data_9HNF
# 
_entry.id   9HNF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9HNF         pdb_00009hnf 10.2210/pdb9hnf/pdb 
WWPDB D_1292142193 ?            ?                   
# 
_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       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HNF 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-10 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8RIP unspecified 
PDB . 8RIQ unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              toerb@mpi-marburg.mpg.de 
_pdbx_contact_author.name_first         Tobias 
_pdbx_contact_author.name_last          Erb 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3685-0894 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Marchal, D.G.' 1 0009-0002-1314-4583 
'Zarzycki, J.'  2 0000-0002-6307-6497 
'Erb, T.J.'     3 0000-0003-3685-0894 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3134 
_citation.page_last                 3134 
_citation.title                     
'Design and implementation of aerobic and ambient CO 2 -reduction as an entry-point for enhanced carbon fixation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57549-4 
_citation.pdbx_database_id_PubMed   40169551 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Satanowski, A.' 1  0000-0003-0775-4799 
primary 'Marchal, D.G.'  2  0009-0002-1314-4583 
primary 'Perret, A.'     3  ?                   
primary 'Petit, J.L.'    4  ?                   
primary 'Bouzon, M.'     5  0000-0002-9581-6584 
primary 'Doring, V.'     6  ?                   
primary 'Dubois, I.'     7  ?                   
primary 'He, H.'         8  0000-0003-1223-2813 
primary 'Smith, E.N.'    9  0000-0002-6628-323X 
primary 'Pellouin, V.'   10 ?                   
primary 'Petri, H.M.'    11 0009-0003-1147-4826 
primary 'Rainaldi, V.'   12 0000-0003-3921-368X 
primary 'Nattermann, M.' 13 ?                   
primary 'Burgener, S.'   14 0000-0003-3703-168X 
primary 'Paczia, N.'     15 0000-0003-3859-8186 
primary 'Zarzycki, J.'   16 0000-0002-6307-6497 
primary 'Heinemann, M.'  17 0000-0002-5512-9077 
primary 'Bar-Even, A.'   18 0000-0002-1039-4328 
primary 'Erb, T.J.'      19 0000-0003-3685-0894 
# 
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 '3-keto-5-aminohexanoate cleavage protein' 36428.133 2   ? ? ? ? 
2 non-polymer syn 'ACETYL COENZYME *A'                       809.571   2   ? ? ? ? 
3 non-polymer syn 'ACETOACETIC ACID'                         102.089   2   ? ? ? ? 
4 non-polymer syn 'ZINC ION'                                 65.409    2   ? ? ? ? 
5 water       nat water                                      18.015    253 ? ? ? ? 
# 
_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       
;MGHHHHHHHHHHSSGHIEGRHGSRMSLNGKVIITCAVTGAIHTPSMSPYLPVSASEITDAAIGAAEAGAAVIHLHARHEG
DGSPDQSVEAFNPILGVIKQASDAVLNITTGGAPTMSIAERIQPAQHYRPELASLNMGTMNFGLFPMLNRYESQLKHQWE
RNYLGNKDIIFRNTFGDVEHVMTTLGAGGTRFEFECYDTSHLYNLKHFYDRGLVKGPLFIQTVFGLMGGIGAHPDDVLHM
KRTADRLFGQDYRWSVLGAGRNQLNIAAMSAAMGGHVRVGLEDNLWAGKGRLAETNAQQVRAARQIVEGLGLEVATPAEA
RELLALKGGDQVNF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGHHHHHHHHHHSSGHIEGRHGSRMSLNGKVIITCAVTGAIHTPSMSPYLPVSASEITDAAIGAAEAGAAVIHLHARHEG
DGSPDQSVEAFNPILGVIKQASDAVLNITTGGAPTMSIAERIQPAQHYRPELASLNMGTMNFGLFPMLNRYESQLKHQWE
RNYLGNKDIIFRNTFGDVEHVMTTLGAGGTRFEFECYDTSHLYNLKHFYDRGLVKGPLFIQTVFGLMGGIGAHPDDVLHM
KRTADRLFGQDYRWSVLGAGRNQLNIAAMSAAMGGHVRVGLEDNLWAGKGRLAETNAQQVRAARQIVEGLGLEVATPAEA
RELLALKGGDQVNF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETYL COENZYME *A' ACO 
3 'ACETOACETIC ACID'   AAE 
4 'ZINC ION'           ZN  
5 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  HIS n 
1 12  HIS n 
1 13  SER n 
1 14  SER n 
1 15  GLY n 
1 16  HIS n 
1 17  ILE n 
1 18  GLU n 
1 19  GLY n 
1 20  ARG n 
1 21  HIS n 
1 22  GLY n 
1 23  SER n 
1 24  ARG n 
1 25  MET n 
1 26  SER n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LYS n 
1 31  VAL n 
1 32  ILE n 
1 33  ILE n 
1 34  THR n 
1 35  CYS n 
1 36  ALA n 
1 37  VAL n 
1 38  THR n 
1 39  GLY n 
1 40  ALA n 
1 41  ILE n 
1 42  HIS n 
1 43  THR n 
1 44  PRO n 
1 45  SER n 
1 46  MET n 
1 47  SER n 
1 48  PRO n 
1 49  TYR n 
1 50  LEU n 
1 51  PRO n 
1 52  VAL n 
1 53  SER n 
1 54  ALA n 
1 55  SER n 
1 56  GLU n 
1 57  ILE n 
1 58  THR n 
1 59  ASP n 
1 60  ALA n 
1 61  ALA n 
1 62  ILE n 
1 63  GLY n 
1 64  ALA n 
1 65  ALA n 
1 66  GLU n 
1 67  ALA n 
1 68  GLY n 
1 69  ALA n 
1 70  ALA n 
1 71  VAL n 
1 72  ILE n 
1 73  HIS n 
1 74  LEU n 
1 75  HIS n 
1 76  ALA n 
1 77  ARG n 
1 78  HIS n 
1 79  GLU n 
1 80  GLY n 
1 81  ASP n 
1 82  GLY n 
1 83  SER n 
1 84  PRO n 
1 85  ASP n 
1 86  GLN n 
1 87  SER n 
1 88  VAL n 
1 89  GLU n 
1 90  ALA n 
1 91  PHE n 
1 92  ASN n 
1 93  PRO n 
1 94  ILE n 
1 95  LEU n 
1 96  GLY n 
1 97  VAL n 
1 98  ILE n 
1 99  LYS n 
1 100 GLN n 
1 101 ALA n 
1 102 SER n 
1 103 ASP n 
1 104 ALA n 
1 105 VAL n 
1 106 LEU n 
1 107 ASN n 
1 108 ILE n 
1 109 THR n 
1 110 THR n 
1 111 GLY n 
1 112 GLY n 
1 113 ALA n 
1 114 PRO n 
1 115 THR n 
1 116 MET n 
1 117 SER n 
1 118 ILE n 
1 119 ALA n 
1 120 GLU n 
1 121 ARG n 
1 122 ILE n 
1 123 GLN n 
1 124 PRO n 
1 125 ALA n 
1 126 GLN n 
1 127 HIS n 
1 128 TYR n 
1 129 ARG n 
1 130 PRO n 
1 131 GLU n 
1 132 LEU n 
1 133 ALA n 
1 134 SER n 
1 135 LEU n 
1 136 ASN n 
1 137 MET n 
1 138 GLY n 
1 139 THR n 
1 140 MET n 
1 141 ASN n 
1 142 PHE n 
1 143 GLY n 
1 144 LEU n 
1 145 PHE n 
1 146 PRO n 
1 147 MET n 
1 148 LEU n 
1 149 ASN n 
1 150 ARG n 
1 151 TYR n 
1 152 GLU n 
1 153 SER n 
1 154 GLN n 
1 155 LEU n 
1 156 LYS n 
1 157 HIS n 
1 158 GLN n 
1 159 TRP n 
1 160 GLU n 
1 161 ARG n 
1 162 ASN n 
1 163 TYR n 
1 164 LEU n 
1 165 GLY n 
1 166 ASN n 
1 167 LYS n 
1 168 ASP n 
1 169 ILE n 
1 170 ILE n 
1 171 PHE n 
1 172 ARG n 
1 173 ASN n 
1 174 THR n 
1 175 PHE n 
1 176 GLY n 
1 177 ASP n 
1 178 VAL n 
1 179 GLU n 
1 180 HIS n 
1 181 VAL n 
1 182 MET n 
1 183 THR n 
1 184 THR n 
1 185 LEU n 
1 186 GLY n 
1 187 ALA n 
1 188 GLY n 
1 189 GLY n 
1 190 THR n 
1 191 ARG n 
1 192 PHE n 
1 193 GLU n 
1 194 PHE n 
1 195 GLU n 
1 196 CYS n 
1 197 TYR n 
1 198 ASP n 
1 199 THR n 
1 200 SER n 
1 201 HIS n 
1 202 LEU n 
1 203 TYR n 
1 204 ASN n 
1 205 LEU n 
1 206 LYS n 
1 207 HIS n 
1 208 PHE n 
1 209 TYR n 
1 210 ASP n 
1 211 ARG n 
1 212 GLY n 
1 213 LEU n 
1 214 VAL n 
1 215 LYS n 
1 216 GLY n 
1 217 PRO n 
1 218 LEU n 
1 219 PHE n 
1 220 ILE n 
1 221 GLN n 
1 222 THR n 
1 223 VAL n 
1 224 PHE n 
1 225 GLY n 
1 226 LEU n 
1 227 MET n 
1 228 GLY n 
1 229 GLY n 
1 230 ILE n 
1 231 GLY n 
1 232 ALA n 
1 233 HIS n 
1 234 PRO n 
1 235 ASP n 
1 236 ASP n 
1 237 VAL n 
1 238 LEU n 
1 239 HIS n 
1 240 MET n 
1 241 LYS n 
1 242 ARG n 
1 243 THR n 
1 244 ALA n 
1 245 ASP n 
1 246 ARG n 
1 247 LEU n 
1 248 PHE n 
1 249 GLY n 
1 250 GLN n 
1 251 ASP n 
1 252 TYR n 
1 253 ARG n 
1 254 TRP n 
1 255 SER n 
1 256 VAL n 
1 257 LEU n 
1 258 GLY n 
1 259 ALA n 
1 260 GLY n 
1 261 ARG n 
1 262 ASN n 
1 263 GLN n 
1 264 LEU n 
1 265 ASN n 
1 266 ILE n 
1 267 ALA n 
1 268 ALA n 
1 269 MET n 
1 270 SER n 
1 271 ALA n 
1 272 ALA n 
1 273 MET n 
1 274 GLY n 
1 275 GLY n 
1 276 HIS n 
1 277 VAL n 
1 278 ARG n 
1 279 VAL n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 ASP n 
1 284 ASN n 
1 285 LEU n 
1 286 TRP n 
1 287 ALA n 
1 288 GLY n 
1 289 LYS n 
1 290 GLY n 
1 291 ARG n 
1 292 LEU n 
1 293 ALA n 
1 294 GLU n 
1 295 THR n 
1 296 ASN n 
1 297 ALA n 
1 298 GLN n 
1 299 GLN n 
1 300 VAL n 
1 301 ARG n 
1 302 ALA n 
1 303 ALA n 
1 304 ARG n 
1 305 GLN n 
1 306 ILE n 
1 307 VAL n 
1 308 GLU n 
1 309 GLY n 
1 310 LEU n 
1 311 GLY n 
1 312 LEU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 THR n 
1 317 PRO n 
1 318 ALA n 
1 319 GLU n 
1 320 ALA n 
1 321 ARG n 
1 322 GLU n 
1 323 LEU n 
1 324 LEU n 
1 325 ALA n 
1 326 LEU n 
1 327 LYS n 
1 328 GLY n 
1 329 GLY n 
1 330 ASP n 
1 331 GLN n 
1 332 VAL n 
1 333 ASN n 
1 334 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   334 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Pden_3578 
_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      'Paracoccus denitrificans PD1222' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     318586 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
AAE non-polymer         . 'ACETOACETIC ACID'   ? 'C4 H6 O3'            102.089 
ACO non-polymer         . 'ACETYL COENZYME *A' ? 'C23 H38 N7 O17 P3 S' 809.571 
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 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'           ? 'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -23 ?   ?   ?   A . n 
A 1 2   GLY 2   -22 ?   ?   ?   A . n 
A 1 3   HIS 3   -21 ?   ?   ?   A . n 
A 1 4   HIS 4   -20 ?   ?   ?   A . n 
A 1 5   HIS 5   -19 ?   ?   ?   A . n 
A 1 6   HIS 6   -18 ?   ?   ?   A . n 
A 1 7   HIS 7   -17 ?   ?   ?   A . n 
A 1 8   HIS 8   -16 ?   ?   ?   A . n 
A 1 9   HIS 9   -15 ?   ?   ?   A . n 
A 1 10  HIS 10  -14 ?   ?   ?   A . n 
A 1 11  HIS 11  -13 ?   ?   ?   A . n 
A 1 12  HIS 12  -12 ?   ?   ?   A . n 
A 1 13  SER 13  -11 ?   ?   ?   A . n 
A 1 14  SER 14  -10 ?   ?   ?   A . n 
A 1 15  GLY 15  -9  ?   ?   ?   A . n 
A 1 16  HIS 16  -8  ?   ?   ?   A . n 
A 1 17  ILE 17  -7  ?   ?   ?   A . n 
A 1 18  GLU 18  -6  ?   ?   ?   A . n 
A 1 19  GLY 19  -5  ?   ?   ?   A . n 
A 1 20  ARG 20  -4  ?   ?   ?   A . n 
A 1 21  HIS 21  -3  ?   ?   ?   A . n 
A 1 22  GLY 22  -2  ?   ?   ?   A . n 
A 1 23  SER 23  -1  ?   ?   ?   A . n 
A 1 24  ARG 24  0   ?   ?   ?   A . n 
A 1 25  MET 25  1   ?   ?   ?   A . n 
A 1 26  SER 26  2   2   SER SER A . n 
A 1 27  LEU 27  3   3   LEU LEU A . n 
A 1 28  ASN 28  4   4   ASN ASN A . n 
A 1 29  GLY 29  5   5   GLY GLY A . n 
A 1 30  LYS 30  6   6   LYS LYS A . n 
A 1 31  VAL 31  7   7   VAL VAL A . n 
A 1 32  ILE 32  8   8   ILE ILE A . n 
A 1 33  ILE 33  9   9   ILE ILE A . n 
A 1 34  THR 34  10  10  THR THR A . n 
A 1 35  CYS 35  11  11  CYS CYS A . n 
A 1 36  ALA 36  12  12  ALA ALA A . n 
A 1 37  VAL 37  13  13  VAL VAL A . n 
A 1 38  THR 38  14  14  THR THR A . n 
A 1 39  GLY 39  15  15  GLY GLY A . n 
A 1 40  ALA 40  16  16  ALA ALA A . n 
A 1 41  ILE 41  17  17  ILE ILE A . n 
A 1 42  HIS 42  18  18  HIS HIS A . n 
A 1 43  THR 43  19  19  THR THR A . n 
A 1 44  PRO 44  20  20  PRO PRO A . n 
A 1 45  SER 45  21  21  SER SER A . n 
A 1 46  MET 46  22  22  MET MET A . n 
A 1 47  SER 47  23  23  SER SER A . n 
A 1 48  PRO 48  24  24  PRO PRO A . n 
A 1 49  TYR 49  25  25  TYR TYR A . n 
A 1 50  LEU 50  26  26  LEU LEU A . n 
A 1 51  PRO 51  27  27  PRO PRO A . n 
A 1 52  VAL 52  28  28  VAL VAL A . n 
A 1 53  SER 53  29  29  SER SER A . n 
A 1 54  ALA 54  30  30  ALA ALA A . n 
A 1 55  SER 55  31  31  SER SER A . n 
A 1 56  GLU 56  32  32  GLU GLU A . n 
A 1 57  ILE 57  33  33  ILE ILE A . n 
A 1 58  THR 58  34  34  THR THR A . n 
A 1 59  ASP 59  35  35  ASP ASP A . n 
A 1 60  ALA 60  36  36  ALA ALA A . n 
A 1 61  ALA 61  37  37  ALA ALA A . n 
A 1 62  ILE 62  38  38  ILE ILE A . n 
A 1 63  GLY 63  39  39  GLY GLY A . n 
A 1 64  ALA 64  40  40  ALA ALA A . n 
A 1 65  ALA 65  41  41  ALA ALA A . n 
A 1 66  GLU 66  42  42  GLU GLU A . n 
A 1 67  ALA 67  43  43  ALA ALA A . n 
A 1 68  GLY 68  44  44  GLY GLY A . n 
A 1 69  ALA 69  45  45  ALA ALA A . n 
A 1 70  ALA 70  46  46  ALA ALA A . n 
A 1 71  VAL 71  47  47  VAL VAL A . n 
A 1 72  ILE 72  48  48  ILE ILE A . n 
A 1 73  HIS 73  49  49  HIS HIS A . n 
A 1 74  LEU 74  50  50  LEU LEU A . n 
A 1 75  HIS 75  51  51  HIS HIS A . n 
A 1 76  ALA 76  52  52  ALA ALA A . n 
A 1 77  ARG 77  53  53  ARG ARG A . n 
A 1 78  HIS 78  54  54  HIS HIS A . n 
A 1 79  GLU 79  55  55  GLU GLU A . n 
A 1 80  GLY 80  56  56  GLY GLY A . n 
A 1 81  ASP 81  57  57  ASP ASP A . n 
A 1 82  GLY 82  58  58  GLY GLY A . n 
A 1 83  SER 83  59  59  SER SER A . n 
A 1 84  PRO 84  60  60  PRO PRO A . n 
A 1 85  ASP 85  61  61  ASP ASP A . n 
A 1 86  GLN 86  62  62  GLN GLN A . n 
A 1 87  SER 87  63  63  SER SER A . n 
A 1 88  VAL 88  64  64  VAL VAL A . n 
A 1 89  GLU 89  65  65  GLU GLU A . n 
A 1 90  ALA 90  66  66  ALA ALA A . n 
A 1 91  PHE 91  67  67  PHE PHE A . n 
A 1 92  ASN 92  68  68  ASN ASN A . n 
A 1 93  PRO 93  69  69  PRO PRO A . n 
A 1 94  ILE 94  70  70  ILE ILE A . n 
A 1 95  LEU 95  71  71  LEU LEU A . n 
A 1 96  GLY 96  72  72  GLY GLY A . n 
A 1 97  VAL 97  73  73  VAL VAL A . n 
A 1 98  ILE 98  74  74  ILE ILE A . n 
A 1 99  LYS 99  75  75  LYS LYS A . n 
A 1 100 GLN 100 76  76  GLN GLN A . n 
A 1 101 ALA 101 77  77  ALA ALA A . n 
A 1 102 SER 102 78  78  SER SER A . n 
A 1 103 ASP 103 79  79  ASP ASP A . n 
A 1 104 ALA 104 80  80  ALA ALA A . n 
A 1 105 VAL 105 81  81  VAL VAL A . n 
A 1 106 LEU 106 82  82  LEU LEU A . n 
A 1 107 ASN 107 83  83  ASN ASN A . n 
A 1 108 ILE 108 84  84  ILE ILE A . n 
A 1 109 THR 109 85  85  THR THR A . n 
A 1 110 THR 110 86  86  THR THR A . n 
A 1 111 GLY 111 87  87  GLY GLY A . n 
A 1 112 GLY 112 88  88  GLY GLY A . n 
A 1 113 ALA 113 89  89  ALA ALA A . n 
A 1 114 PRO 114 90  90  PRO PRO A . n 
A 1 115 THR 115 91  91  THR THR A . n 
A 1 116 MET 116 92  92  MET MET A . n 
A 1 117 SER 117 93  93  SER SER A . n 
A 1 118 ILE 118 94  94  ILE ILE A . n 
A 1 119 ALA 119 95  95  ALA ALA A . n 
A 1 120 GLU 120 96  96  GLU GLU A . n 
A 1 121 ARG 121 97  97  ARG ARG A . n 
A 1 122 ILE 122 98  98  ILE ILE A . n 
A 1 123 GLN 123 99  99  GLN GLN A . n 
A 1 124 PRO 124 100 100 PRO PRO A . n 
A 1 125 ALA 125 101 101 ALA ALA A . n 
A 1 126 GLN 126 102 102 GLN GLN A . n 
A 1 127 HIS 127 103 103 HIS HIS A . n 
A 1 128 TYR 128 104 104 TYR TYR A . n 
A 1 129 ARG 129 105 105 ARG ARG A . n 
A 1 130 PRO 130 106 106 PRO PRO A . n 
A 1 131 GLU 131 107 107 GLU GLU A . n 
A 1 132 LEU 132 108 108 LEU LEU A . n 
A 1 133 ALA 133 109 109 ALA ALA A . n 
A 1 134 SER 134 110 110 SER SER A . n 
A 1 135 LEU 135 111 111 LEU LEU A . n 
A 1 136 ASN 136 112 112 ASN ASN A . n 
A 1 137 MET 137 113 113 MET MET A . n 
A 1 138 GLY 138 114 114 GLY GLY A . n 
A 1 139 THR 139 115 115 THR THR A . n 
A 1 140 MET 140 116 116 MET MET A . n 
A 1 141 ASN 141 117 117 ASN ASN A . n 
A 1 142 PHE 142 118 118 PHE PHE A . n 
A 1 143 GLY 143 119 119 GLY GLY A . n 
A 1 144 LEU 144 120 120 LEU LEU A . n 
A 1 145 PHE 145 121 121 PHE PHE A . n 
A 1 146 PRO 146 122 122 PRO PRO A . n 
A 1 147 MET 147 123 123 MET MET A . n 
A 1 148 LEU 148 124 124 LEU LEU A . n 
A 1 149 ASN 149 125 125 ASN ASN A . n 
A 1 150 ARG 150 126 126 ARG ARG A . n 
A 1 151 TYR 151 127 127 TYR TYR A . n 
A 1 152 GLU 152 128 128 GLU GLU A . n 
A 1 153 SER 153 129 129 SER SER A . n 
A 1 154 GLN 154 130 130 GLN GLN A . n 
A 1 155 LEU 155 131 131 LEU LEU A . n 
A 1 156 LYS 156 132 132 LYS LYS A . n 
A 1 157 HIS 157 133 133 HIS HIS A . n 
A 1 158 GLN 158 134 134 GLN GLN A . n 
A 1 159 TRP 159 135 135 TRP TRP A . n 
A 1 160 GLU 160 136 136 GLU GLU A . n 
A 1 161 ARG 161 137 137 ARG ARG A . n 
A 1 162 ASN 162 138 138 ASN ASN A . n 
A 1 163 TYR 163 139 139 TYR TYR A . n 
A 1 164 LEU 164 140 140 LEU LEU A . n 
A 1 165 GLY 165 141 141 GLY GLY A . n 
A 1 166 ASN 166 142 142 ASN ASN A . n 
A 1 167 LYS 167 143 143 LYS LYS A . n 
A 1 168 ASP 168 144 144 ASP ASP A . n 
A 1 169 ILE 169 145 145 ILE ILE A . n 
A 1 170 ILE 170 146 146 ILE ILE A . n 
A 1 171 PHE 171 147 147 PHE PHE A . n 
A 1 172 ARG 172 148 148 ARG ARG A . n 
A 1 173 ASN 173 149 149 ASN ASN A . n 
A 1 174 THR 174 150 150 THR THR A . n 
A 1 175 PHE 175 151 151 PHE PHE A . n 
A 1 176 GLY 176 152 152 GLY GLY A . n 
A 1 177 ASP 177 153 153 ASP ASP A . n 
A 1 178 VAL 178 154 154 VAL VAL A . n 
A 1 179 GLU 179 155 155 GLU GLU A . n 
A 1 180 HIS 180 156 156 HIS HIS A . n 
A 1 181 VAL 181 157 157 VAL VAL A . n 
A 1 182 MET 182 158 158 MET MET A . n 
A 1 183 THR 183 159 159 THR THR A . n 
A 1 184 THR 184 160 160 THR THR A . n 
A 1 185 LEU 185 161 161 LEU LEU A . n 
A 1 186 GLY 186 162 162 GLY GLY A . n 
A 1 187 ALA 187 163 163 ALA ALA A . n 
A 1 188 GLY 188 164 164 GLY GLY A . n 
A 1 189 GLY 189 165 165 GLY GLY A . n 
A 1 190 THR 190 166 166 THR THR A . n 
A 1 191 ARG 191 167 167 ARG ARG A . n 
A 1 192 PHE 192 168 168 PHE PHE A . n 
A 1 193 GLU 193 169 169 GLU GLU A . n 
A 1 194 PHE 194 170 170 PHE PHE A . n 
A 1 195 GLU 195 171 171 GLU GLU A . n 
A 1 196 CYS 196 172 172 CYS CYS A . n 
A 1 197 TYR 197 173 173 TYR TYR A . n 
A 1 198 ASP 198 174 174 ASP ASP A . n 
A 1 199 THR 199 175 175 THR THR A . n 
A 1 200 SER 200 176 176 SER SER A . n 
A 1 201 HIS 201 177 177 HIS HIS A . n 
A 1 202 LEU 202 178 178 LEU LEU A . n 
A 1 203 TYR 203 179 179 TYR TYR A . n 
A 1 204 ASN 204 180 180 ASN ASN A . n 
A 1 205 LEU 205 181 181 LEU LEU A . n 
A 1 206 LYS 206 182 182 LYS LYS A . n 
A 1 207 HIS 207 183 183 HIS HIS A . n 
A 1 208 PHE 208 184 184 PHE PHE A . n 
A 1 209 TYR 209 185 185 TYR TYR A . n 
A 1 210 ASP 210 186 186 ASP ASP A . n 
A 1 211 ARG 211 187 187 ARG ARG A . n 
A 1 212 GLY 212 188 188 GLY GLY A . n 
A 1 213 LEU 213 189 189 LEU LEU A . n 
A 1 214 VAL 214 190 190 VAL VAL A . n 
A 1 215 LYS 215 191 191 LYS LYS A . n 
A 1 216 GLY 216 192 192 GLY GLY A . n 
A 1 217 PRO 217 193 193 PRO PRO A . n 
A 1 218 LEU 218 194 194 LEU LEU A . n 
A 1 219 PHE 219 195 195 PHE PHE A . n 
A 1 220 ILE 220 196 196 ILE ILE A . n 
A 1 221 GLN 221 197 197 GLN GLN A . n 
A 1 222 THR 222 198 198 THR THR A . n 
A 1 223 VAL 223 199 199 VAL VAL A . n 
A 1 224 PHE 224 200 200 PHE PHE A . n 
A 1 225 GLY 225 201 201 GLY GLY A . n 
A 1 226 LEU 226 202 202 LEU LEU A . n 
A 1 227 MET 227 203 203 MET MET A . n 
A 1 228 GLY 228 204 204 GLY GLY A . n 
A 1 229 GLY 229 205 205 GLY GLY A . n 
A 1 230 ILE 230 206 206 ILE ILE A . n 
A 1 231 GLY 231 207 207 GLY GLY A . n 
A 1 232 ALA 232 208 208 ALA ALA A . n 
A 1 233 HIS 233 209 209 HIS HIS A . n 
A 1 234 PRO 234 210 210 PRO PRO A . n 
A 1 235 ASP 235 211 211 ASP ASP A . n 
A 1 236 ASP 236 212 212 ASP ASP A . n 
A 1 237 VAL 237 213 213 VAL VAL A . n 
A 1 238 LEU 238 214 214 LEU LEU A . n 
A 1 239 HIS 239 215 215 HIS HIS A . n 
A 1 240 MET 240 216 216 MET MET A . n 
A 1 241 LYS 241 217 217 LYS LYS A . n 
A 1 242 ARG 242 218 218 ARG ARG A . n 
A 1 243 THR 243 219 219 THR THR A . n 
A 1 244 ALA 244 220 220 ALA ALA A . n 
A 1 245 ASP 245 221 221 ASP ASP A . n 
A 1 246 ARG 246 222 222 ARG ARG A . n 
A 1 247 LEU 247 223 223 LEU LEU A . n 
A 1 248 PHE 248 224 224 PHE PHE A . n 
A 1 249 GLY 249 225 225 GLY GLY A . n 
A 1 250 GLN 250 226 226 GLN GLN A . n 
A 1 251 ASP 251 227 227 ASP ASP A . n 
A 1 252 TYR 252 228 228 TYR TYR A . n 
A 1 253 ARG 253 229 229 ARG ARG A . n 
A 1 254 TRP 254 230 230 TRP TRP A . n 
A 1 255 SER 255 231 231 SER SER A . n 
A 1 256 VAL 256 232 232 VAL VAL A . n 
A 1 257 LEU 257 233 233 LEU LEU A . n 
A 1 258 GLY 258 234 234 GLY GLY A . n 
A 1 259 ALA 259 235 235 ALA ALA A . n 
A 1 260 GLY 260 236 236 GLY GLY A . n 
A 1 261 ARG 261 237 237 ARG ARG A . n 
A 1 262 ASN 262 238 238 ASN ASN A . n 
A 1 263 GLN 263 239 239 GLN GLN A . n 
A 1 264 LEU 264 240 240 LEU LEU A . n 
A 1 265 ASN 265 241 241 ASN ASN A . n 
A 1 266 ILE 266 242 242 ILE ILE A . n 
A 1 267 ALA 267 243 243 ALA ALA A . n 
A 1 268 ALA 268 244 244 ALA ALA A . n 
A 1 269 MET 269 245 245 MET MET A . n 
A 1 270 SER 270 246 246 SER SER A . n 
A 1 271 ALA 271 247 247 ALA ALA A . n 
A 1 272 ALA 272 248 248 ALA ALA A . n 
A 1 273 MET 273 249 249 MET MET A . n 
A 1 274 GLY 274 250 250 GLY GLY A . n 
A 1 275 GLY 275 251 251 GLY GLY A . n 
A 1 276 HIS 276 252 252 HIS HIS A . n 
A 1 277 VAL 277 253 253 VAL VAL A . n 
A 1 278 ARG 278 254 254 ARG ARG A . n 
A 1 279 VAL 279 255 255 VAL VAL A . n 
A 1 280 GLY 280 256 256 GLY GLY A . n 
A 1 281 LEU 281 257 257 LEU LEU A . n 
A 1 282 GLU 282 258 258 GLU GLU A . n 
A 1 283 ASP 283 259 259 ASP ASP A . n 
A 1 284 ASN 284 260 260 ASN ASN A . n 
A 1 285 LEU 285 261 261 LEU LEU A . n 
A 1 286 TRP 286 262 262 TRP TRP A . n 
A 1 287 ALA 287 263 263 ALA ALA A . n 
A 1 288 GLY 288 264 264 GLY GLY A . n 
A 1 289 LYS 289 265 265 LYS LYS A . n 
A 1 290 GLY 290 266 266 GLY GLY A . n 
A 1 291 ARG 291 267 267 ARG ARG A . n 
A 1 292 LEU 292 268 268 LEU LEU A . n 
A 1 293 ALA 293 269 269 ALA ALA A . n 
A 1 294 GLU 294 270 270 GLU GLU A . n 
A 1 295 THR 295 271 271 THR THR A . n 
A 1 296 ASN 296 272 272 ASN ASN A . n 
A 1 297 ALA 297 273 273 ALA ALA A . n 
A 1 298 GLN 298 274 274 GLN GLN A . n 
A 1 299 GLN 299 275 275 GLN GLN A . n 
A 1 300 VAL 300 276 276 VAL VAL A . n 
A 1 301 ARG 301 277 277 ARG ARG A . n 
A 1 302 ALA 302 278 278 ALA ALA A . n 
A 1 303 ALA 303 279 279 ALA ALA A . n 
A 1 304 ARG 304 280 280 ARG ARG A . n 
A 1 305 GLN 305 281 281 GLN GLN A . n 
A 1 306 ILE 306 282 282 ILE ILE A . n 
A 1 307 VAL 307 283 283 VAL VAL A . n 
A 1 308 GLU 308 284 284 GLU GLU A . n 
A 1 309 GLY 309 285 285 GLY GLY A . n 
A 1 310 LEU 310 286 286 LEU LEU A . n 
A 1 311 GLY 311 287 287 GLY GLY A . n 
A 1 312 LEU 312 288 288 LEU LEU A . n 
A 1 313 GLU 313 289 289 GLU GLU A . n 
A 1 314 VAL 314 290 290 VAL VAL A . n 
A 1 315 ALA 315 291 291 ALA ALA A . n 
A 1 316 THR 316 292 292 THR THR A . n 
A 1 317 PRO 317 293 293 PRO PRO A . n 
A 1 318 ALA 318 294 294 ALA ALA A . n 
A 1 319 GLU 319 295 295 GLU GLU A . n 
A 1 320 ALA 320 296 296 ALA ALA A . n 
A 1 321 ARG 321 297 297 ARG ARG A . n 
A 1 322 GLU 322 298 298 GLU GLU A . n 
A 1 323 LEU 323 299 299 LEU LEU A . n 
A 1 324 LEU 324 300 300 LEU LEU A . n 
A 1 325 ALA 325 301 301 ALA ALA A . n 
A 1 326 LEU 326 302 302 LEU LEU A . n 
A 1 327 LYS 327 303 303 LYS LYS A . n 
A 1 328 GLY 328 304 304 GLY GLY A . n 
A 1 329 GLY 329 305 305 GLY GLY A . n 
A 1 330 ASP 330 306 306 ASP ASP A . n 
A 1 331 GLN 331 307 307 GLN GLN A . n 
A 1 332 VAL 332 308 308 VAL VAL A . n 
A 1 333 ASN 333 309 309 ASN ASN A . n 
A 1 334 PHE 334 310 310 PHE PHE A . n 
B 1 1   MET 1   -23 ?   ?   ?   B . n 
B 1 2   GLY 2   -22 ?   ?   ?   B . n 
B 1 3   HIS 3   -21 ?   ?   ?   B . n 
B 1 4   HIS 4   -20 ?   ?   ?   B . n 
B 1 5   HIS 5   -19 ?   ?   ?   B . n 
B 1 6   HIS 6   -18 ?   ?   ?   B . n 
B 1 7   HIS 7   -17 ?   ?   ?   B . n 
B 1 8   HIS 8   -16 ?   ?   ?   B . n 
B 1 9   HIS 9   -15 ?   ?   ?   B . n 
B 1 10  HIS 10  -14 ?   ?   ?   B . n 
B 1 11  HIS 11  -13 ?   ?   ?   B . n 
B 1 12  HIS 12  -12 ?   ?   ?   B . n 
B 1 13  SER 13  -11 ?   ?   ?   B . n 
B 1 14  SER 14  -10 ?   ?   ?   B . n 
B 1 15  GLY 15  -9  ?   ?   ?   B . n 
B 1 16  HIS 16  -8  ?   ?   ?   B . n 
B 1 17  ILE 17  -7  ?   ?   ?   B . n 
B 1 18  GLU 18  -6  ?   ?   ?   B . n 
B 1 19  GLY 19  -5  ?   ?   ?   B . n 
B 1 20  ARG 20  -4  ?   ?   ?   B . n 
B 1 21  HIS 21  -3  ?   ?   ?   B . n 
B 1 22  GLY 22  -2  ?   ?   ?   B . n 
B 1 23  SER 23  -1  ?   ?   ?   B . n 
B 1 24  ARG 24  0   ?   ?   ?   B . n 
B 1 25  MET 25  1   ?   ?   ?   B . n 
B 1 26  SER 26  2   ?   ?   ?   B . n 
B 1 27  LEU 27  3   3   LEU LEU B . n 
B 1 28  ASN 28  4   4   ASN ASN B . n 
B 1 29  GLY 29  5   5   GLY GLY B . n 
B 1 30  LYS 30  6   6   LYS LYS B . n 
B 1 31  VAL 31  7   7   VAL VAL B . n 
B 1 32  ILE 32  8   8   ILE ILE B . n 
B 1 33  ILE 33  9   9   ILE ILE B . n 
B 1 34  THR 34  10  10  THR THR B . n 
B 1 35  CYS 35  11  11  CYS CYS B . n 
B 1 36  ALA 36  12  12  ALA ALA B . n 
B 1 37  VAL 37  13  13  VAL VAL B . n 
B 1 38  THR 38  14  14  THR THR B . n 
B 1 39  GLY 39  15  15  GLY GLY B . n 
B 1 40  ALA 40  16  16  ALA ALA B . n 
B 1 41  ILE 41  17  17  ILE ILE B . n 
B 1 42  HIS 42  18  18  HIS HIS B . n 
B 1 43  THR 43  19  19  THR THR B . n 
B 1 44  PRO 44  20  20  PRO PRO B . n 
B 1 45  SER 45  21  21  SER SER B . n 
B 1 46  MET 46  22  22  MET MET B . n 
B 1 47  SER 47  23  23  SER SER B . n 
B 1 48  PRO 48  24  24  PRO PRO B . n 
B 1 49  TYR 49  25  25  TYR TYR B . n 
B 1 50  LEU 50  26  26  LEU LEU B . n 
B 1 51  PRO 51  27  27  PRO PRO B . n 
B 1 52  VAL 52  28  28  VAL VAL B . n 
B 1 53  SER 53  29  29  SER SER B . n 
B 1 54  ALA 54  30  30  ALA ALA B . n 
B 1 55  SER 55  31  31  SER SER B . n 
B 1 56  GLU 56  32  32  GLU GLU B . n 
B 1 57  ILE 57  33  33  ILE ILE B . n 
B 1 58  THR 58  34  34  THR THR B . n 
B 1 59  ASP 59  35  35  ASP ASP B . n 
B 1 60  ALA 60  36  36  ALA ALA B . n 
B 1 61  ALA 61  37  37  ALA ALA B . n 
B 1 62  ILE 62  38  38  ILE ILE B . n 
B 1 63  GLY 63  39  39  GLY GLY B . n 
B 1 64  ALA 64  40  40  ALA ALA B . n 
B 1 65  ALA 65  41  41  ALA ALA B . n 
B 1 66  GLU 66  42  42  GLU GLU B . n 
B 1 67  ALA 67  43  43  ALA ALA B . n 
B 1 68  GLY 68  44  44  GLY GLY B . n 
B 1 69  ALA 69  45  45  ALA ALA B . n 
B 1 70  ALA 70  46  46  ALA ALA B . n 
B 1 71  VAL 71  47  47  VAL VAL B . n 
B 1 72  ILE 72  48  48  ILE ILE B . n 
B 1 73  HIS 73  49  49  HIS HIS B . n 
B 1 74  LEU 74  50  50  LEU LEU B . n 
B 1 75  HIS 75  51  51  HIS HIS B . n 
B 1 76  ALA 76  52  52  ALA ALA B . n 
B 1 77  ARG 77  53  53  ARG ARG B . n 
B 1 78  HIS 78  54  54  HIS HIS B . n 
B 1 79  GLU 79  55  55  GLU GLU B . n 
B 1 80  GLY 80  56  56  GLY GLY B . n 
B 1 81  ASP 81  57  57  ASP ASP B . n 
B 1 82  GLY 82  58  58  GLY GLY B . n 
B 1 83  SER 83  59  59  SER SER B . n 
B 1 84  PRO 84  60  60  PRO PRO B . n 
B 1 85  ASP 85  61  61  ASP ASP B . n 
B 1 86  GLN 86  62  62  GLN GLN B . n 
B 1 87  SER 87  63  63  SER SER B . n 
B 1 88  VAL 88  64  64  VAL VAL B . n 
B 1 89  GLU 89  65  65  GLU GLU B . n 
B 1 90  ALA 90  66  66  ALA ALA B . n 
B 1 91  PHE 91  67  67  PHE PHE B . n 
B 1 92  ASN 92  68  68  ASN ASN B . n 
B 1 93  PRO 93  69  69  PRO PRO B . n 
B 1 94  ILE 94  70  70  ILE ILE B . n 
B 1 95  LEU 95  71  71  LEU LEU B . n 
B 1 96  GLY 96  72  72  GLY GLY B . n 
B 1 97  VAL 97  73  73  VAL VAL B . n 
B 1 98  ILE 98  74  74  ILE ILE B . n 
B 1 99  LYS 99  75  75  LYS LYS B . n 
B 1 100 GLN 100 76  76  GLN GLN B . n 
B 1 101 ALA 101 77  77  ALA ALA B . n 
B 1 102 SER 102 78  78  SER SER B . n 
B 1 103 ASP 103 79  79  ASP ASP B . n 
B 1 104 ALA 104 80  80  ALA ALA B . n 
B 1 105 VAL 105 81  81  VAL VAL B . n 
B 1 106 LEU 106 82  82  LEU LEU B . n 
B 1 107 ASN 107 83  83  ASN ASN B . n 
B 1 108 ILE 108 84  84  ILE ILE B . n 
B 1 109 THR 109 85  85  THR THR B . n 
B 1 110 THR 110 86  86  THR THR B . n 
B 1 111 GLY 111 87  87  GLY GLY B . n 
B 1 112 GLY 112 88  88  GLY GLY B . n 
B 1 113 ALA 113 89  89  ALA ALA B . n 
B 1 114 PRO 114 90  90  PRO PRO B . n 
B 1 115 THR 115 91  91  THR THR B . n 
B 1 116 MET 116 92  92  MET MET B . n 
B 1 117 SER 117 93  93  SER SER B . n 
B 1 118 ILE 118 94  94  ILE ILE B . n 
B 1 119 ALA 119 95  95  ALA ALA B . n 
B 1 120 GLU 120 96  96  GLU GLU B . n 
B 1 121 ARG 121 97  97  ARG ARG B . n 
B 1 122 ILE 122 98  98  ILE ILE B . n 
B 1 123 GLN 123 99  99  GLN GLN B . n 
B 1 124 PRO 124 100 100 PRO PRO B . n 
B 1 125 ALA 125 101 101 ALA ALA B . n 
B 1 126 GLN 126 102 102 GLN GLN B . n 
B 1 127 HIS 127 103 103 HIS HIS B . n 
B 1 128 TYR 128 104 104 TYR TYR B . n 
B 1 129 ARG 129 105 105 ARG ARG B . n 
B 1 130 PRO 130 106 106 PRO PRO B . n 
B 1 131 GLU 131 107 107 GLU GLU B . n 
B 1 132 LEU 132 108 108 LEU LEU B . n 
B 1 133 ALA 133 109 109 ALA ALA B . n 
B 1 134 SER 134 110 110 SER SER B . n 
B 1 135 LEU 135 111 111 LEU LEU B . n 
B 1 136 ASN 136 112 112 ASN ASN B . n 
B 1 137 MET 137 113 113 MET MET B . n 
B 1 138 GLY 138 114 114 GLY GLY B . n 
B 1 139 THR 139 115 115 THR THR B . n 
B 1 140 MET 140 116 116 MET MET B . n 
B 1 141 ASN 141 117 117 ASN ASN B . n 
B 1 142 PHE 142 118 118 PHE PHE B . n 
B 1 143 GLY 143 119 119 GLY GLY B . n 
B 1 144 LEU 144 120 120 LEU LEU B . n 
B 1 145 PHE 145 121 121 PHE PHE B . n 
B 1 146 PRO 146 122 122 PRO PRO B . n 
B 1 147 MET 147 123 123 MET MET B . n 
B 1 148 LEU 148 124 124 LEU LEU B . n 
B 1 149 ASN 149 125 125 ASN ASN B . n 
B 1 150 ARG 150 126 126 ARG ARG B . n 
B 1 151 TYR 151 127 127 TYR TYR B . n 
B 1 152 GLU 152 128 128 GLU GLU B . n 
B 1 153 SER 153 129 129 SER SER B . n 
B 1 154 GLN 154 130 130 GLN GLN B . n 
B 1 155 LEU 155 131 131 LEU LEU B . n 
B 1 156 LYS 156 132 132 LYS LYS B . n 
B 1 157 HIS 157 133 133 HIS HIS B . n 
B 1 158 GLN 158 134 134 GLN GLN B . n 
B 1 159 TRP 159 135 135 TRP TRP B . n 
B 1 160 GLU 160 136 136 GLU GLU B . n 
B 1 161 ARG 161 137 137 ARG ARG B . n 
B 1 162 ASN 162 138 138 ASN ASN B . n 
B 1 163 TYR 163 139 139 TYR TYR B . n 
B 1 164 LEU 164 140 140 LEU LEU B . n 
B 1 165 GLY 165 141 141 GLY GLY B . n 
B 1 166 ASN 166 142 142 ASN ASN B . n 
B 1 167 LYS 167 143 143 LYS LYS B . n 
B 1 168 ASP 168 144 144 ASP ASP B . n 
B 1 169 ILE 169 145 145 ILE ILE B . n 
B 1 170 ILE 170 146 146 ILE ILE B . n 
B 1 171 PHE 171 147 147 PHE PHE B . n 
B 1 172 ARG 172 148 148 ARG ARG B . n 
B 1 173 ASN 173 149 149 ASN ASN B . n 
B 1 174 THR 174 150 150 THR THR B . n 
B 1 175 PHE 175 151 151 PHE PHE B . n 
B 1 176 GLY 176 152 152 GLY GLY B . n 
B 1 177 ASP 177 153 153 ASP ASP B . n 
B 1 178 VAL 178 154 154 VAL VAL B . n 
B 1 179 GLU 179 155 155 GLU GLU B . n 
B 1 180 HIS 180 156 156 HIS HIS B . n 
B 1 181 VAL 181 157 157 VAL VAL B . n 
B 1 182 MET 182 158 158 MET MET B . n 
B 1 183 THR 183 159 159 THR THR B . n 
B 1 184 THR 184 160 160 THR THR B . n 
B 1 185 LEU 185 161 161 LEU LEU B . n 
B 1 186 GLY 186 162 162 GLY GLY B . n 
B 1 187 ALA 187 163 163 ALA ALA B . n 
B 1 188 GLY 188 164 164 GLY GLY B . n 
B 1 189 GLY 189 165 165 GLY GLY B . n 
B 1 190 THR 190 166 166 THR THR B . n 
B 1 191 ARG 191 167 167 ARG ARG B . n 
B 1 192 PHE 192 168 168 PHE PHE B . n 
B 1 193 GLU 193 169 169 GLU GLU B . n 
B 1 194 PHE 194 170 170 PHE PHE B . n 
B 1 195 GLU 195 171 171 GLU GLU B . n 
B 1 196 CYS 196 172 172 CYS CYS B . n 
B 1 197 TYR 197 173 173 TYR TYR B . n 
B 1 198 ASP 198 174 174 ASP ASP B . n 
B 1 199 THR 199 175 175 THR THR B . n 
B 1 200 SER 200 176 176 SER SER B . n 
B 1 201 HIS 201 177 177 HIS HIS B . n 
B 1 202 LEU 202 178 178 LEU LEU B . n 
B 1 203 TYR 203 179 179 TYR TYR B . n 
B 1 204 ASN 204 180 180 ASN ASN B . n 
B 1 205 LEU 205 181 181 LEU LEU B . n 
B 1 206 LYS 206 182 182 LYS LYS B . n 
B 1 207 HIS 207 183 183 HIS HIS B . n 
B 1 208 PHE 208 184 184 PHE PHE B . n 
B 1 209 TYR 209 185 185 TYR TYR B . n 
B 1 210 ASP 210 186 186 ASP ASP B . n 
B 1 211 ARG 211 187 187 ARG ARG B . n 
B 1 212 GLY 212 188 188 GLY GLY B . n 
B 1 213 LEU 213 189 189 LEU LEU B . n 
B 1 214 VAL 214 190 190 VAL VAL B . n 
B 1 215 LYS 215 191 191 LYS LYS B . n 
B 1 216 GLY 216 192 192 GLY GLY B . n 
B 1 217 PRO 217 193 193 PRO PRO B . n 
B 1 218 LEU 218 194 194 LEU LEU B . n 
B 1 219 PHE 219 195 195 PHE PHE B . n 
B 1 220 ILE 220 196 196 ILE ILE B . n 
B 1 221 GLN 221 197 197 GLN GLN B . n 
B 1 222 THR 222 198 198 THR THR B . n 
B 1 223 VAL 223 199 199 VAL VAL B . n 
B 1 224 PHE 224 200 200 PHE PHE B . n 
B 1 225 GLY 225 201 201 GLY GLY B . n 
B 1 226 LEU 226 202 202 LEU LEU B . n 
B 1 227 MET 227 203 203 MET MET B . n 
B 1 228 GLY 228 204 204 GLY GLY B . n 
B 1 229 GLY 229 205 205 GLY GLY B . n 
B 1 230 ILE 230 206 206 ILE ILE B . n 
B 1 231 GLY 231 207 207 GLY GLY B . n 
B 1 232 ALA 232 208 208 ALA ALA B . n 
B 1 233 HIS 233 209 209 HIS HIS B . n 
B 1 234 PRO 234 210 210 PRO PRO B . n 
B 1 235 ASP 235 211 211 ASP ASP B . n 
B 1 236 ASP 236 212 212 ASP ASP B . n 
B 1 237 VAL 237 213 213 VAL VAL B . n 
B 1 238 LEU 238 214 214 LEU LEU B . n 
B 1 239 HIS 239 215 215 HIS HIS B . n 
B 1 240 MET 240 216 216 MET MET B . n 
B 1 241 LYS 241 217 217 LYS LYS B . n 
B 1 242 ARG 242 218 218 ARG ARG B . n 
B 1 243 THR 243 219 219 THR THR B . n 
B 1 244 ALA 244 220 220 ALA ALA B . n 
B 1 245 ASP 245 221 221 ASP ASP B . n 
B 1 246 ARG 246 222 222 ARG ARG B . n 
B 1 247 LEU 247 223 223 LEU LEU B . n 
B 1 248 PHE 248 224 224 PHE PHE B . n 
B 1 249 GLY 249 225 225 GLY GLY B . n 
B 1 250 GLN 250 226 226 GLN GLN B . n 
B 1 251 ASP 251 227 227 ASP ASP B . n 
B 1 252 TYR 252 228 228 TYR TYR B . n 
B 1 253 ARG 253 229 229 ARG ARG B . n 
B 1 254 TRP 254 230 230 TRP TRP B . n 
B 1 255 SER 255 231 231 SER SER B . n 
B 1 256 VAL 256 232 232 VAL VAL B . n 
B 1 257 LEU 257 233 233 LEU LEU B . n 
B 1 258 GLY 258 234 234 GLY GLY B . n 
B 1 259 ALA 259 235 235 ALA ALA B . n 
B 1 260 GLY 260 236 236 GLY GLY B . n 
B 1 261 ARG 261 237 237 ARG ARG B . n 
B 1 262 ASN 262 238 238 ASN ASN B . n 
B 1 263 GLN 263 239 239 GLN GLN B . n 
B 1 264 LEU 264 240 240 LEU LEU B . n 
B 1 265 ASN 265 241 241 ASN ASN B . n 
B 1 266 ILE 266 242 242 ILE ILE B . n 
B 1 267 ALA 267 243 243 ALA ALA B . n 
B 1 268 ALA 268 244 244 ALA ALA B . n 
B 1 269 MET 269 245 245 MET MET B . n 
B 1 270 SER 270 246 246 SER SER B . n 
B 1 271 ALA 271 247 247 ALA ALA B . n 
B 1 272 ALA 272 248 248 ALA ALA B . n 
B 1 273 MET 273 249 249 MET MET B . n 
B 1 274 GLY 274 250 250 GLY GLY B . n 
B 1 275 GLY 275 251 251 GLY GLY B . n 
B 1 276 HIS 276 252 252 HIS HIS B . n 
B 1 277 VAL 277 253 253 VAL VAL B . n 
B 1 278 ARG 278 254 254 ARG ARG B . n 
B 1 279 VAL 279 255 255 VAL VAL B . n 
B 1 280 GLY 280 256 256 GLY GLY B . n 
B 1 281 LEU 281 257 257 LEU LEU B . n 
B 1 282 GLU 282 258 258 GLU GLU B . n 
B 1 283 ASP 283 259 259 ASP ASP B . n 
B 1 284 ASN 284 260 260 ASN ASN B . n 
B 1 285 LEU 285 261 261 LEU LEU B . n 
B 1 286 TRP 286 262 262 TRP TRP B . n 
B 1 287 ALA 287 263 263 ALA ALA B . n 
B 1 288 GLY 288 264 264 GLY GLY B . n 
B 1 289 LYS 289 265 265 LYS LYS B . n 
B 1 290 GLY 290 266 266 GLY GLY B . n 
B 1 291 ARG 291 267 267 ARG ARG B . n 
B 1 292 LEU 292 268 268 LEU LEU B . n 
B 1 293 ALA 293 269 269 ALA ALA B . n 
B 1 294 GLU 294 270 270 GLU GLU B . n 
B 1 295 THR 295 271 271 THR THR B . n 
B 1 296 ASN 296 272 272 ASN ASN B . n 
B 1 297 ALA 297 273 273 ALA ALA B . n 
B 1 298 GLN 298 274 274 GLN GLN B . n 
B 1 299 GLN 299 275 275 GLN GLN B . n 
B 1 300 VAL 300 276 276 VAL VAL B . n 
B 1 301 ARG 301 277 277 ARG ARG B . n 
B 1 302 ALA 302 278 278 ALA ALA B . n 
B 1 303 ALA 303 279 279 ALA ALA B . n 
B 1 304 ARG 304 280 280 ARG ARG B . n 
B 1 305 GLN 305 281 281 GLN GLN B . n 
B 1 306 ILE 306 282 282 ILE ILE B . n 
B 1 307 VAL 307 283 283 VAL VAL B . n 
B 1 308 GLU 308 284 284 GLU GLU B . n 
B 1 309 GLY 309 285 285 GLY GLY B . n 
B 1 310 LEU 310 286 286 LEU LEU B . n 
B 1 311 GLY 311 287 287 GLY GLY B . n 
B 1 312 LEU 312 288 288 LEU LEU B . n 
B 1 313 GLU 313 289 289 GLU GLU B . n 
B 1 314 VAL 314 290 290 VAL VAL B . n 
B 1 315 ALA 315 291 291 ALA ALA B . n 
B 1 316 THR 316 292 292 THR THR B . n 
B 1 317 PRO 317 293 293 PRO PRO B . n 
B 1 318 ALA 318 294 294 ALA ALA B . n 
B 1 319 GLU 319 295 295 GLU GLU B . n 
B 1 320 ALA 320 296 296 ALA ALA B . n 
B 1 321 ARG 321 297 297 ARG ARG B . n 
B 1 322 GLU 322 298 298 GLU GLU B . n 
B 1 323 LEU 323 299 299 LEU LEU B . n 
B 1 324 LEU 324 300 300 LEU LEU B . n 
B 1 325 ALA 325 301 301 ALA ALA B . n 
B 1 326 LEU 326 302 302 LEU LEU B . n 
B 1 327 LYS 327 303 303 LYS LYS B . n 
B 1 328 GLY 328 304 304 GLY GLY B . n 
B 1 329 GLY 329 305 305 GLY GLY B . n 
B 1 330 ASP 330 306 306 ASP ASP B . n 
B 1 331 GLN 331 307 307 GLN GLN B . n 
B 1 332 VAL 332 308 308 VAL VAL B . n 
B 1 333 ASN 333 309 309 ASN ASN B . n 
B 1 334 PHE 334 310 310 PHE PHE B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 AAE ? ? AAE ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ACO ? ? ACO ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ZN  ? ? ZN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ACO 1   401 404 ACO ACO A . 
D 3 AAE 1   402 405 AAE AAE A . 
E 4 ZN  1   403 410 ZN  ZN  A . 
F 2 ACO 1   401 404 ACO ACO B . 
G 3 AAE 1   402 405 AAE AAE B . 
H 4 ZN  1   403 410 ZN  ZN  B . 
I 5 HOH 1   501 214 HOH HOH A . 
I 5 HOH 2   502 157 HOH HOH A . 
I 5 HOH 3   503 228 HOH HOH A . 
I 5 HOH 4   504 202 HOH HOH A . 
I 5 HOH 5   505 10  HOH HOH A . 
I 5 HOH 6   506 232 HOH HOH A . 
I 5 HOH 7   507 139 HOH HOH A . 
I 5 HOH 8   508 195 HOH HOH A . 
I 5 HOH 9   509 176 HOH HOH A . 
I 5 HOH 10  510 106 HOH HOH A . 
I 5 HOH 11  511 11  HOH HOH A . 
I 5 HOH 12  512 160 HOH HOH A . 
I 5 HOH 13  513 141 HOH HOH A . 
I 5 HOH 14  514 205 HOH HOH A . 
I 5 HOH 15  515 159 HOH HOH A . 
I 5 HOH 16  516 78  HOH HOH A . 
I 5 HOH 17  517 126 HOH HOH A . 
I 5 HOH 18  518 170 HOH HOH A . 
I 5 HOH 19  519 146 HOH HOH A . 
I 5 HOH 20  520 215 HOH HOH A . 
I 5 HOH 21  521 156 HOH HOH A . 
I 5 HOH 22  522 57  HOH HOH A . 
I 5 HOH 23  523 143 HOH HOH A . 
I 5 HOH 24  524 27  HOH HOH A . 
I 5 HOH 25  525 151 HOH HOH A . 
I 5 HOH 26  526 137 HOH HOH A . 
I 5 HOH 27  527 1   HOH HOH A . 
I 5 HOH 28  528 51  HOH HOH A . 
I 5 HOH 29  529 67  HOH HOH A . 
I 5 HOH 30  530 226 HOH HOH A . 
I 5 HOH 31  531 158 HOH HOH A . 
I 5 HOH 32  532 101 HOH HOH A . 
I 5 HOH 33  533 233 HOH HOH A . 
I 5 HOH 34  534 28  HOH HOH A . 
I 5 HOH 35  535 30  HOH HOH A . 
I 5 HOH 36  536 185 HOH HOH A . 
I 5 HOH 37  537 23  HOH HOH A . 
I 5 HOH 38  538 133 HOH HOH A . 
I 5 HOH 39  539 2   HOH HOH A . 
I 5 HOH 40  540 31  HOH HOH A . 
I 5 HOH 41  541 124 HOH HOH A . 
I 5 HOH 42  542 122 HOH HOH A . 
I 5 HOH 43  543 62  HOH HOH A . 
I 5 HOH 44  544 147 HOH HOH A . 
I 5 HOH 45  545 212 HOH HOH A . 
I 5 HOH 46  546 171 HOH HOH A . 
I 5 HOH 47  547 21  HOH HOH A . 
I 5 HOH 48  548 134 HOH HOH A . 
I 5 HOH 49  549 162 HOH HOH A . 
I 5 HOH 50  550 83  HOH HOH A . 
I 5 HOH 51  551 85  HOH HOH A . 
I 5 HOH 52  552 80  HOH HOH A . 
I 5 HOH 53  553 48  HOH HOH A . 
I 5 HOH 54  554 229 HOH HOH A . 
I 5 HOH 55  555 108 HOH HOH A . 
I 5 HOH 56  556 8   HOH HOH A . 
I 5 HOH 57  557 190 HOH HOH A . 
I 5 HOH 58  558 100 HOH HOH A . 
I 5 HOH 59  559 142 HOH HOH A . 
I 5 HOH 60  560 37  HOH HOH A . 
I 5 HOH 61  561 227 HOH HOH A . 
I 5 HOH 62  562 87  HOH HOH A . 
I 5 HOH 63  563 6   HOH HOH A . 
I 5 HOH 64  564 69  HOH HOH A . 
I 5 HOH 65  565 77  HOH HOH A . 
I 5 HOH 66  566 4   HOH HOH A . 
I 5 HOH 67  567 175 HOH HOH A . 
I 5 HOH 68  568 25  HOH HOH A . 
I 5 HOH 69  569 138 HOH HOH A . 
I 5 HOH 70  570 71  HOH HOH A . 
I 5 HOH 71  571 26  HOH HOH A . 
I 5 HOH 72  572 210 HOH HOH A . 
I 5 HOH 73  573 197 HOH HOH A . 
I 5 HOH 74  574 35  HOH HOH A . 
I 5 HOH 75  575 39  HOH HOH A . 
I 5 HOH 76  576 247 HOH HOH A . 
I 5 HOH 77  577 19  HOH HOH A . 
I 5 HOH 78  578 42  HOH HOH A . 
I 5 HOH 79  579 49  HOH HOH A . 
I 5 HOH 80  580 121 HOH HOH A . 
I 5 HOH 81  581 119 HOH HOH A . 
I 5 HOH 82  582 189 HOH HOH A . 
I 5 HOH 83  583 61  HOH HOH A . 
I 5 HOH 84  584 92  HOH HOH A . 
I 5 HOH 85  585 9   HOH HOH A . 
I 5 HOH 86  586 113 HOH HOH A . 
I 5 HOH 87  587 173 HOH HOH A . 
I 5 HOH 88  588 241 HOH HOH A . 
I 5 HOH 89  589 45  HOH HOH A . 
I 5 HOH 90  590 91  HOH HOH A . 
I 5 HOH 91  591 166 HOH HOH A . 
I 5 HOH 92  592 29  HOH HOH A . 
I 5 HOH 93  593 196 HOH HOH A . 
I 5 HOH 94  594 198 HOH HOH A . 
I 5 HOH 95  595 182 HOH HOH A . 
I 5 HOH 96  596 84  HOH HOH A . 
I 5 HOH 97  597 60  HOH HOH A . 
I 5 HOH 98  598 120 HOH HOH A . 
I 5 HOH 99  599 161 HOH HOH A . 
I 5 HOH 100 600 218 HOH HOH A . 
I 5 HOH 101 601 125 HOH HOH A . 
I 5 HOH 102 602 237 HOH HOH A . 
I 5 HOH 103 603 94  HOH HOH A . 
I 5 HOH 104 604 219 HOH HOH A . 
I 5 HOH 105 605 244 HOH HOH A . 
I 5 HOH 106 606 99  HOH HOH A . 
I 5 HOH 107 607 16  HOH HOH A . 
I 5 HOH 108 608 56  HOH HOH A . 
I 5 HOH 109 609 105 HOH HOH A . 
I 5 HOH 110 610 209 HOH HOH A . 
I 5 HOH 111 611 207 HOH HOH A . 
I 5 HOH 112 612 110 HOH HOH A . 
I 5 HOH 113 613 54  HOH HOH A . 
I 5 HOH 114 614 75  HOH HOH A . 
I 5 HOH 115 615 169 HOH HOH A . 
I 5 HOH 116 616 184 HOH HOH A . 
I 5 HOH 117 617 114 HOH HOH A . 
I 5 HOH 118 618 144 HOH HOH A . 
I 5 HOH 119 619 168 HOH HOH A . 
I 5 HOH 120 620 177 HOH HOH A . 
I 5 HOH 121 621 234 HOH HOH A . 
I 5 HOH 122 622 240 HOH HOH A . 
I 5 HOH 123 623 206 HOH HOH A . 
I 5 HOH 124 624 130 HOH HOH A . 
I 5 HOH 125 625 116 HOH HOH A . 
I 5 HOH 126 626 193 HOH HOH A . 
I 5 HOH 127 627 131 HOH HOH A . 
I 5 HOH 128 628 109 HOH HOH A . 
J 5 HOH 1   501 44  HOH HOH B . 
J 5 HOH 2   502 181 HOH HOH B . 
J 5 HOH 3   503 82  HOH HOH B . 
J 5 HOH 4   504 47  HOH HOH B . 
J 5 HOH 5   505 152 HOH HOH B . 
J 5 HOH 6   506 230 HOH HOH B . 
J 5 HOH 7   507 90  HOH HOH B . 
J 5 HOH 8   508 102 HOH HOH B . 
J 5 HOH 9   509 34  HOH HOH B . 
J 5 HOH 10  510 58  HOH HOH B . 
J 5 HOH 11  511 223 HOH HOH B . 
J 5 HOH 12  512 79  HOH HOH B . 
J 5 HOH 13  513 148 HOH HOH B . 
J 5 HOH 14  514 41  HOH HOH B . 
J 5 HOH 15  515 53  HOH HOH B . 
J 5 HOH 16  516 140 HOH HOH B . 
J 5 HOH 17  517 76  HOH HOH B . 
J 5 HOH 18  518 231 HOH HOH B . 
J 5 HOH 19  519 93  HOH HOH B . 
J 5 HOH 20  520 204 HOH HOH B . 
J 5 HOH 21  521 74  HOH HOH B . 
J 5 HOH 22  522 208 HOH HOH B . 
J 5 HOH 23  523 245 HOH HOH B . 
J 5 HOH 24  524 46  HOH HOH B . 
J 5 HOH 25  525 63  HOH HOH B . 
J 5 HOH 26  526 225 HOH HOH B . 
J 5 HOH 27  527 18  HOH HOH B . 
J 5 HOH 28  528 66  HOH HOH B . 
J 5 HOH 29  529 172 HOH HOH B . 
J 5 HOH 30  530 236 HOH HOH B . 
J 5 HOH 31  531 103 HOH HOH B . 
J 5 HOH 32  532 135 HOH HOH B . 
J 5 HOH 33  533 52  HOH HOH B . 
J 5 HOH 34  534 43  HOH HOH B . 
J 5 HOH 35  535 252 HOH HOH B . 
J 5 HOH 36  536 17  HOH HOH B . 
J 5 HOH 37  537 13  HOH HOH B . 
J 5 HOH 38  538 150 HOH HOH B . 
J 5 HOH 39  539 179 HOH HOH B . 
J 5 HOH 40  540 129 HOH HOH B . 
J 5 HOH 41  541 3   HOH HOH B . 
J 5 HOH 42  542 235 HOH HOH B . 
J 5 HOH 43  543 64  HOH HOH B . 
J 5 HOH 44  544 216 HOH HOH B . 
J 5 HOH 45  545 118 HOH HOH B . 
J 5 HOH 46  546 22  HOH HOH B . 
J 5 HOH 47  547 112 HOH HOH B . 
J 5 HOH 48  548 36  HOH HOH B . 
J 5 HOH 49  549 187 HOH HOH B . 
J 5 HOH 50  550 12  HOH HOH B . 
J 5 HOH 51  551 164 HOH HOH B . 
J 5 HOH 52  552 136 HOH HOH B . 
J 5 HOH 53  553 50  HOH HOH B . 
J 5 HOH 54  554 89  HOH HOH B . 
J 5 HOH 55  555 32  HOH HOH B . 
J 5 HOH 56  556 14  HOH HOH B . 
J 5 HOH 57  557 183 HOH HOH B . 
J 5 HOH 58  558 15  HOH HOH B . 
J 5 HOH 59  559 107 HOH HOH B . 
J 5 HOH 60  560 149 HOH HOH B . 
J 5 HOH 61  561 86  HOH HOH B . 
J 5 HOH 62  562 7   HOH HOH B . 
J 5 HOH 63  563 167 HOH HOH B . 
J 5 HOH 64  564 238 HOH HOH B . 
J 5 HOH 65  565 186 HOH HOH B . 
J 5 HOH 66  566 68  HOH HOH B . 
J 5 HOH 67  567 88  HOH HOH B . 
J 5 HOH 68  568 20  HOH HOH B . 
J 5 HOH 69  569 40  HOH HOH B . 
J 5 HOH 70  570 163 HOH HOH B . 
J 5 HOH 71  571 222 HOH HOH B . 
J 5 HOH 72  572 33  HOH HOH B . 
J 5 HOH 73  573 72  HOH HOH B . 
J 5 HOH 74  574 104 HOH HOH B . 
J 5 HOH 75  575 127 HOH HOH B . 
J 5 HOH 76  576 38  HOH HOH B . 
J 5 HOH 77  577 191 HOH HOH B . 
J 5 HOH 78  578 192 HOH HOH B . 
J 5 HOH 79  579 123 HOH HOH B . 
J 5 HOH 80  580 203 HOH HOH B . 
J 5 HOH 81  581 24  HOH HOH B . 
J 5 HOH 82  582 65  HOH HOH B . 
J 5 HOH 83  583 70  HOH HOH B . 
J 5 HOH 84  584 5   HOH HOH B . 
J 5 HOH 85  585 132 HOH HOH B . 
J 5 HOH 86  586 73  HOH HOH B . 
J 5 HOH 87  587 188 HOH HOH B . 
J 5 HOH 88  588 220 HOH HOH B . 
J 5 HOH 89  589 249 HOH HOH B . 
J 5 HOH 90  590 115 HOH HOH B . 
J 5 HOH 91  591 178 HOH HOH B . 
J 5 HOH 92  592 97  HOH HOH B . 
J 5 HOH 93  593 155 HOH HOH B . 
J 5 HOH 94  594 111 HOH HOH B . 
J 5 HOH 95  595 145 HOH HOH B . 
J 5 HOH 96  596 154 HOH HOH B . 
J 5 HOH 97  597 59  HOH HOH B . 
J 5 HOH 98  598 95  HOH HOH B . 
J 5 HOH 99  599 253 HOH HOH B . 
J 5 HOH 100 600 98  HOH HOH B . 
J 5 HOH 101 601 194 HOH HOH B . 
J 5 HOH 102 602 213 HOH HOH B . 
J 5 HOH 103 603 174 HOH HOH B . 
J 5 HOH 104 604 96  HOH HOH B . 
J 5 HOH 105 605 165 HOH HOH B . 
J 5 HOH 106 606 153 HOH HOH B . 
J 5 HOH 107 607 180 HOH HOH B . 
J 5 HOH 108 608 221 HOH HOH B . 
J 5 HOH 109 609 217 HOH HOH B . 
J 5 HOH 110 610 128 HOH HOH B . 
J 5 HOH 111 611 199 HOH HOH B . 
J 5 HOH 112 612 224 HOH HOH B . 
J 5 HOH 113 613 243 HOH HOH B . 
J 5 HOH 114 614 117 HOH HOH B . 
J 5 HOH 115 615 200 HOH HOH B . 
J 5 HOH 116 616 201 HOH HOH B . 
J 5 HOH 117 617 211 HOH HOH B . 
J 5 HOH 118 618 55  HOH HOH B . 
J 5 HOH 119 619 246 HOH HOH B . 
J 5 HOH 120 620 250 HOH HOH B . 
J 5 HOH 121 621 81  HOH HOH B . 
J 5 HOH 122 622 242 HOH HOH B . 
J 5 HOH 123 623 251 HOH HOH B . 
J 5 HOH 124 624 248 HOH HOH B . 
J 5 HOH 125 625 239 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21.2_5419 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.9       2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 20240723    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 1.21.2_5419 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HNF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     80.900 
_cell.length_a_esd                 ? 
_cell.length_b                     138.480 
_cell.length_b_esd                 ? 
_cell.length_c                     136.360 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9HNF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_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                   9HNF 
_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             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.07 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.8 
_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    
;The enzyme (8.6 mg/mL) in 50 mM HEPES pH 7.8, 150 mM KCl, 1 M L-proline, and 1 mM ZnCl2 was mixed in a 1:1 ratio with 10 % (v/v) pentaerythritol ethoxylate, 10 % v/v 1-Butanol. The final size of the drops was 1 microliter.
Prior to flash freezing the crystals in liquid nitrogen, the mother liquor was supplemented with 15 mM acetyl-CoA, 20 mM acetoacetate, and 20 % (v/v) pentaerythrol propoxylate.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            288 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-09-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HNF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               27.69 
_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                                     44681 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.119 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       591673 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.114 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3628 
_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                               13.5 
_reflns_shell.pdbx_chi_squared                              0.78 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.874 
_reflns_shell.pdbx_Rpim_I_all                               0.234 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.884 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.841 
_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                               ? 
_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                                 9HNF 
_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                            2.10 
_refine.ls_d_res_low                             27.69 
_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                     44675 
_refine.ls_number_reflns_R_free                  1993 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.33 
_refine.ls_percent_reflns_R_free                 4.46 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1759 
_refine.ls_R_factor_R_free                       0.1920 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1752 
_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                          1.67 
_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       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.75 
_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                            0.21 
_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.pdbx_number_atoms_protein        4698 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         118 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               5069 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        27.69 
# 
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' ? 0.003  ? 4914 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.620  ? 6670 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.088 ? 1808 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 731  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 875  ? f_plane_restr      ? ? 
# 
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' 2.10 2.15  . . 141 2994 99.00  . . . . 0.2474 . . . . . . . . . . . 0.2934 
'X-RAY DIFFRACTION' 2.15 2.21  . . 138 3013 100.00 . . . . 0.2476 . . . . . . . . . . . 0.2785 
'X-RAY DIFFRACTION' 2.21 2.28  . . 140 2922 96.00  . . . . 0.3407 . . . . . . . . . . . 0.3832 
'X-RAY DIFFRACTION' 2.28 2.35  . . 137 3057 100.00 . . . . 0.2173 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 2.35 2.43  . . 142 3052 100.00 . . . . 0.1941 . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 2.43 2.53  . . 148 3020 100.00 . . . . 0.1851 . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 2.53 2.65  . . 145 3021 100.00 . . . . 0.1910 . . . . . . . . . . . 0.2168 
'X-RAY DIFFRACTION' 2.65 2.78  . . 137 3058 99.00  . . . . 0.1934 . . . . . . . . . . . 0.2459 
'X-RAY DIFFRACTION' 2.78 2.96  . . 138 3024 99.00  . . . . 0.1961 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 2.96 3.19  . . 147 3045 100.00 . . . . 0.1920 . . . . . . . . . . . 0.2046 
'X-RAY DIFFRACTION' 3.19 3.51  . . 142 3086 100.00 . . . . 0.1720 . . . . . . . . . . . 0.2283 
'X-RAY DIFFRACTION' 3.51 4.01  . . 145 3066 100.00 . . . . 0.1519 . . . . . . . . . . . 0.1669 
'X-RAY DIFFRACTION' 4.01 5.05  . . 145 3111 100.00 . . . . 0.1337 . . . . . . . . . . . 0.1258 
'X-RAY DIFFRACTION' 5.05 27.69 . . 148 3213 99.00  . . . . 0.1481 . . . . . . . . . . . 0.1443 
# 
_struct.entry_id                     9HNF 
_struct.title                        
'Beta-keto acid cleavage enzyme from Paracoccus denitrificans with bound acetoacetate and acetyl-CoA' 
_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        9HNF 
_struct_keywords.text            'aldolase, acetyl-CoA, acetoacetate, BKACE, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A1B802_PARDP 
_struct_ref.pdbx_db_accession          A1B802 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLNGKVIITCAVTGAIHTPSMSPYLPVSASEITDAAIGAAEAGAAVIHLHARHEGDGSPDQSVEAFNPILGVIKQASDA
VLNITTGGAPTMSIAERIQPAQHYRPELASLNMGTMNFGLFPMLNRYESQLKHQWERNYLGNKDIIFRNTFGDVEHVMTT
LGAGGTRFEFECYDTSHLYNLKHFYDRGLVKGPLFIQTVFGLMGGIGAHPDDVLHMKRTADRLFGQDYRWSVLGAGRNQL
NIAAMSAAMGGHVRVGLEDNLWAGKGRLAETNAQQVRAARQIVEGLGLEVATPAEARELLALKGGDQVNF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9HNF A 25 ? 334 ? A1B802 1 ? 310 ? 1 310 
2 1 9HNF B 25 ? 334 ? A1B802 1 ? 310 ? 1 310 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9HNF MET A 1  ? UNP A1B802 ? ? 'initiating methionine' -23 1  
1 9HNF GLY A 2  ? UNP A1B802 ? ? 'expression tag'        -22 2  
1 9HNF HIS A 3  ? UNP A1B802 ? ? 'expression tag'        -21 3  
1 9HNF HIS A 4  ? UNP A1B802 ? ? 'expression tag'        -20 4  
1 9HNF HIS A 5  ? UNP A1B802 ? ? 'expression tag'        -19 5  
1 9HNF HIS A 6  ? UNP A1B802 ? ? 'expression tag'        -18 6  
1 9HNF HIS A 7  ? UNP A1B802 ? ? 'expression tag'        -17 7  
1 9HNF HIS A 8  ? UNP A1B802 ? ? 'expression tag'        -16 8  
1 9HNF HIS A 9  ? UNP A1B802 ? ? 'expression tag'        -15 9  
1 9HNF HIS A 10 ? UNP A1B802 ? ? 'expression tag'        -14 10 
1 9HNF HIS A 11 ? UNP A1B802 ? ? 'expression tag'        -13 11 
1 9HNF HIS A 12 ? UNP A1B802 ? ? 'expression tag'        -12 12 
1 9HNF SER A 13 ? UNP A1B802 ? ? 'expression tag'        -11 13 
1 9HNF SER A 14 ? UNP A1B802 ? ? 'expression tag'        -10 14 
1 9HNF GLY A 15 ? UNP A1B802 ? ? 'expression tag'        -9  15 
1 9HNF HIS A 16 ? UNP A1B802 ? ? 'expression tag'        -8  16 
1 9HNF ILE A 17 ? UNP A1B802 ? ? 'expression tag'        -7  17 
1 9HNF GLU A 18 ? UNP A1B802 ? ? 'expression tag'        -6  18 
1 9HNF GLY A 19 ? UNP A1B802 ? ? 'expression tag'        -5  19 
1 9HNF ARG A 20 ? UNP A1B802 ? ? 'expression tag'        -4  20 
1 9HNF HIS A 21 ? UNP A1B802 ? ? 'expression tag'        -3  21 
1 9HNF GLY A 22 ? UNP A1B802 ? ? 'expression tag'        -2  22 
1 9HNF SER A 23 ? UNP A1B802 ? ? 'expression tag'        -1  23 
1 9HNF ARG A 24 ? UNP A1B802 ? ? 'expression tag'        0   24 
2 9HNF MET B 1  ? UNP A1B802 ? ? 'initiating methionine' -23 25 
2 9HNF GLY B 2  ? UNP A1B802 ? ? 'expression tag'        -22 26 
2 9HNF HIS B 3  ? UNP A1B802 ? ? 'expression tag'        -21 27 
2 9HNF HIS B 4  ? UNP A1B802 ? ? 'expression tag'        -20 28 
2 9HNF HIS B 5  ? UNP A1B802 ? ? 'expression tag'        -19 29 
2 9HNF HIS B 6  ? UNP A1B802 ? ? 'expression tag'        -18 30 
2 9HNF HIS B 7  ? UNP A1B802 ? ? 'expression tag'        -17 31 
2 9HNF HIS B 8  ? UNP A1B802 ? ? 'expression tag'        -16 32 
2 9HNF HIS B 9  ? UNP A1B802 ? ? 'expression tag'        -15 33 
2 9HNF HIS B 10 ? UNP A1B802 ? ? 'expression tag'        -14 34 
2 9HNF HIS B 11 ? UNP A1B802 ? ? 'expression tag'        -13 35 
2 9HNF HIS B 12 ? UNP A1B802 ? ? 'expression tag'        -12 36 
2 9HNF SER B 13 ? UNP A1B802 ? ? 'expression tag'        -11 37 
2 9HNF SER B 14 ? UNP A1B802 ? ? 'expression tag'        -10 38 
2 9HNF GLY B 15 ? UNP A1B802 ? ? 'expression tag'        -9  39 
2 9HNF HIS B 16 ? UNP A1B802 ? ? 'expression tag'        -8  40 
2 9HNF ILE B 17 ? UNP A1B802 ? ? 'expression tag'        -7  41 
2 9HNF GLU B 18 ? UNP A1B802 ? ? 'expression tag'        -6  42 
2 9HNF GLY B 19 ? UNP A1B802 ? ? 'expression tag'        -5  43 
2 9HNF ARG B 20 ? UNP A1B802 ? ? 'expression tag'        -4  44 
2 9HNF HIS B 21 ? UNP A1B802 ? ? 'expression tag'        -3  45 
2 9HNF GLY B 22 ? UNP A1B802 ? ? 'expression tag'        -2  46 
2 9HNF SER B 23 ? UNP A1B802 ? ? 'expression tag'        -1  47 
2 9HNF ARG B 24 ? UNP A1B802 ? ? 'expression tag'        0   48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 16470 ? 
1 MORE         -168  ? 
1 'SSA (A^2)'  38640 ? 
# 
_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 
# 
_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' 4_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 
# 
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 THR A 43  ? SER A 47  ? THR A 19  SER A 23  5 ? 5  
HELX_P HELX_P2  AA2 SER A 53  ? GLY A 68  ? SER A 29  GLY A 44  1 ? 16 
HELX_P HELX_P3  AA3 SER A 87  ? SER A 102 ? SER A 63  SER A 78  1 ? 16 
HELX_P HELX_P4  AA4 SER A 117 ? ILE A 122 ? SER A 93  ILE A 98  1 ? 6  
HELX_P HELX_P5  AA5 ILE A 122 ? ARG A 129 ? ILE A 98  ARG A 105 1 ? 8  
HELX_P HELX_P6  AA6 PHE A 145 ? GLU A 152 ? PHE A 121 GLU A 128 1 ? 8  
HELX_P HELX_P7  AA7 SER A 153 ? LEU A 155 ? SER A 129 LEU A 131 5 ? 3  
HELX_P HELX_P8  AA8 HIS A 157 ? ASN A 166 ? HIS A 133 ASN A 142 1 ? 10 
HELX_P HELX_P9  AA9 THR A 174 ? ALA A 187 ? THR A 150 ALA A 163 1 ? 14 
HELX_P HELX_P10 AB1 ASP A 198 ? ARG A 211 ? ASP A 174 ARG A 187 1 ? 14 
HELX_P HELX_P11 AB2 HIS A 233 ? GLY A 249 ? HIS A 209 GLY A 225 1 ? 17 
HELX_P HELX_P12 AB3 ASN A 262 ? MET A 273 ? ASN A 238 MET A 249 1 ? 12 
HELX_P HELX_P13 AB4 THR A 295 ? LEU A 310 ? THR A 271 LEU A 286 1 ? 16 
HELX_P HELX_P14 AB5 THR A 316 ? ALA A 325 ? THR A 292 ALA A 301 1 ? 10 
HELX_P HELX_P15 AB6 THR B 43  ? SER B 47  ? THR B 19  SER B 23  5 ? 5  
HELX_P HELX_P16 AB7 SER B 53  ? GLY B 68  ? SER B 29  GLY B 44  1 ? 16 
HELX_P HELX_P17 AB8 VAL B 88  ? ALA B 90  ? VAL B 64  ALA B 66  5 ? 3  
HELX_P HELX_P18 AB9 PHE B 91  ? SER B 102 ? PHE B 67  SER B 78  1 ? 12 
HELX_P HELX_P19 AC1 ILE B 122 ? ARG B 129 ? ILE B 98  ARG B 105 1 ? 8  
HELX_P HELX_P20 AC2 PRO B 146 ? GLU B 152 ? PRO B 122 GLU B 128 1 ? 7  
HELX_P HELX_P21 AC3 SER B 153 ? LEU B 155 ? SER B 129 LEU B 131 5 ? 3  
HELX_P HELX_P22 AC4 HIS B 157 ? ASN B 166 ? HIS B 133 ASN B 142 1 ? 10 
HELX_P HELX_P23 AC5 THR B 174 ? ALA B 187 ? THR B 150 ALA B 163 1 ? 14 
HELX_P HELX_P24 AC6 ASP B 198 ? GLY B 212 ? ASP B 174 GLY B 188 1 ? 15 
HELX_P HELX_P25 AC7 HIS B 233 ? GLY B 249 ? HIS B 209 GLY B 225 1 ? 17 
HELX_P HELX_P26 AC8 ASN B 262 ? MET B 273 ? ASN B 238 MET B 249 1 ? 12 
HELX_P HELX_P27 AC9 THR B 295 ? LEU B 310 ? THR B 271 LEU B 286 1 ? 16 
HELX_P HELX_P28 AD1 THR B 316 ? ALA B 325 ? THR B 292 ALA B 301 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 73  NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 49  A ZN 403 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc2  metalc ? ? A HIS 75  NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 51  A ZN 403 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc3  metalc ? ? A GLU 282 OE2 ? ? ? 1_555 E ZN . ZN ? ? A GLU 258 A ZN 403 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc4  metalc ? ? D AAE .   O1  ? ? ? 1_555 E ZN . ZN ? ? A AAE 402 A ZN 403 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc5  metalc ? ? D AAE .   O8  ? ? ? 1_555 E ZN . ZN ? ? A AAE 402 A ZN 403 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc6  metalc ? ? B HIS 73  NE2 ? ? ? 1_555 H ZN . ZN ? ? B HIS 49  B ZN 403 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc7  metalc ? ? B HIS 75  NE2 ? ? ? 1_555 H ZN . ZN ? ? B HIS 51  B ZN 403 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc8  metalc ? ? B GLU 282 OE2 ? ? ? 1_555 H ZN . ZN ? ? B GLU 258 B ZN 403 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc9  metalc ? ? G AAE .   O1  ? ? ? 1_555 H ZN . ZN ? ? B AAE 402 B ZN 403 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc10 metalc ? ? G AAE .   O8  ? ? ? 1_555 H ZN . ZN ? ? B AAE 402 B ZN 403 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 73  ? A HIS 49  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 NE2 ? A HIS 75  ? A HIS 51  ? 1_555 95.9  ? 
2  NE2 ? A HIS 73  ? A HIS 49  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 OE2 ? A GLU 282 ? A GLU 258 ? 1_555 120.9 ? 
3  NE2 ? A HIS 75  ? A HIS 51  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 OE2 ? A GLU 282 ? A GLU 258 ? 1_555 100.6 ? 
4  NE2 ? A HIS 73  ? A HIS 49  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O1  ? D AAE .   ? A AAE 402 ? 1_555 82.8  ? 
5  NE2 ? A HIS 75  ? A HIS 51  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O1  ? D AAE .   ? A AAE 402 ? 1_555 87.0  ? 
6  OE2 ? A GLU 282 ? A GLU 258 ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O1  ? D AAE .   ? A AAE 402 ? 1_555 153.7 ? 
7  NE2 ? A HIS 73  ? A HIS 49  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O8  ? D AAE .   ? A AAE 402 ? 1_555 92.2  ? 
8  NE2 ? A HIS 75  ? A HIS 51  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O8  ? D AAE .   ? A AAE 402 ? 1_555 166.2 ? 
9  OE2 ? A GLU 282 ? A GLU 258 ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O8  ? D AAE .   ? A AAE 402 ? 1_555 84.6  ? 
10 O1  ? D AAE .   ? A AAE 402 ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 O8  ? D AAE .   ? A AAE 402 ? 1_555 83.0  ? 
11 NE2 ? B HIS 73  ? B HIS 49  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 NE2 ? B HIS 75  ? B HIS 51  ? 1_555 94.5  ? 
12 NE2 ? B HIS 73  ? B HIS 49  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 OE2 ? B GLU 282 ? B GLU 258 ? 1_555 112.2 ? 
13 NE2 ? B HIS 75  ? B HIS 51  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 OE2 ? B GLU 282 ? B GLU 258 ? 1_555 102.7 ? 
14 NE2 ? B HIS 73  ? B HIS 49  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O1  ? G AAE .   ? B AAE 402 ? 1_555 92.4  ? 
15 NE2 ? B HIS 75  ? B HIS 51  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O1  ? G AAE .   ? B AAE 402 ? 1_555 92.3  ? 
16 OE2 ? B GLU 282 ? B GLU 258 ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O1  ? G AAE .   ? B AAE 402 ? 1_555 149.7 ? 
17 NE2 ? B HIS 73  ? B HIS 49  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O8  ? G AAE .   ? B AAE 402 ? 1_555 91.8  ? 
18 NE2 ? B HIS 75  ? B HIS 51  ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O8  ? G AAE .   ? B AAE 402 ? 1_555 167.4 ? 
19 OE2 ? B GLU 282 ? B GLU 258 ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O8  ? G AAE .   ? B AAE 402 ? 1_555 84.9  ? 
20 O1  ? G AAE .   ? B AAE 402 ? 1_555 ZN ? H ZN . ? B ZN 403 ? 1_555 O8  ? G AAE .   ? B AAE 402 ? 1_555 76.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 216 A . ? GLY 192 A PRO 217 A ? PRO 193 A 1 -1.86 
2 GLY 216 B . ? GLY 192 B PRO 217 B ? PRO 193 B 1 -1.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 9 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? parallel      
AA6 8 9 ? parallel      
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 30  ? VAL A 31  ? LYS A 6   VAL A 7   
AA1 2 GLU A 313 ? VAL A 314 ? GLU A 289 VAL A 290 
AA2 1 ILE A 33  ? ALA A 36  ? ILE A 9   ALA A 12  
AA2 2 VAL A 71  ? LEU A 74  ? VAL A 47  LEU A 50  
AA2 3 VAL A 105 ? ILE A 108 ? VAL A 81  ILE A 84  
AA2 4 LEU A 132 ? ASN A 136 ? LEU A 108 ASN A 112 
AA2 5 ARG A 191 ? CYS A 196 ? ARG A 167 CYS A 172 
AA2 6 LEU A 218 ? PHE A 224 ? LEU A 194 PHE A 200 
AA2 7 TYR A 252 ? GLY A 258 ? TYR A 228 GLY A 234 
AA2 8 HIS A 276 ? VAL A 279 ? HIS A 252 VAL A 255 
AA2 9 ILE A 33  ? ALA A 36  ? ILE A 9   ALA A 12  
AA3 1 MET A 140 ? ASN A 141 ? MET A 116 ASN A 117 
AA3 2 ILE A 170 ? PHE A 171 ? ILE A 146 PHE A 147 
AA4 1 TRP A 286 ? GLY A 288 ? TRP A 262 GLY A 264 
AA4 2 ARG A 291 ? LEU A 292 ? ARG A 267 LEU A 268 
AA5 1 LYS B 30  ? VAL B 31  ? LYS B 6   VAL B 7   
AA5 2 GLU B 313 ? VAL B 314 ? GLU B 289 VAL B 290 
AA6 1 ILE B 33  ? ALA B 36  ? ILE B 9   ALA B 12  
AA6 2 VAL B 71  ? LEU B 74  ? VAL B 47  LEU B 50  
AA6 3 VAL B 105 ? ILE B 108 ? VAL B 81  ILE B 84  
AA6 4 LEU B 132 ? ASN B 136 ? LEU B 108 ASN B 112 
AA6 5 ARG B 191 ? CYS B 196 ? ARG B 167 CYS B 172 
AA6 6 LEU B 218 ? PHE B 224 ? LEU B 194 PHE B 200 
AA6 7 TYR B 252 ? GLY B 258 ? TYR B 228 GLY B 234 
AA6 8 HIS B 276 ? VAL B 279 ? HIS B 252 VAL B 255 
AA6 9 ILE B 33  ? ALA B 36  ? ILE B 9   ALA B 12  
AA7 1 MET B 140 ? ASN B 141 ? MET B 116 ASN B 117 
AA7 2 ILE B 170 ? PHE B 171 ? ILE B 146 PHE B 147 
# 
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 VAL A 31  ? N VAL A 7   O GLU A 313 ? O GLU A 289 
AA2 1 2 N CYS A 35  ? N CYS A 11  O VAL A 71  ? O VAL A 47  
AA2 2 3 N ILE A 72  ? N ILE A 48  O ASN A 107 ? O ASN A 83  
AA2 3 4 N ILE A 108 ? N ILE A 84  O LEU A 132 ? O LEU A 108 
AA2 4 5 N LEU A 135 ? N LEU A 111 O GLU A 193 ? O GLU A 169 
AA2 5 6 N CYS A 196 ? N CYS A 172 O GLN A 221 ? O GLN A 197 
AA2 6 7 N LEU A 218 ? N LEU A 194 O ARG A 253 ? O ARG A 229 
AA2 7 8 N TRP A 254 ? N TRP A 230 O HIS A 276 ? O HIS A 252 
AA2 8 9 O VAL A 279 ? O VAL A 255 N THR A 34  ? N THR A 10  
AA3 1 2 N MET A 140 ? N MET A 116 O PHE A 171 ? O PHE A 147 
AA4 1 2 N ALA A 287 ? N ALA A 263 O ARG A 291 ? O ARG A 267 
AA5 1 2 N VAL B 31  ? N VAL B 7   O GLU B 313 ? O GLU B 289 
AA6 1 2 N CYS B 35  ? N CYS B 11  O HIS B 73  ? O HIS B 49  
AA6 2 3 N ILE B 72  ? N ILE B 48  O ASN B 107 ? O ASN B 83  
AA6 3 4 N ILE B 108 ? N ILE B 84  O LEU B 132 ? O LEU B 108 
AA6 4 5 N LEU B 135 ? N LEU B 111 O GLU B 195 ? O GLU B 171 
AA6 5 6 N CYS B 196 ? N CYS B 172 O GLN B 221 ? O GLN B 197 
AA6 6 7 N LEU B 218 ? N LEU B 194 O ARG B 253 ? O ARG B 229 
AA6 7 8 N TRP B 254 ? N TRP B 230 O HIS B 276 ? O HIS B 252 
AA6 8 9 O VAL B 279 ? O VAL B 255 N THR B 34  ? N THR B 10  
AA7 1 2 N MET B 140 ? N MET B 116 O PHE B 171 ? O PHE B 147 
# 
_pdbx_entry_details.entry_id                   9HNF 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 3   ? ? -68.60  0.89   
2  1 THR A 14  ? ? -148.58 -43.38 
3  1 VAL A 28  ? ? -122.07 -58.03 
4  1 ASN A 149 ? ? -150.96 71.48  
5  1 ASN A 309 ? ? -103.46 55.25  
6  1 THR B 14  ? ? -151.24 -41.29 
7  1 VAL B 28  ? ? -126.91 -64.42 
8  1 ILE B 94  ? ? -102.52 -79.56 
9  1 ASN B 149 ? ? -153.93 74.46  
10 1 GLN B 307 ? ? -102.04 44.13  
11 1 ASN B 309 ? ? -108.65 53.73  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         5.0053 
_pdbx_refine_tls.origin_y         -13.2895 
_pdbx_refine_tls.origin_z         10.7673 
_pdbx_refine_tls.T[1][1]          0.2903 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0015 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0019 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2568 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0118 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2540 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.1616 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1417 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0861 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6134 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2203 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.5632 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0480 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1467 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0707 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0004 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0453 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0159 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0701 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0259 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0021 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -23 ? A MET 1  
2  1 Y 1 A GLY -22 ? A GLY 2  
3  1 Y 1 A HIS -21 ? A HIS 3  
4  1 Y 1 A HIS -20 ? A HIS 4  
5  1 Y 1 A HIS -19 ? A HIS 5  
6  1 Y 1 A HIS -18 ? A HIS 6  
7  1 Y 1 A HIS -17 ? A HIS 7  
8  1 Y 1 A HIS -16 ? A HIS 8  
9  1 Y 1 A HIS -15 ? A HIS 9  
10 1 Y 1 A HIS -14 ? A HIS 10 
11 1 Y 1 A HIS -13 ? A HIS 11 
12 1 Y 1 A HIS -12 ? A HIS 12 
13 1 Y 1 A SER -11 ? A SER 13 
14 1 Y 1 A SER -10 ? A SER 14 
15 1 Y 1 A GLY -9  ? A GLY 15 
16 1 Y 1 A HIS -8  ? A HIS 16 
17 1 Y 1 A ILE -7  ? A ILE 17 
18 1 Y 1 A GLU -6  ? A GLU 18 
19 1 Y 1 A GLY -5  ? A GLY 19 
20 1 Y 1 A ARG -4  ? A ARG 20 
21 1 Y 1 A HIS -3  ? A HIS 21 
22 1 Y 1 A GLY -2  ? A GLY 22 
23 1 Y 1 A SER -1  ? A SER 23 
24 1 Y 1 A ARG 0   ? A ARG 24 
25 1 Y 1 A MET 1   ? A MET 25 
26 1 Y 1 B MET -23 ? B MET 1  
27 1 Y 1 B GLY -22 ? B GLY 2  
28 1 Y 1 B HIS -21 ? B HIS 3  
29 1 Y 1 B HIS -20 ? B HIS 4  
30 1 Y 1 B HIS -19 ? B HIS 5  
31 1 Y 1 B HIS -18 ? B HIS 6  
32 1 Y 1 B HIS -17 ? B HIS 7  
33 1 Y 1 B HIS -16 ? B HIS 8  
34 1 Y 1 B HIS -15 ? B HIS 9  
35 1 Y 1 B HIS -14 ? B HIS 10 
36 1 Y 1 B HIS -13 ? B HIS 11 
37 1 Y 1 B HIS -12 ? B HIS 12 
38 1 Y 1 B SER -11 ? B SER 13 
39 1 Y 1 B SER -10 ? B SER 14 
40 1 Y 1 B GLY -9  ? B GLY 15 
41 1 Y 1 B HIS -8  ? B HIS 16 
42 1 Y 1 B ILE -7  ? B ILE 17 
43 1 Y 1 B GLU -6  ? B GLU 18 
44 1 Y 1 B GLY -5  ? B GLY 19 
45 1 Y 1 B ARG -4  ? B ARG 20 
46 1 Y 1 B HIS -3  ? B HIS 21 
47 1 Y 1 B GLY -2  ? B GLY 22 
48 1 Y 1 B SER -1  ? B SER 23 
49 1 Y 1 B ARG 0   ? B ARG 24 
50 1 Y 1 B MET 1   ? B MET 25 
51 1 Y 1 B SER 2   ? B SER 26 
# 
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 
AAE O1   O  N N 1   
AAE C2   C  N N 2   
AAE O3   O  N N 3   
AAE C4   C  N N 4   
AAE C5   C  N N 5   
AAE O8   O  N N 6   
AAE C9   C  N N 7   
AAE HO1  H  N N 8   
AAE H41  H  N N 9   
AAE H42  H  N N 10  
AAE H91  H  N N 11  
AAE H92  H  N N 12  
AAE H93  H  N N 13  
ACO N1A  N  Y N 14  
ACO C2A  C  Y N 15  
ACO N3A  N  Y N 16  
ACO C4A  C  Y N 17  
ACO C5A  C  Y N 18  
ACO C6A  C  Y N 19  
ACO N6A  N  N N 20  
ACO N7A  N  Y N 21  
ACO C8A  C  Y N 22  
ACO N9A  N  Y N 23  
ACO C1B  C  N R 24  
ACO C2B  C  N R 25  
ACO O2B  O  N N 26  
ACO C3B  C  N S 27  
ACO O3B  O  N N 28  
ACO P3B  P  N N 29  
ACO O7A  O  N N 30  
ACO O8A  O  N N 31  
ACO O9A  O  N N 32  
ACO C4B  C  N R 33  
ACO O4B  O  N N 34  
ACO C5B  C  N N 35  
ACO O5B  O  N N 36  
ACO P1A  P  N S 37  
ACO O1A  O  N N 38  
ACO O2A  O  N N 39  
ACO O3A  O  N N 40  
ACO P2A  P  N S 41  
ACO O4A  O  N N 42  
ACO O5A  O  N N 43  
ACO O6A  O  N N 44  
ACO CBP  C  N N 45  
ACO CCP  C  N N 46  
ACO CDP  C  N N 47  
ACO CEP  C  N N 48  
ACO CAP  C  N R 49  
ACO OAP  O  N N 50  
ACO C9P  C  N N 51  
ACO O9P  O  N N 52  
ACO N8P  N  N N 53  
ACO C7P  C  N N 54  
ACO C6P  C  N N 55  
ACO C5P  C  N N 56  
ACO O5P  O  N N 57  
ACO N4P  N  N N 58  
ACO C3P  C  N N 59  
ACO C2P  C  N N 60  
ACO S1P  S  N N 61  
ACO C    C  N N 62  
ACO O    O  N N 63  
ACO CH3  C  N N 64  
ACO H2A  H  N N 65  
ACO H61A H  N N 66  
ACO H62A H  N N 67  
ACO H8A  H  N N 68  
ACO H1B  H  N N 69  
ACO H2B  H  N N 70  
ACO HO2A H  N N 71  
ACO H3B  H  N N 72  
ACO HOA8 H  N N 73  
ACO HOA9 H  N N 74  
ACO H4B  H  N N 75  
ACO H51A H  N N 76  
ACO H52A H  N N 77  
ACO HOA2 H  N N 78  
ACO HOA5 H  N N 79  
ACO H121 H  N N 80  
ACO H122 H  N N 81  
ACO H131 H  N N 82  
ACO H132 H  N N 83  
ACO H133 H  N N 84  
ACO H141 H  N N 85  
ACO H142 H  N N 86  
ACO H143 H  N N 87  
ACO H10  H  N N 88  
ACO HO1  H  N N 89  
ACO HN8  H  N N 90  
ACO H71  H  N N 91  
ACO H72  H  N N 92  
ACO H61  H  N N 93  
ACO H62  H  N N 94  
ACO HN4  H  N N 95  
ACO H31  H  N N 96  
ACO H32  H  N N 97  
ACO H21  H  N N 98  
ACO H22  H  N N 99  
ACO HH31 H  N N 100 
ACO HH32 H  N N 101 
ACO HH33 H  N N 102 
ALA N    N  N N 103 
ALA CA   C  N S 104 
ALA C    C  N N 105 
ALA O    O  N N 106 
ALA CB   C  N N 107 
ALA OXT  O  N N 108 
ALA H    H  N N 109 
ALA H2   H  N N 110 
ALA HA   H  N N 111 
ALA HB1  H  N N 112 
ALA HB2  H  N N 113 
ALA HB3  H  N N 114 
ALA HXT  H  N N 115 
ARG N    N  N N 116 
ARG CA   C  N S 117 
ARG C    C  N N 118 
ARG O    O  N N 119 
ARG CB   C  N N 120 
ARG CG   C  N N 121 
ARG CD   C  N N 122 
ARG NE   N  N N 123 
ARG CZ   C  N N 124 
ARG NH1  N  N N 125 
ARG NH2  N  N N 126 
ARG OXT  O  N N 127 
ARG H    H  N N 128 
ARG H2   H  N N 129 
ARG HA   H  N N 130 
ARG HB2  H  N N 131 
ARG HB3  H  N N 132 
ARG HG2  H  N N 133 
ARG HG3  H  N N 134 
ARG HD2  H  N N 135 
ARG HD3  H  N N 136 
ARG HE   H  N N 137 
ARG HH11 H  N N 138 
ARG HH12 H  N N 139 
ARG HH21 H  N N 140 
ARG HH22 H  N N 141 
ARG HXT  H  N N 142 
ASN N    N  N N 143 
ASN CA   C  N S 144 
ASN C    C  N N 145 
ASN O    O  N N 146 
ASN CB   C  N N 147 
ASN CG   C  N N 148 
ASN OD1  O  N N 149 
ASN ND2  N  N N 150 
ASN OXT  O  N N 151 
ASN H    H  N N 152 
ASN H2   H  N N 153 
ASN HA   H  N N 154 
ASN HB2  H  N N 155 
ASN HB3  H  N N 156 
ASN HD21 H  N N 157 
ASN HD22 H  N N 158 
ASN HXT  H  N N 159 
ASP N    N  N N 160 
ASP CA   C  N S 161 
ASP C    C  N N 162 
ASP O    O  N N 163 
ASP CB   C  N N 164 
ASP CG   C  N N 165 
ASP OD1  O  N N 166 
ASP OD2  O  N N 167 
ASP OXT  O  N N 168 
ASP H    H  N N 169 
ASP H2   H  N N 170 
ASP HA   H  N N 171 
ASP HB2  H  N N 172 
ASP HB3  H  N N 173 
ASP HD2  H  N N 174 
ASP HXT  H  N N 175 
CYS N    N  N N 176 
CYS CA   C  N R 177 
CYS C    C  N N 178 
CYS O    O  N N 179 
CYS CB   C  N N 180 
CYS SG   S  N N 181 
CYS OXT  O  N N 182 
CYS H    H  N N 183 
CYS H2   H  N N 184 
CYS HA   H  N N 185 
CYS HB2  H  N N 186 
CYS HB3  H  N N 187 
CYS HG   H  N N 188 
CYS HXT  H  N N 189 
GLN N    N  N N 190 
GLN CA   C  N S 191 
GLN C    C  N N 192 
GLN O    O  N N 193 
GLN CB   C  N N 194 
GLN CG   C  N N 195 
GLN CD   C  N N 196 
GLN OE1  O  N N 197 
GLN NE2  N  N N 198 
GLN OXT  O  N N 199 
GLN H    H  N N 200 
GLN H2   H  N N 201 
GLN HA   H  N N 202 
GLN HB2  H  N N 203 
GLN HB3  H  N N 204 
GLN HG2  H  N N 205 
GLN HG3  H  N N 206 
GLN HE21 H  N N 207 
GLN HE22 H  N N 208 
GLN HXT  H  N N 209 
GLU N    N  N N 210 
GLU CA   C  N S 211 
GLU C    C  N N 212 
GLU O    O  N N 213 
GLU CB   C  N N 214 
GLU CG   C  N N 215 
GLU CD   C  N N 216 
GLU OE1  O  N N 217 
GLU OE2  O  N N 218 
GLU OXT  O  N N 219 
GLU H    H  N N 220 
GLU H2   H  N N 221 
GLU HA   H  N N 222 
GLU HB2  H  N N 223 
GLU HB3  H  N N 224 
GLU HG2  H  N N 225 
GLU HG3  H  N N 226 
GLU HE2  H  N N 227 
GLU HXT  H  N N 228 
GLY N    N  N N 229 
GLY CA   C  N N 230 
GLY C    C  N N 231 
GLY O    O  N N 232 
GLY OXT  O  N N 233 
GLY H    H  N N 234 
GLY H2   H  N N 235 
GLY HA2  H  N N 236 
GLY HA3  H  N N 237 
GLY HXT  H  N N 238 
HIS N    N  N N 239 
HIS CA   C  N S 240 
HIS C    C  N N 241 
HIS O    O  N N 242 
HIS CB   C  N N 243 
HIS CG   C  Y N 244 
HIS ND1  N  Y N 245 
HIS CD2  C  Y N 246 
HIS CE1  C  Y N 247 
HIS NE2  N  Y N 248 
HIS OXT  O  N N 249 
HIS H    H  N N 250 
HIS H2   H  N N 251 
HIS HA   H  N N 252 
HIS HB2  H  N N 253 
HIS HB3  H  N N 254 
HIS HD1  H  N N 255 
HIS HD2  H  N N 256 
HIS HE1  H  N N 257 
HIS HE2  H  N N 258 
HIS HXT  H  N N 259 
HOH O    O  N N 260 
HOH H1   H  N N 261 
HOH H2   H  N N 262 
ILE N    N  N N 263 
ILE CA   C  N S 264 
ILE C    C  N N 265 
ILE O    O  N N 266 
ILE CB   C  N S 267 
ILE CG1  C  N N 268 
ILE CG2  C  N N 269 
ILE CD1  C  N N 270 
ILE OXT  O  N N 271 
ILE H    H  N N 272 
ILE H2   H  N N 273 
ILE HA   H  N N 274 
ILE HB   H  N N 275 
ILE HG12 H  N N 276 
ILE HG13 H  N N 277 
ILE HG21 H  N N 278 
ILE HG22 H  N N 279 
ILE HG23 H  N N 280 
ILE HD11 H  N N 281 
ILE HD12 H  N N 282 
ILE HD13 H  N N 283 
ILE HXT  H  N N 284 
LEU N    N  N N 285 
LEU CA   C  N S 286 
LEU C    C  N N 287 
LEU O    O  N N 288 
LEU CB   C  N N 289 
LEU CG   C  N N 290 
LEU CD1  C  N N 291 
LEU CD2  C  N N 292 
LEU OXT  O  N N 293 
LEU H    H  N N 294 
LEU H2   H  N N 295 
LEU HA   H  N N 296 
LEU HB2  H  N N 297 
LEU HB3  H  N N 298 
LEU HG   H  N N 299 
LEU HD11 H  N N 300 
LEU HD12 H  N N 301 
LEU HD13 H  N N 302 
LEU HD21 H  N N 303 
LEU HD22 H  N N 304 
LEU HD23 H  N N 305 
LEU HXT  H  N N 306 
LYS N    N  N N 307 
LYS CA   C  N S 308 
LYS C    C  N N 309 
LYS O    O  N N 310 
LYS CB   C  N N 311 
LYS CG   C  N N 312 
LYS CD   C  N N 313 
LYS CE   C  N N 314 
LYS NZ   N  N N 315 
LYS OXT  O  N N 316 
LYS H    H  N N 317 
LYS H2   H  N N 318 
LYS HA   H  N N 319 
LYS HB2  H  N N 320 
LYS HB3  H  N N 321 
LYS HG2  H  N N 322 
LYS HG3  H  N N 323 
LYS HD2  H  N N 324 
LYS HD3  H  N N 325 
LYS HE2  H  N N 326 
LYS HE3  H  N N 327 
LYS HZ1  H  N N 328 
LYS HZ2  H  N N 329 
LYS HZ3  H  N N 330 
LYS HXT  H  N N 331 
MET N    N  N N 332 
MET CA   C  N S 333 
MET C    C  N N 334 
MET O    O  N N 335 
MET CB   C  N N 336 
MET CG   C  N N 337 
MET SD   S  N N 338 
MET CE   C  N N 339 
MET OXT  O  N N 340 
MET H    H  N N 341 
MET H2   H  N N 342 
MET HA   H  N N 343 
MET HB2  H  N N 344 
MET HB3  H  N N 345 
MET HG2  H  N N 346 
MET HG3  H  N N 347 
MET HE1  H  N N 348 
MET HE2  H  N N 349 
MET HE3  H  N N 350 
MET HXT  H  N N 351 
PHE N    N  N N 352 
PHE CA   C  N S 353 
PHE C    C  N N 354 
PHE O    O  N N 355 
PHE CB   C  N N 356 
PHE CG   C  Y N 357 
PHE CD1  C  Y N 358 
PHE CD2  C  Y N 359 
PHE CE1  C  Y N 360 
PHE CE2  C  Y N 361 
PHE CZ   C  Y N 362 
PHE OXT  O  N N 363 
PHE H    H  N N 364 
PHE H2   H  N N 365 
PHE HA   H  N N 366 
PHE HB2  H  N N 367 
PHE HB3  H  N N 368 
PHE HD1  H  N N 369 
PHE HD2  H  N N 370 
PHE HE1  H  N N 371 
PHE HE2  H  N N 372 
PHE HZ   H  N N 373 
PHE HXT  H  N N 374 
PRO N    N  N N 375 
PRO CA   C  N S 376 
PRO C    C  N N 377 
PRO O    O  N N 378 
PRO CB   C  N N 379 
PRO CG   C  N N 380 
PRO CD   C  N N 381 
PRO OXT  O  N N 382 
PRO H    H  N N 383 
PRO HA   H  N N 384 
PRO HB2  H  N N 385 
PRO HB3  H  N N 386 
PRO HG2  H  N N 387 
PRO HG3  H  N N 388 
PRO HD2  H  N N 389 
PRO HD3  H  N N 390 
PRO HXT  H  N N 391 
SER N    N  N N 392 
SER CA   C  N S 393 
SER C    C  N N 394 
SER O    O  N N 395 
SER CB   C  N N 396 
SER OG   O  N N 397 
SER OXT  O  N N 398 
SER H    H  N N 399 
SER H2   H  N N 400 
SER HA   H  N N 401 
SER HB2  H  N N 402 
SER HB3  H  N N 403 
SER HG   H  N N 404 
SER HXT  H  N N 405 
THR N    N  N N 406 
THR CA   C  N S 407 
THR C    C  N N 408 
THR O    O  N N 409 
THR CB   C  N R 410 
THR OG1  O  N N 411 
THR CG2  C  N N 412 
THR OXT  O  N N 413 
THR H    H  N N 414 
THR H2   H  N N 415 
THR HA   H  N N 416 
THR HB   H  N N 417 
THR HG1  H  N N 418 
THR HG21 H  N N 419 
THR HG22 H  N N 420 
THR HG23 H  N N 421 
THR HXT  H  N N 422 
TRP N    N  N N 423 
TRP CA   C  N S 424 
TRP C    C  N N 425 
TRP O    O  N N 426 
TRP CB   C  N N 427 
TRP CG   C  Y N 428 
TRP CD1  C  Y N 429 
TRP CD2  C  Y N 430 
TRP NE1  N  Y N 431 
TRP CE2  C  Y N 432 
TRP CE3  C  Y N 433 
TRP CZ2  C  Y N 434 
TRP CZ3  C  Y N 435 
TRP CH2  C  Y N 436 
TRP OXT  O  N N 437 
TRP H    H  N N 438 
TRP H2   H  N N 439 
TRP HA   H  N N 440 
TRP HB2  H  N N 441 
TRP HB3  H  N N 442 
TRP HD1  H  N N 443 
TRP HE1  H  N N 444 
TRP HE3  H  N N 445 
TRP HZ2  H  N N 446 
TRP HZ3  H  N N 447 
TRP HH2  H  N N 448 
TRP HXT  H  N N 449 
TYR N    N  N N 450 
TYR CA   C  N S 451 
TYR C    C  N N 452 
TYR O    O  N N 453 
TYR CB   C  N N 454 
TYR CG   C  Y N 455 
TYR CD1  C  Y N 456 
TYR CD2  C  Y N 457 
TYR CE1  C  Y N 458 
TYR CE2  C  Y N 459 
TYR CZ   C  Y N 460 
TYR OH   O  N N 461 
TYR OXT  O  N N 462 
TYR H    H  N N 463 
TYR H2   H  N N 464 
TYR HA   H  N N 465 
TYR HB2  H  N N 466 
TYR HB3  H  N N 467 
TYR HD1  H  N N 468 
TYR HD2  H  N N 469 
TYR HE1  H  N N 470 
TYR HE2  H  N N 471 
TYR HH   H  N N 472 
TYR HXT  H  N N 473 
VAL N    N  N N 474 
VAL CA   C  N S 475 
VAL C    C  N N 476 
VAL O    O  N N 477 
VAL CB   C  N N 478 
VAL CG1  C  N N 479 
VAL CG2  C  N N 480 
VAL OXT  O  N N 481 
VAL H    H  N N 482 
VAL H2   H  N N 483 
VAL HA   H  N N 484 
VAL HB   H  N N 485 
VAL HG11 H  N N 486 
VAL HG12 H  N N 487 
VAL HG13 H  N N 488 
VAL HG21 H  N N 489 
VAL HG22 H  N N 490 
VAL HG23 H  N N 491 
VAL HXT  H  N N 492 
ZN  ZN   ZN N N 493 
# 
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 
AAE O1  C2   sing N N 1   
AAE O1  HO1  sing N N 2   
AAE C2  O3   doub N N 3   
AAE C2  C4   sing N N 4   
AAE C4  C5   sing N N 5   
AAE C4  H41  sing N N 6   
AAE C4  H42  sing N N 7   
AAE C5  O8   doub N N 8   
AAE C5  C9   sing N N 9   
AAE C9  H91  sing N N 10  
AAE C9  H92  sing N N 11  
AAE C9  H93  sing N N 12  
ACO N1A C2A  sing Y N 13  
ACO N1A C6A  doub Y N 14  
ACO C2A N3A  doub Y N 15  
ACO C2A H2A  sing N N 16  
ACO N3A C4A  sing Y N 17  
ACO C4A C5A  doub Y N 18  
ACO C4A N9A  sing Y N 19  
ACO C5A C6A  sing Y N 20  
ACO C5A N7A  sing Y N 21  
ACO C6A N6A  sing N N 22  
ACO N6A H61A sing N N 23  
ACO N6A H62A sing N N 24  
ACO N7A C8A  doub Y N 25  
ACO C8A N9A  sing Y N 26  
ACO C8A H8A  sing N N 27  
ACO N9A C1B  sing N N 28  
ACO C1B C2B  sing N N 29  
ACO C1B O4B  sing N N 30  
ACO C1B H1B  sing N N 31  
ACO C2B O2B  sing N N 32  
ACO C2B C3B  sing N N 33  
ACO C2B H2B  sing N N 34  
ACO O2B HO2A sing N N 35  
ACO C3B O3B  sing N N 36  
ACO C3B C4B  sing N N 37  
ACO C3B H3B  sing N N 38  
ACO O3B P3B  sing N N 39  
ACO P3B O7A  doub N N 40  
ACO P3B O8A  sing N N 41  
ACO P3B O9A  sing N N 42  
ACO O8A HOA8 sing N N 43  
ACO O9A HOA9 sing N N 44  
ACO C4B O4B  sing N N 45  
ACO C4B C5B  sing N N 46  
ACO C4B H4B  sing N N 47  
ACO C5B O5B  sing N N 48  
ACO C5B H51A sing N N 49  
ACO C5B H52A sing N N 50  
ACO O5B P1A  sing N N 51  
ACO P1A O1A  doub N N 52  
ACO P1A O2A  sing N N 53  
ACO P1A O3A  sing N N 54  
ACO O2A HOA2 sing N N 55  
ACO O3A P2A  sing N N 56  
ACO P2A O4A  doub N N 57  
ACO P2A O5A  sing N N 58  
ACO P2A O6A  sing N N 59  
ACO O5A HOA5 sing N N 60  
ACO O6A CCP  sing N N 61  
ACO CBP CCP  sing N N 62  
ACO CBP CDP  sing N N 63  
ACO CBP CEP  sing N N 64  
ACO CBP CAP  sing N N 65  
ACO CCP H121 sing N N 66  
ACO CCP H122 sing N N 67  
ACO CDP H131 sing N N 68  
ACO CDP H132 sing N N 69  
ACO CDP H133 sing N N 70  
ACO CEP H141 sing N N 71  
ACO CEP H142 sing N N 72  
ACO CEP H143 sing N N 73  
ACO CAP OAP  sing N N 74  
ACO CAP C9P  sing N N 75  
ACO CAP H10  sing N N 76  
ACO OAP HO1  sing N N 77  
ACO C9P O9P  doub N N 78  
ACO C9P N8P  sing N N 79  
ACO N8P C7P  sing N N 80  
ACO N8P HN8  sing N N 81  
ACO C7P C6P  sing N N 82  
ACO C7P H71  sing N N 83  
ACO C7P H72  sing N N 84  
ACO C6P C5P  sing N N 85  
ACO C6P H61  sing N N 86  
ACO C6P H62  sing N N 87  
ACO C5P O5P  doub N N 88  
ACO C5P N4P  sing N N 89  
ACO N4P C3P  sing N N 90  
ACO N4P HN4  sing N N 91  
ACO C3P C2P  sing N N 92  
ACO C3P H31  sing N N 93  
ACO C3P H32  sing N N 94  
ACO C2P S1P  sing N N 95  
ACO C2P H21  sing N N 96  
ACO C2P H22  sing N N 97  
ACO S1P C    sing N N 98  
ACO C   O    doub N N 99  
ACO C   CH3  sing N N 100 
ACO CH3 HH31 sing N N 101 
ACO CH3 HH32 sing N N 102 
ACO CH3 HH33 sing N N 103 
ALA N   CA   sing N N 104 
ALA N   H    sing N N 105 
ALA N   H2   sing N N 106 
ALA CA  C    sing N N 107 
ALA CA  CB   sing N N 108 
ALA CA  HA   sing N N 109 
ALA C   O    doub N N 110 
ALA C   OXT  sing N N 111 
ALA CB  HB1  sing N N 112 
ALA CB  HB2  sing N N 113 
ALA CB  HB3  sing N N 114 
ALA OXT HXT  sing N N 115 
ARG N   CA   sing N N 116 
ARG N   H    sing N N 117 
ARG N   H2   sing N N 118 
ARG CA  C    sing N N 119 
ARG CA  CB   sing N N 120 
ARG CA  HA   sing N N 121 
ARG C   O    doub N N 122 
ARG C   OXT  sing N N 123 
ARG CB  CG   sing N N 124 
ARG CB  HB2  sing N N 125 
ARG CB  HB3  sing N N 126 
ARG CG  CD   sing N N 127 
ARG CG  HG2  sing N N 128 
ARG CG  HG3  sing N N 129 
ARG CD  NE   sing N N 130 
ARG CD  HD2  sing N N 131 
ARG CD  HD3  sing N N 132 
ARG NE  CZ   sing N N 133 
ARG NE  HE   sing N N 134 
ARG CZ  NH1  sing N N 135 
ARG CZ  NH2  doub N N 136 
ARG NH1 HH11 sing N N 137 
ARG NH1 HH12 sing N N 138 
ARG NH2 HH21 sing N N 139 
ARG NH2 HH22 sing N N 140 
ARG OXT HXT  sing N N 141 
ASN N   CA   sing N N 142 
ASN N   H    sing N N 143 
ASN N   H2   sing N N 144 
ASN CA  C    sing N N 145 
ASN CA  CB   sing N N 146 
ASN CA  HA   sing N N 147 
ASN C   O    doub N N 148 
ASN C   OXT  sing N N 149 
ASN CB  CG   sing N N 150 
ASN CB  HB2  sing N N 151 
ASN CB  HB3  sing N N 152 
ASN CG  OD1  doub N N 153 
ASN CG  ND2  sing N N 154 
ASN ND2 HD21 sing N N 155 
ASN ND2 HD22 sing N N 156 
ASN OXT HXT  sing N N 157 
ASP N   CA   sing N N 158 
ASP N   H    sing N N 159 
ASP N   H2   sing N N 160 
ASP CA  C    sing N N 161 
ASP CA  CB   sing N N 162 
ASP CA  HA   sing N N 163 
ASP C   O    doub N N 164 
ASP C   OXT  sing N N 165 
ASP CB  CG   sing N N 166 
ASP CB  HB2  sing N N 167 
ASP CB  HB3  sing N N 168 
ASP CG  OD1  doub N N 169 
ASP CG  OD2  sing N N 170 
ASP OD2 HD2  sing N N 171 
ASP OXT HXT  sing N N 172 
CYS N   CA   sing N N 173 
CYS N   H    sing N N 174 
CYS N   H2   sing N N 175 
CYS CA  C    sing N N 176 
CYS CA  CB   sing N N 177 
CYS CA  HA   sing N N 178 
CYS C   O    doub N N 179 
CYS C   OXT  sing N N 180 
CYS CB  SG   sing N N 181 
CYS CB  HB2  sing N N 182 
CYS CB  HB3  sing N N 183 
CYS SG  HG   sing N N 184 
CYS OXT HXT  sing N N 185 
GLN N   CA   sing N N 186 
GLN N   H    sing N N 187 
GLN N   H2   sing N N 188 
GLN CA  C    sing N N 189 
GLN CA  CB   sing N N 190 
GLN CA  HA   sing N N 191 
GLN C   O    doub N N 192 
GLN C   OXT  sing N N 193 
GLN CB  CG   sing N N 194 
GLN CB  HB2  sing N N 195 
GLN CB  HB3  sing N N 196 
GLN CG  CD   sing N N 197 
GLN CG  HG2  sing N N 198 
GLN CG  HG3  sing N N 199 
GLN CD  OE1  doub N N 200 
GLN CD  NE2  sing N N 201 
GLN NE2 HE21 sing N N 202 
GLN NE2 HE22 sing N N 203 
GLN OXT HXT  sing N N 204 
GLU N   CA   sing N N 205 
GLU N   H    sing N N 206 
GLU N   H2   sing N N 207 
GLU CA  C    sing N N 208 
GLU CA  CB   sing N N 209 
GLU CA  HA   sing N N 210 
GLU C   O    doub N N 211 
GLU C   OXT  sing N N 212 
GLU CB  CG   sing N N 213 
GLU CB  HB2  sing N N 214 
GLU CB  HB3  sing N N 215 
GLU CG  CD   sing N N 216 
GLU CG  HG2  sing N N 217 
GLU CG  HG3  sing N N 218 
GLU CD  OE1  doub N N 219 
GLU CD  OE2  sing N N 220 
GLU OE2 HE2  sing N N 221 
GLU OXT HXT  sing N N 222 
GLY N   CA   sing N N 223 
GLY N   H    sing N N 224 
GLY N   H2   sing N N 225 
GLY CA  C    sing N N 226 
GLY CA  HA2  sing N N 227 
GLY CA  HA3  sing N N 228 
GLY C   O    doub N N 229 
GLY C   OXT  sing N N 230 
GLY OXT HXT  sing N N 231 
HIS N   CA   sing N N 232 
HIS N   H    sing N N 233 
HIS N   H2   sing N N 234 
HIS CA  C    sing N N 235 
HIS CA  CB   sing N N 236 
HIS CA  HA   sing N N 237 
HIS C   O    doub N N 238 
HIS C   OXT  sing N N 239 
HIS CB  CG   sing N N 240 
HIS CB  HB2  sing N N 241 
HIS CB  HB3  sing N N 242 
HIS CG  ND1  sing Y N 243 
HIS CG  CD2  doub Y N 244 
HIS ND1 CE1  doub Y N 245 
HIS ND1 HD1  sing N N 246 
HIS CD2 NE2  sing Y N 247 
HIS CD2 HD2  sing N N 248 
HIS CE1 NE2  sing Y N 249 
HIS CE1 HE1  sing N N 250 
HIS NE2 HE2  sing N N 251 
HIS OXT HXT  sing N N 252 
HOH O   H1   sing N N 253 
HOH O   H2   sing N N 254 
ILE N   CA   sing N N 255 
ILE N   H    sing N N 256 
ILE N   H2   sing N N 257 
ILE CA  C    sing N N 258 
ILE CA  CB   sing N N 259 
ILE CA  HA   sing N N 260 
ILE C   O    doub N N 261 
ILE C   OXT  sing N N 262 
ILE CB  CG1  sing N N 263 
ILE CB  CG2  sing N N 264 
ILE CB  HB   sing N N 265 
ILE CG1 CD1  sing N N 266 
ILE CG1 HG12 sing N N 267 
ILE CG1 HG13 sing N N 268 
ILE CG2 HG21 sing N N 269 
ILE CG2 HG22 sing N N 270 
ILE CG2 HG23 sing N N 271 
ILE CD1 HD11 sing N N 272 
ILE CD1 HD12 sing N N 273 
ILE CD1 HD13 sing N N 274 
ILE OXT HXT  sing N N 275 
LEU N   CA   sing N N 276 
LEU N   H    sing N N 277 
LEU N   H2   sing N N 278 
LEU CA  C    sing N N 279 
LEU CA  CB   sing N N 280 
LEU CA  HA   sing N N 281 
LEU C   O    doub N N 282 
LEU C   OXT  sing N N 283 
LEU CB  CG   sing N N 284 
LEU CB  HB2  sing N N 285 
LEU CB  HB3  sing N N 286 
LEU CG  CD1  sing N N 287 
LEU CG  CD2  sing N N 288 
LEU CG  HG   sing N N 289 
LEU CD1 HD11 sing N N 290 
LEU CD1 HD12 sing N N 291 
LEU CD1 HD13 sing N N 292 
LEU CD2 HD21 sing N N 293 
LEU CD2 HD22 sing N N 294 
LEU CD2 HD23 sing N N 295 
LEU OXT HXT  sing N N 296 
LYS N   CA   sing N N 297 
LYS N   H    sing N N 298 
LYS N   H2   sing N N 299 
LYS CA  C    sing N N 300 
LYS CA  CB   sing N N 301 
LYS CA  HA   sing N N 302 
LYS C   O    doub N N 303 
LYS C   OXT  sing N N 304 
LYS CB  CG   sing N N 305 
LYS CB  HB2  sing N N 306 
LYS CB  HB3  sing N N 307 
LYS CG  CD   sing N N 308 
LYS CG  HG2  sing N N 309 
LYS CG  HG3  sing N N 310 
LYS CD  CE   sing N N 311 
LYS CD  HD2  sing N N 312 
LYS CD  HD3  sing N N 313 
LYS CE  NZ   sing N N 314 
LYS CE  HE2  sing N N 315 
LYS CE  HE3  sing N N 316 
LYS NZ  HZ1  sing N N 317 
LYS NZ  HZ2  sing N N 318 
LYS NZ  HZ3  sing N N 319 
LYS OXT HXT  sing N N 320 
MET N   CA   sing N N 321 
MET N   H    sing N N 322 
MET N   H2   sing N N 323 
MET CA  C    sing N N 324 
MET CA  CB   sing N N 325 
MET CA  HA   sing N N 326 
MET C   O    doub N N 327 
MET C   OXT  sing N N 328 
MET CB  CG   sing N N 329 
MET CB  HB2  sing N N 330 
MET CB  HB3  sing N N 331 
MET CG  SD   sing N N 332 
MET CG  HG2  sing N N 333 
MET CG  HG3  sing N N 334 
MET SD  CE   sing N N 335 
MET CE  HE1  sing N N 336 
MET CE  HE2  sing N N 337 
MET CE  HE3  sing N N 338 
MET OXT HXT  sing N N 339 
PHE N   CA   sing N N 340 
PHE N   H    sing N N 341 
PHE N   H2   sing N N 342 
PHE CA  C    sing N N 343 
PHE CA  CB   sing N N 344 
PHE CA  HA   sing N N 345 
PHE C   O    doub N N 346 
PHE C   OXT  sing N N 347 
PHE CB  CG   sing N N 348 
PHE CB  HB2  sing N N 349 
PHE CB  HB3  sing N N 350 
PHE CG  CD1  doub Y N 351 
PHE CG  CD2  sing Y N 352 
PHE CD1 CE1  sing Y N 353 
PHE CD1 HD1  sing N N 354 
PHE CD2 CE2  doub Y N 355 
PHE CD2 HD2  sing N N 356 
PHE CE1 CZ   doub Y N 357 
PHE CE1 HE1  sing N N 358 
PHE CE2 CZ   sing Y N 359 
PHE CE2 HE2  sing N N 360 
PHE CZ  HZ   sing N N 361 
PHE OXT HXT  sing N N 362 
PRO N   CA   sing N N 363 
PRO N   CD   sing N N 364 
PRO N   H    sing N N 365 
PRO CA  C    sing N N 366 
PRO CA  CB   sing N N 367 
PRO CA  HA   sing N N 368 
PRO C   O    doub N N 369 
PRO C   OXT  sing N N 370 
PRO CB  CG   sing N N 371 
PRO CB  HB2  sing N N 372 
PRO CB  HB3  sing N N 373 
PRO CG  CD   sing N N 374 
PRO CG  HG2  sing N N 375 
PRO CG  HG3  sing N N 376 
PRO CD  HD2  sing N N 377 
PRO CD  HD3  sing N N 378 
PRO OXT HXT  sing N N 379 
SER N   CA   sing N N 380 
SER N   H    sing N N 381 
SER N   H2   sing N N 382 
SER CA  C    sing N N 383 
SER CA  CB   sing N N 384 
SER CA  HA   sing N N 385 
SER C   O    doub N N 386 
SER C   OXT  sing N N 387 
SER CB  OG   sing N N 388 
SER CB  HB2  sing N N 389 
SER CB  HB3  sing N N 390 
SER OG  HG   sing N N 391 
SER OXT HXT  sing N N 392 
THR N   CA   sing N N 393 
THR N   H    sing N N 394 
THR N   H2   sing N N 395 
THR CA  C    sing N N 396 
THR CA  CB   sing N N 397 
THR CA  HA   sing N N 398 
THR C   O    doub N N 399 
THR C   OXT  sing N N 400 
THR CB  OG1  sing N N 401 
THR CB  CG2  sing N N 402 
THR CB  HB   sing N N 403 
THR OG1 HG1  sing N N 404 
THR CG2 HG21 sing N N 405 
THR CG2 HG22 sing N N 406 
THR CG2 HG23 sing N N 407 
THR OXT HXT  sing N N 408 
TRP N   CA   sing N N 409 
TRP N   H    sing N N 410 
TRP N   H2   sing N N 411 
TRP CA  C    sing N N 412 
TRP CA  CB   sing N N 413 
TRP CA  HA   sing N N 414 
TRP C   O    doub N N 415 
TRP C   OXT  sing N N 416 
TRP CB  CG   sing N N 417 
TRP CB  HB2  sing N N 418 
TRP CB  HB3  sing N N 419 
TRP CG  CD1  doub Y N 420 
TRP CG  CD2  sing Y N 421 
TRP CD1 NE1  sing Y N 422 
TRP CD1 HD1  sing N N 423 
TRP CD2 CE2  doub Y N 424 
TRP CD2 CE3  sing Y N 425 
TRP NE1 CE2  sing Y N 426 
TRP NE1 HE1  sing N N 427 
TRP CE2 CZ2  sing Y N 428 
TRP CE3 CZ3  doub Y N 429 
TRP CE3 HE3  sing N N 430 
TRP CZ2 CH2  doub Y N 431 
TRP CZ2 HZ2  sing N N 432 
TRP CZ3 CH2  sing Y N 433 
TRP CZ3 HZ3  sing N N 434 
TRP CH2 HH2  sing N N 435 
TRP OXT HXT  sing N N 436 
TYR N   CA   sing N N 437 
TYR N   H    sing N N 438 
TYR N   H2   sing N N 439 
TYR CA  C    sing N N 440 
TYR CA  CB   sing N N 441 
TYR CA  HA   sing N N 442 
TYR C   O    doub N N 443 
TYR C   OXT  sing N N 444 
TYR CB  CG   sing N N 445 
TYR CB  HB2  sing N N 446 
TYR CB  HB3  sing N N 447 
TYR CG  CD1  doub Y N 448 
TYR CG  CD2  sing Y N 449 
TYR CD1 CE1  sing Y N 450 
TYR CD1 HD1  sing N N 451 
TYR CD2 CE2  doub Y N 452 
TYR CD2 HD2  sing N N 453 
TYR CE1 CZ   doub Y N 454 
TYR CE1 HE1  sing N N 455 
TYR CE2 CZ   sing Y N 456 
TYR CE2 HE2  sing N N 457 
TYR CZ  OH   sing N N 458 
TYR OH  HH   sing N N 459 
TYR OXT HXT  sing N N 460 
VAL N   CA   sing N N 461 
VAL N   H    sing N N 462 
VAL N   H2   sing N N 463 
VAL CA  C    sing N N 464 
VAL CA  CB   sing N N 465 
VAL CA  HA   sing N N 466 
VAL C   O    doub N N 467 
VAL C   OXT  sing N N 468 
VAL CB  CG1  sing N N 469 
VAL CB  CG2  sing N N 470 
VAL CB  HB   sing N N 471 
VAL CG1 HG11 sing N N 472 
VAL CG1 HG12 sing N N 473 
VAL CG1 HG13 sing N N 474 
VAL CG2 HG21 sing N N 475 
VAL CG2 HG22 sing N N 476 
VAL CG2 HG23 sing N N 477 
VAL OXT HXT  sing N N 478 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Max Planck Society'  Germany          ?      1 
'European Commission' 'European Union' 862087 2 
# 
_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   8RIP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HNF 
_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]   0.012361 
_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]   0.007221 
_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]   0.007334 
_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  
P  
S  
ZN 
# 
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   . SER A 1 26  ? 5.057   -3.382  31.849  1.00 59.64  ? 2   SER A N   1 
ATOM   2    C  CA  . SER A 1 26  ? 4.857   -4.806  32.100  1.00 62.06  ? 2   SER A CA  1 
ATOM   3    C  C   . SER A 1 26  ? 3.979   -5.425  31.013  1.00 67.21  ? 2   SER A C   1 
ATOM   4    O  O   . SER A 1 26  ? 4.153   -6.588  30.651  1.00 67.83  ? 2   SER A O   1 
ATOM   5    C  CB  . SER A 1 26  ? 4.228   -5.027  33.474  1.00 61.26  ? 2   SER A CB  1 
ATOM   6    O  OG  . SER A 1 26  ? 2.872   -4.624  33.480  1.00 64.07  ? 2   SER A OG  1 
ATOM   7    N  N   . LEU A 1 27  ? 3.038   -4.637  30.488  1.00 59.35  ? 3   LEU A N   1 
ATOM   8    C  CA  . LEU A 1 27  ? 2.208   -5.082  29.374  1.00 56.57  ? 3   LEU A CA  1 
ATOM   9    C  C   . LEU A 1 27  ? 2.992   -5.230  28.076  1.00 56.28  ? 3   LEU A C   1 
ATOM   10   O  O   . LEU A 1 27  ? 2.397   -5.580  27.048  1.00 51.78  ? 3   LEU A O   1 
ATOM   11   C  CB  . LEU A 1 27  ? 1.050   -4.106  29.161  1.00 51.74  ? 3   LEU A CB  1 
ATOM   12   C  CG  . LEU A 1 27  ? 0.069   -3.943  30.323  1.00 56.88  ? 3   LEU A CG  1 
ATOM   13   C  CD1 . LEU A 1 27  ? -0.907  -2.814  30.034  1.00 53.83  ? 3   LEU A CD1 1 
ATOM   14   C  CD2 . LEU A 1 27  ? -0.682  -5.238  30.590  1.00 52.17  ? 3   LEU A CD2 1 
ATOM   15   N  N   . ASN A 1 28  ? 4.296   -4.969  28.093  1.00 56.05  ? 4   ASN A N   1 
ATOM   16   C  CA  . ASN A 1 28  ? 5.106   -5.099  26.891  1.00 56.79  ? 4   ASN A CA  1 
ATOM   17   C  C   . ASN A 1 28  ? 5.188   -6.556  26.456  1.00 50.46  ? 4   ASN A C   1 
ATOM   18   O  O   . ASN A 1 28  ? 5.347   -7.461  27.280  1.00 50.11  ? 4   ASN A O   1 
ATOM   19   C  CB  . ASN A 1 28  ? 6.507   -4.545  27.141  1.00 63.08  ? 4   ASN A CB  1 
ATOM   20   C  CG  . ASN A 1 28  ? 6.524   -3.033  27.238  1.00 67.98  ? 4   ASN A CG  1 
ATOM   21   O  OD1 . ASN A 1 28  ? 6.060   -2.337  26.333  1.00 71.92  ? 4   ASN A OD1 1 
ATOM   22   N  ND2 . ASN A 1 28  ? 7.049   -2.516  28.343  1.00 70.68  ? 4   ASN A ND2 1 
ATOM   23   N  N   . GLY A 1 29  ? 5.077   -6.775  25.149  1.00 44.16  ? 5   GLY A N   1 
ATOM   24   C  CA  . GLY A 1 29  ? 5.160   -8.117  24.611  1.00 46.08  ? 5   GLY A CA  1 
ATOM   25   C  C   . GLY A 1 29  ? 3.950   -8.982  24.873  1.00 39.86  ? 5   GLY A C   1 
ATOM   26   O  O   . GLY A 1 29  ? 4.045   -10.208 24.773  1.00 39.27  ? 5   GLY A O   1 
ATOM   27   N  N   . LYS A 1 30  ? 2.813   -8.383  25.213  1.00 40.64  ? 6   LYS A N   1 
ATOM   28   C  CA  . LYS A 1 30  ? 1.568   -9.114  25.411  1.00 37.98  ? 6   LYS A CA  1 
ATOM   29   C  C   . LYS A 1 30  ? 0.742   -9.047  24.133  1.00 37.97  ? 6   LYS A C   1 
ATOM   30   O  O   . LYS A 1 30  ? 0.514   -7.959  23.593  1.00 38.40  ? 6   LYS A O   1 
ATOM   31   C  CB  . LYS A 1 30  ? 0.776   -8.536  26.585  1.00 39.44  ? 6   LYS A CB  1 
ATOM   32   C  CG  . LYS A 1 30  ? 1.489   -8.628  27.929  1.00 43.76  ? 6   LYS A CG  1 
ATOM   33   C  CD  . LYS A 1 30  ? 1.679   -10.073 28.361  1.00 42.10  ? 6   LYS A CD  1 
ATOM   34   C  CE  . LYS A 1 30  ? 2.191   -10.175 29.793  1.00 46.23  ? 6   LYS A CE  1 
ATOM   35   N  NZ  . LYS A 1 30  ? 3.599   -9.716  29.931  1.00 54.71  ? 6   LYS A NZ  1 
ATOM   36   N  N   . VAL A 1 31  ? 0.301   -10.208 23.650  1.00 33.27  ? 7   VAL A N   1 
ATOM   37   C  CA  . VAL A 1 31  ? -0.504  -10.309 22.439  1.00 33.53  ? 7   VAL A CA  1 
ATOM   38   C  C   . VAL A 1 31  ? -1.914  -10.736 22.822  1.00 30.90  ? 7   VAL A C   1 
ATOM   39   O  O   . VAL A 1 31  ? -2.100  -11.748 23.508  1.00 31.60  ? 7   VAL A O   1 
ATOM   40   C  CB  . VAL A 1 31  ? 0.108   -11.294 21.428  1.00 32.89  ? 7   VAL A CB  1 
ATOM   41   C  CG1 . VAL A 1 31  ? -0.752  -11.355 20.170  1.00 28.39  ? 7   VAL A CG1 1 
ATOM   42   C  CG2 . VAL A 1 31  ? 1.530   -10.892 21.086  1.00 31.87  ? 7   VAL A CG2 1 
ATOM   43   N  N   . ILE A 1 32  ? -2.901  -9.969  22.367  1.00 31.70  ? 8   ILE A N   1 
ATOM   44   C  CA  . ILE A 1 32  ? -4.311  -10.275 22.584  1.00 29.98  ? 8   ILE A CA  1 
ATOM   45   C  C   . ILE A 1 32  ? -4.769  -11.218 21.481  1.00 27.90  ? 8   ILE A C   1 
ATOM   46   O  O   . ILE A 1 32  ? -4.648  -10.899 20.294  1.00 29.56  ? 8   ILE A O   1 
ATOM   47   C  CB  . ILE A 1 32  ? -5.162  -8.996  22.586  1.00 31.49  ? 8   ILE A CB  1 
ATOM   48   C  CG1 . ILE A 1 32  ? -4.715  -8.047  23.698  1.00 30.28  ? 8   ILE A CG1 1 
ATOM   49   C  CG2 . ILE A 1 32  ? -6.647  -9.340  22.730  1.00 31.42  ? 8   ILE A CG2 1 
ATOM   50   C  CD1 . ILE A 1 32  ? -5.292  -6.654  23.562  1.00 29.18  ? 8   ILE A CD1 1 
ATOM   51   N  N   . ILE A 1 33  ? -5.290  -12.378 21.867  1.00 28.22  ? 9   ILE A N   1 
ATOM   52   C  CA  . ILE A 1 33  ? -5.939  -13.295 20.938  1.00 27.76  ? 9   ILE A CA  1 
ATOM   53   C  C   . ILE A 1 33  ? -7.445  -13.146 21.102  1.00 30.12  ? 9   ILE A C   1 
ATOM   54   O  O   . ILE A 1 33  ? -7.989  -13.398 22.184  1.00 29.78  ? 9   ILE A O   1 
ATOM   55   C  CB  . ILE A 1 33  ? -5.510  -14.751 21.177  1.00 28.84  ? 9   ILE A CB  1 
ATOM   56   C  CG1 . ILE A 1 33  ? -4.005  -14.919 20.957  1.00 26.86  ? 9   ILE A CG1 1 
ATOM   57   C  CG2 . ILE A 1 33  ? -6.294  -15.689 20.250  1.00 25.94  ? 9   ILE A CG2 1 
ATOM   58   C  CD1 . ILE A 1 33  ? -3.494  -16.296 21.334  1.00 28.49  ? 9   ILE A CD1 1 
ATOM   59   N  N   . THR A 1 34  ? -8.114  -12.723 20.035  1.00 26.39  ? 10  THR A N   1 
ATOM   60   C  CA  . THR A 1 34  ? -9.565  -12.781 19.951  1.00 28.84  ? 10  THR A CA  1 
ATOM   61   C  C   . THR A 1 34  ? -9.966  -14.073 19.254  1.00 28.93  ? 10  THR A C   1 
ATOM   62   O  O   . THR A 1 34  ? -9.337  -14.480 18.274  1.00 27.15  ? 10  THR A O   1 
ATOM   63   C  CB  . THR A 1 34  ? -10.122 -11.583 19.179  1.00 29.61  ? 10  THR A CB  1 
ATOM   64   O  OG1 . THR A 1 34  ? -9.771  -10.364 19.849  1.00 30.33  ? 10  THR A OG1 1 
ATOM   65   C  CG2 . THR A 1 34  ? -11.642 -11.676 19.048  1.00 31.43  ? 10  THR A CG2 1 
ATOM   66   N  N   . CYS A 1 35  ? -11.005 -14.724 19.768  1.00 30.18  ? 11  CYS A N   1 
ATOM   67   C  CA  . CYS A 1 35  ? -11.562 -15.904 19.122  1.00 31.65  ? 11  CYS A CA  1 
ATOM   68   C  C   . CYS A 1 35  ? -13.008 -15.626 18.744  1.00 31.95  ? 11  CYS A C   1 
ATOM   69   O  O   . CYS A 1 35  ? -13.847 -15.384 19.619  1.00 33.27  ? 11  CYS A O   1 
ATOM   70   C  CB  . CYS A 1 35  ? -11.476 -17.136 20.016  1.00 32.64  ? 11  CYS A CB  1 
ATOM   71   S  SG  . CYS A 1 35  ? -11.838 -18.648 19.098  1.00 37.06  ? 11  CYS A SG  1 
ATOM   72   N  N   . ALA A 1 36  ? -13.286 -15.655 17.443  1.00 30.27  ? 12  ALA A N   1 
ATOM   73   C  CA  . ALA A 1 36  ? -14.629 -15.476 16.899  1.00 30.79  ? 12  ALA A CA  1 
ATOM   74   C  C   . ALA A 1 36  ? -15.215 -16.860 16.633  1.00 30.38  ? 12  ALA A C   1 
ATOM   75   O  O   . ALA A 1 36  ? -14.821 -17.532 15.676  1.00 30.63  ? 12  ALA A O   1 
ATOM   76   C  CB  . ALA A 1 36  ? -14.576 -14.632 15.627  1.00 28.49  ? 12  ALA A CB  1 
ATOM   77   N  N   . VAL A 1 37  ? -16.175 -17.275 17.465  1.00 29.52  ? 13  VAL A N   1 
ATOM   78   C  CA  . VAL A 1 37  ? -16.476 -18.701 17.568  1.00 30.09  ? 13  VAL A CA  1 
ATOM   79   C  C   . VAL A 1 37  ? -17.404 -19.211 16.461  1.00 33.15  ? 13  VAL A C   1 
ATOM   80   O  O   . VAL A 1 37  ? -17.369 -20.405 16.139  1.00 30.19  ? 13  VAL A O   1 
ATOM   81   C  CB  . VAL A 1 37  ? -17.057 -19.029 18.957  1.00 32.10  ? 13  VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 37  ? -15.992 -18.842 20.030  1.00 31.71  ? 13  VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 37  ? -18.294 -18.184 19.256  1.00 31.71  ? 13  VAL A CG2 1 
ATOM   84   N  N   . THR A 1 38  ? -18.254 -18.365 15.868  1.00 31.19  ? 14  THR A N   1 
ATOM   85   C  CA  . THR A 1 38  ? -19.181 -18.896 14.867  1.00 33.28  ? 14  THR A CA  1 
ATOM   86   C  C   . THR A 1 38  ? -19.534 -17.903 13.763  1.00 32.75  ? 14  THR A C   1 
ATOM   87   O  O   . THR A 1 38  ? -19.579 -18.278 12.587  1.00 33.82  ? 14  THR A O   1 
ATOM   88   C  CB  . THR A 1 38  ? -20.467 -19.398 15.545  1.00 35.28  ? 14  THR A CB  1 
ATOM   89   O  OG1 . THR A 1 38  ? -21.164 -20.282 14.655  1.00 34.97  ? 14  THR A OG1 1 
ATOM   90   C  CG2 . THR A 1 38  ? -21.395 -18.245 15.922  1.00 35.75  ? 14  THR A CG2 1 
ATOM   91   N  N   . GLY A 1 39  ? -19.798 -16.650 14.114  1.00 30.72  ? 15  GLY A N   1 
ATOM   92   C  CA  . GLY A 1 39  ? -20.075 -15.675 13.079  1.00 29.04  ? 15  GLY A CA  1 
ATOM   93   C  C   . GLY A 1 39  ? -21.418 -15.871 12.385  1.00 33.41  ? 15  GLY A C   1 
ATOM   94   O  O   . GLY A 1 39  ? -22.338 -16.526 12.886  1.00 31.75  ? 15  GLY A O   1 
ATOM   95   N  N   . ALA A 1 40  ? -21.510 -15.275 11.194  1.00 32.06  ? 16  ALA A N   1 
ATOM   96   C  CA  . ALA A 1 40  ? -22.722 -15.304 10.393  1.00 34.71  ? 16  ALA A CA  1 
ATOM   97   C  C   . ALA A 1 40  ? -22.472 -15.665 8.935   1.00 35.91  ? 16  ALA A C   1 
ATOM   98   O  O   . ALA A 1 40  ? -23.431 -15.721 8.158   1.00 33.93  ? 16  ALA A O   1 
ATOM   99   C  CB  . ALA A 1 40  ? -23.431 -13.942 10.454  1.00 33.14  ? 16  ALA A CB  1 
ATOM   100  N  N   . ILE A 1 41  ? -21.224 -15.917 8.543   1.00 33.18  ? 17  ILE A N   1 
ATOM   101  C  CA  . ILE A 1 41  ? -20.884 -16.110 7.137   1.00 34.76  ? 17  ILE A CA  1 
ATOM   102  C  C   . ILE A 1 41  ? -20.889 -17.593 6.794   1.00 36.32  ? 17  ILE A C   1 
ATOM   103  O  O   . ILE A 1 41  ? -21.621 -18.026 5.897   1.00 34.30  ? 17  ILE A O   1 
ATOM   104  C  CB  . ILE A 1 41  ? -19.523 -15.468 6.810   1.00 34.98  ? 17  ILE A CB  1 
ATOM   105  C  CG1 . ILE A 1 41  ? -19.569 -13.960 7.082   1.00 36.02  ? 17  ILE A CG1 1 
ATOM   106  C  CG2 . ILE A 1 41  ? -19.136 -15.748 5.367   1.00 34.01  ? 17  ILE A CG2 1 
ATOM   107  C  CD1 . ILE A 1 41  ? -20.713 -13.234 6.390   1.00 39.05  ? 17  ILE A CD1 1 
ATOM   108  N  N   . HIS A 1 42  ? -20.067 -18.380 7.485   1.00 34.16  ? 18  HIS A N   1 
ATOM   109  C  CA  . HIS A 1 42  ? -20.120 -19.824 7.306   1.00 33.85  ? 18  HIS A CA  1 
ATOM   110  C  C   . HIS A 1 42  ? -21.502 -20.340 7.695   1.00 35.54  ? 18  HIS A C   1 
ATOM   111  O  O   . HIS A 1 42  ? -22.217 -19.728 8.493   1.00 34.09  ? 18  HIS A O   1 
ATOM   112  C  CB  . HIS A 1 42  ? -19.043 -20.512 8.149   1.00 31.45  ? 18  HIS A CB  1 
ATOM   113  C  CG  . HIS A 1 42  ? -17.643 -20.200 7.717   1.00 33.97  ? 18  HIS A CG  1 
ATOM   114  N  ND1 . HIS A 1 42  ? -16.617 -19.989 8.614   1.00 32.41  ? 18  HIS A ND1 1 
ATOM   115  C  CD2 . HIS A 1 42  ? -17.095 -20.078 6.485   1.00 31.19  ? 18  HIS A CD2 1 
ATOM   116  C  CE1 . HIS A 1 42  ? -15.501 -19.739 7.953   1.00 32.52  ? 18  HIS A CE1 1 
ATOM   117  N  NE2 . HIS A 1 42  ? -15.763 -19.789 6.659   1.00 34.81  ? 18  HIS A NE2 1 
ATOM   118  N  N   . THR A 1 43  ? -21.876 -21.476 7.124   1.00 32.70  ? 19  THR A N   1 
ATOM   119  C  CA  . THR A 1 43  ? -23.168 -22.093 7.369   1.00 36.38  ? 19  THR A CA  1 
ATOM   120  C  C   . THR A 1 43  ? -22.967 -23.533 7.814   1.00 36.92  ? 19  THR A C   1 
ATOM   121  O  O   . THR A 1 43  ? -21.914 -24.130 7.562   1.00 38.00  ? 19  THR A O   1 
ATOM   122  C  CB  . THR A 1 43  ? -24.056 -22.047 6.115   1.00 37.43  ? 19  THR A CB  1 
ATOM   123  O  OG1 . THR A 1 43  ? -23.528 -22.922 5.113   1.00 37.28  ? 19  THR A OG1 1 
ATOM   124  C  CG2 . THR A 1 43  ? -24.124 -20.626 5.556   1.00 35.20  ? 19  THR A CG2 1 
ATOM   125  N  N   . PRO A 1 44  ? -23.965 -24.121 8.480   1.00 35.02  ? 20  PRO A N   1 
ATOM   126  C  CA  . PRO A 1 44  ? -23.766 -25.454 9.077   1.00 37.31  ? 20  PRO A CA  1 
ATOM   127  C  C   . PRO A 1 44  ? -23.355 -26.533 8.089   1.00 38.13  ? 20  PRO A C   1 
ATOM   128  O  O   . PRO A 1 44  ? -22.593 -27.434 8.464   1.00 39.77  ? 20  PRO A O   1 
ATOM   129  C  CB  . PRO A 1 44  ? -25.137 -25.764 9.699   1.00 40.67  ? 20  PRO A CB  1 
ATOM   130  C  CG  . PRO A 1 44  ? -25.756 -24.437 9.940   1.00 40.18  ? 20  PRO A CG  1 
ATOM   131  C  CD  . PRO A 1 44  ? -25.271 -23.542 8.840   1.00 39.66  ? 20  PRO A CD  1 
ATOM   132  N  N   . SER A 1 45  ? -23.843 -26.490 6.847   1.00 37.07  ? 21  SER A N   1 
ATOM   133  C  CA  . SER A 1 45  ? -23.506 -27.539 5.890   1.00 38.41  ? 21  SER A CA  1 
ATOM   134  C  C   . SER A 1 45  ? -22.021 -27.561 5.554   1.00 35.81  ? 21  SER A C   1 
ATOM   135  O  O   . SER A 1 45  ? -21.532 -28.565 5.026   1.00 41.42  ? 21  SER A O   1 
ATOM   136  C  CB  . SER A 1 45  ? -24.313 -27.363 4.604   1.00 37.33  ? 21  SER A CB  1 
ATOM   137  O  OG  . SER A 1 45  ? -25.703 -27.463 4.851   1.00 42.14  ? 21  SER A OG  1 
ATOM   138  N  N   . MET A 1 46  ? -21.294 -26.483 5.843   1.00 32.30  ? 22  MET A N   1 
ATOM   139  C  CA  . MET A 1 46  ? -19.881 -26.421 5.485   1.00 36.24  ? 22  MET A CA  1 
ATOM   140  C  C   . MET A 1 46  ? -19.010 -27.240 6.427   1.00 35.76  ? 22  MET A C   1 
ATOM   141  O  O   . MET A 1 46  ? -17.949 -27.726 6.018   1.00 34.70  ? 22  MET A O   1 
ATOM   142  C  CB  . MET A 1 46  ? -19.406 -24.969 5.485   1.00 34.99  ? 22  MET A CB  1 
ATOM   143  C  CG  . MET A 1 46  ? -20.128 -24.084 4.493   1.00 36.02  ? 22  MET A CG  1 
ATOM   144  S  SD  . MET A 1 46  ? -19.639 -22.361 4.647   1.00 38.78  ? 22  MET A SD  1 
ATOM   145  C  CE  . MET A 1 46  ? -20.655 -21.610 3.377   1.00 38.96  ? 22  MET A CE  1 
ATOM   146  N  N   . SER A 1 47  ? -19.426 -27.396 7.679   1.00 34.12  ? 23  SER A N   1 
ATOM   147  C  CA  . SER A 1 47  ? -18.632 -28.124 8.659   1.00 36.80  ? 23  SER A CA  1 
ATOM   148  C  C   . SER A 1 47  ? -19.499 -28.532 9.841   1.00 37.85  ? 23  SER A C   1 
ATOM   149  O  O   . SER A 1 47  ? -20.231 -27.696 10.387  1.00 36.54  ? 23  SER A O   1 
ATOM   150  C  CB  . SER A 1 47  ? -17.461 -27.271 9.148   1.00 32.70  ? 23  SER A CB  1 
ATOM   151  O  OG  . SER A 1 47  ? -16.861 -27.858 10.291  1.00 37.79  ? 23  SER A OG  1 
ATOM   152  N  N   . PRO A 1 48  ? -19.436 -29.793 10.283  1.00 38.26  ? 24  PRO A N   1 
ATOM   153  C  CA  . PRO A 1 48  ? -20.206 -30.193 11.468  1.00 38.68  ? 24  PRO A CA  1 
ATOM   154  C  C   . PRO A 1 48  ? -19.668 -29.614 12.764  1.00 38.69  ? 24  PRO A C   1 
ATOM   155  O  O   . PRO A 1 48  ? -20.289 -29.807 13.815  1.00 40.25  ? 24  PRO A O   1 
ATOM   156  C  CB  . PRO A 1 48  ? -20.084 -31.721 11.456  1.00 36.15  ? 24  PRO A CB  1 
ATOM   157  C  CG  . PRO A 1 48  ? -18.746 -31.964 10.838  1.00 37.40  ? 24  PRO A CG  1 
ATOM   158  C  CD  . PRO A 1 48  ? -18.581 -30.890 9.790   1.00 35.55  ? 24  PRO A CD  1 
ATOM   159  N  N   . TYR A 1 49  ? -18.537 -28.913 12.723  1.00 38.52  ? 25  TYR A N   1 
ATOM   160  C  CA  . TYR A 1 49  ? -17.922 -28.344 13.911  1.00 38.88  ? 25  TYR A CA  1 
ATOM   161  C  C   . TYR A 1 49  ? -18.273 -26.876 14.111  1.00 36.99  ? 25  TYR A C   1 
ATOM   162  O  O   . TYR A 1 49  ? -17.871 -26.290 15.122  1.00 36.52  ? 25  TYR A O   1 
ATOM   163  C  CB  . TYR A 1 49  ? -16.404 -28.519 13.837  1.00 35.87  ? 25  TYR A CB  1 
ATOM   164  C  CG  . TYR A 1 49  ? -16.005 -29.935 13.502  1.00 39.04  ? 25  TYR A CG  1 
ATOM   165  C  CD1 . TYR A 1 49  ? -16.237 -30.969 14.399  1.00 41.24  ? 25  TYR A CD1 1 
ATOM   166  C  CD2 . TYR A 1 49  ? -15.410 -30.243 12.286  1.00 38.97  ? 25  TYR A CD2 1 
ATOM   167  C  CE1 . TYR A 1 49  ? -15.884 -32.268 14.097  1.00 43.10  ? 25  TYR A CE1 1 
ATOM   168  C  CE2 . TYR A 1 49  ? -15.052 -31.540 11.976  1.00 40.63  ? 25  TYR A CE2 1 
ATOM   169  C  CZ  . TYR A 1 49  ? -15.291 -32.549 12.884  1.00 44.04  ? 25  TYR A CZ  1 
ATOM   170  O  OH  . TYR A 1 49  ? -14.937 -33.843 12.581  1.00 49.18  ? 25  TYR A OH  1 
ATOM   171  N  N   . LEU A 1 50  ? -19.011 -26.275 13.189  1.00 39.31  ? 26  LEU A N   1 
ATOM   172  C  CA  . LEU A 1 50  ? -19.456 -24.896 13.362  1.00 38.15  ? 26  LEU A CA  1 
ATOM   173  C  C   . LEU A 1 50  ? -20.445 -24.831 14.519  1.00 36.33  ? 26  LEU A C   1 
ATOM   174  O  O   . LEU A 1 50  ? -21.471 -25.522 14.478  1.00 37.27  ? 26  LEU A O   1 
ATOM   175  C  CB  . LEU A 1 50  ? -20.101 -24.381 12.079  1.00 37.88  ? 26  LEU A CB  1 
ATOM   176  C  CG  . LEU A 1 50  ? -20.489 -22.901 12.079  1.00 38.38  ? 26  LEU A CG  1 
ATOM   177  C  CD1 . LEU A 1 50  ? -19.248 -22.013 12.048  1.00 35.04  ? 26  LEU A CD1 1 
ATOM   178  C  CD2 . LEU A 1 50  ? -21.407 -22.597 10.908  1.00 36.89  ? 26  LEU A CD2 1 
ATOM   179  N  N   . PRO A 1 51  ? -20.186 -24.046 15.567  1.00 37.84  ? 27  PRO A N   1 
ATOM   180  C  CA  . PRO A 1 51  ? -21.133 -23.991 16.692  1.00 38.03  ? 27  PRO A CA  1 
ATOM   181  C  C   . PRO A 1 51  ? -22.448 -23.344 16.275  1.00 40.00  ? 27  PRO A C   1 
ATOM   182  O  O   . PRO A 1 51  ? -22.462 -22.294 15.627  1.00 38.64  ? 27  PRO A O   1 
ATOM   183  C  CB  . PRO A 1 51  ? -20.395 -23.149 17.741  1.00 36.71  ? 27  PRO A CB  1 
ATOM   184  C  CG  . PRO A 1 51  ? -18.949 -23.213 17.344  1.00 36.23  ? 27  PRO A CG  1 
ATOM   185  C  CD  . PRO A 1 51  ? -18.951 -23.296 15.855  1.00 34.94  ? 27  PRO A CD  1 
ATOM   186  N  N   . VAL A 1 52  ? -23.557 -23.975 16.659  1.00 38.07  ? 28  VAL A N   1 
ATOM   187  C  CA  . VAL A 1 52  ? -24.884 -23.495 16.285  1.00 41.48  ? 28  VAL A CA  1 
ATOM   188  C  C   . VAL A 1 52  ? -25.719 -23.221 17.529  1.00 41.07  ? 28  VAL A C   1 
ATOM   189  O  O   . VAL A 1 52  ? -26.206 -22.102 17.727  1.00 40.44  ? 28  VAL A O   1 
ATOM   190  C  CB  . VAL A 1 52  ? -25.598 -24.501 15.364  1.00 40.70  ? 28  VAL A CB  1 
ATOM   191  C  CG1 . VAL A 1 52  ? -27.042 -24.074 15.139  1.00 41.51  ? 28  VAL A CG1 1 
ATOM   192  C  CG2 . VAL A 1 52  ? -24.859 -24.620 14.044  1.00 34.86  ? 28  VAL A CG2 1 
ATOM   193  N  N   . SER A 1 53  ? -25.905 -24.239 18.364  1.00 40.94  ? 29  SER A N   1 
ATOM   194  C  CA  . SER A 1 53  ? -26.739 -24.083 19.546  1.00 44.38  ? 29  SER A CA  1 
ATOM   195  C  C   . SER A 1 53  ? -26.064 -23.169 20.565  1.00 43.90  ? 29  SER A C   1 
ATOM   196  O  O   . SER A 1 53  ? -24.851 -22.942 20.533  1.00 42.22  ? 29  SER A O   1 
ATOM   197  C  CB  . SER A 1 53  ? -27.030 -25.442 20.185  1.00 43.45  ? 29  SER A CB  1 
ATOM   198  O  OG  . SER A 1 53  ? -25.880 -25.954 20.835  1.00 44.98  ? 29  SER A OG  1 
ATOM   199  N  N   . ALA A 1 54  ? -26.876 -22.640 21.482  1.00 43.08  ? 30  ALA A N   1 
ATOM   200  C  CA  . ALA A 1 54  ? -26.340 -21.786 22.536  1.00 43.07  ? 30  ALA A CA  1 
ATOM   201  C  C   . ALA A 1 54  ? -25.294 -22.523 23.362  1.00 43.85  ? 30  ALA A C   1 
ATOM   202  O  O   . ALA A 1 54  ? -24.274 -21.941 23.748  1.00 40.81  ? 30  ALA A O   1 
ATOM   203  C  CB  . ALA A 1 54  ? -27.473 -21.283 23.430  1.00 42.28  ? 30  ALA A CB  1 
ATOM   204  N  N   . SER A 1 55  ? -25.524 -23.809 23.639  1.00 42.58  ? 31  SER A N   1 
ATOM   205  C  CA  . SER A 1 55  ? -24.559 -24.570 24.425  1.00 44.83  ? 31  SER A CA  1 
ATOM   206  C  C   . SER A 1 55  ? -23.300 -24.877 23.624  1.00 42.37  ? 31  SER A C   1 
ATOM   207  O  O   . SER A 1 55  ? -22.202 -24.913 24.191  1.00 41.98  ? 31  SER A O   1 
ATOM   208  C  CB  . SER A 1 55  ? -25.199 -25.861 24.938  1.00 47.62  ? 31  SER A CB  1 
ATOM   209  O  OG  . SER A 1 55  ? -25.713 -26.640 23.872  1.00 52.20  ? 31  SER A OG  1 
ATOM   210  N  N   . GLU A 1 56  ? -23.431 -25.105 22.315  1.00 42.22  ? 32  GLU A N   1 
ATOM   211  C  CA  . GLU A 1 56  ? -22.245 -25.255 21.479  1.00 42.02  ? 32  GLU A CA  1 
ATOM   212  C  C   . GLU A 1 56  ? -21.436 -23.965 21.449  1.00 39.60  ? 32  GLU A C   1 
ATOM   213  O  O   . GLU A 1 56  ? -20.200 -23.996 21.471  1.00 38.24  ? 32  GLU A O   1 
ATOM   214  C  CB  . GLU A 1 56  ? -22.641 -25.661 20.060  1.00 42.09  ? 32  GLU A CB  1 
ATOM   215  C  CG  . GLU A 1 56  ? -23.123 -27.096 19.934  1.00 46.22  ? 32  GLU A CG  1 
ATOM   216  C  CD  . GLU A 1 56  ? -23.713 -27.399 18.568  1.00 47.41  ? 32  GLU A CD  1 
ATOM   217  O  OE1 . GLU A 1 56  ? -24.004 -26.443 17.815  1.00 44.16  ? 32  GLU A OE1 1 
ATOM   218  O  OE2 . GLU A 1 56  ? -23.885 -28.595 18.249  1.00 50.26  ? 32  GLU A OE2 1 
ATOM   219  N  N   . ILE A 1 57  ? -22.119 -22.821 21.403  1.00 37.22  ? 33  ILE A N   1 
ATOM   220  C  CA  . ILE A 1 57  ? -21.418 -21.545 21.328  1.00 41.13  ? 33  ILE A CA  1 
ATOM   221  C  C   . ILE A 1 57  ? -20.729 -21.231 22.650  1.00 39.47  ? 33  ILE A C   1 
ATOM   222  O  O   . ILE A 1 57  ? -19.603 -20.721 22.668  1.00 38.30  ? 33  ILE A O   1 
ATOM   223  C  CB  . ILE A 1 57  ? -22.395 -20.430 20.909  1.00 38.24  ? 33  ILE A CB  1 
ATOM   224  C  CG1 . ILE A 1 57  ? -22.801 -20.620 19.443  1.00 37.15  ? 33  ILE A CG1 1 
ATOM   225  C  CG2 . ILE A 1 57  ? -21.767 -19.060 21.130  1.00 33.94  ? 33  ILE A CG2 1 
ATOM   226  C  CD1 . ILE A 1 57  ? -23.923 -19.706 18.982  1.00 38.21  ? 33  ILE A CD1 1 
ATOM   227  N  N   . THR A 1 58  ? -21.382 -21.530 23.778  1.00 39.45  ? 34  THR A N   1 
ATOM   228  C  CA  . THR A 1 58  ? -20.756 -21.252 25.068  1.00 40.10  ? 34  THR A CA  1 
ATOM   229  C  C   . THR A 1 58  ? -19.593 -22.204 25.330  1.00 38.74  ? 34  THR A C   1 
ATOM   230  O  O   . THR A 1 58  ? -18.556 -21.789 25.860  1.00 39.75  ? 34  THR A O   1 
ATOM   231  C  CB  . THR A 1 58  ? -21.782 -21.335 26.202  1.00 40.45  ? 34  THR A CB  1 
ATOM   232  O  OG1 . THR A 1 58  ? -22.302 -22.666 26.300  1.00 41.55  ? 34  THR A OG1 1 
ATOM   233  C  CG2 . THR A 1 58  ? -22.923 -20.352 25.973  1.00 37.58  ? 34  THR A CG2 1 
ATOM   234  N  N   . ASP A 1 59  ? -19.742 -23.481 24.967  1.00 39.87  ? 35  ASP A N   1 
ATOM   235  C  CA  . ASP A 1 59  ? -18.631 -24.418 25.118  1.00 40.23  ? 35  ASP A CA  1 
ATOM   236  C  C   . ASP A 1 59  ? -17.447 -24.005 24.254  1.00 38.57  ? 35  ASP A C   1 
ATOM   237  O  O   . ASP A 1 59  ? -16.293 -24.075 24.692  1.00 37.75  ? 35  ASP A O   1 
ATOM   238  C  CB  . ASP A 1 59  ? -19.073 -25.836 24.757  1.00 43.18  ? 35  ASP A CB  1 
ATOM   239  C  CG  . ASP A 1 59  ? -20.009 -26.440 25.787  1.00 51.33  ? 35  ASP A CG  1 
ATOM   240  O  OD1 . ASP A 1 59  ? -20.026 -25.954 26.939  1.00 52.77  ? 35  ASP A OD1 1 
ATOM   241  O  OD2 . ASP A 1 59  ? -20.721 -27.409 25.445  1.00 50.73  ? 35  ASP A OD2 1 
ATOM   242  N  N   . ALA A 1 60  ? -17.713 -23.582 23.017  1.00 38.85  ? 36  ALA A N   1 
ATOM   243  C  CA  . ALA A 1 60  ? -16.635 -23.114 22.153  1.00 38.69  ? 36  ALA A CA  1 
ATOM   244  C  C   . ALA A 1 60  ? -15.949 -21.893 22.747  1.00 36.62  ? 36  ALA A C   1 
ATOM   245  O  O   . ALA A 1 60  ? -14.719 -21.771 22.691  1.00 32.13  ? 36  ALA A O   1 
ATOM   246  C  CB  . ALA A 1 60  ? -17.181 -22.795 20.761  1.00 33.13  ? 36  ALA A CB  1 
ATOM   247  N  N   . ALA A 1 61  ? -16.730 -20.976 23.322  1.00 35.00  ? 37  ALA A N   1 
ATOM   248  C  CA  . ALA A 1 61  ? -16.156 -19.761 23.889  1.00 36.89  ? 37  ALA A CA  1 
ATOM   249  C  C   . ALA A 1 61  ? -15.303 -20.077 25.112  1.00 36.67  ? 37  ALA A C   1 
ATOM   250  O  O   . ALA A 1 61  ? -14.171 -19.595 25.237  1.00 35.00  ? 37  ALA A O   1 
ATOM   251  C  CB  . ALA A 1 61  ? -17.271 -18.779 24.248  1.00 34.18  ? 37  ALA A CB  1 
ATOM   252  N  N   . ILE A 1 62  ? -15.833 -20.895 26.023  1.00 35.64  ? 38  ILE A N   1 
ATOM   253  C  CA  . ILE A 1 62  ? -15.109 -21.219 27.247  1.00 37.42  ? 38  ILE A CA  1 
ATOM   254  C  C   . ILE A 1 62  ? -13.848 -22.015 26.933  1.00 38.84  ? 38  ILE A C   1 
ATOM   255  O  O   . ILE A 1 62  ? -12.792 -21.794 27.538  1.00 36.88  ? 38  ILE A O   1 
ATOM   256  C  CB  . ILE A 1 62  ? -16.040 -21.971 28.217  1.00 37.77  ? 38  ILE A CB  1 
ATOM   257  C  CG1 . ILE A 1 62  ? -17.105 -21.014 28.757  1.00 38.37  ? 38  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A 1 62  ? -15.249 -22.590 29.358  1.00 38.14  ? 38  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A 1 62  ? -18.339 -21.706 29.308  1.00 39.24  ? 38  ILE A CD1 1 
ATOM   260  N  N   . GLY A 1 63  ? -13.932 -22.951 25.986  1.00 36.56  ? 39  GLY A N   1 
ATOM   261  C  CA  . GLY A 1 63  ? -12.748 -23.703 25.607  1.00 35.26  ? 39  GLY A CA  1 
ATOM   262  C  C   . GLY A 1 63  ? -11.676 -22.824 24.990  1.00 37.14  ? 39  GLY A C   1 
ATOM   263  O  O   . GLY A 1 63  ? -10.482 -23.025 25.226  1.00 33.60  ? 39  GLY A O   1 
ATOM   264  N  N   . ALA A 1 64  ? -12.090 -21.833 24.196  1.00 34.09  ? 40  ALA A N   1 
ATOM   265  C  CA  . ALA A 1 64  ? -11.128 -20.932 23.571  1.00 35.60  ? 40  ALA A CA  1 
ATOM   266  C  C   . ALA A 1 64  ? -10.487 -20.006 24.598  1.00 35.32  ? 40  ALA A C   1 
ATOM   267  O  O   . ALA A 1 64  ? -9.297  -19.685 24.496  1.00 33.42  ? 40  ALA A O   1 
ATOM   268  C  CB  . ALA A 1 64  ? -11.810 -20.117 22.472  1.00 32.63  ? 40  ALA A CB  1 
ATOM   269  N  N   . ALA A 1 65  ? -11.262 -19.555 25.588  1.00 33.70  ? 41  ALA A N   1 
ATOM   270  C  CA  . ALA A 1 65  ? -10.699 -18.699 26.625  1.00 34.67  ? 41  ALA A CA  1 
ATOM   271  C  C   . ALA A 1 65  ? -9.685  -19.458 27.467  1.00 36.29  ? 41  ALA A C   1 
ATOM   272  O  O   . ALA A 1 65  ? -8.619  -18.925 27.796  1.00 36.29  ? 41  ALA A O   1 
ATOM   273  C  CB  . ALA A 1 65  ? -11.811 -18.138 27.508  1.00 35.72  ? 41  ALA A CB  1 
ATOM   274  N  N   . GLU A 1 66  ? -9.998  -20.707 27.821  1.00 35.84  ? 42  GLU A N   1 
ATOM   275  C  CA  . GLU A 1 66  ? -9.073  -21.520 28.600  1.00 36.69  ? 42  GLU A CA  1 
ATOM   276  C  C   . GLU A 1 66  ? -7.824  -21.885 27.807  1.00 38.71  ? 42  GLU A C   1 
ATOM   277  O  O   . GLU A 1 66  ? -6.785  -22.178 28.409  1.00 40.01  ? 42  GLU A O   1 
ATOM   278  C  CB  . GLU A 1 66  ? -9.797  -22.773 29.099  1.00 40.49  ? 42  GLU A CB  1 
ATOM   279  C  CG  . GLU A 1 66  ? -10.879 -22.454 30.132  1.00 44.58  ? 42  GLU A CG  1 
ATOM   280  C  CD  . GLU A 1 66  ? -11.758 -23.640 30.476  1.00 59.16  ? 42  GLU A CD  1 
ATOM   281  O  OE1 . GLU A 1 66  ? -11.721 -24.652 29.742  1.00 63.53  ? 42  GLU A OE1 1 
ATOM   282  O  OE2 . GLU A 1 66  ? -12.491 -23.555 31.486  1.00 53.48  ? 42  GLU A OE2 1 
ATOM   283  N  N   . ALA A 1 67  ? -7.892  -21.856 26.474  1.00 38.87  ? 43  ALA A N   1 
ATOM   284  C  CA  . ALA A 1 67  ? -6.697  -22.026 25.659  1.00 37.60  ? 43  ALA A CA  1 
ATOM   285  C  C   . ALA A 1 67  ? -5.895  -20.738 25.526  1.00 34.48  ? 43  ALA A C   1 
ATOM   286  O  O   . ALA A 1 67  ? -4.734  -20.791 25.112  1.00 32.23  ? 43  ALA A O   1 
ATOM   287  C  CB  . ALA A 1 67  ? -7.071  -22.543 24.268  1.00 32.85  ? 43  ALA A CB  1 
ATOM   288  N  N   . GLY A 1 68  ? -6.484  -19.589 25.855  1.00 33.55  ? 44  GLY A N   1 
ATOM   289  C  CA  . GLY A 1 68  ? -5.730  -18.353 25.920  1.00 32.97  ? 44  GLY A CA  1 
ATOM   290  C  C   . GLY A 1 68  ? -6.330  -17.172 25.182  1.00 34.29  ? 44  GLY A C   1 
ATOM   291  O  O   . GLY A 1 68  ? -5.661  -16.147 25.019  1.00 33.22  ? 44  GLY A O   1 
ATOM   292  N  N   . ALA A 1 69  ? -7.575  -17.288 24.727  1.00 32.50  ? 45  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 69  ? -8.247  -16.161 24.089  1.00 32.18  ? 45  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 69  ? -8.755  -15.210 25.166  1.00 33.59  ? 45  ALA A C   1 
ATOM   295  O  O   . ALA A 1 69  ? -9.612  -15.580 25.974  1.00 32.71  ? 45  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 69  ? -9.397  -16.641 23.207  1.00 28.42  ? 45  ALA A CB  1 
ATOM   297  N  N   . ALA A 1 70  ? -8.214  -13.991 25.186  1.00 30.75  ? 46  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 70  ? -8.654  -12.986 26.144  1.00 32.32  ? 46  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 70  ? -9.975  -12.341 25.748  1.00 31.18  ? 46  ALA A C   1 
ATOM   300  O  O   . ALA A 1 70  ? -10.671 -11.803 26.615  1.00 32.48  ? 46  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 70  ? -7.582  -11.905 26.294  1.00 32.71  ? 46  ALA A CB  1 
ATOM   302  N  N   . VAL A 1 71  ? -10.330 -12.379 24.466  1.00 29.86  ? 47  VAL A N   1 
ATOM   303  C  CA  . VAL A 1 71  ? -11.560 -11.785 23.959  1.00 30.81  ? 47  VAL A CA  1 
ATOM   304  C  C   . VAL A 1 71  ? -12.296 -12.838 23.146  1.00 31.56  ? 47  VAL A C   1 
ATOM   305  O  O   . VAL A 1 71  ? -11.681 -13.563 22.355  1.00 31.78  ? 47  VAL A O   1 
ATOM   306  C  CB  . VAL A 1 71  ? -11.275 -10.539 23.094  1.00 31.89  ? 47  VAL A CB  1 
ATOM   307  C  CG1 . VAL A 1 71  ? -12.574 -9.935  22.579  1.00 31.09  ? 47  VAL A CG1 1 
ATOM   308  C  CG2 . VAL A 1 71  ? -10.467 -9.509  23.876  1.00 29.51  ? 47  VAL A CG2 1 
ATOM   309  N  N   . ILE A 1 72  ? -13.610 -12.926 23.342  1.00 32.14  ? 48  ILE A N   1 
ATOM   310  C  CA  . ILE A 1 72  ? -14.472 -13.803 22.557  1.00 31.67  ? 48  ILE A CA  1 
ATOM   311  C  C   . ILE A 1 72  ? -15.438 -12.928 21.773  1.00 32.74  ? 48  ILE A C   1 
ATOM   312  O  O   . ILE A 1 72  ? -16.199 -12.150 22.364  1.00 33.74  ? 48  ILE A O   1 
ATOM   313  C  CB  . ILE A 1 72  ? -15.243 -14.805 23.431  1.00 32.87  ? 48  ILE A CB  1 
ATOM   314  C  CG1 . ILE A 1 72  ? -14.302 -15.546 24.386  1.00 32.42  ? 48  ILE A CG1 1 
ATOM   315  C  CG2 . ILE A 1 72  ? -15.994 -15.792 22.545  1.00 31.77  ? 48  ILE A CG2 1 
ATOM   316  C  CD1 . ILE A 1 72  ? -13.223 -16.369 23.703  1.00 31.03  ? 48  ILE A CD1 1 
ATOM   317  N  N   . HIS A 1 73  ? -15.407 -13.053 20.451  1.00 30.94  ? 49  HIS A N   1 
ATOM   318  C  CA  . HIS A 1 73  ? -16.320 -12.338 19.571  1.00 30.73  ? 49  HIS A CA  1 
ATOM   319  C  C   . HIS A 1 73  ? -17.500 -13.251 19.257  1.00 31.18  ? 49  HIS A C   1 
ATOM   320  O  O   . HIS A 1 73  ? -17.309 -14.368 18.764  1.00 29.21  ? 49  HIS A O   1 
ATOM   321  C  CB  . HIS A 1 73  ? -15.596 -11.907 18.298  1.00 30.28  ? 49  HIS A CB  1 
ATOM   322  C  CG  . HIS A 1 73  ? -16.468 -11.197 17.314  1.00 33.07  ? 49  HIS A CG  1 
ATOM   323  N  ND1 . HIS A 1 73  ? -16.954 -9.926  17.533  1.00 34.61  ? 49  HIS A ND1 1 
ATOM   324  C  CD2 . HIS A 1 73  ? -16.938 -11.576 16.103  1.00 30.30  ? 49  HIS A CD2 1 
ATOM   325  C  CE1 . HIS A 1 73  ? -17.687 -9.554  16.500  1.00 35.12  ? 49  HIS A CE1 1 
ATOM   326  N  NE2 . HIS A 1 73  ? -17.692 -10.537 15.619  1.00 31.00  ? 49  HIS A NE2 1 
ATOM   327  N  N   . LEU A 1 74  ? -18.714 -12.777 19.536  1.00 30.71  ? 50  LEU A N   1 
ATOM   328  C  CA  . LEU A 1 74  ? -19.890 -13.634 19.608  1.00 32.71  ? 50  LEU A CA  1 
ATOM   329  C  C   . LEU A 1 74  ? -20.957 -13.235 18.599  1.00 34.32  ? 50  LEU A C   1 
ATOM   330  O  O   . LEU A 1 74  ? -21.327 -12.060 18.502  1.00 30.92  ? 50  LEU A O   1 
ATOM   331  C  CB  . LEU A 1 74  ? -20.491 -13.603 21.017  1.00 33.54  ? 50  LEU A CB  1 
ATOM   332  C  CG  . LEU A 1 74  ? -19.656 -14.307 22.086  1.00 34.83  ? 50  LEU A CG  1 
ATOM   333  C  CD1 . LEU A 1 74  ? -20.215 -14.033 23.467  1.00 38.31  ? 50  LEU A CD1 1 
ATOM   334  C  CD2 . LEU A 1 74  ? -19.594 -15.809 21.820  1.00 33.47  ? 50  LEU A CD2 1 
ATOM   335  N  N   . HIS A 1 75  ? -21.436 -14.227 17.849  1.00 31.61  ? 51  HIS A N   1 
ATOM   336  C  CA  . HIS A 1 75  ? -22.714 -14.207 17.153  1.00 32.97  ? 51  HIS A CA  1 
ATOM   337  C  C   . HIS A 1 75  ? -23.598 -15.302 17.735  1.00 33.54  ? 51  HIS A C   1 
ATOM   338  O  O   . HIS A 1 75  ? -23.131 -16.195 18.446  1.00 33.57  ? 51  HIS A O   1 
ATOM   339  C  CB  . HIS A 1 75  ? -22.562 -14.446 15.644  1.00 32.47  ? 51  HIS A CB  1 
ATOM   340  C  CG  . HIS A 1 75  ? -21.847 -13.353 14.917  1.00 33.61  ? 51  HIS A CG  1 
ATOM   341  N  ND1 . HIS A 1 75  ? -22.346 -12.775 13.770  1.00 35.17  ? 51  HIS A ND1 1 
ATOM   342  C  CD2 . HIS A 1 75  ? -20.660 -12.750 15.157  1.00 31.19  ? 51  HIS A CD2 1 
ATOM   343  C  CE1 . HIS A 1 75  ? -21.500 -11.858 13.339  1.00 34.57  ? 51  HIS A CE1 1 
ATOM   344  N  NE2 . HIS A 1 75  ? -20.470 -11.821 14.164  1.00 33.02  ? 51  HIS A NE2 1 
ATOM   345  N  N   . ALA A 1 76  ? -24.885 -15.236 17.409  1.00 35.41  ? 52  ALA A N   1 
ATOM   346  C  CA  . ALA A 1 76  ? -25.838 -16.269 17.779  1.00 36.25  ? 52  ALA A CA  1 
ATOM   347  C  C   . ALA A 1 76  ? -26.524 -16.793 16.524  1.00 36.05  ? 52  ALA A C   1 
ATOM   348  O  O   . ALA A 1 76  ? -26.495 -16.160 15.465  1.00 36.19  ? 52  ALA A O   1 
ATOM   349  C  CB  . ALA A 1 76  ? -26.873 -15.738 18.778  1.00 36.55  ? 52  ALA A CB  1 
ATOM   350  N  N   . ARG A 1 77  ? -27.141 -17.966 16.648  1.00 37.72  ? 53  ARG A N   1 
ATOM   351  C  CA  . ARG A 1 77  ? -27.811 -18.604 15.525  1.00 37.44  ? 53  ARG A CA  1 
ATOM   352  C  C   . ARG A 1 77  ? -29.117 -19.234 15.987  1.00 41.63  ? 53  ARG A C   1 
ATOM   353  O  O   . ARG A 1 77  ? -29.287 -19.563 17.164  1.00 41.94  ? 53  ARG A O   1 
ATOM   354  C  CB  . ARG A 1 77  ? -26.923 -19.675 14.879  1.00 37.00  ? 53  ARG A CB  1 
ATOM   355  C  CG  . ARG A 1 77  ? -25.675 -19.123 14.206  1.00 37.64  ? 53  ARG A CG  1 
ATOM   356  C  CD  . ARG A 1 77  ? -24.756 -20.240 13.728  1.00 36.15  ? 53  ARG A CD  1 
ATOM   357  N  NE  . ARG A 1 77  ? -23.599 -19.726 13.006  1.00 35.62  ? 53  ARG A NE  1 
ATOM   358  C  CZ  . ARG A 1 77  ? -23.578 -19.458 11.706  1.00 36.69  ? 53  ARG A CZ  1 
ATOM   359  N  NH1 . ARG A 1 77  ? -24.645 -19.642 10.943  1.00 36.44  ? 53  ARG A NH1 1 
ATOM   360  N  NH2 . ARG A 1 77  ? -22.459 -18.991 11.158  1.00 31.96  ? 53  ARG A NH2 1 
ATOM   361  N  N   . HIS A 1 78  ? -30.045 -19.388 15.043  1.00 39.09  ? 54  HIS A N   1 
ATOM   362  C  CA  . HIS A 1 78  ? -31.249 -20.167 15.300  1.00 44.74  ? 54  HIS A CA  1 
ATOM   363  C  C   . HIS A 1 78  ? -30.885 -21.639 15.427  1.00 47.76  ? 54  HIS A C   1 
ATOM   364  O  O   . HIS A 1 78  ? -30.256 -22.213 14.532  1.00 47.56  ? 54  HIS A O   1 
ATOM   365  C  CB  . HIS A 1 78  ? -32.266 -19.978 14.176  1.00 41.92  ? 54  HIS A CB  1 
ATOM   366  C  CG  . HIS A 1 78  ? -32.802 -18.585 14.065  1.00 41.36  ? 54  HIS A CG  1 
ATOM   367  N  ND1 . HIS A 1 78  ? -32.402 -17.710 13.078  1.00 41.12  ? 54  HIS A ND1 1 
ATOM   368  C  CD2 . HIS A 1 78  ? -33.715 -17.918 14.810  1.00 42.22  ? 54  HIS A CD2 1 
ATOM   369  C  CE1 . HIS A 1 78  ? -33.041 -16.563 13.223  1.00 41.20  ? 54  HIS A CE1 1 
ATOM   370  N  NE2 . HIS A 1 78  ? -33.844 -16.663 14.266  1.00 41.75  ? 54  HIS A NE2 1 
ATOM   371  N  N   . GLU A 1 79  ? -31.282 -22.255 16.541  1.00 52.48  ? 55  GLU A N   1 
ATOM   372  C  CA  . GLU A 1 79  ? -30.952 -23.658 16.757  1.00 54.07  ? 55  GLU A CA  1 
ATOM   373  C  C   . GLU A 1 79  ? -31.684 -24.577 15.788  1.00 53.01  ? 55  GLU A C   1 
ATOM   374  O  O   . GLU A 1 79  ? -31.242 -25.711 15.577  1.00 53.12  ? 55  GLU A O   1 
ATOM   375  C  CB  . GLU A 1 79  ? -31.267 -24.050 18.202  1.00 57.03  ? 55  GLU A CB  1 
ATOM   376  C  CG  . GLU A 1 79  ? -30.651 -23.109 19.231  1.00 58.93  ? 55  GLU A CG  1 
ATOM   377  C  CD  . GLU A 1 79  ? -30.425 -23.768 20.579  1.00 62.41  ? 55  GLU A CD  1 
ATOM   378  O  OE1 . GLU A 1 79  ? -30.940 -24.887 20.792  1.00 63.46  ? 55  GLU A OE1 1 
ATOM   379  O  OE2 . GLU A 1 79  ? -29.725 -23.165 21.422  1.00 58.93  ? 55  GLU A OE2 1 
ATOM   380  N  N   . GLY A 1 80  ? -32.774 -24.112 15.185  1.00 51.00  ? 56  GLY A N   1 
ATOM   381  C  CA  . GLY A 1 80  ? -33.522 -24.917 14.241  1.00 51.79  ? 56  GLY A CA  1 
ATOM   382  C  C   . GLY A 1 80  ? -32.752 -25.245 12.979  1.00 55.29  ? 56  GLY A C   1 
ATOM   383  O  O   . GLY A 1 80  ? -32.503 -26.420 12.692  1.00 58.95  ? 56  GLY A O   1 
ATOM   384  N  N   . ASP A 1 81  ? -32.369 -24.220 12.214  1.00 52.21  ? 57  ASP A N   1 
ATOM   385  C  CA  . ASP A 1 81  ? -31.677 -24.416 10.945  1.00 50.22  ? 57  ASP A CA  1 
ATOM   386  C  C   . ASP A 1 81  ? -30.302 -23.756 10.906  1.00 43.81  ? 57  ASP A C   1 
ATOM   387  O  O   . ASP A 1 81  ? -29.662 -23.752 9.848   1.00 43.08  ? 57  ASP A O   1 
ATOM   388  C  CB  . ASP A 1 81  ? -32.539 -23.897 9.786   1.00 50.87  ? 57  ASP A CB  1 
ATOM   389  C  CG  . ASP A 1 81  ? -32.801 -22.404 9.869   1.00 49.49  ? 57  ASP A CG  1 
ATOM   390  O  OD1 . ASP A 1 81  ? -32.274 -21.750 10.795  1.00 45.83  ? 57  ASP A OD1 1 
ATOM   391  O  OD2 . ASP A 1 81  ? -33.538 -21.885 9.002   1.00 50.04  ? 57  ASP A OD2 1 
ATOM   392  N  N   . GLY A 1 82  ? -29.831 -23.200 12.020  1.00 43.17  ? 58  GLY A N   1 
ATOM   393  C  CA  . GLY A 1 82  ? -28.495 -22.639 12.088  1.00 43.45  ? 58  GLY A CA  1 
ATOM   394  C  C   . GLY A 1 82  ? -28.315 -21.288 11.431  1.00 42.33  ? 58  GLY A C   1 
ATOM   395  O  O   . GLY A 1 82  ? -27.179 -20.800 11.366  1.00 38.93  ? 58  GLY A O   1 
ATOM   396  N  N   . SER A 1 83  ? -29.386 -20.666 10.942  1.00 41.75  ? 59  SER A N   1 
ATOM   397  C  CA  . SER A 1 83  ? -29.265 -19.368 10.300  1.00 39.47  ? 59  SER A CA  1 
ATOM   398  C  C   . SER A 1 83  ? -28.907 -18.295 11.327  1.00 36.78  ? 59  SER A C   1 
ATOM   399  O  O   . SER A 1 83  ? -29.134 -18.466 12.526  1.00 38.44  ? 59  SER A O   1 
ATOM   400  C  CB  . SER A 1 83  ? -30.566 -18.999 9.590   1.00 38.00  ? 59  SER A CB  1 
ATOM   401  O  OG  . SER A 1 83  ? -31.647 -18.937 10.502  1.00 39.37  ? 59  SER A OG  1 
ATOM   402  N  N   . PRO A 1 84  ? -28.337 -17.177 10.878  1.00 37.20  ? 60  PRO A N   1 
ATOM   403  C  CA  . PRO A 1 84  ? -27.981 -16.108 11.819  1.00 38.29  ? 60  PRO A CA  1 
ATOM   404  C  C   . PRO A 1 84  ? -29.187 -15.605 12.598  1.00 40.19  ? 60  PRO A C   1 
ATOM   405  O  O   . PRO A 1 84  ? -30.272 -15.403 12.046  1.00 40.13  ? 60  PRO A O   1 
ATOM   406  C  CB  . PRO A 1 84  ? -27.402 -15.020 10.908  1.00 37.11  ? 60  PRO A CB  1 
ATOM   407  C  CG  . PRO A 1 84  ? -26.850 -15.775 9.747   1.00 37.23  ? 60  PRO A CG  1 
ATOM   408  C  CD  . PRO A 1 84  ? -27.805 -16.917 9.527   1.00 35.65  ? 60  PRO A CD  1 
ATOM   409  N  N   . ASP A 1 85  ? -28.983 -15.405 13.901  1.00 38.86  ? 61  ASP A N   1 
ATOM   410  C  CA  . ASP A 1 85  ? -30.009 -14.888 14.803  1.00 40.28  ? 61  ASP A CA  1 
ATOM   411  C  C   . ASP A 1 85  ? -29.401 -13.727 15.578  1.00 39.79  ? 61  ASP A C   1 
ATOM   412  O  O   . ASP A 1 85  ? -28.566 -13.937 16.464  1.00 38.81  ? 61  ASP A O   1 
ATOM   413  C  CB  . ASP A 1 85  ? -30.514 -15.978 15.751  1.00 37.75  ? 61  ASP A CB  1 
ATOM   414  C  CG  . ASP A 1 85  ? -31.693 -15.523 16.595  1.00 43.88  ? 61  ASP A CG  1 
ATOM   415  O  OD1 . ASP A 1 85  ? -32.082 -14.339 16.500  1.00 43.43  ? 61  ASP A OD1 1 
ATOM   416  O  OD2 . ASP A 1 85  ? -32.233 -16.355 17.358  1.00 42.46  ? 61  ASP A OD2 1 
ATOM   417  N  N   . GLN A 1 86  ? -29.813 -12.507 15.241  1.00 39.14  ? 62  GLN A N   1 
ATOM   418  C  CA  . GLN A 1 86  ? -29.298 -11.292 15.861  1.00 40.00  ? 62  GLN A CA  1 
ATOM   419  C  C   . GLN A 1 86  ? -30.324 -10.669 16.806  1.00 44.02  ? 62  GLN A C   1 
ATOM   420  O  O   . GLN A 1 86  ? -30.332 -9.456  17.019  1.00 46.51  ? 62  GLN A O   1 
ATOM   421  C  CB  . GLN A 1 86  ? -28.870 -10.304 14.774  1.00 42.67  ? 62  GLN A CB  1 
ATOM   422  C  CG  . GLN A 1 86  ? -28.143 -9.039  15.242  1.00 40.92  ? 62  GLN A CG  1 
ATOM   423  C  CD  . GLN A 1 86  ? -26.866 -9.313  16.017  1.00 39.78  ? 62  GLN A CD  1 
ATOM   424  O  OE1 . GLN A 1 86  ? -26.450 -10.462 16.186  1.00 38.20  ? 62  GLN A OE1 1 
ATOM   425  N  NE2 . GLN A 1 86  ? -26.233 -8.247  16.489  1.00 37.60  ? 62  GLN A NE2 1 
ATOM   426  N  N   . SER A 1 87  ? -31.195 -11.490 17.383  1.00 43.80  ? 63  SER A N   1 
ATOM   427  C  CA  . SER A 1 87  ? -32.175 -10.999 18.338  1.00 45.83  ? 63  SER A CA  1 
ATOM   428  C  C   . SER A 1 87  ? -31.561 -10.904 19.731  1.00 45.96  ? 63  SER A C   1 
ATOM   429  O  O   . SER A 1 87  ? -30.597 -11.601 20.060  1.00 43.24  ? 63  SER A O   1 
ATOM   430  C  CB  . SER A 1 87  ? -33.398 -11.915 18.371  1.00 43.34  ? 63  SER A CB  1 
ATOM   431  O  OG  . SER A 1 87  ? -33.060 -13.193 18.878  1.00 47.04  ? 63  SER A OG  1 
ATOM   432  N  N   . VAL A 1 88  ? -32.133 -10.020 20.551  1.00 46.32  ? 64  VAL A N   1 
ATOM   433  C  CA  . VAL A 1 88  ? -31.668 -9.872  21.929  1.00 45.68  ? 64  VAL A CA  1 
ATOM   434  C  C   . VAL A 1 88  ? -31.783 -11.199 22.667  1.00 46.98  ? 64  VAL A C   1 
ATOM   435  O  O   . VAL A 1 88  ? -30.863 -11.617 23.382  1.00 44.93  ? 64  VAL A O   1 
ATOM   436  C  CB  . VAL A 1 88  ? -32.463 -8.760  22.642  1.00 49.02  ? 64  VAL A CB  1 
ATOM   437  C  CG1 . VAL A 1 88  ? -32.035 -8.645  24.100  1.00 47.15  ? 64  VAL A CG1 1 
ATOM   438  C  CG2 . VAL A 1 88  ? -32.287 -7.429  21.922  1.00 49.05  ? 64  VAL A CG2 1 
ATOM   439  N  N   . GLU A 1 89  ? -32.915 -11.886 22.497  1.00 45.09  ? 65  GLU A N   1 
ATOM   440  C  CA  . GLU A 1 89  ? -33.149 -13.139 23.206  1.00 46.84  ? 65  GLU A CA  1 
ATOM   441  C  C   . GLU A 1 89  ? -32.103 -14.192 22.866  1.00 43.93  ? 65  GLU A C   1 
ATOM   442  O  O   . GLU A 1 89  ? -31.763 -15.022 23.717  1.00 43.87  ? 65  GLU A O   1 
ATOM   443  C  CB  . GLU A 1 89  ? -34.552 -13.657 22.879  1.00 50.42  ? 65  GLU A CB  1 
ATOM   444  C  CG  . GLU A 1 89  ? -34.836 -15.081 23.345  1.00 54.54  ? 65  GLU A CG  1 
ATOM   445  C  CD  . GLU A 1 89  ? -34.746 -15.236 24.851  1.00 62.16  ? 65  GLU A CD  1 
ATOM   446  O  OE1 . GLU A 1 89  ? -35.205 -14.324 25.572  1.00 63.63  ? 65  GLU A OE1 1 
ATOM   447  O  OE2 . GLU A 1 89  ? -34.212 -16.269 25.310  1.00 63.20  ? 65  GLU A OE2 1 
ATOM   448  N  N   . ALA A 1 90  ? -31.586 -14.183 21.636  1.00 43.55  ? 66  ALA A N   1 
ATOM   449  C  CA  . ALA A 1 90  ? -30.678 -15.244 21.210  1.00 45.54  ? 66  ALA A CA  1 
ATOM   450  C  C   . ALA A 1 90  ? -29.385 -15.246 22.017  1.00 39.51  ? 66  ALA A C   1 
ATOM   451  O  O   . ALA A 1 90  ? -28.754 -16.298 22.171  1.00 39.31  ? 66  ALA A O   1 
ATOM   452  C  CB  . ALA A 1 90  ? -30.369 -15.102 19.720  1.00 40.73  ? 66  ALA A CB  1 
ATOM   453  N  N   . PHE A 1 91  ? -28.970 -14.090 22.530  1.00 38.74  ? 67  PHE A N   1 
ATOM   454  C  CA  . PHE A 1 91  ? -27.760 -14.000 23.335  1.00 39.16  ? 67  PHE A CA  1 
ATOM   455  C  C   . PHE A 1 91  ? -28.007 -14.273 24.814  1.00 41.75  ? 67  PHE A C   1 
ATOM   456  O  O   . PHE A 1 91  ? -27.041 -14.426 25.569  1.00 42.70  ? 67  PHE A O   1 
ATOM   457  C  CB  . PHE A 1 91  ? -27.124 -12.612 23.180  1.00 37.50  ? 67  PHE A CB  1 
ATOM   458  C  CG  . PHE A 1 91  ? -26.449 -12.393 21.851  1.00 35.47  ? 67  PHE A CG  1 
ATOM   459  C  CD1 . PHE A 1 91  ? -27.155 -11.884 20.772  1.00 38.37  ? 67  PHE A CD1 1 
ATOM   460  C  CD2 . PHE A 1 91  ? -25.103 -12.686 21.685  1.00 34.94  ? 67  PHE A CD2 1 
ATOM   461  C  CE1 . PHE A 1 91  ? -26.533 -11.678 19.552  1.00 39.01  ? 67  PHE A CE1 1 
ATOM   462  C  CE2 . PHE A 1 91  ? -24.478 -12.480 20.467  1.00 34.30  ? 67  PHE A CE2 1 
ATOM   463  C  CZ  . PHE A 1 91  ? -25.194 -11.976 19.401  1.00 36.38  ? 67  PHE A CZ  1 
ATOM   464  N  N   . ASN A 1 92  ? -29.268 -14.350 25.241  1.00 41.59  ? 68  ASN A N   1 
ATOM   465  C  CA  . ASN A 1 92  ? -29.558 -14.528 26.663  1.00 42.82  ? 68  ASN A CA  1 
ATOM   466  C  C   . ASN A 1 92  ? -28.970 -15.812 27.230  1.00 44.24  ? 68  ASN A C   1 
ATOM   467  O  O   . ASN A 1 92  ? -28.344 -15.756 28.303  1.00 43.41  ? 68  ASN A O   1 
ATOM   468  C  CB  . ASN A 1 92  ? -31.071 -14.468 26.888  1.00 45.52  ? 68  ASN A CB  1 
ATOM   469  C  CG  . ASN A 1 92  ? -31.445 -14.637 28.345  1.00 50.85  ? 68  ASN A CG  1 
ATOM   470  O  OD1 . ASN A 1 92  ? -32.006 -15.659 28.741  1.00 54.49  ? 68  ASN A OD1 1 
ATOM   471  N  ND2 . ASN A 1 92  ? -31.119 -13.638 29.156  1.00 49.78  ? 68  ASN A ND2 1 
ATOM   472  N  N   . PRO A 1 93  ? -29.132 -16.980 26.605  1.00 44.58  ? 69  PRO A N   1 
ATOM   473  C  CA  . PRO A 1 93  ? -28.500 -18.199 27.125  1.00 43.14  ? 69  PRO A CA  1 
ATOM   474  C  C   . PRO A 1 93  ? -27.014 -18.322 26.823  1.00 41.41  ? 69  PRO A C   1 
ATOM   475  O  O   . PRO A 1 93  ? -26.444 -19.392 27.054  1.00 42.34  ? 69  PRO A O   1 
ATOM   476  C  CB  . PRO A 1 93  ? -29.289 -19.313 26.419  1.00 43.48  ? 69  PRO A CB  1 
ATOM   477  C  CG  . PRO A 1 93  ? -29.728 -18.703 25.142  1.00 44.95  ? 69  PRO A CG  1 
ATOM   478  C  CD  . PRO A 1 93  ? -30.001 -17.260 25.446  1.00 43.12  ? 69  PRO A CD  1 
ATOM   479  N  N   . ILE A 1 94  ? -26.372 -17.269 26.321  1.00 41.08  ? 70  ILE A N   1 
ATOM   480  C  CA  . ILE A 1 94  ? -24.964 -17.309 25.925  1.00 41.10  ? 70  ILE A CA  1 
ATOM   481  C  C   . ILE A 1 94  ? -24.103 -16.450 26.849  1.00 41.27  ? 70  ILE A C   1 
ATOM   482  O  O   . ILE A 1 94  ? -23.134 -16.935 27.437  1.00 39.16  ? 70  ILE A O   1 
ATOM   483  C  CB  . ILE A 1 94  ? -24.794 -16.881 24.450  1.00 38.84  ? 70  ILE A CB  1 
ATOM   484  C  CG1 . ILE A 1 94  ? -25.306 -17.977 23.513  1.00 41.23  ? 70  ILE A CG1 1 
ATOM   485  C  CG2 . ILE A 1 94  ? -23.336 -16.555 24.156  1.00 35.23  ? 70  ILE A CG2 1 
ATOM   486  C  CD1 . ILE A 1 94  ? -25.509 -17.512 22.085  1.00 38.19  ? 70  ILE A CD1 1 
ATOM   487  N  N   . LEU A 1 95  ? -24.438 -15.165 26.981  1.00 39.97  ? 71  LEU A N   1 
ATOM   488  C  CA  . LEU A 1 95  ? -23.540 -14.223 27.644  1.00 38.52  ? 71  LEU A CA  1 
ATOM   489  C  C   . LEU A 1 95  ? -23.352 -14.575 29.115  1.00 42.06  ? 71  LEU A C   1 
ATOM   490  O  O   . LEU A 1 95  ? -22.219 -14.709 29.593  1.00 40.04  ? 71  LEU A O   1 
ATOM   491  C  CB  . LEU A 1 95  ? -24.082 -12.801 27.493  1.00 37.67  ? 71  LEU A CB  1 
ATOM   492  C  CG  . LEU A 1 95  ? -24.187 -12.290 26.055  1.00 38.63  ? 71  LEU A CG  1 
ATOM   493  C  CD1 . LEU A 1 95  ? -24.951 -10.976 26.005  1.00 37.39  ? 71  LEU A CD1 1 
ATOM   494  C  CD2 . LEU A 1 95  ? -22.801 -12.132 25.440  1.00 37.92  ? 71  LEU A CD2 1 
ATOM   495  N  N   . GLY A 1 96  ? -24.454 -14.719 29.854  1.00 41.02  ? 72  GLY A N   1 
ATOM   496  C  CA  . GLY A 1 96  ? -24.346 -14.996 31.276  1.00 37.26  ? 72  GLY A CA  1 
ATOM   497  C  C   . GLY A 1 96  ? -23.640 -16.302 31.577  1.00 37.82  ? 72  GLY A C   1 
ATOM   498  O  O   . GLY A 1 96  ? -22.918 -16.406 32.572  1.00 41.64  ? 72  GLY A O   1 
ATOM   499  N  N   . VAL A 1 97  ? -23.831 -17.313 30.729  1.00 38.24  ? 73  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 97  ? -23.175 -18.597 30.954  1.00 40.43  ? 73  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 97  ? -21.663 -18.459 30.815  1.00 37.40  ? 73  VAL A C   1 
ATOM   502  O  O   . VAL A 1 97  ? -20.899 -18.986 31.634  1.00 38.87  ? 73  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 97  ? -23.738 -19.658 29.992  1.00 39.86  ? 73  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 97  ? -22.911 -20.936 30.066  1.00 38.68  ? 73  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 97  ? -25.199 -19.944 30.316  1.00 42.64  ? 73  VAL A CG2 1 
ATOM   506  N  N   . ILE A 1 98  ? -21.203 -17.753 29.780  1.00 36.49  ? 74  ILE A N   1 
ATOM   507  C  CA  . ILE A 1 98  ? -19.765 -17.582 29.586  1.00 38.92  ? 74  ILE A CA  1 
ATOM   508  C  C   . ILE A 1 98  ? -19.169 -16.782 30.735  1.00 37.76  ? 74  ILE A C   1 
ATOM   509  O  O   . ILE A 1 98  ? -18.108 -17.125 31.269  1.00 42.27  ? 74  ILE A O   1 
ATOM   510  C  CB  . ILE A 1 98  ? -19.483 -16.910 28.229  1.00 35.86  ? 74  ILE A CB  1 
ATOM   511  C  CG1 . ILE A 1 98  ? -19.933 -17.815 27.079  1.00 34.45  ? 74  ILE A CG1 1 
ATOM   512  C  CG2 . ILE A 1 98  ? -18.004 -16.575 28.107  1.00 34.18  ? 74  ILE A CG2 1 
ATOM   513  C  CD1 . ILE A 1 98  ? -19.985 -17.118 25.731  1.00 31.83  ? 74  ILE A CD1 1 
ATOM   514  N  N   . LYS A 1 99  ? -19.846 -15.705 31.135  1.00 38.70  ? 75  LYS A N   1 
ATOM   515  C  CA  . LYS A 1 99  ? -19.327 -14.851 32.197  1.00 41.13  ? 75  LYS A CA  1 
ATOM   516  C  C   . LYS A 1 99  ? -19.126 -15.632 33.492  1.00 41.85  ? 75  LYS A C   1 
ATOM   517  O  O   . LYS A 1 99  ? -18.104 -15.469 34.170  1.00 45.69  ? 75  LYS A O   1 
ATOM   518  C  CB  . LYS A 1 99  ? -20.278 -13.675 32.414  1.00 43.66  ? 75  LYS A CB  1 
ATOM   519  C  CG  . LYS A 1 99  ? -19.703 -12.550 33.245  1.00 44.30  ? 75  LYS A CG  1 
ATOM   520  C  CD  . LYS A 1 99  ? -20.724 -11.444 33.438  1.00 47.43  ? 75  LYS A CD  1 
ATOM   521  C  CE  . LYS A 1 99  ? -20.354 -10.557 34.610  1.00 53.73  ? 75  LYS A CE  1 
ATOM   522  N  NZ  . LYS A 1 99  ? -21.400 -9.543  34.907  1.00 54.68  ? 75  LYS A NZ  1 
ATOM   523  N  N   . GLN A 1 100 ? -20.087 -16.489 33.852  1.00 41.74  ? 76  GLN A N   1 
ATOM   524  C  CA  . GLN A 1 100 ? -19.956 -17.275 35.076  1.00 42.18  ? 76  GLN A CA  1 
ATOM   525  C  C   . GLN A 1 100 ? -18.749 -18.201 35.028  1.00 42.31  ? 76  GLN A C   1 
ATOM   526  O  O   . GLN A 1 100 ? -18.145 -18.486 36.068  1.00 43.31  ? 76  GLN A O   1 
ATOM   527  C  CB  . GLN A 1 100 ? -21.223 -18.099 35.319  1.00 43.77  ? 76  GLN A CB  1 
ATOM   528  C  CG  . GLN A 1 100 ? -22.325 -17.358 36.044  1.00 42.95  ? 76  GLN A CG  1 
ATOM   529  C  CD  . GLN A 1 100 ? -21.936 -16.970 37.455  1.00 43.58  ? 76  GLN A CD  1 
ATOM   530  O  OE1 . GLN A 1 100 ? -21.534 -17.810 38.259  1.00 44.57  ? 76  GLN A OE1 1 
ATOM   531  N  NE2 . GLN A 1 100 ? -22.050 -15.688 37.762  1.00 44.29  ? 76  GLN A NE2 1 
ATOM   532  N  N   . ALA A 1 101 ? -18.388 -18.685 33.841  1.00 40.56  ? 77  ALA A N   1 
ATOM   533  C  CA  . ALA A 1 101 ? -17.326 -19.668 33.695  1.00 41.85  ? 77  ALA A CA  1 
ATOM   534  C  C   . ALA A 1 101 ? -15.974 -19.061 33.344  1.00 42.28  ? 77  ALA A C   1 
ATOM   535  O  O   . ALA A 1 101 ? -14.965 -19.771 33.407  1.00 43.13  ? 77  ALA A O   1 
ATOM   536  C  CB  . ALA A 1 101 ? -17.706 -20.690 32.617  1.00 41.99  ? 77  ALA A CB  1 
ATOM   537  N  N   . SER A 1 102 ? -15.921 -17.781 32.984  1.00 43.10  ? 78  SER A N   1 
ATOM   538  C  CA  . SER A 1 102 ? -14.693 -17.201 32.461  1.00 42.94  ? 78  SER A CA  1 
ATOM   539  C  C   . SER A 1 102 ? -14.759 -15.687 32.578  1.00 42.29  ? 78  SER A C   1 
ATOM   540  O  O   . SER A 1 102 ? -15.834 -15.091 32.481  1.00 40.55  ? 78  SER A O   1 
ATOM   541  C  CB  . SER A 1 102 ? -14.472 -17.608 30.999  1.00 39.76  ? 78  SER A CB  1 
ATOM   542  O  OG  . SER A 1 102 ? -13.480 -16.805 30.385  1.00 39.20  ? 78  SER A OG  1 
ATOM   543  N  N   . ASP A 1 103 ? -13.594 -15.072 32.776  1.00 40.22  ? 79  ASP A N   1 
ATOM   544  C  CA  . ASP A 1 103 ? -13.481 -13.622 32.825  1.00 41.80  ? 79  ASP A CA  1 
ATOM   545  C  C   . ASP A 1 103 ? -13.048 -13.030 31.490  1.00 37.19  ? 79  ASP A C   1 
ATOM   546  O  O   . ASP A 1 103 ? -12.664 -11.858 31.439  1.00 39.11  ? 79  ASP A O   1 
ATOM   547  C  CB  . ASP A 1 103 ? -12.504 -13.200 33.926  1.00 46.07  ? 79  ASP A CB  1 
ATOM   548  C  CG  . ASP A 1 103 ? -11.076 -13.623 33.638  1.00 52.44  ? 79  ASP A CG  1 
ATOM   549  O  OD1 . ASP A 1 103 ? -10.882 -14.649 32.950  1.00 54.83  ? 79  ASP A OD1 1 
ATOM   550  O  OD2 . ASP A 1 103 ? -10.145 -12.931 34.104  1.00 59.48  ? 79  ASP A OD2 1 
ATOM   551  N  N   . ALA A 1 104 ? -13.099 -13.813 30.413  1.00 36.52  ? 80  ALA A N   1 
ATOM   552  C  CA  . ALA A 1 104 ? -12.809 -13.286 29.088  1.00 37.06  ? 80  ALA A CA  1 
ATOM   553  C  C   . ALA A 1 104 ? -13.682 -12.074 28.792  1.00 35.25  ? 80  ALA A C   1 
ATOM   554  O  O   . ALA A 1 104 ? -14.803 -11.949 29.294  1.00 34.46  ? 80  ALA A O   1 
ATOM   555  C  CB  . ALA A 1 104 ? -13.041 -14.362 28.023  1.00 35.91  ? 80  ALA A CB  1 
ATOM   556  N  N   . VAL A 1 105 ? -13.158 -11.173 27.970  1.00 34.11  ? 81  VAL A N   1 
ATOM   557  C  CA  . VAL A 1 105 ? -13.936 -10.038 27.489  1.00 34.77  ? 81  VAL A CA  1 
ATOM   558  C  C   . VAL A 1 105 ? -14.864 -10.526 26.386  1.00 33.27  ? 81  VAL A C   1 
ATOM   559  O  O   . VAL A 1 105 ? -14.425 -11.193 25.441  1.00 31.99  ? 81  VAL A O   1 
ATOM   560  C  CB  . VAL A 1 105 ? -13.014 -8.918  26.983  1.00 33.42  ? 81  VAL A CB  1 
ATOM   561  C  CG1 . VAL A 1 105 ? -13.834 -7.732  26.492  1.00 34.22  ? 81  VAL A CG1 1 
ATOM   562  C  CG2 . VAL A 1 105 ? -12.047 -8.495  28.073  1.00 34.11  ? 81  VAL A CG2 1 
ATOM   563  N  N   . LEU A 1 106 ? -16.147 -10.201 26.501  1.00 32.71  ? 82  LEU A N   1 
ATOM   564  C  CA  . LEU A 1 106 ? -17.148 -10.634 25.535  1.00 33.50  ? 82  LEU A CA  1 
ATOM   565  C  C   . LEU A 1 106 ? -17.415 -9.502  24.550  1.00 34.53  ? 82  LEU A C   1 
ATOM   566  O  O   . LEU A 1 106 ? -17.769 -8.387  24.952  1.00 33.73  ? 82  LEU A O   1 
ATOM   567  C  CB  . LEU A 1 106 ? -18.433 -11.072 26.238  1.00 35.01  ? 82  LEU A CB  1 
ATOM   568  C  CG  . LEU A 1 106 ? -18.237 -12.170 27.292  1.00 35.04  ? 82  LEU A CG  1 
ATOM   569  C  CD1 . LEU A 1 106 ? -19.573 -12.721 27.756  1.00 35.36  ? 82  LEU A CD1 1 
ATOM   570  C  CD2 . LEU A 1 106 ? -17.348 -13.298 26.769  1.00 34.33  ? 82  LEU A CD2 1 
ATOM   571  N  N   . ASN A 1 107 ? -17.245 -9.801  23.267  1.00 31.94  ? 83  ASN A N   1 
ATOM   572  C  CA  . ASN A 1 107 ? -17.311 -8.833  22.178  1.00 31.89  ? 83  ASN A CA  1 
ATOM   573  C  C   . ASN A 1 107 ? -18.535 -9.174  21.335  1.00 33.89  ? 83  ASN A C   1 
ATOM   574  O  O   . ASN A 1 107 ? -18.529 -10.165 20.597  1.00 33.84  ? 83  ASN A O   1 
ATOM   575  C  CB  . ASN A 1 107 ? -16.013 -8.889  21.371  1.00 31.15  ? 83  ASN A CB  1 
ATOM   576  C  CG  . ASN A 1 107 ? -16.045 -8.037  20.117  1.00 34.94  ? 83  ASN A CG  1 
ATOM   577  O  OD1 . ASN A 1 107 ? -17.087 -7.524  19.713  1.00 35.15  ? 83  ASN A OD1 1 
ATOM   578  N  ND2 . ASN A 1 107 ? -14.886 -7.903  19.477  1.00 35.88  ? 83  ASN A ND2 1 
ATOM   579  N  N   . ILE A 1 108 ? -19.583 -8.365  21.454  1.00 31.39  ? 84  ILE A N   1 
ATOM   580  C  CA  . ILE A 1 108 ? -20.859 -8.644  20.803  1.00 34.63  ? 84  ILE A CA  1 
ATOM   581  C  C   . ILE A 1 108 ? -20.877 -7.998  19.425  1.00 34.35  ? 84  ILE A C   1 
ATOM   582  O  O   . ILE A 1 108 ? -20.537 -6.819  19.273  1.00 35.66  ? 84  ILE A O   1 
ATOM   583  C  CB  . ILE A 1 108 ? -22.035 -8.142  21.657  1.00 34.45  ? 84  ILE A CB  1 
ATOM   584  C  CG1 . ILE A 1 108 ? -22.085 -8.908  22.981  1.00 33.92  ? 84  ILE A CG1 1 
ATOM   585  C  CG2 . ILE A 1 108 ? -23.349 -8.291  20.886  1.00 34.54  ? 84  ILE A CG2 1 
ATOM   586  C  CD1 . ILE A 1 108 ? -23.173 -8.432  23.934  1.00 33.54  ? 84  ILE A CD1 1 
ATOM   587  N  N   . THR A 1 109 ? -21.288 -8.768  18.423  1.00 33.86  ? 85  THR A N   1 
ATOM   588  C  CA  . THR A 1 109 ? -21.357 -8.254  17.065  1.00 31.60  ? 85  THR A CA  1 
ATOM   589  C  C   . THR A 1 109 ? -22.464 -7.217  16.923  1.00 35.69  ? 85  THR A C   1 
ATOM   590  O  O   . THR A 1 109 ? -23.570 -7.385  17.447  1.00 33.69  ? 85  THR A O   1 
ATOM   591  C  CB  . THR A 1 109 ? -21.603 -9.395  16.075  1.00 34.48  ? 85  THR A CB  1 
ATOM   592  O  OG1 . THR A 1 109 ? -21.518 -8.894  14.737  1.00 35.25  ? 85  THR A OG1 1 
ATOM   593  C  CG2 . THR A 1 109 ? -22.985 -10.018 16.288  1.00 33.15  ? 85  THR A CG2 1 
ATOM   594  N  N   . THR A 1 110 ? -22.149 -6.126  16.224  1.00 32.62  ? 86  THR A N   1 
ATOM   595  C  CA  . THR A 1 110 ? -23.159 -5.249  15.648  1.00 36.28  ? 86  THR A CA  1 
ATOM   596  C  C   . THR A 1 110 ? -23.250 -5.426  14.139  1.00 36.15  ? 86  THR A C   1 
ATOM   597  O  O   . THR A 1 110 ? -23.949 -4.657  13.474  1.00 36.14  ? 86  THR A O   1 
ATOM   598  C  CB  . THR A 1 110 ? -22.876 -3.777  15.970  1.00 33.74  ? 86  THR A CB  1 
ATOM   599  O  OG1 . THR A 1 110 ? -21.828 -3.286  15.124  1.00 32.92  ? 86  THR A OG1 1 
ATOM   600  C  CG2 . THR A 1 110 ? -22.486 -3.593  17.436  1.00 35.35  ? 86  THR A CG2 1 
ATOM   601  N  N   . GLY A 1 111 ? -22.550 -6.413  13.587  1.00 35.19  ? 87  GLY A N   1 
ATOM   602  C  CA  . GLY A 1 111 ? -22.610 -6.683  12.167  1.00 35.23  ? 87  GLY A CA  1 
ATOM   603  C  C   . GLY A 1 111 ? -23.658 -7.720  11.824  1.00 39.33  ? 87  GLY A C   1 
ATOM   604  O  O   . GLY A 1 111 ? -24.324 -7.614  10.790  1.00 40.62  ? 87  GLY A O   1 
ATOM   605  N  N   . GLY A 1 112 ? -23.820 -8.719  12.689  1.00 37.21  ? 88  GLY A N   1 
ATOM   606  C  CA  . GLY A 1 112 ? -24.739 -9.803  12.404  1.00 36.44  ? 88  GLY A CA  1 
ATOM   607  C  C   . GLY A 1 112 ? -24.472 -10.394 11.037  1.00 39.63  ? 88  GLY A C   1 
ATOM   608  O  O   . GLY A 1 112 ? -23.325 -10.487 10.581  1.00 40.16  ? 88  GLY A O   1 
ATOM   609  N  N   . ALA A 1 113 ? -25.546 -10.810 10.369  1.00 40.66  ? 89  ALA A N   1 
ATOM   610  C  CA  . ALA A 1 113 ? -25.427 -11.174 8.964   1.00 41.04  ? 89  ALA A CA  1 
ATOM   611  C  C   . ALA A 1 113 ? -25.393 -9.906  8.110   1.00 42.31  ? 89  ALA A C   1 
ATOM   612  O  O   . ALA A 1 113 ? -26.156 -8.969  8.364   1.00 41.50  ? 89  ALA A O   1 
ATOM   613  C  CB  . ALA A 1 113 ? -26.591 -12.063 8.535   1.00 39.63  ? 89  ALA A CB  1 
ATOM   614  N  N   . PRO A 1 114 ? -24.525 -9.845  7.095   1.00 42.68  ? 90  PRO A N   1 
ATOM   615  C  CA  . PRO A 1 114 ? -24.344 -8.579  6.360   1.00 39.44  ? 90  PRO A CA  1 
ATOM   616  C  C   . PRO A 1 114 ? -25.581 -8.105  5.610   1.00 40.37  ? 90  PRO A C   1 
ATOM   617  O  O   . PRO A 1 114 ? -25.553 -6.997  5.057   1.00 40.17  ? 90  PRO A O   1 
ATOM   618  C  CB  . PRO A 1 114 ? -23.191 -8.891  5.392   1.00 41.61  ? 90  PRO A CB  1 
ATOM   619  C  CG  . PRO A 1 114 ? -23.180 -10.377 5.262   1.00 41.67  ? 90  PRO A CG  1 
ATOM   620  C  CD  . PRO A 1 114 ? -23.655 -10.917 6.579   1.00 41.21  ? 90  PRO A CD  1 
ATOM   621  N  N   . THR A 1 115 ? -26.653 -8.894  5.570   1.00 42.23  ? 91  THR A N   1 
ATOM   622  C  CA  . THR A 1 115 ? -27.907 -8.485  4.951   1.00 42.04  ? 91  THR A CA  1 
ATOM   623  C  C   . THR A 1 115 ? -28.828 -7.740  5.911   1.00 42.51  ? 91  THR A C   1 
ATOM   624  O  O   . THR A 1 115 ? -29.876 -7.246  5.482   1.00 43.30  ? 91  THR A O   1 
ATOM   625  C  CB  . THR A 1 115 ? -28.642 -9.711  4.396   1.00 43.47  ? 91  THR A CB  1 
ATOM   626  O  OG1 . THR A 1 115 ? -28.724 -10.720 5.411   1.00 43.31  ? 91  THR A OG1 1 
ATOM   627  C  CG2 . THR A 1 115 ? -27.917 -10.273 3.178   1.00 41.10  ? 91  THR A CG2 1 
ATOM   628  N  N   . MET A 1 116 ? -28.463 -7.635  7.185   1.00 44.12  ? 92  MET A N   1 
ATOM   629  C  CA  . MET A 1 116 ? -29.361 -7.097  8.195   1.00 42.46  ? 92  MET A CA  1 
ATOM   630  C  C   . MET A 1 116 ? -29.291 -5.571  8.251   1.00 45.37  ? 92  MET A C   1 
ATOM   631  O  O   . MET A 1 116 ? -28.305 -4.946  7.849   1.00 43.07  ? 92  MET A O   1 
ATOM   632  C  CB  . MET A 1 116 ? -29.020 -7.674  9.567   1.00 44.43  ? 92  MET A CB  1 
ATOM   633  C  CG  . MET A 1 116 ? -29.217 -9.177  9.682   1.00 44.55  ? 92  MET A CG  1 
ATOM   634  S  SD  . MET A 1 116 ? -28.801 -9.799  11.327  1.00 47.22  ? 92  MET A SD  1 
ATOM   635  C  CE  . MET A 1 116 ? -29.419 -11.476 11.224  1.00 42.08  ? 92  MET A CE  1 
ATOM   636  N  N   . SER A 1 117 ? -30.361 -4.976  8.778   1.00 44.98  ? 93  SER A N   1 
ATOM   637  C  CA  . SER A 1 117 ? -30.439 -3.537  8.976   1.00 45.29  ? 93  SER A CA  1 
ATOM   638  C  C   . SER A 1 117 ? -29.707 -3.128  10.254  1.00 45.61  ? 93  SER A C   1 
ATOM   639  O  O   . SER A 1 117 ? -29.340 -3.958  11.089  1.00 45.43  ? 93  SER A O   1 
ATOM   640  C  CB  . SER A 1 117 ? -31.897 -3.085  9.053   1.00 44.71  ? 93  SER A CB  1 
ATOM   641  O  OG  . SER A 1 117 ? -32.529 -3.623  10.203  1.00 47.66  ? 93  SER A OG  1 
ATOM   642  N  N   . ILE A 1 118 ? -29.509 -1.816  10.406  1.00 47.15  ? 94  ILE A N   1 
ATOM   643  C  CA  . ILE A 1 118 ? -28.865 -1.299  11.611  1.00 47.02  ? 94  ILE A CA  1 
ATOM   644  C  C   . ILE A 1 118 ? -29.789 -1.443  12.813  1.00 47.19  ? 94  ILE A C   1 
ATOM   645  O  O   . ILE A 1 118 ? -29.348 -1.801  13.912  1.00 45.29  ? 94  ILE A O   1 
ATOM   646  C  CB  . ILE A 1 118 ? -28.441 0.167   11.401  1.00 45.57  ? 94  ILE A CB  1 
ATOM   647  C  CG1 . ILE A 1 118 ? -27.281 0.260   10.403  1.00 41.96  ? 94  ILE A CG1 1 
ATOM   648  C  CG2 . ILE A 1 118 ? -28.073 0.816   12.732  1.00 41.11  ? 94  ILE A CG2 1 
ATOM   649  C  CD1 . ILE A 1 118 ? -26.007 -0.441  10.844  1.00 38.29  ? 94  ILE A CD1 1 
ATOM   650  N  N   . ALA A 1 119 ? -31.082 -1.161  12.630  1.00 44.44  ? 95  ALA A N   1 
ATOM   651  C  CA  . ALA A 1 119 ? -32.025 -1.265  13.740  1.00 50.56  ? 95  ALA A CA  1 
ATOM   652  C  C   . ALA A 1 119 ? -32.025 -2.669  14.331  1.00 51.01  ? 95  ALA A C   1 
ATOM   653  O  O   . ALA A 1 119 ? -32.089 -2.838  15.554  1.00 51.90  ? 95  ALA A O   1 
ATOM   654  C  CB  . ALA A 1 119 ? -33.428 -0.880  13.272  1.00 47.44  ? 95  ALA A CB  1 
ATOM   655  N  N   . GLU A 1 120 ? -31.955 -3.690  13.476  1.00 52.18  ? 96  GLU A N   1 
ATOM   656  C  CA  . GLU A 1 120 ? -31.872 -5.063  13.964  1.00 52.69  ? 96  GLU A CA  1 
ATOM   657  C  C   . GLU A 1 120 ? -30.522 -5.332  14.618  1.00 50.92  ? 96  GLU A C   1 
ATOM   658  O  O   . GLU A 1 120 ? -30.454 -5.850  15.739  1.00 48.79  ? 96  GLU A O   1 
ATOM   659  C  CB  . GLU A 1 120 ? -32.109 -6.038  12.810  1.00 49.62  ? 96  GLU A CB  1 
ATOM   660  C  CG  . GLU A 1 120 ? -31.866 -7.496  13.165  1.00 50.93  ? 96  GLU A CG  1 
ATOM   661  C  CD  . GLU A 1 120 ? -32.263 -8.441  12.049  1.00 57.34  ? 96  GLU A CD  1 
ATOM   662  O  OE1 . GLU A 1 120 ? -32.430 -7.971  10.903  1.00 57.16  ? 96  GLU A OE1 1 
ATOM   663  O  OE2 . GLU A 1 120 ? -32.411 -9.652  12.317  1.00 61.12  ? 96  GLU A OE2 1 
ATOM   664  N  N   . ARG A 1 121 ? -29.434 -4.974  13.930  1.00 44.83  ? 97  ARG A N   1 
ATOM   665  C  CA  . ARG A 1 121 ? -28.103 -5.385  14.360  1.00 45.06  ? 97  ARG A CA  1 
ATOM   666  C  C   . ARG A 1 121 ? -27.693 -4.751  15.683  1.00 42.92  ? 97  ARG A C   1 
ATOM   667  O  O   . ARG A 1 121 ? -26.866 -5.318  16.408  1.00 41.12  ? 97  ARG A O   1 
ATOM   668  C  CB  . ARG A 1 121 ? -27.086 -5.032  13.274  1.00 42.78  ? 97  ARG A CB  1 
ATOM   669  C  CG  . ARG A 1 121 ? -27.028 -6.018  12.117  1.00 40.03  ? 97  ARG A CG  1 
ATOM   670  C  CD  . ARG A 1 121 ? -26.506 -5.354  10.854  1.00 40.60  ? 97  ARG A CD  1 
ATOM   671  N  NE  . ARG A 1 121 ? -25.281 -4.599  11.093  1.00 41.44  ? 97  ARG A NE  1 
ATOM   672  C  CZ  . ARG A 1 121 ? -24.790 -3.689  10.263  1.00 38.19  ? 97  ARG A CZ  1 
ATOM   673  N  NH1 . ARG A 1 121 ? -25.393 -3.394  9.122   1.00 37.79  ? 97  ARG A NH1 1 
ATOM   674  N  NH2 . ARG A 1 121 ? -23.670 -3.051  10.590  1.00 33.88  ? 97  ARG A NH2 1 
ATOM   675  N  N   . ILE A 1 122 ? -28.252 -3.585  16.019  1.00 39.64  ? 98  ILE A N   1 
ATOM   676  C  CA  . ILE A 1 122 ? -27.777 -2.824  17.173  1.00 41.59  ? 98  ILE A CA  1 
ATOM   677  C  C   . ILE A 1 122 ? -28.366 -3.284  18.498  1.00 43.78  ? 98  ILE A C   1 
ATOM   678  O  O   . ILE A 1 122 ? -27.836 -2.924  19.557  1.00 42.24  ? 98  ILE A O   1 
ATOM   679  C  CB  . ILE A 1 122 ? -28.090 -1.330  16.961  1.00 44.63  ? 98  ILE A CB  1 
ATOM   680  C  CG1 . ILE A 1 122 ? -27.331 -0.466  17.970  1.00 44.46  ? 98  ILE A CG1 1 
ATOM   681  C  CG2 . ILE A 1 122 ? -29.589 -1.074  17.072  1.00 46.51  ? 98  ILE A CG2 1 
ATOM   682  C  CD1 . ILE A 1 122 ? -27.512 1.019   17.745  1.00 48.93  ? 98  ILE A CD1 1 
ATOM   683  N  N   . GLN A 1 123 ? -29.432 -4.089  18.478  1.00 43.26  ? 99  GLN A N   1 
ATOM   684  C  CA  . GLN A 1 123 ? -30.197 -4.310  19.705  1.00 45.52  ? 99  GLN A CA  1 
ATOM   685  C  C   . GLN A 1 123 ? -29.426 -5.112  20.745  1.00 41.05  ? 99  GLN A C   1 
ATOM   686  O  O   . GLN A 1 123 ? -29.436 -4.720  21.926  1.00 41.68  ? 99  GLN A O   1 
ATOM   687  C  CB  . GLN A 1 123 ? -31.537 -4.967  19.364  1.00 43.75  ? 99  GLN A CB  1 
ATOM   688  C  CG  . GLN A 1 123 ? -32.488 -4.042  18.628  1.00 50.22  ? 99  GLN A CG  1 
ATOM   689  C  CD  . GLN A 1 123 ? -33.816 -4.701  18.316  1.00 56.41  ? 99  GLN A CD  1 
ATOM   690  O  OE1 . GLN A 1 123 ? -34.355 -5.455  19.126  1.00 57.90  ? 99  GLN A OE1 1 
ATOM   691  N  NE2 . GLN A 1 123 ? -34.348 -4.424  17.131  1.00 58.90  ? 99  GLN A NE2 1 
ATOM   692  N  N   . PRO A 1 124 ? -28.769 -6.228  20.410  1.00 40.99  ? 100 PRO A N   1 
ATOM   693  C  CA  . PRO A 1 124 ? -28.026 -6.965  21.450  1.00 41.63  ? 100 PRO A CA  1 
ATOM   694  C  C   . PRO A 1 124 ? -27.037 -6.104  22.223  1.00 41.30  ? 100 PRO A C   1 
ATOM   695  O  O   . PRO A 1 124 ? -27.089 -6.058  23.459  1.00 40.70  ? 100 PRO A O   1 
ATOM   696  C  CB  . PRO A 1 124 ? -27.329 -8.071  20.647  1.00 42.97  ? 100 PRO A CB  1 
ATOM   697  C  CG  . PRO A 1 124 ? -28.233 -8.310  19.490  1.00 42.00  ? 100 PRO A CG  1 
ATOM   698  C  CD  . PRO A 1 124 ? -28.816 -6.968  19.137  1.00 40.06  ? 100 PRO A CD  1 
ATOM   699  N  N   . ALA A 1 125 ? -26.133 -5.413  21.526  1.00 39.53  ? 101 ALA A N   1 
ATOM   700  C  CA  . ALA A 1 125 ? -25.149 -4.587  22.219  1.00 39.83  ? 101 ALA A CA  1 
ATOM   701  C  C   . ALA A 1 125 ? -25.819 -3.465  23.004  1.00 39.80  ? 101 ALA A C   1 
ATOM   702  O  O   . ALA A 1 125 ? -25.373 -3.113  24.102  1.00 38.43  ? 101 ALA A O   1 
ATOM   703  C  CB  . ALA A 1 125 ? -24.144 -4.017  21.218  1.00 38.89  ? 101 ALA A CB  1 
ATOM   704  N  N   . GLN A 1 126 ? -26.893 -2.890  22.460  1.00 38.71  ? 102 GLN A N   1 
ATOM   705  C  CA  . GLN A 1 126 ? -27.569 -1.802  23.159  1.00 42.97  ? 102 GLN A CA  1 
ATOM   706  C  C   . GLN A 1 126 ? -28.158 -2.278  24.481  1.00 43.26  ? 102 GLN A C   1 
ATOM   707  O  O   . GLN A 1 126 ? -28.139 -1.547  25.478  1.00 43.70  ? 102 GLN A O   1 
ATOM   708  C  CB  . GLN A 1 126 ? -28.663 -1.205  22.274  1.00 45.03  ? 102 GLN A CB  1 
ATOM   709  C  CG  . GLN A 1 126 ? -29.303 0.042   22.860  1.00 43.46  ? 102 GLN A CG  1 
ATOM   710  C  CD  . GLN A 1 126 ? -30.247 0.724   21.894  1.00 48.17  ? 102 GLN A CD  1 
ATOM   711  O  OE1 . GLN A 1 126 ? -30.414 0.286   20.756  1.00 51.09  ? 102 GLN A OE1 1 
ATOM   712  N  NE2 . GLN A 1 126 ? -30.871 1.806   22.343  1.00 46.22  ? 102 GLN A NE2 1 
ATOM   713  N  N   . HIS A 1 127 ? -28.681 -3.505  24.510  1.00 42.60  ? 103 HIS A N   1 
ATOM   714  C  CA  . HIS A 1 127 ? -29.320 -4.015  25.717  1.00 42.54  ? 103 HIS A CA  1 
ATOM   715  C  C   . HIS A 1 127 ? -28.295 -4.495  26.738  1.00 43.25  ? 103 HIS A C   1 
ATOM   716  O  O   . HIS A 1 127 ? -28.372 -4.141  27.920  1.00 42.47  ? 103 HIS A O   1 
ATOM   717  C  CB  . HIS A 1 127 ? -30.277 -5.154  25.362  1.00 43.00  ? 103 HIS A CB  1 
ATOM   718  C  CG  . HIS A 1 127 ? -30.933 -5.779  26.553  1.00 47.16  ? 103 HIS A CG  1 
ATOM   719  N  ND1 . HIS A 1 127 ? -31.853 -5.110  27.331  1.00 51.56  ? 103 HIS A ND1 1 
ATOM   720  C  CD2 . HIS A 1 127 ? -30.792 -7.006  27.108  1.00 46.24  ? 103 HIS A CD2 1 
ATOM   721  C  CE1 . HIS A 1 127 ? -32.256 -5.900  28.310  1.00 54.09  ? 103 HIS A CE1 1 
ATOM   722  N  NE2 . HIS A 1 127 ? -31.627 -7.056  28.198  1.00 50.18  ? 103 HIS A NE2 1 
ATOM   723  N  N   . TYR A 1 128 ? -27.329 -5.303  26.300  1.00 42.42  ? 104 TYR A N   1 
ATOM   724  C  CA  . TYR A 1 128 ? -26.412 -5.962  27.220  1.00 41.29  ? 104 TYR A CA  1 
ATOM   725  C  C   . TYR A 1 128 ? -25.254 -5.077  27.661  1.00 40.39  ? 104 TYR A C   1 
ATOM   726  O  O   . TYR A 1 128 ? -24.571 -5.424  28.630  1.00 39.78  ? 104 TYR A O   1 
ATOM   727  C  CB  . TYR A 1 128 ? -25.868 -7.241  26.579  1.00 39.86  ? 104 TYR A CB  1 
ATOM   728  C  CG  . TYR A 1 128 ? -26.922 -8.311  26.405  1.00 43.98  ? 104 TYR A CG  1 
ATOM   729  C  CD1 . TYR A 1 128 ? -27.438 -8.984  27.503  1.00 42.90  ? 104 TYR A CD1 1 
ATOM   730  C  CD2 . TYR A 1 128 ? -27.403 -8.645  25.146  1.00 42.80  ? 104 TYR A CD2 1 
ATOM   731  C  CE1 . TYR A 1 128 ? -28.401 -9.961  27.355  1.00 42.96  ? 104 TYR A CE1 1 
ATOM   732  C  CE2 . TYR A 1 128 ? -28.366 -9.623  24.987  1.00 39.97  ? 104 TYR A CE2 1 
ATOM   733  C  CZ  . TYR A 1 128 ? -28.861 -10.279 26.096  1.00 45.11  ? 104 TYR A CZ  1 
ATOM   734  O  OH  . TYR A 1 128 ? -29.822 -11.254 25.951  1.00 44.71  ? 104 TYR A OH  1 
ATOM   735  N  N   . ARG A 1 129 ? -25.016 -3.955  26.989  1.00 40.24  ? 105 ARG A N   1 
ATOM   736  C  CA  . ARG A 1 129 ? -23.969 -3.014  27.367  1.00 39.83  ? 105 ARG A CA  1 
ATOM   737  C  C   . ARG A 1 129 ? -22.623 -3.722  27.557  1.00 38.54  ? 105 ARG A C   1 
ATOM   738  O  O   . ARG A 1 129 ? -22.023 -3.648  28.631  1.00 37.70  ? 105 ARG A O   1 
ATOM   739  C  CB  . ARG A 1 129 ? -24.359 -2.258  28.630  1.00 42.12  ? 105 ARG A CB  1 
ATOM   740  C  CG  . ARG A 1 129 ? -25.539 -1.315  28.445  1.00 45.69  ? 105 ARG A CG  1 
ATOM   741  C  CD  . ARG A 1 129 ? -25.781 -0.458  29.683  1.00 49.57  ? 105 ARG A CD  1 
ATOM   742  N  NE  . ARG A 1 129 ? -26.384 -1.208  30.779  1.00 53.62  ? 105 ARG A NE  1 
ATOM   743  C  CZ  . ARG A 1 129 ? -27.681 -1.470  30.886  1.00 59.96  ? 105 ARG A CZ  1 
ATOM   744  N  NH1 . ARG A 1 129 ? -28.543 -1.094  29.953  1.00 55.69  ? 105 ARG A NH1 1 
ATOM   745  N  NH2 . ARG A 1 129 ? -28.125 -2.125  31.955  1.00 54.09  ? 105 ARG A NH2 1 
ATOM   746  N  N   . PRO A 1 130 ? -22.128 -4.412  26.532  1.00 39.92  ? 106 PRO A N   1 
ATOM   747  C  CA  . PRO A 1 130 ? -20.855 -5.125  26.672  1.00 36.04  ? 106 PRO A CA  1 
ATOM   748  C  C   . PRO A 1 130 ? -19.681 -4.169  26.812  1.00 38.62  ? 106 PRO A C   1 
ATOM   749  O  O   . PRO A 1 130 ? -19.775 -2.972  26.531  1.00 35.81  ? 106 PRO A O   1 
ATOM   750  C  CB  . PRO A 1 130 ? -20.758 -5.932  25.373  1.00 33.81  ? 106 PRO A CB  1 
ATOM   751  C  CG  . PRO A 1 130 ? -21.571 -5.156  24.393  1.00 36.20  ? 106 PRO A CG  1 
ATOM   752  C  CD  . PRO A 1 130 ? -22.712 -4.587  25.191  1.00 37.53  ? 106 PRO A CD  1 
ATOM   753  N  N   . GLU A 1 131 ? -18.554 -4.725  27.268  1.00 35.97  ? 107 GLU A N   1 
ATOM   754  C  CA  . GLU A 1 131 ? -17.309 -3.966  27.270  1.00 37.68  ? 107 GLU A CA  1 
ATOM   755  C  C   . GLU A 1 131 ? -16.880 -3.618  25.853  1.00 34.82  ? 107 GLU A C   1 
ATOM   756  O  O   . GLU A 1 131 ? -16.323 -2.541  25.613  1.00 35.66  ? 107 GLU A O   1 
ATOM   757  C  CB  . GLU A 1 131 ? -16.193 -4.758  27.954  1.00 37.16  ? 107 GLU A CB  1 
ATOM   758  C  CG  . GLU A 1 131 ? -16.455 -5.136  29.399  1.00 37.08  ? 107 GLU A CG  1 
ATOM   759  C  CD  . GLU A 1 131 ? -15.285 -5.880  30.016  1.00 40.61  ? 107 GLU A CD  1 
ATOM   760  O  OE1 . GLU A 1 131 ? -14.306 -5.220  30.429  1.00 40.55  ? 107 GLU A OE1 1 
ATOM   761  O  OE2 . GLU A 1 131 ? -15.336 -7.127  30.074  1.00 40.28  ? 107 GLU A OE2 1 
ATOM   762  N  N   . LEU A 1 132 ? -17.134 -4.520  24.906  1.00 33.58  ? 108 LEU A N   1 
ATOM   763  C  CA  . LEU A 1 132 ? -16.672 -4.394  23.534  1.00 32.08  ? 108 LEU A CA  1 
ATOM   764  C  C   . LEU A 1 132 ? -17.801 -4.753  22.582  1.00 35.66  ? 108 LEU A C   1 
ATOM   765  O  O   . LEU A 1 132 ? -18.584 -5.669  22.851  1.00 34.02  ? 108 LEU A O   1 
ATOM   766  C  CB  . LEU A 1 132 ? -15.476 -5.317  23.260  1.00 34.92  ? 108 LEU A CB  1 
ATOM   767  C  CG  . LEU A 1 132 ? -14.069 -4.731  23.159  1.00 35.73  ? 108 LEU A CG  1 
ATOM   768  C  CD1 . LEU A 1 132 ? -13.105 -5.855  22.824  1.00 34.81  ? 108 LEU A CD1 1 
ATOM   769  C  CD2 . LEU A 1 132 ? -13.983 -3.626  22.117  1.00 33.98  ? 108 LEU A CD2 1 
ATOM   770  N  N   . ALA A 1 133 ? -17.877 -4.030  21.469  1.00 33.77  ? 109 ALA A N   1 
ATOM   771  C  CA  . ALA A 1 133 ? -18.757 -4.391  20.369  1.00 34.80  ? 109 ALA A CA  1 
ATOM   772  C  C   . ALA A 1 133 ? -18.058 -4.067  19.059  1.00 34.34  ? 109 ALA A C   1 
ATOM   773  O  O   . ALA A 1 133 ? -17.337 -3.070  18.964  1.00 30.66  ? 109 ALA A O   1 
ATOM   774  C  CB  . ALA A 1 133 ? -20.101 -3.654  20.446  1.00 33.40  ? 109 ALA A CB  1 
ATOM   775  N  N   . SER A 1 134 ? -18.258 -4.918  18.058  1.00 35.49  ? 110 SER A N   1 
ATOM   776  C  CA  . SER A 1 134 ? -17.739 -4.622  16.733  1.00 29.55  ? 110 SER A CA  1 
ATOM   777  C  C   . SER A 1 134 ? -18.490 -3.439  16.133  1.00 32.99  ? 110 SER A C   1 
ATOM   778  O  O   . SER A 1 134 ? -19.683 -3.235  16.384  1.00 34.80  ? 110 SER A O   1 
ATOM   779  C  CB  . SER A 1 134 ? -17.858 -5.845  15.822  1.00 32.34  ? 110 SER A CB  1 
ATOM   780  O  OG  . SER A 1 134 ? -19.213 -6.159  15.545  1.00 33.82  ? 110 SER A OG  1 
ATOM   781  N  N   . LEU A 1 135 ? -17.768 -2.640  15.350  1.00 31.99  ? 111 LEU A N   1 
ATOM   782  C  CA  . LEU A 1 135 ? -18.345 -1.501  14.640  1.00 30.83  ? 111 LEU A CA  1 
ATOM   783  C  C   . LEU A 1 135 ? -17.756 -1.495  13.238  1.00 29.96  ? 111 LEU A C   1 
ATOM   784  O  O   . LEU A 1 135 ? -16.572 -1.190  13.060  1.00 30.98  ? 111 LEU A O   1 
ATOM   785  C  CB  . LEU A 1 135 ? -18.057 -0.184  15.360  1.00 32.63  ? 111 LEU A CB  1 
ATOM   786  C  CG  . LEU A 1 135 ? -18.699 1.066   14.750  1.00 34.78  ? 111 LEU A CG  1 
ATOM   787  C  CD1 . LEU A 1 135 ? -20.212 1.028   14.903  1.00 33.89  ? 111 LEU A CD1 1 
ATOM   788  C  CD2 . LEU A 1 135 ? -18.127 2.329   15.385  1.00 35.25  ? 111 LEU A CD2 1 
ATOM   789  N  N   . ASN A 1 136 ? -18.571 -1.846  12.253  1.00 30.61  ? 112 ASN A N   1 
ATOM   790  C  CA  . ASN A 1 136 ? -18.108 -1.900  10.875  1.00 31.39  ? 112 ASN A CA  1 
ATOM   791  C  C   . ASN A 1 136 ? -18.126 -0.501  10.275  1.00 30.74  ? 112 ASN A C   1 
ATOM   792  O  O   . ASN A 1 136 ? -19.100 0.240   10.434  1.00 30.29  ? 112 ASN A O   1 
ATOM   793  C  CB  . ASN A 1 136 ? -18.974 -2.868  10.078  1.00 28.36  ? 112 ASN A CB  1 
ATOM   794  C  CG  . ASN A 1 136 ? -18.965 -4.267  10.674  1.00 33.72  ? 112 ASN A CG  1 
ATOM   795  O  OD1 . ASN A 1 136 ? -18.063 -5.063  10.406  1.00 31.53  ? 112 ASN A OD1 1 
ATOM   796  N  ND2 . ASN A 1 136 ? -19.961 -4.566  11.505  1.00 31.80  ? 112 ASN A ND2 1 
ATOM   797  N  N   . MET A 1 137 ? -17.043 -0.142  9.587   1.00 30.24  ? 113 MET A N   1 
ATOM   798  C  CA  . MET A 1 137 ? -16.714 1.254   9.330   1.00 29.34  ? 113 MET A CA  1 
ATOM   799  C  C   . MET A 1 137 ? -17.066 1.725   7.925   1.00 31.44  ? 113 MET A C   1 
ATOM   800  O  O   . MET A 1 137 ? -16.767 2.871   7.578   1.00 31.19  ? 113 MET A O   1 
ATOM   801  C  CB  . MET A 1 137 ? -15.224 1.484   9.598   1.00 30.46  ? 113 MET A CB  1 
ATOM   802  C  CG  . MET A 1 137 ? -14.857 1.501   11.081  1.00 28.78  ? 113 MET A CG  1 
ATOM   803  S  SD  . MET A 1 137 ? -15.880 2.635   12.050  1.00 36.91  ? 113 MET A SD  1 
ATOM   804  C  CE  . MET A 1 137 ? -15.652 4.153   11.130  1.00 29.27  ? 113 MET A CE  1 
ATOM   805  N  N   . GLY A 1 138 ? -17.710 0.896   7.115   1.00 30.52  ? 114 GLY A N   1 
ATOM   806  C  CA  . GLY A 1 138 ? -18.083 1.348   5.791   1.00 28.93  ? 114 GLY A CA  1 
ATOM   807  C  C   . GLY A 1 138 ? -19.047 0.431   5.074   1.00 32.46  ? 114 GLY A C   1 
ATOM   808  O  O   . GLY A 1 138 ? -19.088 -0.773  5.343   1.00 32.88  ? 114 GLY A O   1 
ATOM   809  N  N   . THR A 1 139 ? -19.837 0.994   4.163   1.00 27.87  ? 115 THR A N   1 
ATOM   810  C  CA  . THR A 1 139 ? -20.728 0.192   3.341   1.00 30.63  ? 115 THR A CA  1 
ATOM   811  C  C   . THR A 1 139 ? -19.930 -0.501  2.245   1.00 31.49  ? 115 THR A C   1 
ATOM   812  O  O   . THR A 1 139 ? -19.047 0.098   1.626   1.00 30.41  ? 115 THR A O   1 
ATOM   813  C  CB  . THR A 1 139 ? -21.823 1.063   2.723   1.00 32.05  ? 115 THR A CB  1 
ATOM   814  O  OG1 . THR A 1 139 ? -22.591 1.682   3.764   1.00 32.71  ? 115 THR A OG1 1 
ATOM   815  C  CG2 . THR A 1 139 ? -22.745 0.225   1.844   1.00 32.31  ? 115 THR A CG2 1 
ATOM   816  N  N   . MET A 1 140 ? -20.252 -1.767  1.997   1.00 32.99  ? 116 MET A N   1 
ATOM   817  C  CA  . MET A 1 140 ? -19.454 -2.565  1.079   1.00 31.37  ? 116 MET A CA  1 
ATOM   818  C  C   . MET A 1 140 ? -20.299 -3.684  0.496   1.00 31.82  ? 116 MET A C   1 
ATOM   819  O  O   . MET A 1 140 ? -21.267 -4.139  1.111   1.00 31.98  ? 116 MET A O   1 
ATOM   820  C  CB  . MET A 1 140 ? -18.230 -3.156  1.788   1.00 32.87  ? 116 MET A CB  1 
ATOM   821  C  CG  . MET A 1 140 ? -18.565 -3.951  3.046   1.00 30.01  ? 116 MET A CG  1 
ATOM   822  S  SD  . MET A 1 140 ? -17.098 -4.554  3.916   1.00 36.45  ? 116 MET A SD  1 
ATOM   823  C  CE  . MET A 1 140 ? -16.658 -5.973  2.916   1.00 31.40  ? 116 MET A CE  1 
ATOM   824  N  N   . ASN A 1 141 ? -19.920 -4.114  -0.705  1.00 30.80  ? 117 ASN A N   1 
ATOM   825  C  CA  . ASN A 1 141 ? -20.374 -5.400  -1.204  1.00 32.93  ? 117 ASN A CA  1 
ATOM   826  C  C   . ASN A 1 141 ? -19.852 -6.511  -0.301  1.00 33.88  ? 117 ASN A C   1 
ATOM   827  O  O   . ASN A 1 141 ? -18.755 -6.425  0.257   1.00 32.16  ? 117 ASN A O   1 
ATOM   828  C  CB  . ASN A 1 141 ? -19.884 -5.635  -2.634  1.00 32.84  ? 117 ASN A CB  1 
ATOM   829  C  CG  . ASN A 1 141 ? -20.514 -4.694  -3.636  1.00 31.99  ? 117 ASN A CG  1 
ATOM   830  O  OD1 . ASN A 1 141 ? -21.526 -4.055  -3.357  1.00 32.90  ? 117 ASN A OD1 1 
ATOM   831  N  ND2 . ASN A 1 141 ? -19.925 -4.619  -4.825  1.00 33.47  ? 117 ASN A ND2 1 
ATOM   832  N  N   . PHE A 1 142 ? -20.655 -7.559  -0.152  1.00 33.24  ? 118 PHE A N   1 
ATOM   833  C  CA  . PHE A 1 142 ? -20.258 -8.776  0.593   1.00 35.49  ? 118 PHE A CA  1 
ATOM   834  C  C   . PHE A 1 142 ? -20.572 -9.946  -0.337  1.00 35.92  ? 118 PHE A C   1 
ATOM   835  O  O   . PHE A 1 142 ? -21.744 -10.295 -0.513  1.00 36.44  ? 118 PHE A O   1 
ATOM   836  C  CB  . PHE A 1 142 ? -20.939 -8.871  1.961   1.00 35.53  ? 118 PHE A CB  1 
ATOM   837  C  CG  . PHE A 1 142 ? -20.127 -9.567  3.022   1.00 39.22  ? 118 PHE A CG  1 
ATOM   838  C  CD1 . PHE A 1 142 ? -19.739 -10.887 2.870   1.00 42.57  ? 118 PHE A CD1 1 
ATOM   839  C  CD2 . PHE A 1 142 ? -19.741 -8.895  4.170   1.00 39.28  ? 118 PHE A CD2 1 
ATOM   840  C  CE1 . PHE A 1 142 ? -18.988 -11.521 3.847   1.00 41.62  ? 118 PHE A CE1 1 
ATOM   841  C  CE2 . PHE A 1 142 ? -18.988 -9.529  5.143   1.00 40.24  ? 118 PHE A CE2 1 
ATOM   842  C  CZ  . PHE A 1 142 ? -18.615 -10.841 4.981   1.00 40.67  ? 118 PHE A CZ  1 
ATOM   843  N  N   . GLY A 1 143 ? -19.537 -10.544 -0.922  1.00 38.30  ? 119 GLY A N   1 
ATOM   844  C  CA  . GLY A 1 143 ? -19.704 -11.643 -1.855  1.00 42.42  ? 119 GLY A CA  1 
ATOM   845  C  C   . GLY A 1 143 ? -19.462 -12.977 -1.175  1.00 43.68  ? 119 GLY A C   1 
ATOM   846  O  O   . GLY A 1 143 ? -18.429 -13.185 -0.536  1.00 41.08  ? 119 GLY A O   1 
ATOM   847  N  N   . LEU A 1 144 ? -20.431 -13.876 -1.323  1.00 49.72  ? 120 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 144 ? -20.318 -15.209 -0.674  1.00 52.28  ? 120 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 144 ? -20.317 -16.323 -1.722  1.00 56.12  ? 120 LEU A C   1 
ATOM   850  O  O   . LEU A 1 144 ? -20.088 -17.472 -1.349  1.00 56.26  ? 120 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 144 ? -21.497 -15.359 0.291   1.00 47.90  ? 120 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 144 ? -21.599 -14.291 1.376   1.00 46.48  ? 120 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 144 ? -22.811 -14.531 2.259   1.00 47.15  ? 120 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 144 ? -20.333 -14.257 2.213   1.00 47.61  ? 120 LEU A CD2 1 
ATOM   855  N  N   . PHE A 1 145 ? -20.538 -15.991 -2.988  1.00 73.16  ? 121 PHE A N   1 
ATOM   856  C  CA  . PHE A 1 145 ? -20.676 -17.039 -4.036  1.00 76.11  ? 121 PHE A CA  1 
ATOM   857  C  C   . PHE A 1 145 ? -19.360 -17.796 -4.250  1.00 75.73  ? 121 PHE A C   1 
ATOM   858  O  O   . PHE A 1 145 ? -19.415 -18.929 -4.729  1.00 79.47  ? 121 PHE A O   1 
ATOM   859  C  CB  . PHE A 1 145 ? -21.324 -16.472 -5.302  1.00 76.13  ? 121 PHE A CB  1 
ATOM   860  C  CG  . PHE A 1 145 ? -20.857 -15.097 -5.680  1.00 81.43  ? 121 PHE A CG  1 
ATOM   861  C  CD1 . PHE A 1 145 ? -21.283 -13.987 -4.972  1.00 75.27  ? 121 PHE A CD1 1 
ATOM   862  C  CD2 . PHE A 1 145 ? -19.961 -14.930 -6.720  1.00 82.58  ? 121 PHE A CD2 1 
ATOM   863  C  CE1 . PHE A 1 145 ? -20.838 -12.725 -5.316  1.00 73.32  ? 121 PHE A CE1 1 
ATOM   864  C  CE2 . PHE A 1 145 ? -19.515 -13.668 -7.061  1.00 78.99  ? 121 PHE A CE2 1 
ATOM   865  C  CZ  . PHE A 1 145 ? -19.952 -12.579 -6.352  1.00 74.45  ? 121 PHE A CZ  1 
ATOM   866  N  N   . PRO A 1 146 ? -18.175 -17.241 -3.956  1.00 66.36  ? 122 PRO A N   1 
ATOM   867  C  CA  . PRO A 1 146 ? -16.954 -18.033 -3.980  1.00 67.02  ? 122 PRO A CA  1 
ATOM   868  C  C   . PRO A 1 146 ? -17.122 -19.303 -3.132  1.00 64.66  ? 122 PRO A C   1 
ATOM   869  O  O   . PRO A 1 146 ? -16.489 -20.279 -3.415  1.00 64.28  ? 122 PRO A O   1 
ATOM   870  C  CB  . PRO A 1 146 ? -15.973 -17.124 -3.241  1.00 62.82  ? 122 PRO A CB  1 
ATOM   871  C  CG  . PRO A 1 146 ? -16.407 -15.734 -3.618  1.00 62.01  ? 122 PRO A CG  1 
ATOM   872  C  CD  . PRO A 1 146 ? -17.914 -15.820 -3.713  1.00 64.98  ? 122 PRO A CD  1 
ATOM   873  N  N   . MET A 1 147 ? -17.916 -19.229 -2.069  1.00 61.24  ? 123 MET A N   1 
ATOM   874  C  CA  . MET A 1 147 ? -18.169 -20.406 -1.203  1.00 57.00  ? 123 MET A CA  1 
ATOM   875  C  C   . MET A 1 147 ? -19.174 -21.344 -1.885  1.00 54.13  ? 123 MET A C   1 
ATOM   876  O  O   . MET A 1 147 ? -19.295 -22.493 -1.452  1.00 52.43  ? 123 MET A O   1 
ATOM   877  C  CB  . MET A 1 147 ? -18.717 -19.975 0.160   1.00 50.71  ? 123 MET A CB  1 
ATOM   878  C  CG  . MET A 1 147 ? -17.646 -19.788 1.215   1.00 52.00  ? 123 MET A CG  1 
ATOM   879  S  SD  . MET A 1 147 ? -18.194 -18.839 2.657   1.00 51.79  ? 123 MET A SD  1 
ATOM   880  C  CE  . MET A 1 147 ? -19.165 -17.561 1.865   1.00 50.30  ? 123 MET A CE  1 
ATOM   881  N  N   . LEU A 1 148 ? -19.886 -20.891 -2.919  1.00 57.63  ? 124 LEU A N   1 
ATOM   882  C  CA  . LEU A 1 148 ? -20.790 -21.787 -3.630  1.00 58.17  ? 124 LEU A CA  1 
ATOM   883  C  C   . LEU A 1 148 ? -20.029 -22.782 -4.494  1.00 57.80  ? 124 LEU A C   1 
ATOM   884  O  O   . LEU A 1 148 ? -20.501 -23.904 -4.708  1.00 54.78  ? 124 LEU A O   1 
ATOM   885  C  CB  . LEU A 1 148 ? -21.764 -20.984 -4.493  1.00 58.33  ? 124 LEU A CB  1 
ATOM   886  C  CG  . LEU A 1 148 ? -23.164 -20.754 -3.924  1.00 54.49  ? 124 LEU A CG  1 
ATOM   887  C  CD1 . LEU A 1 148 ? -23.933 -19.797 -4.813  1.00 55.54  ? 124 LEU A CD1 1 
ATOM   888  C  CD2 . LEU A 1 148 ? -23.923 -22.063 -3.784  1.00 51.57  ? 124 LEU A CD2 1 
ATOM   889  N  N   . ASN A 1 149 ? -18.855 -22.397 -4.997  1.00 56.78  ? 125 ASN A N   1 
ATOM   890  C  CA  . ASN A 1 149 ? -18.092 -23.303 -5.848  1.00 57.62  ? 125 ASN A CA  1 
ATOM   891  C  C   . ASN A 1 149 ? -17.731 -24.581 -5.102  1.00 53.60  ? 125 ASN A C   1 
ATOM   892  O  O   . ASN A 1 149 ? -17.816 -25.681 -5.660  1.00 57.74  ? 125 ASN A O   1 
ATOM   893  C  CB  . ASN A 1 149 ? -16.832 -22.603 -6.354  1.00 63.45  ? 125 ASN A CB  1 
ATOM   894  C  CG  . ASN A 1 149 ? -17.138 -21.320 -7.107  1.00 70.03  ? 125 ASN A CG  1 
ATOM   895  O  OD1 . ASN A 1 149 ? -17.568 -20.326 -6.519  1.00 70.30  ? 125 ASN A OD1 1 
ATOM   896  N  ND2 . ASN A 1 149 ? -16.903 -21.332 -8.414  1.00 73.14  ? 125 ASN A ND2 1 
ATOM   897  N  N   . ARG A 1 150 ? -17.330 -24.457 -3.837  1.00 54.23  ? 126 ARG A N   1 
ATOM   898  C  CA  . ARG A 1 150 ? -16.904 -25.610 -3.057  1.00 48.67  ? 126 ARG A CA  1 
ATOM   899  C  C   . ARG A 1 150 ? -18.052 -26.313 -2.346  1.00 46.88  ? 126 ARG A C   1 
ATOM   900  O  O   . ARG A 1 150 ? -17.978 -27.527 -2.130  1.00 46.54  ? 126 ARG A O   1 
ATOM   901  C  CB  . ARG A 1 150 ? -15.863 -25.183 -2.014  1.00 48.51  ? 126 ARG A CB  1 
ATOM   902  C  CG  . ARG A 1 150 ? -15.343 -26.323 -1.138  1.00 48.56  ? 126 ARG A CG  1 
ATOM   903  C  CD  . ARG A 1 150 ? -14.593 -25.802 0.076   1.00 48.12  ? 126 ARG A CD  1 
ATOM   904  N  NE  . ARG A 1 150 ? -13.299 -25.225 -0.266  1.00 48.20  ? 126 ARG A NE  1 
ATOM   905  C  CZ  . ARG A 1 150 ? -12.179 -25.921 -0.400  1.00 48.59  ? 126 ARG A CZ  1 
ATOM   906  N  NH1 . ARG A 1 150 ? -12.160 -27.237 -0.260  1.00 48.90  ? 126 ARG A NH1 1 
ATOM   907  N  NH2 . ARG A 1 150 ? -11.048 -25.281 -0.682  1.00 49.94  ? 126 ARG A NH2 1 
ATOM   908  N  N   . TYR A 1 151 ? -19.111 -25.588 -1.978  1.00 47.78  ? 127 TYR A N   1 
ATOM   909  C  CA  . TYR A 1 151 ? -20.102 -26.104 -1.045  1.00 44.95  ? 127 TYR A CA  1 
ATOM   910  C  C   . TYR A 1 151 ? -21.504 -26.273 -1.614  1.00 46.29  ? 127 TYR A C   1 
ATOM   911  O  O   . TYR A 1 151 ? -22.366 -26.813 -0.911  1.00 44.42  ? 127 TYR A O   1 
ATOM   912  C  CB  . TYR A 1 151 ? -20.196 -25.186 0.186   1.00 41.81  ? 127 TYR A CB  1 
ATOM   913  C  CG  . TYR A 1 151 ? -18.965 -25.188 1.067   1.00 43.95  ? 127 TYR A CG  1 
ATOM   914  C  CD1 . TYR A 1 151 ? -18.547 -26.349 1.704   1.00 43.15  ? 127 TYR A CD1 1 
ATOM   915  C  CD2 . TYR A 1 151 ? -18.234 -24.025 1.280   1.00 43.15  ? 127 TYR A CD2 1 
ATOM   916  C  CE1 . TYR A 1 151 ? -17.428 -26.357 2.514   1.00 41.87  ? 127 TYR A CE1 1 
ATOM   917  C  CE2 . TYR A 1 151 ? -17.114 -24.024 2.092   1.00 42.49  ? 127 TYR A CE2 1 
ATOM   918  C  CZ  . TYR A 1 151 ? -16.717 -25.194 2.708   1.00 44.92  ? 127 TYR A CZ  1 
ATOM   919  O  OH  . TYR A 1 151 ? -15.604 -25.210 3.518   1.00 43.92  ? 127 TYR A OH  1 
ATOM   920  N  N   . GLU A 1 152 ? -21.766 -25.847 -2.853  1.00 46.27  ? 128 GLU A N   1 
ATOM   921  C  CA  . GLU A 1 152 ? -23.145 -25.806 -3.338  1.00 46.72  ? 128 GLU A CA  1 
ATOM   922  C  C   . GLU A 1 152 ? -23.830 -27.164 -3.214  1.00 48.44  ? 128 GLU A C   1 
ATOM   923  O  O   . GLU A 1 152 ? -24.979 -27.248 -2.765  1.00 46.91  ? 128 GLU A O   1 
ATOM   924  C  CB  . GLU A 1 152 ? -23.189 -25.321 -4.787  1.00 50.52  ? 128 GLU A CB  1 
ATOM   925  C  CG  . GLU A 1 152 ? -24.601 -25.302 -5.369  1.00 57.86  ? 128 GLU A CG  1 
ATOM   926  C  CD  . GLU A 1 152 ? -24.711 -24.487 -6.644  1.00 60.36  ? 128 GLU A CD  1 
ATOM   927  O  OE1 . GLU A 1 152 ? -23.666 -24.062 -7.179  1.00 59.10  ? 128 GLU A OE1 1 
ATOM   928  O  OE2 . GLU A 1 152 ? -25.850 -24.270 -7.110  1.00 62.20  ? 128 GLU A OE2 1 
ATOM   929  N  N   . SER A 1 153 ? -23.144 -28.241 -3.607  1.00 49.13  ? 129 SER A N   1 
ATOM   930  C  CA  . SER A 1 153 ? -23.767 -29.561 -3.582  1.00 48.19  ? 129 SER A CA  1 
ATOM   931  C  C   . SER A 1 153 ? -23.988 -30.081 -2.165  1.00 44.34  ? 129 SER A C   1 
ATOM   932  O  O   . SER A 1 153 ? -24.779 -31.011 -1.980  1.00 49.70  ? 129 SER A O   1 
ATOM   933  C  CB  . SER A 1 153 ? -22.914 -30.559 -4.366  1.00 47.75  ? 129 SER A CB  1 
ATOM   934  O  OG  . SER A 1 153 ? -21.604 -30.643 -3.830  1.00 55.58  ? 129 SER A OG  1 
ATOM   935  N  N   . GLN A 1 154 ? -23.318 -29.506 -1.167  1.00 46.09  ? 130 GLN A N   1 
ATOM   936  C  CA  . GLN A 1 154 ? -23.423 -29.970 0.210   1.00 46.32  ? 130 GLN A CA  1 
ATOM   937  C  C   . GLN A 1 154 ? -24.518 -29.269 1.003   1.00 45.06  ? 130 GLN A C   1 
ATOM   938  O  O   . GLN A 1 154 ? -24.837 -29.716 2.111   1.00 43.40  ? 130 GLN A O   1 
ATOM   939  C  CB  . GLN A 1 154 ? -22.091 -29.764 0.945   1.00 44.99  ? 130 GLN A CB  1 
ATOM   940  C  CG  . GLN A 1 154 ? -20.864 -30.255 0.196   1.00 47.39  ? 130 GLN A CG  1 
ATOM   941  C  CD  . GLN A 1 154 ? -19.585 -30.023 0.978   1.00 48.28  ? 130 GLN A CD  1 
ATOM   942  O  OE1 . GLN A 1 154 ? -19.601 -29.936 2.207   1.00 48.04  ? 130 GLN A OE1 1 
ATOM   943  N  NE2 . GLN A 1 154 ? -18.470 -29.910 0.267   1.00 49.17  ? 130 GLN A NE2 1 
ATOM   944  N  N   . LEU A 1 155 ? -25.094 -28.193 0.476   1.00 45.07  ? 131 LEU A N   1 
ATOM   945  C  CA  . LEU A 1 155 ? -26.023 -27.383 1.253   1.00 44.11  ? 131 LEU A CA  1 
ATOM   946  C  C   . LEU A 1 155 ? -27.323 -28.140 1.495   1.00 45.19  ? 131 LEU A C   1 
ATOM   947  O  O   . LEU A 1 155 ? -27.920 -28.686 0.563   1.00 49.43  ? 131 LEU A O   1 
ATOM   948  C  CB  . LEU A 1 155 ? -26.300 -26.067 0.532   1.00 42.02  ? 131 LEU A CB  1 
ATOM   949  C  CG  . LEU A 1 155 ? -25.057 -25.233 0.219   1.00 43.78  ? 131 LEU A CG  1 
ATOM   950  C  CD1 . LEU A 1 155 ? -25.437 -23.972 -0.538  1.00 43.64  ? 131 LEU A CD1 1 
ATOM   951  C  CD2 . LEU A 1 155 ? -24.299 -24.892 1.496   1.00 37.13  ? 131 LEU A CD2 1 
ATOM   952  N  N   . LYS A 1 156 ? -27.766 -28.157 2.754   1.00 42.98  ? 132 LYS A N   1 
ATOM   953  C  CA  . LYS A 1 156 ? -28.951 -28.903 3.156   1.00 46.56  ? 132 LYS A CA  1 
ATOM   954  C  C   . LYS A 1 156 ? -30.176 -28.026 3.376   1.00 48.28  ? 132 LYS A C   1 
ATOM   955  O  O   . LYS A 1 156 ? -31.300 -28.530 3.276   1.00 49.47  ? 132 LYS A O   1 
ATOM   956  C  CB  . LYS A 1 156 ? -28.669 -29.683 4.446   1.00 45.09  ? 132 LYS A CB  1 
ATOM   957  C  CG  . LYS A 1 156 ? -27.533 -30.693 4.334   1.00 52.10  ? 132 LYS A CG  1 
ATOM   958  C  CD  . LYS A 1 156 ? -27.939 -31.903 3.508   1.00 55.19  ? 132 LYS A CD  1 
ATOM   959  C  CE  . LYS A 1 156 ? -26.837 -32.955 3.471   1.00 58.97  ? 132 LYS A CE  1 
ATOM   960  N  NZ  . LYS A 1 156 ? -25.680 -32.547 2.626   1.00 56.47  ? 132 LYS A NZ  1 
ATOM   961  N  N   . HIS A 1 157 ? -29.995 -26.742 3.677   1.00 46.66  ? 133 HIS A N   1 
ATOM   962  C  CA  . HIS A 1 157 ? -31.102 -25.838 3.951   1.00 44.85  ? 133 HIS A CA  1 
ATOM   963  C  C   . HIS A 1 157 ? -31.262 -24.843 2.810   1.00 46.32  ? 133 HIS A C   1 
ATOM   964  O  O   . HIS A 1 157 ? -30.273 -24.340 2.266   1.00 42.11  ? 133 HIS A O   1 
ATOM   965  C  CB  . HIS A 1 157 ? -30.889 -25.078 5.261   1.00 44.87  ? 133 HIS A CB  1 
ATOM   966  C  CG  . HIS A 1 157 ? -30.677 -25.963 6.448   1.00 48.53  ? 133 HIS A CG  1 
ATOM   967  N  ND1 . HIS A 1 157 ? -31.679 -26.743 6.983   1.00 53.87  ? 133 HIS A ND1 1 
ATOM   968  C  CD2 . HIS A 1 157 ? -29.580 -26.182 7.211   1.00 50.19  ? 133 HIS A CD2 1 
ATOM   969  C  CE1 . HIS A 1 157 ? -31.207 -27.411 8.020   1.00 55.91  ? 133 HIS A CE1 1 
ATOM   970  N  NE2 . HIS A 1 157 ? -29.936 -27.088 8.181   1.00 56.20  ? 133 HIS A NE2 1 
ATOM   971  N  N   . GLN A 1 158 ? -32.517 -24.551 2.466   1.00 45.83  ? 134 GLN A N   1 
ATOM   972  C  CA  . GLN A 1 158 ? -32.784 -23.600 1.393   1.00 44.42  ? 134 GLN A CA  1 
ATOM   973  C  C   . GLN A 1 158 ? -32.190 -22.232 1.709   1.00 40.77  ? 134 GLN A C   1 
ATOM   974  O  O   . GLN A 1 158 ? -31.712 -21.533 0.808   1.00 41.11  ? 134 GLN A O   1 
ATOM   975  C  CB  . GLN A 1 158 ? -34.293 -23.492 1.156   1.00 44.79  ? 134 GLN A CB  1 
ATOM   976  C  CG  . GLN A 1 158 ? -34.674 -22.628 -0.041  1.00 47.23  ? 134 GLN A CG  1 
ATOM   977  C  CD  . GLN A 1 158 ? -34.170 -23.195 -1.353  1.00 49.17  ? 134 GLN A CD  1 
ATOM   978  O  OE1 . GLN A 1 158 ? -34.194 -24.407 -1.568  1.00 51.14  ? 134 GLN A OE1 1 
ATOM   979  N  NE2 . GLN A 1 158 ? -33.702 -22.320 -2.236  1.00 48.61  ? 134 GLN A NE2 1 
ATOM   980  N  N   . TRP A 1 159 ? -32.206 -21.832 2.984   1.00 40.94  ? 135 TRP A N   1 
ATOM   981  C  CA  . TRP A 1 159 ? -31.680 -20.516 3.334   1.00 39.88  ? 135 TRP A CA  1 
ATOM   982  C  C   . TRP A 1 159 ? -30.195 -20.409 3.012   1.00 41.16  ? 135 TRP A C   1 
ATOM   983  O  O   . TRP A 1 159 ? -29.703 -19.317 2.708   1.00 38.07  ? 135 TRP A O   1 
ATOM   984  C  CB  . TRP A 1 159 ? -31.942 -20.210 4.813   1.00 36.49  ? 135 TRP A CB  1 
ATOM   985  C  CG  . TRP A 1 159 ? -31.066 -20.942 5.798   1.00 41.37  ? 135 TRP A CG  1 
ATOM   986  C  CD1 . TRP A 1 159 ? -31.368 -22.093 6.465   1.00 42.24  ? 135 TRP A CD1 1 
ATOM   987  C  CD2 . TRP A 1 159 ? -29.758 -20.555 6.242   1.00 38.53  ? 135 TRP A CD2 1 
ATOM   988  N  NE1 . TRP A 1 159 ? -30.328 -22.453 7.287   1.00 42.61  ? 135 TRP A NE1 1 
ATOM   989  C  CE2 . TRP A 1 159 ? -29.328 -21.524 7.169   1.00 41.21  ? 135 TRP A CE2 1 
ATOM   990  C  CE3 . TRP A 1 159 ? -28.910 -19.485 5.944   1.00 39.41  ? 135 TRP A CE3 1 
ATOM   991  C  CZ2 . TRP A 1 159 ? -28.086 -21.458 7.797   1.00 40.88  ? 135 TRP A CZ2 1 
ATOM   992  C  CZ3 . TRP A 1 159 ? -27.678 -19.420 6.570   1.00 37.55  ? 135 TRP A CZ3 1 
ATOM   993  C  CH2 . TRP A 1 159 ? -27.277 -20.401 7.484   1.00 38.79  ? 135 TRP A CH2 1 
ATOM   994  N  N   . GLU A 1 160 ? -29.470 -21.529 3.057   1.00 39.80  ? 136 GLU A N   1 
ATOM   995  C  CA  . GLU A 1 160 ? -28.062 -21.512 2.679   1.00 38.72  ? 136 GLU A CA  1 
ATOM   996  C  C   . GLU A 1 160 ? -27.893 -21.218 1.193   1.00 38.82  ? 136 GLU A C   1 
ATOM   997  O  O   . GLU A 1 160 ? -26.982 -20.477 0.800   1.00 37.76  ? 136 GLU A O   1 
ATOM   998  C  CB  . GLU A 1 160 ? -27.412 -22.848 3.037   1.00 40.00  ? 136 GLU A CB  1 
ATOM   999  C  CG  . GLU A 1 160 ? -27.417 -23.155 4.523   1.00 40.60  ? 136 GLU A CG  1 
ATOM   1000 C  CD  . GLU A 1 160 ? -26.808 -24.505 4.838   1.00 41.49  ? 136 GLU A CD  1 
ATOM   1001 O  OE1 . GLU A 1 160 ? -27.399 -25.531 4.442   1.00 41.48  ? 136 GLU A OE1 1 
ATOM   1002 O  OE2 . GLU A 1 160 ? -25.730 -24.538 5.469   1.00 41.16  ? 136 GLU A OE2 1 
ATOM   1003 N  N   . ARG A 1 161 ? -28.762 -21.786 0.355   1.00 37.32  ? 137 ARG A N   1 
ATOM   1004 C  CA  . ARG A 1 161 ? -28.672 -21.568 -1.086  1.00 39.86  ? 137 ARG A CA  1 
ATOM   1005 C  C   . ARG A 1 161 ? -28.984 -20.120 -1.447  1.00 37.40  ? 137 ARG A C   1 
ATOM   1006 O  O   . ARG A 1 161 ? -28.267 -19.499 -2.239  1.00 39.97  ? 137 ARG A O   1 
ATOM   1007 C  CB  . ARG A 1 161 ? -29.624 -22.519 -1.816  1.00 44.55  ? 137 ARG A CB  1 
ATOM   1008 C  CG  . ARG A 1 161 ? -29.293 -23.992 -1.630  1.00 45.76  ? 137 ARG A CG  1 
ATOM   1009 C  CD  . ARG A 1 161 ? -30.489 -24.884 -1.932  1.00 52.45  ? 137 ARG A CD  1 
ATOM   1010 N  NE  . ARG A 1 161 ? -30.282 -26.232 -1.416  1.00 54.52  ? 137 ARG A NE  1 
ATOM   1011 C  CZ  . ARG A 1 161 ? -31.239 -27.011 -0.927  1.00 53.71  ? 137 ARG A CZ  1 
ATOM   1012 N  NH1 . ARG A 1 161 ? -32.502 -26.614 -0.880  1.00 57.38  ? 137 ARG A NH1 1 
ATOM   1013 N  NH2 . ARG A 1 161 ? -30.920 -28.215 -0.463  1.00 55.38  ? 137 ARG A NH2 1 
ATOM   1014 N  N   . ASN A 1 162 ? -30.063 -19.568 -0.885  1.00 40.13  ? 138 ASN A N   1 
ATOM   1015 C  CA  . ASN A 1 162 ? -30.410 -18.178 -1.164  1.00 40.77  ? 138 ASN A CA  1 
ATOM   1016 C  C   . ASN A 1 162 ? -29.315 -17.238 -0.680  1.00 41.16  ? 138 ASN A C   1 
ATOM   1017 O  O   . ASN A 1 162 ? -28.983 -16.253 -1.351  1.00 40.96  ? 138 ASN A O   1 
ATOM   1018 C  CB  . ASN A 1 162 ? -31.739 -17.823 -0.496  1.00 39.05  ? 138 ASN A CB  1 
ATOM   1019 C  CG  . ASN A 1 162 ? -32.884 -18.710 -0.954  1.00 46.56  ? 138 ASN A CG  1 
ATOM   1020 O  OD1 . ASN A 1 162 ? -32.906 -19.190 -2.088  1.00 46.69  ? 138 ASN A OD1 1 
ATOM   1021 N  ND2 . ASN A 1 162 ? -33.846 -18.928 -0.068  1.00 39.36  ? 138 ASN A ND2 1 
ATOM   1022 N  N   . TYR A 1 163 ? -28.743 -17.537 0.485   1.00 40.00  ? 139 TYR A N   1 
ATOM   1023 C  CA  . TYR A 1 163 ? -27.738 -16.676 1.099   1.00 38.75  ? 139 TYR A CA  1 
ATOM   1024 C  C   . TYR A 1 163 ? -26.462 -16.633 0.265   1.00 40.17  ? 139 TYR A C   1 
ATOM   1025 O  O   . TYR A 1 163 ? -26.012 -15.560 -0.154  1.00 38.91  ? 139 TYR A O   1 
ATOM   1026 C  CB  . TYR A 1 163 ? -27.464 -17.193 2.513   1.00 38.66  ? 139 TYR A CB  1 
ATOM   1027 C  CG  . TYR A 1 163 ? -26.612 -16.323 3.405   1.00 39.95  ? 139 TYR A CG  1 
ATOM   1028 C  CD1 . TYR A 1 163 ? -26.835 -14.957 3.514   1.00 41.45  ? 139 TYR A CD1 1 
ATOM   1029 C  CD2 . TYR A 1 163 ? -25.609 -16.887 4.185   1.00 39.36  ? 139 TYR A CD2 1 
ATOM   1030 C  CE1 . TYR A 1 163 ? -26.061 -14.172 4.353   1.00 40.32  ? 139 TYR A CE1 1 
ATOM   1031 C  CE2 . TYR A 1 163 ? -24.837 -16.116 5.023   1.00 41.03  ? 139 TYR A CE2 1 
ATOM   1032 C  CZ  . TYR A 1 163 ? -25.066 -14.759 5.107   1.00 42.55  ? 139 TYR A CZ  1 
ATOM   1033 O  OH  . TYR A 1 163 ? -24.290 -13.994 5.947   1.00 42.22  ? 139 TYR A OH  1 
ATOM   1034 N  N   . LEU A 1 164 ? -25.865 -17.798 0.008   1.00 40.57  ? 140 LEU A N   1 
ATOM   1035 C  CA  . LEU A 1 164 ? -24.598 -17.840 -0.711  1.00 42.61  ? 140 LEU A CA  1 
ATOM   1036 C  C   . LEU A 1 164 ? -24.754 -17.495 -2.186  1.00 44.32  ? 140 LEU A C   1 
ATOM   1037 O  O   . LEU A 1 164 ? -23.785 -17.053 -2.810  1.00 48.70  ? 140 LEU A O   1 
ATOM   1038 C  CB  . LEU A 1 164 ? -23.961 -19.223 -0.565  1.00 44.67  ? 140 LEU A CB  1 
ATOM   1039 C  CG  . LEU A 1 164 ? -23.737 -19.701 0.873   1.00 42.26  ? 140 LEU A CG  1 
ATOM   1040 C  CD1 . LEU A 1 164 ? -23.074 -21.067 0.886   1.00 43.68  ? 140 LEU A CD1 1 
ATOM   1041 C  CD2 . LEU A 1 164 ? -22.911 -18.697 1.658   1.00 45.04  ? 140 LEU A CD2 1 
ATOM   1042 N  N   . GLY A 1 165 ? -25.942 -17.685 -2.759  1.00 41.68  ? 141 GLY A N   1 
ATOM   1043 C  CA  . GLY A 1 165 ? -26.161 -17.310 -4.144  1.00 42.01  ? 141 GLY A CA  1 
ATOM   1044 C  C   . GLY A 1 165 ? -26.444 -15.842 -4.371  1.00 42.86  ? 141 GLY A C   1 
ATOM   1045 O  O   . GLY A 1 165 ? -26.474 -15.401 -5.524  1.00 45.43  ? 141 GLY A O   1 
ATOM   1046 N  N   . ASN A 1 166 ? -26.632 -15.072 -3.302  1.00 39.26  ? 142 ASN A N   1 
ATOM   1047 C  CA  . ASN A 1 166 ? -27.086 -13.690 -3.411  1.00 40.12  ? 142 ASN A CA  1 
ATOM   1048 C  C   . ASN A 1 166 ? -25.928 -12.807 -3.865  1.00 39.81  ? 142 ASN A C   1 
ATOM   1049 O  O   . ASN A 1 166 ? -24.987 -12.561 -3.103  1.00 36.61  ? 142 ASN A O   1 
ATOM   1050 C  CB  . ASN A 1 166 ? -27.649 -13.220 -2.073  1.00 36.79  ? 142 ASN A CB  1 
ATOM   1051 C  CG  . ASN A 1 166 ? -28.259 -11.835 -2.151  1.00 37.47  ? 142 ASN A CG  1 
ATOM   1052 O  OD1 . ASN A 1 166 ? -28.115 -11.131 -3.151  1.00 36.29  ? 142 ASN A OD1 1 
ATOM   1053 N  ND2 . ASN A 1 166 ? -28.940 -11.433 -1.086  1.00 33.01  ? 142 ASN A ND2 1 
ATOM   1054 N  N   . LYS A 1 167 ? -26.005 -12.316 -5.100  1.00 40.92  ? 143 LYS A N   1 
ATOM   1055 C  CA  . LYS A 1 167 ? -24.987 -11.443 -5.669  1.00 38.83  ? 143 LYS A CA  1 
ATOM   1056 C  C   . LYS A 1 167 ? -25.209 -9.970  -5.350  1.00 37.74  ? 143 LYS A C   1 
ATOM   1057 O  O   . LYS A 1 167 ? -24.457 -9.126  -5.851  1.00 34.36  ? 143 LYS A O   1 
ATOM   1058 C  CB  . LYS A 1 167 ? -24.937 -11.615 -7.190  1.00 43.18  ? 143 LYS A CB  1 
ATOM   1059 C  CG  . LYS A 1 167 ? -24.561 -13.006 -7.660  1.00 47.31  ? 143 LYS A CG  1 
ATOM   1060 C  CD  . LYS A 1 167 ? -24.694 -13.112 -9.167  1.00 50.19  ? 143 LYS A CD  1 
ATOM   1061 C  CE  . LYS A 1 167 ? -23.631 -14.017 -9.765  1.00 59.23  ? 143 LYS A CE  1 
ATOM   1062 N  NZ  . LYS A 1 167 ? -23.811 -14.182 -11.234 1.00 59.98  ? 143 LYS A NZ  1 
ATOM   1063 N  N   . ASP A 1 168 ? -26.208 -9.637  -4.533  1.00 34.34  ? 144 ASP A N   1 
ATOM   1064 C  CA  . ASP A 1 168 ? -26.611 -8.252  -4.321  1.00 36.19  ? 144 ASP A CA  1 
ATOM   1065 C  C   . ASP A 1 168 ? -26.565 -7.858  -2.848  1.00 34.72  ? 144 ASP A C   1 
ATOM   1066 O  O   . ASP A 1 168 ? -27.319 -6.988  -2.411  1.00 35.12  ? 144 ASP A O   1 
ATOM   1067 C  CB  . ASP A 1 168 ? -28.011 -8.019  -4.891  1.00 34.53  ? 144 ASP A CB  1 
ATOM   1068 C  CG  . ASP A 1 168 ? -28.055 -8.165  -6.399  1.00 38.65  ? 144 ASP A CG  1 
ATOM   1069 O  OD1 . ASP A 1 168 ? -27.259 -7.494  -7.083  1.00 41.48  ? 144 ASP A OD1 1 
ATOM   1070 O  OD2 . ASP A 1 168 ? -28.875 -8.958  -6.902  1.00 45.28  ? 144 ASP A OD2 1 
ATOM   1071 N  N   . ILE A 1 169 ? -25.681 -8.477  -2.072  1.00 32.59  ? 145 ILE A N   1 
ATOM   1072 C  CA  . ILE A 1 169 ? -25.588 -8.179  -0.647  1.00 33.76  ? 145 ILE A CA  1 
ATOM   1073 C  C   . ILE A 1 169 ? -24.853 -6.859  -0.451  1.00 32.54  ? 145 ILE A C   1 
ATOM   1074 O  O   . ILE A 1 169 ? -23.743 -6.667  -0.963  1.00 31.99  ? 145 ILE A O   1 
ATOM   1075 C  CB  . ILE A 1 169 ? -24.883 -9.315  0.109   1.00 32.06  ? 145 ILE A CB  1 
ATOM   1076 C  CG1 . ILE A 1 169 ? -25.693 -10.607 -0.005  1.00 33.80  ? 145 ILE A CG1 1 
ATOM   1077 C  CG2 . ILE A 1 169 ? -24.682 -8.922  1.573   1.00 35.28  ? 145 ILE A CG2 1 
ATOM   1078 C  CD1 . ILE A 1 169 ? -25.028 -11.810 0.625   1.00 38.02  ? 145 ILE A CD1 1 
ATOM   1079 N  N   . ILE A 1 170 ? -25.471 -5.953  0.302   1.00 29.06  ? 146 ILE A N   1 
ATOM   1080 C  CA  . ILE A 1 170 ? -24.876 -4.679  0.682   1.00 33.47  ? 146 ILE A CA  1 
ATOM   1081 C  C   . ILE A 1 170 ? -24.788 -4.658  2.202   1.00 34.25  ? 146 ILE A C   1 
ATOM   1082 O  O   . ILE A 1 170 ? -25.816 -4.658  2.892   1.00 33.70  ? 146 ILE A O   1 
ATOM   1083 C  CB  . ILE A 1 170 ? -25.684 -3.482  0.166   1.00 32.53  ? 146 ILE A CB  1 
ATOM   1084 C  CG1 . ILE A 1 170 ? -25.671 -3.448  -1.363  1.00 32.62  ? 146 ILE A CG1 1 
ATOM   1085 C  CG2 . ILE A 1 170 ? -25.123 -2.188  0.745   1.00 36.66  ? 146 ILE A CG2 1 
ATOM   1086 C  CD1 . ILE A 1 170 ? -26.722 -2.531  -1.959  1.00 34.80  ? 146 ILE A CD1 1 
ATOM   1087 N  N   . PHE A 1 171 ? -23.565 -4.651  2.721   1.00 32.71  ? 147 PHE A N   1 
ATOM   1088 C  CA  . PHE A 1 171 ? -23.306 -4.554  4.157   1.00 33.57  ? 147 PHE A CA  1 
ATOM   1089 C  C   . PHE A 1 171 ? -23.322 -3.068  4.497   1.00 32.20  ? 147 PHE A C   1 
ATOM   1090 O  O   . PHE A 1 171 ? -22.338 -2.360  4.274   1.00 34.44  ? 147 PHE A O   1 
ATOM   1091 C  CB  . PHE A 1 171 ? -21.971 -5.217  4.487   1.00 33.59  ? 147 PHE A CB  1 
ATOM   1092 C  CG  . PHE A 1 171 ? -21.691 -5.376  5.962   1.00 36.60  ? 147 PHE A CG  1 
ATOM   1093 C  CD1 . PHE A 1 171 ? -22.714 -5.422  6.896   1.00 36.50  ? 147 PHE A CD1 1 
ATOM   1094 C  CD2 . PHE A 1 171 ? -20.381 -5.490  6.408   1.00 37.05  ? 147 PHE A CD2 1 
ATOM   1095 C  CE1 . PHE A 1 171 ? -22.433 -5.576  8.243   1.00 36.87  ? 147 PHE A CE1 1 
ATOM   1096 C  CE2 . PHE A 1 171 ? -20.099 -5.641  7.751   1.00 36.55  ? 147 PHE A CE2 1 
ATOM   1097 C  CZ  . PHE A 1 171 ? -21.124 -5.685  8.668   1.00 35.35  ? 147 PHE A CZ  1 
ATOM   1098 N  N   . ARG A 1 172 ? -24.448 -2.585  5.018   1.00 33.31  ? 148 ARG A N   1 
ATOM   1099 C  CA  . ARG A 1 172 ? -24.697 -1.151  5.137   1.00 34.57  ? 148 ARG A CA  1 
ATOM   1100 C  C   . ARG A 1 172 ? -24.085 -0.605  6.423   1.00 33.37  ? 148 ARG A C   1 
ATOM   1101 O  O   . ARG A 1 172 ? -24.407 -1.074  7.520   1.00 32.44  ? 148 ARG A O   1 
ATOM   1102 C  CB  . ARG A 1 172 ? -26.197 -0.856  5.103   1.00 34.32  ? 148 ARG A CB  1 
ATOM   1103 C  CG  . ARG A 1 172 ? -26.533 0.615   5.345   1.00 37.59  ? 148 ARG A CG  1 
ATOM   1104 C  CD  . ARG A 1 172 ? -28.031 0.868   5.463   1.00 38.01  ? 148 ARG A CD  1 
ATOM   1105 N  NE  . ARG A 1 172 ? -28.278 2.168   6.081   1.00 37.29  ? 148 ARG A NE  1 
ATOM   1106 C  CZ  . ARG A 1 172 ? -28.980 3.158   5.543   1.00 41.68  ? 148 ARG A CZ  1 
ATOM   1107 N  NH1 . ARG A 1 172 ? -29.627 3.012   4.397   1.00 43.47  ? 148 ARG A NH1 1 
ATOM   1108 N  NH2 . ARG A 1 172 ? -29.045 4.324   6.179   1.00 39.54  ? 148 ARG A NH2 1 
ATOM   1109 N  N   . ASN A 1 173 ? -23.224 0.412   6.282   1.00 32.04  ? 149 ASN A N   1 
ATOM   1110 C  CA  . ASN A 1 173 ? -22.637 1.155   7.393   1.00 31.87  ? 149 ASN A CA  1 
ATOM   1111 C  C   . ASN A 1 173 ? -22.352 2.575   6.895   1.00 31.12  ? 149 ASN A C   1 
ATOM   1112 O  O   . ASN A 1 173 ? -21.209 2.984   6.686   1.00 32.64  ? 149 ASN A O   1 
ATOM   1113 C  CB  . ASN A 1 173 ? -21.359 0.501   7.925   1.00 32.72  ? 149 ASN A CB  1 
ATOM   1114 C  CG  . ASN A 1 173 ? -21.573 -0.926  8.383   1.00 34.57  ? 149 ASN A CG  1 
ATOM   1115 O  OD1 . ASN A 1 173 ? -22.041 -1.174  9.498   1.00 32.09  ? 149 ASN A OD1 1 
ATOM   1116 N  ND2 . ASN A 1 173 ? -21.211 -1.878  7.530   1.00 29.27  ? 149 ASN A ND2 1 
ATOM   1117 N  N   . THR A 1 174 ? -23.413 3.353   6.692   1.00 30.50  ? 150 THR A N   1 
ATOM   1118 C  CA  . THR A 1 174 ? -23.242 4.720   6.231   1.00 34.00  ? 150 THR A CA  1 
ATOM   1119 C  C   . THR A 1 174 ? -22.610 5.570   7.331   1.00 33.17  ? 150 THR A C   1 
ATOM   1120 O  O   . THR A 1 174 ? -22.536 5.175   8.498   1.00 30.80  ? 150 THR A O   1 
ATOM   1121 C  CB  . THR A 1 174 ? -24.583 5.325   5.805   1.00 34.56  ? 150 THR A CB  1 
ATOM   1122 O  OG1 . THR A 1 174 ? -25.424 5.501   6.953   1.00 32.22  ? 150 THR A OG1 1 
ATOM   1123 C  CG2 . THR A 1 174 ? -25.287 4.428   4.796   1.00 32.94  ? 150 THR A CG2 1 
ATOM   1124 N  N   . PHE A 1 175 ? -22.145 6.760   6.944   1.00 31.75  ? 151 PHE A N   1 
ATOM   1125 C  CA  . PHE A 1 175 ? -21.602 7.683   7.935   1.00 35.19  ? 151 PHE A CA  1 
ATOM   1126 C  C   . PHE A 1 175 ? -22.640 8.007   9.004   1.00 34.64  ? 151 PHE A C   1 
ATOM   1127 O  O   . PHE A 1 175 ? -22.313 8.095   10.193  1.00 33.96  ? 151 PHE A O   1 
ATOM   1128 C  CB  . PHE A 1 175 ? -21.110 8.960   7.253   1.00 34.85  ? 151 PHE A CB  1 
ATOM   1129 C  CG  . PHE A 1 175 ? -19.901 8.755   6.383   1.00 38.00  ? 151 PHE A CG  1 
ATOM   1130 C  CD1 . PHE A 1 175 ? -18.656 8.539   6.946   1.00 36.66  ? 151 PHE A CD1 1 
ATOM   1131 C  CD2 . PHE A 1 175 ? -20.009 8.784   5.002   1.00 37.57  ? 151 PHE A CD2 1 
ATOM   1132 C  CE1 . PHE A 1 175 ? -17.541 8.351   6.151   1.00 37.77  ? 151 PHE A CE1 1 
ATOM   1133 C  CE2 . PHE A 1 175 ? -18.898 8.599   4.203   1.00 37.04  ? 151 PHE A CE2 1 
ATOM   1134 C  CZ  . PHE A 1 175 ? -17.664 8.382   4.777   1.00 36.29  ? 151 PHE A CZ  1 
ATOM   1135 N  N   . GLY A 1 176 ? -23.901 8.174   8.600   1.00 32.31  ? 152 GLY A N   1 
ATOM   1136 C  CA  . GLY A 1 176 ? -24.956 8.403   9.576   1.00 36.19  ? 152 GLY A CA  1 
ATOM   1137 C  C   . GLY A 1 176 ? -25.182 7.207   10.482  1.00 36.04  ? 152 GLY A C   1 
ATOM   1138 O  O   . GLY A 1 176 ? -25.375 7.361   11.691  1.00 35.38  ? 152 GLY A O   1 
ATOM   1139 N  N   . ASP A 1 177 ? -25.170 5.999   9.910   1.00 33.55  ? 153 ASP A N   1 
ATOM   1140 C  CA  . ASP A 1 177 ? -25.290 4.792   10.722  1.00 34.34  ? 153 ASP A CA  1 
ATOM   1141 C  C   . ASP A 1 177 ? -24.187 4.730   11.770  1.00 38.94  ? 153 ASP A C   1 
ATOM   1142 O  O   . ASP A 1 177 ? -24.453 4.545   12.964  1.00 36.43  ? 153 ASP A O   1 
ATOM   1143 C  CB  . ASP A 1 177 ? -25.226 3.546   9.837   1.00 35.03  ? 153 ASP A CB  1 
ATOM   1144 C  CG  . ASP A 1 177 ? -26.392 3.439   8.880   1.00 37.55  ? 153 ASP A CG  1 
ATOM   1145 O  OD1 . ASP A 1 177 ? -27.487 3.945   9.204   1.00 38.77  ? 153 ASP A OD1 1 
ATOM   1146 O  OD2 . ASP A 1 177 ? -26.209 2.833   7.802   1.00 39.37  ? 153 ASP A OD2 1 
ATOM   1147 N  N   . VAL A 1 178 ? -22.935 4.877   11.332  1.00 33.50  ? 154 VAL A N   1 
ATOM   1148 C  CA  . VAL A 1 178 ? -21.802 4.712   12.236  1.00 35.54  ? 154 VAL A CA  1 
ATOM   1149 C  C   . VAL A 1 178 ? -21.859 5.740   13.358  1.00 38.29  ? 154 VAL A C   1 
ATOM   1150 O  O   . VAL A 1 178 ? -21.619 5.417   14.527  1.00 37.76  ? 154 VAL A O   1 
ATOM   1151 C  CB  . VAL A 1 178 ? -20.482 4.799   11.447  1.00 35.65  ? 154 VAL A CB  1 
ATOM   1152 C  CG1 . VAL A 1 178 ? -19.293 4.828   12.393  1.00 30.83  ? 154 VAL A CG1 1 
ATOM   1153 C  CG2 . VAL A 1 178 ? -20.370 3.629   10.482  1.00 32.47  ? 154 VAL A CG2 1 
ATOM   1154 N  N   . GLU A 1 179 ? -22.172 6.994   13.023  1.00 35.50  ? 155 GLU A N   1 
ATOM   1155 C  CA  . GLU A 1 179 ? -22.286 8.021   14.054  1.00 42.08  ? 155 GLU A CA  1 
ATOM   1156 C  C   . GLU A 1 179 ? -23.386 7.675   15.052  1.00 41.39  ? 155 GLU A C   1 
ATOM   1157 O  O   . GLU A 1 179 ? -23.238 7.905   16.258  1.00 40.69  ? 155 GLU A O   1 
ATOM   1158 C  CB  . GLU A 1 179 ? -22.551 9.383   13.410  1.00 40.82  ? 155 GLU A CB  1 
ATOM   1159 C  CG  . GLU A 1 179 ? -22.786 10.505  14.410  1.00 49.14  ? 155 GLU A CG  1 
ATOM   1160 C  CD  . GLU A 1 179 ? -22.865 11.869  13.751  1.00 56.94  ? 155 GLU A CD  1 
ATOM   1161 O  OE1 . GLU A 1 179 ? -22.426 11.997  12.589  1.00 59.39  ? 155 GLU A OE1 1 
ATOM   1162 O  OE2 . GLU A 1 179 ? -23.369 12.813  14.397  1.00 63.44  ? 155 GLU A OE2 1 
ATOM   1163 N  N   . HIS A 1 180 ? -24.499 7.120   14.567  1.00 37.85  ? 156 HIS A N   1 
ATOM   1164 C  CA  . HIS A 1 180 ? -25.585 6.742   15.463  1.00 41.10  ? 156 HIS A CA  1 
ATOM   1165 C  C   . HIS A 1 180 ? -25.165 5.614   16.398  1.00 41.92  ? 156 HIS A C   1 
ATOM   1166 O  O   . HIS A 1 180 ? -25.485 5.639   17.593  1.00 41.59  ? 156 HIS A O   1 
ATOM   1167 C  CB  . HIS A 1 180 ? -26.814 6.338   14.649  1.00 42.20  ? 156 HIS A CB  1 
ATOM   1168 C  CG  . HIS A 1 180 ? -27.939 5.800   15.477  1.00 45.73  ? 156 HIS A CG  1 
ATOM   1169 N  ND1 . HIS A 1 180 ? -28.337 4.481   15.424  1.00 50.73  ? 156 HIS A ND1 1 
ATOM   1170 C  CD2 . HIS A 1 180 ? -28.750 6.401   16.379  1.00 47.00  ? 156 HIS A CD2 1 
ATOM   1171 C  CE1 . HIS A 1 180 ? -29.346 4.294   16.256  1.00 47.69  ? 156 HIS A CE1 1 
ATOM   1172 N  NE2 . HIS A 1 180 ? -29.615 5.443   16.849  1.00 50.10  ? 156 HIS A NE2 1 
ATOM   1173 N  N   . VAL A 1 181 ? -24.446 4.617   15.878  1.00 38.79  ? 157 VAL A N   1 
ATOM   1174 C  CA  . VAL A 1 181 ? -24.024 3.501   16.718  1.00 41.18  ? 157 VAL A CA  1 
ATOM   1175 C  C   . VAL A 1 181 ? -23.030 3.973   17.771  1.00 41.61  ? 157 VAL A C   1 
ATOM   1176 O  O   . VAL A 1 181 ? -23.113 3.582   18.942  1.00 41.46  ? 157 VAL A O   1 
ATOM   1177 C  CB  . VAL A 1 181 ? -23.437 2.370   15.856  1.00 39.72  ? 157 VAL A CB  1 
ATOM   1178 C  CG1 . VAL A 1 181 ? -22.980 1.218   16.739  1.00 38.43  ? 157 VAL A CG1 1 
ATOM   1179 C  CG2 . VAL A 1 181 ? -24.458 1.886   14.836  1.00 41.74  ? 157 VAL A CG2 1 
ATOM   1180 N  N   . MET A 1 182 ? -22.072 4.814   17.375  1.00 39.84  ? 158 MET A N   1 
ATOM   1181 C  CA  . MET A 1 182 ? -21.121 5.362   18.337  1.00 41.88  ? 158 MET A CA  1 
ATOM   1182 C  C   . MET A 1 182 ? -21.846 6.057   19.481  1.00 42.73  ? 158 MET A C   1 
ATOM   1183 O  O   . MET A 1 182 ? -21.544 5.828   20.658  1.00 44.16  ? 158 MET A O   1 
ATOM   1184 C  CB  . MET A 1 182 ? -20.177 6.341   17.638  1.00 40.38  ? 158 MET A CB  1 
ATOM   1185 C  CG  . MET A 1 182 ? -19.153 5.695   16.723  1.00 39.74  ? 158 MET A CG  1 
ATOM   1186 S  SD  . MET A 1 182 ? -18.284 6.929   15.738  1.00 43.59  ? 158 MET A SD  1 
ATOM   1187 C  CE  . MET A 1 182 ? -17.066 5.909   14.906  1.00 34.81  ? 158 MET A CE  1 
ATOM   1188 N  N   . THR A 1 183 ? -22.810 6.916   19.149  1.00 40.87  ? 159 THR A N   1 
ATOM   1189 C  CA  . THR A 1 183 ? -23.529 7.664   20.172  1.00 43.83  ? 159 THR A CA  1 
ATOM   1190 C  C   . THR A 1 183 ? -24.346 6.734   21.061  1.00 45.51  ? 159 THR A C   1 
ATOM   1191 O  O   . THR A 1 183 ? -24.265 6.805   22.293  1.00 47.70  ? 159 THR A O   1 
ATOM   1192 C  CB  . THR A 1 183 ? -24.432 8.705   19.507  1.00 41.69  ? 159 THR A CB  1 
ATOM   1193 O  OG1 . THR A 1 183 ? -23.624 9.682   18.841  1.00 49.49  ? 159 THR A OG1 1 
ATOM   1194 C  CG2 . THR A 1 183 ? -25.314 9.391   20.536  1.00 47.05  ? 159 THR A CG2 1 
ATOM   1195 N  N   . THR A 1 184 ? -25.137 5.851   20.452  1.00 42.54  ? 160 THR A N   1 
ATOM   1196 C  CA  . THR A 1 184 ? -26.033 4.999   21.227  1.00 45.49  ? 160 THR A CA  1 
ATOM   1197 C  C   . THR A 1 184 ? -25.247 4.057   22.133  1.00 45.71  ? 160 THR A C   1 
ATOM   1198 O  O   . THR A 1 184 ? -25.416 4.064   23.357  1.00 47.79  ? 160 THR A O   1 
ATOM   1199 C  CB  . THR A 1 184 ? -26.946 4.209   20.285  1.00 45.39  ? 160 THR A CB  1 
ATOM   1200 O  OG1 . THR A 1 184 ? -27.706 5.117   19.478  1.00 46.23  ? 160 THR A OG1 1 
ATOM   1201 C  CG2 . THR A 1 184 ? -27.898 3.323   21.078  1.00 46.77  ? 160 THR A CG2 1 
ATOM   1202 N  N   . LEU A 1 185 ? -24.373 3.238   21.545  1.00 44.74  ? 161 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 185 ? -23.660 2.243   22.338  1.00 43.61  ? 161 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 185 ? -22.632 2.886   23.259  1.00 43.37  ? 161 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 185 ? -22.352 2.351   24.338  1.00 45.88  ? 161 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 185 ? -22.983 1.222   21.421  1.00 40.87  ? 161 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 185 ? -23.898 0.473   20.450  1.00 42.40  ? 161 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 185 ? -23.137 -0.652  19.761  1.00 38.41  ? 161 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 185 ? -25.138 -0.067  21.158  1.00 44.18  ? 161 LEU A CD2 1 
ATOM   1210 N  N   . GLY A 1 186 ? -22.064 4.026   22.861  1.00 43.93  ? 162 GLY A N   1 
ATOM   1211 C  CA  . GLY A 1 186 ? -21.067 4.674   23.695  1.00 44.13  ? 162 GLY A CA  1 
ATOM   1212 C  C   . GLY A 1 186 ? -21.618 5.146   25.026  1.00 48.47  ? 162 GLY A C   1 
ATOM   1213 O  O   . GLY A 1 186 ? -20.891 5.195   26.022  1.00 50.75  ? 162 GLY A O   1 
ATOM   1214 N  N   . ALA A 1 187 ? -22.905 5.496   25.066  1.00 45.83  ? 163 ALA A N   1 
ATOM   1215 C  CA  . ALA A 1 187 ? -23.516 5.934   26.315  1.00 50.06  ? 163 ALA A CA  1 
ATOM   1216 C  C   . ALA A 1 187 ? -23.545 4.827   27.360  1.00 50.37  ? 163 ALA A C   1 
ATOM   1217 O  O   . ALA A 1 187 ? -23.624 5.122   28.557  1.00 54.96  ? 163 ALA A O   1 
ATOM   1218 C  CB  . ALA A 1 187 ? -24.937 6.439   26.056  1.00 48.22  ? 163 ALA A CB  1 
ATOM   1219 N  N   . GLY A 1 188 ? -23.484 3.565   26.939  1.00 48.66  ? 164 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 188 ? -23.505 2.453   27.868  1.00 47.41  ? 164 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 188 ? -22.121 1.970   28.254  1.00 46.53  ? 164 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 188 ? -21.967 0.859   28.772  1.00 42.69  ? 164 GLY A O   1 
ATOM   1223 N  N   . GLY A 1 189 ? -21.105 2.796   28.009  1.00 46.86  ? 165 GLY A N   1 
ATOM   1224 C  CA  . GLY A 1 189 ? -19.740 2.448   28.342  1.00 42.02  ? 165 GLY A CA  1 
ATOM   1225 C  C   . GLY A 1 189 ? -19.072 1.482   27.389  1.00 42.12  ? 165 GLY A C   1 
ATOM   1226 O  O   . GLY A 1 189 ? -17.908 1.123   27.613  1.00 38.16  ? 165 GLY A O   1 
ATOM   1227 N  N   . THR A 1 190 ? -19.762 1.051   26.337  1.00 41.94  ? 166 THR A N   1 
ATOM   1228 C  CA  . THR A 1 190 ? -19.174 0.113   25.393  1.00 38.63  ? 166 THR A CA  1 
ATOM   1229 C  C   . THR A 1 190 ? -18.120 0.802   24.538  1.00 39.63  ? 166 THR A C   1 
ATOM   1230 O  O   . THR A 1 190 ? -18.318 1.923   24.059  1.00 39.44  ? 166 THR A O   1 
ATOM   1231 C  CB  . THR A 1 190 ? -20.254 -0.484  24.491  1.00 38.80  ? 166 THR A CB  1 
ATOM   1232 O  OG1 . THR A 1 190 ? -21.269 -1.100  25.293  1.00 36.38  ? 166 THR A OG1 1 
ATOM   1233 C  CG2 . THR A 1 190 ? -19.649 -1.521  23.544  1.00 34.21  ? 166 THR A CG2 1 
ATOM   1234 N  N   . ARG A 1 191 ? -16.994 0.125   24.351  1.00 34.23  ? 167 ARG A N   1 
ATOM   1235 C  CA  . ARG A 1 191 ? -15.962 0.553   23.422  1.00 36.96  ? 167 ARG A CA  1 
ATOM   1236 C  C   . ARG A 1 191 ? -15.963 -0.380  22.218  1.00 36.63  ? 167 ARG A C   1 
ATOM   1237 O  O   . ARG A 1 191 ? -16.525 -1.478  22.257  1.00 35.77  ? 167 ARG A O   1 
ATOM   1238 C  CB  . ARG A 1 191 ? -14.595 0.592   24.111  1.00 37.54  ? 167 ARG A CB  1 
ATOM   1239 C  CG  . ARG A 1 191 ? -14.549 1.649   25.209  1.00 42.11  ? 167 ARG A CG  1 
ATOM   1240 C  CD  . ARG A 1 191 ? -13.165 1.842   25.786  1.00 40.50  ? 167 ARG A CD  1 
ATOM   1241 N  NE  . ARG A 1 191 ? -12.202 2.270   24.779  1.00 43.66  ? 167 ARG A NE  1 
ATOM   1242 C  CZ  . ARG A 1 191 ? -12.047 3.520   24.366  1.00 42.02  ? 167 ARG A CZ  1 
ATOM   1243 N  NH1 . ARG A 1 191 ? -12.797 4.503   24.835  1.00 46.55  ? 167 ARG A NH1 1 
ATOM   1244 N  NH2 . ARG A 1 191 ? -11.116 3.791   23.456  1.00 45.17  ? 167 ARG A NH2 1 
ATOM   1245 N  N   . PHE A 1 192 ? -15.352 0.076   21.132  1.00 33.76  ? 168 PHE A N   1 
ATOM   1246 C  CA  . PHE A 1 192 ? -15.556 -0.545  19.835  1.00 33.81  ? 168 PHE A CA  1 
ATOM   1247 C  C   . PHE A 1 192 ? -14.301 -1.233  19.320  1.00 32.66  ? 168 PHE A C   1 
ATOM   1248 O  O   . PHE A 1 192 ? -13.174 -0.788  19.556  1.00 33.98  ? 168 PHE A O   1 
ATOM   1249 C  CB  . PHE A 1 192 ? -16.024 0.490   18.809  1.00 33.77  ? 168 PHE A CB  1 
ATOM   1250 C  CG  . PHE A 1 192 ? -17.318 1.144   19.175  1.00 34.53  ? 168 PHE A CG  1 
ATOM   1251 C  CD1 . PHE A 1 192 ? -18.488 0.405   19.226  1.00 35.21  ? 168 PHE A CD1 1 
ATOM   1252 C  CD2 . PHE A 1 192 ? -17.368 2.493   19.477  1.00 35.15  ? 168 PHE A CD2 1 
ATOM   1253 C  CE1 . PHE A 1 192 ? -19.683 0.998   19.570  1.00 36.19  ? 168 PHE A CE1 1 
ATOM   1254 C  CE2 . PHE A 1 192 ? -18.562 3.094   19.822  1.00 36.60  ? 168 PHE A CE2 1 
ATOM   1255 C  CZ  . PHE A 1 192 ? -19.722 2.345   19.869  1.00 39.34  ? 168 PHE A CZ  1 
ATOM   1256 N  N   . GLU A 1 193 ? -14.526 -2.341  18.624  1.00 34.80  ? 169 GLU A N   1 
ATOM   1257 C  CA  . GLU A 1 193 ? -13.548 -2.924  17.713  1.00 31.01  ? 169 GLU A CA  1 
ATOM   1258 C  C   . GLU A 1 193 ? -13.932 -2.421  16.326  1.00 31.92  ? 169 GLU A C   1 
ATOM   1259 O  O   . GLU A 1 193 ? -14.916 -2.877  15.739  1.00 34.03  ? 169 GLU A O   1 
ATOM   1260 C  CB  . GLU A 1 193 ? -13.554 -4.445  17.788  1.00 34.30  ? 169 GLU A CB  1 
ATOM   1261 C  CG  . GLU A 1 193 ? -12.554 -5.109  16.855  1.00 31.86  ? 169 GLU A CG  1 
ATOM   1262 C  CD  . GLU A 1 193 ? -12.563 -6.621  16.963  1.00 38.86  ? 169 GLU A CD  1 
ATOM   1263 O  OE1 . GLU A 1 193 ? -13.551 -7.249  16.523  1.00 38.06  ? 169 GLU A OE1 1 
ATOM   1264 O  OE2 . GLU A 1 193 ? -11.582 -7.181  17.500  1.00 43.35  ? 169 GLU A OE2 1 
ATOM   1265 N  N   . PHE A 1 194 ? -13.177 -1.451  15.820  1.00 31.16  ? 170 PHE A N   1 
ATOM   1266 C  CA  . PHE A 1 194 ? -13.487 -0.832  14.537  1.00 32.06  ? 170 PHE A CA  1 
ATOM   1267 C  C   . PHE A 1 194 ? -13.037 -1.769  13.422  1.00 31.12  ? 170 PHE A C   1 
ATOM   1268 O  O   . PHE A 1 194 ? -11.837 -1.929  13.180  1.00 33.27  ? 170 PHE A O   1 
ATOM   1269 C  CB  . PHE A 1 194 ? -12.810 0.531   14.424  1.00 30.97  ? 170 PHE A CB  1 
ATOM   1270 C  CG  . PHE A 1 194 ? -13.158 1.474   15.539  1.00 30.62  ? 170 PHE A CG  1 
ATOM   1271 C  CD1 . PHE A 1 194 ? -14.362 2.163   15.532  1.00 30.37  ? 170 PHE A CD1 1 
ATOM   1272 C  CD2 . PHE A 1 194 ? -12.280 1.678   16.592  1.00 31.65  ? 170 PHE A CD2 1 
ATOM   1273 C  CE1 . PHE A 1 194 ? -14.684 3.031   16.557  1.00 31.76  ? 170 PHE A CE1 1 
ATOM   1274 C  CE2 . PHE A 1 194 ? -12.598 2.547   17.619  1.00 29.84  ? 170 PHE A CE2 1 
ATOM   1275 C  CZ  . PHE A 1 194 ? -13.800 3.224   17.602  1.00 33.09  ? 170 PHE A CZ  1 
ATOM   1276 N  N   . GLU A 1 195 ? -14.001 -2.390  12.747  1.00 32.02  ? 171 GLU A N   1 
ATOM   1277 C  CA  . GLU A 1 195 ? -13.709 -3.355  11.695  1.00 30.13  ? 171 GLU A CA  1 
ATOM   1278 C  C   . GLU A 1 195 ? -13.464 -2.611  10.389  1.00 29.33  ? 171 GLU A C   1 
ATOM   1279 O  O   . GLU A 1 195 ? -14.372 -1.958  9.862   1.00 30.26  ? 171 GLU A O   1 
ATOM   1280 C  CB  . GLU A 1 195 ? -14.863 -4.342  11.532  1.00 28.73  ? 171 GLU A CB  1 
ATOM   1281 C  CG  . GLU A 1 195 ? -15.465 -4.834  12.839  1.00 35.39  ? 171 GLU A CG  1 
ATOM   1282 C  CD  . GLU A 1 195 ? -14.535 -5.751  13.606  1.00 36.43  ? 171 GLU A CD  1 
ATOM   1283 O  OE1 . GLU A 1 195 ? -13.429 -6.041  13.101  1.00 38.23  ? 171 GLU A OE1 1 
ATOM   1284 O  OE2 . GLU A 1 195 ? -14.917 -6.184  14.714  1.00 36.70  ? 171 GLU A OE2 1 
ATOM   1285 N  N   . CYS A 1 196 ? -12.246 -2.716  9.865   1.00 28.39  ? 172 CYS A N   1 
ATOM   1286 C  CA  . CYS A 1 196 ? -11.834 -1.993  8.666   1.00 29.05  ? 172 CYS A CA  1 
ATOM   1287 C  C   . CYS A 1 196 ? -11.451 -3.009  7.598   1.00 27.17  ? 172 CYS A C   1 
ATOM   1288 O  O   . CYS A 1 196 ? -10.478 -3.754  7.758   1.00 28.43  ? 172 CYS A O   1 
ATOM   1289 C  CB  . CYS A 1 196 ? -10.680 -1.046  8.980   1.00 24.71  ? 172 CYS A CB  1 
ATOM   1290 S  SG  . CYS A 1 196 ? -11.101 0.205   10.227  1.00 33.32  ? 172 CYS A SG  1 
ATOM   1291 N  N   . TYR A 1 197 ? -12.220 -3.035  6.514   1.00 25.03  ? 173 TYR A N   1 
ATOM   1292 C  CA  . TYR A 1 197 ? -12.047 -3.996  5.435   1.00 26.05  ? 173 TYR A CA  1 
ATOM   1293 C  C   . TYR A 1 197 ? -11.238 -3.444  4.271   1.00 26.71  ? 173 TYR A C   1 
ATOM   1294 O  O   . TYR A 1 197 ? -10.970 -4.183  3.317   1.00 23.99  ? 173 TYR A O   1 
ATOM   1295 C  CB  . TYR A 1 197 ? -13.419 -4.458  4.929   1.00 24.35  ? 173 TYR A CB  1 
ATOM   1296 C  CG  . TYR A 1 197 ? -14.291 -5.089  5.991   1.00 26.18  ? 173 TYR A CG  1 
ATOM   1297 C  CD1 . TYR A 1 197 ? -14.924 -4.312  6.952   1.00 26.15  ? 173 TYR A CD1 1 
ATOM   1298 C  CD2 . TYR A 1 197 ? -14.490 -6.462  6.024   1.00 26.99  ? 173 TYR A CD2 1 
ATOM   1299 C  CE1 . TYR A 1 197 ? -15.723 -4.887  7.923   1.00 28.18  ? 173 TYR A CE1 1 
ATOM   1300 C  CE2 . TYR A 1 197 ? -15.285 -7.046  6.989   1.00 27.51  ? 173 TYR A CE2 1 
ATOM   1301 C  CZ  . TYR A 1 197 ? -15.902 -6.256  7.935   1.00 30.35  ? 173 TYR A CZ  1 
ATOM   1302 O  OH  . TYR A 1 197 ? -16.698 -6.836  8.896   1.00 29.56  ? 173 TYR A OH  1 
ATOM   1303 N  N   . ASP A 1 198 ? -10.854 -2.171  4.315   1.00 24.90  ? 174 ASP A N   1 
ATOM   1304 C  CA  . ASP A 1 198 ? -10.087 -1.561  3.235   1.00 26.49  ? 174 ASP A CA  1 
ATOM   1305 C  C   . ASP A 1 198 ? -9.633  -0.183  3.698   1.00 27.32  ? 174 ASP A C   1 
ATOM   1306 O  O   . ASP A 1 198 ? -10.035 0.300   4.760   1.00 26.78  ? 174 ASP A O   1 
ATOM   1307 C  CB  . ASP A 1 198 ? -10.910 -1.471  1.944   1.00 24.98  ? 174 ASP A CB  1 
ATOM   1308 C  CG  . ASP A 1 198 ? -10.041 -1.466  0.696   1.00 27.83  ? 174 ASP A CG  1 
ATOM   1309 O  OD1 . ASP A 1 198 ? -8.795  -1.463  0.830   1.00 30.13  ? 174 ASP A OD1 1 
ATOM   1310 O  OD2 . ASP A 1 198 ? -10.602 -1.475  -0.420  1.00 28.29  ? 174 ASP A OD2 1 
ATOM   1311 N  N   . THR A 1 199 ? -8.791  0.449   2.875   1.00 25.42  ? 175 THR A N   1 
ATOM   1312 C  CA  . THR A 1 199 ? -8.199  1.729   3.251   1.00 26.11  ? 175 THR A CA  1 
ATOM   1313 C  C   . THR A 1 199 ? -9.265  2.761   3.587   1.00 24.88  ? 175 THR A C   1 
ATOM   1314 O  O   . THR A 1 199 ? -9.116  3.530   4.545   1.00 27.61  ? 175 THR A O   1 
ATOM   1315 C  CB  . THR A 1 199 ? -7.316  2.252   2.117   1.00 25.87  ? 175 THR A CB  1 
ATOM   1316 O  OG1 . THR A 1 199 ? -6.825  1.151   1.344   1.00 27.07  ? 175 THR A OG1 1 
ATOM   1317 C  CG2 . THR A 1 199 ? -6.147  3.050   2.678   1.00 25.91  ? 175 THR A CG2 1 
ATOM   1318 N  N   . SER A 1 200 ? -10.343 2.800   2.804   1.00 25.42  ? 176 SER A N   1 
ATOM   1319 C  CA  . SER A 1 200 ? -11.356 3.832   2.993   1.00 27.89  ? 176 SER A CA  1 
ATOM   1320 C  C   . SER A 1 200 ? -11.971 3.764   4.384   1.00 28.08  ? 176 SER A C   1 
ATOM   1321 O  O   . SER A 1 200 ? -12.358 4.799   4.940   1.00 28.99  ? 176 SER A O   1 
ATOM   1322 C  CB  . SER A 1 200 ? -12.439 3.703   1.920   1.00 29.04  ? 176 SER A CB  1 
ATOM   1323 O  OG  . SER A 1 200 ? -13.169 2.496   2.063   1.00 29.16  ? 176 SER A OG  1 
ATOM   1324 N  N   . HIS A 1 201 ? -12.060 2.567   4.966   1.00 26.64  ? 177 HIS A N   1 
ATOM   1325 C  CA  . HIS A 1 201 ? -12.637 2.443   6.301   1.00 26.56  ? 177 HIS A CA  1 
ATOM   1326 C  C   . HIS A 1 201 ? -11.738 3.065   7.360   1.00 27.19  ? 177 HIS A C   1 
ATOM   1327 O  O   . HIS A 1 201 ? -12.236 3.565   8.375   1.00 27.00  ? 177 HIS A O   1 
ATOM   1328 C  CB  . HIS A 1 201 ? -12.911 0.974   6.615   1.00 24.70  ? 177 HIS A CB  1 
ATOM   1329 C  CG  . HIS A 1 201 ? -13.915 0.346   5.698   1.00 29.03  ? 177 HIS A CG  1 
ATOM   1330 N  ND1 . HIS A 1 201 ? -14.393 -0.933  5.877   1.00 29.48  ? 177 HIS A ND1 1 
ATOM   1331 C  CD2 . HIS A 1 201 ? -14.537 0.829   4.596   1.00 28.49  ? 177 HIS A CD2 1 
ATOM   1332 C  CE1 . HIS A 1 201 ? -15.261 -1.214  4.922   1.00 30.22  ? 177 HIS A CE1 1 
ATOM   1333 N  NE2 . HIS A 1 201 ? -15.367 -0.161  4.133   1.00 30.19  ? 177 HIS A NE2 1 
ATOM   1334 N  N   . LEU A 1 202 ? -10.419 3.048   7.145   1.00 25.15  ? 178 LEU A N   1 
ATOM   1335 C  CA  . LEU A 1 202 ? -9.522  3.772   8.040   1.00 25.96  ? 178 LEU A CA  1 
ATOM   1336 C  C   . LEU A 1 202 ? -9.710  5.276   7.896   1.00 27.31  ? 178 LEU A C   1 
ATOM   1337 O  O   . LEU A 1 202 ? -9.694  6.011   8.890   1.00 26.45  ? 178 LEU A O   1 
ATOM   1338 C  CB  . LEU A 1 202 ? -8.069  3.399   7.752   1.00 24.81  ? 178 LEU A CB  1 
ATOM   1339 C  CG  . LEU A 1 202 ? -7.637  1.965   8.049   1.00 27.69  ? 178 LEU A CG  1 
ATOM   1340 C  CD1 . LEU A 1 202 ? -6.193  1.766   7.615   1.00 28.66  ? 178 LEU A CD1 1 
ATOM   1341 C  CD2 . LEU A 1 202 ? -7.802  1.645   9.524   1.00 26.11  ? 178 LEU A CD2 1 
ATOM   1342 N  N   . TYR A 1 203 ? -9.875  5.752   6.662   1.00 27.05  ? 179 TYR A N   1 
ATOM   1343 C  CA  . TYR A 1 203 ? -10.148 7.168   6.452   1.00 28.04  ? 179 TYR A CA  1 
ATOM   1344 C  C   . TYR A 1 203 ? -11.496 7.557   7.044   1.00 29.45  ? 179 TYR A C   1 
ATOM   1345 O  O   . TYR A 1 203 ? -11.643 8.648   7.607   1.00 29.37  ? 179 TYR A O   1 
ATOM   1346 C  CB  . TYR A 1 203 ? -10.091 7.495   4.961   1.00 26.38  ? 179 TYR A CB  1 
ATOM   1347 C  CG  . TYR A 1 203 ? -8.684  7.710   4.455   1.00 28.48  ? 179 TYR A CG  1 
ATOM   1348 C  CD1 . TYR A 1 203 ? -8.047  8.933   4.624   1.00 28.55  ? 179 TYR A CD1 1 
ATOM   1349 C  CD2 . TYR A 1 203 ? -7.988  6.693   3.814   1.00 26.24  ? 179 TYR A CD2 1 
ATOM   1350 C  CE1 . TYR A 1 203 ? -6.758  9.138   4.169   1.00 28.38  ? 179 TYR A CE1 1 
ATOM   1351 C  CE2 . TYR A 1 203 ? -6.698  6.891   3.352   1.00 28.31  ? 179 TYR A CE2 1 
ATOM   1352 C  CZ  . TYR A 1 203 ? -6.090  8.114   3.534   1.00 29.32  ? 179 TYR A CZ  1 
ATOM   1353 O  OH  . TYR A 1 203 ? -4.811  8.313   3.074   1.00 30.61  ? 179 TYR A OH  1 
ATOM   1354 N  N   . ASN A 1 204 ? -12.491 6.676   6.932   1.00 26.17  ? 180 ASN A N   1 
ATOM   1355 C  CA  . ASN A 1 204 ? -13.772 6.934   7.581   1.00 28.27  ? 180 ASN A CA  1 
ATOM   1356 C  C   . ASN A 1 204 ? -13.595 7.067   9.088   1.00 29.88  ? 180 ASN A C   1 
ATOM   1357 O  O   . ASN A 1 204 ? -14.121 7.997   9.709   1.00 30.51  ? 180 ASN A O   1 
ATOM   1358 C  CB  . ASN A 1 204 ? -14.767 5.819   7.253   1.00 29.45  ? 180 ASN A CB  1 
ATOM   1359 C  CG  . ASN A 1 204 ? -15.074 5.723   5.769   1.00 31.83  ? 180 ASN A CG  1 
ATOM   1360 O  OD1 . ASN A 1 204 ? -14.683 6.584   4.982   1.00 27.38  ? 180 ASN A OD1 1 
ATOM   1361 N  ND2 . ASN A 1 204 ? -15.788 4.675   5.383   1.00 29.36  ? 180 ASN A ND2 1 
ATOM   1362 N  N   . LEU A 1 205 ? -12.844 6.146   9.695   1.00 31.06  ? 181 LEU A N   1 
ATOM   1363 C  CA  . LEU A 1 205 ? -12.609 6.219   11.134  1.00 32.07  ? 181 LEU A CA  1 
ATOM   1364 C  C   . LEU A 1 205 ? -11.887 7.508   11.504  1.00 32.62  ? 181 LEU A C   1 
ATOM   1365 O  O   . LEU A 1 205 ? -12.225 8.154   12.505  1.00 31.55  ? 181 LEU A O   1 
ATOM   1366 C  CB  . LEU A 1 205 ? -11.809 4.999   11.593  1.00 27.70  ? 181 LEU A CB  1 
ATOM   1367 C  CG  . LEU A 1 205 ? -11.517 4.909   13.093  1.00 31.11  ? 181 LEU A CG  1 
ATOM   1368 C  CD1 . LEU A 1 205 ? -12.802 4.987   13.910  1.00 31.83  ? 181 LEU A CD1 1 
ATOM   1369 C  CD2 . LEU A 1 205 ? -10.761 3.624   13.401  1.00 29.69  ? 181 LEU A CD2 1 
ATOM   1370 N  N   . LYS A 1 206 ? -10.890 7.900   10.706  1.00 30.17  ? 182 LYS A N   1 
ATOM   1371 C  CA  . LYS A 1 206 ? -10.188 9.156   10.951  1.00 31.99  ? 182 LYS A CA  1 
ATOM   1372 C  C   . LYS A 1 206 ? -11.159 10.330  11.015  1.00 32.65  ? 182 LYS A C   1 
ATOM   1373 O  O   . LYS A 1 206 ? -10.985 11.247  11.827  1.00 37.00  ? 182 LYS A O   1 
ATOM   1374 C  CB  . LYS A 1 206 ? -9.140  9.383   9.858   1.00 32.11  ? 182 LYS A CB  1 
ATOM   1375 C  CG  . LYS A 1 206 ? -8.390  10.705  9.947   1.00 33.11  ? 182 LYS A CG  1 
ATOM   1376 C  CD  . LYS A 1 206 ? -7.538  10.783  11.201  1.00 36.07  ? 182 LYS A CD  1 
ATOM   1377 C  CE  . LYS A 1 206 ? -6.552  11.941  11.123  1.00 40.31  ? 182 LYS A CE  1 
ATOM   1378 N  NZ  . LYS A 1 206 ? -5.709  12.038  12.344  1.00 41.85  ? 182 LYS A NZ  1 
ATOM   1379 N  N   . HIS A 1 207 ? -12.190 10.319  10.167  1.00 31.63  ? 183 HIS A N   1 
ATOM   1380 C  CA  . HIS A 1 207 ? -13.165 11.406  10.160  1.00 36.48  ? 183 HIS A CA  1 
ATOM   1381 C  C   . HIS A 1 207 ? -13.863 11.532  11.511  1.00 37.30  ? 183 HIS A C   1 
ATOM   1382 O  O   . HIS A 1 207 ? -14.014 12.637  12.044  1.00 38.67  ? 183 HIS A O   1 
ATOM   1383 C  CB  . HIS A 1 207 ? -14.187 11.182  9.043   1.00 35.94  ? 183 HIS A CB  1 
ATOM   1384 C  CG  . HIS A 1 207 ? -15.432 12.000  9.190   1.00 40.62  ? 183 HIS A CG  1 
ATOM   1385 N  ND1 . HIS A 1 207 ? -15.502 13.325  8.818   1.00 42.56  ? 183 HIS A ND1 1 
ATOM   1386 C  CD2 . HIS A 1 207 ? -16.655 11.681  9.675   1.00 42.28  ? 183 HIS A CD2 1 
ATOM   1387 C  CE1 . HIS A 1 207 ? -16.714 13.787  9.067   1.00 46.10  ? 183 HIS A CE1 1 
ATOM   1388 N  NE2 . HIS A 1 207 ? -17.435 12.809  9.586   1.00 45.06  ? 183 HIS A NE2 1 
ATOM   1389 N  N   . PHE A 1 208 ? -14.300 10.407  12.083  1.00 36.86  ? 184 PHE A N   1 
ATOM   1390 C  CA  . PHE A 1 208 ? -14.986 10.459  13.372  1.00 37.56  ? 184 PHE A CA  1 
ATOM   1391 C  C   . PHE A 1 208 ? -14.007 10.738  14.507  1.00 39.25  ? 184 PHE A C   1 
ATOM   1392 O  O   . PHE A 1 208 ? -14.340 11.447  15.464  1.00 40.78  ? 184 PHE A O   1 
ATOM   1393 C  CB  . PHE A 1 208 ? -15.735 9.151   13.624  1.00 37.37  ? 184 PHE A CB  1 
ATOM   1394 C  CG  . PHE A 1 208 ? -16.841 8.891   12.645  1.00 36.37  ? 184 PHE A CG  1 
ATOM   1395 C  CD1 . PHE A 1 208 ? -18.013 9.627   12.694  1.00 39.52  ? 184 PHE A CD1 1 
ATOM   1396 C  CD2 . PHE A 1 208 ? -16.712 7.909   11.679  1.00 35.75  ? 184 PHE A CD2 1 
ATOM   1397 C  CE1 . PHE A 1 208 ? -19.034 9.392   11.795  1.00 38.67  ? 184 PHE A CE1 1 
ATOM   1398 C  CE2 . PHE A 1 208 ? -17.732 7.668   10.777  1.00 36.61  ? 184 PHE A CE2 1 
ATOM   1399 C  CZ  . PHE A 1 208 ? -18.893 8.410   10.835  1.00 38.31  ? 184 PHE A CZ  1 
ATOM   1400 N  N   . TYR A 1 209 ? -12.796 10.187  14.412  1.00 37.68  ? 185 TYR A N   1 
ATOM   1401 C  CA  . TYR A 1 209 ? -11.769 10.436  15.419  1.00 39.88  ? 185 TYR A CA  1 
ATOM   1402 C  C   . TYR A 1 209 ? -11.418 11.917  15.495  1.00 42.67  ? 185 TYR A C   1 
ATOM   1403 O  O   . TYR A 1 209 ? -11.191 12.453  16.585  1.00 42.17  ? 185 TYR A O   1 
ATOM   1404 C  CB  . TYR A 1 209 ? -10.540 9.587   15.087  1.00 36.89  ? 185 TYR A CB  1 
ATOM   1405 C  CG  . TYR A 1 209 ? -9.333  9.759   15.983  1.00 42.21  ? 185 TYR A CG  1 
ATOM   1406 C  CD1 . TYR A 1 209 ? -9.359  9.356   17.313  1.00 42.81  ? 185 TYR A CD1 1 
ATOM   1407 C  CD2 . TYR A 1 209 ? -8.147  10.282  15.480  1.00 40.14  ? 185 TYR A CD2 1 
ATOM   1408 C  CE1 . TYR A 1 209 ? -8.244  9.496   18.123  1.00 42.84  ? 185 TYR A CE1 1 
ATOM   1409 C  CE2 . TYR A 1 209 ? -7.030  10.423  16.280  1.00 39.92  ? 185 TYR A CE2 1 
ATOM   1410 C  CZ  . TYR A 1 209 ? -7.083  10.029  17.599  1.00 43.59  ? 185 TYR A CZ  1 
ATOM   1411 O  OH  . TYR A 1 209 ? -5.969  10.170  18.392  1.00 43.52  ? 185 TYR A OH  1 
ATOM   1412 N  N   . ASP A 1 210 ? -11.383 12.598  14.347  1.00 40.01  ? 186 ASP A N   1 
ATOM   1413 C  CA  . ASP A 1 210 ? -11.079 14.024  14.337  1.00 42.64  ? 186 ASP A CA  1 
ATOM   1414 C  C   . ASP A 1 210 ? -12.242 14.869  14.836  1.00 43.50  ? 186 ASP A C   1 
ATOM   1415 O  O   . ASP A 1 210 ? -12.022 16.006  15.268  1.00 44.68  ? 186 ASP A O   1 
ATOM   1416 C  CB  . ASP A 1 210 ? -10.685 14.469  12.928  1.00 38.40  ? 186 ASP A CB  1 
ATOM   1417 C  CG  . ASP A 1 210 ? -9.279  14.046  12.556  1.00 44.52  ? 186 ASP A CG  1 
ATOM   1418 O  OD1 . ASP A 1 210 ? -8.540  13.573  13.446  1.00 43.73  ? 186 ASP A OD1 1 
ATOM   1419 O  OD2 . ASP A 1 210 ? -8.915  14.186  11.370  1.00 46.84  ? 186 ASP A OD2 1 
ATOM   1420 N  N   . ARG A 1 211 ? -13.466 14.350  14.779  1.00 44.16  ? 187 ARG A N   1 
ATOM   1421 C  CA  . ARG A 1 211 ? -14.623 15.016  15.359  1.00 44.35  ? 187 ARG A CA  1 
ATOM   1422 C  C   . ARG A 1 211 ? -14.804 14.693  16.836  1.00 45.82  ? 187 ARG A C   1 
ATOM   1423 O  O   . ARG A 1 211 ? -15.733 15.214  17.461  1.00 46.49  ? 187 ARG A O   1 
ATOM   1424 C  CB  . ARG A 1 211 ? -15.894 14.633  14.595  1.00 47.24  ? 187 ARG A CB  1 
ATOM   1425 C  CG  . ARG A 1 211 ? -15.991 15.233  13.201  1.00 48.29  ? 187 ARG A CG  1 
ATOM   1426 C  CD  . ARG A 1 211 ? -17.189 14.678  12.452  1.00 48.14  ? 187 ARG A CD  1 
ATOM   1427 N  NE  . ARG A 1 211 ? -18.432 14.866  13.192  1.00 58.38  ? 187 ARG A NE  1 
ATOM   1428 C  CZ  . ARG A 1 211 ? -19.564 14.224  12.932  1.00 55.55  ? 187 ARG A CZ  1 
ATOM   1429 N  NH1 . ARG A 1 211 ? -19.645 13.330  11.959  1.00 53.32  ? 187 ARG A NH1 1 
ATOM   1430 N  NH2 . ARG A 1 211 ? -20.640 14.483  13.669  1.00 53.34  ? 187 ARG A NH2 1 
ATOM   1431 N  N   . GLY A 1 212 ? -13.947 13.846  17.401  1.00 46.10  ? 188 GLY A N   1 
ATOM   1432 C  CA  . GLY A 1 212 ? -14.022 13.527  18.811  1.00 48.02  ? 188 GLY A CA  1 
ATOM   1433 C  C   . GLY A 1 212 ? -15.140 12.590  19.197  1.00 47.21  ? 188 GLY A C   1 
ATOM   1434 O  O   . GLY A 1 212 ? -15.461 12.488  20.384  1.00 48.98  ? 188 GLY A O   1 
ATOM   1435 N  N   . LEU A 1 213 ? -15.747 11.894  18.234  1.00 45.60  ? 189 LEU A N   1 
ATOM   1436 C  CA  . LEU A 1 213 ? -16.856 11.003  18.551  1.00 46.29  ? 189 LEU A CA  1 
ATOM   1437 C  C   . LEU A 1 213 ? -16.389 9.664   19.109  1.00 44.71  ? 189 LEU A C   1 
ATOM   1438 O  O   . LEU A 1 213 ? -17.194 8.949   19.713  1.00 46.52  ? 189 LEU A O   1 
ATOM   1439 C  CB  . LEU A 1 213 ? -17.726 10.787  17.310  1.00 45.92  ? 189 LEU A CB  1 
ATOM   1440 C  CG  . LEU A 1 213 ? -18.470 12.034  16.815  1.00 53.29  ? 189 LEU A CG  1 
ATOM   1441 C  CD1 . LEU A 1 213 ? -19.354 11.705  15.621  1.00 51.68  ? 189 LEU A CD1 1 
ATOM   1442 C  CD2 . LEU A 1 213 ? -19.299 12.665  17.929  1.00 52.56  ? 189 LEU A CD2 1 
ATOM   1443 N  N   . VAL A 1 214 ? -15.120 9.311   18.922  1.00 45.23  ? 190 VAL A N   1 
ATOM   1444 C  CA  . VAL A 1 214 ? -14.507 8.188   19.618  1.00 45.99  ? 190 VAL A CA  1 
ATOM   1445 C  C   . VAL A 1 214 ? -13.147 8.637   20.134  1.00 48.47  ? 190 VAL A C   1 
ATOM   1446 O  O   . VAL A 1 214 ? -12.460 9.450   19.507  1.00 48.34  ? 190 VAL A O   1 
ATOM   1447 C  CB  . VAL A 1 214 ? -14.366 6.933   18.725  1.00 41.57  ? 190 VAL A CB  1 
ATOM   1448 C  CG1 . VAL A 1 214 ? -15.726 6.292   18.495  1.00 41.08  ? 190 VAL A CG1 1 
ATOM   1449 C  CG2 . VAL A 1 214 ? -13.703 7.277   17.401  1.00 37.45  ? 190 VAL A CG2 1 
ATOM   1450 N  N   . LYS A 1 215 ? -12.766 8.106   21.290  1.00 45.80  ? 191 LYS A N   1 
ATOM   1451 C  CA  . LYS A 1 215 ? -11.522 8.460   21.953  1.00 46.13  ? 191 LYS A CA  1 
ATOM   1452 C  C   . LYS A 1 215 ? -10.578 7.265   21.966  1.00 44.31  ? 191 LYS A C   1 
ATOM   1453 O  O   . LYS A 1 215 ? -11.011 6.110   21.980  1.00 43.10  ? 191 LYS A O   1 
ATOM   1454 C  CB  . LYS A 1 215 ? -11.779 8.928   23.390  1.00 48.22  ? 191 LYS A CB  1 
ATOM   1455 C  CG  . LYS A 1 215 ? -12.616 10.198  23.505  1.00 55.27  ? 191 LYS A CG  1 
ATOM   1456 C  CD  . LYS A 1 215 ? -11.859 11.424  23.009  1.00 59.56  ? 191 LYS A CD  1 
ATOM   1457 C  CE  . LYS A 1 215 ? -12.539 12.716  23.448  1.00 65.12  ? 191 LYS A CE  1 
ATOM   1458 N  NZ  . LYS A 1 215 ? -13.940 12.824  22.952  1.00 65.36  ? 191 LYS A NZ  1 
ATOM   1459 N  N   . GLY A 1 216 ? -9.281  7.556   21.962  1.00 43.58  ? 192 GLY A N   1 
ATOM   1460 C  CA  . GLY A 1 216 ? -8.275  6.524   21.993  1.00 43.62  ? 192 GLY A CA  1 
ATOM   1461 C  C   . GLY A 1 216 ? -8.197  5.855   23.351  1.00 40.53  ? 192 GLY A C   1 
ATOM   1462 O  O   . GLY A 1 216 ? -8.737  6.354   24.341  1.00 40.59  ? 192 GLY A O   1 
ATOM   1463 N  N   . PRO A 1 217 ? -7.524  4.696   23.425  1.00 40.08  ? 193 PRO A N   1 
ATOM   1464 C  CA  . PRO A 1 217 ? -6.891  4.003   22.297  1.00 40.12  ? 193 PRO A CA  1 
ATOM   1465 C  C   . PRO A 1 217 ? -7.912  3.299   21.412  1.00 39.74  ? 193 PRO A C   1 
ATOM   1466 O  O   . PRO A 1 217 ? -8.790  2.606   21.926  1.00 40.23  ? 193 PRO A O   1 
ATOM   1467 C  CB  . PRO A 1 217 ? -5.972  2.991   22.982  1.00 40.17  ? 193 PRO A CB  1 
ATOM   1468 C  CG  . PRO A 1 217 ? -6.649  2.694   24.274  1.00 38.86  ? 193 PRO A CG  1 
ATOM   1469 C  CD  . PRO A 1 217 ? -7.341  3.964   24.692  1.00 37.93  ? 193 PRO A CD  1 
ATOM   1470 N  N   . LEU A 1 218 ? -7.801  3.488   20.100  1.00 39.35  ? 194 LEU A N   1 
ATOM   1471 C  CA  . LEU A 1 218 ? -8.730  2.874   19.164  1.00 35.55  ? 194 LEU A CA  1 
ATOM   1472 C  C   . LEU A 1 218 ? -8.314  1.436   18.892  1.00 35.55  ? 194 LEU A C   1 
ATOM   1473 O  O   . LEU A 1 218 ? -7.159  1.170   18.544  1.00 35.68  ? 194 LEU A O   1 
ATOM   1474 C  CB  . LEU A 1 218 ? -8.773  3.663   17.857  1.00 35.90  ? 194 LEU A CB  1 
ATOM   1475 C  CG  . LEU A 1 218 ? -8.981  5.172   17.972  1.00 37.32  ? 194 LEU A CG  1 
ATOM   1476 C  CD1 . LEU A 1 218 ? -8.838  5.816   16.603  1.00 36.32  ? 194 LEU A CD1 1 
ATOM   1477 C  CD2 . LEU A 1 218 ? -10.335 5.494   18.578  1.00 36.75  ? 194 LEU A CD2 1 
ATOM   1478 N  N   . PHE A 1 219 ? -9.256  0.511   19.053  1.00 33.88  ? 195 PHE A N   1 
ATOM   1479 C  CA  . PHE A 1 219 ? -9.033  -0.901  18.751  1.00 31.56  ? 195 PHE A CA  1 
ATOM   1480 C  C   . PHE A 1 219 ? -9.411  -1.118  17.290  1.00 34.79  ? 195 PHE A C   1 
ATOM   1481 O  O   . PHE A 1 219 ? -10.586 -1.293  16.958  1.00 32.40  ? 195 PHE A O   1 
ATOM   1482 C  CB  . PHE A 1 219 ? -9.852  -1.781  19.688  1.00 32.08  ? 195 PHE A CB  1 
ATOM   1483 C  CG  . PHE A 1 219 ? -9.464  -3.237  19.670  1.00 34.35  ? 195 PHE A CG  1 
ATOM   1484 C  CD1 . PHE A 1 219 ? -8.156  -3.630  19.427  1.00 32.25  ? 195 PHE A CD1 1 
ATOM   1485 C  CD2 . PHE A 1 219 ? -10.416 -4.215  19.909  1.00 34.83  ? 195 PHE A CD2 1 
ATOM   1486 C  CE1 . PHE A 1 219 ? -7.808  -4.969  19.420  1.00 36.58  ? 195 PHE A CE1 1 
ATOM   1487 C  CE2 . PHE A 1 219 ? -10.073 -5.554  19.902  1.00 37.17  ? 195 PHE A CE2 1 
ATOM   1488 C  CZ  . PHE A 1 219 ? -8.768  -5.931  19.655  1.00 34.93  ? 195 PHE A CZ  1 
ATOM   1489 N  N   . ILE A 1 220 ? -8.411  -1.101  16.413  1.00 31.48  ? 196 ILE A N   1 
ATOM   1490 C  CA  . ILE A 1 220 ? -8.623  -1.152  14.972  1.00 30.99  ? 196 ILE A CA  1 
ATOM   1491 C  C   . ILE A 1 220 ? -8.295  -2.555  14.487  1.00 31.47  ? 196 ILE A C   1 
ATOM   1492 O  O   . ILE A 1 220 ? -7.154  -3.016  14.618  1.00 31.83  ? 196 ILE A O   1 
ATOM   1493 C  CB  . ILE A 1 220 ? -7.767  -0.108  14.239  1.00 31.61  ? 196 ILE A CB  1 
ATOM   1494 C  CG1 . ILE A 1 220 ? -8.089  1.297   14.757  1.00 29.08  ? 196 ILE A CG1 1 
ATOM   1495 C  CG2 . ILE A 1 220 ? -7.988  -0.209  12.731  1.00 30.78  ? 196 ILE A CG2 1 
ATOM   1496 C  CD1 . ILE A 1 220 ? -7.323  2.403   14.061  1.00 29.55  ? 196 ILE A CD1 1 
ATOM   1497 N  N   . GLN A 1 221 ? -9.287  -3.230  13.918  1.00 29.19  ? 197 GLN A N   1 
ATOM   1498 C  CA  . GLN A 1 221 ? -9.101  -4.551  13.334  1.00 30.24  ? 197 GLN A CA  1 
ATOM   1499 C  C   . GLN A 1 221 ? -9.184  -4.436  11.819  1.00 30.56  ? 197 GLN A C   1 
ATOM   1500 O  O   . GLN A 1 221 ? -10.217 -4.025  11.277  1.00 31.32  ? 197 GLN A O   1 
ATOM   1501 C  CB  . GLN A 1 221 ? -10.137 -5.546  13.847  1.00 30.02  ? 197 GLN A CB  1 
ATOM   1502 C  CG  . GLN A 1 221 ? -9.921  -6.939  13.293  1.00 31.48  ? 197 GLN A CG  1 
ATOM   1503 C  CD  . GLN A 1 221 ? -10.310 -8.014  14.276  1.00 34.38  ? 197 GLN A CD  1 
ATOM   1504 O  OE1 . GLN A 1 221 ? -9.454  -8.611  14.929  1.00 37.37  ? 197 GLN A OE1 1 
ATOM   1505 N  NE2 . GLN A 1 221 ? -11.609 -8.267  14.393  1.00 36.35  ? 197 GLN A NE2 1 
ATOM   1506 N  N   . THR A 1 222 ? -8.097  -4.793  11.145  1.00 26.53  ? 198 THR A N   1 
ATOM   1507 C  CA  . THR A 1 222 ? -8.026  -4.769  9.692   1.00 28.92  ? 198 THR A CA  1 
ATOM   1508 C  C   . THR A 1 222 ? -8.319  -6.172  9.171   1.00 27.11  ? 198 THR A C   1 
ATOM   1509 O  O   . THR A 1 222 ? -7.637  -7.131  9.550   1.00 27.10  ? 198 THR A O   1 
ATOM   1510 C  CB  . THR A 1 222 ? -6.653  -4.272  9.232   1.00 25.73  ? 198 THR A CB  1 
ATOM   1511 O  OG1 . THR A 1 222 ? -5.621  -5.056  9.842   1.00 26.97  ? 198 THR A OG1 1 
ATOM   1512 C  CG2 . THR A 1 222 ? -6.462  -2.814  9.635   1.00 26.43  ? 198 THR A CG2 1 
ATOM   1513 N  N   . VAL A 1 223 ? -9.335  -6.285  8.314   1.00 23.51  ? 199 VAL A N   1 
ATOM   1514 C  CA  . VAL A 1 223 ? -9.884  -7.564  7.866   1.00 25.22  ? 199 VAL A CA  1 
ATOM   1515 C  C   . VAL A 1 223 ? -9.421  -7.829  6.440   1.00 26.80  ? 199 VAL A C   1 
ATOM   1516 O  O   . VAL A 1 223 ? -9.626  -6.995  5.549   1.00 28.43  ? 199 VAL A O   1 
ATOM   1517 C  CB  . VAL A 1 223 ? -11.422 -7.565  7.946   1.00 28.27  ? 199 VAL A CB  1 
ATOM   1518 C  CG1 . VAL A 1 223 ? -11.983 -8.908  7.506   1.00 26.88  ? 199 VAL A CG1 1 
ATOM   1519 C  CG2 . VAL A 1 223 ? -11.888 -7.222  9.353   1.00 26.43  ? 199 VAL A CG2 1 
ATOM   1520 N  N   . PHE A 1 224 ? -8.833  -9.004  6.216   1.00 27.16  ? 200 PHE A N   1 
ATOM   1521 C  CA  . PHE A 1 224 ? -8.174  -9.336  4.959   1.00 28.59  ? 200 PHE A CA  1 
ATOM   1522 C  C   . PHE A 1 224 ? -8.812  -10.562 4.325   1.00 28.25  ? 200 PHE A C   1 
ATOM   1523 O  O   . PHE A 1 224 ? -9.059  -11.562 5.008   1.00 29.02  ? 200 PHE A O   1 
ATOM   1524 C  CB  . PHE A 1 224 ? -6.681  -9.604  5.177   1.00 24.47  ? 200 PHE A CB  1 
ATOM   1525 C  CG  . PHE A 1 224 ? -5.937  -8.450  5.778   1.00 28.83  ? 200 PHE A CG  1 
ATOM   1526 C  CD1 . PHE A 1 224 ? -5.543  -7.383  4.992   1.00 25.14  ? 200 PHE A CD1 1 
ATOM   1527 C  CD2 . PHE A 1 224 ? -5.621  -8.437  7.126   1.00 24.59  ? 200 PHE A CD2 1 
ATOM   1528 C  CE1 . PHE A 1 224 ? -4.860  -6.321  5.538   1.00 27.88  ? 200 PHE A CE1 1 
ATOM   1529 C  CE2 . PHE A 1 224 ? -4.935  -7.375  7.680   1.00 26.49  ? 200 PHE A CE2 1 
ATOM   1530 C  CZ  . PHE A 1 224 ? -4.553  -6.317  6.886   1.00 25.86  ? 200 PHE A CZ  1 
ATOM   1531 N  N   . GLY A 1 225 ? -9.065  -10.487 3.018   1.00 27.74  ? 201 GLY A N   1 
ATOM   1532 C  CA  . GLY A 1 225 ? -9.403  -11.653 2.227   1.00 26.23  ? 201 GLY A CA  1 
ATOM   1533 C  C   . GLY A 1 225 ? -10.868 -11.834 1.890   1.00 30.51  ? 201 GLY A C   1 
ATOM   1534 O  O   . GLY A 1 225 ? -11.219 -12.857 1.288   1.00 32.63  ? 201 GLY A O   1 
ATOM   1535 N  N   . LEU A 1 226 ? -11.731 -10.891 2.248   1.00 29.45  ? 202 LEU A N   1 
ATOM   1536 C  CA  . LEU A 1 226 ? -13.145 -11.025 1.932   1.00 31.33  ? 202 LEU A CA  1 
ATOM   1537 C  C   . LEU A 1 226 ? -13.427 -10.539 0.518   1.00 30.70  ? 202 LEU A C   1 
ATOM   1538 O  O   . LEU A 1 226 ? -12.782 -9.615  0.013   1.00 29.97  ? 202 LEU A O   1 
ATOM   1539 C  CB  . LEU A 1 226 ? -14.003 -10.238 2.923   1.00 31.59  ? 202 LEU A CB  1 
ATOM   1540 C  CG  . LEU A 1 226 ? -13.912 -10.633 4.397   1.00 35.30  ? 202 LEU A CG  1 
ATOM   1541 C  CD1 . LEU A 1 226 ? -15.117 -10.094 5.153   1.00 34.18  ? 202 LEU A CD1 1 
ATOM   1542 C  CD2 . LEU A 1 226 ? -13.800 -12.139 4.562   1.00 37.11  ? 202 LEU A CD2 1 
ATOM   1543 N  N   . MET A 1 227 ? -14.404 -11.175 -0.125  1.00 31.21  ? 203 MET A N   1 
ATOM   1544 C  CA  . MET A 1 227 ? -14.869 -10.706 -1.423  1.00 34.03  ? 203 MET A CA  1 
ATOM   1545 C  C   . MET A 1 227 ? -15.724 -9.465  -1.201  1.00 33.87  ? 203 MET A C   1 
ATOM   1546 O  O   . MET A 1 227 ? -16.771 -9.533  -0.547  1.00 33.64  ? 203 MET A O   1 
ATOM   1547 C  CB  . MET A 1 227 ? -15.660 -11.786 -2.152  1.00 34.48  ? 203 MET A CB  1 
ATOM   1548 C  CG  . MET A 1 227 ? -15.810 -11.494 -3.629  1.00 41.59  ? 203 MET A CG  1 
ATOM   1549 S  SD  . MET A 1 227 ? -16.987 -12.566 -4.459  1.00 54.86  ? 203 MET A SD  1 
ATOM   1550 C  CE  . MET A 1 227 ? -16.802 -11.999 -6.147  1.00 53.87  ? 203 MET A CE  1 
ATOM   1551 N  N   . GLY A 1 228 ? -15.276 -8.338  -1.743  1.00 32.40  ? 204 GLY A N   1 
ATOM   1552 C  CA  . GLY A 1 228 ? -15.824 -7.039  -1.418  1.00 30.32  ? 204 GLY A CA  1 
ATOM   1553 C  C   . GLY A 1 228 ? -14.926 -6.219  -0.524  1.00 30.61  ? 204 GLY A C   1 
ATOM   1554 O  O   . GLY A 1 228 ? -15.175 -5.019  -0.351  1.00 30.83  ? 204 GLY A O   1 
ATOM   1555 N  N   . GLY A 1 229 ? -13.891 -6.830  0.050   1.00 31.09  ? 205 GLY A N   1 
ATOM   1556 C  CA  . GLY A 1 229 ? -12.911 -6.112  0.836   1.00 26.23  ? 205 GLY A CA  1 
ATOM   1557 C  C   . GLY A 1 229 ? -11.521 -6.212  0.243   1.00 27.31  ? 205 GLY A C   1 
ATOM   1558 O  O   . GLY A 1 229 ? -11.342 -6.694  -0.880  1.00 28.93  ? 205 GLY A O   1 
ATOM   1559 N  N   . ILE A 1 230 ? -10.522 -5.754  0.993   1.00 25.87  ? 206 ILE A N   1 
ATOM   1560 C  CA  . ILE A 1 230 ? -9.146  -5.859  0.537   1.00 26.04  ? 206 ILE A CA  1 
ATOM   1561 C  C   . ILE A 1 230 ? -8.694  -7.315  0.605   1.00 27.25  ? 206 ILE A C   1 
ATOM   1562 O  O   . ILE A 1 230 ? -9.220  -8.123  1.381   1.00 26.79  ? 206 ILE A O   1 
ATOM   1563 C  CB  . ILE A 1 230 ? -8.239  -4.945  1.380   1.00 26.08  ? 206 ILE A CB  1 
ATOM   1564 C  CG1 . ILE A 1 230 ? -6.874  -4.770  0.709   1.00 26.15  ? 206 ILE A CG1 1 
ATOM   1565 C  CG2 . ILE A 1 230 ? -8.080  -5.501  2.794   1.00 23.26  ? 206 ILE A CG2 1 
ATOM   1566 C  CD1 . ILE A 1 230 ? -6.000  -3.728  1.381   1.00 26.32  ? 206 ILE A CD1 1 
ATOM   1567 N  N   . GLY A 1 231 ? -7.716  -7.657  -0.226  1.00 29.05  ? 207 GLY A N   1 
ATOM   1568 C  CA  . GLY A 1 231 ? -7.196  -9.005  -0.262  1.00 26.31  ? 207 GLY A CA  1 
ATOM   1569 C  C   . GLY A 1 231 ? -6.313  -9.310  0.938   1.00 27.35  ? 207 GLY A C   1 
ATOM   1570 O  O   . GLY A 1 231 ? -6.245  -8.570  1.921   1.00 27.49  ? 207 GLY A O   1 
ATOM   1571 N  N   . ALA A 1 232 ? -5.615  -10.443 0.836   1.00 26.97  ? 208 ALA A N   1 
ATOM   1572 C  CA  . ALA A 1 232 ? -4.775  -10.955 1.913   1.00 30.85  ? 208 ALA A CA  1 
ATOM   1573 C  C   . ALA A 1 232 ? -3.307  -11.044 1.507   1.00 31.73  ? 208 ALA A C   1 
ATOM   1574 O  O   . ALA A 1 232 ? -2.545  -11.810 2.107   1.00 31.06  ? 208 ALA A O   1 
ATOM   1575 C  CB  . ALA A 1 232 ? -5.283  -12.324 2.370   1.00 30.25  ? 208 ALA A CB  1 
ATOM   1576 N  N   . HIS A 1 233 ? -2.898  -10.279 0.500   1.00 29.11  ? 209 HIS A N   1 
ATOM   1577 C  CA  . HIS A 1 233 ? -1.501  -10.248 0.100   1.00 30.12  ? 209 HIS A CA  1 
ATOM   1578 C  C   . HIS A 1 233 ? -0.688  -9.468  1.135   1.00 28.79  ? 209 HIS A C   1 
ATOM   1579 O  O   . HIS A 1 233 ? -1.195  -8.525  1.748   1.00 28.64  ? 209 HIS A O   1 
ATOM   1580 C  CB  . HIS A 1 233 ? -1.374  -9.604  -1.280  1.00 29.83  ? 209 HIS A CB  1 
ATOM   1581 C  CG  . HIS A 1 233 ? -0.017  -9.737  -1.898  1.00 34.43  ? 209 HIS A CG  1 
ATOM   1582 N  ND1 . HIS A 1 233 ? 0.987   -8.817  -1.693  1.00 35.02  ? 209 HIS A ND1 1 
ATOM   1583 C  CD2 . HIS A 1 233 ? 0.495   -10.671 -2.736  1.00 35.53  ? 209 HIS A CD2 1 
ATOM   1584 C  CE1 . HIS A 1 233 ? 2.064   -9.183  -2.364  1.00 34.87  ? 209 HIS A CE1 1 
ATOM   1585 N  NE2 . HIS A 1 233 ? 1.791   -10.304 -3.007  1.00 35.03  ? 209 HIS A NE2 1 
ATOM   1586 N  N   . PRO A 1 234 ? 0.572   -9.856  1.372   1.00 30.21  ? 210 PRO A N   1 
ATOM   1587 C  CA  . PRO A 1 234 ? 1.389   -9.105  2.343   1.00 28.34  ? 210 PRO A CA  1 
ATOM   1588 C  C   . PRO A 1 234 ? 1.434   -7.610  2.075   1.00 28.68  ? 210 PRO A C   1 
ATOM   1589 O  O   . PRO A 1 234 ? 1.490   -6.816  3.025   1.00 25.85  ? 210 PRO A O   1 
ATOM   1590 C  CB  . PRO A 1 234 ? 2.776   -9.748  2.200   1.00 30.13  ? 210 PRO A CB  1 
ATOM   1591 C  CG  . PRO A 1 234 ? 2.499   -11.139 1.745   1.00 29.28  ? 210 PRO A CG  1 
ATOM   1592 C  CD  . PRO A 1 234 ? 1.265   -11.064 0.884   1.00 29.70  ? 210 PRO A CD  1 
ATOM   1593 N  N   . ASP A 1 235 ? 1.421   -7.200  0.804   1.00 28.16  ? 211 ASP A N   1 
ATOM   1594 C  CA  . ASP A 1 235 ? 1.342   -5.778  0.484   1.00 30.67  ? 211 ASP A CA  1 
ATOM   1595 C  C   . ASP A 1 235 ? 0.078   -5.153  1.066   1.00 30.05  ? 211 ASP A C   1 
ATOM   1596 O  O   . ASP A 1 235 ? 0.104   -4.015  1.546   1.00 29.79  ? 211 ASP A O   1 
ATOM   1597 C  CB  . ASP A 1 235 ? 1.384   -5.575  -1.032  1.00 32.84  ? 211 ASP A CB  1 
ATOM   1598 C  CG  . ASP A 1 235 ? 2.775   -5.755  -1.615  1.00 43.77  ? 211 ASP A CG  1 
ATOM   1599 O  OD1 . ASP A 1 235 ? 3.768   -5.564  -0.879  1.00 40.11  ? 211 ASP A OD1 1 
ATOM   1600 O  OD2 . ASP A 1 235 ? 2.870   -6.075  -2.821  1.00 47.97  ? 211 ASP A OD2 1 
ATOM   1601 N  N   . ASP A 1 236 ? -1.041  -5.881  1.026   1.00 27.45  ? 212 ASP A N   1 
ATOM   1602 C  CA  . ASP A 1 236 ? -2.279  -5.361  1.600   1.00 28.65  ? 212 ASP A CA  1 
ATOM   1603 C  C   . ASP A 1 236 ? -2.144  -5.169  3.104   1.00 28.48  ? 212 ASP A C   1 
ATOM   1604 O  O   . ASP A 1 236 ? -2.569  -4.143  3.649   1.00 27.58  ? 212 ASP A O   1 
ATOM   1605 C  CB  . ASP A 1 236 ? -3.443  -6.300  1.289   1.00 26.02  ? 212 ASP A CB  1 
ATOM   1606 C  CG  . ASP A 1 236 ? -3.712  -6.425  -0.196  1.00 27.32  ? 212 ASP A CG  1 
ATOM   1607 O  OD1 . ASP A 1 236 ? -3.561  -5.417  -0.914  1.00 29.88  ? 212 ASP A OD1 1 
ATOM   1608 O  OD2 . ASP A 1 236 ? -4.076  -7.533  -0.641  1.00 27.64  ? 212 ASP A OD2 1 
ATOM   1609 N  N   . VAL A 1 237 ? -1.555  -6.150  3.791   1.00 26.27  ? 213 VAL A N   1 
ATOM   1610 C  CA  . VAL A 1 237 ? -1.350  -6.035  5.232   1.00 26.36  ? 213 VAL A CA  1 
ATOM   1611 C  C   . VAL A 1 237 ? -0.519  -4.799  5.553   1.00 27.98  ? 213 VAL A C   1 
ATOM   1612 O  O   . VAL A 1 237 ? -0.905  -3.966  6.381   1.00 27.97  ? 213 VAL A O   1 
ATOM   1613 C  CB  . VAL A 1 237 ? -0.690  -7.312  5.784   1.00 29.78  ? 213 VAL A CB  1 
ATOM   1614 C  CG1 . VAL A 1 237 ? -0.514  -7.210  7.291   1.00 26.86  ? 213 VAL A CG1 1 
ATOM   1615 C  CG2 . VAL A 1 237 ? -1.510  -8.543  5.416   1.00 27.00  ? 213 VAL A CG2 1 
ATOM   1616 N  N   . LEU A 1 238 ? 0.639   -4.662  4.902   1.00 30.86  ? 214 LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 238 ? 1.544   -3.532  5.215   1.00 29.76  ? 214 LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 238 ? 0.858   -2.209  4.863   1.00 31.34  ? 214 LEU A C   1 
ATOM   1619 O  O   . LEU A 1 238 ? 1.049   -1.213  5.572   1.00 28.57  ? 214 LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 238 ? 2.848   -3.709  4.439   1.00 34.56  ? 214 LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 238 ? 4.070   -4.041  5.293   1.00 41.09  ? 214 LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 238 ? 4.376   -2.902  6.252   1.00 36.95  ? 214 LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 238 ? 3.849   -5.335  6.060   1.00 35.47  ? 214 LEU A CD2 1 
ATOM   1624 N  N   . HIS A 1 239 ? 0.079   -2.171  3.780   1.00 28.68  ? 215 HIS A N   1 
ATOM   1625 C  CA  . HIS A 1 239 ? -0.592  -0.932  3.401   1.00 30.14  ? 215 HIS A CA  1 
ATOM   1626 C  C   . HIS A 1 239 ? -1.558  -0.481  4.489   1.00 29.65  ? 215 HIS A C   1 
ATOM   1627 O  O   . HIS A 1 239 ? -1.579  0.697   4.867   1.00 31.45  ? 215 HIS A O   1 
ATOM   1628 C  CB  . HIS A 1 239 ? -1.322  -1.116  2.072   1.00 31.94  ? 215 HIS A CB  1 
ATOM   1629 C  CG  . HIS A 1 239 ? -2.252  0.008   1.738   1.00 32.47  ? 215 HIS A CG  1 
ATOM   1630 N  ND1 . HIS A 1 239 ? -1.810  1.286   1.471   1.00 31.88  ? 215 HIS A ND1 1 
ATOM   1631 C  CD2 . HIS A 1 239 ? -3.602  0.049   1.642   1.00 32.60  ? 215 HIS A CD2 1 
ATOM   1632 C  CE1 . HIS A 1 239 ? -2.847  2.064   1.217   1.00 32.59  ? 215 HIS A CE1 1 
ATOM   1633 N  NE2 . HIS A 1 239 ? -3.946  1.338   1.315   1.00 31.43  ? 215 HIS A NE2 1 
ATOM   1634 N  N   . MET A 1 240 ? -2.371  -1.406  5.007   1.00 27.96  ? 216 MET A N   1 
ATOM   1635 C  CA  . MET A 1 240 ? -3.311  -1.048  6.067   1.00 29.98  ? 216 MET A CA  1 
ATOM   1636 C  C   . MET A 1 240 ? -2.574  -0.637  7.336   1.00 29.94  ? 216 MET A C   1 
ATOM   1637 O  O   . MET A 1 240 ? -2.948  0.345   7.989   1.00 27.95  ? 216 MET A O   1 
ATOM   1638 C  CB  . MET A 1 240 ? -4.258  -2.216  6.348   1.00 24.84  ? 216 MET A CB  1 
ATOM   1639 C  CG  . MET A 1 240 ? -5.164  -2.588  5.175   1.00 23.98  ? 216 MET A CG  1 
ATOM   1640 S  SD  . MET A 1 240 ? -6.460  -1.371  4.826   1.00 27.73  ? 216 MET A SD  1 
ATOM   1641 C  CE  . MET A 1 240 ? -7.477  -1.521  6.294   1.00 31.56  ? 216 MET A CE  1 
ATOM   1642 N  N   . LYS A 1 241 ? -1.525  -1.376  7.703   1.00 26.55  ? 217 LYS A N   1 
ATOM   1643 C  CA  . LYS A 1 241 ? -0.737  -1.014  8.876   1.00 29.26  ? 217 LYS A CA  1 
ATOM   1644 C  C   . LYS A 1 241 ? -0.107  0.359   8.696   1.00 29.61  ? 217 LYS A C   1 
ATOM   1645 O  O   . LYS A 1 241 ? -0.181  1.216   9.584   1.00 31.24  ? 217 LYS A O   1 
ATOM   1646 C  CB  . LYS A 1 241 ? 0.339   -2.072  9.125   1.00 30.39  ? 217 LYS A CB  1 
ATOM   1647 C  CG  . LYS A 1 241 ? 1.308   -1.735  10.250  1.00 29.86  ? 217 LYS A CG  1 
ATOM   1648 C  CD  . LYS A 1 241 ? 0.578   -1.490  11.559  1.00 32.20  ? 217 LYS A CD  1 
ATOM   1649 C  CE  . LYS A 1 241 ? 1.510   -1.641  12.755  1.00 35.07  ? 217 LYS A CE  1 
ATOM   1650 N  NZ  . LYS A 1 241 ? 2.623   -0.646  12.763  1.00 31.89  ? 217 LYS A NZ  1 
ATOM   1651 N  N   . ARG A 1 242 ? 0.519   0.579   7.540   1.00 30.97  ? 218 ARG A N   1 
ATOM   1652 C  CA  . ARG A 1 242 ? 1.143   1.863   7.246   1.00 30.15  ? 218 ARG A CA  1 
ATOM   1653 C  C   . ARG A 1 242 ? 0.129   2.996   7.336   1.00 31.20  ? 218 ARG A C   1 
ATOM   1654 O  O   . ARG A 1 242 ? 0.395   4.038   7.947   1.00 33.15  ? 218 ARG A O   1 
ATOM   1655 C  CB  . ARG A 1 242 ? 1.772   1.796   5.853   1.00 35.95  ? 218 ARG A CB  1 
ATOM   1656 C  CG  . ARG A 1 242 ? 2.676   2.944   5.487   1.00 43.99  ? 218 ARG A CG  1 
ATOM   1657 C  CD  . ARG A 1 242 ? 3.220   2.767   4.073   1.00 42.74  ? 218 ARG A CD  1 
ATOM   1658 N  NE  . ARG A 1 242 ? 3.895   1.484   3.893   1.00 44.10  ? 218 ARG A NE  1 
ATOM   1659 C  CZ  . ARG A 1 242 ? 3.492   0.509   3.083   1.00 46.65  ? 218 ARG A CZ  1 
ATOM   1660 N  NH1 . ARG A 1 242 ? 2.430   0.643   2.302   1.00 42.84  ? 218 ARG A NH1 1 
ATOM   1661 N  NH2 . ARG A 1 242 ? 4.179   -0.630  3.049   1.00 44.51  ? 218 ARG A NH2 1 
ATOM   1662 N  N   . THR A 1 243 ? -1.049  2.804   6.739   1.00 29.97  ? 219 THR A N   1 
ATOM   1663 C  CA  . THR A 1 243 ? -2.066  3.851   6.745   1.00 32.80  ? 219 THR A CA  1 
ATOM   1664 C  C   . THR A 1 243 ? -2.551  4.134   8.162   1.00 30.89  ? 219 THR A C   1 
ATOM   1665 O  O   . THR A 1 243 ? -2.687  5.294   8.566   1.00 27.44  ? 219 THR A O   1 
ATOM   1666 C  CB  . THR A 1 243 ? -3.237  3.445   5.848   1.00 32.02  ? 219 THR A CB  1 
ATOM   1667 O  OG1 . THR A 1 243 ? -2.756  3.130   4.535   1.00 31.45  ? 219 THR A OG1 1 
ATOM   1668 C  CG2 . THR A 1 243 ? -4.247  4.575   5.751   1.00 29.76  ? 219 THR A CG2 1 
ATOM   1669 N  N   . ALA A 1 244 ? -2.821  3.079   8.934   1.00 30.51  ? 220 ALA A N   1 
ATOM   1670 C  CA  . ALA A 1 244 ? -3.243  3.268   10.319  1.00 30.22  ? 220 ALA A CA  1 
ATOM   1671 C  C   . ALA A 1 244 ? -2.185  4.024   11.113  1.00 29.83  ? 220 ALA A C   1 
ATOM   1672 O  O   . ALA A 1 244 ? -2.502  4.954   11.863  1.00 30.76  ? 220 ALA A O   1 
ATOM   1673 C  CB  . ALA A 1 244 ? -3.539  1.916   10.967  1.00 28.33  ? 220 ALA A CB  1 
ATOM   1674 N  N   . ASP A 1 245 ? -0.917  3.629   10.966  1.00 31.06  ? 221 ASP A N   1 
ATOM   1675 C  CA  . ASP A 1 245 ? 0.169   4.344   11.630  1.00 31.60  ? 221 ASP A CA  1 
ATOM   1676 C  C   . ASP A 1 245 ? 0.105   5.837   11.328  1.00 31.25  ? 221 ASP A C   1 
ATOM   1677 O  O   . ASP A 1 245 ? 0.189   6.673   12.234  1.00 30.50  ? 221 ASP A O   1 
ATOM   1678 C  CB  . ASP A 1 245 ? 1.520   3.776   11.189  1.00 31.72  ? 221 ASP A CB  1 
ATOM   1679 C  CG  . ASP A 1 245 ? 1.835   2.438   11.832  1.00 34.55  ? 221 ASP A CG  1 
ATOM   1680 O  OD1 . ASP A 1 245 ? 1.140   2.056   12.795  1.00 33.94  ? 221 ASP A OD1 1 
ATOM   1681 O  OD2 . ASP A 1 245 ? 2.784   1.770   11.369  1.00 36.54  ? 221 ASP A OD2 1 
ATOM   1682 N  N   . ARG A 1 246 ? -0.047  6.187   10.050  1.00 30.58  ? 222 ARG A N   1 
ATOM   1683 C  CA  . ARG A 1 246 ? 0.005   7.590   9.654   1.00 32.44  ? 222 ARG A CA  1 
ATOM   1684 C  C   . ARG A 1 246 ? -1.219  8.353   10.145  1.00 30.68  ? 222 ARG A C   1 
ATOM   1685 O  O   . ARG A 1 246 ? -1.114  9.525   10.521  1.00 30.84  ? 222 ARG A O   1 
ATOM   1686 C  CB  . ARG A 1 246 ? 0.130   7.692   8.134   1.00 32.58  ? 222 ARG A CB  1 
ATOM   1687 C  CG  . ARG A 1 246 ? -0.003  9.103   7.586   1.00 35.64  ? 222 ARG A CG  1 
ATOM   1688 C  CD  . ARG A 1 246 ? 0.371   9.154   6.114   1.00 39.46  ? 222 ARG A CD  1 
ATOM   1689 N  NE  . ARG A 1 246 ? -0.400  8.198   5.328   1.00 35.22  ? 222 ARG A NE  1 
ATOM   1690 C  CZ  . ARG A 1 246 ? -1.611  8.432   4.841   1.00 37.68  ? 222 ARG A CZ  1 
ATOM   1691 N  NH1 . ARG A 1 246 ? -2.232  9.581   5.054   1.00 38.68  ? 222 ARG A NH1 1 
ATOM   1692 N  NH2 . ARG A 1 246 ? -2.214  7.491   4.120   1.00 38.19  ? 222 ARG A NH2 1 
ATOM   1693 N  N   . LEU A 1 247 ? -2.386  7.707   10.160  1.00 30.77  ? 223 LEU A N   1 
ATOM   1694 C  CA  . LEU A 1 247 ? -3.607  8.423   10.514  1.00 32.56  ? 223 LEU A CA  1 
ATOM   1695 C  C   . LEU A 1 247 ? -3.825  8.508   12.021  1.00 32.78  ? 223 LEU A C   1 
ATOM   1696 O  O   . LEU A 1 247 ? -4.434  9.473   12.496  1.00 34.60  ? 223 LEU A O   1 
ATOM   1697 C  CB  . LEU A 1 247 ? -4.822  7.759   9.857   1.00 30.64  ? 223 LEU A CB  1 
ATOM   1698 C  CG  . LEU A 1 247 ? -4.865  7.724   8.325   1.00 32.35  ? 223 LEU A CG  1 
ATOM   1699 C  CD1 . LEU A 1 247 ? -6.197  7.165   7.841   1.00 26.08  ? 223 LEU A CD1 1 
ATOM   1700 C  CD2 . LEU A 1 247 ? -4.613  9.105   7.732   1.00 34.59  ? 223 LEU A CD2 1 
ATOM   1701 N  N   . PHE A 1 248 ? -3.344  7.526   12.789  1.00 29.27  ? 224 PHE A N   1 
ATOM   1702 C  CA  . PHE A 1 248 ? -3.663  7.448   14.210  1.00 33.22  ? 224 PHE A CA  1 
ATOM   1703 C  C   . PHE A 1 248 ? -2.447  7.371   15.122  1.00 33.92  ? 224 PHE A C   1 
ATOM   1704 O  O   . PHE A 1 248 ? -2.621  7.401   16.347  1.00 36.24  ? 224 PHE A O   1 
ATOM   1705 C  CB  . PHE A 1 248 ? -4.570  6.236   14.480  1.00 31.64  ? 224 PHE A CB  1 
ATOM   1706 C  CG  . PHE A 1 248 ? -5.801  6.200   13.615  1.00 28.23  ? 224 PHE A CG  1 
ATOM   1707 C  CD1 . PHE A 1 248 ? -6.859  7.058   13.859  1.00 31.88  ? 224 PHE A CD1 1 
ATOM   1708 C  CD2 . PHE A 1 248 ? -5.897  5.309   12.561  1.00 27.27  ? 224 PHE A CD2 1 
ATOM   1709 C  CE1 . PHE A 1 248 ? -7.991  7.028   13.066  1.00 33.09  ? 224 PHE A CE1 1 
ATOM   1710 C  CE2 . PHE A 1 248 ? -7.026  5.275   11.765  1.00 30.26  ? 224 PHE A CE2 1 
ATOM   1711 C  CZ  . PHE A 1 248 ? -8.073  6.136   12.017  1.00 30.02  ? 224 PHE A CZ  1 
ATOM   1712 N  N   . GLY A 1 249 ? -1.237  7.274   14.580  1.00 32.94  ? 225 GLY A N   1 
ATOM   1713 C  CA  . GLY A 1 249 ? -0.047  7.333   15.417  1.00 37.87  ? 225 GLY A CA  1 
ATOM   1714 C  C   . GLY A 1 249 ? -0.039  6.248   16.478  1.00 39.96  ? 225 GLY A C   1 
ATOM   1715 O  O   . GLY A 1 249 ? -0.259  5.064   16.196  1.00 40.32  ? 225 GLY A O   1 
ATOM   1716 N  N   . GLN A 1 250 ? 0.222   6.656   17.718  1.00 39.81  ? 226 GLN A N   1 
ATOM   1717 C  CA  . GLN A 1 250 ? 0.292   5.750   18.856  1.00 45.21  ? 226 GLN A CA  1 
ATOM   1718 C  C   . GLN A 1 250 ? -1.059  5.529   19.523  1.00 43.06  ? 226 GLN A C   1 
ATOM   1719 O  O   . GLN A 1 250 ? -1.148  4.726   20.458  1.00 44.65  ? 226 GLN A O   1 
ATOM   1720 C  CB  . GLN A 1 250 ? 1.280   6.293   19.897  1.00 49.47  ? 226 GLN A CB  1 
ATOM   1721 C  CG  . GLN A 1 250 ? 2.713   6.414   19.404  1.00 57.74  ? 226 GLN A CG  1 
ATOM   1722 C  CD  . GLN A 1 250 ? 3.469   5.102   19.474  1.00 67.66  ? 226 GLN A CD  1 
ATOM   1723 O  OE1 . GLN A 1 250 ? 3.418   4.396   20.483  1.00 75.56  ? 226 GLN A OE1 1 
ATOM   1724 N  NE2 . GLN A 1 250 ? 4.174   4.768   18.400  1.00 69.11  ? 226 GLN A NE2 1 
ATOM   1725 N  N   . ASP A 1 251 ? -2.108  6.215   19.068  1.00 40.14  ? 227 ASP A N   1 
ATOM   1726 C  CA  . ASP A 1 251 ? -3.397  6.219   19.747  1.00 39.47  ? 227 ASP A CA  1 
ATOM   1727 C  C   . ASP A 1 251 ? -4.306  5.077   19.302  1.00 39.51  ? 227 ASP A C   1 
ATOM   1728 O  O   . ASP A 1 251 ? -5.536  5.203   19.392  1.00 37.42  ? 227 ASP A O   1 
ATOM   1729 C  CB  . ASP A 1 251 ? -4.089  7.566   19.527  1.00 41.67  ? 227 ASP A CB  1 
ATOM   1730 C  CG  . ASP A 1 251 ? -5.104  7.889   20.608  1.00 44.80  ? 227 ASP A CG  1 
ATOM   1731 O  OD1 . ASP A 1 251 ? -5.051  7.263   21.687  1.00 45.58  ? 227 ASP A OD1 1 
ATOM   1732 O  OD2 . ASP A 1 251 ? -5.957  8.773   20.377  1.00 45.76  ? 227 ASP A OD2 1 
ATOM   1733 N  N   . TYR A 1 252 ? -3.744  3.965   18.826  1.00 36.34  ? 228 TYR A N   1 
ATOM   1734 C  CA  . TYR A 1 252 ? -4.561  2.830   18.422  1.00 36.71  ? 228 TYR A CA  1 
ATOM   1735 C  C   . TYR A 1 252 ? -3.835  1.531   18.741  1.00 34.40  ? 228 TYR A C   1 
ATOM   1736 O  O   . TYR A 1 252 ? -2.612  1.497   18.898  1.00 33.35  ? 228 TYR A O   1 
ATOM   1737 C  CB  . TYR A 1 252 ? -4.924  2.896   16.928  1.00 32.59  ? 228 TYR A CB  1 
ATOM   1738 C  CG  . TYR A 1 252 ? -3.897  2.318   15.973  1.00 31.44  ? 228 TYR A CG  1 
ATOM   1739 C  CD1 . TYR A 1 252 ? -2.745  3.021   15.641  1.00 33.43  ? 228 TYR A CD1 1 
ATOM   1740 C  CD2 . TYR A 1 252 ? -4.099  1.080   15.378  1.00 32.20  ? 228 TYR A CD2 1 
ATOM   1741 C  CE1 . TYR A 1 252 ? -1.813  2.496   14.759  1.00 31.62  ? 228 TYR A CE1 1 
ATOM   1742 C  CE2 . TYR A 1 252 ? -3.179  0.551   14.496  1.00 32.34  ? 228 TYR A CE2 1 
ATOM   1743 C  CZ  . TYR A 1 252 ? -2.041  1.261   14.188  1.00 34.83  ? 228 TYR A CZ  1 
ATOM   1744 O  OH  . TYR A 1 252 ? -1.132  0.721   13.310  1.00 34.41  ? 228 TYR A OH  1 
ATOM   1745 N  N   . ARG A 1 253 ? -4.622  0.465   18.865  1.00 33.68  ? 229 ARG A N   1 
ATOM   1746 C  CA  . ARG A 1 253 ? -4.126  -0.897  19.005  1.00 32.53  ? 229 ARG A CA  1 
ATOM   1747 C  C   . ARG A 1 253 ? -4.579  -1.680  17.783  1.00 31.75  ? 229 ARG A C   1 
ATOM   1748 O  O   . ARG A 1 253 ? -5.749  -1.600  17.393  1.00 34.01  ? 229 ARG A O   1 
ATOM   1749 C  CB  . ARG A 1 253 ? -4.648  -1.568  20.280  1.00 33.00  ? 229 ARG A CB  1 
ATOM   1750 C  CG  . ARG A 1 253 ? -4.509  -0.739  21.549  1.00 36.50  ? 229 ARG A CG  1 
ATOM   1751 C  CD  . ARG A 1 253 ? -3.103  -0.784  22.117  1.00 36.61  ? 229 ARG A CD  1 
ATOM   1752 N  NE  . ARG A 1 253 ? -3.009  -0.032  23.364  1.00 42.05  ? 229 ARG A NE  1 
ATOM   1753 C  CZ  . ARG A 1 253 ? -2.701  1.257   23.449  1.00 47.79  ? 229 ARG A CZ  1 
ATOM   1754 N  NH1 . ARG A 1 253 ? -2.416  1.975   22.373  1.00 44.03  ? 229 ARG A NH1 1 
ATOM   1755 N  NH2 . ARG A 1 253 ? -2.680  1.841   24.644  1.00 48.80  ? 229 ARG A NH2 1 
ATOM   1756 N  N   . TRP A 1 254 ? -3.660  -2.430  17.189  1.00 31.23  ? 230 TRP A N   1 
ATOM   1757 C  CA  . TRP A 1 254 ? -3.880  -3.088  15.909  1.00 30.16  ? 230 TRP A CA  1 
ATOM   1758 C  C   . TRP A 1 254 ? -4.229  -4.555  16.119  1.00 30.39  ? 230 TRP A C   1 
ATOM   1759 O  O   . TRP A 1 254 ? -3.538  -5.266  16.856  1.00 32.44  ? 230 TRP A O   1 
ATOM   1760 C  CB  . TRP A 1 254 ? -2.629  -2.967  15.037  1.00 28.38  ? 230 TRP A CB  1 
ATOM   1761 C  CG  . TRP A 1 254 ? -2.765  -3.523  13.652  1.00 28.61  ? 230 TRP A CG  1 
ATOM   1762 C  CD1 . TRP A 1 254 ? -3.874  -3.495  12.855  1.00 28.29  ? 230 TRP A CD1 1 
ATOM   1763 C  CD2 . TRP A 1 254 ? -1.746  -4.191  12.899  1.00 26.66  ? 230 TRP A CD2 1 
ATOM   1764 N  NE1 . TRP A 1 254 ? -3.605  -4.104  11.651  1.00 24.99  ? 230 TRP A NE1 1 
ATOM   1765 C  CE2 . TRP A 1 254 ? -2.306  -4.540  11.654  1.00 28.29  ? 230 TRP A CE2 1 
ATOM   1766 C  CE3 . TRP A 1 254 ? -0.415  -4.529  13.159  1.00 27.68  ? 230 TRP A CE3 1 
ATOM   1767 C  CZ2 . TRP A 1 254 ? -1.579  -5.210  10.672  1.00 25.94  ? 230 TRP A CZ2 1 
ATOM   1768 C  CZ3 . TRP A 1 254 ? 0.303   -5.196  12.184  1.00 28.60  ? 230 TRP A CZ3 1 
ATOM   1769 C  CH2 . TRP A 1 254 ? -0.280  -5.527  10.955  1.00 27.03  ? 230 TRP A CH2 1 
ATOM   1770 N  N   . SER A 1 255 ? -5.302  -5.001  15.473  1.00 30.71  ? 231 SER A N   1 
ATOM   1771 C  CA  . SER A 1 255 ? -5.624  -6.416  15.377  1.00 30.55  ? 231 SER A CA  1 
ATOM   1772 C  C   . SER A 1 255 ? -5.877  -6.753  13.915  1.00 29.37  ? 231 SER A C   1 
ATOM   1773 O  O   . SER A 1 255 ? -6.217  -5.882  13.110  1.00 27.31  ? 231 SER A O   1 
ATOM   1774 C  CB  . SER A 1 255 ? -6.845  -6.787  16.229  1.00 28.83  ? 231 SER A CB  1 
ATOM   1775 O  OG  . SER A 1 255 ? -7.015  -8.193  16.274  1.00 30.05  ? 231 SER A OG  1 
ATOM   1776 N  N   . VAL A 1 256 ? -5.697  -8.028  13.570  1.00 26.29  ? 232 VAL A N   1 
ATOM   1777 C  CA  . VAL A 1 256 ? -5.860  -8.478  12.196  1.00 25.98  ? 232 VAL A CA  1 
ATOM   1778 C  C   . VAL A 1 256 ? -6.770  -9.691  12.155  1.00 27.82  ? 232 VAL A C   1 
ATOM   1779 O  O   . VAL A 1 256 ? -6.865  -10.467 13.113  1.00 25.24  ? 232 VAL A O   1 
ATOM   1780 C  CB  . VAL A 1 256 ? -4.515  -8.820  11.514  1.00 26.35  ? 232 VAL A CB  1 
ATOM   1781 C  CG1 . VAL A 1 256 ? -3.610  -7.603  11.480  1.00 24.59  ? 232 VAL A CG1 1 
ATOM   1782 C  CG2 . VAL A 1 256 ? -3.841  -10.002 12.209  1.00 24.77  ? 232 VAL A CG2 1 
ATOM   1783 N  N   . LEU A 1 257 ? -7.426  -9.855  11.011  1.00 24.89  ? 233 LEU A N   1 
ATOM   1784 C  CA  . LEU A 1 257 ? -8.268  -11.005 10.727  1.00 28.18  ? 233 LEU A CA  1 
ATOM   1785 C  C   . LEU A 1 257 ? -7.928  -11.481 9.326   1.00 29.25  ? 233 LEU A C   1 
ATOM   1786 O  O   . LEU A 1 257 ? -8.117  -10.741 8.355   1.00 28.20  ? 233 LEU A O   1 
ATOM   1787 C  CB  . LEU A 1 257 ? -9.750  -10.637 10.842  1.00 26.72  ? 233 LEU A CB  1 
ATOM   1788 C  CG  . LEU A 1 257 ? -10.824 -11.713 10.700  1.00 30.98  ? 233 LEU A CG  1 
ATOM   1789 C  CD1 . LEU A 1 257 ? -12.167 -11.089 11.026  1.00 28.46  ? 233 LEU A CD1 1 
ATOM   1790 C  CD2 . LEU A 1 257 ? -10.850 -12.332 9.309   1.00 30.17  ? 233 LEU A CD2 1 
ATOM   1791 N  N   . GLY A 1 258 ? -7.412  -12.701 9.226   1.00 27.90  ? 234 GLY A N   1 
ATOM   1792 C  CA  . GLY A 1 258 ? -7.145  -13.303 7.937   1.00 27.26  ? 234 GLY A CA  1 
ATOM   1793 C  C   . GLY A 1 258 ? -8.155  -14.386 7.622   1.00 30.46  ? 234 GLY A C   1 
ATOM   1794 O  O   . GLY A 1 258 ? -8.337  -15.322 8.406   1.00 30.33  ? 234 GLY A O   1 
ATOM   1795 N  N   . ALA A 1 259 ? -8.825  -14.269 6.483   1.00 30.09  ? 235 ALA A N   1 
ATOM   1796 C  CA  . ALA A 1 259 ? -9.885  -15.200 6.135   1.00 33.06  ? 235 ALA A CA  1 
ATOM   1797 C  C   . ALA A 1 259 ? -9.308  -16.522 5.646   1.00 33.01  ? 235 ALA A C   1 
ATOM   1798 O  O   . ALA A 1 259 ? -8.276  -16.556 4.971   1.00 34.86  ? 235 ALA A O   1 
ATOM   1799 C  CB  . ALA A 1 259 ? -10.784 -14.595 5.058   1.00 29.56  ? 235 ALA A CB  1 
ATOM   1800 N  N   . GLY A 1 260 ? -9.984  -17.611 5.996   1.00 30.47  ? 236 GLY A N   1 
ATOM   1801 C  CA  . GLY A 1 260 ? -9.612  -18.912 5.466   1.00 31.99  ? 236 GLY A CA  1 
ATOM   1802 C  C   . GLY A 1 260 ? -8.187  -19.284 5.813   1.00 34.59  ? 236 GLY A C   1 
ATOM   1803 O  O   . GLY A 1 260 ? -7.732  -19.136 6.953   1.00 31.99  ? 236 GLY A O   1 
ATOM   1804 N  N   . ARG A 1 261 ? -7.465  -19.781 4.815   1.00 33.96  ? 237 ARG A N   1 
ATOM   1805 C  CA  . ARG A 1 261 ? -6.118  -20.287 5.029   1.00 39.45  ? 237 ARG A CA  1 
ATOM   1806 C  C   . ARG A 1 261 ? -5.082  -19.183 5.195   1.00 33.45  ? 237 ARG A C   1 
ATOM   1807 O  O   . ARG A 1 261 ? -3.910  -19.493 5.427   1.00 36.08  ? 237 ARG A O   1 
ATOM   1808 C  CB  . ARG A 1 261 ? -5.718  -21.208 3.875   1.00 43.57  ? 237 ARG A CB  1 
ATOM   1809 C  CG  . ARG A 1 261 ? -5.735  -20.555 2.505   1.00 44.25  ? 237 ARG A CG  1 
ATOM   1810 C  CD  . ARG A 1 261 ? -5.341  -21.557 1.438   1.00 52.83  ? 237 ARG A CD  1 
ATOM   1811 N  NE  . ARG A 1 261 ? -4.094  -22.228 1.786   1.00 60.51  ? 237 ARG A NE  1 
ATOM   1812 C  CZ  . ARG A 1 261 ? -3.650  -23.340 1.216   1.00 61.60  ? 237 ARG A CZ  1 
ATOM   1813 N  NH1 . ARG A 1 261 ? -4.325  -23.939 0.247   1.00 56.64  ? 237 ARG A NH1 1 
ATOM   1814 N  NH2 . ARG A 1 261 ? -2.502  -23.867 1.632   1.00 61.57  ? 237 ARG A NH2 1 
ATOM   1815 N  N   . ASN A 1 262 ? -5.473  -17.912 5.089   1.00 33.85  ? 238 ASN A N   1 
ATOM   1816 C  CA  . ASN A 1 262 ? -4.581  -16.819 5.455   1.00 34.12  ? 238 ASN A CA  1 
ATOM   1817 C  C   . ASN A 1 262 ? -4.609  -16.519 6.948   1.00 31.51  ? 238 ASN A C   1 
ATOM   1818 O  O   . ASN A 1 262 ? -3.835  -15.675 7.407   1.00 31.62  ? 238 ASN A O   1 
ATOM   1819 C  CB  . ASN A 1 262 ? -4.945  -15.538 4.696   1.00 35.59  ? 238 ASN A CB  1 
ATOM   1820 C  CG  . ASN A 1 262 ? -5.089  -15.756 3.205   1.00 39.86  ? 238 ASN A CG  1 
ATOM   1821 O  OD1 . ASN A 1 262 ? -4.111  -16.016 2.505   1.00 39.49  ? 238 ASN A OD1 1 
ATOM   1822 N  ND2 . ASN A 1 262 ? -6.314  -15.629 2.708   1.00 41.12  ? 238 ASN A ND2 1 
ATOM   1823 N  N   . GLN A 1 263 ? -5.481  -17.183 7.708   1.00 28.05  ? 239 GLN A N   1 
ATOM   1824 C  CA  . GLN A 1 263 ? -5.691  -16.832 9.108   1.00 30.34  ? 239 GLN A CA  1 
ATOM   1825 C  C   . GLN A 1 263 ? -4.378  -16.801 9.883   1.00 30.54  ? 239 GLN A C   1 
ATOM   1826 O  O   . GLN A 1 263 ? -4.019  -15.782 10.483  1.00 26.64  ? 239 GLN A O   1 
ATOM   1827 C  CB  . GLN A 1 263 ? -6.668  -17.826 9.741   1.00 28.07  ? 239 GLN A CB  1 
ATOM   1828 C  CG  . GLN A 1 263 ? -7.002  -17.540 11.191  1.00 27.06  ? 239 GLN A CG  1 
ATOM   1829 C  CD  . GLN A 1 263 ? -7.979  -18.547 11.754  1.00 30.47  ? 239 GLN A CD  1 
ATOM   1830 O  OE1 . GLN A 1 263 ? -7.653  -19.722 11.908  1.00 30.79  ? 239 GLN A OE1 1 
ATOM   1831 N  NE2 . GLN A 1 263 ? -9.194  -18.096 12.044  1.00 31.52  ? 239 GLN A NE2 1 
ATOM   1832 N  N   . LEU A 1 264 ? -3.650  -17.918 9.888   1.00 27.92  ? 240 LEU A N   1 
ATOM   1833 C  CA  . LEU A 1 264 ? -2.454  -18.005 10.721  1.00 30.04  ? 240 LEU A CA  1 
ATOM   1834 C  C   . LEU A 1 264 ? -1.303  -17.199 10.130  1.00 30.00  ? 240 LEU A C   1 
ATOM   1835 O  O   . LEU A 1 264 ? -0.517  -16.601 10.874  1.00 30.09  ? 240 LEU A O   1 
ATOM   1836 C  CB  . LEU A 1 264 ? -2.054  -19.468 10.912  1.00 31.91  ? 240 LEU A CB  1 
ATOM   1837 C  CG  . LEU A 1 264 ? -3.011  -20.291 11.781  1.00 34.29  ? 240 LEU A CG  1 
ATOM   1838 C  CD1 . LEU A 1 264 ? -2.554  -21.739 11.872  1.00 32.50  ? 240 LEU A CD1 1 
ATOM   1839 C  CD2 . LEU A 1 264 ? -3.138  -19.686 13.171  1.00 29.59  ? 240 LEU A CD2 1 
ATOM   1840 N  N   . ASN A 1 265 ? -1.183  -17.172 8.801   1.00 27.55  ? 241 ASN A N   1 
ATOM   1841 C  CA  . ASN A 1 265 ? -0.154  -16.349 8.172   1.00 30.75  ? 241 ASN A CA  1 
ATOM   1842 C  C   . ASN A 1 265 ? -0.277  -14.897 8.612   1.00 29.54  ? 241 ASN A C   1 
ATOM   1843 O  O   . ASN A 1 265 ? 0.710   -14.265 9.007   1.00 30.37  ? 241 ASN A O   1 
ATOM   1844 C  CB  . ASN A 1 265 ? -0.255  -16.440 6.648   1.00 32.07  ? 241 ASN A CB  1 
ATOM   1845 C  CG  . ASN A 1 265 ? 0.296   -17.739 6.095   1.00 34.52  ? 241 ASN A CG  1 
ATOM   1846 O  OD1 . ASN A 1 265 ? 1.054   -18.445 6.759   1.00 32.32  ? 241 ASN A OD1 1 
ATOM   1847 N  ND2 . ASN A 1 265 ? -0.071  -18.050 4.859   1.00 35.67  ? 241 ASN A ND2 1 
ATOM   1848 N  N   . ILE A 1 266 ? -1.489  -14.350 8.549   1.00 29.32  ? 242 ILE A N   1 
ATOM   1849 C  CA  . ILE A 1 266 ? -1.667  -12.934 8.840   1.00 26.91  ? 242 ILE A CA  1 
ATOM   1850 C  C   . ILE A 1 266 ? -1.587  -12.671 10.339  1.00 27.94  ? 242 ILE A C   1 
ATOM   1851 O  O   . ILE A 1 266 ? -1.079  -11.624 10.758  1.00 26.36  ? 242 ILE A O   1 
ATOM   1852 C  CB  . ILE A 1 266 ? -2.988  -12.451 8.215   1.00 31.25  ? 242 ILE A CB  1 
ATOM   1853 C  CG1 . ILE A 1 266 ? -2.821  -12.445 6.691   1.00 30.73  ? 242 ILE A CG1 1 
ATOM   1854 C  CG2 . ILE A 1 266 ? -3.386  -11.077 8.755   1.00 28.24  ? 242 ILE A CG2 1 
ATOM   1855 C  CD1 . ILE A 1 266 ? -3.964  -11.859 5.920   1.00 31.91  ? 242 ILE A CD1 1 
ATOM   1856 N  N   . ALA A 1 267 ? -2.052  -13.607 11.170  1.00 24.73  ? 243 ALA A N   1 
ATOM   1857 C  CA  . ALA A 1 267 ? -1.857  -13.468 12.609  1.00 27.31  ? 243 ALA A CA  1 
ATOM   1858 C  C   . ALA A 1 267 ? -0.374  -13.370 12.952  1.00 28.35  ? 243 ALA A C   1 
ATOM   1859 O  O   . ALA A 1 267 ? 0.021   -12.581 13.818  1.00 26.32  ? 243 ALA A O   1 
ATOM   1860 C  CB  . ALA A 1 267 ? -2.500  -14.645 13.348  1.00 25.92  ? 243 ALA A CB  1 
ATOM   1861 N  N   . ALA A 1 268 ? 0.463   -14.163 12.279  1.00 29.16  ? 244 ALA A N   1 
ATOM   1862 C  CA  . ALA A 1 268 ? 1.891   -14.155 12.581  1.00 25.79  ? 244 ALA A CA  1 
ATOM   1863 C  C   . ALA A 1 268 ? 2.535   -12.832 12.177  1.00 27.58  ? 244 ALA A C   1 
ATOM   1864 O  O   . ALA A 1 268 ? 3.336   -12.269 12.934  1.00 26.91  ? 244 ALA A O   1 
ATOM   1865 C  CB  . ALA A 1 268 ? 2.579   -15.326 11.882  1.00 25.35  ? 244 ALA A CB  1 
ATOM   1866 N  N   . MET A 1 269 ? 2.206   -12.323 10.989  1.00 26.65  ? 245 MET A N   1 
ATOM   1867 C  CA  . MET A 1 269 ? 2.703   -11.012 10.586  1.00 28.04  ? 245 MET A CA  1 
ATOM   1868 C  C   . MET A 1 269 ? 2.385   -9.962  11.644  1.00 27.79  ? 245 MET A C   1 
ATOM   1869 O  O   . MET A 1 269 ? 3.255   -9.181  12.047  1.00 29.27  ? 245 MET A O   1 
ATOM   1870 C  CB  . MET A 1 269 ? 2.096   -10.607 9.242   1.00 27.30  ? 245 MET A CB  1 
ATOM   1871 C  CG  . MET A 1 269 ? 2.471   -11.507 8.080   1.00 29.24  ? 245 MET A CG  1 
ATOM   1872 S  SD  . MET A 1 269 ? 1.880   -10.856 6.503   1.00 35.53  ? 245 MET A SD  1 
ATOM   1873 C  CE  . MET A 1 269 ? 2.876   -9.369  6.368   1.00 31.52  ? 245 MET A CE  1 
ATOM   1874 N  N   . SER A 1 270 ? 1.131   -9.929  12.103  1.00 23.49  ? 246 SER A N   1 
ATOM   1875 C  CA  . SER A 1 270 ? 0.730   -8.932  13.091  1.00 28.40  ? 246 SER A CA  1 
ATOM   1876 C  C   . SER A 1 270 ? 1.510   -9.102  14.387  1.00 25.96  ? 246 SER A C   1 
ATOM   1877 O  O   . SER A 1 270 ? 2.041   -8.131  14.940  1.00 27.07  ? 246 SER A O   1 
ATOM   1878 C  CB  . SER A 1 270 ? -0.772  -9.032  13.362  1.00 25.76  ? 246 SER A CB  1 
ATOM   1879 O  OG  . SER A 1 270 ? -1.143  -8.163  14.420  1.00 26.04  ? 246 SER A OG  1 
ATOM   1880 N  N   . ALA A 1 271 ? 1.574   -10.332 14.898  1.00 25.87  ? 247 ALA A N   1 
ATOM   1881 C  CA  . ALA A 1 271 ? 2.306   -10.577 16.136  1.00 28.73  ? 247 ALA A CA  1 
ATOM   1882 C  C   . ALA A 1 271 ? 3.768   -10.175 15.996  1.00 28.50  ? 247 ALA A C   1 
ATOM   1883 O  O   . ALA A 1 271 ? 4.374   -9.667  16.946  1.00 30.40  ? 247 ALA A O   1 
ATOM   1884 C  CB  . ALA A 1 271 ? 2.186   -12.048 16.531  1.00 22.76  ? 247 ALA A CB  1 
ATOM   1885 N  N   . ALA A 1 272 ? 4.349   -10.387 14.814  1.00 26.85  ? 248 ALA A N   1 
ATOM   1886 C  CA  . ALA A 1 272 ? 5.740   -10.015 14.587  1.00 30.32  ? 248 ALA A CA  1 
ATOM   1887 C  C   . ALA A 1 272 ? 5.920   -8.512  14.448  1.00 32.69  ? 248 ALA A C   1 
ATOM   1888 O  O   . ALA A 1 272 ? 7.051   -8.027  14.560  1.00 31.14  ? 248 ALA A O   1 
ATOM   1889 C  CB  . ALA A 1 272 ? 6.276   -10.707 13.333  1.00 27.28  ? 248 ALA A CB  1 
ATOM   1890 N  N   . MET A 1 273 ? 4.837   -7.768  14.211  1.00 30.71  ? 249 MET A N   1 
ATOM   1891 C  CA  . MET A 1 273 ? 4.898   -6.333  13.966  1.00 29.59  ? 249 MET A CA  1 
ATOM   1892 C  C   . MET A 1 273 ? 4.316   -5.517  15.114  1.00 31.27  ? 249 MET A C   1 
ATOM   1893 O  O   . MET A 1 273 ? 4.123   -4.305  14.965  1.00 35.35  ? 249 MET A O   1 
ATOM   1894 C  CB  . MET A 1 273 ? 4.168   -5.994  12.663  1.00 31.94  ? 249 MET A CB  1 
ATOM   1895 C  CG  . MET A 1 273 ? 4.851   -6.521  11.405  1.00 30.66  ? 249 MET A CG  1 
ATOM   1896 S  SD  . MET A 1 273 ? 3.833   -6.371  9.917   1.00 37.61  ? 249 MET A SD  1 
ATOM   1897 C  CE  . MET A 1 273 ? 3.540   -4.606  9.901   1.00 33.26  ? 249 MET A CE  1 
ATOM   1898 N  N   . GLY A 1 274 ? 4.035   -6.143  16.253  1.00 30.55  ? 250 GLY A N   1 
ATOM   1899 C  CA  . GLY A 1 274 ? 3.503   -5.439  17.401  1.00 27.89  ? 250 GLY A CA  1 
ATOM   1900 C  C   . GLY A 1 274 ? 1.994   -5.360  17.468  1.00 32.42  ? 250 GLY A C   1 
ATOM   1901 O  O   . GLY A 1 274 ? 1.467   -4.565  18.258  1.00 33.49  ? 250 GLY A O   1 
ATOM   1902 N  N   . GLY A 1 275 ? 1.279   -6.154  16.672  1.00 28.56  ? 251 GLY A N   1 
ATOM   1903 C  CA  . GLY A 1 275 ? -0.165  -6.159  16.676  1.00 28.80  ? 251 GLY A CA  1 
ATOM   1904 C  C   . GLY A 1 275 ? -0.746  -7.357  17.407  1.00 28.93  ? 251 GLY A C   1 
ATOM   1905 O  O   . GLY A 1 275 ? -0.041  -8.170  18.010  1.00 28.17  ? 251 GLY A O   1 
ATOM   1906 N  N   . HIS A 1 276 ? -2.068  -7.460  17.337  1.00 31.18  ? 252 HIS A N   1 
ATOM   1907 C  CA  . HIS A 1 276 ? -2.843  -8.498  17.999  1.00 26.76  ? 252 HIS A CA  1 
ATOM   1908 C  C   . HIS A 1 276 ? -3.559  -9.326  16.939  1.00 27.12  ? 252 HIS A C   1 
ATOM   1909 O  O   . HIS A 1 276 ? -3.585  -8.966  15.759  1.00 25.88  ? 252 HIS A O   1 
ATOM   1910 C  CB  . HIS A 1 276 ? -3.809  -7.862  19.001  1.00 27.25  ? 252 HIS A CB  1 
ATOM   1911 C  CG  . HIS A 1 276 ? -3.132  -6.917  19.946  1.00 29.05  ? 252 HIS A CG  1 
ATOM   1912 N  ND1 . HIS A 1 276 ? -2.392  -7.349  21.024  1.00 29.36  ? 252 HIS A ND1 1 
ATOM   1913 C  CD2 . HIS A 1 276 ? -3.047  -5.565  19.951  1.00 29.69  ? 252 HIS A CD2 1 
ATOM   1914 C  CE1 . HIS A 1 276 ? -1.897  -6.306  21.666  1.00 29.62  ? 252 HIS A CE1 1 
ATOM   1915 N  NE2 . HIS A 1 276 ? -2.279  -5.211  21.034  1.00 29.68  ? 252 HIS A NE2 1 
ATOM   1916 N  N   . VAL A 1 277 ? -4.123  -10.464 17.349  1.00 25.28  ? 253 VAL A N   1 
ATOM   1917 C  CA  . VAL A 1 277 ? -4.588  -11.460 16.392  1.00 26.52  ? 253 VAL A CA  1 
ATOM   1918 C  C   . VAL A 1 277 ? -6.000  -11.921 16.721  1.00 26.14  ? 253 VAL A C   1 
ATOM   1919 O  O   . VAL A 1 277 ? -6.416  -11.959 17.884  1.00 27.86  ? 253 VAL A O   1 
ATOM   1920 C  CB  . VAL A 1 277 ? -3.643  -12.681 16.330  1.00 27.73  ? 253 VAL A CB  1 
ATOM   1921 C  CG1 . VAL A 1 277 ? -2.201  -12.231 16.178  1.00 26.66  ? 253 VAL A CG1 1 
ATOM   1922 C  CG2 . VAL A 1 277 ? -3.818  -13.557 17.557  1.00 27.77  ? 253 VAL A CG2 1 
ATOM   1923 N  N   . ARG A 1 278 ? -6.732  -12.288 15.672  1.00 25.85  ? 254 ARG A N   1 
ATOM   1924 C  CA  . ARG A 1 278 ? -8.042  -12.910 15.781  1.00 28.95  ? 254 ARG A CA  1 
ATOM   1925 C  C   . ARG A 1 278 ? -8.023  -14.236 15.034  1.00 29.31  ? 254 ARG A C   1 
ATOM   1926 O  O   . ARG A 1 278 ? -7.561  -14.301 13.890  1.00 27.75  ? 254 ARG A O   1 
ATOM   1927 C  CB  . ARG A 1 278 ? -9.136  -11.999 15.217  1.00 28.72  ? 254 ARG A CB  1 
ATOM   1928 C  CG  . ARG A 1 278 ? -10.447 -12.720 14.932  1.00 28.84  ? 254 ARG A CG  1 
ATOM   1929 C  CD  . ARG A 1 278 ? -11.591 -11.746 14.661  1.00 29.30  ? 254 ARG A CD  1 
ATOM   1930 N  NE  . ARG A 1 278 ? -12.621 -12.352 13.827  1.00 26.86  ? 254 ARG A NE  1 
ATOM   1931 C  CZ  . ARG A 1 278 ? -13.848 -11.871 13.669  1.00 34.33  ? 254 ARG A CZ  1 
ATOM   1932 N  NH1 . ARG A 1 278 ? -14.251 -10.777 14.296  1.00 30.13  ? 254 ARG A NH1 1 
ATOM   1933 N  NH2 . ARG A 1 278 ? -14.694 -12.505 12.862  1.00 28.19  ? 254 ARG A NH2 1 
ATOM   1934 N  N   . VAL A 1 279 ? -8.513  -15.287 15.689  1.00 25.54  ? 255 VAL A N   1 
ATOM   1935 C  CA  . VAL A 1 279 ? -8.717  -16.586 15.056  1.00 28.17  ? 255 VAL A CA  1 
ATOM   1936 C  C   . VAL A 1 279 ? -10.172 -16.981 15.270  1.00 29.42  ? 255 VAL A C   1 
ATOM   1937 O  O   . VAL A 1 279 ? -10.966 -16.193 15.796  1.00 28.05  ? 255 VAL A O   1 
ATOM   1938 C  CB  . VAL A 1 279 ? -7.764  -17.655 15.623  1.00 30.18  ? 255 VAL A CB  1 
ATOM   1939 C  CG1 . VAL A 1 279 ? -6.313  -17.255 15.401  1.00 28.73  ? 255 VAL A CG1 1 
ATOM   1940 C  CG2 . VAL A 1 279 ? -8.039  -17.886 17.107  1.00 26.78  ? 255 VAL A CG2 1 
ATOM   1941 N  N   . GLY A 1 280 ? -10.533 -18.199 14.870  1.00 30.37  ? 256 GLY A N   1 
ATOM   1942 C  CA  . GLY A 1 280 ? -11.866 -18.701 15.137  1.00 30.76  ? 256 GLY A CA  1 
ATOM   1943 C  C   . GLY A 1 280 ? -12.581 -19.258 13.925  1.00 30.27  ? 256 GLY A C   1 
ATOM   1944 O  O   . GLY A 1 280 ? -12.267 -18.910 12.781  1.00 28.90  ? 256 GLY A O   1 
ATOM   1945 N  N   . LEU A 1 281 ? -13.558 -20.130 14.171  1.00 30.78  ? 257 LEU A N   1 
ATOM   1946 C  CA  . LEU A 1 281 ? -14.300 -20.757 13.085  1.00 32.43  ? 257 LEU A CA  1 
ATOM   1947 C  C   . LEU A 1 281 ? -15.230 -19.785 12.369  1.00 30.57  ? 257 LEU A C   1 
ATOM   1948 O  O   . LEU A 1 281 ? -15.758 -20.135 11.309  1.00 30.49  ? 257 LEU A O   1 
ATOM   1949 C  CB  . LEU A 1 281 ? -15.086 -21.955 13.623  1.00 32.72  ? 257 LEU A CB  1 
ATOM   1950 C  CG  . LEU A 1 281 ? -14.299 -23.272 13.695  1.00 34.31  ? 257 LEU A CG  1 
ATOM   1951 C  CD1 . LEU A 1 281 ? -12.996 -23.113 14.458  1.00 34.98  ? 257 LEU A CD1 1 
ATOM   1952 C  CD2 . LEU A 1 281 ? -15.141 -24.370 14.327  1.00 34.07  ? 257 LEU A CD2 1 
ATOM   1953 N  N   . GLU A 1 282 ? -15.440 -18.580 12.909  1.00 28.78  ? 258 GLU A N   1 
ATOM   1954 C  CA  . GLU A 1 282 ? -16.150 -17.554 12.150  1.00 31.80  ? 258 GLU A CA  1 
ATOM   1955 C  C   . GLU A 1 282 ? -15.408 -17.206 10.866  1.00 29.55  ? 258 GLU A C   1 
ATOM   1956 O  O   . GLU A 1 282 ? -16.033 -16.810 9.875   1.00 30.52  ? 258 GLU A O   1 
ATOM   1957 C  CB  . GLU A 1 282 ? -16.344 -16.294 13.005  1.00 29.75  ? 258 GLU A CB  1 
ATOM   1958 C  CG  . GLU A 1 282 ? -16.808 -15.046 12.220  1.00 32.05  ? 258 GLU A CG  1 
ATOM   1959 C  CD  . GLU A 1 282 ? -17.394 -13.954 13.123  1.00 31.06  ? 258 GLU A CD  1 
ATOM   1960 O  OE1 . GLU A 1 282 ? -17.561 -14.212 14.332  1.00 31.48  ? 258 GLU A OE1 1 
ATOM   1961 O  OE2 . GLU A 1 282 ? -17.689 -12.839 12.633  1.00 30.02  ? 258 GLU A OE2 1 
ATOM   1962 N  N   . ASP A 1 283 ? -14.081 -17.369 10.857  1.00 31.61  ? 259 ASP A N   1 
ATOM   1963 C  CA  . ASP A 1 283 ? -13.237 -16.901 9.766   1.00 30.93  ? 259 ASP A CA  1 
ATOM   1964 C  C   . ASP A 1 283 ? -12.548 -18.012 8.992   1.00 31.86  ? 259 ASP A C   1 
ATOM   1965 O  O   . ASP A 1 283 ? -12.161 -17.786 7.842   1.00 31.02  ? 259 ASP A O   1 
ATOM   1966 C  CB  . ASP A 1 283 ? -12.152 -15.958 10.306  1.00 27.37  ? 259 ASP A CB  1 
ATOM   1967 C  CG  . ASP A 1 283 ? -12.721 -14.832 11.141  1.00 31.21  ? 259 ASP A CG  1 
ATOM   1968 O  OD1 . ASP A 1 283 ? -13.834 -14.368 10.824  1.00 33.43  ? 259 ASP A OD1 1 
ATOM   1969 O  OD2 . ASP A 1 283 ? -12.056 -14.413 12.114  1.00 32.52  ? 259 ASP A OD2 1 
ATOM   1970 N  N   . ASN A 1 284 ? -12.369 -19.188 9.585   1.00 27.83  ? 260 ASN A N   1 
ATOM   1971 C  CA  . ASN A 1 284 ? -11.602 -20.253 8.948   1.00 30.48  ? 260 ASN A CA  1 
ATOM   1972 C  C   . ASN A 1 284 ? -12.081 -21.579 9.511   1.00 31.09  ? 260 ASN A C   1 
ATOM   1973 O  O   . ASN A 1 284 ? -12.060 -21.774 10.729  1.00 30.50  ? 260 ASN A O   1 
ATOM   1974 C  CB  . ASN A 1 284 ? -10.100 -20.064 9.194   1.00 30.03  ? 260 ASN A CB  1 
ATOM   1975 C  CG  . ASN A 1 284 ? -9.262  -21.182 8.603   1.00 31.47  ? 260 ASN A CG  1 
ATOM   1976 O  OD1 . ASN A 1 284 ? -9.635  -21.794 7.602   1.00 30.55  ? 260 ASN A OD1 1 
ATOM   1977 N  ND2 . ASN A 1 284 ? -8.121  -21.454 9.226   1.00 30.07  ? 260 ASN A ND2 1 
ATOM   1978 N  N   . LEU A 1 285 ? -12.515 -22.480 8.632   1.00 30.13  ? 261 LEU A N   1 
ATOM   1979 C  CA  . LEU A 1 285 ? -12.998 -23.791 9.042   1.00 33.67  ? 261 LEU A CA  1 
ATOM   1980 C  C   . LEU A 1 285 ? -11.900 -24.841 9.104   1.00 34.71  ? 261 LEU A C   1 
ATOM   1981 O  O   . LEU A 1 285 ? -12.167 -25.967 9.540   1.00 32.44  ? 261 LEU A O   1 
ATOM   1982 C  CB  . LEU A 1 285 ? -14.086 -24.270 8.077   1.00 34.31  ? 261 LEU A CB  1 
ATOM   1983 C  CG  . LEU A 1 285 ? -15.325 -23.381 8.017   1.00 33.72  ? 261 LEU A CG  1 
ATOM   1984 C  CD1 . LEU A 1 285 ? -16.257 -23.830 6.907   1.00 35.00  ? 261 LEU A CD1 1 
ATOM   1985 C  CD2 . LEU A 1 285 ? -16.029 -23.387 9.366   1.00 33.17  ? 261 LEU A CD2 1 
ATOM   1986 N  N   . TRP A 1 286 ? -10.683 -24.502 8.695   1.00 31.54  ? 262 TRP A N   1 
ATOM   1987 C  CA  . TRP A 1 286 ? -9.630  -25.477 8.475   1.00 36.88  ? 262 TRP A CA  1 
ATOM   1988 C  C   . TRP A 1 286 ? -8.582  -25.416 9.577   1.00 38.05  ? 262 TRP A C   1 
ATOM   1989 O  O   . TRP A 1 286 ? -8.295  -24.353 10.135  1.00 38.88  ? 262 TRP A O   1 
ATOM   1990 C  CB  . TRP A 1 286 ? -8.977  -25.245 7.111   1.00 37.87  ? 262 TRP A CB  1 
ATOM   1991 C  CG  . TRP A 1 286 ? -9.954  -25.423 6.005   1.00 40.70  ? 262 TRP A CG  1 
ATOM   1992 C  CD1 . TRP A 1 286 ? -10.761 -24.466 5.459   1.00 38.02  ? 262 TRP A CD1 1 
ATOM   1993 C  CD2 . TRP A 1 286 ? -10.260 -26.643 5.325   1.00 38.24  ? 262 TRP A CD2 1 
ATOM   1994 N  NE1 . TRP A 1 286 ? -11.544 -25.016 4.474   1.00 40.69  ? 262 TRP A NE1 1 
ATOM   1995 C  CE2 . TRP A 1 286 ? -11.256 -26.351 4.372   1.00 42.96  ? 262 TRP A CE2 1 
ATOM   1996 C  CE3 . TRP A 1 286 ? -9.784  -27.954 5.425   1.00 41.92  ? 262 TRP A CE3 1 
ATOM   1997 C  CZ2 . TRP A 1 286 ? -11.782 -27.321 3.522   1.00 42.82  ? 262 TRP A CZ2 1 
ATOM   1998 C  CZ3 . TRP A 1 286 ? -10.306 -28.915 4.583   1.00 43.95  ? 262 TRP A CZ3 1 
ATOM   1999 C  CH2 . TRP A 1 286 ? -11.296 -28.595 3.643   1.00 43.92  ? 262 TRP A CH2 1 
ATOM   2000 N  N   . ALA A 1 287 ? -8.030  -26.589 9.893   1.00 39.43  ? 263 ALA A N   1 
ATOM   2001 C  CA  . ALA A 1 287 ? -6.871  -26.714 10.762  1.00 42.48  ? 263 ALA A CA  1 
ATOM   2002 C  C   . ALA A 1 287 ? -5.602  -27.086 10.013  1.00 46.32  ? 263 ALA A C   1 
ATOM   2003 O  O   . ALA A 1 287 ? -4.507  -26.896 10.550  1.00 52.14  ? 263 ALA A O   1 
ATOM   2004 C  CB  . ALA A 1 287 ? -7.128  -27.773 11.841  1.00 41.77  ? 263 ALA A CB  1 
ATOM   2005 N  N   . GLY A 1 288 ? -5.725  -27.610 8.801   1.00 46.59  ? 264 GLY A N   1 
ATOM   2006 C  CA  . GLY A 1 288 ? -4.565  -28.008 8.033   1.00 49.82  ? 264 GLY A CA  1 
ATOM   2007 C  C   . GLY A 1 288 ? -4.993  -28.481 6.664   1.00 54.07  ? 264 GLY A C   1 
ATOM   2008 O  O   . GLY A 1 288 ? -6.120  -28.232 6.232   1.00 52.90  ? 264 GLY A O   1 
ATOM   2009 N  N   . LYS A 1 289 ? -4.085  -29.172 5.982   1.00 56.16  ? 265 LYS A N   1 
ATOM   2010 C  CA  . LYS A 1 289 ? -4.391  -29.688 4.655   1.00 57.08  ? 265 LYS A CA  1 
ATOM   2011 C  C   . LYS A 1 289 ? -5.351  -30.868 4.759   1.00 55.58  ? 265 LYS A C   1 
ATOM   2012 O  O   . LYS A 1 289 ? -5.084  -31.842 5.470   1.00 56.47  ? 265 LYS A O   1 
ATOM   2013 C  CB  . LYS A 1 289 ? -3.109  -30.109 3.937   1.00 61.01  ? 265 LYS A CB  1 
ATOM   2014 C  CG  . LYS A 1 289 ? -3.333  -30.587 2.507   1.00 66.83  ? 265 LYS A CG  1 
ATOM   2015 C  CD  . LYS A 1 289 ? -2.035  -31.034 1.847   1.00 76.69  ? 265 LYS A CD  1 
ATOM   2016 C  CE  . LYS A 1 289 ? -1.106  -29.864 1.549   1.00 81.47  ? 265 LYS A CE  1 
ATOM   2017 N  NZ  . LYS A 1 289 ? -1.679  -28.917 0.553   1.00 82.76  ? 265 LYS A NZ  1 
ATOM   2018 N  N   . GLY A 1 290 ? -6.468  -30.779 4.043   1.00 52.69  ? 266 GLY A N   1 
ATOM   2019 C  CA  . GLY A 1 290 ? -7.455  -31.844 4.057   1.00 50.44  ? 266 GLY A CA  1 
ATOM   2020 C  C   . GLY A 1 290 ? -8.017  -32.138 5.427   1.00 48.33  ? 266 GLY A C   1 
ATOM   2021 O  O   . GLY A 1 290 ? -8.470  -33.261 5.675   1.00 47.42  ? 266 GLY A O   1 
ATOM   2022 N  N   . ARG A 1 291 ? -8.012  -31.155 6.326   1.00 43.98  ? 267 ARG A N   1 
ATOM   2023 C  CA  . ARG A 1 291 ? -8.382  -31.377 7.718   1.00 47.66  ? 267 ARG A CA  1 
ATOM   2024 C  C   . ARG A 1 291 ? -9.190  -30.190 8.217   1.00 41.35  ? 267 ARG A C   1 
ATOM   2025 O  O   . ARG A 1 291 ? -8.668  -29.074 8.299   1.00 38.24  ? 267 ARG A O   1 
ATOM   2026 C  CB  . ARG A 1 291 ? -7.136  -31.571 8.587   1.00 46.87  ? 267 ARG A CB  1 
ATOM   2027 C  CG  . ARG A 1 291 ? -7.276  -32.642 9.649   1.00 51.66  ? 267 ARG A CG  1 
ATOM   2028 C  CD  . ARG A 1 291 ? -6.424  -32.311 10.861  1.00 57.77  ? 267 ARG A CD  1 
ATOM   2029 N  NE  . ARG A 1 291 ? -5.124  -31.769 10.483  1.00 57.84  ? 267 ARG A NE  1 
ATOM   2030 C  CZ  . ARG A 1 291 ? -4.361  -31.033 11.278  1.00 60.86  ? 267 ARG A CZ  1 
ATOM   2031 N  NH1 . ARG A 1 291 ? -4.733  -30.735 12.513  1.00 60.45  ? 267 ARG A NH1 1 
ATOM   2032 N  NH2 . ARG A 1 291 ? -3.198  -30.576 10.820  1.00 60.09  ? 267 ARG A NH2 1 
ATOM   2033 N  N   . LEU A 1 292 ? -10.454 -30.429 8.553   1.00 38.86  ? 268 LEU A N   1 
ATOM   2034 C  CA  . LEU A 1 292 ? -11.273 -29.401 9.174   1.00 37.60  ? 268 LEU A CA  1 
ATOM   2035 C  C   . LEU A 1 292 ? -10.879 -29.223 10.635  1.00 38.35  ? 268 LEU A C   1 
ATOM   2036 O  O   . LEU A 1 292 ? -10.453 -30.166 11.307  1.00 35.82  ? 268 LEU A O   1 
ATOM   2037 C  CB  . LEU A 1 292 ? -12.756 -29.760 9.088   1.00 38.34  ? 268 LEU A CB  1 
ATOM   2038 C  CG  . LEU A 1 292 ? -13.406 -29.799 7.704   1.00 40.08  ? 268 LEU A CG  1 
ATOM   2039 C  CD1 . LEU A 1 292 ? -14.821 -30.346 7.815   1.00 37.78  ? 268 LEU A CD1 1 
ATOM   2040 C  CD2 . LEU A 1 292 ? -13.418 -28.418 7.063   1.00 36.96  ? 268 LEU A CD2 1 
ATOM   2041 N  N   . ALA A 1 293 ? -11.024 -27.994 11.123  1.00 35.51  ? 269 ALA A N   1 
ATOM   2042 C  CA  . ALA A 1 293 ? -10.797 -27.706 12.532  1.00 38.47  ? 269 ALA A CA  1 
ATOM   2043 C  C   . ALA A 1 293 ? -11.989 -28.190 13.346  1.00 38.10  ? 269 ALA A C   1 
ATOM   2044 O  O   . ALA A 1 293 ? -13.142 -27.939 12.982  1.00 34.94  ? 269 ALA A O   1 
ATOM   2045 C  CB  . ALA A 1 293 ? -10.580 -26.208 12.743  1.00 33.17  ? 269 ALA A CB  1 
ATOM   2046 N  N   . GLU A 1 294 ? -11.710 -28.886 14.448  1.00 38.03  ? 270 GLU A N   1 
ATOM   2047 C  CA  . GLU A 1 294 ? -12.767 -29.453 15.275  1.00 36.59  ? 270 GLU A CA  1 
ATOM   2048 C  C   . GLU A 1 294 ? -13.234 -28.509 16.373  1.00 35.64  ? 270 GLU A C   1 
ATOM   2049 O  O   . GLU A 1 294 ? -14.397 -28.583 16.787  1.00 36.21  ? 270 GLU A O   1 
ATOM   2050 C  CB  . GLU A 1 294 ? -12.294 -30.770 15.897  1.00 40.07  ? 270 GLU A CB  1 
ATOM   2051 C  CG  . GLU A 1 294 ? -11.929 -31.831 14.865  1.00 47.22  ? 270 GLU A CG  1 
ATOM   2052 C  CD  . GLU A 1 294 ? -11.489 -33.140 15.493  1.00 58.10  ? 270 GLU A CD  1 
ATOM   2053 O  OE1 . GLU A 1 294 ? -11.647 -33.298 16.722  1.00 62.15  ? 270 GLU A OE1 1 
ATOM   2054 O  OE2 . GLU A 1 294 ? -10.986 -34.012 14.753  1.00 61.96  ? 270 GLU A OE2 1 
ATOM   2055 N  N   . THR A 1 295 ? -12.366 -27.621 16.853  1.00 36.51  ? 271 THR A N   1 
ATOM   2056 C  CA  . THR A 1 295 ? -12.733 -26.680 17.901  1.00 35.43  ? 271 THR A CA  1 
ATOM   2057 C  C   . THR A 1 295 ? -12.105 -25.325 17.625  1.00 34.66  ? 271 THR A C   1 
ATOM   2058 O  O   . THR A 1 295 ? -11.105 -25.208 16.913  1.00 33.60  ? 271 THR A O   1 
ATOM   2059 C  CB  . THR A 1 295 ? -12.287 -27.147 19.294  1.00 34.71  ? 271 THR A CB  1 
ATOM   2060 O  OG1 . THR A 1 295 ? -10.858 -27.235 19.334  1.00 35.57  ? 271 THR A OG1 1 
ATOM   2061 C  CG2 . THR A 1 295 ? -12.896 -28.495 19.634  1.00 37.04  ? 271 THR A CG2 1 
ATOM   2062 N  N   . ASN A 1 296 ? -12.712 -24.296 18.217  1.00 35.91  ? 272 ASN A N   1 
ATOM   2063 C  CA  . ASN A 1 296 ? -12.105 -22.972 18.206  1.00 32.30  ? 272 ASN A CA  1 
ATOM   2064 C  C   . ASN A 1 296 ? -10.807 -22.957 19.004  1.00 32.40  ? 272 ASN A C   1 
ATOM   2065 O  O   . ASN A 1 296 ? -9.830  -22.313 18.603  1.00 33.39  ? 272 ASN A O   1 
ATOM   2066 C  CB  . ASN A 1 296 ? -13.091 -21.949 18.770  1.00 32.63  ? 272 ASN A CB  1 
ATOM   2067 C  CG  . ASN A 1 296 ? -14.092 -21.472 17.738  1.00 32.27  ? 272 ASN A CG  1 
ATOM   2068 O  OD1 . ASN A 1 296 ? -13.792 -20.593 16.933  1.00 33.42  ? 272 ASN A OD1 1 
ATOM   2069 N  ND2 . ASN A 1 296 ? -15.291 -22.047 17.759  1.00 30.34  ? 272 ASN A ND2 1 
ATOM   2070 N  N   . ALA A 1 297 ? -10.781 -23.655 20.143  1.00 30.15  ? 273 ALA A N   1 
ATOM   2071 C  CA  . ALA A 1 297 ? -9.578  -23.690 20.968  1.00 35.42  ? 273 ALA A CA  1 
ATOM   2072 C  C   . ALA A 1 297 ? -8.381  -24.188 20.169  1.00 36.60  ? 273 ALA A C   1 
ATOM   2073 O  O   . ALA A 1 297 ? -7.251  -23.724 20.363  1.00 33.23  ? 273 ALA A O   1 
ATOM   2074 C  CB  . ALA A 1 297 ? -9.815  -24.576 22.193  1.00 31.82  ? 273 ALA A CB  1 
ATOM   2075 N  N   . GLN A 1 298 ? -8.619  -25.134 19.261  1.00 34.70  ? 274 GLN A N   1 
ATOM   2076 C  CA  . GLN A 1 298 ? -7.565  -25.643 18.390  1.00 35.24  ? 274 GLN A CA  1 
ATOM   2077 C  C   . GLN A 1 298 ? -6.844  -24.512 17.667  1.00 34.82  ? 274 GLN A C   1 
ATOM   2078 O  O   . GLN A 1 298 ? -5.612  -24.525 17.545  1.00 30.65  ? 274 GLN A O   1 
ATOM   2079 C  CB  . GLN A 1 298 ? -8.194  -26.626 17.403  1.00 37.20  ? 274 GLN A CB  1 
ATOM   2080 C  CG  . GLN A 1 298 ? -7.310  -27.148 16.303  1.00 43.02  ? 274 GLN A CG  1 
ATOM   2081 C  CD  . GLN A 1 298 ? -8.027  -28.212 15.491  1.00 42.73  ? 274 GLN A CD  1 
ATOM   2082 O  OE1 . GLN A 1 298 ? -9.210  -28.479 15.710  1.00 40.47  ? 274 GLN A OE1 1 
ATOM   2083 N  NE2 . GLN A 1 298 ? -7.316  -28.829 14.559  1.00 43.80  ? 274 GLN A NE2 1 
ATOM   2084 N  N   . GLN A 1 299 ? -7.593  -23.514 17.190  1.00 33.12  ? 275 GLN A N   1 
ATOM   2085 C  CA  . GLN A 1 299 ? -6.982  -22.384 16.499  1.00 30.70  ? 275 GLN A CA  1 
ATOM   2086 C  C   . GLN A 1 299 ? -6.326  -21.407 17.467  1.00 31.56  ? 275 GLN A C   1 
ATOM   2087 O  O   . GLN A 1 299 ? -5.308  -20.791 17.127  1.00 29.67  ? 275 GLN A O   1 
ATOM   2088 C  CB  . GLN A 1 299 ? -8.033  -21.663 15.651  1.00 29.42  ? 275 GLN A CB  1 
ATOM   2089 C  CG  . GLN A 1 299 ? -8.620  -22.530 14.543  1.00 29.94  ? 275 GLN A CG  1 
ATOM   2090 C  CD  . GLN A 1 299 ? -9.580  -21.771 13.643  1.00 33.49  ? 275 GLN A CD  1 
ATOM   2091 O  OE1 . GLN A 1 299 ? -10.033 -20.674 13.978  1.00 32.71  ? 275 GLN A OE1 1 
ATOM   2092 N  NE2 . GLN A 1 299 ? -9.896  -22.355 12.490  1.00 31.02  ? 275 GLN A NE2 1 
ATOM   2093 N  N   . VAL A 1 300 ? -6.890  -21.245 18.665  1.00 28.65  ? 276 VAL A N   1 
ATOM   2094 C  CA  . VAL A 1 300 ? -6.251  -20.410 19.677  1.00 31.60  ? 276 VAL A CA  1 
ATOM   2095 C  C   . VAL A 1 300 ? -4.877  -20.966 20.036  1.00 32.97  ? 276 VAL A C   1 
ATOM   2096 O  O   . VAL A 1 300 ? -3.905  -20.216 20.185  1.00 32.86  ? 276 VAL A O   1 
ATOM   2097 C  CB  . VAL A 1 300 ? -7.155  -20.293 20.918  1.00 31.13  ? 276 VAL A CB  1 
ATOM   2098 C  CG1 . VAL A 1 300 ? -6.424  -19.577 22.044  1.00 28.58  ? 276 VAL A CG1 1 
ATOM   2099 C  CG2 . VAL A 1 300 ? -8.452  -19.575 20.566  1.00 29.34  ? 276 VAL A CG2 1 
ATOM   2100 N  N   . ARG A 1 301 ? -4.776  -22.290 20.182  1.00 32.08  ? 277 ARG A N   1 
ATOM   2101 C  CA  . ARG A 1 301 ? -3.498  -22.899 20.541  1.00 33.00  ? 277 ARG A CA  1 
ATOM   2102 C  C   . ARG A 1 301 ? -2.457  -22.692 19.448  1.00 31.02  ? 277 ARG A C   1 
ATOM   2103 O  O   . ARG A 1 301 ? -1.276  -22.471 19.740  1.00 31.51  ? 277 ARG A O   1 
ATOM   2104 C  CB  . ARG A 1 301 ? -3.689  -24.390 20.823  1.00 35.17  ? 277 ARG A CB  1 
ATOM   2105 C  CG  . ARG A 1 301 ? -4.370  -24.682 22.155  1.00 39.48  ? 277 ARG A CG  1 
ATOM   2106 C  CD  . ARG A 1 301 ? -4.314  -26.163 22.499  1.00 45.18  ? 277 ARG A CD  1 
ATOM   2107 N  NE  . ARG A 1 301 ? -5.048  -26.981 21.540  1.00 47.69  ? 277 ARG A NE  1 
ATOM   2108 C  CZ  . ARG A 1 301 ? -6.332  -27.299 21.644  1.00 46.56  ? 277 ARG A CZ  1 
ATOM   2109 N  NH1 . ARG A 1 301 ? -7.069  -26.885 22.664  1.00 45.71  ? 277 ARG A NH1 1 
ATOM   2110 N  NH2 . ARG A 1 301 ? -6.892  -28.051 20.702  1.00 45.82  ? 277 ARG A NH2 1 
ATOM   2111 N  N   . ALA A 1 302 ? -2.870  -22.767 18.182  1.00 30.77  ? 278 ALA A N   1 
ATOM   2112 C  CA  . ALA A 1 302 ? -1.926  -22.548 17.093  1.00 32.68  ? 278 ALA A CA  1 
ATOM   2113 C  C   . ALA A 1 302 ? -1.383  -21.124 17.129  1.00 33.84  ? 278 ALA A C   1 
ATOM   2114 O  O   . ALA A 1 302 ? -0.168  -20.907 17.062  1.00 31.34  ? 278 ALA A O   1 
ATOM   2115 C  CB  . ALA A 1 302 ? -2.593  -22.845 15.750  1.00 27.22  ? 278 ALA A CB  1 
ATOM   2116 N  N   . ALA A 1 303 ? -2.274  -20.137 17.250  1.00 29.75  ? 279 ALA A N   1 
ATOM   2117 C  CA  . ALA A 1 303 ? -1.827  -18.754 17.369  1.00 27.80  ? 279 ALA A CA  1 
ATOM   2118 C  C   . ALA A 1 303 ? -0.944  -18.572 18.595  1.00 29.91  ? 279 ALA A C   1 
ATOM   2119 O  O   . ALA A 1 303 ? 0.081   -17.882 18.539  1.00 28.48  ? 279 ALA A O   1 
ATOM   2120 C  CB  . ALA A 1 303 ? -3.033  -17.817 17.435  1.00 29.16  ? 279 ALA A CB  1 
ATOM   2121 N  N   . ARG A 1 304 ? -1.329  -19.185 19.714  1.00 28.93  ? 280 ARG A N   1 
ATOM   2122 C  CA  . ARG A 1 304 ? -0.537  -19.069 20.932  1.00 31.33  ? 280 ARG A CA  1 
ATOM   2123 C  C   . ARG A 1 304 ? 0.861   -19.636 20.729  1.00 33.56  ? 280 ARG A C   1 
ATOM   2124 O  O   . ARG A 1 304 ? 1.843   -19.097 21.252  1.00 34.00  ? 280 ARG A O   1 
ATOM   2125 C  CB  . ARG A 1 304 ? -1.249  -19.789 22.073  1.00 30.19  ? 280 ARG A CB  1 
ATOM   2126 C  CG  . ARG A 1 304 ? -0.457  -19.859 23.352  1.00 33.45  ? 280 ARG A CG  1 
ATOM   2127 C  CD  . ARG A 1 304 ? -1.306  -20.432 24.460  1.00 36.69  ? 280 ARG A CD  1 
ATOM   2128 N  NE  . ARG A 1 304 ? -0.688  -20.236 25.764  1.00 42.99  ? 280 ARG A NE  1 
ATOM   2129 C  CZ  . ARG A 1 304 ? -1.357  -20.027 26.888  1.00 42.67  ? 280 ARG A CZ  1 
ATOM   2130 N  NH1 . ARG A 1 304 ? -2.679  -19.964 26.907  1.00 38.68  ? 280 ARG A NH1 1 
ATOM   2131 N  NH2 . ARG A 1 304 ? -0.683  -19.868 28.023  1.00 47.75  ? 280 ARG A NH2 1 
ATOM   2132 N  N   . GLN A 1 305 ? 0.964   -20.728 19.974  1.00 30.19  ? 281 GLN A N   1 
ATOM   2133 C  CA  . GLN A 1 305 ? 2.264   -21.317 19.681  1.00 32.35  ? 281 GLN A CA  1 
ATOM   2134 C  C   . GLN A 1 305 ? 3.137   -20.352 18.888  1.00 35.97  ? 281 GLN A C   1 
ATOM   2135 O  O   . GLN A 1 305 ? 4.353   -20.283 19.102  1.00 31.45  ? 281 GLN A O   1 
ATOM   2136 C  CB  . GLN A 1 305 ? 2.060   -22.625 18.920  1.00 33.00  ? 281 GLN A CB  1 
ATOM   2137 C  CG  . GLN A 1 305 ? 3.316   -23.428 18.686  1.00 44.66  ? 281 GLN A CG  1 
ATOM   2138 C  CD  . GLN A 1 305 ? 3.012   -24.801 18.123  1.00 49.46  ? 281 GLN A CD  1 
ATOM   2139 O  OE1 . GLN A 1 305 ? 2.022   -25.431 18.499  1.00 54.94  ? 281 GLN A OE1 1 
ATOM   2140 N  NE2 . GLN A 1 305 ? 3.855   -25.267 17.208  1.00 42.45  ? 281 GLN A NE2 1 
ATOM   2141 N  N   . ILE A 1 306 ? 2.534   -19.598 17.967  1.00 30.55  ? 282 ILE A N   1 
ATOM   2142 C  CA  . ILE A 1 306 ? 3.284   -18.592 17.220  1.00 32.83  ? 282 ILE A CA  1 
ATOM   2143 C  C   . ILE A 1 306 ? 3.702   -17.453 18.141  1.00 31.32  ? 282 ILE A C   1 
ATOM   2144 O  O   . ILE A 1 306 ? 4.849   -16.992 18.111  1.00 29.64  ? 282 ILE A O   1 
ATOM   2145 C  CB  . ILE A 1 306 ? 2.448   -18.075 16.035  1.00 31.00  ? 282 ILE A CB  1 
ATOM   2146 C  CG1 . ILE A 1 306 ? 2.308   -19.163 14.968  1.00 30.40  ? 282 ILE A CG1 1 
ATOM   2147 C  CG2 . ILE A 1 306 ? 3.076   -16.810 15.453  1.00 28.15  ? 282 ILE A CG2 1 
ATOM   2148 C  CD1 . ILE A 1 306 ? 1.156   -18.935 14.013  1.00 30.68  ? 282 ILE A CD1 1 
ATOM   2149 N  N   . VAL A 1 307 ? 2.769   -16.977 18.967  1.00 31.23  ? 283 VAL A N   1 
ATOM   2150 C  CA  . VAL A 1 307 ? 3.072   -15.899 19.905  1.00 32.28  ? 283 VAL A CA  1 
ATOM   2151 C  C   . VAL A 1 307 ? 4.251   -16.283 20.790  1.00 33.56  ? 283 VAL A C   1 
ATOM   2152 O  O   . VAL A 1 307 ? 5.207   -15.517 20.954  1.00 31.64  ? 283 VAL A O   1 
ATOM   2153 C  CB  . VAL A 1 307 ? 1.824   -15.563 20.743  1.00 32.29  ? 283 VAL A CB  1 
ATOM   2154 C  CG1 . VAL A 1 307 ? 2.185   -14.695 21.946  1.00 29.28  ? 283 VAL A CG1 1 
ATOM   2155 C  CG2 . VAL A 1 307 ? 0.783   -14.876 19.878  1.00 28.84  ? 283 VAL A CG2 1 
ATOM   2156 N  N   . GLU A 1 308 ? 4.197   -17.476 21.378  1.00 32.47  ? 284 GLU A N   1 
ATOM   2157 C  CA  . GLU A 1 308 ? 5.232   -17.871 22.324  1.00 36.05  ? 284 GLU A CA  1 
ATOM   2158 C  C   . GLU A 1 308 ? 6.526   -18.246 21.615  1.00 34.71  ? 284 GLU A C   1 
ATOM   2159 O  O   . GLU A 1 308 ? 7.608   -18.114 22.198  1.00 34.65  ? 284 GLU A O   1 
ATOM   2160 C  CB  . GLU A 1 308 ? 4.717   -19.020 23.191  1.00 33.28  ? 284 GLU A CB  1 
ATOM   2161 C  CG  . GLU A 1 308 ? 3.536   -18.603 24.060  1.00 35.71  ? 284 GLU A CG  1 
ATOM   2162 C  CD  . GLU A 1 308 ? 2.940   -19.746 24.857  1.00 39.37  ? 284 GLU A CD  1 
ATOM   2163 O  OE1 . GLU A 1 308 ? 3.281   -20.916 24.581  1.00 38.20  ? 284 GLU A OE1 1 
ATOM   2164 O  OE2 . GLU A 1 308 ? 2.123   -19.467 25.762  1.00 39.59  ? 284 GLU A OE2 1 
ATOM   2165 N  N   . GLY A 1 309 ? 6.440   -18.700 20.363  1.00 32.57  ? 285 GLY A N   1 
ATOM   2166 C  CA  . GLY A 1 309 ? 7.649   -18.921 19.589  1.00 32.25  ? 285 GLY A CA  1 
ATOM   2167 C  C   . GLY A 1 309 ? 8.408   -17.634 19.337  1.00 34.57  ? 285 GLY A C   1 
ATOM   2168 O  O   . GLY A 1 309 ? 9.643   -17.626 19.306  1.00 37.03  ? 285 GLY A O   1 
ATOM   2169 N  N   . LEU A 1 310 ? 7.684   -16.529 19.162  1.00 31.06  ? 286 LEU A N   1 
ATOM   2170 C  CA  . LEU A 1 310 ? 8.302   -15.221 18.990  1.00 33.57  ? 286 LEU A CA  1 
ATOM   2171 C  C   . LEU A 1 310 ? 8.938   -14.695 20.269  1.00 33.76  ? 286 LEU A C   1 
ATOM   2172 O  O   . LEU A 1 310 ? 9.622   -13.667 20.222  1.00 31.73  ? 286 LEU A O   1 
ATOM   2173 C  CB  . LEU A 1 310 ? 7.259   -14.218 18.492  1.00 30.01  ? 286 LEU A CB  1 
ATOM   2174 C  CG  . LEU A 1 310 ? 6.895   -14.307 17.008  1.00 29.99  ? 286 LEU A CG  1 
ATOM   2175 C  CD1 . LEU A 1 310 ? 5.555   -13.632 16.736  1.00 27.58  ? 286 LEU A CD1 1 
ATOM   2176 C  CD2 . LEU A 1 310 ? 7.987   -13.679 16.158  1.00 30.83  ? 286 LEU A CD2 1 
ATOM   2177 N  N   . GLY A 1 311 ? 8.737   -15.366 21.397  1.00 31.91  ? 287 GLY A N   1 
ATOM   2178 C  CA  . GLY A 1 311 ? 9.195   -14.859 22.672  1.00 35.40  ? 287 GLY A CA  1 
ATOM   2179 C  C   . GLY A 1 311 ? 8.234   -13.916 23.352  1.00 32.21  ? 287 GLY A C   1 
ATOM   2180 O  O   . GLY A 1 311 ? 8.618   -13.269 24.333  1.00 35.79  ? 287 GLY A O   1 
ATOM   2181 N  N   . LEU A 1 312 ? 7.002   -13.811 22.861  1.00 30.87  ? 288 LEU A N   1 
ATOM   2182 C  CA  . LEU A 1 312 ? 5.979   -12.962 23.446  1.00 35.20  ? 288 LEU A CA  1 
ATOM   2183 C  C   . LEU A 1 312 ? 5.053   -13.801 24.326  1.00 34.75  ? 288 LEU A C   1 
ATOM   2184 O  O   . LEU A 1 312 ? 5.202   -15.018 24.455  1.00 33.23  ? 288 LEU A O   1 
ATOM   2185 C  CB  . LEU A 1 312 ? 5.192   -12.245 22.347  1.00 34.14  ? 288 LEU A CB  1 
ATOM   2186 C  CG  . LEU A 1 312 ? 6.022   -11.441 21.343  1.00 34.22  ? 288 LEU A CG  1 
ATOM   2187 C  CD1 . LEU A 1 312 ? 5.150   -10.974 20.190  1.00 31.74  ? 288 LEU A CD1 1 
ATOM   2188 C  CD2 . LEU A 1 312 ? 6.688   -10.255 22.019  1.00 33.21  ? 288 LEU A CD2 1 
ATOM   2189 N  N   . GLU A 1 313 ? 4.076   -13.136 24.937  1.00 34.98  ? 289 GLU A N   1 
ATOM   2190 C  CA  . GLU A 1 313 ? 3.133   -13.792 25.828  1.00 37.22  ? 289 GLU A CA  1 
ATOM   2191 C  C   . GLU A 1 313 ? 1.709   -13.436 25.431  1.00 34.40  ? 289 GLU A C   1 
ATOM   2192 O  O   . GLU A 1 313 ? 1.435   -12.335 24.946  1.00 33.83  ? 289 GLU A O   1 
ATOM   2193 C  CB  . GLU A 1 313 ? 3.377   -13.400 27.296  1.00 37.42  ? 289 GLU A CB  1 
ATOM   2194 C  CG  . GLU A 1 313 ? 4.699   -13.904 27.862  1.00 41.83  ? 289 GLU A CG  1 
ATOM   2195 C  CD  . GLU A 1 313 ? 4.927   -13.475 29.298  1.00 48.56  ? 289 GLU A CD  1 
ATOM   2196 O  OE1 . GLU A 1 313 ? 4.159   -12.628 29.799  1.00 56.08  ? 289 GLU A OE1 1 
ATOM   2197 O  OE2 . GLU A 1 313 ? 5.875   -13.986 29.929  1.00 61.34  ? 289 GLU A OE2 1 
ATOM   2198 N  N   . VAL A 1 314 ? 0.808   -14.386 25.642  1.00 35.02  ? 290 VAL A N   1 
ATOM   2199 C  CA  . VAL A 1 314 ? -0.611  -14.167 25.395  1.00 35.06  ? 290 VAL A CA  1 
ATOM   2200 C  C   . VAL A 1 314 ? -1.175  -13.308 26.518  1.00 33.18  ? 290 VAL A C   1 
ATOM   2201 O  O   . VAL A 1 314 ? -0.925  -13.566 27.701  1.00 36.09  ? 290 VAL A O   1 
ATOM   2202 C  CB  . VAL A 1 314 ? -1.351  -15.509 25.287  1.00 37.55  ? 290 VAL A CB  1 
ATOM   2203 C  CG1 . VAL A 1 314 ? -2.849  -15.293 25.222  1.00 38.64  ? 290 VAL A CG1 1 
ATOM   2204 C  CG2 . VAL A 1 314 ? -0.868  -16.277 24.066  1.00 33.16  ? 290 VAL A CG2 1 
ATOM   2205 N  N   . ALA A 1 315 ? -1.929  -12.277 26.150  1.00 34.14  ? 291 ALA A N   1 
ATOM   2206 C  CA  . ALA A 1 315 ? -2.526  -11.398 27.146  1.00 35.30  ? 291 ALA A CA  1 
ATOM   2207 C  C   . ALA A 1 315 ? -3.651  -12.108 27.889  1.00 34.99  ? 291 ALA A C   1 
ATOM   2208 O  O   . ALA A 1 315 ? -4.401  -12.895 27.306  1.00 34.49  ? 291 ALA A O   1 
ATOM   2209 C  CB  . ALA A 1 315 ? -3.067  -10.134 26.482  1.00 34.85  ? 291 ALA A CB  1 
ATOM   2210 N  N   . THR A 1 316 ? -3.763  -11.826 29.185  1.00 35.02  ? 292 THR A N   1 
ATOM   2211 C  CA  . THR A 1 316 ? -4.919  -12.247 29.961  1.00 36.54  ? 292 THR A CA  1 
ATOM   2212 C  C   . THR A 1 316 ? -6.081  -11.300 29.698  1.00 36.28  ? 292 THR A C   1 
ATOM   2213 O  O   . THR A 1 316 ? -5.910  -10.229 29.112  1.00 34.13  ? 292 THR A O   1 
ATOM   2214 C  CB  . THR A 1 316 ? -4.588  -12.264 31.453  1.00 34.46  ? 292 THR A CB  1 
ATOM   2215 O  OG1 . THR A 1 316 ? -4.301  -10.933 31.899  1.00 31.57  ? 292 THR A OG1 1 
ATOM   2216 C  CG2 . THR A 1 316 ? -3.397  -13.168 31.742  1.00 33.55  ? 292 THR A CG2 1 
ATOM   2217 N  N   . PRO A 1 317 ? -7.293  -11.671 30.120  1.00 36.10  ? 293 PRO A N   1 
ATOM   2218 C  CA  . PRO A 1 317 ? -8.415  -10.727 29.991  1.00 36.93  ? 293 PRO A CA  1 
ATOM   2219 C  C   . PRO A 1 317 ? -8.170  -9.415  30.713  1.00 37.14  ? 293 PRO A C   1 
ATOM   2220 O  O   . PRO A 1 317 ? -8.484  -8.346  30.174  1.00 35.39  ? 293 PRO A O   1 
ATOM   2221 C  CB  . PRO A 1 317 ? -9.593  -11.505 30.594  1.00 38.52  ? 293 PRO A CB  1 
ATOM   2222 C  CG  . PRO A 1 317 ? -9.232  -12.937 30.404  1.00 39.00  ? 293 PRO A CG  1 
ATOM   2223 C  CD  . PRO A 1 317 ? -7.738  -13.004 30.563  1.00 34.08  ? 293 PRO A CD  1 
ATOM   2224 N  N   . ALA A 1 318 ? -7.611  -9.466  31.925  1.00 35.32  ? 294 ALA A N   1 
ATOM   2225 C  CA  . ALA A 1 318 ? -7.318  -8.237  32.655  1.00 37.76  ? 294 ALA A CA  1 
ATOM   2226 C  C   . ALA A 1 318 ? -6.314  -7.376  31.900  1.00 36.37  ? 294 ALA A C   1 
ATOM   2227 O  O   . ALA A 1 318 ? -6.425  -6.144  31.891  1.00 38.32  ? 294 ALA A O   1 
ATOM   2228 C  CB  . ALA A 1 318 ? -6.792  -8.568  34.052  1.00 36.92  ? 294 ALA A CB  1 
ATOM   2229 N  N   . GLU A 1 319 ? -5.323  -8.007  31.266  1.00 34.53  ? 295 GLU A N   1 
ATOM   2230 C  CA  . GLU A 1 319 ? -4.349  -7.255  30.483  1.00 35.88  ? 295 GLU A CA  1 
ATOM   2231 C  C   . GLU A 1 319 ? -4.972  -6.692  29.212  1.00 37.45  ? 295 GLU A C   1 
ATOM   2232 O  O   . GLU A 1 319 ? -4.596  -5.600  28.770  1.00 36.04  ? 295 GLU A O   1 
ATOM   2233 C  CB  . GLU A 1 319 ? -3.154  -8.146  30.146  1.00 36.15  ? 295 GLU A CB  1 
ATOM   2234 C  CG  . GLU A 1 319 ? -2.253  -8.435  31.342  1.00 40.22  ? 295 GLU A CG  1 
ATOM   2235 C  CD  . GLU A 1 319 ? -1.277  -9.568  31.089  1.00 41.94  ? 295 GLU A CD  1 
ATOM   2236 O  OE1 . GLU A 1 319 ? -1.452  -10.299 30.090  1.00 38.49  ? 295 GLU A OE1 1 
ATOM   2237 O  OE2 . GLU A 1 319 ? -0.336  -9.727  31.896  1.00 44.00  ? 295 GLU A OE2 1 
ATOM   2238 N  N   . ALA A 1 320 ? -5.920  -7.418  28.616  1.00 34.75  ? 296 ALA A N   1 
ATOM   2239 C  CA  . ALA A 1 320 ? -6.641  -6.885  27.465  1.00 36.40  ? 296 ALA A CA  1 
ATOM   2240 C  C   . ALA A 1 320 ? -7.473  -5.670  27.857  1.00 34.89  ? 296 ALA A C   1 
ATOM   2241 O  O   . ALA A 1 320 ? -7.527  -4.680  27.119  1.00 35.85  ? 296 ALA A O   1 
ATOM   2242 C  CB  . ALA A 1 320 ? -7.528  -7.970  26.855  1.00 34.85  ? 296 ALA A CB  1 
ATOM   2243 N  N   . ARG A 1 321 ? -8.125  -5.727  29.021  1.00 34.30  ? 297 ARG A N   1 
ATOM   2244 C  CA  . ARG A 1 321 ? -8.933  -4.601  29.473  1.00 37.38  ? 297 ARG A CA  1 
ATOM   2245 C  C   . ARG A 1 321 ? -8.092  -3.347  29.665  1.00 37.31  ? 297 ARG A C   1 
ATOM   2246 O  O   . ARG A 1 321 ? -8.581  -2.233  29.447  1.00 35.17  ? 297 ARG A O   1 
ATOM   2247 C  CB  . ARG A 1 321 ? -9.652  -4.962  30.773  1.00 35.24  ? 297 ARG A CB  1 
ATOM   2248 C  CG  . ARG A 1 321 ? -10.713 -6.028  30.591  1.00 36.00  ? 297 ARG A CG  1 
ATOM   2249 C  CD  . ARG A 1 321 ? -11.522 -6.255  31.850  1.00 37.32  ? 297 ARG A CD  1 
ATOM   2250 N  NE  . ARG A 1 321 ? -12.650 -7.139  31.581  1.00 40.92  ? 297 ARG A NE  1 
ATOM   2251 C  CZ  . ARG A 1 321 ? -12.613 -8.461  31.685  1.00 40.34  ? 297 ARG A CZ  1 
ATOM   2252 N  NH1 . ARG A 1 321 ? -11.539 -9.093  32.130  1.00 38.17  ? 297 ARG A NH1 1 
ATOM   2253 N  NH2 . ARG A 1 321 ? -13.683 -9.168  31.333  1.00 38.54  ? 297 ARG A NH2 1 
ATOM   2254 N  N   . GLU A 1 322 ? -6.834  -3.501  30.079  1.00 36.46  ? 298 GLU A N   1 
ATOM   2255 C  CA  . GLU A 1 322 ? -5.983  -2.331  30.257  1.00 39.32  ? 298 GLU A CA  1 
ATOM   2256 C  C   . GLU A 1 322 ? -5.469  -1.813  28.917  1.00 36.15  ? 298 GLU A C   1 
ATOM   2257 O  O   . GLU A 1 322 ? -5.496  -0.604  28.668  1.00 35.97  ? 298 GLU A O   1 
ATOM   2258 C  CB  . GLU A 1 322 ? -4.822  -2.664  31.197  1.00 43.08  ? 298 GLU A CB  1 
ATOM   2259 C  CG  . GLU A 1 322 ? -3.983  -1.457  31.591  1.00 47.43  ? 298 GLU A CG  1 
ATOM   2260 C  CD  . GLU A 1 322 ? -3.154  -1.699  32.839  1.00 60.83  ? 298 GLU A CD  1 
ATOM   2261 O  OE1 . GLU A 1 322 ? -3.688  -2.283  33.805  1.00 66.08  ? 298 GLU A OE1 1 
ATOM   2262 O  OE2 . GLU A 1 322 ? -1.967  -1.306  32.852  1.00 61.09  ? 298 GLU A OE2 1 
ATOM   2263 N  N   . LEU A 1 323 ? -5.017  -2.711  28.036  1.00 35.95  ? 299 LEU A N   1 
ATOM   2264 C  CA  . LEU A 1 323 ? -4.553  -2.282  26.719  1.00 34.98  ? 299 LEU A CA  1 
ATOM   2265 C  C   . LEU A 1 323 ? -5.654  -1.586  25.930  1.00 37.33  ? 299 LEU A C   1 
ATOM   2266 O  O   . LEU A 1 323 ? -5.372  -0.679  25.138  1.00 35.68  ? 299 LEU A O   1 
ATOM   2267 C  CB  . LEU A 1 323 ? -4.031  -3.478  25.919  1.00 33.50  ? 299 LEU A CB  1 
ATOM   2268 C  CG  . LEU A 1 323 ? -2.708  -4.115  26.345  1.00 39.52  ? 299 LEU A CG  1 
ATOM   2269 C  CD1 . LEU A 1 323 ? -2.545  -5.463  25.659  1.00 37.39  ? 299 LEU A CD1 1 
ATOM   2270 C  CD2 . LEU A 1 323 ? -1.532  -3.206  26.017  1.00 36.03  ? 299 LEU A CD2 1 
ATOM   2271 N  N   . LEU A 1 324 ? -6.908  -1.997  26.120  1.00 37.80  ? 300 LEU A N   1 
ATOM   2272 C  CA  . LEU A 1 324 ? -8.023  -1.479  25.340  1.00 35.00  ? 300 LEU A CA  1 
ATOM   2273 C  C   . LEU A 1 324 ? -8.892  -0.499  26.116  1.00 33.72  ? 300 LEU A C   1 
ATOM   2274 O  O   . LEU A 1 324 ? -9.855  0.028   25.553  1.00 35.60  ? 300 LEU A O   1 
ATOM   2275 C  CB  . LEU A 1 324 ? -8.884  -2.639  24.822  1.00 30.41  ? 300 LEU A CB  1 
ATOM   2276 C  CG  . LEU A 1 324 ? -8.146  -3.674  23.964  1.00 37.17  ? 300 LEU A CG  1 
ATOM   2277 C  CD1 . LEU A 1 324 ? -9.073  -4.813  23.563  1.00 34.51  ? 300 LEU A CD1 1 
ATOM   2278 C  CD2 . LEU A 1 324 ? -7.533  -3.029  22.728  1.00 33.17  ? 300 LEU A CD2 1 
ATOM   2279 N  N   . ALA A 1 325 ? -8.582  -0.246  27.389  1.00 36.18  ? 301 ALA A N   1 
ATOM   2280 C  CA  . ALA A 1 325 ? -9.278  0.770   28.181  1.00 35.59  ? 301 ALA A CA  1 
ATOM   2281 C  C   . ALA A 1 325 ? -10.751 0.416   28.383  1.00 37.13  ? 301 ALA A C   1 
ATOM   2282 O  O   . ALA A 1 325 ? -11.632 1.271   28.278  1.00 38.37  ? 301 ALA A O   1 
ATOM   2283 C  CB  . ALA A 1 325 ? -9.144  2.152   27.534  1.00 36.14  ? 301 ALA A CB  1 
ATOM   2284 N  N   . LEU A 1 326 ? -11.023 -0.846  28.693  1.00 36.64  ? 302 LEU A N   1 
ATOM   2285 C  CA  . LEU A 1 326 ? -12.393 -1.318  28.828  1.00 38.10  ? 302 LEU A CA  1 
ATOM   2286 C  C   . LEU A 1 326 ? -12.914 -1.079  30.242  1.00 39.80  ? 302 LEU A C   1 
ATOM   2287 O  O   . LEU A 1 326 ? -12.151 -0.892  31.194  1.00 41.24  ? 302 LEU A O   1 
ATOM   2288 C  CB  . LEU A 1 326 ? -12.484 -2.801  28.470  1.00 36.46  ? 302 LEU A CB  1 
ATOM   2289 C  CG  . LEU A 1 326 ? -11.943 -3.150  27.081  1.00 36.02  ? 302 LEU A CG  1 
ATOM   2290 C  CD1 . LEU A 1 326 ? -12.114 -4.630  26.797  1.00 34.24  ? 302 LEU A CD1 1 
ATOM   2291 C  CD2 . LEU A 1 326 ? -12.618 -2.315  25.997  1.00 34.32  ? 302 LEU A CD2 1 
ATOM   2292 N  N   . LYS A 1 327 ? -14.243 -1.090  30.369  1.00 39.90  ? 303 LYS A N   1 
ATOM   2293 C  CA  . LYS A 1 327 ? -14.897 -0.721  31.618  1.00 42.66  ? 303 LYS A CA  1 
ATOM   2294 C  C   . LYS A 1 327 ? -14.898 -1.838  32.654  1.00 44.47  ? 303 LYS A C   1 
ATOM   2295 O  O   . LYS A 1 327 ? -15.199 -1.570  33.822  1.00 44.24  ? 303 LYS A O   1 
ATOM   2296 C  CB  . LYS A 1 327 ? -16.339 -0.276  31.344  1.00 38.77  ? 303 LYS A CB  1 
ATOM   2297 C  CG  . LYS A 1 327 ? -17.250 -1.358  30.778  1.00 39.55  ? 303 LYS A CG  1 
ATOM   2298 C  CD  . LYS A 1 327 ? -18.665 -0.823  30.573  1.00 40.12  ? 303 LYS A CD  1 
ATOM   2299 C  CE  . LYS A 1 327 ? -19.590 -1.865  29.965  1.00 39.20  ? 303 LYS A CE  1 
ATOM   2300 N  NZ  . LYS A 1 327 ? -21.012 -1.420  29.982  1.00 43.47  ? 303 LYS A NZ  1 
ATOM   2301 N  N   . GLY A 1 328 ? -14.581 -3.063  32.269  1.00 41.16  ? 304 GLY A N   1 
ATOM   2302 C  CA  . GLY A 1 328 ? -14.518 -4.154  33.228  1.00 44.82  ? 304 GLY A CA  1 
ATOM   2303 C  C   . GLY A 1 328 ? -15.671 -5.127  33.056  1.00 45.36  ? 304 GLY A C   1 
ATOM   2304 O  O   . GLY A 1 328 ? -16.799 -4.740  32.727  1.00 43.28  ? 304 GLY A O   1 
ATOM   2305 N  N   . GLY A 1 329 ? -15.384 -6.411  33.285  1.00 45.89  ? 305 GLY A N   1 
ATOM   2306 C  CA  . GLY A 1 329 ? -16.387 -7.444  33.110  1.00 43.75  ? 305 GLY A CA  1 
ATOM   2307 C  C   . GLY A 1 329 ? -17.539 -7.359  34.087  1.00 50.96  ? 305 GLY A C   1 
ATOM   2308 O  O   . GLY A 1 329 ? -18.577 -7.986  33.855  1.00 48.79  ? 305 GLY A O   1 
ATOM   2309 N  N   . ASP A 1 330 ? -17.381 -6.601  35.170  1.00 52.29  ? 306 ASP A N   1 
ATOM   2310 C  CA  . ASP A 1 330 ? -18.435 -6.429  36.162  1.00 54.63  ? 306 ASP A CA  1 
ATOM   2311 C  C   . ASP A 1 330 ? -19.310 -5.211  35.893  1.00 54.23  ? 306 ASP A C   1 
ATOM   2312 O  O   . ASP A 1 330 ? -20.190 -4.906  36.705  1.00 54.75  ? 306 ASP A O   1 
ATOM   2313 C  CB  . ASP A 1 330 ? -17.828 -6.316  37.563  1.00 58.66  ? 306 ASP A CB  1 
ATOM   2314 C  CG  . ASP A 1 330 ? -16.918 -5.112  37.708  1.00 62.23  ? 306 ASP A CG  1 
ATOM   2315 O  OD1 . ASP A 1 330 ? -16.092 -4.878  36.799  1.00 58.52  ? 306 ASP A OD1 1 
ATOM   2316 O  OD2 . ASP A 1 330 ? -17.035 -4.397  38.725  1.00 67.91  ? 306 ASP A OD2 1 
ATOM   2317 N  N   . GLN A 1 331 ? -19.091 -4.510  34.780  1.00 49.71  ? 307 GLN A N   1 
ATOM   2318 C  CA  . GLN A 1 331 ? -19.851 -3.317  34.429  1.00 50.67  ? 307 GLN A CA  1 
ATOM   2319 C  C   . GLN A 1 331 ? -20.740 -3.552  33.212  1.00 47.23  ? 307 GLN A C   1 
ATOM   2320 O  O   . GLN A 1 331 ? -21.017 -2.625  32.448  1.00 46.72  ? 307 GLN A O   1 
ATOM   2321 C  CB  . GLN A 1 331 ? -18.905 -2.142  34.182  1.00 49.45  ? 307 GLN A CB  1 
ATOM   2322 C  CG  . GLN A 1 331 ? -18.176 -1.664  35.430  1.00 51.89  ? 307 GLN A CG  1 
ATOM   2323 C  CD  . GLN A 1 331 ? -19.117 -1.074  36.464  1.00 58.62  ? 307 GLN A CD  1 
ATOM   2324 O  OE1 . GLN A 1 331 ? -19.946 -0.221  36.150  1.00 63.51  ? 307 GLN A OE1 1 
ATOM   2325 N  NE2 . GLN A 1 331 ? -18.997 -1.533  37.704  1.00 62.38  ? 307 GLN A NE2 1 
ATOM   2326 N  N   . VAL A 1 332 ? -21.192 -4.788  33.026  1.00 44.86  ? 308 VAL A N   1 
ATOM   2327 C  CA  . VAL A 1 332 ? -22.022 -5.157  31.892  1.00 46.29  ? 308 VAL A CA  1 
ATOM   2328 C  C   . VAL A 1 332 ? -23.417 -5.504  32.403  1.00 46.49  ? 308 VAL A C   1 
ATOM   2329 O  O   . VAL A 1 332 ? -23.644 -5.669  33.601  1.00 49.00  ? 308 VAL A O   1 
ATOM   2330 C  CB  . VAL A 1 332 ? -21.416 -6.328  31.092  1.00 43.51  ? 308 VAL A CB  1 
ATOM   2331 C  CG1 . VAL A 1 332 ? -19.981 -6.013  30.699  1.00 42.19  ? 308 VAL A CG1 1 
ATOM   2332 C  CG2 . VAL A 1 332 ? -21.480 -7.615  31.899  1.00 43.78  ? 308 VAL A CG2 1 
ATOM   2333 N  N   . ASN A 1 333 ? -24.361 -5.614  31.473  1.00 43.86  ? 309 ASN A N   1 
ATOM   2334 C  CA  . ASN A 1 333 ? -25.745 -5.941  31.816  1.00 45.73  ? 309 ASN A CA  1 
ATOM   2335 C  C   . ASN A 1 333 ? -26.062 -7.400  31.493  1.00 43.78  ? 309 ASN A C   1 
ATOM   2336 O  O   . ASN A 1 333 ? -26.993 -7.706  30.753  1.00 45.68  ? 309 ASN A O   1 
ATOM   2337 C  CB  . ASN A 1 333 ? -26.708 -5.008  31.092  1.00 44.26  ? 309 ASN A CB  1 
ATOM   2338 C  CG  . ASN A 1 333 ? -28.132 -5.138  31.600  1.00 49.15  ? 309 ASN A CG  1 
ATOM   2339 O  OD1 . ASN A 1 333 ? -28.361 -5.374  32.786  1.00 47.90  ? 309 ASN A OD1 1 
ATOM   2340 N  ND2 . ASN A 1 333 ? -29.098 -4.988  30.702  1.00 45.74  ? 309 ASN A ND2 1 
ATOM   2341 N  N   . PHE A 1 334 ? -25.264 -8.307  32.043  1.00 42.75  ? 310 PHE A N   1 
ATOM   2342 C  CA  . PHE A 1 334 ? -25.568 -9.731  31.999  1.00 43.73  ? 310 PHE A CA  1 
ATOM   2343 C  C   . PHE A 1 334 ? -24.745 -10.448 33.063  1.00 47.66  ? 310 PHE A C   1 
ATOM   2344 O  O   . PHE A 1 334 ? -24.805 -11.669 33.203  1.00 48.57  ? 310 PHE A O   1 
ATOM   2345 C  CB  . PHE A 1 334 ? -25.297 -10.324 30.611  1.00 42.64  ? 310 PHE A CB  1 
ATOM   2346 C  CG  . PHE A 1 334 ? -23.935 -10.002 30.053  1.00 42.26  ? 310 PHE A CG  1 
ATOM   2347 C  CD1 . PHE A 1 334 ? -22.833 -10.783 30.371  1.00 43.72  ? 310 PHE A CD1 1 
ATOM   2348 C  CD2 . PHE A 1 334 ? -23.763 -8.935  29.186  1.00 42.02  ? 310 PHE A CD2 1 
ATOM   2349 C  CE1 . PHE A 1 334 ? -21.585 -10.492 29.847  1.00 41.03  ? 310 PHE A CE1 1 
ATOM   2350 C  CE2 . PHE A 1 334 ? -22.517 -8.642  28.659  1.00 41.19  ? 310 PHE A CE2 1 
ATOM   2351 C  CZ  . PHE A 1 334 ? -21.429 -9.422  28.990  1.00 38.57  ? 310 PHE A CZ  1 
ATOM   2352 O  OXT . PHE A 1 334 ? -24.000 -9.812  33.809  1.00 49.06  ? 310 PHE A OXT 1 
ATOM   2353 N  N   . LEU B 1 27  ? 6.660   -30.044 -1.592  1.00 73.44  ? 3   LEU B N   1 
ATOM   2354 C  CA  . LEU B 1 27  ? 7.635   -29.100 -1.057  1.00 72.06  ? 3   LEU B CA  1 
ATOM   2355 C  C   . LEU B 1 27  ? 7.010   -27.737 -0.786  1.00 71.34  ? 3   LEU B C   1 
ATOM   2356 O  O   . LEU B 1 27  ? 7.697   -26.805 -0.367  1.00 65.53  ? 3   LEU B O   1 
ATOM   2357 C  CB  . LEU B 1 27  ? 8.804   -28.925 -2.029  1.00 69.83  ? 3   LEU B CB  1 
ATOM   2358 C  CG  . LEU B 1 27  ? 9.715   -30.119 -2.313  1.00 70.14  ? 3   LEU B CG  1 
ATOM   2359 C  CD1 . LEU B 1 27  ? 10.709  -29.752 -3.404  1.00 65.48  ? 3   LEU B CD1 1 
ATOM   2360 C  CD2 . LEU B 1 27  ? 10.441  -30.559 -1.055  1.00 62.35  ? 3   LEU B CD2 1 
ATOM   2361 N  N   . ASN B 1 28  ? 5.702   -27.624 -1.020  1.00 78.03  ? 4   ASN B N   1 
ATOM   2362 C  CA  . ASN B 1 28  ? 5.079   -26.306 -1.093  1.00 79.87  ? 4   ASN B CA  1 
ATOM   2363 C  C   . ASN B 1 28  ? 5.041   -25.608 0.262   1.00 73.38  ? 4   ASN B C   1 
ATOM   2364 O  O   . ASN B 1 28  ? 5.179   -24.381 0.327   1.00 71.77  ? 4   ASN B O   1 
ATOM   2365 C  CB  . ASN B 1 28  ? 3.671   -26.434 -1.670  1.00 87.74  ? 4   ASN B CB  1 
ATOM   2366 C  CG  . ASN B 1 28  ? 3.666   -27.067 -3.047  1.00 95.18  ? 4   ASN B CG  1 
ATOM   2367 O  OD1 . ASN B 1 28  ? 3.213   -28.198 -3.221  1.00 100.96 ? 4   ASN B OD1 1 
ATOM   2368 N  ND2 . ASN B 1 28  ? 4.174   -26.339 -4.035  1.00 99.33  ? 4   ASN B ND2 1 
ATOM   2369 N  N   . GLY B 1 29  ? 4.853   -26.357 1.347   1.00 59.30  ? 5   GLY B N   1 
ATOM   2370 C  CA  . GLY B 1 29  ? 4.775   -25.758 2.666   1.00 53.77  ? 5   GLY B CA  1 
ATOM   2371 C  C   . GLY B 1 29  ? 5.946   -26.123 3.554   1.00 50.15  ? 5   GLY B C   1 
ATOM   2372 O  O   . GLY B 1 29  ? 5.772   -26.380 4.749   1.00 44.56  ? 5   GLY B O   1 
ATOM   2373 N  N   . LYS B 1 30  ? 7.145   -26.148 2.980   1.00 44.02  ? 6   LYS B N   1 
ATOM   2374 C  CA  . LYS B 1 30  ? 8.364   -26.495 3.697   1.00 42.03  ? 6   LYS B CA  1 
ATOM   2375 C  C   . LYS B 1 30  ? 9.216   -25.246 3.873   1.00 39.88  ? 6   LYS B C   1 
ATOM   2376 O  O   . LYS B 1 30  ? 9.410   -24.484 2.920   1.00 41.01  ? 6   LYS B O   1 
ATOM   2377 C  CB  . LYS B 1 30  ? 9.150   -27.573 2.948   1.00 45.60  ? 6   LYS B CB  1 
ATOM   2378 C  CG  . LYS B 1 30  ? 8.362   -28.856 2.694   1.00 47.55  ? 6   LYS B CG  1 
ATOM   2379 C  CD  . LYS B 1 30  ? 8.159   -29.650 3.973   1.00 46.84  ? 6   LYS B CD  1 
ATOM   2380 C  CE  . LYS B 1 30  ? 7.417   -30.953 3.714   1.00 52.43  ? 6   LYS B CE  1 
ATOM   2381 N  NZ  . LYS B 1 30  ? 5.991   -30.726 3.347   1.00 55.62  ? 6   LYS B NZ  1 
ATOM   2382 N  N   . VAL B 1 31  ? 9.725   -25.042 5.086   1.00 34.45  ? 7   VAL B N   1 
ATOM   2383 C  CA  . VAL B 1 31  ? 10.516  -23.865 5.432   1.00 32.65  ? 7   VAL B CA  1 
ATOM   2384 C  C   . VAL B 1 31  ? 11.924  -24.327 5.783   1.00 33.24  ? 7   VAL B C   1 
ATOM   2385 O  O   . VAL B 1 31  ? 12.110  -25.116 6.717   1.00 33.41  ? 7   VAL B O   1 
ATOM   2386 C  CB  . VAL B 1 31  ? 9.891   -23.077 6.594   1.00 30.31  ? 7   VAL B CB  1 
ATOM   2387 C  CG1 . VAL B 1 31  ? 10.739  -21.856 6.933   1.00 30.29  ? 7   VAL B CG1 1 
ATOM   2388 C  CG2 . VAL B 1 31  ? 8.460   -22.663 6.251   1.00 34.85  ? 7   VAL B CG2 1 
ATOM   2389 N  N   . ILE B 1 32  ? 12.909  -23.845 5.028   1.00 29.70  ? 8   ILE B N   1 
ATOM   2390 C  CA  . ILE B 1 32  ? 14.312  -24.129 5.307   1.00 30.10  ? 8   ILE B CA  1 
ATOM   2391 C  C   . ILE B 1 32  ? 14.752  -23.257 6.474   1.00 26.69  ? 8   ILE B C   1 
ATOM   2392 O  O   . ILE B 1 32  ? 14.642  -22.027 6.414   1.00 24.75  ? 8   ILE B O   1 
ATOM   2393 C  CB  . ILE B 1 32  ? 15.194  -23.861 4.079   1.00 31.40  ? 8   ILE B CB  1 
ATOM   2394 C  CG1 . ILE B 1 32  ? 14.695  -24.628 2.854   1.00 31.94  ? 8   ILE B CG1 1 
ATOM   2395 C  CG2 . ILE B 1 32  ? 16.648  -24.229 4.389   1.00 29.53  ? 8   ILE B CG2 1 
ATOM   2396 C  CD1 . ILE B 1 32  ? 15.348  -24.172 1.562   1.00 29.68  ? 8   ILE B CD1 1 
ATOM   2397 N  N   . ILE B 1 33  ? 15.259  -23.884 7.528   1.00 26.88  ? 9   ILE B N   1 
ATOM   2398 C  CA  . ILE B 1 33  ? 15.919  -23.168 8.612   1.00 27.90  ? 9   ILE B CA  1 
ATOM   2399 C  C   . ILE B 1 33  ? 17.423  -23.298 8.410   1.00 28.75  ? 9   ILE B C   1 
ATOM   2400 O  O   . ILE B 1 33  ? 17.964  -24.411 8.406   1.00 27.94  ? 9   ILE B O   1 
ATOM   2401 C  CB  . ILE B 1 33  ? 15.504  -23.701 9.992   1.00 29.62  ? 9   ILE B CB  1 
ATOM   2402 C  CG1 . ILE B 1 33  ? 13.995  -23.552 10.196  1.00 28.91  ? 9   ILE B CG1 1 
ATOM   2403 C  CG2 . ILE B 1 33  ? 16.272  -22.957 11.085  1.00 27.30  ? 9   ILE B CG2 1 
ATOM   2404 C  CD1 . ILE B 1 33  ? 13.494  -24.165 11.491  1.00 27.91  ? 9   ILE B CD1 1 
ATOM   2405 N  N   . THR B 1 34  ? 18.087  -22.163 8.219   1.00 26.79  ? 10  THR B N   1 
ATOM   2406 C  CA  . THR B 1 34  ? 19.539  -22.075 8.237   1.00 28.04  ? 10  THR B CA  1 
ATOM   2407 C  C   . THR B 1 34  ? 19.984  -21.611 9.617   1.00 29.86  ? 10  THR B C   1 
ATOM   2408 O  O   . THR B 1 34  ? 19.386  -20.702 10.197  1.00 29.95  ? 10  THR B O   1 
ATOM   2409 C  CB  . THR B 1 34  ? 20.051  -21.097 7.175   1.00 29.88  ? 10  THR B CB  1 
ATOM   2410 O  OG1 . THR B 1 34  ? 19.743  -21.593 5.865   1.00 30.42  ? 10  THR B OG1 1 
ATOM   2411 C  CG2 . THR B 1 34  ? 21.563  -20.900 7.307   1.00 31.80  ? 10  THR B CG2 1 
ATOM   2412 N  N   . CYS B 1 35  ? 21.031  -22.237 10.145  1.00 31.21  ? 11  CYS B N   1 
ATOM   2413 C  CA  . CYS B 1 35  ? 21.592  -21.842 11.430  1.00 31.72  ? 11  CYS B CA  1 
ATOM   2414 C  C   . CYS B 1 35  ? 23.043  -21.432 11.235  1.00 32.04  ? 11  CYS B C   1 
ATOM   2415 O  O   . CYS B 1 35  ? 23.872  -22.242 10.804  1.00 33.00  ? 11  CYS B O   1 
ATOM   2416 C  CB  . CYS B 1 35  ? 21.486  -22.966 12.459  1.00 30.91  ? 11  CYS B CB  1 
ATOM   2417 S  SG  . CYS B 1 35  ? 21.882  -22.410 14.129  1.00 37.23  ? 11  CYS B SG  1 
ATOM   2418 N  N   . ALA B 1 36  ? 23.340  -20.174 11.547  1.00 30.59  ? 12  ALA B N   1 
ATOM   2419 C  CA  . ALA B 1 36  ? 24.692  -19.633 11.489  1.00 32.33  ? 12  ALA B CA  1 
ATOM   2420 C  C   . ALA B 1 36  ? 25.267  -19.669 12.902  1.00 28.91  ? 12  ALA B C   1 
ATOM   2421 O  O   . ALA B 1 36  ? 24.855  -18.887 13.764  1.00 28.74  ? 12  ALA B O   1 
ATOM   2422 C  CB  . ALA B 1 36  ? 24.670  -18.216 10.921  1.00 30.54  ? 12  ALA B CB  1 
ATOM   2423 N  N   . VAL B 1 37  ? 26.229  -20.563 13.137  1.00 28.56  ? 13  VAL B N   1 
ATOM   2424 C  CA  . VAL B 1 37  ? 26.534  -20.948 14.509  1.00 31.68  ? 13  VAL B CA  1 
ATOM   2425 C  C   . VAL B 1 37  ? 27.517  -20.017 15.222  1.00 30.07  ? 13  VAL B C   1 
ATOM   2426 O  O   . VAL B 1 37  ? 27.505  -19.971 16.457  1.00 29.63  ? 13  VAL B O   1 
ATOM   2427 C  CB  . VAL B 1 37  ? 27.050  -22.401 14.562  1.00 34.77  ? 13  VAL B CB  1 
ATOM   2428 C  CG1 . VAL B 1 37  ? 25.967  -23.356 14.080  1.00 32.21  ? 13  VAL B CG1 1 
ATOM   2429 C  CG2 . VAL B 1 37  ? 28.324  -22.563 13.739  1.00 31.37  ? 13  VAL B CG2 1 
ATOM   2430 N  N   . THR B 1 38  ? 28.365  -19.268 14.508  1.00 31.21  ? 14  THR B N   1 
ATOM   2431 C  CA  . THR B 1 38  ? 29.284  -18.392 15.241  1.00 31.56  ? 14  THR B CA  1 
ATOM   2432 C  C   . THR B 1 38  ? 29.691  -17.137 14.469  1.00 32.58  ? 14  THR B C   1 
ATOM   2433 O  O   . THR B 1 38  ? 29.769  -16.050 15.053  1.00 30.86  ? 14  THR B O   1 
ATOM   2434 C  CB  . THR B 1 38  ? 30.527  -19.184 15.676  1.00 35.22  ? 14  THR B CB  1 
ATOM   2435 O  OG1 . THR B 1 38  ? 31.306  -18.392 16.583  1.00 34.51  ? 14  THR B OG1 1 
ATOM   2436 C  CG2 . THR B 1 38  ? 31.389  -19.588 14.481  1.00 33.06  ? 14  THR B CG2 1 
ATOM   2437 N  N   . GLY B 1 39  ? 29.960  -17.259 13.174  1.00 31.98  ? 15  GLY B N   1 
ATOM   2438 C  CA  . GLY B 1 39  ? 30.238  -16.058 12.402  1.00 31.23  ? 15  GLY B CA  1 
ATOM   2439 C  C   . GLY B 1 39  ? 31.572  -15.395 12.732  1.00 36.43  ? 15  GLY B C   1 
ATOM   2440 O  O   . GLY B 1 39  ? 32.513  -16.012 13.245  1.00 31.23  ? 15  GLY B O   1 
ATOM   2441 N  N   . ALA B 1 40  ? 31.633  -14.093 12.418  1.00 38.02  ? 16  ALA B N   1 
ATOM   2442 C  CA  . ALA B 1 40  ? 32.831  -13.298 12.649  1.00 39.30  ? 16  ALA B CA  1 
ATOM   2443 C  C   . ALA B 1 40  ? 32.551  -11.913 13.220  1.00 40.51  ? 16  ALA B C   1 
ATOM   2444 O  O   . ALA B 1 40  ? 33.503  -11.153 13.427  1.00 39.16  ? 16  ALA B O   1 
ATOM   2445 C  CB  . ALA B 1 40  ? 33.629  -13.143 11.341  1.00 40.70  ? 16  ALA B CB  1 
ATOM   2446 N  N   . ILE B 1 41  ? 31.296  -11.556 13.474  1.00 33.52  ? 17  ILE B N   1 
ATOM   2447 C  CA  . ILE B 1 41  ? 30.969  -10.230 13.994  1.00 38.45  ? 17  ILE B CA  1 
ATOM   2448 C  C   . ILE B 1 41  ? 30.996  -10.206 15.518  1.00 39.50  ? 17  ILE B C   1 
ATOM   2449 O  O   . ILE B 1 41  ? 31.670  -9.368  16.122  1.00 42.33  ? 17  ILE B O   1 
ATOM   2450 C  CB  . ILE B 1 41  ? 29.599  -9.774  13.454  1.00 42.46  ? 17  ILE B CB  1 
ATOM   2451 C  CG1 . ILE B 1 41  ? 29.623  -9.675  11.925  1.00 46.62  ? 17  ILE B CG1 1 
ATOM   2452 C  CG2 . ILE B 1 41  ? 29.197  -8.449  14.083  1.00 43.17  ? 17  ILE B CG2 1 
ATOM   2453 C  CD1 . ILE B 1 41  ? 30.754  -8.843  11.364  1.00 49.72  ? 17  ILE B CD1 1 
ATOM   2454 N  N   . HIS B 1 42  ? 30.242  -11.092 16.162  1.00 37.03  ? 18  HIS B N   1 
ATOM   2455 C  CA  . HIS B 1 42  ? 30.282  -11.189 17.611  1.00 37.02  ? 18  HIS B CA  1 
ATOM   2456 C  C   . HIS B 1 42  ? 31.649  -11.687 18.059  1.00 39.29  ? 18  HIS B C   1 
ATOM   2457 O  O   . HIS B 1 42  ? 32.358  -12.373 17.318  1.00 34.84  ? 18  HIS B O   1 
ATOM   2458 C  CB  . HIS B 1 42  ? 29.190  -12.131 18.115  1.00 35.93  ? 18  HIS B CB  1 
ATOM   2459 C  CG  . HIS B 1 42  ? 27.801  -11.656 17.819  1.00 39.23  ? 18  HIS B CG  1 
ATOM   2460 N  ND1 . HIS B 1 42  ? 26.784  -12.511 17.454  1.00 36.69  ? 18  HIS B ND1 1 
ATOM   2461 C  CD2 . HIS B 1 42  ? 27.260  -10.415 17.837  1.00 40.03  ? 18  HIS B CD2 1 
ATOM   2462 C  CE1 . HIS B 1 42  ? 25.676  -11.818 17.260  1.00 38.17  ? 18  HIS B CE1 1 
ATOM   2463 N  NE2 . HIS B 1 42  ? 25.938  -10.543 17.486  1.00 41.00  ? 18  HIS B NE2 1 
ATOM   2464 N  N   . THR B 1 43  ? 32.017  -11.335 19.283  1.00 36.87  ? 19  THR B N   1 
ATOM   2465 C  CA  . THR B 1 43  ? 33.300  -11.698 19.856  1.00 41.48  ? 19  THR B CA  1 
ATOM   2466 C  C   . THR B 1 43  ? 33.086  -12.463 21.156  1.00 41.47  ? 19  THR B C   1 
ATOM   2467 O  O   . THR B 1 43  ? 32.020  -12.369 21.776  1.00 39.83  ? 19  THR B O   1 
ATOM   2468 C  CB  . THR B 1 43  ? 34.159  -10.451 20.112  1.00 41.60  ? 19  THR B CB  1 
ATOM   2469 O  OG1 . THR B 1 43  ? 33.571  -9.662  21.152  1.00 40.03  ? 19  THR B OG1 1 
ATOM   2470 C  CG2 . THR B 1 43  ? 34.270  -9.610  18.841  1.00 43.92  ? 19  THR B CG2 1 
ATOM   2471 N  N   . PRO B 1 44  ? 34.083  -13.231 21.602  1.00 40.02  ? 20  PRO B N   1 
ATOM   2472 C  CA  . PRO B 1 44  ? 33.852  -14.136 22.740  1.00 41.19  ? 20  PRO B CA  1 
ATOM   2473 C  C   . PRO B 1 44  ? 33.538  -13.421 24.042  1.00 41.55  ? 20  PRO B C   1 
ATOM   2474 O  O   . PRO B 1 44  ? 32.826  -13.981 24.884  1.00 42.68  ? 20  PRO B O   1 
ATOM   2475 C  CB  . PRO B 1 44  ? 35.167  -14.925 22.838  1.00 40.46  ? 20  PRO B CB  1 
ATOM   2476 C  CG  . PRO B 1 44  ? 35.877  -14.693 21.545  1.00 44.05  ? 20  PRO B CG  1 
ATOM   2477 C  CD  . PRO B 1 44  ? 35.450  -13.350 21.068  1.00 43.35  ? 20  PRO B CD  1 
ATOM   2478 N  N   . SER B 1 45  ? 34.053  -12.207 24.245  1.00 39.62  ? 21  SER B N   1 
ATOM   2479 C  CA  . SER B 1 45  ? 33.737  -11.471 25.463  1.00 45.35  ? 21  SER B CA  1 
ATOM   2480 C  C   . SER B 1 45  ? 32.263  -11.097 25.544  1.00 42.83  ? 21  SER B C   1 
ATOM   2481 O  O   . SER B 1 45  ? 31.779  -10.767 26.633  1.00 44.01  ? 21  SER B O   1 
ATOM   2482 C  CB  . SER B 1 45  ? 34.590  -10.207 25.553  1.00 47.31  ? 21  SER B CB  1 
ATOM   2483 O  OG  . SER B 1 45  ? 35.955  -10.529 25.737  1.00 47.29  ? 21  SER B OG  1 
ATOM   2484 N  N   . MET B 1 46  ? 31.539  -11.142 24.424  1.00 39.67  ? 22  MET B N   1 
ATOM   2485 C  CA  . MET B 1 46  ? 30.131  -10.763 24.434  1.00 42.03  ? 22  MET B CA  1 
ATOM   2486 C  C   . MET B 1 46  ? 29.249  -11.849 25.034  1.00 40.97  ? 22  MET B C   1 
ATOM   2487 O  O   . MET B 1 46  ? 28.196  -11.540 25.601  1.00 42.18  ? 22  MET B O   1 
ATOM   2488 C  CB  . MET B 1 46  ? 29.661  -10.449 23.014  1.00 41.50  ? 22  MET B CB  1 
ATOM   2489 C  CG  . MET B 1 46  ? 30.400  -9.302  22.354  1.00 40.63  ? 22  MET B CG  1 
ATOM   2490 S  SD  . MET B 1 46  ? 29.857  -9.039  20.658  1.00 42.80  ? 22  MET B SD  1 
ATOM   2491 C  CE  . MET B 1 46  ? 30.957  -7.723  20.144  1.00 45.42  ? 22  MET B CE  1 
ATOM   2492 N  N   . SER B 1 47  ? 29.650  -13.111 24.918  1.00 37.74  ? 23  SER B N   1 
ATOM   2493 C  CA  . SER B 1 47  ? 28.849  -14.212 25.434  1.00 40.39  ? 23  SER B CA  1 
ATOM   2494 C  C   . SER B 1 47  ? 29.709  -15.458 25.605  1.00 41.06  ? 23  SER B C   1 
ATOM   2495 O  O   . SER B 1 47  ? 30.429  -15.845 24.675  1.00 37.03  ? 23  SER B O   1 
ATOM   2496 C  CB  . SER B 1 47  ? 27.677  -14.506 24.496  1.00 37.67  ? 23  SER B CB  1 
ATOM   2497 O  OG  . SER B 1 47  ? 26.959  -15.654 24.918  1.00 36.29  ? 23  SER B OG  1 
ATOM   2498 N  N   . PRO B 1 48  ? 29.662  -16.120 26.766  1.00 39.52  ? 24  PRO B N   1 
ATOM   2499 C  CA  . PRO B 1 48  ? 30.405  -17.380 26.921  1.00 40.40  ? 24  PRO B CA  1 
ATOM   2500 C  C   . PRO B 1 48  ? 29.841  -18.514 26.087  1.00 39.56  ? 24  PRO B C   1 
ATOM   2501 O  O   . PRO B 1 48  ? 30.497  -19.557 25.966  1.00 39.49  ? 24  PRO B O   1 
ATOM   2502 C  CB  . PRO B 1 48  ? 30.278  -17.679 28.420  1.00 38.16  ? 24  PRO B CB  1 
ATOM   2503 C  CG  . PRO B 1 48  ? 28.987  -17.043 28.809  1.00 40.83  ? 24  PRO B CG  1 
ATOM   2504 C  CD  . PRO B 1 48  ? 28.860  -15.804 27.963  1.00 38.06  ? 24  PRO B CD  1 
ATOM   2505 N  N   . TYR B 1 49  ? 28.654  -18.344 25.512  1.00 37.13  ? 25  TYR B N   1 
ATOM   2506 C  CA  . TYR B 1 49  ? 28.016  -19.380 24.713  1.00 39.53  ? 25  TYR B CA  1 
ATOM   2507 C  C   . TYR B 1 49  ? 28.363  -19.289 23.233  1.00 38.34  ? 25  TYR B C   1 
ATOM   2508 O  O   . TYR B 1 49  ? 27.967  -20.173 22.464  1.00 37.78  ? 25  TYR B O   1 
ATOM   2509 C  CB  . TYR B 1 49  ? 26.496  -19.306 24.895  1.00 37.47  ? 25  TYR B CB  1 
ATOM   2510 C  CG  . TYR B 1 49  ? 26.076  -19.313 26.349  1.00 41.10  ? 25  TYR B CG  1 
ATOM   2511 C  CD1 . TYR B 1 49  ? 26.124  -20.482 27.099  1.00 41.87  ? 25  TYR B CD1 1 
ATOM   2512 C  CD2 . TYR B 1 49  ? 25.637  -18.153 26.972  1.00 39.25  ? 25  TYR B CD2 1 
ATOM   2513 C  CE1 . TYR B 1 49  ? 25.745  -20.494 28.428  1.00 43.68  ? 25  TYR B CE1 1 
ATOM   2514 C  CE2 . TYR B 1 49  ? 25.255  -18.156 28.301  1.00 42.42  ? 25  TYR B CE2 1 
ATOM   2515 C  CZ  . TYR B 1 49  ? 25.310  -19.329 29.023  1.00 43.92  ? 25  TYR B CZ  1 
ATOM   2516 O  OH  . TYR B 1 49  ? 24.930  -19.334 30.346  1.00 47.31  ? 25  TYR B OH  1 
ATOM   2517 N  N   . LEU B 1 50  ? 29.085  -18.258 22.816  1.00 39.20  ? 26  LEU B N   1 
ATOM   2518 C  CA  . LEU B 1 50  ? 29.520  -18.160 21.427  1.00 39.81  ? 26  LEU B CA  1 
ATOM   2519 C  C   . LEU B 1 50  ? 30.524  -19.268 21.129  1.00 36.89  ? 26  LEU B C   1 
ATOM   2520 O  O   . LEU B 1 50  ? 31.577  -19.318 21.774  1.00 39.75  ? 26  LEU B O   1 
ATOM   2521 C  CB  . LEU B 1 50  ? 30.149  -16.799 21.159  1.00 37.00  ? 26  LEU B CB  1 
ATOM   2522 C  CG  . LEU B 1 50  ? 30.558  -16.552 19.705  1.00 37.68  ? 26  LEU B CG  1 
ATOM   2523 C  CD1 . LEU B 1 50  ? 29.328  -16.382 18.827  1.00 36.05  ? 26  LEU B CD1 1 
ATOM   2524 C  CD2 . LEU B 1 50  ? 31.475  -15.346 19.597  1.00 37.68  ? 26  LEU B CD2 1 
ATOM   2525 N  N   . PRO B 1 51  ? 30.255  -20.166 20.180  1.00 38.68  ? 27  PRO B N   1 
ATOM   2526 C  CA  . PRO B 1 51  ? 31.232  -21.222 19.881  1.00 38.48  ? 27  PRO B CA  1 
ATOM   2527 C  C   . PRO B 1 51  ? 32.533  -20.634 19.356  1.00 40.08  ? 27  PRO B C   1 
ATOM   2528 O  O   . PRO B 1 51  ? 32.534  -19.706 18.544  1.00 38.43  ? 27  PRO B O   1 
ATOM   2529 C  CB  . PRO B 1 51  ? 30.527  -22.074 18.816  1.00 37.06  ? 27  PRO B CB  1 
ATOM   2530 C  CG  . PRO B 1 51  ? 29.082  -21.725 18.919  1.00 35.07  ? 27  PRO B CG  1 
ATOM   2531 C  CD  . PRO B 1 51  ? 29.032  -20.304 19.372  1.00 34.26  ? 27  PRO B CD  1 
ATOM   2532 N  N   . VAL B 1 52  ? 33.651  -21.187 19.827  1.00 39.21  ? 28  VAL B N   1 
ATOM   2533 C  CA  . VAL B 1 52  ? 34.972  -20.717 19.419  1.00 41.41  ? 28  VAL B CA  1 
ATOM   2534 C  C   . VAL B 1 52  ? 35.807  -21.885 18.911  1.00 42.70  ? 28  VAL B C   1 
ATOM   2535 O  O   . VAL B 1 52  ? 36.187  -21.926 17.735  1.00 42.40  ? 28  VAL B O   1 
ATOM   2536 C  CB  . VAL B 1 52  ? 35.694  -20.004 20.577  1.00 40.64  ? 28  VAL B CB  1 
ATOM   2537 C  CG1 . VAL B 1 52  ? 37.130  -19.669 20.178  1.00 44.06  ? 28  VAL B CG1 1 
ATOM   2538 C  CG2 . VAL B 1 52  ? 34.937  -18.751 20.981  1.00 40.54  ? 28  VAL B CG2 1 
ATOM   2539 N  N   . SER B 1 53  ? 36.110  -22.832 19.795  1.00 42.25  ? 29  SER B N   1 
ATOM   2540 C  CA  . SER B 1 53  ? 36.929  -23.969 19.409  1.00 46.90  ? 29  SER B CA  1 
ATOM   2541 C  C   . SER B 1 53  ? 36.232  -24.783 18.324  1.00 46.63  ? 29  SER B C   1 
ATOM   2542 O  O   . SER B 1 53  ? 35.018  -24.686 18.112  1.00 42.10  ? 29  SER B O   1 
ATOM   2543 C  CB  . SER B 1 53  ? 37.225  -24.857 20.617  1.00 45.89  ? 29  SER B CB  1 
ATOM   2544 O  OG  . SER B 1 53  ? 36.050  -25.505 21.071  1.00 46.71  ? 29  SER B OG  1 
ATOM   2545 N  N   . ALA B 1 54  ? 37.026  -25.599 17.628  1.00 43.10  ? 30  ALA B N   1 
ATOM   2546 C  CA  . ALA B 1 54  ? 36.479  -26.438 16.569  1.00 45.00  ? 30  ALA B CA  1 
ATOM   2547 C  C   . ALA B 1 54  ? 35.392  -27.359 17.109  1.00 42.47  ? 30  ALA B C   1 
ATOM   2548 O  O   . ALA B 1 54  ? 34.322  -27.494 16.506  1.00 42.60  ? 30  ALA B O   1 
ATOM   2549 C  CB  . ALA B 1 54  ? 37.598  -27.247 15.912  1.00 45.54  ? 30  ALA B CB  1 
ATOM   2550 N  N   . SER B 1 55  ? 35.644  -27.993 18.257  1.00 42.48  ? 31  SER B N   1 
ATOM   2551 C  CA  . SER B 1 55  ? 34.663  -28.920 18.814  1.00 44.34  ? 31  SER B CA  1 
ATOM   2552 C  C   . SER B 1 55  ? 33.403  -28.201 19.280  1.00 42.70  ? 31  SER B C   1 
ATOM   2553 O  O   . SER B 1 55  ? 32.308  -28.773 19.221  1.00 42.24  ? 31  SER B O   1 
ATOM   2554 C  CB  . SER B 1 55  ? 35.283  -29.710 19.968  1.00 48.21  ? 31  SER B CB  1 
ATOM   2555 O  OG  . SER B 1 55  ? 35.751  -28.845 20.987  1.00 54.30  ? 31  SER B OG  1 
ATOM   2556 N  N   . GLU B 1 56  ? 33.529  -26.959 19.752  1.00 42.96  ? 32  GLU B N   1 
ATOM   2557 C  CA  . GLU B 1 56  ? 32.339  -26.194 20.111  1.00 42.89  ? 32  GLU B CA  1 
ATOM   2558 C  C   . GLU B 1 56  ? 31.515  -25.857 18.876  1.00 41.32  ? 32  GLU B C   1 
ATOM   2559 O  O   . GLU B 1 56  ? 30.281  -25.865 18.923  1.00 37.10  ? 32  GLU B O   1 
ATOM   2560 C  CB  . GLU B 1 56  ? 32.733  -24.917 20.853  1.00 41.39  ? 32  GLU B CB  1 
ATOM   2561 C  CG  . GLU B 1 56  ? 33.189  -25.149 22.285  1.00 44.34  ? 32  GLU B CG  1 
ATOM   2562 C  CD  . GLU B 1 56  ? 33.740  -23.894 22.936  1.00 48.32  ? 32  GLU B CD  1 
ATOM   2563 O  OE1 . GLU B 1 56  ? 33.923  -22.881 22.227  1.00 46.47  ? 32  GLU B OE1 1 
ATOM   2564 O  OE2 . GLU B 1 56  ? 33.991  -23.922 24.160  1.00 53.56  ? 32  GLU B OE2 1 
ATOM   2565 N  N   . ILE B 1 57  ? 32.182  -25.567 17.758  1.00 40.44  ? 33  ILE B N   1 
ATOM   2566 C  CA  . ILE B 1 57  ? 31.462  -25.241 16.534  1.00 37.28  ? 33  ILE B CA  1 
ATOM   2567 C  C   . ILE B 1 57  ? 30.756  -26.474 15.985  1.00 39.95  ? 33  ILE B C   1 
ATOM   2568 O  O   . ILE B 1 57  ? 29.611  -26.396 15.524  1.00 36.52  ? 33  ILE B O   1 
ATOM   2569 C  CB  . ILE B 1 57  ? 32.427  -24.620 15.506  1.00 37.83  ? 33  ILE B CB  1 
ATOM   2570 C  CG1 . ILE B 1 57  ? 32.820  -23.207 15.954  1.00 35.25  ? 33  ILE B CG1 1 
ATOM   2571 C  CG2 . ILE B 1 57  ? 31.796  -24.591 14.118  1.00 35.72  ? 33  ILE B CG2 1 
ATOM   2572 C  CD1 . ILE B 1 57  ? 33.954  -22.591 15.162  1.00 36.90  ? 33  ILE B CD1 1 
ATOM   2573 N  N   . THR B 1 58  ? 31.416  -27.634 16.037  1.00 38.05  ? 34  THR B N   1 
ATOM   2574 C  CA  . THR B 1 58  ? 30.791  -28.852 15.528  1.00 40.23  ? 34  THR B CA  1 
ATOM   2575 C  C   . THR B 1 58  ? 29.650  -29.303 16.430  1.00 35.98  ? 34  THR B C   1 
ATOM   2576 O  O   . THR B 1 58  ? 28.603  -29.739 15.942  1.00 37.79  ? 34  THR B O   1 
ATOM   2577 C  CB  . THR B 1 58  ? 31.831  -29.965 15.384  1.00 39.96  ? 34  THR B CB  1 
ATOM   2578 O  OG1 . THR B 1 58  ? 32.384  -30.280 16.667  1.00 41.12  ? 34  THR B OG1 1 
ATOM   2579 C  CG2 . THR B 1 58  ? 32.947  -29.539 14.437  1.00 40.03  ? 34  THR B CG2 1 
ATOM   2580 N  N   . ASP B 1 59  ? 29.835  -29.211 17.749  1.00 38.50  ? 35  ASP B N   1 
ATOM   2581 C  CA  . ASP B 1 59  ? 28.739  -29.503 18.670  1.00 39.88  ? 35  ASP B CA  1 
ATOM   2582 C  C   . ASP B 1 59  ? 27.555  -28.580 18.414  1.00 39.31  ? 35  ASP B C   1 
ATOM   2583 O  O   . ASP B 1 59  ? 26.401  -29.023 18.377  1.00 40.58  ? 35  ASP B O   1 
ATOM   2584 C  CB  . ASP B 1 59  ? 29.218  -29.369 20.116  1.00 41.97  ? 35  ASP B CB  1 
ATOM   2585 C  CG  . ASP B 1 59  ? 30.095  -30.525 20.551  1.00 46.23  ? 35  ASP B CG  1 
ATOM   2586 O  OD1 . ASP B 1 59  ? 30.255  -31.482 19.765  1.00 47.71  ? 35  ASP B OD1 1 
ATOM   2587 O  OD2 . ASP B 1 59  ? 30.624  -30.477 21.682  1.00 53.24  ? 35  ASP B OD2 1 
ATOM   2588 N  N   . ALA B 1 60  ? 27.825  -27.284 18.242  1.00 37.39  ? 36  ALA B N   1 
ATOM   2589 C  CA  . ALA B 1 60  ? 26.753  -26.339 17.953  1.00 39.43  ? 36  ALA B CA  1 
ATOM   2590 C  C   . ALA B 1 60  ? 26.050  -26.688 16.650  1.00 37.50  ? 36  ALA B C   1 
ATOM   2591 O  O   . ALA B 1 60  ? 24.816  -26.654 16.572  1.00 35.50  ? 36  ALA B O   1 
ATOM   2592 C  CB  . ALA B 1 60  ? 27.311  -24.918 17.891  1.00 35.77  ? 36  ALA B CB  1 
ATOM   2593 N  N   . ALA B 1 61  ? 26.821  -27.030 15.615  1.00 35.72  ? 37  ALA B N   1 
ATOM   2594 C  CA  . ALA B 1 61  ? 26.231  -27.334 14.316  1.00 37.57  ? 37  ALA B CA  1 
ATOM   2595 C  C   . ALA B 1 61  ? 25.381  -28.595 14.373  1.00 37.76  ? 37  ALA B C   1 
ATOM   2596 O  O   . ALA B 1 61  ? 24.284  -28.638 13.803  1.00 35.33  ? 37  ALA B O   1 
ATOM   2597 C  CB  . ALA B 1 61  ? 27.330  -27.483 13.267  1.00 33.84  ? 37  ALA B CB  1 
ATOM   2598 N  N   . ILE B 1 62  ? 25.873  -29.633 15.053  1.00 34.85  ? 38  ILE B N   1 
ATOM   2599 C  CA  . ILE B 1 62  ? 25.148  -30.898 15.105  1.00 37.88  ? 38  ILE B CA  1 
ATOM   2600 C  C   . ILE B 1 62  ? 23.862  -30.746 15.909  1.00 40.50  ? 38  ILE B C   1 
ATOM   2601 O  O   . ILE B 1 62  ? 22.815  -31.288 15.536  1.00 40.04  ? 38  ILE B O   1 
ATOM   2602 C  CB  . ILE B 1 62  ? 26.059  -31.999 15.679  1.00 37.67  ? 38  ILE B CB  1 
ATOM   2603 C  CG1 . ILE B 1 62  ? 27.201  -32.292 14.700  1.00 38.61  ? 38  ILE B CG1 1 
ATOM   2604 C  CG2 . ILE B 1 62  ? 25.258  -33.262 15.969  1.00 39.59  ? 38  ILE B CG2 1 
ATOM   2605 C  CD1 . ILE B 1 62  ? 28.370  -33.043 15.313  1.00 39.89  ? 38  ILE B CD1 1 
ATOM   2606 N  N   . GLY B 1 63  ? 23.915  -30.006 17.017  1.00 40.90  ? 39  GLY B N   1 
ATOM   2607 C  CA  . GLY B 1 63  ? 22.704  -29.770 17.788  1.00 39.16  ? 39  GLY B CA  1 
ATOM   2608 C  C   . GLY B 1 63  ? 21.677  -28.963 17.017  1.00 38.41  ? 39  GLY B C   1 
ATOM   2609 O  O   . GLY B 1 63  ? 20.474  -29.222 17.107  1.00 36.98  ? 39  GLY B O   1 
ATOM   2610 N  N   . ALA B 1 64  ? 22.137  -27.977 16.244  1.00 35.76  ? 40  ALA B N   1 
ATOM   2611 C  CA  . ALA B 1 64  ? 21.217  -27.181 15.439  1.00 37.44  ? 40  ALA B CA  1 
ATOM   2612 C  C   . ALA B 1 64  ? 20.564  -28.026 14.352  1.00 37.57  ? 40  ALA B C   1 
ATOM   2613 O  O   . ALA B 1 64  ? 19.360  -27.898 14.099  1.00 35.70  ? 40  ALA B O   1 
ATOM   2614 C  CB  . ALA B 1 64  ? 21.955  -25.995 14.820  1.00 33.22  ? 40  ALA B CB  1 
ATOM   2615 N  N   . ALA B 1 65  ? 21.344  -28.889 13.696  1.00 37.05  ? 41  ALA B N   1 
ATOM   2616 C  CA  . ALA B 1 65  ? 20.782  -29.772 12.680  1.00 37.37  ? 41  ALA B CA  1 
ATOM   2617 C  C   . ALA B 1 65  ? 19.740  -30.705 13.280  1.00 37.65  ? 41  ALA B C   1 
ATOM   2618 O  O   . ALA B 1 65  ? 18.665  -30.904 12.702  1.00 36.75  ? 41  ALA B O   1 
ATOM   2619 C  CB  . ALA B 1 65  ? 21.896  -30.579 12.015  1.00 37.11  ? 41  ALA B CB  1 
ATOM   2620 N  N   . GLU B 1 66  ? 20.042  -31.291 14.439  1.00 39.44  ? 42  GLU B N   1 
ATOM   2621 C  CA  . GLU B 1 66  ? 19.113  -32.231 15.054  1.00 41.18  ? 42  GLU B CA  1 
ATOM   2622 C  C   . GLU B 1 66  ? 17.832  -31.541 15.500  1.00 41.22  ? 42  GLU B C   1 
ATOM   2623 O  O   . GLU B 1 66  ? 16.773  -32.178 15.551  1.00 43.53  ? 42  GLU B O   1 
ATOM   2624 C  CB  . GLU B 1 66  ? 19.792  -32.932 16.230  1.00 42.87  ? 42  GLU B CB  1 
ATOM   2625 C  CG  . GLU B 1 66  ? 20.862  -33.923 15.789  1.00 49.52  ? 42  GLU B CG  1 
ATOM   2626 C  CD  . GLU B 1 66  ? 21.759  -34.378 16.924  1.00 61.02  ? 42  GLU B CD  1 
ATOM   2627 O  OE1 . GLU B 1 66  ? 21.770  -33.715 17.984  1.00 61.03  ? 42  GLU B OE1 1 
ATOM   2628 O  OE2 . GLU B 1 66  ? 22.457  -35.400 16.751  1.00 65.35  ? 42  GLU B OE2 1 
ATOM   2629 N  N   . ALA B 1 67  ? 17.900  -30.248 15.815  1.00 38.96  ? 43  ALA B N   1 
ATOM   2630 C  CA  . ALA B 1 67  ? 16.706  -29.496 16.172  1.00 39.29  ? 43  ALA B CA  1 
ATOM   2631 C  C   . ALA B 1 67  ? 15.874  -29.104 14.958  1.00 39.70  ? 43  ALA B C   1 
ATOM   2632 O  O   . ALA B 1 67  ? 14.725  -28.686 15.131  1.00 36.96  ? 43  ALA B O   1 
ATOM   2633 C  CB  . ALA B 1 67  ? 17.088  -28.242 16.963  1.00 36.49  ? 43  ALA B CB  1 
ATOM   2634 N  N   . GLY B 1 68  ? 16.421  -29.220 13.747  1.00 38.64  ? 44  GLY B N   1 
ATOM   2635 C  CA  . GLY B 1 68  ? 15.640  -28.995 12.546  1.00 35.67  ? 44  GLY B CA  1 
ATOM   2636 C  C   . GLY B 1 68  ? 16.266  -28.081 11.510  1.00 36.66  ? 44  GLY B C   1 
ATOM   2637 O  O   . GLY B 1 68  ? 15.626  -27.767 10.503  1.00 33.65  ? 44  GLY B O   1 
ATOM   2638 N  N   . ALA B 1 69  ? 17.506  -27.646 11.729  1.00 32.41  ? 45  ALA B N   1 
ATOM   2639 C  CA  . ALA B 1 69  ? 18.187  -26.784 10.768  1.00 33.08  ? 45  ALA B CA  1 
ATOM   2640 C  C   . ALA B 1 69  ? 18.719  -27.624 9.612   1.00 35.57  ? 45  ALA B C   1 
ATOM   2641 O  O   . ALA B 1 69  ? 19.573  -28.495 9.810   1.00 33.03  ? 45  ALA B O   1 
ATOM   2642 C  CB  . ALA B 1 69  ? 19.323  -26.019 11.443  1.00 32.13  ? 45  ALA B CB  1 
ATOM   2643 N  N   . ALA B 1 70  ? 18.219  -27.356 8.402   1.00 32.48  ? 46  ALA B N   1 
ATOM   2644 C  CA  . ALA B 1 70  ? 18.637  -28.123 7.234   1.00 34.66  ? 46  ALA B CA  1 
ATOM   2645 C  C   . ALA B 1 70  ? 19.968  -27.637 6.674   1.00 34.58  ? 46  ALA B C   1 
ATOM   2646 O  O   . ALA B 1 70  ? 20.695  -28.418 6.049   1.00 34.44  ? 46  ALA B O   1 
ATOM   2647 C  CB  . ALA B 1 70  ? 17.563  -28.050 6.147   1.00 35.64  ? 46  ALA B CB  1 
ATOM   2648 N  N   . VAL B 1 71  ? 20.296  -26.365 6.878   1.00 31.04  ? 47  VAL B N   1 
ATOM   2649 C  CA  . VAL B 1 71  ? 21.533  -25.768 6.390   1.00 33.25  ? 47  VAL B CA  1 
ATOM   2650 C  C   . VAL B 1 71  ? 22.294  -25.218 7.585   1.00 32.42  ? 47  VAL B C   1 
ATOM   2651 O  O   . VAL B 1 71  ? 21.710  -24.535 8.435   1.00 33.66  ? 47  VAL B O   1 
ATOM   2652 C  CB  . VAL B 1 71  ? 21.264  -24.649 5.365   1.00 32.98  ? 47  VAL B CB  1 
ATOM   2653 C  CG1 . VAL B 1 71  ? 22.579  -24.047 4.888   1.00 29.63  ? 47  VAL B CG1 1 
ATOM   2654 C  CG2 . VAL B 1 71  ? 20.443  -25.171 4.193   1.00 31.44  ? 47  VAL B CG2 1 
ATOM   2655 N  N   . ILE B 1 72  ? 23.590  -25.511 7.648   1.00 31.85  ? 48  ILE B N   1 
ATOM   2656 C  CA  . ILE B 1 72  ? 24.470  -24.975 8.679   1.00 32.08  ? 48  ILE B CA  1 
ATOM   2657 C  C   . ILE B 1 72  ? 25.464  -24.042 8.006   1.00 32.42  ? 48  ILE B C   1 
ATOM   2658 O  O   . ILE B 1 72  ? 26.205  -24.452 7.104   1.00 33.86  ? 48  ILE B O   1 
ATOM   2659 C  CB  . ILE B 1 72  ? 25.198  -26.083 9.454   1.00 33.50  ? 48  ILE B CB  1 
ATOM   2660 C  CG1 . ILE B 1 72  ? 24.200  -27.089 10.034  1.00 34.92  ? 48  ILE B CG1 1 
ATOM   2661 C  CG2 . ILE B 1 72  ? 26.042  -25.461 10.561  1.00 33.08  ? 48  ILE B CG2 1 
ATOM   2662 C  CD1 . ILE B 1 72  ? 23.220  -26.493 11.030  1.00 31.94  ? 48  ILE B CD1 1 
ATOM   2663 N  N   . HIS B 1 73  ? 25.481  -22.792 8.449   1.00 30.45  ? 49  HIS B N   1 
ATOM   2664 C  CA  . HIS B 1 73  ? 26.365  -21.770 7.912   1.00 32.59  ? 49  HIS B CA  1 
ATOM   2665 C  C   . HIS B 1 73  ? 27.559  -21.606 8.847   1.00 31.73  ? 49  HIS B C   1 
ATOM   2666 O  O   . HIS B 1 73  ? 27.380  -21.409 10.053  1.00 31.42  ? 49  HIS B O   1 
ATOM   2667 C  CB  . HIS B 1 73  ? 25.589  -20.466 7.750   1.00 32.20  ? 49  HIS B CB  1 
ATOM   2668 C  CG  . HIS B 1 73  ? 26.436  -19.309 7.349   1.00 35.98  ? 49  HIS B CG  1 
ATOM   2669 N  ND1 . HIS B 1 73  ? 26.828  -19.088 6.047   1.00 40.56  ? 49  HIS B ND1 1 
ATOM   2670 C  CD2 . HIS B 1 73  ? 26.972  -18.308 8.082   1.00 34.08  ? 49  HIS B CD2 1 
ATOM   2671 C  CE1 . HIS B 1 73  ? 27.568  -17.996 5.996   1.00 39.82  ? 49  HIS B CE1 1 
ATOM   2672 N  NE2 . HIS B 1 73  ? 27.670  -17.507 7.217   1.00 36.14  ? 49  HIS B NE2 1 
ATOM   2673 N  N   . LEU B 1 74  ? 28.772  -21.691 8.292   1.00 33.61  ? 50  LEU B N   1 
ATOM   2674 C  CA  . LEU B 1 74  ? 29.968  -21.976 9.078   1.00 33.22  ? 50  LEU B CA  1 
ATOM   2675 C  C   . LEU B 1 74  ? 31.057  -20.927 8.900   1.00 35.93  ? 50  LEU B C   1 
ATOM   2676 O  O   . LEU B 1 74  ? 31.411  -20.571 7.770   1.00 36.61  ? 50  LEU B O   1 
ATOM   2677 C  CB  . LEU B 1 74  ? 30.537  -23.350 8.700   1.00 34.26  ? 50  LEU B CB  1 
ATOM   2678 C  CG  . LEU B 1 74  ? 29.740  -24.561 9.178   1.00 35.12  ? 50  LEU B CG  1 
ATOM   2679 C  CD1 . LEU B 1 74  ? 30.230  -25.829 8.490   1.00 34.78  ? 50  LEU B CD1 1 
ATOM   2680 C  CD2 . LEU B 1 74  ? 29.848  -24.691 10.687  1.00 32.95  ? 50  LEU B CD2 1 
ATOM   2681 N  N   . HIS B 1 75  ? 31.594  -20.455 10.026  1.00 36.86  ? 51  HIS B N   1 
ATOM   2682 C  CA  . HIS B 1 75  ? 32.891  -19.800 10.116  1.00 35.90  ? 51  HIS B CA  1 
ATOM   2683 C  C   . HIS B 1 75  ? 33.776  -20.602 11.061  1.00 36.87  ? 51  HIS B C   1 
ATOM   2684 O  O   . HIS B 1 75  ? 33.306  -21.476 11.793  1.00 37.96  ? 51  HIS B O   1 
ATOM   2685 C  CB  . HIS B 1 75  ? 32.787  -18.363 10.643  1.00 36.48  ? 51  HIS B CB  1 
ATOM   2686 C  CG  . HIS B 1 75  ? 32.011  -17.443 9.760   1.00 37.10  ? 51  HIS B CG  1 
ATOM   2687 N  ND1 . HIS B 1 75  ? 32.485  -16.207 9.379   1.00 37.20  ? 51  HIS B ND1 1 
ATOM   2688 C  CD2 . HIS B 1 75  ? 30.790  -17.571 9.193   1.00 35.59  ? 51  HIS B CD2 1 
ATOM   2689 C  CE1 . HIS B 1 75  ? 31.590  -15.614 8.611   1.00 38.91  ? 51  HIS B CE1 1 
ATOM   2690 N  NE2 . HIS B 1 75  ? 30.554  -16.423 8.480   1.00 33.71  ? 51  HIS B NE2 1 
ATOM   2691 N  N   . ALA B 1 76  ? 35.068  -20.280 11.055  1.00 36.97  ? 52  ALA B N   1 
ATOM   2692 C  CA  . ALA B 1 76  ? 36.020  -20.824 12.011  1.00 39.17  ? 52  ALA B CA  1 
ATOM   2693 C  C   . ALA B 1 76  ? 36.678  -19.682 12.775  1.00 40.29  ? 52  ALA B C   1 
ATOM   2694 O  O   . ALA B 1 76  ? 36.621  -18.519 12.364  1.00 40.25  ? 52  ALA B O   1 
ATOM   2695 C  CB  . ALA B 1 76  ? 37.088  -21.682 11.316  1.00 37.98  ? 52  ALA B CB  1 
ATOM   2696 N  N   . ARG B 1 77  ? 37.308  -20.022 13.899  1.00 36.75  ? 53  ARG B N   1 
ATOM   2697 C  CA  . ARG B 1 77  ? 37.953  -19.034 14.752  1.00 39.27  ? 53  ARG B CA  1 
ATOM   2698 C  C   . ARG B 1 77  ? 39.264  -19.591 15.294  1.00 45.03  ? 53  ARG B C   1 
ATOM   2699 O  O   . ARG B 1 77  ? 39.443  -20.807 15.405  1.00 43.32  ? 53  ARG B O   1 
ATOM   2700 C  CB  . ARG B 1 77  ? 37.044  -18.624 15.923  1.00 40.66  ? 53  ARG B CB  1 
ATOM   2701 C  CG  . ARG B 1 77  ? 35.757  -17.902 15.520  1.00 37.63  ? 53  ARG B CG  1 
ATOM   2702 C  CD  . ARG B 1 77  ? 34.905  -17.584 16.744  1.00 37.32  ? 53  ARG B CD  1 
ATOM   2703 N  NE  . ARG B 1 77  ? 33.720  -16.796 16.420  1.00 35.62  ? 53  ARG B NE  1 
ATOM   2704 C  CZ  . ARG B 1 77  ? 33.687  -15.471 16.356  1.00 38.77  ? 53  ARG B CZ  1 
ATOM   2705 N  NH1 . ARG B 1 77  ? 34.771  -14.739 16.566  1.00 39.05  ? 53  ARG B NH1 1 
ATOM   2706 N  NH2 . ARG B 1 77  ? 32.539  -14.864 16.070  1.00 36.05  ? 53  ARG B NH2 1 
ATOM   2707 N  N   . HIS B 1 78  ? 40.186  -18.686 15.621  1.00 43.92  ? 54  HIS B N   1 
ATOM   2708 C  CA  . HIS B 1 78  ? 41.391  -19.072 16.345  1.00 46.79  ? 54  HIS B CA  1 
ATOM   2709 C  C   . HIS B 1 78  ? 41.030  -19.428 17.782  1.00 50.82  ? 54  HIS B C   1 
ATOM   2710 O  O   . HIS B 1 78  ? 40.407  -18.632 18.491  1.00 50.08  ? 54  HIS B O   1 
ATOM   2711 C  CB  . HIS B 1 78  ? 42.420  -17.941 16.337  1.00 44.65  ? 54  HIS B CB  1 
ATOM   2712 C  CG  . HIS B 1 78  ? 42.995  -17.644 14.988  1.00 44.11  ? 54  HIS B CG  1 
ATOM   2713 N  ND1 . HIS B 1 78  ? 42.728  -16.476 14.308  1.00 43.51  ? 54  HIS B ND1 1 
ATOM   2714 C  CD2 . HIS B 1 78  ? 43.836  -18.355 14.200  1.00 45.26  ? 54  HIS B CD2 1 
ATOM   2715 C  CE1 . HIS B 1 78  ? 43.375  -16.482 13.156  1.00 41.52  ? 54  HIS B CE1 1 
ATOM   2716 N  NE2 . HIS B 1 78  ? 44.056  -17.611 13.067  1.00 44.13  ? 54  HIS B NE2 1 
ATOM   2717 N  N   . GLU B 1 79  ? 41.426  -20.624 18.217  1.00 57.41  ? 55  GLU B N   1 
ATOM   2718 C  CA  . GLU B 1 79  ? 41.089  -21.054 19.568  1.00 59.40  ? 55  GLU B CA  1 
ATOM   2719 C  C   . GLU B 1 79  ? 41.862  -20.279 20.628  1.00 56.23  ? 55  GLU B C   1 
ATOM   2720 O  O   . GLU B 1 79  ? 41.459  -20.283 21.796  1.00 58.34  ? 55  GLU B O   1 
ATOM   2721 C  CB  . GLU B 1 79  ? 41.341  -22.556 19.718  1.00 61.87  ? 55  GLU B CB  1 
ATOM   2722 C  CG  . GLU B 1 79  ? 40.661  -23.391 18.638  1.00 64.50  ? 55  GLU B CG  1 
ATOM   2723 C  CD  . GLU B 1 79  ? 40.498  -24.850 19.025  1.00 69.57  ? 55  GLU B CD  1 
ATOM   2724 O  OE1 . GLU B 1 79  ? 40.956  -25.237 20.123  1.00 67.79  ? 55  GLU B OE1 1 
ATOM   2725 O  OE2 . GLU B 1 79  ? 39.904  -25.607 18.226  1.00 67.43  ? 55  GLU B OE2 1 
ATOM   2726 N  N   . GLY B 1 80  ? 42.945  -19.606 20.248  1.00 57.73  ? 56  GLY B N   1 
ATOM   2727 C  CA  . GLY B 1 80  ? 43.733  -18.834 21.189  1.00 57.83  ? 56  GLY B CA  1 
ATOM   2728 C  C   . GLY B 1 80  ? 42.995  -17.645 21.769  1.00 57.08  ? 56  GLY B C   1 
ATOM   2729 O  O   . GLY B 1 80  ? 42.862  -17.532 22.991  1.00 60.82  ? 56  GLY B O   1 
ATOM   2730 N  N   . ASP B 1 81  ? 42.513  -16.747 20.907  1.00 49.28  ? 57  ASP B N   1 
ATOM   2731 C  CA  . ASP B 1 81  ? 41.834  -15.537 21.346  1.00 49.18  ? 57  ASP B CA  1 
ATOM   2732 C  C   . ASP B 1 81  ? 40.437  -15.378 20.759  1.00 45.80  ? 57  ASP B C   1 
ATOM   2733 O  O   . ASP B 1 81  ? 39.798  -14.348 21.000  1.00 45.60  ? 57  ASP B O   1 
ATOM   2734 C  CB  . ASP B 1 81  ? 42.676  -14.299 20.998  1.00 48.28  ? 57  ASP B CB  1 
ATOM   2735 C  CG  . ASP B 1 81  ? 42.935  -14.164 19.510  1.00 48.25  ? 57  ASP B CG  1 
ATOM   2736 O  OD1 . ASP B 1 81  ? 42.338  -14.929 18.722  1.00 44.91  ? 57  ASP B OD1 1 
ATOM   2737 O  OD2 . ASP B 1 81  ? 43.746  -13.291 19.129  1.00 49.41  ? 57  ASP B OD2 1 
ATOM   2738 N  N   . GLY B 1 82  ? 39.948  -16.354 19.997  1.00 43.67  ? 58  GLY B N   1 
ATOM   2739 C  CA  . GLY B 1 82  ? 38.597  -16.312 19.479  1.00 47.29  ? 58  GLY B CA  1 
ATOM   2740 C  C   . GLY B 1 82  ? 38.399  -15.456 18.250  1.00 45.25  ? 58  GLY B C   1 
ATOM   2741 O  O   . GLY B 1 82  ? 37.254  -15.281 17.818  1.00 41.41  ? 58  GLY B O   1 
ATOM   2742 N  N   . SER B 1 83  ? 39.471  -14.922 17.669  1.00 42.70  ? 59  SER B N   1 
ATOM   2743 C  CA  . SER B 1 83  ? 39.350  -14.047 16.515  1.00 43.58  ? 59  SER B CA  1 
ATOM   2744 C  C   . SER B 1 83  ? 39.031  -14.852 15.257  1.00 43.30  ? 59  SER B C   1 
ATOM   2745 O  O   . SER B 1 83  ? 39.315  -16.050 15.185  1.00 42.48  ? 59  SER B O   1 
ATOM   2746 C  CB  . SER B 1 83  ? 40.641  -13.258 16.321  1.00 42.02  ? 59  SER B CB  1 
ATOM   2747 O  OG  . SER B 1 83  ? 41.729  -14.123 16.058  1.00 44.38  ? 59  SER B OG  1 
ATOM   2748 N  N   . PRO B 1 84  ? 38.433  -14.213 14.248  1.00 42.21  ? 60  PRO B N   1 
ATOM   2749 C  CA  . PRO B 1 84  ? 38.091  -14.940 13.017  1.00 40.70  ? 60  PRO B CA  1 
ATOM   2750 C  C   . PRO B 1 84  ? 39.304  -15.605 12.380  1.00 43.85  ? 60  PRO B C   1 
ATOM   2751 O  O   . PRO B 1 84  ? 40.408  -15.054 12.368  1.00 40.63  ? 60  PRO B O   1 
ATOM   2752 C  CB  . PRO B 1 84  ? 37.509  -13.846 12.113  1.00 42.91  ? 60  PRO B CB  1 
ATOM   2753 C  CG  . PRO B 1 84  ? 36.971  -12.829 13.059  1.00 43.51  ? 60  PRO B CG  1 
ATOM   2754 C  CD  . PRO B 1 84  ? 37.891  -12.842 14.248  1.00 41.43  ? 60  PRO B CD  1 
ATOM   2755 N  N   . ASP B 1 85  ? 39.083  -16.805 11.841  1.00 42.92  ? 61  ASP B N   1 
ATOM   2756 C  CA  . ASP B 1 85  ? 40.116  -17.579 11.156  1.00 39.61  ? 61  ASP B CA  1 
ATOM   2757 C  C   . ASP B 1 85  ? 39.522  -18.106 9.855   1.00 42.59  ? 61  ASP B C   1 
ATOM   2758 O  O   . ASP B 1 85  ? 38.716  -19.043 9.869   1.00 41.07  ? 61  ASP B O   1 
ATOM   2759 C  CB  . ASP B 1 85  ? 40.621  -18.726 12.033  1.00 39.58  ? 61  ASP B CB  1 
ATOM   2760 C  CG  . ASP B 1 85  ? 41.820  -19.443 11.432  1.00 45.93  ? 61  ASP B CG  1 
ATOM   2761 O  OD1 . ASP B 1 85  ? 42.219  -19.108 10.295  1.00 44.05  ? 61  ASP B OD1 1 
ATOM   2762 O  OD2 . ASP B 1 85  ? 42.366  -20.344 12.105  1.00 44.25  ? 61  ASP B OD2 1 
ATOM   2763 N  N   . GLN B 1 86  ? 39.923  -17.508 8.736   1.00 40.75  ? 62  GLN B N   1 
ATOM   2764 C  CA  . GLN B 1 86  ? 39.394  -17.825 7.413   1.00 40.93  ? 62  GLN B CA  1 
ATOM   2765 C  C   . GLN B 1 86  ? 40.415  -18.600 6.581   1.00 43.53  ? 62  GLN B C   1 
ATOM   2766 O  O   . GLN B 1 86  ? 40.528  -18.412 5.370   1.00 49.35  ? 62  GLN B O   1 
ATOM   2767 C  CB  . GLN B 1 86  ? 38.963  -16.538 6.708   1.00 43.94  ? 62  GLN B CB  1 
ATOM   2768 C  CG  . GLN B 1 86  ? 38.296  -16.686 5.335   1.00 48.01  ? 62  GLN B CG  1 
ATOM   2769 C  CD  . GLN B 1 86  ? 37.033  -17.527 5.355   1.00 45.66  ? 62  GLN B CD  1 
ATOM   2770 O  OE1 . GLN B 1 86  ? 36.637  -18.061 6.391   1.00 43.04  ? 62  GLN B OE1 1 
ATOM   2771 N  NE2 . GLN B 1 86  ? 36.390  -17.645 4.198   1.00 41.06  ? 62  GLN B NE2 1 
ATOM   2772 N  N   . SER B 1 87  ? 41.174  -19.483 7.218   1.00 43.22  ? 63  SER B N   1 
ATOM   2773 C  CA  . SER B 1 87  ? 42.146  -20.298 6.505   1.00 48.41  ? 63  SER B CA  1 
ATOM   2774 C  C   . SER B 1 87  ? 41.545  -21.656 6.152   1.00 48.67  ? 63  SER B C   1 
ATOM   2775 O  O   . SER B 1 87  ? 40.522  -22.075 6.698   1.00 45.08  ? 63  SER B O   1 
ATOM   2776 C  CB  . SER B 1 87  ? 43.416  -20.489 7.334   1.00 44.41  ? 63  SER B CB  1 
ATOM   2777 O  OG  . SER B 1 87  ? 43.200  -21.391 8.405   1.00 50.40  ? 63  SER B OG  1 
ATOM   2778 N  N   . VAL B 1 88  ? 42.204  -22.341 5.215   1.00 48.36  ? 64  VAL B N   1 
ATOM   2779 C  CA  . VAL B 1 88  ? 41.735  -23.654 4.782   1.00 49.53  ? 64  VAL B CA  1 
ATOM   2780 C  C   . VAL B 1 88  ? 41.822  -24.655 5.927   1.00 50.33  ? 64  VAL B C   1 
ATOM   2781 O  O   . VAL B 1 88  ? 40.892  -25.437 6.160   1.00 49.14  ? 64  VAL B O   1 
ATOM   2782 C  CB  . VAL B 1 88  ? 42.541  -24.129 3.557   1.00 53.34  ? 64  VAL B CB  1 
ATOM   2783 C  CG1 . VAL B 1 88  ? 42.122  -25.537 3.152   1.00 50.98  ? 64  VAL B CG1 1 
ATOM   2784 C  CG2 . VAL B 1 88  ? 42.364  -23.159 2.396   1.00 50.82  ? 64  VAL B CG2 1 
ATOM   2785 N  N   . GLU B 1 89  ? 42.939  -24.651 6.659   1.00 57.08  ? 65  GLU B N   1 
ATOM   2786 C  CA  . GLU B 1 89  ? 43.114  -25.621 7.734   1.00 56.86  ? 65  GLU B CA  1 
ATOM   2787 C  C   . GLU B 1 89  ? 42.108  -25.412 8.858   1.00 53.76  ? 65  GLU B C   1 
ATOM   2788 O  O   . GLU B 1 89  ? 41.792  -26.360 9.587   1.00 53.30  ? 65  GLU B O   1 
ATOM   2789 C  CB  . GLU B 1 89  ? 44.538  -25.548 8.285   1.00 60.47  ? 65  GLU B CB  1 
ATOM   2790 C  CG  . GLU B 1 89  ? 44.744  -26.374 9.553   1.00 65.63  ? 65  GLU B CG  1 
ATOM   2791 C  CD  . GLU B 1 89  ? 46.150  -26.926 9.686   1.00 72.45  ? 65  GLU B CD  1 
ATOM   2792 O  OE1 . GLU B 1 89  ? 46.965  -26.728 8.759   1.00 73.71  ? 65  GLU B OE1 1 
ATOM   2793 O  OE2 . GLU B 1 89  ? 46.438  -27.565 10.721  1.00 75.60  ? 65  GLU B OE2 1 
ATOM   2794 N  N   . ALA B 1 90  ? 41.594  -24.190 9.015   1.00 50.52  ? 66  ALA B N   1 
ATOM   2795 C  CA  . ALA B 1 90  ? 40.695  -23.906 10.129  1.00 49.01  ? 66  ALA B CA  1 
ATOM   2796 C  C   . ALA B 1 90  ? 39.416  -24.729 10.052  1.00 42.90  ? 66  ALA B C   1 
ATOM   2797 O  O   . ALA B 1 90  ? 38.830  -25.059 11.089  1.00 41.72  ? 66  ALA B O   1 
ATOM   2798 C  CB  . ALA B 1 90  ? 40.362  -22.415 10.164  1.00 44.93  ? 66  ALA B CB  1 
ATOM   2799 N  N   . PHE B 1 91  ? 38.965  -25.064 8.844   1.00 42.79  ? 67  PHE B N   1 
ATOM   2800 C  CA  . PHE B 1 91  ? 37.751  -25.849 8.662   1.00 41.93  ? 67  PHE B CA  1 
ATOM   2801 C  C   . PHE B 1 91  ? 37.998  -27.351 8.670   1.00 44.56  ? 67  PHE B C   1 
ATOM   2802 O  O   . PHE B 1 91  ? 37.030  -28.121 8.643   1.00 44.09  ? 67  PHE B O   1 
ATOM   2803 C  CB  . PHE B 1 91  ? 37.070  -25.466 7.344   1.00 42.43  ? 67  PHE B CB  1 
ATOM   2804 C  CG  . PHE B 1 91  ? 36.504  -24.077 7.335   1.00 41.83  ? 67  PHE B CG  1 
ATOM   2805 C  CD1 . PHE B 1 91  ? 37.307  -22.988 7.034   1.00 42.44  ? 67  PHE B CD1 1 
ATOM   2806 C  CD2 . PHE B 1 91  ? 35.169  -23.860 7.624   1.00 38.58  ? 67  PHE B CD2 1 
ATOM   2807 C  CE1 . PHE B 1 91  ? 36.786  -21.709 7.025   1.00 40.58  ? 67  PHE B CE1 1 
ATOM   2808 C  CE2 . PHE B 1 91  ? 34.642  -22.582 7.615   1.00 39.16  ? 67  PHE B CE2 1 
ATOM   2809 C  CZ  . PHE B 1 91  ? 35.450  -21.505 7.316   1.00 39.04  ? 67  PHE B CZ  1 
ATOM   2810 N  N   . ASN B 1 92  ? 39.257  -27.785 8.713   1.00 45.38  ? 68  ASN B N   1 
ATOM   2811 C  CA  . ASN B 1 92  ? 39.552  -29.213 8.600   1.00 46.63  ? 68  ASN B CA  1 
ATOM   2812 C  C   . ASN B 1 92  ? 38.964  -30.029 9.742   1.00 44.91  ? 68  ASN B C   1 
ATOM   2813 O  O   . ASN B 1 92  ? 38.351  -31.075 9.470   1.00 42.79  ? 68  ASN B O   1 
ATOM   2814 C  CB  . ASN B 1 92  ? 41.067  -29.417 8.501   1.00 44.18  ? 68  ASN B CB  1 
ATOM   2815 C  CG  . ASN B 1 92  ? 41.443  -30.876 8.356   1.00 52.07  ? 68  ASN B CG  1 
ATOM   2816 O  OD1 . ASN B 1 92  ? 42.038  -31.470 9.257   1.00 54.02  ? 68  ASN B OD1 1 
ATOM   2817 N  ND2 . ASN B 1 92  ? 41.083  -31.468 7.222   1.00 50.87  ? 68  ASN B ND2 1 
ATOM   2818 N  N   . PRO B 1 93  ? 39.113  -29.645 11.011  1.00 44.04  ? 69  PRO B N   1 
ATOM   2819 C  CA  . PRO B 1 93  ? 38.473  -30.397 12.096  1.00 44.56  ? 69  PRO B CA  1 
ATOM   2820 C  C   . PRO B 1 93  ? 36.993  -30.100 12.279  1.00 44.69  ? 69  PRO B C   1 
ATOM   2821 O  O   . PRO B 1 93  ? 36.424  -30.503 13.298  1.00 46.91  ? 69  PRO B O   1 
ATOM   2822 C  CB  . PRO B 1 93  ? 39.273  -29.947 13.328  1.00 42.21  ? 69  PRO B CB  1 
ATOM   2823 C  CG  . PRO B 1 93  ? 39.653  -28.554 13.015  1.00 46.00  ? 69  PRO B CG  1 
ATOM   2824 C  CD  . PRO B 1 93  ? 39.919  -28.523 11.529  1.00 43.82  ? 69  PRO B CD  1 
ATOM   2825 N  N   . ILE B 1 94  ? 36.363  -29.418 11.324  1.00 44.28  ? 70  ILE B N   1 
ATOM   2826 C  CA  . ILE B 1 94  ? 34.977  -28.972 11.444  1.00 41.12  ? 70  ILE B CA  1 
ATOM   2827 C  C   . ILE B 1 94  ? 34.075  -29.691 10.444  1.00 40.82  ? 70  ILE B C   1 
ATOM   2828 O  O   . ILE B 1 94  ? 33.086  -30.317 10.826  1.00 41.89  ? 70  ILE B O   1 
ATOM   2829 C  CB  . ILE B 1 94  ? 34.879  -27.438 11.280  1.00 40.86  ? 70  ILE B CB  1 
ATOM   2830 C  CG1 . ILE B 1 94  ? 35.527  -26.735 12.477  1.00 40.37  ? 70  ILE B CG1 1 
ATOM   2831 C  CG2 . ILE B 1 94  ? 33.426  -27.016 11.100  1.00 37.94  ? 70  ILE B CG2 1 
ATOM   2832 C  CD1 . ILE B 1 94  ? 35.614  -25.225 12.338  1.00 40.72  ? 70  ILE B CD1 1 
ATOM   2833 N  N   . LEU B 1 95  ? 34.403  -29.610 9.154   1.00 42.50  ? 71  LEU B N   1 
ATOM   2834 C  CA  . LEU B 1 95  ? 33.482  -30.075 8.120   1.00 41.06  ? 71  LEU B CA  1 
ATOM   2835 C  C   . LEU B 1 95  ? 33.279  -31.584 8.189   1.00 41.56  ? 71  LEU B C   1 
ATOM   2836 O  O   . LEU B 1 95  ? 32.141  -32.067 8.181   1.00 44.20  ? 71  LEU B O   1 
ATOM   2837 C  CB  . LEU B 1 95  ? 34.000  -29.663 6.743   1.00 41.75  ? 71  LEU B CB  1 
ATOM   2838 C  CG  . LEU B 1 95  ? 34.090  -28.156 6.506   1.00 42.80  ? 71  LEU B CG  1 
ATOM   2839 C  CD1 . LEU B 1 95  ? 34.858  -27.860 5.227   1.00 41.42  ? 71  LEU B CD1 1 
ATOM   2840 C  CD2 . LEU B 1 95  ? 32.698  -27.544 6.449   1.00 37.05  ? 71  LEU B CD2 1 
ATOM   2841 N  N   . GLY B 1 96  ? 34.371  -32.346 8.247   1.00 43.99  ? 72  GLY B N   1 
ATOM   2842 C  CA  . GLY B 1 96  ? 34.244  -33.794 8.249   1.00 43.25  ? 72  GLY B CA  1 
ATOM   2843 C  C   . GLY B 1 96  ? 33.528  -34.317 9.478   1.00 44.93  ? 72  GLY B C   1 
ATOM   2844 O  O   . GLY B 1 96  ? 32.760  -35.279 9.399   1.00 44.50  ? 72  GLY B O   1 
ATOM   2845 N  N   . VAL B 1 97  ? 33.769  -33.692 10.632  1.00 44.70  ? 73  VAL B N   1 
ATOM   2846 C  CA  . VAL B 1 97  ? 33.102  -34.115 11.861  1.00 45.97  ? 73  VAL B CA  1 
ATOM   2847 C  C   . VAL B 1 97  ? 31.592  -33.960 11.723  1.00 44.86  ? 73  VAL B C   1 
ATOM   2848 O  O   . VAL B 1 97  ? 30.822  -34.870 12.050  1.00 45.87  ? 73  VAL B O   1 
ATOM   2849 C  CB  . VAL B 1 97  ? 33.640  -33.318 13.064  1.00 46.99  ? 73  VAL B CB  1 
ATOM   2850 C  CG1 . VAL B 1 97  ? 32.908  -33.718 14.338  1.00 47.55  ? 73  VAL B CG1 1 
ATOM   2851 C  CG2 . VAL B 1 97  ? 35.138  -33.526 13.214  1.00 44.77  ? 73  VAL B CG2 1 
ATOM   2852 N  N   . ILE B 1 98  ? 31.147  -32.801 11.234  1.00 46.01  ? 74  ILE B N   1 
ATOM   2853 C  CA  . ILE B 1 98  ? 29.714  -32.561 11.090  1.00 43.71  ? 74  ILE B CA  1 
ATOM   2854 C  C   . ILE B 1 98  ? 29.117  -33.521 10.069  1.00 45.46  ? 74  ILE B C   1 
ATOM   2855 O  O   . ILE B 1 98  ? 28.052  -34.109 10.290  1.00 46.97  ? 74  ILE B O   1 
ATOM   2856 C  CB  . ILE B 1 98  ? 29.449  -31.096 10.701  1.00 41.98  ? 74  ILE B CB  1 
ATOM   2857 C  CG1 . ILE B 1 98  ? 29.963  -30.151 11.789  1.00 40.39  ? 74  ILE B CG1 1 
ATOM   2858 C  CG2 . ILE B 1 98  ? 27.960  -30.888 10.456  1.00 37.60  ? 74  ILE B CG2 1 
ATOM   2859 C  CD1 . ILE B 1 98  ? 29.955  -28.693 11.381  1.00 35.17  ? 74  ILE B CD1 1 
ATOM   2860 N  N   . LYS B 1 99  ? 29.793  -33.687 8.930   1.00 44.99  ? 75  LYS B N   1 
ATOM   2861 C  CA  . LYS B 1 99  ? 29.267  -34.550 7.878   1.00 47.75  ? 75  LYS B CA  1 
ATOM   2862 C  C   . LYS B 1 99  ? 29.031  -35.967 8.389   1.00 47.02  ? 75  LYS B C   1 
ATOM   2863 O  O   . LYS B 1 99  ? 28.023  -36.598 8.049   1.00 48.01  ? 75  LYS B O   1 
ATOM   2864 C  CB  . LYS B 1 99  ? 30.227  -34.565 6.687   1.00 48.39  ? 75  LYS B CB  1 
ATOM   2865 C  CG  . LYS B 1 99  ? 29.650  -35.216 5.441   1.00 47.77  ? 75  LYS B CG  1 
ATOM   2866 C  CD  . LYS B 1 99  ? 30.705  -35.410 4.365   1.00 46.07  ? 75  LYS B CD  1 
ATOM   2867 C  CE  . LYS B 1 99  ? 30.224  -36.379 3.301   1.00 47.63  ? 75  LYS B CE  1 
ATOM   2868 N  NZ  . LYS B 1 99  ? 31.249  -36.617 2.251   1.00 55.79  ? 75  LYS B NZ  1 
ATOM   2869 N  N   . GLN B 1 100 ? 29.950  -36.485 9.207   1.00 46.86  ? 76  GLN B N   1 
ATOM   2870 C  CA  . GLN B 1 100 ? 29.807  -37.848 9.711   1.00 52.25  ? 76  GLN B CA  1 
ATOM   2871 C  C   . GLN B 1 100 ? 28.578  -37.999 10.597  1.00 50.87  ? 76  GLN B C   1 
ATOM   2872 O  O   . GLN B 1 100 ? 27.988  -39.083 10.657  1.00 55.34  ? 76  GLN B O   1 
ATOM   2873 C  CB  . GLN B 1 100 ? 31.061  -38.259 10.485  1.00 56.15  ? 76  GLN B CB  1 
ATOM   2874 C  CG  . GLN B 1 100 ? 32.172  -38.829 9.618   1.00 65.50  ? 76  GLN B CG  1 
ATOM   2875 C  CD  . GLN B 1 100 ? 31.830  -40.195 9.056   1.00 77.75  ? 76  GLN B CD  1 
ATOM   2876 O  OE1 . GLN B 1 100 ? 31.352  -41.074 9.775   1.00 80.41  ? 76  GLN B OE1 1 
ATOM   2877 N  NE2 . GLN B 1 100 ? 32.068  -40.379 7.762   1.00 80.91  ? 76  GLN B NE2 1 
ATOM   2878 N  N   . ALA B 1 101 ? 28.178  -36.932 11.288  1.00 49.73  ? 77  ALA B N   1 
ATOM   2879 C  CA  . ALA B 1 101 ? 27.084  -36.992 12.246  1.00 48.38  ? 77  ALA B CA  1 
ATOM   2880 C  C   . ALA B 1 101 ? 25.756  -36.509 11.682  1.00 48.90  ? 77  ALA B C   1 
ATOM   2881 O  O   . ALA B 1 101 ? 24.712  -36.777 12.287  1.00 50.43  ? 77  ALA B O   1 
ATOM   2882 C  CB  . ALA B 1 101 ? 27.433  -36.162 13.489  1.00 43.70  ? 77  ALA B CB  1 
ATOM   2883 N  N   . SER B 1 102 ? 25.761  -35.817 10.546  1.00 48.34  ? 78  SER B N   1 
ATOM   2884 C  CA  . SER B 1 102 ? 24.549  -35.197 10.033  1.00 45.77  ? 78  SER B CA  1 
ATOM   2885 C  C   . SER B 1 102 ? 24.634  -35.101 8.518   1.00 45.26  ? 78  SER B C   1 
ATOM   2886 O  O   . SER B 1 102 ? 25.722  -34.969 7.950   1.00 44.11  ? 78  SER B O   1 
ATOM   2887 C  CB  . SER B 1 102 ? 24.344  -33.806 10.649  1.00 44.42  ? 78  SER B CB  1 
ATOM   2888 O  OG  . SER B 1 102 ? 23.448  -33.020 9.881   1.00 41.93  ? 78  SER B OG  1 
ATOM   2889 N  N   . ASP B 1 103 ? 23.472  -35.173 7.867   1.00 44.83  ? 79  ASP B N   1 
ATOM   2890 C  CA  . ASP B 1 103 ? 23.367  -34.950 6.433   1.00 46.38  ? 79  ASP B CA  1 
ATOM   2891 C  C   . ASP B 1 103 ? 22.906  -33.533 6.108   1.00 45.00  ? 79  ASP B C   1 
ATOM   2892 O  O   . ASP B 1 103 ? 22.407  -33.284 5.005   1.00 44.24  ? 79  ASP B O   1 
ATOM   2893 C  CB  . ASP B 1 103 ? 22.425  -35.978 5.801   1.00 48.99  ? 79  ASP B CB  1 
ATOM   2894 C  CG  . ASP B 1 103 ? 21.000  -35.860 6.310   1.00 56.90  ? 79  ASP B CG  1 
ATOM   2895 O  OD1 . ASP B 1 103 ? 20.814  -35.490 7.490   1.00 58.30  ? 79  ASP B OD1 1 
ATOM   2896 O  OD2 . ASP B 1 103 ? 20.063  -36.140 5.529   1.00 60.01  ? 79  ASP B OD2 1 
ATOM   2897 N  N   . ALA B 1 104 ? 23.060  -32.605 7.050   1.00 40.42  ? 80  ALA B N   1 
ATOM   2898 C  CA  . ALA B 1 104 ? 22.714  -31.214 6.798   1.00 39.90  ? 80  ALA B CA  1 
ATOM   2899 C  C   . ALA B 1 104 ? 23.592  -30.633 5.696   1.00 38.46  ? 80  ALA B C   1 
ATOM   2900 O  O   . ALA B 1 104 ? 24.725  -31.070 5.474   1.00 39.59  ? 80  ALA B O   1 
ATOM   2901 C  CB  . ALA B 1 104 ? 22.876  -30.390 8.075   1.00 35.24  ? 80  ALA B CB  1 
ATOM   2902 N  N   . VAL B 1 105 ? 23.053  -29.640 4.993   1.00 37.27  ? 81  VAL B N   1 
ATOM   2903 C  CA  . VAL B 1 105 ? 23.841  -28.920 4.002   1.00 34.51  ? 81  VAL B CA  1 
ATOM   2904 C  C   . VAL B 1 105 ? 24.811  -27.995 4.720   1.00 34.28  ? 81  VAL B C   1 
ATOM   2905 O  O   . VAL B 1 105 ? 24.409  -27.181 5.562   1.00 35.70  ? 81  VAL B O   1 
ATOM   2906 C  CB  . VAL B 1 105 ? 22.927  -28.132 3.052   1.00 34.88  ? 81  VAL B CB  1 
ATOM   2907 C  CG1 . VAL B 1 105 ? 23.749  -27.425 1.989   1.00 31.64  ? 81  VAL B CG1 1 
ATOM   2908 C  CG2 . VAL B 1 105 ? 21.895  -29.047 2.414   1.00 36.45  ? 81  VAL B CG2 1 
ATOM   2909 N  N   . LEU B 1 106 ? 26.093  -28.109 4.390   1.00 32.92  ? 82  LEU B N   1 
ATOM   2910 C  CA  . LEU B 1 106 ? 27.125  -27.282 4.999   1.00 36.30  ? 82  LEU B CA  1 
ATOM   2911 C  C   . LEU B 1 106 ? 27.425  -26.104 4.081   1.00 36.23  ? 82  LEU B C   1 
ATOM   2912 O  O   . LEU B 1 106 ? 27.754  -26.290 2.903   1.00 33.81  ? 82  LEU B O   1 
ATOM   2913 C  CB  . LEU B 1 106 ? 28.383  -28.101 5.284   1.00 34.88  ? 82  LEU B CB  1 
ATOM   2914 C  CG  . LEU B 1 106 ? 28.143  -29.322 6.182   1.00 37.89  ? 82  LEU B CG  1 
ATOM   2915 C  CD1 . LEU B 1 106 ? 29.445  -29.809 6.790   1.00 36.40  ? 82  LEU B CD1 1 
ATOM   2916 C  CD2 . LEU B 1 106 ? 27.117  -29.027 7.278   1.00 35.76  ? 82  LEU B CD2 1 
ATOM   2917 N  N   . ASN B 1 107 ? 27.310  -24.897 4.629   1.00 33.01  ? 83  ASN B N   1 
ATOM   2918 C  CA  . ASN B 1 107 ? 27.408  -23.646 3.884   1.00 32.42  ? 83  ASN B CA  1 
ATOM   2919 C  C   . ASN B 1 107 ? 28.624  -22.892 4.408   1.00 35.23  ? 83  ASN B C   1 
ATOM   2920 O  O   . ASN B 1 107 ? 28.633  -22.440 5.559   1.00 35.52  ? 83  ASN B O   1 
ATOM   2921 C  CB  . ASN B 1 107 ? 26.109  -22.850 4.039   1.00 34.31  ? 83  ASN B CB  1 
ATOM   2922 C  CG  . ASN B 1 107 ? 26.206  -21.423 3.527   1.00 35.73  ? 83  ASN B CG  1 
ATOM   2923 O  OD1 . ASN B 1 107 ? 27.219  -21.004 2.971   1.00 37.83  ? 83  ASN B OD1 1 
ATOM   2924 N  ND2 . ASN B 1 107 ? 25.128  -20.669 3.711   1.00 38.17  ? 83  ASN B ND2 1 
ATOM   2925 N  N   . ILE B 1 108 ? 29.655  -22.775 3.574   1.00 35.03  ? 84  ILE B N   1 
ATOM   2926 C  CA  . ILE B 1 108 ? 30.933  -22.204 3.988   1.00 37.02  ? 84  ILE B CA  1 
ATOM   2927 C  C   . ILE B 1 108 ? 30.960  -20.723 3.641   1.00 37.09  ? 84  ILE B C   1 
ATOM   2928 O  O   . ILE B 1 108 ? 30.610  -20.327 2.522   1.00 35.36  ? 84  ILE B O   1 
ATOM   2929 C  CB  . ILE B 1 108 ? 32.108  -22.942 3.325   1.00 35.40  ? 84  ILE B CB  1 
ATOM   2930 C  CG1 . ILE B 1 108 ? 32.111  -24.415 3.748   1.00 37.25  ? 84  ILE B CG1 1 
ATOM   2931 C  CG2 . ILE B 1 108 ? 33.433  -22.264 3.689   1.00 35.45  ? 84  ILE B CG2 1 
ATOM   2932 C  CD1 . ILE B 1 108 ? 33.219  -25.245 3.117   1.00 37.91  ? 84  ILE B CD1 1 
ATOM   2933 N  N   . THR B 1 109 ? 31.385  -19.904 4.597   1.00 36.40  ? 85  THR B N   1 
ATOM   2934 C  CA  . THR B 1 109 ? 31.466  -18.470 4.367   1.00 36.47  ? 85  THR B CA  1 
ATOM   2935 C  C   . THR B 1 109 ? 32.564  -18.145 3.361   1.00 39.96  ? 85  THR B C   1 
ATOM   2936 O  O   . THR B 1 109 ? 33.624  -18.777 3.342   1.00 38.99  ? 85  THR B O   1 
ATOM   2937 C  CB  . THR B 1 109 ? 31.737  -17.735 5.681   1.00 38.59  ? 85  THR B CB  1 
ATOM   2938 O  OG1 . THR B 1 109 ? 31.639  -16.320 5.475   1.00 37.24  ? 85  THR B OG1 1 
ATOM   2939 C  CG2 . THR B 1 109 ? 33.131  -18.069 6.211   1.00 40.16  ? 85  THR B CG2 1 
ATOM   2940 N  N   . THR B 1 110 ? 32.292  -17.164 2.503   1.00 38.61  ? 86  THR B N   1 
ATOM   2941 C  CA  . THR B 1 110 ? 33.327  -16.506 1.717   1.00 40.63  ? 86  THR B CA  1 
ATOM   2942 C  C   . THR B 1 110 ? 33.543  -15.070 2.174   1.00 45.77  ? 86  THR B C   1 
ATOM   2943 O  O   . THR B 1 110 ? 34.319  -14.339 1.552   1.00 46.13  ? 86  THR B O   1 
ATOM   2944 C  CB  . THR B 1 110 ? 32.986  -16.531 0.224   1.00 38.76  ? 86  THR B CB  1 
ATOM   2945 O  OG1 . THR B 1 110 ? 31.871  -15.666 -0.036  1.00 40.16  ? 86  THR B OG1 1 
ATOM   2946 C  CG2 . THR B 1 110 ? 32.651  -17.951 -0.236  1.00 39.98  ? 86  THR B CG2 1 
ATOM   2947 N  N   . GLY B 1 111 ? 32.873  -14.654 3.246   1.00 51.51  ? 87  GLY B N   1 
ATOM   2948 C  CA  . GLY B 1 111 ? 33.024  -13.313 3.768   1.00 52.47  ? 87  GLY B CA  1 
ATOM   2949 C  C   . GLY B 1 111 ? 34.000  -13.248 4.923   1.00 62.12  ? 87  GLY B C   1 
ATOM   2950 O  O   . GLY B 1 111 ? 34.834  -12.339 4.985   1.00 67.48  ? 87  GLY B O   1 
ATOM   2951 N  N   . GLY B 1 112 ? 33.914  -14.212 5.837   1.00 68.59  ? 88  GLY B N   1 
ATOM   2952 C  CA  . GLY B 1 112 ? 34.745  -14.156 7.027   1.00 70.33  ? 88  GLY B CA  1 
ATOM   2953 C  C   . GLY B 1 112 ? 34.530  -12.852 7.763   1.00 73.98  ? 88  GLY B C   1 
ATOM   2954 O  O   . GLY B 1 112 ? 33.418  -12.313 7.811   1.00 72.44  ? 88  GLY B O   1 
ATOM   2955 N  N   . ALA B 1 113 ? 35.602  -12.328 8.346   1.00 68.53  ? 89  ALA B N   1 
ATOM   2956 C  CA  . ALA B 1 113 ? 35.527  -10.998 8.925   1.00 66.39  ? 89  ALA B CA  1 
ATOM   2957 C  C   . ALA B 1 113 ? 35.436  -9.967  7.800   1.00 69.38  ? 89  ALA B C   1 
ATOM   2958 O  O   . ALA B 1 113 ? 36.106  -10.112 6.773   1.00 71.41  ? 89  ALA B O   1 
ATOM   2959 C  CB  . ALA B 1 113 ? 36.743  -10.717 9.805   1.00 62.56  ? 89  ALA B CB  1 
ATOM   2960 N  N   . PRO B 1 114 ? 34.626  -8.917  7.961   1.00 64.88  ? 90  PRO B N   1 
ATOM   2961 C  CA  . PRO B 1 114 ? 34.442  -7.953  6.865   1.00 62.58  ? 90  PRO B CA  1 
ATOM   2962 C  C   . PRO B 1 114 ? 35.705  -7.197  6.453   1.00 63.31  ? 90  PRO B C   1 
ATOM   2963 O  O   . PRO B 1 114 ? 35.629  -6.388  5.527   1.00 58.21  ? 90  PRO B O   1 
ATOM   2964 C  CB  . PRO B 1 114 ? 33.381  -6.987  7.425   1.00 59.34  ? 90  PRO B CB  1 
ATOM   2965 C  CG  . PRO B 1 114 ? 33.512  -7.091  8.906   1.00 63.54  ? 90  PRO B CG  1 
ATOM   2966 C  CD  . PRO B 1 114 ? 33.925  -8.507  9.191   1.00 65.01  ? 90  PRO B CD  1 
ATOM   2967 N  N   . THR B 1 115 ? 36.857  -7.431  7.096   1.00 67.68  ? 91  THR B N   1 
ATOM   2968 C  CA  . THR B 1 115 ? 38.094  -6.711  6.809   1.00 66.51  ? 91  THR B CA  1 
ATOM   2969 C  C   . THR B 1 115 ? 39.093  -7.558  6.021   1.00 65.60  ? 91  THR B C   1 
ATOM   2970 O  O   . THR B 1 115 ? 40.302  -7.367  6.156   1.00 69.17  ? 91  THR B O   1 
ATOM   2971 C  CB  . THR B 1 115 ? 38.723  -6.244  8.123   1.00 68.25  ? 91  THR B CB  1 
ATOM   2972 O  OG1 . THR B 1 115 ? 38.949  -7.383  8.962   1.00 68.13  ? 91  THR B OG1 1 
ATOM   2973 C  CG2 . THR B 1 115 ? 37.798  -5.273  8.855   1.00 63.88  ? 91  THR B CG2 1 
ATOM   2974 N  N   . MET B 1 116 ? 38.611  -8.487  5.196   1.00 65.86  ? 92  MET B N   1 
ATOM   2975 C  CA  . MET B 1 116 ? 39.453  -9.492  4.556   1.00 66.45  ? 92  MET B CA  1 
ATOM   2976 C  C   . MET B 1 116 ? 39.413  -9.363  3.032   1.00 67.28  ? 92  MET B C   1 
ATOM   2977 O  O   . MET B 1 116 ? 38.573  -8.660  2.461   1.00 64.31  ? 92  MET B O   1 
ATOM   2978 C  CB  . MET B 1 116 ? 39.024  -10.902 4.994   1.00 68.88  ? 92  MET B CB  1 
ATOM   2979 C  CG  . MET B 1 116 ? 39.307  -11.217 6.467   1.00 70.63  ? 92  MET B CG  1 
ATOM   2980 S  SD  . MET B 1 116 ? 39.026  -12.957 6.872   1.00 74.19  ? 92  MET B SD  1 
ATOM   2981 C  CE  . MET B 1 116 ? 39.265  -12.972 8.648   1.00 58.57  ? 92  MET B CE  1 
ATOM   2982 N  N   . SER B 1 117 ? 40.350  -10.066 2.378   1.00 69.19  ? 93  SER B N   1 
ATOM   2983 C  CA  . SER B 1 117 ? 40.572  -10.002 0.937   1.00 63.49  ? 93  SER B CA  1 
ATOM   2984 C  C   . SER B 1 117 ? 39.780  -11.102 0.224   1.00 64.86  ? 93  SER B C   1 
ATOM   2985 O  O   . SER B 1 117 ? 39.034  -11.848 0.850   1.00 65.58  ? 93  SER B O   1 
ATOM   2986 C  CB  . SER B 1 117 ? 42.066  -10.108 0.639   1.00 57.53  ? 93  SER B CB  1 
ATOM   2987 O  OG  . SER B 1 117 ? 42.289  -10.400 -0.729  1.00 62.51  ? 93  SER B OG  1 
ATOM   2988 N  N   . ILE B 1 118 ? 39.955  -11.239 -1.096  1.00 64.37  ? 94  ILE B N   1 
ATOM   2989 C  CA  . ILE B 1 118 ? 39.042  -12.056 -1.900  1.00 64.23  ? 94  ILE B CA  1 
ATOM   2990 C  C   . ILE B 1 118 ? 39.620  -13.419 -2.258  1.00 64.02  ? 94  ILE B C   1 
ATOM   2991 O  O   . ILE B 1 118 ? 39.248  -14.429 -1.649  1.00 61.18  ? 94  ILE B O   1 
ATOM   2992 C  CB  . ILE B 1 118 ? 38.622  -11.310 -3.179  1.00 60.38  ? 94  ILE B CB  1 
ATOM   2993 C  CG1 . ILE B 1 118 ? 37.821  -10.061 -2.812  1.00 58.90  ? 94  ILE B CG1 1 
ATOM   2994 C  CG2 . ILE B 1 118 ? 37.802  -12.224 -4.088  1.00 53.88  ? 94  ILE B CG2 1 
ATOM   2995 C  CD1 . ILE B 1 118 ? 36.547  -10.340 -2.022  1.00 57.88  ? 94  ILE B CD1 1 
ATOM   2996 N  N   . ALA B 1 119 ? 40.493  -13.474 -3.274  1.00 69.61  ? 95  ALA B N   1 
ATOM   2997 C  CA  . ALA B 1 119 ? 41.020  -14.763 -3.724  1.00 68.74  ? 95  ALA B CA  1 
ATOM   2998 C  C   . ALA B 1 119 ? 41.443  -15.631 -2.548  1.00 69.77  ? 95  ALA B C   1 
ATOM   2999 O  O   . ALA B 1 119 ? 41.399  -16.864 -2.634  1.00 68.67  ? 95  ALA B O   1 
ATOM   3000 C  CB  . ALA B 1 119 ? 42.199  -14.561 -4.681  1.00 64.28  ? 95  ALA B CB  1 
ATOM   3001 N  N   . GLU B 1 120 ? 41.841  -15.005 -1.439  1.00 62.75  ? 96  GLU B N   1 
ATOM   3002 C  CA  . GLU B 1 120 ? 42.106  -15.742 -0.212  1.00 57.32  ? 96  GLU B CA  1 
ATOM   3003 C  C   . GLU B 1 120 ? 40.815  -16.112 0.515   1.00 61.01  ? 96  GLU B C   1 
ATOM   3004 O  O   . GLU B 1 120 ? 40.694  -17.230 1.029   1.00 60.96  ? 96  GLU B O   1 
ATOM   3005 C  CB  . GLU B 1 120 ? 43.020  -14.916 0.695   1.00 62.35  ? 96  GLU B CB  1 
ATOM   3006 C  CG  . GLU B 1 120 ? 42.379  -13.656 1.277   1.00 63.47  ? 96  GLU B CG  1 
ATOM   3007 C  CD  . GLU B 1 120 ? 41.757  -13.881 2.651   1.00 66.41  ? 96  GLU B CD  1 
ATOM   3008 O  OE1 . GLU B 1 120 ? 41.650  -15.049 3.081   1.00 65.27  ? 96  GLU B OE1 1 
ATOM   3009 O  OE2 . GLU B 1 120 ? 41.381  -12.885 3.306   1.00 66.82  ? 96  GLU B OE2 1 
ATOM   3010 N  N   . ARG B 1 121 ? 39.839  -15.196 0.573   1.00 61.36  ? 97  ARG B N   1 
ATOM   3011 C  CA  . ARG B 1 121 ? 38.602  -15.498 1.290   1.00 56.25  ? 97  ARG B CA  1 
ATOM   3012 C  C   . ARG B 1 121 ? 37.874  -16.688 0.684   1.00 50.10  ? 97  ARG B C   1 
ATOM   3013 O  O   . ARG B 1 121 ? 37.149  -17.394 1.394   1.00 46.46  ? 97  ARG B O   1 
ATOM   3014 C  CB  . ARG B 1 121 ? 37.664  -14.285 1.310   1.00 55.09  ? 97  ARG B CB  1 
ATOM   3015 C  CG  . ARG B 1 121 ? 37.649  -13.515 2.646   1.00 60.39  ? 97  ARG B CG  1 
ATOM   3016 C  CD  . ARG B 1 121 ? 36.877  -12.174 2.595   1.00 60.32  ? 97  ARG B CD  1 
ATOM   3017 N  NE  . ARG B 1 121 ? 35.662  -12.221 1.788   1.00 58.24  ? 97  ARG B NE  1 
ATOM   3018 C  CZ  . ARG B 1 121 ? 35.075  -11.160 1.244   1.00 52.75  ? 97  ARG B CZ  1 
ATOM   3019 N  NH1 . ARG B 1 121 ? 35.595  -9.947  1.348   1.00 49.84  ? 97  ARG B NH1 1 
ATOM   3020 N  NH2 . ARG B 1 121 ? 33.941  -11.322 0.570   1.00 46.32  ? 97  ARG B NH2 1 
ATOM   3021 N  N   . ILE B 1 122 ? 38.040  -16.924 -0.624  1.00 46.39  ? 98  ILE B N   1 
ATOM   3022 C  CA  . ILE B 1 122 ? 37.336  -18.016 -1.284  1.00 50.74  ? 98  ILE B CA  1 
ATOM   3023 C  C   . ILE B 1 122 ? 38.089  -19.333 -1.191  1.00 47.91  ? 98  ILE B C   1 
ATOM   3024 O  O   . ILE B 1 122 ? 37.607  -20.349 -1.709  1.00 45.57  ? 98  ILE B O   1 
ATOM   3025 C  CB  . ILE B 1 122 ? 37.058  -17.689 -2.769  1.00 51.98  ? 98  ILE B CB  1 
ATOM   3026 C  CG1 . ILE B 1 122 ? 38.354  -17.559 -3.575  1.00 53.28  ? 98  ILE B CG1 1 
ATOM   3027 C  CG2 . ILE B 1 122 ? 36.252  -16.400 -2.891  1.00 50.06  ? 98  ILE B CG2 1 
ATOM   3028 C  CD1 . ILE B 1 122 ? 38.129  -17.600 -5.080  1.00 51.34  ? 98  ILE B CD1 1 
ATOM   3029 N  N   . GLN B 1 123 ? 39.254  -19.354 -0.536  1.00 48.44  ? 99  GLN B N   1 
ATOM   3030 C  CA  . GLN B 1 123 ? 40.076  -20.563 -0.561  1.00 48.81  ? 99  GLN B CA  1 
ATOM   3031 C  C   . GLN B 1 123 ? 39.419  -21.719 0.178   1.00 44.20  ? 99  GLN B C   1 
ATOM   3032 O  O   . GLN B 1 123 ? 39.399  -22.838 -0.364  1.00 42.78  ? 99  GLN B O   1 
ATOM   3033 C  CB  . GLN B 1 123 ? 41.469  -20.255 -0.009  1.00 49.10  ? 99  GLN B CB  1 
ATOM   3034 C  CG  . GLN B 1 123 ? 42.374  -19.577 -1.024  1.00 51.34  ? 99  GLN B CG  1 
ATOM   3035 C  CD  . GLN B 1 123 ? 43.834  -19.632 -0.634  1.00 52.31  ? 99  GLN B CD  1 
ATOM   3036 O  OE1 . GLN B 1 123 ? 44.705  -19.830 -1.481  1.00 53.34  ? 99  GLN B OE1 1 
ATOM   3037 N  NE2 . GLN B 1 123 ? 44.112  -19.453 0.653   1.00 53.47  ? 99  GLN B NE2 1 
ATOM   3038 N  N   . PRO B 1 124 ? 38.883  -21.546 1.390   1.00 43.36  ? 100 PRO B N   1 
ATOM   3039 C  CA  . PRO B 1 124 ? 38.174  -22.670 2.029   1.00 44.03  ? 100 PRO B CA  1 
ATOM   3040 C  C   . PRO B 1 124 ? 37.114  -23.292 1.131   1.00 44.34  ? 100 PRO B C   1 
ATOM   3041 O  O   . PRO B 1 124 ? 37.124  -24.510 0.909   1.00 41.61  ? 100 PRO B O   1 
ATOM   3042 C  CB  . PRO B 1 124 ? 37.575  -22.023 3.285   1.00 43.70  ? 100 PRO B CB  1 
ATOM   3043 C  CG  . PRO B 1 124 ? 38.503  -20.901 3.603   1.00 41.99  ? 100 PRO B CG  1 
ATOM   3044 C  CD  . PRO B 1 124 ? 38.972  -20.371 2.277   1.00 45.82  ? 100 PRO B CD  1 
ATOM   3045 N  N   . ALA B 1 125 ? 36.203  -22.478 0.590   1.00 41.06  ? 101 ALA B N   1 
ATOM   3046 C  CA  . ALA B 1 125 ? 35.178  -23.006 -0.304  1.00 40.72  ? 101 ALA B CA  1 
ATOM   3047 C  C   . ALA B 1 125 ? 35.794  -23.566 -1.580  1.00 42.39  ? 101 ALA B C   1 
ATOM   3048 O  O   . ALA B 1 125 ? 35.304  -24.558 -2.132  1.00 40.75  ? 101 ALA B O   1 
ATOM   3049 C  CB  . ALA B 1 125 ? 34.162  -21.914 -0.638  1.00 42.16  ? 101 ALA B CB  1 
ATOM   3050 N  N   . GLN B 1 126 ? 36.867  -22.940 -2.068  1.00 42.72  ? 102 GLN B N   1 
ATOM   3051 C  CA  . GLN B 1 126 ? 37.530  -23.436 -3.270  1.00 44.24  ? 102 GLN B CA  1 
ATOM   3052 C  C   . GLN B 1 126 ? 38.080  -24.840 -3.048  1.00 42.45  ? 102 GLN B C   1 
ATOM   3053 O  O   . GLN B 1 126 ? 37.905  -25.730 -3.887  1.00 42.88  ? 102 GLN B O   1 
ATOM   3054 C  CB  . GLN B 1 126 ? 38.650  -22.476 -3.677  1.00 45.59  ? 102 GLN B CB  1 
ATOM   3055 C  CG  . GLN B 1 126 ? 39.149  -22.660 -5.098  1.00 44.22  ? 102 GLN B CG  1 
ATOM   3056 C  CD  . GLN B 1 126 ? 40.222  -21.653 -5.468  1.00 51.40  ? 102 GLN B CD  1 
ATOM   3057 O  OE1 . GLN B 1 126 ? 40.786  -20.983 -4.601  1.00 51.49  ? 102 GLN B OE1 1 
ATOM   3058 N  NE2 . GLN B 1 126 ? 40.507  -21.540 -6.760  1.00 49.82  ? 102 GLN B NE2 1 
ATOM   3059 N  N   . HIS B 1 127 ? 38.738  -25.057 -1.908  1.00 41.86  ? 103 HIS B N   1 
ATOM   3060 C  CA  . HIS B 1 127 ? 39.338  -26.357 -1.628  1.00 42.36  ? 103 HIS B CA  1 
ATOM   3061 C  C   . HIS B 1 127 ? 38.277  -27.411 -1.325  1.00 42.93  ? 103 HIS B C   1 
ATOM   3062 O  O   . HIS B 1 127 ? 38.314  -28.519 -1.874  1.00 42.22  ? 103 HIS B O   1 
ATOM   3063 C  CB  . HIS B 1 127 ? 40.314  -26.232 -0.459  1.00 46.52  ? 103 HIS B CB  1 
ATOM   3064 C  CG  . HIS B 1 127 ? 40.826  -27.545 0.043   1.00 47.01  ? 103 HIS B CG  1 
ATOM   3065 N  ND1 . HIS B 1 127 ? 41.794  -28.268 -0.619  1.00 47.80  ? 103 HIS B ND1 1 
ATOM   3066 C  CD2 . HIS B 1 127 ? 40.500  -28.268 1.141   1.00 45.65  ? 103 HIS B CD2 1 
ATOM   3067 C  CE1 . HIS B 1 127 ? 42.046  -29.379 0.051   1.00 48.73  ? 103 HIS B CE1 1 
ATOM   3068 N  NE2 . HIS B 1 127 ? 41.274  -29.403 1.123   1.00 51.39  ? 103 HIS B NE2 1 
ATOM   3069 N  N   . TYR B 1 128 ? 37.320  -27.086 -0.453  1.00 44.16  ? 104 TYR B N   1 
ATOM   3070 C  CA  . TYR B 1 128 ? 36.383  -28.090 0.039   1.00 42.97  ? 104 TYR B CA  1 
ATOM   3071 C  C   . TYR B 1 128 ? 35.205  -28.330 -0.897  1.00 40.71  ? 104 TYR B C   1 
ATOM   3072 O  O   . TYR B 1 128 ? 34.512  -29.342 -0.742  1.00 42.40  ? 104 TYR B O   1 
ATOM   3073 C  CB  . TYR B 1 128 ? 35.865  -27.687 1.421   1.00 42.18  ? 104 TYR B CB  1 
ATOM   3074 C  CG  . TYR B 1 128 ? 36.917  -27.775 2.503   1.00 42.62  ? 104 TYR B CG  1 
ATOM   3075 C  CD1 . TYR B 1 128 ? 37.431  -29.004 2.898   1.00 42.63  ? 104 TYR B CD1 1 
ATOM   3076 C  CD2 . TYR B 1 128 ? 37.395  -26.632 3.130   1.00 42.92  ? 104 TYR B CD2 1 
ATOM   3077 C  CE1 . TYR B 1 128 ? 38.394  -29.093 3.885   1.00 43.10  ? 104 TYR B CE1 1 
ATOM   3078 C  CE2 . TYR B 1 128 ? 38.357  -26.710 4.120   1.00 43.20  ? 104 TYR B CE2 1 
ATOM   3079 C  CZ  . TYR B 1 128 ? 38.851  -27.943 4.494   1.00 45.67  ? 104 TYR B CZ  1 
ATOM   3080 O  OH  . TYR B 1 128 ? 39.807  -28.021 5.479   1.00 45.23  ? 104 TYR B OH  1 
ATOM   3081 N  N   . ARG B 1 129 ? 34.966  -27.443 -1.858  1.00 38.50  ? 105 ARG B N   1 
ATOM   3082 C  CA  . ARG B 1 129 ? 33.893  -27.602 -2.833  1.00 39.68  ? 105 ARG B CA  1 
ATOM   3083 C  C   . ARG B 1 129 ? 32.571  -27.963 -2.150  1.00 41.16  ? 105 ARG B C   1 
ATOM   3084 O  O   . ARG B 1 129 ? 31.989  -29.016 -2.429  1.00 40.14  ? 105 ARG B O   1 
ATOM   3085 C  CB  . ARG B 1 129 ? 34.263  -28.648 -3.875  1.00 43.89  ? 105 ARG B CB  1 
ATOM   3086 C  CG  . ARG B 1 129 ? 35.384  -28.215 -4.810  1.00 48.56  ? 105 ARG B CG  1 
ATOM   3087 C  CD  . ARG B 1 129 ? 35.619  -29.226 -5.924  1.00 54.11  ? 105 ARG B CD  1 
ATOM   3088 N  NE  . ARG B 1 129 ? 36.161  -30.489 -5.436  1.00 56.82  ? 105 ARG B NE  1 
ATOM   3089 C  CZ  . ARG B 1 129 ? 37.446  -30.710 -5.191  1.00 61.34  ? 105 ARG B CZ  1 
ATOM   3090 N  NH1 . ARG B 1 129 ? 38.352  -29.754 -5.331  1.00 59.14  ? 105 ARG B NH1 1 
ATOM   3091 N  NH2 . ARG B 1 129 ? 37.833  -31.919 -4.795  1.00 56.08  ? 105 ARG B NH2 1 
ATOM   3092 N  N   . PRO B 1 130 ? 32.074  -27.111 -1.256  1.00 40.74  ? 106 PRO B N   1 
ATOM   3093 C  CA  . PRO B 1 130 ? 30.810  -27.407 -0.572  1.00 38.03  ? 106 PRO B CA  1 
ATOM   3094 C  C   . PRO B 1 130 ? 29.619  -27.260 -1.506  1.00 37.31  ? 106 PRO B C   1 
ATOM   3095 O  O   . PRO B 1 130 ? 29.711  -26.734 -2.617  1.00 39.46  ? 106 PRO B O   1 
ATOM   3096 C  CB  . PRO B 1 130 ? 30.770  -26.362 0.546   1.00 36.34  ? 106 PRO B CB  1 
ATOM   3097 C  CG  . PRO B 1 130 ? 31.513  -25.205 -0.029  1.00 37.39  ? 106 PRO B CG  1 
ATOM   3098 C  CD  . PRO B 1 130 ? 32.639  -25.821 -0.824  1.00 37.84  ? 106 PRO B CD  1 
ATOM   3099 N  N   . GLU B 1 131 ? 28.470  -27.738 -1.023  1.00 35.86  ? 107 GLU B N   1 
ATOM   3100 C  CA  . GLU B 1 131 ? 27.226  -27.541 -1.758  1.00 36.98  ? 107 GLU B CA  1 
ATOM   3101 C  C   . GLU B 1 131 ? 26.844  -26.067 -1.802  1.00 34.76  ? 107 GLU B C   1 
ATOM   3102 O  O   . GLU B 1 131 ? 26.321  -25.584 -2.813  1.00 34.11  ? 107 GLU B O   1 
ATOM   3103 C  CB  . GLU B 1 131 ? 26.099  -28.350 -1.118  1.00 35.17  ? 107 GLU B CB  1 
ATOM   3104 C  CG  . GLU B 1 131 ? 26.380  -29.829 -0.976  1.00 39.77  ? 107 GLU B CG  1 
ATOM   3105 C  CD  . GLU B 1 131 ? 25.190  -30.582 -0.414  1.00 39.36  ? 107 GLU B CD  1 
ATOM   3106 O  OE1 . GLU B 1 131 ? 24.244  -30.855 -1.182  1.00 37.49  ? 107 GLU B OE1 1 
ATOM   3107 O  OE2 . GLU B 1 131 ? 25.194  -30.884 0.797   1.00 39.53  ? 107 GLU B OE2 1 
ATOM   3108 N  N   . LEU B 1 132 ? 27.097  -25.341 -0.715  1.00 33.65  ? 108 LEU B N   1 
ATOM   3109 C  CA  . LEU B 1 132 ? 26.695  -23.950 -0.578  1.00 35.00  ? 108 LEU B CA  1 
ATOM   3110 C  C   . LEU B 1 132 ? 27.855  -23.116 -0.063  1.00 33.83  ? 108 LEU B C   1 
ATOM   3111 O  O   . LEU B 1 132 ? 28.613  -23.559 0.805   1.00 33.19  ? 108 LEU B O   1 
ATOM   3112 C  CB  . LEU B 1 132 ? 25.512  -23.798 0.390   1.00 33.34  ? 108 LEU B CB  1 
ATOM   3113 C  CG  . LEU B 1 132 ? 24.105  -23.711 -0.190  1.00 34.75  ? 108 LEU B CG  1 
ATOM   3114 C  CD1 . LEU B 1 132 ? 23.111  -23.613 0.955   1.00 33.48  ? 108 LEU B CD1 1 
ATOM   3115 C  CD2 . LEU B 1 132 ? 23.970  -22.521 -1.129  1.00 34.70  ? 108 LEU B CD2 1 
ATOM   3116 N  N   . ALA B 1 133 ? 27.980  -21.905 -0.596  1.00 33.92  ? 109 ALA B N   1 
ATOM   3117 C  CA  . ALA B 1 133 ? 28.882  -20.902 -0.052  1.00 35.20  ? 109 ALA B CA  1 
ATOM   3118 C  C   . ALA B 1 133 ? 28.154  -19.568 -0.026  1.00 35.79  ? 109 ALA B C   1 
ATOM   3119 O  O   . ALA B 1 133 ? 27.354  -19.273 -0.918  1.00 31.16  ? 109 ALA B O   1 
ATOM   3120 C  CB  . ALA B 1 133 ? 30.171  -20.782 -0.873  1.00 35.03  ? 109 ALA B CB  1 
ATOM   3121 N  N   . SER B 1 134 ? 28.415  -18.773 1.006   1.00 34.69  ? 110 SER B N   1 
ATOM   3122 C  CA  . SER B 1 134 ? 27.846  -17.437 1.054   1.00 33.95  ? 110 SER B CA  1 
ATOM   3123 C  C   . SER B 1 134 ? 28.542  -16.543 0.034   1.00 36.75  ? 110 SER B C   1 
ATOM   3124 O  O   . SER B 1 134 ? 29.700  -16.765 -0.334  1.00 40.10  ? 110 SER B O   1 
ATOM   3125 C  CB  . SER B 1 134 ? 27.973  -16.843 2.456   1.00 36.03  ? 110 SER B CB  1 
ATOM   3126 O  OG  . SER B 1 134 ? 29.324  -16.563 2.773   1.00 39.15  ? 110 SER B OG  1 
ATOM   3127 N  N   . LEU B 1 135 ? 27.818  -15.532 -0.434  1.00 36.69  ? 111 LEU B N   1 
ATOM   3128 C  CA  . LEU B 1 135 ? 28.350  -14.612 -1.435  1.00 35.23  ? 111 LEU B CA  1 
ATOM   3129 C  C   . LEU B 1 135 ? 27.742  -13.243 -1.175  1.00 36.28  ? 111 LEU B C   1 
ATOM   3130 O  O   . LEU B 1 135 ? 26.552  -13.030 -1.428  1.00 34.32  ? 111 LEU B O   1 
ATOM   3131 C  CB  . LEU B 1 135 ? 28.037  -15.098 -2.847  1.00 35.80  ? 111 LEU B CB  1 
ATOM   3132 C  CG  . LEU B 1 135 ? 28.605  -14.264 -3.999  1.00 34.30  ? 111 LEU B CG  1 
ATOM   3133 C  CD1 . LEU B 1 135 ? 30.111  -14.119 -3.870  1.00 37.23  ? 111 LEU B CD1 1 
ATOM   3134 C  CD2 . LEU B 1 135 ? 28.246  -14.899 -5.328  1.00 37.50  ? 111 LEU B CD2 1 
ATOM   3135 N  N   . ASN B 1 136 ? 28.553  -12.323 -0.667  1.00 36.04  ? 112 ASN B N   1 
ATOM   3136 C  CA  . ASN B 1 136 ? 28.077  -10.982 -0.363  1.00 37.10  ? 112 ASN B CA  1 
ATOM   3137 C  C   . ASN B 1 136 ? 28.117  -10.123 -1.620  1.00 33.26  ? 112 ASN B C   1 
ATOM   3138 O  O   . ASN B 1 136 ? 29.081  -10.161 -2.388  1.00 33.79  ? 112 ASN B O   1 
ATOM   3139 C  CB  . ASN B 1 136 ? 28.917  -10.382 0.757   1.00 34.29  ? 112 ASN B CB  1 
ATOM   3140 C  CG  . ASN B 1 136 ? 28.913  -11.255 1.996   1.00 40.61  ? 112 ASN B CG  1 
ATOM   3141 O  OD1 . ASN B 1 136 ? 28.086  -11.078 2.889   1.00 44.10  ? 112 ASN B OD1 1 
ATOM   3142 N  ND2 . ASN B 1 136 ? 29.823  -12.224 2.043   1.00 40.09  ? 112 ASN B ND2 1 
ATOM   3143 N  N   . MET B 1 137 ? 27.050  -9.354  -1.832  1.00 33.93  ? 113 MET B N   1 
ATOM   3144 C  CA  . MET B 1 137 ? 26.734  -8.813  -3.146  1.00 32.84  ? 113 MET B CA  1 
ATOM   3145 C  C   . MET B 1 137 ? 27.067  -7.334  -3.305  1.00 33.03  ? 113 MET B C   1 
ATOM   3146 O  O   . MET B 1 137 ? 26.732  -6.749  -4.340  1.00 32.72  ? 113 MET B O   1 
ATOM   3147 C  CB  . MET B 1 137 ? 25.252  -9.042  -3.447  1.00 32.04  ? 113 MET B CB  1 
ATOM   3148 C  CG  . MET B 1 137 ? 24.895  -10.497 -3.711  1.00 31.64  ? 113 MET B CG  1 
ATOM   3149 S  SD  . MET B 1 137 ? 25.896  -11.233 -5.018  1.00 34.96  ? 113 MET B SD  1 
ATOM   3150 C  CE  . MET B 1 137 ? 25.641  -10.051 -6.339  1.00 29.81  ? 113 MET B CE  1 
ATOM   3151 N  N   . GLY B 1 138 ? 27.725  -6.716  -2.332  1.00 31.72  ? 114 GLY B N   1 
ATOM   3152 C  CA  . GLY B 1 138 ? 28.075  -5.317  -2.476  1.00 32.06  ? 114 GLY B CA  1 
ATOM   3153 C  C   . GLY B 1 138 ? 29.076  -4.874  -1.436  1.00 37.42  ? 114 GLY B C   1 
ATOM   3154 O  O   . GLY B 1 138 ? 29.191  -5.467  -0.358  1.00 34.96  ? 114 GLY B O   1 
ATOM   3155 N  N   . THR B 1 139 ? 29.809  -3.821  -1.785  1.00 38.03  ? 115 THR B N   1 
ATOM   3156 C  CA  . THR B 1 139 ? 30.707  -3.174  -0.842  1.00 35.65  ? 115 THR B CA  1 
ATOM   3157 C  C   . THR B 1 139 ? 29.919  -2.225  0.051   1.00 37.67  ? 115 THR B C   1 
ATOM   3158 O  O   . THR B 1 139 ? 29.075  -1.458  -0.423  1.00 37.00  ? 115 THR B O   1 
ATOM   3159 C  CB  . THR B 1 139 ? 31.808  -2.415  -1.580  1.00 37.46  ? 115 THR B CB  1 
ATOM   3160 O  OG1 . THR B 1 139 ? 32.527  -3.317  -2.429  1.00 38.73  ? 115 THR B OG1 1 
ATOM   3161 C  CG2 . THR B 1 139 ? 32.782  -1.779  -0.596  1.00 39.34  ? 115 THR B CG2 1 
ATOM   3162 N  N   . MET B 1 140 ? 30.199  -2.282  1.349   1.00 36.15  ? 116 MET B N   1 
ATOM   3163 C  CA  . MET B 1 140 ? 29.411  -1.547  2.323   1.00 37.54  ? 116 MET B CA  1 
ATOM   3164 C  C   . MET B 1 140 ? 30.266  -1.224  3.537   1.00 39.60  ? 116 MET B C   1 
ATOM   3165 O  O   . MET B 1 140 ? 31.274  -1.882  3.807   1.00 36.29  ? 116 MET B O   1 
ATOM   3166 C  CB  . MET B 1 140 ? 28.180  -2.349  2.763   1.00 37.00  ? 116 MET B CB  1 
ATOM   3167 C  CG  . MET B 1 140 ? 28.526  -3.728  3.316   1.00 36.04  ? 116 MET B CG  1 
ATOM   3168 S  SD  . MET B 1 140 ? 27.097  -4.770  3.679   1.00 36.49  ? 116 MET B SD  1 
ATOM   3169 C  CE  . MET B 1 140 ? 26.535  -4.081  5.233   1.00 34.30  ? 116 MET B CE  1 
ATOM   3170 N  N   . ASN B 1 141 ? 29.846  -0.193  4.266   1.00 37.74  ? 117 ASN B N   1 
ATOM   3171 C  CA  . ASN B 1 141 ? 30.365  0.029   5.604   1.00 37.65  ? 117 ASN B CA  1 
ATOM   3172 C  C   . ASN B 1 141 ? 29.815  -1.031  6.553   1.00 39.39  ? 117 ASN B C   1 
ATOM   3173 O  O   . ASN B 1 141 ? 28.688  -1.510  6.403   1.00 36.71  ? 117 ASN B O   1 
ATOM   3174 C  CB  . ASN B 1 141 ? 29.985  1.423   6.115   1.00 36.86  ? 117 ASN B CB  1 
ATOM   3175 C  CG  . ASN B 1 141 ? 30.609  2.547   5.306   1.00 37.64  ? 117 ASN B CG  1 
ATOM   3176 O  OD1 . ASN B 1 141 ? 31.652  2.380   4.669   1.00 38.91  ? 117 ASN B OD1 1 
ATOM   3177 N  ND2 . ASN B 1 141 ? 29.976  3.713   5.343   1.00 36.18  ? 117 ASN B ND2 1 
ATOM   3178 N  N   . PHE B 1 142 ? 30.641  -1.413  7.525   1.00 42.26  ? 118 PHE B N   1 
ATOM   3179 C  CA  . PHE B 1 142 ? 30.249  -2.299  8.635   1.00 42.28  ? 118 PHE B CA  1 
ATOM   3180 C  C   . PHE B 1 142 ? 30.485  -1.510  9.921   1.00 43.06  ? 118 PHE B C   1 
ATOM   3181 O  O   . PHE B 1 142 ? 31.621  -1.118  10.211  1.00 45.84  ? 118 PHE B O   1 
ATOM   3182 C  CB  . PHE B 1 142 ? 31.034  -3.605  8.619   1.00 49.33  ? 118 PHE B CB  1 
ATOM   3183 C  CG  . PHE B 1 142 ? 30.265  -4.795  8.132   1.00 53.25  ? 118 PHE B CG  1 
ATOM   3184 C  CD1 . PHE B 1 142 ? 30.146  -5.059  6.779   1.00 55.30  ? 118 PHE B CD1 1 
ATOM   3185 C  CD2 . PHE B 1 142 ? 29.643  -5.632  9.040   1.00 58.00  ? 118 PHE B CD2 1 
ATOM   3186 C  CE1 . PHE B 1 142 ? 29.423  -6.161  6.361   1.00 55.01  ? 118 PHE B CE1 1 
ATOM   3187 C  CE2 . PHE B 1 142 ? 28.918  -6.728  8.610   1.00 59.90  ? 118 PHE B CE2 1 
ATOM   3188 C  CZ  . PHE B 1 142 ? 28.810  -6.989  7.270   1.00 56.78  ? 118 PHE B CZ  1 
ATOM   3189 N  N   . GLY B 1 143 ? 29.420  -1.303  10.690  1.00 46.38  ? 119 GLY B N   1 
ATOM   3190 C  CA  . GLY B 1 143 ? 29.473  -0.536  11.920  1.00 49.13  ? 119 GLY B CA  1 
ATOM   3191 C  C   . GLY B 1 143 ? 29.268  -1.448  13.111  1.00 52.09  ? 119 GLY B C   1 
ATOM   3192 O  O   . GLY B 1 143 ? 28.272  -2.174  13.189  1.00 51.36  ? 119 GLY B O   1 
ATOM   3193 N  N   . LEU B 1 144 ? 30.233  -1.416  14.025  1.00 53.50  ? 120 LEU B N   1 
ATOM   3194 C  CA  . LEU B 1 144 ? 30.156  -2.205  15.278  1.00 58.49  ? 120 LEU B CA  1 
ATOM   3195 C  C   . LEU B 1 144 ? 30.456  -1.322  16.494  1.00 62.17  ? 120 LEU B C   1 
ATOM   3196 O  O   . LEU B 1 144 ? 30.256  -1.812  17.610  1.00 66.78  ? 120 LEU B O   1 
ATOM   3197 C  CB  . LEU B 1 144 ? 31.163  -3.350  15.175  1.00 62.17  ? 120 LEU B CB  1 
ATOM   3198 C  CG  . LEU B 1 144 ? 31.197  -4.091  13.841  1.00 60.96  ? 120 LEU B CG  1 
ATOM   3199 C  CD1 . LEU B 1 144 ? 32.541  -4.768  13.636  1.00 61.09  ? 120 LEU B CD1 1 
ATOM   3200 C  CD2 . LEU B 1 144 ? 30.069  -5.107  13.751  1.00 61.44  ? 120 LEU B CD2 1 
ATOM   3201 N  N   . PHE B 1 145 ? 30.879  -0.065  16.333  1.00 61.45  ? 121 PHE B N   1 
ATOM   3202 C  CA  . PHE B 1 145 ? 31.268  0.775   17.461  1.00 64.35  ? 121 PHE B CA  1 
ATOM   3203 C  C   . PHE B 1 145 ? 30.083  1.164   18.342  1.00 70.39  ? 121 PHE B C   1 
ATOM   3204 O  O   . PHE B 1 145 ? 30.294  1.575   19.490  1.00 74.13  ? 121 PHE B O   1 
ATOM   3205 C  CB  . PHE B 1 145 ? 32.014  2.029   16.972  1.00 58.77  ? 121 PHE B CB  1 
ATOM   3206 C  CG  . PHE B 1 145 ? 31.326  2.775   15.853  1.00 58.95  ? 121 PHE B CG  1 
ATOM   3207 C  CD1 . PHE B 1 145 ? 31.510  2.395   14.530  1.00 54.63  ? 121 PHE B CD1 1 
ATOM   3208 C  CD2 . PHE B 1 145 ? 30.523  3.873   16.121  1.00 57.11  ? 121 PHE B CD2 1 
ATOM   3209 C  CE1 . PHE B 1 145 ? 30.887  3.075   13.504  1.00 52.26  ? 121 PHE B CE1 1 
ATOM   3210 C  CE2 . PHE B 1 145 ? 29.899  4.561   15.092  1.00 55.37  ? 121 PHE B CE2 1 
ATOM   3211 C  CZ  . PHE B 1 145 ? 30.085  4.162   13.784  1.00 51.40  ? 121 PHE B CZ  1 
ATOM   3212 N  N   . PRO B 1 146 ? 28.834  1.060   17.873  1.00 71.19  ? 122 PRO B N   1 
ATOM   3213 C  CA  . PRO B 1 146 ? 27.724  1.106   18.840  1.00 75.82  ? 122 PRO B CA  1 
ATOM   3214 C  C   . PRO B 1 146 ? 27.661  -0.146  19.693  1.00 81.25  ? 122 PRO B C   1 
ATOM   3215 O  O   . PRO B 1 146 ? 27.355  -0.065  20.889  1.00 84.46  ? 122 PRO B O   1 
ATOM   3216 C  CB  . PRO B 1 146 ? 26.482  1.264   17.950  1.00 76.55  ? 122 PRO B CB  1 
ATOM   3217 C  CG  . PRO B 1 146 ? 27.000  1.755   16.645  1.00 67.30  ? 122 PRO B CG  1 
ATOM   3218 C  CD  . PRO B 1 146 ? 28.338  1.120   16.488  1.00 64.07  ? 122 PRO B CD  1 
ATOM   3219 N  N   . MET B 1 147 ? 27.940  -1.311  19.103  1.00 80.92  ? 123 MET B N   1 
ATOM   3220 C  CA  . MET B 1 147 ? 28.117  -2.524  19.891  1.00 81.41  ? 123 MET B CA  1 
ATOM   3221 C  C   . MET B 1 147 ? 29.106  -2.299  21.027  1.00 83.36  ? 123 MET B C   1 
ATOM   3222 O  O   . MET B 1 147 ? 29.022  -2.958  22.070  1.00 83.27  ? 123 MET B O   1 
ATOM   3223 C  CB  . MET B 1 147 ? 28.601  -3.655  18.981  1.00 80.68  ? 123 MET B CB  1 
ATOM   3224 C  CG  . MET B 1 147 ? 27.828  -4.960  19.102  1.00 81.06  ? 123 MET B CG  1 
ATOM   3225 S  SD  . MET B 1 147 ? 28.362  -6.226  17.923  1.00 82.83  ? 123 MET B SD  1 
ATOM   3226 C  CE  . MET B 1 147 ? 28.276  -5.358  16.355  1.00 71.81  ? 123 MET B CE  1 
ATOM   3227 N  N   . LEU B 1 148 ? 30.050  -1.373  20.842  1.00 83.79  ? 124 LEU B N   1 
ATOM   3228 C  CA  . LEU B 1 148 ? 31.009  -1.059  21.894  1.00 83.48  ? 124 LEU B CA  1 
ATOM   3229 C  C   . LEU B 1 148 ? 30.334  -0.404  23.091  1.00 86.57  ? 124 LEU B C   1 
ATOM   3230 O  O   . LEU B 1 148 ? 30.812  -0.541  24.223  1.00 85.51  ? 124 LEU B O   1 
ATOM   3231 C  CB  . LEU B 1 148 ? 32.097  -0.140  21.341  1.00 82.08  ? 124 LEU B CB  1 
ATOM   3232 C  CG  . LEU B 1 148 ? 33.380  -0.008  22.159  1.00 81.93  ? 124 LEU B CG  1 
ATOM   3233 C  CD1 . LEU B 1 148 ? 34.208  -1.277  22.058  1.00 73.71  ? 124 LEU B CD1 1 
ATOM   3234 C  CD2 . LEU B 1 148 ? 34.182  1.200   21.701  1.00 79.66  ? 124 LEU B CD2 1 
ATOM   3235 N  N   . ASN B 1 149 ? 29.227  0.306   22.864  1.00 93.28  ? 125 ASN B N   1 
ATOM   3236 C  CA  . ASN B 1 149 ? 28.571  1.035   23.944  1.00 98.59  ? 125 ASN B CA  1 
ATOM   3237 C  C   . ASN B 1 149 ? 28.317  0.135   25.148  1.00 96.14  ? 125 ASN B C   1 
ATOM   3238 O  O   . ASN B 1 149 ? 28.625  0.501   26.289  1.00 96.83  ? 125 ASN B O   1 
ATOM   3239 C  CB  . ASN B 1 149 ? 27.260  1.636   23.436  1.00 99.97  ? 125 ASN B CB  1 
ATOM   3240 C  CG  . ASN B 1 149 ? 27.459  2.531   22.224  1.00 99.63  ? 125 ASN B CG  1 
ATOM   3241 O  OD1 . ASN B 1 149 ? 28.583  2.722   21.756  1.00 99.82  ? 125 ASN B OD1 1 
ATOM   3242 N  ND2 . ASN B 1 149 ? 26.365  3.075   21.705  1.00 96.92  ? 125 ASN B ND2 1 
ATOM   3243 N  N   . ARG B 1 150 ? 27.761  -1.053  24.913  1.00 87.26  ? 126 ARG B N   1 
ATOM   3244 C  CA  . ARG B 1 150 ? 27.364  -1.922  26.014  1.00 84.42  ? 126 ARG B CA  1 
ATOM   3245 C  C   . ARG B 1 150 ? 28.464  -2.881  26.452  1.00 79.25  ? 126 ARG B C   1 
ATOM   3246 O  O   . ARG B 1 150 ? 28.541  -3.216  27.640  1.00 79.69  ? 126 ARG B O   1 
ATOM   3247 C  CB  . ARG B 1 150 ? 26.111  -2.721  25.629  1.00 81.39  ? 126 ARG B CB  1 
ATOM   3248 C  CG  . ARG B 1 150 ? 26.336  -3.881  24.666  1.00 74.50  ? 126 ARG B CG  1 
ATOM   3249 C  CD  . ARG B 1 150 ? 25.130  -4.801  24.642  1.00 74.14  ? 126 ARG B CD  1 
ATOM   3250 N  NE  . ARG B 1 150 ? 23.916  -4.119  24.211  1.00 84.35  ? 126 ARG B NE  1 
ATOM   3251 C  CZ  . ARG B 1 150 ? 22.689  -4.584  24.403  1.00 86.36  ? 126 ARG B CZ  1 
ATOM   3252 N  NH1 . ARG B 1 150 ? 22.472  -5.713  25.057  1.00 83.82  ? 126 ARG B NH1 1 
ATOM   3253 N  NH2 . ARG B 1 150 ? 21.654  -3.896  23.933  1.00 90.68  ? 126 ARG B NH2 1 
ATOM   3254 N  N   . TYR B 1 151 ? 29.319  -3.332  25.531  1.00 77.99  ? 127 TYR B N   1 
ATOM   3255 C  CA  . TYR B 1 151 ? 30.286  -4.381  25.827  1.00 71.00  ? 127 TYR B CA  1 
ATOM   3256 C  C   . TYR B 1 151 ? 31.666  -3.860  26.208  1.00 70.20  ? 127 TYR B C   1 
ATOM   3257 O  O   . TYR B 1 151 ? 32.498  -4.654  26.658  1.00 69.76  ? 127 TYR B O   1 
ATOM   3258 C  CB  . TYR B 1 151 ? 30.443  -5.324  24.624  1.00 62.37  ? 127 TYR B CB  1 
ATOM   3259 C  CG  . TYR B 1 151 ? 29.203  -6.108  24.253  1.00 61.06  ? 127 TYR B CG  1 
ATOM   3260 C  CD1 . TYR B 1 151 ? 28.647  -7.028  25.132  1.00 56.44  ? 127 TYR B CD1 1 
ATOM   3261 C  CD2 . TYR B 1 151 ? 28.605  -5.947  23.010  1.00 60.22  ? 127 TYR B CD2 1 
ATOM   3262 C  CE1 . TYR B 1 151 ? 27.517  -7.752  24.789  1.00 55.51  ? 127 TYR B CE1 1 
ATOM   3263 C  CE2 . TYR B 1 151 ? 27.479  -6.667  22.659  1.00 62.82  ? 127 TYR B CE2 1 
ATOM   3264 C  CZ  . TYR B 1 151 ? 26.941  -7.569  23.550  1.00 57.45  ? 127 TYR B CZ  1 
ATOM   3265 O  OH  . TYR B 1 151 ? 25.818  -8.281  23.200  1.00 60.11  ? 127 TYR B OH  1 
ATOM   3266 N  N   . GLU B 1 152 ? 31.937  -2.562  26.044  1.00 74.89  ? 128 GLU B N   1 
ATOM   3267 C  CA  . GLU B 1 152 ? 33.306  -2.077  26.205  1.00 75.18  ? 128 GLU B CA  1 
ATOM   3268 C  C   . GLU B 1 152 ? 33.884  -2.433  27.568  1.00 74.45  ? 128 GLU B C   1 
ATOM   3269 O  O   . GLU B 1 152 ? 35.102  -2.602  27.699  1.00 72.29  ? 128 GLU B O   1 
ATOM   3270 C  CB  . GLU B 1 152 ? 33.363  -0.565  25.997  1.00 81.25  ? 128 GLU B CB  1 
ATOM   3271 C  CG  . GLU B 1 152 ? 34.774  -0.032  25.799  1.00 84.45  ? 128 GLU B CG  1 
ATOM   3272 C  CD  . GLU B 1 152 ? 34.805  1.310   25.091  1.00 91.06  ? 128 GLU B CD  1 
ATOM   3273 O  OE1 . GLU B 1 152 ? 33.729  1.916   24.910  1.00 92.66  ? 128 GLU B OE1 1 
ATOM   3274 O  OE2 . GLU B 1 152 ? 35.909  1.755   24.711  1.00 96.05  ? 128 GLU B OE2 1 
ATOM   3275 N  N   . SER B 1 153 ? 33.036  -2.556  28.589  1.00 80.24  ? 129 SER B N   1 
ATOM   3276 C  CA  . SER B 1 153 ? 33.539  -2.808  29.935  1.00 76.99  ? 129 SER B CA  1 
ATOM   3277 C  C   . SER B 1 153 ? 34.178  -4.187  30.050  1.00 72.30  ? 129 SER B C   1 
ATOM   3278 O  O   . SER B 1 153 ? 35.169  -4.358  30.768  1.00 73.84  ? 129 SER B O   1 
ATOM   3279 C  CB  . SER B 1 153 ? 32.403  -2.667  30.949  1.00 80.10  ? 129 SER B CB  1 
ATOM   3280 O  OG  . SER B 1 153 ? 31.740  -1.423  30.807  1.00 85.83  ? 129 SER B OG  1 
ATOM   3281 N  N   . GLN B 1 154 ? 33.634  -5.181  29.345  1.00 67.58  ? 130 GLN B N   1 
ATOM   3282 C  CA  . GLN B 1 154 ? 33.969  -6.580  29.579  1.00 63.46  ? 130 GLN B CA  1 
ATOM   3283 C  C   . GLN B 1 154 ? 34.851  -7.177  28.485  1.00 60.19  ? 130 GLN B C   1 
ATOM   3284 O  O   . GLN B 1 154 ? 34.975  -8.402  28.401  1.00 57.56  ? 130 GLN B O   1 
ATOM   3285 C  CB  . GLN B 1 154 ? 32.684  -7.399  29.717  1.00 63.65  ? 130 GLN B CB  1 
ATOM   3286 C  CG  . GLN B 1 154 ? 31.894  -7.521  28.422  1.00 57.67  ? 130 GLN B CG  1 
ATOM   3287 C  CD  . GLN B 1 154 ? 30.423  -7.813  28.652  1.00 60.16  ? 130 GLN B CD  1 
ATOM   3288 O  OE1 . GLN B 1 154 ? 29.706  -7.012  29.251  1.00 62.28  ? 130 GLN B OE1 1 
ATOM   3289 N  NE2 . GLN B 1 154 ? 29.965  -8.963  28.170  1.00 54.12  ? 130 GLN B NE2 1 
ATOM   3290 N  N   . LEU B 1 155 ? 35.477  -6.346  27.655  1.00 61.61  ? 131 LEU B N   1 
ATOM   3291 C  CA  . LEU B 1 155 ? 36.302  -6.850  26.562  1.00 57.91  ? 131 LEU B CA  1 
ATOM   3292 C  C   . LEU B 1 155 ? 37.658  -7.294  27.101  1.00 57.25  ? 131 LEU B C   1 
ATOM   3293 O  O   . LEU B 1 155 ? 38.400  -6.492  27.678  1.00 60.09  ? 131 LEU B O   1 
ATOM   3294 C  CB  . LEU B 1 155 ? 36.471  -5.786  25.481  1.00 57.70  ? 131 LEU B CB  1 
ATOM   3295 C  CG  . LEU B 1 155 ? 35.187  -5.381  24.752  1.00 55.67  ? 131 LEU B CG  1 
ATOM   3296 C  CD1 . LEU B 1 155 ? 35.484  -4.325  23.703  1.00 59.31  ? 131 LEU B CD1 1 
ATOM   3297 C  CD2 . LEU B 1 155 ? 34.503  -6.588  24.121  1.00 49.29  ? 131 LEU B CD2 1 
ATOM   3298 N  N   . LYS B 1 156 ? 37.980  -8.573  26.902  1.00 51.91  ? 132 LYS B N   1 
ATOM   3299 C  CA  . LYS B 1 156 ? 39.199  -9.173  27.428  1.00 55.86  ? 132 LYS B CA  1 
ATOM   3300 C  C   . LYS B 1 156 ? 40.388  -9.007  26.488  1.00 52.78  ? 132 LYS B C   1 
ATOM   3301 O  O   . LYS B 1 156 ? 41.489  -8.676  26.939  1.00 54.37  ? 132 LYS B O   1 
ATOM   3302 C  CB  . LYS B 1 156 ? 38.966  -10.663 27.703  1.00 54.75  ? 132 LYS B CB  1 
ATOM   3303 C  CG  . LYS B 1 156 ? 37.765  -10.954 28.600  1.00 62.93  ? 132 LYS B CG  1 
ATOM   3304 C  CD  . LYS B 1 156 ? 37.399  -12.434 28.590  1.00 69.28  ? 132 LYS B CD  1 
ATOM   3305 C  CE  . LYS B 1 156 ? 36.295  -12.755 29.593  1.00 72.46  ? 132 LYS B CE  1 
ATOM   3306 N  NZ  . LYS B 1 156 ? 34.992  -12.113 29.253  1.00 65.10  ? 132 LYS B NZ  1 
ATOM   3307 N  N   . HIS B 1 157 ? 40.191  -9.223  25.190  1.00 51.32  ? 133 HIS B N   1 
ATOM   3308 C  CA  . HIS B 1 157 ? 41.277  -9.221  24.221  1.00 51.11  ? 133 HIS B CA  1 
ATOM   3309 C  C   . HIS B 1 157 ? 41.391  -7.866  23.537  1.00 52.63  ? 133 HIS B C   1 
ATOM   3310 O  O   . HIS B 1 157 ? 40.382  -7.225  23.225  1.00 49.29  ? 133 HIS B O   1 
ATOM   3311 C  CB  . HIS B 1 157 ? 41.065  -10.310 23.169  1.00 48.87  ? 133 HIS B CB  1 
ATOM   3312 C  CG  . HIS B 1 157 ? 40.929  -11.684 23.744  1.00 50.37  ? 133 HIS B CG  1 
ATOM   3313 N  ND1 . HIS B 1 157 ? 41.975  -12.340 24.356  1.00 52.05  ? 133 HIS B ND1 1 
ATOM   3314 C  CD2 . HIS B 1 157 ? 39.871  -12.527 23.802  1.00 49.96  ? 133 HIS B CD2 1 
ATOM   3315 C  CE1 . HIS B 1 157 ? 41.567  -13.527 24.767  1.00 51.78  ? 133 HIS B CE1 1 
ATOM   3316 N  NE2 . HIS B 1 157 ? 40.294  -13.666 24.442  1.00 53.62  ? 133 HIS B NE2 1 
ATOM   3317 N  N   . GLN B 1 158 ? 42.634  -7.442  23.293  1.00 48.49  ? 134 GLN B N   1 
ATOM   3318 C  CA  . GLN B 1 158 ? 42.866  -6.162  22.634  1.00 50.82  ? 134 GLN B CA  1 
ATOM   3319 C  C   . GLN B 1 158 ? 42.256  -6.139  21.238  1.00 48.92  ? 134 GLN B C   1 
ATOM   3320 O  O   . GLN B 1 158 ? 41.744  -5.104  20.795  1.00 51.20  ? 134 GLN B O   1 
ATOM   3321 C  CB  . GLN B 1 158 ? 44.367  -5.871  22.561  1.00 52.42  ? 134 GLN B CB  1 
ATOM   3322 C  CG  . GLN B 1 158 ? 44.705  -4.499  21.994  1.00 54.95  ? 134 GLN B CG  1 
ATOM   3323 C  CD  . GLN B 1 158 ? 44.143  -3.369  22.836  1.00 60.04  ? 134 GLN B CD  1 
ATOM   3324 O  OE1 . GLN B 1 158 ? 44.174  -3.423  24.065  1.00 65.93  ? 134 GLN B OE1 1 
ATOM   3325 N  NE2 . GLN B 1 158 ? 43.616  -2.343  22.177  1.00 60.79  ? 134 GLN B NE2 1 
ATOM   3326 N  N   . TRP B 1 159 ? 42.307  -7.267  20.525  1.00 47.97  ? 135 TRP B N   1 
ATOM   3327 C  CA  . TRP B 1 159 ? 41.759  -7.293  19.173  1.00 46.92  ? 135 TRP B CA  1 
ATOM   3328 C  C   . TRP B 1 159 ? 40.263  -7.008  19.177  1.00 46.44  ? 135 TRP B C   1 
ATOM   3329 O  O   . TRP B 1 159 ? 39.726  -6.506  18.185  1.00 45.94  ? 135 TRP B O   1 
ATOM   3330 C  CB  . TRP B 1 159 ? 42.056  -8.638  18.499  1.00 43.17  ? 135 TRP B CB  1 
ATOM   3331 C  CG  . TRP B 1 159 ? 41.217  -9.796  18.967  1.00 46.64  ? 135 TRP B CG  1 
ATOM   3332 C  CD1 . TRP B 1 159 ? 41.576  -10.756 19.868  1.00 46.52  ? 135 TRP B CD1 1 
ATOM   3333 C  CD2 . TRP B 1 159 ? 39.887  -10.125 18.540  1.00 44.96  ? 135 TRP B CD2 1 
ATOM   3334 N  NE1 . TRP B 1 159 ? 40.550  -11.657 20.035  1.00 47.34  ? 135 TRP B NE1 1 
ATOM   3335 C  CE2 . TRP B 1 159 ? 39.502  -11.291 19.232  1.00 45.17  ? 135 TRP B CE2 1 
ATOM   3336 C  CE3 . TRP B 1 159 ? 38.984  -9.543  17.645  1.00 44.67  ? 135 TRP B CE3 1 
ATOM   3337 C  CZ2 . TRP B 1 159 ? 38.256  -11.887 19.055  1.00 43.49  ? 135 TRP B CZ2 1 
ATOM   3338 C  CZ3 . TRP B 1 159 ? 37.745  -10.136 17.472  1.00 44.01  ? 135 TRP B CZ3 1 
ATOM   3339 C  CH2 . TRP B 1 159 ? 37.393  -11.295 18.173  1.00 42.37  ? 135 TRP B CH2 1 
ATOM   3340 N  N   . GLU B 1 160 ? 39.578  -7.312  20.281  1.00 47.19  ? 136 GLU B N   1 
ATOM   3341 C  CA  . GLU B 1 160 ? 38.159  -6.986  20.378  1.00 45.34  ? 136 GLU B CA  1 
ATOM   3342 C  C   . GLU B 1 160 ? 37.948  -5.480  20.472  1.00 50.00  ? 136 GLU B C   1 
ATOM   3343 O  O   . GLU B 1 160 ? 37.027  -4.936  19.850  1.00 47.45  ? 136 GLU B O   1 
ATOM   3344 C  CB  . GLU B 1 160 ? 37.541  -7.686  21.587  1.00 46.28  ? 136 GLU B CB  1 
ATOM   3345 C  CG  . GLU B 1 160 ? 37.405  -9.187  21.433  1.00 45.12  ? 136 GLU B CG  1 
ATOM   3346 C  CD  . GLU B 1 160 ? 36.876  -9.852  22.690  1.00 46.38  ? 136 GLU B CD  1 
ATOM   3347 O  OE1 . GLU B 1 160 ? 37.501  -9.684  23.757  1.00 47.03  ? 136 GLU B OE1 1 
ATOM   3348 O  OE2 . GLU B 1 160 ? 35.829  -10.530 22.617  1.00 46.18  ? 136 GLU B OE2 1 
ATOM   3349 N  N   . ARG B 1 161 ? 38.792  -4.790  21.241  1.00 47.47  ? 137 ARG B N   1 
ATOM   3350 C  CA  . ARG B 1 161 ? 38.651  -3.345  21.379  1.00 49.91  ? 137 ARG B CA  1 
ATOM   3351 C  C   . ARG B 1 161 ? 38.952  -2.630  20.067  1.00 48.88  ? 137 ARG B C   1 
ATOM   3352 O  O   . ARG B 1 161 ? 38.242  -1.689  19.691  1.00 50.33  ? 137 ARG B O   1 
ATOM   3353 C  CB  . ARG B 1 161 ? 39.568  -2.837  22.495  1.00 53.64  ? 137 ARG B CB  1 
ATOM   3354 C  CG  . ARG B 1 161 ? 39.280  -3.466  23.853  1.00 57.14  ? 137 ARG B CG  1 
ATOM   3355 C  CD  . ARG B 1 161 ? 40.168  -2.903  24.956  1.00 63.48  ? 137 ARG B CD  1 
ATOM   3356 N  NE  . ARG B 1 161 ? 40.185  -3.779  26.124  1.00 65.71  ? 137 ARG B NE  1 
ATOM   3357 C  CZ  . ARG B 1 161 ? 41.168  -4.615  26.435  1.00 64.91  ? 137 ARG B CZ  1 
ATOM   3358 N  NH1 . ARG B 1 161 ? 42.280  -4.680  25.719  1.00 63.62  ? 137 ARG B NH1 1 
ATOM   3359 N  NH2 . ARG B 1 161 ? 41.035  -5.406  27.497  1.00 62.51  ? 137 ARG B NH2 1 
ATOM   3360 N  N   . ASN B 1 162 ? 39.998  -3.058  19.355  1.00 47.00  ? 138 ASN B N   1 
ATOM   3361 C  CA  . ASN B 1 162 ? 40.312  -2.445  18.068  1.00 49.84  ? 138 ASN B CA  1 
ATOM   3362 C  C   . ASN B 1 162 ? 39.237  -2.753  17.033  1.00 49.17  ? 138 ASN B C   1 
ATOM   3363 O  O   . ASN B 1 162 ? 38.864  -1.884  16.237  1.00 48.32  ? 138 ASN B O   1 
ATOM   3364 C  CB  . ASN B 1 162 ? 41.670  -2.935  17.564  1.00 49.15  ? 138 ASN B CB  1 
ATOM   3365 C  CG  . ASN B 1 162 ? 42.795  -2.671  18.548  1.00 54.34  ? 138 ASN B CG  1 
ATOM   3366 O  OD1 . ASN B 1 162 ? 42.780  -1.686  19.288  1.00 51.89  ? 138 ASN B OD1 1 
ATOM   3367 N  ND2 . ASN B 1 162 ? 43.785  -3.555  18.553  1.00 49.95  ? 138 ASN B ND2 1 
ATOM   3368 N  N   . TYR B 1 163 ? 38.738  -3.990  17.029  1.00 46.71  ? 139 TYR B N   1 
ATOM   3369 C  CA  . TYR B 1 163 ? 37.740  -4.402  16.047  1.00 49.49  ? 139 TYR B CA  1 
ATOM   3370 C  C   . TYR B 1 163 ? 36.455  -3.600  16.206  1.00 50.77  ? 139 TYR B C   1 
ATOM   3371 O  O   . TYR B 1 163 ? 35.958  -2.998  15.247  1.00 52.85  ? 139 TYR B O   1 
ATOM   3372 C  CB  . TYR B 1 163 ? 37.478  -5.901  16.209  1.00 52.39  ? 139 TYR B CB  1 
ATOM   3373 C  CG  . TYR B 1 163 ? 36.616  -6.550  15.148  1.00 56.20  ? 139 TYR B CG  1 
ATOM   3374 C  CD1 . TYR B 1 163 ? 37.053  -6.656  13.834  1.00 63.81  ? 139 TYR B CD1 1 
ATOM   3375 C  CD2 . TYR B 1 163 ? 35.384  -7.103  15.474  1.00 53.72  ? 139 TYR B CD2 1 
ATOM   3376 C  CE1 . TYR B 1 163 ? 36.274  -7.267  12.868  1.00 61.49  ? 139 TYR B CE1 1 
ATOM   3377 C  CE2 . TYR B 1 163 ? 34.599  -7.716  14.517  1.00 61.30  ? 139 TYR B CE2 1 
ATOM   3378 C  CZ  . TYR B 1 163 ? 35.049  -7.797  13.216  1.00 62.31  ? 139 TYR B CZ  1 
ATOM   3379 O  OH  . TYR B 1 163 ? 34.266  -8.410  12.266  1.00 59.29  ? 139 TYR B OH  1 
ATOM   3380 N  N   . LEU B 1 164 ? 35.912  -3.566  17.424  1.00 52.84  ? 140 LEU B N   1 
ATOM   3381 C  CA  . LEU B 1 164 ? 34.623  -2.924  17.645  1.00 54.05  ? 140 LEU B CA  1 
ATOM   3382 C  C   . LEU B 1 164 ? 34.722  -1.405  17.571  1.00 56.24  ? 140 LEU B C   1 
ATOM   3383 O  O   . LEU B 1 164 ? 33.760  -0.746  17.165  1.00 58.42  ? 140 LEU B O   1 
ATOM   3384 C  CB  . LEU B 1 164 ? 34.058  -3.363  18.995  1.00 55.55  ? 140 LEU B CB  1 
ATOM   3385 C  CG  . LEU B 1 164 ? 33.886  -4.879  19.141  1.00 54.66  ? 140 LEU B CG  1 
ATOM   3386 C  CD1 . LEU B 1 164 ? 33.288  -5.233  20.493  1.00 53.20  ? 140 LEU B CD1 1 
ATOM   3387 C  CD2 . LEU B 1 164 ? 33.032  -5.442  18.012  1.00 54.88  ? 140 LEU B CD2 1 
ATOM   3388 N  N   . GLY B 1 165 ? 35.862  -0.834  17.945  1.00 53.57  ? 141 GLY B N   1 
ATOM   3389 C  CA  . GLY B 1 165 ? 36.033  0.601   17.872  1.00 52.82  ? 141 GLY B CA  1 
ATOM   3390 C  C   . GLY B 1 165 ? 36.368  1.141   16.502  1.00 49.71  ? 141 GLY B C   1 
ATOM   3391 O  O   . GLY B 1 165 ? 36.444  2.360   16.327  1.00 54.01  ? 141 GLY B O   1 
ATOM   3392 N  N   . ASN B 1 166 ? 36.560  0.268   15.517  1.00 49.22  ? 142 ASN B N   1 
ATOM   3393 C  CA  . ASN B 1 166 ? 36.999  0.684   14.189  1.00 48.18  ? 142 ASN B CA  1 
ATOM   3394 C  C   . ASN B 1 166 ? 35.825  1.298   13.434  1.00 48.94  ? 142 ASN B C   1 
ATOM   3395 O  O   . ASN B 1 166 ? 34.864  0.603   13.091  1.00 47.48  ? 142 ASN B O   1 
ATOM   3396 C  CB  . ASN B 1 166 ? 37.577  -0.511  13.436  1.00 45.08  ? 142 ASN B CB  1 
ATOM   3397 C  CG  . ASN B 1 166 ? 38.202  -0.122  12.112  1.00 45.50  ? 142 ASN B CG  1 
ATOM   3398 O  OD1 . ASN B 1 166 ? 38.169  1.041   11.711  1.00 44.03  ? 142 ASN B OD1 1 
ATOM   3399 N  ND2 . ASN B 1 166 ? 38.787  -1.099  11.428  1.00 42.09  ? 142 ASN B ND2 1 
ATOM   3400 N  N   . LYS B 1 167 ? 35.901  2.601   13.170  1.00 47.41  ? 143 LYS B N   1 
ATOM   3401 C  CA  . LYS B 1 167 ? 34.876  3.306   12.415  1.00 45.56  ? 143 LYS B CA  1 
ATOM   3402 C  C   . LYS B 1 167 ? 35.150  3.314   10.917  1.00 45.00  ? 143 LYS B C   1 
ATOM   3403 O  O   . LYS B 1 167 ? 34.461  4.026   10.179  1.00 41.02  ? 143 LYS B O   1 
ATOM   3404 C  CB  . LYS B 1 167 ? 34.751  4.747   12.912  1.00 47.50  ? 143 LYS B CB  1 
ATOM   3405 C  CG  . LYS B 1 167 ? 34.376  4.883   14.372  1.00 48.38  ? 143 LYS B CG  1 
ATOM   3406 C  CD  . LYS B 1 167 ? 34.246  6.349   14.743  1.00 55.91  ? 143 LYS B CD  1 
ATOM   3407 C  CE  . LYS B 1 167 ? 33.765  6.540   16.169  1.00 60.96  ? 143 LYS B CE  1 
ATOM   3408 N  NZ  . LYS B 1 167 ? 33.588  7.985   16.485  1.00 63.89  ? 143 LYS B NZ  1 
ATOM   3409 N  N   . ASP B 1 168 ? 36.132  2.540   10.451  1.00 43.04  ? 144 ASP B N   1 
ATOM   3410 C  CA  . ASP B 1 168 ? 36.557  2.562   9.056   1.00 41.24  ? 144 ASP B CA  1 
ATOM   3411 C  C   . ASP B 1 168 ? 36.495  1.178   8.414   1.00 40.19  ? 144 ASP B C   1 
ATOM   3412 O  O   . ASP B 1 168 ? 37.210  0.906   7.448   1.00 40.71  ? 144 ASP B O   1 
ATOM   3413 C  CB  . ASP B 1 168 ? 37.971  3.135   8.942   1.00 42.73  ? 144 ASP B CB  1 
ATOM   3414 C  CG  . ASP B 1 168 ? 38.054  4.582   9.394   1.00 47.94  ? 144 ASP B CG  1 
ATOM   3415 O  OD1 . ASP B 1 168 ? 37.243  5.406   8.919   1.00 46.55  ? 144 ASP B OD1 1 
ATOM   3416 O  OD2 . ASP B 1 168 ? 38.930  4.893   10.229  1.00 50.09  ? 144 ASP B OD2 1 
ATOM   3417 N  N   . ILE B 1 169 ? 35.645  0.289   8.931   1.00 41.40  ? 145 ILE B N   1 
ATOM   3418 C  CA  . ILE B 1 169 ? 35.524  -1.042  8.348   1.00 44.71  ? 145 ILE B CA  1 
ATOM   3419 C  C   . ILE B 1 169 ? 34.788  -0.952  7.018   1.00 45.32  ? 145 ILE B C   1 
ATOM   3420 O  O   . ILE B 1 169 ? 33.702  -0.364  6.926   1.00 40.38  ? 145 ILE B O   1 
ATOM   3421 C  CB  . ILE B 1 169 ? 34.803  -2.004  9.303   1.00 44.64  ? 145 ILE B CB  1 
ATOM   3422 C  CG1 . ILE B 1 169 ? 35.558  -2.129  10.627  1.00 45.76  ? 145 ILE B CG1 1 
ATOM   3423 C  CG2 . ILE B 1 169 ? 34.672  -3.373  8.645   1.00 46.95  ? 145 ILE B CG2 1 
ATOM   3424 C  CD1 . ILE B 1 169 ? 34.756  -2.810  11.717  1.00 48.61  ? 145 ILE B CD1 1 
ATOM   3425 N  N   . ILE B 1 170 ? 35.372  -1.550  5.985   1.00 45.27  ? 146 ILE B N   1 
ATOM   3426 C  CA  . ILE B 1 170 ? 34.782  -1.616  4.655   1.00 42.16  ? 146 ILE B CA  1 
ATOM   3427 C  C   . ILE B 1 170 ? 34.733  -3.084  4.260   1.00 44.97  ? 146 ILE B C   1 
ATOM   3428 O  O   . ILE B 1 170 ? 35.780  -3.719  4.084   1.00 47.98  ? 146 ILE B O   1 
ATOM   3429 C  CB  . ILE B 1 170 ? 35.577  -0.805  3.624   1.00 42.36  ? 146 ILE B CB  1 
ATOM   3430 C  CG1 . ILE B 1 170 ? 35.415  0.694   3.879   1.00 43.09  ? 146 ILE B CG1 1 
ATOM   3431 C  CG2 . ILE B 1 170 ? 35.133  -1.164  2.210   1.00 45.32  ? 146 ILE B CG2 1 
ATOM   3432 C  CD1 . ILE B 1 170 ? 36.407  1.540   3.111   1.00 43.73  ? 146 ILE B CD1 1 
ATOM   3433 N  N   . PHE B 1 171 ? 33.527  -3.624  4.125   1.00 44.26  ? 147 PHE B N   1 
ATOM   3434 C  CA  . PHE B 1 171 ? 33.338  -4.990  3.644   1.00 45.29  ? 147 PHE B CA  1 
ATOM   3435 C  C   . PHE B 1 171 ? 33.361  -4.947  2.121   1.00 41.26  ? 147 PHE B C   1 
ATOM   3436 O  O   . PHE B 1 171 ? 32.391  -4.531  1.486   1.00 40.51  ? 147 PHE B O   1 
ATOM   3437 C  CB  . PHE B 1 171 ? 32.033  -5.563  4.181   1.00 44.37  ? 147 PHE B CB  1 
ATOM   3438 C  CG  . PHE B 1 171 ? 31.826  -7.019  3.875   1.00 50.29  ? 147 PHE B CG  1 
ATOM   3439 C  CD1 . PHE B 1 171 ? 32.902  -7.876  3.695   1.00 49.39  ? 147 PHE B CD1 1 
ATOM   3440 C  CD2 . PHE B 1 171 ? 30.545  -7.532  3.768   1.00 49.58  ? 147 PHE B CD2 1 
ATOM   3441 C  CE1 . PHE B 1 171 ? 32.700  -9.213  3.419   1.00 48.40  ? 147 PHE B CE1 1 
ATOM   3442 C  CE2 . PHE B 1 171 ? 30.341  -8.864  3.489   1.00 49.56  ? 147 PHE B CE2 1 
ATOM   3443 C  CZ  . PHE B 1 171 ? 31.419  -9.706  3.317   1.00 48.90  ? 147 PHE B CZ  1 
ATOM   3444 N  N   . ARG B 1 172 ? 34.476  -5.372  1.531   1.00 39.93  ? 148 ARG B N   1 
ATOM   3445 C  CA  . ARG B 1 172 ? 34.717  -5.197  0.104   1.00 41.66  ? 148 ARG B CA  1 
ATOM   3446 C  C   . ARG B 1 172 ? 34.128  -6.354  -0.693  1.00 42.19  ? 148 ARG B C   1 
ATOM   3447 O  O   . ARG B 1 172 ? 34.434  -7.521  -0.426  1.00 41.73  ? 148 ARG B O   1 
ATOM   3448 C  CB  . ARG B 1 172 ? 36.216  -5.088  -0.179  1.00 42.45  ? 148 ARG B CB  1 
ATOM   3449 C  CG  . ARG B 1 172 ? 36.556  -4.939  -1.661  1.00 48.61  ? 148 ARG B CG  1 
ATOM   3450 C  CD  . ARG B 1 172 ? 38.015  -5.258  -1.951  1.00 49.20  ? 148 ARG B CD  1 
ATOM   3451 N  NE  . ARG B 1 172 ? 38.206  -5.609  -3.355  1.00 50.22  ? 148 ARG B NE  1 
ATOM   3452 C  CZ  . ARG B 1 172 ? 38.730  -4.812  -4.278  1.00 50.85  ? 148 ARG B CZ  1 
ATOM   3453 N  NH1 . ARG B 1 172 ? 39.210  -3.616  -3.975  1.00 53.71  ? 148 ARG B NH1 1 
ATOM   3454 N  NH2 . ARG B 1 172 ? 38.776  -5.229  -5.541  1.00 45.40  ? 148 ARG B NH2 1 
ATOM   3455 N  N   . ASN B 1 173 ? 33.299  -6.016  -1.691  1.00 39.88  ? 149 ASN B N   1 
ATOM   3456 C  CA  . ASN B 1 173 ? 32.717  -6.965  -2.638  1.00 37.37  ? 149 ASN B CA  1 
ATOM   3457 C  C   . ASN B 1 173 ? 32.408  -6.205  -3.933  1.00 38.18  ? 149 ASN B C   1 
ATOM   3458 O  O   . ASN B 1 173 ? 31.261  -5.897  -4.263  1.00 35.62  ? 149 ASN B O   1 
ATOM   3459 C  CB  . ASN B 1 173 ? 31.458  -7.635  -2.081  1.00 36.65  ? 149 ASN B CB  1 
ATOM   3460 C  CG  . ASN B 1 173 ? 31.705  -8.351  -0.772  1.00 40.83  ? 149 ASN B CG  1 
ATOM   3461 O  OD1 . ASN B 1 173 ? 32.215  -9.474  -0.748  1.00 37.20  ? 149 ASN B OD1 1 
ATOM   3462 N  ND2 . ASN B 1 173 ? 31.337  -7.707  0.332   1.00 37.75  ? 149 ASN B ND2 1 
ATOM   3463 N  N   . THR B 1 174 ? 33.454  -5.894  -4.694  1.00 35.78  ? 150 THR B N   1 
ATOM   3464 C  CA  . THR B 1 174 ? 33.279  -5.168  -5.941  1.00 33.53  ? 150 THR B CA  1 
ATOM   3465 C  C   . THR B 1 174 ? 32.597  -6.055  -6.981  1.00 35.71  ? 150 THR B C   1 
ATOM   3466 O  O   . THR B 1 174 ? 32.477  -7.272  -6.824  1.00 35.55  ? 150 THR B O   1 
ATOM   3467 C  CB  . THR B 1 174 ? 34.626  -4.684  -6.477  1.00 41.87  ? 150 THR B CB  1 
ATOM   3468 O  OG1 . THR B 1 174 ? 35.448  -5.812  -6.808  1.00 40.03  ? 150 THR B OG1 1 
ATOM   3469 C  CG2 . THR B 1 174 ? 35.338  -3.828  -5.445  1.00 37.86  ? 150 THR B CG2 1 
ATOM   3470 N  N   . PHE B 1 175 ? 32.143  -5.422  -8.065  1.00 35.00  ? 151 PHE B N   1 
ATOM   3471 C  CA  . PHE B 1 175 ? 31.598  -6.189  -9.180  1.00 38.33  ? 151 PHE B CA  1 
ATOM   3472 C  C   . PHE B 1 175 ? 32.622  -7.189  -9.703  1.00 37.66  ? 151 PHE B C   1 
ATOM   3473 O  O   . PHE B 1 175 ? 32.276  -8.330  -10.030 1.00 36.75  ? 151 PHE B O   1 
ATOM   3474 C  CB  . PHE B 1 175 ? 31.143  -5.247  -10.295 1.00 39.96  ? 151 PHE B CB  1 
ATOM   3475 C  CG  . PHE B 1 175 ? 29.976  -4.381  -9.914  1.00 40.33  ? 151 PHE B CG  1 
ATOM   3476 C  CD1 . PHE B 1 175 ? 28.718  -4.934  -9.739  1.00 40.91  ? 151 PHE B CD1 1 
ATOM   3477 C  CD2 . PHE B 1 175 ? 30.134  -3.018  -9.732  1.00 41.22  ? 151 PHE B CD2 1 
ATOM   3478 C  CE1 . PHE B 1 175 ? 27.640  -4.143  -9.386  1.00 40.48  ? 151 PHE B CE1 1 
ATOM   3479 C  CE2 . PHE B 1 175 ? 29.060  -2.222  -9.380  1.00 40.23  ? 151 PHE B CE2 1 
ATOM   3480 C  CZ  . PHE B 1 175 ? 27.812  -2.787  -9.207  1.00 38.61  ? 151 PHE B CZ  1 
ATOM   3481 N  N   . GLY B 1 176 ? 33.892  -6.782  -9.777  1.00 38.40  ? 152 GLY B N   1 
ATOM   3482 C  CA  . GLY B 1 176 ? 34.929  -7.701  -10.217 1.00 39.60  ? 152 GLY B CA  1 
ATOM   3483 C  C   . GLY B 1 176 ? 35.171  -8.824  -9.227  1.00 38.16  ? 152 GLY B C   1 
ATOM   3484 O  O   . GLY B 1 176 ? 35.369  -9.977  -9.620  1.00 41.71  ? 152 GLY B O   1 
ATOM   3485 N  N   . ASP B 1 177 ? 35.163  -8.505  -7.930  1.00 34.89  ? 153 ASP B N   1 
ATOM   3486 C  CA  . ASP B 1 177 ? 35.307  -9.538  -6.909  1.00 40.85  ? 153 ASP B CA  1 
ATOM   3487 C  C   . ASP B 1 177 ? 34.206  -10.585 -7.029  1.00 39.92  ? 153 ASP B C   1 
ATOM   3488 O  O   . ASP B 1 177 ? 34.476  -11.791 -7.066  1.00 39.29  ? 153 ASP B O   1 
ATOM   3489 C  CB  . ASP B 1 177 ? 35.280  -8.910  -5.514  1.00 43.59  ? 153 ASP B CB  1 
ATOM   3490 C  CG  . ASP B 1 177 ? 36.479  -8.025  -5.241  1.00 46.87  ? 153 ASP B CG  1 
ATOM   3491 O  OD1 . ASP B 1 177 ? 37.521  -8.197  -5.911  1.00 46.09  ? 153 ASP B OD1 1 
ATOM   3492 O  OD2 . ASP B 1 177 ? 36.378  -7.170  -4.333  1.00 45.49  ? 153 ASP B OD2 1 
ATOM   3493 N  N   . VAL B 1 178 ? 32.950  -10.138 -7.079  1.00 37.67  ? 154 VAL B N   1 
ATOM   3494 C  CA  . VAL B 1 178 ? 31.826  -11.069 -7.115  1.00 38.05  ? 154 VAL B CA  1 
ATOM   3495 C  C   . VAL B 1 178 ? 31.883  -11.928 -8.370  1.00 38.99  ? 154 VAL B C   1 
ATOM   3496 O  O   . VAL B 1 178 ? 31.656  -13.143 -8.320  1.00 36.40  ? 154 VAL B O   1 
ATOM   3497 C  CB  . VAL B 1 178 ? 30.497  -10.299 -7.017  1.00 38.01  ? 154 VAL B CB  1 
ATOM   3498 C  CG1 . VAL B 1 178 ? 29.323  -11.222 -7.303  1.00 37.14  ? 154 VAL B CG1 1 
ATOM   3499 C  CG2 . VAL B 1 178 ? 30.364  -9.665  -5.647  1.00 35.01  ? 154 VAL B CG2 1 
ATOM   3500 N  N   . GLU B 1 179 ? 32.170  -11.310 -9.516  1.00 37.99  ? 155 GLU B N   1 
ATOM   3501 C  CA  . GLU B 1 179 ? 32.296  -12.071 -10.753 1.00 42.31  ? 155 GLU B CA  1 
ATOM   3502 C  C   . GLU B 1 179 ? 33.367  -13.148 -10.624 1.00 44.22  ? 155 GLU B C   1 
ATOM   3503 O  O   . GLU B 1 179 ? 33.213  -14.257 -11.149 1.00 45.70  ? 155 GLU B O   1 
ATOM   3504 C  CB  . GLU B 1 179 ? 32.610  -11.118 -11.906 1.00 44.89  ? 155 GLU B CB  1 
ATOM   3505 C  CG  . GLU B 1 179 ? 32.737  -11.777 -13.268 1.00 51.81  ? 155 GLU B CG  1 
ATOM   3506 C  CD  . GLU B 1 179 ? 32.729  -10.767 -14.400 1.00 59.72  ? 155 GLU B CD  1 
ATOM   3507 O  OE1 . GLU B 1 179 ? 32.417  -9.585  -14.143 1.00 61.60  ? 155 GLU B OE1 1 
ATOM   3508 O  OE2 . GLU B 1 179 ? 33.032  -11.154 -15.548 1.00 66.43  ? 155 GLU B OE2 1 
ATOM   3509 N  N   . HIS B 1 180 ? 34.454  -12.843 -9.913  1.00 43.64  ? 156 HIS B N   1 
ATOM   3510 C  CA  . HIS B 1 180 ? 35.516  -13.823 -9.715  1.00 43.77  ? 156 HIS B CA  1 
ATOM   3511 C  C   . HIS B 1 180 ? 35.038  -15.002 -8.873  1.00 45.54  ? 156 HIS B C   1 
ATOM   3512 O  O   . HIS B 1 180 ? 35.352  -16.158 -9.183  1.00 46.25  ? 156 HIS B O   1 
ATOM   3513 C  CB  . HIS B 1 180 ? 36.722  -13.145 -9.063  1.00 43.22  ? 156 HIS B CB  1 
ATOM   3514 C  CG  . HIS B 1 180 ? 37.827  -14.087 -8.699  1.00 49.36  ? 156 HIS B CG  1 
ATOM   3515 N  ND1 . HIS B 1 180 ? 38.657  -14.663 -9.637  1.00 49.07  ? 156 HIS B ND1 1 
ATOM   3516 C  CD2 . HIS B 1 180 ? 38.245  -14.547 -7.495  1.00 52.63  ? 156 HIS B CD2 1 
ATOM   3517 C  CE1 . HIS B 1 180 ? 39.535  -15.439 -9.027  1.00 47.87  ? 156 HIS B CE1 1 
ATOM   3518 N  NE2 . HIS B 1 180 ? 39.307  -15.386 -7.728  1.00 52.10  ? 156 HIS B NE2 1 
ATOM   3519 N  N   . VAL B 1 181 ? 34.280  -14.735 -7.806  1.00 42.20  ? 157 VAL B N   1 
ATOM   3520 C  CA  . VAL B 1 181 ? 33.809  -15.816 -6.940  1.00 42.53  ? 157 VAL B CA  1 
ATOM   3521 C  C   . VAL B 1 181 ? 32.866  -16.738 -7.704  1.00 44.72  ? 157 VAL B C   1 
ATOM   3522 O  O   . VAL B 1 181 ? 32.992  -17.967 -7.652  1.00 45.13  ? 157 VAL B O   1 
ATOM   3523 C  CB  . VAL B 1 181 ? 33.129  -15.244 -5.683  1.00 41.33  ? 157 VAL B CB  1 
ATOM   3524 C  CG1 . VAL B 1 181 ? 32.633  -16.378 -4.795  1.00 41.64  ? 157 VAL B CG1 1 
ATOM   3525 C  CG2 . VAL B 1 181 ? 34.082  -14.336 -4.923  1.00 38.96  ? 157 VAL B CG2 1 
ATOM   3526 N  N   . MET B 1 182 ? 31.896  -16.156 -8.414  1.00 42.25  ? 158 MET B N   1 
ATOM   3527 C  CA  . MET B 1 182 ? 30.939  -16.958 -9.171  1.00 42.78  ? 158 MET B CA  1 
ATOM   3528 C  C   . MET B 1 182 ? 31.650  -17.909 -10.125 1.00 46.81  ? 158 MET B C   1 
ATOM   3529 O  O   . MET B 1 182 ? 31.310  -19.095 -10.210 1.00 49.90  ? 158 MET B O   1 
ATOM   3530 C  CB  . MET B 1 182 ? 29.989  -16.041 -9.943  1.00 42.08  ? 158 MET B CB  1 
ATOM   3531 C  CG  . MET B 1 182 ? 29.018  -15.261 -9.073  1.00 41.30  ? 158 MET B CG  1 
ATOM   3532 S  SD  . MET B 1 182 ? 28.232  -13.926 -9.996  1.00 41.92  ? 158 MET B SD  1 
ATOM   3533 C  CE  . MET B 1 182 ? 26.994  -13.379 -8.821  1.00 35.17  ? 158 MET B CE  1 
ATOM   3534 N  N   . THR B 1 183 ? 32.640  -17.400 -10.860 1.00 45.25  ? 159 THR B N   1 
ATOM   3535 C  CA  . THR B 1 183 ? 33.374  -18.238 -11.802 1.00 47.28  ? 159 THR B CA  1 
ATOM   3536 C  C   . THR B 1 183 ? 34.172  -19.311 -11.073 1.00 47.65  ? 159 THR B C   1 
ATOM   3537 O  O   . THR B 1 183 ? 34.037  -20.506 -11.361 1.00 50.30  ? 159 THR B O   1 
ATOM   3538 C  CB  . THR B 1 183 ? 34.306  -17.373 -12.652 1.00 50.81  ? 159 THR B CB  1 
ATOM   3539 O  OG1 . THR B 1 183 ? 33.536  -16.454 -13.436 1.00 53.53  ? 159 THR B OG1 1 
ATOM   3540 C  CG2 . THR B 1 183 ? 35.154  -18.241 -13.572 1.00 55.10  ? 159 THR B CG2 1 
ATOM   3541 N  N   . THR B 1 184 ? 35.008  -18.898 -10.121 1.00 47.14  ? 160 THR B N   1 
ATOM   3542 C  CA  . THR B 1 184 ? 35.915  -19.833 -9.465  1.00 47.56  ? 160 THR B CA  1 
ATOM   3543 C  C   . THR B 1 184 ? 35.147  -20.909 -8.706  1.00 46.70  ? 160 THR B C   1 
ATOM   3544 O  O   . THR B 1 184 ? 35.416  -22.105 -8.859  1.00 48.28  ? 160 THR B O   1 
ATOM   3545 C  CB  . THR B 1 184 ? 36.849  -19.071 -8.524  1.00 46.92  ? 160 THR B CB  1 
ATOM   3546 O  OG1 . THR B 1 184 ? 37.550  -18.060 -9.259  1.00 48.61  ? 160 THR B OG1 1 
ATOM   3547 C  CG2 . THR B 1 184 ? 37.856  -20.013 -7.882  1.00 50.27  ? 160 THR B CG2 1 
ATOM   3548 N  N   . LEU B 1 185 ? 34.182  -20.503 -7.880  1.00 46.66  ? 161 LEU B N   1 
ATOM   3549 C  CA  . LEU B 1 185 ? 33.483  -21.469 -7.041  1.00 45.91  ? 161 LEU B CA  1 
ATOM   3550 C  C   . LEU B 1 185 ? 32.408  -22.228 -7.807  1.00 45.68  ? 161 LEU B C   1 
ATOM   3551 O  O   . LEU B 1 185 ? 32.106  -23.376 -7.462  1.00 45.67  ? 161 LEU B O   1 
ATOM   3552 C  CB  . LEU B 1 185 ? 32.873  -20.766 -5.829  1.00 42.31  ? 161 LEU B CB  1 
ATOM   3553 C  CG  . LEU B 1 185 ? 33.891  -20.111 -4.892  1.00 44.82  ? 161 LEU B CG  1 
ATOM   3554 C  CD1 . LEU B 1 185 ? 33.217  -19.590 -3.634  1.00 39.38  ? 161 LEU B CD1 1 
ATOM   3555 C  CD2 . LEU B 1 185 ? 35.007  -21.086 -4.538  1.00 43.78  ? 161 LEU B CD2 1 
ATOM   3556 N  N   . GLY B 1 186 ? 31.822  -21.619 -8.838  1.00 44.84  ? 162 GLY B N   1 
ATOM   3557 C  CA  . GLY B 1 186 ? 30.874  -22.348 -9.661  1.00 47.44  ? 162 GLY B CA  1 
ATOM   3558 C  C   . GLY B 1 186 ? 31.477  -23.591 -10.285 1.00 52.49  ? 162 GLY B C   1 
ATOM   3559 O  O   . GLY B 1 186 ? 30.776  -24.583 -10.507 1.00 49.68  ? 162 GLY B O   1 
ATOM   3560 N  N   . ALA B 1 187 ? 32.783  -23.561 -10.565 1.00 52.92  ? 163 ALA B N   1 
ATOM   3561 C  CA  . ALA B 1 187 ? 33.444  -24.692 -11.204 1.00 55.46  ? 163 ALA B CA  1 
ATOM   3562 C  C   . ALA B 1 187 ? 33.557  -25.898 -10.282 1.00 54.10  ? 163 ALA B C   1 
ATOM   3563 O  O   . ALA B 1 187 ? 33.794  -27.010 -10.766 1.00 56.43  ? 163 ALA B O   1 
ATOM   3564 C  CB  . ALA B 1 187 ? 34.836  -24.280 -11.687 1.00 51.61  ? 163 ALA B CB  1 
ATOM   3565 N  N   . GLY B 1 188 ? 33.407  -25.708 -8.976  1.00 50.49  ? 164 GLY B N   1 
ATOM   3566 C  CA  . GLY B 1 188 ? 33.399  -26.801 -8.031  1.00 49.68  ? 164 GLY B CA  1 
ATOM   3567 C  C   . GLY B 1 188 ? 32.031  -27.388 -7.767  1.00 46.51  ? 164 GLY B C   1 
ATOM   3568 O  O   . GLY B 1 188 ? 31.890  -28.225 -6.870  1.00 43.28  ? 164 GLY B O   1 
ATOM   3569 N  N   . GLY B 1 189 ? 31.018  -26.985 -8.532  1.00 44.09  ? 165 GLY B N   1 
ATOM   3570 C  CA  . GLY B 1 189 ? 29.655  -27.393 -8.274  1.00 42.17  ? 165 GLY B CA  1 
ATOM   3571 C  C   . GLY B 1 189 ? 28.983  -26.651 -7.142  1.00 42.18  ? 165 GLY B C   1 
ATOM   3572 O  O   . GLY B 1 189 ? 27.837  -26.975 -6.804  1.00 41.23  ? 165 GLY B O   1 
ATOM   3573 N  N   . THR B 1 190 ? 29.653  -25.665 -6.551  1.00 42.03  ? 166 THR B N   1 
ATOM   3574 C  CA  . THR B 1 190 ? 29.101  -24.920 -5.429  1.00 38.37  ? 166 THR B CA  1 
ATOM   3575 C  C   . THR B 1 190 ? 28.076  -23.902 -5.914  1.00 38.34  ? 166 THR B C   1 
ATOM   3576 O  O   . THR B 1 190 ? 28.351  -23.115 -6.825  1.00 39.13  ? 166 THR B O   1 
ATOM   3577 C  CB  . THR B 1 190 ? 30.220  -24.206 -4.670  1.00 39.21  ? 166 THR B CB  1 
ATOM   3578 O  OG1 . THR B 1 190 ? 31.172  -25.166 -4.195  1.00 40.00  ? 166 THR B OG1 1 
ATOM   3579 C  CG2 . THR B 1 190 ? 29.658  -23.419 -3.492  1.00 34.28  ? 166 THR B CG2 1 
ATOM   3580 N  N   . ARG B 1 191 ? 26.896  -23.924 -5.308  1.00 35.99  ? 167 ARG B N   1 
ATOM   3581 C  CA  . ARG B 1 191 ? 25.900  -22.878 -5.482  1.00 35.42  ? 167 ARG B CA  1 
ATOM   3582 C  C   . ARG B 1 191 ? 25.980  -21.915 -4.302  1.00 35.61  ? 167 ARG B C   1 
ATOM   3583 O  O   . ARG B 1 191 ? 26.622  -22.191 -3.285  1.00 36.66  ? 167 ARG B O   1 
ATOM   3584 C  CB  . ARG B 1 191 ? 24.503  -23.490 -5.634  1.00 35.69  ? 167 ARG B CB  1 
ATOM   3585 C  CG  . ARG B 1 191 ? 24.364  -24.326 -6.912  1.00 37.02  ? 167 ARG B CG  1 
ATOM   3586 C  CD  . ARG B 1 191 ? 22.961  -24.874 -7.106  1.00 40.65  ? 167 ARG B CD  1 
ATOM   3587 N  NE  . ARG B 1 191 ? 21.977  -23.817 -7.307  1.00 44.82  ? 167 ARG B NE  1 
ATOM   3588 C  CZ  . ARG B 1 191 ? 21.856  -23.109 -8.422  1.00 44.20  ? 167 ARG B CZ  1 
ATOM   3589 N  NH1 . ARG B 1 191 ? 22.665  -23.295 -9.451  1.00 48.31  ? 167 ARG B NH1 1 
ATOM   3590 N  NH2 . ARG B 1 191 ? 20.901  -22.187 -8.504  1.00 46.59  ? 167 ARG B NH2 1 
ATOM   3591 N  N   . PHE B 1 192 ? 25.345  -20.758 -4.451  1.00 32.86  ? 168 PHE B N   1 
ATOM   3592 C  CA  . PHE B 1 192 ? 25.583  -19.655 -3.536  1.00 34.59  ? 168 PHE B CA  1 
ATOM   3593 C  C   . PHE B 1 192 ? 24.332  -19.272 -2.762  1.00 35.07  ? 168 PHE B C   1 
ATOM   3594 O  O   . PHE B 1 192 ? 23.201  -19.436 -3.230  1.00 35.62  ? 168 PHE B O   1 
ATOM   3595 C  CB  . PHE B 1 192 ? 26.107  -18.420 -4.277  1.00 35.46  ? 168 PHE B CB  1 
ATOM   3596 C  CG  . PHE B 1 192 ? 27.357  -18.678 -5.062  1.00 35.73  ? 168 PHE B CG  1 
ATOM   3597 C  CD1 . PHE B 1 192 ? 28.556  -18.934 -4.416  1.00 36.51  ? 168 PHE B CD1 1 
ATOM   3598 C  CD2 . PHE B 1 192 ? 27.334  -18.668 -6.445  1.00 37.12  ? 168 PHE B CD2 1 
ATOM   3599 C  CE1 . PHE B 1 192 ? 29.710  -19.175 -5.138  1.00 38.54  ? 168 PHE B CE1 1 
ATOM   3600 C  CE2 . PHE B 1 192 ? 28.482  -18.908 -7.171  1.00 39.43  ? 168 PHE B CE2 1 
ATOM   3601 C  CZ  . PHE B 1 192 ? 29.672  -19.162 -6.517  1.00 40.02  ? 168 PHE B CZ  1 
ATOM   3602 N  N   . GLU B 1 193 ? 24.569  -18.777 -1.554  1.00 32.68  ? 169 GLU B N   1 
ATOM   3603 C  CA  . GLU B 1 193 ? 23.585  -18.029 -0.781  1.00 33.26  ? 169 GLU B CA  1 
ATOM   3604 C  C   . GLU B 1 193 ? 23.946  -16.558 -0.956  1.00 34.49  ? 169 GLU B C   1 
ATOM   3605 O  O   . GLU B 1 193 ? 24.920  -16.073 -0.372  1.00 37.13  ? 169 GLU B O   1 
ATOM   3606 C  CB  . GLU B 1 193 ? 23.604  -18.455 0.682   1.00 35.22  ? 169 GLU B CB  1 
ATOM   3607 C  CG  . GLU B 1 193 ? 22.734  -17.611 1.594   1.00 35.86  ? 169 GLU B CG  1 
ATOM   3608 C  CD  . GLU B 1 193 ? 22.915  -17.966 3.058   1.00 43.01  ? 169 GLU B CD  1 
ATOM   3609 O  OE1 . GLU B 1 193 ? 24.069  -17.953 3.540   1.00 45.62  ? 169 GLU B OE1 1 
ATOM   3610 O  OE2 . GLU B 1 193 ? 21.906  -18.271 3.726   1.00 48.90  ? 169 GLU B OE2 1 
ATOM   3611 N  N   . PHE B 1 194 ? 23.177  -15.853 -1.780  1.00 31.17  ? 170 PHE B N   1 
ATOM   3612 C  CA  . PHE B 1 194 ? 23.475  -14.462 -2.104  1.00 32.94  ? 170 PHE B CA  1 
ATOM   3613 C  C   . PHE B 1 194 ? 23.041  -13.575 -0.943  1.00 33.72  ? 170 PHE B C   1 
ATOM   3614 O  O   . PHE B 1 194 ? 21.846  -13.435 -0.668  1.00 34.19  ? 170 PHE B O   1 
ATOM   3615 C  CB  . PHE B 1 194 ? 22.784  -14.059 -3.403  1.00 32.26  ? 170 PHE B CB  1 
ATOM   3616 C  CG  . PHE B 1 194 ? 23.101  -14.964 -4.562  1.00 32.30  ? 170 PHE B CG  1 
ATOM   3617 C  CD1 . PHE B 1 194 ? 24.262  -14.792 -5.296  1.00 32.60  ? 170 PHE B CD1 1 
ATOM   3618 C  CD2 . PHE B 1 194 ? 22.238  -15.987 -4.915  1.00 32.08  ? 170 PHE B CD2 1 
ATOM   3619 C  CE1 . PHE B 1 194 ? 24.556  -15.624 -6.362  1.00 33.69  ? 170 PHE B CE1 1 
ATOM   3620 C  CE2 . PHE B 1 194 ? 22.526  -16.821 -5.979  1.00 33.01  ? 170 PHE B CE2 1 
ATOM   3621 C  CZ  . PHE B 1 194 ? 23.686  -16.639 -6.703  1.00 34.83  ? 170 PHE B CZ  1 
ATOM   3622 N  N   . GLU B 1 195 ? 24.016  -12.978 -0.263  1.00 33.51  ? 171 GLU B N   1 
ATOM   3623 C  CA  . GLU B 1 195 ? 23.764  -12.142 0.903   1.00 32.12  ? 171 GLU B CA  1 
ATOM   3624 C  C   . GLU B 1 195 ? 23.497  -10.718 0.440   1.00 30.48  ? 171 GLU B C   1 
ATOM   3625 O  O   . GLU B 1 195 ? 24.377  -10.073 -0.138  1.00 30.31  ? 171 GLU B O   1 
ATOM   3626 C  CB  . GLU B 1 195 ? 24.953  -12.176 1.860   1.00 34.35  ? 171 GLU B CB  1 
ATOM   3627 C  CG  . GLU B 1 195 ? 25.572  -13.551 2.027   1.00 37.37  ? 171 GLU B CG  1 
ATOM   3628 C  CD  . GLU B 1 195 ? 24.674  -14.503 2.793   1.00 41.89  ? 171 GLU B CD  1 
ATOM   3629 O  OE1 . GLU B 1 195 ? 23.543  -14.103 3.144   1.00 44.63  ? 171 GLU B OE1 1 
ATOM   3630 O  OE2 . GLU B 1 195 ? 25.101  -15.651 3.045   1.00 44.27  ? 171 GLU B OE2 1 
ATOM   3631 N  N   . CYS B 1 196 ? 22.289  -10.227 0.700   1.00 28.67  ? 172 CYS B N   1 
ATOM   3632 C  CA  . CYS B 1 196 ? 21.849  -8.923  0.218   1.00 28.52  ? 172 CYS B CA  1 
ATOM   3633 C  C   . CYS B 1 196 ? 21.453  -8.074  1.418   1.00 29.50  ? 172 CYS B C   1 
ATOM   3634 O  O   . CYS B 1 196 ? 20.471  -8.375  2.105   1.00 28.22  ? 172 CYS B O   1 
ATOM   3635 C  CB  . CYS B 1 196 ? 20.699  -9.080  -0.775  1.00 29.01  ? 172 CYS B CB  1 
ATOM   3636 S  SG  . CYS B 1 196 ? 21.184  -9.952  -2.296  1.00 29.46  ? 172 CYS B SG  1 
ATOM   3637 N  N   . TYR B 1 197 ? 22.226  -7.016  1.667   1.00 28.69  ? 173 TYR B N   1 
ATOM   3638 C  CA  . TYR B 1 197 ? 22.060  -6.164  2.836   1.00 30.51  ? 173 TYR B CA  1 
ATOM   3639 C  C   . TYR B 1 197 ? 21.268  -4.895  2.549   1.00 27.77  ? 173 TYR B C   1 
ATOM   3640 O  O   . TYR B 1 197 ? 20.988  -4.139  3.486   1.00 28.51  ? 173 TYR B O   1 
ATOM   3641 C  CB  . TYR B 1 197 ? 23.436  -5.780  3.402   1.00 29.84  ? 173 TYR B CB  1 
ATOM   3642 C  CG  . TYR B 1 197 ? 24.296  -6.961  3.797   1.00 32.51  ? 173 TYR B CG  1 
ATOM   3643 C  CD1 . TYR B 1 197 ? 24.917  -7.745  2.835   1.00 31.25  ? 173 TYR B CD1 1 
ATOM   3644 C  CD2 . TYR B 1 197 ? 24.490  -7.286  5.132   1.00 33.78  ? 173 TYR B CD2 1 
ATOM   3645 C  CE1 . TYR B 1 197 ? 25.699  -8.824  3.190   1.00 34.96  ? 173 TYR B CE1 1 
ATOM   3646 C  CE2 . TYR B 1 197 ? 25.273  -8.361  5.497   1.00 34.65  ? 173 TYR B CE2 1 
ATOM   3647 C  CZ  . TYR B 1 197 ? 25.877  -9.127  4.522   1.00 38.23  ? 173 TYR B CZ  1 
ATOM   3648 O  OH  . TYR B 1 197 ? 26.658  -10.201 4.881   1.00 40.20  ? 173 TYR B OH  1 
ATOM   3649 N  N   . ASP B 1 198 ? 20.913  -4.637  1.295   1.00 25.61  ? 174 ASP B N   1 
ATOM   3650 C  CA  . ASP B 1 198 ? 20.131  -3.459  0.932   1.00 27.29  ? 174 ASP B CA  1 
ATOM   3651 C  C   . ASP B 1 198 ? 19.663  -3.635  -0.508  1.00 28.74  ? 174 ASP B C   1 
ATOM   3652 O  O   . ASP B 1 198 ? 20.021  -4.605  -1.184  1.00 30.42  ? 174 ASP B O   1 
ATOM   3653 C  CB  . ASP B 1 198 ? 20.936  -2.170  1.109   1.00 26.95  ? 174 ASP B CB  1 
ATOM   3654 C  CG  . ASP B 1 198 ? 20.050  -0.949  1.292   1.00 30.38  ? 174 ASP B CG  1 
ATOM   3655 O  OD1 . ASP B 1 198 ? 18.815  -1.083  1.164   1.00 32.95  ? 174 ASP B OD1 1 
ATOM   3656 O  OD2 . ASP B 1 198 ? 20.587  0.146   1.564   1.00 30.96  ? 174 ASP B OD2 1 
ATOM   3657 N  N   . THR B 1 199 ? 18.855  -2.679  -0.973  1.00 27.01  ? 175 THR B N   1 
ATOM   3658 C  CA  . THR B 1 199 ? 18.252  -2.787  -2.297  1.00 27.49  ? 175 THR B CA  1 
ATOM   3659 C  C   . THR B 1 199 ? 19.311  -2.906  -3.383  1.00 26.87  ? 175 THR B C   1 
ATOM   3660 O  O   . THR B 1 199 ? 19.144  -3.665  -4.345  1.00 27.95  ? 175 THR B O   1 
ATOM   3661 C  CB  . THR B 1 199 ? 17.365  -1.570  -2.561  1.00 30.11  ? 175 THR B CB  1 
ATOM   3662 O  OG1 . THR B 1 199 ? 16.821  -1.094  -1.323  1.00 27.62  ? 175 THR B OG1 1 
ATOM   3663 C  CG2 . THR B 1 199 ? 16.225  -1.933  -3.510  1.00 29.92  ? 175 THR B CG2 1 
ATOM   3664 N  N   . SER B 1 200 ? 20.408  -2.159  -3.248  1.00 28.68  ? 176 SER B N   1 
ATOM   3665 C  CA  . SER B 1 200 ? 21.432  -2.157  -4.285  1.00 29.88  ? 176 SER B CA  1 
ATOM   3666 C  C   . SER B 1 200 ? 22.008  -3.548  -4.511  1.00 27.07  ? 176 SER B C   1 
ATOM   3667 O  O   . SER B 1 200 ? 22.429  -3.869  -5.628  1.00 28.32  ? 176 SER B O   1 
ATOM   3668 C  CB  . SER B 1 200 ? 22.545  -1.177  -3.913  1.00 30.70  ? 176 SER B CB  1 
ATOM   3669 O  OG  . SER B 1 200 ? 23.177  -1.564  -2.703  1.00 32.95  ? 176 SER B OG  1 
ATOM   3670 N  N   . HIS B 1 201 ? 22.037  -4.386  -3.472  1.00 27.68  ? 177 HIS B N   1 
ATOM   3671 C  CA  . HIS B 1 201 ? 22.603  -5.721  -3.632  1.00 28.23  ? 177 HIS B CA  1 
ATOM   3672 C  C   . HIS B 1 201 ? 21.694  -6.614  -4.466  1.00 29.18  ? 177 HIS B C   1 
ATOM   3673 O  O   . HIS B 1 201 ? 22.184  -7.472  -5.209  1.00 31.36  ? 177 HIS B O   1 
ATOM   3674 C  CB  . HIS B 1 201 ? 22.872  -6.344  -2.262  1.00 28.27  ? 177 HIS B CB  1 
ATOM   3675 C  CG  . HIS B 1 201 ? 23.890  -5.599  -1.452  1.00 31.62  ? 177 HIS B CG  1 
ATOM   3676 N  ND1 . HIS B 1 201 ? 24.427  -6.102  -0.287  1.00 32.57  ? 177 HIS B ND1 1 
ATOM   3677 C  CD2 . HIS B 1 201 ? 24.470  -4.391  -1.642  1.00 31.54  ? 177 HIS B CD2 1 
ATOM   3678 C  CE1 . HIS B 1 201 ? 25.288  -5.232  0.210   1.00 33.90  ? 177 HIS B CE1 1 
ATOM   3679 N  NE2 . HIS B 1 201 ? 25.334  -4.186  -0.595  1.00 35.25  ? 177 HIS B NE2 1 
ATOM   3680 N  N   . LEU B 1 202 ? 20.376  -6.425  -4.369  1.00 29.55  ? 178 LEU B N   1 
ATOM   3681 C  CA  . LEU B 1 202 ? 19.470  -7.144  -5.259  1.00 29.95  ? 178 LEU B CA  1 
ATOM   3682 C  C   . LEU B 1 202 ? 19.656  -6.696  -6.703  1.00 28.30  ? 178 LEU B C   1 
ATOM   3683 O  O   . LEU B 1 202 ? 19.639  -7.522  -7.622  1.00 29.48  ? 178 LEU B O   1 
ATOM   3684 C  CB  . LEU B 1 202 ? 18.023  -6.937  -4.817  1.00 26.56  ? 178 LEU B CB  1 
ATOM   3685 C  CG  . LEU B 1 202 ? 17.631  -7.533  -3.464  1.00 27.36  ? 178 LEU B CG  1 
ATOM   3686 C  CD1 . LEU B 1 202 ? 16.187  -7.185  -3.142  1.00 27.61  ? 178 LEU B CD1 1 
ATOM   3687 C  CD2 . LEU B 1 202 ? 17.833  -9.040  -3.446  1.00 27.37  ? 178 LEU B CD2 1 
ATOM   3688 N  N   . TYR B 1 203 ? 19.831  -5.391  -6.923  1.00 27.19  ? 179 TYR B N   1 
ATOM   3689 C  CA  . TYR B 1 203 ? 20.102  -4.905  -8.272  1.00 27.02  ? 179 TYR B CA  1 
ATOM   3690 C  C   . TYR B 1 203 ? 21.456  -5.394  -8.772  1.00 31.40  ? 179 TYR B C   1 
ATOM   3691 O  O   . TYR B 1 203 ? 21.597  -5.751  -9.948  1.00 31.47  ? 179 TYR B O   1 
ATOM   3692 C  CB  . TYR B 1 203 ? 20.037  -3.380  -8.306  1.00 27.65  ? 179 TYR B CB  1 
ATOM   3693 C  CG  . TYR B 1 203 ? 18.634  -2.831  -8.398  1.00 30.43  ? 179 TYR B CG  1 
ATOM   3694 C  CD1 . TYR B 1 203 ? 17.993  -2.715  -9.625  1.00 31.47  ? 179 TYR B CD1 1 
ATOM   3695 C  CD2 . TYR B 1 203 ? 17.951  -2.425  -7.262  1.00 30.90  ? 179 TYR B CD2 1 
ATOM   3696 C  CE1 . TYR B 1 203 ? 16.710  -2.212  -9.718  1.00 33.49  ? 179 TYR B CE1 1 
ATOM   3697 C  CE2 . TYR B 1 203 ? 16.667  -1.918  -7.343  1.00 32.81  ? 179 TYR B CE2 1 
ATOM   3698 C  CZ  . TYR B 1 203 ? 16.052  -1.817  -8.572  1.00 34.02  ? 179 TYR B CZ  1 
ATOM   3699 O  OH  . TYR B 1 203 ? 14.778  -1.312  -8.657  1.00 32.73  ? 179 TYR B OH  1 
ATOM   3700 N  N   . ASN B 1 204 ? 22.465  -5.411  -7.898  1.00 29.87  ? 180 ASN B N   1 
ATOM   3701 C  CA  . ASN B 1 204 ? 23.753  -5.982  -8.282  1.00 32.04  ? 180 ASN B CA  1 
ATOM   3702 C  C   . ASN B 1 204 ? 23.593  -7.433  -8.717  1.00 33.04  ? 180 ASN B C   1 
ATOM   3703 O  O   . ASN B 1 204 ? 24.183  -7.857  -9.717  1.00 33.79  ? 180 ASN B O   1 
ATOM   3704 C  CB  . ASN B 1 204 ? 24.751  -5.881  -7.126  1.00 30.08  ? 180 ASN B CB  1 
ATOM   3705 C  CG  . ASN B 1 204 ? 25.094  -4.446  -6.770  1.00 33.33  ? 180 ASN B CG  1 
ATOM   3706 O  OD1 . ASN B 1 204 ? 24.832  -3.522  -7.540  1.00 30.88  ? 180 ASN B OD1 1 
ATOM   3707 N  ND2 . ASN B 1 204 ? 25.693  -4.255  -5.600  1.00 32.60  ? 180 ASN B ND2 1 
ATOM   3708 N  N   . LEU B 1 205 ? 22.790  -8.208  -7.980  1.00 31.09  ? 181 LEU B N   1 
ATOM   3709 C  CA  . LEU B 1 205 ? 22.572  -9.605  -8.345  1.00 32.04  ? 181 LEU B CA  1 
ATOM   3710 C  C   . LEU B 1 205 ? 21.831  -9.716  -9.671  1.00 33.44  ? 181 LEU B C   1 
ATOM   3711 O  O   . LEU B 1 205 ? 22.105  -10.620 -10.469 1.00 34.01  ? 181 LEU B O   1 
ATOM   3712 C  CB  . LEU B 1 205 ? 21.799  -10.318 -7.235  1.00 30.46  ? 181 LEU B CB  1 
ATOM   3713 C  CG  . LEU B 1 205 ? 21.477  -11.798 -7.459  1.00 30.91  ? 181 LEU B CG  1 
ATOM   3714 C  CD1 . LEU B 1 205 ? 22.742  -12.607 -7.730  1.00 31.97  ? 181 LEU B CD1 1 
ATOM   3715 C  CD2 . LEU B 1 205 ? 20.732  -12.359 -6.259  1.00 29.86  ? 181 LEU B CD2 1 
ATOM   3716 N  N   . LYS B 1 206 ? 20.891  -8.802  -9.921  1.00 31.78  ? 182 LYS B N   1 
ATOM   3717 C  CA  . LYS B 1 206 ? 20.157  -8.808  -11.182 1.00 33.69  ? 182 LYS B CA  1 
ATOM   3718 C  C   . LYS B 1 206 ? 21.097  -8.615  -12.366 1.00 36.40  ? 182 LYS B C   1 
ATOM   3719 O  O   . LYS B 1 206 ? 20.885  -9.192  -13.440 1.00 36.50  ? 182 LYS B O   1 
ATOM   3720 C  CB  . LYS B 1 206 ? 19.086  -7.717  -11.147 1.00 34.10  ? 182 LYS B CB  1 
ATOM   3721 C  CG  . LYS B 1 206 ? 18.248  -7.581  -12.407 1.00 35.79  ? 182 LYS B CG  1 
ATOM   3722 C  CD  . LYS B 1 206 ? 17.421  -8.823  -12.678 1.00 38.31  ? 182 LYS B CD  1 
ATOM   3723 C  CE  . LYS B 1 206 ? 16.417  -8.573  -13.792 1.00 41.09  ? 182 LYS B CE  1 
ATOM   3724 N  NZ  . LYS B 1 206 ? 15.681  -9.809  -14.174 1.00 42.10  ? 182 LYS B NZ  1 
ATOM   3725 N  N   . HIS B 1 207 ? 22.144  -7.810  -12.188 1.00 34.64  ? 183 HIS B N   1 
ATOM   3726 C  CA  . HIS B 1 207 ? 23.114  -7.599  -13.258 1.00 37.41  ? 183 HIS B CA  1 
ATOM   3727 C  C   . HIS B 1 207 ? 23.798  -8.906  -13.649 1.00 39.43  ? 183 HIS B C   1 
ATOM   3728 O  O   . HIS B 1 207 ? 23.934  -9.218  -14.837 1.00 41.26  ? 183 HIS B O   1 
ATOM   3729 C  CB  . HIS B 1 207 ? 24.140  -6.555  -12.817 1.00 38.52  ? 183 HIS B CB  1 
ATOM   3730 C  CG  . HIS B 1 207 ? 25.388  -6.540  -13.641 1.00 41.52  ? 183 HIS B CG  1 
ATOM   3731 N  ND1 . HIS B 1 207 ? 25.451  -5.959  -14.889 1.00 43.11  ? 183 HIS B ND1 1 
ATOM   3732 C  CD2 . HIS B 1 207 ? 26.626  -7.026  -13.389 1.00 40.76  ? 183 HIS B CD2 1 
ATOM   3733 C  CE1 . HIS B 1 207 ? 26.673  -6.093  -15.373 1.00 44.19  ? 183 HIS B CE1 1 
ATOM   3734 N  NE2 . HIS B 1 207 ? 27.405  -6.736  -14.482 1.00 44.81  ? 183 HIS B NE2 1 
ATOM   3735 N  N   . PHE B 1 208 ? 24.230  -9.689  -12.657 1.00 35.90  ? 184 PHE B N   1 
ATOM   3736 C  CA  . PHE B 1 208 ? 24.903  -10.950 -12.954 1.00 41.07  ? 184 PHE B CA  1 
ATOM   3737 C  C   . PHE B 1 208 ? 23.919  -11.998 -13.456 1.00 41.43  ? 184 PHE B C   1 
ATOM   3738 O  O   . PHE B 1 208 ? 24.246  -12.791 -14.347 1.00 46.02  ? 184 PHE B O   1 
ATOM   3739 C  CB  . PHE B 1 208 ? 25.633  -11.456 -11.711 1.00 38.86  ? 184 PHE B CB  1 
ATOM   3740 C  CG  . PHE B 1 208 ? 26.794  -10.601 -11.308 1.00 40.02  ? 184 PHE B CG  1 
ATOM   3741 C  CD1 . PHE B 1 208 ? 27.914  -10.516 -12.116 1.00 41.14  ? 184 PHE B CD1 1 
ATOM   3742 C  CD2 . PHE B 1 208 ? 26.769  -9.884  -10.125 1.00 38.79  ? 184 PHE B CD2 1 
ATOM   3743 C  CE1 . PHE B 1 208 ? 28.987  -9.731  -11.756 1.00 41.97  ? 184 PHE B CE1 1 
ATOM   3744 C  CE2 . PHE B 1 208 ? 27.843  -9.097  -9.756  1.00 38.11  ? 184 PHE B CE2 1 
ATOM   3745 C  CZ  . PHE B 1 208 ? 28.954  -9.021  -10.574 1.00 39.80  ? 184 PHE B CZ  1 
ATOM   3746 N  N   . TYR B 1 209 ? 22.714  -12.021 -12.888 1.00 40.00  ? 185 TYR B N   1 
ATOM   3747 C  CA  . TYR B 1 209 ? 21.691  -12.960 -13.334 1.00 42.19  ? 185 TYR B CA  1 
ATOM   3748 C  C   . TYR B 1 209 ? 21.376  -12.767 -14.812 1.00 44.17  ? 185 TYR B C   1 
ATOM   3749 O  O   . TYR B 1 209 ? 21.270  -13.742 -15.566 1.00 44.72  ? 185 TYR B O   1 
ATOM   3750 C  CB  . TYR B 1 209 ? 20.441  -12.774 -12.473 1.00 40.86  ? 185 TYR B CB  1 
ATOM   3751 C  CG  . TYR B 1 209 ? 19.266  -13.656 -12.814 1.00 41.80  ? 185 TYR B CG  1 
ATOM   3752 C  CD1 . TYR B 1 209 ? 19.341  -15.035 -12.676 1.00 41.22  ? 185 TYR B CD1 1 
ATOM   3753 C  CD2 . TYR B 1 209 ? 18.065  -13.103 -13.235 1.00 39.02  ? 185 TYR B CD2 1 
ATOM   3754 C  CE1 . TYR B 1 209 ? 18.257  -15.839 -12.970 1.00 44.24  ? 185 TYR B CE1 1 
ATOM   3755 C  CE2 . TYR B 1 209 ? 16.978  -13.897 -13.529 1.00 42.54  ? 185 TYR B CE2 1 
ATOM   3756 C  CZ  . TYR B 1 209 ? 17.077  -15.263 -13.395 1.00 43.76  ? 185 TYR B CZ  1 
ATOM   3757 O  OH  . TYR B 1 209 ? 15.989  -16.052 -13.689 1.00 47.69  ? 185 TYR B OH  1 
ATOM   3758 N  N   . ASP B 1 210 ? 21.239  -11.513 -15.250 1.00 43.00  ? 186 ASP B N   1 
ATOM   3759 C  CA  . ASP B 1 210 ? 20.920  -11.247 -16.649 1.00 45.51  ? 186 ASP B CA  1 
ATOM   3760 C  C   . ASP B 1 210 ? 22.063  -11.643 -17.574 1.00 47.88  ? 186 ASP B C   1 
ATOM   3761 O  O   . ASP B 1 210 ? 21.819  -12.065 -18.710 1.00 53.29  ? 186 ASP B O   1 
ATOM   3762 C  CB  . ASP B 1 210 ? 20.573  -9.770  -16.833 1.00 42.97  ? 186 ASP B CB  1 
ATOM   3763 C  CG  . ASP B 1 210 ? 19.219  -9.415  -16.250 1.00 45.43  ? 186 ASP B CG  1 
ATOM   3764 O  OD1 . ASP B 1 210 ? 18.454  -10.343 -15.912 1.00 47.11  ? 186 ASP B OD1 1 
ATOM   3765 O  OD2 . ASP B 1 210 ? 18.919  -8.208  -16.127 1.00 49.24  ? 186 ASP B OD2 1 
ATOM   3766 N  N   . ARG B 1 211 ? 23.308  -11.511 -17.118 1.00 48.28  ? 187 ARG B N   1 
ATOM   3767 C  CA  . ARG B 1 211 ? 24.451  -11.948 -17.907 1.00 49.65  ? 187 ARG B CA  1 
ATOM   3768 C  C   . ARG B 1 211 ? 24.618  -13.462 -17.917 1.00 50.02  ? 187 ARG B C   1 
ATOM   3769 O  O   . ARG B 1 211 ? 25.470  -13.968 -18.654 1.00 52.81  ? 187 ARG B O   1 
ATOM   3770 C  CB  . ARG B 1 211 ? 25.733  -11.296 -17.382 1.00 49.14  ? 187 ARG B CB  1 
ATOM   3771 C  CG  . ARG B 1 211 ? 25.840  -9.811  -17.687 1.00 49.98  ? 187 ARG B CG  1 
ATOM   3772 C  CD  . ARG B 1 211 ? 27.046  -9.186  -17.000 1.00 54.99  ? 187 ARG B CD  1 
ATOM   3773 N  NE  . ARG B 1 211 ? 28.292  -9.857  -17.353 1.00 64.10  ? 187 ARG B NE  1 
ATOM   3774 C  CZ  . ARG B 1 211 ? 29.461  -9.623  -16.770 1.00 62.01  ? 187 ARG B CZ  1 
ATOM   3775 N  NH1 . ARG B 1 211 ? 29.583  -8.740  -15.793 1.00 57.48  ? 187 ARG B NH1 1 
ATOM   3776 N  NH2 . ARG B 1 211 ? 30.534  -10.296 -17.176 1.00 63.90  ? 187 ARG B NH2 1 
ATOM   3777 N  N   . GLY B 1 212 ? 23.836  -14.191 -17.123 1.00 51.17  ? 188 GLY B N   1 
ATOM   3778 C  CA  . GLY B 1 212 ? 23.926  -15.637 -17.097 1.00 48.86  ? 188 GLY B CA  1 
ATOM   3779 C  C   . GLY B 1 212 ? 25.056  -16.189 -16.263 1.00 51.68  ? 188 GLY B C   1 
ATOM   3780 O  O   . GLY B 1 212 ? 25.388  -17.371 -16.399 1.00 51.49  ? 188 GLY B O   1 
ATOM   3781 N  N   . LEU B 1 213 ? 25.661  -15.372 -15.398 1.00 48.61  ? 189 LEU B N   1 
ATOM   3782 C  CA  . LEU B 1 213 ? 26.763  -15.841 -14.569 1.00 48.09  ? 189 LEU B CA  1 
ATOM   3783 C  C   . LEU B 1 213 ? 26.289  -16.668 -13.381 1.00 48.65  ? 189 LEU B C   1 
ATOM   3784 O  O   . LEU B 1 213 ? 27.100  -17.374 -12.772 1.00 49.15  ? 189 LEU B O   1 
ATOM   3785 C  CB  . LEU B 1 213 ? 27.593  -14.647 -14.091 1.00 47.83  ? 189 LEU B CB  1 
ATOM   3786 C  CG  . LEU B 1 213 ? 28.295  -13.888 -15.224 1.00 54.09  ? 189 LEU B CG  1 
ATOM   3787 C  CD1 . LEU B 1 213 ? 28.852  -12.562 -14.735 1.00 58.74  ? 189 LEU B CD1 1 
ATOM   3788 C  CD2 . LEU B 1 213 ? 29.402  -14.736 -15.841 1.00 53.52  ? 189 LEU B CD2 1 
ATOM   3789 N  N   . VAL B 1 214 ? 25.005  -16.598 -13.040 1.00 47.64  ? 190 VAL B N   1 
ATOM   3790 C  CA  . VAL B 1 214 ? 24.399  -17.488 -12.057 1.00 47.39  ? 190 VAL B CA  1 
ATOM   3791 C  C   . VAL B 1 214 ? 23.035  -17.909 -12.582 1.00 48.25  ? 190 VAL B C   1 
ATOM   3792 O  O   . VAL B 1 214 ? 22.279  -17.085 -13.108 1.00 49.21  ? 190 VAL B O   1 
ATOM   3793 C  CB  . VAL B 1 214 ? 24.271  -16.829 -10.667 1.00 44.14  ? 190 VAL B CB  1 
ATOM   3794 C  CG1 . VAL B 1 214 ? 25.626  -16.774 -9.981  1.00 41.81  ? 190 VAL B CG1 1 
ATOM   3795 C  CG2 . VAL B 1 214 ? 23.663  -15.435 -10.780 1.00 42.35  ? 190 VAL B CG2 1 
ATOM   3796 N  N   . LYS B 1 215 ? 22.728  -19.195 -12.450 1.00 47.38  ? 191 LYS B N   1 
ATOM   3797 C  CA  . LYS B 1 215 ? 21.462  -19.751 -12.899 1.00 46.19  ? 191 LYS B CA  1 
ATOM   3798 C  C   . LYS B 1 215 ? 20.554  -20.008 -11.706 1.00 45.16  ? 191 LYS B C   1 
ATOM   3799 O  O   . LYS B 1 215 ? 21.014  -20.346 -10.613 1.00 44.88  ? 191 LYS B O   1 
ATOM   3800 C  CB  . LYS B 1 215 ? 21.674  -21.055 -13.672 1.00 47.83  ? 191 LYS B CB  1 
ATOM   3801 C  CG  . LYS B 1 215 ? 22.451  -20.896 -14.970 1.00 55.01  ? 191 LYS B CG  1 
ATOM   3802 C  CD  . LYS B 1 215 ? 21.669  -20.098 -16.003 1.00 59.44  ? 191 LYS B CD  1 
ATOM   3803 C  CE  . LYS B 1 215 ? 22.388  -20.073 -17.342 1.00 63.50  ? 191 LYS B CE  1 
ATOM   3804 N  NZ  . LYS B 1 215 ? 23.762  -19.507 -17.230 1.00 65.34  ? 191 LYS B NZ  1 
ATOM   3805 N  N   . GLY B 1 216 ? 19.253  -19.841 -11.929 1.00 44.90  ? 192 GLY B N   1 
ATOM   3806 C  CA  . GLY B 1 216 ? 18.273  -20.080 -10.899 1.00 42.64  ? 192 GLY B CA  1 
ATOM   3807 C  C   . GLY B 1 216 ? 18.186  -21.550 -10.545 1.00 41.89  ? 192 GLY B C   1 
ATOM   3808 O  O   . GLY B 1 216 ? 18.716  -22.411 -11.252 1.00 43.25  ? 192 GLY B O   1 
ATOM   3809 N  N   . PRO B 1 217 ? 17.512  -21.873 -9.431  1.00 41.74  ? 193 PRO B N   1 
ATOM   3810 C  CA  . PRO B 1 217 ? 16.869  -20.925 -8.512  1.00 40.85  ? 193 PRO B CA  1 
ATOM   3811 C  C   . PRO B 1 217 ? 17.874  -20.224 -7.604  1.00 38.63  ? 193 PRO B C   1 
ATOM   3812 O  O   . PRO B 1 217 ? 18.763  -20.879 -7.059  1.00 40.88  ? 193 PRO B O   1 
ATOM   3813 C  CB  . PRO B 1 217 ? 15.926  -21.815 -7.701  1.00 38.34  ? 193 PRO B CB  1 
ATOM   3814 C  CG  . PRO B 1 217 ? 16.599  -23.141 -7.684  1.00 39.58  ? 193 PRO B CG  1 
ATOM   3815 C  CD  . PRO B 1 217 ? 17.322  -23.270 -9.000  1.00 39.03  ? 193 PRO B CD  1 
ATOM   3816 N  N   . LEU B 1 218 ? 17.733  -18.910 -7.446  1.00 37.71  ? 194 LEU B N   1 
ATOM   3817 C  CA  . LEU B 1 218 ? 18.674  -18.125 -6.657  1.00 36.78  ? 194 LEU B CA  1 
ATOM   3818 C  C   . LEU B 1 218 ? 18.290  -18.175 -5.185  1.00 34.87  ? 194 LEU B C   1 
ATOM   3819 O  O   . LEU B 1 218 ? 17.149  -17.873 -4.822  1.00 35.34  ? 194 LEU B O   1 
ATOM   3820 C  CB  . LEU B 1 218 ? 18.701  -16.673 -7.139  1.00 36.19  ? 194 LEU B CB  1 
ATOM   3821 C  CG  . LEU B 1 218 ? 18.995  -16.448 -8.621  1.00 35.29  ? 194 LEU B CG  1 
ATOM   3822 C  CD1 . LEU B 1 218 ? 18.942  -14.963 -8.953  1.00 36.49  ? 194 LEU B CD1 1 
ATOM   3823 C  CD2 . LEU B 1 218 ? 20.344  -17.035 -8.999  1.00 38.58  ? 194 LEU B CD2 1 
ATOM   3824 N  N   . PHE B 1 219 ? 19.246  -18.553 -4.338  1.00 31.87  ? 195 PHE B N   1 
ATOM   3825 C  CA  . PHE B 1 219 ? 19.054  -18.547 -2.888  1.00 32.81  ? 195 PHE B CA  1 
ATOM   3826 C  C   . PHE B 1 219 ? 19.446  -17.161 -2.391  1.00 33.33  ? 195 PHE B C   1 
ATOM   3827 O  O   . PHE B 1 219 ? 20.612  -16.886 -2.108  1.00 33.10  ? 195 PHE B O   1 
ATOM   3828 C  CB  . PHE B 1 219 ? 19.882  -19.648 -2.234  1.00 32.33  ? 195 PHE B CB  1 
ATOM   3829 C  CG  . PHE B 1 219 ? 19.532  -19.916 -0.788  1.00 34.06  ? 195 PHE B CG  1 
ATOM   3830 C  CD1 . PHE B 1 219 ? 18.261  -19.658 -0.292  1.00 35.33  ? 195 PHE B CD1 1 
ATOM   3831 C  CD2 . PHE B 1 219 ? 20.485  -20.437 0.076   1.00 33.80  ? 195 PHE B CD2 1 
ATOM   3832 C  CE1 . PHE B 1 219 ? 17.952  -19.913 1.031   1.00 37.28  ? 195 PHE B CE1 1 
ATOM   3833 C  CE2 . PHE B 1 219 ? 20.177  -20.690 1.400   1.00 38.68  ? 195 PHE B CE2 1 
ATOM   3834 C  CZ  . PHE B 1 219 ? 18.911  -20.427 1.876   1.00 37.43  ? 195 PHE B CZ  1 
ATOM   3835 N  N   . ILE B 1 220 ? 18.458  -16.274 -2.292  1.00 31.39  ? 196 ILE B N   1 
ATOM   3836 C  CA  . ILE B 1 220 ? 18.679  -14.875 -1.938  1.00 32.42  ? 196 ILE B CA  1 
ATOM   3837 C  C   . ILE B 1 220 ? 18.373  -14.696 -0.457  1.00 33.54  ? 196 ILE B C   1 
ATOM   3838 O  O   . ILE B 1 220 ? 17.248  -14.948 -0.009  1.00 31.86  ? 196 ILE B O   1 
ATOM   3839 C  CB  . ILE B 1 220 ? 17.814  -13.935 -2.795  1.00 32.33  ? 196 ILE B CB  1 
ATOM   3840 C  CG1 . ILE B 1 220 ? 18.103  -14.161 -4.281  1.00 27.46  ? 196 ILE B CG1 1 
ATOM   3841 C  CG2 . ILE B 1 220 ? 18.070  -12.477 -2.416  1.00 28.39  ? 196 ILE B CG2 1 
ATOM   3842 C  CD1 . ILE B 1 220 ? 17.401  -13.187 -5.206  1.00 31.72  ? 196 ILE B CD1 1 
ATOM   3843 N  N   . GLN B 1 221 ? 19.371  -14.249 0.300   1.00 31.53  ? 197 GLN B N   1 
ATOM   3844 C  CA  . GLN B 1 221 ? 19.227  -13.984 1.725   1.00 30.49  ? 197 GLN B CA  1 
ATOM   3845 C  C   . GLN B 1 221 ? 19.279  -12.480 1.955   1.00 32.39  ? 197 GLN B C   1 
ATOM   3846 O  O   . GLN B 1 221 ? 20.315  -11.847 1.717   1.00 32.96  ? 197 GLN B O   1 
ATOM   3847 C  CB  . GLN B 1 221 ? 20.321  -14.686 2.524   1.00 34.42  ? 197 GLN B CB  1 
ATOM   3848 C  CG  . GLN B 1 221 ? 20.246  -14.407 4.009   1.00 35.24  ? 197 GLN B CG  1 
ATOM   3849 C  CD  . GLN B 1 221 ? 20.264  -15.673 4.825   1.00 37.07  ? 197 GLN B CD  1 
ATOM   3850 O  OE1 . GLN B 1 221 ? 19.214  -16.234 5.148   1.00 35.88  ? 197 GLN B OE1 1 
ATOM   3851 N  NE2 . GLN B 1 221 ? 21.461  -16.143 5.154   1.00 43.49  ? 197 GLN B NE2 1 
ATOM   3852 N  N   . THR B 1 222 ? 18.169  -11.915 2.422   1.00 29.77  ? 198 THR B N   1 
ATOM   3853 C  CA  . THR B 1 222 ? 18.074  -10.488 2.705   1.00 29.51  ? 198 THR B CA  1 
ATOM   3854 C  C   . THR B 1 222 ? 18.367  -10.261 4.185   1.00 27.73  ? 198 THR B C   1 
ATOM   3855 O  O   . THR B 1 222 ? 17.678  -10.815 5.049   1.00 27.94  ? 198 THR B O   1 
ATOM   3856 C  CB  . THR B 1 222 ? 16.695  -9.952  2.320   1.00 27.39  ? 198 THR B CB  1 
ATOM   3857 O  OG1 . THR B 1 222 ? 15.670  -10.687 3.000   1.00 26.34  ? 198 THR B OG1 1 
ATOM   3858 C  CG2 . THR B 1 222 ? 16.484  -10.084 0.821   1.00 25.72  ? 198 THR B CG2 1 
ATOM   3859 N  N   . VAL B 1 223 ? 19.387  -9.448  4.470   1.00 24.92  ? 199 VAL B N   1 
ATOM   3860 C  CA  . VAL B 1 223 ? 19.926  -9.264  5.816   1.00 26.52  ? 199 VAL B CA  1 
ATOM   3861 C  C   . VAL B 1 223 ? 19.475  -7.909  6.348   1.00 27.73  ? 199 VAL B C   1 
ATOM   3862 O  O   . VAL B 1 223 ? 19.750  -6.870  5.736   1.00 27.40  ? 199 VAL B O   1 
ATOM   3863 C  CB  . VAL B 1 223 ? 21.460  -9.362  5.822   1.00 30.80  ? 199 VAL B CB  1 
ATOM   3864 C  CG1 . VAL B 1 223 ? 22.001  -9.178  7.235   1.00 28.33  ? 199 VAL B CG1 1 
ATOM   3865 C  CG2 . VAL B 1 223 ? 21.914  -10.692 5.226   1.00 29.51  ? 199 VAL B CG2 1 
ATOM   3866 N  N   . PHE B 1 224 ? 18.823  -7.918  7.512   1.00 28.21  ? 200 PHE B N   1 
ATOM   3867 C  CA  . PHE B 1 224 ? 18.223  -6.730  8.102   1.00 26.99  ? 200 PHE B CA  1 
ATOM   3868 C  C   . PHE B 1 224 ? 18.857  -6.410  9.449   1.00 30.34  ? 200 PHE B C   1 
ATOM   3869 O  O   . PHE B 1 224 ? 19.159  -7.313  10.236  1.00 30.56  ? 200 PHE B O   1 
ATOM   3870 C  CB  . PHE B 1 224 ? 16.715  -6.914  8.308   1.00 27.94  ? 200 PHE B CB  1 
ATOM   3871 C  CG  . PHE B 1 224 ? 15.973  -7.311  7.070   1.00 28.27  ? 200 PHE B CG  1 
ATOM   3872 C  CD1 . PHE B 1 224 ? 15.572  -6.357  6.153   1.00 25.70  ? 200 PHE B CD1 1 
ATOM   3873 C  CD2 . PHE B 1 224 ? 15.667  -8.639  6.827   1.00 27.45  ? 200 PHE B CD2 1 
ATOM   3874 C  CE1 . PHE B 1 224 ? 14.890  -6.719  5.012   1.00 26.87  ? 200 PHE B CE1 1 
ATOM   3875 C  CE2 . PHE B 1 224 ? 14.981  -9.008  5.690   1.00 27.09  ? 200 PHE B CE2 1 
ATOM   3876 C  CZ  . PHE B 1 224 ? 14.592  -8.048  4.780   1.00 25.21  ? 200 PHE B CZ  1 
ATOM   3877 N  N   . GLY B 1 225 ? 19.043  -5.118  9.716   1.00 30.33  ? 201 GLY B N   1 
ATOM   3878 C  CA  . GLY B 1 225 ? 19.388  -4.648  11.042  1.00 29.94  ? 201 GLY B CA  1 
ATOM   3879 C  C   . GLY B 1 225 ? 20.844  -4.307  11.281  1.00 32.53  ? 201 GLY B C   1 
ATOM   3880 O  O   . GLY B 1 225 ? 21.175  -3.862  12.385  1.00 32.79  ? 201 GLY B O   1 
ATOM   3881 N  N   . LEU B 1 226 ? 21.722  -4.494  10.297  1.00 32.42  ? 202 LEU B N   1 
ATOM   3882 C  CA  . LEU B 1 226 ? 23.137  -4.196  10.489  1.00 33.61  ? 202 LEU B CA  1 
ATOM   3883 C  C   . LEU B 1 226 ? 23.424  -2.722  10.246  1.00 32.38  ? 202 LEU B C   1 
ATOM   3884 O  O   . LEU B 1 226 ? 22.878  -2.110  9.323   1.00 32.61  ? 202 LEU B O   1 
ATOM   3885 C  CB  . LEU B 1 226 ? 24.004  -5.033  9.549   1.00 34.02  ? 202 LEU B CB  1 
ATOM   3886 C  CG  . LEU B 1 226 ? 23.877  -6.551  9.642   1.00 38.80  ? 202 LEU B CG  1 
ATOM   3887 C  CD1 . LEU B 1 226 ? 25.002  -7.210  8.868   1.00 45.63  ? 202 LEU B CD1 1 
ATOM   3888 C  CD2 . LEU B 1 226 ? 23.886  -7.002  11.081  1.00 40.84  ? 202 LEU B CD2 1 
ATOM   3889 N  N   . MET B 1 227 ? 24.298  -2.157  11.074  1.00 33.05  ? 203 MET B N   1 
ATOM   3890 C  CA  . MET B 1 227 ? 24.787  -0.805  10.841  1.00 34.86  ? 203 MET B CA  1 
ATOM   3891 C  C   . MET B 1 227 ? 25.661  -0.804  9.594   1.00 36.77  ? 203 MET B C   1 
ATOM   3892 O  O   . MET B 1 227 ? 26.706  -1.463  9.558   1.00 36.39  ? 203 MET B O   1 
ATOM   3893 C  CB  . MET B 1 227 ? 25.571  -0.305  12.049  1.00 35.23  ? 203 MET B CB  1 
ATOM   3894 C  CG  . MET B 1 227 ? 25.823  1.192   12.029  1.00 42.14  ? 203 MET B CG  1 
ATOM   3895 S  SD  . MET B 1 227 ? 27.015  1.715   13.273  1.00 53.87  ? 203 MET B SD  1 
ATOM   3896 C  CE  . MET B 1 227 ? 27.070  3.476   12.959  1.00 48.50  ? 203 MET B CE  1 
ATOM   3897 N  N   . GLY B 1 228 ? 25.235  -0.065  8.574   1.00 34.61  ? 204 GLY B N   1 
ATOM   3898 C  CA  . GLY B 1 228 ? 25.820  -0.125  7.254   1.00 32.70  ? 204 GLY B CA  1 
ATOM   3899 C  C   . GLY B 1 228 ? 24.926  -0.788  6.231   1.00 33.55  ? 204 GLY B C   1 
ATOM   3900 O  O   . GLY B 1 228 ? 25.181  -0.661  5.027   1.00 31.93  ? 204 GLY B O   1 
ATOM   3901 N  N   . GLY B 1 229 ? 23.892  -1.497  6.680   1.00 28.92  ? 205 GLY B N   1 
ATOM   3902 C  CA  . GLY B 1 229 ? 22.917  -2.085  5.787   1.00 29.68  ? 205 GLY B CA  1 
ATOM   3903 C  C   . GLY B 1 229 ? 21.533  -1.506  6.004   1.00 31.74  ? 205 GLY B C   1 
ATOM   3904 O  O   . GLY B 1 229 ? 21.369  -0.515  6.724   1.00 27.38  ? 205 GLY B O   1 
ATOM   3905 N  N   . ILE B 1 230 ? 20.529  -2.116  5.376   1.00 26.95  ? 206 ILE B N   1 
ATOM   3906 C  CA  . ILE B 1 230 ? 19.151  -1.696  5.586   1.00 27.63  ? 206 ILE B CA  1 
ATOM   3907 C  C   . ILE B 1 230 ? 18.722  -2.060  7.003   1.00 29.85  ? 206 ILE B C   1 
ATOM   3908 O  O   . ILE B 1 230 ? 19.268  -2.980  7.629   1.00 29.05  ? 206 ILE B O   1 
ATOM   3909 C  CB  . ILE B 1 230 ? 18.237  -2.351  4.535   1.00 29.48  ? 206 ILE B CB  1 
ATOM   3910 C  CG1 . ILE B 1 230 ? 16.874  -1.652  4.484   1.00 29.61  ? 206 ILE B CG1 1 
ATOM   3911 C  CG2 . ILE B 1 230 ? 18.063  -3.836  4.841   1.00 23.76  ? 206 ILE B CG2 1 
ATOM   3912 C  CD1 . ILE B 1 230 ? 15.976  -2.179  3.384   1.00 28.06  ? 206 ILE B CD1 1 
ATOM   3913 N  N   . GLY B 1 231 ? 17.740  -1.327  7.522   1.00 28.45  ? 207 GLY B N   1 
ATOM   3914 C  CA  . GLY B 1 231 ? 17.216  -1.574  8.848   1.00 27.42  ? 207 GLY B CA  1 
ATOM   3915 C  C   . GLY B 1 231 ? 16.295  -2.781  8.890   1.00 29.65  ? 207 GLY B C   1 
ATOM   3916 O  O   . GLY B 1 231 ? 16.185  -3.562  7.943   1.00 27.37  ? 207 GLY B O   1 
ATOM   3917 N  N   . ALA B 1 232 ? 15.610  -2.920  10.028  1.00 29.08  ? 208 ALA B N   1 
ATOM   3918 C  CA  . ALA B 1 232 ? 14.763  -4.077  10.299  1.00 30.67  ? 208 ALA B CA  1 
ATOM   3919 C  C   . ALA B 1 232 ? 13.290  -3.700  10.453  1.00 30.60  ? 208 ALA B C   1 
ATOM   3920 O  O   . ALA B 1 232 ? 12.506  -4.484  10.997  1.00 28.47  ? 208 ALA B O   1 
ATOM   3921 C  CB  . ALA B 1 232 ? 15.258  -4.806  11.550  1.00 26.75  ? 208 ALA B CB  1 
ATOM   3922 N  N   . HIS B 1 233 ? 12.897  -2.519  9.986   1.00 30.77  ? 209 HIS B N   1 
ATOM   3923 C  CA  . HIS B 1 233 ? 11.493  -2.137  10.008  1.00 28.98  ? 209 HIS B CA  1 
ATOM   3924 C  C   . HIS B 1 233 ? 10.692  -3.040  9.067   1.00 29.82  ? 209 HIS B C   1 
ATOM   3925 O  O   . HIS B 1 233 ? 11.208  -3.486  8.039   1.00 28.62  ? 209 HIS B O   1 
ATOM   3926 C  CB  . HIS B 1 233 ? 11.344  -0.673  9.595   1.00 31.19  ? 209 HIS B CB  1 
ATOM   3927 C  CG  . HIS B 1 233 ? 9.979   -0.104  9.837   1.00 34.53  ? 209 HIS B CG  1 
ATOM   3928 N  ND1 . HIS B 1 233 ? 8.951   -0.226  8.928   1.00 33.84  ? 209 HIS B ND1 1 
ATOM   3929 C  CD2 . HIS B 1 233 ? 9.477   0.606   10.876  1.00 35.85  ? 209 HIS B CD2 1 
ATOM   3930 C  CE1 . HIS B 1 233 ? 7.872   0.371   9.399   1.00 36.03  ? 209 HIS B CE1 1 
ATOM   3931 N  NE2 . HIS B 1 233 ? 8.164   0.886   10.580  1.00 35.30  ? 209 HIS B NE2 1 
ATOM   3932 N  N   . PRO B 1 234 ? 9.433   -3.343  9.402   1.00 31.26  ? 210 PRO B N   1 
ATOM   3933 C  CA  . PRO B 1 234 ? 8.627   -4.180  8.495   1.00 30.05  ? 210 PRO B CA  1 
ATOM   3934 C  C   . PRO B 1 234 ? 8.560   -3.655  7.068   1.00 28.17  ? 210 PRO B C   1 
ATOM   3935 O  O   . PRO B 1 234 ? 8.513   -4.455  6.125   1.00 25.35  ? 210 PRO B O   1 
ATOM   3936 C  CB  . PRO B 1 234 ? 7.246   -4.184  9.167   1.00 30.55  ? 210 PRO B CB  1 
ATOM   3937 C  CG  . PRO B 1 234 ? 7.542   -4.006  10.614  1.00 32.38  ? 210 PRO B CG  1 
ATOM   3938 C  CD  . PRO B 1 234 ? 8.743   -3.102  10.684  1.00 31.21  ? 210 PRO B CD  1 
ATOM   3939 N  N   . ASP B 1 235 ? 8.541   -2.331  6.881   1.00 28.33  ? 211 ASP B N   1 
ATOM   3940 C  CA  . ASP B 1 235 ? 8.590   -1.768  5.534   1.00 31.25  ? 211 ASP B CA  1 
ATOM   3941 C  C   . ASP B 1 235 ? 9.891   -2.138  4.828   1.00 31.87  ? 211 ASP B C   1 
ATOM   3942 O  O   . ASP B 1 235 ? 9.906   -2.344  3.609   1.00 30.61  ? 211 ASP B O   1 
ATOM   3943 C  CB  . ASP B 1 235 ? 8.431   -0.246  5.592   1.00 35.71  ? 211 ASP B CB  1 
ATOM   3944 C  CG  . ASP B 1 235 ? 6.978   0.193   5.696   1.00 42.59  ? 211 ASP B CG  1 
ATOM   3945 O  OD1 . ASP B 1 235 ? 6.091   -0.527  5.190   1.00 42.70  ? 211 ASP B OD1 1 
ATOM   3946 O  OD2 . ASP B 1 235 ? 6.729   1.273   6.274   1.00 49.59  ? 211 ASP B OD2 1 
ATOM   3947 N  N   . ASP B 1 236 ? 10.998  -2.213  5.573   1.00 26.52  ? 212 ASP B N   1 
ATOM   3948 C  CA  . ASP B 1 236 ? 12.256  -2.649  4.971   1.00 29.96  ? 212 ASP B CA  1 
ATOM   3949 C  C   . ASP B 1 236 ? 12.143  -4.078  4.459   1.00 28.34  ? 212 ASP B C   1 
ATOM   3950 O  O   . ASP B 1 236 ? 12.585  -4.385  3.345   1.00 24.03  ? 212 ASP B O   1 
ATOM   3951 C  CB  . ASP B 1 236 ? 13.399  -2.537  5.982   1.00 23.44  ? 212 ASP B CB  1 
ATOM   3952 C  CG  . ASP B 1 236 ? 13.718  -1.103  6.346   1.00 29.67  ? 212 ASP B CG  1 
ATOM   3953 O  OD1 . ASP B 1 236 ? 13.542  -0.218  5.483   1.00 27.15  ? 212 ASP B OD1 1 
ATOM   3954 O  OD2 . ASP B 1 236 ? 14.148  -0.865  7.496   1.00 29.60  ? 212 ASP B OD2 1 
ATOM   3955 N  N   . VAL B 1 237 ? 11.545  -4.963  5.259   1.00 27.41  ? 213 VAL B N   1 
ATOM   3956 C  CA  . VAL B 1 237 ? 11.366  -6.352  4.843   1.00 26.24  ? 213 VAL B CA  1 
ATOM   3957 C  C   . VAL B 1 237 ? 10.542  -6.423  3.564   1.00 27.59  ? 213 VAL B C   1 
ATOM   3958 O  O   . VAL B 1 237 ? 10.934  -7.072  2.587   1.00 28.48  ? 213 VAL B O   1 
ATOM   3959 C  CB  . VAL B 1 237 ? 10.716  -7.168  5.975   1.00 26.22  ? 213 VAL B CB  1 
ATOM   3960 C  CG1 . VAL B 1 237 ? 10.448  -8.597  5.517   1.00 26.21  ? 213 VAL B CG1 1 
ATOM   3961 C  CG2 . VAL B 1 237 ? 11.598  -7.152  7.217   1.00 26.48  ? 213 VAL B CG2 1 
ATOM   3962 N  N   . LEU B 1 238 ? 9.378   -5.770  3.558   1.00 28.63  ? 214 LEU B N   1 
ATOM   3963 C  CA  . LEU B 1 238 ? 8.481   -5.842  2.379   1.00 31.52  ? 214 LEU B CA  1 
ATOM   3964 C  C   . LEU B 1 238 ? 9.188   -5.234  1.165   1.00 31.63  ? 214 LEU B C   1 
ATOM   3965 O  O   . LEU B 1 238 ? 9.015   -5.731  0.045   1.00 31.49  ? 214 LEU B O   1 
ATOM   3966 C  CB  . LEU B 1 238 ? 7.177   -5.104  2.680   1.00 31.10  ? 214 LEU B CB  1 
ATOM   3967 C  CG  . LEU B 1 238 ? 5.958   -6.000  2.884   1.00 40.59  ? 214 LEU B CG  1 
ATOM   3968 C  CD1 . LEU B 1 238 ? 5.687   -6.827  1.636   1.00 35.81  ? 214 LEU B CD1 1 
ATOM   3969 C  CD2 . LEU B 1 238 ? 6.158   -6.905  4.089   1.00 35.17  ? 214 LEU B CD2 1 
ATOM   3970 N  N   . HIS B 1 239 ? 9.952   -4.157  1.355   1.00 28.93  ? 215 HIS B N   1 
ATOM   3971 C  CA  . HIS B 1 239 ? 10.637  -3.536  0.228   1.00 29.25  ? 215 HIS B CA  1 
ATOM   3972 C  C   . HIS B 1 239 ? 11.602  -4.514  -0.427  1.00 28.85  ? 215 HIS B C   1 
ATOM   3973 O  O   . HIS B 1 239 ? 11.624  -4.653  -1.655  1.00 32.37  ? 215 HIS B O   1 
ATOM   3974 C  CB  . HIS B 1 239 ? 11.372  -2.281  0.692   1.00 28.42  ? 215 HIS B CB  1 
ATOM   3975 C  CG  . HIS B 1 239 ? 12.284  -1.707  -0.343  1.00 33.86  ? 215 HIS B CG  1 
ATOM   3976 N  ND1 . HIS B 1 239 ? 11.826  -1.202  -1.541  1.00 32.14  ? 215 HIS B ND1 1 
ATOM   3977 C  CD2 . HIS B 1 239 ? 13.630  -1.568  -0.365  1.00 30.74  ? 215 HIS B CD2 1 
ATOM   3978 C  CE1 . HIS B 1 239 ? 12.851  -0.770  -2.254  1.00 32.29  ? 215 HIS B CE1 1 
ATOM   3979 N  NE2 . HIS B 1 239 ? 13.957  -0.980  -1.563  1.00 34.20  ? 215 HIS B NE2 1 
ATOM   3980 N  N   . MET B 1 240 ? 12.414  -5.202  0.379   1.00 28.53  ? 216 MET B N   1 
ATOM   3981 C  CA  . MET B 1 240 ? 13.343  -6.179  -0.180  1.00 28.89  ? 216 MET B CA  1 
ATOM   3982 C  C   . MET B 1 240 ? 12.595  -7.322  -0.858  1.00 26.32  ? 216 MET B C   1 
ATOM   3983 O  O   . MET B 1 240 ? 12.999  -7.787  -1.930  1.00 28.37  ? 216 MET B O   1 
ATOM   3984 C  CB  . MET B 1 240 ? 14.268  -6.709  0.919   1.00 24.39  ? 216 MET B CB  1 
ATOM   3985 C  CG  . MET B 1 240 ? 15.198  -5.656  1.519   1.00 25.32  ? 216 MET B CG  1 
ATOM   3986 S  SD  . MET B 1 240 ? 16.472  -5.063  0.380   1.00 30.41  ? 216 MET B SD  1 
ATOM   3987 C  CE  . MET B 1 240 ? 17.603  -6.452  0.377   1.00 26.21  ? 216 MET B CE  1 
ATOM   3988 N  N   . LYS B 1 241 ? 11.493  -7.781  -0.257  1.00 26.28  ? 217 LYS B N   1 
ATOM   3989 C  CA  . LYS B 1 241 ? 10.706  -8.850  -0.871  1.00 29.49  ? 217 LYS B CA  1 
ATOM   3990 C  C   . LYS B 1 241 ? 10.116  -8.398  -2.200  1.00 27.79  ? 217 LYS B C   1 
ATOM   3991 O  O   . LYS B 1 241 ? 10.250  -9.089  -3.217  1.00 29.66  ? 217 LYS B O   1 
ATOM   3992 C  CB  . LYS B 1 241 ? 9.599   -9.304  0.083   1.00 28.48  ? 217 LYS B CB  1 
ATOM   3993 C  CG  . LYS B 1 241 ? 8.657   -10.371 -0.486  1.00 33.28  ? 217 LYS B CG  1 
ATOM   3994 C  CD  . LYS B 1 241 ? 9.411   -11.619 -0.924  1.00 34.31  ? 217 LYS B CD  1 
ATOM   3995 C  CE  . LYS B 1 241 ? 8.495   -12.841 -1.007  1.00 35.16  ? 217 LYS B CE  1 
ATOM   3996 N  NZ  . LYS B 1 241 ? 7.448   -12.727 -2.063  1.00 33.69  ? 217 LYS B NZ  1 
ATOM   3997 N  N   . ARG B 1 242 ? 9.444   -7.243  -2.207  1.00 29.17  ? 218 ARG B N   1 
ATOM   3998 C  CA  . ARG B 1 242 ? 8.869   -6.722  -3.443  1.00 31.29  ? 218 ARG B CA  1 
ATOM   3999 C  C   . ARG B 1 242 ? 9.927   -6.601  -4.529  1.00 28.40  ? 218 ARG B C   1 
ATOM   4000 O  O   . ARG B 1 242 ? 9.708   -6.999  -5.678  1.00 32.39  ? 218 ARG B O   1 
ATOM   4001 C  CB  . ARG B 1 242 ? 8.224   -5.357  -3.196  1.00 32.72  ? 218 ARG B CB  1 
ATOM   4002 C  CG  . ARG B 1 242 ? 6.794   -5.398  -2.690  1.00 40.78  ? 218 ARG B CG  1 
ATOM   4003 C  CD  . ARG B 1 242 ? 6.150   -4.022  -2.814  1.00 45.54  ? 218 ARG B CD  1 
ATOM   4004 N  NE  . ARG B 1 242 ? 7.006   -2.969  -2.279  1.00 48.35  ? 218 ARG B NE  1 
ATOM   4005 C  CZ  . ARG B 1 242 ? 6.869   -2.408  -1.083  1.00 46.93  ? 218 ARG B CZ  1 
ATOM   4006 N  NH1 . ARG B 1 242 ? 5.873   -2.732  -0.273  1.00 43.44  ? 218 ARG B NH1 1 
ATOM   4007 N  NH2 . ARG B 1 242 ? 7.754   -1.495  -0.691  1.00 39.34  ? 218 ARG B NH2 1 
ATOM   4008 N  N   . THR B 1 243 ? 11.084  -6.035  -4.181  1.00 30.15  ? 219 THR B N   1 
ATOM   4009 C  CA  . THR B 1 243 ? 12.140  -5.839  -5.167  1.00 29.95  ? 219 THR B CA  1 
ATOM   4010 C  C   . THR B 1 243 ? 12.609  -7.172  -5.730  1.00 31.07  ? 219 THR B C   1 
ATOM   4011 O  O   . THR B 1 243 ? 12.758  -7.328  -6.948  1.00 29.92  ? 219 THR B O   1 
ATOM   4012 C  CB  . THR B 1 243 ? 13.305  -5.075  -4.535  1.00 32.89  ? 219 THR B CB  1 
ATOM   4013 O  OG1 . THR B 1 243 ? 12.836  -3.813  -4.036  1.00 30.76  ? 219 THR B OG1 1 
ATOM   4014 C  CG2 . THR B 1 243 ? 14.412  -4.836  -5.555  1.00 31.12  ? 219 THR B CG2 1 
ATOM   4015 N  N   . ALA B 1 244 ? 12.834  -8.155  -4.854  1.00 27.87  ? 220 ALA B N   1 
ATOM   4016 C  CA  . ALA B 1 244 ? 13.264  -9.467  -5.323  1.00 28.59  ? 220 ALA B CA  1 
ATOM   4017 C  C   . ALA B 1 244 ? 12.203  -10.104 -6.210  1.00 30.17  ? 220 ALA B C   1 
ATOM   4018 O  O   . ALA B 1 244 ? 12.527  -10.694 -7.248  1.00 29.96  ? 220 ALA B O   1 
ATOM   4019 C  CB  . ALA B 1 244 ? 13.586  -10.373 -4.135  1.00 29.34  ? 220 ALA B CB  1 
ATOM   4020 N  N   . ASP B 1 245 ? 10.928  -9.993  -5.821  1.00 30.81  ? 221 ASP B N   1 
ATOM   4021 C  CA  . ASP B 1 245 ? 9.856   -10.527 -6.657  1.00 29.34  ? 221 ASP B CA  1 
ATOM   4022 C  C   . ASP B 1 245 ? 9.884   -9.905  -8.048  1.00 30.41  ? 221 ASP B C   1 
ATOM   4023 O  O   . ASP B 1 245 ? 9.735   -10.607 -9.055  1.00 30.56  ? 221 ASP B O   1 
ATOM   4024 C  CB  . ASP B 1 245 ? 8.495   -10.282 -6.002  1.00 31.55  ? 221 ASP B CB  1 
ATOM   4025 C  CG  . ASP B 1 245 ? 8.247   -11.179 -4.806  1.00 34.40  ? 221 ASP B CG  1 
ATOM   4026 O  OD1 . ASP B 1 245 ? 8.945   -12.207 -4.668  1.00 36.78  ? 221 ASP B OD1 1 
ATOM   4027 O  OD2 . ASP B 1 245 ? 7.341   -10.858 -4.008  1.00 33.90  ? 221 ASP B OD2 1 
ATOM   4028 N  N   . ARG B 1 246 ? 10.081  -8.587  -8.123  1.00 28.45  ? 222 ARG B N   1 
ATOM   4029 C  CA  . ARG B 1 246 ? 10.042  -7.905  -9.412  1.00 32.66  ? 222 ARG B CA  1 
ATOM   4030 C  C   . ARG B 1 246 ? 11.265  -8.225  -10.265 1.00 29.92  ? 222 ARG B C   1 
ATOM   4031 O  O   . ARG B 1 246 ? 11.152  -8.319  -11.492 1.00 33.09  ? 222 ARG B O   1 
ATOM   4032 C  CB  . ARG B 1 246 ? 9.921   -6.395  -9.196  1.00 32.20  ? 222 ARG B CB  1 
ATOM   4033 C  CG  . ARG B 1 246 ? 9.948   -5.579  -10.487 1.00 36.07  ? 222 ARG B CG  1 
ATOM   4034 C  CD  . ARG B 1 246 ? 9.612   -4.116  -10.234 1.00 36.73  ? 222 ARG B CD  1 
ATOM   4035 N  NE  . ARG B 1 246 ? 10.418  -3.539  -9.163  1.00 37.49  ? 222 ARG B NE  1 
ATOM   4036 C  CZ  . ARG B 1 246 ? 11.638  -3.042  -9.324  1.00 39.83  ? 222 ARG B CZ  1 
ATOM   4037 N  NH1 . ARG B 1 246 ? 12.247  -3.065  -10.500 1.00 40.29  ? 222 ARG B NH1 1 
ATOM   4038 N  NH2 . ARG B 1 246 ? 12.264  -2.507  -8.279  1.00 37.18  ? 222 ARG B NH2 1 
ATOM   4039 N  N   . LEU B 1 247 ? 12.435  -8.403  -9.645  1.00 28.71  ? 223 LEU B N   1 
ATOM   4040 C  CA  . LEU B 1 247 ? 13.654  -8.622  -10.417 1.00 32.55  ? 223 LEU B CA  1 
ATOM   4041 C  C   . LEU B 1 247 ? 13.846  -10.080 -10.821 1.00 33.24  ? 223 LEU B C   1 
ATOM   4042 O  O   . LEU B 1 247 ? 14.396  -10.346 -11.894 1.00 32.92  ? 223 LEU B O   1 
ATOM   4043 C  CB  . LEU B 1 247 ? 14.879  -8.151  -9.625  1.00 33.27  ? 223 LEU B CB  1 
ATOM   4044 C  CG  . LEU B 1 247 ? 14.977  -6.656  -9.308  1.00 33.30  ? 223 LEU B CG  1 
ATOM   4045 C  CD1 . LEU B 1 247 ? 16.316  -6.339  -8.654  1.00 30.09  ? 223 LEU B CD1 1 
ATOM   4046 C  CD2 . LEU B 1 247 ? 14.781  -5.813  -10.559 1.00 35.44  ? 223 LEU B CD2 1 
ATOM   4047 N  N   . PHE B 1 248 ? 13.414  -11.031 -9.990  1.00 32.11  ? 224 PHE B N   1 
ATOM   4048 C  CA  . PHE B 1 248 ? 13.699  -12.440 -10.220 1.00 34.60  ? 224 PHE B CA  1 
ATOM   4049 C  C   . PHE B 1 248 ? 12.459  -13.319 -10.319 1.00 35.58  ? 224 PHE B C   1 
ATOM   4050 O  O   . PHE B 1 248 ? 12.595  -14.512 -10.617 1.00 34.84  ? 224 PHE B O   1 
ATOM   4051 C  CB  . PHE B 1 248 ? 14.612  -12.975 -9.104  1.00 34.89  ? 224 PHE B CB  1 
ATOM   4052 C  CG  . PHE B 1 248 ? 15.832  -12.128 -8.870  1.00 33.03  ? 224 PHE B CG  1 
ATOM   4053 C  CD1 . PHE B 1 248 ? 16.898  -12.171 -9.752  1.00 35.29  ? 224 PHE B CD1 1 
ATOM   4054 C  CD2 . PHE B 1 248 ? 15.906  -11.284 -7.777  1.00 30.51  ? 224 PHE B CD2 1 
ATOM   4055 C  CE1 . PHE B 1 248 ? 18.019  -11.390 -9.545  1.00 33.35  ? 224 PHE B CE1 1 
ATOM   4056 C  CE2 . PHE B 1 248 ? 17.026  -10.501 -7.563  1.00 31.00  ? 224 PHE B CE2 1 
ATOM   4057 C  CZ  . PHE B 1 248 ? 18.083  -10.554 -8.449  1.00 32.00  ? 224 PHE B CZ  1 
ATOM   4058 N  N   . GLY B 1 249 ? 11.271  -12.777 -10.081 1.00 33.35  ? 225 GLY B N   1 
ATOM   4059 C  CA  . GLY B 1 249 ? 10.050  -13.536 -10.303 1.00 39.57  ? 225 GLY B CA  1 
ATOM   4060 C  C   . GLY B 1 249 ? 10.008  -14.805 -9.473  1.00 40.85  ? 225 GLY B C   1 
ATOM   4061 O  O   . GLY B 1 249 ? 10.122  -14.780 -8.242  1.00 41.42  ? 225 GLY B O   1 
ATOM   4062 N  N   . GLN B 1 250 ? 9.835   -15.936 -10.155 1.00 43.63  ? 226 GLN B N   1 
ATOM   4063 C  CA  . GLN B 1 250 ? 9.719   -17.241 -9.519  1.00 44.07  ? 226 GLN B CA  1 
ATOM   4064 C  C   . GLN B 1 250 ? 11.042  -17.990 -9.463  1.00 41.08  ? 226 GLN B C   1 
ATOM   4065 O  O   . GLN B 1 250 ? 11.083  -19.112 -8.947  1.00 42.70  ? 226 GLN B O   1 
ATOM   4066 C  CB  . GLN B 1 250 ? 8.686   -18.091 -10.266 1.00 47.93  ? 226 GLN B CB  1 
ATOM   4067 C  CG  . GLN B 1 250 ? 7.303   -17.463 -10.347 1.00 53.06  ? 226 GLN B CG  1 
ATOM   4068 C  CD  . GLN B 1 250 ? 6.589   -17.454 -9.011  1.00 61.86  ? 226 GLN B CD  1 
ATOM   4069 O  OE1 . GLN B 1 250 ? 5.999   -18.455 -8.604  1.00 72.08  ? 226 GLN B OE1 1 
ATOM   4070 N  NE2 . GLN B 1 250 ? 6.642   -16.322 -8.318  1.00 60.90  ? 226 GLN B NE2 1 
ATOM   4071 N  N   . ASP B 1 251 ? 12.120  -17.400 -9.979  1.00 37.78  ? 227 ASP B N   1 
ATOM   4072 C  CA  . ASP B 1 251 ? 13.409  -18.068 -10.094 1.00 38.17  ? 227 ASP B CA  1 
ATOM   4073 C  C   . ASP B 1 251 ? 14.300  -17.843 -8.878  1.00 39.44  ? 227 ASP B C   1 
ATOM   4074 O  O   . ASP B 1 251 ? 15.532  -17.843 -9.009  1.00 38.42  ? 227 ASP B O   1 
ATOM   4075 C  CB  . ASP B 1 251 ? 14.118  -17.597 -11.366 1.00 39.44  ? 227 ASP B CB  1 
ATOM   4076 C  CG  . ASP B 1 251 ? 15.070  -18.635 -11.929 1.00 42.65  ? 227 ASP B CG  1 
ATOM   4077 O  OD1 . ASP B 1 251 ? 14.995  -19.811 -11.511 1.00 42.79  ? 227 ASP B OD1 1 
ATOM   4078 O  OD2 . ASP B 1 251 ? 15.895  -18.271 -12.796 1.00 45.25  ? 227 ASP B OD2 1 
ATOM   4079 N  N   . TYR B 1 252 ? 13.719  -17.648 -7.696  1.00 34.93  ? 228 TYR B N   1 
ATOM   4080 C  CA  . TYR B 1 252 ? 14.527  -17.454 -6.503  1.00 36.90  ? 228 TYR B CA  1 
ATOM   4081 C  C   . TYR B 1 252 ? 13.790  -17.997 -5.289  1.00 35.51  ? 228 TYR B C   1 
ATOM   4082 O  O   . TYR B 1 252 ? 12.565  -18.146 -5.288  1.00 35.89  ? 228 TYR B O   1 
ATOM   4083 C  CB  . TYR B 1 252 ? 14.892  -15.975 -6.306  1.00 33.09  ? 228 TYR B CB  1 
ATOM   4084 C  CG  . TYR B 1 252 ? 13.888  -15.145 -5.533  1.00 34.94  ? 228 TYR B CG  1 
ATOM   4085 C  CD1 . TYR B 1 252 ? 12.722  -14.684 -6.131  1.00 34.93  ? 228 TYR B CD1 1 
ATOM   4086 C  CD2 . TYR B 1 252 ? 14.129  -14.790 -4.211  1.00 31.59  ? 228 TYR B CD2 1 
ATOM   4087 C  CE1 . TYR B 1 252 ? 11.813  -13.911 -5.425  1.00 32.58  ? 228 TYR B CE1 1 
ATOM   4088 C  CE2 . TYR B 1 252 ? 13.232  -14.020 -3.502  1.00 30.00  ? 228 TYR B CE2 1 
ATOM   4089 C  CZ  . TYR B 1 252 ? 12.074  -13.586 -4.110  1.00 33.17  ? 228 TYR B CZ  1 
ATOM   4090 O  OH  . TYR B 1 252 ? 11.186  -12.816 -3.397  1.00 35.44  ? 228 TYR B OH  1 
ATOM   4091 N  N   . ARG B 1 253 ? 14.571  -18.319 -4.261  1.00 33.54  ? 229 ARG B N   1 
ATOM   4092 C  CA  . ARG B 1 253 ? 14.062  -18.733 -2.962  1.00 32.26  ? 229 ARG B CA  1 
ATOM   4093 C  C   . ARG B 1 253 ? 14.491  -17.692 -1.941  1.00 31.97  ? 229 ARG B C   1 
ATOM   4094 O  O   . ARG B 1 253 ? 15.671  -17.333 -1.876  1.00 33.24  ? 229 ARG B O   1 
ATOM   4095 C  CB  . ARG B 1 253 ? 14.589  -20.113 -2.567  1.00 32.64  ? 229 ARG B CB  1 
ATOM   4096 C  CG  . ARG B 1 253 ? 14.389  -21.186 -3.622  1.00 36.99  ? 229 ARG B CG  1 
ATOM   4097 C  CD  . ARG B 1 253 ? 12.930  -21.556 -3.800  1.00 35.47  ? 229 ARG B CD  1 
ATOM   4098 N  NE  . ARG B 1 253 ? 12.794  -22.675 -4.725  1.00 41.45  ? 229 ARG B NE  1 
ATOM   4099 C  CZ  . ARG B 1 253 ? 12.611  -22.559 -6.035  1.00 46.24  ? 229 ARG B CZ  1 
ATOM   4100 N  NH1 . ARG B 1 253 ? 12.464  -21.378 -6.615  1.00 41.08  ? 229 ARG B NH1 1 
ATOM   4101 N  NH2 . ARG B 1 253 ? 12.577  -23.659 -6.783  1.00 49.15  ? 229 ARG B NH2 1 
ATOM   4102 N  N   . TRP B 1 254 ? 13.539  -17.215 -1.151  1.00 29.74  ? 230 TRP B N   1 
ATOM   4103 C  CA  . TRP B 1 254 ? 13.754  -16.092 -0.253  1.00 29.07  ? 230 TRP B CA  1 
ATOM   4104 C  C   . TRP B 1 254 ? 14.074  -16.596 1.147   1.00 31.58  ? 230 TRP B C   1 
ATOM   4105 O  O   . TRP B 1 254 ? 13.336  -17.417 1.703   1.00 30.76  ? 230 TRP B O   1 
ATOM   4106 C  CB  . TRP B 1 254 ? 12.517  -15.195 -0.222  1.00 30.30  ? 230 TRP B CB  1 
ATOM   4107 C  CG  . TRP B 1 254 ? 12.670  -13.947 0.593   1.00 28.68  ? 230 TRP B CG  1 
ATOM   4108 C  CD1 . TRP B 1 254 ? 13.771  -13.143 0.676   1.00 28.86  ? 230 TRP B CD1 1 
ATOM   4109 C  CD2 . TRP B 1 254 ? 11.679  -13.359 1.443   1.00 27.68  ? 230 TRP B CD2 1 
ATOM   4110 N  NE1 . TRP B 1 254 ? 13.523  -12.088 1.527   1.00 27.88  ? 230 TRP B NE1 1 
ATOM   4111 C  CE2 . TRP B 1 254 ? 12.246  -12.200 2.011   1.00 25.94  ? 230 TRP B CE2 1 
ATOM   4112 C  CE3 . TRP B 1 254 ? 10.365  -13.703 1.780   1.00 28.67  ? 230 TRP B CE3 1 
ATOM   4113 C  CZ2 . TRP B 1 254 ? 11.547  -11.385 2.896   1.00 28.26  ? 230 TRP B CZ2 1 
ATOM   4114 C  CZ3 . TRP B 1 254 ? 9.673   -12.895 2.659   1.00 25.54  ? 230 TRP B CZ3 1 
ATOM   4115 C  CH2 . TRP B 1 254 ? 10.263  -11.746 3.205   1.00 28.53  ? 230 TRP B CH2 1 
ATOM   4116 N  N   . SER B 1 255 ? 15.176  -16.107 1.708   1.00 30.94  ? 231 SER B N   1 
ATOM   4117 C  CA  . SER B 1 255 ? 15.506  -16.326 3.106   1.00 29.75  ? 231 SER B CA  1 
ATOM   4118 C  C   . SER B 1 255 ? 15.821  -14.982 3.746   1.00 28.87  ? 231 SER B C   1 
ATOM   4119 O  O   . SER B 1 255 ? 16.273  -14.049 3.076   1.00 27.31  ? 231 SER B O   1 
ATOM   4120 C  CB  . SER B 1 255 ? 16.692  -17.285 3.269   1.00 29.05  ? 231 SER B CB  1 
ATOM   4121 O  OG  . SER B 1 255 ? 16.909  -17.592 4.636   1.00 28.01  ? 231 SER B OG  1 
ATOM   4122 N  N   . VAL B 1 256 ? 15.564  -14.885 5.049   1.00 28.52  ? 232 VAL B N   1 
ATOM   4123 C  CA  . VAL B 1 256 ? 15.752  -13.643 5.786   1.00 27.34  ? 232 VAL B CA  1 
ATOM   4124 C  C   . VAL B 1 256 ? 16.714  -13.877 6.938   1.00 28.67  ? 232 VAL B C   1 
ATOM   4125 O  O   . VAL B 1 256 ? 16.820  -14.980 7.486   1.00 26.83  ? 232 VAL B O   1 
ATOM   4126 C  CB  . VAL B 1 256 ? 14.424  -13.065 6.328   1.00 28.09  ? 232 VAL B CB  1 
ATOM   4127 C  CG1 . VAL B 1 256 ? 13.466  -12.757 5.189   1.00 25.44  ? 232 VAL B CG1 1 
ATOM   4128 C  CG2 . VAL B 1 256 ? 13.797  -14.020 7.344   1.00 25.38  ? 232 VAL B CG2 1 
ATOM   4129 N  N   . LEU B 1 257 ? 17.410  -12.807 7.308   1.00 27.04  ? 233 LEU B N   1 
ATOM   4130 C  CA  . LEU B 1 257 ? 18.282  -12.776 8.475   1.00 28.76  ? 233 LEU B CA  1 
ATOM   4131 C  C   . LEU B 1 257 ? 17.959  -11.497 9.236   1.00 29.48  ? 233 LEU B C   1 
ATOM   4132 O  O   . LEU B 1 257 ? 18.246  -10.396 8.753   1.00 29.08  ? 233 LEU B O   1 
ATOM   4133 C  CB  . LEU B 1 257 ? 19.754  -12.821 8.061   1.00 28.95  ? 233 LEU B CB  1 
ATOM   4134 C  CG  . LEU B 1 257 ? 20.834  -12.964 9.138   1.00 31.67  ? 233 LEU B CG  1 
ATOM   4135 C  CD1 . LEU B 1 257 ? 22.196  -12.995 8.467   1.00 31.28  ? 233 LEU B CD1 1 
ATOM   4136 C  CD2 . LEU B 1 257 ? 20.789  -11.851 10.177  1.00 30.38  ? 233 LEU B CD2 1 
ATOM   4137 N  N   . GLY B 1 258 ? 17.353  -11.640 10.409  1.00 28.99  ? 234 GLY B N   1 
ATOM   4138 C  CA  . GLY B 1 258 ? 17.100  -10.503 11.272  1.00 29.10  ? 234 GLY B CA  1 
ATOM   4139 C  C   . GLY B 1 258 ? 18.133  -10.410 12.376  1.00 31.63  ? 234 GLY B C   1 
ATOM   4140 O  O   . GLY B 1 258 ? 18.197  -11.275 13.253  1.00 31.15  ? 234 GLY B O   1 
ATOM   4141 N  N   . ALA B 1 259 ? 18.951  -9.363  12.341  1.00 31.82  ? 235 ALA B N   1 
ATOM   4142 C  CA  . ALA B 1 259 ? 20.020  -9.221  13.317  1.00 34.89  ? 235 ALA B CA  1 
ATOM   4143 C  C   . ALA B 1 259 ? 19.460  -8.989  14.717  1.00 34.40  ? 235 ALA B C   1 
ATOM   4144 O  O   . ALA B 1 259 ? 18.415  -8.359  14.902  1.00 32.46  ? 235 ALA B O   1 
ATOM   4145 C  CB  . ALA B 1 259 ? 20.945  -8.068  12.931  1.00 33.79  ? 235 ALA B CB  1 
ATOM   4146 N  N   . GLY B 1 260 ? 20.171  -9.521  15.706  1.00 35.36  ? 236 GLY B N   1 
ATOM   4147 C  CA  . GLY B 1 260 ? 19.849  -9.240  17.096  1.00 35.76  ? 236 GLY B CA  1 
ATOM   4148 C  C   . GLY B 1 260 ? 18.410  -9.557  17.447  1.00 35.85  ? 236 GLY B C   1 
ATOM   4149 O  O   . GLY B 1 260 ? 17.879  -10.623 17.114  1.00 29.50  ? 236 GLY B O   1 
ATOM   4150 N  N   . ARG B 1 261 ? 17.767  -8.611  18.132  1.00 37.52  ? 237 ARG B N   1 
ATOM   4151 C  CA  . ARG B 1 261 ? 16.424  -8.807  18.662  1.00 43.81  ? 237 ARG B CA  1 
ATOM   4152 C  C   . ARG B 1 261 ? 15.364  -8.961  17.577  1.00 36.65  ? 237 ARG B C   1 
ATOM   4153 O  O   . ARG B 1 261 ? 14.247  -9.385  17.891  1.00 35.46  ? 237 ARG B O   1 
ATOM   4154 C  CB  . ARG B 1 261 ? 16.060  -7.630  19.569  1.00 53.00  ? 237 ARG B CB  1 
ATOM   4155 C  CG  . ARG B 1 261 ? 15.779  -6.342  18.810  1.00 57.40  ? 237 ARG B CG  1 
ATOM   4156 C  CD  . ARG B 1 261 ? 15.802  -5.123  19.719  1.00 69.67  ? 237 ARG B CD  1 
ATOM   4157 N  NE  . ARG B 1 261 ? 14.970  -5.294  20.904  1.00 80.16  ? 237 ARG B NE  1 
ATOM   4158 C  CZ  . ARG B 1 261 ? 14.799  -4.369  21.838  1.00 82.25  ? 237 ARG B CZ  1 
ATOM   4159 N  NH1 . ARG B 1 261 ? 15.378  -3.182  21.751  1.00 82.98  ? 237 ARG B NH1 1 
ATOM   4160 N  NH2 . ARG B 1 261 ? 14.028  -4.641  22.887  1.00 84.41  ? 237 ARG B NH2 1 
ATOM   4161 N  N   . ASN B 1 262 ? 15.677  -8.627  16.324  1.00 31.00  ? 238 ASN B N   1 
ATOM   4162 C  CA  . ASN B 1 262 ? 14.728  -8.757  15.226  1.00 33.61  ? 238 ASN B CA  1 
ATOM   4163 C  C   . ASN B 1 262 ? 14.687  -10.162 14.640  1.00 32.32  ? 238 ASN B C   1 
ATOM   4164 O  O   . ASN B 1 262 ? 13.900  -10.409 13.720  1.00 30.35  ? 238 ASN B O   1 
ATOM   4165 C  CB  . ASN B 1 262 ? 15.076  -7.765  14.113  1.00 31.88  ? 238 ASN B CB  1 
ATOM   4166 C  CG  . ASN B 1 262 ? 15.322  -6.366  14.634  1.00 34.86  ? 238 ASN B CG  1 
ATOM   4167 O  OD1 . ASN B 1 262 ? 14.389  -5.658  15.008  1.00 35.47  ? 238 ASN B OD1 1 
ATOM   4168 N  ND2 . ASN B 1 262 ? 16.586  -5.955  14.652  1.00 35.22  ? 238 ASN B ND2 1 
ATOM   4169 N  N   . GLN B 1 263 ? 15.505  -11.078 15.157  1.00 27.30  ? 239 GLN B N   1 
ATOM   4170 C  CA  . GLN B 1 263 ? 15.698  -12.372 14.510  1.00 29.23  ? 239 GLN B CA  1 
ATOM   4171 C  C   . GLN B 1 263 ? 14.377  -13.107 14.320  1.00 27.61  ? 239 GLN B C   1 
ATOM   4172 O  O   . GLN B 1 263 ? 14.030  -13.506 13.202  1.00 29.44  ? 239 GLN B O   1 
ATOM   4173 C  CB  . GLN B 1 263 ? 16.678  -13.206 15.338  1.00 28.48  ? 239 GLN B CB  1 
ATOM   4174 C  CG  . GLN B 1 263 ? 16.967  -14.595 14.803  1.00 30.20  ? 239 GLN B CG  1 
ATOM   4175 C  CD  . GLN B 1 263 ? 18.014  -15.315 15.634  1.00 33.18  ? 239 GLN B CD  1 
ATOM   4176 O  OE1 . GLN B 1 263 ? 17.768  -15.682 16.783  1.00 33.54  ? 239 GLN B OE1 1 
ATOM   4177 N  NE2 . GLN B 1 263 ? 19.197  -15.501 15.063  1.00 33.36  ? 239 GLN B NE2 1 
ATOM   4178 N  N   . LEU B 1 264 ? 13.620  -13.292 15.399  1.00 27.94  ? 240 LEU B N   1 
ATOM   4179 C  CA  . LEU B 1 264 ? 12.415  -14.108 15.311  1.00 29.39  ? 240 LEU B CA  1 
ATOM   4180 C  C   . LEU B 1 264 ? 11.243  -13.350 14.698  1.00 29.06  ? 240 LEU B C   1 
ATOM   4181 O  O   . LEU B 1 264 ? 10.424  -13.957 13.999  1.00 25.94  ? 240 LEU B O   1 
ATOM   4182 C  CB  . LEU B 1 264 ? 12.048  -14.642 16.696  1.00 29.46  ? 240 LEU B CB  1 
ATOM   4183 C  CG  . LEU B 1 264 ? 13.085  -15.604 17.284  1.00 30.30  ? 240 LEU B CG  1 
ATOM   4184 C  CD1 . LEU B 1 264 ? 12.701  -16.028 18.692  1.00 32.47  ? 240 LEU B CD1 1 
ATOM   4185 C  CD2 . LEU B 1 264 ? 13.269  -16.828 16.389  1.00 28.05  ? 240 LEU B CD2 1 
ATOM   4186 N  N   . ASN B 1 265 ? 11.138  -12.041 14.938  1.00 29.35  ? 241 ASN B N   1 
ATOM   4187 C  CA  . ASN B 1 265 ? 10.103  -11.255 14.272  1.00 29.81  ? 241 ASN B CA  1 
ATOM   4188 C  C   . ASN B 1 265 ? 10.216  -11.389 12.760  1.00 28.75  ? 241 ASN B C   1 
ATOM   4189 O  O   . ASN B 1 265 ? 9.239   -11.711 12.073  1.00 28.75  ? 241 ASN B O   1 
ATOM   4190 C  CB  . ASN B 1 265 ? 10.207  -9.783  14.674  1.00 30.68  ? 241 ASN B CB  1 
ATOM   4191 C  CG  . ASN B 1 265 ? 9.731   -9.520  16.090  1.00 34.31  ? 241 ASN B CG  1 
ATOM   4192 O  OD1 . ASN B 1 265 ? 8.953   -10.290 16.656  1.00 31.40  ? 241 ASN B OD1 1 
ATOM   4193 N  ND2 . ASN B 1 265 ? 10.189  -8.415  16.666  1.00 34.87  ? 241 ASN B ND2 1 
ATOM   4194 N  N   . ILE B 1 266 ? 11.412  -11.144 12.224  1.00 24.84  ? 242 ILE B N   1 
ATOM   4195 C  CA  . ILE B 1 266 ? 11.606  -11.179 10.779  1.00 28.50  ? 242 ILE B CA  1 
ATOM   4196 C  C   . ILE B 1 266 ? 11.512  -12.605 10.247  1.00 25.13  ? 242 ILE B C   1 
ATOM   4197 O  O   . ILE B 1 266 ? 11.002  -12.829 9.141   1.00 27.01  ? 242 ILE B O   1 
ATOM   4198 C  CB  . ILE B 1 266 ? 12.945  -10.497 10.439  1.00 31.63  ? 242 ILE B CB  1 
ATOM   4199 C  CG1 . ILE B 1 266 ? 12.786  -8.987  10.652  1.00 29.42  ? 242 ILE B CG1 1 
ATOM   4200 C  CG2 . ILE B 1 266 ? 13.389  -10.820 9.018   1.00 28.28  ? 242 ILE B CG2 1 
ATOM   4201 C  CD1 . ILE B 1 266 ? 14.039  -8.182  10.486  1.00 31.65  ? 242 ILE B CD1 1 
ATOM   4202 N  N   . ALA B 1 267 ? 11.975  -13.592 11.017  1.00 26.33  ? 243 ALA B N   1 
ATOM   4203 C  CA  . ALA B 1 267 ? 11.762  -14.982 10.626  1.00 25.32  ? 243 ALA B CA  1 
ATOM   4204 C  C   . ALA B 1 267 ? 10.276  -15.288 10.474  1.00 27.76  ? 243 ALA B C   1 
ATOM   4205 O  O   . ALA B 1 267 ? 9.865   -15.963 9.522   1.00 28.28  ? 243 ALA B O   1 
ATOM   4206 C  CB  . ALA B 1 267 ? 12.400  -15.922 11.650  1.00 25.62  ? 243 ALA B CB  1 
ATOM   4207 N  N   . ALA B 1 268 ? 9.451   -14.797 11.402  1.00 26.43  ? 244 ALA B N   1 
ATOM   4208 C  CA  . ALA B 1 268 ? 8.020   -15.082 11.343  1.00 26.19  ? 244 ALA B CA  1 
ATOM   4209 C  C   . ALA B 1 268 ? 7.372   -14.425 10.132  1.00 27.17  ? 244 ALA B C   1 
ATOM   4210 O  O   . ALA B 1 268 ? 6.525   -15.034 9.466   1.00 24.56  ? 244 ALA B O   1 
ATOM   4211 C  CB  . ALA B 1 268 ? 7.342   -14.619 12.630  1.00 24.69  ? 244 ALA B CB  1 
ATOM   4212 N  N   . MET B 1 269 ? 7.748   -13.180 9.831   1.00 26.98  ? 245 MET B N   1 
ATOM   4213 C  CA  . MET B 1 269 ? 7.247   -12.534 8.623   1.00 26.97  ? 245 MET B CA  1 
ATOM   4214 C  C   . MET B 1 269 ? 7.560   -13.375 7.392   1.00 26.37  ? 245 MET B C   1 
ATOM   4215 O  O   . MET B 1 269 ? 6.681   -13.636 6.561   1.00 28.67  ? 245 MET B O   1 
ATOM   4216 C  CB  . MET B 1 269 ? 7.853   -11.137 8.486   1.00 27.23  ? 245 MET B CB  1 
ATOM   4217 C  CG  . MET B 1 269 ? 7.460   -10.181 9.598   1.00 30.12  ? 245 MET B CG  1 
ATOM   4218 S  SD  . MET B 1 269 ? 8.125   -8.522  9.352   1.00 36.82  ? 245 MET B SD  1 
ATOM   4219 C  CE  . MET B 1 269 ? 7.215   -8.024  7.891   1.00 31.48  ? 245 MET B CE  1 
ATOM   4220 N  N   . SER B 1 270 ? 8.811   -13.819 7.263   1.00 27.76  ? 246 SER B N   1 
ATOM   4221 C  CA  . SER B 1 270 ? 9.203   -14.597 6.092   1.00 28.65  ? 246 SER B CA  1 
ATOM   4222 C  C   . SER B 1 270 ? 8.420   -15.899 6.014   1.00 24.87  ? 246 SER B C   1 
ATOM   4223 O  O   . SER B 1 270 ? 7.824   -16.217 4.979   1.00 28.64  ? 246 SER B O   1 
ATOM   4224 C  CB  . SER B 1 270 ? 10.703  -14.884 6.125   1.00 23.91  ? 246 SER B CB  1 
ATOM   4225 O  OG  . SER B 1 270 ? 11.062  -15.756 5.065   1.00 31.37  ? 246 SER B OG  1 
ATOM   4226 N  N   . ALA B 1 271 ? 8.430   -16.680 7.097   1.00 27.49  ? 247 ALA B N   1 
ATOM   4227 C  CA  . ALA B 1 271 ? 7.681   -17.932 7.115   1.00 28.59  ? 247 ALA B CA  1 
ATOM   4228 C  C   . ALA B 1 271 ? 6.232   -17.707 6.711   1.00 29.65  ? 247 ALA B C   1 
ATOM   4229 O  O   . ALA B 1 271 ? 5.642   -18.526 5.997   1.00 30.46  ? 247 ALA B O   1 
ATOM   4230 C  CB  . ALA B 1 271 ? 7.754   -18.565 8.506   1.00 27.97  ? 247 ALA B CB  1 
ATOM   4231 N  N   . ALA B 1 272 ? 5.642   -16.596 7.157   1.00 29.68  ? 248 ALA B N   1 
ATOM   4232 C  CA  . ALA B 1 272 ? 4.249   -16.301 6.846   1.00 27.94  ? 248 ALA B CA  1 
ATOM   4233 C  C   . ALA B 1 272 ? 4.059   -15.829 5.411   1.00 30.23  ? 248 ALA B C   1 
ATOM   4234 O  O   . ALA B 1 272 ? 2.926   -15.833 4.917   1.00 29.87  ? 248 ALA B O   1 
ATOM   4235 C  CB  . ALA B 1 272 ? 3.712   -15.237 7.807   1.00 27.71  ? 248 ALA B CB  1 
ATOM   4236 N  N   . MET B 1 273 ? 5.135   -15.427 4.733   1.00 28.45  ? 249 MET B N   1 
ATOM   4237 C  CA  . MET B 1 273 ? 5.056   -14.887 3.382   1.00 27.81  ? 249 MET B CA  1 
ATOM   4238 C  C   . MET B 1 273 ? 5.633   -15.831 2.334   1.00 30.13  ? 249 MET B C   1 
ATOM   4239 O  O   . MET B 1 273 ? 5.855   -15.413 1.193   1.00 33.41  ? 249 MET B O   1 
ATOM   4240 C  CB  . MET B 1 273 ? 5.772   -13.536 3.324   1.00 29.32  ? 249 MET B CB  1 
ATOM   4241 C  CG  . MET B 1 273 ? 5.112   -12.457 4.172   1.00 27.40  ? 249 MET B CG  1 
ATOM   4242 S  SD  . MET B 1 273 ? 6.114   -10.967 4.346   1.00 37.05  ? 249 MET B SD  1 
ATOM   4243 C  CE  . MET B 1 273 ? 6.365   -10.542 2.622   1.00 34.16  ? 249 MET B CE  1 
ATOM   4244 N  N   . GLY B 1 274 ? 5.883   -17.089 2.688   1.00 28.86  ? 250 GLY B N   1 
ATOM   4245 C  CA  . GLY B 1 274 ? 6.401   -18.056 1.744   1.00 30.34  ? 250 GLY B CA  1 
ATOM   4246 C  C   . GLY B 1 274 ? 7.908   -18.140 1.657   1.00 31.24  ? 250 GLY B C   1 
ATOM   4247 O  O   . GLY B 1 274 ? 8.423   -18.778 0.730   1.00 31.90  ? 250 GLY B O   1 
ATOM   4248 N  N   . GLY B 1 275 ? 8.635   -17.525 2.591   1.00 27.39  ? 251 GLY B N   1 
ATOM   4249 C  CA  . GLY B 1 275 ? 10.080  -17.539 2.581   1.00 26.67  ? 251 GLY B CA  1 
ATOM   4250 C  C   . GLY B 1 275 ? 10.665  -18.478 3.621   1.00 30.80  ? 251 GLY B C   1 
ATOM   4251 O  O   . GLY B 1 275 ? 9.962   -19.232 4.298   1.00 30.93  ? 251 GLY B O   1 
ATOM   4252 N  N   . HIS B 1 276 ? 11.988  -18.412 3.749   1.00 28.72  ? 252 HIS B N   1 
ATOM   4253 C  CA  . HIS B 1 276 ? 12.757  -19.264 4.645   1.00 27.66  ? 252 HIS B CA  1 
ATOM   4254 C  C   . HIS B 1 276 ? 13.491  -18.393 5.657   1.00 28.17  ? 252 HIS B C   1 
ATOM   4255 O  O   . HIS B 1 276 ? 13.506  -17.165 5.552   1.00 28.63  ? 252 HIS B O   1 
ATOM   4256 C  CB  . HIS B 1 276 ? 13.710  -20.143 3.832   1.00 29.13  ? 252 HIS B CB  1 
ATOM   4257 C  CG  . HIS B 1 276 ? 13.043  -20.789 2.658   1.00 32.69  ? 252 HIS B CG  1 
ATOM   4258 N  ND1 . HIS B 1 276 ? 12.336  -21.966 2.761   1.00 32.05  ? 252 HIS B ND1 1 
ATOM   4259 C  CD2 . HIS B 1 276 ? 12.927  -20.394 1.368   1.00 30.27  ? 252 HIS B CD2 1 
ATOM   4260 C  CE1 . HIS B 1 276 ? 11.841  -22.288 1.580   1.00 33.32  ? 252 HIS B CE1 1 
ATOM   4261 N  NE2 . HIS B 1 276 ? 12.184  -21.349 0.717   1.00 33.27  ? 252 HIS B NE2 1 
ATOM   4262 N  N   . VAL B 1 277 ? 14.084  -19.028 6.668   1.00 26.76  ? 253 VAL B N   1 
ATOM   4263 C  CA  . VAL B 1 277 ? 14.537  -18.313 7.855   1.00 28.11  ? 253 VAL B CA  1 
ATOM   4264 C  C   . VAL B 1 277 ? 15.956  -18.726 8.215   1.00 27.93  ? 253 VAL B C   1 
ATOM   4265 O  O   . VAL B 1 277 ? 16.338  -19.893 8.067   1.00 27.66  ? 253 VAL B O   1 
ATOM   4266 C  CB  . VAL B 1 277 ? 13.593  -18.555 9.054   1.00 28.57  ? 253 VAL B CB  1 
ATOM   4267 C  CG1 . VAL B 1 277 ? 12.143  -18.365 8.635   1.00 26.95  ? 253 VAL B CG1 1 
ATOM   4268 C  CG2 . VAL B 1 277 ? 13.813  -19.938 9.642   1.00 29.86  ? 253 VAL B CG2 1 
ATOM   4269 N  N   . ARG B 1 278 ? 16.728  -17.760 8.705   1.00 25.66  ? 254 ARG B N   1 
ATOM   4270 C  CA  . ARG B 1 278 ? 18.055  -17.994 9.250   1.00 30.22  ? 254 ARG B CA  1 
ATOM   4271 C  C   . ARG B 1 278 ? 18.082  -17.545 10.702  1.00 29.02  ? 254 ARG B C   1 
ATOM   4272 O  O   . ARG B 1 278 ? 17.620  -16.445 11.027  1.00 28.45  ? 254 ARG B O   1 
ATOM   4273 C  CB  . ARG B 1 278 ? 19.126  -17.249 8.450   1.00 28.71  ? 254 ARG B CB  1 
ATOM   4274 C  CG  . ARG B 1 278 ? 20.458  -17.131 9.182   1.00 32.35  ? 254 ARG B CG  1 
ATOM   4275 C  CD  . ARG B 1 278 ? 21.573  -16.691 8.250   1.00 32.37  ? 254 ARG B CD  1 
ATOM   4276 N  NE  . ARG B 1 278 ? 22.689  -16.094 8.974   1.00 33.08  ? 254 ARG B NE  1 
ATOM   4277 C  CZ  . ARG B 1 278 ? 23.866  -15.806 8.432   1.00 34.95  ? 254 ARG B CZ  1 
ATOM   4278 N  NH1 . ARG B 1 278 ? 24.135  -16.095 7.170   1.00 34.55  ? 254 ARG B NH1 1 
ATOM   4279 N  NH2 . ARG B 1 278 ? 24.793  -15.209 9.175   1.00 33.15  ? 254 ARG B NH2 1 
ATOM   4280 N  N   . VAL B 1 279 ? 18.622  -18.396 11.570  1.00 26.82  ? 255 VAL B N   1 
ATOM   4281 C  CA  . VAL B 1 279 ? 18.850  -18.046 12.967  1.00 27.95  ? 255 VAL B CA  1 
ATOM   4282 C  C   . VAL B 1 279 ? 20.302  -18.352 13.305  1.00 31.96  ? 255 VAL B C   1 
ATOM   4283 O  O   . VAL B 1 279 ? 21.090  -18.720 12.426  1.00 30.90  ? 255 VAL B O   1 
ATOM   4284 C  CB  . VAL B 1 279 ? 17.891  -18.806 13.900  1.00 29.78  ? 255 VAL B CB  1 
ATOM   4285 C  CG1 . VAL B 1 279 ? 16.447  -18.410 13.613  1.00 29.15  ? 255 VAL B CG1 1 
ATOM   4286 C  CG2 . VAL B 1 279 ? 18.087  -20.314 13.755  1.00 26.58  ? 255 VAL B CG2 1 
ATOM   4287 N  N   . GLY B 1 280 ? 20.667  -18.201 14.577  1.00 31.04  ? 256 GLY B N   1 
ATOM   4288 C  CA  . GLY B 1 280 ? 21.987  -18.589 15.031  1.00 29.74  ? 256 GLY B CA  1 
ATOM   4289 C  C   . GLY B 1 280 ? 22.713  -17.517 15.816  1.00 31.27  ? 256 GLY B C   1 
ATOM   4290 O  O   . GLY B 1 280 ? 22.430  -16.325 15.666  1.00 31.29  ? 256 GLY B O   1 
ATOM   4291 N  N   . LEU B 1 281 ? 23.663  -17.940 16.656  1.00 30.34  ? 257 LEU B N   1 
ATOM   4292 C  CA  . LEU B 1 281 ? 24.439  -17.016 17.474  1.00 31.12  ? 257 LEU B CA  1 
ATOM   4293 C  C   . LEU B 1 281 ? 25.369  -16.127 16.656  1.00 31.84  ? 257 LEU B C   1 
ATOM   4294 O  O   . LEU B 1 281 ? 25.881  -15.141 17.196  1.00 31.53  ? 257 LEU B O   1 
ATOM   4295 C  CB  . LEU B 1 281 ? 25.249  -17.795 18.512  1.00 33.13  ? 257 LEU B CB  1 
ATOM   4296 C  CG  . LEU B 1 281 ? 24.537  -18.116 19.831  1.00 36.60  ? 257 LEU B CG  1 
ATOM   4297 C  CD1 . LEU B 1 281 ? 23.156  -18.708 19.597  1.00 33.39  ? 257 LEU B CD1 1 
ATOM   4298 C  CD2 . LEU B 1 281 ? 25.384  -19.064 20.670  1.00 35.62  ? 257 LEU B CD2 1 
ATOM   4299 N  N   . GLU B 1 282 ? 25.610  -16.448 15.380  1.00 30.39  ? 258 GLU B N   1 
ATOM   4300 C  CA  . GLU B 1 282 ? 26.307  -15.502 14.514  1.00 32.50  ? 258 GLU B CA  1 
ATOM   4301 C  C   . GLU B 1 282 ? 25.527  -14.203 14.382  1.00 33.14  ? 258 GLU B C   1 
ATOM   4302 O  O   . GLU B 1 282 ? 26.124  -13.131 14.231  1.00 35.60  ? 258 GLU B O   1 
ATOM   4303 C  CB  . GLU B 1 282 ? 26.538  -16.111 13.127  1.00 33.21  ? 258 GLU B CB  1 
ATOM   4304 C  CG  . GLU B 1 282 ? 26.918  -15.093 12.037  1.00 32.28  ? 258 GLU B CG  1 
ATOM   4305 C  CD  . GLU B 1 282 ? 27.496  -15.748 10.784  1.00 34.29  ? 258 GLU B CD  1 
ATOM   4306 O  OE1 . GLU B 1 282 ? 27.678  -16.984 10.790  1.00 32.05  ? 258 GLU B OE1 1 
ATOM   4307 O  OE2 . GLU B 1 282 ? 27.777  -15.031 9.795   1.00 34.32  ? 258 GLU B OE2 1 
ATOM   4308 N  N   . ASP B 1 283 ? 24.196  -14.279 14.456  1.00 32.57  ? 259 ASP B N   1 
ATOM   4309 C  CA  . ASP B 1 283 ? 23.327  -13.149 14.168  1.00 35.18  ? 259 ASP B CA  1 
ATOM   4310 C  C   . ASP B 1 283 ? 22.686  -12.532 15.402  1.00 35.69  ? 259 ASP B C   1 
ATOM   4311 O  O   . ASP B 1 283 ? 22.333  -11.350 15.364  1.00 37.14  ? 259 ASP B O   1 
ATOM   4312 C  CB  . ASP B 1 283 ? 22.214  -13.581 13.202  1.00 33.27  ? 259 ASP B CB  1 
ATOM   4313 C  CG  . ASP B 1 283 ? 22.759  -14.199 11.927  1.00 37.81  ? 259 ASP B CG  1 
ATOM   4314 O  OD1 . ASP B 1 283 ? 23.841  -13.767 11.472  1.00 39.40  ? 259 ASP B OD1 1 
ATOM   4315 O  OD2 . ASP B 1 283 ? 22.110  -15.119 11.384  1.00 36.08  ? 259 ASP B OD2 1 
ATOM   4316 N  N   . ASN B 1 284 ? 22.530  -13.289 16.485  1.00 31.70  ? 260 ASN B N   1 
ATOM   4317 C  CA  . ASN B 1 284 ? 21.837  -12.791 17.666  1.00 34.90  ? 260 ASN B CA  1 
ATOM   4318 C  C   . ASN B 1 284 ? 22.293  -13.588 18.877  1.00 32.87  ? 260 ASN B C   1 
ATOM   4319 O  O   . ASN B 1 284 ? 22.214  -14.819 18.877  1.00 30.53  ? 260 ASN B O   1 
ATOM   4320 C  CB  . ASN B 1 284 ? 20.316  -12.899 17.488  1.00 32.82  ? 260 ASN B CB  1 
ATOM   4321 C  CG  . ASN B 1 284 ? 19.554  -12.559 18.752  1.00 35.58  ? 260 ASN B CG  1 
ATOM   4322 O  OD1 . ASN B 1 284 ? 19.937  -11.662 19.504  1.00 36.81  ? 260 ASN B OD1 1 
ATOM   4323 N  ND2 . ASN B 1 284 ? 18.467  -13.285 18.997  1.00 32.98  ? 260 ASN B ND2 1 
ATOM   4324 N  N   . LEU B 1 285 ? 22.762  -12.885 19.904  1.00 35.49  ? 261 LEU B N   1 
ATOM   4325 C  CA  . LEU B 1 285 ? 23.243  -13.521 21.121  1.00 39.68  ? 261 LEU B CA  1 
ATOM   4326 C  C   . LEU B 1 285 ? 22.175  -13.649 22.195  1.00 40.95  ? 261 LEU B C   1 
ATOM   4327 O  O   . LEU B 1 285 ? 22.437  -14.265 23.232  1.00 38.86  ? 261 LEU B O   1 
ATOM   4328 C  CB  . LEU B 1 285 ? 24.425  -12.732 21.693  1.00 38.30  ? 261 LEU B CB  1 
ATOM   4329 C  CG  . LEU B 1 285 ? 25.675  -12.674 20.816  1.00 38.85  ? 261 LEU B CG  1 
ATOM   4330 C  CD1 . LEU B 1 285 ? 26.717  -11.749 21.427  1.00 37.18  ? 261 LEU B CD1 1 
ATOM   4331 C  CD2 . LEU B 1 285 ? 26.244  -14.072 20.609  1.00 38.15  ? 261 LEU B CD2 1 
ATOM   4332 N  N   . TRP B 1 286 ? 20.984  -13.103 21.974  1.00 40.92  ? 262 TRP B N   1 
ATOM   4333 C  CA  . TRP B 1 286 ? 19.991  -12.939 23.025  1.00 43.85  ? 262 TRP B CA  1 
ATOM   4334 C  C   . TRP B 1 286 ? 18.833  -13.905 22.837  1.00 43.00  ? 262 TRP B C   1 
ATOM   4335 O  O   . TRP B 1 286 ? 18.439  -14.213 21.708  1.00 43.67  ? 262 TRP B O   1 
ATOM   4336 C  CB  . TRP B 1 286 ? 19.487  -11.497 23.043  1.00 48.26  ? 262 TRP B CB  1 
ATOM   4337 C  CG  . TRP B 1 286 ? 20.617  -10.546 23.222  1.00 53.69  ? 262 TRP B CG  1 
ATOM   4338 C  CD1 . TRP B 1 286 ? 21.319  -9.908  22.242  1.00 54.72  ? 262 TRP B CD1 1 
ATOM   4339 C  CD2 . TRP B 1 286 ? 21.208  -10.153 24.463  1.00 59.80  ? 262 TRP B CD2 1 
ATOM   4340 N  NE1 . TRP B 1 286 ? 22.305  -9.129  22.798  1.00 62.02  ? 262 TRP B NE1 1 
ATOM   4341 C  CE2 . TRP B 1 286 ? 22.256  -9.262  24.161  1.00 63.27  ? 262 TRP B CE2 1 
ATOM   4342 C  CE3 . TRP B 1 286 ? 20.947  -10.462 25.801  1.00 60.57  ? 262 TRP B CE3 1 
ATOM   4343 C  CZ2 . TRP B 1 286 ? 23.043  -8.678  25.148  1.00 65.93  ? 262 TRP B CZ2 1 
ATOM   4344 C  CZ3 . TRP B 1 286 ? 21.728  -9.878  26.779  1.00 63.78  ? 262 TRP B CZ3 1 
ATOM   4345 C  CH2 . TRP B 1 286 ? 22.763  -8.996  26.449  1.00 64.64  ? 262 TRP B CH2 1 
ATOM   4346 N  N   . ALA B 1 287 ? 18.305  -14.395 23.958  1.00 45.99  ? 263 ALA B N   1 
ATOM   4347 C  CA  . ALA B 1 287 ? 17.110  -15.229 23.975  1.00 50.90  ? 263 ALA B CA  1 
ATOM   4348 C  C   . ALA B 1 287 ? 15.870  -14.435 24.363  1.00 58.86  ? 263 ALA B C   1 
ATOM   4349 O  O   . ALA B 1 287 ? 14.865  -14.460 23.647  1.00 67.19  ? 263 ALA B O   1 
ATOM   4350 C  CB  . ALA B 1 287 ? 17.304  -16.405 24.941  1.00 46.42  ? 263 ALA B CB  1 
ATOM   4351 N  N   . GLY B 1 288 ? 15.926  -13.726 25.486  1.00 60.32  ? 264 GLY B N   1 
ATOM   4352 C  CA  . GLY B 1 288 ? 14.843  -12.863 25.905  1.00 69.97  ? 264 GLY B CA  1 
ATOM   4353 C  C   . GLY B 1 288 ? 15.363  -11.553 26.453  1.00 78.94  ? 264 GLY B C   1 
ATOM   4354 O  O   . GLY B 1 288 ? 16.311  -10.982 25.904  1.00 77.74  ? 264 GLY B O   1 
ATOM   4355 N  N   . LYS B 1 289 ? 14.765  -11.066 27.536  1.00 84.32  ? 265 LYS B N   1 
ATOM   4356 C  CA  . LYS B 1 289 ? 15.165  -9.794  28.128  1.00 85.03  ? 265 LYS B CA  1 
ATOM   4357 C  C   . LYS B 1 289 ? 16.332  -10.039 29.079  1.00 84.57  ? 265 LYS B C   1 
ATOM   4358 O  O   . LYS B 1 289 ? 16.176  -10.710 30.104  1.00 87.81  ? 265 LYS B O   1 
ATOM   4359 C  CB  . LYS B 1 289 ? 13.989  -9.142  28.848  1.00 88.74  ? 265 LYS B CB  1 
ATOM   4360 C  CG  . LYS B 1 289 ? 14.155  -7.637  29.034  1.00 86.66  ? 265 LYS B CG  1 
ATOM   4361 C  CD  . LYS B 1 289 ? 12.921  -6.991  29.649  1.00 87.68  ? 265 LYS B CD  1 
ATOM   4362 C  CE  . LYS B 1 289 ? 11.705  -7.115  28.741  1.00 93.80  ? 265 LYS B CE  1 
ATOM   4363 N  NZ  . LYS B 1 289 ? 10.532  -6.357  29.258  1.00 94.25  ? 265 LYS B NZ  1 
ATOM   4364 N  N   . GLY B 1 290 ? 17.500  -9.495  28.741  1.00 79.80  ? 266 GLY B N   1 
ATOM   4365 C  CA  . GLY B 1 290 ? 18.694  -9.673  29.544  1.00 76.61  ? 266 GLY B CA  1 
ATOM   4366 C  C   . GLY B 1 290 ? 19.153  -11.113 29.638  1.00 75.78  ? 266 GLY B C   1 
ATOM   4367 O  O   . GLY B 1 290 ? 19.985  -11.447 30.486  1.00 75.62  ? 266 GLY B O   1 
ATOM   4368 N  N   . ARG B 1 291 ? 18.633  -11.976 28.771  1.00 66.54  ? 267 ARG B N   1 
ATOM   4369 C  CA  . ARG B 1 291 ? 18.944  -13.400 28.791  1.00 58.86  ? 267 ARG B CA  1 
ATOM   4370 C  C   . ARG B 1 291 ? 19.698  -13.765 27.519  1.00 50.41  ? 267 ARG B C   1 
ATOM   4371 O  O   . ARG B 1 291 ? 19.177  -13.592 26.412  1.00 47.73  ? 267 ARG B O   1 
ATOM   4372 C  CB  . ARG B 1 291 ? 17.669  -14.232 28.925  1.00 58.67  ? 267 ARG B CB  1 
ATOM   4373 C  CG  . ARG B 1 291 ? 17.917  -15.706 29.213  1.00 53.77  ? 267 ARG B CG  1 
ATOM   4374 C  CD  . ARG B 1 291 ? 16.729  -16.357 29.914  1.00 56.78  ? 267 ARG B CD  1 
ATOM   4375 N  NE  . ARG B 1 291 ? 16.499  -15.787 31.238  1.00 56.45  ? 267 ARG B NE  1 
ATOM   4376 C  CZ  . ARG B 1 291 ? 15.568  -14.886 31.531  1.00 59.45  ? 267 ARG B CZ  1 
ATOM   4377 N  NH1 . ARG B 1 291 ? 14.720  -14.439 30.617  1.00 56.13  ? 267 ARG B NH1 1 
ATOM   4378 N  NH2 . ARG B 1 291 ? 15.487  -14.420 32.774  1.00 59.04  ? 267 ARG B NH2 1 
ATOM   4379 N  N   . LEU B 1 292 ? 20.923  -14.254 27.680  1.00 47.88  ? 268 LEU B N   1 
ATOM   4380 C  CA  . LEU B 1 292 ? 21.694  -14.738 26.545  1.00 45.89  ? 268 LEU B CA  1 
ATOM   4381 C  C   . LEU B 1 292 ? 21.173  -16.090 26.072  1.00 42.40  ? 268 LEU B C   1 
ATOM   4382 O  O   . LEU B 1 292 ? 20.767  -16.935 26.876  1.00 38.75  ? 268 LEU B O   1 
ATOM   4383 C  CB  . LEU B 1 292 ? 23.170  -14.867 26.919  1.00 41.84  ? 268 LEU B CB  1 
ATOM   4384 C  CG  . LEU B 1 292 ? 23.957  -13.583 27.172  1.00 43.43  ? 268 LEU B CG  1 
ATOM   4385 C  CD1 . LEU B 1 292 ? 25.323  -13.924 27.741  1.00 42.29  ? 268 LEU B CD1 1 
ATOM   4386 C  CD2 . LEU B 1 292 ? 24.100  -12.776 25.894  1.00 46.18  ? 268 LEU B CD2 1 
ATOM   4387 N  N   . ALA B 1 293 ? 21.185  -16.289 24.756  1.00 38.71  ? 269 ALA B N   1 
ATOM   4388 C  CA  . ALA B 1 293 ? 20.920  -17.608 24.199  1.00 38.68  ? 269 ALA B CA  1 
ATOM   4389 C  C   . ALA B 1 293 ? 22.082  -18.536 24.525  1.00 38.50  ? 269 ALA B C   1 
ATOM   4390 O  O   . ALA B 1 293 ? 23.249  -18.172 24.342  1.00 36.64  ? 269 ALA B O   1 
ATOM   4391 C  CB  . ALA B 1 293 ? 20.717  -17.519 22.688  1.00 37.29  ? 269 ALA B CB  1 
ATOM   4392 N  N   . GLU B 1 294 ? 21.766  -19.737 25.006  1.00 36.04  ? 270 GLU B N   1 
ATOM   4393 C  CA  . GLU B 1 294 ? 22.802  -20.665 25.441  1.00 39.21  ? 270 GLU B CA  1 
ATOM   4394 C  C   . GLU B 1 294 ? 23.234  -21.635 24.348  1.00 36.51  ? 270 GLU B C   1 
ATOM   4395 O  O   . GLU B 1 294 ? 24.377  -22.107 24.374  1.00 39.30  ? 270 GLU B O   1 
ATOM   4396 C  CB  . GLU B 1 294 ? 22.320  -21.441 26.669  1.00 39.32  ? 270 GLU B CB  1 
ATOM   4397 C  CG  . GLU B 1 294 ? 21.917  -20.533 27.823  1.00 42.75  ? 270 GLU B CG  1 
ATOM   4398 C  CD  . GLU B 1 294 ? 21.658  -21.287 29.111  1.00 46.95  ? 270 GLU B CD  1 
ATOM   4399 O  OE1 . GLU B 1 294 ? 22.218  -22.389 29.282  1.00 50.80  ? 270 GLU B OE1 1 
ATOM   4400 O  OE2 . GLU B 1 294 ? 20.893  -20.775 29.955  1.00 50.69  ? 270 GLU B OE2 1 
ATOM   4401 N  N   . THR B 1 295 ? 22.362  -21.946 23.390  1.00 37.63  ? 271 THR B N   1 
ATOM   4402 C  CA  . THR B 1 295 ? 22.735  -22.791 22.266  1.00 36.49  ? 271 THR B CA  1 
ATOM   4403 C  C   . THR B 1 295 ? 22.124  -22.252 20.983  1.00 36.37  ? 271 THR B C   1 
ATOM   4404 O  O   . THR B 1 295 ? 21.145  -21.500 20.995  1.00 35.63  ? 271 THR B O   1 
ATOM   4405 C  CB  . THR B 1 295 ? 22.279  -24.247 22.434  1.00 37.28  ? 271 THR B CB  1 
ATOM   4406 O  OG1 . THR B 1 295 ? 20.848  -24.296 22.520  1.00 39.83  ? 271 THR B OG1 1 
ATOM   4407 C  CG2 . THR B 1 295 ? 22.896  -24.873 23.673  1.00 35.47  ? 271 THR B CG2 1 
ATOM   4408 N  N   . ASN B 1 296 ? 22.727  -22.665 19.868  1.00 36.71  ? 272 ASN B N   1 
ATOM   4409 C  CA  . ASN B 1 296 ? 22.114  -22.455 18.564  1.00 34.33  ? 272 ASN B CA  1 
ATOM   4410 C  C   . ASN B 1 296 ? 20.825  -23.256 18.427  1.00 32.81  ? 272 ASN B C   1 
ATOM   4411 O  O   . ASN B 1 296 ? 19.834  -22.761 17.876  1.00 33.98  ? 272 ASN B O   1 
ATOM   4412 C  CB  . ASN B 1 296 ? 23.101  -22.846 17.465  1.00 32.73  ? 272 ASN B CB  1 
ATOM   4413 C  CG  . ASN B 1 296 ? 24.125  -21.769 17.193  1.00 30.04  ? 272 ASN B CG  1 
ATOM   4414 O  OD1 . ASN B 1 296 ? 23.858  -20.817 16.464  1.00 32.32  ? 272 ASN B OD1 1 
ATOM   4415 N  ND2 . ASN B 1 296 ? 25.309  -21.915 17.776  1.00 30.20  ? 272 ASN B ND2 1 
ATOM   4416 N  N   . ALA B 1 297 ? 20.821  -24.500 18.914  1.00 31.59  ? 273 ALA B N   1 
ATOM   4417 C  CA  . ALA B 1 297 ? 19.628  -25.334 18.820  1.00 36.54  ? 273 ALA B CA  1 
ATOM   4418 C  C   . ALA B 1 297 ? 18.422  -24.641 19.434  1.00 36.74  ? 273 ALA B C   1 
ATOM   4419 O  O   . ALA B 1 297 ? 17.291  -24.822 18.969  1.00 34.62  ? 273 ALA B O   1 
ATOM   4420 C  CB  . ALA B 1 297 ? 19.878  -26.675 19.512  1.00 36.59  ? 273 ALA B CB  1 
ATOM   4421 N  N   . GLN B 1 298 ? 18.651  -23.835 20.470  1.00 36.38  ? 274 GLN B N   1 
ATOM   4422 C  CA  . GLN B 1 298 ? 17.565  -23.131 21.142  1.00 37.34  ? 274 GLN B CA  1 
ATOM   4423 C  C   . GLN B 1 298 ? 16.866  -22.159 20.198  1.00 33.85  ? 274 GLN B C   1 
ATOM   4424 O  O   . GLN B 1 298 ? 15.632  -22.057 20.201  1.00 34.49  ? 274 GLN B O   1 
ATOM   4425 C  CB  . GLN B 1 298 ? 18.138  -22.418 22.368  1.00 37.29  ? 274 GLN B CB  1 
ATOM   4426 C  CG  . GLN B 1 298 ? 17.344  -21.257 22.919  1.00 44.24  ? 274 GLN B CG  1 
ATOM   4427 C  CD  . GLN B 1 298 ? 18.070  -20.605 24.080  1.00 42.36  ? 274 GLN B CD  1 
ATOM   4428 O  OE1 . GLN B 1 298 ? 19.184  -21.001 24.427  1.00 37.49  ? 274 GLN B OE1 1 
ATOM   4429 N  NE2 . GLN B 1 298 ? 17.447  -19.602 24.683  1.00 43.20  ? 274 GLN B NE2 1 
ATOM   4430 N  N   . GLN B 1 299 ? 17.633  -21.443 19.374  1.00 29.91  ? 275 GLN B N   1 
ATOM   4431 C  CA  . GLN B 1 299 ? 17.023  -20.545 18.401  1.00 32.45  ? 275 GLN B CA  1 
ATOM   4432 C  C   . GLN B 1 299 ? 16.355  -21.318 17.270  1.00 33.10  ? 275 GLN B C   1 
ATOM   4433 O  O   . GLN B 1 299 ? 15.330  -20.874 16.738  1.00 31.63  ? 275 GLN B O   1 
ATOM   4434 C  CB  . GLN B 1 299 ? 18.072  -19.580 17.850  1.00 31.53  ? 275 GLN B CB  1 
ATOM   4435 C  CG  . GLN B 1 299 ? 18.664  -18.663 18.912  1.00 29.92  ? 275 GLN B CG  1 
ATOM   4436 C  CD  . GLN B 1 299 ? 19.652  -17.659 18.347  1.00 33.91  ? 275 GLN B CD  1 
ATOM   4437 O  OE1 . GLN B 1 299 ? 20.093  -17.780 17.206  1.00 32.73  ? 275 GLN B OE1 1 
ATOM   4438 N  NE2 . GLN B 1 299 ? 20.002  -16.659 19.148  1.00 31.66  ? 275 GLN B NE2 1 
ATOM   4439 N  N   . VAL B 1 300 ? 16.910  -22.473 16.894  1.00 30.72  ? 276 VAL B N   1 
ATOM   4440 C  CA  . VAL B 1 300 ? 16.266  -23.307 15.885  1.00 30.74  ? 276 VAL B CA  1 
ATOM   4441 C  C   . VAL B 1 300 ? 14.912  -23.796 16.387  1.00 30.06  ? 276 VAL B C   1 
ATOM   4442 O  O   . VAL B 1 300 ? 13.914  -23.761 15.657  1.00 28.44  ? 276 VAL B O   1 
ATOM   4443 C  CB  . VAL B 1 300 ? 17.184  -24.480 15.495  1.00 29.58  ? 276 VAL B CB  1 
ATOM   4444 C  CG1 . VAL B 1 300 ? 16.443  -25.475 14.615  1.00 30.57  ? 276 VAL B CG1 1 
ATOM   4445 C  CG2 . VAL B 1 300 ? 18.427  -23.965 14.780  1.00 30.48  ? 276 VAL B CG2 1 
ATOM   4446 N  N   . ARG B 1 301 ? 14.854  -24.256 17.640  1.00 31.07  ? 277 ARG B N   1 
ATOM   4447 C  CA  . ARG B 1 301 ? 13.586  -24.720 18.199  1.00 32.10  ? 277 ARG B CA  1 
ATOM   4448 C  C   . ARG B 1 301 ? 12.534  -23.616 18.178  1.00 30.28  ? 277 ARG B C   1 
ATOM   4449 O  O   . ARG B 1 301 ? 11.355  -23.876 17.905  1.00 32.76  ? 277 ARG B O   1 
ATOM   4450 C  CB  . ARG B 1 301 ? 13.794  -25.232 19.628  1.00 33.20  ? 277 ARG B CB  1 
ATOM   4451 C  CG  . ARG B 1 301 ? 14.586  -26.536 19.716  1.00 40.12  ? 277 ARG B CG  1 
ATOM   4452 C  CD  . ARG B 1 301 ? 14.483  -27.177 21.098  1.00 45.28  ? 277 ARG B CD  1 
ATOM   4453 N  NE  . ARG B 1 301 ? 15.129  -26.383 22.139  1.00 45.89  ? 277 ARG B NE  1 
ATOM   4454 C  CZ  . ARG B 1 301 ? 16.398  -26.508 22.507  1.00 46.05  ? 277 ARG B CZ  1 
ATOM   4455 N  NH1 . ARG B 1 301 ? 17.208  -27.379 21.924  1.00 43.75  ? 277 ARG B NH1 1 
ATOM   4456 N  NH2 . ARG B 1 301 ? 16.868  -25.741 23.486  1.00 47.63  ? 277 ARG B NH2 1 
ATOM   4457 N  N   . ALA B 1 302 ? 12.935  -22.377 18.468  1.00 28.24  ? 278 ALA B N   1 
ATOM   4458 C  CA  . ALA B 1 302 ? 11.979  -21.276 18.459  1.00 32.33  ? 278 ALA B CA  1 
ATOM   4459 C  C   . ALA B 1 302 ? 11.420  -21.056 17.058  1.00 32.64  ? 278 ALA B C   1 
ATOM   4460 O  O   . ALA B 1 302 ? 10.201  -21.007 16.863  1.00 32.13  ? 278 ALA B O   1 
ATOM   4461 C  CB  . ALA B 1 302 ? 12.638  -20.000 18.984  1.00 29.94  ? 278 ALA B CB  1 
ATOM   4462 N  N   . ALA B 1 303 ? 12.305  -20.920 16.067  1.00 29.07  ? 279 ALA B N   1 
ATOM   4463 C  CA  . ALA B 1 303 ? 11.849  -20.764 14.691  1.00 29.80  ? 279 ALA B CA  1 
ATOM   4464 C  C   . ALA B 1 303 ? 10.961  -21.928 14.276  1.00 30.03  ? 279 ALA B C   1 
ATOM   4465 O  O   . ALA B 1 303 ? 9.966   -21.740 13.567  1.00 30.47  ? 279 ALA B O   1 
ATOM   4466 C  CB  . ALA B 1 303 ? 13.049  -20.646 13.751  1.00 28.24  ? 279 ALA B CB  1 
ATOM   4467 N  N   . ARG B 1 304 ? 11.305  -23.140 14.712  1.00 29.64  ? 280 ARG B N   1 
ATOM   4468 C  CA  . ARG B 1 304 ? 10.503  -24.309 14.370  1.00 32.13  ? 280 ARG B CA  1 
ATOM   4469 C  C   . ARG B 1 304 ? 9.111   -24.225 14.986  1.00 31.55  ? 280 ARG B C   1 
ATOM   4470 O  O   . ARG B 1 304 ? 8.114   -24.568 14.338  1.00 33.01  ? 280 ARG B O   1 
ATOM   4471 C  CB  . ARG B 1 304 ? 11.221  -25.576 14.830  1.00 32.55  ? 280 ARG B CB  1 
ATOM   4472 C  CG  . ARG B 1 304 ? 10.436  -26.851 14.608  1.00 36.74  ? 280 ARG B CG  1 
ATOM   4473 C  CD  . ARG B 1 304 ? 11.315  -28.072 14.803  1.00 38.53  ? 280 ARG B CD  1 
ATOM   4474 N  NE  . ARG B 1 304 ? 10.702  -29.265 14.237  1.00 43.06  ? 280 ARG B NE  1 
ATOM   4475 C  CZ  . ARG B 1 304 ? 11.369  -30.357 13.890  1.00 46.29  ? 280 ARG B CZ  1 
ATOM   4476 N  NH1 . ARG B 1 304 ? 12.678  -30.450 14.057  1.00 45.94  ? 280 ARG B NH1 1 
ATOM   4477 N  NH2 . ARG B 1 304 ? 10.706  -31.378 13.353  1.00 51.42  ? 280 ARG B NH2 1 
ATOM   4478 N  N   . GLN B 1 305 ? 9.021   -23.773 16.239  1.00 29.61  ? 281 GLN B N   1 
ATOM   4479 C  CA  . GLN B 1 305 ? 7.715   -23.588 16.865  1.00 32.55  ? 281 GLN B CA  1 
ATOM   4480 C  C   . GLN B 1 305 ? 6.852   -22.622 16.061  1.00 33.13  ? 281 GLN B C   1 
ATOM   4481 O  O   . GLN B 1 305 ? 5.651   -22.854 15.874  1.00 34.32  ? 281 GLN B O   1 
ATOM   4482 C  CB  . GLN B 1 305 ? 7.893   -23.086 18.298  1.00 32.83  ? 281 GLN B CB  1 
ATOM   4483 C  CG  . GLN B 1 305 ? 6.643   -23.198 19.154  1.00 41.43  ? 281 GLN B CG  1 
ATOM   4484 C  CD  . GLN B 1 305 ? 6.882   -22.785 20.593  1.00 42.56  ? 281 GLN B CD  1 
ATOM   4485 O  OE1 . GLN B 1 305 ? 7.900   -23.135 21.192  1.00 47.78  ? 281 GLN B OE1 1 
ATOM   4486 N  NE2 . GLN B 1 305 ? 5.946   -22.028 21.153  1.00 38.88  ? 281 GLN B NE2 1 
ATOM   4487 N  N   . ILE B 1 306 ? 7.449   -21.532 15.572  1.00 30.60  ? 282 ILE B N   1 
ATOM   4488 C  CA  . ILE B 1 306 ? 6.716   -20.589 14.730  1.00 30.73  ? 282 ILE B CA  1 
ATOM   4489 C  C   . ILE B 1 306 ? 6.275   -21.267 13.438  1.00 30.57  ? 282 ILE B C   1 
ATOM   4490 O  O   . ILE B 1 306 ? 5.111   -21.175 13.030  1.00 30.86  ? 282 ILE B O   1 
ATOM   4491 C  CB  . ILE B 1 306 ? 7.582   -19.348 14.443  1.00 30.37  ? 282 ILE B CB  1 
ATOM   4492 C  CG1 . ILE B 1 306 ? 7.852   -18.574 15.736  1.00 30.23  ? 282 ILE B CG1 1 
ATOM   4493 C  CG2 . ILE B 1 306 ? 6.912   -18.453 13.400  1.00 30.61  ? 282 ILE B CG2 1 
ATOM   4494 C  CD1 . ILE B 1 306 ? 8.938   -17.524 15.604  1.00 30.01  ? 282 ILE B CD1 1 
ATOM   4495 N  N   . VAL B 1 307 ? 7.206   -21.951 12.771  1.00 30.57  ? 283 VAL B N   1 
ATOM   4496 C  CA  . VAL B 1 307 ? 6.898   -22.600 11.498  1.00 32.14  ? 283 VAL B CA  1 
ATOM   4497 C  C   . VAL B 1 307 ? 5.733   -23.569 11.662  1.00 32.86  ? 283 VAL B C   1 
ATOM   4498 O  O   . VAL B 1 307 ? 4.793   -23.585 10.858  1.00 32.34  ? 283 VAL B O   1 
ATOM   4499 C  CB  . VAL B 1 307 ? 8.149   -23.311 10.950  1.00 34.91  ? 283 VAL B CB  1 
ATOM   4500 C  CG1 . VAL B 1 307 ? 7.777   -24.274 9.828   1.00 31.45  ? 283 VAL B CG1 1 
ATOM   4501 C  CG2 . VAL B 1 307 ? 9.171   -22.291 10.462  1.00 31.57  ? 283 VAL B CG2 1 
ATOM   4502 N  N   . GLU B 1 308 ? 5.781   -24.400 12.702  1.00 31.80  ? 284 GLU B N   1 
ATOM   4503 C  CA  . GLU B 1 308 ? 4.747   -25.412 12.885  1.00 34.34  ? 284 GLU B CA  1 
ATOM   4504 C  C   . GLU B 1 308 ? 3.451   -24.814 13.416  1.00 35.67  ? 284 GLU B C   1 
ATOM   4505 O  O   . GLU B 1 308 ? 2.367   -25.297 13.070  1.00 32.77  ? 284 GLU B O   1 
ATOM   4506 C  CB  . GLU B 1 308 ? 5.266   -26.513 13.809  1.00 35.04  ? 284 GLU B CB  1 
ATOM   4507 C  CG  . GLU B 1 308 ? 6.384   -27.329 13.163  1.00 38.01  ? 284 GLU B CG  1 
ATOM   4508 C  CD  . GLU B 1 308 ? 7.059   -28.295 14.116  1.00 39.32  ? 284 GLU B CD  1 
ATOM   4509 O  OE1 . GLU B 1 308 ? 6.641   -28.382 15.289  1.00 39.11  ? 284 GLU B OE1 1 
ATOM   4510 O  OE2 . GLU B 1 308 ? 8.018   -28.968 13.682  1.00 38.90  ? 284 GLU B OE2 1 
ATOM   4511 N  N   . GLY B 1 309 ? 3.534   -23.768 14.240  1.00 33.71  ? 285 GLY B N   1 
ATOM   4512 C  CA  . GLY B 1 309 ? 2.329   -23.053 14.622  1.00 33.15  ? 285 GLY B CA  1 
ATOM   4513 C  C   . GLY B 1 309 ? 1.577   -22.511 13.423  1.00 35.48  ? 285 GLY B C   1 
ATOM   4514 O  O   . GLY B 1 309 ? 0.345   -22.451 13.431  1.00 35.40  ? 285 GLY B O   1 
ATOM   4515 N  N   . LEU B 1 310 ? 2.305   -22.117 12.376  1.00 33.92  ? 286 LEU B N   1 
ATOM   4516 C  CA  . LEU B 1 310 ? 1.692   -21.647 11.139  1.00 33.76  ? 286 LEU B CA  1 
ATOM   4517 C  C   . LEU B 1 310 ? 1.057   -22.767 10.327  1.00 33.71  ? 286 LEU B C   1 
ATOM   4518 O  O   . LEU B 1 310 ? 0.427   -22.482 9.302   1.00 33.69  ? 286 LEU B O   1 
ATOM   4519 C  CB  . LEU B 1 310 ? 2.739   -20.941 10.274  1.00 30.21  ? 286 LEU B CB  1 
ATOM   4520 C  CG  . LEU B 1 310 ? 3.067   -19.482 10.592  1.00 31.81  ? 286 LEU B CG  1 
ATOM   4521 C  CD1 . LEU B 1 310 ? 4.321   -19.062 9.847   1.00 30.91  ? 286 LEU B CD1 1 
ATOM   4522 C  CD2 . LEU B 1 310 ? 1.901   -18.574 10.224  1.00 30.67  ? 286 LEU B CD2 1 
ATOM   4523 N  N   . GLY B 1 311 ? 1.210   -24.021 10.744  1.00 35.01  ? 287 GLY B N   1 
ATOM   4524 C  CA  . GLY B 1 311 ? 0.728   -25.132 9.948   1.00 35.59  ? 287 GLY B CA  1 
ATOM   4525 C  C   . GLY B 1 311 ? 1.664   -25.563 8.844   1.00 35.92  ? 287 GLY B C   1 
ATOM   4526 O  O   . GLY B 1 311 ? 1.242   -26.284 7.935   1.00 38.53  ? 287 GLY B O   1 
ATOM   4527 N  N   . LEU B 1 312 ? 2.924   -25.140 8.893   1.00 33.90  ? 288 LEU B N   1 
ATOM   4528 C  CA  . LEU B 1 312 ? 3.933   -25.524 7.922   1.00 37.54  ? 288 LEU B CA  1 
ATOM   4529 C  C   . LEU B 1 312 ? 4.851   -26.576 8.539   1.00 36.56  ? 288 LEU B C   1 
ATOM   4530 O  O   . LEU B 1 312 ? 4.720   -26.947 9.707   1.00 39.19  ? 288 LEU B O   1 
ATOM   4531 C  CB  . LEU B 1 312 ? 4.727   -24.300 7.461   1.00 35.11  ? 288 LEU B CB  1 
ATOM   4532 C  CG  . LEU B 1 312 ? 3.911   -23.133 6.897   1.00 37.32  ? 288 LEU B CG  1 
ATOM   4533 C  CD1 . LEU B 1 312 ? 4.801   -21.920 6.688   1.00 33.64  ? 288 LEU B CD1 1 
ATOM   4534 C  CD2 . LEU B 1 312 ? 3.232   -23.527 5.595   1.00 39.58  ? 288 LEU B CD2 1 
ATOM   4535 N  N   . GLU B 1 313 ? 5.797   -27.059 7.739   1.00 36.81  ? 289 GLU B N   1 
ATOM   4536 C  CA  . GLU B 1 313 ? 6.761   -28.053 8.183   1.00 39.43  ? 289 GLU B CA  1 
ATOM   4537 C  C   . GLU B 1 313 ? 8.171   -27.561 7.893   1.00 38.21  ? 289 GLU B C   1 
ATOM   4538 O  O   . GLU B 1 313 ? 8.406   -26.819 6.936   1.00 36.44  ? 289 GLU B O   1 
ATOM   4539 C  CB  . GLU B 1 313 ? 6.523   -29.409 7.502   1.00 41.19  ? 289 GLU B CB  1 
ATOM   4540 C  CG  . GLU B 1 313 ? 5.149   -30.002 7.788   1.00 46.41  ? 289 GLU B CG  1 
ATOM   4541 C  CD  . GLU B 1 313 ? 4.983   -31.403 7.233   1.00 60.45  ? 289 GLU B CD  1 
ATOM   4542 O  OE1 . GLU B 1 313 ? 5.504   -32.355 7.852   1.00 62.06  ? 289 GLU B OE1 1 
ATOM   4543 O  OE2 . GLU B 1 313 ? 4.333   -31.551 6.176   1.00 65.18  ? 289 GLU B OE2 1 
ATOM   4544 N  N   . VAL B 1 314 ? 9.106   -27.976 8.741   1.00 36.43  ? 290 VAL B N   1 
ATOM   4545 C  CA  . VAL B 1 314 ? 10.511  -27.634 8.561   1.00 39.14  ? 290 VAL B CA  1 
ATOM   4546 C  C   . VAL B 1 314 ? 11.109  -28.536 7.491   1.00 37.41  ? 290 VAL B C   1 
ATOM   4547 O  O   . VAL B 1 314 ? 10.850  -29.744 7.458   1.00 38.38  ? 290 VAL B O   1 
ATOM   4548 C  CB  . VAL B 1 314 ? 11.271  -27.761 9.894   1.00 39.28  ? 290 VAL B CB  1 
ATOM   4549 C  CG1 . VAL B 1 314 ? 12.763  -27.557 9.681   1.00 39.90  ? 290 VAL B CG1 1 
ATOM   4550 C  CG2 . VAL B 1 314 ? 10.732  -26.761 10.906  1.00 36.70  ? 290 VAL B CG2 1 
ATOM   4551 N  N   . ALA B 1 315 ? 11.910  -27.949 6.608   1.00 38.77  ? 291 ALA B N   1 
ATOM   4552 C  CA  . ALA B 1 315 ? 12.529  -28.718 5.538   1.00 37.86  ? 291 ALA B CA  1 
ATOM   4553 C  C   . ALA B 1 315 ? 13.651  -29.595 6.076   1.00 39.35  ? 291 ALA B C   1 
ATOM   4554 O  O   . ALA B 1 315 ? 14.466  -29.158 6.895   1.00 37.22  ? 291 ALA B O   1 
ATOM   4555 C  CB  . ALA B 1 315 ? 13.078  -27.784 4.460   1.00 37.07  ? 291 ALA B CB  1 
ATOM   4556 N  N   . THR B 1 316 ? 13.686  -30.845 5.612   1.00 37.34  ? 292 THR B N   1 
ATOM   4557 C  CA  . THR B 1 316 ? 14.827  -31.709 5.848   1.00 39.13  ? 292 THR B CA  1 
ATOM   4558 C  C   . THR B 1 316 ? 15.988  -31.264 4.966   1.00 40.71  ? 292 THR B C   1 
ATOM   4559 O  O   . THR B 1 316 ? 15.804  -30.494 4.021   1.00 38.84  ? 292 THR B O   1 
ATOM   4560 C  CB  . THR B 1 316 ? 14.480  -33.165 5.541   1.00 42.21  ? 292 THR B CB  1 
ATOM   4561 O  OG1 . THR B 1 316 ? 14.191  -33.301 4.142   1.00 41.31  ? 292 THR B OG1 1 
ATOM   4562 C  CG2 . THR B 1 316 ? 13.280  -33.631 6.357   1.00 38.97  ? 292 THR B CG2 1 
ATOM   4563 N  N   . PRO B 1 317 ? 17.204  -31.735 5.250   1.00 37.35  ? 293 PRO B N   1 
ATOM   4564 C  CA  . PRO B 1 317 ? 18.311  -31.451 4.323   1.00 41.26  ? 293 PRO B CA  1 
ATOM   4565 C  C   . PRO B 1 317 ? 18.023  -31.911 2.904   1.00 42.21  ? 293 PRO B C   1 
ATOM   4566 O  O   . PRO B 1 317 ? 18.405  -31.229 1.946   1.00 40.72  ? 293 PRO B O   1 
ATOM   4567 C  CB  . PRO B 1 317 ? 19.490  -32.208 4.948   1.00 41.63  ? 293 PRO B CB  1 
ATOM   4568 C  CG  . PRO B 1 317 ? 19.162  -32.277 6.398   1.00 41.43  ? 293 PRO B CG  1 
ATOM   4569 C  CD  . PRO B 1 317 ? 17.667  -32.422 6.469   1.00 39.12  ? 293 PRO B CD  1 
ATOM   4570 N  N   . ALA B 1 318 ? 17.345  -33.050 2.742   1.00 41.45  ? 294 ALA B N   1 
ATOM   4571 C  CA  . ALA B 1 318 ? 17.035  -33.543 1.405   1.00 41.57  ? 294 ALA B CA  1 
ATOM   4572 C  C   . ALA B 1 318 ? 16.042  -32.638 0.690   1.00 40.68  ? 294 ALA B C   1 
ATOM   4573 O  O   . ALA B 1 318 ? 16.122  -32.475 -0.532  1.00 43.58  ? 294 ALA B O   1 
ATOM   4574 C  CB  . ALA B 1 318 ? 16.488  -34.968 1.483   1.00 45.64  ? 294 ALA B CB  1 
ATOM   4575 N  N   . GLU B 1 319 ? 15.101  -32.050 1.424   1.00 38.49  ? 295 GLU B N   1 
ATOM   4576 C  CA  . GLU B 1 319 ? 14.155  -31.131 0.806   1.00 40.95  ? 295 GLU B CA  1 
ATOM   4577 C  C   . GLU B 1 319 ? 14.800  -29.787 0.498   1.00 42.14  ? 295 GLU B C   1 
ATOM   4578 O  O   . GLU B 1 319 ? 14.447  -29.151 -0.500  1.00 41.20  ? 295 GLU B O   1 
ATOM   4579 C  CB  . GLU B 1 319 ? 12.938  -30.956 1.714   1.00 42.89  ? 295 GLU B CB  1 
ATOM   4580 C  CG  . GLU B 1 319 ? 12.127  -32.237 1.873   1.00 46.93  ? 295 GLU B CG  1 
ATOM   4581 C  CD  . GLU B 1 319 ? 11.150  -32.184 3.033   1.00 47.74  ? 295 GLU B CD  1 
ATOM   4582 O  OE1 . GLU B 1 319 ? 11.406  -31.435 3.999   1.00 47.37  ? 295 GLU B OE1 1 
ATOM   4583 O  OE2 . GLU B 1 319 ? 10.125  -32.894 2.980   1.00 53.68  ? 295 GLU B OE2 1 
ATOM   4584 N  N   . ALA B 1 320 ? 15.746  -29.347 1.331   1.00 39.39  ? 296 ALA B N   1 
ATOM   4585 C  CA  . ALA B 1 320 ? 16.495  -28.136 1.017   1.00 40.39  ? 296 ALA B CA  1 
ATOM   4586 C  C   . ALA B 1 320 ? 17.314  -28.315 -0.255  1.00 38.63  ? 296 ALA B C   1 
ATOM   4587 O  O   . ALA B 1 320 ? 17.354  -27.423 -1.110  1.00 37.97  ? 296 ALA B O   1 
ATOM   4588 C  CB  . ALA B 1 320 ? 17.401  -27.760 2.189   1.00 37.23  ? 296 ALA B CB  1 
ATOM   4589 N  N   . ARG B 1 321 ? 17.971  -29.468 -0.401  1.00 39.96  ? 297 ARG B N   1 
ATOM   4590 C  CA  . ARG B 1 321 ? 18.782  -29.709 -1.590  1.00 40.39  ? 297 ARG B CA  1 
ATOM   4591 C  C   . ARG B 1 321 ? 17.947  -29.645 -2.862  1.00 40.26  ? 297 ARG B C   1 
ATOM   4592 O  O   . ARG B 1 321 ? 18.440  -29.201 -3.906  1.00 41.38  ? 297 ARG B O   1 
ATOM   4593 C  CB  . ARG B 1 321 ? 19.484  -31.064 -1.475  1.00 38.43  ? 297 ARG B CB  1 
ATOM   4594 C  CG  . ARG B 1 321 ? 20.557  -31.091 -0.400  1.00 37.72  ? 297 ARG B CG  1 
ATOM   4595 C  CD  . ARG B 1 321 ? 21.348  -32.387 -0.395  1.00 40.21  ? 297 ARG B CD  1 
ATOM   4596 N  NE  . ARG B 1 321 ? 22.498  -32.289 0.496   1.00 38.71  ? 297 ARG B NE  1 
ATOM   4597 C  CZ  . ARG B 1 321 ? 22.523  -32.701 1.758   1.00 41.19  ? 297 ARG B CZ  1 
ATOM   4598 N  NH1 . ARG B 1 321 ? 21.495  -33.334 2.303   1.00 40.02  ? 297 ARG B NH1 1 
ATOM   4599 N  NH2 . ARG B 1 321 ? 23.609  -32.474 2.491   1.00 37.72  ? 297 ARG B NH2 1 
ATOM   4600 N  N   . GLU B 1 322 ? 16.686  -30.075 -2.798  1.00 40.73  ? 298 GLU B N   1 
ATOM   4601 C  CA  . GLU B 1 322 ? 15.818  -30.015 -3.969  1.00 43.65  ? 298 GLU B CA  1 
ATOM   4602 C  C   . GLU B 1 322 ? 15.341  -28.591 -4.232  1.00 41.58  ? 298 GLU B C   1 
ATOM   4603 O  O   . GLU B 1 322 ? 15.324  -28.141 -5.384  1.00 40.31  ? 298 GLU B O   1 
ATOM   4604 C  CB  . GLU B 1 322 ? 14.626  -30.957 -3.780  1.00 50.83  ? 298 GLU B CB  1 
ATOM   4605 C  CG  . GLU B 1 322 ? 13.789  -31.174 -5.031  1.00 60.87  ? 298 GLU B CG  1 
ATOM   4606 C  CD  . GLU B 1 322 ? 12.768  -32.281 -4.859  1.00 69.81  ? 298 GLU B CD  1 
ATOM   4607 O  OE1 . GLU B 1 322 ? 13.025  -33.207 -4.060  1.00 67.14  ? 298 GLU B OE1 1 
ATOM   4608 O  OE2 . GLU B 1 322 ? 11.707  -32.221 -5.516  1.00 73.65  ? 298 GLU B OE2 1 
ATOM   4609 N  N   . LEU B 1 323 ? 14.957  -27.868 -3.179  1.00 40.27  ? 299 LEU B N   1 
ATOM   4610 C  CA  . LEU B 1 323 ? 14.505  -26.493 -3.352  1.00 41.22  ? 299 LEU B CA  1 
ATOM   4611 C  C   . LEU B 1 323 ? 15.614  -25.602 -3.892  1.00 39.65  ? 299 LEU B C   1 
ATOM   4612 O  O   . LEU B 1 323 ? 15.341  -24.661 -4.645  1.00 37.83  ? 299 LEU B O   1 
ATOM   4613 C  CB  . LEU B 1 323 ? 13.990  -25.942 -2.022  1.00 38.36  ? 299 LEU B CB  1 
ATOM   4614 C  CG  . LEU B 1 323 ? 12.612  -26.431 -1.579  1.00 43.84  ? 299 LEU B CG  1 
ATOM   4615 C  CD1 . LEU B 1 323 ? 12.410  -26.197 -0.088  1.00 37.94  ? 299 LEU B CD1 1 
ATOM   4616 C  CD2 . LEU B 1 323 ? 11.527  -25.729 -2.381  1.00 41.92  ? 299 LEU B CD2 1 
ATOM   4617 N  N   . LEU B 1 324 ? 16.865  -25.885 -3.527  1.00 38.20  ? 300 LEU B N   1 
ATOM   4618 C  CA  . LEU B 1 324 ? 17.992  -25.031 -3.872  1.00 38.94  ? 300 LEU B CA  1 
ATOM   4619 C  C   . LEU B 1 324 ? 18.853  -25.591 -4.999  1.00 37.92  ? 300 LEU B C   1 
ATOM   4620 O  O   . LEU B 1 324 ? 19.787  -24.909 -5.434  1.00 36.48  ? 300 LEU B O   1 
ATOM   4621 C  CB  . LEU B 1 324 ? 18.866  -24.797 -2.630  1.00 36.40  ? 300 LEU B CB  1 
ATOM   4622 C  CG  . LEU B 1 324 ? 18.145  -24.227 -1.402  1.00 38.21  ? 300 LEU B CG  1 
ATOM   4623 C  CD1 . LEU B 1 324 ? 19.103  -24.090 -0.229  1.00 35.29  ? 300 LEU B CD1 1 
ATOM   4624 C  CD2 . LEU B 1 324 ? 17.497  -22.889 -1.712  1.00 33.81  ? 300 LEU B CD2 1 
ATOM   4625 N  N   . ALA B 1 325 ? 18.569  -26.808 -5.474  1.00 38.93  ? 301 ALA B N   1 
ATOM   4626 C  CA  . ALA B 1 325 ? 19.277  -27.411 -6.608  1.00 38.43  ? 301 ALA B CA  1 
ATOM   4627 C  C   . ALA B 1 325 ? 20.741  -27.707 -6.278  1.00 38.81  ? 301 ALA B C   1 
ATOM   4628 O  O   . ALA B 1 325 ? 21.637  -27.436 -7.075  1.00 42.74  ? 301 ALA B O   1 
ATOM   4629 C  CB  . ALA B 1 325 ? 19.184  -26.522 -7.853  1.00 37.96  ? 301 ALA B CB  1 
ATOM   4630 N  N   . LEU B 1 326 ? 20.983  -28.288 -5.109  1.00 39.24  ? 302 LEU B N   1 
ATOM   4631 C  CA  . LEU B 1 326 ? 22.344  -28.559 -4.670  1.00 38.77  ? 302 LEU B CA  1 
ATOM   4632 C  C   . LEU B 1 326 ? 22.815  -29.926 -5.164  1.00 42.49  ? 302 LEU B C   1 
ATOM   4633 O  O   . LEU B 1 326 ? 22.022  -30.772 -5.584  1.00 39.56  ? 302 LEU B O   1 
ATOM   4634 C  CB  . LEU B 1 326 ? 22.438  -28.479 -3.147  1.00 38.10  ? 302 LEU B CB  1 
ATOM   4635 C  CG  . LEU B 1 326 ? 21.934  -27.158 -2.555  1.00 37.26  ? 302 LEU B CG  1 
ATOM   4636 C  CD1 . LEU B 1 326 ? 22.099  -27.153 -1.048  1.00 34.86  ? 302 LEU B CD1 1 
ATOM   4637 C  CD2 . LEU B 1 326 ? 22.645  -25.957 -3.176  1.00 31.10  ? 302 LEU B CD2 1 
ATOM   4638 N  N   . LYS B 1 327 ? 24.134  -30.132 -5.105  1.00 40.81  ? 303 LYS B N   1 
ATOM   4639 C  CA  . LYS B 1 327 ? 24.759  -31.299 -5.716  1.00 41.69  ? 303 LYS B CA  1 
ATOM   4640 C  C   . LYS B 1 327 ? 24.747  -32.537 -4.829  1.00 42.52  ? 303 LYS B C   1 
ATOM   4641 O  O   . LYS B 1 327 ? 25.005  -33.634 -5.334  1.00 45.04  ? 303 LYS B O   1 
ATOM   4642 C  CB  . LYS B 1 327 ? 26.205  -30.974 -6.109  1.00 41.81  ? 303 LYS B CB  1 
ATOM   4643 C  CG  . LYS B 1 327 ? 27.110  -30.565 -4.950  1.00 42.98  ? 303 LYS B CG  1 
ATOM   4644 C  CD  . LYS B 1 327 ? 28.554  -30.409 -5.416  1.00 39.91  ? 303 LYS B CD  1 
ATOM   4645 C  CE  . LYS B 1 327 ? 29.440  -29.790 -4.344  1.00 42.14  ? 303 LYS B CE  1 
ATOM   4646 N  NZ  . LYS B 1 327 ? 30.881  -29.812 -4.734  1.00 39.41  ? 303 LYS B NZ  1 
ATOM   4647 N  N   . GLY B 1 328 ? 24.466  -32.399 -3.544  1.00 42.74  ? 304 GLY B N   1 
ATOM   4648 C  CA  . GLY B 1 328 ? 24.426  -33.545 -2.648  1.00 40.04  ? 304 GLY B CA  1 
ATOM   4649 C  C   . GLY B 1 328 ? 25.558  -33.491 -1.638  1.00 41.07  ? 304 GLY B C   1 
ATOM   4650 O  O   . GLY B 1 328 ? 26.686  -33.092 -1.956  1.00 41.12  ? 304 GLY B O   1 
ATOM   4651 N  N   . GLY B 1 329 ? 25.255  -33.900 -0.406  1.00 41.32  ? 305 GLY B N   1 
ATOM   4652 C  CA  . GLY B 1 329 ? 26.225  -33.850 0.674   1.00 41.63  ? 305 GLY B CA  1 
ATOM   4653 C  C   . GLY B 1 329 ? 27.378  -34.816 0.525   1.00 44.31  ? 305 GLY B C   1 
ATOM   4654 O  O   . GLY B 1 329 ? 28.364  -34.687 1.259   1.00 45.79  ? 305 GLY B O   1 
ATOM   4655 N  N   . ASP B 1 330 ? 27.282  -35.772 -0.396  1.00 44.60  ? 306 ASP B N   1 
ATOM   4656 C  CA  . ASP B 1 330 ? 28.354  -36.729 -0.636  1.00 47.61  ? 306 ASP B CA  1 
ATOM   4657 C  C   . ASP B 1 330 ? 29.240  -36.354 -1.815  1.00 46.54  ? 306 ASP B C   1 
ATOM   4658 O  O   . ASP B 1 330 ? 30.236  -37.042 -2.062  1.00 45.90  ? 306 ASP B O   1 
ATOM   4659 C  CB  . ASP B 1 330 ? 27.775  -38.128 -0.867  1.00 44.87  ? 306 ASP B CB  1 
ATOM   4660 C  CG  . ASP B 1 330 ? 27.393  -38.822 0.425   1.00 59.02  ? 306 ASP B CG  1 
ATOM   4661 O  OD1 . ASP B 1 330 ? 28.080  -38.601 1.448   1.00 60.74  ? 306 ASP B OD1 1 
ATOM   4662 O  OD2 . ASP B 1 330 ? 26.405  -39.587 0.419   1.00 61.91  ? 306 ASP B OD2 1 
ATOM   4663 N  N   . GLN B 1 331 ? 28.906  -35.292 -2.545  1.00 46.12  ? 307 GLN B N   1 
ATOM   4664 C  CA  . GLN B 1 331 ? 29.709  -34.813 -3.668  1.00 48.71  ? 307 GLN B CA  1 
ATOM   4665 C  C   . GLN B 1 331 ? 30.536  -33.596 -3.279  1.00 46.92  ? 307 GLN B C   1 
ATOM   4666 O  O   . GLN B 1 331 ? 30.610  -32.613 -4.021  1.00 45.37  ? 307 GLN B O   1 
ATOM   4667 C  CB  . GLN B 1 331 ? 28.811  -34.502 -4.863  1.00 47.12  ? 307 GLN B CB  1 
ATOM   4668 C  CG  . GLN B 1 331 ? 28.059  -35.720 -5.390  1.00 50.80  ? 307 GLN B CG  1 
ATOM   4669 C  CD  . GLN B 1 331 ? 28.014  -35.780 -6.905  1.00 52.41  ? 307 GLN B CD  1 
ATOM   4670 O  OE1 . GLN B 1 331 ? 28.976  -36.199 -7.552  1.00 50.44  ? 307 GLN B OE1 1 
ATOM   4671 N  NE2 . GLN B 1 331 ? 26.891  -35.365 -7.480  1.00 54.45  ? 307 GLN B NE2 1 
ATOM   4672 N  N   . VAL B 1 332 ? 31.162  -33.644 -2.103  1.00 44.74  ? 308 VAL B N   1 
ATOM   4673 C  CA  . VAL B 1 332 ? 32.004  -32.561 -1.610  1.00 44.95  ? 308 VAL B CA  1 
ATOM   4674 C  C   . VAL B 1 332 ? 33.408  -33.103 -1.381  1.00 45.19  ? 308 VAL B C   1 
ATOM   4675 O  O   . VAL B 1 332 ? 33.660  -34.298 -1.568  1.00 47.32  ? 308 VAL B O   1 
ATOM   4676 C  CB  . VAL B 1 332 ? 31.433  -31.946 -0.319  1.00 42.66  ? 308 VAL B CB  1 
ATOM   4677 C  CG1 . VAL B 1 332 ? 30.097  -31.276 -0.593  1.00 41.72  ? 308 VAL B CG1 1 
ATOM   4678 C  CG2 . VAL B 1 332 ? 31.292  -33.012 0.765   1.00 42.43  ? 308 VAL B CG2 1 
ATOM   4679 N  N   . ASN B 1 333 ? 34.328  -32.230 -0.970  1.00 43.55  ? 309 ASN B N   1 
ATOM   4680 C  CA  . ASN B 1 333 ? 35.701  -32.645 -0.712  1.00 45.97  ? 309 ASN B CA  1 
ATOM   4681 C  C   . ASN B 1 333 ? 35.996  -32.637 0.783   1.00 44.72  ? 309 ASN B C   1 
ATOM   4682 O  O   . ASN B 1 333 ? 36.959  -32.004 1.231   1.00 46.47  ? 309 ASN B O   1 
ATOM   4683 C  CB  . ASN B 1 333 ? 36.685  -31.738 -1.454  1.00 46.28  ? 309 ASN B CB  1 
ATOM   4684 C  CG  . ASN B 1 333 ? 38.091  -32.304 -1.481  1.00 49.09  ? 309 ASN B CG  1 
ATOM   4685 O  OD1 . ASN B 1 333 ? 38.286  -33.516 -1.390  1.00 47.60  ? 309 ASN B OD1 1 
ATOM   4686 N  ND2 . ASN B 1 333 ? 39.080  -31.426 -1.604  1.00 48.12  ? 309 ASN B ND2 1 
ATOM   4687 N  N   . PHE B 1 334 ? 35.168  -33.330 1.558   1.00 45.79  ? 310 PHE B N   1 
ATOM   4688 C  CA  . PHE B 1 334 ? 35.418  -33.526 2.982   1.00 46.87  ? 310 PHE B CA  1 
ATOM   4689 C  C   . PHE B 1 334 ? 34.523  -34.641 3.511   1.00 48.39  ? 310 PHE B C   1 
ATOM   4690 O  O   . PHE B 1 334 ? 34.625  -35.049 4.669   1.00 51.72  ? 310 PHE B O   1 
ATOM   4691 C  CB  . PHE B 1 334 ? 35.188  -32.230 3.771   1.00 42.33  ? 310 PHE B CB  1 
ATOM   4692 C  CG  . PHE B 1 334 ? 33.840  -31.602 3.545   1.00 42.93  ? 310 PHE B CG  1 
ATOM   4693 C  CD1 . PHE B 1 334 ? 32.742  -31.990 4.297   1.00 42.83  ? 310 PHE B CD1 1 
ATOM   4694 C  CD2 . PHE B 1 334 ? 33.676  -30.607 2.595   1.00 44.03  ? 310 PHE B CD2 1 
ATOM   4695 C  CE1 . PHE B 1 334 ? 31.505  -31.406 4.095   1.00 42.03  ? 310 PHE B CE1 1 
ATOM   4696 C  CE2 . PHE B 1 334 ? 32.440  -30.020 2.391   1.00 41.54  ? 310 PHE B CE2 1 
ATOM   4697 C  CZ  . PHE B 1 334 ? 31.355  -30.420 3.142   1.00 39.26  ? 310 PHE B CZ  1 
ATOM   4698 O  OXT . PHE B 1 334 ? 33.678  -35.165 2.785   1.00 48.54  ? 310 PHE B OXT 1 
HETATM 4699 N  N1A . ACO C 2 .   ? -1.930  -26.071 5.326   0.90 55.45  ? 401 ACO A N1A 1 
HETATM 4700 C  C2A . ACO C 2 .   ? -2.259  -26.430 4.081   0.90 57.56  ? 401 ACO A C2A 1 
HETATM 4701 N  N3A . ACO C 2 .   ? -3.429  -26.335 3.461   0.90 57.07  ? 401 ACO A N3A 1 
HETATM 4702 C  C4A . ACO C 2 .   ? -4.352  -25.798 4.272   0.90 54.28  ? 401 ACO A C4A 1 
HETATM 4703 C  C5A . ACO C 2 .   ? -4.169  -25.375 5.569   0.90 56.63  ? 401 ACO A C5A 1 
HETATM 4704 C  C6A . ACO C 2 .   ? -2.882  -25.524 6.116   0.90 55.94  ? 401 ACO A C6A 1 
HETATM 4705 N  N6A . ACO C 2 .   ? -2.553  -25.166 7.351   0.90 55.71  ? 401 ACO A N6A 1 
HETATM 4706 N  N7A . ACO C 2 .   ? -5.359  -24.876 6.080   0.90 51.12  ? 401 ACO A N7A 1 
HETATM 4707 C  C8A . ACO C 2 .   ? -6.220  -25.000 5.097   0.90 51.72  ? 401 ACO A C8A 1 
HETATM 4708 N  N9A . ACO C 2 .   ? -5.663  -25.550 3.973   0.90 51.45  ? 401 ACO A N9A 1 
HETATM 4709 C  C1B . ACO C 2 .   ? -6.305  -25.840 2.703   0.90 50.57  ? 401 ACO A C1B 1 
HETATM 4710 C  C2B . ACO C 2 .   ? -7.391  -26.906 2.754   0.90 49.83  ? 401 ACO A C2B 1 
HETATM 4711 O  O2B . ACO C 2 .   ? -6.857  -28.210 2.736   0.90 47.73  ? 401 ACO A O2B 1 
HETATM 4712 C  C3B . ACO C 2 .   ? -8.154  -26.563 1.479   0.90 48.56  ? 401 ACO A C3B 1 
HETATM 4713 O  O3B . ACO C 2 .   ? -7.393  -27.006 0.374   0.90 50.71  ? 401 ACO A O3B 1 
HETATM 4714 P  P3B . ACO C 2 .   ? -8.266  -27.296 -0.933  0.90 49.98  ? 401 ACO A P3B 1 
HETATM 4715 O  O7A . ACO C 2 .   ? -8.812  -26.005 -1.458  0.90 48.82  ? 401 ACO A O7A 1 
HETATM 4716 O  O8A . ACO C 2 .   ? -9.352  -28.256 -0.573  0.90 51.54  ? 401 ACO A O8A 1 
HETATM 4717 O  O9A . ACO C 2 .   ? -7.288  -27.906 -1.883  0.90 53.49  ? 401 ACO A O9A 1 
HETATM 4718 C  C4B . ACO C 2 .   ? -8.167  -25.047 1.546   0.90 49.79  ? 401 ACO A C4B 1 
HETATM 4719 O  O4B . ACO C 2 .   ? -6.947  -24.678 2.241   0.90 52.18  ? 401 ACO A O4B 1 
HETATM 4720 C  C5B . ACO C 2 .   ? -9.340  -24.475 2.298   0.90 47.50  ? 401 ACO A C5B 1 
HETATM 4721 O  O5B . ACO C 2 .   ? -8.983  -23.178 2.819   0.90 46.00  ? 401 ACO A O5B 1 
HETATM 4722 P  P1A . ACO C 2 .   ? -9.487  -21.894 2.019   0.90 46.47  ? 401 ACO A P1A 1 
HETATM 4723 O  O1A . ACO C 2 .   ? -8.819  -21.849 0.687   0.90 51.95  ? 401 ACO A O1A 1 
HETATM 4724 O  O2A . ACO C 2 .   ? -9.393  -20.691 2.894   0.90 42.29  ? 401 ACO A O2A 1 
HETATM 4725 O  O3A . ACO C 2 .   ? -11.032 -22.259 1.811   0.90 49.23  ? 401 ACO A O3A 1 
HETATM 4726 P  P2A . ACO C 2 .   ? -12.125 -21.826 0.724   0.90 49.56  ? 401 ACO A P2A 1 
HETATM 4727 O  O4A . ACO C 2 .   ? -11.467 -21.732 -0.605  0.90 50.52  ? 401 ACO A O4A 1 
HETATM 4728 O  O5A . ACO C 2 .   ? -13.288 -22.733 0.890   0.90 44.76  ? 401 ACO A O5A 1 
HETATM 4729 O  O6A . ACO C 2 .   ? -12.499 -20.344 1.195   0.90 44.96  ? 401 ACO A O6A 1 
HETATM 4730 C  CBP . ACO C 2 .   ? -13.486 -18.678 2.649   0.90 42.00  ? 401 ACO A CBP 1 
HETATM 4731 C  CCP . ACO C 2 .   ? -13.093 -20.144 2.501   0.90 42.30  ? 401 ACO A CCP 1 
HETATM 4732 C  CDP . ACO C 2 .   ? -12.234 -17.803 2.727   0.90 39.51  ? 401 ACO A CDP 1 
HETATM 4733 C  CEP . ACO C 2 .   ? -14.305 -18.247 1.431   0.90 41.51  ? 401 ACO A CEP 1 
HETATM 4734 C  CAP . ACO C 2 .   ? -14.317 -18.506 3.922   0.90 41.53  ? 401 ACO A CAP 1 
HETATM 4735 O  OAP . ACO C 2 .   ? -13.706 -19.270 4.935   0.90 36.48  ? 401 ACO A OAP 1 
HETATM 4736 C  C9P . ACO C 2 .   ? -14.435 -17.066 4.385   0.90 38.85  ? 401 ACO A C9P 1 
HETATM 4737 O  O9P . ACO C 2 .   ? -15.011 -16.245 3.681   0.90 36.74  ? 401 ACO A O9P 1 
HETATM 4738 N  N8P . ACO C 2 .   ? -13.885 -16.768 5.554   0.90 36.86  ? 401 ACO A N8P 1 
HETATM 4739 C  C7P . ACO C 2 .   ? -14.110 -15.525 6.277   0.90 32.59  ? 401 ACO A C7P 1 
HETATM 4740 C  C6P . ACO C 2 .   ? -15.557 -15.318 6.643   0.90 33.29  ? 401 ACO A C6P 1 
HETATM 4741 C  C5P . ACO C 2 .   ? -15.805 -13.898 7.104   0.90 34.32  ? 401 ACO A C5P 1 
HETATM 4742 O  O5P . ACO C 2 .   ? -16.386 -13.094 6.384   0.90 36.31  ? 401 ACO A O5P 1 
HETATM 4743 N  N4P . ACO C 2 .   ? -15.399 -13.571 8.330   0.90 35.13  ? 401 ACO A N4P 1 
HETATM 4744 C  C3P . ACO C 2 .   ? -15.292 -12.195 8.780   0.90 34.95  ? 401 ACO A C3P 1 
HETATM 4745 C  C2P . ACO C 2 .   ? -16.468 -11.804 9.636   0.90 37.73  ? 401 ACO A C2P 1 
HETATM 4746 S  S1P . ACO C 2 .   ? -17.478 -10.450 8.987   0.90 42.30  ? 401 ACO A S1P 1 
HETATM 4747 C  C   . ACO C 2 .   ? -18.988 -10.296 9.846   0.90 39.59  ? 401 ACO A C   1 
HETATM 4748 O  O   . ACO C 2 .   ? -19.213 -10.901 10.858  0.90 40.60  ? 401 ACO A O   1 
HETATM 4749 C  CH3 . ACO C 2 .   ? -19.950 -9.351  9.222   0.90 37.79  ? 401 ACO A CH3 1 
HETATM 4750 O  O1  . AAE D 3 .   ? -19.135 -9.245  13.516  1.00 31.46  ? 402 AAE A O1  1 
HETATM 4751 C  C2  . AAE D 3 .   ? -18.854 -8.150  12.991  1.00 34.61  ? 402 AAE A C2  1 
HETATM 4752 O  O3  . AAE D 3 .   ? -19.488 -7.122  13.205  1.00 35.41  ? 402 AAE A O3  1 
HETATM 4753 C  C4  . AAE D 3 .   ? -17.629 -8.032  12.077  1.00 37.17  ? 402 AAE A C4  1 
HETATM 4754 C  C5  . AAE D 3 .   ? -16.614 -9.159  12.055  1.00 36.12  ? 402 AAE A C5  1 
HETATM 4755 O  O8  . AAE D 3 .   ? -16.765 -10.230 12.638  1.00 34.72  ? 402 AAE A O8  1 
HETATM 4756 C  C9  . AAE D 3 .   ? -15.365 -8.874  11.285  1.00 34.37  ? 402 AAE A C9  1 
HETATM 4757 ZN ZN  . ZN  E 4 .   ? -18.391 -11.135 13.529  1.00 33.76  ? 403 ZN  A ZN  1 
HETATM 4758 N  N1A . ACO F 2 .   ? 12.506  -10.181 24.700  0.78 84.71  ? 401 ACO B N1A 1 
HETATM 4759 C  C2A . ACO F 2 .   ? 12.925  -9.129  25.416  0.78 87.82  ? 401 ACO B C2A 1 
HETATM 4760 N  N3A . ACO F 2 .   ? 14.026  -8.397  25.271  0.78 88.68  ? 401 ACO B N3A 1 
HETATM 4761 C  C4A . ACO F 2 .   ? 14.760  -8.848  24.243  0.78 86.87  ? 401 ACO B C4A 1 
HETATM 4762 C  C5A . ACO F 2 .   ? 14.465  -9.907  23.413  0.78 82.92  ? 401 ACO B C5A 1 
HETATM 4763 C  C6A . ACO F 2 .   ? 13.270  -10.606 23.665  0.78 83.52  ? 401 ACO B C6A 1 
HETATM 4764 N  N6A . ACO F 2 .   ? 12.858  -11.648 22.949  0.78 76.19  ? 401 ACO B N6A 1 
HETATM 4765 N  N7A . ACO F 2 .   ? 15.466  -10.063 22.462  0.78 77.46  ? 401 ACO B N7A 1 
HETATM 4766 C  C8A . ACO F 2 .   ? 16.330  -9.111  22.729  0.78 79.62  ? 401 ACO B C8A 1 
HETATM 4767 N  N9A . ACO F 2 .   ? 15.950  -8.340  23.798  0.78 85.16  ? 401 ACO B N9A 1 
HETATM 4768 C  C1B . ACO F 2 .   ? 16.652  -7.201  24.373  0.78 87.42  ? 401 ACO B C1B 1 
HETATM 4769 C  C2B . ACO F 2 .   ? 17.770  -7.541  25.352  0.78 85.09  ? 401 ACO B C2B 1 
HETATM 4770 O  O2B . ACO F 2 .   ? 17.294  -7.825  26.650  0.78 84.62  ? 401 ACO B O2B 1 
HETATM 4771 C  C3B . ACO F 2 .   ? 18.572  -6.248  25.263  0.78 87.82  ? 401 ACO B C3B 1 
HETATM 4772 O  O3B . ACO F 2 .   ? 17.833  -5.224  25.917  0.78 90.16  ? 401 ACO B O3B 1 
HETATM 4773 P  P3B . ACO F 2 .   ? 18.583  -3.793  25.908  0.78 95.14  ? 401 ACO B P3B 1 
HETATM 4774 O  O7A . ACO F 2 .   ? 18.496  -3.234  24.503  0.78 93.88  ? 401 ACO B O7A 1 
HETATM 4775 O  O8A . ACO F 2 .   ? 20.013  -4.044  26.333  0.78 93.72  ? 401 ACO B O8A 1 
HETATM 4776 O  O9A . ACO F 2 .   ? 17.840  -2.931  26.906  0.78 91.67  ? 401 ACO B O9A 1 
HETATM 4777 C  C4B . ACO F 2 .   ? 18.585  -6.052  23.757  0.78 85.53  ? 401 ACO B C4B 1 
HETATM 4778 O  O4B . ACO F 2 .   ? 17.268  -6.483  23.328  0.78 86.74  ? 401 ACO B O4B 1 
HETATM 4779 C  C5B . ACO F 2 .   ? 19.619  -6.871  23.028  0.78 82.24  ? 401 ACO B C5B 1 
HETATM 4780 O  O5B . ACO F 2 .   ? 19.284  -6.929  21.619  0.78 81.48  ? 401 ACO B O5B 1 
HETATM 4781 P  P1A . ACO F 2 .   ? 19.742  -5.721  20.672  0.78 85.52  ? 401 ACO B P1A 1 
HETATM 4782 O  O1A . ACO F 2 .   ? 19.099  -4.458  21.138  0.78 84.86  ? 401 ACO B O1A 1 
HETATM 4783 O  O2A . ACO F 2 .   ? 19.576  -6.121  19.244  0.78 68.97  ? 401 ACO B O2A 1 
HETATM 4784 O  O3A . ACO F 2 .   ? 21.302  -5.664  21.032  0.78 86.25  ? 401 ACO B O3A 1 
HETATM 4785 P  P2A . ACO F 2 .   ? 22.484  -4.658  20.639  0.78 86.44  ? 401 ACO B P2A 1 
HETATM 4786 O  O4A . ACO F 2 .   ? 21.979  -3.256  20.708  0.78 87.73  ? 401 ACO B O4A 1 
HETATM 4787 O  O5A . ACO F 2 .   ? 23.702  -5.021  21.419  0.78 83.47  ? 401 ACO B O5A 1 
HETATM 4788 O  O6A . ACO F 2 .   ? 22.743  -5.043  19.106  0.78 82.59  ? 401 ACO B O6A 1 
HETATM 4789 C  CBP . ACO F 2 .   ? 23.688  -6.358  17.316  0.78 66.88  ? 401 ACO B CBP 1 
HETATM 4790 C  CCP . ACO F 2 .   ? 23.306  -6.344  18.792  0.78 73.62  ? 401 ACO B CCP 1 
HETATM 4791 C  CDP . ACO F 2 .   ? 22.421  -6.281  16.461  0.78 58.98  ? 401 ACO B CDP 1 
HETATM 4792 C  CEP . ACO F 2 .   ? 24.562  -5.138  17.015  0.78 70.65  ? 401 ACO B CEP 1 
HETATM 4793 C  CAP . ACO F 2 .   ? 24.458  -7.640  16.985  0.78 59.09  ? 401 ACO B CAP 1 
HETATM 4794 O  OAP . ACO F 2 .   ? 23.710  -8.729  17.485  0.78 59.21  ? 401 ACO B OAP 1 
HETATM 4795 C  C9P . ACO F 2 .   ? 24.682  -7.839  15.497  0.78 58.06  ? 401 ACO B C9P 1 
HETATM 4796 O  O9P . ACO F 2 .   ? 25.305  -7.004  14.848  0.78 59.27  ? 401 ACO B O9P 1 
HETATM 4797 N  N8P . ACO F 2 .   ? 24.173  -8.940  14.964  0.78 56.12  ? 401 ACO B N8P 1 
HETATM 4798 C  C7P . ACO F 2 .   ? 24.376  -9.329  13.576  0.78 54.06  ? 401 ACO B C7P 1 
HETATM 4799 C  C6P . ACO F 2 .   ? 25.828  -9.584  13.256  0.78 53.67  ? 401 ACO B C6P 1 
HETATM 4800 C  C5P . ACO F 2 .   ? 26.011  -9.868  11.781  0.78 57.83  ? 401 ACO B C5P 1 
HETATM 4801 O  O5P . ACO F 2 .   ? 26.685  -9.121  11.077  0.78 61.94  ? 401 ACO B O5P 1 
HETATM 4802 N  N4P . ACO F 2 .   ? 25.407  -10.956 11.291  0.78 53.49  ? 401 ACO B N4P 1 
HETATM 4803 C  C3P . ACO F 2 .   ? 25.543  -11.404 9.913   0.78 53.38  ? 401 ACO B C3P 1 
HETATM 4804 C  C2P . ACO F 2 .   ? 26.973  -11.733 9.555   0.78 54.53  ? 401 ACO B C2P 1 
HETATM 4805 S  S1P . ACO F 2 .   ? 27.569  -10.788 8.130   0.78 61.21  ? 401 ACO B S1P 1 
HETATM 4806 C  C   . ACO F 2 .   ? 29.268  -10.865 7.686   0.78 59.82  ? 401 ACO B C   1 
HETATM 4807 O  O   . ACO F 2 .   ? 30.113  -11.410 8.354   0.78 59.36  ? 401 ACO B O   1 
HETATM 4808 C  CH3 . ACO F 2 .   ? 29.556  -10.200 6.392   0.78 57.86  ? 401 ACO B CH3 1 
HETATM 4809 O  O1  . AAE G 3 .   ? 29.150  -14.999 6.067   0.96 37.24  ? 402 AAE B O1  1 
HETATM 4810 C  C2  . AAE G 3 .   ? 28.916  -14.234 5.175   0.96 41.43  ? 402 AAE B C2  1 
HETATM 4811 O  O3  . AAE G 3 .   ? 29.653  -14.117 4.226   0.96 40.77  ? 402 AAE B O3  1 
HETATM 4812 C  C4  . AAE G 3 .   ? 27.635  -13.400 5.212   0.96 45.70  ? 402 AAE B C4  1 
HETATM 4813 C  C5  . AAE G 3 .   ? 26.644  -13.644 6.301   0.96 41.31  ? 402 AAE B C5  1 
HETATM 4814 O  O8  . AAE G 3 .   ? 26.840  -14.438 7.179   0.96 37.74  ? 402 AAE B O8  1 
HETATM 4815 C  C9  . AAE G 3 .   ? 25.364  -12.867 6.242   0.96 42.51  ? 402 AAE B C9  1 
HETATM 4816 ZN ZN  . ZN  H 4 .   ? 28.523  -15.549 7.963   1.00 37.27  ? 403 ZN  B ZN  1 
HETATM 4817 O  O   . HOH I 5 .   ? -13.368 -9.530  16.666  1.00 34.29  ? 501 HOH A O   1 
HETATM 4818 O  O   . HOH I 5 .   ? -31.099 -15.183 9.880   1.00 42.17  ? 502 HOH A O   1 
HETATM 4819 O  O   . HOH I 5 .   ? -32.540 -6.334  9.128   1.00 50.81  ? 503 HOH A O   1 
HETATM 4820 O  O   . HOH I 5 .   ? 0.320   2.390   1.845   1.00 41.58  ? 504 HOH A O   1 
HETATM 4821 O  O   . HOH I 5 .   ? -26.070 -12.853 15.943  1.00 31.27  ? 505 HOH A O   1 
HETATM 4822 O  O   . HOH I 5 .   ? -21.273 -23.969 28.113  1.00 47.50  ? 506 HOH A O   1 
HETATM 4823 O  O   . HOH I 5 .   ? -2.231  5.238   3.097   1.00 45.00  ? 507 HOH A O   1 
HETATM 4824 O  O   . HOH I 5 .   ? -27.006 -13.847 29.183  1.00 41.69  ? 508 HOH A O   1 
HETATM 4825 O  O   . HOH I 5 .   ? -10.163 -9.300  17.221  1.00 36.55  ? 509 HOH A O   1 
HETATM 4826 O  O   . HOH I 5 .   ? -16.056 2.560   28.504  1.00 47.84  ? 510 HOH A O   1 
HETATM 4827 O  O   . HOH I 5 .   ? -21.592 0.127   11.625  1.00 30.17  ? 511 HOH A O   1 
HETATM 4828 O  O   . HOH I 5 .   ? 7.977   -17.738 24.682  1.00 40.61  ? 512 HOH A O   1 
HETATM 4829 O  O   . HOH I 5 .   ? 0.094   -20.738 7.300   1.00 41.39  ? 513 HOH A O   1 
HETATM 4830 O  O   . HOH I 5 .   ? -5.582  -23.144 7.934   1.00 43.85  ? 514 HOH A O   1 
HETATM 4831 O  O   . HOH I 5 .   ? -8.706  -16.132 28.294  1.00 41.84  ? 515 HOH A O   1 
HETATM 4832 O  O   . HOH I 5 .   ? -9.458  -25.262 25.924  1.00 40.32  ? 516 HOH A O   1 
HETATM 4833 O  O   . HOH I 5 .   ? -32.041 -7.419  17.000  1.00 47.01  ? 517 HOH A O   1 
HETATM 4834 O  O   . HOH I 5 .   ? -17.463 -29.689 4.439   1.00 42.89  ? 518 HOH A O   1 
HETATM 4835 O  O   . HOH I 5 .   ? -16.499 -14.154 3.729   1.00 39.58  ? 519 HOH A O   1 
HETATM 4836 O  O   . HOH I 5 .   ? -13.602 -23.240 3.390   1.00 42.82  ? 520 HOH A O   1 
HETATM 4837 O  O   . HOH I 5 .   ? -11.221 11.703  19.162  1.00 47.98  ? 521 HOH A O   1 
HETATM 4838 O  O   . HOH I 5 .   ? -16.322 -26.962 17.420  1.00 37.11  ? 522 HOH A O   1 
HETATM 4839 O  O   . HOH I 5 .   ? -16.456 0.244   1.676   1.00 39.12  ? 523 HOH A O   1 
HETATM 4840 O  O   . HOH I 5 .   ? -19.612 -13.446 10.471  1.00 30.32  ? 524 HOH A O   1 
HETATM 4841 O  O   . HOH I 5 .   ? -11.920 -8.529  19.714  1.00 39.22  ? 525 HOH A O   1 
HETATM 4842 O  O   . HOH I 5 .   ? -13.808 1.953   29.605  1.00 43.50  ? 526 HOH A O   1 
HETATM 4843 O  O   . HOH I 5 .   ? -18.528 -15.547 16.401  1.00 27.93  ? 527 HOH A O   1 
HETATM 4844 O  O   . HOH I 5 .   ? -10.190 0.596   22.989  1.00 37.19  ? 528 HOH A O   1 
HETATM 4845 O  O   . HOH I 5 .   ? 0.260   5.810   4.383   1.00 42.72  ? 529 HOH A O   1 
HETATM 4846 O  O   . HOH I 5 .   ? -1.757  -15.887 3.721   1.00 42.84  ? 530 HOH A O   1 
HETATM 4847 O  O   . HOH I 5 .   ? -21.826 -6.600  35.483  1.00 50.83  ? 531 HOH A O   1 
HETATM 4848 O  O   . HOH I 5 .   ? -10.802 10.948  6.546   1.00 39.37  ? 532 HOH A O   1 
HETATM 4849 O  O   . HOH I 5 .   ? 5.420   -22.388 23.956  1.00 43.54  ? 533 HOH A O   1 
HETATM 4850 O  O   . HOH I 5 .   ? -14.507 -26.668 10.765  1.00 32.41  ? 534 HOH A O   1 
HETATM 4851 O  O   . HOH I 5 .   ? 1.793   -16.957 26.645  1.00 36.44  ? 535 HOH A O   1 
HETATM 4852 O  O   . HOH I 5 .   ? -34.059 -22.991 4.548   1.00 47.84  ? 536 HOH A O   1 
HETATM 4853 O  O   . HOH I 5 .   ? -24.431 -18.231 8.198   1.00 35.71  ? 537 HOH A O   1 
HETATM 4854 O  O   . HOH I 5 .   ? -18.942 -26.318 20.923  1.00 41.83  ? 538 HOH A O   1 
HETATM 4855 O  O   . HOH I 5 .   ? -25.505 -5.645  18.720  1.00 34.54  ? 539 HOH A O   1 
HETATM 4856 O  O   . HOH I 5 .   ? -21.513 -2.403  12.578  1.00 35.18  ? 540 HOH A O   1 
HETATM 4857 O  O   . HOH I 5 .   ? -21.218 -21.338 32.978  1.00 42.54  ? 541 HOH A O   1 
HETATM 4858 O  O   . HOH I 5 .   ? -1.899  -19.376 7.360   1.00 45.52  ? 542 HOH A O   1 
HETATM 4859 O  O   . HOH I 5 .   ? 10.233  -11.409 18.814  1.00 39.17  ? 543 HOH A O   1 
HETATM 4860 O  O   . HOH I 5 .   ? -31.565 -18.458 18.968  1.00 45.28  ? 544 HOH A O   1 
HETATM 4861 O  O   . HOH I 5 .   ? -31.540 1.449   18.554  1.00 60.61  ? 545 HOH A O   1 
HETATM 4862 O  O   . HOH I 5 .   ? -22.799 -0.571  32.142  1.00 51.42  ? 546 HOH A O   1 
HETATM 4863 O  O   . HOH I 5 .   ? -26.752 -4.488  5.641   1.00 38.35  ? 547 HOH A O   1 
HETATM 4864 O  O   . HOH I 5 .   ? -7.345  -9.389  19.032  1.00 29.84  ? 548 HOH A O   1 
HETATM 4865 O  O   . HOH I 5 .   ? -16.438 -12.507 31.429  1.00 45.27  ? 549 HOH A O   1 
HETATM 4866 O  O   . HOH I 5 .   ? 6.580   -8.338  17.903  1.00 33.89  ? 550 HOH A O   1 
HETATM 4867 O  O   . HOH I 5 .   ? -29.728 2.393   8.855   1.00 44.40  ? 551 HOH A O   1 
HETATM 4868 O  O   . HOH I 5 .   ? -17.139 -8.933  29.052  1.00 37.09  ? 552 HOH A O   1 
HETATM 4869 O  O   . HOH I 5 .   ? -11.657 1.277   20.574  1.00 32.35  ? 553 HOH A O   1 
HETATM 4870 O  O   . HOH I 5 .   ? -31.853 0.115   10.298  1.00 54.76  ? 554 HOH A O   1 
HETATM 4871 O  O   . HOH I 5 .   ? 0.160   -12.549 30.039  1.00 40.99  ? 555 HOH A O   1 
HETATM 4872 O  O   . HOH I 5 .   ? -18.737 -7.720  27.464  1.00 35.44  ? 556 HOH A O   1 
HETATM 4873 O  O   . HOH I 5 .   ? -28.507 -6.271  -9.237  1.00 39.96  ? 557 HOH A O   1 
HETATM 4874 O  O   . HOH I 5 .   ? -3.861  -26.656 17.225  1.00 45.43  ? 558 HOH A O   1 
HETATM 4875 O  O   . HOH I 5 .   ? -7.363  -4.638  34.027  1.00 45.46  ? 559 HOH A O   1 
HETATM 4876 O  O   . HOH I 5 .   ? -25.004 -15.759 13.031  1.00 32.08  ? 560 HOH A O   1 
HETATM 4877 O  O   . HOH I 5 .   ? -0.702  -13.734 2.901   1.00 41.00  ? 561 HOH A O   1 
HETATM 4878 O  O   . HOH I 5 .   ? -5.703  -15.283 27.926  1.00 39.60  ? 562 HOH A O   1 
HETATM 4879 O  O   . HOH I 5 .   ? -12.853 -7.634  -3.036  1.00 27.14  ? 563 HOH A O   1 
HETATM 4880 O  O   . HOH I 5 .   ? 3.013   5.033   8.019   1.00 36.89  ? 564 HOH A O   1 
HETATM 4881 O  O   . HOH I 5 .   ? -7.646  -11.752 33.595  1.00 40.17  ? 565 HOH A O   1 
HETATM 4882 O  O   . HOH I 5 .   ? -5.156  -13.418 24.559  1.00 30.39  ? 566 HOH A O   1 
HETATM 4883 O  O   . HOH I 5 .   ? -12.963 -14.537 -0.149  1.00 38.32  ? 567 HOH A O   1 
HETATM 4884 O  O   . HOH I 5 .   ? -10.453 -9.618  -1.572  1.00 31.81  ? 568 HOH A O   1 
HETATM 4885 O  O   . HOH I 5 .   ? -9.381  -15.264 11.859  1.00 31.90  ? 569 HOH A O   1 
HETATM 4886 O  O   . HOH I 5 .   ? -14.722 -2.859  1.410   1.00 33.18  ? 570 HOH A O   1 
HETATM 4887 O  O   . HOH I 5 .   ? -23.267 -10.183 -2.888  1.00 31.48  ? 571 HOH A O   1 
HETATM 4888 O  O   . HOH I 5 .   ? -30.114 -15.920 -3.920  1.00 44.61  ? 572 HOH A O   1 
HETATM 4889 O  O   . HOH I 5 .   ? -11.138 -18.235 31.073  1.00 42.34  ? 573 HOH A O   1 
HETATM 4890 O  O   . HOH I 5 .   ? -25.147 -13.157 13.500  1.00 33.85  ? 574 HOH A O   1 
HETATM 4891 O  O   . HOH I 5 .   ? -27.242 -19.717 19.129  1.00 37.34  ? 575 HOH A O   1 
HETATM 4892 O  O   . HOH I 5 .   ? -32.248 -12.220 13.527  1.00 45.13  ? 576 HOH A O   1 
HETATM 4893 O  O   . HOH I 5 .   ? -15.738 -0.714  27.738  1.00 35.49  ? 577 HOH A O   1 
HETATM 4894 O  O   . HOH I 5 .   ? 2.682   -8.101  18.864  1.00 31.84  ? 578 HOH A O   1 
HETATM 4895 O  O   . HOH I 5 .   ? -5.981  -13.802 11.448  1.00 29.51  ? 579 HOH A O   1 
HETATM 4896 O  O   . HOH I 5 .   ? -11.302 -8.095  3.357   1.00 25.35  ? 580 HOH A O   1 
HETATM 4897 O  O   . HOH I 5 .   ? -0.258  -23.904 22.012  1.00 38.51  ? 581 HOH A O   1 
HETATM 4898 O  O   . HOH I 5 .   ? 1.370   -5.311  24.366  1.00 44.57  ? 582 HOH A O   1 
HETATM 4899 O  O   . HOH I 5 .   ? -8.052  10.167  21.954  1.00 47.62  ? 583 HOH A O   1 
HETATM 4900 O  O   . HOH I 5 .   ? -16.149 -13.172 1.235   1.00 36.55  ? 584 HOH A O   1 
HETATM 4901 O  O   . HOH I 5 .   ? -18.993 -17.204 9.961   1.00 29.95  ? 585 HOH A O   1 
HETATM 4902 O  O   . HOH I 5 .   ? 2.266   -2.160  1.016   1.00 37.21  ? 586 HOH A O   1 
HETATM 4903 O  O   . HOH I 5 .   ? -22.238 -30.307 8.612   1.00 43.17  ? 587 HOH A O   1 
HETATM 4904 O  O   . HOH I 5 .   ? -34.584 -15.379 20.027  1.00 49.88  ? 588 HOH A O   1 
HETATM 4905 O  O   . HOH I 5 .   ? -13.271 -24.144 21.556  1.00 32.31  ? 589 HOH A O   1 
HETATM 4906 O  O   . HOH I 5 .   ? -14.446 2.830   21.330  1.00 36.93  ? 590 HOH A O   1 
HETATM 4907 O  O   . HOH I 5 .   ? -23.260 12.207  17.435  1.00 57.89  ? 591 HOH A O   1 
HETATM 4908 O  O   . HOH I 5 .   ? -15.503 -24.744 18.928  1.00 35.03  ? 592 HOH A O   1 
HETATM 4909 O  O   . HOH I 5 .   ? 6.078   -2.846  13.369  1.00 49.13  ? 593 HOH A O   1 
HETATM 4910 O  O   . HOH I 5 .   ? -6.228  -22.269 11.618  1.00 46.26  ? 594 HOH A O   1 
HETATM 4911 O  O   . HOH I 5 .   ? -35.391 -3.505  10.852  1.00 62.19  ? 595 HOH A O   1 
HETATM 4912 O  O   . HOH I 5 .   ? -29.025 -18.886 20.806  1.00 43.26  ? 596 HOH A O   1 
HETATM 4913 O  O   . HOH I 5 .   ? -12.602 -21.923 5.562   1.00 35.08  ? 597 HOH A O   1 
HETATM 4914 O  O   . HOH I 5 .   ? 4.748   -1.513  10.923  1.00 42.31  ? 598 HOH A O   1 
HETATM 4915 O  O   . HOH I 5 .   ? -28.500 -12.413 -6.664  1.00 41.85  ? 599 HOH A O   1 
HETATM 4916 O  O   . HOH I 5 .   ? -18.083 2.830   2.195   1.00 36.60  ? 600 HOH A O   1 
HETATM 4917 O  O   . HOH I 5 .   ? 4.409   2.775   9.113   1.00 43.86  ? 601 HOH A O   1 
HETATM 4918 O  O   . HOH I 5 .   ? -34.620 -8.392  19.420  1.00 55.38  ? 602 HOH A O   1 
HETATM 4919 O  O   . HOH I 5 .   ? -30.314 -0.057  8.156   1.00 43.34  ? 603 HOH A O   1 
HETATM 4920 O  O   . HOH I 5 .   ? -35.575 -11.363 21.266  1.00 49.32  ? 604 HOH A O   1 
HETATM 4921 O  O   . HOH I 5 .   ? -31.232 6.191   5.404   1.00 44.60  ? 605 HOH A O   1 
HETATM 4922 O  O   . HOH I 5 .   ? -26.655 9.794   12.852  1.00 58.32  ? 606 HOH A O   1 
HETATM 4923 O  O   . HOH I 5 .   ? -22.837 -7.399  -3.713  1.00 30.56  ? 607 HOH A O   1 
HETATM 4924 O  O   . HOH I 5 .   ? -1.040  -2.699  18.602  1.00 33.39  ? 608 HOH A O   1 
HETATM 4925 O  O   . HOH I 5 .   ? -4.382  -20.546 8.653   1.00 39.13  ? 609 HOH A O   1 
HETATM 4926 O  O   . HOH I 5 .   ? -15.930 3.621   2.417   1.00 47.43  ? 610 HOH A O   1 
HETATM 4927 O  O   . HOH I 5 .   ? -18.969 -4.855  -7.677  1.00 43.72  ? 611 HOH A O   1 
HETATM 4928 O  O   . HOH I 5 .   ? -33.092 -20.882 18.558  1.00 52.42  ? 612 HOH A O   1 
HETATM 4929 O  O   . HOH I 5 .   ? -10.276 -8.127  34.765  1.00 42.74  ? 613 HOH A O   1 
HETATM 4930 O  O   . HOH I 5 .   ? -13.043 -7.319  35.071  1.00 49.49  ? 614 HOH A O   1 
HETATM 4931 O  O   . HOH I 5 .   ? -18.343 6.452   21.155  1.00 46.30  ? 615 HOH A O   1 
HETATM 4932 O  O   . HOH I 5 .   ? 7.586   -5.613  16.519  1.00 47.67  ? 616 HOH A O   1 
HETATM 4933 O  O   . HOH I 5 .   ? -20.126 -27.855 -5.261  1.00 53.44  ? 617 HOH A O   1 
HETATM 4934 O  O   . HOH I 5 .   ? 11.118  -18.440 22.032  1.00 49.82  ? 618 HOH A O   1 
HETATM 4935 O  O   . HOH I 5 .   ? -28.518 -24.994 23.792  1.00 49.00  ? 619 HOH A O   1 
HETATM 4936 O  O   . HOH I 5 .   ? 5.462   -8.331  -2.060  1.00 37.39  ? 620 HOH A O   1 
HETATM 4937 O  O   . HOH I 5 .   ? 3.246   -7.423  21.253  1.00 39.80  ? 621 HOH A O   1 
HETATM 4938 O  O   . HOH I 5 .   ? -29.410 -3.442  4.692   1.00 46.83  ? 622 HOH A O   1 
HETATM 4939 O  O   . HOH I 5 .   ? -17.962 -10.380 31.132  1.00 43.07  ? 623 HOH A O   1 
HETATM 4940 O  O   . HOH I 5 .   ? -16.001 -26.368 21.152  1.00 39.77  ? 624 HOH A O   1 
HETATM 4941 O  O   . HOH I 5 .   ? -13.610 -26.246 23.005  1.00 46.18  ? 625 HOH A O   1 
HETATM 4942 O  O   . HOH I 5 .   ? -0.550  -22.083 4.626   1.00 55.82  ? 626 HOH A O   1 
HETATM 4943 O  O   . HOH I 5 .   ? -24.049 -20.966 34.046  1.00 47.01  ? 627 HOH A O   1 
HETATM 4944 O  O   . HOH I 5 .   ? -36.540 -9.193  21.388  1.00 50.20  ? 628 HOH A O   1 
HETATM 4945 O  O   . HOH J 5 .   ? 23.196  -10.042 19.423  1.00 40.28  ? 501 HOH B O   1 
HETATM 4946 O  O   . HOH J 5 .   ? 33.081  -0.477  14.363  1.00 52.24  ? 502 HOH B O   1 
HETATM 4947 O  O   . HOH J 5 .   ? 18.595  -19.942 29.576  1.00 46.86  ? 503 HOH B O   1 
HETATM 4948 O  O   . HOH J 5 .   ? 9.524   -1.190  -2.468  1.00 41.36  ? 504 HOH B O   1 
HETATM 4949 O  O   . HOH J 5 .   ? 41.846  -18.493 3.227   1.00 51.73  ? 505 HOH B O   1 
HETATM 4950 O  O   . HOH J 5 .   ? 36.944  -31.410 7.404   1.00 48.62  ? 506 HOH B O   1 
HETATM 4951 O  O   . HOH J 5 .   ? 31.098  -36.518 13.957  1.00 47.16  ? 507 HOH B O   1 
HETATM 4952 O  O   . HOH J 5 .   ? 41.334  -12.724 12.756  1.00 48.33  ? 508 HOH B O   1 
HETATM 4953 O  O   . HOH J 5 .   ? 28.668  -28.409 1.828   1.00 35.18  ? 509 HOH B O   1 
HETATM 4954 O  O   . HOH J 5 .   ? 12.407  -11.077 17.384  1.00 36.54  ? 510 HOH B O   1 
HETATM 4955 O  O   . HOH J 5 .   ? 24.361  -21.321 31.850  1.00 51.82  ? 511 HOH B O   1 
HETATM 4956 O  O   . HOH J 5 .   ? 38.895  -32.573 2.811   1.00 47.00  ? 512 HOH B O   1 
HETATM 4957 O  O   . HOH J 5 .   ? 31.104  -32.562 17.593  1.00 45.87  ? 513 HOH B O   1 
HETATM 4958 O  O   . HOH J 5 .   ? 21.763  -19.984 -5.322  1.00 34.93  ? 514 HOH B O   1 
HETATM 4959 O  O   . HOH J 5 .   ? 12.043  -6.788  14.952  1.00 35.38  ? 515 HOH B O   1 
HETATM 4960 O  O   . HOH J 5 .   ? 12.179  -1.929  -5.718  1.00 39.02  ? 516 HOH B O   1 
HETATM 4961 O  O   . HOH J 5 .   ? 31.584  -11.302 -2.506  1.00 35.30  ? 517 HOH B O   1 
HETATM 4962 O  O   . HOH J 5 .   ? 16.920  -29.362 20.239  1.00 48.52  ? 518 HOH B O   1 
HETATM 4963 O  O   . HOH J 5 .   ? 4.385   -28.133 16.595  1.00 42.77  ? 519 HOH B O   1 
HETATM 4964 O  O   . HOH J 5 .   ? 36.797  -6.515  3.186   1.00 53.98  ? 520 HOH B O   1 
HETATM 4965 O  O   . HOH J 5 .   ? 16.135  -12.315 21.264  1.00 54.62  ? 521 HOH B O   1 
HETATM 4966 O  O   . HOH J 5 .   ? 23.515  -28.914 -8.196  1.00 45.19  ? 522 HOH B O   1 
HETATM 4967 O  O   . HOH J 5 .   ? 36.707  -10.831 -11.732 1.00 47.39  ? 523 HOH B O   1 
HETATM 4968 O  O   . HOH J 5 .   ? 24.656  -15.894 23.644  1.00 36.47  ? 524 HOH B O   1 
HETATM 4969 O  O   . HOH J 5 .   ? 36.166  -18.387 8.990   1.00 37.71  ? 525 HOH B O   1 
HETATM 4970 O  O   . HOH J 5 .   ? 17.593  -16.674 21.138  1.00 43.19  ? 526 HOH B O   1 
HETATM 4971 O  O   . HOH J 5 .   ? 26.456  -22.368 22.484  1.00 38.56  ? 527 HOH B O   1 
HETATM 4972 O  O   . HOH J 5 .   ? 7.961   -1.409  2.045   1.00 36.95  ? 528 HOH B O   1 
HETATM 4973 O  O   . HOH J 5 .   ? 34.690  -11.793 15.726  1.00 41.11  ? 529 HOH B O   1 
HETATM 4974 O  O   . HOH J 5 .   ? 15.651  -29.588 -7.600  1.00 47.75  ? 530 HOH B O   1 
HETATM 4975 O  O   . HOH J 5 .   ? 21.011  -16.469 -15.372 1.00 47.26  ? 531 HOH B O   1 
HETATM 4976 O  O   . HOH J 5 .   ? 20.143  -22.296 -5.007  1.00 38.57  ? 532 HOH B O   1 
HETATM 4977 O  O   . HOH J 5 .   ? 8.227   -29.404 10.848  1.00 40.56  ? 533 HOH B O   1 
HETATM 4978 O  O   . HOH J 5 .   ? 27.075  -30.348 2.648   1.00 37.99  ? 534 HOH B O   1 
HETATM 4979 O  O   . HOH J 5 .   ? 43.204  -12.628 -1.937  1.00 62.71  ? 535 HOH B O   1 
HETATM 4980 O  O   . HOH J 5 .   ? 35.615  -19.613 1.496   1.00 39.82  ? 536 HOH B O   1 
HETATM 4981 O  O   . HOH J 5 .   ? 35.114  -16.153 12.534  1.00 34.47  ? 537 HOH B O   1 
HETATM 4982 O  O   . HOH J 5 .   ? 9.603   -31.758 5.985   1.00 50.14  ? 538 HOH B O   1 
HETATM 4983 O  O   . HOH J 5 .   ? 25.703  -31.157 19.893  1.00 43.52  ? 539 HOH B O   1 
HETATM 4984 O  O   . HOH J 5 .   ? 21.282  -4.765  7.302   1.00 29.10  ? 540 HOH B O   1 
HETATM 4985 O  O   . HOH J 5 .   ? 15.175  -26.715 8.019   1.00 29.46  ? 541 HOH B O   1 
HETATM 4986 O  O   . HOH J 5 .   ? 13.882  -26.064 -6.873  1.00 46.23  ? 542 HOH B O   1 
HETATM 4987 O  O   . HOH J 5 .   ? 18.495  -31.172 9.974   1.00 43.29  ? 543 HOH B O   1 
HETATM 4988 O  O   . HOH J 5 .   ? 21.944  -21.001 4.063   1.00 46.03  ? 544 HOH B O   1 
HETATM 4989 O  O   . HOH J 5 .   ? 32.663  -17.178 23.757  1.00 39.98  ? 545 HOH B O   1 
HETATM 4990 O  O   . HOH J 5 .   ? 19.460  -14.833 12.315  1.00 32.78  ? 546 HOH B O   1 
HETATM 4991 O  O   . HOH J 5 .   ? 38.287  3.931   13.598  1.00 48.41  ? 547 HOH B O   1 
HETATM 4992 O  O   . HOH J 5 .   ? 7.150   -19.927 4.147   1.00 32.36  ? 548 HOH B O   1 
HETATM 4993 O  O   . HOH J 5 .   ? 10.955  -5.910  12.792  1.00 36.90  ? 549 HOH B O   1 
HETATM 4994 O  O   . HOH J 5 .   ? 28.834  -19.369 11.598  1.00 30.14  ? 550 HOH B O   1 
HETATM 4995 O  O   . HOH J 5 .   ? 41.682  -18.398 -5.066  1.00 53.18  ? 551 HOH B O   1 
HETATM 4996 O  O   . HOH J 5 .   ? 29.724  -12.912 10.779  1.00 37.66  ? 552 HOH B O   1 
HETATM 4997 O  O   . HOH J 5 .   ? 18.580  -18.635 27.128  1.00 43.74  ? 553 HOH B O   1 
HETATM 4998 O  O   . HOH J 5 .   ? 19.521  -30.210 19.528  1.00 41.69  ? 554 HOH B O   1 
HETATM 4999 O  O   . HOH J 5 .   ? 29.109  -13.387 14.540  1.00 33.67  ? 555 HOH B O   1 
HETATM 5000 O  O   . HOH J 5 .   ? 33.278  1.057   10.775  1.00 42.95  ? 556 HOH B O   1 
HETATM 5001 O  O   . HOH J 5 .   ? 39.166  -24.293 13.754  1.00 42.29  ? 557 HOH B O   1 
HETATM 5002 O  O   . HOH J 5 .   ? 15.867  -13.985 11.150  1.00 27.42  ? 558 HOH B O   1 
HETATM 5003 O  O   . HOH J 5 .   ? 13.766  -22.269 22.275  1.00 40.96  ? 559 HOH B O   1 
HETATM 5004 O  O   . HOH J 5 .   ? 5.743   -8.664  -4.689  1.00 35.84  ? 560 HOH B O   1 
HETATM 5005 O  O   . HOH J 5 .   ? 26.340  -33.372 5.502   1.00 42.67  ? 561 HOH B O   1 
HETATM 5006 O  O   . HOH J 5 .   ? 22.935  -1.497  -8.011  1.00 31.39  ? 562 HOH B O   1 
HETATM 5007 O  O   . HOH J 5 .   ? 26.265  -1.491  -0.268  1.00 41.23  ? 563 HOH B O   1 
HETATM 5008 O  O   . HOH J 5 .   ? 41.143  -17.492 -7.369  1.00 53.41  ? 564 HOH B O   1 
HETATM 5009 O  O   . HOH J 5 .   ? 16.219  -1.145  12.131  1.00 43.29  ? 565 HOH B O   1 
HETATM 5010 O  O   . HOH J 5 .   ? 37.430  -22.760 15.117  1.00 41.95  ? 566 HOH B O   1 
HETATM 5011 O  O   . HOH J 5 .   ? 20.667  -4.136  -12.066 1.00 43.86  ? 567 HOH B O   1 
HETATM 5012 O  O   . HOH J 5 .   ? 17.281  -20.336 5.194   1.00 26.57  ? 568 HOH B O   1 
HETATM 5013 O  O   . HOH J 5 .   ? 31.592  -12.879 -0.433  1.00 38.08  ? 569 HOH B O   1 
HETATM 5014 O  O   . HOH J 5 .   ? 24.698  -2.072  2.614   1.00 34.49  ? 570 HOH B O   1 
HETATM 5015 O  O   . HOH J 5 .   ? 41.484  -22.399 13.858  1.00 46.18  ? 571 HOH B O   1 
HETATM 5016 O  O   . HOH J 5 .   ? 32.869  2.178   7.936   1.00 34.31  ? 572 HOH B O   1 
HETATM 5017 O  O   . HOH J 5 .   ? 35.315  -15.973 9.772   1.00 41.31  ? 573 HOH B O   1 
HETATM 5018 O  O   . HOH J 5 .   ? 20.607  -0.394  9.695   1.00 31.91  ? 574 HOH B O   1 
HETATM 5019 O  O   . HOH J 5 .   ? 40.146  0.695   16.144  1.00 51.82  ? 575 HOH B O   1 
HETATM 5020 O  O   . HOH J 5 .   ? 23.315  -25.946 19.075  1.00 34.80  ? 576 HOH B O   1 
HETATM 5021 O  O   . HOH J 5 .   ? 9.482   -15.878 -13.031 1.00 47.00  ? 577 HOH B O   1 
HETATM 5022 O  O   . HOH J 5 .   ? 28.781  -25.680 21.399  1.00 43.72  ? 578 HOH B O   1 
HETATM 5023 O  O   . HOH J 5 .   ? -1.282  -24.822 13.035  1.00 39.64  ? 579 HOH B O   1 
HETATM 5024 O  O   . HOH J 5 .   ? 20.008  -27.013 23.104  1.00 50.97  ? 580 HOH B O   1 
HETATM 5025 O  O   . HOH J 5 .   ? 25.460  -23.588 20.197  1.00 35.14  ? 581 HOH B O   1 
HETATM 5026 O  O   . HOH J 5 .   ? 15.700  -30.466 9.196   1.00 38.77  ? 582 HOH B O   1 
HETATM 5027 O  O   . HOH J 5 .   ? 11.005  -18.667 -1.153  1.00 34.54  ? 583 HOH B O   1 
HETATM 5028 O  O   . HOH J 5 .   ? 6.915   -6.819  -6.557  1.00 34.83  ? 584 HOH B O   1 
HETATM 5029 O  O   . HOH J 5 .   ? 13.613  -29.336 17.775  1.00 46.88  ? 585 HOH B O   1 
HETATM 5030 O  O   . HOH J 5 .   ? 25.476  -27.441 -4.934  1.00 38.30  ? 586 HOH B O   1 
HETATM 5031 O  O   . HOH J 5 .   ? 42.737  -22.262 16.133  1.00 51.01  ? 587 HOH B O   1 
HETATM 5032 O  O   . HOH J 5 .   ? 17.308  -35.349 4.604   1.00 45.42  ? 588 HOH B O   1 
HETATM 5033 O  O   . HOH J 5 .   ? 41.342  -6.263  3.611   1.00 59.88  ? 589 HOH B O   1 
HETATM 5034 O  O   . HOH J 5 .   ? 18.083  -19.162 -14.588 1.00 49.86  ? 590 HOH B O   1 
HETATM 5035 O  O   . HOH J 5 .   ? 12.868  -35.686 2.972   1.00 48.01  ? 591 HOH B O   1 
HETATM 5036 O  O   . HOH J 5 .   ? 39.814  -8.301  -4.029  1.00 52.60  ? 592 HOH B O   1 
HETATM 5037 O  O   . HOH J 5 .   ? 25.870  -1.644  -4.186  1.00 36.74  ? 593 HOH B O   1 
HETATM 5038 O  O   . HOH J 5 .   ? 22.785  -35.591 -0.138  1.00 43.33  ? 594 HOH B O   1 
HETATM 5039 O  O   . HOH J 5 .   ? 19.943  -35.624 1.098   1.00 49.64  ? 595 HOH B O   1 
HETATM 5040 O  O   . HOH J 5 .   ? 24.077  -20.271 -7.153  1.00 39.90  ? 596 HOH B O   1 
HETATM 5041 O  O   . HOH J 5 .   ? 27.976  -32.785 3.579   1.00 42.15  ? 597 HOH B O   1 
HETATM 5042 O  O   . HOH J 5 .   ? 28.200  -19.285 -10.695 1.00 48.79  ? 598 HOH B O   1 
HETATM 5043 O  O   . HOH J 5 .   ? 41.667  -11.580 -5.403  1.00 57.17  ? 599 HOH B O   1 
HETATM 5044 O  O   . HOH J 5 .   ? 5.270   -10.771 -1.029  1.00 37.37  ? 600 HOH B O   1 
HETATM 5045 O  O   . HOH J 5 .   ? 44.952  -9.299  24.217  1.00 51.96  ? 601 HOH B O   1 
HETATM 5046 O  O   . HOH J 5 .   ? 14.976  -18.887 22.886  1.00 62.04  ? 602 HOH B O   1 
HETATM 5047 O  O   . HOH J 5 .   ? 27.973  -1.780  -3.346  1.00 41.63  ? 603 HOH B O   1 
HETATM 5048 O  O   . HOH J 5 .   ? 38.547  -28.173 19.540  1.00 51.52  ? 604 HOH B O   1 
HETATM 5049 O  O   . HOH J 5 .   ? 30.915  -22.187 24.022  1.00 47.19  ? 605 HOH B O   1 
HETATM 5050 O  O   . HOH J 5 .   ? 31.513  -34.056 -7.561  1.00 52.82  ? 606 HOH B O   1 
HETATM 5051 O  O   . HOH J 5 .   ? 21.464  -34.030 12.368  1.00 49.03  ? 607 HOH B O   1 
HETATM 5052 O  O   . HOH J 5 .   ? 45.833  -22.955 6.690   1.00 51.65  ? 608 HOH B O   1 
HETATM 5053 O  O   . HOH J 5 .   ? 40.472  -7.681  -1.495  1.00 61.65  ? 609 HOH B O   1 
HETATM 5054 O  O   . HOH J 5 .   ? 4.570   0.366   8.709   1.00 36.09  ? 610 HOH B O   1 
HETATM 5055 O  O   . HOH J 5 .   ? 9.644   3.011   6.712   1.00 43.70  ? 611 HOH B O   1 
HETATM 5056 O  O   . HOH J 5 .   ? 29.371  -23.307 22.576  1.00 48.11  ? 612 HOH B O   1 
HETATM 5057 O  O   . HOH J 5 .   ? 34.069  -33.204 -5.105  1.00 55.61  ? 613 HOH B O   1 
HETATM 5058 O  O   . HOH J 5 .   ? 10.900  -21.552 22.115  1.00 57.38  ? 614 HOH B O   1 
HETATM 5059 O  O   . HOH J 5 .   ? 9.522   -16.892 -4.009  1.00 58.90  ? 615 HOH B O   1 
HETATM 5060 O  O   . HOH J 5 .   ? 29.835  -27.260 22.960  1.00 47.34  ? 616 HOH B O   1 
HETATM 5061 O  O   . HOH J 5 .   ? 29.474  -36.227 -11.137 1.00 50.27  ? 617 HOH B O   1 
HETATM 5062 O  O   . HOH J 5 .   ? 26.123  -26.115 21.238  1.00 40.48  ? 618 HOH B O   1 
HETATM 5063 O  O   . HOH J 5 .   ? 6.147   -22.139 3.038   1.00 42.60  ? 619 HOH B O   1 
HETATM 5064 O  O   . HOH J 5 .   ? 39.468  -5.054  3.041   1.00 62.83  ? 620 HOH B O   1 
HETATM 5065 O  O   . HOH J 5 .   ? 5.168   4.687   6.010   1.00 40.62  ? 621 HOH B O   1 
HETATM 5066 O  O   . HOH J 5 .   ? 23.988  -27.505 20.958  1.00 52.92  ? 622 HOH B O   1 
HETATM 5067 O  O   . HOH J 5 .   ? 43.219  -7.619  3.201   1.00 66.16  ? 623 HOH B O   1 
HETATM 5068 O  O   . HOH J 5 .   ? 46.184  -26.074 4.845   1.00 57.68  ? 624 HOH B O   1 
HETATM 5069 O  O   . HOH J 5 .   ? 21.607  -1.325  -11.131 1.00 38.36  ? 625 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . SER A 26  ? 0.7560 0.8839 0.6261 0.0419  -0.0232 -0.0851 2   SER A N   
2    C  CA  . SER A 26  ? 0.7852 0.9205 0.6521 0.0445  -0.0206 -0.0709 2   SER A CA  
3    C  C   . SER A 26  ? 0.8514 0.9752 0.7269 0.0429  -0.0153 -0.0613 2   SER A C   
4    O  O   . SER A 26  ? 0.8584 0.9818 0.7373 0.0424  -0.0144 -0.0500 2   SER A O   
5    C  CB  . SER A 26  ? 0.7747 0.9251 0.6280 0.0503  -0.0181 -0.0698 2   SER A CB  
6    O  OG  . SER A 26  ? 0.8117 0.9586 0.6639 0.0524  -0.0121 -0.0711 2   SER A OG  
7    N  N   . LEU A 27  ? 0.7537 0.8682 0.6332 0.0421  -0.0120 -0.0661 3   LEU A N   
8    C  CA  . LEU A 27  ? 0.7192 0.8227 0.6075 0.0400  -0.0079 -0.0584 3   LEU A CA  
9    C  C   . LEU A 27  ? 0.7159 0.8078 0.6146 0.0349  -0.0106 -0.0567 3   LEU A C   
10   O  O   . LEU A 27  ? 0.6597 0.7421 0.5656 0.0327  -0.0078 -0.0511 3   LEU A O   
11   C  CB  . LEU A 27  ? 0.6594 0.7570 0.5497 0.0407  -0.0042 -0.0643 3   LEU A CB  
12   C  CG  . LEU A 27  ? 0.7240 0.8323 0.6050 0.0461  0.0000  -0.0656 3   LEU A CG  
13   C  CD1 . LEU A 27  ? 0.6865 0.7878 0.5712 0.0468  0.0031  -0.0730 3   LEU A CD1 
14   C  CD2 . LEU A 27  ? 0.6626 0.7777 0.5418 0.0483  0.0044  -0.0520 3   LEU A CD2 
15   N  N   . ASN A 28  ? 0.7122 0.8053 0.6119 0.0330  -0.0158 -0.0615 4   ASN A N   
16   C  CA  . ASN A 28  ? 0.7217 0.8050 0.6311 0.0286  -0.0179 -0.0598 4   ASN A CA  
17   C  C   . ASN A 28  ? 0.6409 0.7235 0.5526 0.0286  -0.0162 -0.0473 4   ASN A C   
18   O  O   . ASN A 28  ? 0.6351 0.7277 0.5412 0.0316  -0.0161 -0.0409 4   ASN A O   
19   C  CB  . ASN A 28  ? 0.7998 0.8868 0.7102 0.0269  -0.0239 -0.0670 4   ASN A CB  
20   C  CG  . ASN A 28  ? 0.8626 0.9460 0.7743 0.0254  -0.0258 -0.0800 4   ASN A CG  
21   O  OD1 . ASN A 28  ? 0.9139 0.9858 0.8327 0.0230  -0.0240 -0.0827 4   ASN A OD1 
22   N  ND2 . ASN A 28  ? 0.8957 0.9890 0.8008 0.0269  -0.0297 -0.0880 4   ASN A ND2 
23   N  N   . GLY A 29  ? 0.5623 0.6331 0.4823 0.0253  -0.0148 -0.0440 5   GLY A N   
24   C  CA  . GLY A 29  ? 0.5866 0.6546 0.5097 0.0250  -0.0132 -0.0335 5   GLY A CA  
25   C  C   . GLY A 29  ? 0.5081 0.5776 0.4288 0.0270  -0.0087 -0.0253 5   GLY A C   
26   O  O   . GLY A 29  ? 0.5001 0.5697 0.4223 0.0274  -0.0074 -0.0162 5   GLY A O   
27   N  N   . LYS A 30  ? 0.5185 0.5892 0.4366 0.0282  -0.0060 -0.0280 6   LYS A N   
28   C  CA  . LYS A 30  ? 0.4844 0.5569 0.4018 0.0297  -0.0015 -0.0201 6   LYS A CA  
29   C  C   . LYS A 30  ? 0.4857 0.5462 0.4109 0.0262  0.0005  -0.0189 6   LYS A C   
30   O  O   . LYS A 30  ? 0.4921 0.5469 0.4200 0.0247  0.0000  -0.0260 6   LYS A O   
31   C  CB  . LYS A 30  ? 0.5020 0.5845 0.4120 0.0337  0.0007  -0.0233 6   LYS A CB  
32   C  CG  . LYS A 30  ? 0.5554 0.6514 0.4559 0.0375  -0.0013 -0.0244 6   LYS A CG  
33   C  CD  . LYS A 30  ? 0.5327 0.6351 0.4319 0.0392  -0.0001 -0.0123 6   LYS A CD  
34   C  CE  . LYS A 30  ? 0.5832 0.7014 0.4720 0.0437  -0.0016 -0.0121 6   LYS A CE  
35   N  NZ  . LYS A 30  ? 0.6904 0.8111 0.5774 0.0430  -0.0076 -0.0190 6   LYS A NZ  
36   N  N   . VAL A 31  ? 0.4260 0.4829 0.3551 0.0250  0.0027  -0.0099 7   VAL A N   
37   C  CA  . VAL A 31  ? 0.4303 0.4771 0.3665 0.0215  0.0041  -0.0080 7   VAL A CA  
38   C  C   . VAL A 31  ? 0.3953 0.4463 0.3323 0.0226  0.0081  -0.0019 7   VAL A C   
39   O  O   . VAL A 31  ? 0.4027 0.4596 0.3382 0.0243  0.0101  0.0059  7   VAL A O   
40   C  CB  . VAL A 31  ? 0.4234 0.4616 0.3645 0.0185  0.0030  -0.0035 7   VAL A CB  
41   C  CG1 . VAL A 31  ? 0.3676 0.3962 0.3149 0.0147  0.0040  -0.0024 7   VAL A CG1 
42   C  CG2 . VAL A 31  ? 0.4115 0.4471 0.3525 0.0177  -0.0005 -0.0088 7   VAL A CG2 
43   N  N   . ILE A 32  ? 0.4054 0.4534 0.3456 0.0216  0.0095  -0.0049 8   ILE A N   
44   C  CA  . ILE A 32  ? 0.3815 0.4334 0.3244 0.0222  0.0134  0.0007  8   ILE A CA  
45   C  C   . ILE A 32  ? 0.3552 0.3990 0.3058 0.0179  0.0134  0.0070  8   ILE A C   
46   O  O   . ILE A 32  ? 0.3780 0.4126 0.3326 0.0145  0.0113  0.0038  8   ILE A O   
47   C  CB  . ILE A 32  ? 0.3999 0.4529 0.3437 0.0236  0.0148  -0.0053 8   ILE A CB  
48   C  CG1 . ILE A 32  ? 0.3847 0.4451 0.3207 0.0279  0.0146  -0.0129 8   ILE A CG1 
49   C  CG2 . ILE A 32  ? 0.3960 0.4536 0.3442 0.0241  0.0189  0.0011  8   ILE A CG2 
50   C  CD1 . ILE A 32  ? 0.3709 0.4293 0.3085 0.0291  0.0154  -0.0208 8   ILE A CD1 
51   N  N   . ILE A 33  ? 0.3574 0.4048 0.3100 0.0179  0.0158  0.0159  9   ILE A N   
52   C  CA  . ILE A 33  ? 0.3513 0.3918 0.3118 0.0136  0.0161  0.0218  9   ILE A CA  
53   C  C   . ILE A 33  ? 0.3778 0.4237 0.3431 0.0135  0.0193  0.0253  9   ILE A C   
54   O  O   . ILE A 33  ? 0.3706 0.4265 0.3344 0.0166  0.0228  0.0304  9   ILE A O   
55   C  CB  . ILE A 33  ? 0.3647 0.4043 0.3267 0.0130  0.0167  0.0297  9   ILE A CB  
56   C  CG1 . ILE A 33  ? 0.3426 0.3772 0.3009 0.0133  0.0137  0.0266  9   ILE A CG1 
57   C  CG2 . ILE A 33  ? 0.3275 0.3597 0.2983 0.0082  0.0170  0.0350  9   ILE A CG2 
58   C  CD1 . ILE A 33  ? 0.3628 0.3973 0.3224 0.0139  0.0146  0.0346  9   ILE A CD1 
59   N  N   . THR A 34  ? 0.3305 0.3706 0.3016 0.0103  0.0181  0.0231  10  THR A N   
60   C  CA  . THR A 34  ? 0.3578 0.4021 0.3360 0.0091  0.0205  0.0276  10  THR A CA  
61   C  C   . THR A 34  ? 0.3581 0.3971 0.3438 0.0041  0.0198  0.0344  10  THR A C   
62   O  O   . THR A 34  ? 0.3387 0.3676 0.3251 0.0006  0.0166  0.0323  10  THR A O   
63   C  CB  . THR A 34  ? 0.3673 0.4093 0.3484 0.0085  0.0193  0.0219  10  THR A CB  
64   O  OG1 . THR A 34  ? 0.3772 0.4230 0.3522 0.0131  0.0201  0.0151  10  THR A OG1 
65   C  CG2 . THR A 34  ? 0.3858 0.4330 0.3754 0.0073  0.0215  0.0272  10  THR A CG2 
66   N  N   . CYS A 35  ? 0.3698 0.4156 0.3614 0.0037  0.0230  0.0423  11  CYS A N   
67   C  CA  . CYS A 35  ? 0.3870 0.4280 0.3876 -0.0016 0.0223  0.0485  11  CYS A CA  
68   C  C   . CYS A 35  ? 0.3863 0.4318 0.3958 -0.0039 0.0230  0.0509  11  CYS A C   
69   O  O   . CYS A 35  ? 0.3987 0.4552 0.4103 -0.0009 0.0271  0.0551  11  CYS A O   
70   C  CB  . CYS A 35  ? 0.3978 0.4424 0.4000 -0.0009 0.0252  0.0574  11  CYS A CB  
71   S  SG  . CYS A 35  ? 0.4534 0.4881 0.4668 -0.0081 0.0235  0.0632  11  CYS A SG  
72   N  N   . ALA A 36  ? 0.3659 0.4037 0.3804 -0.0089 0.0192  0.0483  12  ALA A N   
73   C  CA  . ALA A 36  ? 0.3680 0.4098 0.3921 -0.0119 0.0188  0.0506  12  ALA A CA  
74   C  C   . ALA A 36  ? 0.3603 0.4000 0.3941 -0.0175 0.0183  0.0577  12  ALA A C   
75   O  O   . ALA A 36  ? 0.3665 0.3958 0.4015 -0.0222 0.0145  0.0556  12  ALA A O   
76   C  CB  . ALA A 36  ? 0.3412 0.3768 0.3647 -0.0139 0.0144  0.0436  12  ALA A CB  
77   N  N   . VAL A 37  ? 0.3437 0.3933 0.3848 -0.0171 0.0223  0.0659  13  VAL A N   
78   C  CA  . VAL A 37  ? 0.3486 0.3963 0.3983 -0.0215 0.0230  0.0736  13  VAL A CA  
79   C  C   . VAL A 37  ? 0.3846 0.4288 0.4461 -0.0289 0.0192  0.0747  13  VAL A C   
80   O  O   . VAL A 37  ? 0.3475 0.3846 0.4151 -0.0339 0.0178  0.0778  13  VAL A O   
81   C  CB  . VAL A 37  ? 0.3688 0.4290 0.4219 -0.0181 0.0292  0.0832  13  VAL A CB  
82   C  CG1 . VAL A 37  ? 0.3671 0.4297 0.4080 -0.0115 0.0321  0.0826  13  VAL A CG1 
83   C  CG2 . VAL A 37  ? 0.3577 0.4308 0.4162 -0.0161 0.0319  0.0852  13  VAL A CG2 
84   N  N   . THR A 38  ? 0.3569 0.4060 0.4223 -0.0299 0.0174  0.0723  14  THR A N   
85   C  CA  . THR A 38  ? 0.3800 0.4275 0.4570 -0.0372 0.0133  0.0737  14  THR A CA  
86   C  C   . THR A 38  ? 0.3735 0.4209 0.4499 -0.0383 0.0088  0.0674  14  THR A C   
87   O  O   . THR A 38  ? 0.3887 0.4289 0.4675 -0.0440 0.0033  0.0640  14  THR A O   
88   C  CB  . THR A 38  ? 0.3969 0.4561 0.4876 -0.0389 0.0169  0.0837  14  THR A CB  
89   O  OG1 . THR A 38  ? 0.3901 0.4456 0.4929 -0.0473 0.0126  0.0855  14  THR A OG1 
90   C  CG2 . THR A 38  ? 0.3973 0.4702 0.4908 -0.0347 0.0196  0.0851  14  THR A CG2 
91   N  N   . GLY A 39  ? 0.3460 0.4016 0.4196 -0.0329 0.0110  0.0660  15  GLY A N   
92   C  CA  . GLY A 39  ? 0.3249 0.3802 0.3982 -0.0334 0.0069  0.0609  15  GLY A CA  
93   C  C   . GLY A 39  ? 0.3736 0.4355 0.4602 -0.0387 0.0039  0.0648  15  GLY A C   
94   O  O   . GLY A 39  ? 0.3462 0.4160 0.4441 -0.0410 0.0060  0.0722  15  GLY A O   
95   N  N   . ALA A 40  ? 0.3578 0.4171 0.4435 -0.0406 -0.0014 0.0601  16  ALA A N   
96   C  CA  . ALA A 40  ? 0.3850 0.4512 0.4824 -0.0454 -0.0055 0.0629  16  ALA A CA  
97   C  C   . ALA A 40  ? 0.4040 0.4616 0.4990 -0.0516 -0.0129 0.0577  16  ALA A C   
98   O  O   . ALA A 40  ? 0.3740 0.4373 0.4779 -0.0562 -0.0175 0.0593  16  ALA A O   
99   C  CB  . ALA A 40  ? 0.3606 0.4373 0.4613 -0.0403 -0.0040 0.0639  16  ALA A CB  
100  N  N   . ILE A 41  ? 0.3775 0.4224 0.4607 -0.0517 -0.0144 0.0514  17  ILE A N   
101  C  CA  . ILE A 41  ? 0.4018 0.4388 0.4803 -0.0564 -0.0209 0.0456  17  ILE A CA  
102  C  C   . ILE A 41  ? 0.4226 0.4524 0.5050 -0.0635 -0.0238 0.0451  17  ILE A C   
103  O  O   . ILE A 41  ? 0.3943 0.4257 0.4833 -0.0698 -0.0293 0.0446  17  ILE A O   
104  C  CB  . ILE A 41  ? 0.4124 0.4401 0.4764 -0.0522 -0.0207 0.0388  17  ILE A CB  
105  C  CG1 . ILE A 41  ? 0.4243 0.4583 0.4859 -0.0457 -0.0182 0.0389  17  ILE A CG1 
106  C  CG2 . ILE A 41  ? 0.4047 0.4246 0.4630 -0.0568 -0.0268 0.0330  17  ILE A CG2 
107  C  CD1 . ILE A 41  ? 0.4569 0.5005 0.5263 -0.0466 -0.0215 0.0414  17  ILE A CD1 
108  N  N   . HIS A 42  ? 0.3991 0.4209 0.4779 -0.0626 -0.0203 0.0452  18  HIS A N   
109  C  CA  . HIS A 42  ? 0.3957 0.4103 0.4802 -0.0690 -0.0221 0.0456  18  HIS A CA  
110  C  C   . HIS A 42  ? 0.4083 0.4328 0.5092 -0.0734 -0.0220 0.0532  18  HIS A C   
111  O  O   . HIS A 42  ? 0.3838 0.4205 0.4908 -0.0700 -0.0183 0.0594  18  HIS A O   
112  C  CB  . HIS A 42  ? 0.3700 0.3758 0.4492 -0.0662 -0.0175 0.0462  18  HIS A CB  
113  C  CG  . HIS A 42  ? 0.4100 0.4057 0.4748 -0.0627 -0.0179 0.0388  18  HIS A CG  
114  N  ND1 . HIS A 42  ? 0.3937 0.3870 0.4508 -0.0566 -0.0131 0.0392  18  HIS A ND1 
115  C  CD2 . HIS A 42  ? 0.3801 0.3681 0.4370 -0.0645 -0.0224 0.0312  18  HIS A CD2 
116  C  CE1 . HIS A 42  ? 0.4016 0.3863 0.4477 -0.0550 -0.0146 0.0323  18  HIS A CE1 
117  N  NE2 . HIS A 42  ? 0.4320 0.4132 0.4775 -0.0595 -0.0199 0.0275  18  HIS A NE2 
118  N  N   . THR A 43  ? 0.3714 0.3908 0.4802 -0.0812 -0.0261 0.0526  19  THR A N   
119  C  CA  . THR A 43  ? 0.4095 0.4374 0.5354 -0.0868 -0.0268 0.0595  19  THR A CA  
120  C  C   . THR A 43  ? 0.4170 0.4360 0.5498 -0.0910 -0.0250 0.0623  19  THR A C   
121  O  O   . THR A 43  ? 0.4381 0.4431 0.5626 -0.0911 -0.0254 0.0569  19  THR A O   
122  C  CB  . THR A 43  ? 0.4193 0.4513 0.5513 -0.0936 -0.0348 0.0562  19  THR A CB  
123  O  OG1 . THR A 43  ? 0.4235 0.4420 0.5511 -0.0993 -0.0401 0.0483  19  THR A OG1 
124  C  CG2 . THR A 43  ? 0.3912 0.4305 0.5156 -0.0890 -0.0367 0.0534  19  THR A CG2 
125  N  N   . PRO A 44  ? 0.3849 0.4119 0.5337 -0.0945 -0.0229 0.0711  20  PRO A N   
126  C  CA  . PRO A 44  ? 0.4140 0.4330 0.5705 -0.0977 -0.0201 0.0756  20  PRO A CA  
127  C  C   . PRO A 44  ? 0.4296 0.4327 0.5864 -0.1047 -0.0256 0.0682  20  PRO A C   
128  O  O   . PRO A 44  ? 0.4547 0.4460 0.6105 -0.1045 -0.0228 0.0687  20  PRO A O   
129  C  CB  . PRO A 44  ? 0.4457 0.4782 0.6215 -0.1015 -0.0181 0.0862  20  PRO A CB  
130  C  CG  . PRO A 44  ? 0.4346 0.4829 0.6091 -0.0962 -0.0165 0.0887  20  PRO A CG  
131  C  CD  . PRO A 44  ? 0.4338 0.4782 0.5947 -0.0946 -0.0219 0.0784  20  PRO A CD  
132  N  N   . SER A 45  ? 0.4159 0.4184 0.5742 -0.1108 -0.0333 0.0613  21  SER A N   
133  C  CA  . SER A 45  ? 0.4378 0.4253 0.5962 -0.1177 -0.0387 0.0531  21  SER A CA  
134  C  C   . SER A 45  ? 0.4156 0.3884 0.5565 -0.1130 -0.0377 0.0449  21  SER A C   
135  O  O   . SER A 45  ? 0.4917 0.4500 0.6322 -0.1171 -0.0399 0.0390  21  SER A O   
136  C  CB  . SER A 45  ? 0.4217 0.4134 0.5831 -0.1246 -0.0475 0.0468  21  SER A CB  
137  O  OG  . SER A 45  ? 0.4721 0.4773 0.6516 -0.1299 -0.0490 0.0543  21  SER A OG  
138  N  N   . MET A 46  ? 0.3747 0.3509 0.5018 -0.1046 -0.0344 0.0442  22  MET A N   
139  C  CA  . MET A 46  ? 0.4341 0.3978 0.5451 -0.1001 -0.0336 0.0366  22  MET A CA  
140  C  C   . MET A 46  ? 0.4311 0.3856 0.5423 -0.0969 -0.0277 0.0404  22  MET A C   
141  O  O   . MET A 46  ? 0.4248 0.3659 0.5277 -0.0958 -0.0278 0.0341  22  MET A O   
142  C  CB  . MET A 46  ? 0.4203 0.3911 0.5180 -0.0927 -0.0322 0.0348  22  MET A CB  
143  C  CG  . MET A 46  ? 0.4310 0.4104 0.5273 -0.0948 -0.0380 0.0313  22  MET A CG  
144  S  SD  . MET A 46  ? 0.4674 0.4549 0.5510 -0.0858 -0.0354 0.0309  22  MET A SD  
145  C  CE  . MET A 46  ? 0.4660 0.4630 0.5513 -0.0898 -0.0429 0.0281  22  MET A CE  
146  N  N   . SER A 47  ? 0.4046 0.3667 0.5250 -0.0950 -0.0223 0.0510  23  SER A N   
147  C  CA  . SER A 47  ? 0.4408 0.3960 0.5614 -0.0913 -0.0164 0.0562  23  SER A CA  
148  C  C   . SER A 47  ? 0.4461 0.4110 0.5812 -0.0920 -0.0118 0.0688  23  SER A C   
149  O  O   . SER A 47  ? 0.4236 0.4035 0.5610 -0.0897 -0.0099 0.0742  23  SER A O   
150  C  CB  . SER A 47  ? 0.3938 0.3498 0.4988 -0.0821 -0.0127 0.0547  23  SER A CB  
151  O  OG  . SER A 47  ? 0.4586 0.4125 0.5650 -0.0780 -0.0068 0.0620  23  SER A OG  
152  N  N   . PRO A 48  ? 0.4505 0.4074 0.5959 -0.0949 -0.0095 0.0742  24  PRO A N   
153  C  CA  . PRO A 48  ? 0.4479 0.4146 0.6070 -0.0952 -0.0043 0.0875  24  PRO A CA  
154  C  C   . PRO A 48  ? 0.4478 0.4234 0.5988 -0.0858 0.0027  0.0947  24  PRO A C   
155  O  O   . PRO A 48  ? 0.4610 0.4470 0.6213 -0.0848 0.0077  0.1062  24  PRO A O   
156  C  CB  . PRO A 48  ? 0.4165 0.3693 0.5877 -0.1006 -0.0040 0.0902  24  PRO A CB  
157  C  CG  . PRO A 48  ? 0.4420 0.3787 0.6003 -0.0980 -0.0055 0.0805  24  PRO A CG  
158  C  CD  . PRO A 48  ? 0.4225 0.3610 0.5673 -0.0972 -0.0107 0.0689  24  PRO A CD  
159  N  N   . TYR A 49  ? 0.4523 0.4248 0.5864 -0.0791 0.0032  0.0884  25  TYR A N   
160  C  CA  . TYR A 49  ? 0.4572 0.4377 0.5822 -0.0704 0.0090  0.0937  25  TYR A CA  
161  C  C   . TYR A 49  ? 0.4313 0.4257 0.5485 -0.0658 0.0095  0.0919  25  TYR A C   
162  O  O   . TYR A 49  ? 0.4252 0.4278 0.5347 -0.0586 0.0141  0.0955  25  TYR A O   
163  C  CB  . TYR A 49  ? 0.4272 0.3960 0.5399 -0.0657 0.0094  0.0885  25  TYR A CB  
164  C  CG  . TYR A 49  ? 0.4700 0.4233 0.5902 -0.0699 0.0087  0.0888  25  TYR A CG  
165  C  CD1 . TYR A 49  ? 0.4939 0.4470 0.6260 -0.0706 0.0131  0.1002  25  TYR A CD1 
166  C  CD2 . TYR A 49  ? 0.4753 0.4140 0.5912 -0.0729 0.0040  0.0780  25  TYR A CD2 
167  C  CE1 . TYR A 49  ? 0.5198 0.4578 0.6601 -0.0743 0.0127  0.1007  25  TYR A CE1 
168  C  CE2 . TYR A 49  ? 0.4989 0.4226 0.6220 -0.0764 0.0037  0.0776  25  TYR A CE2 
169  C  CZ  . TYR A 49  ? 0.5382 0.4610 0.6740 -0.0771 0.0080  0.0889  25  TYR A CZ  
170  O  OH  . TYR A 49  ? 0.6059 0.5128 0.7500 -0.0804 0.0079  0.0886  25  TYR A OH  
171  N  N   . LEU A 50  ? 0.4590 0.4565 0.5781 -0.0696 0.0048  0.0864  26  LEU A N   
172  C  CA  . LEU A 50  ? 0.4417 0.4523 0.5556 -0.0653 0.0054  0.0854  26  LEU A CA  
173  C  C   . LEU A 50  ? 0.4104 0.4362 0.5340 -0.0636 0.0109  0.0965  26  LEU A C   
174  O  O   . LEU A 50  ? 0.4159 0.4453 0.5548 -0.0695 0.0106  0.1026  26  LEU A O   
175  C  CB  . LEU A 50  ? 0.4375 0.4483 0.5533 -0.0702 -0.0010 0.0784  26  LEU A CB  
176  C  CG  . LEU A 50  ? 0.4417 0.4642 0.5522 -0.0656 -0.0008 0.0765  26  LEU A CG  
177  C  CD1 . LEU A 50  ? 0.4066 0.4244 0.5002 -0.0590 -0.0003 0.0693  26  LEU A CD1 
178  C  CD2 . LEU A 50  ? 0.4198 0.4452 0.5366 -0.0713 -0.0070 0.0728  26  LEU A CD2 
179  N  N   . PRO A 51  ? 0.4289 0.4643 0.5444 -0.0557 0.0161  0.0993  27  PRO A N   
180  C  CA  . PRO A 51  ? 0.4235 0.4742 0.5474 -0.0534 0.0220  0.1100  27  PRO A CA  
181  C  C   . PRO A 51  ? 0.4416 0.5033 0.5750 -0.0560 0.0204  0.1106  27  PRO A C   
182  O  O   . PRO A 51  ? 0.4261 0.4889 0.5532 -0.0545 0.0173  0.1030  27  PRO A O   
183  C  CB  . PRO A 51  ? 0.4093 0.4664 0.5190 -0.0440 0.0269  0.1096  27  PRO A CB  
184  C  CG  . PRO A 51  ? 0.4121 0.4555 0.5089 -0.0423 0.0241  0.1017  27  PRO A CG  
185  C  CD  . PRO A 51  ? 0.3988 0.4311 0.4975 -0.0485 0.0172  0.0934  27  PRO A CD  
186  N  N   . VAL A 52  ? 0.4089 0.4793 0.5584 -0.0600 0.0228  0.1203  28  VAL A N   
187  C  CA  . VAL A 52  ? 0.4442 0.5262 0.6055 -0.0630 0.0213  0.1223  28  VAL A CA  
188  C  C   . VAL A 52  ? 0.4310 0.5307 0.5989 -0.0583 0.0290  0.1329  28  VAL A C   
189  O  O   . VAL A 52  ? 0.4200 0.5310 0.5856 -0.0533 0.0310  0.1318  28  VAL A O   
190  C  CB  . VAL A 52  ? 0.4307 0.5077 0.6081 -0.0736 0.0157  0.1235  28  VAL A CB  
191  C  CG1 . VAL A 52  ? 0.4312 0.5231 0.6230 -0.0766 0.0147  0.1276  28  VAL A CG1 
192  C  CG2 . VAL A 52  ? 0.3646 0.4257 0.5341 -0.0777 0.0080  0.1118  28  VAL A CG2 
193  N  N   . SER A 53  ? 0.4255 0.5279 0.6021 -0.0597 0.0338  0.1434  29  SER A N   
194  C  CA  . SER A 53  ? 0.4608 0.5809 0.6444 -0.0555 0.0416  0.1544  29  SER A CA  
195  C  C   . SER A 53  ? 0.4586 0.5848 0.6248 -0.0447 0.0473  0.1528  29  SER A C   
196  O  O   . SER A 53  ? 0.4459 0.5619 0.5963 -0.0411 0.0458  0.1453  29  SER A O   
197  C  CB  . SER A 53  ? 0.4442 0.5652 0.6413 -0.0596 0.0455  0.1669  29  SER A CB  
198  O  OG  . SER A 53  ? 0.4700 0.5829 0.6561 -0.0557 0.0483  0.1683  29  SER A OG  
199  N  N   . ALA A 54  ? 0.4412 0.5848 0.6108 -0.0395 0.0540  0.1596  30  ALA A N   
200  C  CA  . ALA A 54  ? 0.4440 0.5948 0.5975 -0.0292 0.0598  0.1580  30  ALA A CA  
201  C  C   . ALA A 54  ? 0.4587 0.6045 0.6028 -0.0264 0.0627  0.1618  30  ALA A C   
202  O  O   . ALA A 54  ? 0.4270 0.5697 0.5538 -0.0200 0.0632  0.1551  30  ALA A O   
203  C  CB  . ALA A 54  ? 0.4250 0.5960 0.5854 -0.0244 0.0673  0.1659  30  ALA A CB  
204  N  N   . SER A 55  ? 0.4390 0.5840 0.5950 -0.0312 0.0646  0.1727  31  SER A N   
205  C  CA  . SER A 55  ? 0.4714 0.6121 0.6198 -0.0284 0.0675  0.1777  31  SER A CA  
206  C  C   . SER A 55  ? 0.4497 0.5709 0.5894 -0.0308 0.0609  0.1683  31  SER A C   
207  O  O   . SER A 55  ? 0.4504 0.5681 0.5765 -0.0256 0.0621  0.1671  31  SER A O   
208  C  CB  . SER A 55  ? 0.4996 0.6448 0.6650 -0.0328 0.0718  0.1931  31  SER A CB  
209  O  OG  . SER A 55  ? 0.5552 0.6906 0.7375 -0.0431 0.0664  0.1932  31  SER A OG  
210  N  N   . GLU A 56  ? 0.4495 0.5584 0.5964 -0.0385 0.0539  0.1617  32  GLU A N   
211  C  CA  . GLU A 56  ? 0.4560 0.5472 0.5934 -0.0401 0.0478  0.1515  32  GLU A CA  
212  C  C   . GLU A 56  ? 0.4317 0.5226 0.5505 -0.0332 0.0465  0.1404  32  GLU A C   
213  O  O   . GLU A 56  ? 0.4215 0.5034 0.5282 -0.0303 0.0450  0.1353  32  GLU A O   
214  C  CB  . GLU A 56  ? 0.4572 0.5371 0.6051 -0.0493 0.0407  0.1460  32  GLU A CB  
215  C  CG  . GLU A 56  ? 0.5053 0.5799 0.6709 -0.0572 0.0405  0.1546  32  GLU A CG  
216  C  CD  . GLU A 56  ? 0.5194 0.5857 0.6961 -0.0666 0.0332  0.1486  32  GLU A CD  
217  O  OE1 . GLU A 56  ? 0.4788 0.5476 0.6514 -0.0668 0.0291  0.1402  32  GLU A OE1 
218  O  OE2 . GLU A 56  ? 0.5542 0.6117 0.7438 -0.0737 0.0316  0.1523  32  GLU A OE2 
219  N  N   . ILE A 57  ? 0.3986 0.4995 0.5161 -0.0305 0.0471  0.1368  33  ILE A N   
220  C  CA  . ILE A 57  ? 0.4537 0.5538 0.5553 -0.0245 0.0457  0.1260  33  ILE A CA  
221  C  C   . ILE A 57  ? 0.4345 0.5420 0.5231 -0.0161 0.0511  0.1280  33  ILE A C   
222  O  O   . ILE A 57  ? 0.4264 0.5278 0.5008 -0.0122 0.0492  0.1200  33  ILE A O   
223  C  CB  . ILE A 57  ? 0.4131 0.5215 0.5185 -0.0239 0.0450  0.1222  33  ILE A CB  
224  C  CG1 . ILE A 57  ? 0.3991 0.4987 0.5137 -0.0320 0.0379  0.1178  33  ILE A CG1 
225  C  CG2 . ILE A 57  ? 0.3633 0.4730 0.4534 -0.0165 0.0454  0.1128  33  ILE A CG2 
226  C  CD1 . ILE A 57  ? 0.4070 0.5159 0.5290 -0.0323 0.0370  0.1164  33  ILE A CD1 
227  N  N   . THR A 58  ? 0.4282 0.5496 0.5212 -0.0131 0.0579  0.1387  34  THR A N   
228  C  CA  . THR A 58  ? 0.4380 0.5679 0.5177 -0.0048 0.0630  0.1407  34  THR A CA  
229  C  C   . THR A 58  ? 0.4256 0.5466 0.4999 -0.0049 0.0620  0.1435  34  THR A C   
230  O  O   . THR A 58  ? 0.4433 0.5643 0.5028 0.0008  0.0620  0.1388  34  THR A O   
231  C  CB  . THR A 58  ? 0.4344 0.5826 0.5198 -0.0012 0.0709  0.1520  34  THR A CB  
232  O  OG1 . THR A 58  ? 0.4432 0.5919 0.5437 -0.0067 0.0729  0.1648  34  THR A OG1 
233  C  CG2 . THR A 58  ? 0.3930 0.5506 0.4842 -0.0003 0.0724  0.1493  34  THR A CG2 
234  N  N   . ASP A 59  ? 0.4381 0.5517 0.5249 -0.0113 0.0610  0.1511  35  ASP A N   
235  C  CA  . ASP A 59  ? 0.4471 0.5510 0.5304 -0.0113 0.0600  0.1537  35  ASP A CA  
236  C  C   . ASP A 59  ? 0.4345 0.5240 0.5071 -0.0115 0.0537  0.1407  35  ASP A C   
237  O  O   . ASP A 59  ? 0.4286 0.5155 0.4903 -0.0072 0.0534  0.1392  35  ASP A O   
238  C  CB  . ASP A 59  ? 0.4812 0.5777 0.5817 -0.0187 0.0598  0.1631  35  ASP A CB  
239  C  CG  . ASP A 59  ? 0.5763 0.6869 0.6873 -0.0180 0.0669  0.1784  35  ASP A CG  
240  O  OD1 . ASP A 59  ? 0.5924 0.7178 0.6946 -0.0107 0.0724  0.1828  35  ASP A OD1 
241  O  OD2 . ASP A 59  ? 0.5640 0.6710 0.6924 -0.0250 0.0670  0.1861  35  ASP A OD2 
242  N  N   . ALA A 60  ? 0.4397 0.5208 0.5156 -0.0164 0.0485  0.1317  36  ALA A N   
243  C  CA  . ALA A 60  ? 0.4452 0.5138 0.5112 -0.0164 0.0429  0.1195  36  ALA A CA  
244  C  C   . ALA A 60  ? 0.4221 0.4970 0.4723 -0.0090 0.0437  0.1126  36  ALA A C   
245  O  O   . ALA A 60  ? 0.3709 0.4391 0.4109 -0.0065 0.0414  0.1069  36  ALA A O   
246  C  CB  . ALA A 60  ? 0.3752 0.4362 0.4474 -0.0226 0.0376  0.1120  36  ALA A CB  
247  N  N   . ALA A 61  ? 0.3978 0.4858 0.4463 -0.0052 0.0470  0.1128  37  ALA A N   
248  C  CA  . ALA A 61  ? 0.4246 0.5183 0.4588 0.0017  0.0478  0.1052  37  ALA A CA  
249  C  C   . ALA A 61  ? 0.4230 0.5228 0.4473 0.0074  0.0508  0.1095  37  ALA A C   
250  O  O   . ALA A 61  ? 0.4069 0.5035 0.4194 0.0107  0.0485  0.1022  37  ALA A O   
251  C  CB  . ALA A 61  ? 0.3854 0.4917 0.4214 0.0046  0.0512  0.1047  37  ALA A CB  
252  N  N   . ILE A 62  ? 0.4051 0.5144 0.4346 0.0085  0.0560  0.1217  38  ILE A N   
253  C  CA  . ILE A 62  ? 0.4282 0.5454 0.4483 0.0143  0.0592  0.1273  38  ILE A CA  
254  C  C   . ILE A 62  ? 0.4509 0.5561 0.4687 0.0129  0.0554  0.1271  38  ILE A C   
255  O  O   . ILE A 62  ? 0.4292 0.5369 0.4350 0.0178  0.0547  0.1245  38  ILE A O   
256  C  CB  . ILE A 62  ? 0.4257 0.5560 0.4534 0.0155  0.0659  0.1420  38  ILE A CB  
257  C  CG1 . ILE A 62  ? 0.4288 0.5737 0.4553 0.0192  0.0705  0.1413  38  ILE A CG1 
258  C  CG2 . ILE A 62  ? 0.4308 0.5679 0.4505 0.0206  0.0687  0.1500  38  ILE A CG2 
259  C  CD1 . ILE A 62  ? 0.4318 0.5882 0.4708 0.0182  0.0768  0.1553  38  ILE A CD1 
260  N  N   . GLY A 63  ? 0.4224 0.5147 0.4519 0.0062  0.0529  0.1295  39  GLY A N   
261  C  CA  . GLY A 63  ? 0.4106 0.4905 0.4386 0.0051  0.0496  0.1287  39  GLY A CA  
262  C  C   . GLY A 63  ? 0.4406 0.5130 0.4577 0.0064  0.0446  0.1153  39  GLY A C   
263  O  O   . GLY A 63  ? 0.3991 0.4686 0.4091 0.0093  0.0431  0.1141  39  GLY A O   
264  N  N   . ALA A 64  ? 0.4031 0.4729 0.4195 0.0044  0.0420  0.1056  40  ALA A N   
265  C  CA  . ALA A 64  ? 0.4275 0.4904 0.4347 0.0054  0.0375  0.0933  40  ALA A CA  
266  C  C   . ALA A 64  ? 0.4250 0.4983 0.4188 0.0123  0.0385  0.0895  40  ALA A C   
267  O  O   . ALA A 64  ? 0.4050 0.4741 0.3908 0.0141  0.0354  0.0830  40  ALA A O   
268  C  CB  . ALA A 64  ? 0.3903 0.4485 0.4010 0.0016  0.0347  0.0854  40  ALA A CB  
269  N  N   . ALA A 65  ? 0.4005 0.4878 0.3919 0.0161  0.0429  0.0930  41  ALA A N   
270  C  CA  . ALA A 65  ? 0.4138 0.5116 0.3920 0.0228  0.0439  0.0887  41  ALA A CA  
271  C  C   . ALA A 65  ? 0.4351 0.5365 0.4073 0.0261  0.0442  0.0947  41  ALA A C   
272  O  O   . ALA A 65  ? 0.4381 0.5410 0.3999 0.0295  0.0416  0.0882  41  ALA A O   
273  C  CB  . ALA A 65  ? 0.4226 0.5350 0.3996 0.0265  0.0491  0.0915  41  ALA A CB  
274  N  N   . GLU A 66  ? 0.4263 0.5295 0.4059 0.0252  0.0473  0.1074  42  GLU A N   
275  C  CA  . GLU A 66  ? 0.4372 0.5440 0.4127 0.0285  0.0478  0.1148  42  GLU A CA  
276  C  C   . GLU A 66  ? 0.4673 0.5605 0.4430 0.0265  0.0428  0.1102  42  GLU A C   
277  O  O   . GLU A 66  ? 0.4847 0.5813 0.4541 0.0303  0.0418  0.1125  42  GLU A O   
278  C  CB  . GLU A 66  ? 0.4806 0.5916 0.4661 0.0277  0.0526  0.1304  42  GLU A CB  
279  C  CG  . GLU A 66  ? 0.5275 0.6553 0.5111 0.0312  0.0585  0.1366  42  GLU A CG  
280  C  CD  . GLU A 66  ? 0.7068 0.8382 0.7029 0.0292  0.0636  0.1522  42  GLU A CD  
281  O  OE1 . GLU A 66  ? 0.7623 0.8810 0.7705 0.0239  0.0622  0.1569  42  GLU A OE1 
282  O  OE2 . GLU A 66  ? 0.6302 0.7773 0.6244 0.0330  0.0692  0.1598  42  GLU A OE2 
283  N  N   . ALA A 67  ? 0.4719 0.5506 0.4544 0.0209  0.0396  0.1037  43  ALA A N   
284  C  CA  . ALA A 67  ? 0.4603 0.5266 0.4418 0.0195  0.0351  0.0977  43  ALA A CA  
285  C  C   . ALA A 67  ? 0.4239 0.4913 0.3949 0.0217  0.0315  0.0853  43  ALA A C   
286  O  O   . ALA A 67  ? 0.3985 0.4592 0.3670 0.0218  0.0281  0.0809  43  ALA A O   
287  C  CB  . ALA A 67  ? 0.4017 0.4526 0.3939 0.0128  0.0332  0.0956  43  ALA A CB  
288  N  N   . GLY A 68  ? 0.4113 0.4866 0.3769 0.0234  0.0322  0.0796  44  GLY A N   
289  C  CA  . GLY A 68  ? 0.4065 0.4838 0.3624 0.0258  0.0292  0.0683  44  GLY A CA  
290  C  C   . GLY A 68  ? 0.4243 0.4978 0.3808 0.0237  0.0280  0.0587  44  GLY A C   
291  O  O   . GLY A 68  ? 0.4131 0.4853 0.3637 0.0247  0.0251  0.0488  44  GLY A O   
292  N  N   . ALA A 69  ? 0.3994 0.4713 0.3640 0.0206  0.0301  0.0616  45  ALA A N   
293  C  CA  . ALA A 69  ? 0.3957 0.4655 0.3615 0.0192  0.0293  0.0538  45  ALA A CA  
294  C  C   . ALA A 69  ? 0.4115 0.4942 0.3707 0.0244  0.0324  0.0515  45  ALA A C   
295  O  O   . ALA A 69  ? 0.3965 0.4892 0.3571 0.0264  0.0369  0.0591  45  ALA A O   
296  C  CB  . ALA A 69  ? 0.3461 0.4106 0.3233 0.0141  0.0300  0.0580  45  ALA A CB  
297  N  N   . ALA A 70  ? 0.3779 0.4604 0.3301 0.0265  0.0302  0.0409  46  ALA A N   
298  C  CA  . ALA A 70  ? 0.3964 0.4896 0.3420 0.0315  0.0330  0.0366  46  ALA A CA  
299  C  C   . ALA A 70  ? 0.3795 0.4734 0.3317 0.0309  0.0355  0.0355  46  ALA A C   
300  O  O   . ALA A 70  ? 0.3936 0.4980 0.3425 0.0353  0.0395  0.0351  46  ALA A O   
301  C  CB  . ALA A 70  ? 0.4046 0.4964 0.3416 0.0337  0.0294  0.0251  46  ALA A CB  
302  N  N   . VAL A 71  ? 0.3632 0.4469 0.3243 0.0259  0.0333  0.0350  47  VAL A N   
303  C  CA  . VAL A 71  ? 0.3726 0.4568 0.3412 0.0249  0.0349  0.0344  47  VAL A CA  
304  C  C   . VAL A 71  ? 0.3798 0.4599 0.3596 0.0194  0.0347  0.0427  47  VAL A C   
305  O  O   . VAL A 71  ? 0.3850 0.4554 0.3670 0.0151  0.0312  0.0436  47  VAL A O   
306  C  CB  . VAL A 71  ? 0.3891 0.4650 0.3576 0.0242  0.0316  0.0241  47  VAL A CB  
307  C  CG1 . VAL A 71  ? 0.3757 0.4530 0.3527 0.0237  0.0333  0.0245  47  VAL A CG1 
308  C  CG2 . VAL A 71  ? 0.3614 0.4402 0.3198 0.0289  0.0313  0.0150  47  VAL A CG2 
309  N  N   . ILE A 72  ? 0.3821 0.4698 0.3693 0.0196  0.0384  0.0485  48  ILE A N   
310  C  CA  . ILE A 72  ? 0.3731 0.4579 0.3724 0.0139  0.0379  0.0558  48  ILE A CA  
311  C  C   . ILE A 72  ? 0.3843 0.4690 0.3908 0.0127  0.0372  0.0526  48  ILE A C   
312  O  O   . ILE A 72  ? 0.3936 0.4876 0.4006 0.0170  0.0410  0.0521  48  ILE A O   
313  C  CB  . ILE A 72  ? 0.3831 0.4781 0.3877 0.0144  0.0428  0.0673  48  ILE A CB  
314  C  CG1 . ILE A 72  ? 0.3792 0.4767 0.3759 0.0170  0.0441  0.0712  48  ILE A CG1 
315  C  CG2 . ILE A 72  ? 0.3662 0.4565 0.3843 0.0074  0.0413  0.0741  48  ILE A CG2 
316  C  CD1 . ILE A 72  ? 0.3660 0.4508 0.3622 0.0131  0.0396  0.0707  48  ILE A CD1 
317  N  N   . HIS A 73  ? 0.3631 0.4376 0.3749 0.0072  0.0325  0.0505  49  HIS A N   
318  C  CA  . HIS A 73  ? 0.3580 0.4323 0.3775 0.0055  0.0310  0.0487  49  HIS A CA  
319  C  C   . HIS A 73  ? 0.3581 0.4365 0.3902 0.0008  0.0316  0.0574  49  HIS A C   
320  O  O   . HIS A 73  ? 0.3339 0.4061 0.3697 -0.0045 0.0291  0.0609  49  HIS A O   
321  C  CB  . HIS A 73  ? 0.3571 0.4192 0.3744 0.0024  0.0254  0.0415  49  HIS A CB  
322  C  CG  . HIS A 73  ? 0.3899 0.4518 0.4147 0.0005  0.0234  0.0402  49  HIS A CG  
323  N  ND1 . HIS A 73  ? 0.4075 0.4745 0.4331 0.0051  0.0254  0.0369  49  HIS A ND1 
324  C  CD2 . HIS A 73  ? 0.3539 0.4114 0.3860 -0.0052 0.0193  0.0418  49  HIS A CD2 
325  C  CE1 . HIS A 73  ? 0.4116 0.4777 0.4450 0.0025  0.0228  0.0374  49  HIS A CE1 
326  N  NE2 . HIS A 73  ? 0.3600 0.4209 0.3970 -0.0039 0.0188  0.0402  49  HIS A NE2 
327  N  N   . LEU A 74  ? 0.3461 0.4350 0.3856 0.0027  0.0348  0.0608  50  LEU A N   
328  C  CA  . LEU A 74  ? 0.3648 0.4613 0.4169 -0.0007 0.0368  0.0704  50  LEU A CA  
329  C  C   . LEU A 74  ? 0.3807 0.4790 0.4442 -0.0040 0.0341  0.0709  50  LEU A C   
330  O  O   . LEU A 74  ? 0.3365 0.4384 0.4000 -0.0002 0.0349  0.0670  50  LEU A O   
331  C  CB  . LEU A 74  ? 0.3704 0.4812 0.4227 0.0049  0.0441  0.0764  50  LEU A CB  
332  C  CG  . LEU A 74  ? 0.3893 0.5012 0.4327 0.0074  0.0470  0.0794  50  LEU A CG  
333  C  CD1 . LEU A 74  ? 0.4290 0.5562 0.4702 0.0141  0.0544  0.0839  50  LEU A CD1 
334  C  CD2 . LEU A 74  ? 0.3714 0.4785 0.4218 0.0011  0.0454  0.0871  50  LEU A CD2 
335  N  N   . HIS A 75  ? 0.3440 0.4397 0.4173 -0.0113 0.0308  0.0757  51  HIS A N   
336  C  CA  . HIS A 75  ? 0.3545 0.4563 0.4418 -0.0152 0.0290  0.0796  51  HIS A CA  
337  C  C   . HIS A 75  ? 0.3550 0.4655 0.4541 -0.0183 0.0322  0.0901  51  HIS A C   
338  O  O   . HIS A 75  ? 0.3567 0.4657 0.4532 -0.0185 0.0348  0.0942  51  HIS A O   
339  C  CB  . HIS A 75  ? 0.3509 0.4424 0.4406 -0.0221 0.0212  0.0756  51  HIS A CB  
340  C  CG  . HIS A 75  ? 0.3709 0.4549 0.4513 -0.0197 0.0179  0.0667  51  HIS A CG  
341  N  ND1 . HIS A 75  ? 0.3892 0.4728 0.4743 -0.0221 0.0132  0.0645  51  HIS A ND1 
342  C  CD2 . HIS A 75  ? 0.3469 0.4239 0.4143 -0.0153 0.0184  0.0599  51  HIS A CD2 
343  C  CE1 . HIS A 75  ? 0.3872 0.4636 0.4627 -0.0191 0.0115  0.0572  51  HIS A CE1 
344  N  NE2 . HIS A 75  ? 0.3725 0.4446 0.4375 -0.0152 0.0145  0.0540  51  HIS A NE2 
345  N  N   . ALA A 76  ? 0.3707 0.4907 0.4839 -0.0208 0.0320  0.0951  52  ALA A N   
346  C  CA  . ALA A 76  ? 0.3738 0.5023 0.5013 -0.0251 0.0344  0.1055  52  ALA A CA  
347  C  C   . ALA A 76  ? 0.3679 0.4939 0.5081 -0.0340 0.0275  0.1065  52  ALA A C   
348  O  O   . ALA A 76  ? 0.3716 0.4931 0.5102 -0.0354 0.0219  0.1001  52  ALA A O   
349  C  CB  . ALA A 76  ? 0.3695 0.5153 0.5038 -0.0194 0.0417  0.1121  52  ALA A CB  
350  N  N   . ARG A 77  ? 0.3836 0.5127 0.5367 -0.0401 0.0278  0.1146  53  ARG A N   
351  C  CA  . ARG A 77  ? 0.3765 0.5035 0.5426 -0.0493 0.0210  0.1154  53  ARG A CA  
352  C  C   . ARG A 77  ? 0.4185 0.5593 0.6039 -0.0529 0.0241  0.1267  53  ARG A C   
353  O  O   . ARG A 77  ? 0.4190 0.5675 0.6069 -0.0496 0.0314  0.1345  53  ARG A O   
354  C  CB  . ARG A 77  ? 0.3779 0.4882 0.5398 -0.0558 0.0159  0.1113  53  ARG A CB  
355  C  CG  . ARG A 77  ? 0.3961 0.4930 0.5409 -0.0534 0.0120  0.1003  53  ARG A CG  
356  C  CD  . ARG A 77  ? 0.3840 0.4650 0.5245 -0.0586 0.0084  0.0968  53  ARG A CD  
357  N  NE  . ARG A 77  ? 0.3864 0.4554 0.5117 -0.0567 0.0047  0.0866  53  ARG A NE  
358  C  CZ  . ARG A 77  ? 0.4024 0.4659 0.5258 -0.0604 -0.0021 0.0798  53  ARG A CZ  
359  N  NH1 . ARG A 77  ? 0.3934 0.4622 0.5288 -0.0666 -0.0067 0.0814  53  ARG A NH1 
360  N  NH2 . ARG A 77  ? 0.3506 0.4039 0.4598 -0.0580 -0.0043 0.0714  53  ARG A NH2 
361  N  N   . HIS A 78  ? 0.3804 0.5252 0.5795 -0.0598 0.0183  0.1276  54  HIS A N   
362  C  CA  . HIS A 78  ? 0.4413 0.5976 0.6609 -0.0654 0.0197  0.1381  54  HIS A CA  
363  C  C   . HIS A 78  ? 0.4813 0.6278 0.7056 -0.0723 0.0191  0.1415  54  HIS A C   
364  O  O   . HIS A 78  ? 0.4852 0.6167 0.7053 -0.0781 0.0124  0.1347  54  HIS A O   
365  C  CB  . HIS A 78  ? 0.3989 0.5617 0.6321 -0.0717 0.0125  0.1374  54  HIS A CB  
366  C  CG  . HIS A 78  ? 0.3883 0.5625 0.6208 -0.0651 0.0135  0.1361  54  HIS A CG  
367  N  ND1 . HIS A 78  ? 0.3906 0.5586 0.6132 -0.0636 0.0076  0.1270  54  HIS A ND1 
368  C  CD2 . HIS A 78  ? 0.3906 0.5819 0.6318 -0.0593 0.0199  0.1431  54  HIS A CD2 
369  C  CE1 . HIS A 78  ? 0.3865 0.5668 0.6122 -0.0572 0.0103  0.1286  54  HIS A CE1 
370  N  NE2 . HIS A 78  ? 0.3850 0.5795 0.6218 -0.0544 0.0178  0.1379  54  HIS A NE2 
371  N  N   . GLU A 79  ? 0.5353 0.6902 0.7684 -0.0714 0.0263  0.1524  55  GLU A N   
372  C  CA  . GLU A 79  ? 0.5566 0.7022 0.7954 -0.0774 0.0266  0.1571  55  GLU A CA  
373  C  C   . GLU A 79  ? 0.5383 0.6809 0.7951 -0.0892 0.0193  0.1580  55  GLU A C   
374  O  O   . GLU A 79  ? 0.5430 0.6725 0.8029 -0.0954 0.0170  0.1579  55  GLU A O   
375  C  CB  . GLU A 79  ? 0.5884 0.7454 0.8331 -0.0733 0.0365  0.1698  55  GLU A CB  
376  C  CG  . GLU A 79  ? 0.6166 0.7789 0.8437 -0.0615 0.0437  0.1688  55  GLU A CG  
377  C  CD  . GLU A 79  ? 0.6592 0.8263 0.8857 -0.0577 0.0522  0.1793  55  GLU A CD  
378  O  OE1 . GLU A 79  ? 0.6666 0.8355 0.9091 -0.0639 0.0537  0.1894  55  GLU A OE1 
379  O  OE2 . GLU A 79  ? 0.6200 0.7892 0.8301 -0.0486 0.0573  0.1776  55  GLU A OE2 
380  N  N   . GLY A 80  ? 0.5049 0.6590 0.7739 -0.0925 0.0156  0.1586  56  GLY A N   
381  C  CA  . GLY A 80  ? 0.5096 0.6624 0.7959 -0.1040 0.0079  0.1588  56  GLY A CA  
382  C  C   . GLY A 80  ? 0.5632 0.6976 0.8401 -0.1096 -0.0015 0.1464  56  GLY A C   
383  O  O   . GLY A 80  ? 0.6116 0.7339 0.8942 -0.1172 -0.0045 0.1456  56  GLY A O   
384  N  N   . ASP A 81  ? 0.5296 0.6617 0.7925 -0.1059 -0.0059 0.1367  57  ASP A N   
385  C  CA  . ASP A 81  ? 0.5129 0.6294 0.7659 -0.1106 -0.0147 0.1247  57  ASP A CA  
386  C  C   . ASP A 81  ? 0.4435 0.5482 0.6728 -0.1028 -0.0134 0.1161  57  ASP A C   
387  O  O   . ASP A 81  ? 0.4416 0.5344 0.6606 -0.1053 -0.0200 0.1059  57  ASP A O   
388  C  CB  . ASP A 81  ? 0.5162 0.6409 0.7759 -0.1153 -0.0231 0.1209  57  ASP A CB  
389  C  CG  . ASP A 81  ? 0.4966 0.6337 0.7501 -0.1067 -0.0210 0.1210  57  ASP A CG  
390  O  OD1 . ASP A 81  ? 0.4533 0.5916 0.6964 -0.0973 -0.0133 0.1227  57  ASP A OD1 
391  O  OD2 . ASP A 81  ? 0.4987 0.6445 0.7582 -0.1093 -0.0272 0.1193  57  ASP A OD2 
392  N  N   . GLY A 82  ? 0.4372 0.5453 0.6576 -0.0935 -0.0052 0.1196  58  GLY A N   
393  C  CA  . GLY A 82  ? 0.4515 0.5487 0.6507 -0.0865 -0.0037 0.1120  58  GLY A CA  
394  C  C   . GLY A 82  ? 0.4404 0.5397 0.6285 -0.0817 -0.0066 0.1046  58  GLY A C   
395  O  O   . GLY A 82  ? 0.4061 0.4959 0.5773 -0.0766 -0.0062 0.0977  58  GLY A O   
396  N  N   . SER A 83  ? 0.4256 0.5373 0.6233 -0.0831 -0.0096 0.1063  59  SER A N   
397  C  CA  . SER A 83  ? 0.3991 0.5130 0.5876 -0.0783 -0.0123 0.1003  59  SER A CA  
398  C  C   . SER A 83  ? 0.3664 0.4853 0.5458 -0.0676 -0.0045 0.1014  59  SER A C   
399  O  O   . SER A 83  ? 0.3838 0.5097 0.5672 -0.0640 0.0029  0.1084  59  SER A O   
400  C  CB  . SER A 83  ? 0.3713 0.4986 0.5741 -0.0821 -0.0172 0.1032  59  SER A CB  
401  O  OG  . SER A 83  ? 0.3782 0.5217 0.5961 -0.0804 -0.0115 0.1133  59  SER A OG  
402  N  N   . PRO A 84  ? 0.3770 0.4924 0.5440 -0.0624 -0.0059 0.0946  60  PRO A N   
403  C  CA  . PRO A 84  ? 0.3924 0.5116 0.5508 -0.0524 0.0011  0.0943  60  PRO A CA  
404  C  C   . PRO A 84  ? 0.4065 0.5432 0.5774 -0.0485 0.0066  0.1023  60  PRO A C   
405  O  O   . PRO A 84  ? 0.3980 0.5449 0.5819 -0.0513 0.0035  0.1058  60  PRO A O   
406  C  CB  . PRO A 84  ? 0.3832 0.4963 0.5306 -0.0495 -0.0030 0.0862  60  PRO A CB  
407  C  CG  . PRO A 84  ? 0.3901 0.4911 0.5332 -0.0568 -0.0105 0.0807  60  PRO A CG  
408  C  CD  . PRO A 84  ? 0.3635 0.4693 0.5219 -0.0652 -0.0136 0.0861  60  PRO A CD  
409  N  N   . ASP A 85  ? 0.3896 0.5305 0.5563 -0.0416 0.0148  0.1053  61  ASP A N   
410  C  CA  . ASP A 85  ? 0.3988 0.5564 0.5752 -0.0363 0.0216  0.1124  61  ASP A CA  
411  C  C   . ASP A 85  ? 0.3972 0.5545 0.5601 -0.0260 0.0274  0.1077  61  ASP A C   
412  O  O   . ASP A 85  ? 0.3900 0.5428 0.5419 -0.0224 0.0317  0.1064  61  ASP A O   
413  C  CB  . ASP A 85  ? 0.3610 0.5261 0.5473 -0.0387 0.0268  0.1221  61  ASP A CB  
414  C  CG  . ASP A 85  ? 0.4284 0.6123 0.6266 -0.0338 0.0338  0.1304  61  ASP A CG  
415  O  OD1 . ASP A 85  ? 0.4205 0.6110 0.6187 -0.0279 0.0351  0.1281  61  ASP A OD1 
416  O  OD2 . ASP A 85  ? 0.4042 0.5966 0.6124 -0.0357 0.0385  0.1396  61  ASP A OD2 
417  N  N   . GLN A 86  ? 0.3868 0.5492 0.5512 -0.0213 0.0272  0.1051  62  GLN A N   
418  C  CA  . GLN A 86  ? 0.4019 0.5632 0.5548 -0.0118 0.0320  0.0995  62  GLN A CA  
419  C  C   . GLN A 86  ? 0.4445 0.6220 0.6060 -0.0047 0.0399  0.1050  62  GLN A C   
420  O  O   . GLN A 86  ? 0.4768 0.6561 0.6345 0.0028  0.0429  0.1007  62  GLN A O   
421  C  CB  . GLN A 86  ? 0.4403 0.5932 0.5878 -0.0110 0.0264  0.0919  62  GLN A CB  
422  C  CG  . GLN A 86  ? 0.4238 0.5720 0.5591 -0.0022 0.0301  0.0845  62  GLN A CG  
423  C  CD  . GLN A 86  ? 0.4176 0.5564 0.5372 -0.0002 0.0326  0.0795  62  GLN A CD  
424  O  OE1 . GLN A 86  ? 0.3998 0.5347 0.5170 -0.0049 0.0317  0.0817  62  GLN A OE1 
425  N  NE2 . GLN A 86  ? 0.3946 0.5297 0.5042 0.0070  0.0356  0.0727  62  GLN A NE2 
426  N  N   . SER A 87  ? 0.4337 0.6231 0.6072 -0.0070 0.0436  0.1144  63  SER A N   
427  C  CA  . SER A 87  ? 0.4513 0.6571 0.6330 -0.0002 0.0519  0.1203  63  SER A CA  
428  C  C   . SER A 87  ? 0.4570 0.6638 0.6257 0.0071  0.0600  0.1189  63  SER A C   
429  O  O   . SER A 87  ? 0.4291 0.6270 0.5868 0.0051  0.0595  0.1171  63  SER A O   
430  C  CB  . SER A 87  ? 0.4086 0.6281 0.6099 -0.0059 0.0527  0.1318  63  SER A CB  
431  O  OG  . SER A 87  ? 0.4566 0.6736 0.6571 -0.0108 0.0539  0.1366  63  SER A OG  
432  N  N   . VAL A 88  ? 0.4572 0.6755 0.6271 0.0160  0.0677  0.1196  64  VAL A N   
433  C  CA  . VAL A 88  ? 0.4522 0.6738 0.6095 0.0236  0.0758  0.1181  64  VAL A CA  
434  C  C   . VAL A 88  ? 0.4656 0.6935 0.6259 0.0199  0.0792  0.1278  64  VAL A C   
435  O  O   . VAL A 88  ? 0.4459 0.6687 0.5926 0.0213  0.0811  0.1261  64  VAL A O   
436  C  CB  . VAL A 88  ? 0.4891 0.7238 0.6496 0.0336  0.0838  0.1179  64  VAL A CB  
437  C  CG1 . VAL A 88  ? 0.4683 0.7079 0.6151 0.0415  0.0922  0.1162  64  VAL A CG1 
438  C  CG2 . VAL A 88  ? 0.4929 0.7199 0.6508 0.0374  0.0805  0.1085  64  VAL A CG2 
439  N  N   . GLU A 89  ? 0.4317 0.6710 0.6106 0.0150  0.0799  0.1385  65  GLU A N   
440  C  CA  . GLU A 89  ? 0.4496 0.6959 0.6342 0.0114  0.0837  0.1491  65  GLU A CA  
441  C  C   . GLU A 89  ? 0.4202 0.6512 0.5976 0.0042  0.0779  0.1477  65  GLU A C   
442  O  O   . GLU A 89  ? 0.4203 0.6529 0.5937 0.0042  0.0820  0.1534  65  GLU A O   
443  C  CB  . GLU A 89  ? 0.4824 0.7425 0.6908 0.0061  0.0840  0.1603  65  GLU A CB  
444  C  CG  . GLU A 89  ? 0.5296 0.7948 0.7478 -0.0002 0.0863  0.1721  65  GLU A CG  
445  C  CD  . GLU A 89  ? 0.6252 0.9008 0.8358 0.0072  0.0969  0.1779  65  GLU A CD  
446  O  OE1 . GLU A 89  ? 0.6405 0.9284 0.8487 0.0165  0.1043  0.1775  65  GLU A OE1 
447  O  OE2 . GLU A 89  ? 0.6409 0.9124 0.8480 0.0040  0.0978  0.1830  65  GLU A OE2 
448  N  N   . ALA A 90  ? 0.4209 0.6373 0.5965 -0.0018 0.0687  0.1406  66  ALA A N   
449  C  CA  . ALA A 90  ? 0.4526 0.6545 0.6233 -0.0090 0.0631  0.1395  66  ALA A CA  
450  C  C   . ALA A 90  ? 0.3852 0.5793 0.5365 -0.0040 0.0657  0.1347  66  ALA A C   
451  O  O   . ALA A 90  ? 0.3861 0.5730 0.5346 -0.0080 0.0646  0.1376  66  ALA A O   
452  C  CB  . ALA A 90  ? 0.3959 0.5848 0.5670 -0.0153 0.0531  0.1318  66  ALA A CB  
453  N  N   . PHE A 91  ? 0.3795 0.5748 0.5178 0.0048  0.0690  0.1273  67  PHE A N   
454  C  CA  . PHE A 91  ? 0.3929 0.5823 0.5126 0.0098  0.0712  0.1222  67  PHE A CA  
455  C  C   . PHE A 91  ? 0.4221 0.6254 0.5389 0.0158  0.0804  0.1297  67  PHE A C   
456  O  O   . PHE A 91  ? 0.4400 0.6403 0.5423 0.0193  0.0821  0.1275  67  PHE A O   
457  C  CB  . PHE A 91  ? 0.3783 0.5615 0.4852 0.0160  0.0699  0.1097  67  PHE A CB  
458  C  CG  . PHE A 91  ? 0.3587 0.5260 0.4630 0.0109  0.0610  0.1016  67  PHE A CG  
459  C  CD1 . PHE A 91  ? 0.3920 0.5590 0.5068 0.0081  0.0569  0.1003  67  PHE A CD1 
460  C  CD2 . PHE A 91  ? 0.3608 0.5145 0.4523 0.0093  0.0571  0.0956  67  PHE A CD2 
461  C  CE1 . PHE A 91  ? 0.4057 0.5591 0.5173 0.0037  0.0491  0.0934  67  PHE A CE1 
462  C  CE2 . PHE A 91  ? 0.3580 0.4981 0.4470 0.0050  0.0496  0.0885  67  PHE A CE2 
463  C  CZ  . PHE A 91  ? 0.3812 0.5211 0.4798 0.0022  0.0457  0.0874  67  PHE A CZ  
464  N  N   . ASN A 92  ? 0.4103 0.6295 0.5405 0.0171  0.0862  0.1389  68  ASN A N   
465  C  CA  . ASN A 92  ? 0.4220 0.6561 0.5490 0.0236  0.0957  0.1464  68  ASN A CA  
466  C  C   . ASN A 92  ? 0.4417 0.6738 0.5655 0.0204  0.0967  0.1542  68  ASN A C   
467  O  O   . ASN A 92  ? 0.4347 0.6708 0.5440 0.0269  0.1014  0.1539  68  ASN A O   
468  C  CB  . ASN A 92  ? 0.4444 0.6962 0.5889 0.0245  0.1016  0.1559  68  ASN A CB  
469  C  CG  . ASN A 92  ? 0.5073 0.7761 0.6488 0.0316  0.1121  0.1643  68  ASN A CG  
470  O  OD1 . ASN A 92  ? 0.5466 0.8244 0.6994 0.0282  0.1158  0.1773  68  ASN A OD1 
471  N  ND2 . ASN A 92  ? 0.4973 0.7706 0.6233 0.0415  0.1171  0.1568  68  ASN A ND2 
472  N  N   . PRO A 93  ? 0.4436 0.6701 0.5803 0.0112  0.0926  0.1614  69  PRO A N   
473  C  CA  . PRO A 93  ? 0.4273 0.6502 0.5614 0.0085  0.0936  0.1689  69  PRO A CA  
474  C  C   . PRO A 93  ? 0.4164 0.6221 0.5350 0.0078  0.0877  0.1600  69  PRO A C   
475  O  O   . PRO A 93  ? 0.4301 0.6305 0.5482 0.0048  0.0873  0.1659  69  PRO A O   
476  C  CB  . PRO A 93  ? 0.4249 0.6466 0.5806 -0.0017 0.0907  0.1784  69  PRO A CB  
477  C  CG  . PRO A 93  ? 0.4429 0.6589 0.6060 -0.0060 0.0839  0.1707  69  PRO A CG  
478  C  CD  . PRO A 93  ? 0.4195 0.6440 0.5750 0.0028  0.0874  0.1638  69  PRO A CD  
479  N  N   . ILE A 94  ? 0.4189 0.6161 0.5258 0.0106  0.0834  0.1466  70  ILE A N   
480  C  CA  . ILE A 94  ? 0.4290 0.6101 0.5224 0.0096  0.0775  0.1377  70  ILE A CA  
481  C  C   . ILE A 94  ? 0.4368 0.6205 0.5107 0.0186  0.0804  0.1304  70  ILE A C   
482  O  O   . ILE A 94  ? 0.4145 0.5953 0.4779 0.0203  0.0806  0.1312  70  ILE A O   
483  C  CB  . ILE A 94  ? 0.4041 0.5713 0.5002 0.0043  0.0691  0.1282  70  ILE A CB  
484  C  CG1 . ILE A 94  ? 0.4309 0.5923 0.5433 -0.0056 0.0647  0.1342  70  ILE A CG1 
485  C  CG2 . ILE A 94  ? 0.3684 0.5215 0.4486 0.0055  0.0643  0.1174  70  ILE A CG2 
486  C  CD1 . ILE A 94  ? 0.3936 0.5463 0.5111 -0.0107 0.0573  0.1265  70  ILE A CD1 
487  N  N   . LEU A 95  ? 0.4200 0.6092 0.4895 0.0244  0.0823  0.1230  71  LEU A N   
488  C  CA  . LEU A 95  ? 0.4080 0.5966 0.4592 0.0319  0.0833  0.1130  71  LEU A CA  
489  C  C   . LEU A 95  ? 0.4518 0.6530 0.4934 0.0380  0.0901  0.1190  71  LEU A C   
490  O  O   . LEU A 95  ? 0.4321 0.6293 0.4600 0.0402  0.0887  0.1156  71  LEU A O   
491  C  CB  . LEU A 95  ? 0.3961 0.5882 0.4470 0.0368  0.0847  0.1044  71  LEU A CB  
492  C  CG  . LEU A 95  ? 0.4098 0.5900 0.4682 0.0318  0.0779  0.0980  71  LEU A CG  
493  C  CD1 . LEU A 95  ? 0.3910 0.5771 0.4524 0.0372  0.0806  0.0926  71  LEU A CD1 
494  C  CD2 . LEU A 95  ? 0.4099 0.5737 0.4574 0.0296  0.0709  0.0883  71  LEU A CD2 
495  N  N   . GLY A 96  ? 0.4308 0.6482 0.4797 0.0411  0.0977  0.1283  72  GLY A N   
496  C  CA  . GLY A 96  ? 0.3818 0.6130 0.4208 0.0476  0.1048  0.1345  72  GLY A CA  
497  C  C   . GLY A 96  ? 0.3904 0.6186 0.4279 0.0442  0.1037  0.1436  72  GLY A C   
498  O  O   . GLY A 96  ? 0.4417 0.6754 0.4649 0.0494  0.1061  0.1442  72  GLY A O   
499  N  N   . VAL A 97  ? 0.3937 0.6133 0.4459 0.0355  0.1000  0.1506  73  VAL A N   
500  C  CA  . VAL A 97  ? 0.4228 0.6379 0.4753 0.0322  0.0990  0.1594  73  VAL A CA  
501  C  C   . VAL A 97  ? 0.3938 0.5964 0.4310 0.0331  0.0931  0.1498  73  VAL A C   
502  O  O   . VAL A 97  ? 0.4145 0.6201 0.4423 0.0362  0.0946  0.1543  73  VAL A O   
503  C  CB  . VAL A 97  ? 0.4116 0.6187 0.4842 0.0223  0.0959  0.1674  73  VAL A CB  
504  C  CG1 . VAL A 97  ? 0.3994 0.5979 0.4724 0.0187  0.0939  0.1745  73  VAL A CG1 
505  C  CG2 . VAL A 97  ? 0.4365 0.6584 0.5252 0.0214  0.1024  0.1792  73  VAL A CG2 
506  N  N   . ILE A 98  ? 0.3875 0.5765 0.4224 0.0306  0.0864  0.1371  74  ILE A N   
507  C  CA  . ILE A 98  ? 0.4266 0.6039 0.4482 0.0312  0.0808  0.1279  74  ILE A CA  
508  C  C   . ILE A 98  ? 0.4148 0.6017 0.4184 0.0399  0.0836  0.1222  74  ILE A C   
509  O  O   . ILE A 98  ? 0.4758 0.6617 0.4686 0.0421  0.0823  0.1223  74  ILE A O   
510  C  CB  . ILE A 98  ? 0.3922 0.5545 0.4158 0.0269  0.0736  0.1159  74  ILE A CB  
511  C  CG1 . ILE A 98  ? 0.3723 0.5247 0.4119 0.0179  0.0699  0.1209  74  ILE A CG1 
512  C  CG2 . ILE A 98  ? 0.3790 0.5311 0.3886 0.0283  0.0685  0.1060  74  ILE A CG2 
513  C  CD1 . ILE A 98  ? 0.3417 0.4827 0.3848 0.0138  0.0638  0.1108  74  ILE A CD1 
514  N  N   . LYS A 99  ? 0.4245 0.6209 0.4249 0.0452  0.0876  0.1171  75  LYS A N   
515  C  CA  . LYS A 99  ? 0.4583 0.6634 0.4412 0.0534  0.0901  0.1098  75  LYS A CA  
516  C  C   . LYS A 99  ? 0.4654 0.6840 0.4408 0.0578  0.0951  0.1203  75  LYS A C   
517  O  O   . LYS A 99  ? 0.5184 0.7390 0.4785 0.0619  0.0937  0.1157  75  LYS A O   
518  C  CB  . LYS A 99  ? 0.4874 0.7010 0.4707 0.0584  0.0946  0.1039  75  LYS A CB  
519  C  CG  . LYS A 99  ? 0.4997 0.7182 0.4653 0.0663  0.0956  0.0919  75  LYS A CG  
520  C  CD  . LYS A 99  ? 0.5361 0.7623 0.5037 0.0714  0.1008  0.0866  75  LYS A CD  
521  C  CE  . LYS A 99  ? 0.6187 0.8542 0.5685 0.0803  0.1042  0.0775  75  LYS A CE  
522  N  NZ  . LYS A 99  ? 0.6272 0.8713 0.5791 0.0863  0.1104  0.0729  75  LYS A NZ  
523  N  N   . GLN A 100 ? 0.4570 0.6856 0.4433 0.0568  0.1010  0.1348  76  GLN A N   
524  C  CA  . GLN A 100 ? 0.4601 0.7025 0.4402 0.0610  0.1063  0.1466  76  GLN A CA  
525  C  C   . GLN A 100 ? 0.4660 0.6996 0.4422 0.0583  0.1015  0.1502  76  GLN A C   
526  O  O   . GLN A 100 ? 0.4794 0.7226 0.4435 0.0634  0.1036  0.1545  76  GLN A O   
527  C  CB  . GLN A 100 ? 0.4713 0.7245 0.4671 0.0592  0.1133  0.1627  76  GLN A CB  
528  C  CG  . GLN A 100 ? 0.4555 0.7260 0.4504 0.0656  0.1213  0.1635  76  GLN A CG  
529  C  CD  . GLN A 100 ? 0.4649 0.7510 0.4401 0.0751  0.1264  0.1624  76  GLN A CD  
530  O  OE1 . GLN A 100 ? 0.4766 0.7704 0.4464 0.0770  0.1288  0.1730  76  GLN A OE1 
531  N  NE2 . GLN A 100 ? 0.4759 0.7667 0.4402 0.0814  0.1279  0.1496  76  GLN A NE2 
532  N  N   . ALA A 101 ? 0.4462 0.6624 0.4324 0.0506  0.0951  0.1486  77  ALA A N   
533  C  CA  . ALA A 101 ? 0.4660 0.6729 0.4514 0.0478  0.0910  0.1530  77  ALA A CA  
534  C  C   . ALA A 101 ? 0.4791 0.6754 0.4520 0.0486  0.0839  0.1393  77  ALA A C   
535  O  O   . ALA A 101 ? 0.4926 0.6836 0.4623 0.0479  0.0809  0.1424  77  ALA A O   
536  C  CB  . ALA A 101 ? 0.4657 0.6597 0.4700 0.0389  0.0886  0.1598  77  ALA A CB  
537  N  N   . SER A 102 ? 0.4926 0.6857 0.4592 0.0500  0.0814  0.1250  78  SER A N   
538  C  CA  . SER A 102 ? 0.4973 0.6788 0.4553 0.0494  0.0744  0.1121  78  SER A CA  
539  C  C   . SER A 102 ? 0.4913 0.6754 0.4401 0.0536  0.0741  0.0980  78  SER A C   
540  O  O   . SER A 102 ? 0.4661 0.6545 0.4201 0.0544  0.0776  0.0966  78  SER A O   
541  C  CB  . SER A 102 ? 0.4594 0.6224 0.4289 0.0415  0.0687  0.1099  78  SER A CB  
542  O  OG  . SER A 102 ? 0.4582 0.6106 0.4205 0.0410  0.0626  0.0964  78  SER A OG  
543  N  N   . ASP A 103 ? 0.4703 0.6516 0.4063 0.0560  0.0697  0.0876  79  ASP A N   
544  C  CA  . ASP A 103 ? 0.4931 0.6742 0.4208 0.0594  0.0685  0.0730  79  ASP A CA  
545  C  C   . ASP A 103 ? 0.4388 0.6027 0.3717 0.0543  0.0622  0.0628  79  ASP A C   
546  O  O   . ASP A 103 ? 0.4662 0.6273 0.3925 0.0564  0.0599  0.0501  79  ASP A O   
547  C  CB  . ASP A 103 ? 0.5501 0.7399 0.4604 0.0653  0.0675  0.0669  79  ASP A CB  
548  C  CG  . ASP A 103 ? 0.6349 0.8163 0.5415 0.0627  0.0608  0.0650  79  ASP A CG  
549  O  OD1 . ASP A 103 ? 0.6648 0.8376 0.5809 0.0577  0.0590  0.0731  79  ASP A OD1 
550  O  OD2 . ASP A 103 ? 0.7273 0.9108 0.6218 0.0657  0.0575  0.0552  79  ASP A OD2 
551  N  N   . ALA A 104 ? 0.4300 0.5826 0.3748 0.0477  0.0595  0.0680  80  ALA A N   
552  C  CA  . ALA A 104 ? 0.4402 0.5776 0.3904 0.0429  0.0541  0.0594  80  ALA A CA  
553  C  C   . ALA A 104 ? 0.4161 0.5540 0.3691 0.0443  0.0557  0.0520  80  ALA A C   
554  O  O   . ALA A 104 ? 0.4016 0.5499 0.3579 0.0471  0.0612  0.0564  80  ALA A O   
555  C  CB  . ALA A 104 ? 0.4248 0.5520 0.3878 0.0359  0.0521  0.0670  80  ALA A CB  
556  N  N   . VAL A 105 ? 0.4055 0.5326 0.3578 0.0427  0.0511  0.0412  81  VAL A N   
557  C  CA  . VAL A 105 ? 0.4130 0.5382 0.3700 0.0435  0.0519  0.0347  81  VAL A CA  
558  C  C   . VAL A 105 ? 0.3909 0.5110 0.3623 0.0380  0.0514  0.0412  81  VAL A C   
559  O  O   . VAL A 105 ? 0.3765 0.4864 0.3526 0.0322  0.0471  0.0432  81  VAL A O   
560  C  CB  . VAL A 105 ? 0.4009 0.5161 0.3530 0.0434  0.0472  0.0218  81  VAL A CB  
561  C  CG1 . VAL A 105 ? 0.4098 0.5228 0.3677 0.0447  0.0483  0.0158  81  VAL A CG1 
562  C  CG2 . VAL A 105 ? 0.4124 0.5329 0.3506 0.0482  0.0468  0.0150  81  VAL A CG2 
563  N  N   . LEU A 106 ? 0.3788 0.5066 0.3574 0.0397  0.0558  0.0443  82  LEU A N   
564  C  CA  . LEU A 106 ? 0.3848 0.5102 0.3779 0.0346  0.0553  0.0508  82  LEU A CA  
565  C  C   . LEU A 106 ? 0.3987 0.5168 0.3963 0.0339  0.0526  0.0430  82  LEU A C   
566  O  O   . LEU A 106 ? 0.3878 0.5103 0.3833 0.0392  0.0554  0.0371  82  LEU A O   
567  C  CB  . LEU A 106 ? 0.3968 0.5363 0.3969 0.0366  0.0619  0.0608  82  LEU A CB  
568  C  CG  . LEU A 106 ? 0.3958 0.5439 0.3918 0.0380  0.0654  0.0699  82  LEU A CG  
569  C  CD1 . LEU A 106 ? 0.3920 0.5530 0.3983 0.0384  0.0716  0.0815  82  LEU A CD1 
570  C  CD2 . LEU A 106 ? 0.3900 0.5277 0.3866 0.0322  0.0606  0.0736  82  LEU A CD2 
571  N  N   . ASN A 107 ? 0.3674 0.4747 0.3715 0.0276  0.0473  0.0430  83  ASN A N   
572  C  CA  . ASN A 107 ? 0.3682 0.4673 0.3762 0.0262  0.0437  0.0365  83  ASN A CA  
573  C  C   . ASN A 107 ? 0.3882 0.4894 0.4101 0.0220  0.0432  0.0433  83  ASN A C   
574  O  O   . ASN A 107 ? 0.3874 0.4837 0.4146 0.0158  0.0398  0.0480  83  ASN A O   
575  C  CB  . ASN A 107 ? 0.3651 0.4508 0.3677 0.0225  0.0377  0.0308  83  ASN A CB  
576  C  CG  . ASN A 107 ? 0.4145 0.4915 0.4216 0.0202  0.0338  0.0257  83  ASN A CG  
577  O  OD1 . ASN A 107 ? 0.4131 0.4936 0.4287 0.0206  0.0348  0.0273  83  ASN A OD1 
578  N  ND2 . ASN A 107 ? 0.4317 0.4980 0.4336 0.0179  0.0293  0.0202  83  ASN A ND2 
579  N  N   . ILE A 108 ? 0.3519 0.4606 0.3802 0.0255  0.0465  0.0435  84  ILE A N   
580  C  CA  . ILE A 108 ? 0.3866 0.5003 0.4291 0.0222  0.0465  0.0506  84  ILE A CA  
581  C  C   . ILE A 108 ? 0.3842 0.4892 0.4316 0.0191  0.0410  0.0466  84  ILE A C   
582  O  O   . ILE A 108 ? 0.4036 0.5043 0.4472 0.0227  0.0406  0.0391  84  ILE A O   
583  C  CB  . ILE A 108 ? 0.3776 0.5056 0.4258 0.0281  0.0533  0.0541  84  ILE A CB  
584  C  CG1 . ILE A 108 ? 0.3690 0.5070 0.4127 0.0308  0.0590  0.0599  84  ILE A CG1 
585  C  CG2 . ILE A 108 ? 0.3715 0.5051 0.4358 0.0246  0.0526  0.0611  84  ILE A CG2 
586  C  CD1 . ILE A 108 ? 0.3578 0.5110 0.4054 0.0374  0.0667  0.0632  84  ILE A CD1 
587  N  N   . THR A 109 ? 0.3760 0.4786 0.4319 0.0122  0.0368  0.0515  85  THR A N   
588  C  CA  . THR A 109 ? 0.3483 0.4439 0.4085 0.0090  0.0313  0.0487  85  THR A CA  
589  C  C   . THR A 109 ? 0.3944 0.4979 0.4638 0.0128  0.0333  0.0497  85  THR A C   
590  O  O   . THR A 109 ? 0.3621 0.4775 0.4404 0.0144  0.0374  0.0560  85  THR A O   
591  C  CB  . THR A 109 ? 0.3836 0.4761 0.4504 0.0007  0.0262  0.0535  85  THR A CB  
592  O  OG1 . THR A 109 ? 0.3951 0.4808 0.4635 -0.0022 0.0205  0.0502  85  THR A OG1 
593  C  CG2 . THR A 109 ? 0.3582 0.4627 0.4385 -0.0013 0.0284  0.0627  85  THR A CG2 
594  N  N   . THR A 110 ? 0.3581 0.4551 0.4260 0.0145  0.0308  0.0439  86  THR A N   
595  C  CA  . THR A 110 ? 0.3992 0.5013 0.4778 0.0164  0.0307  0.0458  86  THR A CA  
596  C  C   . THR A 110 ? 0.3977 0.4948 0.4811 0.0101  0.0236  0.0473  86  THR A C   
597  O  O   . THR A 110 ? 0.3938 0.4941 0.4854 0.0114  0.0222  0.0489  86  THR A O   
598  C  CB  . THR A 110 ? 0.3692 0.4684 0.4443 0.0236  0.0335  0.0388  86  THR A CB  
599  O  OG1 . THR A 110 ? 0.3651 0.4516 0.4339 0.0218  0.0288  0.0329  86  THR A OG1 
600  C  CG2 . THR A 110 ? 0.3915 0.4936 0.4580 0.0296  0.0397  0.0347  86  THR A CG2 
601  N  N   . GLY A 111 ? 0.3898 0.4793 0.4680 0.0038  0.0190  0.0469  87  GLY A N   
602  C  CA  . GLY A 111 ? 0.3907 0.4759 0.4720 -0.0023 0.0122  0.0479  87  GLY A CA  
603  C  C   . GLY A 111 ? 0.4364 0.5294 0.5284 -0.0081 0.0100  0.0551  87  GLY A C   
604  O  O   . GLY A 111 ? 0.4493 0.5453 0.5488 -0.0113 0.0054  0.0575  87  GLY A O   
605  N  N   . GLY A 112 ? 0.4078 0.5047 0.5012 -0.0095 0.0131  0.0588  88  GLY A N   
606  C  CA  . GLY A 112 ? 0.3923 0.4956 0.4967 -0.0158 0.0109  0.0655  88  GLY A CA  
607  C  C   . GLY A 112 ? 0.4356 0.5310 0.5392 -0.0233 0.0030  0.0636  88  GLY A C   
608  O  O   . GLY A 112 ? 0.4500 0.5335 0.5425 -0.0245 0.0004  0.0577  88  GLY A O   
609  N  N   . ALA A 113 ? 0.4421 0.5449 0.5579 -0.0285 -0.0008 0.0685  89  ALA A N   
610  C  CA  . ALA A 113 ? 0.4492 0.5461 0.5641 -0.0350 -0.0087 0.0660  89  ALA A CA  
611  C  C   . ALA A 113 ? 0.4660 0.5629 0.5785 -0.0318 -0.0115 0.0632  89  ALA A C   
612  O  O   . ALA A 113 ? 0.4502 0.5565 0.5700 -0.0269 -0.0089 0.0664  89  ALA A O   
613  C  CB  . ALA A 113 ? 0.4238 0.5292 0.5529 -0.0422 -0.0126 0.0717  89  ALA A CB  
614  N  N   . PRO A 114 ? 0.4774 0.5640 0.5801 -0.0341 -0.0163 0.0578  90  PRO A N   
615  C  CA  . PRO A 114 ? 0.4377 0.5235 0.5373 -0.0303 -0.0181 0.0557  90  PRO A CA  
616  C  C   . PRO A 114 ? 0.4418 0.5391 0.5530 -0.0312 -0.0218 0.0609  90  PRO A C   
617  O  O   . PRO A 114 ? 0.4393 0.5372 0.5497 -0.0274 -0.0228 0.0606  90  PRO A O   
618  C  CB  . PRO A 114 ? 0.4736 0.5469 0.5607 -0.0338 -0.0226 0.0497  90  PRO A CB  
619  C  CG  . PRO A 114 ? 0.4752 0.5454 0.5626 -0.0409 -0.0253 0.0493  90  PRO A CG  
620  C  CD  . PRO A 114 ? 0.4653 0.5408 0.5597 -0.0398 -0.0199 0.0535  90  PRO A CD  
621  N  N   . THR A 115 ? 0.4583 0.5652 0.5811 -0.0361 -0.0241 0.0659  91  THR A N   
622  C  CA  . THR A 115 ? 0.4471 0.5672 0.5829 -0.0369 -0.0277 0.0716  91  THR A CA  
623  C  C   . THR A 115 ? 0.4454 0.5773 0.5927 -0.0304 -0.0214 0.0773  91  THR A C   
624  O  O   . THR A 115 ? 0.4474 0.5912 0.6065 -0.0297 -0.0235 0.0826  91  THR A O   
625  C  CB  . THR A 115 ? 0.4608 0.5862 0.6047 -0.0461 -0.0337 0.0741  91  THR A CB  
626  O  OG1 . THR A 115 ? 0.4576 0.5826 0.6053 -0.0483 -0.0296 0.0757  91  THR A OG1 
627  C  CG2 . THR A 115 ? 0.4375 0.5530 0.5709 -0.0522 -0.0410 0.0682  91  THR A CG2 
628  N  N   . MET A 116 ? 0.4676 0.5972 0.6117 -0.0253 -0.0137 0.0763  92  MET A N   
629  C  CA  . MET A 116 ? 0.4391 0.5804 0.5938 -0.0193 -0.0070 0.0813  92  MET A CA  
630  C  C   . MET A 116 ? 0.4763 0.6176 0.6300 -0.0107 -0.0038 0.0798  92  MET A C   
631  O  O   . MET A 116 ? 0.4546 0.5846 0.5973 -0.0086 -0.0049 0.0741  92  MET A O   
632  C  CB  . MET A 116 ? 0.4659 0.6057 0.6167 -0.0174 0.0000  0.0809  92  MET A CB  
633  C  CG  . MET A 116 ? 0.4657 0.6065 0.6204 -0.0252 -0.0019 0.0840  92  MET A CG  
634  S  SD  . MET A 116 ? 0.5013 0.6414 0.6514 -0.0221 0.0068  0.0850  92  MET A SD  
635  C  CE  . MET A 116 ? 0.4313 0.5752 0.5923 -0.0320 0.0038  0.0912  92  MET A CE  
636  N  N   . SER A 117 ? 0.4630 0.6169 0.6292 -0.0055 0.0006  0.0852  93  SER A N   
637  C  CA  . SER A 117 ? 0.4661 0.6207 0.6339 0.0034  0.0048  0.0841  93  SER A CA  
638  C  C   . SER A 117 ? 0.4756 0.6236 0.6339 0.0100  0.0127  0.0785  93  SER A C   
639  O  O   . SER A 117 ? 0.4757 0.6221 0.6283 0.0084  0.0157  0.0772  93  SER A O   
640  C  CB  . SER A 117 ? 0.4473 0.6185 0.6330 0.0069  0.0067  0.0921  93  SER A CB  
641  O  OG  . SER A 117 ? 0.4793 0.6601 0.6715 0.0082  0.0130  0.0957  93  SER A OG  
642  N  N   . ILE A 118 ? 0.4966 0.6411 0.6538 0.0177  0.0161  0.0752  94  ILE A N   
643  C  CA  . ILE A 118 ? 0.4996 0.6385 0.6483 0.0243  0.0234  0.0690  94  ILE A CA  
644  C  C   . ILE A 118 ? 0.4950 0.6467 0.6512 0.0289  0.0309  0.0728  94  ILE A C   
645  O  O   . ILE A 118 ? 0.4741 0.6246 0.6222 0.0308  0.0358  0.0696  94  ILE A O   
646  C  CB  . ILE A 118 ? 0.4845 0.6156 0.6313 0.0309  0.0248  0.0641  94  ILE A CB  
647  C  CG1 . ILE A 118 ? 0.4469 0.5641 0.5834 0.0267  0.0186  0.0597  94  ILE A CG1 
648  C  CG2 . ILE A 118 ? 0.4310 0.5592 0.5720 0.0387  0.0327  0.0577  94  ILE A CG2 
649  C  CD1 . ILE A 118 ? 0.4089 0.5156 0.5304 0.0233  0.0184  0.0532  94  ILE A CD1 
650  N  N   . ALA A 119 ? 0.4504 0.6156 0.6224 0.0310  0.0319  0.0800  95  ALA A N   
651  C  CA  . ALA A 119 ? 0.5206 0.6995 0.7011 0.0358  0.0396  0.0844  95  ALA A CA  
652  C  C   . ALA A 119 ? 0.5255 0.7087 0.7038 0.0300  0.0403  0.0875  95  ALA A C   
653  O  O   . ALA A 119 ? 0.5362 0.7243 0.7115 0.0343  0.0476  0.0873  95  ALA A O   
654  C  CB  . ALA A 119 ? 0.4697 0.6634 0.6693 0.0377  0.0393  0.0928  95  ALA A CB  
655  N  N   . GLU A 120 ? 0.5406 0.7220 0.7201 0.0205  0.0329  0.0905  96  GLU A N   
656  C  CA  . GLU A 120 ? 0.5470 0.7303 0.7248 0.0145  0.0332  0.0934  96  GLU A CA  
657  C  C   . GLU A 120 ? 0.5349 0.7052 0.6947 0.0152  0.0351  0.0861  96  GLU A C   
658  O  O   . GLU A 120 ? 0.5078 0.6819 0.6642 0.0170  0.0408  0.0874  96  GLU A O   
659  C  CB  . GLU A 120 ? 0.5061 0.6892 0.6899 0.0042  0.0243  0.0972  96  GLU A CB  
660  C  CG  . GLU A 120 ? 0.5240 0.7055 0.7058 -0.0029 0.0237  0.0994  96  GLU A CG  
661  C  CD  . GLU A 120 ? 0.6021 0.7845 0.7920 -0.0131 0.0151  0.1028  96  GLU A CD  
662  O  OE1 . GLU A 120 ? 0.5993 0.7809 0.7918 -0.0150 0.0086  0.1018  96  GLU A OE1 
663  O  OE2 . GLU A 120 ? 0.6482 0.8321 0.8420 -0.0192 0.0148  0.1066  96  GLU A OE2 
664  N  N   . ARG A 121 ? 0.4663 0.6222 0.6147 0.0139  0.0303  0.0789  97  ARG A N   
665  C  CA  . ARG A 121 ? 0.4786 0.6223 0.6111 0.0129  0.0305  0.0725  97  ARG A CA  
666  C  C   . ARG A 121 ? 0.4543 0.5981 0.5784 0.0212  0.0382  0.0678  97  ARG A C   
667  O  O   . ARG A 121 ? 0.4366 0.5758 0.5499 0.0209  0.0400  0.0651  97  ARG A O   
668  C  CB  . ARG A 121 ? 0.4574 0.5869 0.5811 0.0101  0.0240  0.0662  97  ARG A CB  
669  C  CG  . ARG A 121 ? 0.4232 0.5491 0.5485 0.0009  0.0162  0.0684  97  ARG A CG  
670  C  CD  . ARG A 121 ? 0.4347 0.5518 0.5560 -0.0005 0.0102  0.0644  97  ARG A CD  
671  N  NE  . ARG A 121 ? 0.4534 0.5589 0.5621 0.0038  0.0119  0.0567  97  ARG A NE  
672  C  CZ  . ARG A 121 ? 0.4157 0.5141 0.5212 0.0051  0.0089  0.0533  97  ARG A CZ  
673  N  NH1 . ARG A 121 ? 0.4071 0.5089 0.5199 0.0029  0.0041  0.0569  97  ARG A NH1 
674  N  NH2 . ARG A 121 ? 0.3679 0.4562 0.4631 0.0085  0.0108  0.0464  97  ARG A NH2 
675  N  N   . ILE A 122 ? 0.4094 0.5585 0.5383 0.0289  0.0428  0.0667  98  ILE A N   
676  C  CA  . ILE A 122 ? 0.4376 0.5852 0.5573 0.0370  0.0495  0.0601  98  ILE A CA  
677  C  C   . ILE A 122 ? 0.4608 0.6211 0.5816 0.0408  0.0572  0.0641  98  ILE A C   
678  O  O   . ILE A 122 ? 0.4452 0.6043 0.5553 0.0466  0.0623  0.0584  98  ILE A O   
679  C  CB  . ILE A 122 ? 0.4750 0.6215 0.5994 0.0440  0.0514  0.0563  98  ILE A CB  
680  C  CG1 . ILE A 122 ? 0.4786 0.6193 0.5915 0.0514  0.0566  0.0467  98  ILE A CG1 
681  C  CG2 . ILE A 122 ? 0.4882 0.6501 0.6289 0.0477  0.0554  0.0639  98  ILE A CG2 
682  C  CD1 . ILE A 122 ? 0.5349 0.6718 0.6524 0.0581  0.0584  0.0419  98  ILE A CD1 
683  N  N   . GLN A 123 ? 0.4459 0.6185 0.5792 0.0376  0.0581  0.0740  99  GLN A N   
684  C  CA  . GLN A 123 ? 0.4684 0.6555 0.6055 0.0426  0.0665  0.0790  99  GLN A CA  
685  C  C   . GLN A 123 ? 0.4166 0.6025 0.5407 0.0424  0.0696  0.0780  99  GLN A C   
686  O  O   . GLN A 123 ? 0.4246 0.6166 0.5423 0.0499  0.0770  0.0757  99  GLN A O   
687  C  CB  . GLN A 123 ? 0.4351 0.6363 0.5907 0.0386  0.0664  0.0904  99  GLN A CB  
688  C  CG  . GLN A 123 ? 0.5106 0.7175 0.6801 0.0412  0.0654  0.0925  99  GLN A CG  
689  C  CD  . GLN A 123 ? 0.5774 0.7997 0.7662 0.0370  0.0649  0.1039  99  GLN A CD  
690  O  OE1 . GLN A 123 ? 0.5909 0.8245 0.7846 0.0367  0.0700  0.1107  99  GLN A OE1 
691  N  NE2 . GLN A 123 ? 0.6048 0.8282 0.8048 0.0336  0.0586  0.1065  99  GLN A NE2 
692  N  N   . PRO A 124 ? 0.4196 0.5985 0.5394 0.0346  0.0646  0.0798  100 PRO A N   
693  C  CA  . PRO A 124 ? 0.4319 0.6103 0.5397 0.0353  0.0678  0.0797  100 PRO A CA  
694  C  C   . PRO A 124 ? 0.4351 0.6076 0.5265 0.0423  0.0706  0.0694  100 PRO A C   
695  O  O   . PRO A 124 ? 0.4268 0.6078 0.5119 0.0483  0.0775  0.0695  100 PRO A O   
696  C  CB  . PRO A 124 ? 0.4529 0.6207 0.5590 0.0259  0.0604  0.0812  100 PRO A CB  
697  C  CG  . PRO A 124 ? 0.4347 0.6048 0.5563 0.0197  0.0555  0.0865  100 PRO A CG  
698  C  CD  . PRO A 124 ? 0.4072 0.5805 0.5342 0.0252  0.0564  0.0833  100 PRO A CD  
699  N  N   . ALA A 125 ? 0.4197 0.5783 0.5040 0.0417  0.0654  0.0604  101 ALA A N   
700  C  CA  . ALA A 125 ? 0.4304 0.5828 0.5002 0.0475  0.0672  0.0500  101 ALA A CA  
701  C  C   . ALA A 125 ? 0.4268 0.5875 0.4979 0.0568  0.0743  0.0465  101 ALA A C   
702  O  O   . ALA A 125 ? 0.4126 0.5754 0.4722 0.0627  0.0789  0.0406  101 ALA A O   
703  C  CB  . ALA A 125 ? 0.4254 0.5619 0.4903 0.0446  0.0603  0.0420  101 ALA A CB  
704  N  N   . GLN A 126 ? 0.4067 0.5724 0.4916 0.0584  0.0754  0.0497  102 GLN A N   
705  C  CA  . GLN A 126 ? 0.4574 0.6306 0.5448 0.0678  0.0825  0.0463  102 GLN A CA  
706  C  C   . GLN A 126 ? 0.4566 0.6452 0.5421 0.0726  0.0909  0.0511  102 GLN A C   
707  O  O   . GLN A 126 ? 0.4633 0.6559 0.5413 0.0808  0.0972  0.0447  102 GLN A O   
708  C  CB  . GLN A 126 ? 0.4765 0.6534 0.5810 0.0684  0.0819  0.0507  102 GLN A CB  
709  C  CG  . GLN A 126 ? 0.4536 0.6359 0.5617 0.0785  0.0891  0.0463  102 GLN A CG  
710  C  CD  . GLN A 126 ? 0.5069 0.6913 0.6319 0.0794  0.0877  0.0503  102 GLN A CD  
711  O  OE1 . GLN A 126 ? 0.5420 0.7242 0.6752 0.0722  0.0809  0.0561  102 GLN A OE1 
712  N  NE2 . GLN A 126 ? 0.4790 0.6680 0.6091 0.0886  0.0941  0.0471  102 GLN A NE2 
713  N  N   . HIS A 127 ? 0.4428 0.6405 0.5351 0.0674  0.0911  0.0623  103 HIS A N   
714  C  CA  . HIS A 127 ? 0.4368 0.6504 0.5290 0.0717  0.0995  0.0689  103 HIS A CA  
715  C  C   . HIS A 127 ? 0.4522 0.6645 0.5265 0.0730  0.1011  0.0654  103 HIS A C   
716  O  O   . HIS A 127 ? 0.4423 0.6634 0.5081 0.0808  0.1083  0.0627  103 HIS A O   
717  C  CB  . HIS A 127 ? 0.4340 0.6578 0.5418 0.0653  0.0991  0.0828  103 HIS A CB  
718  C  CG  . HIS A 127 ? 0.4806 0.7214 0.5898 0.0688  0.1078  0.0914  103 HIS A CG  
719  N  ND1 . HIS A 127 ? 0.5303 0.7852 0.6437 0.0776  0.1167  0.0925  103 HIS A ND1 
720  C  CD2 . HIS A 127 ? 0.4680 0.7141 0.5750 0.0651  0.1092  0.0996  103 HIS A CD2 
721  C  CE1 . HIS A 127 ? 0.5576 0.8267 0.6709 0.0791  0.1234  0.1013  103 HIS A CE1 
722  N  NE2 . HIS A 127 ? 0.5110 0.7749 0.6207 0.0715  0.1189  0.1061  103 HIS A NE2 
723  N  N   . TYR A 128 ? 0.4472 0.6491 0.5155 0.0657  0.0944  0.0656  104 TYR A N   
724  C  CA  . TYR A 128 ? 0.4378 0.6399 0.4913 0.0662  0.0955  0.0650  104 TYR A CA  
725  C  C   . TYR A 128 ? 0.4349 0.6282 0.4714 0.0708  0.0943  0.0514  104 TYR A C   
726  O  O   . TYR A 128 ? 0.4306 0.6270 0.4537 0.0732  0.0962  0.0499  104 TYR A O   
727  C  CB  . TYR A 128 ? 0.4215 0.6162 0.4768 0.0568  0.0891  0.0712  104 TYR A CB  
728  C  CG  . TYR A 128 ? 0.4652 0.6697 0.5360 0.0519  0.0908  0.0850  104 TYR A CG  
729  C  CD1 . TYR A 128 ? 0.4465 0.6657 0.5179 0.0547  0.0980  0.0941  104 TYR A CD1 
730  C  CD2 . TYR A 128 ? 0.4472 0.6468 0.5322 0.0444  0.0850  0.0890  104 TYR A CD2 
731  C  CE1 . TYR A 128 ? 0.4391 0.6673 0.5261 0.0498  0.0997  0.1071  104 TYR A CE1 
732  C  CE2 . TYR A 128 ? 0.4033 0.6119 0.5034 0.0393  0.0861  0.1011  104 TYR A CE2 
733  C  CZ  . TYR A 128 ? 0.4632 0.6858 0.5649 0.0419  0.0935  0.1103  104 TYR A CZ  
734  O  OH  . TYR A 128 ? 0.4497 0.6813 0.5679 0.0364  0.0946  0.1227  104 TYR A OH  
735  N  N   . ARG A 129 ? 0.4363 0.6191 0.4735 0.0721  0.0911  0.0419  105 ARG A N   
736  C  CA  . ARG A 129 ? 0.4387 0.6128 0.4619 0.0762  0.0898  0.0284  105 ARG A CA  
737  C  C   . ARG A 129 ? 0.4290 0.5961 0.4392 0.0721  0.0850  0.0263  105 ARG A C   
738  O  O   . ARG A 129 ? 0.4216 0.5927 0.4180 0.0765  0.0875  0.0214  105 ARG A O   
739  C  CB  . ARG A 129 ? 0.4665 0.6511 0.4827 0.0860  0.0980  0.0231  105 ARG A CB  
740  C  CG  . ARG A 129 ? 0.5061 0.6955 0.5345 0.0914  0.1028  0.0226  105 ARG A CG  
741  C  CD  . ARG A 129 ? 0.5554 0.7530 0.5750 0.1017  0.1108  0.0147  105 ARG A CD  
742  N  NE  . ARG A 129 ? 0.6019 0.8172 0.6183 0.1053  0.1182  0.0229  105 ARG A NE  
743  C  CZ  . ARG A 129 ? 0.6733 0.9024 0.7025 0.1075  0.1244  0.0331  105 ARG A CZ  
744  N  NH1 . ARG A 129 ? 0.6139 0.8418 0.6603 0.1063  0.1237  0.0368  105 ARG A NH1 
745  N  NH2 . ARG A 129 ? 0.5949 0.8403 0.6199 0.1111  0.1316  0.0403  105 ARG A NH2 
746  N  N   . PRO A 130 ? 0.4484 0.6057 0.4626 0.0640  0.0781  0.0297  106 PRO A N   
747  C  CA  . PRO A 130 ? 0.4051 0.5559 0.4082 0.0604  0.0738  0.0283  106 PRO A CA  
748  C  C   . PRO A 130 ? 0.4448 0.5861 0.4363 0.0627  0.0707  0.0151  106 PRO A C   
749  O  O   . PRO A 130 ? 0.4104 0.5465 0.4037 0.0657  0.0707  0.0068  106 PRO A O   
750  C  CB  . PRO A 130 ? 0.3768 0.5186 0.3890 0.0515  0.0675  0.0342  106 PRO A CB  
751  C  CG  . PRO A 130 ? 0.4041 0.5430 0.4285 0.0509  0.0664  0.0334  106 PRO A CG  
752  C  CD  . PRO A 130 ? 0.4150 0.5671 0.4437 0.0580  0.0740  0.0350  106 PRO A CD  
753  N  N   . GLU A 131 ? 0.4158 0.5549 0.3958 0.0614  0.0681  0.0134  107 GLU A N   
754  C  CA  . GLU A 131 ? 0.4440 0.5734 0.4143 0.0619  0.0638  0.0016  107 GLU A CA  
755  C  C   . GLU A 131 ? 0.4104 0.5251 0.3877 0.0563  0.0575  -0.0014 107 GLU A C   
756  O  O   . GLU A 131 ? 0.4245 0.5309 0.3996 0.0576  0.0553  -0.0114 107 GLU A O   
757  C  CB  . GLU A 131 ? 0.4408 0.5719 0.3990 0.0610  0.0617  0.0020  107 GLU A CB  
758  C  CG  . GLU A 131 ? 0.4377 0.5841 0.3869 0.0667  0.0675  0.0052  107 GLU A CG  
759  C  CD  . GLU A 131 ? 0.4857 0.6338 0.4234 0.0659  0.0647  0.0060  107 GLU A CD  
760  O  OE1 . GLU A 131 ? 0.4895 0.6348 0.4166 0.0679  0.0619  -0.0045 107 GLU A OE1 
761  O  OE2 . GLU A 131 ? 0.4796 0.6316 0.4194 0.0630  0.0651  0.0173  107 GLU A OE2 
762  N  N   . LEU A 132 ? 0.3929 0.5043 0.3788 0.0501  0.0547  0.0072  108 LEU A N   
763  C  CA  . LEU A 132 ? 0.3765 0.4749 0.3677 0.0444  0.0486  0.0056  108 LEU A CA  
764  C  C   . LEU A 132 ? 0.4168 0.5163 0.4216 0.0408  0.0484  0.0138  108 LEU A C   
765  O  O   . LEU A 132 ? 0.3916 0.4997 0.4013 0.0397  0.0510  0.0229  108 LEU A O   
766  C  CB  . LEU A 132 ? 0.4166 0.5083 0.4020 0.0394  0.0438  0.0066  108 LEU A CB  
767  C  CG  . LEU A 132 ? 0.4327 0.5151 0.4098 0.0391  0.0397  -0.0029 108 LEU A CG  
768  C  CD1 . LEU A 132 ? 0.4237 0.5012 0.3976 0.0342  0.0357  0.0007  108 LEU A CD1 
769  C  CD2 . LEU A 132 ? 0.4121 0.4843 0.3946 0.0380  0.0368  -0.0089 108 LEU A CD2 
770  N  N   . ALA A 133 ? 0.3936 0.4848 0.4047 0.0388  0.0450  0.0109  109 ALA A N   
771  C  CA  . ALA A 133 ? 0.4027 0.4938 0.4259 0.0343  0.0429  0.0180  109 ALA A CA  
772  C  C   . ALA A 133 ? 0.4008 0.4792 0.4248 0.0299  0.0367  0.0144  109 ALA A C   
773  O  O   . ALA A 133 ? 0.3580 0.4293 0.3778 0.0320  0.0356  0.0065  109 ALA A O   
774  C  CB  . ALA A 133 ? 0.3789 0.4782 0.4121 0.0386  0.0471  0.0202  109 ALA A CB  
775  N  N   . SER A 134 ? 0.4144 0.4901 0.4438 0.0236  0.0328  0.0202  110 SER A N   
776  C  CA  . SER A 134 ? 0.3423 0.4077 0.3729 0.0195  0.0272  0.0177  110 SER A CA  
777  C  C   . SER A 134 ? 0.3829 0.4488 0.4217 0.0220  0.0274  0.0169  110 SER A C   
778  O  O   . SER A 134 ? 0.4000 0.4751 0.4471 0.0246  0.0306  0.0211  110 SER A O   
779  C  CB  . SER A 134 ? 0.3772 0.4403 0.4112 0.0124  0.0231  0.0236  110 SER A CB  
780  O  OG  . SER A 134 ? 0.3895 0.4610 0.4346 0.0109  0.0237  0.0306  110 SER A OG  
781  N  N   . LEU A 135 ? 0.3741 0.4305 0.4110 0.0215  0.0242  0.0119  111 LEU A N   
782  C  CA  . LEU A 135 ? 0.3571 0.4124 0.4020 0.0236  0.0238  0.0117  111 LEU A CA  
783  C  C   . LEU A 135 ? 0.3491 0.3956 0.3938 0.0186  0.0180  0.0119  111 LEU A C   
784  O  O   . LEU A 135 ? 0.3672 0.4048 0.4051 0.0179  0.0163  0.0065  111 LEU A O   
785  C  CB  . LEU A 135 ? 0.3812 0.4341 0.4244 0.0301  0.0273  0.0043  111 LEU A CB  
786  C  CG  . LEU A 135 ? 0.4058 0.4573 0.4585 0.0334  0.0278  0.0044  111 LEU A CG  
787  C  CD1 . LEU A 135 ? 0.3870 0.4502 0.4502 0.0360  0.0310  0.0111  111 LEU A CD1 
788  C  CD2 . LEU A 135 ? 0.4146 0.4602 0.4646 0.0388  0.0306  -0.0044 111 LEU A CD2 
789  N  N   . ASN A 136 ? 0.3537 0.4036 0.4057 0.0152  0.0151  0.0181  112 ASN A N   
790  C  CA  . ASN A 136 ? 0.3661 0.4092 0.4173 0.0105  0.0096  0.0188  112 ASN A CA  
791  C  C   . ASN A 136 ? 0.3576 0.3971 0.4132 0.0138  0.0093  0.0174  112 ASN A C   
792  O  O   . ASN A 136 ? 0.3470 0.3924 0.4114 0.0179  0.0117  0.0198  112 ASN A O   
793  C  CB  . ASN A 136 ? 0.3241 0.3728 0.3808 0.0053  0.0061  0.0254  112 ASN A CB  
794  C  CG  . ASN A 136 ? 0.3920 0.4433 0.4459 0.0019  0.0066  0.0272  112 ASN A CG  
795  O  OD1 . ASN A 136 ? 0.3690 0.4134 0.4154 -0.0020 0.0041  0.0252  112 ASN A OD1 
796  N  ND2 . ASN A 136 ? 0.3623 0.4235 0.4225 0.0036  0.0101  0.0314  112 ASN A ND2 
797  N  N   . MET A 137 ? 0.3562 0.3863 0.4065 0.0121  0.0067  0.0140  113 MET A N   
798  C  CA  . MET A 137 ? 0.3457 0.3702 0.3989 0.0157  0.0076  0.0113  113 MET A CA  
799  C  C   . MET A 137 ? 0.3705 0.3945 0.4294 0.0142  0.0040  0.0164  113 MET A C   
800  O  O   . MET A 137 ? 0.3681 0.3869 0.4302 0.0168  0.0045  0.0153  113 MET A O   
801  C  CB  . MET A 137 ? 0.3659 0.3808 0.4106 0.0153  0.0076  0.0043  113 MET A CB  
802  C  CG  . MET A 137 ? 0.3460 0.3616 0.3860 0.0187  0.0115  -0.0017 113 MET A CG  
803  S  SD  . MET A 137 ? 0.4447 0.4653 0.4924 0.0262  0.0169  -0.0036 113 MET A SD  
804  C  CE  . MET A 137 ? 0.3483 0.3604 0.4034 0.0281  0.0160  -0.0045 113 MET A CE  
805  N  N   . GLY A 138 ? 0.3565 0.3860 0.4171 0.0100  0.0003  0.0221  114 GLY A N   
806  C  CA  . GLY A 138 ? 0.3345 0.3651 0.3997 0.0088  -0.0034 0.0272  114 GLY A CA  
807  C  C   . GLY A 138 ? 0.3752 0.4144 0.4436 0.0045  -0.0074 0.0331  114 GLY A C   
808  O  O   . GLY A 138 ? 0.3811 0.4223 0.4458 0.0005  -0.0085 0.0326  114 GLY A O   
809  N  N   . THR A 139 ? 0.3127 0.3574 0.3888 0.0051  -0.0100 0.0389  115 THR A N   
810  C  CA  . THR A 139 ? 0.3437 0.3970 0.4229 0.0005  -0.0149 0.0443  115 THR A CA  
811  C  C   . THR A 139 ? 0.3597 0.4079 0.4289 -0.0052 -0.0200 0.0429  115 THR A C   
812  O  O   . THR A 139 ? 0.3501 0.3913 0.4140 -0.0046 -0.0206 0.0416  115 THR A O   
813  C  CB  . THR A 139 ? 0.3550 0.4170 0.4458 0.0035  -0.0163 0.0514  115 THR A CB  
814  O  OG1 . THR A 139 ? 0.3585 0.4254 0.4590 0.0093  -0.0110 0.0524  115 THR A OG1 
815  C  CG2 . THR A 139 ? 0.3537 0.4258 0.4479 -0.0018 -0.0223 0.0567  115 THR A CG2 
816  N  N   . MET A 140 ? 0.3783 0.4300 0.4453 -0.0109 -0.0235 0.0433  116 MET A N   
817  C  CA  . MET A 140 ? 0.3632 0.4092 0.4197 -0.0162 -0.0277 0.0405  116 MET A CA  
818  C  C   . MET A 140 ? 0.3658 0.4189 0.4243 -0.0221 -0.0330 0.0428  116 MET A C   
819  O  O   . MET A 140 ? 0.3625 0.4231 0.4295 -0.0230 -0.0324 0.0453  116 MET A O   
820  C  CB  . MET A 140 ? 0.3886 0.4246 0.4357 -0.0169 -0.0248 0.0340  116 MET A CB  
821  C  CG  . MET A 140 ? 0.3508 0.3889 0.4006 -0.0171 -0.0217 0.0330  116 MET A CG  
822  S  SD  . MET A 140 ? 0.4394 0.4668 0.4785 -0.0171 -0.0183 0.0263  116 MET A SD  
823  C  CE  . MET A 140 ? 0.3795 0.4024 0.4110 -0.0242 -0.0233 0.0245  116 MET A CE  
824  N  N   . ASN A 141 ? 0.3560 0.4071 0.4071 -0.0263 -0.0380 0.0417  117 ASN A N   
825  C  CA  . ASN A 141 ? 0.3825 0.4365 0.4324 -0.0330 -0.0430 0.0409  117 ASN A CA  
826  C  C   . ASN A 141 ? 0.3980 0.4451 0.4443 -0.0353 -0.0403 0.0362  117 ASN A C   
827  O  O   . ASN A 141 ? 0.3815 0.4196 0.4210 -0.0329 -0.0363 0.0322  117 ASN A O   
828  C  CB  . ASN A 141 ? 0.3853 0.4370 0.4254 -0.0365 -0.0484 0.0390  117 ASN A CB  
829  C  CG  . ASN A 141 ? 0.3705 0.4309 0.4141 -0.0349 -0.0520 0.0448  117 ASN A CG  
830  O  OD1 . ASN A 141 ? 0.3752 0.4447 0.4302 -0.0322 -0.0517 0.0505  117 ASN A OD1 
831  N  ND2 . ASN A 141 ? 0.3932 0.4516 0.4270 -0.0363 -0.0554 0.0437  117 ASN A ND2 
832  N  N   . PHE A 142 ? 0.3864 0.4382 0.4383 -0.0401 -0.0427 0.0372  118 PHE A N   
833  C  CA  . PHE A 142 ? 0.4178 0.4634 0.4674 -0.0430 -0.0408 0.0338  118 PHE A CA  
834  C  C   . PHE A 142 ? 0.4236 0.4692 0.4720 -0.0505 -0.0470 0.0320  118 PHE A C   
835  O  O   . PHE A 142 ? 0.4239 0.4787 0.4820 -0.0541 -0.0506 0.0355  118 PHE A O   
836  C  CB  . PHE A 142 ? 0.4131 0.4643 0.4726 -0.0409 -0.0360 0.0374  118 PHE A CB  
837  C  CG  . PHE A 142 ? 0.4640 0.5074 0.5189 -0.0402 -0.0314 0.0344  118 PHE A CG  
838  C  CD1 . PHE A 142 ? 0.5098 0.5467 0.5610 -0.0455 -0.0332 0.0316  118 PHE A CD1 
839  C  CD2 . PHE A 142 ? 0.4651 0.5078 0.5194 -0.0342 -0.0252 0.0343  118 PHE A CD2 
840  C  CE1 . PHE A 142 ? 0.5012 0.5315 0.5487 -0.0444 -0.0290 0.0299  118 PHE A CE1 
841  C  CE2 . PHE A 142 ? 0.4808 0.5176 0.5304 -0.0334 -0.0214 0.0321  118 PHE A CE2 
842  C  CZ  . PHE A 142 ? 0.4893 0.5202 0.5359 -0.0384 -0.0232 0.0304  118 PHE A CZ  
843  N  N   . GLY A 143 ? 0.4609 0.4964 0.4979 -0.0528 -0.0484 0.0261  119 GLY A N   
844  C  CA  . GLY A 143 ? 0.5147 0.5484 0.5488 -0.0596 -0.0543 0.0227  119 GLY A CA  
845  C  C   . GLY A 143 ? 0.5326 0.5590 0.5679 -0.0631 -0.0526 0.0199  119 GLY A C   
846  O  O   . GLY A 143 ? 0.5047 0.5221 0.5342 -0.0604 -0.0480 0.0173  119 GLY A O   
847  N  N   . LEU A 144 ? 0.6048 0.6356 0.6485 -0.0691 -0.0566 0.0209  120 LEU A N   
848  C  CA  . LEU A 144 ? 0.6384 0.6624 0.6855 -0.0730 -0.0551 0.0193  120 LEU A CA  
849  C  C   . LEU A 144 ? 0.6901 0.7084 0.7338 -0.0801 -0.0612 0.0133  120 LEU A C   
850  O  O   . LEU A 144 ? 0.6939 0.7042 0.7395 -0.0834 -0.0602 0.0110  120 LEU A O   
851  C  CB  . LEU A 144 ? 0.5746 0.6083 0.6371 -0.0739 -0.0534 0.0263  120 LEU A CB  
852  C  CG  . LEU A 144 ? 0.5534 0.5932 0.6195 -0.0667 -0.0471 0.0316  120 LEU A CG  
853  C  CD1 . LEU A 144 ? 0.5532 0.6036 0.6345 -0.0678 -0.0452 0.0386  120 LEU A CD1 
854  C  CD2 . LEU A 144 ? 0.5740 0.6039 0.6311 -0.0618 -0.0410 0.0291  120 LEU A CD2 
855  N  N   . PHE A 145 ? 0.9063 0.9285 0.9448 -0.0822 -0.0672 0.0108  121 PHE A N   
856  C  CA  . PHE A 145 ? 0.9460 0.9643 0.9814 -0.0894 -0.0738 0.0043  121 PHE A CA  
857  C  C   . PHE A 145 ? 0.9504 0.9533 0.9737 -0.0892 -0.0717 -0.0035 121 PHE A C   
858  O  O   . PHE A 145 ? 1.0000 0.9965 1.0230 -0.0950 -0.0753 -0.0092 121 PHE A O   
859  C  CB  . PHE A 145 ? 0.9438 0.9722 0.9766 -0.0914 -0.0811 0.0040  121 PHE A CB  
860  C  CG  . PHE A 145 ? 1.0123 1.0446 1.0369 -0.0848 -0.0794 0.0065  121 PHE A CG  
861  C  CD1 . PHE A 145 ? 0.9290 0.9696 0.9613 -0.0795 -0.0757 0.0142  121 PHE A CD1 
862  C  CD2 . PHE A 145 ? 1.0337 1.0608 1.0433 -0.0837 -0.0809 0.0011  121 PHE A CD2 
863  C  CE1 . PHE A 145 ? 0.9056 0.9486 0.9315 -0.0736 -0.0740 0.0166  121 PHE A CE1 
864  C  CE2 . PHE A 145 ? 0.9892 1.0197 0.9924 -0.0777 -0.0790 0.0042  121 PHE A CE2 
865  C  CZ  . PHE A 145 ? 0.9263 0.9642 0.9381 -0.0729 -0.0757 0.0119  121 PHE A CZ  
866  N  N   . PRO A 146 ? 0.8370 0.8335 0.8509 -0.0828 -0.0662 -0.0043 122 PRO A N   
867  C  CA  . PRO A 146 ? 0.8530 0.8355 0.8579 -0.0823 -0.0634 -0.0106 122 PRO A CA  
868  C  C   . PRO A 146 ? 0.8224 0.7981 0.8363 -0.0858 -0.0616 -0.0106 122 PRO A C   
869  O  O   . PRO A 146 ? 0.8228 0.7874 0.8322 -0.0879 -0.0617 -0.0166 122 PRO A O   
870  C  CB  . PRO A 146 ? 0.8021 0.7826 0.8023 -0.0747 -0.0567 -0.0079 122 PRO A CB  
871  C  CG  . PRO A 146 ? 0.7883 0.7796 0.7882 -0.0717 -0.0580 -0.0037 122 PRO A CG  
872  C  CD  . PRO A 146 ? 0.8185 0.8206 0.8299 -0.0761 -0.0628 0.0003  122 PRO A CD  
873  N  N   . MET A 147 ? 0.7726 0.7551 0.7992 -0.0858 -0.0594 -0.0034 123 MET A N   
874  C  CA  . MET A 147 ? 0.7172 0.6946 0.7539 -0.0891 -0.0574 -0.0015 123 MET A CA  
875  C  C   . MET A 147 ? 0.6778 0.6563 0.7226 -0.0978 -0.0640 -0.0040 123 MET A C   
876  O  O   . MET A 147 ? 0.6559 0.6276 0.7085 -0.1018 -0.0633 -0.0041 123 MET A O   
877  C  CB  . MET A 147 ? 0.6312 0.6170 0.6784 -0.0859 -0.0524 0.0075  123 MET A CB  
878  C  CG  . MET A 147 ? 0.6511 0.6314 0.6933 -0.0793 -0.0452 0.0091  123 MET A CG  
879  S  SD  . MET A 147 ? 0.6419 0.6342 0.6918 -0.0736 -0.0395 0.0183  123 MET A SD  
880  C  CE  . MET A 147 ? 0.6180 0.6232 0.6699 -0.0734 -0.0438 0.0199  123 MET A CE  
881  N  N   . LEU A 148 ? 0.7196 0.7066 0.7634 -0.1008 -0.0705 -0.0056 124 LEU A N   
882  C  CA  . LEU A 148 ? 0.7237 0.7119 0.7747 -0.1095 -0.0777 -0.0091 124 LEU A CA  
883  C  C   . LEU A 148 ? 0.7269 0.7011 0.7681 -0.1128 -0.0803 -0.0197 124 LEU A C   
884  O  O   . LEU A 148 ? 0.6879 0.6572 0.7365 -0.1200 -0.0841 -0.0234 124 LEU A O   
885  C  CB  . LEU A 148 ? 0.7204 0.7232 0.7727 -0.1114 -0.0843 -0.0075 124 LEU A CB  
886  C  CG  . LEU A 148 ? 0.6611 0.6784 0.7310 -0.1139 -0.0857 0.0012  124 LEU A CG  
887  C  CD1 . LEU A 148 ? 0.6697 0.7015 0.7391 -0.1141 -0.0918 0.0030  124 LEU A CD1 
888  C  CD2 . LEU A 148 ? 0.6202 0.6354 0.7038 -0.1226 -0.0891 0.0004  124 LEU A CD2 
889  N  N   . ASN A 149 ? 0.7215 0.6890 0.7468 -0.1078 -0.0782 -0.0247 125 ASN A N   
890  C  CA  . ASN A 149 ? 0.7399 0.6943 0.7551 -0.1102 -0.0800 -0.0352 125 ASN A CA  
891  C  C   . ASN A 149 ? 0.6910 0.6320 0.7134 -0.1121 -0.0764 -0.0366 125 ASN A C   
892  O  O   . ASN A 149 ? 0.7461 0.6782 0.7696 -0.1179 -0.0800 -0.0441 125 ASN A O   
893  C  CB  . ASN A 149 ? 0.8206 0.7712 0.8189 -0.1034 -0.0769 -0.0387 125 ASN A CB  
894  C  CG  . ASN A 149 ? 0.9020 0.8654 0.8935 -0.1011 -0.0801 -0.0365 125 ASN A CG  
895  O  OD1 . ASN A 149 ? 0.9001 0.8736 0.8974 -0.0978 -0.0782 -0.0282 125 ASN A OD1 
896  N  ND2 . ASN A 149 ? 0.9455 0.9086 0.9247 -0.1025 -0.0846 -0.0437 125 ASN A ND2 
897  N  N   . ARG A 150 ? 0.6978 0.6372 0.7253 -0.1073 -0.0693 -0.0295 126 ARG A N   
898  C  CA  . ARG A 150 ? 0.6293 0.5565 0.6633 -0.1081 -0.0651 -0.0292 126 ARG A CA  
899  C  C   . ARG A 150 ? 0.5994 0.5300 0.6519 -0.1140 -0.0661 -0.0232 126 ARG A C   
900  O  O   . ARG A 150 ? 0.5965 0.5160 0.6560 -0.1179 -0.0655 -0.0251 126 ARG A O   
901  C  CB  . ARG A 150 ? 0.6294 0.5540 0.6596 -0.0999 -0.0570 -0.0242 126 ARG A CB  
902  C  CG  . ARG A 150 ? 0.6319 0.5447 0.6686 -0.0996 -0.0522 -0.0225 126 ARG A CG  
903  C  CD  . ARG A 150 ? 0.6262 0.5408 0.6615 -0.0919 -0.0450 -0.0154 126 ARG A CD  
904  N  NE  . ARG A 150 ? 0.6333 0.5440 0.6542 -0.0857 -0.0425 -0.0198 126 ARG A NE  
905  C  CZ  . ARG A 150 ? 0.6442 0.5424 0.6595 -0.0834 -0.0398 -0.0245 126 ARG A CZ  
906  N  NH1 . ARG A 150 ? 0.6494 0.5367 0.6718 -0.0867 -0.0393 -0.0260 126 ARG A NH1 
907  N  NH2 . ARG A 150 ? 0.6659 0.5627 0.6691 -0.0777 -0.0374 -0.0276 126 ARG A NH2 
908  N  N   . TYR A 151 ? 0.6029 0.5484 0.6640 -0.1148 -0.0674 -0.0156 127 TYR A N   
909  C  CA  . TYR A 151 ? 0.5593 0.5099 0.6386 -0.1187 -0.0663 -0.0074 127 TYR A CA  
910  C  C   . TYR A 151 ? 0.5692 0.5296 0.6601 -0.1269 -0.0737 -0.0071 127 TYR A C   
911  O  O   . TYR A 151 ? 0.5386 0.5030 0.6461 -0.1311 -0.0731 -0.0004 127 TYR A O   
912  C  CB  . TYR A 151 ? 0.5151 0.4761 0.5977 -0.1120 -0.0599 0.0030  127 TYR A CB  
913  C  CG  . TYR A 151 ? 0.5472 0.5000 0.6226 -0.1047 -0.0524 0.0047  127 TYR A CG  
914  C  CD1 . TYR A 151 ? 0.5389 0.4807 0.6199 -0.1058 -0.0488 0.0060  127 TYR A CD1 
915  C  CD2 . TYR A 151 ? 0.5396 0.4961 0.6037 -0.0969 -0.0489 0.0054  127 TYR A CD2 
916  C  CE1 . TYR A 151 ? 0.5268 0.4625 0.6016 -0.0991 -0.0423 0.0081  127 TYR A CE1 
917  C  CE2 . TYR A 151 ? 0.5353 0.4855 0.5934 -0.0906 -0.0426 0.0068  127 TYR A CE2 
918  C  CZ  . TYR A 151 ? 0.5677 0.5080 0.6309 -0.0916 -0.0395 0.0083  127 TYR A CZ  
919  O  OH  . TYR A 151 ? 0.5587 0.4938 0.6163 -0.0853 -0.0336 0.0101  127 TYR A OH  
920  N  N   . GLU A 152 ? 0.5699 0.5349 0.6532 -0.1294 -0.0808 -0.0136 128 GLU A N   
921  C  CA  . GLU A 152 ? 0.5675 0.5453 0.6622 -0.1364 -0.0881 -0.0119 128 GLU A CA  
922  C  C   . GLU A 152 ? 0.5858 0.5582 0.6964 -0.1456 -0.0910 -0.0128 128 GLU A C   
923  O  O   . GLU A 152 ? 0.5571 0.5405 0.6847 -0.1500 -0.0925 -0.0055 128 GLU A O   
924  C  CB  . GLU A 152 ? 0.6185 0.6004 0.7008 -0.1380 -0.0957 -0.0199 128 GLU A CB  
925  C  CG  . GLU A 152 ? 0.7028 0.6989 0.7966 -0.1455 -0.1043 -0.0187 128 GLU A CG  
926  C  CD  . GLU A 152 ? 0.7358 0.7406 0.8172 -0.1450 -0.1111 -0.0233 128 GLU A CD  
927  O  OE1 . GLU A 152 ? 0.7279 0.7263 0.7913 -0.1396 -0.1094 -0.0286 128 GLU A OE1 
928  O  OE2 . GLU A 152 ? 0.7514 0.7704 0.8414 -0.1499 -0.1181 -0.0211 128 GLU A OE2 
929  N  N   . SER A 153 ? 0.6017 0.5571 0.7079 -0.1487 -0.0917 -0.0217 129 SER A N   
930  C  CA  . SER A 153 ? 0.5869 0.5355 0.7086 -0.1580 -0.0950 -0.0236 129 SER A CA  
931  C  C   . SER A 153 ? 0.5330 0.4804 0.6712 -0.1576 -0.0880 -0.0126 129 SER A C   
932  O  O   . SER A 153 ? 0.5956 0.5417 0.7511 -0.1656 -0.0903 -0.0107 129 SER A O   
933  C  CB  . SER A 153 ? 0.5907 0.5203 0.7032 -0.1605 -0.0970 -0.0366 129 SER A CB  
934  O  OG  . SER A 153 ? 0.6973 0.6145 0.8000 -0.1527 -0.0889 -0.0366 129 SER A OG  
935  N  N   . GLN A 154 ? 0.5565 0.5048 0.6898 -0.1487 -0.0795 -0.0053 130 GLN A N   
936  C  CA  . GLN A 154 ? 0.5553 0.5030 0.7019 -0.1472 -0.0722 0.0055  130 GLN A CA  
937  C  C   . GLN A 154 ? 0.5288 0.4954 0.6879 -0.1466 -0.0704 0.0175  130 GLN A C   
938  O  O   . GLN A 154 ? 0.5027 0.4712 0.6751 -0.1466 -0.0650 0.0272  130 GLN A O   
939  C  CB  . GLN A 154 ? 0.5452 0.4844 0.6797 -0.1377 -0.0640 0.0072  130 GLN A CB  
940  C  CG  . GLN A 154 ? 0.5862 0.5081 0.7064 -0.1362 -0.0645 -0.0041 130 GLN A CG  
941  C  CD  . GLN A 154 ? 0.6029 0.5185 0.7130 -0.1269 -0.0565 -0.0013 130 GLN A CD  
942  O  OE1 . GLN A 154 ? 0.5961 0.5164 0.7127 -0.1230 -0.0503 0.0089  130 GLN A OE1 
943  N  NE2 . GLN A 154 ? 0.6227 0.5287 0.7168 -0.1231 -0.0566 -0.0104 130 GLN A NE2 
944  N  N   . LEU A 155 ? 0.5254 0.5063 0.6809 -0.1455 -0.0744 0.0174  131 LEU A N   
945  C  CA  . LEU A 155 ? 0.5037 0.5028 0.6695 -0.1430 -0.0717 0.0285  131 LEU A CA  
946  C  C   . LEU A 155 ? 0.5074 0.5140 0.6959 -0.1518 -0.0744 0.0347  131 LEU A C   
947  O  O   . LEU A 155 ? 0.5591 0.5652 0.7539 -0.1606 -0.0826 0.0288  131 LEU A O   
948  C  CB  . LEU A 155 ? 0.4760 0.4875 0.6329 -0.1397 -0.0756 0.0267  131 LEU A CB  
949  C  CG  . LEU A 155 ? 0.5077 0.5127 0.6432 -0.1314 -0.0732 0.0211  131 LEU A CG  
950  C  CD1 . LEU A 155 ? 0.5038 0.5215 0.6329 -0.1289 -0.0774 0.0203  131 LEU A CD1 
951  C  CD2 . LEU A 155 ? 0.4255 0.4281 0.5571 -0.1229 -0.0636 0.0271  131 LEU A CD2 
952  N  N   . LYS A 156 ? 0.4726 0.4870 0.6735 -0.1495 -0.0674 0.0465  132 LYS A N   
953  C  CA  . LYS A 156 ? 0.5076 0.5296 0.7317 -0.1573 -0.0683 0.0543  132 LYS A CA  
954  C  C   . LYS A 156 ? 0.5183 0.5624 0.7536 -0.1568 -0.0690 0.0626  132 LYS A C   
955  O  O   . LYS A 156 ? 0.5242 0.5769 0.7787 -0.1650 -0.0729 0.0667  132 LYS A O   
956  C  CB  . LYS A 156 ? 0.4882 0.5042 0.7207 -0.1556 -0.0597 0.0631  132 LYS A CB  
957  C  CG  . LYS A 156 ? 0.5868 0.5809 0.8120 -0.1563 -0.0585 0.0565  132 LYS A CG  
958  C  CD  . LYS A 156 ? 0.6255 0.6095 0.8622 -0.1677 -0.0658 0.0500  132 LYS A CD  
959  C  CE  . LYS A 156 ? 0.6825 0.6442 0.9138 -0.1679 -0.0637 0.0440  132 LYS A CE  
960  N  NZ  . LYS A 156 ? 0.6621 0.6132 0.8704 -0.1630 -0.0658 0.0317  132 LYS A NZ  
961  N  N   . HIS A 157 ? 0.4982 0.5516 0.7231 -0.1476 -0.0651 0.0653  133 HIS A N   
962  C  CA  . HIS A 157 ? 0.4650 0.5391 0.7002 -0.1456 -0.0646 0.0734  133 HIS A CA  
963  C  C   . HIS A 157 ? 0.4844 0.5653 0.7103 -0.1445 -0.0717 0.0672  133 HIS A C   
964  O  O   . HIS A 157 ? 0.4405 0.5123 0.6472 -0.1399 -0.0726 0.0593  133 HIS A O   
965  C  CB  . HIS A 157 ? 0.4639 0.5449 0.6962 -0.1353 -0.0542 0.0821  133 HIS A CB  
966  C  CG  . HIS A 157 ? 0.5096 0.5854 0.7491 -0.1350 -0.0465 0.0894  133 HIS A CG  
967  N  ND1 . HIS A 157 ? 0.5674 0.6511 0.8285 -0.1412 -0.0452 0.0986  133 HIS A ND1 
968  C  CD2 . HIS A 157 ? 0.5380 0.6026 0.7665 -0.1292 -0.0398 0.0895  133 HIS A CD2 
969  C  CE1 . HIS A 157 ? 0.5948 0.6719 0.8575 -0.1390 -0.0378 0.1044  133 HIS A CE1 
970  N  NE2 . HIS A 157 ? 0.6089 0.6746 0.8519 -0.1317 -0.0345 0.0990  133 HIS A NE2 
971  N  N   . GLN A 158 ? 0.4678 0.5654 0.7082 -0.1487 -0.0766 0.0715  134 GLN A N   
972  C  CA  . GLN A 158 ? 0.4494 0.5556 0.6829 -0.1477 -0.0836 0.0672  134 GLN A CA  
973  C  C   . GLN A 158 ? 0.4071 0.5159 0.6260 -0.1360 -0.0779 0.0684  134 GLN A C   
974  O  O   . GLN A 158 ? 0.4171 0.5236 0.6215 -0.1333 -0.0820 0.0620  134 GLN A O   
975  C  CB  . GLN A 158 ? 0.4406 0.5667 0.6945 -0.1533 -0.0889 0.0738  134 GLN A CB  
976  C  CG  . GLN A 158 ? 0.4699 0.6061 0.7186 -0.1534 -0.0974 0.0699  134 GLN A CG  
977  C  CD  . GLN A 158 ? 0.5023 0.6269 0.7391 -0.1599 -0.1069 0.0575  134 GLN A CD  
978  O  OE1 . GLN A 158 ? 0.5283 0.6439 0.7710 -0.1688 -0.1106 0.0528  134 GLN A OE1 
979  N  NE2 . GLN A 158 ? 0.5006 0.6255 0.7208 -0.1555 -0.1105 0.0521  134 GLN A NE2 
980  N  N   . TRP A 159 ? 0.4065 0.5201 0.6290 -0.1289 -0.0683 0.0766  135 TRP A N   
981  C  CA  . TRP A 159 ? 0.3965 0.5124 0.6064 -0.1180 -0.0629 0.0773  135 TRP A CA  
982  C  C   . TRP A 159 ? 0.4258 0.5243 0.6139 -0.1141 -0.0621 0.0682  135 TRP A C   
983  O  O   . TRP A 159 ? 0.3907 0.4893 0.5665 -0.1075 -0.0615 0.0655  135 TRP A O   
984  C  CB  . TRP A 159 ? 0.3486 0.4722 0.5657 -0.1115 -0.0527 0.0868  135 TRP A CB  
985  C  CG  . TRP A 159 ? 0.4162 0.5276 0.6280 -0.1096 -0.0456 0.0873  135 TRP A CG  
986  C  CD1 . TRP A 159 ? 0.4236 0.5335 0.6477 -0.1147 -0.0430 0.0927  135 TRP A CD1 
987  C  CD2 . TRP A 159 ? 0.3903 0.4900 0.5838 -0.1020 -0.0404 0.0831  135 TRP A CD2 
988  N  NE1 . TRP A 159 ? 0.4355 0.5338 0.6497 -0.1104 -0.0365 0.0923  135 TRP A NE1 
989  C  CE2 . TRP A 159 ? 0.4261 0.5182 0.6215 -0.1027 -0.0349 0.0862  135 TRP A CE2 
990  C  CE3 . TRP A 159 ? 0.4085 0.5037 0.5852 -0.0949 -0.0398 0.0773  135 TRP A CE3 
991  C  CZ2 . TRP A 159 ? 0.4304 0.5116 0.6111 -0.0964 -0.0294 0.0836  135 TRP A CZ2 
992  C  CZ3 . TRP A 159 ? 0.3933 0.4773 0.5560 -0.0891 -0.0343 0.0744  135 TRP A CZ3 
993  C  CH2 . TRP A 159 ? 0.4106 0.4881 0.5752 -0.0898 -0.0294 0.0774  135 TRP A CH2 
994  N  N   . GLU A 160 ? 0.4149 0.4982 0.5990 -0.1182 -0.0619 0.0637  136 GLU A N   
995  C  CA  . GLU A 160 ? 0.4131 0.4803 0.5777 -0.1149 -0.0615 0.0550  136 GLU A CA  
996  C  C   . GLU A 160 ? 0.4185 0.4835 0.5731 -0.1177 -0.0700 0.0464  136 GLU A C   
997  O  O   . GLU A 160 ? 0.4123 0.4717 0.5507 -0.1121 -0.0693 0.0416  136 GLU A O   
998  C  CB  . GLU A 160 ? 0.4344 0.4865 0.5990 -0.1188 -0.0595 0.0526  136 GLU A CB  
999  C  CG  . GLU A 160 ? 0.4389 0.4925 0.6111 -0.1153 -0.0506 0.0614  136 GLU A CG  
1000 C  CD  . GLU A 160 ? 0.4547 0.4935 0.6283 -0.1191 -0.0489 0.0601  136 GLU A CD  
1001 O  OE1 . GLU A 160 ? 0.4513 0.4876 0.6371 -0.1280 -0.0534 0.0596  136 GLU A OE1 
1002 O  OE2 . GLU A 160 ? 0.4570 0.4867 0.6201 -0.1132 -0.0432 0.0595  136 GLU A OE2 
1003 N  N   . ARG A 161 ? 0.3946 0.4645 0.5587 -0.1264 -0.0781 0.0447  137 ARG A N   
1004 C  CA  . ARG A 161 ? 0.4303 0.4995 0.5846 -0.1294 -0.0868 0.0366  137 ARG A CA  
1005 C  C   . ARG A 161 ? 0.3961 0.4784 0.5465 -0.1233 -0.0878 0.0398  137 ARG A C   
1006 O  O   . ARG A 161 ? 0.4353 0.5134 0.5700 -0.1199 -0.0898 0.0344  137 ARG A O   
1007 C  CB  . ARG A 161 ? 0.4842 0.5574 0.6510 -0.1405 -0.0957 0.0342  137 ARG A CB  
1008 C  CG  . ARG A 161 ? 0.5033 0.5615 0.6741 -0.1472 -0.0956 0.0298  137 ARG A CG  
1009 C  CD  . ARG A 161 ? 0.5793 0.6443 0.7692 -0.1581 -0.1025 0.0308  137 ARG A CD  
1010 N  NE  . ARG A 161 ? 0.6071 0.6589 0.8054 -0.1636 -0.1002 0.0297  137 ARG A NE  
1011 C  CZ  . ARG A 161 ? 0.5880 0.6450 0.8076 -0.1708 -0.1008 0.0358  137 ARG A CZ  
1012 N  NH1 . ARG A 161 ? 0.6229 0.6990 0.8584 -0.1736 -0.1038 0.0433  137 ARG A NH1 
1013 N  NH2 . ARG A 161 ? 0.6117 0.6547 0.8378 -0.1750 -0.0981 0.0351  137 ARG A NH2 
1014 N  N   . ASN A 162 ? 0.4203 0.5187 0.5856 -0.1218 -0.0861 0.0492  138 ASN A N   
1015 C  CA  . ASN A 162 ? 0.4249 0.5357 0.5884 -0.1155 -0.0865 0.0530  138 ASN A CA  
1016 C  C   . ASN A 162 ? 0.4373 0.5404 0.5862 -0.1055 -0.0790 0.0522  138 ASN A C   
1017 O  O   . ASN A 162 ? 0.4376 0.5421 0.5765 -0.1010 -0.0807 0.0505  138 ASN A O   
1018 C  CB  . ASN A 162 ? 0.3906 0.5194 0.5739 -0.1150 -0.0847 0.0635  138 ASN A CB  
1019 C  CG  . ASN A 162 ? 0.4770 0.6151 0.6771 -0.1253 -0.0923 0.0650  138 ASN A CG  
1020 O  OD1 . ASN A 162 ? 0.4807 0.6164 0.6768 -0.1321 -0.1013 0.0583  138 ASN A OD1 
1021 N  ND2 . ASN A 162 ? 0.3758 0.5249 0.5947 -0.1265 -0.0888 0.0739  138 ASN A ND2 
1022 N  N   . TYR A 163 ? 0.4255 0.5208 0.5735 -0.1021 -0.0709 0.0537  139 TYR A N   
1023 C  CA  . TYR A 163 ? 0.4159 0.5049 0.5517 -0.0929 -0.0637 0.0530  139 TYR A CA  
1024 C  C   . TYR A 163 ? 0.4446 0.5198 0.5618 -0.0920 -0.0659 0.0442  139 TYR A C   
1025 O  O   . TYR A 163 ? 0.4317 0.5073 0.5395 -0.0865 -0.0656 0.0429  139 TYR A O   
1026 C  CB  . TYR A 163 ? 0.4149 0.4997 0.5544 -0.0905 -0.0555 0.0566  139 TYR A CB  
1027 C  CG  . TYR A 163 ? 0.4356 0.5167 0.5655 -0.0811 -0.0476 0.0570  139 TYR A CG  
1028 C  CD1 . TYR A 163 ? 0.4521 0.5414 0.5813 -0.0742 -0.0454 0.0596  139 TYR A CD1 
1029 C  CD2 . TYR A 163 ? 0.4345 0.5041 0.5571 -0.0792 -0.0424 0.0549  139 TYR A CD2 
1030 C  CE1 . TYR A 163 ? 0.4418 0.5273 0.5627 -0.0660 -0.0384 0.0591  139 TYR A CE1 
1031 C  CE2 . TYR A 163 ? 0.4593 0.5262 0.5733 -0.0711 -0.0358 0.0549  139 TYR A CE2 
1032 C  CZ  . TYR A 163 ? 0.4762 0.5509 0.5894 -0.0647 -0.0339 0.0565  139 TYR A CZ  
1033 O  OH  . TYR A 163 ? 0.4759 0.5475 0.5808 -0.0570 -0.0277 0.0556  139 TYR A OH  
1034 N  N   . LEU A 164 ? 0.4554 0.5182 0.5678 -0.0972 -0.0677 0.0382  140 LEU A N   
1035 C  CA  . LEU A 164 ? 0.4915 0.5411 0.5865 -0.0960 -0.0687 0.0298  140 LEU A CA  
1036 C  C   . LEU A 164 ? 0.5143 0.5672 0.6025 -0.0986 -0.0767 0.0253  140 LEU A C   
1037 O  O   . LEU A 164 ? 0.5769 0.6230 0.6504 -0.0953 -0.0768 0.0203  140 LEU A O   
1038 C  CB  . LEU A 164 ? 0.5230 0.5584 0.6158 -0.1004 -0.0682 0.0248  140 LEU A CB  
1039 C  CG  . LEU A 164 ? 0.4917 0.5233 0.5906 -0.0980 -0.0605 0.0296  140 LEU A CG  
1040 C  CD1 . LEU A 164 ? 0.5152 0.5322 0.6122 -0.1023 -0.0603 0.0248  140 LEU A CD1 
1041 C  CD2 . LEU A 164 ? 0.5301 0.5608 0.6204 -0.0887 -0.0534 0.0315  140 LEU A CD2 
1042 N  N   . GLY A 165 ? 0.4736 0.5377 0.5723 -0.1045 -0.0835 0.0273  141 GLY A N   
1043 C  CA  . GLY A 165 ? 0.4781 0.5477 0.5704 -0.1068 -0.0914 0.0239  141 GLY A CA  
1044 C  C   . GLY A 165 ? 0.4854 0.5665 0.5768 -0.1003 -0.0911 0.0295  141 GLY A C   
1045 O  O   . GLY A 165 ? 0.5189 0.6044 0.6028 -0.1009 -0.0970 0.0273  141 GLY A O   
1046 N  N   . ASN A 166 ? 0.4358 0.5216 0.5342 -0.0940 -0.0842 0.0365  142 ASN A N   
1047 C  CA  . ASN A 166 ? 0.4420 0.5393 0.5432 -0.0879 -0.0835 0.0427  142 ASN A CA  
1048 C  C   . ASN A 166 ? 0.4460 0.5355 0.5311 -0.0818 -0.0813 0.0394  142 ASN A C   
1049 O  O   . ASN A 166 ? 0.4108 0.4906 0.4896 -0.0767 -0.0743 0.0380  142 ASN A O   
1050 C  CB  . ASN A 166 ? 0.3933 0.4974 0.5073 -0.0830 -0.0763 0.0503  142 ASN A CB  
1051 C  CG  . ASN A 166 ? 0.3959 0.5122 0.5155 -0.0767 -0.0756 0.0569  142 ASN A CG  
1052 O  OD1 . ASN A 166 ? 0.3824 0.5011 0.4953 -0.0752 -0.0796 0.0563  142 ASN A OD1 
1053 N  ND2 . ASN A 166 ? 0.3325 0.4569 0.4647 -0.0727 -0.0699 0.0634  142 ASN A ND2 
1054 N  N   . LYS A 167 ? 0.4605 0.5550 0.5394 -0.0823 -0.0874 0.0387  143 LYS A N   
1055 C  CA  . LYS A 167 ? 0.4407 0.5293 0.5054 -0.0769 -0.0858 0.0367  143 LYS A CA  
1056 C  C   . LYS A 167 ? 0.4229 0.5187 0.4925 -0.0691 -0.0818 0.0441  143 LYS A C   
1057 O  O   . LYS A 167 ? 0.3845 0.4766 0.4444 -0.0646 -0.0806 0.0437  143 LYS A O   
1058 C  CB  . LYS A 167 ? 0.4983 0.5895 0.5530 -0.0809 -0.0939 0.0329  143 LYS A CB  
1059 C  CG  . LYS A 167 ? 0.5560 0.6383 0.6034 -0.0881 -0.0978 0.0239  143 LYS A CG  
1060 C  CD  . LYS A 167 ? 0.5939 0.6813 0.6319 -0.0920 -0.1064 0.0202  143 LYS A CD  
1061 C  CE  . LYS A 167 ? 0.7181 0.7918 0.7405 -0.0949 -0.1073 0.0098  143 LYS A CE  
1062 N  NZ  . LYS A 167 ? 0.7290 0.8086 0.7414 -0.0988 -0.1158 0.0055  143 LYS A NZ  
1063 N  N   . ASP A 168 ? 0.3715 0.4770 0.4563 -0.0672 -0.0795 0.0507  144 ASP A N   
1064 C  CA  . ASP A 168 ? 0.3900 0.5035 0.4815 -0.0599 -0.0765 0.0577  144 ASP A CA  
1065 C  C   . ASP A 168 ? 0.3700 0.4810 0.4682 -0.0542 -0.0676 0.0599  144 ASP A C   
1066 O  O   . ASP A 168 ? 0.3682 0.4885 0.4776 -0.0493 -0.0649 0.0663  144 ASP A O   
1067 C  CB  . ASP A 168 ? 0.3589 0.4898 0.4633 -0.0619 -0.0826 0.0645  144 ASP A CB  
1068 C  CG  . ASP A 168 ? 0.4123 0.5475 0.5088 -0.0662 -0.0916 0.0629  144 ASP A CG  
1069 O  OD1 . ASP A 168 ? 0.4536 0.5841 0.5383 -0.0628 -0.0916 0.0618  144 ASP A OD1 
1070 O  OD2 . ASP A 168 ? 0.4916 0.6352 0.5937 -0.0732 -0.0988 0.0626  144 ASP A OD2 
1071 N  N   . ILE A 169 ? 0.3493 0.4482 0.4409 -0.0545 -0.0628 0.0547  145 ILE A N   
1072 C  CA  . ILE A 169 ? 0.3631 0.4601 0.4595 -0.0493 -0.0546 0.0562  145 ILE A CA  
1073 C  C   . ILE A 169 ? 0.3511 0.4432 0.4420 -0.0414 -0.0498 0.0560  145 ILE A C   
1074 O  O   . ILE A 169 ? 0.3517 0.4338 0.4301 -0.0408 -0.0501 0.0515  145 ILE A O   
1075 C  CB  . ILE A 169 ? 0.3468 0.4334 0.4379 -0.0522 -0.0516 0.0514  145 ILE A CB  
1076 C  CG1 . ILE A 169 ? 0.3645 0.4558 0.4637 -0.0601 -0.0559 0.0522  145 ILE A CG1 
1077 C  CG2 . ILE A 169 ? 0.3873 0.4723 0.4810 -0.0461 -0.0431 0.0527  145 ILE A CG2 
1078 C  CD1 . ILE A 169 ? 0.4230 0.5037 0.5180 -0.0634 -0.0534 0.0481  145 ILE A CD1 
1079 N  N   . ILE A 170 ? 0.3016 0.4004 0.4022 -0.0355 -0.0452 0.0607  146 ILE A N   
1080 C  CA  . ILE A 170 ? 0.3600 0.4539 0.4578 -0.0278 -0.0399 0.0603  146 ILE A CA  
1081 C  C   . ILE A 170 ? 0.3697 0.4616 0.4702 -0.0237 -0.0323 0.0591  146 ILE A C   
1082 O  O   . ILE A 170 ? 0.3555 0.4574 0.4676 -0.0221 -0.0298 0.0636  146 ILE A O   
1083 C  CB  . ILE A 170 ? 0.3418 0.4453 0.4489 -0.0234 -0.0410 0.0666  146 ILE A CB  
1084 C  CG1 . ILE A 170 ? 0.3437 0.4495 0.4463 -0.0269 -0.0486 0.0681  146 ILE A CG1 
1085 C  CG2 . ILE A 170 ? 0.3964 0.4938 0.5026 -0.0153 -0.0347 0.0658  146 ILE A CG2 
1086 C  CD1 . ILE A 170 ? 0.3634 0.4819 0.4772 -0.0239 -0.0513 0.0760  146 ILE A CD1 
1087 N  N   . PHE A 171 ? 0.3577 0.4378 0.4475 -0.0219 -0.0286 0.0533  147 PHE A N   
1088 C  CA  . PHE A 171 ? 0.3693 0.4471 0.4591 -0.0176 -0.0215 0.0513  147 PHE A CA  
1089 C  C   . PHE A 171 ? 0.3508 0.4288 0.4438 -0.0099 -0.0173 0.0518  147 PHE A C   
1090 O  O   . PHE A 171 ? 0.3846 0.4535 0.4702 -0.0074 -0.0165 0.0480  147 PHE A O   
1091 C  CB  . PHE A 171 ? 0.3778 0.4435 0.4549 -0.0194 -0.0203 0.0450  147 PHE A CB  
1092 C  CG  . PHE A 171 ? 0.4169 0.4812 0.4927 -0.0160 -0.0139 0.0431  147 PHE A CG  
1093 C  CD1 . PHE A 171 ? 0.4090 0.4833 0.4945 -0.0136 -0.0101 0.0473  147 PHE A CD1 
1094 C  CD2 . PHE A 171 ? 0.4296 0.4836 0.4945 -0.0149 -0.0118 0.0374  147 PHE A CD2 
1095 C  CE1 . PHE A 171 ? 0.4146 0.4885 0.4976 -0.0102 -0.0042 0.0457  147 PHE A CE1 
1096 C  CE2 . PHE A 171 ? 0.4241 0.4779 0.4870 -0.0117 -0.0064 0.0358  147 PHE A CE2 
1097 C  CZ  . PHE A 171 ? 0.4027 0.4664 0.4740 -0.0093 -0.0026 0.0398  147 PHE A CZ  
1098 N  N   . ARG A 172 ? 0.3573 0.4458 0.4624 -0.0060 -0.0144 0.0565  148 ARG A N   
1099 C  CA  . ARG A 172 ? 0.3710 0.4608 0.4818 0.0013  -0.0111 0.0578  148 ARG A CA  
1100 C  C   . ARG A 172 ? 0.3592 0.4429 0.4659 0.0072  -0.0040 0.0525  148 ARG A C   
1101 O  O   . ARG A 172 ? 0.3454 0.4335 0.4537 0.0084  0.0003  0.0521  148 ARG A O   
1102 C  CB  . ARG A 172 ? 0.3578 0.4621 0.4840 0.0034  -0.0110 0.0653  148 ARG A CB  
1103 C  CG  . ARG A 172 ? 0.3962 0.5020 0.5300 0.0118  -0.0067 0.0669  148 ARG A CG  
1104 C  CD  . ARG A 172 ? 0.3911 0.5120 0.5411 0.0147  -0.0056 0.0744  148 ARG A CD  
1105 N  NE  . ARG A 172 ? 0.3798 0.5007 0.5365 0.0238  0.0007  0.0743  148 ARG A NE  
1106 C  CZ  . ARG A 172 ? 0.4298 0.5562 0.5976 0.0284  0.0003  0.0798  148 ARG A CZ  
1107 N  NH1 . ARG A 172 ? 0.4475 0.5824 0.6218 0.0249  -0.0062 0.0868  148 ARG A NH1 
1108 N  NH2 . ARG A 172 ? 0.4021 0.5256 0.5748 0.0368  0.0067  0.0781  148 ARG A NH2 
1109 N  N   . ASN A 173 ? 0.3470 0.4213 0.4490 0.0108  -0.0027 0.0484  149 ASN A N   
1110 C  CA  . ASN A 173 ? 0.3480 0.4162 0.4468 0.0166  0.0034  0.0425  149 ASN A CA  
1111 C  C   . ASN A 173 ? 0.3394 0.4017 0.4413 0.0211  0.0039  0.0419  149 ASN A C   
1112 O  O   . ASN A 173 ? 0.3648 0.4163 0.4593 0.0209  0.0034  0.0371  149 ASN A O   
1113 C  CB  . ASN A 173 ? 0.3661 0.4251 0.4518 0.0141  0.0039  0.0358  149 ASN A CB  
1114 C  CG  . ASN A 173 ? 0.3888 0.4526 0.4719 0.0096  0.0035  0.0371  149 ASN A CG  
1115 O  OD1 . ASN A 173 ? 0.3548 0.4244 0.4402 0.0122  0.0080  0.0373  149 ASN A OD1 
1116 N  ND2 . ASN A 173 ? 0.3243 0.3852 0.4025 0.0030  -0.0017 0.0378  149 ASN A ND2 
1117 N  N   . THR A 174 ? 0.3250 0.3946 0.4391 0.0254  0.0050  0.0473  150 THR A N   
1118 C  CA  . THR A 174 ? 0.3695 0.4337 0.4886 0.0301  0.0058  0.0477  150 THR A CA  
1119 C  C   . THR A 174 ? 0.3626 0.4182 0.4795 0.0358  0.0119  0.0398  150 THR A C   
1120 O  O   . THR A 174 ? 0.3337 0.3902 0.4463 0.0371  0.0158  0.0349  150 THR A O   
1121 C  CB  . THR A 174 ? 0.3682 0.4430 0.5021 0.0339  0.0058  0.0559  150 THR A CB  
1122 O  OG1 . THR A 174 ? 0.3337 0.4156 0.4751 0.0394  0.0117  0.0555  150 THR A OG1 
1123 C  CG2 . THR A 174 ? 0.3433 0.4284 0.4797 0.0279  -0.0007 0.0632  150 THR A CG2 
1124 N  N   . PHE A 175 ? 0.3465 0.3936 0.4663 0.0390  0.0126  0.0387  151 PHE A N   
1125 C  CA  . PHE A 175 ? 0.3931 0.4316 0.5124 0.0444  0.0179  0.0307  151 PHE A CA  
1126 C  C   . PHE A 175 ? 0.3810 0.4270 0.5080 0.0510  0.0238  0.0299  151 PHE A C   
1127 O  O   . PHE A 175 ? 0.3750 0.4183 0.4971 0.0540  0.0283  0.0221  151 PHE A O   
1128 C  CB  . PHE A 175 ? 0.3903 0.4190 0.5147 0.0469  0.0177  0.0310  151 PHE A CB  
1129 C  CG  . PHE A 175 ? 0.4359 0.4563 0.5518 0.0411  0.0133  0.0304  151 PHE A CG  
1130 C  CD1 . PHE A 175 ? 0.4252 0.4369 0.5307 0.0388  0.0138  0.0219  151 PHE A CD1 
1131 C  CD2 . PHE A 175 ? 0.4289 0.4512 0.5472 0.0383  0.0087  0.0384  151 PHE A CD2 
1132 C  CE1 . PHE A 175 ? 0.4439 0.4487 0.5424 0.0339  0.0103  0.0216  151 PHE A CE1 
1133 C  CE2 . PHE A 175 ? 0.4273 0.4427 0.5375 0.0335  0.0053  0.0379  151 PHE A CE2 
1134 C  CZ  . PHE A 175 ? 0.4239 0.4304 0.5246 0.0313  0.0062  0.0296  151 PHE A CZ  
1135 N  N   . GLY A 176 ? 0.3441 0.4005 0.4832 0.0535  0.0239  0.0381  152 GLY A N   
1136 C  CA  . GLY A 176 ? 0.3876 0.4528 0.5348 0.0599  0.0298  0.0383  152 GLY A CA  
1137 C  C   . GLY A 176 ? 0.3851 0.4584 0.5258 0.0575  0.0314  0.0369  152 GLY A C   
1138 O  O   . GLY A 176 ? 0.3764 0.4519 0.5161 0.0625  0.0374  0.0319  152 GLY A O   
1139 N  N   . ASP A 177 ? 0.3535 0.4316 0.4898 0.0500  0.0261  0.0413  153 ASP A N   
1140 C  CA  . ASP A 177 ? 0.3633 0.4479 0.4937 0.0471  0.0274  0.0405  153 ASP A CA  
1141 C  C   . ASP A 177 ? 0.4287 0.5047 0.5461 0.0480  0.0306  0.0308  153 ASP A C   
1142 O  O   . ASP A 177 ? 0.3958 0.4769 0.5113 0.0516  0.0359  0.0281  153 ASP A O   
1143 C  CB  . ASP A 177 ? 0.3721 0.4596 0.4991 0.0382  0.0206  0.0454  153 ASP A CB  
1144 C  CG  . ASP A 177 ? 0.3964 0.4948 0.5357 0.0365  0.0169  0.0549  153 ASP A CG  
1145 O  OD1 . ASP A 177 ? 0.4044 0.5125 0.5559 0.0419  0.0205  0.0591  153 ASP A OD1 
1146 O  OD2 . ASP A 177 ? 0.4204 0.5183 0.5572 0.0299  0.0102  0.0579  153 ASP A OD2 
1147 N  N   . VAL A 178 ? 0.3669 0.4306 0.4754 0.0449  0.0273  0.0259  154 VAL A N   
1148 C  CA  . VAL A 178 ? 0.3994 0.4556 0.4955 0.0448  0.0290  0.0170  154 VAL A CA  
1149 C  C   . VAL A 178 ? 0.4344 0.4889 0.5316 0.0526  0.0354  0.0100  154 VAL A C   
1150 O  O   . VAL A 178 ? 0.4294 0.4861 0.5191 0.0545  0.0389  0.0048  154 VAL A O   
1151 C  CB  . VAL A 178 ? 0.4073 0.4513 0.4960 0.0402  0.0243  0.0137  154 VAL A CB  
1152 C  CG1 . VAL A 178 ? 0.3525 0.3890 0.4300 0.0407  0.0260  0.0043  154 VAL A CG1 
1153 C  CG2 . VAL A 178 ? 0.3675 0.4134 0.4528 0.0326  0.0185  0.0192  154 VAL A CG2 
1154 N  N   . GLU A 179 ? 0.3972 0.4479 0.5037 0.0574  0.0369  0.0097  155 GLU A N   
1155 C  CA  . GLU A 179 ? 0.4808 0.5291 0.5891 0.0652  0.0432  0.0023  155 GLU A CA  
1156 C  C   . GLU A 179 ? 0.4666 0.5281 0.5779 0.0699  0.0488  0.0040  155 GLU A C   
1157 O  O   . GLU A 179 ? 0.4595 0.5214 0.5650 0.0746  0.0539  -0.0036 155 GLU A O   
1158 C  CB  . GLU A 179 ? 0.4629 0.5048 0.5831 0.0696  0.0439  0.0031  155 GLU A CB  
1159 C  CG  . GLU A 179 ? 0.5681 0.6069 0.6922 0.0782  0.0506  -0.0047 155 GLU A CG  
1160 C  CD  . GLU A 179 ? 0.6660 0.6957 0.8018 0.0821  0.0511  -0.0043 155 GLU A CD  
1161 O  OE1 . GLU A 179 ? 0.6980 0.7220 0.8364 0.0777  0.0460  0.0006  155 GLU A OE1 
1162 O  OE2 . GLU A 179 ? 0.7463 0.7748 0.8891 0.0899  0.0569  -0.0087 155 GLU A OE2 
1163 N  N   . HIS A 180 ? 0.4149 0.4881 0.5353 0.0687  0.0481  0.0141  156 HIS A N   
1164 C  CA  . HIS A 180 ? 0.4500 0.5370 0.5746 0.0729  0.0537  0.0172  156 HIS A CA  
1165 C  C   . HIS A 180 ? 0.4631 0.5543 0.5753 0.0700  0.0548  0.0148  156 HIS A C   
1166 O  O   . HIS A 180 ? 0.4578 0.5554 0.5672 0.0753  0.0611  0.0116  156 HIS A O   
1167 C  CB  . HIS A 180 ? 0.4554 0.5544 0.5934 0.0711  0.0516  0.0290  156 HIS A CB  
1168 C  CG  . HIS A 180 ? 0.4931 0.6077 0.6368 0.0741  0.0570  0.0338  156 HIS A CG  
1169 N  ND1 . HIS A 180 ? 0.5531 0.6777 0.6969 0.0681  0.0548  0.0407  156 HIS A ND1 
1170 C  CD2 . HIS A 180 ? 0.5045 0.6268 0.6544 0.0826  0.0647  0.0327  156 HIS A CD2 
1171 C  CE1 . HIS A 180 ? 0.5079 0.6459 0.6582 0.0725  0.0609  0.0445  156 HIS A CE1 
1172 N  NE2 . HIS A 180 ? 0.5375 0.6748 0.6912 0.0815  0.0672  0.0396  156 HIS A NE2 
1173 N  N   . VAL A 181 ? 0.4272 0.5149 0.5319 0.0620  0.0490  0.0167  157 VAL A N   
1174 C  CA  . VAL A 181 ? 0.4598 0.5511 0.5536 0.0592  0.0498  0.0155  157 VAL A CA  
1175 C  C   . VAL A 181 ? 0.4717 0.5562 0.5533 0.0629  0.0528  0.0046  157 VAL A C   
1176 O  O   . VAL A 181 ? 0.4695 0.5610 0.5448 0.0658  0.0574  0.0026  157 VAL A O   
1177 C  CB  . VAL A 181 ? 0.4440 0.5318 0.5334 0.0500  0.0429  0.0195  157 VAL A CB  
1178 C  CG1 . VAL A 181 ? 0.4300 0.5210 0.5091 0.0475  0.0440  0.0190  157 VAL A CG1 
1179 C  CG2 . VAL A 181 ? 0.4631 0.5584 0.5642 0.0460  0.0395  0.0295  157 VAL A CG2 
1180 N  N   . MET A 182 ? 0.4546 0.5261 0.5330 0.0628  0.0502  -0.0025 158 MET A N   
1181 C  CA  . MET A 182 ? 0.4862 0.5511 0.5542 0.0660  0.0523  -0.0137 158 MET A CA  
1182 C  C   . MET A 182 ? 0.4942 0.5655 0.5638 0.0747  0.0598  -0.0182 158 MET A C   
1183 O  O   . MET A 182 ? 0.5145 0.5897 0.5738 0.0774  0.0631  -0.0238 158 MET A O   
1184 C  CB  . MET A 182 ? 0.4718 0.5221 0.5402 0.0649  0.0488  -0.0196 158 MET A CB  
1185 C  CG  . MET A 182 ? 0.4679 0.5109 0.5310 0.0569  0.0420  -0.0177 158 MET A CG  
1186 S  SD  . MET A 182 ? 0.5204 0.5481 0.5877 0.0559  0.0386  -0.0220 158 MET A SD  
1187 C  CE  . MET A 182 ? 0.4139 0.4362 0.4726 0.0470  0.0318  -0.0198 158 MET A CE  
1188 N  N   . THR A 183 ? 0.4659 0.5389 0.5482 0.0796  0.0627  -0.0158 159 THR A N   
1189 C  CA  . THR A 183 ? 0.5006 0.5792 0.5854 0.0886  0.0704  -0.0205 159 THR A CA  
1190 C  C   . THR A 183 ? 0.5172 0.6119 0.5999 0.0905  0.0752  -0.0153 159 THR A C   
1191 O  O   . THR A 183 ? 0.5464 0.6456 0.6203 0.0955  0.0804  -0.0218 159 THR A O   
1192 C  CB  . THR A 183 ? 0.4686 0.5460 0.5695 0.0933  0.0723  -0.0173 159 THR A CB  
1193 O  OG1 . THR A 183 ? 0.5719 0.6339 0.6746 0.0925  0.0688  -0.0228 159 THR A OG1 
1194 C  CG2 . THR A 183 ? 0.5327 0.6173 0.6376 0.1032  0.0809  -0.0212 159 THR A CG2 
1195 N  N   . THR A 184 ? 0.4738 0.5778 0.5646 0.0865  0.0735  -0.0034 160 THR A N   
1196 C  CA  . THR A 184 ? 0.5055 0.6256 0.5973 0.0881  0.0785  0.0032  160 THR A CA  
1197 C  C   . THR A 184 ? 0.5128 0.6348 0.5891 0.0856  0.0786  0.0005  160 THR A C   
1198 O  O   . THR A 184 ? 0.5387 0.6686 0.6083 0.0913  0.0849  -0.0030 160 THR A O   
1199 C  CB  . THR A 184 ? 0.4973 0.6257 0.6018 0.0828  0.0753  0.0162  160 THR A CB  
1200 O  OG1 . THR A 184 ? 0.5031 0.6312 0.6222 0.0858  0.0752  0.0193  160 THR A OG1 
1201 C  CG2 . THR A 184 ? 0.5080 0.6534 0.6155 0.0841  0.0806  0.0238  160 THR A CG2 
1202 N  N   . LEU A 185 ? 0.5046 0.6201 0.5750 0.0775  0.0719  0.0023  161 LEU A N   
1203 C  CA  . LEU A 185 ? 0.4939 0.6120 0.5511 0.0749  0.0717  0.0015  161 LEU A CA  
1204 C  C   . LEU A 185 ? 0.4975 0.6094 0.5409 0.0790  0.0731  -0.0109 161 LEU A C   
1205 O  O   . LEU A 185 ? 0.5307 0.6492 0.5633 0.0807  0.0760  -0.0124 161 LEU A O   
1206 C  CB  . LEU A 185 ? 0.4619 0.5738 0.5173 0.0655  0.0643  0.0063  161 LEU A CB  
1207 C  CG  . LEU A 185 ? 0.4752 0.5926 0.5433 0.0602  0.0616  0.0178  161 LEU A CG  
1208 C  CD1 . LEU A 185 ? 0.4281 0.5394 0.4918 0.0515  0.0550  0.0210  161 LEU A CD1 
1209 C  CD2 . LEU A 185 ? 0.4900 0.6237 0.5651 0.0630  0.0676  0.0259  161 LEU A CD2 
1210 N  N   . GLY A 186 ? 0.5086 0.6082 0.5525 0.0804  0.0710  -0.0196 162 GLY A N   
1211 C  CA  . GLY A 186 ? 0.5173 0.6105 0.5490 0.0836  0.0716  -0.0322 162 GLY A CA  
1212 C  C   . GLY A 186 ? 0.5707 0.6731 0.5978 0.0923  0.0794  -0.0378 162 GLY A C   
1213 O  O   . GLY A 186 ? 0.6039 0.7068 0.6176 0.0945  0.0804  -0.0463 162 GLY A O   
1214 N  N   . ALA A 187 ? 0.5309 0.6414 0.5689 0.0976  0.0851  -0.0333 163 ALA A N   
1215 C  CA  . ALA A 187 ? 0.5826 0.7029 0.6166 0.1066  0.0934  -0.0383 163 ALA A CA  
1216 C  C   . ALA A 187 ? 0.5857 0.7197 0.6086 0.1069  0.0965  -0.0342 163 ALA A C   
1217 O  O   . ALA A 187 ? 0.6445 0.7856 0.6580 0.1137  0.1023  -0.0408 163 ALA A O   
1218 C  CB  . ALA A 187 ? 0.5517 0.6791 0.6015 0.1120  0.0989  -0.0325 163 ALA A CB  
1219 N  N   . GLY A 188 ? 0.5624 0.7004 0.5862 0.0997  0.0928  -0.0234 164 GLY A N   
1220 C  CA  . GLY A 188 ? 0.5453 0.6960 0.5602 0.0996  0.0957  -0.0177 164 GLY A CA  
1221 C  C   . GLY A 188 ? 0.5411 0.6864 0.5404 0.0959  0.0909  -0.0229 164 GLY A C   
1222 O  O   . GLY A 188 ? 0.4918 0.6454 0.4847 0.0937  0.0913  -0.0161 164 GLY A O   
1223 N  N   . GLY A 189 ? 0.5516 0.6833 0.5458 0.0951  0.0863  -0.0343 165 GLY A N   
1224 C  CA  . GLY A 189 ? 0.4965 0.6231 0.4770 0.0917  0.0814  -0.0398 165 GLY A CA  
1225 C  C   . GLY A 189 ? 0.4992 0.6192 0.4818 0.0827  0.0743  -0.0326 165 GLY A C   
1226 O  O   . GLY A 189 ? 0.4538 0.5699 0.4261 0.0798  0.0700  -0.0363 165 GLY A O   
1227 N  N   . THR A 190 ? 0.4930 0.6120 0.4886 0.0784  0.0729  -0.0228 166 THR A N   
1228 C  CA  . THR A 190 ? 0.4526 0.5650 0.4501 0.0700  0.0664  -0.0165 166 THR A CA  
1229 C  C   . THR A 190 ? 0.4706 0.5676 0.4675 0.0666  0.0601  -0.0242 166 THR A C   
1230 O  O   . THR A 190 ? 0.4684 0.5586 0.4717 0.0687  0.0602  -0.0294 166 THR A O   
1231 C  CB  . THR A 190 ? 0.4489 0.5649 0.4605 0.0664  0.0663  -0.0048 166 THR A CB  
1232 O  OG1 . THR A 190 ? 0.4124 0.5436 0.4263 0.0695  0.0725  0.0030  166 THR A OG1 
1233 C  CG2 . THR A 190 ? 0.3926 0.5019 0.4053 0.0578  0.0598  0.0009  166 THR A CG2 
1234 N  N   . ARG A 191 ? 0.4064 0.4980 0.3962 0.0615  0.0551  -0.0244 167 ARG A N   
1235 C  CA  . ARG A 191 ? 0.4454 0.5234 0.4356 0.0571  0.0490  -0.0295 167 ARG A CA  
1236 C  C   . ARG A 191 ? 0.4405 0.5144 0.4369 0.0499  0.0446  -0.0205 167 ARG A C   
1237 O  O   . ARG A 191 ? 0.4265 0.5076 0.4251 0.0479  0.0457  -0.0114 167 ARG A O   
1238 C  CB  . ARG A 191 ? 0.4579 0.5328 0.4356 0.0570  0.0464  -0.0377 167 ARG A CB  
1239 C  CG  . ARG A 191 ? 0.5170 0.5945 0.4883 0.0637  0.0499  -0.0485 167 ARG A CG  
1240 C  CD  . ARG A 191 ? 0.5016 0.5756 0.4618 0.0631  0.0463  -0.0578 167 ARG A CD  
1241 N  NE  . ARG A 191 ? 0.5447 0.6055 0.5088 0.0580  0.0405  -0.0614 167 ARG A NE  
1242 C  CZ  . ARG A 191 ? 0.5253 0.5764 0.4949 0.0589  0.0397  -0.0692 167 ARG A CZ  
1243 N  NH1 . ARG A 191 ? 0.5815 0.6336 0.5537 0.0647  0.0441  -0.0750 167 ARG A NH1 
1244 N  NH2 . ARG A 191 ? 0.5677 0.6078 0.5407 0.0539  0.0345  -0.0711 167 ARG A NH2 
1245 N  N   . PHE A 192 ? 0.4068 0.4693 0.4067 0.0462  0.0399  -0.0231 168 PHE A N   
1246 C  CA  . PHE A 192 ? 0.4064 0.4649 0.4134 0.0403  0.0361  -0.0156 168 PHE A CA  
1247 C  C   . PHE A 192 ? 0.3963 0.4472 0.3974 0.0348  0.0310  -0.0160 168 PHE A C   
1248 O  O   . PHE A 192 ? 0.4171 0.4623 0.4118 0.0350  0.0292  -0.0233 168 PHE A O   
1249 C  CB  . PHE A 192 ? 0.4045 0.4571 0.4214 0.0405  0.0350  -0.0162 168 PHE A CB  
1250 C  CG  . PHE A 192 ? 0.4091 0.4691 0.4338 0.0461  0.0400  -0.0148 168 PHE A CG  
1251 C  CD1 . PHE A 192 ? 0.4121 0.4826 0.4430 0.0459  0.0424  -0.0059 168 PHE A CD1 
1252 C  CD2 . PHE A 192 ? 0.4175 0.4740 0.4441 0.0515  0.0425  -0.0222 168 PHE A CD2 
1253 C  CE1 . PHE A 192 ? 0.4194 0.4977 0.4582 0.0513  0.0474  -0.0042 168 PHE A CE1 
1254 C  CE2 . PHE A 192 ? 0.4310 0.4944 0.4653 0.0572  0.0476  -0.0210 168 PHE A CE2 
1255 C  CZ  . PHE A 192 ? 0.4598 0.5346 0.5002 0.0572  0.0501  -0.0117 168 PHE A CZ  
1256 N  N   . GLU A 193 ? 0.4222 0.4736 0.4263 0.0298  0.0288  -0.0082 169 GLU A N   
1257 C  CA  . GLU A 193 ? 0.3779 0.4208 0.3797 0.0242  0.0238  -0.0078 169 GLU A CA  
1258 C  C   . GLU A 193 ? 0.3886 0.4257 0.3983 0.0216  0.0210  -0.0061 169 GLU A C   
1259 O  O   . GLU A 193 ? 0.4118 0.4526 0.4286 0.0194  0.0207  0.0005  169 GLU A O   
1260 C  CB  . GLU A 193 ? 0.4191 0.4650 0.4191 0.0206  0.0232  -0.0009 169 GLU A CB  
1261 C  CG  . GLU A 193 ? 0.3921 0.4291 0.3896 0.0153  0.0185  -0.0007 169 GLU A CG  
1262 C  CD  . GLU A 193 ? 0.4803 0.5193 0.4769 0.0120  0.0182  0.0057  169 GLU A CD  
1263 O  OE1 . GLU A 193 ? 0.4668 0.5087 0.4704 0.0093  0.0182  0.0120  169 GLU A OE1 
1264 O  OE2 . GLU A 193 ? 0.5398 0.5777 0.5296 0.0121  0.0178  0.0046  169 GLU A OE2 
1265 N  N   . PHE A 194 ? 0.3819 0.4108 0.3911 0.0217  0.0190  -0.0117 170 PHE A N   
1266 C  CA  . PHE A 194 ? 0.3926 0.4166 0.4091 0.0199  0.0167  -0.0099 170 PHE A CA  
1267 C  C   . PHE A 194 ? 0.3826 0.4021 0.3976 0.0139  0.0123  -0.0061 170 PHE A C   
1268 O  O   . PHE A 194 ? 0.4139 0.4269 0.4232 0.0117  0.0101  -0.0093 170 PHE A O   
1269 C  CB  . PHE A 194 ? 0.3810 0.3976 0.3981 0.0222  0.0165  -0.0168 170 PHE A CB  
1270 C  CG  . PHE A 194 ? 0.3753 0.3949 0.3931 0.0283  0.0207  -0.0222 170 PHE A CG  
1271 C  CD1 . PHE A 194 ? 0.3680 0.3916 0.3942 0.0321  0.0236  -0.0202 170 PHE A CD1 
1272 C  CD2 . PHE A 194 ? 0.3912 0.4100 0.4012 0.0304  0.0216  -0.0298 170 PHE A CD2 
1273 C  CE1 . PHE A 194 ? 0.3848 0.4107 0.4114 0.0382  0.0279  -0.0259 170 PHE A CE1 
1274 C  CE2 . PHE A 194 ? 0.3675 0.3889 0.3772 0.0360  0.0254  -0.0359 170 PHE A CE2 
1275 C  CZ  . PHE A 194 ? 0.4049 0.4295 0.4229 0.0401  0.0288  -0.0342 170 PHE A CZ  
1276 N  N   . GLU A 195 ? 0.3909 0.4143 0.4114 0.0112  0.0111  0.0005  171 GLU A N   
1277 C  CA  . GLU A 195 ? 0.3686 0.3884 0.3877 0.0055  0.0071  0.0037  171 GLU A CA  
1278 C  C   . GLU A 195 ? 0.3598 0.3736 0.3810 0.0039  0.0040  0.0033  171 GLU A C   
1279 O  O   . GLU A 195 ? 0.3681 0.3850 0.3967 0.0050  0.0037  0.0063  171 GLU A O   
1280 C  CB  . GLU A 195 ? 0.3468 0.3735 0.3713 0.0027  0.0067  0.0104  171 GLU A CB  
1281 C  CG  . GLU A 195 ? 0.4281 0.4631 0.4535 0.0052  0.0108  0.0126  171 GLU A CG  
1282 C  CD  . GLU A 195 ? 0.4446 0.4777 0.4619 0.0046  0.0116  0.0112  171 GLU A CD  
1283 O  OE1 . GLU A 195 ? 0.4720 0.4971 0.4835 0.0020  0.0088  0.0084  171 GLU A OE1 
1284 O  OE2 . GLU A 195 ? 0.4458 0.4860 0.4627 0.0068  0.0151  0.0135  171 GLU A OE2 
1285 N  N   . CYS A 196 ? 0.3524 0.3587 0.3677 0.0017  0.0018  0.0003  172 CYS A N   
1286 C  CA  . CYS A 196 ? 0.3623 0.3630 0.3786 0.0004  -0.0007 0.0001  172 CYS A CA  
1287 C  C   . CYS A 196 ? 0.3408 0.3385 0.3530 -0.0047 -0.0042 0.0021  172 CYS A C   
1288 O  O   . CYS A 196 ? 0.3603 0.3541 0.3660 -0.0063 -0.0046 -0.0003 172 CYS A O   
1289 C  CB  . CYS A 196 ? 0.3101 0.3047 0.3239 0.0026  0.0004  -0.0056 172 CYS A CB  
1290 S  SG  . CYS A 196 ? 0.4169 0.4138 0.4352 0.0087  0.0045  -0.0097 172 CYS A SG  
1291 N  N   . TYR A 197 ? 0.3118 0.3116 0.3276 -0.0068 -0.0069 0.0063  173 TYR A N   
1292 C  CA  . TYR A 197 ? 0.3268 0.3245 0.3386 -0.0117 -0.0105 0.0078  173 TYR A CA  
1293 C  C   . TYR A 197 ? 0.3380 0.3305 0.3464 -0.0126 -0.0124 0.0070  173 TYR A C   
1294 O  O   . TYR A 197 ? 0.3059 0.2963 0.3095 -0.0162 -0.0152 0.0074  173 TYR A O   
1295 C  CB  . TYR A 197 ? 0.3010 0.3057 0.3185 -0.0140 -0.0129 0.0127  173 TYR A CB  
1296 C  CG  . TYR A 197 ? 0.3206 0.3316 0.3427 -0.0136 -0.0109 0.0147  173 TYR A CG  
1297 C  CD1 . TYR A 197 ? 0.3165 0.3328 0.3443 -0.0091 -0.0073 0.0155  173 TYR A CD1 
1298 C  CD2 . TYR A 197 ? 0.3311 0.3426 0.3520 -0.0177 -0.0122 0.0158  173 TYR A CD2 
1299 C  CE1 . TYR A 197 ? 0.3386 0.3616 0.3704 -0.0084 -0.0049 0.0179  173 TYR A CE1 
1300 C  CE2 . TYR A 197 ? 0.3339 0.3515 0.3598 -0.0175 -0.0100 0.0186  173 TYR A CE2 
1301 C  CZ  . TYR A 197 ? 0.3661 0.3900 0.3972 -0.0128 -0.0062 0.0199  173 TYR A CZ  
1302 O  OH  . TYR A 197 ? 0.3520 0.3831 0.3880 -0.0123 -0.0035 0.0233  173 TYR A OH  
1303 N  N   . ASP A 198 ? 0.3150 0.3053 0.3259 -0.0094 -0.0108 0.0060  174 ASP A N   
1304 C  CA  . ASP A 198 ? 0.3373 0.3231 0.3461 -0.0100 -0.0120 0.0064  174 ASP A CA  
1305 C  C   . ASP A 198 ? 0.3474 0.3301 0.3607 -0.0063 -0.0094 0.0045  174 ASP A C   
1306 O  O   . ASP A 198 ? 0.3385 0.3228 0.3561 -0.0031 -0.0070 0.0027  174 ASP A O   
1307 C  CB  . ASP A 198 ? 0.3162 0.3059 0.3269 -0.0118 -0.0153 0.0116  174 ASP A CB  
1308 C  CG  . ASP A 198 ? 0.3556 0.3417 0.3603 -0.0138 -0.0170 0.0121  174 ASP A CG  
1309 O  OD1 . ASP A 198 ? 0.3880 0.3684 0.3883 -0.0138 -0.0154 0.0086  174 ASP A OD1 
1310 O  OD2 . ASP A 198 ? 0.3603 0.3501 0.3646 -0.0154 -0.0200 0.0162  174 ASP A OD2 
1311 N  N   . THR A 199 ? 0.3250 0.3033 0.3374 -0.0067 -0.0098 0.0050  175 THR A N   
1312 C  CA  . THR A 199 ? 0.3336 0.3075 0.3509 -0.0039 -0.0075 0.0029  175 THR A CA  
1313 C  C   . THR A 199 ? 0.3142 0.2905 0.3408 -0.0003 -0.0061 0.0049  175 THR A C   
1314 O  O   . THR A 199 ? 0.3481 0.3220 0.3788 0.0027  -0.0035 0.0008  175 THR A O   
1315 C  CB  . THR A 199 ? 0.3322 0.3021 0.3488 -0.0053 -0.0081 0.0051  175 THR A CB  
1316 O  OG1 . THR A 199 ? 0.3502 0.3203 0.3582 -0.0086 -0.0100 0.0056  175 THR A OG1 
1317 C  CG2 . THR A 199 ? 0.3338 0.2978 0.3527 -0.0042 -0.0060 0.0007  175 THR A CG2 
1318 N  N   . SER A 200 ? 0.3181 0.2995 0.3482 -0.0003 -0.0078 0.0109  176 SER A N   
1319 C  CA  . SER A 200 ? 0.3452 0.3293 0.3854 0.0037  -0.0063 0.0138  176 SER A CA  
1320 C  C   . SER A 200 ? 0.3458 0.3327 0.3886 0.0066  -0.0036 0.0100  176 SER A C   
1321 O  O   . SER A 200 ? 0.3550 0.3410 0.4054 0.0109  -0.0009 0.0090  176 SER A O   
1322 C  CB  . SER A 200 ? 0.3563 0.3474 0.3995 0.0029  -0.0093 0.0215  176 SER A CB  
1323 O  OG  . SER A 200 ? 0.3569 0.3544 0.3969 0.0004  -0.0112 0.0220  176 SER A OG  
1324 N  N   . HIS A 201 ? 0.3283 0.3185 0.3652 0.0046  -0.0040 0.0080  177 HIS A N   
1325 C  CA  . HIS A 201 ? 0.3256 0.3196 0.3642 0.0075  -0.0010 0.0051  177 HIS A CA  
1326 C  C   . HIS A 201 ? 0.3359 0.3245 0.3728 0.0102  0.0018  -0.0022 177 HIS A C   
1327 O  O   . HIS A 201 ? 0.3316 0.3223 0.3720 0.0143  0.0049  -0.0050 177 HIS A O   
1328 C  CB  . HIS A 201 ? 0.3022 0.3010 0.3354 0.0045  -0.0021 0.0059  177 HIS A CB  
1329 C  CG  . HIS A 201 ? 0.3540 0.3589 0.3899 0.0017  -0.0052 0.0122  177 HIS A CG  
1330 N  ND1 . HIS A 201 ? 0.3589 0.3686 0.3928 -0.0014 -0.0064 0.0138  177 HIS A ND1 
1331 C  CD2 . HIS A 201 ? 0.3446 0.3521 0.3857 0.0013  -0.0076 0.0174  177 HIS A CD2 
1332 C  CE1 . HIS A 201 ? 0.3654 0.3800 0.4029 -0.0039 -0.0097 0.0190  177 HIS A CE1 
1333 N  NE2 . HIS A 201 ? 0.3639 0.3779 0.4054 -0.0022 -0.0106 0.0214  177 HIS A NE2 
1334 N  N   . LEU A 202 ? 0.3140 0.2961 0.3457 0.0079  0.0008  -0.0055 178 LEU A N   
1335 C  CA  . LEU A 202 ? 0.3260 0.3030 0.3572 0.0099  0.0027  -0.0126 178 LEU A CA  
1336 C  C   . LEU A 202 ? 0.3415 0.3142 0.3820 0.0132  0.0043  -0.0132 178 LEU A C   
1337 O  O   . LEU A 202 ? 0.3303 0.3012 0.3734 0.0166  0.0068  -0.0190 178 LEU A O   
1338 C  CB  . LEU A 202 ? 0.3152 0.2872 0.3402 0.0065  0.0010  -0.0152 178 LEU A CB  
1339 C  CG  . LEU A 202 ? 0.3538 0.3284 0.3700 0.0039  -0.0002 -0.0158 178 LEU A CG  
1340 C  CD1 . LEU A 202 ? 0.3692 0.3388 0.3811 0.0011  -0.0016 -0.0178 178 LEU A CD1 
1341 C  CD2 . LEU A 202 ? 0.3334 0.3120 0.3467 0.0063  0.0018  -0.0201 178 LEU A CD2 
1342 N  N   . TYR A 203 ? 0.3372 0.3081 0.3826 0.0123  0.0030  -0.0072 179 TYR A N   
1343 C  CA  . TYR A 203 ? 0.3476 0.3144 0.4033 0.0156  0.0047  -0.0063 179 TYR A CA  
1344 C  C   . TYR A 203 ? 0.3616 0.3333 0.4240 0.0203  0.0071  -0.0054 179 TYR A C   
1345 O  O   . TYR A 203 ? 0.3596 0.3273 0.4290 0.0244  0.0100  -0.0091 179 TYR A O   
1346 C  CB  . TYR A 203 ? 0.3259 0.2913 0.3850 0.0137  0.0026  0.0015  179 TYR A CB  
1347 C  CG  . TYR A 203 ? 0.3556 0.3143 0.4122 0.0107  0.0018  0.0001  179 TYR A CG  
1348 C  CD1 . TYR A 203 ? 0.3566 0.3076 0.4207 0.0120  0.0035  -0.0027 179 TYR A CD1 
1349 C  CD2 . TYR A 203 ? 0.3298 0.2898 0.3775 0.0064  -0.0006 0.0015  179 TYR A CD2 
1350 C  CE1 . TYR A 203 ? 0.3565 0.3022 0.4198 0.0090  0.0029  -0.0034 179 TYR A CE1 
1351 C  CE2 . TYR A 203 ? 0.3583 0.3131 0.4044 0.0039  -0.0009 0.0007  179 TYR A CE2 
1352 C  CZ  . TYR A 203 ? 0.3706 0.3187 0.4248 0.0051  0.0009  -0.0015 179 TYR A CZ  
1353 O  OH  . TYR A 203 ? 0.3884 0.3322 0.4423 0.0024  0.0007  -0.0017 179 TYR A OH  
1354 N  N   . ASN A 204 ? 0.3177 0.2980 0.3786 0.0199  0.0063  -0.0008 180 ASN A N   
1355 C  CA  . ASN A 204 ? 0.3401 0.3266 0.4073 0.0244  0.0090  0.0003  180 ASN A CA  
1356 C  C   . ASN A 204 ? 0.3616 0.3475 0.4261 0.0277  0.0126  -0.0083 180 ASN A C   
1357 O  O   . ASN A 204 ? 0.3676 0.3527 0.4388 0.0328  0.0161  -0.0111 180 ASN A O   
1358 C  CB  . ASN A 204 ? 0.3521 0.3486 0.4181 0.0224  0.0071  0.0065  180 ASN A CB  
1359 C  CG  . ASN A 204 ? 0.3808 0.3794 0.4493 0.0195  0.0032  0.0146  180 ASN A CG  
1360 O  OD1 . ASN A 204 ? 0.3249 0.3183 0.3971 0.0199  0.0025  0.0168  180 ASN A OD1 
1361 N  ND2 . ASN A 204 ? 0.3473 0.3539 0.4141 0.0165  0.0006  0.0192  180 ASN A ND2 
1362 N  N   . LEU A 205 ? 0.3798 0.3661 0.4342 0.0249  0.0118  -0.0126 181 LEU A N   
1363 C  CA  . LEU A 205 ? 0.3939 0.3807 0.4441 0.0279  0.0148  -0.0206 181 LEU A CA  
1364 C  C   . LEU A 205 ? 0.4026 0.3806 0.4562 0.0303  0.0162  -0.0281 181 LEU A C   
1365 O  O   . LEU A 205 ? 0.3884 0.3666 0.4439 0.0351  0.0196  -0.0340 181 LEU A O   
1366 C  CB  . LEU A 205 ? 0.3416 0.3303 0.3807 0.0243  0.0131  -0.0228 181 LEU A CB  
1367 C  CG  . LEU A 205 ? 0.3861 0.3772 0.4189 0.0271  0.0157  -0.0304 181 LEU A CG  
1368 C  CD1 . LEU A 205 ? 0.3914 0.3907 0.4273 0.0320  0.0197  -0.0296 181 LEU A CD1 
1369 C  CD2 . LEU A 205 ? 0.3706 0.3642 0.3934 0.0235  0.0137  -0.0304 181 LEU A CD2 
1370 N  N   . LYS A 206 ? 0.3739 0.3441 0.4285 0.0271  0.0137  -0.0281 182 LYS A N   
1371 C  CA  . LYS A 206 ? 0.3982 0.3592 0.4579 0.0286  0.0147  -0.0347 182 LYS A CA  
1372 C  C   . LYS A 206 ? 0.4035 0.3626 0.4745 0.0340  0.0180  -0.0343 182 LYS A C   
1373 O  O   . LYS A 206 ? 0.4593 0.4132 0.5335 0.0373  0.0203  -0.0425 182 LYS A O   
1374 C  CB  . LYS A 206 ? 0.4014 0.3557 0.4628 0.0242  0.0119  -0.0319 182 LYS A CB  
1375 C  CG  . LYS A 206 ? 0.4149 0.3591 0.4839 0.0248  0.0126  -0.0373 182 LYS A CG  
1376 C  CD  . LYS A 206 ? 0.4548 0.3970 0.5186 0.0248  0.0128  -0.0486 182 LYS A CD  
1377 C  CE  . LYS A 206 ? 0.5094 0.4413 0.5808 0.0236  0.0124  -0.0538 182 LYS A CE  
1378 N  NZ  . LYS A 206 ? 0.5310 0.4616 0.5973 0.0232  0.0118  -0.0653 182 LYS A NZ  
1379 N  N   . HIS A 207 ? 0.3871 0.3504 0.4644 0.0351  0.0180  -0.0252 183 HIS A N   
1380 C  CA  . HIS A 207 ? 0.4449 0.4070 0.5341 0.0407  0.0212  -0.0235 183 HIS A CA  
1381 C  C   . HIS A 207 ? 0.4542 0.4204 0.5427 0.0462  0.0254  -0.0302 183 HIS A C   
1382 O  O   . HIS A 207 ? 0.4711 0.4317 0.5665 0.0510  0.0287  -0.0359 183 HIS A O   
1383 C  CB  . HIS A 207 ? 0.4340 0.4025 0.5291 0.0407  0.0199  -0.0118 183 HIS A CB  
1384 C  CG  . HIS A 207 ? 0.4885 0.4597 0.5952 0.0471  0.0234  -0.0090 183 HIS A CG  
1385 N  ND1 . HIS A 207 ? 0.5116 0.4750 0.6302 0.0506  0.0252  -0.0080 183 HIS A ND1 
1386 C  CD2 . HIS A 207 ? 0.5054 0.4864 0.6146 0.0509  0.0258  -0.0067 183 HIS A CD2 
1387 C  CE1 . HIS A 207 ? 0.5519 0.5200 0.6796 0.0566  0.0285  -0.0053 183 HIS A CE1 
1388 N  NE2 . HIS A 207 ? 0.5369 0.5162 0.6591 0.0569  0.0290  -0.0045 183 HIS A NE2 
1389 N  N   . PHE A 208 ? 0.4480 0.4241 0.5284 0.0457  0.0257  -0.0294 184 PHE A N   
1390 C  CA  . PHE A 208 ? 0.4555 0.4372 0.5344 0.0511  0.0302  -0.0349 184 PHE A CA  
1391 C  C   . PHE A 208 ? 0.4811 0.4578 0.5524 0.0518  0.0311  -0.0471 184 PHE A C   
1392 O  O   . PHE A 208 ? 0.5002 0.4763 0.5731 0.0574  0.0351  -0.0545 184 PHE A O   
1393 C  CB  . PHE A 208 ? 0.4507 0.4449 0.5242 0.0501  0.0303  -0.0294 184 PHE A CB  
1394 C  CG  . PHE A 208 ? 0.4331 0.4340 0.5149 0.0497  0.0294  -0.0183 184 PHE A CG  
1395 C  CD1 . PHE A 208 ? 0.4679 0.4727 0.5609 0.0556  0.0330  -0.0153 184 PHE A CD1 
1396 C  CD2 . PHE A 208 ? 0.4253 0.4290 0.5040 0.0436  0.0248  -0.0111 184 PHE A CD2 
1397 C  CE1 . PHE A 208 ? 0.4520 0.4642 0.5532 0.0551  0.0316  -0.0049 184 PHE A CE1 
1398 C  CE2 . PHE A 208 ? 0.4315 0.4420 0.5176 0.0430  0.0232  -0.0014 184 PHE A CE2 
1399 C  CZ  . PHE A 208 ? 0.4476 0.4628 0.5452 0.0486  0.0264  0.0019  184 PHE A CZ  
1400 N  N   . TYR A 209 ? 0.4651 0.4387 0.5280 0.0464  0.0273  -0.0494 185 TYR A N   
1401 C  CA  . TYR A 209 ? 0.4967 0.4662 0.5525 0.0463  0.0272  -0.0607 185 TYR A CA  
1402 C  C   . TYR A 209 ? 0.5328 0.4912 0.5971 0.0487  0.0284  -0.0682 185 TYR A C   
1403 O  O   . TYR A 209 ? 0.5281 0.4845 0.5896 0.0519  0.0303  -0.0789 185 TYR A O   
1404 C  CB  . TYR A 209 ? 0.4619 0.4303 0.5095 0.0399  0.0226  -0.0600 185 TYR A CB  
1405 C  CG  . TYR A 209 ? 0.5327 0.4979 0.5734 0.0387  0.0212  -0.0706 185 TYR A CG  
1406 C  CD1 . TYR A 209 ? 0.5411 0.5132 0.5724 0.0414  0.0228  -0.0770 185 TYR A CD1 
1407 C  CD2 . TYR A 209 ? 0.5084 0.4646 0.5520 0.0348  0.0182  -0.0735 185 TYR A CD2 
1408 C  CE1 . TYR A 209 ? 0.5443 0.5146 0.5689 0.0402  0.0208  -0.0866 185 TYR A CE1 
1409 C  CE2 . TYR A 209 ? 0.5081 0.4623 0.5463 0.0333  0.0163  -0.0830 185 TYR A CE2 
1410 C  CZ  . TYR A 209 ? 0.5555 0.5169 0.5839 0.0360  0.0174  -0.0897 185 TYR A CZ  
1411 O  OH  . TYR A 209 ? 0.5568 0.5173 0.5796 0.0344  0.0149  -0.0991 185 TYR A OH  
1412 N  N   . ASP A 210 ? 0.4980 0.4491 0.5729 0.0474  0.0273  -0.0626 186 ASP A N   
1413 C  CA  . ASP A 210 ? 0.5319 0.4713 0.6170 0.0495  0.0286  -0.0685 186 ASP A CA  
1414 C  C   . ASP A 210 ? 0.5401 0.4794 0.6333 0.0570  0.0337  -0.0709 186 ASP A C   
1415 O  O   . ASP A 210 ? 0.5561 0.4860 0.6557 0.0598  0.0356  -0.0794 186 ASP A O   
1416 C  CB  . ASP A 210 ? 0.4774 0.4097 0.5718 0.0459  0.0262  -0.0604 186 ASP A CB  
1417 C  CG  . ASP A 210 ? 0.5580 0.4870 0.6466 0.0391  0.0220  -0.0612 186 ASP A CG  
1418 O  OD1 . ASP A 210 ? 0.5506 0.4815 0.6296 0.0374  0.0207  -0.0693 186 ASP A OD1 
1419 O  OD2 . ASP A 210 ? 0.5869 0.5122 0.6808 0.0358  0.0200  -0.0535 186 ASP A OD2 
1420 N  N   . ARG A 211 ? 0.5450 0.4942 0.6388 0.0602  0.0360  -0.0637 187 ARG A N   
1421 C  CA  . ARG A 211 ? 0.5443 0.4957 0.6451 0.0680  0.0414  -0.0657 187 ARG A CA  
1422 C  C   . ARG A 211 ? 0.5641 0.5222 0.6547 0.0718  0.0446  -0.0753 187 ARG A C   
1423 O  O   . ARG A 211 ? 0.5703 0.5310 0.6652 0.0788  0.0498  -0.0783 187 ARG A O   
1424 C  CB  . ARG A 211 ? 0.5755 0.5361 0.6833 0.0698  0.0424  -0.0528 187 ARG A CB  
1425 C  CG  . ARG A 211 ? 0.5867 0.5414 0.7066 0.0684  0.0404  -0.0433 187 ARG A CG  
1426 C  CD  . ARG A 211 ? 0.5794 0.5453 0.7043 0.0693  0.0401  -0.0306 187 ARG A CD  
1427 N  NE  . ARG A 211 ? 0.7049 0.6785 0.8349 0.0765  0.0454  -0.0310 187 ARG A NE  
1428 C  CZ  . ARG A 211 ? 0.6638 0.6501 0.7968 0.0777  0.0459  -0.0219 187 ARG A CZ  
1429 N  NH1 . ARG A 211 ? 0.6342 0.6267 0.7652 0.0720  0.0411  -0.0122 187 ARG A NH1 
1430 N  NH2 . ARG A 211 ? 0.6317 0.6250 0.7702 0.0847  0.0513  -0.0228 187 ARG A NH2 
1431 N  N   . GLY A 212 ? 0.5710 0.5325 0.6481 0.0676  0.0419  -0.0797 188 GLY A N   
1432 C  CA  . GLY A 212 ? 0.5966 0.5652 0.6627 0.0711  0.0446  -0.0885 188 GLY A CA  
1433 C  C   . GLY A 212 ? 0.5828 0.5658 0.6450 0.0740  0.0478  -0.0817 188 GLY A C   
1434 O  O   . GLY A 212 ? 0.6054 0.5953 0.6604 0.0786  0.0516  -0.0880 188 GLY A O   
1435 N  N   . LEU A 213 ? 0.5591 0.5476 0.6259 0.0714  0.0464  -0.0689 189 LEU A N   
1436 C  CA  . LEU A 213 ? 0.5637 0.5662 0.6290 0.0736  0.0493  -0.0617 189 LEU A CA  
1437 C  C   . LEU A 213 ? 0.5455 0.5561 0.5972 0.0697  0.0474  -0.0608 189 LEU A C   
1438 O  O   . LEU A 213 ? 0.5655 0.5880 0.6142 0.0721  0.0507  -0.0570 189 LEU A O   
1439 C  CB  . LEU A 213 ? 0.5543 0.5599 0.6306 0.0720  0.0480  -0.0488 189 LEU A CB  
1440 C  CG  . LEU A 213 ? 0.6442 0.6450 0.7354 0.0772  0.0508  -0.0472 189 LEU A CG  
1441 C  CD1 . LEU A 213 ? 0.6186 0.6251 0.7197 0.0755  0.0489  -0.0338 189 LEU A CD1 
1442 C  CD2 . LEU A 213 ? 0.6328 0.6376 0.7265 0.0859  0.0578  -0.0535 189 LEU A CD2 
1443 N  N   . VAL A 214 ? 0.5565 0.5614 0.6008 0.0640  0.0426  -0.0637 190 VAL A N   
1444 C  CA  . VAL A 214 ? 0.5683 0.5796 0.5995 0.0612  0.0410  -0.0647 190 VAL A CA  
1445 C  C   . VAL A 214 ? 0.6046 0.6084 0.6285 0.0597  0.0384  -0.0757 190 VAL A C   
1446 O  O   . VAL A 214 ? 0.6049 0.5976 0.6343 0.0575  0.0358  -0.0791 190 VAL A O   
1447 C  CB  . VAL A 214 ? 0.5118 0.5260 0.5416 0.0546  0.0370  -0.0542 190 VAL A CB  
1448 C  CG1 . VAL A 214 ? 0.5004 0.5247 0.5357 0.0558  0.0394  -0.0442 190 VAL A CG1 
1449 C  CG2 . VAL A 214 ? 0.4612 0.4650 0.4967 0.0497  0.0324  -0.0517 190 VAL A CG2 
1450 N  N   . LYS A 215 ? 0.5725 0.5832 0.5845 0.0608  0.0391  -0.0808 191 LYS A N   
1451 C  CA  . LYS A 215 ? 0.5808 0.5869 0.5849 0.0597  0.0364  -0.0918 191 LYS A CA  
1452 C  C   . LYS A 215 ? 0.5595 0.5695 0.5544 0.0544  0.0321  -0.0883 191 LYS A C   
1453 O  O   . LYS A 215 ? 0.5426 0.5612 0.5339 0.0534  0.0328  -0.0796 191 LYS A O   
1454 C  CB  . LYS A 215 ? 0.6080 0.6196 0.6047 0.0661  0.0405  -0.1021 191 LYS A CB  
1455 C  CG  . LYS A 215 ? 0.6958 0.7027 0.7014 0.0722  0.0451  -0.1076 191 LYS A CG  
1456 C  CD  . LYS A 215 ? 0.7525 0.7443 0.7661 0.0705  0.0424  -0.1156 191 LYS A CD  
1457 C  CE  . LYS A 215 ? 0.8223 0.8091 0.8427 0.0774  0.0473  -0.1242 191 LYS A CE  
1458 N  NZ  . LYS A 215 ? 0.8209 0.8109 0.8516 0.0817  0.0522  -0.1151 191 LYS A NZ  
1459 N  N   . GLY A 216 ? 0.5534 0.5568 0.5455 0.0509  0.0278  -0.0949 192 GLY A N   
1460 C  CA  . GLY A 216 ? 0.5555 0.5621 0.5397 0.0463  0.0237  -0.0923 192 GLY A CA  
1461 C  C   . GLY A 216 ? 0.5168 0.5349 0.4882 0.0492  0.0250  -0.0952 192 GLY A C   
1462 O  O   . GLY A 216 ? 0.5173 0.5401 0.4849 0.0546  0.0286  -0.1017 192 GLY A O   
1463 N  N   . PRO A 217 ? 0.5118 0.5349 0.4763 0.0458  0.0221  -0.0902 193 PRO A N   
1464 C  CA  . PRO A 217 ? 0.5126 0.5308 0.4808 0.0399  0.0183  -0.0827 193 PRO A CA  
1465 C  C   . PRO A 217 ? 0.5055 0.5248 0.4796 0.0387  0.0202  -0.0713 193 PRO A C   
1466 O  O   . PRO A 217 ? 0.5097 0.5378 0.4809 0.0412  0.0235  -0.0661 193 PRO A O   
1467 C  CB  . PRO A 217 ? 0.5144 0.5396 0.4724 0.0384  0.0158  -0.0821 193 PRO A CB  
1468 C  CG  . PRO A 217 ? 0.4967 0.5335 0.4462 0.0437  0.0196  -0.0830 193 PRO A CG  
1469 C  CD  . PRO A 217 ? 0.4847 0.5196 0.4369 0.0484  0.0229  -0.0914 193 PRO A CD  
1470 N  N   . LEU A 218 ? 0.5007 0.5115 0.4829 0.0349  0.0181  -0.0673 194 LEU A N   
1471 C  CA  . LEU A 218 ? 0.4504 0.4620 0.4384 0.0333  0.0190  -0.0572 194 LEU A CA  
1472 C  C   . LEU A 218 ? 0.4510 0.4655 0.4343 0.0294  0.0168  -0.0502 194 LEU A C   
1473 O  O   . LEU A 218 ? 0.4549 0.4651 0.4357 0.0259  0.0133  -0.0513 194 LEU A O   
1474 C  CB  . LEU A 218 ? 0.4548 0.4569 0.4525 0.0311  0.0175  -0.0557 194 LEU A CB  
1475 C  CG  . LEU A 218 ? 0.4724 0.4688 0.4767 0.0345  0.0192  -0.0626 194 LEU A CG  
1476 C  CD1 . LEU A 218 ? 0.4597 0.4470 0.4734 0.0317  0.0173  -0.0594 194 LEU A CD1 
1477 C  CD2 . LEU A 218 ? 0.4623 0.4648 0.4693 0.0402  0.0240  -0.0623 194 LEU A CD2 
1478 N  N   . PHE A 219 ? 0.4275 0.4493 0.4105 0.0299  0.0190  -0.0429 195 PHE A N   
1479 C  CA  . PHE A 219 ? 0.3984 0.4222 0.3785 0.0262  0.0174  -0.0356 195 PHE A CA  
1480 C  C   . PHE A 219 ? 0.4388 0.4571 0.4262 0.0221  0.0154  -0.0297 195 PHE A C   
1481 O  O   . PHE A 219 ? 0.4054 0.4272 0.3985 0.0223  0.0170  -0.0242 195 PHE A O   
1482 C  CB  . PHE A 219 ? 0.4024 0.4369 0.3795 0.0286  0.0208  -0.0305 195 PHE A CB  
1483 C  CG  . PHE A 219 ? 0.4317 0.4682 0.4052 0.0254  0.0194  -0.0240 195 PHE A CG  
1484 C  CD1 . PHE A 219 ? 0.4083 0.4397 0.3775 0.0226  0.0159  -0.0258 195 PHE A CD1 
1485 C  CD2 . PHE A 219 ? 0.4348 0.4784 0.4103 0.0253  0.0219  -0.0159 195 PHE A CD2 
1486 C  CE1 . PHE A 219 ? 0.4634 0.4962 0.4301 0.0202  0.0150  -0.0198 195 PHE A CE1 
1487 C  CE2 . PHE A 219 ? 0.4649 0.5093 0.4382 0.0224  0.0209  -0.0099 195 PHE A CE2 
1488 C  CZ  . PHE A 219 ? 0.4399 0.4785 0.4087 0.0201  0.0175  -0.0119 195 PHE A CZ  
1489 N  N   . ILE A 220 ? 0.3995 0.4100 0.3868 0.0184  0.0119  -0.0308 196 ILE A N   
1490 C  CA  . ILE A 220 ? 0.3931 0.3982 0.3861 0.0148  0.0097  -0.0263 196 ILE A CA  
1491 C  C   . ILE A 220 ? 0.4004 0.4051 0.3902 0.0108  0.0078  -0.0212 196 ILE A C   
1492 O  O   . ILE A 220 ? 0.4075 0.4098 0.3922 0.0094  0.0062  -0.0231 196 ILE A O   
1493 C  CB  . ILE A 220 ? 0.4029 0.3996 0.3984 0.0137  0.0077  -0.0307 196 ILE A CB  
1494 C  CG1 . ILE A 220 ? 0.3698 0.3656 0.3694 0.0178  0.0098  -0.0363 196 ILE A CG1 
1495 C  CG2 . ILE A 220 ? 0.3924 0.3846 0.3924 0.0102  0.0056  -0.0254 196 ILE A CG2 
1496 C  CD1 . ILE A 220 ? 0.3772 0.3643 0.3813 0.0167  0.0082  -0.0400 196 ILE A CD1 
1497 N  N   . GLN A 221 ? 0.3695 0.3765 0.3631 0.0088  0.0078  -0.0148 197 GLN A N   
1498 C  CA  . GLN A 221 ? 0.3839 0.3893 0.3757 0.0047  0.0058  -0.0103 197 GLN A CA  
1499 C  C   . GLN A 221 ? 0.3887 0.3886 0.3839 0.0012  0.0029  -0.0085 197 GLN A C   
1500 O  O   . GLN A 221 ? 0.3956 0.3976 0.3967 0.0011  0.0028  -0.0057 197 GLN A O   
1501 C  CB  . GLN A 221 ? 0.3782 0.3907 0.3720 0.0045  0.0076  -0.0045 197 GLN A CB  
1502 C  CG  . GLN A 221 ? 0.3979 0.4076 0.3906 0.0001  0.0056  -0.0005 197 GLN A CG  
1503 C  CD  . GLN A 221 ? 0.4328 0.4485 0.4250 0.0006  0.0079  0.0040  197 GLN A CD  
1504 O  OE1 . GLN A 221 ? 0.4726 0.4879 0.4594 0.0013  0.0084  0.0036  197 GLN A OE1 
1505 N  NE2 . GLN A 221 ? 0.4536 0.4755 0.4519 0.0002  0.0095  0.0090  197 GLN A NE2 
1506 N  N   . THR A 222 ? 0.3410 0.3347 0.3324 -0.0014 0.0007  -0.0098 198 THR A N   
1507 C  CA  . THR A 222 ? 0.3724 0.3613 0.3651 -0.0047 -0.0019 -0.0083 198 THR A CA  
1508 C  C   . THR A 222 ? 0.3500 0.3385 0.3414 -0.0084 -0.0035 -0.0046 198 THR A C   
1509 O  O   . THR A 222 ? 0.3519 0.3387 0.3392 -0.0092 -0.0033 -0.0049 198 THR A O   
1510 C  CB  . THR A 222 ? 0.3350 0.3178 0.3246 -0.0051 -0.0029 -0.0121 198 THR A CB  
1511 O  OG1 . THR A 222 ? 0.3528 0.3345 0.3372 -0.0052 -0.0027 -0.0140 198 THR A OG1 
1512 C  CG2 . THR A 222 ? 0.3431 0.3253 0.3358 -0.0020 -0.0018 -0.0159 198 THR A CG2 
1513 N  N   . VAL A 223 ? 0.3025 0.2927 0.2980 -0.0106 -0.0051 -0.0011 199 VAL A N   
1514 C  CA  . VAL A 223 ? 0.3240 0.3145 0.3200 -0.0145 -0.0068 0.0022  199 VAL A CA  
1515 C  C   . VAL A 223 ? 0.3469 0.3318 0.3397 -0.0179 -0.0100 0.0013  199 VAL A C   
1516 O  O   . VAL A 223 ? 0.3671 0.3520 0.3612 -0.0181 -0.0116 0.0016  199 VAL A O   
1517 C  CB  . VAL A 223 ? 0.3576 0.3555 0.3611 -0.0150 -0.0069 0.0066  199 VAL A CB  
1518 C  CG1 . VAL A 223 ? 0.3394 0.3374 0.3446 -0.0197 -0.0090 0.0096  199 VAL A CG1 
1519 C  CG2 . VAL A 223 ? 0.3313 0.3355 0.3374 -0.0109 -0.0030 0.0073  199 VAL A CG2 
1520 N  N   . PHE A 224 ? 0.3543 0.3346 0.3431 -0.0204 -0.0108 0.0005  200 PHE A N   
1521 C  CA  . PHE A 224 ? 0.3760 0.3504 0.3599 -0.0230 -0.0131 -0.0014 200 PHE A CA  
1522 C  C   . PHE A 224 ? 0.3720 0.3451 0.3564 -0.0274 -0.0156 -0.0003 200 PHE A C   
1523 O  O   . PHE A 224 ? 0.3810 0.3541 0.3675 -0.0285 -0.0147 0.0011  200 PHE A O   
1524 C  CB  . PHE A 224 ? 0.3275 0.2964 0.3059 -0.0217 -0.0116 -0.0047 200 PHE A CB  
1525 C  CG  . PHE A 224 ? 0.3825 0.3523 0.3608 -0.0181 -0.0097 -0.0066 200 PHE A CG  
1526 C  CD1 . PHE A 224 ? 0.3363 0.3047 0.3142 -0.0176 -0.0103 -0.0077 200 PHE A CD1 
1527 C  CD2 . PHE A 224 ? 0.3279 0.3000 0.3065 -0.0154 -0.0075 -0.0073 200 PHE A CD2 
1528 C  CE1 . PHE A 224 ? 0.3706 0.3390 0.3496 -0.0148 -0.0087 -0.0098 200 PHE A CE1 
1529 C  CE2 . PHE A 224 ? 0.3518 0.3246 0.3303 -0.0125 -0.0063 -0.0100 200 PHE A CE2 
1530 C  CZ  . PHE A 224 ? 0.3443 0.3148 0.3236 -0.0124 -0.0069 -0.0115 200 PHE A CZ  
1531 N  N   . GLY A 225 ? 0.3664 0.3387 0.3490 -0.0300 -0.0187 -0.0008 201 GLY A N   
1532 C  CA  . GLY A 225 ? 0.3486 0.3181 0.3298 -0.0345 -0.0216 -0.0016 201 GLY A CA  
1533 C  C   . GLY A 225 ? 0.3988 0.3743 0.3862 -0.0378 -0.0248 0.0013  201 GLY A C   
1534 O  O   . GLY A 225 ? 0.4265 0.3997 0.4137 -0.0421 -0.0276 0.0001  201 GLY A O   
1535 N  N   . LEU A 226 ? 0.3808 0.3639 0.3744 -0.0360 -0.0245 0.0049  202 LEU A N   
1536 C  CA  . LEU A 226 ? 0.3999 0.3901 0.4006 -0.0389 -0.0275 0.0083  202 LEU A CA  
1537 C  C   . LEU A 226 ? 0.3919 0.3843 0.3901 -0.0407 -0.0318 0.0082  202 LEU A C   
1538 O  O   . LEU A 226 ? 0.3847 0.3758 0.3782 -0.0380 -0.0313 0.0074  202 LEU A O   
1539 C  CB  . LEU A 226 ? 0.3977 0.3960 0.4067 -0.0357 -0.0250 0.0126  202 LEU A CB  
1540 C  CG  . LEU A 226 ? 0.4435 0.4424 0.4552 -0.0335 -0.0206 0.0137  202 LEU A CG  
1541 C  CD1 . LEU A 226 ? 0.4230 0.4317 0.4440 -0.0314 -0.0188 0.0184  202 LEU A CD1 
1542 C  CD2 . LEU A 226 ? 0.4679 0.4625 0.4794 -0.0374 -0.0211 0.0134  202 LEU A CD2 
1543 N  N   . MET A 227 ? 0.3959 0.3922 0.3975 -0.0454 -0.0363 0.0091  203 MET A N   
1544 C  CA  . MET A 227 ? 0.4307 0.4316 0.4305 -0.0471 -0.0410 0.0099  203 MET A CA  
1545 C  C   . MET A 227 ? 0.4230 0.4332 0.4307 -0.0438 -0.0405 0.0154  203 MET A C   
1546 O  O   . MET A 227 ? 0.4145 0.4316 0.4320 -0.0441 -0.0403 0.0192  203 MET A O   
1547 C  CB  . MET A 227 ? 0.4353 0.4381 0.4366 -0.0534 -0.0464 0.0086  203 MET A CB  
1548 C  CG  . MET A 227 ? 0.5263 0.5324 0.5217 -0.0553 -0.0516 0.0076  203 MET A CG  
1549 S  SD  . MET A 227 ? 0.6915 0.7027 0.6904 -0.0630 -0.0592 0.0062  203 MET A SD  
1550 C  CE  . MET A 227 ? 0.6813 0.6961 0.6692 -0.0633 -0.0642 0.0047  203 MET A CE  
1551 N  N   . GLY A 228 ? 0.4055 0.4160 0.4097 -0.0404 -0.0400 0.0164  204 GLY A N   
1552 C  CA  . GLY A 228 ? 0.3746 0.3913 0.3861 -0.0360 -0.0383 0.0212  204 GLY A CA  
1553 C  C   . GLY A 228 ? 0.3803 0.3918 0.3910 -0.0308 -0.0327 0.0199  204 GLY A C   
1554 O  O   . GLY A 228 ? 0.3804 0.3949 0.3962 -0.0267 -0.0310 0.0229  204 GLY A O   
1555 N  N   . GLY A 229 ? 0.3909 0.3946 0.3957 -0.0309 -0.0301 0.0154  205 GLY A N   
1556 C  CA  . GLY A 229 ? 0.3316 0.3303 0.3347 -0.0266 -0.0256 0.0133  205 GLY A CA  
1557 C  C   . GLY A 229 ? 0.3510 0.3420 0.3449 -0.0269 -0.0253 0.0096  205 GLY A C   
1558 O  O   . GLY A 229 ? 0.3738 0.3635 0.3619 -0.0299 -0.0283 0.0088  205 GLY A O   
1559 N  N   . ILE A 230 ? 0.3347 0.3211 0.3271 -0.0239 -0.0216 0.0071  206 ILE A N   
1560 C  CA  . ILE A 230 ? 0.3416 0.3213 0.3264 -0.0240 -0.0208 0.0039  206 ILE A CA  
1561 C  C   . ILE A 230 ? 0.3601 0.3357 0.3396 -0.0268 -0.0212 0.0008  206 ILE A C   
1562 O  O   . ILE A 230 ? 0.3530 0.3297 0.3352 -0.0278 -0.0210 0.0009  206 ILE A O   
1563 C  CB  . ILE A 230 ? 0.3426 0.3194 0.3288 -0.0203 -0.0172 0.0021  206 ILE A CB  
1564 C  CG1 . ILE A 230 ? 0.3471 0.3187 0.3276 -0.0203 -0.0165 0.0001  206 ILE A CG1 
1565 C  CG2 . ILE A 230 ? 0.3068 0.2832 0.2939 -0.0192 -0.0149 -0.0002 206 ILE A CG2 
1566 C  CD1 . ILE A 230 ? 0.3491 0.3184 0.3324 -0.0173 -0.0137 -0.0015 206 ILE A CD1 
1567 N  N   . GLY A 231 ? 0.3869 0.3577 0.3591 -0.0278 -0.0216 -0.0017 207 GLY A N   
1568 C  CA  . GLY A 231 ? 0.3556 0.3213 0.3229 -0.0299 -0.0217 -0.0050 207 GLY A CA  
1569 C  C   . GLY A 231 ? 0.3698 0.3321 0.3374 -0.0277 -0.0183 -0.0069 207 GLY A C   
1570 O  O   . GLY A 231 ? 0.3695 0.3339 0.3410 -0.0249 -0.0162 -0.0061 207 GLY A O   
1571 N  N   . ALA A 232 ? 0.3683 0.3251 0.3314 -0.0289 -0.0178 -0.0096 208 ALA A N   
1572 C  CA  . ALA A 232 ? 0.4183 0.3723 0.3816 -0.0269 -0.0151 -0.0108 208 ALA A CA  
1573 C  C   . ALA A 232 ? 0.4327 0.3820 0.3908 -0.0255 -0.0134 -0.0136 208 ALA A C   
1574 O  O   . ALA A 232 ? 0.4256 0.3717 0.3830 -0.0244 -0.0116 -0.0148 208 ALA A O   
1575 C  CB  . ALA A 232 ? 0.4107 0.3628 0.3758 -0.0290 -0.0155 -0.0105 208 ALA A CB  
1576 N  N   . HIS A 233 ? 0.4006 0.3500 0.3556 -0.0253 -0.0136 -0.0140 209 HIS A N   
1577 C  CA  . HIS A 233 ? 0.4157 0.3620 0.3669 -0.0237 -0.0116 -0.0161 209 HIS A CA  
1578 C  C   . HIS A 233 ? 0.3970 0.3448 0.3520 -0.0209 -0.0094 -0.0158 209 HIS A C   
1579 O  O   . HIS A 233 ? 0.3923 0.3438 0.3519 -0.0200 -0.0096 -0.0144 209 HIS A O   
1580 C  CB  . HIS A 233 ? 0.4131 0.3602 0.3602 -0.0243 -0.0123 -0.0156 209 HIS A CB  
1581 C  CG  . HIS A 233 ? 0.4738 0.4181 0.4164 -0.0230 -0.0099 -0.0174 209 HIS A CG  
1582 N  ND1 . HIS A 233 ? 0.4800 0.4255 0.4251 -0.0209 -0.0076 -0.0165 209 HIS A ND1 
1583 C  CD2 . HIS A 233 ? 0.4911 0.4316 0.4271 -0.0235 -0.0093 -0.0202 209 HIS A CD2 
1584 C  CE1 . HIS A 233 ? 0.4802 0.4237 0.4211 -0.0200 -0.0055 -0.0180 209 HIS A CE1 
1585 N  NE2 . HIS A 233 ? 0.4853 0.4256 0.4201 -0.0213 -0.0063 -0.0204 209 HIS A NE2 
1586 N  N   . PRO A 234 ? 0.4163 0.3617 0.3699 -0.0193 -0.0074 -0.0175 210 PRO A N   
1587 C  CA  . PRO A 234 ? 0.3905 0.3384 0.3480 -0.0170 -0.0059 -0.0178 210 PRO A CA  
1588 C  C   . PRO A 234 ? 0.3929 0.3431 0.3536 -0.0167 -0.0059 -0.0169 210 PRO A C   
1589 O  O   . PRO A 234 ? 0.3547 0.3074 0.3200 -0.0154 -0.0057 -0.0173 210 PRO A O   
1590 C  CB  . PRO A 234 ? 0.4147 0.3601 0.3701 -0.0158 -0.0040 -0.0193 210 PRO A CB  
1591 C  CG  . PRO A 234 ? 0.4067 0.3478 0.3580 -0.0168 -0.0042 -0.0201 210 PRO A CG  
1592 C  CD  . PRO A 234 ? 0.4128 0.3537 0.3620 -0.0195 -0.0064 -0.0196 210 PRO A CD  
1593 N  N   . ASP A 235 ? 0.3872 0.3369 0.3458 -0.0177 -0.0061 -0.0156 211 ASP A N   
1594 C  CA  . ASP A 235 ? 0.4170 0.3687 0.3797 -0.0174 -0.0060 -0.0137 211 ASP A CA  
1595 C  C   . ASP A 235 ? 0.4069 0.3609 0.3739 -0.0172 -0.0075 -0.0124 211 ASP A C   
1596 O  O   . ASP A 235 ? 0.4014 0.3564 0.3741 -0.0160 -0.0070 -0.0122 211 ASP A O   
1597 C  CB  . ASP A 235 ? 0.4458 0.3973 0.4045 -0.0183 -0.0060 -0.0114 211 ASP A CB  
1598 C  CG  . ASP A 235 ? 0.5855 0.5358 0.5416 -0.0177 -0.0036 -0.0121 211 ASP A CG  
1599 O  OD1 . ASP A 235 ? 0.5379 0.4882 0.4980 -0.0166 -0.0021 -0.0134 211 ASP A OD1 
1600 O  OD2 . ASP A 235 ? 0.6408 0.5910 0.5910 -0.0183 -0.0033 -0.0113 211 ASP A OD2 
1601 N  N   . ASP A 236 ? 0.3743 0.3291 0.3395 -0.0184 -0.0092 -0.0117 212 ASP A N   
1602 C  CA  . ASP A 236 ? 0.3868 0.3449 0.3568 -0.0180 -0.0101 -0.0101 212 ASP A CA  
1603 C  C   . ASP A 236 ? 0.3830 0.3423 0.3566 -0.0160 -0.0088 -0.0121 212 ASP A C   
1604 O  O   . ASP A 236 ? 0.3694 0.3306 0.3481 -0.0144 -0.0084 -0.0120 212 ASP A O   
1605 C  CB  . ASP A 236 ? 0.3536 0.3131 0.3218 -0.0201 -0.0123 -0.0088 212 ASP A CB  
1606 C  CG  . ASP A 236 ? 0.3715 0.3310 0.3356 -0.0221 -0.0142 -0.0072 212 ASP A CG  
1607 O  OD1 . ASP A 236 ? 0.4033 0.3639 0.3682 -0.0214 -0.0141 -0.0051 212 ASP A OD1 
1608 O  OD2 . ASP A 236 ? 0.3772 0.3357 0.3373 -0.0244 -0.0159 -0.0082 212 ASP A OD2 
1609 N  N   . VAL A 237 ? 0.3564 0.3146 0.3273 -0.0158 -0.0082 -0.0140 213 VAL A N   
1610 C  CA  . VAL A 237 ? 0.3561 0.3166 0.3290 -0.0137 -0.0071 -0.0159 213 VAL A CA  
1611 C  C   . VAL A 237 ? 0.3754 0.3359 0.3516 -0.0122 -0.0064 -0.0182 213 VAL A C   
1612 O  O   . VAL A 237 ? 0.3735 0.3362 0.3532 -0.0105 -0.0060 -0.0195 213 VAL A O   
1613 C  CB  . VAL A 237 ? 0.4008 0.3603 0.3702 -0.0135 -0.0066 -0.0166 213 VAL A CB  
1614 C  CG1 . VAL A 237 ? 0.3622 0.3256 0.3329 -0.0111 -0.0057 -0.0180 213 VAL A CG1 
1615 C  CG2 . VAL A 237 ? 0.3667 0.3251 0.3342 -0.0155 -0.0073 -0.0146 213 VAL A CG2 
1616 N  N   . LEU A 238 ? 0.4130 0.3710 0.3884 -0.0128 -0.0060 -0.0188 214 LEU A N   
1617 C  CA  . LEU A 238 ? 0.3976 0.3556 0.3774 -0.0120 -0.0055 -0.0210 214 LEU A CA  
1618 C  C   . LEU A 238 ? 0.4160 0.3735 0.4011 -0.0118 -0.0055 -0.0199 214 LEU A C   
1619 O  O   . LEU A 238 ? 0.3793 0.3369 0.3694 -0.0107 -0.0052 -0.0226 214 LEU A O   
1620 C  CB  . LEU A 238 ? 0.4594 0.4156 0.4382 -0.0129 -0.0047 -0.0208 214 LEU A CB  
1621 C  CG  . LEU A 238 ? 0.5414 0.4993 0.5207 -0.0120 -0.0045 -0.0235 214 LEU A CG  
1622 C  CD1 . LEU A 238 ? 0.4864 0.4461 0.4713 -0.0113 -0.0051 -0.0268 214 LEU A CD1 
1623 C  CD2 . LEU A 238 ? 0.4712 0.4305 0.4461 -0.0110 -0.0047 -0.0238 214 LEU A CD2 
1624 N  N   . HIS A 239 ? 0.3828 0.3396 0.3672 -0.0127 -0.0059 -0.0161 215 HIS A N   
1625 C  CA  . HIS A 239 ? 0.3994 0.3561 0.3896 -0.0121 -0.0059 -0.0140 215 HIS A CA  
1626 C  C   . HIS A 239 ? 0.3913 0.3499 0.3853 -0.0101 -0.0057 -0.0157 215 HIS A C   
1627 O  O   . HIS A 239 ? 0.4125 0.3699 0.4127 -0.0087 -0.0050 -0.0171 215 HIS A O   
1628 C  CB  . HIS A 239 ? 0.4227 0.3800 0.4107 -0.0134 -0.0069 -0.0092 215 HIS A CB  
1629 C  CG  . HIS A 239 ? 0.4271 0.3853 0.4212 -0.0123 -0.0071 -0.0059 215 HIS A CG  
1630 N  ND1 . HIS A 239 ? 0.4183 0.3742 0.4189 -0.0115 -0.0059 -0.0046 215 HIS A ND1 
1631 C  CD2 . HIS A 239 ? 0.4272 0.3884 0.4231 -0.0117 -0.0082 -0.0031 215 HIS A CD2 
1632 C  CE1 . HIS A 239 ? 0.4251 0.3823 0.4310 -0.0102 -0.0062 -0.0011 215 HIS A CE1 
1633 N  NE2 . HIS A 239 ? 0.4101 0.3709 0.4132 -0.0102 -0.0076 -0.0002 215 HIS A NE2 
1634 N  N   . MET A 240 ? 0.3700 0.3316 0.3608 -0.0099 -0.0062 -0.0155 216 MET A N   
1635 C  CA  . MET A 240 ? 0.3936 0.3581 0.3875 -0.0076 -0.0054 -0.0168 216 MET A CA  
1636 C  C   . MET A 240 ? 0.3929 0.3575 0.3874 -0.0058 -0.0044 -0.0222 216 MET A C   
1637 O  O   . MET A 240 ? 0.3660 0.3309 0.3650 -0.0035 -0.0035 -0.0247 216 MET A O   
1638 C  CB  . MET A 240 ? 0.3282 0.2965 0.3190 -0.0081 -0.0059 -0.0147 216 MET A CB  
1639 C  CG  . MET A 240 ? 0.3170 0.2862 0.3078 -0.0101 -0.0075 -0.0100 216 MET A CG  
1640 S  SD  . MET A 240 ? 0.3610 0.3331 0.3597 -0.0084 -0.0075 -0.0066 216 MET A SD  
1641 C  CE  . MET A 240 ? 0.4066 0.3841 0.4082 -0.0057 -0.0057 -0.0076 216 MET A CE  
1642 N  N   . LYS A 241 ? 0.3513 0.3159 0.3415 -0.0065 -0.0048 -0.0243 217 LYS A N   
1643 C  CA  . LYS A 241 ? 0.3852 0.3510 0.3755 -0.0051 -0.0045 -0.0295 217 LYS A CA  
1644 C  C   . LYS A 241 ? 0.3888 0.3511 0.3852 -0.0051 -0.0046 -0.0324 217 LYS A C   
1645 O  O   . LYS A 241 ? 0.4083 0.3709 0.4077 -0.0034 -0.0042 -0.0369 217 LYS A O   
1646 C  CB  . LYS A 241 ? 0.4008 0.3676 0.3861 -0.0059 -0.0052 -0.0300 217 LYS A CB  
1647 C  CG  . LYS A 241 ? 0.3934 0.3626 0.3788 -0.0048 -0.0057 -0.0352 217 LYS A CG  
1648 C  CD  . LYS A 241 ? 0.4220 0.3955 0.4061 -0.0020 -0.0051 -0.0382 217 LYS A CD  
1649 C  CE  . LYS A 241 ? 0.4578 0.4358 0.4390 -0.0008 -0.0062 -0.0426 217 LYS A CE  
1650 N  NZ  . LYS A 241 ? 0.4166 0.3927 0.4022 -0.0019 -0.0076 -0.0475 217 LYS A NZ  
1651 N  N   . ARG A 242 ? 0.4065 0.3654 0.4050 -0.0072 -0.0048 -0.0297 218 ARG A N   
1652 C  CA  . ARG A 242 ? 0.3949 0.3501 0.4006 -0.0078 -0.0046 -0.0312 218 ARG A CA  
1653 C  C   . ARG A 242 ? 0.4068 0.3601 0.4187 -0.0060 -0.0038 -0.0314 218 ARG A C   
1654 O  O   . ARG A 242 ? 0.4302 0.3812 0.4479 -0.0051 -0.0035 -0.0360 218 ARG A O   
1655 C  CB  . ARG A 242 ? 0.4690 0.4219 0.4753 -0.0100 -0.0044 -0.0265 218 ARG A CB  
1656 C  CG  . ARG A 242 ? 0.5692 0.5188 0.5834 -0.0112 -0.0039 -0.0270 218 ARG A CG  
1657 C  CD  . ARG A 242 ? 0.5539 0.5027 0.5675 -0.0130 -0.0031 -0.0213 218 ARG A CD  
1658 N  NE  . ARG A 242 ? 0.5728 0.5240 0.5790 -0.0138 -0.0033 -0.0211 218 ARG A NE  
1659 C  CZ  . ARG A 242 ? 0.6070 0.5591 0.6062 -0.0140 -0.0032 -0.0177 218 ARG A CZ  
1660 N  NH1 . ARG A 242 ? 0.5594 0.5111 0.5574 -0.0139 -0.0033 -0.0138 218 ARG A NH1 
1661 N  NH2 . ARG A 242 ? 0.5814 0.5347 0.5749 -0.0143 -0.0030 -0.0185 218 ARG A NH2 
1662 N  N   . THR A 243 ? 0.3910 0.3453 0.4024 -0.0053 -0.0034 -0.0266 219 THR A N   
1663 C  CA  . THR A 243 ? 0.4250 0.3781 0.4431 -0.0031 -0.0024 -0.0257 219 THR A CA  
1664 C  C   . THR A 243 ? 0.4000 0.3550 0.4186 -0.0001 -0.0015 -0.0315 219 THR A C   
1665 O  O   . THR A 243 ? 0.3552 0.3070 0.3805 0.0017  -0.0004 -0.0349 219 THR A O   
1666 C  CB  . THR A 243 ? 0.4146 0.3702 0.4318 -0.0030 -0.0027 -0.0190 219 THR A CB  
1667 O  OG1 . THR A 243 ? 0.4085 0.3631 0.4235 -0.0056 -0.0037 -0.0142 219 THR A OG1 
1668 C  CG2 . THR A 243 ? 0.3835 0.3383 0.4090 -0.0004 -0.0016 -0.0171 219 THR A CG2 
1669 N  N   . ALA A 244 ? 0.3958 0.3558 0.4075 0.0005  -0.0016 -0.0327 220 ALA A N   
1670 C  CA  . ALA A 244 ? 0.3915 0.3546 0.4021 0.0035  -0.0004 -0.0380 220 ALA A CA  
1671 C  C   . ALA A 244 ? 0.3870 0.3476 0.3990 0.0038  -0.0009 -0.0456 220 ALA A C   
1672 O  O   . ALA A 244 ? 0.3979 0.3575 0.4135 0.0064  0.0003  -0.0509 220 ALA A O   
1673 C  CB  . ALA A 244 ? 0.3681 0.3375 0.3709 0.0038  -0.0004 -0.0368 220 ALA A CB  
1674 N  N   . ASP A 245 ? 0.4034 0.3634 0.4131 0.0011  -0.0026 -0.0466 221 ASP A N   
1675 C  CA  . ASP A 245 ? 0.4100 0.3683 0.4222 0.0005  -0.0037 -0.0537 221 ASP A CA  
1676 C  C   . ASP A 245 ? 0.4046 0.3561 0.4267 0.0007  -0.0030 -0.0560 221 ASP A C   
1677 O  O   . ASP A 245 ? 0.3946 0.3447 0.4195 0.0022  -0.0030 -0.0635 221 ASP A O   
1678 C  CB  . ASP A 245 ? 0.4121 0.3704 0.4227 -0.0027 -0.0055 -0.0525 221 ASP A CB  
1679 C  CG  . ASP A 245 ? 0.4488 0.4134 0.4506 -0.0024 -0.0064 -0.0522 221 ASP A CG  
1680 O  OD1 . ASP A 245 ? 0.4412 0.4104 0.4381 0.0002  -0.0057 -0.0538 221 ASP A OD1 
1681 O  OD2 . ASP A 245 ? 0.4743 0.4394 0.4746 -0.0045 -0.0073 -0.0499 221 ASP A OD2 
1682 N  N   . ARG A 246 ? 0.3956 0.3430 0.4233 -0.0007 -0.0024 -0.0497 222 ARG A N   
1683 C  CA  . ARG A 246 ? 0.4178 0.3583 0.4564 -0.0007 -0.0016 -0.0505 222 ARG A CA  
1684 C  C   . ARG A 246 ? 0.3947 0.3337 0.4372 0.0033  0.0003  -0.0526 222 ARG A C   
1685 O  O   . ARG A 246 ? 0.3959 0.3294 0.4463 0.0043  0.0010  -0.0579 222 ARG A O   
1686 C  CB  . ARG A 246 ? 0.4192 0.3569 0.4617 -0.0028 -0.0013 -0.0419 222 ARG A CB  
1687 C  CG  . ARG A 246 ? 0.4563 0.3871 0.5108 -0.0025 0.0000  -0.0402 222 ARG A CG  
1688 C  CD  . ARG A 246 ? 0.5041 0.4336 0.5616 -0.0049 0.0002  -0.0314 222 ARG A CD  
1689 N  NE  . ARG A 246 ? 0.4513 0.3856 0.5013 -0.0044 0.0001  -0.0244 222 ARG A NE  
1690 C  CZ  . ARG A 246 ? 0.4814 0.4166 0.5336 -0.0022 0.0008  -0.0192 222 ARG A CZ  
1691 N  NH1 . ARG A 246 ? 0.4924 0.4235 0.5539 0.0004  0.0022  -0.0197 222 ARG A NH1 
1692 N  NH2 . ARG A 246 ? 0.4885 0.4287 0.5337 -0.0025 0.0000  -0.0136 222 ARG A NH2 
1693 N  N   . LEU A 247 ? 0.3957 0.3396 0.4337 0.0056  0.0014  -0.0488 223 LEU A N   
1694 C  CA  . LEU A 247 ? 0.4170 0.3603 0.4599 0.0098  0.0037  -0.0496 223 LEU A CA  
1695 C  C   . LEU A 247 ? 0.4202 0.3663 0.4591 0.0130  0.0048  -0.0584 223 LEU A C   
1696 O  O   . LEU A 247 ? 0.4423 0.3855 0.4870 0.0165  0.0069  -0.0625 223 LEU A O   
1697 C  CB  . LEU A 247 ? 0.3916 0.3398 0.4327 0.0109  0.0044  -0.0412 223 LEU A CB  
1698 C  CG  . LEU A 247 ? 0.4127 0.3593 0.4571 0.0085  0.0034  -0.0322 223 LEU A CG  
1699 C  CD1 . LEU A 247 ? 0.3317 0.2841 0.3751 0.0098  0.0037  -0.0253 223 LEU A CD1 
1700 C  CD2 . LEU A 247 ? 0.4399 0.3790 0.4954 0.0088  0.0043  -0.0311 223 LEU A CD2 
1701 N  N   . PHE A 248 ? 0.3770 0.3290 0.4062 0.0122  0.0035  -0.0613 224 PHE A N   
1702 C  CA  . PHE A 248 ? 0.4272 0.3842 0.4508 0.0156  0.0047  -0.0684 224 PHE A CA  
1703 C  C   . PHE A 248 ? 0.4374 0.3957 0.4558 0.0141  0.0024  -0.0765 224 PHE A C   
1704 O  O   . PHE A 248 ? 0.4672 0.4299 0.4801 0.0171  0.0031  -0.0832 224 PHE A O   
1705 C  CB  . PHE A 248 ? 0.4069 0.3725 0.4230 0.0171  0.0059  -0.0632 224 PHE A CB  
1706 C  CG  . PHE A 248 ? 0.3618 0.3279 0.3829 0.0182  0.0076  -0.0551 224 PHE A CG  
1707 C  CD1 . PHE A 248 ? 0.4061 0.3718 0.4334 0.0224  0.0105  -0.0562 224 PHE A CD1 
1708 C  CD2 . PHE A 248 ? 0.3496 0.3170 0.3695 0.0150  0.0061  -0.0468 224 PHE A CD2 
1709 C  CE1 . PHE A 248 ? 0.4190 0.3864 0.4518 0.0234  0.0117  -0.0483 224 PHE A CE1 
1710 C  CE2 . PHE A 248 ? 0.3855 0.3544 0.4100 0.0157  0.0069  -0.0396 224 PHE A CE2 
1711 C  CZ  . PHE A 248 ? 0.3800 0.3493 0.4113 0.0198  0.0096  -0.0400 224 PHE A CZ  
1712 N  N   . GLY A 249 ? 0.4255 0.3809 0.4453 0.0099  -0.0004 -0.0758 225 GLY A N   
1713 C  CA  . GLY A 249 ? 0.4883 0.4454 0.5051 0.0084  -0.0030 -0.0836 225 GLY A CA  
1714 C  C   . GLY A 249 ? 0.5155 0.4822 0.5207 0.0101  -0.0036 -0.0850 225 GLY A C   
1715 O  O   . GLY A 249 ? 0.5202 0.4916 0.5199 0.0097  -0.0033 -0.0778 225 GLY A O   
1716 N  N   . GLN A 250 ? 0.5137 0.4836 0.5152 0.0120  -0.0044 -0.0943 226 GLN A N   
1717 C  CA  . GLN A 250 ? 0.5826 0.5626 0.5727 0.0140  -0.0050 -0.0961 226 GLN A CA  
1718 C  C   . GLN A 250 ? 0.5553 0.5406 0.5403 0.0189  -0.0012 -0.0952 226 GLN A C   
1719 O  O   . GLN A 250 ? 0.5755 0.5700 0.5510 0.0211  -0.0009 -0.0951 226 GLN A O   
1720 C  CB  . GLN A 250 ? 0.6365 0.6189 0.6242 0.0136  -0.0082 -0.1068 226 GLN A CB  
1721 C  CG  . GLN A 250 ? 0.7404 0.7201 0.7334 0.0086  -0.0122 -0.1077 226 GLN A CG  
1722 C  CD  . GLN A 250 ? 0.8657 0.8531 0.8521 0.0073  -0.0142 -0.1022 226 GLN A CD  
1723 O  OE1 . GLN A 250 ? 0.9658 0.9624 0.9425 0.0098  -0.0147 -0.1031 226 GLN A OE1 
1724 N  NE2 . GLN A 250 ? 0.8834 0.8674 0.8751 0.0036  -0.0152 -0.0960 226 GLN A NE2 
1725 N  N   . ASP A 251 ? 0.5177 0.4980 0.5092 0.0209  0.0019  -0.0939 227 ASP A N   
1726 C  CA  . ASP A 251 ? 0.5087 0.4940 0.4971 0.0260  0.0059  -0.0941 227 ASP A CA  
1727 C  C   . ASP A 251 ? 0.5082 0.4987 0.4945 0.0264  0.0079  -0.0831 227 ASP A C   
1728 O  O   . ASP A 251 ? 0.4802 0.4731 0.4686 0.0298  0.0115  -0.0806 227 ASP A O   
1729 C  CB  . ASP A 251 ? 0.5359 0.5137 0.5335 0.0286  0.0084  -0.0983 227 ASP A CB  
1730 C  CG  . ASP A 251 ? 0.5751 0.5581 0.5689 0.0347  0.0124  -0.1033 227 ASP A CG  
1731 O  OD1 . ASP A 251 ? 0.5855 0.5778 0.5687 0.0367  0.0127  -0.1059 227 ASP A OD1 
1732 O  OD2 . ASP A 251 ? 0.5863 0.5645 0.5879 0.0377  0.0155  -0.1044 227 ASP A OD2 
1733 N  N   . TYR A 252 ? 0.4684 0.4609 0.4515 0.0229  0.0058  -0.0766 228 TYR A N   
1734 C  CA  . TYR A 252 ? 0.4722 0.4691 0.4538 0.0226  0.0073  -0.0668 228 TYR A CA  
1735 C  C   . TYR A 252 ? 0.4437 0.4459 0.4176 0.0208  0.0054  -0.0634 228 TYR A C   
1736 O  O   . TYR A 252 ? 0.4314 0.4328 0.4029 0.0189  0.0025  -0.0670 228 TYR A O   
1737 C  CB  . TYR A 252 ? 0.4195 0.4098 0.4091 0.0197  0.0069  -0.0601 228 TYR A CB  
1738 C  CG  . TYR A 252 ? 0.4063 0.3925 0.3959 0.0150  0.0038  -0.0565 228 TYR A CG  
1739 C  CD1 . TYR A 252 ? 0.4325 0.4127 0.4252 0.0127  0.0014  -0.0609 228 TYR A CD1 
1740 C  CD2 . TYR A 252 ? 0.4160 0.4042 0.4033 0.0128  0.0033  -0.0488 228 TYR A CD2 
1741 C  CE1 . TYR A 252 ? 0.4104 0.3878 0.4033 0.0088  -0.0008 -0.0574 228 TYR A CE1 
1742 C  CE2 . TYR A 252 ? 0.4191 0.4035 0.4060 0.0090  0.0010  -0.0460 228 TYR A CE2 
1743 C  CZ  . TYR A 252 ? 0.4515 0.4309 0.4411 0.0072  -0.0009 -0.0501 228 TYR A CZ  
1744 O  OH  . TYR A 252 ? 0.4472 0.4236 0.4365 0.0039  -0.0027 -0.0471 228 TYR A OH  
1745 N  N   . ARG A 253 ? 0.4335 0.4416 0.4046 0.0215  0.0073  -0.0562 229 ARG A N   
1746 C  CA  . ARG A 253 ? 0.4194 0.4317 0.3851 0.0198  0.0062  -0.0509 229 ARG A CA  
1747 C  C   . ARG A 253 ? 0.4092 0.4177 0.3793 0.0165  0.0060  -0.0426 229 ARG A C   
1748 O  O   . ARG A 253 ? 0.4364 0.4452 0.4108 0.0170  0.0080  -0.0388 229 ARG A O   
1749 C  CB  . ARG A 253 ? 0.4241 0.4469 0.3829 0.0234  0.0087  -0.0492 229 ARG A CB  
1750 C  CG  . ARG A 253 ? 0.4684 0.4964 0.4218 0.0275  0.0095  -0.0578 229 ARG A CG  
1751 C  CD  . ARG A 253 ? 0.4712 0.5010 0.4189 0.0268  0.0059  -0.0630 229 ARG A CD  
1752 N  NE  . ARG A 253 ? 0.5401 0.5758 0.4818 0.0306  0.0063  -0.0719 229 ARG A NE  
1753 C  CZ  . ARG A 253 ? 0.6137 0.6445 0.5578 0.0310  0.0051  -0.0818 229 ARG A CZ  
1754 N  NH1 . ARG A 253 ? 0.5665 0.5866 0.5197 0.0278  0.0036  -0.0833 229 ARG A NH1 
1755 N  NH2 . ARG A 253 ? 0.6266 0.6633 0.5641 0.0347  0.0056  -0.0904 229 ARG A NH2 
1756 N  N   . TRP A 254 ? 0.4041 0.4094 0.3731 0.0132  0.0036  -0.0400 230 TRP A N   
1757 C  CA  . TRP A 254 ? 0.3911 0.3914 0.3635 0.0097  0.0028  -0.0339 230 TRP A CA  
1758 C  C   . TRP A 254 ? 0.3936 0.3980 0.3632 0.0091  0.0036  -0.0273 230 TRP A C   
1759 O  O   . TRP A 254 ? 0.4200 0.4279 0.3847 0.0099  0.0033  -0.0268 230 TRP A O   
1760 C  CB  . TRP A 254 ? 0.3704 0.3642 0.3438 0.0067  0.0001  -0.0355 230 TRP A CB  
1761 C  CG  . TRP A 254 ? 0.3741 0.3627 0.3501 0.0034  -0.0007 -0.0304 230 TRP A CG  
1762 C  CD1 . TRP A 254 ? 0.3693 0.3565 0.3490 0.0024  -0.0002 -0.0266 230 TRP A CD1 
1763 C  CD2 . TRP A 254 ? 0.3513 0.3359 0.3259 0.0008  -0.0024 -0.0290 230 TRP A CD2 
1764 N  NE1 . TRP A 254 ? 0.3290 0.3116 0.3089 -0.0009 -0.0016 -0.0233 230 TRP A NE1 
1765 C  CE2 . TRP A 254 ? 0.3725 0.3531 0.3492 -0.0017 -0.0027 -0.0249 230 TRP A CE2 
1766 C  CE3 . TRP A 254 ? 0.3651 0.3497 0.3370 0.0005  -0.0036 -0.0309 230 TRP A CE3 
1767 C  CZ2 . TRP A 254 ? 0.3447 0.3209 0.3201 -0.0043 -0.0038 -0.0231 230 TRP A CZ2 
1768 C  CZ3 . TRP A 254 ? 0.3783 0.3585 0.3500 -0.0019 -0.0044 -0.0286 230 TRP A CZ3 
1769 C  CH2 . TRP A 254 ? 0.3594 0.3353 0.3325 -0.0041 -0.0043 -0.0250 230 TRP A CH2 
1770 N  N   . SER A 255 ? 0.3966 0.4004 0.3700 0.0076  0.0044  -0.0219 231 SER A N   
1771 C  CA  . SER A 255 ? 0.3943 0.3995 0.3671 0.0058  0.0047  -0.0154 231 SER A CA  
1772 C  C   . SER A 255 ? 0.3802 0.3790 0.3569 0.0017  0.0029  -0.0125 231 SER A C   
1773 O  O   . SER A 255 ? 0.3538 0.3496 0.3341 0.0010  0.0021  -0.0139 231 SER A O   
1774 C  CB  . SER A 255 ? 0.3694 0.3826 0.3433 0.0078  0.0077  -0.0112 231 SER A CB  
1775 O  OG  . SER A 255 ? 0.3846 0.3989 0.3584 0.0059  0.0081  -0.0049 231 SER A OG  
1776 N  N   . VAL A 256 ? 0.3421 0.3388 0.3179 -0.0008 0.0022  -0.0086 232 VAL A N   
1777 C  CA  . VAL A 256 ? 0.3395 0.3301 0.3175 -0.0048 0.0002  -0.0067 232 VAL A CA  
1778 C  C   . VAL A 256 ? 0.3614 0.3535 0.3420 -0.0070 0.0006  -0.0012 232 VAL A C   
1779 O  O   . VAL A 256 ? 0.3276 0.3236 0.3076 -0.0058 0.0024  0.0019  232 VAL A O   
1780 C  CB  . VAL A 256 ? 0.3475 0.3316 0.3222 -0.0063 -0.0014 -0.0089 232 VAL A CB  
1781 C  CG1 . VAL A 256 ? 0.3260 0.3087 0.2997 -0.0047 -0.0020 -0.0140 232 VAL A CG1 
1782 C  CG2 . VAL A 256 ? 0.3283 0.3128 0.3001 -0.0057 -0.0007 -0.0070 232 VAL A CG2 
1783 N  N   . LEU A 257 ? 0.3242 0.3134 0.3082 -0.0104 -0.0012 0.0003  233 LEU A N   
1784 C  CA  . LEU A 257 ? 0.3647 0.3539 0.3522 -0.0137 -0.0017 0.0048  233 LEU A CA  
1785 C  C   . LEU A 257 ? 0.3812 0.3628 0.3674 -0.0176 -0.0047 0.0034  233 LEU A C   
1786 O  O   . LEU A 257 ? 0.3682 0.3486 0.3548 -0.0186 -0.0066 0.0017  233 LEU A O   
1787 C  CB  . LEU A 257 ? 0.3418 0.3378 0.3358 -0.0139 -0.0012 0.0081  233 LEU A CB  
1788 C  CG  . LEU A 257 ? 0.3929 0.3913 0.3929 -0.0175 -0.0016 0.0133  233 LEU A CG  
1789 C  CD1 . LEU A 257 ? 0.3559 0.3630 0.3626 -0.0163 -0.0003 0.0164  233 LEU A CD1 
1790 C  CD2 . LEU A 257 ? 0.3847 0.3765 0.3852 -0.0225 -0.0055 0.0125  233 LEU A CD2 
1791 N  N   . GLY A 258 ? 0.3662 0.3429 0.3509 -0.0194 -0.0049 0.0041  234 GLY A N   
1792 C  CA  . GLY A 258 ? 0.3611 0.3306 0.3442 -0.0230 -0.0075 0.0022  234 GLY A CA  
1793 C  C   . GLY A 258 ? 0.4002 0.3689 0.3882 -0.0272 -0.0088 0.0051  234 GLY A C   
1794 O  O   . GLY A 258 ? 0.3974 0.3665 0.3884 -0.0274 -0.0072 0.0086  234 GLY A O   
1795 N  N   . ALA A 259 ? 0.3954 0.3633 0.3846 -0.0306 -0.0119 0.0041  235 ALA A N   
1796 C  CA  . ALA A 259 ? 0.4311 0.3992 0.4259 -0.0352 -0.0139 0.0065  235 ALA A CA  
1797 C  C   . ALA A 259 ? 0.4342 0.3930 0.4271 -0.0381 -0.0148 0.0043  235 ALA A C   
1798 O  O   . ALA A 259 ? 0.4619 0.4143 0.4482 -0.0374 -0.0151 0.0000  235 ALA A O   
1799 C  CB  . ALA A 259 ? 0.3850 0.3565 0.3816 -0.0379 -0.0176 0.0059  235 ALA A CB  
1800 N  N   . GLY A 260 ? 0.4001 0.3582 0.3996 -0.0411 -0.0148 0.0075  236 GLY A N   
1801 C  CA  . GLY A 260 ? 0.4226 0.3710 0.4219 -0.0444 -0.0158 0.0052  236 GLY A CA  
1802 C  C   . GLY A 260 ? 0.4595 0.4013 0.4534 -0.0407 -0.0130 0.0035  236 GLY A C   
1803 O  O   . GLY A 260 ? 0.4254 0.3706 0.4195 -0.0367 -0.0097 0.0069  236 GLY A O   
1804 N  N   . ARG A 261 ? 0.4562 0.3892 0.4451 -0.0419 -0.0143 -0.0018 237 ARG A N   
1805 C  CA  . ARG A 261 ? 0.5293 0.4555 0.5142 -0.0386 -0.0116 -0.0034 237 ARG A CA  
1806 C  C   . ARG A 261 ? 0.4543 0.3840 0.4328 -0.0338 -0.0101 -0.0049 237 ARG A C   
1807 O  O   . ARG A 261 ? 0.4897 0.4155 0.4655 -0.0306 -0.0079 -0.0058 237 ARG A O   
1808 C  CB  . ARG A 261 ? 0.5860 0.5016 0.5680 -0.0412 -0.0131 -0.0091 237 ARG A CB  
1809 C  CG  . ARG A 261 ? 0.5970 0.5125 0.5720 -0.0428 -0.0161 -0.0148 237 ARG A CG  
1810 C  CD  . ARG A 261 ? 0.7102 0.6153 0.6816 -0.0450 -0.0172 -0.0210 237 ARG A CD  
1811 N  NE  . ARG A 261 ? 0.8103 0.7083 0.7804 -0.0413 -0.0135 -0.0217 237 ARG A NE  
1812 C  CZ  . ARG A 261 ? 0.8279 0.7154 0.7971 -0.0422 -0.0131 -0.0262 237 ARG A CZ  
1813 N  NH1 . ARG A 261 ? 0.7671 0.6494 0.7357 -0.0470 -0.0164 -0.0312 237 ARG A NH1 
1814 N  NH2 . ARG A 261 ? 0.8293 0.7115 0.7984 -0.0379 -0.0093 -0.0258 237 ARG A NH2 
1815 N  N   . ASN A 262 ? 0.4574 0.3942 0.4345 -0.0331 -0.0111 -0.0049 238 ASN A N   
1816 C  CA  . ASN A 262 ? 0.4610 0.4015 0.4341 -0.0288 -0.0095 -0.0057 238 ASN A CA  
1817 C  C   . ASN A 262 ? 0.4248 0.3719 0.4007 -0.0255 -0.0071 -0.0016 238 ASN A C   
1818 O  O   . ASN A 262 ? 0.4260 0.3763 0.3992 -0.0221 -0.0060 -0.0027 238 ASN A O   
1819 C  CB  . ASN A 262 ? 0.4789 0.4235 0.4499 -0.0292 -0.0114 -0.0075 238 ASN A CB  
1820 C  CG  . ASN A 262 ? 0.5356 0.4758 0.5030 -0.0325 -0.0141 -0.0110 238 ASN A CG  
1821 O  OD1 . ASN A 262 ? 0.5346 0.4693 0.4967 -0.0319 -0.0136 -0.0145 238 ASN A OD1 
1822 N  ND2 . ASN A 262 ? 0.5495 0.4930 0.5196 -0.0358 -0.0170 -0.0100 238 ASN A ND2 
1823 N  N   . GLN A 263 ? 0.3782 0.3279 0.3596 -0.0266 -0.0064 0.0029  239 GLN A N   
1824 C  CA  . GLN A 263 ? 0.4038 0.3616 0.3873 -0.0234 -0.0040 0.0070  239 GLN A CA  
1825 C  C   . GLN A 263 ? 0.4075 0.3656 0.3871 -0.0191 -0.0021 0.0067  239 GLN A C   
1826 O  O   . GLN A 263 ? 0.3572 0.3209 0.3341 -0.0159 -0.0014 0.0055  239 GLN A O   
1827 C  CB  . GLN A 263 ? 0.3722 0.3318 0.3624 -0.0254 -0.0030 0.0128  239 GLN A CB  
1828 C  CG  . GLN A 263 ? 0.3557 0.3248 0.3477 -0.0220 -0.0001 0.0177  239 GLN A CG  
1829 C  CD  . GLN A 263 ? 0.3956 0.3669 0.3951 -0.0241 0.0013  0.0244  239 GLN A CD  
1830 O  OE1 . GLN A 263 ? 0.4006 0.3665 0.4026 -0.0250 0.0022  0.0273  239 GLN A OE1 
1831 N  NE2 . GLN A 263 ? 0.4047 0.3839 0.4089 -0.0249 0.0018  0.0273  239 GLN A NE2 
1832 N  N   . LEU A 264 ? 0.3764 0.3285 0.3561 -0.0189 -0.0012 0.0076  240 LEU A N   
1833 C  CA  . LEU A 264 ? 0.4035 0.3572 0.3806 -0.0147 0.0005  0.0085  240 LEU A CA  
1834 C  C   . LEU A 264 ? 0.4051 0.3573 0.3774 -0.0131 -0.0003 0.0031  240 LEU A C   
1835 O  O   . LEU A 264 ? 0.4053 0.3626 0.3753 -0.0097 0.0002  0.0026  240 LEU A O   
1836 C  CB  . LEU A 264 ? 0.4282 0.3760 0.4082 -0.0145 0.0019  0.0120  240 LEU A CB  
1837 C  CG  . LEU A 264 ? 0.4554 0.4060 0.4414 -0.0154 0.0034  0.0190  240 LEU A CG  
1838 C  CD1 . LEU A 264 ? 0.4339 0.3771 0.4238 -0.0153 0.0049  0.0227  240 LEU A CD1 
1839 C  CD2 . LEU A 264 ? 0.3926 0.3547 0.3772 -0.0117 0.0050  0.0230  240 LEU A CD2 
1840 N  N   . ASN A 265 ? 0.3768 0.3224 0.3474 -0.0155 -0.0017 -0.0010 241 ASN A N   
1841 C  CA  . ASN A 265 ? 0.4190 0.3638 0.3856 -0.0142 -0.0021 -0.0053 241 ASN A CA  
1842 C  C   . ASN A 265 ? 0.4015 0.3536 0.3674 -0.0129 -0.0026 -0.0065 241 ASN A C   
1843 O  O   . ASN A 265 ? 0.4115 0.3664 0.3760 -0.0103 -0.0023 -0.0081 241 ASN A O   
1844 C  CB  . ASN A 265 ? 0.4387 0.3769 0.4031 -0.0171 -0.0034 -0.0090 241 ASN A CB  
1845 C  CG  . ASN A 265 ? 0.4725 0.4024 0.4365 -0.0175 -0.0025 -0.0100 241 ASN A CG  
1846 O  OD1 . ASN A 265 ? 0.4447 0.3734 0.4101 -0.0150 -0.0007 -0.0081 241 ASN A OD1 
1847 N  ND2 . ASN A 265 ? 0.4897 0.4139 0.4515 -0.0206 -0.0039 -0.0133 241 ASN A ND2 
1848 N  N   . ILE A 266 ? 0.3971 0.3521 0.3647 -0.0146 -0.0035 -0.0058 242 ILE A N   
1849 C  CA  . ILE A 266 ? 0.3649 0.3253 0.3324 -0.0133 -0.0038 -0.0074 242 ILE A CA  
1850 C  C   . ILE A 266 ? 0.3754 0.3429 0.3433 -0.0100 -0.0025 -0.0060 242 ILE A C   
1851 O  O   . ILE A 266 ? 0.3547 0.3256 0.3215 -0.0080 -0.0026 -0.0088 242 ILE A O   
1852 C  CB  . ILE A 266 ? 0.4187 0.3803 0.3885 -0.0157 -0.0051 -0.0068 242 ILE A CB  
1853 C  CG1 . ILE A 266 ? 0.4146 0.3706 0.3824 -0.0183 -0.0068 -0.0090 242 ILE A CG1 
1854 C  CG2 . ILE A 266 ? 0.3781 0.3456 0.3494 -0.0137 -0.0048 -0.0076 242 ILE A CG2 
1855 C  CD1 . ILE A 266 ? 0.4283 0.3860 0.3979 -0.0206 -0.0087 -0.0085 242 ILE A CD1 
1856 N  N   . ALA A 267 ? 0.3335 0.3034 0.3028 -0.0095 -0.0013 -0.0018 243 ALA A N   
1857 C  CA  . ALA A 267 ? 0.3640 0.3413 0.3322 -0.0060 0.0001  -0.0002 243 ALA A CA  
1858 C  C   . ALA A 267 ? 0.3781 0.3559 0.3434 -0.0036 -0.0002 -0.0024 243 ALA A C   
1859 O  O   . ALA A 267 ? 0.3510 0.3349 0.3143 -0.0010 -0.0003 -0.0045 243 ALA A O   
1860 C  CB  . ALA A 267 ? 0.3450 0.3244 0.3154 -0.0060 0.0018  0.0060  243 ALA A CB  
1861 N  N   . ALA A 268 ? 0.3903 0.3619 0.3556 -0.0043 -0.0004 -0.0023 244 ALA A N   
1862 C  CA  . ALA A 268 ? 0.3478 0.3206 0.3115 -0.0019 -0.0007 -0.0036 244 ALA A CA  
1863 C  C   . ALA A 268 ? 0.3705 0.3441 0.3334 -0.0020 -0.0020 -0.0090 244 ALA A C   
1864 O  O   . ALA A 268 ? 0.3604 0.3396 0.3226 0.0002  -0.0027 -0.0109 244 ALA A O   
1865 C  CB  . ALA A 268 ? 0.3443 0.3100 0.3090 -0.0023 0.0000  -0.0022 244 ALA A CB  
1866 N  N   . MET A 269 ? 0.3601 0.3287 0.3236 -0.0045 -0.0025 -0.0114 245 MET A N   
1867 C  CA  . MET A 269 ? 0.3775 0.3467 0.3414 -0.0048 -0.0034 -0.0155 245 MET A CA  
1868 C  C   . MET A 269 ? 0.3721 0.3477 0.3362 -0.0032 -0.0039 -0.0175 245 MET A C   
1869 O  O   . MET A 269 ? 0.3896 0.3682 0.3542 -0.0021 -0.0048 -0.0208 245 MET A O   
1870 C  CB  . MET A 269 ? 0.3696 0.3336 0.3340 -0.0075 -0.0038 -0.0163 245 MET A CB  
1871 C  CG  . MET A 269 ? 0.3968 0.3544 0.3598 -0.0090 -0.0034 -0.0158 245 MET A CG  
1872 S  SD  . MET A 269 ? 0.4780 0.4317 0.4402 -0.0119 -0.0042 -0.0170 245 MET A SD  
1873 C  CE  . MET A 269 ? 0.4259 0.3818 0.3900 -0.0110 -0.0042 -0.0194 245 MET A CE  
1874 N  N   . SER A 270 ? 0.3167 0.2948 0.2809 -0.0031 -0.0033 -0.0159 246 SER A N   
1875 C  CA  . SER A 270 ? 0.3770 0.3611 0.3411 -0.0011 -0.0032 -0.0183 246 SER A CA  
1876 C  C   . SER A 270 ? 0.3447 0.3354 0.3061 0.0017  -0.0034 -0.0191 246 SER A C   
1877 O  O   . SER A 270 ? 0.3579 0.3519 0.3188 0.0029  -0.0045 -0.0237 246 SER A O   
1878 C  CB  . SER A 270 ? 0.3425 0.3289 0.3075 -0.0011 -0.0019 -0.0156 246 SER A CB  
1879 O  OG  . SER A 270 ? 0.3441 0.3368 0.3084 0.0016  -0.0012 -0.0181 246 SER A OG  
1880 N  N   . ALA A 271 ? 0.3435 0.3362 0.3032 0.0028  -0.0026 -0.0144 247 ALA A N   
1881 C  CA  . ALA A 271 ? 0.3781 0.3784 0.3350 0.0058  -0.0030 -0.0139 247 ALA A CA  
1882 C  C   . ALA A 271 ? 0.3751 0.3754 0.3324 0.0059  -0.0051 -0.0177 247 ALA A C   
1883 O  O   . ALA A 271 ? 0.3974 0.4048 0.3528 0.0078  -0.0066 -0.0206 247 ALA A O   
1884 C  CB  . ALA A 271 ? 0.3023 0.3036 0.2587 0.0068  -0.0016 -0.0070 247 ALA A CB  
1885 N  N   . ALA A 272 ? 0.3556 0.3490 0.3157 0.0038  -0.0052 -0.0177 248 ALA A N   
1886 C  CA  . ALA A 272 ? 0.3987 0.3926 0.3606 0.0038  -0.0068 -0.0206 248 ALA A CA  
1887 C  C   . ALA A 272 ? 0.4280 0.4221 0.3919 0.0026  -0.0082 -0.0266 248 ALA A C   
1888 O  O   . ALA A 272 ? 0.4068 0.4035 0.3728 0.0025  -0.0099 -0.0295 248 ALA A O   
1889 C  CB  . ALA A 272 ? 0.3620 0.3486 0.3260 0.0024  -0.0058 -0.0186 248 ALA A CB  
1890 N  N   . MET A 273 ? 0.4037 0.3954 0.3679 0.0016  -0.0076 -0.0282 249 MET A N   
1891 C  CA  . MET A 273 ? 0.3889 0.3791 0.3563 0.0004  -0.0085 -0.0334 249 MET A CA  
1892 C  C   . MET A 273 ? 0.4090 0.4043 0.3747 0.0022  -0.0089 -0.0375 249 MET A C   
1893 O  O   . MET A 273 ? 0.4604 0.4535 0.4292 0.0015  -0.0093 -0.0419 249 MET A O   
1894 C  CB  . MET A 273 ? 0.4203 0.4033 0.3902 -0.0018 -0.0074 -0.0321 249 MET A CB  
1895 C  CG  . MET A 273 ? 0.4054 0.3832 0.3764 -0.0037 -0.0070 -0.0297 249 MET A CG  
1896 S  SD  . MET A 273 ? 0.4953 0.4664 0.4672 -0.0060 -0.0059 -0.0273 249 MET A SD  
1897 C  CE  . MET A 273 ? 0.4389 0.4095 0.4155 -0.0063 -0.0064 -0.0309 249 MET A CE  
1898 N  N   . GLY A 274 ? 0.3993 0.4013 0.3603 0.0048  -0.0086 -0.0360 250 GLY A N   
1899 C  CA  . GLY A 274 ? 0.3646 0.3725 0.3226 0.0071  -0.0087 -0.0401 250 GLY A CA  
1900 C  C   . GLY A 274 ? 0.4223 0.4298 0.3797 0.0081  -0.0060 -0.0383 250 GLY A C   
1901 O  O   . GLY A 274 ? 0.4351 0.4463 0.3909 0.0102  -0.0055 -0.0426 250 GLY A O   
1902 N  N   . GLY A 275 ? 0.3743 0.3777 0.3332 0.0067  -0.0044 -0.0323 251 GLY A N   
1903 C  CA  . GLY A 275 ? 0.3770 0.3809 0.3365 0.0073  -0.0021 -0.0297 251 GLY A CA  
1904 C  C   . GLY A 275 ? 0.3778 0.3872 0.3342 0.0088  -0.0003 -0.0237 251 GLY A C   
1905 O  O   . GLY A 275 ? 0.3680 0.3812 0.3212 0.0099  -0.0008 -0.0214 251 GLY A O   
1906 N  N   . HIS A 276 ? 0.4053 0.4156 0.3637 0.0089  0.0018  -0.0205 252 HIS A N   
1907 C  CA  . HIS A 276 ? 0.3479 0.3637 0.3051 0.0101  0.0041  -0.0140 252 HIS A CA  
1908 C  C   . HIS A 276 ? 0.3527 0.3629 0.3147 0.0066  0.0044  -0.0085 252 HIS A C   
1909 O  O   . HIS A 276 ? 0.3383 0.3416 0.3035 0.0039  0.0030  -0.0102 252 HIS A O   
1910 C  CB  . HIS A 276 ? 0.3520 0.3756 0.3077 0.0135  0.0067  -0.0152 252 HIS A CB  
1911 C  CG  . HIS A 276 ? 0.3750 0.4033 0.3256 0.0166  0.0059  -0.0224 252 HIS A CG  
1912 N  ND1 . HIS A 276 ? 0.3785 0.4140 0.3229 0.0190  0.0055  -0.0223 252 HIS A ND1 
1913 C  CD2 . HIS A 276 ? 0.3833 0.4099 0.3346 0.0175  0.0053  -0.0302 252 HIS A CD2 
1914 C  CE1 . HIS A 276 ? 0.3820 0.4205 0.3228 0.0211  0.0042  -0.0303 252 HIS A CE1 
1915 N  NE2 . HIS A 276 ? 0.3833 0.4159 0.3285 0.0201  0.0042  -0.0354 252 HIS A NE2 
1916 N  N   . VAL A 277 ? 0.3282 0.3415 0.2909 0.0066  0.0062  -0.0018 253 VAL A N   
1917 C  CA  . VAL A 277 ? 0.3444 0.3517 0.3116 0.0028  0.0059  0.0029  253 VAL A CA  
1918 C  C   . VAL A 277 ? 0.3365 0.3486 0.3079 0.0024  0.0083  0.0087  253 VAL A C   
1919 O  O   . VAL A 277 ? 0.3559 0.3767 0.3258 0.0055  0.0109  0.0114  253 VAL A O   
1920 C  CB  . VAL A 277 ? 0.3613 0.3648 0.3274 0.0020  0.0053  0.0060  253 VAL A CB  
1921 C  CG1 . VAL A 277 ? 0.3498 0.3508 0.3124 0.0030  0.0033  0.0009  253 VAL A CG1 
1922 C  CG2 . VAL A 277 ? 0.3598 0.3705 0.3249 0.0045  0.0076  0.0122  253 VAL A CG2 
1923 N  N   . ARG A 278 ? 0.3327 0.3399 0.3096 -0.0016 0.0073  0.0107  254 ARG A N   
1924 C  CA  . ARG A 278 ? 0.3687 0.3796 0.3515 -0.0032 0.0089  0.0168  254 ARG A CA  
1925 C  C   . ARG A 278 ? 0.3745 0.3783 0.3610 -0.0076 0.0076  0.0205  254 ARG A C   
1926 O  O   . ARG A 278 ? 0.3577 0.3532 0.3437 -0.0104 0.0049  0.0171  254 ARG A O   
1927 C  CB  . ARG A 278 ? 0.3636 0.3765 0.3510 -0.0041 0.0086  0.0155  254 ARG A CB  
1928 C  CG  . ARG A 278 ? 0.3617 0.3770 0.3571 -0.0074 0.0091  0.0216  254 ARG A CG  
1929 C  CD  . ARG A 278 ? 0.3642 0.3845 0.3646 -0.0070 0.0094  0.0212  254 ARG A CD  
1930 N  NE  . ARG A 278 ? 0.3307 0.3506 0.3391 -0.0118 0.0076  0.0253  254 ARG A NE  
1931 C  CZ  . ARG A 278 ? 0.4209 0.4473 0.4364 -0.0120 0.0080  0.0276  254 ARG A CZ  
1932 N  NH1 . ARG A 278 ? 0.3654 0.3985 0.3810 -0.0073 0.0107  0.0264  254 ARG A NH1 
1933 N  NH2 . ARG A 278 ? 0.3407 0.3668 0.3637 -0.0170 0.0056  0.0311  254 ARG A NH2 
1934 N  N   . VAL A 279 ? 0.3244 0.3315 0.3146 -0.0080 0.0097  0.0273  255 VAL A N   
1935 C  CA  . VAL A 279 ? 0.3581 0.3584 0.3537 -0.0125 0.0088  0.0311  255 VAL A CA  
1936 C  C   . VAL A 279 ? 0.3692 0.3752 0.3733 -0.0148 0.0103  0.0373  255 VAL A C   
1937 O  O   . VAL A 279 ? 0.3485 0.3634 0.3538 -0.0127 0.0121  0.0382  255 VAL A O   
1938 C  CB  . VAL A 279 ? 0.3852 0.3825 0.3791 -0.0111 0.0100  0.0345  255 VAL A CB  
1939 C  CG1 . VAL A 279 ? 0.3708 0.3636 0.3573 -0.0088 0.0084  0.0287  255 VAL A CG1 
1940 C  CG2 . VAL A 279 ? 0.3388 0.3464 0.3324 -0.0073 0.0137  0.0412  255 VAL A CG2 
1941 N  N   . GLY A 280 ? 0.3807 0.3816 0.3915 -0.0192 0.0097  0.0415  256 GLY A N   
1942 C  CA  . GLY A 280 ? 0.3806 0.3872 0.4010 -0.0219 0.0112  0.0482  256 GLY A CA  
1943 C  C   . GLY A 280 ? 0.3739 0.3743 0.4019 -0.0286 0.0077  0.0475  256 GLY A C   
1944 O  O   . GLY A 280 ? 0.3599 0.3534 0.3847 -0.0307 0.0039  0.0409  256 GLY A O   
1945 N  N   . LEU A 281 ? 0.3760 0.3792 0.4143 -0.0320 0.0088  0.0545  257 LEU A N   
1946 C  CA  . LEU A 281 ? 0.3958 0.3937 0.4425 -0.0390 0.0051  0.0538  257 LEU A CA  
1947 C  C   . LEU A 281 ? 0.3696 0.3732 0.4187 -0.0407 0.0023  0.0510  257 LEU A C   
1948 O  O   . LEU A 281 ? 0.3683 0.3679 0.4224 -0.0465 -0.0019 0.0488  257 LEU A O   
1949 C  CB  . LEU A 281 ? 0.3949 0.3946 0.4535 -0.0426 0.0072  0.0626  257 LEU A CB  
1950 C  CG  . LEU A 281 ? 0.4183 0.4071 0.4782 -0.0440 0.0078  0.0644  257 LEU A CG  
1951 C  CD1 . LEU A 281 ? 0.4306 0.4183 0.4801 -0.0374 0.0105  0.0641  257 LEU A CD1 
1952 C  CD2 . LEU A 281 ? 0.4099 0.4015 0.4830 -0.0473 0.0104  0.0744  257 LEU A CD2 
1953 N  N   . GLU A 282 ? 0.3450 0.3579 0.3906 -0.0358 0.0045  0.0507  258 GLU A N   
1954 C  CA  . GLU A 282 ? 0.3813 0.3985 0.4285 -0.0365 0.0018  0.0476  258 GLU A CA  
1955 C  C   . GLU A 282 ? 0.3583 0.3660 0.3983 -0.0381 -0.0029 0.0396  258 GLU A C   
1956 O  O   . GLU A 282 ? 0.3693 0.3781 0.4122 -0.0411 -0.0067 0.0376  258 GLU A O   
1957 C  CB  . GLU A 282 ? 0.3530 0.3801 0.3971 -0.0300 0.0054  0.0479  258 GLU A CB  
1958 C  CG  . GLU A 282 ? 0.3812 0.4112 0.4255 -0.0293 0.0029  0.0439  258 GLU A CG  
1959 C  CD  . GLU A 282 ? 0.3645 0.4055 0.4101 -0.0235 0.0071  0.0456  258 GLU A CD  
1960 O  OE1 . GLU A 282 ? 0.3674 0.4149 0.4136 -0.0205 0.0119  0.0500  258 GLU A OE1 
1961 O  OE2 . GLU A 282 ? 0.3506 0.3937 0.3962 -0.0217 0.0059  0.0426  258 GLU A OE2 
1962 N  N   . ASP A 283 ? 0.3902 0.3895 0.4212 -0.0361 -0.0026 0.0355  259 ASP A N   
1963 C  CA  . ASP A 283 ? 0.3868 0.3784 0.4101 -0.0364 -0.0060 0.0283  259 ASP A CA  
1964 C  C   . ASP A 283 ? 0.4031 0.3832 0.4242 -0.0401 -0.0083 0.0253  259 ASP A C   
1965 O  O   . ASP A 283 ? 0.3960 0.3704 0.4123 -0.0418 -0.0116 0.0198  259 ASP A O   
1966 C  CB  . ASP A 283 ? 0.3447 0.3363 0.3589 -0.0305 -0.0037 0.0250  259 ASP A CB  
1967 C  CG  . ASP A 283 ? 0.3895 0.3913 0.4049 -0.0261 -0.0010 0.0266  259 ASP A CG  
1968 O  OD1 . ASP A 283 ? 0.4136 0.4213 0.4351 -0.0274 -0.0020 0.0284  259 ASP A OD1 
1969 O  OD2 . ASP A 283 ? 0.4070 0.4113 0.4174 -0.0213 0.0019  0.0260  259 ASP A OD2 
1970 N  N   . ASN A 284 ? 0.3521 0.3286 0.3766 -0.0411 -0.0063 0.0290  260 ASN A N   
1971 C  CA  . ASN A 284 ? 0.3902 0.3548 0.4129 -0.0437 -0.0078 0.0258  260 ASN A CA  
1972 C  C   . ASN A 284 ? 0.3955 0.3581 0.4275 -0.0467 -0.0063 0.0318  260 ASN A C   
1973 O  O   . ASN A 284 ? 0.3856 0.3533 0.4199 -0.0435 -0.0022 0.0382  260 ASN A O   
1974 C  CB  . ASN A 284 ? 0.3893 0.3490 0.4027 -0.0388 -0.0059 0.0227  260 ASN A CB  
1975 C  CG  . ASN A 284 ? 0.4121 0.3596 0.4240 -0.0406 -0.0066 0.0197  260 ASN A CG  
1976 O  OD1 . ASN A 284 ? 0.4018 0.3430 0.4161 -0.0455 -0.0097 0.0165  260 ASN A OD1 
1977 N  ND2 . ASN A 284 ? 0.3966 0.3413 0.4047 -0.0364 -0.0039 0.0204  260 ASN A ND2 
1978 N  N   . LEU A 285 ? 0.3840 0.3395 0.4214 -0.0527 -0.0095 0.0299  261 LEU A N   
1979 C  CA  . LEU A 285 ? 0.4264 0.3785 0.4744 -0.0565 -0.0084 0.0354  261 LEU A CA  
1980 C  C   . LEU A 285 ? 0.4443 0.3842 0.4903 -0.0555 -0.0068 0.0343  261 LEU A C   
1981 O  O   . LEU A 285 ? 0.4137 0.3497 0.4690 -0.0579 -0.0052 0.0396  261 LEU A O   
1982 C  CB  . LEU A 285 ? 0.4324 0.3828 0.4886 -0.0642 -0.0131 0.0335  261 LEU A CB  
1983 C  CG  . LEU A 285 ? 0.4190 0.3823 0.4800 -0.0657 -0.0148 0.0359  261 LEU A CG  
1984 C  CD1 . LEU A 285 ? 0.4334 0.3950 0.5014 -0.0734 -0.0206 0.0327  261 LEU A CD1 
1985 C  CD2 . LEU A 285 ? 0.4056 0.3796 0.4752 -0.0637 -0.0101 0.0458  261 LEU A CD2 
1986 N  N   . TRP A 286 ? 0.4096 0.3438 0.4450 -0.0518 -0.0069 0.0283  262 TRP A N   
1987 C  CA  . TRP A 286 ? 0.4819 0.4038 0.5155 -0.0510 -0.0059 0.0258  262 TRP A CA  
1988 C  C   . TRP A 286 ? 0.4973 0.4214 0.5271 -0.0443 -0.0016 0.0301  262 TRP A C   
1989 O  O   . TRP A 286 ? 0.5069 0.4399 0.5305 -0.0398 -0.0004 0.0308  262 TRP A O   
1990 C  CB  . TRP A 286 ? 0.5000 0.4140 0.5249 -0.0518 -0.0091 0.0158  262 TRP A CB  
1991 C  CG  . TRP A 286 ? 0.5356 0.4474 0.5636 -0.0585 -0.0139 0.0112  262 TRP A CG  
1992 C  CD1 . TRP A 286 ? 0.4993 0.4194 0.5258 -0.0606 -0.0172 0.0094  262 TRP A CD1 
1993 C  CD2 . TRP A 286 ? 0.5060 0.4072 0.5399 -0.0642 -0.0161 0.0080  262 TRP A CD2 
1994 N  NE1 . TRP A 286 ? 0.5331 0.4494 0.5636 -0.0672 -0.0217 0.0054  262 TRP A NE1 
1995 C  CE2 . TRP A 286 ? 0.5644 0.4687 0.5994 -0.0698 -0.0213 0.0040  262 TRP A CE2 
1996 C  CE3 . TRP A 286 ? 0.5550 0.4440 0.5938 -0.0650 -0.0144 0.0080  262 TRP A CE3 
1997 C  CZ2 . TRP A 286 ? 0.5636 0.4596 0.6037 -0.0765 -0.0251 -0.0008 262 TRP A CZ2 
1998 C  CZ3 . TRP A 286 ? 0.5820 0.4615 0.6264 -0.0715 -0.0178 0.0031  262 TRP A CZ3 
1999 C  CH2 . TRP A 286 ? 0.5803 0.4635 0.6251 -0.0774 -0.0233 -0.0016 262 TRP A CH2 
2000 N  N   . ALA A 287 ? 0.5162 0.4319 0.5502 -0.0437 0.0006  0.0331  263 ALA A N   
2001 C  CA  . ALA A 287 ? 0.5558 0.4720 0.5862 -0.0373 0.0041  0.0367  263 ALA A CA  
2002 C  C   . ALA A 287 ? 0.6100 0.5151 0.6350 -0.0354 0.0038  0.0302  263 ALA A C   
2003 O  O   . ALA A 287 ? 0.6847 0.5917 0.7048 -0.0298 0.0059  0.0314  263 ALA A O   
2004 C  CB  . ALA A 287 ? 0.5436 0.4600 0.5836 -0.0369 0.0075  0.0470  263 ALA A CB  
2005 N  N   . GLY A 288 ? 0.6168 0.5110 0.6425 -0.0397 0.0013  0.0232  264 GLY A N   
2006 C  CA  . GLY A 288 ? 0.6628 0.5464 0.6835 -0.0377 0.0016  0.0167  264 GLY A CA  
2007 C  C   . GLY A 288 ? 0.7200 0.5935 0.7409 -0.0433 -0.0017 0.0084  264 GLY A C   
2008 O  O   . GLY A 288 ? 0.7034 0.5800 0.7265 -0.0485 -0.0050 0.0069  264 GLY A O   
2009 N  N   . LYS A 289 ? 0.7512 0.6130 0.7697 -0.0419 -0.0009 0.0027  265 LYS A N   
2010 C  CA  . LYS A 289 ? 0.7667 0.6181 0.7839 -0.0468 -0.0040 -0.0064 265 LYS A CA  
2011 C  C   . LYS A 289 ? 0.7462 0.5901 0.7757 -0.0526 -0.0049 -0.0041 265 LYS A C   
2012 O  O   . LYS A 289 ? 0.7567 0.5943 0.7947 -0.0512 -0.0017 0.0015  265 LYS A O   
2013 C  CB  . LYS A 289 ? 0.8219 0.6631 0.8331 -0.0431 -0.0021 -0.0133 265 LYS A CB  
2014 C  CG  . LYS A 289 ? 0.9003 0.7312 0.9079 -0.0475 -0.0051 -0.0241 265 LYS A CG  
2015 C  CD  . LYS A 289 ? 1.0304 0.8514 1.0320 -0.0430 -0.0024 -0.0308 265 LYS A CD  
2016 C  CE  . LYS A 289 ? 1.0920 0.9213 1.0822 -0.0380 -0.0013 -0.0328 265 LYS A CE  
2017 N  NZ  . LYS A 289 ? 1.1093 0.9447 1.0907 -0.0414 -0.0054 -0.0386 265 LYS A NZ  
2018 N  N   . GLY A 290 ? 0.7086 0.5535 0.7398 -0.0593 -0.0094 -0.0082 266 GLY A N   
2019 C  CA  . GLY A 290 ? 0.6781 0.5164 0.7220 -0.0659 -0.0110 -0.0066 266 GLY A CA  
2020 C  C   . GLY A 290 ? 0.6454 0.4898 0.7012 -0.0658 -0.0081 0.0059  266 GLY A C   
2021 O  O   . GLY A 290 ? 0.6324 0.4689 0.7005 -0.0696 -0.0075 0.0093  266 GLY A O   
2022 N  N   . ARG A 291 ? 0.5867 0.4450 0.6392 -0.0616 -0.0062 0.0128  267 ARG A N   
2023 C  CA  . ARG A 291 ? 0.6280 0.4934 0.6895 -0.0600 -0.0026 0.0251  267 ARG A CA  
2024 C  C   . ARG A 291 ? 0.5431 0.4251 0.6027 -0.0598 -0.0034 0.0293  267 ARG A C   
2025 O  O   . ARG A 291 ? 0.5047 0.3945 0.5538 -0.0552 -0.0031 0.0274  267 ARG A O   
2026 C  CB  . ARG A 291 ? 0.6192 0.4836 0.6779 -0.0523 0.0022  0.0302  267 ARG A CB  
2027 C  CG  . ARG A 291 ? 0.6766 0.5386 0.7477 -0.0518 0.0060  0.0411  267 ARG A CG  
2028 C  CD  . ARG A 291 ? 0.7524 0.6230 0.8195 -0.0439 0.0102  0.0493  267 ARG A CD  
2029 N  NE  . ARG A 291 ? 0.7578 0.6269 0.8131 -0.0385 0.0102  0.0427  267 ARG A NE  
2030 C  CZ  . ARG A 291 ? 0.7950 0.6743 0.8432 -0.0321 0.0121  0.0462  267 ARG A CZ  
2031 N  NH1 . ARG A 291 ? 0.7850 0.6767 0.8350 -0.0298 0.0142  0.0557  267 ARG A NH1 
2032 N  NH2 . ARG A 291 ? 0.7889 0.6663 0.8278 -0.0279 0.0119  0.0398  267 ARG A NH2 
2033 N  N   . LEU A 292 ? 0.5062 0.3936 0.5768 -0.0648 -0.0041 0.0350  268 LEU A N   
2034 C  CA  . LEU A 292 ? 0.4849 0.3883 0.5554 -0.0640 -0.0038 0.0403  268 LEU A CA  
2035 C  C   . LEU A 292 ? 0.4916 0.4036 0.5618 -0.0576 0.0015  0.0501  268 LEU A C   
2036 O  O   . LEU A 292 ? 0.4594 0.3663 0.5351 -0.0559 0.0049  0.0563  268 LEU A O   
2037 C  CB  . LEU A 292 ? 0.4886 0.3960 0.5721 -0.0713 -0.0060 0.0439  268 LEU A CB  
2038 C  CG  . LEU A 292 ? 0.5118 0.4148 0.5964 -0.0784 -0.0123 0.0348  268 LEU A CG  
2039 C  CD1 . LEU A 292 ? 0.4760 0.3830 0.5764 -0.0858 -0.0140 0.0401  268 LEU A CD1 
2040 C  CD2 . LEU A 292 ? 0.4734 0.3846 0.5464 -0.0765 -0.0152 0.0287  268 LEU A CD2 
2041 N  N   . ALA A 293 ? 0.4534 0.3787 0.5170 -0.0538 0.0023  0.0514  269 ALA A N   
2042 C  CA  . ALA A 293 ? 0.4880 0.4236 0.5502 -0.0479 0.0069  0.0600  269 ALA A CA  
2043 C  C   . ALA A 293 ? 0.4765 0.4198 0.5512 -0.0506 0.0094  0.0704  269 ALA A C   
2044 O  O   . ALA A 293 ? 0.4328 0.3811 0.5137 -0.0553 0.0073  0.0703  269 ALA A O   
2045 C  CB  . ALA A 293 ? 0.4209 0.3672 0.4720 -0.0432 0.0068  0.0567  269 ALA A CB  
2046 N  N   . GLU A 294 ? 0.4737 0.4187 0.5526 -0.0474 0.0138  0.0800  270 GLU A N   
2047 C  CA  . GLU A 294 ? 0.4489 0.4011 0.5404 -0.0497 0.0170  0.0913  270 GLU A CA  
2048 C  C   . GLU A 294 ? 0.4321 0.4022 0.5198 -0.0450 0.0204  0.0973  270 GLU A C   
2049 O  O   . GLU A 294 ? 0.4331 0.4121 0.5305 -0.0476 0.0221  0.1043  270 GLU A O   
2050 C  CB  . GLU A 294 ? 0.4928 0.4378 0.5920 -0.0489 0.0204  0.0999  270 GLU A CB  
2051 C  CG  . GLU A 294 ? 0.5876 0.5139 0.6926 -0.0537 0.0177  0.0942  270 GLU A CG  
2052 C  CD  . GLU A 294 ? 0.7250 0.6434 0.8392 -0.0525 0.0214  0.1033  270 GLU A CD  
2053 O  OE1 . GLU A 294 ? 0.7718 0.7002 0.8895 -0.0490 0.0261  0.1155  270 GLU A OE1 
2054 O  OE2 . GLU A 294 ? 0.7780 0.6803 0.8960 -0.0549 0.0199  0.0985  270 GLU A OE2 
2055 N  N   . THR A 295 ? 0.4458 0.4215 0.5201 -0.0381 0.0214  0.0945  271 THR A N   
2056 C  CA  . THR A 295 ? 0.4283 0.4203 0.4976 -0.0331 0.0246  0.0986  271 THR A CA  
2057 C  C   . THR A 295 ? 0.4222 0.4170 0.4777 -0.0291 0.0224  0.0887  271 THR A C   
2058 O  O   . THR A 295 ? 0.4142 0.3995 0.4629 -0.0286 0.0195  0.0808  271 THR A O   
2059 C  CB  . THR A 295 ? 0.4172 0.4163 0.4853 -0.0275 0.0297  0.1090  271 THR A CB  
2060 O  OG1 . THR A 295 ? 0.4333 0.4261 0.4923 -0.0232 0.0290  0.1055  271 THR A OG1 
2061 C  CG2 . THR A 295 ? 0.4426 0.4392 0.5255 -0.0312 0.0325  0.1203  271 THR A CG2 
2062 N  N   . ASN A 296 ? 0.4348 0.4428 0.4869 -0.0262 0.0242  0.0894  272 ASN A N   
2063 C  CA  . ASN A 296 ? 0.3919 0.4036 0.4317 -0.0216 0.0229  0.0812  272 ASN A CA  
2064 C  C   . ASN A 296 ? 0.3961 0.4088 0.4261 -0.0156 0.0244  0.0814  272 ASN A C   
2065 O  O   . ASN A 296 ? 0.4131 0.4215 0.4342 -0.0135 0.0219  0.0733  272 ASN A O   
2066 C  CB  . ASN A 296 ? 0.3916 0.4171 0.4310 -0.0193 0.0252  0.0823  272 ASN A CB  
2067 C  CG  . ASN A 296 ? 0.3853 0.4100 0.4309 -0.0241 0.0221  0.0782  272 ASN A CG  
2068 O  OD1 . ASN A 296 ? 0.4030 0.4239 0.4428 -0.0241 0.0188  0.0695  272 ASN A OD1 
2069 N  ND2 . ASN A 296 ? 0.3553 0.3842 0.4132 -0.0283 0.0233  0.0851  272 ASN A ND2 
2070 N  N   . ALA A 297 ? 0.3649 0.3839 0.3968 -0.0127 0.0285  0.0913  273 ALA A N   
2071 C  CA  . ALA A 297 ? 0.4337 0.4554 0.4567 -0.0068 0.0296  0.0925  273 ALA A CA  
2072 C  C   . ALA A 297 ? 0.4538 0.4618 0.4751 -0.0078 0.0265  0.0875  273 ALA A C   
2073 O  O   . ALA A 297 ? 0.4139 0.4225 0.4260 -0.0036 0.0253  0.0831  273 ALA A O   
2074 C  CB  . ALA A 297 ? 0.3840 0.4139 0.4112 -0.0043 0.0343  0.1055  273 ALA A CB  
2075 N  N   . GLN A 298 ? 0.4307 0.4265 0.4611 -0.0132 0.0251  0.0880  274 GLN A N   
2076 C  CA  . GLN A 298 ? 0.4425 0.4246 0.4719 -0.0141 0.0225  0.0826  274 GLN A CA  
2077 C  C   . GLN A 298 ? 0.4412 0.4213 0.4606 -0.0130 0.0192  0.0711  274 GLN A C   
2078 O  O   . GLN A 298 ? 0.3916 0.3674 0.4056 -0.0101 0.0183  0.0677  274 GLN A O   
2079 C  CB  . GLN A 298 ? 0.4677 0.4375 0.5081 -0.0209 0.0212  0.0825  274 GLN A CB  
2080 C  CG  . GLN A 298 ? 0.5467 0.5013 0.5864 -0.0227 0.0185  0.0755  274 GLN A CG  
2081 C  CD  . GLN A 298 ? 0.5430 0.4862 0.5941 -0.0294 0.0174  0.0758  274 GLN A CD  
2082 O  OE1 . GLN A 298 ? 0.5102 0.4575 0.5702 -0.0333 0.0182  0.0813  274 GLN A OE1 
2083 N  NE2 . GLN A 298 ? 0.5613 0.4905 0.6126 -0.0309 0.0156  0.0699  274 GLN A NE2 
2084 N  N   . GLN A 299 ? 0.4190 0.4026 0.4367 -0.0150 0.0175  0.0657  275 GLN A N   
2085 C  CA  . GLN A 299 ? 0.3916 0.3737 0.4010 -0.0141 0.0146  0.0557  275 GLN A CA  
2086 C  C   . GLN A 299 ? 0.4022 0.3944 0.4026 -0.0081 0.0156  0.0544  275 GLN A C   
2087 O  O   . GLN A 299 ? 0.3814 0.3710 0.3751 -0.0063 0.0136  0.0477  275 GLN A O   
2088 C  CB  . GLN A 299 ? 0.3746 0.3571 0.3862 -0.0181 0.0124  0.0511  275 GLN A CB  
2089 C  CG  . GLN A 299 ? 0.3819 0.3543 0.4013 -0.0245 0.0102  0.0504  275 GLN A CG  
2090 C  CD  . GLN A 299 ? 0.4258 0.3997 0.4468 -0.0283 0.0074  0.0458  275 GLN A CD  
2091 O  OE1 . GLN A 299 ? 0.4138 0.3968 0.4323 -0.0261 0.0079  0.0450  275 GLN A OE1 
2092 N  NE2 . GLN A 299 ? 0.3962 0.3611 0.4214 -0.0338 0.0043  0.0426  275 GLN A NE2 
2093 N  N   . VAL A 300 ? 0.3615 0.3654 0.3616 -0.0052 0.0186  0.0605  276 VAL A N   
2094 C  CA  . VAL A 300 ? 0.3986 0.4126 0.3896 0.0005  0.0194  0.0590  276 VAL A CA  
2095 C  C   . VAL A 300 ? 0.4179 0.4297 0.4051 0.0036  0.0190  0.0603  276 VAL A C   
2096 O  O   . VAL A 300 ? 0.4182 0.4323 0.3981 0.0066  0.0173  0.0546  276 VAL A O   
2097 C  CB  . VAL A 300 ? 0.3881 0.4155 0.3793 0.0033  0.0233  0.0659  276 VAL A CB  
2098 C  CG1 . VAL A 300 ? 0.3557 0.3937 0.3366 0.0094  0.0240  0.0642  276 VAL A CG1 
2099 C  CG2 . VAL A 300 ? 0.3630 0.3937 0.3579 0.0009  0.0237  0.0638  276 VAL A CG2 
2100 N  N   . ARG A 301 ? 0.4060 0.4136 0.3994 0.0030  0.0206  0.0682  277 ARG A N   
2101 C  CA  . ARG A 301 ? 0.4188 0.4248 0.4101 0.0065  0.0205  0.0707  277 ARG A CA  
2102 C  C   . ARG A 301 ? 0.3980 0.3936 0.3870 0.0054  0.0173  0.0621  277 ARG A C   
2103 O  O   . ARG A 301 ? 0.4050 0.4031 0.3890 0.0091  0.0162  0.0602  277 ARG A O   
2104 C  CB  . ARG A 301 ? 0.4448 0.4467 0.4447 0.0058  0.0231  0.0813  277 ARG A CB  
2105 C  CG  . ARG A 301 ? 0.4948 0.5094 0.4958 0.0085  0.0269  0.0920  277 ARG A CG  
2106 C  CD  . ARG A 301 ? 0.5654 0.5759 0.5754 0.0086  0.0295  0.1034  277 ARG A CD  
2107 N  NE  . ARG A 301 ? 0.5976 0.5952 0.6189 0.0024  0.0296  0.1041  277 ARG A NE  
2108 C  CZ  . ARG A 301 ? 0.5801 0.5797 0.6095 -0.0012 0.0317  0.1096  277 ARG A CZ  
2109 N  NH1 . ARG A 301 ? 0.5651 0.5793 0.5926 0.0010  0.0346  0.1156  277 ARG A NH1 
2110 N  NH2 . ARG A 301 ? 0.5713 0.5585 0.6111 -0.0073 0.0308  0.1090  277 ARG A NH2 
2111 N  N   . ALA A 302 ? 0.3971 0.3820 0.3901 0.0005  0.0158  0.0571  278 ALA A N   
2112 C  CA  . ALA A 302 ? 0.4252 0.4008 0.4156 -0.0003 0.0132  0.0490  278 ALA A CA  
2113 C  C   . ALA A 302 ? 0.4405 0.4223 0.4229 0.0018  0.0113  0.0417  278 ALA A C   
2114 O  O   . ALA A 302 ? 0.4102 0.3915 0.3891 0.0042  0.0102  0.0385  278 ALA A O   
2115 C  CB  . ALA A 302 ? 0.3583 0.3227 0.3533 -0.0060 0.0119  0.0449  278 ALA A CB  
2116 N  N   . ALA A 303 ? 0.3874 0.3752 0.3679 0.0008  0.0110  0.0391  279 ALA A N   
2117 C  CA  . ALA A 303 ? 0.3629 0.3562 0.3370 0.0028  0.0094  0.0323  279 ALA A CA  
2118 C  C   . ALA A 303 ? 0.3882 0.3910 0.3571 0.0078  0.0097  0.0340  279 ALA A C   
2119 O  O   . ALA A 303 ? 0.3711 0.3750 0.3359 0.0094  0.0078  0.0285  279 ALA A O   
2120 C  CB  . ALA A 303 ? 0.3785 0.3770 0.3525 0.0016  0.0097  0.0304  279 ALA A CB  
2121 N  N   . ARG A 304 ? 0.3731 0.3835 0.3425 0.0102  0.0121  0.0419  280 ARG A N   
2122 C  CA  . ARG A 304 ? 0.4019 0.4229 0.3657 0.0151  0.0122  0.0441  280 ARG A CA  
2123 C  C   . ARG A 304 ? 0.4313 0.4483 0.3954 0.0167  0.0107  0.0445  280 ARG A C   
2124 O  O   . ARG A 304 ? 0.4363 0.4600 0.3955 0.0197  0.0088  0.0415  280 ARG A O   
2125 C  CB  . ARG A 304 ? 0.3843 0.4139 0.3490 0.0174  0.0155  0.0541  280 ARG A CB  
2126 C  CG  . ARG A 304 ? 0.4236 0.4651 0.3823 0.0227  0.0156  0.0579  280 ARG A CG  
2127 C  CD  . ARG A 304 ? 0.4612 0.5125 0.4201 0.0250  0.0193  0.0679  280 ARG A CD  
2128 N  NE  . ARG A 304 ? 0.5392 0.6045 0.4899 0.0304  0.0192  0.0704  280 ARG A NE  
2129 C  CZ  . ARG A 304 ? 0.5324 0.6108 0.4781 0.0336  0.0218  0.0745  280 ARG A CZ  
2130 N  NH1 . ARG A 304 ? 0.4805 0.5601 0.4292 0.0319  0.0251  0.0770  280 ARG A NH1 
2131 N  NH2 . ARG A 304 ? 0.5952 0.6865 0.5324 0.0386  0.0210  0.0762  280 ARG A NH2 
2132 N  N   . GLN A 305 ? 0.3900 0.3964 0.3606 0.0147  0.0115  0.0478  281 GLN A N   
2133 C  CA  . GLN A 305 ? 0.4185 0.4202 0.3905 0.0164  0.0106  0.0481  281 GLN A CA  
2134 C  C   . GLN A 305 ? 0.4663 0.4652 0.4352 0.0157  0.0078  0.0385  281 GLN A C   
2135 O  O   . GLN A 305 ? 0.4084 0.4106 0.3760 0.0185  0.0065  0.0377  281 GLN A O   
2136 C  CB  . GLN A 305 ? 0.4283 0.4175 0.4081 0.0141  0.0123  0.0522  281 GLN A CB  
2137 C  CG  . GLN A 305 ? 0.5767 0.5607 0.5594 0.0167  0.0124  0.0539  281 GLN A CG  
2138 C  CD  . GLN A 305 ? 0.6389 0.6106 0.6298 0.0148  0.0146  0.0585  281 GLN A CD  
2139 O  OE1 . GLN A 305 ? 0.7070 0.6782 0.7023 0.0133  0.0165  0.0649  281 GLN A OE1 
2140 N  NE2 . GLN A 305 ? 0.5526 0.5142 0.5460 0.0149  0.0145  0.0550  281 GLN A NE2 
2141 N  N   . ILE A 306 ? 0.3995 0.3932 0.3680 0.0120  0.0070  0.0319  282 ILE A N   
2142 C  CA  . ILE A 306 ? 0.4300 0.4215 0.3960 0.0111  0.0047  0.0236  282 ILE A CA  
2143 C  C   . ILE A 306 ? 0.4087 0.4115 0.3696 0.0136  0.0030  0.0202  282 ILE A C   
2144 O  O   . ILE A 306 ? 0.3871 0.3921 0.3468 0.0149  0.0010  0.0165  282 ILE A O   
2145 C  CB  . ILE A 306 ? 0.4091 0.3929 0.3760 0.0067  0.0043  0.0185  282 ILE A CB  
2146 C  CG1 . ILE A 306 ? 0.4039 0.3760 0.3752 0.0041  0.0052  0.0197  282 ILE A CG1 
2147 C  CG2 . ILE A 306 ? 0.3738 0.3578 0.3381 0.0062  0.0022  0.0107  282 ILE A CG2 
2148 C  CD1 . ILE A 306 ? 0.4088 0.3753 0.3814 -0.0004 0.0047  0.0170  282 ILE A CD1 
2149 N  N   . VAL A 307 ? 0.4061 0.4163 0.3642 0.0143  0.0036  0.0210  283 VAL A N   
2150 C  CA  . VAL A 307 ? 0.4177 0.4384 0.3702 0.0167  0.0021  0.0169  283 VAL A CA  
2151 C  C   . VAL A 307 ? 0.4320 0.4606 0.3824 0.0205  0.0008  0.0197  283 VAL A C   
2152 O  O   . VAL A 307 ? 0.4070 0.4399 0.3552 0.0213  -0.0020 0.0143  283 VAL A O   
2153 C  CB  . VAL A 307 ? 0.4164 0.4442 0.3661 0.0176  0.0039  0.0186  283 VAL A CB  
2154 C  CG1 . VAL A 307 ? 0.3765 0.4165 0.3195 0.0211  0.0026  0.0151  283 VAL A CG1 
2155 C  CG2 . VAL A 307 ? 0.3740 0.3957 0.3260 0.0142  0.0044  0.0145  283 VAL A CG2 
2156 N  N   . GLU A 308 ? 0.4169 0.4480 0.3686 0.0227  0.0026  0.0287  284 GLU A N   
2157 C  CA  . GLU A 308 ? 0.4598 0.5003 0.4095 0.0268  0.0014  0.0327  284 GLU A CA  
2158 C  C   . GLU A 308 ? 0.4432 0.4783 0.3972 0.0269  -0.0001 0.0318  284 GLU A C   
2159 O  O   . GLU A 308 ? 0.4402 0.4836 0.3928 0.0297  -0.0025 0.0318  284 GLU A O   
2160 C  CB  . GLU A 308 ? 0.4230 0.4682 0.3733 0.0294  0.0042  0.0437  284 GLU A CB  
2161 C  CG  . GLU A 308 ? 0.4526 0.5061 0.3981 0.0302  0.0060  0.0451  284 GLU A CG  
2162 C  CD  . GLU A 308 ? 0.4968 0.5551 0.4440 0.0324  0.0095  0.0571  284 GLU A CD  
2163 O  OE1 . GLU A 308 ? 0.4819 0.5340 0.4354 0.0326  0.0107  0.0642  284 GLU A OE1 
2164 O  OE2 . GLU A 308 ? 0.4979 0.5658 0.4404 0.0341  0.0113  0.0594  284 GLU A OE2 
2165 N  N   . GLY A 309 ? 0.4187 0.4407 0.3780 0.0240  0.0012  0.0310  285 GLY A N   
2166 C  CA  . GLY A 309 ? 0.4152 0.4320 0.3783 0.0243  0.0002  0.0290  285 GLY A CA  
2167 C  C   . GLY A 309 ? 0.4440 0.4643 0.4052 0.0233  -0.0028 0.0205  285 GLY A C   
2168 O  O   . GLY A 309 ? 0.4735 0.4969 0.4368 0.0249  -0.0044 0.0198  285 GLY A O   
2169 N  N   . LEU A 310 ? 0.4007 0.4206 0.3588 0.0206  -0.0036 0.0142  286 LEU A N   
2170 C  CA  . LEU A 310 ? 0.4318 0.4547 0.3890 0.0194  -0.0064 0.0062  286 LEU A CA  
2171 C  C   . LEU A 310 ? 0.4309 0.4672 0.3844 0.0221  -0.0093 0.0049  286 LEU A C   
2172 O  O   . LEU A 310 ? 0.4041 0.4435 0.3579 0.0210  -0.0121 -0.0017 286 LEU A O   
2173 C  CB  . LEU A 310 ? 0.3888 0.4071 0.3444 0.0162  -0.0060 0.0006  286 LEU A CB  
2174 C  CG  . LEU A 310 ? 0.3915 0.3975 0.3504 0.0128  -0.0045 -0.0008 286 LEU A CG  
2175 C  CD1 . LEU A 310 ? 0.3624 0.3655 0.3200 0.0104  -0.0038 -0.0033 286 LEU A CD1 
2176 C  CD2 . LEU A 310 ? 0.4022 0.4054 0.3639 0.0115  -0.0059 -0.0057 286 LEU A CD2 
2177 N  N   . GLY A 311 ? 0.4058 0.4505 0.3561 0.0254  -0.0089 0.0111  287 GLY A N   
2178 C  CA  . GLY A 311 ? 0.4471 0.5057 0.3922 0.0281  -0.0119 0.0096  287 GLY A CA  
2179 C  C   . GLY A 311 ? 0.4072 0.4707 0.3459 0.0278  -0.0120 0.0047  287 GLY A C   
2180 O  O   . GLY A 311 ? 0.4505 0.5251 0.3841 0.0296  -0.0149 0.0009  287 GLY A O   
2181 N  N   . LEU A 312 ? 0.3926 0.4486 0.3316 0.0259  -0.0090 0.0045  288 LEU A N   
2182 C  CA  . LEU A 312 ? 0.4479 0.5079 0.3816 0.0261  -0.0082 0.0004  288 LEU A CA  
2183 C  C   . LEU A 312 ? 0.4413 0.5074 0.3715 0.0289  -0.0050 0.0087  288 LEU A C   
2184 O  O   . LEU A 312 ? 0.4213 0.4877 0.3536 0.0304  -0.0036 0.0177  288 LEU A O   
2185 C  CB  . LEU A 312 ? 0.4369 0.4860 0.3741 0.0224  -0.0070 -0.0047 288 LEU A CB  
2186 C  CG  . LEU A 312 ? 0.4388 0.4810 0.3804 0.0194  -0.0094 -0.0116 288 LEU A CG  
2187 C  CD1 . LEU A 312 ? 0.4098 0.4413 0.3549 0.0160  -0.0076 -0.0140 288 LEU A CD1 
2188 C  CD2 . LEU A 312 ? 0.4245 0.4739 0.3633 0.0199  -0.0128 -0.0198 288 LEU A CD2 
2189 N  N   . GLU A 313 ? 0.4442 0.5153 0.3695 0.0298  -0.0036 0.0059  289 GLU A N   
2190 C  CA  . GLU A 313 ? 0.4712 0.5497 0.3931 0.0326  -0.0001 0.0136  289 GLU A CA  
2191 C  C   . GLU A 313 ? 0.4365 0.5101 0.3603 0.0309  0.0033  0.0127  289 GLU A C   
2192 O  O   . GLU A 313 ? 0.4306 0.4998 0.3550 0.0290  0.0025  0.0043  289 GLU A O   
2193 C  CB  . GLU A 313 ? 0.4718 0.5659 0.3841 0.0370  -0.0013 0.0121  289 GLU A CB  
2194 C  CG  . GLU A 313 ? 0.5257 0.6277 0.4360 0.0394  -0.0047 0.0151  289 GLU A CG  
2195 C  CD  . GLU A 313 ? 0.6089 0.7273 0.5087 0.0436  -0.0065 0.0129  289 GLU A CD  
2196 O  OE1 . GLU A 313 ? 0.7049 0.8274 0.5986 0.0446  -0.0053 0.0069  289 GLU A OE1 
2197 O  OE2 . GLU A 313 ? 0.7686 0.8962 0.6660 0.0462  -0.0091 0.0171  289 GLU A OE2 
2198 N  N   . VAL A 314 ? 0.4433 0.5180 0.3693 0.0314  0.0071  0.0220  290 VAL A N   
2199 C  CA  . VAL A 314 ? 0.4437 0.5161 0.3723 0.0300  0.0104  0.0228  290 VAL A CA  
2200 C  C   . VAL A 314 ? 0.4185 0.5028 0.3394 0.0338  0.0120  0.0192  290 VAL A C   
2201 O  O   . VAL A 314 ? 0.4537 0.5500 0.3677 0.0379  0.0125  0.0225  290 VAL A O   
2202 C  CB  . VAL A 314 ? 0.4739 0.5442 0.4085 0.0290  0.0139  0.0343  290 VAL A CB  
2203 C  CG1 . VAL A 314 ? 0.4865 0.5575 0.4241 0.0280  0.0174  0.0359  290 VAL A CG1 
2204 C  CG2 . VAL A 314 ? 0.4202 0.4772 0.3624 0.0252  0.0124  0.0359  290 VAL A CG2 
2205 N  N   . ALA A 315 ? 0.4314 0.5126 0.3533 0.0327  0.0127  0.0123  291 ALA A N   
2206 C  CA  . ALA A 315 ? 0.4449 0.5362 0.3599 0.0365  0.0147  0.0077  291 ALA A CA  
2207 C  C   . ALA A 315 ? 0.4383 0.5384 0.3528 0.0390  0.0199  0.0173  291 ALA A C   
2208 O  O   . ALA A 315 ? 0.4309 0.5262 0.3535 0.0364  0.0222  0.0250  291 ALA A O   
2209 C  CB  . ALA A 315 ? 0.4406 0.5252 0.3585 0.0350  0.0145  -0.0015 291 ALA A CB  
2210 N  N   . THR A 316 ? 0.4373 0.5509 0.3425 0.0440  0.0217  0.0166  292 THR A N   
2211 C  CA  . THR A 316 ? 0.4536 0.5773 0.3577 0.0470  0.0274  0.0246  292 THR A CA  
2212 C  C   . THR A 316 ? 0.4497 0.5719 0.3567 0.0472  0.0303  0.0193  292 THR A C   
2213 O  O   . THR A 316 ? 0.4246 0.5394 0.3326 0.0458  0.0278  0.0088  292 THR A O   
2214 C  CB  . THR A 316 ? 0.4258 0.5657 0.3177 0.0528  0.0283  0.0257  292 THR A CB  
2215 O  OG1 . THR A 316 ? 0.3910 0.5343 0.2744 0.0553  0.0264  0.0124  292 THR A OG1 
2216 C  CG2 . THR A 316 ? 0.4143 0.5566 0.3036 0.0532  0.0251  0.0315  292 THR A CG2 
2217 N  N   . PRO A 317 ? 0.4442 0.5738 0.3537 0.0489  0.0359  0.0269  293 PRO A N   
2218 C  CA  . PRO A 317 ? 0.4536 0.5837 0.3657 0.0500  0.0391  0.0220  293 PRO A CA  
2219 C  C   . PRO A 317 ? 0.4579 0.5933 0.3600 0.0546  0.0388  0.0097  293 PRO A C   
2220 O  O   . PRO A 317 ? 0.4369 0.5657 0.3422 0.0541  0.0383  0.0008  293 PRO A O   
2221 C  CB  . PRO A 317 ? 0.4692 0.6099 0.3845 0.0520  0.0455  0.0339  293 PRO A CB  
2222 C  CG  . PRO A 317 ? 0.4745 0.6129 0.3946 0.0489  0.0447  0.0455  293 PRO A CG  
2223 C  CD  . PRO A 317 ? 0.4155 0.5515 0.3279 0.0493  0.0396  0.0412  293 PRO A CD  
2224 N  N   . ALA A 318 ? 0.4349 0.5822 0.3250 0.0591  0.0389  0.0087  294 ALA A N   
2225 C  CA  . ALA A 318 ? 0.4675 0.6197 0.3473 0.0633  0.0381  -0.0042 294 ALA A CA  
2226 C  C   . ALA A 318 ? 0.4535 0.5935 0.3349 0.0599  0.0318  -0.0160 294 ALA A C   
2227 O  O   . ALA A 318 ? 0.4798 0.6166 0.3597 0.0611  0.0314  -0.0276 294 ALA A O   
2228 C  CB  . ALA A 318 ? 0.4563 0.6241 0.3223 0.0683  0.0384  -0.0026 294 ALA A CB  
2229 N  N   . GLU A 319 ? 0.4314 0.5643 0.3163 0.0557  0.0271  -0.0129 295 GLU A N   
2230 C  CA  . GLU A 319 ? 0.4514 0.5729 0.3390 0.0521  0.0214  -0.0228 295 GLU A CA  
2231 C  C   . GLU A 319 ? 0.4720 0.5802 0.3707 0.0484  0.0219  -0.0252 295 GLU A C   
2232 O  O   . GLU A 319 ? 0.4560 0.5567 0.3565 0.0472  0.0192  -0.0355 295 GLU A O   
2233 C  CB  . GLU A 319 ? 0.4553 0.5740 0.3442 0.0491  0.0170  -0.0179 295 GLU A CB  
2234 C  CG  . GLU A 319 ? 0.5063 0.6377 0.3842 0.0526  0.0147  -0.0179 295 GLU A CG  
2235 C  CD  . GLU A 319 ? 0.5276 0.6579 0.4081 0.0506  0.0117  -0.0096 295 GLU A CD  
2236 O  OE1 . GLU A 319 ? 0.4840 0.6044 0.3741 0.0469  0.0125  -0.0026 295 GLU A OE1 
2237 O  OE2 . GLU A 319 ? 0.5531 0.6926 0.4259 0.0528  0.0086  -0.0102 295 GLU A OE2 
2238 N  N   . ALA A 320 ? 0.4360 0.5416 0.3427 0.0466  0.0251  -0.0157 296 ALA A N   
2239 C  CA  . ALA A 320 ? 0.4570 0.5522 0.3738 0.0436  0.0257  -0.0173 296 ALA A CA  
2240 C  C   . ALA A 320 ? 0.4372 0.5353 0.3530 0.0474  0.0288  -0.0249 296 ALA A C   
2241 O  O   . ALA A 320 ? 0.4506 0.5396 0.3717 0.0460  0.0274  -0.0320 296 ALA A O   
2242 C  CB  . ALA A 320 ? 0.4350 0.5286 0.3604 0.0408  0.0282  -0.0055 296 ALA A CB  
2243 N  N   . ARG A 321 ? 0.4277 0.5384 0.3370 0.0526  0.0334  -0.0232 297 ARG A N   
2244 C  CA  . ARG A 321 ? 0.4660 0.5801 0.3740 0.0570  0.0371  -0.0307 297 ARG A CA  
2245 C  C   . ARG A 321 ? 0.4685 0.5779 0.3713 0.0581  0.0336  -0.0451 297 ARG A C   
2246 O  O   . ARG A 321 ? 0.4417 0.5463 0.3483 0.0597  0.0350  -0.0528 297 ARG A O   
2247 C  CB  . ARG A 321 ? 0.4363 0.5661 0.3365 0.0628  0.0429  -0.0262 297 ARG A CB  
2248 C  CG  . ARG A 321 ? 0.4418 0.5764 0.3495 0.0619  0.0473  -0.0122 297 ARG A CG  
2249 C  CD  . ARG A 321 ? 0.4553 0.6062 0.3565 0.0680  0.0539  -0.0076 297 ARG A CD  
2250 N  NE  . ARG A 321 ? 0.4963 0.6511 0.4074 0.0666  0.0584  0.0056  297 ARG A NE  
2251 C  CZ  . ARG A 321 ? 0.4869 0.6456 0.4001 0.0643  0.0589  0.0180  297 ARG A CZ  
2252 N  NH1 . ARG A 321 ? 0.4615 0.6221 0.3668 0.0641  0.0558  0.0198  297 ARG A NH1 
2253 N  NH2 . ARG A 321 ? 0.4598 0.6206 0.3841 0.0622  0.0626  0.0290  297 ARG A NH2 
2254 N  N   . GLU A 322 ? 0.4597 0.5706 0.3550 0.0573  0.0290  -0.0488 298 GLU A N   
2255 C  CA  . GLU A 322 ? 0.4986 0.6052 0.3901 0.0576  0.0251  -0.0627 298 GLU A CA  
2256 C  C   . GLU A 322 ? 0.4601 0.5512 0.3621 0.0521  0.0210  -0.0660 298 GLU A C   
2257 O  O   . GLU A 322 ? 0.4590 0.5430 0.3645 0.0524  0.0204  -0.0757 298 GLU A O   
2258 C  CB  . GLU A 322 ? 0.5471 0.6624 0.4274 0.0586  0.0212  -0.0654 298 GLU A CB  
2259 C  CG  . GLU A 322 ? 0.6045 0.7176 0.4801 0.0591  0.0170  -0.0806 298 GLU A CG  
2260 C  CD  . GLU A 322 ? 0.7743 0.9005 0.6364 0.0618  0.0142  -0.0840 298 GLU A CD  
2261 O  OE1 . GLU A 322 ? 0.8393 0.9788 0.6924 0.0665  0.0181  -0.0786 298 GLU A OE1 
2262 O  OE2 . GLU A 322 ? 0.7789 0.9028 0.6396 0.0592  0.0081  -0.0916 298 GLU A OE2 
2263 N  N   . LEU A 323 ? 0.4575 0.5433 0.3650 0.0474  0.0185  -0.0578 299 LEU A N   
2264 C  CA  . LEU A 323 ? 0.4467 0.5188 0.3637 0.0424  0.0151  -0.0599 299 LEU A CA  
2265 C  C   . LEU A 323 ? 0.4757 0.5408 0.4017 0.0423  0.0181  -0.0601 299 LEU A C   
2266 O  O   . LEU A 323 ? 0.4561 0.5110 0.3885 0.0401  0.0160  -0.0657 299 LEU A O   
2267 C  CB  . LEU A 323 ? 0.4280 0.4964 0.3486 0.0380  0.0129  -0.0504 299 LEU A CB  
2268 C  CG  . LEU A 323 ? 0.5048 0.5772 0.4197 0.0372  0.0089  -0.0499 299 LEU A CG  
2269 C  CD1 . LEU A 323 ? 0.4774 0.5470 0.3962 0.0341  0.0086  -0.0389 299 LEU A CD1 
2270 C  CD2 . LEU A 323 ? 0.4622 0.5282 0.3786 0.0347  0.0041  -0.0594 299 LEU A CD2 
2271 N  N   . LEU A 324 ? 0.4794 0.5501 0.4069 0.0447  0.0230  -0.0533 300 LEU A N   
2272 C  CA  . LEU A 324 ? 0.4424 0.5080 0.3795 0.0447  0.0257  -0.0517 300 LEU A CA  
2273 C  C   . LEU A 324 ? 0.4250 0.4955 0.3607 0.0505  0.0302  -0.0579 300 LEU A C   
2274 O  O   . LEU A 324 ? 0.4471 0.5143 0.3913 0.0513  0.0328  -0.0568 300 LEU A O   
2275 C  CB  . LEU A 324 ? 0.3816 0.4497 0.3241 0.0426  0.0278  -0.0391 300 LEU A CB  
2276 C  CG  . LEU A 324 ? 0.4684 0.5307 0.4131 0.0370  0.0239  -0.0329 300 LEU A CG  
2277 C  CD1 . LEU A 324 ? 0.4320 0.4969 0.3822 0.0350  0.0260  -0.0214 300 LEU A CD1 
2278 C  CD2 . LEU A 324 ? 0.4199 0.4698 0.3706 0.0330  0.0199  -0.0370 300 LEU A CD2 
2279 N  N   . ALA A 325 ? 0.4570 0.5357 0.3821 0.0548  0.0312  -0.0645 301 ALA A N   
2280 C  CA  . ALA A 325 ? 0.4489 0.5317 0.3715 0.0608  0.0355  -0.0726 301 ALA A CA  
2281 C  C   . ALA A 325 ? 0.4645 0.5555 0.3906 0.0644  0.0420  -0.0646 301 ALA A C   
2282 O  O   . ALA A 325 ? 0.4789 0.5683 0.4108 0.0677  0.0457  -0.0678 301 ALA A O   
2283 C  CB  . ALA A 325 ? 0.4576 0.5279 0.3876 0.0602  0.0339  -0.0823 301 ALA A CB  
2284 N  N   . LEU A 326 ? 0.4562 0.5564 0.3796 0.0639  0.0437  -0.0537 302 LEU A N   
2285 C  CA  . LEU A 326 ? 0.4702 0.5788 0.3985 0.0664  0.0497  -0.0444 302 LEU A CA  
2286 C  C   . LEU A 326 ? 0.4904 0.6126 0.4091 0.0738  0.0555  -0.0475 302 LEU A C   
2287 O  O   . LEU A 326 ? 0.5112 0.6383 0.4176 0.0765  0.0544  -0.0548 302 LEU A O   
2288 C  CB  . LEU A 326 ? 0.4474 0.5589 0.3788 0.0620  0.0490  -0.0308 302 LEU A CB  
2289 C  CG  . LEU A 326 ? 0.4434 0.5421 0.3829 0.0549  0.0434  -0.0279 302 LEU A CG  
2290 C  CD1 . LEU A 326 ? 0.4189 0.5203 0.3617 0.0510  0.0433  -0.0152 302 LEU A CD1 
2291 C  CD2 . LEU A 326 ? 0.4210 0.5111 0.3720 0.0535  0.0433  -0.0297 302 LEU A CD2 
2292 N  N   . LYS A 327 ? 0.4873 0.6167 0.4120 0.0772  0.0618  -0.0419 303 LYS A N   
2293 C  CA  . LYS A 327 ? 0.5206 0.6629 0.4375 0.0850  0.0685  -0.0452 303 LYS A CA  
2294 C  C   . LYS A 327 ? 0.5417 0.6990 0.4489 0.0870  0.0713  -0.0367 303 LYS A C   
2295 O  O   . LYS A 327 ? 0.5382 0.7074 0.4354 0.0937  0.0763  -0.0403 303 LYS A O   
2296 C  CB  . LYS A 327 ? 0.4667 0.6116 0.3949 0.0883  0.0746  -0.0418 303 LYS A CB  
2297 C  CG  . LYS A 327 ? 0.4711 0.6209 0.4107 0.0849  0.0766  -0.0262 303 LYS A CG  
2298 C  CD  . LYS A 327 ? 0.4731 0.6271 0.4242 0.0886  0.0825  -0.0235 303 LYS A CD  
2299 C  CE  . LYS A 327 ? 0.4556 0.6146 0.4194 0.0845  0.0838  -0.0084 303 LYS A CE  
2300 N  NZ  . LYS A 327 ? 0.5033 0.6703 0.4780 0.0890  0.0904  -0.0048 303 LYS A NZ  
2301 N  N   . GLY A 328 ? 0.4989 0.6561 0.4088 0.0817  0.0686  -0.0255 304 GLY A N   
2302 C  CA  . GLY A 328 ? 0.5435 0.7142 0.4451 0.0834  0.0711  -0.0164 304 GLY A CA  
2303 C  C   . GLY A 328 ? 0.5446 0.7225 0.4565 0.0823  0.0761  -0.0012 304 GLY A C   
2304 O  O   . GLY A 328 ? 0.5145 0.6937 0.4364 0.0837  0.0803  0.0006  304 GLY A O   
2305 N  N   . GLY A 329 ? 0.5500 0.7330 0.4606 0.0797  0.0756  0.0101  305 GLY A N   
2306 C  CA  . GLY A 329 ? 0.5172 0.7062 0.4388 0.0777  0.0798  0.0251  305 GLY A CA  
2307 C  C   . GLY A 329 ? 0.6035 0.8090 0.5239 0.0842  0.0887  0.0299  305 GLY A C   
2308 O  O   . GLY A 329 ? 0.5703 0.7809 0.5026 0.0826  0.0927  0.0414  305 GLY A O   
2309 N  N   . ASP A 330 ? 0.6220 0.8364 0.5285 0.0915  0.0918  0.0212  306 ASP A N   
2310 C  CA  . ASP A 330 ? 0.6470 0.8781 0.5507 0.0988  0.1008  0.0245  306 ASP A CA  
2311 C  C   . ASP A 330 ? 0.6405 0.8695 0.5504 0.1026  0.1044  0.0159  306 ASP A C   
2312 O  O   . ASP A 330 ? 0.6435 0.8859 0.5510 0.1095  0.1124  0.0168  306 ASP A O   
2313 C  CB  . ASP A 330 ? 0.7005 0.9441 0.5843 0.1054  0.1028  0.0198  306 ASP A CB  
2314 C  CG  . ASP A 330 ? 0.7521 0.9880 0.6244 0.1077  0.0981  0.0013  306 ASP A CG  
2315 O  OD1 . ASP A 330 ? 0.7090 0.9292 0.5852 0.1020  0.0905  -0.0048 306 ASP A OD1 
2316 O  OD2 . ASP A 330 ? 0.8250 1.0707 0.6847 0.1152  0.1022  -0.0074 306 ASP A OD2 
2317 N  N   . GLN A 331 ? 0.5859 0.7988 0.5039 0.0986  0.0990  0.0081  307 GLN A N   
2318 C  CA  . GLN A 331 ? 0.5969 0.8061 0.5222 0.1020  0.1018  0.0002  307 GLN A CA  
2319 C  C   . GLN A 331 ? 0.5487 0.7523 0.4936 0.0969  0.1012  0.0087  307 GLN A C   
2320 O  O   . GLN A 331 ? 0.5426 0.7369 0.4958 0.0968  0.0998  0.0022  307 GLN A O   
2321 C  CB  . GLN A 331 ? 0.5881 0.7838 0.5070 0.1024  0.0964  -0.0165 307 GLN A CB  
2322 C  CG  . GLN A 331 ? 0.6232 0.8253 0.5231 0.1083  0.0972  -0.0276 307 GLN A CG  
2323 C  CD  . GLN A 331 ? 0.7057 0.9214 0.6004 0.1177  0.1062  -0.0310 307 GLN A CD  
2324 O  OE1 . GLN A 331 ? 0.7655 0.9784 0.6691 0.1209  0.1100  -0.0351 307 GLN A OE1 
2325 N  NE2 . GLN A 331 ? 0.7529 0.9840 0.6331 0.1224  0.1100  -0.0289 307 GLN A NE2 
2326 N  N   . VAL A 332 ? 0.5141 0.7235 0.4669 0.0926  0.1022  0.0234  308 VAL A N   
2327 C  CA  . VAL A 332 ? 0.5274 0.7327 0.4987 0.0869  0.1009  0.0321  308 VAL A CA  
2328 C  C   . VAL A 332 ? 0.5214 0.7433 0.5017 0.0904  0.1094  0.0430  308 VAL A C   
2329 O  O   . VAL A 332 ? 0.5514 0.7875 0.5230 0.0964  0.1161  0.0456  308 VAL A O   
2330 C  CB  . VAL A 332 ? 0.4935 0.6902 0.4693 0.0778  0.0943  0.0398  308 VAL A CB  
2331 C  CG1 . VAL A 332 ? 0.4848 0.6671 0.4512 0.0750  0.0867  0.0295  308 VAL A CG1 
2332 C  CG2 . VAL A 332 ? 0.4941 0.7024 0.4671 0.0774  0.0977  0.0521  308 VAL A CG2 
2333 N  N   . ASN A 333 ? 0.4826 0.7033 0.4805 0.0866  0.1092  0.0497  309 ASN A N   
2334 C  CA  . ASN A 333 ? 0.4972 0.7336 0.5068 0.0890  0.1168  0.0608  309 ASN A CA  
2335 C  C   . ASN A 333 ? 0.4677 0.7076 0.4880 0.0815  0.1155  0.0759  309 ASN A C   
2336 O  O   . ASN A 333 ? 0.4854 0.7272 0.5229 0.0772  0.1153  0.0838  309 ASN A O   
2337 C  CB  . ASN A 333 ? 0.4743 0.7096 0.4979 0.0907  0.1179  0.0582  309 ASN A CB  
2338 C  CG  . ASN A 333 ? 0.5264 0.7798 0.5614 0.0951  0.1268  0.0681  309 ASN A CG  
2339 O  OD1 . ASN A 333 ? 0.5083 0.7758 0.5357 0.1009  0.1343  0.0715  309 ASN A OD1 
2340 N  ND2 . ASN A 333 ? 0.4769 0.7309 0.5302 0.0924  0.1261  0.0731  309 ASN A ND2 
2341 N  N   . PHE A 334 ? 0.4578 0.6983 0.4682 0.0796  0.1145  0.0799  310 PHE A N   
2342 C  CA  . PHE A 334 ? 0.4655 0.7108 0.4851 0.0737  0.1149  0.0948  310 PHE A CA  
2343 C  C   . PHE A 334 ? 0.5185 0.7691 0.5234 0.0759  0.1167  0.0983  310 PHE A C   
2344 O  O   . PHE A 334 ? 0.5270 0.7812 0.5372 0.0717  0.1173  0.1108  310 PHE A O   
2345 C  CB  . PHE A 334 ? 0.4532 0.6832 0.4836 0.0636  0.1062  0.0967  310 PHE A CB  
2346 C  CG  . PHE A 334 ? 0.4577 0.6708 0.4773 0.0611  0.0982  0.0854  310 PHE A CG  
2347 C  CD1 . PHE A 334 ? 0.4811 0.6895 0.4905 0.0591  0.0953  0.0866  310 PHE A CD1 
2348 C  CD2 . PHE A 334 ? 0.4580 0.6600 0.4785 0.0609  0.0938  0.0744  310 PHE A CD2 
2349 C  CE1 . PHE A 334 ? 0.4549 0.6486 0.4554 0.0568  0.0882  0.0767  310 PHE A CE1 
2350 C  CE2 . PHE A 334 ? 0.4555 0.6426 0.4670 0.0584  0.0868  0.0648  310 PHE A CE2 
2351 C  CZ  . PHE A 334 ? 0.4269 0.6101 0.4286 0.0564  0.0840  0.0658  310 PHE A CZ  
2352 O  OXT . PHE A 334 ? 0.5415 0.7931 0.5295 0.0819  0.1173  0.0888  310 PHE A OXT 
2353 N  N   . LEU B 27  ? 1.0064 0.8193 0.9645 -0.0047 0.0205  -0.0568 3   LEU B N   
2354 C  CA  . LEU B 27  ? 0.9851 0.8099 0.9428 0.0000  0.0225  -0.0511 3   LEU B CA  
2355 C  C   . LEU B 27  ? 0.9730 0.8105 0.9272 -0.0034 0.0186  -0.0476 3   LEU B C   
2356 O  O   . LEU B 27  ? 0.8961 0.7439 0.8498 -0.0006 0.0195  -0.0434 3   LEU B O   
2357 C  CB  . LEU B 27  ? 0.9592 0.7840 0.9102 0.0046  0.0263  -0.0565 3   LEU B CB  
2358 C  CG  . LEU B 27  ? 0.9657 0.7794 0.9199 0.0099  0.0314  -0.0600 3   LEU B CG  
2359 C  CD1 . LEU B 27  ? 0.9087 0.7247 0.8546 0.0139  0.0350  -0.0658 3   LEU B CD1 
2360 C  CD2 . LEU B 27  ? 0.8628 0.6780 0.8283 0.0148  0.0340  -0.0512 3   LEU B CD2 
2361 N  N   . ASN B 28  ? 1.0584 0.8952 1.0110 -0.0095 0.0144  -0.0493 4   ASN B N   
2362 C  CA  . ASN B 28  ? 1.0797 0.9275 1.0276 -0.0126 0.0109  -0.0477 4   ASN B CA  
2363 C  C   . ASN B 28  ? 0.9922 0.8500 0.9460 -0.0115 0.0104  -0.0390 4   ASN B C   
2364 O  O   . ASN B 28  ? 0.9696 0.8372 0.9201 -0.0112 0.0095  -0.0372 4   ASN B O   
2365 C  CB  . ASN B 28  ? 1.1809 1.0259 1.1268 -0.0192 0.0064  -0.0514 4   ASN B CB  
2366 C  CG  . ASN B 28  ? 1.2805 1.1166 1.2193 -0.0206 0.0062  -0.0611 4   ASN B CG  
2367 O  OD1 . ASN B 28  ? 1.3561 1.1815 1.2982 -0.0230 0.0056  -0.0649 4   ASN B OD1 
2368 N  ND2 . ASN B 28  ? 1.3349 1.1753 1.2638 -0.0190 0.0069  -0.0651 4   ASN B ND2 
2369 N  N   . GLY B 29  ? 0.8118 0.6672 0.7741 -0.0110 0.0111  -0.0335 5   GLY B N   
2370 C  CA  . GLY B 29  ? 0.7370 0.6022 0.7037 -0.0098 0.0106  -0.0256 5   GLY B CA  
2371 C  C   . GLY B 29  ? 0.6890 0.5559 0.6606 -0.0040 0.0139  -0.0206 5   GLY B C   
2372 O  O   . GLY B 29  ? 0.6150 0.4854 0.5927 -0.0029 0.0140  -0.0136 5   GLY B O   
2373 N  N   . LYS B 30  ? 0.6126 0.4780 0.5817 0.0001  0.0166  -0.0237 6   LYS B N   
2374 C  CA  . LYS B 30  ? 0.5850 0.4527 0.5591 0.0060  0.0197  -0.0193 6   LYS B CA  
2375 C  C   . LYS B 30  ? 0.5547 0.4344 0.5262 0.0083  0.0196  -0.0182 6   LYS B C   
2376 O  O   . LYS B 30  ? 0.5704 0.4519 0.5358 0.0073  0.0194  -0.0231 6   LYS B O   
2377 C  CB  . LYS B 30  ? 0.6335 0.4903 0.6088 0.0093  0.0235  -0.0233 6   LYS B CB  
2378 C  CG  . LYS B 30  ? 0.6616 0.5047 0.6403 0.0068  0.0236  -0.0255 6   LYS B CG  
2379 C  CD  . LYS B 30  ? 0.6497 0.4918 0.6383 0.0081  0.0241  -0.0170 6   LYS B CD  
2380 C  CE  . LYS B 30  ? 0.7236 0.5512 0.7174 0.0053  0.0245  -0.0189 6   LYS B CE  
2381 N  NZ  . LYS B 30  ? 0.7653 0.5915 0.7564 -0.0021 0.0205  -0.0220 6   LYS B NZ  
2382 N  N   . VAL B 31  ? 0.4816 0.3697 0.4578 0.0113  0.0195  -0.0117 7   VAL B N   
2383 C  CA  . VAL B 31  ? 0.4551 0.3551 0.4303 0.0130  0.0188  -0.0105 7   VAL B CA  
2384 C  C   . VAL B 31  ? 0.4601 0.3626 0.4404 0.0189  0.0216  -0.0076 7   VAL B C   
2385 O  O   . VAL B 31  ? 0.4602 0.3629 0.4463 0.0217  0.0223  -0.0019 7   VAL B O   
2386 C  CB  . VAL B 31  ? 0.4221 0.3318 0.3979 0.0113  0.0157  -0.0062 7   VAL B CB  
2387 C  CG1 . VAL B 31  ? 0.4181 0.3392 0.3934 0.0128  0.0146  -0.0060 7   VAL B CG1 
2388 C  CG2 . VAL B 31  ? 0.4816 0.3891 0.4535 0.0060  0.0132  -0.0086 7   VAL B CG2 
2389 N  N   . ILE B 32  ? 0.4149 0.3200 0.3938 0.0208  0.0234  -0.0108 8   ILE B N   
2390 C  CA  . ILE B 32  ? 0.4165 0.3261 0.4010 0.0263  0.0260  -0.0080 8   ILE B CA  
2391 C  C   . ILE B 32  ? 0.3676 0.2910 0.3553 0.0271  0.0232  -0.0032 8   ILE B C   
2392 O  O   . ILE B 32  ? 0.3418 0.2721 0.3264 0.0242  0.0208  -0.0051 8   ILE B O   
2393 C  CB  . ILE B 32  ? 0.4340 0.3427 0.4163 0.0280  0.0291  -0.0128 8   ILE B CB  
2394 C  CG1 . ILE B 32  ? 0.4470 0.3425 0.4242 0.0269  0.0315  -0.0190 8   ILE B CG1 
2395 C  CG2 . ILE B 32  ? 0.4061 0.3201 0.3958 0.0341  0.0320  -0.0093 8   ILE B CG2 
2396 C  CD1 . ILE B 32  ? 0.4198 0.3157 0.3922 0.0278  0.0344  -0.0242 8   ILE B CD1 
2397 N  N   . ILE B 33  ? 0.3666 0.2941 0.3605 0.0310  0.0233  0.0029  9   ILE B N   
2398 C  CA  . ILE B 33  ? 0.3739 0.3154 0.3709 0.0325  0.0206  0.0071  9   ILE B CA  
2399 C  C   . ILE B 33  ? 0.3809 0.3276 0.3839 0.0373  0.0230  0.0082  9   ILE B C   
2400 O  O   . ILE B 33  ? 0.3704 0.3127 0.3785 0.0419  0.0260  0.0112  9   ILE B O   
2401 C  CB  . ILE B 33  ? 0.3934 0.3389 0.3929 0.0339  0.0188  0.0139  9   ILE B CB  
2402 C  CG1 . ILE B 33  ? 0.3875 0.3289 0.3819 0.0292  0.0170  0.0131  9   ILE B CG1 
2403 C  CG2 . ILE B 33  ? 0.3581 0.3191 0.3600 0.0357  0.0157  0.0173  9   ILE B CG2 
2404 C  CD1 . ILE B 33  ? 0.3730 0.3178 0.3697 0.0306  0.0160  0.0204  9   ILE B CD1 
2405 N  N   . THR B 34  ? 0.3530 0.3088 0.3563 0.0362  0.0217  0.0061  10  THR B N   
2406 C  CA  . THR B 34  ? 0.3636 0.3280 0.3739 0.0402  0.0230  0.0081  10  THR B CA  
2407 C  C   . THR B 34  ? 0.3806 0.3591 0.3951 0.0410  0.0187  0.0127  10  THR B C   
2408 O  O   . THR B 34  ? 0.3812 0.3648 0.3919 0.0372  0.0147  0.0114  10  THR B O   
2409 C  CB  . THR B 34  ? 0.3864 0.3530 0.3958 0.0382  0.0243  0.0033  10  THR B CB  
2410 O  OG1 . THR B 34  ? 0.3988 0.3535 0.4036 0.0381  0.0285  -0.0010 10  THR B OG1 
2411 C  CG2 . THR B 34  ? 0.4040 0.3818 0.4223 0.0418  0.0252  0.0060  10  THR B CG2 
2412 N  N   . CYS B 35  ? 0.3929 0.3780 0.4151 0.0463  0.0194  0.0179  11  CYS B N   
2413 C  CA  . CYS B 35  ? 0.3930 0.3931 0.4193 0.0475  0.0150  0.0223  11  CYS B CA  
2414 C  C   . CYS B 35  ? 0.3907 0.4015 0.4253 0.0497  0.0153  0.0229  11  CYS B C   
2415 O  O   . CYS B 35  ? 0.4012 0.4105 0.4422 0.0546  0.0192  0.0256  11  CYS B O   
2416 C  CB  . CYS B 35  ? 0.3815 0.3825 0.4103 0.0518  0.0147  0.0299  11  CYS B CB  
2417 S  SG  . CYS B 35  ? 0.4547 0.4749 0.4851 0.0526  0.0084  0.0347  11  CYS B SG  
2418 N  N   . ALA B 36  ? 0.3685 0.3899 0.4038 0.0462  0.0111  0.0204  12  ALA B N   
2419 C  CA  . ALA B 36  ? 0.3835 0.4170 0.4278 0.0472  0.0104  0.0210  12  ALA B CA  
2420 C  C   . ALA B 36  ? 0.3336 0.3820 0.3826 0.0495  0.0053  0.0260  12  ALA B C   
2421 O  O   . ALA B 36  ? 0.3305 0.3857 0.3757 0.0461  0.0000  0.0242  12  ALA B O   
2422 C  CB  . ALA B 36  ? 0.3606 0.3961 0.4038 0.0415  0.0089  0.0151  12  ALA B CB  
2423 N  N   . VAL B 37  ? 0.3246 0.3787 0.3820 0.0554  0.0068  0.0322  13  VAL B N   
2424 C  CA  . VAL B 37  ? 0.3591 0.4253 0.4192 0.0586  0.0025  0.0386  13  VAL B CA  
2425 C  C   . VAL B 37  ? 0.3303 0.4153 0.3968 0.0572  -0.0034 0.0385  13  VAL B C   
2426 O  O   . VAL B 37  ? 0.3216 0.4176 0.3867 0.0579  -0.0087 0.0415  13  VAL B O   
2427 C  CB  . VAL B 37  ? 0.3968 0.4609 0.4635 0.0661  0.0065  0.0464  13  VAL B CB  
2428 C  CG1 . VAL B 37  ? 0.3726 0.4183 0.4330 0.0670  0.0112  0.0463  13  VAL B CG1 
2429 C  CG2 . VAL B 37  ? 0.3490 0.4165 0.4265 0.0696  0.0103  0.0472  13  VAL B CG2 
2430 N  N   . THR B 38  ? 0.3409 0.4304 0.4145 0.0551  -0.0028 0.0352  14  THR B N   
2431 C  CA  . THR B 38  ? 0.3370 0.4446 0.4178 0.0532  -0.0091 0.0350  14  THR B CA  
2432 C  C   . THR B 38  ? 0.3478 0.4571 0.4330 0.0476  -0.0094 0.0288  14  THR B C   
2433 O  O   . THR B 38  ? 0.3228 0.4410 0.4086 0.0427  -0.0153 0.0247  14  THR B O   
2434 C  CB  . THR B 38  ? 0.3751 0.4956 0.4675 0.0596  -0.0094 0.0429  14  THR B CB  
2435 O  OG1 . THR B 38  ? 0.3578 0.4972 0.4562 0.0574  -0.0168 0.0428  14  THR B OG1 
2436 C  CG2 . THR B 38  ? 0.3456 0.4628 0.4476 0.0628  -0.0026 0.0445  14  THR B CG2 
2437 N  N   . GLY B 39  ? 0.3417 0.4429 0.4303 0.0482  -0.0030 0.0280  15  GLY B N   
2438 C  CA  . GLY B 39  ? 0.3307 0.4328 0.4229 0.0427  -0.0027 0.0230  15  GLY B CA  
2439 C  C   . GLY B 39  ? 0.3861 0.5058 0.4923 0.0415  -0.0064 0.0244  15  GLY B C   
2440 O  O   . GLY B 39  ? 0.3134 0.4449 0.4285 0.0461  -0.0076 0.0300  15  GLY B O   
2441 N  N   . ALA B 40  ? 0.4047 0.5263 0.5137 0.0350  -0.0085 0.0193  16  ALA B N   
2442 C  CA  . ALA B 40  ? 0.4109 0.5484 0.5341 0.0323  -0.0124 0.0196  16  ALA B CA  
2443 C  C   . ALA B 40  ? 0.4250 0.5663 0.5478 0.0247  -0.0192 0.0131  16  ALA B C   
2444 O  O   . ALA B 40  ? 0.3995 0.5535 0.5347 0.0213  -0.0231 0.0125  16  ALA B O   
2445 C  CB  . ALA B 40  ? 0.4254 0.5626 0.5584 0.0326  -0.0057 0.0214  16  ALA B CB  
2446 N  N   . ILE B 41  ? 0.3443 0.4751 0.4542 0.0219  -0.0208 0.0081  17  ILE B N   
2447 C  CA  . ILE B 41  ? 0.4062 0.5390 0.5155 0.0150  -0.0268 0.0011  17  ILE B CA  
2448 C  C   . ILE B 41  ? 0.4166 0.5609 0.5233 0.0152  -0.0349 -0.0004 17  ILE B C   
2449 O  O   . ILE B 41  ? 0.4457 0.6021 0.5606 0.0112  -0.0412 -0.0036 17  ILE B O   
2450 C  CB  . ILE B 41  ? 0.4665 0.5827 0.5640 0.0121  -0.0241 -0.0036 17  ILE B CB  
2451 C  CG1 . ILE B 41  ? 0.5217 0.6282 0.6215 0.0116  -0.0167 -0.0023 17  ILE B CG1 
2452 C  CG2 . ILE B 41  ? 0.4755 0.5929 0.5720 0.0059  -0.0302 -0.0110 17  ILE B CG2 
2453 C  CD1 . ILE B 41  ? 0.5533 0.6679 0.6682 0.0082  -0.0163 -0.0017 17  ILE B CD1 
2454 N  N   . HIS B 42  ? 0.3902 0.5313 0.4855 0.0194  -0.0350 0.0017  18  HIS B N   
2455 C  CA  . HIS B 42  ? 0.3872 0.5406 0.4790 0.0205  -0.0422 0.0015  18  HIS B CA  
2456 C  C   . HIS B 42  ? 0.4061 0.5768 0.5099 0.0238  -0.0451 0.0073  18  HIS B C   
2457 O  O   . HIS B 42  ? 0.3468 0.5178 0.4590 0.0276  -0.0401 0.0133  18  HIS B O   
2458 C  CB  . HIS B 42  ? 0.3805 0.5266 0.4583 0.0249  -0.0405 0.0042  18  HIS B CB  
2459 C  CG  . HIS B 42  ? 0.4311 0.5621 0.4973 0.0218  -0.0384 -0.0013 18  HIS B CG  
2460 N  ND1 . HIS B 42  ? 0.4064 0.5244 0.4633 0.0248  -0.0331 0.0016  18  HIS B ND1 
2461 C  CD2 . HIS B 42  ? 0.4434 0.5706 0.5069 0.0160  -0.0409 -0.0094 18  HIS B CD2 
2462 C  CE1 . HIS B 42  ? 0.4312 0.5390 0.4800 0.0210  -0.0326 -0.0042 18  HIS B CE1 
2463 N  NE2 . HIS B 42  ? 0.4641 0.5769 0.5167 0.0159  -0.0371 -0.0108 18  HIS B NE2 
2464 N  N   . THR B 43  ? 0.3702 0.5559 0.4746 0.0227  -0.0533 0.0054  19  THR B N   
2465 C  CA  . THR B 43  ? 0.4185 0.6232 0.5344 0.0254  -0.0576 0.0107  19  THR B CA  
2466 C  C   . THR B 43  ? 0.4180 0.6323 0.5253 0.0302  -0.0621 0.0148  19  THR B C   
2467 O  O   . THR B 43  ? 0.4037 0.6127 0.4970 0.0298  -0.0636 0.0113  19  THR B O   
2468 C  CB  . THR B 43  ? 0.4120 0.6294 0.5394 0.0187  -0.0646 0.0046  19  THR B CB  
2469 O  OG1 . THR B 43  ? 0.3941 0.6146 0.5121 0.0147  -0.0718 -0.0036 19  THR B OG1 
2470 C  CG2 . THR B 43  ? 0.4420 0.6492 0.5775 0.0135  -0.0599 0.0010  19  THR B CG2 
2471 N  N   . PRO B 44  ? 0.3918 0.6212 0.5077 0.0353  -0.0642 0.0227  20  PRO B N   
2472 C  CA  . PRO B 44  ? 0.4065 0.6443 0.5142 0.0411  -0.0671 0.0289  20  PRO B CA  
2473 C  C   . PRO B 44  ? 0.4104 0.6594 0.5089 0.0379  -0.0761 0.0228  20  PRO B C   
2474 O  O   . PRO B 44  ? 0.4285 0.6786 0.5147 0.0416  -0.0770 0.0257  20  PRO B O   
2475 C  CB  . PRO B 44  ? 0.3873 0.6405 0.5093 0.0466  -0.0678 0.0385  20  PRO B CB  
2476 C  CG  . PRO B 44  ? 0.4299 0.6781 0.5657 0.0449  -0.0624 0.0383  20  PRO B CG  
2477 C  CD  . PRO B 44  ? 0.4245 0.6643 0.5583 0.0364  -0.0633 0.0274  20  PRO B CD  
2478 N  N   . SER B 45  ? 0.3811 0.6388 0.4854 0.0312  -0.0826 0.0143  21  SER B N   
2479 C  CA  . SER B 45  ? 0.4535 0.7212 0.5484 0.0280  -0.0912 0.0067  21  SER B CA  
2480 C  C   . SER B 45  ? 0.4324 0.6843 0.5108 0.0262  -0.0887 0.0001  21  SER B C   
2481 O  O   . SER B 45  ? 0.4488 0.7076 0.5157 0.0256  -0.0942 -0.0047 21  SER B O   
2482 C  CB  . SER B 45  ? 0.4711 0.7493 0.5772 0.0206  -0.0985 -0.0021 21  SER B CB  
2483 O  OG  . SER B 45  ? 0.4596 0.7565 0.5806 0.0223  -0.1026 0.0041  21  SER B OG  
2484 N  N   . MET B 46  ? 0.3996 0.6314 0.4764 0.0254  -0.0804 -0.0004 22  MET B N   
2485 C  CA  . MET B 46  ? 0.4391 0.6561 0.5016 0.0235  -0.0778 -0.0064 22  MET B CA  
2486 C  C   . MET B 46  ? 0.4309 0.6456 0.4803 0.0297  -0.0751 0.0005  22  MET B C   
2487 O  O   . MET B 46  ? 0.4519 0.6625 0.4883 0.0290  -0.0758 -0.0042 22  MET B O   
2488 C  CB  . MET B 46  ? 0.4379 0.6354 0.5036 0.0206  -0.0704 -0.0086 22  MET B CB  
2489 C  CG  . MET B 46  ? 0.4224 0.6204 0.5008 0.0141  -0.0722 -0.0150 22  MET B CG  
2490 S  SD  . MET B 46  ? 0.4562 0.6326 0.5374 0.0116  -0.0629 -0.0157 22  MET B SD  
2491 C  CE  . MET B 46  ? 0.4817 0.6639 0.5802 0.0043  -0.0662 -0.0213 22  MET B CE  
2492 N  N   . SER B 47  ? 0.3879 0.6050 0.4412 0.0360  -0.0717 0.0116  23  SER B N   
2493 C  CA  . SER B 47  ? 0.4259 0.6401 0.4688 0.0419  -0.0686 0.0194  23  SER B CA  
2494 C  C   . SER B 47  ? 0.4286 0.6521 0.4793 0.0488  -0.0676 0.0317  23  SER B C   
2495 O  O   . SER B 47  ? 0.3748 0.5946 0.4376 0.0501  -0.0637 0.0354  23  SER B O   
2496 C  CB  . SER B 47  ? 0.4006 0.5928 0.4378 0.0415  -0.0603 0.0191  23  SER B CB  
2497 O  OG  . SER B 47  ? 0.3869 0.5757 0.4164 0.0470  -0.0569 0.0276  23  SER B OG  
2498 N  N   . PRO B 48  ? 0.4069 0.6430 0.4515 0.0537  -0.0709 0.0385  24  PRO B N   
2499 C  CA  . PRO B 48  ? 0.4129 0.6567 0.4654 0.0610  -0.0693 0.0515  24  PRO B CA  
2500 C  C   . PRO B 48  ? 0.4081 0.6336 0.4614 0.0651  -0.0599 0.0588  24  PRO B C   
2501 O  O   . PRO B 48  ? 0.4033 0.6317 0.4656 0.0711  -0.0573 0.0689  24  PRO B O   
2502 C  CB  . PRO B 48  ? 0.3819 0.6428 0.4250 0.0647  -0.0751 0.0564  24  PRO B CB  
2503 C  CG  . PRO B 48  ? 0.4235 0.6771 0.4509 0.0611  -0.0753 0.0485  24  PRO B CG  
2504 C  CD  . PRO B 48  ? 0.3911 0.6341 0.4208 0.0534  -0.0752 0.0355  24  PRO B CD  
2505 N  N   . TYR B 49  ? 0.3863 0.5933 0.4313 0.0621  -0.0549 0.0538  25  TYR B N   
2506 C  CA  . TYR B 49  ? 0.4227 0.6116 0.4678 0.0652  -0.0464 0.0594  25  TYR B CA  
2507 C  C   . TYR B 49  ? 0.4091 0.5845 0.4632 0.0632  -0.0410 0.0558  25  TYR B C   
2508 O  O   . TYR B 49  ? 0.4067 0.5669 0.4619 0.0658  -0.0341 0.0597  25  TYR B O   
2509 C  CB  . TYR B 49  ? 0.4050 0.5821 0.4365 0.0631  -0.0441 0.0565  25  TYR B CB  
2510 C  CG  . TYR B 49  ? 0.4499 0.6406 0.4711 0.0650  -0.0489 0.0594  25  TYR B CG  
2511 C  CD1 . TYR B 49  ? 0.4575 0.6550 0.4785 0.0717  -0.0480 0.0717  25  TYR B CD1 
2512 C  CD2 . TYR B 49  ? 0.4275 0.6245 0.4393 0.0605  -0.0539 0.0500  25  TYR B CD2 
2513 C  CE1 . TYR B 49  ? 0.4792 0.6904 0.4902 0.0737  -0.0521 0.0751  25  TYR B CE1 
2514 C  CE2 . TYR B 49  ? 0.4667 0.6770 0.4681 0.0626  -0.0580 0.0523  25  TYR B CE2 
2515 C  CZ  . TYR B 49  ? 0.4835 0.7012 0.4840 0.0692  -0.0571 0.0650  25  TYR B CZ  
2516 O  OH  . TYR B 49  ? 0.5255 0.7574 0.5148 0.0716  -0.0609 0.0679  25  TYR B OH  
2517 N  N   . LEU B 50  ? 0.4161 0.5966 0.4766 0.0587  -0.0440 0.0486  26  LEU B N   
2518 C  CA  . LEU B 50  ? 0.4245 0.5944 0.4939 0.0572  -0.0387 0.0462  26  LEU B CA  
2519 C  C   . LEU B 50  ? 0.3823 0.5559 0.4635 0.0640  -0.0352 0.0556  26  LEU B C   
2520 O  O   . LEU B 50  ? 0.4098 0.6012 0.4992 0.0664  -0.0399 0.0600  26  LEU B O   
2521 C  CB  . LEU B 50  ? 0.3846 0.5614 0.4598 0.0510  -0.0428 0.0377  26  LEU B CB  
2522 C  CG  . LEU B 50  ? 0.3937 0.5605 0.4774 0.0489  -0.0372 0.0351  26  LEU B CG  
2523 C  CD1 . LEU B 50  ? 0.3831 0.5295 0.4573 0.0460  -0.0318 0.0301  26  LEU B CD1 
2524 C  CD2 . LEU B 50  ? 0.3869 0.5646 0.4801 0.0437  -0.0418 0.0295  26  LEU B CD2 
2525 N  N   . PRO B 51  ? 0.4097 0.5676 0.4924 0.0672  -0.0273 0.0587  27  PRO B N   
2526 C  CA  . PRO B 51  ? 0.4023 0.5630 0.4969 0.0741  -0.0235 0.0672  27  PRO B CA  
2527 C  C   . PRO B 51  ? 0.4146 0.5859 0.5223 0.0731  -0.0244 0.0655  27  PRO B C   
2528 O  O   . PRO B 51  ? 0.3952 0.5616 0.5035 0.0676  -0.0235 0.0577  27  PRO B O   
2529 C  CB  . PRO B 51  ? 0.3926 0.5314 0.4844 0.0761  -0.0148 0.0674  27  PRO B CB  
2530 C  CG  . PRO B 51  ? 0.3758 0.5030 0.4536 0.0714  -0.0151 0.0621  27  PRO B CG  
2531 C  CD  . PRO B 51  ? 0.3637 0.5006 0.4374 0.0649  -0.0217 0.0546  27  PRO B CD  
2532 N  N   . VAL B 52  ? 0.3947 0.5811 0.5139 0.0787  -0.0262 0.0735  28  VAL B N   
2533 C  CA  . VAL B 52  ? 0.4136 0.6125 0.5473 0.0783  -0.0272 0.0733  28  VAL B CA  
2534 C  C   . VAL B 52  ? 0.4260 0.6247 0.5718 0.0866  -0.0209 0.0820  28  VAL B C   
2535 O  O   . VAL B 52  ? 0.4227 0.6135 0.5749 0.0872  -0.0144 0.0800  28  VAL B O   
2536 C  CB  . VAL B 52  ? 0.3945 0.6170 0.5325 0.0761  -0.0373 0.0737  28  VAL B CB  
2537 C  CG1 . VAL B 52  ? 0.4272 0.6641 0.5829 0.0762  -0.0381 0.0751  28  VAL B CG1 
2538 C  CG2 . VAL B 52  ? 0.3971 0.6190 0.5241 0.0677  -0.0431 0.0635  28  VAL B CG2 
2539 N  N   . SER B 53  ? 0.4161 0.6238 0.5653 0.0934  -0.0226 0.0918  29  SER B N   
2540 C  CA  . SER B 53  ? 0.4707 0.6787 0.6325 0.1021  -0.0167 0.1006  29  SER B CA  
2541 C  C   . SER B 53  ? 0.4769 0.6604 0.6345 0.1047  -0.0068 0.0992  29  SER B C   
2542 O  O   . SER B 53  ? 0.4294 0.5967 0.5735 0.1007  -0.0053 0.0937  29  SER B O   
2543 C  CB  . SER B 53  ? 0.4525 0.6734 0.6176 0.1090  -0.0205 0.1121  29  SER B CB  
2544 O  OG  . SER B 53  ? 0.4712 0.6797 0.6239 0.1102  -0.0191 0.1145  29  SER B OG  
2545 N  N   . ALA B 54  ? 0.4291 0.6101 0.5985 0.1115  -0.0001 0.1040  30  ALA B N   
2546 C  CA  . ALA B 54  ? 0.4618 0.6200 0.6281 0.1146  0.0094  0.1021  30  ALA B CA  
2547 C  C   . ALA B 54  ? 0.4372 0.5824 0.5942 0.1168  0.0103  0.1059  30  ALA B C   
2548 O  O   . ALA B 54  ? 0.4488 0.5745 0.5953 0.1138  0.0142  0.1001  30  ALA B O   
2549 C  CB  . ALA B 54  ? 0.4630 0.6229 0.6446 0.1229  0.0162  0.1075  30  ALA B CB  
2550 N  N   . SER B 55  ? 0.4321 0.5888 0.5933 0.1220  0.0066  0.1162  31  SER B N   
2551 C  CA  . SER B 55  ? 0.4617 0.6071 0.6158 0.1245  0.0079  0.1215  31  SER B CA  
2552 C  C   . SER B 55  ? 0.4478 0.5890 0.5857 0.1167  0.0033  0.1155  31  SER B C   
2553 O  O   . SER B 55  ? 0.4501 0.5750 0.5799 0.1162  0.0065  0.1155  31  SER B O   
2554 C  CB  . SER B 55  ? 0.5027 0.6635 0.6655 0.1321  0.0048  0.1351  31  SER B CB  
2555 O  OG  . SER B 55  ? 0.5722 0.7566 0.7345 0.1294  -0.0046 0.1365  31  SER B OG  
2556 N  N   . GLU B 56  ? 0.4476 0.6033 0.5812 0.1106  -0.0040 0.1104  32  GLU B N   
2557 C  CA  . GLU B 56  ? 0.4533 0.6045 0.5718 0.1033  -0.0077 0.1035  32  GLU B CA  
2558 C  C   . GLU B 56  ? 0.4427 0.5732 0.5540 0.0980  -0.0025 0.0934  32  GLU B C   
2559 O  O   . GLU B 56  ? 0.3970 0.5155 0.4971 0.0946  -0.0018 0.0903  32  GLU B O   
2560 C  CB  . GLU B 56  ? 0.4285 0.5993 0.5449 0.0981  -0.0166 0.0993  32  GLU B CB  
2561 C  CG  . GLU B 56  ? 0.4583 0.6498 0.5765 0.1019  -0.0234 0.1083  32  GLU B CG  
2562 C  CD  . GLU B 56  ? 0.5021 0.7136 0.6200 0.0968  -0.0324 0.1030  32  GLU B CD  
2563 O  OE1 . GLU B 56  ? 0.4790 0.6885 0.5982 0.0907  -0.0329 0.0934  32  GLU B OE1 
2564 O  OE2 . GLU B 56  ? 0.5631 0.7924 0.6796 0.0988  -0.0391 0.1086  32  GLU B OE2 
2565 N  N   . ILE B 57  ? 0.4304 0.5577 0.5485 0.0975  0.0014  0.0886  33  ILE B N   
2566 C  CA  . ILE B 57  ? 0.3988 0.5078 0.5100 0.0929  0.0063  0.0794  33  ILE B CA  
2567 C  C   . ILE B 57  ? 0.4401 0.5291 0.5488 0.0966  0.0134  0.0812  33  ILE B C   
2568 O  O   . ILE B 57  ? 0.4052 0.4788 0.5035 0.0923  0.0152  0.0755  33  ILE B O   
2569 C  CB  . ILE B 57  ? 0.4018 0.5144 0.5211 0.0918  0.0089  0.0747  33  ILE B CB  
2570 C  CG1 . ILE B 57  ? 0.3636 0.4923 0.4835 0.0856  0.0016  0.0705  33  ILE B CG1 
2571 C  CG2 . ILE B 57  ? 0.3837 0.4768 0.4968 0.0892  0.0155  0.0670  33  ILE B CG2 
2572 C  CD1 . ILE B 57  ? 0.3782 0.5149 0.5091 0.0848  0.0033  0.0682  33  ILE B CD1 
2573 N  N   . THR B 58  ? 0.4128 0.5015 0.5316 0.1047  0.0172  0.0893  34  THR B N   
2574 C  CA  . THR B 58  ? 0.4474 0.5161 0.5652 0.1083  0.0239  0.0909  34  THR B CA  
2575 C  C   . THR B 58  ? 0.3978 0.4615 0.5079 0.1072  0.0216  0.0951  34  THR B C   
2576 O  O   . THR B 58  ? 0.4289 0.4744 0.5323 0.1050  0.0251  0.0916  34  THR B O   
2577 C  CB  . THR B 58  ? 0.4390 0.5087 0.5708 0.1177  0.0289  0.0986  34  THR B CB  
2578 O  OG1 . THR B 58  ? 0.4456 0.5323 0.5844 0.1224  0.0243  0.1097  34  THR B OG1 
2579 C  CG2 . THR B 58  ? 0.4353 0.5104 0.5752 0.1191  0.0321  0.0946  34  THR B CG2 
2580 N  N   . ASP B 59  ? 0.4240 0.5041 0.5349 0.1086  0.0157  0.1028  35  ASP B N   
2581 C  CA  . ASP B 59  ? 0.4450 0.5226 0.5476 0.1072  0.0133  0.1070  35  ASP B CA  
2582 C  C   . ASP B 59  ? 0.4447 0.5149 0.5339 0.0986  0.0115  0.0972  35  ASP B C   
2583 O  O   . ASP B 59  ? 0.4675 0.5241 0.5502 0.0966  0.0136  0.0969  35  ASP B O   
2584 C  CB  . ASP B 59  ? 0.4635 0.5632 0.5678 0.1099  0.0067  0.1159  35  ASP B CB  
2585 C  CG  . ASP B 59  ? 0.5112 0.6168 0.6283 0.1192  0.0087  0.1285  35  ASP B CG  
2586 O  OD1 . ASP B 59  ? 0.5324 0.6232 0.6571 0.1236  0.0157  0.1301  35  ASP B OD1 
2587 O  OD2 . ASP B 59  ? 0.5927 0.7178 0.7123 0.1222  0.0033  0.1366  35  ASP B OD2 
2588 N  N   . ALA B 60  ? 0.4187 0.4978 0.5043 0.0934  0.0075  0.0893  36  ALA B N   
2589 C  CA  . ALA B 60  ? 0.4507 0.5230 0.5245 0.0856  0.0059  0.0800  36  ALA B CA  
2590 C  C   . ALA B 60  ? 0.4344 0.4852 0.5053 0.0835  0.0121  0.0738  36  ALA B C   
2591 O  O   . ALA B 60  ? 0.4155 0.4557 0.4776 0.0794  0.0125  0.0707  36  ALA B O   
2592 C  CB  . ALA B 60  ? 0.4004 0.4852 0.4736 0.0808  0.0011  0.0729  36  ALA B CB  
2593 N  N   . ALA B 61  ? 0.4113 0.4564 0.4894 0.0864  0.0170  0.0720  37  ALA B N   
2594 C  CA  . ALA B 61  ? 0.4424 0.4681 0.5169 0.0845  0.0227  0.0652  37  ALA B CA  
2595 C  C   . ALA B 61  ? 0.4503 0.4607 0.5239 0.0868  0.0262  0.0691  37  ALA B C   
2596 O  O   . ALA B 61  ? 0.4267 0.4228 0.4928 0.0824  0.0278  0.0636  37  ALA B O   
2597 C  CB  . ALA B 61  ? 0.3930 0.4174 0.4755 0.0881  0.0275  0.0630  37  ALA B CB  
2598 N  N   . ILE B 62  ? 0.4095 0.4228 0.4917 0.0935  0.0274  0.0790  38  ILE B N   
2599 C  CA  . ILE B 62  ? 0.4524 0.4506 0.5361 0.0960  0.0313  0.0835  38  ILE B CA  
2600 C  C   . ILE B 62  ? 0.4887 0.4861 0.5639 0.0913  0.0278  0.0853  38  ILE B C   
2601 O  O   . ILE B 62  ? 0.4893 0.4708 0.5611 0.0887  0.0304  0.0834  38  ILE B O   
2602 C  CB  . ILE B 62  ? 0.4441 0.4468 0.5403 0.1048  0.0334  0.0947  38  ILE B CB  
2603 C  CG1 . ILE B 62  ? 0.4540 0.4540 0.5591 0.1098  0.0384  0.0921  38  ILE B CG1 
2604 C  CG2 . ILE B 62  ? 0.4724 0.4608 0.5710 0.1070  0.0366  0.1011  38  ILE B CG2 
2605 C  CD1 . ILE B 62  ? 0.4622 0.4725 0.5808 0.1187  0.0394  0.1030  38  ILE B CD1 
2606 N  N   . GLY B 63  ? 0.4892 0.5040 0.5609 0.0901  0.0220  0.0889  39  GLY B N   
2607 C  CA  . GLY B 63  ? 0.4698 0.4853 0.5328 0.0859  0.0191  0.0902  39  GLY B CA  
2608 C  C   . GLY B 63  ? 0.4668 0.4726 0.5200 0.0782  0.0189  0.0794  39  GLY B C   
2609 O  O   . GLY B 63  ? 0.4534 0.4502 0.5017 0.0750  0.0196  0.0794  39  GLY B O   
2610 N  N   . ALA B 64  ? 0.4331 0.4412 0.4842 0.0753  0.0180  0.0706  40  ALA B N   
2611 C  CA  . ALA B 64  ? 0.4603 0.4597 0.5027 0.0684  0.0178  0.0608  40  ALA B CA  
2612 C  C   . ALA B 64  ? 0.4686 0.4479 0.5109 0.0675  0.0230  0.0574  40  ALA B C   
2613 O  O   . ALA B 64  ? 0.4501 0.4205 0.4858 0.0626  0.0228  0.0536  40  ALA B O   
2614 C  CB  . ALA B 64  ? 0.4047 0.4110 0.4464 0.0660  0.0162  0.0534  40  ALA B CB  
2615 N  N   . ALA B 65  ? 0.4619 0.4341 0.5118 0.0724  0.0275  0.0583  41  ALA B N   
2616 C  CA  . ALA B 65  ? 0.4724 0.4252 0.5224 0.0719  0.0324  0.0545  41  ALA B CA  
2617 C  C   . ALA B 65  ? 0.4786 0.4228 0.5292 0.0714  0.0329  0.0602  41  ALA B C   
2618 O  O   . ALA B 65  ? 0.4730 0.4041 0.5192 0.0669  0.0339  0.0553  41  ALA B O   
2619 C  CB  . ALA B 65  ? 0.4679 0.4156 0.5265 0.0783  0.0374  0.0550  41  ALA B CB  
2620 N  N   . GLU B 66  ? 0.4966 0.4487 0.5534 0.0760  0.0321  0.0710  42  GLU B N   
2621 C  CA  . GLU B 66  ? 0.5204 0.4649 0.5793 0.0760  0.0331  0.0780  42  GLU B CA  
2622 C  C   . GLU B 66  ? 0.5230 0.4702 0.5729 0.0695  0.0297  0.0764  42  GLU B C   
2623 O  O   . GLU B 66  ? 0.5556 0.4924 0.6058 0.0669  0.0311  0.0784  42  GLU B O   
2624 C  CB  . GLU B 66  ? 0.5356 0.4903 0.6029 0.0829  0.0330  0.0911  42  GLU B CB  
2625 C  CG  . GLU B 66  ? 0.6182 0.5666 0.6967 0.0900  0.0376  0.0942  42  GLU B CG  
2626 C  CD  . GLU B 66  ? 0.7564 0.7189 0.8432 0.0973  0.0367  0.1070  42  GLU B CD  
2627 O  OE1 . GLU B 66  ? 0.7521 0.7322 0.8346 0.0967  0.0317  0.1118  42  GLU B OE1 
2628 O  OE2 . GLU B 66  ? 0.8097 0.7661 0.9073 0.1038  0.0408  0.1121  42  GLU B OE2 
2629 N  N   . ALA B 67  ? 0.4923 0.4531 0.5348 0.0666  0.0254  0.0727  43  ALA B N   
2630 C  CA  . ALA B 67  ? 0.4985 0.4619 0.5324 0.0608  0.0224  0.0701  43  ALA B CA  
2631 C  C   . ALA B 67  ? 0.5098 0.4604 0.5383 0.0547  0.0233  0.0597  43  ALA B C   
2632 O  O   . ALA B 67  ? 0.4772 0.4271 0.5000 0.0498  0.0217  0.0580  43  ALA B O   
2633 C  CB  . ALA B 67  ? 0.4587 0.4406 0.4871 0.0602  0.0175  0.0693  43  ALA B CB  
2634 N  N   . GLY B 68  ? 0.4988 0.4404 0.5288 0.0550  0.0259  0.0531  44  GLY B N   
2635 C  CA  . GLY B 68  ? 0.4672 0.3963 0.4919 0.0497  0.0268  0.0438  44  GLY B CA  
2636 C  C   . GLY B 68  ? 0.4805 0.4110 0.5014 0.0485  0.0267  0.0351  44  GLY B C   
2637 O  O   . GLY B 68  ? 0.4470 0.3691 0.4624 0.0441  0.0271  0.0275  44  GLY B O   
2638 N  N   . ALA B 69  ? 0.4219 0.3636 0.4458 0.0522  0.0263  0.0364  45  ALA B N   
2639 C  CA  . ALA B 69  ? 0.4304 0.3744 0.4520 0.0512  0.0267  0.0293  45  ALA B CA  
2640 C  C   . ALA B 69  ? 0.4649 0.3970 0.4897 0.0543  0.0319  0.0259  45  ALA B C   
2641 O  O   . ALA B 69  ? 0.4302 0.3620 0.4629 0.0602  0.0346  0.0307  45  ALA B O   
2642 C  CB  . ALA B 69  ? 0.4116 0.3725 0.4367 0.0537  0.0241  0.0322  45  ALA B CB  
2643 N  N   . ALA B 70  ? 0.4309 0.3537 0.4494 0.0505  0.0332  0.0177  46  ALA B N   
2644 C  CA  . ALA B 70  ? 0.4621 0.3732 0.4817 0.0532  0.0382  0.0130  46  ALA B CA  
2645 C  C   . ALA B 70  ? 0.4577 0.3765 0.4799 0.0567  0.0406  0.0113  46  ALA B C   
2646 O  O   . ALA B 70  ? 0.4564 0.3692 0.4827 0.0616  0.0454  0.0102  46  ALA B O   
2647 C  CB  . ALA B 70  ? 0.4812 0.3804 0.4923 0.0478  0.0384  0.0048  46  ALA B CB  
2648 N  N   . VAL B 71  ? 0.4090 0.3408 0.4295 0.0544  0.0375  0.0111  47  VAL B N   
2649 C  CA  . VAL B 71  ? 0.4329 0.3737 0.4568 0.0569  0.0393  0.0100  47  VAL B CA  
2650 C  C   . VAL B 71  ? 0.4147 0.3720 0.4453 0.0584  0.0357  0.0164  47  VAL B C   
2651 O  O   . VAL B 71  ? 0.4291 0.3929 0.4569 0.0546  0.0307  0.0178  47  VAL B O   
2652 C  CB  . VAL B 71  ? 0.4319 0.3730 0.4482 0.0519  0.0391  0.0032  47  VAL B CB  
2653 C  CG1 . VAL B 71  ? 0.3845 0.3355 0.4058 0.0545  0.0414  0.0032  47  VAL B CG1 
2654 C  CG2 . VAL B 71  ? 0.4201 0.3460 0.4286 0.0501  0.0420  -0.0034 47  VAL B CG2 
2655 N  N   . ILE B 72  ? 0.4020 0.3666 0.4416 0.0639  0.0380  0.0200  48  ILE B N   
2656 C  CA  . ILE B 72  ? 0.3968 0.3785 0.4436 0.0655  0.0343  0.0256  48  ILE B CA  
2657 C  C   . ILE B 72  ? 0.3969 0.3878 0.4471 0.0650  0.0353  0.0229  48  ILE B C   
2658 O  O   . ILE B 72  ? 0.4148 0.4029 0.4689 0.0688  0.0408  0.0218  48  ILE B O   
2659 C  CB  . ILE B 72  ? 0.4104 0.3957 0.4668 0.0726  0.0355  0.0337  48  ILE B CB  
2660 C  CG1 . ILE B 72  ? 0.4326 0.4075 0.4865 0.0732  0.0354  0.0371  48  ILE B CG1 
2661 C  CG2 . ILE B 72  ? 0.3965 0.4011 0.4594 0.0735  0.0306  0.0392  48  ILE B CG2 
2662 C  CD1 . ILE B 72  ? 0.3954 0.3751 0.4430 0.0682  0.0296  0.0384  48  ILE B CD1 
2663 N  N   . HIS B 73  ? 0.3686 0.3705 0.4180 0.0603  0.0304  0.0220  49  HIS B N   
2664 C  CA  . HIS B 73  ? 0.3910 0.4023 0.4448 0.0587  0.0307  0.0200  49  HIS B CA  
2665 C  C   . HIS B 73  ? 0.3707 0.3991 0.4358 0.0615  0.0277  0.0257  49  HIS B C   
2666 O  O   . HIS B 73  ? 0.3641 0.4003 0.4294 0.0605  0.0220  0.0285  49  HIS B O   
2667 C  CB  . HIS B 73  ? 0.3886 0.3999 0.4351 0.0513  0.0271  0.0149  49  HIS B CB  
2668 C  CG  . HIS B 73  ? 0.4311 0.4528 0.4833 0.0489  0.0267  0.0136  49  HIS B CG  
2669 N  ND1 . HIS B 73  ? 0.4900 0.5086 0.5424 0.0490  0.0319  0.0111  49  HIS B ND1 
2670 C  CD2 . HIS B 73  ? 0.4005 0.4357 0.4587 0.0461  0.0217  0.0145  49  HIS B CD2 
2671 C  CE1 . HIS B 73  ? 0.4747 0.5045 0.5339 0.0463  0.0303  0.0113  49  HIS B CE1 
2672 N  NE2 . HIS B 73  ? 0.4236 0.4631 0.4866 0.0443  0.0240  0.0130  49  HIS B NE2 
2673 N  N   . LEU B 74  ? 0.3892 0.4240 0.4636 0.0652  0.0314  0.0274  50  LEU B N   
2674 C  CA  . LEU B 74  ? 0.3753 0.4248 0.4621 0.0700  0.0299  0.0340  50  LEU B CA  
2675 C  C   . LEU B 74  ? 0.4015 0.4659 0.4976 0.0679  0.0286  0.0339  50  LEU B C   
2676 O  O   . LEU B 74  ? 0.4105 0.4728 0.5079 0.0673  0.0334  0.0311  50  LEU B O   
2677 C  CB  . LEU B 74  ? 0.3883 0.4324 0.4810 0.0781  0.0363  0.0379  50  LEU B CB  
2678 C  CG  . LEU B 74  ? 0.4045 0.4369 0.4928 0.0814  0.0370  0.0405  50  LEU B CG  
2679 C  CD1 . LEU B 74  ? 0.4016 0.4248 0.4950 0.0889  0.0445  0.0422  50  LEU B CD1 
2680 C  CD2 . LEU B 74  ? 0.3719 0.4159 0.4641 0.0826  0.0308  0.0475  50  LEU B CD2 
2681 N  N   . HIS B 75  ? 0.4059 0.4859 0.5087 0.0669  0.0221  0.0373  51  HIS B N   
2682 C  CA  . HIS B 75  ? 0.3836 0.4807 0.4996 0.0668  0.0204  0.0396  51  HIS B CA  
2683 C  C   . HIS B 75  ? 0.3882 0.4980 0.5146 0.0730  0.0183  0.0474  51  HIS B C   
2684 O  O   . HIS B 75  ? 0.4046 0.5107 0.5270 0.0765  0.0171  0.0510  51  HIS B O   
2685 C  CB  . HIS B 75  ? 0.3879 0.4942 0.5038 0.0590  0.0132  0.0358  51  HIS B CB  
2686 C  CG  . HIS B 75  ? 0.4020 0.4980 0.5098 0.0528  0.0148  0.0291  51  HIS B CG  
2687 N  ND1 . HIS B 75  ? 0.3988 0.5018 0.5127 0.0474  0.0135  0.0266  51  HIS B ND1 
2688 C  CD2 . HIS B 75  ? 0.3925 0.4722 0.4874 0.0510  0.0174  0.0250  51  HIS B CD2 
2689 C  CE1 . HIS B 75  ? 0.4275 0.5188 0.5322 0.0431  0.0154  0.0215  51  HIS B CE1 
2690 N  NE2 . HIS B 75  ? 0.3701 0.4476 0.4631 0.0451  0.0176  0.0203  51  HIS B NE2 
2691 N  N   . ALA B 76  ? 0.3796 0.5051 0.5201 0.0744  0.0179  0.0507  52  ALA B N   
2692 C  CA  . ALA B 76  ? 0.3984 0.5397 0.5504 0.0797  0.0146  0.0584  52  ALA B CA  
2693 C  C   . ALA B 76  ? 0.4035 0.5641 0.5633 0.0744  0.0063  0.0580  52  ALA B C   
2694 O  O   . ALA B 76  ? 0.4027 0.5642 0.5622 0.0674  0.0048  0.0523  52  ALA B O   
2695 C  CB  . ALA B 76  ? 0.3783 0.5222 0.5426 0.0876  0.0220  0.0636  52  ALA B CB  
2696 N  N   . ARG B 77  ? 0.3509 0.5272 0.5182 0.0776  0.0008  0.0642  53  ARG B N   
2697 C  CA  . ARG B 77  ? 0.3739 0.5697 0.5486 0.0728  -0.0081 0.0636  53  ARG B CA  
2698 C  C   . ARG B 77  ? 0.4350 0.6501 0.6257 0.0789  -0.0100 0.0723  53  ARG B C   
2699 O  O   . ARG B 77  ? 0.4131 0.6265 0.6063 0.0871  -0.0062 0.0794  53  ARG B O   
2700 C  CB  . ARG B 77  ? 0.3951 0.5920 0.5577 0.0686  -0.0163 0.0604  53  ARG B CB  
2701 C  CG  . ARG B 77  ? 0.3672 0.5475 0.5151 0.0620  -0.0156 0.0517  53  ARG B CG  
2702 C  CD  . ARG B 77  ? 0.3663 0.5489 0.5028 0.0590  -0.0231 0.0491  53  ARG B CD  
2703 N  NE  . ARG B 77  ? 0.3536 0.5223 0.4776 0.0527  -0.0229 0.0408  53  ARG B NE  
2704 C  CZ  . ARG B 77  ? 0.3924 0.5637 0.5171 0.0453  -0.0268 0.0337  53  ARG B CZ  
2705 N  NH1 . ARG B 77  ? 0.3864 0.5734 0.5237 0.0425  -0.0313 0.0331  53  ARG B NH1 
2706 N  NH2 . ARG B 77  ? 0.3662 0.5240 0.4794 0.0406  -0.0261 0.0270  53  ARG B NH2 
2707 N  N   . HIS B 78  ? 0.4108 0.6445 0.6134 0.0747  -0.0160 0.0718  54  HIS B N   
2708 C  CA  . HIS B 78  ? 0.4349 0.6902 0.6527 0.0794  -0.0201 0.0799  54  HIS B CA  
2709 C  C   . HIS B 78  ? 0.4856 0.7490 0.6962 0.0810  -0.0282 0.0831  54  HIS B C   
2710 O  O   . HIS B 78  ? 0.4790 0.7439 0.6799 0.0745  -0.0354 0.0770  54  HIS B O   
2711 C  CB  . HIS B 78  ? 0.3967 0.6702 0.6295 0.0733  -0.0251 0.0779  54  HIS B CB  
2712 C  CG  . HIS B 78  ? 0.3877 0.6577 0.6306 0.0727  -0.0170 0.0771  54  HIS B CG  
2713 N  ND1 . HIS B 78  ? 0.3827 0.6467 0.6240 0.0643  -0.0164 0.0696  54  HIS B ND1 
2714 C  CD2 . HIS B 78  ? 0.3975 0.6698 0.6524 0.0796  -0.0089 0.0833  54  HIS B CD2 
2715 C  CE1 . HIS B 78  ? 0.3543 0.6175 0.6057 0.0661  -0.0083 0.0716  54  HIS B CE1 
2716 N  NE2 . HIS B 78  ? 0.3829 0.6513 0.6426 0.0754  -0.0035 0.0795  54  HIS B NE2 
2717 N  N   . GLU B 79  ? 0.5656 0.8344 0.7812 0.0899  -0.0267 0.0928  55  GLU B N   
2718 C  CA  . GLU B 79  ? 0.5905 0.8674 0.7991 0.0924  -0.0337 0.0974  55  GLU B CA  
2719 C  C   . GLU B 79  ? 0.5394 0.8418 0.7553 0.0886  -0.0451 0.0975  55  GLU B C   
2720 O  O   . GLU B 79  ? 0.5666 0.8767 0.7734 0.0882  -0.0524 0.0985  55  GLU B O   
2721 C  CB  . GLU B 79  ? 0.6205 0.8963 0.8339 0.1033  -0.0288 0.1088  55  GLU B CB  
2722 C  CG  . GLU B 79  ? 0.6641 0.9147 0.8719 0.1072  -0.0175 0.1081  55  GLU B CG  
2723 C  CD  . GLU B 79  ? 0.7300 0.9753 0.9380 0.1167  -0.0138 0.1181  55  GLU B CD  
2724 O  OE1 . GLU B 79  ? 0.7003 0.9624 0.9132 0.1209  -0.0196 0.1267  55  GLU B OE1 
2725 O  OE2 . GLU B 79  ? 0.7114 0.9357 0.9148 0.1200  -0.0051 0.1173  55  GLU B OE2 
2726 N  N   . GLY B 80  ? 0.5487 0.8646 0.7803 0.0856  -0.0467 0.0965  56  GLY B N   
2727 C  CA  . GLY B 80  ? 0.5390 0.8793 0.7790 0.0813  -0.0578 0.0958  56  GLY B CA  
2728 C  C   . GLY B 80  ? 0.5340 0.8734 0.7615 0.0717  -0.0658 0.0848  56  GLY B C   
2729 O  O   . GLY B 80  ? 0.5793 0.9312 0.8003 0.0709  -0.0748 0.0848  56  GLY B O   
2730 N  N   . ASP B 81  ? 0.4411 0.7661 0.6650 0.0645  -0.0624 0.0755  57  ASP B N   
2731 C  CA  . ASP B 81  ? 0.4441 0.7667 0.6578 0.0553  -0.0692 0.0645  57  ASP B CA  
2732 C  C   . ASP B 81  ? 0.4154 0.7126 0.6119 0.0528  -0.0632 0.0579  57  ASP B C   
2733 O  O   . ASP B 81  ? 0.4172 0.7100 0.6053 0.0454  -0.0676 0.0484  57  ASP B O   
2734 C  CB  . ASP B 81  ? 0.4243 0.7571 0.6528 0.0471  -0.0731 0.0587  57  ASP B CB  
2735 C  CG  . ASP B 81  ? 0.4248 0.7460 0.6624 0.0464  -0.0632 0.0589  57  ASP B CG  
2736 O  OD1 . ASP B 81  ? 0.3909 0.6944 0.6209 0.0515  -0.0536 0.0614  57  ASP B OD1 
2737 O  OD2 . ASP B 81  ? 0.4315 0.7619 0.6840 0.0408  -0.0650 0.0565  57  ASP B OD2 
2738 N  N   . GLY B 82  ? 0.3957 0.6763 0.5873 0.0588  -0.0536 0.0623  58  GLY B N   
2739 C  CA  . GLY B 82  ? 0.4546 0.7122 0.6300 0.0569  -0.0483 0.0568  58  GLY B CA  
2740 C  C   . GLY B 82  ? 0.4326 0.6774 0.6095 0.0510  -0.0433 0.0499  58  GLY B C   
2741 O  O   . GLY B 82  ? 0.3944 0.6211 0.5581 0.0486  -0.0398 0.0447  58  GLY B O   
2742 N  N   . SER B 83  ? 0.3917 0.6459 0.5847 0.0487  -0.0427 0.0502  59  SER B N   
2743 C  CA  . SER B 83  ? 0.4055 0.6494 0.6010 0.0429  -0.0380 0.0446  59  SER B CA  
2744 C  C   . SER B 83  ? 0.4088 0.6357 0.6008 0.0480  -0.0266 0.0475  59  SER B C   
2745 O  O   . SER B 83  ? 0.3977 0.6246 0.5917 0.0561  -0.0221 0.0545  59  SER B O   
2746 C  CB  . SER B 83  ? 0.3737 0.6343 0.5887 0.0389  -0.0408 0.0451  59  SER B CB  
2747 O  OG  . SER B 83  ? 0.3952 0.6667 0.6242 0.0459  -0.0369 0.0541  59  SER B OG  
2748 N  N   . PRO B 84  ? 0.4015 0.6139 0.5882 0.0435  -0.0218 0.0420  60  PRO B N   
2749 C  CA  . PRO B 84  ? 0.3893 0.5858 0.5713 0.0480  -0.0113 0.0437  60  PRO B CA  
2750 C  C   . PRO B 84  ? 0.4215 0.6264 0.6183 0.0542  -0.0052 0.0506  60  PRO B C   
2751 O  O   . PRO B 84  ? 0.3702 0.5909 0.5829 0.0523  -0.0072 0.0527  60  PRO B O   
2752 C  CB  . PRO B 84  ? 0.4226 0.6079 0.6000 0.0409  -0.0089 0.0369  60  PRO B CB  
2753 C  CG  . PRO B 84  ? 0.4308 0.6189 0.6034 0.0339  -0.0179 0.0308  60  PRO B CG  
2754 C  CD  . PRO B 84  ? 0.3943 0.6027 0.5771 0.0344  -0.0259 0.0337  60  PRO B CD  
2755 N  N   . ASP B 85  ? 0.4149 0.6089 0.6068 0.0618  0.0024  0.0541  61  ASP B N   
2756 C  CA  . ASP B 85  ? 0.3672 0.5663 0.5714 0.0690  0.0097  0.0603  61  ASP B CA  
2757 C  C   . ASP B 85  ? 0.4146 0.5942 0.6094 0.0720  0.0199  0.0579  61  ASP B C   
2758 O  O   . ASP B 85  ? 0.4038 0.5693 0.5872 0.0761  0.0226  0.0576  61  ASP B O   
2759 C  CB  . ASP B 85  ? 0.3619 0.5700 0.5719 0.0770  0.0080  0.0679  61  ASP B CB  
2760 C  CG  . ASP B 85  ? 0.4345 0.6506 0.6599 0.0847  0.0149  0.0747  61  ASP B CG  
2761 O  OD1 . ASP B 85  ? 0.4098 0.6239 0.6402 0.0841  0.0217  0.0733  61  ASP B OD1 
2762 O  OD2 . ASP B 85  ? 0.4079 0.6329 0.6406 0.0917  0.0138  0.0820  61  ASP B OD2 
2763 N  N   . GLN B 86  ? 0.3898 0.5691 0.5895 0.0698  0.0254  0.0563  62  GLN B N   
2764 C  CA  . GLN B 86  ? 0.4009 0.5634 0.5910 0.0717  0.0347  0.0532  62  GLN B CA  
2765 C  C   . GLN B 86  ? 0.4289 0.5956 0.6295 0.0798  0.0438  0.0580  62  GLN B C   
2766 O  O   . GLN B 86  ? 0.5046 0.6663 0.7040 0.0801  0.0514  0.0562  62  GLN B O   
2767 C  CB  . GLN B 86  ? 0.4419 0.6002 0.6276 0.0634  0.0348  0.0479  62  GLN B CB  
2768 C  CG  . GLN B 86  ? 0.5029 0.6446 0.6767 0.0642  0.0433  0.0441  62  GLN B CG  
2769 C  CD  . GLN B 86  ? 0.4852 0.6083 0.6416 0.0663  0.0441  0.0404  62  GLN B CD  
2770 O  OE1 . GLN B 86  ? 0.4534 0.5754 0.6066 0.0677  0.0390  0.0412  62  GLN B OE1 
2771 N  NE2 . GLN B 86  ? 0.4353 0.5443 0.5805 0.0665  0.0506  0.0364  62  GLN B NE2 
2772 N  N   . SER B 87  ? 0.4183 0.5946 0.6291 0.0868  0.0434  0.0643  63  SER B N   
2773 C  CA  . SER B 87  ? 0.4792 0.6594 0.7006 0.0954  0.0523  0.0690  63  SER B CA  
2774 C  C   . SER B 87  ? 0.4921 0.6542 0.7031 0.1031  0.0588  0.0680  63  SER B C   
2775 O  O   . SER B 87  ? 0.4548 0.6047 0.6534 0.1023  0.0552  0.0657  63  SER B O   
2776 C  CB  . SER B 87  ? 0.4147 0.6168 0.6558 0.0993  0.0487  0.0771  63  SER B CB  
2777 O  OG  . SER B 87  ? 0.4912 0.6931 0.7306 0.1039  0.0442  0.0808  63  SER B OG  
2778 N  N   . VAL B 88  ? 0.4867 0.6473 0.7033 0.1107  0.0686  0.0697  64  VAL B N   
2779 C  CA  . VAL B 88  ? 0.5102 0.6532 0.7185 0.1183  0.0755  0.0682  64  VAL B CA  
2780 C  C   . VAL B 88  ? 0.5180 0.6629 0.7315 0.1241  0.0717  0.0742  64  VAL B C   
2781 O  O   . VAL B 88  ? 0.5119 0.6407 0.7144 0.1257  0.0715  0.0722  64  VAL B O   
2782 C  CB  . VAL B 88  ? 0.5565 0.6992 0.7708 0.1257  0.0871  0.0684  64  VAL B CB  
2783 C  CG1 . VAL B 88  ? 0.5354 0.6596 0.7423 0.1340  0.0941  0.0662  64  VAL B CG1 
2784 C  CG2 . VAL B 88  ? 0.5278 0.6681 0.7351 0.1201  0.0911  0.0630  64  VAL B CG2 
2785 N  N   . GLU B 89  ? 0.5909 0.7561 0.8218 0.1272  0.0685  0.0822  65  GLU B N   
2786 C  CA  . GLU B 89  ? 0.5848 0.7537 0.8219 0.1335  0.0651  0.0893  65  GLU B CA  
2787 C  C   . GLU B 89  ? 0.5504 0.7158 0.7765 0.1277  0.0554  0.0884  65  GLU B C   
2788 O  O   . GLU B 89  ? 0.5466 0.7072 0.7713 0.1325  0.0540  0.0928  65  GLU B O   
2789 C  CB  . GLU B 89  ? 0.6151 0.8089 0.8735 0.1375  0.0629  0.0982  65  GLU B CB  
2790 C  CG  . GLU B 89  ? 0.6756 0.8771 0.9408 0.1431  0.0575  0.1068  65  GLU B CG  
2791 C  CD  . GLU B 89  ? 0.7490 0.9683 1.0355 0.1521  0.0604  0.1163  65  GLU B CD  
2792 O  OE1 . GLU B 89  ? 0.7598 0.9848 1.0560 0.1545  0.0674  0.1160  65  GLU B OE1 
2793 O  OE2 . GLU B 89  ? 0.7834 1.0116 1.0773 0.1571  0.0559  0.1245  65  GLU B OE2 
2794 N  N   . ALA B 90  ? 0.5111 0.6790 0.7297 0.1177  0.0490  0.0831  66  ALA B N   
2795 C  CA  . ALA B 90  ? 0.4956 0.6623 0.7043 0.1123  0.0398  0.0821  66  ALA B CA  
2796 C  C   . ALA B 90  ? 0.4308 0.5752 0.6239 0.1136  0.0423  0.0790  66  ALA B C   
2797 O  O   . ALA B 90  ? 0.4178 0.5614 0.6058 0.1134  0.0367  0.0817  66  ALA B O   
2798 C  CB  . ALA B 90  ? 0.4440 0.6155 0.6477 0.1015  0.0337  0.0759  66  ALA B CB  
2799 N  N   . PHE B 91  ? 0.4379 0.5647 0.6233 0.1148  0.0505  0.0735  67  PHE B N   
2800 C  CA  . PHE B 91  ? 0.4388 0.5440 0.6103 0.1155  0.0531  0.0698  67  PHE B CA  
2801 C  C   . PHE B 91  ? 0.4730 0.5702 0.6500 0.1254  0.0589  0.0749  67  PHE B C   
2802 O  O   . PHE B 91  ? 0.4761 0.5556 0.6436 0.1263  0.0606  0.0729  67  PHE B O   
2803 C  CB  . PHE B 91  ? 0.4543 0.5441 0.6138 0.1114  0.0584  0.0606  67  PHE B CB  
2804 C  CG  . PHE B 91  ? 0.4483 0.5410 0.5999 0.1014  0.0529  0.0553  67  PHE B CG  
2805 C  CD1 . PHE B 91  ? 0.4486 0.5556 0.6082 0.0978  0.0520  0.0551  67  PHE B CD1 
2806 C  CD2 . PHE B 91  ? 0.4159 0.4969 0.5532 0.0957  0.0488  0.0508  67  PHE B CD2 
2807 C  CE1 . PHE B 91  ? 0.4266 0.5352 0.5800 0.0887  0.0471  0.0503  67  PHE B CE1 
2808 C  CE2 . PHE B 91  ? 0.4247 0.5079 0.5554 0.0870  0.0440  0.0460  67  PHE B CE2 
2809 C  CZ  . PHE B 91  ? 0.4161 0.5125 0.5548 0.0836  0.0431  0.0457  67  PHE B CZ  
2810 N  N   . ASN B 92  ? 0.4739 0.5837 0.6668 0.1329  0.0620  0.0816  68  ASN B N   
2811 C  CA  . ASN B 92  ? 0.4904 0.5916 0.6899 0.1431  0.0686  0.0862  68  ASN B CA  
2812 C  C   . ASN B 92  ? 0.4706 0.5674 0.6685 0.1454  0.0642  0.0923  68  ASN B C   
2813 O  O   . ASN B 92  ? 0.4515 0.5295 0.6450 0.1493  0.0692  0.0913  68  ASN B O   
2814 C  CB  . ASN B 92  ? 0.4473 0.5656 0.6658 0.1507  0.0723  0.0931  68  ASN B CB  
2815 C  CG  . ASN B 92  ? 0.5474 0.6569 0.7741 0.1621  0.0798  0.0979  68  ASN B CG  
2816 O  OD1 . ASN B 92  ? 0.5644 0.6846 0.8034 0.1682  0.0775  0.1078  68  ASN B OD1 
2817 N  ND2 . ASN B 92  ? 0.5410 0.6309 0.7611 0.1650  0.0887  0.0909  68  ASN B ND2 
2818 N  N   . PRO B 93  ? 0.4528 0.5661 0.6544 0.1433  0.0554  0.0988  69  PRO B N   
2819 C  CA  . PRO B 93  ? 0.4617 0.5711 0.6604 0.1452  0.0514  0.1051  69  PRO B CA  
2820 C  C   . PRO B 93  ? 0.4739 0.5693 0.6550 0.1375  0.0479  0.0991  69  PRO B C   
2821 O  O   . PRO B 93  ? 0.5030 0.5983 0.6809 0.1377  0.0435  0.1045  69  PRO B O   
2822 C  CB  . PRO B 93  ? 0.4201 0.5553 0.6285 0.1456  0.0429  0.1137  69  PRO B CB  
2823 C  CG  . PRO B 93  ? 0.4640 0.6116 0.6721 0.1381  0.0393  0.1076  69  PRO B CG  
2824 C  CD  . PRO B 93  ? 0.4396 0.5767 0.6487 0.1391  0.0485  0.1009  69  PRO B CD  
2825 N  N   . ILE B 94  ? 0.4759 0.5604 0.6461 0.1309  0.0499  0.0886  70  ILE B N   
2826 C  CA  . ILE B 94  ? 0.4450 0.5183 0.5992 0.1229  0.0463  0.0824  70  ILE B CA  
2827 C  C   . ILE B 94  ? 0.4523 0.5010 0.5976 0.1232  0.0531  0.0760  70  ILE B C   
2828 O  O   . ILE B 94  ? 0.4722 0.5085 0.6109 0.1226  0.0524  0.0768  70  ILE B O   
2829 C  CB  . ILE B 94  ? 0.4407 0.5229 0.5890 0.1140  0.0414  0.0758  70  ILE B CB  
2830 C  CG1 . ILE B 94  ? 0.4246 0.5297 0.5797 0.1123  0.0329  0.0813  70  ILE B CG1 
2831 C  CG2 . ILE B 94  ? 0.4140 0.4817 0.5460 0.1064  0.0395  0.0683  70  ILE B CG2 
2832 C  CD1 . ILE B 94  ? 0.4266 0.5414 0.5791 0.1039  0.0281  0.0750  70  ILE B CD1 
2833 N  N   . LEU B 95  ? 0.4759 0.5178 0.6210 0.1241  0.0597  0.0695  71  LEU B N   
2834 C  CA  . LEU B 95  ? 0.4687 0.4884 0.6030 0.1228  0.0652  0.0613  71  LEU B CA  
2835 C  C   . LEU B 95  ? 0.4787 0.4836 0.6168 0.1298  0.0699  0.0646  71  LEU B C   
2836 O  O   . LEU B 95  ? 0.5204 0.5091 0.6498 0.1271  0.0697  0.0616  71  LEU B O   
2837 C  CB  . LEU B 95  ? 0.4783 0.4964 0.6117 0.1231  0.0714  0.0542  71  LEU B CB  
2838 C  CG  . LEU B 95  ? 0.4890 0.5189 0.6184 0.1155  0.0675  0.0505  71  LEU B CG  
2839 C  CD1 . LEU B 95  ? 0.4701 0.5018 0.6020 0.1175  0.0745  0.0463  71  LEU B CD1 
2840 C  CD2 . LEU B 95  ? 0.4246 0.4445 0.5386 0.1067  0.0633  0.0440  71  LEU B CD2 
2841 N  N   . GLY B 96  ? 0.5032 0.5132 0.6551 0.1389  0.0743  0.0708  72  GLY B N   
2842 C  CA  . GLY B 96  ? 0.4972 0.4919 0.6542 0.1461  0.0796  0.0739  72  GLY B CA  
2843 C  C   . GLY B 96  ? 0.5191 0.5118 0.6761 0.1455  0.0744  0.0816  72  GLY B C   
2844 O  O   . GLY B 96  ? 0.5206 0.4949 0.6752 0.1467  0.0772  0.0809  72  GLY B O   
2845 N  N   . VAL B 97  ? 0.5090 0.5209 0.6686 0.1436  0.0669  0.0890  73  VAL B N   
2846 C  CA  . VAL B 97  ? 0.5251 0.5376 0.6838 0.1430  0.0619  0.0971  73  VAL B CA  
2847 C  C   . VAL B 97  ? 0.5211 0.5181 0.6651 0.1351  0.0602  0.0903  73  VAL B C   
2848 O  O   . VAL B 97  ? 0.5385 0.5223 0.6818 0.1361  0.0613  0.0936  73  VAL B O   
2849 C  CB  . VAL B 97  ? 0.5286 0.5661 0.6906 0.1417  0.0537  0.1046  73  VAL B CB  
2850 C  CG1 . VAL B 97  ? 0.5360 0.5752 0.6954 0.1412  0.0487  0.1129  73  VAL B CG1 
2851 C  CG2 . VAL B 97  ? 0.4898 0.5436 0.6679 0.1497  0.0552  0.1119  73  VAL B CG2 
2852 N  N   . ILE B 98  ? 0.5389 0.5375 0.6718 0.1270  0.0574  0.0813  74  ILE B N   
2853 C  CA  . ILE B 98  ? 0.5185 0.5042 0.6379 0.1193  0.0554  0.0749  74  ILE B CA  
2854 C  C   . ILE B 98  ? 0.5494 0.5115 0.6662 0.1205  0.0621  0.0688  74  ILE B C   
2855 O  O   . ILE B 98  ? 0.5744 0.5233 0.6868 0.1181  0.0617  0.0690  74  ILE B O   
2856 C  CB  . ILE B 98  ? 0.4976 0.4902 0.6070 0.1111  0.0515  0.0667  74  ILE B CB  
2857 C  CG1 . ILE B 98  ? 0.4693 0.4843 0.5812 0.1093  0.0443  0.0720  74  ILE B CG1 
2858 C  CG2 . ILE B 98  ? 0.4512 0.4300 0.5473 0.1037  0.0500  0.0602  74  ILE B CG2 
2859 C  CD1 . ILE B 98  ? 0.4027 0.4254 0.5082 0.1021  0.0410  0.0644  74  ILE B CD1 
2860 N  N   . LYS B 99  ? 0.5445 0.5013 0.6638 0.1240  0.0682  0.0630  75  LYS B N   
2861 C  CA  . LYS B 99  ? 0.5880 0.5226 0.7037 0.1250  0.0745  0.0554  75  LYS B CA  
2862 C  C   . LYS B 99  ? 0.5801 0.5023 0.7040 0.1304  0.0771  0.0619  75  LYS B C   
2863 O  O   . LYS B 99  ? 0.6005 0.5041 0.7194 0.1277  0.0786  0.0574  75  LYS B O   
2864 C  CB  . LYS B 99  ? 0.5955 0.5291 0.7140 0.1297  0.0813  0.0494  75  LYS B CB  
2865 C  CG  . LYS B 99  ? 0.5973 0.5091 0.7088 0.1296  0.0872  0.0388  75  LYS B CG  
2866 C  CD  . LYS B 99  ? 0.5745 0.4860 0.6899 0.1361  0.0949  0.0341  75  LYS B CD  
2867 C  CE  . LYS B 99  ? 0.6035 0.4921 0.7140 0.1380  0.1013  0.0245  75  LYS B CE  
2868 N  NZ  . LYS B 99  ? 0.7060 0.5942 0.8197 0.1452  0.1095  0.0196  75  LYS B NZ  
2869 N  N   . GLN B 100 ? 0.5704 0.5027 0.7076 0.1380  0.0776  0.0730  76  GLN B N   
2870 C  CA  . GLN B 100 ? 0.6392 0.5601 0.7859 0.1438  0.0804  0.0806  76  GLN B CA  
2871 C  C   . GLN B 100 ? 0.6249 0.5413 0.7666 0.1383  0.0755  0.0850  76  GLN B C   
2872 O  O   . GLN B 100 ? 0.6859 0.5855 0.8314 0.1399  0.0784  0.0872  76  GLN B O   
2873 C  CB  . GLN B 100 ? 0.6785 0.6142 0.8406 0.1531  0.0812  0.0929  76  GLN B CB  
2874 C  CG  . GLN B 100 ? 0.7949 0.7269 0.9670 0.1618  0.0891  0.0907  76  GLN B CG  
2875 C  CD  . GLN B 100 ? 0.9567 0.8640 1.1333 0.1665  0.0962  0.0880  76  GLN B CD  
2876 O  OE1 . GLN B 100 ? 0.9913 0.8904 1.1737 0.1683  0.0959  0.0957  76  GLN B OE1 
2877 N  NE2 . GLN B 100 ? 1.0015 0.8970 1.1757 0.1684  0.1029  0.0769  76  GLN B NE2 
2878 N  N   . ALA B 101 ? 0.6083 0.5391 0.7419 0.1319  0.0684  0.0864  77  ALA B N   
2879 C  CA  . ALA B 101 ? 0.5930 0.5230 0.7221 0.1272  0.0638  0.0918  77  ALA B CA  
2880 C  C   . ALA B 101 ? 0.6079 0.5265 0.7235 0.1178  0.0621  0.0816  77  ALA B C   
2881 O  O   . ALA B 101 ? 0.6301 0.5434 0.7427 0.1141  0.0598  0.0851  77  ALA B O   
2882 C  CB  . ALA B 101 ? 0.5259 0.4800 0.6546 0.1266  0.0569  0.1001  77  ALA B CB  
2883 N  N   . SER B 102 ? 0.6047 0.5197 0.7124 0.1141  0.0633  0.0698  78  SER B N   
2884 C  CA  . SER B 102 ? 0.5790 0.4862 0.6737 0.1051  0.0609  0.0607  78  SER B CA  
2885 C  C   . SER B 102 ? 0.5781 0.4740 0.6675 0.1040  0.0652  0.0484  78  SER B C   
2886 O  O   . SER B 102 ? 0.5607 0.4616 0.6539 0.1088  0.0687  0.0464  78  SER B O   
2887 C  CB  . SER B 102 ? 0.5587 0.4835 0.6457 0.0994  0.0542  0.0610  78  SER B CB  
2888 O  OG  . SER B 102 ? 0.5330 0.4519 0.6081 0.0916  0.0526  0.0508  78  SER B OG  
2889 N  N   . ASP B 103 ? 0.5805 0.4618 0.6610 0.0979  0.0651  0.0403  79  ASP B N   
2890 C  CA  . ASP B 103 ? 0.6060 0.4777 0.6785 0.0956  0.0682  0.0280  79  ASP B CA  
2891 C  C   . ASP B 103 ? 0.5894 0.4701 0.6502 0.0882  0.0638  0.0222  79  ASP B C   
2892 O  O   . ASP B 103 ? 0.5857 0.4578 0.6374 0.0843  0.0649  0.0124  79  ASP B O   
2893 C  CB  . ASP B 103 ? 0.6471 0.4967 0.7177 0.0937  0.0708  0.0218  79  ASP B CB  
2894 C  CG  . ASP B 103 ? 0.7503 0.5959 0.8157 0.0859  0.0658  0.0228  79  ASP B CG  
2895 O  OD1 . ASP B 103 ? 0.7634 0.6208 0.8309 0.0848  0.0616  0.0318  79  ASP B OD1 
2896 O  OD2 . ASP B 103 ? 0.7966 0.6277 0.8559 0.0811  0.0660  0.0144  79  ASP B OD2 
2897 N  N   . ALA B 104 ? 0.5258 0.4234 0.5866 0.0863  0.0587  0.0282  80  ALA B N   
2898 C  CA  . ALA B 104 ? 0.5194 0.4258 0.5706 0.0798  0.0548  0.0233  80  ALA B CA  
2899 C  C   . ALA B 104 ? 0.5005 0.4107 0.5499 0.0812  0.0581  0.0172  80  ALA B C   
2900 O  O   . ALA B 104 ? 0.5113 0.4242 0.5686 0.0879  0.0625  0.0191  80  ALA B O   
2901 C  CB  . ALA B 104 ? 0.4538 0.3781 0.5070 0.0785  0.0491  0.0306  80  ALA B CB  
2902 N  N   . VAL B 105 ? 0.4887 0.3995 0.5281 0.0751  0.0563  0.0103  81  VAL B N   
2903 C  CA  . VAL B 105 ? 0.4525 0.3689 0.4897 0.0758  0.0591  0.0055  81  VAL B CA  
2904 C  C   . VAL B 105 ? 0.4409 0.3766 0.4849 0.0768  0.0564  0.0114  81  VAL B C   
2905 O  O   . VAL B 105 ? 0.4565 0.4010 0.4989 0.0723  0.0506  0.0141  81  VAL B O   
2906 C  CB  . VAL B 105 ? 0.4630 0.3746 0.4878 0.0690  0.0578  -0.0026 81  VAL B CB  
2907 C  CG1 . VAL B 105 ? 0.4207 0.3383 0.4434 0.0701  0.0614  -0.0066 81  VAL B CG1 
2908 C  CG2 . VAL B 105 ? 0.4910 0.3845 0.5095 0.0674  0.0593  -0.0086 81  VAL B CG2 
2909 N  N   . LEU B 106 ? 0.4189 0.3613 0.4706 0.0825  0.0606  0.0130  82  LEU B N   
2910 C  CA  . LEU B 106 ? 0.4528 0.4140 0.5125 0.0835  0.0582  0.0184  82  LEU B CA  
2911 C  C   . LEU B 106 ? 0.4511 0.4186 0.5069 0.0799  0.0591  0.0136  82  LEU B C   
2912 O  O   . LEU B 106 ? 0.4230 0.3851 0.4764 0.0821  0.0650  0.0089  82  LEU B O   
2913 C  CB  . LEU B 106 ? 0.4285 0.3955 0.5013 0.0920  0.0620  0.0246  82  LEU B CB  
2914 C  CG  . LEU B 106 ? 0.4669 0.4276 0.5450 0.0963  0.0617  0.0307  82  LEU B CG  
2915 C  CD1 . LEU B 106 ? 0.4395 0.4118 0.5319 0.1041  0.0633  0.0391  82  LEU B CD1 
2916 C  CD2 . LEU B 106 ? 0.4411 0.4033 0.5144 0.0909  0.0548  0.0336  82  LEU B CD2 
2917 N  N   . ASN B 107 ? 0.4069 0.3856 0.4619 0.0744  0.0534  0.0147  83  ASN B N   
2918 C  CA  . ASN B 107 ? 0.3988 0.3830 0.4502 0.0697  0.0532  0.0108  83  ASN B CA  
2919 C  C   . ASN B 107 ? 0.4245 0.4269 0.4873 0.0705  0.0513  0.0157  83  ASN B C   
2920 O  O   . ASN B 107 ? 0.4237 0.4357 0.4903 0.0683  0.0451  0.0193  83  ASN B O   
2921 C  CB  . ASN B 107 ? 0.4275 0.4075 0.4686 0.0621  0.0480  0.0073  83  ASN B CB  
2922 C  CG  . ASN B 107 ? 0.4437 0.4311 0.4829 0.0569  0.0466  0.0048  83  ASN B CG  
2923 O  OD1 . ASN B 107 ? 0.4657 0.4610 0.5108 0.0585  0.0498  0.0057  83  ASN B OD1 
2924 N  ND2 . ASN B 107 ? 0.4781 0.4627 0.5097 0.0507  0.0422  0.0022  83  ASN B ND2 
2925 N  N   . ILE B 108 ? 0.4182 0.4260 0.4868 0.0737  0.0566  0.0157  84  ILE B N   
2926 C  CA  . ILE B 108 ? 0.4331 0.4586 0.5149 0.0750  0.0555  0.0208  84  ILE B CA  
2927 C  C   . ILE B 108 ? 0.4317 0.4648 0.5128 0.0683  0.0532  0.0187  84  ILE B C   
2928 O  O   . ILE B 108 ? 0.4144 0.4412 0.4881 0.0661  0.0568  0.0144  84  ILE B O   
2929 C  CB  . ILE B 108 ? 0.4086 0.4370 0.4993 0.0828  0.0631  0.0231  84  ILE B CB  
2930 C  CG1 . ILE B 108 ? 0.4339 0.4544 0.5271 0.0898  0.0654  0.0257  84  ILE B CG1 
2931 C  CG2 . ILE B 108 ? 0.3977 0.4460 0.5033 0.0836  0.0619  0.0285  84  ILE B CG2 
2932 C  CD1 . ILE B 108 ? 0.4387 0.4606 0.5409 0.0984  0.0734  0.0277  84  ILE B CD1 
2933 N  N   . THR B 109 ? 0.4157 0.4627 0.5047 0.0651  0.0470  0.0218  85  THR B N   
2934 C  CA  . THR B 109 ? 0.4137 0.4678 0.5041 0.0586  0.0444  0.0201  85  THR B CA  
2935 C  C   . THR B 109 ? 0.4527 0.5143 0.5515 0.0604  0.0505  0.0216  85  THR B C   
2936 O  O   . THR B 109 ? 0.4344 0.5034 0.5435 0.0664  0.0541  0.0257  85  THR B O   
2937 C  CB  . THR B 109 ? 0.4337 0.5010 0.5315 0.0549  0.0362  0.0224  85  THR B CB  
2938 O  OG1 . THR B 109 ? 0.4149 0.4864 0.5135 0.0479  0.0334  0.0198  85  THR B OG1 
2939 C  CG2 . THR B 109 ? 0.4434 0.5260 0.5564 0.0596  0.0361  0.0284  85  THR B CG2 
2940 N  N   . THR B 110 ? 0.4374 0.4974 0.5322 0.0555  0.0519  0.0188  86  THR B N   
2941 C  CA  . THR B 110 ? 0.4564 0.5266 0.5607 0.0554  0.0563  0.0212  86  THR B CA  
2942 C  C   . THR B 110 ? 0.5154 0.5961 0.6276 0.0482  0.0506  0.0221  86  THR B C   
2943 O  O   . THR B 110 ? 0.5140 0.6034 0.6351 0.0466  0.0536  0.0245  86  THR B O   
2944 C  CB  . THR B 110 ? 0.4390 0.5001 0.5335 0.0563  0.0637  0.0183  86  THR B CB  
2945 O  OG1 . THR B 110 ? 0.4628 0.5163 0.5468 0.0496  0.0606  0.0146  86  THR B OG1 
2946 C  CG2 . THR B 110 ? 0.4616 0.5103 0.5471 0.0629  0.0690  0.0157  86  THR B CG2 
2947 N  N   . GLY B 111 ? 0.5892 0.6692 0.6988 0.0437  0.0426  0.0203  87  GLY B N   
2948 C  CA  . GLY B 111 ? 0.5960 0.6846 0.7129 0.0368  0.0366  0.0199  87  GLY B CA  
2949 C  C   . GLY B 111 ? 0.7085 0.8126 0.8392 0.0371  0.0311  0.0232  87  GLY B C   
2950 O  O   . GLY B 111 ? 0.7680 0.8841 0.9117 0.0334  0.0293  0.0249  87  GLY B O   
2951 N  N   . GLY B 112 ? 0.7909 0.8954 0.9197 0.0413  0.0284  0.0244  88  GLY B N   
2952 C  CA  . GLY B 112 ? 0.8040 0.9239 0.9445 0.0416  0.0221  0.0274  88  GLY B CA  
2953 C  C   . GLY B 112 ? 0.8476 0.9731 0.9903 0.0337  0.0141  0.0239  88  GLY B C   
2954 O  O   . GLY B 112 ? 0.8351 0.9504 0.9668 0.0293  0.0119  0.0191  88  GLY B O   
2955 N  N   . ALA B 113 ? 0.7680 0.9101 0.9256 0.0318  0.0097  0.0261  89  ALA B N   
2956 C  CA  . ALA B 113 ? 0.7378 0.8852 0.8994 0.0238  0.0025  0.0220  89  ALA B CA  
2957 C  C   . ALA B 113 ? 0.7767 0.9188 0.9408 0.0187  0.0066  0.0203  89  ALA B C   
2958 O  O   . ALA B 113 ? 0.7995 0.9436 0.9703 0.0210  0.0136  0.0242  89  ALA B O   
2959 C  CB  . ALA B 113 ? 0.6772 0.8444 0.8552 0.0227  -0.0036 0.0245  89  ALA B CB  
2960 N  N   . PRO B 114 ? 0.7235 0.8591 0.8825 0.0122  0.0027  0.0150  90  PRO B N   
2961 C  CA  . PRO B 114 ? 0.6959 0.8252 0.8565 0.0077  0.0069  0.0142  90  PRO B CA  
2962 C  C   . PRO B 114 ? 0.6945 0.8367 0.8743 0.0045  0.0080  0.0179  90  PRO B C   
2963 O  O   . PRO B 114 ? 0.6304 0.7685 0.8129 0.0009  0.0119  0.0185  90  PRO B O   
2964 C  CB  . PRO B 114 ? 0.6599 0.7815 0.8132 0.0016  0.0010  0.0078  90  PRO B CB  
2965 C  CG  . PRO B 114 ? 0.7099 0.8400 0.8644 0.0012  -0.0075 0.0052  90  PRO B CG  
2966 C  CD  . PRO B 114 ? 0.7274 0.8624 0.8801 0.0088  -0.0057 0.0097  90  PRO B CD  
2967 N  N   . THR B 115 ? 0.7400 0.8981 0.9336 0.0058  0.0049  0.0209  91  THR B N   
2968 C  CA  . THR B 115 ? 0.7137 0.8857 0.9276 0.0023  0.0053  0.0246  91  THR B CA  
2969 C  C   . THR B 115 ? 0.6969 0.8767 0.9189 0.0089  0.0133  0.0318  91  THR B C   
2970 O  O   . THR B 115 ? 0.7307 0.9265 0.9709 0.0082  0.0124  0.0360  91  THR B O   
2971 C  CB  . THR B 115 ? 0.7271 0.9134 0.9526 -0.0018 -0.0048 0.0224  91  THR B CB  
2972 O  OG1 . THR B 115 ? 0.7245 0.9174 0.9467 0.0045  -0.0075 0.0241  91  THR B OG1 
2973 C  CG2 . THR B 115 ? 0.6765 0.8554 0.8951 -0.0085 -0.0122 0.0144  91  THR B CG2 
2974 N  N   . MET B 116 ? 0.7080 0.8769 0.9173 0.0153  0.0211  0.0332  92  MET B N   
2975 C  CA  . MET B 116 ? 0.7118 0.8866 0.9263 0.0230  0.0289  0.0390  92  MET B CA  
2976 C  C   . MET B 116 ? 0.7256 0.8939 0.9370 0.0243  0.0390  0.0412  92  MET B C   
2977 O  O   . MET B 116 ? 0.6945 0.8519 0.8970 0.0200  0.0400  0.0384  92  MET B O   
2978 C  CB  . MET B 116 ? 0.7488 0.9171 0.9514 0.0307  0.0294  0.0386  92  MET B CB  
2979 C  CG  . MET B 116 ? 0.7660 0.9443 0.9733 0.0312  0.0205  0.0388  92  MET B CG  
2980 S  SD  . MET B 116 ? 0.8164 0.9889 1.0137 0.0412  0.0227  0.0409  92  MET B SD  
2981 C  CE  . MET B 116 ? 0.6123 0.7982 0.8147 0.0400  0.0111  0.0412  92  MET B CE  
2982 N  N   . SER B 117 ? 0.7447 0.9206 0.9638 0.0307  0.0466  0.0466  93  SER B N   
2983 C  CA  . SER B 117 ? 0.6734 0.8473 0.8917 0.0329  0.0569  0.0496  93  SER B CA  
2984 C  C   . SER B 117 ? 0.7023 0.8608 0.9012 0.0398  0.0634  0.0469  93  SER B C   
2985 O  O   . SER B 117 ? 0.7184 0.8675 0.9057 0.0422  0.0598  0.0431  93  SER B O   
2986 C  CB  . SER B 117 ? 0.5853 0.7771 0.8235 0.0361  0.0618  0.0567  93  SER B CB  
2987 O  OG  . SER B 117 ? 0.6502 0.8399 0.8851 0.0409  0.0730  0.0597  93  SER B OG  
2988 N  N   . ILE B 118 ? 0.6980 0.8545 0.8935 0.0432  0.0732  0.0490  94  ILE B N   
2989 C  CA  . ILE B 118 ? 0.7083 0.8487 0.8836 0.0480  0.0788  0.0449  94  ILE B CA  
2990 C  C   . ILE B 118 ? 0.7055 0.8466 0.8803 0.0580  0.0861  0.0462  94  ILE B C   
2991 O  O   . ILE B 118 ? 0.6741 0.8079 0.8423 0.0622  0.0838  0.0434  94  ILE B O   
2992 C  CB  . ILE B 118 ? 0.6638 0.7992 0.8313 0.0452  0.0845  0.0451  94  ILE B CB  
2993 C  CG1 . ILE B 118 ? 0.6471 0.7781 0.8129 0.0359  0.0771  0.0431  94  ILE B CG1 
2994 C  CG2 . ILE B 118 ? 0.5932 0.7138 0.7404 0.0506  0.0905  0.0407  94  ILE B CG2 
2995 C  CD1 . ILE B 118 ? 0.6435 0.7608 0.7948 0.0341  0.0698  0.0366  94  ILE B CD1 
2996 N  N   . ALA B 119 ? 0.7716 0.9205 0.9528 0.0621  0.0954  0.0503  95  ALA B N   
2997 C  CA  . ALA B 119 ? 0.7611 0.9096 0.9412 0.0722  0.1034  0.0508  95  ALA B CA  
2998 C  C   . ALA B 119 ? 0.7699 0.9225 0.9586 0.0765  0.0988  0.0520  95  ALA B C   
2999 O  O   . ALA B 119 ? 0.7603 0.9056 0.9431 0.0843  0.1029  0.0502  95  ALA B O   
3000 C  CB  . ALA B 119 ? 0.6960 0.8582 0.8881 0.0759  0.1130  0.0567  95  ALA B CB  
3001 N  N   . GLU B 120 ? 0.6726 0.8367 0.8750 0.0713  0.0902  0.0549  96  GLU B N   
3002 C  CA  . GLU B 120 ? 0.6003 0.7686 0.8091 0.0745  0.0843  0.0562  96  GLU B CA  
3003 C  C   . GLU B 120 ? 0.6575 0.8102 0.8502 0.0726  0.0776  0.0505  96  GLU B C   
3004 O  O   . GLU B 120 ? 0.6596 0.8074 0.8492 0.0786  0.0772  0.0504  96  GLU B O   
3005 C  CB  . GLU B 120 ? 0.6508 0.8384 0.8798 0.0696  0.0772  0.0611  96  GLU B CB  
3006 C  CG  . GLU B 120 ? 0.6659 0.8525 0.8931 0.0589  0.0679  0.0579  96  GLU B CG  
3007 C  CD  . GLU B 120 ? 0.7060 0.8893 0.9279 0.0570  0.0577  0.0548  96  GLU B CD  
3008 O  OE1 . GLU B 120 ? 0.6944 0.8737 0.9117 0.0637  0.0580  0.0552  96  GLU B OE1 
3009 O  OE2 . GLU B 120 ? 0.7105 0.8953 0.9331 0.0488  0.0495  0.0522  96  GLU B OE2 
3010 N  N   . ARG B 121 ? 0.6679 0.8129 0.8508 0.0646  0.0725  0.0463  97  ARG B N   
3011 C  CA  . ARG B 121 ? 0.6125 0.7440 0.7809 0.0626  0.0662  0.0413  97  ARG B CA  
3012 C  C   . ARG B 121 ? 0.5452 0.6600 0.6982 0.0687  0.0720  0.0377  97  ARG B C   
3013 O  O   . ARG B 121 ? 0.5049 0.6106 0.6498 0.0700  0.0681  0.0355  97  ARG B O   
3014 C  CB  . ARG B 121 ? 0.6023 0.7279 0.7630 0.0534  0.0609  0.0373  97  ARG B CB  
3015 C  CG  . ARG B 121 ? 0.6644 0.7981 0.8323 0.0471  0.0503  0.0370  97  ARG B CG  
3016 C  CD  . ARG B 121 ? 0.6665 0.7956 0.8299 0.0382  0.0459  0.0333  97  ARG B CD  
3017 N  NE  . ARG B 121 ? 0.6516 0.7640 0.7973 0.0375  0.0492  0.0291  97  ARG B NE  
3018 C  CZ  . ARG B 121 ? 0.5851 0.6925 0.7267 0.0315  0.0489  0.0272  97  ARG B CZ  
3019 N  NH1 . ARG B 121 ? 0.5409 0.6577 0.6950 0.0255  0.0462  0.0290  97  ARG B NH1 
3020 N  NH2 . ARG B 121 ? 0.5139 0.6069 0.6391 0.0314  0.0513  0.0236  97  ARG B NH2 
3021 N  N   . ILE B 122 ? 0.5012 0.6118 0.6496 0.0724  0.0812  0.0369  98  ILE B N   
3022 C  CA  . ILE B 122 ? 0.5668 0.6611 0.7001 0.0777  0.0866  0.0323  98  ILE B CA  
3023 C  C   . ILE B 122 ? 0.5283 0.6238 0.6682 0.0873  0.0918  0.0346  98  ILE B C   
3024 O  O   . ILE B 122 ? 0.5069 0.5885 0.6360 0.0924  0.0966  0.0304  98  ILE B O   
3025 C  CB  . ILE B 122 ? 0.5879 0.6763 0.7108 0.0773  0.0940  0.0293  98  ILE B CB  
3026 C  CG1 . ILE B 122 ? 0.5959 0.6976 0.7307 0.0817  0.1024  0.0340  98  ILE B CG1 
3027 C  CG2 . ILE B 122 ? 0.5663 0.6527 0.6829 0.0681  0.0892  0.0276  98  ILE B CG2 
3028 C  CD1 . ILE B 122 ? 0.5777 0.6730 0.7001 0.0839  0.1113  0.0310  98  ILE B CD1 
3029 N  N   . GLN B 123 ? 0.5236 0.6353 0.6816 0.0900  0.0907  0.0410  99  GLN B N   
3030 C  CA  . GLN B 123 ? 0.5248 0.6389 0.6908 0.1000  0.0967  0.0440  99  GLN B CA  
3031 C  C   . GLN B 123 ? 0.4728 0.5744 0.6323 0.1039  0.0939  0.0424  99  GLN B C   
3032 O  O   . GLN B 123 ? 0.4598 0.5508 0.6149 0.1114  0.1008  0.0403  99  GLN B O   
3033 C  CB  . GLN B 123 ? 0.5139 0.6498 0.7018 0.1017  0.0955  0.0520  99  GLN B CB  
3034 C  CG  . GLN B 123 ? 0.5354 0.6831 0.7321 0.1018  0.1027  0.0547  99  GLN B CG  
3035 C  CD  . GLN B 123 ? 0.5332 0.7017 0.7526 0.1060  0.1038  0.0627  99  GLN B CD  
3036 O  OE1 . GLN B 123 ? 0.5412 0.7170 0.7684 0.1116  0.1130  0.0656  99  GLN B OE1 
3037 N  NE2 . GLN B 123 ? 0.5408 0.7198 0.7709 0.1033  0.0945  0.0664  99  GLN B NE2 
3038 N  N   . PRO B 124 ? 0.4622 0.5642 0.6210 0.0995  0.0844  0.0433  100 PRO B N   
3039 C  CA  . PRO B 124 ? 0.4772 0.5664 0.6292 0.1031  0.0824  0.0423  100 PRO B CA  
3040 C  C   . PRO B 124 ? 0.4940 0.5619 0.6287 0.1039  0.0873  0.0350  100 PRO B C   
3041 O  O   . PRO B 124 ? 0.4632 0.5212 0.5968 0.1112  0.0925  0.0341  100 PRO B O   
3042 C  CB  . PRO B 124 ? 0.4722 0.5653 0.6227 0.0960  0.0715  0.0432  100 PRO B CB  
3043 C  CG  . PRO B 124 ? 0.4396 0.5524 0.6035 0.0919  0.0677  0.0470  100 PRO B CG  
3044 C  CD  . PRO B 124 ? 0.4870 0.6017 0.6523 0.0916  0.0753  0.0456  100 PRO B CD  
3045 N  N   . ALA B 125 ? 0.4591 0.5199 0.5811 0.0967  0.0856  0.0295  101 ALA B N   
3046 C  CA  . ALA B 125 ? 0.4666 0.5086 0.5721 0.0970  0.0895  0.0222  101 ALA B CA  
3047 C  C   . ALA B 125 ? 0.4888 0.5280 0.5936 0.1037  0.1000  0.0199  101 ALA B C   
3048 O  O   . ALA B 125 ? 0.4763 0.5003 0.5719 0.1078  0.1045  0.0147  101 ALA B O   
3049 C  CB  . ALA B 125 ? 0.4902 0.5279 0.5837 0.0880  0.0854  0.0178  101 ALA B CB  
3050 N  N   . GLN B 126 ? 0.4849 0.5387 0.5994 0.1050  0.1042  0.0234  102 GLN B N   
3051 C  CA  . GLN B 126 ? 0.5045 0.5576 0.6187 0.1120  0.1148  0.0217  102 GLN B CA  
3052 C  C   . GLN B 126 ? 0.4810 0.5299 0.6022 0.1219  0.1196  0.0229  102 GLN B C   
3053 O  O   . GLN B 126 ? 0.4934 0.5296 0.6064 0.1276  0.1267  0.0172  102 GLN B O   
3054 C  CB  . GLN B 126 ? 0.5113 0.5833 0.6375 0.1114  0.1181  0.0270  102 GLN B CB  
3055 C  CG  . GLN B 126 ? 0.4953 0.5674 0.6176 0.1169  0.1292  0.0247  102 GLN B CG  
3056 C  CD  . GLN B 126 ? 0.5754 0.6669 0.7106 0.1156  0.1324  0.0310  102 GLN B CD  
3057 O  OE1 . GLN B 126 ? 0.5668 0.6726 0.7171 0.1119  0.1266  0.0374  102 GLN B OE1 
3058 N  NE2 . GLN B 126 ? 0.5569 0.6496 0.6865 0.1186  0.1415  0.0293  102 GLN B NE2 
3059 N  N   . HIS B 127 ? 0.4649 0.5242 0.6013 0.1243  0.1156  0.0301  103 HIS B N   
3060 C  CA  . HIS B 127 ? 0.4691 0.5259 0.6145 0.1341  0.1200  0.0328  103 HIS B CA  
3061 C  C   . HIS B 127 ? 0.4866 0.5230 0.6217 0.1353  0.1183  0.0283  103 HIS B C   
3062 O  O   . HIS B 127 ? 0.4824 0.5065 0.6152 0.1427  0.1254  0.0247  103 HIS B O   
3063 C  CB  . HIS B 127 ? 0.5092 0.5845 0.6739 0.1359  0.1153  0.0426  103 HIS B CB  
3064 C  CG  . HIS B 127 ? 0.5128 0.5859 0.6876 0.1456  0.1183  0.0469  103 HIS B CG  
3065 N  ND1 . HIS B 127 ? 0.5190 0.5945 0.7028 0.1555  0.1281  0.0482  103 HIS B ND1 
3066 C  CD2 . HIS B 127 ? 0.4961 0.5647 0.6737 0.1474  0.1130  0.0506  103 HIS B CD2 
3067 C  CE1 . HIS B 127 ? 0.5290 0.6011 0.7213 0.1629  0.1286  0.0525  103 HIS B CE1 
3068 N  NE2 . HIS B 127 ? 0.5652 0.6333 0.7540 0.1581  0.1195  0.0544  103 HIS B NE2 
3069 N  N   . TYR B 128 ? 0.5054 0.5378 0.6346 0.1282  0.1092  0.0283  104 TYR B N   
3070 C  CA  . TYR B 128 ? 0.4982 0.5137 0.6208 0.1292  0.1069  0.0262  104 TYR B CA  
3071 C  C   . TYR B 128 ? 0.4822 0.4780 0.5866 0.1261  0.1091  0.0162  104 TYR B C   
3072 O  O   . TYR B 128 ? 0.5105 0.4903 0.6103 0.1280  0.1094  0.0133  104 TYR B O   
3073 C  CB  . TYR B 128 ? 0.4858 0.5065 0.6101 0.1234  0.0966  0.0310  104 TYR B CB  
3074 C  CG  . TYR B 128 ? 0.4799 0.5179 0.6216 0.1274  0.0937  0.0409  104 TYR B CG  
3075 C  CD1 . TYR B 128 ? 0.4775 0.5131 0.6290 0.1364  0.0970  0.0458  104 TYR B CD1 
3076 C  CD2 . TYR B 128 ? 0.4751 0.5318 0.6239 0.1223  0.0873  0.0453  104 TYR B CD2 
3077 C  CE1 . TYR B 128 ? 0.4725 0.5251 0.6400 0.1404  0.0940  0.0555  104 TYR B CE1 
3078 C  CE2 . TYR B 128 ? 0.4678 0.5415 0.6323 0.1258  0.0840  0.0540  104 TYR B CE2 
3079 C  CZ  . TYR B 128 ? 0.4965 0.5685 0.6701 0.1349  0.0872  0.0594  104 TYR B CZ  
3080 O  OH  . TYR B 128 ? 0.4797 0.5698 0.6691 0.1386  0.0835  0.0687  104 TYR B OH  
3081 N  N   . ARG B 129 ? 0.4570 0.4540 0.5518 0.1213  0.1106  0.0111  105 ARG B N   
3082 C  CA  . ARG B 129 ? 0.4834 0.4638 0.5606 0.1183  0.1125  0.0016  105 ARG B CA  
3083 C  C   . ARG B 129 ? 0.5093 0.4761 0.5786 0.1133  0.1057  -0.0007 105 ARG B C   
3084 O  O   . ARG B 129 ? 0.5038 0.4539 0.5672 0.1159  0.1081  -0.0059 105 ARG B O   
3085 C  CB  . ARG B 129 ? 0.5409 0.5111 0.6154 0.1266  0.1223  -0.0041 105 ARG B CB  
3086 C  CG  . ARG B 129 ? 0.5947 0.5772 0.6732 0.1310  0.1301  -0.0034 105 ARG B CG  
3087 C  CD  . ARG B 129 ? 0.6706 0.6419 0.7435 0.1390  0.1401  -0.0107 105 ARG B CD  
3088 N  NE  . ARG B 129 ? 0.7030 0.6686 0.7872 0.1478  0.1437  -0.0085 105 ARG B NE  
3089 C  CZ  . ARG B 129 ? 0.7506 0.7289 0.8512 0.1555  0.1484  -0.0015 105 ARG B CZ  
3090 N  NH1 . ARG B 129 ? 0.7135 0.7115 0.8221 0.1550  0.1498  0.0042  105 ARG B NH1 
3091 N  NH2 . ARG B 129 ? 0.6831 0.6543 0.7934 0.1638  0.1518  0.0002  105 ARG B NH2 
3092 N  N   . PRO B 130 ? 0.5017 0.4752 0.5711 0.1062  0.0973  0.0029  106 PRO B N   
3093 C  CA  . PRO B 130 ? 0.4735 0.4356 0.5358 0.1015  0.0910  0.0014  106 PRO B CA  
3094 C  C   . PRO B 130 ? 0.4743 0.4230 0.5201 0.0962  0.0910  -0.0074 106 PRO B C   
3095 O  O   . PRO B 130 ? 0.5036 0.4534 0.5422 0.0952  0.0946  -0.0119 106 PRO B O   
3096 C  CB  . PRO B 130 ? 0.4458 0.4218 0.5130 0.0957  0.0829  0.0074  106 PRO B CB  
3097 C  CG  . PRO B 130 ? 0.4538 0.4434 0.5236 0.0938  0.0843  0.0080  106 PRO B CG  
3098 C  CD  . PRO B 130 ? 0.4566 0.4484 0.5329 0.1020  0.0932  0.0082  106 PRO B CD  
3099 N  N   . GLU B 131 ? 0.4620 0.3986 0.5020 0.0928  0.0866  -0.0093 107 GLU B N   
3100 C  CA  . GLU B 131 ? 0.4848 0.4101 0.5100 0.0868  0.0849  -0.0170 107 GLU B CA  
3101 C  C   . GLU B 131 ? 0.4552 0.3902 0.4752 0.0794  0.0801  -0.0164 107 GLU B C   
3102 O  O   . GLU B 131 ? 0.4519 0.3834 0.4608 0.0760  0.0811  -0.0221 107 GLU B O   
3103 C  CB  . GLU B 131 ? 0.4672 0.3791 0.4898 0.0845  0.0810  -0.0179 107 GLU B CB  
3104 C  CG  . GLU B 131 ? 0.5272 0.4278 0.5562 0.0914  0.0853  -0.0178 107 GLU B CG  
3105 C  CD  . GLU B 131 ? 0.5273 0.4143 0.5540 0.0882  0.0815  -0.0185 107 GLU B CD  
3106 O  OE1 . GLU B 131 ? 0.5114 0.3855 0.5277 0.0846  0.0815  -0.0265 107 GLU B OE1 
3107 O  OE2 . GLU B 131 ? 0.5256 0.4157 0.5608 0.0891  0.0783  -0.0107 107 GLU B OE2 
3108 N  N   . LEU B 132 ? 0.4344 0.3817 0.4623 0.0770  0.0749  -0.0098 108 LEU B N   
3109 C  CA  . LEU B 132 ? 0.4499 0.4056 0.4745 0.0699  0.0698  -0.0091 108 LEU B CA  
3110 C  C   . LEU B 132 ? 0.4253 0.3984 0.4616 0.0707  0.0689  -0.0030 108 LEU B C   
3111 O  O   . LEU B 132 ? 0.4113 0.3912 0.4586 0.0748  0.0684  0.0024  108 LEU B O   
3112 C  CB  . LEU B 132 ? 0.4314 0.3832 0.4522 0.0645  0.0626  -0.0084 108 LEU B CB  
3113 C  CG  . LEU B 132 ? 0.4575 0.3975 0.4652 0.0591  0.0606  -0.0145 108 LEU B CG  
3114 C  CD1 . LEU B 132 ? 0.4421 0.3807 0.4492 0.0548  0.0540  -0.0122 108 LEU B CD1 
3115 C  CD2 . LEU B 132 ? 0.4576 0.4020 0.4586 0.0549  0.0609  -0.0173 108 LEU B CD2 
3116 N  N   . ALA B 133 ? 0.4245 0.4052 0.4591 0.0665  0.0685  -0.0036 109 ALA B N   
3117 C  CA  . ALA B 133 ? 0.4315 0.4285 0.4773 0.0649  0.0661  0.0017  109 ALA B CA  
3118 C  C   . ALA B 133 ? 0.4399 0.4393 0.4806 0.0570  0.0611  0.0004  109 ALA B C   
3119 O  O   . ALA B 133 ? 0.3875 0.3792 0.4173 0.0540  0.0622  -0.0039 109 ALA B O   
3120 C  CB  . ALA B 133 ? 0.4238 0.4299 0.4771 0.0693  0.0729  0.0036  109 ALA B CB  
3121 N  N   . SER B 134 ? 0.4197 0.4297 0.4685 0.0538  0.0553  0.0039  110 SER B N   
3122 C  CA  . SER B 134 ? 0.4105 0.4231 0.4565 0.0466  0.0509  0.0027  110 SER B CA  
3123 C  C   . SER B 134 ? 0.4424 0.4620 0.4921 0.0454  0.0549  0.0036  110 SER B C   
3124 O  O   . SER B 134 ? 0.4793 0.5066 0.5376 0.0496  0.0598  0.0064  110 SER B O   
3125 C  CB  . SER B 134 ? 0.4311 0.4531 0.4847 0.0437  0.0436  0.0053  110 SER B CB  
3126 O  OG  . SER B 134 ? 0.4613 0.4976 0.5288 0.0455  0.0439  0.0096  110 SER B OG  
3127 N  N   . LEU B 135 ? 0.4445 0.4616 0.4880 0.0398  0.0533  0.0016  111 LEU B N   
3128 C  CA  . LEU B 135 ? 0.4231 0.4461 0.4695 0.0382  0.0572  0.0032  111 LEU B CA  
3129 C  C   . LEU B 135 ? 0.4358 0.4604 0.4825 0.0310  0.0519  0.0031  111 LEU B C   
3130 O  O   . LEU B 135 ? 0.4176 0.4330 0.4533 0.0280  0.0500  0.0000  111 LEU B O   
3131 C  CB  . LEU B 135 ? 0.4367 0.4518 0.4717 0.0409  0.0638  0.0005  111 LEU B CB  
3132 C  CG  . LEU B 135 ? 0.4150 0.4366 0.4516 0.0401  0.0690  0.0029  111 LEU B CG  
3133 C  CD1 . LEU B 135 ? 0.4423 0.4777 0.4947 0.0429  0.0723  0.0081  111 LEU B CD1 
3134 C  CD2 . LEU B 135 ? 0.4627 0.4764 0.4858 0.0435  0.0752  -0.0006 111 LEU B CD2 
3135 N  N   . ASN B 136 ? 0.4246 0.4606 0.4844 0.0283  0.0496  0.0063  112 ASN B N   
3136 C  CA  . ASN B 136 ? 0.4368 0.4740 0.4988 0.0217  0.0447  0.0059  112 ASN B CA  
3137 C  C   . ASN B 136 ? 0.3883 0.4260 0.4495 0.0195  0.0491  0.0078  112 ASN B C   
3138 O  O   . ASN B 136 ? 0.3909 0.4352 0.4578 0.0220  0.0550  0.0113  112 ASN B O   
3139 C  CB  . ASN B 136 ? 0.3925 0.4413 0.4691 0.0193  0.0397  0.0078  112 ASN B CB  
3140 C  CG  . ASN B 136 ? 0.4721 0.5220 0.5490 0.0220  0.0354  0.0069  112 ASN B CG  
3141 O  OD1 . ASN B 136 ? 0.5191 0.5654 0.5913 0.0195  0.0296  0.0041  112 ASN B OD1 
3142 N  ND2 . ASN B 136 ? 0.4619 0.5170 0.5442 0.0277  0.0385  0.0096  112 ASN B ND2 
3143 N  N   . MET B 137 ? 0.4013 0.4324 0.4555 0.0151  0.0466  0.0061  113 MET B N   
3144 C  CA  . MET B 137 ? 0.3903 0.4187 0.4386 0.0140  0.0511  0.0077  113 MET B CA  
3145 C  C   . MET B 137 ? 0.3871 0.4217 0.4461 0.0089  0.0504  0.0115  113 MET B C   
3146 O  O   . MET B 137 ? 0.3853 0.4181 0.4400 0.0076  0.0536  0.0138  113 MET B O   
3147 C  CB  . MET B 137 ? 0.3893 0.4059 0.4220 0.0130  0.0493  0.0038  113 MET B CB  
3148 C  CG  . MET B 137 ? 0.3905 0.3998 0.4118 0.0179  0.0516  0.0003  113 MET B CG  
3149 S  SD  . MET B 137 ? 0.4321 0.4447 0.4514 0.0238  0.0608  0.0018  113 MET B SD  
3150 C  CE  . MET B 137 ? 0.3675 0.3823 0.3829 0.0207  0.0640  0.0052  113 MET B CE  
3151 N  N   . GLY B 138 ? 0.3634 0.4053 0.4364 0.0060  0.0462  0.0124  114 GLY B N   
3152 C  CA  . GLY B 138 ? 0.3621 0.4092 0.4469 0.0008  0.0456  0.0158  114 GLY B CA  
3153 C  C   . GLY B 138 ? 0.4210 0.4780 0.5227 -0.0017 0.0415  0.0163  114 GLY B C   
3154 O  O   . GLY B 138 ? 0.3890 0.4478 0.4915 -0.0004 0.0371  0.0132  114 GLY B O   
3155 N  N   . THR B 139 ? 0.4218 0.4859 0.5374 -0.0054 0.0430  0.0207  115 THR B N   
3156 C  CA  . THR B 139 ? 0.3826 0.4562 0.5156 -0.0092 0.0383  0.0209  115 THR B CA  
3157 C  C   . THR B 139 ? 0.4098 0.4778 0.5438 -0.0148 0.0309  0.0161  115 THR B C   
3158 O  O   . THR B 139 ? 0.4054 0.4654 0.5351 -0.0176 0.0312  0.0161  115 THR B O   
3159 C  CB  . THR B 139 ? 0.3970 0.4803 0.5460 -0.0115 0.0429  0.0276  115 THR B CB  
3160 O  OG1 . THR B 139 ? 0.4117 0.5007 0.5592 -0.0056 0.0505  0.0318  115 THR B OG1 
3161 C  CG2 . THR B 139 ? 0.4107 0.5047 0.5791 -0.0159 0.0375  0.0274  115 THR B CG2 
3162 N  N   . MET B 140 ? 0.3871 0.4596 0.5267 -0.0161 0.0242  0.0120  116 MET B N   
3163 C  CA  . MET B 140 ? 0.4070 0.4741 0.5453 -0.0204 0.0171  0.0061  116 MET B CA  
3164 C  C   . MET B 140 ? 0.4253 0.5026 0.5769 -0.0233 0.0105  0.0032  116 MET B C   
3165 O  O   . MET B 140 ? 0.3775 0.4654 0.5358 -0.0209 0.0107  0.0054  116 MET B O   
3166 C  CB  . MET B 140 ? 0.4093 0.4670 0.5296 -0.0171 0.0151  0.0015  116 MET B CB  
3167 C  CG  . MET B 140 ? 0.3974 0.4593 0.5127 -0.0118 0.0147  0.0011  116 MET B CG  
3168 S  SD  . MET B 140 ? 0.4135 0.4642 0.5088 -0.0079 0.0135  -0.0028 116 MET B SD  
3169 C  CE  . MET B 140 ? 0.3854 0.4364 0.4813 -0.0117 0.0047  -0.0091 116 MET B CE  
3170 N  N   . ASN B 141 ? 0.4014 0.4757 0.5569 -0.0286 0.0047  -0.0018 117 ASN B N   
3171 C  CA  . ASN B 141 ? 0.3949 0.4773 0.5584 -0.0311 -0.0030 -0.0068 117 ASN B CA  
3172 C  C   . ASN B 141 ? 0.4218 0.5035 0.5714 -0.0266 -0.0064 -0.0107 117 ASN B C   
3173 O  O   . ASN B 141 ? 0.3964 0.4679 0.5306 -0.0237 -0.0048 -0.0119 117 ASN B O   
3174 C  CB  . ASN B 141 ? 0.3841 0.4621 0.5544 -0.0377 -0.0081 -0.0123 117 ASN B CB  
3175 C  CG  . ASN B 141 ? 0.3880 0.4672 0.5749 -0.0429 -0.0053 -0.0081 117 ASN B CG  
3176 O  OD1 . ASN B 141 ? 0.3976 0.4856 0.5952 -0.0426 -0.0013 -0.0017 117 ASN B OD1 
3177 N  ND2 . ASN B 141 ? 0.3713 0.4419 0.5614 -0.0476 -0.0072 -0.0114 117 ASN B ND2 
3178 N  N   . PHE B 142 ? 0.4521 0.5455 0.6079 -0.0260 -0.0112 -0.0119 118 PHE B N   
3179 C  CA  . PHE B 142 ? 0.4554 0.5505 0.6003 -0.0223 -0.0156 -0.0152 118 PHE B CA  
3180 C  C   . PHE B 142 ? 0.4610 0.5629 0.6123 -0.0268 -0.0243 -0.0217 118 PHE B C   
3181 O  O   . PHE B 142 ? 0.4871 0.6010 0.6536 -0.0298 -0.0275 -0.0213 118 PHE B O   
3182 C  CB  . PHE B 142 ? 0.5418 0.6454 0.6872 -0.0163 -0.0131 -0.0099 118 PHE B CB  
3183 C  CG  . PHE B 142 ? 0.5996 0.6940 0.7298 -0.0102 -0.0079 -0.0075 118 PHE B CG  
3184 C  CD1 . PHE B 142 ? 0.6288 0.7164 0.7561 -0.0082 -0.0002 -0.0035 118 PHE B CD1 
3185 C  CD2 . PHE B 142 ? 0.6640 0.7569 0.7829 -0.0067 -0.0109 -0.0095 118 PHE B CD2 
3186 C  CE1 . PHE B 142 ? 0.6325 0.7115 0.7460 -0.0030 0.0040  -0.0024 118 PHE B CE1 
3187 C  CE2 . PHE B 142 ? 0.6953 0.7792 0.8015 -0.0016 -0.0064 -0.0075 118 PHE B CE2 
3188 C  CZ  . PHE B 142 ? 0.6590 0.7357 0.7626 0.0000  0.0008  -0.0044 118 PHE B CZ  
3189 N  N   . GLY B 143 ? 0.5090 0.6041 0.6490 -0.0273 -0.0281 -0.0280 119 GLY B N   
3190 C  CA  . GLY B 143 ? 0.5410 0.6413 0.6843 -0.0312 -0.0362 -0.0356 119 GLY B CA  
3191 C  C   . GLY B 143 ? 0.5800 0.6865 0.7125 -0.0270 -0.0406 -0.0375 119 GLY B C   
3192 O  O   . GLY B 143 ? 0.5782 0.6773 0.6958 -0.0228 -0.0384 -0.0369 119 GLY B O   
3193 N  N   . LEU B 144 ? 0.5904 0.7113 0.7311 -0.0282 -0.0469 -0.0393 120 LEU B N   
3194 C  CA  . LEU B 144 ? 0.6538 0.7833 0.7854 -0.0243 -0.0520 -0.0407 120 LEU B CA  
3195 C  C   . LEU B 144 ? 0.6959 0.8345 0.8316 -0.0289 -0.0611 -0.0493 120 LEU B C   
3196 O  O   . LEU B 144 ? 0.7552 0.9007 0.8815 -0.0260 -0.0658 -0.0515 120 LEU B O   
3197 C  CB  . LEU B 144 ? 0.6948 0.8357 0.8316 -0.0195 -0.0504 -0.0326 120 LEU B CB  
3198 C  CG  . LEU B 144 ? 0.6818 0.8154 0.8187 -0.0157 -0.0413 -0.0247 120 LEU B CG  
3199 C  CD1 . LEU B 144 ? 0.6751 0.8219 0.8243 -0.0129 -0.0401 -0.0178 120 LEU B CD1 
3200 C  CD2 . LEU B 144 ? 0.6972 0.8201 0.8170 -0.0102 -0.0372 -0.0227 120 LEU B CD2 
3201 N  N   . PHE B 145 ? 0.6826 0.8210 0.8312 -0.0358 -0.0638 -0.0543 121 PHE B N   
3202 C  CA  . PHE B 145 ? 0.7147 0.8620 0.8684 -0.0406 -0.0729 -0.0633 121 PHE B CA  
3203 C  C   . PHE B 145 ? 0.7986 0.9388 0.9373 -0.0404 -0.0760 -0.0723 121 PHE B C   
3204 O  O   . PHE B 145 ? 0.8432 0.9922 0.9811 -0.0425 -0.0839 -0.0802 121 PHE B O   
3205 C  CB  . PHE B 145 ? 0.6375 0.7849 0.8106 -0.0484 -0.0744 -0.0662 121 PHE B CB  
3206 C  CG  . PHE B 145 ? 0.6447 0.7753 0.8199 -0.0509 -0.0678 -0.0655 121 PHE B CG  
3207 C  CD1 . PHE B 145 ? 0.5900 0.7161 0.7695 -0.0490 -0.0596 -0.0559 121 PHE B CD1 
3208 C  CD2 . PHE B 145 ? 0.6257 0.7455 0.7987 -0.0548 -0.0699 -0.0743 121 PHE B CD2 
3209 C  CE1 . PHE B 145 ? 0.5643 0.6762 0.7451 -0.0511 -0.0539 -0.0546 121 PHE B CE1 
3210 C  CE2 . PHE B 145 ? 0.6079 0.7127 0.7834 -0.0568 -0.0640 -0.0727 121 PHE B CE2 
3211 C  CZ  . PHE B 145 ? 0.5574 0.6588 0.7367 -0.0550 -0.0561 -0.0625 121 PHE B CZ  
3212 N  N   . PRO B 146 ? 0.8177 0.9429 0.9443 -0.0378 -0.0703 -0.0717 122 PRO B N   
3213 C  CA  . PRO B 146 ? 0.8830 1.0044 0.9936 -0.0358 -0.0728 -0.0785 122 PRO B CA  
3214 C  C   . PRO B 146 ? 0.9525 1.0838 1.0509 -0.0295 -0.0745 -0.0748 122 PRO B C   
3215 O  O   . PRO B 146 ? 0.9940 1.1315 1.0834 -0.0287 -0.0798 -0.0811 122 PRO B O   
3216 C  CB  . PRO B 146 ? 0.9005 1.0042 1.0039 -0.0346 -0.0657 -0.0770 122 PRO B CB  
3217 C  CG  . PRO B 146 ? 0.7805 0.8786 0.8980 -0.0381 -0.0612 -0.0725 122 PRO B CG  
3218 C  CD  . PRO B 146 ? 0.7318 0.8431 0.8595 -0.0376 -0.0620 -0.0661 122 PRO B CD  
3219 N  N   . MET B 147 ? 0.9479 1.0809 1.0458 -0.0249 -0.0697 -0.0647 123 MET B N   
3220 C  CA  . MET B 147 ? 0.9531 1.0970 1.0430 -0.0191 -0.0714 -0.0598 123 MET B CA  
3221 C  C   . MET B 147 ? 0.9700 1.1320 1.0654 -0.0208 -0.0803 -0.0637 123 MET B C   
3222 O  O   . MET B 147 ? 0.9688 1.1406 1.0546 -0.0168 -0.0839 -0.0630 123 MET B O   
3223 C  CB  . MET B 147 ? 0.9426 1.0864 1.0365 -0.0148 -0.0653 -0.0488 123 MET B CB  
3224 C  CG  . MET B 147 ? 0.9533 1.0931 1.0335 -0.0080 -0.0612 -0.0426 123 MET B CG  
3225 S  SD  . MET B 147 ? 0.9750 1.1120 1.0604 -0.0031 -0.0535 -0.0312 123 MET B SD  
3226 C  CE  . MET B 147 ? 0.8372 0.9609 0.9304 -0.0078 -0.0476 -0.0323 123 MET B CE  
3227 N  N   . LEU B 148 ? 0.9685 1.1357 1.0796 -0.0268 -0.0840 -0.0676 124 LEU B N   
3228 C  CA  . LEU B 148 ? 0.9565 1.1413 1.0740 -0.0293 -0.0933 -0.0723 124 LEU B CA  
3229 C  C   . LEU B 148 ? 0.9990 1.1850 1.1051 -0.0309 -0.0996 -0.0835 124 LEU B C   
3230 O  O   . LEU B 148 ? 0.9814 1.1830 1.0846 -0.0303 -0.1072 -0.0866 124 LEU B O   
3231 C  CB  . LEU B 148 ? 0.9306 1.1191 1.0688 -0.0363 -0.0955 -0.0742 124 LEU B CB  
3232 C  CG  . LEU B 148 ? 0.9181 1.1271 1.0677 -0.0390 -0.1046 -0.0761 124 LEU B CG  
3233 C  CD1 . LEU B 148 ? 0.8084 1.0304 0.9619 -0.0332 -0.1031 -0.0645 124 LEU B CD1 
3234 C  CD2 . LEU B 148 ? 0.8825 1.0922 1.0522 -0.0475 -0.1072 -0.0808 124 LEU B CD2 
3235 N  N   . ASN B 149 ? 1.0917 1.2618 1.1907 -0.0325 -0.0965 -0.0897 125 ASN B N   
3236 C  CA  . ASN B 149 ? 1.1623 1.3325 1.2512 -0.0339 -0.1018 -0.1015 125 ASN B CA  
3237 C  C   . ASN B 149 ? 1.1325 1.3149 1.2056 -0.0280 -0.1052 -0.1002 125 ASN B C   
3238 O  O   . ASN B 149 ? 1.1383 1.3330 1.2079 -0.0293 -0.1132 -0.1081 125 ASN B O   
3239 C  CB  . ASN B 149 ? 1.1884 1.3393 1.2705 -0.0344 -0.0961 -0.1054 125 ASN B CB  
3240 C  CG  . ASN B 149 ? 1.1832 1.3219 1.2806 -0.0399 -0.0924 -0.1055 125 ASN B CG  
3241 O  OD1 . ASN B 149 ? 1.1782 1.3229 1.2916 -0.0436 -0.0939 -0.1028 125 ASN B OD1 
3242 N  ND2 . ASN B 149 ? 1.1557 1.2780 1.2487 -0.0402 -0.0874 -0.1080 125 ASN B ND2 
3243 N  N   . ARG B 150 ? 1.0241 1.2037 1.0875 -0.0215 -0.0992 -0.0902 126 ARG B N   
3244 C  CA  . ARG B 150 ? 0.9901 1.1796 1.0380 -0.0155 -0.1012 -0.0878 126 ARG B CA  
3245 C  C   . ARG B 150 ? 0.9172 1.1248 0.9693 -0.0123 -0.1050 -0.0796 126 ARG B C   
3246 O  O   . ARG B 150 ? 0.9210 1.1429 0.9639 -0.0093 -0.1104 -0.0806 126 ARG B O   
3247 C  CB  . ARG B 150 ? 0.9600 1.1370 0.9956 -0.0102 -0.0929 -0.0812 126 ARG B CB  
3248 C  CG  . ARG B 150 ? 0.8725 1.0455 0.9126 -0.0065 -0.0864 -0.0683 126 ARG B CG  
3249 C  CD  . ARG B 150 ? 0.8754 1.0399 0.9017 -0.0010 -0.0802 -0.0624 126 ARG B CD  
3250 N  NE  . ARG B 150 ? 1.0119 1.1605 1.0325 -0.0029 -0.0761 -0.0679 126 ARG B NE  
3251 C  CZ  . ARG B 150 ? 1.0438 1.1856 1.0518 0.0007  -0.0720 -0.0658 126 ARG B CZ  
3252 N  NH1 . ARG B 150 ? 1.0121 1.1611 1.0114 0.0062  -0.0714 -0.0586 126 ARG B NH1 
3253 N  NH2 . ARG B 150 ? 1.1042 1.2322 1.1092 -0.0013 -0.0685 -0.0707 126 ARG B NH2 
3254 N  N   . TYR B 151 ? 0.8964 1.1046 0.9622 -0.0123 -0.1020 -0.0713 127 TYR B N   
3255 C  CA  . TYR B 151 ? 0.8011 1.0251 0.8715 -0.0080 -0.1041 -0.0617 127 TYR B CA  
3256 C  C   . TYR B 151 ? 0.7805 1.0216 0.8653 -0.0123 -0.1124 -0.0648 127 TYR B C   
3257 O  O   . TYR B 151 ? 0.7683 1.0255 0.8566 -0.0087 -0.1157 -0.0576 127 TYR B O   
3258 C  CB  . TYR B 151 ? 0.6925 0.9082 0.7693 -0.0045 -0.0955 -0.0501 127 TYR B CB  
3259 C  CG  . TYR B 151 ? 0.6852 0.8861 0.7489 0.0004  -0.0876 -0.0451 127 TYR B CG  
3260 C  CD1 . TYR B 151 ? 0.6293 0.8353 0.6796 0.0063  -0.0878 -0.0405 127 TYR B CD1 
3261 C  CD2 . TYR B 151 ? 0.6800 0.8628 0.7453 -0.0011 -0.0800 -0.0444 127 TYR B CD2 
3262 C  CE1 . TYR B 151 ? 0.6255 0.8182 0.6653 0.0102  -0.0807 -0.0357 127 TYR B CE1 
3263 C  CE2 . TYR B 151 ? 0.7209 0.8909 0.7751 0.0029  -0.0734 -0.0402 127 TYR B CE2 
3264 C  CZ  . TYR B 151 ? 0.6554 0.8302 0.6974 0.0083  -0.0738 -0.0359 127 TYR B CZ  
3265 O  OH  . TYR B 151 ? 0.6964 0.8586 0.7287 0.0117  -0.0673 -0.0316 127 TYR B OH  
3266 N  N   . GLU B 152 ? 0.8377 1.0761 0.9318 -0.0200 -0.1161 -0.0750 128 GLU B N   
3267 C  CA  . GLU B 152 ? 0.8305 1.0843 0.9418 -0.0249 -0.1234 -0.0771 128 GLU B CA  
3268 C  C   . GLU B 152 ? 0.8154 1.0914 0.9219 -0.0227 -0.1328 -0.0780 128 GLU B C   
3269 O  O   . GLU B 152 ? 0.7780 1.0706 0.8981 -0.0237 -0.1379 -0.0743 128 GLU B O   
3270 C  CB  . GLU B 152 ? 0.9066 1.1533 1.0272 -0.0338 -0.1266 -0.0893 128 GLU B CB  
3271 C  CG  . GLU B 152 ? 0.9358 1.1948 1.0783 -0.0399 -0.1321 -0.0900 128 GLU B CG  
3272 C  CD  . GLU B 152 ? 1.0191 1.2659 1.1749 -0.0483 -0.1314 -0.0978 128 GLU B CD  
3273 O  OE1 . GLU B 152 ? 1.0480 1.2777 1.1950 -0.0495 -0.1279 -0.1043 128 GLU B OE1 
3274 O  OE2 . GLU B 152 ? 1.0731 1.3275 1.2488 -0.0536 -0.1341 -0.0970 128 GLU B OE2 
3275 N  N   . SER B 153 ? 0.8945 1.1723 0.9821 -0.0195 -0.1353 -0.0825 129 SER B N   
3276 C  CA  . SER B 153 ? 0.8480 1.1478 0.9295 -0.0176 -0.1447 -0.0840 129 SER B CA  
3277 C  C   . SER B 153 ? 0.7833 1.0968 0.8668 -0.0104 -0.1438 -0.0692 129 SER B C   
3278 O  O   . SER B 153 ? 0.7939 1.1286 0.8831 -0.0102 -0.1520 -0.0676 129 SER B O   
3279 C  CB  . SER B 153 ? 0.8953 1.1933 0.9548 -0.0151 -0.1462 -0.0914 129 SER B CB  
3280 O  OG  . SER B 153 ? 0.9732 1.2570 1.0309 -0.0209 -0.1461 -0.1049 129 SER B OG  
3281 N  N   . GLN B 154 ? 0.7287 1.0305 0.8084 -0.0045 -0.1342 -0.0582 130 GLN B N   
3282 C  CA  . GLN B 154 ? 0.6736 0.9858 0.7517 0.0035  -0.1324 -0.0442 130 GLN B CA  
3283 C  C   . GLN B 154 ? 0.6267 0.9378 0.7225 0.0050  -0.1272 -0.0339 130 GLN B C   
3284 O  O   . GLN B 154 ? 0.5927 0.9065 0.6880 0.0122  -0.1230 -0.0217 130 GLN B O   
3285 C  CB  . GLN B 154 ? 0.6858 0.9866 0.7460 0.0099  -0.1254 -0.0390 130 GLN B CB  
3286 C  CG  . GLN B 154 ? 0.6179 0.8946 0.6788 0.0098  -0.1147 -0.0368 130 GLN B CG  
3287 C  CD  . GLN B 154 ? 0.6596 0.9237 0.7024 0.0130  -0.1096 -0.0372 130 GLN B CD  
3288 O  OE1 . GLN B 154 ? 0.6907 0.9527 0.7229 0.0104  -0.1124 -0.0473 130 GLN B OE1 
3289 N  NE2 . GLN B 154 ? 0.5870 0.8425 0.6268 0.0188  -0.1019 -0.0263 130 GLN B NE2 
3290 N  N   . LEU B 155 ? 0.6406 0.9479 0.7525 -0.0015 -0.1271 -0.0383 131 LEU B N   
3291 C  CA  . LEU B 155 ? 0.5886 0.8947 0.7171 -0.0001 -0.1214 -0.0289 131 LEU B CA  
3292 C  C   . LEU B 155 ? 0.5679 0.8982 0.7091 0.0019  -0.1280 -0.0225 131 LEU B C   
3293 O  O   . LEU B 155 ? 0.5962 0.9413 0.7457 -0.0037 -0.1373 -0.0293 131 LEU B O   
3294 C  CB  . LEU B 155 ? 0.5855 0.8799 0.7268 -0.0076 -0.1185 -0.0350 131 LEU B CB  
3295 C  CG  . LEU B 155 ? 0.5713 0.8414 0.7023 -0.0092 -0.1110 -0.0397 131 LEU B CG  
3296 C  CD1 . LEU B 155 ? 0.6158 0.8766 0.7611 -0.0164 -0.1085 -0.0443 131 LEU B CD1 
3297 C  CD2 . LEU B 155 ? 0.4976 0.7554 0.6199 -0.0017 -0.1013 -0.0298 131 LEU B CD2 
3298 N  N   . LYS B 156 ? 0.4981 0.8324 0.6417 0.0098  -0.1233 -0.0094 132 LYS B N   
3299 C  CA  . LYS B 156 ? 0.5367 0.8940 0.6918 0.0134  -0.1288 -0.0012 132 LYS B CA  
3300 C  C   . LYS B 156 ? 0.4883 0.8506 0.6665 0.0110  -0.1268 0.0026  132 LYS B C   
3301 O  O   . LYS B 156 ? 0.4971 0.8798 0.6890 0.0082  -0.1349 0.0023  132 LYS B O   
3302 C  CB  . LYS B 156 ? 0.5247 0.8837 0.6719 0.0237  -0.1243 0.0117  132 LYS B CB  
3303 C  CG  . LYS B 156 ? 0.6373 0.9916 0.7621 0.0268  -0.1251 0.0100  132 LYS B CG  
3304 C  CD  . LYS B 156 ? 0.7211 1.0713 0.8398 0.0365  -0.1182 0.0234  132 LYS B CD  
3305 C  CE  . LYS B 156 ? 0.7688 1.1178 0.8666 0.0398  -0.1194 0.0231  132 LYS B CE  
3306 N  NZ  . LYS B 156 ? 0.6869 1.0151 0.7716 0.0356  -0.1151 0.0136  132 LYS B NZ  
3307 N  N   . HIS B 157 ? 0.4739 0.8190 0.6569 0.0120  -0.1162 0.0062  133 HIS B N   
3308 C  CA  . HIS B 157 ? 0.4628 0.8122 0.6669 0.0112  -0.1125 0.0115  133 HIS B CA  
3309 C  C   . HIS B 157 ? 0.4813 0.8236 0.6950 0.0015  -0.1128 0.0022  133 HIS B C   
3310 O  O   . HIS B 157 ? 0.4484 0.7728 0.6515 -0.0024 -0.1100 -0.0056 133 HIS B O   
3311 C  CB  . HIS B 157 ? 0.4392 0.7747 0.6429 0.0187  -0.1003 0.0212  133 HIS B CB  
3312 C  CG  . HIS B 157 ? 0.4593 0.7993 0.6552 0.0284  -0.0990 0.0310  133 HIS B CG  
3313 N  ND1 . HIS B 157 ? 0.4699 0.8315 0.6764 0.0333  -0.1035 0.0397  133 HIS B ND1 
3314 C  CD2 . HIS B 157 ? 0.4644 0.7902 0.6438 0.0340  -0.0935 0.0342  133 HIS B CD2 
3315 C  CE1 . HIS B 157 ? 0.4703 0.8302 0.6670 0.0418  -0.1007 0.0480  133 HIS B CE1 
3316 N  NE2 . HIS B 157 ? 0.5061 0.8444 0.6867 0.0422  -0.0946 0.0448  133 HIS B NE2 
3317 N  N   . GLN B 158 ? 0.4167 0.7737 0.6518 -0.0023 -0.1159 0.0038  134 GLN B N   
3318 C  CA  . GLN B 158 ? 0.4439 0.7957 0.6911 -0.0117 -0.1161 -0.0037 134 GLN B CA  
3319 C  C   . GLN B 158 ? 0.4281 0.7573 0.6733 -0.0113 -0.1040 -0.0020 134 GLN B C   
3320 O  O   . GLN B 158 ? 0.4616 0.7778 0.7061 -0.0181 -0.1030 -0.0099 134 GLN B O   
3321 C  CB  . GLN B 158 ? 0.4489 0.8216 0.7212 -0.0151 -0.1207 -0.0001 134 GLN B CB  
3322 C  CG  . GLN B 158 ? 0.4770 0.8466 0.7644 -0.0256 -0.1220 -0.0075 134 GLN B CG  
3323 C  CD  . GLN B 158 ? 0.5449 0.9117 0.8244 -0.0337 -0.1312 -0.0215 134 GLN B CD  
3324 O  OE1 . GLN B 158 ? 0.6177 0.9975 0.8900 -0.0335 -0.1409 -0.0258 134 GLN B OE1 
3325 N  NE2 . GLN B 158 ? 0.5597 0.9095 0.8403 -0.0404 -0.1279 -0.0286 134 GLN B NE2 
3326 N  N   . TRP B 159 ? 0.4179 0.7424 0.6625 -0.0031 -0.0948 0.0081  135 TRP B N   
3327 C  CA  . TRP B 159 ? 0.4122 0.7164 0.6542 -0.0024 -0.0835 0.0097  135 TRP B CA  
3328 C  C   . TRP B 159 ? 0.4199 0.7034 0.6412 -0.0038 -0.0815 0.0025  135 TRP B C   
3329 O  O   . TRP B 159 ? 0.4195 0.6868 0.6392 -0.0067 -0.0751 0.0000  135 TRP B O   
3330 C  CB  . TRP B 159 ? 0.3646 0.6676 0.6081 0.0071  -0.0745 0.0209  135 TRP B CB  
3331 C  CG  . TRP B 159 ? 0.4170 0.7126 0.6425 0.0151  -0.0724 0.0242  135 TRP B CG  
3332 C  CD1 . TRP B 159 ? 0.4114 0.7203 0.6358 0.0216  -0.0761 0.0306  135 TRP B CD1 
3333 C  CD2 . TRP B 159 ? 0.4093 0.6828 0.6163 0.0172  -0.0659 0.0222  135 TRP B CD2 
3334 N  NE1 . TRP B 159 ? 0.4320 0.7280 0.6389 0.0276  -0.0722 0.0328  135 TRP B NE1 
3335 C  CE2 . TRP B 159 ? 0.4152 0.6895 0.6113 0.0248  -0.0660 0.0274  135 TRP B CE2 
3336 C  CE3 . TRP B 159 ? 0.4147 0.6686 0.6141 0.0134  -0.0603 0.0168  135 TRP B CE3 
3337 C  CZ2 . TRP B 159 ? 0.4059 0.6620 0.5846 0.0282  -0.0607 0.0271  135 TRP B CZ2 
3338 C  CZ3 . TRP B 159 ? 0.4180 0.6545 0.5995 0.0170  -0.0554 0.0164  135 TRP B CZ3 
3339 C  CH2 . TRP B 159 ? 0.4002 0.6377 0.5718 0.0240  -0.0556 0.0213  135 TRP B CH2 
3340 N  N   . GLU B 160 ? 0.4342 0.7189 0.6400 -0.0016 -0.0869 -0.0005 136 GLU B N   
3341 C  CA  . GLU B 160 ? 0.4229 0.6897 0.6101 -0.0030 -0.0855 -0.0076 136 GLU B CA  
3342 C  C   . GLU B 160 ? 0.4822 0.7453 0.6723 -0.0125 -0.0904 -0.0188 136 GLU B C   
3343 O  O   . GLU B 160 ? 0.4582 0.7034 0.6413 -0.0152 -0.0858 -0.0233 136 GLU B O   
3344 C  CB  . GLU B 160 ? 0.4389 0.7099 0.6097 0.0019  -0.0899 -0.0073 136 GLU B CB  
3345 C  CG  . GLU B 160 ? 0.4268 0.6956 0.5919 0.0114  -0.0836 0.0034  136 GLU B CG  
3346 C  CD  . GLU B 160 ? 0.4455 0.7205 0.5960 0.0161  -0.0883 0.0049  136 GLU B CD  
3347 O  OE1 . GLU B 160 ? 0.4465 0.7405 0.6000 0.0154  -0.0973 0.0039  136 GLU B OE1 
3348 O  OE2 . GLU B 160 ? 0.4523 0.7139 0.5886 0.0203  -0.0830 0.0071  136 GLU B OE2 
3349 N  N   . ARG B 161 ? 0.4410 0.7208 0.6420 -0.0176 -0.0999 -0.0234 137 ARG B N   
3350 C  CA  . ARG B 161 ? 0.4716 0.7478 0.6770 -0.0269 -0.1050 -0.0347 137 ARG B CA  
3351 C  C   . ARG B 161 ? 0.4567 0.7235 0.6768 -0.0318 -0.0987 -0.0337 137 ARG B C   
3352 O  O   . ARG B 161 ? 0.4810 0.7330 0.6983 -0.0369 -0.0971 -0.0406 137 ARG B O   
3353 C  CB  . ARG B 161 ? 0.5086 0.8059 0.7234 -0.0313 -0.1170 -0.0399 137 ARG B CB  
3354 C  CG  . ARG B 161 ? 0.5545 0.8628 0.7538 -0.0266 -0.1239 -0.0411 137 ARG B CG  
3355 C  CD  . ARG B 161 ? 0.6247 0.9546 0.8325 -0.0314 -0.1365 -0.0473 137 ARG B CD  
3356 N  NE  . ARG B 161 ? 0.6519 0.9970 0.8478 -0.0251 -0.1421 -0.0440 137 ARG B NE  
3357 C  CZ  . ARG B 161 ? 0.6325 0.9969 0.8370 -0.0205 -0.1450 -0.0345 137 ARG B CZ  
3358 N  NH1 . ARG B 161 ? 0.6062 0.9788 0.8321 -0.0217 -0.1432 -0.0278 137 ARG B NH1 
3359 N  NH2 . ARG B 161 ? 0.6022 0.9788 0.7940 -0.0143 -0.1495 -0.0311 137 ARG B NH2 
3360 N  N   . ASN B 162 ? 0.4247 0.7002 0.6608 -0.0301 -0.0948 -0.0246 138 ASN B N   
3361 C  CA  . ASN B 162 ? 0.4587 0.7265 0.7086 -0.0341 -0.0879 -0.0223 138 ASN B CA  
3362 C  C   . ASN B 162 ? 0.4618 0.7080 0.6984 -0.0305 -0.0774 -0.0199 138 ASN B C   
3363 O  O   . ASN B 162 ? 0.4542 0.6880 0.6938 -0.0354 -0.0735 -0.0226 138 ASN B O   
3364 C  CB  . ASN B 162 ? 0.4383 0.7216 0.7075 -0.0320 -0.0854 -0.0125 138 ASN B CB  
3365 C  CG  . ASN B 162 ? 0.4914 0.7979 0.7754 -0.0356 -0.0962 -0.0140 138 ASN B CG  
3366 O  OD1 . ASN B 162 ? 0.4584 0.7684 0.7449 -0.0430 -0.1051 -0.0236 138 ASN B OD1 
3367 N  ND2 . ASN B 162 ? 0.4269 0.7497 0.7213 -0.0302 -0.0955 -0.0047 138 ASN B ND2 
3368 N  N   . TYR B 163 ? 0.4368 0.6787 0.6593 -0.0221 -0.0728 -0.0145 139 TYR B N   
3369 C  CA  . TYR B 163 ? 0.4827 0.7053 0.6926 -0.0184 -0.0632 -0.0121 139 TYR B CA  
3370 C  C   . TYR B 163 ? 0.5085 0.7154 0.7051 -0.0225 -0.0644 -0.0209 139 TYR B C   
3371 O  O   . TYR B 163 ? 0.5395 0.7327 0.7360 -0.0253 -0.0589 -0.0219 139 TYR B O   
3372 C  CB  . TYR B 163 ? 0.5234 0.7455 0.7217 -0.0091 -0.0596 -0.0055 139 TYR B CB  
3373 C  CG  . TYR B 163 ? 0.5814 0.7855 0.7683 -0.0046 -0.0495 -0.0021 139 TYR B CG  
3374 C  CD1 . TYR B 163 ? 0.6765 0.8765 0.8716 -0.0035 -0.0412 0.0031  139 TYR B CD1 
3375 C  CD2 . TYR B 163 ? 0.5603 0.7526 0.7283 -0.0011 -0.0484 -0.0038 139 TYR B CD2 
3376 C  CE1 . TYR B 163 ? 0.6561 0.8404 0.8401 0.0006  -0.0325 0.0055  139 TYR B CE1 
3377 C  CE2 . TYR B 163 ? 0.6648 0.8412 0.8229 0.0026  -0.0399 -0.0011 139 TYR B CE2 
3378 C  CZ  . TYR B 163 ? 0.6765 0.8489 0.8423 0.0034  -0.0322 0.0032  139 TYR B CZ  
3379 O  OH  . TYR B 163 ? 0.6469 0.8040 0.8020 0.0070  -0.0243 0.0051  139 TYR B OH  
3380 N  N   . LEU B 164 ? 0.5376 0.7471 0.7229 -0.0224 -0.0715 -0.0270 140 LEU B N   
3381 C  CA  . LEU B 164 ? 0.5625 0.7574 0.7339 -0.0250 -0.0721 -0.0350 140 LEU B CA  
3382 C  C   . LEU B 164 ? 0.5878 0.7798 0.7694 -0.0338 -0.0758 -0.0432 140 LEU B C   
3383 O  O   . LEU B 164 ? 0.6227 0.7992 0.7980 -0.0362 -0.0729 -0.0477 140 LEU B O   
3384 C  CB  . LEU B 164 ? 0.5847 0.7846 0.7413 -0.0218 -0.0781 -0.0387 140 LEU B CB  
3385 C  CG  . LEU B 164 ? 0.5760 0.7779 0.7227 -0.0131 -0.0745 -0.0302 140 LEU B CG  
3386 C  CD1 . LEU B 164 ? 0.5607 0.7681 0.6927 -0.0103 -0.0803 -0.0333 140 LEU B CD1 
3387 C  CD2 . LEU B 164 ? 0.5875 0.7716 0.7261 -0.0096 -0.0646 -0.0257 140 LEU B CD2 
3388 N  N   . GLY B 165 ? 0.5435 0.7500 0.7418 -0.0387 -0.0821 -0.0451 141 GLY B N   
3389 C  CA  . GLY B 165 ? 0.5310 0.7347 0.7412 -0.0474 -0.0857 -0.0527 141 GLY B CA  
3390 C  C   . GLY B 165 ? 0.4894 0.6857 0.7137 -0.0508 -0.0785 -0.0478 141 GLY B C   
3391 O  O   . GLY B 165 ? 0.5416 0.7335 0.7768 -0.0582 -0.0805 -0.0532 141 GLY B O   
3392 N  N   . ASN B 166 ? 0.4836 0.6784 0.7082 -0.0455 -0.0701 -0.0377 142 ASN B N   
3393 C  CA  . ASN B 166 ? 0.4674 0.6579 0.7054 -0.0479 -0.0628 -0.0318 142 ASN B CA  
3394 C  C   . ASN B 166 ? 0.4867 0.6571 0.7157 -0.0494 -0.0574 -0.0341 142 ASN B C   
3395 O  O   . ASN B 166 ? 0.4775 0.6369 0.6897 -0.0439 -0.0522 -0.0321 142 ASN B O   
3396 C  CB  . ASN B 166 ? 0.4258 0.6219 0.6653 -0.0409 -0.0555 -0.0209 142 ASN B CB  
3397 C  CG  . ASN B 166 ? 0.4264 0.6217 0.6809 -0.0431 -0.0480 -0.0142 142 ASN B CG  
3398 O  OD1 . ASN B 166 ? 0.4064 0.5962 0.6702 -0.0499 -0.0480 -0.0167 142 ASN B OD1 
3399 N  ND2 . ASN B 166 ? 0.3805 0.5813 0.6375 -0.0370 -0.0413 -0.0053 142 ASN B ND2 
3400 N  N   . LYS B 167 ? 0.4648 0.6306 0.7059 -0.0570 -0.0587 -0.0380 143 LYS B N   
3401 C  CA  . LYS B 167 ? 0.4492 0.5970 0.6847 -0.0588 -0.0536 -0.0393 143 LYS B CA  
3402 C  C   . LYS B 167 ? 0.4411 0.5848 0.6841 -0.0582 -0.0441 -0.0297 143 LYS B C   
3403 O  O   . LYS B 167 ? 0.3955 0.5259 0.6373 -0.0603 -0.0399 -0.0295 143 LYS B O   
3404 C  CB  . LYS B 167 ? 0.4722 0.6157 0.7170 -0.0670 -0.0597 -0.0485 143 LYS B CB  
3405 C  CG  . LYS B 167 ? 0.4854 0.6317 0.7213 -0.0678 -0.0689 -0.0595 143 LYS B CG  
3406 C  CD  . LYS B 167 ? 0.5795 0.7196 0.8252 -0.0759 -0.0741 -0.0692 143 LYS B CD  
3407 C  CE  . LYS B 167 ? 0.6466 0.7883 0.8814 -0.0763 -0.0827 -0.0813 143 LYS B CE  
3408 N  NZ  . LYS B 167 ? 0.6831 0.8170 0.9274 -0.0840 -0.0872 -0.0916 143 LYS B NZ  
3409 N  N   . ASP B 168 ? 0.4098 0.5650 0.6604 -0.0549 -0.0404 -0.0215 144 ASP B N   
3410 C  CA  . ASP B 168 ? 0.3846 0.5387 0.6437 -0.0542 -0.0314 -0.0123 144 ASP B CA  
3411 C  C   . ASP B 168 ? 0.3752 0.5294 0.6224 -0.0454 -0.0240 -0.0053 144 ASP B C   
3412 O  O   . ASP B 168 ? 0.3772 0.5366 0.6329 -0.0435 -0.0171 0.0028  144 ASP B O   
3413 C  CB  . ASP B 168 ? 0.3902 0.5590 0.6743 -0.0595 -0.0328 -0.0086 144 ASP B CB  
3414 C  CG  . ASP B 168 ? 0.4522 0.6192 0.7502 -0.0690 -0.0393 -0.0153 144 ASP B CG  
3415 O  OD1 . ASP B 168 ? 0.4404 0.5928 0.7356 -0.0719 -0.0368 -0.0171 144 ASP B OD1 
3416 O  OD2 . ASP B 168 ? 0.4704 0.6505 0.7824 -0.0735 -0.0469 -0.0189 144 ASP B OD2 
3417 N  N   . ILE B 169 ? 0.3988 0.5473 0.6269 -0.0400 -0.0251 -0.0082 145 ILE B N   
3418 C  CA  . ILE B 169 ? 0.4450 0.5918 0.6620 -0.0318 -0.0183 -0.0024 145 ILE B CA  
3419 C  C   . ILE B 169 ? 0.4600 0.5933 0.6688 -0.0305 -0.0098 0.0010  145 ILE B C   
3420 O  O   . ILE B 169 ? 0.4046 0.5251 0.6043 -0.0328 -0.0102 -0.0031 145 ILE B O   
3421 C  CB  . ILE B 169 ? 0.4506 0.5950 0.6506 -0.0268 -0.0220 -0.0061 145 ILE B CB  
3422 C  CG1 . ILE B 169 ? 0.4574 0.6169 0.6646 -0.0276 -0.0307 -0.0088 145 ILE B CG1 
3423 C  CG2 . ILE B 169 ? 0.4843 0.6255 0.6741 -0.0187 -0.0148 -0.0003 145 ILE B CG2 
3424 C  CD1 . ILE B 169 ? 0.4996 0.6569 0.6905 -0.0239 -0.0354 -0.0130 145 ILE B CD1 
3425 N  N   . ILE B 170 ? 0.4572 0.5938 0.6691 -0.0264 -0.0019 0.0084  146 ILE B N   
3426 C  CA  . ILE B 170 ? 0.4243 0.5501 0.6275 -0.0243 0.0066  0.0122  146 ILE B CA  
3427 C  C   . ILE B 170 ? 0.4642 0.5890 0.6556 -0.0159 0.0121  0.0152  146 ILE B C   
3428 O  O   . ILE B 170 ? 0.4958 0.6315 0.6959 -0.0122 0.0151  0.0200  146 ILE B O   
3429 C  CB  . ILE B 170 ? 0.4199 0.5507 0.6388 -0.0277 0.0120  0.0184  146 ILE B CB  
3430 C  CG1 . ILE B 170 ? 0.4265 0.5546 0.6561 -0.0362 0.0073  0.0154  146 ILE B CG1 
3431 C  CG2 . ILE B 170 ? 0.4635 0.5864 0.6720 -0.0236 0.0216  0.0234  146 ILE B CG2 
3432 C  CD1 . ILE B 170 ? 0.4253 0.5612 0.6750 -0.0405 0.0113  0.0220  146 ILE B CD1 
3433 N  N   . PHE B 171 ? 0.4658 0.5775 0.6385 -0.0128 0.0133  0.0124  147 PHE B N   
3434 C  CA  . PHE B 171 ? 0.4842 0.5920 0.6449 -0.0053 0.0189  0.0145  147 PHE B CA  
3435 C  C   . PHE B 171 ? 0.4352 0.5389 0.5936 -0.0037 0.0278  0.0190  147 PHE B C   
3436 O  O   . PHE B 171 ? 0.4327 0.5255 0.5812 -0.0053 0.0297  0.0178  147 PHE B O   
3437 C  CB  . PHE B 171 ? 0.4824 0.5784 0.6252 -0.0034 0.0159  0.0095  147 PHE B CB  
3438 C  CG  . PHE B 171 ? 0.5625 0.6541 0.6941 0.0040  0.0205  0.0109  147 PHE B CG  
3439 C  CD1 . PHE B 171 ? 0.5457 0.6462 0.6845 0.0091  0.0243  0.0152  147 PHE B CD1 
3440 C  CD2 . PHE B 171 ? 0.5635 0.6419 0.6783 0.0057  0.0209  0.0078  147 PHE B CD2 
3441 C  CE1 . PHE B 171 ? 0.5383 0.6334 0.6674 0.0160  0.0285  0.0160  147 PHE B CE1 
3442 C  CE2 . PHE B 171 ? 0.5680 0.6414 0.6735 0.0119  0.0249  0.0086  147 PHE B CE2 
3443 C  CZ  . PHE B 171 ? 0.5548 0.6359 0.6673 0.0171  0.0288  0.0125  147 PHE B CZ  
3444 N  N   . ARG B 172 ? 0.4120 0.5254 0.5797 -0.0003 0.0335  0.0245  148 ARG B N   
3445 C  CA  . ARG B 172 ? 0.4340 0.5469 0.6022 0.0010  0.0422  0.0294  148 ARG B CA  
3446 C  C   . ARG B 172 ? 0.4496 0.5532 0.6003 0.0078  0.0485  0.0288  148 ARG B C   
3447 O  O   . ARG B 172 ? 0.4441 0.5494 0.5920 0.0137  0.0498  0.0285  148 ARG B O   
3448 C  CB  . ARG B 172 ? 0.4324 0.5610 0.6195 0.0017  0.0460  0.0357  148 ARG B CB  
3449 C  CG  . ARG B 172 ? 0.5098 0.6398 0.6975 0.0036  0.0559  0.0416  148 ARG B CG  
3450 C  CD  . ARG B 172 ? 0.5066 0.6523 0.7104 0.0069  0.0611  0.0479  148 ARG B CD  
3451 N  NE  . ARG B 172 ? 0.5214 0.6669 0.7196 0.0118  0.0718  0.0524  148 ARG B NE  
3452 C  CZ  . ARG B 172 ? 0.5241 0.6762 0.7317 0.0095  0.0776  0.0588  148 ARG B CZ  
3453 N  NH1 . ARG B 172 ? 0.5519 0.7114 0.7774 0.0021  0.0741  0.0619  148 ARG B NH1 
3454 N  NH2 . ARG B 172 ? 0.4583 0.6095 0.6572 0.0148  0.0873  0.0621  148 ARG B NH2 
3455 N  N   . ASN B 173 ? 0.4271 0.5213 0.5667 0.0069  0.0523  0.0288  149 ASN B N   
3456 C  CA  . ASN B 173 ? 0.4038 0.4892 0.5267 0.0125  0.0584  0.0279  149 ASN B CA  
3457 C  C   . ASN B 173 ? 0.4164 0.4991 0.5352 0.0106  0.0638  0.0311  149 ASN B C   
3458 O  O   . ASN B 173 ? 0.3915 0.4639 0.4981 0.0086  0.0625  0.0288  149 ASN B O   
3459 C  CB  . ASN B 173 ? 0.4044 0.4771 0.5112 0.0135  0.0540  0.0217  149 ASN B CB  
3460 C  CG  . ASN B 173 ? 0.4551 0.5308 0.5655 0.0154  0.0486  0.0194  149 ASN B CG  
3461 O  OD1 . ASN B 173 ? 0.4086 0.4863 0.5185 0.0214  0.0516  0.0201  149 ASN B OD1 
3462 N  ND2 . ASN B 173 ? 0.4149 0.4908 0.5287 0.0106  0.0407  0.0166  149 ASN B ND2 
3463 N  N   . THR B 174 ? 0.3790 0.4720 0.5086 0.0115  0.0701  0.0373  150 THR B N   
3464 C  CA  . THR B 174 ? 0.3516 0.4441 0.4784 0.0101  0.0758  0.0418  150 THR B CA  
3465 C  C   . THR B 174 ? 0.3887 0.4730 0.4952 0.0156  0.0815  0.0397  150 THR B C   
3466 O  O   . THR B 174 ? 0.3911 0.4712 0.4885 0.0209  0.0822  0.0353  150 THR B O   
3467 C  CB  . THR B 174 ? 0.4466 0.5535 0.5906 0.0100  0.0818  0.0497  150 THR B CB  
3468 O  OG1 . THR B 174 ? 0.4214 0.5345 0.5650 0.0174  0.0880  0.0506  150 THR B OG1 
3469 C  CG2 . THR B 174 ? 0.3860 0.5014 0.5510 0.0040  0.0757  0.0512  150 THR B CG2 
3470 N  N   . PHE B 175 ? 0.3826 0.4648 0.4825 0.0143  0.0854  0.0430  151 PHE B N   
3471 C  CA  . PHE B 175 ? 0.4330 0.5094 0.5139 0.0194  0.0911  0.0412  151 PHE B CA  
3472 C  C   . PHE B 175 ? 0.4220 0.5054 0.5035 0.0266  0.0989  0.0422  151 PHE B C   
3473 O  O   . PHE B 175 ? 0.4174 0.4942 0.4846 0.0320  0.1013  0.0369  151 PHE B O   
3474 C  CB  . PHE B 175 ? 0.4554 0.5317 0.5311 0.0170  0.0945  0.0463  151 PHE B CB  
3475 C  CG  . PHE B 175 ? 0.4641 0.5317 0.5367 0.0111  0.0874  0.0448  151 PHE B CG  
3476 C  CD1 . PHE B 175 ? 0.4808 0.5367 0.5371 0.0116  0.0831  0.0381  151 PHE B CD1 
3477 C  CD2 . PHE B 175 ? 0.4693 0.5406 0.5562 0.0051  0.0853  0.0503  151 PHE B CD2 
3478 C  CE1 . PHE B 175 ? 0.4785 0.5271 0.5326 0.0067  0.0770  0.0370  151 PHE B CE1 
3479 C  CE2 . PHE B 175 ? 0.4603 0.5233 0.5449 0.0003  0.0793  0.0488  151 PHE B CE2 
3480 C  CZ  . PHE B 175 ? 0.4490 0.5010 0.5170 0.0013  0.0752  0.0423  151 PHE B CZ  
3481 N  N   . GLY B 176 ? 0.4211 0.5180 0.5200 0.0267  0.1030  0.0487  152 GLY B N   
3482 C  CA  . GLY B 176 ? 0.4329 0.5375 0.5343 0.0339  0.1108  0.0501  152 GLY B CA  
3483 C  C   . GLY B 176 ? 0.4148 0.5172 0.5180 0.0378  0.1076  0.0449  152 GLY B C   
3484 O  O   . GLY B 176 ? 0.4631 0.5634 0.5583 0.0449  0.1128  0.0419  152 GLY B O   
3485 N  N   . ASP B 177 ? 0.3696 0.4726 0.4835 0.0333  0.0990  0.0437  153 ASP B N   
3486 C  CA  . ASP B 177 ? 0.4454 0.5463 0.5606 0.0367  0.0952  0.0395  153 ASP B CA  
3487 C  C   . ASP B 177 ? 0.4453 0.5311 0.5402 0.0403  0.0946  0.0323  153 ASP B C   
3488 O  O   . ASP B 177 ? 0.4395 0.5230 0.5305 0.0469  0.0980  0.0298  153 ASP B O   
3489 C  CB  . ASP B 177 ? 0.4753 0.5787 0.6022 0.0307  0.0854  0.0390  153 ASP B CB  
3490 C  CG  . ASP B 177 ? 0.5042 0.6232 0.6534 0.0272  0.0851  0.0453  153 ASP B CG  
3491 O  OD1 . ASP B 177 ? 0.4879 0.6175 0.6458 0.0310  0.0926  0.0505  153 ASP B OD1 
3492 O  OD2 . ASP B 177 ? 0.4830 0.6038 0.6414 0.0206  0.0773  0.0448  153 ASP B OD2 
3493 N  N   . VAL B 178 ? 0.4244 0.4996 0.5072 0.0358  0.0901  0.0289  154 VAL B N   
3494 C  CA  . VAL B 178 ? 0.4399 0.5010 0.5048 0.0380  0.0884  0.0220  154 VAL B CA  
3495 C  C   . VAL B 178 ? 0.4570 0.5148 0.5095 0.0443  0.0969  0.0201  154 VAL B C   
3496 O  O   . VAL B 178 ? 0.4296 0.4795 0.4738 0.0492  0.0980  0.0150  154 VAL B O   
3497 C  CB  . VAL B 178 ? 0.4455 0.4976 0.5012 0.0317  0.0824  0.0197  154 VAL B CB  
3498 C  CG1 . VAL B 178 ? 0.4453 0.4837 0.4823 0.0338  0.0816  0.0131  154 VAL B CG1 
3499 C  CG2 . VAL B 178 ? 0.4034 0.4571 0.4695 0.0265  0.0738  0.0196  154 VAL B CG2 
3500 N  N   . GLU B 179 ? 0.4430 0.5065 0.4938 0.0444  0.1030  0.0241  155 GLU B N   
3501 C  CA  . GLU B 179 ? 0.5024 0.5643 0.5409 0.0507  0.1115  0.0220  155 GLU B CA  
3502 C  C   . GLU B 179 ? 0.5228 0.5891 0.5681 0.0581  0.1170  0.0215  155 GLU B C   
3503 O  O   . GLU B 179 ? 0.5480 0.6070 0.5816 0.0641  0.1213  0.0160  155 GLU B O   
3504 C  CB  . GLU B 179 ? 0.5323 0.6028 0.5706 0.0496  0.1175  0.0282  155 GLU B CB  
3505 C  CG  . GLU B 179 ? 0.6247 0.6951 0.6487 0.0560  0.1266  0.0262  155 GLU B CG  
3506 C  CD  . GLU B 179 ? 0.7237 0.8014 0.7441 0.0541  0.1313  0.0324  155 GLU B CD  
3507 O  OE1 . GLU B 179 ? 0.7445 0.8244 0.7718 0.0474  0.1267  0.0375  155 GLU B OE1 
3508 O  OE2 . GLU B 179 ? 0.8108 0.8919 0.8213 0.0595  0.1397  0.0323  155 GLU B OE2 
3509 N  N   . HIS B 180 ? 0.5050 0.5831 0.5699 0.0579  0.1166  0.0271  156 HIS B N   
3510 C  CA  . HIS B 180 ? 0.5019 0.5856 0.5756 0.0653  0.1215  0.0277  156 HIS B CA  
3511 C  C   . HIS B 180 ? 0.5297 0.6021 0.5984 0.0682  0.1172  0.0215  156 HIS B C   
3512 O  O   . HIS B 180 ? 0.5412 0.6099 0.6061 0.0757  0.1227  0.0184  156 HIS B O   
3513 C  CB  . HIS B 180 ? 0.4818 0.5817 0.5787 0.0634  0.1206  0.0354  156 HIS B CB  
3514 C  CG  . HIS B 180 ? 0.5533 0.6605 0.6618 0.0706  0.1245  0.0369  156 HIS B CG  
3515 N  ND1 . HIS B 180 ? 0.5475 0.6605 0.6566 0.0783  0.1350  0.0385  156 HIS B ND1 
3516 C  CD2 . HIS B 180 ? 0.5898 0.7001 0.7100 0.0717  0.1194  0.0375  156 HIS B CD2 
3517 C  CE1 . HIS B 180 ? 0.5261 0.6451 0.6476 0.0839  0.1363  0.0401  156 HIS B CE1 
3518 N  NE2 . HIS B 180 ? 0.5778 0.6955 0.7062 0.0799  0.1267  0.0398  156 HIS B NE2 
3519 N  N   . VAL B 181 ? 0.4892 0.5560 0.5583 0.0626  0.1077  0.0199  157 VAL B N   
3520 C  CA  . VAL B 181 ? 0.4979 0.5547 0.5632 0.0651  0.1035  0.0152  157 VAL B CA  
3521 C  C   . VAL B 181 ? 0.5371 0.5787 0.5833 0.0681  0.1063  0.0079  157 VAL B C   
3522 O  O   . VAL B 181 ? 0.5453 0.5803 0.5891 0.0743  0.1092  0.0044  157 VAL B O   
3523 C  CB  . VAL B 181 ? 0.4823 0.5371 0.5508 0.0583  0.0931  0.0152  157 VAL B CB  
3524 C  CG1 . VAL B 181 ? 0.4907 0.5360 0.5554 0.0610  0.0892  0.0114  157 VAL B CG1 
3525 C  CG2 . VAL B 181 ? 0.4410 0.5109 0.5284 0.0550  0.0898  0.0214  157 VAL B CG2 
3526 N  N   . MET B 182 ? 0.5123 0.5478 0.5451 0.0637  0.1052  0.0053  158 MET B N   
3527 C  CA  . MET B 182 ? 0.5298 0.5515 0.5441 0.0657  0.1069  -0.0022 158 MET B CA  
3528 C  C   . MET B 182 ? 0.5822 0.6037 0.5925 0.0739  0.1165  -0.0048 158 MET B C   
3529 O  O   . MET B 182 ? 0.6279 0.6380 0.6303 0.0782  0.1179  -0.0112 158 MET B O   
3530 C  CB  . MET B 182 ? 0.5258 0.5451 0.5281 0.0601  0.1052  -0.0030 158 MET B CB  
3531 C  CG  . MET B 182 ? 0.5168 0.5327 0.5198 0.0525  0.0958  -0.0024 158 MET B CG  
3532 S  SD  . MET B 182 ? 0.5271 0.5445 0.5213 0.0465  0.0948  -0.0003 158 MET B SD  
3533 C  CE  . MET B 182 ? 0.4439 0.4542 0.4383 0.0393  0.0840  -0.0016 158 MET B CE  
3534 N  N   . THR B 183 ? 0.5564 0.5904 0.5725 0.0764  0.1235  0.0001  159 THR B N   
3535 C  CA  . THR B 183 ? 0.5830 0.6181 0.5954 0.0848  0.1335  -0.0022 159 THR B CA  
3536 C  C   . THR B 183 ? 0.5839 0.6188 0.6079 0.0913  0.1354  -0.0023 159 THR B C   
3537 O  O   . THR B 183 ? 0.6234 0.6479 0.6397 0.0972  0.1390  -0.0089 159 THR B O   
3538 C  CB  . THR B 183 ? 0.6205 0.6711 0.6387 0.0858  0.1406  0.0045  159 THR B CB  
3539 O  OG1 . THR B 183 ? 0.6592 0.7094 0.6655 0.0805  0.1395  0.0050  159 THR B OG1 
3540 C  CG2 . THR B 183 ? 0.6748 0.7282 0.6903 0.0952  0.1516  0.0024  159 THR B CG2 
3541 N  N   . THR B 184 ? 0.5672 0.6138 0.6102 0.0904  0.1329  0.0049  160 THR B N   
3542 C  CA  . THR B 184 ? 0.5672 0.6167 0.6231 0.0972  0.1352  0.0066  160 THR B CA  
3543 C  C   . THR B 184 ? 0.5632 0.5974 0.6139 0.0984  0.1303  0.0011  160 THR B C   
3544 O  O   . THR B 184 ? 0.5857 0.6131 0.6355 0.1059  0.1353  -0.0024 160 THR B O   
3545 C  CB  . THR B 184 ? 0.5466 0.6125 0.6236 0.0946  0.1316  0.0155  160 THR B CB  
3546 O  OG1 . THR B 184 ? 0.5613 0.6411 0.6444 0.0930  0.1364  0.0210  160 THR B OG1 
3547 C  CG2 . THR B 184 ? 0.5826 0.6536 0.6740 0.1021  0.1341  0.0183  160 THR B CG2 
3548 N  N   . LEU B 185 ? 0.5656 0.5942 0.6133 0.0912  0.1208  0.0005  161 LEU B N   
3549 C  CA  . LEU B 185 ? 0.5613 0.5771 0.6061 0.0919  0.1160  -0.0031 161 LEU B CA  
3550 C  C   . LEU B 185 ? 0.5703 0.5686 0.5967 0.0925  0.1175  -0.0121 161 LEU B C   
3551 O  O   . LEU B 185 ? 0.5747 0.5614 0.5993 0.0961  0.1173  -0.0159 161 LEU B O   
3552 C  CB  . LEU B 185 ? 0.5138 0.5312 0.5625 0.0844  0.1057  -0.0002 161 LEU B CB  
3553 C  CG  . LEU B 185 ? 0.5338 0.5678 0.6012 0.0834  0.1027  0.0078  161 LEU B CG  
3554 C  CD1 . LEU B 185 ? 0.4643 0.4982 0.5337 0.0767  0.0925  0.0091  161 LEU B CD1 
3555 C  CD2 . LEU B 185 ? 0.5146 0.5541 0.5947 0.0917  0.1070  0.0112  161 LEU B CD2 
3556 N  N   . GLY B 186 ? 0.5647 0.5611 0.5777 0.0891  0.1188  -0.0155 162 GLY B N   
3557 C  CA  . GLY B 186 ? 0.6085 0.5898 0.6040 0.0898  0.1203  -0.0246 162 GLY B CA  
3558 C  C   . GLY B 186 ? 0.6751 0.6505 0.6688 0.0989  0.1288  -0.0295 162 GLY B C   
3559 O  O   . GLY B 186 ? 0.6478 0.6080 0.6318 0.1004  0.1288  -0.0374 162 GLY B O   
3560 N  N   . ALA B 187 ? 0.6732 0.6605 0.6772 0.1050  0.1361  -0.0251 163 ALA B N   
3561 C  CA  . ALA B 187 ? 0.7071 0.6899 0.7101 0.1145  0.1452  -0.0297 163 ALA B CA  
3562 C  C   . ALA B 187 ? 0.6900 0.6634 0.7020 0.1191  0.1441  -0.0305 163 ALA B C   
3563 O  O   . ALA B 187 ? 0.7236 0.6878 0.7327 0.1265  0.1506  -0.0364 163 ALA B O   
3564 C  CB  . ALA B 187 ? 0.6493 0.6491 0.6628 0.1199  0.1536  -0.0236 163 ALA B CB  
3565 N  N   . GLY B 188 ? 0.6400 0.6157 0.6627 0.1152  0.1363  -0.0246 164 GLY B N   
3566 C  CA  . GLY B 188 ? 0.6300 0.5970 0.6607 0.1190  0.1344  -0.0241 164 GLY B CA  
3567 C  C   . GLY B 188 ? 0.5995 0.5485 0.6193 0.1147  0.1287  -0.0305 164 GLY B C   
3568 O  O   . GLY B 188 ? 0.5586 0.5003 0.5854 0.1166  0.1261  -0.0290 164 GLY B O   
3569 N  N   . GLY B 189 ? 0.5765 0.5188 0.5801 0.1090  0.1267  -0.0370 165 GLY B N   
3570 C  CA  . GLY B 189 ? 0.5604 0.4875 0.5544 0.1038  0.1204  -0.0423 165 GLY B CA  
3571 C  C   . GLY B 189 ? 0.5580 0.4889 0.5558 0.0961  0.1109  -0.0366 165 GLY B C   
3572 O  O   . GLY B 189 ? 0.5519 0.4713 0.5434 0.0916  0.1054  -0.0400 165 GLY B O   
3573 N  N   . THR B 190 ? 0.5472 0.4942 0.5554 0.0943  0.1087  -0.0284 166 THR B N   
3574 C  CA  . THR B 190 ? 0.4980 0.4496 0.5102 0.0875  0.0999  -0.0234 166 THR B CA  
3575 C  C   . THR B 190 ? 0.5020 0.4528 0.5021 0.0796  0.0957  -0.0262 166 THR B C   
3576 O  O   . THR B 190 ? 0.5111 0.4687 0.5068 0.0786  0.0988  -0.0265 166 THR B O   
3577 C  CB  . THR B 190 ? 0.4976 0.4668 0.5254 0.0883  0.0990  -0.0145 166 THR B CB  
3578 O  OG1 . THR B 190 ? 0.5030 0.4740 0.5429 0.0961  0.1027  -0.0111 166 THR B OG1 
3579 C  CG2 . THR B 190 ? 0.4325 0.4065 0.4637 0.0814  0.0898  -0.0103 166 THR B CG2 
3580 N  N   . ARG B 191 ? 0.4765 0.4192 0.4716 0.0741  0.0888  -0.0277 167 ARG B N   
3581 C  CA  . ARG B 191 ? 0.4719 0.4154 0.4585 0.0664  0.0836  -0.0287 167 ARG B CA  
3582 C  C   . ARG B 191 ? 0.4677 0.4217 0.4637 0.0622  0.0773  -0.0219 167 ARG B C   
3583 O  O   . ARG B 191 ? 0.4753 0.4346 0.4829 0.0647  0.0761  -0.0171 167 ARG B O   
3584 C  CB  . ARG B 191 ? 0.4842 0.4127 0.4593 0.0631  0.0802  -0.0350 167 ARG B CB  
3585 C  CG  . ARG B 191 ? 0.5080 0.4262 0.4722 0.0664  0.0857  -0.0432 167 ARG B CG  
3586 C  CD  . ARG B 191 ? 0.5623 0.4665 0.5158 0.0622  0.0817  -0.0498 167 ARG B CD  
3587 N  NE  . ARG B 191 ? 0.6168 0.5239 0.5624 0.0549  0.0763  -0.0498 167 ARG B NE  
3588 C  CZ  . ARG B 191 ? 0.6108 0.5219 0.5466 0.0533  0.0780  -0.0522 167 ARG B CZ  
3589 N  NH1 . ARG B 191 ? 0.6635 0.5770 0.5953 0.0583  0.0849  -0.0548 167 ARG B NH1 
3590 N  NH2 . ARG B 191 ? 0.6423 0.5557 0.5723 0.0469  0.0727  -0.0514 167 ARG B NH2 
3591 N  N   . PHE B 192 ? 0.4332 0.3907 0.4244 0.0558  0.0734  -0.0216 168 PHE B N   
3592 C  CA  . PHE B 192 ? 0.4484 0.4171 0.4487 0.0519  0.0685  -0.0161 168 PHE B CA  
3593 C  C   . PHE B 192 ? 0.4574 0.4216 0.4534 0.0460  0.0611  -0.0168 168 PHE B C   
3594 O  O   . PHE B 192 ? 0.4713 0.4258 0.4563 0.0432  0.0597  -0.0211 168 PHE B O   
3595 C  CB  . PHE B 192 ? 0.4555 0.4344 0.4573 0.0497  0.0706  -0.0138 168 PHE B CB  
3596 C  CG  . PHE B 192 ? 0.4553 0.4406 0.4618 0.0555  0.0784  -0.0123 168 PHE B CG  
3597 C  CD1 . PHE B 192 ? 0.4574 0.4518 0.4779 0.0596  0.0801  -0.0077 168 PHE B CD1 
3598 C  CD2 . PHE B 192 ? 0.4769 0.4600 0.4736 0.0570  0.0842  -0.0154 168 PHE B CD2 
3599 C  CE1 . PHE B 192 ? 0.4792 0.4803 0.5050 0.0653  0.0876  -0.0061 168 PHE B CE1 
3600 C  CE2 . PHE B 192 ? 0.5025 0.4922 0.5033 0.0627  0.0919  -0.0140 168 PHE B CE2 
3601 C  CZ  . PHE B 192 ? 0.5021 0.5006 0.5179 0.0669  0.0939  -0.0093 168 PHE B CZ  
3602 N  N   . GLU B 193 ? 0.4215 0.3935 0.4267 0.0442  0.0564  -0.0125 169 GLU B N   
3603 C  CA  . GLU B 193 ? 0.4297 0.4015 0.4327 0.0384  0.0496  -0.0123 169 GLU B CA  
3604 C  C   . GLU B 193 ? 0.4405 0.4221 0.4478 0.0345  0.0484  -0.0102 169 GLU B C   
3605 O  O   . GLU B 193 ? 0.4666 0.4591 0.4850 0.0349  0.0476  -0.0065 169 GLU B O   
3606 C  CB  . GLU B 193 ? 0.4516 0.4257 0.4611 0.0392  0.0453  -0.0094 169 GLU B CB  
3607 C  CG  . GLU B 193 ? 0.4594 0.4354 0.4676 0.0338  0.0387  -0.0091 169 GLU B CG  
3608 C  CD  . GLU B 193 ? 0.5461 0.5271 0.5607 0.0352  0.0347  -0.0057 169 GLU B CD  
3609 O  OE1 . GLU B 193 ? 0.5726 0.5636 0.5970 0.0380  0.0350  -0.0022 169 GLU B OE1 
3610 O  OE2 . GLU B 193 ? 0.6240 0.5998 0.6340 0.0336  0.0314  -0.0062 169 GLU B OE2 
3611 N  N   . PHE B 194 ? 0.4023 0.3805 0.4015 0.0307  0.0483  -0.0123 170 PHE B N   
3612 C  CA  . PHE B 194 ? 0.4208 0.4068 0.4241 0.0271  0.0479  -0.0100 170 PHE B CA  
3613 C  C   . PHE B 194 ? 0.4279 0.4173 0.4360 0.0225  0.0412  -0.0090 170 PHE B C   
3614 O  O   . PHE B 194 ? 0.4381 0.4213 0.4395 0.0195  0.0374  -0.0112 170 PHE B O   
3615 C  CB  . PHE B 194 ? 0.4172 0.3985 0.4100 0.0251  0.0502  -0.0119 170 PHE B CB  
3616 C  CG  . PHE B 194 ? 0.4214 0.3988 0.4072 0.0297  0.0566  -0.0142 170 PHE B CG  
3617 C  CD1 . PHE B 194 ? 0.4210 0.4061 0.4115 0.0328  0.0625  -0.0116 170 PHE B CD1 
3618 C  CD2 . PHE B 194 ? 0.4259 0.3922 0.4006 0.0309  0.0567  -0.0192 170 PHE B CD2 
3619 C  CE1 . PHE B 194 ? 0.4384 0.4201 0.4215 0.0375  0.0689  -0.0143 170 PHE B CE1 
3620 C  CE2 . PHE B 194 ? 0.4415 0.4037 0.4092 0.0351  0.0625  -0.0224 170 PHE B CE2 
3621 C  CZ  . PHE B 194 ? 0.4607 0.4306 0.4321 0.0387  0.0688  -0.0202 170 PHE B CZ  
3622 N  N   . GLU B 195 ? 0.4177 0.4176 0.4379 0.0220  0.0397  -0.0059 171 GLU B N   
3623 C  CA  . GLU B 195 ? 0.3969 0.4010 0.4224 0.0181  0.0334  -0.0058 171 GLU B CA  
3624 C  C   . GLU B 195 ? 0.3752 0.3809 0.4021 0.0131  0.0324  -0.0055 171 GLU B C   
3625 O  O   . GLU B 195 ? 0.3683 0.3806 0.4027 0.0125  0.0353  -0.0028 171 GLU B O   
3626 C  CB  . GLU B 195 ? 0.4173 0.4324 0.4552 0.0197  0.0316  -0.0031 171 GLU B CB  
3627 C  CG  . GLU B 195 ? 0.4551 0.4705 0.4944 0.0258  0.0345  -0.0017 171 GLU B CG  
3628 C  CD  . GLU B 195 ? 0.5172 0.5250 0.5493 0.0272  0.0318  -0.0032 171 GLU B CD  
3629 O  OE1 . GLU B 195 ? 0.5559 0.5586 0.5814 0.0235  0.0280  -0.0055 171 GLU B OE1 
3630 O  OE2 . GLU B 195 ? 0.5470 0.5542 0.5809 0.0322  0.0338  -0.0016 171 GLU B OE2 
3631 N  N   . CYS B 196 ? 0.3563 0.3561 0.3770 0.0096  0.0286  -0.0078 172 CYS B N   
3632 C  CA  . CYS B 196 ? 0.3543 0.3537 0.3757 0.0053  0.0278  -0.0074 172 CYS B CA  
3633 C  C   . CYS B 196 ? 0.3645 0.3657 0.3905 0.0017  0.0218  -0.0091 172 CYS B C   
3634 O  O   . CYS B 196 ? 0.3521 0.3485 0.3718 0.0014  0.0185  -0.0116 172 CYS B O   
3635 C  CB  . CYS B 196 ? 0.3676 0.3581 0.3767 0.0048  0.0295  -0.0086 172 CYS B CB  
3636 S  SG  . CYS B 196 ? 0.3760 0.3649 0.3784 0.0089  0.0367  -0.0078 172 CYS B SG  
3637 N  N   . TYR B 197 ? 0.3481 0.3564 0.3854 -0.0011 0.0205  -0.0078 173 TYR B N   
3638 C  CA  . TYR B 197 ? 0.3684 0.3794 0.4114 -0.0044 0.0148  -0.0103 173 TYR B CA  
3639 C  C   . TYR B 197 ? 0.3350 0.3416 0.3784 -0.0085 0.0135  -0.0111 173 TYR B C   
3640 O  O   . TYR B 197 ? 0.3429 0.3502 0.3900 -0.0112 0.0089  -0.0142 173 TYR B O   
3641 C  CB  . TYR B 197 ? 0.3516 0.3735 0.4085 -0.0052 0.0133  -0.0092 173 TYR B CB  
3642 C  CG  . TYR B 197 ? 0.3830 0.4108 0.4416 -0.0008 0.0142  -0.0077 173 TYR B CG  
3643 C  CD1 . TYR B 197 ? 0.3670 0.3954 0.4251 0.0029  0.0201  -0.0045 173 TYR B CD1 
3644 C  CD2 . TYR B 197 ? 0.3965 0.4296 0.4572 0.0000  0.0093  -0.0094 173 TYR B CD2 
3645 C  CE1 . TYR B 197 ? 0.4115 0.4449 0.4721 0.0075  0.0212  -0.0029 173 TYR B CE1 
3646 C  CE2 . TYR B 197 ? 0.4048 0.4437 0.4679 0.0044  0.0101  -0.0072 173 TYR B CE2 
3647 C  CZ  . TYR B 197 ? 0.4501 0.4888 0.5137 0.0082  0.0161  -0.0039 173 TYR B CZ  
3648 O  OH  . TYR B 197 ? 0.4722 0.5162 0.5391 0.0130  0.0172  -0.0014 173 TYR B OH  
3649 N  N   . ASP B 198 ? 0.3104 0.3127 0.3499 -0.0089 0.0174  -0.0086 174 ASP B N   
3650 C  CA  . ASP B 198 ? 0.3329 0.3309 0.3730 -0.0123 0.0166  -0.0082 174 ASP B CA  
3651 C  C   . ASP B 198 ? 0.3554 0.3492 0.3874 -0.0112 0.0211  -0.0049 174 ASP B C   
3652 O  O   . ASP B 198 ? 0.3784 0.3728 0.4048 -0.0080 0.0249  -0.0037 174 ASP B O   
3653 C  CB  . ASP B 198 ? 0.3220 0.3251 0.3767 -0.0160 0.0156  -0.0070 174 ASP B CB  
3654 C  CG  . ASP B 198 ? 0.3665 0.3643 0.4234 -0.0195 0.0129  -0.0084 174 ASP B CG  
3655 O  OD1 . ASP B 198 ? 0.4046 0.3958 0.4517 -0.0188 0.0123  -0.0096 174 ASP B OD1 
3656 O  OD2 . ASP B 198 ? 0.3689 0.3693 0.4382 -0.0229 0.0115  -0.0084 174 ASP B OD2 
3657 N  N   . THR B 199 ? 0.3350 0.3248 0.3664 -0.0136 0.0207  -0.0036 175 THR B N   
3658 C  CA  . THR B 199 ? 0.3452 0.3317 0.3677 -0.0126 0.0242  -0.0005 175 THR B CA  
3659 C  C   . THR B 199 ? 0.3348 0.3266 0.3595 -0.0112 0.0298  0.0041  175 THR B C   
3660 O  O   . THR B 199 ? 0.3524 0.3429 0.3668 -0.0085 0.0332  0.0050  175 THR B O   
3661 C  CB  . THR B 199 ? 0.3790 0.3619 0.4033 -0.0154 0.0228  0.0014  175 THR B CB  
3662 O  OG1 . THR B 199 ? 0.3469 0.3273 0.3751 -0.0172 0.0179  -0.0028 175 THR B OG1 
3663 C  CG2 . THR B 199 ? 0.3823 0.3606 0.3939 -0.0142 0.0237  0.0026  175 THR B CG2 
3664 N  N   . SER B 200 ? 0.3513 0.3492 0.3894 -0.0129 0.0309  0.0069  176 SER B N   
3665 C  CA  . SER B 200 ? 0.3631 0.3672 0.4049 -0.0116 0.0367  0.0122  176 SER B CA  
3666 C  C   . SER B 200 ? 0.3291 0.3354 0.3642 -0.0070 0.0400  0.0107  176 SER B C   
3667 O  O   . SER B 200 ? 0.3454 0.3544 0.3763 -0.0045 0.0456  0.0140  176 SER B O   
3668 C  CB  . SER B 200 ? 0.3653 0.3763 0.4248 -0.0147 0.0367  0.0152  176 SER B CB  
3669 O  OG  . SER B 200 ? 0.3905 0.4050 0.4566 -0.0147 0.0332  0.0111  176 SER B OG  
3670 N  N   . HIS B 201 ? 0.3374 0.3427 0.3715 -0.0056 0.0368  0.0060  177 HIS B N   
3671 C  CA  . HIS B 201 ? 0.3455 0.3522 0.3747 -0.0009 0.0399  0.0048  177 HIS B CA  
3672 C  C   . HIS B 201 ? 0.3655 0.3648 0.3786 0.0017  0.0419  0.0027  177 HIS B C   
3673 O  O   . HIS B 201 ? 0.3945 0.3947 0.4025 0.0056  0.0468  0.0028  177 HIS B O   
3674 C  CB  . HIS B 201 ? 0.3443 0.3522 0.3776 0.0000  0.0358  0.0013  177 HIS B CB  
3675 C  CG  . HIS B 201 ? 0.3787 0.3952 0.4276 -0.0023 0.0336  0.0028  177 HIS B CG  
3676 N  ND1 . HIS B 201 ? 0.3875 0.4083 0.4417 -0.0012 0.0302  0.0008  177 HIS B ND1 
3677 C  CD2 . HIS B 201 ? 0.3720 0.3937 0.4327 -0.0059 0.0339  0.0061  177 HIS B CD2 
3678 C  CE1 . HIS B 201 ? 0.3970 0.4259 0.4653 -0.0042 0.0282  0.0022  177 HIS B CE1 
3679 N  NE2 . HIS B 201 ? 0.4124 0.4415 0.4854 -0.0072 0.0305  0.0053  177 HIS B NE2 
3680 N  N   . LEU B 202 ? 0.3751 0.3674 0.3803 -0.0003 0.0383  0.0005  178 LEU B N   
3681 C  CA  . LEU B 202 ? 0.3870 0.3732 0.3777 0.0013  0.0396  -0.0015 178 LEU B CA  
3682 C  C   . LEU B 202 ? 0.3665 0.3556 0.3533 0.0018  0.0445  0.0026  178 LEU B C   
3683 O  O   . LEU B 202 ? 0.3855 0.3730 0.3618 0.0048  0.0481  0.0012  178 LEU B O   
3684 C  CB  . LEU B 202 ? 0.3482 0.3278 0.3333 -0.0013 0.0344  -0.0039 178 LEU B CB  
3685 C  CG  . LEU B 202 ? 0.3590 0.3354 0.3450 -0.0014 0.0300  -0.0079 178 LEU B CG  
3686 C  CD1 . LEU B 202 ? 0.3656 0.3367 0.3469 -0.0039 0.0256  -0.0095 178 LEU B CD1 
3687 C  CD2 . LEU B 202 ? 0.3622 0.3355 0.3422 0.0023  0.0317  -0.0109 178 LEU B CD2 
3688 N  N   . TYR B 203 ? 0.3483 0.3415 0.3432 -0.0011 0.0448  0.0076  179 TYR B N   
3689 C  CA  . TYR B 203 ? 0.3457 0.3431 0.3379 -0.0004 0.0498  0.0129  179 TYR B CA  
3690 C  C   . TYR B 203 ? 0.3977 0.4020 0.3932 0.0030  0.0561  0.0149  179 TYR B C   
3691 O  O   . TYR B 203 ? 0.4010 0.4073 0.3874 0.0059  0.0612  0.0163  179 TYR B O   
3692 C  CB  . TYR B 203 ? 0.3494 0.3493 0.3518 -0.0043 0.0489  0.0187  179 TYR B CB  
3693 C  CG  . TYR B 203 ? 0.3886 0.3827 0.3851 -0.0066 0.0449  0.0186  179 TYR B CG  
3694 C  CD1 . TYR B 203 ? 0.4052 0.3994 0.3911 -0.0058 0.0468  0.0218  179 TYR B CD1 
3695 C  CD2 . TYR B 203 ? 0.3944 0.3839 0.3958 -0.0093 0.0391  0.0155  179 TYR B CD2 
3696 C  CE1 . TYR B 203 ? 0.4337 0.4237 0.4151 -0.0077 0.0430  0.0223  179 TYR B CE1 
3697 C  CE2 . TYR B 203 ? 0.4217 0.4065 0.4186 -0.0109 0.0358  0.0157  179 TYR B CE2 
3698 C  CZ  . TYR B 203 ? 0.4400 0.4251 0.4274 -0.0101 0.0377  0.0194  179 TYR B CZ  
3699 O  OH  . TYR B 203 ? 0.4261 0.4075 0.4100 -0.0116 0.0343  0.0202  179 TYR B OH  
3700 N  N   . ASN B 204 ? 0.3726 0.3814 0.3809 0.0030  0.0559  0.0150  180 ASN B N   
3701 C  CA  . ASN B 204 ? 0.3964 0.4122 0.4088 0.0069  0.0618  0.0168  180 ASN B CA  
3702 C  C   . ASN B 204 ? 0.4151 0.4264 0.4139 0.0119  0.0644  0.0117  180 ASN B C   
3703 O  O   . ASN B 204 ? 0.4250 0.4399 0.4191 0.0157  0.0709  0.0131  180 ASN B O   
3704 C  CB  . ASN B 204 ? 0.3645 0.3858 0.3927 0.0061  0.0598  0.0170  180 ASN B CB  
3705 C  CG  . ASN B 204 ? 0.3989 0.4252 0.4422 0.0010  0.0577  0.0215  180 ASN B CG  
3706 O  OD1 . ASN B 204 ? 0.3676 0.3945 0.4113 -0.0012 0.0595  0.0261  180 ASN B OD1 
3707 N  ND2 . ASN B 204 ? 0.3842 0.4142 0.4402 -0.0009 0.0538  0.0203  180 ASN B ND2 
3708 N  N   . LEU B 205 ? 0.3953 0.3984 0.3877 0.0120  0.0597  0.0058  181 LEU B N   
3709 C  CA  . LEU B 205 ? 0.4132 0.4105 0.3938 0.0162  0.0618  0.0006  181 LEU B CA  
3710 C  C   . LEU B 205 ? 0.4370 0.4310 0.4025 0.0169  0.0642  -0.0005 181 LEU B C   
3711 O  O   . LEU B 205 ? 0.4475 0.4404 0.4042 0.0211  0.0690  -0.0034 181 LEU B O   
3712 C  CB  . LEU B 205 ? 0.3966 0.3859 0.3750 0.0155  0.0561  -0.0045 181 LEU B CB  
3713 C  CG  . LEU B 205 ? 0.4083 0.3898 0.3762 0.0193  0.0574  -0.0102 181 LEU B CG  
3714 C  CD1 . LEU B 205 ? 0.4194 0.4046 0.3908 0.0248  0.0636  -0.0101 181 LEU B CD1 
3715 C  CD2 . LEU B 205 ? 0.3972 0.3720 0.3655 0.0180  0.0517  -0.0135 181 LEU B CD2 
3716 N  N   . LYS B 206 ? 0.4175 0.4102 0.3797 0.0129  0.0610  0.0015  182 LYS B N   
3717 C  CA  . LYS B 206 ? 0.4470 0.4382 0.3949 0.0133  0.0625  0.0012  182 LYS B CA  
3718 C  C   . LYS B 206 ? 0.4791 0.4785 0.4253 0.0164  0.0701  0.0055  182 LYS B C   
3719 O  O   . LYS B 206 ? 0.4852 0.4839 0.4176 0.0192  0.0733  0.0030  182 LYS B O   
3720 C  CB  . LYS B 206 ? 0.4526 0.4426 0.4004 0.0087  0.0577  0.0042  182 LYS B CB  
3721 C  CG  . LYS B 206 ? 0.4787 0.4686 0.4126 0.0086  0.0583  0.0050  182 LYS B CG  
3722 C  CD  . LYS B 206 ? 0.5179 0.5004 0.4373 0.0100  0.0563  -0.0029 182 LYS B CD  
3723 C  CE  . LYS B 206 ? 0.5573 0.5403 0.4635 0.0090  0.0550  -0.0022 182 LYS B CE  
3724 N  NZ  . LYS B 206 ? 0.5771 0.5534 0.4691 0.0100  0.0532  -0.0105 182 LYS B NZ  
3725 N  N   . HIS B 207 ? 0.4494 0.4571 0.4097 0.0159  0.0730  0.0119  183 HIS B N   
3726 C  CA  . HIS B 207 ? 0.4814 0.4981 0.4419 0.0190  0.0808  0.0170  183 HIS B CA  
3727 C  C   . HIS B 207 ? 0.5092 0.5259 0.4631 0.0249  0.0862  0.0121  183 HIS B C   
3728 O  O   . HIS B 207 ? 0.5353 0.5547 0.4779 0.0284  0.0918  0.0120  183 HIS B O   
3729 C  CB  . HIS B 207 ? 0.4862 0.5116 0.4659 0.0168  0.0823  0.0245  183 HIS B CB  
3730 C  CG  . HIS B 207 ? 0.5194 0.5551 0.5032 0.0204  0.0908  0.0297  183 HIS B CG  
3731 N  ND1 . HIS B 207 ? 0.5392 0.5812 0.5175 0.0212  0.0961  0.0359  183 HIS B ND1 
3732 C  CD2 . HIS B 207 ? 0.5045 0.5463 0.4978 0.0237  0.0952  0.0302  183 HIS B CD2 
3733 C  CE1 . HIS B 207 ? 0.5478 0.5993 0.5319 0.0249  0.1037  0.0399  183 HIS B CE1 
3734 N  NE2 . HIS B 207 ? 0.5525 0.6040 0.5462 0.0264  0.1033  0.0364  183 HIS B NE2 
3735 N  N   . PHE B 208 ? 0.4632 0.4767 0.4240 0.0265  0.0848  0.0081  184 PHE B N   
3736 C  CA  . PHE B 208 ? 0.5304 0.5432 0.4868 0.0326  0.0901  0.0035  184 PHE B CA  
3737 C  C   . PHE B 208 ? 0.5445 0.5468 0.4828 0.0343  0.0889  -0.0048 184 PHE B C   
3738 O  O   . PHE B 208 ? 0.6059 0.6079 0.5345 0.0392  0.0947  -0.0085 184 PHE B O   
3739 C  CB  . PHE B 208 ? 0.4979 0.5108 0.4678 0.0338  0.0886  0.0026  184 PHE B CB  
3740 C  CG  . PHE B 208 ? 0.5027 0.5271 0.4908 0.0328  0.0904  0.0100  184 PHE B CG  
3741 C  CD1 . PHE B 208 ? 0.5121 0.5464 0.5044 0.0365  0.0985  0.0145  184 PHE B CD1 
3742 C  CD2 . PHE B 208 ? 0.4824 0.5081 0.4834 0.0281  0.0841  0.0122  184 PHE B CD2 
3743 C  CE1 . PHE B 208 ? 0.5129 0.5584 0.5233 0.0351  0.1001  0.0215  184 PHE B CE1 
3744 C  CE2 . PHE B 208 ? 0.4644 0.5007 0.4827 0.0266  0.0853  0.0184  184 PHE B CE2 
3745 C  CZ  . PHE B 208 ? 0.4807 0.5270 0.5043 0.0299  0.0932  0.0233  184 PHE B CZ  
3746 N  N   . TYR B 209 ? 0.5306 0.5244 0.4647 0.0303  0.0816  -0.0082 185 TYR B N   
3747 C  CA  . TYR B 209 ? 0.5669 0.5510 0.4853 0.0308  0.0795  -0.0160 185 TYR B CA  
3748 C  C   . TYR B 209 ? 0.5959 0.5828 0.4994 0.0319  0.0829  -0.0163 185 TYR B C   
3749 O  O   . TYR B 209 ? 0.6085 0.5912 0.4993 0.0353  0.0857  -0.0230 185 TYR B O   
3750 C  CB  . TYR B 209 ? 0.5524 0.5293 0.4709 0.0256  0.0710  -0.0177 185 TYR B CB  
3751 C  CG  . TYR B 209 ? 0.5723 0.5392 0.4767 0.0249  0.0677  -0.0253 185 TYR B CG  
3752 C  CD1 . TYR B 209 ? 0.5690 0.5278 0.4696 0.0281  0.0689  -0.0324 185 TYR B CD1 
3753 C  CD2 . TYR B 209 ? 0.5402 0.5060 0.4365 0.0209  0.0631  -0.0251 185 TYR B CD2 
3754 C  CE1 . TYR B 209 ? 0.6142 0.5637 0.5033 0.0268  0.0655  -0.0395 185 TYR B CE1 
3755 C  CE2 . TYR B 209 ? 0.5914 0.5490 0.4760 0.0197  0.0595  -0.0319 185 TYR B CE2 
3756 C  CZ  . TYR B 209 ? 0.6107 0.5600 0.4918 0.0224  0.0606  -0.0394 185 TYR B CZ  
3757 O  OH  . TYR B 209 ? 0.6668 0.6076 0.5374 0.0206  0.0568  -0.0465 185 TYR B OH  
3758 N  N   . ASP B 210 ? 0.5782 0.5726 0.4832 0.0290  0.0827  -0.0090 186 ASP B N   
3759 C  CA  . ASP B 210 ? 0.6132 0.6119 0.5040 0.0300  0.0857  -0.0079 186 ASP B CA  
3760 C  C   . ASP B 210 ? 0.6421 0.6478 0.5291 0.0360  0.0950  -0.0075 186 ASP B C   
3761 O  O   . ASP B 210 ? 0.7159 0.7222 0.5867 0.0387  0.0979  -0.0112 186 ASP B O   
3762 C  CB  . ASP B 210 ? 0.5772 0.5826 0.4728 0.0259  0.0837  0.0013  186 ASP B CB  
3763 C  CG  . ASP B 210 ? 0.6109 0.6096 0.5057 0.0207  0.0751  0.0001  186 ASP B CG  
3764 O  OD1 . ASP B 210 ? 0.6374 0.6272 0.5252 0.0202  0.0708  -0.0078 186 ASP B OD1 
3765 O  OD2 . ASP B 210 ? 0.6555 0.6579 0.5573 0.0172  0.0728  0.0073  186 ASP B OD2 
3766 N  N   . ARG B 211 ? 0.6404 0.6520 0.5419 0.0382  0.0996  -0.0031 187 ARG B N   
3767 C  CA  . ARG B 211 ? 0.6561 0.6748 0.5557 0.0444  0.1089  -0.0027 187 ARG B CA  
3768 C  C   . ARG B 211 ? 0.6660 0.6765 0.5582 0.0496  0.1113  -0.0129 187 ARG B C   
3769 O  O   . ARG B 211 ? 0.7010 0.7162 0.5892 0.0556  0.1194  -0.0141 187 ARG B O   
3770 C  CB  . ARG B 211 ? 0.6397 0.6683 0.5593 0.0448  0.1128  0.0058  187 ARG B CB  
3771 C  CG  . ARG B 211 ? 0.6445 0.6828 0.5716 0.0410  0.1133  0.0166  187 ARG B CG  
3772 C  CD  . ARG B 211 ? 0.6977 0.7448 0.6468 0.0402  0.1157  0.0240  187 ARG B CD  
3773 N  NE  . ARG B 211 ? 0.8096 0.8636 0.7621 0.0465  0.1242  0.0242  187 ARG B NE  
3774 C  CZ  . ARG B 211 ? 0.7742 0.8363 0.7455 0.0471  0.1269  0.0293  187 ARG B CZ  
3775 N  NH1 . ARG B 211 ? 0.7106 0.7746 0.6989 0.0415  0.1215  0.0341  187 ARG B NH1 
3776 N  NH2 . ARG B 211 ? 0.7952 0.8639 0.7687 0.0535  0.1351  0.0292  187 ARG B NH2 
3777 N  N   . GLY B 212 ? 0.6850 0.6835 0.5758 0.0476  0.1048  -0.0199 188 GLY B N   
3778 C  CA  . GLY B 212 ? 0.6608 0.6500 0.5456 0.0521  0.1066  -0.0294 188 GLY B CA  
3779 C  C   . GLY B 212 ? 0.6913 0.6814 0.5911 0.0561  0.1101  -0.0284 188 GLY B C   
3780 O  O   . GLY B 212 ? 0.6921 0.6760 0.5883 0.0614  0.1139  -0.0353 188 GLY B O   
3781 N  N   . LEU B 213 ? 0.6441 0.6417 0.5613 0.0539  0.1087  -0.0203 189 LEU B N   
3782 C  CA  . LEU B 213 ? 0.6316 0.6318 0.5640 0.0575  0.1114  -0.0185 189 LEU B CA  
3783 C  C   . LEU B 213 ? 0.6409 0.6303 0.5774 0.0566  0.1053  -0.0231 189 LEU B C   
3784 O  O   . LEU B 213 ? 0.6439 0.6334 0.5903 0.0608  0.1077  -0.0232 189 LEU B O   
3785 C  CB  . LEU B 213 ? 0.6182 0.6313 0.5679 0.0550  0.1117  -0.0084 189 LEU B CB  
3786 C  CG  . LEU B 213 ? 0.6937 0.7190 0.6426 0.0567  0.1191  -0.0022 189 LEU B CG  
3787 C  CD1 . LEU B 213 ? 0.7431 0.7794 0.7092 0.0522  0.1177  0.0077  189 LEU B CD1 
3788 C  CD2 . LEU B 213 ? 0.6849 0.7148 0.6337 0.0648  0.1287  -0.0038 189 LEU B CD2 
3789 N  N   . VAL B 214 ? 0.6332 0.6140 0.5630 0.0514  0.0978  -0.0263 190 VAL B N   
3790 C  CA  . VAL B 214 ? 0.6332 0.6029 0.5644 0.0506  0.0926  -0.0310 190 VAL B CA  
3791 C  C   . VAL B 214 ? 0.6531 0.6119 0.5683 0.0479  0.0887  -0.0381 190 VAL B C   
3792 O  O   . VAL B 214 ? 0.6670 0.6281 0.5748 0.0436  0.0859  -0.0369 190 VAL B O   
3793 C  CB  . VAL B 214 ? 0.5868 0.5590 0.5313 0.0460  0.0859  -0.0258 190 VAL B CB  
3794 C  CG1 . VAL B 214 ? 0.5489 0.5302 0.5097 0.0492  0.0888  -0.0205 190 VAL B CG1 
3795 C  CG2 . VAL B 214 ? 0.5626 0.5399 0.5065 0.0399  0.0818  -0.0213 190 VAL B CG2 
3796 N  N   . LYS B 215 ? 0.6473 0.5947 0.5582 0.0503  0.0886  -0.0454 191 LYS B N   
3797 C  CA  . LYS B 215 ? 0.6405 0.5770 0.5376 0.0476  0.0847  -0.0530 191 LYS B CA  
3798 C  C   . LYS B 215 ? 0.6281 0.5569 0.5306 0.0432  0.0772  -0.0532 191 LYS B C   
3799 O  O   . LYS B 215 ? 0.6209 0.5489 0.5355 0.0446  0.0765  -0.0504 191 LYS B O   
3800 C  CB  . LYS B 215 ? 0.6670 0.5950 0.5552 0.0530  0.0899  -0.0620 191 LYS B CB  
3801 C  CG  . LYS B 215 ? 0.7583 0.6936 0.6382 0.0577  0.0978  -0.0630 191 LYS B CG  
3802 C  CD  . LYS B 215 ? 0.8177 0.7574 0.6833 0.0539  0.0958  -0.0634 191 LYS B CD  
3803 C  CE  . LYS B 215 ? 0.8702 0.8170 0.7256 0.0592  0.1040  -0.0650 191 LYS B CE  
3804 N  NZ  . LYS B 215 ? 0.8854 0.8444 0.7529 0.0632  0.1107  -0.0566 191 LYS B NZ  
3805 N  N   . GLY B 216 ? 0.6295 0.5535 0.5230 0.0380  0.0715  -0.0562 192 GLY B N   
3806 C  CA  . GLY B 216 ? 0.6019 0.5190 0.4995 0.0337  0.0647  -0.0565 192 GLY B CA  
3807 C  C   . GLY B 216 ? 0.5961 0.5010 0.4946 0.0362  0.0653  -0.0624 192 GLY B C   
3808 O  O   . GLY B 216 ? 0.6164 0.5167 0.5102 0.0409  0.0705  -0.0679 192 GLY B O   
3809 N  N   . PRO B 217 ? 0.5939 0.4933 0.4989 0.0332  0.0601  -0.0611 193 PRO B N   
3810 C  CA  . PRO B 217 ? 0.5789 0.4835 0.4896 0.0281  0.0541  -0.0552 193 PRO B CA  
3811 C  C   . PRO B 217 ? 0.5434 0.4578 0.4665 0.0299  0.0552  -0.0477 193 PRO B C   
3812 O  O   . PRO B 217 ? 0.5694 0.4834 0.5005 0.0343  0.0582  -0.0464 193 PRO B O   
3813 C  CB  . PRO B 217 ? 0.5498 0.4442 0.4626 0.0257  0.0498  -0.0574 193 PRO B CB  
3814 C  CG  . PRO B 217 ? 0.5673 0.4536 0.4829 0.0310  0.0542  -0.0610 193 PRO B CG  
3815 C  CD  . PRO B 217 ? 0.5627 0.4499 0.4701 0.0350  0.0602  -0.0657 193 PRO B CD  
3816 N  N   . LEU B 218 ? 0.5282 0.4513 0.4534 0.0264  0.0526  -0.0428 194 LEU B N   
3817 C  CA  . LEU B 218 ? 0.5091 0.4421 0.4462 0.0272  0.0531  -0.0363 194 LEU B CA  
3818 C  C   . LEU B 218 ? 0.4825 0.4147 0.4276 0.0253  0.0480  -0.0337 194 LEU B C   
3819 O  O   . LEU B 218 ? 0.4903 0.4197 0.4326 0.0209  0.0430  -0.0340 194 LEU B O   
3820 C  CB  . LEU B 218 ? 0.4988 0.4407 0.4355 0.0243  0.0526  -0.0324 194 LEU B CB  
3821 C  CG  . LEU B 218 ? 0.4895 0.4341 0.4174 0.0259  0.0575  -0.0337 194 LEU B CG  
3822 C  CD1 . LEU B 218 ? 0.5012 0.4545 0.4307 0.0225  0.0566  -0.0283 194 LEU B CD1 
3823 C  CD2 . LEU B 218 ? 0.5290 0.4767 0.4602 0.0319  0.0645  -0.0338 194 LEU B CD2 
3824 N  N   . PHE B 219 ? 0.4400 0.3756 0.3951 0.0288  0.0494  -0.0308 195 PHE B N   
3825 C  CA  . PHE B 219 ? 0.4489 0.3860 0.4117 0.0275  0.0449  -0.0275 195 PHE B CA  
3826 C  C   . PHE B 219 ? 0.4495 0.3977 0.4192 0.0250  0.0426  -0.0232 195 PHE B C   
3827 O  O   . PHE B 219 ? 0.4409 0.3974 0.4193 0.0273  0.0444  -0.0199 195 PHE B O   
3828 C  CB  . PHE B 219 ? 0.4408 0.3768 0.4109 0.0327  0.0472  -0.0262 195 PHE B CB  
3829 C  CG  . PHE B 219 ? 0.4607 0.3970 0.4366 0.0320  0.0428  -0.0230 195 PHE B CG  
3830 C  CD1 . PHE B 219 ? 0.4792 0.4121 0.4512 0.0273  0.0378  -0.0235 195 PHE B CD1 
3831 C  CD2 . PHE B 219 ? 0.4526 0.3935 0.4381 0.0363  0.0437  -0.0191 195 PHE B CD2 
3832 C  CE1 . PHE B 219 ? 0.5019 0.4360 0.4786 0.0270  0.0343  -0.0203 195 PHE B CE1 
3833 C  CE2 . PHE B 219 ? 0.5124 0.4547 0.5025 0.0359  0.0397  -0.0157 195 PHE B CE2 
3834 C  CZ  . PHE B 219 ? 0.4994 0.4383 0.4847 0.0313  0.0352  -0.0163 195 PHE B CZ  
3835 N  N   . ILE B 220 ? 0.4261 0.3743 0.3924 0.0200  0.0384  -0.0232 196 ILE B N   
3836 C  CA  . ILE B 220 ? 0.4343 0.3912 0.4065 0.0171  0.0361  -0.0201 196 ILE B CA  
3837 C  C   . ILE B 220 ? 0.4458 0.4050 0.4236 0.0155  0.0311  -0.0186 196 ILE B C   
3838 O  O   . ILE B 220 ? 0.4278 0.3816 0.4012 0.0135  0.0278  -0.0200 196 ILE B O   
3839 C  CB  . ILE B 220 ? 0.4357 0.3915 0.4012 0.0131  0.0350  -0.0207 196 ILE B CB  
3840 C  CG1 . ILE B 220 ? 0.3769 0.3312 0.3352 0.0150  0.0400  -0.0222 196 ILE B CG1 
3841 C  CG2 . ILE B 220 ? 0.3807 0.3443 0.3537 0.0102  0.0329  -0.0174 196 ILE B CG2 
3842 C  CD1 . ILE B 220 ? 0.4326 0.3878 0.3848 0.0117  0.0394  -0.0215 196 ILE B CD1 
3843 N  N   . GLN B 221 ? 0.4141 0.3821 0.4017 0.0164  0.0304  -0.0158 197 GLN B N   
3844 C  CA  . GLN B 221 ? 0.3979 0.3700 0.3905 0.0152  0.0256  -0.0146 197 GLN B CA  
3845 C  C   . GLN B 221 ? 0.4182 0.3968 0.4156 0.0112  0.0228  -0.0140 197 GLN B C   
3846 O  O   . GLN B 221 ? 0.4205 0.4062 0.4254 0.0112  0.0243  -0.0123 197 GLN B O   
3847 C  CB  . GLN B 221 ? 0.4431 0.4210 0.4436 0.0192  0.0261  -0.0121 197 GLN B CB  
3848 C  CG  . GLN B 221 ? 0.4501 0.4340 0.4550 0.0182  0.0210  -0.0108 197 GLN B CG  
3849 C  CD  . GLN B 221 ? 0.4736 0.4560 0.4789 0.0220  0.0207  -0.0089 197 GLN B CD  
3850 O  OE1 . GLN B 221 ? 0.4628 0.4383 0.4621 0.0215  0.0194  -0.0095 197 GLN B OE1 
3851 N  NE2 . GLN B 221 ? 0.5501 0.5392 0.5631 0.0260  0.0220  -0.0059 197 GLN B NE2 
3852 N  N   . THR B 222 ? 0.3870 0.3630 0.3809 0.0079  0.0190  -0.0154 198 THR B N   
3853 C  CA  . THR B 222 ? 0.3809 0.3612 0.3793 0.0043  0.0162  -0.0156 198 THR B CA  
3854 C  C   . THR B 222 ? 0.3542 0.3409 0.3584 0.0041  0.0120  -0.0158 198 THR B C   
3855 O  O   . THR B 222 ? 0.3587 0.3436 0.3591 0.0048  0.0096  -0.0165 198 THR B O   
3856 C  CB  . THR B 222 ? 0.3583 0.3324 0.3499 0.0013  0.0148  -0.0170 198 THR B CB  
3857 O  OG1 . THR B 222 ? 0.3483 0.3180 0.3343 0.0016  0.0126  -0.0183 198 THR B OG1 
3858 C  CG2 . THR B 222 ? 0.3407 0.3103 0.3263 0.0013  0.0185  -0.0167 198 THR B CG2 
3859 N  N   . VAL B 223 ? 0.3128 0.3077 0.3265 0.0030  0.0110  -0.0152 199 VAL B N   
3860 C  CA  . VAL B 223 ? 0.3283 0.3312 0.3481 0.0031  0.0069  -0.0157 199 VAL B CA  
3861 C  C   . VAL B 223 ? 0.3423 0.3466 0.3647 -0.0011 0.0030  -0.0186 199 VAL B C   
3862 O  O   . VAL B 223 ? 0.3362 0.3410 0.3640 -0.0039 0.0037  -0.0186 199 VAL B O   
3863 C  CB  . VAL B 223 ? 0.3761 0.3881 0.4059 0.0047  0.0080  -0.0133 199 VAL B CB  
3864 C  CG1 . VAL B 223 ? 0.3397 0.3611 0.3755 0.0046  0.0029  -0.0140 199 VAL B CG1 
3865 C  CG2 . VAL B 223 ? 0.3612 0.3711 0.3890 0.0094  0.0126  -0.0106 199 VAL B CG2 
3866 N  N   . PHE B 224 ? 0.3493 0.3544 0.3683 -0.0012 -0.0009 -0.0208 200 PHE B N   
3867 C  CA  . PHE B 224 ? 0.3335 0.3387 0.3535 -0.0044 -0.0044 -0.0245 200 PHE B CA  
3868 C  C   . PHE B 224 ? 0.3711 0.3856 0.3960 -0.0047 -0.0091 -0.0269 200 PHE B C   
3869 O  O   . PHE B 224 ? 0.3729 0.3924 0.3959 -0.0017 -0.0103 -0.0256 200 PHE B O   
3870 C  CB  . PHE B 224 ? 0.3509 0.3492 0.3615 -0.0043 -0.0048 -0.0258 200 PHE B CB  
3871 C  CG  . PHE B 224 ? 0.3599 0.3497 0.3647 -0.0042 -0.0012 -0.0239 200 PHE B CG  
3872 C  CD1 . PHE B 224 ? 0.3283 0.3140 0.3341 -0.0068 0.0000  -0.0241 200 PHE B CD1 
3873 C  CD2 . PHE B 224 ? 0.3527 0.3388 0.3514 -0.0015 0.0009  -0.0218 200 PHE B CD2 
3874 C  CE1 . PHE B 224 ? 0.3474 0.3265 0.3472 -0.0067 0.0029  -0.0223 200 PHE B CE1 
3875 C  CE2 . PHE B 224 ? 0.3525 0.3311 0.3455 -0.0018 0.0037  -0.0210 200 PHE B CE2 
3876 C  CZ  . PHE B 224 ? 0.3298 0.3054 0.3228 -0.0043 0.0045  -0.0213 200 PHE B CZ  
3877 N  N   . GLY B 225 ? 0.3681 0.3849 0.3993 -0.0082 -0.0117 -0.0305 201 GLY B N   
3878 C  CA  . GLY B 225 ? 0.3596 0.3843 0.3938 -0.0090 -0.0169 -0.0346 201 GLY B CA  
3879 C  C   . GLY B 225 ? 0.3853 0.4198 0.4308 -0.0104 -0.0192 -0.0348 201 GLY B C   
3880 O  O   . GLY B 225 ? 0.3853 0.4271 0.4334 -0.0116 -0.0242 -0.0389 201 GLY B O   
3881 N  N   . LEU B 226 ? 0.3813 0.4169 0.4336 -0.0104 -0.0158 -0.0306 202 LEU B N   
3882 C  CA  . LEU B 226 ? 0.3888 0.4348 0.4535 -0.0118 -0.0178 -0.0300 202 LEU B CA  
3883 C  C   . LEU B 226 ? 0.3698 0.4155 0.4448 -0.0172 -0.0193 -0.0331 202 LEU B C   
3884 O  O   . LEU B 226 ? 0.3757 0.4128 0.4506 -0.0191 -0.0161 -0.0324 202 LEU B O   
3885 C  CB  . LEU B 226 ? 0.3919 0.4402 0.4605 -0.0090 -0.0130 -0.0239 202 LEU B CB  
3886 C  CG  . LEU B 226 ? 0.4553 0.5030 0.5159 -0.0035 -0.0107 -0.0203 202 LEU B CG  
3887 C  CD1 . LEU B 226 ? 0.5380 0.5902 0.6055 -0.0008 -0.0065 -0.0152 202 LEU B CD1 
3888 C  CD2 . LEU B 226 ? 0.4796 0.5347 0.5375 -0.0016 -0.0158 -0.0216 202 LEU B CD2 
3889 N  N   . MET B 227 ? 0.3720 0.4272 0.4564 -0.0198 -0.0244 -0.0363 203 MET B N   
3890 C  CA  . MET B 227 ? 0.3905 0.4462 0.4877 -0.0253 -0.0259 -0.0389 203 MET B CA  
3891 C  C   . MET B 227 ? 0.4109 0.4681 0.5180 -0.0260 -0.0208 -0.0324 203 MET B C   
3892 O  O   . MET B 227 ? 0.4012 0.4676 0.5140 -0.0241 -0.0202 -0.0286 203 MET B O   
3893 C  CB  . MET B 227 ? 0.3890 0.4555 0.4941 -0.0281 -0.0330 -0.0444 203 MET B CB  
3894 C  CG  . MET B 227 ? 0.4730 0.5378 0.5904 -0.0345 -0.0356 -0.0492 203 MET B CG  
3895 S  SD  . MET B 227 ? 0.6126 0.6919 0.7421 -0.0384 -0.0442 -0.0553 203 MET B SD  
3896 C  CE  . MET B 227 ? 0.5421 0.6146 0.6861 -0.0460 -0.0456 -0.0605 203 MET B CE  
3897 N  N   . GLY B 228 ? 0.3857 0.4343 0.4949 -0.0283 -0.0169 -0.0307 204 GLY B N   
3898 C  CA  . GLY B 228 ? 0.3595 0.4082 0.4747 -0.0281 -0.0109 -0.0239 204 GLY B CA  
3899 C  C   . GLY B 228 ? 0.3776 0.4171 0.4801 -0.0245 -0.0051 -0.0201 204 GLY B C   
3900 O  O   . GLY B 228 ? 0.3566 0.3946 0.4621 -0.0245 0.0003  -0.0149 204 GLY B O   
3901 N  N   . GLY B 229 ? 0.3253 0.3594 0.4139 -0.0215 -0.0061 -0.0226 205 GLY B N   
3902 C  CA  . GLY B 229 ? 0.3420 0.3672 0.4185 -0.0187 -0.0016 -0.0200 205 GLY B CA  
3903 C  C   . GLY B 229 ? 0.3735 0.3897 0.4427 -0.0201 -0.0034 -0.0236 205 GLY B C   
3904 O  O   . GLY B 229 ? 0.3166 0.3327 0.3909 -0.0232 -0.0073 -0.0280 205 GLY B O   
3905 N  N   . ILE B 230 ? 0.3192 0.3280 0.3768 -0.0177 -0.0005 -0.0220 206 ILE B N   
3906 C  CA  . ILE B 230 ? 0.3328 0.3339 0.3832 -0.0184 -0.0020 -0.0248 206 ILE B CA  
3907 C  C   . ILE B 230 ? 0.3618 0.3649 0.4074 -0.0172 -0.0064 -0.0296 206 ILE B C   
3908 O  O   . ILE B 230 ? 0.3503 0.3592 0.3943 -0.0148 -0.0076 -0.0295 206 ILE B O   
3909 C  CB  . ILE B 230 ? 0.3620 0.3563 0.4019 -0.0163 0.0019  -0.0217 206 ILE B CB  
3910 C  CG1 . ILE B 230 ? 0.3675 0.3545 0.4030 -0.0176 0.0009  -0.0232 206 ILE B CG1 
3911 C  CG2 . ILE B 230 ? 0.2926 0.2870 0.3232 -0.0125 0.0022  -0.0216 206 ILE B CG2 
3912 C  CD1 . ILE B 230 ? 0.3530 0.3342 0.3790 -0.0161 0.0040  -0.0201 206 ILE B CD1 
3913 N  N   . GLY B 231 ? 0.3463 0.3451 0.3896 -0.0185 -0.0087 -0.0335 207 GLY B N   
3914 C  CA  . GLY B 231 ? 0.3344 0.3353 0.3722 -0.0172 -0.0125 -0.0380 207 GLY B CA  
3915 C  C   . GLY B 231 ? 0.3676 0.3655 0.3935 -0.0138 -0.0110 -0.0360 207 GLY B C   
3916 O  O   . GLY B 231 ? 0.3411 0.3357 0.3631 -0.0123 -0.0075 -0.0318 207 GLY B O   
3917 N  N   . ALA B 232 ? 0.3618 0.3610 0.3822 -0.0126 -0.0137 -0.0394 208 ALA B N   
3918 C  CA  . ALA B 232 ? 0.3857 0.3834 0.3962 -0.0095 -0.0127 -0.0374 208 ALA B CA  
3919 C  C   . ALA B 232 ? 0.3885 0.3806 0.3934 -0.0096 -0.0127 -0.0392 208 ALA B C   
3920 O  O   . ALA B 232 ? 0.3639 0.3561 0.3616 -0.0075 -0.0126 -0.0384 208 ALA B O   
3921 C  CB  . ALA B 232 ? 0.3340 0.3398 0.3425 -0.0072 -0.0154 -0.0381 208 ALA B CB  
3922 N  N   . HIS B 233 ? 0.3909 0.3786 0.3999 -0.0119 -0.0124 -0.0410 209 HIS B N   
3923 C  CA  . HIS B 233 ? 0.3711 0.3538 0.3760 -0.0117 -0.0119 -0.0420 209 HIS B CA  
3924 C  C   . HIS B 233 ? 0.3855 0.3634 0.3842 -0.0107 -0.0091 -0.0371 209 HIS B C   
3925 O  O   . HIS B 233 ? 0.3707 0.3469 0.3699 -0.0111 -0.0071 -0.0337 209 HIS B O   
3926 C  CB  . HIS B 233 ? 0.3982 0.3767 0.4103 -0.0142 -0.0119 -0.0441 209 HIS B CB  
3927 C  CG  . HIS B 233 ? 0.4426 0.4171 0.4523 -0.0135 -0.0118 -0.0459 209 HIS B CG  
3928 N  ND1 . HIS B 233 ? 0.4365 0.4060 0.4432 -0.0132 -0.0096 -0.0419 209 HIS B ND1 
3929 C  CD2 . HIS B 233 ? 0.4590 0.4342 0.4689 -0.0129 -0.0135 -0.0514 209 HIS B CD2 
3930 C  CE1 . HIS B 233 ? 0.4650 0.4326 0.4712 -0.0123 -0.0098 -0.0443 209 HIS B CE1 
3931 N  NE2 . HIS B 233 ? 0.4543 0.4249 0.4622 -0.0120 -0.0119 -0.0502 209 HIS B NE2 
3932 N  N   . PRO B 234 ? 0.4062 0.3823 0.3992 -0.0095 -0.0090 -0.0370 210 PRO B N   
3933 C  CA  . PRO B 234 ? 0.3941 0.3657 0.3819 -0.0093 -0.0070 -0.0329 210 PRO B CA  
3934 C  C   . PRO B 234 ? 0.3711 0.3381 0.3611 -0.0110 -0.0053 -0.0305 210 PRO B C   
3935 O  O   . PRO B 234 ? 0.3375 0.3020 0.3237 -0.0110 -0.0037 -0.0275 210 PRO B O   
3936 C  CB  . PRO B 234 ? 0.4018 0.3732 0.3858 -0.0083 -0.0074 -0.0336 210 PRO B CB  
3937 C  CG  . PRO B 234 ? 0.4230 0.4002 0.4071 -0.0068 -0.0093 -0.0373 210 PRO B CG  
3938 C  CD  . PRO B 234 ? 0.4054 0.3844 0.3959 -0.0082 -0.0107 -0.0405 210 PRO B CD  
3939 N  N   . ASP B 235 ? 0.3716 0.3373 0.3676 -0.0124 -0.0056 -0.0318 211 ASP B N   
3940 C  CA  . ASP B 235 ? 0.4088 0.3711 0.4074 -0.0139 -0.0038 -0.0285 211 ASP B CA  
3941 C  C   . ASP B 235 ? 0.4155 0.3794 0.4159 -0.0144 -0.0023 -0.0264 211 ASP B C   
3942 O  O   . ASP B 235 ? 0.4010 0.3629 0.3992 -0.0147 -0.0001 -0.0228 211 ASP B O   
3943 C  CB  . ASP B 235 ? 0.4633 0.4238 0.4698 -0.0152 -0.0043 -0.0298 211 ASP B CB  
3944 C  CG  . ASP B 235 ? 0.5518 0.5096 0.5569 -0.0145 -0.0046 -0.0298 211 ASP B CG  
3945 O  OD1 . ASP B 235 ? 0.5555 0.5124 0.5544 -0.0138 -0.0041 -0.0270 211 ASP B OD1 
3946 O  OD2 . ASP B 235 ? 0.6390 0.5956 0.6498 -0.0145 -0.0054 -0.0329 211 ASP B OD2 
3947 N  N   . ASP B 236 ? 0.3450 0.3132 0.3494 -0.0143 -0.0032 -0.0286 212 ASP B N   
3948 C  CA  . ASP B 236 ? 0.3869 0.3577 0.3936 -0.0143 -0.0014 -0.0264 212 ASP B CA  
3949 C  C   . ASP B 236 ? 0.3696 0.3391 0.3682 -0.0122 0.0004  -0.0242 212 ASP B C   
3950 O  O   . ASP B 236 ? 0.3157 0.2843 0.3131 -0.0121 0.0032  -0.0215 212 ASP B O   
3951 C  CB  . ASP B 236 ? 0.3003 0.2771 0.3132 -0.0144 -0.0034 -0.0291 212 ASP B CB  
3952 C  CG  . ASP B 236 ? 0.3757 0.3534 0.3981 -0.0170 -0.0052 -0.0319 212 ASP B CG  
3953 O  OD1 . ASP B 236 ? 0.3436 0.3176 0.3703 -0.0187 -0.0036 -0.0298 212 ASP B OD1 
3954 O  OD2 . ASP B 236 ? 0.3723 0.3543 0.3979 -0.0172 -0.0083 -0.0361 212 ASP B OD2 
3955 N  N   . VAL B 237 ? 0.3597 0.3291 0.3527 -0.0107 -0.0009 -0.0255 213 VAL B N   
3956 C  CA  . VAL B 237 ? 0.3479 0.3149 0.3342 -0.0090 0.0007  -0.0238 213 VAL B CA  
3957 C  C   . VAL B 237 ? 0.3683 0.3302 0.3496 -0.0099 0.0023  -0.0221 213 VAL B C   
3958 O  O   . VAL B 237 ? 0.3813 0.3415 0.3594 -0.0092 0.0046  -0.0207 213 VAL B O   
3959 C  CB  . VAL B 237 ? 0.3487 0.3164 0.3311 -0.0075 -0.0010 -0.0248 213 VAL B CB  
3960 C  CG1 . VAL B 237 ? 0.3518 0.3156 0.3284 -0.0062 0.0006  -0.0230 213 VAL B CG1 
3961 C  CG2 . VAL B 237 ? 0.3486 0.3227 0.3349 -0.0063 -0.0028 -0.0262 213 VAL B CG2 
3962 N  N   . LEU B 238 ? 0.3825 0.3424 0.3629 -0.0112 0.0009  -0.0222 214 LEU B N   
3963 C  CA  . LEU B 238 ? 0.4220 0.3782 0.3974 -0.0121 0.0017  -0.0203 214 LEU B CA  
3964 C  C   . LEU B 238 ? 0.4227 0.3792 0.3999 -0.0128 0.0039  -0.0180 214 LEU B C   
3965 O  O   . LEU B 238 ? 0.4235 0.3781 0.3948 -0.0127 0.0054  -0.0165 214 LEU B O   
3966 C  CB  . LEU B 238 ? 0.4167 0.3721 0.3929 -0.0130 -0.0002 -0.0203 214 LEU B CB  
3967 C  CG  . LEU B 238 ? 0.5393 0.4930 0.5101 -0.0130 -0.0013 -0.0203 214 LEU B CG  
3968 C  CD1 . LEU B 238 ? 0.4818 0.4326 0.4463 -0.0137 -0.0006 -0.0190 214 LEU B CD1 
3969 C  CD2 . LEU B 238 ? 0.4705 0.4255 0.4405 -0.0116 -0.0018 -0.0219 214 LEU B CD2 
3970 N  N   . HIS B 239 ? 0.3850 0.3440 0.3701 -0.0135 0.0042  -0.0176 215 HIS B N   
3971 C  CA  . HIS B 239 ? 0.3878 0.3478 0.3756 -0.0142 0.0067  -0.0143 215 HIS B CA  
3972 C  C   . HIS B 239 ? 0.3836 0.3449 0.3679 -0.0126 0.0096  -0.0136 215 HIS B C   
3973 O  O   . HIS B 239 ? 0.4299 0.3906 0.4095 -0.0124 0.0120  -0.0112 215 HIS B O   
3974 C  CB  . HIS B 239 ? 0.3729 0.3353 0.3717 -0.0155 0.0064  -0.0142 215 HIS B CB  
3975 C  CG  . HIS B 239 ? 0.4395 0.4039 0.4430 -0.0163 0.0094  -0.0102 215 HIS B CG  
3976 N  ND1 . HIS B 239 ? 0.4188 0.3820 0.4203 -0.0168 0.0112  -0.0057 215 HIS B ND1 
3977 C  CD2 . HIS B 239 ? 0.3963 0.3648 0.4068 -0.0165 0.0112  -0.0093 215 HIS B CD2 
3978 C  CE1 . HIS B 239 ? 0.4180 0.3842 0.4247 -0.0172 0.0142  -0.0021 215 HIS B CE1 
3979 N  NE2 . HIS B 239 ? 0.4391 0.4086 0.4518 -0.0172 0.0143  -0.0042 215 HIS B NE2 
3980 N  N   . MET B 240 ? 0.3781 0.3415 0.3644 -0.0113 0.0095  -0.0156 216 MET B N   
3981 C  CA  . MET B 240 ? 0.3831 0.3476 0.3669 -0.0092 0.0126  -0.0151 216 MET B CA  
3982 C  C   . MET B 240 ? 0.3558 0.3154 0.3289 -0.0081 0.0134  -0.0160 216 MET B C   
3983 O  O   . MET B 240 ? 0.3834 0.3425 0.3521 -0.0068 0.0165  -0.0152 216 MET B O   
3984 C  CB  . MET B 240 ? 0.3234 0.2915 0.3120 -0.0077 0.0119  -0.0166 216 MET B CB  
3985 C  CG  . MET B 240 ? 0.3295 0.3033 0.3291 -0.0090 0.0108  -0.0163 216 MET B CG  
3986 S  SD  . MET B 240 ? 0.3904 0.3685 0.3968 -0.0094 0.0150  -0.0124 216 MET B SD  
3987 C  CE  . MET B 240 ? 0.3362 0.3177 0.3419 -0.0056 0.0178  -0.0123 216 MET B CE  
3988 N  N   . LYS B 241 ? 0.3577 0.3139 0.3269 -0.0085 0.0106  -0.0178 217 LYS B N   
3989 C  CA  . LYS B 241 ? 0.4030 0.3543 0.3634 -0.0082 0.0108  -0.0191 217 LYS B CA  
3990 C  C   . LYS B 241 ? 0.3835 0.3338 0.3386 -0.0095 0.0114  -0.0177 217 LYS B C   
3991 O  O   . LYS B 241 ? 0.4101 0.3586 0.3584 -0.0086 0.0135  -0.0185 217 LYS B O   
3992 C  CB  . LYS B 241 ? 0.3914 0.3403 0.3505 -0.0089 0.0077  -0.0205 217 LYS B CB  
3993 C  CG  . LYS B 241 ? 0.4565 0.4001 0.4080 -0.0094 0.0072  -0.0218 217 LYS B CG  
3994 C  CD  . LYS B 241 ? 0.4716 0.4121 0.4197 -0.0073 0.0099  -0.0235 217 LYS B CD  
3995 C  CE  . LYS B 241 ? 0.4862 0.4205 0.4292 -0.0080 0.0088  -0.0256 217 LYS B CE  
3996 N  NZ  . LYS B 241 ? 0.4703 0.4026 0.4070 -0.0105 0.0072  -0.0266 217 LYS B NZ  
3997 N  N   . ARG B 242 ? 0.3995 0.3513 0.3575 -0.0114 0.0096  -0.0157 218 ARG B N   
3998 C  CA  . ARG B 242 ? 0.4278 0.3798 0.3813 -0.0124 0.0099  -0.0133 218 ARG B CA  
3999 C  C   . ARG B 242 ? 0.3908 0.3453 0.3428 -0.0112 0.0139  -0.0112 218 ARG B C   
4000 O  O   . ARG B 242 ? 0.4443 0.3984 0.3879 -0.0109 0.0151  -0.0110 218 ARG B O   
4001 C  CB  . ARG B 242 ? 0.4433 0.3969 0.4029 -0.0139 0.0081  -0.0105 218 ARG B CB  
4002 C  CG  . ARG B 242 ? 0.5465 0.4983 0.5048 -0.0150 0.0046  -0.0115 218 ARG B CG  
4003 C  CD  . ARG B 242 ? 0.6045 0.5577 0.5681 -0.0159 0.0035  -0.0081 218 ARG B CD  
4004 N  NE  . ARG B 242 ? 0.6366 0.5910 0.6095 -0.0159 0.0047  -0.0073 218 ARG B NE  
4005 C  CZ  . ARG B 242 ? 0.6164 0.5706 0.5962 -0.0160 0.0032  -0.0094 218 ARG B CZ  
4006 N  NH1 . ARG B 242 ? 0.5731 0.5263 0.5513 -0.0158 0.0010  -0.0116 218 ARG B NH1 
4007 N  NH2 . ARG B 242 ? 0.5171 0.4722 0.5054 -0.0164 0.0040  -0.0093 218 ARG B NH2 
4008 N  N   . THR B 243 ? 0.4092 0.3670 0.3694 -0.0107 0.0159  -0.0097 219 THR B N   
4009 C  CA  . THR B 243 ? 0.4054 0.3667 0.3658 -0.0095 0.0202  -0.0069 219 THR B CA  
4010 C  C   . THR B 243 ? 0.4227 0.3827 0.3751 -0.0070 0.0229  -0.0097 219 THR B C   
4011 O  O   . THR B 243 ? 0.4101 0.3713 0.3555 -0.0060 0.0258  -0.0085 219 THR B O   
4012 C  CB  . THR B 243 ? 0.4373 0.4028 0.4098 -0.0098 0.0214  -0.0051 219 THR B CB  
4013 O  OG1 . THR B 243 ? 0.4076 0.3732 0.3878 -0.0121 0.0189  -0.0033 219 THR B OG1 
4014 C  CG2 . THR B 243 ? 0.4128 0.3829 0.3869 -0.0086 0.0263  -0.0012 219 THR B CG2 
4015 N  N   . ALA B 244 ? 0.3828 0.3403 0.3359 -0.0057 0.0222  -0.0133 220 ALA B N   
4016 C  CA  . ALA B 244 ? 0.3950 0.3498 0.3414 -0.0031 0.0249  -0.0163 220 ALA B CA  
4017 C  C   . ALA B 244 ? 0.4205 0.3707 0.3552 -0.0037 0.0239  -0.0189 220 ALA B C   
4018 O  O   . ALA B 244 ? 0.4205 0.3701 0.3477 -0.0018 0.0270  -0.0206 220 ALA B O   
4019 C  CB  . ALA B 244 ? 0.4039 0.3566 0.3543 -0.0016 0.0239  -0.0188 220 ALA B CB  
4020 N  N   . ASP B 245 ? 0.4299 0.3774 0.3632 -0.0062 0.0195  -0.0197 221 ASP B N   
4021 C  CA  . ASP B 245 ? 0.4159 0.3600 0.3391 -0.0075 0.0176  -0.0220 221 ASP B CA  
4022 C  C   . ASP B 245 ? 0.4302 0.3783 0.3472 -0.0074 0.0194  -0.0196 221 ASP B C   
4023 O  O   . ASP B 245 ? 0.4360 0.3825 0.3428 -0.0067 0.0204  -0.0226 221 ASP B O   
4024 C  CB  . ASP B 245 ? 0.4438 0.3863 0.3686 -0.0103 0.0127  -0.0218 221 ASP B CB  
4025 C  CG  . ASP B 245 ? 0.4802 0.4185 0.4083 -0.0103 0.0111  -0.0245 221 ASP B CG  
4026 O  OD1 . ASP B 245 ? 0.5117 0.4468 0.4389 -0.0082 0.0132  -0.0271 221 ASP B OD1 
4027 O  OD2 . ASP B 245 ? 0.4725 0.4110 0.4043 -0.0121 0.0078  -0.0235 221 ASP B OD2 
4028 N  N   . ARG B 246 ? 0.4016 0.3548 0.3244 -0.0081 0.0199  -0.0142 222 ARG B N   
4029 C  CA  . ARG B 246 ? 0.4552 0.4130 0.3727 -0.0081 0.0215  -0.0104 222 ARG B CA  
4030 C  C   . ARG B 246 ? 0.4208 0.3815 0.3345 -0.0051 0.0272  -0.0102 222 ARG B C   
4031 O  O   . ARG B 246 ? 0.4635 0.4267 0.3673 -0.0043 0.0288  -0.0097 222 ARG B O   
4032 C  CB  . ARG B 246 ? 0.4451 0.4068 0.3717 -0.0095 0.0208  -0.0040 222 ARG B CB  
4033 C  CG  . ARG B 246 ? 0.4935 0.4607 0.4164 -0.0093 0.0229  0.0018  222 ARG B CG  
4034 C  CD  . ARG B 246 ? 0.4978 0.4673 0.4306 -0.0109 0.0216  0.0081  222 ARG B CD  
4035 N  NE  . ARG B 246 ? 0.5031 0.4721 0.4491 -0.0113 0.0225  0.0086  222 ARG B NE  
4036 C  CZ  . ARG B 246 ? 0.5294 0.5019 0.4822 -0.0106 0.0266  0.0120  222 ARG B CZ  
4037 N  NH1 . ARG B 246 ? 0.5353 0.5125 0.4830 -0.0091 0.0309  0.0156  222 ARG B NH1 
4038 N  NH2 . ARG B 246 ? 0.4917 0.4639 0.4571 -0.0116 0.0263  0.0118  222 ARG B NH2 
4039 N  N   . LEU B 247 ? 0.4027 0.3640 0.3241 -0.0033 0.0302  -0.0104 223 LEU B N   
4040 C  CA  . LEU B 247 ? 0.4507 0.4159 0.3702 -0.0002 0.0362  -0.0094 223 LEU B CA  
4041 C  C   . LEU B 247 ? 0.4640 0.4248 0.3740 0.0026  0.0382  -0.0159 223 LEU B C   
4042 O  O   . LEU B 247 ? 0.4615 0.4252 0.3641 0.0052  0.0428  -0.0163 223 LEU B O   
4043 C  CB  . LEU B 247 ? 0.4539 0.4229 0.3871 0.0005  0.0386  -0.0064 223 LEU B CB  
4044 C  CG  . LEU B 247 ? 0.4492 0.4226 0.3934 -0.0020 0.0376  -0.0002 223 LEU B CG  
4045 C  CD1 . LEU B 247 ? 0.4027 0.3805 0.3599 -0.0014 0.0402  0.0018  223 LEU B CD1 
4046 C  CD2 . LEU B 247 ? 0.4763 0.4542 0.4163 -0.0024 0.0398  0.0054  223 LEU B CD2 
4047 N  N   . PHE B 248 ? 0.4520 0.4059 0.3622 0.0022  0.0353  -0.0210 224 PHE B N   
4048 C  CA  . PHE B 248 ? 0.4875 0.4360 0.3913 0.0050  0.0375  -0.0272 224 PHE B CA  
4049 C  C   . PHE B 248 ? 0.5052 0.4461 0.4005 0.0030  0.0333  -0.0330 224 PHE B C   
4050 O  O   . PHE B 248 ? 0.4997 0.4348 0.3892 0.0050  0.0350  -0.0388 224 PHE B O   
4051 C  CB  . PHE B 248 ? 0.4883 0.4353 0.4021 0.0072  0.0390  -0.0277 224 PHE B CB  
4052 C  CG  . PHE B 248 ? 0.4586 0.4136 0.3828 0.0086  0.0424  -0.0222 224 PHE B CG  
4053 C  CD1 . PHE B 248 ? 0.4861 0.4459 0.4089 0.0120  0.0485  -0.0210 224 PHE B CD1 
4054 C  CD2 . PHE B 248 ? 0.4220 0.3800 0.3575 0.0064  0.0394  -0.0186 224 PHE B CD2 
4055 C  CE1 . PHE B 248 ? 0.4552 0.4230 0.3889 0.0128  0.0515  -0.0156 224 PHE B CE1 
4056 C  CE2 . PHE B 248 ? 0.4221 0.3876 0.3681 0.0070  0.0420  -0.0140 224 PHE B CE2 
4057 C  CZ  . PHE B 248 ? 0.4332 0.4037 0.3788 0.0100  0.0480  -0.0122 224 PHE B CZ  
4058 N  N   . GLY B 249 ? 0.4771 0.4178 0.3724 -0.0008 0.0281  -0.0315 225 GLY B N   
4059 C  CA  . GLY B 249 ? 0.5603 0.4953 0.4480 -0.0032 0.0239  -0.0364 225 GLY B CA  
4060 C  C   . GLY B 249 ? 0.5783 0.5051 0.4688 -0.0027 0.0232  -0.0412 225 GLY B C   
4061 O  O   . GLY B 249 ? 0.5826 0.5085 0.4828 -0.0028 0.0222  -0.0391 225 GLY B O   
4062 N  N   . GLN B 250 ? 0.6183 0.5390 0.5003 -0.0021 0.0238  -0.0477 226 GLN B N   
4063 C  CA  . GLN B 250 ? 0.6261 0.5377 0.5105 -0.0017 0.0233  -0.0524 226 GLN B CA  
4064 C  C   . GLN B 250 ? 0.5885 0.4973 0.4751 0.0033  0.0291  -0.0544 226 GLN B C   
4065 O  O   . GLN B 250 ? 0.6107 0.5115 0.5001 0.0043  0.0294  -0.0577 226 GLN B O   
4066 C  CB  . GLN B 250 ? 0.6802 0.5855 0.5553 -0.0044 0.0201  -0.0592 226 GLN B CB  
4067 C  CG  . GLN B 250 ? 0.7447 0.6532 0.6183 -0.0094 0.0140  -0.0573 226 GLN B CG  
4068 C  CD  . GLN B 250 ? 0.8533 0.7601 0.7371 -0.0119 0.0105  -0.0541 226 GLN B CD  
4069 O  OE1 . GLN B 250 ? 0.9845 0.8841 0.8701 -0.0138 0.0084  -0.0576 226 GLN B OE1 
4070 N  NE2 . GLN B 250 ? 0.8366 0.7499 0.7274 -0.0121 0.0100  -0.0476 226 GLN B NE2 
4071 N  N   . ASP B 251 ? 0.5447 0.4600 0.4308 0.0065  0.0338  -0.0518 227 ASP B N   
4072 C  CA  . ASP B 251 ? 0.5494 0.4635 0.4373 0.0118  0.0398  -0.0534 227 ASP B CA  
4073 C  C   . ASP B 251 ? 0.5599 0.4774 0.4613 0.0138  0.0412  -0.0481 227 ASP B C   
4074 O  O   . ASP B 251 ? 0.5444 0.4660 0.4495 0.0179  0.0463  -0.0465 227 ASP B O   
4075 C  CB  . ASP B 251 ? 0.5659 0.4865 0.4462 0.0145  0.0447  -0.0533 227 ASP B CB  
4076 C  CG  . ASP B 251 ? 0.6090 0.5258 0.4857 0.0199  0.0509  -0.0584 227 ASP B CG  
4077 O  OD1 . ASP B 251 ? 0.6134 0.5207 0.4916 0.0211  0.0508  -0.0634 227 ASP B OD1 
4078 O  OD2 . ASP B 251 ? 0.6410 0.5644 0.5137 0.0231  0.0562  -0.0573 227 ASP B OD2 
4079 N  N   . TYR B 252 ? 0.5006 0.4174 0.4093 0.0110  0.0367  -0.0453 228 TYR B N   
4080 C  CA  . TYR B 252 ? 0.5203 0.4411 0.4409 0.0127  0.0373  -0.0407 228 TYR B CA  
4081 C  C   . TYR B 252 ? 0.5026 0.4184 0.4280 0.0109  0.0331  -0.0405 228 TYR B C   
4082 O  O   . TYR B 252 ? 0.5103 0.4217 0.4317 0.0073  0.0292  -0.0423 228 TYR B O   
4083 C  CB  . TYR B 252 ? 0.4668 0.3977 0.3929 0.0113  0.0367  -0.0350 228 TYR B CB  
4084 C  CG  . TYR B 252 ? 0.4886 0.4210 0.4178 0.0069  0.0312  -0.0325 228 TYR B CG  
4085 C  CD1 . TYR B 252 ? 0.4912 0.4226 0.4135 0.0033  0.0281  -0.0332 228 TYR B CD1 
4086 C  CD2 . TYR B 252 ? 0.4419 0.3777 0.3808 0.0066  0.0291  -0.0293 228 TYR B CD2 
4087 C  CE1 . TYR B 252 ? 0.4597 0.3927 0.3855 -0.0001 0.0236  -0.0308 228 TYR B CE1 
4088 C  CE2 . TYR B 252 ? 0.4205 0.3577 0.3617 0.0031  0.0246  -0.0275 228 TYR B CE2 
4089 C  CZ  . TYR B 252 ? 0.4632 0.3988 0.3983 -0.0001 0.0221  -0.0282 228 TYR B CZ  
4090 O  OH  . TYR B 252 ? 0.4903 0.4276 0.4285 -0.0030 0.0180  -0.0264 228 TYR B OH  
4091 N  N   . ARG B 253 ? 0.4742 0.3916 0.4087 0.0137  0.0342  -0.0377 229 ARG B N   
4092 C  CA  . ARG B 253 ? 0.4567 0.3719 0.3970 0.0127  0.0308  -0.0358 229 ARG B CA  
4093 C  C   . ARG B 253 ? 0.4472 0.3719 0.3955 0.0121  0.0289  -0.0307 229 ARG B C   
4094 O  O   . ARG B 253 ? 0.4594 0.3905 0.4130 0.0148  0.0314  -0.0284 229 ARG B O   
4095 C  CB  . ARG B 253 ? 0.4624 0.3713 0.4063 0.0167  0.0334  -0.0367 229 ARG B CB  
4096 C  CG  . ARG B 253 ? 0.5232 0.4221 0.4600 0.0178  0.0360  -0.0428 229 ARG B CG  
4097 C  CD  . ARG B 253 ? 0.5084 0.3997 0.4396 0.0132  0.0320  -0.0462 229 ARG B CD  
4098 N  NE  . ARG B 253 ? 0.5896 0.4706 0.5147 0.0142  0.0342  -0.0529 229 ARG B NE  
4099 C  CZ  . ARG B 253 ? 0.6541 0.5337 0.5692 0.0134  0.0351  -0.0583 229 ARG B CZ  
4100 N  NH1 . ARG B 253 ? 0.5877 0.4755 0.4977 0.0114  0.0340  -0.0569 229 ARG B NH1 
4101 N  NH2 . ARG B 253 ? 0.6960 0.5657 0.6059 0.0148  0.0372  -0.0653 229 ARG B NH2 
4102 N  N   . TRP B 254 ? 0.4183 0.3440 0.3677 0.0088  0.0245  -0.0292 230 TRP B N   
4103 C  CA  . TRP B 254 ? 0.4050 0.3391 0.3605 0.0076  0.0221  -0.0257 230 TRP B CA  
4104 C  C   . TRP B 254 ? 0.4338 0.3701 0.3959 0.0096  0.0209  -0.0231 230 TRP B C   
4105 O  O   . TRP B 254 ? 0.4254 0.3568 0.3867 0.0093  0.0195  -0.0230 230 TRP B O   
4106 C  CB  . TRP B 254 ? 0.4213 0.3559 0.3739 0.0033  0.0184  -0.0257 230 TRP B CB  
4107 C  CG  . TRP B 254 ? 0.3964 0.3385 0.3549 0.0020  0.0161  -0.0233 230 TRP B CG  
4108 C  CD1 . TRP B 254 ? 0.3944 0.3434 0.3588 0.0029  0.0172  -0.0216 230 TRP B CD1 
4109 C  CD2 . TRP B 254 ? 0.3829 0.3264 0.3424 -0.0005 0.0124  -0.0226 230 TRP B CD2 
4110 N  NE1 . TRP B 254 ? 0.3789 0.3326 0.3477 0.0008  0.0141  -0.0207 230 TRP B NE1 
4111 C  CE2 . TRP B 254 ? 0.3565 0.3070 0.3219 -0.0009 0.0113  -0.0213 230 TRP B CE2 
4112 C  CE3 . TRP B 254 ? 0.3976 0.3374 0.3541 -0.0024 0.0099  -0.0230 230 TRP B CE3 
4113 C  CZ2 . TRP B 254 ? 0.3843 0.3376 0.3519 -0.0028 0.0081  -0.0212 230 TRP B CZ2 
4114 C  CZ3 . TRP B 254 ? 0.3560 0.2994 0.3148 -0.0040 0.0071  -0.0221 230 TRP B CZ3 
4115 C  CH2 . TRP B 254 ? 0.3902 0.3399 0.3540 -0.0040 0.0063  -0.0215 230 TRP B CH2 
4116 N  N   . SER B 255 ? 0.4207 0.3651 0.3898 0.0114  0.0213  -0.0207 231 SER B N   
4117 C  CA  . SER B 255 ? 0.4019 0.3512 0.3771 0.0130  0.0193  -0.0178 231 SER B CA  
4118 C  C   . SER B 255 ? 0.3862 0.3447 0.3660 0.0111  0.0165  -0.0167 231 SER B C   
4119 O  O   . SER B 255 ? 0.3649 0.3267 0.3462 0.0098  0.0174  -0.0173 231 SER B O   
4120 C  CB  . SER B 255 ? 0.3910 0.3415 0.3713 0.0179  0.0223  -0.0159 231 SER B CB  
4121 O  OG  . SER B 255 ? 0.3744 0.3299 0.3598 0.0196  0.0200  -0.0125 231 SER B OG  
4122 N  N   . VAL B 256 ? 0.3796 0.3423 0.3618 0.0109  0.0131  -0.0153 232 VAL B N   
4123 C  CA  . VAL B 256 ? 0.3606 0.3314 0.3468 0.0089  0.0099  -0.0155 232 VAL B CA  
4124 C  C   . VAL B 256 ? 0.3726 0.3520 0.3649 0.0116  0.0084  -0.0132 232 VAL B C   
4125 O  O   . VAL B 256 ? 0.3494 0.3281 0.3418 0.0147  0.0089  -0.0107 232 VAL B O   
4126 C  CB  . VAL B 256 ? 0.3719 0.3412 0.3541 0.0060  0.0068  -0.0168 232 VAL B CB  
4127 C  CG1 . VAL B 256 ? 0.3424 0.3047 0.3193 0.0033  0.0078  -0.0185 232 VAL B CG1 
4128 C  CG2 . VAL B 256 ? 0.3386 0.3070 0.3188 0.0076  0.0056  -0.0149 232 VAL B CG2 
4129 N  N   . LEU B 257 ? 0.3473 0.3349 0.3453 0.0102  0.0063  -0.0139 233 LEU B N   
4130 C  CA  . LEU B 257 ? 0.3637 0.3614 0.3676 0.0119  0.0035  -0.0124 233 LEU B CA  
4131 C  C   . LEU B 257 ? 0.3709 0.3737 0.3757 0.0085  -0.0008 -0.0154 233 LEU B C   
4132 O  O   . LEU B 257 ? 0.3641 0.3681 0.3727 0.0056  -0.0011 -0.0175 233 LEU B O   
4133 C  CB  . LEU B 257 ? 0.3614 0.3651 0.3734 0.0137  0.0054  -0.0107 233 LEU B CB  
4134 C  CG  . LEU B 257 ? 0.3895 0.4050 0.4089 0.0160  0.0027  -0.0084 233 LEU B CG  
4135 C  CD1 . LEU B 257 ? 0.3799 0.4006 0.4080 0.0177  0.0055  -0.0065 233 LEU B CD1 
4136 C  CD2 . LEU B 257 ? 0.3698 0.3932 0.3912 0.0129  -0.0028 -0.0111 233 LEU B CD2 
4137 N  N   . GLY B 258 ? 0.3649 0.3704 0.3663 0.0091  -0.0038 -0.0155 234 GLY B N   
4138 C  CA  . GLY B 258 ? 0.3644 0.3752 0.3662 0.0066  -0.0078 -0.0191 234 GLY B CA  
4139 C  C   . GLY B 258 ? 0.3908 0.4135 0.3976 0.0079  -0.0114 -0.0189 234 GLY B C   
4140 O  O   . GLY B 258 ? 0.3839 0.4112 0.3886 0.0111  -0.0125 -0.0159 234 GLY B O   
4141 N  N   . ALA B 259 ? 0.3890 0.4172 0.4029 0.0054  -0.0135 -0.0218 235 ALA B N   
4142 C  CA  . ALA B 259 ? 0.4218 0.4624 0.4416 0.0061  -0.0176 -0.0220 235 ALA B CA  
4143 C  C   . ALA B 259 ? 0.4155 0.4618 0.4297 0.0064  -0.0220 -0.0247 235 ALA B C   
4144 O  O   . ALA B 259 ? 0.3943 0.4358 0.4031 0.0045  -0.0225 -0.0285 235 ALA B O   
4145 C  CB  . ALA B 259 ? 0.4032 0.4479 0.4328 0.0024  -0.0190 -0.0249 235 ALA B CB  
4146 N  N   . GLY B 260 ? 0.4236 0.4808 0.4391 0.0091  -0.0250 -0.0225 236 GLY B N   
4147 C  CA  . GLY B 260 ? 0.4278 0.4931 0.4380 0.0095  -0.0296 -0.0253 236 GLY B CA  
4148 C  C   . GLY B 260 ? 0.4344 0.4936 0.4342 0.0107  -0.0279 -0.0250 236 GLY B C   
4149 O  O   . GLY B 260 ? 0.3572 0.4102 0.3533 0.0133  -0.0242 -0.0196 236 GLY B O   
4150 N  N   . ARG B 261 ? 0.4564 0.5171 0.4519 0.0088  -0.0306 -0.0310 237 ARG B N   
4151 C  CA  . ARG B 261 ? 0.5405 0.5979 0.5264 0.0102  -0.0294 -0.0310 237 ARG B CA  
4152 C  C   . ARG B 261 ? 0.4549 0.4989 0.4389 0.0091  -0.0247 -0.0296 237 ARG B C   
4153 O  O   . ARG B 261 ? 0.4430 0.4840 0.4203 0.0105  -0.0229 -0.0277 237 ARG B O   
4154 C  CB  . ARG B 261 ? 0.6564 0.7185 0.6389 0.0085  -0.0331 -0.0389 237 ARG B CB  
4155 C  CG  . ARG B 261 ? 0.7135 0.7673 0.7003 0.0043  -0.0327 -0.0453 237 ARG B CG  
4156 C  CD  . ARG B 261 ? 0.8672 0.9264 0.8534 0.0025  -0.0371 -0.0542 237 ARG B CD  
4157 N  NE  . ARG B 261 ? 1.0017 1.0662 0.9777 0.0054  -0.0379 -0.0556 237 ARG B NE  
4158 C  CZ  . ARG B 261 ? 1.0277 1.0972 1.0004 0.0049  -0.0412 -0.0637 237 ARG B CZ  
4159 N  NH1 . ARG B 261 ? 1.0349 1.1038 1.0144 0.0011  -0.0444 -0.0715 237 ARG B NH1 
4160 N  NH2 . ARG B 261 ? 1.0565 1.1316 1.0190 0.0082  -0.0412 -0.0641 237 ARG B NH2 
4161 N  N   . ASN B 262 ? 0.3838 0.4204 0.3736 0.0066  -0.0226 -0.0302 238 ASN B N   
4162 C  CA  . ASN B 262 ? 0.4215 0.4462 0.4092 0.0054  -0.0186 -0.0289 238 ASN B CA  
4163 C  C   . ASN B 262 ? 0.4072 0.4271 0.3936 0.0078  -0.0151 -0.0226 238 ASN B C   
4164 O  O   . ASN B 262 ? 0.3861 0.3967 0.3704 0.0069  -0.0121 -0.0216 238 ASN B O   
4165 C  CB  . ASN B 262 ? 0.3993 0.4188 0.3932 0.0019  -0.0178 -0.0319 238 ASN B CB  
4166 C  CG  . ASN B 262 ? 0.4344 0.4580 0.4321 -0.0007 -0.0213 -0.0383 238 ASN B CG  
4167 O  OD1 . ASN B 262 ? 0.4441 0.4653 0.4383 -0.0016 -0.0220 -0.0422 238 ASN B OD1 
4168 N  ND2 . ASN B 262 ? 0.4343 0.4639 0.4398 -0.0020 -0.0235 -0.0396 238 ASN B ND2 
4169 N  N   . GLN B 263 ? 0.3411 0.3673 0.3291 0.0110  -0.0156 -0.0185 239 GLN B N   
4170 C  CA  . GLN B 263 ? 0.3669 0.3879 0.3558 0.0134  -0.0121 -0.0130 239 GLN B CA  
4171 C  C   . GLN B 263 ? 0.3512 0.3636 0.3342 0.0136  -0.0095 -0.0106 239 GLN B C   
4172 O  O   . GLN B 263 ? 0.3777 0.3804 0.3604 0.0127  -0.0064 -0.0102 239 GLN B O   
4173 C  CB  . GLN B 263 ? 0.3534 0.3836 0.3452 0.0173  -0.0134 -0.0083 239 GLN B CB  
4174 C  CG  . GLN B 263 ? 0.3763 0.4013 0.3700 0.0205  -0.0096 -0.0025 239 GLN B CG  
4175 C  CD  . GLN B 263 ? 0.4092 0.4443 0.4072 0.0248  -0.0111 0.0026  239 GLN B CD  
4176 O  OE1 . GLN B 263 ? 0.4126 0.4545 0.4074 0.0270  -0.0131 0.0058  239 GLN B OE1 
4177 N  NE2 . GLN B 263 ? 0.4084 0.4456 0.4137 0.0262  -0.0100 0.0037  239 GLN B NE2 
4178 N  N   . LEU B 264 ? 0.3557 0.3720 0.3340 0.0148  -0.0107 -0.0092 240 LEU B N   
4179 C  CA  . LEU B 264 ? 0.3777 0.3871 0.3519 0.0151  -0.0082 -0.0059 240 LEU B CA  
4180 C  C   . LEU B 264 ? 0.3767 0.3794 0.3482 0.0116  -0.0075 -0.0098 240 LEU B C   
4181 O  O   . LEU B 264 ? 0.3403 0.3345 0.3106 0.0106  -0.0052 -0.0080 240 LEU B O   
4182 C  CB  . LEU B 264 ? 0.3771 0.3943 0.3480 0.0179  -0.0092 -0.0016 240 LEU B CB  
4183 C  CG  . LEU B 264 ? 0.3846 0.4082 0.3584 0.0219  -0.0095 0.0041  240 LEU B CG  
4184 C  CD1 . LEU B 264 ? 0.4104 0.4431 0.3801 0.0248  -0.0106 0.0089  240 LEU B CD1 
4185 C  CD2 . LEU B 264 ? 0.3580 0.3720 0.3356 0.0231  -0.0059 0.0085  240 LEU B CD2 
4186 N  N   . ASN B 265 ? 0.3793 0.3855 0.3504 0.0098  -0.0097 -0.0150 241 ASN B N   
4187 C  CA  . ASN B 265 ? 0.3877 0.3875 0.3574 0.0069  -0.0089 -0.0183 241 ASN B CA  
4188 C  C   . ASN B 265 ? 0.3766 0.3674 0.3485 0.0049  -0.0068 -0.0183 241 ASN B C   
4189 O  O   . ASN B 265 ? 0.3795 0.3633 0.3493 0.0036  -0.0052 -0.0173 241 ASN B O   
4190 C  CB  . ASN B 265 ? 0.3970 0.4010 0.3676 0.0054  -0.0114 -0.0242 241 ASN B CB  
4191 C  CG  . ASN B 265 ? 0.4417 0.4537 0.4082 0.0072  -0.0131 -0.0255 241 ASN B CG  
4192 O  OD1 . ASN B 265 ? 0.4058 0.4190 0.3683 0.0090  -0.0119 -0.0216 241 ASN B OD1 
4193 N  ND2 . ASN B 265 ? 0.4466 0.4640 0.4142 0.0066  -0.0159 -0.0312 241 ASN B ND2 
4194 N  N   . ILE B 266 ? 0.3254 0.3171 0.3015 0.0047  -0.0069 -0.0193 242 ILE B N   
4195 C  CA  . ILE B 266 ? 0.3736 0.3580 0.3511 0.0032  -0.0046 -0.0195 242 ILE B CA  
4196 C  C   . ILE B 266 ? 0.3336 0.3121 0.3093 0.0048  -0.0020 -0.0160 242 ILE B C   
4197 O  O   . ILE B 266 ? 0.3606 0.3315 0.3343 0.0033  -0.0002 -0.0164 242 ILE B O   
4198 C  CB  . ILE B 266 ? 0.4101 0.3984 0.3934 0.0028  -0.0051 -0.0211 242 ILE B CB  
4199 C  CG1 . ILE B 266 ? 0.3805 0.3712 0.3661 0.0002  -0.0073 -0.0253 242 ILE B CG1 
4200 C  CG2 . ILE B 266 ? 0.3693 0.3518 0.3536 0.0024  -0.0019 -0.0201 242 ILE B CG2 
4201 C  CD1 . ILE B 266 ? 0.4049 0.4002 0.3977 -0.0009 -0.0083 -0.0270 242 ILE B CD1 
4202 N  N   . ALA B 267 ? 0.3474 0.3292 0.3239 0.0078  -0.0019 -0.0126 243 ALA B N   
4203 C  CA  . ALA B 267 ? 0.3371 0.3121 0.3126 0.0093  0.0006  -0.0093 243 ALA B CA  
4204 C  C   . ALA B 267 ? 0.3714 0.3403 0.3430 0.0072  0.0010  -0.0089 243 ALA B C   
4205 O  O   . ALA B 267 ? 0.3813 0.3416 0.3516 0.0062  0.0028  -0.0091 243 ALA B O   
4206 C  CB  . ALA B 267 ? 0.3384 0.3187 0.3163 0.0131  0.0005  -0.0047 243 ALA B CB  
4207 N  N   . ALA B 268 ? 0.3537 0.3271 0.3235 0.0066  -0.0007 -0.0087 244 ALA B N   
4208 C  CA  . ALA B 268 ? 0.3529 0.3220 0.3202 0.0048  -0.0003 -0.0077 244 ALA B CA  
4209 C  C   . ALA B 268 ? 0.3677 0.3309 0.3336 0.0014  -0.0003 -0.0112 244 ALA B C   
4210 O  O   . ALA B 268 ? 0.3373 0.2940 0.3020 -0.0004 0.0005  -0.0105 244 ALA B O   
4211 C  CB  . ALA B 268 ? 0.3319 0.3085 0.2976 0.0054  -0.0017 -0.0067 244 ALA B CB  
4212 N  N   . MET B 269 ? 0.3643 0.3300 0.3308 0.0004  -0.0013 -0.0146 245 MET B N   
4213 C  CA  . MET B 269 ? 0.3661 0.3270 0.3316 -0.0023 -0.0011 -0.0169 245 MET B CA  
4214 C  C   . MET B 269 ? 0.3613 0.3152 0.3255 -0.0028 0.0007  -0.0169 245 MET B C   
4215 O  O   . MET B 269 ? 0.3930 0.3416 0.3547 -0.0049 0.0009  -0.0173 245 MET B O   
4216 C  CB  . MET B 269 ? 0.3674 0.3319 0.3352 -0.0030 -0.0020 -0.0198 245 MET B CB  
4217 C  CG  . MET B 269 ? 0.4018 0.3721 0.3706 -0.0028 -0.0039 -0.0214 245 MET B CG  
4218 S  SD  . MET B 269 ? 0.4844 0.4569 0.4575 -0.0042 -0.0050 -0.0252 245 MET B SD  
4219 C  CE  . MET B 269 ? 0.4194 0.3852 0.3917 -0.0067 -0.0040 -0.0248 245 MET B CE  
4220 N  N   . SER B 270 ? 0.3781 0.3324 0.3441 -0.0006 0.0021  -0.0166 246 SER B N   
4221 C  CA  . SER B 270 ? 0.3922 0.3399 0.3565 -0.0004 0.0044  -0.0173 246 SER B CA  
4222 C  C   . SER B 270 ? 0.3472 0.2882 0.3097 -0.0006 0.0050  -0.0162 246 SER B C   
4223 O  O   . SER B 270 ? 0.3981 0.3328 0.3574 -0.0027 0.0054  -0.0181 246 SER B O   
4224 C  CB  . SER B 270 ? 0.3302 0.2805 0.2978 0.0027  0.0061  -0.0167 246 SER B CB  
4225 O  OG  . SER B 270 ? 0.4274 0.3712 0.3933 0.0036  0.0088  -0.0176 246 SER B OG  
4226 N  N   . ALA B 271 ? 0.3791 0.3216 0.3439 0.0013  0.0050  -0.0129 247 ALA B N   
4227 C  CA  . ALA B 271 ? 0.3952 0.3310 0.3599 0.0008  0.0057  -0.0112 247 ALA B CA  
4228 C  C   . ALA B 271 ? 0.4103 0.3434 0.3728 -0.0031 0.0042  -0.0123 247 ALA B C   
4229 O  O   . ALA B 271 ? 0.4235 0.3490 0.3849 -0.0050 0.0045  -0.0133 247 ALA B O   
4230 C  CB  . ALA B 271 ? 0.3848 0.3248 0.3529 0.0034  0.0057  -0.0062 247 ALA B CB  
4231 N  N   . ALA B 272 ? 0.4089 0.3481 0.3709 -0.0044 0.0024  -0.0123 248 ALA B N   
4232 C  CA  . ALA B 272 ? 0.3875 0.3256 0.3484 -0.0077 0.0009  -0.0127 248 ALA B CA  
4233 C  C   . ALA B 272 ? 0.4188 0.3532 0.3765 -0.0101 0.0003  -0.0162 248 ALA B C   
4234 O  O   . ALA B 272 ? 0.4152 0.3477 0.3719 -0.0131 -0.0011 -0.0166 248 ALA B O   
4235 C  CB  . ALA B 272 ? 0.3817 0.3277 0.3436 -0.0075 -0.0004 -0.0116 248 ALA B CB  
4236 N  N   . MET B 273 ? 0.3969 0.3310 0.3531 -0.0089 0.0014  -0.0184 249 MET B N   
4237 C  CA  . MET B 273 ? 0.3908 0.3227 0.3433 -0.0107 0.0012  -0.0210 249 MET B CA  
4238 C  C   . MET B 273 ? 0.4234 0.3489 0.3726 -0.0102 0.0030  -0.0234 249 MET B C   
4239 O  O   . MET B 273 ? 0.4665 0.3912 0.4118 -0.0108 0.0035  -0.0255 249 MET B O   
4240 C  CB  . MET B 273 ? 0.4077 0.3450 0.3614 -0.0098 0.0014  -0.0213 249 MET B CB  
4241 C  CG  . MET B 273 ? 0.3805 0.3233 0.3371 -0.0105 -0.0004 -0.0202 249 MET B CG  
4242 S  SD  . MET B 273 ? 0.4999 0.4481 0.4600 -0.0095 -0.0002 -0.0209 249 MET B SD  
4243 C  CE  . MET B 273 ? 0.4651 0.4105 0.4223 -0.0108 0.0009  -0.0214 249 MET B CE  
4244 N  N   . GLY B 274 ? 0.4084 0.3292 0.3589 -0.0088 0.0043  -0.0231 250 GLY B N   
4245 C  CA  . GLY B 274 ? 0.4305 0.3441 0.3781 -0.0080 0.0064  -0.0261 250 GLY B CA  
4246 C  C   . GLY B 274 ? 0.4411 0.3558 0.3899 -0.0040 0.0095  -0.0263 250 GLY B C   
4247 O  O   . GLY B 274 ? 0.4523 0.3617 0.3980 -0.0028 0.0118  -0.0294 250 GLY B O   
4248 N  N   . GLY B 275 ? 0.3885 0.3103 0.3417 -0.0019 0.0097  -0.0234 251 GLY B N   
4249 C  CA  . GLY B 275 ? 0.3777 0.3022 0.3335 0.0018  0.0123  -0.0230 251 GLY B CA  
4250 C  C   . GLY B 275 ? 0.4283 0.3530 0.3892 0.0051  0.0133  -0.0200 251 GLY B C   
4251 O  O   . GLY B 275 ? 0.4305 0.3522 0.3927 0.0047  0.0124  -0.0180 251 GLY B O   
4252 N  N   . HIS B 276 ? 0.3991 0.3283 0.3637 0.0085  0.0152  -0.0189 252 HIS B N   
4253 C  CA  . HIS B 276 ? 0.3834 0.3140 0.3534 0.0125  0.0164  -0.0154 252 HIS B CA  
4254 C  C   . HIS B 276 ? 0.3845 0.3266 0.3592 0.0136  0.0146  -0.0127 252 HIS B C   
4255 O  O   . HIS B 276 ? 0.3887 0.3361 0.3629 0.0114  0.0129  -0.0141 252 HIS B O   
4256 C  CB  . HIS B 276 ? 0.4033 0.3290 0.3743 0.0161  0.0205  -0.0168 252 HIS B CB  
4257 C  CG  . HIS B 276 ? 0.4540 0.3689 0.4192 0.0145  0.0220  -0.0213 252 HIS B CG  
4258 N  ND1 . HIS B 276 ? 0.4490 0.3547 0.4141 0.0141  0.0222  -0.0217 252 HIS B ND1 
4259 C  CD2 . HIS B 276 ? 0.4263 0.3386 0.3853 0.0128  0.0231  -0.0258 252 HIS B CD2 
4260 C  CE1 . HIS B 276 ? 0.4698 0.3673 0.4289 0.0122  0.0230  -0.0269 252 HIS B CE1 
4261 N  NE2 . HIS B 276 ? 0.4691 0.3710 0.4239 0.0116  0.0236  -0.0294 252 HIS B NE2 
4262 N  N   . VAL B 277 ? 0.3638 0.3097 0.3433 0.0171  0.0146  -0.0087 253 VAL B N   
4263 C  CA  . VAL B 277 ? 0.3759 0.3331 0.3590 0.0177  0.0117  -0.0062 253 VAL B CA  
4264 C  C   . VAL B 277 ? 0.3694 0.3328 0.3590 0.0222  0.0130  -0.0032 253 VAL B C   
4265 O  O   . VAL B 277 ? 0.3668 0.3254 0.3587 0.0257  0.0157  -0.0010 253 VAL B O   
4266 C  CB  . VAL B 277 ? 0.3815 0.3406 0.3633 0.0172  0.0093  -0.0032 253 VAL B CB  
4267 C  CG1 . VAL B 277 ? 0.3649 0.3174 0.3415 0.0132  0.0086  -0.0055 253 VAL B CG1 
4268 C  CG2 . VAL B 277 ? 0.3975 0.3544 0.3826 0.0210  0.0109  0.0018  253 VAL B CG2 
4269 N  N   . ARG B 278 ? 0.3360 0.3100 0.3291 0.0220  0.0107  -0.0032 254 ARG B N   
4270 C  CA  . ARG B 278 ? 0.3884 0.3712 0.3886 0.0259  0.0107  0.0001  254 ARG B CA  
4271 C  C   . ARG B 278 ? 0.3691 0.3629 0.3706 0.0259  0.0062  0.0022  254 ARG B C   
4272 O  O   . ARG B 278 ? 0.3615 0.3590 0.3606 0.0224  0.0031  -0.0009 254 ARG B O   
4273 C  CB  . ARG B 278 ? 0.3663 0.3536 0.3711 0.0256  0.0120  -0.0020 254 ARG B CB  
4274 C  CG  . ARG B 278 ? 0.4054 0.4051 0.4187 0.0283  0.0105  0.0011  254 ARG B CG  
4275 C  CD  . ARG B 278 ? 0.4026 0.4057 0.4218 0.0287  0.0132  0.0002  254 ARG B CD  
4276 N  NE  . ARG B 278 ? 0.4040 0.4209 0.4319 0.0291  0.0102  0.0019  254 ARG B NE  
4277 C  CZ  . ARG B 278 ? 0.4229 0.4461 0.4589 0.0301  0.0122  0.0027  254 ARG B CZ  
4278 N  NH1 . ARG B 278 ? 0.4198 0.4371 0.4557 0.0314  0.0177  0.0021  254 ARG B NH1 
4279 N  NH2 . ARG B 278 ? 0.3928 0.4293 0.4373 0.0296  0.0085  0.0040  254 ARG B NH2 
4280 N  N   . VAL B 279 ? 0.3383 0.3373 0.3435 0.0301  0.0058  0.0074  255 VAL B N   
4281 C  CA  . VAL B 279 ? 0.3481 0.3595 0.3543 0.0309  0.0014  0.0098  255 VAL B CA  
4282 C  C   . VAL B 279 ? 0.3927 0.4142 0.4073 0.0349  0.0010  0.0136  255 VAL B C   
4283 O  O   . VAL B 279 ? 0.3786 0.3973 0.3982 0.0369  0.0044  0.0139  255 VAL B O   
4284 C  CB  . VAL B 279 ? 0.3732 0.3832 0.3751 0.0322  0.0008  0.0140  255 VAL B CB  
4285 C  CG1 . VAL B 279 ? 0.3703 0.3722 0.3651 0.0280  0.0009  0.0104  255 VAL B CG1 
4286 C  CG2 . VAL B 279 ? 0.3336 0.3373 0.3389 0.0366  0.0045  0.0198  255 VAL B CG2 
4287 N  N   . GLY B 280 ? 0.3764 0.4106 0.3923 0.0364  -0.0033 0.0164  256 GLY B N   
4288 C  CA  . GLY B 280 ? 0.3536 0.3988 0.3777 0.0405  -0.0043 0.0210  256 GLY B CA  
4289 C  C   . GLY B 280 ? 0.3668 0.4273 0.3939 0.0388  -0.0100 0.0188  256 GLY B C   
4290 O  O   . GLY B 280 ? 0.3677 0.4286 0.3925 0.0339  -0.0122 0.0124  256 GLY B O   
4291 N  N   . LEU B 281 ? 0.3489 0.4223 0.3817 0.0427  -0.0125 0.0241  257 LEU B N   
4292 C  CA  . LEU B 281 ? 0.3522 0.4416 0.3886 0.0411  -0.0186 0.0221  257 LEU B CA  
4293 C  C   . LEU B 281 ? 0.3576 0.4498 0.4024 0.0381  -0.0187 0.0177  257 LEU B C   
4294 O  O   . LEU B 281 ? 0.3489 0.4524 0.3968 0.0350  -0.0241 0.0141  257 LEU B O   
4295 C  CB  . LEU B 281 ? 0.3716 0.4747 0.4125 0.0465  -0.0213 0.0298  257 LEU B CB  
4296 C  CG  . LEU B 281 ? 0.4164 0.5254 0.4489 0.0483  -0.0245 0.0332  257 LEU B CG  
4297 C  CD1 . LEU B 281 ? 0.3835 0.4776 0.4076 0.0482  -0.0202 0.0342  257 LEU B CD1 
4298 C  CD2 . LEU B 281 ? 0.3979 0.5195 0.4358 0.0545  -0.0261 0.0426  257 LEU B CD2 
4299 N  N   . GLU B 282 ? 0.3412 0.4238 0.3899 0.0387  -0.0130 0.0180  258 GLU B N   
4300 C  CA  . GLU B 282 ? 0.3649 0.4491 0.4206 0.0352  -0.0124 0.0139  258 GLU B CA  
4301 C  C   . GLU B 282 ? 0.3763 0.4563 0.4267 0.0288  -0.0147 0.0065  258 GLU B C   
4302 O  O   . GLU B 282 ? 0.4033 0.4893 0.4600 0.0249  -0.0170 0.0029  258 GLU B O   
4303 C  CB  . GLU B 282 ? 0.3766 0.4504 0.4350 0.0374  -0.0051 0.0152  258 GLU B CB  
4304 C  CG  . GLU B 282 ? 0.3638 0.4361 0.4266 0.0332  -0.0032 0.0110  258 GLU B CG  
4305 C  CD  . GLU B 282 ? 0.3897 0.4564 0.4568 0.0366  0.0039  0.0132  258 GLU B CD  
4306 O  OE1 . GLU B 282 ? 0.3620 0.4259 0.4297 0.0423  0.0071  0.0176  258 GLU B OE1 
4307 O  OE2 . GLU B 282 ? 0.3896 0.4547 0.4596 0.0338  0.0066  0.0108  258 GLU B OE2 
4308 N  N   . ASP B 283 ? 0.3760 0.4458 0.4157 0.0276  -0.0139 0.0045  259 ASP B N   
4309 C  CA  . ASP B 283 ? 0.4128 0.4763 0.4474 0.0222  -0.0149 -0.0019 259 ASP B CA  
4310 C  C   . ASP B 283 ? 0.4195 0.4885 0.4481 0.0203  -0.0203 -0.0053 259 ASP B C   
4311 O  O   . ASP B 283 ? 0.4385 0.5063 0.4663 0.0158  -0.0224 -0.0113 259 ASP B O   
4312 C  CB  . ASP B 283 ? 0.3964 0.4443 0.4236 0.0219  -0.0099 -0.0024 259 ASP B CB  
4313 C  CG  . ASP B 283 ? 0.4547 0.4963 0.4858 0.0240  -0.0042 -0.0001 259 ASP B CG  
4314 O  OD1 . ASP B 283 ? 0.4699 0.5175 0.5096 0.0236  -0.0036 -0.0001 259 ASP B OD1 
4315 O  OD2 . ASP B 283 ? 0.4380 0.4691 0.4639 0.0259  -0.0003 0.0014  259 ASP B OD2 
4316 N  N   . ASN B 284 ? 0.3683 0.4433 0.3929 0.0239  -0.0223 -0.0014 260 ASN B N   
4317 C  CA  . ASN B 284 ? 0.4095 0.4899 0.4268 0.0228  -0.0268 -0.0045 260 ASN B CA  
4318 C  C   . ASN B 284 ? 0.3798 0.4726 0.3965 0.0273  -0.0297 0.0012  260 ASN B C   
4319 O  O   . ASN B 284 ? 0.3512 0.4414 0.3673 0.0317  -0.0266 0.0083  260 ASN B O   
4320 C  CB  . ASN B 284 ? 0.3903 0.4587 0.3979 0.0219  -0.0239 -0.0056 260 ASN B CB  
4321 C  CG  . ASN B 284 ? 0.4260 0.5004 0.4255 0.0219  -0.0275 -0.0077 260 ASN B CG  
4322 O  OD1 . ASN B 284 ? 0.4382 0.5223 0.4381 0.0202  -0.0324 -0.0126 260 ASN B OD1 
4323 N  ND2 . ASN B 284 ? 0.3973 0.4663 0.3896 0.0238  -0.0250 -0.0043 260 ASN B ND2 
4324 N  N   . LEU B 285 ? 0.4084 0.5146 0.4253 0.0263  -0.0359 -0.0021 261 LEU B N   
4325 C  CA  . LEU B 285 ? 0.4571 0.5776 0.4729 0.0305  -0.0396 0.0032  261 LEU B CA  
4326 C  C   . LEU B 285 ? 0.4765 0.5992 0.4803 0.0319  -0.0409 0.0034  261 LEU B C   
4327 O  O   . LEU B 285 ? 0.4469 0.5814 0.4482 0.0359  -0.0435 0.0089  261 LEU B O   
4328 C  CB  . LEU B 285 ? 0.4321 0.5683 0.4549 0.0287  -0.0462 -0.0004 261 LEU B CB  
4329 C  CG  . LEU B 285 ? 0.4338 0.5720 0.4702 0.0279  -0.0453 0.0009  261 LEU B CG  
4330 C  CD1 . LEU B 285 ? 0.4051 0.5589 0.4487 0.0249  -0.0525 -0.0037 261 LEU B CD1 
4331 C  CD2 . LEU B 285 ? 0.4229 0.5625 0.4643 0.0340  -0.0417 0.0110  261 LEU B CD2 
4332 N  N   . TRP B 286 ? 0.4819 0.5944 0.4785 0.0290  -0.0390 -0.0017 262 TRP B N   
4333 C  CA  . TRP B 286 ? 0.5214 0.6376 0.5071 0.0297  -0.0406 -0.0032 262 TRP B CA  
4334 C  C   . TRP B 286 ? 0.5159 0.6219 0.4961 0.0321  -0.0351 0.0029  262 TRP B C   
4335 O  O   . TRP B 286 ? 0.5281 0.6203 0.5110 0.0308  -0.0304 0.0038  262 TRP B O   
4336 C  CB  . TRP B 286 ? 0.5792 0.6929 0.5617 0.0249  -0.0428 -0.0140 262 TRP B CB  
4337 C  CG  . TRP B 286 ? 0.6426 0.7656 0.6318 0.0220  -0.0484 -0.0203 262 TRP B CG  
4338 C  CD1 . TRP B 286 ? 0.6538 0.7722 0.6531 0.0182  -0.0482 -0.0238 262 TRP B CD1 
4339 C  CD2 . TRP B 286 ? 0.7153 0.8547 0.7022 0.0225  -0.0551 -0.0234 262 TRP B CD2 
4340 N  NE1 . TRP B 286 ? 0.7405 0.8710 0.7451 0.0160  -0.0545 -0.0289 262 TRP B NE1 
4341 C  CE2 . TRP B 286 ? 0.7545 0.8980 0.7514 0.0185  -0.0590 -0.0293 262 TRP B CE2 
4342 C  CE3 . TRP B 286 ? 0.7243 0.8758 0.7015 0.0260  -0.0581 -0.0218 262 TRP B CE3 
4343 C  CZ2 . TRP B 286 ? 0.7827 0.9417 0.7805 0.0174  -0.0664 -0.0342 262 TRP B CZ2 
4344 C  CZ3 . TRP B 286 ? 0.7597 0.9270 0.7366 0.0253  -0.0654 -0.0268 262 TRP B CZ3 
4345 C  CH2 . TRP B 286 ? 0.7660 0.9368 0.7532 0.0209  -0.0697 -0.0333 262 TRP B CH2 
4346 N  N   . ALA B 287 ? 0.5538 0.6674 0.5263 0.0354  -0.0358 0.0073  263 ALA B N   
4347 C  CA  . ALA B 287 ? 0.6204 0.7260 0.5876 0.0372  -0.0310 0.0131  263 ALA B CA  
4348 C  C   . ALA B 287 ? 0.7248 0.8285 0.6832 0.0350  -0.0308 0.0073  263 ALA B C   
4349 O  O   . ALA B 287 ? 0.8348 0.9260 0.7923 0.0330  -0.0268 0.0065  263 ALA B O   
4350 C  CB  . ALA B 287 ? 0.5609 0.6763 0.5265 0.0427  -0.0310 0.0238  263 ALA B CB  
4351 N  N   . GLY B 288 ? 0.7412 0.8576 0.6931 0.0355  -0.0351 0.0029  264 GLY B N   
4352 C  CA  . GLY B 288 ? 0.8664 0.9820 0.8102 0.0340  -0.0349 -0.0038 264 GLY B CA  
4353 C  C   . GLY B 288 ? 0.9778 1.1020 0.9196 0.0318  -0.0405 -0.0145 264 GLY B C   
4354 O  O   . GLY B 288 ? 0.9604 1.0837 0.9098 0.0289  -0.0433 -0.0193 264 GLY B O   
4355 N  N   . LYS B 289 ? 1.0464 1.1789 0.9783 0.0331  -0.0421 -0.0185 265 LYS B N   
4356 C  CA  . LYS B 289 ? 1.0538 1.1938 0.9830 0.0311  -0.0475 -0.0299 265 LYS B CA  
4357 C  C   . LYS B 289 ? 1.0426 1.1999 0.9708 0.0333  -0.0535 -0.0283 265 LYS B C   
4358 O  O   . LYS B 289 ? 1.0824 1.2514 1.0024 0.0378  -0.0539 -0.0222 265 LYS B O   
4359 C  CB  . LYS B 289 ? 1.1039 1.2450 1.0226 0.0319  -0.0463 -0.0359 265 LYS B CB  
4360 C  CG  . LYS B 289 ? 1.0777 1.2191 0.9958 0.0284  -0.0504 -0.0500 265 LYS B CG  
4361 C  CD  . LYS B 289 ? 1.0940 1.2349 1.0024 0.0297  -0.0481 -0.0561 265 LYS B CD  
4362 C  CE  . LYS B 289 ? 1.1758 1.3018 1.0865 0.0290  -0.0415 -0.0529 265 LYS B CE  
4363 N  NZ  . LYS B 289 ? 1.1842 1.3094 1.0873 0.0301  -0.0392 -0.0595 265 LYS B NZ  
4364 N  N   . GLY B 290 ? 0.9784 1.1382 0.9152 0.0302  -0.0580 -0.0332 266 GLY B N   
4365 C  CA  . GLY B 290 ? 0.9321 1.1089 0.8698 0.0318  -0.0643 -0.0319 266 GLY B CA  
4366 C  C   . GLY B 290 ? 0.9189 1.1014 0.8590 0.0366  -0.0628 -0.0180 266 GLY B C   
4367 O  O   . GLY B 290 ? 0.9117 1.1105 0.8509 0.0393  -0.0676 -0.0146 266 GLY B O   
4368 N  N   . ARG B 291 ? 0.8050 0.9744 0.7488 0.0377  -0.0562 -0.0100 267 ARG B N   
4369 C  CA  . ARG B 291 ? 0.7059 0.8778 0.6529 0.0424  -0.0537 0.0033  267 ARG B CA  
4370 C  C   . ARG B 291 ? 0.5977 0.7598 0.5578 0.0409  -0.0514 0.0061  267 ARG B C   
4371 O  O   . ARG B 291 ? 0.5679 0.7140 0.5314 0.0380  -0.0470 0.0035  267 ARG B O   
4372 C  CB  . ARG B 291 ? 0.7079 0.8731 0.6483 0.0452  -0.0476 0.0108  267 ARG B CB  
4373 C  CG  . ARG B 291 ? 0.6437 0.8131 0.5863 0.0506  -0.0453 0.0251  267 ARG B CG  
4374 C  CD  . ARG B 291 ? 0.6844 0.8547 0.6182 0.0538  -0.0413 0.0323  267 ARG B CD  
4375 N  NE  . ARG B 291 ? 0.6790 0.8651 0.6008 0.0555  -0.0451 0.0289  267 ARG B NE  
4376 C  CZ  . ARG B 291 ? 0.7203 0.9052 0.6334 0.0536  -0.0447 0.0203  267 ARG B CZ  
4377 N  NH1 . ARG B 291 ? 0.6828 0.8517 0.5981 0.0498  -0.0407 0.0148  267 ARG B NH1 
4378 N  NH2 . ARG B 291 ? 0.7136 0.9142 0.6155 0.0557  -0.0483 0.0170  267 ARG B NH2 
4379 N  N   . LEU B 292 ? 0.5599 0.7322 0.5272 0.0432  -0.0544 0.0113  268 LEU B N   
4380 C  CA  . LEU B 292 ? 0.5331 0.6976 0.5128 0.0430  -0.0516 0.0151  268 LEU B CA  
4381 C  C   . LEU B 292 ? 0.4921 0.6459 0.4730 0.0468  -0.0449 0.0255  268 LEU B C   
4382 O  O   . LEU B 292 ? 0.4459 0.6049 0.4215 0.0512  -0.0440 0.0337  268 LEU B O   
4383 C  CB  . LEU B 292 ? 0.4739 0.6540 0.4618 0.0449  -0.0568 0.0180  268 LEU B CB  
4384 C  CG  . LEU B 292 ? 0.4896 0.6798 0.4807 0.0403  -0.0638 0.0077  268 LEU B CG  
4385 C  CD1 . LEU B 292 ? 0.4666 0.6750 0.4651 0.0430  -0.0693 0.0127  268 LEU B CD1 
4386 C  CD2 . LEU B 292 ? 0.5260 0.7032 0.5254 0.0348  -0.0616 0.0004  268 LEU B CD2 
4387 N  N   . ALA B 293 ? 0.4480 0.5868 0.4360 0.0451  -0.0402 0.0251  269 ALA B N   
4388 C  CA  . ALA B 293 ? 0.4500 0.5783 0.4413 0.0485  -0.0342 0.0341  269 ALA B CA  
4389 C  C   . ALA B 293 ? 0.4417 0.5801 0.4410 0.0538  -0.0352 0.0433  269 ALA B C   
4390 O  O   . ALA B 293 ? 0.4129 0.5590 0.4200 0.0534  -0.0383 0.0414  269 ALA B O   
4391 C  CB  . ALA B 293 ? 0.4366 0.5475 0.4329 0.0453  -0.0295 0.0302  269 ALA B CB  
4392 N  N   . GLU B 294 ? 0.4110 0.5494 0.4092 0.0588  -0.0325 0.0537  270 GLU B N   
4393 C  CA  . GLU B 294 ? 0.4452 0.5939 0.4508 0.0646  -0.0335 0.0637  270 GLU B CA  
4394 C  C   . GLU B 294 ? 0.4117 0.5477 0.4279 0.0671  -0.0277 0.0685  270 GLU B C   
4395 O  O   . GLU B 294 ? 0.4412 0.5851 0.4668 0.0711  -0.0286 0.0740  270 GLU B O   
4396 C  CB  . GLU B 294 ? 0.4457 0.6033 0.4451 0.0693  -0.0339 0.0737  270 GLU B CB  
4397 C  CG  . GLU B 294 ? 0.4883 0.6599 0.4760 0.0677  -0.0393 0.0689  270 GLU B CG  
4398 C  CD  . GLU B 294 ? 0.5393 0.7235 0.5210 0.0730  -0.0402 0.0798  270 GLU B CD  
4399 O  OE1 . GLU B 294 ? 0.5847 0.7723 0.5734 0.0785  -0.0387 0.0914  270 GLU B OE1 
4400 O  OE2 . GLU B 294 ? 0.5883 0.7793 0.5584 0.0721  -0.0420 0.0770  270 GLU B OE2 
4401 N  N   . THR B 295 ? 0.4324 0.5495 0.4477 0.0650  -0.0220 0.0664  271 THR B N   
4402 C  CA  . THR B 295 ? 0.4194 0.5234 0.4437 0.0670  -0.0165 0.0690  271 THR B CA  
4403 C  C   . THR B 295 ? 0.4241 0.5117 0.4463 0.0616  -0.0132 0.0596  271 THR B C   
4404 O  O   . THR B 295 ? 0.4186 0.5024 0.4326 0.0570  -0.0141 0.0534  271 THR B O   
4405 C  CB  . THR B 295 ? 0.4313 0.5273 0.4577 0.0717  -0.0118 0.0794  271 THR B CB  
4406 O  OG1 . THR B 295 ? 0.4696 0.5560 0.4876 0.0687  -0.0099 0.0783  271 THR B OG1 
4407 C  CG2 . THR B 295 ? 0.4022 0.5143 0.4312 0.0778  -0.0146 0.0904  271 THR B CG2 
4408 N  N   . ASN B 296 ? 0.4288 0.5074 0.4588 0.0627  -0.0092 0.0590  272 ASN B N   
4409 C  CA  . ASN B 296 ? 0.4049 0.4668 0.4329 0.0587  -0.0052 0.0519  272 ASN B CA  
4410 C  C   . ASN B 296 ? 0.3919 0.4398 0.4151 0.0583  -0.0015 0.0542  272 ASN B C   
4411 O  O   . ASN B 296 ? 0.4119 0.4503 0.4289 0.0534  -0.0006 0.0480  272 ASN B O   
4412 C  CB  . ASN B 296 ? 0.3833 0.4399 0.4203 0.0610  -0.0013 0.0515  272 ASN B CB  
4413 C  CG  . ASN B 296 ? 0.3443 0.4113 0.3858 0.0589  -0.0041 0.0464  272 ASN B CG  
4414 O  OD1 . ASN B 296 ? 0.3757 0.4381 0.4142 0.0539  -0.0041 0.0386  272 ASN B OD1 
4415 N  ND2 . ASN B 296 ? 0.3388 0.4202 0.3884 0.0628  -0.0066 0.0514  272 ASN B ND2 
4416 N  N   . ALA B 297 ? 0.3757 0.4221 0.4025 0.0632  0.0007  0.0634  273 ALA B N   
4417 C  CA  . ALA B 297 ? 0.4437 0.4770 0.4678 0.0626  0.0042  0.0664  273 ALA B CA  
4418 C  C   . ALA B 297 ? 0.4486 0.4844 0.4631 0.0583  0.0018  0.0639  273 ALA B C   
4419 O  O   . ALA B 297 ? 0.4270 0.4505 0.4380 0.0550  0.0042  0.0617  273 ALA B O   
4420 C  CB  . ALA B 297 ? 0.4418 0.4762 0.4722 0.0688  0.0062  0.0781  273 ALA B CB  
4421 N  N   . GLN B 298 ? 0.4401 0.4919 0.4503 0.0583  -0.0031 0.0638  274 GLN B N   
4422 C  CA  . GLN B 298 ? 0.4540 0.5098 0.4549 0.0550  -0.0053 0.0612  274 GLN B CA  
4423 C  C   . GLN B 298 ? 0.4145 0.4608 0.4110 0.0489  -0.0049 0.0507  274 GLN B C   
4424 O  O   . GLN B 298 ? 0.4263 0.4666 0.4175 0.0461  -0.0037 0.0494  274 GLN B O   
4425 C  CB  . GLN B 298 ? 0.4481 0.5234 0.4453 0.0565  -0.0108 0.0618  274 GLN B CB  
4426 C  CG  . GLN B 298 ? 0.5375 0.6185 0.5251 0.0527  -0.0139 0.0550  274 GLN B CG  
4427 C  CD  . GLN B 298 ? 0.5082 0.6086 0.4925 0.0544  -0.0197 0.0546  274 GLN B CD  
4428 O  OE1 . GLN B 298 ? 0.4415 0.5515 0.4313 0.0581  -0.0217 0.0596  274 GLN B OE1 
4429 N  NE2 . GLN B 298 ? 0.5199 0.6262 0.4955 0.0517  -0.0225 0.0484  274 GLN B NE2 
4430 N  N   . GLN B 299 ? 0.3639 0.4093 0.3633 0.0470  -0.0058 0.0439  275 GLN B N   
4431 C  CA  . GLN B 299 ? 0.4001 0.4365 0.3962 0.0417  -0.0052 0.0349  275 GLN B CA  
4432 C  C   . GLN B 299 ? 0.4137 0.4331 0.4109 0.0405  -0.0004 0.0347  275 GLN B C   
4433 O  O   . GLN B 299 ? 0.3992 0.4107 0.3918 0.0363  0.0003  0.0299  275 GLN B O   
4434 C  CB  . GLN B 299 ? 0.3858 0.4266 0.3855 0.0401  -0.0072 0.0288  275 GLN B CB  
4435 C  CG  . GLN B 299 ? 0.3603 0.4175 0.3589 0.0400  -0.0127 0.0270  275 GLN B CG  
4436 C  CD  . GLN B 299 ? 0.4079 0.4691 0.4115 0.0376  -0.0147 0.0209  275 GLN B CD  
4437 O  OE1 . GLN B 299 ? 0.3938 0.4474 0.4025 0.0371  -0.0116 0.0196  275 GLN B OE1 
4438 N  NE2 . GLN B 299 ? 0.3757 0.4491 0.3781 0.0360  -0.0199 0.0170  275 GLN B NE2 
4439 N  N   . VAL B 300 ? 0.3835 0.3971 0.3869 0.0441  0.0028  0.0396  276 VAL B N   
4440 C  CA  . VAL B 300 ? 0.3888 0.3859 0.3931 0.0431  0.0071  0.0389  276 VAL B CA  
4441 C  C   . VAL B 300 ? 0.3830 0.3755 0.3839 0.0415  0.0078  0.0425  276 VAL B C   
4442 O  O   . VAL B 300 ? 0.3670 0.3488 0.3650 0.0375  0.0092  0.0385  276 VAL B O   
4443 C  CB  . VAL B 300 ? 0.3731 0.3652 0.3855 0.0480  0.0106  0.0434  276 VAL B CB  
4444 C  CG1 . VAL B 300 ? 0.3911 0.3659 0.4044 0.0471  0.0148  0.0428  276 VAL B CG1 
4445 C  CG2 . VAL B 300 ? 0.3821 0.3777 0.3982 0.0490  0.0107  0.0392  276 VAL B CG2 
4446 N  N   . ARG B 301 ? 0.3927 0.3939 0.3940 0.0447  0.0068  0.0506  277 ARG B N   
4447 C  CA  . ARG B 301 ? 0.4075 0.4059 0.4063 0.0434  0.0079  0.0551  277 ARG B CA  
4448 C  C   . ARG B 301 ? 0.3865 0.3862 0.3778 0.0384  0.0060  0.0487  277 ARG B C   
4449 O  O   . ARG B 301 ? 0.4210 0.4125 0.4112 0.0353  0.0077  0.0487  277 ARG B O   
4450 C  CB  . ARG B 301 ? 0.4170 0.4277 0.4167 0.0480  0.0070  0.0652  277 ARG B CB  
4451 C  CG  . ARG B 301 ? 0.5027 0.5106 0.5110 0.0533  0.0095  0.0738  277 ARG B CG  
4452 C  CD  . ARG B 301 ? 0.5643 0.5827 0.5734 0.0575  0.0092  0.0855  277 ARG B CD  
4453 N  NE  . ARG B 301 ? 0.5673 0.6048 0.5716 0.0598  0.0048  0.0863  277 ARG B NE  
4454 C  CZ  . ARG B 301 ? 0.5645 0.6121 0.5729 0.0644  0.0029  0.0899  277 ARG B CZ  
4455 N  NH1 . ARG B 301 ? 0.5347 0.5753 0.5524 0.0678  0.0055  0.0933  277 ARG B NH1 
4456 N  NH2 . ARG B 301 ? 0.5803 0.6458 0.5836 0.0657  -0.0019 0.0898  277 ARG B NH2 
4457 N  N   . ALA B 302 ? 0.3586 0.3685 0.3457 0.0375  0.0026  0.0433  278 ALA B N   
4458 C  CA  . ALA B 302 ? 0.4122 0.4231 0.3930 0.0333  0.0010  0.0371  278 ALA B CA  
4459 C  C   . ALA B 302 ? 0.4207 0.4181 0.4016 0.0289  0.0027  0.0307  278 ALA B C   
4460 O  O   . ALA B 302 ? 0.4167 0.4088 0.3952 0.0258  0.0036  0.0298  278 ALA B O   
4461 C  CB  . ALA B 302 ? 0.3790 0.4022 0.3565 0.0332  -0.0030 0.0319  278 ALA B CB  
4462 N  N   . ALA B 303 ? 0.3759 0.3687 0.3597 0.0287  0.0031  0.0266  279 ALA B N   
4463 C  CA  . ALA B 303 ? 0.3895 0.3703 0.3727 0.0250  0.0047  0.0208  279 ALA B CA  
4464 C  C   . ALA B 303 ? 0.3956 0.3648 0.3804 0.0241  0.0075  0.0238  279 ALA B C   
4465 O  O   . ALA B 303 ? 0.4046 0.3664 0.3869 0.0201  0.0079  0.0202  279 ALA B O   
4466 C  CB  . ALA B 303 ? 0.3694 0.3479 0.3558 0.0260  0.0056  0.0174  279 ALA B CB  
4467 N  N   . ARG B 304 ? 0.3898 0.3573 0.3792 0.0277  0.0094  0.0306  280 ARG B N   
4468 C  CA  . ARG B 304 ? 0.4242 0.3800 0.4166 0.0267  0.0121  0.0336  280 ARG B CA  
4469 C  C   . ARG B 304 ? 0.4171 0.3745 0.4072 0.0238  0.0115  0.0363  280 ARG B C   
4470 O  O   . ARG B 304 ? 0.4386 0.3865 0.4292 0.0201  0.0124  0.0345  280 ARG B O   
4471 C  CB  . ARG B 304 ? 0.4277 0.3820 0.4268 0.0317  0.0143  0.0412  280 ARG B CB  
4472 C  CG  . ARG B 304 ? 0.4834 0.4253 0.4873 0.0307  0.0171  0.0451  280 ARG B CG  
4473 C  CD  . ARG B 304 ? 0.5047 0.4428 0.5164 0.0360  0.0198  0.0515  280 ARG B CD  
4474 N  NE  . ARG B 304 ? 0.5654 0.4880 0.5825 0.0346  0.0227  0.0525  280 ARG B NE  
4475 C  CZ  . ARG B 304 ? 0.6071 0.5203 0.6313 0.0382  0.0258  0.0546  280 ARG B CZ  
4476 N  NH1 . ARG B 304 ? 0.5999 0.5184 0.6271 0.0438  0.0266  0.0568  280 ARG B NH1 
4477 N  NH2 . ARG B 304 ? 0.6755 0.5737 0.7046 0.0361  0.0281  0.0543  280 ARG B NH2 
4478 N  N   . GLN B 305 ? 0.3891 0.3593 0.3767 0.0256  0.0099  0.0404  281 GLN B N   
4479 C  CA  . GLN B 305 ? 0.4261 0.3995 0.4112 0.0233  0.0098  0.0428  281 GLN B CA  
4480 C  C   . GLN B 305 ? 0.4359 0.4057 0.4172 0.0184  0.0086  0.0350  281 GLN B C   
4481 O  O   . GLN B 305 ? 0.4522 0.4174 0.4343 0.0151  0.0094  0.0359  281 GLN B O   
4482 C  CB  . GLN B 305 ? 0.4256 0.4147 0.4070 0.0265  0.0082  0.0469  281 GLN B CB  
4483 C  CG  . GLN B 305 ? 0.5335 0.5273 0.5132 0.0257  0.0092  0.0521  281 GLN B CG  
4484 C  CD  . GLN B 305 ? 0.5441 0.5540 0.5189 0.0295  0.0079  0.0562  281 GLN B CD  
4485 O  OE1 . GLN B 305 ? 0.6078 0.6244 0.5834 0.0337  0.0071  0.0605  281 GLN B OE1 
4486 N  NE2 . GLN B 305 ? 0.4969 0.5137 0.4666 0.0283  0.0076  0.0547  281 GLN B NE2 
4487 N  N   . ILE B 306 ? 0.4042 0.3764 0.3821 0.0177  0.0067  0.0279  282 ILE B N   
4488 C  CA  . ILE B 306 ? 0.4080 0.3767 0.3829 0.0134  0.0057  0.0210  282 ILE B CA  
4489 C  C   . ILE B 306 ? 0.4097 0.3651 0.3868 0.0104  0.0070  0.0188  282 ILE B C   
4490 O  O   . ILE B 306 ? 0.4149 0.3663 0.3915 0.0067  0.0069  0.0175  282 ILE B O   
4491 C  CB  . ILE B 306 ? 0.4028 0.3762 0.3751 0.0136  0.0036  0.0147  282 ILE B CB  
4492 C  CG1 . ILE B 306 ? 0.3975 0.3840 0.3670 0.0158  0.0016  0.0154  282 ILE B CG1 
4493 C  CG2 . ILE B 306 ? 0.4083 0.3766 0.3783 0.0094  0.0029  0.0084  282 ILE B CG2 
4494 C  CD1 . ILE B 306 ? 0.3932 0.3849 0.3622 0.0162  -0.0006 0.0100  282 ILE B CD1 
4495 N  N   . VAL B 307 ? 0.4110 0.3598 0.3906 0.0120  0.0084  0.0180  283 VAL B N   
4496 C  CA  . VAL B 307 ? 0.4348 0.3708 0.4155 0.0093  0.0096  0.0146  283 VAL B CA  
4497 C  C   . VAL B 307 ? 0.4448 0.3747 0.4289 0.0070  0.0105  0.0186  283 VAL B C   
4498 O  O   . VAL B 307 ? 0.4406 0.3641 0.4240 0.0027  0.0099  0.0151  283 VAL B O   
4499 C  CB  . VAL B 307 ? 0.4708 0.4013 0.4541 0.0126  0.0116  0.0139  283 VAL B CB  
4500 C  CG1 . VAL B 307 ? 0.4312 0.3477 0.4159 0.0105  0.0133  0.0109  283 VAL B CG1 
4501 C  CG2 . VAL B 307 ? 0.4278 0.3632 0.4085 0.0136  0.0109  0.0090  283 VAL B CG2 
4502 N  N   . GLU B 308 ? 0.4292 0.3616 0.4176 0.0097  0.0119  0.0263  284 GLU B N   
4503 C  CA  . GLU B 308 ? 0.4617 0.3880 0.4551 0.0075  0.0131  0.0311  284 GLU B CA  
4504 C  C   . GLU B 308 ? 0.4767 0.4098 0.4687 0.0044  0.0119  0.0328  284 GLU B C   
4505 O  O   . GLU B 308 ? 0.4408 0.3681 0.4363 0.0004  0.0121  0.0334  284 GLU B O   
4506 C  CB  . GLU B 308 ? 0.4683 0.3952 0.4677 0.0117  0.0154  0.0399  284 GLU B CB  
4507 C  CG  . GLU B 308 ? 0.5078 0.4256 0.5106 0.0146  0.0172  0.0385  284 GLU B CG  
4508 C  CD  . GLU B 308 ? 0.5217 0.4415 0.5306 0.0199  0.0193  0.0478  284 GLU B CD  
4509 O  OE1 . GLU B 308 ? 0.5158 0.4443 0.5259 0.0211  0.0194  0.0559  284 GLU B OE1 
4510 O  OE2 . GLU B 308 ? 0.5174 0.4306 0.5301 0.0231  0.0211  0.0474  284 GLU B OE2 
4511 N  N   . GLY B 309 ? 0.4493 0.3947 0.4367 0.0062  0.0108  0.0333  285 GLY B N   
4512 C  CA  . GLY B 309 ? 0.4408 0.3925 0.4264 0.0037  0.0100  0.0335  285 GLY B CA  
4513 C  C   . GLY B 309 ? 0.4726 0.4184 0.4569 -0.0011 0.0084  0.0267  285 GLY B C   
4514 O  O   . GLY B 309 ? 0.4707 0.4174 0.4570 -0.0043 0.0082  0.0279  285 GLY B O   
4515 N  N   . LEU B 310 ? 0.4556 0.3963 0.4371 -0.0015 0.0074  0.0199  286 LEU B N   
4516 C  CA  . LEU B 310 ? 0.4560 0.3912 0.4356 -0.0058 0.0058  0.0137  286 LEU B CA  
4517 C  C   . LEU B 310 ? 0.4576 0.3819 0.4412 -0.0094 0.0060  0.0134  286 LEU B C   
4518 O  O   . LEU B 310 ? 0.4591 0.3795 0.4413 -0.0133 0.0042  0.0086  286 LEU B O   
4519 C  CB  . LEU B 310 ? 0.4130 0.3466 0.3882 -0.0048 0.0050  0.0074  286 LEU B CB  
4520 C  CG  . LEU B 310 ? 0.4315 0.3742 0.4029 -0.0035 0.0037  0.0048  286 LEU B CG  
4521 C  CD1 . LEU B 310 ? 0.4214 0.3623 0.3905 -0.0021 0.0037  0.0004  286 LEU B CD1 
4522 C  CD2 . LEU B 310 ? 0.4170 0.3616 0.3869 -0.0068 0.0021  0.0025  286 LEU B CD2 
4523 N  N   . GLY B 311 ? 0.4740 0.3934 0.4630 -0.0083 0.0079  0.0183  287 GLY B N   
4524 C  CA  . GLY B 311 ? 0.4837 0.3912 0.4772 -0.0119 0.0080  0.0170  287 GLY B CA  
4525 C  C   . GLY B 311 ? 0.4920 0.3895 0.4833 -0.0111 0.0085  0.0108  287 GLY B C   
4526 O  O   . GLY B 311 ? 0.5279 0.4151 0.5210 -0.0146 0.0080  0.0070  287 GLY B O   
4527 N  N   . LEU B 312 ? 0.4667 0.3672 0.4544 -0.0067 0.0095  0.0094  288 LEU B N   
4528 C  CA  . LEU B 312 ? 0.5160 0.4084 0.5018 -0.0049 0.0107  0.0041  288 LEU B CA  
4529 C  C   . LEU B 312 ? 0.5029 0.3920 0.4943 -0.0003 0.0136  0.0091  288 LEU B C   
4530 O  O   . LEU B 312 ? 0.5331 0.4268 0.5292 0.0016  0.0144  0.0169  288 LEU B O   
4531 C  CB  . LEU B 312 ? 0.4854 0.3841 0.4647 -0.0033 0.0100  -0.0005 288 LEU B CB  
4532 C  CG  . LEU B 312 ? 0.5136 0.4165 0.4879 -0.0072 0.0073  -0.0044 288 LEU B CG  
4533 C  CD1 . LEU B 312 ? 0.4662 0.3759 0.4360 -0.0051 0.0070  -0.0071 288 LEU B CD1 
4534 C  CD2 . LEU B 312 ? 0.5460 0.4398 0.5182 -0.0114 0.0061  -0.0100 288 LEU B CD2 
4535 N  N   . GLU B 313 ? 0.5088 0.3902 0.4997 0.0021  0.0155  0.0048  289 GLU B N   
4536 C  CA  . GLU B 313 ? 0.5413 0.4189 0.5380 0.0071  0.0185  0.0091  289 GLU B CA  
4537 C  C   . GLU B 313 ? 0.5253 0.4073 0.5192 0.0118  0.0198  0.0066  289 GLU B C   
4538 O  O   . GLU B 313 ? 0.5048 0.3871 0.4926 0.0106  0.0192  -0.0002 289 GLU B O   
4539 C  CB  . GLU B 313 ? 0.5672 0.4292 0.5688 0.0059  0.0204  0.0067  289 GLU B CB  
4540 C  CG  . GLU B 313 ? 0.6331 0.4905 0.6397 0.0009  0.0191  0.0097  289 GLU B CG  
4541 C  CD  . GLU B 313 ? 0.8141 0.6555 0.8272 -0.0003 0.0209  0.0076  289 GLU B CD  
4542 O  OE1 . GLU B 313 ? 0.8334 0.6704 0.8543 0.0036  0.0238  0.0137  289 GLU B OE1 
4543 O  OE2 . GLU B 313 ? 0.8777 0.7107 0.8882 -0.0052 0.0193  -0.0003 289 GLU B OE2 
4544 N  N   . VAL B 314 ? 0.4997 0.3858 0.4986 0.0171  0.0216  0.0128  290 VAL B N   
4545 C  CA  . VAL B 314 ? 0.5326 0.4235 0.5309 0.0219  0.0230  0.0116  290 VAL B CA  
4546 C  C   . VAL B 314 ? 0.5143 0.3928 0.5143 0.0240  0.0264  0.0068  290 VAL B C   
4547 O  O   . VAL B 314 ? 0.5284 0.3959 0.5338 0.0245  0.0284  0.0083  290 VAL B O   
4548 C  CB  . VAL B 314 ? 0.5292 0.4305 0.5326 0.0269  0.0232  0.0203  290 VAL B CB  
4549 C  CG1 . VAL B 314 ? 0.5350 0.4412 0.5398 0.0319  0.0247  0.0195  290 VAL B CG1 
4550 C  CG2 . VAL B 314 ? 0.4934 0.4076 0.4934 0.0250  0.0198  0.0235  290 VAL B CG2 
4551 N  N   . ALA B 315 ? 0.5324 0.4125 0.5282 0.0252  0.0274  0.0010  291 ALA B N   
4552 C  CA  . ALA B 315 ? 0.5243 0.3937 0.5206 0.0278  0.0311  -0.0043 291 ALA B CA  
4553 C  C   . ALA B 315 ? 0.5405 0.4095 0.5453 0.0347  0.0345  0.0012  291 ALA B C   
4554 O  O   . ALA B 315 ? 0.5084 0.3894 0.5164 0.0382  0.0340  0.0068  291 ALA B O   
4555 C  CB  . ALA B 315 ? 0.5154 0.3884 0.5047 0.0275  0.0316  -0.0112 291 ALA B CB  
4556 N  N   . THR B 316 ? 0.5183 0.3733 0.5272 0.0366  0.0378  -0.0007 292 THR B N   
4557 C  CA  . THR B 316 ? 0.5389 0.3918 0.5561 0.0438  0.0419  0.0033  292 THR B CA  
4558 C  C   . THR B 316 ? 0.5587 0.4151 0.5731 0.0475  0.0447  -0.0019 292 THR B C   
4559 O  O   . THR B 316 ? 0.5376 0.3948 0.5434 0.0442  0.0440  -0.0093 292 THR B O   
4560 C  CB  . THR B 316 ? 0.5819 0.4173 0.6048 0.0446  0.0449  0.0020  292 THR B CB  
4561 O  OG1 . THR B 316 ? 0.5765 0.4006 0.5927 0.0420  0.0461  -0.0093 292 THR B OG1 
4562 C  CG2 . THR B 316 ? 0.5408 0.3725 0.5676 0.0404  0.0424  0.0076  292 THR B CG2 
4563 N  N   . PRO B 317 ? 0.5126 0.3719 0.5347 0.0545  0.0481  0.0024  293 PRO B N   
4564 C  CA  . PRO B 317 ? 0.5618 0.4235 0.5823 0.0584  0.0517  -0.0026 293 PRO B CA  
4565 C  C   . PRO B 317 ? 0.5807 0.4281 0.5949 0.0573  0.0549  -0.0131 293 PRO B C   
4566 O  O   . PRO B 317 ? 0.5630 0.4138 0.5704 0.0570  0.0562  -0.0192 293 PRO B O   
4567 C  CB  . PRO B 317 ? 0.5618 0.4264 0.5937 0.0665  0.0552  0.0047  293 PRO B CB  
4568 C  CG  . PRO B 317 ? 0.5550 0.4269 0.5923 0.0662  0.0515  0.0148  293 PRO B CG  
4569 C  CD  . PRO B 317 ? 0.5303 0.3934 0.5628 0.0595  0.0486  0.0129  293 PRO B CD  
4570 N  N   . ALA B 318 ? 0.5756 0.4073 0.5919 0.0566  0.0560  -0.0155 294 ALA B N   
4571 C  CA  . ALA B 318 ? 0.5839 0.4016 0.5938 0.0553  0.0585  -0.0265 294 ALA B CA  
4572 C  C   . ALA B 318 ? 0.5762 0.3955 0.5740 0.0477  0.0545  -0.0333 294 ALA B C   
4573 O  O   . ALA B 318 ? 0.6170 0.4326 0.6063 0.0472  0.0562  -0.0423 294 ALA B O   
4574 C  CB  . ALA B 318 ? 0.6391 0.4393 0.6555 0.0555  0.0601  -0.0275 294 ALA B CB  
4575 N  N   . GLU B 319 ? 0.5467 0.3720 0.5436 0.0421  0.0492  -0.0289 295 GLU B N   
4576 C  CA  . GLU B 319 ? 0.5805 0.4084 0.5669 0.0353  0.0453  -0.0342 295 GLU B CA  
4577 C  C   . GLU B 319 ? 0.5929 0.4348 0.5736 0.0358  0.0450  -0.0344 295 GLU B C   
4578 O  O   . GLU B 319 ? 0.5839 0.4263 0.5552 0.0325  0.0440  -0.0408 295 GLU B O   
4579 C  CB  . GLU B 319 ? 0.6038 0.4337 0.5921 0.0297  0.0403  -0.0292 295 GLU B CB  
4580 C  CG  . GLU B 319 ? 0.6578 0.4733 0.6518 0.0277  0.0403  -0.0295 295 GLU B CG  
4581 C  CD  . GLU B 319 ? 0.6652 0.4846 0.6642 0.0238  0.0367  -0.0216 295 GLU B CD  
4582 O  OE1 . GLU B 319 ? 0.6555 0.4883 0.6559 0.0251  0.0352  -0.0142 295 GLU B OE1 
4583 O  OE2 . GLU B 319 ? 0.7428 0.5523 0.7444 0.0195  0.0353  -0.0229 295 GLU B OE2 
4584 N  N   . ALA B 320 ? 0.5521 0.4056 0.5390 0.0398  0.0456  -0.0273 296 ALA B N   
4585 C  CA  . ALA B 320 ? 0.5616 0.4278 0.5451 0.0405  0.0458  -0.0274 296 ALA B CA  
4586 C  C   . ALA B 320 ? 0.5418 0.4046 0.5214 0.0441  0.0509  -0.0338 296 ALA B C   
4587 O  O   . ALA B 320 ? 0.5343 0.4020 0.5063 0.0421  0.0510  -0.0377 296 ALA B O   
4588 C  CB  . ALA B 320 ? 0.5145 0.3935 0.5065 0.0441  0.0453  -0.0188 296 ALA B CB  
4589 N  N   . ARG B 321 ? 0.5596 0.4142 0.5445 0.0498  0.0557  -0.0347 297 ARG B N   
4590 C  CA  . ARG B 321 ? 0.5674 0.4187 0.5486 0.0542  0.0613  -0.0410 297 ARG B CA  
4591 C  C   . ARG B 321 ? 0.5726 0.4159 0.5412 0.0499  0.0609  -0.0508 297 ARG B C   
4592 O  O   . ARG B 321 ? 0.5880 0.4346 0.5495 0.0513  0.0639  -0.0555 297 ARG B O   
4593 C  CB  . ARG B 321 ? 0.5429 0.3848 0.5326 0.0611  0.0664  -0.0407 297 ARG B CB  
4594 C  CG  . ARG B 321 ? 0.5263 0.3785 0.5283 0.0667  0.0676  -0.0309 297 ARG B CG  
4595 C  CD  . ARG B 321 ? 0.5578 0.4012 0.5687 0.0745  0.0734  -0.0302 297 ARG B CD  
4596 N  NE  . ARG B 321 ? 0.5309 0.3868 0.5533 0.0803  0.0746  -0.0208 297 ARG B NE  
4597 C  CZ  . ARG B 321 ? 0.5581 0.4168 0.5901 0.0819  0.0723  -0.0118 297 ARG B CZ  
4598 N  NH1 . ARG B 321 ? 0.5464 0.3951 0.5792 0.0787  0.0696  -0.0102 297 ARG B NH1 
4599 N  NH2 . ARG B 321 ? 0.5065 0.3789 0.5479 0.0868  0.0728  -0.0036 297 ARG B NH2 
4600 N  N   . GLU B 322 ? 0.5827 0.4164 0.5485 0.0445  0.0570  -0.0536 298 GLU B N   
4601 C  CA  . GLU B 322 ? 0.6259 0.4528 0.5797 0.0399  0.0556  -0.0629 298 GLU B CA  
4602 C  C   . GLU B 322 ? 0.5984 0.4370 0.5445 0.0349  0.0516  -0.0620 298 GLU B C   
4603 O  O   . GLU B 322 ? 0.5851 0.4252 0.5211 0.0340  0.0525  -0.0679 298 GLU B O   
4604 C  CB  . GLU B 322 ? 0.7209 0.5344 0.6760 0.0355  0.0524  -0.0659 298 GLU B CB  
4605 C  CG  . GLU B 322 ? 0.8548 0.6596 0.7985 0.0312  0.0509  -0.0767 298 GLU B CG  
4606 C  CD  . GLU B 322 ? 0.9716 0.7619 0.9191 0.0273  0.0484  -0.0801 298 GLU B CD  
4607 O  OE1 . GLU B 322 ? 0.9365 0.7196 0.8951 0.0303  0.0504  -0.0759 298 GLU B OE1 
4608 O  OE2 . GLU B 322 ? 1.0241 0.8105 0.9640 0.0212  0.0444  -0.0864 298 GLU B OE2 
4609 N  N   . LEU B 323 ? 0.5774 0.4245 0.5283 0.0318  0.0473  -0.0545 299 LEU B N   
4610 C  CA  . LEU B 323 ? 0.5879 0.4454 0.5329 0.0273  0.0437  -0.0533 299 LEU B CA  
4611 C  C   . LEU B 323 ? 0.5651 0.4331 0.5082 0.0306  0.0470  -0.0524 299 LEU B C   
4612 O  O   . LEU B 323 ? 0.5430 0.4162 0.4783 0.0277  0.0459  -0.0542 299 LEU B O   
4613 C  CB  . LEU B 323 ? 0.5473 0.4117 0.4987 0.0244  0.0391  -0.0457 299 LEU B CB  
4614 C  CG  . LEU B 323 ? 0.6189 0.4761 0.5707 0.0194  0.0349  -0.0459 299 LEU B CG  
4615 C  CD1 . LEU B 323 ? 0.5394 0.4031 0.4992 0.0189  0.0323  -0.0375 299 LEU B CD1 
4616 C  CD2 . LEU B 323 ? 0.5974 0.4554 0.5401 0.0135  0.0312  -0.0502 299 LEU B CD2 
4617 N  N   . LEU B 324 ? 0.5431 0.4145 0.4938 0.0365  0.0512  -0.0490 300 LEU B N   
4618 C  CA  . LEU B 324 ? 0.5483 0.4311 0.5001 0.0395  0.0544  -0.0467 300 LEU B CA  
4619 C  C   . LEU B 324 ? 0.5378 0.4172 0.4859 0.0448  0.0611  -0.0519 300 LEU B C   
4620 O  O   . LEU B 324 ? 0.5161 0.4051 0.4648 0.0474  0.0645  -0.0501 300 LEU B O   
4621 C  CB  . LEU B 324 ? 0.5090 0.4013 0.4729 0.0424  0.0542  -0.0386 300 LEU B CB  
4622 C  CG  . LEU B 324 ? 0.5291 0.4262 0.4967 0.0380  0.0480  -0.0334 300 LEU B CG  
4623 C  CD1 . LEU B 324 ? 0.4852 0.3920 0.4638 0.0413  0.0478  -0.0262 300 LEU B CD1 
4624 C  CD2 . LEU B 324 ? 0.4733 0.3766 0.4347 0.0324  0.0444  -0.0339 300 LEU B CD2 
4625 N  N   . ALA B 325 ? 0.5561 0.4221 0.5009 0.0466  0.0633  -0.0583 301 ALA B N   
4626 C  CA  . ALA B 325 ? 0.5530 0.4144 0.4929 0.0519  0.0699  -0.0648 301 ALA B CA  
4627 C  C   . ALA B 325 ? 0.5526 0.4193 0.5029 0.0595  0.0757  -0.0604 301 ALA B C   
4628 O  O   . ALA B 325 ? 0.6011 0.4738 0.5491 0.0636  0.0811  -0.0617 301 ALA B O   
4629 C  CB  . ALA B 325 ? 0.5492 0.4165 0.4767 0.0499  0.0708  -0.0688 301 ALA B CB  
4630 N  N   . LEU B 326 ? 0.5546 0.4198 0.5167 0.0617  0.0748  -0.0547 302 LEU B N   
4631 C  CA  . LEU B 326 ? 0.5426 0.4143 0.5161 0.0690  0.0795  -0.0493 302 LEU B CA  
4632 C  C   . LEU B 326 ? 0.5933 0.4527 0.5686 0.0757  0.0859  -0.0545 302 LEU B C   
4633 O  O   . LEU B 326 ? 0.5630 0.4075 0.5326 0.0743  0.0857  -0.0617 302 LEU B O   
4634 C  CB  . LEU B 326 ? 0.5282 0.4060 0.5135 0.0686  0.0753  -0.0400 302 LEU B CB  
4635 C  CG  . LEU B 326 ? 0.5143 0.4033 0.4982 0.0620  0.0689  -0.0355 302 LEU B CG  
4636 C  CD1 . LEU B 326 ? 0.4780 0.3736 0.4728 0.0624  0.0652  -0.0270 302 LEU B CD1 
4637 C  CD2 . LEU B 326 ? 0.4326 0.3346 0.4146 0.0617  0.0706  -0.0348 302 LEU B CD2 
4638 N  N   . LYS B 327 ? 0.5669 0.4328 0.5511 0.0832  0.0916  -0.0509 303 LYS B N   
4639 C  CA  . LYS B 327 ? 0.5808 0.4366 0.5668 0.0908  0.0989  -0.0561 303 LYS B CA  
4640 C  C   . LYS B 327 ? 0.5911 0.4362 0.5883 0.0944  0.0991  -0.0532 303 LYS B C   
4641 O  O   . LYS B 327 ? 0.6268 0.4595 0.6250 0.1000  0.1047  -0.0589 303 LYS B O   
4642 C  CB  . LYS B 327 ? 0.5762 0.4446 0.5676 0.0977  0.1057  -0.0532 303 LYS B CB  
4643 C  CG  . LYS B 327 ? 0.5810 0.4642 0.5878 0.1001  0.1043  -0.0416 303 LYS B CG  
4644 C  CD  . LYS B 327 ? 0.5360 0.4307 0.5495 0.1075  0.1116  -0.0392 303 LYS B CD  
4645 C  CE  . LYS B 327 ? 0.5537 0.4658 0.5818 0.1085  0.1092  -0.0280 303 LYS B CE  
4646 N  NZ  . LYS B 327 ? 0.5124 0.4354 0.5497 0.1163  0.1166  -0.0250 303 LYS B NZ  
4647 N  N   . GLY B 328 ? 0.5897 0.4392 0.5951 0.0918  0.0936  -0.0445 304 GLY B N   
4648 C  CA  . GLY B 328 ? 0.5550 0.3952 0.5713 0.0952  0.0938  -0.0402 304 GLY B CA  
4649 C  C   . GLY B 328 ? 0.5587 0.4122 0.5895 0.1010  0.0947  -0.0291 304 GLY B C   
4650 O  O   . GLY B 328 ? 0.5543 0.4191 0.5889 0.1058  0.0988  -0.0273 304 GLY B O   
4651 N  N   . GLY B 329 ? 0.5592 0.4121 0.5986 0.1005  0.0908  -0.0211 305 GLY B N   
4652 C  CA  . GLY B 329 ? 0.5542 0.4207 0.6069 0.1055  0.0904  -0.0099 305 GLY B CA  
4653 C  C   . GLY B 329 ? 0.5852 0.4493 0.6492 0.1157  0.0976  -0.0078 305 GLY B C   
4654 O  O   . GLY B 329 ? 0.5955 0.4734 0.6709 0.1205  0.0978  0.0012  305 GLY B O   
4655 N  N   . ASP B 330 ? 0.5953 0.4425 0.6567 0.1191  0.1035  -0.0162 306 ASP B N   
4656 C  CA  . ASP B 330 ? 0.6312 0.4744 0.7032 0.1295  0.1112  -0.0153 306 ASP B CA  
4657 C  C   . ASP B 330 ? 0.6173 0.4660 0.6851 0.1337  0.1178  -0.0217 306 ASP B C   
4658 O  O   . ASP B 330 ? 0.6065 0.4542 0.6833 0.1429  0.1249  -0.0209 306 ASP B O   
4659 C  CB  . ASP B 330 ? 0.6038 0.4237 0.6773 0.1317  0.1143  -0.0206 306 ASP B CB  
4660 C  CG  . ASP B 330 ? 0.7807 0.5966 0.8652 0.1319  0.1108  -0.0106 306 ASP B CG  
4661 O  OD1 . ASP B 330 ? 0.7940 0.6248 0.8892 0.1352  0.1089  0.0013  306 ASP B OD1 
4662 O  OD2 . ASP B 330 ? 0.8237 0.6221 0.9066 0.1286  0.1097  -0.0144 306 ASP B OD2 
4663 N  N   . GLN B 331 ? 0.6142 0.4690 0.6690 0.1275  0.1159  -0.0274 307 GLN B N   
4664 C  CA  . GLN B 331 ? 0.6461 0.5082 0.6962 0.1309  0.1221  -0.0325 307 GLN B CA  
4665 C  C   . GLN B 331 ? 0.6140 0.4991 0.6695 0.1301  0.1201  -0.0242 307 GLN B C   
4666 O  O   . GLN B 331 ? 0.5944 0.4880 0.6416 0.1267  0.1206  -0.0274 307 GLN B O   
4667 C  CB  . GLN B 331 ? 0.6352 0.4883 0.6670 0.1252  0.1220  -0.0444 307 GLN B CB  
4668 C  CG  . GLN B 331 ? 0.6913 0.5215 0.7175 0.1260  0.1242  -0.0543 307 GLN B CG  
4669 C  CD  . GLN B 331 ? 0.7186 0.5422 0.7306 0.1272  0.1296  -0.0671 307 GLN B CD  
4670 O  OE1 . GLN B 331 ? 0.6928 0.5166 0.7072 0.1355  0.1379  -0.0701 307 GLN B OE1 
4671 N  NE2 . GLN B 331 ? 0.7512 0.5695 0.7482 0.1190  0.1250  -0.0745 307 GLN B NE2 
4672 N  N   . VAL B 332 ? 0.5780 0.4738 0.6482 0.1330  0.1177  -0.0133 308 VAL B N   
4673 C  CA  . VAL B 332 ? 0.5707 0.4887 0.6484 0.1321  0.1152  -0.0052 308 VAL B CA  
4674 C  C   . VAL B 332 ? 0.5653 0.4923 0.6593 0.1422  0.1210  0.0015  308 VAL B C   
4675 O  O   . VAL B 332 ? 0.5945 0.5098 0.6935 0.1497  0.1268  0.0000  308 VAL B O   
4676 C  CB  . VAL B 332 ? 0.5385 0.4642 0.6182 0.1253  0.1056  0.0019  308 VAL B CB  
4677 C  CG1 . VAL B 332 ? 0.5340 0.4529 0.5983 0.1156  0.1002  -0.0043 308 VAL B CG1 
4678 C  CG2 . VAL B 332 ? 0.5346 0.4538 0.6236 0.1290  0.1038  0.0084  308 VAL B CG2 
4679 N  N   . ASN B 333 ? 0.5346 0.4824 0.6377 0.1423  0.1193  0.0089  309 ASN B N   
4680 C  CA  . ASN B 333 ? 0.5557 0.5151 0.6757 0.1515  0.1242  0.0162  309 ASN B CA  
4681 C  C   . ASN B 333 ? 0.5317 0.5030 0.6646 0.1518  0.1173  0.0276  309 ASN B C   
4682 O  O   . ASN B 333 ? 0.5435 0.5348 0.6876 0.1528  0.1157  0.0348  309 ASN B O   
4683 C  CB  . ASN B 333 ? 0.5533 0.5291 0.6762 0.1525  0.1284  0.0165  309 ASN B CB  
4684 C  CG  . ASN B 333 ? 0.5799 0.5656 0.7195 0.1631  0.1355  0.0223  309 ASN B CG  
4685 O  OD1 . ASN B 333 ? 0.5626 0.5379 0.7082 0.1711  0.1401  0.0227  309 ASN B OD1 
4686 N  ND2 . ASN B 333 ? 0.5582 0.5641 0.7062 0.1633  0.1366  0.0270  309 ASN B ND2 
4687 N  N   . PHE B 334 ? 0.5496 0.5093 0.6810 0.1506  0.1132  0.0294  310 PHE B N   
4688 C  CA  . PHE B 334 ? 0.5560 0.5257 0.6990 0.1521  0.1075  0.0405  310 PHE B CA  
4689 C  C   . PHE B 334 ? 0.5817 0.5337 0.7233 0.1532  0.1064  0.0414  310 PHE B C   
4690 O  O   . PHE B 334 ? 0.6192 0.5763 0.7697 0.1555  0.1026  0.0510  310 PHE B O   
4691 C  CB  . PHE B 334 ? 0.4941 0.4799 0.6344 0.1435  0.0981  0.0440  310 PHE B CB  
4692 C  CG  . PHE B 334 ? 0.5105 0.4866 0.6341 0.1336  0.0936  0.0366  310 PHE B CG  
4693 C  CD1 . PHE B 334 ? 0.5143 0.4804 0.6326 0.1300  0.0886  0.0377  310 PHE B CD1 
4694 C  CD2 . PHE B 334 ? 0.5270 0.5048 0.6411 0.1282  0.0944  0.0294  310 PHE B CD2 
4695 C  CE1 . PHE B 334 ? 0.5116 0.4698 0.6156 0.1212  0.0845  0.0313  310 PHE B CE1 
4696 C  CE2 . PHE B 334 ? 0.5031 0.4727 0.6027 0.1195  0.0901  0.0232  310 PHE B CE2 
4697 C  CZ  . PHE B 334 ? 0.4790 0.4389 0.5737 0.1161  0.0851  0.0240  310 PHE B CZ  
4698 O  OXT . PHE B 334 ? 0.5934 0.5257 0.7250 0.1516  0.1094  0.0328  310 PHE B OXT 
4699 N  N1A . ACO C .   ? 0.7454 0.6244 0.7372 -0.0314 -0.0007 -0.0060 401 ACO A N1A 
4700 C  C2A . ACO C .   ? 0.7755 0.6467 0.7649 -0.0354 -0.0031 -0.0131 401 ACO A C2A 
4701 N  N3A . ACO C .   ? 0.7687 0.6406 0.7591 -0.0410 -0.0068 -0.0156 401 ACO A N3A 
4702 C  C4A . ACO C .   ? 0.7285 0.6103 0.7236 -0.0423 -0.0076 -0.0094 401 ACO A C4A 
4703 C  C5A . ACO C .   ? 0.7548 0.6448 0.7522 -0.0384 -0.0049 -0.0020 401 ACO A C5A 
4704 C  C6A . ACO C .   ? 0.7473 0.6358 0.7425 -0.0328 -0.0016 -0.0004 401 ACO A C6A 
4705 N  N6A . ACO C .   ? 0.7412 0.6378 0.7375 -0.0286 0.0007  0.0060  401 ACO A N6A 
4706 N  N7A . ACO C .   ? 0.6805 0.5797 0.6823 -0.0409 -0.0062 0.0025  401 ACO A N7A 
4707 C  C8A . ACO C .   ? 0.6886 0.5852 0.6913 -0.0464 -0.0099 -0.0017 401 ACO A C8A 
4708 N  N9A . ACO C .   ? 0.6901 0.5763 0.6883 -0.0476 -0.0111 -0.0093 401 ACO A N9A 
4709 C  C1B . ACO C .   ? 0.6811 0.5624 0.6780 -0.0531 -0.0153 -0.0161 401 ACO A C1B 
4710 C  C2B . ACO C .   ? 0.6696 0.5465 0.6772 -0.0593 -0.0173 -0.0146 401 ACO A C2B 
4711 O  O2B . ACO C .   ? 0.6460 0.5099 0.6576 -0.0595 -0.0154 -0.0164 401 ACO A O2B 
4712 C  C3B . ACO C .   ? 0.6543 0.5327 0.6579 -0.0644 -0.0227 -0.0213 401 ACO A C3B 
4713 O  O3B . ACO C .   ? 0.6876 0.5560 0.6832 -0.0643 -0.0235 -0.0304 401 ACO A O3B 
4714 P  P3B . ACO C .   ? 0.6797 0.5458 0.6736 -0.0712 -0.0296 -0.0383 401 ACO A P3B 
4715 O  O7A . ACO C .   ? 0.6629 0.5413 0.6509 -0.0717 -0.0330 -0.0381 401 ACO A O7A 
4716 O  O8A . ACO C .   ? 0.6960 0.5591 0.7033 -0.0775 -0.0317 -0.0357 401 ACO A O8A 
4717 O  O9A . ACO C .   ? 0.7309 0.5852 0.7162 -0.0697 -0.0289 -0.0476 401 ACO A O9A 
4718 C  C4B . ACO C .   ? 0.6679 0.5586 0.6651 -0.0612 -0.0230 -0.0193 401 ACO A C4B 
4719 O  O4B . ACO C .   ? 0.6996 0.5906 0.6925 -0.0545 -0.0183 -0.0170 401 ACO A O4B 
4720 C  C5B . ACO C .   ? 0.6325 0.5348 0.6375 -0.0629 -0.0238 -0.0121 401 ACO A C5B 
4721 O  O5B . ACO C .   ? 0.6119 0.5236 0.6121 -0.0576 -0.0217 -0.0090 401 ACO A O5B 
4722 P  P1A . ACO C .   ? 0.6168 0.5371 0.6118 -0.0582 -0.0251 -0.0111 401 ACO A P1A 
4723 O  O1A . ACO C .   ? 0.6915 0.6059 0.6765 -0.0585 -0.0272 -0.0189 401 ACO A O1A 
4724 O  O2A . ACO C .   ? 0.5608 0.4906 0.5553 -0.0533 -0.0225 -0.0063 401 ACO A O2A 
4725 O  O3A . ACO C .   ? 0.6471 0.5718 0.6515 -0.0646 -0.0292 -0.0091 401 ACO A O3A 
4726 P  P2A . ACO C .   ? 0.6491 0.5801 0.6540 -0.0695 -0.0352 -0.0115 401 ACO A P2A 
4727 O  O4A . ACO C .   ? 0.6668 0.5925 0.6603 -0.0697 -0.0378 -0.0195 401 ACO A O4A 
4728 O  O5A . ACO C .   ? 0.5840 0.5157 0.6008 -0.0757 -0.0377 -0.0091 401 ACO A O5A 
4729 O  O6A . ACO C .   ? 0.5865 0.5301 0.5916 -0.0656 -0.0341 -0.0063 401 ACO A O6A 
4730 C  CBP . ACO C .   ? 0.5403 0.5021 0.5535 -0.0604 -0.0306 0.0041  401 ACO A CBP 
4731 C  CCP . ACO C .   ? 0.5475 0.4984 0.5615 -0.0639 -0.0309 0.0012  401 ACO A CCP 
4732 C  CDP . ACO C .   ? 0.5128 0.4722 0.5161 -0.0545 -0.0277 0.0017  401 ACO A CDP 
4733 C  CEP . ACO C .   ? 0.5325 0.4992 0.5455 -0.0641 -0.0363 0.0021  401 ACO A CEP 
4734 C  CAP . ACO C .   ? 0.5281 0.4987 0.5511 -0.0590 -0.0276 0.0115  401 ACO A CAP 
4735 O  OAP . ACO C .   ? 0.4654 0.4312 0.4895 -0.0572 -0.0233 0.0137  401 ACO A OAP 
4736 C  C9P . ACO C .   ? 0.4916 0.4711 0.5133 -0.0538 -0.0254 0.0140  401 ACO A C9P 
4737 O  O9P . ACO C .   ? 0.4628 0.4480 0.4849 -0.0543 -0.0283 0.0137  401 ACO A O9P 
4738 N  N8P . ACO C .   ? 0.4665 0.4472 0.4869 -0.0487 -0.0205 0.0163  401 ACO A N8P 
4739 C  C7P . ACO C .   ? 0.4094 0.3986 0.4304 -0.0437 -0.0178 0.0187  401 ACO A C7P 
4740 C  C6P . ACO C .   ? 0.4112 0.4111 0.4426 -0.0448 -0.0177 0.0242  401 ACO A C6P 
4741 C  C5P . ACO C .   ? 0.4217 0.4293 0.4531 -0.0394 -0.0154 0.0253  401 ACO A C5P 
4742 O  O5P . ACO C .   ? 0.4447 0.4566 0.4782 -0.0396 -0.0179 0.0253  401 ACO A O5P 
4743 N  N4P . ACO C .   ? 0.4319 0.4417 0.4614 -0.0344 -0.0105 0.0265  401 ACO A N4P 
4744 C  C3P . ACO C .   ? 0.4289 0.4431 0.4561 -0.0288 -0.0081 0.0253  401 ACO A C3P 
4745 C  C2P . ACO C .   ? 0.4576 0.4829 0.4931 -0.0264 -0.0050 0.0303  401 ACO A C2P 
4746 S  S1P . ACO C .   ? 0.5110 0.5436 0.5526 -0.0247 -0.0065 0.0311  401 ACO A S1P 
4747 C  C   . ACO C .   ? 0.4682 0.5145 0.5217 -0.0228 -0.0031 0.0378  401 ACO A C   
4748 O  O   . ACO C .   ? 0.4789 0.5292 0.5346 -0.0220 0.0005  0.0411  401 ACO A O   
4749 C  CH3 . ACO C .   ? 0.4407 0.4938 0.5015 -0.0218 -0.0047 0.0396  401 ACO A CH3 
4750 O  O1  . AAE D .   ? 0.3609 0.4229 0.4116 -0.0072 0.0128  0.0398  402 AAE A O1  
4751 C  C2  . AAE D .   ? 0.4027 0.4612 0.4511 -0.0049 0.0114  0.0352  402 AAE A C2  
4752 O  O3  . AAE D .   ? 0.4095 0.4736 0.4623 -0.0005 0.0138  0.0351  402 AAE A O3  
4753 C  C4  . AAE D .   ? 0.4419 0.4884 0.4821 -0.0072 0.0072  0.0295  402 AAE A C4  
4754 C  C5  . AAE D .   ? 0.4334 0.4723 0.4667 -0.0106 0.0056  0.0283  402 AAE A C5  
4755 O  O8  . AAE D .   ? 0.4144 0.4556 0.4490 -0.0123 0.0071  0.0321  402 AAE A O8  
4756 C  C9  . AAE D .   ? 0.4174 0.4460 0.4427 -0.0115 0.0026  0.0225  402 AAE A C9  
4757 ZN ZN  . ZN  E .   ? 0.3935 0.4484 0.4407 -0.0135 0.0109  0.0422  403 ZN  A ZN  
4758 N  N1A . ACO F .   ? 1.0622 1.1544 1.0021 0.0251  -0.0313 -0.0248 401 ACO B N1A 
4759 C  C2A . ACO F .   ? 1.0998 1.2000 1.0371 0.0243  -0.0358 -0.0335 401 ACO B C2A 
4760 N  N3A . ACO F .   ? 1.1078 1.2109 1.0508 0.0218  -0.0402 -0.0396 401 ACO B N3A 
4761 C  C4A . ACO F .   ? 1.0838 1.1810 1.0358 0.0203  -0.0392 -0.0354 401 ACO B C4A 
4762 C  C5A . ACO F .   ? 1.0358 1.1244 0.9905 0.0214  -0.0345 -0.0270 401 ACO B C5A 
4763 C  C6A . ACO F .   ? 1.0465 1.1322 0.9949 0.0237  -0.0306 -0.0217 401 ACO B C6A 
4764 N  N6A . ACO F .   ? 0.9558 1.0329 0.9064 0.0244  -0.0263 -0.0142 401 ACO B N6A 
4765 N  N7A . ACO F .   ? 0.9647 1.0495 0.9287 0.0198  -0.0346 -0.0255 401 ACO B N7A 
4766 C  C8A . ACO F .   ? 0.9888 1.0802 0.9564 0.0176  -0.0392 -0.0323 401 ACO B C8A 
4767 N  N9A . ACO F .   ? 1.0588 1.1574 1.0194 0.0176  -0.0424 -0.0389 401 ACO B N9A 
4768 C  C1B . ACO F .   ? 1.0842 1.1907 1.0466 0.0151  -0.0481 -0.0481 401 ACO B C1B 
4769 C  C2B . ACO F .   ? 1.0493 1.1723 1.0116 0.0171  -0.0536 -0.0467 401 ACO B C2B 
4770 O  O2B . ACO F .   ? 1.0436 1.1772 0.9945 0.0209  -0.0552 -0.0461 401 ACO B O2B 
4771 C  C3B . ACO F .   ? 1.0807 1.2055 1.0503 0.0123  -0.0585 -0.0568 401 ACO B C3B 
4772 O  O3B . ACO F .   ? 1.1129 1.2373 1.0756 0.0111  -0.0602 -0.0666 401 ACO B O3B 
4773 P  P3B . ACO F .   ? 1.1729 1.2982 1.1437 0.0056  -0.0655 -0.0783 401 ACO B P3B 
4774 O  O7A . ACO F .   ? 1.1586 1.2687 1.1398 0.0016  -0.0617 -0.0788 401 ACO B O7A 
4775 O  O8A . ACO F .   ? 1.1482 1.2878 1.1249 0.0052  -0.0714 -0.0769 401 ACO B O8A 
4776 O  O9A . ACO F .   ? 1.1314 1.2591 1.0926 0.0059  -0.0677 -0.0884 401 ACO B O9A 
4777 C  C4B . ACO F .   ? 1.0534 1.1637 1.0327 0.0091  -0.0542 -0.0554 401 ACO B C4B 
4778 O  O4B . ACO F .   ? 1.0745 1.1737 1.0475 0.0107  -0.0483 -0.0518 401 ACO B O4B 
4779 C  C5B . ACO F .   ? 1.0083 1.1199 0.9967 0.0097  -0.0532 -0.0476 401 ACO B C5B 
4780 O  O5B . ACO F .   ? 1.0018 1.0988 0.9953 0.0080  -0.0476 -0.0451 401 ACO B O5B 
4781 P  P1A . ACO F .   ? 1.0516 1.1420 1.0555 0.0025  -0.0479 -0.0511 401 ACO B P1A 
4782 O  O1A . ACO F .   ? 1.0451 1.1330 1.0461 -0.0003 -0.0503 -0.0607 401 ACO B O1A 
4783 O  O2A . ACO F .   ? 0.8447 0.9232 0.8527 0.0021  -0.0421 -0.0458 401 ACO B O2A 
4784 O  O3A . ACO F .   ? 1.0533 1.1571 1.0665 0.0016  -0.0531 -0.0511 401 ACO B O3A 
4785 P  P2A . ACO F .   ? 1.0499 1.1573 1.0771 -0.0035 -0.0565 -0.0557 401 ACO B P2A 
4786 O  O4A . ACO F .   ? 1.0680 1.1694 1.0959 -0.0080 -0.0583 -0.0655 401 ACO B O4A 
4787 O  O5A . ACO F .   ? 1.0052 1.1291 1.0371 -0.0024 -0.0619 -0.0540 401 ACO B O5A 
4788 O  O6A . ACO F .   ? 1.0018 1.0996 1.0367 -0.0038 -0.0503 -0.0492 401 ACO B O6A 
4789 C  CBP . ACO F .   ? 0.8011 0.8940 0.8460 -0.0009 -0.0422 -0.0366 401 ACO B CBP 
4790 C  CCP . ACO F .   ? 0.8865 0.9878 0.9230 0.0004  -0.0475 -0.0402 401 ACO B CCP 
4791 C  CDP . ACO F .   ? 0.7086 0.7859 0.7465 -0.0014 -0.0369 -0.0369 401 ACO B CDP 
4792 C  CEP . ACO F .   ? 0.8435 0.9399 0.9011 -0.0063 -0.0450 -0.0413 401 ACO B CEP 
4793 C  CAP . ACO F .   ? 0.6998 0.7971 0.7482 0.0036  -0.0394 -0.0281 401 ACO B CAP 
4794 O  OAP . ACO F .   ? 0.7054 0.8008 0.7433 0.0083  -0.0379 -0.0241 401 ACO B OAP 
4795 C  C9P . ACO F .   ? 0.6880 0.7763 0.7418 0.0034  -0.0331 -0.0245 401 ACO B C9P 
4796 O  O9P . ACO F .   ? 0.7000 0.7887 0.7634 -0.0003 -0.0328 -0.0262 401 ACO B O9P 
4797 N  N8P . ACO F .   ? 0.6680 0.7485 0.7158 0.0074  -0.0279 -0.0194 401 ACO B N8P 
4798 C  C7P . ACO F .   ? 0.6436 0.7160 0.6946 0.0082  -0.0217 -0.0159 401 ACO B C7P 
4799 C  C6P . ACO F .   ? 0.6315 0.7132 0.6945 0.0096  -0.0209 -0.0121 401 ACO B C6P 
4800 C  C5P . ACO F .   ? 0.6861 0.7597 0.7515 0.0105  -0.0140 -0.0093 401 ACO B C5P 
4801 O  O5P . ACO F .   ? 0.7344 0.8102 0.8087 0.0076  -0.0127 -0.0097 401 ACO B O5P 
4802 N  N4P . ACO F .   ? 0.6368 0.7010 0.6944 0.0143  -0.0093 -0.0065 401 ACO B N4P 
4803 C  C3P . ACO F .   ? 0.6379 0.6944 0.6959 0.0160  -0.0026 -0.0043 401 ACO B C3P 
4804 C  C2P . ACO F .   ? 0.6457 0.7111 0.7151 0.0187  -0.0002 -0.0003 401 ACO B C2P 
4805 S  S1P . ACO F .   ? 0.7279 0.7927 0.8049 0.0154  0.0043  -0.0006 401 ACO B S1P 
4806 C  C   . ACO F .   ? 0.7009 0.7783 0.7935 0.0176  0.0072  0.0040  401 ACO B C   
4807 O  O   . ACO F .   ? 0.6894 0.7769 0.7891 0.0208  0.0054  0.0071  401 ACO B O   
4808 C  CH3 . ACO F .   ? 0.6756 0.7507 0.7721 0.0154  0.0123  0.0046  401 ACO B CH3 
4809 O  O1  . AAE G .   ? 0.4268 0.4832 0.5048 0.0366  0.0245  0.0111  402 AAE B O1  
4810 C  C2  . AAE G .   ? 0.4820 0.5347 0.5576 0.0331  0.0266  0.0088  402 AAE B C2  
4811 O  O3  . AAE G .   ? 0.4710 0.5265 0.5517 0.0344  0.0318  0.0103  402 AAE B O3  
4812 C  C4  . AAE G .   ? 0.5419 0.5866 0.6079 0.0273  0.0232  0.0045  402 AAE B C4  
4813 C  C5  . AAE G .   ? 0.4900 0.5308 0.5487 0.0265  0.0180  0.0028  402 AAE B C5  
4814 O  O8  . AAE G .   ? 0.4433 0.4874 0.5034 0.0299  0.0162  0.0051  402 AAE B O8  
4815 C  C9  . AAE G .   ? 0.5108 0.5436 0.5606 0.0215  0.0156  -0.0013 402 AAE B C9  
4816 ZN ZN  . ZN  H .   ? 0.4276 0.4866 0.5019 0.0374  0.0165  0.0122  403 ZN  B ZN  
4817 O  O   . HOH I .   ? 0.4192 0.4610 0.4227 0.0039  0.0175  0.0208  501 HOH A O   
4818 O  O   . HOH I .   ? 0.4198 0.5691 0.6132 -0.0602 -0.0103 0.1025  502 HOH A O   
4819 O  O   . HOH I .   ? 0.5191 0.6990 0.7125 -0.0122 0.0004  0.0991  503 HOH A O   
4820 O  O   . HOH I .   ? 0.5405 0.4914 0.5479 -0.0120 -0.0037 -0.0084 504 HOH A O   
4821 O  O   . HOH I .   ? 0.3135 0.4408 0.4338 -0.0171 0.0273  0.0878  505 HOH A O   
4822 O  O   . HOH I .   ? 0.5192 0.6745 0.6110 -0.0003 0.0802  0.1807  506 HOH A O   
4823 O  O   . HOH I .   ? 0.5779 0.5259 0.6061 -0.0057 -0.0024 -0.0084 507 HOH A O   
4824 O  O   . HOH I .   ? 0.4248 0.6579 0.5015 0.0409  0.1031  0.1335  508 HOH A O   
4825 O  O   . HOH I .   ? 0.4579 0.4885 0.4424 0.0067  0.0145  0.0094  509 HOH A O   
4826 O  O   . HOH I .   ? 0.5859 0.6910 0.5407 0.0829  0.0659  -0.0597 510 HOH A O   
4827 O  O   . HOH I .   ? 0.3326 0.4001 0.4138 0.0237  0.0186  0.0284  511 HOH A O   
4828 O  O   . HOH I .   ? 0.5103 0.5807 0.4519 0.0362  -0.0055 0.0356  512 HOH A O   
4829 O  O   . HOH I .   ? 0.5597 0.4799 0.5329 -0.0174 0.0004  -0.0026 513 HOH A O   
4830 O  O   . HOH I .   ? 0.5819 0.5020 0.5824 -0.0349 -0.0036 0.0114  514 HOH A O   
4831 O  O   . HOH I .   ? 0.5105 0.6234 0.4557 0.0355  0.0405  0.0669  515 HOH A O   
4832 O  O   . HOH I .   ? 0.4836 0.5476 0.5009 0.0105  0.0455  0.1315  516 HOH A O   
4833 O  O   . HOH I .   ? 0.4711 0.6693 0.6458 0.0142  0.0485  0.1032  517 HOH A O   
4834 O  O   . HOH I .   ? 0.5366 0.4510 0.6420 -0.1056 -0.0342 0.0204  518 HOH A O   
4835 O  O   . HOH I .   ? 0.4901 0.4937 0.5200 -0.0503 -0.0288 0.0196  519 HOH A O   
4836 O  O   . HOH I .   ? 0.5527 0.4892 0.5851 -0.0723 -0.0296 0.0049  520 HOH A O   
4837 O  O   . HOH I .   ? 0.6039 0.5743 0.6447 0.0572  0.0337  -0.0934 521 HOH A O   
4838 O  O   . HOH I .   ? 0.4347 0.4406 0.5349 -0.0468 0.0243  0.1084  522 HOH A O   
4839 O  O   . HOH I .   ? 0.4724 0.4943 0.5195 -0.0052 -0.0181 0.0319  523 HOH A O   
4840 O  O   . HOH I .   ? 0.3473 0.3940 0.4108 -0.0332 -0.0031 0.0468  524 HOH A O   
4841 O  O   . HOH I .   ? 0.4841 0.5376 0.4682 0.0165  0.0240  0.0124  525 HOH A O   
4842 O  O   . HOH I .   ? 0.5384 0.6445 0.4700 0.0800  0.0586  -0.0686 526 HOH A O   
4843 O  O   . HOH I .   ? 0.3144 0.3770 0.3697 -0.0186 0.0206  0.0644  527 HOH A O   
4844 O  O   . HOH I .   ? 0.4669 0.5151 0.4311 0.0441  0.0291  -0.0520 528 HOH A O   
4845 O  O   . HOH I .   ? 0.5495 0.4918 0.5819 -0.0079 -0.0017 -0.0193 529 HOH A O   
4846 O  O   . HOH I .   ? 0.5784 0.5115 0.5380 -0.0246 -0.0083 -0.0147 530 HOH A O   
4847 O  O   . HOH I .   ? 0.5821 0.8279 0.5213 0.1002  0.1155  0.0446  531 HOH A O   
4848 O  O   . HOH I .   ? 0.4861 0.4383 0.5716 0.0260  0.0110  -0.0072 532 HOH A O   
4849 O  O   . HOH I .   ? 0.5496 0.5928 0.5119 0.0355  0.0091  0.0698  533 HOH A O   
4850 O  O   . HOH I .   ? 0.4005 0.3512 0.4799 -0.0641 -0.0028 0.0556  534 HOH A O   
4851 O  O   . HOH I .   ? 0.4581 0.5405 0.3860 0.0358  0.0086  0.0428  535 HOH A O   
4852 O  O   . HOH I .   ? 0.4722 0.6082 0.7374 -0.1357 -0.0611 0.0974  536 HOH A O   
4853 O  O   . HOH I .   ? 0.3903 0.4528 0.5137 -0.0696 -0.0204 0.0661  537 HOH A O   
4854 O  O   . HOH I .   ? 0.4730 0.5293 0.5871 -0.0377 0.0416  0.1395  538 HOH A O   
4855 O  O   . HOH I .   ? 0.3613 0.4989 0.4522 0.0281  0.0492  0.0586  539 HOH A O   
4856 O  O   . HOH I .   ? 0.3964 0.4705 0.4699 0.0164  0.0187  0.0321  540 HOH A O   
4857 O  O   . HOH I .   ? 0.4526 0.6718 0.4919 0.0350  0.1033  0.1847  541 HOH A O   
4858 O  O   . HOH I .   ? 0.6084 0.5386 0.5828 -0.0216 -0.0027 -0.0015 542 HOH A O   
4859 O  O   . HOH I .   ? 0.4991 0.5312 0.4581 0.0150  -0.0149 -0.0161 543 HOH A O   
4860 O  O   . HOH I .   ? 0.4414 0.6301 0.6489 -0.0389 0.0465  0.1514  544 HOH A O   
4861 O  O   . HOH I .   ? 0.6544 0.8353 0.8133 0.0709  0.0732  0.0626  545 HOH A O   
4862 O  O   . HOH I .   ? 0.5964 0.7916 0.5657 0.1066  0.1084  -0.0068 546 HOH A O   
4863 O  O   . HOH I .   ? 0.4067 0.5185 0.5322 -0.0134 -0.0158 0.0669  547 HOH A O   
4864 O  O   . HOH I .   ? 0.3783 0.4106 0.3449 0.0123  0.0137  0.0021  548 HOH A O   
4865 O  O   . HOH I .   ? 0.5288 0.7081 0.4830 0.0561  0.0750  0.0723  549 HOH A O   
4866 O  O   . HOH I .   ? 0.4383 0.4553 0.3940 0.0090  -0.0118 -0.0298 550 HOH A O   
4867 O  O   . HOH I .   ? 0.4599 0.5965 0.6306 0.0357  0.0168  0.0745  551 HOH A O   
4868 O  O   . HOH I .   ? 0.4297 0.5850 0.3944 0.0552  0.0685  0.0408  552 HOH A O   
4869 O  O   . HOH I .   ? 0.4020 0.4387 0.3885 0.0405  0.0288  -0.0431 553 HOH A O   
4870 O  O   . HOH I .   ? 0.5751 0.7427 0.7628 0.0303  0.0215  0.0863  554 HOH A O   
4871 O  O   . HOH I .   ? 0.5141 0.6356 0.4077 0.0461  0.0092  0.0143  555 HOH A O   
4872 O  O   . HOH I .   ? 0.4043 0.5529 0.3895 0.0530  0.0684  0.0377  556 HOH A O   
4873 O  O   . HOH I .   ? 0.4248 0.5810 0.5125 -0.0619 -0.1045 0.0727  557 HOH A O   
4874 O  O   . HOH I .   ? 0.5829 0.5400 0.6032 -0.0082 0.0194  0.0722  558 HOH A O   
4875 O  O   . HOH I .   ? 0.5697 0.7267 0.4310 0.0730  0.0383  -0.0418 559 HOH A O   
4876 O  O   . HOH I .   ? 0.3333 0.4297 0.4559 -0.0412 0.0080  0.0830  560 HOH A O   
4877 O  O   . HOH I .   ? 0.5550 0.4928 0.5099 -0.0220 -0.0080 -0.0172 561 HOH A O   
4878 O  O   . HOH I .   ? 0.4903 0.5930 0.4214 0.0365  0.0296  0.0496  562 HOH A O   
4879 O  O   . HOH I .   ? 0.3493 0.3474 0.3347 -0.0373 -0.0380 0.0110  563 HOH A O   
4880 O  O   . HOH I .   ? 0.4762 0.4230 0.5026 -0.0092 -0.0049 -0.0418 564 HOH A O   
4881 O  O   . HOH I .   ? 0.4912 0.6608 0.3741 0.0637  0.0443  0.0331  565 HOH A O   
4882 O  O   . HOH I .   ? 0.3809 0.4507 0.3229 0.0260  0.0206  0.0267  566 HOH A O   
4883 O  O   . HOH I .   ? 0.4963 0.4712 0.4886 -0.0529 -0.0363 -0.0009 567 HOH A O   
4884 O  O   . HOH I .   ? 0.4184 0.3970 0.3934 -0.0375 -0.0311 0.0004  568 HOH A O   
4885 O  O   . HOH I .   ? 0.4085 0.3972 0.4061 -0.0202 0.0009  0.0199  569 HOH A O   
4886 O  O   . HOH I .   ? 0.4082 0.4200 0.4323 -0.0164 -0.0220 0.0227  570 HOH A O   
4887 O  O   . HOH I .   ? 0.3541 0.4254 0.4165 -0.0614 -0.0648 0.0387  571 HOH A O   
4888 O  O   . HOH I .   ? 0.4783 0.5999 0.6169 -0.1094 -0.0993 0.0473  572 HOH A O   
4889 O  O   . HOH I .   ? 0.5028 0.6520 0.4539 0.0427  0.0578  0.1030  573 HOH A O   
4890 O  O   . HOH I .   ? 0.3549 0.4612 0.4699 -0.0275 0.0131  0.0782  574 HOH A O   
4891 O  O   . HOH I .   ? 0.3729 0.5133 0.5326 -0.0375 0.0415  0.1339  575 HOH A O   
4892 O  O   . HOH I .   ? 0.4448 0.6277 0.6420 -0.0291 0.0184  0.1141  576 HOH A O   
4893 O  O   . HOH I .   ? 0.4266 0.5395 0.3825 0.0702  0.0606  -0.0323 577 HOH A O   
4894 O  O   . HOH I .   ? 0.4138 0.4329 0.3630 0.0115  -0.0055 -0.0267 578 HOH A O   
4895 O  O   . HOH I .   ? 0.3871 0.3663 0.3677 -0.0141 -0.0005 0.0069  579 HOH A O   
4896 O  O   . HOH I .   ? 0.3260 0.3143 0.3228 -0.0261 -0.0189 0.0063  580 HOH A O   
4897 O  O   . HOH I .   ? 0.4889 0.5016 0.4727 0.0181  0.0198  0.0784  581 HOH A O   
4898 O  O   . HOH I .   ? 0.5707 0.6280 0.4945 0.0260  -0.0046 -0.0473 582 HOH A O   
4899 O  O   . HOH I .   ? 0.6081 0.5902 0.6111 0.0510  0.0253  -0.1154 583 HOH A O   
4900 O  O   . HOH I .   ? 0.4562 0.4578 0.4748 -0.0521 -0.0367 0.0136  584 HOH A O   
4901 O  O   . HOH I .   ? 0.3472 0.3751 0.4156 -0.0479 -0.0077 0.0493  585 HOH A O   
4902 O  O   . HOH I .   ? 0.4934 0.4467 0.4736 -0.0154 -0.0040 -0.0117 586 HOH A O   
4903 O  O   . HOH I .   ? 0.5000 0.4657 0.6746 -0.1149 -0.0221 0.0715  587 HOH A O   
4904 O  O   . HOH I .   ? 0.4759 0.7146 0.7048 -0.0193 0.0615  0.1600  588 HOH A O   
4905 O  O   . HOH I .   ? 0.3796 0.4200 0.4282 -0.0141 0.0365  0.1100  589 HOH A O   
4906 O  O   . HOH I .   ? 0.4519 0.4995 0.4516 0.0525  0.0399  -0.0434 590 HOH A O   
4907 O  O   . HOH I .   ? 0.6800 0.7176 0.8018 0.0970  0.0671  -0.0274 591 HOH A O   
4908 O  O   . HOH I .   ? 0.4098 0.4359 0.4851 -0.0319 0.0291  0.1052  592 HOH A O   
4909 O  O   . HOH I .   ? 0.6337 0.6192 0.6140 -0.0032 -0.0115 -0.0461 593 HOH A O   
4910 O  O   . HOH I .   ? 0.6017 0.5489 0.6072 -0.0263 0.0033  0.0295  594 HOH A O   
4911 O  O   . HOH I .   ? 0.6387 0.8563 0.8679 0.0128  0.0193  0.1130  595 HOH A O   
4912 O  O   . HOH I .   ? 0.4329 0.6059 0.6049 -0.0282 0.0548  0.1475  596 HOH A O   
4913 O  O   . HOH I .   ? 0.4529 0.3994 0.4806 -0.0599 -0.0200 0.0139  597 HOH A O   
4914 O  O   . HOH I .   ? 0.5492 0.5210 0.5373 -0.0064 -0.0086 -0.0421 598 HOH A O   
4915 O  O   . HOH I .   ? 0.4556 0.5808 0.5535 -0.0919 -0.1041 0.0456  599 HOH A O   
4916 O  O   . HOH I .   ? 0.4303 0.4597 0.5006 0.0064  -0.0129 0.0394  600 HOH A O   
4917 O  O   . HOH I .   ? 0.5658 0.5225 0.5782 -0.0098 -0.0073 -0.0449 601 HOH A O   
4918 O  O   . HOH I .   ? 0.5534 0.7944 0.7562 0.0203  0.0675  0.1260  602 HOH A O   
4919 O  O   . HOH I .   ? 0.4422 0.5904 0.6141 0.0202  0.0075  0.0815  603 HOH A O   
4920 O  O   . HOH I .   ? 0.4637 0.7271 0.6830 0.0113  0.0778  0.1501  604 HOH A O   
4921 O  O   . HOH I .   ? 0.4487 0.5918 0.6541 0.0487  0.0081  0.0938  605 HOH A O   
4922 O  O   . HOH I .   ? 0.6599 0.7363 0.8196 0.0814  0.0505  0.0274  606 HOH A O   
4923 O  O   . HOH I .   ? 0.3424 0.4188 0.4000 -0.0494 -0.0626 0.0450  607 HOH A O   
4924 O  O   . HOH I .   ? 0.4330 0.4436 0.3921 0.0137  -0.0009 -0.0479 608 HOH A O   
4925 O  O   . HOH I .   ? 0.5213 0.4566 0.5090 -0.0264 -0.0024 0.0090  609 HOH A O   
4926 O  O   . HOH I .   ? 0.5762 0.5884 0.6374 0.0073  -0.0097 0.0313  610 HOH A O   
4927 O  O   . HOH I .   ? 0.5307 0.5892 0.5414 -0.0409 -0.0646 0.0415  611 HOH A O   
4928 O  O   . HOH I .   ? 0.5170 0.7119 0.7629 -0.0576 0.0430  0.1691  612 HOH A O   
4929 O  O   . HOH I .   ? 0.5227 0.7064 0.3949 0.0762  0.0561  0.0057  613 HOH A O   
4930 O  O   . HOH I .   ? 0.6013 0.7962 0.4828 0.0828  0.0700  0.0086  614 HOH A O   
4931 O  O   . HOH I .   ? 0.5575 0.6087 0.5931 0.0725  0.0555  -0.0456 615 HOH A O   
4932 O  O   . HOH I .   ? 0.6121 0.6206 0.5787 0.0034  -0.0148 -0.0426 616 HOH A O   
4933 O  O   . HOH I .   ? 0.6801 0.6110 0.7393 -0.1366 -0.0887 -0.0428 617 HOH A O   
4934 O  O   . HOH I .   ? 0.6270 0.6785 0.5873 0.0344  -0.0081 0.0317  618 HOH A O   
4935 O  O   . HOH I .   ? 0.4966 0.6658 0.6993 -0.0427 0.0705  0.1970  619 HOH A O   
4936 O  O   . HOH I .   ? 0.5097 0.4547 0.4562 -0.0153 0.0016  -0.0179 620 HOH A O   
4937 O  O   . HOH I .   ? 0.5121 0.5487 0.4517 0.0169  -0.0076 -0.0330 621 HOH A O   
4938 O  O   . HOH I .   ? 0.4947 0.6348 0.6499 -0.0107 -0.0199 0.0815  622 HOH A O   
4939 O  O   . HOH I .   ? 0.4981 0.6808 0.4576 0.0614  0.0795  0.0593  623 HOH A O   
4940 O  O   . HOH I .   ? 0.4613 0.5010 0.5489 -0.0287 0.0396  0.1300  624 HOH A O   
4941 O  O   . HOH I .   ? 0.5487 0.5942 0.6116 -0.0140 0.0439  0.1332  625 HOH A O   
4942 O  O   . HOH I .   ? 0.7496 0.6511 0.7203 -0.0248 -0.0023 -0.0125 626 HOH A O   
4943 O  O   . HOH I .   ? 0.4915 0.7455 0.5493 0.0395  0.1193  0.2014  627 HOH A O   
4944 O  O   . HOH I .   ? 0.4690 0.7452 0.6933 0.0256  0.0842  0.1456  628 HOH A O   
4945 O  O   . HOH J .   ? 0.4662 0.5733 0.4910 0.0151  -0.0416 -0.0190 501 HOH B O   
4946 O  O   . HOH J .   ? 0.5521 0.7021 0.7308 -0.0363 -0.0551 -0.0382 502 HOH B O   
4947 O  O   . HOH J .   ? 0.5506 0.7226 0.5072 0.0656  -0.0365 0.0664  503 HOH B O   
4948 O  O   . HOH J .   ? 0.5409 0.4995 0.5310 -0.0166 0.0093  -0.0033 504 HOH B O   
4949 O  O   . HOH J .   ? 0.5295 0.6959 0.7400 0.0866  0.0684  0.0591  505 HOH B O   
4950 O  O   . HOH J .   ? 0.5449 0.5855 0.7170 0.1457  0.0798  0.0735  506 HOH B O   
4951 O  O   . HOH J .   ? 0.5474 0.5372 0.7074 0.1469  0.0601  0.1165  507 HOH B O   
4952 O  O   . HOH J .   ? 0.4545 0.6961 0.6859 0.0377  -0.0181 0.0468  508 HOH B O   
4953 O  O   . HOH J .   ? 0.4436 0.3898 0.5032 0.0952  0.0775  0.0066  509 HOH B O   
4954 O  O   . HOH J .   ? 0.4632 0.4920 0.4333 0.0127  -0.0165 -0.0188 510 HOH B O   
4955 O  O   . HOH J .   ? 0.5810 0.8247 0.5634 0.0830  -0.0576 0.0920  511 HOH B O   
4956 O  O   . HOH J .   ? 0.5302 0.5487 0.7069 0.1646  0.1145  0.0542  512 HOH B O   
4957 O  O   . HOH J .   ? 0.5127 0.5784 0.6518 0.1300  0.0290  0.1244  513 HOH B O   
4958 O  O   . HOH J .   ? 0.4758 0.4140 0.4373 0.0415  0.0628  -0.0316 514 HOH B O   
4959 O  O   . HOH J .   ? 0.4503 0.4625 0.4317 0.0012  -0.0175 -0.0373 515 HOH B O   
4960 O  O   . HOH J .   ? 0.5109 0.4785 0.4931 -0.0141 0.0207  0.0062  516 HOH B O   
4961 O  O   . HOH J .   ? 0.3973 0.4599 0.4838 0.0314  0.0635  0.0176  517 HOH B O   
4962 O  O   . HOH J .   ? 0.6015 0.6092 0.6328 0.0689  0.0147  0.0958  518 HOH B O   
4963 O  O   . HOH J .   ? 0.5588 0.4975 0.5687 0.0163  0.0192  0.0644  519 HOH B O   
4964 O  O   . HOH J .   ? 0.5718 0.7143 0.7651 0.0050  0.0280  0.0287  520 HOH B O   
4965 O  O   . HOH J .   ? 0.6755 0.7523 0.6475 0.0235  -0.0287 -0.0102 521 HOH B O   
4966 O  O   . HOH J .   ? 0.6330 0.4999 0.5841 0.0783  0.0957  -0.0680 522 HOH B O   
4967 O  O   . HOH J .   ? 0.5328 0.6450 0.6228 0.0573  0.1326  0.0464  523 HOH B O   
4968 O  O   . HOH J .   ? 0.4048 0.5591 0.4219 0.0445  -0.0455 0.0244  524 HOH B O   
4969 O  O   . HOH J .   ? 0.3831 0.5148 0.5349 0.0669  0.0242  0.0445  525 HOH B O   
4970 O  O   . HOH J .   ? 0.5267 0.6041 0.5100 0.0364  -0.0216 0.0189  526 HOH B O   
4971 O  O   . HOH J .   ? 0.4260 0.5647 0.4745 0.0732  -0.0244 0.0728  527 HOH B O   
4972 O  O   . HOH J .   ? 0.4842 0.4404 0.4795 -0.0158 0.0006  -0.0177 528 HOH B O   
4973 O  O   . HOH J .   ? 0.4115 0.5955 0.5549 0.0256  -0.0355 0.0175  529 HOH B O   
4974 O  O   . HOH J .   ? 0.6901 0.5123 0.6117 0.0386  0.0598  -0.0859 530 HOH B O   
4975 O  O   . HOH J .   ? 0.6510 0.6139 0.5305 0.0411  0.0864  -0.0406 531 HOH B O   
4976 O  O   . HOH J .   ? 0.5332 0.4462 0.4860 0.0418  0.0601  -0.0404 532 HOH B O   
4977 O  O   . HOH J .   ? 0.5475 0.4353 0.5583 0.0188  0.0226  0.0297  533 HOH B O   
4978 O  O   . HOH J .   ? 0.4888 0.4088 0.5459 0.0958  0.0757  0.0068  534 HOH B O   
4979 O  O   . HOH J .   ? 0.6536 0.8443 0.8846 0.0596  0.0902  0.0637  535 HOH B O   
4980 O  O   . HOH J .   ? 0.4378 0.5147 0.5605 0.0781  0.0706  0.0297  536 HOH B O   
4981 O  O   . HOH J .   ? 0.3372 0.4911 0.4813 0.0510  -0.0038 0.0380  537 HOH B O   
4982 O  O   . HOH J .   ? 0.6863 0.5232 0.6956 0.0194  0.0307  -0.0005 538 HOH B O   
4983 O  O   . HOH J .   ? 0.5043 0.5569 0.5925 0.1054  0.0162  0.1179  539 HOH B O   
4984 O  O   . HOH J .   ? 0.3454 0.3658 0.3945 -0.0098 -0.0042 -0.0229 540 HOH B O   
4985 O  O   . HOH J .   ? 0.4017 0.3122 0.4055 0.0372  0.0282  0.0103  541 HOH B O   
4986 O  O   . HOH J .   ? 0.6630 0.5152 0.5784 0.0239  0.0457  -0.0721 542 HOH B O   
4987 O  O   . HOH J .   ? 0.5663 0.4712 0.6074 0.0635  0.0400  0.0370  543 HOH B O   
4988 O  O   . HOH J .   ? 0.5918 0.5541 0.6030 0.0424  0.0360  -0.0036 544 HOH B O   
4989 O  O   . HOH J .   ? 0.3992 0.6301 0.4899 0.0582  -0.0596 0.0502  545 HOH B O   
4990 O  O   . HOH J .   ? 0.4051 0.4261 0.4143 0.0219  -0.0036 -0.0022 546 HOH B O   
4991 O  O   . HOH J .   ? 0.4543 0.6464 0.7386 -0.0696 -0.0685 -0.0391 547 HOH B O   
4992 O  O   . HOH J .   ? 0.4528 0.3651 0.4115 -0.0025 0.0087  -0.0188 548 HOH B O   
4993 O  O   . HOH J .   ? 0.4738 0.4701 0.4582 -0.0028 -0.0134 -0.0372 549 HOH B O   
4994 O  O   . HOH J .   ? 0.3323 0.4026 0.4102 0.0554  0.0103  0.0300  550 HOH B O   
4995 O  O   . HOH J .   ? 0.5736 0.7068 0.7402 0.0997  0.1251  0.0462  551 HOH B O   
4996 O  O   . HOH J .   ? 0.4146 0.5093 0.5070 0.0269  -0.0031 0.0097  552 HOH B O   
4997 O  O   . HOH J .   ? 0.5172 0.6613 0.4835 0.0555  -0.0339 0.0477  553 HOH B O   
4998 O  O   . HOH J .   ? 0.5089 0.5183 0.5568 0.0790  0.0172  0.0991  554 HOH B O   
4999 O  O   . HOH J .   ? 0.3607 0.4750 0.4435 0.0291  -0.0198 0.0105  555 HOH B O   
5000 O  O   . HOH J .   ? 0.4339 0.5630 0.6349 -0.0430 -0.0366 -0.0265 556 HOH B O   
5001 O  O   . HOH J .   ? 0.4124 0.5888 0.6057 0.1090  0.0176  0.0901  557 HOH B O   
5002 O  O   . HOH J .   ? 0.3512 0.3482 0.3424 0.0137  -0.0017 -0.0096 558 HOH B O   
5003 O  O   . HOH J .   ? 0.5082 0.5600 0.4882 0.0471  -0.0042 0.0583  559 HOH B O   
5004 O  O   . HOH J .   ? 0.4945 0.4393 0.4279 -0.0155 0.0039  -0.0175 560 HOH B O   
5005 O  O   . HOH J .   ? 0.5465 0.4498 0.6248 0.1046  0.0730  0.0265  561 HOH B O   
5006 O  O   . HOH J .   ? 0.3779 0.3958 0.4190 -0.0081 0.0547  0.0305  562 HOH B O   
5007 O  O   . HOH J .   ? 0.4758 0.5132 0.5774 -0.0174 0.0269  0.0086  563 HOH B O   
5008 O  O   . HOH J .   ? 0.5851 0.7127 0.7316 0.0973  0.1365  0.0427  564 HOH B O   
5009 O  O   . HOH J .   ? 0.5357 0.5442 0.5649 -0.0158 -0.0219 -0.0512 565 HOH B O   
5010 O  O   . HOH J .   ? 0.4159 0.5919 0.5861 0.0946  0.0035  0.0809  566 HOH B O   
5011 O  O   . HOH J .   ? 0.5598 0.5703 0.5364 0.0037  0.0647  0.0271  567 HOH B O   
5012 O  O   . HOH J .   ? 0.3582 0.3037 0.3476 0.0274  0.0240  -0.0083 568 HOH B O   
5013 O  O   . HOH J .   ? 0.4322 0.4937 0.5211 0.0362  0.0558  0.0152  569 HOH B O   
5014 O  O   . HOH J .   ? 0.3973 0.4273 0.4861 -0.0176 0.0127  -0.0057 570 HOH B O   
5015 O  O   . HOH J .   ? 0.4384 0.6568 0.6596 0.1029  0.0097  0.0914  571 HOH B O   
5016 O  O   . HOH J .   ? 0.3280 0.4383 0.5372 -0.0462 -0.0210 -0.0159 572 HOH B O   
5017 O  O   . HOH J .   ? 0.4288 0.5657 0.5749 0.0511  0.0117  0.0355  573 HOH B O   
5018 O  O   . HOH J .   ? 0.3748 0.3959 0.4417 -0.0230 -0.0185 -0.0410 574 HOH B O   
5019 O  O   . HOH J .   ? 0.4832 0.7262 0.7594 -0.0538 -0.0824 -0.0318 575 HOH B O   
5020 O  O   . HOH J .   ? 0.4056 0.4638 0.4527 0.0754  0.0027  0.0765  576 HOH B O   
5021 O  O   . HOH J .   ? 0.6679 0.5935 0.5243 -0.0016 0.0252  -0.0534 577 HOH B O   
5022 O  O   . HOH J .   ? 0.4823 0.6148 0.5641 0.0924  -0.0118 0.0968  578 HOH B O   
5023 O  O   . HOH J .   ? 0.5245 0.4563 0.5254 -0.0109 0.0101  0.0358  579 HOH B O   
5024 O  O   . HOH J .   ? 0.6126 0.6863 0.6377 0.0770  -0.0018 0.0999  580 HOH B O   
5025 O  O   . HOH J .   ? 0.3948 0.4944 0.4458 0.0731  -0.0105 0.0707  581 HOH B O   
5026 O  O   . HOH J .   ? 0.5190 0.4100 0.5442 0.0488  0.0357  0.0260  582 HOH B O   
5027 O  O   . HOH J .   ? 0.4868 0.3973 0.4282 0.0036  0.0197  -0.0335 583 HOH B O   
5028 O  O   . HOH J .   ? 0.4792 0.4317 0.4124 -0.0143 0.0085  -0.0101 584 HOH B O   
5029 O  O   . HOH J .   ? 0.5973 0.5631 0.6208 0.0524  0.0199  0.0773  585 HOH B O   
5030 O  O   . HOH J .   ? 0.5212 0.4234 0.5107 0.0805  0.0900  -0.0392 586 HOH B O   
5031 O  O   . HOH J .   ? 0.4807 0.7392 0.7181 0.1044  -0.0066 0.1025  587 HOH B O   
5032 O  O   . HOH J .   ? 0.6225 0.4413 0.6619 0.0632  0.0585  0.0004  588 HOH B O   
5033 O  O   . HOH J .   ? 0.6055 0.8053 0.8643 0.0053  0.0286  0.0453  589 HOH B O   
5034 O  O   . HOH J .   ? 0.7012 0.6291 0.5642 0.0351  0.0719  -0.0626 590 HOH B O   
5035 O  O   . HOH J .   ? 0.6718 0.4589 0.6935 0.0379  0.0489  -0.0203 591 HOH B O   
5036 O  O   . HOH J .   ? 0.5476 0.7053 0.7457 0.0309  0.0860  0.0564  592 HOH B O   
5037 O  O   . HOH J .   ? 0.4263 0.4596 0.5102 -0.0121 0.0449  0.0224  593 HOH B O   
5038 O  O   . HOH J .   ? 0.5978 0.4161 0.6326 0.0924  0.0862  -0.0274 594 HOH B O   
5039 O  O   . HOH J .   ? 0.6828 0.4905 0.7127 0.0764  0.0736  -0.0241 595 HOH B O   
5040 O  O   . HOH J .   ? 0.5349 0.4830 0.4982 0.0522  0.0778  -0.0318 596 HOH B O   
5041 O  O   . HOH J .   ? 0.5381 0.4474 0.6158 0.1102  0.0820  0.0169  597 HOH B O   
5042 O  O   . HOH J .   ? 0.6340 0.6169 0.6028 0.0684  0.1070  -0.0244 598 HOH B O   
5043 O  O   . HOH J .   ? 0.6027 0.7704 0.7990 0.0573  0.1087  0.0606  599 HOH B O   
5044 O  O   . HOH J .   ? 0.5127 0.4513 0.4559 -0.0147 0.0011  -0.0223 600 HOH B O   
5045 O  O   . HOH J .   ? 0.4372 0.8405 0.6967 0.0104  -0.1224 0.0257  601 HOH B O   
5046 O  O   . HOH J .   ? 0.7705 0.8459 0.7409 0.0425  -0.0155 0.0370  602 HOH B O   
5047 O  O   . HOH J .   ? 0.4753 0.5245 0.5819 -0.0124 0.0450  0.0242  603 HOH B O   
5048 O  O   . HOH J .   ? 0.5195 0.7255 0.7127 0.1332  -0.0014 0.1343  604 HOH B O   
5049 O  O   . HOH J .   ? 0.5037 0.7044 0.5849 0.0830  -0.0394 0.0861  605 HOH B O   
5050 O  O   . HOH J .   ? 0.7024 0.5745 0.7300 0.1420  0.1440  -0.0530 606 HOH B O   
5051 O  O   . HOH J .   ? 0.6228 0.5406 0.6997 0.0884  0.0466  0.0688  607 HOH B O   
5052 O  O   . HOH J .   ? 0.4924 0.7072 0.7630 0.1250  0.0666  0.0924  608 HOH B O   
5053 O  O   . HOH J .   ? 0.6494 0.8210 0.8720 0.0227  0.0680  0.0547  609 HOH B O   
5054 O  O   . HOH J .   ? 0.4700 0.4316 0.4697 -0.0097 -0.0071 -0.0389 610 HOH B O   
5055 O  O   . HOH J .   ? 0.5570 0.5156 0.5878 -0.0191 -0.0070 -0.0383 611 HOH B O   
5056 O  O   . HOH J .   ? 0.5297 0.6930 0.6051 0.0837  -0.0261 0.0860  612 HOH B O   
5057 O  O   . HOH J .   ? 0.7088 0.6242 0.7800 0.1501  0.1418  -0.0220 613 HOH B O   
5058 O  O   . HOH J .   ? 0.7229 0.7643 0.6931 0.0398  -0.0012 0.0529  614 HOH B O   
5059 O  O   . HOH J .   ? 0.8004 0.7138 0.7237 -0.0031 0.0170  -0.0383 615 HOH B O   
5060 O  O   . HOH J .   ? 0.5173 0.6703 0.6109 0.1051  -0.0139 0.1183  616 HOH B O   
5061 O  O   . HOH J .   ? 0.7040 0.5217 0.6843 0.1429  0.1543  -0.0980 617 HOH B O   
5062 O  O   . HOH J .   ? 0.4570 0.5609 0.5201 0.0870  -0.0066 0.0933  618 HOH B O   
5063 O  O   . HOH J .   ? 0.5890 0.4825 0.5469 -0.0056 0.0095  -0.0230 619 HOH B O   
5064 O  O   . HOH J .   ? 0.6577 0.8328 0.8967 -0.0023 0.0280  0.0383  620 HOH B O   
5065 O  O   . HOH J .   ? 0.5225 0.4686 0.5524 -0.0144 -0.0044 -0.0336 621 HOH B O   
5066 O  O   . HOH J .   ? 0.6268 0.7019 0.6822 0.0863  0.0012  0.0973  622 HOH B O   
5067 O  O   . HOH J .   ? 0.6717 0.8932 0.9491 0.0162  0.0371  0.0560  623 HOH B O   
5068 O  O   . HOH J .   ? 0.5774 0.7654 0.8489 0.1512  0.0927  0.0944  624 HOH B O   
5069 O  O   . HOH J .   ? 0.4755 0.4933 0.4888 -0.0044 0.0632  0.0399  625 HOH B O   
# 
