 73.11722  ? 89  LEU A CD1 1 
ATOM   301  C CD2 . LEU A 1 66  ? 25.01569  20.25635  6.02592  1.000 92.82436  ? 89  LEU A CD2 1 
ATOM   302  N N   . ALA A 1 67  ? 20.78955  22.60074  7.17501  1.000 88.09969  ? 90  ALA A N   1 
ATOM   303  C CA  . ALA A 1 67  ? 20.40027  23.96538  6.83141  1.000 71.85530  ? 90  ALA A CA  1 
ATOM   304  C C   . ALA A 1 67  ? 19.82952  24.69598  8.04137  1.000 78.02762  ? 90  ALA A C   1 
ATOM   305  O O   . ALA A 1 67  ? 20.11458  25.88028  8.25415  1.000 84.37462  ? 90  ALA A O   1 
ATOM   306  C CB  . ALA A 1 67  ? 19.39181  23.95119  5.68319  1.000 65.17495  ? 90  ALA A CB  1 
ATOM   307  N N   . ALA A 1 68  ? 19.01552  24.00407  8.84418  1.000 84.17118  ? 91  ALA A N   1 
ATOM   308  C CA  . ALA A 1 68  ? 18.35490  24.65155  9.97300  1.000 64.47238  ? 91  ALA A CA  1 
ATOM   309  C C   . ALA A 1 68  ? 19.36167  25.03892  11.04758 1.000 82.51662  ? 91  ALA A C   1 
ATOM   310  O O   . ALA A 1 68  ? 19.26134  26.12313  11.63354 1.000 90.99270  ? 91  ALA A O   1 
ATOM   311  C CB  . ALA A 1 68  ? 17.27714  23.73408  10.54866 1.000 64.67631  ? 91  ALA A CB  1 
ATOM   312  N N   . ASN A 1 69  ? 20.34182  24.17432  11.31807 1.000 80.90346  ? 92  ASN A N   1 
ATOM   313  C CA  . ASN A 1 69  ? 21.32599  24.48701  12.34887 1.000 82.33445  ? 92  ASN A CA  1 
ATOM   314  C C   . ASN A 1 69  ? 22.20766  25.64736  11.90797 1.000 87.95082  ? 92  ASN A C   1 
ATOM   315  O O   . ASN A 1 69  ? 22.63467  26.45406  12.74211 1.000 84.00652  ? 92  ASN A O   1 
ATOM   316  C CB  . ASN A 1 69  ? 22.15389  23.25187  12.69774 1.000 91.58287  ? 92  ASN A CB  1 
ATOM   317  C CG  . ASN A 1 69  ? 21.29633  22.09881  13.17835 1.000 100.89936 ? 92  ASN A CG  1 
ATOM   318  O OD1 . ASN A 1 69  ? 20.09626  22.04517  12.90198 1.000 91.50796  ? 92  ASN A OD1 1 
ATOM   319  N ND2 . ASN A 1 69  ? 21.90363  21.17702  13.91619 1.000 113.82519 ? 92  ASN A ND2 1 
ATOM   320  N N   . ILE A 1 70  ? 22.47112  25.75785  10.60530 1.000 80.23138  ? 93  ILE A N   1 
ATOM   321  C CA  . ILE A 1 70  ? 23.29137  26.85234  10.10158 1.000 77.27897  ? 93  ILE A CA  1 
ATOM   322  C C   . ILE A 1 70  ? 22.53334  28.16330  10.25894 1.000 71.50608  ? 93  ILE A C   1 
ATOM   323  O O   . ILE A 1 70  ? 23.05067  29.13356  10.82186 1.000 84.03984  ? 93  ILE A O   1 
ATOM   324  C CB  . ILE A 1 70  ? 23.69784  26.59503  8.63780  1.000 81.97936  ? 93  ILE A CB  1 
ATOM   325  C CG1 . ILE A 1 70  ? 24.68819  25.43143  8.55207  1.000 78.87464  ? 93  ILE A CG1 1 
ATOM   326  C CG2 . ILE A 1 70  ? 24.28802  27.85528  8.00803  1.000 62.30476  ? 93  ILE A CG2 1 
ATOM   327  C CD1 . ILE A 1 70  ? 25.75260  25.43752  9.63227  1.000 104.08143 ? 93  ILE A CD1 1 
ATOM   328  N N   . LEU A 1 71  ? 21.29501  28.21431  9.76086  1.000 69.99976  ? 94  LEU A N   1 
ATOM   329  C CA  . LEU A 1 71  ? 20.52118  29.44541  9.86100  1.000 69.56533  ? 94  LEU A CA  1 
ATOM   330  C C   . LEU A 1 71  ? 20.31450  29.85447  11.30914 1.000 71.12071  ? 94  LEU A C   1 
ATOM   331  O O   . LEU A 1 71  ? 20.28037  31.05246  11.61555 1.000 66.79919  ? 94  LEU A O   1 
ATOM   332  C CB  . LEU A 1 71  ? 19.15417  29.28151  9.19886  1.000 80.10555  ? 94  LEU A CB  1 
ATOM   333  C CG  . LEU A 1 71  ? 18.98468  29.28814  7.68438  1.000 73.11517  ? 94  LEU A CG  1 
ATOM   334  C CD1 . LEU A 1 71  ? 17.51450  29.10878  7.32049  1.000 66.36935  ? 94  LEU A CD1 1 
ATOM   335  C CD2 . LEU A 1 71  ? 19.51123  30.61738  7.15909  1.000 70.52062  ? 94  LEU A CD2 1 
ATOM   336  N N   . GLN A 1 72  ? 20.16707  28.87924  12.21171 1.000 69.13908  ? 95  GLN A N   1 
ATOM   337  C CA  . GLN A 1 72  ? 20.01662  29.20361  13.62519 1.000 65.10300  ? 95  GLN A CA  1 
ATOM   338  C C   . GLN A 1 72  ? 21.28678  29.83389  14.17948 1.000 70.19357  ? 95  GLN A C   1 
ATOM   339  O O   . GLN A 1 72  ? 21.23457  30.87765  14.83972 1.000 71.16595  ? 95  GLN A O   1 
ATOM   340  C CB  . GLN A 1 72  ? 19.63276  27.94998  14.41078 1.000 65.88854  ? 95  GLN A CB  1 
ATOM   341  C CG  . GLN A 1 72  ? 18.17184  27.55072  14.24590 1.000 81.70988  ? 95  GLN A CG  1 
ATOM   342  C CD  . GLN A 1 72  ? 17.87742  26.13909  14.72221 1.000 78.01143  ? 95  GLN A CD  1 
ATOM   343  O OE1 . GLN A 1 72  ? 16.72968  25.79911  15.01129 1.000 75.52163  ? 95  GLN A OE1 1 
ATOM   344  N NE2 . GLN A 1 72  ? 18.91066  25.30665  14.79420 1.000 87.35796  ? 95  GLN A NE2 1 
ATOM   345  N N   . TRP A 1 73  ? 22.43992  29.20578  13.92611 1.000 74.15621  ? 96  TRP A N   1 
ATOM   346  C CA  . TRP A 1 73  ? 23.70981  29.78376  14.35921 1.000 71.47205  ? 96  TRP A CA  1 
ATOM   347  C C   . TRP A 1 73  ? 23.88966  31.19279  13.80847 1.000 70.55449  ? 96  TRP A C   1 
ATOM   348  O O   . TRP A 1 73  ? 24.27311  32.11169  14.54210 1.000 68.20898  ? 96  TRP A O   1 
ATOM   349  C CB  . TRP A 1 73  ? 24.87516  28.87347  13.97018 1.000 59.98108  ? 96  TRP A CB  1 
ATOM   350  C CG  . TRP A 1 73  ? 25.06782  27.78650  14.97372 1.000 72.66852  ? 96  TRP A CG  1 
ATOM   351  C CD1 . TRP A 1 73  ? 24.72263  26.47337  14.84665 1.000 93.25678  ? 96  TRP A CD1 1 
ATOM   352  C CD2 . TRP A 1 73  ? 25.59984  27.93581  16.29510 1.000 72.14709  ? 96  TRP A CD2 1 
ATOM   353  N NE1 . TRP A 1 73  ? 25.03617  25.78865  15.99702 1.000 90.26968  ? 96  TRP A NE1 1 
ATOM   354  C CE2 . TRP A 1 73  ? 25.57386  26.66532  16.90234 1.000 73.56592  ? 96  TRP A CE2 1 
ATOM   355  C CE3 . TRP A 1 73  ? 26.10892  29.02003  17.01866 1.000 77.10814  ? 96  TRP A CE3 1 
ATOM   356  C CZ2 . TRP A 1 73  ? 26.03604  26.44811  18.19835 1.000 76.32665  ? 96  TRP A CZ2 1 
ATOM   357  C CZ3 . TRP A 1 73  ? 26.56865  28.80266  18.30436 1.000 77.51586  ? 96  TRP A CZ3 1 
ATOM   358  C CH2 . TRP A 1 73  ? 26.52890  27.52671  18.88104 1.000 83.89229  ? 96  TRP A CH2 1 
ATOM   359  N N   . ILE A 1 74  ? 23.63010  31.37732  12.51126 1.000 71.30580  ? 97  ILE A N   1 
ATOM   360  C CA  . ILE A 1 74  ? 23.72086  32.70590  11.91050 1.000 64.37648  ? 97  ILE A CA  1 
ATOM   361  C C   . ILE A 1 74  ? 22.86883  33.67878  12.71061 1.000 63.33263  ? 97  ILE A C   1 
ATOM   362  O O   . ILE A 1 74  ? 23.29761  34.79309  13.03650 1.000 60.84803  ? 97  ILE A O   1 
ATOM   363  C CB  . ILE A 1 74  ? 23.30883  32.65705  10.42350 1.000 53.44049  ? 97  ILE A CB  1 
ATOM   364  C CG1 . ILE A 1 74  ? 24.42072  32.02361  9.58658  1.000 43.37265  ? 97  ILE A CG1 1 
ATOM   365  C CG2 . ILE A 1 74  ? 22.97582  34.04708  9.90760  1.000 52.49652  ? 97  ILE A CG2 1 
ATOM   366  C CD1 . ILE A 1 74  ? 24.12829  31.99039  8.10277  1.000 56.42191  ? 97  ILE A CD1 1 
ATOM   367  N N   . THR A 1 75  ? 21.65280  33.25258  13.05848 1.000 63.78426  ? 98  THR A N   1 
ATOM   368  C CA  . THR A 1 75  ? 20.69059  34.12227  13.72021 1.000 65.51586  ? 98  THR A CA  1 
ATOM   369  C C   . THR A 1 75  ? 21.09111  34.37026  15.16567 1.000 64.83192  ? 98  THR A C   1 
ATOM   370  O O   . THR A 1 75  ? 20.95650  35.49108  15.66821 1.000 59.72425  ? 98  THR A O   1 
ATOM   371  C CB  . THR A 1 75  ? 19.29423  33.50492  13.66446 1.000 74.70791  ? 98  THR A CB  1 
ATOM   372  O OG1 . THR A 1 75  ? 18.90964  33.33530  12.30100 1.000 85.18174  ? 98  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 75  ? 18.27289  34.40655  14.34916 1.000 56.80360  ? 98  THR A CG2 1 
ATOM   374  N N   . PHE A 1 76  ? 21.60494  33.33881  15.84798 1.000 66.90097  ? 99  PHE A N   1 
ATOM   375  C CA  . PHE A 1 76  ? 22.03170  33.52731  17.22781 1.000 60.59063  ? 99  PHE A CA  1 
ATOM   376  C C   . PHE A 1 76  ? 23.16365  34.53453  17.27847 1.000 70.53665  ? 99  PHE A C   1 
ATOM   377  O O   . PHE A 1 76  ? 23.15068  35.47992  18.07668 1.000 61.33369  ? 99  PHE A O   1 
ATOM   378  C CB  . PHE A 1 76  ? 22.57944  32.20736  17.77047 1.000 81.54658  ? 99  PHE A CB  1 
ATOM   379  C CG  . PHE A 1 76  ? 23.24545  32.34248  19.11117 1.000 79.58358  ? 99  PHE A CG  1 
ATOM   380  C CD1 . PHE A 1 76  ? 22.43481  32.59283  20.21302 1.000 76.80431  ? 99  PHE A CD1 1 
ATOM   381  C CD2 . PHE A 1 76  ? 24.64512  32.34040  19.27196 1.000 77.74166  ? 99  PHE A CD2 1 
ATOM   382  C CE1 . PHE A 1 76  ? 22.95971  32.74199  21.46041 1.000 86.19160  ? 99  PHE A CE1 1 
ATOM   383  C CE2 . PHE A 1 76  ? 25.20348  32.51549  20.54601 1.000 86.63363  ? 99  PHE A CE2 1 
ATOM   384  C CZ  . PHE A 1 76  ? 24.34074  32.72090  21.64254 1.000 80.15649  ? 99  PHE A CZ  1 
ATOM   385  N N   . ALA A 1 77  ? 24.14833  34.33622  16.39951 1.000 78.66178  ? 100 ALA A N   1 
ATOM   386  C CA  . ALA A 1 77  ? 25.32641  35.18899  16.32130 1.000 67.11738  ? 100 ALA A CA  1 
ATOM   387  C C   . ALA A 1 77  ? 24.96475  36.60804  15.90826 1.000 65.42463  ? 100 ALA A C   1 
ATOM   388  O O   . ALA A 1 77  ? 25.38029  37.58719  16.53967 1.000 63.61644  ? 100 ALA A O   1 
ATOM   389  C CB  . ALA A 1 77  ? 26.32361  34.57734  15.33751 1.000 42.75317  ? 100 ALA A CB  1 
ATOM   390  N N   . LEU A 1 78  ? 24.17314  36.73027  14.83907 1.000 68.57543  ? 101 LEU A N   1 
ATOM   391  C CA  . LEU A 1 78  ? 23.83916  38.04613  14.30332 1.000 62.36305  ? 101 LEU A CA  1 
ATOM   392  C C   . LEU A 1 78  ? 22.98657  38.81647  15.30422 1.000 55.75814  ? 101 LEU A C   1 
ATOM   393  O O   . LEU A 1 78  ? 23.13247  40.03618  15.44666 1.000 63.26064  ? 101 LEU A O   1 
ATOM   394  C CB  . LEU A 1 78  ? 23.15629  37.88869  12.93829 1.000 58.48222  ? 101 LEU A CB  1 
ATOM   395  C CG  . LEU A 1 78  ? 22.71114  39.02412  12.00327 1.000 61.21010  ? 101 LEU A CG  1 
ATOM   396  C CD1 . LEU A 1 78  ? 21.66049  39.95492  12.57573 1.000 53.09959  ? 101 LEU A CD1 1 
ATOM   397  C CD2 . LEU A 1 78  ? 23.94241  39.80316  11.51445 1.000 58.17711  ? 101 LEU A CD2 1 
ATOM   398  N N   . SER A 1 79  ? 22.09973  38.11584  16.01624 1.000 59.86926  ? 102 SER A N   1 
ATOM   399  C CA  . SER A 1 79  ? 21.26860  38.77628  17.01533 1.000 59.05595  ? 102 SER A CA  1 
ATOM   400  C C   . SER A 1 79  ? 22.13712  39.24857  18.17231 1.000 62.95892  ? 102 SER A C   1 
ATOM   401  O O   . SER A 1 79  ? 21.89728  40.31628  18.74722 1.000 66.14124  ? 102 SER A O   1 
ATOM   402  C CB  . SER A 1 79  ? 20.16651  37.83930  17.50387 1.000 58.73199  ? 102 SER A CB  1 
ATOM   403  O OG  . SER A 1 79  ? 20.49606  37.27921  18.76238 1.000 74.73710  ? 102 SER A OG  1 
ATOM   404  N N   . ALA A 1 80  ? 23.15987  38.46175  18.51617 1.000 76.00702  ? 103 ALA A N   1 
ATOM   405  C CA  . ALA A 1 80  ? 24.08187  38.84733  19.57758 1.000 68.21450  ? 103 ALA A CA  1 
ATOM   406  C C   . ALA A 1 80  ? 24.92524  40.02708  19.11861 1.000 74.76911  ? 103 ALA A C   1 
ATOM   407  O O   . ALA A 1 80  ? 25.21494  40.93776  19.90159 1.000 73.19390  ? 103 ALA A O   1 
ATOM   408  C CB  . ALA A 1 80  ? 24.96233  37.66401  19.97803 1.000 72.85008  ? 103 ALA A CB  1 
ATOM   409  N N   . LEU A 1 81  ? 25.32768  40.02005  17.84586 1.000 82.19873  ? 104 LEU A N   1 
ATOM   410  C CA  . LEU A 1 81  ? 26.05566  41.15062  17.27653 1.000 67.05344  ? 104 LEU A CA  1 
ATOM   411  C C   . LEU A 1 81  ? 25.19363  42.40726  17.32589 1.000 76.43577  ? 104 LEU A C   1 
ATOM   412  O O   . LEU A 1 81  ? 25.66168  43.47372  17.74134 1.000 79.47836  ? 104 LEU A O   1 
ATOM   413  C CB  . LEU A 1 81  ? 26.48609  40.85092  15.84178 1.000 59.52655  ? 104 LEU A CB  1 
ATOM   414  C CG  . LEU A 1 81  ? 27.53115  39.75559  15.60752 1.000 76.76187  ? 104 LEU A CG  1 
ATOM   415  C CD1 . LEU A 1 81  ? 28.12709  39.88351  14.21456 1.000 68.80802  ? 104 LEU A CD1 1 
ATOM   416  C CD2 . LEU A 1 81  ? 28.62523  39.81215  16.66279 1.000 81.51041  ? 104 LEU A CD2 1 
ATOM   417  N N   . CYS A 1 82  ? 23.92554  42.29735  16.90202 1.000 83.13377  ? 105 CYS A N   1 
ATOM   418  C CA  . CYS A 1 82  ? 23.01567  43.43893  16.95866 1.000 69.51739  ? 105 CYS A CA  1 
ATOM   419  C C   . CYS A 1 82  ? 22.91011  43.99357  18.37041 1.000 70.25826  ? 105 CYS A C   1 
ATOM   420  O O   . CYS A 1 82  ? 22.88460  45.21457  18.55382 1.000 71.12269  ? 105 CYS A O   1 
ATOM   421  C CB  . CYS A 1 82  ? 21.62919  43.04591  16.43919 1.000 74.92276  ? 105 CYS A CB  1 
ATOM   422  S SG  . CYS A 1 82  ? 21.55949  42.66079  14.68466 1.000 82.80153  ? 105 CYS A SG  1 
ATOM   423  N N   . LEU A 1 83  ? 22.82684  43.12426  19.38187 1.000 63.11429  ? 106 LEU A N   1 
ATOM   424  C CA  . LEU A 1 83  ? 22.67507  43.62358  20.74663 1.000 55.40302  ? 106 LEU A CA  1 
ATOM   425  C C   . LEU A 1 83  ? 23.90914  44.44176  21.10764 1.000 79.71044  ? 106 LEU A C   1 
ATOM   426  O O   . LEU A 1 83  ? 23.80760  45.61323  21.49935 1.000 98.72666  ? 106 LEU A O   1 
ATOM   427  C CB  . LEU A 1 83  ? 22.47999  42.45321  21.71313 1.000 61.19517  ? 106 LEU A CB  1 
ATOM   428  C CG  . LEU A 1 83  ? 21.76443  42.63192  23.05922 1.000 76.43135  ? 106 LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 83  ? 21.97032  41.39399  23.90849 1.000 52.44450  ? 106 LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 83  ? 22.25542  43.85522  23.81766 1.000 75.38752  ? 106 LEU A CD2 1 
ATOM   431  N N   . MET A 1 84  ? 25.08983  43.81765  21.01143 1.000 87.33262  ? 107 MET A N   1 
ATOM   432  C CA  . MET A 1 84  ? 26.34171  44.52313  21.27370 1.000 84.80461  ? 107 MET A CA  1 
ATOM   433  C C   . MET A 1 84  ? 26.42831  45.76952  20.40806 1.000 91.96618  ? 107 MET A C   1 
ATOM   434  O O   . MET A 1 84  ? 26.84677  46.83092  20.87750 1.000 99.62435  ? 107 MET A O   1 
ATOM   435  C CB  . MET A 1 84  ? 27.55879  43.61237  21.08024 1.000 83.19171  ? 107 MET A CB  1 
ATOM   436  C CG  . MET A 1 84  ? 27.85733  42.70632  22.27346 1.000 86.10249  ? 107 MET A CG  1 
ATOM   437  S SD  . MET A 1 84  ? 27.00170  41.12853  22.35996 1.000 121.18897 ? 107 MET A SD  1 
ATOM   438  C CE  . MET A 1 84  ? 27.99634  40.27261  23.58213 1.000 73.46078  ? 107 MET A CE  1 
ATOM   439  N N   . PHE A 1 85  ? 26.03870  45.64894  19.13168 1.000 102.71919 ? 108 PHE A N   1 
ATOM   440  C CA  . PHE A 1 85  ? 26.15424  46.76528  18.19754 1.000 103.87673 ? 108 PHE A CA  1 
ATOM   441  C C   . PHE A 1 85  ? 25.29971  47.94044  18.65035 1.000 101.96255 ? 108 PHE A C   1 
ATOM   442  O O   . PHE A 1 85  ? 25.74281  49.09446  18.59953 1.000 109.48660 ? 108 PHE A O   1 
ATOM   443  C CB  . PHE A 1 85  ? 25.68790  46.35032  16.79963 1.000 101.35275 ? 108 PHE A CB  1 
ATOM   444  C CG  . PHE A 1 85  ? 25.58367  47.50152  15.84339 1.000 105.73495 ? 108 PHE A CG  1 
ATOM   445  C CD1 . PHE A 1 85  ? 26.70469  48.27257  15.59151 1.000 117.34219 ? 108 PHE A CD1 1 
ATOM   446  C CD2 . PHE A 1 85  ? 24.36387  47.87200  15.26650 1.000 92.30631  ? 108 PHE A CD2 1 
ATOM   447  C CE1 . PHE A 1 85  ? 26.65384  49.34170  14.72929 1.000 114.60100 ? 108 PHE A CE1 1 
ATOM   448  C CE2 . PHE A 1 85  ? 24.29597  48.96006  14.40523 1.000 91.78272  ? 108 PHE A CE2 1 
ATOM   449  C CZ  . PHE A 1 85  ? 25.44571  49.69612  14.13797 1.000 104.81640 ? 108 PHE A CZ  1 
ATOM   450  N N   . TYR A 1 86  ? 24.06261  47.66829  19.08269 1.000 96.34700  ? 109 TYR A N   1 
ATOM   451  C CA  . TYR A 1 86  ? 23.19396  48.72196  19.59240 1.000 93.09090  ? 109 TYR A CA  1 
ATOM   452  C C   . TYR A 1 86  ? 23.72148  49.26091  20.91095 1.000 103.44648 ? 109 TYR A C   1 
ATOM   453  O O   . TYR A 1 86  ? 23.34223  50.36194  21.32674 1.000 112.22010 ? 109 TYR A O   1 
ATOM   454  C CB  . TYR A 1 86  ? 21.77798  48.19105  19.81945 1.000 71.49795  ? 109 TYR A CB  1 
ATOM   455  C CG  . TYR A 1 86  ? 21.06154  47.64113  18.60262 1.000 84.07471  ? 109 TYR A CG  1 
ATOM   456  C CD1 . TYR A 1 86  ? 21.33253  48.11099  17.32276 1.000 84.48875  ? 109 TYR A CD1 1 
ATOM   457  C CD2 . TYR A 1 86  ? 20.11717  46.62984  18.74158 1.000 75.37215  ? 109 TYR A CD2 1 
ATOM   458  C CE1 . TYR A 1 86  ? 20.67143  47.59136  16.21806 1.000 69.92000  ? 109 TYR A CE1 1 
ATOM   459  C CE2 . TYR A 1 86  ? 19.45850  46.10593  17.64969 1.000 63.87089  ? 109 TYR A CE2 1 
ATOM   460  C CZ  . TYR A 1 86  ? 19.73579  46.58892  16.39177 1.000 67.50571  ? 109 TYR A CZ  1 
ATOM   461  O OH  . TYR A 1 86  ? 19.06615  46.06160  15.31242 1.000 76.02421  ? 109 TYR A OH  1 
ATOM   462  N N   . GLY A 1 87  ? 24.57486  48.48074  21.57291 1.000 105.10444 ? 110 GLY A N   1 
ATOM   463  C CA  . GLY A 1 87  ? 25.17282  48.70532  22.87413 1.000 103.22657 ? 110 GLY A CA  1 
ATOM   464  C C   . GLY A 1 87  ? 26.24332  49.77185  22.87680 1.000 125.19689 ? 110 GLY A C   1 
ATOM   465  O O   . GLY A 1 87  ? 26.63460  50.23353  23.95408 1.000 127.60803 ? 110 GLY A O   1 
ATOM   466  N N   . TYR A 1 88  ? 26.71793  50.16733  21.69838 1.000 135.34000 ? 111 TYR A N   1 
ATOM   467  C CA  . TYR A 1 88  ? 27.77595  51.15815  21.55175 1.000 128.36022 ? 111 TYR A CA  1 
ATOM   468  C C   . TYR A 1 88  ? 27.31190  52.50180  22.09166 1.000 133.43064 ? 111 TYR A C   1 
ATOM   469  O O   . TYR A 1 88  ? 26.11350  52.75842  22.20285 1.000 134.37694 ? 111 TYR A O   1 
ATOM   470  C CB  . TYR A 1 88  ? 28.13236  51.34082  20.06752 1.000 133.67789 ? 111 TYR A CB  1 
ATOM   471  C CG  . TYR A 1 88  ? 28.82307  50.18304  19.37485 1.000 139.67147 ? 111 TYR A CG  1 
ATOM   472  C CD1 . TYR A 1 88  ? 28.92014  48.93530  19.97208 1.000 135.12268 ? 111 TYR A CD1 1 
ATOM   473  C CD2 . TYR A 1 88  ? 29.33545  50.33448  18.08653 1.000 136.17646 ? 111 TYR A CD2 1 
ATOM   474  C CE1 . TYR A 1 88  ? 29.52434  47.87359  19.32329 1.000 132.65942 ? 111 TYR A CE1 1 
ATOM   475  C CE2 . TYR A 1 88  ? 29.94634  49.27836  17.42971 1.000 133.58139 ? 111 TYR A CE2 1 
ATOM   476  C CZ  . TYR A 1 88  ? 30.03683  48.05051  18.05419 1.000 129.86825 ? 111 TYR A CZ  1 
ATOM   477  O OH  . TYR A 1 88  ? 30.64142  46.99153  17.41657 1.000 132.13510 ? 111 TYR A OH  1 
ATOM   478  N N   . CYS A 1 95  ? 14.37135  54.76012  25.65033 1.000 50.73038  ? 118 CYS A N   1 
ATOM   479  C CA  . CYS A 1 95  ? 14.65789  54.97825  24.23529 1.000 85.80108  ? 118 CYS A CA  1 
ATOM   480  C C   . CYS A 1 95  ? 15.64762  53.93334  23.72345 1.000 79.39089  ? 118 CYS A C   1 
ATOM   481  O O   . CYS A 1 95  ? 16.65044  53.65392  24.37921 1.000 72.19512  ? 118 CYS A O   1 
ATOM   482  C CB  . CYS A 1 95  ? 15.20745  56.38990  24.00863 1.000 62.86522  ? 118 CYS A CB  1 
ATOM   483  N N   . GLY A 1 96  ? 15.37057  53.35867  22.55148 1.000 74.83794  ? 119 GLY A N   1 
ATOM   484  C CA  . GLY A 1 96  ? 16.16891  52.25791  22.04907 1.000 62.49965  ? 119 GLY A CA  1 
ATOM   485  C C   . GLY A 1 96  ? 15.84104  50.90032  22.63376 1.000 67.94507  ? 119 GLY A C   1 
ATOM   486  O O   . GLY A 1 96  ? 16.48365  49.91358  22.25895 1.000 58.25637  ? 119 GLY A O   1 
ATOM   487  N N   . TRP A 1 97  ? 14.85782  50.81776  23.53284 1.000 67.93523  ? 120 TRP A N   1 
ATOM   488  C CA  . TRP A 1 97  ? 14.57116  49.57767  24.24944 1.000 49.74861  ? 120 TRP A CA  1 
ATOM   489  C C   . TRP A 1 97  ? 13.95579  48.51563  23.34495 1.000 49.65474  ? 120 TRP A C   1 
ATOM   490  O O   . TRP A 1 97  ? 14.09204  47.31783  23.62165 1.000 54.83615  ? 120 TRP A O   1 
ATOM   491  C CB  . TRP A 1 97  ? 13.66024  49.86920  25.44493 1.000 57.26451  ? 120 TRP A CB  1 
ATOM   492  C CG  . TRP A 1 97  ? 12.24306  50.22091  25.08146 1.000 57.53393  ? 120 TRP A CG  1 
ATOM   493  C CD1 . TRP A 1 97  ? 11.72575  51.47564  24.91928 1.000 52.75517  ? 120 TRP A CD1 1 
ATOM   494  C CD2 . TRP A 1 97  ? 11.15399  49.30976  24.87840 1.000 46.12973  ? 120 TRP A CD2 1 
ATOM   495  N NE1 . TRP A 1 97  ? 10.38860  51.40057  24.60675 1.000 48.96927  ? 120 TRP A NE1 1 
ATOM   496  C CE2 . TRP A 1 97  ? 10.01224  50.08321  24.57710 1.000 52.33890  ? 120 TRP A CE2 1 
ATOM   497  C CE3 . TRP A 1 97  ? 11.03598  47.91646  24.91126 1.000 36.30647  ? 120 TRP A CE3 1 
ATOM   498  C CZ2 . TRP A 1 97  ? 8.76794   49.50933  24.31088 1.000 38.84658  ? 120 TRP A CZ2 1 
ATOM   499  C CZ3 . TRP A 1 97  ? 9.80083   47.34772  24.64452 1.000 48.25028  ? 120 TRP A CZ3 1 
ATOM   500  C CH2 . TRP A 1 97  ? 8.68232   48.14464  24.34877 1.000 36.83279  ? 120 TRP A CH2 1 
ATOM   501  N N   . GLU A 1 98  ? 13.27512  48.92579  22.27210 1.000 55.97966  ? 121 GLU A N   1 
ATOM   502  C CA  . GLU A 1 98  ? 12.59722  47.96128  21.40863 1.000 40.29112  ? 121 GLU A CA  1 
ATOM   503  C C   . GLU A 1 98  ? 13.58336  47.09182  20.63331 1.000 42.00021  ? 121 GLU A C   1 
ATOM   504  O O   . GLU A 1 98  ? 13.38622  45.87549  20.53065 1.000 38.26515  ? 121 GLU A O   1 
ATOM   505  C CB  . GLU A 1 98  ? 11.65469  48.68336  20.44175 1.000 31.15058  ? 121 GLU A CB  1 
ATOM   506  C CG  . GLU A 1 98  ? 10.74013  49.70566  21.08776 1.000 27.27666  ? 121 GLU A CG  1 
ATOM   507  C CD  . GLU A 1 98  ? 11.12387  51.12448  20.73046 1.000 37.10903  ? 121 GLU A CD  1 
ATOM   508  O OE1 . GLU A 1 98  ? 12.33972  51.41082  20.69993 1.000 53.21240  ? 121 GLU A OE1 1 
ATOM   509  O OE2 . GLU A 1 98  ? 10.21632  51.95344  20.48571 1.000 37.91350  ? 121 GLU A OE2 1 
ATOM   510  N N   . GLU A 1 99  ? 14.63466  47.68449  20.05945 1.000 56.91617  ? 122 GLU A N   1 
ATOM   511  C CA  . GLU A 1 99  ? 15.62396  46.86532  19.36186 1.000 43.47165  ? 122 GLU A CA  1 
ATOM   512  C C   . GLU A 1 99  ? 16.27608  45.84742  20.29797 1.000 46.48748  ? 122 GLU A C   1 
ATOM   513  O O   . GLU A 1 99  ? 16.52467  44.70293  19.90150 1.000 46.45543  ? 122 GLU A O   1 
ATOM   514  C CB  . GLU A 1 99  ? 16.67238  47.75542  18.69225 1.000 59.54640  ? 122 GLU A CB  1 
ATOM   515  C CG  . GLU A 1 99  ? 16.09508  48.84266  17.78348 1.000 57.13399  ? 122 GLU A CG  1 
ATOM   516  C CD  . GLU A 1 99  ? 15.85948  50.15322  18.50769 1.000 63.54839  ? 122 GLU A CD  1 
ATOM   517  O OE1 . GLU A 1 99  ? 16.74469  51.03566  18.45142 1.000 62.17247  ? 122 GLU A OE1 1 
ATOM   518  O OE2 . GLU A 1 99  ? 14.78713  50.29885  19.13353 1.000 65.79279  ? 122 GLU A OE2 1 
ATOM   519  N N   . ILE A 1 100 ? 16.55494  46.23875  21.54346 1.000 52.80898  ? 123 ILE A N   1 
ATOM   520  C CA  . ILE A 1 100 ? 17.25910  45.34951  22.46946 1.000 51.09388  ? 123 ILE A CA  1 
ATOM   521  C C   . ILE A 1 100 ? 16.34514  44.22722  22.94148 1.000 49.79494  ? 123 ILE A C   1 
ATOM   522  O O   . ILE A 1 100 ? 16.75187  43.05851  22.99208 1.000 53.42727  ? 123 ILE A O   1 
ATOM   523  C CB  . ILE A 1 100 ? 17.89237  46.12307  23.64821 1.000 48.05799  ? 123 ILE A CB  1 
ATOM   524  C CG1 . ILE A 1 100 ? 19.10956  46.95265  23.18167 1.000 32.09391  ? 123 ILE A CG1 1 
ATOM   525  C CG2 . ILE A 1 100 ? 18.18613  45.19190  24.85664 1.000 59.92190  ? 123 ILE A CG2 1 
ATOM   526  C CD1 . ILE A 1 100 ? 18.83132  48.10182  22.18660 1.000 59.72206  ? 123 ILE A CD1 1 
ATOM   527  N N   . TYR A 1 101 ? 15.09449  44.55214  23.27796 1.000 46.65531  ? 124 TYR A N   1 
ATOM   528  C CA  . TYR A 1 101 ? 14.19723  43.52378  23.79404 1.000 42.74114  ? 124 TYR A CA  1 
ATOM   529  C C   . TYR A 1 101 ? 14.03324  42.39720  22.77880 1.000 47.26207  ? 124 TYR A C   1 
ATOM   530  O O   . TYR A 1 101 ? 14.13298  41.21571  23.12973 1.000 47.41361  ? 124 TYR A O   1 
ATOM   531  C CB  . TYR A 1 101 ? 12.84473  44.13734  24.16331 1.000 37.68735  ? 124 TYR A CB  1 
ATOM   532  C CG  . TYR A 1 101 ? 11.90573  43.16543  24.84219 1.000 35.35032  ? 124 TYR A CG  1 
ATOM   533  C CD1 . TYR A 1 101 ? 12.04398  42.87626  26.19449 1.000 44.41385  ? 124 TYR A CD1 1 
ATOM   534  C CD2 . TYR A 1 101 ? 10.87844  42.54963  24.14362 1.000 38.24134  ? 124 TYR A CD2 1 
ATOM   535  C CE1 . TYR A 1 101 ? 11.20644  41.98243  26.82511 1.000 34.82709  ? 124 TYR A CE1 1 
ATOM   536  C CE2 . TYR A 1 101 ? 10.02291  41.66344  24.77115 1.000 35.38567  ? 124 TYR A CE2 1 
ATOM   537  C CZ  . TYR A 1 101 ? 10.19605  41.38296  26.11192 1.000 24.61713  ? 124 TYR A CZ  1 
ATOM   538  O OH  . TYR A 1 101 ? 9.34260   40.51212  26.74807 1.000 31.72416  ? 124 TYR A OH  1 
ATOM   539  N N   . VAL A 1 102 ? 13.79455  42.74376  21.50888 1.000 47.84237  ? 125 VAL A N   1 
ATOM   540  C CA  . VAL A 1 102 ? 13.59394  41.72205  20.48086 1.000 32.83184  ? 125 VAL A CA  1 
ATOM   541  C C   . VAL A 1 102 ? 14.87088  40.91225  20.28495 1.000 41.62334  ? 125 VAL A C   1 
ATOM   542  O O   . VAL A 1 102 ? 14.83818  39.67995  20.17040 1.000 52.25695  ? 125 VAL A O   1 
ATOM   543  C CB  . VAL A 1 102 ? 13.13630  42.36818  19.16125 1.000 28.39328  ? 125 VAL A CB  1 
ATOM   544  C CG1 . VAL A 1 102 ? 12.93449  41.29573  18.08949 1.000 23.38923  ? 125 VAL A CG1 1 
ATOM   545  C CG2 . VAL A 1 102 ? 11.87673  43.19349  19.37655 1.000 34.78323  ? 125 VAL A CG2 1 
ATOM   546  N N   . ALA A 1 103 ? 16.01408  41.59907  20.22288 1.000 51.13609  ? 126 ALA A N   1 
ATOM   547  C CA  . ALA A 1 103 ? 17.28997  40.93017  19.98812 1.000 44.36266  ? 126 ALA A CA  1 
ATOM   548  C C   . ALA A 1 103 ? 17.65904  40.02965  21.15986 1.000 45.68724  ? 126 ALA A C   1 
ATOM   549  O O   . ALA A 1 103 ? 18.21016  38.93960  20.96337 1.000 55.00559  ? 126 ALA A O   1 
ATOM   550  C CB  . ALA A 1 103 ? 18.39001  41.95858  19.72365 1.000 44.93412  ? 126 ALA A CB  1 
ATOM   551  N N   . THR A 1 104 ? 17.35411  40.46655  22.38482 1.000 44.61532  ? 127 THR A N   1 
ATOM   552  C CA  . THR A 1 104 ? 17.53343  39.60568  23.55013 1.000 43.20413  ? 127 THR A CA  1 
ATOM   553  C C   . THR A 1 104 ? 16.69452  38.34179  23.43407 1.000 40.65371  ? 127 THR A C   1 
ATOM   554  O O   . THR A 1 104 ? 17.19995  37.23200  23.63986 1.000 50.69617  ? 127 THR A O   1 
ATOM   555  C CB  . THR A 1 104 ? 17.17215  40.36259  24.82876 1.000 47.72264  ? 127 THR A CB  1 
ATOM   556  O OG1 . THR A 1 104 ? 17.89603  41.59814  24.88104 1.000 57.57848  ? 127 THR A OG1 1 
ATOM   557  C CG2 . THR A 1 104 ? 17.49315  39.52594  26.05365 1.000 38.21361  ? 127 THR A CG2 1 
ATOM   558  N N   . ILE A 1 105 ? 15.40447  38.48435  23.12427 1.000 32.91824  ? 128 ILE A N   1 
ATOM   559  C CA  . ILE A 1 105 ? 14.54822  37.30400  23.08389 1.000 34.70696  ? 128 ILE A CA  1 
ATOM   560  C C   . ILE A 1 105 ? 15.03366  36.34043  22.00527 1.000 47.56392  ? 128 ILE A C   1 
ATOM   561  O O   . ILE A 1 105 ? 15.09077  35.12344  22.22644 1.000 58.58315  ? 128 ILE A O   1 
ATOM   562  C CB  . ILE A 1 105 ? 13.07937  37.71629  22.86615 1.000 38.43626  ? 128 ILE A CB  1 
ATOM   563  C CG1 . ILE A 1 105 ? 12.59055  38.58420  24.02806 1.000 45.31063  ? 128 ILE A CG1 1 
ATOM   564  C CG2 . ILE A 1 105 ? 12.19438  36.49043  22.72078 1.000 31.95758  ? 128 ILE A CG2 1 
ATOM   565  C CD1 . ILE A 1 105 ? 12.55317  37.86041  25.35337 1.000 53.64752  ? 128 ILE A CD1 1 
ATOM   566  N N   . GLU A 1 106 ? 15.40804  36.86912  20.82781 1.000 39.99013  ? 129 GLU A N   1 
ATOM   567  C CA  . GLU A 1 106 ? 15.88492  36.00802  19.74501 1.000 50.58977  ? 129 GLU A CA  1 
ATOM   568  C C   . GLU A 1 106 ? 17.07335  35.17330  20.20498 1.000 59.71415  ? 129 GLU A C   1 
ATOM   569  O O   . GLU A 1 106 ? 17.18901  33.99140  19.85537 1.000 48.39424  ? 129 GLU A O   1 
ATOM   570  C CB  . GLU A 1 106 ? 16.26073  36.83868  18.52168 1.000 57.97993  ? 129 GLU A CB  1 
ATOM   571  C CG  . GLU A 1 106 ? 15.17478  36.93950  17.47780 1.000 67.31749  ? 129 GLU A CG  1 
ATOM   572  C CD  . GLU A 1 106 ? 15.74251  37.32955  16.13973 1.000 83.07492  ? 129 GLU A CD  1 
ATOM   573  O OE1 . GLU A 1 106 ? 16.34096  38.42072  16.05637 1.000 70.71549  ? 129 GLU A OE1 1 
ATOM   574  O OE2 . GLU A 1 106 ? 15.60382  36.54104  15.18042 1.000 86.07029  ? 129 GLU A OE2 1 
ATOM   575  N N   . MET A 1 107 ? 17.95165  35.77211  21.01682 1.000 51.32890  ? 130 MET A N   1 
ATOM   576  C CA  . MET A 1 107 ? 19.14617  35.08071  21.49408 1.000 51.34928  ? 130 MET A CA  1 
ATOM   577  C C   . MET A 1 107 ? 18.73792  33.97390  22.44308 1.000 52.38869  ? 130 MET A C   1 
ATOM   578  O O   . MET A 1 107 ? 19.15206  32.81796  22.29275 1.000 58.74687  ? 130 MET A O   1 
ATOM   579  C CB  . MET A 1 107 ? 20.11190  36.04089  22.18054 1.000 45.11013  ? 130 MET A CB  1 
ATOM   580  C CG  . MET A 1 107 ? 21.52943  35.50142  22.21782 1.000 67.54575  ? 130 MET A CG  1 
ATOM   581  S SD  . MET A 1 107 ? 22.64763  36.48686  23.21606 1.000 72.71952  ? 130 MET A SD  1 
ATOM   582  C CE  . MET A 1 107 ? 21.78742  38.05218  23.18936 1.000 51.12123  ? 130 MET A CE  1 
ATOM   583  N N   . ILE A 1 108 ? 17.96158  34.34382  23.46491 1.000 44.54651  ? 131 ILE A N   1 
ATOM   584  C CA  . ILE A 1 108 ? 17.39094  33.38267  24.40259 1.000 47.83747  ? 131 ILE A CA  1 
ATOM   585  C C   . ILE A 1 108 ? 16.71531  32.25645  23.63554 1.000 47.56045  ? 131 ILE A C   1 
ATOM   586  O O   . ILE A 1 108 ? 16.75760  31.09359  24.05138 1.000 55.32619  ? 131 ILE A O   1 
ATOM   587  C CB  . ILE A 1 108 ? 16.42460  34.08421  25.37599 1.000 51.62077  ? 131 ILE A CB  1 
ATOM   588  C CG1 . ILE A 1 108 ? 17.15929  35.16805  26.16997 1.000 44.48151  ? 131 ILE A CG1 1 
ATOM   589  C CG2 . ILE A 1 108 ? 15.76132  33.07635  26.30617 1.000 43.51824  ? 131 ILE A CG2 1 
ATOM   590  C CD1 . ILE A 1 108 ? 16.23945  36.23229  26.72008 1.000 56.34693  ? 131 ILE A CD1 1 
ATOM   591  N N   . LYS A 1 109 ? 16.04977  32.58722  22.52440 1.000 43.74553  ? 132 LYS A N   1 
ATOM   592  C CA  . LYS A 1 109 ? 15.31002  31.58053  21.76905 1.000 29.68880  ? 132 LYS A CA  1 
ATOM   593  C C   . LYS A 1 109 ? 16.26120  30.48192  21.31049 1.000 35.42818  ? 132 LYS A C   1 
ATOM   594  O O   . LYS A 1 109 ? 15.93012  29.29202  21.38689 1.000 42.15673  ? 132 LYS A O   1 
ATOM   595  C CB  . LYS A 1 109 ? 14.60073  32.23065  20.58262 1.000 48.47728  ? 132 LYS A CB  1 
ATOM   596  C CG  . LYS A 1 109 ? 13.95861  31.25736  19.60777 1.000 41.17840  ? 132 LYS A CG  1 
ATOM   597  C CD  . LYS A 1 109 ? 14.05979  31.78013  18.18291 1.000 42.35821  ? 132 LYS A CD  1 
ATOM   598  C CE  . LYS A 1 109 ? 13.23128  30.94317  17.23166 1.000 51.12900  ? 132 LYS A CE  1 
ATOM   599  N NZ  . LYS A 1 109 ? 11.84166  30.79200  17.73715 1.000 46.57116  ? 132 LYS A NZ  1 
ATOM   600  N N   . PHE A 1 110 ? 17.44140  30.86603  20.81024 1.000 51.45659  ? 133 PHE A N   1 
ATOM   601  C CA  . PHE A 1 110 ? 18.37079  29.90063  20.22997 1.000 56.65312  ? 133 PHE A CA  1 
ATOM   602  C C   . PHE A 1 110 ? 18.88289  28.94142  21.29103 1.000 58.67282  ? 133 PHE A C   1 
ATOM   603  O O   . PHE A 1 110 ? 19.01343  27.74056  21.02954 1.000 69.51239  ? 133 PHE A O   1 
ATOM   604  C CB  . PHE A 1 110 ? 19.54729  30.61007  19.54721 1.000 67.28238  ? 133 PHE A CB  1 
ATOM   605  C CG  . PHE A 1 110 ? 20.66994  29.67312  19.10667 1.000 86.16203  ? 133 PHE A CG  1 
ATOM   606  C CD1 . PHE A 1 110 ? 20.89208  29.41694  17.76101 1.000 76.64071  ? 133 PHE A CD1 1 
ATOM   607  C CD2 . PHE A 1 110 ? 21.56600  29.13519  20.03662 1.000 85.61471  ? 133 PHE A CD2 1 
ATOM   608  C CE1 . PHE A 1 110 ? 21.93442  28.58799  17.35906 1.000 72.71747  ? 133 PHE A CE1 1 
ATOM   609  C CE2 . PHE A 1 110 ? 22.59898  28.30351  19.64328 1.000 79.23390  ? 133 PHE A CE2 1 
ATOM   610  C CZ  . PHE A 1 110 ? 22.78752  28.03340  18.30350 1.000 86.74741  ? 133 PHE A CZ  1 
ATOM   611  N N   . ILE A 1 111 ? 19.15876  29.44367  22.49862 1.000 55.13469  ? 134 ILE A N   1 
ATOM   612  C CA  . ILE A 1 111 ? 19.68065  28.57032  23.54509 1.000 55.84065  ? 134 ILE A CA  1 
ATOM   613  C C   . ILE A 1 111 ? 18.64176  27.51108  23.86708 1.000 52.89120  ? 134 ILE A C   1 
ATOM   614  O O   . ILE A 1 111 ? 18.98932  26.36501  24.17875 1.000 71.39198  ? 134 ILE A O   1 
ATOM   615  C CB  . ILE A 1 111 ? 20.12456  29.36509  24.79315 1.000 68.79149  ? 134 ILE A CB  1 
ATOM   616  C CG1 . ILE A 1 111 ? 18.93763  29.82794  25.63669 1.000 53.00285  ? 134 ILE A CG1 1 
ATOM   617  C CG2 . ILE A 1 111 ? 20.98268  30.55677  24.37937 1.000 54.94425  ? 134 ILE A CG2 1 
ATOM   618  C CD1 . ILE A 1 111 ? 19.25155  29.92242  27.11616 1.000 64.75552  ? 134 ILE A CD1 1 
ATOM   619  N N   . ILE A 1 112 ? 17.35748  27.86452  23.80636 1.000 57.35873  ? 135 ILE A N   1 
ATOM   620  C CA  . ILE A 1 112 ? 16.32872  26.86566  24.05799 1.000 53.11857  ? 135 ILE A CA  1 
ATOM   621  C C   . ILE A 1 112 ? 16.27050  25.90327  22.87654 1.000 58.35351  ? 135 ILE A C   1 
ATOM   622  O O   . ILE A 1 112 ? 16.23127  24.68050  23.05842 1.000 68.24042  ? 135 ILE A O   1 
ATOM   623  C CB  . ILE A 1 112 ? 14.97275  27.54175  24.31810 1.000 41.29288  ? 135 ILE A CB  1 
ATOM   624  C CG1 . ILE A 1 112 ? 15.07741  28.48956  25.51437 1.000 27.85173  ? 135 ILE A CG1 1 
ATOM   625  C CG2 . ILE A 1 112 ? 13.89657  26.49951  24.53388 1.000 59.65513  ? 135 ILE A CG2 1 
ATOM   626  C CD1 . ILE A 1 112 ? 13.82942  29.31658  25.75145 1.000 42.97285  ? 135 ILE A CD1 1 
ATOM   627  N N   . GLU A 1 113 ? 16.24411  26.44136  21.64766 1.000 53.37637  ? 136 GLU A N   1 
ATOM   628  C CA  . GLU A 1 113 ? 16.30878  25.58803  20.46224 1.000 58.41430  ? 136 GLU A CA  1 
ATOM   629  C C   . GLU A 1 113 ? 17.53069  24.68435  20.54795 1.000 63.47347  ? 136 GLU A C   1 
ATOM   630  O O   . GLU A 1 113 ? 17.46268  23.47964  20.28558 1.000 80.79930  ? 136 GLU A O   1 
ATOM   631  C CB  . GLU A 1 113 ? 16.37434  26.43230  19.18619 1.000 51.37671  ? 136 GLU A CB  1 
ATOM   632  C CG  . GLU A 1 113 ? 15.11060  27.16088  18.83027 1.000 59.76708  ? 136 GLU A CG  1 
ATOM   633  C CD  . GLU A 1 113 ? 15.16998  27.78344  17.44917 1.000 77.64007  ? 136 GLU A CD  1 
ATOM   634  O OE1 . GLU A 1 113 ? 16.17447  28.46493  17.14672 1.000 74.32256  ? 136 GLU A OE1 1 
ATOM   635  O OE2 . GLU A 1 113 ? 14.21176  27.59329  16.66867 1.000 65.26227  ? 136 GLU A OE2 1 
ATOM   636  N N   . TYR A 1 114 ? 18.67039  25.27331  20.91195 1.000 74.88421  ? 137 TYR A N   1 
ATOM   637  C CA  . TYR A 1 114 ? 19.93541  24.54752  20.91723 1.000 71.01396  ? 137 TYR A CA  1 
ATOM   638  C C   . TYR A 1 114 ? 19.90141  23.36998  21.87772 1.000 66.41372  ? 137 TYR A C   1 
ATOM   639  O O   . TYR A 1 114 ? 20.41617  22.29289  21.56482 1.000 55.91798  ? 137 TYR A O   1 
ATOM   640  C CB  . TYR A 1 114 ? 21.08950  25.47923  21.27427 1.000 71.23248  ? 137 TYR A CB  1 
ATOM   641  C CG  . TYR A 1 114 ? 22.41568  24.76491  21.39173 1.000 80.26464  ? 137 TYR A CG  1 
ATOM   642  C CD1 . TYR A 1 114 ? 23.08025  24.27672  20.27336 1.000 80.23997  ? 137 TYR A CD1 1 
ATOM   643  C CD2 . TYR A 1 114 ? 23.00035  24.57715  22.63798 1.000 77.15212  ? 137 TYR A CD2 1 
ATOM   644  C CE1 . TYR A 1 114 ? 24.29721  23.62344  20.39855 1.000 78.01855  ? 137 TYR A CE1 1 
ATOM   645  C CE2 . TYR A 1 114 ? 24.20672  23.93038  22.77344 1.000 67.07606  ? 137 TYR A CE2 1 
ATOM   646  C CZ  . TYR A 1 114 ? 24.85402  23.45491  21.65420 1.000 98.36645  ? 137 TYR A CZ  1 
ATOM   647  O OH  . TYR A 1 114 ? 26.06172  22.80897  21.79931 1.000 142.83991 ? 137 TYR A OH  1 
ATOM   648  N N   . PHE A 1 115 ? 19.29094  23.54246  23.04112 1.000 61.05083  ? 138 PHE A N   1 
ATOM   649  C CA  . PHE A 1 115 ? 19.31394  22.46506  24.01032 1.000 60.55774  ? 138 PHE A CA  1 
ATOM   650  C C   . PHE A 1 115 ? 18.10509  21.55055  23.91901 1.000 73.10645  ? 138 PHE A C   1 
ATOM   651  O O   . PHE A 1 115 ? 18.24445  20.34002  24.14420 1.000 79.08867  ? 138 PHE A O   1 
ATOM   652  C CB  . PHE A 1 115 ? 19.33333  22.99586  25.44656 1.000 58.44202  ? 138 PHE A CB  1 
ATOM   653  C CG  . PHE A 1 115 ? 20.61745  23.62672  25.88398 1.000 75.56888  ? 138 PHE A CG  1 
ATOM   654  C CD1 . PHE A 1 115 ? 21.85843  23.02521  25.64738 1.000 74.76716  ? 138 PHE A CD1 1 
ATOM   655  C CD2 . PHE A 1 115 ? 20.56137  24.80088  26.62475 1.000 82.41009  ? 138 PHE A CD2 1 
ATOM   656  C CE1 . PHE A 1 115 ? 23.02604  23.63042  26.09764 1.000 61.76162  ? 138 PHE A CE1 1 
ATOM   657  C CE2 . PHE A 1 115 ? 21.70093  25.41085  27.08391 1.000 90.98481  ? 138 PHE A CE2 1 
ATOM   658  C CZ  . PHE A 1 115 ? 22.94533  24.83010  26.82279 1.000 76.93853  ? 138 PHE A CZ  1 
ATOM   659  N N   . HIS A 1 116 ? 16.93455  22.08453  23.57376 1.000 64.83019  ? 139 HIS A N   1 
ATOM   660  C CA  . HIS A 1 116 ? 15.67959  21.35015  23.71861 1.000 59.50201  ? 139 HIS A CA  1 
ATOM   661  C C   . HIS A 1 116 ? 14.71149  21.62621  22.57095 1.000 63.79714  ? 139 HIS A C   1 
ATOM   662  O O   . HIS A 1 116 ? 13.49988  21.73029  22.78871 1.000 67.57674  ? 139 HIS A O   1 
ATOM   663  C CB  . HIS A 1 116 ? 15.00224  21.68339  25.04722 1.000 64.76845  ? 139 HIS A CB  1 
ATOM   664  C CG  . HIS A 1 116 ? 15.87927  21.48448  26.24299 1.000 77.01133  ? 139 HIS A CG  1 
ATOM   665  N ND1 . HIS A 1 116 ? 16.14649  20.24044  26.77306 1.000 82.40349  ? 139 HIS A ND1 1 
ATOM   666  C CD2 . HIS A 1 116 ? 16.52482  22.37609  27.03141 1.000 66.24965  ? 139 HIS A CD2 1 
ATOM   667  C CE1 . HIS A 1 116 ? 16.93433  20.37354  27.82546 1.000 80.81289  ? 139 HIS A CE1 1 
ATOM   668  N NE2 . HIS A 1 116 ? 17.17927  21.65940  28.00321 1.000 80.41744  ? 139 HIS A NE2 1 
ATOM   669  N N   . GLU A 1 117 ? 15.21894  21.77232  21.33915 1.000 64.28371  ? 140 GLU A N   1 
ATOM   670  C CA  . GLU A 1 117 ? 14.37800  22.25832  20.24177 1.000 66.88947  ? 140 GLU A CA  1 
ATOM   671  C C   . GLU A 1 117 ? 13.12971  21.40284  20.07825 1.000 60.64946  ? 140 GLU A C   1 
ATOM   672  O O   . GLU A 1 117 ? 12.04140  21.92389  19.80750 1.000 78.78597  ? 140 GLU A O   1 
ATOM   673  C CB  . GLU A 1 117 ? 15.16247  22.27257  18.93098 1.000 78.45462  ? 140 GLU A CB  1 
ATOM   674  C CG  . GLU A 1 117 ? 14.46165  22.98784  17.78892 1.000 82.30169  ? 140 GLU A CG  1 
ATOM   675  C CD  . GLU A 1 117 ? 15.29689  23.01212  16.52421 1.000 93.04294  ? 140 GLU A CD  1 
ATOM   676  O OE1 . GLU A 1 117 ? 16.48826  22.63892  16.59049 1.000 111.64506 ? 140 GLU A OE1 1 
ATOM   677  O OE2 . GLU A 1 117 ? 14.75987  23.39531  15.46311 1.000 95.51318  ? 140 GLU A OE2 1 
ATOM   678  N N   . PHE A 1 118 ? 13.26785  20.08818  20.22302 1.000 59.41054  ? 141 PHE A N   1 
ATOM   679  C CA  . PHE A 1 118 ? 12.18777  19.15309  19.94757 1.000 42.21738  ? 141 PHE A CA  1 
ATOM   680  C C   . PHE A 1 118 ? 11.69657  18.49076  21.22452 1.000 35.82140  ? 141 PHE A C   1 
ATOM   681  O O   . PHE A 1 118 ? 10.94789  17.51087  21.16847 1.000 42.96894  ? 141 PHE A O   1 
ATOM   682  C CB  . PHE A 1 118 ? 12.63846  18.12530  18.91538 1.000 35.48527  ? 141 PHE A CB  1 
ATOM   683  C CG  . PHE A 1 118 ? 12.85370  18.71834  17.55929 1.000 49.83829  ? 141 PHE A CG  1 
ATOM   684  C CD1 . PHE A 1 118 ? 11.77288  19.08032  16.77495 1.000 50.42089  ? 141 PHE A CD1 1 
ATOM   685  C CD2 . PHE A 1 118 ? 14.13211  18.95764  17.08542 1.000 66.63747  ? 141 PHE A CD2 1 
ATOM   686  C CE1 . PHE A 1 118 ? 11.96144  19.64187  15.53186 1.000 58.88333  ? 141 PHE A CE1 1 
ATOM   687  C CE2 . PHE A 1 118 ? 14.32721  19.52032  15.84184 1.000 66.60546  ? 141 PHE A CE2 1 
ATOM   688  C CZ  . PHE A 1 118 ? 13.23844  19.86459  15.06583 1.000 74.48901  ? 141 PHE A CZ  1 
ATOM   689  N N   . ASP A 1 119 ? 12.10889  19.02067  22.37028 1.000 47.64927  ? 142 ASP A N   1 
ATOM   690  C CA  . ASP A 1 119 ? 11.61915  18.62525  23.67991 1.000 52.93257  ? 142 ASP A CA  1 
ATOM   691  C C   . ASP A 1 119 ? 10.36276  19.42336  24.01029 1.000 43.55277  ? 142 ASP A C   1 
ATOM   692  O O   . ASP A 1 119 ? 10.26276  20.61126  23.69037 1.000 41.48526  ? 142 ASP A O   1 
ATOM   693  C CB  . ASP A 1 119 ? 12.69167  18.83855  24.74985 1.000 55.43892  ? 142 ASP A CB  1 
ATOM   694  C CG  . ASP A 1 119 ? 13.93609  18.00063  24.50445 1.000 66.48101  ? 142 ASP A CG  1 
ATOM   695  O OD1 . ASP A 1 119 ? 13.82585  16.94214  23.84866 1.000 64.71556  ? 142 ASP A OD1 1 
ATOM   696  O OD2 . ASP A 1 119 ? 15.02598  18.39847  24.96820 1.000 78.67897  ? 142 ASP A OD2 1 
ATOM   697  N N   . GLU A 1 120 ? 9.40230   18.75898  24.62829 1.000 39.38317  ? 143 GLU A N   1 
ATOM   698  C CA  . GLU A 1 120 ? 8.21660   19.44727  25.12394 1.000 40.51352  ? 143 GLU A CA  1 
ATOM   699  C C   . GLU A 1 120 ? 8.59031   20.39393  26.25979 1.000 57.56130  ? 143 GLU A C   1 
ATOM   700  O O   . GLU A 1 120 ? 9.34620   20.01038  27.16171 1.000 49.44478  ? 143 GLU A O   1 
ATOM   701  C CB  . GLU A 1 120 ? 7.18093   18.43991  25.60682 1.000 45.83513  ? 143 GLU A CB  1 
ATOM   702  C CG  . GLU A 1 120 ? 6.37659   17.80549  24.50100 1.000 29.95714  ? 143 GLU A CG  1 
ATOM   703  C CD  . GLU A 1 120 ? 4.89476   17.85312  24.78123 1.000 31.98374  ? 143 GLU A CD  1 
ATOM   704  O OE1 . GLU A 1 120 ? 4.49714   18.56843  25.72526 1.000 46.77329  ? 143 GLU A OE1 1 
ATOM   705  O OE2 . GLU A 1 120 ? 4.12820   17.17611  24.06219 1.000 47.44127  ? 143 GLU A OE2 1 
ATOM   706  N N   . PRO A 1 121 ? 8.09522   21.64049  26.24389 1.000 53.59789  ? 144 PRO A N   1 
ATOM   707  C CA  . PRO A 1 121 ? 7.14595   22.20366  25.28286 1.000 40.00999  ? 144 PRO A CA  1 
ATOM   708  C C   . PRO A 1 121 ? 7.70445   23.15075  24.22702 1.000 41.19215  ? 144 PRO A C   1 
ATOM   709  O O   . PRO A 1 121 ? 6.96804   24.03425  23.79074 1.000 38.48528  ? 144 PRO A O   1 
ATOM   710  C CB  . PRO A 1 121 ? 6.19792   22.94157  26.22161 1.000 44.18880  ? 144 PRO A CB  1 
ATOM   711  C CG  . PRO A 1 121 ? 7.18417   23.60659  27.19020 1.000 43.90515  ? 144 PRO A CG  1 
ATOM   712  C CD  . PRO A 1 121 ? 8.36344   22.62242  27.30959 1.000 37.30662  ? 144 PRO A CD  1 
ATOM   713  N N   . ALA A 1 122 ? 8.96494   23.04496  23.79763 1.000 51.10331  ? 145 ALA A N   1 
ATOM   714  C CA  . ALA A 1 122 ? 9.37240   23.76644  22.59569 1.000 27.37881  ? 145 ALA A CA  1 
ATOM   715  C C   . ALA A 1 122 ? 8.58397   23.28868  21.38141 1.000 37.64103  ? 145 ALA A C   1 
ATOM   716  O O   . ALA A 1 122 ? 8.15145   24.09714  20.54936 1.000 31.77153  ? 145 ALA A O   1 
ATOM   717  C CB  . ALA A 1 122 ? 10.87260  23.59964  22.36754 1.000 35.19038  ? 145 ALA A CB  1 
ATOM   718  N N   . VAL A 1 123 ? 8.36035   21.97983  21.28477 1.000 33.34121  ? 146 VAL A N   1 
ATOM   719  C CA  . VAL A 1 123 ? 7.37340   21.38712  20.39132 1.000 24.14849  ? 146 VAL A CA  1 
ATOM   720  C C   . VAL A 1 123 ? 6.34982   20.67490  21.25782 1.000 25.09743  ? 146 VAL A C   1 
ATOM   721  O O   . VAL A 1 123 ? 6.71701   19.85888  22.11080 1.000 43.35276  ? 146 VAL A O   1 
ATOM   722  C CB  . VAL A 1 123 ? 8.01243   20.40350  19.39467 1.000 38.09227  ? 146 VAL A CB  1 
ATOM   723  C CG1 . VAL A 1 123 ? 6.93315   19.76379  18.52226 1.000 22.93212  ? 146 VAL A CG1 1 
ATOM   724  C CG2 . VAL A 1 123 ? 9.08197   21.09895  18.55095 1.000 25.84341  ? 146 VAL A CG2 1 
ATOM   725  N N   . ILE A 1 124 ? 5.07626   20.96278  21.03630 1.000 28.32297  ? 147 ILE A N   1 
ATOM   726  C CA  . ILE A 1 124 ? 4.01056   20.25251  21.72901 1.000 28.59181  ? 147 ILE A CA  1 
ATOM   727  C C   . ILE A 1 124 ? 3.56010   19.07460  20.87990 1.000 29.41030  ? 147 ILE A C   1 
ATOM   728  O O   . ILE A 1 124 ? 3.11483   19.24932  19.73963 1.000 29.55877  ? 147 ILE A O   1 
ATOM   729  C CB  . ILE A 1 124 ? 2.83176   21.18163  22.04990 1.000 30.66502  ? 147 ILE A CB  1 
ATOM   730  C CG1 . ILE A 1 124 ? 3.29872   22.35083  22.92009 1.000 22.55550  ? 147 ILE A CG1 1 
ATOM   731  C CG2 . ILE A 1 124 ? 1.71487   20.39705  22.73157 1.000 29.87968  ? 147 ILE A CG2 1 
ATOM   732  C CD1 . ILE A 1 124 ? 2.25680   23.43666  23.08943 1.000 21.11122  ? 147 ILE A CD1 1 
ATOM   733  N N   . TYR A 1 125 ? 3.68457   17.87417  21.43864 1.000 36.42808  ? 148 TYR A N   1 
ATOM   734  C CA  . TYR A 1 125 ? 3.12735   16.66074  20.85552 1.000 30.95782  ? 148 TYR A CA  1 
ATOM   735  C C   . TYR A 1 125 ? 1.81950   16.37015  21.58381 1.000 35.40226  ? 148 TYR A C   1 
ATOM   736  O O   . TYR A 1 125 ? 1.83115   15.95511  22.74801 1.000 36.32479  ? 148 TYR A O   1 
ATOM   737  C CB  . TYR A 1 125 ? 4.09520   15.48500  20.97421 1.000 29.12749  ? 148 TYR A CB  1 
ATOM   738  C CG  . TYR A 1 125 ? 5.49079   15.77024  20.47300 1.000 32.51029  ? 148 TYR A CG  1 
ATOM   739  C CD1 . TYR A 1 125 ? 6.43015   16.39797  21.28232 1.000 33.08720  ? 148 TYR A CD1 1 
ATOM   740  C CD2 . TYR A 1 125 ? 5.86397   15.42613  19.18010 1.000 37.78629  ? 148 TYR A CD2 1 
ATOM   741  C CE1 . TYR A 1 125 ? 7.71028   16.65452  20.82529 1.000 28.35258  ? 148 TYR A CE1 1 
ATOM   742  C CE2 . TYR A 1 125 ? 7.13694   15.68565  18.71182 1.000 54.99984  ? 148 TYR A CE2 1 
ATOM   743  C CZ  . TYR A 1 125 ? 8.05756   16.29752  19.53928 1.000 39.21005  ? 148 TYR A CZ  1 
ATOM   744  O OH  . TYR A 1 125 ? 9.32501   16.56315  19.07150 1.000 44.32218  ? 148 TYR A OH  1 
ATOM   745  N N   . SER A 1 126 ? 0.69701   16.58929  20.90590 1.000 17.68068  ? 149 SER A N   1 
ATOM   746  C CA  . SER A 1 126 ? -0.60734  16.60393  21.55020 1.000 29.40485  ? 149 SER A CA  1 
ATOM   747  C C   . SER A 1 126 ? -1.38185  15.34073  21.19293 1.000 34.65409  ? 149 SER A C   1 
ATOM   748  O O   . SER A 1 126 ? -1.00190  14.58133  20.29506 1.000 35.85388  ? 149 SER A O   1 
ATOM   749  C CB  . SER A 1 126 ? -1.39313  17.86275  21.16007 1.000 31.52293  ? 149 SER A CB  1 
ATOM   750  O OG  . SER A 1 126 ? -1.58237  17.94686  19.75852 1.000 41.67701  ? 149 SER A OG  1 
ATOM   751  N N   . SER A 1 127 ? -2.47645  15.11211  21.93073 1.000 32.80628  ? 150 SER A N   1 
ATOM   752  C CA  . SER A 1 127 ? -3.18629  13.83886  21.84114 1.000 27.51787  ? 150 SER A CA  1 
ATOM   753  C C   . SER A 1 127 ? -3.84780  13.64956  20.48621 1.000 22.78660  ? 150 SER A C   1 
ATOM   754  O O   . SER A 1 127 ? -4.12119  12.51102  20.09358 1.000 38.87576  ? 150 SER A O   1 
ATOM   755  C CB  . SER A 1 127 ? -4.24078  13.72838  22.94474 1.000 29.10210  ? 150 SER A CB  1 
ATOM   756  O OG  . SER A 1 127 ? -5.08001  14.86909  22.97490 1.000 39.13088  ? 150 SER A OG  1 
ATOM   757  N N   . ASN A 1 128 ? -4.11078  14.73415  19.76794 1.000 33.36001  ? 151 ASN A N   1 
ATOM   758  C CA  . ASN A 1 128 ? -4.67165  14.64660  18.42864 1.000 28.61833  ? 151 ASN A CA  1 
ATOM   759  C C   . ASN A 1 128 ? -3.60914  14.40044  17.36421 1.000 19.75844  ? 151 ASN A C   1 
ATOM   760  O O   . ASN A 1 128 ? -3.94572  14.35136  16.17970 1.000 32.34194  ? 151 ASN A O   1 
ATOM   761  C CB  . ASN A 1 128 ? -5.49497  15.90641  18.11540 1.000 19.22160  ? 151 ASN A CB  1 
ATOM   762  C CG  . ASN A 1 128 ? -4.64544  17.16083  17.97055 1.000 30.20298  ? 151 ASN A CG  1 
ATOM   763  O OD1 . ASN A 1 128 ? -3.41541  17.10938  17.92801 1.000 39.34642  ? 151 ASN A OD1 1 
ATOM   764  N ND2 . ASN A 1 128 ? -5.31254  18.30442  17.89050 1.000 35.43508  ? 151 ASN A ND2 1 
ATOM   765  N N   . GLY A 1 129 ? -2.34481  14.23884  17.75585 1.000 25.29349  ? 152 GLY A N   1 
ATOM   766  C CA  . GLY A 1 129 ? -1.28307  13.86883  16.84353 1.000 28.08136  ? 152 GLY A CA  1 
ATOM   767  C C   . GLY A 1 129 ? -0.47042  15.03032  16.30972 1.000 35.49995  ? 152 GLY A C   1 
ATOM   768  O O   . GLY A 1 129 ? 0.56790   14.79866  15.67636 1.000 36.68406  ? 152 GLY A O   1 
ATOM   769  N N   . ASN A 1 130 ? -0.90638  16.26410  16.54788 1.000 29.04057  ? 153 ASN A N   1 
ATOM   770  C CA  . ASN A 1 130 ? -0.20221  17.43169  16.03815 1.000 37.54777  ? 153 ASN A CA  1 
ATOM   771  C C   . ASN A 1 130 ? 1.14685   17.61304  16.72330 1.000 35.12570  ? 153 ASN A C   1 
ATOM   772  O O   . ASN A 1 130 ? 1.33702   17.24939  17.88822 1.000 31.58379  ? 153 ASN A O   1 
ATOM   773  C CB  . ASN A 1 130 ? -1.04154  18.69455  16.23508 1.000 27.86850  ? 153 ASN A CB  1 
ATOM   774  C CG  . ASN A 1 130 ? -2.16800  18.80536  15.23640 1.000 39.11793  ? 153 ASN A CG  1 
ATOM   775  O OD1 . ASN A 1 130 ? -2.30746  17.96233  14.35171 1.000 49.83276  ? 153 ASN A OD1 1 
ATOM   776  N ND2 . ASN A 1 130 ? -2.98915  19.84252  15.37772 1.000 40.40249  ? 153 ASN A ND2 1 
ATOM   777  N N   . LYS A 1 131 ? 2.09835   18.15645  15.96501 1.000 36.41124  ? 154 LYS A N   1 
ATOM   778  C CA  . LYS A 1 131 ? 3.31877   18.74311  16.50814 1.000 36.83131  ? 154 LYS A CA  1 
ATOM   779  C C   . LYS A 1 131 ? 3.17369   20.25419  16.36591 1.000 34.23563  ? 154 LYS A C   1 
ATOM   780  O O   . LYS A 1 131 ? 3.10508   20.77335  15.24635 1.000 46.31219  ? 154 LYS A O   1 
ATOM   781  C CB  . LYS A 1 131 ? 4.55405   18.24552  15.76314 1.000 20.34444  ? 154 LYS A CB  1 
ATOM   782  C CG  . LYS A 1 131 ? 4.86906   16.77116  15.94094 1.000 30.78234  ? 154 LYS A CG  1 
ATOM   783  C CD  . LYS A 1 131 ? 6.00628   16.37617  15.01031 1.000 34.46677  ? 154 LYS A CD  1 
ATOM   784  C CE  . LYS A 1 131 ? 6.28261   14.89031  15.04602 1.000 41.73479  ? 154 LYS A CE  1 
ATOM   785  N NZ  . LYS A 1 131 ? 7.29847   14.49462  14.02448 1.000 33.43061  ? 154 LYS A NZ  1 
ATOM   786  N N   . THR A 1 132 ? 3.10356   20.95998  17.48869 1.000 27.05395  ? 155 THR A N   1 
ATOM   787  C CA  . THR A 1 132 ? 2.91728   22.40487  17.47780 1.000 19.07064  ? 155 THR A CA  1 
ATOM   788  C C   . THR A 1 132 ? 4.14102   23.07188  18.08615 1.000 24.79748  ? 155 THR A C   1 
ATOM   789  O O   . THR A 1 132 ? 4.54758   22.73124  19.20306 1.000 29.98880  ? 155 THR A O   1 
ATOM   790  C CB  . THR A 1 132 ? 1.64808   22.80175  18.22799 1.000 31.92650  ? 155 THR A CB  1 
ATOM   791  O OG1 . THR A 1 132 ? 0.51386   22.18656  17.60030 1.000 29.82187  ? 155 THR A OG1 1 
ATOM   792  C CG2 . THR A 1 132 ? 1.47575   24.31051  18.20364 1.000 26.11177  ? 155 THR A CG2 1 
ATOM   793  N N   . VAL A 1 133 ? 4.74345   23.99245  17.33596 1.000 24.26963  ? 156 VAL A N   1 
ATOM   794  C CA  . VAL A 1 133 ? 5.98133   24.64933  17.73774 1.000 26.73680  ? 156 VAL A CA  1 
ATOM   795  C C   . VAL A 1 133 ? 5.63021   25.80793  18.66312 1.000 25.50536  ? 156 VAL A C   1 
ATOM   796  O O   . VAL A 1 133 ? 5.59352   26.96739  18.23089 1.000 23.36648  ? 156 VAL A O   1 
ATOM   797  C CB  . VAL A 1 133 ? 6.77435   25.13072  16.50758 1.000 19.75400  ? 156 VAL A CB  1 
ATOM   798  C CG1 . VAL A 1 133 ? 8.17727   25.58778  16.90614 1.000 19.84869  ? 156 VAL A CG1 1 
ATOM   799  C CG2 . VAL A 1 133 ? 6.83124   24.03924  15.44777 1.000 18.37387  ? 156 VAL A CG2 1 
ATOM   800  N N   . TRP A 1 134 ? 5.37167   25.51056  19.94240 1.000 29.57715  ? 157 TRP A N   1 
ATOM   801  C CA  . TRP A 1 134 ? 4.98921   26.57259  20.87087 1.000 28.18154  ? 157 TRP A CA  1 
ATOM   802  C C   . TRP A 1 134 ? 6.06542   27.64193  20.98177 1.000 38.57353  ? 157 TRP A C   1 
ATOM   803  O O   . TRP A 1 134 ? 5.74468   28.82365  21.16734 1.000 42.24775  ? 157 TRP A O   1 
ATOM   804  C CB  . TRP A 1 134 ? 4.67132   25.98555  22.24651 1.000 25.77600  ? 157 TRP A CB  1 
ATOM   805  C CG  . TRP A 1 134 ? 4.56198   27.01928  23.31069 1.000 21.94031  ? 157 TRP A CG  1 
ATOM   806  C CD1 . TRP A 1 134 ? 5.39445   27.19884  24.37868 1.000 28.01067  ? 157 TRP A CD1 1 
ATOM   807  C CD2 . TRP A 1 134 ? 3.59376   28.06945  23.37386 1.000 28.57957  ? 157 TRP A CD2 1 
ATOM   808  N NE1 . TRP A 1 134 ? 4.97656   28.27543  25.12737 1.000 37.99114  ? 157 TRP A NE1 1 
ATOM   809  C CE2 . TRP A 1 134 ? 3.87578   28.83052  24.52696 1.000 37.80395  ? 157 TRP A CE2 1 
ATOM   810  C CE3 . TRP A 1 134 ? 2.50443   28.43013  22.57549 1.000 24.77461  ? 157 TRP A CE3 1 
ATOM   811  C CZ2 . TRP A 1 134 ? 3.10775   29.93221  24.89945 1.000 23.51302  ? 157 TRP A CZ2 1 
ATOM   812  C CZ3 . TRP A 1 134 ? 1.74559   29.52213  22.94332 1.000 26.98971  ? 157 TRP A CZ3 1 
ATOM   813  C CH2 . TRP A 1 134 ? 2.05029   30.26265  24.09589 1.000 24.47381  ? 157 TRP A CH2 1 
ATOM   814  N N   . LEU A 1 135 ? 7.33925   27.24709  20.86367 1.000 33.75983  ? 158 LEU A N   1 
ATOM   815  C CA  . LEU A 1 135 ? 8.43887   28.20386  20.95574 1.000 25.29237  ? 158 LEU A CA  1 
ATOM   816  C C   . LEU A 1 135 ? 8.24575   29.33786  19.96150 1.000 29.68762  ? 158 LEU A C   1 
ATOM   817  O O   . LEU A 1 135 ? 8.45105   30.51114  20.29268 1.000 37.54888  ? 158 LEU A O   1 
ATOM   818  C CB  . LEU A 1 135 ? 9.78202   27.50642  20.75774 1.000 29.88291  ? 158 LEU A CB  1 
ATOM   819  C CG  . LEU A 1 135 ? 10.96216  28.47326  20.88575 1.000 57.44416  ? 158 LEU A CG  1 
ATOM   820  C CD1 . LEU A 1 135 ? 11.06515  29.01813  22.28677 1.000 50.29675  ? 158 LEU A CD1 1 
ATOM   821  C CD2 . LEU A 1 135 ? 12.25984  27.76761  20.54252 1.000 42.25112  ? 158 LEU A CD2 1 
ATOM   822  N N   . ARG A 1 136 ? 7.82595   29.00263  18.73986 1.000 28.48187  ? 159 ARG A N   1 
ATOM   823  C CA  . ARG A 1 136 ? 7.65833   30.01271  17.70158 1.000 36.62551  ? 159 ARG A CA  1 
ATOM   824  C C   . ARG A 1 136 ? 6.53253   30.96765  18.07576 1.000 23.86001  ? 159 ARG A C   1 
ATOM   825  O O   . ARG A 1 136 ? 6.70287   32.19274  18.03954 1.000 29.05474  ? 159 ARG A O   1 
ATOM   826  C CB  . ARG A 1 136 ? 7.38880   29.32800  16.36097 1.000 19.44435  ? 159 ARG A CB  1 
ATOM   827  C CG  . ARG A 1 136 ? 7.09917   30.26126  15.20043 1.000 25.33999  ? 159 ARG A CG  1 
ATOM   828  C CD  . ARG A 1 136 ? 6.69331   29.43749  13.98253 1.000 23.86160  ? 159 ARG A CD  1 
ATOM   829  N NE  . ARG A 1 136 ? 7.67843   28.39562  13.71881 1.000 23.90803  ? 159 ARG A NE  1 
ATOM   830  C CZ  . ARG A 1 136 ? 7.41969   27.23985  13.12086 1.000 43.55626  ? 159 ARG A CZ  1 
ATOM   831  N NH1 . ARG A 1 136 ? 6.20789   26.94878  12.66826 1.000 27.60857  ? 159 ARG A NH1 1 
ATOM   832  N NH2 . ARG A 1 136 ? 8.40685   26.36070  12.95629 1.000 25.77012  ? 159 ARG A NH2 1 
ATOM   833  N N   . TYR A 1 137 ? 5.36728   30.42497  18.42694 1.000 23.67635  ? 160 TYR A N   1 
ATOM   834  C CA  . TYR A 1 137 ? 4.21284   31.28061  18.66472 1.000 25.17253  ? 160 TYR A CA  1 
ATOM   835  C C   . TYR A 1 137 ? 4.43816   32.09973  19.92678 1.000 29.06315  ? 160 TYR A C   1 
ATOM   836  O O   . TYR A 1 137 ? 4.09116   33.28610  19.97923 1.000 36.79652  ? 160 TYR A O   1 
ATOM   837  C CB  . TYR A 1 137 ? 2.94129   30.43798  18.74934 1.000 19.39374  ? 160 TYR A CB  1 
ATOM   838  C CG  . TYR A 1 137 ? 2.74938   29.58482  17.51448 1.000 24.22509  ? 160 TYR A CG  1 
ATOM   839  C CD1 . TYR A 1 137 ? 2.64546   30.16329  16.25512 1.000 29.56887  ? 160 TYR A CD1 1 
ATOM   840  C CD2 . TYR A 1 137 ? 2.70526   28.20252  17.60393 1.000 20.82452  ? 160 TYR A CD2 1 
ATOM   841  C CE1 . TYR A 1 137 ? 2.48441   29.38755  15.12213 1.000 27.38736  ? 160 TYR A CE1 1 
ATOM   842  C CE2 . TYR A 1 137 ? 2.54287   27.41766  16.47567 1.000 33.75848  ? 160 TYR A CE2 1 
ATOM   843  C CZ  . TYR A 1 137 ? 2.43439   28.01592  15.23775 1.000 22.62404  ? 160 TYR A CZ  1 
ATOM   844  O OH  . TYR A 1 137 ? 2.27178   27.23708  14.11298 1.000 28.66443  ? 160 TYR A OH  1 
ATOM   845  N N   . ALA A 1 138 ? 5.02557   31.47481  20.95207 1.000 26.81541  ? 161 ALA A N   1 
ATOM   846  C CA  . ALA A 1 138 ? 5.40227   32.20064  22.16145 1.000 24.55067  ? 161 ALA A CA  1 
ATOM   847  C C   . ALA A 1 138 ? 6.37246   33.32681  21.83364 1.000 33.09345  ? 161 ALA A C   1 
ATOM   848  O O   . ALA A 1 138 ? 6.21112   34.45958  22.30439 1.000 39.61185  ? 161 ALA A O   1 
ATOM   849  C CB  . ALA A 1 138 ? 6.01943   31.24369  23.18028 1.000 18.24416  ? 161 ALA A CB  1 
ATOM   850  N N   . GLU A 1 139 ? 7.39717   33.02554  21.02994 1.000 31.77812  ? 162 GLU A N   1 
ATOM   851  C CA  . GLU A 1 139 ? 8.33386   34.05552  20.58565 1.000 16.96516  ? 162 GLU A CA  1 
ATOM   852  C C   . GLU A 1 139 ? 7.60168   35.18338  19.86321 1.000 35.02303  ? 162 GLU A C   1 
ATOM   853  O O   . GLU A 1 139 ? 7.90501   36.36240  20.08481 1.000 41.39622  ? 162 GLU A O   1 
ATOM   854  C CB  . GLU A 1 139 ? 9.42781   33.42440  19.72346 1.000 24.60581  ? 162 GLU A CB  1 
ATOM   855  C CG  . GLU A 1 139 ? 10.52142  34.36337  19.24199 1.000 35.09456  ? 162 GLU A CG  1 
ATOM   856  C CD  . GLU A 1 139 ? 10.51262  34.54153  17.74254 1.000 54.46990  ? 162 GLU A CD  1 
ATOM   857  O OE1 . GLU A 1 139 ? 11.60591  34.71474  17.15859 1.000 58.98852  ? 162 GLU A OE1 1 
ATOM   858  O OE2 . GLU A 1 139 ? 9.41865   34.49169  17.14588 1.000 68.11822  ? 162 GLU A OE2 1 
ATOM   859  N N   . TRP A 1 140 ? 6.65200   34.84761  18.97721 1.000 27.19035  ? 163 TRP A N   1 
ATOM   860  C CA  . TRP A 1 140 ? 5.90103   35.89532  18.28315 1.000 21.80412  ? 163 TRP A CA  1 
ATOM   861  C C   . TRP A 1 140 ? 5.18023   36.78709  19.28459 1.000 22.58717  ? 163 TRP A C   1 
ATOM   862  O O   . TRP A 1 140 ? 5.13104   38.01206  19.12033 1.000 34.97360  ? 163 TRP A O   1 
ATOM   863  C CB  . TRP A 1 140 ? 4.88625   35.30546  17.30105 1.000 26.04844  ? 163 TRP A CB  1 
ATOM   864  C CG  . TRP A 1 140 ? 5.46005   34.53814  16.15405 1.000 27.65926  ? 163 TRP A CG  1 
ATOM   865  C CD1 . TRP A 1 140 ? 6.77867   34.41145  15.82005 1.000 31.00118  ? 163 TRP A CD1 1 
ATOM   866  C CD2 . TRP A 1 140 ? 4.72136   33.83873  15.14542 1.000 25.09447  ? 163 TRP A CD2 1 
ATOM   867  N NE1 . TRP A 1 140 ? 6.90775   33.64837  14.68222 1.000 39.71620  ? 163 TRP A NE1 1 
ATOM   868  C CE2 . TRP A 1 140 ? 5.65933   33.28585  14.24701 1.000 39.61019  ? 163 TRP A CE2 1 
ATOM   869  C CE3 . TRP A 1 140 ? 3.35791   33.61534  14.92132 1.000 26.60243  ? 163 TRP A CE3 1 
ATOM   870  C CZ2 . TRP A 1 140 ? 5.27719   32.52041  13.14339 1.000 28.52083  ? 163 TRP A CZ2 1 
ATOM   871  C CZ3 . TRP A 1 140 ? 2.97951   32.85325  13.82347 1.000 38.33279  ? 163 TRP A CZ3 1 
ATOM   872  C CH2 . TRP A 1 140 ? 3.93709   32.31718  12.94902 1.000 37.99283  ? 163 TRP A CH2 1 
ATOM   873  N N   . LEU A 1 141 ? 4.59337   36.17970  20.31859 1.000 30.68857  ? 164 LEU A N   1 
ATOM   874  C CA  . LEU A 1 141 ? 3.86484   36.93535  21.33183 1.000 31.32305  ? 164 LEU A CA  1 
ATOM   875  C C   . LEU A 1 141 ? 4.79349   37.87531  22.09166 1.000 26.48175  ? 164 LEU A C   1 
ATOM   876  O O   . LEU A 1 141 ? 4.37361   38.95444  22.52340 1.000 28.25277  ? 164 LEU A O   1 
ATOM   877  C CB  . LEU A 1 141 ? 3.18022   35.96584  22.29516 1.000 26.78039  ? 164 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 141 ? 1.91142   35.29355  21.76302 1.000 32.82431  ? 164 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 141 ? 1.53364   34.10974  22.63454 1.000 42.97363  ? 164 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 141 ? 0.75837   36.28455  21.67587 1.000 26.16262  ? 164 LEU A CD2 1 
ATOM   881  N N   . LEU A 1 142 ? 6.05813   37.48554  22.25711 1.000 26.19339  ? 165 LEU A N   1 
ATOM   882  C CA  . LEU A 1 142 ? 7.02091   38.31636  22.97050 1.000 21.60680  ? 165 LEU A CA  1 
ATOM   883  C C   . LEU A 1 142 ? 7.52591   39.46022  22.09792 1.000 25.92472  ? 165 LEU A C   1 
ATOM   884  O O   . LEU A 1 142 ? 7.73136   40.57616  22.59033 1.000 31.47982  ? 165 LEU A O   1 
ATOM   885  C CB  . LEU A 1 142 ? 8.18524   37.46211  23.47074 1.000 26.55713  ? 165 LEU A CB  1 
ATOM   886  C CG  . LEU A 1 142 ? 7.83566   36.50837  24.61527 1.000 22.78391  ? 165 LEU A CG  1 
ATOM   887  C CD1 . LEU A 1 142 ? 9.02483   35.63595  24.97302 1.000 19.01593  ? 165 LEU A CD1 1 
ATOM   888  C CD2 . LEU A 1 142 ? 7.34191   37.28317  25.82781 1.000 14.36784  ? 165 LEU A CD2 1 
ATOM   889  N N   . THR A 1 143 ? 7.73840   39.20510  20.80886 1.000 25.75265  ? 166 THR A N   1 
ATOM   890  C CA  . THR A 1 143 ? 8.48992   40.10544  19.94286 1.000 19.70482  ? 166 THR A CA  1 
ATOM   891  C C   . THR A 1 143 ? 7.59086   40.95176  19.04993 1.000 17.64870  ? 166 THR A C   1 
ATOM   892  O O   . THR A 1 143 ? 7.85896   42.14561  18.88251 1.000 29.00627  ? 166 THR A O   1 
ATOM   893  C CB  . THR A 1 143 ? 9.47688   39.31236  19.08029 1.000 20.48276  ? 166 THR A CB  1 
ATOM   894  O OG1 . THR A 1 143 ? 8.75468   38.43328  18.20677 1.000 33.01726  ? 166 THR A OG1 1 
ATOM   895  C CG2 . THR A 1 143 ? 10.40587  38.49352  19.96582 1.000 23.33334  ? 166 THR A CG2 1 
ATOM   896  N N   . CYS A 1 144 ? 6.54977   40.36932  18.44458 1.000 22.55096  ? 167 CYS A N   1 
ATOM   897  C CA  . CYS A 1 144 ? 5.76173   41.12086  17.46595 1.000 34.87317  ? 167 CYS A CA  1 
ATOM   898  C C   . CYS A 1 144 ? 5.13793   42.37776  18.05687 1.000 21.77177  ? 167 CYS A C   1 
ATOM   899  O O   . CYS A 1 144 ? 5.22057   43.43733  17.41006 1.000 35.99325  ? 167 CYS A O   1 
ATOM   900  C CB  . CYS A 1 144 ? 4.69505   40.22607  16.83102 1.000 30.02041  ? 167 CYS A CB  1 
ATOM   901  S SG  . CYS A 1 144 ? 5.38428   38.87236  15.90391 1.000 32.48063  ? 167 CYS A SG  1 
ATOM   902  N N   . PRO A 1 145 ? 4.49830   42.35222  19.23339 1.000 20.59071  ? 168 PRO A N   1 
ATOM   903  C CA  . PRO A 1 145 ? 3.96092   43.61546  19.76539 1.000 29.69659  ? 168 PRO A CA  1 
ATOM   904  C C   . PRO A 1 145 ? 5.03877   44.66881  19.93103 1.000 29.69406  ? 168 PRO A C   1 
ATOM   905  O O   . PRO A 1 145 ? 4.77186   45.85632  19.70371 1.000 36.20708  ? 168 PRO A O   1 
ATOM   906  C CB  . PRO A 1 145 ? 3.32942   43.21251  21.10761 1.000 31.36544  ? 168 PRO A CB  1 
ATOM   907  C CG  . PRO A 1 145 ? 3.10681   41.74334  21.02078 1.000 14.86894  ? 168 PRO A CG  1 
ATOM   908  C CD  . PRO A 1 145 ? 4.13574   41.19537  20.07683 1.000 22.71804  ? 168 PRO A CD  1 
ATOM   909  N N   . VAL A 1 146 ? 6.26807   44.26183  20.26129 1.000 27.50763  ? 169 VAL A N   1 
ATOM   910  C CA  . VAL A 1 146 ? 7.33586   45.23313  20.48313 1.000 27.46418  ? 169 VAL A CA  1 
ATOM   911  C C   . VAL A 1 146 ? 7.77116   45.84221  19.15747 1.000 25.20009  ? 169 VAL A C   1 
ATOM   912  O O   . VAL A 1 146 ? 8.04726   47.04631  19.07382 1.000 28.58633  ? 169 VAL A O   1 
ATOM   913  C CB  . VAL A 1 146 ? 8.51680   44.58012  21.22362 1.000 17.35886  ? 169 VAL A CB  1 
ATOM   914  C CG1 . VAL A 1 146 ? 9.67868   45.55613  21.33175 1.000 26.94870  ? 169 VAL A CG1 1 
ATOM   915  C CG2 . VAL A 1 146 ? 8.07972   44.11724  22.60293 1.000 19.40109  ? 169 VAL A CG2 1 
ATOM   916  N N   . ILE A 1 147 ? 7.84193   45.02243  18.10323 1.000 26.17019  ? 170 ILE A N   1 
ATOM   917  C CA  . ILE A 1 147 ? 8.08307   45.54849  16.76083 1.000 27.82662  ? 170 ILE A CA  1 
ATOM   918  C C   . ILE A 1 147 ? 7.01252   46.56969  16.39952 1.000 42.54837  ? 170 ILE A C   1 
ATOM   919  O O   . ILE A 1 147 ? 7.30680   47.62813  15.82642 1.000 38.39727  ? 170 ILE A O   1 
ATOM   920  C CB  . ILE A 1 147 ? 8.14062   44.40726  15.72885 1.000 22.89950  ? 170 ILE A CB  1 
ATOM   921  C CG1 . ILE A 1 147 ? 9.48075   43.67270  15.80562 1.000 27.38717  ? 170 ILE A CG1 1 
ATOM   922  C CG2 . ILE A 1 147 ? 7.91279   44.94769  14.32848 1.000 27.56379  ? 170 ILE A CG2 1 
ATOM   923  C CD1 . ILE A 1 147 ? 9.42260   42.25548  15.27519 1.000 26.04722  ? 170 ILE A CD1 1 
ATOM   924  N N   . LEU A 1 148 ? 5.75292   46.27513  16.73583 1.000 35.49745  ? 171 LEU A N   1 
ATOM   925  C CA  . LEU A 1 148 ? 4.67783   47.19082  16.37674 1.000 31.19255  ? 171 LEU A CA  1 
ATOM   926  C C   . LEU A 1 148 ? 4.73950   48.45566  17.22082 1.000 31.02472  ? 171 LEU A C   1 
ATOM   927  O O   . LEU A 1 148 ? 4.40394   49.54279  16.73350 1.000 31.50249  ? 171 LEU A O   1 
ATOM   928  C CB  . LEU A 1 148 ? 3.32770   46.49775  16.53443 1.000 27.28097  ? 171 LEU A CB  1 
ATOM   929  C CG  . LEU A 1 148 ? 3.05685   45.41057  15.49260 1.000 31.37145  ? 171 LEU A CG  1 
ATOM   930  C CD1 . LEU A 1 148 ? 1.67427   44.81816  15.69246 1.000 43.72965  ? 171 LEU A CD1 1 
ATOM   931  C CD2 . LEU A 1 148 ? 3.22061   45.94825  14.07752 1.000 24.38116  ? 171 LEU A CD2 1 
ATOM   932  N N   . ILE A 1 149 ? 5.19152   48.34173  18.47193 1.000 25.47568  ? 172 ILE A N   1 
ATOM   933  C CA  . ILE A 1 149 ? 5.40981   49.53334  19.28687 1.000 22.36454  ? 172 ILE A CA  1 
ATOM   934  C C   . ILE A 1 149 ? 6.50791   50.37905  18.65471 1.000 32.85879  ? 172 ILE A C   1 
ATOM   935  O O   . ILE A 1 149 ? 6.39149   51.60623  18.54745 1.000 44.24055  ? 172 ILE A O   1 
ATOM   936  C CB  . ILE A 1 149 ? 5.74044   49.14466  20.73792 1.000 16.08412  ? 172 ILE A CB  1 
ATOM   937  C CG1 . ILE A 1 149 ? 4.50431   48.54766  21.41410 1.000 17.16715  ? 172 ILE A CG1 1 
ATOM   938  C CG2 . ILE A 1 149 ? 6.22248   50.35160  21.51234 1.000 20.58644  ? 172 ILE A CG2 1 
ATOM   939  C CD1 . ILE A 1 149 ? 4.81446   47.77662  22.68277 1.000 23.42681  ? 172 ILE A CD1 1 
ATOM   940  N N   . HIS A 1 150 ? 7.60408   49.72655  18.24909 1.000 27.61582  ? 173 HIS A N   1 
ATOM   941  C CA  . HIS A 1 150 ? 8.66726   50.39848  17.50643 1.000 18.44134  ? 173 HIS A CA  1 
ATOM   942  C C   . HIS A 1 150 ? 8.08850   51.08791  16.27818 1.000 25.83225  ? 173 HIS A C   1 
ATOM   943  O O   . HIS A 1 150 ? 8.36048   52.26746  16.02224 1.000 29.73440  ? 173 HIS A O   1 
ATOM   944  C CB  . HIS A 1 150 ? 9.74061   49.38013  17.10537 1.000 24.09676  ? 173 HIS A CB  1 
ATOM   945  C CG  . HIS A 1 150 ? 10.96937  49.98425  16.49371 1.000 31.20062  ? 173 HIS A CG  1 
ATOM   946  N ND1 . HIS A 1 150 ? 11.06524  51.31825  16.15719 1.000 38.87013  ? 173 HIS A ND1 1 
ATOM   947  C CD2 . HIS A 1 150 ? 12.16164  49.42924  16.16794 1.000 30.79774  ? 173 HIS A CD2 1 
ATOM   948  C CE1 . HIS A 1 150 ? 12.25969  51.55716  15.64452 1.000 38.41509  ? 173 HIS A CE1 1 
ATOM   949  N NE2 . HIS A 1 150 ? 12.94452  50.42715  15.63960 1.000 29.77737  ? 173 HIS A NE2 1 
ATOM   950  N N   . LEU A 1 151 ? 7.28886   50.35029  15.50073 1.000 30.54844  ? 174 LEU A N   1 
ATOM   951  C CA  . LEU A 1 151 ? 6.70786   50.89800  14.27927 1.000 28.81139  ? 174 LEU A CA  1 
ATOM   952  C C   . LEU A 1 151 ? 5.91012   52.16132  14.57301 1.000 32.80498  ? 174 LEU A C   1 
ATOM   953  O O   . LEU A 1 151 ? 5.95812   53.13115  13.80646 1.000 42.59726  ? 174 LEU A O   1 
ATOM   954  C CB  . LEU A 1 151 ? 5.81995   49.84362  13.61688 1.000 29.27651  ? 174 LEU A CB  1 
ATOM   955  C CG  . LEU A 1 151 ? 4.97129   50.29940  12.42977 1.000 32.21289  ? 174 LEU A CG  1 
ATOM   956  C CD1 . LEU A 1 151 ? 5.84034   50.85757  11.31805 1.000 47.16292  ? 174 LEU A CD1 1 
ATOM   957  C CD2 . LEU A 1 151 ? 4.10503   49.15210  11.92674 1.000 25.96979  ? 174 LEU A CD2 1 
ATOM   958  N N   . SER A 1 152 ? 5.19248   52.17650  15.69650 1.000 33.90530  ? 175 SER A N   1 
ATOM   959  C CA  . SER A 1 152 ? 4.37073   53.31608  16.08074 1.000 20.45156  ? 175 SER A CA  1 
ATOM   960  C C   . SER A 1 152 ? 5.19815   54.52255  16.48943 1.000 24.23550  ? 175 SER A C   1 
ATOM   961  O O   . SER A 1 152 ? 4.62827   55.59907  16.69638 1.000 62.30632  ? 175 SER A O   1 
ATOM   962  C CB  . SER A 1 152 ? 3.43092   52.92635  17.21840 1.000 28.66469  ? 175 SER A CB  1 
ATOM   963  O OG  . SER A 1 152 ? 2.66949   51.78391  16.86442 1.000 39.80795  ? 175 SER A OG  1 
ATOM   964  N N   . ASN A 1 153 ? 6.51401   54.36829  16.63123 1.000 24.51282  ? 176 ASN A N   1 
ATOM   965  C CA  . ASN A 1 153 ? 7.40341   55.47563  16.95849 1.000 38.65316  ? 176 ASN A CA  1 
ATOM   966  C C   . ASN A 1 153 ? 8.72382   55.28316  16.20688 1.000 39.34688  ? 176 ASN A C   1 
ATOM   967  O O   . ASN A 1 153 ? 9.80012   55.15157  16.78594 1.000 37.81109  ? 176 ASN A O   1 
ATOM   968  C CB  . ASN A 1 153 ? 7.60577   55.57242  18.47102 1.000 42.42715  ? 176 ASN A CB  1 
ATOM   969  C CG  . ASN A 1 153 ? 8.31924   56.84220  18.88680 1.000 34.67120  ? 176 ASN A CG  1 
ATOM   970  O OD1 . ASN A 1 153 ? 8.30296   57.84019  18.16805 1.000 57.66779  ? 176 ASN A OD1 1 
ATOM   971  N ND2 . ASN A 1 153 ? 8.94654   56.81244  20.05756 1.000 41.96255  ? 176 ASN A ND2 1 
ATOM   972  N N   . LEU A 1 154 ? 8.62506   55.26982  14.87275 1.000 30.90202  ? 177 LEU A N   1 
ATOM   973  C CA  . LEU A 1 154 ? 9.79056   55.01336  14.03047 1.000 33.77168  ? 177 LEU A CA  1 
ATOM   974  C C   . LEU A 1 154 ? 10.86306  56.07761  14.23614 1.000 36.57019  ? 177 LEU A C   1 
ATOM   975  O O   . LEU A 1 154 ? 12.06018  55.76723  14.26650 1.000 40.04500  ? 177 LEU A O   1 
ATOM   976  C CB  . LEU A 1 154 ? 9.36290   54.93968  12.56463 1.000 29.77654  ? 177 LEU A CB  1 
ATOM   977  C CG  . LEU A 1 154 ? 8.79808   53.59309  12.10978 1.000 31.40591  ? 177 LEU A CG  1 
ATOM   978  C CD1 . LEU A 1 154 ? 8.32096   53.67590  10.67536 1.000 38.85163  ? 177 LEU A CD1 1 
ATOM   979  C CD2 . LEU A 1 154 ? 9.85159   52.50519  12.25751 1.000 34.41949  ? 177 LEU A CD2 1 
ATOM   980  N N   . THR A 1 155 ? 10.45430  57.34085  14.37089 1.000 40.47463  ? 178 THR A N   1 
ATOM   981  C CA  . THR A 1 155 ? 11.41661  58.42092  14.55484 1.000 42.82067  ? 178 THR A CA  1 
ATOM   982  C C   . THR A 1 155 ? 12.04155  58.37579  15.94180 1.000 48.65498  ? 178 THR A C   1 
ATOM   983  O O   . THR A 1 155 ? 13.13721  58.91258  16.13645 1.000 57.80573  ? 178 THR A O   1 
ATOM   984  C CB  . THR A 1 155 ? 10.75515  59.78187  14.33450 1.000 34.47920  ? 178 THR A CB  1 
ATOM   985  O OG1 . THR A 1 155 ? 9.82111   60.03684  15.39105 1.000 40.46157  ? 178 THR A OG1 1 
ATOM   986  C CG2 . THR A 1 155 ? 10.01791  59.80411  13.00231 1.000 37.41826  ? 178 THR A CG2 1 
ATOM   987  N N   . GLY A 1 156 ? 11.35413  57.76881  16.90891 1.000 48.95183  ? 179 GLY A N   1 
ATOM   988  C CA  . GLY A 1 156 ? 11.78205  57.74338  18.28876 1.000 46.80154  ? 179 GLY A CA  1 
ATOM   989  C C   . GLY A 1 156 ? 11.54428  59.01873  19.06001 1.000 50.51691  ? 179 GLY A C   1 
ATOM   990  O O   . GLY A 1 156 ? 11.88558  59.07398  20.24902 1.000 54.22577  ? 179 GLY A O   1 
ATOM   991  N N   . LEU A 1 157 ? 10.93922  60.03212  18.44297 1.000 44.63974  ? 180 LEU A N   1 
ATOM   992  C CA  . LEU A 1 157 ? 10.77222  61.31078  19.11623 1.000 54.16536  ? 180 LEU A CA  1 
ATOM   993  C C   . LEU A 1 157 ? 9.48484   61.36491  19.91757 1.000 64.94131  ? 180 LEU A C   1 
ATOM   994  O O   . LEU A 1 157 ? 9.43573   62.03395  20.95659 1.000 82.00855  ? 180 LEU A O   1 
ATOM   995  C CB  . LEU A 1 157 ? 10.75821  62.44419  18.08684 1.000 51.00193  ? 180 LEU A CB  1 
ATOM   996  C CG  . LEU A 1 157 ? 11.92206  62.51011  17.09876 1.000 56.08808  ? 180 LEU A CG  1 
ATOM   997  C CD1 . LEU A 1 157 ? 11.71463  63.65474  16.11838 1.000 44.86284  ? 180 LEU A CD1 1 
ATOM   998  C CD2 . LEU A 1 157 ? 13.24156  62.65366  17.83800 1.000 57.07861  ? 180 LEU A CD2 1 
ATOM   999  N N   . ALA A 1 158 ? 8.44736   60.67431  19.45189 1.000 63.18206  ? 181 ALA A N   1 
ATOM   1000 C CA  . ALA A 1 158 ? 7.16189   60.69277  20.13213 1.000 65.66552  ? 181 ALA A CA  1 
ATOM   1001 C C   . ALA A 1 158 ? 7.28643   60.11411  21.53541 1.000 74.34600  ? 181 ALA A C   1 
ATOM   1002 O O   . ALA A 1 158 ? 8.04630   59.17080  21.77379 1.000 88.49963  ? 181 ALA A O   1 
ATOM   1003 C CB  . ALA A 1 158 ? 6.12153   59.91106  19.32888 1.000 58.41601  ? 181 ALA A CB  1 
ATOM   1004 N N   . ASN A 1 159 ? 6.53542   60.69214  22.46827 1.000 73.02800  ? 182 ASN A N   1 
ATOM   1005 C CA  . ASN A 1 159 ? 6.40476   60.15075  23.81099 1.000 81.42411  ? 182 ASN A CA  1 
ATOM   1006 C C   . ASN A 1 159 ? 5.04227   59.52442  24.04707 1.000 74.89473  ? 182 ASN A C   1 
ATOM   1007 O O   . ASN A 1 159 ? 4.84405   58.88097  25.08386 1.000 76.59789  ? 182 ASN A O   1 
ATOM   1008 C CB  . ASN A 1 159 ? 6.67384   61.22924  24.87155 1.000 96.45817  ? 182 ASN A CB  1 
ATOM   1009 C CG  . ASN A 1 159 ? 8.07643   61.80258  24.77607 1.000 111.43416 ? 182 ASN A CG  1 
ATOM   1010 O OD1 . ASN A 1 159 ? 8.30189   62.97687  25.07118 1.000 81.74680  ? 182 ASN A OD1 1 
ATOM   1011 N ND2 . ASN A 1 159 ? 9.03162   60.96773  24.37090 1.000 94.84509  ? 182 ASN A ND2 1 
ATOM   1012 N N   . ASP A 1 160 ? 4.10613   59.69921  23.11832 1.000 75.30647  ? 183 ASP A N   1 
ATOM   1013 C CA  . ASP A 1 160 ? 2.75619   59.18208  23.24369 1.000 84.02092  ? 183 ASP A CA  1 
ATOM   1014 C C   . ASP A 1 160 ? 2.42061   58.29307  22.05009 1.000 92.75004  ? 183 ASP A C   1 
ATOM   1015 O O   . ASP A 1 160 ? 3.10241   58.30620  21.02030 1.000 88.92239  ? 183 ASP A O   1 
ATOM   1016 C CB  . ASP A 1 160 ? 1.74573   60.33113  23.34746 1.000 87.44102  ? 183 ASP A CB  1 
ATOM   1017 C CG  . ASP A 1 160 ? 1.88472   61.11402  24.63908 1.000 97.56905  ? 183 ASP A CG  1 
ATOM   1018 O OD1 . ASP A 1 160 ? 2.89942   61.82650  24.79560 1.000 102.20248 ? 183 ASP A OD1 1 
ATOM   1019 O OD2 . ASP A 1 160 ? 0.98189   61.01805  25.49743 1.000 109.09196 ? 183 ASP A OD2 1 
ATOM   1020 N N   . TYR A 1 161 ? 1.35222   57.51369  22.20812 1.000 95.03276  ? 184 TYR A N   1 
ATOM   1021 C CA  . TYR A 1 161 ? 0.81572   56.64953  21.16527 1.000 86.46699  ? 184 TYR A CA  1 
ATOM   1022 C C   . TYR A 1 161 ? -0.68017  56.90228  21.04287 1.000 78.72309  ? 184 TYR A C   1 
ATOM   1023 O O   . TYR A 1 161 ? -1.37259  57.04163  22.05516 1.000 81.84358  ? 184 TYR A O   1 
ATOM   1024 C CB  . TYR A 1 161 ? 1.09454   55.17110  21.47673 1.000 90.28575  ? 184 TYR A CB  1 
ATOM   1025 C CG  . TYR A 1 161 ? 2.56763   54.85098  21.64802 1.000 67.35618  ? 184 TYR A CG  1 
ATOM   1026 C CD1 . TYR A 1 161 ? 3.19191   54.99323  22.88217 1.000 67.67812  ? 184 TYR A CD1 1 
ATOM   1027 C CD2 . TYR A 1 161 ? 3.33288   54.41099  20.57537 1.000 50.42789  ? 184 TYR A CD2 1 
ATOM   1028 C CE1 . TYR A 1 161 ? 4.53470   54.70246  23.04322 1.000 58.50834  ? 184 TYR A CE1 1 
ATOM   1029 C CE2 . TYR A 1 161 ? 4.67614   54.11959  20.72610 1.000 47.12534  ? 184 TYR A CE2 1 
ATOM   1030 C CZ  . TYR A 1 161 ? 5.27218   54.26628  21.96207 1.000 56.97280  ? 184 TYR A CZ  1 
ATOM   1031 O OH  . TYR A 1 161 ? 6.61182   53.98120  22.11439 1.000 58.38806  ? 184 TYR A OH  1 
ATOM   1032 N N   . ASN A 1 162 ? -1.18516  56.94635  19.81111 1.000 70.92223  ? 185 ASN A N   1 
ATOM   1033 C CA  . ASN A 1 162 ? -2.60129  57.22547  19.62485 1.000 82.51570  ? 185 ASN A CA  1 
ATOM   1034 C C   . ASN A 1 162 ? -3.45264  55.98732  19.91963 1.000 61.27652  ? 185 ASN A C   1 
ATOM   1035 O O   . ASN A 1 162 ? -2.94889  54.91247  20.25848 1.000 54.85617  ? 185 ASN A O   1 
ATOM   1036 C CB  . ASN A 1 162 ? -2.84366  57.75409  18.21145 1.000 89.46820  ? 185 ASN A CB  1 
ATOM   1037 C CG  . ASN A 1 162 ? -2.26802  56.84652  17.13647 1.000 64.78980  ? 185 ASN A CG  1 
ATOM   1038 O OD1 . ASN A 1 162 ? -1.88238  55.70937  17.40280 1.000 68.45411  ? 185 ASN A OD1 1 
ATOM   1039 N ND2 . ASN A 1 162 ? -2.20139  57.35463  15.91194 1.000 81.90643  ? 185 ASN A ND2 1 
ATOM   1040 N N   . LYS A 1 163 ? -4.77501  56.15242  19.80836 1.000 67.24362  ? 186 LYS A N   1 
ATOM   1041 C CA  . LYS A 1 163 ? -5.68086  55.01030  19.89715 1.000 55.09339  ? 186 LYS A CA  1 
ATOM   1042 C C   . LYS A 1 163 ? -5.39444  53.96730  18.82261 1.000 57.36495  ? 186 LYS A C   1 
ATOM   1043 O O   . LYS A 1 163 ? -5.50760  52.76187  19.07814 1.000 40.26964  ? 186 LYS A O   1 
ATOM   1044 C CB  . LYS A 1 163 ? -7.13254  55.48506  19.81203 1.000 47.43909  ? 186 LYS A CB  1 
ATOM   1045 N N   . ARG A 1 164 ? -5.02048  54.40477  17.61411 1.000 61.10265  ? 187 ARG A N   1 
ATOM   1046 C CA  . ARG A 1 164 ? -4.83056  53.44708  16.52529 1.000 71.80209  ? 187 ARG A CA  1 
ATOM   1047 C C   . ARG A 1 164 ? -3.69624  52.47725  16.84360 1.000 61.14091  ? 187 ARG A C   1 
ATOM   1048 O O   . ARG A 1 164 ? -3.75642  51.29893  16.46749 1.000 51.06734  ? 187 ARG A O   1 
ATOM   1049 C CB  . ARG A 1 164 ? -4.66279  54.17270  15.18417 1.000 69.21125  ? 187 ARG A CB  1 
ATOM   1050 C CG  . ARG A 1 164 ? -3.83065  53.47091  14.12054 1.000 65.54707  ? 187 ARG A CG  1 
ATOM   1051 C CD  . ARG A 1 164 ? -3.24767  54.48394  13.14827 1.000 49.46825  ? 187 ARG A CD  1 
ATOM   1052 N NE  . ARG A 1 164 ? -1.97210  55.06756  13.53415 1.000 94.16775  ? 187 ARG A NE  1 
ATOM   1053 C CZ  . ARG A 1 164 ? -1.20871  55.75981  12.70025 1.000 94.50808  ? 187 ARG A CZ  1 
ATOM   1054 N NH1 . ARG A 1 164 ? -1.57870  55.97536  11.44748 1.000 90.38756  ? 187 ARG A NH1 1 
ATOM   1055 N NH2 . ARG A 1 164 ? -0.05760  56.26424  13.13733 1.000 67.28761  ? 187 ARG A NH2 1 
ATOM   1056 N N   . THR A 1 165 ? -2.64966  52.95841  17.52640 1.000 59.67169  ? 188 THR A N   1 
ATOM   1057 C CA  . THR A 1 165 ? -1.56425  52.07679  17.95463 1.000 50.60403  ? 188 THR A CA  1 
ATOM   1058 C C   . THR A 1 165 ? -2.11019  50.90081  18.75389 1.000 42.17547  ? 188 THR A C   1 
ATOM   1059 O O   . THR A 1 165 ? -1.68875  49.75358  18.56216 1.000 38.35120  ? 188 THR A O   1 
ATOM   1060 C CB  . THR A 1 165 ? -0.54986  52.84867  18.80127 1.000 37.85421  ? 188 THR A CB  1 
ATOM   1061 O OG1 . THR A 1 165 ? -0.10429  54.01316  18.09330 1.000 60.97421  ? 188 THR A OG1 1 
ATOM   1062 C CG2 . THR A 1 165 ? 0.62253   51.96005  19.17993 1.000 27.37775  ? 188 THR A CG2 1 
ATOM   1063 N N   . MET A 1 166 ? -3.03831  51.17883  19.67124 1.000 42.53407  ? 189 MET A N   1 
ATOM   1064 C CA  . MET A 1 166 ? -3.54638  50.15253  20.56994 1.000 27.83289  ? 189 MET A CA  1 
ATOM   1065 C C   . MET A 1 166 ? -4.30823  49.09483  19.78357 1.000 27.63077  ? 189 MET A C   1 
ATOM   1066 O O   . MET A 1 166 ? -4.21013  47.89803  20.07756 1.000 33.00618  ? 189 MET A O   1 
ATOM   1067 C CB  . MET A 1 166 ? -4.41651  50.79394  21.64955 1.000 26.25012  ? 189 MET A CB  1 
ATOM   1068 C CG  . MET A 1 166 ? -3.59839  51.65215  22.59722 1.000 43.78705  ? 189 MET A CG  1 
ATOM   1069 S SD  . MET A 1 166 ? -2.00904  50.88976  22.98193 1.000 58.82288  ? 189 MET A SD  1 
ATOM   1070 C CE  . MET A 1 166 ? -1.97792  51.08038  24.76311 1.000 43.32324  ? 189 MET A CE  1 
ATOM   1071 N N   . GLY A 1 167 ? -5.05994  49.52315  18.77010 1.000 39.68651  ? 190 GLY A N   1 
ATOM   1072 C CA  . GLY A 1 167 ? -5.76066  48.57808  17.91714 1.000 26.00980  ? 190 GLY A CA  1 
ATOM   1073 C C   . GLY A 1 167 ? -4.79170  47.70265  17.14705 1.000 28.49348  ? 190 GLY A C   1 
ATOM   1074 O O   . GLY A 1 167 ? -5.03496  46.50800  16.95158 1.000 31.69518  ? 190 GLY A O   1 
ATOM   1075 N N   . LEU A 1 168 ? -3.68546  48.29160  16.68580 1.000 45.28324  ? 191 LEU A N   1 
ATOM   1076 C CA  . LEU A 1 168 ? -2.65438  47.51418  16.00655 1.000 40.21312  ? 191 LEU A CA  1 
ATOM   1077 C C   . LEU A 1 168 ? -2.18269  46.36748  16.89688 1.000 40.44496  ? 191 LEU A C   1 
ATOM   1078 O O   . LEU A 1 168 ? -2.01572  45.23553  16.42605 1.000 52.15475  ? 191 LEU A O   1 
ATOM   1079 C CB  . LEU A 1 168 ? -1.50714  48.43977  15.61068 1.000 32.63190  ? 191 LEU A CB  1 
ATOM   1080 C CG  . LEU A 1 168 ? -0.27255  47.87132  14.93156 1.000 56.50582  ? 191 LEU A CG  1 
ATOM   1081 C CD1 . LEU A 1 168 ? -0.48512  47.80902  13.42916 1.000 53.34051  ? 191 LEU A CD1 1 
ATOM   1082 C CD2 . LEU A 1 168 ? 0.90468   48.76933  15.26849 1.000 59.78737  ? 191 LEU A CD2 1 
ATOM   1083 N N   . LEU A 1 169 ? -1.95705  46.64094  18.18569 1.000 29.92906  ? 192 LEU A N   1 
ATOM   1084 C CA  . LEU A 1 169 ? -1.39284  45.63079  19.07965 1.000 22.20017  ? 192 LEU A CA  1 
ATOM   1085 C C   . LEU A 1 169 ? -2.42930  44.54531  19.35949 1.000 23.82551  ? 192 LEU A C   1 
ATOM   1086 O O   . LEU A 1 169 ? -2.10983  43.34997  19.36398 1.000 22.84166  ? 192 LEU A O   1 
ATOM   1087 C CB  . LEU A 1 169 ? -0.91896  46.27188  20.38344 1.000 21.84530  ? 192 LEU A CB  1 
ATOM   1088 C CG  . LEU A 1 169 ? 0.26302   47.23602  20.30929 1.000 34.92588  ? 192 LEU A CG  1 
ATOM   1089 C CD1 . LEU A 1 169 ? 0.56856   47.78459  21.68948 1.000 33.80849  ? 192 LEU A CD1 1 
ATOM   1090 C CD2 . LEU A 1 169 ? 1.48315   46.53069  19.73647 1.000 37.51051  ? 192 LEU A CD2 1 
ATOM   1091 N N   . VAL A 1 170 ? -3.68163  44.95293  19.58863 1.000 30.13532  ? 193 VAL A N   1 
ATOM   1092 C CA  . VAL A 1 170 ? -4.74347  44.02281  19.96731 1.000 25.97856  ? 193 VAL A CA  1 
ATOM   1093 C C   . VAL A 1 170 ? -5.08188  43.11545  18.79069 1.000 25.15152  ? 193 VAL A C   1 
ATOM   1094 O O   . VAL A 1 170 ? -5.31736  41.91153  18.96270 1.000 27.66057  ? 193 VAL A O   1 
ATOM   1095 C CB  . VAL A 1 170 ? -5.98046  44.79326  20.46971 1.000 30.73961  ? 193 VAL A CB  1 
ATOM   1096 C CG1 . VAL A 1 170 ? -7.15258  43.85013  20.68756 1.000 27.12848  ? 193 VAL A CG1 1 
ATOM   1097 C CG2 . VAL A 1 170 ? -5.65687  45.53977  21.75267 1.000 36.63868  ? 193 VAL A CG2 1 
ATOM   1098 N N   . SER A 1 171 ? -5.10830  43.67604  17.57697 1.000 30.33499  ? 194 SER A N   1 
ATOM   1099 C CA  . SER A 1 171 ? -5.36284  42.86244  16.39196 1.000 34.88646  ? 194 SER A CA  1 
ATOM   1100 C C   . SER A 1 171 ? -4.24228  41.85315  16.19813 1.000 20.71988  ? 194 SER A C   1 
ATOM   1101 O O   . SER A 1 171 ? -4.48641  40.71503  15.78194 1.000 34.41012  ? 194 SER A O   1 
ATOM   1102 C CB  . SER A 1 171 ? -5.50334  43.74285  15.15093 1.000 33.76197  ? 194 SER A CB  1 
ATOM   1103 O OG  . SER A 1 171 ? -4.29919  44.43884  14.87566 1.000 29.06270  ? 194 SER A OG  1 
ATOM   1104 N N   . ASP A 1 172 ? -3.00320  42.25094  16.49250 1.000 25.65856  ? 195 ASP A N   1 
ATOM   1105 C CA  . ASP A 1 172 ? -1.87418  41.37011  16.22018 1.000 25.98685  ? 195 ASP A CA  1 
ATOM   1106 C C   . ASP A 1 172 ? -1.83548  40.23350  17.22877 1.000 24.62095  ? 195 ASP A C   1 
ATOM   1107 O O   . ASP A 1 172 ? -1.52006  39.09155  16.87180 1.000 37.87932  ? 195 ASP A O   1 
ATOM   1108 C CB  . ASP A 1 172 ? -0.56166  42.14546  16.24475 1.000 21.95239  ? 195 ASP A CB  1 
ATOM   1109 C CG  . ASP A 1 172 ? 0.63674   41.24754  16.02166 1.000 29.28952  ? 195 ASP A CG  1 
ATOM   1110 O OD1 . ASP A 1 172 ? 0.73557   40.63244  14.93876 1.000 38.48338  ? 195 ASP A OD1 1 
ATOM   1111 O OD2 . ASP A 1 172 ? 1.48106   41.15127  16.93560 1.000 39.01881  ? 195 ASP A OD2 1 
ATOM   1112 N N   . ILE A 1 173 ? -2.14349  40.52812  18.49533 1.000 22.09903  ? 196 ILE A N   1 
ATOM   1113 C CA  . ILE A 1 173 ? -2.17619  39.47595  19.50772 1.000 15.10628  ? 196 ILE A CA  1 
ATOM   1114 C C   . ILE A 1 173 ? -3.22005  38.44182  19.12139 1.000 19.79781  ? 196 ILE A C   1 
ATOM   1115 O O   . ILE A 1 173 ? -2.97502  37.23018  19.19221 1.000 37.07243  ? 196 ILE A O   1 
ATOM   1116 C CB  . ILE A 1 173 ? -2.44894  40.05915  20.90632 1.000 13.96630  ? 196 ILE A CB  1 
ATOM   1117 C CG1 . ILE A 1 173 ? -1.27748  40.92054  21.36875 1.000 10.54437  ? 196 ILE A CG1 1 
ATOM   1118 C CG2 . ILE A 1 173 ? -2.69031  38.93952  21.90356 1.000 12.28252  ? 196 ILE A CG2 1 
ATOM   1119 C CD1 . ILE A 1 173 ? -1.66995  41.98558  22.37557 1.000 23.62973  ? 196 ILE A CD1 1 
ATOM   1120 N N   . GLY A 1 174 ? -4.39908  38.90664  18.69633 1.000 17.56511  ? 197 GLY A N   1 
ATOM   1121 C CA  . GLY A 1 174 ? -5.44763  37.98305  18.29711 1.000 12.78216  ? 197 GLY A CA  1 
ATOM   1122 C C   . GLY A 1 174 ? -4.99718  37.09748  17.15362 1.000 14.26300  ? 197 GLY A C   1 
ATOM   1123 O O   . GLY A 1 174 ? -5.25492  35.89142  17.15500 1.000 25.39112  ? 197 GLY A O   1 
ATOM   1124 N N   . THR A 1 175 ? -4.29171  37.67991  16.17698 1.000 20.65978  ? 198 THR A N   1 
ATOM   1125 C CA  . THR A 1 175 ? -3.79848  36.90532  15.04100 1.000 23.65167  ? 198 THR A CA  1 
ATOM   1126 C C   . THR A 1 175 ? -3.00256  35.70904  15.53647 1.000 18.57332  ? 198 THR A C   1 
ATOM   1127 O O   . THR A 1 175 ? -3.23354  34.56854  15.11803 1.000 28.76685  ? 198 THR A O   1 
ATOM   1128 C CB  . THR A 1 175 ? -2.92594  37.77620  14.13303 1.000 31.03143  ? 198 THR A CB  1 
ATOM   1129 O OG1 . THR A 1 175 ? -3.68375  38.88900  13.63908 1.000 33.89207  ? 198 THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 175 ? -2.39589  36.95668  12.96553 1.000 34.36662  ? 198 THR A CG2 1 
ATOM   1131 N N   . ILE A 1 176 ? -2.04044  35.96261  16.42179 1.000 25.02920  ? 199 ILE A N   1 
ATOM   1132 C CA  . ILE A 1 176 ? -1.16008  34.90323  16.89720 1.000 17.03420  ? 199 ILE A CA  1 
ATOM   1133 C C   . ILE A 1 176 ? -1.96037  33.87304  17.68481 1.000 20.56687  ? 199 ILE A C   1 
ATOM   1134 O O   . ILE A 1 176 ? -1.73772  32.66148  17.55726 1.000 15.73383  ? 199 ILE A O   1 
ATOM   1135 C CB  . ILE A 1 176 ? -0.02547  35.51089  17.73514 1.000 14.79127  ? 199 ILE A CB  1 
ATOM   1136 C CG1 . ILE A 1 176 ? 0.76970   36.48530  16.86837 1.000 12.55855  ? 199 ILE A CG1 1 
ATOM   1137 C CG2 . ILE A 1 176 ? 0.86246   34.41032  18.30009 1.000 20.39242  ? 199 ILE A CG2 1 
ATOM   1138 C CD1 . ILE A 1 176 ? 1.52675   37.51348  17.64639 1.000 16.43665  ? 199 ILE A CD1 1 
ATOM   1139 N N   . VAL A 1 177 ? -2.89302  34.33905  18.52620 1.000 23.60438  ? 200 VAL A N   1 
ATOM   1140 C CA  . VAL A 1 177 ? -3.68635  33.42636  19.35099 1.000 16.21357  ? 200 VAL A CA  1 
ATOM   1141 C C   . VAL A 1 177 ? -4.54637  32.52634  18.47055 1.000 23.74652  ? 200 VAL A C   1 
ATOM   1142 O O   . VAL A 1 177 ? -4.64654  31.31390  18.70605 1.000 27.06342  ? 200 VAL A O   1 
ATOM   1143 C CB  . VAL A 1 177 ? -4.53893  34.21807  20.35803 1.000 21.22681  ? 200 VAL A CB  1 
ATOM   1144 C CG1 . VAL A 1 177 ? -5.49598  33.28864  21.07768 1.000 23.91910  ? 200 VAL A CG1 1 
ATOM   1145 C CG2 . VAL A 1 177 ? -3.64411  34.95012  21.35493 1.000 23.74026  ? 200 VAL A CG2 1 
ATOM   1146 N N   . TRP A 1 178 ? -5.19726  33.10741  17.45479 1.000 26.19260  ? 201 TRP A N   1 
ATOM   1147 C CA  . TRP A 1 178 ? -5.98032  32.30593  16.51567 1.000 17.56027  ? 201 TRP A CA  1 
ATOM   1148 C C   . TRP A 1 178 ? -5.07227  31.38323  15.71487 1.000 21.32237  ? 201 TRP A C   1 
ATOM   1149 O O   . TRP A 1 178 ? -5.38968  30.20188  15.52764 1.000 26.27430  ? 201 TRP A O   1 
ATOM   1150 C CB  . TRP A 1 178 ? -6.80267  33.20332  15.58970 1.000 21.37456  ? 201 TRP A CB  1 
ATOM   1151 C CG  . TRP A 1 178 ? -7.72428  34.13578  16.31610 1.000 22.98451  ? 201 TRP A CG  1 
ATOM   1152 C CD1 . TRP A 1 178 ? -7.93441  35.45777  16.04412 1.000 35.34231  ? 201 TRP A CD1 1 
ATOM   1153 C CD2 . TRP A 1 178 ? -8.58862  33.81048  17.41573 1.000 27.26873  ? 201 TRP A CD2 1 
ATOM   1154 N NE1 . TRP A 1 178 ? -8.85372  35.98117  16.92194 1.000 42.48915  ? 201 TRP A NE1 1 
ATOM   1155 C CE2 . TRP A 1 178 ? -9.27395  34.98957  17.76988 1.000 34.70791  ? 201 TRP A CE2 1 
ATOM   1156 C CE3 . TRP A 1 178 ? -8.84513  32.63859  18.13810 1.000 33.29190  ? 201 TRP A CE3 1 
ATOM   1157 C CZ2 . TRP A 1 178 ? -10.19716 35.03102  18.81190 1.000 35.32582  ? 201 TRP A CZ2 1 
ATOM   1158 C CZ3 . TRP A 1 178 ? -9.76085  32.68189  19.17083 1.000 30.03714  ? 201 TRP A CZ3 1 
ATOM   1159 C CH2 . TRP A 1 178 ? -10.42717 33.86921  19.49758 1.000 35.62121  ? 201 TRP A CH2 1 
ATOM   1160 N N   . GLY A 1 179 ? -3.93548  31.90627  15.23715 1.000 22.68719  ? 202 GLY A N   1 
ATOM   1161 C CA  . GLY A 1 179 ? -3.01931  31.07772  14.47077 1.000 15.40229  ? 202 GLY A CA  1 
ATOM   1162 C C   . GLY A 1 179 ? -2.49186  29.92507  15.30007 1.000 18.87307  ? 202 GLY A C   1 
ATOM   1163 O O   . GLY A 1 179 ? -2.41144  28.78964  14.82279 1.000 27.63638  ? 202 GLY A O   1 
ATOM   1164 N N   . THR A 1 180 ? -2.13663  30.19812  16.55853 1.000 28.23848  ? 203 THR A N   1 
ATOM   1165 C CA  . THR A 1 180 ? -1.64039  29.13975  17.43104 1.000 18.83936  ? 203 THR A CA  1 
ATOM   1166 C C   . THR A 1 180 ? -2.72407  28.09410  17.63162 1.000 19.87397  ? 203 THR A C   1 
ATOM   1167 O O   . THR A 1 180 ? -2.47128  26.88595  17.54454 1.000 38.13036  ? 203 THR A O   1 
ATOM   1168 C CB  . THR A 1 180 ? -1.21106  29.72327  18.77721 1.000 25.50012  ? 203 THR A CB  1 
ATOM   1169 O OG1 . THR A 1 180 ? -0.31416  30.82137  18.56291 1.000 25.74941  ? 203 THR A OG1 1 
ATOM   1170 C CG2 . THR A 1 180 ? -0.52701  28.66183  19.62424 1.000 23.82434  ? 203 THR A CG2 1 
ATOM   1171 N N   . THR A 1 181 ? -3.94622  28.55325  17.91588 1.000 24.33345  ? 204 THR A N   1 
ATOM   1172 C CA  . THR A 1 181 ? -5.06331  27.63671  18.11318 1.000 29.76712  ? 204 THR A CA  1 
ATOM   1173 C C   . THR A 1 181 ? -5.29170  26.79994  16.86319 1.000 34.90335  ? 204 THR A C   1 
ATOM   1174 O O   . THR A 1 181 ? -5.51311  25.58542  16.94951 1.000 29.47623  ? 204 THR A O   1 
ATOM   1175 C CB  . THR A 1 181 ? -6.32736  28.41146  18.48585 1.000 16.76340  ? 204 THR A CB  1 
ATOM   1176 O OG1 . THR A 1 181 ? -6.08082  29.19109  19.66483 1.000 19.01530  ? 204 THR A OG1 1 
ATOM   1177 C CG2 . THR A 1 181 ? -7.48401  27.45515  18.73663 1.000 24.52667  ? 204 THR A CG2 1 
ATOM   1178 N N   . ALA A 1 182 ? -5.21546  27.43664  15.68833 1.000 31.66647  ? 205 ALA A N   1 
ATOM   1179 C CA  . ALA A 1 182 ? -5.35056  26.71219  14.42831 1.000 21.98135  ? 205 ALA A CA  1 
ATOM   1180 C C   . ALA A 1 182 ? -4.28063  25.63865  14.30197 1.000 29.00576  ? 205 ALA A C   1 
ATOM   1181 O O   . ALA A 1 182 ? -4.57643  24.50088  13.91476 1.000 37.58597  ? 205 ALA A O   1 
ATOM   1182 C CB  . ALA A 1 182 ? -5.27495  27.68507  13.25223 1.000 25.46941  ? 205 ALA A CB  1 
ATOM   1183 N N   . ALA A 1 183 ? -3.03154  25.97836  14.63658 1.000 33.76890  ? 206 ALA A N   1 
ATOM   1184 C CA  . ALA A 1 183 ? -1.95152  25.00076  14.54778 1.000 28.99589  ? 206 ALA A CA  1 
ATOM   1185 C C   . ALA A 1 183 ? -2.20241  23.83571  15.49467 1.000 31.92502  ? 206 ALA A C   1 
ATOM   1186 O O   . ALA A 1 183 ? -1.90797  22.67981  15.16511 1.000 42.32467  ? 206 ALA A O   1 
ATOM   1187 C CB  . ALA A 1 183 ? -0.61093  25.66900  14.85396 1.000 28.28059  ? 206 ALA A CB  1 
ATOM   1188 N N   . LEU A 1 184 ? -2.77086  24.11971  16.66842 1.000 30.10669  ? 207 LEU A N   1 
ATOM   1189 C CA  . LEU A 1 184 ? -3.05965  23.07422  17.64277 1.000 30.60462  ? 207 LEU A CA  1 
ATOM   1190 C C   . LEU A 1 184 ? -4.24585  22.21444  17.21817 1.000 36.71789  ? 207 LEU A C   1 
ATOM   1191 O O   . LEU A 1 184 ? -4.38591  21.08533  17.70078 1.000 42.78041  ? 207 LEU A O   1 
ATOM   1192 C CB  . LEU A 1 184 ? -3.34787  23.71232  19.00182 1.000 24.97363  ? 207 LEU A CB  1 
ATOM   1193 C CG  . LEU A 1 184 ? -2.16777  24.29207  19.77861 1.000 31.97776  ? 207 LEU A CG  1 
ATOM   1194 C CD1 . LEU A 1 184 ? -2.67853  25.12600  20.94010 1.000 21.78611  ? 207 LEU A CD1 1 
ATOM   1195 C CD2 . LEU A 1 184 ? -1.27595  23.17119  20.28561 1.000 29.66508  ? 207 LEU A CD2 1 
ATOM   1196 N N   . SER A 1 185 ? -5.10816  22.73602  16.34568 1.000 36.73470  ? 208 SER A N   1 
ATOM   1197 C CA  . SER A 1 185 ? -6.34029  22.08505  15.93087 1.000 29.48264  ? 208 SER A CA  1 
ATOM   1198 C C   . SER A 1 185 ? -6.13078  21.25614  14.66410 1.000 37.84925  ? 208 SER A C   1 
ATOM   1199 O O   . SER A 1 185 ? -5.02626  21.14823  14.12432 1.000 34.74172  ? 208 SER A O   1 
ATOM   1200 C CB  . SER A 1 185 ? -7.44279  23.11782  15.70878 1.000 24.71797  ? 208 SER A CB  1 
ATOM   1201 O OG  . SER A 1 185 ? -7.73016  23.81972  16.90102 1.000 39.01266  ? 208 SER A OG  1 
ATOM   1202 N N   . LYS A 1 186 ? -7.22690  20.66937  14.18396 1.000 48.79976  ? 209 LYS A N   1 
ATOM   1203 C CA  . LYS A 1 186 ? -7.24792  19.85549  12.97696 1.000 57.24385  ? 209 LYS A CA  1 
ATOM   1204 C C   . LYS A 1 186 ? -8.53462  20.13932  12.21711 1.000 50.48804  ? 209 LYS A C   1 
ATOM   1205 O O   . LYS A 1 186 ? -9.49546  20.68349  12.76852 1.000 51.32456  ? 209 LYS A O   1 
ATOM   1206 C CB  . LYS A 1 186 ? -7.16726  18.34952  13.27325 1.000 46.40850  ? 209 LYS A CB  1 
ATOM   1207 C CG  . LYS A 1 186 ? -5.80160  17.82947  13.67982 1.000 48.72005  ? 209 LYS A CG  1 
ATOM   1208 C CD  . LYS A 1 186 ? -5.65069  16.38944  13.20153 1.000 44.88331  ? 209 LYS A CD  1 
ATOM   1209 C CE  . LYS A 1 186 ? -4.30669  15.79775  13.57895 1.000 60.69585  ? 209 LYS A CE  1 
ATOM   1210 N NZ  . LYS A 1 186 ? -3.36168  15.68518  12.42781 1.000 62.96115  ? 209 LYS A NZ  1 
ATOM   1211 N N   . GLY A 1 187 ? -8.54953  19.73304  10.94717 1.000 39.42075  ? 210 GLY A N   1 
ATOM   1212 C CA  . GLY A 1 187 ? -9.78732  19.73009  10.18511 1.000 49.83478  ? 210 GLY A CA  1 
ATOM   1213 C C   . GLY A 1 187 ? -10.42302 21.10433  10.15273 1.000 47.58394  ? 210 GLY A C   1 
ATOM   1214 O O   . GLY A 1 187 ? -9.75304  22.12562  9.96065  1.000 51.27398  ? 210 GLY A O   1 
ATOM   1215 N N   . TYR A 1 188 ? -11.74679 21.13172  10.32555 1.000 67.58016  ? 211 TYR A N   1 
ATOM   1216 C CA  . TYR A 1 188 ? -12.49520 22.36638  10.11793 1.000 59.50792  ? 211 TYR A CA  1 
ATOM   1217 C C   . TYR A 1 188 ? -12.22802 23.36739  11.23565 1.000 46.58581  ? 211 TYR A C   1 
ATOM   1218 O O   . TYR A 1 188 ? -12.30127 24.58177  11.01329 1.000 53.55625  ? 211 TYR A O   1 
ATOM   1219 C CB  . TYR A 1 188 ? -13.98777 22.05484  9.99966  1.000 57.65968  ? 211 TYR A CB  1 
ATOM   1220 C CG  . TYR A 1 188 ? -14.32635 21.21938  8.78044  1.000 92.76948  ? 211 TYR A CG  1 
ATOM   1221 C CD1 . TYR A 1 188 ? -14.18812 19.83589  8.79951  1.000 98.03733  ? 211 TYR A CD1 1 
ATOM   1222 C CD2 . TYR A 1 188 ? -14.77273 21.81591  7.60625  1.000 109.39545 ? 211 TYR A CD2 1 
ATOM   1223 C CE1 . TYR A 1 188 ? -14.48309 19.07067  7.68392  1.000 118.43287 ? 211 TYR A CE1 1 
ATOM   1224 C CE2 . TYR A 1 188 ? -15.07741 21.05774  6.48745  1.000 108.07962 ? 211 TYR A CE2 1 
ATOM   1225 C CZ  . TYR A 1 188 ? -14.92871 19.68588  6.53188  1.000 125.77812 ? 211 TYR A CZ  1 
ATOM   1226 O OH  . TYR A 1 188 ? -15.23473 18.92408  5.42635  1.000 124.43990 ? 211 TYR A OH  1 
ATOM   1227 N N   . VAL A 1 189 ? -11.91480 22.87564  12.43606 1.000 36.62047  ? 212 VAL A N   1 
ATOM   1228 C CA  . VAL A 1 189 ? -11.57900 23.75751  13.54963 1.000 35.23939  ? 212 VAL A CA  1 
ATOM   1229 C C   . VAL A 1 189 ? -10.32773 24.56057  13.22116 1.000 45.45923  ? 212 VAL A C   1 
ATOM   1230 O O   . VAL A 1 189 ? -10.26437 25.77309  13.46259 1.000 45.96537  ? 212 VAL A O   1 
ATOM   1231 C CB  . VAL A 1 189 ? -11.41069 22.94142  14.84358 1.000 42.72092  ? 212 VAL A CB  1 
ATOM   1232 C CG1 . VAL A 1 189 ? -11.08765 23.85802  16.01155 1.000 48.59971  ? 212 VAL A CG1 1 
ATOM   1233 C CG2 . VAL A 1 189 ? -12.66829 22.13892  15.12020 1.000 55.14545  ? 212 VAL A CG2 1 
ATOM   1234 N N   . ARG A 1 190 ? -9.31209  23.89265  12.66751 1.000 47.42647  ? 213 ARG A N   1 
ATOM   1235 C CA  . ARG A 1 190 ? -8.11154  24.58887  12.21602 1.000 39.08156  ? 213 ARG A CA  1 
ATOM   1236 C C   . ARG A 1 190 ? -8.45833  25.66353  11.19237 1.000 45.95913  ? 213 ARG A C   1 
ATOM   1237 O O   . ARG A 1 190 ? -7.90980  26.77208  11.23577 1.000 50.02293  ? 213 ARG A O   1 
ATOM   1238 C CB  . ARG A 1 190 ? -7.11022  23.58266  11.65115 1.000 33.37902  ? 213 ARG A CB  1 
ATOM   1239 C CG  . ARG A 1 190 ? -5.96011  24.20116  10.89025 1.000 44.14341  ? 213 ARG A CG  1 
ATOM   1240 C CD  . ARG A 1 190 ? -5.00395  23.12396  10.42545 1.000 37.69578  ? 213 ARG A CD  1 
ATOM   1241 N NE  . ARG A 1 190 ? -4.25394  22.57110  11.54802 1.000 37.01881  ? 213 ARG A NE  1 
ATOM   1242 C CZ  . ARG A 1 190 ? -3.34990  21.60676  11.44523 1.000 37.46868  ? 213 ARG A CZ  1 
ATOM   1243 N NH1 . ARG A 1 190 ? -3.04572  21.06814  10.27596 1.000 50.34457  ? 213 ARG A NH1 1 
ATOM   1244 N NH2 . ARG A 1 190 ? -2.73472  21.17344  12.54283 1.000 39.95603  ? 213 ARG A NH2 1 
ATOM   1245 N N   . VAL A 1 191 ? -9.34905  25.34849  10.24897 1.000 48.02200  ? 214 VAL A N   1 
ATOM   1246 C CA  . VAL A 1 191 ? -9.59955  26.26114  9.13856  1.000 43.47497  ? 214 VAL A CA  1 
ATOM   1247 C C   . VAL A 1 191 ? -10.25085 27.53701  9.65507  1.000 37.89134  ? 214 VAL A C   1 
ATOM   1248 O O   . VAL A 1 191 ? -9.89165  28.64805  9.24482  1.000 43.86200  ? 214 VAL A O   1 
ATOM   1249 C CB  . VAL A 1 191 ? -10.46862 25.58266  8.06485  1.000 29.33138  ? 214 VAL A CB  1 
ATOM   1250 C CG1 . VAL A 1 191 ? -10.87309 26.59399  7.00679  1.000 46.45188  ? 214 VAL A CG1 1 
ATOM   1251 C CG2 . VAL A 1 191 ? -9.73454  24.40926  7.44537  1.000 29.33403  ? 214 VAL A CG2 1 
ATOM   1252 N N   . ILE A 1 192 ? -11.22497 27.39467  10.55667 1.000 40.42816  ? 215 ILE A N   1 
ATOM   1253 C CA  . ILE A 1 192 ? -11.94884 28.55168  11.07795 1.000 44.08058  ? 215 ILE A CA  1 
ATOM   1254 C C   . ILE A 1 192 ? -10.99787 29.48389  11.81760 1.000 34.23547  ? 215 ILE A C   1 
ATOM   1255 O O   . ILE A 1 192 ? -10.94568 30.68963  11.54656 1.000 39.16904  ? 215 ILE A O   1 
ATOM   1256 C CB  . ILE A 1 192 ? -13.10066 28.09513  11.98800 1.000 30.56994  ? 215 ILE A CB  1 
ATOM   1257 C CG1 . ILE A 1 192 ? -14.13052 27.30792  11.17596 1.000 41.07028  ? 215 ILE A CG1 1 
ATOM   1258 C CG2 . ILE A 1 192 ? -13.74739 29.30564  12.63718 1.000 17.67162  ? 215 ILE A CG2 1 
ATOM   1259 C CD1 . ILE A 1 192 ? -15.16960 26.60547  12.01841 1.000 45.24277  ? 215 ILE A CD1 1 
ATOM   1260 N N   . PHE A 1 193 ? -10.22579 28.93610  12.76108 1.000 36.92237  ? 216 PHE A N   1 
ATOM   1261 C CA  . PHE A 1 193 ? -9.33080  29.77129  13.55677 1.000 36.48304  ? 216 PHE A CA  1 
ATOM   1262 C C   . PHE A 1 193 ? -8.27665  30.42924  12.68157 1.000 32.52243  ? 216 PHE A C   1 
ATOM   1263 O O   . PHE A 1 193 ? -7.89727  31.58269  12.91497 1.000 40.60495  ? 216 PHE A O   1 
ATOM   1264 C CB  . PHE A 1 193 ? -8.68757  28.95314  14.67411 1.000 31.03964  ? 216 PHE A CB  1 
ATOM   1265 C CG  . PHE A 1 193 ? -9.61643  28.67025  15.81867 1.000 25.92014  ? 216 PHE A CG  1 
ATOM   1266 C CD1 . PHE A 1 193 ? -10.07693 29.70590  16.61647 1.000 31.23423  ? 216 PHE A CD1 1 
ATOM   1267 C CD2 . PHE A 1 193 ? -10.01352 27.37961  16.11070 1.000 30.57124  ? 216 PHE A CD2 1 
ATOM   1268 C CE1 . PHE A 1 193 ? -10.92594 29.45926  17.67536 1.000 43.43146  ? 216 PHE A CE1 1 
ATOM   1269 C CE2 . PHE A 1 193 ? -10.86220 27.12535  17.17037 1.000 30.00170  ? 216 PHE A CE2 1 
ATOM   1270 C CZ  . PHE A 1 193 ? -11.31929 28.16528  17.95254 1.000 48.36749  ? 216 PHE A CZ  1 
ATOM   1271 N N   . PHE A 1 194 ? -7.80165  29.71657  11.66182 1.000 30.99918  ? 217 PHE A N   1 
ATOM   1272 C CA  . PHE A 1 194 ? -6.89670  30.32714  10.69626 1.000 42.64026  ? 217 PHE A CA  1 
ATOM   1273 C C   . PHE A 1 194 ? -7.54640  31.53501  10.02994 1.000 44.56378  ? 217 PHE A C   1 
ATOM   1274 O O   . PHE A 1 194 ? -6.92102  32.59411  9.89810  1.000 60.75752  ? 217 PHE A O   1 
ATOM   1275 C CB  . PHE A 1 194 ? -6.46021  29.30861  9.64480  1.000 44.36529  ? 217 PHE A CB  1 
ATOM   1276 C CG  . PHE A 1 194 ? -5.50856  29.87325  8.62609  1.000 46.96608  ? 217 PHE A CG  1 
ATOM   1277 C CD1 . PHE A 1 194 ? -4.15011  29.93941  8.89093  1.000 46.00340  ? 217 PHE A CD1 1 
ATOM   1278 C CD2 . PHE A 1 194 ? -5.97407  30.35728  7.41227  1.000 50.50061  ? 217 PHE A CD2 1 
ATOM   1279 C CE1 . PHE A 1 194 ? -3.27166  30.46627  7.96139  1.000 45.31735  ? 217 PHE A CE1 1 
ATOM   1280 C CE2 . PHE A 1 194 ? -5.09995  30.88714  6.47928  1.000 58.23931  ? 217 PHE A CE2 1 
ATOM   1281 C CZ  . PHE A 1 194 ? -3.74640  30.94032  6.75519  1.000 53.48711  ? 217 PHE A CZ  1 
ATOM   1282 N N   . LEU A 1 195 ? -8.80638  31.39758  9.60369  1.000 37.69713  ? 218 LEU A N   1 
ATOM   1283 C CA  . LEU A 1 195 ? -9.46117  32.50103  8.90760  1.000 44.17468  ? 218 LEU A CA  1 
ATOM   1284 C C   . LEU A 1 195 ? -9.66145  33.70364  9.82430  1.000 45.19442  ? 218 LEU A C   1 
ATOM   1285 O O   . LEU A 1 195 ? -9.48874  34.84973  9.38845  1.000 47.34288  ? 218 LEU A O   1 
ATOM   1286 C CB  . LEU A 1 195 ? -10.79320 32.02988  8.32937  1.000 52.38717  ? 218 LEU A CB  1 
ATOM   1287 C CG  . LEU A 1 195 ? -10.64894 31.06654  7.15106  1.000 50.90780  ? 218 LEU A CG  1 
ATOM   1288 C CD1 . LEU A 1 195 ? -12.01188 30.56850  6.69364  1.000 63.03708  ? 218 LEU A CD1 1 
ATOM   1289 C CD2 . LEU A 1 195 ? -9.88652  31.72604  6.00978  1.000 42.90384  ? 218 LEU A CD2 1 
ATOM   1290 N N   . MET A 1 196 ? -10.02909 33.48024  11.09058 1.000 27.29021  ? 219 MET A N   1 
ATOM   1291 C CA  . MET A 1 196 ? -10.09815 34.61416  12.01263 1.000 44.09288  ? 219 MET A CA  1 
ATOM   1292 C C   . MET A 1 196 ? -8.73245  35.26492  12.15049 1.000 41.01919  ? 219 MET A C   1 
ATOM   1293 O O   . MET A 1 196 ? -8.62577  36.49507  12.23526 1.000 40.10357  ? 219 MET A O   1 
ATOM   1294 C CB  . MET A 1 196 ? -10.67750 34.24456  13.36835 1.000 34.28308  ? 219 MET A CB  1 
ATOM   1295 C CG  . MET A 1 196 ? -11.63032 33.09752  13.37288 1.000 44.42123  ? 219 MET A CG  1 
ATOM   1296 S SD  . MET A 1 196 ? -12.07957 32.87161  15.09302 1.000 57.37478  ? 219 MET A SD  1 
ATOM   1297 C CE  . MET A 1 196 ? -12.95388 34.42169  15.37763 1.000 35.84126  ? 219 MET A CE  1 
ATOM   1298 N N   . GLY A 1 197 ? -7.67814  34.44761  12.19299 1.000 33.07200  ? 220 GLY A N   1 
ATOM   1299 C CA  . GLY A 1 197 ? -6.33828  35.00148  12.19492 1.000 26.19997  ? 220 GLY A CA  1 
ATOM   1300 C C   . GLY A 1 197 ? -6.13097  35.84740  10.95635 1.000 38.53390  ? 220 GLY A C   1 
ATOM   1301 O O   . GLY A 1 197 ? -5.53694  36.92724  11.02139 1.000 41.24255  ? 220 GLY A O   1 
ATOM   1302 N N   . LEU A 1 198 ? -6.60658  35.35861  9.80732  1.000 38.69792  ? 221 LEU A N   1 
ATOM   1303 C CA  . LEU A 1 198 ? -6.45402  36.10679  8.56716  1.000 33.62861  ? 221 LEU A CA  1 
ATOM   1304 C C   . LEU A 1 198 ? -7.20380  37.43094  8.65916  1.000 33.10135  ? 221 LEU A C   1 
ATOM   1305 O O   . LEU A 1 198 ? -6.70257  38.47046  8.21271  1.000 31.62602  ? 221 LEU A O   1 
ATOM   1306 C CB  . LEU A 1 198 ? -6.97156  35.28401  7.38820  1.000 36.66167  ? 221 LEU A CB  1 
ATOM   1307 C CG  . LEU A 1 198 ? -6.31124  35.51279  6.02927  1.000 43.05589  ? 221 LEU A CG  1 
ATOM   1308 C CD1 . LEU A 1 198 ? -4.86337  35.06131  6.03880  1.000 46.44526  ? 221 LEU A CD1 1 
ATOM   1309 C CD2 . LEU A 1 198 ? -7.10060  34.80133  4.93826  1.000 73.25959  ? 221 LEU A CD2 1 
ATOM   1310 N N   . CYS A 1 199 ? -8.41244  37.41516  9.23745  1.000 26.07274  ? 222 CYS A N   1 
ATOM   1311 C CA  . CYS A 1 199 ? -9.15432  38.66483  9.38850  1.000 33.66952  ? 222 CYS A CA  1 
ATOM   1312 C C   . CYS A 1 199 ? -8.42960  39.60362  10.33964 1.000 35.19262  ? 222 CYS A C   1 
ATOM   1313 O O   . CYS A 1 199 ? -8.29314  40.80033  10.05575 1.000 41.01418  ? 222 CYS A O   1 
ATOM   1314 C CB  . CYS A 1 199 ? -10.57576 38.39994  9.88198  1.000 39.20445  ? 222 CYS A CB  1 
ATOM   1315 S SG  . CYS A 1 199 ? -11.61986 37.41820  8.77937  1.000 43.20579  ? 222 CYS A SG  1 
ATOM   1316 N N   . TYR A 1 200 ? -7.94560  39.07730  11.46684 1.000 27.61897  ? 223 TYR A N   1 
ATOM   1317 C CA  . TYR A 1 200 ? -7.18880  39.91466  12.38524 1.000 32.50860  ? 223 TYR A CA  1 
ATOM   1318 C C   . TYR A 1 200 ? -5.93693  40.41802  11.68439 1.000 35.73648  ? 223 TYR A C   1 
ATOM   1319 O O   . TYR A 1 200 ? -5.54738  41.58366  11.83645 1.000 40.44553  ? 223 TYR A O   1 
ATOM   1320 C CB  . TYR A 1 200 ? -6.81972  39.13361  13.65082 1.000 27.70226  ? 223 TYR A CB  1 
ATOM   1321 C CG  . TYR A 1 200 ? -7.82526  39.20385  14.78300 1.000 34.07692  ? 223 TYR A CG  1 
ATOM   1322 C CD1 . TYR A 1 200 ? -9.08278  38.61639  14.66964 1.000 31.90298  ? 223 TYR A CD1 1 
ATOM   1323 C CD2 . TYR A 1 200 ? -7.50670  39.84811  15.97209 1.000 24.79841  ? 223 TYR A CD2 1 
ATOM   1324 C CE1 . TYR A 1 200 ? -9.99378  38.67447  15.71273 1.000 27.47439  ? 223 TYR A CE1 1 
ATOM   1325 C CE2 . TYR A 1 200 ? -8.40468  39.91232  17.01516 1.000 25.75113  ? 223 TYR A CE2 1 
ATOM   1326 C CZ  . TYR A 1 200 ? -9.64527  39.32762  16.88394 1.000 33.16069  ? 223 TYR A CZ  1 
ATOM   1327 O OH  . TYR A 1 200 ? -10.52779 39.39881  17.93758 1.000 40.52363  ? 223 TYR A OH  1 
ATOM   1328 N N   . GLY A 1 201 ? -5.28149  39.52677  10.93089 1.000 38.95539  ? 224 GLY A N   1 
ATOM   1329 C CA  . GLY A 1 201 ? -4.03300  39.87796  10.27883 1.000 31.74946  ? 224 GLY A CA  1 
ATOM   1330 C C   . GLY A 1 201 ? -4.18413  40.98407  9.26138  1.000 39.33067  ? 224 GLY A C   1 
ATOM   1331 O O   . GLY A 1 201 ? -3.39720  41.93314  9.24174  1.000 38.28500  ? 224 GLY A O   1 
ATOM   1332 N N   . ILE A 1 202 ? -5.21901  40.89704  8.43098  1.000 45.69279  ? 225 ILE A N   1 
ATOM   1333 C CA  . ILE A 1 202 ? -5.45861  41.94866  7.45653  1.000 48.99618  ? 225 ILE A CA  1 
ATOM   1334 C C   . ILE A 1 202 ? -5.62258  43.27853  8.16711  1.000 45.84809  ? 225 ILE A C   1 
ATOM   1335 O O   . ILE A 1 202 ? -5.05974  44.29655  7.74609  1.000 58.26015  ? 225 ILE A O   1 
ATOM   1336 C CB  . ILE A 1 202 ? -6.69036  41.62712  6.59650  1.000 46.91054  ? 225 ILE A CB  1 
ATOM   1337 C CG1 . ILE A 1 202 ? -6.40701  40.47724  5.60777  1.000 46.26896  ? 225 ILE A CG1 1 
ATOM   1338 C CG2 . ILE A 1 202 ? -7.11076  42.90073  5.78937  1.000 51.46198  ? 225 ILE A CG2 1 
ATOM   1339 C CD1 . ILE A 1 202 ? -7.65137  39.70519  5.22627  1.000 32.54520  ? 225 ILE A CD1 1 
ATOM   1340 N N   . TYR A 1 203 ? -6.40961  43.29173  9.24654  1.000 30.99838  ? 226 TYR A N   1 
ATOM   1341 C CA  . TYR A 1 203 ? -6.56774  44.51610  10.01976 1.000 32.33190  ? 226 TYR A CA  1 
ATOM   1342 C C   . TYR A 1 203 ? -5.21570  45.01218  10.51101 1.000 35.23946  ? 226 TYR A C   1 
ATOM   1343 O O   . TYR A 1 203 ? -4.96422  46.22132  10.52238 1.000 38.31475  ? 226 TYR A O   1 
ATOM   1344 C CB  . TYR A 1 203 ? -7.52587  44.28207  11.19330 1.000 40.66306  ? 226 TYR A CB  1 
ATOM   1345 C CG  . TYR A 1 203 ? -7.82836  45.51845  12.03085 1.000 38.87806  ? 226 TYR A CG  1 
ATOM   1346 C CD1 . TYR A 1 203 ? -6.94239  45.95869  13.01379 1.000 50.15853  ? 226 TYR A CD1 1 
ATOM   1347 C CD2 . TYR A 1 203 ? -9.00030  46.23632  11.84380 1.000 36.26583  ? 226 TYR A CD2 1 
ATOM   1348 C CE1 . TYR A 1 203 ? -7.21607  47.08279  13.76956 1.000 53.35623  ? 226 TYR A CE1 1 
ATOM   1349 C CE2 . TYR A 1 203 ? -9.28411  47.35304  12.60008 1.000 43.57255  ? 226 TYR A CE2 1 
ATOM   1350 C CZ  . TYR A 1 203 ? -8.38870  47.77518  13.55672 1.000 50.10050  ? 226 TYR A CZ  1 
ATOM   1351 O OH  . TYR A 1 203 ? -8.67087  48.88257  14.32160 1.000 62.31435  ? 226 TYR A OH  1 
ATOM   1352 N N   . THR A 1 204 ? -4.33091  44.09705  10.92116 1.000 42.21065  ? 227 THR A N   1 
ATOM   1353 C CA  . THR A 1 204 ? -2.99705  44.50596  11.35999 1.000 27.31607  ? 227 THR A CA  1 
ATOM   1354 C C   . THR A 1 204 ? -2.23147  45.11197  10.18696 1.000 38.23496  ? 227 THR A C   1 
ATOM   1355 O O   . THR A 1 204 ? -1.64290  46.19607  10.30161 1.000 37.07631  ? 227 THR A O   1 
ATOM   1356 C CB  . THR A 1 204 ? -2.23801  43.32011  11.95615 1.000 27.18975  ? 227 THR A CB  1 
ATOM   1357 O OG1 . THR A 1 204 ? -3.03767  42.71103  12.97947 1.000 35.11869  ? 227 THR A OG1 1 
ATOM   1358 C CG2 . THR A 1 204 ? -0.92750  43.78805  12.56522 1.000 22.63043  ? 227 THR A CG2 1 
ATOM   1359 N N   . PHE A 1 205 ? -2.21064  44.40160  9.05044  1.000 47.16608  ? 228 PHE A N   1 
ATOM   1360 C CA  . PHE A 1 205 ? -1.42936  44.84114  7.89629  1.000 41.16685  ? 228 PHE A CA  1 
ATOM   1361 C C   . PHE A 1 205 ? -1.93274  46.20012  7.42970  1.000 41.41900  ? 228 PHE A C   1 
ATOM   1362 O O   . PHE A 1 205 ? -1.14034  47.08915  7.09420  1.000 45.48355  ? 228 PHE A O   1 
ATOM   1363 C CB  . PHE A 1 205 ? -1.49228  43.80278  6.77591  1.000 33.09999  ? 228 PHE A CB  1 
ATOM   1364 C CG  . PHE A 1 205 ? -0.54168  42.64973  6.96789  1.000 45.95334  ? 228 PHE A CG  1 
ATOM   1365 C CD1 . PHE A 1 205 ? 0.66183   42.60342  6.28442  1.000 47.11617  ? 228 PHE A CD1 1 
ATOM   1366 C CD2 . PHE A 1 205 ? -0.84861  41.61610  7.83777  1.000 72.87115  ? 228 PHE A CD2 1 
ATOM   1367 C CE1 . PHE A 1 205 ? 1.53921   41.54192  6.46577  1.000 78.16825  ? 228 PHE A CE1 1 
ATOM   1368 C CE2 . PHE A 1 205 ? 0.02048   40.55565  8.02596  1.000 69.41364  ? 228 PHE A CE2 1 
ATOM   1369 C CZ  . PHE A 1 205 ? 1.21581   40.51659  7.33749  1.000 74.77201  ? 228 PHE A CZ  1 
ATOM   1370 N N   . PHE A 1 206 ? -3.25677  46.36754  7.39482  1.000 38.03518  ? 229 PHE A N   1 
ATOM   1371 C CA  . PHE A 1 206 ? -3.85725  47.60282  6.90470  1.000 46.58382  ? 229 PHE A CA  1 
ATOM   1372 C C   . PHE A 1 206 ? -3.38160  48.77154  7.75333  1.000 47.36591  ? 229 PHE A C   1 
ATOM   1373 O O   . PHE A 1 206 ? -2.95123  49.80590  7.22960  1.000 51.72917  ? 229 PHE A O   1 
ATOM   1374 C CB  . PHE A 1 206 ? -5.38318  47.49724  6.93175  1.000 70.91013  ? 229 PHE A CB  1 
ATOM   1375 C CG  . PHE A 1 206 ? -6.08368  48.72229  6.41836  1.000 78.95530  ? 229 PHE A CG  1 
ATOM   1376 C CD1 . PHE A 1 206 ? -6.09795  49.01878  5.06546  1.000 87.28248  ? 229 PHE A CD1 1 
ATOM   1377 C CD2 . PHE A 1 206 ? -6.72173  49.58519  7.29684  1.000 76.25858  ? 229 PHE A CD2 1 
ATOM   1378 C CE1 . PHE A 1 206 ? -6.73914  50.15242  4.59801  1.000 85.72367  ? 229 PHE A CE1 1 
ATOM   1379 C CE2 . PHE A 1 206 ? -7.36358  50.71866  6.83594  1.000 79.04731  ? 229 PHE A CE2 1 
ATOM   1380 C CZ  . PHE A 1 206 ? -7.37219  51.00292  5.48515  1.000 84.45639  ? 229 PHE A CZ  1 
ATOM   1381 N N   . ASN A 1 207 ? -3.45008  48.61754  9.07694  1.000 56.09902  ? 230 ASN A N   1 
ATOM   1382 C CA  . ASN A 1 207 ? -3.10402  49.71298  9.97238  1.000 37.21546  ? 230 ASN A CA  1 
ATOM   1383 C C   . ASN A 1 207 ? -1.59779  49.93641  9.97434  1.000 26.01242  ? 230 ASN A C   1 
ATOM   1384 O O   . ASN A 1 207 ? -1.14223  51.07941  10.07940 1.000 31.53017  ? 230 ASN A O   1 
ATOM   1385 C CB  . ASN A 1 207 ? -3.62267  49.42703  11.37980 1.000 39.95478  ? 230 ASN A CB  1 
ATOM   1386 C CG  . ASN A 1 207 ? -5.11304  49.66600  11.50543 1.000 51.14460  ? 230 ASN A CG  1 
ATOM   1387 O OD1 . ASN A 1 207 ? -5.56067  50.80684  11.63806 1.000 61.17480  ? 230 ASN A OD1 1 
ATOM   1388 N ND2 . ASN A 1 207 ? -5.89318  48.59505  11.42814 1.000 49.93805  ? 230 ASN A ND2 1 
ATOM   1389 N N   . ALA A 1 208 ? -0.80698  48.85788  9.87491  1.000 36.76134  ? 231 ALA A N   1 
ATOM   1390 C CA  . ALA A 1 208 ? 0.63701   49.02531  9.71723  1.000 34.79298  ? 231 ALA A CA  1 
ATOM   1391 C C   . ALA A 1 208 ? 0.92253   49.88952  8.49609  1.000 42.30244  ? 231 ALA A C   1 
ATOM   1392 O O   . ALA A 1 208 ? 1.83377   50.72678  8.50995  1.000 39.69479  ? 231 ALA A O   1 
ATOM   1393 C CB  . ALA A 1 208 ? 1.32194   47.66574  9.59490  1.000 38.34789  ? 231 ALA A CB  1 
ATOM   1394 N N   . ALA A 1 209 ? 0.15236   49.68111  7.42328  1.000 50.42105  ? 232 ALA A N   1 
ATOM   1395 C CA  . ALA A 1 209 ? 0.35249   50.41432  6.17842  1.000 41.08951  ? 232 ALA A CA  1 
ATOM   1396 C C   . ALA A 1 209 ? 0.09118   51.89024  6.42494  1.000 41.43270  ? 232 ALA A C   1 
ATOM   1397 O O   . ALA A 1 209 ? 0.83148   52.76079  5.95096  1.000 46.65153  ? 232 ALA A O   1 
ATOM   1398 C CB  . ALA A 1 209 ? -0.55594  49.86660  5.07955  1.000 41.24910  ? 232 ALA A CB  1 
ATOM   1399 N N   . LYS A 1 210 ? -0.97415  52.17217  7.17846  1.000 49.45524  ? 233 LYS A N   1 
ATOM   1400 C CA  . LYS A 1 210 ? -1.33209  53.53087  7.56588  1.000 36.75910  ? 233 LYS A CA  1 
ATOM   1401 C C   . LYS A 1 210 ? -0.16991  54.19447  8.29752  1.000 50.16199  ? 233 LYS A C   1 
ATOM   1402 O O   . LYS A 1 210 ? 0.14980   55.36300  8.04882  1.000 58.38597  ? 233 LYS A O   1 
ATOM   1403 C CB  . LYS A 1 210 ? -2.55494  53.43072  8.47825  1.000 43.64509  ? 233 LYS A CB  1 
ATOM   1404 C CG  . LYS A 1 210 ? -3.84064  54.11924  8.09345  1.000 56.52734  ? 233 LYS A CG  1 
ATOM   1405 C CD  . LYS A 1 210 ? -4.62376  54.35245  9.38812  1.000 85.47401  ? 233 LYS A CD  1 
ATOM   1406 C CE  . LYS A 1 210 ? -5.50805  55.57850  9.37416  1.000 91.28886  ? 233 LYS A CE  1 
ATOM   1407 N NZ  . LYS A 1 210 ? -6.36224  55.59730  10.60170 1.000 83.81777  ? 233 LYS A NZ  1 
ATOM   1408 N N   . VAL A 1 211 ? 0.45135   53.46871  9.23352  1.000 54.26721  ? 234 VAL A N   1 
ATOM   1409 C CA  . VAL A 1 211 ? 1.54676   54.02489  10.02895 1.000 40.47843  ? 234 VAL A CA  1 
ATOM   1410 C C   . VAL A 1 211 ? 2.71131   54.41339  9.12341  1.000 37.23720  ? 234 VAL A C   1 
ATOM   1411 O O   . VAL A 1 211 ? 3.29100   55.49814  9.25079  1.000 43.36810  ? 234 VAL A O   1 
ATOM   1412 C CB  . VAL A 1 211 ? 1.98612   53.03148  11.11907 1.000 32.42531  ? 234 VAL A CB  1 
ATOM   1413 C CG1 . VAL A 1 211 ? 3.16061   53.59547  11.90124 1.000 43.32742  ? 234 VAL A CG1 1 
ATOM   1414 C CG2 . VAL A 1 211 ? 0.83069   52.72848  12.05453 1.000 33.93586  ? 234 VAL A CG2 1 
ATOM   1415 N N   . TYR A 1 212 ? 3.09553   53.50497  8.22107  1.000 37.62541  ? 235 TYR A N   1 
ATOM   1416 C CA  . TYR A 1 212 ? 4.22532   53.75132  7.32808  1.000 39.66490  ? 235 TYR A CA  1 
ATOM   1417 C C   . TYR A 1 212 ? 3.97137   54.93950  6.40875  1.000 52.29146  ? 235 TYR A C   1 
ATOM   1418 O O   . TYR A 1 212 ? 4.89957   55.69353  6.09012  1.000 50.27726  ? 235 TYR A O   1 
ATOM   1419 C CB  . TYR A 1 212 ? 4.51827   52.50700  6.49169  1.000 42.25360  ? 235 TYR A CB  1 
ATOM   1420 C CG  . TYR A 1 212 ? 5.34662   51.44764  7.17656  1.000 35.06755  ? 235 TYR A CG  1 
ATOM   1421 C CD1 . TYR A 1 212 ? 6.71213   51.62345  7.36496  1.000 41.56317  ? 235 TYR A CD1 1 
ATOM   1422 C CD2 . TYR A 1 212 ? 4.77089   50.26145  7.61305  1.000 36.56624  ? 235 TYR A CD2 1 
ATOM   1423 C CE1 . TYR A 1 212 ? 7.47953   50.65238  7.98498  1.000 42.08691  ? 235 TYR A CE1 1 
ATOM   1424 C CE2 . TYR A 1 212 ? 5.52930   49.28255  8.22847  1.000 33.21428  ? 235 TYR A CE2 1 
ATOM   1425 C CZ  . TYR A 1 212 ? 6.88244   49.48390  8.41271  1.000 28.91479  ? 235 TYR A CZ  1 
ATOM   1426 O OH  . TYR A 1 212 ? 7.64024   48.51052  9.02180  1.000 28.56687  ? 235 TYR A OH  1 
ATOM   1427 N N   . ILE A 1 213 ? 2.72552   55.11366  5.95716  1.000 45.75234  ? 236 ILE A N   1 
ATOM   1428 C CA  . ILE A 1 213 ? 2.38880   56.27400  5.13282  1.000 59.53534  ? 236 ILE A CA  1 
ATOM   1429 C C   . ILE A 1 213 ? 2.59945   57.56459  5.91823  1.000 65.56776  ? 236 ILE A C   1 
ATOM   1430 O O   . ILE A 1 213 ? 3.24014   58.50653  5.43430  1.000 66.84968  ? 236 ILE A O   1 
ATOM   1431 C CB  . ILE A 1 213 ? 0.94743   56.15872  4.60271  1.000 42.84968  ? 236 ILE A CB  1 
ATOM   1432 C CG1 . ILE A 1 213 ? 0.88793   55.18417  3.42511  1.000 48.09756  ? 236 ILE A CG1 1 
ATOM   1433 C CG2 . ILE A 1 213 ? 0.41988   57.52018  4.17832  1.000 42.83058  ? 236 ILE A CG2 1 
ATOM   1434 C CD1 . ILE A 1 213 ? -0.49582  54.61285  3.17421  1.000 51.76222  ? 236 ILE A CD1 1 
ATOM   1435 N N   . GLU A 1 214 ? 2.07346   57.62433  7.14666  1.000 47.23841  ? 237 GLU A N   1 
ATOM   1436 C CA  . GLU A 1 214 ? 2.34120   58.77577  8.00500  1.000 47.90099  ? 237 GLU A CA  1 
ATOM   1437 C C   . GLU A 1 214 ? 3.83633   58.94471  8.24444  1.000 52.79533  ? 237 GLU A C   1 
ATOM   1438 O O   . GLU A 1 214 ? 4.35279   60.06805  8.20269  1.000 68.82714  ? 237 GLU A O   1 
ATOM   1439 C CB  . GLU A 1 214 ? 1.58159   58.65096  9.32461  1.000 64.58305  ? 237 GLU A CB  1 
ATOM   1440 C CG  . GLU A 1 214 ? 0.07125   58.61915  9.14901  1.000 77.45355  ? 237 GLU A CG  1 
ATOM   1441 C CD  . GLU A 1 214 ? -0.67436  58.68669  10.46636 1.000 90.92832  ? 237 GLU A CD  1 
ATOM   1442 O OE1 . GLU A 1 214 ? -0.02725  58.92011  11.51115 1.000 66.03817  ? 237 GLU A OE1 1 
ATOM   1443 O OE2 . GLU A 1 214 ? -1.91152  58.50870  10.45519 1.000 106.66924 ? 237 GLU A OE2 1 
ATOM   1444 N N   . ALA A 1 215 ? 4.54653   57.84318  8.51076  1.000 57.28673  ? 238 ALA A N   1 
ATOM   1445 C CA  . ALA A 1 215 ? 5.96301   57.94360  8.85069  1.000 52.88382  ? 238 ALA A CA  1 
ATOM   1446 C C   . ALA A 1 215 ? 6.74169   58.53220  7.68350  1.000 43.10158  ? 238 ALA A C   1 
ATOM   1447 O O   . ALA A 1 215 ? 7.62983   59.37234  7.87498  1.000 39.46811  ? 238 ALA A O   1 
ATOM   1448 C CB  . ALA A 1 215 ? 6.51799   56.57195  9.23463  1.000 40.77443  ? 238 ALA A CB  1 
ATOM   1449 N N   . TYR A 1 216 ? 6.42295   58.08625  6.46554  1.000 56.31711  ? 239 TYR A N   1 
ATOM   1450 C CA  . TYR A 1 216 ? 7.15398   58.51274  5.27702  1.000 65.98357  ? 239 TYR A CA  1 
ATOM   1451 C C   . TYR A 1 216 ? 7.07842   60.02971  5.13427  1.000 58.91183  ? 239 TYR A C   1 
ATOM   1452 O O   . TYR A 1 216 ? 8.08796   60.69636  4.88095  1.000 62.86664  ? 239 TYR A O   1 
ATOM   1453 C CB  . TYR A 1 216 ? 6.60411   57.79786  4.03882  1.000 56.53943  ? 239 TYR A CB  1 
ATOM   1454 C CG  . TYR A 1 216 ? 7.28799   58.15873  2.73471  1.000 47.78179  ? 239 TYR A CG  1 
ATOM   1455 C CD1 . TYR A 1 216 ? 8.41952   57.47068  2.31233  1.000 47.83884  ? 239 TYR A CD1 1 
ATOM   1456 C CD2 . TYR A 1 216 ? 6.79184   59.16430  1.91553  1.000 50.05151  ? 239 TYR A CD2 1 
ATOM   1457 C CE1 . TYR A 1 216 ? 9.05274   57.79320  1.12264  1.000 73.69001  ? 239 TYR A CE1 1 
ATOM   1458 C CE2 . TYR A 1 216 ? 7.41146   59.48901  0.72058  1.000 62.32161  ? 239 TYR A CE2 1 
ATOM   1459 C CZ  . TYR A 1 216 ? 8.54268   58.80139  0.32856  1.000 78.37503  ? 239 TYR A CZ  1 
ATOM   1460 O OH  . TYR A 1 216 ? 9.15841   59.11660  -0.86395 1.000 55.67267  ? 239 TYR A OH  1 
ATOM   1461 N N   . HIS A 1 217 ? 5.88159   60.59184  5.31074  1.000 51.25698  ? 240 HIS A N   1 
ATOM   1462 C CA  . HIS A 1 217 ? 5.64010   62.02376  5.17852  1.000 52.77273  ? 240 HIS A CA  1 
ATOM   1463 C C   . HIS A 1 217 ? 6.02792   62.80398  6.42942  1.000 51.18312  ? 240 HIS A C   1 
ATOM   1464 O O   . HIS A 1 217 ? 5.91297   64.03480  6.43489  1.000 47.68436  ? 240 HIS A O   1 
ATOM   1465 C CB  . HIS A 1 217 ? 4.16614   62.29251  4.85081  1.000 55.53121  ? 240 HIS A CB  1 
ATOM   1466 C CG  . HIS A 1 217 ? 3.72672   61.74944  3.52604  1.000 54.52834  ? 240 HIS A CG  1 
ATOM   1467 N ND1 . HIS A 1 217 ? 4.60892   61.23739  2.59913  1.000 65.20194  ? 240 HIS A ND1 1 
ATOM   1468 C CD2 . HIS A 1 217 ? 2.49639   61.64768  2.96930  1.000 58.40057  ? 240 HIS A CD2 1 
ATOM   1469 C CE1 . HIS A 1 217 ? 3.94133   60.83917  1.53053  1.000 74.26203  ? 240 HIS A CE1 1 
ATOM   1470 N NE2 . HIS A 1 217 ? 2.65736   61.07668  1.72978  1.000 86.36534  ? 240 HIS A NE2 1 
ATOM   1471 N N   . THR A 1 218 ? 6.45436   62.12196  7.49113  1.000 54.25939  ? 241 THR A N   1 
ATOM   1472 C CA  . THR A 1 218 ? 6.88452   62.77269  8.72403  1.000 57.08799  ? 241 THR A CA  1 
ATOM   1473 C C   . THR A 1 218 ? 8.38816   63.03281  8.73777  1.000 60.74244  ? 241 THR A C   1 
ATOM   1474 O O   . THR A 1 218 ? 8.82980   64.10281  9.17176  1.000 60.03606  ? 241 THR A O   1 
ATOM   1475 C CB  . THR A 1 218 ? 6.49239   61.92854  9.93801  1.000 48.05062  ? 241 THR A CB  1 
ATOM   1476 O OG1 . THR A 1 218 ? 5.06425   61.84708  10.02073 1.000 47.72175  ? 241 THR A OG1 1 
ATOM   1477 C CG2 . THR A 1 218 ? 7.03535   62.55144  11.21542 1.000 59.67479  ? 241 THR A CG2 1 
ATOM   1478 N N   . VAL A 1 219 ? 9.17998   62.06945  8.27736  1.000 59.38341  ? 242 VAL A N   1 
ATOM   1479 C CA  . VAL A 1 219 ? 10.63763  62.10447  8.37734  1.000 58.14369  ? 242 VAL A CA  1 
ATOM   1480 C C   . VAL A 1 219 ? 11.19499  63.05713  7.32257  1.000 57.34986  ? 242 VAL A C   1 
ATOM   1481 O O   . VAL A 1 219 ? 10.50859  63.34781  6.33198  1.000 64.59766  ? 242 VAL A O   1 
ATOM   1482 C CB  . VAL A 1 219 ? 11.22844  60.69212  8.22395  1.000 59.53821  ? 242 VAL A CB  1 
ATOM   1483 C CG1 . VAL A 1 219 ? 10.67262  59.76402  9.29951  1.000 39.20791  ? 242 VAL A CG1 1 
ATOM   1484 C CG2 . VAL A 1 219 ? 10.94984  60.14238  6.83061  1.000 51.44566  ? 242 VAL A CG2 1 
ATOM   1485 N N   . PRO A 1 220 ? 12.41601  63.60156  7.51231  1.000 55.50840  ? 243 PRO A N   1 
ATOM   1486 C CA  . PRO A 1 220 ? 13.02221  64.47911  6.49317  1.000 62.52021  ? 243 PRO A CA  1 
ATOM   1487 C C   . PRO A 1 220 ? 13.06553  63.89815  5.08479  1.000 61.07265  ? 243 PRO A C   1 
ATOM   1488 O O   . PRO A 1 220 ? 12.98153  62.68125  4.88984  1.000 67.28943  ? 243 PRO A O   1 
ATOM   1489 C CB  . PRO A 1 220 ? 14.44059  64.72153  7.02894  1.000 75.19576  ? 243 PRO A CB  1 
ATOM   1490 C CG  . PRO A 1 220 ? 14.37805  64.43051  8.47698  1.000 56.42906  ? 243 PRO A CG  1 
ATOM   1491 C CD  . PRO A 1 220 ? 13.26435  63.45646  8.70794  1.000 65.92057  ? 243 PRO A CD  1 
ATOM   1492 N N   . LYS A 1 221 ? 13.21347  64.78704  4.09587  1.000 68.20882  ? 244 LYS A N   1 
ATOM   1493 C CA  . LYS A 1 221 ? 12.97092  64.45154  2.69521  1.000 68.21227  ? 244 LYS A CA  1 
ATOM   1494 C C   . LYS A 1 221 ? 13.99478  63.48682  2.11245  1.000 67.61791  ? 244 LYS A C   1 
ATOM   1495 O O   . LYS A 1 221 ? 13.69709  62.82150  1.11423  1.000 75.92003  ? 244 LYS A O   1 
ATOM   1496 C CB  . LYS A 1 221 ? 12.93702  65.72701  1.85168  1.000 34.50683  ? 244 LYS A CB  1 
ATOM   1497 N N   . GLY A 1 222 ? 15.18090  63.38705  2.69894  1.000 58.11053  ? 245 GLY A N   1 
ATOM   1498 C CA  . GLY A 1 222 ? 16.23951  62.64135  2.05157  1.000 68.90777  ? 245 GLY A CA  1 
ATOM   1499 C C   . GLY A 1 222 ? 16.37197  61.17468  2.40775  1.000 71.47324  ? 245 GLY A C   1 
ATOM   1500 O O   . GLY A 1 222 ? 15.49809  60.35450  2.10568  1.000 64.15161  ? 245 GLY A O   1 
ATOM   1501 N N   . ARG A 1 223 ? 17.49834  60.84801  3.04155  1.000 83.37855  ? 246 ARG A N   1 
ATOM   1502 C CA  . ARG A 1 223 ? 17.81745  59.47266  3.41186  1.000 75.08507  ? 246 ARG A CA  1 
ATOM   1503 C C   . ARG A 1 223 ? 16.75004  58.86389  4.31500  1.000 73.61901  ? 246 ARG A C   1 
ATOM   1504 O O   . ARG A 1 223 ? 16.43042  57.67532  4.19162  1.000 63.52399  ? 246 ARG A O   1 
ATOM   1505 C CB  . ARG A 1 223 ? 19.17935  59.49325  4.09559  1.000 71.66094  ? 246 ARG A CB  1 
ATOM   1506 C CG  . ARG A 1 223 ? 20.26186  58.64791  3.50211  1.000 78.94324  ? 246 ARG A CG  1 
ATOM   1507 C CD  . ARG A 1 223 ? 21.42638  58.73781  4.45655  1.000 88.06370  ? 246 ARG A CD  1 
ATOM   1508 N NE  . ARG A 1 223 ? 21.94488  60.10162  4.38405  1.000 110.59468 ? 246 ARG A NE  1 
ATOM   1509 C CZ  . ARG A 1 223 ? 22.95381  60.57842  5.09611  1.000 116.26178 ? 246 ARG A CZ  1 
ATOM   1510 N NH1 . ARG A 1 223 ? 23.59299  59.82839  5.97700  1.000 97.65295  ? 246 ARG A NH1 1 
ATOM   1511 N NH2 . ARG A 1 223 ? 23.32722  61.84206  4.91887  1.000 102.64439 ? 246 ARG A NH2 1 
ATOM   1512 N N   . CYS A 1 224 ? 16.20145  59.65957  5.24046  1.000 79.91910  ? 247 CYS A N   1 
ATOM   1513 C CA  . CYS A 1 224 ? 15.21466  59.14646  6.18925  1.000 61.32079  ? 247 CYS A CA  1 
ATOM   1514 C C   . CYS A 1 224 ? 14.02463  58.52684  5.46434  1.000 59.06216  ? 247 CYS A C   1 
ATOM   1515 O O   . CYS A 1 224 ? 13.48497  57.50008  5.89565  1.000 68.52298  ? 247 CYS A O   1 
ATOM   1516 C CB  . CYS A 1 224 ? 14.75929  60.26644  7.12327  1.000 71.87708  ? 247 CYS A CB  1 
ATOM   1517 S SG  . CYS A 1 224 ? 16.02271  60.77321  8.31777  1.000 71.24224  ? 247 CYS A SG  1 
ATOM   1518 N N   . ARG A 1 225 ? 13.60211  59.14314  4.35688  1.000 63.70094  ? 248 ARG A N   1 
ATOM   1519 C CA  . ARG A 1 225 ? 12.50277  58.61024  3.56187  1.000 61.11699  ? 248 ARG A CA  1 
ATOM   1520 C C   . ARG A 1 225 ? 12.90953  57.36708  2.77503  1.000 67.69763  ? 248 ARG A C   1 
ATOM   1521 O O   . ARG A 1 225 ? 12.04064  56.55922  2.42889  1.000 69.19667  ? 248 ARG A O   1 
ATOM   1522 C CB  . ARG A 1 225 ? 11.98041  59.70173  2.62185  1.000 68.72775  ? 248 ARG A CB  1 
ATOM   1523 C CG  . ARG A 1 225 ? 10.75161  60.45663  3.13357  1.000 52.70668  ? 248 ARG A CG  1 
ATOM   1524 C CD  . ARG A 1 225 ? 10.12381  61.29850  2.02481  1.000 60.04161  ? 248 ARG A CD  1 
ATOM   1525 N NE  . ARG A 1 225 ? 8.92598   62.01563  2.45160  1.000 64.22437  ? 248 ARG A NE  1 
ATOM   1526 C CZ  . ARG A 1 225 ? 8.92318   63.15895  3.12429  1.000 54.75192  ? 248 ARG A CZ  1 
ATOM   1527 N NH1 . ARG A 1 225 ? 10.04532  63.73017  3.52187  1.000 56.72161  ? 248 ARG A NH1 1 
ATOM   1528 N NH2 . ARG A 1 225 ? 7.76212   63.74148  3.41095  1.000 57.16545  ? 248 ARG A NH2 1 
ATOM   1529 N N   . GLN A 1 226 ? 14.20529  57.19329  2.48884  1.000 83.51403  ? 249 GLN A N   1 
ATOM   1530 C CA  . GLN A 1 226 ? 14.67136  55.95704  1.86231  1.000 72.65798  ? 249 GLN A CA  1 
ATOM   1531 C C   . GLN A 1 226 ? 14.55221  54.78794  2.83120  1.000 66.94317  ? 249 GLN A C   1 
ATOM   1532 O O   . GLN A 1 226 ? 14.05084  53.71601  2.46974  1.000 63.45158  ? 249 GLN A O   1 
ATOM   1533 C CB  . GLN A 1 226 ? 16.11410  56.10156  1.37107  1.000 73.49327  ? 249 GLN A CB  1 
ATOM   1534 C CG  . GLN A 1 226 ? 16.27029  56.88236  0.07382  1.000 73.11566  ? 249 GLN A CG  1 
ATOM   1535 C CD  . GLN A 1 226 ? 17.66671  57.44968  -0.09476 1.000 94.51560  ? 249 GLN A CD  1 
ATOM   1536 O OE1 . GLN A 1 226 ? 17.92924  58.60364  0.24296  1.000 112.16690 ? 249 GLN A OE1 1 
ATOM   1537 N NE2 . GLN A 1 226 ? 18.57473  56.63268  -0.61935 1.000 83.13499  ? 249 GLN A NE2 1 
ATOM   1538 N N   . VAL A 1 227 ? 15.00690  54.98587  4.07244  1.000 64.80421  ? 250 VAL A N   1 
ATOM   1539 C CA  . VAL A 1 227 ? 15.01489  53.91232  5.06567  1.000 51.08169  ? 250 VAL A CA  1 
ATOM   1540 C C   . VAL A 1 227 ? 13.58933  53.45956  5.35747  1.000 43.84462  ? 250 VAL A C   1 
ATOM   1541 O O   . VAL A 1 227 ? 13.30089  52.25761  5.41375  1.000 54.60486  ? 250 VAL A O   1 
ATOM   1542 C CB  . VAL A 1 227 ? 15.73510  54.37343  6.34695  1.000 55.99650  ? 250 VAL A CB  1 
ATOM   1543 C CG1 . VAL A 1 227 ? 15.62939  53.31899  7.43499  1.000 61.05969  ? 250 VAL A CG1 1 
ATOM   1544 C CG2 . VAL A 1 227 ? 17.19296  54.68261  6.06092  1.000 37.23973  ? 250 VAL A CG2 1 
ATOM   1545 N N   . VAL A 1 228 ? 12.68060  54.41908  5.55521  1.000 46.78659  ? 251 VAL A N   1 
ATOM   1546 C CA  . VAL A 1 228 ? 11.28021  54.10117  5.83331  1.000 45.01790  ? 251 VAL A CA  1 
ATOM   1547 C C   . VAL A 1 228 ? 10.69319  53.27206  4.69585  1.000 53.58499  ? 251 VAL A C   1 
ATOM   1548 O O   . VAL A 1 228 ? 9.96956   52.29424  4.92585  1.000 60.76307  ? 251 VAL A O   1 
ATOM   1549 C CB  . VAL A 1 228 ? 10.47957  55.39501  6.06680  1.000 39.07617  ? 251 VAL A CB  1 
ATOM   1550 C CG1 . VAL A 1 228 ? 8.98622   55.10591  6.05904  1.000 48.57275  ? 251 VAL A CG1 1 
ATOM   1551 C CG2 . VAL A 1 228 ? 10.91465  56.05773  7.36431  1.000 47.60195  ? 251 VAL A CG2 1 
ATOM   1552 N N   . THR A 1 229 ? 10.98982  53.65666  3.45273  1.000 66.57566  ? 252 THR A N   1 
ATOM   1553 C CA  . THR A 1 229 ? 10.53570  52.89137  2.29472  1.000 55.62030  ? 252 THR A CA  1 
ATOM   1554 C C   . THR A 1 229 ? 11.08559  51.46741  2.33689  1.000 47.89391  ? 252 THR A C   1 
ATOM   1555 O O   . THR A 1 229 ? 10.36245  50.50328  2.05621  1.000 40.38271  ? 252 THR A O   1 
ATOM   1556 C CB  . THR A 1 229 ? 10.94363  53.59309  0.99690  1.000 49.70643  ? 252 THR A CB  1 
ATOM   1557 O OG1 . THR A 1 229 ? 10.17412  54.78932  0.83426  1.000 68.22425  ? 252 THR A OG1 1 
ATOM   1558 C CG2 . THR A 1 229 ? 10.69268  52.68673  -0.19935 1.000 55.50308  ? 252 THR A CG2 1 
ATOM   1559 N N   . GLY A 1 230 ? 12.37071  51.32028  2.66773  1.000 50.95627  ? 253 GLY A N   1 
ATOM   1560 C CA  . GLY A 1 230 ? 12.95415  49.99222  2.79973  1.000 40.87668  ? 253 GLY A CA  1 
ATOM   1561 C C   . GLY A 1 230 ? 12.24484  49.15551  3.84857  1.000 51.75162  ? 253 GLY A C   1 
ATOM   1562 O O   . GLY A 1 230 ? 12.03347  47.95215  3.66356  1.000 51.36733  ? 253 GLY A O   1 
ATOM   1563 N N   . MET A 1 231 ? 11.87512  49.78056  4.96845  1.000 43.92850  ? 254 MET A N   1 
ATOM   1564 C CA  . MET A 1 231 ? 11.26868  49.04751  6.07154  1.000 33.33038  ? 254 MET A CA  1 
ATOM   1565 C C   . MET A 1 231 ? 9.88714   48.56086  5.69788  1.000 32.75771  ? 254 MET A C   1 
ATOM   1566 O O   . MET A 1 231 ? 9.49641   47.45043  6.06987  1.000 38.40078  ? 254 MET A O   1 
ATOM   1567 C CB  . MET A 1 231 ? 11.15095  49.95734  7.27952  1.000 40.20010  ? 254 MET A CB  1 
ATOM   1568 C CG  . MET A 1 231 ? 12.43357  50.34336  7.90760  1.000 38.24787  ? 254 MET A CG  1 
ATOM   1569 S SD  . MET A 1 231 ? 11.96643  51.26903  9.35872  1.000 42.23924  ? 254 MET A SD  1 
ATOM   1570 C CE  . MET A 1 231 ? 13.48332  51.15362  10.21125 1.000 33.27963  ? 254 MET A CE  1 
ATOM   1571 N N   . ALA A 1 232 ? 9.15669   49.36522  4.92656  1.000 39.04294  ? 255 ALA A N   1 
ATOM   1572 C CA  . ALA A 1 232 ? 7.82735   48.97199  4.48794  1.000 32.16214  ? 255 ALA A CA  1 
ATOM   1573 C C   . ALA A 1 232 ? 7.92464   47.72642  3.62547  1.000 37.71775  ? 255 ALA A C   1 
ATOM   1574 O O   . ALA A 1 232 ? 7.16647   46.76590  3.80925  1.000 42.94242  ? 255 ALA A O   1 
ATOM   1575 C CB  . ALA A 1 232 ? 7.16071   50.12254  3.73379  1.000 38.26886  ? 255 ALA A CB  1 
ATOM   1576 N N   . TRP A 1 233 ? 8.86324   47.72673  2.67734  1.000 47.29198  ? 256 TRP A N   1 
ATOM   1577 C CA  . TRP A 1 233 ? 9.04348   46.56577  1.81932  1.000 45.11744  ? 256 TRP A CA  1 
ATOM   1578 C C   . TRP A 1 233 ? 9.38985   45.35293  2.67611  1.000 50.00508  ? 256 TRP A C   1 
ATOM   1579 O O   . TRP A 1 233 ? 8.73340   44.30794  2.59069  1.000 57.88061  ? 256 TRP A O   1 
ATOM   1580 C CB  . TRP A 1 233 ? 10.15777  46.85444  0.81205  1.000 57.64699  ? 256 TRP A CB  1 
ATOM   1581 C CG  . TRP A 1 233 ? 9.70769   47.56851  -0.43391 1.000 55.84833  ? 256 TRP A CG  1 
ATOM   1582 C CD1 . TRP A 1 233 ? 9.91182   48.88771  -0.72795 1.000 71.86925  ? 256 TRP A CD1 1 
ATOM   1583 C CD2 . TRP A 1 233 ? 8.98630   47.01961  -1.54317 1.000 67.98344  ? 256 TRP A CD2 1 
ATOM   1584 N NE1 . TRP A 1 233 ? 9.36436   49.19346  -1.94774 1.000 89.95710  ? 256 TRP A NE1 1 
ATOM   1585 C CE2 . TRP A 1 233 ? 8.78962   48.06495  -2.47014 1.000 85.94101  ? 256 TRP A CE2 1 
ATOM   1586 C CE3 . TRP A 1 233 ? 8.48842   45.74838  -1.84492 1.000 77.73845  ? 256 TRP A CE3 1 
ATOM   1587 C CZ2 . TRP A 1 233 ? 8.11784   47.87746  -3.67546 1.000 94.78283  ? 256 TRP A CZ2 1 
ATOM   1588 C CZ3 . TRP A 1 233 ? 7.82028   45.56526  -3.04292 1.000 66.58148  ? 256 TRP A CZ3 1 
ATOM   1589 C CH2 . TRP A 1 233 ? 7.64163   46.62424  -3.94276 1.000 79.57587  ? 256 TRP A CH2 1 
ATOM   1590 N N   . LEU A 1 234 ? 10.44340  45.47576  3.49468  1.000 40.60621  ? 257 LEU A N   1 
ATOM   1591 C CA  . LEU A 1 234 ? 10.83855  44.41094  4.41679  1.000 32.06578  ? 257 LEU A CA  1 
ATOM   1592 C C   . LEU A 1 234 ? 9.65943   43.92518  5.25048  1.000 44.14518  ? 257 LEU A C   1 
ATOM   1593 O O   . LEU A 1 234 ? 9.43257   42.71845  5.39217  1.000 55.23299  ? 257 LEU A O   1 
ATOM   1594 C CB  . LEU A 1 234 ? 11.95307  44.89933  5.34007  1.000 39.04641  ? 257 LEU A CB  1 
ATOM   1595 C CG  . LEU A 1 234 ? 13.37548  44.47961  4.99377  1.000 45.36204  ? 257 LEU A CG  1 
ATOM   1596 C CD1 . LEU A 1 234 ? 14.34109  45.01707  6.03912  1.000 51.91558  ? 257 LEU A CD1 1 
ATOM   1597 C CD2 . LEU A 1 234 ? 13.45420  42.96885  4.89730  1.000 41.18658  ? 257 LEU A CD2 1 
ATOM   1598 N N   . PHE A 1 235 ? 8.90829   44.86971  5.82646  1.000 41.79213  ? 258 PHE A N   1 
ATOM   1599 C CA  . PHE A 1 235 ? 7.86479   44.53698  6.79367  1.000 32.43501  ? 258 PHE A CA  1 
ATOM   1600 C C   . PHE A 1 235 ? 6.76452   43.71019  6.14440  1.000 50.66775  ? 258 PHE A C   1 
ATOM   1601 O O   . PHE A 1 235 ? 6.44245   42.60722  6.60419  1.000 46.00042  ? 258 PHE A O   1 
ATOM   1602 C CB  . PHE A 1 235 ? 7.29052   45.81854  7.40462  1.000 26.58414  ? 258 PHE A CB  1 
ATOM   1603 C CG  . PHE A 1 235 ? 6.20936   45.58199  8.42152  1.000 39.92294  ? 258 PHE A CG  1 
ATOM   1604 C CD1 . PHE A 1 235 ? 6.53048   45.40679  9.75987  1.000 45.31220  ? 258 PHE A CD1 1 
ATOM   1605 C CD2 . PHE A 1 235 ? 4.87505   45.54051  8.04633  1.000 39.76395  ? 258 PHE A CD2 1 
ATOM   1606 C CE1 . PHE A 1 235 ? 5.54227   45.19128  10.70465 1.000 40.19800  ? 258 PHE A CE1 1 
ATOM   1607 C CE2 . PHE A 1 235 ? 3.88259   45.32162  8.98561  1.000 38.36841  ? 258 PHE A CE2 1 
ATOM   1608 C CZ  . PHE A 1 235 ? 4.21635   45.14858  10.31670 1.000 43.80346  ? 258 PHE A CZ  1 
ATOM   1609 N N   . PHE A 1 236 ? 6.18838   44.22540  5.05481  1.000 54.98295  ? 259 PHE A N   1 
ATOM   1610 C CA  . PHE A 1 236 ? 5.03385   43.57932  4.44268  1.000 43.85408  ? 259 PHE A CA  1 
ATOM   1611 C C   . PHE A 1 236 ? 5.42458   42.26405  3.79071  1.000 44.81269  ? 259 PHE A C   1 
ATOM   1612 O O   . PHE A 1 236 ? 4.62162   41.32355  3.76163  1.000 40.93273  ? 259 PHE A O   1 
ATOM   1613 C CB  . PHE A 1 236 ? 4.38977   44.52832  3.43588  1.000 36.93480  ? 259 PHE A CB  1 
ATOM   1614 C CG  . PHE A 1 236 ? 3.62658   45.64753  4.08031  1.000 31.19260  ? 259 PHE A CG  1 
ATOM   1615 C CD1 . PHE A 1 236 ? 3.93728   46.96814  3.80531  1.000 36.47567  ? 259 PHE A CD1 1 
ATOM   1616 C CD2 . PHE A 1 236 ? 2.60496   45.37482  4.97890  1.000 48.72939  ? 259 PHE A CD2 1 
ATOM   1617 C CE1 . PHE A 1 236 ? 3.23563   47.99907  4.40825  1.000 43.88328  ? 259 PHE A CE1 1 
ATOM   1618 C CE2 . PHE A 1 236 ? 1.90026   46.39827  5.58396  1.000 35.32458  ? 259 PHE A CE2 1 
ATOM   1619 C CZ  . PHE A 1 236 ? 2.21741   47.71000  5.30025  1.000 35.22474  ? 259 PHE A CZ  1 
ATOM   1620 N N   . VAL A 1 237 ? 6.65563   42.16963  3.29033  1.000 55.29679  ? 260 VAL A N   1 
ATOM   1621 C CA  . VAL A 1 237 ? 7.09780   40.94059  2.64362  1.000 51.67931  ? 260 VAL A CA  1 
ATOM   1622 C C   . VAL A 1 237 ? 7.35848   39.87459  3.69765  1.000 39.53145  ? 260 VAL A C   1 
ATOM   1623 O O   . VAL A 1 237 ? 6.87626   38.74124  3.59146  1.000 53.97321  ? 260 VAL A O   1 
ATOM   1624 C CB  . VAL A 1 237 ? 8.34312   41.20243  1.77790  1.000 44.01139  ? 260 VAL A CB  1 
ATOM   1625 C CG1 . VAL A 1 237 ? 9.01935   39.89234  1.41067  1.000 34.37611  ? 260 VAL A CG1 1 
ATOM   1626 C CG2 . VAL A 1 237 ? 7.95911   41.97856  0.52461  1.000 37.72103  ? 260 VAL A CG2 1 
ATOM   1627 N N   . SER A 1 238 ? 8.10578   40.22990  4.74544  1.000 47.05471  ? 261 SER A N   1 
ATOM   1628 C CA  . SER A 1 238 ? 8.47585   39.24297  5.75388  1.000 49.14641  ? 261 SER A CA  1 
ATOM   1629 C C   . SER A 1 238 ? 7.26649   38.83840  6.59066  1.000 45.45443  ? 261 SER A C   1 
ATOM   1630 O O   . SER A 1 238 ? 7.02439   37.64522  6.80395  1.000 49.71825  ? 261 SER A O   1 
ATOM   1631 C CB  . SER A 1 238 ? 9.59128   39.79575  6.63733  1.000 40.21826  ? 261 SER A CB  1 
ATOM   1632 O OG  . SER A 1 238 ? 9.13594   40.91783  7.37182  1.000 52.53437  ? 261 SER A OG  1 
ATOM   1633 N N   . TRP A 1 239 ? 6.46533   39.81281  7.03531  1.000 41.12299  ? 262 TRP A N   1 
ATOM   1634 C CA  . TRP A 1 239 ? 5.26740   39.46917  7.79971  1.000 50.20876  ? 262 TRP A CA  1 
ATOM   1635 C C   . TRP A 1 239 ? 4.25484   38.75287  6.91927  1.000 49.13290  ? 262 TRP A C   1 
ATOM   1636 O O   . TRP A 1 239 ? 3.54134   37.85647  7.38340  1.000 50.35476  ? 262 TRP A O   1 
ATOM   1637 C CB  . TRP A 1 239 ? 4.64102   40.71083  8.43538  1.000 34.62522  ? 262 TRP A CB  1 
ATOM   1638 C CG  . TRP A 1 239 ? 5.38035   41.23588  9.62349  1.000 36.45356  ? 262 TRP A CG  1 
ATOM   1639 C CD1 . TRP A 1 239 ? 6.70918   41.53301  9.70417  1.000 39.38169  ? 262 TRP A CD1 1 
ATOM   1640 C CD2 . TRP A 1 239 ? 4.82158   41.54124  10.90673 1.000 37.72009  ? 262 TRP A CD2 1 
ATOM   1641 N NE1 . TRP A 1 239 ? 7.01440   41.99940  10.96131 1.000 33.46894  ? 262 TRP A NE1 1 
ATOM   1642 C CE2 . TRP A 1 239 ? 5.87131   42.01807  11.71698 1.000 49.12457  ? 262 TRP A CE2 1 
ATOM   1643 C CE3 . TRP A 1 239 ? 3.53470   41.45701  11.44902 1.000 41.77230  ? 262 TRP A CE3 1 
ATOM   1644 C CZ2 . TRP A 1 239 ? 5.67505   42.40706  13.04285 1.000 51.64759  ? 262 TRP A CZ2 1 
ATOM   1645 C CZ3 . TRP A 1 239 ? 3.34092   41.84368  12.76411 1.000 36.50029  ? 262 TRP A CZ3 1 
ATOM   1646 C CH2 . TRP A 1 239 ? 4.40600   42.31362  13.54629 1.000 39.69227  ? 262 TRP A CH2 1 
ATOM   1647 N N   . GLY A 1 240 ? 4.16991   39.14514  5.64846  1.000 57.31523  ? 263 GLY A N   1 
ATOM   1648 C CA  . GLY A 1 240 ? 3.23617   38.51561  4.73760  1.000 50.68191  ? 263 GLY A CA  1 
ATOM   1649 C C   . GLY A 1 240 ? 3.59854   37.08262  4.42084  1.000 52.05681  ? 263 GLY A C   1 
ATOM   1650 O O   . GLY A 1 240 ? 2.71814   36.29493  4.05406  1.000 49.06062  ? 263 GLY A O   1 
ATOM   1651 N N   . MET A 1 241 ? 4.87416   36.72287  4.58301  1.000 45.39568  ? 264 MET A N   1 
ATOM   1652 C CA  . MET A 1 241 ? 5.31656   35.36742  4.29949  1.000 36.92656  ? 264 MET A CA  1 
ATOM   1653 C C   . MET A 1 241 ? 4.82774   34.39007  5.36325  1.000 42.69099  ? 264 MET A C   1 
ATOM   1654 O O   . MET A 1 241 ? 4.78898   33.18016  5.11288  1.000 51.09529  ? 264 MET A O   1 
ATOM   1655 C CB  . MET A 1 241 ? 6.84367   35.31484  4.23262  1.000 49.20141  ? 264 MET A CB  1 
ATOM   1656 C CG  . MET A 1 241 ? 7.46717   35.69031  2.88967  1.000 53.21541  ? 264 MET A CG  1 
ATOM   1657 S SD  . MET A 1 241 ? 7.15551   34.58528  1.50681  1.000 72.43948  ? 264 MET A SD  1 
ATOM   1658 C CE  . MET A 1 241 ? 5.83147   35.48357  0.68657  1.000 83.13891  ? 264 MET A CE  1 
ATOM   1659 N N   . PHE A 1 242 ? 4.46555   34.89481  6.54730  1.000 53.67552  ? 265 PHE A N   1 
ATOM   1660 C CA  . PHE A 1 242 ? 4.15270   34.01569  7.67392  1.000 41.36490  ? 265 PHE A CA  1 
ATOM   1661 C C   . PHE A 1 242 ? 2.88559   33.20325  7.43146  1.000 45.87696  ? 265 PHE A C   1 
ATOM   1662 O O   . PHE A 1 242 ? 2.93410   31.97015  7.58959  1.000 46.95029  ? 265 PHE A O   1 
ATOM   1663 C CB  . PHE A 1 242 ? 4.08206   34.81864  8.97861  1.000 42.82978  ? 265 PHE A CB  1 
ATOM   1664 C CG  . PHE A 1 242 ? 5.42697   35.14260  9.57548  1.000 51.27342  ? 265 PHE A CG  1 
ATOM   1665 C CD1 . PHE A 1 242 ? 6.04424   36.35489  9.32078  1.000 58.94964  ? 265 PHE A CD1 1 
ATOM   1666 C CD2 . PHE A 1 242 ? 6.06664   34.23578  10.40667 1.000 57.60877  ? 265 PHE A CD2 1 
ATOM   1667 C CE1 . PHE A 1 242 ? 7.28033   36.65631  9.87838  1.000 52.63023  ? 265 PHE A CE1 1 
ATOM   1668 C CE2 . PHE A 1 242 ? 7.30407   34.52897  10.96903 1.000 49.98772  ? 265 PHE A CE2 1 
ATOM   1669 C CZ  . PHE A 1 242 ? 7.91134   35.74246  10.70075 1.000 39.35009  ? 265 PHE A CZ  1 
ATOM   1670 N N   . PRO A 1 243 ? 1.73202   33.79594  7.08346  1.000 48.05448  ? 266 PRO A N   1 
ATOM   1671 C CA  . PRO A 1 243 ? 0.55985   32.94876  6.79116  1.000 46.09853  ? 266 PRO A CA  1 
ATOM   1672 C C   . PRO A 1 243 ? 0.82163   31.95943  5.67354  1.000 51.87731  ? 266 PRO A C   1 
ATOM   1673 O O   . PRO A 1 243 ? 0.24612   30.86337  5.67856  1.000 48.41765  ? 266 PRO A O   1 
ATOM   1674 C CB  . PRO A 1 243 ? -0.53433  33.95423  6.39907  1.000 51.45324  ? 266 PRO A CB  1 
ATOM   1675 C CG  . PRO A 1 243 ? 0.14653   35.26069  6.20551  1.000 49.33714  ? 266 PRO A CG  1 
ATOM   1676 C CD  . PRO A 1 243 ? 1.41921   35.23350  6.97307  1.000 45.74517  ? 266 PRO A CD  1 
ATOM   1677 N N   . ILE A 1 244 ? 1.69469   32.30609  4.72625  1.000 53.83105  ? 267 ILE A N   1 
ATOM   1678 C CA  . ILE A 1 244 ? 2.01693   31.39036  3.63721  1.000 48.72771  ? 267 ILE A CA  1 
ATOM   1679 C C   . ILE A 1 244 ? 2.80678   30.19935  4.16591  1.000 44.01088  ? 267 ILE A C   1 
ATOM   1680 O O   . ILE A 1 244 ? 2.52215   29.05021  3.81078  1.000 53.86719  ? 267 ILE A O   1 
ATOM   1681 C CB  . ILE A 1 244 ? 2.74067   32.13324  2.50215  1.000 30.74234  ? 267 ILE A CB  1 
ATOM   1682 C CG1 . ILE A 1 244 ? 1.89277   33.33553  2.07847  1.000 26.00262  ? 267 ILE A CG1 1 
ATOM   1683 C CG2 . ILE A 1 244 ? 3.01902   31.20148  1.33938  1.000 39.21702  ? 267 ILE A CG2 1 
ATOM   1684 C CD1 . ILE A 1 244 ? 2.62537   34.36778  1.28581  1.000 48.57936  ? 267 ILE A CD1 1 
ATOM   1685 N N   . LEU A 1 245 ? 3.80229   30.44116  5.02644  1.000 36.84114  ? 268 LEU A N   1 
ATOM   1686 C CA  . LEU A 1 245 ? 4.57837   29.31870  5.54898  1.000 40.52334  ? 268 LEU A CA  1 
ATOM   1687 C C   . LEU A 1 245 ? 3.69605   28.43242  6.41349  1.000 46.17225  ? 268 LEU A C   1 
ATOM   1688 O O   . LEU A 1 245 ? 3.92133   27.21902  6.50131  1.000 50.66623  ? 268 LEU A O   1 
ATOM   1689 C CB  . LEU A 1 245 ? 5.79164   29.80119  6.34270  1.000 48.57908  ? 268 LEU A CB  1 
ATOM   1690 C CG  . LEU A 1 245 ? 6.97039   30.33667  5.53077  1.000 38.12902  ? 268 LEU A CG  1 
ATOM   1691 C CD1 . LEU A 1 245 ? 8.15148   30.64134  6.44470  1.000 29.23593  ? 268 LEU A CD1 1 
ATOM   1692 C CD2 . LEU A 1 245 ? 7.35895   29.33347  4.45798  1.000 25.37770  ? 268 LEU A CD2 1 
ATOM   1693 N N   . PHE A 1 246 ? 2.70130   29.03436  7.06625  1.000 49.78205  ? 269 PHE A N   1 
ATOM   1694 C CA  . PHE A 1 246 ? 1.74815   28.28420  7.87621  1.000 39.51515  ? 269 PHE A CA  1 
ATOM   1695 C C   . PHE A 1 246 ? 0.96880   27.30758  7.00101  1.000 43.31959  ? 269 PHE A C   1 
ATOM   1696 O O   . PHE A 1 246 ? 0.92947   26.10184  7.27265  1.000 47.84022  ? 269 PHE A O   1 
ATOM   1697 C CB  . PHE A 1 246 ? 0.80716   29.25861  8.59184  1.000 48.14744  ? 269 PHE A CB  1 
ATOM   1698 C CG  . PHE A 1 246 ? -0.05235  28.62494  9.65497  1.000 51.57353  ? 269 PHE A CG  1 
ATOM   1699 C CD1 . PHE A 1 246 ? -1.15557  27.85576  9.31324  1.000 41.47490  ? 269 PHE A CD1 1 
ATOM   1700 C CD2 . PHE A 1 246 ? 0.23970   28.80879  10.99869 1.000 40.99578  ? 269 PHE A CD2 1 
ATOM   1701 C CE1 . PHE A 1 246 ? -1.94557  27.27576  10.28829 1.000 34.60694  ? 269 PHE A CE1 1 
ATOM   1702 C CE2 . PHE A 1 246 ? -0.54787  28.23024  11.97998 1.000 43.07437  ? 269 PHE A CE2 1 
ATOM   1703 C CZ  . PHE A 1 246 ? -1.64289  27.46337  11.62310 1.000 39.02441  ? 269 PHE A CZ  1 
ATOM   1704 N N   . ILE A 1 247 ? 0.33789   27.82497  5.94109  1.000 60.12273  ? 270 ILE A N   1 
ATOM   1705 C CA  . ILE A 1 247 ? -0.44636  27.00714  5.01340  1.000 48.67457  ? 270 ILE A CA  1 
ATOM   1706 C C   . ILE A 1 247 ? 0.37766   25.84338  4.46015  1.000 57.13260  ? 270 ILE A C   1 
ATOM   1707 O O   . ILE A 1 247 ? -0.12816  24.72212  4.31656  1.000 70.30555  ? 270 ILE A O   1 
ATOM   1708 C CB  . ILE A 1 247 ? -1.00215  27.89825  3.88441  1.000 32.18949  ? 270 ILE A CB  1 
ATOM   1709 C CG1 . ILE A 1 247 ? -2.11304  28.80418  4.41962  1.000 47.51864  ? 270 ILE A CG1 1 
ATOM   1710 C CG2 . ILE A 1 247 ? -1.53308  27.05627  2.74152  1.000 65.44280  ? 270 ILE A CG2 1 
ATOM   1711 C CD1 . ILE A 1 247 ? -2.47568  29.94341  3.48794  1.000 61.03474  ? 270 ILE A CD1 1 
ATOM   1712 N N   . LEU A 1 248 ? 1.66515   26.07258  4.17867  1.000 52.28146  ? 271 LEU A N   1 
ATOM   1713 C CA  . LEU A 1 248 ? 2.50694   25.03450  3.58033  1.000 50.21260  ? 271 LEU A CA  1 
ATOM   1714 C C   . LEU A 1 248 ? 3.03925   24.04077  4.60476  1.000 49.70258  ? 271 LEU A C   1 
ATOM   1715 O O   . LEU A 1 248 ? 3.39817   22.91868  4.22974  1.000 51.40931  ? 271 LEU A O   1 
ATOM   1716 C CB  . LEU A 1 248 ? 3.69669   25.62965  2.81522  1.000 49.53948  ? 271 LEU A CB  1 
ATOM   1717 C CG  . LEU A 1 248 ? 3.58889   26.36843  1.47481  1.000 50.33019  ? 271 LEU A CG  1 
ATOM   1718 C CD1 . LEU A 1 248 ? 2.38132   27.28809  1.35563  1.000 64.98625  ? 271 LEU A CD1 1 
ATOM   1719 C CD2 . LEU A 1 248 ? 4.88628   27.13482  1.21581  1.000 32.49709  ? 271 LEU A CD2 1 
ATOM   1720 N N   . GLY A 1 249 ? 3.11296   24.42417  5.87509  1.000 41.99415  ? 272 GLY A N   1 
ATOM   1721 C CA  . GLY A 1 249 ? 3.80500   23.63683  6.86518  1.000 47.00555  ? 272 GLY A CA  1 
ATOM   1722 C C   . GLY A 1 249 ? 2.92812   22.53820  7.42937  1.000 46.67017  ? 272 GLY A C   1 
ATOM   1723 O O   . GLY A 1 249 ? 1.76699   22.35037  7.03588  1.000 47.88944  ? 272 GLY A O   1 
ATOM   1724 N N   . PRO A 1 250 ? 3.49877   21.76795  8.36111  1.000 35.73292  ? 273 PRO A N   1 
ATOM   1725 C CA  . PRO A 1 250 ? 2.69475   20.76158  9.08019  1.000 37.30141  ? 273 PRO A CA  1 
ATOM   1726 C C   . PRO A 1 250 ? 1.42781   21.33005  9.69332  1.000 48.49848  ? 273 PRO A C   1 
ATOM   1727 O O   . PRO A 1 250 ? 0.45116   20.59083  9.87946  1.000 42.77565  ? 273 PRO A O   1 
ATOM   1728 C CB  . PRO A 1 250 ? 3.66063   20.23681  10.15220 1.000 29.01346  ? 273 PRO A CB  1 
ATOM   1729 C CG  . PRO A 1 250 ? 5.02440   20.55261  9.63813  1.000 35.65959  ? 273 PRO A CG  1 
ATOM   1730 C CD  . PRO A 1 250 ? 4.89861   21.80128  8.81724  1.000 47.29569  ? 273 PRO A CD  1 
ATOM   1731 N N   . GLU A 1 251 ? 1.41822   22.62133  10.02880 1.000 53.04685  ? 274 GLU A N   1 
ATOM   1732 C CA  . GLU A 1 251 ? 0.23727   23.25256  10.60126 1.000 44.86820  ? 274 GLU A CA  1 
ATOM   1733 C C   . GLU A 1 251 ? -0.88703  23.39909  9.57999  1.000 54.34307  ? 274 GLU A C   1 
ATOM   1734 O O   . GLU A 1 251 ? -2.00895  23.74899  9.96121  1.000 63.63795  ? 274 GLU A O   1 
ATOM   1735 C CB  . GLU A 1 251 ? 0.60862   24.62040  11.18367 1.000 44.79649  ? 274 GLU A CB  1 
ATOM   1736 C CG  . GLU A 1 251 ? 1.50791   25.46049  10.28238 1.000 44.23197  ? 274 GLU A CG  1 
ATOM   1737 C CD  . GLU A 1 251 ? 2.92978   25.59581  10.80933 1.000 51.05289  ? 274 GLU A CD  1 
ATOM   1738 O OE1 . GLU A 1 251 ? 3.70606   24.62020  10.69462 1.000 48.75440  ? 274 GLU A OE1 1 
ATOM   1739 O OE2 . GLU A 1 251 ? 3.27488   26.68348  11.32566 1.000 52.02057  ? 274 GLU A OE2 1 
ATOM   1740 N N   . GLY A 1 252 ? -0.60332  23.16739  8.29899  1.000 39.50951  ? 275 GLY A N   1 
ATOM   1741 C CA  . GLY A 1 252 ? -1.55597  23.34621  7.21988  1.000 41.16733  ? 275 GLY A CA  1 
ATOM   1742 C C   . GLY A 1 252 ? -1.67189  22.08093  6.39192  1.000 67.58914  ? 275 GLY A C   1 
ATOM   1743 O O   . GLY A 1 252 ? -2.31254  21.11129  6.81116  1.000 64.11294  ? 275 GLY A O   1 
ATOM   1744 N N   . PHE A 1 253 ? -1.04887  22.08028  5.21300  1.000 64.62540  ? 276 PHE A N   1 
ATOM   1745 C CA  . PHE A 1 253 ? -1.15510  20.99659  4.24281  1.000 62.71924  ? 276 PHE A CA  1 
ATOM   1746 C C   . PHE A 1 253 ? 0.07882   20.10249  4.21193  1.000 61.22930  ? 276 PHE A C   1 
ATOM   1747 O O   . PHE A 1 253 ? 0.18098   19.23501  3.33904  1.000 78.66413  ? 276 PHE A O   1 
ATOM   1748 C CB  . PHE A 1 253 ? -1.45288  21.54539  2.84650  1.000 61.42413  ? 276 PHE A CB  1 
ATOM   1749 C CG  . PHE A 1 253 ? -2.80282  22.19405  2.72973  1.000 79.80406  ? 276 PHE A CG  1 
ATOM   1750 C CD1 . PHE A 1 253 ? -2.94011  23.46709  2.20204  1.000 77.31252  ? 276 PHE A CD1 1 
ATOM   1751 C CD2 . PHE A 1 253 ? -3.94264  21.51501  3.13871  1.000 74.93056  ? 276 PHE A CD2 1 
ATOM   1752 C CE1 . PHE A 1 253 ? -4.18994  24.05541  2.09301  1.000 76.62470  ? 276 PHE A CE1 1 
ATOM   1753 C CE2 . PHE A 1 253 ? -5.19147  22.09522  3.03281  1.000 76.47840  ? 276 PHE A CE2 1 
ATOM   1754 C CZ  . PHE A 1 253 ? -5.31593  23.36763  2.50899  1.000 87.63555  ? 276 PHE A CZ  1 
ATOM   1755 N N   . GLY A 1 254 ? 1.01410   20.29702  5.13774  1.000 57.63468  ? 277 GLY A N   1 
ATOM   1756 C CA  . GLY A 1 254 ? 2.16798   19.41923  5.24433  1.000 50.93433  ? 277 GLY A CA  1 
ATOM   1757 C C   . GLY A 1 254 ? 3.03359   19.32492  4.00921  1.000 63.85280  ? 277 GLY A C   1 
ATOM   1758 O O   . GLY A 1 254 ? 3.71260   18.31039  3.81327  1.000 87.90775  ? 277 GLY A O   1 
ATOM   1759 N N   . VAL A 1 255 ? 3.02280   20.35321  3.15941  1.000 59.97939  ? 278 VAL A N   1 
ATOM   1760 C CA  . VAL A 1 255 ? 3.97870   20.40373  2.05644  1.000 62.54364  ? 278 VAL A CA  1 
ATOM   1761 C C   . VAL A 1 255 ? 5.39649   20.43036  2.61252  1.000 57.64099  ? 278 VAL A C   1 
ATOM   1762 O O   . VAL A 1 255 ? 6.23960   19.59593  2.26334  1.000 62.45741  ? 278 VAL A O   1 
ATOM   1763 C CB  . VAL A 1 255 ? 3.69972   21.61777  1.15198  1.000 67.54708  ? 278 VAL A CB  1 
ATOM   1764 C CG1 . VAL A 1 255 ? 4.76974   21.73438  0.07267  1.000 42.51140  ? 278 VAL A CG1 1 
ATOM   1765 C CG2 . VAL A 1 255 ? 2.31408   21.50948  0.53114  1.000 59.72240  ? 278 VAL A CG2 1 
ATOM   1766 N N   . LEU A 1 256 ? 5.67516   21.38921  3.49003  1.000 67.72064  ? 279 LEU A N   1 
ATOM   1767 C CA  . LEU A 1 256 ? 6.97671   21.49102  4.12851  1.000 65.90271  ? 279 LEU A CA  1 
ATOM   1768 C C   . LEU A 1 256 ? 7.03834   20.53963  5.32061  1.000 60.27053  ? 279 LEU A C   1 
ATOM   1769 O O   . LEU A 1 256 ? 6.04317   20.31490  6.01620  1.000 63.11454  ? 279 LEU A O   1 
ATOM   1770 C CB  . LEU A 1 256 ? 7.24039   22.92872  4.58061  1.000 69.01876  ? 279 LEU A CB  1 
ATOM   1771 C CG  . LEU A 1 256 ? 7.47930   23.96263  3.47565  1.000 63.43161  ? 279 LEU A CG  1 
ATOM   1772 C CD1 . LEU A 1 256 ? 7.33206   25.37915  4.01224  1.000 61.21359  ? 279 LEU A CD1 1 
ATOM   1773 C CD2 . LEU A 1 256 ? 8.84871   23.77122  2.84468  1.000 69.03269  ? 279 LEU A CD2 1 
ATOM   1774 N N   . SER A 1 257 ? 8.22296   19.97962  5.55180  1.000 50.12291  ? 280 SER A N   1 
ATOM   1775 C CA  . SER A 1 257 ? 8.50946   19.24716  6.77620  1.000 44.34737  ? 280 SER A CA  1 
ATOM   1776 C C   . SER A 1 257 ? 8.78414   20.20159  7.93689  1.000 45.59590  ? 280 SER A C   1 
ATOM   1777 O O   . SER A 1 257 ? 8.75351   21.42721  7.79638  1.000 47.24418  ? 280 SER A O   1 
ATOM   1778 C CB  . SER A 1 257 ? 9.69756   18.31516  6.56396  1.000 52.84483  ? 280 SER A CB  1 
ATOM   1779 O OG  . SER A 1 257 ? 10.89349  19.06653  6.45858  1.000 42.87182  ? 280 SER A OG  1 
ATOM   1780 N N   . VAL A 1 258 ? 9.04947   19.62006  9.10986  1.000 50.70690  ? 281 VAL A N   1 
ATOM   1781 C CA  . VAL A 1 258 ? 9.32123   20.42040  10.30133 1.000 36.93944  ? 281 VAL A CA  1 
ATOM   1782 C C   . VAL A 1 258 ? 10.61444  21.20524  10.12309 1.000 40.28578  ? 281 VAL A C   1 
ATOM   1783 O O   . VAL A 1 258 ? 10.67916  22.40457  10.41933 1.000 47.45772  ? 281 VAL A O   1 
ATOM   1784 C CB  . VAL A 1 258 ? 9.36988   19.52441  11.54956 1.000 32.57010  ? 281 VAL A CB  1 
ATOM   1785 C CG1 . VAL A 1 258 ? 9.90087   20.30657  12.74222 1.000 36.56302  ? 281 VAL A CG1 1 
ATOM   1786 C CG2 . VAL A 1 258 ? 7.99114   18.95871  11.83761 1.000 38.22697  ? 281 VAL A CG2 1 
ATOM   1787 N N   . TYR A 1 259 ? 11.67126  20.53175  9.66261  1.000 54.24282  ? 282 TYR A N   1 
ATOM   1788 C CA  . TYR A 1 259 ? 12.92903  21.22016  9.39103  1.000 54.07340  ? 282 TYR A CA  1 
ATOM   1789 C C   . TYR A 1 259 ? 12.74064  22.25230  8.28606  1.000 44.28605  ? 282 TYR A C   1 
ATOM   1790 O O   . TYR A 1 259 ? 13.22064  23.38718  8.39150  1.000 45.78615  ? 282 TYR A O   1 
ATOM   1791 C CB  . TYR A 1 259 ? 14.02657  20.22125  9.02506  1.000 60.40472  ? 282 TYR A CB  1 
ATOM   1792 C CG  . TYR A 1 259 ? 14.40575  19.26620  10.13496 1.000 76.03478  ? 282 TYR A CG  1 
ATOM   1793 C CD1 . TYR A 1 259 ? 14.57699  19.72084  11.43569 1.000 66.59121  ? 282 TYR A CD1 1 
ATOM   1794 C CD2 . TYR A 1 259 ? 14.62524  17.91702  9.87745  1.000 73.49352  ? 282 TYR A CD2 1 
ATOM   1795 C CE1 . TYR A 1 259 ? 14.94619  18.86149  12.45004 1.000 68.04726  ? 282 TYR A CE1 1 
ATOM   1796 C CE2 . TYR A 1 259 ? 14.98664  17.04557  10.89186 1.000 74.73458  ? 282 TYR A CE2 1 
ATOM   1797 C CZ  . TYR A 1 259 ? 15.14625  17.52771  12.17814 1.000 83.64428  ? 282 TYR A CZ  1 
ATOM   1798 O OH  . TYR A 1 259 ? 15.49621  16.68079  13.20551 1.000 83.07189  ? 282 TYR A OH  1 
ATOM   1799 N N   . GLY A 1 260 ? 12.05597  21.86054  7.20624  1.000 47.47176  ? 283 GLY A N   1 
ATOM   1800 C CA  . GLY A 1 260 ? 11.72059  22.80909  6.15185  1.000 41.00039  ? 283 GLY A CA  1 
ATOM   1801 C C   . GLY A 1 260 ? 11.04987  24.05554  6.69063  1.000 52.31506  ? 283 GLY A C   1 
ATOM   1802 O O   . GLY A 1 260 ? 11.36217  25.17453  6.28056  1.000 61.45162  ? 283 GLY A O   1 
ATOM   1803 N N   . SER A 1 261 ? 10.07965  23.87799  7.58484  1.000 59.04142  ? 284 SER A N   1 
ATOM   1804 C CA  . SER A 1 261 ? 9.37786   25.03174  8.13297  1.000 42.21209  ? 284 SER A CA  1 
ATOM   1805 C C   . SER A 1 261 ? 10.31570  25.88103  8.98652  1.000 45.14138  ? 284 SER A C   1 
ATOM   1806 O O   . SER A 1 261 ? 10.28596  27.11576  8.91085  1.000 47.56630  ? 284 SER A O   1 
ATOM   1807 C CB  . SER A 1 261 ? 8.16851   24.57347  8.94842  1.000 42.44985  ? 284 SER A CB  1 
ATOM   1808 O OG  . SER A 1 261 ? 7.54085   25.66760  9.59668  1.000 54.68593  ? 284 SER A OG  1 
ATOM   1809 N N   . THR A 1 262 ? 11.17163  25.23172  9.78410  1.000 36.18916  ? 285 THR A N   1 
ATOM   1810 C CA  . THR A 1 262 ? 12.16845  25.94863  10.57913 1.000 42.72378  ? 285 THR A CA  1 
ATOM   1811 C C   . THR A 1 262 ? 13.07675  26.82027  9.71288  1.000 37.57839  ? 285 THR A C   1 
ATOM   1812 O O   . THR A 1 262 ? 13.27053  28.00589  10.00820 1.000 44.56099  ? 285 THR A O   1 
ATOM   1813 C CB  . THR A 1 262 ? 13.00024  24.95376  11.39399 1.000 46.59963  ? 285 THR A CB  1 
ATOM   1814 O OG1 . THR A 1 262 ? 12.14504  24.21804  12.27926 1.000 39.02195  ? 285 THR A OG1 1 
ATOM   1815 C CG2 . THR A 1 262 ? 14.05127  25.68579  12.21443 1.000 45.02743  ? 285 THR A CG2 1 
ATOM   1816 N N   . VAL A 1 263 ? 13.65118  26.25330  8.64493  1.000 45.76278  ? 286 VAL A N   1 
ATOM   1817 C CA  . VAL A 1 263 ? 14.52952  27.03625  7.76926  1.000 49.40409  ? 286 VAL A CA  1 
ATOM   1818 C C   . VAL A 1 263 ? 13.79331  28.26598  7.23539  1.000 43.94212  ? 286 VAL A C   1 
ATOM   1819 O O   . VAL A 1 263 ? 14.29912  29.39183  7.31947  1.000 47.15327  ? 286 VAL A O   1 
ATOM   1820 C CB  . VAL A 1 263 ? 15.15935  26.16581  6.65644  1.000 48.76521  ? 286 VAL A CB  1 
ATOM   1821 C CG1 . VAL A 1 263 ? 15.80716  24.91772  7.25782  1.000 55.28121  ? 286 VAL A CG1 1 
ATOM   1822 C CG2 . VAL A 1 263 ? 14.19312  25.79047  5.54478  1.000 60.74667  ? 286 VAL A CG2 1 
ATOM   1823 N N   . GLY A 1 264 ? 12.60184  28.07327  6.66080  1.000 41.83453  ? 287 GLY A N   1 
ATOM   1824 C CA  . GLY A 1 264 ? 11.85570  29.21228  6.14843  1.000 32.00608  ? 287 GLY A CA  1 
ATOM   1825 C C   . GLY A 1 264 ? 11.61303  30.25657  7.22133  1.000 48.85157  ? 287 GLY A C   1 
ATOM   1826 O O   . GLY A 1 264 ? 11.77134  31.45643  6.97928  1.000 49.62164  ? 287 GLY A O   1 
ATOM   1827 N N   . HIS A 1 265 ? 11.26121  29.81562  8.43337  1.000 58.52056  ? 288 HIS A N   1 
ATOM   1828 C CA  . HIS A 1 265 ? 10.83856  30.76249  9.45914  1.000 39.53011  ? 288 HIS A CA  1 
ATOM   1829 C C   . HIS A 1 265 ? 12.02832  31.56361  9.96221  1.000 46.17692  ? 288 HIS A C   1 
ATOM   1830 O O   . HIS A 1 265 ? 11.88486  32.74615  10.29296 1.000 53.30547  ? 288 HIS A O   1 
ATOM   1831 C CB  . HIS A 1 265 ? 10.15005  30.04443  10.61840 1.000 35.62419  ? 288 HIS A CB  1 
ATOM   1832 C CG  . HIS A 1 265 ? 8.68403   29.82985  10.40921 1.000 39.60654  ? 288 HIS A CG  1 
ATOM   1833 N ND1 . HIS A 1 265 ? 8.15684   28.62722  9.99006  1.000 43.36382  ? 288 HIS A ND1 1 
ATOM   1834 C CD2 . HIS A 1 265 ? 7.63237   30.66884  10.56359 1.000 34.65408  ? 288 HIS A CD2 1 
ATOM   1835 C CE1 . HIS A 1 265 ? 6.84337   28.73513  9.89477  1.000 48.01076  ? 288 HIS A CE1 1 
ATOM   1836 N NE2 . HIS A 1 265 ? 6.49973   29.96402  10.23765 1.000 31.04774  ? 288 HIS A NE2 1 
ATOM   1837 N N   . THR A 1 266 ? 13.20941  30.94115  10.01308 1.000 45.43309  ? 289 THR A N   1 
ATOM   1838 C CA  . THR A 1 266 ? 14.39675  31.65034  10.47194 1.000 46.13554  ? 289 THR A CA  1 
ATOM   1839 C C   . THR A 1 266 ? 14.81580  32.70374  9.45715  1.000 40.43210  ? 289 THR A C   1 
ATOM   1840 O O   . THR A 1 266 ? 15.34233  33.75651  9.83658  1.000 45.16706  ? 289 THR A O   1 
ATOM   1841 C CB  . THR A 1 266 ? 15.53750  30.66578  10.72809 1.000 46.39735  ? 289 THR A CB  1 
ATOM   1842 O OG1 . THR A 1 266 ? 15.01429  29.47653  11.33431 1.000 61.79401  ? 289 THR A OG1 1 
ATOM   1843 C CG2 . THR A 1 266 ? 16.57217  31.28148  11.65593 1.000 60.88136  ? 289 THR A CG2 1 
ATOM   1844 N N   . ILE A 1 267 ? 14.59153  32.43794  8.16860  1.000 42.78075  ? 290 ILE A N   1 
ATOM   1845 C CA  . ILE A 1 267 ? 14.92080  33.41599  7.13345  1.000 46.83220  ? 290 ILE A CA  1 
ATOM   1846 C C   . ILE A 1 267 ? 14.10267  34.68199  7.34827  1.000 42.55880  ? 290 ILE A C   1 
ATOM   1847 O O   . ILE A 1 267 ? 14.64685  35.78107  7.51148  1.000 57.13682  ? 290 ILE A O   1 
ATOM   1848 C CB  . ILE A 1 267 ? 14.68612  32.82651  5.73288  1.000 52.32306  ? 290 ILE A CB  1 
ATOM   1849 C CG1 . ILE A 1 267 ? 15.73541  31.75710  5.42246  1.000 52.45910  ? 290 ILE A CG1 1 
ATOM   1850 C CG2 . ILE A 1 267 ? 14.71495  33.93216  4.68681  1.000 37.78331  ? 290 ILE A CG2 1 
ATOM   1851 C CD1 . ILE A 1 267 ? 15.52083  31.05997  4.09692  1.000 34.30901  ? 290 ILE A CD1 1 
ATOM   1852 N N   . ILE A 1 268 ? 12.77431  34.53878  7.35293  1.000 40.79292  ? 291 ILE A N   1 
ATOM   1853 C CA  . ILE A 1 268 ? 11.89323  35.69291  7.47058  1.000 49.25854  ? 291 ILE A CA  1 
ATOM   1854 C C   . ILE A 1 268 ? 11.97593  36.29359  8.87110  1.000 51.18308  ? 291 ILE A C   1 
ATOM   1855 O O   . ILE A 1 268 ? 11.60346  37.45733  9.06529  1.000 42.83221  ? 291 ILE A O   1 
ATOM   1856 C CB  . ILE A 1 268 ? 10.44815  35.32908  7.08310  1.000 44.72370  ? 291 ILE A CB  1 
ATOM   1857 C CG1 . ILE A 1 268 ? 9.83979   34.33762  8.07202  1.000 50.33211  ? 291 ILE A CG1 1 
ATOM   1858 C CG2 . ILE A 1 268 ? 10.40621  34.75845  5.67345  1.000 44.14967  ? 291 ILE A CG2 1 
ATOM   1859 C CD1 . ILE A 1 268 ? 8.41235   33.97266  7.73040  1.000 44.08893  ? 291 ILE A CD1 1 
ATOM   1860 N N   . ASP A 1 269 ? 12.45669  35.52707  9.85738  1.000 46.52045  ? 292 ASP A N   1 
ATOM   1861 C CA  . ASP A 1 269 ? 12.77130  36.10960  11.16123 1.000 41.07243  ? 292 ASP A CA  1 
ATOM   1862 C C   . ASP A 1 269 ? 13.87633  37.15345  11.03511 1.000 50.10177  ? 292 ASP A C   1 
ATOM   1863 O O   . ASP A 1 269 ? 13.77303  38.25265  11.59279 1.000 53.08403  ? 292 ASP A O   1 
ATOM   1864 C CB  . ASP A 1 269 ? 13.17740  35.01261  12.14556 1.000 41.37162  ? 292 ASP A CB  1 
ATOM   1865 C CG  . ASP A 1 269 ? 11.98432  34.33222  12.79715 1.000 53.41216  ? 292 ASP A CG  1 
ATOM   1866 O OD1 . ASP A 1 269 ? 10.84241  34.81491  12.62790 1.000 69.72865  ? 292 ASP A OD1 1 
ATOM   1867 O OD2 . ASP A 1 269 ? 12.19474  33.30844  13.48051 1.000 48.95928  ? 292 ASP A OD2 1 
ATOM   1868 N N   . LEU A 1 270 ? 14.95570  36.80505  10.32780 1.000 61.32350  ? 293 LEU A N   1 
ATOM   1869 C CA  . LEU A 1 270 ? 16.07059  37.72019  10.10933 1.000 60.99864  ? 293 LEU A CA  1 
ATOM   1870 C C   . LEU A 1 270 ? 15.56410  38.99836  9.45086  1.000 52.63047  ? 293 LEU A C   1 
ATOM   1871 O O   . LEU A 1 270 ? 15.97664  40.10655  9.81874  1.000 59.59413  ? 293 LEU A O   1 
ATOM   1872 C CB  . LEU A 1 270 ? 17.16448  37.03022  9.30323  1.000 49.57336  ? 293 LEU A CB  1 
ATOM   1873 C CG  . LEU A 1 270 ? 17.91544  36.03630  10.22373 1.000 54.08967  ? 293 LEU A CG  1 
ATOM   1874 C CD1 . LEU A 1 270 ? 18.73658  35.04092  9.40374  1.000 55.59131  ? 293 LEU A CD1 1 
ATOM   1875 C CD2 . LEU A 1 270 ? 18.77627  36.70369  11.34108 1.000 62.85411  ? 293 LEU A CD2 1 
ATOM   1876 N N   . MET A 1 271 ? 14.61929  38.85847  8.51244  1.000 28.91810  ? 294 MET A N   1 
ATOM   1877 C CA  . MET A 1 271 ? 14.06387  40.01785  7.81916  1.000 32.78855  ? 294 MET A CA  1 
ATOM   1878 C C   . MET A 1 271 ? 13.19772  40.83750  8.76191  1.000 42.18712  ? 294 MET A C   1 
ATOM   1879 O O   . MET A 1 271 ? 13.37129  42.05706  8.87792  1.000 39.38009  ? 294 MET A O   1 
ATOM   1880 C CB  . MET A 1 271 ? 13.17745  39.56331  6.65427  1.000 49.96050  ? 294 MET A CB  1 
ATOM   1881 C CG  . MET A 1 271 ? 13.80758  38.80497  5.50612  1.000 52.16539  ? 294 MET A CG  1 
ATOM   1882 S SD  . MET A 1 271 ? 12.51128  38.43258  4.30831  1.000 53.47591  ? 294 MET A SD  1 
ATOM   1883 C CE  . MET A 1 271 ? 12.74299  39.82347  3.19587  1.000 56.54318  ? 294 MET A CE  1 
ATOM   1884 N N   . SER A 1 272 ? 12.26317  40.18363  9.44324  1.000 47.96598  ? 295 SER A N   1 
ATOM   1885 C CA  . SER A 1 272 ? 11.21657  40.87557  10.18033 1.000 36.36950  ? 295 SER A CA  1 
ATOM   1886 C C   . SER A 1 272 ? 11.77690  41.52437  11.43587 1.000 35.33778  ? 295 SER A C   1 
ATOM   1887 O O   . SER A 1 272 ? 11.26592  42.54386  11.89329 1.000 30.44366  ? 295 SER A O   1 
ATOM   1888 C CB  . SER A 1 272 ? 10.08236  39.90968  10.54300 1.000 33.37324  ? 295 SER A CB  1 
ATOM   1889 O OG  . SER A 1 272 ? 10.54979  38.85867  11.37649 1.000 44.21541  ? 295 SER A OG  1 
ATOM   1890 N N   . LYS A 1 273 A 12.83655  40.93277  11.97925 1.000 31.51727  ? 296 LYS A N   1 
ATOM   1891 C CA  . LYS A 1 273 A 13.37968  41.35821  13.29904 1.000 32.70901  ? 296 LYS A CA  1 
ATOM   1892 C C   . LYS A 1 273 A 14.77094  41.97194  13.11755 1.000 45.01040  ? 296 LYS A C   1 
ATOM   1893 O O   . LYS A 1 273 A 14.87945  43.21342  13.19949 1.000 44.10860  ? 296 LYS A O   1 
ATOM   1894 C CB  . LYS A 1 273 A 13.45829  40.17090  14.25820 1.000 33.95861  ? 296 LYS A CB  1 
ATOM   1895 C CG  . LYS A 1 273 A 12.13449  39.46052  14.47629 1.000 41.49616  ? 296 LYS A CG  1 
ATOM   1896 C CD  . LYS A 1 273 A 12.30293  38.01373  14.89850 1.000 52.29066  ? 296 LYS A CD  1 
ATOM   1897 C CE  . LYS A 1 273 A 11.34351  37.62417  15.99874 1.000 47.09477  ? 296 LYS A CE  1 
ATOM   1898 N NZ  . LYS A 1 273 A 10.08105  37.07504  15.45742 1.000 45.50923  ? 296 LYS A NZ  1 
ATOM   1899 N N   . ASN A 1 274 ? 15.77957  41.13168  12.90054 1.000 48.31365  ? 297 ASN A N   1 
ATOM   1900 C CA  . ASN A 1 274 ? 17.17334  41.55897  12.82348 1.000 44.90466  ? 297 ASN A CA  1 
ATOM   1901 C C   . ASN A 1 274 ? 17.36853  42.70504  11.83820 1.000 38.97217  ? 297 ASN A C   1 
ATOM   1902 O O   . ASN A 1 274 ? 17.85982  43.76804  12.22365 1.000 42.15271  ? 297 ASN A O   1 
ATOM   1903 C CB  . ASN A 1 274 ? 18.05132  40.36788  12.46985 1.000 47.77974  ? 297 ASN A CB  1 
ATOM   1904 C CG  . ASN A 1 274 ? 17.94064  39.25622  13.49528 1.000 61.39387  ? 297 ASN A CG  1 
ATOM   1905 O OD1 . ASN A 1 274 ? 17.03155  38.42676  13.43188 1.000 62.23880  ? 297 ASN A OD1 1 
ATOM   1906 N ND2 . ASN A 1 274 ? 18.85853  39.24321  14.45795 1.000 53.52030  ? 297 ASN A ND2 1 
ATOM   1907 N N   . CYS A 1 275 ? 16.99801  42.49747  10.57044 1.000 38.27673  ? 298 CYS A N   1 
ATOM   1908 C CA  . CYS A 1 275 ? 17.30588  43.50259  9.55546  1.000 36.91387  ? 298 CYS A CA  1 
ATOM   1909 C C   . CYS A 1 275 ? 16.45515  44.74148  9.78678  1.000 44.29546  ? 298 CYS A C   1 
ATOM   1910 O O   . CYS A 1 275 ? 16.92990  45.87353  9.63606  1.000 55.05648  ? 298 CYS A O   1 
ATOM   1911 C CB  . CYS A 1 275 ? 17.07243  42.94672  8.15084  1.000 31.29800  ? 298 CYS A CB  1 
ATOM   1912 S SG  . CYS A 1 275 ? 18.11031  41.53512  7.70826  1.000 54.83637  ? 298 CYS A SG  1 
ATOM   1913 N N   . TRP A 1 276 ? 15.18593  44.53244  10.13776 1.000 45.39079  ? 299 TRP A N   1 
ATOM   1914 C CA  . TRP A 1 276 ? 14.25218  45.63125  10.34551 1.000 39.65609  ? 299 TRP A CA  1 
ATOM   1915 C C   . TRP A 1 276 ? 14.70414  46.44230  11.55919 1.000 29.59077  ? 299 TRP A C   1 
ATOM   1916 O O   . TRP A 1 276 ? 14.71421  47.67861  11.53160 1.000 37.65265  ? 299 TRP A O   1 
ATOM   1917 C CB  . TRP A 1 276 ? 12.83775  45.06176  10.50069 1.000 38.42277  ? 299 TRP A CB  1 
ATOM   1918 C CG  . TRP A 1 276 ? 11.72310  46.05407  10.51430 1.000 39.31657  ? 299 TRP A CG  1 
ATOM   1919 C CD1 . TRP A 1 276 ? 10.99507  46.47769  9.43574  1.000 31.67800  ? 299 TRP A CD1 1 
ATOM   1920 C CD2 . TRP A 1 276 ? 11.17557  46.71985  11.65445 1.000 41.38160  ? 299 TRP A CD2 1 
ATOM   1921 N NE1 . TRP A 1 276 ? 10.04063  47.38132  9.83569  1.000 40.35388  ? 299 TRP A NE1 1 
ATOM   1922 C CE2 . TRP A 1 276 ? 10.13050  47.54739  11.19351 1.000 40.27732  ? 299 TRP A CE2 1 
ATOM   1923 C CE3 . TRP A 1 276 ? 11.47453  46.70745  13.01842 1.000 31.19811  ? 299 TRP A CE3 1 
ATOM   1924 C CZ2 . TRP A 1 276 ? 9.38280   48.35045  12.05035 1.000 35.16510  ? 299 TRP A CZ2 1 
ATOM   1925 C CZ3 . TRP A 1 276 ? 10.73154  47.50426  13.86565 1.000 39.59997  ? 299 TRP A CZ3 1 
ATOM   1926 C CH2 . TRP A 1 276 ? 9.69767   48.31471  13.37945 1.000 37.24825  ? 299 TRP A CH2 1 
ATOM   1927 N N   . GLY A 1 277 ? 15.08214  45.73886  12.63741 1.000 38.34279  ? 300 GLY A N   1 
ATOM   1928 C CA  . GLY A 1 277 ? 15.61800  46.39042  13.82976 1.000 52.99456  ? 300 GLY A CA  1 
ATOM   1929 C C   . GLY A 1 277 ? 16.88520  47.17617  13.52944 1.000 52.98615  ? 300 GLY A C   1 
ATOM   1930 O O   . GLY A 1 277 ? 17.07330  48.28237  14.04300 1.000 53.54225  ? 300 GLY A O   1 
ATOM   1931 N N   . LEU A 1 278 ? 17.77380  46.61176  12.69476 1.000 63.35616  ? 301 LEU A N   1 
ATOM   1932 C CA  . LEU A 1 278 ? 18.96819  47.34034  12.25290 1.000 50.82622  ? 301 LEU A CA  1 
ATOM   1933 C C   . LEU A 1 278 ? 18.61003  48.64998  11.60392 1.000 50.63519  ? 301 LEU A C   1 
ATOM   1934 O O   . LEU A 1 278 ? 19.15895  49.69990  11.95896 1.000 57.71547  ? 301 LEU A O   1 
ATOM   1935 C CB  . LEU A 1 278 ? 19.81307  46.52181  11.27419 1.000 48.03120  ? 301 LEU A CB  1 
ATOM   1936 C CG  . LEU A 1 278 ? 21.32811  46.47058  11.50264 1.000 57.69473  ? 301 LEU A CG  1 
ATOM   1937 C CD1 . LEU A 1 278 ? 21.79181  46.37891  12.92366 1.000 66.57557  ? 301 LEU A CD1 1 
ATOM   1938 C CD2 . LEU A 1 278 ? 21.91653  45.32431  10.66868 1.000 63.08136  ? 301 LEU A CD2 1 
ATOM   1939 N N   . LEU A 1 279 ? 17.69486  48.60872  10.64733 1.000 43.11623  ? 302 LEU A N   1 
ATOM   1940 C CA  . LEU A 1 279 ? 17.27966  49.83348  9.99270  1.000 42.79978  ? 302 LEU A CA  1 
ATOM   1941 C C   . LEU A 1 279 ? 16.68916  50.78767  11.01792 1.000 50.87729  ? 302 LEU A C   1 
ATOM   1942 O O   . LEU A 1 279 ? 16.95263  51.99503  10.97267 1.000 53.01249  ? 302 LEU A O   1 
ATOM   1943 C CB  . LEU A 1 279 ? 16.27934  49.51701  8.88710  1.000 39.71597  ? 302 LEU A CB  1 
ATOM   1944 C CG  . LEU A 1 279 ? 16.85637  48.92692  7.60290  1.000 46.71096  ? 302 LEU A CG  1 
ATOM   1945 C CD1 . LEU A 1 279 ? 15.73102  48.63715  6.62071  1.000 42.15529  ? 302 LEU A CD1 1 
ATOM   1946 C CD2 . LEU A 1 279 ? 17.88248  49.87446  7.00023  1.000 45.59518  ? 302 LEU A CD2 1 
ATOM   1947 N N   . GLY A 1 280 ? 15.90129  50.26322  11.96369 1.000 41.12936  ? 303 GLY A N   1 
ATOM   1948 C CA  . GLY A 1 280 ? 15.24260  51.13880  12.91884 1.000 39.40724  ? 303 GLY A CA  1 
ATOM   1949 C C   . GLY A 1 280 ? 16.24164  51.88496  13.77265 1.000 45.88038  ? 303 GLY A C   1 
ATOM   1950 O O   . GLY A 1 280 ? 16.07174  53.07741  14.04121 1.000 51.45103  ? 303 GLY A O   1 
ATOM   1951 N N   . HIS A 1 281 ? 17.30212  51.20049  14.20201 1.000 49.03720  ? 304 HIS A N   1 
ATOM   1952 C CA  . HIS A 1 281 ? 18.35952  51.89319  14.92204 1.000 61.44584  ? 304 HIS A CA  1 
ATOM   1953 C C   . HIS A 1 281 ? 18.98049  52.94534  14.01355 1.000 51.37680  ? 304 HIS A C   1 
ATOM   1954 O O   . HIS A 1 281 ? 19.14027  54.10793  14.40075 1.000 48.66828  ? 304 HIS A O   1 
ATOM   1955 C CB  . HIS A 1 281 ? 19.40642  50.89590  15.41641 1.000 62.02838  ? 304 HIS A CB  1 
ATOM   1956 C CG  . HIS A 1 281 ? 20.48183  51.51787  16.24980 1.000 64.81501  ? 304 HIS A CG  1 
ATOM   1957 N ND1 . HIS A 1 281 ? 20.31848  51.79082  17.59133 1.000 52.97361  ? 304 HIS A ND1 1 
ATOM   1958 C CD2 . HIS A 1 281 ? 21.73388  51.92342  15.93245 1.000 71.92716  ? 304 HIS A CD2 1 
ATOM   1959 C CE1 . HIS A 1 281 ? 21.42479  52.33572  18.06476 1.000 76.14209  ? 304 HIS A CE1 1 
ATOM   1960 N NE2 . HIS A 1 281 ? 22.29899  52.42799  17.07851 1.000 91.60240  ? 304 HIS A NE2 1 
ATOM   1961 N N   . TYR A 1 282 ? 19.31228  52.54641  12.78204 1.000 52.73058  ? 305 TYR A N   1 
ATOM   1962 C CA  . TYR A 1 282 ? 19.86792  53.47252  11.80040 1.000 38.86961  ? 305 TYR A CA  1 
ATOM   1963 C C   . TYR A 1 282 ? 18.92827  54.65049  11.56121 1.000 42.64737  ? 305 TYR A C   1 
ATOM   1964 O O   . TYR A 1 282 ? 19.35688  55.80819  11.55787 1.000 47.04166  ? 305 TYR A O   1 
ATOM   1965 C CB  . TYR A 1 282 ? 20.15547  52.72918  10.49481 1.000 44.50237  ? 305 TYR A CB  1 
ATOM   1966 C CG  . TYR A 1 282 ? 20.77279  53.59007  9.41852  1.000 57.31133  ? 305 TYR A CG  1 
ATOM   1967 C CD1 . TYR A 1 282 ? 21.97956  54.24673  9.63242  1.000 64.28230  ? 305 TYR A CD1 1 
ATOM   1968 C CD2 . TYR A 1 282 ? 20.14983  53.74621  8.18622  1.000 56.91840  ? 305 TYR A CD2 1 
ATOM   1969 C CE1 . TYR A 1 282 ? 22.55011  55.03609  8.64684  1.000 47.38496  ? 305 TYR A CE1 1 
ATOM   1970 C CE2 . TYR A 1 282 ? 20.71031  54.53286  7.19524  1.000 48.36924  ? 305 TYR A CE2 1 
ATOM   1971 C CZ  . TYR A 1 282 ? 21.90998  55.17531  7.43018  1.000 56.84949  ? 305 TYR A CZ  1 
ATOM   1972 O OH  . TYR A 1 282 ? 22.46709  55.96152  6.44642  1.000 65.78159  ? 305 TYR A OH  1 
ATOM   1973 N N   . LEU A 1 283 ? 17.64120  54.37650  11.33079 1.000 53.45614  ? 306 LEU A N   1 
ATOM   1974 C CA  . LEU A 1 283 ? 16.70024  55.47040  11.09944 1.000 40.21269  ? 306 LEU A CA  1 
ATOM   1975 C C   . LEU A 1 283 ? 16.69281  56.44163  12.27248 1.000 37.01445  ? 306 LEU A C   1 
ATOM   1976 O O   . LEU A 1 283 ? 16.70833  57.66241  12.07713 1.000 50.85923  ? 306 LEU A O   1 
ATOM   1977 C CB  . LEU A 1 283 ? 15.28925  54.93007  10.85665 1.000 42.60013  ? 306 LEU A CB  1 
ATOM   1978 C CG  . LEU A 1 283 ? 14.20184  56.00367  10.68645 1.000 26.93555  ? 306 LEU A CG  1 
ATOM   1979 C CD1 . LEU A 1 283 ? 14.54742  56.95995  9.55307  1.000 55.05839  ? 306 LEU A CD1 1 
ATOM   1980 C CD2 . LEU A 1 283 ? 12.82554  55.39271  10.47361 1.000 33.48656  ? 306 LEU A CD2 1 
ATOM   1981 N N   . ARG A 1 284 ? 16.68451  55.91302  13.50037 1.000 51.90862  ? 307 ARG A N   1 
ATOM   1982 C CA  . ARG A 1 284 ? 16.60933  56.76092  14.68714 1.000 44.72526  ? 307 ARG A CA  1 
ATOM   1983 C C   . ARG A 1 284 ? 17.86158  57.61914  14.84969 1.000 57.33582  ? 307 ARG A C   1 
ATOM   1984 O O   . ARG A 1 284 ? 17.76648  58.78103  15.26430 1.000 50.40019  ? 307 ARG A O   1 
ATOM   1985 C CB  . ARG A 1 284 ? 16.35299  55.89181  15.91488 1.000 36.85145  ? 307 ARG A CB  1 
ATOM   1986 C CG  . ARG A 1 284 ? 14.89122  55.49601  16.02169 1.000 36.44301  ? 307 ARG A CG  1 
ATOM   1987 C CD  . ARG A 1 284 ? 14.65053  54.34652  16.98117 1.000 49.92475  ? 307 ARG A CD  1 
ATOM   1988 N NE  . ARG A 1 284 ? 13.24173  54.26260  17.34820 1.000 38.34703  ? 307 ARG A NE  1 
ATOM   1989 C CZ  . ARG A 1 284 ? 12.76222  53.49926  18.31999 1.000 44.09519  ? 307 ARG A CZ  1 
ATOM   1990 N NH1 . ARG A 1 284 ? 13.55288  52.72000  19.04061 1.000 51.03932  ? 307 ARG A NH1 1 
ATOM   1991 N NH2 . ARG A 1 284 ? 11.45597  53.51526  18.57245 1.000 43.38531  ? 307 ARG A NH2 1 
ATOM   1992 N N   . VAL A 1 285 ? 19.04210  57.07287  14.53038 1.000 54.85821  ? 308 VAL A N   1 
ATOM   1993 C CA  . VAL A 1 285 ? 20.25902  57.88605  14.56276 1.000 46.40714  ? 308 VAL A CA  1 
ATOM   1994 C C   . VAL A 1 285 ? 20.11896  59.03862  13.57574 1.000 47.73906  ? 308 VAL A C   1 
ATOM   1995 O O   . VAL A 1 285 ? 20.46261  60.18621  13.88662 1.000 63.96453  ? 308 VAL A O   1 
ATOM   1996 C CB  . VAL A 1 285 ? 21.54281  57.04920  14.34530 1.000 50.55957  ? 308 VAL A CB  1 
ATOM   1997 C CG1 . VAL A 1 285 ? 21.54612  55.80642  15.23611 1.000 48.96833  ? 308 VAL A CG1 1 
ATOM   1998 C CG2 . VAL A 1 285 ? 21.81345  56.71096  12.88883 1.000 55.17137  ? 308 VAL A CG2 1 
ATOM   1999 N N   . LEU A 1 286 ? 19.61269  58.75196  12.37008 1.000 51.47664  ? 309 LEU A N   1 
ATOM   2000 C CA  . LEU A 1 286 ? 19.49911  59.78572  11.34776 1.000 49.71358  ? 309 LEU A CA  1 
ATOM   2001 C C   . LEU A 1 286 ? 18.52938  60.86350  11.80855 1.000 44.75606  ? 309 LEU A C   1 
ATOM   2002 O O   . LEU A 1 286 ? 18.76500  62.05720  11.58509 1.000 59.36330  ? 309 LEU A O   1 
ATOM   2003 C CB  . LEU A 1 286 ? 19.02767  59.16552  10.03266 1.000 53.00105  ? 309 LEU A CB  1 
ATOM   2004 C CG  . LEU A 1 286 ? 19.99571  59.10925  8.85135  1.000 60.52000  ? 309 LEU A CG  1 
ATOM   2005 C CD1 . LEU A 1 286 ? 21.22875  58.29492  9.19922  1.000 59.79799  ? 309 LEU A CD1 1 
ATOM   2006 C CD2 . LEU A 1 286 ? 19.29136  58.51961  7.63836  1.000 51.84171  ? 309 LEU A CD2 1 
ATOM   2007 N N   . ILE A 1 287 ? 17.42310  60.46043  12.43898 1.000 37.28081  ? 310 ILE A N   1 
ATOM   2008 C CA  . ILE A 1 287 ? 16.46290  61.43738  12.94238 1.000 47.01081  ? 310 ILE A CA  1 
ATOM   2009 C C   . ILE A 1 287 ? 17.13940  62.29136  14.00688 1.000 47.83524  ? 310 ILE A C   1 
ATOM   2010 O O   . ILE A 1 287 ? 16.93999  63.51065  14.07821 1.000 57.11673  ? 310 ILE A O   1 
ATOM   2011 C CB  . ILE A 1 287 ? 15.20636  60.73340  13.48670 1.000 52.10384  ? 310 ILE A CB  1 
ATOM   2012 C CG1 . ILE A 1 287 ? 14.48172  59.99340  12.36078 1.000 52.30772  ? 310 ILE A CG1 1 
ATOM   2013 C CG2 . ILE A 1 287 ? 14.27918  61.73701  14.16357 1.000 52.65763  ? 310 ILE A CG2 1 
ATOM   2014 C CD1 . ILE A 1 287 ? 13.93182  60.90555  11.28605 1.000 50.49709  ? 310 ILE A CD1 1 
ATOM   2015 N N   . HIS A 1 288 ? 17.97151  61.65623  14.83770 1.000 38.44097  ? 311 HIS A N   1 
ATOM   2016 C CA  . HIS A 1 288 ? 18.61209  62.34148  15.95354 1.000 41.58634  ? 311 HIS A CA  1 
ATOM   2017 C C   . HIS A 1 288 ? 19.61856  63.35825  15.43432 1.000 41.10806  ? 311 HIS A C   1 
ATOM   2018 O O   . HIS A 1 288 ? 19.67555  64.49398  15.92126 1.000 45.66139  ? 311 HIS A O   1 
ATOM   2019 C CB  . HIS A 1 288 ? 19.28046  61.32339  16.87842 1.000 56.39437  ? 311 HIS A CB  1 
ATOM   2020 C CG  . HIS A 1 288 ? 19.76051  61.90398  18.17136 1.000 62.60836  ? 311 HIS A CG  1 
ATOM   2021 N ND1 . HIS A 1 288 ? 18.90163  62.31143  19.16941 1.000 71.16801  ? 311 HIS A ND1 1 
ATOM   2022 C CD2 . HIS A 1 288 ? 21.01121  62.14865  18.62820 1.000 61.02738  ? 311 HIS A CD2 1 
ATOM   2023 C CE1 . HIS A 1 288 ? 19.60262  62.77983  20.18648 1.000 64.70686  ? 311 HIS A CE1 1 
ATOM   2024 N NE2 . HIS A 1 288 ? 20.88528  62.69313  19.88311 1.000 74.94683  ? 311 HIS A NE2 1 
ATOM   2025 N N   . GLU A 1 289 ? 20.41497  62.96376  14.43798 1.000 54.42033  ? 312 GLU A N   1 
ATOM   2026 C CA  . GLU A 1 289 ? 21.38681  63.87630  13.84355 1.000 55.73241  ? 312 GLU A CA  1 
ATOM   2027 C C   . GLU A 1 289 ? 20.67526  65.08240  13.24267 1.000 55.09067  ? 312 GLU A C   1 
ATOM   2028 O O   . GLU A 1 289 ? 21.16939  66.21350  13.33137 1.000 56.82200  ? 312 GLU A O   1 
ATOM   2029 C CB  . GLU A 1 289 ? 22.22739  63.15550  12.78820 1.000 62.46683  ? 312 GLU A CB  1 
ATOM   2030 C CG  . GLU A 1 289 ? 23.37363  62.33205  13.36384 1.000 75.74314  ? 312 GLU A CG  1 
ATOM   2031 C CD  . GLU A 1 289 ? 24.05921  61.46668  12.32010 1.000 86.09443  ? 312 GLU A CD  1 
ATOM   2032 O OE1 . GLU A 1 289 ? 23.80658  61.67346  11.11328 1.000 96.81979  ? 312 GLU A OE1 1 
ATOM   2033 O OE2 . GLU A 1 289 ? 24.85205  60.58054  12.70584 1.000 67.16936  ? 312 GLU A OE2 1 
ATOM   2034 N N   . HIS A 1 290 ? 19.52489  64.85456  12.60147 1.000 46.59425  ? 313 HIS A N   1 
ATOM   2035 C CA  . HIS A 1 290 ? 18.79018  65.95365  11.98801 1.000 46.75586  ? 313 HIS A CA  1 
ATOM   2036 C C   . HIS A 1 290 ? 18.39987  66.97759  13.04436 1.000 54.44142  ? 313 HIS A C   1 
ATOM   2037 O O   . HIS A 1 290 ? 18.54414  68.18785  12.83304 1.000 54.23278  ? 313 HIS A O   1 
ATOM   2038 C CB  . HIS A 1 290 ? 17.55867  65.41900  11.25680 1.000 40.00758  ? 313 HIS A CB  1 
ATOM   2039 C CG  . HIS A 1 290 ? 16.73870  66.48448  10.59871 1.000 48.37153  ? 313 HIS A CG  1 
ATOM   2040 N ND1 . HIS A 1 290 ? 15.80873  67.23847  11.28231 1.000 61.61126  ? 313 HIS A ND1 1 
ATOM   2041 C CD2 . HIS A 1 290 ? 16.71474  66.92782  9.31935  1.000 52.63602  ? 313 HIS A CD2 1 
ATOM   2042 C CE1 . HIS A 1 290 ? 15.24361  68.09622  10.45118 1.000 77.22431  ? 313 HIS A CE1 1 
ATOM   2043 N NE2 . HIS A 1 290 ? 15.77619  67.92910  9.25391  1.000 75.63218  ? 313 HIS A NE2 1 
ATOM   2044 N N   . ILE A 1 291 ? 17.91296  66.51086  14.19456 1.000 47.76764  ? 314 ILE A N   1 
ATOM   2045 C CA  . ILE A 1 291 ? 17.42665  67.43604  15.20729 1.000 50.36101  ? 314 ILE A CA  1 
ATOM   2046 C C   . ILE A 1 291 ? 18.60527  68.13090  15.87685 1.000 51.66067  ? 314 ILE A C   1 
ATOM   2047 O O   . ILE A 1 291 ? 18.50611  69.29172  16.28807 1.000 56.88650  ? 314 ILE A O   1 
ATOM   2048 C CB  . ILE A 1 291 ? 16.53888  66.70055  16.23192 1.000 56.38381  ? 314 ILE A CB  1 
ATOM   2049 C CG1 . ILE A 1 291 ? 15.12660  66.50630  15.67815 1.000 33.83236  ? 314 ILE A CG1 1 
ATOM   2050 C CG2 . ILE A 1 291 ? 16.49422  67.44169  17.57390 1.000 83.57538  ? 314 ILE A CG2 1 
ATOM   2051 C CD1 . ILE A 1 291 ? 14.15255  66.02563  16.70513 1.000 51.37443  ? 314 ILE A CD1 1 
ATOM   2052 N N   . LEU A 1 292 ? 19.73613  67.43883  16.01558 1.000 57.94127  ? 315 LEU A N   1 
ATOM   2053 C CA  . LEU A 1 292 ? 20.90406  68.06670  16.62969 1.000 46.90385  ? 315 LEU A CA  1 
ATOM   2054 C C   . LEU A 1 292 ? 21.46918  69.17584  15.74703 1.000 56.49911  ? 315 LEU A C   1 
ATOM   2055 O O   . LEU A 1 292 ? 21.69037  70.30293  16.20479 1.000 68.05505  ? 315 LEU A O   1 
ATOM   2056 C CB  . LEU A 1 292 ? 21.96269  67.00876  16.93941 1.000 37.09031  ? 315 LEU A CB  1 
ATOM   2057 C CG  . LEU A 1 292 ? 21.61764  66.10404  18.13394 1.000 36.25216  ? 315 LEU A CG  1 
ATOM   2058 C CD1 . LEU A 1 292 ? 22.74759  65.12525  18.38759 1.000 49.05285  ? 315 LEU A CD1 1 
ATOM   2059 C CD2 . LEU A 1 292 ? 21.32896  66.94319  19.37483 1.000 34.46950  ? 315 LEU A CD2 1 
ATOM   2060 N N   . ILE A 1 293 ? 21.69286  68.87961  14.46940 1.000 51.72710  ? 316 ILE A N   1 
ATOM   2061 C CA  . ILE A 1 293 ? 22.23179  69.88665  13.56082 1.000 51.84754  ? 316 ILE A CA  1 
ATOM   2062 C C   . ILE A 1 293 ? 21.20764  70.97974  13.29017 1.000 51.66572  ? 316 ILE A C   1 
ATOM   2063 O O   . ILE A 1 293 ? 21.53387  72.16961  13.33582 1.000 61.13896  ? 316 ILE A O   1 
ATOM   2064 C CB  . ILE A 1 293 ? 22.70859  69.23271  12.25298 1.000 61.35327  ? 316 ILE A CB  1 
ATOM   2065 C CG1 . ILE A 1 293 ? 23.85904  68.25116  12.51258 1.000 47.12722  ? 316 ILE A CG1 1 
ATOM   2066 C CG2 . ILE A 1 293 ? 23.18123  70.32925  11.26481 1.000 68.67103  ? 316 ILE A CG2 1 
ATOM   2067 C CD1 . ILE A 1 293 ? 24.02310  67.20566  11.42609 1.000 65.82318  ? 316 ILE A CD1 1 
ATOM   2068 N N   . HIS A 1 294 ? 19.95290  70.59792  13.01929 1.000 59.60530  ? 317 HIS A N   1 
ATOM   2069 C CA  . HIS A 1 294 ? 18.94560  71.53456  12.52843 1.000 70.09983  ? 317 HIS A CA  1 
ATOM   2070 C C   . HIS A 1 294 ? 17.90203  71.95597  13.55192 1.000 59.80833  ? 317 HIS A C   1 
ATOM   2071 O O   . HIS A 1 294 ? 17.15746  72.90155  13.27885 1.000 63.68429  ? 317 HIS A O   1 
ATOM   2072 C CB  . HIS A 1 294 ? 18.20405  70.96232  11.30358 1.000 57.87026  ? 317 HIS A CB  1 
ATOM   2073 C CG  . HIS A 1 294 ? 19.10346  70.56869  10.17555 1.000 53.96138  ? 317 HIS A CG  1 
ATOM   2074 N ND1 . HIS A 1 294 ? 19.86453  69.42063  10.20392 1.000 64.77242  ? 317 HIS A ND1 1 
ATOM   2075 C CD2 . HIS A 1 294 ? 19.35745  71.16071  8.98464  1.000 65.52790  ? 317 HIS A CD2 1 
ATOM   2076 C CE1 . HIS A 1 294 ? 20.55479  69.32494  9.08219  1.000 75.83450  ? 317 HIS A CE1 1 
ATOM   2077 N NE2 . HIS A 1 294 ? 20.26482  70.36776  8.32495  1.000 91.46999  ? 317 HIS A NE2 1 
ATOM   2078 N N   . GLY A 1 295 ? 17.83582  71.31991  14.71237 1.000 69.77634  ? 318 GLY A N   1 
ATOM   2079 C CA  . GLY A 1 295 ? 16.70710  71.48903  15.61229 1.000 54.28035  ? 318 GLY A CA  1 
ATOM   2080 C C   . GLY A 1 295 ? 15.42939  70.83802  15.11183 1.000 74.29456  ? 318 GLY A C   1 
ATOM   2081 O O   . GLY A 1 295 ? 15.34780  70.27339  14.02100 1.000 90.18843  ? 318 GLY A O   1 
ATOM   2082 N N   . ASP A 1 296 ? 14.40762  70.93166  15.95884 1.000 73.91671  ? 319 ASP A N   1 
ATOM   2083 C CA  . ASP A 1 296 ? 13.09193  70.34459  15.71506 1.000 75.83589  ? 319 ASP A CA  1 
ATOM   2084 C C   . ASP A 1 296 ? 12.20239  71.43742  15.12948 1.000 84.13842  ? 319 ASP A C   1 
ATOM   2085 O O   . ASP A 1 296 ? 11.52802  72.17562  15.85412 1.000 94.70646  ? 319 ASP A O   1 
ATOM   2086 C CB  . ASP A 1 296 ? 12.52393  69.75610  17.00347 1.000 56.58890  ? 319 ASP A CB  1 
ATOM   2087 C CG  . ASP A 1 296 ? 11.33823  68.84603  16.76370 1.000 67.78158  ? 319 ASP A CG  1 
ATOM   2088 O OD1 . ASP A 1 296 ? 10.42961  69.24278  16.00844 1.000 84.98645  ? 319 ASP A OD1 1 
ATOM   2089 O OD2 . ASP A 1 296 ? 11.31509  67.73218  17.32521 1.000 62.28808  ? 319 ASP A OD2 1 
ATOM   2090 N N   . ILE A 1 297 ? 12.19404  71.52947  13.79914 1.000 75.82795  ? 320 ILE A N   1 
ATOM   2091 C CA  . ILE A 1 297 ? 11.36581  72.48702  13.07342 1.000 79.90242  ? 320 ILE A CA  1 
ATOM   2092 C C   . ILE A 1 297 ? 10.28722  71.70659  12.33567 1.000 92.70166  ? 320 ILE A C   1 
ATOM   2093 O O   . ILE A 1 297 ? 10.59620  70.77817  11.57762 1.000 84.35631  ? 320 ILE A O   1 
ATOM   2094 C CB  . ILE A 1 297 ? 12.20014  73.30859  12.07482 1.000 85.20817  ? 320 ILE A CB  1 
ATOM   2095 C CG1 . ILE A 1 297 ? 13.56353  73.66823  12.66516 1.000 90.83226  ? 320 ILE A CG1 1 
ATOM   2096 C CG2 . ILE A 1 297 ? 11.46439  74.58053  11.69163 1.000 91.71402  ? 320 ILE A CG2 1 
ATOM   2097 C CD1 . ILE A 1 297 ? 14.59659  74.02206  11.60361 1.000 66.50308  ? 320 ILE A CD1 1 
ATOM   2098 N N   . ARG A 1 298 ? 9.02699   72.06938  12.55809 1.000 104.49131 ? 321 ARG A N   1 
ATOM   2099 C CA  . ARG A 1 298 ? 7.92002   71.30384  12.01209 1.000 77.09889  ? 321 ARG A CA  1 
ATOM   2100 C C   . ARG A 1 298 ? 7.08620   72.13717  11.04961 1.000 82.67029  ? 321 ARG A C   1 
ATOM   2101 O O   . ARG A 1 298 ? 6.98451   73.36219  11.17858 1.000 102.74458 ? 321 ARG A O   1 
ATOM   2102 C CB  . ARG A 1 298 ? 6.98205   70.82298  13.12993 1.000 81.34169  ? 321 ARG A CB  1 
ATOM   2103 C CG  . ARG A 1 298 ? 6.89355   69.32829  13.34027 1.000 73.76621  ? 321 ARG A CG  1 
ATOM   2104 C CD  . ARG A 1 298 ? 7.87391   68.88778  14.40457 1.000 70.84597  ? 321 ARG A CD  1 
ATOM   2105 N NE  . ARG A 1 298 ? 8.11854   67.45200  14.37450 1.000 64.77686  ? 321 ARG A NE  1 
ATOM   2106 C CZ  . ARG A 1 298 ? 7.42073   66.56152  15.06684 1.000 77.24753  ? 321 ARG A CZ  1 
ATOM   2107 N NH1 . ARG A 1 298 ? 6.41454   66.92518  15.84750 1.000 91.93786  ? 321 ARG A NH1 1 
ATOM   2108 N NH2 . ARG A 1 298 ? 7.73269   65.27269  14.96595 1.000 64.92682  ? 321 ARG A NH2 1 
ATOM   2109 N N   . LYS A 1 299 ? 6.48326   71.44800  10.08229 1.000 86.39515  ? 322 LYS A N   1 
ATOM   2110 C CA  . LYS A 1 299 ? 5.51545   72.03374  9.16789  1.000 101.01162 ? 322 LYS A CA  1 
ATOM   2111 C C   . LYS A 1 299 ? 4.32028   71.09240  9.12302  1.000 84.14928  ? 322 LYS A C   1 
ATOM   2112 O O   . LYS A 1 299 ? 4.49435   69.87022  9.08353  1.000 84.15998  ? 322 LYS A O   1 
ATOM   2113 C CB  . LYS A 1 299 ? 6.11884   72.27177  7.76723  1.000 102.57619 ? 322 LYS A CB  1 
ATOM   2114 C CG  . LYS A 1 299 ? 5.90653   71.16886  6.73939  1.000 82.33088  ? 322 LYS A CG  1 
ATOM   2115 C CD  . LYS A 1 299 ? 5.92712   71.75034  5.33218  1.000 100.37202 ? 322 LYS A CD  1 
ATOM   2116 C CE  . LYS A 1 299 ? 6.29092   70.71392  4.27992  1.000 88.78342  ? 322 LYS A CE  1 
ATOM   2117 N NZ  . LYS A 1 299 ? 7.71261   70.28780  4.36541  1.000 85.51112  ? 322 LYS A NZ  1 
ATOM   2118 N N   . THR A 1 300 ? 3.10884   71.63977  9.16439  1.000 98.69401  ? 323 THR A N   1 
ATOM   2119 C CA  . THR A 1 300 ? 1.92901   70.78696  9.07299  1.000 95.99684  ? 323 THR A CA  1 
ATOM   2120 C C   . THR A 1 300 ? 1.60896   70.49800  7.61042  1.000 104.55323 ? 323 THR A C   1 
ATOM   2121 O O   . THR A 1 300 ? 1.31332   71.42532  6.84735  1.000 121.60812 ? 323 THR A O   1 
ATOM   2122 C CB  . THR A 1 300 ? 0.73653   71.44964  9.76101  1.000 111.38099 ? 323 THR A CB  1 
ATOM   2123 O OG1 . THR A 1 300 ? 0.38562   72.64790  9.05938  1.000 137.90572 ? 323 THR A OG1 1 
ATOM   2124 C CG2 . THR A 1 300 ? 1.07521   71.79215  11.20311 1.000 109.70545 ? 323 THR A CG2 1 
ATOM   2125 N N   . THR A 1 301 ? 1.66640   69.22712  7.21000  1.000 103.79755 ? 324 THR A N   1 
ATOM   2126 C CA  . THR A 1 301 ? 1.12031   68.80912  5.92688  1.000 100.63448 ? 324 THR A CA  1 
ATOM   2127 C C   . THR A 1 301 ? -0.10572  67.92846  6.13294  1.000 104.99442 ? 324 THR A C   1 
ATOM   2128 O O   . THR A 1 301 ? -0.12461  67.07595  7.02679  1.000 103.09639 ? 324 THR A O   1 
ATOM   2129 C CB  . THR A 1 301 ? 2.16575   68.07194  5.08399  1.000 87.59744  ? 324 THR A CB  1 
ATOM   2130 O OG1 . THR A 1 301 ? 2.21425   66.69634  5.47127  1.000 72.46231  ? 324 THR A OG1 1 
ATOM   2131 C CG2 . THR A 1 301 ? 3.53770   68.70328  5.25464  1.000 75.22157  ? 324 THR A CG2 1 
ATOM   2132 N N   . LYS A 1 302 ? -1.12584  68.12352  5.30202  1.000 103.70215 ? 325 LYS A N   1 
ATOM   2133 C CA  . LYS A 1 302 ? -2.35550  67.35405  5.41491  1.000 104.76379 ? 325 LYS A CA  1 
ATOM   2134 C C   . LYS A 1 302 ? -2.47768  66.47005  4.17814  1.000 110.87623 ? 325 LYS A C   1 
ATOM   2135 O O   . LYS A 1 302 ? -2.11518  66.88481  3.07250  1.000 104.89271 ? 325 LYS A O   1 
ATOM   2136 C CB  . LYS A 1 302 ? -3.58224  68.26363  5.65294  1.000 101.83587 ? 325 LYS A CB  1 
ATOM   2137 C CG  . LYS A 1 302 ? -4.19337  69.13104  4.53197  1.000 107.41253 ? 325 LYS A CG  1 
ATOM   2138 C CD  . LYS A 1 302 ? -4.87073  68.34632  3.41875  1.000 103.13117 ? 325 LYS A CD  1 
ATOM   2139 C CE  . LYS A 1 302 ? -5.52829  69.26029  2.39197  1.000 96.27911  ? 325 LYS A CE  1 
ATOM   2140 N NZ  . LYS A 1 302 ? -6.42496  68.51285  1.45846  1.000 100.97498 ? 325 LYS A NZ  1 
ATOM   2141 N N   . LEU A 1 303 ? -2.94895  65.24006  4.36714  1.000 108.46151 ? 326 LEU A N   1 
ATOM   2142 C CA  . LEU A 1 303 ? -3.00848  64.24949  3.29487  1.000 110.36099 ? 326 LEU A CA  1 
ATOM   2143 C C   . LEU A 1 303 ? -4.46547  63.86008  3.07439  1.000 118.13706 ? 326 LEU A C   1 
ATOM   2144 O O   . LEU A 1 303 ? -5.06032  63.17055  3.90900  1.000 125.24540 ? 326 LEU A O   1 
ATOM   2145 C CB  . LEU A 1 303 ? -2.16148  63.02476  3.63815  1.000 102.42796 ? 326 LEU A CB  1 
ATOM   2146 N N   . ASN A 1 304 ? -5.03068  64.27947  1.94489  1.000 119.21163 ? 327 ASN A N   1 
ATOM   2147 C CA  . ASN A 1 304 ? -6.42161  63.97461  1.61819  1.000 124.38293 ? 327 ASN A CA  1 
ATOM   2148 C C   . ASN A 1 304 ? -6.52554  62.82286  0.62183  1.000 112.19196 ? 327 ASN A C   1 
ATOM   2149 O O   . ASN A 1 304 ? -5.62027  62.60002  -0.18153 1.000 117.28679 ? 327 ASN A O   1 
ATOM   2150 C CB  . ASN A 1 304 ? -7.12087  65.21461  1.05812  1.000 108.47119 ? 327 ASN A CB  1 
ATOM   2151 N N   . THR A 1 308 ? -9.40983  58.85417  2.64080  1.000 112.53347 ? 331 THR A N   1 
ATOM   2152 C CA  . THR A 1 308 ? -9.32979  59.42337  3.98092  1.000 133.42827 ? 331 THR A CA  1 
ATOM   2153 C C   . THR A 1 308 ? -8.42035  60.64810  3.99828  1.000 138.92084 ? 331 THR A C   1 
ATOM   2154 O O   . THR A 1 308 ? -7.48678  60.74910  3.20217  1.000 133.49986 ? 331 THR A O   1 
ATOM   2155 C CB  . THR A 1 308 ? -8.81225  58.39271  5.00232  1.000 111.45968 ? 331 THR A CB  1 
ATOM   2156 N N   . GLU A 1 309 ? -8.70098  61.58043  4.90717  1.000 141.47021 ? 332 GLU A N   1 
ATOM   2157 C CA  . GLU A 1 309 ? -7.92161  62.80556  5.05526  1.000 126.80787 ? 332 GLU A CA  1 
ATOM   2158 C C   . GLU A 1 309 ? -7.19125  62.76271  6.39300  1.000 132.87881 ? 332 GLU A C   1 
ATOM   2159 O O   . GLU A 1 309 ? -7.82475  62.77725  7.45370  1.000 129.81824 ? 332 GLU A O   1 
ATOM   2160 C CB  . GLU A 1 309 ? -8.81865  64.03770  4.95649  1.000 114.73181 ? 332 GLU A CB  1 
ATOM   2161 N N   . ILE A 1 310 ? -5.86152  62.71185  6.33985  1.000 133.54856 ? 333 ILE A N   1 
ATOM   2162 C CA  . ILE A 1 310 ? -5.02300  62.63383  7.52992  1.000 122.67633 ? 333 ILE A CA  1 
ATOM   2163 C C   . ILE A 1 310 ? -4.03991  63.79742  7.51588  1.000 112.26025 ? 333 ILE A C   1 
ATOM   2164 O O   . ILE A 1 310 ? -3.63446  64.27872  6.45331  1.000 109.93241 ? 333 ILE A O   1 
ATOM   2165 C CB  . ILE A 1 310 ? -4.27619  61.28519  7.61966  1.000 124.73943 ? 333 ILE A CB  1 
ATOM   2166 C CG1 . ILE A 1 310 ? -3.83504  60.82602  6.22857  1.000 120.19556 ? 333 ILE A CG1 1 
ATOM   2167 C CG2 . ILE A 1 310 ? -5.15506  60.23024  8.27705  1.000 114.07781 ? 333 ILE A CG2 1 
ATOM   2168 C CD1 . ILE A 1 310 ? -2.73175  59.79274  6.24811  1.000 102.94760 ? 333 ILE A CD1 1 
ATOM   2169 N N   . GLU A 1 311 ? -3.64633  64.24106  8.70865  1.000 107.46055 ? 334 GLU A N   1 
ATOM   2170 C CA  . GLU A 1 311 ? -2.68445  65.32042  8.87268  1.000 99.77898  ? 334 GLU A CA  1 
ATOM   2171 C C   . GLU A 1 311 ? -1.45388  64.80163  9.60084  1.000 98.74966  ? 334 GLU A C   1 
ATOM   2172 O O   . GLU A 1 311 ? -1.55792  64.03629  10.56460 1.000 94.90845  ? 334 GLU A O   1 
ATOM   2173 C CB  . GLU A 1 311 ? -3.29194  66.51984  9.61567  1.000 92.45596  ? 334 GLU A CB  1 
ATOM   2174 C CG  . GLU A 1 311 ? -2.28949  67.32175  10.43361 1.000 103.51661 ? 334 GLU A CG  1 
ATOM   2175 C CD  . GLU A 1 311 ? -2.91291  68.52076  11.11628 1.000 113.54433 ? 334 GLU A CD  1 
ATOM   2176 O OE1 . GLU A 1 311 ? -2.15698  69.34701  11.67107 1.000 109.93660 ? 334 GLU A OE1 1 
ATOM   2177 O OE2 . GLU A 1 311 ? -4.15549  68.64833  11.08073 1.000 116.91008 ? 334 GLU A OE2 1 
ATOM   2178 N N   . VAL A 1 312 ? -0.28752  65.23929  9.13354  1.000 97.85074  ? 335 VAL A N   1 
ATOM   2179 C CA  . VAL A 1 312 ? 1.01235   64.83067  9.66778  1.000 74.32175  ? 335 VAL A CA  1 
ATOM   2180 C C   . VAL A 1 312 ? 1.90354   66.06307  9.75624  1.000 75.58820  ? 335 VAL A C   1 
ATOM   2181 O O   . VAL A 1 312 ? 1.88331   66.93056  8.87416  1.000 89.49084  ? 335 VAL A O   1 
ATOM   2182 C CB  . VAL A 1 312 ? 1.69646   63.71354  8.83868  1.000 69.47601  ? 335 VAL A CB  1 
ATOM   2183 C CG1 . VAL A 1 312 ? 0.71014   62.60577  8.48028  1.000 75.81874  ? 335 VAL A CG1 1 
ATOM   2184 C CG2 . VAL A 1 312 ? 2.37290   64.26412  7.58564  1.000 75.49382  ? 335 VAL A CG2 1 
ATOM   2185 N N   . GLU A 1 313 ? 2.64142   66.16036  10.86199 1.000 69.83317  ? 336 GLU A N   1 
ATOM   2186 C CA  . GLU A 1 313 ? 3.59806   67.24136  11.06923 1.000 85.88256  ? 336 GLU A CA  1 
ATOM   2187 C C   . GLU A 1 313 ? 4.96758   66.75702  10.62423 1.000 78.82091  ? 336 GLU A C   1 
ATOM   2188 O O   . GLU A 1 313 ? 5.67516   66.04562  11.34547 1.000 61.81290  ? 336 GLU A O   1 
ATOM   2189 C CB  . GLU A 1 313 ? 3.59303   67.72087  12.51656 1.000 65.11589  ? 336 GLU A CB  1 
ATOM   2190 C CG  . GLU A 1 313 ? 3.22063   69.20348  12.67396 1.000 89.57271  ? 336 GLU A CG  1 
ATOM   2191 C CD  . GLU A 1 313 ? 3.25564   69.65275  14.11749 1.000 107.45926 ? 336 GLU A CD  1 
ATOM   2192 O OE1 . GLU A 1 313 ? 3.55298   70.84435  14.37459 1.000 125.83299 ? 336 GLU A OE1 1 
ATOM   2193 O OE2 . GLU A 1 313 ? 2.91984   68.82876  14.98994 1.000 102.78770 ? 336 GLU A OE2 1 
ATOM   2194 N N   . THR A 1 314 ? 5.32958   67.19118  9.42074  1.000 80.67690  ? 337 THR A N   1 
ATOM   2195 C CA  . THR A 1 314 ? 6.59692   66.88180  8.78902  1.000 65.93842  ? 337 THR A CA  1 
ATOM   2196 C C   . THR A 1 314 ? 7.74134   67.68404  9.40139  1.000 73.88696  ? 337 THR A C   1 
ATOM   2197 O O   . THR A 1 314 ? 7.61366   68.87873  9.69270  1.000 78.14362  ? 337 THR A O   1 
ATOM   2198 C CB  . THR A 1 314 ? 6.48976   67.14627  7.28098  1.000 61.76675  ? 337 THR A CB  1 
ATOM   2199 O OG1 . THR A 1 314 ? 5.32091   66.50521  6.74876  1.000 80.79735  ? 337 THR A OG1 1 
ATOM   2200 C CG2 . THR A 1 314 ? 7.78522   66.74061  6.52945  1.000 62.38197  ? 337 THR A CG2 1 
ATOM   2201 N N   . LEU A 1 315 ? 8.86689   66.99893  9.59872  1.000 69.13224  ? 338 LEU A N   1 
ATOM   2202 C CA  . LEU A 1 315 ? 10.12400  67.64524  9.96621  1.000 64.93577  ? 338 LEU A CA  1 
ATOM   2203 C C   . LEU A 1 315 ? 10.77853  68.27717  8.74779  1.000 64.91963  ? 338 LEU A C   1 
ATOM   2204 O O   . LEU A 1 315 ? 10.88046  67.65761  7.68445  1.000 70.75266  ? 338 LEU A O   1 
ATOM   2205 C CB  . LEU A 1 315 ? 11.07698  66.64974  10.63367 1.000 50.26037  ? 338 LEU A CB  1 
ATOM   2206 C CG  . LEU A 1 315 ? 10.67716  66.18212  12.03759 1.000 78.59465  ? 338 LEU A CG  1 
ATOM   2207 C CD1 . LEU A 1 315 ? 11.26709  64.81799  12.33318 1.000 65.00687  ? 338 LEU A CD1 1 
ATOM   2208 C CD2 . LEU A 1 315 ? 11.13898  67.19754  13.07532 1.000 70.15959  ? 338 LEU A CD2 1 
ATOM   2209 N N   . VAL A 1 316 ? 11.22552  69.51765  8.92187  1.000 79.42972  ? 339 VAL A N   1 
ATOM   2210 C CA  . VAL A 1 316 ? 11.86513  70.28115  7.86200  1.000 85.40467  ? 339 VAL A CA  1 
ATOM   2211 C C   . VAL A 1 316 ? 13.24596  70.68448  8.35118  1.000 86.34201  ? 339 VAL A C   1 
ATOM   2212 O O   . VAL A 1 316 ? 13.61875  70.41789  9.50159  1.000 75.33313  ? 339 VAL A O   1 
ATOM   2213 C CB  . VAL A 1 316 ? 11.03977  71.52455  7.46842  1.000 89.95904  ? 339 VAL A CB  1 
ATOM   2214 C CG1 . VAL A 1 316 ? 9.72856   71.12583  6.81495  1.000 86.62901  ? 339 VAL A CG1 1 
ATOM   2215 C CG2 . VAL A 1 316 ? 10.77981  72.40581  8.68250  1.000 87.16868  ? 339 VAL A CG2 1 
ATOM   2216 N N   . GLU A 1 317 ? 14.01717  71.31576  7.47102  1.000 97.64012  ? 340 GLU A N   1 
ATOM   2217 C CA  . GLU A 1 317 ? 15.41079  71.60847  7.75733  1.000 96.00397  ? 340 GLU A CA  1 
ATOM   2218 C C   . GLU A 1 317 ? 15.67864  73.04050  8.19213  1.000 102.18681 ? 340 GLU A C   1 
ATOM   2219 O O   . GLU A 1 317 ? 16.61945  73.27317  8.96009  1.000 104.86670 ? 340 GLU A O   1 
ATOM   2220 C CB  . GLU A 1 317 ? 16.21155  71.32561  6.48411  1.000 89.07117  ? 340 GLU A CB  1 
ATOM   2221 C CG  . GLU A 1 317 ? 16.45610  69.85401  6.21615  1.000 104.09364 ? 340 GLU A CG  1 
ATOM   2222 C CD  . GLU A 1 317 ? 17.21292  69.62771  4.92272  1.000 114.52519 ? 340 GLU A CD  1 
ATOM   2223 O OE1 . GLU A 1 317 ? 16.89806  68.64500  4.21422  1.000 108.16361 ? 340 GLU A OE1 1 
ATOM   2224 O OE2 . GLU A 1 317 ? 18.10477  70.43815  4.60467  1.000 132.11110 ? 340 GLU A OE2 1 
ATOM   2225 N N   . ASP A 1 318 ? 14.88535  74.00431  7.73155  1.000 90.10663  ? 341 ASP A N   1 
ATOM   2226 C CA  . ASP A 1 318 ? 15.13485  75.40742  8.02543  1.000 109.23760 ? 341 ASP A CA  1 
ATOM   2227 C C   . ASP A 1 318 ? 13.81597  76.10738  8.31595  1.000 112.32162 ? 341 ASP A C   1 
ATOM   2228 O O   . ASP A 1 318 ? 12.73808  75.61351  7.97358  1.000 115.57596 ? 341 ASP A O   1 
ATOM   2229 C CB  . ASP A 1 318 ? 15.88722  76.09594  6.87981  1.000 112.63331 ? 341 ASP A CB  1 
ATOM   2230 C CG  . ASP A 1 318 ? 15.06895  76.18004  5.61488  1.000 110.11823 ? 341 ASP A CG  1 
ATOM   2231 O OD1 . ASP A 1 318 ? 14.35647  75.20104  5.30756  1.000 116.68766 ? 341 ASP A OD1 1 
ATOM   2232 O OD2 . ASP A 1 318 ? 15.14804  77.21679  4.92303  1.000 88.91712  ? 341 ASP A OD2 1 
ATOM   2233 N N   . GLU A 1 319 ? 13.91335  77.27336  8.95445  1.000 104.85823 ? 342 GLU A N   1 
ATOM   2234 C CA  . GLU A 1 319 ? 12.72576  77.97961  9.41431  1.000 109.77732 ? 342 GLU A CA  1 
ATOM   2235 C C   . GLU A 1 319 ? 11.97624  78.67048  8.28173  1.000 118.11260 ? 342 GLU A C   1 
ATOM   2236 O O   . GLU A 1 319 ? 10.88488  79.19972  8.51932  1.000 107.22929 ? 342 GLU A O   1 
ATOM   2237 C CB  . GLU A 1 319 ? 13.10277  79.00589  10.48637 1.000 86.13275  ? 342 GLU A CB  1 
ATOM   2238 N N   . ALA A 1 320 ? 12.52838  78.67573  7.06300  1.000 139.99905 ? 343 ALA A N   1 
ATOM   2239 C CA  . ALA A 1 320 ? 11.80158  79.17610  5.90005  1.000 149.73573 ? 343 ALA A CA  1 
ATOM   2240 C C   . ALA A 1 320 ? 10.54524  78.37088  5.60312  1.000 137.19431 ? 343 ALA A C   1 
ATOM   2241 O O   . ALA A 1 320 ? 9.74709   78.78621  4.75517  1.000 129.30266 ? 343 ALA A O   1 
ATOM   2242 C CB  . ALA A 1 320 ? 12.70860  79.18384  4.66874  1.000 150.79584 ? 343 ALA A CB  1 
ATOM   2243 N N   . GLU A 1 321 ? 10.35829  77.23482  6.26788  1.000 126.23803 ? 344 GLU A N   1 
ATOM   2244 C CA  . GLU A 1 321 ? 9.15087   76.42999  6.15860  1.000 131.99984 ? 344 GLU A CA  1 
ATOM   2245 C C   . GLU A 1 321 ? 8.59558   76.29947  7.56994  1.000 132.74126 ? 344 GLU A C   1 
ATOM   2246 O O   . GLU A 1 321 ? 9.26885   75.76671  8.45905  1.000 122.52033 ? 344 GLU A O   1 
ATOM   2247 C CB  . GLU A 1 321 ? 9.44922   75.06801  5.52815  1.000 127.61187 ? 344 GLU A CB  1 
ATOM   2248 C CG  . GLU A 1 321 ? 9.51655   75.11299  4.00069  1.000 119.61412 ? 344 GLU A CG  1 
ATOM   2249 C CD  . GLU A 1 321 ? 8.46619   74.25149  3.32530  1.000 126.55647 ? 344 GLU A CD  1 
ATOM   2250 O OE1 . GLU A 1 321 ? 7.28874   74.30903  3.73838  1.000 132.80258 ? 344 GLU A OE1 1 
ATOM   2251 O OE2 . GLU A 1 321 ? 8.81882   73.52223  2.37318  1.000 123.71495 ? 344 GLU A OE2 1 
ATOM   2252 N N   . ALA A 1 322 ? 7.37200   76.78384  7.77002  1.000 142.67005 ? 345 ALA A N   1 
ATOM   2253 C CA  . ALA A 1 322 ? 6.58916   76.49858  8.96625  1.000 138.08583 ? 345 ALA A CA  1 
ATOM   2254 C C   . ALA A 1 322 ? 5.11133   76.65121  8.64432  1.000 140.59877 ? 345 ALA A C   1 
ATOM   2255 O O   . ALA A 1 322 ? 4.29766   76.98210  9.51262  1.000 150.94979 ? 345 ALA A O   1 
ATOM   2256 C CB  . ALA A 1 322 ? 6.99387   77.42157  10.11730 1.000 146.99825 ? 345 ALA A CB  1 
ATOM   2257 N N   . GLY A 1 323 ? 4.77084   76.40076  7.39047  1.000 133.32283 ? 346 GLY A N   1 
ATOM   2258 C CA  . GLY A 1 323 ? 3.49556   76.77011  6.82032  1.000 145.62015 ? 346 GLY A CA  1 
ATOM   2259 C C   . GLY A 1 323 ? 2.48143   75.65965  6.96873  1.000 144.17687 ? 346 GLY A C   1 
ATOM   2260 O O   . GLY A 1 323 ? 2.57951   74.79977  7.84778  1.000 130.20226 ? 346 GLY A O   1 
ATOM   2261 N N   . ALA A 1 324 ? 1.49311   75.67615  6.07994  1.000 141.87210 ? 347 ALA A N   1 
ATOM   2262 C CA  . ALA A 1 324 ? 0.41095   74.69630  6.07732  1.000 121.73950 ? 347 ALA A CA  1 
ATOM   2263 C C   . ALA A 1 324 ? 0.35452   74.22252  4.63405  1.000 128.54324 ? 347 ALA A C   1 
ATOM   2264 O O   . ALA A 1 324 ? -0.33922  74.78630  3.78371  1.000 139.56378 ? 347 ALA A O   1 
ATOM   2265 C CB  . ALA A 1 324 ? -0.91089  75.29328  6.54862  1.000 127.14562 ? 347 ALA A CB  1 
ATOM   2266 N N   . VAL A 1 325 ? 1.11180   73.15935  4.39411  1.000 134.03694 ? 348 VAL A N   1 
ATOM   2267 C CA  . VAL A 1 325 ? 1.21976   72.49133  3.11708  1.000 134.73493 ? 348 VAL A CA  1 
ATOM   2268 C C   . VAL A 1 325 ? 0.25611   71.31172  3.10415  1.000 137.19883 ? 348 VAL A C   1 
ATOM   2269 O O   . VAL A 1 325 ? -0.18573  70.82709  4.14700  1.000 136.59426 ? 348 VAL A O   1 
ATOM   2270 C CB  . VAL A 1 325 ? 2.69103   72.05086  2.90722  1.000 119.67174 ? 348 VAL A CB  1 
ATOM   2271 C CG1 . VAL A 1 325 ? 2.91545   71.46699  1.55414  1.000 110.13894 ? 348 VAL A CG1 1 
ATOM   2272 C CG2 . VAL A 1 325 ? 3.61987   73.23940  3.11740  1.000 135.38302 ? 348 VAL A CG2 1 
ATOM   2273 N N   . SER A 1 326 ? -0.13305  70.87867  1.90507  1.000 138.96739 ? 349 SER A N   1 
ATOM   2274 C CA  . SER A 1 326 ? -0.95264  69.67839  1.78215  1.000 136.45320 ? 349 SER A CA  1 
ATOM   2275 C C   . SER A 1 326 ? -0.46637  68.73042  0.69307  1.000 139.08772 ? 349 SER A C   1 
ATOM   2276 O O   . SER A 1 326 ? 0.57998   68.96210  0.08103  1.000 146.47284 ? 349 SER A O   1 
ATOM   2277 C CB  . SER A 1 326 ? -2.39764  70.07419  1.50299  1.000 133.70334 ? 349 SER A CB  1 
ATOM   2278 O OG  . SER A 1 326 ? -2.79885  71.15829  2.32048  1.000 130.91250 ? 349 SER A OG  1 
ATOM   2279 N N   . SER A 1 327 ? -1.22649  67.65879  0.44903  1.000 131.60176 ? 350 SER A N   1 
ATOM   2280 C CA  . SER A 1 327 ? -0.89643  66.69349  -0.59416 1.000 131.02498 ? 350 SER A CA  1 
ATOM   2281 C C   . SER A 1 327 ? -2.06178  65.74747  -0.86429 1.000 124.36841 ? 350 SER A C   1 
ATOM   2282 O O   . SER A 1 327 ? -2.43422  64.94149  -0.00536 1.000 127.21703 ? 350 SER A O   1 
ATOM   2283 C CB  . SER A 1 327 ? 0.34629   65.88459  -0.21034 1.000 115.44494 ? 350 SER A CB  1 
ATOM   2284 O OG  . SER A 1 327 ? 1.52982   66.51525  -0.66704 1.000 93.92557  ? 350 SER A OG  1 
ATOM   2285 N N   . GLU A 1 328 ? -2.63537  65.84145  -2.06197 1.000 115.93971 ? 351 GLU A N   1 
ATOM   2286 C CA  . GLU A 1 328 ? -3.75370  64.99642  -2.46093 1.000 116.97737 ? 351 GLU A CA  1 
ATOM   2287 C C   . GLU A 1 328 ? -3.26067  63.62425  -2.90575 1.000 123.79907 ? 351 GLU A C   1 
ATOM   2288 O O   . GLU A 1 328 ? -2.31450  63.52086  -3.69302 1.000 122.93067 ? 351 GLU A O   1 
ATOM   2289 C CB  . GLU A 1 328 ? -4.57356  65.66793  -3.56430 1.000 114.39491 ? 351 GLU A CB  1 
ATOM   2290 C CG  . GLU A 1 328 ? -5.42151  66.86457  -3.10211 1.000 110.87175 ? 351 GLU A CG  1 
ATOM   2291 C CD  . GLU A 1 328 ? -4.62372  68.12321  -2.79480 1.000 123.05517 ? 351 GLU A CD  1 
ATOM   2292 O OE1 . GLU A 1 328 ? -4.98322  69.19261  -3.33082 1.000 120.54927 ? 351 GLU A OE1 1 
ATOM   2293 O OE2 . GLU A 1 328 ? -3.65780  68.06008  -2.00589 1.000 136.22655 ? 351 GLU A OE2 1 
ATOM   2294 N N   . ASP A 1 329 ? -3.90022  62.57410  -2.39873 1.000 140.50154 ? 352 ASP A N   1 
ATOM   2295 C CA  . ASP A 1 329 ? -3.52134  61.20451  -2.73556 1.000 137.56863 ? 352 ASP A CA  1 
ATOM   2296 C C   . ASP A 1 329 ? -4.43897  60.63406  -3.81248 1.000 133.68938 ? 352 ASP A C   1 
ATOM   2297 O O   . ASP A 1 329 ? -4.07584  60.57792  -4.98748 1.000 127.59158 ? 352 ASP A O   1 
ATOM   2298 C CB  . ASP A 1 329 ? -3.56412  60.31151  -1.49476 1.000 130.63361 ? 352 ASP A CB  1 
ATOM   2299 C CG  . ASP A 1 329 ? -2.70299  60.83829  -0.36796 1.000 137.92597 ? 352 ASP A CG  1 
ATOM   2300 O OD1 . ASP A 1 329 ? -1.69811  61.52251  -0.65630 1.000 139.56490 ? 352 ASP A OD1 1 
ATOM   2301 O OD2 . ASP A 1 329 ? -3.03555  60.57175  0.80662  1.000 131.83451 ? 352 ASP A OD2 1 
HETATM 2302 C C18 . OLC B 2 .   ? -1.77056  38.52181  5.87908  1.000 65.08694  ? 401 OLC A C18 1 
HETATM 2303 C C10 . OLC B 2 .   ? -3.30038  33.31441  2.81130  1.000 64.51591  ? 401 OLC A C10 1 
HETATM 2304 C C9  . OLC B 2 .   ? -4.25368  32.80843  2.01040  1.000 76.79237  ? 401 OLC A C9  1 
HETATM 2305 C C17 . OLC B 2 .   ? -2.62350  39.68234  5.32075  1.000 70.51786  ? 401 OLC A C17 1 
HETATM 2306 C C11 . OLC B 2 .   ? -2.05647  33.78811  2.01725  1.000 62.52351  ? 401 OLC A C11 1 
HETATM 2307 C C8  . OLC B 2 .   ? -5.64524  32.16335  1.74678  1.000 71.68234  ? 401 OLC A C8  1 
HETATM 2308 C C24 . OLC B 2 .   ? -5.62179  20.80700  6.36903  1.000 92.26553  ? 401 OLC A C24 1 
HETATM 2309 C C16 . OLC B 2 .   ? -2.76760  39.52898  3.78523  1.000 88.46730  ? 401 OLC A C16 1 
HETATM 2310 C C12 . OLC B 2 .   ? -1.44002  35.03960  2.70592  1.000 54.26590  ? 401 OLC A C12 1 
HETATM 2311 C C7  . OLC B 2 .   ? -6.19261  31.52703  3.05138  1.000 82.96160  ? 401 OLC A C7  1 
HETATM 2312 C C15 . OLC B 2 .   ? -3.55515  38.23357  3.45513  1.000 82.01759  ? 401 OLC A C15 1 
HETATM 2313 C C13 . OLC B 2 .   ? -2.57822  35.90171  3.32205  1.000 78.28396  ? 401 OLC A C13 1 
HETATM 2314 C C6  . OLC B 2 .   ? -6.14057  29.97455  2.94371  1.000 75.92997  ? 401 OLC A C6  1 
HETATM 2315 C C14 . OLC B 2 .   ? -2.67265  37.27865  2.60378  1.000 80.42100  ? 401 OLC A C14 1 
HETATM 2316 C C5  . OLC B 2 .   ? -7.16687  29.35467  3.93450  1.000 61.51708  ? 401 OLC A C5  1 
HETATM 2317 C C4  . OLC B 2 .   ? -6.96163  27.81407  4.00066  1.000 45.08923  ? 401 OLC A C4  1 
HETATM 2318 C C3  . OLC B 2 .   ? -6.25144  27.45786  5.33613  1.000 49.64753  ? 401 OLC A C3  1 
HETATM 2319 C C2  . OLC B 2 .   ? -6.88097  26.17469  5.94019  1.000 63.23531  ? 401 OLC A C2  1 
HETATM 2320 C C21 . OLC B 2 .   ? -6.42742  23.06165  7.14428  1.000 77.39338  ? 401 OLC A C21 1 
HETATM 2321 C C1  . OLC B 2 .   ? -5.75526  25.21077  6.38445  1.000 72.82345  ? 401 OLC A C1  1 
HETATM 2322 C C22 . OLC B 2 .   ? -6.85743  21.67746  6.63546  1.000 94.99700  ? 401 OLC A C22 1 
HETATM 2323 O O19 . OLC B 2 .   ? -4.80634  25.63619  6.96503  1.000 60.47187  ? 401 OLC A O19 1 
HETATM 2324 O O25 . OLC B 2 .   ? -5.90158  19.88056  5.34145  1.000 83.97994  ? 401 OLC A O25 1 
HETATM 2325 O O23 . OLC B 2 .   ? -7.65987  21.06140  7.59973  1.000 89.65942  ? 401 OLC A O23 1 
HETATM 2326 O O20 . OLC B 2 .   ? -5.85518  23.82621  6.09792  1.000 77.69793  ? 401 OLC A O20 1 
HETATM 2327 C C10 . OLC C 2 .   ? -19.96841 36.72394  19.42206 1.000 86.67988  ? 402 OLC A C10 1 
HETATM 2328 C C9  . OLC C 2 .   ? -19.93902 38.03166  19.11185 1.000 78.83734  ? 402 OLC A C9  1 
HETATM 2329 C C11 . OLC C 2 .   ? -21.34833 36.07804  19.14148 1.000 75.69349  ? 402 OLC A C11 1 
HETATM 2330 C C8  . OLC C 2 .   ? -20.57943 39.34748  18.58269 1.000 90.79330  ? 402 OLC A C8  1 
HETATM 2331 C C12 . OLC C 2 .   ? -22.37632 36.56515  20.20289 1.000 85.25849  ? 402 OLC A C12 1 
HETATM 2332 C C7  . OLC C 2 .   ? -19.46461 40.31321  18.09748 1.000 87.57558  ? 402 OLC A C7  1 
HETATM 2333 C C13 . OLC C 2 .   ? -23.81406 36.47531  19.61656 1.000 89.61134  ? 402 OLC A C13 1 
HETATM 2334 C C6  . OLC C 2 .   ? -19.86027 40.94314  16.72918 1.000 86.98823  ? 402 OLC A C6  1 
HETATM 2335 C C14 . OLC C 2 .   ? -24.73757 37.50259  20.33162 1.000 87.09869  ? 402 OLC A C14 1 
HETATM 2336 C C5  . OLC C 2 .   ? -18.85148 40.49527  15.63207 1.000 76.64779  ? 402 OLC A C5  1 
HETATM 2337 C C4  . OLC C 2 .   ? -19.28446 39.11649  15.05317 1.000 64.78710  ? 402 OLC A C4  1 
HETATM 2338 C C3  . OLC C 2 .   ? -18.29953 38.01803  15.54270 1.000 67.59516  ? 402 OLC A C3  1 
HETATM 2339 C C2  . OLC C 2 .   ? -19.05089 36.66562  15.67099 1.000 77.90417  ? 402 OLC A C2  1 
HETATM 2340 C C1  . OLC C 2 .   ? -18.03072 35.50209  15.67928 1.000 89.58540  ? 402 OLC A C1  1 
HETATM 2341 O O19 . OLC C 2 .   ? -18.39517 34.39438  15.91502 1.000 87.27195  ? 402 OLC A O19 1 
HETATM 2342 O O20 . OLC C 2 .   ? -16.66415 35.75182  15.40839 1.000 90.80040  ? 402 OLC A O20 1 
HETATM 2343 C C24 . OLC D 2 .   ? 24.71872  16.39416  0.14431  1.000 113.06637 ? 403 OLC A C24 1 
HETATM 2344 C C7  . OLC D 2 .   ? 22.79933  19.32970  1.20995  1.000 65.75738  ? 403 OLC A C7  1 
HETATM 2345 C C6  . OLC D 2 .   ? 22.73885  19.90235  -0.23629 1.000 78.74569  ? 403 OLC A C6  1 
HETATM 2346 C C5  . OLC D 2 .   ? 21.32357  20.48744  -0.50958 1.000 94.66098  ? 403 OLC A C5  1 
HETATM 2347 C C4  . OLC D 2 .   ? 20.50011  19.49676  -1.38313 1.000 92.49455  ? 403 OLC A C4  1 
HETATM 2348 C C3  . OLC D 2 .   ? 21.29548  19.17335  -2.67769 1.000 84.76349  ? 403 OLC A C3  1 
HETATM 2349 C C2  . OLC D 2 .   ? 20.66946  17.94013  -3.38127 1.000 104.29321 ? 403 OLC A C2  1 
HETATM 2350 C C21 . OLC D 2 .   ? 22.81038  15.65564  -1.30771 1.000 123.67970 ? 403 OLC A C21 1 
HETATM 2351 C C1  . OLC D 2 .   ? 21.40792  16.65827  -2.92946 1.000 122.69667 ? 403 OLC A C1  1 
HETATM 2352 C C22 . OLC D 2 .   ? 24.30744  15.48053  -1.01643 1.000 116.31422 ? 403 OLC A C22 1 
HETATM 2353 O O19 . OLC D 2 .   ? 20.96954  15.58835  -3.21165 1.000 133.56383 ? 403 OLC A O19 1 
HETATM 2354 O O25 . OLC D 2 .   ? 25.25724  17.59283  -0.36776 1.000 108.36988 ? 403 OLC A O25 1 
HETATM 2355 O O23 . OLC D 2 .   ? 24.56267  14.14913  -0.67609 1.000 110.91475 ? 403 OLC A O23 1 
HETATM 2356 O O20 . OLC D 2 .   ? 22.60338  16.75338  -2.17849 1.000 106.89133 ? 403 OLC A O20 1 
HETATM 2357 C C9  . OLC E 2 .   ? -11.88308 39.84334  12.87722 1.000 37.58109  ? 404 OLC A C9  1 
HETATM 2358 C C8  . OLC E 2 .   ? -11.66803 41.38186  12.78696 1.000 37.16113  ? 404 OLC A C8  1 
HETATM 2359 C C24 . OLC E 2 .   ? -12.79668 51.10029  18.31894 1.000 69.32894  ? 404 OLC A C24 1 
HETATM 2360 C C7  . OLC E 2 .   ? -11.78140 42.01077  14.20165 1.000 37.59010  ? 404 OLC A C7  1 
HETATM 2361 C C6  . OLC E 2 .   ? -10.65083 43.06387  14.40123 1.000 32.21383  ? 404 OLC A C6  1 
HETATM 2362 C C5  . OLC E 2 .   ? -10.28939 43.16604  15.91098 1.000 29.03892  ? 404 OLC A C5  1 
HETATM 2363 C C4  . OLC E 2 .   ? -9.32522  44.36633  16.13792 1.000 38.25859  ? 404 OLC A C4  1 
HETATM 2364 C C3  . OLC E 2 .   ? -9.96140  45.34201  17.16671 1.000 38.92894  ? 404 OLC A C3  1 
HETATM 2365 C C2  . OLC E 2 .   ? -9.06738  46.60440  17.29371 1.000 51.60300  ? 404 OLC A C2  1 
HETATM 2366 C C21 . OLC E 2 .   ? -10.83732 49.59583  18.79720 1.000 69.53399  ? 404 OLC A C21 1 
HETATM 2367 C C1  . OLC E 2 .   ? -9.69096  47.56403  18.33358 1.000 78.41998  ? 404 OLC A C1  1 
HETATM 2368 C C22 . OLC E 2 .   ? -11.28810 50.89058  18.10337 1.000 83.27966  ? 404 OLC A C22 1 
HETATM 2369 O O19 . OLC E 2 .   ? -10.06167 47.12752  19.37619 1.000 85.07561  ? 404 OLC A O19 1 
HETATM 2370 O O25 . OLC E 2 .   ? -13.06129 52.42012  18.74890 1.000 53.57934  ? 404 OLC A O25 1 
HETATM 2371 O O23 . OLC E 2 .   ? -10.57400 51.96720  18.63493 1.000 92.45533  ? 404 OLC A O23 1 
HETATM 2372 O O20 . OLC E 2 .   ? -9.82612  48.94746  18.04487 1.000 65.95616  ? 404 OLC A O20 1 
HETATM 2373 C C10 . OLC F 2 .   ? -9.91146  28.68190  21.06865 1.000 54.49184  ? 405 OLC A C10 1 
HETATM 2374 C C9  . OLC F 2 .   ? -9.87676  27.45161  21.61262 1.000 52.07614  ? 405 OLC A C9  1 
HETATM 2375 C C11 . OLC F 2 .   ? -9.06172  29.71519  21.85343 1.000 36.08402  ? 405 OLC A C11 1 
HETATM 2376 C C8  . OLC F 2 .   ? -10.27285 25.94465  21.65483 1.000 61.33033  ? 405 OLC A C8  1 
HETATM 2377 C C24 . OLC F 2 .   ? -16.26549 15.14042  17.79964 1.000 106.50106 ? 405 OLC A C24 1 
HETATM 2378 C C7  . OLC F 2 .   ? -10.55800 25.41572  20.22106 1.000 62.57183  ? 405 OLC A C7  1 
HETATM 2379 C C6  . OLC F 2 .   ? -12.01773 24.87655  20.13019 1.000 82.32655  ? 405 OLC A C6  1 
HETATM 2380 C C5  . OLC F 2 .   ? -12.08911 23.37579  20.54357 1.000 67.38425  ? 405 OLC A C5  1 
HETATM 2381 C C4  . OLC F 2 .   ? -11.90903 22.46777  19.28969 1.000 92.14828  ? 405 OLC A C4  1 
HETATM 2382 C C3  . OLC F 2 .   ? -12.57683 21.08220  19.52940 1.000 80.69624  ? 405 OLC A C3  1 
HETATM 2383 C C2  . OLC F 2 .   ? -13.51228 20.72537  18.34074 1.000 75.64805  ? 405 OLC A C2  1 
HETATM 2384 C C21 . OLC F 2 .   ? -14.78407 17.15597  17.98521 1.000 110.07272 ? 405 OLC A C21 1 
HETATM 2385 C C1  . OLC F 2 .   ? -13.55052 19.19240  18.12228 1.000 77.87639  ? 405 OLC A C1  1 
HETATM 2386 C C22 . OLC F 2 .   ? -15.96488 16.40197  18.61771 1.000 98.44872  ? 405 OLC A C22 1 
HETATM 2387 O O19 . OLC F 2 .   ? -12.64438 18.64283  17.58064 1.000 77.95363  ? 405 OLC A O19 1 
HETATM 2388 O O25 . OLC F 2 .   ? -16.97851 14.22240  18.59923 1.000 102.54935 ? 405 OLC A O25 1 
HETATM 2389 O O23 . OLC F 2 .   ? -15.65821 16.03588  19.93197 1.000 68.10796  ? 405 OLC A O23 1 
HETATM 2390 O O20 . OLC F 2 .   ? -14.66841 18.44387  18.56491 1.000 107.12570 ? 405 OLC A O20 1 
HETATM 2391 C C8  . OLC G 2 .   ? 3.48527   51.81687  2.18529  1.000 53.22179  ? 406 OLC A C8  1 
HETATM 2392 C C7  . OLC G 2 .   ? 4.90528   52.29330  1.78017  1.000 38.25018  ? 406 OLC A C7  1 
HETATM 2393 C C6  . OLC G 2 .   ? 4.96910   53.84844  1.84549  1.000 40.40203  ? 406 OLC A C6  1 
HETATM 2394 C C5  . OLC G 2 .   ? 6.20010   54.34723  1.03601  1.000 55.14555  ? 406 OLC A C5  1 
HETATM 2395 C C4  . OLC G 2 .   ? 5.88570   55.72703  0.38581  1.000 65.03314  ? 406 OLC A C4  1 
HETATM 2396 C C3  . OLC G 2 .   ? 6.24047   55.68090  -1.12807 1.000 85.17021  ? 406 OLC A C3  1 
HETATM 2397 C C2  . OLC G 2 .   ? 6.18424   57.11469  -1.72191 1.000 83.58076  ? 406 OLC A C2  1 
HETATM 2398 C C1  . OLC G 2 .   ? 4.78033   57.37951  -2.31559 1.000 102.26698 ? 406 OLC A C1  1 
HETATM 2399 O O19 . OLC G 2 .   ? 4.44931   56.84135  -3.32418 1.000 100.70380 ? 406 OLC A O19 1 
HETATM 2400 O O20 . OLC G 2 .   ? 3.89091   58.26341  -1.65924 1.000 104.87038 ? 406 OLC A O20 1 
HETATM 2401 C C8  . OLC H 2 .   ? -3.82757  43.87733  3.88765  1.000 50.92293  ? 407 OLC A C8  1 
HETATM 2402 C C7  . OLC H 2 .   ? -3.07671  45.17528  3.48824  1.000 57.20542  ? 407 OLC A C7  1 
HETATM 2403 C C6  . OLC H 2 .   ? -4.11321  46.27139  3.10315  1.000 70.89832  ? 407 OLC A C6  1 
HETATM 2404 C C5  . OLC H 2 .   ? -3.49516  47.21931  2.03558  1.000 70.19113  ? 407 OLC A C5  1 
HETATM 2405 C C4  . OLC H 2 .   ? -2.99889  48.52868  2.71329  1.000 63.16497  ? 407 OLC A C4  1 
HETATM 2406 C C3  . OLC H 2 .   ? -3.37229  49.74753  1.82476  1.000 62.99733  ? 407 OLC A C3  1 
HETATM 2407 C C2  . OLC H 2 .   ? -2.92714  51.05799  2.52836  1.000 77.36076  ? 407 OLC A C2  1 
HETATM 2408 C C1  . OLC H 2 .   ? -4.17247  51.90171  2.88666  1.000 84.26582  ? 407 OLC A C1  1 
HETATM 2409 O O19 . OLC H 2 .   ? -4.10072  52.74965  3.71827  1.000 86.56027  ? 407 OLC A O19 1 
HETATM 2410 O O20 . OLC H 2 .   ? -5.39765  51.66408  2.22228  1.000 93.23778  ? 407 OLC A O20 1 
HETATM 2411 C C10 . OLC I 2 .   ? 15.00245  37.67761  29.89456 1.000 57.09376  ? 408 OLC A C10 1 
HETATM 2412 C C9  . OLC I 2 .   ? 14.44284  38.65442  29.16156 1.000 44.09813  ? 408 OLC A C9  1 
HETATM 2413 C C8  . OLC I 2 .   ? 14.23819  40.14555  28.77150 1.000 49.16043  ? 408 OLC A C8  1 
HETATM 2414 C C7  . OLC I 2 .   ? 14.68512  41.05684  29.94599 1.000 50.83451  ? 408 OLC A C7  1 
HETATM 2415 C C6  . OLC I 2 .   ? 15.54758  42.23294  29.39896 1.000 50.41147  ? 408 OLC A C6  1 
HETATM 2416 C C5  . OLC I 2 .   ? 14.64122  43.19863  28.58151 1.000 57.21584  ? 408 OLC A C5  1 
HETATM 2417 C C4  . OLC I 2 .   ? 15.49945  44.30374  27.89619 1.000 57.32378  ? 408 OLC A C4  1 
HETATM 2418 C C3  . OLC I 2 .   ? 14.71465  45.64768  27.89021 1.000 60.12527  ? 408 OLC A C3  1 
HETATM 2419 C C2  . OLC I 2 .   ? 15.67870  46.81984  27.56021 1.000 40.73193  ? 408 OLC A C2  1 
HETATM 2420 C C9  . OLC J 2 .   ? 9.77043   56.51911  -3.40868 1.000 69.10646  ? 409 OLC A C9  1 
HETATM 2421 C C8  . OLC J 2 .   ? 10.13377  55.16870  -4.08944 1.000 75.11793  ? 409 OLC A C8  1 
HETATM 2422 C C7  . OLC J 2 .   ? 11.30766  54.49463  -3.33062 1.000 69.95083  ? 409 OLC A C7  1 
HETATM 2423 C C6  . OLC J 2 .   ? 11.38111  52.98943  -3.72275 1.000 74.29589  ? 409 OLC A C6  1 
HETATM 2424 C C5  . OLC J 2 .   ? 12.85498  52.50041  -3.64494 1.000 84.28685  ? 409 OLC A C5  1 
HETATM 2425 C C4  . OLC J 2 .   ? 12.94947  51.30171  -2.65648 1.000 66.32421  ? 409 OLC A C4  1 
HETATM 2426 C C3  . OLC J 2 .   ? 12.66748  49.97295  -3.41152 1.000 71.48939  ? 409 OLC A C3  1 
HETATM 2427 C C2  . OLC J 2 .   ? 13.13013  48.77316  -2.54131 1.000 69.66120  ? 409 OLC A C2  1 
HETATM 2428 C C1  . RET K 3 .   ? -0.65401  33.41261  11.01473 1.000 47.88098  ? 410 RET A C1  1 
HETATM 2429 C C2  . RET K 3 .   ? -1.86946  32.54763  10.63859 1.000 47.52551  ? 410 RET A C2  1 
HETATM 2430 C C3  . RET K 3 .   ? -3.18452  33.30977  10.68737 1.000 47.25652  ? 410 RET A C3  1 
HETATM 2431 C C4  . RET K 3 .   ? -3.14987  34.47614  9.72174  1.000 46.97097  ? 410 RET A C4  1 
HETATM 2432 C C5  . RET K 3 .   ? -1.85786  35.24980  9.75257  1.000 45.69513  ? 410 RET A C5  1 
HETATM 2433 C C6  . RET K 3 .   ? -0.77917  34.83340  10.43597 1.000 57.46511  ? 410 RET A C6  1 
HETATM 2434 C C7  . RET K 3 .   ? 0.35236   35.79415  10.64558 1.000 57.49398  ? 410 RET A C7  1 
HETATM 2435 C C8  . RET K 3 .   ? 1.50578   35.70770  11.31075 1.000 54.50632  ? 410 RET A C8  1 
HETATM 2436 C C9  . RET K 3 .   ? 2.52619   36.73726  11.43049 1.000 51.01311  ? 410 RET A C9  1 
HETATM 2437 C C10 . RET K 3 .   ? 3.65194   36.46377  12.13300 1.000 52.43272  ? 410 RET A C10 1 
HETATM 2438 C C11 . RET K 3 .   ? 4.78094   37.31576  12.35362 1.000 38.63514  ? 410 RET A C11 1 
HETATM 2439 C C12 . RET K 3 .   ? 5.84319   36.92499  13.07393 1.000 41.14510  ? 410 RET A C12 1 
HETATM 2440 C C13 . RET K 3 .   ? 7.04305   37.69086  13.36885 1.000 46.00493  ? 410 RET A C13 1 
HETATM 2441 C C14 . RET K 3 .   ? 7.99130   37.14364  14.16834 1.000 56.70842  ? 410 RET A C14 1 
HETATM 2442 C C15 . RET K 3 .   ? 9.24166   37.74538  14.66817 1.000 41.30959  ? 410 RET A C15 1 
HETATM 2443 C C16 . RET K 3 .   ? -0.58904  33.44356  12.54686 1.000 33.89514  ? 410 RET A C16 1 
HETATM 2444 C C17 . RET K 3 .   ? 0.58918   32.69627  10.47196 1.000 48.00750  ? 410 RET A C17 1 
HETATM 2445 C C18 . RET K 3 .   ? -1.91791  36.51923  8.95050  1.000 33.65935  ? 410 RET A C18 1 
HETATM 2446 C C19 . RET K 3 .   ? 2.28485   38.05619  10.75133 1.000 41.99956  ? 410 RET A C19 1 
HETATM 2447 C C20 . RET K 3 .   ? 7.14974   39.07917  12.80626 1.000 38.72739  ? 410 RET A C20 1 
HETATM 2448 O O   . HOH L 4 .   ? 4.77230   26.29092  8.41893  1.000 40.89926  ? 501 HOH A O   1 
HETATM 2449 O O   . HOH L 4 .   ? 4.27470   28.72124  11.86303 1.000 31.58038  ? 502 HOH A O   1 
HETATM 2450 O O   . HOH L 4 .   ? 4.22315   30.83462  10.12985 1.000 42.47070  ? 503 HOH A O   1 
HETATM 2451 O O   . HOH L 4 .   ? 5.09888   8.10532   20.88179 1.000 36.06626  ? 504 HOH A O   1 
HETATM 2452 O O   . HOH L 4 .   ? 9.89452   32.47571  14.30745 1.000 36.38358  ? 505 HOH A O   1 
HETATM 2453 O O   . HOH L 4 .   ? 6.07201   10.80800  27.80545 1.000 34.24693  ? 506 HOH A O   1 
HETATM 2454 O O   . HOH L 4 .   ? 8.94118   43.64012  11.54852 1.000 27.70262  ? 507 HOH A O   1 
HETATM 2455 O O   . HOH L 4 .   ? -8.04914  51.38552  18.42219 1.000 62.45023  ? 508 HOH A O   1 
HETATM 2456 O O   . HOH L 4 .   ? -4.63721  -9.33341  6.49963  1.000 83.06331  ? 509 HOH A O   1 
HETATM 2457 O O   . HOH L 4 .   ? 12.41928  12.24052  6.31569  1.000 45.24283  ? 510 HOH A O   1 
HETATM 2458 O O   . HOH L 4 .   ? 2.55474   38.63010  14.32614 1.000 46.92449  ? 511 HOH A O   1 
HETATM 2459 O O   . HOH L 4 .   ? 3.59328   24.64855  14.50473 1.000 32.42189  ? 512 HOH A O   1 
HETATM 2460 O O   . HOH L 4 .   ? 3.31373   3.56918   29.30858 1.000 23.43993  ? 513 HOH A 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   . MET A 27  ? 0.61440 0.62461 0.78786 0.03386  0.12098  -0.06781 50  MET A N   
2    C CA  . MET A 27  ? 0.96584 0.97564 1.13667 0.03490  0.12219  -0.06466 50  MET A CA  
3    C C   . MET A 27  ? 1.09876 1.11119 1.26865 0.04130  0.12340  -0.05975 50  MET A C   
4    O O   . MET A 27  ? 1.07156 1.08510 1.24532 0.04406  0.12436  -0.05739 50  MET A O   
5    C CB  . MET A 27  ? 0.61744 0.62415 0.79268 0.03076  0.12418  -0.06327 50  MET A CB  
6    N N   . LEU A 28  ? 0.94428 0.95798 1.10916 0.04374  0.12334  -0.05809 51  LEU A N   
7    C CA  . LEU A 28  ? 0.75381 0.77033 0.91770 0.04958  0.12478  -0.05282 51  LEU A CA  
8    C C   . LEU A 28  ? 0.75477 0.76973 0.92042 0.04876  0.12725  -0.04841 51  LEU A C   
9    O O   . LEU A 28  ? 0.79226 0.80960 0.95514 0.05288  0.12810  -0.04453 51  LEU A O   
10   C CB  . LEU A 28  ? 0.76171 0.78167 0.91859 0.05386  0.12282  -0.05396 51  LEU A CB  
11   N N   . PHE A 29  ? 0.72874 0.74001 0.89901 0.04357  0.12835  -0.04902 52  PHE A N   
12   C CA  . PHE A 29  ? 0.61336 0.62301 0.78798 0.04291  0.13103  -0.04436 52  PHE A CA  
13   C C   . PHE A 29  ? 0.70028 0.70819 0.88309 0.04136  0.13236  -0.04340 52  PHE A C   
14   O O   . PHE A 29  ? 0.55705 0.56484 0.74177 0.04031  0.13117  -0.04669 52  PHE A O   
15   C CB  . PHE A 29  ? 0.47132 0.47813 0.64450 0.03819  0.13121  -0.04577 52  PHE A CB  
16   C CG  . PHE A 29  ? 0.58696 0.59162 0.75948 0.03272  0.12935  -0.05179 52  PHE A CG  
17   C CD1 . PHE A 29  ? 0.51176 0.51420 0.69016 0.02870  0.12966  -0.05384 52  PHE A CD1 
18   C CD2 . PHE A 29  ? 0.49599 0.50110 0.66227 0.03163  0.12726  -0.05530 52  PHE A CD2 
19   C CE1 . PHE A 29  ? 0.60372 0.60488 0.78146 0.02382  0.12798  -0.05910 52  PHE A CE1 
20   C CE2 . PHE A 29  ? 0.56837 0.57192 0.73436 0.02662  0.12562  -0.06034 52  PHE A CE2 
21   C CZ  . PHE A 29  ? 0.67721 0.67900 0.84879 0.02275  0.12602  -0.06215 52  PHE A CZ  
22   N N   . GLN A 30  ? 0.66323 0.66986 0.85118 0.04131  0.13481  -0.03878 53  GLN A N   
23   C CA  . GLN A 30  ? 0.52359 0.52848 0.72016 0.04012  0.13617  -0.03744 53  GLN A CA  
24   C C   . GLN A 30  ? 0.72349 0.72504 0.92305 0.03391  0.13532  -0.04278 53  GLN A C   
25   O O   . GLN A 30  ? 0.68727 0.68682 0.88543 0.02997  0.13526  -0.04462 53  GLN A O   
26   C CB  . GLN A 30  ? 0.48609 0.49037 0.68774 0.04143  0.13891  -0.03111 53  GLN A CB  
27   C CG  . GLN A 30  ? 0.54285 0.54576 0.75411 0.04131  0.14039  -0.02873 53  GLN A CG  
28   C CD  . GLN A 30  ? 0.54300 0.54845 0.75529 0.04516  0.13975  -0.02823 53  GLN A CD  
29   O OE1 . GLN A 30  ? 0.61573 0.62492 0.82440 0.05041  0.13983  -0.02477 53  GLN A OE1 
30   N NE2 . GLN A 30  ? 0.50116 0.50489 0.71838 0.04266  0.13905  -0.03171 53  GLN A NE2 
31   N N   . THR A 31  ? 0.65731 0.65862 0.86094 0.03316  0.13461  -0.04524 54  THR A N   
32   C CA  . THR A 31  ? 0.54704 0.54593 0.75389 0.02770  0.13371  -0.05029 54  THR A CA  
33   C C   . THR A 31  ? 0.76652 0.76364 0.98285 0.02667  0.13502  -0.04922 54  THR A C   
34   O O   . THR A 31  ? 0.76950 0.76455 0.98942 0.02202  0.13464  -0.05289 54  THR A O   
35   C CB  . THR A 31  ? 0.58188 0.58220 0.78468 0.02693  0.13114  -0.05552 54  THR A CB  
36   O OG1 . THR A 31  ? 0.63219 0.63465 0.83618 0.03124  0.13093  -0.05410 54  THR A OG1 
37   C CG2 . THR A 31  ? 0.52468 0.52629 0.71890 0.02706  0.12957  -0.05738 54  THR A CG2 
38   N N   . SER A 32  ? 0.66482 0.66291 0.88545 0.03089  0.13646  -0.04435 55  SER A N   
39   C CA  . SER A 32  ? 0.66684 0.66320 0.89723 0.03032  0.13773  -0.04279 55  SER A CA  
40   C C   . SER A 32  ? 0.63440 0.62928 0.86972 0.03074  0.14017  -0.03740 55  SER A C   
41   O O   . SER A 32  ? 0.55168 0.54837 0.78443 0.03464  0.14134  -0.03218 55  SER A O   
42   C CB  . SER A 32  ? 0.60894 0.60739 0.84174 0.03466  0.13767  -0.04074 55  SER A CB  
43   O OG  . SER A 32  ? 0.91006 0.91068 1.14249 0.03987  0.13923  -0.03411 55  SER A OG  
44   N N   . TYR A 33  ? 0.64467 0.63654 0.88713 0.02680  0.14084  -0.03871 56  TYR A N   
45   C CA  . TYR A 33  ? 0.56633 0.55648 0.81481 0.02675  0.14308  -0.03389 56  TYR A CA  
46   C C   . TYR A 33  ? 0.48155 0.46893 0.74058 0.02374  0.14352  -0.03539 56  TYR A C   
47   O O   . TYR A 33  ? 0.86277 0.84956 1.12331 0.02102  0.14198  -0.04084 56  TYR A O   
48   C CB  . TYR A 33  ? 0.41979 0.40910 0.66315 0.02433  0.14332  -0.03437 56  TYR A CB  
49   C CG  . TYR A 33  ? 0.38217 0.36973 0.62394 0.01871  0.14178  -0.04114 56  TYR A CG  
50   C CD1 . TYR A 33  ? 0.38449 0.37343 0.61849 0.01746  0.13960  -0.04605 56  TYR A CD1 
51   C CD2 . TYR A 33  ? 0.51298 0.49783 0.76135 0.01472  0.14243  -0.04258 56  TYR A CD2 
52   C CE1 . TYR A 33  ? 0.49060 0.47848 0.72326 0.01241  0.13820  -0.05179 56  TYR A CE1 
53   C CE2 . TYR A 33  ? 0.67421 0.65812 0.92101 0.00978  0.14097  -0.04865 56  TYR A CE2 
54   C CZ  . TYR A 33  ? 0.50204 0.48758 0.74092 0.00866  0.13891  -0.05304 56  TYR A CZ  
55   O OH  . TYR A 33  ? 0.91182 0.89692 1.14926 0.00384  0.13749  -0.05862 56  TYR A OH  
56   N N   . THR A 34  ? 0.47578 0.46163 0.74236 0.02429  0.14556  -0.03047 57  THR A N   
57   C CA  . THR A 34  ? 0.49962 0.48258 0.77691 0.02124  0.14605  -0.03171 57  THR A CA  
58   C C   . THR A 34  ? 0.56893 0.54974 0.84833 0.01839  0.14719  -0.03083 57  THR A C   
59   O O   . THR A 34  ? 0.59600 0.57745 0.87282 0.02047  0.14862  -0.02572 57  THR A O   
60   C CB  . THR A 34  ? 0.58567 0.56853 0.87247 0.02457  0.14737  -0.02636 57  THR A CB  
61   O OG1 . THR A 34  ? 0.75022 0.73366 1.03854 0.02766  0.14951  -0.01873 57  THR A OG1 
62   C CG2 . THR A 34  ? 0.45375 0.43917 0.73767 0.02812  0.14639  -0.02633 57  THR A CG2 
63   N N   . LEU A 35  ? 0.62525 0.60384 0.90911 0.01369  0.14647  -0.03595 58  LEU A N   
64   C CA  . LEU A 35  ? 0.78133 0.75758 1.07021 0.01100  0.14762  -0.03508 58  LEU A CA  
65   C C   . LEU A 35  ? 0.75007 0.72460 1.05153 0.01224  0.14920  -0.03058 58  LEU A C   
66   O O   . LEU A 35  ? 0.92813 0.90222 1.23658 0.01230  0.14863  -0.03206 58  LEU A O   
67   C CB  . LEU A 35  ? 0.90574 0.88081 1.19448 0.00561  0.14608  -0.04254 58  LEU A CB  
68   C CG  . LEU A 35  ? 0.65962 0.63606 0.93705 0.00338  0.14446  -0.04720 58  LEU A CG  
69   C CD1 . LEU A 35  ? 0.68568 0.66079 0.96417 -0.00166 0.14380  -0.05208 58  LEU A CD1 
70   C CD2 . LEU A 35  ? 0.56560 0.54329 0.83436 0.00607  0.14520  -0.04301 58  LEU A CD2 
71   N N   . GLU A 36  ? 0.59445 0.56809 0.89903 0.01320  0.15110  -0.02498 59  GLU A N   
72   C CA  . GLU A 36  ? 0.80196 0.77378 1.11918 0.01396  0.15262  -0.02035 59  GLU A CA  
73   C C   . GLU A 36  ? 0.80529 0.77460 1.12709 0.01055  0.15335  -0.02085 59  GLU A C   
74   O O   . GLU A 36  ? 0.77676 0.74606 1.09105 0.00833  0.15297  -0.02350 59  GLU A O   
75   C CB  . GLU A 36  ? 0.61436 0.58803 0.93240 0.01929  0.15442  -0.01140 59  GLU A CB  
76   C CG  . GLU A 36  ? 0.65130 0.62778 0.96478 0.02315  0.15375  -0.01044 59  GLU A CG  
77   C CD  . GLU A 36  ? 0.83544 0.81095 1.15756 0.02291  0.15293  -0.01254 59  GLU A CD  
78   O OE1 . GLU A 36  ? 0.86401 0.83707 1.19785 0.02146  0.15356  -0.01139 59  GLU A OE1 
79   O OE2 . GLU A 36  ? 0.83637 0.81360 1.15373 0.02419  0.15156  -0.01540 59  GLU A OE2 
80   N N   . ASN A 37  ? 0.72777 0.69496 1.06229 0.01023  0.15434  -0.01809 60  ASN A N   
81   C CA  . ASN A 37  ? 0.64414 0.60887 0.98489 0.00759  0.15523  -0.01743 60  ASN A CA  
82   C C   . ASN A 37  ? 0.89122 0.85497 1.22785 0.00272  0.15369  -0.02556 60  ASN A C   
83   O O   . ASN A 37  ? 0.91025 0.87342 1.24236 0.00118  0.15409  -0.02558 60  ASN A O   
84   C CB  . ASN A 37  ? 0.59648 0.56198 0.93377 0.01018  0.15715  -0.00993 60  ASN A CB  
85   C CG  . ASN A 37  ? 0.83419 0.80072 1.17796 0.01469  0.15885  -0.00116 60  ASN A CG  
86   O OD1 . ASN A 37  ? 0.95077 0.91745 1.30064 0.01616  0.15853  -0.00060 60  ASN A OD1 
87   N ND2 . ASN A 37  ? 0.73030 0.69778 1.07260 0.01697  0.16058  0.00593  60  ASN A ND2 
88   N N   . ASN A 38  ? 0.75097 0.71485 1.08891 0.00037  0.15182  -0.03244 61  ASN A N   
89   C CA  . ASN A 38  ? 0.98183 0.94538 1.31696 -0.00429 0.15019  -0.04033 61  ASN A CA  
90   C C   . ASN A 38  ? 1.04103 1.00623 1.36190 -0.00479 0.14960  -0.04204 61  ASN A C   
91   O O   . ASN A 38  ? 0.94396 0.90851 1.26122 -0.00770 0.14928  -0.04483 61  ASN A O   
92   C CB  . ASN A 38  ? 1.08029 1.04131 1.42430 -0.00715 0.15071  -0.04110 61  ASN A CB  
93   C CG  . ASN A 38  ? 1.15298 1.11412 1.49642 -0.01183 0.14881  -0.04970 61  ASN A CG  
94   O OD1 . ASN A 38  ? 1.30962 1.27275 1.64910 -0.01306 0.14706  -0.05506 61  ASN A OD1 
95   N ND2 . ASN A 38  ? 1.07768 1.03696 1.42493 -0.01433 0.14908  -0.05096 61  ASN A ND2 
96   N N   . GLY A 39  ? 0.96187 0.92925 1.27471 -0.00183 0.14937  -0.04033 62  GLY A N   
97   C CA  . GLY A 39  ? 0.87803 0.84717 1.17781 -0.00222 0.14849  -0.04228 62  GLY A CA  
98   C C   . GLY A 39  ? 0.77421 0.74339 1.06825 -0.00076 0.14986  -0.03730 62  GLY A C   
99   O O   . GLY A 39  ? 0.76749 0.73776 1.05131 -0.00177 0.14903  -0.03934 62  GLY A O   
100  N N   . SER A 40  ? 0.60378 0.57198 0.90416 0.00160  0.15187  -0.03066 63  SER A N   
101  C CA  . SER A 40  ? 0.59095 0.55940 0.88648 0.00292  0.15319  -0.02570 63  SER A CA  
102  C C   . SER A 40  ? 0.55221 0.52335 0.84237 0.00800  0.15414  -0.01941 63  SER A C   
103  O O   . SER A 40  ? 0.59526 0.56738 0.87943 0.00940  0.15496  -0.01564 63  SER A O   
104  C CB  . SER A 40  ? 0.56841 0.53436 0.87407 0.00213  0.15475  -0.02211 63  SER A CB  
105  O OG  . SER A 40  ? 0.68611 0.65179 1.00185 0.00499  0.15604  -0.01683 63  SER A OG  
106  N N   . VAL A 41  ? 0.41814 0.39071 0.71017 0.01091  0.15397  -0.01822 64  VAL A N   
107  C CA  . VAL A 41  ? 0.50168 0.47727 0.78883 0.01607  0.15473  -0.01244 64  VAL A CA  
108  C C   . VAL A 41  ? 0.50624 0.48373 0.78742 0.01714  0.15297  -0.01647 64  VAL A C   
109  O O   . VAL A 41  ? 0.63354 0.61005 0.91958 0.01549  0.15192  -0.02069 64  VAL A O   
110  C CB  . VAL A 41  ? 0.42755 0.40326 0.72466 0.01947  0.15661  -0.00497 64  VAL A CB  
111  C CG1 . VAL A 41  ? 0.49759 0.47709 0.78930 0.02499  0.15720  0.00070  64  VAL A CG1 
112  C CG2 . VAL A 41  ? 0.55653 0.53042 0.85993 0.01845  0.15829  -0.00065 64  VAL A CG2 
113  N N   . ILE A 42  ? 0.40054 0.38086 0.67122 0.01985  0.15252  -0.01541 65  ILE A N   
114  C CA  . ILE A 42  ? 0.57956 0.56210 0.84438 0.02173  0.15094  -0.01816 65  ILE A CA  
115  C C   . ILE A 42  ? 0.55427 0.53999 0.81808 0.02773  0.15200  -0.01138 65  ILE A C   
116  O O   . ILE A 42  ? 0.59620 0.58365 0.85655 0.03038  0.15319  -0.00614 65  ILE A O   
117  C CB  . ILE A 42  ? 0.47291 0.45625 0.72665 0.01971  0.14910  -0.02348 65  ILE A CB  
118  C CG1 . ILE A 42  ? 0.53710 0.51777 0.79236 0.01376  0.14801  -0.03001 65  ILE A CG1 
119  C CG2 . ILE A 42  ? 0.58818 0.57413 0.83582 0.02221  0.14744  -0.02576 65  ILE A CG2 
120  C CD1 . ILE A 42  ? 0.56765 0.54914 0.81250 0.01162  0.14626  -0.03459 65  ILE A CD1 
121  N N   . CYS A 43  ? 0.41876 0.40546 0.68575 0.02987  0.15152  -0.01141 66  CYS A N   
122  C CA  . CYS A 43  ? 0.58544 0.57555 0.85160 0.03559  0.15217  -0.00575 66  CYS A CA  
123  C C   . CYS A 43  ? 0.51111 0.50373 0.76916 0.03735  0.15019  -0.00965 66  CYS A C   
124  O O   . CYS A 43  ? 0.54806 0.53933 0.80602 0.03441  0.14852  -0.01602 66  CYS A O   
125  C CB  . CYS A 43  ? 0.63239 0.62154 0.91033 0.03683  0.15334  -0.00185 66  CYS A CB  
126  S SG  . CYS A 43  ? 0.68356 0.66977 0.97267 0.03503  0.15563  0.00329  66  CYS A SG  
127  N N   . ILE A 44  ? 0.41125 0.40780 0.66277 0.04226  0.15034  -0.00574 67  ILE A N   
128  C CA  . ILE A 44  ? 0.53565 0.53494 0.77885 0.04434  0.14838  -0.00924 67  ILE A CA  
129  C C   . ILE A 44  ? 0.37382 0.37725 0.61711 0.05059  0.14905  -0.00331 67  ILE A C   
130  O O   . ILE A 44  ? 0.34892 0.35371 0.59607 0.05347  0.15098  0.00384  67  ILE A O   
131  C CB  . ILE A 44  ? 0.73271 0.73327 0.96507 0.04397  0.14727  -0.01179 67  ILE A CB  
132  C CG1 . ILE A 44  ? 0.54473 0.54690 0.77501 0.04643  0.14895  -0.00563 67  ILE A CG1 
133  C CG2 . ILE A 44  ? 0.32083 0.31790 0.55188 0.03786  0.14613  -0.01835 67  ILE A CG2 
134  C CD1 . ILE A 44  ? 0.46037 0.46583 0.67959 0.04905  0.14776  -0.00638 67  ILE A CD1 
135  N N   . PRO A 45  ? 0.38025 0.38590 0.61942 0.05268  0.14738  -0.00621 68  PRO A N   
136  C CA  . PRO A 45  ? 0.46622 0.47663 0.70352 0.05897  0.14773  -0.00098 68  PRO A CA  
137  C C   . PRO A 45  ? 0.38928 0.40310 0.61887 0.06218  0.14813  0.00259  68  PRO A C   
138  O O   . PRO A 45  ? 0.53163 0.54513 0.75380 0.06041  0.14697  -0.00144 68  PRO A O   
139  C CB  . PRO A 45  ? 0.50981 0.52162 0.74267 0.05969  0.14543  -0.00648 68  PRO A CB  
140  C CG  . PRO A 45  ? 0.55326 0.56072 0.78873 0.05375  0.14427  -0.01347 68  PRO A CG  
141  C CD  . PRO A 45  ? 0.43110 0.43537 0.66734 0.04951  0.14509  -0.01412 68  PRO A CD  
142  N N   . ASN A 46  ? 0.37259 0.38992 0.60415 0.06699  0.14974  0.01040  69  ASN A N   
143  C CA  . ASN A 46  ? 0.24755 0.26935 0.47168 0.07115  0.15003  0.01450  69  ASN A CA  
144  C C   . ASN A 46  ? 0.42693 0.45366 0.64270 0.07571  0.14812  0.01269  69  ASN A C   
145  O O   . ASN A 46  ? 0.43449 0.46629 0.64923 0.08128  0.14851  0.01798  69  ASN A O   
146  C CB  . ASN A 46  ? 0.37990 0.40392 0.60961 0.07439  0.15244  0.02384  69  ASN A CB  
147  C CG  . ASN A 46  ? 0.40892 0.43696 0.63154 0.07765  0.15290  0.02802  69  ASN A CG  
148  O OD1 . ASN A 46  ? 0.70309 0.73233 0.91656 0.07778  0.15133  0.02379  69  ASN A OD1 
149  N ND2 . ASN A 46  ? 0.58193 0.61219 0.80890 0.08031  0.15496  0.03641  69  ASN A ND2 
150  N N   . ASN A 47  ? 0.53751 0.56288 0.74725 0.07322  0.14592  0.00502  70  ASN A N   
151  C CA  . ASN A 47  ? 0.45288 0.48216 0.65520 0.07671  0.14372  0.00181  70  ASN A CA  
152  C C   . ASN A 47  ? 0.54496 0.57636 0.73751 0.07779  0.14238  -0.00043 70  ASN A C   
153  O O   . ASN A 47  ? 0.67859 0.71249 0.86468 0.07975  0.14016  -0.00458 70  ASN A O   
154  C CB  . ASN A 47  ? 0.44924 0.47568 0.65278 0.07337  0.14194  -0.00529 70  ASN A CB  
155  C CG  . ASN A 47  ? 0.51517 0.53643 0.71840 0.06673  0.14119  -0.01142 70  ASN A CG  
156  O OD1 . ASN A 47  ? 0.67025 0.68977 0.87241 0.06451  0.14201  -0.01057 70  ASN A OD1 
157  N ND2 . ASN A 47  ? 0.63569 0.65471 0.83980 0.06354  0.13957  -0.01750 70  ASN A ND2 
158  N N   . GLY A 48  ? 0.41724 0.44770 0.60886 0.07657  0.14359  0.00217  71  GLY A N   
159  C CA  . GLY A 48  ? 0.50077 0.53296 0.68370 0.07743  0.14244  0.00038  71  GLY A CA  
160  C C   . GLY A 48  ? 0.62399 0.65190 0.80363 0.07194  0.14087  -0.00695 71  GLY A C   
161  O O   . GLY A 48  ? 0.58415 0.61274 0.75754 0.07197  0.14015  -0.00810 71  GLY A O   
162  N N   . GLN A 49  ? 0.44416 0.46791 0.62786 0.06724  0.14026  -0.01176 72  GLN A N   
163  C CA  . GLN A 49  ? 0.41291 0.43305 0.59349 0.06195  0.13858  -0.01863 72  GLN A CA  
164  C C   . GLN A 49  ? 0.40397 0.42022 0.58701 0.05734  0.14000  -0.01792 72  GLN A C   
165  O O   . GLN A 49  ? 0.54714 0.56177 0.73712 0.05644  0.14218  -0.01372 72  GLN A O   
166  C CB  . GLN A 49  ? 0.50757 0.52531 0.69131 0.05872  0.13726  -0.02393 72  GLN A CB  
167  C CG  . GLN A 49  ? 0.58018 0.60150 0.76061 0.06265  0.13540  -0.02592 72  GLN A CG  
168  C CD  . GLN A 49  ? 0.65611 0.67508 0.83849 0.05899  0.13375  -0.03186 72  GLN A CD  
169  O OE1 . GLN A 49  ? 0.85381 0.86870 1.04010 0.05357  0.13398  -0.03448 72  GLN A OE1 
170  N NE2 . GLN A 49  ? 1.04757 1.06943 1.22727 0.06205  0.13201  -0.03401 72  GLN A NE2 
171  N N   . CYS A 50  ? 0.35755 0.37233 0.53507 0.05439  0.13864  -0.02211 73  CYS A N   
172  C CA  . CYS A 50  ? 0.32906 0.34005 0.50808 0.04943  0.13952  -0.02271 73  CYS A CA  
173  C C   . CYS A 50  ? 0.45258 0.45939 0.63718 0.04368  0.13925  -0.02700 73  CYS A C   
174  O O   . CYS A 50  ? 0.52360 0.53030 0.70854 0.04284  0.13770  -0.03109 73  CYS A O   
175  C CB  . CYS A 50  ? 0.29946 0.31065 0.47052 0.04845  0.13793  -0.02583 73  CYS A CB  
176  S SG  . CYS A 50  ? 0.32159 0.33828 0.48534 0.05550  0.13769  -0.02190 73  CYS A SG  
177  N N   . PHE A 51  ? 0.43663 0.44019 0.62544 0.03968  0.14064  -0.02624 74  PHE A N   
178  C CA  . PHE A 51  ? 0.51889 0.51883 0.71354 0.03438  0.14053  -0.02998 74  PHE A CA  
179  C C   . PHE A 51  ? 0.35943 0.35654 0.55317 0.02948  0.14064  -0.03197 74  PHE A C   
180  O O   . PHE A 51  ? 0.42358 0.42069 0.61634 0.03018  0.14198  -0.02826 74  PHE A O   
181  C CB  . PHE A 51  ? 0.54332 0.54225 0.74754 0.03496  0.14247  -0.02631 74  PHE A CB  
182  C CG  . PHE A 51  ? 0.39094 0.38613 0.60172 0.02947  0.14255  -0.02984 74  PHE A CG  
183  C CD1 . PHE A 51  ? 0.25830 0.25282 0.47072 0.02731  0.14099  -0.03491 74  PHE A CD1 
184  C CD2 . PHE A 51  ? 0.28864 0.28127 0.50404 0.02664  0.14410  -0.02813 74  PHE A CD2 
185  C CE1 . PHE A 51  ? 0.41771 0.40935 0.63601 0.02250  0.14093  -0.03831 74  PHE A CE1 
186  C CE2 . PHE A 51  ? 0.31808 0.30767 0.53956 0.02186  0.14402  -0.03165 74  PHE A CE2 
187  C CZ  . PHE A 51  ? 0.47595 0.46517 0.69882 0.01983  0.14242  -0.03679 74  PHE A CZ  
188  N N   . CYS A 52  ? 0.33741 0.33246 0.53136 0.02462  0.13918  -0.03773 75  CYS A N   
189  C CA  . CYS A 52  ? 0.30864 0.30101 0.50308 0.01955  0.13929  -0.03987 75  CYS A CA  
190  C C   . CYS A 52  ? 0.38017 0.37098 0.57701 0.01481  0.13786  -0.04571 75  CYS A C   
191  O O   . CYS A 52  ? 0.37322 0.36528 0.56708 0.01483  0.13598  -0.04933 75  CYS A O   
192  C CB  . CYS A 52  ? 0.29868 0.29170 0.48500 0.01925  0.13837  -0.04063 75  CYS A CB  
193  S SG  . CYS A 52  ? 0.40714 0.39737 0.59417 0.01460  0.13932  -0.04057 75  CYS A SG  
194  N N   . LEU A 53  ? 0.39350 0.38185 0.59593 0.01089  0.13871  -0.04659 76  LEU A N   
195  C CA  . LEU A 53  ? 0.47747 0.46479 0.68268 0.00647  0.13744  -0.05201 76  LEU A CA  
196  C C   . LEU A 53  ? 0.56278 0.55071 0.76100 0.00353  0.13537  -0.05647 76  LEU A C   
197  O O   . LEU A 53  ? 0.64901 0.63773 0.84661 0.00169  0.13366  -0.06078 76  LEU A O   
198  C CB  . LEU A 53  ? 0.28318 0.26802 0.49567 0.00317  0.13873  -0.05201 76  LEU A CB  
199  C CG  . LEU A 53  ? 0.28635 0.27036 0.50801 0.00486  0.14024  -0.04937 76  LEU A CG  
200  C CD1 . LEU A 53  ? 0.49442 0.47592 0.72319 0.00147  0.14134  -0.04970 76  LEU A CD1 
201  C CD2 . LEU A 53  ? 0.51635 0.50130 0.74035 0.00511  0.13899  -0.05253 76  LEU A CD2 
202  N N   . ALA A 54  ? 0.43396 0.42162 0.62722 0.00301  0.13551  -0.05532 77  ALA A N   
203  C CA  . ALA A 54  ? 0.49698 0.48503 0.68425 -0.00002 0.13367  -0.05914 77  ALA A CA  
204  C C   . ALA A 54  ? 0.51668 0.50685 0.69943 0.00168  0.13170  -0.06154 77  ALA A C   
205  O O   . ALA A 54  ? 0.56133 0.55202 0.74184 -0.00144 0.12994  -0.06578 77  ALA A O   
206  C CB  . ALA A 54  ? 0.46456 0.45219 0.64707 0.00022  0.13420  -0.05677 77  ALA A CB  
207  N N   . TRP A 55  ? 0.49429 0.48595 0.67582 0.00668  0.13194  -0.05878 78  TRP A N   
208  C CA  . TRP A 55  ? 0.48992 0.48369 0.66721 0.00879  0.12999  -0.06097 78  TRP A CA  
209  C C   . TRP A 55  ? 0.57427 0.56839 0.75502 0.00694  0.12888  -0.06467 78  TRP A C   
210  O O   . TRP A 55  ? 0.66333 0.65893 0.84074 0.00696  0.12690  -0.06776 78  TRP A O   
211  C CB  . TRP A 55  ? 0.31330 0.30897 0.48877 0.01491  0.13054  -0.05709 78  TRP A CB  
212  C CG  . TRP A 55  ? 0.28744 0.28356 0.45891 0.01743  0.13145  -0.05342 78  TRP A CG  
213  C CD1 . TRP A 55  ? 0.31811 0.31338 0.48557 0.01515  0.13110  -0.05413 78  TRP A CD1 
214  C CD2 . TRP A 55  ? 0.31793 0.31588 0.48888 0.02292  0.13278  -0.04837 78  TRP A CD2 
215  N NE1 . TRP A 55  ? 0.35656 0.35287 0.52101 0.01885  0.13213  -0.04998 78  TRP A NE1 
216  C CE2 . TRP A 55  ? 0.39534 0.39348 0.56181 0.02369  0.13318  -0.04633 78  TRP A CE2 
217  C CE3 . TRP A 55  ? 0.49514 0.49485 0.66906 0.02734  0.13370  -0.04520 78  TRP A CE3 
218  C CZ2 . TRP A 55  ? 0.30556 0.30586 0.47033 0.02876  0.13444  -0.04128 78  TRP A CZ2 
219  C CZ3 . TRP A 55  ? 0.46555 0.46748 0.63786 0.03239  0.13499  -0.03998 78  TRP A CZ3 
220  C CH2 . TRP A 55  ? 0.27698 0.27931 0.44468 0.03307  0.13534  -0.03809 78  TRP A CH2 
221  N N   . LEU A 56  ? 0.58233 0.57522 0.76989 0.00545  0.13004  -0.06448 79  LEU A N   
222  C CA  . LEU A 56  ? 0.54432 0.53783 0.73545 0.00440  0.12906  -0.06763 79  LEU A CA  
223  C C   . LEU A 56  ? 0.55572 0.54895 0.74771 -0.00109 0.12790  -0.07240 79  LEU A C   
224  O O   . LEU A 56  ? 0.85798 0.85202 1.05282 -0.00238 0.12698  -0.07540 79  LEU A O   
225  C CB  . LEU A 56  ? 0.51589 0.50852 0.71448 0.00609  0.13076  -0.06505 79  LEU A CB  
226  C CG  . LEU A 56  ? 0.42606 0.41925 0.62500 0.01153  0.13233  -0.05951 79  LEU A CG  
227  C CD1 . LEU A 56  ? 0.45107 0.44279 0.65854 0.01211  0.13434  -0.05654 79  LEU A CD1 
228  C CD2 . LEU A 56  ? 0.47355 0.46926 0.66895 0.01570  0.13111  -0.05950 79  LEU A CD2 
229  N N   . LYS A 57  ? 0.43061 0.42296 0.62042 -0.00422 0.12798  -0.07302 80  LYS A N   
230  C CA  . LYS A 57  ? 0.61936 0.61214 0.80919 -0.00919 0.12677  -0.07740 80  LYS A CA  
231  C C   . LYS A 57  ? 0.72900 0.72401 0.91545 -0.00939 0.12463  -0.08065 80  LYS A C   
232  O O   . LYS A 57  ? 0.62284 0.61871 0.80466 -0.00647 0.12386  -0.07974 80  LYS A O   
233  C CB  . LYS A 57  ? 0.53850 0.53035 0.72515 -0.01180 0.12701  -0.07713 80  LYS A CB  
234  C CG  . LYS A 57  ? 0.51834 0.50806 0.70936 -0.01276 0.12891  -0.07494 80  LYS A CG  
235  C CD  . LYS A 57  ? 0.55502 0.54389 0.74288 -0.01558 0.12901  -0.07499 80  LYS A CD  
236  C CE  . LYS A 57  ? 0.68575 0.67497 0.86681 -0.01338 0.12865  -0.07297 80  LYS A CE  
237  N NZ  . LYS A 57  ? 0.77600 0.76353 0.95618 -0.01292 0.13016  -0.06950 80  LYS A NZ  
238  N N   . SER A 58  ? 0.65063 0.64679 0.83949 -0.01278 0.12362  -0.08454 81  SER A N   
239  C CA  . SER A 58  ? 0.60474 0.60320 0.79108 -0.01311 0.12166  -0.08757 81  SER A CA  
240  C C   . SER A 58  ? 0.79276 0.79189 0.97322 -0.01417 0.12055  -0.08829 81  SER A C   
241  O O   . SER A 58  ? 0.68879 0.68703 0.86772 -0.01641 0.12103  -0.08782 81  SER A O   
242  C CB  . SER A 58  ? 0.84924 0.84920 1.03941 -0.01674 0.12089  -0.09150 81  SER A CB  
243  O OG  . SER A 58  ? 1.03463 1.03477 1.22459 -0.02101 0.12085  -0.09325 81  SER A OG  
244  N N   . ASN A 59  ? 0.73886 0.73958 0.91630 -0.01245 0.11900  -0.08949 82  ASN A N   
245  C CA  . ASN A 59  ? 0.64780 0.64948 0.82060 -0.01357 0.11762  -0.09087 82  ASN A CA  
246  C C   . ASN A 59  ? 0.89298 0.89652 1.06682 -0.01824 0.11656  -0.09465 82  ASN A C   
247  O O   . ASN A 59  ? 0.80575 0.81004 0.97663 -0.01999 0.11568  -0.09577 82  ASN A O   
248  C CB  . ASN A 59  ? 0.89721 0.89991 1.06684 -0.00961 0.11626  -0.09080 82  ASN A CB  
249  C CG  . ASN A 59  ? 0.71745 0.71896 0.88517 -0.00467 0.11722  -0.08696 82  ASN A CG  
250  O OD1 . ASN A 59  ? 0.49261 0.49259 0.65931 -0.00443 0.11854  -0.08435 82  ASN A OD1 
251  N ND2 . ASN A 59  ? 0.60285 0.60539 0.77013 -0.00060 0.11657  -0.08653 82  ASN A ND2 
252  N N   . GLY A 60  ? 0.93973 0.94426 1.11789 -0.02020 0.11666  -0.09659 83  GLY A N   
253  C CA  . GLY A 60  ? 0.69198 0.69871 0.87145 -0.02457 0.11587  -0.09998 83  GLY A CA  
254  C C   . GLY A 60  ? 0.70671 0.71559 0.88947 -0.02478 0.11504  -0.10256 83  GLY A C   
255  O O   . GLY A 60  ? 0.69067 0.69907 0.87500 -0.02167 0.11515  -0.10169 83  GLY A O   
256  N N   . THR A 61  ? 0.85021 0.86168 1.03396 -0.02846 0.11423  -0.10569 84  THR A N   
257  C CA  . THR A 61  ? 1.01080 1.02492 1.19764 -0.02933 0.11337  -0.10858 84  THR A CA  
258  C C   . THR A 61  ? 0.94845 0.96401 1.13372 -0.02719 0.11199  -0.10940 84  THR A C   
259  O O   . THR A 61  ? 0.87413 0.88916 1.05582 -0.02571 0.11142  -0.10844 84  THR A O   
260  C CB  . THR A 61  ? 1.00134 1.01821 1.18928 -0.03383 0.11294  -0.11154 84  THR A CB  
261  O OG1 . THR A 61  ? 0.97301 0.99191 1.15824 -0.03516 0.11187  -0.11276 84  THR A OG1 
262  C CG2 . THR A 61  ? 0.56169 0.57703 0.74963 -0.03595 0.11401  -0.11067 84  THR A CG2 
263  N N   . ASN A 62  ? 1.14620 0.93927 1.57914 -0.08438 0.44409  -0.15171 85  ASN A N   
264  C CA  . ASN A 62  ? 1.05153 0.86072 1.48638 -0.07674 0.44087  -0.13703 85  ASN A CA  
265  C C   . ASN A 62  ? 0.97913 0.80327 1.40248 -0.07616 0.42849  -0.14082 85  ASN A C   
266  O O   . ASN A 62  ? 0.85479 0.69711 1.27558 -0.07422 0.42124  -0.13138 85  ASN A O   
267  C CB  . ASN A 62  ? 1.17990 0.97928 1.62523 -0.06593 0.45167  -0.12767 85  ASN A CB  
268  C CG  . ASN A 62  ? 1.33753 1.12755 1.79586 -0.06557 0.46322  -0.11819 85  ASN A CG  
269  O OD1 . ASN A 62  ? 1.68154 1.46990 2.14672 -0.05701 0.46745  -0.10487 85  ASN A OD1 
270  N ND2 . ASN A 62  ? 0.98206 0.76407 1.43901 -0.07545 0.46305  -0.12352 85  ASN A ND2 
271  N N   . ALA A 63  ? 1.06936 0.88640 1.48530 -0.07859 0.42522  -0.15386 86  ALA A N   
272  C CA  . ALA A 63  ? 1.05331 0.88371 1.45836 -0.07920 0.41367  -0.15821 86  ALA A CA  
273  C C   . ALA A 63  ? 1.08017 0.92400 1.47713 -0.08674 0.40329  -0.16216 86  ALA A C   
274  O O   . ALA A 63  ? 0.87387 0.73460 1.26517 -0.08536 0.39455  -0.15781 86  ALA A O   
275  C CB  . ALA A 63  ? 0.95273 0.77341 1.35149 -0.08180 0.41159  -0.17025 86  ALA A CB  
276  N N   . GLU A 64  ? 1.18744 1.02429 1.58346 -0.09475 0.40397  -0.17054 87  GLU A N   
277  C CA  . GLU A 64  ? 0.84325 0.69273 1.23153 -0.10128 0.39444  -0.17449 87  GLU A CA  
278  C C   . GLU A 64  ? 0.81730 0.68233 1.20843 -0.09772 0.39220  -0.15931 87  GLU A C   
279  O O   . GLU A 64  ? 0.78276 0.66434 1.16609 -0.09903 0.38159  -0.15793 87  GLU A O   
280  C CB  . GLU A 64  ? 0.63902 0.47804 1.02743 -0.10972 0.39734  -0.18495 87  GLU A CB  
281  C CG  . GLU A 64  ? 0.56246 0.39362 0.94490 -0.11667 0.39395  -0.19921 87  GLU A CG  
282  C CD  . GLU A 64  ? 0.75119 0.57643 1.13430 -0.12655 0.39601  -0.20828 87  GLU A CD  
283  O OE1 . GLU A 64  ? 0.76218 0.57819 1.15323 -0.12624 0.40553  -0.20502 87  GLU A OE1 
284  O OE2 . GLU A 64  ? 0.87075 0.70432 1.24697 -0.13436 0.38812  -0.21729 87  GLU A OE2 
285  N N   . LYS A 65  ? 0.89263 0.75255 1.29478 -0.09367 0.40158  -0.14726 88  LYS A N   
286  C CA  . LYS A 65  ? 0.95000 0.82441 1.35488 -0.09096 0.39867  -0.13120 88  LYS A CA  
287  C C   . LYS A 65  ? 0.90552 0.79435 1.30764 -0.08484 0.39252  -0.12272 88  LYS A C   
288  O O   . LYS A 65  ? 0.95221 0.85803 1.34926 -0.08566 0.38338  -0.11613 88  LYS A O   
289  C CB  . LYS A 65  ? 1.04509 0.90948 1.46279 -0.08751 0.41026  -0.11952 88  LYS A CB  
290  C CG  . LYS A 65  ? 1.10445 0.98267 1.52528 -0.08468 0.40729  -0.10175 88  LYS A CG  
291  C CD  . LYS A 65  ? 1.09505 0.98230 1.51167 -0.09141 0.40107  -0.10003 88  LYS A CD  
292  C CE  . LYS A 65  ? 1.23738 1.12715 1.66242 -0.08843 0.40492  -0.08219 88  LYS A CE  
293  N NZ  . LYS A 65  ? 0.96968 0.87971 1.38891 -0.08963 0.39436  -0.07320 88  LYS A NZ  
294  N N   . LEU A 66  ? 1.06970 0.95260 1.47502 -0.07868 0.39734  -0.12246 89  LEU A N   
295  C CA  . LEU A 66  ? 1.27340 1.17099 1.67682 -0.07286 0.39210  -0.11336 89  LEU A CA  
296  C C   . LEU A 66  ? 1.04090 0.95184 1.43179 -0.07791 0.37917  -0.12107 89  LEU A C   
297  O O   . LEU A 66  ? 1.04581 0.97380 1.43339 -0.07723 0.37138  -0.11216 89  LEU A O   
298  C CB  . LEU A 66  ? 1.15184 1.04103 1.55984 -0.06558 0.39928  -0.11356 89  LEU A CB  
299  C CG  . LEU A 66  ? 0.92968 0.83383 1.33826 -0.05829 0.39634  -0.10199 89  LEU A CG  
300  C CD1 . LEU A 66  ? 0.81647 0.72782 1.23383 -0.05314 0.39967  -0.08370 89  LEU A CD1 
301  C CD2 . LEU A 66  ? 1.07337 0.96941 1.48412 -0.05194 0.40225  -0.10575 89  LEU A CD2 
302  N N   . ALA A 67  ? 1.02024 0.92304 1.40411 -0.08336 0.37671  -0.13773 90  ALA A N   
303  C CA  . ALA A 67  ? 0.81498 0.72828 1.18691 -0.08859 0.36485  -0.14691 90  ALA A CA  
304  C C   . ALA A 67  ? 0.89021 0.81663 1.25785 -0.09284 0.35710  -0.14373 90  ALA A C   
305  O O   . ALA A 67  ? 0.96789 0.90938 1.32858 -0.09400 0.34745  -0.14212 90  ALA A O   
306  C CB  . ALA A 67  ? 0.73670 0.63702 1.10263 -0.09441 0.36405  -0.16511 90  ALA A CB  
307  N N   . ALA A 68  ? 0.96840 0.88968 1.34003 -0.09543 0.36114  -0.14275 91  ALA A N   
308  C CA  . ALA A 68  ? 0.71625 0.65022 1.08318 -0.09964 0.35363  -0.14076 91  ALA A CA  
309  C C   . ALA A 68  ? 0.93881 0.88834 1.30811 -0.09535 0.35013  -0.12329 91  ALA A C   
310  O O   . ALA A 68  ? 1.04347 1.00798 1.40586 -0.09772 0.34041  -0.12210 91  ALA A O   
311  C CB  . ALA A 68  ? 0.72032 0.64578 1.09130 -0.10350 0.35924  -0.14308 91  ALA A CB  
312  N N   . ASN A 69  ? 0.91623 0.86241 1.29532 -0.08901 0.35788  -0.10974 92  ASN A N   
313  C CA  . ASN A 69  ? 0.92867 0.88932 1.31034 -0.08491 0.35463  -0.09244 92  ASN A CA  
314  C C   . ASN A 69  ? 0.99747 0.97097 1.37329 -0.08336 0.34672  -0.09071 92  ASN A C   
315  O O   . ASN A 69  ? 0.94329 0.93232 1.31625 -0.08344 0.33925  -0.08134 92  ASN A O   
316  C CB  . ASN A 69  ? 1.04419 0.99764 1.43791 -0.07830 0.36503  -0.07888 92  ASN A CB  
317  C CG  . ASN A 69  ? 1.16436 1.10506 1.56430 -0.08064 0.37295  -0.07972 92  ASN A CG  
318  O OD1 . ASN A 69  ? 1.04901 0.98285 1.44502 -0.08681 0.37267  -0.09277 92  ASN A OD1 
319  N ND2 . ASN A 69  ? 1.32574 1.26366 1.73544 -0.07603 0.37987  -0.06553 92  ASN A ND2 
320  N N   . ILE A 70  ? 0.90237 0.86987 1.27618 -0.08244 0.34806  -0.09964 93  ILE A N   
321  C CA  . ILE A 70  ? 0.86272 0.84261 1.23092 -0.08182 0.34068  -0.09840 93  ILE A CA  
322  C C   . ILE A 70  ? 0.79006 0.77957 1.14728 -0.08889 0.32926  -0.10744 93  ILE A C   
323  O O   . ILE A 70  ? 0.94483 0.94979 1.29851 -0.08969 0.32129  -0.09984 93  ILE A O   
324  C CB  . ILE A 70  ? 0.92507 0.89618 1.29359 -0.07933 0.34511  -0.10630 93  ILE A CB  
325  C CG1 . ILE A 70  ? 0.88403 0.84924 1.26361 -0.07101 0.35573  -0.09530 93  ILE A CG1 
326  C CG2 . ILE A 70  ? 0.67415 0.65815 1.03500 -0.08098 0.33631  -0.10825 93  ILE A CG2 
327  C CD1 . ILE A 70  ? 1.19700 1.17544 1.58218 -0.06607 0.35515  -0.07585 93  ILE A CD1 
328  N N   . LEU A 71  ? 0.77579 0.75629 1.12760 -0.09422 0.32828  -0.12397 94  LEU A N   
329  C CA  . LEU A 71  ? 0.77085 0.76010 1.11222 -0.10060 0.31768  -0.13408 94  LEU A CA  
330  C C   . LEU A 71  ? 0.78649 0.78855 1.12723 -0.10190 0.31256  -0.12528 94  LEU A C   
331  O O   . LEU A 71  ? 0.72978 0.74480 1.06349 -0.10518 0.30292  -0.12676 94  LEU A O   
332  C CB  . LEU A 71  ? 0.90997 0.88720 1.24647 -0.10570 0.31818  -0.15263 94  LEU A CB  
333  C CG  . LEU A 71  ? 0.82650 0.79236 1.15918 -0.10715 0.31925  -0.16669 94  LEU A CG  
334  C CD1 . LEU A 71  ? 0.74610 0.70144 1.07419 -0.11291 0.31888  -0.18322 94  LEU A CD1 
335  C CD2 . LEU A 71  ? 0.79250 0.76976 1.11721 -0.10893 0.30995  -0.16973 94  LEU A CD2 
336  N N   . GLN A 72  ? 0.76008 0.75878 1.10811 -0.09966 0.31881  -0.11630 95  GLN A N   
337  C CA  . GLN A 72  ? 0.70484 0.71620 1.05257 -0.10053 0.31428  -0.10686 95  GLN A CA  
338  C C   . GLN A 72  ? 0.76430 0.78962 1.11312 -0.09725 0.30971  -0.09136 95  GLN A C   
339  O O   . GLN A 72  ? 0.77384 0.81298 1.11716 -0.09999 0.30090  -0.08956 95  GLN A O   
340  C CB  . GLN A 72  ? 0.71453 0.71876 1.07017 -0.09911 0.32242  -0.10011 95  GLN A CB  
341  C CG  . GLN A 72  ? 0.91860 0.91417 1.27183 -0.10430 0.32442  -0.11430 95  GLN A CG  
342  C CD  . GLN A 72  ? 0.87228 0.85729 1.23451 -0.10336 0.33427  -0.10843 95  GLN A CD  
343  O OE1 . GLN A 72  ? 0.84202 0.82428 1.20318 -0.10791 0.33533  -0.11540 95  GLN A OE1 
344  N NE2 . GLN A 72  ? 0.98951 0.96889 1.36080 -0.09763 0.34159  -0.09569 95  GLN A NE2 
345  N N   . TRP A 73  ? 0.81307 0.83534 1.16919 -0.09138 0.31570  -0.08007 96  TRP A N   
346  C CA  . TRP A 73  ? 0.77416 0.81001 1.13144 -0.08830 0.31144  -0.06500 96  TRP A CA  
347  C C   . TRP A 73  ? 0.76211 0.80800 1.11065 -0.09256 0.30162  -0.07132 96  TRP A C   
348  O O   . TRP A 73  ? 0.72895 0.78871 1.07398 -0.09418 0.29339  -0.06350 96  TRP A O   
349  C CB  . TRP A 73  ? 0.62730 0.65820 0.99350 -0.08112 0.31978  -0.05424 96  TRP A CB  
350  C CG  . TRP A 73  ? 0.78616 0.81374 1.16117 -0.07679 0.32658  -0.04146 96  TRP A CG  
351  C CD1 . TRP A 73  ? 1.04953 1.06191 1.43190 -0.07440 0.33692  -0.04313 96  TRP A CD1 
352  C CD2 . TRP A 73  ? 0.77488 0.81431 1.15207 -0.07500 0.32323  -0.02527 96  TRP A CD2 
353  N NE1 . TRP A 73  ? 1.00885 1.02295 1.39803 -0.07123 0.34029  -0.02877 96  TRP A NE1 
354  C CE2 . TRP A 73  ? 0.79284 0.82360 1.17873 -0.07137 0.33186  -0.01769 96  TRP A CE2 
355  C CE3 . TRP A 73  ? 0.83364 0.88978 1.20634 -0.07634 0.31376  -0.01632 96  TRP A CE3 
356  C CZ2 . TRP A 73  ? 0.82390 0.86247 1.21369 -0.06887 0.33105  -0.00173 96  TRP A CZ2 
357  C CZ3 . TRP A 73  ? 0.83497 0.89875 1.21153 -0.07369 0.31304  -0.00040 96  TRP A CZ3 
358  C CH2 . TRP A 73  ? 0.91584 0.97102 1.30066 -0.06991 0.32150  0.00663  96  TRP A CH2 
359  N N   . ILE A 74  ? 0.77541 0.81392 1.11996 -0.09465 0.30190  -0.08533 97  ILE A N   
360  C CA  . ILE A 74  ? 0.68884 0.73462 1.02255 -0.09907 0.29066  -0.09257 97  ILE A CA  
361  C C   . ILE A 74  ? 0.67768 0.72946 0.99921 -0.10329 0.27746  -0.09742 97  ILE A C   
362  O O   . ILE A 74  ? 0.64646 0.70794 0.95755 -0.10444 0.26385  -0.09262 97  ILE A O   
363  C CB  . ILE A 74  ? 0.55484 0.58996 0.88570 -0.10124 0.29342  -0.10919 97  ILE A CB  
364  C CG1 . ILE A 74  ? 0.42584 0.45808 0.76404 -0.09593 0.30142  -0.10269 97  ILE A CG1 
365  C CG2 . ILE A 74  ? 0.54721 0.58582 0.86160 -0.10640 0.27780  -0.11988 97  ILE A CG2 
366  C CD1 . ILE A 74  ? 0.59570 0.61789 0.93018 -0.09743 0.30332  -0.11793 97  ILE A CD1 
367  N N   . THR A 75  ? 0.68487 0.73123 1.00742 -0.10551 0.28115  -0.10673 98  THR A N   
368  C CA  . THR A 75  ? 0.70885 0.76081 1.01964 -0.10907 0.26933  -0.11402 98  THR A CA  
369  C C   . THR A 75  ? 0.69615 0.76016 1.00701 -0.10697 0.26428  -0.09862 98  THR A C   
370  O O   . THR A 75  ? 0.63292 0.70520 0.93113 -0.10835 0.24986  -0.09923 98  THR A O   
371  C CB  . THR A 75  ? 0.82708 0.87133 1.14015 -0.11201 0.27587  -0.12777 98  THR A CB  
372  O OG1 . THR A 75  ? 0.96389 0.99668 1.27595 -0.11415 0.27972  -0.14255 98  THR A OG1 
373  C CG2 . THR A 75  ? 0.60193 0.65364 0.90271 -0.11500 0.26366  -0.13586 98  THR A CG2 
374  N N   . PHE A 76  ? 0.71756 0.78221 1.04216 -0.10341 0.27561  -0.08460 99  PHE A N   
375  C CA  . PHE A 76  ? 0.63358 0.70970 0.95889 -0.10133 0.27138  -0.06922 99  PHE A CA  
376  C C   . PHE A 76  ? 0.75904 0.84416 1.07687 -0.09998 0.25986  -0.05923 99  PHE A C   
377  O O   . PHE A 76  ? 0.64278 0.73724 0.95037 -0.10072 0.24701  -0.05555 99  PHE A O   
378  C CB  . PHE A 76  ? 0.89419 0.96808 1.23613 -0.09743 0.28600  -0.05510 99  PHE A CB  
379  C CG  . PHE A 76  ? 0.86475 0.95034 1.20873 -0.09475 0.28257  -0.03723 99  PHE A CG  
380  C CD1 . PHE A 76  ? 0.82872 0.92119 1.16830 -0.09660 0.27752  -0.03755 99  PHE A CD1 
381  C CD2 . PHE A 76  ? 0.83794 0.92910 1.18679 -0.09058 0.28297  -0.02081 99  PHE A CD2 
382  C CE1 . PHE A 76  ? 0.94366 1.04687 1.28436 -0.09437 0.27397  -0.02207 99  PHE A CE1 
383  C CE2 . PHE A 76  ? 0.94652 1.04866 1.29651 -0.08846 0.27903  -0.00468 99  PHE A CE2 
384  C CZ  . PHE A 76  ? 0.86406 0.97176 1.20976 -0.09043 0.27445  -0.00558 99  PHE A CZ  
385  N N   . ALA A 77  ? 0.86126 0.94374 1.18379 -0.09804 0.26417  -0.05493 100 ALA A N   
386  C CA  . ALA A 77  ? 0.71400 0.80536 1.03080 -0.09720 0.25449  -0.04444 100 ALA A CA  
387  C C   . ALA A 77  ? 0.69795 0.79132 0.99657 -0.10178 0.23732  -0.05511 100 ALA A C   
388  O O   . ALA A 77  ? 0.67535 0.77767 0.96412 -0.10251 0.22384  -0.04764 100 ALA A O   
389  C CB  . ALA A 77  ? 0.40328 0.49161 0.72953 -0.09421 0.26415  -0.03980 100 ALA A CB  
390  N N   . LEU A 78  ? 0.74259 0.82684 1.03613 -0.10494 0.23724  -0.07288 101 LEU A N   
391  C CA  . LEU A 78  ? 0.66965 0.75412 0.94574 -0.10930 0.22105  -0.08397 101 LEU A CA  
392  C C   . LEU A 78  ? 0.58839 0.67727 0.85290 -0.11070 0.20890  -0.08803 101 LEU A C   
393  O O   . LEU A 78  ? 0.68689 0.78025 0.93647 -0.11265 0.19233  -0.08833 101 LEU A O   
394  C CB  . LEU A 78  ? 0.62478 0.69801 0.89927 -0.11208 0.22508  -0.10209 101 LEU A CB  
395  C CG  . LEU A 78  ? 0.66595 0.73557 0.92418 -0.11689 0.21150  -0.11707 101 LEU A CG  
396  C CD1 . LEU A 78  ? 0.56773 0.63849 0.81132 -0.11933 0.19760  -0.12722 101 LEU A CD1 
397  C CD2 . LEU A 78  ? 0.62763 0.70306 0.87978 -0.11799 0.20242  -0.10800 101 LEU A CD2 
398  N N   . SER A 79  ? 0.63866 0.72659 0.90950 -0.10966 0.21660  -0.09096 102 SER A N   
399  C CA  . SER A 79  ? 0.62980 0.72366 0.89040 -0.11024 0.20601  -0.09470 102 SER A CA  
400  C C   . SER A 79  ? 0.67637 0.78126 0.93452 -0.10779 0.19813  -0.07714 102 SER A C   
401  O O   . SER A 79  ? 0.71965 0.82999 0.96343 -0.10836 0.18270  -0.07877 102 SER A O   
402  C CB  . SER A 79  ? 0.62349 0.71546 0.89260 -0.11006 0.21708  -0.10068 102 SER A CB  
403  O OG  . SER A 79  ? 0.82072 0.92031 1.09864 -0.10712 0.22237  -0.08534 102 SER A OG  
404  N N   . ALA A 80  ? 0.83609 0.94400 1.10783 -0.10476 0.20830  -0.06034 103 ALA A N   
405  C CA  . ALA A 80  ? 0.73430 0.85270 1.00485 -0.10244 0.20168  -0.04251 103 ALA A CA  
406  C C   . ALA A 80  ? 0.82055 0.94187 1.07846 -0.10429 0.18677  -0.03923 103 ALA A C   
407  O O   . ALA A 80  ? 0.80180 0.93028 1.04896 -0.10432 0.17292  -0.03226 103 ALA A O   
408  C CB  . ALA A 80  ? 0.78629 0.90670 1.07498 -0.09860 0.21680  -0.02590 103 ALA A CB  
409  N N   . LEU A 81  ? 0.91622 1.03202 1.17494 -0.10606 0.18916  -0.04403 104 LEU A N   
410  C CA  . LEU A 81  ? 0.72783 0.84603 0.97386 -0.10901 0.17469  -0.04221 104 LEU A CA  
411  C C   . LEU A 81  ? 0.85404 0.97009 1.08008 -0.11235 0.15657  -0.05534 104 LEU A C   
412  O O   . LEU A 81  ? 0.89528 1.01628 1.10826 -0.11369 0.14047  -0.04908 104 LEU A O   
413  C CB  . LEU A 81  ? 0.63274 0.74555 0.88344 -0.11049 0.18151  -0.04704 104 LEU A CB  
414  C CG  . LEU A 81  ? 0.84422 0.95968 1.11270 -0.10666 0.19738  -0.03396 104 LEU A CG  
415  C CD1 . LEU A 81  ? 0.74430 0.85781 1.01228 -0.10860 0.19835  -0.03756 104 LEU A CD1 
416  C CD2 . LEU A 81  ? 0.89920 1.02624 1.17159 -0.10388 0.19507  -0.01285 104 LEU A CD2 
417  N N   . CYS A 82  ? 0.94244 1.05082 1.16545 -0.11362 0.15858  -0.07371 105 CYS A N   
418  C CA  . CYS A 82  ? 0.77700 0.88320 0.98114 -0.11592 0.14181  -0.08744 105 CYS A CA  
419  C C   . CYS A 82  ? 0.78624 0.90058 0.98267 -0.11356 0.13130  -0.08009 105 CYS A C   
420  O O   . CYS A 82  ? 0.80285 0.91794 0.98155 -0.11490 0.11278  -0.08258 105 CYS A O   
421  C CB  . CYS A 82  ? 0.84780 0.94630 1.05263 -0.11687 0.14807  -0.10711 105 CYS A CB  
422  S SG  . CYS A 82  ? 0.94990 1.03726 1.15892 -0.12019 0.15645  -0.11970 105 CYS A SG  
423  N N   . LEU A 83  ? 0.68975 0.80976 0.89854 -0.11003 0.14231  -0.07128 106 LEU A N   
424  C CA  . LEU A 83  ? 0.59172 0.72010 0.79324 -0.10754 0.13275  -0.06475 106 LEU A CA  
425  C C   . LEU A 83  ? 0.90039 1.03396 1.09429 -0.10773 0.12016  -0.04932 106 LEU A C   
426  O O   . LEU A 83  ? 1.14663 1.28162 1.32291 -0.10825 0.10184  -0.05131 106 LEU A O   
427  C CB  . LEU A 83  ? 0.65788 0.79171 0.87554 -0.10425 0.14805  -0.05640 106 LEU A CB  
428  C CG  . LEU A 83  ? 0.84964 0.99174 1.06266 -0.10165 0.14322  -0.05580 106 LEU A CG  
429  C CD1 . LEU A 83  ? 0.53806 0.68542 0.76918 -0.09915 0.15936  -0.04275 106 LEU A CD1 
430  C CD2 . LEU A 83  ? 0.83971 0.98784 1.03683 -0.10053 0.12425  -0.04850 106 LEU A CD2 
431  N N   . MET A 84  ? 0.99155 1.12817 1.19852 -0.10710 0.12967  -0.03348 107 MET A N   
432  C CA  . MET A 84  ? 0.95954 1.10197 1.16068 -0.10785 0.11881  -0.01777 107 MET A CA  
433  C C   . MET A 84  ? 1.05797 1.19542 1.24090 -0.11246 0.10142  -0.02601 107 MET A C   
434  O O   . MET A 84  ? 1.15885 1.29919 1.32723 -0.11370 0.08414  -0.02001 107 MET A O   
435  C CB  . MET A 84  ? 0.93190 1.07849 1.15051 -0.10645 0.13279  -0.00149 107 MET A CB  
436  C CG  . MET A 84  ? 0.96168 1.11539 1.19444 -0.10189 0.14395  0.01315  107 MET A CG  
437  S SD  . MET A 84  ? 1.40125 1.55052 1.65286 -0.09889 0.16624  0.00728  107 MET A SD  
438  C CE  . MET A 84  ? 0.78850 0.94713 1.05555 -0.09432 0.17611  0.03079  107 MET A CE  
439  N N   . PHE A 85  ? 1.19677 1.32614 1.37996 -0.11525 0.10549  -0.03967 108 PHE A N   
440  C CA  . PHE A 85  ? 1.21867 1.34277 1.38540 -0.12021 0.08988  -0.04741 108 PHE A CA  
441  C C   . PHE A 85  ? 1.20251 1.32331 1.34829 -0.12085 0.07050  -0.05830 108 PHE A C   
442  O O   . PHE A 85  ? 1.30363 1.42353 1.43284 -0.12389 0.05200  -0.05568 108 PHE A O   
443  C CB  . PHE A 85  ? 1.18811 1.30368 1.35916 -0.12265 0.09874  -0.06218 108 PHE A CB  
444  C CG  . PHE A 85  ? 1.25175 1.36084 1.40486 -0.12798 0.08237  -0.07275 108 PHE A CG  
445  C CD1 . PHE A 85  ? 1.40022 1.51285 1.54540 -0.13169 0.07064  -0.06139 108 PHE A CD1 
446  C CD2 . PHE A 85  ? 1.08808 1.18796 1.23118 -0.12954 0.07735  -0.09344 108 PHE A CD2 
447  C CE1 . PHE A 85  ? 1.37322 1.47970 1.50140 -0.13723 0.05483  -0.07002 108 PHE A CE1 
448  C CE2 . PHE A 85  ? 1.08938 1.18271 1.21524 -0.13456 0.06137  -0.10268 108 PHE A CE2 
449  C CZ  . PHE A 85  ? 1.25601 1.35230 1.37424 -0.13858 0.04994  -0.09082 108 PHE A CZ  
450  N N   . TYR A 86  ? 1.13200 1.25100 1.27775 -0.11798 0.07404  -0.07074 109 TYR A N   
451  C CA  . TYR A 86  ? 1.09787 1.21496 1.22421 -0.11721 0.05636  -0.08157 109 TYR A CA  
452  C C   . TYR A 86  ? 1.22875 1.35357 1.34817 -0.11456 0.04538  -0.06736 109 TYR A C   
453  O O   . TYR A 86  ? 1.34687 1.46993 1.44705 -0.11405 0.02663  -0.07294 109 TYR A O   
454  C CB  . TYR A 86  ? 0.82345 0.93971 0.95344 -0.11434 0.06450  -0.09682 109 TYR A CB  
455  C CG  . TYR A 86  ? 0.98337 1.09157 1.11952 -0.11672 0.07518  -0.11262 109 TYR A CG  
456  C CD1 . TYR A 86  ? 0.99350 1.09354 1.12315 -0.12128 0.06985  -0.11932 109 TYR A CD1 
457  C CD2 . TYR A 86  ? 0.86875 0.97771 1.01734 -0.11474 0.09065  -0.12041 109 TYR A CD2 
458  C CE1 . TYR A 86  ? 0.80959 0.90214 0.94491 -0.12333 0.07979  -0.13381 109 TYR A CE1 
459  C CE2 . TYR A 86  ? 0.72380 0.82501 0.87799 -0.11705 0.10036  -0.13458 109 TYR A CE2 
460  C CZ  . TYR A 86  ? 0.77483 0.86772 0.92237 -0.12110 0.09499  -0.14143 109 TYR A CZ  
461  O OH  . TYR A 86  ? 0.88353 0.96856 1.03648 -0.12328 0.10466  -0.15570 109 TYR A OH  
462  N N   . GLY A 87  ? 1.19819 1.33081 1.46449 -0.16293 -0.07639 0.06843  110 GLY A N   
463  C CA  . GLY A 87  ? 1.17203 1.30706 1.44305 -0.16260 -0.08209 0.06644  110 GLY A CA  
464  C C   . GLY A 87  ? 1.44841 1.58377 1.72473 -0.16847 -0.08445 0.06773  110 GLY A C   
465  O O   . GLY A 87  ? 1.47828 1.61319 1.75706 -0.16877 -0.09008 0.06618  110 GLY A O   
466  N N   . TYR A 88  ? 1.57613 1.71217 1.85400 -0.17302 -0.08020 0.07044  111 TYR A N   
467  C CA  . TYR A 88  ? 1.48576 1.62255 1.76880 -0.17894 -0.08168 0.07189  111 TYR A CA  
468  C C   . TYR A 88  ? 1.55571 1.68101 1.83304 -0.18111 -0.08888 0.07149  111 TYR A C   
469  O O   . TYR A 88  ? 1.57387 1.68961 1.84224 -0.17881 -0.09150 0.07071  111 TYR A O   
470  C CB  . TYR A 88  ? 1.55253 1.69042 1.83620 -0.18299 -0.07546 0.07477  111 TYR A CB  
471  C CG  . TYR A 88  ? 1.62251 1.77191 1.91246 -0.18193 -0.06790 0.07544  111 TYR A CG  
472  C CD1 . TYR A 88  ? 1.56092 1.71860 1.85453 -0.17696 -0.06635 0.07360  111 TYR A CD1 
473  C CD2 . TYR A 88  ? 1.57701 1.72850 1.86857 -0.18568 -0.06217 0.07779  111 TYR A CD2 
474  C CE1 . TYR A 88  ? 1.52466 1.69239 1.82340 -0.17572 -0.05942 0.07405  111 TYR A CE1 
475  C CE2 . TYR A 88  ? 1.53907 1.70062 1.83579 -0.18446 -0.05518 0.07818  111 TYR A CE2 
476  C CZ  . TYR A 88  ? 1.48819 1.65778 1.78843 -0.17945 -0.05387 0.07630  111 TYR A CZ  
477  O OH  . TYR A 88  ? 1.51210 1.69138 1.81705 -0.17799 -0.04702 0.07650  111 TYR A OH  
478  N N   . CYS A 95  ? 0.57532 0.59973 0.75247 -0.14634 -0.12427 0.05300  118 CYS A N   
479  C CA  . CYS A 95  ? 1.01882 1.04392 1.19731 -0.15107 -0.11931 0.05661  118 CYS A CA  
480  C C   . CYS A 95  ? 0.92961 0.96825 1.11863 -0.15244 -0.11297 0.05861  118 CYS A C   
481  O O   . CYS A 95  ? 0.83278 0.87980 1.03051 -0.15293 -0.11363 0.05825  118 CYS A O   
482  C CB  . CYS A 95  ? 0.73020 0.74963 0.90876 -0.15648 -0.12233 0.05827  118 CYS A CB  
483  N N   . GLY A 96  ? 0.87156 0.91234 1.05960 -0.15288 -0.10668 0.06066  119 GLY A N   
484  C CA  . GLY A 96  ? 0.70811 0.76154 0.90505 -0.15319 -0.10014 0.06229  119 GLY A CA  
485  C C   . GLY A 96  ? 0.77431 0.83454 0.97276 -0.14755 -0.09851 0.06022  119 GLY A C   
486  O O   . GLY A 96  ? 0.64560 0.71663 0.85125 -0.14723 -0.09297 0.06138  119 GLY A O   
487  N N   . TRP A 97  ? 0.77850 0.83267 0.97006 -0.14291 -0.10303 0.05709  120 TRP A N   
488  C CA  . TRP A 97  ? 0.54566 0.60605 0.73851 -0.13732 -0.10223 0.05470  120 TRP A CA  
489  C C   . TRP A 97  ? 0.54409 0.60774 0.73482 -0.13502 -0.09575 0.05574  120 TRP A C   
490  O O   . TRP A 97  ? 0.60540 0.67785 0.80027 -0.13147 -0.09280 0.05486  120 TRP A O   
491  C CB  . TRP A 97  ? 0.64617 0.69831 0.83131 -0.13294 -0.10883 0.05087  120 TRP A CB  
492  C CG  . TRP A 97  ? 0.65743 0.69803 0.83056 -0.13101 -0.11001 0.05001  120 TRP A CG  
493  C CD1 . TRP A 97  ? 0.60335 0.63222 0.76889 -0.13304 -0.11385 0.05007  120 TRP A CD1 
494  C CD2 . TRP A 97  ? 0.51537 0.55496 0.68240 -0.12641 -0.10746 0.04875  120 TRP A CD2 
495  N NE1 . TRP A 97  ? 0.56165 0.58226 0.71669 -0.12998 -0.11375 0.04891  120 TRP A NE1 
496  C CE2 . TRP A 97  ? 0.60198 0.62893 0.75774 -0.12597 -0.10990 0.04808  120 TRP A CE2 
497  C CE3 . TRP A 97  ? 0.38715 0.43532 0.55701 -0.12256 -0.10328 0.04811  120 TRP A CE3 
498  C CZ2 . TRP A 97  ? 0.43534 0.45799 0.58266 -0.12195 -0.10833 0.04676  120 TRP A CZ2 
499  C CZ3 . TRP A 97  ? 0.54256 0.58656 0.70418 -0.11865 -0.10174 0.04690  120 TRP A CZ3 
500  C CH2 . TRP A 97  ? 0.40590 0.43721 0.55637 -0.11844 -0.10428 0.04622  120 TRP A CH2 
501  N N   . GLU A 98  ? 0.62875 0.68538 0.81284 -0.13681 -0.09336 0.05754  121 GLU A N   
502  C CA  . GLU A 98  ? 0.43034 0.48914 0.61140 -0.13445 -0.08721 0.05847  121 GLU A CA  
503  C C   . GLU A 98  ? 0.44485 0.51593 0.63504 -0.13586 -0.07972 0.06104  121 GLU A C   
504  O O   . GLU A 98  ? 0.39478 0.47272 0.58640 -0.13215 -0.07533 0.06070  121 GLU A O   
505  C CB  . GLU A 98  ? 0.32150 0.36928 0.49280 -0.13610 -0.08645 0.05972  121 GLU A CB  
506  C CG  . GLU A 98  ? 0.27996 0.31474 0.44169 -0.13512 -0.09370 0.05732  121 GLU A CG  
507  C CD  . GLU A 98  ? 0.40726 0.43499 0.56773 -0.14028 -0.09639 0.05889  121 GLU A CD  
508  O OE1 . GLU A 98  ? 0.60627 0.64014 0.77541 -0.14414 -0.09585 0.06055  121 GLU A OE1 
509  O OE2 . GLU A 98  ? 0.42458 0.44069 0.57527 -0.14039 -0.09903 0.05838  121 GLU A OE2 
510  N N   . GLU A 99  ? 0.63086 0.70478 0.82691 -0.14098 -0.07796 0.06349  122 GLU A N   
511  C CA  . GLU A 99  ? 0.45385 0.53947 0.65840 -0.14202 -0.07088 0.06556  122 GLU A CA  
512  C C   . GLU A 99  ? 0.48581 0.58228 0.69822 -0.13871 -0.07091 0.06381  122 GLU A C   
513  O O   . GLU A 99  ? 0.48119 0.58655 0.69735 -0.13637 -0.06490 0.06432  122 GLU A O   
514  C CB  . GLU A 99  ? 0.65558 0.74200 0.86492 -0.14810 -0.06971 0.06808  122 GLU A CB  
515  C CG  . GLU A 99  ? 0.63129 0.70672 0.83282 -0.15151 -0.06990 0.06971  122 GLU A CG  
516  C CD  . GLU A 99  ? 0.71727 0.78264 0.91464 -0.15351 -0.07795 0.06856  122 GLU A CD  
517  O OE1 . GLU A 99  ? 0.69847 0.76377 0.90003 -0.15816 -0.07970 0.06976  122 GLU A OE1 
518  O OE2 . GLU A 99  ? 0.75091 0.80836 0.94056 -0.15029 -0.08248 0.06632  122 GLU A OE2 
519  N N   . ILE A 100 ? 0.56542 0.66111 0.77997 -0.13821 -0.07749 0.06159  123 ILE A N   
520  C CA  . ILE A 100 ? 0.53783 0.64362 0.75989 -0.13525 -0.07775 0.05982  123 ILE A CA  
521  C C   . ILE A 100 ? 0.52225 0.62941 0.74032 -0.12888 -0.07701 0.05748  123 ILE A C   
522  O O   . ILE A 100 ? 0.56324 0.68032 0.78643 -0.12596 -0.07280 0.05715  123 ILE A O   
523  C CB  . ILE A 100 ? 0.49863 0.60324 0.72412 -0.13664 -0.08470 0.05813  123 ILE A CB  
524  C CG1 . ILE A 100 ? 0.29335 0.40050 0.52557 -0.14283 -0.08415 0.06058  123 ILE A CG1 
525  C CG2 . ILE A 100 ? 0.64495 0.75703 0.87478 -0.13193 -0.08633 0.05521  123 ILE A CG2 
526  C CD1 . ILE A 100 ? 0.64797 0.74608 0.87511 -0.14764 -0.08402 0.06299  123 ILE A CD1 
527  N N   . TYR A 101 ? 0.48899 0.58615 0.69756 -0.12649 -0.08097 0.05570  124 TYR A N   
528  C CA  . TYR A 101 ? 0.44051 0.53859 0.64487 -0.12035 -0.08071 0.05318  124 TYR A CA  
529  C C   . TYR A 101 ? 0.49532 0.59995 0.70048 -0.11865 -0.07265 0.05497  124 TYR A C   
530  O O   . TYR A 101 ? 0.49353 0.60626 0.70171 -0.11440 -0.06998 0.05371  124 TYR A O   
531  C CB  . TYR A 101 ? 0.38446 0.46989 0.57760 -0.11839 -0.08588 0.05106  124 TYR A CB  
532  C CG  . TYR A 101 ? 0.35642 0.44209 0.54464 -0.11190 -0.08649 0.04792  124 TYR A CG  
533  C CD1 . TYR A 101 ? 0.47011 0.55788 0.65953 -0.10813 -0.09077 0.04447  124 TYR A CD1 
534  C CD2 . TYR A 101 ? 0.39580 0.47942 0.57778 -0.10946 -0.08271 0.04829  124 TYR A CD2 
535  C CE1 . TYR A 101 ? 0.35025 0.43823 0.53479 -0.10202 -0.09114 0.04140  124 TYR A CE1 
536  C CE2 . TYR A 101 ? 0.36109 0.44501 0.53840 -0.10349 -0.08330 0.04530  124 TYR A CE2 
537  C CZ  . TYR A 101 ? 0.22356 0.30966 0.40212 -0.09974 -0.08751 0.04180  124 TYR A CZ  
538  O OH  . TYR A 101 ? 0.31534 0.40144 0.48860 -0.09359 -0.08798 0.03859  124 TYR A OH  
539  N N   . VAL A 102 ? 0.50485 0.60595 0.70698 -0.12173 -0.06846 0.05782  125 VAL A N   
540  C CA  . VAL A 102 ? 0.31304 0.41951 0.51491 -0.11995 -0.06041 0.05951  125 VAL A CA  
541  C C   . VAL A 102 ? 0.41680 0.53601 0.62869 -0.12009 -0.05524 0.06051  125 VAL A C   
542  O O   . VAL A 102 ? 0.54855 0.67508 0.76189 -0.11603 -0.05039 0.06006  125 VAL A O   
543  C CB  . VAL A 102 ? 0.26112 0.36048 0.45722 -0.12336 -0.05704 0.06221  125 VAL A CB  
544  C CG1 . VAL A 102 ? 0.19624 0.30095 0.39150 -0.12113 -0.04833 0.06377  125 VAL A CG1 
545  C CG2 . VAL A 102 ? 0.34991 0.43612 0.53557 -0.12310 -0.06241 0.06097  125 VAL A CG2 
546  N N   . ALA A 103 ? 0.53421 0.65598 0.75275 -0.12471 -0.05614 0.06178  126 ALA A N   
547  C CA  . ALA A 103 ? 0.44144 0.57481 0.66933 -0.12530 -0.05140 0.06266  126 ALA A CA  
548  C C   . ALA A 103 ? 0.45403 0.59509 0.68679 -0.12098 -0.05324 0.05996  126 ALA A C   
549  O O   . ALA A 103 ? 0.56736 0.71784 0.80476 -0.11852 -0.04802 0.05989  126 ALA A O   
550  C CB  . ALA A 103 ? 0.44669 0.58040 0.68020 -0.13140 -0.05263 0.06442  126 ALA A CB  
551  N N   . THR A 104 ? 0.44245 0.57915 0.67358 -0.11976 -0.06056 0.05749  127 THR A N   
552  C CA  . THR A 104 ? 0.42159 0.56431 0.65567 -0.11502 -0.06254 0.05450  127 THR A CA  
553  C C   . THR A 104 ? 0.38986 0.53507 0.61972 -0.10921 -0.05853 0.05336  127 THR A C   
554  O O   . THR A 104 ? 0.51251 0.66686 0.74684 -0.10589 -0.05506 0.05243  127 THR A O   
555  C CB  . THR A 104 ? 0.48218 0.61791 0.71315 -0.11435 -0.07102 0.05179  127 THR A CB  
556  O OG1 . THR A 104 ? 0.60699 0.73960 0.84114 -0.11983 -0.07467 0.05297  127 THR A OG1 
557  C CG2 . THR A 104 ? 0.35853 0.50064 0.59277 -0.10969 -0.07295 0.04861  127 THR A CG2 
558  N N   . ILE A 105 ? 0.29760 0.43460 0.51854 -0.10780 -0.05901 0.05328  128 ILE A N   
559  C CA  . ILE A 105 ? 0.32105 0.46011 0.53755 -0.10212 -0.05558 0.05202  128 ILE A CA  
560  C C   . ILE A 105 ? 0.48000 0.62731 0.69990 -0.10150 -0.04679 0.05411  128 ILE A C   
561  O O   . ILE A 105 ? 0.61682 0.77108 0.83799 -0.09677 -0.04342 0.05272  128 ILE A O   
562  C CB  . ILE A 105 ? 0.37534 0.50366 0.58140 -0.10119 -0.05766 0.05168  128 ILE A CB  
563  C CG1 . ILE A 105 ? 0.46667 0.58649 0.66844 -0.10086 -0.06645 0.04885  128 ILE A CG1 
564  C CG2 . ILE A 105 ? 0.29403 0.42476 0.49545 -0.09553 -0.05356 0.05064  128 ILE A CG2 
565  C CD1 . ILE A 105 ? 0.57087 0.69431 0.77318 -0.09552 -0.06962 0.04503  128 ILE A CD1 
566  N N   . GLU A 106 ? 0.38412 0.53038 0.60495 -0.10605 -0.04289 0.05720  129 GLU A N   
567  C CA  . GLU A 106 ? 0.51530 0.66846 0.73842 -0.10537 -0.03439 0.05889  129 GLU A CA  
568  C C   . GLU A 106 ? 0.62439 0.78848 0.85600 -0.10371 -0.03256 0.05775  129 GLU A C   
569  O O   . GLU A 106 ? 0.47883 0.64912 0.71082 -0.09990 -0.02680 0.05728  129 GLU A O   
570  C CB  . GLU A 106 ? 0.60987 0.76001 0.83310 -0.11085 -0.03128 0.06195  129 GLU A CB  
571  C CG  . GLU A 106 ? 0.73348 0.87641 0.94786 -0.11061 -0.02768 0.06338  129 GLU A CG  
572  C CD  . GLU A 106 ? 0.93282 1.07564 1.14801 -0.11466 -0.02225 0.06601  129 GLU A CD  
573  O OE1 . GLU A 106 ? 0.77618 0.91637 0.99432 -0.11991 -0.02517 0.06724  129 GLU A OE1 
574  O OE2 . GLU A 106 ? 0.97084 1.11601 1.18342 -0.11244 -0.01512 0.06659  129 GLU A OE2 
575  N N   . MET A 107 ? 0.51539 0.68151 0.75337 -0.10636 -0.03757 0.05709  130 MET A N   
576  C CA  . MET A 107 ? 0.50952 0.68575 0.75577 -0.10524 -0.03632 0.05597  130 MET A CA  
577  C C   . MET A 107 ? 0.52207 0.70167 0.76679 -0.09881 -0.03713 0.05286  130 MET A C   
578  O O   . MET A 107 ? 0.59934 0.78641 0.84636 -0.09540 -0.03223 0.05207  130 MET A O   
579  C CB  . MET A 107 ? 0.42809 0.60503 0.68086 -0.10957 -0.04179 0.05590  130 MET A CB  
580  C CG  . MET A 107 ? 0.70568 0.89315 0.96759 -0.11017 -0.03893 0.05578  130 MET A CG  
581  S SD  . MET A 107 ? 0.76812 0.95719 1.03770 -0.11437 -0.04561 0.05520  130 MET A SD  
582  C CE  . MET A 107 ? 0.50099 0.67712 0.76426 -0.11850 -0.05148 0.05637  130 MET A CE  
583  N N   . ILE A 108 ? 0.42608 0.59983 0.66665 -0.09708 -0.04358 0.05078  131 ILE A N   
584  C CA  . ILE A 108 ? 0.46827 0.64359 0.70575 -0.09079 -0.04488 0.04753  131 ILE A CA  
585  C C   . ILE A 108 ? 0.46575 0.64284 0.69849 -0.08659 -0.03822 0.04779  131 ILE A C   
586  O O   . ILE A 108 ? 0.56228 0.74476 0.79510 -0.08153 -0.03601 0.04564  131 ILE A O   
587  C CB  . ILE A 108 ? 0.52119 0.68761 0.75256 -0.08978 -0.05240 0.04539  131 ILE A CB  
588  C CG1 . ILE A 108 ? 0.42995 0.59447 0.66567 -0.09361 -0.05882 0.04487  131 ILE A CG1 
589  C CG2 . ILE A 108 ? 0.41961 0.58715 0.64674 -0.08302 -0.05346 0.04180  131 ILE A CG2 
590  C CD1 . ILE A 108 ? 0.58626 0.73958 0.81508 -0.09445 -0.06569 0.04370  131 ILE A CD1 
591  N N   . LYS A 109 ? 0.42075 0.59276 0.64862 -0.08846 -0.03498 0.05023  132 LYS A N   
592  C CA  . LYS A 109 ? 0.24439 0.41700 0.46664 -0.08441 -0.02866 0.05046  132 LYS A CA  
593  C C   . LYS A 109 ? 0.31249 0.49421 0.53941 -0.08250 -0.02212 0.05041  132 LYS A C   
594  O O   . LYS A 109 ? 0.39772 0.58239 0.62165 -0.07709 -0.01869 0.04868  132 LYS A O   
595  C CB  . LYS A 109 ? 0.48655 0.65216 0.70321 -0.08743 -0.02607 0.05325  132 LYS A CB  
596  C CG  . LYS A 109 ? 0.39590 0.56198 0.60671 -0.08379 -0.01865 0.05380  132 LYS A CG  
597  C CD  . LYS A 109 ? 0.41244 0.57544 0.62154 -0.08782 -0.01379 0.05685  132 LYS A CD  
598  C CE  . LYS A 109 ? 0.52665 0.68795 0.72807 -0.08407 -0.00705 0.05710  132 LYS A CE  
599  N NZ  . LYS A 109 ? 0.47323 0.62918 0.66708 -0.08050 -0.00972 0.05582  132 LYS A NZ  
600  N N   . PHE A 110 ? 0.51186 0.69763 0.74562 -0.08685 -0.02036 0.05212  133 PHE A N   
601  C CA  . PHE A 110 ? 0.57373 0.76736 0.81147 -0.08553 -0.01403 0.05207  133 PHE A CA  
602  C C   . PHE A 110 ? 0.59586 0.79618 0.83727 -0.08125 -0.01530 0.04903  133 PHE A C   
603  O O   . PHE A 110 ? 0.73212 0.93665 0.97239 -0.07711 -0.01032 0.04776  133 PHE A O   
604  C CB  . PHE A 110 ? 0.70519 0.90160 0.94964 -0.09139 -0.01258 0.05431  133 PHE A CB  
605  C CG  . PHE A 110 ? 0.93973 1.14471 1.18933 -0.09033 -0.00708 0.05380  133 PHE A CG  
606  C CD1 . PHE A 110 ? 0.81953 1.02492 1.06754 -0.09136 -0.00039 0.05529  133 PHE A CD1 
607  C CD2 . PHE A 110 ? 0.92822 1.14045 1.18430 -0.08869 -0.00895 0.05170  133 PHE A CD2 
608  C CE1 . PHE A 110 ? 0.76591 0.97863 1.01839 -0.09051 0.00426  0.05454  133 PHE A CE1 
609  C CE2 . PHE A 110 ? 0.84338 1.06309 1.10405 -0.08786 -0.00425 0.05109  133 PHE A CE2 
610  C CZ  . PHE A 110 ? 0.93906 1.15897 1.19797 -0.08882 0.00228  0.05249  133 PHE A CZ  
611  N N   . ILE A 111 ? 0.54968 0.75038 0.79481 -0.08201 -0.02200 0.04757  134 ILE A N   
612  C CA  . ILE A 111 ? 0.55550 0.76230 0.80389 -0.07801 -0.02338 0.04448  134 ILE A CA  
613  C C   . ILE A 111 ? 0.52117 0.72631 0.76214 -0.07146 -0.02201 0.04209  134 ILE A C   
614  O O   . ILE A 111 ? 0.75352 0.96385 0.99520 -0.06719 -0.01952 0.03985  134 ILE A O   
615  C CB  . ILE A 111 ? 0.71811 0.92472 0.97093 -0.07997 -0.03097 0.04314  134 ILE A CB  
616  C CG1 . ILE A 111 ? 0.52297 0.72175 0.76914 -0.07810 -0.03690 0.04152  134 ILE A CG1 
617  C CG2 . ILE A 111 ? 0.54074 0.74728 0.79962 -0.08683 -0.03247 0.04577  134 ILE A CG2 
618  C CD1 . ILE A 111 ? 0.67078 0.87057 0.91906 -0.07649 -0.04317 0.03841  134 ILE A CD1 
619  N N   . ILE A 112 ? 0.58273 0.78039 0.81624 -0.07053 -0.02368 0.04235  135 ILE A N   
620  C CA  . ILE A 112 ? 0.53212 0.72800 0.75814 -0.06432 -0.02213 0.04010  135 ILE A CA  
621  C C   . ILE A 112 ? 0.59880 0.79653 0.82184 -0.06222 -0.01398 0.04107  135 ILE A C   
622  O O   . ILE A 112 ? 0.72387 0.92438 0.94457 -0.05712 -0.01096 0.03877  135 ILE A O   
623  C CB  . ILE A 112 ? 0.38762 0.57494 0.60637 -0.06400 -0.02637 0.03998  135 ILE A CB  
624  C CG1 . ILE A 112 ? 0.21764 0.40211 0.43849 -0.06587 -0.03471 0.03846  135 ILE A CG1 
625  C CG2 . ILE A 112 ? 0.62344 0.80901 0.83417 -0.05757 -0.02449 0.03762  135 ILE A CG2 
626  C CD1 . ILE A 112 ? 0.41469 0.58972 0.62837 -0.06625 -0.03958 0.03819  135 ILE A CD1 
627  N N   . GLU A 113 ? 0.53682 0.73214 0.75910 -0.06602 -0.01038 0.04422  136 GLU A N   
628  C CA  . GLU A 113 ? 0.60123 0.79778 0.82047 -0.06433 -0.00261 0.04493  136 GLU A CA  
629  C C   . GLU A 113 ? 0.66078 0.86510 0.88582 -0.06297 0.00021  0.04345  136 GLU A C   
630  O O   . GLU A 113 ? 0.88095 1.08664 1.10242 -0.05851 0.00468  0.04173  136 GLU A O   
631  C CB  . GLU A 113 ? 0.51330 0.70663 0.73215 -0.06938 0.00033  0.04829  136 GLU A CB  
632  C CG  . GLU A 113 ? 0.62472 0.80975 0.83641 -0.07037 -0.00092 0.04979  136 GLU A CG  
633  C CD  . GLU A 113 ? 0.85279 1.03438 1.06280 -0.07454 0.00320  0.05269  136 GLU A CD  
634  O OE1 . GLU A 113 ? 0.80782 0.99178 1.02432 -0.07946 0.00286  0.05425  136 GLU A OE1 
635  O OE2 . GLU A 113 ? 0.70048 0.87680 0.90239 -0.07282 0.00676  0.05322  136 GLU A OE2 
636  N N   . TYR A 114 ? 0.80080 1.00983 1.03463 -0.06694 -0.00256 0.04400  137 TYR A N   
637  C CA  . TYR A 114 ? 0.74713 0.96382 0.98726 -0.06650 0.00002  0.04288  137 TYR A CA  
638  C C   . TYR A 114 ? 0.68830 0.90788 0.92724 -0.06064 -0.00066 0.03927  137 TYR A C   
639  O O   . TYR A 114 ? 0.55406 0.77733 0.79324 -0.05795 0.00370  0.03786  137 TYR A O   
640  C CB  . TYR A 114 ? 0.74533 0.96624 0.99493 -0.07182 -0.00362 0.04399  137 TYR A CB  
641  C CG  . TYR A 114 ? 0.85463 1.08386 1.11120 -0.07140 -0.00152 0.04267  137 TYR A CG  
642  C CD1 . TYR A 114 ? 0.85285 1.08518 1.11072 -0.07224 0.00463  0.04349  137 TYR A CD1 
643  C CD2 . TYR A 114 ? 0.81203 1.04579 1.07361 -0.07008 -0.00587 0.04036  137 TYR A CD2 
644  C CE1 . TYR A 114 ? 0.82005 1.05995 1.08435 -0.07189 0.00630  0.04212  137 TYR A CE1 
645  C CE2 . TYR A 114 ? 0.67976 0.92111 0.94771 -0.06970 -0.00414 0.03906  137 TYR A CE2 
646  C CZ  . TYR A 114 ? 1.07451 1.31901 1.34396 -0.07064 0.00190  0.03998  137 TYR A CZ  
647  O OH  . TYR A 114 ? 1.63312 1.88516 1.90898 -0.07028 0.00344  0.03855  137 TYR A OH  
648  N N   . PHE A 115 ? 0.62172 0.83908 0.85885 -0.05855 -0.00617 0.03748  138 PHE A N   
649  C CA  . PHE A 115 ? 0.61502 0.83488 0.85102 -0.05315 -0.00710 0.03378  138 PHE A CA  
650  C C   . PHE A 115 ? 0.77885 0.99378 1.00508 -0.04757 -0.00463 0.03209  138 PHE A C   
651  O O   . PHE A 115 ? 0.85467 1.07136 1.07898 -0.04309 -0.00223 0.02945  138 PHE A O   
652  C CB  . PHE A 115 ? 0.58735 0.80735 0.82582 -0.05306 -0.01448 0.03186  138 PHE A CB  
653  C CG  . PHE A 115 ? 0.79927 1.02476 1.04725 -0.05721 -0.01752 0.03233  138 PHE A CG  
654  C CD1 . PHE A 115 ? 0.78456 1.01734 1.03892 -0.05767 -0.01429 0.03202  138 PHE A CD1 
655  C CD2 . PHE A 115 ? 0.88608 1.10898 1.13615 -0.06039 -0.02405 0.03270  138 PHE A CD2 
656  C CE1 . PHE A 115 ? 0.61523 0.85313 0.87830 -0.06147 -0.01731 0.03238  138 PHE A CE1 
657  C CE2 . PHE A 115 ? 0.99047 1.21778 1.24876 -0.06414 -0.02716 0.03300  138 PHE A CE2 
658  C CZ  . PHE A 115 ? 0.80772 1.04286 1.07274 -0.06473 -0.02373 0.03291  138 PHE A CZ  
659  N N   . HIS A 116 ? 0.67832 0.88675 0.89818 -0.04783 -0.00514 0.03348  139 HIS A N   
660  C CA  . HIS A 116 ? 0.61572 0.81900 0.82608 -0.04249 -0.00412 0.03159  139 HIS A CA  
661  C C   . HIS A 116 ? 0.67432 0.87182 0.87787 -0.04326 -0.00050 0.03407  139 HIS A C   
662  O O   . HIS A 116 ? 0.72633 0.91839 0.92288 -0.04103 -0.00210 0.03355  139 HIS A O   
663  C CB  . HIS A 116 ? 0.68402 0.88464 0.89224 -0.04048 -0.01081 0.02922  139 HIS A CB  
664  C CG  . HIS A 116 ? 0.83555 1.04102 1.04951 -0.03962 -0.01480 0.02648  139 HIS A CG  
665  N ND1 . HIS A 116 ? 0.90339 1.11129 1.11628 -0.03482 -0.01328 0.02314  139 HIS A ND1 
666  C CD2 . HIS A 116 ? 0.69643 0.90409 0.91666 -0.04290 -0.02038 0.02642  139 HIS A CD2 
667  C CE1 . HIS A 116 ? 0.88002 1.09201 1.09849 -0.03516 -0.01757 0.02118  139 HIS A CE1 
668  N NE2 . HIS A 116 ? 0.87355 1.08553 1.09642 -0.03998 -0.02189 0.02313  139 HIS A NE2 
669  N N   . GLU A 117 ? 0.67966 0.87802 0.88481 -0.04641 0.00432  0.03661  140 GLU A N   
670  C CA  . GLU A 117 ? 0.71658 0.90915 0.91576 -0.04803 0.00723  0.03912  140 GLU A CA  
671  C C   . GLU A 117 ? 0.64287 0.83005 0.83149 -0.04261 0.00985  0.03751  140 GLU A C   
672  O O   . GLU A 117 ? 0.87641 1.05798 1.05912 -0.04280 0.00927  0.03869  140 GLU A O   
673  C CB  . GLU A 117 ? 0.86181 1.05594 1.06316 -0.05116 0.01272  0.04112  140 GLU A CB  
674  C CG  . GLU A 117 ? 0.91425 1.10239 1.11044 -0.05384 0.01525  0.04380  140 GLU A CG  
675  C CD  . GLU A 117 ? 1.04914 1.23869 1.24738 -0.05691 0.02042  0.04529  140 GLU A CD  
676  O OE1 . GLU A 117 ? 1.28043 1.47621 1.48537 -0.05772 0.02139  0.04462  140 GLU A OE1 
677  O OE2 . GLU A 117 ? 1.08395 1.26824 1.27688 -0.05842 0.02347  0.04692  140 GLU A OE2 
678  N N   . PHE A 118 ? 0.62775 0.81601 0.81357 -0.03786 0.01268  0.03476  141 PHE A N   
679  C CA  . PHE A 118 ? 0.41547 0.59787 0.59072 -0.03279 0.01577  0.03307  141 PHE A CA  
680  C C   . PHE A 118 ? 0.33563 0.51730 0.50812 -0.02797 0.01231  0.02975  141 PHE A C   
681  O O   . PHE A 118 ? 0.43057 0.60745 0.59460 -0.02334 0.01462  0.02773  141 PHE A O   
682  C CB  . PHE A 118 ? 0.33139 0.51316 0.50372 -0.03138 0.02198  0.03236  141 PHE A CB  
683  C CG  . PHE A 118 ? 0.51359 0.69410 0.68594 -0.03538 0.02572  0.03508  141 PHE A CG  
684  C CD1 . PHE A 118 ? 0.52589 0.69962 0.69026 -0.03539 0.02758  0.03631  141 PHE A CD1 
685  C CD2 . PHE A 118 ? 0.72191 0.90783 0.90218 -0.03922 0.02720  0.03627  141 PHE A CD2 
686  C CE1 . PHE A 118 ? 0.63380 0.80573 0.79777 -0.03905 0.03090  0.03849  141 PHE A CE1 
687  C CE2 . PHE A 118 ? 0.72214 0.90645 0.90210 -0.04294 0.03055  0.03851  141 PHE A CE2 
688  C CZ  . PHE A 118 ? 0.82713 1.00426 0.99885 -0.04284 0.03237  0.03956  141 PHE A CZ  
689  N N   . ASP A 119 ? 0.48197 0.66749 0.66100 -0.02910 0.00659  0.02893  142 ASP A N   
690  C CA  . ASP A 119 ? 0.55010 0.73440 0.72670 -0.02501 0.00224  0.02556  142 ASP A CA  
691  C C   . ASP A 119 ? 0.43473 0.61398 0.60610 -0.02483 -0.00159 0.02589  142 ASP A C   
692  O O   . ASP A 119 ? 0.40782 0.58664 0.58179 -0.02931 -0.00369 0.02866  142 ASP A O   
693  C CB  . ASP A 119 ? 0.57687 0.76715 0.76242 -0.02629 -0.00236 0.02404  142 ASP A CB  
694  C CG  . ASP A 119 ? 0.71320 0.90879 0.90399 -0.02620 0.00114  0.02340  142 ASP A CG  
695  O OD1 . ASP A 119 ? 0.69320 0.88662 0.87907 -0.02343 0.00625  0.02273  142 ASP A OD1 
696  O OD2 . ASP A 119 ? 0.86280 1.06433 1.06232 -0.02895 -0.00142 0.02346  142 ASP A OD2 
697  N N   . GLU A 120 ? 0.38600 0.56073 0.54965 -0.01977 -0.00256 0.02300  143 GLU A N   
698  C CA  . GLU A 120 ? 0.40364 0.57365 0.56205 -0.01899 -0.00696 0.02247  143 GLU A CA  
699  C C   . GLU A 120 ? 0.61693 0.78890 0.78124 -0.02123 -0.01456 0.02126  143 GLU A C   
700  O O   . GLU A 120 ? 0.51165 0.68686 0.68017 -0.01995 -0.01686 0.01862  143 GLU A O   
701  C CB  . GLU A 120 ? 0.47624 0.64048 0.62480 -0.01284 -0.00636 0.01920  143 GLU A CB  
702  C CG  . GLU A 120 ? 0.27975 0.43914 0.41935 -0.01086 -0.00016 0.02047  143 GLU A CG  
703  C CD  . GLU A 120 ? 0.31100 0.46370 0.44054 -0.00763 -0.00177 0.01920  143 GLU A CD  
704  O OE1 . GLU A 120 ? 0.49838 0.65030 0.62850 -0.00759 -0.00798 0.01766  143 GLU A OE1 
705  O OE2 . GLU A 120 ? 0.51157 0.65904 0.63194 -0.00513 0.00290  0.01941  143 GLU A OE2 
706  N N   . PRO A 121 ? 0.56764 0.73692 0.73191 -0.02470 -0.01876 0.02297  144 PRO A N   
707  C CA  . PRO A 121 ? 0.39866 0.56362 0.55792 -0.02645 -0.01694 0.02589  144 PRO A CA  
708  C C   . PRO A 121 ? 0.41132 0.57753 0.57626 -0.03295 -0.01523 0.03047  144 PRO A C   
709  O O   . PRO A 121 ? 0.37953 0.54116 0.54158 -0.03567 -0.01679 0.03251  144 PRO A O   
710  C CB  . PRO A 121 ? 0.45497 0.61444 0.60956 -0.02560 -0.02423 0.02366  144 PRO A CB  
711  C CG  . PRO A 121 ? 0.44809 0.60991 0.61019 -0.02841 -0.03022 0.02245  144 PRO A CG  
712  C CD  . PRO A 121 ? 0.36020 0.52904 0.52824 -0.02701 -0.02651 0.02159  144 PRO A CD  
713  N N   . ALA A 122 ? 0.53256 0.70408 0.70506 -0.03574 -0.01233 0.03200  145 ALA A N   
714  C CA  . ALA A 122 ? 0.23103 0.40251 0.40673 -0.04117 -0.00920 0.03608  145 ALA A CA  
715  C C   . ALA A 122 ? 0.36484 0.53271 0.53264 -0.03944 -0.00254 0.03751  145 ALA A C   
716  O O   . ALA A 122 ? 0.29247 0.45643 0.45828 -0.04296 -0.00161 0.04033  145 ALA A O   
717  C CB  . ALA A 122 ? 0.32492 0.50283 0.50932 -0.04372 -0.00699 0.03684  145 ALA A CB  
718  N N   . VAL A 123 ? 0.31214 0.48013 0.47455 -0.03400 0.00191  0.03530  146 VAL A N   
719  C CA  . VAL A 123 ? 0.20078 0.36356 0.35319 -0.03090 0.00724  0.03544  146 VAL A CA  
720  C C   . VAL A 123 ? 0.21629 0.37610 0.36120 -0.02506 0.00539  0.03217  146 VAL A C   
721  O O   . VAL A 123 ? 0.44645 0.60835 0.59241 -0.02172 0.00419  0.02918  146 VAL A O   
722  C CB  . VAL A 123 ? 0.37767 0.54100 0.52866 -0.02970 0.01411  0.03524  146 VAL A CB  
723  C CG1 . VAL A 123 ? 0.19193 0.34813 0.33125 -0.02623 0.01889  0.03466  146 VAL A CG1 
724  C CG2 . VAL A 123 ? 0.21908 0.38548 0.37737 -0.03536 0.01589  0.03808  146 VAL A CG2 
725  N N   . ILE A 124 ? 0.26153 0.41608 0.39853 -0.02381 0.00524  0.03256  147 ILE A N   
726  C CA  . ILE A 124 ? 0.26909 0.41989 0.39738 -0.01804 0.00413  0.02936  147 ILE A CA  
727  C C   . ILE A 124 ? 0.28426 0.43016 0.40304 -0.01408 0.01085  0.02845  147 ILE A C   
728  O O   . ILE A 124 ? 0.28907 0.43110 0.40292 -0.01514 0.01492  0.03033  147 ILE A O   
729  C CB  . ILE A 124 ? 0.29787 0.44530 0.42196 -0.01851 -0.00045 0.02967  147 ILE A CB  
730  C CG1 . ILE A 124 ? 0.19165 0.34130 0.32405 -0.02276 -0.00842 0.02988  147 ILE A CG1 
731  C CG2 . ILE A 124 ? 0.29277 0.43582 0.40670 -0.01214 -0.00124 0.02596  147 ILE A CG2 
732  C CD1 . ILE A 124 ? 0.17624 0.32107 0.30481 -0.02461 -0.01387 0.03037  147 ILE A CD1 
733  N N   . TYR A 125 ? 0.37456 0.51925 0.49029 -0.00976 0.01156  0.02531  148 TYR A N   
734  C CA  . TYR A 125 ? 0.31115 0.44876 0.41634 -0.00586 0.01621  0.02366  148 TYR A CA  
735  C C   . TYR A 125 ? 0.37268 0.50443 0.46802 -0.00160 0.01392  0.02135  148 TYR A C   
736  O O   . TYR A 125 ? 0.38426 0.51615 0.47977 0.00085  0.01051  0.01884  148 TYR A O   
737  C CB  . TYR A 125 ? 0.28686 0.42545 0.39440 -0.00453 0.01809  0.02183  148 TYR A CB  
738  C CG  . TYR A 125 ? 0.32394 0.46940 0.44191 -0.00852 0.01962  0.02358  148 TYR A CG  
739  C CD1 . TYR A 125 ? 0.32496 0.47822 0.45399 -0.01106 0.01576  0.02403  148 TYR A CD1 
740  C CD2 . TYR A 125 ? 0.39195 0.53548 0.50827 -0.00989 0.02456  0.02445  148 TYR A CD2 
741  C CE1 . TYR A 125 ? 0.25998 0.41922 0.39807 -0.01485 0.01713  0.02562  148 TYR A CE1 
742  C CE2 . TYR A 125 ? 0.60492 0.75458 0.73025 -0.01355 0.02601  0.02591  148 TYR A CE2 
743  C CZ  . TYR A 125 ? 0.39866 0.55629 0.53485 -0.01604 0.02243  0.02665  148 TYR A CZ  
744  O OH  . TYR A 125 ? 0.45857 0.62206 0.60341 -0.01982 0.02382  0.02810  148 TYR A OH  
745  N N   . SER A 126 ? 0.15317 0.27912 0.23950 -0.00076 0.01570  0.02198  149 SER A N   
746  C CA  . SER A 126 ? 0.30640 0.42741 0.38344 0.00265  0.01313  0.02009  149 SER A CA  
747  C C   . SER A 126 ? 0.38056 0.49136 0.44477 0.00627  0.01597  0.01797  149 SER A C   
748  O O   . SER A 126 ? 0.39688 0.50616 0.45924 0.00613  0.01949  0.01917  149 SER A O   
749  C CB  . SER A 126 ? 0.33332 0.45505 0.40936 0.00071  0.01199  0.02217  149 SER A CB  
750  O OG  . SER A 126 ? 0.46449 0.58223 0.53682 -0.00092 0.01692  0.02425  149 SER A OG  
751  N N   . SER A 127 ? 0.36209 0.46747 0.41693 0.00949  0.01348  0.01575  150 SER A N   
752  C CA  . SER A 127 ? 0.30141 0.40076 0.34338 0.01294  0.01426  0.01546  150 SER A CA  
753  C C   . SER A 127 ? 0.24550 0.34002 0.28027 0.01325  0.01681  0.01744  150 SER A C   
754  O O   . SER A 127 ? 0.45250 0.54437 0.48023 0.01560  0.01702  0.01848  150 SER A O   
755  C CB  . SER A 127 ? 0.32606 0.42103 0.35866 0.01580  0.01064  0.01273  150 SER A CB  
756  O OG  . SER A 127 ? 0.45449 0.54647 0.48584 0.01529  0.00916  0.01150  150 SER A OG  
757  N N   . ASN A 128 ? 0.37904 0.47232 0.41617 0.01089  0.01818  0.01799  151 ASN A N   
758  C CA  . ASN A 128 ? 0.32239 0.41095 0.35403 0.01096  0.02047  0.01971  151 ASN A CA  
759  C C   . ASN A 128 ? 0.20690 0.29893 0.24491 0.00869  0.02407  0.02211  151 ASN A C   
760  O O   . ASN A 128 ? 0.36849 0.45704 0.40332 0.00853  0.02603  0.02349  151 ASN A O   
761  C CB  . ASN A 128 ? 0.20520 0.29004 0.23509 0.00940  0.02051  0.01910  151 ASN A CB  
762  C CG  . ASN A 128 ? 0.33820 0.43025 0.37913 0.00496  0.02182  0.02097  151 ASN A CG  
763  O OD1 . ASN A 128 ? 0.44869 0.54720 0.49910 0.00257  0.02286  0.02235  151 ASN A OD1 
764  N ND2 . ASN A 128 ? 0.40436 0.49788 0.44413 0.00394  0.02104  0.02259  151 ASN A ND2 
765  N N   . GLY A 129 ? 0.27172 0.37050 0.31882 0.00705  0.02469  0.02246  152 GLY A N   
766  C CA  . GLY A 129 ? 0.30392 0.40643 0.35662 0.00526  0.02778  0.02458  152 GLY A CA  
767  C C   . GLY A 129 ? 0.39339 0.49986 0.45559 0.00032  0.02969  0.02559  152 GLY A C   
768  O O   . GLY A 129 ? 0.40507 0.51568 0.47307 -0.00157 0.03201  0.02720  152 GLY A O   
769  N N   . ASN A 130 ? 0.31141 0.41671 0.37529 -0.00199 0.02852  0.02476  153 ASN A N   
770  C CA  . ASN A 130 ? 0.41482 0.52456 0.48726 -0.00706 0.02960  0.02697  153 ASN A CA  
771  C C   . ASN A 130 ? 0.37666 0.49637 0.46158 -0.00946 0.02795  0.02828  153 ASN A C   
772  O O   . ASN A 130 ? 0.32966 0.45301 0.41737 -0.00747 0.02487  0.02692  153 ASN A O   
773  C CB  . ASN A 130 ? 0.29228 0.40270 0.36390 -0.00850 0.02748  0.02924  153 ASN A CB  
774  C CG  . ASN A 130 ? 0.44154 0.54232 0.50245 -0.00760 0.02981  0.02854  153 ASN A CG  
775  O OD1 . ASN A 130 ? 0.58140 0.67572 0.63629 -0.00612 0.03241  0.02673  153 ASN A OD1 
776  N ND2 . ASN A 130 ? 0.45861 0.55908 0.51742 -0.00863 0.02818  0.03033  153 ASN A ND2 
777  N N   . LYS A 131 ? 0.38935 0.51270 0.48141 -0.01384 0.02987  0.03055  154 LYS A N   
778  C CA  . LYS A 131 ? 0.38740 0.51990 0.49212 -0.01756 0.02759  0.03248  154 LYS A CA  
779  C C   . LYS A 131 ? 0.35246 0.48665 0.46170 -0.02251 0.02536  0.03604  154 LYS A C   
780  O O   . LYS A 131 ? 0.50726 0.63790 0.61449 -0.02532 0.02827  0.03781  154 LYS A O   
781  C CB  . LYS A 131 ? 0.17623 0.31114 0.28563 -0.01935 0.03101  0.03235  154 LYS A CB  
782  C CG  . LYS A 131 ? 0.30981 0.44352 0.41626 -0.01544 0.03249  0.02918  154 LYS A CG  
783  C CD  . LYS A 131 ? 0.35355 0.49149 0.46454 -0.01730 0.03581  0.03129  154 LYS A CD  
784  C CE  . LYS A 131 ? 0.44609 0.58531 0.55433 -0.01326 0.03697  0.03140  154 LYS A CE  
785  N NZ  . LYS A 131 ? 0.33841 0.48134 0.45046 -0.01488 0.04030  0.03347  154 LYS A NZ  
786  N N   . THR A 132 ? 0.25820 0.39669 0.37304 -0.02381 0.01967  0.03673  155 THR A N   
787  C CA  . THR A 132 ? 0.15564 0.29434 0.27462 -0.02911 0.01602  0.03983  155 THR A CA  
788  C C   . THR A 132 ? 0.22198 0.36693 0.35328 -0.03376 0.01162  0.04101  155 THR A C   
789  O O   . THR A 132 ? 0.28481 0.43407 0.42056 -0.03195 0.00782  0.03888  155 THR A O   
790  C CB  . THR A 132 ? 0.32094 0.45729 0.43483 -0.02736 0.01159  0.03912  155 THR A CB  
791  O OG1 . THR A 132 ? 0.30047 0.43048 0.40215 -0.02298 0.01607  0.03792  155 THR A OG1 
792  C CG2 . THR A 132 ? 0.24645 0.38133 0.36435 -0.03368 0.00678  0.04209  155 THR A CG2 
793  N N   . VAL A 133 ? 0.21383 0.35841 0.34989 -0.03955 0.01220  0.04400  156 VAL A N   
794  C CA  . VAL A 133 ? 0.23975 0.38926 0.38686 -0.04433 0.00861  0.04514  156 VAL A CA  
795  C C   . VAL A 133 ? 0.22368 0.37151 0.37389 -0.04769 0.00037  0.04564  156 VAL A C   
796  O O   . VAL A 133 ? 0.19757 0.34132 0.34893 -0.05314 -0.00172 0.04814  156 VAL A O   
797  C CB  . VAL A 133 ? 0.15059 0.29949 0.30049 -0.04901 0.01269  0.04773  156 VAL A CB  
798  C CG1 . VAL A 133 ? 0.14609 0.30089 0.30718 -0.05320 0.00987  0.04847  156 VAL A CG1 
799  C CG2 . VAL A 133 ? 0.13548 0.28318 0.27946 -0.04548 0.02028  0.04658  156 VAL A CG2 
800  N N   . TRP A 134 ? 0.40671 0.39454 0.32255 -0.01710 -0.03367 -0.04712 157 TRP A N   
801  C CA  . TRP A 134 ? 0.38899 0.37538 0.30641 -0.01871 -0.03120 -0.04308 157 TRP A CA  
802  C C   . TRP A 134 ? 0.51964 0.50747 0.43850 -0.01678 -0.02921 -0.04246 157 TRP A C   
803  O O   . TRP A 134 ? 0.56537 0.55399 0.48586 -0.01878 -0.02645 -0.03951 157 TRP A O   
804  C CB  . TRP A 134 ? 0.35924 0.34326 0.27686 -0.02098 -0.03076 -0.04109 157 TRP A CB  
805  C CG  . TRP A 134 ? 0.30975 0.29419 0.22969 -0.02284 -0.02752 -0.03750 157 TRP A CG  
806  C CD1 . TRP A 134 ? 0.38592 0.37088 0.30747 -0.02246 -0.02588 -0.03666 157 TRP A CD1 
807  C CD2 . TRP A 134 ? 0.39304 0.37845 0.31440 -0.02570 -0.02513 -0.03440 157 TRP A CD2 
808  N NE1 . TRP A 134 ? 0.51102 0.49742 0.43505 -0.02513 -0.02253 -0.03325 157 TRP A NE1 
809  C CE2 . TRP A 134 ? 0.50842 0.49542 0.43253 -0.02717 -0.02193 -0.03189 157 TRP A CE2 
810  C CE3 . TRP A 134 ? 0.34498 0.33055 0.26579 -0.02734 -0.02528 -0.03358 157 TRP A CE3 
811  C CZ2 . TRP A 134 ? 0.32582 0.31513 0.25244 -0.03023 -0.01877 -0.02881 157 TRP A CZ2 
812  C CZ3 . TRP A 134 ? 0.37162 0.35917 0.29469 -0.03029 -0.02220 -0.03039 157 TRP A CZ3 
813  C CH2 . TRP A 134 ? 0.33805 0.32770 0.26415 -0.03172 -0.01893 -0.02813 157 TRP A CH2 
814  N N   . LEU A 135 ? 0.45843 0.44706 0.37723 -0.01358 -0.03003 -0.04473 158 LEU A N   
815  C CA  . LEU A 135 ? 0.35131 0.33937 0.27032 -0.01212 -0.02836 -0.04347 158 LEU A CA  
816  C C   . LEU A 135 ? 0.40726 0.39544 0.32530 -0.01261 -0.02741 -0.04254 158 LEU A C   
817  O O   . LEU A 135 ? 0.50526 0.49564 0.42579 -0.01469 -0.02404 -0.04003 158 LEU A O   
818  C CB  . LEU A 135 ? 0.40961 0.39731 0.32849 -0.00855 -0.02948 -0.04526 158 LEU A CB  
819  C CG  . LEU A 135 ? 0.76034 0.74496 0.67731 -0.00822 -0.02781 -0.04322 158 LEU A CG  
820  C CD1 . LEU A 135 ? 0.66832 0.65497 0.58776 -0.01051 -0.02531 -0.04152 158 LEU A CD1 
821  C CD2 . LEU A 135 ? 0.57098 0.55026 0.48411 -0.00545 -0.02948 -0.04378 158 LEU A CD2 
822  N N   . ARG A 136 ? 0.39256 0.38037 0.30925 -0.01139 -0.02930 -0.04404 159 ARG A N   
823  C CA  . ARG A 136 ? 0.49611 0.48394 0.41155 -0.01191 -0.02851 -0.04331 159 ARG A CA  
824  C C   . ARG A 136 ? 0.33226 0.32333 0.25098 -0.01591 -0.02559 -0.04061 159 ARG A C   
825  O O   . ARG A 136 ? 0.39598 0.39040 0.31757 -0.01767 -0.02233 -0.03865 159 ARG A O   
826  C CB  . ARG A 136 ? 0.27952 0.26618 0.19309 -0.00968 -0.03125 -0.04542 159 ARG A CB  
827  C CG  . ARG A 136 ? 0.35495 0.34116 0.26670 -0.01042 -0.03072 -0.04472 159 ARG A CG  
828  C CD  . ARG A 136 ? 0.33703 0.32235 0.24725 -0.00815 -0.03371 -0.04702 159 ARG A CD  
829  N NE  . ARG A 136 ? 0.33847 0.32221 0.24772 -0.00438 -0.03583 -0.04918 159 ARG A NE  
830  C CZ  . ARG A 136 ? 0.57786 0.58080 0.49628 -0.00609 -0.03397 -0.05529 159 ARG A CZ  
831  N NH1 . ARG A 136 ? 0.37617 0.37958 0.29325 -0.00956 -0.03440 -0.05558 159 ARG A NH1 
832  N NH2 . ARG A 136 ? 0.35197 0.36082 0.26635 -0.02065 -0.02700 -0.05487 159 ARG A NH2 
833  N N   . TYR A 137 ? 0.32991 0.32068 0.24901 -0.01775 -0.02630 -0.04018 160 TYR A N   
834  C CA  . TYR A 137 ? 0.34731 0.34018 0.26895 -0.02160 -0.02362 -0.03717 160 TYR A CA  
835  C C   . TYR A 137 ? 0.39442 0.38990 0.31995 -0.02394 -0.01986 -0.03437 160 TYR A C   
836  O O   . TYR A 137 ? 0.49002 0.48920 0.41888 -0.02630 -0.01669 -0.03223 160 TYR A O   
837  C CB  . TYR A 137 ? 0.27527 0.26610 0.19550 -0.02328 -0.02547 -0.03702 160 TYR A CB  
838  C CG  . TYR A 137 ? 0.33796 0.32736 0.25512 -0.02113 -0.02914 -0.04019 160 TYR A CG  
839  C CD1 . TYR A 137 ? 0.40558 0.39596 0.32194 -0.02020 -0.02948 -0.04097 160 TYR A CD1 
840  C CD2 . TYR A 137 ? 0.29599 0.28382 0.21144 -0.02034 -0.03199 -0.04250 160 TYR A CD2 
841  C CE1 . TYR A 137 ? 0.37896 0.36879 0.29284 -0.01820 -0.03274 -0.04412 160 TYR A CE1 
842  C CE2 . TYR A 137 ? 0.46031 0.44855 0.37381 -0.01908 -0.03477 -0.04566 160 TYR A CE2 
843  C CZ  . TYR A 137 ? 0.31907 0.30860 0.23194 -0.01781 -0.03519 -0.04662 160 TYR A CZ  
844  O OH  . TYR A 137 ? 0.39557 0.38642 0.30712 -0.01709 -0.03734 -0.04956 160 TYR A OH  
845  N N   . ALA A 138 ? 0.36644 0.36049 0.29193 -0.02328 -0.02018 -0.03455 161 ALA A N   
846  C CA  . ALA A 138 ? 0.33569 0.33228 0.26485 -0.02510 -0.01682 -0.03225 161 ALA A CA  
847  C C   . ALA A 138 ? 0.44170 0.44212 0.37358 -0.02461 -0.01448 -0.03208 161 ALA A C   
848  O O   . ALA A 138 ? 0.52142 0.52603 0.45762 -0.02706 -0.01109 -0.02992 161 ALA A O   
849  C CB  . ALA A 138 ? 0.25696 0.25110 0.18513 -0.02393 -0.01799 -0.03291 161 ALA A CB  
850  N N   . GLU A 139 ? 0.42627 0.42541 0.35574 -0.02150 -0.01634 -0.03437 162 GLU A N   
851  C CA  . GLU A 139 ? 0.23662 0.23949 0.16849 -0.02116 -0.01428 -0.03425 162 GLU A CA  
852  C C   . GLU A 139 ? 0.46305 0.46997 0.39770 -0.02321 -0.01225 -0.03307 162 GLU A C   
853  O O   . GLU A 139 ? 0.54049 0.55250 0.47987 -0.02479 -0.00917 -0.03169 162 GLU A O   
854  C CB  . GLU A 139 ? 0.33587 0.33558 0.26345 -0.01766 -0.01694 -0.03678 162 GLU A CB  
855  C CG  . GLU A 139 ? 0.46669 0.47026 0.39648 -0.01731 -0.01498 -0.03677 162 GLU A CG  
856  C CD  . GLU A 139 ? 0.71301 0.71627 0.64033 -0.01623 -0.01610 -0.03802 162 GLU A CD  
857  O OE1 . GLU A 139 ? 0.77026 0.77427 0.69677 -0.01487 -0.01601 -0.03895 162 GLU A OE1 
858  O OE2 . GLU A 139 ? 0.88653 0.88892 0.81273 -0.01686 -0.01703 -0.03804 162 GLU A OE2 
859  N N   . TRP A 140 ? 0.36541 0.37034 0.29736 -0.02314 -0.01409 -0.03372 163 TRP A N   
860  C CA  . TRP A 140 ? 0.29509 0.30379 0.22957 -0.02513 -0.01222 -0.03257 163 TRP A CA  
861  C C   . TRP A 140 ? 0.30219 0.31456 0.24146 -0.02865 -0.00886 -0.02974 163 TRP A C   
862  O O   . TRP A 140 ? 0.45603 0.47331 0.39950 -0.03027 -0.00618 -0.02854 163 TRP A O   
863  C CB  . TRP A 140 ? 0.35111 0.35678 0.28183 -0.02474 -0.01484 -0.03355 163 TRP A CB  
864  C CG  . TRP A 140 ? 0.37436 0.37637 0.30020 -0.02134 -0.01829 -0.03639 163 TRP A CG  
865  C CD1 . TRP A 140 ? 0.41755 0.41863 0.34172 -0.01882 -0.01902 -0.03788 163 TRP A CD1 
866  C CD2 . TRP A 140 ? 0.34431 0.34304 0.26613 -0.02022 -0.02149 -0.03799 163 TRP A CD2 
867  N NE1 . TRP A 140 ? 0.53124 0.52784 0.44995 -0.01621 -0.02252 -0.04021 163 TRP A NE1 
868  C CE2 . TRP A 140 ? 0.53072 0.52609 0.44819 -0.01681 -0.02422 -0.04051 163 TRP A CE2 
869  C CE3 . TRP A 140 ? 0.36376 0.36191 0.28510 -0.02191 -0.02235 -0.03747 163 TRP A CE3 
870  C CZ2 . TRP A 140 ? 0.39309 0.38466 0.30591 -0.01475 -0.02794 -0.04276 163 TRP A CZ2 
871  C CZ3 . TRP A 140 ? 0.51464 0.50982 0.43201 -0.01999 -0.02593 -0.03979 163 TRP A CZ3 
872  C CH2 . TRP A 140 ? 0.51263 0.50488 0.42605 -0.01624 -0.02875 -0.04259 163 TRP A CH2 
873  N N   . LEU A 141 ? 0.40580 0.41578 0.34444 -0.02987 -0.00909 -0.02869 164 LEU A N   
874  C CA  . LEU A 141 ? 0.41163 0.42435 0.35415 -0.03317 -0.00611 -0.02596 164 LEU A CA  
875  C C   . LEU A 141 ? 0.34737 0.36424 0.29458 -0.03374 -0.00331 -0.02506 164 LEU A C   
876  O O   . LEU A 141 ? 0.36707 0.38785 0.31856 -0.03622 -0.00055 -0.02316 164 LEU A O   
877  C CB  . LEU A 141 ? 0.35610 0.36498 0.29646 -0.03410 -0.00722 -0.02513 164 LEU A CB  
878  C CG  . LEU A 141 ? 0.43478 0.44058 0.37181 -0.03487 -0.00932 -0.02509 164 LEU A CG  
879  C CD1 . LEU A 141 ? 0.56562 0.56717 0.50001 -0.03512 -0.01115 -0.02486 164 LEU A CD1 
880  C CD2 . LEU A 141 ? 0.34851 0.35742 0.28813 -0.03797 -0.00697 -0.02282 164 LEU A CD2 
881  N N   . LEU A 142 ? 0.34422 0.36029 0.29072 -0.03146 -0.00413 -0.02648 165 LEU A N   
882  C CA  . LEU A 142 ? 0.28340 0.30330 0.23426 -0.03191 -0.00178 -0.02576 165 LEU A CA  
883  C C   . LEU A 142 ? 0.33543 0.36012 0.28947 -0.03186 -0.00041 -0.02605 165 LEU A C   
884  O O   . LEU A 142 ? 0.40266 0.43178 0.36164 -0.03359 0.00210  -0.02472 165 LEU A O   
885  C CB  . LEU A 142 ? 0.34763 0.36495 0.29648 -0.02957 -0.00321 -0.02709 165 LEU A CB  
886  C CG  . LEU A 142 ? 0.30171 0.31528 0.24869 -0.02997 -0.00401 -0.02649 165 LEU A CG  
887  C CD1 . LEU A 142 ? 0.25560 0.26656 0.20036 -0.02738 -0.00568 -0.02805 165 LEU A CD1 
888  C CD2 . LEU A 142 ? 0.19280 0.20909 0.14402 -0.03302 -0.00109 -0.02395 165 LEU A CD2 
889  N N   . THR A 143 ? 0.33446 0.35828 0.28575 -0.02989 -0.00218 -0.02782 166 THR A N   
890  C CA  . THR A 143 ? 0.25563 0.28369 0.20937 -0.02924 -0.00130 -0.02847 166 THR A CA  
891  C C   . THR A 143 ? 0.22807 0.25901 0.18349 -0.03075 -0.00036 -0.02785 166 THR A C   
892  O O   . THR A 143 ? 0.36870 0.40474 0.32866 -0.03188 0.00165  -0.02716 166 THR A O   
893  C CB  . THR A 143 ? 0.26774 0.29319 0.21732 -0.02592 -0.00378 -0.03088 166 THR A CB  
894  O OG1 . THR A 143 ? 0.42970 0.45068 0.37412 -0.02472 -0.00643 -0.03210 166 THR A OG1 
895  C CG2 . THR A 143 ? 0.30532 0.32797 0.25327 -0.02440 -0.00470 -0.03149 166 THR A CG2 
896  N N   . CYS A 144 ? 0.29238 0.32021 0.24425 -0.03078 -0.00194 -0.02814 167 CYS A N   
897  C CA  . CYS A 144 ? 0.44716 0.47763 0.40023 -0.03194 -0.00127 -0.02776 167 CYS A CA  
898  C C   . CYS A 144 ? 0.27786 0.31295 0.23642 -0.03511 0.00177  -0.02547 167 CYS A C   
899  O O   . CYS A 144 ? 0.45541 0.49493 0.41724 -0.03577 0.00309  -0.02528 167 CYS A O   
900  C CB  . CYS A 144 ? 0.38879 0.41482 0.33702 -0.03161 -0.00362 -0.02835 167 CYS A CB  
901  S SG  . CYS A 144 ? 0.42399 0.44450 0.36563 -0.02774 -0.00763 -0.03134 167 CYS A SG  
902  N N   . PRO A 145 ? 0.26276 0.29707 0.22252 -0.03713 0.00287  -0.02374 168 PRO A N   
903  C CA  . PRO A 145 ? 0.37491 0.41356 0.33987 -0.03999 0.00559  -0.02171 168 PRO A CA  
904  C C   . PRO A 145 ? 0.37178 0.41501 0.34145 -0.04000 0.00715  -0.02173 168 PRO A C   
905  O O   . PRO A 145 ? 0.45152 0.49895 0.42523 -0.04162 0.00874  -0.02086 168 PRO A O   
906  C CB  . PRO A 145 ? 0.39685 0.43323 0.36166 -0.04164 0.00616  -0.02013 168 PRO A CB  
907  C CG  . PRO A 145 ? 0.19168 0.22246 0.15081 -0.04009 0.00359  -0.02113 168 PRO A CG  
908  C CD  . PRO A 145 ? 0.29247 0.32190 0.24881 -0.03699 0.00155  -0.02353 168 PRO A CD  
909  N N   . VAL A 146 ? 0.34450 0.38701 0.31365 -0.03816 0.00654  -0.02277 169 VAL A N   
910  C CA  . VAL A 146 ? 0.34106 0.38783 0.31462 -0.03825 0.00787  -0.02273 169 VAL A CA  
911  C C   . VAL A 146 ? 0.31099 0.36102 0.28548 -0.03727 0.00765  -0.02384 169 VAL A C   
912  O O   . VAL A 146 ? 0.35086 0.40545 0.32985 -0.03844 0.00907  -0.02326 169 VAL A O   
913  C CB  . VAL A 146 ? 0.21397 0.25903 0.18655 -0.03660 0.00723  -0.02347 169 VAL A CB  
914  C CG1 . VAL A 146 ? 0.33254 0.38201 0.30938 -0.03659 0.00833  -0.02356 169 VAL A CG1 
915  C CG2 . VAL A 146 ? 0.24081 0.28323 0.21311 -0.03784 0.00770  -0.02219 169 VAL A CG2 
916  N N   . ILE A 147 ? 0.32555 0.37314 0.29566 -0.03508 0.00570  -0.02549 170 ILE A N   
917  C CA  . ILE A 147 ? 0.34540 0.39591 0.31598 -0.03420 0.00543  -0.02651 170 ILE A CA  
918  C C   . ILE A 147 ? 0.52982 0.58343 0.50339 -0.03660 0.00685  -0.02520 170 ILE A C   
919  O O   . ILE A 147 ? 0.47455 0.53274 0.45164 -0.03710 0.00780  -0.02514 170 ILE A O   
920  C CB  . ILE A 147 ? 0.28628 0.33278 0.25101 -0.03155 0.00286  -0.02847 170 ILE A CB  
921  C CG1 . ILE A 147 ? 0.34446 0.38920 0.30693 -0.02888 0.00150  -0.03005 170 ILE A CG1 
922  C CG2 . ILE A 147 ? 0.34443 0.39354 0.30933 -0.03123 0.00268  -0.02915 170 ILE A CG2 
923  C CD1 . ILE A 147 ? 0.33172 0.37043 0.28752 -0.02643 -0.00141 -0.03180 170 ILE A CD1 
924  N N   . LEU A 148 ? 0.44177 0.49298 0.41399 -0.03814 0.00695  -0.02410 171 LEU A N   
925  C CA  . LEU A 148 ? 0.38548 0.43944 0.36025 -0.04040 0.00820  -0.02285 171 LEU A CA  
926  C C   . LEU A 148 ? 0.38010 0.43808 0.36062 -0.04267 0.01036  -0.02129 171 LEU A C   
927  O O   . LEU A 148 ? 0.38456 0.44472 0.36767 -0.04298 0.01086  -0.02063 171 LEU A O   
928  C CB  . LEU A 148 ? 0.33821 0.38850 0.30984 -0.04146 0.00763  -0.02206 171 LEU A CB  
929  C CG  . LEU A 148 ? 0.39321 0.43959 0.35917 -0.03951 0.00519  -0.02362 171 LEU A CG  
930  C CD1 . LEU A 148 ? 0.55175 0.59481 0.51497 -0.04092 0.00460  -0.02262 171 LEU A CD1 
931  C CD2 . LEU A 148 ? 0.30361 0.35283 0.26994 -0.03864 0.00490  -0.02468 171 LEU A CD2 
932  N N   . ILE A 149 ? 0.30973 0.36680 0.29143 -0.04306 0.01091  -0.02066 172 ILE A N   
933  C CA  . ILE A 149 ? 0.27044 0.32476 0.25455 -0.04088 0.01065  -0.01902 172 ILE A CA  
934  C C   . ILE A 149 ? 0.40172 0.45880 0.38796 -0.03961 0.01058  -0.01972 172 ILE A C   
935  O O   . ILE A 149 ? 0.54582 0.60150 0.53362 -0.03809 0.01024  -0.01862 172 ILE A O   
936  C CB  . ILE A 149 ? 0.19202 0.24318 0.17592 -0.04035 0.01060  -0.01827 172 ILE A CB  
937  C CG1 . ILE A 149 ? 0.20745 0.25533 0.18949 -0.04119 0.01050  -0.01717 172 ILE A CG1 
938  C CG2 . ILE A 149 ? 0.24910 0.29778 0.23531 -0.03793 0.01020  -0.01696 172 ILE A CG2 
939  C CD1 . ILE A 149 ? 0.28779 0.33338 0.26895 -0.04132 0.01054  -0.01686 172 ILE A CD1 
940  N N   . HIS A 150 ? 0.33392 0.39510 0.32025 -0.04022 0.01088  -0.02162 173 HIS A N   
941  C CA  . HIS A 150 ? 0.21594 0.28058 0.20417 -0.03913 0.01078  -0.02252 173 HIS A CA  
942  C C   . HIS A 150 ? 0.30879 0.37524 0.29748 -0.03910 0.01066  -0.02257 173 HIS A C   
943  O O   . HIS A 150 ? 0.35790 0.42374 0.34813 -0.03769 0.01034  -0.02176 173 HIS A O   
944  C CB  . HIS A 150 ? 0.28788 0.35363 0.27406 -0.03774 0.01003  -0.02458 173 HIS A CB  
945  C CG  . HIS A 150 ? 0.37583 0.44552 0.36413 -0.03661 0.00995  -0.02553 173 HIS A CG  
946  N ND1 . HIS A 150 ? 0.47093 0.54337 0.46259 -0.03712 0.01052  -0.02474 173 HIS A ND1 
947  C CD2 . HIS A 150 ? 0.37135 0.44092 0.35790 -0.03418 0.00889  -0.02701 173 HIS A CD2 
948  C CE1 . HIS A 150 ? 0.46339 0.53969 0.45651 -0.03619 0.01036  -0.02588 173 HIS A CE1 
949  N NE2 . HIS A 150 ? 0.35565 0.43013 0.34563 -0.03423 0.00936  -0.02724 173 HIS A NE2 
950  N N   . LEU A 151 ? 0.36861 0.43662 0.35547 -0.04044 0.01073  -0.02348 174 LEU A N   
951  C CA  . LEU A 151 ? 0.34564 0.41610 0.33296 -0.04074 0.01073  -0.02369 174 LEU A CA  
952  C C   . LEU A 151 ? 0.39733 0.46355 0.38556 -0.03966 0.01043  -0.02142 174 LEU A C   
953  O O   . LEU A 151 ? 0.52059 0.58784 0.51007 -0.03879 0.01022  -0.02120 174 LEU A O   
954  C CB  . LEU A 151 ? 0.35453 0.42106 0.33678 -0.03985 0.00942  -0.02430 174 LEU A CB  
955  C CG  . LEU A 151 ? 0.39111 0.45949 0.37334 -0.04042 0.00941  -0.02433 174 LEU A CG  
956  C CD1 . LEU A 151 ? 0.57872 0.65096 0.56229 -0.03905 0.00915  -0.02554 174 LEU A CD1 
957  C CD2 . LEU A 151 ? 0.31542 0.37914 0.29217 -0.03958 0.00785  -0.02491 174 LEU A CD2 
958  N N   . SER A 152 ? 0.41308 0.47448 0.40069 -0.03943 0.01030  -0.01980 175 SER A N   
959  C CA  . SER A 152 ? 0.24369 0.30116 0.23222 -0.03806 0.00989  -0.01785 175 SER A CA  
960  C C   . SER A 152 ? 0.29143 0.34743 0.28198 -0.03611 0.00956  -0.01706 175 SER A C   
961  O O   . SER A 152 ? 0.77416 0.82751 0.76569 -0.03494 0.00921  -0.01570 175 SER A O   
962  C CB  . SER A 152 ? 0.34938 0.40283 0.33691 -0.03816 0.00978  -0.01658 175 SER A CB  
963  O OG  . SER A 152 ? 0.49091 0.54543 0.47618 -0.04024 0.01005  -0.01722 175 SER A OG  
964  N N   . ASN A 153 ? 0.29417 0.35188 0.28532 -0.03582 0.00966  -0.01792 176 ASN A N   
965  C CA  . ASN A 153 ? 0.47310 0.52964 0.46590 -0.03425 0.00935  -0.01724 176 ASN A CA  
966  C C   . ASN A 153 ? 0.48023 0.54119 0.47359 -0.03439 0.00949  -0.01883 176 ASN A C   
967  O O   . ASN A 153 ? 0.46056 0.52171 0.45438 -0.03393 0.00949  -0.01912 176 ASN A O   
968  C CB  . ASN A 153 ? 0.52214 0.57473 0.51517 -0.03334 0.00918  -0.01611 176 ASN A CB  
969  C CG  . ASN A 153 ? 0.42399 0.47482 0.41854 -0.03183 0.00881  -0.01520 176 ASN A CG  
970  O OD1 . ASN A 153 ? 0.71479 0.76615 0.71017 -0.03134 0.00861  -0.01496 176 ASN A OD1 
971  N ND2 . ASN A 153 ? 0.51695 0.56567 0.51177 -0.03118 0.00872  -0.01471 176 ASN A ND2 
972  N N   . LEU A 154 ? 0.37195 0.43682 0.36536 -0.03495 0.00958  -0.01992 177 LEU A N   
973  C CA  . LEU A 154 ? 0.40636 0.47637 0.40044 -0.03496 0.00967  -0.02168 177 LEU A CA  
974  C C   . LEU A 154 ? 0.44158 0.51082 0.43710 -0.03358 0.00935  -0.02104 177 LEU A C   
975  O O   . LEU A 154 ? 0.48453 0.55640 0.48059 -0.03329 0.00936  -0.02208 177 LEU A O   
976  C CB  . LEU A 154 ? 0.35436 0.42865 0.34837 -0.03559 0.00974  -0.02284 177 LEU A CB  
977  C CG  . LEU A 154 ? 0.37438 0.45191 0.36699 -0.03721 0.01012  -0.02446 177 LEU A CG  
978  C CD1 . LEU A 154 ? 0.46732 0.54891 0.45996 -0.03770 0.01013  -0.02547 177 LEU A CD1 
979  C CD2 . LEU A 154 ? 0.41123 0.49268 0.40388 -0.03740 0.01029  -0.02646 177 LEU A CD2 
980  N N   . THR A 155 ? 0.49196 0.55779 0.48810 -0.03275 0.00904  -0.01942 178 THR A N   
981  C CA  . THR A 155 ? 0.52159 0.58651 0.51889 -0.03166 0.00873  -0.01877 178 THR A CA  
982  C C   . THR A 155 ? 0.59647 0.65833 0.59386 -0.03112 0.00867  -0.01807 178 THR A C   
983  O O   . THR A 155 ? 0.71204 0.77413 0.71019 -0.03048 0.00850  -0.01800 178 THR A O   
984  C CB  . THR A 155 ? 0.41663 0.47891 0.41451 -0.03101 0.00842  -0.01738 178 THR A CB  
985  O OG1 . THR A 155 ? 0.49405 0.55165 0.49166 -0.03066 0.00830  -0.01596 178 THR A OG1 
986  C CG2 . THR A 155 ? 0.45299 0.51803 0.45070 -0.03158 0.00849  -0.01797 178 THR A CG2 
987  N N   . GLY A 156 ? 0.60145 0.66046 0.59804 -0.03138 0.00878  -0.01751 179 GLY A N   
988  C CA  . GLY A 156 ? 0.57526 0.63108 0.57191 -0.03081 0.00869  -0.01671 179 GLY A CA  
989  C C   . GLY A 156 ? 0.62914 0.67624 0.61403 -0.02747 0.00790  -0.01718 179 GLY A C   
990  O O   . GLY A 156 ? 0.67119 0.72119 0.66795 -0.03017 0.00726  -0.01545 179 GLY A O   
991  N N   . LEU A 157 ? 0.54894 0.60119 0.54598 -0.03046 0.00716  -0.01558 180 LEU A N   
992  C CA  . LEU A 157 ? 0.67595 0.72191 0.66018 -0.02772 0.00773  -0.01645 180 LEU A CA  
993  C C   . LEU A 157 ? 0.81342 0.85714 0.79692 -0.02799 0.00772  -0.01582 180 LEU A C   
994  O O   . LEU A 157 ? 1.02495 1.07116 1.01984 -0.03074 0.00704  -0.01409 180 LEU A O   
995  C CB  . LEU A 157 ? 0.63535 0.68280 0.61969 -0.02776 0.00762  -0.01655 180 LEU A CB  
996  C CG  . LEU A 157 ? 0.69865 0.74875 0.68369 -0.02748 0.00759  -0.01719 180 LEU A CG  
997  C CD1 . LEU A 157 ? 0.55607 0.60745 0.54106 -0.02760 0.00748  -0.01718 180 LEU A CD1 
998  C CD2 . LEU A 157 ? 0.71116 0.76109 0.69648 -0.02720 0.00759  -0.01727 180 LEU A CD2 
999  N N   . ALA A 158 ? 0.79120 0.83502 0.77441 -0.02828 0.00774  -0.01579 181 ALA A N   
1000 C CA  . ALA A 158 ? 0.82351 0.86547 0.80601 -0.02856 0.00770  -0.01520 181 ALA A CA  
1001 C C   . ALA A 158 ? 0.93418 0.97420 0.91643 -0.02846 0.00774  -0.01491 181 ALA A C   
1002 O O   . ALA A 158 ? 1.10810 1.15232 1.10217 -0.03118 0.00719  -0.01392 181 ALA A O   
1003 C CB  . ALA A 158 ? 0.73159 0.77417 0.71378 -0.02896 0.00772  -0.01526 181 ALA A CB  
1004 N N   . ASN A 159 ? 0.91822 0.95652 0.90000 -0.02849 0.00765  -0.01435 182 ASN A N   
1005 C CA  . ASN A 159 ? 1.02038 1.06047 1.01290 -0.03126 0.00702  -0.01285 182 ASN A CA  
1006 C C   . ASN A 159 ? 0.93824 0.97735 0.93007 -0.03163 0.00697  -0.01251 182 ASN A C   
1007 O O   . ASN A 159 ? 0.96048 0.99807 0.95182 -0.03163 0.00698  -0.01227 182 ASN A O   
1008 C CB  . ASN A 159 ? 1.21612 1.25128 1.19756 -0.02813 0.00759  -0.01369 182 ASN A CB  
1009 C CG  . ASN A 159 ? 1.40057 1.44001 1.39340 -0.03064 0.00700  -0.01282 182 ASN A CG  
1010 O OD1 . ASN A 159 ? 1.02953 1.06498 1.01150 -0.02772 0.00756  -0.01381 182 ASN A OD1 
1011 N ND2 . ASN A 159 ? 1.19479 1.23172 1.17717 -0.02777 0.00774  -0.01444 182 ASN A ND2 
1012 N N   . ASP A 160 ? 0.94318 0.98318 0.93495 -0.03198 0.00691  -0.01248 183 ASP A N   
1013 C CA  . ASP A 160 ? 1.05402 1.09328 1.04511 -0.03241 0.00684  -0.01214 183 ASP A CA  
1014 C C   . ASP A 160 ? 1.16912 1.20612 1.14884 -0.02995 0.00753  -0.01351 183 ASP A C   
1015 O O   . ASP A 160 ? 1.11478 1.15720 1.10666 -0.03284 0.00699  -0.01284 183 ASP A O   
1016 C CB  . ASP A 160 ? 1.09754 1.13646 1.08836 -0.03243 0.00667  -0.01177 183 ASP A CB  
1017 C CG  . ASP A 160 ? 1.23115 1.26517 1.21086 -0.02914 0.00720  -0.01253 183 ASP A CG  
1018 O OD1 . ASP A 160 ? 1.28966 1.32374 1.26983 -0.02878 0.00724  -0.01271 183 ASP A OD1 
1019 O OD2 . ASP A 160 ? 1.37759 1.41053 1.35688 -0.02920 0.00708  -0.01212 183 ASP A OD2 
1020 N N   . TYR A 161 ? 1.19348 1.23338 1.18395 -0.03340 0.00685  -0.01208 184 TYR A N   
1021 C CA  . TYR A 161 ? 1.08471 1.12562 1.07503 -0.03400 0.00690  -0.01220 184 TYR A CA  
1022 C C   . TYR A 161 ? 0.98697 1.02754 0.97661 -0.03450 0.00672  -0.01174 184 TYR A C   
1023 O O   . TYR A 161 ? 1.02716 1.06630 1.01622 -0.03451 0.00658  -0.01129 184 TYR A O   
1024 C CB  . TYR A 161 ? 1.13851 1.17515 1.11678 -0.03122 0.00766  -0.01338 184 TYR A CB  
1025 C CG  . TYR A 161 ? 0.84772 0.88474 0.82677 -0.03074 0.00784  -0.01388 184 TYR A CG  
1026 C CD1 . TYR A 161 ? 0.85215 0.88792 0.83139 -0.03032 0.00784  -0.01373 184 TYR A CD1 
1027 C CD2 . TYR A 161 ? 0.62735 0.67110 0.61758 -0.03404 0.00893  -0.01302 184 TYR A CD2 
1028 C CE1 . TYR A 161 ? 0.73564 0.77184 0.71557 -0.02990 0.00798  -0.01416 184 TYR A CE1 
1029 C CE2 . TYR A 161 ? 0.58502 0.63010 0.57543 -0.03407 0.00911  -0.01385 184 TYR A CE2 
1030 C CZ  . TYR A 161 ? 0.71028 0.75307 0.70136 -0.03300 0.00896  -0.01323 184 TYR A CZ  
1031 O OH  . TYR A 161 ? 0.72768 0.77185 0.71896 -0.03304 0.00913  -0.01404 184 TYR A OH  
1032 N N   . ASN A 162 ? 0.88764 0.92968 0.87740 -0.03491 0.00671  -0.01186 185 ASN A N   
1033 C CA  . ASN A 162 ? 1.03500 1.08727 1.01295 -0.04415 0.00888  -0.01557 185 ASN A CA  
1034 C C   . ASN A 162 ? 0.76639 0.80728 0.75455 -0.03616 0.00644  -0.01105 185 ASN A C   
1035 O O   . ASN A 162 ? 0.68541 0.72557 0.67331 -0.03630 0.00656  -0.01113 185 ASN A O   
1036 C CB  . ASN A 162 ? 1.12738 1.16738 1.10462 -0.03247 0.00710  -0.01271 185 ASN A CB  
1037 C CG  . ASN A 162 ? 0.80884 0.85409 0.79879 -0.03588 0.00669  -0.01213 185 ASN A CG  
1038 O OD1 . ASN A 162 ? 0.86102 0.90173 0.83819 -0.03288 0.00744  -0.01335 185 ASN A OD1 
1039 N ND2 . ASN A 162 ? 1.02477 1.07197 1.01533 -0.03589 0.00672  -0.01245 185 ASN A ND2 
1040 N N   . LYS A 163 ? 0.84219 0.88302 0.82974 -0.03669 0.00622  -0.01059 186 LYS A N   
1041 C CA  . LYS A 163 ? 0.68893 0.72896 0.67541 -0.03758 0.00610  -0.01017 186 LYS A CA  
1042 C C   . LYS A 163 ? 0.72289 0.76008 0.69664 -0.03487 0.00684  -0.01139 186 LYS A C   
1043 O O   . LYS A 163 ? 0.50191 0.54245 0.48571 -0.03901 0.00817  -0.00953 186 LYS A O   
1044 C CB  . LYS A 163 ? 0.59208 0.63233 0.57806 -0.03806 0.00580  -0.00963 186 LYS A CB  
1045 N N   . ARG A 164 ? 0.76416 0.80712 0.75035 -0.03778 0.00819  -0.01003 187 ARG A N   
1046 C CA  . ARG A 164 ? 0.89949 0.94522 0.88344 -0.04011 0.00854  -0.01117 187 ARG A CA  
1047 C C   . ARG A 164 ? 0.76461 0.81111 0.74736 -0.04108 0.00889  -0.01219 187 ARG A C   
1048 O O   . ARG A 164 ? 0.63746 0.68525 0.61761 -0.04341 0.00912  -0.01297 187 ARG A O   
1049 C CB  . ARG A 164 ? 0.86555 0.91390 0.85026 -0.04013 0.00862  -0.01177 187 ARG A CB  
1050 C CG  . ARG A 164 ? 0.81837 0.87039 0.80173 -0.04190 0.00905  -0.01341 187 ARG A CG  
1051 C CD  . ARG A 164 ? 0.61339 0.66765 0.59852 -0.04094 0.00907  -0.01392 187 ARG A CD  
1052 N NE  . ARG A 164 ? 1.17896 1.23314 1.16585 -0.03941 0.00908  -0.01419 187 ARG A NE  
1053 C CZ  . ARG A 164 ? 1.18208 1.23858 1.17021 -0.03883 0.00911  -0.01484 187 ARG A CZ  
1054 N NH1 . ARG A 164 ? 1.12907 1.18822 1.11703 -0.03952 0.00915  -0.01534 187 ARG A NH1 
1055 N NH2 . ARG A 164 ? 0.83698 0.89314 0.82650 -0.03755 0.00905  -0.01493 187 ARG A NH2 
1056 N N   . THR A 165 ? 0.74569 0.79142 0.73015 -0.03947 0.00890  -0.01223 188 THR A N   
1057 C CA  . THR A 165 ? 0.63095 0.67728 0.61450 -0.04019 0.00920  -0.01314 188 THR A CA  
1058 C C   . THR A 165 ? 0.52552 0.57009 0.50687 -0.04151 0.00921  -0.01282 188 THR A C   
1059 O O   . THR A 165 ? 0.47739 0.52327 0.45651 -0.04354 0.00952  -0.01386 188 THR A O   
1060 C CB  . THR A 165 ? 0.46918 0.51418 0.45492 -0.03809 0.00908  -0.01282 188 THR A CB  
1061 O OG1 . THR A 165 ? 0.76100 0.80719 0.74856 -0.03695 0.00898  -0.01291 188 THR A OG1 
1062 C CG2 . THR A 165 ? 0.33645 0.38240 0.32138 -0.03881 0.00941  -0.01384 188 THR A CG2 
1063 N N   . MET A 166 ? 0.53082 0.57252 0.51276 -0.04043 0.00884  -0.01142 189 MET A N   
1064 C CA  . MET A 166 ? 0.34589 0.38565 0.32599 -0.04139 0.00874  -0.01093 189 MET A CA  
1065 C C   . MET A 166 ? 0.34411 0.38481 0.32093 -0.04425 0.00878  -0.01125 189 MET A C   
1066 O O   . MET A 166 ? 0.41329 0.45339 0.38740 -0.04620 0.00884  -0.01155 189 MET A O   
1067 C CB  . MET A 166 ? 0.32617 0.36325 0.30797 -0.03946 0.00831  -0.00947 189 MET A CB  
1068 C CG  . MET A 166 ? 0.54785 0.58365 0.53222 -0.03710 0.00821  -0.00917 189 MET A CG  
1069 S SD  . MET A 166 ? 0.73834 0.77468 0.72198 -0.03762 0.00859  -0.01019 189 MET A SD  
1070 C CE  . MET A 166 ? 0.54726 0.57760 0.52122 -0.03329 0.00721  -0.01121 189 MET A CE  
1071 N N   . GLY A 167 ? 0.49637 0.53838 0.47315 -0.04471 0.00868  -0.01116 190 GLY A N   
1072 C CA  . GLY A 167 ? 0.32395 0.36693 0.29738 -0.04768 0.00863  -0.01145 190 GLY A CA  
1073 C C   . GLY A 167 ? 0.35531 0.40080 0.32651 -0.05003 0.00907  -0.01314 190 GLY A C   
1074 O O   . GLY A 167 ? 0.39722 0.44238 0.36467 -0.05299 0.00900  -0.01344 190 GLY A O   
1075 N N   . LEU A 168 ? 0.56641 0.61442 0.53973 -0.04888 0.00946  -0.01428 191 LEU A N   
1076 C CA  . LEU A 168 ? 0.50173 0.55269 0.47350 -0.05060 0.00986  -0.01620 191 LEU A CA  
1077 C C   . LEU A 168 ? 0.50717 0.55372 0.47584 -0.04944 0.00875  -0.01656 191 LEU A C   
1078 O O   . LEU A 168 ? 0.65845 0.70093 0.62227 -0.04756 0.00652  -0.01791 191 LEU A O   
1079 C CB  . LEU A 168 ? 0.40362 0.45755 0.37869 -0.04873 0.01021  -0.01714 191 LEU A CB  
1080 C CG  . LEU A 168 ? 0.70664 0.76056 0.67976 -0.04665 0.00914  -0.01928 191 LEU A CG  
1081 C CD1 . LEU A 168 ? 0.66715 0.72146 0.63809 -0.04557 0.00797  -0.02048 191 LEU A CD1 
1082 C CD2 . LEU A 168 ? 0.74545 0.80316 0.72303 -0.04635 0.01033  -0.01949 191 LEU A CD2 
1083 N N   . LEU A 169 ? 0.37305 0.41981 0.34430 -0.05009 0.00991  -0.01548 192 LEU A N   
1084 C CA  . LEU A 169 ? 0.27706 0.32048 0.24597 -0.04935 0.00919  -0.01581 192 LEU A CA  
1085 C C   . LEU A 169 ? 0.30059 0.33953 0.26514 -0.05000 0.00787  -0.01511 192 LEU A C   
1086 O O   . LEU A 169 ? 0.29102 0.32560 0.25126 -0.04827 0.00579  -0.01621 192 LEU A O   
1087 C CB  . LEU A 169 ? 0.27154 0.31460 0.24388 -0.04814 0.00990  -0.01483 192 LEU A CB  
1088 C CG  . LEU A 169 ? 0.43549 0.48040 0.41114 -0.04589 0.01012  -0.01547 192 LEU A CG  
1089 C CD1 . LEU A 169 ? 0.42158 0.46364 0.39935 -0.04343 0.00987  -0.01432 192 LEU A CD1 
1090 C CD2 . LEU A 169 ? 0.46763 0.51537 0.44222 -0.04683 0.01039  -0.01748 192 LEU A CD2 
1091 N N   . VAL A 170 ? 0.37979 0.41977 0.34545 -0.05251 0.00889  -0.01329 193 VAL A N   
1092 C CA  . VAL A 170 ? 0.32964 0.36582 0.29161 -0.05360 0.00780  -0.01223 193 VAL A CA  
1093 C C   . VAL A 170 ? 0.32198 0.35477 0.27890 -0.05230 0.00517  -0.01349 193 VAL A C   
1094 O O   . VAL A 170 ? 0.35680 0.38487 0.30931 -0.05170 0.00299  -0.01379 193 VAL A O   
1095 C CB  . VAL A 170 ? 0.38928 0.42510 0.35358 -0.05293 0.00795  -0.01038 193 VAL A CB  
1096 C CG1 . VAL A 170 ? 0.34565 0.37886 0.30624 -0.05524 0.00715  -0.00911 193 VAL A CG1 
1097 C CG2 . VAL A 170 ? 0.46313 0.49778 0.43119 -0.04954 0.00804  -0.00980 193 VAL A CG2 
1098 N N   . SER A 171 ? 0.38665 0.42176 0.34419 -0.05184 0.00512  -0.01433 194 SER A N   
1099 C CA  . SER A 171 ? 0.44690 0.47888 0.39975 -0.05043 0.00243  -0.01578 194 SER A CA  
1100 C C   . SER A 171 ? 0.26981 0.29815 0.21930 -0.04731 0.00005  -0.01812 194 SER A C   
1101 O O   . SER A 171 ? 0.44634 0.47006 0.39102 -0.04614 -0.00290 -0.01922 194 SER A O   
1102 C CB  . SER A 171 ? 0.43090 0.46648 0.38543 -0.05044 0.00302  -0.01627 194 SER A CB  
1103 O OG  . SER A 171 ? 0.36931 0.40811 0.32683 -0.04892 0.00401  -0.01748 194 SER A OG  
1104 N N   . ASP A 172 ? 0.33085 0.36120 0.28286 -0.04593 0.00108  -0.01896 195 ASP A N   
1105 C CA  . ASP A 172 ? 0.33703 0.36435 0.28600 -0.04281 -0.00115 -0.02128 195 ASP A CA  
1106 C C   . ASP A 172 ? 0.32218 0.34495 0.26835 -0.04243 -0.00259 -0.02122 195 ASP A C   
1107 O O   . ASP A 172 ? 0.49303 0.51140 0.43481 -0.04021 -0.00562 -0.02306 195 ASP A O   
1108 C CB  . ASP A 172 ? 0.28351 0.31453 0.23605 -0.04160 0.00038  -0.02202 195 ASP A CB  
1109 C CG  . ASP A 172 ? 0.37849 0.40649 0.32789 -0.03838 -0.00185 -0.02432 195 ASP A CG  
1110 O OD1 . ASP A 172 ? 0.49703 0.52257 0.44259 -0.03635 -0.00433 -0.02619 195 ASP A OD1 
1111 O OD2 . ASP A 172 ? 0.50128 0.52929 0.45197 -0.03783 -0.00122 -0.02429 195 ASP A OD2 
1112 N N   . ILE A 173 ? 0.28906 0.31283 0.23778 -0.04451 -0.00060 -0.01919 196 ILE A N   
1113 C CA  . ILE A 173 ? 0.20269 0.22235 0.14893 -0.04440 -0.00183 -0.01891 196 ILE A CA  
1114 C C   . ILE A 173 ? 0.26511 0.28039 0.20673 -0.04477 -0.00456 -0.01895 196 ILE A C   
1115 O O   . ILE A 173 ? 0.48667 0.49743 0.42449 -0.04314 -0.00738 -0.02029 196 ILE A O   
1116 C CB  . ILE A 173 ? 0.18634 0.20811 0.13620 -0.04680 0.00089  -0.01656 196 ILE A CB  
1117 C CG1 . ILE A 173 ? 0.14032 0.16580 0.09452 -0.04620 0.00298  -0.01679 196 ILE A CG1 
1118 C CG2 . ILE A 173 ? 0.16742 0.18486 0.11441 -0.04701 -0.00046 -0.01601 196 ILE A CG2 
1119 C CD1 . ILE A 173 ? 0.30319 0.33239 0.26225 -0.04883 0.00595  -0.01459 196 ILE A CD1 
1120 N N   . GLY A 174 ? 0.23623 0.25289 0.17828 -0.04694 -0.00390 -0.01752 197 GLY A N   
1121 C CA  . GLY A 174 ? 0.17834 0.19110 0.11623 -0.04760 -0.00656 -0.01736 197 GLY A CA  
1122 C C   . GLY A 174 ? 0.19954 0.20897 0.13342 -0.04474 -0.01011 -0.02023 197 GLY A C   
1123 O O   . GLY A 174 ? 0.34329 0.34812 0.27334 -0.04409 -0.01323 -0.02106 197 GLY A O   
1124 N N   . THR A 175 ? 0.27943 0.29126 0.21429 -0.04297 -0.00979 -0.02185 198 THR A N   
1125 C CA  . THR A 175 ? 0.31954 0.32848 0.25064 -0.03998 -0.01316 -0.02477 198 THR A CA  
1126 C C   . THR A 175 ? 0.25752 0.26231 0.18588 -0.03763 -0.01568 -0.02655 198 THR A C   
1127 O O   . THR A 175 ? 0.38930 0.38995 0.31376 -0.03636 -0.01927 -0.02822 198 THR A O   
1128 C CB  . THR A 175 ? 0.41121 0.42368 0.34416 -0.03831 -0.01202 -0.02606 198 THR A CB  
1129 O OG1 . THR A 175 ? 0.44513 0.46173 0.38088 -0.04051 -0.00975 -0.02450 198 THR A OG1 
1130 C CG2 . THR A 175 ? 0.45593 0.46520 0.38465 -0.03501 -0.01562 -0.02915 198 THR A CG2 
1131 N N   . ILE A 176 ? 0.33809 0.34420 0.26870 -0.03703 -0.01392 -0.02634 199 ILE A N   
1132 C CA  . ILE A 176 ? 0.23875 0.24139 0.16709 -0.03463 -0.01611 -0.02811 199 ILE A CA  
1133 C C   . ILE A 176 ? 0.28544 0.28434 0.21167 -0.03598 -0.01779 -0.02727 199 ILE A C   
1134 O O   . ILE A 176 ? 0.22659 0.22165 0.14957 -0.03411 -0.02114 -0.02931 199 ILE A O   
1135 C CB  . ILE A 176 ? 0.20836 0.21366 0.13998 -0.03415 -0.01352 -0.02766 199 ILE A CB  
1136 C CG1 . ILE A 176 ? 0.17815 0.18720 0.11181 -0.03295 -0.01213 -0.02850 199 ILE A CG1 
1137 C CG2 . ILE A 176 ? 0.28125 0.28301 0.21056 -0.03177 -0.01569 -0.02934 199 ILE A CG2 
1138 C CD1 . ILE A 176 ? 0.22420 0.23764 0.16268 -0.03383 -0.00870 -0.02720 199 ILE A CD1 
1139 N N   . VAL A 177 ? 0.32282 0.32300 0.25104 -0.03931 -0.01551 -0.02427 200 VAL A N   
1140 C CA  . VAL A 177 ? 0.23100 0.22773 0.15731 -0.04097 -0.01689 -0.02300 200 VAL A CA  
1141 C C   . VAL A 177 ? 0.32878 0.32211 0.25137 -0.04105 -0.02045 -0.02394 200 VAL A C   
1142 O O   . VAL A 177 ? 0.37305 0.36237 0.29286 -0.04060 -0.02338 -0.02479 200 VAL A O   
1143 C CB  . VAL A 177 ? 0.29272 0.29190 0.22190 -0.04448 -0.01362 -0.01951 200 VAL A CB  
1144 C CG1 . VAL A 177 ? 0.32883 0.32436 0.25563 -0.04643 -0.01524 -0.01793 200 VAL A CG1 
1145 C CG2 . VAL A 177 ? 0.32230 0.32452 0.25520 -0.04439 -0.01049 -0.01880 200 VAL A CG2 
1146 N N   . TRP A 178 ? 0.35918 0.35418 0.28184 -0.04180 -0.02025 -0.02373 201 TRP A N   
1147 C CA  . TRP A 178 ? 0.25197 0.24400 0.17124 -0.04185 -0.02371 -0.02476 201 TRP A CA  
1148 C C   . TRP A 178 ? 0.30126 0.29098 0.21792 -0.03819 -0.02712 -0.02862 201 TRP A C   
1149 O O   . TRP A 178 ? 0.36614 0.35225 0.27990 -0.03795 -0.03052 -0.02986 201 TRP A O   
1150 C CB  . TRP A 178 ? 0.29910 0.29381 0.21922 -0.04334 -0.02257 -0.02375 201 TRP A CB  
1151 C CG  . TRP A 178 ? 0.31760 0.31520 0.24051 -0.04688 -0.01921 -0.02016 201 TRP A CG  
1152 C CD1 . TRP A 178 ? 0.47144 0.47379 0.39762 -0.04809 -0.01597 -0.01887 201 TRP A CD1 
1153 C CD2 . TRP A 178 ? 0.37241 0.36855 0.29513 -0.04967 -0.01883 -0.01744 201 TRP A CD2 
1154 N NE1 . TRP A 178 ? 0.56071 0.56481 0.48887 -0.05132 -0.01358 -0.01570 201 TRP A NE1 
1155 C CE2 . TRP A 178 ? 0.46416 0.46448 0.39011 -0.05232 -0.01527 -0.01470 201 TRP A CE2 
1156 C CE3 . TRP A 178 ? 0.45096 0.44280 0.37118 -0.05021 -0.02121 -0.01702 201 TRP A CE3 
1157 C CZ2 . TRP A 178 ? 0.47176 0.47212 0.39834 -0.05531 -0.01404 -0.01165 201 TRP A CZ2 
1158 C CZ3 . TRP A 178 ? 0.40960 0.40131 0.33037 -0.05330 -0.01999 -0.01380 201 TRP A CZ3 
1159 C CH2 . TRP A 178 ? 0.47788 0.47386 0.40171 -0.05574 -0.01644 -0.01118 201 TRP A CH2 
1160 N N   . GLY A 179 ? 0.31744 0.30940 0.23518 -0.03543 -0.02626 -0.03053 202 GLY A N   
1161 C CA  . GLY A 179 ? 0.22651 0.21685 0.14186 -0.03168 -0.02938 -0.03434 202 GLY A CA  
1162 C C   . GLY A 179 ? 0.27175 0.25940 0.18594 -0.03065 -0.03115 -0.03553 202 GLY A C   
1163 O O   . GLY A 179 ? 0.38427 0.36981 0.29598 -0.02927 -0.03446 -0.03815 202 GLY A O   
1164 N N   . THR A 180 ? 0.38954 0.37766 0.30573 -0.03158 -0.02881 -0.03365 203 THR A N   
1165 C CA  . THR A 180 ? 0.27163 0.25729 0.18689 -0.03081 -0.03026 -0.03452 203 THR A CA  
1166 C C   . THR A 180 ? 0.28673 0.26874 0.19966 -0.03309 -0.03269 -0.03373 203 THR A C   
1167 O O   . THR A 180 ? 0.51954 0.49895 0.43029 -0.03207 -0.03558 -0.03584 203 THR A O   
1168 C CB  . THR A 180 ? 0.35466 0.34161 0.27261 -0.03185 -0.02708 -0.03221 203 THR A CB  
1169 O OG1 . THR A 180 ? 0.35589 0.34627 0.27620 -0.03049 -0.02458 -0.03235 203 THR A OG1 
1170 C CG2 . THR A 180 ? 0.33453 0.31914 0.25155 -0.03063 -0.02855 -0.03338 203 THR A CG2 
1171 N N   . THR A 181 ? 0.34310 0.32496 0.25650 -0.03647 -0.03146 -0.03051 204 THR A N   
1172 C CA  . THR A 181 ? 0.41398 0.39203 0.32501 -0.03899 -0.03383 -0.02914 204 THR A CA  
1173 C C   . THR A 181 ? 0.48069 0.45665 0.38883 -0.03801 -0.03752 -0.03173 204 THR A C   
1174 O O   . THR A 181 ? 0.41413 0.38610 0.31973 -0.03854 -0.04055 -0.03234 204 THR A O   
1175 C CB  . THR A 181 ? 0.24856 0.22764 0.16074 -0.04264 -0.03172 -0.02530 204 THR A CB  
1176 O OG1 . THR A 181 ? 0.27532 0.25680 0.19037 -0.04364 -0.02810 -0.02306 204 THR A OG1 
1177 C CG2 . THR A 181 ? 0.34912 0.32404 0.25874 -0.04534 -0.03437 -0.02352 204 THR A CG2 
1178 N N   . ALA A 182 ? 0.43873 0.41727 0.34718 -0.03667 -0.03731 -0.03323 205 ALA A N   
1179 C CA  . ALA A 182 ? 0.31738 0.29458 0.22323 -0.03556 -0.04061 -0.03598 205 ALA A CA  
1180 C C   . ALA A 182 ? 0.40721 0.38329 0.31158 -0.03298 -0.04276 -0.03949 205 ALA A C   
1181 O O   . ALA A 182 ? 0.51803 0.49060 0.41947 -0.03361 -0.04593 -0.04065 205 ALA A O   
1182 C CB  . ALA A 182 ? 0.36008 0.34082 0.26682 -0.03415 -0.03963 -0.03711 205 ALA A CB  
1183 N N   . ALA A 183 ? 0.46600 0.44484 0.37222 -0.03032 -0.04106 -0.04100 206 ALA A N   
1184 C CA  . ALA A 183 ? 0.40601 0.38464 0.31106 -0.02811 -0.04262 -0.04430 206 ALA A CA  
1185 C C   . ALA A 183 ? 0.44536 0.41910 0.34854 -0.02999 -0.04430 -0.04316 206 ALA A C   
1186 O O   . ALA A 183 ? 0.57895 0.54985 0.47934 -0.02972 -0.04687 -0.04514 206 ALA A O   
1187 C CB  . ALA A 183 ? 0.39476 0.37736 0.30241 -0.02513 -0.04034 -0.04560 206 ALA A CB  
1188 N N   . LEU A 184 ? 0.42243 0.39470 0.32678 -0.03212 -0.04290 -0.03971 207 LEU A N   
1189 C CA  . LEU A 184 ? 0.43089 0.39840 0.33354 -0.03391 -0.04451 -0.03824 207 LEU A CA  
1190 C C   . LEU A 184 ? 0.51105 0.47360 0.41047 -0.03641 -0.04783 -0.03714 207 LEU A C   
1191 O O   . LEU A 184 ? 0.59027 0.54785 0.48733 -0.03744 -0.05031 -0.03665 207 LEU A O   
1192 C CB  . LEU A 184 ? 0.35863 0.32668 0.26357 -0.03562 -0.04177 -0.03477 207 LEU A CB  
1193 C CG  . LEU A 184 ? 0.44535 0.41661 0.35304 -0.03362 -0.03897 -0.03525 207 LEU A CG  
1194 C CD1 . LEU A 184 ? 0.31523 0.28740 0.22514 -0.03592 -0.03593 -0.03146 207 LEU A CD1 
1195 C CD2 . LEU A 184 ? 0.41723 0.38625 0.32366 -0.03228 -0.04056 -0.03707 207 LEU A CD2 
1196 N N   . SER A 185 ? 0.51100 0.47452 0.41023 -0.03746 -0.04805 -0.03653 208 SER A N   
1197 C CA  . SER A 185 ? 0.42153 0.38067 0.31800 -0.04010 -0.05107 -0.03503 208 SER A CA  
1198 C C   . SER A 185 ? 0.52924 0.48621 0.42265 -0.03885 -0.05435 -0.03816 208 SER A C   
1199 O O   . SER A 185 ? 0.48922 0.44828 0.38253 -0.03607 -0.05415 -0.04151 208 SER A O   
1200 C CB  . SER A 185 ? 0.35996 0.32136 0.25785 -0.04224 -0.04942 -0.03237 208 SER A CB  
1201 O OG  . SER A 185 ? 0.53971 0.50263 0.43996 -0.04390 -0.04643 -0.02914 208 SER A OG  
1202 N N   . LYS A 186 ? 0.67023 0.62294 0.56101 -0.04113 -0.05739 -0.03688 209 LYS A N   
1203 C CA  . LYS A 186 ? 0.77932 0.72896 0.66672 -0.04052 -0.06086 -0.03928 209 LYS A CA  
1204 C C   . LYS A 186 ? 0.69423 0.64324 0.58085 -0.04276 -0.06212 -0.03764 209 LYS A C   
1205 O O   . LYS A 186 ? 0.70416 0.65371 0.59223 -0.04528 -0.06095 -0.03423 209 LYS A O   
1206 C CB  . LYS A 186 ? 0.64575 0.58807 0.52949 -0.04102 -0.06477 -0.03941 209 LYS A CB  
1207 C CG  . LYS A 186 ? 0.67524 0.61726 0.55864 -0.03849 -0.06439 -0.04178 209 LYS A CG  
1208 C CD  . LYS A 186 ? 0.63062 0.56538 0.50936 -0.03814 -0.06893 -0.04320 209 LYS A CD  
1209 C CE  . LYS A 186 ? 0.83148 0.76528 0.70941 -0.03568 -0.06879 -0.04539 209 LYS A CE  
1210 N NZ  . LYS A 186 ? 0.86032 0.79543 0.73648 -0.03302 -0.06908 -0.04909 209 LYS A NZ  
1211 N N   . GLY A 187 ? 0.55532 0.50304 0.43944 -0.04196 -0.06456 -0.04000 210 GLY A N   
1212 C CA  . GLY A 187 ? 0.68834 0.63417 0.57099 -0.04423 -0.06666 -0.03853 210 GLY A CA  
1213 C C   . GLY A 187 ? 0.65695 0.60819 0.54283 -0.04524 -0.06339 -0.03659 210 GLY A C   
1214 O O   . GLY A 187 ? 0.70083 0.65792 0.58943 -0.04311 -0.06008 -0.03803 210 GLY A O   
1215 N N   . TYR A 188 ? 0.91107 0.86013 0.79653 -0.04860 -0.06444 -0.03309 211 TYR A N   
1216 C CA  . TYR A 188 ? 0.80656 0.76006 0.69441 -0.04992 -0.06177 -0.03108 211 TYR A CA  
1217 C C   . TYR A 188 ? 0.64035 0.59794 0.53176 -0.04996 -0.05739 -0.02915 211 TYR A C   
1218 O O   . TYR A 188 ? 0.72619 0.68863 0.62008 -0.04969 -0.05423 -0.02863 211 TYR A O   
1219 C CB  . TYR A 188 ? 0.78483 0.73488 0.67109 -0.05374 -0.06422 -0.02770 211 TYR A CB  
1220 C CG  . TYR A 188 ? 1.23192 1.17813 1.11477 -0.05382 -0.06846 -0.02944 211 TYR A CG  
1221 C CD1 . TYR A 188 ? 1.30191 1.24164 1.18142 -0.05392 -0.07257 -0.03024 211 TYR A CD1 
1222 C CD2 . TYR A 188 ? 1.44162 1.39043 1.32447 -0.05377 -0.06841 -0.03023 211 TYR A CD2 
1223 C CE1 . TYR A 188 ? 1.56267 1.49842 1.43883 -0.05401 -0.07655 -0.03176 211 TYR A CE1 
1224 C CE2 . TYR A 188 ? 1.42722 1.37246 1.30684 -0.05386 -0.07230 -0.03183 211 TYR A CE2 
1225 C CZ  . TYR A 188 ? 1.65472 1.59333 1.53095 -0.05400 -0.07638 -0.03258 211 TYR A CZ  
1226 O OH  . TYR A 188 ? 1.64029 1.57480 1.51306 -0.05414 -0.08038 -0.03405 211 TYR A OH  
1227 N N   . VAL A 189 ? 0.51479 0.47025 0.40638 -0.05036 -0.05718 -0.02801 212 VAL A N   
1228 C CA  . VAL A 189 ? 0.49504 0.45407 0.38982 -0.05034 -0.05311 -0.02630 212 VAL A CA  
1229 C C   . VAL A 189 ? 0.62211 0.58601 0.51912 -0.04676 -0.05032 -0.02931 212 VAL A C   
1230 O O   . VAL A 189 ? 0.62611 0.59437 0.52599 -0.04672 -0.04666 -0.02811 212 VAL A O   
1231 C CB  . VAL A 189 ? 0.59116 0.54666 0.48537 -0.05122 -0.05385 -0.02485 212 VAL A CB  
1232 C CG1 . VAL A 189 ? 0.66333 0.62250 0.56074 -0.05133 -0.04961 -0.02302 212 VAL A CG1 
1233 C CG2 . VAL A 189 ? 0.75091 0.70149 0.64287 -0.05479 -0.05693 -0.02167 212 VAL A CG2 
1234 N N   . ARG A 190 ? 0.64771 0.61089 0.54339 -0.04385 -0.05203 -0.03310 213 ARG A N   
1235 C CA  . ARG A 190 ? 0.53979 0.50774 0.43739 -0.04035 -0.04985 -0.03610 213 ARG A CA  
1236 C C   . ARG A 190 ? 0.62522 0.59702 0.52400 -0.03998 -0.04848 -0.03631 213 ARG A C   
1237 O O   . ARG A 190 ? 0.67436 0.65043 0.57585 -0.03851 -0.04534 -0.03636 213 ARG A O   
1238 C CB  . ARG A 190 ? 0.46873 0.43533 0.36420 -0.03778 -0.05224 -0.04005 213 ARG A CB  
1239 C CG  . ARG A 190 ? 0.60281 0.57464 0.49980 -0.03425 -0.05061 -0.04345 213 ARG A CG  
1240 C CD  . ARG A 190 ? 0.52240 0.49292 0.41695 -0.03242 -0.05272 -0.04698 213 ARG A CD  
1241 N NE  . ARG A 190 ? 0.51429 0.48317 0.40909 -0.03199 -0.05231 -0.04685 213 ARG A NE  
1242 C CZ  . ARG A 190 ? 0.52134 0.48834 0.41396 -0.03075 -0.05377 -0.04925 213 ARG A CZ  
1243 N NH1 . ARG A 190 ? 0.68562 0.65188 0.57536 -0.02990 -0.05568 -0.05193 213 ARG A NH1 
1244 N NH2 . ARG A 190 ? 0.55322 0.51868 0.44625 -0.03049 -0.05327 -0.04876 213 ARG A NH2 
1245 N N   . VAL A 191 ? 0.65264 0.62268 0.54930 -0.04135 -0.05091 -0.03632 214 VAL A N   
1246 C CA  . VAL A 191 ? 0.59362 0.56718 0.49105 -0.04069 -0.04999 -0.03699 214 VAL A CA  
1247 C C   . VAL A 191 ? 0.52107 0.49739 0.42124 -0.04276 -0.04646 -0.03338 214 VAL A C   
1248 O O   . VAL A 191 ? 0.59464 0.57504 0.49688 -0.04144 -0.04388 -0.03371 214 VAL A O   
1249 C CB  . VAL A 191 ? 0.41643 0.38719 0.31084 -0.04200 -0.05353 -0.03759 214 VAL A CB  
1250 C CG1 . VAL A 191 ? 0.63175 0.60613 0.52708 -0.04173 -0.05240 -0.03774 214 VAL A CG1 
1251 C CG2 . VAL A 191 ? 0.41821 0.38658 0.30977 -0.04003 -0.05664 -0.04130 214 VAL A CG2 
1252 N N   . ILE A 192 ? 0.55392 0.52809 0.45407 -0.04621 -0.04626 -0.02973 215 ILE A N   
1253 C CA  . ILE A 192 ? 0.59837 0.57547 0.50102 -0.04872 -0.04277 -0.02610 215 ILE A CA  
1254 C C   . ILE A 192 ? 0.47141 0.45217 0.37722 -0.04727 -0.03881 -0.02596 215 ILE A C   
1255 O O   . ILE A 192 ? 0.53175 0.51659 0.43991 -0.04724 -0.03577 -0.02526 215 ILE A O   
1256 C CB  . ILE A 192 ? 0.42848 0.40270 0.33034 -0.05257 -0.04351 -0.02231 215 ILE A CB  
1257 C CG1 . ILE A 192 ? 0.56362 0.53433 0.46253 -0.05439 -0.04740 -0.02195 215 ILE A CG1 
1258 C CG2 . ILE A 192 ? 0.26292 0.24091 0.16761 -0.05507 -0.03948 -0.01870 215 ILE A CG2 
1259 C CD1 . ILE A 192 ? 0.61815 0.58511 0.51576 -0.05794 -0.04910 -0.01844 215 ILE A CD1 
1260 N N   . PHE A 193 ? 0.50589 0.48516 0.41183 -0.04619 -0.03882 -0.02654 216 PHE A N   
1261 C CA  . PHE A 193 ? 0.49828 0.48071 0.40720 -0.04507 -0.03519 -0.02616 216 PHE A CA  
1262 C C   . PHE A 193 ? 0.44671 0.43226 0.35673 -0.04176 -0.03422 -0.02895 216 PHE A C   
1263 O O   . PHE A 193 ? 0.54687 0.53613 0.45980 -0.04172 -0.03070 -0.02789 216 PHE A O   
1264 C CB  . PHE A 193 ? 0.43028 0.41025 0.33884 -0.04442 -0.03579 -0.02644 216 PHE A CB  
1265 C CG  . PHE A 193 ? 0.36616 0.34411 0.27458 -0.04782 -0.03547 -0.02290 216 PHE A CG  
1266 C CD1 . PHE A 193 ? 0.43154 0.41256 0.34266 -0.05009 -0.03172 -0.01969 216 PHE A CD1 
1267 C CD2 . PHE A 193 ? 0.42758 0.40072 0.33326 -0.04882 -0.03888 -0.02272 216 PHE A CD2 
1268 C CE1 . PHE A 193 ? 0.58656 0.56611 0.49753 -0.05311 -0.03140 -0.01644 216 PHE A CE1 
1269 C CE2 . PHE A 193 ? 0.42105 0.39234 0.32653 -0.05192 -0.03870 -0.01927 216 PHE A CE2 
1270 C CZ  . PHE A 193 ? 0.65168 0.62631 0.55976 -0.05398 -0.03495 -0.01617 216 PHE A CZ  
1271 N N   . PHE A 194 ? 0.42859 0.41286 0.33638 -0.03911 -0.03730 -0.03246 217 PHE A N   
1272 C CA  . PHE A 194 ? 0.57486 0.56201 0.48327 -0.03593 -0.03675 -0.03505 217 PHE A CA  
1273 C C   . PHE A 194 ? 0.59775 0.58788 0.50759 -0.03739 -0.03460 -0.03331 217 PHE A C   
1274 O O   . PHE A 194 ? 0.80099 0.79443 0.71309 -0.03643 -0.03184 -0.03311 217 PHE A O   
1275 C CB  . PHE A 194 ? 0.59809 0.58386 0.50373 -0.03319 -0.04052 -0.03913 217 PHE A CB  
1276 C CG  . PHE A 194 ? 0.62996 0.61864 0.53590 -0.02963 -0.04027 -0.04189 217 PHE A CG  
1277 C CD1 . PHE A 194 ? 0.61710 0.60698 0.52384 -0.02649 -0.03957 -0.04373 217 PHE A CD1 
1278 C CD2 . PHE A 194 ? 0.67454 0.66448 0.57977 -0.02943 -0.04079 -0.04243 217 PHE A CD2 
1279 C CE1 . PHE A 194 ? 0.60787 0.59964 0.51435 -0.02317 -0.03958 -0.04589 217 PHE A CE1 
1280 C CE2 . PHE A 194 ? 0.77191 0.76393 0.67699 -0.02611 -0.04070 -0.04470 217 PHE A CE2 
1281 C CZ  . PHE A 194 ? 0.71138 0.70400 0.61689 -0.02297 -0.04017 -0.04632 217 PHE A CZ  
1282 N N   . LEU A 195 ? 0.51153 0.50061 0.42017 -0.03995 -0.03578 -0.03188 218 LEU A N   
1283 C CA  . LEU A 195 ? 0.59209 0.58426 0.50208 -0.04140 -0.03383 -0.03036 218 LEU A CA  
1284 C C   . LEU A 195 ? 0.60257 0.59831 0.51630 -0.04380 -0.02925 -0.02699 218 LEU A C   
1285 O O   . LEU A 195 ? 0.62766 0.62738 0.54378 -0.04379 -0.02655 -0.02653 218 LEU A O   
1286 C CB  . LEU A 195 ? 0.69749 0.68765 0.60534 -0.04380 -0.03622 -0.02938 218 LEU A CB  
1287 C CG  . LEU A 195 ? 0.68061 0.66842 0.58523 -0.04159 -0.04041 -0.03290 218 LEU A CG  
1288 C CD1 . LEU A 195 ? 0.83570 0.82116 0.73827 -0.04447 -0.04283 -0.03149 218 LEU A CD1 
1289 C CD2 . LEU A 195 ? 0.57817 0.56887 0.48312 -0.03849 -0.03996 -0.03548 218 LEU A CD2 
1290 N N   . MET A 196 ? 0.37591 0.37060 0.29039 -0.04597 -0.02825 -0.02463 219 MET A N   
1291 C CA  . MET A 196 ? 0.58613 0.58472 0.50448 -0.04796 -0.02382 -0.02183 219 MET A CA  
1292 C C   . MET A 196 ? 0.54547 0.54680 0.46627 -0.04552 -0.02160 -0.02324 219 MET A C   
1293 O O   . MET A 196 ? 0.53115 0.53705 0.45556 -0.04645 -0.01805 -0.02193 219 MET A O   
1294 C CB  . MET A 196 ? 0.46233 0.45936 0.38091 -0.05048 -0.02320 -0.01917 219 MET A CB  
1295 C CG  . MET A 196 ? 0.59335 0.58591 0.50855 -0.05202 -0.02670 -0.01850 219 MET A CG  
1296 S SD  . MET A 196 ? 0.75745 0.74900 0.67353 -0.05470 -0.02525 -0.01521 219 MET A SD  
1297 C CE  . MET A 196 ? 0.48157 0.47878 0.40146 -0.05781 -0.02066 -0.01178 219 MET A CE  
1298 N N   . GLY A 197 ? 0.44625 0.44502 0.36532 -0.04250 -0.02370 -0.02587 220 GLY A N   
1299 C CA  . GLY A 197 ? 0.35780 0.35890 0.27878 -0.04003 -0.02204 -0.02730 220 GLY A CA  
1300 C C   . GLY A 197 ? 0.51277 0.51685 0.43450 -0.03900 -0.02133 -0.02829 220 GLY A C   
1301 O O   . GLY A 197 ? 0.54457 0.55276 0.46970 -0.03901 -0.01823 -0.02767 220 GLY A O   
1302 N N   . LEU A 198 ? 0.51648 0.51868 0.43519 -0.03817 -0.02426 -0.02986 221 LEU A N   
1303 C CA  . LEU A 198 ? 0.45131 0.45607 0.37035 -0.03717 -0.02382 -0.03083 221 LEU A CA  
1304 C C   . LEU A 198 ? 0.44174 0.45129 0.36467 -0.04038 -0.01999 -0.02788 221 LEU A C   
1305 O O   . LEU A 198 ? 0.42078 0.43444 0.34642 -0.04001 -0.01763 -0.02788 221 LEU A O   
1306 C CB  . LEU A 198 ? 0.49204 0.49382 0.40711 -0.03596 -0.02782 -0.03294 221 LEU A CB  
1307 C CG  . LEU A 198 ? 0.57330 0.57574 0.48689 -0.03301 -0.02903 -0.03552 221 LEU A CG  
1308 C CD1 . LEU A 198 ? 0.61721 0.61809 0.52940 -0.02920 -0.03030 -0.03817 221 LEU A CD1 
1309 C CD2 . LEU A 198 ? 0.95773 0.95786 0.86794 -0.03258 -0.03266 -0.03715 221 LEU A CD2 
1310 N N   . CYS A 199 ? 0.35265 0.36197 0.27602 -0.04360 -0.01936 -0.02534 222 CYS A N   
1311 C CA  . CYS A 199 ? 0.44601 0.46008 0.37320 -0.04659 -0.01574 -0.02259 222 CYS A CA  
1312 C C   . CYS A 199 ? 0.46244 0.48048 0.39424 -0.04704 -0.01196 -0.02145 222 CYS A C   
1313 O O   . CYS A 199 ? 0.53326 0.55625 0.46884 -0.04770 -0.00916 -0.02080 222 CYS A O   
1314 C CB  . CYS A 199 ? 0.51679 0.52958 0.44322 -0.04988 -0.01599 -0.01999 222 CYS A CB  
1315 S SG  . CYS A 199 ? 0.57040 0.57913 0.49209 -0.05017 -0.02032 -0.02079 222 CYS A SG  
1316 N N   . TYR A 200 ? 0.36719 0.38326 0.29894 -0.04669 -0.01195 -0.02126 223 TYR A N   
1317 C CA  . TYR A 200 ? 0.42647 0.44614 0.36257 -0.04698 -0.00864 -0.02037 223 TYR A CA  
1318 C C   . TYR A 200 ? 0.46611 0.48814 0.40358 -0.04442 -0.00818 -0.02241 223 TYR A C   
1319 O O   . TYR A 200 ? 0.52257 0.54955 0.46463 -0.04514 -0.00515 -0.02160 223 TYR A O   
1320 C CB  . TYR A 200 ? 0.36688 0.38354 0.30214 -0.04674 -0.00913 -0.02009 223 TYR A CB  
1321 C CG  . TYR A 200 ? 0.44720 0.46395 0.38362 -0.04989 -0.00765 -0.01719 223 TYR A CG  
1322 C CD1 . TYR A 200 ? 0.42145 0.43560 0.35512 -0.05174 -0.00936 -0.01595 223 TYR A CD1 
1323 C CD2 . TYR A 200 ? 0.32753 0.34695 0.26775 -0.05100 -0.00469 -0.01568 223 TYR A CD2 
1324 C CE1 . TYR A 200 ? 0.36502 0.37931 0.29958 -0.05461 -0.00806 -0.01318 223 TYR A CE1 
1325 C CE2 . TYR A 200 ? 0.33924 0.35878 0.28041 -0.05372 -0.00340 -0.01312 223 TYR A CE2 
1326 C CZ  . TYR A 200 ? 0.43489 0.45191 0.37316 -0.05550 -0.00504 -0.01182 223 TYR A CZ  
1327 O OH  . TYR A 200 ? 0.52775 0.54506 0.46691 -0.05821 -0.00375 -0.00914 223 TYR A OH  
1328 N N   . GLY A 201 ? 0.50935 0.52787 0.44290 -0.04139 -0.01134 -0.02510 224 GLY A N   
1329 C CA  . GLY A 201 ? 0.41729 0.43755 0.35150 -0.03878 -0.01121 -0.02705 224 GLY A CA  
1330 C C   . GLY A 201 ? 0.51096 0.53581 0.44762 -0.03935 -0.00957 -0.02685 224 GLY A C   
1331 O O   . GLY A 201 ? 0.49497 0.52422 0.43546 -0.03912 -0.00724 -0.02677 224 GLY A O   
1332 N N   . ILE A 202 ? 0.59242 0.61653 0.52717 -0.04027 -0.01077 -0.02668 225 ILE A N   
1333 C CA  . ILE A 202 ? 0.63198 0.66056 0.56910 -0.04098 -0.00921 -0.02639 225 ILE A CA  
1334 C C   . ILE A 202 ? 0.58815 0.62249 0.53137 -0.04358 -0.00514 -0.02403 225 ILE A C   
1335 O O   . ILE A 202 ? 0.74257 0.78163 0.68942 -0.04339 -0.00324 -0.02417 225 ILE A O   
1336 C CB  . ILE A 202 ? 0.60713 0.63393 0.54133 -0.04199 -0.01107 -0.02622 225 ILE A CB  
1337 C CG1 . ILE A 202 ? 0.60257 0.62433 0.53110 -0.03899 -0.01536 -0.02909 225 ILE A CG1 
1338 C CG2 . ILE A 202 ? 0.66179 0.69409 0.59944 -0.04347 -0.00873 -0.02527 225 ILE A CG2 
1339 C CD1 . ILE A 202 ? 0.43111 0.44934 0.35612 -0.04009 -0.01808 -0.02891 225 ILE A CD1 
1340 N N   . TYR A 203 ? 0.39976 0.43381 0.34423 -0.04606 -0.00392 -0.02186 226 TYR A N   
1341 C CA  . TYR A 203 ? 0.41304 0.45219 0.36324 -0.04841 -0.00034 -0.01975 226 TYR A CA  
1342 C C   . TYR A 203 ? 0.44793 0.48957 0.40144 -0.04709 0.00111  -0.02044 226 TYR A C   
1343 O O   . TYR A 203 ? 0.48350 0.53031 0.44197 -0.04802 0.00350  -0.01976 226 TYR A O   
1344 C CB  . TYR A 203 ? 0.51898 0.55670 0.46933 -0.05092 0.00038  -0.01749 226 TYR A CB  
1345 C CG  . TYR A 203 ? 0.49282 0.53547 0.44890 -0.05341 0.00377  -0.01534 226 TYR A CG  
1346 C CD1 . TYR A 203 ? 0.63392 0.67838 0.59349 -0.05319 0.00544  -0.01517 226 TYR A CD1 
1347 C CD2 . TYR A 203 ? 0.45818 0.50358 0.41618 -0.05595 0.00507  -0.01356 226 TYR A CD2 
1348 C CE1 . TYR A 203 ? 0.67126 0.71995 0.63608 -0.05535 0.00810  -0.01344 226 TYR A CE1 
1349 C CE2 . TYR A 203 ? 0.54752 0.59725 0.51078 -0.05806 0.00778  -0.01184 226 TYR A CE2 
1350 C CZ  . TYR A 203 ? 0.62948 0.67853 0.59558 -0.05548 0.00816  -0.01208 226 TYR A CZ  
1351 O OH  . TYR A 203 ? 0.78344 0.83099 0.75322 -0.05213 0.00807  -0.01104 226 TYR A OH  
1352 N N   . THR A 204 ? 0.53827 0.57634 0.48920 -0.04496 -0.00047 -0.02180 227 THR A N   
1353 C CA  . THR A 204 ? 0.34793 0.38823 0.30173 -0.04364 0.00070  -0.02248 227 THR A CA  
1354 C C   . THR A 204 ? 0.48476 0.52827 0.43972 -0.04203 0.00074  -0.02398 227 THR A C   
1355 O O   . THR A 204 ? 0.46684 0.51525 0.42664 -0.04253 0.00288  -0.02354 227 THR A O   
1356 C CB  . THR A 204 ? 0.34906 0.38462 0.29940 -0.04157 -0.00126 -0.02373 227 THR A CB  
1357 O OG1 . THR A 204 ? 0.45092 0.48346 0.39997 -0.04316 -0.00147 -0.02230 227 THR A OG1 
1358 C CG2 . THR A 204 ? 0.28937 0.32747 0.24302 -0.04062 0.00020  -0.02405 227 THR A CG2 
1359 N N   . PHE A 205 ? 0.60032 0.64099 0.55079 -0.04003 -0.00184 -0.02582 228 PHE A N   
1360 C CA  . PHE A 205 ? 0.52333 0.56660 0.47422 -0.03821 -0.00208 -0.02739 228 PHE A CA  
1361 C C   . PHE A 205 ? 0.52299 0.57214 0.47860 -0.04027 0.00032  -0.02610 228 PHE A C   
1362 O O   . PHE A 205 ? 0.57174 0.62545 0.53098 -0.03985 0.00166  -0.02642 228 PHE A O   
1363 C CB  . PHE A 205 ? 0.42473 0.46338 0.36953 -0.03585 -0.00549 -0.02952 228 PHE A CB  
1364 C CG  . PHE A 205 ? 0.59055 0.62431 0.53116 -0.03298 -0.00800 -0.03146 228 PHE A CG  
1365 C CD1 . PHE A 205 ? 0.60547 0.63968 0.54505 -0.03035 -0.00880 -0.03334 228 PHE A CD1 
1366 C CD2 . PHE A 205 ? 0.93408 0.96288 0.87181 -0.03295 -0.00959 -0.03135 228 PHE A CD2 
1367 C CE1 . PHE A 205 ? 1.00169 1.03117 0.93718 -0.02772 -0.01116 -0.03508 228 PHE A CE1 
1368 C CE2 . PHE A 205 ? 0.89309 0.91732 0.82699 -0.03026 -0.01204 -0.03318 228 PHE A CE2 
1369 C CZ  . PHE A 205 ? 0.96133 0.98571 0.89396 -0.02762 -0.01284 -0.03505 228 PHE A CZ  
1370 N N   . PHE A 206 ? 0.48014 0.52927 0.43575 -0.04254 0.00073  -0.02463 229 PHE A N   
1371 C CA  . PHE A 206 ? 0.58529 0.63965 0.54503 -0.04453 0.00275  -0.02343 229 PHE A CA  
1372 C C   . PHE A 206 ? 0.59149 0.65073 0.55747 -0.04594 0.00550  -0.02217 229 PHE A C   
1373 O O   . PHE A 206 ? 0.64387 0.70794 0.61366 -0.04603 0.00671  -0.02230 229 PHE A O   
1374 C CB  . PHE A 206 ? 0.89420 0.94732 0.85274 -0.04688 0.00272  -0.02184 229 PHE A CB  
1375 C CG  . PHE A 206 ? 0.99305 1.05132 0.95558 -0.04894 0.00463  -0.02059 229 PHE A CG  
1376 C CD1 . PHE A 206 ? 1.09810 1.15821 1.06002 -0.04809 0.00400  -0.02164 229 PHE A CD1 
1377 C CD2 . PHE A 206 ? 0.95643 1.01770 0.92336 -0.05167 0.00694  -0.01843 229 PHE A CD2 
1378 C CE1 . PHE A 206 ? 1.07549 1.14042 1.04119 -0.04998 0.00570  -0.02050 229 PHE A CE1 
1379 C CE2 . PHE A 206 ? 0.98894 1.05488 0.95962 -0.05348 0.00848  -0.01738 229 PHE A CE2 
1380 C CZ  . PHE A 206 ? 1.05702 1.12482 1.02712 -0.05267 0.00789  -0.01839 229 PHE A CZ  
1381 N N   . ASN A 207 ? 0.70217 0.76011 0.66922 -0.04704 0.00633  -0.02098 230 ASN A N   
1382 C CA  . ASN A 207 ? 0.45971 0.52178 0.43253 -0.04855 0.00866  -0.01974 230 ASN A CA  
1383 C C   . ASN A 207 ? 0.31668 0.38047 0.29120 -0.04662 0.00871  -0.02105 230 ASN A C   
1384 O O   . ASN A 207 ? 0.38339 0.45178 0.36284 -0.04740 0.01021  -0.02062 230 ASN A O   
1385 C CB  . ASN A 207 ? 0.49500 0.55495 0.46815 -0.05019 0.00937  -0.01816 230 ASN A CB  
1386 C CG  . ASN A 207 ? 0.63705 0.69611 0.61011 -0.05189 0.00963  -0.01638 230 ASN A CG  
1387 O OD1 . ASN A 207 ? 0.76373 0.82139 0.73924 -0.04961 0.00937  -0.01522 230 ASN A OD1 
1388 N ND2 . ASN A 207 ? 0.62433 0.68011 0.59298 -0.05281 0.00851  -0.01622 230 ASN A ND2 
1389 N N   . ALA A 208 ? 0.45540 0.51548 0.42588 -0.04411 0.00691  -0.02266 231 ALA A N   
1390 C CA  . ALA A 208 ? 0.42947 0.49133 0.40118 -0.04211 0.00679  -0.02401 231 ALA A CA  
1391 C C   . ALA A 208 ? 0.52238 0.58872 0.49620 -0.04168 0.00710  -0.02470 231 ALA A C   
1392 O O   . ALA A 208 ? 0.48670 0.55711 0.46441 -0.04150 0.00808  -0.02484 231 ALA A O   
1393 C CB  . ALA A 208 ? 0.47794 0.53481 0.44429 -0.03931 0.00444  -0.02582 231 ALA A CB  
1394 N N   . ALA A 209 ? 0.62633 0.69192 0.59751 -0.04152 0.00615  -0.02515 232 ALA A N   
1395 C CA  . ALA A 209 ? 0.50629 0.57593 0.47900 -0.04102 0.00629  -0.02586 232 ALA A CA  
1396 C C   . ALA A 209 ? 0.50669 0.58192 0.48565 -0.04346 0.00856  -0.02428 232 ALA A C   
1397 O O   . ALA A 209 ? 0.57018 0.64987 0.55249 -0.04312 0.00918  -0.02468 232 ALA A O   
1398 C CB  . ALA A 209 ? 0.51050 0.57781 0.47897 -0.04061 0.00477  -0.02649 232 ALA A CB  
1399 N N   . LYS A 210 ? 0.60791 0.68281 0.58836 -0.04595 0.00963  -0.02250 233 LYS A N   
1400 C CA  . LYS A 210 ? 0.44622 0.52045 0.43001 -0.04552 0.01014  -0.02068 233 LYS A CA  
1401 C C   . LYS A 210 ? 0.61572 0.68859 0.60162 -0.04339 0.01004  -0.02041 233 LYS A C   
1402 O O   . LYS A 210 ? 0.71939 0.79183 0.70719 -0.04170 0.00979  -0.01981 233 LYS A O   
1403 C CB  . LYS A 210 ? 0.53547 0.60479 0.51805 -0.04583 0.00992  -0.01885 233 LYS A CB  
1404 C CG  . LYS A 210 ? 0.69913 0.76686 0.68179 -0.04564 0.00962  -0.01752 233 LYS A CG  
1405 C CD  . LYS A 210 ? 1.06738 1.13003 1.05021 -0.04464 0.00931  -0.01568 233 LYS A CD  
1406 C CE  . LYS A 210 ? 1.14119 1.20169 1.12568 -0.04302 0.00892  -0.01423 233 LYS A CE  
1407 N NZ  . LYS A 210 ? 1.04790 1.10437 1.03242 -0.04229 0.00863  -0.01276 233 LYS A NZ  
1408 N N   . VAL A 211 ? 0.66820 0.74012 0.65359 -0.04358 0.01020  -0.02076 234 VAL A N   
1409 C CA  . VAL A 211 ? 0.49349 0.56388 0.48063 -0.04174 0.01007  -0.02041 234 VAL A CA  
1410 C C   . VAL A 211 ? 0.45045 0.52527 0.43912 -0.04099 0.01009  -0.02179 234 VAL A C   
1411 O O   . VAL A 211 ? 0.52796 0.60148 0.51835 -0.03930 0.00982  -0.02101 234 VAL A O   
1412 C CB  . VAL A 211 ? 0.39226 0.46135 0.37840 -0.04231 0.01027  -0.02070 234 VAL A CB  
1413 C CG1 . VAL A 211 ? 0.53020 0.59796 0.51808 -0.04051 0.01013  -0.02038 234 VAL A CG1 
1414 C CG2 . VAL A 211 ? 0.41336 0.47795 0.39810 -0.04281 0.01016  -0.01918 234 VAL A CG2 
1415 N N   . TYR A 212 ? 0.45374 0.53408 0.44177 -0.04225 0.01038  -0.02397 235 TYR A N   
1416 C CA  . TYR A 212 ? 0.47745 0.56267 0.46697 -0.04123 0.01028  -0.02554 235 TYR A CA  
1417 C C   . TYR A 212 ? 0.63673 0.72260 0.62751 -0.04041 0.01005  -0.02485 235 TYR A C   
1418 O O   . TYR A 212 ? 0.61022 0.69747 0.60262 -0.03900 0.00983  -0.02499 235 TYR A O   
1419 C CB  . TYR A 212 ? 0.51326 0.59505 0.49714 -0.03844 0.00839  -0.02737 235 TYR A CB  
1420 C CG  . TYR A 212 ? 0.42455 0.50244 0.40542 -0.03659 0.00737  -0.02825 235 TYR A CG  
1421 C CD1 . TYR A 212 ? 0.50556 0.58554 0.48811 -0.03528 0.00740  -0.02896 235 TYR A CD1 
1422 C CD2 . TYR A 212 ? 0.44699 0.51910 0.42326 -0.03614 0.00626  -0.02838 235 TYR A CD2 
1423 C CE1 . TYR A 212 ? 0.51428 0.59075 0.49407 -0.03356 0.00645  -0.02977 235 TYR A CE1 
1424 C CE2 . TYR A 212 ? 0.40672 0.47513 0.38015 -0.03441 0.00518  -0.02923 235 TYR A CE2 
1425 C CZ  . TYR A 212 ? 0.35092 0.42156 0.32615 -0.03311 0.00533  -0.02993 235 TYR A CZ  
1426 O OH  . TYR A 212 ? 0.34867 0.41567 0.32106 -0.03138 0.00426  -0.03077 235 TYR A OH  
1427 N N   . ILE A 213 ? 0.55460 0.63932 0.54447 -0.04125 0.01004  -0.02407 236 ILE A N   
1428 C CA  . ILE A 213 ? 0.72881 0.81354 0.71973 -0.04040 0.00978  -0.02328 236 ILE A CA  
1429 C C   . ILE A 213 ? 0.80638 0.88619 0.79870 -0.03863 0.00943  -0.02134 236 ILE A C   
1430 O O   . ILE A 213 ? 0.82185 0.90258 0.81556 -0.03750 0.00921  -0.02123 236 ILE A O   
1431 C CB  . ILE A 213 ? 0.51810 0.60230 0.50769 -0.04169 0.00982  -0.02275 236 ILE A CB  
1432 C CG1 . ILE A 213 ? 0.58283 0.67325 0.57141 -0.04331 0.01008  -0.02494 236 ILE A CG1 
1433 C CG2 . ILE A 213 ? 0.51815 0.60033 0.50889 -0.04057 0.00949  -0.02129 236 ILE A CG2 
1434 C CD1 . ILE A 213 ? 0.63079 0.71928 0.61666 -0.04475 0.00991  -0.02451 236 ILE A CD1 
1435 N N   . GLU A 214 ? 0.57606 0.65080 0.56799 -0.03839 0.00936  -0.01987 237 GLU A N   
1436 C CA  . GLU A 214 ? 0.58541 0.65590 0.57870 -0.03671 0.00902  -0.01830 237 GLU A CA  
1437 C C   . GLU A 214 ? 0.64667 0.71835 0.64097 -0.03586 0.00898  -0.01890 237 GLU A C   
1438 O O   . GLU A 214 ? 0.84963 0.92029 0.84520 -0.03468 0.00870  -0.01823 237 GLU A O   
1439 C CB  . GLU A 214 ? 0.79847 0.86414 0.79125 -0.03650 0.00892  -0.01694 237 GLU A CB  
1440 C CG  . GLU A 214 ? 0.96222 1.02648 0.95418 -0.03712 0.00886  -0.01615 237 GLU A CG  
1441 C CD  . GLU A 214 ? 1.13445 1.19410 1.12631 -0.03651 0.00866  -0.01473 237 GLU A CD  
1442 O OE1 . GLU A 214 ? 0.81973 0.87709 0.81233 -0.03547 0.00855  -0.01426 237 GLU A OE1 
1443 O OE2 . GLU A 214 ? 1.33444 1.39298 1.32553 -0.03706 0.00860  -0.01411 237 GLU A OE2 
1444 N N   . ALA A 215 ? 0.70302 0.77690 0.69672 -0.03649 0.00926  -0.02018 238 ALA A N   
1445 C CA  . ALA A 215 ? 0.64659 0.72150 0.64125 -0.03565 0.00920  -0.02071 238 ALA A CA  
1446 C C   . ALA A 215 ? 0.52097 0.59995 0.51674 -0.03509 0.00906  -0.02157 238 ALA A C   
1447 O O   . ALA A 215 ? 0.47486 0.55303 0.47172 -0.03402 0.00882  -0.02107 238 ALA A O   
1448 C CB  . ALA A 215 ? 0.49273 0.56995 0.48657 -0.03648 0.00952  -0.02218 238 ALA A CB  
1449 N N   . TYR A 216 ? 0.68693 0.77049 0.68237 -0.03585 0.00919  -0.02291 239 TYR A N   
1450 C CA  . TYR A 216 ? 0.80746 0.89568 0.80394 -0.03526 0.00904  -0.02395 239 TYR A CA  
1451 C C   . TYR A 216 ? 0.71857 0.80382 0.71599 -0.03431 0.00871  -0.02230 239 TYR A C   
1452 O O   . TYR A 216 ? 0.76790 0.85438 0.76637 -0.03340 0.00849  -0.02237 239 TYR A O   
1453 C CB  . TYR A 216 ? 0.68630 0.77974 0.68220 -0.03620 0.00920  -0.02559 239 TYR A CB  
1454 C CG  . TYR A 216 ? 0.57319 0.67210 0.57020 -0.03542 0.00899  -0.02683 239 TYR A CG  
1455 C CD1 . TYR A 216 ? 0.57174 0.67646 0.56946 -0.03476 0.00892  -0.02895 239 TYR A CD1 
1456 C CD2 . TYR A 216 ? 0.60192 0.70047 0.59933 -0.03519 0.00881  -0.02596 239 TYR A CD2 
1457 C CE1 . TYR A 216 ? 0.89703 1.00703 0.89582 -0.03376 0.00864  -0.03010 239 TYR A CE1 
1458 C CE2 . TYR A 216 ? 0.75533 0.85892 0.75369 -0.03444 0.00861  -0.02703 239 TYR A CE2 
1459 C CZ  . TYR A 216 ? 0.95651 1.06583 0.95555 -0.03368 0.00851  -0.02908 239 TYR A CZ  
1460 O OH  . TYR A 216 ? 0.66690 0.78149 0.66692 -0.03267 0.00822  -0.03016 239 TYR A OH  
1461 N N   . HIS A 217 ? 0.62302 0.70444 0.62007 -0.03449 0.00864  -0.02085 240 HIS A N   
1462 C CA  . HIS A 217 ? 0.64284 0.72152 0.64077 -0.03363 0.00831  -0.01941 240 HIS A CA  
1463 C C   . HIS A 217 ? 0.62412 0.69798 0.62263 -0.03266 0.00808  -0.01801 240 HIS A C   
1464 O O   . HIS A 217 ? 0.58032 0.65189 0.57958 -0.03192 0.00778  -0.01691 240 HIS A O   
1465 C CB  . HIS A 217 ? 0.67851 0.75549 0.67593 -0.03409 0.00828  -0.01859 240 HIS A CB  
1466 C CG  . HIS A 217 ? 0.66443 0.74607 0.66132 -0.03504 0.00846  -0.01981 240 HIS A CG  
1467 N ND1 . HIS A 217 ? 0.79765 0.88494 0.79478 -0.03518 0.00856  -0.02158 240 HIS A ND1 
1468 C CD2 . HIS A 217 ? 0.71367 0.79544 0.70985 -0.03582 0.00852  -0.01960 240 HIS A CD2 
1469 C CE1 . HIS A 217 ? 0.91142 1.00220 0.90800 -0.03601 0.00868  -0.02246 240 HIS A CE1 
1470 N NE2 . HIS A 217 ? 1.06606 1.15345 1.06198 -0.03652 0.00868  -0.02122 240 HIS A NE2 
1471 N N   . THR A 218 ? 0.66368 0.73609 0.66184 -0.03268 0.00820  -0.01808 241 THR A N   
1472 C CA  . THR A 218 ? 0.70073 0.76894 0.69941 -0.03177 0.00798  -0.01690 241 THR A CA  
1473 C C   . THR A 218 ? 0.74621 0.81610 0.74563 -0.03124 0.00790  -0.01740 241 THR A C   
1474 O O   . THR A 218 ? 0.74467 0.80630 0.73013 -0.02812 0.00721  -0.01859 241 THR A O   
1475 C CB  . THR A 218 ? 0.58745 0.65292 0.58534 -0.03202 0.00813  -0.01657 241 THR A CB  
1476 O OG1 . THR A 218 ? 0.58415 0.64762 0.58144 -0.03237 0.00814  -0.01587 241 THR A OG1 
1477 C CG2 . THR A 218 ? 0.73568 0.79776 0.73392 -0.03165 0.00681  -0.01623 241 THR A CG2 
1478 N N   . VAL A 219 ? 0.91784 0.62584 0.71261 -0.15383 0.10832  0.01960  242 VAL A N   
1479 C CA  . VAL A 219 ? 0.90007 0.61135 0.69778 -0.15798 0.11010  0.01907  242 VAL A CA  
1480 C C   . VAL A 219 ? 0.89095 0.59884 0.68925 -0.16251 0.11112  0.02509  242 VAL A C   
1481 O O   . VAL A 219 ? 0.98451 0.68946 0.78045 -0.16221 0.11072  0.02917  242 VAL A O   
1482 C CB  . VAL A 219 ? 0.91508 0.63477 0.71233 -0.15746 0.11116  0.01482  242 VAL A CB  
1483 C CG1 . VAL A 219 ? 0.65644 0.37968 0.45361 -0.15300 0.11007  0.00928  242 VAL A CG1 
1484 C CG2 . VAL A 219 ? 0.81289 0.53459 0.60722 -0.15743 0.11156  0.01699  242 VAL A CG2 
1485 N N   . PRO A 220 ? 0.86642 0.57461 0.66803 -0.16678 0.11240  0.02609  243 PRO A N   
1486 C CA  . PRO A 220 ? 0.95572 0.66144 0.75832 -0.17136 0.11348  0.03216  243 PRO A CA  
1487 C C   . PRO A 220 ? 0.93699 0.64655 0.73694 -0.17223 0.11456  0.03463  243 PRO A C   
1488 O O   . PRO A 220 ? 1.01444 0.72985 0.81240 -0.17011 0.11485  0.03095  243 PRO A O   
1489 C CB  . PRO A 220 ? 1.11421 0.82220 0.92068 -0.17527 0.11487  0.03107  243 PRO A CB  
1490 C CG  . PRO A 220 ? 0.87577 0.58455 0.68372 -0.17274 0.11408  0.02556  243 PRO A CG  
1491 C CD  . PRO A 220 ? 0.99635 0.70722 0.80111 -0.16751 0.11288  0.02186  243 PRO A CD  
1492 N N   . LYS A 221 ? 1.02831 0.73474 0.82858 -0.17547 0.11513  0.04112  244 LYS A N   
1493 C CA  . LYS A 221 ? 1.02846 0.73733 0.82597 -0.17590 0.11588  0.04471  244 LYS A CA  
1494 C C   . LYS A 221 ? 1.01815 0.73539 0.81563 -0.17800 0.11784  0.04302  244 LYS A C   
1495 O O   . LYS A 221 ? 1.12292 0.84388 0.91781 -0.17719 0.11830  0.04401  244 LYS A O   
1496 C CB  . LYS A 221 ? 0.60299 0.30667 0.40144 -0.17907 0.11608  0.05255  244 LYS A CB  
1497 N N   . GLY A 222 ? 0.89571 0.61614 0.69609 -0.18062 0.11896  0.04048  245 GLY A N   
1498 C CA  . GLY A 222 ? 1.02981 0.75785 0.83052 -0.18329 0.12091  0.03975  245 GLY A CA  
1499 C C   . GLY A 222 ? 1.06034 0.79520 0.86012 -0.18068 0.12097  0.03293  245 GLY A C   
1500 O O   . GLY A 222 ? 0.96797 0.70448 0.76502 -0.17707 0.12010  0.03105  245 GLY A O   
1501 N N   . ARG A 223 ? 1.20894 0.94782 1.01125 -0.18261 0.12199  0.02935  246 ARG A N   
1502 C CA  . ARG A 223 ? 1.10164 0.84743 0.90382 -0.18068 0.12216  0.02295  246 ARG A CA  
1503 C C   . ARG A 223 ? 1.08391 0.82847 0.88481 -0.17532 0.12024  0.01825  246 ARG A C   
1504 O O   . ARG A 223 ? 0.95490 0.70422 0.75450 -0.17254 0.11983  0.01453  246 ARG A O   
1505 C CB  . ARG A 223 ? 1.05615 0.80502 0.86161 -0.18376 0.12343  0.02045  246 ARG A CB  
1506 C CG  . ARG A 223 ? 1.14551 0.90231 0.95166 -0.18626 0.12513  0.01884  246 ARG A CG  
1507 C CD  . ARG A 223 ? 1.25937 1.01796 1.06870 -0.18846 0.12597  0.01575  246 ARG A CD  
1508 N NE  . ARG A 223 ? 1.54565 1.29952 1.35693 -0.19246 0.12669  0.02091  246 ARG A NE  
1509 C CZ  . ARG A 223 ? 1.61645 1.37015 1.43081 -0.19523 0.12747  0.02009  246 ARG A CZ  
1510 N NH1 . ARG A 223 ? 1.37887 1.13690 1.19460 -0.19447 0.12774  0.01426  246 ARG A NH1 
1511 N NH2 . ARG A 223 ? 1.44488 1.19397 1.26117 -0.19883 0.12795  0.02538  246 ARG A NH2 
1512 N N   . CYS A 224 ? 1.16552 0.90398 0.96706 -0.17387 0.11902  0.01843  247 CYS A N   
1513 C CA  . CYS A 224 ? 0.93056 0.66819 0.73116 -0.16889 0.11727  0.01418  247 CYS A CA  
1514 C C   . CYS A 224 ? 0.90304 0.64083 0.70023 -0.16533 0.11617  0.01456  247 CYS A C   
1515 O O   . CYS A 224 ? 1.02205 0.76309 0.81842 -0.16150 0.11520  0.01011  247 CYS A O   
1516 C CB  . CYS A 224 ? 1.06617 0.79685 0.86799 -0.16828 0.11616  0.01542  247 CYS A CB  
1517 S SG  . CYS A 224 ? 1.05652 0.78766 0.86270 -0.17124 0.11708  0.01328  247 CYS A SG  
1518 N N   . ARG A 225 ? 0.96352 0.69794 0.75888 -0.16656 0.11627  0.02006  248 ARG A N   
1519 C CA  . ARG A 225 ? 0.93185 0.66637 0.72394 -0.16346 0.11534  0.02090  248 ARG A CA  
1520 C C   . ARG A 225 ? 1.01286 0.75499 0.80435 -0.16359 0.11622  0.01884  248 ARG A C   
1521 O O   . ARG A 225 ? 1.03202 0.77575 0.82139 -0.16015 0.11522  0.01734  248 ARG A O   
1522 C CB  . ARG A 225 ? 1.03067 0.75945 0.82122 -0.16491 0.11528  0.02775  248 ARG A CB  
1523 C CG  . ARG A 225 ? 0.83064 0.55199 0.61998 -0.16191 0.11337  0.02905  248 ARG A CG  
1524 C CD  . ARG A 225 ? 0.92575 0.64239 0.71317 -0.16280 0.11322  0.03567  248 ARG A CD  
1525 N NE  . ARG A 225 ? 0.98149 0.69101 0.76773 -0.15991 0.11131  0.03697  248 ARG A NE  
1526 C CZ  . ARG A 225 ? 0.86286 0.56632 0.65115 -0.16104 0.11068  0.03884  248 ARG A CZ  
1527 N NH1 . ARG A 225 ? 0.88668 0.59007 0.67841 -0.16489 0.11173  0.03948  248 ARG A NH1 
1528 N NH2 . ARG A 225 ? 0.89589 0.59322 0.68292 -0.15822 0.10886  0.04003  248 ARG A NH2 
1529 N N   . GLN A 226 ? 1.21092 0.95784 1.00440 -0.16747 0.11802  0.01870  249 GLN A N   
1530 C CA  . GLN A 226 ? 1.07084 0.82552 0.86431 -0.16762 0.11879  0.01607  249 GLN A CA  
1531 C C   . GLN A 226 ? 0.99685 0.75543 0.79125 -0.16411 0.11776  0.00919  249 GLN A C   
1532 O O   . GLN A 226 ? 0.95170 0.71408 0.74509 -0.16141 0.11704  0.00678  249 GLN A O   
1533 C CB  . GLN A 226 ? 1.07930 0.83829 0.87482 -0.17272 0.12097  0.01759  249 GLN A CB  
1534 C CG  . GLN A 226 ? 1.07515 0.83320 0.86970 -0.17614 0.12225  0.02456  249 GLN A CG  
1535 C CD  . GLN A 226 ? 1.34462 1.10484 1.14170 -0.18142 0.12426  0.02685  249 GLN A CD  
1536 O OE1 . GLN A 226 ? 1.56943 1.32458 1.36783 -0.18369 0.12449  0.03007  249 GLN A OE1 
1537 N NE2 . GLN A 226 ? 1.19762 0.96554 0.99560 -0.18342 0.12568  0.02518  249 GLN A NE2 
1538 N N   . VAL A 227 ? 0.96928 0.72715 0.76584 -0.16412 0.11766  0.00617  250 VAL A N   
1539 C CA  . VAL A 227 ? 0.79358 0.55579 0.59151 -0.16107 0.11687  -0.00006 250 VAL A CA  
1540 C C   . VAL A 227 ? 0.70316 0.46356 0.49917 -0.15588 0.11482  -0.00156 250 VAL A C   
1541 O O   . VAL A 227 ? 0.83780 0.60298 0.63395 -0.15306 0.11404  -0.00532 250 VAL A O   
1542 C CB  . VAL A 227 ? 0.85519 0.61663 0.65579 -0.16216 0.11725  -0.00224 250 VAL A CB  
1543 C CG1 . VAL A 227 ? 0.91736 0.68324 0.71939 -0.15866 0.11636  -0.00818 250 VAL A CG1 
1544 C CG2 . VAL A 227 ? 0.61610 0.38009 0.41875 -0.16720 0.11926  -0.00123 250 VAL A CG2 
1545 N N   . VAL A 228 ? 0.74324 0.49677 0.53767 -0.15456 0.11386  0.00141  251 VAL A N   
1546 C CA  . VAL A 228 ? 0.72220 0.47361 0.51466 -0.14968 0.11190  0.00036  251 VAL A CA  
1547 C C   . VAL A 228 ? 0.83056 0.58451 0.62091 -0.14812 0.11148  0.00090  251 VAL A C   
1548 O O   . VAL A 228 ? 0.92073 0.67732 0.71067 -0.14422 0.11014  -0.00231 251 VAL A O   
1549 C CB  . VAL A 228 ? 0.65010 0.39343 0.44119 -0.14917 0.11108  0.00413  251 VAL A CB  
1550 C CG1 . VAL A 228 ? 0.77200 0.51305 0.56050 -0.14443 0.10916  0.00388  251 VAL A CG1 
1551 C CG2 . VAL A 228 ? 0.75792 0.49926 0.55148 -0.14989 0.11114  0.00274  251 VAL A CG2 
1552 N N   . THR A 229 ? 0.99565 0.74907 0.78485 -0.15115 0.11261  0.00519  252 THR A N   
1553 C CA  . THR A 229 ? 0.85649 0.61288 0.64395 -0.15009 0.11244  0.00602  252 THR A CA  
1554 C C   . THR A 229 ? 0.75534 0.51965 0.54476 -0.14945 0.11256  0.00108  252 THR A C   
1555 O O   . THR A 229 ? 0.65960 0.42644 0.44832 -0.14624 0.11138  -0.00089 252 THR A O   
1556 C CB  . THR A 229 ? 0.78223 0.53776 0.56862 -0.15399 0.11398  0.01180  252 THR A CB  
1557 O OG1 . THR A 229 ? 1.01991 0.76801 0.80429 -0.15379 0.11346  0.01658  252 THR A OG1 
1558 C CG2 . THR A 229 ? 0.85447 0.61475 0.63965 -0.15333 0.11412  0.01230  252 THR A CG2 
1559 N N   . GLY A 230 ? 0.79191 0.56021 0.58399 -0.15253 0.11393  -0.00088 253 GLY A N   
1560 C CA  . GLY A 230 ? 0.66100 0.43680 0.45533 -0.15201 0.11398  -0.00576 253 GLY A CA  
1561 C C   . GLY A 230 ? 0.79803 0.57510 0.59319 -0.14731 0.11213  -0.01048 253 GLY A C   
1562 O O   . GLY A 230 ? 0.79122 0.57325 0.58725 -0.14514 0.11131  -0.01354 253 GLY A O   
1563 N N   . MET A 231 ? 0.70031 0.47328 0.49550 -0.14572 0.11145  -0.01097 254 MET A N   
1564 C CA  . MET A 231 ? 0.56508 0.33993 0.36139 -0.14143 0.10987  -0.01512 254 MET A CA  
1565 C C   . MET A 231 ? 0.55892 0.33259 0.35313 -0.13729 0.10806  -0.01482 254 MET A C   
1566 O O   . MET A 231 ? 0.62853 0.40651 0.42401 -0.13404 0.10682  -0.01834 254 MET A O   
1567 C CB  . MET A 231 ? 0.65333 0.42402 0.45007 -0.14094 0.10967  -0.01498 254 MET A CB  
1568 C CG  . MET A 231 ? 0.62728 0.39942 0.42654 -0.14430 0.11119  -0.01602 254 MET A CG  
1569 S SD  . MET A 231 ? 0.67921 0.44666 0.47903 -0.14261 0.11046  -0.01605 254 MET A SD  
1570 C CE  . MET A 231 ? 0.56300 0.33495 0.36652 -0.14549 0.11200  -0.01905 254 MET A CE  
1571 N N   . ALA A 232 ? 0.64141 0.40946 0.43258 -0.13741 0.10788  -0.01047 255 ALA A N   
1572 C CA  . ALA A 232 ? 0.55552 0.32206 0.34444 -0.13358 0.10622  -0.00987 255 ALA A CA  
1573 C C   . ALA A 232 ? 0.62367 0.39607 0.41336 -0.13310 0.10606  -0.01156 255 ALA A C   
1574 O O   . ALA A 232 ? 0.68888 0.46376 0.47898 -0.12931 0.10445  -0.01415 255 ALA A O   
1575 C CB  . ALA A 232 ? 0.63628 0.39587 0.42188 -0.13430 0.10629  -0.00455 255 ALA A CB  
1576 N N   . TRP A 233 ? 0.74392 0.51888 0.53408 -0.13700 0.10770  -0.01000 256 TRP A N   
1577 C CA  . TRP A 233 ? 0.71400 0.49498 0.50528 -0.13695 0.10767  -0.01153 256 TRP A CA  
1578 C C   . TRP A 233 ? 0.77275 0.55976 0.56745 -0.13511 0.10687  -0.01714 256 TRP A C   
1579 O O   . TRP A 233 ? 0.87124 0.66124 0.66672 -0.13187 0.10536  -0.01941 256 TRP A O   
1580 C CB  . TRP A 233 ? 0.87174 0.65522 0.66336 -0.14189 0.10982  -0.00894 256 TRP A CB  
1581 C CG  . TRP A 233 ? 0.85103 0.63130 0.63965 -0.14317 0.11047  -0.00331 256 TRP A CG  
1582 C CD1 . TRP A 233 ? 1.05613 0.83156 0.84301 -0.14602 0.11169  0.00157  256 TRP A CD1 
1583 C CD2 . TRP A 233 ? 1.00465 0.78656 0.79184 -0.14164 0.10994  -0.00170 256 TRP A CD2 
1584 N NE1 . TRP A 233 ? 1.28647 1.06063 1.07085 -0.14632 0.11200  0.00624  256 TRP A NE1 
1585 C CE2 . TRP A 233 ? 1.23427 1.01241 1.01868 -0.14363 0.11100  0.00430  256 TRP A CE2 
1586 C CE3 . TRP A 233 ? 1.12638 0.91273 0.91460 -0.13878 0.10866  -0.00459 256 TRP A CE3 
1587 C CZ2 . TRP A 233 ? 1.34666 1.12561 1.12905 -0.14275 0.11093  0.00748  256 TRP A CZ2 
1588 C CZ3 . TRP A 233 ? 0.98552 0.77241 0.77187 -0.13797 0.10854  -0.00157 256 TRP A CZ3 
1589 C CH2 . TRP A 233 ? 1.15228 0.93562 0.93562 -0.13990 0.10973  0.00440  256 TRP A CH2 
1590 N N   . LEU A 234 ? 0.65227 0.44133 0.44926 -0.13720 0.10788  -0.01926 257 LEU A N   
1591 C CA  . LEU A 234 ? 0.54103 0.33589 0.34144 -0.13553 0.10725  -0.02433 257 LEU A CA  
1592 C C   . LEU A 234 ? 0.69417 0.48851 0.49464 -0.13039 0.10511  -0.02621 257 LEU A C   
1593 O O   . LEU A 234 ? 0.83217 0.63161 0.63482 -0.12783 0.10391  -0.02932 257 LEU A O   
1594 C CB  . LEU A 234 ? 0.62861 0.42413 0.43085 -0.13810 0.10859  -0.02563 257 LEU A CB  
1595 C CG  . LEU A 234 ? 0.70595 0.50699 0.51062 -0.14193 0.11020  -0.02727 257 LEU A CG  
1596 C CD1 . LEU A 234 ? 0.78839 0.58943 0.59473 -0.14392 0.11135  -0.02856 257 LEU A CD1 
1597 C CD2 . LEU A 234 ? 0.64978 0.45794 0.45718 -0.14006 0.10926  -0.03129 257 LEU A CD2 
1598 N N   . PHE A 235 ? 0.66705 0.45549 0.46537 -0.12891 0.10460  -0.02422 258 PHE A N   
1599 C CA  . PHE A 235 ? 0.54852 0.33678 0.34708 -0.12428 0.10274  -0.02585 258 PHE A CA  
1600 C C   . PHE A 235 ? 0.77945 0.56860 0.57710 -0.12086 0.10102  -0.02593 258 PHE A C   
1601 O O   . PHE A 235 ? 0.71792 0.51196 0.51793 -0.11782 0.09967  -0.02892 258 PHE A O   
1602 C CB  . PHE A 235 ? 0.47743 0.25893 0.27372 -0.12380 0.10263  -0.02329 258 PHE A CB  
1603 C CG  . PHE A 235 ? 0.64632 0.42776 0.44280 -0.11925 0.10080  -0.02459 258 PHE A CG  
1604 C CD1 . PHE A 235 ? 0.71257 0.49723 0.51185 -0.11828 0.10070  -0.02711 258 PHE A CD1 
1605 C CD2 . PHE A 235 ? 0.64613 0.42461 0.44011 -0.11598 0.09921  -0.02312 258 PHE A CD2 
1606 C CE1 . PHE A 235 ? 0.64744 0.43273 0.44717 -0.11424 0.09905  -0.02794 258 PHE A CE1 
1607 C CE2 . PHE A 235 ? 0.62822 0.40711 0.42249 -0.11189 0.09752  -0.02416 258 PHE A CE2 
1608 C CZ  . PHE A 235 ? 0.69489 0.47734 0.49210 -0.11107 0.09745  -0.02646 258 PHE A CZ  
1609 N N   . PHE A 236 ? 0.83667 0.62133 0.63111 -0.12135 0.10105  -0.02245 259 PHE A N   
1610 C CA  . PHE A 236 ? 0.69614 0.48074 0.48937 -0.11796 0.09937  -0.02214 259 PHE A CA  
1611 C C   . PHE A 236 ? 0.70521 0.49638 0.50109 -0.11807 0.09914  -0.02452 259 PHE A C   
1612 O O   . PHE A 236 ? 0.65496 0.44855 0.45175 -0.11456 0.09739  -0.02609 259 PHE A O   
1613 C CB  . PHE A 236 ? 0.61198 0.39020 0.40117 -0.11867 0.09964  -0.01753 259 PHE A CB  
1614 C CG  . PHE A 236 ? 0.54230 0.31395 0.32892 -0.11727 0.09916  -0.01543 259 PHE A CG  
1615 C CD1 . PHE A 236 ? 0.61172 0.37792 0.39627 -0.12034 0.10050  -0.01169 259 PHE A CD1 
1616 C CD2 . PHE A 236 ? 0.76454 0.53582 0.55113 -0.11295 0.09731  -0.01707 259 PHE A CD2 
1617 C CE1 . PHE A 236 ? 0.70821 0.46839 0.49076 -0.11910 0.09994  -0.00981 259 PHE A CE1 
1618 C CE2 . PHE A 236 ? 0.59739 0.36298 0.38181 -0.11171 0.09683  -0.01522 259 PHE A CE2 
1619 C CZ  . PHE A 236 ? 0.59868 0.35858 0.38112 -0.11478 0.09811  -0.01170 259 PHE A CZ  
1620 N N   . VAL A 237 ? 0.83641 0.63081 0.63381 -0.12207 0.10083  -0.02483 260 VAL A N   
1621 C CA  . VAL A 237 ? 0.78746 0.58843 0.58768 -0.12252 0.10068  -0.02712 260 VAL A CA  
1622 C C   . VAL A 237 ? 0.63033 0.43714 0.43455 -0.12039 0.09969  -0.03172 260 VAL A C   
1623 O O   . VAL A 237 ? 0.81119 0.62203 0.61751 -0.11765 0.09815  -0.03378 260 VAL A O   
1624 C CB  . VAL A 237 ? 0.68950 0.49259 0.49013 -0.12758 0.10286  -0.02585 260 VAL A CB  
1625 C CG1 . VAL A 237 ? 0.56358 0.37453 0.36803 -0.12827 0.10277  -0.02917 260 VAL A CG1 
1626 C CG2 . VAL A 237 ? 0.61234 0.41140 0.40949 -0.12919 0.10365  -0.02091 260 VAL A CG2 
1627 N N   . SER A 238 ? 0.72495 0.53244 0.53048 -0.12152 0.10055  -0.03316 261 SER A N   
1628 C CA  . SER A 238 ? 0.74801 0.56172 0.55760 -0.11977 0.09988  -0.03718 261 SER A CA  
1629 C C   . SER A 238 ? 0.70111 0.51487 0.51108 -0.11476 0.09779  -0.03786 261 SER A C   
1630 O O   . SER A 238 ? 0.75224 0.57152 0.56531 -0.11214 0.09645  -0.04026 261 SER A O   
1631 C CB  . SER A 238 ? 0.63431 0.44868 0.44512 -0.12236 0.10147  -0.03819 261 SER A CB  
1632 O OG  . SER A 238 ? 0.79296 0.60165 0.60146 -0.12174 0.10157  -0.03618 261 SER A OG  
1633 N N   . TRP A 239 ? 0.64920 0.45709 0.45620 -0.11338 0.09744  -0.03556 262 TRP A N   
1634 C CA  . TRP A 239 ? 0.76410 0.57225 0.57136 -0.10869 0.09544  -0.03590 262 TRP A CA  
1635 C C   . TRP A 239 ? 0.75066 0.55898 0.55718 -0.10606 0.09380  -0.03540 262 TRP A C   
1636 O O   . TRP A 239 ? 0.76420 0.57623 0.57282 -0.10233 0.09202  -0.03678 262 TRP A O   
1637 C CB  . TRP A 239 ? 0.56983 0.37168 0.37409 -0.10799 0.09544  -0.03355 262 TRP A CB  
1638 C CG  . TRP A 239 ? 0.59220 0.39481 0.39806 -0.10929 0.09647  -0.03444 262 TRP A CG  
1639 C CD1 . TRP A 239 ? 0.62847 0.43225 0.43560 -0.11314 0.09836  -0.03523 262 TRP A CD1 
1640 C CD2 . TRP A 239 ? 0.60810 0.41048 0.41461 -0.10679 0.09565  -0.03452 262 TRP A CD2 
1641 N NE1 . TRP A 239 ? 0.55301 0.35711 0.36155 -0.11311 0.09877  -0.03588 262 TRP A NE1 
1642 C CE2 . TRP A 239 ? 0.75163 0.55498 0.55989 -0.10930 0.09714  -0.03541 262 TRP A CE2 
1643 C CE3 . TRP A 239 ? 0.65986 0.46155 0.46575 -0.10273 0.09378  -0.03386 262 TRP A CE3 
1644 C CZ2 . TRP A 239 ? 0.78305 0.58672 0.59260 -0.10790 0.09684  -0.03563 262 TRP A CZ2 
1645 C CZ3 . TRP A 239 ? 0.59249 0.39470 0.39966 -0.10142 0.09347  -0.03401 262 TRP A CZ3 
1646 C CH2 . TRP A 239 ? 0.63196 0.43516 0.44101 -0.10401 0.09499  -0.03488 262 TRP A CH2 
1647 N N   . GLY A 240 ? 0.85648 0.66102 0.66021 -0.10796 0.09438  -0.03314 263 GLY A N   
1648 C CA  . GLY A 240 ? 0.77275 0.57720 0.57574 -0.10569 0.09295  -0.03247 263 GLY A CA  
1649 C C   . GLY A 240 ? 0.78636 0.59806 0.59350 -0.10520 0.09226  -0.03534 263 GLY A C   
1650 O O   . GLY A 240 ? 0.74772 0.56082 0.55554 -0.10221 0.09053  -0.03562 263 GLY A O   
1651 N N   . MET A 241 ? 0.69942 0.51587 0.50954 -0.10803 0.09352  -0.03751 264 MET A N   
1652 C CA  . MET A 241 ? 0.58830 0.41201 0.40273 -0.10783 0.09295  -0.04038 264 MET A CA  
1653 C C   . MET A 241 ? 0.65845 0.48718 0.47644 -0.10369 0.09118  -0.04267 264 MET A C   
1654 O O   . MET A 241 ? 0.75992 0.59652 0.58495 -0.10151 0.08907  -0.04296 264 MET A O   
1655 C CB  . MET A 241 ? 0.74181 0.56926 0.55837 -0.11205 0.09486  -0.04208 264 MET A CB  
1656 C CG  . MET A 241 ? 0.79354 0.61984 0.60856 -0.11624 0.09640  -0.04031 264 MET A CG  
1657 S SD  . MET A 241 ? 1.03507 0.86537 0.85194 -0.11600 0.09544  -0.04057 264 MET A SD  
1658 C CE  . MET A 241 ? 1.17493 0.99740 0.98657 -0.11458 0.09497  -0.03586 264 MET A CE  
1659 N N   . PHE A 242 ? 0.79802 0.62553 0.61588 -0.10171 0.09076  -0.04207 265 PHE A N   
1660 C CA  . PHE A 242 ? 0.63572 0.47256 0.46340 -0.09699 0.08752  -0.04126 265 PHE A CA  
1661 C C   . PHE A 242 ? 0.69013 0.53065 0.52233 -0.09213 0.08403  -0.03921 265 PHE A C   
1662 O O   . PHE A 242 ? 0.69774 0.54751 0.53864 -0.08948 0.08159  -0.03916 265 PHE A O   
1663 C CB  . PHE A 242 ? 0.65539 0.49007 0.48188 -0.09644 0.08798  -0.04090 265 PHE A CB  
1664 C CG  . PHE A 242 ? 0.76204 0.59762 0.58850 -0.09993 0.09039  -0.04299 265 PHE A CG  
1665 C CD1 . PHE A 242 ? 0.86435 0.69203 0.68344 -0.10440 0.09357  -0.04345 265 PHE A CD1 
1666 C CD2 . PHE A 242 ? 0.83619 0.68125 0.67143 -0.09842 0.08900  -0.04378 265 PHE A CD2 
1667 C CE1 . PHE A 242 ? 0.78322 0.61264 0.60385 -0.10731 0.09529  -0.04475 265 PHE A CE1 
1668 C CE2 . PHE A 242 ? 0.73936 0.58530 0.57465 -0.10152 0.09120  -0.04575 265 PHE A CE2 
1669 C CZ  . PHE A 242 ? 0.61044 0.44776 0.43693 -0.10629 0.09485  -0.04693 265 PHE A CZ  
1670 N N   . PRO A 243 ? 0.72168 0.55560 0.54857 -0.09066 0.08359  -0.03749 266 PRO A N   
1671 C CA  . PRO A 243 ? 0.69403 0.53195 0.52556 -0.08611 0.08024  -0.03567 266 PRO A CA  
1672 C C   . PRO A 243 ? 0.76482 0.60682 0.59947 -0.08658 0.07971  -0.03630 266 PRO A C   
1673 O O   . PRO A 243 ? 0.71619 0.56536 0.55810 -0.08281 0.07668  -0.03532 266 PRO A O   
1674 C CB  . PRO A 243 ? 0.76780 0.59610 0.59109 -0.08561 0.08073  -0.03414 266 PRO A CB  
1675 C CG  . PRO A 243 ? 0.74744 0.56610 0.56105 -0.09049 0.08466  -0.03530 266 PRO A CG  
1676 C CD  . PRO A 243 ? 0.69962 0.52228 0.51621 -0.09291 0.08605  -0.03712 266 PRO A CD  
1677 N N   . ILE A 244 ? 0.79276 0.63050 0.62208 -0.09135 0.08266  -0.03797 267 ILE A N   
1678 C CA  . ILE A 244 ? 0.72588 0.56758 0.55798 -0.09234 0.08241  -0.03880 267 ILE A CA  
1679 C C   . ILE A 244 ? 0.65905 0.51197 0.50119 -0.09117 0.08088  -0.03995 267 ILE A C   
1680 O O   . ILE A 244 ? 0.77939 0.63917 0.62814 -0.08863 0.07857  -0.03960 267 ILE A O   
1681 C CB  . ILE A 244 ? 0.50369 0.33761 0.32677 -0.09829 0.08618  -0.04034 267 ILE A CB  
1682 C CG1 . ILE A 244 ? 0.45020 0.27344 0.26435 -0.09879 0.08729  -0.03829 267 ILE A CG1 
1683 C CG2 . ILE A 244 ? 0.60877 0.44680 0.43449 -0.09959 0.08599  -0.04124 267 ILE A CG2 
1684 C CD1 . ILE A 244 ? 0.73841 0.55786 0.54953 -0.10323 0.08952  -0.03601 267 ILE A CD1 
1685 N N   . LEU A 245 ? 0.56718 0.42204 0.41057 -0.09294 0.08218  -0.04132 268 LEU A N   
1686 C CA  . LEU A 245 ? 0.60733 0.47247 0.45990 -0.09181 0.08086  -0.04245 268 LEU A CA  
1687 C C   . LEU A 245 ? 0.67393 0.54596 0.53445 -0.08619 0.07719  -0.04060 268 LEU A C   
1688 O O   . LEU A 245 ? 0.72534 0.60595 0.59379 -0.08424 0.07537  -0.04090 268 LEU A O   
1689 C CB  . LEU A 245 ? 0.70947 0.57486 0.56146 -0.09475 0.08305  -0.04425 268 LEU A CB  
1690 C CG  . LEU A 245 ? 0.58029 0.44182 0.42662 -0.10063 0.08656  -0.04660 268 LEU A CG  
1691 C CD1 . LEU A 245 ? 0.46676 0.33003 0.31404 -0.10285 0.08827  -0.04833 268 LEU A CD1 
1692 C CD2 . LEU A 245 ? 0.41580 0.28266 0.26578 -0.10158 0.08614  -0.04775 268 LEU A CD2 
1693 N N   . PHE A 246 ? 0.72164 0.58994 0.57991 -0.08378 0.07619  -0.03873 269 PHE A N   
1694 C CA  . PHE A 246 ? 0.58746 0.46157 0.45237 -0.07876 0.07278  -0.03683 269 PHE A CA  
1695 C C   . PHE A 246 ? 0.63333 0.51087 0.50176 -0.07613 0.07049  -0.03577 269 PHE A C   
1696 O O   . PHE A 246 ? 0.68516 0.57100 0.56155 -0.07352 0.06829  -0.03550 269 PHE A O   
1697 C CB  . PHE A 246 ? 0.70008 0.56859 0.56071 -0.07726 0.07244  -0.03520 269 PHE A CB  
1698 C CG  . PHE A 246 ? 0.73936 0.61376 0.60645 -0.07274 0.06924  -0.03345 269 PHE A CG  
1699 C CD1 . PHE A 246 ? 0.60929 0.48673 0.47983 -0.06910 0.06640  -0.03172 269 PHE A CD1 
1700 C CD2 . PHE A 246 ? 0.60380 0.48055 0.47330 -0.07235 0.06915  -0.03357 269 PHE A CD2 
1701 C CE1 . PHE A 246 ? 0.51869 0.40137 0.39484 -0.06532 0.06357  -0.03014 269 PHE A CE1 
1702 C CE2 . PHE A 246 ? 0.62652 0.50847 0.50164 -0.06858 0.06631  -0.03201 269 PHE A CE2 
1703 C CZ  . PHE A 246 ? 0.57318 0.45805 0.45153 -0.06513 0.06353  -0.03028 269 PHE A CZ  
1704 N N   . ILE A 247 ? 0.85042 0.72127 0.71270 -0.07689 0.07113  -0.03516 270 ILE A N   
1705 C CA  . ILE A 247 ? 0.70387 0.57694 0.56860 -0.07464 0.06918  -0.03417 270 ILE A CA  
1706 C C   . ILE A 247 ? 0.80650 0.68699 0.67729 -0.07547 0.06895  -0.03568 270 ILE A C   
1707 O O   . ILE A 247 ? 0.96905 0.85596 0.84628 -0.07233 0.06645  -0.03484 270 ILE A O   
1708 C CB  . ILE A 247 ? 0.50129 0.36469 0.35708 -0.07646 0.07075  -0.03374 270 ILE A CB  
1709 C CG1 . ILE A 247 ? 0.69895 0.55634 0.55020 -0.07429 0.07011  -0.03187 270 ILE A CG1 
1710 C CG2 . ILE A 247 ? 0.92108 0.78651 0.77894 -0.07523 0.06940  -0.03328 270 ILE A CG2 
1711 C CD1 . ILE A 247 ? 0.87735 0.72354 0.71815 -0.07677 0.07245  -0.03167 270 ILE A CD1 
1712 N N   . LEU A 248 ? 0.74581 0.62584 0.61481 -0.07973 0.07158  -0.03798 271 LEU A N   
1713 C CA  . LEU A 248 ? 0.71554 0.60245 0.58986 -0.08093 0.07161  -0.03971 271 LEU A CA  
1714 C C   . LEU A 248 ? 0.70300 0.59929 0.58618 -0.07874 0.07011  -0.04016 271 LEU A C   
1715 O O   . LEU A 248 ? 0.72020 0.62359 0.60953 -0.07809 0.06919  -0.04103 271 LEU A O   
1716 C CB  . LEU A 248 ? 0.71008 0.59320 0.57900 -0.08669 0.07507  -0.04217 271 LEU A CB  
1717 C CG  . LEU A 248 ? 0.72573 0.60059 0.58600 -0.09062 0.07741  -0.04259 271 LEU A CG  
1718 C CD1 . LEU A 248 ? 0.91668 0.78258 0.76993 -0.08934 0.07735  -0.04043 271 LEU A CD1 
1719 C CD2 . LEU A 248 ? 0.50297 0.37412 0.35765 -0.09656 0.08109  -0.04498 271 LEU A CD2 
1720 N N   . GLY A 249 ? 0.60515 0.50148 0.48896 -0.07776 0.06999  -0.03969 272 GLY A N   
1721 C CA  . GLY A 249 ? 0.66368 0.56766 0.55466 -0.07665 0.06929  -0.04046 272 GLY A CA  
1722 C C   . GLY A 249 ? 0.65488 0.56526 0.55311 -0.07198 0.06611  -0.03865 272 GLY A C   
1723 O O   . GLY A 249 ? 0.67073 0.58009 0.56875 -0.06945 0.06430  -0.03678 272 GLY A O   
1724 N N   . PRO A 250 ? 0.51197 0.42902 0.41670 -0.07095 0.06550  -0.03928 273 PRO A N   
1725 C CA  . PRO A 250 ? 0.52773 0.45044 0.43912 -0.06690 0.06273  -0.03761 273 PRO A CA  
1726 C C   . PRO A 250 ? 0.67163 0.59058 0.58051 -0.06444 0.06115  -0.03516 273 PRO A C   
1727 O O   . PRO A 250 ? 0.59680 0.51889 0.50959 -0.06120 0.05873  -0.03343 273 PRO A O   
1728 C CB  . PRO A 250 ? 0.41916 0.34734 0.33588 -0.06713 0.06307  -0.03898 273 PRO A CB  
1729 C CG  . PRO A 250 ? 0.50423 0.43180 0.41887 -0.07097 0.06569  -0.04159 273 PRO A CG  
1730 C CD  . PRO A 250 ? 0.65722 0.57656 0.56324 -0.07360 0.06741  -0.04160 273 PRO A CD  
1731 N N   . GLU A 251 ? 0.73356 0.64591 0.63607 -0.06600 0.06252  -0.03505 274 GLU A N   
1732 C CA  . GLU A 251 ? 0.63213 0.54073 0.53194 -0.06384 0.06117  -0.03294 274 GLU A CA  
1733 C C   . GLU A 251 ? 0.75450 0.65931 0.65098 -0.06247 0.06014  -0.03143 274 GLU A C   
1734 O O   . GLU A 251 ? 0.87348 0.77599 0.76848 -0.06016 0.05859  -0.02956 274 GLU A O   
1735 C CB  . GLU A 251 ? 0.63532 0.53769 0.52905 -0.06619 0.06326  -0.03351 274 GLU A CB  
1736 C CG  . GLU A 251 ? 0.63221 0.52886 0.51954 -0.07042 0.06639  -0.03535 274 GLU A CG  
1737 C CD  . GLU A 251 ? 0.71774 0.61610 0.60593 -0.07336 0.06853  -0.03756 274 GLU A CD  
1738 O OE1 . GLU A 251 ? 0.68470 0.58938 0.57837 -0.07359 0.06840  -0.03883 274 GLU A OE1 
1739 O OE2 . GLU A 251 ? 0.73331 0.62661 0.61662 -0.07547 0.07043  -0.03808 274 GLU A OE2 
1740 N N   . GLY A 252 ? 0.56733 0.47137 0.46248 -0.06395 0.06100  -0.03230 275 GLY A N   
1741 C CA  . GLY A 252 ? 0.59091 0.49084 0.48242 -0.06308 0.06034  -0.03115 275 GLY A CA  
1742 C C   . GLY A 252 ? 0.92185 0.82754 0.81869 -0.06176 0.05898  -0.03115 275 GLY A C   
1743 O O   . GLY A 252 ? 0.87397 0.78527 0.77676 -0.05855 0.05659  -0.02984 275 GLY A O   
1744 N N   . PHE A 253 ? 0.88553 0.78978 0.78016 -0.06447 0.06062  -0.03271 276 PHE A N   
1745 C CA  . PHE A 253 ? 0.85842 0.76738 0.75725 -0.06366 0.05962  -0.03292 276 PHE A CA  
1746 C C   . PHE A 253 ? 0.83529 0.75132 0.73982 -0.06524 0.06045  -0.03510 276 PHE A C   
1747 O O   . PHE A 253 ? 1.05358 0.97375 0.96155 -0.06519 0.06005  -0.03577 276 PHE A O   
1748 C CB  . PHE A 253 ? 0.84624 0.74879 0.73881 -0.06552 0.06067  -0.03314 276 PHE A CB  
1749 C CG  . PHE A 253 ? 1.08265 0.97901 0.97053 -0.06333 0.05954  -0.03093 276 PHE A CG  
1750 C CD1 . PHE A 253 ? 1.05734 0.94398 0.93620 -0.06582 0.06158  -0.03105 276 PHE A CD1 
1751 C CD2 . PHE A 253 ? 1.01819 0.91832 0.91050 -0.05893 0.05657  -0.02877 276 PHE A CD2 
1752 C CE1 . PHE A 253 ? 1.05198 0.93289 0.92652 -0.06366 0.06060  -0.02912 276 PHE A CE1 
1753 C CE2 . PHE A 253 ? 1.04092 0.93577 0.92914 -0.05680 0.05542  -0.02688 276 PHE A CE2 
1754 C CZ  . PHE A 253 ? 1.18833 1.07364 1.06778 -0.05903 0.05741  -0.02710 276 PHE A CZ  
1755 N N   . GLY A 254 ? 0.78887 0.70644 0.69454 -0.06664 0.06161  -0.03632 277 GLY A N   
1756 C CA  . GLY A 254 ? 0.69973 0.62431 0.61123 -0.06778 0.06229  -0.03843 277 GLY A CA  
1757 C C   . GLY A 254 ? 0.86364 0.78861 0.77387 -0.07111 0.06402  -0.04072 277 GLY A C   
1758 O O   . GLY A 254 ? 1.16394 1.09597 1.08019 -0.07123 0.06396  -0.04229 277 GLY A O   
1759 N N   . VAL A 255 ? 0.81966 0.73713 0.72215 -0.07404 0.06567  -0.04110 278 VAL A N   
1760 C CA  . VAL A 255 ? 0.85286 0.77015 0.75336 -0.07823 0.06774  -0.04362 278 VAL A CA  
1761 C C   . VAL A 255 ? 0.78920 0.70957 0.69132 -0.08084 0.06953  -0.04597 278 VAL A C   
1762 O O   . VAL A 255 ? 0.84638 0.77331 0.75341 -0.08182 0.06979  -0.04801 278 VAL A O   
1763 C CB  . VAL A 255 ? 0.92275 0.83013 0.81360 -0.08161 0.06969  -0.04352 278 VAL A CB  
1764 C CG1 . VAL A 255 ? 0.60667 0.51368 0.49489 -0.08694 0.07228  -0.04629 278 VAL A CG1 
1765 C CG2 . VAL A 255 ? 0.82505 0.72955 0.71457 -0.07895 0.06790  -0.04133 278 VAL A CG2 
1766 N N   . LEU A 256 ? 0.91973 0.83553 0.81782 -0.08196 0.07080  -0.04581 279 LEU A N   
1767 C CA  . LEU A 256 ? 0.89549 0.81369 0.79482 -0.08429 0.07248  -0.04788 279 LEU A CA  
1768 C C   . LEU A 256 ? 0.81900 0.74458 0.72642 -0.08072 0.07066  -0.04743 279 LEU A C   
1769 O O   . LEU A 256 ? 0.85411 0.78022 0.76374 -0.07705 0.06861  -0.04518 279 LEU A O   
1770 C CB  . LEU A 256 ? 0.94026 0.85033 0.83181 -0.08712 0.07474  -0.04794 279 LEU A CB  
1771 C CG  . LEU A 256 ? 0.87510 0.77723 0.75778 -0.09194 0.07745  -0.04891 279 LEU A CG  
1772 C CD1 . LEU A 256 ? 0.85259 0.74583 0.72742 -0.09361 0.07925  -0.04819 279 LEU A CD1 
1773 C CD2 . LEU A 256 ? 0.94496 0.85004 0.82793 -0.09635 0.07960  -0.05193 279 LEU A CD2 
1774 N N   . SER A 257 ? 0.68719 0.61835 0.59890 -0.08204 0.07153  -0.04968 280 SER A N   
1775 C CA  . SER A 257 ? 0.60987 0.54689 0.52823 -0.07961 0.07050  -0.04969 280 SER A CA  
1776 C C   . SER A 257 ? 0.62813 0.56112 0.54319 -0.08043 0.07151  -0.04940 280 SER A C   
1777 O O   . SER A 257 ? 0.65389 0.57958 0.56158 -0.08282 0.07310  -0.04922 280 SER A O   
1778 C CB  . SER A 257 ? 0.71324 0.65742 0.63721 -0.08077 0.07116  -0.05238 280 SER A CB  
1779 O OG  . SER A 257 ? 0.58909 0.53086 0.50898 -0.08494 0.07373  -0.05458 280 SER A OG  
1780 N N   . VAL A 258 ? 0.68942 0.62717 0.61005 -0.07851 0.07067  -0.04946 281 VAL A N   
1781 C CA  . VAL A 258 ? 0.51675 0.45162 0.43516 -0.07907 0.07147  -0.04927 281 VAL A CA  
1782 C C   . VAL A 258 ? 0.56145 0.49363 0.47560 -0.08346 0.07439  -0.05165 281 VAL A C   
1783 O O   . VAL A 258 ? 0.65645 0.58230 0.56442 -0.08548 0.07593  -0.05148 281 VAL A O   
1784 C CB  . VAL A 258 ? 0.45696 0.39792 0.38263 -0.07624 0.06993  -0.04903 281 VAL A CB  
1785 C CG1 . VAL A 258 ? 0.50890 0.44766 0.43266 -0.07735 0.07105  -0.04940 281 VAL A CG1 
1786 C CG2 . VAL A 258 ? 0.52713 0.46948 0.45584 -0.07229 0.06721  -0.04649 281 VAL A CG2 
1787 N N   . TYR A 259 ? 0.73548 0.67254 0.65297 -0.08506 0.07524  -0.05400 282 TYR A N   
1788 C CA  . TYR A 259 ? 0.73540 0.67026 0.64889 -0.08951 0.07804  -0.05641 282 TYR A CA  
1789 C C   . TYR A 259 ? 0.61660 0.54418 0.52188 -0.09283 0.07973  -0.05645 282 TYR A C   
1790 O O   . TYR A 259 ? 0.63967 0.56136 0.53863 -0.09620 0.08204  -0.05716 282 TYR A O   
1791 C CB  . TYR A 259 ? 0.81140 0.75337 0.73034 -0.09041 0.07842  -0.05896 282 TYR A CB  
1792 C CG  . TYR A 259 ? 1.00464 0.95318 0.93115 -0.08780 0.07728  -0.05937 282 TYR A CG  
1793 C CD1 . TYR A 259 ? 0.88556 0.83274 0.81187 -0.08735 0.07752  -0.05892 282 TYR A CD1 
1794 C CD2 . TYR A 259 ? 0.96752 0.92355 0.90136 -0.08598 0.07609  -0.06040 282 TYR A CD2 
1795 C CE1 . TYR A 259 ? 0.89987 0.85275 0.83286 -0.08523 0.07656  -0.05942 282 TYR A CE1 
1796 C CE2 . TYR A 259 ? 0.97914 0.94070 0.91973 -0.08380 0.07520  -0.06094 282 TYR A CE2 
1797 C CZ  . TYR A 259 ? 1.09274 1.05260 1.03276 -0.08348 0.07542  -0.06041 282 TYR A CZ  
1798 O OH  . TYR A 259 ? 1.08160 1.04664 1.02811 -0.08145 0.07456  -0.06099 282 TYR A OH  
1799 N N   . GLY A 260 ? 0.65690 0.58469 0.56212 -0.09212 0.07872  -0.05579 283 GLY A N   
1800 C CA  . GLY A 260 ? 0.58005 0.50045 0.47732 -0.09513 0.08018  -0.05560 283 GLY A CA  
1801 C C   . GLY A 260 ? 0.72835 0.64043 0.61895 -0.09529 0.08085  -0.05385 283 GLY A C   
1802 O O   . GLY A 260 ? 0.84901 0.75398 0.73189 -0.09928 0.08338  -0.05454 283 GLY A O   
1803 N N   . SER A 261 ? 0.81241 0.72517 0.70572 -0.09109 0.07864  -0.05156 284 SER A N   
1804 C CA  . SER A 261 ? 0.60371 0.50905 0.49110 -0.09094 0.07909  -0.04992 284 SER A CA  
1805 C C   . SER A 261 ? 0.64262 0.54538 0.52717 -0.09365 0.08136  -0.05123 284 SER A C   
1806 O O   . SER A 261 ? 0.67852 0.57336 0.55542 -0.09633 0.08342  -0.05119 284 SER A O   
1807 C CB  . SER A 261 ? 0.60457 0.51221 0.49612 -0.08593 0.07610  -0.04736 284 SER A CB  
1808 O OG  . SER A 261 ? 0.76340 0.66460 0.64981 -0.08569 0.07647  -0.04596 284 SER A OG  
1809 N N   . THR A 262 ? 0.52513 0.43430 0.41560 -0.09313 0.08115  -0.05248 285 THR A N   
1810 C CA  . THR A 262 ? 0.60918 0.51660 0.49753 -0.09579 0.08334  -0.05396 285 THR A CA  
1811 C C   . THR A 262 ? 0.54810 0.45023 0.42947 -0.10123 0.08663  -0.05598 285 THR A C   
1812 O O   . THR A 262 ? 0.64091 0.53634 0.51587 -0.10388 0.08880  -0.05619 285 THR A O   
1813 C CB  . THR A 262 ? 0.65291 0.56856 0.54910 -0.09444 0.08256  -0.05519 285 THR A CB  
1814 O OG1 . THR A 262 ? 0.55358 0.47346 0.45561 -0.08981 0.07973  -0.05329 285 THR A OG1 
1815 C CG2 . THR A 262 ? 0.63427 0.54821 0.52835 -0.09721 0.08483  -0.05678 285 THR A CG2 
1816 N N   . VAL A 263 ? 0.65043 0.55550 0.53285 -0.10318 0.08714  -0.05757 286 VAL A N   
1817 C CA  . VAL A 263 ? 0.70035 0.60072 0.57606 -0.10882 0.09033  -0.05960 286 VAL A CA  
1818 C C   . VAL A 263 ? 0.63765 0.52792 0.50402 -0.11091 0.09182  -0.05838 286 VAL A C   
1819 O O   . VAL A 263 ? 0.68282 0.56654 0.54225 -0.11481 0.09463  -0.05921 286 VAL A O   
1820 C CB  . VAL A 263 ? 0.68949 0.59523 0.56814 -0.11052 0.09041  -0.06148 286 VAL A CB  
1821 C CG1 . VAL A 263 ? 0.76563 0.68116 0.65365 -0.10794 0.08883  -0.06256 286 VAL A CG1 
1822 C CG2 . VAL A 263 ? 0.84162 0.74676 0.71972 -0.10940 0.08906  -0.06030 286 VAL A CG2 
1823 N N   . GLY A 264 ? 0.61171 0.50031 0.47750 -0.10846 0.09007  -0.05643 287 GLY A N   
1824 C CA  . GLY A 264 ? 0.49353 0.37224 0.35031 -0.11022 0.09145  -0.05521 287 GLY A CA  
1825 C C   . GLY A 264 ? 0.71006 0.58314 0.56294 -0.10989 0.09229  -0.05425 287 GLY A C   
1826 O O   . GLY A 264 ? 0.72556 0.59006 0.56978 -0.11368 0.09506  -0.05460 287 GLY A O   
1827 N N   . HIS A 265 ? 0.82888 0.70670 0.68794 -0.10564 0.09006  -0.05314 288 HIS A N   
1828 C CA  . HIS A 265 ? 0.59111 0.46398 0.44688 -0.10489 0.09049  -0.05202 288 HIS A CA  
1829 C C   . HIS A 265 ? 0.67731 0.54754 0.52966 -0.10896 0.09353  -0.05400 288 HIS A C   
1830 O O   . HIS A 265 ? 0.77234 0.63502 0.61801 -0.11077 0.09541  -0.05369 288 HIS A O   
1831 C CB  . HIS A 265 ? 0.53708 0.41609 0.40039 -0.09962 0.08732  -0.05038 288 HIS A CB  
1832 C CG  . HIS A 265 ? 0.58769 0.46574 0.45143 -0.09579 0.08478  -0.04786 288 HIS A CG  
1833 N ND1 . HIS A 265 ? 0.63116 0.51543 0.50103 -0.09257 0.08209  -0.04701 288 HIS A ND1 
1834 C CD2 . HIS A 265 ? 0.52879 0.40037 0.38754 -0.09467 0.08456  -0.04605 288 HIS A CD2 
1835 C CE1 . HIS A 265 ? 0.69128 0.57299 0.55992 -0.08967 0.08029  -0.04477 288 HIS A CE1 
1836 N NE2 . HIS A 265 ? 0.48121 0.35529 0.34317 -0.09082 0.08170  -0.04416 288 HIS A NE2 
1837 N N   . THR A 266 ? 0.66443 0.54069 0.52113 -0.11050 0.09412  -0.05609 289 THR A N   
1838 C CA  . THR A 266 ? 0.67501 0.54919 0.52874 -0.11445 0.09701  -0.05810 289 THR A CA  
1839 C C   . THR A 266 ? 0.60885 0.47454 0.45284 -0.12008 0.10044  -0.05923 289 THR A C   
1840 O O   . THR A 266 ? 0.67264 0.53259 0.51091 -0.12340 0.10314  -0.06007 289 THR A O   
1841 C CB  . THR A 266 ? 0.67302 0.55595 0.53392 -0.11456 0.09668  -0.06008 289 THR A CB  
1842 O OG1 . THR A 266 ? 0.86242 0.75328 0.73219 -0.10934 0.09328  -0.05888 289 THR A OG1 
1843 C CG2 . THR A 266 ? 0.85710 0.73920 0.71691 -0.11702 0.09886  -0.06167 289 THR A CG2 
1844 N N   . ILE A 267 ? 0.63966 0.50435 0.48147 -0.12142 0.10047  -0.05928 290 ILE A N   
1845 C CA  . ILE A 267 ? 0.69538 0.55347 0.53056 -0.12624 0.10271  -0.05858 290 ILE A CA  
1846 C C   . ILE A 267 ? 0.64540 0.49546 0.47618 -0.12572 0.10272  -0.05507 290 ILE A C   
1847 O O   . ILE A 267 ? 0.83214 0.67815 0.66065 -0.12856 0.10428  -0.05360 290 ILE A O   
1848 C CB  . ILE A 267 ? 0.76439 0.62402 0.59963 -0.12710 0.10212  -0.05841 290 ILE A CB  
1849 C CG1 . ILE A 267 ? 0.76210 0.62956 0.60155 -0.12873 0.10252  -0.06192 290 ILE A CG1 
1850 C CG2 . ILE A 267 ? 0.58358 0.43746 0.41455 -0.13064 0.10331  -0.05501 290 ILE A CG2 
1851 C CD1 . ILE A 267 ? 0.53103 0.40116 0.37140 -0.12950 0.10182  -0.06210 290 ILE A CD1 
1852 N N   . ILE A 268 ? 0.62416 0.47194 0.45384 -0.12203 0.10096  -0.05365 291 ILE A N   
1853 C CA  . ILE A 268 ? 0.73531 0.57551 0.56078 -0.12128 0.10080  -0.05033 291 ILE A CA  
1854 C C   . ILE A 268 ? 0.76001 0.59897 0.58574 -0.12029 0.10114  -0.05039 291 ILE A C   
1855 O O   . ILE A 268 ? 0.65746 0.49010 0.47988 -0.12080 0.10157  -0.04785 291 ILE A O   
1856 C CB  . ILE A 268 ? 0.67887 0.51727 0.50315 -0.11752 0.09876  -0.04896 291 ILE A CB  
1857 C CG1 . ILE A 268 ? 0.74708 0.59041 0.57490 -0.11299 0.09700  -0.05074 291 ILE A CG1 
1858 C CG2 . ILE A 268 ? 0.67115 0.51091 0.49543 -0.11874 0.09850  -0.04881 291 ILE A CG2 
1859 C CD1 . ILE A 268 ? 0.66778 0.51075 0.49665 -0.10877 0.09427  -0.04839 291 ILE A CD1 
1860 N N   . ASP A 269 ? 0.69755 0.54261 0.52741 -0.11889 0.10098  -0.05310 292 ASP A N   
1861 C CA  . ASP A 269 ? 0.62845 0.47305 0.45906 -0.11870 0.10163  -0.05326 292 ASP A CA  
1862 C C   . ASP A 269 ? 0.74451 0.58582 0.57331 -0.12331 0.10384  -0.05273 292 ASP A C   
1863 O O   . ASP A 269 ? 0.78461 0.62100 0.61135 -0.12398 0.10445  -0.05096 292 ASP A O   
1864 C CB  . ASP A 269 ? 0.62736 0.48036 0.46421 -0.11635 0.10080  -0.05562 292 ASP A CB  
1865 C CG  . ASP A 269 ? 0.77625 0.63388 0.61929 -0.11052 0.09708  -0.05332 292 ASP A CG  
1866 O OD1 . ASP A 269 ? 0.98590 0.83836 0.82511 -0.10893 0.09636  -0.05143 292 ASP A OD1 
1867 O OD2 . ASP A 269 ? 0.71411 0.58045 0.56567 -0.10763 0.09493  -0.05342 292 ASP A OD2 
1868 N N   . LEU A 270 ? 0.88529 0.72960 0.71512 -0.12656 0.10502  -0.05424 293 LEU A N   
1869 C CA  . LEU A 270 ? 0.88245 0.72434 0.71088 -0.13120 0.10714  -0.05363 293 LEU A CA  
1870 C C   . LEU A 270 ? 0.78063 0.61458 0.60451 -0.13292 0.10760  -0.04967 293 LEU A C   
1871 O O   . LEU A 270 ? 0.87070 0.70052 0.69309 -0.13518 0.10886  -0.04809 293 LEU A O   
1872 C CB  . LEU A 270 ? 0.73545 0.58237 0.56575 -0.13419 0.10807  -0.05572 293 LEU A CB  
1873 C CG  . LEU A 270 ? 0.78867 0.64290 0.62359 -0.13302 0.10809  -0.05953 293 LEU A CG  
1874 C CD1 . LEU A 270 ? 0.80486 0.66514 0.64221 -0.13483 0.10842  -0.06206 293 LEU A CD1 
1875 C CD2 . LEU A 270 ? 0.89956 0.75336 0.73524 -0.13451 0.10951  -0.06015 293 LEU A CD2 
1876 N N   . MET A 271 ? 0.48173 0.31347 0.30356 -0.13165 0.10652  -0.04788 294 MET A N   
1877 C CA  . MET A 271 ? 0.53460 0.35901 0.35221 -0.13300 0.10688  -0.04381 294 MET A CA  
1878 C C   . MET A 271 ? 0.65591 0.47519 0.47182 -0.13055 0.10621  -0.04219 294 MET A C   
1879 O O   . MET A 271 ? 0.62286 0.43679 0.43662 -0.13271 0.10727  -0.03972 294 MET A O   
1880 C CB  . MET A 271 ? 0.75278 0.57657 0.56891 -0.13169 0.10573  -0.04243 294 MET A CB  
1881 C CG  . MET A 271 ? 0.77870 0.60715 0.59620 -0.13402 0.10622  -0.04335 294 MET A CG  
1882 S SD  . MET A 271 ? 0.79654 0.62322 0.61208 -0.13179 0.10468  -0.04117 294 MET A SD  
1883 C CE  . MET A 271 ? 0.83867 0.65959 0.65013 -0.13608 0.10656  -0.03603 294 MET A CE  
1884 N N   . SER A 272 ? 0.72809 0.54921 0.54519 -0.12612 0.10441  -0.04341 295 SER A N   
1885 C CA  . SER A 272 ? 0.58336 0.39986 0.39865 -0.12341 0.10346  -0.04162 295 SER A CA  
1886 C C   . SER A 272 ? 0.56999 0.38613 0.38655 -0.12418 0.10435  -0.04218 295 SER A C   
1887 O O   . SER A 272 ? 0.51045 0.32127 0.32501 -0.12384 0.10431  -0.04006 295 SER A O   
1888 C CB  . SER A 272 ? 0.54397 0.36348 0.36059 -0.11851 0.10125  -0.04267 295 SER A CB  
1889 O OG  . SER A 272 ? 0.67732 0.50424 0.49843 -0.11702 0.10089  -0.04584 295 SER A OG  
1890 N N   . LYS A 273 A 0.51854 0.34041 0.33856 -0.12527 0.10516  -0.04505 296 LYS A N   
1891 C CA  . LYS A 273 A 0.53268 0.35545 0.35467 -0.12556 0.10589  -0.04603 296 LYS A CA  
1892 C C   . LYS A 273 A 0.68867 0.51075 0.51077 -0.13031 0.10806  -0.04622 296 LYS A C   
1893 O O   . LYS A 273 A 0.67987 0.49617 0.49989 -0.13247 0.10898  -0.04387 296 LYS A O   
1894 C CB  . LYS A 273 A 0.54448 0.37489 0.37090 -0.12261 0.10500  -0.04906 296 LYS A CB  
1895 C CG  . LYS A 273 A 0.63918 0.47129 0.46619 -0.11793 0.10278  -0.04880 296 LYS A CG  
1896 C CD  . LYS A 273 A 0.77153 0.61206 0.60322 -0.11552 0.10186  -0.05151 296 LYS A CD  
1897 C CE  . LYS A 273 A 0.70405 0.54728 0.53805 -0.11125 0.10012  -0.05127 296 LYS A CE  
1898 N NZ  . LYS A 273 A 0.68416 0.52735 0.51763 -0.10794 0.09800  -0.04997 296 LYS A NZ  
1899 N N   . ASN A 274 ? 0.72775 0.55559 0.55237 -0.13182 0.10879  -0.04885 297 ASN A N   
1900 C CA  . ASN A 274 ? 0.68418 0.51256 0.50944 -0.13617 0.11080  -0.04949 297 ASN A CA  
1901 C C   . ASN A 274 ? 0.61227 0.43441 0.43409 -0.13997 0.11197  -0.04610 297 ASN A C   
1902 O O   . ASN A 274 ? 0.65399 0.47243 0.47519 -0.14241 0.11317  -0.04466 297 ASN A O   
1903 C CB  . ASN A 274 ? 0.71725 0.55279 0.54537 -0.13697 0.11113  -0.05267 297 ASN A CB  
1904 C CG  . ASN A 274 ? 0.88620 0.72822 0.71826 -0.13335 0.11007  -0.05569 297 ASN A CG  
1905 O OD1 . ASN A 274 ? 0.89585 0.74017 0.72877 -0.12981 0.10836  -0.05606 297 ASN A OD1 
1906 N ND2 . ASN A 274 ? 0.78458 0.62968 0.61926 -0.13420 0.11106  -0.05762 297 ASN A ND2 
1907 N N   . CYS A 275 ? 0.60441 0.42561 0.42432 -0.14053 0.11163  -0.04461 298 CYS A N   
1908 C CA  . CYS A 275 ? 0.58967 0.40607 0.40683 -0.14445 0.11290  -0.04109 298 CYS A CA  
1909 C C   . CYS A 275 ? 0.68664 0.49539 0.50099 -0.14382 0.11260  -0.03750 298 CYS A C   
1910 O O   . CYS A 275 ? 0.82478 0.62918 0.63793 -0.14712 0.11389  -0.03480 298 CYS A O   
1911 C CB  . CYS A 275 ? 0.51844 0.33625 0.33449 -0.14506 0.11261  -0.04016 298 CYS A CB  
1912 S SG  . CYS A 275 ? 0.81241 0.63922 0.63190 -0.14632 0.11298  -0.04418 298 CYS A SG  
1913 N N   . TRP A 276 ? 0.70133 0.50851 0.51480 -0.13961 0.11083  -0.03734 299 TRP A N   
1914 C CA  . TRP A 276 ? 0.63195 0.43204 0.44276 -0.13857 0.11029  -0.03411 299 TRP A CA  
1915 C C   . TRP A 276 ? 0.50463 0.30295 0.31673 -0.13941 0.11100  -0.03435 299 TRP A C   
1916 O O   . TRP A 276 ? 0.60925 0.40162 0.41976 -0.14146 0.11166  -0.03130 299 TRP A O   
1917 C CB  . TRP A 276 ? 0.61666 0.41662 0.42662 -0.13370 0.10818  -0.03440 299 TRP A CB  
1918 C CG  . TRP A 276 ? 0.63136 0.42424 0.43825 -0.13226 0.10737  -0.03109 299 TRP A CG  
1919 C CD1 . TRP A 276 ? 0.53725 0.32548 0.34089 -0.13235 0.10701  -0.02784 299 TRP A CD1 
1920 C CD2 . TRP A 276 ? 0.65848 0.44840 0.46543 -0.13039 0.10676  -0.03069 299 TRP A CD2 
1921 N NE1 . TRP A 276 ? 0.64980 0.43209 0.45137 -0.13065 0.10619  -0.02550 299 TRP A NE1 
1922 C CE2 . TRP A 276 ? 0.64784 0.43109 0.45142 -0.12947 0.10601  -0.02724 299 TRP A CE2 
1923 C CE3 . TRP A 276 ? 0.52776 0.32020 0.33742 -0.12947 0.10680  -0.03281 299 TRP A CE3 
1924 C CZ2 . TRP A 276 ? 0.58474 0.36375 0.38762 -0.12770 0.10523  -0.02603 299 TRP A CZ2 
1925 C CZ3 . TRP A 276 ? 0.63571 0.42414 0.44476 -0.12777 0.10607  -0.03150 299 TRP A CZ3 
1926 C CH2 . TRP A 276 ? 0.60927 0.39103 0.41496 -0.12692 0.10527  -0.02822 299 TRP A CH2 
1927 N N   . GLY A 277 ? 0.61263 0.41631 0.42790 -0.13782 0.11084  -0.03786 300 GLY A N   
1928 C CA  . GLY A 277 ? 0.79782 0.60087 0.61486 -0.13868 0.11159  -0.03847 300 GLY A CA  
1929 C C   . GLY A 277 ? 0.79821 0.59959 0.61544 -0.14366 0.11360  -0.03746 300 GLY A C   
1930 O O   . GLY A 277 ? 0.80676 0.60373 0.62388 -0.14530 0.11424  -0.03575 300 GLY A O   
1931 N N   . LEU A 278 ? 0.92815 0.73320 0.74589 -0.14620 0.11458  -0.03845 301 LEU A N   
1932 C CA  . LEU A 278 ? 0.76988 0.57360 0.58768 -0.15117 0.11649  -0.03708 301 LEU A CA  
1933 C C   . LEU A 278 ? 0.77087 0.56711 0.58593 -0.15333 0.11684  -0.03227 301 LEU A C   
1934 O O   . LEU A 278 ? 0.86158 0.65428 0.67706 -0.15604 0.11785  -0.03055 301 LEU A O   
1935 C CB  . LEU A 278 ? 0.73257 0.54139 0.55101 -0.15346 0.11732  -0.03841 301 LEU A CB  
1936 C CG  . LEU A 278 ? 0.85290 0.66553 0.67370 -0.15704 0.11905  -0.04034 301 LEU A CG  
1937 C CD1 . LEU A 278 ? 0.96370 0.77865 0.78722 -0.15596 0.11926  -0.04325 301 LEU A CD1 
1938 C CD2 . LEU A 278 ? 0.91864 0.73768 0.74048 -0.15795 0.11931  -0.04261 301 LEU A CD2 
1939 N N   . LEU A 279 ? 0.67733 0.47112 0.48977 -0.15216 0.11597  -0.02993 302 LEU A N   
1940 C CA  . LEU A 279 ? 0.67653 0.46326 0.48641 -0.15398 0.11620  -0.02502 302 LEU A CA  
1941 C C   . LEU A 279 ? 0.78065 0.56203 0.59043 -0.15253 0.11554  -0.02390 302 LEU A C   
1942 O O   . LEU A 279 ? 0.80953 0.58572 0.61898 -0.15532 0.11628  -0.02066 302 LEU A O   
1943 C CB  . LEU A 279 ? 0.63880 0.42426 0.44597 -0.15228 0.11520  -0.02300 302 LEU A CB  
1944 C CG  . LEU A 279 ? 0.72616 0.51556 0.53309 -0.15472 0.11608  -0.02253 302 LEU A CG  
1945 C CD1 . LEU A 279 ? 0.66982 0.45773 0.47416 -0.15254 0.11494  -0.02050 302 LEU A CD1 
1946 C CD2 . LEU A 279 ? 0.71259 0.50028 0.51953 -0.15995 0.11800  -0.01916 302 LEU A CD2 
1947 N N   . GLY A 280 ? 0.65649 0.43934 0.46690 -0.14827 0.11412  -0.02643 303 GLY A N   
1948 C CA  . GLY A 280 ? 0.63627 0.41438 0.44664 -0.14670 0.11337  -0.02532 303 GLY A CA  
1949 C C   . GLY A 280 ? 0.71767 0.49508 0.53050 -0.14950 0.11460  -0.02568 303 GLY A C   
1950 O O   . GLY A 280 ? 0.79029 0.56176 0.60285 -0.15072 0.11462  -0.02295 303 GLY A O   
1951 N N   . HIS A 281 ? 0.75480 0.53818 0.57022 -0.15059 0.11558  -0.02901 304 HIS A N   
1952 C CA  . HIS A 281 ? 0.91132 0.69423 0.72911 -0.15360 0.11690  -0.02934 304 HIS A CA  
1953 C C   . HIS A 281 ? 0.78569 0.56388 0.60251 -0.15826 0.11814  -0.02543 304 HIS A C   
1954 O O   . HIS A 281 ? 0.75283 0.52599 0.57035 -0.16018 0.11846  -0.02315 304 HIS A O   
1955 C CB  . HIS A 281 ? 0.91526 0.70572 0.73582 -0.15396 0.11777  -0.03357 304 HIS A CB  
1956 C CG  . HIS A 281 ? 0.94967 0.74017 0.77283 -0.15671 0.11909  -0.03431 304 HIS A CG  
1957 N ND1 . HIS A 281 ? 0.79901 0.58949 0.62425 -0.15498 0.11870  -0.03567 304 HIS A ND1 
1958 C CD2 . HIS A 281 ? 1.03935 0.83006 0.86349 -0.16110 0.12077  -0.03382 304 HIS A CD2 
1959 C CE1 . HIS A 281 ? 1.09172 0.88222 0.91911 -0.15815 0.12008  -0.03609 304 HIS A CE1 
1960 N NE2 . HIS A 281 ? 1.28772 1.07830 1.11446 -0.16188 0.12134  -0.03498 304 HIS A NE2 
1961 N N   . TYR A 282 ? 0.80271 0.58263 0.61818 -0.16014 0.11877  -0.02441 305 TYR A N   
1962 C CA  . TYR A 282 ? 0.62868 0.40489 0.44330 -0.16460 0.11996  -0.02018 305 TYR A CA  
1963 C C   . TYR A 282 ? 0.67979 0.44805 0.49256 -0.16441 0.11913  -0.01558 305 TYR A C   
1964 O O   . TYR A 282 ? 0.73671 0.50038 0.55028 -0.16759 0.11982  -0.01239 305 TYR A O   
1965 C CB  . TYR A 282 ? 0.69917 0.47920 0.51252 -0.16595 0.12053  -0.01977 305 TYR A CB  
1966 C CG  . TYR A 282 ? 0.86247 0.63992 0.67518 -0.17066 0.12189  -0.01512 305 TYR A CG  
1967 C CD1 . TYR A 282 ? 0.95007 0.72747 0.76489 -0.17481 0.12342  -0.01432 305 TYR A CD1 
1968 C CD2 . TYR A 282 ? 0.85905 0.63439 0.66920 -0.17097 0.12167  -0.01130 305 TYR A CD2 
1969 C CE1 . TYR A 282 ? 0.73680 0.51227 0.55134 -0.17921 0.12467  -0.00967 305 TYR A CE1 
1970 C CE2 . TYR A 282 ? 0.75148 0.52506 0.56127 -0.17530 0.12298  -0.00656 305 TYR A CE2 
1971 C CZ  . TYR A 282 ? 0.85808 0.63180 0.67014 -0.17943 0.12447  -0.00568 305 TYR A CZ  
1972 O OH  . TYR A 282 ? 0.97168 0.74403 0.78368 -0.18379 0.12578  -0.00060 305 TYR A OH  
1973 N N   . LEU A 283 ? 0.81805 0.58455 0.62848 -0.16073 0.11760  -0.01506 306 LEU A N   
1974 C CA  . LEU A 283 ? 0.65345 0.41238 0.46206 -0.16033 0.11671  -0.01077 306 LEU A CA  
1975 C C   . LEU A 283 ? 0.61368 0.36846 0.42424 -0.16043 0.11639  -0.01055 306 LEU A C   
1976 O O   . LEU A 283 ? 0.79100 0.53969 0.60172 -0.16284 0.11652  -0.00654 306 LEU A O   
1977 C CB  . LEU A 283 ? 0.68482 0.44302 0.49078 -0.15584 0.11499  -0.01097 306 LEU A CB  
1978 C CG  . LEU A 283 ? 0.48968 0.24010 0.29365 -0.15486 0.11386  -0.00686 306 LEU A CG  
1979 C CD1 . LEU A 283 ? 0.84760 0.59372 0.65065 -0.15890 0.11480  -0.00153 306 LEU A CD1 
1980 C CD2 . LEU A 283 ? 0.57360 0.32379 0.37495 -0.15030 0.11216  -0.00739 306 LEU A CD2 
1981 N N   . ARG A 284 ? 0.80054 0.55879 0.61296 -0.15790 0.11595  -0.01470 307 ARG A N   
1982 C CA  . ARG A 284 ? 0.70998 0.46488 0.52449 -0.15766 0.11554  -0.01479 307 ARG A CA  
1983 C C   . ARG A 284 ? 0.86934 0.62272 0.68644 -0.16232 0.11702  -0.01355 307 ARG A C   
1984 O O   . ARG A 284 ? 0.78298 0.53065 0.60134 -0.16359 0.11669  -0.01115 307 ARG A O   
1985 C CB  . ARG A 284 ? 0.60800 0.36809 0.42410 -0.15393 0.11485  -0.01936 307 ARG A CB  
1986 C CG  . ARG A 284 ? 0.60376 0.36312 0.41779 -0.14926 0.11300  -0.01955 307 ARG A CG  
1987 C CD  . ARG A 284 ? 0.77177 0.53786 0.58729 -0.14553 0.11235  -0.02387 307 ARG A CD  
1988 N NE  . ARG A 284 ? 0.62610 0.39063 0.44028 -0.14130 0.11049  -0.02358 307 ARG A NE  
1989 C CZ  . ARG A 284 ? 0.69683 0.46610 0.51248 -0.13771 0.10955  -0.02641 307 ARG A CZ  
1990 N NH1 . ARG A 284 ? 0.78158 0.55753 0.60016 -0.13763 0.11025  -0.02978 307 ARG A NH1 
1991 N NH2 . ARG A 284 ? 0.68890 0.45635 0.50319 -0.13413 0.10785  -0.02567 307 ARG A NH2 
1992 N N   . VAL A 285 ? 0.83594 0.59433 0.65409 -0.16495 0.11856  -0.01512 308 VAL A N   
1993 C CA  . VAL A 285 ? 0.72858 0.48560 0.54909 -0.16964 0.12001  -0.01362 308 VAL A CA  
1994 C C   . VAL A 285 ? 0.74800 0.49839 0.56748 -0.17265 0.12008  -0.00783 308 VAL A C   
1995 O O   . VAL A 285 ? 0.95441 0.69999 0.77596 -0.17524 0.12024  -0.00529 308 VAL A O   
1996 C CB  . VAL A 285 ? 0.77848 0.54239 0.60016 -0.17190 0.12164  -0.01637 308 VAL A CB  
1997 C CG1 . VAL A 285 ? 0.75576 0.52640 0.57841 -0.16846 0.12134  -0.02185 308 VAL A CG1 
1998 C CG2 . VAL A 285 ? 0.83702 0.60254 0.65670 -0.17404 0.12241  -0.01423 308 VAL A CG2 
1999 N N   . LEU A 286 ? 0.79639 0.54654 0.61295 -0.17237 0.11992  -0.00550 309 LEU A N   
2000 C CA  . LEU A 286 ? 0.77622 0.52077 0.59189 -0.17528 0.12009  0.00040  309 LEU A CA  
2001 C C   . LEU A 286 ? 0.71594 0.45288 0.53170 -0.17389 0.11857  0.00304  309 LEU A C   
2002 O O   . LEU A 286 ? 0.90228 0.63377 0.71948 -0.17699 0.11870  0.00736  309 LEU A O   
2003 C CB  . LEU A 286 ? 0.81832 0.56469 0.63079 -0.17465 0.12012  0.00209  309 LEU A CB  
2004 C CG  . LEU A 286 ? 0.91256 0.66190 0.72502 -0.17890 0.12183  0.00468  309 LEU A CG  
2005 C CD1 . LEU A 286 ? 0.90042 0.65679 0.71484 -0.18044 0.12318  0.00043  309 LEU A CD1 
2006 C CD2 . LEU A 286 ? 0.80323 0.55403 0.61249 -0.17754 0.12156  0.00637  309 LEU A CD2 
2007 N N   . ILE A 287 ? 0.62183 0.35839 0.43629 -0.16926 0.11703  0.00065  310 ILE A N   
2008 C CA  . ILE A 287 ? 0.74731 0.47695 0.56194 -0.16768 0.11546  0.00277  310 ILE A CA  
2009 C C   . ILE A 287 ? 0.75718 0.48457 0.57577 -0.16973 0.11564  0.00233  310 ILE A C   
2010 O O   . ILE A 287 ? 0.87649 0.59716 0.69653 -0.17128 0.11495  0.00590  310 ILE A O   
2011 C CB  . ILE A 287 ? 0.81209 0.54286 0.62476 -0.16227 0.11385  -0.00011 310 ILE A CB  
2012 C CG1 . ILE A 287 ? 0.81545 0.54765 0.62435 -0.16036 0.11351  0.00078  310 ILE A CG1 
2013 C CG2 . ILE A 287 ? 0.82112 0.54523 0.63440 -0.16064 0.11221  0.00157  310 ILE A CG2 
2014 C CD1 . ILE A 287 ? 0.79529 0.52108 0.60229 -0.16175 0.11311  0.00644  310 ILE A CD1 
2015 N N   . HIS A 288 ? 0.63563 0.36869 0.45626 -0.16983 0.11654  -0.00202 311 HIS A N   
2016 C CA  . HIS A 288 ? 0.67461 0.40635 0.49913 -0.17140 0.11672  -0.00308 311 HIS A CA  
2017 C C   . HIS A 288 ? 0.66897 0.39726 0.49569 -0.17668 0.11777  0.00077  311 HIS A C   
2018 O O   . HIS A 288 ? 0.72754 0.45032 0.55706 -0.17830 0.11717  0.00288  311 HIS A O   
2019 C CB  . HIS A 288 ? 0.85915 0.59842 0.68516 -0.17019 0.11754  -0.00855 311 HIS A CB  
2020 C CG  . HIS A 288 ? 0.93681 0.67533 0.76669 -0.17091 0.11754  -0.01020 311 HIS A CG  
2021 N ND1 . HIS A 288 ? 1.04576 0.78153 0.87677 -0.16813 0.11603  -0.01091 311 HIS A ND1 
2022 C CD2 . HIS A 288 ? 0.91514 0.65544 0.74818 -0.17412 0.11885  -0.01129 311 HIS A CD2 
2023 C CE1 . HIS A 288 ? 0.96262 0.69854 0.79740 -0.16961 0.11639  -0.01238 311 HIS A CE1 
2024 N NE2 . HIS A 288 ? 1.09102 0.82957 0.92705 -0.17322 0.11810  -0.01265 311 HIS A NE2 
2025 N N   . GLU A 289 ? 0.83678 0.56839 0.66256 -0.17945 0.11927  0.00184  312 GLU A N   
2026 C CA  . GLU A 289 ? 0.85356 0.58256 0.68145 -0.18463 0.12036  0.00594  312 GLU A CA  
2027 C C   . GLU A 289 ? 0.84814 0.56910 0.67596 -0.18569 0.11925  0.01180  312 GLU A C   
2028 O O   . GLU A 289 ? 0.87054 0.58685 0.70158 -0.18907 0.11926  0.01510  312 GLU A O   
2029 C CB  . GLU A 289 ? 0.93746 0.67201 0.76399 -0.18707 0.12209  0.00623  312 GLU A CB  
2030 C CG  . GLU A 289 ? 1.10273 0.84430 0.93086 -0.18793 0.12349  0.00145  312 GLU A CG  
2031 C CD  . GLU A 289 ? 1.23236 0.97994 1.05890 -0.18969 0.12496  0.00118  312 GLU A CD  
2032 O OE1 . GLU A 289 ? 1.36931 1.11543 1.19398 -0.19108 0.12514  0.00539  312 GLU A OE1 
2033 O OE2 . GLU A 289 ? 0.99030 0.74422 0.81761 -0.18969 0.12592  -0.00318 312 GLU A OE2 
2034 N N   . HIS A 290 ? 0.74226 0.46150 0.56661 -0.18288 0.11823  0.01330  313 HIS A N   
2035 C CA  . HIS A 290 ? 0.74689 0.45860 0.57101 -0.18364 0.11711  0.01895  313 HIS A CA  
2036 C C   . HIS A 290 ? 0.84527 0.55080 0.67246 -0.18304 0.11556  0.01923  313 HIS A C   
2037 O O   . HIS A 290 ? 0.84377 0.54322 0.67361 -0.18597 0.11510  0.02382  313 HIS A O   
2038 C CB  . HIS A 290 ? 0.66299 0.37441 0.48271 -0.18010 0.11620  0.01970  313 HIS A CB  
2039 C CG  . HIS A 290 ? 0.77159 0.47550 0.59081 -0.18055 0.11501  0.02547  313 HIS A CG  
2040 N ND1 . HIS A 290 ? 0.94106 0.63873 0.76116 -0.17837 0.11308  0.02605  313 HIS A ND1 
2041 C CD2 . HIS A 290 ? 0.82665 0.52847 0.64481 -0.18294 0.11547  0.03105  313 HIS A CD2 
2042 C CE1 . HIS A 290 ? 1.14093 0.83272 0.96052 -0.17935 0.11233  0.03163  313 HIS A CE1 
2043 N NE2 . HIS A 290 ? 1.12034 0.81459 0.93875 -0.18212 0.11379  0.03488  313 HIS A NE2 
2044 N N   . ILE A 291 ? 0.76017 0.46736 0.58742 -0.17932 0.11467  0.01448  314 ILE A N   
2045 C CA  . ILE A 291 ? 0.79392 0.49553 0.62404 -0.17837 0.11303  0.01457  314 ILE A CA  
2046 C C   . ILE A 291 ? 0.80899 0.50988 0.64400 -0.18212 0.11371  0.01442  314 ILE A C   
2047 O O   . ILE A 291 ? 0.87615 0.57069 0.71459 -0.18349 0.11252  0.01678  314 ILE A O   
2048 C CB  . ILE A 291 ? 0.86974 0.57403 0.69856 -0.17328 0.11195  0.00976  314 ILE A CB  
2049 C CG1 . ILE A 291 ? 0.58624 0.28810 0.41113 -0.16966 0.11055  0.01116  314 ILE A CG1 
2050 C CG2 . ILE A 291 ? 1.21378 0.91506 1.04665 -0.17288 0.11082  0.00825  314 ILE A CG2 
2051 C CD1 . ILE A 291 ? 0.80816 0.51149 0.63234 -0.16487 0.10918  0.00739  314 ILE A CD1 
2052 N N   . LEU A 292 ? 0.88619 0.59347 0.72185 -0.18382 0.11553  0.01155  315 LEU A N   
2053 C CA  . LEU A 292 ? 0.74500 0.45188 0.58526 -0.18746 0.11626  0.01134  315 LEU A CA  
2054 C C   . LEU A 292 ? 0.86746 0.56928 0.70997 -0.19230 0.11655  0.01732  315 LEU A C   
2055 O O   . LEU A 292 ? 1.01422 0.71057 0.86099 -0.19447 0.11568  0.01945  315 LEU A O   
2056 C CB  . LEU A 292 ? 0.61797 0.33314 0.45815 -0.18799 0.11816  0.00684  315 LEU A CB  
2057 C CG  . LEU A 292 ? 0.60584 0.32591 0.44567 -0.18378 0.11783  0.00094  315 LEU A CG  
2058 C CD1 . LEU A 292 ? 0.76520 0.49319 0.60540 -0.18467 0.11969  -0.00309 315 LEU A CD1 
2059 C CD2 . LEU A 292 ? 0.58341 0.29937 0.42690 -0.18299 0.11645  0.00016  315 LEU A CD2 
2060 N N   . ILE A 293 ? 0.80725 0.51091 0.64724 -0.19407 0.11768  0.02028  316 ILE A N   
2061 C CA  . ILE A 293 ? 0.80940 0.50898 0.65159 -0.19874 0.11808  0.02647  316 ILE A CA  
2062 C C   . ILE A 293 ? 0.80965 0.50079 0.65263 -0.19827 0.11609  0.03128  316 ILE A C   
2063 O O   . ILE A 293 ? 0.93005 0.61557 0.77737 -0.20143 0.11543  0.03518  316 ILE A O   
2064 C CB  . ILE A 293 ? 0.92911 0.63364 0.76840 -0.20064 0.11988  0.02845  316 ILE A CB  
2065 C CG1 . ILE A 293 ? 0.74625 0.45885 0.58552 -0.20168 0.12180  0.02392  316 ILE A CG1 
2066 C CG2 . ILE A 293 ? 1.02235 0.72276 0.86408 -0.20546 0.12027  0.03568  316 ILE A CG2 
2067 C CD1 . ILE A 293 ? 0.98223 0.70105 0.81770 -0.20166 0.12321  0.02372  316 ILE A CD1 
2068 N N   . HIS A 294 ? 0.91187 0.60192 0.75094 -0.19429 0.11499  0.03105  317 HIS A N   
2069 C CA  . HIS A 294 ? 1.04729 0.72979 0.88639 -0.19379 0.11324  0.03602  317 HIS A CA  
2070 C C   . HIS A 294 ? 0.91827 0.59585 0.75832 -0.19024 0.11095  0.03407  317 HIS A C   
2071 O O   . HIS A 294 ? 0.96936 0.63987 0.81049 -0.19020 0.10929  0.03819  317 HIS A O   
2072 C CB  . HIS A 294 ? 0.89362 0.57753 0.72766 -0.19216 0.11354  0.03830  317 HIS A CB  
2073 C CG  . HIS A 294 ? 0.84286 0.53162 0.67581 -0.19553 0.11568  0.04075  317 HIS A CG  
2074 N ND1 . HIS A 294 ? 0.97763 0.67444 0.80899 -0.19555 0.11742  0.03647  317 HIS A ND1 
2075 C CD2 . HIS A 294 ? 0.98977 0.67679 0.82320 -0.19897 0.11635  0.04714  317 HIS A CD2 
2076 C CE1 . HIS A 294 ? 1.11691 0.81672 0.94774 -0.19889 0.11906  0.03994  317 HIS A CE1 
2077 N NE2 . HIS A 294 ? 1.31641 1.01059 1.14844 -0.20102 0.11852  0.04655  317 HIS A NE2 
2078 N N   . GLY A 295 ? 1.09150 0.56559 0.99409 0.03253  -0.00452 0.01611  318 GLY A N   
2079 C CA  . GLY A 295 ? 0.88607 0.37309 0.80325 0.03893  -0.00480 0.01990  318 GLY A CA  
2080 C C   . GLY A 295 ? 1.13109 0.63362 1.05814 0.03386  -0.00917 0.02032  318 GLY A C   
2081 O O   . GLY A 295 ? 1.33332 0.83730 1.25613 0.02534  -0.01249 0.01784  318 GLY A O   
2082 N N   . ASP A 296 ? 1.11778 0.63221 1.05850 0.03946  -0.00910 0.02360  319 ASP A N   
2083 C CA  . ASP A 296 ? 1.13287 0.66328 1.08527 0.03605  -0.01269 0.02452  319 ASP A CA  
2084 C C   . ASP A 296 ? 1.23538 0.77380 1.18770 0.04020  -0.02100 0.02913  319 ASP A C   
2085 O O   . ASP A 296 ? 1.36440 0.90962 1.32440 0.04860  -0.02211 0.03341  319 ASP A O   
2086 C CB  . ASP A 296 ? 0.88137 0.41991 0.84884 0.03950  -0.00741 0.02522  319 ASP A CB  
2087 C CG  . ASP A 296 ? 1.01416 0.56777 0.99346 0.03411  -0.00967 0.02493  319 ASP A CG  
2088 O OD1 . ASP A 296 ? 1.22841 0.79143 1.20926 0.03346  -0.01685 0.02735  319 ASP A OD1 
2089 O OD2 . ASP A 296 ? 0.94120 0.49723 0.92823 0.03048  -0.00431 0.02226  319 ASP A OD2 
2090 N N   . ILE A 297 ? 1.13327 0.67099 1.07685 0.03420  -0.02693 0.02820  320 ILE A N   
2091 C CA  . ILE A 297 ? 1.18275 0.72789 1.12528 0.03686  -0.03530 0.03215  320 ILE A CA  
2092 C C   . ILE A 297 ? 1.33798 0.89650 1.28777 0.02973  -0.03974 0.03148  320 ILE A C   
2093 O O   . ILE A 297 ? 1.23442 0.79067 1.18007 0.02044  -0.03942 0.02738  320 ILE A O   
2094 C CB  . ILE A 297 ? 1.25927 0.79289 1.18536 0.03591  -0.03913 0.03190  320 ILE A CB  
2095 C CG1 . ILE A 297 ? 1.33882 0.85651 1.25589 0.03963  -0.03325 0.03057  320 ILE A CG1 
2096 C CG2 . ILE A 297 ? 1.33996 0.87950 1.26525 0.04196  -0.04665 0.03690  320 ILE A CG2 
2097 C CD1 . ILE A 297 ? 1.04059 0.54536 0.94086 0.03549  -0.03538 0.02847  320 ILE A CD1 
2098 N N   . ARG A 298 ? 1.47903 1.05147 1.43969 0.03402  -0.04383 0.03544  321 ARG A N   
2099 C CA  . ARG A 298 ? 1.12459 0.71082 1.09399 0.02795  -0.04760 0.03503  321 ARG A CA  
2100 C C   . ARG A 298 ? 1.19333 0.78712 1.16065 0.02878  -0.05671 0.03835  321 ARG A C   
2101 O O   . ARG A 298 ? 1.44881 1.04164 1.41338 0.03654  -0.05989 0.04229  321 ARG A O   
2102 C CB  . ARG A 298 ? 1.16860 0.76706 1.15495 0.03147  -0.04449 0.03665  321 ARG A CB  
2103 C CG  . ARG A 298 ? 1.06889 0.67110 1.06279 0.02396  -0.03975 0.03267  321 ARG A CG  
2104 C CD  . ARG A 298 ? 1.03524 0.62749 1.02910 0.02577  -0.03085 0.03031  321 ARG A CD  
2105 N NE  . ARG A 298 ? 0.95752 0.54940 0.95431 0.01714  -0.02628 0.02556  321 ARG A NE  
2106 C CZ  . ARG A 298 ? 1.10762 0.70940 1.11804 0.01598  -0.02310 0.02515  321 ARG A CZ  
2107 N NH1 . ARG A 298 ? 1.28578 0.89896 1.30848 0.02273  -0.02390 0.02913  321 ARG A NH1 
2108 N NH2 . ARG A 298 ? 0.95161 0.55191 0.96340 0.00779  -0.01906 0.02062  321 ARG A NH2 
2109 N N   . LYS A 299 ? 1.23748 0.83889 1.20626 0.02066  -0.06091 0.03669  322 LYS A N   
2110 C CA  . LYS A 299 ? 1.41933 1.03029 1.38837 0.02046  -0.06959 0.03959  322 LYS A CA  
2111 C C   . LYS A 299 ? 1.19613 0.82250 1.17866 0.01591  -0.07105 0.03926  322 LYS A C   
2112 O O   . LYS A 299 ? 1.19530 0.82182 1.18058 0.00853  -0.06730 0.03526  322 LYS A O   
2113 C CB  . LYS A 299 ? 1.44691 1.04972 1.40080 0.01449  -0.07431 0.03773  322 LYS A CB  
2114 C CG  . LYS A 299 ? 1.18949 0.79615 1.14256 0.00339  -0.07639 0.03393  322 LYS A CG  
2115 C CD  . LYS A 299 ? 1.42252 1.02709 1.36407 -0.00008 -0.08397 0.03430  322 LYS A CD  
2116 C CE  . LYS A 299 ? 1.27876 0.88048 1.21412 -0.01140 -0.08447 0.02945  322 LYS A CE  
2117 N NZ  . LYS A 299 ? 1.24580 0.83214 1.17109 -0.01471 -0.07828 0.02528  322 LYS A NZ  
2118 N N   . THR A 300 ? 1.37311 1.01246 1.36436 0.02034  -0.07631 0.04342  323 THR A N   
2119 C CA  . THR A 300 ? 1.32966 0.98408 1.33371 0.01605  -0.07816 0.04328  323 THR A CA  
2120 C C   . THR A 300 ? 1.43880 1.09653 1.43722 0.00762  -0.08476 0.04168  323 THR A C   
2121 O O   . THR A 300 ? 1.65633 1.31532 1.64890 0.00955  -0.09160 0.04429  323 THR A O   
2122 C CB  . THR A 300 ? 1.51604 1.18347 1.53246 0.02427  -0.08086 0.04833  323 THR A CB  
2123 O OG1 . THR A 300 ? 1.85348 1.52236 1.86395 0.02812  -0.08839 0.05188  323 THR A OG1 
2124 C CG2 . THR A 300 ? 1.49433 1.15814 1.51583 0.03293  -0.07445 0.05001  323 THR A CG2 
2125 N N   . THR A 301 ? 1.42822 1.08733 1.42829 -0.00168 -0.08283 0.03743  324 THR A N   
2126 C CA  . THR A 301 ? 1.38675 1.05211 1.38479 -0.00975 -0.08906 0.03607  324 THR A CA  
2127 C C   . THR A 301 ? 1.43158 1.11275 1.44498 -0.01274 -0.08975 0.03620  324 THR A C   
2128 O O   . THR A 301 ? 1.40373 1.08716 1.42631 -0.01337 -0.08359 0.03462  324 THR A O   
2129 C CB  . THR A 301 ? 1.22932 0.88347 1.21551 -0.01895 -0.08732 0.03089  324 THR A CB  
2130 O OG1 . THR A 301 ? 1.03451 0.69076 1.02797 -0.02504 -0.08176 0.02709  324 THR A OG1 
2131 C CG2 . THR A 301 ? 1.08256 0.71994 1.05558 -0.01573 -0.08381 0.03009  324 THR A CG2 
2132 N N   . LYS A 302 ? 1.41065 1.10272 1.42684 -0.01468 -0.09725 0.03804  325 LYS A N   
2133 C CA  . LYS A 302 ? 1.41407 1.12176 1.44471 -0.01749 -0.09867 0.03840  325 LYS A CA  
2134 C C   . LYS A 302 ? 1.49197 1.20184 1.51898 -0.02836 -0.10212 0.03479  325 LYS A C   
2135 O O   . LYS A 302 ? 1.42207 1.12632 1.43706 -0.03154 -0.10692 0.03415  325 LYS A O   
2136 C CB  . LYS A 302 ? 1.36978 1.09019 1.40933 -0.01002 -0.10410 0.04381  325 LYS A CB  
2137 C CG  . LYS A 302 ? 1.44056 1.16574 1.47488 -0.00979 -0.11341 0.04646  325 LYS A CG  
2138 C CD  . LYS A 302 ? 1.38295 1.11661 1.41895 -0.01901 -0.11840 0.04440  325 LYS A CD  
2139 C CE  . LYS A 302 ? 1.29590 1.03480 1.32746 -0.01800 -0.12761 0.04737  325 LYS A CE  
2140 N NZ  . LYS A 302 ? 1.35014 1.10010 1.38635 -0.02592 -0.13266 0.04601  325 LYS A NZ  
2141 N N   . LEU A 303 ? 1.45546 1.17304 1.49254 -0.03415 -0.09951 0.03233  326 LEU A N   
2142 C CA  . LEU A 303 ? 1.47984 1.19915 1.51422 -0.04488 -0.10179 0.02841  326 LEU A CA  
2143 C C   . LEU A 303 ? 1.56822 1.30489 1.61556 -0.04690 -0.10649 0.03001  326 LEU A C   
2144 O O   . LEU A 303 ? 1.65092 1.39619 1.71164 -0.04644 -0.10289 0.03009  326 LEU A O   
2145 C CB  . LEU A 303 ? 1.38203 1.09391 1.41586 -0.05105 -0.09425 0.02341  326 LEU A CB  
2146 N N   . ASN A 304 ? 1.58148 1.32320 1.62482 -0.04931 -0.11447 0.03121  327 ASN A N   
2147 C CA  . ASN A 304 ? 1.63771 1.39582 1.69246 -0.05139 -0.11968 0.03279  327 ASN A CA  
2148 C C   . ASN A 304 ? 1.48285 1.24350 1.53644 -0.06262 -0.12139 0.02853  327 ASN A C   
2149 O O   . ASN A 304 ? 1.55507 1.30513 1.59616 -0.06844 -0.12140 0.02518  327 ASN A O   
2150 C CB  . ASN A 304 ? 1.43510 1.19872 1.48759 -0.04624 -0.12780 0.03726  327 ASN A CB  
2151 N N   . THR A 308 ? 1.45516 1.25731 1.56329 -0.07372 -0.11132 0.02494  331 THR A N   
2152 C CA  . THR A 308 ? 1.71820 1.51937 1.83210 -0.06422 -0.10652 0.02794  331 THR A CA  
2153 C C   . THR A 308 ? 1.79624 1.58481 1.89731 -0.05779 -0.10672 0.02967  331 THR A C   
2154 O O   . THR A 308 ? 1.73608 1.51311 1.82320 -0.06172 -0.10752 0.02718  331 THR A O   
2155 C CB  . THR A 308 ? 1.43918 1.23672 1.55905 -0.06587 -0.09754 0.02503  331 THR A CB  
2156 N N   . GLU A 309 ? 1.82616 1.61703 1.93203 -0.04787 -0.10603 0.03395  332 GLU A N   
2157 C CA  . GLU A 309 ? 1.64773 1.42756 1.74283 -0.04071 -0.10611 0.03608  332 GLU A CA  
2158 C C   . GLU A 309 ? 1.72635 1.49867 1.82376 -0.03527 -0.09765 0.03591  332 GLU A C   
2159 O O   . GLU A 309 ? 1.68075 1.46113 1.79062 -0.02964 -0.09499 0.03839  332 GLU A O   
2160 C CB  . GLU A 309 ? 1.49116 1.27924 1.58889 -0.03324 -0.11277 0.04137  332 GLU A CB  
2161 N N   . ILE A 310 ? 1.74397 1.50089 1.82937 -0.03695 -0.09345 0.03298  333 ILE A N   
2162 C CA  . ILE A 310 ? 1.60905 1.35713 1.69496 -0.03248 -0.08524 0.03230  333 ILE A CA  
2163 C C   . ILE A 310 ? 1.48601 1.22070 1.55867 -0.02662 -0.08525 0.03364  333 ILE A C   
2164 O O   . ILE A 310 ? 1.46269 1.19119 1.52305 -0.02923 -0.08994 0.03309  333 ILE A O   
2165 C CB  . ILE A 310 ? 1.63760 1.37933 1.72261 -0.04050 -0.07884 0.02694  333 ILE A CB  
2166 C CG1 . ILE A 310 ? 1.58549 1.32202 1.65937 -0.05011 -0.08238 0.02318  333 ILE A CG1 
2167 C CG2 . ILE A 310 ? 1.49308 1.24718 1.59417 -0.04279 -0.07594 0.02642  333 ILE A CG2 
2168 C CD1 . ILE A 310 ? 1.37263 1.09811 1.44080 -0.05691 -0.07602 0.01788  333 ILE A CD1 
2169 N N   . GLU A 311 ? 1.42590 1.15604 1.50107 -0.01871 -0.07989 0.03537  334 GLU A N   
2170 C CA  . GLU A 311 ? 1.33676 1.05399 1.40039 -0.01249 -0.07899 0.03668  334 GLU A CA  
2171 C C   . GLU A 311 ? 1.32944 1.03374 1.38886 -0.01306 -0.07042 0.03337  334 GLU A C   
2172 O O   . GLU A 311 ? 1.27643 0.98383 1.34583 -0.01280 -0.06444 0.03236  334 GLU A O   
2173 C CB  . GLU A 311 ? 1.24032 0.96302 1.30957 -0.00145 -0.08092 0.04217  334 GLU A CB  
2174 C CG  . GLU A 311 ? 1.38677 1.09697 1.44942 0.00626  -0.07628 0.04325  334 GLU A CG  
2175 C CD  . GLU A 311 ? 1.51012 1.22592 1.57814 0.01705  -0.07858 0.04868  334 GLU A CD  
2176 O OE1 . GLU A 311 ? 1.46977 1.17570 1.53161 0.02387  -0.07599 0.05006  334 GLU A OE1 
2177 O OE2 . GLU A 311 ? 1.54459 1.27460 1.62286 0.01871  -0.08307 0.05156  334 GLU A OE2 
2178 N N   . VAL A 312 ? 1.32786 1.01763 1.37238 -0.01376 -0.06991 0.03173  335 VAL A N   
2179 C CA  . VAL A 312 ? 1.03668 0.71244 1.07477 -0.01467 -0.06229 0.02836  335 VAL A CA  
2180 C C   . VAL A 312 ? 1.06078 0.72419 1.08704 -0.00789 -0.06236 0.03017  335 VAL A C   
2181 O O   . VAL A 312 ? 1.24036 0.90199 1.25788 -0.00711 -0.06863 0.03187  335 VAL A O   
2182 C CB  . VAL A 312 ? 0.97984 0.64912 1.01081 -0.02567 -0.06073 0.02280  335 VAL A CB  
2183 C CG1 . VAL A 312 ? 1.05232 0.73465 1.09380 -0.03294 -0.06252 0.02126  335 VAL A CG1 
2184 C CG2 . VAL A 312 ? 1.06455 0.72440 1.07947 -0.02906 -0.06550 0.02170  335 VAL A CG2 
2185 N N   . GLU A 313 ? 0.99048 0.64583 1.01703 -0.00265 -0.05544 0.03001  336 GLU A N   
2186 C CA  . GLU A 313 ? 1.20168 0.84425 1.21722 0.00377  -0.05441 0.03136  336 GLU A CA  
2187 C C   . GLU A 313 ? 1.12162 0.74900 1.12422 -0.00235 -0.05063 0.02660  336 GLU A C   
2188 O O   . GLU A 313 ? 0.90802 0.52885 0.91174 -0.00357 -0.04332 0.02372  336 GLU A O   
2189 C CB  . GLU A 313 ? 0.93614 0.57876 0.95921 0.01354  -0.04944 0.03419  336 GLU A CB  
2190 C CG  . GLU A 313 ? 1.24569 0.89013 1.26753 0.02320  -0.05401 0.03944  336 GLU A CG  
2191 C CD  . GLU A 313 ? 1.46992 1.11402 1.49902 0.03278  -0.04888 0.04207  336 GLU A CD  
2192 O OE1 . GLU A 313 ? 1.70619 1.34492 1.72998 0.04067  -0.05012 0.04513  336 GLU A OE1 
2193 O OE2 . GLU A 313 ? 1.40498 1.05491 1.44557 0.03255  -0.04388 0.04125  336 GLU A OE2 
2194 N N   . THR A 314 ? 1.15114 0.77295 1.14127 -0.00597 -0.05585 0.02593  337 THR A N   
2195 C CA  . THR A 314 ? 0.97388 0.58135 0.95013 -0.01189 -0.05367 0.02171  337 THR A CA  
2196 C C   . THR A 314 ? 1.08224 0.67551 1.04962 -0.00534 -0.04950 0.02224  337 THR A C   
2197 O O   . THR A 314 ? 1.13678 0.72957 1.10275 0.00303  -0.05190 0.02634  337 THR A O   
2198 C CB  . THR A 314 ? 0.92432 0.53176 0.89077 -0.01754 -0.06123 0.02124  337 THR A CB  
2199 O OG1 . THR A 314 ? 1.15759 0.77926 1.13308 -0.02274 -0.06560 0.02128  337 THR A OG1 
2200 C CG2 . THR A 314 ? 0.94179 0.53474 0.89370 -0.02460 -0.05918 0.01655  337 THR A CG2 
2201 N N   . LEU A 315 ? 1.02785 0.60952 0.98934 -0.00928 -0.04318 0.01800  338 LEU A N   
2202 C CA  . LEU A 315 ? 0.98340 0.54975 0.93411 -0.00490 -0.03931 0.01757  338 LEU A CA  
2203 C C   . LEU A 315 ? 0.99150 0.54869 0.92646 -0.00776 -0.04411 0.01689  338 LEU A C   
2204 O O   . LEU A 315 ? 1.06739 0.62401 0.99687 -0.01653 -0.04665 0.01380  338 LEU A O   
2205 C CB  . LEU A 315 ? 0.80056 0.35806 0.75105 -0.00818 -0.03072 0.01319  338 LEU A CB  
2206 C CG  . LEU A 315 ? 1.15271 0.71623 1.11730 -0.00370 -0.02474 0.01403  338 LEU A CG  
2207 C CD1 . LEU A 315 ? 0.98145 0.54067 0.94784 -0.01057 -0.01795 0.00900  338 LEU A CD1 
2208 C CD2 . LEU A 315 ? 1.04840 0.60538 1.01196 0.00677  -0.02156 0.01703  338 LEU A CD2 
2209 N N   . VAL A 316 ? 1.18008 0.73007 1.10782 -0.00024 -0.04527 0.01981  339 VAL A N   
2210 C CA  . VAL A 316 ? 1.26383 0.80467 1.17649 -0.00161 -0.04978 0.01974  339 VAL A CA  
2211 C C   . VAL A 316 ? 1.28444 0.80908 1.18709 0.00183  -0.04432 0.01845  339 VAL A C   
2212 O O   . VAL A 316 ? 1.14433 0.66574 1.05224 0.00558  -0.03752 0.01790  339 VAL A O   
2213 C CB  . VAL A 316 ? 1.31921 0.86701 1.23181 0.00430  -0.05752 0.02488  339 VAL A CB  
2214 C CG1 . VAL A 316 ? 1.26914 0.83226 1.19010 0.00005  -0.06349 0.02585  339 VAL A CG1 
2215 C CG2 . VAL A 316 ? 1.28092 0.83069 1.20041 0.01546  -0.05562 0.02918  339 VAL A CG2 
2216 N N   . GLU A 317 ? 1.43580 0.95015 1.32393 0.00043  -0.04726 0.01790  340 GLU A N   
2217 C CA  . GLU A 317 ? 1.42413 0.92228 1.30131 0.00223  -0.04231 0.01605  340 GLU A CA  
2218 C C   . GLU A 317 ? 1.50578 0.99848 1.37838 0.01221  -0.04352 0.02020  340 GLU A C   
2219 O O   . GLU A 317 ? 1.54455 1.02651 1.41340 0.01643  -0.03788 0.01955  340 GLU A O   
2220 C CB  . GLU A 317 ? 1.34403 0.83308 1.20719 -0.00630 -0.04429 0.01232  340 GLU A CB  
2221 C CG  . GLU A 317 ? 1.53386 1.02269 1.39853 -0.01613 -0.04066 0.00706  340 GLU A CG  
2222 C CD  . GLU A 317 ? 1.67353 1.15370 1.52421 -0.02435 -0.04302 0.00356  340 GLU A CD  
2223 O OE1 . GLU A 317 ? 1.59076 1.07596 1.44301 -0.03303 -0.04440 0.00057  340 GLU A OE1 
2224 O OE2 . GLU A 317 ? 1.90430 1.37284 1.74248 -0.02214 -0.04360 0.00383  340 GLU A OE2 
2225 N N   . ASP A 318 ? 1.35038 0.85009 1.22318 0.01615  -0.05068 0.02441  341 ASP A N   
2226 C CA  . ASP A 318 ? 1.59618 1.09059 1.46376 0.02531  -0.05251 0.02838  341 ASP A CA  
2227 C C   . ASP A 318 ? 1.62715 1.13536 1.50520 0.03193  -0.05753 0.03354  341 ASP A C   
2228 O O   . ASP A 318 ? 1.66116 1.18237 1.54784 0.02846  -0.06112 0.03403  341 ASP A O   
2229 C CB  . ASP A 318 ? 1.64805 1.13213 1.49937 0.02290  -0.05676 0.02789  341 ASP A CB  
2230 C CG  . ASP A 318 ? 1.61395 1.10652 1.46352 0.01796  -0.06498 0.02880  341 ASP A CG  
2231 O OD1 . ASP A 318 ? 1.69140 1.19372 1.54847 0.01160  -0.06590 0.02705  341 ASP A OD1 
2232 O OD2 . ASP A 318 ? 1.34949 0.83885 1.19011 0.02036  -0.07049 0.03121  341 ASP A OD2 
2233 N N   . GLU A 319 ? 1.53389 1.03913 1.41111 0.04160  -0.05779 0.03739  342 GLU A N   
2234 C CA  . GLU A 319 ? 1.58857 1.10622 1.47625 0.04899  -0.06171 0.04240  342 GLU A CA  
2235 C C   . GLU A 319 ? 1.69312 1.21739 1.57724 0.04807  -0.07087 0.04509  342 GLU A C   
2236 O O   . GLU A 319 ? 1.54847 1.08430 1.44145 0.05330  -0.07494 0.04914  342 GLU A O   
2237 C CB  . GLU A 319 ? 1.29095 0.80293 1.17877 0.05976  -0.05887 0.04558  342 GLU A CB  
2238 N N   . ALA A 320 ? 1.97684 1.49418 1.84830 0.04160  -0.07421 0.04293  343 ALA A N   
2239 C CA  . ALA A 320 ? 2.09905 1.62305 1.96718 0.03945  -0.08291 0.04497  343 ALA A CA  
2240 C C   . ALA A 320 ? 1.93114 1.47080 1.81082 0.03463  -0.08604 0.04489  343 ALA A C   
2241 O O   . ALA A 320 ? 1.82870 1.37617 1.70804 0.03363  -0.09343 0.04706  343 ALA A O   
2242 C CB  . ALA A 320 ? 2.12139 1.63444 1.97373 0.03259  -0.08512 0.04209  343 ALA A CB  
2243 N N   . GLU A 321 ? 1.78746 1.33179 1.67723 0.03159  -0.08065 0.04242  344 GLU A N   
2244 C CA  . GLU A 321 ? 1.85121 1.41075 1.75343 0.02762  -0.08282 0.04240  344 GLU A CA  
2245 C C   . GLU A 321 ? 1.85333 1.42024 1.77000 0.03428  -0.07827 0.04440  344 GLU A C   
2246 O O   . GLU A 321 ? 1.72527 1.28599 1.64396 0.03494  -0.07080 0.04219  344 GLU A O   
2247 C CB  . GLU A 321 ? 1.79660 1.35496 1.69711 0.01652  -0.08073 0.03713  344 GLU A CB  
2248 C CG  . GLU A 321 ? 1.69947 1.25615 1.58918 0.00931  -0.08713 0.03577  344 GLU A CG  
2249 C CD  . GLU A 321 ? 1.78044 1.35031 1.67781 0.00214  -0.09110 0.03473  344 GLU A CD  
2250 O OE1 . GLU A 321 ? 1.85085 1.43424 1.76080 0.00557  -0.09338 0.03771  344 GLU A OE1 
2251 O OE2 . GLU A 321 ? 1.74772 1.31443 1.63846 -0.00692 -0.09199 0.03093  344 GLU A OE2 
2252 N N   . ALA A 322 ? 1.97135 1.55146 1.89800 0.03917  -0.08278 0.04855  345 ALA A N   
2253 C CA  . ALA A 322 ? 1.90471 1.49502 1.84690 0.04411  -0.07943 0.05038  345 ALA A CA  
2254 C C   . ALA A 322 ? 1.92771 1.53450 1.87990 0.04480  -0.08605 0.05358  345 ALA A C   
2255 O O   . ALA A 322 ? 2.05191 1.66797 2.01553 0.05170  -0.08591 0.05700  345 ALA A O   
2256 C CB  . ALA A 322 ? 2.01926 1.60388 1.96212 0.05465  -0.07580 0.05329  345 ALA A CB  
2257 N N   . GLY A 323 ? 1.83581 1.44621 1.78364 0.03758  -0.09184 0.05242  346 GLY A N   
2258 C CA  . GLY A 323 ? 1.98507 1.60905 1.93878 0.03813  -0.09951 0.05560  346 GLY A CA  
2259 C C   . GLY A 323 ? 1.95757 1.59540 1.92509 0.03342  -0.09906 0.05451  346 GLY A C   
2260 O O   . GLY A 323 ? 1.77755 1.41640 1.75314 0.03264  -0.09253 0.05258  346 GLY A O   
2261 N N   . ALA A 324 ? 1.92391 1.57249 1.89409 0.03014  -0.10619 0.05575  347 ALA A N   
2262 C CA  . ALA A 324 ? 1.65983 1.32270 1.64302 0.02551  -0.10700 0.05504  347 ALA A CA  
2263 C C   . ALA A 324 ? 1.74821 1.41167 1.72418 0.01588  -0.11213 0.05241  347 ALA A C   
2264 O O   . ALA A 324 ? 1.88623 1.55605 1.86051 0.01569  -0.11969 0.05468  347 ALA A O   
2265 C CB  . ALA A 324 ? 1.71936 1.39668 1.71491 0.03246  -0.11096 0.05990  347 ALA A CB  
2266 N N   . VAL A 325 ? 1.82148 1.47806 1.79326 0.00791  -0.10772 0.04750  348 VAL A N   
2267 C CA  . VAL A 325 ? 1.83287 1.48864 1.79780 -0.00214 -0.11106 0.04409  348 VAL A CA  
2268 C C   . VAL A 325 ? 1.85542 1.52442 1.83309 -0.00808 -0.11105 0.04251  348 VAL A C   
2269 O O   . VAL A 325 ? 1.84137 1.51701 1.83158 -0.00548 -0.10662 0.04298  348 VAL A O   
2270 C CB  . VAL A 325 ? 1.65165 1.29125 1.60408 -0.00703 -0.10590 0.03958  348 VAL A CB  
2271 C CG1 . VAL A 325 ? 1.53458 1.17188 1.47831 -0.01705 -0.10942 0.03609  348 VAL A CG1 
2272 C CG2 . VAL A 325 ? 1.85857 1.48546 1.79991 -0.00009 -0.10520 0.04144  348 VAL A CG2 
2273 N N   . SER A 326 ? 1.87728 1.55078 1.85206 -0.01593 -0.11637 0.04085  349 SER A N   
2274 C CA  . SER A 326 ? 1.83797 1.52299 1.82364 -0.02265 -0.11634 0.03881  349 SER A CA  
2275 C C   . SER A 326 ? 1.87546 1.55595 1.85328 -0.03369 -0.11692 0.03391  349 SER A C   
2276 O O   . SER A 326 ? 1.97795 1.64566 1.94169 -0.03622 -0.11676 0.03188  349 SER A O   
2277 C CB  . SER A 326 ? 1.79480 1.49552 1.78979 -0.02038 -0.12342 0.04263  349 SER A CB  
2278 O OG  . SER A 326 ? 1.75679 1.46069 1.75659 -0.00989 -0.12413 0.04745  349 SER A OG  
2279 N N   . SER A 327 ? 1.77411 1.46510 1.76106 -0.04030 -0.11761 0.03200  350 SER A N   
2280 C CA  . SER A 327 ? 1.76974 1.45804 1.75057 -0.05105 -0.11850 0.02738  350 SER A CA  
2281 C C   . SER A 327 ? 1.67645 1.37963 1.66936 -0.05670 -0.12102 0.02664  350 SER A C   
2282 O O   . SER A 327 ? 1.70642 1.41585 1.71140 -0.05695 -0.11632 0.02586  350 SER A O   
2283 C CB  . SER A 327 ? 1.57835 1.25412 1.55391 -0.05499 -0.11054 0.02280  350 SER A CB  
2284 O OG  . SER A 327 ? 1.31604 0.97688 1.27582 -0.05460 -0.11030 0.02182  350 SER A OG  
2285 N N   . GLU A 328 ? 1.56890 1.27773 1.55855 -0.06126 -0.12846 0.02685  351 GLU A N   
2286 C CA  . GLU A 328 ? 1.57385 1.29676 1.57399 -0.06697 -0.13169 0.02615  351 GLU A CA  
2287 C C   . GLU A 328 ? 1.66208 1.38150 1.66022 -0.07735 -0.12839 0.02056  351 GLU A C   
2288 O O   . GLU A 328 ? 1.65920 1.36749 1.64412 -0.08245 -0.12844 0.01750  351 GLU A O   
2289 C CB  . GLU A 328 ? 1.53956 1.26994 1.53699 -0.06754 -0.14110 0.02868  351 GLU A CB  
2290 C CG  . GLU A 328 ? 1.49033 1.22857 1.49372 -0.05775 -0.14508 0.03444  351 GLU A CG  
2291 C CD  . GLU A 328 ? 1.65168 1.37867 1.64519 -0.04981 -0.14445 0.03695  351 GLU A CD  
2292 O OE1 . GLU A 328 ? 1.62086 1.34964 1.60983 -0.04586 -0.15091 0.04033  351 GLU A OE1 
2293 O OE2 . GLU A 328 ? 1.82298 1.53954 1.81347 -0.04736 -0.13757 0.03563  351 GLU A OE2 
2294 N N   . ASP A 329 ? 1.86608 1.59501 1.87733 -0.08044 -0.12550 0.01924  352 ASP A N   
2295 C CA  . ASP A 329 ? 1.82975 1.55651 1.84072 -0.09019 -0.12215 0.01399  352 ASP A CA  
2296 C C   . ASP A 329 ? 1.77593 1.51353 1.79013 -0.09766 -0.12850 0.01298  352 ASP A C   
2297 O O   . ASP A 329 ? 1.70391 1.43672 1.70727 -0.10373 -0.13237 0.01079  352 ASP A O   
2298 C CB  . ASP A 329 ? 1.73697 1.46652 1.76000 -0.08950 -0.11446 0.01274  352 ASP A CB  
2299 C CG  . ASP A 329 ? 1.83344 1.55289 1.85422 -0.08197 -0.10799 0.01376  352 ASP A CG  
2300 O OD1 . ASP A 329 ? 1.86297 1.56954 1.87032 -0.08025 -0.10775 0.01343  352 ASP A OD1 
2301 O OD2 . ASP A 329 ? 1.75074 1.47516 1.78321 -0.07772 -0.10318 0.01492  352 ASP A OD2 
2428 C C1  . RET K .   ? 0.71063 0.55663 0.55200 -0.07836 0.07583  -0.03296 410 RET A C1  
2429 C C2  . RET K .   ? 0.70343 0.55333 0.54899 -0.07409 0.07245  -0.03110 410 RET A C2  
2430 C C3  . RET K .   ? 0.70358 0.54758 0.54437 -0.07204 0.07160  -0.02933 410 RET A C3  
2431 C C4  . RET K .   ? 0.70713 0.54008 0.53748 -0.07522 0.07459  -0.02974 410 RET A C4  
2432 C C5  . RET K .   ? 0.69412 0.52254 0.51955 -0.08007 0.07827  -0.03169 410 RET A C5  
2433 C C6  . RET K .   ? 0.83955 0.67387 0.66999 -0.08136 0.07877  -0.03310 410 RET A C6  
2434 C C7  . RET K .   ? 0.84354 0.67254 0.66842 -0.08599 0.08242  -0.03489 410 RET A C7  
2435 C C8  . RET K .   ? 0.80355 0.63616 0.63128 -0.08808 0.08371  -0.03652 410 RET A C8  
2436 C C9  . RET K .   ? 0.76346 0.58994 0.58487 -0.09276 0.08743  -0.03822 410 RET A C9  
2437 C C10 . RET K .   ? 0.77831 0.60991 0.60398 -0.09429 0.08826  -0.03984 410 RET A C10 
2438 C C11 . RET K .   ? 0.60662 0.43382 0.42752 -0.09883 0.09176  -0.04171 410 RET A C11 
2439 C C12 . RET K .   ? 0.63471 0.46789 0.46073 -0.09984 0.09223  -0.04327 410 RET A C12 
2440 C C13 . RET K .   ? 0.69788 0.52850 0.52159 -0.10399 0.09508  -0.04465 410 RET A C13 
2441 C C14 . RET K .   ? 0.82974 0.66668 0.65824 -0.10447 0.09553  -0.04666 410 RET A C14 
2442 C C15 . RET K .   ? 0.63479 0.47135 0.46344 -0.10795 0.09773  -0.04785 410 RET A C15 
2443 C C16 . RET K .   ? 0.53067 0.38087 0.37632 -0.07698 0.07493  -0.03279 410 RET A C16 
2444 C C17 . RET K .   ? 0.70975 0.56010 0.55421 -0.08083 0.07695  -0.03484 410 RET A C17 
2445 C C18 . RET K .   ? 0.54940 0.36590 0.36360 -0.08330 0.08134  -0.03189 410 RET A C18 
2446 C C19 . RET K .   ? 0.65618 0.47159 0.46802 -0.09546 0.08971  -0.03744 410 RET A C19 
2447 C C20 . RET K .   ? 0.61000 0.43248 0.42898 -0.10697 0.09640  -0.04246 410 RET A C20 
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