data_9H0Y
# 
_entry.id   9H0Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9H0Y         pdb_00009h0y 10.2210/pdb9h0y/pdb 
WWPDB D_1292142281 ?            ?                   
# 
_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       2025-06-18 
_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                        9H0Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-09 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wulf.blankenfeldt@helmholz-hzi.de 
_pdbx_contact_author.name_first         Wulf 
_pdbx_contact_author.name_last          Blankenfeldt 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9886-9668 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ornago, C.'       1 0009-0004-6180-9206 
'Blankenfeldt, W.' 2 0000-0001-9886-9668 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            296 
_citation.language                  ? 
_citation.page_first                117832 
_citation.page_last                 117832 
_citation.title                     
;Innovative zinc-binding inhibitors of Legionella pneumophila ProA reduce collagen and flagellin degradation, TLR5 evasion, and human lung tissue inflammation.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2025.117832 
_citation.pdbx_database_id_PubMed   40479898 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Scheithauer, L.'  1  ? 
primary 'Ornago, C.'       2  ? 
primary 'Selmar, J.'       3  ? 
primary 'Schutz, C.'       4  ? 
primary 'Bianchi, G.'      5  ? 
primary 'Kiefer, A.'       6  ? 
primary 'Haupenthal, J.'   7  ? 
primary 'Dellmann, A.'     8  ? 
primary 'Huynh, D.'        9  ? 
primary 'Zhang, R.'        10 ? 
primary 'Blankenfeldt, W.' 11 ? 
primary 'Hirsch, A.H.'     12 ? 
primary 'Steinert, M.'     13 ? 
# 
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 'Zinc metalloproteinase' 37788.734 1   3.4.24.- ? ? ? 
2 non-polymer syn 
;[(2~{R})-1-[[(2~{R})-1-[(3,4-dichlorophenyl)amino]-3-methyl-1-oxidanylidene-butan-2-yl]amino]-4-methyl-1-oxidanylidene-pentan-2-yl]phosphonic acid
;
439.271   1   ?        ? ? ? 
3 non-polymer syn '(R,R)-2,3-BUTANEDIOL' 90.121    5   ?        ? ? ? 
4 non-polymer syn GLYCEROL 92.094    3   ?        ? ? ? 
5 non-polymer syn 'ZINC ION' 65.409    1   ?        ? ? ? 
6 non-polymer nat 'SULFATE ION' 96.063    2   ?        ? ? ? 
7 water       nat water 18.015    294 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PEP1,PRO A' 
# 
_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       
;EKVQAKGMGFGGNRKIGEYQFGKDLPLLEITRDSSVEMCFMENTDVKVVDMGHKYYSNNKPMQFTCKETPDTQSTKTYYT
GYSADGYDRDNGAASPTNDALYAGYVIKHMYHDWYGVEALTKSDGSPMQLVMRVHYGQGYENAYWDGKQMTFGDGDTMMY
PLVSLGVGGHEVSHGFTEQHSGLEYFGQSGGMNESFSDMAAQAAEYYSVGKNSWQIGPEIMKEDSGYDALRYMDKPSRDG
MSIDVADDYYGGLDVHYSSGVYNHLFYILANQPNWNLRMAFDVMVKANMDYWTPYSTFDEGGCGMLSAAKDLGYNLDDIK
KSLSEVTINYQSCYVD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EKVQAKGMGFGGNRKIGEYQFGKDLPLLEITRDSSVEMCFMENTDVKVVDMGHKYYSNNKPMQFTCKETPDTQSTKTYYT
GYSADGYDRDNGAASPTNDALYAGYVIKHMYHDWYGVEALTKSDGSPMQLVMRVHYGQGYENAYWDGKQMTFGDGDTMMY
PLVSLGVGGHEVSHGFTEQHSGLEYFGQSGGMNESFSDMAAQAAEYYSVGKNSWQIGPEIMKEDSGYDALRYMDKPSRDG
MSIDVADDYYGGLDVHYSSGVYNHLFYILANQPNWNLRMAFDVMVKANMDYWTPYSTFDEGGCGMLSAAKDLGYNLDDIK
KSLSEVTINYQSCYVD
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;[(2~{R})-1-[[(2~{R})-1-[(3,4-dichlorophenyl)amino]-3-methyl-1-oxidanylidene-butan-2-yl]amino]-4-methyl-1-oxidanylidene-pentan-2-yl]phosphonic acid
;
A1IRL 
3 '(R,R)-2,3-BUTANEDIOL' BU3   
4 GLYCEROL GOL   
5 'ZINC ION' ZN    
6 'SULFATE ION' SO4   
7 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   LYS n 
1 3   VAL n 
1 4   GLN n 
1 5   ALA n 
1 6   LYS n 
1 7   GLY n 
1 8   MET n 
1 9   GLY n 
1 10  PHE n 
1 11  GLY n 
1 12  GLY n 
1 13  ASN n 
1 14  ARG n 
1 15  LYS n 
1 16  ILE n 
1 17  GLY n 
1 18  GLU n 
1 19  TYR n 
1 20  GLN n 
1 21  PHE n 
1 22  GLY n 
1 23  LYS n 
1 24  ASP n 
1 25  LEU n 
1 26  PRO n 
1 27  LEU n 
1 28  LEU n 
1 29  GLU n 
1 30  ILE n 
1 31  THR n 
1 32  ARG n 
1 33  ASP n 
1 34  SER n 
1 35  SER n 
1 36  VAL n 
1 37  GLU n 
1 38  MET n 
1 39  CYS n 
1 40  PHE n 
1 41  MET n 
1 42  GLU n 
1 43  ASN n 
1 44  THR n 
1 45  ASP n 
1 46  VAL n 
1 47  LYS n 
1 48  VAL n 
1 49  VAL n 
1 50  ASP n 
1 51  MET n 
1 52  GLY n 
1 53  HIS n 
1 54  LYS n 
1 55  TYR n 
1 56  TYR n 
1 57  SER n 
1 58  ASN n 
1 59  ASN n 
1 60  LYS n 
1 61  PRO n 
1 62  MET n 
1 63  GLN n 
1 64  PHE n 
1 65  THR n 
1 66  CYS n 
1 67  LYS n 
1 68  GLU n 
1 69  THR n 
1 70  PRO n 
1 71  ASP n 
1 72  THR n 
1 73  GLN n 
1 74  SER n 
1 75  THR n 
1 76  LYS n 
1 77  THR n 
1 78  TYR n 
1 79  TYR n 
1 80  THR n 
1 81  GLY n 
1 82  TYR n 
1 83  SER n 
1 84  ALA n 
1 85  ASP n 
1 86  GLY n 
1 87  TYR n 
1 88  ASP n 
1 89  ARG n 
1 90  ASP n 
1 91  ASN n 
1 92  GLY n 
1 93  ALA n 
1 94  ALA n 
1 95  SER n 
1 96  PRO n 
1 97  THR n 
1 98  ASN n 
1 99  ASP n 
1 100 ALA n 
1 101 LEU n 
1 102 TYR n 
1 103 ALA n 
1 104 GLY n 
1 105 TYR n 
1 106 VAL n 
1 107 ILE n 
1 108 LYS n 
1 109 HIS n 
1 110 MET n 
1 111 TYR n 
1 112 HIS n 
1 113 ASP n 
1 114 TRP n 
1 115 TYR n 
1 116 GLY n 
1 117 VAL n 
1 118 GLU n 
1 119 ALA n 
1 120 LEU n 
1 121 THR n 
1 122 LYS n 
1 123 SER n 
1 124 ASP n 
1 125 GLY n 
1 126 SER n 
1 127 PRO n 
1 128 MET n 
1 129 GLN n 
1 130 LEU n 
1 131 VAL n 
1 132 MET n 
1 133 ARG n 
1 134 VAL n 
1 135 HIS n 
1 136 TYR n 
1 137 GLY n 
1 138 GLN n 
1 139 GLY n 
1 140 TYR n 
1 141 GLU n 
1 142 ASN n 
1 143 ALA n 
1 144 TYR n 
1 145 TRP n 
1 146 ASP n 
1 147 GLY n 
1 148 LYS n 
1 149 GLN n 
1 150 MET n 
1 151 THR n 
1 152 PHE n 
1 153 GLY n 
1 154 ASP n 
1 155 GLY n 
1 156 ASP n 
1 157 THR n 
1 158 MET n 
1 159 MET n 
1 160 TYR n 
1 161 PRO n 
1 162 LEU n 
1 163 VAL n 
1 164 SER n 
1 165 LEU n 
1 166 GLY n 
1 167 VAL n 
1 168 GLY n 
1 169 GLY n 
1 170 HIS n 
1 171 GLU n 
1 172 VAL n 
1 173 SER n 
1 174 HIS n 
1 175 GLY n 
1 176 PHE n 
1 177 THR n 
1 178 GLU n 
1 179 GLN n 
1 180 HIS n 
1 181 SER n 
1 182 GLY n 
1 183 LEU n 
1 184 GLU n 
1 185 TYR n 
1 186 PHE n 
1 187 GLY n 
1 188 GLN n 
1 189 SER n 
1 190 GLY n 
1 191 GLY n 
1 192 MET n 
1 193 ASN n 
1 194 GLU n 
1 195 SER n 
1 196 PHE n 
1 197 SER n 
1 198 ASP n 
1 199 MET n 
1 200 ALA n 
1 201 ALA n 
1 202 GLN n 
1 203 ALA n 
1 204 ALA n 
1 205 GLU n 
1 206 TYR n 
1 207 TYR n 
1 208 SER n 
1 209 VAL n 
1 210 GLY n 
1 211 LYS n 
1 212 ASN n 
1 213 SER n 
1 214 TRP n 
1 215 GLN n 
1 216 ILE n 
1 217 GLY n 
1 218 PRO n 
1 219 GLU n 
1 220 ILE n 
1 221 MET n 
1 222 LYS n 
1 223 GLU n 
1 224 ASP n 
1 225 SER n 
1 226 GLY n 
1 227 TYR n 
1 228 ASP n 
1 229 ALA n 
1 230 LEU n 
1 231 ARG n 
1 232 TYR n 
1 233 MET n 
1 234 ASP n 
1 235 LYS n 
1 236 PRO n 
1 237 SER n 
1 238 ARG n 
1 239 ASP n 
1 240 GLY n 
1 241 MET n 
1 242 SER n 
1 243 ILE n 
1 244 ASP n 
1 245 VAL n 
1 246 ALA n 
1 247 ASP n 
1 248 ASP n 
1 249 TYR n 
1 250 TYR n 
1 251 GLY n 
1 252 GLY n 
1 253 LEU n 
1 254 ASP n 
1 255 VAL n 
1 256 HIS n 
1 257 TYR n 
1 258 SER n 
1 259 SER n 
1 260 GLY n 
1 261 VAL n 
1 262 TYR n 
1 263 ASN n 
1 264 HIS n 
1 265 LEU n 
1 266 PHE n 
1 267 TYR n 
1 268 ILE n 
1 269 LEU n 
1 270 ALA n 
1 271 ASN n 
1 272 GLN n 
1 273 PRO n 
1 274 ASN n 
1 275 TRP n 
1 276 ASN n 
1 277 LEU n 
1 278 ARG n 
1 279 MET n 
1 280 ALA n 
1 281 PHE n 
1 282 ASP n 
1 283 VAL n 
1 284 MET n 
1 285 VAL n 
1 286 LYS n 
1 287 ALA n 
1 288 ASN n 
1 289 MET n 
1 290 ASP n 
1 291 TYR n 
1 292 TRP n 
1 293 THR n 
1 294 PRO n 
1 295 TYR n 
1 296 SER n 
1 297 THR n 
1 298 PHE n 
1 299 ASP n 
1 300 GLU n 
1 301 GLY n 
1 302 GLY n 
1 303 CYS n 
1 304 GLY n 
1 305 MET n 
1 306 LEU n 
1 307 SER n 
1 308 ALA n 
1 309 ALA n 
1 310 LYS n 
1 311 ASP n 
1 312 LEU n 
1 313 GLY n 
1 314 TYR n 
1 315 ASN n 
1 316 LEU n 
1 317 ASP n 
1 318 ASP n 
1 319 ILE n 
1 320 LYS n 
1 321 LYS n 
1 322 SER n 
1 323 LEU n 
1 324 SER n 
1 325 GLU n 
1 326 VAL n 
1 327 THR n 
1 328 ILE n 
1 329 ASN n 
1 330 TYR n 
1 331 GLN n 
1 332 SER n 
1 333 CYS n 
1 334 TYR n 
1 335 VAL n 
1 336 ASP 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                   336 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Legionella pneumophila str. Corby' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     400673 
_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      'Legionella pneumophila str. Corby' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     400673 
_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 
A1IRL non-polymer         . 
;[(2~{R})-1-[[(2~{R})-1-[(3,4-dichlorophenyl)amino]-3-methyl-1-oxidanylidene-butan-2-yl]amino]-4-methyl-1-oxidanylidene-pentan-2-yl]phosphonic acid
;
?                               'C17 H25 Cl2 N2 O5 P' 439.271 
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 
BU3   non-polymer         . '(R,R)-2,3-BUTANEDIOL' ?                               'C4 H10 O2'           90.121  
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  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'            92.094  
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER ?                               'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'       149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'          105.093 
SO4   non-polymer         . 'SULFATE ION' ?                               'O4 S -2'             96.063  
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'          119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'       204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'         117.146 
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   GLU 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  PHE 10  10  10  PHE PHE A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  PRO 26  26  26  PRO PRO A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  MET 38  38  38  MET MET A . n 
A 1 39  CYS 39  39  39  CYS CYS A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  MET 51  51  51  MET MET A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  CYS 66  66  66  CYS CYS A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  ASP 71  71  ?   ?   ?   A . n 
A 1 72  THR 72  72  ?   ?   ?   A . n 
A 1 73  GLN 73  73  ?   ?   ?   A . n 
A 1 74  SER 74  74  ?   ?   ?   A . n 
A 1 75  THR 75  75  ?   ?   ?   A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 TRP 114 114 114 TRP TRP A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 MET 128 128 128 MET MET A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 MET 132 132 132 MET MET A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 HIS 135 135 135 HIS HIS A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 TRP 145 145 145 TRP TRP A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 MET 150 150 150 MET MET A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 MET 159 159 159 MET MET A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 PRO 161 161 161 PRO PRO A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 HIS 170 170 170 HIS HIS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 VAL 172 172 172 VAL VAL A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLN 179 179 179 GLN GLN A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 GLN 202 202 202 GLN GLN A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 TRP 214 214 214 TRP TRP A . n 
A 1 215 GLN 215 215 215 GLN GLN A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 MET 221 221 221 MET MET A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 TYR 232 232 232 TYR TYR A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 VAL 245 245 245 VAL VAL A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 TYR 249 249 249 TYR TYR A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 HIS 256 256 256 HIS HIS A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 TRP 275 275 275 TRP TRP A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 MET 279 279 279 MET MET A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 PHE 281 281 281 PHE PHE A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 MET 284 284 284 MET MET A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 ASN 288 288 288 ASN ASN A . n 
A 1 289 MET 289 289 289 MET MET A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 TRP 292 292 292 TRP TRP A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 CYS 303 303 303 CYS CYS A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 MET 305 305 305 MET MET A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 TYR 314 314 314 TYR TYR A . n 
A 1 315 ASN 315 315 315 ASN ASN A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ILE 319 319 319 ILE ILE A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 GLU 325 325 325 GLU GLU A . n 
A 1 326 VAL 326 326 326 VAL VAL A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 CYS 333 333 333 CYS CYS A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 ASP 336 336 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IRL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IRL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1IRL 1   401 402 A1IRL HPS A . 
C 3 BU3   1   402 404 BU3   BU3 A . 
D 3 BU3   1   403 405 BU3   BU3 A . 
E 4 GOL   1   404 406 GOL   GOL A . 
F 3 BU3   1   405 408 BU3   BU3 A . 
G 4 GOL   1   406 410 GOL   GOL A . 
H 3 BU3   1   407 412 BU3   BU3 A . 
I 3 BU3   1   408 413 BU3   BU3 A . 
J 4 GOL   1   409 414 GOL   GOL A . 
K 5 ZN    1   410 1   ZN    ZN  A . 
L 6 SO4   1   411 4   SO4   SO4 A . 
M 6 SO4   1   412 7   SO4   SO4 A . 
N 7 HOH   1   501 255 HOH   HOH A . 
N 7 HOH   2   502 227 HOH   HOH A . 
N 7 HOH   3   503 213 HOH   HOH A . 
N 7 HOH   4   504 225 HOH   HOH A . 
N 7 HOH   5   505 191 HOH   HOH A . 
N 7 HOH   6   506 272 HOH   HOH A . 
N 7 HOH   7   507 210 HOH   HOH A . 
N 7 HOH   8   508 77  HOH   HOH A . 
N 7 HOH   9   509 81  HOH   HOH A . 
N 7 HOH   10  510 194 HOH   HOH A . 
N 7 HOH   11  511 67  HOH   HOH A . 
N 7 HOH   12  512 205 HOH   HOH A . 
N 7 HOH   13  513 130 HOH   HOH A . 
N 7 HOH   14  514 95  HOH   HOH A . 
N 7 HOH   15  515 74  HOH   HOH A . 
N 7 HOH   16  516 35  HOH   HOH A . 
N 7 HOH   17  517 247 HOH   HOH A . 
N 7 HOH   18  518 46  HOH   HOH A . 
N 7 HOH   19  519 79  HOH   HOH A . 
N 7 HOH   20  520 184 HOH   HOH A . 
N 7 HOH   21  521 151 HOH   HOH A . 
N 7 HOH   22  522 116 HOH   HOH A . 
N 7 HOH   23  523 68  HOH   HOH A . 
N 7 HOH   24  524 98  HOH   HOH A . 
N 7 HOH   25  525 106 HOH   HOH A . 
N 7 HOH   26  526 218 HOH   HOH A . 
N 7 HOH   27  527 85  HOH   HOH A . 
N 7 HOH   28  528 99  HOH   HOH A . 
N 7 HOH   29  529 82  HOH   HOH A . 
N 7 HOH   30  530 159 HOH   HOH A . 
N 7 HOH   31  531 253 HOH   HOH A . 
N 7 HOH   32  532 173 HOH   HOH A . 
N 7 HOH   33  533 53  HOH   HOH A . 
N 7 HOH   34  534 59  HOH   HOH A . 
N 7 HOH   35  535 26  HOH   HOH A . 
N 7 HOH   36  536 204 HOH   HOH A . 
N 7 HOH   37  537 31  HOH   HOH A . 
N 7 HOH   38  538 163 HOH   HOH A . 
N 7 HOH   39  539 179 HOH   HOH A . 
N 7 HOH   40  540 171 HOH   HOH A . 
N 7 HOH   41  541 57  HOH   HOH A . 
N 7 HOH   42  542 122 HOH   HOH A . 
N 7 HOH   43  543 94  HOH   HOH A . 
N 7 HOH   44  544 97  HOH   HOH A . 
N 7 HOH   45  545 8   HOH   HOH A . 
N 7 HOH   46  546 44  HOH   HOH A . 
N 7 HOH   47  547 43  HOH   HOH A . 
N 7 HOH   48  548 60  HOH   HOH A . 
N 7 HOH   49  549 84  HOH   HOH A . 
N 7 HOH   50  550 265 HOH   HOH A . 
N 7 HOH   51  551 156 HOH   HOH A . 
N 7 HOH   52  552 56  HOH   HOH A . 
N 7 HOH   53  553 54  HOH   HOH A . 
N 7 HOH   54  554 120 HOH   HOH A . 
N 7 HOH   55  555 83  HOH   HOH A . 
N 7 HOH   56  556 254 HOH   HOH A . 
N 7 HOH   57  557 154 HOH   HOH A . 
N 7 HOH   58  558 52  HOH   HOH A . 
N 7 HOH   59  559 142 HOH   HOH A . 
N 7 HOH   60  560 18  HOH   HOH A . 
N 7 HOH   61  561 110 HOH   HOH A . 
N 7 HOH   62  562 3   HOH   HOH A . 
N 7 HOH   63  563 62  HOH   HOH A . 
N 7 HOH   64  564 284 HOH   HOH A . 
N 7 HOH   65  565 114 HOH   HOH A . 
N 7 HOH   66  566 180 HOH   HOH A . 
N 7 HOH   67  567 220 HOH   HOH A . 
N 7 HOH   68  568 80  HOH   HOH A . 
N 7 HOH   69  569 109 HOH   HOH A . 
N 7 HOH   70  570 161 HOH   HOH A . 
N 7 HOH   71  571 162 HOH   HOH A . 
N 7 HOH   72  572 285 HOH   HOH A . 
N 7 HOH   73  573 193 HOH   HOH A . 
N 7 HOH   74  574 6   HOH   HOH A . 
N 7 HOH   75  575 23  HOH   HOH A . 
N 7 HOH   76  576 5   HOH   HOH A . 
N 7 HOH   77  577 125 HOH   HOH A . 
N 7 HOH   78  578 262 HOH   HOH A . 
N 7 HOH   79  579 78  HOH   HOH A . 
N 7 HOH   80  580 21  HOH   HOH A . 
N 7 HOH   81  581 172 HOH   HOH A . 
N 7 HOH   82  582 22  HOH   HOH A . 
N 7 HOH   83  583 58  HOH   HOH A . 
N 7 HOH   84  584 211 HOH   HOH A . 
N 7 HOH   85  585 71  HOH   HOH A . 
N 7 HOH   86  586 49  HOH   HOH A . 
N 7 HOH   87  587 224 HOH   HOH A . 
N 7 HOH   88  588 244 HOH   HOH A . 
N 7 HOH   89  589 212 HOH   HOH A . 
N 7 HOH   90  590 111 HOH   HOH A . 
N 7 HOH   91  591 10  HOH   HOH A . 
N 7 HOH   92  592 1   HOH   HOH A . 
N 7 HOH   93  593 24  HOH   HOH A . 
N 7 HOH   94  594 175 HOH   HOH A . 
N 7 HOH   95  595 15  HOH   HOH A . 
N 7 HOH   96  596 11  HOH   HOH A . 
N 7 HOH   97  597 33  HOH   HOH A . 
N 7 HOH   98  598 102 HOH   HOH A . 
N 7 HOH   99  599 63  HOH   HOH A . 
N 7 HOH   100 600 261 HOH   HOH A . 
N 7 HOH   101 601 112 HOH   HOH A . 
N 7 HOH   102 602 118 HOH   HOH A . 
N 7 HOH   103 603 157 HOH   HOH A . 
N 7 HOH   104 604 28  HOH   HOH A . 
N 7 HOH   105 605 37  HOH   HOH A . 
N 7 HOH   106 606 117 HOH   HOH A . 
N 7 HOH   107 607 76  HOH   HOH A . 
N 7 HOH   108 608 48  HOH   HOH A . 
N 7 HOH   109 609 2   HOH   HOH A . 
N 7 HOH   110 610 133 HOH   HOH A . 
N 7 HOH   111 611 16  HOH   HOH A . 
N 7 HOH   112 612 282 HOH   HOH A . 
N 7 HOH   113 613 126 HOH   HOH A . 
N 7 HOH   114 614 105 HOH   HOH A . 
N 7 HOH   115 615 12  HOH   HOH A . 
N 7 HOH   116 616 17  HOH   HOH A . 
N 7 HOH   117 617 65  HOH   HOH A . 
N 7 HOH   118 618 25  HOH   HOH A . 
N 7 HOH   119 619 38  HOH   HOH A . 
N 7 HOH   120 620 128 HOH   HOH A . 
N 7 HOH   121 621 32  HOH   HOH A . 
N 7 HOH   122 622 178 HOH   HOH A . 
N 7 HOH   123 623 20  HOH   HOH A . 
N 7 HOH   124 624 209 HOH   HOH A . 
N 7 HOH   125 625 181 HOH   HOH A . 
N 7 HOH   126 626 104 HOH   HOH A . 
N 7 HOH   127 627 90  HOH   HOH A . 
N 7 HOH   128 628 149 HOH   HOH A . 
N 7 HOH   129 629 13  HOH   HOH A . 
N 7 HOH   130 630 103 HOH   HOH A . 
N 7 HOH   131 631 234 HOH   HOH A . 
N 7 HOH   132 632 45  HOH   HOH A . 
N 7 HOH   133 633 7   HOH   HOH A . 
N 7 HOH   134 634 196 HOH   HOH A . 
N 7 HOH   135 635 40  HOH   HOH A . 
N 7 HOH   136 636 34  HOH   HOH A . 
N 7 HOH   137 637 123 HOH   HOH A . 
N 7 HOH   138 638 14  HOH   HOH A . 
N 7 HOH   139 639 170 HOH   HOH A . 
N 7 HOH   140 640 293 HOH   HOH A . 
N 7 HOH   141 641 69  HOH   HOH A . 
N 7 HOH   142 642 169 HOH   HOH A . 
N 7 HOH   143 643 19  HOH   HOH A . 
N 7 HOH   144 644 183 HOH   HOH A . 
N 7 HOH   145 645 131 HOH   HOH A . 
N 7 HOH   146 646 214 HOH   HOH A . 
N 7 HOH   147 647 197 HOH   HOH A . 
N 7 HOH   148 648 89  HOH   HOH A . 
N 7 HOH   149 649 168 HOH   HOH A . 
N 7 HOH   150 650 206 HOH   HOH A . 
N 7 HOH   151 651 198 HOH   HOH A . 
N 7 HOH   152 652 136 HOH   HOH A . 
N 7 HOH   153 653 66  HOH   HOH A . 
N 7 HOH   154 654 9   HOH   HOH A . 
N 7 HOH   155 655 192 HOH   HOH A . 
N 7 HOH   156 656 236 HOH   HOH A . 
N 7 HOH   157 657 195 HOH   HOH A . 
N 7 HOH   158 658 274 HOH   HOH A . 
N 7 HOH   159 659 155 HOH   HOH A . 
N 7 HOH   160 660 288 HOH   HOH A . 
N 7 HOH   161 661 135 HOH   HOH A . 
N 7 HOH   162 662 242 HOH   HOH A . 
N 7 HOH   163 663 51  HOH   HOH A . 
N 7 HOH   164 664 29  HOH   HOH A . 
N 7 HOH   165 665 200 HOH   HOH A . 
N 7 HOH   166 666 115 HOH   HOH A . 
N 7 HOH   167 667 292 HOH   HOH A . 
N 7 HOH   168 668 119 HOH   HOH A . 
N 7 HOH   169 669 4   HOH   HOH A . 
N 7 HOH   170 670 27  HOH   HOH A . 
N 7 HOH   171 671 36  HOH   HOH A . 
N 7 HOH   172 672 55  HOH   HOH A . 
N 7 HOH   173 673 153 HOH   HOH A . 
N 7 HOH   174 674 185 HOH   HOH A . 
N 7 HOH   175 675 138 HOH   HOH A . 
N 7 HOH   176 676 280 HOH   HOH A . 
N 7 HOH   177 677 140 HOH   HOH A . 
N 7 HOH   178 678 88  HOH   HOH A . 
N 7 HOH   179 679 240 HOH   HOH A . 
N 7 HOH   180 680 174 HOH   HOH A . 
N 7 HOH   181 681 30  HOH   HOH A . 
N 7 HOH   182 682 241 HOH   HOH A . 
N 7 HOH   183 683 160 HOH   HOH A . 
N 7 HOH   184 684 42  HOH   HOH A . 
N 7 HOH   185 685 50  HOH   HOH A . 
N 7 HOH   186 686 208 HOH   HOH A . 
N 7 HOH   187 687 100 HOH   HOH A . 
N 7 HOH   188 688 124 HOH   HOH A . 
N 7 HOH   189 689 165 HOH   HOH A . 
N 7 HOH   190 690 75  HOH   HOH A . 
N 7 HOH   191 691 246 HOH   HOH A . 
N 7 HOH   192 692 61  HOH   HOH A . 
N 7 HOH   193 693 230 HOH   HOH A . 
N 7 HOH   194 694 101 HOH   HOH A . 
N 7 HOH   195 695 147 HOH   HOH A . 
N 7 HOH   196 696 113 HOH   HOH A . 
N 7 HOH   197 697 260 HOH   HOH A . 
N 7 HOH   198 698 266 HOH   HOH A . 
N 7 HOH   199 699 286 HOH   HOH A . 
N 7 HOH   200 700 164 HOH   HOH A . 
N 7 HOH   201 701 47  HOH   HOH A . 
N 7 HOH   202 702 235 HOH   HOH A . 
N 7 HOH   203 703 72  HOH   HOH A . 
N 7 HOH   204 704 271 HOH   HOH A . 
N 7 HOH   205 705 39  HOH   HOH A . 
N 7 HOH   206 706 144 HOH   HOH A . 
N 7 HOH   207 707 182 HOH   HOH A . 
N 7 HOH   208 708 145 HOH   HOH A . 
N 7 HOH   209 709 141 HOH   HOH A . 
N 7 HOH   210 710 70  HOH   HOH A . 
N 7 HOH   211 711 107 HOH   HOH A . 
N 7 HOH   212 712 143 HOH   HOH A . 
N 7 HOH   213 713 167 HOH   HOH A . 
N 7 HOH   214 714 228 HOH   HOH A . 
N 7 HOH   215 715 91  HOH   HOH A . 
N 7 HOH   216 716 166 HOH   HOH A . 
N 7 HOH   217 717 190 HOH   HOH A . 
N 7 HOH   218 718 257 HOH   HOH A . 
N 7 HOH   219 719 290 HOH   HOH A . 
N 7 HOH   220 720 134 HOH   HOH A . 
N 7 HOH   221 721 223 HOH   HOH A . 
N 7 HOH   222 722 64  HOH   HOH A . 
N 7 HOH   223 723 152 HOH   HOH A . 
N 7 HOH   224 724 281 HOH   HOH A . 
N 7 HOH   225 725 207 HOH   HOH A . 
N 7 HOH   226 726 270 HOH   HOH A . 
N 7 HOH   227 727 276 HOH   HOH A . 
N 7 HOH   228 728 250 HOH   HOH A . 
N 7 HOH   229 729 245 HOH   HOH A . 
N 7 HOH   230 730 251 HOH   HOH A . 
N 7 HOH   231 731 278 HOH   HOH A . 
N 7 HOH   232 732 202 HOH   HOH A . 
N 7 HOH   233 733 252 HOH   HOH A . 
N 7 HOH   234 734 237 HOH   HOH A . 
N 7 HOH   235 735 243 HOH   HOH A . 
N 7 HOH   236 736 222 HOH   HOH A . 
N 7 HOH   237 737 186 HOH   HOH A . 
N 7 HOH   238 738 219 HOH   HOH A . 
N 7 HOH   239 739 158 HOH   HOH A . 
N 7 HOH   240 740 273 HOH   HOH A . 
N 7 HOH   241 741 92  HOH   HOH A . 
N 7 HOH   242 742 249 HOH   HOH A . 
N 7 HOH   243 743 287 HOH   HOH A . 
N 7 HOH   244 744 263 HOH   HOH A . 
N 7 HOH   245 745 93  HOH   HOH A . 
N 7 HOH   246 746 233 HOH   HOH A . 
N 7 HOH   247 747 229 HOH   HOH A . 
N 7 HOH   248 748 258 HOH   HOH A . 
N 7 HOH   249 749 203 HOH   HOH A . 
N 7 HOH   250 750 238 HOH   HOH A . 
N 7 HOH   251 751 268 HOH   HOH A . 
N 7 HOH   252 752 129 HOH   HOH A . 
N 7 HOH   253 753 41  HOH   HOH A . 
N 7 HOH   254 754 277 HOH   HOH A . 
N 7 HOH   255 755 232 HOH   HOH A . 
N 7 HOH   256 756 215 HOH   HOH A . 
N 7 HOH   257 757 188 HOH   HOH A . 
N 7 HOH   258 758 264 HOH   HOH A . 
N 7 HOH   259 759 121 HOH   HOH A . 
N 7 HOH   260 760 279 HOH   HOH A . 
N 7 HOH   261 761 239 HOH   HOH A . 
N 7 HOH   262 762 187 HOH   HOH A . 
N 7 HOH   263 763 221 HOH   HOH A . 
N 7 HOH   264 764 248 HOH   HOH A . 
N 7 HOH   265 765 269 HOH   HOH A . 
N 7 HOH   266 766 148 HOH   HOH A . 
N 7 HOH   267 767 176 HOH   HOH A . 
N 7 HOH   268 768 275 HOH   HOH A . 
N 7 HOH   269 769 201 HOH   HOH A . 
N 7 HOH   270 770 87  HOH   HOH A . 
N 7 HOH   271 771 137 HOH   HOH A . 
N 7 HOH   272 772 294 HOH   HOH A . 
N 7 HOH   273 773 189 HOH   HOH A . 
N 7 HOH   274 774 132 HOH   HOH A . 
N 7 HOH   275 775 127 HOH   HOH A . 
N 7 HOH   276 776 216 HOH   HOH A . 
N 7 HOH   277 777 231 HOH   HOH A . 
N 7 HOH   278 778 256 HOH   HOH A . 
N 7 HOH   279 779 199 HOH   HOH A . 
N 7 HOH   280 780 217 HOH   HOH A . 
N 7 HOH   281 781 150 HOH   HOH A . 
N 7 HOH   282 782 283 HOH   HOH A . 
N 7 HOH   283 783 108 HOH   HOH A . 
N 7 HOH   284 784 146 HOH   HOH A . 
N 7 HOH   285 785 86  HOH   HOH A . 
N 7 HOH   286 786 139 HOH   HOH A . 
N 7 HOH   287 787 259 HOH   HOH A . 
N 7 HOH   288 788 177 HOH   HOH A . 
N 7 HOH   289 789 291 HOH   HOH A . 
N 7 HOH   290 790 73  HOH   HOH A . 
N 7 HOH   291 791 289 HOH   HOH A . 
N 7 HOH   292 792 96  HOH   HOH A . 
N 7 HOH   293 793 267 HOH   HOH A . 
N 7 HOH   294 794 226 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.04 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H0Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     40.650 
_cell.length_a_esd                 ? 
_cell.length_b                     56.510 
_cell.length_b_esd                 ? 
_cell.length_c                     74.120 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9H0Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H0Y 
_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             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.10 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    'IndexHT condidion A5: 0.2 M (NH4)2SO4; 0.1M HEPES pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2022-08-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.03285 
_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, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03285 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H0Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               40.42 
_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                                     52208 
_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                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.5 
_reflns_shell.d_res_low                                     1.533 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2562 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.727 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.864 
_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                                 9H0Y 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.51 
_refine.ls_d_res_low                             40.42 
_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                     52195 
_refine.ls_number_reflns_R_free                  2571 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.85 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1579 
_refine.ls_R_factor_R_free                       0.1656 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1575 
_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                          1.36 
_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             1.10 
_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                 17.10 
_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                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.51 
_refine_hist.d_res_low                        40.42 
_refine_hist.number_atoms_solvent             294 
_refine_hist.number_atoms_total               2974 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2594 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 2788 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.118  ? 3769 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.058 ? 1020 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.068  ? 375  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.012  ? 492  ? 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' 1.51 1.54  . . 138 2712 99.00  . . . . 0.2530 . . . . . . . . . . . 0.2607 
'X-RAY DIFFRACTION' 1.54 1.57  . . 158 2749 99.00  . . . . 0.2297 . . . . . . . . . . . 0.2471 
'X-RAY DIFFRACTION' 1.57 1.60  . . 133 2714 98.00  . . . . 0.2142 . . . . . . . . . . . 0.2445 
'X-RAY DIFFRACTION' 1.60 1.64  . . 129 2648 95.00  . . . . 0.2000 . . . . . . . . . . . 0.2224 
'X-RAY DIFFRACTION' 1.64 1.68  . . 145 2735 99.00  . . . . 0.1996 . . . . . . . . . . . 0.2043 
'X-RAY DIFFRACTION' 1.68 1.73  . . 147 2789 100.00 . . . . 0.2060 . . . . . . . . . . . 0.2578 
'X-RAY DIFFRACTION' 1.73 1.78  . . 132 2767 100.00 . . . . 0.1992 . . . . . . . . . . . 0.1679 
'X-RAY DIFFRACTION' 1.78 1.83  . . 151 2797 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 1.83 1.90  . . 142 2748 100.00 . . . . 0.1701 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 1.90 1.98  . . 148 2780 100.00 . . . . 0.1608 . . . . . . . . . . . 0.1698 
'X-RAY DIFFRACTION' 1.98 2.06  . . 142 2749 100.00 . . . . 0.1653 . . . . . . . . . . . 0.1633 
'X-RAY DIFFRACTION' 2.06 2.17  . . 152 2729 98.00  . . . . 0.1580 . . . . . . . . . . . 0.1942 
'X-RAY DIFFRACTION' 2.17 2.31  . . 155 2671 96.00  . . . . 0.1503 . . . . . . . . . . . 0.1449 
'X-RAY DIFFRACTION' 2.31 2.49  . . 148 2788 100.00 . . . . 0.1458 . . . . . . . . . . . 0.1530 
'X-RAY DIFFRACTION' 2.49 2.74  . . 131 2814 100.00 . . . . 0.1493 . . . . . . . . . . . 0.1592 
'X-RAY DIFFRACTION' 2.74 3.13  . . 152 2814 100.00 . . . . 0.1550 . . . . . . . . . . . 0.1699 
'X-RAY DIFFRACTION' 3.14 3.95  . . 152 2758 99.00  . . . . 0.1343 . . . . . . . . . . . 0.1177 
'X-RAY DIFFRACTION' 3.95 40.42 . . 116 2862 98.00  . . . . 0.1438 . . . . . . . . . . . 0.1594 
# 
_struct.entry_id                     9H0Y 
_struct.title                        'ProA in complex with inhibitor 7' 
_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        9H0Y 
_struct_keywords.text            'ProA, Legionella pneumophila, inhibitor, antibiotics, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
N N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PROA_LEGPN 
_struct_ref.pdbx_db_accession          P21347 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EKVQAKGMGFGGNRKIGEYQFGKDLPLLEITRDSSVEMCFMENTDVKVVDMGHKYYSNNKPMQFTCKETPDTQSTKTYYT
GYSADGYDRDNGAASPTNDALYAGYVIKHMYHDWYGVEALTKSDGSPMQLVMRVHYGQGYENAYWDGKQMTFGDGDTMMY
PLVSLGVGGHEVSHGFTEQHSGLEYFGQSGGMNESFSDMAAQAAEYYSVGKNSWQIGPEIMKEDSGYDALRYMDKPSRDG
MSIDVADDYYGGLDVHYSSGVYNHLFYILANQPNWNLRMAFDVMVKANMDYWTPYSTFDEGGCGMLSAAKDLGYNLDDIK
KSLSEVTINYQSCYVD
;
_struct_ref.pdbx_align_begin           208 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H0Y 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 336 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P21347 
_struct_ref_seq.db_align_beg                  208 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  543 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       336 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 2030  ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  14030 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 95  ? GLY A 116 ? SER A 95  GLY A 116 1 ? 22 
HELX_P HELX_P2  AA2 SER A 164 ? HIS A 180 ? SER A 164 HIS A 180 1 ? 17 
HELX_P HELX_P3  AA3 PHE A 186 ? GLY A 210 ? PHE A 186 GLY A 210 1 ? 25 
HELX_P HELX_P4  AA4 GLY A 217 ? MET A 221 ? GLY A 217 MET A 221 5 ? 5  
HELX_P HELX_P5  AA5 LYS A 235 ? GLY A 240 ? LYS A 235 GLY A 240 5 ? 6  
HELX_P HELX_P6  AA6 VAL A 245 ? TYR A 249 ? VAL A 245 TYR A 249 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 254 ? SER A 259 ? ASP A 254 SER A 259 1 ? 6  
HELX_P HELX_P8  AA8 SER A 259 ? ASN A 271 ? SER A 259 ASN A 271 1 ? 13 
HELX_P HELX_P9  AA9 ASN A 276 ? TYR A 291 ? ASN A 276 TYR A 291 1 ? 16 
HELX_P HELX_P10 AB1 THR A 297 ? GLY A 313 ? THR A 297 GLY A 313 1 ? 17 
HELX_P HELX_P11 AB2 ASN A 315 ? VAL A 326 ? ASN A 315 VAL A 326 1 ? 12 
HELX_P HELX_P12 AB3 TYR A 330 ? VAL A 335 ? TYR A 330 VAL A 335 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS   39  SG  ? ? ? 1_555 A CYS 66  SG ? ? A CYS   39  A CYS 66  1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf2 disulf ? ? A CYS   303 SG  ? ? ? 1_555 A CYS 333 SG ? ? A CYS   303 A CYS 333 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc1 metalc ? ? A HIS   170 NE2 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS   170 A ZN  410 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc2 metalc ? ? A HIS   174 NE2 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS   174 A ZN  410 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc3 metalc ? ? A GLU   194 OE2 ? ? ? 1_555 K ZN  .   ZN ? ? A GLU   194 A ZN  410 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc4 metalc ? ? B A1IRL .   O4  ? ? ? 1_555 K ZN  .   ZN ? ? A A1IRL 401 A ZN  410 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 170 ? A HIS 170 ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555 NE2 ? A HIS   174 ? A HIS   174 ? 1_555 100.0 ? 
2 NE2 ? A HIS 170 ? A HIS 170 ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555 OE2 ? A GLU   194 ? A GLU   194 ? 1_555 124.5 ? 
3 NE2 ? A HIS 174 ? A HIS 174 ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555 OE2 ? A GLU   194 ? A GLU   194 ? 1_555 92.4  ? 
4 NE2 ? A HIS 170 ? A HIS 170 ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555 O4  ? B A1IRL .   ? A A1IRL 401 ? 1_555 112.5 ? 
5 NE2 ? A HIS 174 ? A HIS 174 ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555 O4  ? B A1IRL .   ? A A1IRL 401 ? 1_555 133.0 ? 
6 OE2 ? A GLU 194 ? A GLU 194 ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555 O4  ? B A1IRL .   ? A A1IRL 401 ? 1_555 95.8  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 39  ? CYS A 66  ? CYS A 39  ? 1_555 CYS A 66  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 303 ? CYS A 333 ? CYS A 303 ? 1_555 CYS A 333 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA4 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 GLY A 17  ? PHE A 21  ? GLY A 17  PHE A 21  
AA1 2 VAL A 3   ? ASN A 13  ? VAL A 3   ASN A 13  
AA1 3 LEU A 28  ? ASP A 33  ? LEU A 28  ASP A 33  
AA1 4 MET A 38  ? PHE A 40  ? MET A 38  PHE A 40  
AA1 5 GLN A 63  ? THR A 65  ? GLN A 63  THR A 65  
AA2 1 GLY A 17  ? PHE A 21  ? GLY A 17  PHE A 21  
AA2 2 VAL A 3   ? ASN A 13  ? VAL A 3   ASN A 13  
AA2 3 THR A 77  ? TYR A 79  ? THR A 77  TYR A 79  
AA3 1 VAL A 46  ? ASP A 50  ? VAL A 46  ASP A 50  
AA3 2 LEU A 130 ? TYR A 136 ? LEU A 130 TYR A 136 
AA3 3 MET A 150 ? GLY A 153 ? MET A 150 GLY A 153 
AA3 4 ALA A 143 ? TRP A 145 ? ALA A 143 TRP A 145 
AA4 1 GLN A 215 ? ILE A 216 ? GLN A 215 ILE A 216 
AA4 2 ARG A 231 ? TYR A 232 ? ARG A 231 TYR A 232 
# 
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 O PHE A 21  ? O PHE A 21  N GLY A 9   ? N GLY A 9   
AA1 2 3 N VAL A 3   ? N VAL A 3   O ARG A 32  ? O ARG A 32  
AA1 3 4 N ASP A 33  ? N ASP A 33  O MET A 38  ? O MET A 38  
AA1 4 5 N CYS A 39  ? N CYS A 39  O PHE A 64  ? O PHE A 64  
AA2 1 2 O PHE A 21  ? O PHE A 21  N GLY A 9   ? N GLY A 9   
AA2 2 3 N MET A 8   ? N MET A 8   O TYR A 78  ? O TYR A 78  
AA3 1 2 N LYS A 47  ? N LYS A 47  O MET A 132 ? O MET A 132 
AA3 2 3 N ARG A 133 ? N ARG A 133 O MET A 150 ? O MET A 150 
AA3 3 4 O THR A 151 ? O THR A 151 N TYR A 144 ? N TYR A 144 
AA4 1 2 N ILE A 216 ? N ILE A 216 O ARG A 231 ? O ARG A 231 
# 
_pdbx_entry_details.entry_id                   9H0Y 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 631 ? ? O A HOH 782 ? ? 1.82 
2 1 O   A HOH 724 ? ? O A HOH 740 ? ? 1.90 
3 1 NE2 A GLN 272 ? ? O A HOH 501 ? ? 1.90 
4 1 O   A HOH 758 ? ? O A HOH 772 ? ? 1.93 
5 1 O   A HOH 747 ? ? O A HOH 794 ? ? 1.96 
6 1 O   A HOH 657 ? ? O A HOH 730 ? ? 2.16 
7 1 O   A GLY 125 ? ? O A HOH 502 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     557 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     704 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.01 
# 
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 LYS A 23  ? ? -140.86 -59.70  
2  1 ASP A 88  ? ? -154.88 62.33   
3  1 SER A 95  ? ? -164.18 85.38   
4  1 GLU A 141 ? ? -102.36 59.71   
5  1 LYS A 148 ? ? -144.12 -10.97  
6  1 ASP A 156 ? ? -150.29 -112.04 
7  1 LEU A 162 ? ? -90.25  57.83   
8  1 HIS A 180 ? ? -119.04 -98.58  
9  1 TYR A 185 ? ? -92.44  58.49   
10 1 MET A 241 ? ? -143.63 -29.80  
11 1 MET A 241 ? ? -140.77 -35.43  
12 1 ASN A 274 ? ? 82.38   -10.89  
13 1 TYR A 291 ? ? -133.76 -42.27  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     231 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.078 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_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         14.2430 
_pdbx_refine_tls.origin_y         -4.0005 
_pdbx_refine_tls.origin_z         16.6502 
_pdbx_refine_tls.T[1][1]          0.1280 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0029 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0119 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1133 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0205 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1215 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.8347 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.5445 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.7541 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9017 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.6441 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.2836 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0704 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1365 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0712 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0147 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0672 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0120 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0180 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1414 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0028 
_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 GLU 1   ? A GLU 1   
2 1 Y 1 A ASP 71  ? A ASP 71  
3 1 Y 1 A THR 72  ? A THR 72  
4 1 Y 1 A GLN 73  ? A GLN 73  
5 1 Y 1 A SER 74  ? A SER 74  
6 1 Y 1 A THR 75  ? A THR 75  
7 1 Y 1 A ASP 336 ? A ASP 336 
# 
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 
A1IRL C1   C  Y N 1   
A1IRL C2   C  Y N 2   
A1IRL C3   C  Y N 3   
A1IRL C4   C  Y N 4   
A1IRL C5   C  Y N 5   
A1IRL C6   C  Y N 6   
A1IRL C10  C  N N 7   
A1IRL C11  C  N N 8   
A1IRL C12  C  N N 9   
A1IRL C13  C  N R 10  
A1IRL C14  C  N N 11  
A1IRL C15  C  N N 12  
A1IRL C16  C  N N 13  
A1IRL C17  C  N N 14  
A1IRL C7   C  N N 15  
A1IRL C8   C  N R 16  
A1IRL C9   C  N N 17  
A1IRL N1   N  N N 18  
A1IRL N2   N  N N 19  
A1IRL O1   O  N N 20  
A1IRL O2   O  N N 21  
A1IRL O3   O  N N 22  
A1IRL O4   O  N N 23  
A1IRL O5   O  N N 24  
A1IRL P1   P  N N 25  
A1IRL CL1  CL N N 26  
A1IRL CL2  CL N N 27  
A1IRL H1   H  N N 28  
A1IRL H2   H  N N 29  
A1IRL H3   H  N N 30  
A1IRL H10  H  N N 31  
A1IRL H9   H  N N 32  
A1IRL H8   H  N N 33  
A1IRL H12  H  N N 34  
A1IRL H13  H  N N 35  
A1IRL H11  H  N N 36  
A1IRL H14  H  N N 37  
A1IRL H16  H  N N 38  
A1IRL H15  H  N N 39  
A1IRL H17  H  N N 40  
A1IRL H18  H  N N 41  
A1IRL H20  H  N N 42  
A1IRL H19  H  N N 43  
A1IRL H22  H  N N 44  
A1IRL H21  H  N N 45  
A1IRL H23  H  N N 46  
A1IRL H5   H  N N 47  
A1IRL H7   H  N N 48  
A1IRL H4   H  N N 49  
A1IRL H6   H  N N 50  
A1IRL H24  H  N N 51  
A1IRL H25  H  N N 52  
ALA   N    N  N N 53  
ALA   CA   C  N S 54  
ALA   C    C  N N 55  
ALA   O    O  N N 56  
ALA   CB   C  N N 57  
ALA   OXT  O  N N 58  
ALA   H    H  N N 59  
ALA   H2   H  N N 60  
ALA   HA   H  N N 61  
ALA   HB1  H  N N 62  
ALA   HB2  H  N N 63  
ALA   HB3  H  N N 64  
ALA   HXT  H  N N 65  
ARG   N    N  N N 66  
ARG   CA   C  N S 67  
ARG   C    C  N N 68  
ARG   O    O  N N 69  
ARG   CB   C  N N 70  
ARG   CG   C  N N 71  
ARG   CD   C  N N 72  
ARG   NE   N  N N 73  
ARG   CZ   C  N N 74  
ARG   NH1  N  N N 75  
ARG   NH2  N  N N 76  
ARG   OXT  O  N N 77  
ARG   H    H  N N 78  
ARG   H2   H  N N 79  
ARG   HA   H  N N 80  
ARG   HB2  H  N N 81  
ARG   HB3  H  N N 82  
ARG   HG2  H  N N 83  
ARG   HG3  H  N N 84  
ARG   HD2  H  N N 85  
ARG   HD3  H  N N 86  
ARG   HE   H  N N 87  
ARG   HH11 H  N N 88  
ARG   HH12 H  N N 89  
ARG   HH21 H  N N 90  
ARG   HH22 H  N N 91  
ARG   HXT  H  N N 92  
ASN   N    N  N N 93  
ASN   CA   C  N S 94  
ASN   C    C  N N 95  
ASN   O    O  N N 96  
ASN   CB   C  N N 97  
ASN   CG   C  N N 98  
ASN   OD1  O  N N 99  
ASN   ND2  N  N N 100 
ASN   OXT  O  N N 101 
ASN   H    H  N N 102 
ASN   H2   H  N N 103 
ASN   HA   H  N N 104 
ASN   HB2  H  N N 105 
ASN   HB3  H  N N 106 
ASN   HD21 H  N N 107 
ASN   HD22 H  N N 108 
ASN   HXT  H  N N 109 
ASP   N    N  N N 110 
ASP   CA   C  N S 111 
ASP   C    C  N N 112 
ASP   O    O  N N 113 
ASP   CB   C  N N 114 
ASP   CG   C  N N 115 
ASP   OD1  O  N N 116 
ASP   OD2  O  N N 117 
ASP   OXT  O  N N 118 
ASP   H    H  N N 119 
ASP   H2   H  N N 120 
ASP   HA   H  N N 121 
ASP   HB2  H  N N 122 
ASP   HB3  H  N N 123 
ASP   HD2  H  N N 124 
ASP   HXT  H  N N 125 
BU3   O6   O  N N 126 
BU3   C3   C  N R 127 
BU3   C4   C  N N 128 
BU3   C2   C  N R 129 
BU3   O5   O  N N 130 
BU3   C1   C  N N 131 
BU3   HO6  H  N N 132 
BU3   H3   H  N N 133 
BU3   H41  H  N N 134 
BU3   H42  H  N N 135 
BU3   H43  H  N N 136 
BU3   H2   H  N N 137 
BU3   HO5  H  N N 138 
BU3   H11  H  N N 139 
BU3   H12  H  N N 140 
BU3   H13  H  N N 141 
CYS   N    N  N N 142 
CYS   CA   C  N R 143 
CYS   C    C  N N 144 
CYS   O    O  N N 145 
CYS   CB   C  N N 146 
CYS   SG   S  N N 147 
CYS   OXT  O  N N 148 
CYS   H    H  N N 149 
CYS   H2   H  N N 150 
CYS   HA   H  N N 151 
CYS   HB2  H  N N 152 
CYS   HB3  H  N N 153 
CYS   HG   H  N N 154 
CYS   HXT  H  N N 155 
GLN   N    N  N N 156 
GLN   CA   C  N S 157 
GLN   C    C  N N 158 
GLN   O    O  N N 159 
GLN   CB   C  N N 160 
GLN   CG   C  N N 161 
GLN   CD   C  N N 162 
GLN   OE1  O  N N 163 
GLN   NE2  N  N N 164 
GLN   OXT  O  N N 165 
GLN   H    H  N N 166 
GLN   H2   H  N N 167 
GLN   HA   H  N N 168 
GLN   HB2  H  N N 169 
GLN   HB3  H  N N 170 
GLN   HG2  H  N N 171 
GLN   HG3  H  N N 172 
GLN   HE21 H  N N 173 
GLN   HE22 H  N N 174 
GLN   HXT  H  N N 175 
GLU   N    N  N N 176 
GLU   CA   C  N S 177 
GLU   C    C  N N 178 
GLU   O    O  N N 179 
GLU   CB   C  N N 180 
GLU   CG   C  N N 181 
GLU   CD   C  N N 182 
GLU   OE1  O  N N 183 
GLU   OE2  O  N N 184 
GLU   OXT  O  N N 185 
GLU   H    H  N N 186 
GLU   H2   H  N N 187 
GLU   HA   H  N N 188 
GLU   HB2  H  N N 189 
GLU   HB3  H  N N 190 
GLU   HG2  H  N N 191 
GLU   HG3  H  N N 192 
GLU   HE2  H  N N 193 
GLU   HXT  H  N N 194 
GLY   N    N  N N 195 
GLY   CA   C  N N 196 
GLY   C    C  N N 197 
GLY   O    O  N N 198 
GLY   OXT  O  N N 199 
GLY   H    H  N N 200 
GLY   H2   H  N N 201 
GLY   HA2  H  N N 202 
GLY   HA3  H  N N 203 
GLY   HXT  H  N N 204 
GOL   C1   C  N N 205 
GOL   O1   O  N N 206 
GOL   C2   C  N N 207 
GOL   O2   O  N N 208 
GOL   C3   C  N N 209 
GOL   O3   O  N N 210 
GOL   H11  H  N N 211 
GOL   H12  H  N N 212 
GOL   HO1  H  N N 213 
GOL   H2   H  N N 214 
GOL   HO2  H  N N 215 
GOL   H31  H  N N 216 
GOL   H32  H  N N 217 
GOL   HO3  H  N N 218 
HIS   N    N  N N 219 
HIS   CA   C  N S 220 
HIS   C    C  N N 221 
HIS   O    O  N N 222 
HIS   CB   C  N N 223 
HIS   CG   C  Y N 224 
HIS   ND1  N  Y N 225 
HIS   CD2  C  Y N 226 
HIS   CE1  C  Y N 227 
HIS   NE2  N  Y N 228 
HIS   OXT  O  N N 229 
HIS   H    H  N N 230 
HIS   H2   H  N N 231 
HIS   HA   H  N N 232 
HIS   HB2  H  N N 233 
HIS   HB3  H  N N 234 
HIS   HD1  H  N N 235 
HIS   HD2  H  N N 236 
HIS   HE1  H  N N 237 
HIS   HE2  H  N N 238 
HIS   HXT  H  N N 239 
HOH   O    O  N N 240 
HOH   H1   H  N N 241 
HOH   H2   H  N N 242 
ILE   N    N  N N 243 
ILE   CA   C  N S 244 
ILE   C    C  N N 245 
ILE   O    O  N N 246 
ILE   CB   C  N S 247 
ILE   CG1  C  N N 248 
ILE   CG2  C  N N 249 
ILE   CD1  C  N N 250 
ILE   OXT  O  N N 251 
ILE   H    H  N N 252 
ILE   H2   H  N N 253 
ILE   HA   H  N N 254 
ILE   HB   H  N N 255 
ILE   HG12 H  N N 256 
ILE   HG13 H  N N 257 
ILE   HG21 H  N N 258 
ILE   HG22 H  N N 259 
ILE   HG23 H  N N 260 
ILE   HD11 H  N N 261 
ILE   HD12 H  N N 262 
ILE   HD13 H  N N 263 
ILE   HXT  H  N N 264 
LEU   N    N  N N 265 
LEU   CA   C  N S 266 
LEU   C    C  N N 267 
LEU   O    O  N N 268 
LEU   CB   C  N N 269 
LEU   CG   C  N N 270 
LEU   CD1  C  N N 271 
LEU   CD2  C  N N 272 
LEU   OXT  O  N N 273 
LEU   H    H  N N 274 
LEU   H2   H  N N 275 
LEU   HA   H  N N 276 
LEU   HB2  H  N N 277 
LEU   HB3  H  N N 278 
LEU   HG   H  N N 279 
LEU   HD11 H  N N 280 
LEU   HD12 H  N N 281 
LEU   HD13 H  N N 282 
LEU   HD21 H  N N 283 
LEU   HD22 H  N N 284 
LEU   HD23 H  N N 285 
LEU   HXT  H  N N 286 
LYS   N    N  N N 287 
LYS   CA   C  N S 288 
LYS   C    C  N N 289 
LYS   O    O  N N 290 
LYS   CB   C  N N 291 
LYS   CG   C  N N 292 
LYS   CD   C  N N 293 
LYS   CE   C  N N 294 
LYS   NZ   N  N N 295 
LYS   OXT  O  N N 296 
LYS   H    H  N N 297 
LYS   H2   H  N N 298 
LYS   HA   H  N N 299 
LYS   HB2  H  N N 300 
LYS   HB3  H  N N 301 
LYS   HG2  H  N N 302 
LYS   HG3  H  N N 303 
LYS   HD2  H  N N 304 
LYS   HD3  H  N N 305 
LYS   HE2  H  N N 306 
LYS   HE3  H  N N 307 
LYS   HZ1  H  N N 308 
LYS   HZ2  H  N N 309 
LYS   HZ3  H  N N 310 
LYS   HXT  H  N N 311 
MET   N    N  N N 312 
MET   CA   C  N S 313 
MET   C    C  N N 314 
MET   O    O  N N 315 
MET   CB   C  N N 316 
MET   CG   C  N N 317 
MET   SD   S  N N 318 
MET   CE   C  N N 319 
MET   OXT  O  N N 320 
MET   H    H  N N 321 
MET   H2   H  N N 322 
MET   HA   H  N N 323 
MET   HB2  H  N N 324 
MET   HB3  H  N N 325 
MET   HG2  H  N N 326 
MET   HG3  H  N N 327 
MET   HE1  H  N N 328 
MET   HE2  H  N N 329 
MET   HE3  H  N N 330 
MET   HXT  H  N N 331 
PHE   N    N  N N 332 
PHE   CA   C  N S 333 
PHE   C    C  N N 334 
PHE   O    O  N N 335 
PHE   CB   C  N N 336 
PHE   CG   C  Y N 337 
PHE   CD1  C  Y N 338 
PHE   CD2  C  Y N 339 
PHE   CE1  C  Y N 340 
PHE   CE2  C  Y N 341 
PHE   CZ   C  Y N 342 
PHE   OXT  O  N N 343 
PHE   H    H  N N 344 
PHE   H2   H  N N 345 
PHE   HA   H  N N 346 
PHE   HB2  H  N N 347 
PHE   HB3  H  N N 348 
PHE   HD1  H  N N 349 
PHE   HD2  H  N N 350 
PHE   HE1  H  N N 351 
PHE   HE2  H  N N 352 
PHE   HZ   H  N N 353 
PHE   HXT  H  N N 354 
PRO   N    N  N N 355 
PRO   CA   C  N S 356 
PRO   C    C  N N 357 
PRO   O    O  N N 358 
PRO   CB   C  N N 359 
PRO   CG   C  N N 360 
PRO   CD   C  N N 361 
PRO   OXT  O  N N 362 
PRO   H    H  N N 363 
PRO   HA   H  N N 364 
PRO   HB2  H  N N 365 
PRO   HB3  H  N N 366 
PRO   HG2  H  N N 367 
PRO   HG3  H  N N 368 
PRO   HD2  H  N N 369 
PRO   HD3  H  N N 370 
PRO   HXT  H  N N 371 
SER   N    N  N N 372 
SER   CA   C  N S 373 
SER   C    C  N N 374 
SER   O    O  N N 375 
SER   CB   C  N N 376 
SER   OG   O  N N 377 
SER   OXT  O  N N 378 
SER   H    H  N N 379 
SER   H2   H  N N 380 
SER   HA   H  N N 381 
SER   HB2  H  N N 382 
SER   HB3  H  N N 383 
SER   HG   H  N N 384 
SER   HXT  H  N N 385 
SO4   S    S  N N 386 
SO4   O1   O  N N 387 
SO4   O2   O  N N 388 
SO4   O3   O  N N 389 
SO4   O4   O  N N 390 
THR   N    N  N N 391 
THR   CA   C  N S 392 
THR   C    C  N N 393 
THR   O    O  N N 394 
THR   CB   C  N R 395 
THR   OG1  O  N N 396 
THR   CG2  C  N N 397 
THR   OXT  O  N N 398 
THR   H    H  N N 399 
THR   H2   H  N N 400 
THR   HA   H  N N 401 
THR   HB   H  N N 402 
THR   HG1  H  N N 403 
THR   HG21 H  N N 404 
THR   HG22 H  N N 405 
THR   HG23 H  N N 406 
THR   HXT  H  N N 407 
TRP   N    N  N N 408 
TRP   CA   C  N S 409 
TRP   C    C  N N 410 
TRP   O    O  N N 411 
TRP   CB   C  N N 412 
TRP   CG   C  Y N 413 
TRP   CD1  C  Y N 414 
TRP   CD2  C  Y N 415 
TRP   NE1  N  Y N 416 
TRP   CE2  C  Y N 417 
TRP   CE3  C  Y N 418 
TRP   CZ2  C  Y N 419 
TRP   CZ3  C  Y N 420 
TRP   CH2  C  Y N 421 
TRP   OXT  O  N N 422 
TRP   H    H  N N 423 
TRP   H2   H  N N 424 
TRP   HA   H  N N 425 
TRP   HB2  H  N N 426 
TRP   HB3  H  N N 427 
TRP   HD1  H  N N 428 
TRP   HE1  H  N N 429 
TRP   HE3  H  N N 430 
TRP   HZ2  H  N N 431 
TRP   HZ3  H  N N 432 
TRP   HH2  H  N N 433 
TRP   HXT  H  N N 434 
TYR   N    N  N N 435 
TYR   CA   C  N S 436 
TYR   C    C  N N 437 
TYR   O    O  N N 438 
TYR   CB   C  N N 439 
TYR   CG   C  Y N 440 
TYR   CD1  C  Y N 441 
TYR   CD2  C  Y N 442 
TYR   CE1  C  Y N 443 
TYR   CE2  C  Y N 444 
TYR   CZ   C  Y N 445 
TYR   OH   O  N N 446 
TYR   OXT  O  N N 447 
TYR   H    H  N N 448 
TYR   H2   H  N N 449 
TYR   HA   H  N N 450 
TYR   HB2  H  N N 451 
TYR   HB3  H  N N 452 
TYR   HD1  H  N N 453 
TYR   HD2  H  N N 454 
TYR   HE1  H  N N 455 
TYR   HE2  H  N N 456 
TYR   HH   H  N N 457 
TYR   HXT  H  N N 458 
VAL   N    N  N N 459 
VAL   CA   C  N S 460 
VAL   C    C  N N 461 
VAL   O    O  N N 462 
VAL   CB   C  N N 463 
VAL   CG1  C  N N 464 
VAL   CG2  C  N N 465 
VAL   OXT  O  N N 466 
VAL   H    H  N N 467 
VAL   H2   H  N N 468 
VAL   HA   H  N N 469 
VAL   HB   H  N N 470 
VAL   HG11 H  N N 471 
VAL   HG12 H  N N 472 
VAL   HG13 H  N N 473 
VAL   HG21 H  N N 474 
VAL   HG22 H  N N 475 
VAL   HG23 H  N N 476 
VAL   HXT  H  N N 477 
ZN    ZN   ZN N N 478 
# 
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 
A1IRL O4  P1   doub N N 1   
A1IRL O3  P1   sing N N 2   
A1IRL P1  O2   sing N N 3   
A1IRL P1  C13  sing N N 4   
A1IRL C14 C13  sing N N 5   
A1IRL C14 C15  sing N N 6   
A1IRL C17 C15  sing N N 7   
A1IRL O5  C12  doub N N 8   
A1IRL C13 C12  sing N N 9   
A1IRL C15 C16  sing N N 10  
A1IRL C12 N2   sing N N 11  
A1IRL CL2 C4   sing N N 12  
A1IRL CL1 C3   sing N N 13  
A1IRL C4  C3   doub Y N 14  
A1IRL C4  C5   sing Y N 15  
A1IRL C3  C2   sing Y N 16  
A1IRL C5  C6   doub Y N 17  
A1IRL C2  C1   doub Y N 18  
A1IRL C6  C1   sing Y N 19  
A1IRL C6  N1   sing N N 20  
A1IRL N1  C7   sing N N 21  
A1IRL N2  C8   sing N N 22  
A1IRL C7  O1   doub N N 23  
A1IRL C7  C8   sing N N 24  
A1IRL C8  C9   sing N N 25  
A1IRL C9  C11  sing N N 26  
A1IRL C9  C10  sing N N 27  
A1IRL C1  H1   sing N N 28  
A1IRL C2  H2   sing N N 29  
A1IRL C5  H3   sing N N 30  
A1IRL C10 H10  sing N N 31  
A1IRL C10 H9   sing N N 32  
A1IRL C10 H8   sing N N 33  
A1IRL C11 H12  sing N N 34  
A1IRL C11 H13  sing N N 35  
A1IRL C11 H11  sing N N 36  
A1IRL C13 H14  sing N N 37  
A1IRL C14 H16  sing N N 38  
A1IRL C14 H15  sing N N 39  
A1IRL C15 H17  sing N N 40  
A1IRL C16 H18  sing N N 41  
A1IRL C16 H20  sing N N 42  
A1IRL C16 H19  sing N N 43  
A1IRL C17 H22  sing N N 44  
A1IRL C17 H21  sing N N 45  
A1IRL C17 H23  sing N N 46  
A1IRL C8  H5   sing N N 47  
A1IRL C9  H7   sing N N 48  
A1IRL N1  H4   sing N N 49  
A1IRL N2  H6   sing N N 50  
A1IRL O2  H24  sing N N 51  
A1IRL O3  H25  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
BU3   O6  C3   sing N N 122 
BU3   O6  HO6  sing N N 123 
BU3   C3  C4   sing N N 124 
BU3   C3  C2   sing N N 125 
BU3   C3  H3   sing N N 126 
BU3   C4  H41  sing N N 127 
BU3   C4  H42  sing N N 128 
BU3   C4  H43  sing N N 129 
BU3   C2  O5   sing N N 130 
BU3   C2  C1   sing N N 131 
BU3   C2  H2   sing N N 132 
BU3   O5  HO5  sing N N 133 
BU3   C1  H11  sing N N 134 
BU3   C1  H12  sing N N 135 
BU3   C1  H13  sing N N 136 
CYS   N   CA   sing N N 137 
CYS   N   H    sing N N 138 
CYS   N   H2   sing N N 139 
CYS   CA  C    sing N N 140 
CYS   CA  CB   sing N N 141 
CYS   CA  HA   sing N N 142 
CYS   C   O    doub N N 143 
CYS   C   OXT  sing N N 144 
CYS   CB  SG   sing N N 145 
CYS   CB  HB2  sing N N 146 
CYS   CB  HB3  sing N N 147 
CYS   SG  HG   sing N N 148 
CYS   OXT HXT  sing N N 149 
GLN   N   CA   sing N N 150 
GLN   N   H    sing N N 151 
GLN   N   H2   sing N N 152 
GLN   CA  C    sing N N 153 
GLN   CA  CB   sing N N 154 
GLN   CA  HA   sing N N 155 
GLN   C   O    doub N N 156 
GLN   C   OXT  sing N N 157 
GLN   CB  CG   sing N N 158 
GLN   CB  HB2  sing N N 159 
GLN   CB  HB3  sing N N 160 
GLN   CG  CD   sing N N 161 
GLN   CG  HG2  sing N N 162 
GLN   CG  HG3  sing N N 163 
GLN   CD  OE1  doub N N 164 
GLN   CD  NE2  sing N N 165 
GLN   NE2 HE21 sing N N 166 
GLN   NE2 HE22 sing N N 167 
GLN   OXT HXT  sing N N 168 
GLU   N   CA   sing N N 169 
GLU   N   H    sing N N 170 
GLU   N   H2   sing N N 171 
GLU   CA  C    sing N N 172 
GLU   CA  CB   sing N N 173 
GLU   CA  HA   sing N N 174 
GLU   C   O    doub N N 175 
GLU   C   OXT  sing N N 176 
GLU   CB  CG   sing N N 177 
GLU   CB  HB2  sing N N 178 
GLU   CB  HB3  sing N N 179 
GLU   CG  CD   sing N N 180 
GLU   CG  HG2  sing N N 181 
GLU   CG  HG3  sing N N 182 
GLU   CD  OE1  doub N N 183 
GLU   CD  OE2  sing N N 184 
GLU   OE2 HE2  sing N N 185 
GLU   OXT HXT  sing N N 186 
GLY   N   CA   sing N N 187 
GLY   N   H    sing N N 188 
GLY   N   H2   sing N N 189 
GLY   CA  C    sing N N 190 
GLY   CA  HA2  sing N N 191 
GLY   CA  HA3  sing N N 192 
GLY   C   O    doub N N 193 
GLY   C   OXT  sing N N 194 
GLY   OXT HXT  sing N N 195 
GOL   C1  O1   sing N N 196 
GOL   C1  C2   sing N N 197 
GOL   C1  H11  sing N N 198 
GOL   C1  H12  sing N N 199 
GOL   O1  HO1  sing N N 200 
GOL   C2  O2   sing N N 201 
GOL   C2  C3   sing N N 202 
GOL   C2  H2   sing N N 203 
GOL   O2  HO2  sing N N 204 
GOL   C3  O3   sing N N 205 
GOL   C3  H31  sing N N 206 
GOL   C3  H32  sing N N 207 
GOL   O3  HO3  sing N N 208 
HIS   N   CA   sing N N 209 
HIS   N   H    sing N N 210 
HIS   N   H2   sing N N 211 
HIS   CA  C    sing N N 212 
HIS   CA  CB   sing N N 213 
HIS   CA  HA   sing N N 214 
HIS   C   O    doub N N 215 
HIS   C   OXT  sing N N 216 
HIS   CB  CG   sing N N 217 
HIS   CB  HB2  sing N N 218 
HIS   CB  HB3  sing N N 219 
HIS   CG  ND1  sing Y N 220 
HIS   CG  CD2  doub Y N 221 
HIS   ND1 CE1  doub Y N 222 
HIS   ND1 HD1  sing N N 223 
HIS   CD2 NE2  sing Y N 224 
HIS   CD2 HD2  sing N N 225 
HIS   CE1 NE2  sing Y N 226 
HIS   CE1 HE1  sing N N 227 
HIS   NE2 HE2  sing N N 228 
HIS   OXT HXT  sing N N 229 
HOH   O   H1   sing N N 230 
HOH   O   H2   sing N N 231 
ILE   N   CA   sing N N 232 
ILE   N   H    sing N N 233 
ILE   N   H2   sing N N 234 
ILE   CA  C    sing N N 235 
ILE   CA  CB   sing N N 236 
ILE   CA  HA   sing N N 237 
ILE   C   O    doub N N 238 
ILE   C   OXT  sing N N 239 
ILE   CB  CG1  sing N N 240 
ILE   CB  CG2  sing N N 241 
ILE   CB  HB   sing N N 242 
ILE   CG1 CD1  sing N N 243 
ILE   CG1 HG12 sing N N 244 
ILE   CG1 HG13 sing N N 245 
ILE   CG2 HG21 sing N N 246 
ILE   CG2 HG22 sing N N 247 
ILE   CG2 HG23 sing N N 248 
ILE   CD1 HD11 sing N N 249 
ILE   CD1 HD12 sing N N 250 
ILE   CD1 HD13 sing N N 251 
ILE   OXT HXT  sing N N 252 
LEU   N   CA   sing N N 253 
LEU   N   H    sing N N 254 
LEU   N   H2   sing N N 255 
LEU   CA  C    sing N N 256 
LEU   CA  CB   sing N N 257 
LEU   CA  HA   sing N N 258 
LEU   C   O    doub N N 259 
LEU   C   OXT  sing N N 260 
LEU   CB  CG   sing N N 261 
LEU   CB  HB2  sing N N 262 
LEU   CB  HB3  sing N N 263 
LEU   CG  CD1  sing N N 264 
LEU   CG  CD2  sing N N 265 
LEU   CG  HG   sing N N 266 
LEU   CD1 HD11 sing N N 267 
LEU   CD1 HD12 sing N N 268 
LEU   CD1 HD13 sing N N 269 
LEU   CD2 HD21 sing N N 270 
LEU   CD2 HD22 sing N N 271 
LEU   CD2 HD23 sing N N 272 
LEU   OXT HXT  sing N N 273 
LYS   N   CA   sing N N 274 
LYS   N   H    sing N N 275 
LYS   N   H2   sing N N 276 
LYS   CA  C    sing N N 277 
LYS   CA  CB   sing N N 278 
LYS   CA  HA   sing N N 279 
LYS   C   O    doub N N 280 
LYS   C   OXT  sing N N 281 
LYS   CB  CG   sing N N 282 
LYS   CB  HB2  sing N N 283 
LYS   CB  HB3  sing N N 284 
LYS   CG  CD   sing N N 285 
LYS   CG  HG2  sing N N 286 
LYS   CG  HG3  sing N N 287 
LYS   CD  CE   sing N N 288 
LYS   CD  HD2  sing N N 289 
LYS   CD  HD3  sing N N 290 
LYS   CE  NZ   sing N N 291 
LYS   CE  HE2  sing N N 292 
LYS   CE  HE3  sing N N 293 
LYS   NZ  HZ1  sing N N 294 
LYS   NZ  HZ2  sing N N 295 
LYS   NZ  HZ3  sing N N 296 
LYS   OXT HXT  sing N N 297 
MET   N   CA   sing N N 298 
MET   N   H    sing N N 299 
MET   N   H2   sing N N 300 
MET   CA  C    sing N N 301 
MET   CA  CB   sing N N 302 
MET   CA  HA   sing N N 303 
MET   C   O    doub N N 304 
MET   C   OXT  sing N N 305 
MET   CB  CG   sing N N 306 
MET   CB  HB2  sing N N 307 
MET   CB  HB3  sing N N 308 
MET   CG  SD   sing N N 309 
MET   CG  HG2  sing N N 310 
MET   CG  HG3  sing N N 311 
MET   SD  CE   sing N N 312 
MET   CE  HE1  sing N N 313 
MET   CE  HE2  sing N N 314 
MET   CE  HE3  sing N N 315 
MET   OXT HXT  sing N N 316 
PHE   N   CA   sing N N 317 
PHE   N   H    sing N N 318 
PHE   N   H2   sing N N 319 
PHE   CA  C    sing N N 320 
PHE   CA  CB   sing N N 321 
PHE   CA  HA   sing N N 322 
PHE   C   O    doub N N 323 
PHE   C   OXT  sing N N 324 
PHE   CB  CG   sing N N 325 
PHE   CB  HB2  sing N N 326 
PHE   CB  HB3  sing N N 327 
PHE   CG  CD1  doub Y N 328 
PHE   CG  CD2  sing Y N 329 
PHE   CD1 CE1  sing Y N 330 
PHE   CD1 HD1  sing N N 331 
PHE   CD2 CE2  doub Y N 332 
PHE   CD2 HD2  sing N N 333 
PHE   CE1 CZ   doub Y N 334 
PHE   CE1 HE1  sing N N 335 
PHE   CE2 CZ   sing Y N 336 
PHE   CE2 HE2  sing N N 337 
PHE   CZ  HZ   sing N N 338 
PHE   OXT HXT  sing N N 339 
PRO   N   CA   sing N N 340 
PRO   N   CD   sing N N 341 
PRO   N   H    sing N N 342 
PRO   CA  C    sing N N 343 
PRO   CA  CB   sing N N 344 
PRO   CA  HA   sing N N 345 
PRO   C   O    doub N N 346 
PRO   C   OXT  sing N N 347 
PRO   CB  CG   sing N N 348 
PRO   CB  HB2  sing N N 349 
PRO   CB  HB3  sing N N 350 
PRO   CG  CD   sing N N 351 
PRO   CG  HG2  sing N N 352 
PRO   CG  HG3  sing N N 353 
PRO   CD  HD2  sing N N 354 
PRO   CD  HD3  sing N N 355 
PRO   OXT HXT  sing N N 356 
SER   N   CA   sing N N 357 
SER   N   H    sing N N 358 
SER   N   H2   sing N N 359 
SER   CA  C    sing N N 360 
SER   CA  CB   sing N N 361 
SER   CA  HA   sing N N 362 
SER   C   O    doub N N 363 
SER   C   OXT  sing N N 364 
SER   CB  OG   sing N N 365 
SER   CB  HB2  sing N N 366 
SER   CB  HB3  sing N N 367 
SER   OG  HG   sing N N 368 
SER   OXT HXT  sing N N 369 
SO4   S   O1   doub N N 370 
SO4   S   O2   doub N N 371 
SO4   S   O3   sing N N 372 
SO4   S   O4   sing N N 373 
THR   N   CA   sing N N 374 
THR   N   H    sing N N 375 
THR   N   H2   sing N N 376 
THR   CA  C    sing N N 377 
THR   CA  CB   sing N N 378 
THR   CA  HA   sing N N 379 
THR   C   O    doub N N 380 
THR   C   OXT  sing N N 381 
THR   CB  OG1  sing N N 382 
THR   CB  CG2  sing N N 383 
THR   CB  HB   sing N N 384 
THR   OG1 HG1  sing N N 385 
THR   CG2 HG21 sing N N 386 
THR   CG2 HG22 sing N N 387 
THR   CG2 HG23 sing N N 388 
THR   OXT HXT  sing N N 389 
TRP   N   CA   sing N N 390 
TRP   N   H    sing N N 391 
TRP   N   H2   sing N N 392 
TRP   CA  C    sing N N 393 
TRP   CA  CB   sing N N 394 
TRP   CA  HA   sing N N 395 
TRP   C   O    doub N N 396 
TRP   C   OXT  sing N N 397 
TRP   CB  CG   sing N N 398 
TRP   CB  HB2  sing N N 399 
TRP   CB  HB3  sing N N 400 
TRP   CG  CD1  doub Y N 401 
TRP   CG  CD2  sing Y N 402 
TRP   CD1 NE1  sing Y N 403 
TRP   CD1 HD1  sing N N 404 
TRP   CD2 CE2  doub Y N 405 
TRP   CD2 CE3  sing Y N 406 
TRP   NE1 CE2  sing Y N 407 
TRP   NE1 HE1  sing N N 408 
TRP   CE2 CZ2  sing Y N 409 
TRP   CE3 CZ3  doub Y N 410 
TRP   CE3 HE3  sing N N 411 
TRP   CZ2 CH2  doub Y N 412 
TRP   CZ2 HZ2  sing N N 413 
TRP   CZ3 CH2  sing Y N 414 
TRP   CZ3 HZ3  sing N N 415 
TRP   CH2 HH2  sing N N 416 
TRP   OXT HXT  sing N N 417 
TYR   N   CA   sing N N 418 
TYR   N   H    sing N N 419 
TYR   N   H2   sing N N 420 
TYR   CA  C    sing N N 421 
TYR   CA  CB   sing N N 422 
TYR   CA  HA   sing N N 423 
TYR   C   O    doub N N 424 
TYR   C   OXT  sing N N 425 
TYR   CB  CG   sing N N 426 
TYR   CB  HB2  sing N N 427 
TYR   CB  HB3  sing N N 428 
TYR   CG  CD1  doub Y N 429 
TYR   CG  CD2  sing Y N 430 
TYR   CD1 CE1  sing Y N 431 
TYR   CD1 HD1  sing N N 432 
TYR   CD2 CE2  doub Y N 433 
TYR   CD2 HD2  sing N N 434 
TYR   CE1 CZ   doub Y N 435 
TYR   CE1 HE1  sing N N 436 
TYR   CE2 CZ   sing Y N 437 
TYR   CE2 HE2  sing N N 438 
TYR   CZ  OH   sing N N 439 
TYR   OH  HH   sing N N 440 
TYR   OXT HXT  sing N N 441 
VAL   N   CA   sing N N 442 
VAL   N   H    sing N N 443 
VAL   N   H2   sing N N 444 
VAL   CA  C    sing N N 445 
VAL   CA  CB   sing N N 446 
VAL   CA  HA   sing N N 447 
VAL   C   O    doub N N 448 
VAL   C   OXT  sing N N 449 
VAL   CB  CG1  sing N N 450 
VAL   CB  CG2  sing N N 451 
VAL   CB  HB   sing N N 452 
VAL   CG1 HG11 sing N N 453 
VAL   CG1 HG12 sing N N 454 
VAL   CG1 HG13 sing N N 455 
VAL   CG2 HG21 sing N N 456 
VAL   CG2 HG22 sing N N 457 
VAL   CG2 HG23 sing N N 458 
VAL   OXT HXT  sing N N 459 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   6YZE 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    9H0Y 
_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]   0.024600 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002603 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017696 
_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]   0.013567 
_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  
CL 
H  
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    . LYS   A 1 2   ? 33.521  19.457  18.496  1.00 50.56 ? 2   LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 2   ? 33.319  18.089  18.956  1.00 44.14 ? 2   LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 2   ? 34.082  17.109  18.069  1.00 47.67 ? 2   LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 2   ? 34.149  17.295  16.855  1.00 52.89 ? 2   LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 2   ? 31.835  17.726  18.962  1.00 46.76 ? 2   LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 2   ? 31.176  17.795  20.333  1.00 49.25 ? 2   LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 2   ? 29.708  17.382  20.270  1.00 43.41 ? 2   LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 2   ? 28.783  18.421  20.892  1.00 45.51 ? 2   LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 2   ? 27.424  17.859  21.166  1.00 46.56 ? 2   LYS   A NZ   1 
ATOM   10   H  HA   . LYS   A 1 2   ? 33.655  18.007  19.861  1.00 52.99 ? 2   LYS   A HA   1 
ATOM   11   H  HB2  . LYS   A 1 2   ? 31.363  18.339  18.377  1.00 56.14 ? 2   LYS   A HB2  1 
ATOM   12   H  HB3  . LYS   A 1 2   ? 31.736  16.819  18.633  1.00 56.14 ? 2   LYS   A HB3  1 
ATOM   13   H  HG2  . LYS   A 1 2   ? 31.635  17.193  20.939  1.00 59.12 ? 2   LYS   A HG2  1 
ATOM   14   H  HG3  . LYS   A 1 2   ? 31.222  18.705  20.664  1.00 59.12 ? 2   LYS   A HG3  1 
ATOM   15   H  HD2  . LYS   A 1 2   ? 29.451  17.268  19.342  1.00 52.11 ? 2   LYS   A HD2  1 
ATOM   16   H  HD3  . LYS   A 1 2   ? 29.592  16.549  20.753  1.00 52.11 ? 2   LYS   A HD3  1 
ATOM   17   H  HE2  . LYS   A 1 2   ? 29.161  18.724  21.732  1.00 54.63 ? 2   LYS   A HE2  1 
ATOM   18   H  HE3  . LYS   A 1 2   ? 28.684  19.167  20.280  1.00 54.63 ? 2   LYS   A HE3  1 
ATOM   19   H  HZ1  . LYS   A 1 2   ? 26.904  18.484  21.528  1.00 55.89 ? 2   LYS   A HZ1  1 
ATOM   20   H  HZ2  . LYS   A 1 2   ? 27.053  17.578  20.408  1.00 55.89 ? 2   LYS   A HZ2  1 
ATOM   21   H  HZ3  . LYS   A 1 2   ? 27.487  17.173  21.729  1.00 55.89 ? 2   LYS   A HZ3  1 
ATOM   22   N  N    . VAL   A 1 3   ? 34.683  16.075  18.663  1.00 41.01 ? 3   VAL   A N    1 
ATOM   23   C  CA   . VAL   A 1 3   ? 35.519  15.095  17.907  1.00 42.04 ? 3   VAL   A CA   1 
ATOM   24   C  C    . VAL   A 1 3   ? 34.941  13.690  18.106  1.00 36.85 ? 3   VAL   A C    1 
ATOM   25   O  O    . VAL   A 1 3   ? 33.990  13.563  18.880  1.00 40.47 ? 3   VAL   A O    1 
ATOM   26   C  CB   . VAL   A 1 3   ? 36.987  15.159  18.367  1.00 39.69 ? 3   VAL   A CB   1 
ATOM   27   C  CG1  . VAL   A 1 3   ? 37.562  16.561  18.217  1.00 43.93 ? 3   VAL   A CG1  1 
ATOM   28   C  CG2  . VAL   A 1 3   ? 37.163  14.661  19.797  1.00 46.08 ? 3   VAL   A CG2  1 
ATOM   29   H  H    . VAL   A 1 3   ? 34.630  15.907  19.505  1.00 49.23 ? 3   VAL   A H    1 
ATOM   30   H  HA   . VAL   A 1 3   ? 35.488  15.304  16.961  1.00 50.46 ? 3   VAL   A HA   1 
ATOM   31   H  HB   . VAL   A 1 3   ? 37.508  14.574  17.795  1.00 47.64 ? 3   VAL   A HB   1 
ATOM   32   H  HG11 . VAL   A 1 3   ? 38.499  16.546  18.468  1.00 52.73 ? 3   VAL   A HG11 1 
ATOM   33   H  HG12 . VAL   A 1 3   ? 37.471  16.842  17.293  1.00 52.73 ? 3   VAL   A HG12 1 
ATOM   34   H  HG13 . VAL   A 1 3   ? 37.074  17.167  18.797  1.00 52.73 ? 3   VAL   A HG13 1 
ATOM   35   H  HG21 . VAL   A 1 3   ? 38.055  14.889  20.102  1.00 55.32 ? 3   VAL   A HG21 1 
ATOM   36   H  HG22 . VAL   A 1 3   ? 36.501  15.088  20.363  1.00 55.32 ? 3   VAL   A HG22 1 
ATOM   37   H  HG23 . VAL   A 1 3   ? 37.043  13.699  19.816  1.00 55.32 ? 3   VAL   A HG23 1 
ATOM   38   N  N    . GLN   A 1 4   ? 35.487  12.686  17.425  1.00 37.40 ? 4   GLN   A N    1 
ATOM   39   C  CA   . GLN   A 1 4   ? 35.048  11.281  17.609  1.00 37.85 ? 4   GLN   A CA   1 
ATOM   40   C  C    . GLN   A 1 4   ? 35.852  10.690  18.771  1.00 33.21 ? 4   GLN   A C    1 
ATOM   41   O  O    . GLN   A 1 4   ? 37.075  10.931  18.813  1.00 36.19 ? 4   GLN   A O    1 
ATOM   42   C  CB   . GLN   A 1 4   ? 35.238  10.482  16.321  1.00 42.16 ? 4   GLN   A CB   1 
ATOM   43   C  CG   . GLN   A 1 4   ? 34.420  11.012  15.149  1.00 56.82 ? 4   GLN   A CG   1 
ATOM   44   C  CD   . GLN   A 1 4   ? 34.420  10.087  13.953  1.00 71.52 ? 4   GLN   A CD   1 
ATOM   45   O  OE1  . GLN   A 1 4   ? 33.371  9.605   13.512  1.00 73.37 ? 4   GLN   A OE1  1 
ATOM   46   N  NE2  . GLN   A 1 4   ? 35.602  9.830   13.413  1.00 57.68 ? 4   GLN   A NE2  1 
ATOM   47   H  H    . GLN   A 1 4   ? 36.116  12.781  16.846  1.00 44.90 ? 4   GLN   A H    1 
ATOM   48   H  HA   . GLN   A 1 4   ? 34.107  11.264  17.845  1.00 45.44 ? 4   GLN   A HA   1 
ATOM   49   H  HB2  . GLN   A 1 4   ? 36.174  10.513  16.068  1.00 50.61 ? 4   GLN   A HB2  1 
ATOM   50   H  HB3  . GLN   A 1 4   ? 34.970  9.563   16.480  1.00 50.61 ? 4   GLN   A HB3  1 
ATOM   51   H  HG2  . GLN   A 1 4   ? 33.501  11.129  15.435  1.00 68.20 ? 4   GLN   A HG2  1 
ATOM   52   H  HG3  . GLN   A 1 4   ? 34.790  11.863  14.867  1.00 68.20 ? 4   GLN   A HG3  1 
ATOM   53   H  HE21 . GLN   A 1 4   ? 36.312  10.183  13.745  1.00 69.24 ? 4   GLN   A HE21 1 
ATOM   54   H  HE22 . GLN   A 1 4   ? 35.659  9.310   12.730  1.00 69.24 ? 4   GLN   A HE22 1 
ATOM   55   N  N    . ALA   A 1 5   ? 35.194  9.988   19.692  1.00 30.59 ? 5   ALA   A N    1 
ATOM   56   C  CA   . ALA   A 1 5   ? 35.863  9.345   20.846  1.00 25.72 ? 5   ALA   A CA   1 
ATOM   57   C  C    . ALA   A 1 5   ? 35.316  7.930   21.017  1.00 29.84 ? 5   ALA   A C    1 
ATOM   58   O  O    . ALA   A 1 5   ? 34.470  7.536   20.196  1.00 30.23 ? 5   ALA   A O    1 
ATOM   59   C  CB   . ALA   A 1 5   ? 35.662  10.178  22.092  1.00 32.82 ? 5   ALA   A CB   1 
ATOM   60   H  H    . ALA   A 1 5   ? 34.343  9.862   19.678  1.00 36.73 ? 5   ALA   A H    1 
ATOM   61   H  HA   . ALA   A 1 5   ? 36.815  9.284   20.672  1.00 30.88 ? 5   ALA   A HA   1 
ATOM   62   H  HB1  . ALA   A 1 5   ? 36.052  9.713   22.848  1.00 39.40 ? 5   ALA   A HB1  1 
ATOM   63   H  HB2  . ALA   A 1 5   ? 36.098  11.036  21.971  1.00 39.40 ? 5   ALA   A HB2  1 
ATOM   64   H  HB3  . ALA   A 1 5   ? 34.712  10.307  22.237  1.00 39.40 ? 5   ALA   A HB3  1 
ATOM   65   N  N    . LYS   A 1 6   ? 35.806  7.181   22.003  1.00 25.80 ? 6   LYS   A N    1 
ATOM   66   C  CA   . LYS   A 1 6   ? 35.339  5.830   22.295  1.00 24.21 ? 6   LYS   A CA   1 
ATOM   67   C  C    . LYS   A 1 6   ? 34.892  5.707   23.745  1.00 25.09 ? 6   LYS   A C    1 
ATOM   68   O  O    . LYS   A 1 6   ? 35.509  6.277   24.652  1.00 27.27 ? 6   LYS   A O    1 
ATOM   69   C  CB   . LYS   A 1 6   ? 36.425  4.778   22.040  1.00 25.52 ? 6   LYS   A CB   1 
ATOM   70   C  CG   . LYS   A 1 6   ? 36.825  4.576   20.596  1.00 31.77 ? 6   LYS   A CG   1 
ATOM   71   C  CD   . LYS   A 1 6   ? 35.760  3.861   19.780  1.00 38.87 ? 6   LYS   A CD   1 
ATOM   72   C  CE   . LYS   A 1 6   ? 36.202  3.760   18.326  1.00 47.69 ? 6   LYS   A CE   1 
ATOM   73   N  NZ   . LYS   A 1 6   ? 35.697  2.526   17.668  1.00 47.29 ? 6   LYS   A NZ   1 
ATOM   74   H  H    . LYS   A 1 6   ? 36.430  7.444   22.533  1.00 30.97 ? 6   LYS   A H    1 
ATOM   75   H  HA   . LYS   A 1 6   ? 34.581  5.626   21.727  1.00 29.07 ? 6   LYS   A HA   1 
ATOM   76   H  HB2  . LYS   A 1 6   ? 37.222  5.038   22.527  1.00 30.65 ? 6   LYS   A HB2  1 
ATOM   77   H  HB3  . LYS   A 1 6   ? 36.108  3.925   22.374  1.00 30.65 ? 6   LYS   A HB3  1 
ATOM   78   H  HG2  . LYS   A 1 6   ? 36.983  5.442   20.188  1.00 38.15 ? 6   LYS   A HG2  1 
ATOM   79   H  HG3  . LYS   A 1 6   ? 37.634  4.042   20.565  1.00 38.15 ? 6   LYS   A HG3  1 
ATOM   80   H  HD2  . LYS   A 1 6   ? 35.632  2.964   20.127  1.00 46.67 ? 6   LYS   A HD2  1 
ATOM   81   H  HD3  . LYS   A 1 6   ? 34.931  4.363   19.816  1.00 46.67 ? 6   LYS   A HD3  1 
ATOM   82   H  HE2  . LYS   A 1 6   ? 35.860  4.524   17.836  1.00 57.25 ? 6   LYS   A HE2  1 
ATOM   83   H  HE3  . LYS   A 1 6   ? 37.171  3.747   18.288  1.00 57.25 ? 6   LYS   A HE3  1 
ATOM   84   H  HZ1  . LYS   A 1 6   ? 34.808  2.507   17.699  1.00 56.77 ? 6   LYS   A HZ1  1 
ATOM   85   H  HZ2  . LYS   A 1 6   ? 35.957  2.507   16.817  1.00 56.77 ? 6   LYS   A HZ2  1 
ATOM   86   H  HZ3  . LYS   A 1 6   ? 36.016  1.807   18.084  1.00 56.77 ? 6   LYS   A HZ3  1 
ATOM   87   N  N    . GLY   A 1 7   ? 33.840  4.923   23.961  1.00 23.10 ? 7   GLY   A N    1 
ATOM   88   C  CA   . GLY   A 1 7   ? 33.279  4.764   25.286  1.00 21.88 ? 7   GLY   A CA   1 
ATOM   89   C  C    . GLY   A 1 7   ? 33.425  3.352   25.805  1.00 18.64 ? 7   GLY   A C    1 
ATOM   90   O  O    . GLY   A 1 7   ? 33.053  2.392   25.122  1.00 21.59 ? 7   GLY   A O    1 
ATOM   91   H  H    . GLY   A 1 7   ? 33.435  4.473   23.351  1.00 27.74 ? 7   GLY   A H    1 
ATOM   92   H  HA2  . GLY   A 1 7   ? 33.720  5.366   25.905  1.00 26.28 ? 7   GLY   A HA2  1 
ATOM   93   H  HA3  . GLY   A 1 7   ? 32.335  4.986   25.264  1.00 26.28 ? 7   GLY   A HA3  1 
ATOM   94   N  N    . MET   A 1 8   ? 33.978  3.216   27.005  1.00 21.35 ? 8   MET   A N    1 
ATOM   95   C  CA   . MET   A 1 8   ? 34.119  1.941   27.694  1.00 22.24 ? 8   MET   A CA   1 
ATOM   96   C  C    . MET   A 1 8   ? 33.081  1.858   28.806  1.00 20.41 ? 8   MET   A C    1 
ATOM   97   O  O    . MET   A 1 8   ? 32.884  2.824   29.543  1.00 21.34 ? 8   MET   A O    1 
ATOM   98   C  CB   . MET   A 1 8   ? 35.513  1.829   28.305  1.00 28.90 ? 8   MET   A CB   1 
ATOM   99   C  CG   . MET   A 1 8   ? 35.755  0.582   29.127  1.00 28.79 ? 8   MET   A CG   1 
ATOM   100  S  SD   . MET   A 1 8   ? 37.494  0.488   29.565  1.00 34.52 ? 8   MET   A SD   1 
ATOM   101  C  CE   . MET   A 1 8   ? 38.030  -0.731  28.374  1.00 44.42 ? 8   MET   A CE   1 
ATOM   102  H  H    . MET   A 1 8   ? 34.291  3.877   27.457  1.00 25.64 ? 8   MET   A H    1 
ATOM   103  H  HA   . MET   A 1 8   ? 33.991  1.211   27.069  1.00 26.71 ? 8   MET   A HA   1 
ATOM   104  H  HB2  . MET   A 1 8   ? 36.166  1.837   27.587  1.00 34.70 ? 8   MET   A HB2  1 
ATOM   105  H  HB3  . MET   A 1 8   ? 35.658  2.593   28.884  1.00 34.70 ? 8   MET   A HB3  1 
ATOM   106  H  HG2  . MET   A 1 8   ? 35.233  0.620   29.943  1.00 34.57 ? 8   MET   A HG2  1 
ATOM   107  H  HG3  . MET   A 1 8   ? 35.522  -0.203  28.607  1.00 34.57 ? 8   MET   A HG3  1 
ATOM   108  H  HE1  . MET   A 1 8   ? 38.968  -0.928  28.525  1.00 53.32 ? 8   MET   A HE1  1 
ATOM   109  H  HE2  . MET   A 1 8   ? 37.502  -1.536  28.484  1.00 53.32 ? 8   MET   A HE2  1 
ATOM   110  H  HE3  . MET   A 1 8   ? 37.906  -0.374  27.481  1.00 53.32 ? 8   MET   A HE3  1 
ATOM   111  N  N    . GLY   A 1 9   ? 32.435  0.706   28.952  1.00 19.87 ? 9   GLY   A N    1 
ATOM   112  C  CA   . GLY   A 1 9   ? 31.482  0.552   30.039  1.00 20.13 ? 9   GLY   A CA   1 
ATOM   113  C  C    . GLY   A 1 9   ? 30.753  -0.771  29.951  1.00 20.68 ? 9   GLY   A C    1 
ATOM   114  O  O    . GLY   A 1 9   ? 31.206  -1.695  29.275  1.00 20.97 ? 9   GLY   A O    1 
ATOM   115  H  H    . GLY   A 1 9   ? 32.528  0.015   28.448  1.00 23.86 ? 9   GLY   A H    1 
ATOM   116  H  HA2  . GLY   A 1 9   ? 31.947  0.595   30.889  1.00 24.18 ? 9   GLY   A HA2  1 
ATOM   117  H  HA3  . GLY   A 1 9   ? 30.830  1.269   30.005  1.00 24.18 ? 9   GLY   A HA3  1 
ATOM   118  N  N    . PHE   A 1 10  ? 29.605  -0.848  30.619  1.00 18.77 ? 10  PHE   A N    1 
ATOM   119  C  CA   . PHE   A 1 10  ? 28.916  -2.119  30.796  1.00 16.23 ? 10  PHE   A CA   1 
ATOM   120  C  C    . PHE   A 1 10  ? 27.532  -2.095  30.169  1.00 16.55 ? 10  PHE   A C    1 
ATOM   121  O  O    . PHE   A 1 10  ? 27.009  -1.057  29.773  1.00 17.29 ? 10  PHE   A O    1 
ATOM   122  C  CB   . PHE   A 1 10  ? 28.866  -2.459  32.287  1.00 19.25 ? 10  PHE   A CB   1 
ATOM   123  C  CG   . PHE   A 1 10  ? 30.228  -2.527  32.889  1.00 21.64 ? 10  PHE   A CG   1 
ATOM   124  C  CD1  . PHE   A 1 10  ? 31.019  -3.646  32.713  1.00 22.14 ? 10  PHE   A CD1  1 
ATOM   125  C  CD2  . PHE   A 1 10  ? 30.762  -1.432  33.543  1.00 20.90 ? 10  PHE   A CD2  1 
ATOM   126  C  CE1  . PHE   A 1 10  ? 32.302  -3.692  33.217  1.00 26.22 ? 10  PHE   A CE1  1 
ATOM   127  C  CE2  . PHE   A 1 10  ? 32.044  -1.471  34.056  1.00 24.56 ? 10  PHE   A CE2  1 
ATOM   128  C  CZ   . PHE   A 1 10  ? 32.820  -2.603  33.885  1.00 24.94 ? 10  PHE   A CZ   1 
ATOM   129  H  H    . PHE   A 1 10  ? 29.205  -0.177  30.979  1.00 22.54 ? 10  PHE   A H    1 
ATOM   130  H  HA   . PHE   A 1 10  ? 29.424  -2.817  30.355  1.00 19.49 ? 10  PHE   A HA   1 
ATOM   131  H  HB2  . PHE   A 1 10  ? 28.363  -1.773  32.753  1.00 23.12 ? 10  PHE   A HB2  1 
ATOM   132  H  HB3  . PHE   A 1 10  ? 28.441  -3.323  32.403  1.00 23.12 ? 10  PHE   A HB3  1 
ATOM   133  H  HD1  . PHE   A 1 10  ? 30.679  -4.381  32.256  1.00 26.59 ? 10  PHE   A HD1  1 
ATOM   134  H  HD2  . PHE   A 1 10  ? 30.246  -0.666  33.653  1.00 25.10 ? 10  PHE   A HD2  1 
ATOM   135  H  HE1  . PHE   A 1 10  ? 32.817  -4.458  33.107  1.00 31.48 ? 10  PHE   A HE1  1 
ATOM   136  H  HE2  . PHE   A 1 10  ? 32.387  -0.735  34.509  1.00 29.49 ? 10  PHE   A HE2  1 
ATOM   137  H  HZ   . PHE   A 1 10  ? 33.680  -2.637  34.238  1.00 29.94 ? 10  PHE   A HZ   1 
ATOM   138  N  N    . GLY   A 1 11  ? 26.979  -3.299  30.027  1.00 16.57 ? 11  GLY   A N    1 
ATOM   139  C  CA   . GLY   A 1 11  ? 25.636  -3.494  29.532  1.00 17.86 ? 11  GLY   A CA   1 
ATOM   140  C  C    . GLY   A 1 11  ? 25.084  -4.788  30.095  1.00 16.04 ? 11  GLY   A C    1 
ATOM   141  O  O    . GLY   A 1 11  ? 25.758  -5.494  30.844  1.00 17.56 ? 11  GLY   A O    1 
ATOM   142  H  H    . GLY   A 1 11  ? 27.382  -4.034  30.219  1.00 19.90 ? 11  GLY   A H    1 
ATOM   143  H  HA2  . GLY   A 1 11  ? 25.068  -2.758  29.809  1.00 21.45 ? 11  GLY   A HA2  1 
ATOM   144  H  HA3  . GLY   A 1 11  ? 25.641  -3.545  28.563  1.00 21.45 ? 11  GLY   A HA3  1 
ATOM   145  N  N    . GLY   A 1 12  ? 23.851  -5.101  29.721  1.00 17.09 ? 12  GLY   A N    1 
ATOM   146  C  CA   . GLY   A 1 12  ? 23.206  -6.324  30.173  1.00 17.57 ? 12  GLY   A CA   1 
ATOM   147  C  C    . GLY   A 1 12  ? 22.304  -6.092  31.369  1.00 17.71 ? 12  GLY   A C    1 
ATOM   148  O  O    . GLY   A 1 12  ? 22.014  -4.964  31.775  1.00 17.45 ? 12  GLY   A O    1 
ATOM   149  H  H    . GLY   A 1 12  ? 23.364  -4.618  29.202  1.00 20.52 ? 12  GLY   A H    1 
ATOM   150  H  HA2  . GLY   A 1 12  ? 22.671  -6.692  29.452  1.00 21.11 ? 12  GLY   A HA2  1 
ATOM   151  H  HA3  . GLY   A 1 12  ? 23.881  -6.976  30.418  1.00 21.11 ? 12  GLY   A HA3  1 
ATOM   152  N  N    . ASN   A 1 13  ? 21.830  -7.191  31.939  1.00 18.23 ? 13  ASN   A N    1 
ATOM   153  C  CA   . ASN   A 1 13  ? 20.961  -7.115  33.106  1.00 18.74 ? 13  ASN   A CA   1 
ATOM   154  C  C    . ASN   A 1 13  ? 21.138  -8.358  33.967  1.00 20.32 ? 13  ASN   A C    1 
ATOM   155  O  O    . ASN   A 1 13  ? 21.934  -9.252  33.660  1.00 21.46 ? 13  ASN   A O    1 
ATOM   156  C  CB   . ASN   A 1 13  ? 19.479  -6.879  32.723  1.00 16.12 ? 13  ASN   A CB   1 
ATOM   157  C  CG   . ASN   A 1 13  ? 18.921  -8.002  31.875  1.00 18.55 ? 13  ASN   A CG   1 
ATOM   158  O  OD1  . ASN   A 1 13  ? 19.126  -9.174  32.177  1.00 19.88 ? 13  ASN   A OD1  1 
ATOM   159  N  ND2  . ASN   A 1 13  ? 18.072  -7.651  30.908  1.00 18.71 ? 13  ASN   A ND2  1 
ATOM   160  H  H    . ASN   A 1 13  ? 21.995  -7.991  31.671  1.00 21.90 ? 13  ASN   A H    1 
ATOM   161  H  HA   . ASN   A 1 13  ? 21.241  -6.357  33.642  1.00 22.50 ? 13  ASN   A HA   1 
ATOM   162  H  HB2  . ASN   A 1 13  ? 18.947  -6.818  33.532  1.00 19.36 ? 13  ASN   A HB2  1 
ATOM   163  H  HB3  . ASN   A 1 13  ? 19.410  -6.055  32.216  1.00 19.36 ? 13  ASN   A HB3  1 
ATOM   164  H  HD21 . ASN   A 1 13  ? 17.717  -8.254  30.408  1.00 22.47 ? 13  ASN   A HD21 1 
ATOM   165  H  HD22 . ASN   A 1 13  ? 17.929  -6.819  30.743  1.00 22.47 ? 13  ASN   A HD22 1 
ATOM   166  N  N    . ARG   A 1 14  ? 20.398  -8.393  35.083  1.00 21.29 ? 14  ARG   A N    1 
ATOM   167  C  CA   . ARG   A 1 14  ? 20.588  -9.460  36.059  1.00 23.72 ? 14  ARG   A CA   1 
ATOM   168  C  C    . ARG   A 1 14  ? 20.261  -10.829 35.477  1.00 26.14 ? 14  ARG   A C    1 
ATOM   169  O  O    . ARG   A 1 14  ? 20.850  -11.833 35.891  1.00 30.15 ? 14  ARG   A O    1 
ATOM   170  C  CB   . ARG   A 1 14  ? 19.708  -9.251  37.300  1.00 27.57 ? 14  ARG   A CB   1 
ATOM   171  C  CG   . ARG   A 1 14  ? 20.043  -8.091  38.223  1.00 40.64 ? 14  ARG   A CG   1 
ATOM   172  C  CD   . ARG   A 1 14  ? 19.434  -8.351  39.613  1.00 55.22 ? 14  ARG   A CD   1 
ATOM   173  N  NE   . ARG   A 1 14  ? 18.731  -7.193  40.157  1.00 63.69 ? 14  ARG   A NE   1 
ATOM   174  C  CZ   . ARG   A 1 14  ? 19.316  -6.076  40.560  1.00 58.34 ? 14  ARG   A CZ   1 
ATOM   175  N  NH1  . ARG   A 1 14  ? 20.631  -5.937  40.536  1.00 59.78 ? 14  ARG   A NH1  1 
ATOM   176  N  NH2  . ARG   A 1 14  ? 18.562  -5.070  40.994  1.00 61.26 ? 14  ARG   A NH2  1 
ATOM   177  H  H    . ARG   A 1 14  ? 19.792  -7.820  35.291  1.00 25.57 ? 14  ARG   A H    1 
ATOM   178  H  HA   . ARG   A 1 14  ? 21.515  -9.467  36.344  1.00 28.48 ? 14  ARG   A HA   1 
ATOM   179  H  HB2  . ARG   A 1 14  ? 18.795  -9.120  37.000  1.00 33.11 ? 14  ARG   A HB2  1 
ATOM   180  H  HB3  . ARG   A 1 14  ? 19.754  -10.061 37.832  1.00 33.11 ? 14  ARG   A HB3  1 
ATOM   181  H  HG2  . ARG   A 1 14  ? 21.006  -8.014  38.315  1.00 48.78 ? 14  ARG   A HG2  1 
ATOM   182  H  HG3  . ARG   A 1 14  ? 19.666  -7.271  37.867  1.00 48.78 ? 14  ARG   A HG3  1 
ATOM   183  H  HD2  . ARG   A 1 14  ? 18.797  -9.080  39.551  1.00 66.29 ? 14  ARG   A HD2  1 
ATOM   184  H  HD3  . ARG   A 1 14  ? 20.145  -8.585  40.229  1.00 66.29 ? 14  ARG   A HD3  1 
ATOM   185  H  HE   . ARG   A 1 14  ? 17.875  -7.240  40.220  1.00 76.45 ? 14  ARG   A HE   1 
ATOM   186  H  HH11 . ARG   A 1 14  ? 21.129  -6.580  40.255  1.00 71.76 ? 14  ARG   A HH11 1 
ATOM   187  H  HH12 . ARG   A 1 14  ? 20.990  -5.202  40.803  1.00 71.76 ? 14  ARG   A HH12 1 
ATOM   188  H  HH21 . ARG   A 1 14  ? 17.706  -5.152  41.014  1.00 73.54 ? 14  ARG   A HH21 1 
ATOM   189  H  HH22 . ARG   A 1 14  ? 18.931  -4.340  41.261  1.00 73.54 ? 14  ARG   A HH22 1 
ATOM   190  N  N    . LYS   A 1 15  ? 19.309  -10.896 34.540  1.00 25.80 ? 15  LYS   A N    1 
ATOM   191  C  CA   . LYS   A 1 15  ? 18.915  -12.182 33.976  1.00 28.72 ? 15  LYS   A CA   1 
ATOM   192  C  C    . LYS   A 1 15  ? 19.942  -12.704 32.979  1.00 26.46 ? 15  LYS   A C    1 
ATOM   193  O  O    . LYS   A 1 15  ? 20.394  -13.848 33.092  1.00 29.72 ? 15  LYS   A O    1 
ATOM   194  C  CB   . LYS   A 1 15  ? 17.547  -12.071 33.296  1.00 22.94 ? 15  LYS   A CB   1 
ATOM   195  C  CG   . LYS   A 1 15  ? 17.107  -13.348 32.590  1.00 28.37 ? 15  LYS   A CG   1 
ATOM   196  C  CD   . LYS   A 1 15  ? 15.691  -13.211 32.067  1.00 27.83 ? 15  LYS   A CD   1 
ATOM   197  C  CE   . LYS   A 1 15  ? 15.237  -14.462 31.346  1.00 30.03 ? 15  LYS   A CE   1 
ATOM   198  N  NZ   . LYS   A 1 15  ? 13.802  -14.313 30.987  1.00 32.74 ? 15  LYS   A NZ   1 
ATOM   199  H  H    . LYS   A 1 15  ? 18.884  -10.220 34.221  1.00 30.98 ? 15  LYS   A H    1 
ATOM   200  H  HA   . LYS   A 1 15  ? 18.840  -12.830 34.694  1.00 34.48 ? 15  LYS   A HA   1 
ATOM   201  H  HB2  . LYS   A 1 15  ? 16.880  -11.858 33.968  1.00 27.55 ? 15  LYS   A HB2  1 
ATOM   202  H  HB3  . LYS   A 1 15  ? 17.584  -11.363 32.634  1.00 27.55 ? 15  LYS   A HB3  1 
ATOM   203  H  HG2  . LYS   A 1 15  ? 17.691  -13.522 31.835  1.00 34.06 ? 15  LYS   A HG2  1 
ATOM   204  H  HG3  . LYS   A 1 15  ? 17.133  -14.089 33.216  1.00 34.06 ? 15  LYS   A HG3  1 
ATOM   205  H  HD2  . LYS   A 1 15  ? 15.089  -13.055 32.812  1.00 33.42 ? 15  LYS   A HD2  1 
ATOM   206  H  HD3  . LYS   A 1 15  ? 15.651  -12.470 31.443  1.00 33.42 ? 15  LYS   A HD3  1 
ATOM   207  H  HE2  . LYS   A 1 15  ? 15.752  -14.578 30.532  1.00 36.06 ? 15  LYS   A HE2  1 
ATOM   208  H  HE3  . LYS   A 1 15  ? 15.335  -15.231 31.929  1.00 36.06 ? 15  LYS   A HE3  1 
ATOM   209  H  HZ1  . LYS   A 1 15  ? 13.315  -14.200 31.723  1.00 39.30 ? 15  LYS   A HZ1  1 
ATOM   210  H  HZ2  . LYS   A 1 15  ? 13.693  -13.607 30.456  1.00 39.30 ? 15  LYS   A HZ2  1 
ATOM   211  H  HZ3  . LYS   A 1 15  ? 13.518  -15.041 30.561  1.00 39.30 ? 15  LYS   A HZ3  1 
ATOM   212  N  N    . ILE   A 1 16  ? 20.312  -11.899 31.982  1.00 25.12 ? 16  ILE   A N    1 
ATOM   213  C  CA   . ILE   A 1 16  ? 21.217  -12.377 30.937  1.00 25.47 ? 16  ILE   A CA   1 
ATOM   214  C  C    . ILE   A 1 16  ? 22.675  -12.182 31.303  1.00 23.09 ? 16  ILE   A C    1 
ATOM   215  O  O    . ILE   A 1 16  ? 23.555  -12.774 30.655  1.00 26.56 ? 16  ILE   A O    1 
ATOM   216  C  CB   . ILE   A 1 16  ? 20.890  -11.694 29.595  1.00 24.00 ? 16  ILE   A CB   1 
ATOM   217  C  CG1  . ILE   A 1 16  ? 21.346  -10.237 29.613  1.00 25.03 ? 16  ILE   A CG1  1 
ATOM   218  C  CG2  . ILE   A 1 16  ? 19.412  -11.831 29.298  1.00 28.97 ? 16  ILE   A CG2  1 
ATOM   219  C  CD1  . ILE   A 1 16  ? 20.910  -9.471  28.397  1.00 27.99 ? 16  ILE   A CD1  1 
ATOM   220  H  H    . ILE   A 1 16  ? 20.057  -11.083 31.889  1.00 30.16 ? 16  ILE   A H    1 
ATOM   221  H  HA   . ILE   A 1 16  ? 21.074  -13.329 30.818  1.00 30.58 ? 16  ILE   A HA   1 
ATOM   222  H  HB   . ILE   A 1 16  ? 21.381  -12.154 28.896  1.00 28.82 ? 16  ILE   A HB   1 
ATOM   223  H  HG12 . ILE   A 1 16  ? 20.974  -9.798  30.394  1.00 30.06 ? 16  ILE   A HG12 1 
ATOM   224  H  HG13 . ILE   A 1 16  ? 22.315  -10.204 29.644  1.00 30.06 ? 16  ILE   A HG13 1 
ATOM   225  H  HG21 . ILE   A 1 16  ? 19.258  -11.640 28.360  1.00 34.78 ? 16  ILE   A HG21 1 
ATOM   226  H  HG22 . ILE   A 1 16  ? 19.134  -12.738 29.500  1.00 34.78 ? 16  ILE   A HG22 1 
ATOM   227  H  HG23 . ILE   A 1 16  ? 18.919  -11.204 29.851  1.00 34.78 ? 16  ILE   A HG23 1 
ATOM   228  H  HD11 . ILE   A 1 16  ? 21.387  -8.627  28.369  1.00 33.61 ? 16  ILE   A HD11 1 
ATOM   229  H  HD12 . ILE   A 1 16  ? 21.115  -9.993  27.606  1.00 33.61 ? 16  ILE   A HD12 1 
ATOM   230  H  HD13 . ILE   A 1 16  ? 19.955  -9.310  28.448  1.00 33.61 ? 16  ILE   A HD13 1 
ATOM   231  N  N    . GLY   A 1 17  ? 22.961  -11.409 32.338  1.00 22.05 ? 17  GLY   A N    1 
ATOM   232  C  CA   . GLY   A 1 17  ? 24.321  -11.166 32.762  1.00 24.82 ? 17  GLY   A CA   1 
ATOM   233  C  C    . GLY   A 1 17  ? 24.828  -9.821  32.283  1.00 19.60 ? 17  GLY   A C    1 
ATOM   234  O  O    . GLY   A 1 17  ? 24.266  -9.180  31.394  1.00 21.93 ? 17  GLY   A O    1 
ATOM   235  H  H    . GLY   A 1 17  ? 22.372  -11.007 32.818  1.00 26.47 ? 17  GLY   A H    1 
ATOM   236  H  HA2  . GLY   A 1 17  ? 24.366  -11.185 33.731  1.00 29.80 ? 17  GLY   A HA2  1 
ATOM   237  H  HA3  . GLY   A 1 17  ? 24.904  -11.859 32.413  1.00 29.80 ? 17  GLY   A HA3  1 
ATOM   238  N  N    . GLU   A 1 18  ? 25.923  -9.410  32.900  1.00 24.43 ? 18  GLU   A N    1 
ATOM   239  C  CA   . GLU   A 1 18  ? 26.593  -8.159  32.588  1.00 22.21 ? 18  GLU   A CA   1 
ATOM   240  C  C    . GLU   A 1 18  ? 27.749  -8.441  31.640  1.00 22.90 ? 18  GLU   A C    1 
ATOM   241  O  O    . GLU   A 1 18  ? 28.411  -9.478  31.747  1.00 30.94 ? 18  GLU   A O    1 
ATOM   242  C  CB   . GLU   A 1 18  ? 27.075  -7.518  33.887  1.00 29.58 ? 18  GLU   A CB   1 
ATOM   243  C  CG   . GLU   A 1 18  ? 27.505  -6.082  33.778  1.00 30.63 ? 18  GLU   A CG   1 
ATOM   244  C  CD   . GLU   A 1 18  ? 27.914  -5.510  35.119  1.00 36.56 ? 18  GLU   A CD   1 
ATOM   245  O  OE1  . GLU   A 1 18  ? 27.022  -5.311  35.975  1.00 36.19 ? 18  GLU   A OE1  1 
ATOM   246  O  OE2  . GLU   A 1 18  ? 29.115  -5.234  35.317  1.00 31.93 ? 18  GLU   A OE2  1 
ATOM   247  H  H    . GLU   A 1 18  ? 26.311  -9.855  33.526  1.00 29.33 ? 18  GLU   A H    1 
ATOM   248  H  HA   . GLU   A 1 18  ? 25.973  -7.554  32.153  1.00 26.67 ? 18  GLU   A HA   1 
ATOM   249  H  HB2  . GLU   A 1 18  ? 26.354  -7.557  34.535  1.00 35.51 ? 18  GLU   A HB2  1 
ATOM   250  H  HB3  . GLU   A 1 18  ? 27.834  -8.025  34.216  1.00 35.51 ? 18  GLU   A HB3  1 
ATOM   251  H  HG2  . GLU   A 1 18  ? 28.265  -6.022  33.179  1.00 36.77 ? 18  GLU   A HG2  1 
ATOM   252  H  HG3  . GLU   A 1 18  ? 26.767  -5.553  33.436  1.00 36.77 ? 18  GLU   A HG3  1 
ATOM   253  N  N    . TYR   A 1 19  ? 27.968  -7.541  30.688  1.00 20.68 ? 19  TYR   A N    1 
ATOM   254  C  CA   . TYR   A 1 19  ? 29.099  -7.651  29.774  1.00 20.04 ? 19  TYR   A CA   1 
ATOM   255  C  C    . TYR   A 1 19  ? 29.726  -6.273  29.634  1.00 20.68 ? 19  TYR   A C    1 
ATOM   256  O  O    . TYR   A 1 19  ? 29.166  -5.264  30.078  1.00 21.56 ? 19  TYR   A O    1 
ATOM   257  C  CB   . TYR   A 1 19  ? 28.685  -8.208  28.401  1.00 21.74 ? 19  TYR   A CB   1 
ATOM   258  C  CG   . TYR   A 1 19  ? 27.400  -7.613  27.909  1.00 19.16 ? 19  TYR   A CG   1 
ATOM   259  C  CD1  . TYR   A 1 19  ? 27.375  -6.365  27.301  1.00 21.41 ? 19  TYR   A CD1  1 
ATOM   260  C  CD2  . TYR   A 1 19  ? 26.201  -8.278  28.089  1.00 20.53 ? 19  TYR   A CD2  1 
ATOM   261  C  CE1  . TYR   A 1 19  ? 26.188  -5.805  26.872  1.00 20.09 ? 19  TYR   A CE1  1 
ATOM   262  C  CE2  . TYR   A 1 19  ? 25.014  -7.734  27.659  1.00 19.86 ? 19  TYR   A CE2  1 
ATOM   263  C  CZ   . TYR   A 1 19  ? 25.009  -6.499  27.053  1.00 19.08 ? 19  TYR   A CZ   1 
ATOM   264  O  OH   . TYR   A 1 19  ? 23.808  -5.971  26.639  1.00 21.14 ? 19  TYR   A OH   1 
ATOM   265  H  H    . TYR   A 1 19  ? 27.472  -6.852  30.550  1.00 24.83 ? 19  TYR   A H    1 
ATOM   266  H  HA   . TYR   A 1 19  ? 29.763  -8.247  30.154  1.00 24.06 ? 19  TYR   A HA   1 
ATOM   267  H  HB2  . TYR   A 1 19  ? 29.378  -8.006  27.753  1.00 26.11 ? 19  TYR   A HB2  1 
ATOM   268  H  HB3  . TYR   A 1 19  ? 28.565  -9.168  28.471  1.00 26.11 ? 19  TYR   A HB3  1 
ATOM   269  H  HD1  . TYR   A 1 19  ? 28.171  -5.899  27.181  1.00 25.71 ? 19  TYR   A HD1  1 
ATOM   270  H  HD2  . TYR   A 1 19  ? 26.199  -9.113  28.499  1.00 24.65 ? 19  TYR   A HD2  1 
ATOM   271  H  HE1  . TYR   A 1 19  ? 26.184  -4.971  26.460  1.00 24.13 ? 19  TYR   A HE1  1 
ATOM   272  H  HE2  . TYR   A 1 19  ? 24.217  -8.196  27.783  1.00 23.85 ? 19  TYR   A HE2  1 
ATOM   273  H  HH   . TYR   A 1 19  ? 23.931  -5.217  26.290  1.00 25.38 ? 19  TYR   A HH   1 
ATOM   274  N  N    . GLN   A 1 20  ? 30.894  -6.228  28.989  1.00 21.18 ? 20  GLN   A N    1 
ATOM   275  C  CA   . GLN   A 1 20  ? 31.678  -5.006  28.911  1.00 21.74 ? 20  GLN   A CA   1 
ATOM   276  C  C    . GLN   A 1 20  ? 31.976  -4.600  27.474  1.00 19.43 ? 20  GLN   A C    1 
ATOM   277  O  O    . GLN   A 1 20  ? 32.559  -5.379  26.703  1.00 22.27 ? 20  GLN   A O    1 
ATOM   278  C  CB   . GLN   A 1 20  ? 32.989  -5.145  29.688  1.00 24.32 ? 20  GLN   A CB   1 
ATOM   279  C  CG   . GLN   A 1 20  ? 33.741  -3.835  29.820  1.00 25.35 ? 20  GLN   A CG   1 
ATOM   280  C  CD   . GLN   A 1 20  ? 35.169  -4.025  30.274  1.00 34.17 ? 20  GLN   A CD   1 
ATOM   281  O  OE1  . GLN   A 1 20  ? 35.471  -4.937  31.042  1.00 34.05 ? 20  GLN   A OE1  1 
ATOM   282  N  NE2  . GLN   A 1 20  ? 36.054  -3.140  29.831  1.00 40.00 ? 20  GLN   A NE2  1 
ATOM   283  H  H    . GLN   A 1 20  ? 31.252  -6.899  28.587  1.00 25.43 ? 20  GLN   A H    1 
ATOM   284  H  HA   . GLN   A 1 20  ? 31.175  -4.284  29.318  1.00 26.11 ? 20  GLN   A HA   1 
ATOM   285  H  HB2  . GLN   A 1 20  ? 32.793  -5.469  30.581  1.00 29.20 ? 20  GLN   A HB2  1 
ATOM   286  H  HB3  . GLN   A 1 20  ? 33.563  -5.775  29.226  1.00 29.20 ? 20  GLN   A HB3  1 
ATOM   287  H  HG2  . GLN   A 1 20  ? 33.762  -3.385  28.962  1.00 30.44 ? 20  GLN   A HG2  1 
ATOM   288  H  HG3  . GLN   A 1 20  ? 33.291  -3.278  30.475  1.00 30.44 ? 20  GLN   A HG3  1 
ATOM   289  H  HE21 . GLN   A 1 20  ? 35.804  -2.512  29.300  1.00 48.02 ? 20  GLN   A HE21 1 
ATOM   290  H  HE22 . GLN   A 1 20  ? 36.879  -3.203  30.064  1.00 48.02 ? 20  GLN   A HE22 1 
ATOM   291  N  N    . PHE   A 1 21  ? 31.590  -3.374  27.131  1.00 18.74 ? 21  PHE   A N    1 
ATOM   292  C  CA   . PHE   A 1 21  ? 32.037  -2.721  25.909  1.00 19.20 ? 21  PHE   A CA   1 
ATOM   293  C  C    . PHE   A 1 21  ? 33.501  -2.350  26.092  1.00 21.06 ? 21  PHE   A C    1 
ATOM   294  O  O    . PHE   A 1 21  ? 33.842  -1.561  26.981  1.00 22.40 ? 21  PHE   A O    1 
ATOM   295  C  CB   . PHE   A 1 21  ? 31.182  -1.489  25.637  1.00 19.03 ? 21  PHE   A CB   1 
ATOM   296  C  CG   . PHE   A 1 21  ? 29.732  -1.820  25.429  1.00 17.80 ? 21  PHE   A CG   1 
ATOM   297  C  CD1  . PHE   A 1 21  ? 29.287  -2.362  24.237  1.00 18.44 ? 21  PHE   A CD1  1 
ATOM   298  C  CD2  . PHE   A 1 21  ? 28.821  -1.632  26.457  1.00 18.91 ? 21  PHE   A CD2  1 
ATOM   299  C  CE1  . PHE   A 1 21  ? 27.959  -2.684  24.068  1.00 18.92 ? 21  PHE   A CE1  1 
ATOM   300  C  CE2  . PHE   A 1 21  ? 27.493  -1.958  26.295  1.00 15.89 ? 21  PHE   A CE2  1 
ATOM   301  C  CZ   . PHE   A 1 21  ? 27.058  -2.477  25.102  1.00 18.13 ? 21  PHE   A CZ   1 
ATOM   302  H  H    . PHE   A 1 21  ? 31.057  -2.891  27.602  1.00 22.51 ? 21  PHE   A H    1 
ATOM   303  H  HA   . PHE   A 1 21  ? 31.958  -3.331  25.159  1.00 23.06 ? 21  PHE   A HA   1 
ATOM   304  H  HB2  . PHE   A 1 21  ? 31.246  -0.887  26.395  1.00 22.85 ? 21  PHE   A HB2  1 
ATOM   305  H  HB3  . PHE   A 1 21  ? 31.507  -1.050  24.836  1.00 22.85 ? 21  PHE   A HB3  1 
ATOM   306  H  HD1  . PHE   A 1 21  ? 29.888  -2.501  23.541  1.00 22.14 ? 21  PHE   A HD1  1 
ATOM   307  H  HD2  . PHE   A 1 21  ? 29.111  -1.279  27.267  1.00 22.72 ? 21  PHE   A HD2  1 
ATOM   308  H  HE1  . PHE   A 1 21  ? 27.666  -3.038  23.260  1.00 22.72 ? 21  PHE   A HE1  1 
ATOM   309  H  HE2  . PHE   A 1 21  ? 26.890  -1.816  26.989  1.00 19.09 ? 21  PHE   A HE2  1 
ATOM   310  H  HZ   . PHE   A 1 21  ? 26.161  -2.694  24.988  1.00 21.77 ? 21  PHE   A HZ   1 
ATOM   311  N  N    . GLY   A 1 22  ? 34.377  -2.959  25.301  1.00 21.28 ? 22  GLY   A N    1 
ATOM   312  C  CA   . GLY   A 1 22  ? 35.803  -2.860  25.518  1.00 21.89 ? 22  GLY   A CA   1 
ATOM   313  C  C    . GLY   A 1 22  ? 36.460  -4.169  25.883  1.00 19.72 ? 22  GLY   A C    1 
ATOM   314  O  O    . GLY   A 1 22  ? 37.695  -4.215  25.970  1.00 23.78 ? 22  GLY   A O    1 
ATOM   315  H  H    . GLY   A 1 22  ? 34.161  -3.442  24.623  1.00 25.55 ? 22  GLY   A H    1 
ATOM   316  H  HA2  . GLY   A 1 22  ? 36.223  -2.528  24.709  1.00 26.28 ? 22  GLY   A HA2  1 
ATOM   317  H  HA3  . GLY   A 1 22  ? 35.979  -2.226  26.230  1.00 26.28 ? 22  GLY   A HA3  1 
ATOM   318  N  N    . LYS   A 1 23  ? 35.674  -5.216  26.129  1.00 21.65 ? 23  LYS   A N    1 
ATOM   319  C  CA   . LYS   A 1 23  ? 36.229  -6.552  26.464  1.00 24.10 ? 23  LYS   A CA   1 
ATOM   320  C  C    . LYS   A 1 23  ? 35.391  -7.635  25.779  1.00 27.34 ? 23  LYS   A C    1 
ATOM   321  O  O    . LYS   A 1 23  ? 35.967  -8.406  24.986  1.00 28.71 ? 23  LYS   A O    1 
ATOM   322  C  CB   . LYS   A 1 23  ? 36.247  -6.736  27.984  1.00 28.30 ? 23  LYS   A CB   1 
ATOM   323  C  CG   . LYS   A 1 23  ? 36.908  -8.015  28.461  1.00 35.94 ? 23  LYS   A CG   1 
ATOM   324  C  CD   . LYS   A 1 23  ? 36.735  -8.264  29.952  1.00 50.58 ? 23  LYS   A CD   1 
ATOM   325  C  CE   . LYS   A 1 23  ? 37.626  -9.351  30.456  1.00 60.33 ? 23  LYS   A CE   1 
ATOM   326  N  NZ   . LYS   A 1 23  ? 37.378  -10.628 29.784  1.00 74.36 ? 23  LYS   A NZ   1 
ATOM   327  H  H    . LYS   A 1 23  ? 34.815  -5.191  26.112  1.00 26.00 ? 23  LYS   A H    1 
ATOM   328  H  HA   . LYS   A 1 23  ? 37.140  -6.616  26.136  1.00 28.94 ? 23  LYS   A HA   1 
ATOM   329  H  HB2  . LYS   A 1 23  ? 36.726  -5.992  28.381  1.00 33.98 ? 23  LYS   A HB2  1 
ATOM   330  H  HB3  . LYS   A 1 23  ? 35.332  -6.744  28.304  1.00 33.98 ? 23  LYS   A HB3  1 
ATOM   331  H  HG2  . LYS   A 1 23  ? 36.519  -8.767  27.988  1.00 43.15 ? 23  LYS   A HG2  1 
ATOM   332  H  HG3  . LYS   A 1 23  ? 37.859  -7.965  28.276  1.00 43.15 ? 23  LYS   A HG3  1 
ATOM   333  H  HD2  . LYS   A 1 23  ? 36.949  -7.451  30.436  1.00 60.71 ? 23  LYS   A HD2  1 
ATOM   334  H  HD3  . LYS   A 1 23  ? 35.816  -8.523  30.126  1.00 60.71 ? 23  LYS   A HD3  1 
ATOM   335  H  HE2  . LYS   A 1 23  ? 38.550  -9.102  30.299  1.00 72.42 ? 23  LYS   A HE2  1 
ATOM   336  H  HE3  . LYS   A 1 23  ? 37.470  -9.475  31.405  1.00 72.42 ? 23  LYS   A HE3  1 
ATOM   337  H  HZ1  . LYS   A 1 23  ? 37.534  -10.548 28.911  1.00 89.25 ? 23  LYS   A HZ1  1 
ATOM   338  H  HZ2  . LYS   A 1 23  ? 37.914  -11.256 30.117  1.00 89.25 ? 23  LYS   A HZ2  1 
ATOM   339  H  HZ3  . LYS   A 1 23  ? 36.532  -10.876 29.905  1.00 89.25 ? 23  LYS   A HZ3  1 
ATOM   340  N  N    . ASP   A 1 24  ? 34.095  -7.703  26.081  1.00 21.67 ? 24  ASP   A N    1 
ATOM   341  C  CA   . ASP   A 1 24  ? 33.203  -8.697  25.493  1.00 21.69 ? 24  ASP   A CA   1 
ATOM   342  C  C    . ASP   A 1 24  ? 32.707  -8.250  24.126  1.00 26.07 ? 24  ASP   A C    1 
ATOM   343  O  O    . ASP   A 1 24  ? 32.539  -9.072  23.216  1.00 28.50 ? 24  ASP   A O    1 
ATOM   344  C  CB   . ASP   A 1 24  ? 32.017  -8.922  26.428  1.00 27.81 ? 24  ASP   A CB   1 
ATOM   345  C  CG   . ASP   A 1 24  ? 32.434  -9.467  27.775  1.00 31.64 ? 24  ASP   A CG   1 
ATOM   346  O  OD1  . ASP   A 1 24  ? 33.098  -10.521 27.836  1.00 34.45 ? 24  ASP   A OD1  1 
ATOM   347  O  OD2  . ASP   A 1 24  ? 32.184  -8.762  28.775  1.00 25.82 ? 24  ASP   A OD2  1 
ATOM   348  H  H    . ASP   A 1 24  ? 33.703  -7.174  26.634  1.00 26.02 ? 24  ASP   A H    1 
ATOM   349  H  HA   . ASP   A 1 24  ? 33.677  -9.537  25.389  1.00 26.05 ? 24  ASP   A HA   1 
ATOM   350  H  HB2  . ASP   A 1 24  ? 31.564  -8.077  26.573  1.00 33.39 ? 24  ASP   A HB2  1 
ATOM   351  H  HB3  . ASP   A 1 24  ? 31.410  -9.559  26.021  1.00 33.39 ? 24  ASP   A HB3  1 
ATOM   352  N  N    . LEU   A 1 25  ? 32.451  -6.961  23.979  1.00 21.82 ? 25  LEU   A N    1 
ATOM   353  C  CA   . LEU   A 1 25  ? 31.917  -6.330  22.787  1.00 20.22 ? 25  LEU   A CA   1 
ATOM   354  C  C    . LEU   A 1 25  ? 32.807  -5.147  22.457  1.00 20.94 ? 25  LEU   A C    1 
ATOM   355  O  O    . LEU   A 1 25  ? 33.576  -4.686  23.307  1.00 22.84 ? 25  LEU   A O    1 
ATOM   356  C  CB   . LEU   A 1 25  ? 30.478  -5.856  23.026  1.00 22.49 ? 25  LEU   A CB   1 
ATOM   357  C  CG   . LEU   A 1 25  ? 29.437  -6.975  23.108  1.00 25.59 ? 25  LEU   A CG   1 
ATOM   358  C  CD1  . LEU   A 1 25  ? 28.098  -6.393  23.552  1.00 26.22 ? 25  LEU   A CD1  1 
ATOM   359  C  CD2  . LEU   A 1 25  ? 29.313  -7.713  21.785  1.00 28.34 ? 25  LEU   A CD2  1 
ATOM   360  H  H    . LEU   A 1 25  ? 32.591  -6.391  24.608  1.00 26.20 ? 25  LEU   A H    1 
ATOM   361  H  HA   . LEU   A 1 25  ? 31.932  -6.958  22.049  1.00 24.28 ? 25  LEU   A HA   1 
ATOM   362  H  HB2  . LEU   A 1 25  ? 30.449  -5.368  23.864  1.00 27.00 ? 25  LEU   A HB2  1 
ATOM   363  H  HB3  . LEU   A 1 25  ? 30.220  -5.269  22.298  1.00 27.00 ? 25  LEU   A HB3  1 
ATOM   364  H  HG   . LEU   A 1 25  ? 29.719  -7.616  23.779  1.00 30.73 ? 25  LEU   A HG   1 
ATOM   365  H  HD11 . LEU   A 1 25  ? 27.446  -7.109  23.606  1.00 31.49 ? 25  LEU   A HD11 1 
ATOM   366  H  HD12 . LEU   A 1 25  ? 28.207  -5.978  24.422  1.00 31.49 ? 25  LEU   A HD12 1 
ATOM   367  H  HD13 . LEU   A 1 25  ? 27.811  -5.732  22.903  1.00 31.49 ? 25  LEU   A HD13 1 
ATOM   368  H  HD21 . LEU   A 1 25  ? 28.546  -8.305  21.825  1.00 34.02 ? 25  LEU   A HD21 1 
ATOM   369  H  HD22 . LEU   A 1 25  ? 29.194  -7.065  21.073  1.00 34.02 ? 25  LEU   A HD22 1 
ATOM   370  H  HD23 . LEU   A 1 25  ? 30.121  -8.228  21.632  1.00 34.02 ? 25  LEU   A HD23 1 
ATOM   371  N  N    . PRO   A 1 26  ? 32.725  -4.623  21.239  1.00 19.59 ? 26  PRO   A N    1 
ATOM   372  C  CA   . PRO   A 1 26  ? 33.521  -3.440  20.898  1.00 20.27 ? 26  PRO   A CA   1 
ATOM   373  C  C    . PRO   A 1 26  ? 33.202  -2.239  21.772  1.00 21.06 ? 26  PRO   A C    1 
ATOM   374  O  O    . PRO   A 1 26  ? 32.141  -2.146  22.398  1.00 22.85 ? 26  PRO   A O    1 
ATOM   375  C  CB   . PRO   A 1 26  ? 33.139  -3.163  19.433  1.00 23.56 ? 26  PRO   A CB   1 
ATOM   376  C  CG   . PRO   A 1 26  ? 32.681  -4.519  18.927  1.00 23.72 ? 26  PRO   A CG   1 
ATOM   377  C  CD   . PRO   A 1 26  ? 31.905  -5.073  20.096  1.00 21.04 ? 26  PRO   A CD   1 
ATOM   378  H  HA   . PRO   A 1 26  ? 34.469  -3.640  20.954  1.00 24.34 ? 26  PRO   A HA   1 
ATOM   379  H  HB2  . PRO   A 1 26  ? 32.418  -2.515  19.395  1.00 28.29 ? 26  PRO   A HB2  1 
ATOM   380  H  HB3  . PRO   A 1 26  ? 33.915  -2.852  18.941  1.00 28.29 ? 26  PRO   A HB3  1 
ATOM   381  H  HG2  . PRO   A 1 26  ? 32.111  -4.409  18.150  1.00 28.48 ? 26  PRO   A HG2  1 
ATOM   382  H  HG3  . PRO   A 1 26  ? 33.449  -5.075  18.723  1.00 28.48 ? 26  PRO   A HG3  1 
ATOM   383  H  HD2  . PRO   A 1 26  ? 31.018  -4.682  20.135  1.00 25.27 ? 26  PRO   A HD2  1 
ATOM   384  H  HD3  . PRO   A 1 26  ? 31.872  -6.041  20.051  1.00 25.27 ? 26  PRO   A HD3  1 
ATOM   385  N  N    . LEU   A 1 27  ? 34.138  -1.298  21.778  1.00 22.45 ? 27  LEU   A N    1 
ATOM   386  C  CA   . LEU   A 1 27  ? 33.921  0.005   22.393  1.00 21.56 ? 27  LEU   A CA   1 
ATOM   387  C  C    . LEU   A 1 27  ? 32.789  0.739   21.689  1.00 23.67 ? 27  LEU   A C    1 
ATOM   388  O  O    . LEU   A 1 27  ? 32.501  0.499   20.512  1.00 22.52 ? 27  LEU   A O    1 
ATOM   389  C  CB   . LEU   A 1 27  ? 35.212  0.813   22.304  1.00 22.34 ? 27  LEU   A CB   1 
ATOM   390  C  CG   . LEU   A 1 27  ? 36.316  0.358   23.258  1.00 22.00 ? 27  LEU   A CG   1 
ATOM   391  C  CD1  . LEU   A 1 27  ? 37.629  1.059   22.858  1.00 28.67 ? 27  LEU   A CD1  1 
ATOM   392  C  CD2  . LEU   A 1 27  ? 36.031  0.612   24.722  1.00 26.63 ? 27  LEU   A CD2  1 
ATOM   393  H  H    . LEU   A 1 27  ? 34.918  -1.391  21.428  1.00 26.96 ? 27  LEU   A H    1 
ATOM   394  H  HA   . LEU   A 1 27  ? 33.686  -0.108  23.327  1.00 25.89 ? 27  LEU   A HA   1 
ATOM   395  H  HB2  . LEU   A 1 27  ? 35.558  0.745   21.400  1.00 26.82 ? 27  LEU   A HB2  1 
ATOM   396  H  HB3  . LEU   A 1 27  ? 35.012  1.740   22.508  1.00 26.82 ? 27  LEU   A HB3  1 
ATOM   397  H  HG   . LEU   A 1 27  ? 36.447  -0.597  23.146  1.00 26.42 ? 27  LEU   A HG   1 
ATOM   398  H  HD11 . LEU   A 1 27  ? 38.333  0.779   23.464  1.00 34.42 ? 27  LEU   A HD11 1 
ATOM   399  H  HD12 . LEU   A 1 27  ? 37.856  0.809   21.949  1.00 34.42 ? 27  LEU   A HD12 1 
ATOM   400  H  HD13 . LEU   A 1 27  ? 37.504  2.019   22.916  1.00 34.42 ? 27  LEU   A HD13 1 
ATOM   401  H  HD21 . LEU   A 1 27  ? 36.801  0.340   25.245  1.00 31.98 ? 27  LEU   A HD21 1 
ATOM   402  H  HD22 . LEU   A 1 27  ? 35.861  1.558   24.850  1.00 31.98 ? 27  LEU   A HD22 1 
ATOM   403  H  HD23 . LEU   A 1 27  ? 35.253  0.097   24.987  1.00 31.98 ? 27  LEU   A HD23 1 
ATOM   404  N  N    . LEU   A 1 28  ? 32.149  1.643   22.419  1.00 20.95 ? 28  LEU   A N    1 
ATOM   405  C  CA   . LEU   A 1 28  ? 31.040  2.428   21.909  1.00 19.05 ? 28  LEU   A CA   1 
ATOM   406  C  C    . LEU   A 1 28  ? 31.569  3.660   21.186  1.00 19.38 ? 28  LEU   A C    1 
ATOM   407  O  O    . LEU   A 1 28  ? 32.601  4.225   21.560  1.00 21.76 ? 28  LEU   A O    1 
ATOM   408  C  CB   . LEU   A 1 28  ? 30.142  2.865   23.061  1.00 18.81 ? 28  LEU   A CB   1 
ATOM   409  C  CG   . LEU   A 1 28  ? 29.469  1.747   23.855  1.00 18.35 ? 28  LEU   A CG   1 
ATOM   410  C  CD1  . LEU   A 1 28  ? 28.901  2.334   25.147  1.00 19.49 ? 28  LEU   A CD1  1 
ATOM   411  C  CD2  . LEU   A 1 28  ? 28.389  1.070   23.061  1.00 21.51 ? 28  LEU   A CD2  1 
ATOM   412  H  H    . LEU   A 1 28  ? 32.347  1.823   23.236  1.00 25.15 ? 28  LEU   A H    1 
ATOM   413  H  HA   . LEU   A 1 28  ? 30.518  1.898   21.287  1.00 22.88 ? 28  LEU   A HA   1 
ATOM   414  H  HB2  . LEU   A 1 28  ? 30.677  3.380   23.685  1.00 22.59 ? 28  LEU   A HB2  1 
ATOM   415  H  HB3  . LEU   A 1 28  ? 29.438  3.427   22.701  1.00 22.59 ? 28  LEU   A HB3  1 
ATOM   416  H  HG   . LEU   A 1 28  ? 30.133  1.081   24.092  1.00 22.04 ? 28  LEU   A HG   1 
ATOM   417  H  HD11 . LEU   A 1 28  ? 28.459  1.629   25.646  1.00 23.41 ? 28  LEU   A HD11 1 
ATOM   418  H  HD12 . LEU   A 1 28  ? 29.628  2.705   25.671  1.00 23.41 ? 28  LEU   A HD12 1 
ATOM   419  H  HD13 . LEU   A 1 28  ? 28.264  3.031   24.924  1.00 23.41 ? 28  LEU   A HD13 1 
ATOM   420  H  HD21 . LEU   A 1 28  ? 27.980  0.382   23.608  1.00 25.83 ? 28  LEU   A HD21 1 
ATOM   421  H  HD22 . LEU   A 1 28  ? 27.725  1.729   22.806  1.00 25.83 ? 28  LEU   A HD22 1 
ATOM   422  H  HD23 . LEU   A 1 28  ? 28.782  0.673   22.268  1.00 25.83 ? 28  LEU   A HD23 1 
ATOM   423  N  N    . GLU   A 1 29  ? 30.846  4.081   20.151  1.00 22.69 ? 29  GLU   A N    1 
ATOM   424  C  CA   . GLU   A 1 29  ? 31.221  5.261   19.373  1.00 24.49 ? 29  GLU   A CA   1 
ATOM   425  C  C    . GLU   A 1 29  ? 30.535  6.481   19.979  1.00 20.64 ? 29  GLU   A C    1 
ATOM   426  O  O    . GLU   A 1 29  ? 29.307  6.598   19.929  1.00 21.75 ? 29  GLU   A O    1 
ATOM   427  C  CB   . GLU   A 1 29  ? 30.826  5.095   17.906  1.00 34.69 ? 29  GLU   A CB   1 
ATOM   428  C  CG   . GLU   A 1 29  ? 30.939  3.672   17.372  1.00 41.26 ? 29  GLU   A CG   1 
ATOM   429  C  CD   . GLU   A 1 29  ? 32.366  3.252   17.077  1.00 52.23 ? 29  GLU   A CD   1 
ATOM   430  O  OE1  . GLU   A 1 29  ? 33.285  4.062   17.318  1.00 47.47 ? 29  GLU   A OE1  1 
ATOM   431  O  OE2  . GLU   A 1 29  ? 32.571  2.110   16.615  1.00 56.11 ? 29  GLU   A OE2  1 
ATOM   432  H  H    . GLU   A 1 29  ? 30.124  3.700   19.881  1.00 27.25 ? 29  GLU   A H    1 
ATOM   433  H  HA   . GLU   A 1 29  ? 32.181  5.391   19.421  1.00 29.41 ? 29  GLU   A HA   1 
ATOM   434  H  HB2  . GLU   A 1 29  ? 29.903  5.374   17.801  1.00 41.65 ? 29  GLU   A HB2  1 
ATOM   435  H  HB3  . GLU   A 1 29  ? 31.400  5.659   17.365  1.00 41.65 ? 29  GLU   A HB3  1 
ATOM   436  H  HG2  . GLU   A 1 29  ? 30.564  3.043   18.006  1.00 49.53 ? 29  GLU   A HG2  1 
ATOM   437  H  HG3  . GLU   A 1 29  ? 30.445  3.620   16.539  1.00 49.53 ? 29  GLU   A HG3  1 
ATOM   438  N  N    . ILE   A 1 30  ? 31.323  7.401   20.533  1.00 26.25 ? 30  ILE   A N    1 
ATOM   439  C  CA   . ILE   A 1 30  ? 30.802  8.586   21.197  1.00 25.81 ? 30  ILE   A CA   1 
ATOM   440  C  C    . ILE   A 1 30  ? 31.478  9.824   20.613  1.00 24.24 ? 30  ILE   A C    1 
ATOM   441  O  O    . ILE   A 1 30  ? 32.267  9.736   19.671  1.00 26.74 ? 30  ILE   A O    1 
ATOM   442  C  CB   . ILE   A 1 30  ? 30.995  8.522   22.724  1.00 21.32 ? 30  ILE   A CB   1 
ATOM   443  C  CG1  . ILE   A 1 30  ? 32.469  8.355   23.074  1.00 24.02 ? 30  ILE   A CG1  1 
ATOM   444  C  CG2  . ILE   A 1 30  ? 30.216  7.347   23.300  1.00 22.70 ? 30  ILE   A CG2  1 
ATOM   445  C  CD1  . ILE   A 1 30  ? 32.788  8.644   24.526  1.00 26.72 ? 30  ILE   A CD1  1 
ATOM   446  H  H    . ILE   A 1 30  ? 32.182  7.357   20.535  1.00 31.51 ? 30  ILE   A H    1 
ATOM   447  H  HA   . ILE   A 1 30  ? 29.851  8.657   21.021  1.00 30.99 ? 30  ILE   A HA   1 
ATOM   448  H  HB   . ILE   A 1 30  ? 30.666  9.343   23.122  1.00 25.61 ? 30  ILE   A HB   1 
ATOM   449  H  HG12 . ILE   A 1 30  ? 32.730  7.439   22.891  1.00 28.84 ? 30  ILE   A HG12 1 
ATOM   450  H  HG13 . ILE   A 1 30  ? 32.998  8.959   22.533  1.00 28.84 ? 30  ILE   A HG13 1 
ATOM   451  H  HG21 . ILE   A 1 30  ? 30.291  7.361   24.267  1.00 27.26 ? 30  ILE   A HG21 1 
ATOM   452  H  HG22 . ILE   A 1 30  ? 29.285  7.429   23.039  1.00 27.26 ? 30  ILE   A HG22 1 
ATOM   453  H  HG23 . ILE   A 1 30  ? 30.586  6.521   22.951  1.00 27.26 ? 30  ILE   A HG23 1 
ATOM   454  H  HD11 . ILE   A 1 30  ? 33.747  8.578   24.657  1.00 32.09 ? 30  ILE   A HD11 1 
ATOM   455  H  HD12 . ILE   A 1 30  ? 32.485  9.540   24.743  1.00 32.09 ? 30  ILE   A HD12 1 
ATOM   456  H  HD13 . ILE   A 1 30  ? 32.332  7.996   25.085  1.00 32.09 ? 30  ILE   A HD13 1 
ATOM   457  N  N    . THR   A 1 31  ? 31.157  10.987  21.185  1.00 24.94 ? 31  THR   A N    1 
ATOM   458  C  CA   . THR   A 1 31  ? 31.751  12.248  20.762  1.00 28.95 ? 31  THR   A CA   1 
ATOM   459  C  C    . THR   A 1 31  ? 32.224  13.013  21.993  1.00 28.80 ? 31  THR   A C    1 
ATOM   460  O  O    . THR   A 1 31  ? 31.701  12.829  23.096  1.00 25.87 ? 31  THR   A O    1 
ATOM   461  C  CB   . THR   A 1 31  ? 30.767  13.120  19.966  1.00 34.24 ? 31  THR   A CB   1 
ATOM   462  O  OG1  . THR   A 1 31  ? 29.438  13.007  20.486  1.00 33.73 ? 31  THR   A OG1  1 
ATOM   463  C  CG2  . THR   A 1 31  ? 30.723  12.674  18.510  1.00 33.41 ? 31  THR   A CG2  1 
ATOM   464  H  H    . THR   A 1 31  ? 30.591  11.069  21.827  1.00 29.95 ? 31  THR   A H    1 
ATOM   465  H  HA   . THR   A 1 31  ? 32.522  12.070  20.201  1.00 34.76 ? 31  THR   A HA   1 
ATOM   466  H  HB   . THR   A 1 31  ? 31.052  14.047  19.998  1.00 41.11 ? 31  THR   A HB   1 
ATOM   467  H  HG1  . THR   A 1 31  ? 29.164  12.217  20.408  1.00 40.49 ? 31  THR   A HG1  1 
ATOM   468  H  HG21 . THR   A 1 31  ? 30.098  13.225  18.013  1.00 40.11 ? 31  THR   A HG21 1 
ATOM   469  H  HG22 . THR   A 1 31  ? 31.603  12.757  18.111  1.00 40.11 ? 31  THR   A HG22 1 
ATOM   470  H  HG23 . THR   A 1 31  ? 30.439  11.748  18.456  1.00 40.11 ? 31  THR   A HG23 1 
ATOM   471  N  N    . ARG   A 1 32  ? 33.217  13.884  21.806  1.00 28.06 ? 32  ARG   A N    1 
ATOM   472  C  CA   . ARG   A 1 32  ? 33.782  14.621  22.928  1.00 28.07 ? 32  ARG   A CA   1 
ATOM   473  C  C    . ARG   A 1 32  ? 34.029  16.073  22.536  1.00 33.48 ? 32  ARG   A C    1 
ATOM   474  O  O    . ARG   A 1 32  ? 34.434  16.358  21.405  1.00 36.45 ? 32  ARG   A O    1 
ATOM   475  C  CB   . ARG   A 1 32  ? 35.104  13.987  23.396  1.00 30.69 ? 32  ARG   A CB   1 
ATOM   476  C  CG   . ARG   A 1 32  ? 35.856  14.765  24.474  1.00 33.47 ? 32  ARG   A CG   1 
ATOM   477  C  CD   . ARG   A 1 32  ? 36.854  13.862  25.201  1.00 33.81 ? 32  ARG   A CD   1 
ATOM   478  N  NE   . ARG   A 1 32  ? 37.354  14.421  26.452  1.00 33.29 ? 32  ARG   A NE   1 
ATOM   479  C  CZ   . ARG   A 1 32  ? 38.519  15.042  26.596  1.00 36.90 ? 32  ARG   A CZ   1 
ATOM   480  N  NH1  . ARG   A 1 32  ? 39.284  15.326  25.554  1.00 39.35 ? 32  ARG   A NH1  1 
ATOM   481  N  NH2  . ARG   A 1 32  ? 38.923  15.384  27.815  1.00 37.28 ? 32  ARG   A NH2  1 
ATOM   482  H  H    . ARG   A 1 32  ? 33.576  14.063  21.045  1.00 33.69 ? 32  ARG   A H    1 
ATOM   483  H  HA   . ARG   A 1 32  ? 33.159  14.611  23.671  1.00 33.70 ? 32  ARG   A HA   1 
ATOM   484  H  HB2  . ARG   A 1 32  ? 34.911  13.105  23.751  1.00 36.84 ? 32  ARG   A HB2  1 
ATOM   485  H  HB3  . ARG   A 1 32  ? 35.694  13.906  22.630  1.00 36.84 ? 32  ARG   A HB3  1 
ATOM   486  H  HG2  . ARG   A 1 32  ? 36.346  15.494  24.063  1.00 40.19 ? 32  ARG   A HG2  1 
ATOM   487  H  HG3  . ARG   A 1 32  ? 35.223  15.108  25.124  1.00 40.19 ? 32  ARG   A HG3  1 
ATOM   488  H  HD2  . ARG   A 1 32  ? 36.414  13.024  25.415  1.00 40.60 ? 32  ARG   A HD2  1 
ATOM   489  H  HD3  . ARG   A 1 32  ? 37.608  13.691  24.617  1.00 40.60 ? 32  ARG   A HD3  1 
ATOM   490  H  HE   . ARG   A 1 32  ? 36.857  14.342  27.149  1.00 39.97 ? 32  ARG   A HE   1 
ATOM   491  H  HH11 . ARG   A 1 32  ? 39.037  15.107  24.761  1.00 47.23 ? 32  ARG   A HH11 1 
ATOM   492  H  HH12 . ARG   A 1 32  ? 40.033  15.732  25.672  1.00 47.23 ? 32  ARG   A HH12 1 
ATOM   493  H  HH21 . ARG   A 1 32  ? 38.430  15.207  28.497  1.00 44.76 ? 32  ARG   A HH21 1 
ATOM   494  H  HH22 . ARG   A 1 32  ? 39.672  15.794  27.921  1.00 44.76 ? 32  ARG   A HH22 1 
ATOM   495  N  N    . ASP   A 1 33  ? 33.766  16.981  23.476  1.00 33.00 ? 33  ASP   A N    1 
ATOM   496  C  CA   . ASP   A 1 33  ? 34.167  18.386  23.383  1.00 35.45 ? 33  ASP   A CA   1 
ATOM   497  C  C    . ASP   A 1 33  ? 35.343  18.578  24.334  1.00 33.98 ? 33  ASP   A C    1 
ATOM   498  O  O    . ASP   A 1 33  ? 35.154  18.806  25.534  1.00 37.88 ? 33  ASP   A O    1 
ATOM   499  C  CB   . ASP   A 1 33  ? 33.022  19.331  23.724  1.00 35.02 ? 33  ASP   A CB   1 
ATOM   500  C  CG   . ASP   A 1 33  ? 33.403  20.790  23.536  1.00 40.63 ? 33  ASP   A CG   1 
ATOM   501  O  OD1  . ASP   A 1 33  ? 34.601  21.073  23.304  1.00 40.34 ? 33  ASP   A OD1  1 
ATOM   502  O  OD2  . ASP   A 1 33  ? 32.511  21.660  23.629  1.00 44.68 ? 33  ASP   A OD2  1 
ATOM   503  H  H    . ASP   A 1 33  ? 33.342  16.800  24.202  1.00 39.62 ? 33  ASP   A H    1 
ATOM   504  H  HA   . ASP   A 1 33  ? 34.466  18.579  22.481  1.00 42.55 ? 33  ASP   A HA   1 
ATOM   505  H  HB2  . ASP   A 1 33  ? 32.269  19.139  23.144  1.00 42.05 ? 33  ASP   A HB2  1 
ATOM   506  H  HB3  . ASP   A 1 33  ? 32.770  19.202  24.652  1.00 42.05 ? 33  ASP   A HB3  1 
ATOM   507  N  N    . SER   A 1 34  ? 36.557  18.504  23.786  1.00 39.62 ? 34  SER   A N    1 
ATOM   508  C  CA   . SER   A 1 34  ? 37.752  18.474  24.620  1.00 39.11 ? 34  SER   A CA   1 
ATOM   509  C  C    . SER   A 1 34  ? 37.939  19.769  25.396  1.00 42.85 ? 34  SER   A C    1 
ATOM   510  O  O    . SER   A 1 34  ? 38.575  19.768  26.456  1.00 45.08 ? 34  SER   A O    1 
ATOM   511  C  CB   . SER   A 1 34  ? 38.967  18.196  23.738  1.00 49.29 ? 34  SER   A CB   1 
ATOM   512  O  OG   . SER   A 1 34  ? 38.895  16.883  23.212  1.00 59.60 ? 34  SER   A OG   1 
ATOM   513  H  H    . SER   A 1 34  ? 36.712  18.470  22.941  1.00 47.56 ? 34  SER   A H    1 
ATOM   514  H  HA   . SER   A 1 34  ? 37.673  17.749  25.260  1.00 46.95 ? 34  SER   A HA   1 
ATOM   515  H  HB2  . SER   A 1 34  ? 38.981  18.832  23.006  1.00 59.17 ? 34  SER   A HB2  1 
ATOM   516  H  HB3  . SER   A 1 34  ? 39.773  18.282  24.271  1.00 59.17 ? 34  SER   A HB3  1 
ATOM   517  H  HG   . SER   A 1 34  ? 39.564  16.731  22.727  1.00 71.54 ? 34  SER   A HG   1 
ATOM   518  N  N    . SER   A 1 35  ? 37.395  20.878  24.892  1.00 42.71 ? 35  SER   A N    1 
ATOM   519  C  CA   . SER   A 1 35  ? 37.565  22.156  25.573  1.00 45.49 ? 35  SER   A CA   1 
ATOM   520  C  C    . SER   A 1 35  ? 36.910  22.159  26.944  1.00 44.40 ? 35  SER   A C    1 
ATOM   521  O  O    . SER   A 1 35  ? 37.409  22.814  27.868  1.00 45.50 ? 35  SER   A O    1 
ATOM   522  C  CB   . SER   A 1 35  ? 36.976  23.278  24.719  1.00 45.31 ? 35  SER   A CB   1 
ATOM   523  O  OG   . SER   A 1 35  ? 35.616  23.501  25.065  1.00 55.52 ? 35  SER   A OG   1 
ATOM   524  H  H    . SER   A 1 35  ? 36.931  20.915  24.169  1.00 51.27 ? 35  SER   A H    1 
ATOM   525  H  HA   . SER   A 1 35  ? 38.512  22.330  25.690  1.00 54.61 ? 35  SER   A HA   1 
ATOM   526  H  HB2  . SER   A 1 35  ? 37.480  24.092  24.874  1.00 54.39 ? 35  SER   A HB2  1 
ATOM   527  H  HB3  . SER   A 1 35  ? 37.029  23.027  23.784  1.00 54.39 ? 35  SER   A HB3  1 
ATOM   528  H  HG   . SER   A 1 35  ? 35.169  22.802  24.937  1.00 66.64 ? 35  SER   A HG   1 
ATOM   529  N  N    . VAL   A 1 36  ? 35.796  21.444  27.091  1.00 42.31 ? 36  VAL   A N    1 
ATOM   530  C  CA   . VAL   A 1 36  ? 35.021  21.421  28.321  1.00 39.14 ? 36  VAL   A CA   1 
ATOM   531  C  C    . VAL   A 1 36  ? 35.065  20.053  28.985  1.00 35.49 ? 36  VAL   A C    1 
ATOM   532  O  O    . VAL   A 1 36  ? 34.381  19.835  29.992  1.00 38.75 ? 36  VAL   A O    1 
ATOM   533  C  CB   . VAL   A 1 36  ? 33.568  21.853  28.061  1.00 43.64 ? 36  VAL   A CB   1 
ATOM   534  C  CG1  . VAL   A 1 36  ? 33.508  23.347  27.750  1.00 48.14 ? 36  VAL   A CG1  1 
ATOM   535  C  CG2  . VAL   A 1 36  ? 32.950  21.045  26.925  1.00 39.67 ? 36  VAL   A CG2  1 
ATOM   536  H  H    . VAL   A 1 36  ? 35.465  20.949  26.471  1.00 50.79 ? 36  VAL   A H    1 
ATOM   537  H  HA   . VAL   A 1 36  ? 35.406  22.058  28.943  1.00 46.99 ? 36  VAL   A HA   1 
ATOM   538  H  HB   . VAL   A 1 36  ? 33.044  21.693  28.861  1.00 52.39 ? 36  VAL   A HB   1 
ATOM   539  H  HG11 . VAL   A 1 36  ? 32.584  23.600  27.598  1.00 57.79 ? 36  VAL   A HG11 1 
ATOM   540  H  HG12 . VAL   A 1 36  ? 33.867  23.841  28.504  1.00 57.79 ? 36  VAL   A HG12 1 
ATOM   541  H  HG13 . VAL   A 1 36  ? 34.035  23.525  26.956  1.00 57.79 ? 36  VAL   A HG13 1 
ATOM   542  H  HG21 . VAL   A 1 36  ? 31.986  21.154  26.948  1.00 47.62 ? 36  VAL   A HG21 1 
ATOM   543  H  HG22 . VAL   A 1 36  ? 33.301  21.376  26.085  1.00 47.62 ? 36  VAL   A HG22 1 
ATOM   544  H  HG23 . VAL   A 1 36  ? 33.180  20.110  27.037  1.00 47.62 ? 36  VAL   A HG23 1 
ATOM   545  N  N    . GLU   A 1 37  ? 35.858  19.126  28.445  1.00 34.06 ? 37  GLU   A N    1 
ATOM   546  C  CA   . GLU   A 1 37  ? 35.964  17.767  28.973  1.00 33.91 ? 37  GLU   A CA   1 
ATOM   547  C  C    . GLU   A 1 37  ? 34.584  17.143  29.167  1.00 33.86 ? 37  GLU   A C    1 
ATOM   548  O  O    . GLU   A 1 37  ? 34.281  16.527  30.194  1.00 31.13 ? 37  GLU   A O    1 
ATOM   549  C  CB   . GLU   A 1 37  ? 36.787  17.748  30.262  1.00 40.31 ? 37  GLU   A CB   1 
ATOM   550  C  CG   . GLU   A 1 37  ? 38.211  18.247  30.061  1.00 39.09 ? 37  GLU   A CG   1 
ATOM   551  C  CD   . GLU   A 1 37  ? 39.076  18.073  31.292  1.00 49.37 ? 37  GLU   A CD   1 
ATOM   552  O  OE1  . GLU   A 1 37  ? 38.596  18.344  32.411  1.00 49.33 ? 37  GLU   A OE1  1 
ATOM   553  O  OE2  . GLU   A 1 37  ? 40.216  17.585  31.141  1.00 53.15 ? 37  GLU   A OE2  1 
ATOM   554  H  H    . GLU   A 1 37  ? 36.356  19.262  27.758  1.00 40.89 ? 37  GLU   A H    1 
ATOM   555  H  HA   . GLU   A 1 37  ? 36.436  17.224  28.322  1.00 40.71 ? 37  GLU   A HA   1 
ATOM   556  H  HB2  . GLU   A 1 37  ? 36.359  18.320  30.918  1.00 48.39 ? 37  GLU   A HB2  1 
ATOM   557  H  HB3  . GLU   A 1 37  ? 36.832  16.838  30.594  1.00 48.39 ? 37  GLU   A HB3  1 
ATOM   558  H  HG2  . GLU   A 1 37  ? 38.620  17.750  29.335  1.00 46.93 ? 37  GLU   A HG2  1 
ATOM   559  H  HG3  . GLU   A 1 37  ? 38.186  19.192  29.843  1.00 46.93 ? 37  GLU   A HG3  1 
ATOM   560  N  N    . MET   A 1 38  ? 33.746  17.314  28.146  1.00 32.31 ? 38  MET   A N    1 
ATOM   561  C  CA   A MET   A 1 38  ? 32.401  16.761  28.116  0.58 30.54 ? 38  MET   A CA   1 
ATOM   562  C  CA   B MET   A 1 38  ? 32.396  16.768  28.115  0.42 30.59 ? 38  MET   A CA   1 
ATOM   563  C  C    . MET   A 1 38  ? 32.280  15.767  26.973  1.00 26.43 ? 38  MET   A C    1 
ATOM   564  O  O    . MET   A 1 38  ? 32.775  16.012  25.866  1.00 29.16 ? 38  MET   A O    1 
ATOM   565  C  CB   A MET   A 1 38  ? 31.356  17.862  27.941  0.58 32.76 ? 38  MET   A CB   1 
ATOM   566  C  CB   B MET   A 1 38  ? 31.351  17.871  27.909  0.42 32.75 ? 38  MET   A CB   1 
ATOM   567  C  CG   A MET   A 1 38  ? 29.928  17.406  28.183  0.58 32.67 ? 38  MET   A CG   1 
ATOM   568  C  CG   B MET   A 1 38  ? 31.030  18.731  29.118  0.42 34.75 ? 38  MET   A CG   1 
ATOM   569  S  SD   A MET   A 1 38  ? 29.616  16.767  29.844  0.58 33.92 ? 38  MET   A SD   1 
ATOM   570  S  SD   B MET   A 1 38  ? 30.418  17.878  30.585  0.42 40.88 ? 38  MET   A SD   1 
ATOM   571  C  CE   A MET   A 1 38  ? 30.658  17.816  30.853  0.58 39.30 ? 38  MET   A CE   1 
ATOM   572  C  CE   B MET   A 1 38  ? 29.223  16.750  29.879  0.42 34.44 ? 38  MET   A CE   1 
ATOM   573  H  H    A MET   A 1 38  ? 33.944  17.761  27.439  0.58 38.79 ? 38  MET   A H    1 
ATOM   574  H  H    B MET   A 1 38  ? 33.947  17.758  27.438  0.42 38.79 ? 38  MET   A H    1 
ATOM   575  H  HA   A MET   A 1 38  ? 32.226  16.303  28.952  0.58 36.67 ? 38  MET   A HA   1 
ATOM   576  H  HA   B MET   A 1 38  ? 32.207  16.321  28.955  0.42 36.72 ? 38  MET   A HA   1 
ATOM   577  H  HB2  A MET   A 1 38  ? 31.555  18.590  28.549  0.58 39.33 ? 38  MET   A HB2  1 
ATOM   578  H  HB2  B MET   A 1 38  ? 31.671  18.464  27.212  0.42 39.32 ? 38  MET   A HB2  1 
ATOM   579  H  HB3  A MET   A 1 38  ? 31.404  18.185  27.028  0.58 39.33 ? 38  MET   A HB3  1 
ATOM   580  H  HB3  B MET   A 1 38  ? 30.524  17.456  27.619  0.42 39.32 ? 38  MET   A HB3  1 
ATOM   581  H  HG2  A MET   A 1 38  ? 29.334  18.160  28.042  0.58 39.22 ? 38  MET   A HG2  1 
ATOM   582  H  HG2  B MET   A 1 38  ? 31.838  19.202  29.377  0.42 41.72 ? 38  MET   A HG2  1 
ATOM   583  H  HG3  A MET   A 1 38  ? 29.716  16.701  27.552  0.58 39.22 ? 38  MET   A HG3  1 
ATOM   584  H  HG3  B MET   A 1 38  ? 30.353  19.376  28.859  0.42 41.72 ? 38  MET   A HG3  1 
ATOM   585  H  HE1  A MET   A 1 38  ? 30.451  17.658  31.787  0.58 47.17 ? 38  MET   A HE1  1 
ATOM   586  H  HE1  B MET   A 1 38  ? 28.764  16.287  30.597  0.42 41.35 ? 38  MET   A HE1  1 
ATOM   587  H  HE2  A MET   A 1 38  ? 31.588  17.603  30.681  0.58 47.17 ? 38  MET   A HE2  1 
ATOM   588  H  HE2  B MET   A 1 38  ? 28.586  17.256  29.351  0.42 41.35 ? 38  MET   A HE2  1 
ATOM   589  H  HE3  A MET   A 1 38  ? 30.483  18.743  30.629  0.58 47.17 ? 38  MET   A HE3  1 
ATOM   590  H  HE3  B MET   A 1 38  ? 29.686  16.110  29.316  0.42 41.35 ? 38  MET   A HE3  1 
ATOM   591  N  N    . CYS   A 1 39  ? 31.604  14.652  27.239  1.00 28.27 ? 39  CYS   A N    1 
ATOM   592  C  CA   . CYS   A 1 39  ? 31.367  13.622  26.240  1.00 25.85 ? 39  CYS   A CA   1 
ATOM   593  C  C    . CYS   A 1 39  ? 29.866  13.493  26.013  1.00 24.16 ? 39  CYS   A C    1 
ATOM   594  O  O    . CYS   A 1 39  ? 29.058  13.871  26.866  1.00 24.52 ? 39  CYS   A O    1 
ATOM   595  C  CB   . CYS   A 1 39  ? 31.950  12.281  26.685  1.00 24.79 ? 39  CYS   A CB   1 
ATOM   596  S  SG   . CYS   A 1 39  ? 33.721  12.105  26.348  1.00 25.99 ? 39  CYS   A SG   1 
ATOM   597  H  H    . CYS   A 1 39  ? 31.267  14.468  28.009  1.00 33.94 ? 39  CYS   A H    1 
ATOM   598  H  HA   . CYS   A 1 39  ? 31.784  13.875  25.402  1.00 31.04 ? 39  CYS   A HA   1 
ATOM   599  H  HB2  . CYS   A 1 39  ? 31.819  12.184  27.641  1.00 29.77 ? 39  CYS   A HB2  1 
ATOM   600  H  HB3  . CYS   A 1 39  ? 31.488  11.569  26.216  1.00 29.77 ? 39  CYS   A HB3  1 
ATOM   601  N  N    . PHE   A 1 40  ? 29.494  12.979  24.840  1.00 22.18 ? 40  PHE   A N    1 
ATOM   602  C  CA   . PHE   A 1 40  ? 28.065  12.839  24.466  1.00 22.55 ? 40  PHE   A CA   1 
ATOM   603  C  C    . PHE   A 1 40  ? 27.837  11.430  23.975  1.00 22.32 ? 40  PHE   A C    1 
ATOM   604  O  O    . PHE   A 1 40  ? 28.678  10.913  23.225  1.00 23.98 ? 40  PHE   A O    1 
ATOM   605  C  CB   . PHE   A 1 40  ? 27.742  13.890  23.404  1.00 26.88 ? 40  PHE   A CB   1 
ATOM   606  C  CG   . PHE   A 1 40  ? 28.173  15.293  23.803  1.00 27.62 ? 40  PHE   A CG   1 
ATOM   607  C  CD1  . PHE   A 1 40  ? 29.453  15.753  23.516  1.00 28.80 ? 40  PHE   A CD1  1 
ATOM   608  C  CD2  . PHE   A 1 40  ? 27.305  16.135  24.486  1.00 30.37 ? 40  PHE   A CD2  1 
ATOM   609  C  CE1  . PHE   A 1 40  ? 29.846  17.026  23.892  1.00 37.38 ? 40  PHE   A CE1  1 
ATOM   610  C  CE2  . PHE   A 1 40  ? 27.704  17.408  24.858  1.00 32.69 ? 40  PHE   A CE2  1 
ATOM   611  C  CZ   . PHE   A 1 40  ? 28.971  17.850  24.560  1.00 34.66 ? 40  PHE   A CZ   1 
ATOM   612  H  H    . PHE   A 1 40  ? 30.041  12.702  24.238  1.00 26.64 ? 40  PHE   A H    1 
ATOM   613  H  HA   . PHE   A 1 40  ? 27.504  12.995  25.241  1.00 27.08 ? 40  PHE   A HA   1 
ATOM   614  H  HB2  . PHE   A 1 40  ? 28.202  13.659  22.582  1.00 32.27 ? 40  PHE   A HB2  1 
ATOM   615  H  HB3  . PHE   A 1 40  ? 26.784  13.903  23.255  1.00 32.27 ? 40  PHE   A HB3  1 
ATOM   616  H  HD1  . PHE   A 1 40  ? 30.050  15.202  23.064  1.00 34.58 ? 40  PHE   A HD1  1 
ATOM   617  H  HD2  . PHE   A 1 40  ? 26.446  15.843  24.690  1.00 36.47 ? 40  PHE   A HD2  1 
ATOM   618  H  HE1  . PHE   A 1 40  ? 30.703  17.326  23.690  1.00 44.88 ? 40  PHE   A HE1  1 
ATOM   619  H  HE2  . PHE   A 1 40  ? 27.113  17.966  25.310  1.00 39.25 ? 40  PHE   A HE2  1 
ATOM   620  H  HZ   . PHE   A 1 40  ? 29.236  18.705  24.811  1.00 41.61 ? 40  PHE   A HZ   1 
ATOM   621  N  N    . MET   A 1 41  ? 26.732  10.818  24.387  1.00 20.85 ? 41  MET   A N    1 
ATOM   622  C  CA   . MET   A 1 41  ? 26.380  9.457   23.920  1.00 18.63 ? 41  MET   A CA   1 
ATOM   623  C  C    . MET   A 1 41  ? 25.814  9.624   22.513  1.00 18.76 ? 41  MET   A C    1 
ATOM   624  O  O    . MET   A 1 41  ? 24.633  9.370   22.336  1.00 21.23 ? 41  MET   A O    1 
ATOM   625  C  CB   . MET   A 1 41  ? 25.356  8.813   24.861  1.00 20.85 ? 41  MET   A CB   1 
ATOM   626  C  CG   . MET   A 1 41  ? 25.910  8.498   26.234  1.00 21.60 ? 41  MET   A CG   1 
ATOM   627  S  SD   . MET   A 1 41  ? 27.181  7.220   26.172  1.00 19.74 ? 41  MET   A SD   1 
ATOM   628  C  CE   . MET   A 1 41  ? 26.165  5.773   25.840  1.00 21.26 ? 41  MET   A CE   1 
ATOM   629  H  H    . MET   A 1 41  ? 26.164  11.159  24.935  1.00 25.04 ? 41  MET   A H    1 
ATOM   630  H  HA   . MET   A 1 41  ? 27.175  8.902   23.891  1.00 22.37 ? 41  MET   A HA   1 
ATOM   631  H  HB2  . MET   A 1 41  ? 24.610  9.422   24.973  1.00 25.04 ? 41  MET   A HB2  1 
ATOM   632  H  HB3  . MET   A 1 41  ? 25.046  7.984   24.466  1.00 25.04 ? 41  MET   A HB3  1 
ATOM   633  H  HG2  . MET   A 1 41  ? 26.306  9.300   26.610  1.00 25.93 ? 41  MET   A HG2  1 
ATOM   634  H  HG3  . MET   A 1 41  ? 25.191  8.182   26.803  1.00 25.93 ? 41  MET   A HG3  1 
ATOM   635  H  HE1  . MET   A 1 41  ? 26.739  4.994   25.771  1.00 25.53 ? 41  MET   A HE1  1 
ATOM   636  H  HE2  . MET   A 1 41  ? 25.536  5.656   26.569  1.00 25.53 ? 41  MET   A HE2  1 
ATOM   637  H  HE3  . MET   A 1 41  ? 25.686  5.905   25.008  1.00 25.53 ? 41  MET   A HE3  1 
ATOM   638  N  N    . GLU   A 1 42  ? 26.633  10.061  21.559  1.00 22.86 ? 42  GLU   A N    1 
ATOM   639  C  CA   . GLU   A 1 42  ? 26.120  10.357  20.204  1.00 23.43 ? 42  GLU   A CA   1 
ATOM   640  C  C    . GLU   A 1 42  ? 27.205  10.209  19.142  1.00 23.88 ? 42  GLU   A C    1 
ATOM   641  O  O    . GLU   A 1 42  ? 28.384  10.376  19.470  1.00 24.06 ? 42  GLU   A O    1 
ATOM   642  C  CB   . GLU   A 1 42  ? 25.559  11.780  20.161  1.00 24.11 ? 42  GLU   A CB   1 
ATOM   643  C  CG   . GLU   A 1 42  ? 24.978  12.182  18.807  1.00 29.83 ? 42  GLU   A CG   1 
ATOM   644  C  CD   . GLU   A 1 42  ? 24.418  13.593  18.756  1.00 34.95 ? 42  GLU   A CD   1 
ATOM   645  O  OE1  . GLU   A 1 42  ? 24.428  14.271  19.797  1.00 36.19 ? 42  GLU   A OE1  1 
ATOM   646  O  OE2  . GLU   A 1 42  ? 23.985  14.032  17.674  1.00 37.00 ? 42  GLU   A OE2  1 
ATOM   647  H  H    . GLU   A 1 42  ? 27.477  10.195  21.659  1.00 27.45 ? 42  GLU   A H    1 
ATOM   648  H  HA   . GLU   A 1 42  ? 25.402  9.741   19.992  1.00 28.14 ? 42  GLU   A HA   1 
ATOM   649  H  HB2  . GLU   A 1 42  ? 24.851  11.856  20.820  1.00 28.95 ? 42  GLU   A HB2  1 
ATOM   650  H  HB3  . GLU   A 1 42  ? 26.272  12.402  20.373  1.00 28.95 ? 42  GLU   A HB3  1 
ATOM   651  H  HG2  . GLU   A 1 42  ? 25.675  12.125  18.135  1.00 35.81 ? 42  GLU   A HG2  1 
ATOM   652  H  HG3  . GLU   A 1 42  ? 24.258  11.571  18.584  1.00 35.81 ? 42  GLU   A HG3  1 
ATOM   653  N  N    . ASN   A 1 43  ? 26.833  9.778   17.952  1.00 24.33 ? 43  ASN   A N    1 
ATOM   654  C  CA   . ASN   A 1 43  ? 27.690  9.747   16.779  1.00 24.86 ? 43  ASN   A CA   1 
ATOM   655  C  C    . ASN   A 1 43  ? 26.823  10.127  15.590  1.00 28.60 ? 43  ASN   A C    1 
ATOM   656  O  O    . ASN   A 1 43  ? 25.644  10.452  15.745  1.00 25.48 ? 43  ASN   A O    1 
ATOM   657  C  CB   . ASN   A 1 43  ? 28.358  8.377   16.610  1.00 25.71 ? 43  ASN   A CB   1 
ATOM   658  C  CG   . ASN   A 1 43  ? 27.353  7.251   16.652  1.00 26.68 ? 43  ASN   A CG   1 
ATOM   659  O  OD1  . ASN   A 1 43  ? 26.579  7.054   15.720  1.00 23.34 ? 43  ASN   A OD1  1 
ATOM   660  N  ND2  . ASN   A 1 43  ? 27.397  6.469   17.724  1.00 24.08 ? 43  ASN   A ND2  1 
ATOM   661  H  H    . ASN   A 1 43  ? 26.042  9.481   17.790  1.00 29.21 ? 43  ASN   A H    1 
ATOM   662  H  HA   . ASN   A 1 43  ? 28.387  10.415  16.873  1.00 29.85 ? 43  ASN   A HA   1 
ATOM   663  H  HB2  . ASN   A 1 43  ? 28.812  8.346   15.753  1.00 30.87 ? 43  ASN   A HB2  1 
ATOM   664  H  HB3  . ASN   A 1 43  ? 28.994  8.242   17.330  1.00 30.87 ? 43  ASN   A HB3  1 
ATOM   665  H  HD21 . ASN   A 1 43  ? 26.850  5.810   17.798  1.00 28.91 ? 43  ASN   A HD21 1 
ATOM   666  H  HD22 . ASN   A 1 43  ? 27.960  6.633   18.353  1.00 28.91 ? 43  ASN   A HD22 1 
ATOM   667  N  N    . THR   A 1 44  ? 27.403  10.086  14.390  1.00 29.17 ? 44  THR   A N    1 
ATOM   668  C  CA   . THR   A 1 44  ? 26.644  10.519  13.222  1.00 31.96 ? 44  THR   A CA   1 
ATOM   669  C  C    . THR   A 1 44  ? 25.341  9.733   13.099  1.00 31.08 ? 44  THR   A C    1 
ATOM   670  O  O    . THR   A 1 44  ? 24.288  10.305  12.797  1.00 33.86 ? 44  THR   A O    1 
ATOM   671  C  CB   . THR   A 1 44  ? 27.481  10.383  11.949  1.00 37.89 ? 44  THR   A CB   1 
ATOM   672  O  OG1  . THR   A 1 44  ? 28.083  9.088   11.868  1.00 44.51 ? 44  THR   A OG1  1 
ATOM   673  C  CG2  . THR   A 1 44  ? 28.587  11.427  11.955  1.00 36.99 ? 44  THR   A CG2  1 
ATOM   674  H  H    . THR   A 1 44  ? 28.206  9.821   14.230  1.00 35.02 ? 44  THR   A H    1 
ATOM   675  H  HA   . THR   A 1 44  ? 26.416  11.456  13.328  1.00 38.37 ? 44  THR   A HA   1 
ATOM   676  H  HB   . THR   A 1 44  ? 26.920  10.531  11.172  1.00 45.49 ? 44  THR   A HB   1 
ATOM   677  H  HG1  . THR   A 1 44  ? 27.488  8.495   11.860  1.00 53.43 ? 44  THR   A HG1  1 
ATOM   678  H  HG21 . THR   A 1 44  ? 29.121  11.348  11.149  1.00 44.40 ? 44  THR   A HG21 1 
ATOM   679  H  HG22 . THR   A 1 44  ? 28.202  12.317  11.992  1.00 44.40 ? 44  THR   A HG22 1 
ATOM   680  H  HG23 . THR   A 1 44  ? 29.160  11.298  12.727  1.00 44.40 ? 44  THR   A HG23 1 
ATOM   681  N  N    . ASP   A 1 45  ? 25.383  8.438   13.399  1.00 26.44 ? 45  ASP   A N    1 
ATOM   682  C  CA   . ASP   A 1 45  ? 24.292  7.513   13.105  1.00 24.46 ? 45  ASP   A CA   1 
ATOM   683  C  C    . ASP   A 1 45  ? 23.296  7.343   14.235  1.00 25.27 ? 45  ASP   A C    1 
ATOM   684  O  O    . ASP   A 1 45  ? 22.132  7.023   13.962  1.00 24.14 ? 45  ASP   A O    1 
ATOM   685  C  CB   . ASP   A 1 45  ? 24.911  6.163   12.737  1.00 30.51 ? 45  ASP   A CB   1 
ATOM   686  C  CG   . ASP   A 1 45  ? 25.678  6.231   11.457  1.00 38.64 ? 45  ASP   A CG   1 
ATOM   687  O  OD1  . ASP   A 1 45  ? 25.603  7.303   10.822  1.00 42.00 ? 45  ASP   A OD1  1 
ATOM   688  O  OD2  . ASP   A 1 45  ? 26.445  5.298   11.139  1.00 37.38 ? 45  ASP   A OD2  1 
ATOM   689  H  H    . ASP   A 1 45  ? 26.053  8.061   13.784  1.00 31.75 ? 45  ASP   A H    1 
ATOM   690  H  HA   . ASP   A 1 45  ? 23.805  7.839   12.332  1.00 29.37 ? 45  ASP   A HA   1 
ATOM   691  H  HB2  . ASP   A 1 45  ? 25.520  5.889   13.441  1.00 36.63 ? 45  ASP   A HB2  1 
ATOM   692  H  HB3  . ASP   A 1 45  ? 24.204  5.508   12.633  1.00 36.63 ? 45  ASP   A HB3  1 
ATOM   693  N  N    . VAL   A 1 46  ? 23.707  7.545   15.488  1.00 22.39 ? 46  VAL   A N    1 
ATOM   694  C  CA   . VAL   A 1 46  ? 22.861  7.248   16.644  1.00 20.07 ? 46  VAL   A CA   1 
ATOM   695  C  C    . VAL   A 1 46  ? 23.041  8.329   17.700  1.00 20.73 ? 46  VAL   A C    1 
ATOM   696  O  O    . VAL   A 1 46  ? 24.169  8.714   18.024  1.00 21.33 ? 46  VAL   A O    1 
ATOM   697  C  CB   . VAL   A 1 46  ? 23.198  5.868   17.255  1.00 19.86 ? 46  VAL   A CB   1 
ATOM   698  C  CG1  . VAL   A 1 46  ? 22.281  5.544   18.441  1.00 21.64 ? 46  VAL   A CG1  1 
ATOM   699  C  CG2  . VAL   A 1 46  ? 23.142  4.783   16.195  1.00 22.81 ? 46  VAL   A CG2  1 
ATOM   700  H  H    . VAL   A 1 46  ? 24.481  7.857   15.696  1.00 26.89 ? 46  VAL   A H    1 
ATOM   701  H  HA   . VAL   A 1 46  ? 21.931  7.241   16.370  1.00 24.10 ? 46  VAL   A HA   1 
ATOM   702  H  HB   . VAL   A 1 46  ? 24.107  5.897   17.592  1.00 23.86 ? 46  VAL   A HB   1 
ATOM   703  H  HG11 . VAL   A 1 46  ? 22.409  4.616   18.693  1.00 25.98 ? 46  VAL   A HG11 1 
ATOM   704  H  HG12 . VAL   A 1 46  ? 22.508  6.122   19.186  1.00 25.98 ? 46  VAL   A HG12 1 
ATOM   705  H  HG13 . VAL   A 1 46  ? 21.359  5.690   18.176  1.00 25.98 ? 46  VAL   A HG13 1 
ATOM   706  H  HG21 . VAL   A 1 46  ? 23.280  3.922   16.620  1.00 27.39 ? 46  VAL   A HG21 1 
ATOM   707  H  HG22 . VAL   A 1 46  ? 22.272  4.806   15.766  1.00 27.39 ? 46  VAL   A HG22 1 
ATOM   708  H  HG23 . VAL   A 1 46  ? 23.839  4.943   15.540  1.00 27.39 ? 46  VAL   A HG23 1 
ATOM   709  N  N    . LYS   A 1 47  ? 21.928  8.789   18.266  1.00 19.73 ? 47  LYS   A N    1 
ATOM   710  C  CA   . LYS   A 1 47  ? 21.931  9.667   19.431  1.00 19.89 ? 47  LYS   A CA   1 
ATOM   711  C  C    . LYS   A 1 47  ? 21.149  8.988   20.550  1.00 19.87 ? 47  LYS   A C    1 
ATOM   712  O  O    . LYS   A 1 47  ? 20.014  8.554   20.330  1.00 19.88 ? 47  LYS   A O    1 
ATOM   713  C  CB   . LYS   A 1 47  ? 21.274  11.017  19.124  1.00 22.91 ? 47  LYS   A CB   1 
ATOM   714  C  CG   . LYS   A 1 47  ? 20.988  11.832  20.376  1.00 22.24 ? 47  LYS   A CG   1 
ATOM   715  C  CD   . LYS   A 1 47  ? 20.721  13.303  20.108  1.00 23.99 ? 47  LYS   A CD   1 
ATOM   716  C  CE   . LYS   A 1 47  ? 19.442  13.503  19.305  1.00 29.96 ? 47  LYS   A CE   1 
ATOM   717  N  NZ   . LYS   A 1 47  ? 19.125  14.954  19.174  1.00 31.00 ? 47  LYS   A NZ   1 
ATOM   718  H  H    . LYS   A 1 47  ? 21.138  8.600   17.984  1.00 23.69 ? 47  LYS   A H    1 
ATOM   719  H  HA   . LYS   A 1 47  ? 22.840  9.820   19.731  1.00 23.89 ? 47  LYS   A HA   1 
ATOM   720  H  HB2  . LYS   A 1 47  ? 21.867  11.535  18.558  1.00 27.51 ? 47  LYS   A HB2  1 
ATOM   721  H  HB3  . LYS   A 1 47  ? 20.432  10.862  18.668  1.00 27.51 ? 47  LYS   A HB3  1 
ATOM   722  H  HG2  . LYS   A 1 47  ? 20.202  11.470  20.814  1.00 26.70 ? 47  LYS   A HG2  1 
ATOM   723  H  HG3  . LYS   A 1 47  ? 21.753  11.772  20.970  1.00 26.70 ? 47  LYS   A HG3  1 
ATOM   724  H  HD2  . LYS   A 1 47  ? 20.625  13.770  20.953  1.00 28.81 ? 47  LYS   A HD2  1 
ATOM   725  H  HD3  . LYS   A 1 47  ? 21.459  13.675  19.601  1.00 28.81 ? 47  LYS   A HD3  1 
ATOM   726  H  HE2  . LYS   A 1 47  ? 19.558  13.133  18.416  1.00 35.98 ? 47  LYS   A HE2  1 
ATOM   727  H  HE3  . LYS   A 1 47  ? 18.704  13.068  19.760  1.00 35.98 ? 47  LYS   A HE3  1 
ATOM   728  H  HZ1  . LYS   A 1 47  ? 18.377  15.060  18.704  1.00 37.22 ? 47  LYS   A HZ1  1 
ATOM   729  H  HZ2  . LYS   A 1 47  ? 19.014  15.315  19.980  1.00 37.22 ? 47  LYS   A HZ2  1 
ATOM   730  H  HZ3  . LYS   A 1 47  ? 19.790  15.374  18.758  1.00 37.22 ? 47  LYS   A HZ3  1 
ATOM   731  N  N    . VAL   A 1 48  ? 21.720  8.919   21.752  1.00 20.11 ? 48  VAL   A N    1 
ATOM   732  C  CA   . VAL   A 1 48  ? 20.998  8.406   22.914  1.00 17.96 ? 48  VAL   A CA   1 
ATOM   733  C  C    . VAL   A 1 48  ? 20.569  9.589   23.778  1.00 19.69 ? 48  VAL   A C    1 
ATOM   734  O  O    . VAL   A 1 48  ? 21.392  10.450  24.122  1.00 20.70 ? 48  VAL   A O    1 
ATOM   735  C  CB   . VAL   A 1 48  ? 21.833  7.398   23.726  1.00 18.44 ? 48  VAL   A CB   1 
ATOM   736  C  CG1  . VAL   A 1 48  ? 21.161  7.134   25.088  1.00 19.45 ? 48  VAL   A CG1  1 
ATOM   737  C  CG2  . VAL   A 1 48  ? 22.044  6.113   22.927  1.00 19.80 ? 48  VAL   A CG2  1 
ATOM   738  H  H    . VAL   A 1 48  ? 22.527  9.164   21.921  1.00 24.15 ? 48  VAL   A H    1 
ATOM   739  H  HA   . VAL   A 1 48  ? 20.198  7.950   22.613  1.00 21.57 ? 48  VAL   A HA   1 
ATOM   740  H  HB   . VAL   A 1 48  ? 22.706  7.785   23.898  1.00 22.15 ? 48  VAL   A HB   1 
ATOM   741  H  HG11 . VAL   A 1 48  ? 21.512  6.308   25.455  1.00 23.36 ? 48  VAL   A HG11 1 
ATOM   742  H  HG12 . VAL   A 1 48  ? 21.357  7.870   25.689  1.00 23.36 ? 48  VAL   A HG12 1 
ATOM   743  H  HG13 . VAL   A 1 48  ? 20.203  7.055   24.957  1.00 23.36 ? 48  VAL   A HG13 1 
ATOM   744  H  HG21 . VAL   A 1 48  ? 22.581  5.500   23.453  1.00 23.78 ? 48  VAL   A HG21 1 
ATOM   745  H  HG22 . VAL   A 1 48  ? 21.180  5.716   22.735  1.00 23.78 ? 48  VAL   A HG22 1 
ATOM   746  H  HG23 . VAL   A 1 48  ? 22.501  6.328   22.099  1.00 23.78 ? 48  VAL   A HG23 1 
ATOM   747  N  N    . VAL   A 1 49  ? 19.280  9.619   24.130  1.00 20.89 ? 49  VAL   A N    1 
ATOM   748  C  CA   . VAL   A 1 49  ? 18.691  10.649  24.981  1.00 20.64 ? 49  VAL   A CA   1 
ATOM   749  C  C    . VAL   A 1 49  ? 18.348  9.981   26.304  1.00 18.66 ? 49  VAL   A C    1 
ATOM   750  O  O    . VAL   A 1 49  ? 17.729  8.909   26.318  1.00 20.61 ? 49  VAL   A O    1 
ATOM   751  C  CB   . VAL   A 1 49  ? 17.436  11.267  24.331  1.00 21.69 ? 49  VAL   A CB   1 
ATOM   752  C  CG1  . VAL   A 1 49  ? 16.699  12.206  25.303  1.00 24.94 ? 49  VAL   A CG1  1 
ATOM   753  C  CG2  . VAL   A 1 49  ? 17.791  11.963  23.022  1.00 23.35 ? 49  VAL   A CG2  1 
ATOM   754  H  H    . VAL   A 1 49  ? 18.709  9.028   23.876  1.00 25.09 ? 49  VAL   A H    1 
ATOM   755  H  HA   . VAL   A 1 49  ? 19.338  11.353  25.144  1.00 24.78 ? 49  VAL   A HA   1 
ATOM   756  H  HB   . VAL   A 1 49  ? 16.824  10.546  24.113  1.00 26.05 ? 49  VAL   A HB   1 
ATOM   757  H  HG11 . VAL   A 1 49  ? 16.022  12.697  24.812  1.00 29.94 ? 49  VAL   A HG11 1 
ATOM   758  H  HG12 . VAL   A 1 49  ? 16.281  11.678  26.001  1.00 29.94 ? 49  VAL   A HG12 1 
ATOM   759  H  HG13 . VAL   A 1 49  ? 17.338  12.824  25.690  1.00 29.94 ? 49  VAL   A HG13 1 
ATOM   760  H  HG21 . VAL   A 1 49  ? 16.985  12.344  22.639  1.00 28.04 ? 49  VAL   A HG21 1 
ATOM   761  H  HG22 . VAL   A 1 49  ? 18.436  12.664  23.203  1.00 28.04 ? 49  VAL   A HG22 1 
ATOM   762  H  HG23 . VAL   A 1 49  ? 18.171  11.312  22.411  1.00 28.04 ? 49  VAL   A HG23 1 
ATOM   763  N  N    . ASP   A 1 50  ? 18.770  10.589  27.408  1.00 21.73 ? 50  ASP   A N    1 
ATOM   764  C  CA   . ASP   A 1 50  ? 18.373  10.151  28.742  1.00 19.53 ? 50  ASP   A CA   1 
ATOM   765  C  C    . ASP   A 1 50  ? 17.110  10.927  29.104  1.00 20.74 ? 50  ASP   A C    1 
ATOM   766  O  O    . ASP   A 1 50  ? 17.183  12.128  29.383  1.00 21.22 ? 50  ASP   A O    1 
ATOM   767  C  CB   . ASP   A 1 50  ? 19.482  10.436  29.752  1.00 18.89 ? 50  ASP   A CB   1 
ATOM   768  C  CG   . ASP   A 1 50  ? 19.153  9.948   31.162  1.00 22.14 ? 50  ASP   A CG   1 
ATOM   769  O  OD1  . ASP   A 1 50  ? 18.002  9.561   31.443  1.00 21.95 ? 50  ASP   A OD1  1 
ATOM   770  O  OD2  . ASP   A 1 50  ? 20.041  10.066  32.033  1.00 23.27 ? 50  ASP   A OD2  1 
ATOM   771  H  H    . ASP   A 1 50  ? 19.296  11.269  27.411  1.00 26.10 ? 50  ASP   A H    1 
ATOM   772  H  HA   . ASP   A 1 50  ? 18.177  9.201   28.741  1.00 23.45 ? 50  ASP   A HA   1 
ATOM   773  H  HB2  . ASP   A 1 50  ? 20.293  9.989   29.463  1.00 22.69 ? 50  ASP   A HB2  1 
ATOM   774  H  HB3  . ASP   A 1 50  ? 19.630  11.394  29.795  1.00 22.69 ? 50  ASP   A HB3  1 
ATOM   775  N  N    . MET   A 1 51  ? 15.954  10.257  29.106  1.00 23.01 ? 51  MET   A N    1 
ATOM   776  C  CA   A MET   A 1 51  ? 14.707  10.954  29.415  0.39 21.51 ? 51  MET   A CA   1 
ATOM   777  C  CA   B MET   A 1 51  ? 14.700  10.933  29.423  0.61 21.49 ? 51  MET   A CA   1 
ATOM   778  C  C    . MET   A 1 51  ? 14.555  11.245  30.906  1.00 23.85 ? 51  MET   A C    1 
ATOM   779  O  O    . MET   A 1 51  ? 13.639  11.987  31.279  1.00 26.09 ? 51  MET   A O    1 
ATOM   780  C  CB   A MET   A 1 51  ? 13.512  10.130  28.909  0.39 22.92 ? 51  MET   A CB   1 
ATOM   781  C  CB   B MET   A 1 51  ? 13.498  10.088  28.995  0.61 22.93 ? 51  MET   A CB   1 
ATOM   782  C  CG   A MET   A 1 51  ? 13.544  9.860   27.403  0.39 25.09 ? 51  MET   A CG   1 
ATOM   783  C  CG   B MET   A 1 51  ? 13.461  9.722   27.537  0.61 25.36 ? 51  MET   A CG   1 
ATOM   784  S  SD   A MET   A 1 51  ? 11.978  9.985   26.509  0.39 25.34 ? 51  MET   A SD   1 
ATOM   785  S  SD   B MET   A 1 51  ? 13.149  11.144  26.474  0.61 23.46 ? 51  MET   A SD   1 
ATOM   786  C  CE   A MET   A 1 51  ? 11.342  11.557  27.083  0.39 25.30 ? 51  MET   A CE   1 
ATOM   787  C  CE   B MET   A 1 51  ? 11.428  11.466  26.842  0.61 24.96 ? 51  MET   A CE   1 
ATOM   788  H  H    A MET   A 1 51  ? 15.867  9.418   28.936  0.39 27.63 ? 51  MET   A H    1 
ATOM   789  H  H    B MET   A 1 51  ? 15.872  9.419   28.929  0.61 27.63 ? 51  MET   A H    1 
ATOM   790  H  HA   A MET   A 1 51  ? 14.701  11.798  28.937  0.39 25.84 ? 51  MET   A HA   1 
ATOM   791  H  HA   B MET   A 1 51  ? 14.665  11.766  28.927  0.61 25.81 ? 51  MET   A HA   1 
ATOM   792  H  HB2  A MET   A 1 51  ? 13.514  9.272   29.361  0.39 27.52 ? 51  MET   A HB2  1 
ATOM   793  H  HB2  B MET   A 1 51  ? 13.507  9.261   29.503  0.61 27.54 ? 51  MET   A HB2  1 
ATOM   794  H  HB3  A MET   A 1 51  ? 12.694  10.606  29.118  0.39 27.52 ? 51  MET   A HB3  1 
ATOM   795  H  HB3  B MET   A 1 51  ? 12.688  10.582  29.195  0.61 27.54 ? 51  MET   A HB3  1 
ATOM   796  H  HG2  A MET   A 1 51  ? 14.156  10.494  26.997  0.39 30.12 ? 51  MET   A HG2  1 
ATOM   797  H  HG2  B MET   A 1 51  ? 14.315  9.339   27.284  0.61 30.45 ? 51  MET   A HG2  1 
ATOM   798  H  HG3  A MET   A 1 51  ? 13.880  8.960   27.266  0.39 30.12 ? 51  MET   A HG3  1 
ATOM   799  H  HG3  B MET   A 1 51  ? 12.751  9.077   27.391  0.61 30.45 ? 51  MET   A HG3  1 
ATOM   800  H  HE1  A MET   A 1 51  ? 10.701  11.892  26.437  0.39 30.38 ? 51  MET   A HE1  1 
ATOM   801  H  HE1  B MET   A 1 51  ? 11.110  12.177  26.264  0.61 29.97 ? 51  MET   A HE1  1 
ATOM   802  H  HE2  A MET   A 1 51  ? 10.910  11.429  27.942  0.39 30.38 ? 51  MET   A HE2  1 
ATOM   803  H  HE2  B MET   A 1 51  ? 10.916  10.658  26.685  0.61 29.97 ? 51  MET   A HE2  1 
ATOM   804  H  HE3  A MET   A 1 51  ? 12.079  12.180  27.172  0.39 30.38 ? 51  MET   A HE3  1 
ATOM   805  H  HE3  B MET   A 1 51  ? 11.347  11.734  27.771  0.61 29.97 ? 51  MET   A HE3  1 
ATOM   806  N  N    . GLY   A 1 52  ? 15.415  10.691  31.760  1.00 23.45 ? 52  GLY   A N    1 
ATOM   807  C  CA   . GLY   A 1 52  ? 15.356  10.985  33.186  1.00 24.67 ? 52  GLY   A CA   1 
ATOM   808  C  C    . GLY   A 1 52  ? 14.052  10.605  33.853  1.00 25.51 ? 52  GLY   A C    1 
ATOM   809  O  O    . GLY   A 1 52  ? 13.644  11.265  34.820  1.00 26.95 ? 52  GLY   A O    1 
ATOM   810  H  H    . GLY   A 1 52  ? 16.040  10.143  31.538  1.00 28.16 ? 52  GLY   A H    1 
ATOM   811  H  HA2  . GLY   A 1 52  ? 16.073  10.511  33.636  1.00 29.62 ? 52  GLY   A HA2  1 
ATOM   812  H  HA3  . GLY   A 1 52  ? 15.495  11.936  33.318  1.00 29.62 ? 52  GLY   A HA3  1 
ATOM   813  N  N    . HIS   A 1 53  ? 13.387  9.556   33.359  1.00 25.60 ? 53  HIS   A N    1 
ATOM   814  C  CA   . HIS   A 1 53  ? 12.076  9.102   33.832  1.00 26.29 ? 53  HIS   A CA   1 
ATOM   815  C  C    . HIS   A 1 53  ? 10.977  10.124  33.606  1.00 24.61 ? 53  HIS   A C    1 
ATOM   816  O  O    . HIS   A 1 53  ? 9.888   10.005  34.181  1.00 27.36 ? 53  HIS   A O    1 
ATOM   817  C  CB   . HIS   A 1 53  ? 12.158  8.666   35.296  1.00 25.71 ? 53  HIS   A CB   1 
ATOM   818  C  CG   . HIS   A 1 53  ? 13.130  7.552   35.511  1.00 26.30 ? 53  HIS   A CG   1 
ATOM   819  N  ND1  . HIS   A 1 53  ? 14.036  7.523   36.548  1.00 32.63 ? 53  HIS   A ND1  1 
ATOM   820  C  CD2  . HIS   A 1 53  ? 13.335  6.418   34.799  1.00 25.68 ? 53  HIS   A CD2  1 
ATOM   821  C  CE1  . HIS   A 1 53  ? 14.763  6.422   36.464  1.00 39.21 ? 53  HIS   A CE1  1 
ATOM   822  N  NE2  . HIS   A 1 53  ? 14.355  5.733   35.413  1.00 29.30 ? 53  HIS   A NE2  1 
ATOM   823  H  H    . HIS   A 1 53  ? 13.692  9.070   32.718  1.00 30.74 ? 53  HIS   A H    1 
ATOM   824  H  HA   . HIS   A 1 53  ? 11.833  8.316   33.319  1.00 31.56 ? 53  HIS   A HA   1 
ATOM   825  H  HB2  . HIS   A 1 53  ? 12.439  9.419   35.838  1.00 30.87 ? 53  HIS   A HB2  1 
ATOM   826  H  HB3  . HIS   A 1 53  ? 11.284  8.360   35.583  1.00 30.87 ? 53  HIS   A HB3  1 
ATOM   827  H  HD2  . HIS   A 1 53  ? 12.874  6.154   34.036  1.00 30.84 ? 53  HIS   A HD2  1 
ATOM   828  H  HE1  . HIS   A 1 53  ? 15.440  6.171   37.050  1.00 47.07 ? 53  HIS   A HE1  1 
ATOM   829  H  HE2  . HIS   A 1 53  ? 14.675  4.977   35.156  1.00 35.17 ? 53  HIS   A HE2  1 
ATOM   830  N  N    . LYS   A 1 54  ? 11.191  11.040  32.660  1.00 25.65 ? 54  LYS   A N    1 
ATOM   831  C  CA   . LYS   A 1 54  ? 10.155  12.030  32.276  1.00 29.19 ? 54  LYS   A CA   1 
ATOM   832  C  C    . LYS   A 1 54  ? 9.427   11.518  31.028  1.00 28.59 ? 54  LYS   A C    1 
ATOM   833  O  O    . LYS   A 1 54  ? 9.993   10.651  30.335  1.00 26.08 ? 54  LYS   A O    1 
ATOM   834  C  CB   . LYS   A 1 54  ? 10.784  13.391  31.969  1.00 26.32 ? 54  LYS   A CB   1 
ATOM   835  C  CG   . LYS   A 1 54  ? 11.593  13.990  33.105  1.00 33.65 ? 54  LYS   A CG   1 
ATOM   836  C  CD   . LYS   A 1 54  ? 10.789  14.156  34.387  1.00 42.00 ? 54  LYS   A CD   1 
ATOM   837  C  CE   . LYS   A 1 54  ? 11.354  15.218  35.265  1.00 44.71 ? 54  LYS   A CE   1 
ATOM   838  N  NZ   . LYS   A 1 54  ? 10.439  15.528  36.363  1.00 47.68 ? 54  LYS   A NZ   1 
ATOM   839  H  H    . LYS   A 1 54  ? 11.925  11.117  32.219  1.00 30.80 ? 54  LYS   A H    1 
ATOM   840  H  HA   . LYS   A 1 54  ? 9.512   12.134  32.995  1.00 35.05 ? 54  LYS   A HA   1 
ATOM   841  H  HB2  . LYS   A 1 54  ? 11.376  13.293  31.207  1.00 31.60 ? 54  LYS   A HB2  1 
ATOM   842  H  HB3  . LYS   A 1 54  ? 10.076  14.017  31.752  1.00 31.60 ? 54  LYS   A HB3  1 
ATOM   843  H  HG2  . LYS   A 1 54  ? 12.345  13.408  33.297  1.00 40.40 ? 54  LYS   A HG2  1 
ATOM   844  H  HG3  . LYS   A 1 54  ? 11.913  14.865  32.835  1.00 40.40 ? 54  LYS   A HG3  1 
ATOM   845  H  HD2  . LYS   A 1 54  ? 9.878   14.402  34.162  1.00 50.41 ? 54  LYS   A HD2  1 
ATOM   846  H  HD3  . LYS   A 1 54  ? 10.798  13.320  34.879  1.00 50.41 ? 54  LYS   A HD3  1 
ATOM   847  H  HE2  . LYS   A 1 54  ? 12.193  14.911  35.643  1.00 53.67 ? 54  LYS   A HE2  1 
ATOM   848  H  HE3  . LYS   A 1 54  ? 11.493  16.026  34.747  1.00 53.67 ? 54  LYS   A HE3  1 
ATOM   849  H  HZ1  . LYS   A 1 54  ? 10.708  16.263  36.786  1.00 57.23 ? 54  LYS   A HZ1  1 
ATOM   850  H  HZ2  . LYS   A 1 54  ? 9.619   15.662  36.045  1.00 57.23 ? 54  LYS   A HZ2  1 
ATOM   851  H  HZ3  . LYS   A 1 54  ? 10.417  14.852  36.941  1.00 57.23 ? 54  LYS   A HZ3  1 
ATOM   852  N  N    . TYR   A 1 55  ? 8.246   12.059  30.730  1.00 30.74 ? 55  TYR   A N    1 
ATOM   853  C  CA   . TYR   A 1 55  ? 7.442   11.641  29.550  1.00 34.93 ? 55  TYR   A CA   1 
ATOM   854  C  C    . TYR   A 1 55  ? 7.693   12.609  28.397  1.00 35.08 ? 55  TYR   A C    1 
ATOM   855  O  O    . TYR   A 1 55  ? 7.042   12.457  27.343  1.00 40.74 ? 55  TYR   A O    1 
ATOM   856  C  CB   . TYR   A 1 55  ? 5.990   11.563  30.026  1.00 34.21 ? 55  TYR   A CB   1 
ATOM   857  C  CG   . TYR   A 1 55  ? 5.737   10.468  31.053  1.00 32.87 ? 55  TYR   A CG   1 
ATOM   858  C  CD1  . TYR   A 1 55  ? 5.931   10.693  32.410  1.00 30.52 ? 55  TYR   A CD1  1 
ATOM   859  C  CD2  . TYR   A 1 55  ? 5.299   9.211   30.661  1.00 31.48 ? 55  TYR   A CD2  1 
ATOM   860  C  CE1  . TYR   A 1 55  ? 5.699   9.699   33.345  1.00 30.83 ? 55  TYR   A CE1  1 
ATOM   861  C  CE2  . TYR   A 1 55  ? 5.061   8.209   31.585  1.00 30.86 ? 55  TYR   A CE2  1 
ATOM   862  C  CZ   . TYR   A 1 55  ? 5.264   8.454   32.931  1.00 30.12 ? 55  TYR   A CZ   1 
ATOM   863  O  OH   . TYR   A 1 55  ? 5.022   7.471   33.842  1.00 39.75 ? 55  TYR   A OH   1 
ATOM   864  H  H    . TYR   A 1 55  ? 7.874   12.679  31.195  1.00 36.90 ? 55  TYR   A H    1 
ATOM   865  H  HA   . TYR   A 1 55  ? 7.719   10.755  29.271  1.00 41.93 ? 55  TYR   A HA   1 
ATOM   866  H  HB2  . TYR   A 1 55  ? 5.748   12.411  30.431  1.00 41.07 ? 55  TYR   A HB2  1 
ATOM   867  H  HB3  . TYR   A 1 55  ? 5.419   11.389  29.261  1.00 41.07 ? 55  TYR   A HB3  1 
ATOM   868  H  HD1  . TYR   A 1 55  ? 6.224   11.528  32.696  1.00 36.64 ? 55  TYR   A HD1  1 
ATOM   869  H  HD2  . TYR   A 1 55  ? 5.161   9.039   29.758  1.00 37.79 ? 55  TYR   A HD2  1 
ATOM   870  H  HE1  . TYR   A 1 55  ? 5.833   9.869   34.249  1.00 37.02 ? 55  TYR   A HE1  1 
ATOM   871  H  HE2  . TYR   A 1 55  ? 4.767   7.373   31.302  1.00 37.06 ? 55  TYR   A HE2  1 
ATOM   872  H  HH   . TYR   A 1 55  ? 4.765   6.773   33.451  1.00 47.71 ? 55  TYR   A HH   1 
ATOM   873  N  N    . TYR   A 1 56  ? 8.603   13.572  28.578  1.00 33.83 ? 56  TYR   A N    1 
ATOM   874  C  CA   . TYR   A 1 56  ? 8.971   14.545  27.514  1.00 39.34 ? 56  TYR   A CA   1 
ATOM   875  C  C    . TYR   A 1 56  ? 10.457  14.849  27.634  1.00 30.03 ? 56  TYR   A C    1 
ATOM   876  O  O    . TYR   A 1 56  ? 11.024  14.586  28.712  1.00 34.52 ? 56  TYR   A O    1 
ATOM   877  C  CB   . TYR   A 1 56  ? 8.205   15.865  27.622  1.00 47.75 ? 56  TYR   A CB   1 
ATOM   878  C  CG   . TYR   A 1 56  ? 8.569   16.663  28.865  1.00 58.76 ? 56  TYR   A CG   1 
ATOM   879  C  CD1  . TYR   A 1 56  ? 9.670   17.511  28.884  1.00 59.91 ? 56  TYR   A CD1  1 
ATOM   880  C  CD2  . TYR   A 1 56  ? 7.813   16.560  30.022  1.00 58.92 ? 56  TYR   A CD2  1 
ATOM   881  C  CE1  . TYR   A 1 56  ? 10.008  18.227  30.020  1.00 64.29 ? 56  TYR   A CE1  1 
ATOM   882  C  CE2  . TYR   A 1 56  ? 8.137   17.273  31.164  1.00 60.88 ? 56  TYR   A CE2  1 
ATOM   883  C  CZ   . TYR   A 1 56  ? 9.238   18.110  31.162  1.00 69.84 ? 56  TYR   A CZ   1 
ATOM   884  O  OH   . TYR   A 1 56  ? 9.562   18.816  32.284  1.00 75.07 ? 56  TYR   A OH   1 
ATOM   885  H  H    . TYR   A 1 56  ? 9.034   13.696  29.311  1.00 40.62 ? 56  TYR   A H    1 
ATOM   886  H  HA   . TYR   A 1 56  ? 8.801   14.157  26.641  1.00 47.23 ? 56  TYR   A HA   1 
ATOM   887  H  HB2  . TYR   A 1 56  ? 8.407   16.411  26.846  1.00 57.32 ? 56  TYR   A HB2  1 
ATOM   888  H  HB3  . TYR   A 1 56  ? 7.254   15.676  27.656  1.00 57.32 ? 56  TYR   A HB3  1 
ATOM   889  H  HD1  . TYR   A 1 56  ? 10.195  17.593  28.121  1.00 71.91 ? 56  TYR   A HD1  1 
ATOM   890  H  HD2  . TYR   A 1 56  ? 7.073   15.997  30.032  1.00 70.73 ? 56  TYR   A HD2  1 
ATOM   891  H  HE1  . TYR   A 1 56  ? 10.748  18.790  30.013  1.00 77.17 ? 56  TYR   A HE1  1 
ATOM   892  H  HE2  . TYR   A 1 56  ? 7.616   17.189  31.930  1.00 73.08 ? 56  TYR   A HE2  1 
ATOM   893  H  HH   . TYR   A 1 56  ? 9.012   18.650  32.897  1.00 90.11 ? 56  TYR   A HH   1 
ATOM   894  N  N    . SER   A 1 57  ? 11.070  15.399  26.582  1.00 33.25 ? 57  SER   A N    1 
ATOM   895  C  CA   . SER   A 1 57  ? 12.486  15.760  26.613  1.00 29.89 ? 57  SER   A CA   1 
ATOM   896  C  C    . SER   A 1 57  ? 12.810  16.697  25.455  1.00 32.47 ? 57  SER   A C    1 
ATOM   897  O  O    . SER   A 1 57  ? 12.129  16.698  24.426  1.00 35.74 ? 57  SER   A O    1 
ATOM   898  C  CB   . SER   A 1 57  ? 13.364  14.504  26.569  1.00 30.21 ? 57  SER   A CB   1 
ATOM   899  O  OG   . SER   A 1 57  ? 14.681  14.797  26.148  1.00 29.91 ? 57  SER   A OG   1 
ATOM   900  H  H    . SER   A 1 57  ? 10.683  15.573  25.834  1.00 39.92 ? 57  SER   A H    1 
ATOM   901  H  HA   . SER   A 1 57  ? 12.675  16.229  27.441  1.00 35.88 ? 57  SER   A HA   1 
ATOM   902  H  HB2  . SER   A 1 57  ? 13.397  14.111  27.455  1.00 36.27 ? 57  SER   A HB2  1 
ATOM   903  H  HB3  . SER   A 1 57  ? 12.971  13.877  25.943  1.00 36.27 ? 57  SER   A HB3  1 
ATOM   904  H  HG   . SER   A 1 57  ? 15.037  15.344  26.677  1.00 35.91 ? 57  SER   A HG   1 
ATOM   905  N  N    . ASN   A 1 58  ? 13.868  17.501  25.641  1.00 35.14 ? 58  ASN   A N    1 
ATOM   906  C  CA   . ASN   A 1 58  ? 14.398  18.323  24.551  1.00 38.93 ? 58  ASN   A CA   1 
ATOM   907  C  C    . ASN   A 1 58  ? 15.244  17.524  23.561  1.00 34.91 ? 58  ASN   A C    1 
ATOM   908  O  O    . ASN   A 1 58  ? 15.724  18.096  22.573  1.00 34.93 ? 58  ASN   A O    1 
ATOM   909  C  CB   . ASN   A 1 58  ? 15.235  19.505  25.075  1.00 37.41 ? 58  ASN   A CB   1 
ATOM   910  C  CG   . ASN   A 1 58  ? 16.383  19.071  25.981  1.00 43.33 ? 58  ASN   A CG   1 
ATOM   911  O  OD1  . ASN   A 1 58  ? 16.984  18.014  25.791  1.00 39.97 ? 58  ASN   A OD1  1 
ATOM   912  N  ND2  . ASN   A 1 58  ? 16.725  19.926  26.945  1.00 43.68 ? 58  ASN   A ND2  1 
ATOM   913  H  H    . ASN   A 1 58  ? 14.291  17.585  26.385  1.00 42.19 ? 58  ASN   A H    1 
ATOM   914  H  HA   . ASN   A 1 58  ? 13.650  18.694  24.058  1.00 46.73 ? 58  ASN   A HA   1 
ATOM   915  H  HB2  . ASN   A 1 58  ? 15.614  19.982  24.320  1.00 44.91 ? 58  ASN   A HB2  1 
ATOM   916  H  HB3  . ASN   A 1 58  ? 14.660  20.097  25.585  1.00 44.91 ? 58  ASN   A HB3  1 
ATOM   917  H  HD21 . ASN   A 1 58  ? 16.288  20.660  27.043  1.00 52.43 ? 58  ASN   A HD21 1 
ATOM   918  H  HD22 . ASN   A 1 58  ? 17.369  19.733  27.482  1.00 52.43 ? 58  ASN   A HD22 1 
ATOM   919  N  N    . ASN   A 1 59  ? 15.454  16.228  23.817  1.00 30.65 ? 59  ASN   A N    1 
ATOM   920  C  CA   . ASN   A 1 59  ? 16.174  15.315  22.928  1.00 31.21 ? 59  ASN   A CA   1 
ATOM   921  C  C    . ASN   A 1 59  ? 17.637  15.676  22.727  1.00 30.25 ? 59  ASN   A C    1 
ATOM   922  O  O    . ASN   A 1 59  ? 18.268  15.216  21.770  1.00 30.30 ? 59  ASN   A O    1 
ATOM   923  C  CB   . ASN   A 1 59  ? 15.447  15.200  21.587  1.00 30.32 ? 59  ASN   A CB   1 
ATOM   924  C  CG   . ASN   A 1 59  ? 14.104  14.526  21.723  1.00 33.06 ? 59  ASN   A CG   1 
ATOM   925  O  OD1  . ASN   A 1 59  ? 13.903  13.727  22.637  1.00 29.40 ? 59  ASN   A OD1  1 
ATOM   926  N  ND2  . ASN   A 1 59  ? 13.164  14.871  20.852  1.00 35.99 ? 59  ASN   A ND2  1 
ATOM   927  H  H    . ASN   A 1 59  ? 15.176  15.840  24.532  1.00 36.79 ? 59  ASN   A H    1 
ATOM   928  H  HA   . ASN   A 1 59  ? 16.158  14.434  23.333  1.00 37.47 ? 59  ASN   A HA   1 
ATOM   929  H  HB2  . ASN   A 1 59  ? 15.304  16.087  21.222  1.00 36.40 ? 59  ASN   A HB2  1 
ATOM   930  H  HB3  . ASN   A 1 59  ? 15.987  14.672  20.978  1.00 36.40 ? 59  ASN   A HB3  1 
ATOM   931  H  HD21 . ASN   A 1 59  ? 12.383  14.513  20.898  1.00 43.21 ? 59  ASN   A HD21 1 
ATOM   932  H  HD22 . ASN   A 1 59  ? 13.341  15.440  20.231  1.00 43.21 ? 59  ASN   A HD22 1 
ATOM   933  N  N    . LYS   A 1 60  ? 18.209  16.449  23.638  1.00 29.25 ? 60  LYS   A N    1 
ATOM   934  C  CA   . LYS   A 1 60  ? 19.646  16.641  23.628  1.00 30.17 ? 60  LYS   A CA   1 
ATOM   935  C  C    . LYS   A 1 60  ? 20.338  15.324  23.980  1.00 29.46 ? 60  LYS   A C    1 
ATOM   936  O  O    . LYS   A 1 60  ? 19.810  14.527  24.762  1.00 30.95 ? 60  LYS   A O    1 
ATOM   937  C  CB   . LYS   A 1 60  ? 20.044  17.730  24.619  1.00 37.09 ? 60  LYS   A CB   1 
ATOM   938  C  CG   . LYS   A 1 60  ? 19.699  19.122  24.127  1.00 41.05 ? 60  LYS   A CG   1 
ATOM   939  C  CD   . LYS   A 1 60  ? 20.013  20.194  25.156  1.00 43.22 ? 60  LYS   A CD   1 
ATOM   940  C  CE   . LYS   A 1 60  ? 19.197  21.454  24.880  1.00 54.93 ? 60  LYS   A CE   1 
ATOM   941  N  NZ   . LYS   A 1 60  ? 19.332  21.918  23.468  1.00 62.27 ? 60  LYS   A NZ   1 
ATOM   942  H  H    . LYS   A 1 60  ? 17.793  16.868  24.264  1.00 35.12 ? 60  LYS   A H    1 
ATOM   943  H  HA   . LYS   A 1 60  ? 19.920  16.917  22.740  1.00 36.23 ? 60  LYS   A HA   1 
ATOM   944  H  HB2  . LYS   A 1 60  ? 19.576  17.583  25.456  1.00 44.53 ? 60  LYS   A HB2  1 
ATOM   945  H  HB3  . LYS   A 1 60  ? 21.002  17.691  24.763  1.00 44.53 ? 60  LYS   A HB3  1 
ATOM   946  H  HG2  . LYS   A 1 60  ? 20.214  19.312  23.327  1.00 49.28 ? 60  LYS   A HG2  1 
ATOM   947  H  HG3  . LYS   A 1 60  ? 18.750  19.163  23.930  1.00 49.28 ? 60  LYS   A HG3  1 
ATOM   948  H  HD2  . LYS   A 1 60  ? 19.786  19.869  26.041  1.00 51.88 ? 60  LYS   A HD2  1 
ATOM   949  H  HD3  . LYS   A 1 60  ? 20.955  20.421  25.109  1.00 51.88 ? 60  LYS   A HD3  1 
ATOM   950  H  HE2  . LYS   A 1 60  ? 18.260  21.269  25.048  1.00 65.93 ? 60  LYS   A HE2  1 
ATOM   951  H  HE3  . LYS   A 1 60  ? 19.506  22.166  25.462  1.00 65.93 ? 60  LYS   A HE3  1 
ATOM   952  H  HZ1  . LYS   A 1 60  ? 18.890  22.682  23.356  1.00 74.74 ? 60  LYS   A HZ1  1 
ATOM   953  H  HZ2  . LYS   A 1 60  ? 20.190  22.049  23.272  1.00 74.74 ? 60  LYS   A HZ2  1 
ATOM   954  H  HZ3  . LYS   A 1 60  ? 18.998  21.307  22.913  1.00 74.74 ? 60  LYS   A HZ3  1 
ATOM   955  N  N    . PRO   A 1 61  ? 21.516  15.069  23.414  1.00 25.93 ? 61  PRO   A N    1 
ATOM   956  C  CA   . PRO   A 1 61  ? 22.213  13.814  23.722  1.00 27.09 ? 61  PRO   A CA   1 
ATOM   957  C  C    . PRO   A 1 61  ? 22.608  13.747  25.188  1.00 25.58 ? 61  PRO   A C    1 
ATOM   958  O  O    . PRO   A 1 61  ? 22.935  14.756  25.816  1.00 26.21 ? 61  PRO   A O    1 
ATOM   959  C  CB   . PRO   A 1 61  ? 23.448  13.861  22.812  1.00 25.11 ? 61  PRO   A CB   1 
ATOM   960  C  CG   . PRO   A 1 61  ? 23.695  15.360  22.642  1.00 26.70 ? 61  PRO   A CG   1 
ATOM   961  C  CD   . PRO   A 1 61  ? 22.292  15.907  22.478  1.00 30.81 ? 61  PRO   A CD   1 
ATOM   962  H  HA   . PRO   A 1 61  ? 21.663  13.048  23.492  1.00 32.53 ? 61  PRO   A HA   1 
ATOM   963  H  HB2  . PRO   A 1 61  ? 24.200  13.431  23.249  1.00 30.15 ? 61  PRO   A HB2  1 
ATOM   964  H  HB3  . PRO   A 1 61  ? 23.250  13.441  21.960  1.00 30.15 ? 61  PRO   A HB3  1 
ATOM   965  H  HG2  . PRO   A 1 61  ? 24.120  15.720  23.436  1.00 32.06 ? 61  PRO   A HG2  1 
ATOM   966  H  HG3  . PRO   A 1 61  ? 24.231  15.525  21.851  1.00 32.06 ? 61  PRO   A HG3  1 
ATOM   967  H  HD2  . PRO   A 1 61  ? 22.258  16.839  22.744  1.00 36.99 ? 61  PRO   A HD2  1 
ATOM   968  H  HD3  . PRO   A 1 61  ? 21.981  15.781  21.568  1.00 36.99 ? 61  PRO   A HD3  1 
ATOM   969  N  N    . MET   A 1 62  ? 22.573  12.534  25.732  1.00 24.26 ? 62  MET   A N    1 
ATOM   970  C  CA   . MET   A 1 62  ? 23.123  12.299  27.058  1.00 22.43 ? 62  MET   A CA   1 
ATOM   971  C  C    . MET   A 1 62  ? 24.555  12.811  27.107  1.00 21.92 ? 62  MET   A C    1 
ATOM   972  O  O    . MET   A 1 62  ? 25.374  12.469  26.251  1.00 24.13 ? 62  MET   A O    1 
ATOM   973  C  CB   . MET   A 1 62  ? 23.119  10.806  27.370  1.00 21.39 ? 62  MET   A CB   1 
ATOM   974  C  CG   . MET   A 1 62  ? 23.337  10.481  28.830  1.00 24.92 ? 62  MET   A CG   1 
ATOM   975  S  SD   . MET   A 1 62  ? 23.320  8.699   29.076  1.00 22.01 ? 62  MET   A SD   1 
ATOM   976  C  CE   . MET   A 1 62  ? 24.259  8.520   30.573  1.00 24.52 ? 62  MET   A CE   1 
ATOM   977  H  H    . MET   A 1 62  ? 22.239  11.837  25.356  1.00 29.13 ? 62  MET   A H    1 
ATOM   978  H  HA   . MET   A 1 62  ? 22.587  12.759  27.723  1.00 26.93 ? 62  MET   A HA   1 
ATOM   979  H  HB2  . MET   A 1 62  ? 22.262  10.435  27.109  1.00 25.68 ? 62  MET   A HB2  1 
ATOM   980  H  HB3  . MET   A 1 62  ? 23.829  10.381  26.865  1.00 25.68 ? 62  MET   A HB3  1 
ATOM   981  H  HG2  . MET   A 1 62  ? 24.199  10.824  29.114  1.00 29.92 ? 62  MET   A HG2  1 
ATOM   982  H  HG3  . MET   A 1 62  ? 22.624  10.872  29.358  1.00 29.92 ? 62  MET   A HG3  1 
ATOM   983  H  HE1  . MET   A 1 62  ? 24.337  7.577   30.785  1.00 29.44 ? 62  MET   A HE1  1 
ATOM   984  H  HE2  . MET   A 1 62  ? 25.140  8.904   30.440  1.00 29.44 ? 62  MET   A HE2  1 
ATOM   985  H  HE3  . MET   A 1 62  ? 23.800  8.984   31.290  1.00 29.44 ? 62  MET   A HE3  1 
ATOM   986  N  N    . GLN   A 1 63  ? 24.872  13.617  28.117  1.00 22.07 ? 63  GLN   A N    1 
ATOM   987  C  CA   . GLN   A 1 63  ? 26.210  14.187  28.231  1.00 23.81 ? 63  GLN   A CA   1 
ATOM   988  C  C    . GLN   A 1 63  ? 26.810  13.846  29.587  1.00 25.46 ? 63  GLN   A C    1 
ATOM   989  O  O    . GLN   A 1 63  ? 26.115  13.849  30.610  1.00 27.24 ? 63  GLN   A O    1 
ATOM   990  C  CB   . GLN   A 1 63  ? 26.175  15.696  28.027  1.00 30.78 ? 63  GLN   A CB   1 
ATOM   991  C  CG   . GLN   A 1 63  ? 25.493  16.483  29.102  1.00 38.68 ? 63  GLN   A CG   1 
ATOM   992  C  CD   . GLN   A 1 63  ? 25.495  17.958  28.779  1.00 49.99 ? 63  GLN   A CD   1 
ATOM   993  O  OE1  . GLN   A 1 63  ? 25.571  18.346  27.609  1.00 37.64 ? 63  GLN   A OE1  1 
ATOM   994  N  NE2  . GLN   A 1 63  ? 25.465  18.789  29.809  1.00 57.57 ? 63  GLN   A NE2  1 
ATOM   995  H  H    . GLN   A 1 63  ? 24.333  13.848  28.746  1.00 26.51 ? 63  GLN   A H    1 
ATOM   996  H  HA   . GLN   A 1 63  ? 26.781  13.806  27.548  1.00 28.60 ? 63  GLN   A HA   1 
ATOM   997  H  HB2  . GLN   A 1 63  ? 27.088  16.018  27.967  1.00 36.95 ? 63  GLN   A HB2  1 
ATOM   998  H  HB3  . GLN   A 1 63  ? 25.713  15.881  27.195  1.00 36.95 ? 63  GLN   A HB3  1 
ATOM   999  H  HG2  . GLN   A 1 63  ? 24.572  16.189  29.181  1.00 46.44 ? 63  GLN   A HG2  1 
ATOM   1000 H  HG3  . GLN   A 1 63  ? 25.960  16.358  29.943  1.00 46.44 ? 63  GLN   A HG3  1 
ATOM   1001 H  HE21 . GLN   A 1 63  ? 25.421  18.479  30.610  1.00 69.10 ? 63  GLN   A HE21 1 
ATOM   1002 H  HE22 . GLN   A 1 63  ? 25.469  19.639  29.676  1.00 69.10 ? 63  GLN   A HE22 1 
ATOM   1003 N  N    . PHE   A 1 64  ? 28.109  13.542  29.583  1.00 25.94 ? 64  PHE   A N    1 
ATOM   1004 C  CA   . PHE   A 1 64  ? 28.796  13.078  30.778  1.00 26.48 ? 64  PHE   A CA   1 
ATOM   1005 C  C    . PHE   A 1 64  ? 30.234  13.576  30.751  1.00 26.00 ? 64  PHE   A C    1 
ATOM   1006 O  O    . PHE   A 1 64  ? 30.849  13.710  29.690  1.00 26.44 ? 64  PHE   A O    1 
ATOM   1007 C  CB   . PHE   A 1 64  ? 28.735  11.539  30.914  1.00 21.95 ? 64  PHE   A CB   1 
ATOM   1008 C  CG   . PHE   A 1 64  ? 29.380  10.779  29.777  1.00 20.80 ? 64  PHE   A CG   1 
ATOM   1009 C  CD1  . PHE   A 1 64  ? 28.729  10.635  28.560  1.00 24.47 ? 64  PHE   A CD1  1 
ATOM   1010 C  CD2  . PHE   A 1 64  ? 30.625  10.182  29.940  1.00 24.82 ? 64  PHE   A CD2  1 
ATOM   1011 C  CE1  . PHE   A 1 64  ? 29.314  9.932   27.526  1.00 25.03 ? 64  PHE   A CE1  1 
ATOM   1012 C  CE2  . PHE   A 1 64  ? 31.218  9.476   28.904  1.00 22.59 ? 64  PHE   A CE2  1 
ATOM   1013 C  CZ   . PHE   A 1 64  ? 30.559  9.352   27.696  1.00 23.41 ? 64  PHE   A CZ   1 
ATOM   1014 H  H    . PHE   A 1 64  ? 28.616  13.598  28.890  1.00 31.15 ? 64  PHE   A H    1 
ATOM   1015 H  HA   . PHE   A 1 64  ? 28.364  13.462  31.557  1.00 31.79 ? 64  PHE   A HA   1 
ATOM   1016 H  HB2  . PHE   A 1 64  ? 29.188  11.282  31.733  1.00 26.36 ? 64  PHE   A HB2  1 
ATOM   1017 H  HB3  . PHE   A 1 64  ? 27.804  11.269  30.957  1.00 26.36 ? 64  PHE   A HB3  1 
ATOM   1018 H  HD1  . PHE   A 1 64  ? 27.893  11.024  28.437  1.00 29.38 ? 64  PHE   A HD1  1 
ATOM   1019 H  HD2  . PHE   A 1 64  ? 31.071  10.267  30.751  1.00 29.80 ? 64  PHE   A HD2  1 
ATOM   1020 H  HE1  . PHE   A 1 64  ? 28.871  9.848   26.713  1.00 30.06 ? 64  PHE   A HE1  1 
ATOM   1021 H  HE2  . PHE   A 1 64  ? 32.054  9.086   29.022  1.00 27.13 ? 64  PHE   A HE2  1 
ATOM   1022 H  HZ   . PHE   A 1 64  ? 30.951  8.878   26.998  1.00 28.12 ? 64  PHE   A HZ   1 
ATOM   1023 N  N    . THR   A 1 65  ? 30.781  13.848  31.937  1.00 26.46 ? 65  THR   A N    1 
ATOM   1024 C  CA   . THR   A 1 65  ? 32.154  14.368  32.076  1.00 25.29 ? 65  THR   A CA   1 
ATOM   1025 C  C    . THR   A 1 65  ? 33.139  13.298  31.685  1.00 29.86 ? 65  THR   A C    1 
ATOM   1026 O  O    . THR   A 1 65  ? 32.982  12.156  32.153  1.00 26.00 ? 65  THR   A O    1 
ATOM   1027 C  CB   . THR   A 1 65  ? 32.377  14.833  33.514  1.00 29.42 ? 65  THR   A CB   1 
ATOM   1028 O  OG1  . THR   A 1 65  ? 31.579  16.002  33.660  1.00 34.79 ? 65  THR   A OG1  1 
ATOM   1029 C  CG2  . THR   A 1 65  ? 33.832  15.158  33.799  1.00 29.97 ? 65  THR   A CG2  1 
ATOM   1030 H  H    . THR   A 1 65  ? 30.376  13.740  32.688  1.00 31.77 ? 65  THR   A H    1 
ATOM   1031 H  HA   . THR   A 1 65  ? 32.274  15.128  31.485  1.00 30.37 ? 65  THR   A HA   1 
ATOM   1032 H  HB   . THR   A 1 65  ? 32.078  14.149  34.134  1.00 35.32 ? 65  THR   A HB   1 
ATOM   1033 H  HG1  . THR   A 1 65  ? 31.659  16.309  34.438  1.00 41.77 ? 65  THR   A HG1  1 
ATOM   1034 H  HG21 . THR   A 1 65  ? 33.902  15.651  34.631  1.00 35.98 ? 65  THR   A HG21 1 
ATOM   1035 H  HG22 . THR   A 1 65  ? 34.349  14.341  33.874  1.00 35.98 ? 65  THR   A HG22 1 
ATOM   1036 H  HG23 . THR   A 1 65  ? 34.197  15.699  33.082  1.00 35.98 ? 65  THR   A HG23 1 
ATOM   1037 N  N    . CYS   A 1 66  ? 34.105  13.637  30.838  1.00 31.22 ? 66  CYS   A N    1 
ATOM   1038 C  CA   . CYS   A 1 66  ? 35.195  12.711  30.447  1.00 26.92 ? 66  CYS   A CA   1 
ATOM   1039 C  C    . CYS   A 1 66  ? 36.475  13.546  30.496  1.00 32.32 ? 66  CYS   A C    1 
ATOM   1040 O  O    . CYS   A 1 66  ? 36.638  14.376  29.599  1.00 33.93 ? 66  CYS   A O    1 
ATOM   1041 C  CB   . CYS   A 1 66  ? 34.913  12.080  29.091  1.00 29.11 ? 66  CYS   A CB   1 
ATOM   1042 S  SG   . CYS   A 1 66  ? 34.544  13.274  27.782  1.00 29.63 ? 66  CYS   A SG   1 
ATOM   1043 H  H    . CYS   A 1 66  ? 34.162  14.409  30.463  1.00 37.48 ? 66  CYS   A H    1 
ATOM   1044 H  HA   . CYS   A 1 66  ? 35.267  12.002  31.105  1.00 32.32 ? 66  CYS   A HA   1 
ATOM   1045 H  HB2  . CYS   A 1 66  ? 35.689  11.575  28.817  1.00 34.95 ? 66  CYS   A HB2  1 
ATOM   1046 H  HB3  . CYS   A 1 66  ? 34.149  11.488  29.175  1.00 34.95 ? 66  CYS   A HB3  1 
ATOM   1047 N  N    . LYS   A 1 67  ? 37.304  13.372  31.524  1.00 38.49 ? 67  LYS   A N    1 
ATOM   1048 C  CA   . LYS   A 1 67  ? 38.503  14.230  31.714  1.00 44.24 ? 67  LYS   A CA   1 
ATOM   1049 C  C    . LYS   A 1 67  ? 39.728  13.615  31.029  1.00 48.97 ? 67  LYS   A C    1 
ATOM   1050 O  O    . LYS   A 1 67  ? 39.817  12.369  30.985  1.00 47.18 ? 67  LYS   A O    1 
ATOM   1051 C  CB   . LYS   A 1 67  ? 38.777  14.408  33.208  1.00 44.80 ? 67  LYS   A CB   1 
ATOM   1052 C  CG   . LYS   A 1 67  ? 37.662  15.112  33.960  1.00 49.82 ? 67  LYS   A CG   1 
ATOM   1053 C  CD   . LYS   A 1 67  ? 38.080  15.618  35.333  1.00 58.32 ? 67  LYS   A CD   1 
ATOM   1054 C  CE   . LYS   A 1 67  ? 38.573  14.524  36.221  1.00 66.41 ? 67  LYS   A CE   1 
ATOM   1055 N  NZ   . LYS   A 1 67  ? 38.902  15.038  37.551  1.00 75.16 ? 67  LYS   A NZ   1 
ATOM   1056 H  H    . LYS   A 1 67  ? 37.205  12.770  32.130  1.00 46.20 ? 67  LYS   A H    1 
ATOM   1057 H  HA   . LYS   A 1 67  ? 38.340  15.104  31.325  1.00 53.11 ? 67  LYS   A HA   1 
ATOM   1058 H  HB2  . LYS   A 1 67  ? 38.898  13.533  33.609  1.00 53.78 ? 67  LYS   A HB2  1 
ATOM   1059 H  HB3  . LYS   A 1 67  ? 39.585  14.933  33.317  1.00 53.78 ? 67  LYS   A HB3  1 
ATOM   1060 H  HG2  . LYS   A 1 67  ? 37.366  15.875  33.439  1.00 59.80 ? 67  LYS   A HG2  1 
ATOM   1061 H  HG3  . LYS   A 1 67  ? 36.927  14.492  34.083  1.00 59.80 ? 67  LYS   A HG3  1 
ATOM   1062 H  HD2  . LYS   A 1 67  ? 38.795  16.265  35.228  1.00 70.00 ? 67  LYS   A HD2  1 
ATOM   1063 H  HD3  . LYS   A 1 67  ? 37.316  16.033  35.763  1.00 70.00 ? 67  LYS   A HD3  1 
ATOM   1064 H  HE2  . LYS   A 1 67  ? 37.882  13.850  36.316  1.00 79.71 ? 67  LYS   A HE2  1 
ATOM   1065 H  HE3  . LYS   A 1 67  ? 39.375  14.134  35.840  1.00 79.71 ? 67  LYS   A HE3  1 
ATOM   1066 H  HZ1  . LYS   A 1 67  ? 39.194  14.376  38.069  1.00 90.22 ? 67  LYS   A HZ1  1 
ATOM   1067 H  HZ2  . LYS   A 1 67  ? 39.537  15.658  37.489  1.00 90.22 ? 67  LYS   A HZ2  1 
ATOM   1068 H  HZ3  . LYS   A 1 67  ? 38.180  15.400  37.924  1.00 90.22 ? 67  LYS   A HZ3  1 
ATOM   1069 N  N    . GLU   A 1 68  ? 40.642  14.458  30.537  1.00 53.02 ? 68  GLU   A N    1 
ATOM   1070 C  CA   . GLU   A 1 68  ? 41.884  13.966  29.889  1.00 51.81 ? 68  GLU   A CA   1 
ATOM   1071 C  C    . GLU   A 1 68  ? 42.634  13.091  30.897  1.00 53.57 ? 68  GLU   A C    1 
ATOM   1072 O  O    . GLU   A 1 68  ? 43.156  12.037  30.484  1.00 43.82 ? 68  GLU   A O    1 
ATOM   1073 C  CB   . GLU   A 1 68  ? 42.740  15.144  29.427  1.00 52.87 ? 68  GLU   A CB   1 
ATOM   1074 C  CG   . GLU   A 1 68  ? 44.124  14.729  28.938  1.00 58.12 ? 68  GLU   A CG   1 
ATOM   1075 C  CD   . GLU   A 1 68  ? 44.910  15.844  28.274  1.00 61.96 ? 68  GLU   A CD   1 
ATOM   1076 O  OE1  . GLU   A 1 68  ? 45.154  16.871  28.940  1.00 57.70 ? 68  GLU   A OE1  1 
ATOM   1077 O  OE2  . GLU   A 1 68  ? 45.281  15.680  27.094  1.00 62.85 ? 68  GLU   A OE2  1 
ATOM   1078 H  H    . GLU   A 1 68  ? 40.575  15.315  30.562  1.00 63.65 ? 68  GLU   A H    1 
ATOM   1079 H  HA   . GLU   A 1 68  ? 41.656  13.424  29.118  1.00 62.19 ? 68  GLU   A HA   1 
ATOM   1080 H  HB2  . GLU   A 1 68  ? 42.288  15.593  28.696  1.00 63.46 ? 68  GLU   A HB2  1 
ATOM   1081 H  HB3  . GLU   A 1 68  ? 42.858  15.757  30.169  1.00 63.46 ? 68  GLU   A HB3  1 
ATOM   1082 H  HG2  . GLU   A 1 68  ? 44.644  14.418  29.695  1.00 69.76 ? 68  GLU   A HG2  1 
ATOM   1083 H  HG3  . GLU   A 1 68  ? 44.024  14.012  28.292  1.00 69.76 ? 68  GLU   A HG3  1 
ATOM   1084 N  N    . THR   A 1 69  ? 42.673  13.500  32.168  1.00 51.11 ? 69  THR   A N    1 
ATOM   1085 C  CA   . THR   A 1 69  ? 43.320  12.729  33.249  1.00 55.88 ? 69  THR   A CA   1 
ATOM   1086 C  C    . THR   A 1 69  ? 42.229  12.138  34.116  1.00 59.22 ? 69  THR   A C    1 
ATOM   1087 O  O    . THR   A 1 69  ? 41.628  12.895  34.908  1.00 56.88 ? 69  THR   A O    1 
ATOM   1088 C  CB   . THR   A 1 69  ? 44.260  13.635  34.039  1.00 49.25 ? 69  THR   A CB   1 
ATOM   1089 O  OG1  . THR   A 1 69  ? 45.169  14.130  33.063  1.00 54.42 ? 69  THR   A OG1  1 
ATOM   1090 C  CG2  . THR   A 1 69  ? 45.003  12.888  35.131  1.00 43.96 ? 69  THR   A CG2  1 
ATOM   1091 H  H    . THR   A 1 69  ? 42.325  14.238  32.440  1.00 61.35 ? 69  THR   A H    1 
ATOM   1092 H  HA   . THR   A 1 69  ? 43.851  12.019  32.862  1.00 67.07 ? 69  THR   A HA   1 
ATOM   1093 H  HB   . THR   A 1 69  ? 43.763  14.368  34.435  1.00 59.12 ? 69  THR   A HB   1 
ATOM   1094 H  HG1  . THR   A 1 69  ? 45.580  13.492  32.703  1.00 65.33 ? 69  THR   A HG1  1 
ATOM   1095 H  HG21 . THR   A 1 69  ? 45.638  13.480  35.563  1.00 52.77 ? 69  THR   A HG21 1 
ATOM   1096 H  HG22 . THR   A 1 69  ? 44.377  12.560  35.795  1.00 52.77 ? 69  THR   A HG22 1 
ATOM   1097 H  HG23 . THR   A 1 69  ? 45.483  12.136  34.750  1.00 52.77 ? 69  THR   A HG23 1 
ATOM   1098 N  N    . PRO   A 1 70  ? 41.916  10.829  33.998  1.00 57.69 ? 70  PRO   A N    1 
ATOM   1099 C  CA   . PRO   A 1 70  ? 40.820  10.180  34.779  1.00 60.67 ? 70  PRO   A CA   1 
ATOM   1100 C  C    . PRO   A 1 70  ? 41.169  10.161  36.263  1.00 59.21 ? 70  PRO   A C    1 
ATOM   1101 O  O    . PRO   A 1 70  ? 42.379  10.249  36.570  1.00 55.06 ? 70  PRO   A O    1 
ATOM   1102 C  CB   . PRO   A 1 70  ? 40.703  8.787   34.162  1.00 52.13 ? 70  PRO   A CB   1 
ATOM   1103 C  CG   . PRO   A 1 70  ? 42.101  8.514   33.644  1.00 53.60 ? 70  PRO   A CG   1 
ATOM   1104 C  CD   . PRO   A 1 70  ? 42.573  9.823   33.105  1.00 51.43 ? 70  PRO   A CD   1 
ATOM   1105 H  HA   . PRO   A 1 70  ? 39.986  10.659  34.651  1.00 72.82 ? 70  PRO   A HA   1 
ATOM   1106 H  HB2  . PRO   A 1 70  ? 40.452  8.143   34.842  1.00 62.57 ? 70  PRO   A HB2  1 
ATOM   1107 H  HB3  . PRO   A 1 70  ? 40.059  8.798   33.437  1.00 62.57 ? 70  PRO   A HB3  1 
ATOM   1108 H  HG2  . PRO   A 1 70  ? 42.668  8.218   34.373  1.00 64.34 ? 70  PRO   A HG2  1 
ATOM   1109 H  HG3  . PRO   A 1 70  ? 42.065  7.846   32.942  1.00 64.34 ? 70  PRO   A HG3  1 
ATOM   1110 H  HD2  . PRO   A 1 70  ? 43.537  9.884   33.177  1.00 61.74 ? 70  PRO   A HD2  1 
ATOM   1111 H  HD3  . PRO   A 1 70  ? 42.276  9.939   32.189  1.00 61.74 ? 70  PRO   A HD3  1 
ATOM   1112 N  N    . LYS   A 1 76  ? 40.485  8.826   21.680  1.00 42.49 ? 76  LYS   A N    1 
ATOM   1113 C  CA   . LYS   A 1 76  ? 40.752  8.413   23.057  1.00 40.18 ? 76  LYS   A CA   1 
ATOM   1114 C  C    . LYS   A 1 76  ? 39.491  7.740   23.638  1.00 29.71 ? 76  LYS   A C    1 
ATOM   1115 O  O    . LYS   A 1 76  ? 38.385  7.886   23.095  1.00 32.34 ? 76  LYS   A O    1 
ATOM   1116 C  CB   . LYS   A 1 76  ? 41.178  9.620   23.893  1.00 44.63 ? 76  LYS   A CB   1 
ATOM   1117 C  CG   . LYS   A 1 76  ? 42.394  9.390   24.790  1.00 51.19 ? 76  LYS   A CG   1 
ATOM   1118 C  CD   . LYS   A 1 76  ? 43.639  9.063   23.969  1.00 44.36 ? 76  LYS   A CD   1 
ATOM   1119 C  CE   . LYS   A 1 76  ? 44.916  9.243   24.789  1.00 55.13 ? 76  LYS   A CE   1 
ATOM   1120 N  NZ   . LYS   A 1 76  ? 45.427  10.645  24.737  1.00 51.58 ? 76  LYS   A NZ   1 
ATOM   1121 H  HA   . LYS   A 1 76  ? 41.470  7.762   23.062  1.00 48.23 ? 76  LYS   A HA   1 
ATOM   1122 H  HB2  . LYS   A 1 76  ? 41.392  10.351  23.293  1.00 53.58 ? 76  LYS   A HB2  1 
ATOM   1123 H  HB3  . LYS   A 1 76  ? 40.438  9.875   24.465  1.00 53.58 ? 76  LYS   A HB3  1 
ATOM   1124 H  HG2  . LYS   A 1 76  ? 42.570  10.194  25.303  1.00 61.45 ? 76  LYS   A HG2  1 
ATOM   1125 H  HG3  . LYS   A 1 76  ? 42.217  8.644   25.384  1.00 61.45 ? 76  LYS   A HG3  1 
ATOM   1126 H  HD2  . LYS   A 1 76  ? 43.597  8.140   23.676  1.00 53.25 ? 76  LYS   A HD2  1 
ATOM   1127 H  HD3  . LYS   A 1 76  ? 43.683  9.657   23.204  1.00 53.25 ? 76  LYS   A HD3  1 
ATOM   1128 H  HE2  . LYS   A 1 76  ? 44.708  9.038   25.710  1.00 66.17 ? 76  LYS   A HE2  1 
ATOM   1129 H  HE3  . LYS   A 1 76  ? 45.603  8.648   24.456  1.00 66.17 ? 76  LYS   A HE3  1 
ATOM   1130 H  HZ1  . LYS   A 1 76  ? 46.211  10.698  25.154  1.00 61.91 ? 76  LYS   A HZ1  1 
ATOM   1131 H  HZ2  . LYS   A 1 76  ? 45.532  10.899  23.890  1.00 61.91 ? 76  LYS   A HZ2  1 
ATOM   1132 H  HZ3  . LYS   A 1 76  ? 44.850  11.194  25.133  1.00 61.91 ? 76  LYS   A HZ3  1 
ATOM   1133 N  N    . THR   A 1 77  ? 39.673  7.008   24.740  1.00 32.19 ? 77  THR   A N    1 
ATOM   1134 C  CA   . THR   A 1 77  ? 38.644  6.157   25.333  1.00 30.58 ? 77  THR   A CA   1 
ATOM   1135 C  C    . THR   A 1 77  ? 38.356  6.593   26.761  1.00 27.32 ? 77  THR   A C    1 
ATOM   1136 O  O    . THR   A 1 77  ? 39.284  6.809   27.546  1.00 28.46 ? 77  THR   A O    1 
ATOM   1137 C  CB   . THR   A 1 77  ? 39.071  4.682   25.304  1.00 31.87 ? 77  THR   A CB   1 
ATOM   1138 O  OG1  . THR   A 1 77  ? 39.443  4.335   23.963  1.00 32.61 ? 77  THR   A OG1  1 
ATOM   1139 C  CG2  . THR   A 1 77  ? 37.967  3.761   25.809  1.00 33.03 ? 77  THR   A CG2  1 
ATOM   1140 H  H    . THR   A 1 77  ? 40.414  6.990   25.176  1.00 38.65 ? 77  THR   A H    1 
ATOM   1141 H  HA   . THR   A 1 77  ? 37.828  6.243   24.819  1.00 36.71 ? 77  THR   A HA   1 
ATOM   1142 H  HB   . THR   A 1 77  ? 39.841  4.567   25.882  1.00 38.26 ? 77  THR   A HB   1 
ATOM   1143 H  HG1  . THR   A 1 77  ? 39.680  3.530   23.930  1.00 39.15 ? 77  THR   A HG1  1 
ATOM   1144 H  HG21 . THR   A 1 77  ? 38.223  2.835   25.676  1.00 39.65 ? 77  THR   A HG21 1 
ATOM   1145 H  HG22 . THR   A 1 77  ? 37.813  3.912   26.755  1.00 39.65 ? 77  THR   A HG22 1 
ATOM   1146 H  HG23 . THR   A 1 77  ? 37.145  3.932   25.324  1.00 39.65 ? 77  THR   A HG23 1 
ATOM   1147 N  N    . TYR   A 1 78  ? 37.062  6.678   27.092  1.00 26.08 ? 78  TYR   A N    1 
ATOM   1148 C  CA   . TYR   A 1 78  ? 36.586  7.201   28.361  1.00 24.97 ? 78  TYR   A CA   1 
ATOM   1149 C  C    . TYR   A 1 78  ? 35.505  6.285   28.915  1.00 23.53 ? 78  TYR   A C    1 
ATOM   1150 O  O    . TYR   A 1 78  ? 34.727  5.696   28.164  1.00 23.11 ? 78  TYR   A O    1 
ATOM   1151 C  CB   . TYR   A 1 78  ? 36.002  8.618   28.180  1.00 25.49 ? 78  TYR   A CB   1 
ATOM   1152 C  CG   . TYR   A 1 78  ? 36.979  9.547   27.506  1.00 24.58 ? 78  TYR   A CG   1 
ATOM   1153 C  CD1  . TYR   A 1 78  ? 37.894  10.280  28.246  1.00 28.91 ? 78  TYR   A CD1  1 
ATOM   1154 C  CD2  . TYR   A 1 78  ? 36.993  9.683   26.123  1.00 28.83 ? 78  TYR   A CD2  1 
ATOM   1155 C  CE1  . TYR   A 1 78  ? 38.803  11.121  27.635  1.00 31.35 ? 78  TYR   A CE1  1 
ATOM   1156 C  CE2  . TYR   A 1 78  ? 37.898  10.523  25.499  1.00 34.58 ? 78  TYR   A CE2  1 
ATOM   1157 C  CZ   . TYR   A 1 78  ? 38.798  11.240  26.258  1.00 36.02 ? 78  TYR   A CZ   1 
ATOM   1158 O  OH   . TYR   A 1 78  ? 39.701  12.080  25.650  1.00 37.40 ? 78  TYR   A OH   1 
ATOM   1159 H  H    . TYR   A 1 78  ? 36.425  6.427   26.572  1.00 31.32 ? 78  TYR   A H    1 
ATOM   1160 H  HA   . TYR   A 1 78  ? 37.317  7.242   28.997  1.00 29.99 ? 78  TYR   A HA   1 
ATOM   1161 H  HB2  . TYR   A 1 78  ? 35.205  8.566   27.630  1.00 30.61 ? 78  TYR   A HB2  1 
ATOM   1162 H  HB3  . TYR   A 1 78  ? 35.785  8.987   29.050  1.00 30.61 ? 78  TYR   A HB3  1 
ATOM   1163 H  HD1  . TYR   A 1 78  ? 37.901  10.198  29.172  1.00 34.71 ? 78  TYR   A HD1  1 
ATOM   1164 H  HD2  . TYR   A 1 78  ? 36.389  9.197   25.609  1.00 34.62 ? 78  TYR   A HD2  1 
ATOM   1165 H  HE1  . TYR   A 1 78  ? 39.410  11.606  28.146  1.00 37.64 ? 78  TYR   A HE1  1 
ATOM   1166 H  HE2  . TYR   A 1 78  ? 37.897  10.606  24.573  1.00 41.51 ? 78  TYR   A HE2  1 
ATOM   1167 H  HH   . TYR   A 1 78  ? 39.594  12.062  24.817  1.00 44.90 ? 78  TYR   A HH   1 
ATOM   1168 N  N    . TYR   A 1 79  ? 35.450  6.186   30.240  1.00 22.83 ? 79  TYR   A N    1 
ATOM   1169 C  CA   . TYR   A 1 79  ? 34.354  5.472   30.882  1.00 20.97 ? 79  TYR   A CA   1 
ATOM   1170 C  C    . TYR   A 1 79  ? 33.039  6.225   30.736  1.00 21.53 ? 79  TYR   A C    1 
ATOM   1171 O  O    . TYR   A 1 79  ? 32.978  7.446   30.922  1.00 22.82 ? 79  TYR   A O    1 
ATOM   1172 C  CB   . TYR   A 1 79  ? 34.655  5.259   32.361  1.00 23.75 ? 79  TYR   A CB   1 
ATOM   1173 C  CG   . TYR   A 1 79  ? 35.493  4.044   32.638  1.00 30.02 ? 79  TYR   A CG   1 
ATOM   1174 C  CD1  . TYR   A 1 79  ? 34.936  2.774   32.606  1.00 31.92 ? 79  TYR   A CD1  1 
ATOM   1175 C  CD2  . TYR   A 1 79  ? 36.846  4.162   32.919  1.00 34.96 ? 79  TYR   A CD2  1 
ATOM   1176 C  CE1  . TYR   A 1 79  ? 35.702  1.656   32.858  1.00 39.48 ? 79  TYR   A CE1  1 
ATOM   1177 C  CE2  . TYR   A 1 79  ? 37.619  3.050   33.170  1.00 35.91 ? 79  TYR   A CE2  1 
ATOM   1178 C  CZ   . TYR   A 1 79  ? 37.042  1.798   33.136  1.00 39.42 ? 79  TYR   A CZ   1 
ATOM   1179 O  OH   . TYR   A 1 79  ? 37.809  0.683   33.384  1.00 44.72 ? 79  TYR   A OH   1 
ATOM   1180 H  H    . TYR   A 1 79  ? 36.028  6.519   30.783  1.00 27.42 ? 79  TYR   A H    1 
ATOM   1181 H  HA   . TYR   A 1 79  ? 34.254  4.602   30.465  1.00 25.18 ? 79  TYR   A HA   1 
ATOM   1182 H  HB2  . TYR   A 1 79  ? 35.133  6.033   32.698  1.00 28.52 ? 79  TYR   A HB2  1 
ATOM   1183 H  HB3  . TYR   A 1 79  ? 33.817  5.157   32.839  1.00 28.52 ? 79  TYR   A HB3  1 
ATOM   1184 H  HD1  . TYR   A 1 79  ? 34.030  2.676   32.418  1.00 38.32 ? 79  TYR   A HD1  1 
ATOM   1185 H  HD2  . TYR   A 1 79  ? 37.237  5.006   32.942  1.00 41.97 ? 79  TYR   A HD2  1 
ATOM   1186 H  HE1  . TYR   A 1 79  ? 35.316  0.810   32.835  1.00 47.39 ? 79  TYR   A HE1  1 
ATOM   1187 H  HE2  . TYR   A 1 79  ? 38.525  3.143   33.359  1.00 43.11 ? 79  TYR   A HE2  1 
ATOM   1188 H  HH   . TYR   A 1 79  ? 38.603  0.909   33.538  1.00 53.68 ? 79  TYR   A HH   1 
ATOM   1189 N  N    . THR   A 1 80  ? 31.980  5.478   30.425  1.00 18.78 ? 80  THR   A N    1 
ATOM   1190 C  CA   . THR   A 1 80  ? 30.659  6.048   30.269  1.00 16.93 ? 80  THR   A CA   1 
ATOM   1191 C  C    . THR   A 1 80  ? 30.043  6.335   31.637  1.00 20.14 ? 80  THR   A C    1 
ATOM   1192 O  O    . THR   A 1 80  ? 30.577  5.960   32.688  1.00 19.78 ? 80  THR   A O    1 
ATOM   1193 C  CB   . THR   A 1 80  ? 29.750  5.102   29.487  1.00 19.87 ? 80  THR   A CB   1 
ATOM   1194 O  OG1  . THR   A 1 80  ? 29.597  3.869   30.199  1.00 20.68 ? 80  THR   A OG1  1 
ATOM   1195 C  CG2  . THR   A 1 80  ? 30.338  4.801   28.116  1.00 21.48 ? 80  THR   A CG2  1 
ATOM   1196 H  H    . THR   A 1 80  ? 32.009  4.628   30.299  1.00 22.55 ? 80  THR   A H    1 
ATOM   1197 H  HA   . THR   A 1 80  ? 30.724  6.883   29.781  1.00 20.34 ? 80  THR   A HA   1 
ATOM   1198 H  HB   . THR   A 1 80  ? 28.881  5.515   29.365  1.00 23.86 ? 80  THR   A HB   1 
ATOM   1199 H  HG1  . THR   A 1 80  ? 29.199  4.003   30.926  1.00 24.84 ? 80  THR   A HG1  1 
ATOM   1200 H  HG21 . THR   A 1 80  ? 29.725  4.248   27.607  1.00 25.80 ? 80  THR   A HG21 1 
ATOM   1201 H  HG22 . THR   A 1 80  ? 30.492  5.628   27.633  1.00 25.80 ? 80  THR   A HG22 1 
ATOM   1202 H  HG23 . THR   A 1 80  ? 31.181  4.330   28.212  1.00 25.80 ? 80  THR   A HG23 1 
ATOM   1203 N  N    . GLY   A 1 81  ? 28.909  7.010   31.611  1.00 20.78 ? 81  GLY   A N    1 
ATOM   1204 C  CA   . GLY   A 1 81  ? 28.134  7.239   32.810  1.00 20.76 ? 81  GLY   A CA   1 
ATOM   1205 C  C    . GLY   A 1 81  ? 28.420  8.588   33.433  1.00 20.97 ? 81  GLY   A C    1 
ATOM   1206 O  O    . GLY   A 1 81  ? 29.507  9.155   33.292  1.00 21.28 ? 81  GLY   A O    1 
ATOM   1207 H  H    . GLY   A 1 81  ? 28.563  7.350   30.901  1.00 24.96 ? 81  GLY   A H    1 
ATOM   1208 H  HA2  . GLY   A 1 81  ? 27.189  7.194   32.596  1.00 24.93 ? 81  GLY   A HA2  1 
ATOM   1209 H  HA3  . GLY   A 1 81  ? 28.334  6.550   33.463  1.00 24.93 ? 81  GLY   A HA3  1 
ATOM   1210 N  N    . TYR   A 1 82  ? 27.419  9.107   34.141  1.00 21.79 ? 82  TYR   A N    1 
ATOM   1211 C  CA   . TYR   A 1 82  ? 27.556  10.391  34.818  1.00 21.05 ? 82  TYR   A CA   1 
ATOM   1212 C  C    . TYR   A 1 82  ? 28.627  10.375  35.898  1.00 24.43 ? 82  TYR   A C    1 
ATOM   1213 O  O    . TYR   A 1 82  ? 29.122  11.447  36.266  1.00 22.11 ? 82  TYR   A O    1 
ATOM   1214 C  CB   . TYR   A 1 82  ? 26.217  10.763  35.432  1.00 20.13 ? 82  TYR   A CB   1 
ATOM   1215 C  CG   . TYR   A 1 82  ? 25.120  11.001  34.422  1.00 20.44 ? 82  TYR   A CG   1 
ATOM   1216 C  CD1  . TYR   A 1 82  ? 25.363  11.710  33.253  1.00 23.09 ? 82  TYR   A CD1  1 
ATOM   1217 C  CD2  . TYR   A 1 82  ? 23.842  10.501  34.632  1.00 20.87 ? 82  TYR   A CD2  1 
ATOM   1218 C  CE1  . TYR   A 1 82  ? 24.361  11.932  32.331  1.00 20.99 ? 82  TYR   A CE1  1 
ATOM   1219 C  CE2  . TYR   A 1 82  ? 22.827  10.718  33.712  1.00 21.61 ? 82  TYR   A CE2  1 
ATOM   1220 C  CZ   . TYR   A 1 82  ? 23.100  11.435  32.559  1.00 23.35 ? 82  TYR   A CZ   1 
ATOM   1221 O  OH   . TYR   A 1 82  ? 22.125  11.675  31.617  1.00 24.12 ? 82  TYR   A OH   1 
ATOM   1222 H  H    . TYR   A 1 82  ? 26.651  8.734   34.244  1.00 26.17 ? 82  TYR   A H    1 
ATOM   1223 H  HA   . TYR   A 1 82  ? 27.800  11.070  34.170  1.00 25.28 ? 82  TYR   A HA   1 
ATOM   1224 H  HB2  . TYR   A 1 82  ? 25.931  10.042  36.015  1.00 24.17 ? 82  TYR   A HB2  1 
ATOM   1225 H  HB3  . TYR   A 1 82  ? 26.326  11.578  35.947  1.00 24.17 ? 82  TYR   A HB3  1 
ATOM   1226 H  HD1  . TYR   A 1 82  ? 26.213  12.052  33.094  1.00 27.73 ? 82  TYR   A HD1  1 
ATOM   1227 H  HD2  . TYR   A 1 82  ? 23.660  10.023  35.409  1.00 25.06 ? 82  TYR   A HD2  1 
ATOM   1228 H  HE1  . TYR   A 1 82  ? 24.539  12.413  31.555  1.00 25.21 ? 82  TYR   A HE1  1 
ATOM   1229 H  HE2  . TYR   A 1 82  ? 21.974  10.382  33.866  1.00 25.95 ? 82  TYR   A HE2  1 
ATOM   1230 H  HH   . TYR   A 1 82  ? 21.400  11.327  31.859  1.00 28.96 ? 82  TYR   A HH   1 
ATOM   1231 N  N    . SER   A 1 83  ? 28.981  9.198   36.428  1.00 23.45 ? 83  SER   A N    1 
ATOM   1232 C  CA   . SER   A 1 83  ? 30.076  9.056   37.382  1.00 27.45 ? 83  SER   A CA   1 
ATOM   1233 C  C    . SER   A 1 83  ? 31.332  8.438   36.769  1.00 26.68 ? 83  SER   A C    1 
ATOM   1234 O  O    . SER   A 1 83  ? 32.260  8.085   37.505  1.00 26.42 ? 83  SER   A O    1 
ATOM   1235 C  CB   . SER   A 1 83  ? 29.630  8.219   38.589  1.00 30.85 ? 83  SER   A CB   1 
ATOM   1236 O  OG   . SER   A 1 83  ? 28.462  8.754   39.186  1.00 34.95 ? 83  SER   A OG   1 
ATOM   1237 H  H    . SER   A 1 83  ? 28.590  8.454   36.243  1.00 28.16 ? 83  SER   A H    1 
ATOM   1238 H  HA   . SER   A 1 83  ? 30.316  9.936   37.712  1.00 32.96 ? 83  SER   A HA   1 
ATOM   1239 H  HB2  . SER   A 1 83  ? 29.445  7.314   38.292  1.00 37.03 ? 83  SER   A HB2  1 
ATOM   1240 H  HB3  . SER   A 1 83  ? 30.343  8.211   39.246  1.00 37.03 ? 83  SER   A HB3  1 
ATOM   1241 H  HG   . SER   A 1 83  ? 28.234  8.283   39.843  1.00 41.96 ? 83  SER   A HG   1 
ATOM   1242 N  N    . ALA   A 1 84  ? 31.389  8.299   35.441  1.00 22.65 ? 84  ALA   A N    1 
ATOM   1243 C  CA   . ALA   A 1 84  ? 32.593  7.835   34.747  1.00 23.21 ? 84  ALA   A CA   1 
ATOM   1244 C  C    . ALA   A 1 84  ? 33.067  6.489   35.289  1.00 22.99 ? 84  ALA   A C    1 
ATOM   1245 O  O    . ALA   A 1 84  ? 34.264  6.264   35.497  1.00 25.84 ? 84  ALA   A O    1 
ATOM   1246 C  CB   . ALA   A 1 84  ? 33.715  8.874   34.830  1.00 27.32 ? 84  ALA   A CB   1 
ATOM   1247 H  H    . ALA   A 1 84  ? 30.733  8.470   34.912  1.00 27.20 ? 84  ALA   A H    1 
ATOM   1248 H  HA   . ALA   A 1 84  ? 32.379  7.712   33.809  1.00 27.87 ? 84  ALA   A HA   1 
ATOM   1249 H  HB1  . ALA   A 1 84  ? 34.493  8.536   34.359  1.00 32.80 ? 84  ALA   A HB1  1 
ATOM   1250 H  HB2  . ALA   A 1 84  ? 33.412  9.699   34.420  1.00 32.80 ? 84  ALA   A HB2  1 
ATOM   1251 H  HB3  . ALA   A 1 84  ? 33.933  9.029   35.762  1.00 32.80 ? 84  ALA   A HB3  1 
ATOM   1252 N  N    . ASP   A 1 85  ? 32.113  5.584   35.516  1.00 21.21 ? 85  ASP   A N    1 
ATOM   1253 C  CA   . ASP   A 1 85  ? 32.397  4.251   36.017  1.00 24.40 ? 85  ASP   A CA   1 
ATOM   1254 C  C    . ASP   A 1 85  ? 31.902  3.151   35.090  1.00 21.21 ? 85  ASP   A C    1 
ATOM   1255 O  O    . ASP   A 1 85  ? 31.974  1.975   35.464  1.00 24.07 ? 85  ASP   A O    1 
ATOM   1256 C  CB   . ASP   A 1 85  ? 31.766  4.043   37.408  1.00 28.63 ? 85  ASP   A CB   1 
ATOM   1257 C  CG   . ASP   A 1 85  ? 30.262  4.308   37.432  1.00 27.85 ? 85  ASP   A CG   1 
ATOM   1258 O  OD1  . ASP   A 1 85  ? 29.668  4.538   36.361  1.00 24.53 ? 85  ASP   A OD1  1 
ATOM   1259 O  OD2  . ASP   A 1 85  ? 29.668  4.249   38.527  1.00 32.15 ? 85  ASP   A OD2  1 
ATOM   1260 H  H    . ASP   A 1 85  ? 31.276  5.728   35.382  1.00 25.47 ? 85  ASP   A H    1 
ATOM   1261 H  HA   . ASP   A 1 85  ? 33.357  4.147   36.110  1.00 29.29 ? 85  ASP   A HA   1 
ATOM   1262 H  HB2  . ASP   A 1 85  ? 31.912  3.125   37.686  1.00 34.38 ? 85  ASP   A HB2  1 
ATOM   1263 H  HB3  . ASP   A 1 85  ? 32.186  4.650   38.037  1.00 34.38 ? 85  ASP   A HB3  1 
ATOM   1264 N  N    . GLY   A 1 86  ? 31.381  3.494   33.913  1.00 21.32 ? 86  GLY   A N    1 
ATOM   1265 C  CA   . GLY   A 1 86  ? 30.852  2.511   32.991  1.00 18.11 ? 86  GLY   A CA   1 
ATOM   1266 C  C    . GLY   A 1 86  ? 29.400  2.128   33.199  1.00 19.58 ? 86  GLY   A C    1 
ATOM   1267 O  O    . GLY   A 1 86  ? 28.881  1.311   32.425  1.00 20.00 ? 86  GLY   A O    1 
ATOM   1268 H  H    . GLY   A 1 86  ? 31.325  4.303   33.627  1.00 25.60 ? 86  GLY   A H    1 
ATOM   1269 H  HA2  . GLY   A 1 86  ? 30.941  2.852   32.087  1.00 21.75 ? 86  GLY   A HA2  1 
ATOM   1270 H  HA3  . GLY   A 1 86  ? 31.384  1.703   33.057  1.00 21.75 ? 86  GLY   A HA3  1 
ATOM   1271 N  N    . TYR   A 1 87  ? 28.723  2.702   34.193  1.00 19.22 ? 87  TYR   A N    1 
ATOM   1272 C  CA   . TYR   A 1 87  ? 27.395  2.260   34.588  1.00 19.63 ? 87  TYR   A CA   1 
ATOM   1273 C  C    . TYR   A 1 87  ? 26.369  3.379   34.428  1.00 18.74 ? 87  TYR   A C    1 
ATOM   1274 O  O    . TYR   A 1 87  ? 26.705  4.568   34.397  1.00 21.99 ? 87  TYR   A O    1 
ATOM   1275 C  CB   . TYR   A 1 87  ? 27.387  1.763   36.048  1.00 19.06 ? 87  TYR   A CB   1 
ATOM   1276 C  CG   . TYR   A 1 87  ? 28.083  0.438   36.223  1.00 20.52 ? 87  TYR   A CG   1 
ATOM   1277 C  CD1  . TYR   A 1 87  ? 27.466  -0.741  35.845  1.00 19.42 ? 87  TYR   A CD1  1 
ATOM   1278 C  CD2  . TYR   A 1 87  ? 29.368  0.368   36.754  1.00 23.60 ? 87  TYR   A CD2  1 
ATOM   1279 C  CE1  . TYR   A 1 87  ? 28.106  -1.957  35.987  1.00 20.91 ? 87  TYR   A CE1  1 
ATOM   1280 C  CE2  . TYR   A 1 87  ? 30.015  -0.846  36.906  1.00 24.76 ? 87  TYR   A CE2  1 
ATOM   1281 C  CZ   . TYR   A 1 87  ? 29.375  -2.005  36.513  1.00 22.80 ? 87  TYR   A CZ   1 
ATOM   1282 O  OH   . TYR   A 1 87  ? 30.009  -3.219  36.658  1.00 28.79 ? 87  TYR   A OH   1 
ATOM   1283 H  H    . TYR   A 1 87  ? 29.020  3.361   34.659  1.00 23.08 ? 87  TYR   A H    1 
ATOM   1284 H  HA   . TYR   A 1 87  ? 27.122  1.522   34.021  1.00 23.58 ? 87  TYR   A HA   1 
ATOM   1285 H  HB2  . TYR   A 1 87  ? 27.840  2.415   36.605  1.00 22.90 ? 87  TYR   A HB2  1 
ATOM   1286 H  HB3  . TYR   A 1 87  ? 26.468  1.659   36.341  1.00 22.90 ? 87  TYR   A HB3  1 
ATOM   1287 H  HD1  . TYR   A 1 87  ? 26.610  -0.714  35.482  1.00 23.33 ? 87  TYR   A HD1  1 
ATOM   1288 H  HD2  . TYR   A 1 87  ? 29.799  1.151   37.012  1.00 28.34 ? 87  TYR   A HD2  1 
ATOM   1289 H  HE1  . TYR   A 1 87  ? 27.679  -2.742  35.729  1.00 25.11 ? 87  TYR   A HE1  1 
ATOM   1290 H  HE2  . TYR   A 1 87  ? 30.874  -0.880  37.261  1.00 29.73 ? 87  TYR   A HE2  1 
ATOM   1291 H  HH   . TYR   A 1 87  ? 29.507  -3.839  36.394  1.00 34.57 ? 87  TYR   A HH   1 
ATOM   1292 N  N    . ASP   A 1 88  ? 25.106  2.968   34.311  1.00 18.55 ? 88  ASP   A N    1 
ATOM   1293 C  CA   . ASP   A 1 88  ? 23.957  3.871   34.304  1.00 18.01 ? 88  ASP   A CA   1 
ATOM   1294 C  C    . ASP   A 1 88  ? 22.796  3.007   34.790  1.00 20.29 ? 88  ASP   A C    1 
ATOM   1295 O  O    . ASP   A 1 88  ? 21.845  2.751   34.040  1.00 19.42 ? 88  ASP   A O    1 
ATOM   1296 C  CB   . ASP   A 1 88  ? 23.705  4.454   32.921  1.00 17.83 ? 88  ASP   A CB   1 
ATOM   1297 C  CG   . ASP   A 1 88  ? 22.466  5.346   32.878  1.00 20.24 ? 88  ASP   A CG   1 
ATOM   1298 O  OD1  . ASP   A 1 88  ? 22.062  5.896   33.929  1.00 23.16 ? 88  ASP   A OD1  1 
ATOM   1299 O  OD2  . ASP   A 1 88  ? 21.934  5.550   31.768  1.00 21.84 ? 88  ASP   A OD2  1 
ATOM   1300 H  H    . ASP   A 1 88  ? 24.884  2.141   34.232  1.00 22.28 ? 88  ASP   A H    1 
ATOM   1301 H  HA   . ASP   A 1 88  ? 24.099  4.596   34.933  1.00 21.63 ? 88  ASP   A HA   1 
ATOM   1302 H  HB2  . ASP   A 1 88  ? 24.470  4.989   32.659  1.00 21.42 ? 88  ASP   A HB2  1 
ATOM   1303 H  HB3  . ASP   A 1 88  ? 23.575  3.729   32.290  1.00 21.42 ? 88  ASP   A HB3  1 
ATOM   1304 N  N    . ARG   A 1 89  ? 22.889  2.511   36.021  1.00 22.20 ? 89  ARG   A N    1 
ATOM   1305 C  CA   . ARG   A 1 89  ? 22.030  1.418   36.457  1.00 19.22 ? 89  ARG   A CA   1 
ATOM   1306 C  C    . ARG   A 1 89  ? 20.583  1.840   36.627  1.00 19.10 ? 89  ARG   A C    1 
ATOM   1307 O  O    . ARG   A 1 89  ? 20.282  2.938   37.106  1.00 21.47 ? 89  ARG   A O    1 
ATOM   1308 C  CB   . ARG   A 1 89  ? 22.530  0.824   37.776  1.00 21.66 ? 89  ARG   A CB   1 
ATOM   1309 C  CG   . ARG   A 1 89  ? 23.892  0.179   37.730  1.00 26.26 ? 89  ARG   A CG   1 
ATOM   1310 C  CD   . ARG   A 1 89  ? 24.155  -0.553  39.044  1.00 30.30 ? 89  ARG   A CD   1 
ATOM   1311 N  NE   . ARG   A 1 89  ? 25.472  -1.180  39.075  1.00 30.95 ? 89  ARG   A NE   1 
ATOM   1312 C  CZ   . ARG   A 1 89  ? 26.609  -0.569  39.375  1.00 30.66 ? 89  ARG   A CZ   1 
ATOM   1313 N  NH1  . ARG   A 1 89  ? 26.648  0.720   39.670  1.00 38.81 ? 89  ARG   A NH1  1 
ATOM   1314 N  NH2  . ARG   A 1 89  ? 27.741  -1.267  39.384  1.00 34.68 ? 89  ARG   A NH2  1 
ATOM   1315 H  H    . ARG   A 1 89  ? 23.440  2.790   36.620  1.00 26.65 ? 89  ARG   A H    1 
ATOM   1316 H  HA   . ARG   A 1 89  ? 22.057  0.718   35.787  1.00 23.08 ? 89  ARG   A HA   1 
ATOM   1317 H  HB2  . ARG   A 1 89  ? 22.568  1.534   38.436  1.00 26.02 ? 89  ARG   A HB2  1 
ATOM   1318 H  HB3  . ARG   A 1 89  ? 21.898  0.147   38.065  1.00 26.02 ? 89  ARG   A HB3  1 
ATOM   1319 H  HG2  . ARG   A 1 89  ? 23.924  -0.464  37.005  1.00 31.53 ? 89  ARG   A HG2  1 
ATOM   1320 H  HG3  . ARG   A 1 89  ? 24.572  0.861   37.613  1.00 31.53 ? 89  ARG   A HG3  1 
ATOM   1321 H  HD2  . ARG   A 1 89  ? 24.103  0.080   39.777  1.00 36.38 ? 89  ARG   A HD2  1 
ATOM   1322 H  HD3  . ARG   A 1 89  ? 23.489  -1.249  39.158  1.00 36.38 ? 89  ARG   A HD3  1 
ATOM   1323 H  HE   . ARG   A 1 89  ? 25.515  -2.015  38.874  1.00 37.16 ? 89  ARG   A HE   1 
ATOM   1324 H  HH11 . ARG   A 1 89  ? 25.925  1.185   39.670  1.00 46.60 ? 89  ARG   A HH11 1 
ATOM   1325 H  HH12 . ARG   A 1 89  ? 27.399  1.094   39.861  1.00 46.60 ? 89  ARG   A HH12 1 
ATOM   1326 H  HH21 . ARG   A 1 89  ? 27.731  -2.106  39.194  1.00 41.64 ? 89  ARG   A HH21 1 
ATOM   1327 H  HH22 . ARG   A 1 89  ? 28.484  -0.879  39.577  1.00 41.64 ? 89  ARG   A HH22 1 
ATOM   1328 N  N    . ASP   A 1 90  ? 19.682  0.934   36.255  1.00 19.67 ? 90  ASP   A N    1 
ATOM   1329 C  CA   . ASP   A 1 90  ? 18.266  1.101   36.537  1.00 19.19 ? 90  ASP   A CA   1 
ATOM   1330 C  C    . ASP   A 1 90  ? 17.568  -0.245  36.468  1.00 19.63 ? 90  ASP   A C    1 
ATOM   1331 O  O    . ASP   A 1 90  ? 17.736  -0.981  35.491  1.00 19.64 ? 90  ASP   A O    1 
ATOM   1332 C  CB   . ASP   A 1 90  ? 17.610  2.066   35.555  1.00 23.16 ? 90  ASP   A CB   1 
ATOM   1333 C  CG   . ASP   A 1 90  ? 16.318  2.600   36.088  1.00 31.33 ? 90  ASP   A CG   1 
ATOM   1334 O  OD1  . ASP   A 1 90  ? 15.329  1.840   36.085  1.00 28.14 ? 90  ASP   A OD1  1 
ATOM   1335 O  OD2  . ASP   A 1 90  ? 16.305  3.745   36.574  1.00 37.14 ? 90  ASP   A OD2  1 
ATOM   1336 H  H    . ASP   A 1 90  ? 19.871  0.208   35.834  1.00 23.62 ? 90  ASP   A H    1 
ATOM   1337 H  HA   . ASP   A 1 90  ? 18.157  1.456   37.433  1.00 23.04 ? 90  ASP   A HA   1 
ATOM   1338 H  HB2  . ASP   A 1 90  ? 18.206  2.815   35.396  1.00 27.81 ? 90  ASP   A HB2  1 
ATOM   1339 H  HB3  . ASP   A 1 90  ? 17.427  1.601   34.724  1.00 27.81 ? 90  ASP   A HB3  1 
ATOM   1340 N  N    . ASN   A 1 91  ? 16.784  -0.556  37.507  1.00 21.92 ? 91  ASN   A N    1 
ATOM   1341 C  CA   . ASN   A 1 91  ? 15.899  -1.721  37.504  1.00 21.47 ? 91  ASN   A CA   1 
ATOM   1342 C  C    . ASN   A 1 91  ? 16.557  -2.992  37.000  1.00 20.91 ? 91  ASN   A C    1 
ATOM   1343 O  O    . ASN   A 1 91  ? 15.983  -3.757  36.227  1.00 22.01 ? 91  ASN   A O    1 
ATOM   1344 C  CB   . ASN   A 1 91  ? 14.605  -1.407  36.740  1.00 21.65 ? 91  ASN   A CB   1 
ATOM   1345 C  CG   . ASN   A 1 91  ? 13.543  -2.461  36.956  1.00 20.06 ? 91  ASN   A CG   1 
ATOM   1346 O  OD1  . ASN   A 1 91  ? 13.437  -3.027  38.040  1.00 22.32 ? 91  ASN   A OD1  1 
ATOM   1347 N  ND2  . ASN   A 1 91  ? 12.683  -2.662  35.949  1.00 21.02 ? 91  ASN   A ND2  1 
ATOM   1348 H  H    . ASN   A 1 91  ? 16.749  -0.099  38.235  1.00 26.32 ? 91  ASN   A H    1 
ATOM   1349 H  HA   . ASN   A 1 91  ? 15.642  -1.892  38.423  1.00 25.78 ? 91  ASN   A HA   1 
ATOM   1350 H  HB2  . ASN   A 1 91  ? 14.253  -0.557  37.047  1.00 26.00 ? 91  ASN   A HB2  1 
ATOM   1351 H  HB3  . ASN   A 1 91  ? 14.799  -1.364  35.791  1.00 26.00 ? 91  ASN   A HB3  1 
ATOM   1352 H  HD21 . ASN   A 1 91  ? 12.057  -3.246  36.029  1.00 25.24 ? 91  ASN   A HD21 1 
ATOM   1353 H  HD22 . ASN   A 1 91  ? 12.779  -2.234  35.210  1.00 25.24 ? 91  ASN   A HD22 1 
ATOM   1354 N  N    . GLY   A 1 92  ? 17.755  -3.248  37.501  1.00 21.25 ? 92  GLY   A N    1 
ATOM   1355 C  CA   . GLY   A 1 92  ? 18.418  -4.496  37.223  1.00 23.79 ? 92  GLY   A CA   1 
ATOM   1356 C  C    . GLY   A 1 92  ? 19.258  -4.518  35.970  1.00 21.23 ? 92  GLY   A C    1 
ATOM   1357 O  O    . GLY   A 1 92  ? 19.869  -5.552  35.678  1.00 21.16 ? 92  GLY   A O    1 
ATOM   1358 H  H    . GLY   A 1 92  ? 18.201  -2.712  38.004  1.00 25.52 ? 92  GLY   A H    1 
ATOM   1359 H  HA2  . GLY   A 1 92  ? 18.996  -4.716  37.971  1.00 28.56 ? 92  GLY   A HA2  1 
ATOM   1360 H  HA3  . GLY   A 1 92  ? 17.751  -5.196  37.146  1.00 28.56 ? 92  GLY   A HA3  1 
ATOM   1361 N  N    . ALA   A 1 93  ? 19.311  -3.416  35.227  1.00 20.19 ? 93  ALA   A N    1 
ATOM   1362 C  CA   . ALA   A 1 93  ? 20.180  -3.292  34.063  1.00 20.32 ? 93  ALA   A CA   1 
ATOM   1363 C  C    . ALA   A 1 93  ? 21.408  -2.456  34.400  1.00 20.56 ? 93  ALA   A C    1 
ATOM   1364 O  O    . ALA   A 1 93  ? 21.320  -1.469  35.139  1.00 20.87 ? 93  ALA   A O    1 
ATOM   1365 C  CB   . ALA   A 1 93  ? 19.440  -2.656  32.882  1.00 17.30 ? 93  ALA   A CB   1 
ATOM   1366 H  H    . ALA   A 1 93  ? 18.842  -2.712  35.381  1.00 24.25 ? 93  ALA   A H    1 
ATOM   1367 H  HA   . ALA   A 1 93  ? 20.480  -4.173  33.791  1.00 24.40 ? 93  ALA   A HA   1 
ATOM   1368 H  HB1  . ALA   A 1 93  ? 20.045  -2.596  32.126  1.00 20.78 ? 93  ALA   A HB1  1 
ATOM   1369 H  HB2  . ALA   A 1 93  ? 18.677  -3.210  32.653  1.00 20.78 ? 93  ALA   A HB2  1 
ATOM   1370 H  HB3  . ALA   A 1 93  ? 19.141  -1.770  33.138  1.00 20.78 ? 93  ALA   A HB3  1 
ATOM   1371 N  N    . ALA   A 1 94  ? 22.548  -2.837  33.819  1.00 19.70 ? 94  ALA   A N    1 
ATOM   1372 C  CA   . ALA   A 1 94  ? 23.813  -2.162  34.102  1.00 17.77 ? 94  ALA   A CA   1 
ATOM   1373 C  C    . ALA   A 1 94  ? 23.865  -0.764  33.500  1.00 17.34 ? 94  ALA   A C    1 
ATOM   1374 O  O    . ALA   A 1 94  ? 24.364  0.175   34.140  1.00 17.68 ? 94  ALA   A O    1 
ATOM   1375 C  CB   . ALA   A 1 94  ? 24.982  -2.993  33.563  1.00 19.50 ? 94  ALA   A CB   1 
ATOM   1376 H  H    . ALA   A 1 94  ? 22.614  -3.484  33.257  1.00 23.66 ? 94  ALA   A H    1 
ATOM   1377 H  HA   . ALA   A 1 94  ? 23.920  -2.079  35.062  1.00 21.34 ? 94  ALA   A HA   1 
ATOM   1378 H  HB1  . ALA   A 1 94  ? 25.813  -2.532  33.758  1.00 23.42 ? 94  ALA   A HB1  1 
ATOM   1379 H  HB2  . ALA   A 1 94  ? 24.976  -3.862  33.994  1.00 23.42 ? 94  ALA   A HB2  1 
ATOM   1380 H  HB3  . ALA   A 1 94  ? 24.879  -3.098  32.604  1.00 23.42 ? 94  ALA   A HB3  1 
ATOM   1381 N  N    . SER   A 1 95  ? 23.426  -0.614  32.256  1.00 17.65 ? 95  SER   A N    1 
ATOM   1382 C  CA   . SER   A 1 95  ? 23.468  0.666   31.558  1.00 16.47 ? 95  SER   A CA   1 
ATOM   1383 C  C    . SER   A 1 95  ? 22.562  0.620   30.336  1.00 16.44 ? 95  SER   A C    1 
ATOM   1384 O  O    . SER   A 1 95  ? 23.028  0.341   29.226  1.00 16.94 ? 95  SER   A O    1 
ATOM   1385 C  CB   . SER   A 1 95  ? 24.887  1.034   31.121  1.00 15.74 ? 95  SER   A CB   1 
ATOM   1386 O  OG   . SER   A 1 95  ? 24.902  2.317   30.515  1.00 17.72 ? 95  SER   A OG   1 
ATOM   1387 H  H    . SER   A 1 95  ? 23.092  -1.252  31.785  1.00 21.20 ? 95  SER   A H    1 
ATOM   1388 H  HA   . SER   A 1 95  ? 23.148  1.363   32.151  1.00 19.78 ? 95  SER   A HA   1 
ATOM   1389 H  HB2  . SER   A 1 95  ? 25.466  1.043   31.899  1.00 18.91 ? 95  SER   A HB2  1 
ATOM   1390 H  HB3  . SER   A 1 95  ? 25.200  0.378   30.480  1.00 18.91 ? 95  SER   A HB3  1 
ATOM   1391 H  HG   . SER   A 1 95  ? 24.167  2.474   30.143  1.00 21.28 ? 95  SER   A HG   1 
ATOM   1392 N  N    . PRO   A 1 96  ? 21.270  0.893   30.490  1.00 17.04 ? 96  PRO   A N    1 
ATOM   1393 C  CA   . PRO   A 1 96  ? 20.395  0.942   29.305  1.00 17.18 ? 96  PRO   A CA   1 
ATOM   1394 C  C    . PRO   A 1 96  ? 20.858  1.926   28.247  1.00 17.94 ? 96  PRO   A C    1 
ATOM   1395 O  O    . PRO   A 1 96  ? 20.611  1.699   27.055  1.00 17.56 ? 96  PRO   A O    1 
ATOM   1396 C  CB   . PRO   A 1 96  ? 19.036  1.331   29.903  1.00 19.12 ? 96  PRO   A CB   1 
ATOM   1397 C  CG   . PRO   A 1 96  ? 19.109  0.740   31.314  1.00 17.77 ? 96  PRO   A CG   1 
ATOM   1398 C  CD   . PRO   A 1 96  ? 20.512  1.079   31.744  1.00 19.04 ? 96  PRO   A CD   1 
ATOM   1399 H  HA   . PRO   A 1 96  ? 20.325  0.060   28.907  1.00 20.63 ? 96  PRO   A HA   1 
ATOM   1400 H  HB2  . PRO   A 1 96  ? 18.950  2.296   29.935  1.00 22.97 ? 96  PRO   A HB2  1 
ATOM   1401 H  HB3  . PRO   A 1 96  ? 18.317  0.929   29.391  1.00 22.97 ? 96  PRO   A HB3  1 
ATOM   1402 H  HG2  . PRO   A 1 96  ? 18.454  1.166   31.889  1.00 21.35 ? 96  PRO   A HG2  1 
ATOM   1403 H  HG3  . PRO   A 1 96  ? 18.975  -0.220  31.281  1.00 21.35 ? 96  PRO   A HG3  1 
ATOM   1404 H  HD2  . PRO   A 1 96  ? 20.565  2.001   32.042  1.00 22.86 ? 96  PRO   A HD2  1 
ATOM   1405 H  HD3  . PRO   A 1 96  ? 20.819  0.461   32.426  1.00 22.86 ? 96  PRO   A HD3  1 
ATOM   1406 N  N    . THR   A 1 97  ? 21.542  3.001   28.637  1.00 15.95 ? 97  THR   A N    1 
ATOM   1407 C  CA   . THR   A 1 97  ? 21.991  3.977   27.650  1.00 16.35 ? 97  THR   A CA   1 
ATOM   1408 C  C    . THR   A 1 97  ? 23.148  3.433   26.817  1.00 17.50 ? 97  THR   A C    1 
ATOM   1409 O  O    . THR   A 1 97  ? 23.207  3.674   25.604  1.00 16.76 ? 97  THR   A O    1 
ATOM   1410 C  CB   . THR   A 1 97  ? 22.380  5.277   28.348  1.00 17.40 ? 97  THR   A CB   1 
ATOM   1411 O  OG1  . THR   A 1 97  ? 23.160  4.978   29.513  1.00 17.48 ? 97  THR   A OG1  1 
ATOM   1412 C  CG2  . THR   A 1 97  ? 21.139  6.047   28.787  1.00 20.11 ? 97  THR   A CG2  1 
ATOM   1413 H  H    . THR   A 1 97  ? 21.755  3.185   29.450  1.00 19.16 ? 97  THR   A H    1 
ATOM   1414 H  HA   . THR   A 1 97  ? 21.257  4.172   27.047  1.00 19.64 ? 97  THR   A HA   1 
ATOM   1415 H  HB   . THR   A 1 97  ? 22.895  5.833   27.743  1.00 20.90 ? 97  THR   A HB   1 
ATOM   1416 H  HG1  . THR   A 1 97  ? 23.378  5.689   29.903  1.00 20.99 ? 97  THR   A HG1  1 
ATOM   1417 H  HG21 . THR   A 1 97  ? 21.342  6.567   29.580  1.00 24.15 ? 97  THR   A HG21 1 
ATOM   1418 H  HG22 . THR   A 1 97  ? 20.862  6.652   28.085  1.00 24.15 ? 97  THR   A HG22 1 
ATOM   1419 H  HG23 . THR   A 1 97  ? 20.442  5.414   29.003  1.00 24.15 ? 97  THR   A HG23 1 
ATOM   1420 N  N    . ASN   A 1 98  ? 24.076  2.694   27.435  1.00 14.99 ? 98  ASN   A N    1 
ATOM   1421 C  CA   . ASN   A 1 98  ? 25.119  2.027   26.651  1.00 15.48 ? 98  ASN   A CA   1 
ATOM   1422 C  C    . ASN   A 1 98  ? 24.494  1.020   25.685  1.00 17.94 ? 98  ASN   A C    1 
ATOM   1423 O  O    . ASN   A 1 98  ? 24.840  0.973   24.496  1.00 16.07 ? 98  ASN   A O    1 
ATOM   1424 C  CB   . ASN   A 1 98  ? 26.110  1.289   27.554  1.00 15.18 ? 98  ASN   A CB   1 
ATOM   1425 C  CG   . ASN   A 1 98  ? 27.078  2.211   28.268  1.00 16.43 ? 98  ASN   A CG   1 
ATOM   1426 O  OD1  . ASN   A 1 98  ? 27.124  3.418   28.020  1.00 18.65 ? 98  ASN   A OD1  1 
ATOM   1427 N  ND2  . ASN   A 1 98  ? 27.893  1.629   29.147  1.00 18.65 ? 98  ASN   A ND2  1 
ATOM   1428 H  H    . ASN   A 1 98  ? 24.123  2.566   28.283  1.00 18.00 ? 98  ASN   A H    1 
ATOM   1429 H  HA   . ASN   A 1 98  ? 25.607  2.687   26.134  1.00 18.60 ? 98  ASN   A HA   1 
ATOM   1430 H  HB2  . ASN   A 1 98  ? 25.615  0.798   28.228  1.00 18.24 ? 98  ASN   A HB2  1 
ATOM   1431 H  HB3  . ASN   A 1 98  ? 26.629  0.674   27.013  1.00 18.24 ? 98  ASN   A HB3  1 
ATOM   1432 H  HD21 . ASN   A 1 98  ? 28.466  2.102   29.581  1.00 22.40 ? 98  ASN   A HD21 1 
ATOM   1433 H  HD22 . ASN   A 1 98  ? 27.837  0.783   29.290  1.00 22.40 ? 98  ASN   A HD22 1 
ATOM   1434 N  N    . ASP   A 1 99  ? 23.591  0.175   26.196  1.00 16.44 ? 99  ASP   A N    1 
ATOM   1435 C  CA   . ASP   A 1 99  ? 22.947  -0.831  25.355  1.00 15.07 ? 99  ASP   A CA   1 
ATOM   1436 C  C    . ASP   A 1 99  ? 22.187  -0.198  24.204  1.00 18.00 ? 99  ASP   A C    1 
ATOM   1437 O  O    . ASP   A 1 99  ? 22.135  -0.773  23.109  1.00 16.29 ? 99  ASP   A O    1 
ATOM   1438 C  CB   . ASP   A 1 99  ? 22.034  -1.714  26.212  1.00 14.90 ? 99  ASP   A CB   1 
ATOM   1439 C  CG   . ASP   A 1 99  ? 22.791  -2.817  26.943  1.00 19.11 ? 99  ASP   A CG   1 
ATOM   1440 O  OD1  . ASP   A 1 99  ? 23.866  -3.227  26.444  1.00 19.96 ? 99  ASP   A OD1  1 
ATOM   1441 O  OD2  . ASP   A 1 99  ? 22.339  -3.244  28.024  1.00 17.96 ? 99  ASP   A OD2  1 
ATOM   1442 H  H    . ASP   A 1 99  ? 23.339  0.166   27.018  1.00 19.74 ? 99  ASP   A H    1 
ATOM   1443 H  HA   . ASP   A 1 99  ? 23.634  -1.397  24.970  1.00 18.10 ? 99  ASP   A HA   1 
ATOM   1444 H  HB2  . ASP   A 1 99  ? 21.594  -1.162  26.877  1.00 17.89 ? 99  ASP   A HB2  1 
ATOM   1445 H  HB3  . ASP   A 1 99  ? 21.373  -2.134  25.639  1.00 17.89 ? 99  ASP   A HB3  1 
ATOM   1446 N  N    . ALA   A 1 100 ? 21.619  0.995   24.411  1.00 15.06 ? 100 ALA   A N    1 
ATOM   1447 C  CA   . ALA   A 1 100 ? 20.889  1.672   23.337  1.00 15.65 ? 100 ALA   A CA   1 
ATOM   1448 C  C    . ALA   A 1 100 ? 21.832  2.165   22.253  1.00 16.90 ? 100 ALA   A C    1 
ATOM   1449 O  O    . ALA   A 1 100 ? 21.515  2.092   21.056  1.00 16.90 ? 100 ALA   A O    1 
ATOM   1450 C  CB   . ALA   A 1 100 ? 20.086  2.851   23.891  1.00 17.30 ? 100 ALA   A CB   1 
ATOM   1451 H  H    . ALA   A 1 100 ? 21.642  1.427   25.154  1.00 18.09 ? 100 ALA   A H    1 
ATOM   1452 H  HA   . ALA   A 1 100 ? 20.267  1.047   22.933  1.00 18.80 ? 100 ALA   A HA   1 
ATOM   1453 H  HB1  . ALA   A 1 100 ? 19.621  3.287   23.160  1.00 20.78 ? 100 ALA   A HB1  1 
ATOM   1454 H  HB2  . ALA   A 1 100 ? 19.446  2.518   24.539  1.00 20.78 ? 100 ALA   A HB2  1 
ATOM   1455 H  HB3  . ALA   A 1 100 ? 20.695  3.476   24.316  1.00 20.78 ? 100 ALA   A HB3  1 
ATOM   1456 N  N    . LEU   A 1 101 ? 22.979  2.717   22.654  1.00 16.61 ? 101 LEU   A N    1 
ATOM   1457 C  CA   . LEU   A 1 101 ? 23.950  3.196   21.681  1.00 15.31 ? 101 LEU   A CA   1 
ATOM   1458 C  C    . LEU   A 1 101 ? 24.474  2.039   20.845  1.00 17.98 ? 101 LEU   A C    1 
ATOM   1459 O  O    . LEU   A 1 101 ? 24.567  2.144   19.617  1.00 17.87 ? 101 LEU   A O    1 
ATOM   1460 C  CB   . LEU   A 1 101 ? 25.082  3.917   22.410  1.00 18.69 ? 101 LEU   A CB   1 
ATOM   1461 C  CG   . LEU   A 1 101 ? 26.032  4.765   21.553  1.00 19.09 ? 101 LEU   A CG   1 
ATOM   1462 C  CD1  . LEU   A 1 101 ? 25.293  5.802   20.712  1.00 21.63 ? 101 LEU   A CD1  1 
ATOM   1463 C  CD2  . LEU   A 1 101 ? 27.083  5.450   22.435  1.00 19.18 ? 101 LEU   A CD2  1 
ATOM   1464 H  H    . LEU   A 1 101 ? 23.213  2.823   23.475  1.00 19.95 ? 101 LEU   A H    1 
ATOM   1465 H  HA   . LEU   A 1 101 ? 23.515  3.826   21.087  1.00 18.39 ? 101 LEU   A HA   1 
ATOM   1466 H  HB2  . LEU   A 1 101 ? 24.688  4.508   23.070  1.00 22.45 ? 101 LEU   A HB2  1 
ATOM   1467 H  HB3  . LEU   A 1 101 ? 25.623  3.250   22.862  1.00 22.45 ? 101 LEU   A HB3  1 
ATOM   1468 H  HG   . LEU   A 1 101 ? 26.503  4.177   20.942  1.00 22.92 ? 101 LEU   A HG   1 
ATOM   1469 H  HD11 . LEU   A 1 101 ? 25.942  6.401   20.311  1.00 25.98 ? 101 LEU   A HD11 1 
ATOM   1470 H  HD12 . LEU   A 1 101 ? 24.790  5.348   20.018  1.00 25.98 ? 101 LEU   A HD12 1 
ATOM   1471 H  HD13 . LEU   A 1 101 ? 24.692  6.303   21.285  1.00 25.98 ? 101 LEU   A HD13 1 
ATOM   1472 H  HD21 . LEU   A 1 101 ? 27.754  5.858   21.866  1.00 23.03 ? 101 LEU   A HD21 1 
ATOM   1473 H  HD22 . LEU   A 1 101 ? 26.649  6.130   22.973  1.00 23.03 ? 101 LEU   A HD22 1 
ATOM   1474 H  HD23 . LEU   A 1 101 ? 27.496  4.785   23.008  1.00 23.03 ? 101 LEU   A HD23 1 
ATOM   1475 N  N    . TYR   A 1 102 ? 24.775  0.905   21.489  1.00 17.85 ? 102 TYR   A N    1 
ATOM   1476 C  CA   . TYR   A 1 102 ? 25.220  -0.277  20.758  1.00 14.39 ? 102 TYR   A CA   1 
ATOM   1477 C  C    . TYR   A 1 102 ? 24.110  -0.831  19.863  1.00 17.70 ? 102 TYR   A C    1 
ATOM   1478 O  O    . TYR   A 1 102 ? 24.351  -1.171  18.694  1.00 18.89 ? 102 TYR   A O    1 
ATOM   1479 C  CB   . TYR   A 1 102 ? 25.724  -1.346  21.735  1.00 19.93 ? 102 TYR   A CB   1 
ATOM   1480 C  CG   . TYR   A 1 102 ? 26.227  -2.575  21.017  1.00 19.50 ? 102 TYR   A CG   1 
ATOM   1481 C  CD1  . TYR   A 1 102 ? 27.397  -2.542  20.274  1.00 23.34 ? 102 TYR   A CD1  1 
ATOM   1482 C  CD2  . TYR   A 1 102 ? 25.510  -3.764  21.060  1.00 20.47 ? 102 TYR   A CD2  1 
ATOM   1483 C  CE1  . TYR   A 1 102 ? 27.845  -3.661  19.593  1.00 24.48 ? 102 TYR   A CE1  1 
ATOM   1484 C  CE2  . TYR   A 1 102 ? 25.954  -4.889  20.388  1.00 22.73 ? 102 TYR   A CE2  1 
ATOM   1485 C  CZ   . TYR   A 1 102 ? 27.123  -4.835  19.658  1.00 26.55 ? 102 TYR   A CZ   1 
ATOM   1486 O  OH   . TYR   A 1 102 ? 27.554  -5.959  18.990  1.00 31.59 ? 102 TYR   A OH   1 
ATOM   1487 H  H    . TYR   A 1 102 ? 24.729  0.799   22.341  1.00 21.44 ? 102 TYR   A H    1 
ATOM   1488 H  HA   . TYR   A 1 102 ? 25.962  -0.027  20.186  1.00 17.29 ? 102 TYR   A HA   1 
ATOM   1489 H  HB2  . TYR   A 1 102 ? 26.455  -0.981  22.258  1.00 23.93 ? 102 TYR   A HB2  1 
ATOM   1490 H  HB3  . TYR   A 1 102 ? 24.996  -1.613  22.318  1.00 23.93 ? 102 TYR   A HB3  1 
ATOM   1491 H  HD1  . TYR   A 1 102 ? 27.886  -1.752  20.226  1.00 28.03 ? 102 TYR   A HD1  1 
ATOM   1492 H  HD2  . TYR   A 1 102 ? 24.720  -3.805  21.549  1.00 24.59 ? 102 TYR   A HD2  1 
ATOM   1493 H  HE1  . TYR   A 1 102 ? 28.635  -3.625  19.103  1.00 29.40 ? 102 TYR   A HE1  1 
ATOM   1494 H  HE2  . TYR   A 1 102 ? 25.466  -5.679  20.429  1.00 27.29 ? 102 TYR   A HE2  1 
ATOM   1495 H  HH   . TYR   A 1 102 ? 27.019  -6.593  19.120  1.00 37.93 ? 102 TYR   A HH   1 
ATOM   1496 N  N    . ALA   A 1 103 ? 22.890  -0.935  20.387  1.00 16.21 ? 103 ALA   A N    1 
ATOM   1497 C  CA   . ALA   A 1 103 ? 21.798  -1.471  19.581  1.00 16.97 ? 103 ALA   A CA   1 
ATOM   1498 C  C    . ALA   A 1 103 ? 21.568  -0.629  18.332  1.00 19.96 ? 103 ALA   A C    1 
ATOM   1499 O  O    . ALA   A 1 103 ? 21.342  -1.169  17.243  1.00 18.78 ? 103 ALA   A O    1 
ATOM   1500 C  CB   . ALA   A 1 103 ? 20.512  -1.559  20.406  1.00 18.00 ? 103 ALA   A CB   1 
ATOM   1501 H  H    . ALA   A 1 103 ? 22.673  -0.708  21.187  1.00 19.47 ? 103 ALA   A H    1 
ATOM   1502 H  HA   . ALA   A 1 103 ? 22.034  -2.364  19.292  1.00 20.38 ? 103 ALA   A HA   1 
ATOM   1503 H  HB1  . ALA   A 1 103 ? 19.804  -1.917  19.849  1.00 21.62 ? 103 ALA   A HB1  1 
ATOM   1504 H  HB2  . ALA   A 1 103 ? 20.664  -2.143  21.165  1.00 21.62 ? 103 ALA   A HB2  1 
ATOM   1505 H  HB3  . ALA   A 1 103 ? 20.274  -0.671  20.714  1.00 21.62 ? 103 ALA   A HB3  1 
ATOM   1506 N  N    . GLY   A 1 104 ? 21.600  0.696   18.468  1.00 16.60 ? 104 GLY   A N    1 
ATOM   1507 C  CA   . GLY   A 1 104 ? 21.451  1.545   17.300  1.00 17.30 ? 104 GLY   A CA   1 
ATOM   1508 C  C    . GLY   A 1 104 ? 22.543  1.305   16.277  1.00 18.75 ? 104 GLY   A C    1 
ATOM   1509 O  O    . GLY   A 1 104 ? 22.286  1.288   15.064  1.00 21.01 ? 104 GLY   A O    1 
ATOM   1510 H  H    . GLY   A 1 104 ? 21.705  1.116   19.211  1.00 19.94 ? 104 GLY   A H    1 
ATOM   1511 H  HA2  . GLY   A 1 104 ? 20.593  1.373   16.881  1.00 20.78 ? 104 GLY   A HA2  1 
ATOM   1512 H  HA3  . GLY   A 1 104 ? 21.481  2.476   17.570  1.00 20.78 ? 104 GLY   A HA3  1 
ATOM   1513 N  N    . TYR   A 1 105 ? 23.780  1.119   16.746  1.00 17.74 ? 105 TYR   A N    1 
ATOM   1514 C  CA   . TYR   A 1 105 ? 24.885  0.797   15.851  1.00 17.51 ? 105 TYR   A CA   1 
ATOM   1515 C  C    . TYR   A 1 105 ? 24.574  -0.467  15.064  1.00 18.54 ? 105 TYR   A C    1 
ATOM   1516 O  O    . TYR   A 1 105 ? 24.661  -0.490  13.828  1.00 20.51 ? 105 TYR   A O    1 
ATOM   1517 C  CB   . TYR   A 1 105 ? 26.182  0.627   16.658  1.00 22.23 ? 105 TYR   A CB   1 
ATOM   1518 C  CG   . TYR   A 1 105 ? 27.386  0.286   15.798  1.00 24.64 ? 105 TYR   A CG   1 
ATOM   1519 C  CD1  . TYR   A 1 105 ? 27.660  -1.025  15.409  1.00 23.75 ? 105 TYR   A CD1  1 
ATOM   1520 C  CD2  . TYR   A 1 105 ? 28.241  1.287   15.350  1.00 27.35 ? 105 TYR   A CD2  1 
ATOM   1521 C  CE1  . TYR   A 1 105 ? 28.755  -1.322  14.600  1.00 29.74 ? 105 TYR   A CE1  1 
ATOM   1522 C  CE2  . TYR   A 1 105 ? 29.338  0.996   14.547  1.00 27.14 ? 105 TYR   A CE2  1 
ATOM   1523 C  CZ   . TYR   A 1 105 ? 29.592  -0.309  14.171  1.00 30.37 ? 105 TYR   A CZ   1 
ATOM   1524 O  OH   . TYR   A 1 105 ? 30.677  -0.593  13.369  1.00 31.95 ? 105 TYR   A OH   1 
ATOM   1525 H  H    . TYR   A 1 105 ? 24.001  1.174   17.575  1.00 21.31 ? 105 TYR   A H    1 
ATOM   1526 H  HA   . TYR   A 1 105 ? 25.011  1.525   15.222  1.00 21.04 ? 105 TYR   A HA   1 
ATOM   1527 H  HB2  . TYR   A 1 105 ? 26.373  1.456   17.123  1.00 26.69 ? 105 TYR   A HB2  1 
ATOM   1528 H  HB3  . TYR   A 1 105 ? 26.062  -0.091  17.299  1.00 26.69 ? 105 TYR   A HB3  1 
ATOM   1529 H  HD1  . TYR   A 1 105 ? 27.099  -1.712  15.689  1.00 28.51 ? 105 TYR   A HD1  1 
ATOM   1530 H  HD2  . TYR   A 1 105 ? 28.076  2.169   15.593  1.00 32.83 ? 105 TYR   A HD2  1 
ATOM   1531 H  HE1  . TYR   A 1 105 ? 28.924  -2.202  14.351  1.00 35.71 ? 105 TYR   A HE1  1 
ATOM   1532 H  HE2  . TYR   A 1 105 ? 29.897  1.680   14.258  1.00 32.59 ? 105 TYR   A HE2  1 
ATOM   1533 H  HH   . TYR   A 1 105 ? 31.093  0.114   13.187  1.00 38.36 ? 105 TYR   A HH   1 
ATOM   1534 N  N    . VAL   A 1 106 ? 24.193  -1.533  15.771  1.00 19.48 ? 106 VAL   A N    1 
ATOM   1535 C  CA   . VAL   A 1 106 ? 23.932  -2.817  15.131  1.00 17.68 ? 106 VAL   A CA   1 
ATOM   1536 C  C    . VAL   A 1 106 ? 22.822  -2.679  14.095  1.00 19.39 ? 106 VAL   A C    1 
ATOM   1537 O  O    . VAL   A 1 106 ? 22.945  -3.161  12.963  1.00 20.08 ? 106 VAL   A O    1 
ATOM   1538 C  CB   . VAL   A 1 106 ? 23.590  -3.881  16.190  1.00 21.93 ? 106 VAL   A CB   1 
ATOM   1539 C  CG1  . VAL   A 1 106 ? 23.001  -5.125  15.531  1.00 23.12 ? 106 VAL   A CG1  1 
ATOM   1540 C  CG2  . VAL   A 1 106 ? 24.825  -4.203  17.033  1.00 23.14 ? 106 VAL   A CG2  1 
ATOM   1541 H  H    . VAL   A 1 106 ? 24.079  -1.536  16.623  1.00 23.40 ? 106 VAL   A H    1 
ATOM   1542 H  HA   . VAL   A 1 106 ? 24.735  -3.105  14.669  1.00 21.24 ? 106 VAL   A HA   1 
ATOM   1543 H  HB   . VAL   A 1 106 ? 22.916  -3.518  16.786  1.00 26.34 ? 106 VAL   A HB   1 
ATOM   1544 H  HG11 . VAL   A 1 106 ? 23.061  -5.867  16.153  1.00 27.77 ? 106 VAL   A HG11 1 
ATOM   1545 H  HG12 . VAL   A 1 106 ? 22.072  -4.958  15.307  1.00 27.77 ? 106 VAL   A HG12 1 
ATOM   1546 H  HG13 . VAL   A 1 106 ? 23.507  -5.327  14.729  1.00 27.77 ? 106 VAL   A HG13 1 
ATOM   1547 H  HG21 . VAL   A 1 106 ? 24.598  -4.895  17.674  1.00 27.79 ? 106 VAL   A HG21 1 
ATOM   1548 H  HG22 . VAL   A 1 106 ? 25.534  -4.513  16.448  1.00 27.79 ? 106 VAL   A HG22 1 
ATOM   1549 H  HG23 . VAL   A 1 106 ? 25.108  -3.400  17.498  1.00 27.79 ? 106 VAL   A HG23 1 
ATOM   1550 N  N    . ILE   A 1 107 ? 21.724  -2.025  14.461  1.00 17.86 ? 107 ILE   A N    1 
ATOM   1551 C  CA   . ILE   A 1 107 ? 20.592  -1.961  13.546  1.00 17.28 ? 107 ILE   A CA   1 
ATOM   1552 C  C    . ILE   A 1 107 ? 20.946  -1.130  12.319  1.00 17.96 ? 107 ILE   A C    1 
ATOM   1553 O  O    . ILE   A 1 107 ? 20.626  -1.505  11.179  1.00 20.93 ? 107 ILE   A O    1 
ATOM   1554 C  CB   . ILE   A 1 107 ? 19.361  -1.402  14.280  1.00 15.73 ? 107 ILE   A CB   1 
ATOM   1555 C  CG1  . ILE   A 1 107 ? 18.941  -2.342  15.411  1.00 18.38 ? 107 ILE   A CG1  1 
ATOM   1556 C  CG2  . ILE   A 1 107 ? 18.224  -1.205  13.303  1.00 20.00 ? 107 ILE   A CG2  1 
ATOM   1557 C  CD1  . ILE   A 1 107 ? 18.257  -1.637  16.576  1.00 20.68 ? 107 ILE   A CD1  1 
ATOM   1558 H  H    . ILE   A 1 107 ? 21.611  -1.621  15.212  1.00 21.45 ? 107 ILE   A H    1 
ATOM   1559 H  HA   . ILE   A 1 107 ? 20.379  -2.859  13.247  1.00 20.75 ? 107 ILE   A HA   1 
ATOM   1560 H  HB   . ILE   A 1 107 ? 19.593  -0.541  14.663  1.00 18.90 ? 107 ILE   A HB   1 
ATOM   1561 H  HG12 . ILE   A 1 107 ? 18.319  -2.996  15.056  1.00 22.07 ? 107 ILE   A HG12 1 
ATOM   1562 H  HG13 . ILE   A 1 107 ? 19.726  -2.793  15.759  1.00 22.07 ? 107 ILE   A HG13 1 
ATOM   1563 H  HG21 . ILE   A 1 107 ? 17.396  -1.116  13.800  1.00 24.02 ? 107 ILE   A HG21 1 
ATOM   1564 H  HG22 . ILE   A 1 107 ? 18.385  -0.401  12.784  1.00 24.02 ? 107 ILE   A HG22 1 
ATOM   1565 H  HG23 . ILE   A 1 107 ? 18.175  -1.976  12.717  1.00 24.02 ? 107 ILE   A HG23 1 
ATOM   1566 H  HD11 . ILE   A 1 107 ? 18.067  -2.287  17.270  1.00 24.83 ? 107 ILE   A HD11 1 
ATOM   1567 H  HD12 . ILE   A 1 107 ? 18.849  -0.949  16.919  1.00 24.83 ? 107 ILE   A HD12 1 
ATOM   1568 H  HD13 . ILE   A 1 107 ? 17.432  -1.236  16.261  1.00 24.83 ? 107 ILE   A HD13 1 
ATOM   1569 N  N    . LYS   A 1 108 ? 21.608  0.008   12.529  1.00 19.32 ? 108 LYS   A N    1 
ATOM   1570 C  CA   . LYS   A 1 108 ? 22.033  0.857   11.423  1.00 20.47 ? 108 LYS   A CA   1 
ATOM   1571 C  C    . LYS   A 1 108 ? 22.940  0.088   10.470  1.00 22.20 ? 108 LYS   A C    1 
ATOM   1572 O  O    . LYS   A 1 108 ? 22.760  0.133   9.247   1.00 22.43 ? 108 LYS   A O    1 
ATOM   1573 C  CB   . LYS   A 1 108 ? 22.751  2.080   11.995  1.00 25.54 ? 108 LYS   A CB   1 
ATOM   1574 C  CG   . LYS   A 1 108 ? 23.436  3.021   11.023  1.00 29.20 ? 108 LYS   A CG   1 
ATOM   1575 C  CD   . LYS   A 1 108 ? 22.453  3.928   10.311  1.00 28.78 ? 108 LYS   A CD   1 
ATOM   1576 C  CE   . LYS   A 1 108 ? 23.185  4.775   9.291   1.00 34.43 ? 108 LYS   A CE   1 
ATOM   1577 N  NZ   . LYS   A 1 108 ? 23.566  3.976   8.099   1.00 40.66 ? 108 LYS   A NZ   1 
ATOM   1578 H  H    . LYS   A 1 108 ? 21.823  0.309   13.305  1.00 23.20 ? 108 LYS   A H    1 
ATOM   1579 H  HA   . LYS   A 1 108 ? 21.255  1.160   10.930  1.00 24.58 ? 108 LYS   A HA   1 
ATOM   1580 H  HB2  . LYS   A 1 108 ? 22.100  2.606   12.485  1.00 30.67 ? 108 LYS   A HB2  1 
ATOM   1581 H  HB3  . LYS   A 1 108 ? 23.432  1.765   12.610  1.00 30.67 ? 108 LYS   A HB3  1 
ATOM   1582 H  HG2  . LYS   A 1 108 ? 24.058  3.580   11.513  1.00 35.06 ? 108 LYS   A HG2  1 
ATOM   1583 H  HG3  . LYS   A 1 108 ? 23.913  2.509   10.353  1.00 35.06 ? 108 LYS   A HG3  1 
ATOM   1584 H  HD2  . LYS   A 1 108 ? 21.790  3.391   9.849   1.00 34.56 ? 108 LYS   A HD2  1 
ATOM   1585 H  HD3  . LYS   A 1 108 ? 22.028  4.517   10.954  1.00 34.56 ? 108 LYS   A HD3  1 
ATOM   1586 H  HE2  . LYS   A 1 108 ? 22.608  5.499   9.002   1.00 41.33 ? 108 LYS   A HE2  1 
ATOM   1587 H  HE3  . LYS   A 1 108 ? 23.994  5.129   9.689   1.00 41.33 ? 108 LYS   A HE3  1 
ATOM   1588 H  HZ1  . LYS   A 1 108 ? 23.986  4.493   7.509   1.00 48.81 ? 108 LYS   A HZ1  1 
ATOM   1589 H  HZ2  . LYS   A 1 108 ? 24.107  3.311   8.339   1.00 48.81 ? 108 LYS   A HZ2  1 
ATOM   1590 H  HZ3  . LYS   A 1 108 ? 22.839  3.633   7.718   1.00 48.81 ? 108 LYS   A HZ3  1 
ATOM   1591 N  N    . HIS   A 1 109 ? 23.924  -0.630  11.011  1.00 21.96 ? 109 HIS   A N    1 
ATOM   1592 C  CA   . HIS   A 1 109 ? 24.890  -1.315  10.161  1.00 22.25 ? 109 HIS   A CA   1 
ATOM   1593 C  C    . HIS   A 1 109 ? 24.303  -2.581  9.557   1.00 25.13 ? 109 HIS   A C    1 
ATOM   1594 O  O    . HIS   A 1 109 ? 24.681  -2.941  8.441   1.00 24.64 ? 109 HIS   A O    1 
ATOM   1595 C  CB   . HIS   A 1 109 ? 26.171  -1.538  10.966  1.00 26.42 ? 109 HIS   A CB   1 
ATOM   1596 C  CG   . HIS   A 1 109 ? 26.941  -0.269  11.177  1.00 24.67 ? 109 HIS   A CG   1 
ATOM   1597 N  ND1  . HIS   A 1 109 ? 27.908  0.175   10.302  1.00 29.95 ? 109 HIS   A ND1  1 
ATOM   1598 C  CD2  . HIS   A 1 109 ? 26.795  0.715   12.097  1.00 26.61 ? 109 HIS   A CD2  1 
ATOM   1599 C  CE1  . HIS   A 1 109 ? 28.377  1.340   10.713  1.00 30.73 ? 109 HIS   A CE1  1 
ATOM   1600 N  NE2  . HIS   A 1 109 ? 27.712  1.693   11.798  1.00 28.36 ? 109 HIS   A NE2  1 
ATOM   1601 H  H    . HIS   A 1 109 ? 24.051  -0.734  11.855  1.00 26.38 ? 109 HIS   A H    1 
ATOM   1602 H  HA   . HIS   A 1 109 ? 25.116  -0.726  9.424   1.00 26.72 ? 109 HIS   A HA   1 
ATOM   1603 H  HB2  . HIS   A 1 109 ? 25.940  -1.898  11.836  1.00 31.72 ? 109 HIS   A HB2  1 
ATOM   1604 H  HB3  . HIS   A 1 109 ? 26.741  -2.160  10.488  1.00 31.72 ? 109 HIS   A HB3  1 
ATOM   1605 H  HD1  . HIS   A 1 109 ? 28.165  -0.269  9.646   1.00 35.96 ? 109 HIS   A HD1  1 
ATOM   1606 H  HD2  . HIS   A 1 109 ? 26.207  0.716   12.816  1.00 31.95 ? 109 HIS   A HD2  1 
ATOM   1607 H  HE1  . HIS   A 1 109 ? 29.051  1.832   10.303  1.00 36.90 ? 109 HIS   A HE1  1 
ATOM   1608 N  N    . MET   A 1 110 ? 23.326  -3.215  10.211  1.00 23.15 ? 110 MET   A N    1 
ATOM   1609 C  CA   A MET   A 1 110 ? 22.647  -4.345  9.587   0.41 22.58 ? 110 MET   A CA   1 
ATOM   1610 C  CA   B MET   A 1 110 ? 22.648  -4.346  9.586   0.59 22.54 ? 110 MET   A CA   1 
ATOM   1611 C  C    . MET   A 1 110 ? 21.947  -3.909  8.304   1.00 26.23 ? 110 MET   A C    1 
ATOM   1612 O  O    . MET   A 1 110 ? 22.151  -4.504  7.241   1.00 25.59 ? 110 MET   A O    1 
ATOM   1613 C  CB   A MET   A 1 110 ? 21.672  -4.968  10.587  0.41 21.72 ? 110 MET   A CB   1 
ATOM   1614 C  CB   B MET   A 1 110 ? 21.660  -4.974  10.570  0.59 21.67 ? 110 MET   A CB   1 
ATOM   1615 C  CG   A MET   A 1 110 ? 21.010  -6.254  10.129  0.41 24.11 ? 110 MET   A CG   1 
ATOM   1616 C  CG   B MET   A 1 110 ? 21.002  -6.248  10.063  0.59 24.11 ? 110 MET   A CG   1 
ATOM   1617 S  SD   A MET   A 1 110 ? 19.388  -6.474  10.895  0.41 24.27 ? 110 MET   A SD   1 
ATOM   1618 S  SD   B MET   A 1 110 ? 19.484  -5.943  9.141   0.59 23.55 ? 110 MET   A SD   1 
ATOM   1619 C  CE   A MET   A 1 110 ? 18.478  -5.114  10.167  0.41 25.26 ? 110 MET   A CE   1 
ATOM   1620 C  CE   B MET   A 1 110 ? 18.434  -5.241  10.409  0.59 24.63 ? 110 MET   A CE   1 
ATOM   1621 H  H    A MET   A 1 110 ? 23.045  -3.014  10.999  0.41 27.80 ? 110 MET   A H    1 
ATOM   1622 H  H    B MET   A 1 110 ? 23.045  -3.014  10.998  0.59 27.80 ? 110 MET   A H    1 
ATOM   1623 H  HA   A MET   A 1 110 ? 23.308  -5.019  9.364   0.41 27.11 ? 110 MET   A HA   1 
ATOM   1624 H  HA   B MET   A 1 110 ? 23.309  -5.020  9.363   0.59 27.07 ? 110 MET   A HA   1 
ATOM   1625 H  HB2  A MET   A 1 110 ? 22.157  -5.167  11.403  0.41 26.08 ? 110 MET   A HB2  1 
ATOM   1626 H  HB2  B MET   A 1 110 ? 22.134  -5.193  11.388  0.59 26.02 ? 110 MET   A HB2  1 
ATOM   1627 H  HB3  A MET   A 1 110 ? 20.974  -4.323  10.776  0.41 26.08 ? 110 MET   A HB3  1 
ATOM   1628 H  HB3  B MET   A 1 110 ? 20.961  -4.330  10.761  0.59 26.02 ? 110 MET   A HB3  1 
ATOM   1629 H  HG2  A MET   A 1 110 ? 20.889  -6.231  9.167   0.41 28.95 ? 110 MET   A HG2  1 
ATOM   1630 H  HG2  B MET   A 1 110 ? 21.621  -6.709  9.475   0.59 28.95 ? 110 MET   A HG2  1 
ATOM   1631 H  HG3  A MET   A 1 110 ? 21.568  -7.007  10.378  0.41 28.95 ? 110 MET   A HG3  1 
ATOM   1632 H  HG3  B MET   A 1 110 ? 20.783  -6.812  10.821  0.59 28.95 ? 110 MET   A HG3  1 
ATOM   1633 H  HE1  A MET   A 1 110 ? 17.530  -5.254  10.319  0.41 30.33 ? 110 MET   A HE1  1 
ATOM   1634 H  HE1  B MET   A 1 110 ? 17.520  -5.219  10.084  0.59 29.57 ? 110 MET   A HE1  1 
ATOM   1635 H  HE2  A MET   A 1 110 ? 18.760  -4.284  10.582  0.41 30.33 ? 110 MET   A HE2  1 
ATOM   1636 H  HE2  B MET   A 1 110 ? 18.489  -5.793  11.205  0.59 29.57 ? 110 MET   A HE2  1 
ATOM   1637 H  HE3  A MET   A 1 110 ? 18.658  -5.088  9.214   0.41 30.33 ? 110 MET   A HE3  1 
ATOM   1638 H  HE3  B MET   A 1 110 ? 18.736  -4.341  10.609  0.59 29.57 ? 110 MET   A HE3  1 
ATOM   1639 N  N    . TYR   A 1 111 ? 21.137  -2.842  8.370   1.00 22.60 ? 111 TYR   A N    1 
ATOM   1640 C  CA   . TYR   A 1 111 ? 20.433  -2.375  7.171   1.00 22.79 ? 111 TYR   A CA   1 
ATOM   1641 C  C    . TYR   A 1 111 ? 21.398  -1.841  6.107   1.00 24.92 ? 111 TYR   A C    1 
ATOM   1642 O  O    . TYR   A 1 111 ? 21.134  -1.985  4.906   1.00 25.11 ? 111 TYR   A O    1 
ATOM   1643 C  CB   . TYR   A 1 111 ? 19.414  -1.300  7.562   1.00 23.26 ? 111 TYR   A CB   1 
ATOM   1644 C  CG   . TYR   A 1 111 ? 18.064  -1.841  8.005   1.00 21.20 ? 111 TYR   A CG   1 
ATOM   1645 C  CD1  . TYR   A 1 111 ? 17.178  -2.423  7.108   1.00 23.04 ? 111 TYR   A CD1  1 
ATOM   1646 C  CD2  . TYR   A 1 111 ? 17.695  -1.792  9.344   1.00 20.59 ? 111 TYR   A CD2  1 
ATOM   1647 C  CE1  . TYR   A 1 111 ? 15.954  -2.923  7.531   1.00 22.15 ? 111 TYR   A CE1  1 
ATOM   1648 C  CE2  . TYR   A 1 111 ? 16.473  -2.288  9.777   1.00 19.90 ? 111 TYR   A CE2  1 
ATOM   1649 C  CZ   . TYR   A 1 111 ? 15.608  -2.860  8.864   1.00 17.98 ? 111 TYR   A CZ   1 
ATOM   1650 O  OH   . TYR   A 1 111 ? 14.391  -3.364  9.270   1.00 19.00 ? 111 TYR   A OH   1 
ATOM   1651 H  H    . TYR   A 1 111 ? 20.982  -2.383  9.080   1.00 27.14 ? 111 TYR   A H    1 
ATOM   1652 H  HA   . TYR   A 1 111 ? 19.947  -3.120  6.784   1.00 27.37 ? 111 TYR   A HA   1 
ATOM   1653 H  HB2  . TYR   A 1 111 ? 19.777  -0.780  8.295   1.00 27.93 ? 111 TYR   A HB2  1 
ATOM   1654 H  HB3  . TYR   A 1 111 ? 19.263  -0.724  6.797   1.00 27.93 ? 111 TYR   A HB3  1 
ATOM   1655 H  HD1  . TYR   A 1 111 ? 17.405  -2.472  6.208   1.00 27.67 ? 111 TYR   A HD1  1 
ATOM   1656 H  HD2  . TYR   A 1 111 ? 18.276  -1.410  9.962   1.00 24.73 ? 111 TYR   A HD2  1 
ATOM   1657 H  HE1  . TYR   A 1 111 ? 15.371  -3.307  6.917   1.00 26.60 ? 111 TYR   A HE1  1 
ATOM   1658 H  HE2  . TYR   A 1 111 ? 16.242  -2.244  10.677  1.00 23.90 ? 111 TYR   A HE2  1 
ATOM   1659 H  HH   . TYR   A 1 111 ? 14.302  -3.266  10.099  1.00 22.81 ? 111 TYR   A HH   1 
ATOM   1660 N  N    . HIS   A 1 112 ? 22.515  -1.233  6.512   1.00 21.71 ? 112 HIS   A N    1 
ATOM   1661 C  CA   . HIS   A 1 112 ? 23.461  -0.739  5.517   1.00 24.62 ? 112 HIS   A CA   1 
ATOM   1662 C  C    . HIS   A 1 112 ? 24.230  -1.893  4.885   1.00 27.12 ? 112 HIS   A C    1 
ATOM   1663 O  O    . HIS   A 1 112 ? 24.415  -1.940  3.662   1.00 27.76 ? 112 HIS   A O    1 
ATOM   1664 C  CB   . HIS   A 1 112 ? 24.447  0.239   6.146   1.00 27.43 ? 112 HIS   A CB   1 
ATOM   1665 C  CG   . HIS   A 1 112 ? 25.518  0.689   5.203   1.00 28.47 ? 112 HIS   A CG   1 
ATOM   1666 N  ND1  . HIS   A 1 112 ? 26.795  0.172   5.230   1.00 39.35 ? 112 HIS   A ND1  1 
ATOM   1667 C  CD2  . HIS   A 1 112 ? 25.512  1.627   4.226   1.00 34.05 ? 112 HIS   A CD2  1 
ATOM   1668 C  CE1  . HIS   A 1 112 ? 27.523  0.755   4.295   1.00 39.45 ? 112 HIS   A CE1  1 
ATOM   1669 N  NE2  . HIS   A 1 112 ? 26.772  1.648   3.677   1.00 39.86 ? 112 HIS   A NE2  1 
ATOM   1670 H  H    . HIS   A 1 112 ? 22.741  -1.098  7.331   1.00 26.07 ? 112 HIS   A H    1 
ATOM   1671 H  HA   . HIS   A 1 112 ? 22.977  -0.275  4.816   1.00 29.56 ? 112 HIS   A HA   1 
ATOM   1672 H  HB2  . HIS   A 1 112 ? 23.963  1.025   6.444   1.00 32.94 ? 112 HIS   A HB2  1 
ATOM   1673 H  HB3  . HIS   A 1 112 ? 24.877  -0.191  6.902   1.00 32.94 ? 112 HIS   A HB3  1 
ATOM   1674 H  HD2  . HIS   A 1 112 ? 24.807  2.148   3.976   1.00 40.88 ? 112 HIS   A HD2  1 
ATOM   1675 H  HE1  . HIS   A 1 112 ? 28.416  0.573   4.116   1.00 47.36 ? 112 HIS   A HE1  1 
ATOM   1676 H  HE2  . HIS   A 1 112 ? 27.028  2.155   3.031   1.00 47.86 ? 112 HIS   A HE2  1 
ATOM   1677 N  N    . ASP   A 1 113 ? 24.723  -2.811  5.712   1.00 26.65 ? 113 ASP   A N    1 
ATOM   1678 C  CA   . ASP   A 1 113 ? 25.564  -3.902  5.226   1.00 29.76 ? 113 ASP   A CA   1 
ATOM   1679 C  C    . ASP   A 1 113 ? 24.772  -4.889  4.384   1.00 27.61 ? 113 ASP   A C    1 
ATOM   1680 O  O    . ASP   A 1 113 ? 25.253  -5.344  3.340   1.00 30.07 ? 113 ASP   A O    1 
ATOM   1681 C  CB   . ASP   A 1 113 ? 26.204  -4.587  6.432   1.00 29.70 ? 113 ASP   A CB   1 
ATOM   1682 C  CG   . ASP   A 1 113 ? 27.374  -3.808  7.008   1.00 32.03 ? 113 ASP   A CG   1 
ATOM   1683 O  OD1  . ASP   A 1 113 ? 27.575  -2.630  6.638   1.00 30.67 ? 113 ASP   A OD1  1 
ATOM   1684 O  OD2  . ASP   A 1 113 ? 27.983  -4.320  7.974   1.00 29.28 ? 113 ASP   A OD2  1 
ATOM   1685 H  H    . ASP   A 1 113 ? 24.585  -2.825  6.561   1.00 32.00 ? 113 ASP   A H    1 
ATOM   1686 H  HA   . ASP   A 1 113 ? 26.273  -3.536  4.674   1.00 35.73 ? 113 ASP   A HA   1 
ATOM   1687 H  HB2  . ASP   A 1 113 ? 25.538  -4.695  7.128   1.00 35.66 ? 113 ASP   A HB2  1 
ATOM   1688 H  HB3  . ASP   A 1 113 ? 26.535  -5.457  6.157   1.00 35.66 ? 113 ASP   A HB3  1 
ATOM   1689 N  N    . TRP   A 1 114 ? 23.547  -5.219  4.808   1.00 26.79 ? 114 TRP   A N    1 
ATOM   1690 C  CA   . TRP   A 1 114 ? 22.766  -6.243  4.117   1.00 28.96 ? 114 TRP   A CA   1 
ATOM   1691 C  C    . TRP   A 1 114 ? 21.978  -5.710  2.927   1.00 34.10 ? 114 TRP   A C    1 
ATOM   1692 O  O    . TRP   A 1 114 ? 21.731  -6.465  1.978   1.00 31.53 ? 114 TRP   A O    1 
ATOM   1693 C  CB   . TRP   A 1 114 ? 21.811  -6.926  5.100   1.00 28.36 ? 114 TRP   A CB   1 
ATOM   1694 C  CG   . TRP   A 1 114 ? 22.478  -7.847  6.068   1.00 31.54 ? 114 TRP   A CG   1 
ATOM   1695 C  CD1  . TRP   A 1 114 ? 23.819  -8.033  6.240   1.00 33.46 ? 114 TRP   A CD1  1 
ATOM   1696 C  CD2  . TRP   A 1 114 ? 21.829  -8.717  7.000   1.00 32.96 ? 114 TRP   A CD2  1 
ATOM   1697 N  NE1  . TRP   A 1 114 ? 24.043  -8.972  7.215   1.00 36.79 ? 114 TRP   A NE1  1 
ATOM   1698 C  CE2  . TRP   A 1 114 ? 22.837  -9.404  7.702   1.00 30.72 ? 114 TRP   A CE2  1 
ATOM   1699 C  CE3  . TRP   A 1 114 ? 20.491  -8.980  7.308   1.00 32.35 ? 114 TRP   A CE3  1 
ATOM   1700 C  CZ2  . TRP   A 1 114 ? 22.550  -10.339 8.695   1.00 38.44 ? 114 TRP   A CZ2  1 
ATOM   1701 C  CZ3  . TRP   A 1 114 ? 20.208  -9.906  8.293   1.00 32.97 ? 114 TRP   A CZ3  1 
ATOM   1702 C  CH2  . TRP   A 1 114 ? 21.230  -10.574 8.974   1.00 30.58 ? 114 TRP   A CH2  1 
ATOM   1703 H  H    . TRP   A 1 114 ? 23.152  -4.867  5.486   1.00 32.17 ? 114 TRP   A H    1 
ATOM   1704 H  HA   . TRP   A 1 114 ? 23.374  -6.919  3.779   1.00 34.77 ? 114 TRP   A HA   1 
ATOM   1705 H  HB2  . TRP   A 1 114 ? 21.351  -6.243  5.612   1.00 34.06 ? 114 TRP   A HB2  1 
ATOM   1706 H  HB3  . TRP   A 1 114 ? 21.166  -7.446  4.595   1.00 34.06 ? 114 TRP   A HB3  1 
ATOM   1707 H  HD1  . TRP   A 1 114 ? 24.484  -7.597  5.757   1.00 40.17 ? 114 TRP   A HD1  1 
ATOM   1708 H  HE1  . TRP   A 1 114 ? 24.815  -9.239  7.484   1.00 44.16 ? 114 TRP   A HE1  1 
ATOM   1709 H  HE3  . TRP   A 1 114 ? 19.805  -8.541  6.858   1.00 38.84 ? 114 TRP   A HE3  1 
ATOM   1710 H  HZ2  . TRP   A 1 114 ? 23.228  -10.783 9.151   1.00 46.15 ? 114 TRP   A HZ2  1 
ATOM   1711 H  HZ3  . TRP   A 1 114 ? 19.322  -10.090 8.506   1.00 39.58 ? 114 TRP   A HZ3  1 
ATOM   1712 H  HH2  . TRP   A 1 114 ? 21.008  -11.192 9.633   1.00 36.71 ? 114 TRP   A HH2  1 
ATOM   1713 N  N    . TYR   A 1 115 ? 21.566  -4.435  2.943   1.00 31.73 ? 115 TYR   A N    1 
ATOM   1714 C  CA   . TYR   A 1 115 ? 20.650  -3.930  1.924   1.00 28.90 ? 115 TYR   A CA   1 
ATOM   1715 C  C    . TYR   A 1 115 ? 21.110  -2.622  1.298   1.00 33.65 ? 115 TYR   A C    1 
ATOM   1716 O  O    . TYR   A 1 115 ? 20.448  -2.136  0.375   1.00 35.92 ? 115 TYR   A O    1 
ATOM   1717 C  CB   . TYR   A 1 115 ? 19.223  -3.780  2.514   1.00 29.71 ? 115 TYR   A CB   1 
ATOM   1718 C  CG   . TYR   A 1 115 ? 18.836  -5.101  3.140   1.00 26.40 ? 115 TYR   A CG   1 
ATOM   1719 C  CD1  . TYR   A 1 115 ? 18.583  -6.194  2.335   1.00 31.06 ? 115 TYR   A CD1  1 
ATOM   1720 C  CD2  . TYR   A 1 115 ? 18.793  -5.270  4.514   1.00 25.82 ? 115 TYR   A CD2  1 
ATOM   1721 C  CE1  . TYR   A 1 115 ? 18.308  -7.412  2.861   1.00 27.05 ? 115 TYR   A CE1  1 
ATOM   1722 C  CE2  . TYR   A 1 115 ? 18.504  -6.501  5.065   1.00 24.04 ? 115 TYR   A CE2  1 
ATOM   1723 C  CZ   . TYR   A 1 115 ? 18.258  -7.570  4.220   1.00 26.94 ? 115 TYR   A CZ   1 
ATOM   1724 O  OH   . TYR   A 1 115 ? 17.956  -8.821  4.699   1.00 25.54 ? 115 TYR   A OH   1 
ATOM   1725 H  H    . TYR   A 1 115 ? 21.802  -3.851  3.529   1.00 38.09 ? 115 TYR   A H    1 
ATOM   1726 H  HA   . TYR   A 1 115 ? 20.596  -4.580  1.207   1.00 34.70 ? 115 TYR   A HA   1 
ATOM   1727 H  HB2  . TYR   A 1 115 ? 19.218  -3.093  3.199   1.00 35.67 ? 115 TYR   A HB2  1 
ATOM   1728 H  HB3  . TYR   A 1 115 ? 18.593  -3.570  1.807   1.00 35.67 ? 115 TYR   A HB3  1 
ATOM   1729 H  HD1  . TYR   A 1 115 ? 18.632  -6.099  1.411   1.00 37.29 ? 115 TYR   A HD1  1 
ATOM   1730 H  HD2  . TYR   A 1 115 ? 18.976  -4.548  5.072   1.00 31.00 ? 115 TYR   A HD2  1 
ATOM   1731 H  HE1  . TYR   A 1 115 ? 18.133  -8.133  2.301   1.00 32.48 ? 115 TYR   A HE1  1 
ATOM   1732 H  HE2  . TYR   A 1 115 ? 18.469  -6.610  5.988   1.00 28.87 ? 115 TYR   A HE2  1 
ATOM   1733 H  HH   . TYR   A 1 115 ? 17.860  -9.358  4.060   1.00 30.66 ? 115 TYR   A HH   1 
ATOM   1734 N  N    . GLY   A 1 116 ? 22.232  -2.064  1.738   1.00 27.32 ? 116 GLY   A N    1 
ATOM   1735 C  CA   . GLY   A 1 116 ? 22.669  -0.786  1.215   1.00 29.28 ? 116 GLY   A CA   1 
ATOM   1736 C  C    . GLY   A 1 116 ? 21.647  0.310   1.373   1.00 37.44 ? 116 GLY   A C    1 
ATOM   1737 O  O    . GLY   A 1 116 ? 21.546  1.165   0.501   1.00 39.36 ? 116 GLY   A O    1 
ATOM   1738 H  H    . GLY   A 1 116 ? 22.752  -2.404  2.333   1.00 32.80 ? 116 GLY   A H    1 
ATOM   1739 H  HA2  . GLY   A 1 116 ? 23.479  -0.514  1.673   1.00 35.15 ? 116 GLY   A HA2  1 
ATOM   1740 H  HA3  . GLY   A 1 116 ? 22.870  -0.879  0.271   1.00 35.15 ? 116 GLY   A HA3  1 
ATOM   1741 N  N    . VAL   A 1 117 ? 20.889  0.311   2.469   1.00 31.39 ? 117 VAL   A N    1 
ATOM   1742 C  CA   . VAL   A 1 117 ? 19.851  1.304   2.710   1.00 40.25 ? 117 VAL   A CA   1 
ATOM   1743 C  C    . VAL   A 1 117 ? 19.992  1.882   4.111   1.00 32.61 ? 117 VAL   A C    1 
ATOM   1744 O  O    . VAL   A 1 117 ? 20.549  1.253   5.017   1.00 31.12 ? 117 VAL   A O    1 
ATOM   1745 C  CB   . VAL   A 1 117 ? 18.424  0.725   2.520   1.00 38.39 ? 117 VAL   A CB   1 
ATOM   1746 C  CG1  . VAL   A 1 117 ? 18.310  -0.004  1.189   1.00 41.79 ? 117 VAL   A CG1  1 
ATOM   1747 C  CG2  . VAL   A 1 117 ? 18.064  -0.215  3.669   1.00 35.70 ? 117 VAL   A CG2  1 
ATOM   1748 H  H    . VAL   A 1 117 ? 20.961  -0.268  3.100   1.00 37.68 ? 117 VAL   A H    1 
ATOM   1749 H  HA   . VAL   A 1 117 ? 19.960  2.033   2.080   1.00 48.32 ? 117 VAL   A HA   1 
ATOM   1750 H  HB   . VAL   A 1 117 ? 17.785  1.455   2.518   1.00 46.09 ? 117 VAL   A HB   1 
ATOM   1751 H  HG11 . VAL   A 1 117 ? 17.378  -0.030  0.923   1.00 50.17 ? 117 VAL   A HG11 1 
ATOM   1752 H  HG12 . VAL   A 1 117 ? 18.832  0.471   0.523   1.00 50.17 ? 117 VAL   A HG12 1 
ATOM   1753 H  HG13 . VAL   A 1 117 ? 18.650  -0.905  1.296   1.00 50.17 ? 117 VAL   A HG13 1 
ATOM   1754 H  HG21 . VAL   A 1 117 ? 17.311  -0.765  3.402   1.00 42.85 ? 117 VAL   A HG21 1 
ATOM   1755 H  HG22 . VAL   A 1 117 ? 18.829  -0.777  3.868   1.00 42.85 ? 117 VAL   A HG22 1 
ATOM   1756 H  HG23 . VAL   A 1 117 ? 17.829  0.311   4.449   1.00 42.85 ? 117 VAL   A HG23 1 
ATOM   1757 N  N    . GLU   A 1 118 ? 19.487  3.106   4.277   1.00 30.27 ? 118 GLU   A N    1 
ATOM   1758 C  CA   . GLU   A 1 118 ? 19.349  3.691   5.600   1.00 29.52 ? 118 GLU   A CA   1 
ATOM   1759 C  C    . GLU   A 1 118 ? 18.274  2.935   6.367   1.00 26.71 ? 118 GLU   A C    1 
ATOM   1760 O  O    . GLU   A 1 118 ? 17.262  2.515   5.799   1.00 30.62 ? 118 GLU   A O    1 
ATOM   1761 C  CB   . GLU   A 1 118 ? 18.987  5.175   5.501   1.00 30.64 ? 118 GLU   A CB   1 
ATOM   1762 C  CG   . GLU   A 1 118 ? 20.111  6.091   5.006   1.00 42.89 ? 118 GLU   A CG   1 
ATOM   1763 C  CD   . GLU   A 1 118 ? 21.304  6.165   5.949   1.00 44.28 ? 118 GLU   A CD   1 
ATOM   1764 O  OE1  . GLU   A 1 118 ? 21.114  6.203   7.181   1.00 38.41 ? 118 GLU   A OE1  1 
ATOM   1765 O  OE2  . GLU   A 1 118 ? 22.446  6.216   5.452   1.00 39.42 ? 118 GLU   A OE2  1 
ATOM   1766 H  H    . GLU   A 1 118 ? 19.219  3.614   3.637   1.00 36.35 ? 118 GLU   A H    1 
ATOM   1767 H  HA   . GLU   A 1 118 ? 20.187  3.608   6.081   1.00 35.44 ? 118 GLU   A HA   1 
ATOM   1768 H  HB2  . GLU   A 1 118 ? 18.242  5.270   4.887   1.00 36.78 ? 118 GLU   A HB2  1 
ATOM   1769 H  HB3  . GLU   A 1 118 ? 18.724  5.486   6.381   1.00 36.78 ? 118 GLU   A HB3  1 
ATOM   1770 H  HG2  . GLU   A 1 118 ? 20.428  5.764   4.150   1.00 51.48 ? 118 GLU   A HG2  1 
ATOM   1771 H  HG3  . GLU   A 1 118 ? 19.756  6.987   4.905   1.00 51.48 ? 118 GLU   A HG3  1 
ATOM   1772 N  N    . ALA   A 1 119 ? 18.508  2.719   7.658   1.00 24.91 ? 119 ALA   A N    1 
ATOM   1773 C  CA   . ALA   A 1 119 ? 17.443  2.179   8.491   1.00 24.07 ? 119 ALA   A CA   1 
ATOM   1774 C  C    . ALA   A 1 119 ? 16.257  3.131   8.510   1.00 24.40 ? 119 ALA   A C    1 
ATOM   1775 O  O    . ALA   A 1 119 ? 15.097  2.693   8.439   1.00 24.57 ? 119 ALA   A O    1 
ATOM   1776 C  CB   . ALA   A 1 119 ? 17.969  1.929   9.901   1.00 21.48 ? 119 ALA   A CB   1 
ATOM   1777 H  H    . ALA   A 1 119 ? 19.251  2.871   8.064   1.00 29.91 ? 119 ALA   A H    1 
ATOM   1778 H  HA   . ALA   A 1 119 ? 17.147  1.332   8.123   1.00 28.90 ? 119 ALA   A HA   1 
ATOM   1779 H  HB1  . ALA   A 1 119 ? 17.251  1.570   10.446  1.00 25.80 ? 119 ALA   A HB1  1 
ATOM   1780 H  HB2  . ALA   A 1 119 ? 18.701  1.294   9.857   1.00 25.80 ? 119 ALA   A HB2  1 
ATOM   1781 H  HB3  . ALA   A 1 119 ? 18.281  2.768   10.275  1.00 25.80 ? 119 ALA   A HB3  1 
ATOM   1782 N  N    . LEU   A 1 120 ? 16.533  4.438   8.577   1.00 21.96 ? 120 LEU   A N    1 
ATOM   1783 C  CA   . LEU   A 1 120 ? 15.529  5.485   8.667   1.00 23.08 ? 120 LEU   A CA   1 
ATOM   1784 C  C    . LEU   A 1 120 ? 15.914  6.650   7.766   1.00 30.04 ? 120 LEU   A C    1 
ATOM   1785 O  O    . LEU   A 1 120 ? 17.102  6.958   7.630   1.00 28.80 ? 120 LEU   A O    1 
ATOM   1786 C  CB   . LEU   A 1 120 ? 15.391  5.999   10.106  1.00 21.33 ? 120 LEU   A CB   1 
ATOM   1787 C  CG   . LEU   A 1 120 ? 14.943  5.017   11.188  1.00 20.32 ? 120 LEU   A CG   1 
ATOM   1788 C  CD1  . LEU   A 1 120 ? 15.055  5.683   12.555  1.00 22.00 ? 120 LEU   A CD1  1 
ATOM   1789 C  CD2  . LEU   A 1 120 ? 13.541  4.523   10.882  1.00 24.29 ? 120 LEU   A CD2  1 
ATOM   1790 H  H    . LEU   A 1 120 ? 17.335  4.748   8.571   1.00 26.37 ? 120 LEU   A H    1 
ATOM   1791 H  HA   . LEU   A 1 120 ? 14.670  5.140   8.376   1.00 27.71 ? 120 LEU   A HA   1 
ATOM   1792 H  HB2  . LEU   A 1 120 ? 16.254  6.348   10.379  1.00 25.61 ? 120 LEU   A HB2  1 
ATOM   1793 H  HB3  . LEU   A 1 120 ? 14.745  6.722   10.099  1.00 25.61 ? 120 LEU   A HB3  1 
ATOM   1794 H  HG   . LEU   A 1 120 ? 15.537  4.250   11.181  1.00 24.40 ? 120 LEU   A HG   1 
ATOM   1795 H  HD11 . LEU   A 1 120 ? 15.060  4.996   13.240  1.00 26.42 ? 120 LEU   A HD11 1 
ATOM   1796 H  HD12 . LEU   A 1 120 ? 15.879  6.193   12.593  1.00 26.42 ? 120 LEU   A HD12 1 
ATOM   1797 H  HD13 . LEU   A 1 120 ? 14.295  6.271   12.683  1.00 26.42 ? 120 LEU   A HD13 1 
ATOM   1798 H  HD21 . LEU   A 1 120 ? 13.241  3.956   11.610  1.00 29.16 ? 120 LEU   A HD21 1 
ATOM   1799 H  HD22 . LEU   A 1 120 ? 12.950  5.287   10.792  1.00 29.16 ? 120 LEU   A HD22 1 
ATOM   1800 H  HD23 . LEU   A 1 120 ? 13.557  4.018   10.054  1.00 29.16 ? 120 LEU   A HD23 1 
ATOM   1801 N  N    . THR   A 1 121 ? 14.903  7.306   7.179   1.00 29.26 ? 121 THR   A N    1 
ATOM   1802 C  CA   . THR   A 1 121 ? 15.096  8.499   6.362   1.00 36.43 ? 121 THR   A CA   1 
ATOM   1803 C  C    . THR   A 1 121 ? 14.005  9.533   6.635   1.00 34.37 ? 121 THR   A C    1 
ATOM   1804 O  O    . THR   A 1 121 ? 12.916  9.215   7.119   1.00 33.87 ? 121 THR   A O    1 
ATOM   1805 C  CB   . THR   A 1 121 ? 15.091  8.185   4.847   1.00 41.22 ? 121 THR   A CB   1 
ATOM   1806 O  OG1  . THR   A 1 121 ? 13.744  7.868   4.447   1.00 39.99 ? 121 THR   A OG1  1 
ATOM   1807 C  CG2  . THR   A 1 121 ? 16.041  7.062   4.480   1.00 37.13 ? 121 THR   A CG2  1 
ATOM   1808 H  H    . THR   A 1 121 ? 14.079  7.068   7.245   1.00 35.13 ? 121 THR   A H    1 
ATOM   1809 H  HA   . THR   A 1 121 ? 15.951  8.899   6.583   1.00 43.74 ? 121 THR   A HA   1 
ATOM   1810 H  HB   . THR   A 1 121 ? 15.377  8.978   4.367   1.00 49.48 ? 121 THR   A HB   1 
ATOM   1811 H  HG1  . THR   A 1 121 ? 13.722  7.694   3.625   1.00 48.00 ? 121 THR   A HG1  1 
ATOM   1812 H  HG21 . THR   A 1 121 ? 15.897  6.796   3.558   1.00 44.58 ? 121 THR   A HG21 1 
ATOM   1813 H  HG22 . THR   A 1 121 ? 16.958  7.360   4.581   1.00 44.58 ? 121 THR   A HG22 1 
ATOM   1814 H  HG23 . THR   A 1 121 ? 15.896  6.295   5.055   1.00 44.58 ? 121 THR   A HG23 1 
ATOM   1815 N  N    . LYS   A 1 122 ? 14.286  10.793  6.287   1.00 32.65 ? 122 LYS   A N    1 
ATOM   1816 C  CA   . LYS   A 1 122 ? 13.320  11.898  6.506   1.00 42.08 ? 122 LYS   A CA   1 
ATOM   1817 C  C    . LYS   A 1 122 ? 12.274  11.856  5.385   1.00 46.03 ? 122 LYS   A C    1 
ATOM   1818 O  O    . LYS   A 1 122 ? 12.379  10.965  4.527   1.00 45.41 ? 122 LYS   A O    1 
ATOM   1819 C  CB   . LYS   A 1 122 ? 14.069  13.234  6.545   1.00 42.36 ? 122 LYS   A CB   1 
ATOM   1820 C  CG   . LYS   A 1 122 ? 15.212  13.290  7.545   1.00 47.42 ? 122 LYS   A CG   1 
ATOM   1821 C  CD   . LYS   A 1 122 ? 15.673  14.704  7.873   1.00 49.82 ? 122 LYS   A CD   1 
ATOM   1822 C  CE   . LYS   A 1 122 ? 16.982  14.727  8.593   1.00 52.02 ? 122 LYS   A CE   1 
ATOM   1823 N  NZ   . LYS   A 1 122 ? 18.105  14.452  7.694   1.00 52.33 ? 122 LYS   A NZ   1 
ATOM   1824 H  H    . LYS   A 1 122 ? 15.024  11.042  5.923   1.00 39.20 ? 122 LYS   A H    1 
ATOM   1825 H  HA   . LYS   A 1 122 ? 12.868  11.772  7.355   1.00 50.51 ? 122 LYS   A HA   1 
ATOM   1826 H  HB2  . LYS   A 1 122 ? 14.439  13.407  5.665   1.00 50.84 ? 122 LYS   A HB2  1 
ATOM   1827 H  HB3  . LYS   A 1 122 ? 13.440  13.935  6.778   1.00 50.84 ? 122 LYS   A HB3  1 
ATOM   1828 H  HG2  . LYS   A 1 122 ? 14.924  12.873  8.372   1.00 56.92 ? 122 LYS   A HG2  1 
ATOM   1829 H  HG3  . LYS   A 1 122 ? 15.970  12.808  7.180   1.00 56.92 ? 122 LYS   A HG3  1 
ATOM   1830 H  HD2  . LYS   A 1 122 ? 15.775  15.203  7.048   1.00 59.80 ? 122 LYS   A HD2  1 
ATOM   1831 H  HD3  . LYS   A 1 122 ? 15.011  15.130  8.440   1.00 59.80 ? 122 LYS   A HD3  1 
ATOM   1832 H  HE2  . LYS   A 1 122 ? 17.115  15.605  8.984   1.00 62.44 ? 122 LYS   A HE2  1 
ATOM   1833 H  HE3  . LYS   A 1 122 ? 16.976  14.049  9.287   1.00 62.44 ? 122 LYS   A HE3  1 
ATOM   1834 H  HZ1  . LYS   A 1 122 ? 18.010  13.647  7.326   1.00 62.81 ? 122 LYS   A HZ1  1 
ATOM   1835 H  HZ2  . LYS   A 1 122 ? 18.134  15.064  7.048   1.00 62.81 ? 122 LYS   A HZ2  1 
ATOM   1836 H  HZ3  . LYS   A 1 122 ? 18.870  14.474  8.148   1.00 62.81 ? 122 LYS   A HZ3  1 
ATOM   1837 N  N    . SER   A 1 123 ? 11.307  12.774  5.397   1.00 51.87 ? 123 SER   A N    1 
ATOM   1838 C  CA   . SER   A 1 123 ? 10.227  12.808  4.377   1.00 51.65 ? 123 SER   A CA   1 
ATOM   1839 C  C    . SER   A 1 123 ? 10.818  13.103  2.993   1.00 50.92 ? 123 SER   A C    1 
ATOM   1840 O  O    . SER   A 1 123 ? 10.158  12.742  1.997   1.00 53.69 ? 123 SER   A O    1 
ATOM   1841 C  CB   . SER   A 1 123 ? 9.179   13.820  4.743   1.00 56.74 ? 123 SER   A CB   1 
ATOM   1842 O  OG   . SER   A 1 123 ? 8.605   13.521  6.008   1.00 69.32 ? 123 SER   A OG   1 
ATOM   1843 H  H    . SER   A 1 123 ? 11.244  13.398  5.986   1.00 62.27 ? 123 SER   A H    1 
ATOM   1844 H  HA   . SER   A 1 123 ? 9.801   11.937  4.340   1.00 62.00 ? 123 SER   A HA   1 
ATOM   1845 H  HB2  . SER   A 1 123 ? 9.589   14.698  4.782   1.00 68.10 ? 123 SER   A HB2  1 
ATOM   1846 H  HB3  . SER   A 1 123 ? 8.481   13.809  4.069   1.00 68.10 ? 123 SER   A HB3  1 
ATOM   1847 H  HG   . SER   A 1 123 ? 8.021   14.093  6.201   1.00 83.21 ? 123 SER   A HG   1 
ATOM   1848 N  N    . ASP   A 1 124 ? 12.008  13.710  2.930   1.00 49.28 ? 124 ASP   A N    1 
ATOM   1849 C  CA   . ASP   A 1 124 ? 12.630  14.111  1.636   1.00 47.78 ? 124 ASP   A CA   1 
ATOM   1850 C  C    . ASP   A 1 124 ? 13.733  13.127  1.229   1.00 45.92 ? 124 ASP   A C    1 
ATOM   1851 O  O    . ASP   A 1 124 ? 14.443  13.444  0.252   1.00 51.72 ? 124 ASP   A O    1 
ATOM   1852 C  CB   . ASP   A 1 124 ? 13.135  15.545  1.692   1.00 50.69 ? 124 ASP   A CB   1 
ATOM   1853 C  CG   . ASP   A 1 124 ? 14.177  15.837  2.759   1.00 60.32 ? 124 ASP   A CG   1 
ATOM   1854 O  OD1  . ASP   A 1 124 ? 14.488  14.916  3.533   1.00 52.03 ? 124 ASP   A OD1  1 
ATOM   1855 O  OD2  . ASP   A 1 124 ? 14.670  16.983  2.803   1.00 74.02 ? 124 ASP   A OD2  1 
ATOM   1856 H  H    . ASP   A 1 124 ? 12.486  13.907  3.617   1.00 59.15 ? 124 ASP   A H    1 
ATOM   1857 H  HA   . ASP   A 1 124 ? 11.948  14.076  0.948   1.00 57.35 ? 124 ASP   A HA   1 
ATOM   1858 H  HB2  . ASP   A 1 124 ? 13.530  15.764  0.834   1.00 60.84 ? 124 ASP   A HB2  1 
ATOM   1859 H  HB3  . ASP   A 1 124 ? 12.379  16.129  1.858   1.00 60.84 ? 124 ASP   A HB3  1 
ATOM   1860 N  N    . GLY   A 1 125 ? 13.894  11.993  1.920   1.00 53.29 ? 125 GLY   A N    1 
ATOM   1861 C  CA   . GLY   A 1 125 ? 14.853  10.984  1.532   1.00 47.38 ? 125 GLY   A CA   1 
ATOM   1862 C  C    . GLY   A 1 125 ? 16.222  11.110  2.164   1.00 49.91 ? 125 GLY   A C    1 
ATOM   1863 O  O    . GLY   A 1 125 ? 17.043  10.197  2.003   1.00 40.55 ? 125 GLY   A O    1 
ATOM   1864 H  H    . GLY   A 1 125 ? 13.448  11.791  2.627   1.00 63.96 ? 125 GLY   A H    1 
ATOM   1865 H  HA2  . GLY   A 1 125 ? 14.499  10.111  1.763   1.00 56.87 ? 125 GLY   A HA2  1 
ATOM   1866 H  HA3  . GLY   A 1 125 ? 14.967  11.014  0.569   1.00 56.87 ? 125 GLY   A HA3  1 
ATOM   1867 N  N    . SER   A 1 126 ? 16.497  12.200  2.873   1.00 46.05 ? 126 SER   A N    1 
ATOM   1868 C  CA   . SER   A 1 126 ? 17.787  12.353  3.533   1.00 43.17 ? 126 SER   A CA   1 
ATOM   1869 C  C    . SER   A 1 126 ? 17.906  11.374  4.700   1.00 45.84 ? 126 SER   A C    1 
ATOM   1870 O  O    . SER   A 1 126 ? 16.905  11.067  5.357   1.00 36.10 ? 126 SER   A O    1 
ATOM   1871 C  CB   . SER   A 1 126 ? 17.977  13.796  4.013   1.00 43.92 ? 126 SER   A CB   1 
ATOM   1872 O  OG   . SER   A 1 126 ? 17.118  14.137  5.092   1.00 52.25 ? 126 SER   A OG   1 
ATOM   1873 H  H    . SER   A 1 126 ? 15.958  12.861  2.987   1.00 55.28 ? 126 SER   A H    1 
ATOM   1874 H  HA   . SER   A 1 126 ? 18.480  12.165  2.884   1.00 51.82 ? 126 SER   A HA   1 
ATOM   1875 H  HB2  . SER   A 1 126 ? 18.896  13.912  4.296   1.00 52.73 ? 126 SER   A HB2  1 
ATOM   1876 H  HB3  . SER   A 1 126 ? 17.790  14.393  3.272   1.00 52.73 ? 126 SER   A HB3  1 
ATOM   1877 H  HG   . SER   A 1 126 ? 16.316  14.069  4.853   1.00 62.72 ? 126 SER   A HG   1 
ATOM   1878 N  N    . PRO   A 1 127 ? 19.103  10.836  4.950   1.00 37.51 ? 127 PRO   A N    1 
ATOM   1879 C  CA   . PRO   A 1 127 ? 19.273  9.899   6.070   1.00 35.66 ? 127 PRO   A CA   1 
ATOM   1880 C  C    . PRO   A 1 127 ? 18.805  10.507  7.380   1.00 31.73 ? 127 PRO   A C    1 
ATOM   1881 O  O    . PRO   A 1 127 ? 18.960  11.705  7.625   1.00 35.76 ? 127 PRO   A O    1 
ATOM   1882 C  CB   . PRO   A 1 127 ? 20.785  9.649   6.075   1.00 43.30 ? 127 PRO   A CB   1 
ATOM   1883 C  CG   . PRO   A 1 127 ? 21.095  9.630   4.591   1.00 37.35 ? 127 PRO   A CG   1 
ATOM   1884 C  CD   . PRO   A 1 127 ? 20.297  10.838  4.074   1.00 44.98 ? 127 PRO   A CD   1 
ATOM   1885 H  HA   . PRO   A 1 127 ? 18.801  9.068   5.902   1.00 42.81 ? 127 PRO   A HA   1 
ATOM   1886 H  HB2  . PRO   A 1 127 ? 21.244  10.377  6.522   1.00 51.98 ? 127 PRO   A HB2  1 
ATOM   1887 H  HB3  . PRO   A 1 127 ? 20.984  8.796   6.491   1.00 51.98 ? 127 PRO   A HB3  1 
ATOM   1888 H  HG2  . PRO   A 1 127 ? 22.046  9.758   4.450   1.00 44.84 ? 127 PRO   A HG2  1 
ATOM   1889 H  HG3  . PRO   A 1 127 ? 20.784  8.805   4.189   1.00 44.84 ? 127 PRO   A HG3  1 
ATOM   1890 H  HD2  . PRO   A 1 127 ? 20.804  11.656  4.190   1.00 53.99 ? 127 PRO   A HD2  1 
ATOM   1891 H  HD3  . PRO   A 1 127 ? 20.046  10.699  3.148   1.00 53.99 ? 127 PRO   A HD3  1 
ATOM   1892 N  N    . MET   A 1 128 ? 18.230  9.661   8.234   1.00 29.77 ? 128 MET   A N    1 
ATOM   1893 C  CA   A MET   A 1 128 ? 17.707  10.076  9.526   0.76 30.13 ? 128 MET   A CA   1 
ATOM   1894 C  CA   B MET   A 1 128 ? 17.709  10.080  9.529   0.24 30.33 ? 128 MET   A CA   1 
ATOM   1895 C  C    . MET   A 1 128 ? 18.519  9.391   10.615  1.00 26.87 ? 128 MET   A C    1 
ATOM   1896 O  O    . MET   A 1 128 ? 18.632  8.160   10.627  1.00 27.16 ? 128 MET   A O    1 
ATOM   1897 C  CB   A MET   A 1 128 ? 16.222  9.726   9.624   0.76 30.62 ? 128 MET   A CB   1 
ATOM   1898 C  CB   B MET   A 1 128 ? 16.220  9.751   9.678   0.24 30.80 ? 128 MET   A CB   1 
ATOM   1899 C  CG   A MET   A 1 128 ? 15.473  10.392  10.752  0.76 33.34 ? 128 MET   A CG   1 
ATOM   1900 C  CG   B MET   A 1 128 ? 15.493  10.600  10.731  0.24 33.81 ? 128 MET   A CG   1 
ATOM   1901 S  SD   A MET   A 1 128 ? 13.701  10.158  10.546  0.76 43.43 ? 128 MET   A SD   1 
ATOM   1902 S  SD   B MET   A 1 128 ? 14.061  9.785   11.455  0.24 32.43 ? 128 MET   A SD   1 
ATOM   1903 C  CE   A MET   A 1 128 ? 13.457  8.772   11.651  0.76 33.50 ? 128 MET   A CE   1 
ATOM   1904 C  CE   B MET   A 1 128 ? 13.070  9.555   9.984   0.24 36.16 ? 128 MET   A CE   1 
ATOM   1905 H  H    A MET   A 1 128 ? 18.131  8.821   8.079   0.76 35.75 ? 128 MET   A H    1 
ATOM   1906 H  H    B MET   A 1 128 ? 18.129  8.821   8.080   0.24 35.75 ? 128 MET   A H    1 
ATOM   1907 H  HA   A MET   A 1 128 ? 17.797  11.037  9.618   0.76 36.17 ? 128 MET   A HA   1 
ATOM   1908 H  HA   B MET   A 1 128 ? 17.813  11.040  9.620   0.24 36.41 ? 128 MET   A HA   1 
ATOM   1909 H  HB2  A MET   A 1 128 ? 15.790  9.985   8.795   0.76 36.77 ? 128 MET   A HB2  1 
ATOM   1910 H  HB2  B MET   A 1 128 ? 15.782  9.898   8.825   0.24 36.98 ? 128 MET   A HB2  1 
ATOM   1911 H  HB3  A MET   A 1 128 ? 16.140  8.767   9.746   0.76 36.77 ? 128 MET   A HB3  1 
ATOM   1912 H  HB3  B MET   A 1 128 ? 16.131  8.820   9.936   0.24 36.98 ? 128 MET   A HB3  1 
ATOM   1913 H  HG2  A MET   A 1 128 ? 15.741  9.997   11.597  0.76 40.02 ? 128 MET   A HG2  1 
ATOM   1914 H  HG2  B MET   A 1 128 ? 16.112  10.805  11.449  0.24 40.59 ? 128 MET   A HG2  1 
ATOM   1915 H  HG3  A MET   A 1 128 ? 15.660  11.344  10.747  0.76 40.02 ? 128 MET   A HG3  1 
ATOM   1916 H  HG3  B MET   A 1 128 ? 15.188  11.421  10.315  0.24 40.59 ? 128 MET   A HG3  1 
ATOM   1917 H  HE1  A MET   A 1 128 ? 12.705  8.245   11.337  0.76 40.22 ? 128 MET   A HE1  1 
ATOM   1918 H  HE1  B MET   A 1 128 ? 12.170  9.307   10.246  0.24 43.41 ? 128 MET   A HE1  1 
ATOM   1919 H  HE2  A MET   A 1 128 ? 14.262  8.233   11.656  0.76 40.22 ? 128 MET   A HE2  1 
ATOM   1920 H  HE2  B MET   A 1 128 ? 13.052  10.385  9.482   0.24 43.41 ? 128 MET   A HE2  1 
ATOM   1921 H  HE3  A MET   A 1 128 ? 13.280  9.108   12.544  0.76 40.22 ? 128 MET   A HE3  1 
ATOM   1922 H  HE3  B MET   A 1 128 ? 13.466  8.852   9.447   0.24 43.41 ? 128 MET   A HE3  1 
ATOM   1923 N  N    . GLN   A 1 129 ? 19.098  10.192  11.507  1.00 26.21 ? 129 GLN   A N    1 
ATOM   1924 C  CA   . GLN   A 1 129 ? 19.780  9.661   12.679  1.00 26.42 ? 129 GLN   A CA   1 
ATOM   1925 C  C    . GLN   A 1 129 ? 18.811  8.862   13.543  1.00 26.76 ? 129 GLN   A C    1 
ATOM   1926 O  O    . GLN   A 1 129 ? 17.667  9.271   13.757  1.00 24.45 ? 129 GLN   A O    1 
ATOM   1927 C  CB   . GLN   A 1 129 ? 20.354  10.812  13.497  1.00 26.86 ? 129 GLN   A CB   1 
ATOM   1928 C  CG   . GLN   A 1 129 ? 21.207  10.393  14.677  1.00 27.76 ? 129 GLN   A CG   1 
ATOM   1929 C  CD   . GLN   A 1 129 ? 21.671  11.587  15.481  1.00 26.16 ? 129 GLN   A CD   1 
ATOM   1930 O  OE1  . GLN   A 1 129 ? 20.861  12.451  15.835  1.00 27.57 ? 129 GLN   A OE1  1 
ATOM   1931 N  NE2  . GLN   A 1 129 ? 22.960  11.634  15.803  1.00 25.68 ? 129 GLN   A NE2  1 
ATOM   1932 H  H    . GLN   A 1 129 ? 19.109  11.050  11.454  1.00 31.47 ? 129 GLN   A H    1 
ATOM   1933 H  HA   . GLN   A 1 129 ? 20.506  9.080   12.403  1.00 31.72 ? 129 GLN   A HA   1 
ATOM   1934 H  HB2  . GLN   A 1 129 ? 20.906  11.358  12.916  1.00 32.26 ? 129 GLN   A HB2  1 
ATOM   1935 H  HB3  . GLN   A 1 129 ? 19.619  11.343  13.841  1.00 32.26 ? 129 GLN   A HB3  1 
ATOM   1936 H  HG2  . GLN   A 1 129 ? 20.688  9.819   15.262  1.00 33.33 ? 129 GLN   A HG2  1 
ATOM   1937 H  HG3  . GLN   A 1 129 ? 21.991  9.922   14.353  1.00 33.33 ? 129 GLN   A HG3  1 
ATOM   1938 H  HE21 . GLN   A 1 129 ? 23.491  11.010  15.542  1.00 30.84 ? 129 GLN   A HE21 1 
ATOM   1939 H  HE22 . GLN   A 1 129 ? 23.265  12.294  16.262  1.00 30.84 ? 129 GLN   A HE22 1 
ATOM   1940 N  N    . LEU   A 1 130 ? 19.287  7.728   14.059  1.00 22.51 ? 130 LEU   A N    1 
ATOM   1941 C  CA   . LEU   A 1 130 ? 18.509  6.934   15.003  1.00 18.89 ? 130 LEU   A CA   1 
ATOM   1942 C  C    . LEU   A 1 130 ? 18.550  7.609   16.367  1.00 22.60 ? 130 LEU   A C    1 
ATOM   1943 O  O    . LEU   A 1 130 ? 19.622  7.716   16.972  1.00 21.91 ? 130 LEU   A O    1 
ATOM   1944 C  CB   . LEU   A 1 130 ? 19.073  5.526   15.121  1.00 19.45 ? 130 LEU   A CB   1 
ATOM   1945 C  CG   . LEU   A 1 130 ? 18.555  4.504   14.116  1.00 26.14 ? 130 LEU   A CG   1 
ATOM   1946 C  CD1  . LEU   A 1 130 ? 18.844  4.985   12.712  1.00 29.18 ? 130 LEU   A CD1  1 
ATOM   1947 C  CD2  . LEU   A 1 130 ? 19.209  3.172   14.370  1.00 23.74 ? 130 LEU   A CD2  1 
ATOM   1948 H  H    . LEU   A 1 130 ? 20.060  7.398   13.876  1.00 27.03 ? 130 LEU   A H    1 
ATOM   1949 H  HA   . LEU   A 1 130 ? 17.587  6.879   14.707  1.00 22.69 ? 130 LEU   A HA   1 
ATOM   1950 H  HB2  . LEU   A 1 130 ? 20.036  5.574   15.013  1.00 23.36 ? 130 LEU   A HB2  1 
ATOM   1951 H  HB3  . LEU   A 1 130 ? 18.866  5.189   16.007  1.00 23.36 ? 130 LEU   A HB3  1 
ATOM   1952 H  HG   . LEU   A 1 130 ? 17.596  4.403   14.218  1.00 31.38 ? 130 LEU   A HG   1 
ATOM   1953 H  HD11 . LEU   A 1 130 ? 18.628  4.276   12.086  1.00 35.03 ? 130 LEU   A HD11 1 
ATOM   1954 H  HD12 . LEU   A 1 130 ? 18.300  5.766   12.526  1.00 35.03 ? 130 LEU   A HD12 1 
ATOM   1955 H  HD13 . LEU   A 1 130 ? 19.785  5.211   12.644  1.00 35.03 ? 130 LEU   A HD13 1 
ATOM   1956 H  HD21 . LEU   A 1 130 ? 18.873  2.528   13.727  1.00 28.51 ? 130 LEU   A HD21 1 
ATOM   1957 H  HD22 . LEU   A 1 130 ? 20.169  3.268   14.272  1.00 28.51 ? 130 LEU   A HD22 1 
ATOM   1958 H  HD23 . LEU   A 1 130 ? 18.995  2.882   15.271  1.00 28.51 ? 130 LEU   A HD23 1 
ATOM   1959 N  N    . VAL   A 1 131 ? 17.407  8.068   16.856  1.00 19.88 ? 131 VAL   A N    1 
ATOM   1960 C  CA   . VAL   A 1 131 ? 17.332  8.726   18.155  1.00 20.77 ? 131 VAL   A CA   1 
ATOM   1961 C  C    . VAL   A 1 131 ? 16.707  7.726   19.120  1.00 21.23 ? 131 VAL   A C    1 
ATOM   1962 O  O    . VAL   A 1 131 ? 15.527  7.372   18.985  1.00 19.40 ? 131 VAL   A O    1 
ATOM   1963 C  CB   . VAL   A 1 131 ? 16.540  10.036  18.085  1.00 24.52 ? 131 VAL   A CB   1 
ATOM   1964 C  CG1  . VAL   A 1 131 ? 16.365  10.638  19.473  1.00 22.48 ? 131 VAL   A CG1  1 
ATOM   1965 C  CG2  . VAL   A 1 131 ? 17.237  11.022  17.149  1.00 25.12 ? 131 VAL   A CG2  1 
ATOM   1966 H  H    . VAL   A 1 131 ? 16.651  8.011   16.451  1.00 23.87 ? 131 VAL   A H    1 
ATOM   1967 H  HA   . VAL   A 1 131 ? 18.227  8.931   18.468  1.00 24.94 ? 131 VAL   A HA   1 
ATOM   1968 H  HB   . VAL   A 1 131 ? 15.658  9.853   17.725  1.00 29.45 ? 131 VAL   A HB   1 
ATOM   1969 H  HG11 . VAL   A 1 131 ? 16.037  11.546  19.382  1.00 27.00 ? 131 VAL   A HG11 1 
ATOM   1970 H  HG12 . VAL   A 1 131 ? 15.727  10.106  19.973  1.00 27.00 ? 131 VAL   A HG12 1 
ATOM   1971 H  HG13 . VAL   A 1 131 ? 17.223  10.641  19.926  1.00 27.00 ? 131 VAL   A HG13 1 
ATOM   1972 H  HG21 . VAL   A 1 131 ? 16.736  11.853  17.136  1.00 30.17 ? 131 VAL   A HG21 1 
ATOM   1973 H  HG22 . VAL   A 1 131 ? 18.137  11.183  17.474  1.00 30.17 ? 131 VAL   A HG22 1 
ATOM   1974 H  HG23 . VAL   A 1 131 ? 17.270  10.642  16.257  1.00 30.17 ? 131 VAL   A HG23 1 
ATOM   1975 N  N    . MET   A 1 132 ? 17.516  7.266   20.079  1.00 18.58 ? 132 MET   A N    1 
ATOM   1976 C  CA   . MET   A 1 132 ? 17.156  6.192   20.992  1.00 16.85 ? 132 MET   A CA   1 
ATOM   1977 C  C    . MET   A 1 132 ? 16.977  6.832   22.370  1.00 21.52 ? 132 MET   A C    1 
ATOM   1978 O  O    . MET   A 1 132 ? 17.963  7.228   23.009  1.00 20.26 ? 132 MET   A O    1 
ATOM   1979 C  CB   . MET   A 1 132 ? 18.230  5.115   21.051  1.00 18.58 ? 132 MET   A CB   1 
ATOM   1980 C  CG   . MET   A 1 132 ? 18.618  4.551   19.698  1.00 20.41 ? 132 MET   A CG   1 
ATOM   1981 S  SD   . MET   A 1 132 ? 17.564  3.256   19.077  1.00 19.65 ? 132 MET   A SD   1 
ATOM   1982 C  CE   . MET   A 1 132 ? 18.186  1.790   19.986  1.00 19.35 ? 132 MET   A CE   1 
ATOM   1983 H  H    . MET   A 1 132 ? 18.306  7.576   20.220  1.00 22.31 ? 132 MET   A H    1 
ATOM   1984 H  HA   . MET   A 1 132 ? 16.322  5.785   20.709  1.00 20.24 ? 132 MET   A HA   1 
ATOM   1985 H  HB2  . MET   A 1 132 ? 19.028  5.493   21.453  1.00 22.31 ? 132 MET   A HB2  1 
ATOM   1986 H  HB3  . MET   A 1 132 ? 17.905  4.381   21.595  1.00 22.31 ? 132 MET   A HB3  1 
ATOM   1987 H  HG2  . MET   A 1 132 ? 18.612  5.268   19.045  1.00 24.52 ? 132 MET   A HG2  1 
ATOM   1988 H  HG3  . MET   A 1 132 ? 19.514  4.186   19.766  1.00 24.52 ? 132 MET   A HG3  1 
ATOM   1989 H  HE1  . MET   A 1 132 ? 17.672  1.012   19.719  1.00 23.24 ? 132 MET   A HE1  1 
ATOM   1990 H  HE2  . MET   A 1 132 ? 19.122  1.659   19.770  1.00 23.24 ? 132 MET   A HE2  1 
ATOM   1991 H  HE3  . MET   A 1 132 ? 18.084  1.943   20.938  1.00 23.24 ? 132 MET   A HE3  1 
ATOM   1992 N  N    . ARG   A 1 133 ? 15.726  6.939   22.817  1.00 20.62 ? 133 ARG   A N    1 
ATOM   1993 C  CA   . ARG   A 1 133 ? 15.374  7.632   24.051  1.00 19.24 ? 133 ARG   A CA   1 
ATOM   1994 C  C    . ARG   A 1 133 ? 15.125  6.595   25.136  1.00 19.57 ? 133 ARG   A C    1 
ATOM   1995 O  O    . ARG   A 1 133 ? 14.227  5.752   25.011  1.00 19.74 ? 133 ARG   A O    1 
ATOM   1996 C  CB   . ARG   A 1 133 ? 14.149  8.513   23.833  1.00 19.78 ? 133 ARG   A CB   1 
ATOM   1997 C  CG   . ARG   A 1 133 ? 14.283  9.355   22.577  1.00 22.21 ? 133 ARG   A CG   1 
ATOM   1998 C  CD   . ARG   A 1 133 ? 13.426  10.581  22.648  1.00 23.83 ? 133 ARG   A CD   1 
ATOM   1999 N  NE   . ARG   A 1 133 ? 12.019  10.210  22.712  1.00 23.31 ? 133 ARG   A NE   1 
ATOM   2000 C  CZ   . ARG   A 1 133 ? 11.056  11.013  23.138  1.00 26.57 ? 133 ARG   A CZ   1 
ATOM   2001 N  NH1  . ARG   A 1 133 ? 11.272  12.306  23.327  1.00 25.58 ? 133 ARG   A NH1  1 
ATOM   2002 N  NH2  . ARG   A 1 133 ? 9.849   10.510  23.380  1.00 25.31 ? 133 ARG   A NH2  1 
ATOM   2003 H  H    . ARG   A 1 133 ? 15.046  6.607   22.408  1.00 24.76 ? 133 ARG   A H    1 
ATOM   2004 H  HA   . ARG   A 1 133 ? 16.112  8.196   24.328  1.00 23.11 ? 133 ARG   A HA   1 
ATOM   2005 H  HB2  . ARG   A 1 133 ? 13.364  7.951   23.740  1.00 23.76 ? 133 ARG   A HB2  1 
ATOM   2006 H  HB3  . ARG   A 1 133 ? 14.046  9.110   24.590  1.00 23.76 ? 133 ARG   A HB3  1 
ATOM   2007 H  HG2  . ARG   A 1 133 ? 15.206  9.634   22.475  1.00 26.67 ? 133 ARG   A HG2  1 
ATOM   2008 H  HG3  . ARG   A 1 133 ? 14.003  8.832   21.809  1.00 26.67 ? 133 ARG   A HG3  1 
ATOM   2009 H  HD2  . ARG   A 1 133 ? 13.648  11.086  23.445  1.00 28.61 ? 133 ARG   A HD2  1 
ATOM   2010 H  HD3  . ARG   A 1 133 ? 13.566  11.120  21.854  1.00 28.61 ? 133 ARG   A HD3  1 
ATOM   2011 H  HE   . ARG   A 1 133 ? 11.800  9.419   22.457  1.00 28.00 ? 133 ARG   A HE   1 
ATOM   2012 H  HH11 . ARG   A 1 133 ? 12.051  12.640  23.182  1.00 30.72 ? 133 ARG   A HH11 1 
ATOM   2013 H  HH12 . ARG   A 1 133 ? 10.632  12.812  23.600  1.00 30.72 ? 133 ARG   A HH12 1 
ATOM   2014 H  HH21 . ARG   A 1 133 ? 9.699   9.673   23.253  1.00 30.39 ? 133 ARG   A HH21 1 
ATOM   2015 H  HH22 . ARG   A 1 133 ? 9.213   11.026  23.643  1.00 30.39 ? 133 ARG   A HH22 1 
ATOM   2016 N  N    . VAL   A 1 134 ? 15.916  6.685   26.202  1.00 19.22 ? 134 VAL   A N    1 
ATOM   2017 C  CA   A VAL   A 1 134 ? 16.046  5.672   27.237  0.60 19.28 ? 134 VAL   A CA   1 
ATOM   2018 C  CA   B VAL   A 1 134 ? 15.969  5.651   27.221  0.40 19.24 ? 134 VAL   A CA   1 
ATOM   2019 C  C    . VAL   A 1 134 ? 15.566  6.260   28.558  1.00 18.91 ? 134 VAL   A C    1 
ATOM   2020 O  O    . VAL   A 1 134 ? 15.533  7.481   28.738  1.00 19.39 ? 134 VAL   A O    1 
ATOM   2021 C  CB   A VAL   A 1 134 ? 17.516  5.201   27.319  0.60 22.00 ? 134 VAL   A CB   1 
ATOM   2022 C  CB   B VAL   A 1 134 ? 17.374  5.029   27.313  0.40 22.50 ? 134 VAL   A CB   1 
ATOM   2023 C  CG1  A VAL   A 1 134 ? 17.674  4.029   28.241  0.60 17.61 ? 134 VAL   A CG1  1 
ATOM   2024 C  CG1  B VAL   A 1 134 ? 17.783  4.428   25.979  0.40 25.56 ? 134 VAL   A CG1  1 
ATOM   2025 C  CG2  A VAL   A 1 134 ? 18.052  4.884   25.905  0.60 26.01 ? 134 VAL   A CG2  1 
ATOM   2026 C  CG2  B VAL   A 1 134 ? 18.333  6.101   27.751  0.40 23.48 ? 134 VAL   A CG2  1 
ATOM   2027 H  H    A VAL   A 1 134 ? 16.416  7.369   26.351  0.60 23.09 ? 134 VAL   A H    1 
ATOM   2028 H  H    B VAL   A 1 134 ? 16.435  7.352   26.356  0.40 23.09 ? 134 VAL   A H    1 
ATOM   2029 H  HA   A VAL   A 1 134 ? 15.489  4.909   27.018  0.60 23.16 ? 134 VAL   A HA   1 
ATOM   2030 H  HA   B VAL   A 1 134 ? 15.338  4.948   27.003  0.40 23.11 ? 134 VAL   A HA   1 
ATOM   2031 H  HB   A VAL   A 1 134 ? 18.051  5.927   27.677  0.60 26.42 ? 134 VAL   A HB   1 
ATOM   2032 H  HB   B VAL   A 1 134 ? 17.373  4.325   27.981  0.40 27.02 ? 134 VAL   A HB   1 
ATOM   2033 H  HG11 A VAL   A 1 134 ? 18.569  3.669   28.139  0.60 21.15 ? 134 VAL   A HG11 1 
ATOM   2034 H  HG11 B VAL   A 1 134 ? 18.650  4.005   26.078  0.40 30.69 ? 134 VAL   A HG11 1 
ATOM   2035 H  HG12 A VAL   A 1 134 ? 17.539  4.323   29.155  0.60 21.15 ? 134 VAL   A HG12 1 
ATOM   2036 H  HG12 B VAL   A 1 134 ? 17.122  3.770   25.714  0.40 30.69 ? 134 VAL   A HG12 1 
ATOM   2037 H  HG13 A VAL   A 1 134 ? 17.018  3.354   28.008  0.60 21.15 ? 134 VAL   A HG13 1 
ATOM   2038 H  HG13 B VAL   A 1 134 ? 17.832  5.134   25.316  0.40 30.69 ? 134 VAL   A HG13 1 
ATOM   2039 H  HG21 A VAL   A 1 134 ? 18.911  4.440   25.985  0.60 31.23 ? 134 VAL   A HG21 1 
ATOM   2040 H  HG21 B VAL   A 1 134 ? 19.136  5.999   27.224  0.40 28.20 ? 134 VAL   A HG21 1 
ATOM   2041 H  HG22 A VAL   A 1 134 ? 17.421  4.304   25.452  0.60 31.23 ? 134 VAL   A HG22 1 
ATOM   2042 H  HG22 B VAL   A 1 134 ? 17.948  6.974   27.593  0.40 28.20 ? 134 VAL   A HG22 1 
ATOM   2043 H  HG23 A VAL   A 1 134 ? 18.153  5.712   25.411  0.60 31.23 ? 134 VAL   A HG23 1 
ATOM   2044 H  HG23 B VAL   A 1 134 ? 18.503  5.994   28.697  0.40 28.20 ? 134 VAL   A HG23 1 
ATOM   2045 N  N    . HIS   A 1 135 ? 15.224  5.379   29.491  1.00 17.77 ? 135 HIS   A N    1 
ATOM   2046 C  CA   . HIS   A 1 135 ? 14.695  5.775   30.798  1.00 19.94 ? 135 HIS   A CA   1 
ATOM   2047 C  C    . HIS   A 1 135 ? 13.409  6.589   30.673  1.00 20.85 ? 135 HIS   A C    1 
ATOM   2048 O  O    . HIS   A 1 135 ? 13.173  7.529   31.442  1.00 20.66 ? 135 HIS   A O    1 
ATOM   2049 C  CB   . HIS   A 1 135 ? 15.702  6.568   31.650  1.00 21.49 ? 135 HIS   A CB   1 
ATOM   2050 C  CG   . HIS   A 1 135 ? 17.056  5.949   31.790  1.00 19.87 ? 135 HIS   A CG   1 
ATOM   2051 N  ND1  . HIS   A 1 135 ? 17.276  4.812   32.539  1.00 21.85 ? 135 HIS   A ND1  1 
ATOM   2052 C  CD2  . HIS   A 1 135 ? 18.282  6.386   31.408  1.00 20.74 ? 135 HIS   A CD2  1 
ATOM   2053 C  CE1  . HIS   A 1 135 ? 18.568  4.526   32.537  1.00 20.09 ? 135 HIS   A CE1  1 
ATOM   2054 N  NE2  . HIS   A 1 135 ? 19.200  5.471   31.864  1.00 18.42 ? 135 HIS   A NE2  1 
ATOM   2055 H  H    . HIS   A 1 135 ? 15.289  4.527   29.391  1.00 21.35 ? 135 HIS   A H    1 
ATOM   2056 H  HA   . HIS   A 1 135 ? 14.476  4.969   31.291  1.00 23.94 ? 135 HIS   A HA   1 
ATOM   2057 H  HB2  . HIS   A 1 135 ? 15.822  7.443   31.248  1.00 25.80 ? 135 HIS   A HB2  1 
ATOM   2058 H  HB3  . HIS   A 1 135 ? 15.335  6.670   32.542  1.00 25.80 ? 135 HIS   A HB3  1 
ATOM   2059 H  HD1  . HIS   A 1 135 ? 16.664  4.337   32.911  1.00 26.24 ? 135 HIS   A HD1  1 
ATOM   2060 H  HD2  . HIS   A 1 135 ? 18.464  7.142   30.897  1.00 24.91 ? 135 HIS   A HD2  1 
ATOM   2061 H  HE1  . HIS   A 1 135 ? 18.965  3.795   32.953  1.00 24.12 ? 135 HIS   A HE1  1 
ATOM   2062 H  HE2  . HIS   A 1 135 ? 20.049  5.505   31.728  1.00 22.13 ? 135 HIS   A HE2  1 
ATOM   2063 N  N    . TYR   A 1 136 ? 12.567  6.247   29.707  1.00 19.63 ? 136 TYR   A N    1 
ATOM   2064 C  CA   . TYR   A 1 136 ? 11.306  6.954   29.545  1.00 19.67 ? 136 TYR   A CA   1 
ATOM   2065 C  C    . TYR   A 1 136 ? 10.334  6.599   30.661  1.00 20.58 ? 136 TYR   A C    1 
ATOM   2066 O  O    . TYR   A 1 136 ? 10.110  5.423   30.954  1.00 19.90 ? 136 TYR   A O    1 
ATOM   2067 C  CB   . TYR   A 1 136 ? 10.693  6.613   28.194  1.00 20.22 ? 136 TYR   A CB   1 
ATOM   2068 C  CG   . TYR   A 1 136 ? 9.281   7.101   27.989  1.00 21.58 ? 136 TYR   A CG   1 
ATOM   2069 C  CD1  . TYR   A 1 136 ? 9.027   8.377   27.505  1.00 23.04 ? 136 TYR   A CD1  1 
ATOM   2070 C  CD2  . TYR   A 1 136 ? 8.199   6.269   28.246  1.00 21.53 ? 136 TYR   A CD2  1 
ATOM   2071 C  CE1  . TYR   A 1 136 ? 7.732   8.814   27.297  1.00 24.73 ? 136 TYR   A CE1  1 
ATOM   2072 C  CE2  . TYR   A 1 136 ? 6.908   6.694   28.038  1.00 23.96 ? 136 TYR   A CE2  1 
ATOM   2073 C  CZ   . TYR   A 1 136 ? 6.678   7.964   27.564  1.00 25.23 ? 136 TYR   A CZ   1 
ATOM   2074 O  OH   . TYR   A 1 136 ? 5.382   8.379   27.370  1.00 30.40 ? 136 TYR   A OH   1 
ATOM   2075 H  H    . TYR   A 1 136 ? 12.700  5.616   29.138  1.00 23.58 ? 136 TYR   A H    1 
ATOM   2076 H  HA   . TYR   A 1 136 ? 11.468  7.910   29.574  1.00 23.63 ? 136 TYR   A HA   1 
ATOM   2077 H  HB2  . TYR   A 1 136 ? 11.242  7.007   27.498  1.00 24.29 ? 136 TYR   A HB2  1 
ATOM   2078 H  HB3  . TYR   A 1 136 ? 10.686  5.648   28.094  1.00 24.29 ? 136 TYR   A HB3  1 
ATOM   2079 H  HD1  . TYR   A 1 136 ? 9.737   8.947   27.321  1.00 27.66 ? 136 TYR   A HD1  1 
ATOM   2080 H  HD2  . TYR   A 1 136 ? 8.351   5.408   28.562  1.00 25.85 ? 136 TYR   A HD2  1 
ATOM   2081 H  HE1  . TYR   A 1 136 ? 7.573   9.673   26.978  1.00 29.70 ? 136 TYR   A HE1  1 
ATOM   2082 H  HE2  . TYR   A 1 136 ? 6.194   6.127   28.221  1.00 28.78 ? 136 TYR   A HE2  1 
ATOM   2083 H  HH   . TYR   A 1 136 ? 4.849   7.762   27.572  1.00 36.49 ? 136 TYR   A HH   1 
ATOM   2084 N  N    . GLY   A 1 137 ? 9.765   7.628   31.290  1.00 23.30 ? 137 GLY   A N    1 
ATOM   2085 C  CA   . GLY   A 1 137 ? 8.651   7.437   32.201  1.00 22.27 ? 137 GLY   A CA   1 
ATOM   2086 C  C    . GLY   A 1 137 ? 9.027   6.789   33.522  1.00 21.46 ? 137 GLY   A C    1 
ATOM   2087 O  O    . GLY   A 1 137 ? 10.192  6.578   33.849  1.00 22.88 ? 137 GLY   A O    1 
ATOM   2088 H  H    . GLY   A 1 137 ? 10.011  8.447   31.202  1.00 27.98 ? 137 GLY   A H    1 
ATOM   2089 H  HA2  . GLY   A 1 137 ? 8.247   8.298   32.392  1.00 26.74 ? 137 GLY   A HA2  1 
ATOM   2090 H  HA3  . GLY   A 1 137 ? 7.983   6.880   31.772  1.00 26.74 ? 137 GLY   A HA3  1 
ATOM   2091 N  N    . GLN   A 1 138 ? 7.987   6.463   34.289  1.00 22.53 ? 138 GLN   A N    1 
ATOM   2092 C  CA   . GLN   A 1 138 ? 8.134   5.860   35.609  1.00 23.15 ? 138 GLN   A CA   1 
ATOM   2093 C  C    . GLN   A 1 138 ? 7.514   4.468   35.552  1.00 25.28 ? 138 GLN   A C    1 
ATOM   2094 O  O    . GLN   A 1 138 ? 6.295   4.328   35.407  1.00 28.01 ? 138 GLN   A O    1 
ATOM   2095 C  CB   . GLN   A 1 138 ? 7.454   6.750   36.650  1.00 32.94 ? 138 GLN   A CB   1 
ATOM   2096 C  CG   . GLN   A 1 138 ? 7.780   8.222   36.471  1.00 35.81 ? 138 GLN   A CG   1 
ATOM   2097 C  CD   . GLN   A 1 138 ? 7.172   9.112   37.535  1.00 56.59 ? 138 GLN   A CD   1 
ATOM   2098 O  OE1  . GLN   A 1 138 ? 6.584   10.148  37.230  1.00 54.97 ? 138 GLN   A OE1  1 
ATOM   2099 N  NE2  . GLN   A 1 138 ? 7.278   8.692   38.788  1.00 51.69 ? 138 GLN   A NE2  1 
ATOM   2100 H  H    . GLN   A 1 138 ? 7.167   6.585   34.059  1.00 27.06 ? 138 GLN   A H    1 
ATOM   2101 H  HA   . GLN   A 1 138 ? 9.074   5.776   35.834  1.00 27.80 ? 138 GLN   A HA   1 
ATOM   2102 H  HB2  . GLN   A 1 138 ? 6.493   6.645   36.576  1.00 39.55 ? 138 GLN   A HB2  1 
ATOM   2103 H  HB3  . GLN   A 1 138 ? 7.750   6.479   37.533  1.00 39.55 ? 138 GLN   A HB3  1 
ATOM   2104 H  HG2  . GLN   A 1 138 ? 8.743   8.336   36.502  1.00 43.00 ? 138 GLN   A HG2  1 
ATOM   2105 H  HG3  . GLN   A 1 138 ? 7.440   8.520   35.613  1.00 43.00 ? 138 GLN   A HG3  1 
ATOM   2106 H  HE21 . GLN   A 1 138 ? 7.692   7.959   38.964  1.00 62.04 ? 138 GLN   A HE21 1 
ATOM   2107 H  HE22 . GLN   A 1 138 ? 6.946   9.162   39.427  1.00 62.04 ? 138 GLN   A HE22 1 
ATOM   2108 N  N    . GLY   A 1 139 ? 8.357   3.444   35.642  1.00 24.07 ? 139 GLY   A N    1 
ATOM   2109 C  CA   . GLY   A 1 139 ? 7.877   2.072   35.592  1.00 23.02 ? 139 GLY   A CA   1 
ATOM   2110 C  C    . GLY   A 1 139 ? 7.200   1.699   34.292  1.00 24.85 ? 139 GLY   A C    1 
ATOM   2111 O  O    . GLY   A 1 139 ? 6.243   0.913   34.300  1.00 24.81 ? 139 GLY   A O    1 
ATOM   2112 H  H    . GLY   A 1 139 ? 9.209   3.519   35.732  1.00 28.90 ? 139 GLY   A H    1 
ATOM   2113 H  HA2  . GLY   A 1 139 ? 8.624   1.470   35.728  1.00 27.64 ? 139 GLY   A HA2  1 
ATOM   2114 H  HA3  . GLY   A 1 139 ? 7.242   1.932   36.312  1.00 27.64 ? 139 GLY   A HA3  1 
ATOM   2115 N  N    . TYR   A 1 140 ? 7.687   2.223   33.171  1.00 23.25 ? 140 TYR   A N    1 
ATOM   2116 C  CA   . TYR   A 1 140 ? 7.043   2.034   31.872  1.00 22.19 ? 140 TYR   A CA   1 
ATOM   2117 C  C    . TYR   A 1 140 ? 7.519   0.721   31.256  1.00 20.01 ? 140 TYR   A C    1 
ATOM   2118 O  O    . TYR   A 1 140 ? 8.704   0.575   30.922  1.00 17.95 ? 140 TYR   A O    1 
ATOM   2119 C  CB   . TYR   A 1 140 ? 7.334   3.222   30.957  1.00 22.49 ? 140 TYR   A CB   1 
ATOM   2120 C  CG   . TYR   A 1 140 ? 6.591   3.195   29.635  1.00 22.54 ? 140 TYR   A CG   1 
ATOM   2121 C  CD1  . TYR   A 1 140 ? 5.229   3.452   29.564  1.00 28.75 ? 140 TYR   A CD1  1 
ATOM   2122 C  CD2  . TYR   A 1 140 ? 7.264   2.910   28.458  1.00 20.23 ? 140 TYR   A CD2  1 
ATOM   2123 C  CE1  . TYR   A 1 140 ? 4.559   3.424   28.351  1.00 30.24 ? 140 TYR   A CE1  1 
ATOM   2124 C  CE2  . TYR   A 1 140 ? 6.616   2.882   27.251  1.00 25.79 ? 140 TYR   A CE2  1 
ATOM   2125 C  CZ   . TYR   A 1 140 ? 5.266   3.135   27.196  1.00 27.19 ? 140 TYR   A CZ   1 
ATOM   2126 O  OH   . TYR   A 1 140 ? 4.647   3.096   25.975  1.00 38.24 ? 140 TYR   A OH   1 
ATOM   2127 H  H    . TYR   A 1 140 ? 8.401   2.700   33.135  1.00 27.91 ? 140 TYR   A H    1 
ATOM   2128 H  HA   . TYR   A 1 140 ? 6.083   1.978   31.998  1.00 26.65 ? 140 TYR   A HA   1 
ATOM   2129 H  HB2  . TYR   A 1 140 ? 7.084   4.038   31.419  1.00 27.01 ? 140 TYR   A HB2  1 
ATOM   2130 H  HB3  . TYR   A 1 140 ? 8.284   3.237   30.760  1.00 27.01 ? 140 TYR   A HB3  1 
ATOM   2131 H  HD1  . TYR   A 1 140 ? 4.758   3.644   30.343  1.00 34.52 ? 140 TYR   A HD1  1 
ATOM   2132 H  HD2  . TYR   A 1 140 ? 8.177   2.737   28.487  1.00 24.29 ? 140 TYR   A HD2  1 
ATOM   2133 H  HE1  . TYR   A 1 140 ? 3.646   3.597   28.313  1.00 36.31 ? 140 TYR   A HE1  1 
ATOM   2134 H  HE2  . TYR   A 1 140 ? 7.087   2.687   26.473  1.00 30.96 ? 140 TYR   A HE2  1 
ATOM   2135 H  HH   . TYR   A 1 140 ? 5.205   2.909   25.376  1.00 45.91 ? 140 TYR   A HH   1 
ATOM   2136 N  N    . GLU   A 1 141 ? 6.599   -0.225  31.103  1.00 19.60 ? 141 GLU   A N    1 
ATOM   2137 C  CA   . GLU   A 1 141 ? 6.925   -1.572  30.629  1.00 17.70 ? 141 GLU   A CA   1 
ATOM   2138 C  C    . GLU   A 1 141 ? 6.538   -1.714  29.161  1.00 18.01 ? 141 GLU   A C    1 
ATOM   2139 O  O    . GLU   A 1 141 ? 5.714   -2.552  28.767  1.00 18.68 ? 141 GLU   A O    1 
ATOM   2140 C  CB   . GLU   A 1 141 ? 6.226   -2.611  31.501  1.00 19.53 ? 141 GLU   A CB   1 
ATOM   2141 C  CG   . GLU   A 1 141 ? 6.574   -2.490  32.993  1.00 22.92 ? 141 GLU   A CG   1 
ATOM   2142 C  CD   . GLU   A 1 141 ? 6.324   -3.758  33.805  1.00 30.14 ? 141 GLU   A CD   1 
ATOM   2143 O  OE1  . GLU   A 1 141 ? 5.135   -4.074  33.993  1.00 29.33 ? 141 GLU   A OE1  1 
ATOM   2144 O  OE2  . GLU   A 1 141 ? 7.277   -4.360  34.359  1.00 23.65 ? 141 GLU   A OE2  1 
ATOM   2145 H  H    . GLU   A 1 141 ? 5.763   -0.112  31.269  1.00 23.54 ? 141 GLU   A H    1 
ATOM   2146 H  HA   . GLU   A 1 141 ? 7.882   -1.713  30.703  1.00 21.26 ? 141 GLU   A HA   1 
ATOM   2147 H  HB2  . GLU   A 1 141 ? 5.266   -2.503  31.409  1.00 23.45 ? 141 GLU   A HB2  1 
ATOM   2148 H  HB3  . GLU   A 1 141 ? 6.488   -3.497  31.205  1.00 23.45 ? 141 GLU   A HB3  1 
ATOM   2149 H  HG2  . GLU   A 1 141 ? 7.513   -2.268  33.078  1.00 27.52 ? 141 GLU   A HG2  1 
ATOM   2150 H  HG3  . GLU   A 1 141 ? 6.035   -1.782  33.380  1.00 27.52 ? 141 GLU   A HG3  1 
ATOM   2151 N  N    . ASN   A 1 142 ? 7.152   -0.856  28.350  1.00 16.82 ? 142 ASN   A N    1 
ATOM   2152 C  CA   . ASN   A 1 142 ? 6.951   -0.903  26.909  1.00 15.88 ? 142 ASN   A CA   1 
ATOM   2153 C  C    . ASN   A 1 142 ? 8.036   -0.076  26.216  1.00 17.52 ? 142 ASN   A C    1 
ATOM   2154 O  O    . ASN   A 1 142 ? 8.907   0.524   26.859  1.00 17.99 ? 142 ASN   A O    1 
ATOM   2155 C  CB   . ASN   A 1 142 ? 5.571   -0.365  26.517  1.00 17.60 ? 142 ASN   A CB   1 
ATOM   2156 C  CG   . ASN   A 1 142 ? 4.898   -1.210  25.460  1.00 17.08 ? 142 ASN   A CG   1 
ATOM   2157 O  OD1  . ASN   A 1 142 ? 5.556   -1.797  24.600  1.00 16.83 ? 142 ASN   A OD1  1 
ATOM   2158 N  ND2  . ASN   A 1 142 ? 3.574   -1.216  25.471  1.00 21.44 ? 142 ASN   A ND2  1 
ATOM   2159 H  H    . ASN   A 1 142 ? 7.690   -0.238  28.611  1.00 20.20 ? 142 ASN   A H    1 
ATOM   2160 H  HA   . ASN   A 1 142 ? 7.022   -1.821  26.603  1.00 19.08 ? 142 ASN   A HA   1 
ATOM   2161 H  HB2  . ASN   A 1 142 ? 5.000   -0.351  27.301  1.00 21.14 ? 142 ASN   A HB2  1 
ATOM   2162 H  HB3  . ASN   A 1 142 ? 5.670   0.531   26.161  1.00 21.14 ? 142 ASN   A HB3  1 
ATOM   2163 H  HD21 . ASN   A 1 142 ? 3.141   -1.676  24.887  1.00 25.75 ? 142 ASN   A HD21 1 
ATOM   2164 H  HD22 . ASN   A 1 142 ? 3.147   -0.783  26.080  1.00 25.75 ? 142 ASN   A HD22 1 
ATOM   2165 N  N    . ALA   A 1 143 ? 7.961   -0.062  24.888  1.00 16.38 ? 143 ALA   A N    1 
ATOM   2166 C  CA   . ALA   A 1 143 ? 8.775   0.757   24.003  1.00 14.76 ? 143 ALA   A CA   1 
ATOM   2167 C  C    . ALA   A 1 143 ? 7.865   1.166   22.851  1.00 15.75 ? 143 ALA   A C    1 
ATOM   2168 O  O    . ALA   A 1 143 ? 6.812   0.554   22.640  1.00 16.59 ? 143 ALA   A O    1 
ATOM   2169 C  CB   . ALA   A 1 143 ? 10.016  -0.002  23.514  1.00 15.41 ? 143 ALA   A CB   1 
ATOM   2170 H  H    . ALA   A 1 143 ? 7.406   -0.554  24.453  1.00 19.68 ? 143 ALA   A H    1 
ATOM   2171 H  HA   . ALA   A 1 143 ? 9.062   1.555   24.473  1.00 17.73 ? 143 ALA   A HA   1 
ATOM   2172 H  HB1  . ALA   A 1 143 ? 10.529  0.577   22.929  1.00 18.52 ? 143 ALA   A HB1  1 
ATOM   2173 H  HB2  . ALA   A 1 143 ? 10.552  -0.257  24.281  1.00 18.52 ? 143 ALA   A HB2  1 
ATOM   2174 H  HB3  . ALA   A 1 143 ? 9.731   -0.793  23.030  1.00 18.52 ? 143 ALA   A HB3  1 
ATOM   2175 N  N    . TYR   A 1 144 ? 8.250   2.210   22.111  1.00 16.03 ? 144 TYR   A N    1 
ATOM   2176 C  CA   . TYR   A 1 144 ? 7.383   2.636   21.016  1.00 16.53 ? 144 TYR   A CA   1 
ATOM   2177 C  C    . TYR   A 1 144 ? 8.155   3.464   19.992  1.00 18.65 ? 144 TYR   A C    1 
ATOM   2178 O  O    . TYR   A 1 144 ? 9.169   4.097   20.297  1.00 18.07 ? 144 TYR   A O    1 
ATOM   2179 C  CB   . TYR   A 1 144 ? 6.157   3.434   21.541  1.00 18.34 ? 144 TYR   A CB   1 
ATOM   2180 C  CG   . TYR   A 1 144 ? 6.458   4.816   22.107  1.00 20.90 ? 144 TYR   A CG   1 
ATOM   2181 C  CD1  . TYR   A 1 144 ? 6.725   5.003   23.457  1.00 22.23 ? 144 TYR   A CD1  1 
ATOM   2182 C  CD2  . TYR   A 1 144 ? 6.400   5.943   21.294  1.00 23.25 ? 144 TYR   A CD2  1 
ATOM   2183 C  CE1  . TYR   A 1 144 ? 6.997   6.267   23.964  1.00 24.96 ? 144 TYR   A CE1  1 
ATOM   2184 C  CE2  . TYR   A 1 144 ? 6.647   7.195   21.794  1.00 24.96 ? 144 TYR   A CE2  1 
ATOM   2185 C  CZ   . TYR   A 1 144 ? 6.951   7.359   23.122  1.00 24.67 ? 144 TYR   A CZ   1 
ATOM   2186 O  OH   . TYR   A 1 144 ? 7.198   8.634   23.582  1.00 29.24 ? 144 TYR   A OH   1 
ATOM   2187 H  H    . TYR   A 1 144 ? 8.971   2.666   22.216  1.00 19.26 ? 144 TYR   A H    1 
ATOM   2188 H  HA   . TYR   A 1 144 ? 7.048   1.847   20.562  1.00 19.85 ? 144 TYR   A HA   1 
ATOM   2189 H  HB2  . TYR   A 1 144 ? 5.532   3.551   20.808  1.00 22.02 ? 144 TYR   A HB2  1 
ATOM   2190 H  HB3  . TYR   A 1 144 ? 5.735   2.918   22.246  1.00 22.02 ? 144 TYR   A HB3  1 
ATOM   2191 H  HD1  . TYR   A 1 144 ? 6.769   4.265   24.021  1.00 26.70 ? 144 TYR   A HD1  1 
ATOM   2192 H  HD2  . TYR   A 1 144 ? 6.207   5.843   20.390  1.00 27.92 ? 144 TYR   A HD2  1 
ATOM   2193 H  HE1  . TYR   A 1 144 ? 7.191   6.379   24.867  1.00 29.97 ? 144 TYR   A HE1  1 
ATOM   2194 H  HE2  . TYR   A 1 144 ? 6.624   7.933   21.229  1.00 29.97 ? 144 TYR   A HE2  1 
ATOM   2195 H  HH   . TYR   A 1 144 ? 7.372   8.614   24.404  1.00 35.11 ? 144 TYR   A HH   1 
ATOM   2196 N  N    . TRP   A 1 145 ? 7.634   3.433   18.763  1.00 16.45 ? 145 TRP   A N    1 
ATOM   2197 C  CA   . TRP   A 1 145 ? 8.042   4.273   17.645  1.00 16.24 ? 145 TRP   A CA   1 
ATOM   2198 C  C    . TRP   A 1 145 ? 6.959   5.329   17.440  1.00 19.81 ? 145 TRP   A C    1 
ATOM   2199 O  O    . TRP   A 1 145 ? 5.765   5.027   17.531  1.00 18.55 ? 145 TRP   A O    1 
ATOM   2200 C  CB   . TRP   A 1 145 ? 8.217   3.413   16.385  1.00 16.77 ? 145 TRP   A CB   1 
ATOM   2201 C  CG   . TRP   A 1 145 ? 8.114   4.155   15.096  1.00 15.93 ? 145 TRP   A CG   1 
ATOM   2202 C  CD1  . TRP   A 1 145 ? 7.042   4.214   14.253  1.00 18.73 ? 145 TRP   A CD1  1 
ATOM   2203 C  CD2  . TRP   A 1 145 ? 9.153   4.921   14.484  1.00 21.16 ? 145 TRP   A CD2  1 
ATOM   2204 N  NE1  . TRP   A 1 145 ? 7.346   4.995   13.160  1.00 20.31 ? 145 TRP   A NE1  1 
ATOM   2205 C  CE2  . TRP   A 1 145 ? 8.638   5.436   13.278  1.00 18.44 ? 145 TRP   A CE2  1 
ATOM   2206 C  CE3  . TRP   A 1 145 ? 10.470  5.230   14.844  1.00 20.33 ? 145 TRP   A CE3  1 
ATOM   2207 C  CZ2  . TRP   A 1 145 ? 9.397   6.249   12.430  1.00 23.21 ? 145 TRP   A CZ2  1 
ATOM   2208 C  CZ3  . TRP   A 1 145 ? 11.219  6.032   14.002  1.00 19.77 ? 145 TRP   A CZ3  1 
ATOM   2209 C  CH2  . TRP   A 1 145 ? 10.679  6.534   12.811  1.00 22.56 ? 145 TRP   A CH2  1 
ATOM   2210 H  H    . TRP   A 1 145 ? 7.000   2.894   18.546  1.00 19.75 ? 145 TRP   A H    1 
ATOM   2211 H  HA   . TRP   A 1 145 ? 8.882   4.714   17.848  1.00 19.51 ? 145 TRP   A HA   1 
ATOM   2212 H  HB2  . TRP   A 1 145 ? 9.093   2.998   16.414  1.00 20.14 ? 145 TRP   A HB2  1 
ATOM   2213 H  HB3  . TRP   A 1 145 ? 7.532   2.726   16.383  1.00 20.14 ? 145 TRP   A HB3  1 
ATOM   2214 H  HD1  . TRP   A 1 145 ? 6.222   3.801   14.402  1.00 22.50 ? 145 TRP   A HD1  1 
ATOM   2215 H  HE1  . TRP   A 1 145 ? 6.815   5.171   12.507  1.00 24.40 ? 145 TRP   A HE1  1 
ATOM   2216 H  HE3  . TRP   A 1 145 ? 10.833  4.905   15.636  1.00 24.41 ? 145 TRP   A HE3  1 
ATOM   2217 H  HZ2  . TRP   A 1 145 ? 9.044   6.581   11.636  1.00 27.88 ? 145 TRP   A HZ2  1 
ATOM   2218 H  HZ3  . TRP   A 1 145 ? 12.094  6.246   14.233  1.00 23.74 ? 145 TRP   A HZ3  1 
ATOM   2219 H  HH2  . TRP   A 1 145 ? 11.207  7.069   12.263  1.00 27.09 ? 145 TRP   A HH2  1 
ATOM   2220 N  N    . ASP   A 1 146 ? 7.368   6.574   17.165  1.00 19.59 ? 146 ASP   A N    1 
ATOM   2221 C  CA   . ASP   A 1 146 ? 6.432   7.696   17.123  1.00 21.85 ? 146 ASP   A CA   1 
ATOM   2222 C  C    . ASP   A 1 146 ? 6.526   8.494   15.825  1.00 24.76 ? 146 ASP   A C    1 
ATOM   2223 O  O    . ASP   A 1 146 ? 5.981   9.601   15.741  1.00 24.87 ? 146 ASP   A O    1 
ATOM   2224 C  CB   . ASP   A 1 146 ? 6.667   8.598   18.341  1.00 25.94 ? 146 ASP   A CB   1 
ATOM   2225 C  CG   . ASP   A 1 146 ? 7.916   9.447   18.202  1.00 23.34 ? 146 ASP   A CG   1 
ATOM   2226 O  OD1  . ASP   A 1 146 ? 8.742   9.138   17.316  1.00 24.20 ? 146 ASP   A OD1  1 
ATOM   2227 O  OD2  . ASP   A 1 146 ? 8.118   10.362  19.029  1.00 28.52 ? 146 ASP   A OD2  1 
ATOM   2228 H  H    . ASP   A 1 146 ? 8.183   6.791   17.000  1.00 23.53 ? 146 ASP   A H    1 
ATOM   2229 H  HA   . ASP   A 1 146 ? 5.527   7.352   17.186  1.00 26.24 ? 146 ASP   A HA   1 
ATOM   2230 H  HB2  . ASP   A 1 146 ? 5.908   9.193   18.447  1.00 31.14 ? 146 ASP   A HB2  1 
ATOM   2231 H  HB3  . ASP   A 1 146 ? 6.767   8.043   19.129  1.00 31.14 ? 146 ASP   A HB3  1 
ATOM   2232 N  N    . GLY   A 1 147 ? 7.188   7.953   14.806  1.00 20.65 ? 147 GLY   A N    1 
ATOM   2233 C  CA   . GLY   A 1 147 ? 7.356   8.637   13.549  1.00 23.63 ? 147 GLY   A CA   1 
ATOM   2234 C  C    . GLY   A 1 147 ? 8.708   9.295   13.368  1.00 26.24 ? 147 GLY   A C    1 
ATOM   2235 O  O    . GLY   A 1 147 ? 9.064   9.644   12.234  1.00 25.80 ? 147 GLY   A O    1 
ATOM   2236 H  H    . GLY   A 1 147 ? 7.553   7.175   14.828  1.00 24.80 ? 147 GLY   A H    1 
ATOM   2237 H  HA2  . GLY   A 1 147 ? 7.232   8.002   12.826  1.00 28.37 ? 147 GLY   A HA2  1 
ATOM   2238 H  HA3  . GLY   A 1 147 ? 6.675   9.323   13.465  1.00 28.37 ? 147 GLY   A HA3  1 
ATOM   2239 N  N    . LYS   A 1 148 ? 9.476   9.469   14.441  1.00 24.77 ? 148 LYS   A N    1 
ATOM   2240 C  CA   . LYS   A 1 148 ? 10.786  10.091  14.314  1.00 27.96 ? 148 LYS   A CA   1 
ATOM   2241 C  C    . LYS   A 1 148 ? 11.851  9.529   15.236  1.00 22.40 ? 148 LYS   A C    1 
ATOM   2242 O  O    . LYS   A 1 148 ? 13.027  9.844   15.030  1.00 25.71 ? 148 LYS   A O    1 
ATOM   2243 C  CB   . LYS   A 1 148 ? 10.671  11.607  14.556  1.00 26.17 ? 148 LYS   A CB   1 
ATOM   2244 C  CG   . LYS   A 1 148 ? 10.390  12.003  16.013  1.00 29.42 ? 148 LYS   A CG   1 
ATOM   2245 C  CD   . LYS   A 1 148 ? 10.032  13.493  16.154  1.00 36.56 ? 148 LYS   A CD   1 
ATOM   2246 C  CE   . LYS   A 1 148 ? 10.783  14.164  17.309  1.00 49.99 ? 148 LYS   A CE   1 
ATOM   2247 N  NZ   . LYS   A 1 148 ? 10.580  15.646  17.359  1.00 55.51 ? 148 LYS   A NZ   1 
ATOM   2248 H  H    . LYS   A 1 148 ? 9.264   9.239   15.242  1.00 29.74 ? 148 LYS   A H    1 
ATOM   2249 H  HA   . LYS   A 1 148 ? 11.101  9.965   13.405  1.00 33.57 ? 148 LYS   A HA   1 
ATOM   2250 H  HB2  . LYS   A 1 148 ? 11.505  12.027  14.293  1.00 31.42 ? 148 LYS   A HB2  1 
ATOM   2251 H  HB3  . LYS   A 1 148 ? 9.946   11.953  14.012  1.00 31.42 ? 148 LYS   A HB3  1 
ATOM   2252 H  HG2  . LYS   A 1 148 ? 9.643   11.481  16.346  1.00 35.33 ? 148 LYS   A HG2  1 
ATOM   2253 H  HG3  . LYS   A 1 148 ? 11.181  11.833  16.548  1.00 35.33 ? 148 LYS   A HG3  1 
ATOM   2254 H  HD2  . LYS   A 1 148 ? 10.266  13.955  15.334  1.00 43.89 ? 148 LYS   A HD2  1 
ATOM   2255 H  HD3  . LYS   A 1 148 ? 9.081   13.576  16.324  1.00 43.89 ? 148 LYS   A HD3  1 
ATOM   2256 H  HE2  . LYS   A 1 148 ? 10.467  13.793  18.147  1.00 60.01 ? 148 LYS   A HE2  1 
ATOM   2257 H  HE3  . LYS   A 1 148 ? 11.733  13.995  17.208  1.00 60.01 ? 148 LYS   A HE3  1 
ATOM   2258 H  HZ1  . LYS   A 1 148 ? 11.033  15.992  18.043  1.00 66.63 ? 148 LYS   A HZ1  1 
ATOM   2259 H  HZ2  . LYS   A 1 148 ? 10.868  16.018  16.603  1.00 66.63 ? 148 LYS   A HZ2  1 
ATOM   2260 H  HZ3  . LYS   A 1 148 ? 9.715   15.831  17.461  1.00 66.63 ? 148 LYS   A HZ3  1 
ATOM   2261 N  N    . GLN   A 1 149 ? 11.505  8.701   16.222  1.00 20.51 ? 149 GLN   A N    1 
ATOM   2262 C  CA   . GLN   A 1 149 ? 12.469  8.238   17.210  1.00 21.31 ? 149 GLN   A CA   1 
ATOM   2263 C  C    . GLN   A 1 149 ? 11.885  7.030   17.932  1.00 19.68 ? 149 GLN   A C    1 
ATOM   2264 O  O    . GLN   A 1 149 ? 10.703  6.708   17.799  1.00 19.45 ? 149 GLN   A O    1 
ATOM   2265 C  CB   . GLN   A 1 149 ? 12.812  9.367   18.180  1.00 25.38 ? 149 GLN   A CB   1 
ATOM   2266 C  CG   . GLN   A 1 149 ? 11.670  9.778   19.079  1.00 23.27 ? 149 GLN   A CG   1 
ATOM   2267 C  CD   . GLN   A 1 149 ? 11.730  11.244  19.417  1.00 27.75 ? 149 GLN   A CD   1 
ATOM   2268 O  OE1  . GLN   A 1 149 ? 12.795  11.851  19.402  1.00 28.29 ? 149 GLN   A OE1  1 
ATOM   2269 N  NE2  . GLN   A 1 149 ? 10.583  11.811  19.776  1.00 27.58 ? 149 GLN   A NE2  1 
ATOM   2270 H  H    . GLN   A 1 149 ? 10.711  8.392   16.339  1.00 24.63 ? 149 GLN   A H    1 
ATOM   2271 H  HA   . GLN   A 1 149 ? 13.283  7.962   16.761  1.00 25.60 ? 149 GLN   A HA   1 
ATOM   2272 H  HB2  . GLN   A 1 149 ? 13.545  9.079   18.747  1.00 30.48 ? 149 GLN   A HB2  1 
ATOM   2273 H  HB3  . GLN   A 1 149 ? 13.081  10.145  17.668  1.00 30.48 ? 149 GLN   A HB3  1 
ATOM   2274 H  HG2  . GLN   A 1 149 ? 10.829  9.605   18.628  1.00 27.95 ? 149 GLN   A HG2  1 
ATOM   2275 H  HG3  . GLN   A 1 149 ? 11.717  9.274   19.906  1.00 27.95 ? 149 GLN   A HG3  1 
ATOM   2276 H  HE21 . GLN   A 1 149 ? 9.858   11.348  19.782  1.00 33.11 ? 149 GLN   A HE21 1 
ATOM   2277 H  HE22 . GLN   A 1 149 ? 10.562  12.645  19.983  1.00 33.11 ? 149 GLN   A HE22 1 
ATOM   2278 N  N    . MET   A 1 150 ? 12.754  6.367   18.690  1.00 18.79 ? 150 MET   A N    1 
ATOM   2279 C  CA   . MET   A 1 150 ? 12.479  5.115   19.389  1.00 17.97 ? 150 MET   A CA   1 
ATOM   2280 C  C    . MET   A 1 150 ? 12.612  5.373   20.881  1.00 18.59 ? 150 MET   A C    1 
ATOM   2281 O  O    . MET   A 1 150 ? 13.636  5.898   21.325  1.00 18.49 ? 150 MET   A O    1 
ATOM   2282 C  CB   . MET   A 1 150 ? 13.471  4.040   18.927  1.00 19.03 ? 150 MET   A CB   1 
ATOM   2283 C  CG   . MET   A 1 150 ? 13.158  3.532   17.521  1.00 18.02 ? 150 MET   A CG   1 
ATOM   2284 S  SD   . MET   A 1 150 ? 13.685  4.624   16.157  1.00 19.57 ? 150 MET   A SD   1 
ATOM   2285 C  CE   . MET   A 1 150 ? 15.424  4.938   16.550  1.00 20.55 ? 150 MET   A CE   1 
ATOM   2286 H  H    . MET   A 1 150 ? 13.558  6.643   18.820  1.00 22.57 ? 150 MET   A H    1 
ATOM   2287 H  HA   . MET   A 1 150 ? 11.578  4.817   19.187  1.00 21.58 ? 150 MET   A HA   1 
ATOM   2288 H  HB2  . MET   A 1 150 ? 14.367  4.410   18.930  1.00 22.86 ? 150 MET   A HB2  1 
ATOM   2289 H  HB3  . MET   A 1 150 ? 13.422  3.286   19.534  1.00 22.86 ? 150 MET   A HB3  1 
ATOM   2290 H  HG2  . MET   A 1 150 ? 13.601  2.678   17.398  1.00 21.64 ? 150 MET   A HG2  1 
ATOM   2291 H  HG3  . MET   A 1 150 ? 12.199  3.412   17.444  1.00 21.64 ? 150 MET   A HG3  1 
ATOM   2292 H  HE1  . MET   A 1 150 ? 15.865  5.296   15.763  1.00 24.68 ? 150 MET   A HE1  1 
ATOM   2293 H  HE2  . MET   A 1 150 ? 15.473  5.579   17.276  1.00 24.68 ? 150 MET   A HE2  1 
ATOM   2294 H  HE3  . MET   A 1 150 ? 15.845  4.105   16.814  1.00 24.68 ? 150 MET   A HE3  1 
ATOM   2295 N  N    . THR   A 1 151 ? 11.589  5.008   21.657  1.00 16.56 ? 151 THR   A N    1 
ATOM   2296 C  CA   . THR   A 1 151 ? 11.516  5.344   23.076  1.00 16.35 ? 151 THR   A CA   1 
ATOM   2297 C  C    . THR   A 1 151 ? 11.299  4.069   23.882  1.00 15.80 ? 151 THR   A C    1 
ATOM   2298 O  O    . THR   A 1 151 ? 10.456  3.240   23.523  1.00 18.38 ? 151 THR   A O    1 
ATOM   2299 C  CB   . THR   A 1 151 ? 10.396  6.365   23.309  1.00 20.15 ? 151 THR   A CB   1 
ATOM   2300 O  OG1  . THR   A 1 151 ? 10.631  7.523   22.489  1.00 20.40 ? 151 THR   A OG1  1 
ATOM   2301 C  CG2  . THR   A 1 151 ? 10.325  6.798   24.759  1.00 20.12 ? 151 THR   A CG2  1 
ATOM   2302 H  H    . THR   A 1 151 ? 10.913  4.556   21.376  1.00 19.89 ? 151 THR   A H    1 
ATOM   2303 H  HA   . THR   A 1 151 ? 12.354  5.743   23.358  1.00 19.64 ? 151 THR   A HA   1 
ATOM   2304 H  HB   . THR   A 1 151 ? 9.547   5.966   23.065  1.00 24.20 ? 151 THR   A HB   1 
ATOM   2305 H  HG1  . THR   A 1 151 ? 10.627  7.306   21.677  1.00 24.50 ? 151 THR   A HG1  1 
ATOM   2306 H  HG21 . THR   A 1 151 ? 9.678   7.514   24.858  1.00 24.16 ? 151 THR   A HG21 1 
ATOM   2307 H  HG22 . THR   A 1 151 ? 10.056  6.052   25.317  1.00 24.16 ? 151 THR   A HG22 1 
ATOM   2308 H  HG23 . THR   A 1 151 ? 11.193  7.116   25.053  1.00 24.16 ? 151 THR   A HG23 1 
ATOM   2309 N  N    . PHE   A 1 152 ? 12.071  3.921   24.959  1.00 16.64 ? 152 PHE   A N    1 
ATOM   2310 C  CA   . PHE   A 1 152 ? 12.184  2.679   25.712  1.00 16.80 ? 152 PHE   A CA   1 
ATOM   2311 C  C    . PHE   A 1 152 ? 12.027  2.957   27.197  1.00 18.54 ? 152 PHE   A C    1 
ATOM   2312 O  O    . PHE   A 1 152 ? 12.756  3.787   27.759  1.00 17.31 ? 152 PHE   A O    1 
ATOM   2313 C  CB   . PHE   A 1 152 ? 13.547  2.030   25.473  1.00 16.71 ? 152 PHE   A CB   1 
ATOM   2314 C  CG   . PHE   A 1 152 ? 13.919  1.847   24.026  1.00 15.36 ? 152 PHE   A CG   1 
ATOM   2315 C  CD1  . PHE   A 1 152 ? 13.580  0.697   23.333  1.00 16.81 ? 152 PHE   A CD1  1 
ATOM   2316 C  CD2  . PHE   A 1 152 ? 14.591  2.852   23.355  1.00 16.84 ? 152 PHE   A CD2  1 
ATOM   2317 C  CE1  . PHE   A 1 152 ? 13.944  0.538   22.000  1.00 18.33 ? 152 PHE   A CE1  1 
ATOM   2318 C  CE2  . PHE   A 1 152 ? 14.949  2.705   22.022  1.00 17.55 ? 152 PHE   A CE2  1 
ATOM   2319 C  CZ   . PHE   A 1 152 ? 14.616  1.554   21.345  1.00 16.52 ? 152 PHE   A CZ   1 
ATOM   2320 H  H    . PHE   A 1 152 ? 12.556  4.554   25.282  1.00 19.99 ? 152 PHE   A H    1 
ATOM   2321 H  HA   . PHE   A 1 152 ? 11.490  2.061   25.435  1.00 20.18 ? 152 PHE   A HA   1 
ATOM   2322 H  HB2  . PHE   A 1 152 ? 14.229  2.585   25.882  1.00 20.07 ? 152 PHE   A HB2  1 
ATOM   2323 H  HB3  . PHE   A 1 152 ? 13.548  1.154   25.889  1.00 20.07 ? 152 PHE   A HB3  1 
ATOM   2324 H  HD1  . PHE   A 1 152 ? 13.130  0.011   23.772  1.00 20.20 ? 152 PHE   A HD1  1 
ATOM   2325 H  HD2  . PHE   A 1 152 ? 14.821  3.631   23.808  1.00 20.22 ? 152 PHE   A HD2  1 
ATOM   2326 H  HE1  . PHE   A 1 152 ? 13.714  -0.239  21.543  1.00 22.01 ? 152 PHE   A HE1  1 
ATOM   2327 H  HE2  . PHE   A 1 152 ? 15.405  3.387   21.584  1.00 21.08 ? 152 PHE   A HE2  1 
ATOM   2328 H  HZ   . PHE   A 1 152 ? 14.854  1.454   20.451  1.00 19.85 ? 152 PHE   A HZ   1 
ATOM   2329 N  N    . GLY   A 1 153 ? 11.104  2.248   27.841  1.00 16.76 ? 153 GLY   A N    1 
ATOM   2330 C  CA   . GLY   A 1 153 ? 10.940  2.366   29.275  1.00 18.47 ? 153 GLY   A CA   1 
ATOM   2331 C  C    . GLY   A 1 153 ? 12.004  1.604   30.050  1.00 17.44 ? 153 GLY   A C    1 
ATOM   2332 O  O    . GLY   A 1 153 ? 12.778  0.821   29.496  1.00 17.65 ? 153 GLY   A O    1 
ATOM   2333 H  H    . GLY   A 1 153 ? 10.563  1.694   27.466  1.00 20.13 ? 153 GLY   A H    1 
ATOM   2334 H  HA2  . GLY   A 1 153 ? 10.987  3.301   29.529  1.00 22.19 ? 153 GLY   A HA2  1 
ATOM   2335 H  HA3  . GLY   A 1 153 ? 10.070  2.023   29.529  1.00 22.19 ? 153 GLY   A HA3  1 
ATOM   2336 N  N    . ASP   A 1 154 ? 12.045  1.853   31.362  1.00 20.18 ? 154 ASP   A N    1 
ATOM   2337 C  CA   . ASP   A 1 154 ? 12.936  1.108   32.237  1.00 20.76 ? 154 ASP   A CA   1 
ATOM   2338 C  C    . ASP   A 1 154 ? 12.269  -0.124  32.857  1.00 20.02 ? 154 ASP   A C    1 
ATOM   2339 O  O    . ASP   A 1 154 ? 12.885  -0.801  33.689  1.00 20.27 ? 154 ASP   A O    1 
ATOM   2340 C  CB   . ASP   A 1 154 ? 13.496  1.974   33.375  1.00 21.77 ? 154 ASP   A CB   1 
ATOM   2341 C  CG   . ASP   A 1 154 ? 14.738  2.742   32.952  1.00 21.95 ? 154 ASP   A CG   1 
ATOM   2342 O  OD1  . ASP   A 1 154 ? 15.534  2.193   32.173  1.00 20.70 ? 154 ASP   A OD1  1 
ATOM   2343 O  OD2  . ASP   A 1 154 ? 15.042  3.794   33.545  1.00 28.45 ? 154 ASP   A OD2  1 
ATOM   2344 H  H    . ASP   A 1 154 ? 11.568  2.446   31.763  1.00 24.24 ? 154 ASP   A H    1 
ATOM   2345 H  HA   . ASP   A 1 154 ? 13.688  0.793   31.713  1.00 24.94 ? 154 ASP   A HA   1 
ATOM   2346 H  HB2  . ASP   A 1 154 ? 12.822  2.617   33.646  1.00 26.14 ? 154 ASP   A HB2  1 
ATOM   2347 H  HB3  . ASP   A 1 154 ? 13.735  1.406   34.124  1.00 26.14 ? 154 ASP   A HB3  1 
ATOM   2348 N  N    . GLY   A 1 155 ? 11.045  -0.437  32.426  1.00 18.66 ? 155 GLY   A N    1 
ATOM   2349 C  CA   . GLY   A 1 155 ? 10.312  -1.603  32.949  1.00 19.44 ? 155 GLY   A CA   1 
ATOM   2350 C  C    . GLY   A 1 155 ? 9.918   -1.372  34.391  1.00 23.34 ? 155 GLY   A C    1 
ATOM   2351 O  O    . GLY   A 1 155 ? 10.097  -0.240  34.868  1.00 22.55 ? 155 GLY   A O    1 
ATOM   2352 H  H    . GLY   A 1 155 ? 10.612  0.007   31.830  1.00 22.41 ? 155 GLY   A H    1 
ATOM   2353 H  HA2  . GLY   A 1 155 ? 9.514   -1.751  32.420  1.00 23.35 ? 155 GLY   A HA2  1 
ATOM   2354 H  HA3  . GLY   A 1 155 ? 10.872  -2.393  32.900  1.00 23.35 ? 155 GLY   A HA3  1 
ATOM   2355 N  N    . ASP   A 1 156 ? 9.386   -2.394  35.059  1.00 20.18 ? 156 ASP   A N    1 
ATOM   2356 C  CA   . ASP   A 1 156 ? 8.980   -2.279  36.485  1.00 23.80 ? 156 ASP   A CA   1 
ATOM   2357 C  C    . ASP   A 1 156 ? 9.122   -3.649  37.156  1.00 27.54 ? 156 ASP   A C    1 
ATOM   2358 O  O    . ASP   A 1 156 ? 10.263  -4.109  37.277  1.00 25.45 ? 156 ASP   A O    1 
ATOM   2359 C  CB   . ASP   A 1 156 ? 7.602   -1.647  36.603  1.00 27.40 ? 156 ASP   A CB   1 
ATOM   2360 C  CG   . ASP   A 1 156 ? 7.173   -1.283  38.017  1.00 29.48 ? 156 ASP   A CG   1 
ATOM   2361 O  OD1  . ASP   A 1 156 ? 7.984   -1.476  38.946  1.00 35.49 ? 156 ASP   A OD1  1 
ATOM   2362 O  OD2  . ASP   A 1 156 ? 6.029   -0.819  38.181  1.00 37.01 ? 156 ASP   A OD2  1 
ATOM   2363 H  H    . ASP   A 1 156 ? 9.245   -3.171  34.719  1.00 24.24 ? 156 ASP   A H    1 
ATOM   2364 H  HA   . ASP   A 1 156 ? 9.603   -1.682  36.927  1.00 28.57 ? 156 ASP   A HA   1 
ATOM   2365 H  HB2  . ASP   A 1 156 ? 7.593   -0.831  36.078  1.00 32.90 ? 156 ASP   A HB2  1 
ATOM   2366 H  HB3  . ASP   A 1 156 ? 6.946   -2.267  36.248  1.00 32.90 ? 156 ASP   A HB3  1 
ATOM   2367 N  N    . THR   A 1 157 ? 8.025   -4.299  37.548  1.00 26.59 ? 157 THR   A N    1 
ATOM   2368 C  CA   . THR   A 1 157 ? 8.081   -5.570  38.298  1.00 28.41 ? 157 THR   A CA   1 
ATOM   2369 C  C    . THR   A 1 157 ? 8.122   -6.734  37.338  1.00 25.46 ? 157 THR   A C    1 
ATOM   2370 O  O    . THR   A 1 157 ? 8.584   -7.808  37.769  1.00 31.78 ? 157 THR   A O    1 
ATOM   2371 C  CB   . THR   A 1 157 ? 6.876   -5.674  39.234  1.00 28.83 ? 157 THR   A CB   1 
ATOM   2372 O  OG1  . THR   A 1 157 ? 5.761   -5.951  38.393  1.00 34.89 ? 157 THR   A OG1  1 
ATOM   2373 C  CG2  . THR   A 1 157 ? 6.637   -4.401  40.025  1.00 34.37 ? 157 THR   A CG2  1 
ATOM   2374 H  H    . THR   A 1 157 ? 7.224   -4.028  37.393  1.00 31.93 ? 157 THR   A H    1 
ATOM   2375 H  HA   . THR   A 1 157 ? 8.888   -5.590  38.836  1.00 34.11 ? 157 THR   A HA   1 
ATOM   2376 H  HB   . THR   A 1 157 ? 7.007   -6.407  39.855  1.00 34.61 ? 157 THR   A HB   1 
ATOM   2377 H  HG1  . THR   A 1 157 ? 5.063   -6.020  38.855  1.00 41.89 ? 157 THR   A HG1  1 
ATOM   2378 H  HG21 . THR   A 1 157 ? 5.946   -4.549  40.689  1.00 41.27 ? 157 THR   A HG21 1 
ATOM   2379 H  HG22 . THR   A 1 157 ? 7.454   -4.133  40.475  1.00 41.27 ? 157 THR   A HG22 1 
ATOM   2380 H  HG23 . THR   A 1 157 ? 6.355   -3.688  39.431  1.00 41.27 ? 157 THR   A HG23 1 
ATOM   2381 N  N    . MET   A 1 158 ? 7.689   -6.561  36.084  1.00 22.88 ? 158 MET   A N    1 
ATOM   2382 C  CA   . MET   A 1 158 ? 7.599   -7.671  35.145  1.00 24.04 ? 158 MET   A CA   1 
ATOM   2383 C  C    . MET   A 1 158 ? 8.731   -7.700  34.131  1.00 22.80 ? 158 MET   A C    1 
ATOM   2384 O  O    . MET   A 1 158 ? 9.051   -8.772  33.605  1.00 21.96 ? 158 MET   A O    1 
ATOM   2385 C  CB   . MET   A 1 158 ? 6.278   -7.598  34.373  1.00 30.69 ? 158 MET   A CB   1 
ATOM   2386 C  CG   . MET   A 1 158 ? 5.031   -7.677  35.218  1.00 39.17 ? 158 MET   A CG   1 
ATOM   2387 S  SD   . MET   A 1 158 ? 4.674   -9.357  35.737  1.00 42.44 ? 158 MET   A SD   1 
ATOM   2388 C  CE   . MET   A 1 158 ? 3.501   -9.771  34.442  1.00 38.34 ? 158 MET   A CE   1 
ATOM   2389 H  H    . MET   A 1 158 ? 7.441   -5.806  35.756  1.00 27.48 ? 158 MET   A H    1 
ATOM   2390 H  HA   . MET   A 1 158 ? 7.605   -8.503  35.643  1.00 28.87 ? 158 MET   A HA   1 
ATOM   2391 H  HB2  . MET   A 1 158 ? 6.250   -6.757  33.891  1.00 36.84 ? 158 MET   A HB2  1 
ATOM   2392 H  HB3  . MET   A 1 158 ? 6.250   -8.334  33.742  1.00 36.84 ? 158 MET   A HB3  1 
ATOM   2393 H  HG2  . MET   A 1 158 ? 5.148   -7.134  36.013  1.00 47.02 ? 158 MET   A HG2  1 
ATOM   2394 H  HG3  . MET   A 1 158 ? 4.276   -7.353  34.702  1.00 47.02 ? 158 MET   A HG3  1 
ATOM   2395 H  HE1  . MET   A 1 158 ? 3.131   -10.649 34.624  1.00 46.03 ? 158 MET   A HE1  1 
ATOM   2396 H  HE2  . MET   A 1 158 ? 2.793   -9.109  34.434  1.00 46.03 ? 158 MET   A HE2  1 
ATOM   2397 H  HE3  . MET   A 1 158 ? 3.961   -9.774  33.588  1.00 46.03 ? 158 MET   A HE3  1 
ATOM   2398 N  N    . MET   A 1 159 ? 9.335   -6.553  33.839  1.00 22.01 ? 159 MET   A N    1 
ATOM   2399 C  CA   . MET   A 1 159 ? 10.332  -6.433  32.787  1.00 19.42 ? 159 MET   A CA   1 
ATOM   2400 C  C    . MET   A 1 159 ? 11.501  -5.594  33.260  1.00 18.32 ? 159 MET   A C    1 
ATOM   2401 O  O    . MET   A 1 159 ? 11.315  -4.620  33.997  1.00 20.02 ? 159 MET   A O    1 
ATOM   2402 C  CB   . MET   A 1 159 ? 9.732   -5.761  31.552  1.00 19.87 ? 159 MET   A CB   1 
ATOM   2403 C  CG   . MET   A 1 159 ? 8.590   -6.518  30.956  1.00 23.16 ? 159 MET   A CG   1 
ATOM   2404 S  SD   . MET   A 1 159 ? 7.838   -5.649  29.588  1.00 24.97 ? 159 MET   A SD   1 
ATOM   2405 C  CE   . MET   A 1 159 ? 6.226   -6.390  29.660  1.00 25.61 ? 159 MET   A CE   1 
ATOM   2406 H  H    . MET   A 1 159 ? 9.179   -5.813  34.248  1.00 26.43 ? 159 MET   A H    1 
ATOM   2407 H  HA   . MET   A 1 159 ? 10.647  -7.315  32.536  1.00 23.32 ? 159 MET   A HA   1 
ATOM   2408 H  HB2  . MET   A 1 159 ? 9.408   -4.881  31.800  1.00 23.86 ? 159 MET   A HB2  1 
ATOM   2409 H  HB3  . MET   A 1 159 ? 10.421  -5.679  30.874  1.00 23.86 ? 159 MET   A HB3  1 
ATOM   2410 H  HG2  . MET   A 1 159 ? 8.913   -7.372  30.629  1.00 27.81 ? 159 MET   A HG2  1 
ATOM   2411 H  HG3  . MET   A 1 159 ? 7.913   -6.656  31.636  1.00 27.81 ? 159 MET   A HG3  1 
ATOM   2412 H  HE1  . MET   A 1 159 ? 5.602   -5.840  29.164  1.00 30.76 ? 159 MET   A HE1  1 
ATOM   2413 H  HE2  . MET   A 1 159 ? 6.268   -7.277  29.271  1.00 30.76 ? 159 MET   A HE2  1 
ATOM   2414 H  HE3  . MET   A 1 159 ? 5.945   -6.447  30.587  1.00 30.76 ? 159 MET   A HE3  1 
ATOM   2415 N  N    . TYR   A 1 160 ? 12.696  -5.982  32.803  1.00 19.05 ? 160 TYR   A N    1 
ATOM   2416 C  CA   . TYR   A 1 160 ? 13.885  -5.169  32.920  1.00 20.77 ? 160 TYR   A CA   1 
ATOM   2417 C  C    . TYR   A 1 160 ? 13.747  -4.013  31.927  1.00 18.24 ? 160 TYR   A C    1 
ATOM   2418 O  O    . TYR   A 1 160 ? 12.851  -4.017  31.076  1.00 18.55 ? 160 TYR   A O    1 
ATOM   2419 C  CB   . TYR   A 1 160 ? 15.147  -5.977  32.579  1.00 18.81 ? 160 TYR   A CB   1 
ATOM   2420 C  CG   . TYR   A 1 160 ? 15.460  -7.028  33.616  1.00 18.79 ? 160 TYR   A CG   1 
ATOM   2421 C  CD1  . TYR   A 1 160 ? 16.114  -6.709  34.791  1.00 21.78 ? 160 TYR   A CD1  1 
ATOM   2422 C  CD2  . TYR   A 1 160 ? 15.120  -8.358  33.397  1.00 19.21 ? 160 TYR   A CD2  1 
ATOM   2423 C  CE1  . TYR   A 1 160 ? 16.371  -7.669  35.751  1.00 24.38 ? 160 TYR   A CE1  1 
ATOM   2424 C  CE2  . TYR   A 1 160 ? 15.395  -9.329  34.335  1.00 19.76 ? 160 TYR   A CE2  1 
ATOM   2425 C  CZ   . TYR   A 1 160 ? 16.023  -8.980  35.511  1.00 22.50 ? 160 TYR   A CZ   1 
ATOM   2426 O  OH   . TYR   A 1 160 ? 16.292  -9.939  36.455  1.00 26.05 ? 160 TYR   A OH   1 
ATOM   2427 H  H    . TYR   A 1 160 ? 12.835  -6.735  32.412  1.00 22.88 ? 160 TYR   A H    1 
ATOM   2428 H  HA   . TYR   A 1 160 ? 13.963  -4.814  33.819  1.00 24.95 ? 160 TYR   A HA   1 
ATOM   2429 H  HB2  . TYR   A 1 160 ? 15.012  -6.426  31.730  1.00 22.59 ? 160 TYR   A HB2  1 
ATOM   2430 H  HB3  . TYR   A 1 160 ? 15.907  -5.380  32.519  1.00 22.59 ? 160 TYR   A HB3  1 
ATOM   2431 H  HD1  . TYR   A 1 160 ? 16.340  -5.823  34.960  1.00 26.16 ? 160 TYR   A HD1  1 
ATOM   2432 H  HD2  . TYR   A 1 160 ? 14.688  -8.595  32.608  1.00 23.06 ? 160 TYR   A HD2  1 
ATOM   2433 H  HE1  . TYR   A 1 160 ? 16.806  -7.437  36.540  1.00 29.28 ? 160 TYR   A HE1  1 
ATOM   2434 H  HE2  . TYR   A 1 160 ? 15.150  -10.213 34.179  1.00 23.73 ? 160 TYR   A HE2  1 
ATOM   2435 H  HH   . TYR   A 1 160 ? 16.035  -10.691 36.182  1.00 31.28 ? 160 TYR   A HH   1 
ATOM   2436 N  N    . PRO   A 1 161 ? 14.640  -3.027  31.976  1.00 17.49 ? 161 PRO   A N    1 
ATOM   2437 C  CA   . PRO   A 1 161 ? 14.618  -1.976  30.946  1.00 20.37 ? 161 PRO   A CA   1 
ATOM   2438 C  C    . PRO   A 1 161 ? 14.623  -2.580  29.549  1.00 17.88 ? 161 PRO   A C    1 
ATOM   2439 O  O    . PRO   A 1 161 ? 15.366  -3.518  29.255  1.00 17.92 ? 161 PRO   A O    1 
ATOM   2440 C  CB   . PRO   A 1 161 ? 15.886  -1.169  31.241  1.00 17.18 ? 161 PRO   A CB   1 
ATOM   2441 C  CG   . PRO   A 1 161 ? 16.012  -1.289  32.756  1.00 18.13 ? 161 PRO   A CG   1 
ATOM   2442 C  CD   . PRO   A 1 161 ? 15.604  -2.725  33.056  1.00 17.58 ? 161 PRO   A CD   1 
ATOM   2443 H  HA   . PRO   A 1 161 ? 13.839  -1.410  31.052  1.00 24.46 ? 161 PRO   A HA   1 
ATOM   2444 H  HB2  . PRO   A 1 161 ? 16.648  -1.569  30.793  1.00 20.64 ? 161 PRO   A HB2  1 
ATOM   2445 H  HB3  . PRO   A 1 161 ? 15.764  -0.245  30.972  1.00 20.64 ? 161 PRO   A HB3  1 
ATOM   2446 H  HG2  . PRO   A 1 161 ? 16.930  -1.127  33.024  1.00 21.77 ? 161 PRO   A HG2  1 
ATOM   2447 H  HG3  . PRO   A 1 161 ? 15.410  -0.662  33.187  1.00 21.77 ? 161 PRO   A HG3  1 
ATOM   2448 H  HD2  . PRO   A 1 161 ? 16.375  -3.310  33.002  1.00 21.11 ? 161 PRO   A HD2  1 
ATOM   2449 H  HD3  . PRO   A 1 161 ? 15.172  -2.781  33.923  1.00 21.11 ? 161 PRO   A HD3  1 
ATOM   2450 N  N    . LEU   A 1 162 ? 13.752  -2.051  28.694  1.00 16.39 ? 162 LEU   A N    1 
ATOM   2451 C  CA   . LEU   A 1 162 ? 13.441  -2.673  27.406  1.00 16.14 ? 162 LEU   A CA   1 
ATOM   2452 C  C    . LEU   A 1 162 ? 14.380  -2.150  26.320  1.00 18.83 ? 162 LEU   A C    1 
ATOM   2453 O  O    . LEU   A 1 162 ? 13.968  -1.593  25.300  1.00 22.45 ? 162 LEU   A O    1 
ATOM   2454 C  CB   . LEU   A 1 162 ? 11.984  -2.415  27.052  1.00 17.53 ? 162 LEU   A CB   1 
ATOM   2455 C  CG   . LEU   A 1 162 ? 10.912  -3.116  27.881  1.00 17.96 ? 162 LEU   A CG   1 
ATOM   2456 C  CD1  . LEU   A 1 162 ? 10.520  -2.271  29.076  1.00 18.85 ? 162 LEU   A CD1  1 
ATOM   2457 C  CD2  . LEU   A 1 162 ? 9.703   -3.413  26.996  1.00 22.72 ? 162 LEU   A CD2  1 
ATOM   2458 H  H    . LEU   A 1 162 ? 13.321  -1.321  28.838  1.00 19.68 ? 162 LEU   A H    1 
ATOM   2459 H  HA   . LEU   A 1 162 ? 13.568  -3.632  27.478  1.00 19.39 ? 162 LEU   A HA   1 
ATOM   2460 H  HB2  . LEU   A 1 162 ? 11.823  -1.462  27.129  1.00 21.05 ? 162 LEU   A HB2  1 
ATOM   2461 H  HB3  . LEU   A 1 162 ? 11.849  -2.685  26.130  1.00 21.05 ? 162 LEU   A HB3  1 
ATOM   2462 H  HG   . LEU   A 1 162 ? 11.262  -3.959  28.208  1.00 21.57 ? 162 LEU   A HG   1 
ATOM   2463 H  HD11 . LEU   A 1 162 ? 9.836   -2.738  29.581  1.00 22.64 ? 162 LEU   A HD11 1 
ATOM   2464 H  HD12 . LEU   A 1 162 ? 11.302  -2.128  29.632  1.00 22.64 ? 162 LEU   A HD12 1 
ATOM   2465 H  HD13 . LEU   A 1 162 ? 10.177  -1.420  28.762  1.00 22.64 ? 162 LEU   A HD13 1 
ATOM   2466 H  HD21 . LEU   A 1 162 ? 9.007   -3.817  27.538  1.00 27.28 ? 162 LEU   A HD21 1 
ATOM   2467 H  HD22 . LEU   A 1 162 ? 9.382   -2.582  26.611  1.00 27.28 ? 162 LEU   A HD22 1 
ATOM   2468 H  HD23 . LEU   A 1 162 ? 9.970   -4.023  26.291  1.00 27.28 ? 162 LEU   A HD23 1 
ATOM   2469 N  N    . VAL   A 1 163 ? 15.671  -2.338  26.559  1.00 17.57 ? 163 VAL   A N    1 
ATOM   2470 C  CA   . VAL   A 1 163 ? 16.715  -1.953  25.626  1.00 19.47 ? 163 VAL   A CA   1 
ATOM   2471 C  C    . VAL   A 1 163 ? 17.503  -3.211  25.334  1.00 22.19 ? 163 VAL   A C    1 
ATOM   2472 O  O    . VAL   A 1 163 ? 18.230  -3.714  26.202  1.00 22.17 ? 163 VAL   A O    1 
ATOM   2473 C  CB   . VAL   A 1 163 ? 17.621  -0.854  26.186  1.00 19.03 ? 163 VAL   A CB   1 
ATOM   2474 C  CG1  . VAL   A 1 163 ? 18.668  -0.467  25.164  1.00 22.50 ? 163 VAL   A CG1  1 
ATOM   2475 C  CG2  . VAL   A 1 163 ? 16.806  0.360   26.569  1.00 24.73 ? 163 VAL   A CG2  1 
ATOM   2476 H  H    . VAL   A 1 163 ? 15.974  -2.699  27.278  1.00 21.11 ? 163 VAL   A H    1 
ATOM   2477 H  HA   . VAL   A 1 163 ? 16.319  -1.637  24.799  1.00 23.38 ? 163 VAL   A HA   1 
ATOM   2478 H  HB   . VAL   A 1 163 ? 18.073  -1.182  26.979  1.00 22.85 ? 163 VAL   A HB   1 
ATOM   2479 H  HG11 . VAL   A 1 163 ? 19.133  0.326   25.475  1.00 27.02 ? 163 VAL   A HG11 1 
ATOM   2480 H  HG12 . VAL   A 1 163 ? 19.297  -1.198  25.060  1.00 27.02 ? 163 VAL   A HG12 1 
ATOM   2481 H  HG13 . VAL   A 1 163 ? 18.230  -0.282  24.319  1.00 27.02 ? 163 VAL   A HG13 1 
ATOM   2482 H  HG21 . VAL   A 1 163 ? 17.406  1.060   26.872  1.00 29.70 ? 163 VAL   A HG21 1 
ATOM   2483 H  HG22 . VAL   A 1 163 ? 16.308  0.663   25.793  1.00 29.70 ? 163 VAL   A HG22 1 
ATOM   2484 H  HG23 . VAL   A 1 163 ? 16.194  0.118   27.281  1.00 29.70 ? 163 VAL   A HG23 1 
ATOM   2485 N  N    . SER   A 1 164 ? 17.317  -3.753  24.144  1.00 21.03 ? 164 SER   A N    1 
ATOM   2486 C  CA   . SER   A 1 164 ? 18.101  -4.879  23.686  1.00 18.63 ? 164 SER   A CA   1 
ATOM   2487 C  C    . SER   A 1 164 ? 18.169  -4.765  22.174  1.00 17.99 ? 164 SER   A C    1 
ATOM   2488 O  O    . SER   A 1 164 ? 17.453  -3.960  21.564  1.00 18.45 ? 164 SER   A O    1 
ATOM   2489 C  CB   . SER   A 1 164 ? 17.484  -6.221  24.068  1.00 18.38 ? 164 SER   A CB   1 
ATOM   2490 O  OG   . SER   A 1 164 ? 16.218  -6.339  23.464  1.00 18.74 ? 164 SER   A OG   1 
ATOM   2491 H  H    . SER   A 1 164 ? 16.732  -3.481  23.575  1.00 25.25 ? 164 SER   A H    1 
ATOM   2492 H  HA   . SER   A 1 164 ? 18.999  -4.829  24.048  1.00 22.37 ? 164 SER   A HA   1 
ATOM   2493 H  HB2  . SER   A 1 164 ? 18.057  -6.938  23.755  1.00 22.07 ? 164 SER   A HB2  1 
ATOM   2494 H  HB3  . SER   A 1 164 ? 17.385  -6.266  25.032  1.00 22.07 ? 164 SER   A HB3  1 
ATOM   2495 H  HG   . SER   A 1 164 ? 15.870  -7.075  23.669  1.00 22.51 ? 164 SER   A HG   1 
ATOM   2496 N  N    . LEU   A 1 165 ? 18.997  -5.610  21.566  1.00 17.30 ? 165 LEU   A N    1 
ATOM   2497 C  CA   . LEU   A 1 165 ? 19.051  -5.637  20.112  1.00 17.95 ? 165 LEU   A CA   1 
ATOM   2498 C  C    . LEU   A 1 165 ? 17.677  -5.912  19.525  1.00 16.23 ? 165 LEU   A C    1 
ATOM   2499 O  O    . LEU   A 1 165 ? 17.264  -5.281  18.545  1.00 17.82 ? 165 LEU   A O    1 
ATOM   2500 C  CB   . LEU   A 1 165 ? 20.028  -6.695  19.620  1.00 19.03 ? 165 LEU   A CB   1 
ATOM   2501 C  CG   . LEU   A 1 165 ? 21.507  -6.422  19.848  1.00 23.24 ? 165 LEU   A CG   1 
ATOM   2502 C  CD1  . LEU   A 1 165 ? 22.293  -7.592  19.260  1.00 26.54 ? 165 LEU   A CD1  1 
ATOM   2503 C  CD2  . LEU   A 1 165 ? 21.924  -5.112  19.228  1.00 30.53 ? 165 LEU   A CD2  1 
ATOM   2504 H  H    . LEU   A 1 165 ? 19.524  -6.163  21.961  1.00 20.78 ? 165 LEU   A H    1 
ATOM   2505 H  HA   . LEU   A 1 165 ? 19.343  -4.771  19.789  1.00 21.55 ? 165 LEU   A HA   1 
ATOM   2506 H  HB2  . LEU   A 1 165 ? 19.819  -7.530  20.067  1.00 22.86 ? 165 LEU   A HB2  1 
ATOM   2507 H  HB3  . LEU   A 1 165 ? 19.901  -6.803  18.664  1.00 22.86 ? 165 LEU   A HB3  1 
ATOM   2508 H  HG   . LEU   A 1 165 ? 21.661  -6.378  20.799  1.00 27.91 ? 165 LEU   A HG   1 
ATOM   2509 H  HD11 . LEU   A 1 165 ? 23.240  -7.442  19.409  1.00 31.86 ? 165 LEU   A HD11 1 
ATOM   2510 H  HD12 . LEU   A 1 165 ? 22.015  -8.411  19.699  1.00 31.86 ? 165 LEU   A HD12 1 
ATOM   2511 H  HD13 . LEU   A 1 165 ? 22.111  -7.648  18.309  1.00 31.86 ? 165 LEU   A HD13 1 
ATOM   2512 H  HD21 . LEU   A 1 165 ? 22.892  -5.050  19.241  1.00 36.65 ? 165 LEU   A HD21 1 
ATOM   2513 H  HD22 . LEU   A 1 165 ? 21.600  -5.077  18.314  1.00 36.65 ? 165 LEU   A HD22 1 
ATOM   2514 H  HD23 . LEU   A 1 165 ? 21.538  -4.390  19.746  1.00 36.65 ? 165 LEU   A HD23 1 
ATOM   2515 N  N    . GLY   A 1 166 ? 16.969  -6.889  20.098  1.00 16.34 ? 166 GLY   A N    1 
ATOM   2516 C  CA   . GLY   A 1 166 ? 15.684  -7.279  19.548  1.00 17.89 ? 166 GLY   A CA   1 
ATOM   2517 C  C    . GLY   A 1 166 ? 14.638  -6.196  19.707  1.00 17.47 ? 166 GLY   A C    1 
ATOM   2518 O  O    . GLY   A 1 166 ? 13.910  -5.876  18.760  1.00 17.79 ? 166 GLY   A O    1 
ATOM   2519 H  H    . GLY   A 1 166 ? 17.211  -7.331  20.795  1.00 19.63 ? 166 GLY   A H    1 
ATOM   2520 H  HA2  . GLY   A 1 166 ? 15.783  -7.475  18.603  1.00 21.48 ? 166 GLY   A HA2  1 
ATOM   2521 H  HA3  . GLY   A 1 166 ? 15.369  -8.079  19.997  1.00 21.48 ? 166 GLY   A HA3  1 
ATOM   2522 N  N    . VAL   A 1 167 ? 14.545  -5.606  20.902  1.00 15.91 ? 167 VAL   A N    1 
ATOM   2523 C  CA   . VAL   A 1 167 ? 13.542  -4.570  21.101  1.00 17.16 ? 167 VAL   A CA   1 
ATOM   2524 C  C    . VAL   A 1 167 ? 13.886  -3.354  20.253  1.00 16.35 ? 167 VAL   A C    1 
ATOM   2525 O  O    . VAL   A 1 167 ? 13.015  -2.760  19.613  1.00 16.16 ? 167 VAL   A O    1 
ATOM   2526 C  CB   . VAL   A 1 167 ? 13.396  -4.204  22.590  1.00 16.45 ? 167 VAL   A CB   1 
ATOM   2527 C  CG1  . VAL   A 1 167 ? 12.477  -2.991  22.726  1.00 17.71 ? 167 VAL   A CG1  1 
ATOM   2528 C  CG2  . VAL   A 1 167 ? 12.860  -5.392  23.380  1.00 19.17 ? 167 VAL   A CG2  1 
ATOM   2529 H  H    . VAL   A 1 167 ? 15.034  -5.782  21.587  1.00 19.12 ? 167 VAL   A H    1 
ATOM   2530 H  HA   . VAL   A 1 167 ? 12.685  -4.907  20.797  1.00 20.62 ? 167 VAL   A HA   1 
ATOM   2531 H  HB   . VAL   A 1 167 ? 14.266  -3.968  22.948  1.00 19.76 ? 167 VAL   A HB   1 
ATOM   2532 H  HG11 . VAL   A 1 167 ? 12.160  -2.939  23.641  1.00 21.27 ? 167 VAL   A HG11 1 
ATOM   2533 H  HG12 . VAL   A 1 167 ? 12.973  -2.188  22.504  1.00 21.27 ? 167 VAL   A HG12 1 
ATOM   2534 H  HG13 . VAL   A 1 167 ? 11.725  -3.096  22.123  1.00 21.27 ? 167 VAL   A HG13 1 
ATOM   2535 H  HG21 . VAL   A 1 167 ? 12.769  -5.136  24.311  1.00 23.03 ? 167 VAL   A HG21 1 
ATOM   2536 H  HG22 . VAL   A 1 167 ? 11.996  -5.646  23.020  1.00 23.03 ? 167 VAL   A HG22 1 
ATOM   2537 H  HG23 . VAL   A 1 167 ? 13.483  -6.131  23.299  1.00 23.03 ? 167 VAL   A HG23 1 
ATOM   2538 N  N    . GLY   A 1 168 ? 15.170  -2.980  20.206  1.00 16.15 ? 168 GLY   A N    1 
ATOM   2539 C  CA   . GLY   A 1 168 ? 15.576  -1.877  19.351  1.00 15.21 ? 168 GLY   A CA   1 
ATOM   2540 C  C    . GLY   A 1 168 ? 15.323  -2.155  17.883  1.00 16.18 ? 168 GLY   A C    1 
ATOM   2541 O  O    . GLY   A 1 168 ? 14.850  -1.282  17.150  1.00 15.95 ? 168 GLY   A O    1 
ATOM   2542 H  H    . GLY   A 1 168 ? 15.808  -3.345  20.652  1.00 19.40 ? 168 GLY   A H    1 
ATOM   2543 H  HA2  . GLY   A 1 168 ? 15.086  -1.078  19.601  1.00 18.27 ? 168 GLY   A HA2  1 
ATOM   2544 H  HA3  . GLY   A 1 168 ? 16.523  -1.707  19.472  1.00 18.27 ? 168 GLY   A HA3  1 
ATOM   2545 N  N    . GLY   A 1 169 ? 15.640  -3.368  17.426  1.00 14.37 ? 169 GLY   A N    1 
ATOM   2546 C  CA   . GLY   A 1 169 ? 15.384  -3.707  16.035  1.00 14.85 ? 169 GLY   A CA   1 
ATOM   2547 C  C    . GLY   A 1 169 ? 13.911  -3.650  15.693  1.00 14.30 ? 169 GLY   A C    1 
ATOM   2548 O  O    . GLY   A 1 169 ? 13.534  -3.201  14.605  1.00 15.21 ? 169 GLY   A O    1 
ATOM   2549 H  H    . GLY   A 1 169 ? 15.996  -3.996  17.893  1.00 17.27 ? 169 GLY   A H    1 
ATOM   2550 H  HA2  . GLY   A 1 169 ? 15.858  -3.088  15.458  1.00 17.84 ? 169 GLY   A HA2  1 
ATOM   2551 H  HA3  . GLY   A 1 169 ? 15.707  -4.604  15.856  1.00 17.84 ? 169 GLY   A HA3  1 
ATOM   2552 N  N    . HIS   A 1 170 ? 13.064  -4.112  16.607  1.00 12.41 ? 170 HIS   A N    1 
ATOM   2553 C  CA   . HIS   A 1 170 ? 11.618  -4.043  16.417  1.00 13.23 ? 170 HIS   A CA   1 
ATOM   2554 C  C    . HIS   A 1 170 ? 11.155  -2.597  16.269  1.00 14.27 ? 170 HIS   A C    1 
ATOM   2555 O  O    . HIS   A 1 170 ? 10.420  -2.265  15.332  1.00 15.13 ? 170 HIS   A O    1 
ATOM   2556 C  CB   . HIS   A 1 170 ? 10.953  -4.720  17.602  1.00 14.60 ? 170 HIS   A CB   1 
ATOM   2557 C  CG   . HIS   A 1 170 ? 9.470   -4.776  17.538  1.00 13.54 ? 170 HIS   A CG   1 
ATOM   2558 N  ND1  . HIS   A 1 170 ? 8.764   -5.935  17.283  1.00 13.04 ? 170 HIS   A ND1  1 
ATOM   2559 C  CD2  . HIS   A 1 170 ? 8.561   -3.790  17.628  1.00 13.32 ? 170 HIS   A CD2  1 
ATOM   2560 C  CE1  . HIS   A 1 170 ? 7.476   -5.665  17.293  1.00 12.13 ? 170 HIS   A CE1  1 
ATOM   2561 N  NE2  . HIS   A 1 170 ? 7.334   -4.372  17.486  1.00 15.17 ? 170 HIS   A NE2  1 
ATOM   2562 H  H    . HIS   A 1 170 ? 13.302  -4.472  17.351  1.00 14.91 ? 170 HIS   A H    1 
ATOM   2563 H  HA   . HIS   A 1 170 ? 11.375  -4.526  15.612  1.00 15.89 ? 170 HIS   A HA   1 
ATOM   2564 H  HB2  . HIS   A 1 170 ? 11.278  -5.632  17.659  1.00 17.53 ? 170 HIS   A HB2  1 
ATOM   2565 H  HB3  . HIS   A 1 170 ? 11.193  -4.237  18.408  1.00 17.53 ? 170 HIS   A HB3  1 
ATOM   2566 H  HD1  . HIS   A 1 170 ? 9.108   -6.717  17.187  1.00 15.67 ? 170 HIS   A HD1  1 
ATOM   2567 H  HD2  . HIS   A 1 170 ? 8.733   -2.891  17.794  1.00 16.00 ? 170 HIS   A HD2  1 
ATOM   2568 H  HE1  . HIS   A 1 170 ? 6.789   -6.275  17.149  1.00 14.57 ? 170 HIS   A HE1  1 
ATOM   2569 N  N    . GLU   A 1 171 ? 11.614  -1.708  17.159  1.00 14.79 ? 171 GLU   A N    1 
ATOM   2570 C  CA   . GLU   A 1 171 ? 11.107  -0.339  17.130  1.00 14.14 ? 171 GLU   A CA   1 
ATOM   2571 C  C    . GLU   A 1 171 ? 11.647  0.434   15.927  1.00 15.16 ? 171 GLU   A C    1 
ATOM   2572 O  O    . GLU   A 1 171 ? 10.887  1.134   15.247  1.00 16.69 ? 171 GLU   A O    1 
ATOM   2573 C  CB   . GLU   A 1 171 ? 11.441  0.383   18.437  1.00 16.68 ? 171 GLU   A CB   1 
ATOM   2574 C  CG   . GLU   A 1 171 ? 10.744  -0.203  19.666  1.00 16.55 ? 171 GLU   A CG   1 
ATOM   2575 C  CD   . GLU   A 1 171 ? 9.220   -0.219  19.572  1.00 16.47 ? 171 GLU   A CD   1 
ATOM   2576 O  OE1  . GLU   A 1 171 ? 8.648   0.447   18.684  1.00 17.37 ? 171 GLU   A OE1  1 
ATOM   2577 O  OE2  . GLU   A 1 171 ? 8.597   -0.925  20.390  1.00 17.32 ? 171 GLU   A OE2  1 
ATOM   2578 H  H    . GLU   A 1 171 ? 12.199  -1.869  17.768  1.00 17.77 ? 171 GLU   A H    1 
ATOM   2579 H  HA   . GLU   A 1 171 ? 10.142  -0.371  17.042  1.00 16.99 ? 171 GLU   A HA   1 
ATOM   2580 H  HB2  . GLU   A 1 171 ? 12.398  0.331   18.586  1.00 20.04 ? 171 GLU   A HB2  1 
ATOM   2581 H  HB3  . GLU   A 1 171 ? 11.171  1.311   18.358  1.00 20.04 ? 171 GLU   A HB3  1 
ATOM   2582 H  HG2  . GLU   A 1 171 ? 11.042  -1.118  19.786  1.00 19.88 ? 171 GLU   A HG2  1 
ATOM   2583 H  HG3  . GLU   A 1 171 ? 10.986  0.325   20.443  1.00 19.88 ? 171 GLU   A HG3  1 
ATOM   2584 N  N    . VAL   A 1 172 ? 12.951  0.332   15.644  1.00 14.83 ? 172 VAL   A N    1 
ATOM   2585 C  CA   . VAL   A 1 172 ? 13.488  1.003   14.458  1.00 14.99 ? 172 VAL   A CA   1 
ATOM   2586 C  C    . VAL   A 1 172 ? 12.749  0.541   13.211  1.00 15.95 ? 172 VAL   A C    1 
ATOM   2587 O  O    . VAL   A 1 172 ? 12.461  1.331   12.301  1.00 16.65 ? 172 VAL   A O    1 
ATOM   2588 C  CB   . VAL   A 1 172 ? 15.004  0.760   14.318  1.00 15.01 ? 172 VAL   A CB   1 
ATOM   2589 C  CG1  . VAL   A 1 172 ? 15.481  1.273   12.949  1.00 19.72 ? 172 VAL   A CG1  1 
ATOM   2590 C  CG2  . VAL   A 1 172 ? 15.740  1.433   15.449  1.00 18.85 ? 172 VAL   A CG2  1 
ATOM   2591 H  H    . VAL   A 1 172 ? 13.528  -0.106  16.108  1.00 17.82 ? 172 VAL   A H    1 
ATOM   2592 H  HA   . VAL   A 1 172 ? 13.348  1.959   14.549  1.00 18.01 ? 172 VAL   A HA   1 
ATOM   2593 H  HB   . VAL   A 1 172 ? 15.181  -0.193  14.364  1.00 18.03 ? 172 VAL   A HB   1 
ATOM   2594 H  HG11 . VAL   A 1 172 ? 16.441  1.405   12.982  1.00 23.68 ? 172 VAL   A HG11 1 
ATOM   2595 H  HG12 . VAL   A 1 172 ? 15.262  0.618   12.268  1.00 23.68 ? 172 VAL   A HG12 1 
ATOM   2596 H  HG13 . VAL   A 1 172 ? 15.040  2.115   12.756  1.00 23.68 ? 172 VAL   A HG13 1 
ATOM   2597 H  HG21 . VAL   A 1 172 ? 16.687  1.240   15.368  1.00 22.64 ? 172 VAL   A HG21 1 
ATOM   2598 H  HG22 . VAL   A 1 172 ? 15.591  2.389   15.394  1.00 22.64 ? 172 VAL   A HG22 1 
ATOM   2599 H  HG23 . VAL   A 1 172 ? 15.404  1.092   16.293  1.00 22.64 ? 172 VAL   A HG23 1 
ATOM   2600 N  N    . SER   A 1 173 ? 12.432  -0.749  13.143  1.00 14.53 ? 173 SER   A N    1 
ATOM   2601 C  CA   . SER   A 1 173 ? 11.822  -1.292  11.943  1.00 13.58 ? 173 SER   A CA   1 
ATOM   2602 C  C    . SER   A 1 173 ? 10.348  -0.918  11.792  1.00 15.02 ? 173 SER   A C    1 
ATOM   2603 O  O    . SER   A 1 173 ? 9.826   -1.025  10.682  1.00 15.53 ? 173 SER   A O    1 
ATOM   2604 C  CB   . SER   A 1 173 ? 12.035  -2.805  11.914  1.00 15.40 ? 173 SER   A CB   1 
ATOM   2605 O  OG   . SER   A 1 173 ? 13.430  -3.073  11.868  1.00 17.27 ? 173 SER   A OG   1 
ATOM   2606 H  H    . SER   A 1 173 ? 12.559  -1.322  13.772  1.00 17.45 ? 173 SER   A H    1 
ATOM   2607 H  HA   . SER   A 1 173 ? 12.288  -0.924  11.176  1.00 16.31 ? 173 SER   A HA   1 
ATOM   2608 H  HB2  . SER   A 1 173 ? 11.658  -3.199  12.716  1.00 18.50 ? 173 SER   A HB2  1 
ATOM   2609 H  HB3  . SER   A 1 173 ? 11.610  -3.175  11.124  1.00 18.50 ? 173 SER   A HB3  1 
ATOM   2610 H  HG   . SER   A 1 173 ? 13.806  -2.758  12.550  1.00 20.74 ? 173 SER   A HG   1 
ATOM   2611 N  N    . HIS   A 1 174 ? 9.675   -0.449  12.847  1.00 16.27 ? 174 HIS   A N    1 
ATOM   2612 C  CA   . HIS   A 1 174 ? 8.378   0.196   12.626  1.00 15.75 ? 174 HIS   A CA   1 
ATOM   2613 C  C    . HIS   A 1 174 ? 8.571   1.425   11.740  1.00 16.23 ? 174 HIS   A C    1 
ATOM   2614 O  O    . HIS   A 1 174 ? 7.749   1.718   10.863  1.00 16.97 ? 174 HIS   A O    1 
ATOM   2615 C  CB   . HIS   A 1 174 ? 7.763   0.603   13.958  1.00 16.17 ? 174 HIS   A CB   1 
ATOM   2616 C  CG   . HIS   A 1 174 ? 6.935   -0.461  14.590  1.00 15.23 ? 174 HIS   A CG   1 
ATOM   2617 N  ND1  . HIS   A 1 174 ? 5.992   -1.207  13.914  1.00 14.56 ? 174 HIS   A ND1  1 
ATOM   2618 C  CD2  . HIS   A 1 174 ? 6.937   -0.913  15.860  1.00 14.32 ? 174 HIS   A CD2  1 
ATOM   2619 C  CE1  . HIS   A 1 174 ? 5.434   -2.064  14.745  1.00 17.16 ? 174 HIS   A CE1  1 
ATOM   2620 N  NE2  . HIS   A 1 174 ? 5.988   -1.898  15.930  1.00 13.96 ? 174 HIS   A NE2  1 
ATOM   2621 H  H    . HIS   A 1 174 ? 9.934   -0.489  13.666  1.00 19.55 ? 174 HIS   A H    1 
ATOM   2622 H  HA   . HIS   A 1 174 ? 7.777   -0.420  12.178  1.00 18.92 ? 174 HIS   A HA   1 
ATOM   2623 H  HB2  . HIS   A 1 174 ? 8.476   0.830   14.575  1.00 19.42 ? 174 HIS   A HB2  1 
ATOM   2624 H  HB3  . HIS   A 1 174 ? 7.194   1.375   13.816  1.00 19.42 ? 174 HIS   A HB3  1 
ATOM   2625 H  HD1  . HIS   A 1 174 ? 5.792   -1.120  13.082  1.00 17.49 ? 174 HIS   A HD1  1 
ATOM   2626 H  HD2  . HIS   A 1 174 ? 7.467   -0.603  16.558  1.00 17.20 ? 174 HIS   A HD2  1 
ATOM   2627 H  HE1  . HIS   A 1 174 ? 4.767   -2.676  14.534  1.00 20.62 ? 174 HIS   A HE1  1 
ATOM   2628 N  N    . GLY   A 1 175 ? 9.675   2.147   11.953  1.00 17.39 ? 175 GLY   A N    1 
ATOM   2629 C  CA   . GLY   A 1 175 ? 9.998   3.271   11.094  1.00 16.00 ? 175 GLY   A CA   1 
ATOM   2630 C  C    . GLY   A 1 175 ? 10.365  2.845   9.689   1.00 17.37 ? 175 GLY   A C    1 
ATOM   2631 O  O    . GLY   A 1 175 ? 9.939   3.466   8.712   1.00 18.61 ? 175 GLY   A O    1 
ATOM   2632 H  H    . GLY   A 1 175 ? 10.243  2.003   12.583  1.00 20.89 ? 175 GLY   A H    1 
ATOM   2633 H  HA2  . GLY   A 1 175 ? 9.232   3.863   11.040  1.00 19.21 ? 175 GLY   A HA2  1 
ATOM   2634 H  HA3  . GLY   A 1 175 ? 10.743  3.764   11.471  1.00 19.21 ? 175 GLY   A HA3  1 
ATOM   2635 N  N    . PHE   A 1 176 ? 11.158  1.779   9.559   1.00 15.38 ? 176 PHE   A N    1 
ATOM   2636 C  CA   . PHE   A 1 176 ? 11.481  1.277   8.226   1.00 16.34 ? 176 PHE   A CA   1 
ATOM   2637 C  C    . PHE   A 1 176 ? 10.203  0.950   7.459   1.00 15.90 ? 176 PHE   A C    1 
ATOM   2638 O  O    . PHE   A 1 176 ? 10.038  1.354   6.305   1.00 16.64 ? 176 PHE   A O    1 
ATOM   2639 C  CB   . PHE   A 1 176 ? 12.403  0.058   8.322   1.00 18.43 ? 176 PHE   A CB   1 
ATOM   2640 C  CG   . PHE   A 1 176 ? 12.877  -0.466  6.986   1.00 18.09 ? 176 PHE   A CG   1 
ATOM   2641 C  CD1  . PHE   A 1 176 ? 12.129  -1.366  6.247   1.00 18.31 ? 176 PHE   A CD1  1 
ATOM   2642 C  CD2  . PHE   A 1 176 ? 14.074  -0.010  6.458   1.00 19.36 ? 176 PHE   A CD2  1 
ATOM   2643 C  CE1  . PHE   A 1 176 ? 12.591  -1.829  5.024   1.00 21.07 ? 176 PHE   A CE1  1 
ATOM   2644 C  CE2  . PHE   A 1 176 ? 14.528  -0.456  5.236   1.00 20.53 ? 176 PHE   A CE2  1 
ATOM   2645 C  CZ   . PHE   A 1 176 ? 13.785  -1.365  4.517   1.00 21.99 ? 176 PHE   A CZ   1 
ATOM   2646 H  H    . PHE   A 1 176 ? 11.512  1.340   10.209  1.00 18.47 ? 176 PHE   A H    1 
ATOM   2647 H  HA   . PHE   A 1 176 ? 11.953  1.969   7.736   1.00 19.62 ? 176 PHE   A HA   1 
ATOM   2648 H  HB2  . PHE   A 1 176 ? 13.187  0.301   8.839   1.00 22.13 ? 176 PHE   A HB2  1 
ATOM   2649 H  HB3  . PHE   A 1 176 ? 11.926  -0.659  8.768   1.00 22.13 ? 176 PHE   A HB3  1 
ATOM   2650 H  HD1  . PHE   A 1 176 ? 11.323  -1.684  6.586   1.00 21.99 ? 176 PHE   A HD1  1 
ATOM   2651 H  HD2  . PHE   A 1 176 ? 14.582  0.603   6.939   1.00 23.26 ? 176 PHE   A HD2  1 
ATOM   2652 H  HE1  . PHE   A 1 176 ? 12.085  -2.438  4.536   1.00 25.31 ? 176 PHE   A HE1  1 
ATOM   2653 H  HE2  . PHE   A 1 176 ? 15.338  -0.147  4.899   1.00 24.65 ? 176 PHE   A HE2  1 
ATOM   2654 H  HZ   . PHE   A 1 176 ? 14.092  -1.671  3.694   1.00 26.41 ? 176 PHE   A HZ   1 
ATOM   2655 N  N    . THR   A 1 177 ? 9.255   0.269   8.107   1.00 15.86 ? 177 THR   A N    1 
ATOM   2656 C  CA   . THR   A 1 177 ? 7.990   -0.054  7.444   1.00 15.19 ? 177 THR   A CA   1 
ATOM   2657 C  C    . THR   A 1 177 ? 7.196   1.196   7.100   1.00 17.40 ? 177 THR   A C    1 
ATOM   2658 O  O    . THR   A 1 177 ? 6.657   1.309   5.990   1.00 16.33 ? 177 THR   A O    1 
ATOM   2659 C  CB   . THR   A 1 177 ? 7.175   -1.001  8.322   1.00 15.74 ? 177 THR   A CB   1 
ATOM   2660 O  OG1  . THR   A 1 177 ? 7.912   -2.222  8.459   1.00 16.54 ? 177 THR   A OG1  1 
ATOM   2661 C  CG2  . THR   A 1 177 ? 5.788   -1.249  7.755   1.00 15.52 ? 177 THR   A CG2  1 
ATOM   2662 H  H    . THR   A 1 177 ? 9.318   -0.013  8.917   1.00 19.05 ? 177 THR   A H    1 
ATOM   2663 H  HA   . THR   A 1 177 ? 8.184   -0.516  6.614   1.00 18.25 ? 177 THR   A HA   1 
ATOM   2664 H  HB   . THR   A 1 177 ? 7.069   -0.600  9.199   1.00 18.90 ? 177 THR   A HB   1 
ATOM   2665 H  HG1  . THR   A 1 177 ? 7.485   -2.763  8.939   1.00 19.87 ? 177 THR   A HG1  1 
ATOM   2666 H  HG21 . THR   A 1 177 ? 5.387   -2.018  8.190   1.00 18.65 ? 177 THR   A HG21 1 
ATOM   2667 H  HG22 . THR   A 1 177 ? 5.223   -0.475  7.903   1.00 18.65 ? 177 THR   A HG22 1 
ATOM   2668 H  HG23 . THR   A 1 177 ? 5.846   -1.423  6.802   1.00 18.65 ? 177 THR   A HG23 1 
ATOM   2669 N  N    . GLU   A 1 178 ? 7.109   2.141   8.029   1.00 18.03 ? 178 GLU   A N    1 
ATOM   2670 C  CA   . GLU   A 1 178 ? 6.323   3.342   7.785   1.00 18.80 ? 178 GLU   A CA   1 
ATOM   2671 C  C    . GLU   A 1 178 ? 6.861   4.083   6.567   1.00 20.72 ? 178 GLU   A C    1 
ATOM   2672 O  O    . GLU   A 1 178 ? 6.102   4.674   5.790   1.00 22.51 ? 178 GLU   A O    1 
ATOM   2673 C  CB   . GLU   A 1 178 ? 6.387   4.223   9.021   1.00 17.88 ? 178 GLU   A CB   1 
ATOM   2674 C  CG   . GLU   A 1 178 ? 5.668   5.537   8.938   1.00 21.56 ? 178 GLU   A CG   1 
ATOM   2675 C  CD   . GLU   A 1 178 ? 5.722   6.265   10.264  1.00 30.40 ? 178 GLU   A CD   1 
ATOM   2676 O  OE1  . GLU   A 1 178 ? 5.187   5.734   11.262  1.00 27.01 ? 178 GLU   A OE1  1 
ATOM   2677 O  OE2  . GLU   A 1 178 ? 6.253   7.393   10.295  1.00 41.60 ? 178 GLU   A OE2  1 
ATOM   2678 H  H    . GLU   A 1 178 ? 7.490   2.112   8.799   1.00 21.66 ? 178 GLU   A H    1 
ATOM   2679 H  HA   . GLU   A 1 178 ? 5.398   3.102   7.620   1.00 22.58 ? 178 GLU   A HA   1 
ATOM   2680 H  HB2  . GLU   A 1 178 ? 6.004   3.732   9.765   1.00 21.48 ? 178 GLU   A HB2  1 
ATOM   2681 H  HB3  . GLU   A 1 178 ? 7.319   4.416   9.209   1.00 21.48 ? 178 GLU   A HB3  1 
ATOM   2682 H  HG2  . GLU   A 1 178 ? 6.090   6.095   8.267   1.00 25.89 ? 178 GLU   A HG2  1 
ATOM   2683 H  HG3  . GLU   A 1 178 ? 4.738   5.382   8.712   1.00 25.89 ? 178 GLU   A HG3  1 
ATOM   2684 N  N    . GLN   A 1 179 ? 8.187   4.076   6.404   1.00 18.82 ? 179 GLN   A N    1 
ATOM   2685 C  CA   . GLN   A 1 179 ? 8.840   4.867   5.329   1.00 19.76 ? 179 GLN   A CA   1 
ATOM   2686 C  C    . GLN   A 1 179 ? 8.933   4.056   4.029   1.00 20.42 ? 179 GLN   A C    1 
ATOM   2687 O  O    . GLN   A 1 179 ? 9.414   4.628   3.032   1.00 23.64 ? 179 GLN   A O    1 
ATOM   2688 C  CB   . GLN   A 1 179 ? 10.196  5.306   5.883   1.00 22.46 ? 179 GLN   A CB   1 
ATOM   2689 C  CG   . GLN   A 1 179 ? 10.088  6.323   7.017   1.00 23.05 ? 179 GLN   A CG   1 
ATOM   2690 C  CD   . GLN   A 1 179 ? 11.298  6.360   7.926   1.00 30.84 ? 179 GLN   A CD   1 
ATOM   2691 O  OE1  . GLN   A 1 179 ? 12.258  5.608   7.755   1.00 32.13 ? 179 GLN   A OE1  1 
ATOM   2692 N  NE2  . GLN   A 1 179 ? 11.261  7.234   8.920   1.00 29.16 ? 179 GLN   A NE2  1 
ATOM   2693 H  H    . GLN   A 1 179 ? 8.735   3.629   6.893   1.00 22.61 ? 179 GLN   A H    1 
ATOM   2694 H  HA   . GLN   A 1 179 ? 8.314   5.662   5.152   1.00 23.73 ? 179 GLN   A HA   1 
ATOM   2695 H  HB2  . GLN   A 1 179 ? 10.661  4.526   6.224   1.00 26.97 ? 179 GLN   A HB2  1 
ATOM   2696 H  HB3  . GLN   A 1 179 ? 10.711  5.711   5.168   1.00 26.97 ? 179 GLN   A HB3  1 
ATOM   2697 H  HG2  . GLN   A 1 179 ? 9.979   7.207   6.633   1.00 27.68 ? 179 GLN   A HG2  1 
ATOM   2698 H  HG3  . GLN   A 1 179 ? 9.316   6.105   7.562   1.00 27.68 ? 179 GLN   A HG3  1 
ATOM   2699 H  HE21 . GLN   A 1 179 ? 10.577  7.746   9.018   1.00 35.02 ? 179 GLN   A HE21 1 
ATOM   2700 H  HE22 . GLN   A 1 179 ? 11.923  7.292   9.465   1.00 35.02 ? 179 GLN   A HE22 1 
ATOM   2701 N  N    . HIS   A 1 180 ? 8.487   2.798   4.027   1.00 19.07 ? 180 HIS   A N    1 
ATOM   2702 C  CA   . HIS   A 1 180 ? 8.488   1.942   2.808   1.00 20.46 ? 180 HIS   A CA   1 
ATOM   2703 C  C    . HIS   A 1 180 ? 7.067   1.505   2.427   1.00 17.32 ? 180 HIS   A C    1 
ATOM   2704 O  O    . HIS   A 1 180 ? 6.358   2.311   1.799   1.00 22.11 ? 180 HIS   A O    1 
ATOM   2705 C  CB   . HIS   A 1 180 ? 9.469   0.778   2.983   1.00 19.92 ? 180 HIS   A CB   1 
ATOM   2706 C  CG   . HIS   A 1 180 ? 10.894  1.208   2.927   1.00 20.57 ? 180 HIS   A CG   1 
ATOM   2707 N  ND1  . HIS   A 1 180 ? 11.615  1.620   4.026   1.00 23.25 ? 180 HIS   A ND1  1 
ATOM   2708 C  CD2  . HIS   A 1 180 ? 11.721  1.305   1.884   1.00 23.74 ? 180 HIS   A CD2  1 
ATOM   2709 C  CE1  . HIS   A 1 180 ? 12.840  1.944   3.647   1.00 25.47 ? 180 HIS   A CE1  1 
ATOM   2710 N  NE2  . HIS   A 1 180 ? 12.927  1.759   2.350   1.00 25.88 ? 180 HIS   A NE2  1 
ATOM   2711 H  H    . HIS   A 1 180 ? 8.173   2.400   4.721   1.00 22.91 ? 180 HIS   A H    1 
ATOM   2712 H  HA   . HIS   A 1 180 ? 8.820   2.476   2.070   1.00 24.58 ? 180 HIS   A HA   1 
ATOM   2713 H  HB2  . HIS   A 1 180 ? 9.315   0.363   3.846   1.00 23.92 ? 180 HIS   A HB2  1 
ATOM   2714 H  HB3  . HIS   A 1 180 ? 9.323   0.133   2.274   1.00 23.92 ? 180 HIS   A HB3  1 
ATOM   2715 H  HD1  . HIS   A 1 180 ? 11.317  1.657   4.832   1.00 27.92 ? 180 HIS   A HD1  1 
ATOM   2716 H  HD2  . HIS   A 1 180 ? 11.517  1.096   1.001   1.00 28.51 ? 180 HIS   A HD2  1 
ATOM   2717 H  HE1  . HIS   A 1 180 ? 13.521  2.248   4.202   1.00 30.59 ? 180 HIS   A HE1  1 
ATOM   2718 N  N    . SER   A 1 181 ? 6.653   0.291   2.795   1.00 17.01 ? 181 SER   A N    1 
ATOM   2719 C  CA   . SER   A 1 181 ? 5.301   -0.225  2.455   1.00 18.39 ? 181 SER   A CA   1 
ATOM   2720 C  C    . SER   A 1 181 ? 4.217   0.649   3.090   1.00 20.83 ? 181 SER   A C    1 
ATOM   2721 O  O    . SER   A 1 181 ? 3.146   0.787   2.468   1.00 20.41 ? 181 SER   A O    1 
ATOM   2722 C  CB   . SER   A 1 181 ? 5.137   -1.656  2.894   1.00 17.69 ? 181 SER   A CB   1 
ATOM   2723 O  OG   . SER   A 1 181 ? 5.215   -1.769  4.307   1.00 18.47 ? 181 SER   A OG   1 
ATOM   2724 H  H    . SER   A 1 181 ? 7.130   -0.264  3.246   1.00 20.43 ? 181 SER   A H    1 
ATOM   2725 H  HA   . SER   A 1 181 ? 5.185   -0.193  1.493   1.00 22.08 ? 181 SER   A HA   1 
ATOM   2726 H  HB2  . SER   A 1 181 ? 4.271   -1.978  2.600   1.00 21.25 ? 181 SER   A HB2  1 
ATOM   2727 H  HB3  . SER   A 1 181 ? 5.842   -2.190  2.496   1.00 21.25 ? 181 SER   A HB3  1 
ATOM   2728 H  HG   . SER   A 1 181 ? 5.961   -1.493  4.576   1.00 22.18 ? 181 SER   A HG   1 
ATOM   2729 N  N    . GLY   A 1 182 ? 4.452   1.186   4.288   1.00 17.94 ? 182 GLY   A N    1 
ATOM   2730 C  CA   . GLY   A 1 182 ? 3.436   1.942   4.990   1.00 18.86 ? 182 GLY   A CA   1 
ATOM   2731 C  C    . GLY   A 1 182 ? 2.305   1.102   5.525   1.00 19.02 ? 182 GLY   A C    1 
ATOM   2732 O  O    . GLY   A 1 182 ? 1.200   1.625   5.725   1.00 18.60 ? 182 GLY   A O    1 
ATOM   2733 H  H    . GLY   A 1 182 ? 5.198   1.122   4.711   1.00 21.55 ? 182 GLY   A H    1 
ATOM   2734 H  HA2  . GLY   A 1 182 ? 3.845   2.407   5.736   1.00 22.65 ? 182 GLY   A HA2  1 
ATOM   2735 H  HA3  . GLY   A 1 182 ? 3.061   2.605   4.389   1.00 22.65 ? 182 GLY   A HA3  1 
ATOM   2736 N  N    . LEU   A 1 183 ? 2.540   -0.188  5.758   1.00 17.14 ? 183 LEU   A N    1 
ATOM   2737 C  CA   . LEU   A 1 183 ? 1.522   -1.083  6.281   1.00 17.11 ? 183 LEU   A CA   1 
ATOM   2738 C  C    . LEU   A 1 183 ? 0.769   -0.411  7.421   1.00 15.83 ? 183 LEU   A C    1 
ATOM   2739 O  O    . LEU   A 1 183 ? 1.367   -0.015  8.428   1.00 17.19 ? 183 LEU   A O    1 
ATOM   2740 C  CB   . LEU   A 1 183 ? 2.165   -2.377  6.776   1.00 16.95 ? 183 LEU   A CB   1 
ATOM   2741 C  CG   . LEU   A 1 183 ? 2.647   -3.372  5.722   1.00 17.21 ? 183 LEU   A CG   1 
ATOM   2742 C  CD1  . LEU   A 1 183 ? 3.621   -4.377  6.387   1.00 15.92 ? 183 LEU   A CD1  1 
ATOM   2743 C  CD2  . LEU   A 1 183 ? 1.528   -4.084  5.003   1.00 17.81 ? 183 LEU   A CD2  1 
ATOM   2744 H  H    . LEU   A 1 183 ? 3.297   -0.572  5.617   1.00 20.59 ? 183 LEU   A H    1 
ATOM   2745 H  HA   . LEU   A 1 183 ? 0.889   -1.301  5.579   1.00 20.55 ? 183 LEU   A HA   1 
ATOM   2746 H  HB2  . LEU   A 1 183 ? 2.935   -2.141  7.317   1.00 20.36 ? 183 LEU   A HB2  1 
ATOM   2747 H  HB3  . LEU   A 1 183 ? 1.517   -2.841  7.329   1.00 20.36 ? 183 LEU   A HB3  1 
ATOM   2748 H  HG   . LEU   A 1 183 ? 3.151   -2.883  5.053   1.00 20.67 ? 183 LEU   A HG   1 
ATOM   2749 H  HD11 . LEU   A 1 183 ? 3.914   -5.019  5.722   1.00 19.13 ? 183 LEU   A HD11 1 
ATOM   2750 H  HD12 . LEU   A 1 183 ? 4.384   -3.892  6.738   1.00 19.13 ? 183 LEU   A HD12 1 
ATOM   2751 H  HD13 . LEU   A 1 183 ? 3.159   -4.834  7.107   1.00 19.13 ? 183 LEU   A HD13 1 
ATOM   2752 H  HD21 . LEU   A 1 183 ? 1.909   -4.697  4.355   1.00 21.39 ? 183 LEU   A HD21 1 
ATOM   2753 H  HD22 . LEU   A 1 183 ? 0.999   -4.574  5.651   1.00 21.39 ? 183 LEU   A HD22 1 
ATOM   2754 H  HD23 . LEU   A 1 183 ? 0.975   -3.427  4.552   1.00 21.39 ? 183 LEU   A HD23 1 
ATOM   2755 N  N    . GLU   A 1 184 ? -0.547  -0.281  7.262   1.00 16.90 ? 184 GLU   A N    1 
ATOM   2756 C  CA   . GLU   A 1 184 ? -1.367  0.427   8.236   1.00 17.83 ? 184 GLU   A CA   1 
ATOM   2757 C  C    . GLU   A 1 184 ? -1.543  -0.434  9.486   1.00 16.10 ? 184 GLU   A C    1 
ATOM   2758 O  O    . GLU   A 1 184 ? -1.622  -1.662  9.414   1.00 17.23 ? 184 GLU   A O    1 
ATOM   2759 C  CB   . GLU   A 1 184 ? -2.718  0.773   7.618   1.00 17.34 ? 184 GLU   A CB   1 
ATOM   2760 C  CG   . GLU   A 1 184 ? -2.632  1.927   6.620   1.00 20.97 ? 184 GLU   A CG   1 
ATOM   2761 C  CD   . GLU   A 1 184 ? -2.484  3.281   7.281   1.00 27.03 ? 184 GLU   A CD   1 
ATOM   2762 O  OE1  . GLU   A 1 184 ? -2.935  3.439   8.431   1.00 34.00 ? 184 GLU   A OE1  1 
ATOM   2763 O  OE2  . GLU   A 1 184 ? -1.905  4.189   6.649   1.00 30.98 ? 184 GLU   A OE2  1 
ATOM   2764 H  H    . GLU   A 1 184 ? -0.989  -0.596  6.595   1.00 20.30 ? 184 GLU   A H    1 
ATOM   2765 H  HA   . GLU   A 1 184 ? -0.925  1.252   8.491   1.00 21.42 ? 184 GLU   A HA   1 
ATOM   2766 H  HB2  . GLU   A 1 184 ? -3.058  -0.004  7.148   1.00 20.83 ? 184 GLU   A HB2  1 
ATOM   2767 H  HB3  . GLU   A 1 184 ? -3.333  1.029   8.323   1.00 20.83 ? 184 GLU   A HB3  1 
ATOM   2768 H  HG2  . GLU   A 1 184 ? -1.862  1.790   6.046   1.00 25.18 ? 184 GLU   A HG2  1 
ATOM   2769 H  HG3  . GLU   A 1 184 ? -3.440  1.941   6.089   1.00 25.18 ? 184 GLU   A HG3  1 
ATOM   2770 N  N    . TYR   A 1 185 ? -1.622  0.225   10.642  1.00 19.15 ? 185 TYR   A N    1 
ATOM   2771 C  CA   . TYR   A 1 185 ? -1.449  -0.460  11.929  1.00 15.98 ? 185 TYR   A CA   1 
ATOM   2772 C  C    . TYR   A 1 185 ? -2.769  -0.940  12.530  1.00 18.44 ? 185 TYR   A C    1 
ATOM   2773 O  O    . TYR   A 1 185 ? -3.124  -0.612  13.666  1.00 19.26 ? 185 TYR   A O    1 
ATOM   2774 C  CB   . TYR   A 1 185 ? -0.722  0.453   12.900  1.00 17.02 ? 185 TYR   A CB   1 
ATOM   2775 C  CG   . TYR   A 1 185 ? -0.002  -0.259  14.012  1.00 17.88 ? 185 TYR   A CG   1 
ATOM   2776 C  CD1  . TYR   A 1 185 ? 1.023   -1.152  13.752  1.00 15.32 ? 185 TYR   A CD1  1 
ATOM   2777 C  CD2  . TYR   A 1 185 ? -0.333  -0.005  15.336  1.00 18.28 ? 185 TYR   A CD2  1 
ATOM   2778 C  CE1  . TYR   A 1 185 ? 1.695   -1.786  14.783  1.00 16.35 ? 185 TYR   A CE1  1 
ATOM   2779 C  CE2  . TYR   A 1 185 ? 0.331   -0.630  16.368  1.00 18.30 ? 185 TYR   A CE2  1 
ATOM   2780 C  CZ   . TYR   A 1 185 ? 1.345   -1.520  16.087  1.00 16.73 ? 185 TYR   A CZ   1 
ATOM   2781 O  OH   . TYR   A 1 185 ? 2.001   -2.142  17.126  1.00 17.82 ? 185 TYR   A OH   1 
ATOM   2782 H  H    . TYR   A 1 185 ? -1.775  1.069   10.711  1.00 23.00 ? 185 TYR   A H    1 
ATOM   2783 H  HA   . TYR   A 1 185 ? -0.894  -1.242  11.787  1.00 19.20 ? 185 TYR   A HA   1 
ATOM   2784 H  HB2  . TYR   A 1 185 ? -0.063  0.966   12.407  1.00 20.44 ? 185 TYR   A HB2  1 
ATOM   2785 H  HB3  . TYR   A 1 185 ? -1.367  1.054   13.304  1.00 20.44 ? 185 TYR   A HB3  1 
ATOM   2786 H  HD1  . TYR   A 1 185 ? 1.263   -1.330  12.871  1.00 18.40 ? 185 TYR   A HD1  1 
ATOM   2787 H  HD2  . TYR   A 1 185 ? -1.014  0.598   15.529  1.00 21.95 ? 185 TYR   A HD2  1 
ATOM   2788 H  HE1  . TYR   A 1 185 ? 2.379   -2.387  14.596  1.00 19.64 ? 185 TYR   A HE1  1 
ATOM   2789 H  HE2  . TYR   A 1 185 ? 0.095   -0.453  17.250  1.00 21.98 ? 185 TYR   A HE2  1 
ATOM   2790 H  HH   . TYR   A 1 185 ? 2.592   -2.657  16.825  1.00 21.41 ? 185 TYR   A HH   1 
ATOM   2791 N  N    . PHE   A 1 186 ? -3.454  -1.776  11.759  1.00 17.74 ? 186 PHE   A N    1 
ATOM   2792 C  CA   . PHE   A 1 186 ? -4.678  -2.450  12.164  1.00 16.86 ? 186 PHE   A CA   1 
ATOM   2793 C  C    . PHE   A 1 186 ? -4.947  -3.546  11.144  1.00 17.61 ? 186 PHE   A C    1 
ATOM   2794 O  O    . PHE   A 1 186 ? -4.367  -3.554  10.051  1.00 17.66 ? 186 PHE   A O    1 
ATOM   2795 C  CB   . PHE   A 1 186 ? -5.851  -1.479  12.249  1.00 19.49 ? 186 PHE   A CB   1 
ATOM   2796 C  CG   . PHE   A 1 186 ? -6.003  -0.570  11.052  1.00 23.25 ? 186 PHE   A CG   1 
ATOM   2797 C  CD1  . PHE   A 1 186 ? -6.438  -1.065  9.831   1.00 34.11 ? 186 PHE   A CD1  1 
ATOM   2798 C  CD2  . PHE   A 1 186 ? -5.708  0.777   11.146  1.00 35.56 ? 186 PHE   A CD2  1 
ATOM   2799 C  CE1  . PHE   A 1 186 ? -6.590  -0.231  8.747   1.00 38.14 ? 186 PHE   A CE1  1 
ATOM   2800 C  CE2  . PHE   A 1 186 ? -5.854  1.612   10.053  1.00 37.10 ? 186 PHE   A CE2  1 
ATOM   2801 C  CZ   . PHE   A 1 186 ? -6.297  1.107   8.857   1.00 30.33 ? 186 PHE   A CZ   1 
ATOM   2802 H  H    . PHE   A 1 186 ? -3.215  -1.976  10.958  1.00 21.31 ? 186 PHE   A H    1 
ATOM   2803 H  HA   . PHE   A 1 186 ? -4.552  -2.860  13.034  1.00 20.25 ? 186 PHE   A HA   1 
ATOM   2804 H  HB2  . PHE   A 1 186 ? -6.671  -1.990  12.336  1.00 23.41 ? 186 PHE   A HB2  1 
ATOM   2805 H  HB3  . PHE   A 1 186 ? -5.732  -0.918  13.031  1.00 23.41 ? 186 PHE   A HB3  1 
ATOM   2806 H  HD1  . PHE   A 1 186 ? -6.646  -1.968  9.749   1.00 40.95 ? 186 PHE   A HD1  1 
ATOM   2807 H  HD2  . PHE   A 1 186 ? -5.414  1.127   11.956  1.00 42.69 ? 186 PHE   A HD2  1 
ATOM   2808 H  HE1  . PHE   A 1 186 ? -6.884  -0.576  7.935   1.00 45.78 ? 186 PHE   A HE1  1 
ATOM   2809 H  HE2  . PHE   A 1 186 ? -5.655  2.517   10.130  1.00 44.54 ? 186 PHE   A HE2  1 
ATOM   2810 H  HZ   . PHE   A 1 186 ? -6.391  1.667   8.120   1.00 36.41 ? 186 PHE   A HZ   1 
ATOM   2811 N  N    . GLY   A 1 187 ? -5.827  -4.474  11.519  1.00 18.00 ? 187 GLY   A N    1 
ATOM   2812 C  CA   . GLY   A 1 187 ? -6.218  -5.537  10.620  1.00 17.06 ? 187 GLY   A CA   1 
ATOM   2813 C  C    . GLY   A 1 187 ? -5.045  -6.401  10.192  1.00 15.83 ? 187 GLY   A C    1 
ATOM   2814 O  O    . GLY   A 1 187 ? -4.061  -6.585  10.920  1.00 18.12 ? 187 GLY   A O    1 
ATOM   2815 H  H    . GLY   A 1 187 ? -6.208  -4.504  12.290  1.00 21.62 ? 187 GLY   A H    1 
ATOM   2816 H  HA2  . GLY   A 1 187 ? -6.873  -6.102  11.058  1.00 20.49 ? 187 GLY   A HA2  1 
ATOM   2817 H  HA3  . GLY   A 1 187 ? -6.623  -5.155  9.826   1.00 20.49 ? 187 GLY   A HA3  1 
ATOM   2818 N  N    . GLN   A 1 188 ? -5.155  -6.953  8.984   1.00 16.89 ? 188 GLN   A N    1 
ATOM   2819 C  CA   . GLN   A 1 188 ? -4.110  -7.839  8.481   1.00 16.15 ? 188 GLN   A CA   1 
ATOM   2820 C  C    . GLN   A 1 188 ? -2.817  -7.098  8.192   1.00 15.96 ? 188 GLN   A C    1 
ATOM   2821 O  O    . GLN   A 1 188 ? -1.733  -7.606  8.501   1.00 15.94 ? 188 GLN   A O    1 
ATOM   2822 C  CB   . GLN   A 1 188 ? -4.615  -8.576  7.243   1.00 17.36 ? 188 GLN   A CB   1 
ATOM   2823 C  CG   . GLN   A 1 188 ? -5.769  -9.538  7.489   1.00 16.76 ? 188 GLN   A CG   1 
ATOM   2824 C  CD   . GLN   A 1 188 ? -6.322  -10.048 6.183   1.00 18.42 ? 188 GLN   A CD   1 
ATOM   2825 O  OE1  . GLN   A 1 188 ? -5.627  -10.743 5.450   1.00 19.37 ? 188 GLN   A OE1  1 
ATOM   2826 N  NE2  . GLN   A 1 188 ? -7.605  -9.796  5.925   1.00 24.38 ? 188 GLN   A NE2  1 
ATOM   2827 H  H    . GLN   A 1 188 ? -5.814  -6.832  8.445   1.00 20.29 ? 188 GLN   A H    1 
ATOM   2828 H  HA   . GLN   A 1 188 ? -3.918  -8.505  9.160   1.00 19.40 ? 188 GLN   A HA   1 
ATOM   2829 H  HB2  . GLN   A 1 188 ? -4.915  -7.920  6.595   1.00 20.85 ? 188 GLN   A HB2  1 
ATOM   2830 H  HB3  . GLN   A 1 188 ? -3.882  -9.089  6.870   1.00 20.85 ? 188 GLN   A HB3  1 
ATOM   2831 H  HG2  . GLN   A 1 188 ? -5.454  -10.295 8.006   1.00 20.14 ? 188 GLN   A HG2  1 
ATOM   2832 H  HG3  . GLN   A 1 188 ? -6.478  -9.076  7.963   1.00 20.14 ? 188 GLN   A HG3  1 
ATOM   2833 H  HE21 . GLN   A 1 188 ? -8.067  -9.319  6.471   1.00 29.27 ? 188 GLN   A HE21 1 
ATOM   2834 H  HE22 . GLN   A 1 188 ? -7.960  -10.078 5.194   1.00 29.27 ? 188 GLN   A HE22 1 
ATOM   2835 N  N    . SER   A 1 189 ? -2.893  -5.913  7.578   1.00 17.20 ? 189 SER   A N    1 
ATOM   2836 C  CA   . SER   A 1 189 ? -1.672  -5.149  7.331   1.00 16.47 ? 189 SER   A CA   1 
ATOM   2837 C  C    . SER   A 1 189 ? -0.954  -4.827  8.634   1.00 14.45 ? 189 SER   A C    1 
ATOM   2838 O  O    . SER   A 1 189 ? 0.282   -4.778  8.670   1.00 15.01 ? 189 SER   A O    1 
ATOM   2839 C  CB   . SER   A 1 189 ? -1.996  -3.865  6.563   1.00 17.36 ? 189 SER   A CB   1 
ATOM   2840 O  OG   . SER   A 1 189 ? -2.877  -3.027  7.286   1.00 17.96 ? 189 SER   A OG   1 
ATOM   2841 H  H    . SER   A 1 189 ? -3.618  -5.541  7.303   1.00 20.66 ? 189 SER   A H    1 
ATOM   2842 H  HA   . SER   A 1 189 ? -1.073  -5.681  6.784   1.00 19.78 ? 189 SER   A HA   1 
ATOM   2843 H  HB2  . SER   A 1 189 ? -1.171  -3.383  6.398   1.00 20.85 ? 189 SER   A HB2  1 
ATOM   2844 H  HB3  . SER   A 1 189 ? -2.412  -4.102  5.719   1.00 20.85 ? 189 SER   A HB3  1 
ATOM   2845 H  HG   . SER   A 1 189 ? -2.524  -2.798  8.013   1.00 21.57 ? 189 SER   A HG   1 
ATOM   2846 N  N    . GLY   A 1 190 ? -1.710  -4.614  9.713   1.00 16.29 ? 190 GLY   A N    1 
ATOM   2847 C  CA   . GLY   A 1 190 ? -1.092  -4.304  10.989  1.00 15.43 ? 190 GLY   A CA   1 
ATOM   2848 C  C    . GLY   A 1 190 ? -0.420  -5.512  11.607  1.00 14.13 ? 190 GLY   A C    1 
ATOM   2849 O  O    . GLY   A 1 190 ? 0.631   -5.388  12.244  1.00 13.88 ? 190 GLY   A O    1 
ATOM   2850 H  H    . GLY   A 1 190 ? -2.569  -4.644  9.727   1.00 19.57 ? 190 GLY   A H    1 
ATOM   2851 H  HA2  . GLY   A 1 190 ? -0.426  -3.610  10.866  1.00 18.54 ? 190 GLY   A HA2  1 
ATOM   2852 H  HA3  . GLY   A 1 190 ? -1.767  -3.978  11.605  1.00 18.54 ? 190 GLY   A HA3  1 
ATOM   2853 N  N    . GLY   A 1 191 ? -1.018  -6.692  11.440  1.00 15.33 ? 191 GLY   A N    1 
ATOM   2854 C  CA   . GLY   A 1 191 ? -0.333  -7.914  11.823  1.00 14.63 ? 191 GLY   A CA   1 
ATOM   2855 C  C    . GLY   A 1 191 ? 0.971   -8.090  11.078  1.00 15.06 ? 191 GLY   A C    1 
ATOM   2856 O  O    . GLY   A 1 191 ? 1.986   -8.452  11.672  1.00 15.24 ? 191 GLY   A O    1 
ATOM   2857 H  H    . GLY   A 1 191 ? -1.805  -6.806  11.113  1.00 18.41 ? 191 GLY   A H    1 
ATOM   2858 H  HA2  . GLY   A 1 191 ? -0.145  -7.896  12.774  1.00 17.58 ? 191 GLY   A HA2  1 
ATOM   2859 H  HA3  . GLY   A 1 191 ? -0.901  -8.677  11.635  1.00 17.58 ? 191 GLY   A HA3  1 
ATOM   2860 N  N    . MET   A 1 192 ? 0.961   -7.821  9.770   1.00 15.23 ? 192 MET   A N    1 
ATOM   2861 C  CA   . MET   A 1 192 ? 2.199   -7.863  8.994   1.00 15.44 ? 192 MET   A CA   1 
ATOM   2862 C  C    . MET   A 1 192 ? 3.203   -6.832  9.475   1.00 15.14 ? 192 MET   A C    1 
ATOM   2863 O  O    . MET   A 1 192 ? 4.416   -7.098  9.489   1.00 14.42 ? 192 MET   A O    1 
ATOM   2864 C  CB   . MET   A 1 192 ? 1.906   -7.666  7.508   1.00 16.78 ? 192 MET   A CB   1 
ATOM   2865 C  CG   . MET   A 1 192 ? 1.020   -8.711  6.887   1.00 17.98 ? 192 MET   A CG   1 
ATOM   2866 S  SD   . MET   A 1 192 ? 0.629   -8.386  5.163   1.00 17.69 ? 192 MET   A SD   1 
ATOM   2867 C  CE   . MET   A 1 192 ? 2.230   -8.274  4.434   1.00 21.62 ? 192 MET   A CE   1 
ATOM   2868 H  H    . MET   A 1 192 ? 0.261   -7.615  9.316   1.00 18.30 ? 192 MET   A H    1 
ATOM   2869 H  HA   . MET   A 1 192 ? 2.593   -8.743  9.097   1.00 18.55 ? 192 MET   A HA   1 
ATOM   2870 H  HB2  . MET   A 1 192 ? 1.472   -6.807  7.390   1.00 20.16 ? 192 MET   A HB2  1 
ATOM   2871 H  HB3  . MET   A 1 192 ? 2.749   -7.673  7.030   1.00 20.16 ? 192 MET   A HB3  1 
ATOM   2872 H  HG2  . MET   A 1 192 ? 1.468   -9.570  6.933   1.00 21.60 ? 192 MET   A HG2  1 
ATOM   2873 H  HG3  . MET   A 1 192 ? 0.185   -8.748  7.379   1.00 21.60 ? 192 MET   A HG3  1 
ATOM   2874 H  HE1  . MET   A 1 192 ? 2.132   -8.184  3.473   1.00 25.96 ? 192 MET   A HE1  1 
ATOM   2875 H  HE2  . MET   A 1 192 ? 2.688   -7.498  4.792   1.00 25.96 ? 192 MET   A HE2  1 
ATOM   2876 H  HE3  . MET   A 1 192 ? 2.729   -9.079  4.642   1.00 25.96 ? 192 MET   A HE3  1 
ATOM   2877 N  N    . ASN   A 1 193 ? 2.730   -5.640  9.832   1.00 15.56 ? 193 ASN   A N    1 
ATOM   2878 C  CA   . ASN   A 1 193 ? 3.599   -4.586  10.336  1.00 14.72 ? 193 ASN   A CA   1 
ATOM   2879 C  C    . ASN   A 1 193 ? 4.307   -5.046  11.600  1.00 14.76 ? 193 ASN   A C    1 
ATOM   2880 O  O    . ASN   A 1 193 ? 5.539   -4.990  11.696  1.00 14.47 ? 193 ASN   A O    1 
ATOM   2881 C  CB   . ASN   A 1 193 ? 2.745   -3.335  10.575  1.00 15.52 ? 193 ASN   A CB   1 
ATOM   2882 C  CG   . ASN   A 1 193 ? 3.539   -2.151  11.067  1.00 15.86 ? 193 ASN   A CG   1 
ATOM   2883 O  OD1  . ASN   A 1 193 ? 4.403   -2.278  11.935  1.00 15.87 ? 193 ASN   A OD1  1 
ATOM   2884 N  ND2  . ASN   A 1 193 ? 3.258   -0.977  10.505  1.00 15.53 ? 193 ASN   A ND2  1 
ATOM   2885 H  H    . ASN   A 1 193 ? 1.900   -5.417  9.790   1.00 18.69 ? 193 ASN   A H    1 
ATOM   2886 H  HA   . ASN   A 1 193 ? 4.271   -4.375  9.669   1.00 17.69 ? 193 ASN   A HA   1 
ATOM   2887 H  HB2  . ASN   A 1 193 ? 2.319   -3.082  9.741   1.00 18.64 ? 193 ASN   A HB2  1 
ATOM   2888 H  HB3  . ASN   A 1 193 ? 2.070   -3.538  11.241  1.00 18.64 ? 193 ASN   A HB3  1 
ATOM   2889 H  HD21 . ASN   A 1 193 ? 3.683   -0.271  10.750  1.00 18.65 ? 193 ASN   A HD21 1 
ATOM   2890 H  HD22 . ASN   A 1 193 ? 2.649   -0.925  9.900   1.00 18.65 ? 193 ASN   A HD22 1 
ATOM   2891 N  N    . GLU   A 1 194 ? 3.538   -5.545  12.564  1.00 13.52 ? 194 GLU   A N    1 
ATOM   2892 C  CA   . GLU   A 1 194 ? 4.109   -6.103  13.780  1.00 15.39 ? 194 GLU   A CA   1 
ATOM   2893 C  C    . GLU   A 1 194 ? 5.092   -7.218  13.469  1.00 14.60 ? 194 GLU   A C    1 
ATOM   2894 O  O    . GLU   A 1 194 ? 6.182   -7.276  14.049  1.00 13.96 ? 194 GLU   A O    1 
ATOM   2895 C  CB   . GLU   A 1 194 ? 2.970   -6.622  14.649  1.00 14.77 ? 194 GLU   A CB   1 
ATOM   2896 C  CG   . GLU   A 1 194 ? 2.518   -5.686  15.739  1.00 14.10 ? 194 GLU   A CG   1 
ATOM   2897 C  CD   . GLU   A 1 194 ? 3.671   -5.121  16.530  1.00 12.97 ? 194 GLU   A CD   1 
ATOM   2898 O  OE1  . GLU   A 1 194 ? 4.307   -5.922  17.241  1.00 15.24 ? 194 GLU   A OE1  1 
ATOM   2899 O  OE2  . GLU   A 1 194 ? 3.888   -3.890  16.494  1.00 16.21 ? 194 GLU   A OE2  1 
ATOM   2900 H  H    . GLU   A 1 194 ? 2.679   -5.569  12.534  1.00 16.24 ? 194 GLU   A H    1 
ATOM   2901 H  HA   . GLU   A 1 194 ? 4.591   -5.404  14.244  1.00 18.48 ? 194 GLU   A HA   1 
ATOM   2902 H  HB2  . GLU   A 1 194 ? 2.204   -6.811  14.085  1.00 17.74 ? 194 GLU   A HB2  1 
ATOM   2903 H  HB3  . GLU   A 1 194 ? 3.268   -7.438  15.079  1.00 17.74 ? 194 GLU   A HB3  1 
ATOM   2904 H  HG2  . GLU   A 1 194 ? 2.035   -4.945  15.340  1.00 16.94 ? 194 GLU   A HG2  1 
ATOM   2905 H  HG3  . GLU   A 1 194 ? 1.941   -6.168  16.351  1.00 16.94 ? 194 GLU   A HG3  1 
ATOM   2906 N  N    . SER   A 1 195 ? 4.725   -8.121  12.557  1.00 14.89 ? 195 SER   A N    1 
ATOM   2907 C  CA   . SER   A 1 195 ? 5.593   -9.256  12.262  1.00 14.61 ? 195 SER   A CA   1 
ATOM   2908 C  C    . SER   A 1 195 ? 6.919   -8.808  11.686  1.00 14.71 ? 195 SER   A C    1 
ATOM   2909 O  O    . SER   A 1 195 ? 7.974   -9.325  12.068  1.00 14.61 ? 195 SER   A O    1 
ATOM   2910 C  CB   . SER   A 1 195 ? 4.917   -10.221 11.294  1.00 15.03 ? 195 SER   A CB   1 
ATOM   2911 O  OG   . SER   A 1 195 ? 3.711   -10.726 11.800  1.00 17.00 ? 195 SER   A OG   1 
ATOM   2912 H  H    . SER   A 1 195 ? 3.994   -8.099  12.105  1.00 17.88 ? 195 SER   A H    1 
ATOM   2913 H  HA   . SER   A 1 195 ? 5.772   -9.733  13.087  1.00 17.55 ? 195 SER   A HA   1 
ATOM   2914 H  HB2  . SER   A 1 195 ? 4.734   -9.752  10.465  1.00 18.06 ? 195 SER   A HB2  1 
ATOM   2915 H  HB3  . SER   A 1 195 ? 5.518   -10.963 11.124  1.00 18.06 ? 195 SER   A HB3  1 
ATOM   2916 H  HG   . SER   A 1 195 ? 3.560   -11.488 11.482  1.00 20.42 ? 195 SER   A HG   1 
ATOM   2917 N  N    . PHE   A 1 196 ? 6.890   -7.872  10.733  1.00 14.79 ? 196 PHE   A N    1 
ATOM   2918 C  CA   . PHE   A 1 196 ? 8.147   -7.425  10.151  1.00 13.94 ? 196 PHE   A CA   1 
ATOM   2919 C  C    . PHE   A 1 196 ? 9.083   -6.920  11.242  1.00 13.53 ? 196 PHE   A C    1 
ATOM   2920 O  O    . PHE   A 1 196 ? 10.293  -7.181  11.213  1.00 14.32 ? 196 PHE   A O    1 
ATOM   2921 C  CB   . PHE   A 1 196 ? 7.920   -6.327  9.112   1.00 15.60 ? 196 PHE   A CB   1 
ATOM   2922 C  CG   . PHE   A 1 196 ? 9.198   -5.882  8.461   1.00 12.94 ? 196 PHE   A CG   1 
ATOM   2923 C  CD1  . PHE   A 1 196 ? 9.732   -6.628  7.426   1.00 15.66 ? 196 PHE   A CD1  1 
ATOM   2924 C  CD2  . PHE   A 1 196 ? 9.910   -4.787  8.933   1.00 15.20 ? 196 PHE   A CD2  1 
ATOM   2925 C  CE1  . PHE   A 1 196 ? 10.938  -6.264  6.835   1.00 16.33 ? 196 PHE   A CE1  1 
ATOM   2926 C  CE2  . PHE   A 1 196 ? 11.116  -4.413  8.348   1.00 16.00 ? 196 PHE   A CE2  1 
ATOM   2927 C  CZ   . PHE   A 1 196 ? 11.633  -5.158  7.299   1.00 16.37 ? 196 PHE   A CZ   1 
ATOM   2928 H  H    . PHE   A 1 196 ? 6.183   -7.496  10.419  1.00 17.76 ? 196 PHE   A H    1 
ATOM   2929 H  HA   . PHE   A 1 196 ? 8.576   -8.174  9.709   1.00 16.74 ? 196 PHE   A HA   1 
ATOM   2930 H  HB2  . PHE   A 1 196 ? 7.330   -6.663  8.419   1.00 18.74 ? 196 PHE   A HB2  1 
ATOM   2931 H  HB3  . PHE   A 1 196 ? 7.519   -5.558  9.546   1.00 18.74 ? 196 PHE   A HB3  1 
ATOM   2932 H  HD1  . PHE   A 1 196 ? 9.273   -7.374  7.112   1.00 18.81 ? 196 PHE   A HD1  1 
ATOM   2933 H  HD2  . PHE   A 1 196 ? 9.568   -4.287  9.639   1.00 18.26 ? 196 PHE   A HD2  1 
ATOM   2934 H  HE1  . PHE   A 1 196 ? 11.279  -6.764  6.129   1.00 19.62 ? 196 PHE   A HE1  1 
ATOM   2935 H  HE2  . PHE   A 1 196 ? 11.576  -3.668  8.662   1.00 19.22 ? 196 PHE   A HE2  1 
ATOM   2936 H  HZ   . PHE   A 1 196 ? 12.435  -4.909  6.899   1.00 19.67 ? 196 PHE   A HZ   1 
ATOM   2937 N  N    . SER   A 1 197 ? 8.539   -6.196  12.222  1.00 14.19 ? 197 SER   A N    1 
ATOM   2938 C  CA   . SER   A 1 197 ? 9.364   -5.698  13.316  1.00 14.18 ? 197 SER   A CA   1 
ATOM   2939 C  C    . SER   A 1 197 ? 9.885   -6.846  14.180  1.00 15.25 ? 197 SER   A C    1 
ATOM   2940 O  O    . SER   A 1 197 ? 11.026  -6.785  14.658  1.00 14.06 ? 197 SER   A O    1 
ATOM   2941 C  CB   . SER   A 1 197 ? 8.550   -4.685  14.138  1.00 13.83 ? 197 SER   A CB   1 
ATOM   2942 O  OG   . SER   A 1 197 ? 8.552   -3.395  13.528  1.00 15.99 ? 197 SER   A OG   1 
ATOM   2943 H  H    . SER   A 1 197 ? 7.707   -5.984  12.274  1.00 17.04 ? 197 SER   A H    1 
ATOM   2944 H  HA   . SER   A 1 197 ? 10.130  -5.233  12.945  1.00 17.03 ? 197 SER   A HA   1 
ATOM   2945 H  HB2  . SER   A 1 197 ? 7.635   -4.999  14.214  1.00 16.61 ? 197 SER   A HB2  1 
ATOM   2946 H  HB3  . SER   A 1 197 ? 8.949   -4.610  15.013  1.00 16.61 ? 197 SER   A HB3  1 
ATOM   2947 H  HG   . SER   A 1 197 ? 9.339   -3.109  13.464  1.00 19.20 ? 197 SER   A HG   1 
ATOM   2948 N  N    . ASP   A 1 198 ? 9.093   -7.912  14.373  1.00 13.90 ? 198 ASP   A N    1 
ATOM   2949 C  CA   . ASP   A 1 198 ? 9.596   -9.059  15.127  1.00 15.21 ? 198 ASP   A CA   1 
ATOM   2950 C  C    . ASP   A 1 198 ? 10.641  -9.830  14.316  1.00 18.00 ? 198 ASP   A C    1 
ATOM   2951 O  O    . ASP   A 1 198 ? 11.597  -10.381 14.891  1.00 15.64 ? 198 ASP   A O    1 
ATOM   2952 C  CB   . ASP   A 1 198 ? 8.464   -10.015 15.536  1.00 14.89 ? 198 ASP   A CB   1 
ATOM   2953 C  CG   . ASP   A 1 198 ? 7.580   -9.451  16.655  1.00 15.03 ? 198 ASP   A CG   1 
ATOM   2954 O  OD1  . ASP   A 1 198 ? 8.056   -8.586  17.425  1.00 15.24 ? 198 ASP   A OD1  1 
ATOM   2955 O  OD2  . ASP   A 1 198 ? 6.464   -9.989  16.849  1.00 14.73 ? 198 ASP   A OD2  1 
ATOM   2956 H  H    . ASP   A 1 198 ? 8.286   -7.991  14.086  1.00 16.69 ? 198 ASP   A H    1 
ATOM   2957 H  HA   . ASP   A 1 198 ? 10.024  -8.739  15.936  1.00 18.27 ? 198 ASP   A HA   1 
ATOM   2958 H  HB2  . ASP   A 1 198 ? 7.900   -10.184 14.765  1.00 17.89 ? 198 ASP   A HB2  1 
ATOM   2959 H  HB3  . ASP   A 1 198 ? 8.852   -10.847 15.851  1.00 17.89 ? 198 ASP   A HB3  1 
ATOM   2960 N  N    . MET   A 1 199 ? 10.490  -9.869  12.989  1.00 14.00 ? 199 MET   A N    1 
ATOM   2961 C  CA   . MET   A 1 199 ? 11.511  -10.470 12.146  1.00 15.78 ? 199 MET   A CA   1 
ATOM   2962 C  C    . MET   A 1 199 ? 12.823  -9.700  12.264  1.00 15.91 ? 199 MET   A C    1 
ATOM   2963 O  O    . MET   A 1 199 ? 13.908  -10.295 12.339  1.00 15.78 ? 199 MET   A O    1 
ATOM   2964 C  CB   . MET   A 1 199 ? 11.080  -10.490 10.676  1.00 15.98 ? 199 MET   A CB   1 
ATOM   2965 C  CG   . MET   A 1 199 ? 9.836   -11.282 10.370  1.00 15.55 ? 199 MET   A CG   1 
ATOM   2966 S  SD   . MET   A 1 199 ? 9.370   -10.937 8.650   1.00 16.69 ? 199 MET   A SD   1 
ATOM   2967 C  CE   . MET   A 1 199 ? 7.609   -11.299 8.670   1.00 16.10 ? 199 MET   A CE   1 
ATOM   2968 H  H    . MET   A 1 199 ? 9.812   -9.557  12.562  1.00 16.82 ? 199 MET   A H    1 
ATOM   2969 H  HA   . MET   A 1 199 ? 11.655  -11.386 12.429  1.00 18.96 ? 199 MET   A HA   1 
ATOM   2970 H  HB2  . MET   A 1 199 ? 10.919  -9.577  10.392  1.00 19.20 ? 199 MET   A HB2  1 
ATOM   2971 H  HB3  . MET   A 1 199 ? 11.802  -10.869 10.151  1.00 19.20 ? 199 MET   A HB3  1 
ATOM   2972 H  HG2  . MET   A 1 199 ? 10.006  -12.226 10.476  1.00 18.67 ? 199 MET   A HG2  1 
ATOM   2973 H  HG3  . MET   A 1 199 ? 9.114   -11.000 10.950  1.00 18.67 ? 199 MET   A HG3  1 
ATOM   2974 H  HE1  . MET   A 1 199 ? 7.246   -11.146 7.784   1.00 19.34 ? 199 MET   A HE1  1 
ATOM   2975 H  HE2  . MET   A 1 199 ? 7.481   -12.226 8.925   1.00 19.34 ? 199 MET   A HE2  1 
ATOM   2976 H  HE3  . MET   A 1 199 ? 7.174   -10.715 9.311   1.00 19.34 ? 199 MET   A HE3  1 
ATOM   2977 N  N    . ALA   A 1 200 ? 12.743  -8.364  12.271  1.00 14.70 ? 200 ALA   A N    1 
ATOM   2978 C  CA   . ALA   A 1 200 ? 13.936  -7.536  12.362  1.00 15.37 ? 200 ALA   A CA   1 
ATOM   2979 C  C    . ALA   A 1 200 ? 14.629  -7.693  13.707  1.00 15.52 ? 200 ALA   A C    1 
ATOM   2980 O  O    . ALA   A 1 200 ? 15.853  -7.527  13.798  1.00 16.36 ? 200 ALA   A O    1 
ATOM   2981 C  CB   . ALA   A 1 200 ? 13.582  -6.068  12.135  1.00 16.67 ? 200 ALA   A CB   1 
ATOM   2982 H  H    . ALA   A 1 200 ? 12.008  -7.920  12.224  1.00 17.66 ? 200 ALA   A H    1 
ATOM   2983 H  HA   . ALA   A 1 200 ? 14.560  -7.805  11.670  1.00 18.47 ? 200 ALA   A HA   1 
ATOM   2984 H  HB1  . ALA   A 1 200 ? 14.390  -5.535  12.200  1.00 20.03 ? 200 ALA   A HB1  1 
ATOM   2985 H  HB2  . ALA   A 1 200 ? 13.191  -5.971  11.253  1.00 20.03 ? 200 ALA   A HB2  1 
ATOM   2986 H  HB3  . ALA   A 1 200 ? 12.946  -5.789  12.812  1.00 20.03 ? 200 ALA   A HB3  1 
ATOM   2987 N  N    . ALA   A 1 201 ? 13.873  -7.985  14.764  1.00 15.10 ? 201 ALA   A N    1 
ATOM   2988 C  CA   . ALA   A 1 201 ? 14.496  -8.299  16.045  1.00 15.43 ? 201 ALA   A CA   1 
ATOM   2989 C  C    . ALA   A 1 201 ? 15.427  -9.492  15.903  1.00 16.07 ? 201 ALA   A C    1 
ATOM   2990 O  O    . ALA   A 1 201 ? 16.560  -9.481  16.407  1.00 16.66 ? 201 ALA   A O    1 
ATOM   2991 C  CB   . ALA   A 1 201 ? 13.423  -8.577  17.098  1.00 14.55 ? 201 ALA   A CB   1 
ATOM   2992 H  H    . ALA   A 1 201 ? 13.013  -8.008  14.766  1.00 18.14 ? 201 ALA   A H    1 
ATOM   2993 H  HA   . ALA   A 1 201 ? 15.021  -7.538  16.340  1.00 18.53 ? 201 ALA   A HA   1 
ATOM   2994 H  HB1  . ALA   A 1 201 ? 13.855  -8.783  17.942  1.00 17.47 ? 201 ALA   A HB1  1 
ATOM   2995 H  HB2  . ALA   A 1 201 ? 12.865  -7.790  17.195  1.00 17.47 ? 201 ALA   A HB2  1 
ATOM   2996 H  HB3  . ALA   A 1 201 ? 12.885  -9.331  16.809  1.00 17.47 ? 201 ALA   A HB3  1 
ATOM   2997 N  N    . GLN   A 1 202 ? 14.958  -10.543 15.220  1.00 15.66 ? 202 GLN   A N    1 
ATOM   2998 C  CA   . GLN   A 1 202 ? 15.791  -11.724 14.964  1.00 17.99 ? 202 GLN   A CA   1 
ATOM   2999 C  C    . GLN   A 1 202 ? 16.989  -11.359 14.106  1.00 18.14 ? 202 GLN   A C    1 
ATOM   3000 O  O    . GLN   A 1 202 ? 18.109  -11.807 14.370  1.00 18.29 ? 202 GLN   A O    1 
ATOM   3001 C  CB   . GLN   A 1 202 ? 14.955  -12.790 14.248  1.00 16.22 ? 202 GLN   A CB   1 
ATOM   3002 C  CG   . GLN   A 1 202 ? 13.701  -13.162 14.990  1.00 16.45 ? 202 GLN   A CG   1 
ATOM   3003 C  CD   . GLN   A 1 202 ? 13.909  -13.654 16.405  1.00 19.16 ? 202 GLN   A CD   1 
ATOM   3004 O  OE1  . GLN   A 1 202 ? 14.758  -14.522 16.663  1.00 17.48 ? 202 GLN   A OE1  1 
ATOM   3005 N  NE2  . GLN   A 1 202 ? 13.210  -13.042 17.347  1.00 22.11 ? 202 GLN   A NE2  1 
ATOM   3006 H  H    . GLN   A 1 202 ? 14.164  -10.594 14.894  1.00 18.81 ? 202 GLN   A H    1 
ATOM   3007 H  HA   . GLN   A 1 202 ? 16.110  -12.089 15.804  1.00 21.60 ? 202 GLN   A HA   1 
ATOM   3008 H  HB2  . GLN   A 1 202 ? 14.700  -12.458 13.373  1.00 19.49 ? 202 GLN   A HB2  1 
ATOM   3009 H  HB3  . GLN   A 1 202 ? 15.488  -13.594 14.156  1.00 19.49 ? 202 GLN   A HB3  1 
ATOM   3010 H  HG2  . GLN   A 1 202 ? 13.122  -12.385 15.032  1.00 19.76 ? 202 GLN   A HG2  1 
ATOM   3011 H  HG3  . GLN   A 1 202 ? 13.255  -13.870 14.500  1.00 19.76 ? 202 GLN   A HG3  1 
ATOM   3012 H  HE21 . GLN   A 1 202 ? 12.641  -12.433 17.134  1.00 26.56 ? 202 GLN   A HE21 1 
ATOM   3013 H  HE22 . GLN   A 1 202 ? 13.297  -13.279 18.169  1.00 26.56 ? 202 GLN   A HE22 1 
ATOM   3014 N  N    . ALA   A 1 203 ? 16.773  -10.562 13.054  1.00 18.60 ? 203 ALA   A N    1 
ATOM   3015 C  CA   . ALA   A 1 203 ? 17.875  -10.210 12.164  1.00 17.75 ? 203 ALA   A CA   1 
ATOM   3016 C  C    . ALA   A 1 203 ? 18.954  -9.433  12.906  1.00 20.33 ? 203 ALA   A C    1 
ATOM   3017 O  O    . ALA   A 1 203 ? 20.149  -9.639  12.666  1.00 22.11 ? 203 ALA   A O    1 
ATOM   3018 C  CB   . ALA   A 1 203 ? 17.350  -9.407  10.974  1.00 18.68 ? 203 ALA   A CB   1 
ATOM   3019 H  H    . ALA   A 1 203 ? 16.013  -10.220 12.840  1.00 22.34 ? 203 ALA   A H    1 
ATOM   3020 H  HA   . ALA   A 1 203 ? 18.276  -11.024 11.822  1.00 21.32 ? 203 ALA   A HA   1 
ATOM   3021 H  HB1  . ALA   A 1 203 ? 18.093  -9.181  10.393  1.00 22.44 ? 203 ALA   A HB1  1 
ATOM   3022 H  HB2  . ALA   A 1 203 ? 16.704  -9.945  10.491  1.00 22.44 ? 203 ALA   A HB2  1 
ATOM   3023 H  HB3  . ALA   A 1 203 ? 16.928  -8.597  11.302  1.00 22.44 ? 203 ALA   A HB3  1 
ATOM   3024 N  N    . ALA   A 1 204 ? 18.563  -8.534  13.814  1.00 18.40 ? 204 ALA   A N    1 
ATOM   3025 C  CA   . ALA   A 1 204 ? 19.560  -7.794  14.588  1.00 18.03 ? 204 ALA   A CA   1 
ATOM   3026 C  C    . ALA   A 1 204 ? 20.404  -8.744  15.430  1.00 22.05 ? 204 ALA   A C    1 
ATOM   3027 O  O    . ALA   A 1 204 ? 21.633  -8.615  15.487  1.00 20.95 ? 204 ALA   A O    1 
ATOM   3028 C  CB   . ALA   A 1 204 ? 18.878  -6.751  15.483  1.00 18.53 ? 204 ALA   A CB   1 
ATOM   3029 H  H    . ALA   A 1 204 ? 17.746  -8.338  13.997  1.00 22.09 ? 204 ALA   A H    1 
ATOM   3030 H  HA   . ALA   A 1 204 ? 20.152  -7.326  13.978  1.00 21.66 ? 204 ALA   A HA   1 
ATOM   3031 H  HB1  . ALA   A 1 204 ? 19.557  -6.274  15.985  1.00 22.25 ? 204 ALA   A HB1  1 
ATOM   3032 H  HB2  . ALA   A 1 204 ? 18.383  -6.132  14.924  1.00 22.25 ? 204 ALA   A HB2  1 
ATOM   3033 H  HB3  . ALA   A 1 204 ? 18.273  -7.204  16.091  1.00 22.25 ? 204 ALA   A HB3  1 
ATOM   3034 N  N    . GLU   A 1 205 ? 19.761  -9.702  16.104  1.00 17.99 ? 205 GLU   A N    1 
ATOM   3035 C  CA   . GLU   A 1 205 ? 20.500  -10.693 16.887  1.00 19.42 ? 205 GLU   A CA   1 
ATOM   3036 C  C    . GLU   A 1 205 ? 21.448  -11.490 16.005  1.00 21.66 ? 205 GLU   A C    1 
ATOM   3037 O  O    . GLU   A 1 205 ? 22.618  -11.711 16.360  1.00 22.05 ? 205 GLU   A O    1 
ATOM   3038 C  CB   . GLU   A 1 205 ? 19.531  -11.643 17.595  1.00 20.45 ? 205 GLU   A CB   1 
ATOM   3039 C  CG   . GLU   A 1 205 ? 18.739  -10.976 18.698  1.00 19.07 ? 205 GLU   A CG   1 
ATOM   3040 C  CD   . GLU   A 1 205 ? 17.807  -11.919 19.447  1.00 21.34 ? 205 GLU   A CD   1 
ATOM   3041 O  OE1  . GLU   A 1 205 ? 17.825  -13.147 19.210  1.00 22.28 ? 205 GLU   A OE1  1 
ATOM   3042 O  OE2  . GLU   A 1 205 ? 17.057  -11.406 20.305  1.00 18.79 ? 205 GLU   A OE2  1 
ATOM   3043 H  H    . GLU   A 1 205 ? 18.907  -9.798  16.124  1.00 21.60 ? 205 GLU   A H    1 
ATOM   3044 H  HA   . GLU   A 1 205 ? 21.026  -10.238 17.563  1.00 23.33 ? 205 GLU   A HA   1 
ATOM   3045 H  HB2  . GLU   A 1 205 ? 18.901  -11.992 16.945  1.00 24.56 ? 205 GLU   A HB2  1 
ATOM   3046 H  HB3  . GLU   A 1 205 ? 20.036  -12.371 17.989  1.00 24.56 ? 205 GLU   A HB3  1 
ATOM   3047 H  HG2  . GLU   A 1 205 ? 19.358  -10.598 19.342  1.00 22.90 ? 205 GLU   A HG2  1 
ATOM   3048 H  HG3  . GLU   A 1 205 ? 18.198  -10.271 18.311  1.00 22.90 ? 205 GLU   A HG3  1 
ATOM   3049 N  N    . TYR   A 1 206 ? 20.954  -11.941 14.857  1.00 20.85 ? 206 TYR   A N    1 
ATOM   3050 C  CA   . TYR   A 1 206 ? 21.774  -12.707 13.925  1.00 27.57 ? 206 TYR   A CA   1 
ATOM   3051 C  C    . TYR   A 1 206 ? 22.975  -11.900 13.462  1.00 29.51 ? 206 TYR   A C    1 
ATOM   3052 O  O    . TYR   A 1 206 ? 24.098  -12.417 13.424  1.00 32.93 ? 206 TYR   A O    1 
ATOM   3053 C  CB   . TYR   A 1 206 ? 20.905  -13.136 12.749  1.00 24.96 ? 206 TYR   A CB   1 
ATOM   3054 C  CG   . TYR   A 1 206 ? 21.392  -14.348 12.005  1.00 34.62 ? 206 TYR   A CG   1 
ATOM   3055 C  CD1  . TYR   A 1 206 ? 21.309  -15.609 12.581  1.00 33.91 ? 206 TYR   A CD1  1 
ATOM   3056 C  CD2  . TYR   A 1 206 ? 21.942  -14.241 10.736  1.00 45.00 ? 206 TYR   A CD2  1 
ATOM   3057 C  CE1  . TYR   A 1 206 ? 21.747  -16.732 11.908  1.00 44.78 ? 206 TYR   A CE1  1 
ATOM   3058 C  CE2  . TYR   A 1 206 ? 22.379  -15.362 10.052  1.00 48.64 ? 206 TYR   A CE2  1 
ATOM   3059 C  CZ   . TYR   A 1 206 ? 22.284  -16.606 10.646  1.00 54.07 ? 206 TYR   A CZ   1 
ATOM   3060 O  OH   . TYR   A 1 206 ? 22.720  -17.731 9.984   1.00 67.13 ? 206 TYR   A OH   1 
ATOM   3061 H  H    . TYR   A 1 206 ? 20.145  -11.816 14.594  1.00 25.03 ? 206 TYR   A H    1 
ATOM   3062 H  HA   . TYR   A 1 206 ? 22.099  -13.506 14.369  1.00 33.10 ? 206 TYR   A HA   1 
ATOM   3063 H  HB2  . TYR   A 1 206 ? 20.015  -13.335 13.079  1.00 29.98 ? 206 TYR   A HB2  1 
ATOM   3064 H  HB3  . TYR   A 1 206 ? 20.860  -12.403 12.115  1.00 29.98 ? 206 TYR   A HB3  1 
ATOM   3065 H  HD1  . TYR   A 1 206 ? 20.944  -15.700 13.432  1.00 40.71 ? 206 TYR   A HD1  1 
ATOM   3066 H  HD2  . TYR   A 1 206 ? 22.004  -13.405 10.333  1.00 54.01 ? 206 TYR   A HD2  1 
ATOM   3067 H  HE1  . TYR   A 1 206 ? 21.682  -17.570 12.306  1.00 53.75 ? 206 TYR   A HE1  1 
ATOM   3068 H  HE2  . TYR   A 1 206 ? 22.744  -15.277 9.201   1.00 58.39 ? 206 TYR   A HE2  1 
ATOM   3069 H  HH   . TYR   A 1 206 ? 22.598  -18.411 10.462  1.00 80.58 ? 206 TYR   A HH   1 
ATOM   3070 N  N    . TYR   A 1 207 ? 22.768  -10.623 13.134  1.00 26.22 ? 207 TYR   A N    1 
ATOM   3071 C  CA   . TYR   A 1 207 ? 23.882  -9.781  12.705  1.00 27.97 ? 207 TYR   A CA   1 
ATOM   3072 C  C    . TYR   A 1 207 ? 24.942  -9.680  13.800  1.00 29.84 ? 207 TYR   A C    1 
ATOM   3073 O  O    . TYR   A 1 207 ? 26.145  -9.770  13.518  1.00 34.60 ? 207 TYR   A O    1 
ATOM   3074 C  CB   . TYR   A 1 207 ? 23.366  -8.386  12.321  1.00 32.00 ? 207 TYR   A CB   1 
ATOM   3075 C  CG   . TYR   A 1 207 ? 24.458  -7.439  11.863  1.00 30.57 ? 207 TYR   A CG   1 
ATOM   3076 C  CD1  . TYR   A 1 207 ? 25.186  -6.689  12.775  1.00 29.55 ? 207 TYR   A CD1  1 
ATOM   3077 C  CD2  . TYR   A 1 207 ? 24.756  -7.293  10.512  1.00 32.45 ? 207 TYR   A CD2  1 
ATOM   3078 C  CE1  . TYR   A 1 207 ? 26.193  -5.833  12.361  1.00 32.81 ? 207 TYR   A CE1  1 
ATOM   3079 C  CE2  . TYR   A 1 207 ? 25.752  -6.427  10.086  1.00 27.91 ? 207 TYR   A CE2  1 
ATOM   3080 C  CZ   . TYR   A 1 207 ? 26.471  -5.703  11.019  1.00 34.18 ? 207 TYR   A CZ   1 
ATOM   3081 O  OH   . TYR   A 1 207 ? 27.469  -4.842  10.619  1.00 35.96 ? 207 TYR   A OH   1 
ATOM   3082 H  H    . TYR   A 1 207 ? 22.005  -10.227 13.151  1.00 31.49 ? 207 TYR   A H    1 
ATOM   3083 H  HA   . TYR   A 1 207 ? 24.295  -10.176 11.921  1.00 33.59 ? 207 TYR   A HA   1 
ATOM   3084 H  HB2  . TYR   A 1 207 ? 22.729  -8.479  11.596  1.00 38.42 ? 207 TYR   A HB2  1 
ATOM   3085 H  HB3  . TYR   A 1 207 ? 22.932  -7.989  13.092  1.00 38.42 ? 207 TYR   A HB3  1 
ATOM   3086 H  HD1  . TYR   A 1 207 ? 25.007  -6.776  13.683  1.00 35.48 ? 207 TYR   A HD1  1 
ATOM   3087 H  HD2  . TYR   A 1 207 ? 24.277  -7.783  9.883   1.00 38.96 ? 207 TYR   A HD2  1 
ATOM   3088 H  HE1  . TYR   A 1 207 ? 26.672  -5.339  12.987  1.00 39.39 ? 207 TYR   A HE1  1 
ATOM   3089 H  HE2  . TYR   A 1 207 ? 25.944  -6.343  9.180   1.00 33.51 ? 207 TYR   A HE2  1 
ATOM   3090 H  HH   . TYR   A 1 207 ? 27.540  -4.853  9.782   1.00 43.17 ? 207 TYR   A HH   1 
ATOM   3091 N  N    . SER   A 1 208 ? 24.521  -9.505  15.056  1.00 28.12 ? 208 SER   A N    1 
ATOM   3092 C  CA   . SER   A 1 208 ? 25.460  -9.265  16.152  1.00 27.00 ? 208 SER   A CA   1 
ATOM   3093 C  C    . SER   A 1 208 ? 26.229  -10.526 16.513  1.00 34.27 ? 208 SER   A C    1 
ATOM   3094 O  O    . SER   A 1 208 ? 27.463  -10.491 16.645  1.00 30.45 ? 208 SER   A O    1 
ATOM   3095 C  CB   . SER   A 1 208 ? 24.700  -8.727  17.376  1.00 32.96 ? 208 SER   A CB   1 
ATOM   3096 O  OG   . SER   A 1 208 ? 25.564  -8.256  18.398  1.00 34.59 ? 208 SER   A OG   1 
ATOM   3097 H  H    . SER   A 1 208 ? 23.696  -9.521  15.298  1.00 33.76 ? 208 SER   A H    1 
ATOM   3098 H  HA   . SER   A 1 208 ? 26.101  -8.591  15.877  1.00 32.42 ? 208 SER   A HA   1 
ATOM   3099 H  HB2  . SER   A 1 208 ? 24.132  -7.995  17.090  1.00 39.57 ? 208 SER   A HB2  1 
ATOM   3100 H  HB3  . SER   A 1 208 ? 24.153  -9.441  17.739  1.00 39.57 ? 208 SER   A HB3  1 
ATOM   3101 H  HG   . SER   A 1 208 ? 26.061  -8.879  18.664  1.00 41.53 ? 208 SER   A HG   1 
ATOM   3102 N  N    . VAL   A 1 209 ? 25.527  -11.653 16.693  1.00 31.91 ? 209 VAL   A N    1 
ATOM   3103 C  CA   . VAL   A 1 209 ? 26.199  -12.837 17.236  1.00 29.12 ? 209 VAL   A CA   1 
ATOM   3104 C  C    . VAL   A 1 209 ? 26.003  -14.108 16.419  1.00 32.94 ? 209 VAL   A C    1 
ATOM   3105 O  O    . VAL   A 1 209 ? 26.425  -15.204 16.835  1.00 36.72 ? 209 VAL   A O    1 
ATOM   3106 C  CB   . VAL   A 1 209 ? 25.742  -13.111 18.684  1.00 34.66 ? 209 VAL   A CB   1 
ATOM   3107 C  CG1  . VAL   A 1 209 ? 26.198  -12.005 19.613  1.00 38.58 ? 209 VAL   A CG1  1 
ATOM   3108 C  CG2  . VAL   A 1 209 ? 24.218  -13.277 18.770  1.00 30.34 ? 209 VAL   A CG2  1 
ATOM   3109 H  H    . VAL   A 1 209 ? 24.692  -11.755 16.516  1.00 38.32 ? 209 VAL   A H    1 
ATOM   3110 H  HA   . VAL   A 1 209 ? 27.149  -12.668 17.270  1.00 34.97 ? 209 VAL   A HA   1 
ATOM   3111 H  HB   . VAL   A 1 209 ? 26.147  -13.938 18.988  1.00 41.61 ? 209 VAL   A HB   1 
ATOM   3112 H  HG11 . VAL   A 1 209 ? 25.857  -12.181 20.504  1.00 46.31 ? 209 VAL   A HG11 1 
ATOM   3113 H  HG12 . VAL   A 1 209 ? 27.168  -11.985 19.627  1.00 46.31 ? 209 VAL   A HG12 1 
ATOM   3114 H  HG13 . VAL   A 1 209 ? 25.854  -11.159 19.288  1.00 46.31 ? 209 VAL   A HG13 1 
ATOM   3115 H  HG21 . VAL   A 1 209 ? 23.981  -13.545 19.672  1.00 36.43 ? 209 VAL   A HG21 1 
ATOM   3116 H  HG22 . VAL   A 1 209 ? 23.796  -12.430 18.556  1.00 36.43 ? 209 VAL   A HG22 1 
ATOM   3117 H  HG23 . VAL   A 1 209 ? 23.935  -13.956 18.139  1.00 36.43 ? 209 VAL   A HG23 1 
ATOM   3118 N  N    . GLY   A 1 210 ? 25.383  -13.985 15.252  1.00 27.27 ? 210 GLY   A N    1 
ATOM   3119 C  CA   . GLY   A 1 210 ? 25.227  -15.159 14.416  1.00 28.57 ? 210 GLY   A CA   1 
ATOM   3120 C  C    . GLY   A 1 210 ? 24.205  -16.166 14.893  1.00 37.77 ? 210 GLY   A C    1 
ATOM   3121 O  O    . GLY   A 1 210 ? 24.176  -17.291 14.387  1.00 37.07 ? 210 GLY   A O    1 
ATOM   3122 H  H    . GLY   A 1 210 ? 25.054  -13.258 14.931  1.00 32.74 ? 210 GLY   A H    1 
ATOM   3123 H  HA2  . GLY   A 1 210 ? 24.971  -14.876 13.524  1.00 34.30 ? 210 GLY   A HA2  1 
ATOM   3124 H  HA3  . GLY   A 1 210 ? 26.082  -15.612 14.351  1.00 34.30 ? 210 GLY   A HA3  1 
ATOM   3125 N  N    . LYS   A 1 211 ? 23.364  -15.792 15.857  1.00 29.10 ? 211 LYS   A N    1 
ATOM   3126 C  CA   . LYS   A 1 211 ? 22.322  -16.668 16.368  1.00 30.26 ? 211 LYS   A CA   1 
ATOM   3127 C  C    . LYS   A 1 211 ? 21.177  -15.794 16.863  1.00 25.39 ? 211 LYS   A C    1 
ATOM   3128 O  O    . LYS   A 1 211 ? 21.370  -14.622 17.193  1.00 24.80 ? 211 LYS   A O    1 
ATOM   3129 C  CB   . LYS   A 1 211 ? 22.821  -17.556 17.514  1.00 31.09 ? 211 LYS   A CB   1 
ATOM   3130 C  CG   . LYS   A 1 211 ? 23.990  -16.958 18.283  1.00 46.07 ? 211 LYS   A CG   1 
ATOM   3131 C  CD   . LYS   A 1 211 ? 24.508  -17.881 19.384  1.00 47.72 ? 211 LYS   A CD   1 
ATOM   3132 C  CE   . LYS   A 1 211 ? 23.783  -17.658 20.709  1.00 59.63 ? 211 LYS   A CE   1 
ATOM   3133 N  NZ   . LYS   A 1 211 ? 23.887  -16.245 21.171  1.00 72.53 ? 211 LYS   A NZ   1 
ATOM   3134 H  H    . LYS   A 1 211 ? 23.380  -15.020 16.236  1.00 34.94 ? 211 LYS   A H    1 
ATOM   3135 H  HA   . LYS   A 1 211 ? 21.993  -17.237 15.654  1.00 36.33 ? 211 LYS   A HA   1 
ATOM   3136 H  HB2  . LYS   A 1 211 ? 22.094  -17.697 18.141  1.00 37.33 ? 211 LYS   A HB2  1 
ATOM   3137 H  HB3  . LYS   A 1 211 ? 23.110  -18.407 17.148  1.00 37.33 ? 211 LYS   A HB3  1 
ATOM   3138 H  HG2  . LYS   A 1 211 ? 24.725  -16.799 17.671  1.00 55.30 ? 211 LYS   A HG2  1 
ATOM   3139 H  HG3  . LYS   A 1 211 ? 23.708  -16.123 18.685  1.00 55.30 ? 211 LYS   A HG3  1 
ATOM   3140 H  HD2  . LYS   A 1 211 ? 24.371  -18.803 19.116  1.00 57.29 ? 211 LYS   A HD2  1 
ATOM   3141 H  HD3  . LYS   A 1 211 ? 25.453  -17.710 19.524  1.00 57.29 ? 211 LYS   A HD3  1 
ATOM   3142 H  HE2  . LYS   A 1 211 ? 22.843  -17.871 20.598  1.00 71.58 ? 211 LYS   A HE2  1 
ATOM   3143 H  HE3  . LYS   A 1 211 ? 24.177  -18.228 21.388  1.00 71.58 ? 211 LYS   A HE3  1 
ATOM   3144 H  HZ1  . LYS   A 1 211 ? 23.366  -15.721 20.675  1.00 87.06 ? 211 LYS   A HZ1  1 
ATOM   3145 H  HZ2  . LYS   A 1 211 ? 23.629  -16.185 22.021  1.00 87.06 ? 211 LYS   A HZ2  1 
ATOM   3146 H  HZ3  . LYS   A 1 211 ? 24.729  -15.965 21.105  1.00 87.06 ? 211 LYS   A HZ3  1 
ATOM   3147 N  N    . ASN   A 1 212 ? 19.988  -16.386 16.950  1.00 26.57 ? 212 ASN   A N    1 
ATOM   3148 C  CA   . ASN   A 1 212 ? 18.785  -15.661 17.343  1.00 21.73 ? 212 ASN   A CA   1 
ATOM   3149 C  C    . ASN   A 1 212 ? 17.872  -16.608 18.099  1.00 21.33 ? 212 ASN   A C    1 
ATOM   3150 O  O    . ASN   A 1 212 ? 17.921  -17.829 17.919  1.00 23.71 ? 212 ASN   A O    1 
ATOM   3151 C  CB   . ASN   A 1 212 ? 18.137  -15.039 16.096  1.00 18.58 ? 212 ASN   A CB   1 
ATOM   3152 C  CG   . ASN   A 1 212 ? 17.664  -16.084 15.118  1.00 25.79 ? 212 ASN   A CG   1 
ATOM   3153 O  OD1  . ASN   A 1 212 ? 18.472  -16.662 14.388  1.00 26.57 ? 212 ASN   A OD1  1 
ATOM   3154 N  ND2  . ASN   A 1 212 ? 16.355  -16.299 15.049  1.00 22.57 ? 212 ASN   A ND2  1 
ATOM   3155 H  H    . ASN   A 1 212 ? 19.852  -17.219 16.784  1.00 31.90 ? 212 ASN   A H    1 
ATOM   3156 H  HA   . ASN   A 1 212 ? 19.031  -14.940 17.943  1.00 26.10 ? 212 ASN   A HA   1 
ATOM   3157 H  HB2  . ASN   A 1 212 ? 17.370  -14.510 16.367  1.00 22.32 ? 212 ASN   A HB2  1 
ATOM   3158 H  HB3  . ASN   A 1 212 ? 18.788  -14.478 15.646  1.00 22.32 ? 212 ASN   A HB3  1 
ATOM   3159 H  HD21 . ASN   A 1 212 ? 16.045  -16.882 14.500  1.00 27.10 ? 212 ASN   A HD21 1 
ATOM   3160 H  HD22 . ASN   A 1 212 ? 15.820  -15.869 15.567  1.00 27.10 ? 212 ASN   A HD22 1 
ATOM   3161 N  N    . SER   A 1 213 ? 17.040  -16.027 18.969  1.00 19.36 ? 213 SER   A N    1 
ATOM   3162 C  CA   . SER   A 1 213 ? 16.293  -16.808 19.946  1.00 19.59 ? 213 SER   A CA   1 
ATOM   3163 C  C    . SER   A 1 213 ? 14.964  -17.352 19.416  1.00 18.80 ? 213 SER   A C    1 
ATOM   3164 O  O    . SER   A 1 213 ? 14.386  -18.239 20.054  1.00 20.37 ? 213 SER   A O    1 
ATOM   3165 C  CB   . SER   A 1 213 ? 15.960  -15.951 21.168  1.00 20.96 ? 213 SER   A CB   1 
ATOM   3166 O  OG   . SER   A 1 213 ? 15.040  -14.937 20.772  1.00 19.82 ? 213 SER   A OG   1 
ATOM   3167 H  H    . SER   A 1 213 ? 16.894  -15.181 19.010  1.00 23.25 ? 213 SER   A H    1 
ATOM   3168 H  HA   . SER   A 1 213 ? 16.834  -17.558 20.238  1.00 23.52 ? 213 SER   A HA   1 
ATOM   3169 H  HB2  . SER   A 1 213 ? 15.554  -16.507 21.852  1.00 25.17 ? 213 SER   A HB2  1 
ATOM   3170 H  HB3  . SER   A 1 213 ? 16.771  -15.538 21.504  1.00 25.17 ? 213 SER   A HB3  1 
ATOM   3171 H  HG   . SER   A 1 213 ? 14.844  -14.454 21.431  1.00 23.80 ? 213 SER   A HG   1 
ATOM   3172 N  N    . TRP   A 1 214 ? 14.460  -16.810 18.306  1.00 17.14 ? 214 TRP   A N    1 
ATOM   3173 C  CA   . TRP   A 1 214 ? 13.112  -17.066 17.782  1.00 18.54 ? 214 TRP   A CA   1 
ATOM   3174 C  C    . TRP   A 1 214 ? 12.027  -16.638 18.765  1.00 19.56 ? 214 TRP   A C    1 
ATOM   3175 O  O    . TRP   A 1 214 ? 10.879  -17.077 18.656  1.00 18.38 ? 214 TRP   A O    1 
ATOM   3176 C  CB   . TRP   A 1 214 ? 12.919  -18.542 17.380  1.00 18.20 ? 214 TRP   A CB   1 
ATOM   3177 C  CG   . TRP   A 1 214 ? 13.714  -18.892 16.166  1.00 19.47 ? 214 TRP   A CG   1 
ATOM   3178 C  CD1  . TRP   A 1 214 ? 14.693  -19.837 16.078  1.00 24.09 ? 214 TRP   A CD1  1 
ATOM   3179 C  CD2  . TRP   A 1 214 ? 13.617  -18.292 14.865  1.00 18.56 ? 214 TRP   A CD2  1 
ATOM   3180 N  NE1  . TRP   A 1 214 ? 15.225  -19.848 14.808  1.00 24.13 ? 214 TRP   A NE1  1 
ATOM   3181 C  CE2  . TRP   A 1 214 ? 14.574  -18.919 14.043  1.00 23.19 ? 214 TRP   A CE2  1 
ATOM   3182 C  CE3  . TRP   A 1 214 ? 12.814  -17.287 14.317  1.00 20.64 ? 214 TRP   A CE3  1 
ATOM   3183 C  CZ2  . TRP   A 1 214 ? 14.754  -18.569 12.701  1.00 25.08 ? 214 TRP   A CZ2  1 
ATOM   3184 C  CZ3  . TRP   A 1 214 ? 12.993  -16.944 12.985  1.00 22.88 ? 214 TRP   A CZ3  1 
ATOM   3185 C  CH2  . TRP   A 1 214 ? 13.953  -17.586 12.193  1.00 25.75 ? 214 TRP   A CH2  1 
ATOM   3186 H  H    . TRP   A 1 214 ? 14.903  -16.262 17.813  1.00 20.59 ? 214 TRP   A H    1 
ATOM   3187 H  HA   . TRP   A 1 214 ? 12.995  -16.532 16.981  1.00 22.26 ? 214 TRP   A HA   1 
ATOM   3188 H  HB2  . TRP   A 1 214 ? 13.208  -19.114 18.107  1.00 21.86 ? 214 TRP   A HB2  1 
ATOM   3189 H  HB3  . TRP   A 1 214 ? 11.983  -18.700 17.183  1.00 21.86 ? 214 TRP   A HB3  1 
ATOM   3190 H  HD1  . TRP   A 1 214 ? 14.979  -20.375 16.781  1.00 28.93 ? 214 TRP   A HD1  1 
ATOM   3191 H  HE1  . TRP   A 1 214 ? 15.851  -20.370 14.534  1.00 28.97 ? 214 TRP   A HE1  1 
ATOM   3192 H  HE3  . TRP   A 1 214 ? 12.179  -16.851 14.838  1.00 24.79 ? 214 TRP   A HE3  1 
ATOM   3193 H  HZ2  . TRP   A 1 214 ? 15.386  -18.999 12.171  1.00 30.12 ? 214 TRP   A HZ2  1 
ATOM   3194 H  HZ3  . TRP   A 1 214 ? 12.465  -16.276 12.611  1.00 27.48 ? 214 TRP   A HZ3  1 
ATOM   3195 H  HH2  . TRP   A 1 214 ? 14.047  -17.338 11.302  1.00 30.92 ? 214 TRP   A HH2  1 
ATOM   3196 N  N    . GLN   A 1 215 ? 12.374  -15.782 19.720  1.00 17.13 ? 215 GLN   A N    1 
ATOM   3197 C  CA   . GLN   A 1 215 ? 11.440  -15.243 20.693  1.00 16.70 ? 215 GLN   A CA   1 
ATOM   3198 C  C    . GLN   A 1 215 ? 11.634  -13.737 20.731  1.00 16.08 ? 215 GLN   A C    1 
ATOM   3199 O  O    . GLN   A 1 215 ? 12.665  -13.216 20.301  1.00 17.67 ? 215 GLN   A O    1 
ATOM   3200 C  CB   . GLN   A 1 215 ? 11.671  -15.844 22.077  1.00 17.35 ? 215 GLN   A CB   1 
ATOM   3201 C  CG   . GLN   A 1 215 ? 11.492  -17.348 22.109  1.00 18.76 ? 215 GLN   A CG   1 
ATOM   3202 C  CD   . GLN   A 1 215 ? 11.763  -17.950 23.470  1.00 20.61 ? 215 GLN   A CD   1 
ATOM   3203 O  OE1  . GLN   A 1 215 ? 12.145  -17.253 24.414  1.00 23.61 ? 215 GLN   A OE1  1 
ATOM   3204 N  NE2  . GLN   A 1 215 ? 11.574  -19.259 23.579  1.00 24.29 ? 215 GLN   A NE2  1 
ATOM   3205 H  H    . GLN   A 1 215 ? 13.175  -15.488 19.826  1.00 20.58 ? 215 GLN   A H    1 
ATOM   3206 H  HA   . GLN   A 1 215 ? 10.529  -15.433 20.418  1.00 20.06 ? 215 GLN   A HA   1 
ATOM   3207 H  HB2  . GLN   A 1 215 ? 12.577  -15.645 22.360  1.00 20.84 ? 215 GLN   A HB2  1 
ATOM   3208 H  HB3  . GLN   A 1 215 ? 11.037  -15.454 22.699  1.00 20.84 ? 215 GLN   A HB3  1 
ATOM   3209 H  HG2  . GLN   A 1 215 ? 10.578  -17.561 21.865  1.00 22.52 ? 215 GLN   A HG2  1 
ATOM   3210 H  HG3  . GLN   A 1 215 ? 12.106  -17.752 21.476  1.00 22.52 ? 215 GLN   A HG3  1 
ATOM   3211 H  HE21 . GLN   A 1 215 ? 11.308  -19.713 22.899  1.00 29.16 ? 215 GLN   A HE21 1 
ATOM   3212 H  HE22 . GLN   A 1 215 ? 11.714  -19.653 24.331  1.00 29.16 ? 215 GLN   A HE22 1 
ATOM   3213 N  N    . ILE   A 1 216 ? 10.620  -13.039 21.231  1.00 14.90 ? 216 ILE   A N    1 
ATOM   3214 C  CA   . ILE   A 1 216 ? 10.665  -11.594 21.411  1.00 13.18 ? 216 ILE   A CA   1 
ATOM   3215 C  C    . ILE   A 1 216 ? 10.670  -11.309 22.903  1.00 17.23 ? 216 ILE   A C    1 
ATOM   3216 O  O    . ILE   A 1 216 ? 9.761   -11.730 23.628  1.00 17.05 ? 216 ILE   A O    1 
ATOM   3217 C  CB   . ILE   A 1 216 ? 9.485   -10.890 20.717  1.00 15.05 ? 216 ILE   A CB   1 
ATOM   3218 C  CG1  . ILE   A 1 216 ? 9.457   -11.234 19.223  1.00 14.73 ? 216 ILE   A CG1  1 
ATOM   3219 C  CG2  . ILE   A 1 216 ? 9.571   -9.393  20.936  1.00 17.10 ? 216 ILE   A CG2  1 
ATOM   3220 C  CD1  . ILE   A 1 216 ? 10.616  -10.698 18.412  1.00 16.46 ? 216 ILE   A CD1  1 
ATOM   3221 H  H    . ILE   A 1 216 ? 9.876   -13.391 21.480  1.00 17.90 ? 216 ILE   A H    1 
ATOM   3222 H  HA   . ILE   A 1 216 ? 11.489  -11.247 21.036  1.00 15.84 ? 216 ILE   A HA   1 
ATOM   3223 H  HB   . ILE   A 1 216 ? 8.662   -11.209 21.118  1.00 18.08 ? 216 ILE   A HB   1 
ATOM   3224 H  HG12 . ILE   A 1 216 ? 9.454   -12.199 19.126  1.00 17.69 ? 216 ILE   A HG12 1 
ATOM   3225 H  HG13 . ILE   A 1 216 ? 8.643   -10.869 18.841  1.00 17.69 ? 216 ILE   A HG13 1 
ATOM   3226 H  HG21 . ILE   A 1 216 ? 8.953   -8.952  20.332  1.00 20.54 ? 216 ILE   A HG21 1 
ATOM   3227 H  HG22 . ILE   A 1 216 ? 9.334   -9.191  21.855  1.00 20.54 ? 216 ILE   A HG22 1 
ATOM   3228 H  HG23 . ILE   A 1 216 ? 10.477  -9.099  20.754  1.00 20.54 ? 216 ILE   A HG23 1 
ATOM   3229 H  HD11 . ILE   A 1 216 ? 10.522  -10.998 17.495  1.00 19.78 ? 216 ILE   A HD11 1 
ATOM   3230 H  HD12 . ILE   A 1 216 ? 10.605  -9.729  18.444  1.00 19.78 ? 216 ILE   A HD12 1 
ATOM   3231 H  HD13 . ILE   A 1 216 ? 11.446  -11.033 18.785  1.00 19.78 ? 216 ILE   A HD13 1 
ATOM   3232 N  N    . GLY   A 1 217 ? 11.714  -10.639 23.367  1.00 15.72 ? 217 GLY   A N    1 
ATOM   3233 C  CA   . GLY   A 1 217 ? 11.785  -10.170 24.727  1.00 17.53 ? 217 GLY   A CA   1 
ATOM   3234 C  C    . GLY   A 1 217 ? 12.180  -11.127 25.845  1.00 19.94 ? 217 GLY   A C    1 
ATOM   3235 O  O    . GLY   A 1 217 ? 12.091  -10.737 27.012  1.00 20.05 ? 217 GLY   A O    1 
ATOM   3236 H  H    . GLY   A 1 217 ? 12.407  -10.442 22.897  1.00 18.88 ? 217 GLY   A H    1 
ATOM   3237 H  HA2  . GLY   A 1 217 ? 12.416  -9.433  24.753  1.00 21.05 ? 217 GLY   A HA2  1 
ATOM   3238 H  HA3  . GLY   A 1 217 ? 10.915  -9.810  24.961  1.00 21.05 ? 217 GLY   A HA3  1 
ATOM   3239 N  N    . PRO   A 1 218 ? 12.636  -12.362 25.577  1.00 16.42 ? 218 PRO   A N    1 
ATOM   3240 C  CA   . PRO   A 1 218 ? 13.026  -13.195 26.732  1.00 17.48 ? 218 PRO   A CA   1 
ATOM   3241 C  C    . PRO   A 1 218 ? 14.098  -12.523 27.574  1.00 19.35 ? 218 PRO   A C    1 
ATOM   3242 O  O    . PRO   A 1 218 ? 14.103  -12.674 28.801  1.00 20.90 ? 218 PRO   A O    1 
ATOM   3243 C  CB   . PRO   A 1 218 ? 13.538  -14.497 26.094  1.00 19.40 ? 218 PRO   A CB   1 
ATOM   3244 C  CG   . PRO   A 1 218 ? 13.975  -14.094 24.745  1.00 19.30 ? 218 PRO   A CG   1 
ATOM   3245 C  CD   . PRO   A 1 218 ? 12.951  -13.051 24.309  1.00 16.66 ? 218 PRO   A CD   1 
ATOM   3246 H  HA   . PRO   A 1 218 ? 12.254  -13.388 27.286  1.00 21.00 ? 218 PRO   A HA   1 
ATOM   3247 H  HB2  . PRO   A 1 218 ? 14.283  -14.845 26.609  1.00 23.30 ? 218 PRO   A HB2  1 
ATOM   3248 H  HB3  . PRO   A 1 218 ? 12.818  -15.145 26.045  1.00 23.30 ? 218 PRO   A HB3  1 
ATOM   3249 H  HG2  . PRO   A 1 218 ? 14.864  -13.708 24.789  1.00 23.18 ? 218 PRO   A HG2  1 
ATOM   3250 H  HG3  . PRO   A 1 218 ? 13.960  -14.861 24.152  1.00 23.18 ? 218 PRO   A HG3  1 
ATOM   3251 H  HD2  . PRO   A 1 218 ? 13.354  -12.439 23.675  1.00 20.01 ? 218 PRO   A HD2  1 
ATOM   3252 H  HD3  . PRO   A 1 218 ? 12.160  -13.479 23.945  1.00 20.01 ? 218 PRO   A HD3  1 
ATOM   3253 N  N    . GLU   A 1 219 ? 14.983  -11.747 26.940  1.00 18.90 ? 219 GLU   A N    1 
ATOM   3254 C  CA   . GLU   A 1 219 ? 16.107  -11.131 27.631  1.00 18.74 ? 219 GLU   A CA   1 
ATOM   3255 C  C    . GLU   A 1 219 ? 15.663  -10.016 28.572  1.00 21.98 ? 219 GLU   A C    1 
ATOM   3256 O  O    . GLU   A 1 219 ? 16.453  -9.602  29.430  1.00 23.35 ? 219 GLU   A O    1 
ATOM   3257 C  CB   . GLU   A 1 219 ? 17.116  -10.577 26.614  1.00 18.80 ? 219 GLU   A CB   1 
ATOM   3258 C  CG   . GLU   A 1 219 ? 16.596  -9.440  25.731  1.00 19.56 ? 219 GLU   A CG   1 
ATOM   3259 C  CD   . GLU   A 1 219 ? 15.875  -9.880  24.468  1.00 19.09 ? 219 GLU   A CD   1 
ATOM   3260 O  OE1  . GLU   A 1 219 ? 15.448  -11.047 24.370  1.00 20.41 ? 219 GLU   A OE1  1 
ATOM   3261 O  OE2  . GLU   A 1 219 ? 15.677  -9.013  23.586  1.00 20.14 ? 219 GLU   A OE2  1 
ATOM   3262 H  H    . GLU   A 1 219 ? 14.949  -11.565 26.101  1.00 22.70 ? 219 GLU   A H    1 
ATOM   3263 H  HA   . GLU   A 1 219 ? 16.558  -11.807 28.161  1.00 22.51 ? 219 GLU   A HA   1 
ATOM   3264 H  HB2  . GLU   A 1 219 ? 17.887  -10.241 27.097  1.00 22.58 ? 219 GLU   A HB2  1 
ATOM   3265 H  HB3  . GLU   A 1 219 ? 17.390  -11.300 26.028  1.00 22.58 ? 219 GLU   A HB3  1 
ATOM   3266 H  HG2  . GLU   A 1 219 ? 15.976  -8.901  26.242  1.00 23.49 ? 219 GLU   A HG2  1 
ATOM   3267 H  HG3  . GLU   A 1 219 ? 17.350  -8.894  25.459  1.00 23.49 ? 219 GLU   A HG3  1 
ATOM   3268 N  N    . ILE   A 1 220 ? 14.433  -9.527  28.455  1.00 19.10 ? 220 ILE   A N    1 
ATOM   3269 C  CA   . ILE   A 1 220 ? 13.961  -8.456  29.320  1.00 20.44 ? 220 ILE   A CA   1 
ATOM   3270 C  C    . ILE   A 1 220 ? 12.794  -8.860  30.207  1.00 18.36 ? 220 ILE   A C    1 
ATOM   3271 O  O    . ILE   A 1 220 ? 12.349  -8.044  31.017  1.00 19.62 ? 220 ILE   A O    1 
ATOM   3272 C  CB   . ILE   A 1 220 ? 13.633  -7.185  28.506  1.00 27.33 ? 220 ILE   A CB   1 
ATOM   3273 C  CG1  . ILE   A 1 220 ? 12.628  -7.455  27.384  1.00 21.46 ? 220 ILE   A CG1  1 
ATOM   3274 C  CG2  . ILE   A 1 220 ? 14.924  -6.584  27.917  1.00 23.25 ? 220 ILE   A CG2  1 
ATOM   3275 C  CD1  . ILE   A 1 220 ? 11.215  -7.562  27.824  1.00 25.73 ? 220 ILE   A CD1  1 
ATOM   3276 H  H    . ILE   A 1 220 ? 13.852  -9.802  27.884  1.00 22.94 ? 220 ILE   A H    1 
ATOM   3277 H  HA   . ILE   A 1 220 ? 14.683  -8.215  29.920  1.00 24.54 ? 220 ILE   A HA   1 
ATOM   3278 H  HB   . ILE   A 1 220 ? 13.244  -6.532  29.109  1.00 32.81 ? 220 ILE   A HB   1 
ATOM   3279 H  HG12 . ILE   A 1 220 ? 12.678  -6.724  26.748  1.00 25.77 ? 220 ILE   A HG12 1 
ATOM   3280 H  HG13 . ILE   A 1 220 ? 12.861  -8.284  26.940  1.00 25.77 ? 220 ILE   A HG13 1 
ATOM   3281 H  HG21 . ILE   A 1 220 ? 14.759  -5.659  27.676  1.00 27.92 ? 220 ILE   A HG21 1 
ATOM   3282 H  HG22 . ILE   A 1 220 ? 15.628  -6.631  28.583  1.00 27.92 ? 220 ILE   A HG22 1 
ATOM   3283 H  HG23 . ILE   A 1 220 ? 15.178  -7.090  27.131  1.00 27.92 ? 220 ILE   A HG23 1 
ATOM   3284 H  HD11 . ILE   A 1 220 ? 10.637  -7.413  27.059  1.00 30.90 ? 220 ILE   A HD11 1 
ATOM   3285 H  HD12 . ILE   A 1 220 ? 11.060  -8.449  28.185  1.00 30.90 ? 220 ILE   A HD12 1 
ATOM   3286 H  HD13 . ILE   A 1 220 ? 11.043  -6.890  28.502  1.00 30.90 ? 220 ILE   A HD13 1 
ATOM   3287 N  N    . MET   A 1 221 ? 12.333  -10.115 30.144  1.00 19.54 ? 221 MET   A N    1 
ATOM   3288 C  CA   . MET   A 1 221 ? 11.275  -10.545 31.047  1.00 22.86 ? 221 MET   A CA   1 
ATOM   3289 C  C    . MET   A 1 221 ? 11.919  -10.966 32.380  1.00 21.66 ? 221 MET   A C    1 
ATOM   3290 O  O    . MET   A 1 221 ? 12.861  -11.764 32.391  1.00 23.76 ? 221 MET   A O    1 
ATOM   3291 C  CB   . MET   A 1 221 ? 10.508  -11.730 30.466  1.00 24.35 ? 221 MET   A CB   1 
ATOM   3292 C  CG   . MET   A 1 221 ? 9.594   -11.403 29.287  1.00 27.42 ? 221 MET   A CG   1 
ATOM   3293 S  SD   . MET   A 1 221 ? 8.579   -9.946  29.392  1.00 25.60 ? 221 MET   A SD   1 
ATOM   3294 C  CE   . MET   A 1 221 ? 7.615   -10.400 30.907  1.00 28.13 ? 221 MET   A CE   1 
ATOM   3295 H  H    . MET   A 1 221 ? 12.612  -10.719 29.599  1.00 23.47 ? 221 MET   A H    1 
ATOM   3296 H  HA   . MET   A 1 221 ? 10.657  -9.814  31.202  1.00 27.45 ? 221 MET   A HA   1 
ATOM   3297 H  HB2  . MET   A 1 221 ? 11.150  -12.391 30.162  1.00 29.24 ? 221 MET   A HB2  1 
ATOM   3298 H  HB3  . MET   A 1 221 ? 9.957   -12.113 31.166  1.00 29.24 ? 221 MET   A HB3  1 
ATOM   3299 H  HG2  . MET   A 1 221 ? 10.150  -11.303 28.498  1.00 32.93 ? 221 MET   A HG2  1 
ATOM   3300 H  HG3  . MET   A 1 221 ? 8.995   -12.155 29.158  1.00 32.93 ? 221 MET   A HG3  1 
ATOM   3301 H  HE1  . MET   A 1 221 ? 7.109   -9.626  31.200  1.00 33.77 ? 221 MET   A HE1  1 
ATOM   3302 H  HE2  . MET   A 1 221 ? 7.011   -11.125 30.689  1.00 33.77 ? 221 MET   A HE2  1 
ATOM   3303 H  HE3  . MET   A 1 221 ? 8.229   -10.676 31.605  1.00 33.77 ? 221 MET   A HE3  1 
ATOM   3304 N  N    . LYS   A 1 222 ? 11.405  -10.450 33.499  1.00 20.33 ? 222 LYS   A N    1 
ATOM   3305 C  CA   . LYS   A 1 222 ? 11.960  -10.823 34.798  1.00 20.63 ? 222 LYS   A CA   1 
ATOM   3306 C  C    . LYS   A 1 222 ? 11.704  -12.304 35.074  1.00 25.85 ? 222 LYS   A C    1 
ATOM   3307 O  O    . LYS   A 1 222 ? 10.666  -12.862 34.703  1.00 27.43 ? 222 LYS   A O    1 
ATOM   3308 C  CB   . LYS   A 1 222 ? 11.342  -9.977  35.909  1.00 26.15 ? 222 LYS   A CB   1 
ATOM   3309 C  CG   . LYS   A 1 222 ? 11.616  -8.480  35.795  1.00 29.16 ? 222 LYS   A CG   1 
ATOM   3310 C  CD   . LYS   A 1 222 ? 12.658  -7.982  36.800  1.00 33.93 ? 222 LYS   A CD   1 
ATOM   3311 C  CE   . LYS   A 1 222 ? 12.768  -6.459  36.751  1.00 24.43 ? 222 LYS   A CE   1 
ATOM   3312 N  NZ   . LYS   A 1 222 ? 12.470  -5.786  38.047  1.00 32.91 ? 222 LYS   A NZ   1 
ATOM   3313 H  H    . LYS   A 1 222 ? 10.749  -9.894  33.532  1.00 24.41 ? 222 LYS   A H    1 
ATOM   3314 H  HA   . LYS   A 1 222 ? 12.918  -10.673 34.795  1.00 24.78 ? 222 LYS   A HA   1 
ATOM   3315 H  HB2  . LYS   A 1 222 ? 10.380  -10.101 35.894  1.00 31.40 ? 222 LYS   A HB2  1 
ATOM   3316 H  HB3  . LYS   A 1 222 ? 11.697  -10.277 36.760  1.00 31.40 ? 222 LYS   A HB3  1 
ATOM   3317 H  HG2  . LYS   A 1 222 ? 11.944  -8.286  34.903  1.00 35.01 ? 222 LYS   A HG2  1 
ATOM   3318 H  HG3  . LYS   A 1 222 ? 10.791  -7.997  35.957  1.00 35.01 ? 222 LYS   A HG3  1 
ATOM   3319 H  HD2  . LYS   A 1 222 ? 12.392  -8.241  37.696  1.00 40.73 ? 222 LYS   A HD2  1 
ATOM   3320 H  HD3  . LYS   A 1 222 ? 13.524  -8.360  36.582  1.00 40.73 ? 222 LYS   A HD3  1 
ATOM   3321 H  HE2  . LYS   A 1 222 ? 13.673  -6.220  36.495  1.00 29.34 ? 222 LYS   A HE2  1 
ATOM   3322 H  HE3  . LYS   A 1 222 ? 12.142  -6.122  36.092  1.00 29.34 ? 222 LYS   A HE3  1 
ATOM   3323 H  HZ1  . LYS   A 1 222 ? 12.550  -4.904  37.957  1.00 39.51 ? 222 LYS   A HZ1  1 
ATOM   3324 H  HZ2  . LYS   A 1 222 ? 11.640  -5.976  38.305  1.00 39.51 ? 222 LYS   A HZ2  1 
ATOM   3325 H  HZ3  . LYS   A 1 222 ? 13.038  -6.066  38.672  1.00 39.51 ? 222 LYS   A HZ3  1 
ATOM   3326 N  N    . GLU   A 1 223 ? 12.655  -12.937 35.765  1.00 24.53 ? 223 GLU   A N    1 
ATOM   3327 C  CA   . GLU   A 1 223 ? 12.569  -14.372 36.021  1.00 33.50 ? 223 GLU   A CA   1 
ATOM   3328 C  C    . GLU   A 1 223 ? 11.390  -14.762 36.908  1.00 31.41 ? 223 GLU   A C    1 
ATOM   3329 O  O    . GLU   A 1 223 ? 10.996  -15.935 36.894  1.00 35.23 ? 223 GLU   A O    1 
ATOM   3330 C  CB   . GLU   A 1 223 ? 13.890  -14.861 36.632  1.00 38.30 ? 223 GLU   A CB   1 
ATOM   3331 C  CG   . GLU   A 1 223 ? 15.104  -14.570 35.754  1.00 38.50 ? 223 GLU   A CG   1 
ATOM   3332 C  CD   . GLU   A 1 223 ? 15.887  -13.352 36.200  1.00 41.49 ? 223 GLU   A CD   1 
ATOM   3333 O  OE1  . GLU   A 1 223 ? 15.281  -12.262 36.291  1.00 31.97 ? 223 GLU   A OE1  1 
ATOM   3334 O  OE2  . GLU   A 1 223 ? 17.107  -13.474 36.437  1.00 36.49 ? 223 GLU   A OE2  1 
ATOM   3335 H  H    . GLU   A 1 223 ? 13.354  -12.559 36.093  1.00 29.46 ? 223 GLU   A H    1 
ATOM   3336 H  HA   . GLU   A 1 223 ? 12.455  -14.827 35.172  1.00 40.22 ? 223 GLU   A HA   1 
ATOM   3337 H  HB2  . GLU   A 1 223 ? 14.025  -14.418 37.484  1.00 45.98 ? 223 GLU   A HB2  1 
ATOM   3338 H  HB3  . GLU   A 1 223 ? 13.840  -15.821 36.763  1.00 45.98 ? 223 GLU   A HB3  1 
ATOM   3339 H  HG2  . GLU   A 1 223 ? 15.701  -15.334 35.780  1.00 46.22 ? 223 GLU   A HG2  1 
ATOM   3340 H  HG3  . GLU   A 1 223 ? 14.804  -14.415 34.845  1.00 46.22 ? 223 GLU   A HG3  1 
ATOM   3341 N  N    . ASP   A 1 224 ? 10.799  -13.825 37.660  1.00 27.38 ? 224 ASP   A N    1 
ATOM   3342 C  CA   . ASP   A 1 224 ? 9.617   -14.128 38.463  1.00 25.92 ? 224 ASP   A CA   1 
ATOM   3343 C  C    . ASP   A 1 224 ? 8.318   -13.599 37.852  1.00 28.43 ? 224 ASP   A C    1 
ATOM   3344 O  O    . ASP   A 1 224 ? 7.288   -13.543 38.538  1.00 29.98 ? 224 ASP   A O    1 
ATOM   3345 C  CB   . ASP   A 1 224 ? 9.750   -13.587 39.890  1.00 30.60 ? 224 ASP   A CB   1 
ATOM   3346 C  CG   . ASP   A 1 224 ? 10.417  -12.233 39.941  1.00 42.43 ? 224 ASP   A CG   1 
ATOM   3347 O  OD1  . ASP   A 1 224 ? 10.156  -11.402 39.046  1.00 34.59 ? 224 ASP   A OD1  1 
ATOM   3348 O  OD2  . ASP   A 1 224 ? 11.157  -11.989 40.916  1.00 48.90 ? 224 ASP   A OD2  1 
ATOM   3349 H  H    . ASP   A 1 224 ? 11.064  -13.009 37.711  1.00 32.88 ? 224 ASP   A H    1 
ATOM   3350 H  HA   . ASP   A 1 224 ? 9.530   -15.091 38.531  1.00 31.12 ? 224 ASP   A HA   1 
ATOM   3351 H  HB2  . ASP   A 1 224 ? 8.870   -13.504 40.288  1.00 36.73 ? 224 ASP   A HB2  1 
ATOM   3352 H  HB3  . ASP   A 1 224 ? 10.291  -14.202 40.409  1.00 36.73 ? 224 ASP   A HB3  1 
ATOM   3353 N  N    . SER   A 1 225 ? 8.335   -13.219 36.575  1.00 25.91 ? 225 SER   A N    1 
ATOM   3354 C  CA   . SER   A 1 225 ? 7.124   -12.689 35.962  1.00 27.68 ? 225 SER   A CA   1 
ATOM   3355 C  C    . SER   A 1 225 ? 6.122   -13.781 35.614  1.00 26.70 ? 225 SER   A C    1 
ATOM   3356 O  O    . SER   A 1 225 ? 4.919   -13.509 35.511  1.00 30.88 ? 225 SER   A O    1 
ATOM   3357 C  CB   . SER   A 1 225 ? 7.468   -11.915 34.689  1.00 24.78 ? 225 SER   A CB   1 
ATOM   3358 O  OG   . SER   A 1 225 ? 7.979   -12.776 33.681  1.00 23.80 ? 225 SER   A OG   1 
ATOM   3359 H  H    . SER   A 1 225 ? 9.018   -13.257 36.054  1.00 31.11 ? 225 SER   A H    1 
ATOM   3360 H  HA   . SER   A 1 225 ? 6.698   -12.076 36.581  1.00 33.24 ? 225 SER   A HA   1 
ATOM   3361 H  HB2  . SER   A 1 225 ? 6.665   -11.484 34.357  1.00 29.75 ? 225 SER   A HB2  1 
ATOM   3362 H  HB3  . SER   A 1 225 ? 8.138   -11.246 34.900  1.00 29.75 ? 225 SER   A HB3  1 
ATOM   3363 H  HG   . SER   A 1 225 ? 8.677   -13.156 33.954  1.00 28.58 ? 225 SER   A HG   1 
ATOM   3364 N  N    . GLY   A 1 226 ? 6.595   -15.001 35.401  1.00 27.86 ? 226 GLY   A N    1 
ATOM   3365 C  CA   . GLY   A 1 226 ? 5.754   -16.054 34.889  1.00 30.37 ? 226 GLY   A CA   1 
ATOM   3366 C  C    . GLY   A 1 226 ? 5.660   -16.114 33.384  1.00 28.17 ? 226 GLY   A C    1 
ATOM   3367 O  O    . GLY   A 1 226 ? 4.902   -16.943 32.862  1.00 30.04 ? 226 GLY   A O    1 
ATOM   3368 H  H    . GLY   A 1 226 ? 7.408   -15.241 35.548  1.00 33.45 ? 226 GLY   A H    1 
ATOM   3369 H  HA2  . GLY   A 1 226 ? 6.094   -16.907 35.201  1.00 36.46 ? 226 GLY   A HA2  1 
ATOM   3370 H  HA3  . GLY   A 1 226 ? 4.857   -15.943 35.241  1.00 36.46 ? 226 GLY   A HA3  1 
ATOM   3371 N  N    . TYR   A 1 227 ? 6.396   -15.262 32.675  1.00 25.25 ? 227 TYR   A N    1 
ATOM   3372 C  CA   . TYR   A 1 227 ? 6.447   -15.251 31.219  1.00 23.72 ? 227 TYR   A CA   1 
ATOM   3373 C  C    . TYR   A 1 227 ? 7.893   -15.459 30.800  1.00 24.71 ? 227 TYR   A C    1 
ATOM   3374 O  O    . TYR   A 1 227 ? 8.773   -14.702 31.221  1.00 29.93 ? 227 TYR   A O    1 
ATOM   3375 C  CB   . TYR   A 1 227 ? 5.941   -13.921 30.670  1.00 24.42 ? 227 TYR   A CB   1 
ATOM   3376 C  CG   . TYR   A 1 227 ? 4.507   -13.621 30.993  1.00 30.65 ? 227 TYR   A CG   1 
ATOM   3377 C  CD1  . TYR   A 1 227 ? 3.472   -14.156 30.239  1.00 37.63 ? 227 TYR   A CD1  1 
ATOM   3378 C  CD2  . TYR   A 1 227 ? 4.184   -12.812 32.071  1.00 29.97 ? 227 TYR   A CD2  1 
ATOM   3379 C  CE1  . TYR   A 1 227 ? 2.151   -13.872 30.540  1.00 39.61 ? 227 TYR   A CE1  1 
ATOM   3380 C  CE2  . TYR   A 1 227 ? 2.872   -12.528 32.384  1.00 32.90 ? 227 TYR   A CE2  1 
ATOM   3381 C  CZ   . TYR   A 1 227 ? 1.859   -13.058 31.619  1.00 39.50 ? 227 TYR   A CZ   1 
ATOM   3382 O  OH   . TYR   A 1 227 ? 0.555   -12.763 31.948  1.00 46.42 ? 227 TYR   A OH   1 
ATOM   3383 H  H    . TYR   A 1 227 ? 6.893   -14.658 33.031  1.00 30.31 ? 227 TYR   A H    1 
ATOM   3384 H  HA   . TYR   A 1 227 ? 5.905   -15.970 30.858  1.00 28.48 ? 227 TYR   A HA   1 
ATOM   3385 H  HB2  . TYR   A 1 227 ? 6.482   -13.210 31.046  1.00 29.32 ? 227 TYR   A HB2  1 
ATOM   3386 H  HB3  . TYR   A 1 227 ? 6.032   -13.927 29.704  1.00 29.32 ? 227 TYR   A HB3  1 
ATOM   3387 H  HD1  . TYR   A 1 227 ? 3.669   -14.700 29.511  1.00 45.18 ? 227 TYR   A HD1  1 
ATOM   3388 H  HD2  . TYR   A 1 227 ? 4.866   -12.449 32.589  1.00 35.98 ? 227 TYR   A HD2  1 
ATOM   3389 H  HE1  . TYR   A 1 227 ? 1.465   -14.233 30.026  1.00 47.55 ? 227 TYR   A HE1  1 
ATOM   3390 H  HE2  . TYR   A 1 227 ? 2.672   -11.980 33.107  1.00 39.50 ? 227 TYR   A HE2  1 
ATOM   3391 H  HH   . TYR   A 1 227 ? 0.535   -12.261 32.621  1.00 55.73 ? 227 TYR   A HH   1 
ATOM   3392 N  N    . ASP   A 1 228 ? 8.144   -16.471 29.968  1.00 24.38 ? 228 ASP   A N    1 
ATOM   3393 C  CA   . ASP   A 1 228 ? 9.499   -16.632 29.459  1.00 22.81 ? 228 ASP   A CA   1 
ATOM   3394 C  C    . ASP   A 1 228 ? 9.840   -15.624 28.367  1.00 21.90 ? 228 ASP   A C    1 
ATOM   3395 O  O    . ASP   A 1 228 ? 11.024  -15.340 28.158  1.00 21.88 ? 228 ASP   A O    1 
ATOM   3396 C  CB   . ASP   A 1 228 ? 9.727   -18.033 28.900  1.00 24.38 ? 228 ASP   A CB   1 
ATOM   3397 C  CG   . ASP   A 1 228 ? 9.625   -19.105 29.947  1.00 36.72 ? 228 ASP   A CG   1 
ATOM   3398 O  OD1  . ASP   A 1 228 ? 9.905   -18.818 31.133  1.00 40.95 ? 228 ASP   A OD1  1 
ATOM   3399 O  OD2  . ASP   A 1 228 ? 9.291   -20.247 29.576  1.00 49.45 ? 228 ASP   A OD2  1 
ATOM   3400 H  H    . ASP   A 1 228 ? 7.573   -17.053 29.695  1.00 29.27 ? 228 ASP   A H    1 
ATOM   3401 H  HA   . ASP   A 1 228 ? 10.124  -16.500 30.189  1.00 27.39 ? 228 ASP   A HA   1 
ATOM   3402 H  HB2  . ASP   A 1 228 ? 9.059   -18.214 28.220  1.00 29.27 ? 228 ASP   A HB2  1 
ATOM   3403 H  HB3  . ASP   A 1 228 ? 10.615  -18.077 28.512  1.00 29.27 ? 228 ASP   A HB3  1 
ATOM   3404 N  N    . ALA   A 1 229 ? 8.835   -15.104 27.667  1.00 18.06 ? 229 ALA   A N    1 
ATOM   3405 C  CA   . ALA   A 1 229 ? 9.041   -14.189 26.548  1.00 17.80 ? 229 ALA   A CA   1 
ATOM   3406 C  C    . ALA   A 1 229 ? 7.742   -13.440 26.298  1.00 18.85 ? 229 ALA   A C    1 
ATOM   3407 O  O    . ALA   A 1 229 ? 6.674   -13.847 26.765  1.00 20.67 ? 229 ALA   A O    1 
ATOM   3408 C  CB   . ALA   A 1 229 ? 9.471   -14.930 25.275  1.00 19.83 ? 229 ALA   A CB   1 
ATOM   3409 H  H    . ALA   A 1 229 ? 8.006   -15.270 27.825  1.00 21.69 ? 229 ALA   A H    1 
ATOM   3410 H  HA   . ALA   A 1 229 ? 9.729   -13.545 26.778  1.00 21.38 ? 229 ALA   A HA   1 
ATOM   3411 H  HB1  . ALA   A 1 229 ? 9.596   -14.285 24.561  1.00 23.82 ? 229 ALA   A HB1  1 
ATOM   3412 H  HB2  . ALA   A 1 229 ? 10.303  -15.397 25.448  1.00 23.82 ? 229 ALA   A HB2  1 
ATOM   3413 H  HB3  . ALA   A 1 229 ? 8.779   -15.565 25.031  1.00 23.82 ? 229 ALA   A HB3  1 
ATOM   3414 N  N    . LEU   A 1 230 ? 7.847   -12.340 25.541  1.00 18.38 ? 230 LEU   A N    1 
ATOM   3415 C  CA   . LEU   A 1 230 ? 6.654   -11.651 25.048  1.00 19.51 ? 230 LEU   A CA   1 
ATOM   3416 C  C    . LEU   A 1 230 ? 5.947   -12.471 23.971  1.00 19.83 ? 230 LEU   A C    1 
ATOM   3417 O  O    . LEU   A 1 230 ? 4.723   -12.645 24.014  1.00 19.91 ? 230 LEU   A O    1 
ATOM   3418 C  CB   . LEU   A 1 230 ? 7.022   -10.273 24.490  1.00 20.13 ? 230 LEU   A CB   1 
ATOM   3419 C  CG   . LEU   A 1 230 ? 7.616   -9.252  25.454  1.00 22.62 ? 230 LEU   A CG   1 
ATOM   3420 C  CD1  . LEU   A 1 230 ? 8.042   -7.981  24.741  1.00 23.95 ? 230 LEU   A CD1  1 
ATOM   3421 C  CD2  . LEU   A 1 230 ? 6.606   -8.932  26.545  1.00 22.40 ? 230 LEU   A CD2  1 
ATOM   3422 H  H    . LEU   A 1 230 ? 8.590   -11.979 25.303  1.00 22.08 ? 230 LEU   A H    1 
ATOM   3423 H  HA   . LEU   A 1 230 ? 6.034   -11.525 25.783  1.00 23.43 ? 230 LEU   A HA   1 
ATOM   3424 H  HB2  . LEU   A 1 230 ? 7.669   -10.401 23.779  1.00 24.18 ? 230 LEU   A HB2  1 
ATOM   3425 H  HB3  . LEU   A 1 230 ? 6.218   -9.877  24.119  1.00 24.18 ? 230 LEU   A HB3  1 
ATOM   3426 H  HG   . LEU   A 1 230 ? 8.401   -9.636  25.876  1.00 27.17 ? 230 LEU   A HG   1 
ATOM   3427 H  HD11 . LEU   A 1 230 ? 8.414   -7.364  25.391  1.00 28.76 ? 230 LEU   A HD11 1 
ATOM   3428 H  HD12 . LEU   A 1 230 ? 8.711   -8.203  24.074  1.00 28.76 ? 230 LEU   A HD12 1 
ATOM   3429 H  HD13 . LEU   A 1 230 ? 7.267   -7.584  24.314  1.00 28.76 ? 230 LEU   A HD13 1 
ATOM   3430 H  HD21 . LEU   A 1 230 ? 6.946   -8.201  27.085  1.00 26.90 ? 230 LEU   A HD21 1 
ATOM   3431 H  HD22 . LEU   A 1 230 ? 5.767   -8.676  26.132  1.00 26.90 ? 230 LEU   A HD22 1 
ATOM   3432 H  HD23 . LEU   A 1 230 ? 6.477   -9.719  27.097  1.00 26.90 ? 230 LEU   A HD23 1 
ATOM   3433 N  N    . ARG   A 1 231 ? 6.697   -12.968 22.990  1.00 17.53 ? 231 ARG   A N    1 
ATOM   3434 C  CA   . ARG   A 1 231 ? 6.134   -13.714 21.872  1.00 15.49 ? 231 ARG   A CA   1 
ATOM   3435 C  C    . ARG   A 1 231 ? 7.108   -14.811 21.462  1.00 15.19 ? 231 ARG   A C    1 
ATOM   3436 O  O    . ARG   A 1 231 ? 8.319   -14.711 21.684  1.00 15.53 ? 231 ARG   A O    1 
ATOM   3437 C  CB   . ARG   A 1 231 ? 5.872   -12.806 20.662  1.00 14.60 ? 231 ARG   A CB   1 
ATOM   3438 C  CG   . ARG   A 1 231 ? 4.669   -11.911 20.796  1.00 15.88 ? 231 ARG   A CG   1 
ATOM   3439 C  CD   . ARG   A 1 231 ? 4.504   -10.972 19.602  1.00 14.84 ? 231 ARG   A CD   1 
ATOM   3440 N  NE   . ARG   A 1 231 ? 5.526   -9.927  19.558  1.00 14.03 ? 231 ARG   A NE   1 
ATOM   3441 C  CZ   . ARG   A 1 231 ? 5.410   -8.738  20.133  1.00 14.16 ? 231 ARG   A CZ   1 
ATOM   3442 N  NH1  . ARG   A 1 231 ? 4.497   -8.508  21.063  1.00 16.67 ? 231 ARG   A NH1  1 
ATOM   3443 N  NH2  . ARG   A 1 231 ? 6.241   -7.763  19.779  1.00 13.88 ? 231 ARG   A NH2  1 
ATOM   3444 H  H    . ARG   A 1 231 ? 7.552   -12.883 22.951  1.00 21.06 ? 231 ARG   A H    1 
ATOM   3445 H  HA   . ARG   A 1 231 ? 5.297   -14.126 22.139  1.00 18.61 ? 231 ARG   A HA   1 
ATOM   3446 H  HB2  . ARG   A 1 231 ? 6.647   -12.238 20.527  1.00 17.54 ? 231 ARG   A HB2  1 
ATOM   3447 H  HB3  . ARG   A 1 231 ? 5.737   -13.364 19.880  1.00 17.54 ? 231 ARG   A HB3  1 
ATOM   3448 H  HG2  . ARG   A 1 231 ? 3.871   -12.459 20.860  1.00 19.08 ? 231 ARG   A HG2  1 
ATOM   3449 H  HG3  . ARG   A 1 231 ? 4.765   -11.369 21.594  1.00 19.08 ? 231 ARG   A HG3  1 
ATOM   3450 H  HD2  . ARG   A 1 231 ? 4.569   -11.488 18.784  1.00 17.82 ? 231 ARG   A HD2  1 
ATOM   3451 H  HD3  . ARG   A 1 231 ? 3.636   -10.543 19.655  1.00 17.82 ? 231 ARG   A HD3  1 
ATOM   3452 H  HE   . ARG   A 1 231 ? 6.252   -10.095 19.130  1.00 16.85 ? 231 ARG   A HE   1 
ATOM   3453 H  HH11 . ARG   A 1 231 ? 3.949   -9.129  21.293  1.00 20.03 ? 231 ARG   A HH11 1 
ATOM   3454 H  HH12 . ARG   A 1 231 ? 4.444   -7.732  21.430  1.00 20.03 ? 231 ARG   A HH12 1 
ATOM   3455 H  HH21 . ARG   A 1 231 ? 6.845   -7.908  19.184  1.00 16.68 ? 231 ARG   A HH21 1 
ATOM   3456 H  HH22 . ARG   A 1 231 ? 6.189   -6.994  20.161  1.00 16.68 ? 231 ARG   A HH22 1 
ATOM   3457 N  N    . TYR   A 1 232 ? 6.558   -15.840 20.828  1.00 17.04 ? 232 TYR   A N    1 
ATOM   3458 C  CA   . TYR   A 1 232 ? 7.285   -16.984 20.288  1.00 16.74 ? 232 TYR   A CA   1 
ATOM   3459 C  C    . TYR   A 1 232 ? 7.019   -17.051 18.794  1.00 17.94 ? 232 TYR   A C    1 
ATOM   3460 O  O    . TYR   A 1 232 ? 5.864   -17.028 18.367  1.00 18.79 ? 232 TYR   A O    1 
ATOM   3461 C  CB   . TYR   A 1 232 ? 6.807   -18.263 20.958  1.00 17.78 ? 232 TYR   A CB   1 
ATOM   3462 C  CG   . TYR   A 1 232 ? 6.871   -18.219 22.470  1.00 20.47 ? 232 TYR   A CG   1 
ATOM   3463 C  CD1  . TYR   A 1 232 ? 8.021   -18.595 23.143  1.00 24.08 ? 232 TYR   A CD1  1 
ATOM   3464 C  CD2  . TYR   A 1 232 ? 5.802   -17.738 23.221  1.00 22.61 ? 232 TYR   A CD2  1 
ATOM   3465 C  CE1  . TYR   A 1 232 ? 8.089   -18.557 24.521  1.00 24.77 ? 232 TYR   A CE1  1 
ATOM   3466 C  CE2  . TYR   A 1 232 ? 5.866   -17.677 24.601  1.00 23.63 ? 232 TYR   A CE2  1 
ATOM   3467 C  CZ   . TYR   A 1 232 ? 7.012   -18.088 25.249  1.00 28.26 ? 232 TYR   A CZ   1 
ATOM   3468 O  OH   . TYR   A 1 232 ? 7.076   -18.031 26.622  1.00 34.20 ? 232 TYR   A OH   1 
ATOM   3469 H  H    . TYR   A 1 232 ? 5.711   -15.899 20.691  1.00 20.46 ? 232 TYR   A H    1 
ATOM   3470 H  HA   . TYR   A 1 232 ? 8.237   -16.880 20.439  1.00 20.11 ? 232 TYR   A HA   1 
ATOM   3471 H  HB2  . TYR   A 1 232 ? 5.884   -18.423 20.705  1.00 21.35 ? 232 TYR   A HB2  1 
ATOM   3472 H  HB3  . TYR   A 1 232 ? 7.363   -18.999 20.659  1.00 21.35 ? 232 TYR   A HB3  1 
ATOM   3473 H  HD1  . TYR   A 1 232 ? 8.747   -18.919 22.660  1.00 28.92 ? 232 TYR   A HD1  1 
ATOM   3474 H  HD2  . TYR   A 1 232 ? 5.025   -17.466 22.788  1.00 27.15 ? 232 TYR   A HD2  1 
ATOM   3475 H  HE1  . TYR   A 1 232 ? 8.866   -18.825 24.957  1.00 29.75 ? 232 TYR   A HE1  1 
ATOM   3476 H  HE2  . TYR   A 1 232 ? 5.138   -17.368 25.090  1.00 28.37 ? 232 TYR   A HE2  1 
ATOM   3477 H  HH   . TYR   A 1 232 ? 6.356   -17.728 26.931  1.00 41.06 ? 232 TYR   A HH   1 
ATOM   3478 N  N    . MET   A 1 233 ? 8.073   -17.128 17.992  1.00 17.49 ? 233 MET   A N    1 
ATOM   3479 C  CA   . MET   A 1 233 ? 7.875   -17.148 16.550  1.00 17.24 ? 233 MET   A CA   1 
ATOM   3480 C  C    . MET   A 1 233 ? 7.760   -18.558 15.988  1.00 18.75 ? 233 MET   A C    1 
ATOM   3481 O  O    . MET   A 1 233 ? 7.202   -18.728 14.898  1.00 18.52 ? 233 MET   A O    1 
ATOM   3482 C  CB   . MET   A 1 233 ? 9.025   -16.383 15.892  1.00 16.02 ? 233 MET   A CB   1 
ATOM   3483 C  CG   . MET   A 1 233 ? 8.979   -14.897 16.223  1.00 20.43 ? 233 MET   A CG   1 
ATOM   3484 S  SD   . MET   A 1 233 ? 10.332  -13.967 15.491  1.00 19.23 ? 233 MET   A SD   1 
ATOM   3485 C  CE   . MET   A 1 233 ? 9.513   -13.559 13.935  1.00 16.47 ? 233 MET   A CE   1 
ATOM   3486 H  H    . MET   A 1 233 ? 8.893   -17.169 18.249  1.00 21.01 ? 233 MET   A H    1 
ATOM   3487 H  HA   . MET   A 1 233 ? 7.057   -16.670 16.343  1.00 20.71 ? 233 MET   A HA   1 
ATOM   3488 H  HB2  . MET   A 1 233 ? 9.869   -16.739 16.212  1.00 19.24 ? 233 MET   A HB2  1 
ATOM   3489 H  HB3  . MET   A 1 233 ? 8.964   -16.481 14.929  1.00 19.24 ? 233 MET   A HB3  1 
ATOM   3490 H  HG2  . MET   A 1 233 ? 8.147   -14.526 15.891  1.00 24.54 ? 233 MET   A HG2  1 
ATOM   3491 H  HG3  . MET   A 1 233 ? 9.029   -14.787 17.185  1.00 24.54 ? 233 MET   A HG3  1 
ATOM   3492 H  HE1  . MET   A 1 233 ? 10.136  -13.079 13.367  1.00 19.79 ? 233 MET   A HE1  1 
ATOM   3493 H  HE2  . MET   A 1 233 ? 9.234   -14.380 13.501  1.00 19.79 ? 233 MET   A HE2  1 
ATOM   3494 H  HE3  . MET   A 1 233 ? 8.740   -13.004 14.122  1.00 19.79 ? 233 MET   A HE3  1 
ATOM   3495 N  N    . ASP   A 1 234 ? 8.244   -19.578 16.705  1.00 18.09 ? 234 ASP   A N    1 
ATOM   3496 C  CA   . ASP   A 1 234 ? 8.128   -20.940 16.191  1.00 17.66 ? 234 ASP   A CA   1 
ATOM   3497 C  C    . ASP   A 1 234 ? 6.702   -21.455 16.324  1.00 19.19 ? 234 ASP   A C    1 
ATOM   3498 O  O    . ASP   A 1 234 ? 6.237   -22.228 15.478  1.00 22.55 ? 234 ASP   A O    1 
ATOM   3499 C  CB   . ASP   A 1 234 ? 9.072   -21.871 16.951  1.00 23.24 ? 234 ASP   A CB   1 
ATOM   3500 C  CG   . ASP   A 1 234 ? 8.728   -21.972 18.421  1.00 21.50 ? 234 ASP   A CG   1 
ATOM   3501 O  OD1  . ASP   A 1 234 ? 8.666   -20.929 19.108  1.00 24.74 ? 234 ASP   A OD1  1 
ATOM   3502 O  OD2  . ASP   A 1 234 ? 8.565   -23.109 18.908  1.00 29.49 ? 234 ASP   A OD2  1 
ATOM   3503 H  H    . ASP   A 1 234 ? 8.633   -19.509 17.469  1.00 21.72 ? 234 ASP   A H    1 
ATOM   3504 H  HA   . ASP   A 1 234 ? 8.373   -20.953 15.253  1.00 21.21 ? 234 ASP   A HA   1 
ATOM   3505 H  HB2  . ASP   A 1 234 ? 9.017   -22.760 16.567  1.00 27.91 ? 234 ASP   A HB2  1 
ATOM   3506 H  HB3  . ASP   A 1 234 ? 9.978   -21.533 16.877  1.00 27.91 ? 234 ASP   A HB3  1 
ATOM   3507 N  N    . LYS   A 1 235 ? 6.014   -21.049 17.385  1.00 17.65 ? 235 LYS   A N    1 
ATOM   3508 C  CA   . LYS   A 1 235 ? 4.632   -21.453 17.639  1.00 17.49 ? 235 LYS   A CA   1 
ATOM   3509 C  C    . LYS   A 1 235 ? 3.968   -20.310 18.380  1.00 18.02 ? 235 LYS   A C    1 
ATOM   3510 O  O    . LYS   A 1 235 ? 3.894   -20.302 19.616  1.00 20.44 ? 235 LYS   A O    1 
ATOM   3511 C  CB   . LYS   A 1 235 ? 4.567   -22.740 18.457  1.00 22.20 ? 235 LYS   A CB   1 
ATOM   3512 C  CG   . LYS   A 1 235 ? 3.159   -23.270 18.657  1.00 25.12 ? 235 LYS   A CG   1 
ATOM   3513 C  CD   . LYS   A 1 235 ? 3.208   -24.542 19.487  1.00 29.20 ? 235 LYS   A CD   1 
ATOM   3514 C  CE   . LYS   A 1 235 ? 1.846   -24.928 20.042  1.00 45.70 ? 235 LYS   A CE   1 
ATOM   3515 N  NZ   . LYS   A 1 235 ? 1.777   -26.393 20.330  1.00 50.46 ? 235 LYS   A NZ   1 
ATOM   3516 H  H    . LYS   A 1 235 ? 6.333   -20.526 17.989  1.00 21.20 ? 235 LYS   A H    1 
ATOM   3517 H  HA   . LYS   A 1 235 ? 4.171   -21.602 16.799  1.00 21.01 ? 235 LYS   A HA   1 
ATOM   3518 H  HB2  . LYS   A 1 235 ? 5.080   -23.426 18.001  1.00 26.66 ? 235 LYS   A HB2  1 
ATOM   3519 H  HB3  . LYS   A 1 235 ? 4.948   -22.573 19.333  1.00 26.66 ? 235 LYS   A HB3  1 
ATOM   3520 H  HG2  . LYS   A 1 235 ? 2.626   -22.612 19.130  1.00 30.17 ? 235 LYS   A HG2  1 
ATOM   3521 H  HG3  . LYS   A 1 235 ? 2.763   -23.477 17.796  1.00 30.17 ? 235 LYS   A HG3  1 
ATOM   3522 H  HD2  . LYS   A 1 235 ? 3.524   -25.271 18.931  1.00 35.05 ? 235 LYS   A HD2  1 
ATOM   3523 H  HD3  . LYS   A 1 235 ? 3.811   -24.409 20.235  1.00 35.05 ? 235 LYS   A HD3  1 
ATOM   3524 H  HE2  . LYS   A 1 235 ? 1.692   -24.448 20.871  1.00 54.86 ? 235 LYS   A HE2  1 
ATOM   3525 H  HE3  . LYS   A 1 235 ? 1.159   -24.710 19.392  1.00 54.86 ? 235 LYS   A HE3  1 
ATOM   3526 H  HZ1  . LYS   A 1 235 ? 0.975   -26.602 20.654  1.00 60.57 ? 235 LYS   A HZ1  1 
ATOM   3527 H  HZ2  . LYS   A 1 235 ? 1.917   -26.856 19.583  1.00 60.57 ? 235 LYS   A HZ2  1 
ATOM   3528 H  HZ3  . LYS   A 1 235 ? 2.397   -26.615 20.929  1.00 60.57 ? 235 LYS   A HZ3  1 
ATOM   3529 N  N    . PRO   A 1 236 ? 3.506   -19.296 17.651  1.00 16.92 ? 236 PRO   A N    1 
ATOM   3530 C  CA   . PRO   A 1 236 ? 2.961   -18.100 18.327  1.00 15.05 ? 236 PRO   A CA   1 
ATOM   3531 C  C    . PRO   A 1 236 ? 1.892   -18.400 19.362  1.00 17.31 ? 236 PRO   A C    1 
ATOM   3532 O  O    . PRO   A 1 236 ? 1.820   -17.710 20.389  1.00 16.28 ? 236 PRO   A O    1 
ATOM   3533 C  CB   . PRO   A 1 236 ? 2.414   -17.272 17.154  1.00 16.20 ? 236 PRO   A CB   1 
ATOM   3534 C  CG   . PRO   A 1 236 ? 3.316   -17.642 15.987  1.00 16.56 ? 236 PRO   A CG   1 
ATOM   3535 C  CD   . PRO   A 1 236 ? 3.620   -19.119 16.188  1.00 17.75 ? 236 PRO   A CD   1 
ATOM   3536 H  HA   . PRO   A 1 236 ? 3.673   -17.605 18.757  1.00 18.08 ? 236 PRO   A HA   1 
ATOM   3537 H  HB2  . PRO   A 1 236 ? 1.494   -17.523 16.974  1.00 19.46 ? 236 PRO   A HB2  1 
ATOM   3538 H  HB3  . PRO   A 1 236 ? 2.482   -16.326 17.358  1.00 19.46 ? 236 PRO   A HB3  1 
ATOM   3539 H  HG2  . PRO   A 1 236 ? 2.846   -17.498 15.151  1.00 19.89 ? 236 PRO   A HG2  1 
ATOM   3540 H  HG3  . PRO   A 1 236 ? 4.130   -17.115 16.021  1.00 19.89 ? 236 PRO   A HG3  1 
ATOM   3541 H  HD2  . PRO   A 1 236 ? 2.965   -19.665 15.727  1.00 21.32 ? 236 PRO   A HD2  1 
ATOM   3542 H  HD3  . PRO   A 1 236 ? 4.522   -19.320 15.892  1.00 21.32 ? 236 PRO   A HD3  1 
ATOM   3543 N  N    . SER   A 1 237 ? 1.060   -19.421 19.136  1.00 17.55 ? 237 SER   A N    1 
ATOM   3544 C  CA   . SER   A 1 237 ? -0.029  -19.746 20.048  1.00 17.59 ? 237 SER   A CA   1 
ATOM   3545 C  C    . SER   A 1 237 ? 0.453   -20.190 21.424  1.00 16.85 ? 237 SER   A C    1 
ATOM   3546 O  O    . SER   A 1 237 ? -0.373  -20.325 22.336  1.00 21.57 ? 237 SER   A O    1 
ATOM   3547 C  CB   . SER   A 1 237 ? -0.917  -20.839 19.436  1.00 20.88 ? 237 SER   A CB   1 
ATOM   3548 O  OG   . SER   A 1 237 ? -0.193  -22.038 19.203  1.00 21.32 ? 237 SER   A OG   1 
ATOM   3549 H  H    . SER   A 1 237 ? 1.110   -19.942 18.454  1.00 21.08 ? 237 SER   A H    1 
ATOM   3550 H  HA   . SER   A 1 237 ? -0.577  -18.955 20.170  1.00 21.13 ? 237 SER   A HA   1 
ATOM   3551 H  HB2  . SER   A 1 237 ? -1.646  -21.028 20.047  1.00 25.07 ? 237 SER   A HB2  1 
ATOM   3552 H  HB3  . SER   A 1 237 ? -1.271  -20.518 18.592  1.00 25.07 ? 237 SER   A HB3  1 
ATOM   3553 H  HG   . SER   A 1 237 ? 0.442   -21.892 18.672  1.00 25.61 ? 237 SER   A HG   1 
ATOM   3554 N  N    . ARG   A 1 238 ? 1.752   -20.419 21.601  1.00 21.63 ? 238 ARG   A N    1 
ATOM   3555 C  CA   . ARG   A 1 238 ? 2.267   -20.716 22.935  1.00 19.77 ? 238 ARG   A CA   1 
ATOM   3556 C  C    . ARG   A 1 238 ? 1.936   -19.616 23.942  1.00 22.56 ? 238 ARG   A C    1 
ATOM   3557 O  O    . ARG   A 1 238 ? 1.865   -19.891 25.144  1.00 24.94 ? 238 ARG   A O    1 
ATOM   3558 C  CB   . ARG   A 1 238 ? 3.779   -20.932 22.866  1.00 22.26 ? 238 ARG   A CB   1 
ATOM   3559 C  CG   . ARG   A 1 238 ? 4.411   -21.320 24.192  1.00 35.06 ? 238 ARG   A CG   1 
ATOM   3560 C  CD   . ARG   A 1 238 ? 5.901   -21.642 24.052  1.00 41.35 ? 238 ARG   A CD   1 
ATOM   3561 N  NE   . ARG   A 1 238 ? 6.168   -22.822 23.237  1.00 40.58 ? 238 ARG   A NE   1 
ATOM   3562 C  CZ   . ARG   A 1 238 ? 6.619   -22.803 21.989  1.00 37.79 ? 238 ARG   A CZ   1 
ATOM   3563 N  NH1  . ARG   A 1 238 ? 6.963   -21.673 21.392  1.00 36.88 ? 238 ARG   A NH1  1 
ATOM   3564 N  NH2  . ARG   A 1 238 ? 6.739   -23.950 21.325  1.00 44.38 ? 238 ARG   A NH2  1 
ATOM   3565 H  H    . ARG   A 1 238 ? 2.346   -20.410 20.979  1.00 25.98 ? 238 ARG   A H    1 
ATOM   3566 H  HA   . ARG   A 1 238 ? 1.863   -21.539 23.251  1.00 23.74 ? 238 ARG   A HA   1 
ATOM   3567 H  HB2  . ARG   A 1 238 ? 3.964   -21.642 22.231  1.00 26.73 ? 238 ARG   A HB2  1 
ATOM   3568 H  HB3  . ARG   A 1 238 ? 4.198   -20.109 22.568  1.00 26.73 ? 238 ARG   A HB3  1 
ATOM   3569 H  HG2  . ARG   A 1 238 ? 4.322   -20.583 24.816  1.00 42.10 ? 238 ARG   A HG2  1 
ATOM   3570 H  HG3  . ARG   A 1 238 ? 3.963   -22.108 24.539  1.00 42.10 ? 238 ARG   A HG3  1 
ATOM   3571 H  HD2  . ARG   A 1 238 ? 6.352   -20.878 23.665  1.00 49.64 ? 238 ARG   A HD2  1 
ATOM   3572 H  HD3  . ARG   A 1 238 ? 6.261   -21.814 24.936  1.00 49.64 ? 238 ARG   A HD3  1 
ATOM   3573 H  HE   . ARG   A 1 238 ? 6.022   -23.591 23.593  1.00 48.71 ? 238 ARG   A HE   1 
ATOM   3574 H  HH11 . ARG   A 1 238 ? 6.891   -20.922 21.801  1.00 44.28 ? 238 ARG   A HH11 1 
ATOM   3575 H  HH12 . ARG   A 1 238 ? 7.255   -21.691 20.583  1.00 44.28 ? 238 ARG   A HH12 1 
ATOM   3576 H  HH21 . ARG   A 1 238 ? 6.523   -24.691 21.704  1.00 53.27 ? 238 ARG   A HH21 1 
ATOM   3577 H  HH22 . ARG   A 1 238 ? 7.037   -23.951 20.518  1.00 53.27 ? 238 ARG   A HH22 1 
ATOM   3578 N  N    . ASP   A 1 239 ? 1.717   -18.374 23.491  1.00 20.08 ? 239 ASP   A N    1 
ATOM   3579 C  CA   . ASP   A 1 239 ? 1.424   -17.280 24.420  1.00 21.73 ? 239 ASP   A CA   1 
ATOM   3580 C  C    . ASP   A 1 239 ? -0.049  -17.205 24.808  1.00 22.49 ? 239 ASP   A C    1 
ATOM   3581 O  O    . ASP   A 1 239 ? -0.415  -16.339 25.613  1.00 24.92 ? 239 ASP   A O    1 
ATOM   3582 C  CB   . ASP   A 1 239 ? 1.911   -15.944 23.821  1.00 18.52 ? 239 ASP   A CB   1 
ATOM   3583 C  CG   . ASP   A 1 239 ? 1.046   -15.429 22.665  1.00 18.40 ? 239 ASP   A CG   1 
ATOM   3584 O  OD1  . ASP   A 1 239 ? 0.009   -16.041 22.324  1.00 19.93 ? 239 ASP   A OD1  1 
ATOM   3585 O  OD2  . ASP   A 1 239 ? 1.467   -14.430 22.036  1.00 19.19 ? 239 ASP   A OD2  1 
ATOM   3586 H  H    . ASP   A 1 239 ? 1.733   -18.143 22.663  1.00 24.12 ? 239 ASP   A H    1 
ATOM   3587 H  HA   . ASP   A 1 239 ? 1.928   -17.430 25.235  1.00 26.10 ? 239 ASP   A HA   1 
ATOM   3588 H  HB2  . ASP   A 1 239 ? 1.906   -15.269 24.518  1.00 22.24 ? 239 ASP   A HB2  1 
ATOM   3589 H  HB3  . ASP   A 1 239 ? 2.813   -16.063 23.485  1.00 22.24 ? 239 ASP   A HB3  1 
ATOM   3590 N  N    . GLY   A 1 240 ? -0.891  -18.091 24.282  1.00 21.15 ? 240 GLY   A N    1 
ATOM   3591 C  CA   . GLY   A 1 240 ? -2.279  -18.159 24.679  1.00 24.49 ? 240 GLY   A CA   1 
ATOM   3592 C  C    . GLY   A 1 240 ? -3.238  -17.299 23.889  1.00 23.17 ? 240 GLY   A C    1 
ATOM   3593 O  O    . GLY   A 1 240 ? -4.454  -17.397 24.116  1.00 26.37 ? 240 GLY   A O    1 
ATOM   3594 H  H    . GLY   A 1 240 ? -0.673  -18.670 23.684  1.00 25.40 ? 240 GLY   A H    1 
ATOM   3595 H  HA2  . GLY   A 1 240 ? -2.578  -19.079 24.604  1.00 29.41 ? 240 GLY   A HA2  1 
ATOM   3596 H  HA3  . GLY   A 1 240 ? -2.349  -17.900 25.611  1.00 29.41 ? 240 GLY   A HA3  1 
ATOM   3597 N  N    . MET   A 1 241 ? -2.746  -16.474 22.966  1.00 21.32 ? 241 MET   A N    1 
ATOM   3598 C  CA   B MET   A 1 241 ? -3.635  -15.607 22.197  0.40 23.87 ? 241 MET   A CA   1 
ATOM   3599 C  CA   C MET   A 1 241 ? -3.593  -15.552 22.222  0.60 23.87 ? 241 MET   A CA   1 
ATOM   3600 C  C    . MET   A 1 241 ? -3.220  -15.411 20.749  1.00 21.02 ? 241 MET   A C    1 
ATOM   3601 O  O    . MET   A 1 241 ? -4.100  -15.187 19.909  1.00 21.86 ? 241 MET   A O    1 
ATOM   3602 C  CB   B MET   A 1 241 ? -3.750  -14.222 22.844  0.40 25.13 ? 241 MET   A CB   1 
ATOM   3603 C  CB   C MET   A 1 241 ? -3.541  -14.162 22.869  0.60 25.02 ? 241 MET   A CB   1 
ATOM   3604 C  CG   B MET   A 1 241 ? -4.844  -13.411 22.197  0.40 29.89 ? 241 MET   A CG   1 
ATOM   3605 C  CG   C MET   A 1 241 ? -4.634  -13.217 22.413  0.60 31.51 ? 241 MET   A CG   1 
ATOM   3606 S  SD   B MET   A 1 241 ? -5.826  -12.432 23.328  0.40 32.48 ? 241 MET   A SD   1 
ATOM   3607 S  SD   C MET   A 1 241 ? -6.279  -13.779 22.869  0.60 37.21 ? 241 MET   A SD   1 
ATOM   3608 C  CE   B MET   A 1 241 ? -6.913  -11.644 22.144  0.40 24.86 ? 241 MET   A CE   1 
ATOM   3609 C  CE   C MET   A 1 241 ? -6.104  -13.709 24.647  0.60 25.87 ? 241 MET   A CE   1 
ATOM   3610 H  H    B MET   A 1 241 ? -1.913  -16.398 22.768  0.40 25.60 ? 241 MET   A H    1 
ATOM   3611 H  H    C MET   A 1 241 ? -1.914  -16.431 22.752  0.60 25.60 ? 241 MET   A H    1 
ATOM   3612 H  HA   B MET   A 1 241 ? -4.521  -16.002 22.202  0.40 28.66 ? 241 MET   A HA   1 
ATOM   3613 H  HA   C MET   A 1 241 ? -4.509  -15.867 22.274  0.60 28.66 ? 241 MET   A HA   1 
ATOM   3614 H  HB2  B MET   A 1 241 ? -3.961  -14.323 23.785  0.40 30.18 ? 241 MET   A HB2  1 
ATOM   3615 H  HB2  C MET   A 1 241 ? -3.597  -14.260 23.830  0.60 30.04 ? 241 MET   A HB2  1 
ATOM   3616 H  HB3  B MET   A 1 241 ? -2.912  -13.746 22.735  0.40 30.18 ? 241 MET   A HB3  1 
ATOM   3617 H  HB3  C MET   A 1 241 ? -2.693  -13.752 22.639  0.60 30.04 ? 241 MET   A HB3  1 
ATOM   3618 H  HG2  B MET   A 1 241 ? -4.449  -12.816 21.549  0.40 35.89 ? 241 MET   A HG2  1 
ATOM   3619 H  HG2  C MET   A 1 241 ? -4.494  -12.356 22.833  0.60 37.83 ? 241 MET   A HG2  1 
ATOM   3620 H  HG3  B MET   A 1 241 ? -5.450  -14.019 21.745  0.40 35.89 ? 241 MET   A HG3  1 
ATOM   3621 H  HG3  C MET   A 1 241 ? -4.600  -13.128 21.448  0.60 37.83 ? 241 MET   A HG3  1 
ATOM   3622 H  HE1  B MET   A 1 241 ? -7.716  -11.351 22.602  0.40 29.85 ? 241 MET   A HE1  1 
ATOM   3623 H  HE1  C MET   A 1 241 ? -6.943  -13.979 25.049  0.60 31.06 ? 241 MET   A HE1  1 
ATOM   3624 H  HE2  B MET   A 1 241 ? -6.456  -10.883 21.753  0.40 29.85 ? 241 MET   A HE2  1 
ATOM   3625 H  HE2  C MET   A 1 241 ? -5.404  -14.317 24.927  0.60 31.06 ? 241 MET   A HE2  1 
ATOM   3626 H  HE3  B MET   A 1 241 ? -7.144  -12.285 21.454  0.40 29.85 ? 241 MET   A HE3  1 
ATOM   3627 H  HE3  C MET   A 1 241 ? -5.884  -12.802 24.910  0.60 31.06 ? 241 MET   A HE3  1 
ATOM   3628 N  N    . SER   A 1 242 ? -1.931  -15.467 20.435  1.00 17.40 ? 242 SER   A N    1 
ATOM   3629 C  CA   . SER   A 1 242 ? -1.484  -15.296 19.065  1.00 16.16 ? 242 SER   A CA   1 
ATOM   3630 C  C    . SER   A 1 242 ? -1.894  -16.503 18.228  1.00 16.93 ? 242 SER   A C    1 
ATOM   3631 O  O    . SER   A 1 242 ? -2.140  -17.596 18.746  1.00 18.32 ? 242 SER   A O    1 
ATOM   3632 C  CB   . SER   A 1 242 ? 0.033   -15.101 19.022  1.00 16.16 ? 242 SER   A CB   1 
ATOM   3633 O  OG   . SER   A 1 242 ? 0.415   -13.878 19.636  1.00 16.56 ? 242 SER   A OG   1 
ATOM   3634 H  H    . SER   A 1 242 ? -1.297  -15.603 20.999  1.00 20.90 ? 242 SER   A H    1 
ATOM   3635 H  HA   . SER   A 1 242 ? -1.903  -14.507 18.687  1.00 19.42 ? 242 SER   A HA   1 
ATOM   3636 H  HB2  . SER   A 1 242 ? 0.457   -15.835 19.493  1.00 19.42 ? 242 SER   A HB2  1 
ATOM   3637 H  HB3  . SER   A 1 242 ? 0.322   -15.092 18.096  1.00 19.42 ? 242 SER   A HB3  1 
ATOM   3638 H  HG   . SER   A 1 242 ? 0.172   -13.872 20.440  1.00 19.90 ? 242 SER   A HG   1 
ATOM   3639 N  N    . ILE   A 1 243 ? -1.964  -16.296 16.914  1.00 16.13 ? 243 ILE   A N    1 
ATOM   3640 C  CA   . ILE   A 1 243 ? -2.436  -17.315 15.984  1.00 17.74 ? 243 ILE   A CA   1 
ATOM   3641 C  C    . ILE   A 1 243 ? -1.289  -17.816 15.122  1.00 18.17 ? 243 ILE   A C    1 
ATOM   3642 O  O    . ILE   A 1 243 ? -0.326  -17.098 14.833  1.00 17.64 ? 243 ILE   A O    1 
ATOM   3643 C  CB   . ILE   A 1 243 ? -3.608  -16.796 15.114  1.00 17.09 ? 243 ILE   A CB   1 
ATOM   3644 C  CG1  . ILE   A 1 243 ? -3.211  -15.533 14.338  1.00 17.12 ? 243 ILE   A CG1  1 
ATOM   3645 C  CG2  . ILE   A 1 243 ? -4.866  -16.614 15.981  1.00 18.12 ? 243 ILE   A CG2  1 
ATOM   3646 C  CD1  . ILE   A 1 243 ? -4.203  -15.157 13.234  1.00 18.27 ? 243 ILE   A CD1  1 
ATOM   3647 H  H    . ILE   A 1 243 ? -1.739  -15.559 16.532  1.00 19.37 ? 243 ILE   A H    1 
ATOM   3648 H  HA   . ILE   A 1 243 ? -2.768  -18.071 16.493  1.00 21.31 ? 243 ILE   A HA   1 
ATOM   3649 H  HB   . ILE   A 1 243 ? -3.807  -17.484 14.460  1.00 20.52 ? 243 ILE   A HB   1 
ATOM   3650 H  HG12 . ILE   A 1 243 ? -3.160  -14.788 14.958  1.00 20.56 ? 243 ILE   A HG12 1 
ATOM   3651 H  HG13 . ILE   A 1 243 ? -2.347  -15.674 13.922  1.00 20.56 ? 243 ILE   A HG13 1 
ATOM   3652 H  HG21 . ILE   A 1 243 ? -5.601  -16.327 15.416  1.00 21.76 ? 243 ILE   A HG21 1 
ATOM   3653 H  HG22 . ILE   A 1 243 ? -5.083  -17.460 16.402  1.00 21.76 ? 243 ILE   A HG22 1 
ATOM   3654 H  HG23 . ILE   A 1 243 ? -4.688  -15.943 16.659  1.00 21.76 ? 243 ILE   A HG23 1 
ATOM   3655 H  HD11 . ILE   A 1 243 ? -3.869  -14.378 12.762  1.00 21.94 ? 243 ILE   A HD11 1 
ATOM   3656 H  HD12 . ILE   A 1 243 ? -4.290  -15.904 12.621  1.00 21.94 ? 243 ILE   A HD12 1 
ATOM   3657 H  HD13 . ILE   A 1 243 ? -5.062  -14.957 13.637  1.00 21.94 ? 243 ILE   A HD13 1 
ATOM   3658 N  N    . ASP   A 1 244 ? -1.413  -19.076 14.694  1.00 17.59 ? 244 ASP   A N    1 
ATOM   3659 C  CA   . ASP   A 1 244 ? -0.355  -19.771 13.977  1.00 16.49 ? 244 ASP   A CA   1 
ATOM   3660 C  C    . ASP   A 1 244 ? -0.580  -19.826 12.474  1.00 18.26 ? 244 ASP   A C    1 
ATOM   3661 O  O    . ASP   A 1 244 ? 0.380   -20.062 11.729  1.00 18.81 ? 244 ASP   A O    1 
ATOM   3662 C  CB   . ASP   A 1 244 ? -0.224  -21.217 14.483  1.00 19.18 ? 244 ASP   A CB   1 
ATOM   3663 C  CG   . ASP   A 1 244 ? 0.171   -21.312 15.945  1.00 18.45 ? 244 ASP   A CG   1 
ATOM   3664 O  OD1  . ASP   A 1 244 ? 0.756   -20.349 16.493  1.00 20.24 ? 244 ASP   A OD1  1 
ATOM   3665 O  OD2  . ASP   A 1 244 ? -0.135  -22.362 16.553  1.00 22.73 ? 244 ASP   A OD2  1 
ATOM   3666 H  H    . ASP   A 1 244 ? -2.118  -19.554 14.813  1.00 21.13 ? 244 ASP   A H    1 
ATOM   3667 H  HA   . ASP   A 1 244 ? 0.488   -19.319 14.138  1.00 19.81 ? 244 ASP   A HA   1 
ATOM   3668 H  HB2  . ASP   A 1 244 ? -1.077  -21.665 14.376  1.00 23.04 ? 244 ASP   A HB2  1 
ATOM   3669 H  HB3  . ASP   A 1 244 ? 0.455   -21.672 13.961  1.00 23.04 ? 244 ASP   A HB3  1 
ATOM   3670 N  N    . VAL   A 1 245 ? -1.823  -19.658 12.014  1.00 17.39 ? 245 VAL   A N    1 
ATOM   3671 C  CA   . VAL   A 1 245 ? -2.156  -19.719 10.594  1.00 17.10 ? 245 VAL   A CA   1 
ATOM   3672 C  C    . VAL   A 1 245 ? -3.170  -18.625 10.290  1.00 20.03 ? 245 VAL   A C    1 
ATOM   3673 O  O    . VAL   A 1 245 ? -3.904  -18.158 11.167  1.00 18.89 ? 245 VAL   A O    1 
ATOM   3674 C  CB   . VAL   A 1 245 ? -2.714  -21.101 10.182  1.00 21.75 ? 245 VAL   A CB   1 
ATOM   3675 C  CG1  . VAL   A 1 245 ? -1.687  -22.193 10.449  1.00 23.78 ? 245 VAL   A CG1  1 
ATOM   3676 C  CG2  . VAL   A 1 245 ? -4.021  -21.381 10.908  1.00 23.23 ? 245 VAL   A CG2  1 
ATOM   3677 H  H    . VAL   A 1 245 ? -2.503  -19.505 12.518  1.00 20.88 ? 245 VAL   A H    1 
ATOM   3678 H  HA   . VAL   A 1 245 ? -1.358  -19.546 10.070  1.00 20.54 ? 245 VAL   A HA   1 
ATOM   3679 H  HB   . VAL   A 1 245 ? -2.899  -21.093 9.230   1.00 26.12 ? 245 VAL   A HB   1 
ATOM   3680 H  HG11 . VAL   A 1 245 ? -2.007  -23.027 10.071  1.00 28.55 ? 245 VAL   A HG11 1 
ATOM   3681 H  HG12 . VAL   A 1 245 ? -0.846  -21.943 10.037  1.00 28.55 ? 245 VAL   A HG12 1 
ATOM   3682 H  HG13 . VAL   A 1 245 ? -1.569  -22.287 11.407  1.00 28.55 ? 245 VAL   A HG13 1 
ATOM   3683 H  HG21 . VAL   A 1 245 ? -4.256  -22.314 10.783  1.00 27.89 ? 245 VAL   A HG21 1 
ATOM   3684 H  HG22 . VAL   A 1 245 ? -3.905  -21.194 11.853  1.00 27.89 ? 245 VAL   A HG22 1 
ATOM   3685 H  HG23 . VAL   A 1 245 ? -4.717  -20.813 10.542  1.00 27.89 ? 245 VAL   A HG23 1 
ATOM   3686 N  N    . ALA   A 1 246 ? -3.217  -18.230 9.015   1.00 18.33 ? 246 ALA   A N    1 
ATOM   3687 C  CA   . ALA   A 1 246 ? -4.079  -17.125 8.614   1.00 18.70 ? 246 ALA   A CA   1 
ATOM   3688 C  C    . ALA   A 1 246 ? -5.553  -17.456 8.799   1.00 19.63 ? 246 ALA   A C    1 
ATOM   3689 O  O    . ALA   A 1 246 ? -6.363  -16.555 9.041   1.00 22.87 ? 246 ALA   A O    1 
ATOM   3690 C  CB   . ALA   A 1 246 ? -3.807  -16.742 7.159   1.00 17.86 ? 246 ALA   A CB   1 
ATOM   3691 H  H    . ALA   A 1 246 ? -2.765  -18.582 8.374   1.00 22.01 ? 246 ALA   A H    1 
ATOM   3692 H  HA   . ALA   A 1 246 ? -3.876  -16.354 9.167   1.00 22.45 ? 246 ALA   A HA   1 
ATOM   3693 H  HB1  . ALA   A 1 246 ? -4.389  -16.007 6.912   1.00 21.45 ? 246 ALA   A HB1  1 
ATOM   3694 H  HB2  . ALA   A 1 246 ? -2.879  -16.473 7.072   1.00 21.45 ? 246 ALA   A HB2  1 
ATOM   3695 H  HB3  . ALA   A 1 246 ? -3.984  -17.509 6.593   1.00 21.45 ? 246 ALA   A HB3  1 
ATOM   3696 N  N    . ASP   A 1 247 ? -5.927  -18.729 8.680   1.00 18.38 ? 247 ASP   A N    1 
ATOM   3697 C  CA   . ASP   A 1 247 ? -7.328  -19.103 8.800   1.00 21.14 ? 247 ASP   A CA   1 
ATOM   3698 C  C    . ASP   A 1 247 ? -7.881  -18.886 10.206  1.00 19.95 ? 247 ASP   A C    1 
ATOM   3699 O  O    . ASP   A 1 247 ? -9.102  -18.933 10.384  1.00 23.52 ? 247 ASP   A O    1 
ATOM   3700 C  CB   . ASP   A 1 247 ? -7.520  -20.571 8.412   1.00 24.20 ? 247 ASP   A CB   1 
ATOM   3701 C  CG   . ASP   A 1 247 ? -7.478  -20.797 6.908   1.00 27.99 ? 247 ASP   A CG   1 
ATOM   3702 O  OD1  . ASP   A 1 247 ? -7.600  -19.830 6.119   1.00 33.63 ? 247 ASP   A OD1  1 
ATOM   3703 O  OD2  . ASP   A 1 247 ? -7.318  -21.973 6.519   1.00 34.63 ? 247 ASP   A OD2  1 
ATOM   3704 H  H    . ASP   A 1 247 ? -5.393  -19.387 8.531   1.00 22.08 ? 247 ASP   A H    1 
ATOM   3705 H  HA   . ASP   A 1 247 ? -7.851  -18.561 8.189   1.00 25.39 ? 247 ASP   A HA   1 
ATOM   3706 H  HB2  . ASP   A 1 247 ? -6.812  -21.099 8.814   1.00 29.06 ? 247 ASP   A HB2  1 
ATOM   3707 H  HB3  . ASP   A 1 247 ? -8.383  -20.873 8.736   1.00 29.06 ? 247 ASP   A HB3  1 
ATOM   3708 N  N    . ASP   A 1 248 ? -7.030  -18.651 11.199  1.00 19.88 ? 248 ASP   A N    1 
ATOM   3709 C  CA   . ASP   A 1 248 ? -7.483  -18.405 12.564  1.00 20.35 ? 248 ASP   A CA   1 
ATOM   3710 C  C    . ASP   A 1 248 ? -7.653  -16.916 12.862  1.00 19.40 ? 248 ASP   A C    1 
ATOM   3711 O  O    . ASP   A 1 248 ? -7.951  -16.552 14.007  1.00 21.28 ? 248 ASP   A O    1 
ATOM   3712 C  CB   . ASP   A 1 248 ? -6.510  -19.046 13.556  1.00 20.58 ? 248 ASP   A CB   1 
ATOM   3713 C  CG   . ASP   A 1 248 ? -6.544  -20.572 13.504  1.00 26.58 ? 248 ASP   A CG   1 
ATOM   3714 O  OD1  . ASP   A 1 248 ? -7.497  -21.129 12.913  1.00 27.97 ? 248 ASP   A OD1  1 
ATOM   3715 O  OD2  . ASP   A 1 248 ? -5.633  -21.224 14.060  1.00 30.16 ? 248 ASP   A OD2  1 
ATOM   3716 H  H    . ASP   A 1 248 ? -6.175  -18.629 11.108  1.00 23.88 ? 248 ASP   A H    1 
ATOM   3717 H  HA   . ASP   A 1 248 ? -8.347  -18.828 12.687  1.00 24.44 ? 248 ASP   A HA   1 
ATOM   3718 H  HB2  . ASP   A 1 248 ? -5.608  -18.758 13.346  1.00 24.72 ? 248 ASP   A HB2  1 
ATOM   3719 H  HB3  . ASP   A 1 248 ? -6.747  -18.770 14.455  1.00 24.72 ? 248 ASP   A HB3  1 
ATOM   3720 N  N    . TYR   A 1 249 ? -7.494  -16.063 11.850  1.00 19.48 ? 249 TYR   A N    1 
ATOM   3721 C  CA   . TYR   A 1 249 ? -7.650  -14.626 12.018  1.00 18.57 ? 249 TYR   A CA   1 
ATOM   3722 C  C    . TYR   A 1 249 ? -9.119  -14.257 12.207  1.00 21.16 ? 249 TYR   A C    1 
ATOM   3723 O  O    . TYR   A 1 249 ? -10.007 -14.857 11.595  1.00 24.49 ? 249 TYR   A O    1 
ATOM   3724 C  CB   . TYR   A 1 249 ? -7.073  -13.889 10.799  1.00 21.61 ? 249 TYR   A CB   1 
ATOM   3725 C  CG   . TYR   A 1 249 ? -7.278  -12.395 10.850  1.00 20.84 ? 249 TYR   A CG   1 
ATOM   3726 C  CD1  . TYR   A 1 249 ? -6.463  -11.596 11.632  1.00 21.25 ? 249 TYR   A CD1  1 
ATOM   3727 C  CD2  . TYR   A 1 249 ? -8.314  -11.786 10.147  1.00 23.30 ? 249 TYR   A CD2  1 
ATOM   3728 C  CE1  . TYR   A 1 249 ? -6.659  -10.225 11.705  1.00 19.60 ? 249 TYR   A CE1  1 
ATOM   3729 C  CE2  . TYR   A 1 249 ? -8.513  -10.418 10.211  1.00 22.64 ? 249 TYR   A CE2  1 
ATOM   3730 C  CZ   . TYR   A 1 249 ? -7.680  -9.643  10.990  1.00 24.64 ? 249 TYR   A CZ   1 
ATOM   3731 O  OH   . TYR   A 1 249 ? -7.867  -8.286  11.069  1.00 27.43 ? 249 TYR   A OH   1 
ATOM   3732 H  H    . TYR   A 1 249 ? -7.293  -16.297 11.047  1.00 23.40 ? 249 TYR   A H    1 
ATOM   3733 H  HA   . TYR   A 1 249 ? -7.161  -14.341 12.806  1.00 22.31 ? 249 TYR   A HA   1 
ATOM   3734 H  HB2  . TYR   A 1 249 ? -6.119  -14.057 10.753  1.00 25.95 ? 249 TYR   A HB2  1 
ATOM   3735 H  HB3  . TYR   A 1 249 ? -7.506  -14.222 9.997   1.00 25.95 ? 249 TYR   A HB3  1 
ATOM   3736 H  HD1  . TYR   A 1 249 ? -5.771  -11.985 12.117  1.00 25.52 ? 249 TYR   A HD1  1 
ATOM   3737 H  HD2  . TYR   A 1 249 ? -8.877  -12.306 9.620   1.00 27.98 ? 249 TYR   A HD2  1 
ATOM   3738 H  HE1  . TYR   A 1 249 ? -6.098  -9.700  12.229  1.00 23.54 ? 249 TYR   A HE1  1 
ATOM   3739 H  HE2  . TYR   A 1 249 ? -9.205  -10.023 9.731   1.00 27.18 ? 249 TYR   A HE2  1 
ATOM   3740 H  HH   . TYR   A 1 249 ? -8.518  -8.057  10.589  1.00 32.94 ? 249 TYR   A HH   1 
ATOM   3741 N  N    . TYR   A 1 250 ? -9.376  -13.274 13.078  1.00 19.91 ? 250 TYR   A N    1 
ATOM   3742 C  CA   . TYR   A 1 250 ? -10.707 -12.689 13.248  1.00 20.95 ? 250 TYR   A CA   1 
ATOM   3743 C  C    . TYR   A 1 250 ? -10.524 -11.182 13.410  1.00 25.73 ? 250 TYR   A C    1 
ATOM   3744 O  O    . TYR   A 1 250 ? -9.458  -10.705 13.808  1.00 22.73 ? 250 TYR   A O    1 
ATOM   3745 C  CB   . TYR   A 1 250 ? -11.489 -13.319 14.438  1.00 22.34 ? 250 TYR   A CB   1 
ATOM   3746 C  CG   . TYR   A 1 250 ? -10.745 -13.466 15.752  1.00 25.18 ? 250 TYR   A CG   1 
ATOM   3747 C  CD1  . TYR   A 1 250 ? -9.941  -14.570 15.993  1.00 25.96 ? 250 TYR   A CD1  1 
ATOM   3748 C  CD2  . TYR   A 1 250 ? -10.920 -12.547 16.792  1.00 23.52 ? 250 TYR   A CD2  1 
ATOM   3749 C  CE1  . TYR   A 1 250 ? -9.258  -14.720 17.200  1.00 24.61 ? 250 TYR   A CE1  1 
ATOM   3750 C  CE2  . TYR   A 1 250 ? -10.253 -12.704 18.015  1.00 30.72 ? 250 TYR   A CE2  1 
ATOM   3751 C  CZ   . TYR   A 1 250 ? -9.430  -13.797 18.211  1.00 28.81 ? 250 TYR   A CZ   1 
ATOM   3752 O  OH   . TYR   A 1 250 ? -8.755  -13.970 19.405  1.00 27.55 ? 250 TYR   A OH   1 
ATOM   3753 H  H    . TYR   A 1 250 ? -8.781  -12.924 13.591  1.00 23.91 ? 250 TYR   A H    1 
ATOM   3754 H  HA   . TYR   A 1 250 ? -11.223 -12.841 12.441  1.00 25.15 ? 250 TYR   A HA   1 
ATOM   3755 H  HB2  . TYR   A 1 250 ? -12.269 -12.768 14.611  1.00 26.82 ? 250 TYR   A HB2  1 
ATOM   3756 H  HB3  . TYR   A 1 250 ? -11.778 -14.206 14.173  1.00 26.82 ? 250 TYR   A HB3  1 
ATOM   3757 H  HD1  . TYR   A 1 250 ? -9.813  -15.196 15.317  1.00 31.17 ? 250 TYR   A HD1  1 
ATOM   3758 H  HD2  . TYR   A 1 250 ? -11.468 -11.809 16.662  1.00 28.24 ? 250 TYR   A HD2  1 
ATOM   3759 H  HE1  . TYR   A 1 250 ? -8.711  -15.460 17.335  1.00 29.56 ? 250 TYR   A HE1  1 
ATOM   3760 H  HE2  . TYR   A 1 250 ? -10.362 -12.074 18.691  1.00 36.88 ? 250 TYR   A HE2  1 
ATOM   3761 H  HH   . TYR   A 1 250 ? -8.943  -13.346 19.934  1.00 33.08 ? 250 TYR   A HH   1 
ATOM   3762 N  N    . GLY   A 1 251 ? -11.577 -10.428 13.087  1.00 30.36 ? 251 GLY   A N    1 
ATOM   3763 C  CA   . GLY   A 1 251 ? -11.468 -8.982  12.954  1.00 29.53 ? 251 GLY   A CA   1 
ATOM   3764 C  C    . GLY   A 1 251 ? -11.127 -8.245  14.234  1.00 29.34 ? 251 GLY   A C    1 
ATOM   3765 O  O    . GLY   A 1 251 ? -10.644 -7.105  14.172  1.00 36.77 ? 251 GLY   A O    1 
ATOM   3766 H  H    . GLY   A 1 251 ? -12.367 -10.735 12.940  1.00 36.45 ? 251 GLY   A H    1 
ATOM   3767 H  HA2  . GLY   A 1 251 ? -10.782 -8.777  12.300  1.00 35.45 ? 251 GLY   A HA2  1 
ATOM   3768 H  HA3  . GLY   A 1 251 ? -12.310 -8.632  12.624  1.00 35.45 ? 251 GLY   A HA3  1 
ATOM   3769 N  N    . GLY   A 1 252 ? -11.375 -8.853  15.396  1.00 25.50 ? 252 GLY   A N    1 
ATOM   3770 C  CA   . GLY   A 1 252 ? -11.076 -8.245  16.675  1.00 26.34 ? 252 GLY   A CA   1 
ATOM   3771 C  C    . GLY   A 1 252 ? -9.723  -8.589  17.250  1.00 23.00 ? 252 GLY   A C    1 
ATOM   3772 O  O    . GLY   A 1 252 ? -9.412  -8.231  18.391  1.00 26.37 ? 252 GLY   A O    1 
ATOM   3773 H  H    . GLY   A 1 252 ? -11.724 -9.636  15.462  1.00 30.62 ? 252 GLY   A H    1 
ATOM   3774 H  HA2  . GLY   A 1 252 ? -11.125 -7.281  16.584  1.00 31.63 ? 252 GLY   A HA2  1 
ATOM   3775 H  HA3  . GLY   A 1 252 ? -11.750 -8.519  17.317  1.00 31.63 ? 252 GLY   A HA3  1 
ATOM   3776 N  N    . LEU   A 1 253 ? -8.897  -9.285  16.489  1.00 20.75 ? 253 LEU   A N    1 
ATOM   3777 C  CA   . LEU   A 1 253 ? -7.606  -9.720  16.986  1.00 20.01 ? 253 LEU   A CA   1 
ATOM   3778 C  C    . LEU   A 1 253 ? -6.602  -8.583  16.842  1.00 18.24 ? 253 LEU   A C    1 
ATOM   3779 O  O    . LEU   A 1 253 ? -6.425  -8.031  15.753  1.00 20.22 ? 253 LEU   A O    1 
ATOM   3780 C  CB   . LEU   A 1 253 ? -7.152  -10.941 16.200  1.00 20.41 ? 253 LEU   A CB   1 
ATOM   3781 C  CG   . LEU   A 1 253 ? -5.936  -11.735 16.678  1.00 25.28 ? 253 LEU   A CG   1 
ATOM   3782 C  CD1  . LEU   A 1 253 ? -6.217  -12.261 18.066  1.00 21.30 ? 253 LEU   A CD1  1 
ATOM   3783 C  CD2  . LEU   A 1 253 ? -5.690  -12.851 15.676  1.00 21.16 ? 253 LEU   A CD2  1 
ATOM   3784 H  H    . LEU   A 1 253 ? -9.060  -9.519  15.678  1.00 24.92 ? 253 LEU   A H    1 
ATOM   3785 H  HA   . LEU   A 1 253 ? -7.681  -9.955  17.924  1.00 24.03 ? 253 LEU   A HA   1 
ATOM   3786 H  HB2  . LEU   A 1 253 ? -7.895  -11.564 16.172  1.00 24.51 ? 253 LEU   A HB2  1 
ATOM   3787 H  HB3  . LEU   A 1 253 ? -6.954  -10.650 15.296  1.00 24.51 ? 253 LEU   A HB3  1 
ATOM   3788 H  HG   . LEU   A 1 253 ? -5.156  -11.160 16.709  1.00 30.36 ? 253 LEU   A HG   1 
ATOM   3789 H  HD11 . LEU   A 1 253 ? -5.472  -12.815 18.347  1.00 25.58 ? 253 LEU   A HD11 1 
ATOM   3790 H  HD12 . LEU   A 1 253 ? -6.321  -11.515 18.677  1.00 25.58 ? 253 LEU   A HD12 1 
ATOM   3791 H  HD13 . LEU   A 1 253 ? -7.027  -12.788 18.043  1.00 25.58 ? 253 LEU   A HD13 1 
ATOM   3792 H  HD21 . LEU   A 1 253 ? -4.924  -13.371 15.965  1.00 25.41 ? 253 LEU   A HD21 1 
ATOM   3793 H  HD22 . LEU   A 1 253 ? -6.477  -13.416 15.634  1.00 25.41 ? 253 LEU   A HD22 1 
ATOM   3794 H  HD23 . LEU   A 1 253 ? -5.516  -12.460 14.805  1.00 25.41 ? 253 LEU   A HD23 1 
ATOM   3795 N  N    . ASP   A 1 254 ? -5.967  -8.217  17.949  1.00 17.17 ? 254 ASP   A N    1 
ATOM   3796 C  CA   . ASP   A 1 254 ? -4.988  -7.140  17.935  1.00 17.87 ? 254 ASP   A CA   1 
ATOM   3797 C  C    . ASP   A 1 254 ? -3.772  -7.517  17.091  1.00 17.09 ? 254 ASP   A C    1 
ATOM   3798 O  O    . ASP   A 1 254 ? -3.438  -8.698  16.944  1.00 16.28 ? 254 ASP   A O    1 
ATOM   3799 C  CB   . ASP   A 1 254 ? -4.539  -6.814  19.361  1.00 18.11 ? 254 ASP   A CB   1 
ATOM   3800 C  CG   . ASP   A 1 254 ? -3.601  -5.640  19.420  1.00 18.06 ? 254 ASP   A CG   1 
ATOM   3801 O  OD1  . ASP   A 1 254 ? -4.092  -4.503  19.263  1.00 21.12 ? 254 ASP   A OD1  1 
ATOM   3802 O  OD2  . ASP   A 1 254 ? -2.382  -5.863  19.604  1.00 16.78 ? 254 ASP   A OD2  1 
ATOM   3803 H  H    . ASP   A 1 254 ? -6.085  -8.577  18.721  1.00 20.62 ? 254 ASP   A H    1 
ATOM   3804 H  HA   . ASP   A 1 254 ? -5.391  -6.345  17.552  1.00 21.46 ? 254 ASP   A HA   1 
ATOM   3805 H  HB2  . ASP   A 1 254 ? -5.319  -6.602  19.897  1.00 21.75 ? 254 ASP   A HB2  1 
ATOM   3806 H  HB3  . ASP   A 1 254 ? -4.080  -7.584  19.732  1.00 21.75 ? 254 ASP   A HB3  1 
ATOM   3807 N  N    . VAL   A 1 255 ? -3.089  -6.492  16.567  1.00 16.62 ? 255 VAL   A N    1 
ATOM   3808 C  CA   . VAL   A 1 255 ? -1.929  -6.705  15.697  1.00 13.91 ? 255 VAL   A CA   1 
ATOM   3809 C  C    . VAL   A 1 255 ? -0.818  -7.493  16.397  1.00 14.24 ? 255 VAL   A C    1 
ATOM   3810 O  O    . VAL   A 1 255 ? -0.006  -8.142  15.732  1.00 15.40 ? 255 VAL   A O    1 
ATOM   3811 C  CB   . VAL   A 1 255 ? -1.383  -5.356  15.178  1.00 15.20 ? 255 VAL   A CB   1 
ATOM   3812 C  CG1  . VAL   A 1 255 ? -2.395  -4.664  14.257  1.00 16.52 ? 255 VAL   A CG1  1 
ATOM   3813 C  CG2  . VAL   A 1 255 ? -0.989  -4.460  16.349  1.00 16.50 ? 255 VAL   A CG2  1 
ATOM   3814 H  H    . VAL   A 1 255 ? -3.282  -5.665  16.699  1.00 19.97 ? 255 VAL   A H    1 
ATOM   3815 H  HA   . VAL   A 1 255 ? -2.213  -7.222  14.927  1.00 16.71 ? 255 VAL   A HA   1 
ATOM   3816 H  HB   . VAL   A 1 255 ? -0.582  -5.527  14.658  1.00 18.26 ? 255 VAL   A HB   1 
ATOM   3817 H  HG11 . VAL   A 1 255 ? -2.021  -3.822  13.953  1.00 19.84 ? 255 VAL   A HG11 1 
ATOM   3818 H  HG12 . VAL   A 1 255 ? -2.575  -5.240  13.497  1.00 19.84 ? 255 VAL   A HG12 1 
ATOM   3819 H  HG13 . VAL   A 1 255 ? -3.213  -4.503  14.752  1.00 19.84 ? 255 VAL   A HG13 1 
ATOM   3820 H  HG21 . VAL   A 1 255 ? -0.644  -3.624  16.000  1.00 19.81 ? 255 VAL   A HG21 1 
ATOM   3821 H  HG22 . VAL   A 1 255 ? -1.770  -4.289  16.898  1.00 19.81 ? 255 VAL   A HG22 1 
ATOM   3822 H  HG23 . VAL   A 1 255 ? -0.305  -4.903  16.874  1.00 19.81 ? 255 VAL   A HG23 1 
ATOM   3823 N  N    . HIS   A 1 256 ? -0.744  -7.430  17.732  1.00 15.18 ? 256 HIS   A N    1 
ATOM   3824 C  CA   . HIS   A 1 256 ? 0.288   -8.145  18.489  1.00 15.47 ? 256 HIS   A CA   1 
ATOM   3825 C  C    . HIS   A 1 256 ? 0.002   -9.630  18.628  1.00 16.29 ? 256 HIS   A C    1 
ATOM   3826 O  O    . HIS   A 1 256 ? 0.849   -10.365 19.149  1.00 15.05 ? 256 HIS   A O    1 
ATOM   3827 C  CB   . HIS   A 1 256 ? 0.429   -7.491  19.871  1.00 15.13 ? 256 HIS   A CB   1 
ATOM   3828 C  CG   . HIS   A 1 256 ? 0.982   -6.102  19.800  1.00 16.52 ? 256 HIS   A CG   1 
ATOM   3829 N  ND1  . HIS   A 1 256 ? 0.178   -4.985  19.822  1.00 16.18 ? 256 HIS   A ND1  1 
ATOM   3830 C  CD2  . HIS   A 1 256 ? 2.255   -5.649  19.714  1.00 15.43 ? 256 HIS   A CD2  1 
ATOM   3831 C  CE1  . HIS   A 1 256 ? 0.926   -3.905  19.715  1.00 17.30 ? 256 HIS   A CE1  1 
ATOM   3832 N  NE2  . HIS   A 1 256 ? 2.194   -4.279  19.657  1.00 16.95 ? 256 HIS   A NE2  1 
ATOM   3833 H  H    . HIS   A 1 256 ? -1.284  -6.976  18.224  1.00 18.23 ? 256 HIS   A H    1 
ATOM   3834 H  HA   . HIS   A 1 256 ? 1.136   -8.049  18.028  1.00 18.59 ? 256 HIS   A HA   1 
ATOM   3835 H  HB2  . HIS   A 1 256 ? -0.445  -7.445  20.290  1.00 18.18 ? 256 HIS   A HB2  1 
ATOM   3836 H  HB3  . HIS   A 1 256 ? 1.029   -8.026  20.414  1.00 18.18 ? 256 HIS   A HB3  1 
ATOM   3837 H  HD1  . HIS   A 1 256 ? -0.681  -4.992  19.862  1.00 19.43 ? 256 HIS   A HD1  1 
ATOM   3838 H  HD2  . HIS   A 1 256 ? 3.025   -6.169  19.677  1.00 18.53 ? 256 HIS   A HD2  1 
ATOM   3839 H  HE1  . HIS   A 1 256 ? 0.617   -3.028  19.713  1.00 20.78 ? 256 HIS   A HE1  1 
ATOM   3840 H  HE2  . HIS   A 1 256 ? 2.870   -3.750  19.601  1.00 20.36 ? 256 HIS   A HE2  1 
ATOM   3841 N  N    . TYR   A 1 257 ? -1.169  -10.074 18.187  1.00 15.38 ? 257 TYR   A N    1 
ATOM   3842 C  CA   . TYR   A 1 257 ? -1.566  -11.473 18.171  1.00 14.08 ? 257 TYR   A CA   1 
ATOM   3843 C  C    . TYR   A 1 257 ? -1.711  -12.002 16.753  1.00 16.67 ? 257 TYR   A C    1 
ATOM   3844 O  O    . TYR   A 1 257 ? -1.315  -13.134 16.467  1.00 15.83 ? 257 TYR   A O    1 
ATOM   3845 C  CB   . TYR   A 1 257 ? -2.889  -11.620 18.932  1.00 16.70 ? 257 TYR   A CB   1 
ATOM   3846 C  CG   . TYR   A 1 257 ? -2.803  -11.134 20.377  1.00 15.84 ? 257 TYR   A CG   1 
ATOM   3847 C  CD1  . TYR   A 1 257 ? -1.710  -11.432 21.180  1.00 17.00 ? 257 TYR   A CD1  1 
ATOM   3848 C  CD2  . TYR   A 1 257 ? -3.809  -10.336 20.919  1.00 16.54 ? 257 TYR   A CD2  1 
ATOM   3849 C  CE1  . TYR   A 1 257 ? -1.632  -10.971 22.490  1.00 18.07 ? 257 TYR   A CE1  1 
ATOM   3850 C  CE2  . TYR   A 1 257 ? -3.739  -9.876  22.226  1.00 19.67 ? 257 TYR   A CE2  1 
ATOM   3851 C  CZ   . TYR   A 1 257 ? -2.647  -10.204 23.010  1.00 21.12 ? 257 TYR   A CZ   1 
ATOM   3852 O  OH   . TYR   A 1 257 ? -2.551  -9.751  24.309  1.00 22.77 ? 257 TYR   A OH   1 
ATOM   3853 H  H    . TYR   A 1 257 ? -1.781  -9.555  17.877  1.00 18.47 ? 257 TYR   A H    1 
ATOM   3854 H  HA   . TYR   A 1 257 ? -0.892  -12.004 18.622  1.00 16.91 ? 257 TYR   A HA   1 
ATOM   3855 H  HB2  . TYR   A 1 257 ? -3.571  -11.098 18.481  1.00 20.06 ? 257 TYR   A HB2  1 
ATOM   3856 H  HB3  . TYR   A 1 257 ? -3.143  -12.556 18.946  1.00 20.06 ? 257 TYR   A HB3  1 
ATOM   3857 H  HD1  . TYR   A 1 257 ? -1.022  -11.957 20.839  1.00 20.42 ? 257 TYR   A HD1  1 
ATOM   3858 H  HD2  . TYR   A 1 257 ? -4.549  -10.119 20.399  1.00 19.87 ? 257 TYR   A HD2  1 
ATOM   3859 H  HE1  . TYR   A 1 257 ? -0.897  -11.189 23.017  1.00 21.71 ? 257 TYR   A HE1  1 
ATOM   3860 H  HE2  . TYR   A 1 257 ? -4.424  -9.353  22.575  1.00 23.62 ? 257 TYR   A HE2  1 
ATOM   3861 H  HH   . TYR   A 1 257 ? -3.229  -9.296  24.506  1.00 27.34 ? 257 TYR   A HH   1 
ATOM   3862 N  N    . SER   A 1 258 ? -2.245  -11.192 15.835  1.00 16.23 ? 258 SER   A N    1 
ATOM   3863 C  CA   . SER   A 1 258 ? -2.282  -11.587 14.434  1.00 15.58 ? 258 SER   A CA   1 
ATOM   3864 C  C    . SER   A 1 258 ? -0.899  -11.557 13.804  1.00 16.45 ? 258 SER   A C    1 
ATOM   3865 O  O    . SER   A 1 258 ? -0.715  -12.110 12.710  1.00 15.57 ? 258 SER   A O    1 
ATOM   3866 C  CB   . SER   A 1 258 ? -3.230  -10.671 13.678  1.00 17.05 ? 258 SER   A CB   1 
ATOM   3867 O  OG   . SER   A 1 258 ? -2.673  -9.383  13.614  1.00 16.38 ? 258 SER   A OG   1 
ATOM   3868 H  H    . SER   A 1 258 ? -2.587  -10.420 15.999  1.00 19.49 ? 258 SER   A H    1 
ATOM   3869 H  HA   . SER   A 1 258 ? -2.623  -12.493 14.369  1.00 18.71 ? 258 SER   A HA   1 
ATOM   3870 H  HB2  . SER   A 1 258 ? -3.356  -11.011 12.778  1.00 20.48 ? 258 SER   A HB2  1 
ATOM   3871 H  HB3  . SER   A 1 258 ? -4.079  -10.631 14.146  1.00 20.48 ? 258 SER   A HB3  1 
ATOM   3872 H  HG   . SER   A 1 258 ? -3.189  -8.867  13.198  1.00 19.67 ? 258 SER   A HG   1 
ATOM   3873 N  N    . SER   A 1 259 ? 0.074   -10.946 14.483  1.00 15.47 ? 259 SER   A N    1 
ATOM   3874 C  CA   . SER   A 1 259 ? 1.462   -11.027 14.051  1.00 14.12 ? 259 SER   A CA   1 
ATOM   3875 C  C    . SER   A 1 259 ? 1.972   -12.462 14.038  1.00 14.65 ? 259 SER   A C    1 
ATOM   3876 O  O    . SER   A 1 259 ? 2.997   -12.742 13.412  1.00 15.06 ? 259 SER   A O    1 
ATOM   3877 C  CB   . SER   A 1 259 ? 2.356   -10.192 14.966  1.00 14.45 ? 259 SER   A CB   1 
ATOM   3878 O  OG   . SER   A 1 259 ? 2.228   -10.614 16.310  1.00 13.99 ? 259 SER   A OG   1 
ATOM   3879 H  H    . SER   A 1 259 ? -0.046  -10.479 15.195  1.00 18.59 ? 259 SER   A H    1 
ATOM   3880 H  HA   . SER   A 1 259 ? 1.536   -10.672 13.151  1.00 16.96 ? 259 SER   A HA   1 
ATOM   3881 H  HB2  . SER   A 1 259 ? 3.280   -10.292 14.687  1.00 17.36 ? 259 SER   A HB2  1 
ATOM   3882 H  HB3  . SER   A 1 259 ? 2.086   -9.264  14.901  1.00 17.36 ? 259 SER   A HB3  1 
ATOM   3883 H  HG   . SER   A 1 259 ? 2.723   -10.150 16.805  1.00 16.81 ? 259 SER   A HG   1 
ATOM   3884 N  N    . GLY   A 1 260 ? 1.286   -13.376 14.720  1.00 13.90 ? 260 GLY   A N    1 
ATOM   3885 C  CA   . GLY   A 1 260 ? 1.709   -14.761 14.678  1.00 14.51 ? 260 GLY   A CA   1 
ATOM   3886 C  C    . GLY   A 1 260 ? 1.762   -15.342 13.278  1.00 16.44 ? 260 GLY   A C    1 
ATOM   3887 O  O    . GLY   A 1 260 ? 2.569   -16.232 13.008  1.00 15.86 ? 260 GLY   A O    1 
ATOM   3888 H  H    . GLY   A 1 260 ? 0.591   -13.222 15.202  1.00 16.70 ? 260 GLY   A H    1 
ATOM   3889 H  HA2  . GLY   A 1 260 ? 2.594   -14.834 15.067  1.00 17.43 ? 260 GLY   A HA2  1 
ATOM   3890 H  HA3  . GLY   A 1 260 ? 1.101   -15.294 15.211  1.00 17.43 ? 260 GLY   A HA3  1 
ATOM   3891 N  N    . VAL   A 1 261 ? 0.900   -14.864 12.374  1.00 15.54 ? 261 VAL   A N    1 
ATOM   3892 C  CA   . VAL   A 1 261 ? 0.843   -15.460 11.035  1.00 15.98 ? 261 VAL   A CA   1 
ATOM   3893 C  C    . VAL   A 1 261 ? 2.185   -15.285 10.324  1.00 15.33 ? 261 VAL   A C    1 
ATOM   3894 O  O    . VAL   A 1 261 ? 2.819   -16.261 9.906   1.00 16.13 ? 261 VAL   A O    1 
ATOM   3895 C  CB   . VAL   A 1 261 ? -0.306  -14.854 10.207  1.00 14.77 ? 261 VAL   A CB   1 
ATOM   3896 C  CG1  . VAL   A 1 261 ? -0.302  -15.427 8.768   1.00 18.78 ? 261 VAL   A CG1  1 
ATOM   3897 C  CG2  . VAL   A 1 261 ? -1.659  -15.087 10.881  1.00 17.14 ? 261 VAL   A CG2  1 
ATOM   3898 H  H    . VAL   A 1 261 ? 0.352   -14.214 12.505  1.00 18.67 ? 261 VAL   A H    1 
ATOM   3899 H  HA   . VAL   A 1 261 ? 0.676   -16.411 11.123  1.00 19.19 ? 261 VAL   A HA   1 
ATOM   3900 H  HB   . VAL   A 1 261 ? -0.170  -13.896 10.143  1.00 17.75 ? 261 VAL   A HB   1 
ATOM   3901 H  HG11 . VAL   A 1 261 ? -1.142  -15.201 8.338   1.00 22.56 ? 261 VAL   A HG11 1 
ATOM   3902 H  HG12 . VAL   A 1 261 ? 0.436   -15.039 8.273   1.00 22.56 ? 261 VAL   A HG12 1 
ATOM   3903 H  HG13 . VAL   A 1 261 ? -0.203  -16.391 8.813   1.00 22.56 ? 261 VAL   A HG13 1 
ATOM   3904 H  HG21 . VAL   A 1 261 ? -2.359  -14.719 10.319  1.00 20.59 ? 261 VAL   A HG21 1 
ATOM   3905 H  HG22 . VAL   A 1 261 ? -1.794  -16.041 10.996  1.00 20.59 ? 261 VAL   A HG22 1 
ATOM   3906 H  HG23 . VAL   A 1 261 ? -1.662  -14.646 11.745  1.00 20.59 ? 261 VAL   A HG23 1 
ATOM   3907 N  N    . TYR   A 1 262 ? 2.627   -14.036 10.161  1.00 14.62 ? 262 TYR   A N    1 
ATOM   3908 C  CA   . TYR   A 1 262 ? 3.871   -13.792 9.443   1.00 13.67 ? 262 TYR   A CA   1 
ATOM   3909 C  C    . TYR   A 1 262 ? 5.091   -14.110 10.295  1.00 14.51 ? 262 TYR   A C    1 
ATOM   3910 O  O    . TYR   A 1 262 ? 6.163   -14.372 9.736   1.00 14.71 ? 262 TYR   A O    1 
ATOM   3911 C  CB   . TYR   A 1 262 ? 3.912   -12.345 8.922   1.00 15.57 ? 262 TYR   A CB   1 
ATOM   3912 C  CG   . TYR   A 1 262 ? 3.371   -12.240 7.497   1.00 16.88 ? 262 TYR   A CG   1 
ATOM   3913 C  CD1  . TYR   A 1 262 ? 2.045   -12.566 7.210   1.00 15.84 ? 262 TYR   A CD1  1 
ATOM   3914 C  CD2  . TYR   A 1 262 ? 4.187   -11.860 6.440   1.00 17.88 ? 262 TYR   A CD2  1 
ATOM   3915 C  CE1  . TYR   A 1 262 ? 1.555   -12.509 5.913   1.00 14.79 ? 262 TYR   A CE1  1 
ATOM   3916 C  CE2  . TYR   A 1 262 ? 3.695   -11.792 5.142   1.00 16.99 ? 262 TYR   A CE2  1 
ATOM   3917 C  CZ   . TYR   A 1 262 ? 2.390   -12.119 4.882   1.00 15.05 ? 262 TYR   A CZ   1 
ATOM   3918 O  OH   . TYR   A 1 262 ? 1.922   -12.048 3.589   1.00 17.72 ? 262 TYR   A OH   1 
ATOM   3919 H  H    . TYR   A 1 262 ? 2.232   -13.329 10.451  1.00 17.56 ? 262 TYR   A H    1 
ATOM   3920 H  HA   . TYR   A 1 262 ? 3.896   -14.376 8.670   1.00 16.43 ? 262 TYR   A HA   1 
ATOM   3921 H  HB2  . TYR   A 1 262 ? 3.364   -11.783 9.491   1.00 18.70 ? 262 TYR   A HB2  1 
ATOM   3922 H  HB3  . TYR   A 1 262 ? 4.830   -12.030 8.923   1.00 18.70 ? 262 TYR   A HB3  1 
ATOM   3923 H  HD1  . TYR   A 1 262 ? 1.482   -12.836 7.899   1.00 19.02 ? 262 TYR   A HD1  1 
ATOM   3924 H  HD2  . TYR   A 1 262 ? 5.076   -11.643 6.604   1.00 21.47 ? 262 TYR   A HD2  1 
ATOM   3925 H  HE1  . TYR   A 1 262 ? 0.667   -12.725 5.739   1.00 17.77 ? 262 TYR   A HE1  1 
ATOM   3926 H  HE2  . TYR   A 1 262 ? 4.255   -11.533 4.447   1.00 20.40 ? 262 TYR   A HE2  1 
ATOM   3927 H  HH   . TYR   A 1 262 ? 1.112   -12.268 3.564   1.00 21.28 ? 262 TYR   A HH   1 
ATOM   3928 N  N    . ASN   A 1 263 ? 4.952   -14.121 11.627  1.00 14.70 ? 263 ASN   A N    1 
ATOM   3929 C  CA   . ASN   A 1 263 ? 6.073   -14.554 12.457  1.00 14.59 ? 263 ASN   A CA   1 
ATOM   3930 C  C    . ASN   A 1 263 ? 6.337   -16.039 12.233  1.00 15.78 ? 263 ASN   A C    1 
ATOM   3931 O  O    . ASN   A 1 263 ? 7.488   -16.470 12.064  1.00 14.49 ? 263 ASN   A O    1 
ATOM   3932 C  CB   . ASN   A 1 263 ? 5.783   -14.313 13.937  1.00 15.23 ? 263 ASN   A CB   1 
ATOM   3933 C  CG   . ASN   A 1 263 ? 5.975   -12.870 14.340  1.00 13.38 ? 263 ASN   A CG   1 
ATOM   3934 O  OD1  . ASN   A 1 263 ? 6.312   -12.018 13.512  1.00 16.20 ? 263 ASN   A OD1  1 
ATOM   3935 N  ND2  . ASN   A 1 263 ? 5.842   -12.595 15.636  1.00 15.37 ? 263 ASN   A ND2  1 
ATOM   3936 H  H    . ASN   A 1 263 ? 4.244   -13.891 12.058  1.00 17.66 ? 263 ASN   A H    1 
ATOM   3937 H  HA   . ASN   A 1 263 ? 6.870   -14.058 12.212  1.00 17.52 ? 263 ASN   A HA   1 
ATOM   3938 H  HB2  . ASN   A 1 263 ? 4.862   -14.556 14.122  1.00 18.29 ? 263 ASN   A HB2  1 
ATOM   3939 H  HB3  . ASN   A 1 263 ? 6.384   -14.857 14.470  1.00 18.29 ? 263 ASN   A HB3  1 
ATOM   3940 H  HD21 . ASN   A 1 263 ? 5.948   -11.789 15.918  1.00 18.46 ? 263 ASN   A HD21 1 
ATOM   3941 H  HD22 . ASN   A 1 263 ? 5.620   -13.217 16.187  1.00 18.46 ? 263 ASN   A HD22 1 
ATOM   3942 N  N    . HIS   A 1 264 ? 5.268   -16.836 12.238  1.00 14.66 ? 264 HIS   A N    1 
ATOM   3943 C  CA   . HIS   A 1 264 ? 5.381   -18.267 11.997  1.00 14.19 ? 264 HIS   A CA   1 
ATOM   3944 C  C    . HIS   A 1 264 ? 5.879   -18.526 10.580  1.00 16.73 ? 264 HIS   A C    1 
ATOM   3945 O  O    . HIS   A 1 264 ? 6.744   -19.382 10.360  1.00 17.19 ? 264 HIS   A O    1 
ATOM   3946 C  CB   . HIS   A 1 264 ? 4.013   -18.903 12.250  1.00 16.03 ? 264 HIS   A CB   1 
ATOM   3947 C  CG   . HIS   A 1 264 ? 4.040   -20.391 12.352  1.00 18.25 ? 264 HIS   A CG   1 
ATOM   3948 N  ND1  . HIS   A 1 264 ? 2.898   -21.156 12.260  1.00 19.97 ? 264 HIS   A ND1  1 
ATOM   3949 C  CD2  . HIS   A 1 264 ? 5.057   -21.252 12.573  1.00 18.60 ? 264 HIS   A CD2  1 
ATOM   3950 C  CE1  . HIS   A 1 264 ? 3.217   -22.433 12.390  1.00 22.68 ? 264 HIS   A CE1  1 
ATOM   3951 N  NE2  . HIS   A 1 264 ? 4.522   -22.518 12.583  1.00 19.91 ? 264 HIS   A NE2  1 
ATOM   3952 H  H    . HIS   A 1 264 ? 4.463   -16.567 12.380  1.00 17.61 ? 264 HIS   A H    1 
ATOM   3953 H  HA   . HIS   A 1 264 ? 6.019   -18.648 12.621  1.00 17.04 ? 264 HIS   A HA   1 
ATOM   3954 H  HB2  . HIS   A 1 264 ? 3.658   -18.556 13.084  1.00 19.26 ? 264 HIS   A HB2  1 
ATOM   3955 H  HB3  . HIS   A 1 264 ? 3.421   -18.668 11.519  1.00 19.26 ? 264 HIS   A HB3  1 
ATOM   3956 H  HD1  . HIS   A 1 264 ? 2.106   -20.853 12.120  1.00 23.98 ? 264 HIS   A HD1  1 
ATOM   3957 H  HD2  . HIS   A 1 264 ? 5.954   -21.031 12.679  1.00 22.34 ? 264 HIS   A HD2  1 
ATOM   3958 H  HE1  . HIS   A 1 264 ? 2.623   -23.148 12.361  1.00 27.24 ? 264 HIS   A HE1  1 
ATOM   3959 N  N    . LEU   A 1 265 ? 5.372   -17.756 9.615   1.00 16.39 ? 265 LEU   A N    1 
ATOM   3960 C  CA   . LEU   A 1 265 ? 5.826   -17.878 8.231   1.00 18.05 ? 265 LEU   A CA   1 
ATOM   3961 C  C    . LEU   A 1 265 ? 7.322   -17.620 8.113   1.00 17.35 ? 265 LEU   A C    1 
ATOM   3962 O  O    . LEU   A 1 265 ? 8.033   -18.341 7.403   1.00 17.15 ? 265 LEU   A O    1 
ATOM   3963 C  CB   . LEU   A 1 265 ? 5.047   -16.896 7.362   1.00 15.81 ? 265 LEU   A CB   1 
ATOM   3964 C  CG   . LEU   A 1 265 ? 5.496   -16.690 5.927   1.00 14.25 ? 265 LEU   A CG   1 
ATOM   3965 C  CD1  . LEU   A 1 265 ? 5.400   -17.976 5.137   1.00 17.63 ? 265 LEU   A CD1  1 
ATOM   3966 C  CD2  . LEU   A 1 265 ? 4.654   -15.619 5.263   1.00 19.25 ? 265 LEU   A CD2  1 
ATOM   3967 H  H    . LEU   A 1 265 ? 4.766   -17.158 9.736   1.00 19.68 ? 265 LEU   A H    1 
ATOM   3968 H  HA   . LEU   A 1 265 ? 5.646   -18.776 7.912   1.00 21.68 ? 265 LEU   A HA   1 
ATOM   3969 H  HB2  . LEU   A 1 265 ? 4.125   -17.194 7.329   1.00 18.99 ? 265 LEU   A HB2  1 
ATOM   3970 H  HB3  . LEU   A 1 265 ? 5.084   -16.029 7.793   1.00 18.99 ? 265 LEU   A HB3  1 
ATOM   3971 H  HG   . LEU   A 1 265 ? 6.420   -16.395 5.916   1.00 17.12 ? 265 LEU   A HG   1 
ATOM   3972 H  HD11 . LEU   A 1 265 ? 5.671   -17.805 4.222   1.00 21.17 ? 265 LEU   A HD11 1 
ATOM   3973 H  HD12 . LEU   A 1 265 ? 5.986   -18.637 5.537   1.00 21.17 ? 265 LEU   A HD12 1 
ATOM   3974 H  HD13 . LEU   A 1 265 ? 4.483   -18.291 5.157   1.00 21.17 ? 265 LEU   A HD13 1 
ATOM   3975 H  HD21 . LEU   A 1 265 ? 4.899   -15.561 4.326   1.00 23.12 ? 265 LEU   A HD21 1 
ATOM   3976 H  HD22 . LEU   A 1 265 ? 3.718   -15.858 5.346   1.00 23.12 ? 265 LEU   A HD22 1 
ATOM   3977 H  HD23 . LEU   A 1 265 ? 4.819   -14.770 5.702   1.00 23.12 ? 265 LEU   A HD23 1 
ATOM   3978 N  N    . PHE   A 1 266 ? 7.811   -16.577 8.780   1.00 15.90 ? 266 PHE   A N    1 
ATOM   3979 C  CA   . PHE   A 1 266 ? 9.232   -16.242 8.722   1.00 16.21 ? 266 PHE   A CA   1 
ATOM   3980 C  C    . PHE   A 1 266 ? 10.066  -17.380 9.298   1.00 18.02 ? 266 PHE   A C    1 
ATOM   3981 O  O    . PHE   A 1 266 ? 11.073  -17.795 8.708   1.00 18.14 ? 266 PHE   A O    1 
ATOM   3982 C  CB   . PHE   A 1 266 ? 9.449   -14.913 9.466   1.00 15.48 ? 266 PHE   A CB   1 
ATOM   3983 C  CG   . PHE   A 1 266 ? 10.878  -14.452 9.521   1.00 18.00 ? 266 PHE   A CG   1 
ATOM   3984 C  CD1  . PHE   A 1 266 ? 11.507  -13.969 8.388   1.00 19.84 ? 266 PHE   A CD1  1 
ATOM   3985 C  CD2  . PHE   A 1 266 ? 11.570  -14.433 10.718  1.00 18.12 ? 266 PHE   A CD2  1 
ATOM   3986 C  CE1  . PHE   A 1 266 ? 12.815  -13.525 8.438   1.00 18.96 ? 266 PHE   A CE1  1 
ATOM   3987 C  CE2  . PHE   A 1 266 ? 12.875  -13.985 10.772  1.00 20.26 ? 266 PHE   A CE2  1 
ATOM   3988 C  CZ   . PHE   A 1 266 ? 13.496  -13.527 9.634   1.00 18.16 ? 266 PHE   A CZ   1 
ATOM   3989 H  H    . PHE   A 1 266 ? 7.343   -16.049 9.272   1.00 19.10 ? 266 PHE   A H    1 
ATOM   3990 H  HA   . PHE   A 1 266 ? 9.492   -16.116 7.796   1.00 19.47 ? 266 PHE   A HA   1 
ATOM   3991 H  HB2  . PHE   A 1 266 ? 8.934   -14.222 9.021   1.00 18.60 ? 266 PHE   A HB2  1 
ATOM   3992 H  HB3  . PHE   A 1 266 ? 9.138   -15.015 10.379  1.00 18.60 ? 266 PHE   A HB3  1 
ATOM   3993 H  HD1  . PHE   A 1 266 ? 11.053  -13.967 7.577   1.00 23.83 ? 266 PHE   A HD1  1 
ATOM   3994 H  HD2  . PHE   A 1 266 ? 11.158  -14.742 11.492  1.00 21.77 ? 266 PHE   A HD2  1 
ATOM   3995 H  HE1  . PHE   A 1 266 ? 13.231  -13.215 7.666   1.00 22.78 ? 266 PHE   A HE1  1 
ATOM   3996 H  HE2  . PHE   A 1 266 ? 13.334  -13.990 11.581  1.00 24.33 ? 266 PHE   A HE2  1 
ATOM   3997 H  HZ   . PHE   A 1 266 ? 14.376  -13.228 9.671   1.00 21.81 ? 266 PHE   A HZ   1 
ATOM   3998 N  N    . TYR   A 1 267 ? 9.639   -17.920 10.440  1.00 18.03 ? 267 TYR   A N    1 
ATOM   3999 C  CA   . TYR   A 1 267 ? 10.312  -19.067 11.037  1.00 19.60 ? 267 TYR   A CA   1 
ATOM   4000 C  C    . TYR   A 1 267 ? 10.311  -20.256 10.085  1.00 19.13 ? 267 TYR   A C    1 
ATOM   4001 O  O    . TYR   A 1 267 ? 11.344  -20.908 9.886   1.00 21.12 ? 267 TYR   A O    1 
ATOM   4002 C  CB   . TYR   A 1 267 ? 9.612   -19.441 12.341  1.00 17.54 ? 267 TYR   A CB   1 
ATOM   4003 C  CG   . TYR   A 1 267 ? 10.148  -20.676 13.010  1.00 18.90 ? 267 TYR   A CG   1 
ATOM   4004 C  CD1  . TYR   A 1 267 ? 11.271  -20.609 13.816  1.00 19.21 ? 267 TYR   A CD1  1 
ATOM   4005 C  CD2  . TYR   A 1 267 ? 9.540   -21.913 12.833  1.00 21.52 ? 267 TYR   A CD2  1 
ATOM   4006 C  CE1  . TYR   A 1 267 ? 11.769  -21.725 14.438  1.00 22.60 ? 267 TYR   A CE1  1 
ATOM   4007 C  CE2  . TYR   A 1 267 ? 10.041  -23.052 13.460  1.00 23.26 ? 267 TYR   A CE2  1 
ATOM   4008 C  CZ   . TYR   A 1 267 ? 11.162  -22.944 14.259  1.00 23.71 ? 267 TYR   A CZ   1 
ATOM   4009 O  OH   . TYR   A 1 267 ? 11.688  -24.051 14.888  1.00 27.32 ? 267 TYR   A OH   1 
ATOM   4010 H  H    . TYR   A 1 267 ? 8.961   -17.638 10.887  1.00 21.66 ? 267 TYR   A H    1 
ATOM   4011 H  HA   . TYR   A 1 267 ? 11.232  -18.834 11.237  1.00 23.54 ? 267 TYR   A HA   1 
ATOM   4012 H  HB2  . TYR   A 1 267 ? 9.707   -18.705 12.965  1.00 21.07 ? 267 TYR   A HB2  1 
ATOM   4013 H  HB3  . TYR   A 1 267 ? 8.672   -19.592 12.155  1.00 21.07 ? 267 TYR   A HB3  1 
ATOM   4014 H  HD1  . TYR   A 1 267 ? 11.689  -19.789 13.946  1.00 23.07 ? 267 TYR   A HD1  1 
ATOM   4015 H  HD2  . TYR   A 1 267 ? 8.784   -21.980 12.295  1.00 25.85 ? 267 TYR   A HD2  1 
ATOM   4016 H  HE1  . TYR   A 1 267 ? 12.525  -21.658 14.975  1.00 27.14 ? 267 TYR   A HE1  1 
ATOM   4017 H  HE2  . TYR   A 1 267 ? 9.629   -23.876 13.337  1.00 27.94 ? 267 TYR   A HE2  1 
ATOM   4018 H  HH   . TYR   A 1 267 ? 11.232  -24.731 14.702  1.00 32.80 ? 267 TYR   A HH   1 
ATOM   4019 N  N    . ILE   A 1 268 ? 9.161   -20.552 9.479   1.00 17.38 ? 268 ILE   A N    1 
ATOM   4020 C  CA   . ILE   A 1 268 ? 9.076   -21.693 8.573   1.00 19.18 ? 268 ILE   A CA   1 
ATOM   4021 C  C    . ILE   A 1 268 ? 10.013  -21.497 7.387   1.00 20.33 ? 268 ILE   A C    1 
ATOM   4022 O  O    . ILE   A 1 268 ? 10.756  -22.407 7.006   1.00 21.42 ? 268 ILE   A O    1 
ATOM   4023 C  CB   . ILE   A 1 268 ? 7.624   -21.919 8.114   1.00 19.20 ? 268 ILE   A CB   1 
ATOM   4024 C  CG1  . ILE   A 1 268 ? 6.773   -22.443 9.273   1.00 21.09 ? 268 ILE   A CG1  1 
ATOM   4025 C  CG2  . ILE   A 1 268 ? 7.569   -22.895 6.949   1.00 22.40 ? 268 ILE   A CG2  1 
ATOM   4026 C  CD1  . ILE   A 1 268 ? 5.282   -22.258 9.083   1.00 21.00 ? 268 ILE   A CD1  1 
ATOM   4027 H  H    . ILE   A 1 268 ? 8.427   -20.114 9.574   1.00 20.88 ? 268 ILE   A H    1 
ATOM   4028 H  HA   . ILE   A 1 268 ? 9.363   -22.489 9.047   1.00 23.03 ? 268 ILE   A HA   1 
ATOM   4029 H  HB   . ILE   A 1 268 ? 7.258   -21.070 7.822   1.00 23.05 ? 268 ILE   A HB   1 
ATOM   4030 H  HG12 . ILE   A 1 268 ? 6.941   -23.393 9.378   1.00 25.32 ? 268 ILE   A HG12 1 
ATOM   4031 H  HG13 . ILE   A 1 268 ? 7.027   -21.974 10.083  1.00 25.32 ? 268 ILE   A HG13 1 
ATOM   4032 H  HG21 . ILE   A 1 268 ? 6.662   -23.227 6.858   1.00 26.89 ? 268 ILE   A HG21 1 
ATOM   4033 H  HG22 . ILE   A 1 268 ? 7.834   -22.437 6.136   1.00 26.89 ? 268 ILE   A HG22 1 
ATOM   4034 H  HG23 . ILE   A 1 268 ? 8.172   -23.633 7.128   1.00 26.89 ? 268 ILE   A HG23 1 
ATOM   4035 H  HD11 . ILE   A 1 268 ? 4.823   -22.558 9.883   1.00 25.21 ? 268 ILE   A HD11 1 
ATOM   4036 H  HD12 . ILE   A 1 268 ? 5.098   -21.318 8.929   1.00 25.21 ? 268 ILE   A HD12 1 
ATOM   4037 H  HD13 . ILE   A 1 268 ? 4.992   -22.781 8.319   1.00 25.21 ? 268 ILE   A HD13 1 
ATOM   4038 N  N    . LEU   A 1 269 ? 9.995   -20.307 6.786   1.00 18.78 ? 269 LEU   A N    1 
ATOM   4039 C  CA   . LEU   A 1 269 ? 10.792  -20.079 5.584   1.00 18.66 ? 269 LEU   A CA   1 
ATOM   4040 C  C    . LEU   A 1 269 ? 12.281  -20.176 5.890   1.00 20.10 ? 269 LEU   A C    1 
ATOM   4041 O  O    . LEU   A 1 269 ? 13.030  -20.842 5.161   1.00 22.14 ? 269 LEU   A O    1 
ATOM   4042 C  CB   . LEU   A 1 269 ? 10.452  -18.717 4.982   1.00 17.93 ? 269 LEU   A CB   1 
ATOM   4043 C  CG   . LEU   A 1 269 ? 11.288  -18.308 3.769   1.00 18.38 ? 269 LEU   A CG   1 
ATOM   4044 C  CD1  . LEU   A 1 269 ? 11.105  -19.323 2.656   1.00 22.70 ? 269 LEU   A CD1  1 
ATOM   4045 C  CD2  . LEU   A 1 269 ? 10.874  -16.927 3.309   1.00 22.30 ? 269 LEU   A CD2  1 
ATOM   4046 H  H    . LEU   A 1 269 ? 9.538   -19.628 7.049   1.00 22.55 ? 269 LEU   A H    1 
ATOM   4047 H  HA   . LEU   A 1 269 ? 10.575  -20.761 4.930   1.00 22.41 ? 269 LEU   A HA   1 
ATOM   4048 H  HB2  . LEU   A 1 269 ? 9.523   -18.727 4.705   1.00 21.54 ? 269 LEU   A HB2  1 
ATOM   4049 H  HB3  . LEU   A 1 269 ? 10.579  -18.039 5.665   1.00 21.54 ? 269 LEU   A HB3  1 
ATOM   4050 H  HG   . LEU   A 1 269 ? 12.227  -18.280 4.010   1.00 22.07 ? 269 LEU   A HG   1 
ATOM   4051 H  HD11 . LEU   A 1 269 ? 11.524  -18.984 1.850   1.00 27.26 ? 269 LEU   A HD11 1 
ATOM   4052 H  HD12 . LEU   A 1 269 ? 11.521  -20.159 2.918   1.00 27.26 ? 269 LEU   A HD12 1 
ATOM   4053 H  HD13 . LEU   A 1 269 ? 10.156  -19.457 2.504   1.00 27.26 ? 269 LEU   A HD13 1 
ATOM   4054 H  HD21 . LEU   A 1 269 ? 11.410  -16.677 2.540   1.00 26.78 ? 269 LEU   A HD21 1 
ATOM   4055 H  HD22 . LEU   A 1 269 ? 9.935   -16.944 3.067   1.00 26.78 ? 269 LEU   A HD22 1 
ATOM   4056 H  HD23 . LEU   A 1 269 ? 11.018  -16.297 4.032   1.00 26.78 ? 269 LEU   A HD23 1 
ATOM   4057 N  N    . ALA   A 1 270 ? 12.718  -19.555 6.989   1.00 20.46 ? 270 ALA   A N    1 
ATOM   4058 C  CA   . ALA   A 1 270 ? 14.126  -19.583 7.366   1.00 17.78 ? 270 ALA   A CA   1 
ATOM   4059 C  C    . ALA   A 1 270 ? 14.636  -20.990 7.630   1.00 22.81 ? 270 ALA   A C    1 
ATOM   4060 O  O    . ALA   A 1 270 ? 15.850  -21.215 7.581   1.00 25.75 ? 270 ALA   A O    1 
ATOM   4061 C  CB   . ALA   A 1 270 ? 14.342  -18.721 8.610   1.00 20.70 ? 270 ALA   A CB   1 
ATOM   4062 H  H    . ALA   A 1 270 ? 12.217  -19.112 7.530   1.00 24.57 ? 270 ALA   A H    1 
ATOM   4063 H  HA   . ALA   A 1 270 ? 14.653  -19.205 6.644   1.00 21.35 ? 270 ALA   A HA   1 
ATOM   4064 H  HB1  . ALA   A 1 270 ? 15.281  -18.746 8.852   1.00 24.85 ? 270 ALA   A HB1  1 
ATOM   4065 H  HB2  . ALA   A 1 270 ? 14.076  -17.810 8.412   1.00 24.85 ? 270 ALA   A HB2  1 
ATOM   4066 H  HB3  . ALA   A 1 270 ? 13.803  -19.074 9.335   1.00 24.85 ? 270 ALA   A HB3  1 
ATOM   4067 N  N    . ASN   A 1 271 ? 13.746  -21.929 7.924   1.00 22.33 ? 271 ASN   A N    1 
ATOM   4068 C  CA   . ASN   A 1 271 ? 14.095  -23.307 8.236   1.00 25.14 ? 271 ASN   A CA   1 
ATOM   4069 C  C    . ASN   A 1 271 ? 13.825  -24.282 7.104   1.00 29.60 ? 271 ASN   A C    1 
ATOM   4070 O  O    . ASN   A 1 271 ? 13.928  -25.496 7.312   1.00 31.94 ? 271 ASN   A O    1 
ATOM   4071 C  CB   . ASN   A 1 271 ? 13.351  -23.736 9.493   1.00 25.94 ? 271 ASN   A CB   1 
ATOM   4072 C  CG   . ASN   A 1 271 ? 13.982  -23.219 10.764  1.00 28.47 ? 271 ASN   A CG   1 
ATOM   4073 O  OD1  . ASN   A 1 271 ? 15.038  -23.707 11.179  1.00 31.28 ? 271 ASN   A OD1  1 
ATOM   4074 N  ND2  . ASN   A 1 271 ? 13.405  -22.171 11.340  1.00 25.39 ? 271 ASN   A ND2  1 
ATOM   4075 H  H    . ASN   A 1 271 ? 12.899  -21.785 7.950   1.00 26.81 ? 271 ASN   A H    1 
ATOM   4076 H  HA   . ASN   A 1 271 ? 15.044  -23.348 8.433   1.00 30.19 ? 271 ASN   A HA   1 
ATOM   4077 H  HB2  . ASN   A 1 271 ? 12.443  -23.397 9.452   1.00 31.15 ? 271 ASN   A HB2  1 
ATOM   4078 H  HB3  . ASN   A 1 271 ? 13.340  -24.705 9.539   1.00 31.15 ? 271 ASN   A HB3  1 
ATOM   4079 H  HD21 . ASN   A 1 271 ? 13.737  -21.840 12.061  1.00 30.49 ? 271 ASN   A HD21 1 
ATOM   4080 H  HD22 . ASN   A 1 271 ? 12.679  -21.847 11.013  1.00 30.49 ? 271 ASN   A HD22 1 
ATOM   4081 N  N    . GLN   A 1 272 ? 13.496  -23.794 5.914   1.00 23.92 ? 272 GLN   A N    1 
ATOM   4082 C  CA   . GLN   A 1 272 ? 13.450  -24.677 4.760   1.00 24.57 ? 272 GLN   A CA   1 
ATOM   4083 C  C    . GLN   A 1 272 ? 14.877  -25.111 4.418   1.00 27.99 ? 272 GLN   A C    1 
ATOM   4084 O  O    . GLN   A 1 272 ? 15.842  -24.414 4.750   1.00 29.44 ? 272 GLN   A O    1 
ATOM   4085 C  CB   . GLN   A 1 272 ? 12.809  -23.973 3.566   1.00 25.61 ? 272 GLN   A CB   1 
ATOM   4086 C  CG   . GLN   A 1 272 ? 11.329  -23.638 3.763   1.00 24.05 ? 272 GLN   A CG   1 
ATOM   4087 C  CD   . GLN   A 1 272 ? 10.460  -24.809 4.189   1.00 29.47 ? 272 GLN   A CD   1 
ATOM   4088 O  OE1  . GLN   A 1 272 ? 10.377  -25.829 3.497   1.00 33.57 ? 272 GLN   A OE1  1 
ATOM   4089 N  NE2  . GLN   A 1 272 ? 9.857   -24.694 5.367   1.00 38.01 ? 272 GLN   A NE2  1 
ATOM   4090 H  H    . GLN   A 1 272 ? 13.299  -22.973 5.750   1.00 28.73 ? 272 GLN   A H    1 
ATOM   4091 H  HA   . GLN   A 1 272 ? 12.928  -25.463 4.980   1.00 29.51 ? 272 GLN   A HA   1 
ATOM   4092 H  HB2  . GLN   A 1 272 ? 13.282  -23.142 3.404   1.00 30.75 ? 272 GLN   A HB2  1 
ATOM   4093 H  HB3  . GLN   A 1 272 ? 12.881  -24.549 2.789   1.00 30.75 ? 272 GLN   A HB3  1 
ATOM   4094 H  HG2  . GLN   A 1 272 ? 11.256  -22.954 4.447   1.00 28.88 ? 272 GLN   A HG2  1 
ATOM   4095 H  HG3  . GLN   A 1 272 ? 10.975  -23.300 2.926   1.00 28.88 ? 272 GLN   A HG3  1 
ATOM   4096 H  HE21 . GLN   A 1 272 ? 9.946   -23.973 5.827   1.00 45.64 ? 272 GLN   A HE21 1 
ATOM   4097 H  HE22 . GLN   A 1 272 ? 9.357   -25.331 5.658   1.00 45.64 ? 272 GLN   A HE22 1 
ATOM   4098 N  N    . PRO   A 1 273 ? 15.063  -26.268 3.749   1.00 29.14 ? 273 PRO   A N    1 
ATOM   4099 C  CA   . PRO   A 1 273 ? 16.422  -26.783 3.432   1.00 30.49 ? 273 PRO   A CA   1 
ATOM   4100 C  C    . PRO   A 1 273 ? 17.198  -25.729 2.656   1.00 25.64 ? 273 PRO   A C    1 
ATOM   4101 O  O    . PRO   A 1 273 ? 16.606  -25.117 1.745   1.00 37.13 ? 273 PRO   A O    1 
ATOM   4102 C  CB   . PRO   A 1 273 ? 16.165  -28.066 2.643   1.00 31.72 ? 273 PRO   A CB   1 
ATOM   4103 C  CG   . PRO   A 1 273 ? 14.750  -28.466 3.012   1.00 32.28 ? 273 PRO   A CG   1 
ATOM   4104 C  CD   . PRO   A 1 273 ? 14.014  -27.184 3.201   1.00 29.82 ? 273 PRO   A CD   1 
ATOM   4105 H  HA   . PRO   A 1 273 ? 16.900  -26.998 4.248   1.00 36.61 ? 273 PRO   A HA   1 
ATOM   4106 H  HB2  . PRO   A 1 273 ? 16.236  -27.887 1.692   1.00 38.08 ? 273 PRO   A HB2  1 
ATOM   4107 H  HB3  . PRO   A 1 273 ? 16.798  -28.750 2.913   1.00 38.08 ? 273 PRO   A HB3  1 
ATOM   4108 H  HG2  . PRO   A 1 273 ? 14.358  -28.982 2.290   1.00 38.75 ? 273 PRO   A HG2  1 
ATOM   4109 H  HG3  . PRO   A 1 273 ? 14.760  -28.979 3.835   1.00 38.75 ? 273 PRO   A HG3  1 
ATOM   4110 H  HD2  . PRO   A 1 273 ? 13.686  -26.853 2.350   1.00 35.80 ? 273 PRO   A HD2  1 
ATOM   4111 H  HD3  . PRO   A 1 273 ? 13.294  -27.303 3.840   1.00 35.80 ? 273 PRO   A HD3  1 
ATOM   4112 N  N    . ASN   A 1 274 ? 18.438  -25.446 3.056   1.00 33.20 ? 274 ASN   A N    1 
ATOM   4113 C  CA   . ASN   A 1 274 ? 19.323  -24.496 2.324   1.00 49.63 ? 274 ASN   A CA   1 
ATOM   4114 C  C    . ASN   A 1 274 ? 19.030  -23.041 2.699   1.00 43.09 ? 274 ASN   A C    1 
ATOM   4115 O  O    . ASN   A 1 274 ? 19.833  -22.169 2.313   1.00 46.03 ? 274 ASN   A O    1 
ATOM   4116 C  CB   . ASN   A 1 274 ? 19.199  -24.614 0.812   1.00 54.70 ? 274 ASN   A CB   1 
ATOM   4117 C  CG   . ASN   A 1 274 ? 20.472  -24.170 0.145   1.00 63.95 ? 274 ASN   A CG   1 
ATOM   4118 O  OD1  . ASN   A 1 274 ? 20.571  -23.015 -0.278  1.00 71.29 ? 274 ASN   A OD1  1 
ATOM   4119 N  ND2  . ASN   A 1 274 ? 21.470  -25.042 0.117   1.00 63.21 ? 274 ASN   A ND2  1 
ATOM   4120 H  H    . ASN   A 1 274 ? 18.805  -25.788 3.754   1.00 39.86 ? 274 ASN   A H    1 
ATOM   4121 H  HA   . ASN   A 1 274 ? 20.245  -24.684 2.561   1.00 59.58 ? 274 ASN   A HA   1 
ATOM   4122 H  HB2  . ASN   A 1 274 ? 19.013  -25.522 0.619   1.00 65.66 ? 274 ASN   A HB2  1 
ATOM   4123 H  HB3  . ASN   A 1 274 ? 18.476  -24.046 0.502   1.00 65.66 ? 274 ASN   A HB3  1 
ATOM   4124 H  HD21 . ASN   A 1 274 ? 22.218  -24.827 -0.249  1.00 75.87 ? 274 ASN   A HD21 1 
ATOM   4125 H  HD22 . ASN   A 1 274 ? 21.359  -25.833 0.437   1.00 75.87 ? 274 ASN   A HD22 1 
ATOM   4126 N  N    . TRP   A 1 275 ? 17.936  -22.780 3.412   1.00 27.86 ? 275 TRP   A N    1 
ATOM   4127 C  CA   . TRP   A 1 275 ? 17.546  -21.396 3.767   1.00 27.05 ? 275 TRP   A CA   1 
ATOM   4128 C  C    . TRP   A 1 275 ? 18.112  -21.035 5.130   1.00 27.22 ? 275 TRP   A C    1 
ATOM   4129 O  O    . TRP   A 1 275 ? 18.436  -21.964 5.894   1.00 28.66 ? 275 TRP   A O    1 
ATOM   4130 C  CB   . TRP   A 1 275 ? 16.017  -21.252 3.773   1.00 26.07 ? 275 TRP   A CB   1 
ATOM   4131 C  CG   . TRP   A 1 275 ? 15.404  -21.031 2.415   1.00 23.38 ? 275 TRP   A CG   1 
ATOM   4132 C  CD1  . TRP   A 1 275 ? 15.193  -21.969 1.448   1.00 28.09 ? 275 TRP   A CD1  1 
ATOM   4133 C  CD2  . TRP   A 1 275 ? 14.884  -19.790 1.889   1.00 21.79 ? 275 TRP   A CD2  1 
ATOM   4134 N  NE1  . TRP   A 1 275 ? 14.605  -21.398 0.352   1.00 25.38 ? 275 TRP   A NE1  1 
ATOM   4135 C  CE2  . TRP   A 1 275 ? 14.397  -20.067 0.593   1.00 21.47 ? 275 TRP   A CE2  1 
ATOM   4136 C  CE3  . TRP   A 1 275 ? 14.788  -18.483 2.378   1.00 22.84 ? 275 TRP   A CE3  1 
ATOM   4137 C  CZ2  . TRP   A 1 275 ? 13.826  -19.085 -0.212  1.00 23.14 ? 275 TRP   A CZ2  1 
ATOM   4138 C  CZ3  . TRP   A 1 275 ? 14.221  -17.514 1.581   1.00 23.21 ? 275 TRP   A CZ3  1 
ATOM   4139 C  CH2  . TRP   A 1 275 ? 13.747  -17.812 0.304   1.00 24.59 ? 275 TRP   A CH2  1 
ATOM   4140 H  H    . TRP   A 1 275 ? 17.395  -23.379 3.708   1.00 33.45 ? 275 TRP   A H    1 
ATOM   4141 H  HA   . TRP   A 1 275 ? 17.909  -20.780 3.111   1.00 32.48 ? 275 TRP   A HA   1 
ATOM   4142 H  HB2  . TRP   A 1 275 ? 15.630  -22.061 4.142   1.00 31.30 ? 275 TRP   A HB2  1 
ATOM   4143 H  HB3  . TRP   A 1 275 ? 15.780  -20.494 4.329   1.00 31.30 ? 275 TRP   A HB3  1 
ATOM   4144 H  HD1  . TRP   A 1 275 ? 15.434  -22.865 1.516   1.00 33.72 ? 275 TRP   A HD1  1 
ATOM   4145 H  HE1  . TRP   A 1 275 ? 14.390  -21.813 -0.370  1.00 30.47 ? 275 TRP   A HE1  1 
ATOM   4146 H  HE3  . TRP   A 1 275 ? 15.100  -18.272 3.228   1.00 27.43 ? 275 TRP   A HE3  1 
ATOM   4147 H  HZ2  . TRP   A 1 275 ? 13.509  -19.282 -1.064  1.00 27.79 ? 275 TRP   A HZ2  1 
ATOM   4148 H  HZ3  . TRP   A 1 275 ? 14.157  -16.643 1.899   1.00 27.87 ? 275 TRP   A HZ3  1 
ATOM   4149 H  HH2  . TRP   A 1 275 ? 13.373  -17.135 -0.212  1.00 29.53 ? 275 TRP   A HH2  1 
ATOM   4150 N  N    . ASN   A 1 276 ? 18.277  -19.744 5.414   1.00 24.30 ? 276 ASN   A N    1 
ATOM   4151 C  CA   . ASN   A 1 276 ? 18.659  -19.277 6.730   1.00 22.33 ? 276 ASN   A CA   1 
ATOM   4152 C  C    . ASN   A 1 276 ? 17.873  -18.004 7.012   1.00 20.69 ? 276 ASN   A C    1 
ATOM   4153 O  O    . ASN   A 1 276 ? 17.080  -17.542 6.183   1.00 20.43 ? 276 ASN   A O    1 
ATOM   4154 C  CB   . ASN   A 1 276 ? 20.173  -19.060 6.844   1.00 22.92 ? 276 ASN   A CB   1 
ATOM   4155 C  CG   . ASN   A 1 276 ? 20.737  -18.126 5.785   1.00 26.87 ? 276 ASN   A CG   1 
ATOM   4156 O  OD1  . ASN   A 1 276 ? 20.080  -17.189 5.328   1.00 26.89 ? 276 ASN   A OD1  1 
ATOM   4157 N  ND2  . ASN   A 1 276 ? 21.963  -18.406 5.366   1.00 33.99 ? 276 ASN   A ND2  1 
ATOM   4158 H  H    . ASN   A 1 276 ? 18.169  -19.110 4.843   1.00 29.17 ? 276 ASN   A H    1 
ATOM   4159 H  HA   . ASN   A 1 276 ? 18.401  -19.941 7.389   1.00 26.82 ? 276 ASN   A HA   1 
ATOM   4160 H  HB2  . ASN   A 1 276 ? 20.371  -18.678 7.713   1.00 27.53 ? 276 ASN   A HB2  1 
ATOM   4161 H  HB3  . ASN   A 1 276 ? 20.619  -19.916 6.752   1.00 27.53 ? 276 ASN   A HB3  1 
ATOM   4162 H  HD21 . ASN   A 1 276 ? 22.335  -17.915 4.766   1.00 40.80 ? 276 ASN   A HD21 1 
ATOM   4163 H  HD22 . ASN   A 1 276 ? 22.391  -19.071 5.703   1.00 40.80 ? 276 ASN   A HD22 1 
ATOM   4164 N  N    . LEU   A 1 277 ? 18.106  -17.451 8.200   1.00 23.15 ? 277 LEU   A N    1 
ATOM   4165 C  CA   . LEU   A 1 277 ? 17.414  -16.237 8.620   1.00 22.46 ? 277 LEU   A CA   1 
ATOM   4166 C  C    . LEU   A 1 277 ? 17.667  -15.097 7.642   1.00 21.49 ? 277 LEU   A C    1 
ATOM   4167 O  O    . LEU   A 1 277 ? 16.745  -14.347 7.292   1.00 19.15 ? 277 LEU   A O    1 
ATOM   4168 C  CB   . LEU   A 1 277 ? 17.883  -15.837 10.017  1.00 21.28 ? 277 LEU   A CB   1 
ATOM   4169 C  CG   . LEU   A 1 277 ? 17.220  -14.567 10.550  1.00 25.39 ? 277 LEU   A CG   1 
ATOM   4170 C  CD1  . LEU   A 1 277 ? 16.938  -14.675 12.045  1.00 36.48 ? 277 LEU   A CD1  1 
ATOM   4171 C  CD2  . LEU   A 1 277 ? 18.045  -13.323 10.253  1.00 31.17 ? 277 LEU   A CD2  1 
ATOM   4172 H  H    . LEU   A 1 277 ? 18.660  -17.760 8.781   1.00 27.80 ? 277 LEU   A H    1 
ATOM   4173 H  HA   . LEU   A 1 277 ? 16.459  -16.405 8.654   1.00 26.97 ? 277 LEU   A HA   1 
ATOM   4174 H  HB2  . LEU   A 1 277 ? 17.679  -16.558 10.633  1.00 25.56 ? 277 LEU   A HB2  1 
ATOM   4175 H  HB3  . LEU   A 1 277 ? 18.841  -15.686 9.994   1.00 25.56 ? 277 LEU   A HB3  1 
ATOM   4176 H  HG   . LEU   A 1 277 ? 16.366  -14.460 10.103  1.00 30.48 ? 277 LEU   A HG   1 
ATOM   4177 H  HD11 . LEU   A 1 277 ? 16.773  -13.786 12.393  1.00 43.79 ? 277 LEU   A HD11 1 
ATOM   4178 H  HD12 . LEU   A 1 277 ? 16.159  -15.237 12.182  1.00 43.79 ? 277 LEU   A HD12 1 
ATOM   4179 H  HD13 . LEU   A 1 277 ? 17.711  -15.063 12.485  1.00 43.79 ? 277 LEU   A HD13 1 
ATOM   4180 H  HD21 . LEU   A 1 277 ? 17.444  -12.574 10.113  1.00 37.42 ? 277 LEU   A HD21 1 
ATOM   4181 H  HD22 . LEU   A 1 277 ? 18.624  -13.144 11.011  1.00 37.42 ? 277 LEU   A HD22 1 
ATOM   4182 H  HD23 . LEU   A 1 277 ? 18.580  -13.469 9.459   1.00 37.42 ? 277 LEU   A HD23 1 
ATOM   4183 N  N    . ARG   A 1 278 ? 18.926  -14.916 7.231   1.00 20.14 ? 278 ARG   A N    1 
ATOM   4184 C  CA   . ARG   A 1 278 ? 19.256  -13.793 6.358   1.00 23.08 ? 278 ARG   A CA   1 
ATOM   4185 C  C    . ARG   A 1 278 ? 18.512  -13.881 5.037   1.00 20.86 ? 278 ARG   A C    1 
ATOM   4186 O  O    . ARG   A 1 278 ? 17.992  -12.877 4.537   1.00 21.54 ? 278 ARG   A O    1 
ATOM   4187 C  CB   . ARG   A 1 278 ? 20.765  -13.712 6.120   1.00 24.20 ? 278 ARG   A CB   1 
ATOM   4188 C  CG   . ARG   A 1 278 ? 21.117  -12.562 5.190   1.00 29.29 ? 278 ARG   A CG   1 
ATOM   4189 C  CD   . ARG   A 1 278 ? 22.592  -12.253 5.118   1.00 44.94 ? 278 ARG   A CD   1 
ATOM   4190 N  NE   . ARG   A 1 278 ? 22.803  -11.115 4.232   1.00 43.44 ? 278 ARG   A NE   1 
ATOM   4191 C  CZ   . ARG   A 1 278 ? 23.986  -10.592 3.942   1.00 49.09 ? 278 ARG   A CZ   1 
ATOM   4192 N  NH1  . ARG   A 1 278 ? 25.076  -10.938 4.605   1.00 50.15 ? 278 ARG   A NH1  1 
ATOM   4193 N  NH2  . ARG   A 1 278 ? 24.079  -9.702  2.959   1.00 57.78 ? 278 ARG   A NH2  1 
ATOM   4194 H  H    . ARG   A 1 278 ? 19.592  -15.419 7.440   1.00 24.19 ? 278 ARG   A H    1 
ATOM   4195 H  HA   . ARG   A 1 278 ? 18.983  -12.971 6.795   1.00 27.71 ? 278 ARG   A HA   1 
ATOM   4196 H  HB2  . ARG   A 1 278 ? 21.216  -13.568 6.967   1.00 29.06 ? 278 ARG   A HB2  1 
ATOM   4197 H  HB3  . ARG   A 1 278 ? 21.070  -14.538 5.712   1.00 29.06 ? 278 ARG   A HB3  1 
ATOM   4198 H  HG2  . ARG   A 1 278 ? 20.823  -12.783 4.292   1.00 35.16 ? 278 ARG   A HG2  1 
ATOM   4199 H  HG3  . ARG   A 1 278 ? 20.662  -11.762 5.497   1.00 35.16 ? 278 ARG   A HG3  1 
ATOM   4200 H  HD2  . ARG   A 1 278 ? 22.922  -12.025 6.001   1.00 53.94 ? 278 ARG   A HD2  1 
ATOM   4201 H  HD3  . ARG   A 1 278 ? 23.069  -13.018 4.761   1.00 53.94 ? 278 ARG   A HD3  1 
ATOM   4202 H  HE   . ARG   A 1 278 ? 22.109  -10.757 3.871   1.00 52.14 ? 278 ARG   A HE   1 
ATOM   4203 H  HH11 . ARG   A 1 278 ? 25.031  -11.519 5.237   1.00 60.20 ? 278 ARG   A HH11 1 
ATOM   4204 H  HH12 . ARG   A 1 278 ? 25.833  -10.583 4.402   1.00 60.20 ? 278 ARG   A HH12 1 
ATOM   4205 H  HH21 . ARG   A 1 278 ? 23.375  -9.465  2.525   1.00 69.36 ? 278 ARG   A HH21 1 
ATOM   4206 H  HH22 . ARG   A 1 278 ? 24.839  -9.347  2.771   1.00 69.36 ? 278 ARG   A HH22 1 
ATOM   4207 N  N    . MET   A 1 279 ? 18.446  -15.072 4.448   1.00 21.79 ? 279 MET   A N    1 
ATOM   4208 C  CA   A MET   A 1 279 ? 17.745  -15.216 3.177   0.16 24.19 ? 279 MET   A CA   1 
ATOM   4209 C  CA   B MET   A 1 279 ? 17.744  -15.216 3.179   0.84 24.24 ? 279 MET   A CA   1 
ATOM   4210 C  C    . MET   A 1 279 ? 16.260  -14.926 3.336   1.00 21.41 ? 279 MET   A C    1 
ATOM   4211 O  O    . MET   A 1 279 ? 15.659  -14.252 2.493   1.00 20.80 ? 279 MET   A O    1 
ATOM   4212 C  CB   A MET   A 1 279 ? 17.956  -16.618 2.612   0.16 24.24 ? 279 MET   A CB   1 
ATOM   4213 C  CB   B MET   A 1 279 ? 17.966  -16.621 2.647   0.84 24.15 ? 279 MET   A CB   1 
ATOM   4214 C  CG   A MET   A 1 279 ? 19.168  -16.721 1.721   0.16 28.19 ? 279 MET   A CG   1 
ATOM   4215 C  CG   B MET   A 1 279 ? 19.341  -16.751 2.088   0.84 27.34 ? 279 MET   A CG   1 
ATOM   4216 S  SD   A MET   A 1 279 ? 19.429  -18.401 1.151   0.16 34.69 ? 279 MET   A SD   1 
ATOM   4217 S  SD   B MET   A 1 279 ? 19.589  -18.383 1.432   0.84 36.18 ? 279 MET   A SD   1 
ATOM   4218 C  CE   A MET   A 1 279 ? 20.324  -19.069 2.548   0.16 31.15 ? 279 MET   A CE   1 
ATOM   4219 C  CE   B MET   A 1 279 ? 18.340  -18.355 0.148   0.84 34.98 ? 279 MET   A CE   1 
ATOM   4220 H  H    A MET   A 1 279 ? 18.791  -15.797 4.756   0.16 26.17 ? 279 MET   A H    1 
ATOM   4221 H  H    B MET   A 1 279 ? 18.792  -15.797 4.755   0.84 26.17 ? 279 MET   A H    1 
ATOM   4222 H  HA   A MET   A 1 279 ? 18.119  -14.584 2.543   0.16 29.05 ? 279 MET   A HA   1 
ATOM   4223 H  HA   B MET   A 1 279 ? 18.120  -14.591 2.539   0.84 29.11 ? 279 MET   A HA   1 
ATOM   4224 H  HB2  A MET   A 1 279 ? 18.071  -17.240 3.347   0.16 29.10 ? 279 MET   A HB2  1 
ATOM   4225 H  HB2  B MET   A 1 279 ? 17.866  -17.260 3.370   0.84 29.00 ? 279 MET   A HB2  1 
ATOM   4226 H  HB3  A MET   A 1 279 ? 17.178  -16.866 2.088   0.16 29.10 ? 279 MET   A HB3  1 
ATOM   4227 H  HB3  B MET   A 1 279 ? 17.320  -16.797 1.947   0.84 29.00 ? 279 MET   A HB3  1 
ATOM   4228 H  HG2  A MET   A 1 279 ? 19.043  -16.153 0.945   0.16 33.85 ? 279 MET   A HG2  1 
ATOM   4229 H  HG2  B MET   A 1 279 ? 19.461  -16.110 1.370   0.84 32.83 ? 279 MET   A HG2  1 
ATOM   4230 H  HG3  A MET   A 1 279 ? 19.954  -16.443 2.217   0.16 33.85 ? 279 MET   A HG3  1 
ATOM   4231 H  HG3  B MET   A 1 279 ? 19.992  -16.600 2.791   0.84 32.83 ? 279 MET   A HG3  1 
ATOM   4232 H  HE1  A MET   A 1 279 ? 20.711  -19.921 2.297   0.16 37.39 ? 279 MET   A HE1  1 
ATOM   4233 H  HE1  B MET   A 1 279 ? 18.585  -18.991 -0.542  0.84 42.00 ? 279 MET   A HE1  1 
ATOM   4234 H  HE2  A MET   A 1 279 ? 21.026  -18.448 2.797   0.16 37.39 ? 279 MET   A HE2  1 
ATOM   4235 H  HE2  B MET   A 1 279 ? 17.483  -18.597 0.533   0.84 42.00 ? 279 MET   A HE2  1 
ATOM   4236 H  HE3  A MET   A 1 279 ? 19.710  -19.188 3.289   0.16 37.39 ? 279 MET   A HE3  1 
ATOM   4237 H  HE3  B MET   A 1 279 ? 18.296  -17.462 -0.229  0.84 42.00 ? 279 MET   A HE3  1 
ATOM   4238 N  N    . ALA   A 1 280 ? 15.653  -15.434 4.406   1.00 20.32 ? 280 ALA   A N    1 
ATOM   4239 C  CA   . ALA   A 1 280 ? 14.244  -15.155 4.655   1.00 20.32 ? 280 ALA   A CA   1 
ATOM   4240 C  C    . ALA   A 1 280 ? 14.015  -13.661 4.841   1.00 19.36 ? 280 ALA   A C    1 
ATOM   4241 O  O    . ALA   A 1 280 ? 13.072  -13.090 4.275   1.00 19.23 ? 280 ALA   A O    1 
ATOM   4242 C  CB   . ALA   A 1 280 ? 13.768  -15.931 5.883   1.00 21.36 ? 280 ALA   A CB   1 
ATOM   4243 H  H    . ALA   A 1 280 ? 16.029  -15.936 4.994   1.00 24.40 ? 280 ALA   A H    1 
ATOM   4244 H  HA   . ALA   A 1 280 ? 13.722  -15.448 3.892   1.00 24.40 ? 280 ALA   A HA   1 
ATOM   4245 H  HB1  . ALA   A 1 280 ? 12.830  -15.735 6.036   1.00 25.65 ? 280 ALA   A HB1  1 
ATOM   4246 H  HB2  . ALA   A 1 280 ? 13.886  -16.880 5.722   1.00 25.65 ? 280 ALA   A HB2  1 
ATOM   4247 H  HB3  . ALA   A 1 280 ? 14.293  -15.658 6.652   1.00 25.65 ? 280 ALA   A HB3  1 
ATOM   4248 N  N    . PHE   A 1 281 ? 14.870  -13.008 5.626   1.00 17.72 ? 281 PHE   A N    1 
ATOM   4249 C  CA   . PHE   A 1 281 ? 14.712  -11.576 5.852   1.00 18.61 ? 281 PHE   A CA   1 
ATOM   4250 C  C    . PHE   A 1 281 ? 14.934  -10.791 4.565   1.00 18.13 ? 281 PHE   A C    1 
ATOM   4251 O  O    . PHE   A 1 281 ? 14.252  -9.788  4.334   1.00 18.97 ? 281 PHE   A O    1 
ATOM   4252 C  CB   . PHE   A 1 281 ? 15.647  -11.104 6.974   1.00 19.50 ? 281 PHE   A CB   1 
ATOM   4253 C  CG   . PHE   A 1 281 ? 15.271  -9.762  7.562   1.00 16.78 ? 281 PHE   A CG   1 
ATOM   4254 C  CD1  . PHE   A 1 281 ? 13.999  -9.542  8.077   1.00 18.75 ? 281 PHE   A CD1  1 
ATOM   4255 C  CD2  . PHE   A 1 281 ? 16.193  -8.730  7.620   1.00 19.15 ? 281 PHE   A CD2  1 
ATOM   4256 C  CE1  . PHE   A 1 281 ? 13.648  -8.308  8.613   1.00 20.03 ? 281 PHE   A CE1  1 
ATOM   4257 C  CE2  . PHE   A 1 281 ? 15.853  -7.500  8.167   1.00 18.46 ? 281 PHE   A CE2  1 
ATOM   4258 C  CZ   . PHE   A 1 281 ? 14.574  -7.288  8.655   1.00 18.05 ? 281 PHE   A CZ   1 
ATOM   4259 H  H    . PHE   A 1 281 ? 15.539  -13.365 6.032   1.00 21.29 ? 281 PHE   A H    1 
ATOM   4260 H  HA   . PHE   A 1 281 ? 13.800  -11.413 6.137   1.00 22.36 ? 281 PHE   A HA   1 
ATOM   4261 H  HB2  . PHE   A 1 281 ? 15.629  -11.757 7.691   1.00 23.42 ? 281 PHE   A HB2  1 
ATOM   4262 H  HB3  . PHE   A 1 281 ? 16.547  -11.030 6.620   1.00 23.42 ? 281 PHE   A HB3  1 
ATOM   4263 H  HD1  . PHE   A 1 281 ? 13.367  -10.223 8.043   1.00 22.52 ? 281 PHE   A HD1  1 
ATOM   4264 H  HD2  . PHE   A 1 281 ? 17.051  -8.862  7.286   1.00 23.00 ? 281 PHE   A HD2  1 
ATOM   4265 H  HE1  . PHE   A 1 281 ? 12.791  -8.173  8.949   1.00 24.06 ? 281 PHE   A HE1  1 
ATOM   4266 H  HE2  . PHE   A 1 281 ? 16.479  -6.813  8.191   1.00 22.17 ? 281 PHE   A HE2  1 
ATOM   4267 H  HZ   . PHE   A 1 281 ? 14.345  -6.465  9.023   1.00 21.67 ? 281 PHE   A HZ   1 
ATOM   4268 N  N    . ASP   A 1 282 ? 15.835  -11.255 3.685   1.00 19.09 ? 282 ASP   A N    1 
ATOM   4269 C  CA   . ASP   A 1 282 ? 16.024  -10.582 2.395   1.00 19.63 ? 282 ASP   A CA   1 
ATOM   4270 C  C    . ASP   A 1 282 ? 14.701  -10.468 1.644   1.00 20.73 ? 282 ASP   A C    1 
ATOM   4271 O  O    . ASP   A 1 282 ? 14.379  -9.422  1.067   1.00 20.01 ? 282 ASP   A O    1 
ATOM   4272 C  CB   . ASP   A 1 282 ? 17.017  -11.336 1.502   1.00 21.03 ? 282 ASP   A CB   1 
ATOM   4273 C  CG   . ASP   A 1 282 ? 18.455  -11.231 1.958   1.00 28.93 ? 282 ASP   A CG   1 
ATOM   4274 O  OD1  . ASP   A 1 282 ? 18.810  -10.331 2.757   1.00 27.74 ? 282 ASP   A OD1  1 
ATOM   4275 O  OD2  . ASP   A 1 282 ? 19.254  -12.052 1.452   1.00 29.21 ? 282 ASP   A OD2  1 
ATOM   4276 H  H    . ASP   A 1 282 ? 16.337  -11.942 3.809   1.00 22.93 ? 282 ASP   A H    1 
ATOM   4277 H  HA   . ASP   A 1 282 ? 16.367  -9.687  2.546   1.00 23.57 ? 282 ASP   A HA   1 
ATOM   4278 H  HB2  . ASP   A 1 282 ? 16.777  -12.276 1.492   1.00 25.25 ? 282 ASP   A HB2  1 
ATOM   4279 H  HB3  . ASP   A 1 282 ? 16.965  -10.975 0.603   1.00 25.25 ? 282 ASP   A HB3  1 
ATOM   4280 N  N    . VAL   A 1 283 ? 13.947  -11.569 1.592   1.00 18.87 ? 283 VAL   A N    1 
ATOM   4281 C  CA   . VAL   A 1 283 ? 12.669  -11.578 0.880   1.00 20.27 ? 283 VAL   A CA   1 
ATOM   4282 C  C    . VAL   A 1 283 ? 11.702  -10.589 1.520   1.00 19.07 ? 283 VAL   A C    1 
ATOM   4283 O  O    . VAL   A 1 283 ? 11.031  -9.809  0.831   1.00 18.98 ? 283 VAL   A O    1 
ATOM   4284 C  CB   . VAL   A 1 283 ? 12.090  -13.005 0.860   1.00 18.19 ? 283 VAL   A CB   1 
ATOM   4285 C  CG1  . VAL   A 1 283 ? 10.645  -13.013 0.380   1.00 19.57 ? 283 VAL   A CG1  1 
ATOM   4286 C  CG2  . VAL   A 1 283 ? 12.981  -13.917 0.040   1.00 22.00 ? 283 VAL   A CG2  1 
ATOM   4287 H  H    . VAL   A 1 283 ? 14.153  -12.319 1.959   1.00 22.67 ? 283 VAL   A H    1 
ATOM   4288 H  HA   . VAL   A 1 283 ? 12.817  -11.301 -0.038  1.00 24.35 ? 283 VAL   A HA   1 
ATOM   4289 H  HB   . VAL   A 1 283 ? 12.091  -13.345 1.769   1.00 21.85 ? 283 VAL   A HB   1 
ATOM   4290 H  HG11 . VAL   A 1 283 ? 10.401  -13.920 0.136   1.00 23.50 ? 283 VAL   A HG11 1 
ATOM   4291 H  HG12 . VAL   A 1 283 ? 10.070  -12.698 1.095   1.00 23.50 ? 283 VAL   A HG12 1 
ATOM   4292 H  HG13 . VAL   A 1 283 ? 10.566  -12.432 -0.392  1.00 23.50 ? 283 VAL   A HG13 1 
ATOM   4293 H  HG21 . VAL   A 1 283 ? 12.590  -14.805 0.019   1.00 26.42 ? 283 VAL   A HG21 1 
ATOM   4294 H  HG22 . VAL   A 1 283 ? 13.049  -13.564 -0.861  1.00 26.42 ? 283 VAL   A HG22 1 
ATOM   4295 H  HG23 . VAL   A 1 283 ? 13.860  -13.952 0.449   1.00 26.42 ? 283 VAL   A HG23 1 
ATOM   4296 N  N    . MET   A 1 284 ? 11.588  -10.635 2.852   1.00 18.59 ? 284 MET   A N    1 
ATOM   4297 C  CA   . MET   A 1 284 ? 10.717  -9.712  3.590   1.00 16.08 ? 284 MET   A CA   1 
ATOM   4298 C  C    . MET   A 1 284 ? 11.095  -8.257  3.390   1.00 18.44 ? 284 MET   A C    1 
ATOM   4299 O  O    . MET   A 1 284 ? 10.216  -7.413  3.183   1.00 16.67 ? 284 MET   A O    1 
ATOM   4300 C  CB   . MET   A 1 284 ? 10.773  -10.121 5.067   1.00 15.21 ? 284 MET   A CB   1 
ATOM   4301 C  CG   . MET   A 1 284 ? 10.211  -11.499 5.412   1.00 18.67 ? 284 MET   A CG   1 
ATOM   4302 S  SD   . MET   A 1 284 ? 8.497   -11.812 4.881   1.00 17.97 ? 284 MET   A SD   1 
ATOM   4303 C  CE   . MET   A 1 284 ? 8.251   -13.418 5.620   1.00 17.69 ? 284 MET   A CE   1 
ATOM   4304 H  H    . MET   A 1 284 ? 12.007  -11.194 3.354   1.00 22.32 ? 284 MET   A H    1 
ATOM   4305 H  HA   . MET   A 1 284 ? 9.805   -9.837  3.284   1.00 19.31 ? 284 MET   A HA   1 
ATOM   4306 H  HB2  . MET   A 1 284 ? 11.701  -10.110 5.350   1.00 18.28 ? 284 MET   A HB2  1 
ATOM   4307 H  HB3  . MET   A 1 284 ? 10.272  -9.469  5.582   1.00 18.28 ? 284 MET   A HB3  1 
ATOM   4308 H  HG2  . MET   A 1 284 ? 10.764  -12.161 4.968   1.00 22.42 ? 284 MET   A HG2  1 
ATOM   4309 H  HG3  . MET   A 1 284 ? 10.268  -11.638 6.364   1.00 22.42 ? 284 MET   A HG3  1 
ATOM   4310 H  HE1  . MET   A 1 284 ? 7.354   -13.725 5.416   1.00 21.25 ? 284 MET   A HE1  1 
ATOM   4311 H  HE2  . MET   A 1 284 ? 8.903   -14.036 5.255   1.00 21.25 ? 284 MET   A HE2  1 
ATOM   4312 H  HE3  . MET   A 1 284 ? 8.366   -13.344 6.580   1.00 21.25 ? 284 MET   A HE3  1 
ATOM   4313 N  N    . VAL   A 1 285 ? 12.388  -7.935  3.459   1.00 17.70 ? 285 VAL   A N    1 
ATOM   4314 C  CA   . VAL   A 1 285 ? 12.810  -6.541  3.316   1.00 17.92 ? 285 VAL   A CA   1 
ATOM   4315 C  C    . VAL   A 1 285 ? 12.480  -6.039  1.915   1.00 18.22 ? 285 VAL   A C    1 
ATOM   4316 O  O    . VAL   A 1 285 ? 11.947  -4.936  1.733   1.00 19.39 ? 285 VAL   A O    1 
ATOM   4317 C  CB   . VAL   A 1 285 ? 14.311  -6.403  3.634   1.00 17.01 ? 285 VAL   A CB   1 
ATOM   4318 C  CG1  . VAL   A 1 285 ? 14.836  -5.051  3.160   1.00 18.79 ? 285 VAL   A CG1  1 
ATOM   4319 C  CG2  . VAL   A 1 285 ? 14.562  -6.615  5.122   1.00 18.80 ? 285 VAL   A CG2  1 
ATOM   4320 H  H    . VAL   A 1 285 ? 13.030  -8.494  3.585   1.00 21.26 ? 285 VAL   A H    1 
ATOM   4321 H  HA   . VAL   A 1 285 ? 12.319  -5.997  3.951   1.00 21.52 ? 285 VAL   A HA   1 
ATOM   4322 H  HB   . VAL   A 1 285 ? 14.795  -7.092  3.153   1.00 20.43 ? 285 VAL   A HB   1 
ATOM   4323 H  HG11 . VAL   A 1 285 ? 15.626  -4.824  3.675   1.00 22.57 ? 285 VAL   A HG11 1 
ATOM   4324 H  HG12 . VAL   A 1 285 ? 15.064  -5.114  2.220   1.00 22.57 ? 285 VAL   A HG12 1 
ATOM   4325 H  HG13 . VAL   A 1 285 ? 14.151  -4.378  3.296   1.00 22.57 ? 285 VAL   A HG13 1 
ATOM   4326 H  HG21 . VAL   A 1 285 ? 15.514  -6.543  5.295   1.00 22.58 ? 285 VAL   A HG21 1 
ATOM   4327 H  HG22 . VAL   A 1 285 ? 14.082  -5.936  5.622   1.00 22.58 ? 285 VAL   A HG22 1 
ATOM   4328 H  HG23 . VAL   A 1 285 ? 14.246  -7.497  5.373   1.00 22.58 ? 285 VAL   A HG23 1 
ATOM   4329 N  N    . LYS   A 1 286 ? 12.786  -6.851  0.897   1.00 19.45 ? 286 LYS   A N    1 
ATOM   4330 C  CA   . LYS   A 1 286 ? 12.526  -6.444  -0.479  1.00 20.87 ? 286 LYS   A CA   1 
ATOM   4331 C  C    . LYS   A 1 286 ? 11.026  -6.314  -0.745  1.00 18.06 ? 286 LYS   A C    1 
ATOM   4332 O  O    . LYS   A 1 286 ? 10.595  -5.394  -1.451  1.00 20.16 ? 286 LYS   A O    1 
ATOM   4333 C  CB   . LYS   A 1 286 ? 13.184  -7.435  -1.443  1.00 22.06 ? 286 LYS   A CB   1 
ATOM   4334 C  CG   . LYS   A 1 286 ? 12.923  -7.123  -2.906  1.00 29.65 ? 286 LYS   A CG   1 
ATOM   4335 C  CD   . LYS   A 1 286 ? 14.046  -7.591  -3.830  1.00 35.11 ? 286 LYS   A CD   1 
ATOM   4336 C  CE   . LYS   A 1 286 ? 14.084  -6.766  -5.112  1.00 40.00 ? 286 LYS   A CE   1 
ATOM   4337 N  NZ   . LYS   A 1 286 ? 14.668  -5.408  -4.933  1.00 47.80 ? 286 LYS   A NZ   1 
ATOM   4338 H  H    . LYS   A 1 286 ? 13.140  -7.631  0.979   1.00 23.36 ? 286 LYS   A H    1 
ATOM   4339 H  HA   . LYS   A 1 286 ? 12.927  -5.575  -0.631  1.00 25.07 ? 286 LYS   A HA   1 
ATOM   4340 H  HB2  . LYS   A 1 286 ? 14.143  -7.418  -1.299  1.00 26.49 ? 286 LYS   A HB2  1 
ATOM   4341 H  HB3  . LYS   A 1 286 ? 12.841  -8.323  -1.261  1.00 26.49 ? 286 LYS   A HB3  1 
ATOM   4342 H  HG2  . LYS   A 1 286 ? 12.105  -7.565  -3.182  1.00 35.60 ? 286 LYS   A HG2  1 
ATOM   4343 H  HG3  . LYS   A 1 286 ? 12.831  -6.163  -3.011  1.00 35.60 ? 286 LYS   A HG3  1 
ATOM   4344 H  HD2  . LYS   A 1 286 ? 14.900  -7.495  -3.381  1.00 42.15 ? 286 LYS   A HD2  1 
ATOM   4345 H  HD3  . LYS   A 1 286 ? 13.892  -8.517  -4.071  1.00 42.15 ? 286 LYS   A HD3  1 
ATOM   4346 H  HE2  . LYS   A 1 286 ? 14.622  -7.235  -5.769  1.00 48.02 ? 286 LYS   A HE2  1 
ATOM   4347 H  HE3  . LYS   A 1 286 ? 13.178  -6.659  -5.443  1.00 48.02 ? 286 LYS   A HE3  1 
ATOM   4348 H  HZ1  . LYS   A 1 286 ? 15.506  -5.474  -4.640  1.00 57.38 ? 286 LYS   A HZ1  1 
ATOM   4349 H  HZ2  . LYS   A 1 286 ? 14.666  -4.972  -5.709  1.00 57.38 ? 286 LYS   A HZ2  1 
ATOM   4350 H  HZ3  . LYS   A 1 286 ? 14.190  -4.947  -4.340  1.00 57.38 ? 286 LYS   A HZ3  1 
ATOM   4351 N  N    . ALA   A 1 287 ? 10.215  -7.201  -0.163  1.00 18.54 ? 287 ALA   A N    1 
ATOM   4352 C  CA   . ALA   A 1 287 ? 8.765   -7.053  -0.272  1.00 18.49 ? 287 ALA   A CA   1 
ATOM   4353 C  C    . ALA   A 1 287 ? 8.292   -5.762  0.390   1.00 19.70 ? 287 ALA   A C    1 
ATOM   4354 O  O    . ALA   A 1 287 ? 7.463   -5.035  -0.169  1.00 18.90 ? 287 ALA   A O    1 
ATOM   4355 C  CB   . ALA   A 1 287 ? 8.064   -8.259  0.356   1.00 19.87 ? 287 ALA   A CB   1 
ATOM   4356 H  H    . ALA   A 1 287 ? 10.474  -7.884  0.291   1.00 22.26 ? 287 ALA   A H    1 
ATOM   4357 H  HA   . ALA   A 1 287 ? 8.520   -7.017  -1.210  1.00 22.20 ? 287 ALA   A HA   1 
ATOM   4358 H  HB1  . ALA   A 1 287 ? 7.104   -8.144  0.274   1.00 23.86 ? 287 ALA   A HB1  1 
ATOM   4359 H  HB2  . ALA   A 1 287 ? 8.342   -9.063  -0.110  1.00 23.86 ? 287 ALA   A HB2  1 
ATOM   4360 H  HB3  . ALA   A 1 287 ? 8.312   -8.316  1.292   1.00 23.86 ? 287 ALA   A HB3  1 
ATOM   4361 N  N    . ASN   A 1 288 ? 8.814   -5.463  1.581   1.00 18.88 ? 288 ASN   A N    1 
ATOM   4362 C  CA   . ASN   A 1 288 ? 8.451   -4.226  2.268   1.00 17.80 ? 288 ASN   A CA   1 
ATOM   4363 C  C    . ASN   A 1 288 ? 8.827   -3.020  1.399   1.00 18.39 ? 288 ASN   A C    1 
ATOM   4364 O  O    . ASN   A 1 288 ? 8.050   -2.068  1.262   1.00 19.95 ? 288 ASN   A O    1 
ATOM   4365 C  CB   . ASN   A 1 288 ? 9.188   -4.166  3.616   1.00 17.13 ? 288 ASN   A CB   1 
ATOM   4366 C  CG   . ASN   A 1 288 ? 8.513   -3.248  4.633   1.00 17.45 ? 288 ASN   A CG   1 
ATOM   4367 O  OD1  . ASN   A 1 288 ? 7.908   -2.235  4.293   1.00 19.26 ? 288 ASN   A OD1  1 
ATOM   4368 N  ND2  . ASN   A 1 288 ? 8.705   -3.568  5.915   1.00 18.38 ? 288 ASN   A ND2  1 
ATOM   4369 H  H    . ASN   A 1 288 ? 9.375   -5.956  2.008   1.00 22.68 ? 288 ASN   A H    1 
ATOM   4370 H  HA   . ASN   A 1 288 ? 7.495   -4.208  2.432   1.00 21.38 ? 288 ASN   A HA   1 
ATOM   4371 H  HB2  . ASN   A 1 288 ? 9.222   -5.058  3.996   1.00 20.57 ? 288 ASN   A HB2  1 
ATOM   4372 H  HB3  . ASN   A 1 288 ? 10.088  -3.836  3.468   1.00 20.57 ? 288 ASN   A HB3  1 
ATOM   4373 H  HD21 . ASN   A 1 288 ? 8.356   -3.085  6.535   1.00 22.08 ? 288 ASN   A HD21 1 
ATOM   4374 H  HD22 . ASN   A 1 288 ? 9.148   -4.276  6.119   1.00 22.08 ? 288 ASN   A HD22 1 
ATOM   4375 N  N    . MET   A 1 289 ? 10.004  -3.074  0.764   1.00 18.09 ? 289 MET   A N    1 
ATOM   4376 C  CA   A MET   A 1 289 ? 10.498  -1.926  0.011   0.65 21.67 ? 289 MET   A CA   1 
ATOM   4377 C  CA   B MET   A 1 289 ? 10.498  -1.921  0.014   0.35 21.69 ? 289 MET   A CA   1 
ATOM   4378 C  C    . MET   A 1 289 ? 9.748   -1.730  -1.299  1.00 23.28 ? 289 MET   A C    1 
ATOM   4379 O  O    . MET   A 1 289 ? 9.498   -0.586  -1.705  1.00 22.10 ? 289 MET   A O    1 
ATOM   4380 C  CB   A MET   A 1 289 ? 11.979  -2.112  -0.287  0.65 22.49 ? 289 MET   A CB   1 
ATOM   4381 C  CB   B MET   A 1 289 ? 12.000  -2.084  -0.251  0.35 22.54 ? 289 MET   A CB   1 
ATOM   4382 C  CG   A MET   A 1 289 ? 12.856  -1.937  0.909   0.65 19.74 ? 289 MET   A CG   1 
ATOM   4383 C  CG   B MET   A 1 289 ? 12.873  -1.855  0.971   0.35 19.83 ? 289 MET   A CG   1 
ATOM   4384 S  SD   A MET   A 1 289 ? 14.554  -2.289  0.494   0.65 27.88 ? 289 MET   A SD   1 
ATOM   4385 S  SD   B MET   A 1 289 ? 14.643  -1.897  0.672   0.35 24.39 ? 289 MET   A SD   1 
ATOM   4386 C  CE   A MET   A 1 289 ? 14.974  -0.782  -0.376  0.65 25.97 ? 289 MET   A CE   1 
ATOM   4387 C  CE   B MET   A 1 289 ? 14.773  -3.532  -0.038  0.35 21.77 ? 289 MET   A CE   1 
ATOM   4388 H  H    A MET   A 1 289 ? 10.526  -3.757  0.756   0.65 21.73 ? 289 MET   A H    1 
ATOM   4389 H  H    B MET   A 1 289 ? 10.526  -3.757  0.754   0.35 21.73 ? 289 MET   A H    1 
ATOM   4390 H  HA   A MET   A 1 289 ? 10.399  -1.128  0.553   0.65 26.02 ? 289 MET   A HA   1 
ATOM   4391 H  HA   B MET   A 1 289 ? 10.380  -1.125  0.556   0.35 26.04 ? 289 MET   A HA   1 
ATOM   4392 H  HB2  A MET   A 1 289 ? 12.119  -3.008  -0.630  0.65 27.01 ? 289 MET   A HB2  1 
ATOM   4393 H  HB2  B MET   A 1 289 ? 12.162  -2.986  -0.568  0.35 27.06 ? 289 MET   A HB2  1 
ATOM   4394 H  HB3  A MET   A 1 289 ? 12.248  -1.459  -0.952  0.65 27.01 ? 289 MET   A HB3  1 
ATOM   4395 H  HB3  B MET   A 1 289 ? 12.268  -1.445  -0.930  0.35 27.06 ? 289 MET   A HB3  1 
ATOM   4396 H  HG2  A MET   A 1 289 ? 12.804  -1.022  1.218   0.65 23.71 ? 289 MET   A HG2  1 
ATOM   4397 H  HG2  B MET   A 1 289 ? 12.666  -0.991  1.345   0.35 23.81 ? 289 MET   A HG2  1 
ATOM   4398 H  HG3  A MET   A 1 289 ? 12.577  -2.548  1.609   0.65 23.71 ? 289 MET   A HG3  1 
ATOM   4399 H  HG3  B MET   A 1 289 ? 12.673  -2.545  1.623   0.35 23.81 ? 289 MET   A HG3  1 
ATOM   4400 H  HE1  A MET   A 1 289 ? 15.898  -0.833  -0.667  0.65 31.19 ? 289 MET   A HE1  1 
ATOM   4401 H  HE1  B MET   A 1 289 ? 15.697  -3.825  0.007   0.35 26.14 ? 289 MET   A HE1  1 
ATOM   4402 H  HE2  A MET   A 1 289 ? 14.390  -0.687  -1.145  0.65 31.19 ? 289 MET   A HE2  1 
ATOM   4403 H  HE2  B MET   A 1 289 ? 14.207  -4.136  0.465   0.35 26.14 ? 289 MET   A HE2  1 
ATOM   4404 H  HE3  A MET   A 1 289 ? 14.857  -0.029  0.224   0.65 31.19 ? 289 MET   A HE3  1 
ATOM   4405 H  HE3  B MET   A 1 289 ? 14.479  -3.499  -0.962  0.35 26.14 ? 289 MET   A HE3  1 
ATOM   4406 N  N    . ASP   A 1 290 ? 9.399   -2.827  -1.984  1.00 20.13 ? 290 ASP   A N    1 
ATOM   4407 C  CA   . ASP   A 1 290 ? 9.020   -2.776  -3.391  1.00 23.40 ? 290 ASP   A CA   1 
ATOM   4408 C  C    . ASP   A 1 290 ? 7.614   -3.252  -3.738  1.00 22.20 ? 290 ASP   A C    1 
ATOM   4409 O  O    . ASP   A 1 290 ? 7.146   -2.940  -4.840  1.00 25.75 ? 290 ASP   A O    1 
ATOM   4410 C  CB   . ASP   A 1 290 ? 10.012  -3.623  -4.210  1.00 25.61 ? 290 ASP   A CB   1 
ATOM   4411 C  CG   . ASP   A 1 290 ? 11.401  -2.997  -4.323  1.00 30.94 ? 290 ASP   A CG   1 
ATOM   4412 O  OD1  . ASP   A 1 290 ? 11.610  -1.883  -3.808  1.00 30.59 ? 290 ASP   A OD1  1 
ATOM   4413 O  OD2  . ASP   A 1 290 ? 12.318  -3.674  -4.835  1.00 39.29 ? 290 ASP   A OD2  1 
ATOM   4414 H  H    . ASP   A 1 290 ? 9.376   -3.618  -1.647  1.00 24.17 ? 290 ASP   A H    1 
ATOM   4415 H  HA   . ASP   A 1 290 ? 9.098   -1.860  -3.698  1.00 28.10 ? 290 ASP   A HA   1 
ATOM   4416 H  HB2  . ASP   A 1 290 ? 10.110  -4.489  -3.785  1.00 30.75 ? 290 ASP   A HB2  1 
ATOM   4417 H  HB3  . ASP   A 1 290 ? 9.662   -3.734  -5.108  1.00 30.75 ? 290 ASP   A HB3  1 
ATOM   4418 N  N    . TYR   A 1 291 ? 6.921   -3.984  -2.848  1.00 22.50 ? 291 TYR   A N    1 
ATOM   4419 C  CA   . TYR   A 1 291 ? 5.658   -4.607  -3.248  1.00 21.25 ? 291 TYR   A CA   1 
ATOM   4420 C  C    . TYR   A 1 291 ? 4.511   -4.435  -2.268  1.00 20.69 ? 291 TYR   A C    1 
ATOM   4421 O  O    . TYR   A 1 291 ? 3.381   -4.204  -2.708  1.00 22.72 ? 291 TYR   A O    1 
ATOM   4422 C  CB   . TYR   A 1 291 ? 5.921   -6.094  -3.488  1.00 22.61 ? 291 TYR   A CB   1 
ATOM   4423 C  CG   . TYR   A 1 291 ? 6.807   -6.306  -4.679  1.00 22.45 ? 291 TYR   A CG   1 
ATOM   4424 C  CD1  . TYR   A 1 291 ? 6.359   -5.991  -5.953  1.00 27.11 ? 291 TYR   A CD1  1 
ATOM   4425 C  CD2  . TYR   A 1 291 ? 8.113   -6.746  -4.536  1.00 22.02 ? 291 TYR   A CD2  1 
ATOM   4426 C  CE1  . TYR   A 1 291 ? 7.167   -6.155  -7.053  1.00 27.32 ? 291 TYR   A CE1  1 
ATOM   4427 C  CE2  . TYR   A 1 291 ? 8.935   -6.911  -5.640  1.00 24.03 ? 291 TYR   A CE2  1 
ATOM   4428 C  CZ   . TYR   A 1 291 ? 8.459   -6.610  -6.897  1.00 28.59 ? 291 TYR   A CZ   1 
ATOM   4429 O  OH   . TYR   A 1 291 ? 9.262   -6.770  -8.000  1.00 31.05 ? 291 TYR   A OH   1 
ATOM   4430 H  H    . TYR   A 1 291 ? 7.156   -4.129  -2.033  1.00 27.02 ? 291 TYR   A H    1 
ATOM   4431 H  HA   . TYR   A 1 291 ? 5.370   -4.222  -4.089  1.00 25.51 ? 291 TYR   A HA   1 
ATOM   4432 H  HB2  . TYR   A 1 291 ? 6.361   -6.471  -2.710  1.00 27.15 ? 291 TYR   A HB2  1 
ATOM   4433 H  HB3  . TYR   A 1 291 ? 5.079   -6.546  -3.651  1.00 27.15 ? 291 TYR   A HB3  1 
ATOM   4434 H  HD1  . TYR   A 1 291 ? 5.489   -5.684  -6.068  1.00 32.55 ? 291 TYR   A HD1  1 
ATOM   4435 H  HD2  . TYR   A 1 291 ? 8.437   -6.951  -3.689  1.00 26.44 ? 291 TYR   A HD2  1 
ATOM   4436 H  HE1  . TYR   A 1 291 ? 6.845   -5.951  -7.901  1.00 32.80 ? 291 TYR   A HE1  1 
ATOM   4437 H  HE2  . TYR   A 1 291 ? 9.805   -7.220  -5.532  1.00 28.85 ? 291 TYR   A HE2  1 
ATOM   4438 H  HH   . TYR   A 1 291 ? 10.034  -6.998  -7.762  1.00 37.28 ? 291 TYR   A HH   1 
ATOM   4439 N  N    . TRP   A 1 292 ? 4.755   -4.572  -0.973  1.00 19.25 ? 292 TRP   A N    1 
ATOM   4440 C  CA   . TRP   A 1 292 ? 3.664   -4.502  -0.012  1.00 19.00 ? 292 TRP   A CA   1 
ATOM   4441 C  C    . TRP   A 1 292 ? 2.998   -3.132  -0.030  1.00 18.79 ? 292 TRP   A C    1 
ATOM   4442 O  O    . TRP   A 1 292 ? 3.661   -2.099  -0.127  1.00 22.00 ? 292 TRP   A O    1 
ATOM   4443 C  CB   . TRP   A 1 292 ? 4.190   -4.807  1.384   1.00 20.31 ? 292 TRP   A CB   1 
ATOM   4444 C  CG   . TRP   A 1 292 ? 4.525   -6.238  1.659   1.00 17.90 ? 292 TRP   A CG   1 
ATOM   4445 C  CD1  . TRP   A 1 292 ? 4.190   -7.331  0.911   1.00 17.70 ? 292 TRP   A CD1  1 
ATOM   4446 C  CD2  . TRP   A 1 292 ? 5.281   -6.728  2.769   1.00 16.32 ? 292 TRP   A CD2  1 
ATOM   4447 N  NE1  . TRP   A 1 292 ? 4.681   -8.476  1.498   1.00 17.01 ? 292 TRP   A NE1  1 
ATOM   4448 C  CE2  . TRP   A 1 292 ? 5.358   -8.128  2.639   1.00 16.79 ? 292 TRP   A CE2  1 
ATOM   4449 C  CE3  . TRP   A 1 292 ? 5.895   -6.116  3.865   1.00 17.85 ? 292 TRP   A CE3  1 
ATOM   4450 C  CZ2  . TRP   A 1 292 ? 6.026   -8.925  3.567   1.00 17.94 ? 292 TRP   A CZ2  1 
ATOM   4451 C  CZ3  . TRP   A 1 292 ? 6.561   -6.906  4.776   1.00 17.50 ? 292 TRP   A CZ3  1 
ATOM   4452 C  CH2  . TRP   A 1 292 ? 6.627   -8.292  4.623   1.00 15.07 ? 292 TRP   A CH2  1 
ATOM   4453 H  H    . TRP   A 1 292 ? 5.531   -4.705  -0.628  1.00 23.12 ? 292 TRP   A H    1 
ATOM   4454 H  HA   . TRP   A 1 292 ? 2.993   -5.164  -0.240  1.00 22.82 ? 292 TRP   A HA   1 
ATOM   4455 H  HB2  . TRP   A 1 292 ? 4.997   -4.289  1.526   1.00 24.39 ? 292 TRP   A HB2  1 
ATOM   4456 H  HB3  . TRP   A 1 292 ? 3.517   -4.538  2.029   1.00 24.39 ? 292 TRP   A HB3  1 
ATOM   4457 H  HD1  . TRP   A 1 292 ? 3.691   -7.307  0.127   1.00 21.25 ? 292 TRP   A HD1  1 
ATOM   4458 H  HE1  . TRP   A 1 292 ? 4.585   -9.275  1.196   1.00 20.43 ? 292 TRP   A HE1  1 
ATOM   4459 H  HE3  . TRP   A 1 292 ? 5.859   -5.193  3.974   1.00 21.43 ? 292 TRP   A HE3  1 
ATOM   4460 H  HZ2  . TRP   A 1 292 ? 6.074   -9.848  3.466   1.00 21.55 ? 292 TRP   A HZ2  1 
ATOM   4461 H  HZ3  . TRP   A 1 292 ? 6.973   -6.508  5.509   1.00 21.02 ? 292 TRP   A HZ3  1 
ATOM   4462 H  HH2  . TRP   A 1 292 ? 7.079   -8.798  5.259   1.00 18.11 ? 292 TRP   A HH2  1 
ATOM   4463 N  N    . THR   A 1 293 ? 1.673   -3.132  0.079   1.00 19.31 ? 293 THR   A N    1 
ATOM   4464 C  CA   . THR   A 1 293 ? 0.860   -1.923  0.034   1.00 19.18 ? 293 THR   A CA   1 
ATOM   4465 C  C    . THR   A 1 293 ? 0.277   -1.619  1.408   1.00 19.00 ? 293 THR   A C    1 
ATOM   4466 O  O    . THR   A 1 293 ? 0.247   -2.487  2.289   1.00 18.95 ? 293 THR   A O    1 
ATOM   4467 C  CB   . THR   A 1 293 ? -0.257  -2.076  -1.012  1.00 25.61 ? 293 THR   A CB   1 
ATOM   4468 O  OG1  . THR   A 1 293 ? -1.289  -2.924  -0.487  1.00 26.75 ? 293 THR   A OG1  1 
ATOM   4469 C  CG2  . THR   A 1 293 ? 0.285   -2.643  -2.329  1.00 25.06 ? 293 THR   A CG2  1 
ATOM   4470 H  H    . THR   A 1 293 ? 1.207   -3.847  0.184   1.00 23.19 ? 293 THR   A H    1 
ATOM   4471 H  HA   . THR   A 1 293 ? 1.423   -1.181  -0.232  1.00 23.03 ? 293 THR   A HA   1 
ATOM   4472 H  HB   . THR   A 1 293 ? -0.634  -1.202  -1.198  1.00 30.75 ? 293 THR   A HB   1 
ATOM   4473 H  HG1  . THR   A 1 293 ? -0.974  -3.681  -0.306  1.00 32.12 ? 293 THR   A HG1  1 
ATOM   4474 H  HG21 . THR   A 1 293 ? -0.400  -2.601  -3.014  1.00 30.09 ? 293 THR   A HG21 1 
ATOM   4475 H  HG22 . THR   A 1 293 ? 1.053   -2.127  -2.620  1.00 30.09 ? 293 THR   A HG22 1 
ATOM   4476 H  HG23 . THR   A 1 293 ? 0.554   -3.567  -2.208  1.00 30.09 ? 293 THR   A HG23 1 
ATOM   4477 N  N    . PRO   A 1 294 ? -0.143  -0.378  1.652   1.00 18.66 ? 294 PRO   A N    1 
ATOM   4478 C  CA   . PRO   A 1 294 ? -0.522  -0.011  3.032   1.00 19.99 ? 294 PRO   A CA   1 
ATOM   4479 C  C    . PRO   A 1 294 ? -1.680  -0.815  3.598   1.00 16.71 ? 294 PRO   A C    1 
ATOM   4480 O  O    . PRO   A 1 294 ? -1.698  -1.042  4.812   1.00 17.46 ? 294 PRO   A O    1 
ATOM   4481 C  CB   . PRO   A 1 294 ? -0.849  1.488   2.926   1.00 19.57 ? 294 PRO   A CB   1 
ATOM   4482 C  CG   . PRO   A 1 294 ? -0.030  1.951   1.730   1.00 23.68 ? 294 PRO   A CG   1 
ATOM   4483 C  CD   . PRO   A 1 294 ? -0.137  0.796   0.756   1.00 19.51 ? 294 PRO   A CD   1 
ATOM   4484 H  HA   . PRO   A 1 294 ? 0.243   -0.119  3.618   1.00 24.01 ? 294 PRO   A HA   1 
ATOM   4485 H  HB2  . PRO   A 1 294 ? -1.798  1.609   2.765   1.00 23.50 ? 294 PRO   A HB2  1 
ATOM   4486 H  HB3  . PRO   A 1 294 ? -0.571  1.945   3.735   1.00 23.50 ? 294 PRO   A HB3  1 
ATOM   4487 H  HG2  . PRO   A 1 294 ? -0.417  2.758   1.356   1.00 28.43 ? 294 PRO   A HG2  1 
ATOM   4488 H  HG3  . PRO   A 1 294 ? 0.891   2.097   1.996   1.00 28.43 ? 294 PRO   A HG3  1 
ATOM   4489 H  HD2  . PRO   A 1 294 ? -0.967  0.848   0.257   1.00 23.43 ? 294 PRO   A HD2  1 
ATOM   4490 H  HD3  . PRO   A 1 294 ? 0.634   0.784   0.169   1.00 23.43 ? 294 PRO   A HD3  1 
ATOM   4491 N  N    . TYR   A 1 295 ? -2.635  -1.265  2.776   1.00 19.65 ? 295 TYR   A N    1 
ATOM   4492 C  CA   . TYR   A 1 295 ? -3.772  -2.054  3.249   1.00 19.62 ? 295 TYR   A CA   1 
ATOM   4493 C  C    . TYR   A 1 295 ? -3.647  -3.527  2.863   1.00 19.55 ? 295 TYR   A C    1 
ATOM   4494 O  O    . TYR   A 1 295 ? -4.653  -4.224  2.723   1.00 22.70 ? 295 TYR   A O    1 
ATOM   4495 C  CB   . TYR   A 1 295 ? -5.099  -1.463  2.741   1.00 21.67 ? 295 TYR   A CB   1 
ATOM   4496 C  CG   . TYR   A 1 295 ? -5.281  -0.095  3.339   1.00 23.78 ? 295 TYR   A CG   1 
ATOM   4497 C  CD1  . TYR   A 1 295 ? -5.893  0.061   4.571   1.00 23.61 ? 295 TYR   A CD1  1 
ATOM   4498 C  CD2  . TYR   A 1 295 ? -4.779  1.031   2.705   1.00 19.62 ? 295 TYR   A CD2  1 
ATOM   4499 C  CE1  . TYR   A 1 295 ? -6.012  1.296   5.153   1.00 21.90 ? 295 TYR   A CE1  1 
ATOM   4500 C  CE2  . TYR   A 1 295 ? -4.894  2.275   3.275   1.00 21.34 ? 295 TYR   A CE2  1 
ATOM   4501 C  CZ   . TYR   A 1 295 ? -5.520  2.400   4.497   1.00 23.98 ? 295 TYR   A CZ   1 
ATOM   4502 O  OH   . TYR   A 1 295 ? -5.650  3.634   5.086   1.00 25.06 ? 295 TYR   A OH   1 
ATOM   4503 H  H    . TYR   A 1 295 ? -2.644  -1.123  1.928   1.00 23.60 ? 295 TYR   A H    1 
ATOM   4504 H  HA   . TYR   A 1 295 ? -3.793  -2.013  4.218   1.00 23.56 ? 295 TYR   A HA   1 
ATOM   4505 H  HB2  . TYR   A 1 295 ? -5.074  -1.381  1.775   1.00 26.03 ? 295 TYR   A HB2  1 
ATOM   4506 H  HB3  . TYR   A 1 295 ? -5.838  -2.026  3.020   1.00 26.03 ? 295 TYR   A HB3  1 
ATOM   4507 H  HD1  . TYR   A 1 295 ? -6.219  -0.687  5.017   1.00 28.35 ? 295 TYR   A HD1  1 
ATOM   4508 H  HD2  . TYR   A 1 295 ? -4.351  0.942   1.884   1.00 23.56 ? 295 TYR   A HD2  1 
ATOM   4509 H  HE1  . TYR   A 1 295 ? -6.435  1.388   5.976   1.00 26.30 ? 295 TYR   A HE1  1 
ATOM   4510 H  HE2  . TYR   A 1 295 ? -4.563  3.026   2.837   1.00 25.63 ? 295 TYR   A HE2  1 
ATOM   4511 H  HH   . TYR   A 1 295 ? -5.254  4.214   4.626   1.00 30.09 ? 295 TYR   A HH   1 
ATOM   4512 N  N    . SER   A 1 296 ? -2.418  -4.019  2.727   1.00 18.71 ? 296 SER   A N    1 
ATOM   4513 C  CA   . SER   A 1 296 ? -2.190  -5.400  2.324   1.00 17.10 ? 296 SER   A CA   1 
ATOM   4514 C  C    . SER   A 1 296 ? -2.994  -6.378  3.166   1.00 19.07 ? 296 SER   A C    1 
ATOM   4515 O  O    . SER   A 1 296 ? -3.050  -6.260  4.395   1.00 19.12 ? 296 SER   A O    1 
ATOM   4516 C  CB   . SER   A 1 296 ? -0.699  -5.731  2.461   1.00 18.01 ? 296 SER   A CB   1 
ATOM   4517 O  OG   . SER   A 1 296 ? -0.397  -7.012  1.954   1.00 19.06 ? 296 SER   A OG   1 
ATOM   4518 H  H    . SER   A 1 296 ? -1.697  -3.570  2.863   1.00 22.47 ? 296 SER   A H    1 
ATOM   4519 H  HA   . SER   A 1 296 ? -2.446  -5.512  1.395   1.00 20.54 ? 296 SER   A HA   1 
ATOM   4520 H  HB2  . SER   A 1 296 ? -0.186  -5.071  1.969   1.00 21.63 ? 296 SER   A HB2  1 
ATOM   4521 H  HB3  . SER   A 1 296 ? -0.457  -5.702  3.400   1.00 21.63 ? 296 SER   A HB3  1 
ATOM   4522 H  HG   . SER   A 1 296 ? -0.812  -7.599  2.388   1.00 22.89 ? 296 SER   A HG   1 
ATOM   4523 N  N    . THR   A 1 297 ? -3.585  -7.370  2.498   1.00 19.53 ? 297 THR   A N    1 
ATOM   4524 C  CA   . THR   A 1 297 ? -4.054  -8.557  3.196   1.00 19.04 ? 297 THR   A CA   1 
ATOM   4525 C  C    . THR   A 1 297 ? -2.874  -9.521  3.366   1.00 17.02 ? 297 THR   A C    1 
ATOM   4526 O  O    . THR   A 1 297 ? -1.818  -9.361  2.742   1.00 18.84 ? 297 THR   A O    1 
ATOM   4527 C  CB   . THR   A 1 297 ? -5.133  -9.290  2.408   1.00 21.19 ? 297 THR   A CB   1 
ATOM   4528 O  OG1  . THR   A 1 297 ? -4.649  -9.581  1.092   1.00 21.77 ? 297 THR   A OG1  1 
ATOM   4529 C  CG2  . THR   A 1 297 ? -6.381  -8.421  2.252   1.00 24.84 ? 297 THR   A CG2  1 
ATOM   4530 H  H    . THR   A 1 297 ? -3.723  -7.377  1.649   1.00 23.45 ? 297 THR   A H    1 
ATOM   4531 H  HA   . THR   A 1 297 ? -4.402  -8.319  4.070   1.00 22.87 ? 297 THR   A HA   1 
ATOM   4532 H  HB   . THR   A 1 297 ? -5.375  -10.112 2.862   1.00 25.45 ? 297 THR   A HB   1 
ATOM   4533 H  HG1  . THR   A 1 297 ? -5.239  -9.985  0.652   1.00 26.14 ? 297 THR   A HG1  1 
ATOM   4534 H  HG21 . THR   A 1 297 ? -7.052  -8.894  1.735   1.00 29.83 ? 297 THR   A HG21 1 
ATOM   4535 H  HG22 . THR   A 1 297 ? -6.748  -8.208  3.124   1.00 29.83 ? 297 THR   A HG22 1 
ATOM   4536 H  HG23 . THR   A 1 297 ? -6.156  -7.596  1.795   1.00 29.83 ? 297 THR   A HG23 1 
ATOM   4537 N  N    . PHE   A 1 298 ? -3.067  -10.568 4.179   1.00 18.00 ? 298 PHE   A N    1 
ATOM   4538 C  CA   . PHE   A 1 298 ? -2.048  -11.611 4.276   1.00 15.57 ? 298 PHE   A CA   1 
ATOM   4539 C  C    . PHE   A 1 298 ? -1.765  -12.253 2.916   1.00 17.89 ? 298 PHE   A C    1 
ATOM   4540 O  O    . PHE   A 1 298 ? -0.610  -12.528 2.572   1.00 17.28 ? 298 PHE   A O    1 
ATOM   4541 C  CB   . PHE   A 1 298 ? -2.469  -12.706 5.260   1.00 17.50 ? 298 PHE   A CB   1 
ATOM   4542 C  CG   . PHE   A 1 298 ? -2.584  -12.271 6.691   1.00 18.11 ? 298 PHE   A CG   1 
ATOM   4543 C  CD1  . PHE   A 1 298 ? -1.649  -11.431 7.272   1.00 16.82 ? 298 PHE   A CD1  1 
ATOM   4544 C  CD2  . PHE   A 1 298 ? -3.637  -12.733 7.468   1.00 19.49 ? 298 PHE   A CD2  1 
ATOM   4545 C  CE1  . PHE   A 1 298 ? -1.763  -11.065 8.600   1.00 17.47 ? 298 PHE   A CE1  1 
ATOM   4546 C  CE2  . PHE   A 1 298 ? -3.761  -12.362 8.787   1.00 19.78 ? 298 PHE   A CE2  1 
ATOM   4547 C  CZ   . PHE   A 1 298 ? -2.825  -11.530 9.356   1.00 17.06 ? 298 PHE   A CZ   1 
ATOM   4548 H  H    . PHE   A 1 298 ? -3.761  -10.693 4.671   1.00 21.61 ? 298 PHE   A H    1 
ATOM   4549 H  HA   . PHE   A 1 298 ? -1.221  -11.216 4.594   1.00 18.71 ? 298 PHE   A HA   1 
ATOM   4550 H  HB2  . PHE   A 1 298 ? -3.336  -13.047 4.988   1.00 21.02 ? 298 PHE   A HB2  1 
ATOM   4551 H  HB3  . PHE   A 1 298 ? -1.814  -13.420 5.224   1.00 21.02 ? 298 PHE   A HB3  1 
ATOM   4552 H  HD1  . PHE   A 1 298 ? -0.932  -11.120 6.768   1.00 20.21 ? 298 PHE   A HD1  1 
ATOM   4553 H  HD2  . PHE   A 1 298 ? -4.271  -13.299 7.090   1.00 23.40 ? 298 PHE   A HD2  1 
ATOM   4554 H  HE1  . PHE   A 1 298 ? -1.134  -10.497 8.982   1.00 20.98 ? 298 PHE   A HE1  1 
ATOM   4555 H  HE2  . PHE   A 1 298 ? -4.473  -12.678 9.295   1.00 23.76 ? 298 PHE   A HE2  1 
ATOM   4556 H  HZ   . PHE   A 1 298 ? -2.908  -11.277 10.247  1.00 20.49 ? 298 PHE   A HZ   1 
ATOM   4557 N  N    . ASP   A 1 299 ? -2.818  -12.552 2.153   1.00 18.48 ? 299 ASP   A N    1 
ATOM   4558 C  CA   . ASP   A 1 299 ? -2.638  -13.162 0.837   1.00 19.38 ? 299 ASP   A CA   1 
ATOM   4559 C  C    . ASP   A 1 299 ? -1.878  -12.245 -0.108  1.00 19.27 ? 299 ASP   A C    1 
ATOM   4560 O  O    . ASP   A 1 299 ? -0.977  -12.686 -0.830  1.00 21.52 ? 299 ASP   A O    1 
ATOM   4561 C  CB   . ASP   A 1 299 ? -4.002  -13.542 0.248   1.00 18.54 ? 299 ASP   A CB   1 
ATOM   4562 C  CG   . ASP   A 1 299 ? -4.641  -14.730 0.931   1.00 23.44 ? 299 ASP   A CG   1 
ATOM   4563 O  OD1  . ASP   A 1 299 ? -3.973  -15.401 1.747   1.00 21.74 ? 299 ASP   A OD1  1 
ATOM   4564 O  OD2  . ASP   A 1 299 ? -5.845  -14.963 0.687   1.00 25.87 ? 299 ASP   A OD2  1 
ATOM   4565 H  H    . ASP   A 1 299 ? -3.638  -12.413 2.372   1.00 22.20 ? 299 ASP   A H    1 
ATOM   4566 H  HA   . ASP   A 1 299 ? -2.120  -13.975 0.937   1.00 23.27 ? 299 ASP   A HA   1 
ATOM   4567 H  HB2  . ASP   A 1 299 ? -4.604  -12.787 0.338   1.00 22.27 ? 299 ASP   A HB2  1 
ATOM   4568 H  HB3  . ASP   A 1 299 ? -3.888  -13.763 -0.690  1.00 22.27 ? 299 ASP   A HB3  1 
ATOM   4569 N  N    . GLU   A 1 300 ? -2.245  -10.963 -0.146  1.00 19.66 ? 300 GLU   A N    1 
ATOM   4570 C  CA   . GLU   A 1 300 ? -1.519  -10.021 -0.998  1.00 17.86 ? 300 GLU   A CA   1 
ATOM   4571 C  C    . GLU   A 1 300 ? -0.063  -9.910  -0.575  1.00 20.30 ? 300 GLU   A C    1 
ATOM   4572 O  O    . GLU   A 1 300 ? 0.824   -9.765  -1.426  1.00 20.62 ? 300 GLU   A O    1 
ATOM   4573 C  CB   . GLU   A 1 300 ? -2.217  -8.662  -0.945  1.00 19.78 ? 300 GLU   A CB   1 
ATOM   4574 C  CG   . GLU   A 1 300 ? -3.521  -8.633  -1.744  1.00 21.42 ? 300 GLU   A CG   1 
ATOM   4575 C  CD   . GLU   A 1 300 ? -4.407  -7.434  -1.445  1.00 29.95 ? 300 GLU   A CD   1 
ATOM   4576 O  OE1  . GLU   A 1 300 ? -4.069  -6.613  -0.565  1.00 23.17 ? 300 GLU   A OE1  1 
ATOM   4577 O  OE2  . GLU   A 1 300 ? -5.457  -7.324  -2.104  1.00 31.08 ? 300 GLU   A OE2  1 
ATOM   4578 H  H    . GLU   A 1 300 ? -2.895  -10.620 0.301   1.00 23.61 ? 300 GLU   A H    1 
ATOM   4579 H  HA   . GLU   A 1 300 ? -1.543  -10.337 -1.915  1.00 21.45 ? 300 GLU   A HA   1 
ATOM   4580 H  HB2  . GLU   A 1 300 ? -2.426  -8.451  -0.022  1.00 23.75 ? 300 GLU   A HB2  1 
ATOM   4581 H  HB3  . GLU   A 1 300 ? -1.625  -7.988  -1.314  1.00 23.75 ? 300 GLU   A HB3  1 
ATOM   4582 H  HG2  . GLU   A 1 300 ? -3.306  -8.613  -2.690  1.00 25.72 ? 300 GLU   A HG2  1 
ATOM   4583 H  HG3  . GLU   A 1 300 ? -4.029  -9.434  -1.540  1.00 25.72 ? 300 GLU   A HG3  1 
ATOM   4584 N  N    . GLY   A 1 301 ? 0.213   -10.001 0.728   1.00 18.73 ? 301 GLY   A N    1 
ATOM   4585 C  CA   . GLY   A 1 301 ? 1.590   -9.957  1.174   1.00 18.37 ? 301 GLY   A CA   1 
ATOM   4586 C  C    . GLY   A 1 301 ? 2.396   -11.135 0.673   1.00 19.18 ? 301 GLY   A C    1 
ATOM   4587 O  O    . GLY   A 1 301 ? 3.599   -11.009 0.430   1.00 18.06 ? 301 GLY   A O    1 
ATOM   4588 H  H    . GLY   A 1 301 ? -0.370  -10.087 1.355   1.00 22.49 ? 301 GLY   A H    1 
ATOM   4589 H  HA2  . GLY   A 1 301 ? 2.007   -9.141  0.856   1.00 22.07 ? 301 GLY   A HA2  1 
ATOM   4590 H  HA3  . GLY   A 1 301 ? 1.615   -9.959  2.143   1.00 22.07 ? 301 GLY   A HA3  1 
ATOM   4591 N  N    . GLY   A 1 302 ? 1.746   -12.284 0.497   1.00 18.41 ? 302 GLY   A N    1 
ATOM   4592 C  CA   . GLY   A 1 302 ? 2.429   -13.429 -0.080  1.00 18.75 ? 302 GLY   A CA   1 
ATOM   4593 C  C    . GLY   A 1 302 ? 2.816   -13.201 -1.528  1.00 19.83 ? 302 GLY   A C    1 
ATOM   4594 O  O    . GLY   A 1 302 ? 3.902   -13.599 -1.960  1.00 19.75 ? 302 GLY   A O    1 
ATOM   4595 H  H    . GLY   A 1 302 ? 0.922   -12.422 0.701   1.00 22.11 ? 302 GLY   A H    1 
ATOM   4596 H  HA2  . GLY   A 1 302 ? 3.234   -13.615 0.428   1.00 22.52 ? 302 GLY   A HA2  1 
ATOM   4597 H  HA3  . GLY   A 1 302 ? 1.851   -14.207 -0.035  1.00 22.52 ? 302 GLY   A HA3  1 
ATOM   4598 N  N    . CYS   A 1 303 ? 1.936   -12.561 -2.300  1.00 22.25 ? 303 CYS   A N    1 
ATOM   4599 C  CA   . CYS   A 1 303 ? 2.299   -12.185 -3.661  1.00 23.47 ? 303 CYS   A CA   1 
ATOM   4600 C  C    . CYS   A 1 303 ? 3.541   -11.302 -3.665  1.00 22.05 ? 303 CYS   A C    1 
ATOM   4601 O  O    . CYS   A 1 303 ? 4.431   -11.465 -4.507  1.00 22.08 ? 303 CYS   A O    1 
ATOM   4602 C  CB   . CYS   A 1 303 ? 1.142   -11.452 -4.337  1.00 24.06 ? 303 CYS   A CB   1 
ATOM   4603 S  SG   . CYS   A 1 303 ? -0.464  -12.256 -4.267  1.00 25.46 ? 303 CYS   A SG   1 
ATOM   4604 H  H    . CYS   A 1 303 ? 1.140   -12.338 -2.064  1.00 26.72 ? 303 CYS   A H    1 
ATOM   4605 H  HA   . CYS   A 1 303 ? 2.494   -12.985 -4.173  1.00 28.18 ? 303 CYS   A HA   1 
ATOM   4606 H  HB2  . CYS   A 1 303 ? 1.047   -10.583 -3.917  1.00 28.89 ? 303 CYS   A HB2  1 
ATOM   4607 H  HB3  . CYS   A 1 303 ? 1.364   -11.334 -5.274  1.00 28.89 ? 303 CYS   A HB3  1 
ATOM   4608 N  N    . GLY   A 1 304 ? 3.602   -10.327 -2.751  1.00 20.06 ? 304 GLY   A N    1 
ATOM   4609 C  CA   . GLY   A 1 304 ? 4.774   -9.470  -2.672  1.00 21.22 ? 304 GLY   A CA   1 
ATOM   4610 C  C    . GLY   A 1 304 ? 6.041   -10.230 -2.339  1.00 19.84 ? 304 GLY   A C    1 
ATOM   4611 O  O    . GLY   A 1 304 ? 7.116   -9.931  -2.857  1.00 20.83 ? 304 GLY   A O    1 
ATOM   4612 H  H    . GLY   A 1 304 ? 2.986   -10.148 -2.178  1.00 24.09 ? 304 GLY   A H    1 
ATOM   4613 H  HA2  . GLY   A 1 304 ? 4.902   -9.021  -3.522  1.00 25.48 ? 304 GLY   A HA2  1 
ATOM   4614 H  HA3  . GLY   A 1 304 ? 4.634   -8.796  -1.989  1.00 25.48 ? 304 GLY   A HA3  1 
ATOM   4615 N  N    . MET   A 1 305 ? 5.931   -11.234 -1.467  1.00 18.66 ? 305 MET   A N    1 
ATOM   4616 C  CA   . MET   A 1 305 ? 7.078   -12.073 -1.123  1.00 18.27 ? 305 MET   A CA   1 
ATOM   4617 C  C    . MET   A 1 305 ? 7.547   -12.835 -2.358  1.00 17.25 ? 305 MET   A C    1 
ATOM   4618 O  O    . MET   A 1 305 ? 8.749   -12.951 -2.616  1.00 19.49 ? 305 MET   A O    1 
ATOM   4619 C  CB   . MET   A 1 305 ? 6.599   -13.045 -0.052  1.00 16.15 ? 305 MET   A CB   1 
ATOM   4620 C  CG   . MET   A 1 305 ? 6.531   -12.422 1.318   1.00 16.99 ? 305 MET   A CG   1 
ATOM   4621 S  SD   . MET   A 1 305 ? 6.027   -13.575 2.613   1.00 18.32 ? 305 MET   A SD   1 
ATOM   4622 C  CE   . MET   A 1 305 ? 7.482   -14.692 2.593   1.00 21.73 ? 305 MET   A CE   1 
ATOM   4623 H  H    . MET   A 1 305 ? 5.203   -11.448 -1.062  1.00 22.41 ? 305 MET   A H    1 
ATOM   4624 H  HA   . MET   A 1 305 ? 7.799   -11.530 -0.766  1.00 21.94 ? 305 MET   A HA   1 
ATOM   4625 H  HB2  . MET   A 1 305 ? 5.711   -13.359 -0.283  1.00 19.40 ? 305 MET   A HB2  1 
ATOM   4626 H  HB3  . MET   A 1 305 ? 7.214   -13.794 -0.012  1.00 19.40 ? 305 MET   A HB3  1 
ATOM   4627 H  HG2  . MET   A 1 305 ? 7.408   -12.080 1.550   1.00 20.41 ? 305 MET   A HG2  1 
ATOM   4628 H  HG3  . MET   A 1 305 ? 5.888   -11.696 1.300   1.00 20.41 ? 305 MET   A HG3  1 
ATOM   4629 H  HE1  . MET   A 1 305 ? 7.413   -15.311 3.336   1.00 26.10 ? 305 MET   A HE1  1 
ATOM   4630 H  HE2  . MET   A 1 305 ? 7.494   -15.181 1.756   1.00 26.10 ? 305 MET   A HE2  1 
ATOM   4631 H  HE3  . MET   A 1 305 ? 8.289   -14.161 2.679   1.00 26.10 ? 305 MET   A HE3  1 
ATOM   4632 N  N    . LEU   A 1 306 ? 6.591   -13.373 -3.124  1.00 20.11 ? 306 LEU   A N    1 
ATOM   4633 C  CA   . LEU   A 1 306 ? 6.935   -14.128 -4.321  1.00 21.65 ? 306 LEU   A CA   1 
ATOM   4634 C  C    . LEU   A 1 306 ? 7.604   -13.232 -5.358  1.00 22.30 ? 306 LEU   A C    1 
ATOM   4635 O  O    . LEU   A 1 306 ? 8.604   -13.622 -5.976  1.00 23.56 ? 306 LEU   A O    1 
ATOM   4636 C  CB   . LEU   A 1 306 ? 5.673   -14.778 -4.893  1.00 21.34 ? 306 LEU   A CB   1 
ATOM   4637 C  CG   . LEU   A 1 306 ? 5.207   -15.994 -4.090  1.00 23.57 ? 306 LEU   A CG   1 
ATOM   4638 C  CD1  . LEU   A 1 306 ? 3.804   -16.421 -4.564  1.00 25.00 ? 306 LEU   A CD1  1 
ATOM   4639 C  CD2  . LEU   A 1 306 ? 6.183   -17.162 -4.140  1.00 26.47 ? 306 LEU   A CD2  1 
ATOM   4640 H  H    . LEU   A 1 306 ? 5.747   -13.313 -2.970  1.00 24.16 ? 306 LEU   A H    1 
ATOM   4641 H  HA   . LEU   A 1 306 ? 7.562   -14.829 -4.085  1.00 26.00 ? 306 LEU   A HA   1 
ATOM   4642 H  HB2  . LEU   A 1 306 ? 4.955   -14.126 -4.892  1.00 25.63 ? 306 LEU   A HB2  1 
ATOM   4643 H  HB3  . LEU   A 1 306 ? 5.853   -15.070 -5.800  1.00 25.63 ? 306 LEU   A HB3  1 
ATOM   4644 H  HG   . LEU   A 1 306 ? 5.127   -15.729 -3.160  1.00 28.30 ? 306 LEU   A HG   1 
ATOM   4645 H  HD11 . LEU   A 1 306 ? 3.518   -17.191 -4.048  1.00 30.02 ? 306 LEU   A HD11 1 
ATOM   4646 H  HD12 . LEU   A 1 306 ? 3.188   -15.684 -4.429  1.00 30.02 ? 306 LEU   A HD12 1 
ATOM   4647 H  HD13 . LEU   A 1 306 ? 3.845   -16.650 -5.506  1.00 30.02 ? 306 LEU   A HD13 1 
ATOM   4648 H  HD21 . LEU   A 1 306 ? 5.762   -17.940 -3.743  1.00 31.78 ? 306 LEU   A HD21 1 
ATOM   4649 H  HD22 . LEU   A 1 306 ? 6.410   -17.344 -5.065  1.00 31.78 ? 306 LEU   A HD22 1 
ATOM   4650 H  HD23 . LEU   A 1 306 ? 6.983   -16.930 -3.643  1.00 31.78 ? 306 LEU   A HD23 1 
ATOM   4651 N  N    . SER   A 1 307 ? 7.078   -12.019 -5.557  1.00 22.45 ? 307 SER   A N    1 
ATOM   4652 C  CA   . SER   A 1 307 ? 7.718   -11.098 -6.489  1.00 23.95 ? 307 SER   A CA   1 
ATOM   4653 C  C    . SER   A 1 307 ? 9.116   -10.724 -6.023  1.00 24.43 ? 307 SER   A C    1 
ATOM   4654 O  O    . SER   A 1 307 ? 10.052  -10.645 -6.827  1.00 25.14 ? 307 SER   A O    1 
ATOM   4655 C  CB   . SER   A 1 307 ? 6.887   -9.829  -6.667  1.00 25.34 ? 307 SER   A CB   1 
ATOM   4656 O  OG   . SER   A 1 307 ? 5.627   -10.124 -7.221  1.00 25.15 ? 307 SER   A OG   1 
ATOM   4657 H  H    . SER   A 1 307 ? 6.370   -11.715 -5.174  1.00 26.96 ? 307 SER   A H    1 
ATOM   4658 H  HA   . SER   A 1 307 ? 7.796   -11.529 -7.355  1.00 28.76 ? 307 SER   A HA   1 
ATOM   4659 H  HB2  . SER   A 1 307 ? 6.761   -9.411  -5.801  1.00 30.43 ? 307 SER   A HB2  1 
ATOM   4660 H  HB3  . SER   A 1 307 ? 7.359   -9.225  -7.261  1.00 30.43 ? 307 SER   A HB3  1 
ATOM   4661 H  HG   . SER   A 1 307 ? 5.181   -9.418  -7.313  1.00 30.20 ? 307 SER   A HG   1 
ATOM   4662 N  N    . ALA   A 1 308 ? 9.272   -10.454 -4.727  1.00 21.58 ? 308 ALA   A N    1 
ATOM   4663 C  CA   . ALA   A 1 308 ? 10.582  -10.121 -4.191  1.00 21.36 ? 308 ALA   A CA   1 
ATOM   4664 C  C    . ALA   A 1 308 ? 11.560  -11.273 -4.392  1.00 24.28 ? 308 ALA   A C    1 
ATOM   4665 O  O    . ALA   A 1 308 ? 12.703  -11.070 -4.814  1.00 24.16 ? 308 ALA   A O    1 
ATOM   4666 C  CB   . ALA   A 1 308 ? 10.456  -9.767  -2.710  1.00 23.57 ? 308 ALA   A CB   1 
ATOM   4667 H  H    . ALA   A 1 308 ? 8.639   -10.458 -4.145  1.00 25.92 ? 308 ALA   A H    1 
ATOM   4668 H  HA   . ALA   A 1 308 ? 10.929  -9.345  -4.659  1.00 25.65 ? 308 ALA   A HA   1 
ATOM   4669 H  HB1  . ALA   A 1 308 ? 11.339  -9.584  -2.355  1.00 28.30 ? 308 ALA   A HB1  1 
ATOM   4670 H  HB2  . ALA   A 1 308 ? 9.892   -8.983  -2.619  1.00 28.30 ? 308 ALA   A HB2  1 
ATOM   4671 H  HB3  . ALA   A 1 308 ? 10.060  -10.517 -2.239  1.00 28.30 ? 308 ALA   A HB3  1 
ATOM   4672 N  N    . ALA   A 1 309 ? 11.118  -12.498 -4.101  1.00 21.86 ? 309 ALA   A N    1 
ATOM   4673 C  CA   . ALA   A 1 309 ? 12.002  -13.649 -4.259  1.00 25.76 ? 309 ALA   A CA   1 
ATOM   4674 C  C    . ALA   A 1 309 ? 12.395  -13.832 -5.719  1.00 26.59 ? 309 ALA   A C    1 
ATOM   4675 O  O    . ALA   A 1 309 ? 13.539  -14.194 -6.024  1.00 25.11 ? 309 ALA   A O    1 
ATOM   4676 C  CB   . ALA   A 1 309 ? 11.330  -14.914 -3.727  1.00 23.01 ? 309 ALA   A CB   1 
ATOM   4677 H  H    . ALA   A 1 309 ? 10.328  -12.685 -3.817  1.00 26.25 ? 309 ALA   A H    1 
ATOM   4678 H  HA   . ALA   A 1 309 ? 12.812  -13.500 -3.746  1.00 30.93 ? 309 ALA   A HA   1 
ATOM   4679 H  HB1  . ALA   A 1 309 ? 11.928  -15.667 -3.854  1.00 27.63 ? 309 ALA   A HB1  1 
ATOM   4680 H  HB2  . ALA   A 1 309 ? 11.144  -14.793 -2.783  1.00 27.63 ? 309 ALA   A HB2  1 
ATOM   4681 H  HB3  . ALA   A 1 309 ? 10.503  -15.060 -4.212  1.00 27.63 ? 309 ALA   A HB3  1 
ATOM   4682 N  N    . LYS   A 1 310 ? 11.456  -13.589 -6.635  1.00 26.45 ? 310 LYS   A N    1 
ATOM   4683 C  CA   . LYS   A 1 310 ? 11.782  -13.678 -8.052  1.00 25.94 ? 310 LYS   A CA   1 
ATOM   4684 C  C    . LYS   A 1 310 ? 12.854  -12.660 -8.416  1.00 26.83 ? 310 LYS   A C    1 
ATOM   4685 O  O    . LYS   A 1 310 ? 13.799  -12.983 -9.147  1.00 28.96 ? 310 LYS   A O    1 
ATOM   4686 C  CB   . LYS   A 1 310 ? 10.519  -13.491 -8.892  1.00 27.36 ? 310 LYS   A CB   1 
ATOM   4687 C  CG   . LYS   A 1 310 ? 10.763  -13.553 -10.388 1.00 31.76 ? 310 LYS   A CG   1 
ATOM   4688 C  CD   . LYS   A 1 310 ? 9.472   -13.575 -11.190 1.00 40.99 ? 310 LYS   A CD   1 
ATOM   4689 C  CE   . LYS   A 1 310 ? 8.946   -12.165 -11.439 1.00 57.57 ? 310 LYS   A CE   1 
ATOM   4690 N  NZ   . LYS   A 1 310 ? 9.252   -11.658 -12.809 1.00 55.07 ? 310 LYS   A NZ   1 
ATOM   4691 H  H    . LYS   A 1 310 ? 10.641  -13.375 -6.464  1.00 31.76 ? 310 LYS   A H    1 
ATOM   4692 H  HA   . LYS   A 1 310 ? 12.135  -14.562 -8.238  1.00 31.15 ? 310 LYS   A HA   1 
ATOM   4693 H  HB2  . LYS   A 1 310 ? 9.887   -14.191 -8.665  1.00 32.85 ? 310 LYS   A HB2  1 
ATOM   4694 H  HB3  . LYS   A 1 310 ? 10.135  -12.623 -8.690  1.00 32.85 ? 310 LYS   A HB3  1 
ATOM   4695 H  HG2  . LYS   A 1 310 ? 11.275  -12.775 -10.660 1.00 38.13 ? 310 LYS   A HG2  1 
ATOM   4696 H  HG3  . LYS   A 1 310 ? 11.256  -14.363 -10.593 1.00 38.13 ? 310 LYS   A HG3  1 
ATOM   4697 H  HD2  . LYS   A 1 310 ? 9.636   -13.994 -12.049 1.00 49.20 ? 310 LYS   A HD2  1 
ATOM   4698 H  HD3  . LYS   A 1 310 ? 8.797   -14.069 -10.699 1.00 49.20 ? 310 LYS   A HD3  1 
ATOM   4699 H  HE2  . LYS   A 1 310 ? 7.986   -12.143 -11.304 1.00 69.10 ? 310 LYS   A HE2  1 
ATOM   4700 H  HE3  . LYS   A 1 310 ? 9.390   -11.587 -10.817 1.00 69.10 ? 310 LYS   A HE3  1 
ATOM   4701 H  HZ1  . LYS   A 1 310 ? 8.927   -10.835 -12.908 1.00 66.10 ? 310 LYS   A HZ1  1 
ATOM   4702 H  HZ2  . LYS   A 1 310 ? 10.133  -11.639 -12.936 1.00 66.10 ? 310 LYS   A HZ2  1 
ATOM   4703 H  HZ3  . LYS   A 1 310 ? 8.883   -12.190 -13.419 1.00 66.10 ? 310 LYS   A HZ3  1 
ATOM   4704 N  N    . ASP   A 1 311 ? 12.752  -11.435 -7.880  1.00 24.66 ? 311 ASP   A N    1 
ATOM   4705 C  CA   . ASP   A 1 311 ? 13.758  -10.416 -8.168  1.00 26.75 ? 311 ASP   A CA   1 
ATOM   4706 C  C    . ASP   A 1 311 ? 15.132  -10.850 -7.671  1.00 26.11 ? 311 ASP   A C    1 
ATOM   4707 O  O    . ASP   A 1 311 ? 16.157  -10.559 -8.302  1.00 29.64 ? 311 ASP   A O    1 
ATOM   4708 C  CB   . ASP   A 1 311 ? 13.391  -9.079  -7.517  1.00 26.34 ? 311 ASP   A CB   1 
ATOM   4709 C  CG   . ASP   A 1 311 ? 12.136  -8.444  -8.102  1.00 28.22 ? 311 ASP   A CG   1 
ATOM   4710 O  OD1  . ASP   A 1 311 ? 11.763  -8.739  -9.258  1.00 30.57 ? 311 ASP   A OD1  1 
ATOM   4711 O  OD2  . ASP   A 1 311 ? 11.546  -7.594  -7.402  1.00 31.74 ? 311 ASP   A OD2  1 
ATOM   4712 H  H    . ASP   A 1 311 ? 12.120  -11.177 -7.357  1.00 29.61 ? 311 ASP   A H    1 
ATOM   4713 H  HA   . ASP   A 1 311 ? 13.811  -10.282 -9.127  1.00 32.12 ? 311 ASP   A HA   1 
ATOM   4714 H  HB2  . ASP   A 1 311 ? 13.239  -9.222  -6.570  1.00 31.63 ? 311 ASP   A HB2  1 
ATOM   4715 H  HB3  . ASP   A 1 311 ? 14.125  -8.458  -7.644  1.00 31.63 ? 311 ASP   A HB3  1 
ATOM   4716 N  N    . LEU   A 1 312 ? 15.171  -11.538 -6.531  1.00 24.85 ? 312 LEU   A N    1 
ATOM   4717 C  CA   . LEU   A 1 312 ? 16.409  -11.945 -5.885  1.00 25.30 ? 312 LEU   A CA   1 
ATOM   4718 C  C    . LEU   A 1 312 ? 16.960  -13.262 -6.420  1.00 26.56 ? 312 LEU   A C    1 
ATOM   4719 O  O    . LEU   A 1 312 ? 18.112  -13.593 -6.118  1.00 30.17 ? 312 LEU   A O    1 
ATOM   4720 C  CB   . LEU   A 1 312 ? 16.164  -12.079 -4.381  1.00 25.46 ? 312 LEU   A CB   1 
ATOM   4721 C  CG   . LEU   A 1 312 ? 15.833  -10.808 -3.595  1.00 23.67 ? 312 LEU   A CG   1 
ATOM   4722 C  CD1  . LEU   A 1 312 ? 15.239  -11.133 -2.245  1.00 25.58 ? 312 LEU   A CD1  1 
ATOM   4723 C  CD2  . LEU   A 1 312 ? 17.082  -9.957  -3.433  1.00 31.54 ? 312 LEU   A CD2  1 
ATOM   4724 H  H    . LEU   A 1 312 ? 14.468  -11.786 -6.102  1.00 29.84 ? 312 LEU   A H    1 
ATOM   4725 H  HA   . LEU   A 1 312 ? 17.080  -11.259 -6.023  1.00 30.38 ? 312 LEU   A HA   1 
ATOM   4726 H  HB2  . LEU   A 1 312 ? 15.423  -12.692 -4.253  1.00 30.57 ? 312 LEU   A HB2  1 
ATOM   4727 H  HB3  . LEU   A 1 312 ? 16.962  -12.459 -3.981  1.00 30.57 ? 312 LEU   A HB3  1 
ATOM   4728 H  HG   . LEU   A 1 312 ? 15.181  -10.293 -4.094  1.00 28.43 ? 312 LEU   A HG   1 
ATOM   4729 H  HD11 . LEU   A 1 312 ? 15.048  -10.305 -1.777  1.00 30.72 ? 312 LEU   A HD11 1 
ATOM   4730 H  HD12 . LEU   A 1 312 ? 14.420  -11.637 -2.374  1.00 30.72 ? 312 LEU   A HD12 1 
ATOM   4731 H  HD13 . LEU   A 1 312 ? 15.877  -11.660 -1.739  1.00 30.72 ? 312 LEU   A HD13 1 
ATOM   4732 H  HD21 . LEU   A 1 312 ? 16.858  -9.163  -2.923  1.00 37.86 ? 312 LEU   A HD21 1 
ATOM   4733 H  HD22 . LEU   A 1 312 ? 17.756  -10.473 -2.963  1.00 37.86 ? 312 LEU   A HD22 1 
ATOM   4734 H  HD23 . LEU   A 1 312 ? 17.409  -9.706  -4.311  1.00 37.86 ? 312 LEU   A HD23 1 
ATOM   4735 N  N    . GLY   A 1 313 ? 16.175  -14.020 -7.180  1.00 26.09 ? 313 GLY   A N    1 
ATOM   4736 C  CA   . GLY   A 1 313 ? 16.595  -15.324 -7.654  1.00 31.50 ? 313 GLY   A CA   1 
ATOM   4737 C  C    . GLY   A 1 313 ? 16.395  -16.461 -6.679  1.00 30.28 ? 313 GLY   A C    1 
ATOM   4738 O  O    . GLY   A 1 313 ? 16.920  -17.559 -6.908  1.00 33.94 ? 313 GLY   A O    1 
ATOM   4739 H  H    . GLY   A 1 313 ? 15.385  -13.795 -7.436  1.00 31.33 ? 313 GLY   A H    1 
ATOM   4740 H  HA2  . GLY   A 1 313 ? 16.104  -15.536 -8.463  1.00 37.82 ? 313 GLY   A HA2  1 
ATOM   4741 H  HA3  . GLY   A 1 313 ? 17.538  -15.287 -7.879  1.00 37.82 ? 313 GLY   A HA3  1 
ATOM   4742 N  N    . TYR   A 1 314 ? 15.650  -16.239 -5.604  1.00 24.67 ? 314 TYR   A N    1 
ATOM   4743 C  CA   . TYR   A 1 314 ? 15.453  -17.233 -4.566  1.00 24.52 ? 314 TYR   A CA   1 
ATOM   4744 C  C    . TYR   A 1 314 ? 14.376  -18.237 -4.990  1.00 29.30 ? 314 TYR   A C    1 
ATOM   4745 O  O    . TYR   A 1 314 ? 13.518  -17.941 -5.828  1.00 28.27 ? 314 TYR   A O    1 
ATOM   4746 C  CB   . TYR   A 1 314 ? 15.078  -16.508 -3.278  1.00 24.70 ? 314 TYR   A CB   1 
ATOM   4747 C  CG   . TYR   A 1 314 ? 16.198  -15.699 -2.641  1.00 24.88 ? 314 TYR   A CG   1 
ATOM   4748 C  CD1  . TYR   A 1 314 ? 17.403  -15.455 -3.302  1.00 26.01 ? 314 TYR   A CD1  1 
ATOM   4749 C  CD2  . TYR   A 1 314 ? 16.032  -15.163 -1.378  1.00 26.42 ? 314 TYR   A CD2  1 
ATOM   4750 C  CE1  . TYR   A 1 314 ? 18.413  -14.715 -2.695  1.00 31.89 ? 314 TYR   A CE1  1 
ATOM   4751 C  CE2  . TYR   A 1 314 ? 17.023  -14.428 -0.776  1.00 25.75 ? 314 TYR   A CE2  1 
ATOM   4752 C  CZ   . TYR   A 1 314 ? 18.209  -14.206 -1.436  1.00 29.10 ? 314 TYR   A CZ   1 
ATOM   4753 O  OH   . TYR   A 1 314 ? 19.189  -13.467 -0.813  1.00 28.59 ? 314 TYR   A OH   1 
ATOM   4754 H  H    . TYR   A 1 314 ? 15.238  -15.500 -5.452  1.00 29.62 ? 314 TYR   A H    1 
ATOM   4755 H  HA   . TYR   A 1 314 ? 16.280  -17.718 -4.419  1.00 29.45 ? 314 TYR   A HA   1 
ATOM   4756 H  HB2  . TYR   A 1 314 ? 14.349  -15.897 -3.469  1.00 29.65 ? 314 TYR   A HB2  1 
ATOM   4757 H  HB3  . TYR   A 1 314 ? 14.787  -17.166 -2.628  1.00 29.65 ? 314 TYR   A HB3  1 
ATOM   4758 H  HD1  . TYR   A 1 314 ? 17.541  -15.804 -4.152  1.00 31.23 ? 314 TYR   A HD1  1 
ATOM   4759 H  HD2  . TYR   A 1 314 ? 15.235  -15.311 -0.922  1.00 31.73 ? 314 TYR   A HD2  1 
ATOM   4760 H  HE1  . TYR   A 1 314 ? 19.215  -14.561 -3.140  1.00 38.29 ? 314 TYR   A HE1  1 
ATOM   4761 H  HE2  . TYR   A 1 314 ? 16.893  -14.081 0.077   1.00 30.92 ? 314 TYR   A HE2  1 
ATOM   4762 H  HH   . TYR   A 1 314 ? 18.926  -13.223 -0.054  1.00 34.32 ? 314 TYR   A HH   1 
ATOM   4763 N  N    . ASN   A 1 315 ? 14.448  -19.443 -4.419  1.00 26.76 ? 315 ASN   A N    1 
ATOM   4764 C  CA   . ASN   A 1 315 ? 13.512  -20.511 -4.768  1.00 25.80 ? 315 ASN   A CA   1 
ATOM   4765 C  C    . ASN   A 1 315 ? 12.081  -20.172 -4.402  1.00 24.13 ? 315 ASN   A C    1 
ATOM   4766 O  O    . ASN   A 1 315 ? 11.756  -19.982 -3.228  1.00 27.39 ? 315 ASN   A O    1 
ATOM   4767 C  CB   . ASN   A 1 315 ? 13.914  -21.818 -4.085  1.00 29.47 ? 315 ASN   A CB   1 
ATOM   4768 C  CG   . ASN   A 1 315 ? 13.224  -23.037 -4.695  1.00 30.61 ? 315 ASN   A CG   1 
ATOM   4769 O  OD1  . ASN   A 1 315 ? 12.122  -23.408 -4.265  1.00 28.49 ? 315 ASN   A OD1  1 
ATOM   4770 N  ND2  . ASN   A 1 315 ? 13.839  -23.648 -5.696  1.00 33.53 ? 315 ASN   A ND2  1 
ATOM   4771 H  H    . ASN   A 1 315 ? 15.030  -19.666 -3.827  1.00 32.13 ? 315 ASN   A H    1 
ATOM   4772 H  HA   . ASN   A 1 315 ? 13.546  -20.655 -5.727  1.00 30.98 ? 315 ASN   A HA   1 
ATOM   4773 H  HB2  . ASN   A 1 315 ? 14.867  -21.945 -4.188  1.00 35.39 ? 315 ASN   A HB2  1 
ATOM   4774 H  HB3  . ASN   A 1 315 ? 13.680  -21.774 -3.145  1.00 35.39 ? 315 ASN   A HB3  1 
ATOM   4775 H  HD21 . ASN   A 1 315 ? 13.480  -24.337 -6.065  1.00 40.25 ? 315 ASN   A HD21 1 
ATOM   4776 H  HD22 . ASN   A 1 315 ? 14.602  -23.361 -5.971  1.00 40.25 ? 315 ASN   A HD22 1 
ATOM   4777 N  N    . LEU   A 1 316 ? 11.206  -20.166 -5.403  1.00 26.58 ? 316 LEU   A N    1 
ATOM   4778 C  CA   . LEU   A 1 316 ? 9.814   -19.816 -5.155  1.00 25.51 ? 316 LEU   A CA   1 
ATOM   4779 C  C    . LEU   A 1 316 ? 9.029   -20.984 -4.565  1.00 24.84 ? 316 LEU   A C    1 
ATOM   4780 O  O    . LEU   A 1 316 ? 8.056   -20.763 -3.836  1.00 26.19 ? 316 LEU   A O    1 
ATOM   4781 C  CB   . LEU   A 1 316 ? 9.163   -19.356 -6.457  1.00 26.53 ? 316 LEU   A CB   1 
ATOM   4782 C  CG   . LEU   A 1 316 ? 9.779   -18.120 -7.111  1.00 30.15 ? 316 LEU   A CG   1 
ATOM   4783 C  CD1  . LEU   A 1 316 ? 8.894   -17.609 -8.256  1.00 39.50 ? 316 LEU   A CD1  1 
ATOM   4784 C  CD2  . LEU   A 1 316 ? 10.061  -17.001 -6.120  1.00 32.39 ? 316 LEU   A CD2  1 
ATOM   4785 H  H    . LEU   A 1 316 ? 11.389  -20.357 -6.221  1.00 31.92 ? 316 LEU   A H    1 
ATOM   4786 H  HA   . LEU   A 1 316 ? 9.778   -19.085 -4.519  1.00 30.63 ? 316 LEU   A HA   1 
ATOM   4787 H  HB2  . LEU   A 1 316 ? 9.219   -20.081 -7.099  1.00 31.85 ? 316 LEU   A HB2  1 
ATOM   4788 H  HB3  . LEU   A 1 316 ? 8.231   -19.155 -6.278  1.00 31.85 ? 316 LEU   A HB3  1 
ATOM   4789 H  HG   . LEU   A 1 316 ? 10.629  -18.377 -7.500  1.00 36.20 ? 316 LEU   A HG   1 
ATOM   4790 H  HD11 . LEU   A 1 316 ? 9.314   -16.831 -8.656  1.00 47.42 ? 316 LEU   A HD11 1 
ATOM   4791 H  HD12 . LEU   A 1 316 ? 8.799   -18.311 -8.918  1.00 47.42 ? 316 LEU   A HD12 1 
ATOM   4792 H  HD13 . LEU   A 1 316 ? 8.024   -17.370 -7.899  1.00 47.42 ? 316 LEU   A HD13 1 
ATOM   4793 H  HD21 . LEU   A 1 316 ? 10.306  -16.200 -6.610  1.00 38.88 ? 316 LEU   A HD21 1 
ATOM   4794 H  HD22 . LEU   A 1 316 ? 9.262   -16.836 -5.595  1.00 38.88 ? 316 LEU   A HD22 1 
ATOM   4795 H  HD23 . LEU   A 1 316 ? 10.790  -17.269 -5.539  1.00 38.88 ? 316 LEU   A HD23 1 
ATOM   4796 N  N    . ASP   A 1 317 ? 9.410   -22.227 -4.872  1.00 25.25 ? 317 ASP   A N    1 
ATOM   4797 C  CA   . ASP   A 1 317 ? 8.651   -23.353 -4.336  1.00 24.60 ? 317 ASP   A CA   1 
ATOM   4798 C  C    . ASP   A 1 317 ? 8.807   -23.442 -2.828  1.00 27.52 ? 317 ASP   A C    1 
ATOM   4799 O  O    . ASP   A 1 317 ? 7.860   -23.815 -2.125  1.00 27.17 ? 317 ASP   A O    1 
ATOM   4800 C  CB   . ASP   A 1 317 ? 9.090   -24.656 -4.999  1.00 25.99 ? 317 ASP   A CB   1 
ATOM   4801 C  CG   . ASP   A 1 317 ? 8.799   -24.676 -6.481  1.00 29.25 ? 317 ASP   A CG   1 
ATOM   4802 O  OD1  . ASP   A 1 317 ? 7.627   -24.461 -6.865  1.00 27.06 ? 317 ASP   A OD1  1 
ATOM   4803 O  OD2  . ASP   A 1 317 ? 9.744   -24.906 -7.264  1.00 34.75 ? 317 ASP   A OD2  1 
ATOM   4804 H  H    . ASP   A 1 317 ? 10.079  -22.438 -5.370  1.00 30.31 ? 317 ASP   A H    1 
ATOM   4805 H  HA   . ASP   A 1 317 ? 7.710   -23.220 -4.532  1.00 29.53 ? 317 ASP   A HA   1 
ATOM   4806 H  HB2  . ASP   A 1 317 ? 10.046  -24.767 -4.879  1.00 31.21 ? 317 ASP   A HB2  1 
ATOM   4807 H  HB3  . ASP   A 1 317 ? 8.615   -25.396 -4.589  1.00 31.21 ? 317 ASP   A HB3  1 
ATOM   4808 N  N    . ASP   A 1 318 ? 9.981   -23.081 -2.313  1.00 24.21 ? 318 ASP   A N    1 
ATOM   4809 C  CA   . ASP   A 1 318 ? 10.183  -23.131 -0.878  1.00 24.38 ? 318 ASP   A CA   1 
ATOM   4810 C  C    . ASP   A 1 318 ? 9.298   -22.092 -0.191  1.00 27.62 ? 318 ASP   A C    1 
ATOM   4811 O  O    . ASP   A 1 318 ? 8.803   -22.327 0.918   1.00 27.63 ? 318 ASP   A O    1 
ATOM   4812 C  CB   . ASP   A 1 318 ? 11.645  -22.858 -0.520  1.00 25.63 ? 318 ASP   A CB   1 
ATOM   4813 C  CG   . ASP   A 1 318 ? 12.557  -24.007 -0.908  1.00 32.57 ? 318 ASP   A CG   1 
ATOM   4814 O  OD1  . ASP   A 1 318 ? 12.159  -25.177 -0.749  1.00 32.04 ? 318 ASP   A OD1  1 
ATOM   4815 O  OD2  . ASP   A 1 318 ? 13.733  -23.723 -1.230  1.00 29.56 ? 318 ASP   A OD2  1 
ATOM   4816 H  H    . ASP   A 1 318 ? 10.660  -22.810 -2.766  1.00 29.08 ? 318 ASP   A H    1 
ATOM   4817 H  HA   . ASP   A 1 318 ? 9.942   -24.010 -0.546  1.00 29.28 ? 318 ASP   A HA   1 
ATOM   4818 H  HB2  . ASP   A 1 318 ? 11.944  -22.064 -0.990  1.00 30.77 ? 318 ASP   A HB2  1 
ATOM   4819 H  HB3  . ASP   A 1 318 ? 11.718  -22.726 0.438   1.00 30.77 ? 318 ASP   A HB3  1 
ATOM   4820 N  N    . ILE   A 1 319 ? 9.091   -20.949 -0.843  1.00 24.99 ? 319 ILE   A N    1 
ATOM   4821 C  CA   . ILE   A 1 319 ? 8.232   -19.907 -0.302  1.00 23.23 ? 319 ILE   A CA   1 
ATOM   4822 C  C    . ILE   A 1 319 ? 6.779   -20.350 -0.366  1.00 20.53 ? 319 ILE   A C    1 
ATOM   4823 O  O    . ILE   A 1 319 ? 6.030   -20.224 0.609   1.00 21.08 ? 319 ILE   A O    1 
ATOM   4824 C  CB   . ILE   A 1 319 ? 8.458   -18.604 -1.082  1.00 26.35 ? 319 ILE   A CB   1 
ATOM   4825 C  CG1  . ILE   A 1 319 ? 9.840   -18.052 -0.746  1.00 27.65 ? 319 ILE   A CG1  1 
ATOM   4826 C  CG2  . ILE   A 1 319 ? 7.395   -17.565 -0.755  1.00 27.82 ? 319 ILE   A CG2  1 
ATOM   4827 C  CD1  . ILE   A 1 319 ? 10.382  -17.199 -1.813  1.00 30.30 ? 319 ILE   A CD1  1 
ATOM   4828 H  H    . ILE   A 1 319 ? 9.440   -20.755 -1.604  1.00 30.01 ? 319 ILE   A H    1 
ATOM   4829 H  HA   . ILE   A 1 319 ? 8.463   -19.750 0.627   1.00 27.90 ? 319 ILE   A HA   1 
ATOM   4830 H  HB   . ILE   A 1 319 ? 8.422   -18.799 -2.032  1.00 31.64 ? 319 ILE   A HB   1 
ATOM   4831 H  HG12 . ILE   A 1 319 ? 9.779   -17.519 0.062   1.00 33.20 ? 319 ILE   A HG12 1 
ATOM   4832 H  HG13 . ILE   A 1 319 ? 10.455  -18.790 -0.611  1.00 33.20 ? 319 ILE   A HG13 1 
ATOM   4833 H  HG21 . ILE   A 1 319 ? 7.705   -16.694 -1.047  1.00 33.40 ? 319 ILE   A HG21 1 
ATOM   4834 H  HG22 . ILE   A 1 319 ? 6.574   -17.793 -1.217  1.00 33.40 ? 319 ILE   A HG22 1 
ATOM   4835 H  HG23 . ILE   A 1 319 ? 7.247   -17.557 0.204   1.00 33.40 ? 319 ILE   A HG23 1 
ATOM   4836 H  HD11 . ILE   A 1 319 ? 11.253  -16.869 -1.541  1.00 36.38 ? 319 ILE   A HD11 1 
ATOM   4837 H  HD12 . ILE   A 1 319 ? 10.465  -17.724 -2.625  1.00 36.38 ? 319 ILE   A HD12 1 
ATOM   4838 H  HD13 . ILE   A 1 319 ? 9.777   -16.455 -1.960  1.00 36.38 ? 319 ILE   A HD13 1 
ATOM   4839 N  N    . LYS   A 1 320 ? 6.361   -20.888 -1.516  1.00 20.61 ? 320 LYS   A N    1 
ATOM   4840 C  CA   . LYS   A 1 320 ? 4.993   -21.363 -1.675  1.00 23.71 ? 320 LYS   A CA   1 
ATOM   4841 C  C    . LYS   A 1 320 ? 4.665   -22.432 -0.638  1.00 22.35 ? 320 LYS   A C    1 
ATOM   4842 O  O    . LYS   A 1 320 ? 3.576   -22.429 -0.051  1.00 21.90 ? 320 LYS   A O    1 
ATOM   4843 C  CB   . LYS   A 1 320 ? 4.824   -21.908 -3.095  1.00 24.56 ? 320 LYS   A CB   1 
ATOM   4844 C  CG   . LYS   A 1 320 ? 4.669   -20.814 -4.153  1.00 24.42 ? 320 LYS   A CG   1 
ATOM   4845 C  CD   . LYS   A 1 320 ? 4.726   -21.361 -5.583  1.00 28.08 ? 320 LYS   A CD   1 
ATOM   4846 C  CE   . LYS   A 1 320 ? 4.716   -20.200 -6.584  1.00 27.80 ? 320 LYS   A CE   1 
ATOM   4847 N  NZ   . LYS   A 1 320 ? 5.103   -20.593 -7.964  1.00 31.83 ? 320 LYS   A NZ   1 
ATOM   4848 H  H    . LYS   A 1 320 ? 6.852   -20.987 -2.215  1.00 24.75 ? 320 LYS   A H    1 
ATOM   4849 H  HA   . LYS   A 1 320 ? 4.378   -20.622 -1.556  1.00 28.47 ? 320 LYS   A HA   1 
ATOM   4850 H  HB2  . LYS   A 1 320 ? 5.609   -22.430 -3.323  1.00 29.49 ? 320 LYS   A HB2  1 
ATOM   4851 H  HB3  . LYS   A 1 320 ? 4.036   -22.471 -3.125  1.00 29.49 ? 320 LYS   A HB3  1 
ATOM   4852 H  HG2  . LYS   A 1 320 ? 3.813   -20.375 -4.032  1.00 29.32 ? 320 LYS   A HG2  1 
ATOM   4853 H  HG3  . LYS   A 1 320 ? 5.389   -20.172 -4.049  1.00 29.32 ? 320 LYS   A HG3  1 
ATOM   4854 H  HD2  . LYS   A 1 320 ? 5.544   -21.868 -5.705  1.00 33.72 ? 320 LYS   A HD2  1 
ATOM   4855 H  HD3  . LYS   A 1 320 ? 3.950   -21.919 -5.749  1.00 33.72 ? 320 LYS   A HD3  1 
ATOM   4856 H  HE2  . LYS   A 1 320 ? 3.824   -19.821 -6.617  1.00 33.37 ? 320 LYS   A HE2  1 
ATOM   4857 H  HE3  . LYS   A 1 320 ? 5.346   -19.526 -6.284  1.00 33.37 ? 320 LYS   A HE3  1 
ATOM   4858 H  HZ1  . LYS   A 1 320 ? 4.740   -20.032 -8.552  1.00 38.21 ? 320 LYS   A HZ1  1 
ATOM   4859 H  HZ2  . LYS   A 1 320 ? 5.989   -20.569 -8.050  1.00 38.21 ? 320 LYS   A HZ2  1 
ATOM   4860 H  HZ3  . LYS   A 1 320 ? 4.819   -21.418 -8.138  1.00 38.21 ? 320 LYS   A HZ3  1 
ATOM   4861 N  N    . LYS   A 1 321 ? 5.594   -23.360 -0.397  1.00 23.31 ? 321 LYS   A N    1 
ATOM   4862 C  CA   . LYS   A 1 321 ? 5.333   -24.387 0.603   1.00 23.56 ? 321 LYS   A CA   1 
ATOM   4863 C  C    . LYS   A 1 321 ? 5.149   -23.745 1.974   1.00 23.48 ? 321 LYS   A C    1 
ATOM   4864 O  O    . LYS   A 1 321 ? 4.232   -24.113 2.718   1.00 24.08 ? 321 LYS   A O    1 
ATOM   4865 C  CB   . LYS   A 1 321 ? 6.464   -25.413 0.613   1.00 25.03 ? 321 LYS   A CB   1 
ATOM   4866 C  CG   . LYS   A 1 321 ? 6.418   -26.371 1.794   1.00 29.02 ? 321 LYS   A CG   1 
ATOM   4867 C  CD   . LYS   A 1 321 ? 7.488   -27.455 1.683   1.00 41.25 ? 321 LYS   A CD   1 
ATOM   4868 C  CE   . LYS   A 1 321 ? 7.431   -28.415 2.869   1.00 49.79 ? 321 LYS   A CE   1 
ATOM   4869 N  NZ   . LYS   A 1 321 ? 8.080   -27.857 4.092   1.00 49.00 ? 321 LYS   A NZ   1 
ATOM   4870 H  H    . LYS   A 1 321 ? 6.359   -23.414 -0.787  1.00 27.99 ? 321 LYS   A H    1 
ATOM   4871 H  HA   . LYS   A 1 321 ? 4.511   -24.849 0.375   1.00 28.29 ? 321 LYS   A HA   1 
ATOM   4872 H  HB2  . LYS   A 1 321 ? 6.413   -25.941 -0.199  1.00 30.05 ? 321 LYS   A HB2  1 
ATOM   4873 H  HB3  . LYS   A 1 321 ? 7.312   -24.943 0.646   1.00 30.05 ? 321 LYS   A HB3  1 
ATOM   4874 H  HG2  . LYS   A 1 321 ? 6.577   -25.880 2.615   1.00 34.85 ? 321 LYS   A HG2  1 
ATOM   4875 H  HG3  . LYS   A 1 321 ? 5.550   -26.802 1.823   1.00 34.85 ? 321 LYS   A HG3  1 
ATOM   4876 H  HD2  . LYS   A 1 321 ? 7.344   -27.965 0.871   1.00 49.52 ? 321 LYS   A HD2  1 
ATOM   4877 H  HD3  . LYS   A 1 321 ? 8.365   -27.040 1.669   1.00 49.52 ? 321 LYS   A HD3  1 
ATOM   4878 H  HE2  . LYS   A 1 321 ? 6.503   -28.602 3.080   1.00 59.76 ? 321 LYS   A HE2  1 
ATOM   4879 H  HE3  . LYS   A 1 321 ? 7.890   -29.236 2.634   1.00 59.76 ? 321 LYS   A HE3  1 
ATOM   4880 H  HZ1  . LYS   A 1 321 ? 8.027   -28.444 4.759   1.00 58.82 ? 321 LYS   A HZ1  1 
ATOM   4881 H  HZ2  . LYS   A 1 321 ? 8.937   -27.682 3.928   1.00 58.82 ? 321 LYS   A HZ2  1 
ATOM   4882 H  HZ3  . LYS   A 1 321 ? 7.673   -27.104 4.336   1.00 58.82 ? 321 LYS   A HZ3  1 
ATOM   4883 N  N    . SER   A 1 322 ? 5.972   -22.741 2.294   1.00 21.95 ? 322 SER   A N    1 
ATOM   4884 C  CA   . SER   A 1 322 ? 5.861   -22.058 3.580   1.00 20.58 ? 322 SER   A CA   1 
ATOM   4885 C  C    . SER   A 1 322 ? 4.551   -21.285 3.683   1.00 21.66 ? 322 SER   A C    1 
ATOM   4886 O  O    . SER   A 1 322 ? 3.888   -21.309 4.731   1.00 21.55 ? 322 SER   A O    1 
ATOM   4887 C  CB   . SER   A 1 322 ? 7.048   -21.111 3.771   1.00 20.10 ? 322 SER   A CB   1 
ATOM   4888 O  OG   . SER   A 1 322 ? 8.290   -21.781 3.666   1.00 22.04 ? 322 SER   A OG   1 
ATOM   4889 H  H    . SER   A 1 322 ? 6.597   -22.441 1.786   1.00 26.36 ? 322 SER   A H    1 
ATOM   4890 H  HA   . SER   A 1 322 ? 5.881   -22.716 4.293   1.00 24.71 ? 322 SER   A HA   1 
ATOM   4891 H  HB2  . SER   A 1 322 ? 7.008   -20.421 3.091   1.00 24.13 ? 322 SER   A HB2  1 
ATOM   4892 H  HB3  . SER   A 1 322 ? 6.986   -20.707 4.651   1.00 24.13 ? 322 SER   A HB3  1 
ATOM   4893 H  HG   . SER   A 1 322 ? 8.364   -22.132 2.906   1.00 26.47 ? 322 SER   A HG   1 
ATOM   4894 N  N    . LEU   A 1 323 ? 4.168   -20.582 2.616   1.00 19.86 ? 323 LEU   A N    1 
ATOM   4895 C  CA   . LEU   A 1 323 ? 2.899   -19.867 2.611   1.00 19.87 ? 323 LEU   A CA   1 
ATOM   4896 C  C    . LEU   A 1 323 ? 1.730   -20.820 2.839   1.00 21.44 ? 323 LEU   A C    1 
ATOM   4897 O  O    . LEU   A 1 323 ? 0.804   -20.507 3.597   1.00 20.18 ? 323 LEU   A O    1 
ATOM   4898 C  CB   . LEU   A 1 323 ? 2.739   -19.119 1.289   1.00 22.11 ? 323 LEU   A CB   1 
ATOM   4899 C  CG   . LEU   A 1 323 ? 3.607   -17.875 1.082   1.00 19.97 ? 323 LEU   A CG   1 
ATOM   4900 C  CD1  . LEU   A 1 323 ? 3.530   -17.476 -0.409  1.00 21.85 ? 323 LEU   A CD1  1 
ATOM   4901 C  CD2  . LEU   A 1 323 ? 3.226   -16.705 1.969   1.00 21.06 ? 323 LEU   A CD2  1 
ATOM   4902 H  H    . LEU   A 1 323 ? 4.623   -20.505 1.890   1.00 23.85 ? 323 LEU   A H    1 
ATOM   4903 H  HA   . LEU   A 1 323 ? 2.900   -19.215 3.329   1.00 23.87 ? 323 LEU   A HA   1 
ATOM   4904 H  HB2  . LEU   A 1 323 ? 2.946   -19.734 0.568   1.00 26.55 ? 323 LEU   A HB2  1 
ATOM   4905 H  HB3  . LEU   A 1 323 ? 1.814   -18.837 1.212   1.00 26.55 ? 323 LEU   A HB3  1 
ATOM   4906 H  HG   . LEU   A 1 323 ? 4.529   -18.104 1.278   1.00 23.98 ? 323 LEU   A HG   1 
ATOM   4907 H  HD11 . LEU   A 1 323 ? 4.066   -16.680 -0.550  1.00 26.24 ? 323 LEU   A HD11 1 
ATOM   4908 H  HD12 . LEU   A 1 323 ? 3.872   -18.206 -0.949  1.00 26.24 ? 323 LEU   A HD12 1 
ATOM   4909 H  HD13 . LEU   A 1 323 ? 2.605   -17.298 -0.640  1.00 26.24 ? 323 LEU   A HD13 1 
ATOM   4910 H  HD21 . LEU   A 1 323 ? 3.805   -15.954 1.766   1.00 25.29 ? 323 LEU   A HD21 1 
ATOM   4911 H  HD22 . LEU   A 1 323 ? 2.302   -16.467 1.797   1.00 25.29 ? 323 LEU   A HD22 1 
ATOM   4912 H  HD23 . LEU   A 1 323 ? 3.333   -16.965 2.897   1.00 25.29 ? 323 LEU   A HD23 1 
ATOM   4913 N  N    . SER   A 1 324 ? 1.751   -21.991 2.191   1.00 21.39 ? 324 SER   A N    1 
ATOM   4914 C  CA   A SER   A 1 324 ? 0.644   -22.925 2.363   0.41 21.31 ? 324 SER   A CA   1 
ATOM   4915 C  CA   B SER   A 1 324 ? 0.660   -22.945 2.356   0.59 21.28 ? 324 SER   A CA   1 
ATOM   4916 C  C    . SER   A 1 324 ? 0.574   -23.430 3.800   1.00 22.62 ? 324 SER   A C    1 
ATOM   4917 O  O    . SER   A 1 324 ? -0.525  -23.673 4.317   1.00 21.99 ? 324 SER   A O    1 
ATOM   4918 C  CB   A SER   A 1 324 ? 0.773   -24.109 1.404   0.41 24.33 ? 324 SER   A CB   1 
ATOM   4919 C  CB   B SER   A 1 324 ? 0.851   -24.125 1.403   0.59 24.29 ? 324 SER   A CB   1 
ATOM   4920 O  OG   A SER   A 1 324 ? 2.099   -24.596 1.357   0.41 29.70 ? 324 SER   A OG   1 
ATOM   4921 O  OG   B SER   A 1 324 ? -0.349  -24.874 1.284   0.59 30.38 ? 324 SER   A OG   1 
ATOM   4922 H  H    A SER   A 1 324 ? 2.376   -22.258 1.663   0.41 25.69 ? 324 SER   A H    1 
ATOM   4923 H  H    B SER   A 1 324 ? 2.376   -22.249 1.660   0.59 25.69 ? 324 SER   A H    1 
ATOM   4924 H  HA   A SER   A 1 324 ? -0.188  -22.468 2.165   0.41 25.59 ? 324 SER   A HA   1 
ATOM   4925 H  HA   B SER   A 1 324 ? -0.178  -22.510 2.134   0.59 25.55 ? 324 SER   A HA   1 
ATOM   4926 H  HB2  A SER   A 1 324 ? 0.188   -24.822 1.705   0.41 29.21 ? 324 SER   A HB2  1 
ATOM   4927 H  HB2  B SER   A 1 324 ? 1.101   -23.788 0.529   0.59 29.17 ? 324 SER   A HB2  1 
ATOM   4928 H  HB3  A SER   A 1 324 ? 0.513   -23.822 0.515   0.41 29.21 ? 324 SER   A HB3  1 
ATOM   4929 H  HB3  B SER   A 1 324 ? 1.550   -24.701 1.749   0.59 29.17 ? 324 SER   A HB3  1 
ATOM   4930 H  HG   A SER   A 1 324 ? 2.339   -24.850 2.121   0.41 35.66 ? 324 SER   A HG   1 
ATOM   4931 H  HG   B SER   A 1 324 ? -0.578  -25.172 2.036   0.59 36.47 ? 324 SER   A HG   1 
ATOM   4932 N  N    . GLU   A 1 325 ? 1.722   -23.578 4.464   1.00 21.56 ? 325 GLU   A N    1 
ATOM   4933 C  CA   . GLU   A 1 325 ? 1.742   -24.053 5.843   1.00 21.38 ? 325 GLU   A CA   1 
ATOM   4934 C  C    . GLU   A 1 325 ? 1.128   -23.070 6.823   1.00 20.06 ? 325 GLU   A C    1 
ATOM   4935 O  O    . GLU   A 1 325 ? 0.693   -23.495 7.901   1.00 29.32 ? 325 GLU   A O    1 
ATOM   4936 C  CB   . GLU   A 1 325 ? 3.166   -24.402 6.258   1.00 24.36 ? 325 GLU   A CB   1 
ATOM   4937 C  CG   . GLU   A 1 325 ? 3.599   -25.730 5.678   1.00 30.97 ? 325 GLU   A CG   1 
ATOM   4938 C  CD   . GLU   A 1 325 ? 5.012   -26.077 6.044   1.00 40.42 ? 325 GLU   A CD   1 
ATOM   4939 O  OE1  . GLU   A 1 325 ? 5.461   -25.675 7.129   1.00 34.98 ? 325 GLU   A OE1  1 
ATOM   4940 O  OE2  . GLU   A 1 325 ? 5.682   -26.749 5.221   1.00 48.76 ? 325 GLU   A OE2  1 
ATOM   4941 H  H    . GLU   A 1 325 ? 2.500   -23.410 4.137   1.00 25.89 ? 325 GLU   A H    1 
ATOM   4942 H  HA   . GLU   A 1 325 ? 1.220   -24.869 5.890   1.00 25.67 ? 325 GLU   A HA   1 
ATOM   4943 H  HB2  . GLU   A 1 325 ? 3.771   -23.717 5.935   1.00 29.25 ? 325 GLU   A HB2  1 
ATOM   4944 H  HB3  . GLU   A 1 325 ? 3.212   -24.462 7.225   1.00 29.25 ? 325 GLU   A HB3  1 
ATOM   4945 H  HG2  . GLU   A 1 325 ? 3.019   -26.429 6.018   1.00 37.18 ? 325 GLU   A HG2  1 
ATOM   4946 H  HG3  . GLU   A 1 325 ? 3.540   -25.689 4.711   1.00 37.18 ? 325 GLU   A HG3  1 
ATOM   4947 N  N    . VAL   A 1 326 ? 1.058   -21.789 6.479   1.00 20.30 ? 326 VAL   A N    1 
ATOM   4948 C  CA   . VAL   A 1 326 ? 0.319   -20.828 7.290   1.00 20.54 ? 326 VAL   A CA   1 
ATOM   4949 C  C    . VAL   A 1 326 ? -1.032  -20.471 6.652   1.00 21.63 ? 326 VAL   A C    1 
ATOM   4950 O  O    . VAL   A 1 326 ? -1.630  -19.460 7.010   1.00 20.25 ? 326 VAL   A O    1 
ATOM   4951 C  CB   . VAL   A 1 326 ? 1.150   -19.565 7.586   1.00 19.99 ? 326 VAL   A CB   1 
ATOM   4952 C  CG1  . VAL   A 1 326 ? 2.385   -19.915 8.420   1.00 22.64 ? 326 VAL   A CG1  1 
ATOM   4953 C  CG2  . VAL   A 1 326 ? 1.545   -18.823 6.316   1.00 22.82 ? 326 VAL   A CG2  1 
ATOM   4954 H  H    . VAL   A 1 326 ? 1.429   -21.451 5.781   1.00 24.38 ? 326 VAL   A H    1 
ATOM   4955 H  HA   . VAL   A 1 326 ? 0.125   -21.239 8.146   1.00 24.66 ? 326 VAL   A HA   1 
ATOM   4956 H  HB   . VAL   A 1 326 ? 0.607   -18.961 8.115   1.00 24.00 ? 326 VAL   A HB   1 
ATOM   4957 H  HG11 . VAL   A 1 326 ? 2.883   -19.103 8.602   1.00 27.19 ? 326 VAL   A HG11 1 
ATOM   4958 H  HG12 . VAL   A 1 326 ? 2.098   -20.321 9.253   1.00 27.19 ? 326 VAL   A HG12 1 
ATOM   4959 H  HG13 . VAL   A 1 326 ? 2.937   -20.537 7.921   1.00 27.19 ? 326 VAL   A HG13 1 
ATOM   4960 H  HG21 . VAL   A 1 326 ? 2.075   -18.047 6.557   1.00 27.41 ? 326 VAL   A HG21 1 
ATOM   4961 H  HG22 . VAL   A 1 326 ? 2.065   -19.416 5.752   1.00 27.41 ? 326 VAL   A HG22 1 
ATOM   4962 H  HG23 . VAL   A 1 326 ? 0.742   -18.543 5.850   1.00 27.41 ? 326 VAL   A HG23 1 
ATOM   4963 N  N    . THR   A 1 327 ? -1.518  -21.300 5.715   1.00 20.13 ? 327 THR   A N    1 
ATOM   4964 C  CA   . THR   A 1 327 ? -2.824  -21.163 5.039   1.00 20.48 ? 327 THR   A CA   1 
ATOM   4965 C  C    . THR   A 1 327 ? -3.025  -19.812 4.351   1.00 19.43 ? 327 THR   A C    1 
ATOM   4966 O  O    . THR   A 1 327 ? -4.134  -19.270 4.309   1.00 24.36 ? 327 THR   A O    1 
ATOM   4967 C  CB   . THR   A 1 327 ? -3.990  -21.484 5.992   1.00 18.83 ? 327 THR   A CB   1 
ATOM   4968 O  OG1  . THR   A 1 327 ? -4.255  -20.386 6.876   1.00 21.06 ? 327 THR   A OG1  1 
ATOM   4969 C  CG2  . THR   A 1 327 ? -3.707  -22.744 6.788   1.00 19.54 ? 327 THR   A CG2  1 
ATOM   4970 H  H    . THR   A 1 327 ? -1.084  -21.989 5.439   1.00 24.18 ? 327 THR   A H    1 
ATOM   4971 H  HA   . THR   A 1 327 ? -2.855  -21.832 4.337   1.00 24.60 ? 327 THR   A HA   1 
ATOM   4972 H  HB   . THR   A 1 327 ? -4.784  -21.648 5.460   1.00 22.61 ? 327 THR   A HB   1 
ATOM   4973 H  HG1  . THR   A 1 327 ? -3.575  -20.220 7.340   1.00 25.29 ? 327 THR   A HG1  1 
ATOM   4974 H  HG21 . THR   A 1 327 ? -4.497  -23.005 7.286   1.00 23.46 ? 327 THR   A HG21 1 
ATOM   4975 H  HG22 . THR   A 1 327 ? -3.459  -23.465 6.189   1.00 23.46 ? 327 THR   A HG22 1 
ATOM   4976 H  HG23 . THR   A 1 327 ? -2.980  -22.588 7.411   1.00 23.46 ? 327 THR   A HG23 1 
ATOM   4977 N  N    . ILE   A 1 328 ? -1.961  -19.306 3.726   1.00 20.69 ? 328 ILE   A N    1 
ATOM   4978 C  CA   . ILE   A 1 328 ? -2.056  -18.143 2.850   1.00 19.07 ? 328 ILE   A CA   1 
ATOM   4979 C  C    . ILE   A 1 328 ? -2.306  -18.628 1.425   1.00 23.20 ? 328 ILE   A C    1 
ATOM   4980 O  O    . ILE   A 1 328 ? -1.660  -19.571 0.948   1.00 24.93 ? 328 ILE   A O    1 
ATOM   4981 C  CB   . ILE   A 1 328 ? -0.782  -17.285 2.940   1.00 21.00 ? 328 ILE   A CB   1 
ATOM   4982 C  CG1  . ILE   A 1 328 ? -0.826  -16.440 4.221   1.00 21.17 ? 328 ILE   A CG1  1 
ATOM   4983 C  CG2  . ILE   A 1 328 ? -0.637  -16.384 1.721   1.00 23.56 ? 328 ILE   A CG2  1 
ATOM   4984 C  CD1  . ILE   A 1 328 ? 0.508   -15.836 4.620   1.00 23.92 ? 328 ILE   A CD1  1 
ATOM   4985 H  H    . ILE   A 1 328 ? -1.165  -19.624 3.795   1.00 24.85 ? 328 ILE   A H    1 
ATOM   4986 H  HA   . ILE   A 1 328 ? -2.809  -17.596 3.122   1.00 22.91 ? 328 ILE   A HA   1 
ATOM   4987 H  HB   . ILE   A 1 328 ? -0.013  -17.875 2.983   1.00 25.21 ? 328 ILE   A HB   1 
ATOM   4988 H  HG12 . ILE   A 1 328 ? -1.452  -15.711 4.091   1.00 25.42 ? 328 ILE   A HG12 1 
ATOM   4989 H  HG13 . ILE   A 1 328 ? -1.126  -17.001 4.953   1.00 25.42 ? 328 ILE   A HG13 1 
ATOM   4990 H  HG21 . ILE   A 1 328 ? -0.027  -15.661 1.931   1.00 28.30 ? 328 ILE   A HG21 1 
ATOM   4991 H  HG22 . ILE   A 1 328 ? -0.287  -16.904 0.981   1.00 28.30 ? 328 ILE   A HG22 1 
ATOM   4992 H  HG23 . ILE   A 1 328 ? -1.507  -16.024 1.492   1.00 28.30 ? 328 ILE   A HG23 1 
ATOM   4993 H  HD11 . ILE   A 1 328 ? 0.421   -15.434 5.498   1.00 28.72 ? 328 ILE   A HD11 1 
ATOM   4994 H  HD12 . ILE   A 1 328 ? 1.177   -16.538 4.642   1.00 28.72 ? 328 ILE   A HD12 1 
ATOM   4995 H  HD13 . ILE   A 1 328 ? 0.758   -15.161 3.970   1.00 28.72 ? 328 ILE   A HD13 1 
ATOM   4996 N  N    . ASN   A 1 329 ? -3.260  -17.988 0.749   1.00 22.05 ? 329 ASN   A N    1 
ATOM   4997 C  CA   . ASN   A 1 329 ? -3.683  -18.364 -0.600  1.00 26.51 ? 329 ASN   A CA   1 
ATOM   4998 C  C    . ASN   A 1 329 ? -2.811  -17.588 -1.581  1.00 27.15 ? 329 ASN   A C    1 
ATOM   4999 O  O    . ASN   A 1 329 ? -3.034  -16.400 -1.817  1.00 30.60 ? 329 ASN   A O    1 
ATOM   5000 C  CB   . ASN   A 1 329 ? -5.163  -18.042 -0.792  1.00 24.80 ? 329 ASN   A CB   1 
ATOM   5001 C  CG   . ASN   A 1 329 ? -5.647  -18.265 -2.217  1.00 37.91 ? 329 ASN   A CG   1 
ATOM   5002 O  OD1  . ASN   A 1 329 ? -4.864  -18.576 -3.110  1.00 34.94 ? 329 ASN   A OD1  1 
ATOM   5003 N  ND2  . ASN   A 1 329 ? -6.947  -18.083 -2.434  1.00 45.27 ? 329 ASN   A ND2  1 
ATOM   5004 H  H    . ASN   A 1 329 ? -3.690  -17.312 1.062   1.00 26.48 ? 329 ASN   A H    1 
ATOM   5005 H  HA   . ASN   A 1 329 ? -3.546  -19.314 -0.738  1.00 31.83 ? 329 ASN   A HA   1 
ATOM   5006 H  HB2  . ASN   A 1 329 ? -5.687  -18.611 -0.207  1.00 29.78 ? 329 ASN   A HB2  1 
ATOM   5007 H  HB3  . ASN   A 1 329 ? -5.313  -17.110 -0.568  1.00 29.78 ? 329 ASN   A HB3  1 
ATOM   5008 H  HD21 . ASN   A 1 329 ? -7.465  -17.862 -1.784  1.00 54.34 ? 329 ASN   A HD21 1 
ATOM   5009 H  HD22 . ASN   A 1 329 ? -7.271  -18.195 -3.223  1.00 54.34 ? 329 ASN   A HD22 1 
ATOM   5010 N  N    . TYR   A 1 330 ? -1.803  -18.254 -2.154  1.00 21.76 ? 330 TYR   A N    1 
ATOM   5011 C  CA   . TYR   A 1 330 ? -0.948  -17.611 -3.146  1.00 22.52 ? 330 TYR   A CA   1 
ATOM   5012 C  C    . TYR   A 1 330 ? -1.390  -17.896 -4.577  1.00 24.46 ? 330 TYR   A C    1 
ATOM   5013 O  O    . TYR   A 1 330 ? -0.871  -17.281 -5.512  1.00 25.13 ? 330 TYR   A O    1 
ATOM   5014 C  CB   . TYR   A 1 330 ? 0.500   -18.056 -2.955  1.00 21.82 ? 330 TYR   A CB   1 
ATOM   5015 C  CG   . TYR   A 1 330 ? 0.809   -19.515 -3.206  1.00 23.64 ? 330 TYR   A CG   1 
ATOM   5016 C  CD1  . TYR   A 1 330 ? 0.953   -19.997 -4.497  1.00 23.91 ? 330 TYR   A CD1  1 
ATOM   5017 C  CD2  . TYR   A 1 330 ? 0.937   -20.413 -2.154  1.00 25.13 ? 330 TYR   A CD2  1 
ATOM   5018 C  CE1  . TYR   A 1 330 ? 1.257   -21.319 -4.739  1.00 27.54 ? 330 TYR   A CE1  1 
ATOM   5019 C  CE2  . TYR   A 1 330 ? 1.223   -21.749 -2.383  1.00 27.25 ? 330 TYR   A CE2  1 
ATOM   5020 C  CZ   . TYR   A 1 330 ? 1.381   -22.196 -3.687  1.00 26.53 ? 330 TYR   A CZ   1 
ATOM   5021 O  OH   . TYR   A 1 330 ? 1.671   -23.511 -3.974  1.00 29.53 ? 330 TYR   A OH   1 
ATOM   5022 H  H    . TYR   A 1 330 ? -1.598  -19.072 -1.985  1.00 26.13 ? 330 TYR   A H    1 
ATOM   5023 H  HA   . TYR   A 1 330 ? -0.979  -16.651 -3.014  1.00 27.04 ? 330 TYR   A HA   1 
ATOM   5024 H  HB2  . TYR   A 1 330 ? 1.056   -17.538 -3.558  1.00 26.20 ? 330 TYR   A HB2  1 
ATOM   5025 H  HB3  . TYR   A 1 330 ? 0.756   -17.863 -2.040  1.00 26.20 ? 330 TYR   A HB3  1 
ATOM   5026 H  HD1  . TYR   A 1 330 ? 0.878   -19.409 -5.213  1.00 28.71 ? 330 TYR   A HD1  1 
ATOM   5027 H  HD2  . TYR   A 1 330 ? 0.838   -20.110 -1.280  1.00 30.18 ? 330 TYR   A HD2  1 
ATOM   5028 H  HE1  . TYR   A 1 330 ? 1.353   -21.623 -5.609  1.00 33.06 ? 330 TYR   A HE1  1 
ATOM   5029 H  HE2  . TYR   A 1 330 ? 1.314   -22.339 -1.670  1.00 32.72 ? 330 TYR   A HE2  1 
ATOM   5030 H  HH   . TYR   A 1 330 ? 1.724   -23.955 -3.263  1.00 35.45 ? 330 TYR   A HH   1 
ATOM   5031 N  N    . GLN   A 1 331 ? -2.345  -18.806 -4.766  1.00 24.88 ? 331 GLN   A N    1 
ATOM   5032 C  CA   . GLN   A 1 331 ? -2.888  -19.043 -6.094  1.00 28.06 ? 331 GLN   A CA   1 
ATOM   5033 C  C    . GLN   A 1 331 ? -3.547  -17.776 -6.627  1.00 27.89 ? 331 GLN   A C    1 
ATOM   5034 O  O    . GLN   A 1 331 ? -3.445  -17.477 -7.823  1.00 32.04 ? 331 GLN   A O    1 
ATOM   5035 C  CB   . GLN   A 1 331 ? -3.853  -20.220 -5.991  1.00 26.89 ? 331 GLN   A CB   1 
ATOM   5036 C  CG   . GLN   A 1 331 ? -3.126  -21.558 -5.715  1.00 32.81 ? 331 GLN   A CG   1 
ATOM   5037 C  CD   . GLN   A 1 331 ? -2.758  -21.775 -4.233  1.00 36.17 ? 331 GLN   A CD   1 
ATOM   5038 O  OE1  . GLN   A 1 331 ? -3.224  -21.063 -3.339  1.00 31.99 ? 331 GLN   A OE1  1 
ATOM   5039 N  NE2  . GLN   A 1 331 ? -1.920  -22.779 -3.979  1.00 32.09 ? 331 GLN   A NE2  1 
ATOM   5040 H  H    . GLN   A 1 331 ? -2.693  -19.288 -4.146  1.00 29.87 ? 331 GLN   A H    1 
ATOM   5041 H  HA   . GLN   A 1 331 ? -2.169  -19.289 -6.697  1.00 33.69 ? 331 GLN   A HA   1 
ATOM   5042 H  HB2  . GLN   A 1 331 ? -4.474  -20.058 -5.263  1.00 32.29 ? 331 GLN   A HB2  1 
ATOM   5043 H  HB3  . GLN   A 1 331 ? -4.336  -20.307 -6.827  1.00 32.29 ? 331 GLN   A HB3  1 
ATOM   5044 H  HG2  . GLN   A 1 331 ? -3.703  -22.289 -5.987  1.00 39.39 ? 331 GLN   A HG2  1 
ATOM   5045 H  HG3  . GLN   A 1 331 ? -2.305  -21.580 -6.230  1.00 39.39 ? 331 GLN   A HG3  1 
ATOM   5046 H  HE21 . GLN   A 1 331 ? -1.614  -23.258 -4.625  1.00 38.52 ? 331 GLN   A HE21 1 
ATOM   5047 H  HE22 . GLN   A 1 331 ? -1.681  -22.946 -3.170  1.00 38.52 ? 331 GLN   A HE22 1 
ATOM   5048 N  N    . SER   A 1 332 ? -4.142  -16.978 -5.729  1.00 30.26 ? 332 SER   A N    1 
ATOM   5049 C  CA   . SER   A 1 332 ? -4.742  -15.701 -6.103  1.00 40.77 ? 332 SER   A CA   1 
ATOM   5050 C  C    . SER   A 1 332 ? -3.755  -14.783 -6.813  1.00 43.14 ? 332 SER   A C    1 
ATOM   5051 O  O    . SER   A 1 332 ? -4.160  -13.989 -7.671  1.00 39.28 ? 332 SER   A O    1 
ATOM   5052 C  CB   . SER   A 1 332 ? -5.309  -15.019 -4.849  1.00 37.89 ? 332 SER   A CB   1 
ATOM   5053 O  OG   . SER   A 1 332 ? -4.336  -14.863 -3.827  1.00 42.90 ? 332 SER   A OG   1 
ATOM   5054 H  H    . SER   A 1 332 ? -4.209  -17.161 -4.891  1.00 36.33 ? 332 SER   A H    1 
ATOM   5055 H  HA   . SER   A 1 332 ? -5.480  -15.868 -6.710  1.00 48.94 ? 332 SER   A HA   1 
ATOM   5056 H  HB2  . SER   A 1 332 ? -5.642  -14.142 -5.097  1.00 45.49 ? 332 SER   A HB2  1 
ATOM   5057 H  HB3  . SER   A 1 332 ? -6.037  -15.559 -4.504  1.00 45.49 ? 332 SER   A HB3  1 
ATOM   5058 H  HG   . SER   A 1 332 ? -4.043  -15.614 -3.591  1.00 51.49 ? 332 SER   A HG   1 
ATOM   5059 N  N    . CYS   A 1 333 ? -2.465  -14.877 -6.474  1.00 29.06 ? 333 CYS   A N    1 
ATOM   5060 C  CA   . CYS   A 1 333 ? -1.468  -13.983 -7.057  1.00 29.96 ? 333 CYS   A CA   1 
ATOM   5061 C  C    . CYS   A 1 333 ? -1.364  -14.141 -8.563  1.00 34.79 ? 333 CYS   A C    1 
ATOM   5062 O  O    . CYS   A 1 333 ? -0.965  -13.206 -9.267  1.00 34.85 ? 333 CYS   A O    1 
ATOM   5063 C  CB   . CYS   A 1 333 ? -0.096  -14.251 -6.445  1.00 27.63 ? 333 CYS   A CB   1 
ATOM   5064 S  SG   . CYS   A 1 333 ? -0.089  -14.207 -4.668  1.00 25.73 ? 333 CYS   A SG   1 
ATOM   5065 H  H    . CYS   A 1 333 ? -2.147  -15.446 -5.913  1.00 34.90 ? 333 CYS   A H    1 
ATOM   5066 H  HA   . CYS   A 1 333 ? -1.712  -13.064 -6.865  1.00 35.97 ? 333 CYS   A HA   1 
ATOM   5067 H  HB2  . CYS   A 1 333 ? 0.204   -15.131 -6.722  1.00 33.17 ? 333 CYS   A HB2  1 
ATOM   5068 H  HB3  . CYS   A 1 333 ? 0.525   -13.577 -6.761  1.00 33.17 ? 333 CYS   A HB3  1 
ATOM   5069 N  N    . TYR   A 1 334 ? -1.664  -15.326 -9.068  1.00 34.14 ? 334 TYR   A N    1 
ATOM   5070 C  CA   . TYR   A 1 334 ? -1.535  -15.649 -10.475 1.00 38.63 ? 334 TYR   A CA   1 
ATOM   5071 C  C    . TYR   A 1 334 ? -2.844  -15.462 -11.215 1.00 36.28 ? 334 TYR   A C    1 
ATOM   5072 O  O    . TYR   A 1 334 ? -3.002  -15.983 -12.326 1.00 47.13 ? 334 TYR   A O    1 
ATOM   5073 C  CB   . TYR   A 1 334 ? -0.999  -17.063 -10.575 1.00 39.14 ? 334 TYR   A CB   1 
ATOM   5074 C  CG   . TYR   A 1 334 ? 0.382   -17.206 -9.958  1.00 36.19 ? 334 TYR   A CG   1 
ATOM   5075 C  CD1  . TYR   A 1 334 ? 1.520   -16.863 -10.675 1.00 38.28 ? 334 TYR   A CD1  1 
ATOM   5076 C  CD2  . TYR   A 1 334 ? 0.543   -17.615 -8.636  1.00 35.13 ? 334 TYR   A CD2  1 
ATOM   5077 C  CE1  . TYR   A 1 334 ? 2.778   -16.997 -10.130 1.00 36.78 ? 334 TYR   A CE1  1 
ATOM   5078 C  CE2  . TYR   A 1 334 ? 1.802   -17.736 -8.072  1.00 35.70 ? 334 TYR   A CE2  1 
ATOM   5079 C  CZ   . TYR   A 1 334 ? 2.915   -17.418 -8.825  1.00 34.56 ? 334 TYR   A CZ   1 
ATOM   5080 O  OH   . TYR   A 1 334 ? 4.179   -17.527 -8.295  1.00 38.77 ? 334 TYR   A OH   1 
ATOM   5081 H  H    . TYR   A 1 334 ? -1.955  -15.983 -8.596  1.00 40.99 ? 334 TYR   A H    1 
ATOM   5082 H  HA   . TYR   A 1 334 ? -0.881  -15.055 -10.876 1.00 46.38 ? 334 TYR   A HA   1 
ATOM   5083 H  HB2  . TYR   A 1 334 ? -1.601  -17.664 -10.108 1.00 46.99 ? 334 TYR   A HB2  1 
ATOM   5084 H  HB3  . TYR   A 1 334 ? -0.938  -17.313 -11.510 1.00 46.99 ? 334 TYR   A HB3  1 
ATOM   5085 H  HD1  . TYR   A 1 334 ? 1.435   -16.588 -11.559 1.00 45.95 ? 334 TYR   A HD1  1 
ATOM   5086 H  HD2  . TYR   A 1 334 ? -0.206  -17.838 -8.132  1.00 42.17 ? 334 TYR   A HD2  1 
ATOM   5087 H  HE1  . TYR   A 1 334 ? 3.530   -16.775 -10.630 1.00 44.16 ? 334 TYR   A HE1  1 
ATOM   5088 H  HE2  . TYR   A 1 334 ? 1.897   -18.026 -7.194  1.00 42.85 ? 334 TYR   A HE2  1 
ATOM   5089 H  HH   . TYR   A 1 334 ? 4.134   -17.775 -7.494  1.00 46.55 ? 334 TYR   A HH   1 
ATOM   5090 N  N    . VAL   A 1 335 ? -3.756  -14.681 -10.626 1.00 44.67 ? 335 VAL   A N    1 
ATOM   5091 C  CA   . VAL   A 1 335 ? -5.074  -14.361 -11.180 1.00 50.44 ? 335 VAL   A CA   1 
ATOM   5092 C  C    . VAL   A 1 335 ? -5.704  -15.619 -11.757 1.00 53.42 ? 335 VAL   A C    1 
ATOM   5093 O  O    . VAL   A 1 335 ? -6.113  -16.505 -11.005 1.00 48.76 ? 335 VAL   A O    1 
ATOM   5094 C  CB   . VAL   A 1 335 ? -5.001  -13.214 -12.218 1.00 43.73 ? 335 VAL   A CB   1 
ATOM   5095 C  CG1  . VAL   A 1 335 ? -4.200  -12.037 -11.646 1.00 52.58 ? 335 VAL   A CG1  1 
ATOM   5096 C  CG2  . VAL   A 1 335 ? -4.411  -13.674 -13.534 1.00 52.35 ? 335 VAL   A CG2  1 
ATOM   5097 H  H    . VAL   A 1 335 ? -3.625  -14.304 -9.864  1.00 53.62 ? 335 VAL   A H    1 
ATOM   5098 H  HA   . VAL   A 1 335 ? -5.644  -14.058 -10.456 1.00 60.54 ? 335 VAL   A HA   1 
ATOM   5099 H  HB   . VAL   A 1 335 ? -5.901  -12.898 -12.394 1.00 52.49 ? 335 VAL   A HB   1 
ATOM   5100 H  HG11 . VAL   A 1 335 ? -4.262  -11.287 -12.258 1.00 63.12 ? 335 VAL   A HG11 1 
ATOM   5101 H  HG12 . VAL   A 1 335 ? -4.572  -11.792 -10.784 1.00 63.12 ? 335 VAL   A HG12 1 
ATOM   5102 H  HG13 . VAL   A 1 335 ? -3.273  -12.305 -11.543 1.00 63.12 ? 335 VAL   A HG13 1 
ATOM   5103 H  HG21 . VAL   A 1 335 ? -4.422  -12.928 -14.154 1.00 62.84 ? 335 VAL   A HG21 1 
ATOM   5104 H  HG22 . VAL   A 1 335 ? -3.497  -13.961 -13.390 1.00 62.84 ? 335 VAL   A HG22 1 
ATOM   5105 H  HG23 . VAL   A 1 335 ? -4.939  -14.402 -13.896 1.00 62.84 ? 335 VAL   A HG23 1 
HETATM 5106 C  C1   . A1IRL B 2 .   ? -0.250  -6.654  23.236  1.00 23.41 ? 401 A1IRL A C1   1 
HETATM 5107 C  C2   . A1IRL B 2 .   ? -1.622  -6.733  23.082  1.00 22.05 ? 401 A1IRL A C2   1 
HETATM 5108 C  C3   . A1IRL B 2 .   ? -2.363  -5.583  22.863  1.00 19.48 ? 401 A1IRL A C3   1 
HETATM 5109 C  C4   . A1IRL B 2 .   ? -1.727  -4.354  22.788  1.00 20.90 ? 401 A1IRL A C4   1 
HETATM 5110 C  C5   . A1IRL B 2 .   ? -0.360  -4.266  22.952  1.00 17.02 ? 401 A1IRL A C5   1 
HETATM 5111 C  C6   . A1IRL B 2 .   ? 0.382   -5.420  23.178  1.00 19.65 ? 401 A1IRL A C6   1 
HETATM 5112 C  C10  . A1IRL B 2 .   ? 3.459   -6.170  26.271  1.00 21.79 ? 401 A1IRL A C10  1 
HETATM 5113 C  C11  . A1IRL B 2 .   ? 5.621   -4.930  26.063  1.00 19.71 ? 401 A1IRL A C11  1 
HETATM 5114 C  C12  . A1IRL B 2 .   ? 5.279   -4.632  22.091  1.00 17.30 ? 401 A1IRL A C12  1 
HETATM 5115 C  C13  . A1IRL B 2 .   ? 5.997   -3.409  21.520  1.00 13.36 ? 401 A1IRL A C13  1 
HETATM 5116 C  C14  . A1IRL B 2 .   ? 7.297   -4.014  20.968  1.00 13.67 ? 401 A1IRL A C14  1 
HETATM 5117 C  C15  . A1IRL B 2 .   ? 8.124   -4.840  21.950  1.00 14.29 ? 401 A1IRL A C15  1 
HETATM 5118 C  C16  . A1IRL B 2 .   ? 8.604   -4.006  23.116  1.00 16.46 ? 401 A1IRL A C16  1 
HETATM 5119 C  C17  . A1IRL B 2 .   ? 9.311   -5.463  21.192  1.00 15.43 ? 401 A1IRL A C17  1 
HETATM 5120 C  C7   . A1IRL B 2 .   ? 2.844   -5.784  23.621  1.00 30.25 ? 401 A1IRL A C7   1 
HETATM 5121 C  C8   . A1IRL B 2 .   ? 3.937   -4.843  24.129  1.00 27.43 ? 401 A1IRL A C8   1 
HETATM 5122 C  C9   . A1IRL B 2 .   ? 4.143   -4.943  25.661  1.00 17.15 ? 401 A1IRL A C9   1 
HETATM 5123 N  N1   . A1IRL B 2 .   ? 1.735   -5.082  23.348  1.00 21.44 ? 401 A1IRL A N1   1 
HETATM 5124 N  N2   . A1IRL B 2 .   ? 5.184   -4.647  23.424  1.00 30.18 ? 401 A1IRL A N2   1 
HETATM 5125 O  O1   . A1IRL B 2 .   ? 2.958   -7.013  23.626  1.00 32.63 ? 401 A1IRL A O1   1 
HETATM 5126 O  O2   . A1IRL B 2 .   ? 4.013   -1.706  21.073  1.00 18.26 ? 401 A1IRL A O2   1 
HETATM 5127 O  O3   . A1IRL B 2 .   ? 6.209   -1.222  19.909  1.00 19.28 ? 401 A1IRL A O3   1 
HETATM 5128 O  O4   . A1IRL B 2 .   ? 4.723   -3.130  19.159  1.00 13.43 ? 401 A1IRL A O4   1 
HETATM 5129 O  O5   . A1IRL B 2 .   ? 4.934   -5.569  21.374  1.00 16.08 ? 401 A1IRL A O5   1 
HETATM 5130 P  P1   . A1IRL B 2 .   ? 5.209   -2.323  20.317  1.00 15.56 ? 401 A1IRL A P1   1 
HETATM 5131 CL CL1  . A1IRL B 2 .   ? -4.086  -5.700  22.718  1.00 24.53 ? 401 A1IRL A CL1  1 
HETATM 5132 CL CL2  . A1IRL B 2 .   ? -2.616  -2.906  22.441  1.00 26.59 ? 401 A1IRL A CL2  1 
HETATM 5133 H  H1   . A1IRL B 2 .   ? 0.327   -7.563  23.402  1.00 28.11 ? 401 A1IRL A H1   1 
HETATM 5134 H  H2   . A1IRL B 2 .   ? -2.136  -7.686  23.133  1.00 26.47 ? 401 A1IRL A H2   1 
HETATM 5135 H  H3   . A1IRL B 2 .   ? 0.111   -3.286  22.900  1.00 20.44 ? 401 A1IRL A H3   1 
HETATM 5136 H  H10  . A1IRL B 2 .   ? 2.376   -6.137  26.156  1.00 26.17 ? 401 A1IRL A H10  1 
HETATM 5137 H  H9   . A1IRL B 2 .   ? 3.648   -6.249  27.341  1.00 26.17 ? 401 A1IRL A H9   1 
HETATM 5138 H  H8   . A1IRL B 2 .   ? 3.788   -7.109  25.829  1.00 26.17 ? 401 A1IRL A H8   1 
HETATM 5139 H  H12  . A1IRL B 2 .   ? 6.098   -3.975  25.849  1.00 23.67 ? 401 A1IRL A H12  1 
HETATM 5140 H  H13  . A1IRL B 2 .   ? 6.208   -5.700  25.564  1.00 23.67 ? 401 A1IRL A H13  1 
HETATM 5141 H  H11  . A1IRL B 2 .   ? 5.749   -5.082  27.132  1.00 23.67 ? 401 A1IRL A H11  1 
HETATM 5142 H  H14  . A1IRL B 2 .   ? 6.244   -2.779  22.372  1.00 16.05 ? 401 A1IRL A H14  1 
HETATM 5143 H  H16  . A1IRL B 2 .   ? 7.908   -3.201  20.581  1.00 16.42 ? 401 A1IRL A H16  1 
HETATM 5144 H  H15  . A1IRL B 2 .   ? 7.049   -4.622  20.099  1.00 16.42 ? 401 A1IRL A H15  1 
HETATM 5145 H  H17  . A1IRL B 2 .   ? 7.536   -5.663  22.350  1.00 17.16 ? 401 A1IRL A H17  1 
HETATM 5146 H  H18  . A1IRL B 2 .   ? 9.214   -3.164  22.793  1.00 19.77 ? 401 A1IRL A H18  1 
HETATM 5147 H  H20  . A1IRL B 2 .   ? 9.224   -4.588  23.796  1.00 19.77 ? 401 A1IRL A H20  1 
HETATM 5148 H  H19  . A1IRL B 2 .   ? 7.788   -3.600  23.711  1.00 19.77 ? 401 A1IRL A H19  1 
HETATM 5149 H  H22  . A1IRL B 2 .   ? 9.973   -4.707  20.772  1.00 18.53 ? 401 A1IRL A H22  1 
HETATM 5150 H  H21  . A1IRL B 2 .   ? 8.995   -6.115  20.379  1.00 18.53 ? 401 A1IRL A H21  1 
HETATM 5151 H  H23  . A1IRL B 2 .   ? 9.937   -6.067  21.847  1.00 18.53 ? 401 A1IRL A H23  1 
HETATM 5152 H  H5   . A1IRL B 2 .   ? 3.489   -3.855  24.106  1.00 32.94 ? 401 A1IRL A H5   1 
HETATM 5153 H  H7   . A1IRL B 2 .   ? 3.694   -4.063  26.120  1.00 20.60 ? 401 A1IRL A H7   1 
HETATM 5154 H  H4   . A1IRL B 2 .   ? 1.869   -4.087  23.212  1.00 25.75 ? 401 A1IRL A H4   1 
HETATM 5155 H  H6   . A1IRL B 2 .   ? 6.004   -4.493  23.985  1.00 36.24 ? 401 A1IRL A H6   1 
HETATM 5156 H  H24  . A1IRL B 2 .   ? 3.562   -0.886  20.741  1.00 21.93 ? 401 A1IRL A H24  1 
HETATM 5157 H  H25  . A1IRL B 2 .   ? 6.005   -0.605  19.158  1.00 23.16 ? 401 A1IRL A H25  1 
HETATM 5158 O  O6   . BU3   C 3 .   ? -5.180  -5.387  5.958   1.00 24.18 ? 402 BU3   A O6   1 
HETATM 5159 C  C3   . BU3   C 3 .   ? -6.280  -4.483  5.873   1.00 32.13 ? 402 BU3   A C3   1 
HETATM 5160 C  C4   . BU3   C 3 .   ? -6.074  -3.293  6.762   1.00 31.16 ? 402 BU3   A C4   1 
HETATM 5161 C  C2   . BU3   C 3 .   ? -7.529  -5.333  6.120   1.00 34.24 ? 402 BU3   A C2   1 
HETATM 5162 O  O5   . BU3   C 3 .   ? -7.496  -5.960  7.384   1.00 30.33 ? 402 BU3   A O5   1 
HETATM 5163 C  C1   . BU3   C 3 .   ? -7.725  -6.361  5.011   1.00 33.73 ? 402 BU3   A C1   1 
HETATM 5164 H  HO6  . BU3   C 3 .   ? -4.548  -5.081  5.479   1.00 29.04 ? 402 BU3   A HO6  1 
HETATM 5165 H  H3   . BU3   C 3 .   ? -6.309  -4.185  4.950   1.00 38.57 ? 402 BU3   A H3   1 
HETATM 5166 H  H41  . BU3   C 3 .   ? -5.330  -2.754  6.451   1.00 37.41 ? 402 BU3   A H41  1 
HETATM 5167 H  H42  . BU3   C 3 .   ? -5.879  -3.569  7.671   1.00 37.41 ? 402 BU3   A H42  1 
HETATM 5168 H  H43  . BU3   C 3 .   ? -6.865  -2.731  6.786   1.00 37.41 ? 402 BU3   A H43  1 
HETATM 5169 H  H2   . BU3   C 3 .   ? -8.292  -4.734  6.136   1.00 41.10 ? 402 BU3   A H2   1 
HETATM 5170 H  HO5  . BU3   C 3 .   ? -8.296  -6.057  7.653   1.00 36.41 ? 402 BU3   A HO5  1 
HETATM 5171 H  H11  . BU3   C 3 .   ? -8.640  -6.681  4.995   1.00 40.49 ? 402 BU3   A H11  1 
HETATM 5172 H  H12  . BU3   C 3 .   ? -7.145  -7.127  5.143   1.00 40.49 ? 402 BU3   A H12  1 
HETATM 5173 H  H13  . BU3   C 3 .   ? -7.521  -5.984  4.141   1.00 40.49 ? 402 BU3   A H13  1 
HETATM 5174 O  O6   . BU3   D 3 .   ? 22.893  -6.180  35.976  1.00 41.61 ? 403 BU3   A O6   1 
HETATM 5175 C  C3   . BU3   D 3 .   ? 23.997  -5.594  36.643  1.00 44.69 ? 403 BU3   A C3   1 
HETATM 5176 C  C4   . BU3   D 3 .   ? 24.681  -6.633  37.526  1.00 42.15 ? 403 BU3   A C4   1 
HETATM 5177 C  C2   . BU3   D 3 .   ? 23.666  -4.305  37.395  1.00 39.80 ? 403 BU3   A C2   1 
HETATM 5178 O  O5   . BU3   D 3 .   ? 24.466  -4.172  38.568  1.00 47.12 ? 403 BU3   A O5   1 
HETATM 5179 C  C1   . BU3   D 3 .   ? 22.200  -4.118  37.716  1.00 41.34 ? 403 BU3   A C1   1 
HETATM 5180 H  HO6  . BU3   D 3 .   ? 23.110  -6.307  35.164  1.00 49.95 ? 403 BU3   A HO6  1 
HETATM 5181 H  H3   . BU3   D 3 .   ? 24.613  -5.348  35.936  1.00 53.65 ? 403 BU3   A H3   1 
HETATM 5182 H  H41  . BU3   D 3 .   ? 24.771  -7.478  37.058  1.00 50.59 ? 403 BU3   A H41  1 
HETATM 5183 H  H42  . BU3   D 3 .   ? 24.167  -6.795  38.333  1.00 50.59 ? 403 BU3   A H42  1 
HETATM 5184 H  H43  . BU3   D 3 .   ? 25.566  -6.339  37.793  1.00 50.59 ? 403 BU3   A H43  1 
HETATM 5185 H  H2   . BU3   D 3 .   ? 23.941  -3.574  36.820  1.00 47.78 ? 403 BU3   A H2   1 
HETATM 5186 H  HO5  . BU3   D 3 .   ? 24.178  -3.507  39.012  1.00 56.57 ? 403 BU3   A HO5  1 
HETATM 5187 H  H11  . BU3   D 3 .   ? 21.770  -4.972  37.877  1.00 49.62 ? 403 BU3   A H11  1 
HETATM 5188 H  H12  . BU3   D 3 .   ? 21.737  -3.686  36.981  1.00 49.62 ? 403 BU3   A H12  1 
HETATM 5189 H  H13  . BU3   D 3 .   ? 22.080  -3.565  38.504  1.00 49.62 ? 403 BU3   A H13  1 
HETATM 5190 C  C1   . GOL   E 4 .   ? 8.599   -27.345 -2.033  1.00 41.19 ? 404 GOL   A C1   1 
HETATM 5191 O  O1   . GOL   E 4 .   ? 9.032   -26.764 -0.840  1.00 54.10 ? 404 GOL   A O1   1 
HETATM 5192 C  C2   . GOL   E 4 .   ? 9.855   -27.732 -2.842  1.00 42.83 ? 404 GOL   A C2   1 
HETATM 5193 O  O2   . GOL   E 4 .   ? 10.857  -26.770 -2.758  1.00 43.34 ? 404 GOL   A O2   1 
HETATM 5194 C  C3   . GOL   E 4 .   ? 10.285  -29.102 -2.275  1.00 48.57 ? 404 GOL   A C3   1 
HETATM 5195 O  O3   . GOL   E 4 .   ? 11.208  -29.645 -3.191  1.00 45.82 ? 404 GOL   A O3   1 
HETATM 5196 H  H11  . GOL   E 4 .   ? 8.050   -26.745 -2.562  1.00 49.45 ? 404 GOL   A H11  1 
HETATM 5197 H  H12  . GOL   E 4 .   ? 8.048   -28.125 -1.871  1.00 49.45 ? 404 GOL   A H12  1 
HETATM 5198 H  H2   . GOL   E 4 .   ? 9.640   -27.805 -3.785  1.00 51.41 ? 404 GOL   A H2   1 
HETATM 5199 H  HO2  . GOL   E 4 .   ? 10.956  -26.567 -1.939  1.00 52.02 ? 404 GOL   A HO2  1 
HETATM 5200 H  H31  . GOL   E 4 .   ? 9.505   -29.659 -2.134  1.00 58.31 ? 404 GOL   A H31  1 
HETATM 5201 H  H32  . GOL   E 4 .   ? 10.675  -28.981 -1.395  1.00 58.31 ? 404 GOL   A H32  1 
HETATM 5202 H  HO3  . GOL   E 4 .   ? 10.753  -30.042 -3.789  1.00 55.01 ? 404 GOL   A HO3  1 
HETATM 5203 O  O6   . BU3   F 3 .   ? 8.690   13.303  37.228  1.00 45.68 ? 405 BU3   A O6   1 
HETATM 5204 C  C3   . BU3   F 3 .   ? 9.204   12.916  38.486  1.00 48.47 ? 405 BU3   A C3   1 
HETATM 5205 C  C4   . BU3   F 3 .   ? 9.142   14.059  39.488  1.00 42.72 ? 405 BU3   A C4   1 
HETATM 5206 C  C2   . BU3   F 3 .   ? 10.617  12.334  38.379  1.00 52.11 ? 405 BU3   A C2   1 
HETATM 5207 O  O5   . BU3   F 3 .   ? 11.565  13.348  38.080  1.00 46.74 ? 405 BU3   A O5   1 
HETATM 5208 C  C1   . BU3   F 3 .   ? 10.728  11.188  37.395  1.00 40.99 ? 405 BU3   A C1   1 
HETATM 5209 H  HO6  . BU3   F 3 .   ? 7.844   13.221  37.250  1.00 54.83 ? 405 BU3   A HO6  1 
HETATM 5210 H  H3   . BU3   F 3 .   ? 8.625   12.202  38.796  1.00 58.19 ? 405 BU3   A H3   1 
HETATM 5211 H  H41  . BU3   F 3 .   ? 8.222   14.276  39.708  1.00 51.29 ? 405 BU3   A H41  1 
HETATM 5212 H  H42  . BU3   F 3 .   ? 9.557   14.858  39.128  1.00 51.29 ? 405 BU3   A H42  1 
HETATM 5213 H  H43  . BU3   F 3 .   ? 9.603   13.831  40.310  1.00 51.29 ? 405 BU3   A H43  1 
HETATM 5214 H  H2   . BU3   F 3 .   ? 10.856  12.006  39.260  1.00 62.55 ? 405 BU3   A H2   1 
HETATM 5215 H  HO5  . BU3   F 3 .   ? 12.321  13.101  38.380  1.00 56.10 ? 405 BU3   A HO5  1 
HETATM 5216 H  H11  . BU3   F 3 .   ? 11.256  11.446  36.623  1.00 49.21 ? 405 BU3   A H11  1 
HETATM 5217 H  H12  . BU3   F 3 .   ? 9.852   10.917  37.078  1.00 49.21 ? 405 BU3   A H12  1 
HETATM 5218 H  H13  . BU3   F 3 .   ? 11.146  10.414  37.803  1.00 49.21 ? 405 BU3   A H13  1 
HETATM 5219 C  C1   . GOL   G 4 .   ? 17.279  -20.775 -3.009  1.00 42.11 ? 406 GOL   A C1   1 
HETATM 5220 O  O1   . GOL   G 4 .   ? 16.478  -19.817 -2.350  1.00 35.04 ? 406 GOL   A O1   1 
HETATM 5221 C  C2   . GOL   G 4 .   ? 18.179  -21.503 -1.979  1.00 43.65 ? 406 GOL   A C2   1 
HETATM 5222 O  O2   . GOL   G 4 .   ? 17.866  -21.298 -0.668  1.00 57.10 ? 406 GOL   A O2   1 
HETATM 5223 C  C3   . GOL   G 4 .   ? 18.036  -23.000 -2.359  1.00 50.59 ? 406 GOL   A C3   1 
HETATM 5224 O  O3   . GOL   G 4 .   ? 16.769  -23.460 -1.895  1.00 54.26 ? 406 GOL   A O3   1 
HETATM 5225 H  H11  . GOL   G 4 .   ? 17.831  -20.388 -3.689  1.00 50.55 ? 406 GOL   A H11  1 
HETATM 5226 H  H12  . GOL   G 4 .   ? 16.740  -21.418 -3.467  1.00 50.55 ? 406 GOL   A H12  1 
HETATM 5227 H  HO1  . GOL   G 4 .   ? 16.408  -20.075 -1.543  1.00 42.07 ? 406 GOL   A HO1  1 
HETATM 5228 H  H2   . GOL   G 4 .   ? 19.100  -21.214 -2.075  1.00 52.39 ? 406 GOL   A H2   1 
HETATM 5229 H  H31  . GOL   G 4 .   ? 18.785  -23.492 -1.990  1.00 60.73 ? 406 GOL   A H31  1 
HETATM 5230 H  H32  . GOL   G 4 .   ? 18.128  -23.091 -3.315  1.00 60.73 ? 406 GOL   A H32  1 
HETATM 5231 H  HO3  . GOL   G 4 .   ? 16.605  -23.038 -1.175  1.00 65.13 ? 406 GOL   A HO3  1 
HETATM 5232 O  O6   . BU3   H 3 .   ? 20.886  -6.808  23.453  1.00 23.87 ? 407 BU3   A O6   1 
HETATM 5233 C  C3   . BU3   H 3 .   ? 22.139  -6.194  23.700  1.00 32.92 ? 407 BU3   A C3   1 
HETATM 5234 C  C4   . BU3   H 3 .   ? 22.113  -4.690  23.481  1.00 34.17 ? 407 BU3   A C4   1 
HETATM 5235 C  C2   . BU3   H 3 .   ? 23.246  -6.872  22.876  1.00 33.68 ? 407 BU3   A C2   1 
HETATM 5236 O  O5   . BU3   H 3 .   ? 22.995  -8.248  22.625  1.00 33.26 ? 407 BU3   A O5   1 
HETATM 5237 C  C1   . BU3   H 3 .   ? 24.638  -6.682  23.482  1.00 31.23 ? 407 BU3   A C1   1 
HETATM 5238 H  HO6  . BU3   H 3 .   ? 20.484  -6.900  24.196  1.00 28.67 ? 407 BU3   A HO6  1 
HETATM 5239 H  H3   . BU3   H 3 .   ? 22.334  -6.367  24.634  1.00 39.52 ? 407 BU3   A H3   1 
HETATM 5240 H  H41  . BU3   H 3 .   ? 21.407  -4.277  24.002  1.00 41.02 ? 407 BU3   A H41  1 
HETATM 5241 H  H42  . BU3   H 3 .   ? 21.954  -4.478  22.548  1.00 41.02 ? 407 BU3   A H42  1 
HETATM 5242 H  H43  . BU3   H 3 .   ? 22.955  -4.283  23.738  1.00 41.02 ? 407 BU3   A H43  1 
HETATM 5243 H  H2   . BU3   H 3 .   ? 23.261  -6.445  22.009  1.00 40.43 ? 407 BU3   A H2   1 
HETATM 5244 H  HO5  . BU3   H 3 .   ? 23.112  -8.392  21.796  1.00 39.93 ? 407 BU3   A HO5  1 
HETATM 5245 H  H11  . BU3   H 3 .   ? 24.932  -7.490  23.930  1.00 37.50 ? 407 BU3   A H11  1 
HETATM 5246 H  H12  . BU3   H 3 .   ? 24.637  -5.964  24.135  1.00 37.50 ? 407 BU3   A H12  1 
HETATM 5247 H  H13  . BU3   H 3 .   ? 25.291  -6.458  22.800  1.00 37.50 ? 407 BU3   A H13  1 
HETATM 5248 O  O6   . BU3   I 3 .   ? 0.113   -20.935 -8.807  1.00 44.81 ? 408 BU3   A O6   1 
HETATM 5249 C  C3   . BU3   I 3 .   ? 1.219   -21.609 -9.355  1.00 44.54 ? 408 BU3   A C3   1 
HETATM 5250 C  C4   . BU3   I 3 .   ? 2.292   -21.763 -8.273  1.00 27.50 ? 408 BU3   A C4   1 
HETATM 5251 C  C2   . BU3   I 3 .   ? 1.846   -20.997 -10.605 1.00 47.81 ? 408 BU3   A C2   1 
HETATM 5252 O  O5   . BU3   I 3 .   ? 0.938   -21.067 -11.687 1.00 59.43 ? 408 BU3   A O5   1 
HETATM 5253 C  C1   . BU3   I 3 .   ? 3.174   -21.643 -10.961 1.00 42.56 ? 408 BU3   A C1   1 
HETATM 5254 H  HO6  . BU3   I 3 .   ? -0.508  -21.502 -8.681  1.00 53.79 ? 408 BU3   A HO6  1 
HETATM 5255 H  H3   . BU3   I 3 .   ? 0.895   -22.490 -9.599  1.00 53.47 ? 408 BU3   A H3   1 
HETATM 5256 H  H41  . BU3   I 3 .   ? 2.773   -20.932 -8.188  1.00 33.02 ? 408 BU3   A H41  1 
HETATM 5257 H  H42  . BU3   I 3 .   ? 2.926   -22.466 -8.481  1.00 33.02 ? 408 BU3   A H42  1 
HETATM 5258 H  H43  . BU3   I 3 .   ? 1.892   -21.959 -7.418  1.00 33.02 ? 408 BU3   A H43  1 
HETATM 5259 H  H2   . BU3   I 3 .   ? 1.988   -20.053 -10.431 1.00 57.39 ? 408 BU3   A H2   1 
HETATM 5260 H  HO5  . BU3   I 3 .   ? 0.902   -20.301 -12.053 1.00 71.33 ? 408 BU3   A HO5  1 
HETATM 5261 H  H11  . BU3   I 3 .   ? 3.377   -21.516 -11.901 1.00 51.09 ? 408 BU3   A H11  1 
HETATM 5262 H  H12  . BU3   I 3 .   ? 3.899   -21.255 -10.447 1.00 51.09 ? 408 BU3   A H12  1 
HETATM 5263 H  H13  . BU3   I 3 .   ? 3.162   -22.596 -10.781 1.00 51.09 ? 408 BU3   A H13  1 
HETATM 5264 C  C1   . GOL   J 4 .   ? 29.081  -0.597  7.827   1.00 33.76 ? 409 GOL   A C1   1 
HETATM 5265 O  O1   . GOL   J 4 .   ? 28.549  -1.549  8.698   1.00 58.70 ? 409 GOL   A O1   1 
HETATM 5266 C  C2   . GOL   J 4 .   ? 30.306  -1.241  7.160   1.00 50.14 ? 409 GOL   A C2   1 
HETATM 5267 O  O2   . GOL   J 4 .   ? 31.050  -0.289  6.486   1.00 44.74 ? 409 GOL   A O2   1 
HETATM 5268 C  C3   . GOL   J 4 .   ? 31.064  -1.934  8.301   1.00 42.42 ? 409 GOL   A C3   1 
HETATM 5269 O  O3   . GOL   J 4 .   ? 30.679  -3.289  8.246   1.00 51.29 ? 409 GOL   A O3   1 
HETATM 5270 H  H11  . GOL   J 4 .   ? 29.359  0.224   8.262   1.00 40.54 ? 409 GOL   A H11  1 
HETATM 5271 H  H12  . GOL   J 4 .   ? 28.439  -0.333  7.153   1.00 40.54 ? 409 GOL   A H12  1 
HETATM 5272 H  H2   . GOL   J 4 .   ? 30.029  -1.885  6.489   1.00 60.18 ? 409 GOL   A H2   1 
HETATM 5273 H  H31  . GOL   J 4 .   ? 30.869  -1.495  9.143   1.00 50.92 ? 409 GOL   A H31  1 
HETATM 5274 H  H32  . GOL   J 4 .   ? 32.011  -1.828  8.168   1.00 50.92 ? 409 GOL   A H32  1 
HETATM 5275 H  HO3  . GOL   J 4 .   ? 29.830  -3.304  8.292   1.00 61.57 ? 409 GOL   A HO3  1 
HETATM 5276 ZN ZN   . ZN    K 5 .   ? 5.532   -3.291  17.433  1.00 14.99 ? 410 ZN    A ZN   1 
HETATM 5277 S  S    . SO4   L 6 .   ? 4.487   -26.355 22.967  1.00 97.56 ? 411 SO4   A S    1 
HETATM 5278 O  O1   . SO4   L 6 .   ? 5.619   -26.259 23.845  1.00 75.85 ? 411 SO4   A O1   1 
HETATM 5279 O  O2   . SO4   L 6 .   ? 4.932   -26.719 21.649  1.00 83.92 ? 411 SO4   A O2   1 
HETATM 5280 O  O3   . SO4   L 6 .   ? 3.582   -27.358 23.458  1.00 83.69 ? 411 SO4   A O3   1 
HETATM 5281 O  O4   . SO4   L 6 .   ? 3.812   -25.087 22.913  1.00 73.25 ? 411 SO4   A O4   1 
HETATM 5282 S  S    . SO4   M 6 .   ? 8.812   14.819  21.634  1.00 78.02 ? 412 SO4   A S    1 
HETATM 5283 O  O1   . SO4   M 6 .   ? 7.711   13.911  21.319  1.00 62.15 ? 412 SO4   A O1   1 
HETATM 5284 O  O2   . SO4   M 6 .   ? 9.393   14.483  22.935  1.00 45.29 ? 412 SO4   A O2   1 
HETATM 5285 O  O3   . SO4   M 6 .   ? 9.832   14.734  20.591  1.00 41.83 ? 412 SO4   A O3   1 
HETATM 5286 O  O4   . SO4   M 6 .   ? 8.291   16.183  21.650  1.00 65.69 ? 412 SO4   A O4   1 
HETATM 5287 O  O    . HOH   N 7 .   ? 10.473  -25.101 7.121   1.00 46.68 ? 501 HOH   A O    1 
HETATM 5288 O  O    . HOH   N 7 .   ? 17.529  8.321   0.990   1.00 49.89 ? 502 HOH   A O    1 
HETATM 5289 O  O    . HOH   N 7 .   ? 18.690  -15.061 36.955  1.00 42.83 ? 503 HOH   A O    1 
HETATM 5290 O  O    . HOH   N 7 .   ? 27.766  4.829   9.273   1.00 36.40 ? 504 HOH   A O    1 
HETATM 5291 O  O    . HOH   N 7 .   ? 4.892   -25.919 9.424   1.00 47.22 ? 505 HOH   A O    1 
HETATM 5292 O  O    . HOH   N 7 .   ? 13.929  5.509   4.165   1.00 39.99 ? 506 HOH   A O    1 
HETATM 5293 O  O    . HOH   N 7 .   ? 24.522  6.360   6.745   1.00 30.21 ? 507 HOH   A O    1 
HETATM 5294 O  O    . HOH   N 7 .   ? 27.651  4.338   13.089  1.00 33.59 ? 508 HOH   A O    1 
HETATM 5295 O  O    . HOH   N 7 .   ? 13.202  2.638   37.148  1.00 36.10 ? 509 HOH   A O    1 
HETATM 5296 O  O    . HOH   N 7 .   ? 20.039  -8.235  25.361  1.00 32.87 ? 510 HOH   A O    1 
HETATM 5297 O  O    . HOH   N 7 .   ? -1.745  -5.134  -1.643  1.00 33.80 ? 511 HOH   A O    1 
HETATM 5298 O  O    . HOH   N 7 .   ? 8.210   -20.848 27.360  1.00 48.58 ? 512 HOH   A O    1 
HETATM 5299 O  O    . HOH   N 7 .   ? 22.079  -20.185 10.095  1.00 39.82 ? 513 HOH   A O    1 
HETATM 5300 O  O    . HOH   N 7 .   ? 8.009   11.692  35.386  1.00 33.76 ? 514 HOH   A O    1 
HETATM 5301 O  O    . HOH   N 7 .   ? 13.168  -18.038 26.618  1.00 39.22 ? 515 HOH   A O    1 
HETATM 5302 O  O    . HOH   N 7 .   ? 8.962   1.525   -0.372  1.00 28.24 ? 516 HOH   A O    1 
HETATM 5303 O  O    . HOH   N 7 .   ? -2.793  -24.814 3.978   1.00 40.32 ? 517 HOH   A O    1 
HETATM 5304 O  O    . HOH   N 7 .   ? 13.310  3.635   6.504   1.00 25.45 ? 518 HOH   A O    1 
HETATM 5305 O  O    . HOH   N 7 .   ? 30.947  -6.964  34.825  1.00 39.81 ? 519 HOH   A O    1 
HETATM 5306 O  O    . HOH   N 7 .   ? 4.135   0.691   22.007  1.00 25.25 ? 520 HOH   A O    1 
HETATM 5307 O  O    . HOH   N 7 .   ? -6.359  -17.983 4.821   1.00 39.05 ? 521 HOH   A O    1 
HETATM 5308 O  O    . HOH   N 7 .   ? -0.682  -23.825 20.996  1.00 41.14 ? 522 HOH   A O    1 
HETATM 5309 O  O    . HOH   N 7 .   ? 0.648   4.140   5.923   1.00 31.83 ? 523 HOH   A O    1 
HETATM 5310 O  O    . HOH   N 7 .   ? 20.836  5.483   36.166  1.00 32.72 ? 524 HOH   A O    1 
HETATM 5311 O  O    . HOH   N 7 .   ? 10.967  -26.730 1.142   1.00 31.10 ? 525 HOH   A O    1 
HETATM 5312 O  O    . HOH   N 7 .   ? -7.461  -16.606 1.890   1.00 34.47 ? 526 HOH   A O    1 
HETATM 5313 O  O    . HOH   N 7 .   ? 13.366  -17.266 -8.334  1.00 34.51 ? 527 HOH   A O    1 
HETATM 5314 O  O    . HOH   N 7 .   ? 14.385  -15.243 -10.307 1.00 36.43 ? 528 HOH   A O    1 
HETATM 5315 O  O    . HOH   N 7 .   ? 18.865  -18.731 12.845  1.00 31.15 ? 529 HOH   A O    1 
HETATM 5316 O  O    . HOH   N 7 .   ? 20.373  13.146  5.963   1.00 41.80 ? 530 HOH   A O    1 
HETATM 5317 O  O    . HOH   N 7 .   ? 41.392  14.219  37.157  1.00 49.92 ? 531 HOH   A O    1 
HETATM 5318 O  O    . HOH   N 7 .   ? 41.900  12.982  26.758  1.00 48.96 ? 532 HOH   A O    1 
HETATM 5319 O  O    . HOH   N 7 .   ? -5.964  -4.909  0.557   1.00 30.36 ? 533 HOH   A O    1 
HETATM 5320 O  O    . HOH   N 7 .   ? 31.148  11.386  33.868  1.00 29.31 ? 534 HOH   A O    1 
HETATM 5321 O  O    . HOH   N 7 .   ? 16.035  -12.825 22.266  1.00 21.14 ? 535 HOH   A O    1 
HETATM 5322 O  O    . HOH   N 7 .   ? 10.036  -24.580 -9.858  1.00 37.75 ? 536 HOH   A O    1 
HETATM 5323 O  O    . HOH   N 7 .   ? 10.212  3.589   32.841  1.00 20.38 ? 537 HOH   A O    1 
HETATM 5324 O  O    . HOH   N 7 .   ? 42.752  11.051  28.064  1.00 41.19 ? 538 HOH   A O    1 
HETATM 5325 O  O    . HOH   N 7 .   ? 14.149  13.311  17.660  1.00 35.43 ? 539 HOH   A O    1 
HETATM 5326 O  O    . HOH   N 7 .   ? 32.993  -9.071  31.277  1.00 39.31 ? 540 HOH   A O    1 
HETATM 5327 O  O    . HOH   N 7 .   ? 34.419  9.625   31.391  1.00 27.29 ? 541 HOH   A O    1 
HETATM 5328 O  O    . HOH   N 7 .   ? 8.810   -16.448 35.165  1.00 38.88 ? 542 HOH   A O    1 
HETATM 5329 O  O    . HOH   N 7 .   ? 6.442   -12.742 40.931  1.00 36.11 ? 543 HOH   A O    1 
HETATM 5330 O  O    . HOH   N 7 .   ? 27.064  4.780   38.759  1.00 34.81 ? 544 HOH   A O    1 
HETATM 5331 O  O    . HOH   N 7 .   ? 9.337   7.106   20.193  1.00 20.00 ? 545 HOH   A O    1 
HETATM 5332 O  O    . HOH   N 7 .   ? -7.647  -7.124  13.559  1.00 28.90 ? 546 HOH   A O    1 
HETATM 5333 O  O    . HOH   N 7 .   ? 1.864   -0.765  19.412  1.00 28.09 ? 547 HOH   A O    1 
HETATM 5334 O  O    . HOH   N 7 .   ? 33.359  0.830   37.451  1.00 31.46 ? 548 HOH   A O    1 
HETATM 5335 O  O    . HOH   N 7 .   ? -1.443  3.116   10.633  1.00 38.10 ? 549 HOH   A O    1 
HETATM 5336 O  O    . HOH   N 7 .   ? 9.142   18.044  34.816  1.00 53.11 ? 550 HOH   A O    1 
HETATM 5337 O  O    . HOH   N 7 .   ? -10.347 -16.550 9.545   1.00 39.67 ? 551 HOH   A O    1 
HETATM 5338 O  O    . HOH   N 7 .   ? 12.187  -26.003 -7.096  1.00 29.61 ? 552 HOH   A O    1 
HETATM 5339 O  O    . HOH   N 7 .   ? -6.621  -10.609 -0.411  1.00 27.34 ? 553 HOH   A O    1 
HETATM 5340 O  O    . HOH   N 7 .   ? 3.417   1.818   0.004   1.00 31.37 ? 554 HOH   A O    1 
HETATM 5341 O  O    . HOH   N 7 .   ? 9.011   8.620   9.752   1.00 33.08 ? 555 HOH   A O    1 
HETATM 5342 O  O    . HOH   N 7 .   ? 43.459  14.396  25.592  1.00 51.43 ? 556 HOH   A O    1 
HETATM 5343 O  O    . HOH   N 7 .   ? 5.408   4.777   3.195   1.00 32.77 ? 557 HOH   A O    1 
HETATM 5344 O  O    . HOH   N 7 .   ? -6.671  -15.973 19.907  1.00 31.45 ? 558 HOH   A O    1 
HETATM 5345 O  O    . HOH   N 7 .   ? 15.160  2.469   1.030   1.00 38.15 ? 559 HOH   A O    1 
HETATM 5346 O  O    . HOH   N 7 .   ? 25.810  5.432   29.438  1.00 18.77 ? 560 HOH   A O    1 
HETATM 5347 O  O    . HOH   N 7 .   ? 3.320   -8.840  -6.682  1.00 31.97 ? 561 HOH   A O    1 
HETATM 5348 O  O    . HOH   N 7 .   ? -4.563  -7.467  13.458  1.00 17.64 ? 562 HOH   A O    1 
HETATM 5349 O  O    . HOH   N 7 .   ? 15.993  14.441  28.476  1.00 29.30 ? 563 HOH   A O    1 
HETATM 5350 O  O    . HOH   N 7 .   ? -4.399  -23.618 14.199  1.00 42.19 ? 564 HOH   A O    1 
HETATM 5351 O  O    . HOH   N 7 .   ? 29.400  2.035   40.048  1.00 40.29 ? 565 HOH   A O    1 
HETATM 5352 O  O    . HOH   N 7 .   ? 14.360  12.179  14.759  1.00 29.60 ? 566 HOH   A O    1 
HETATM 5353 O  O    . HOH   N 7 .   ? 2.312   -2.156  23.127  1.00 24.48 ? 567 HOH   A O    1 
HETATM 5354 O  O    . HOH   N 7 .   ? 2.391   -4.265  -5.227  1.00 33.24 ? 568 HOH   A O    1 
HETATM 5355 O  O    . HOH   N 7 .   ? 11.570  0.925   36.822  1.00 39.87 ? 569 HOH   A O    1 
HETATM 5356 O  O    . HOH   N 7 .   ? -7.142  -14.183 -1.571  1.00 39.29 ? 570 HOH   A O    1 
HETATM 5357 O  O    . HOH   N 7 .   ? 6.759   10.672  21.366  1.00 33.24 ? 571 HOH   A O    1 
HETATM 5358 O  O    . HOH   N 7 .   ? -1.717  -20.701 -12.160 1.00 44.79 ? 572 HOH   A O    1 
HETATM 5359 O  O    . HOH   N 7 .   ? 4.062   7.160   13.290  1.00 35.77 ? 573 HOH   A O    1 
HETATM 5360 O  O    . HOH   N 7 .   ? 22.081  -2.466  30.621  1.00 17.41 ? 574 HOH   A O    1 
HETATM 5361 O  O    . HOH   N 7 .   ? 2.089   -12.194 23.488  1.00 19.53 ? 575 HOH   A O    1 
HETATM 5362 O  O    . HOH   N 7 .   ? 7.371   -2.959  11.025  1.00 15.83 ? 576 HOH   A O    1 
HETATM 5363 O  O    . HOH   N 7 .   ? 3.481   -5.345  32.239  1.00 36.28 ? 577 HOH   A O    1 
HETATM 5364 O  O    . HOH   N 7 .   ? 8.757   -25.537 17.683  1.00 49.58 ? 578 HOH   A O    1 
HETATM 5365 O  O    . HOH   N 7 .   ? 3.249   -3.567  29.339  1.00 32.43 ? 579 HOH   A O    1 
HETATM 5366 O  O    . HOH   N 7 .   ? 0.477   -5.938  -0.395  1.00 19.27 ? 580 HOH   A O    1 
HETATM 5367 O  O    . HOH   N 7 .   ? 19.873  -4.335  28.435  1.00 31.32 ? 581 HOH   A O    1 
HETATM 5368 O  O    . HOH   N 7 .   ? 13.630  -9.303  21.806  1.00 20.49 ? 582 HOH   A O    1 
HETATM 5369 O  O    . HOH   N 7 .   ? 13.210  -16.523 29.288  1.00 28.93 ? 583 HOH   A O    1 
HETATM 5370 O  O    . HOH   N 7 .   ? 47.842  13.693  33.460  1.00 32.10 ? 584 HOH   A O    1 
HETATM 5371 O  O    . HOH   N 7 .   ? -4.119  -18.740 20.254  1.00 29.91 ? 585 HOH   A O    1 
HETATM 5372 O  O    . HOH   N 7 .   ? 6.210   -24.676 12.645  1.00 38.50 ? 586 HOH   A O    1 
HETATM 5373 O  O    . HOH   N 7 .   ? 2.847   -27.082 2.236   1.00 39.66 ? 587 HOH   A O    1 
HETATM 5374 O  O    . HOH   N 7 .   ? 3.896   3.499   12.186  1.00 34.20 ? 588 HOH   A O    1 
HETATM 5375 O  O    . HOH   N 7 .   ? 3.735   5.670   15.803  1.00 34.37 ? 589 HOH   A O    1 
HETATM 5376 O  O    . HOH   N 7 .   ? 21.123  -6.465  26.904  1.00 32.77 ? 590 HOH   A O    1 
HETATM 5377 O  O    . HOH   N 7 .   ? -4.829  -3.908  16.688  1.00 19.78 ? 591 HOH   A O    1 
HETATM 5378 O  O    . HOH   N 7 .   ? 3.953   -8.702  17.266  1.00 15.00 ? 592 HOH   A O    1 
HETATM 5379 O  O    . HOH   N 7 .   ? 15.206  2.486   29.458  1.00 18.44 ? 593 HOH   A O    1 
HETATM 5380 O  O    . HOH   N 7 .   ? 34.267  0.278   18.352  1.00 36.73 ? 594 HOH   A O    1 
HETATM 5381 O  O    . HOH   N 7 .   ? 17.746  -9.133  21.693  1.00 19.22 ? 595 HOH   A O    1 
HETATM 5382 O  O    . HOH   N 7 .   ? 15.315  8.317   14.907  1.00 21.40 ? 596 HOH   A O    1 
HETATM 5383 O  O    . HOH   N 7 .   ? 27.748  6.514   36.248  1.00 24.61 ? 597 HOH   A O    1 
HETATM 5384 O  O    . HOH   N 7 .   ? 17.314  -24.270 7.082   1.00 34.52 ? 598 HOH   A O    1 
HETATM 5385 O  O    . HOH   N 7 .   ? -3.521  -1.401  16.283  1.00 27.80 ? 599 HOH   A O    1 
HETATM 5386 O  O    . HOH   N 7 .   ? 23.058  -14.933 29.002  1.00 42.52 ? 600 HOH   A O    1 
HETATM 5387 O  O    . HOH   N 7 .   ? 4.372   0.088   36.162  1.00 38.44 ? 601 HOH   A O    1 
HETATM 5388 O  O    . HOH   N 7 .   ? 13.855  14.600  30.389  1.00 41.61 ? 602 HOH   A O    1 
HETATM 5389 O  O    . HOH   N 7 .   ? 5.078   -3.817  36.759  1.00 44.72 ? 603 HOH   A O    1 
HETATM 5390 O  O    . HOH   N 7 .   ? 3.448   1.823   8.458   1.00 21.19 ? 604 HOH   A O    1 
HETATM 5391 O  O    . HOH   N 7 .   ? 19.294  5.678   9.217   1.00 27.45 ? 605 HOH   A O    1 
HETATM 5392 O  O    . HOH   N 7 .   ? 11.858  5.258   1.859   1.00 37.08 ? 606 HOH   A O    1 
HETATM 5393 O  O    . HOH   N 7 .   ? -2.766  -23.258 16.394  1.00 32.28 ? 607 HOH   A O    1 
HETATM 5394 O  O    . HOH   N 7 .   ? 21.544  2.070   7.654   1.00 25.92 ? 608 HOH   A O    1 
HETATM 5395 O  O    . HOH   N 7 .   ? 2.378   -13.098 17.815  1.00 16.30 ? 609 HOH   A O    1 
HETATM 5396 O  O    . HOH   N 7 .   ? 27.046  15.180  20.120  1.00 38.65 ? 610 HOH   A O    1 
HETATM 5397 O  O    . HOH   N 7 .   ? 6.264   -1.344  -0.803  1.00 19.93 ? 611 HOH   A O    1 
HETATM 5398 O  O    . HOH   N 7 .   ? -7.267  -23.634 11.698  1.00 44.80 ? 612 HOH   A O    1 
HETATM 5399 O  O    . HOH   N 7 .   ? -3.836  1.831   14.819  1.00 35.71 ? 613 HOH   A O    1 
HETATM 5400 O  O    . HOH   N 7 .   ? 1.306   -24.371 15.248  1.00 35.80 ? 614 HOH   A O    1 
HETATM 5401 O  O    . HOH   N 7 .   ? 4.974   1.384   10.951  1.00 20.97 ? 615 HOH   A O    1 
HETATM 5402 O  O    . HOH   N 7 .   ? 3.678   -15.637 20.678  1.00 17.34 ? 616 HOH   A O    1 
HETATM 5403 O  O    . HOH   N 7 .   ? 23.715  17.426  25.495  1.00 33.57 ? 617 HOH   A O    1 
HETATM 5404 O  O    . HOH   N 7 .   ? -5.566  -12.651 3.399   1.00 20.26 ? 618 HOH   A O    1 
HETATM 5405 O  O    . HOH   N 7 .   ? -3.567  -20.554 15.831  1.00 26.12 ? 619 HOH   A O    1 
HETATM 5406 O  O    . HOH   N 7 .   ? -8.046  -8.116  -1.379  1.00 43.50 ? 620 HOH   A O    1 
HETATM 5407 O  O    . HOH   N 7 .   ? 20.279  8.053   34.086  1.00 25.21 ? 621 HOH   A O    1 
HETATM 5408 O  O    . HOH   N 7 .   ? 16.404  -7.841  -0.057  1.00 29.32 ? 622 HOH   A O    1 
HETATM 5409 O  O    . HOH   N 7 .   ? 17.663  -4.777  30.259  1.00 20.49 ? 623 HOH   A O    1 
HETATM 5410 O  O    . HOH   N 7 .   ? 13.808  -30.053 -2.218  1.00 39.98 ? 624 HOH   A O    1 
HETATM 5411 O  O    . HOH   N 7 .   ? 16.788  11.934  13.641  1.00 32.02 ? 625 HOH   A O    1 
HETATM 5412 O  O    . HOH   N 7 .   ? 19.125  11.585  34.209  1.00 35.23 ? 626 HOH   A O    1 
HETATM 5413 O  O    . HOH   N 7 .   ? 11.257  -14.973 32.501  1.00 35.65 ? 627 HOH   A O    1 
HETATM 5414 O  O    . HOH   N 7 .   ? 3.361   -1.911  33.726  1.00 38.70 ? 628 HOH   A O    1 
HETATM 5415 O  O    . HOH   N 7 .   ? 27.307  7.779   29.434  1.00 19.08 ? 629 HOH   A O    1 
HETATM 5416 O  O    . HOH   N 7 .   ? 3.999   -14.641 26.430  1.00 31.94 ? 630 HOH   A O    1 
HETATM 5417 O  O    . HOH   N 7 .   ? 23.781  -9.982  24.698  1.00 48.43 ? 631 HOH   A O    1 
HETATM 5418 O  O    . HOH   N 7 .   ? 19.759  13.302  27.298  1.00 28.32 ? 632 HOH   A O    1 
HETATM 5419 O  O    . HOH   N 7 .   ? 1.133   -11.532 10.664  1.00 16.49 ? 633 HOH   A O    1 
HETATM 5420 O  O    . HOH   N 7 .   ? -5.785  -8.504  -4.648  1.00 41.10 ? 634 HOH   A O    1 
HETATM 5421 O  O    . HOH   N 7 .   ? -5.024  -15.245 4.363   1.00 26.81 ? 635 HOH   A O    1 
HETATM 5422 O  O    . HOH   N 7 .   ? 14.324  -10.961 19.745  1.00 20.40 ? 636 HOH   A O    1 
HETATM 5423 O  O    . HOH   N 7 .   ? 32.684  -3.571  37.503  1.00 39.99 ? 637 HOH   A O    1 
HETATM 5424 O  O    . HOH   N 7 .   ? 2.077   -10.047 21.685  1.00 17.29 ? 638 HOH   A O    1 
HETATM 5425 O  O    . HOH   N 7 .   ? 32.210  -12.683 26.226  1.00 37.91 ? 639 HOH   A O    1 
HETATM 5426 O  O    . HOH   N 7 .   ? 4.463   -7.818  40.092  1.00 43.65 ? 640 HOH   A O    1 
HETATM 5427 O  O    . HOH   N 7 .   ? -8.679  -18.282 16.139  1.00 33.19 ? 641 HOH   A O    1 
HETATM 5428 O  O    . HOH   N 7 .   ? 27.401  -4.481  38.667  1.00 37.25 ? 642 HOH   A O    1 
HETATM 5429 O  O    . HOH   N 7 .   ? 33.282  -8.989  20.471  1.00 19.76 ? 643 HOH   A O    1 
HETATM 5430 O  O    . HOH   N 7 .   ? 16.758  15.050  17.588  1.00 41.22 ? 644 HOH   A O    1 
HETATM 5431 O  O    . HOH   N 7 .   ? -3.217  -20.534 22.362  1.00 35.68 ? 645 HOH   A O    1 
HETATM 5432 O  O    . HOH   N 7 .   ? 44.559  16.799  32.262  1.00 47.71 ? 646 HOH   A O    1 
HETATM 5433 O  O    . HOH   N 7 .   ? 5.521   1.271   18.704  1.00 22.68 ? 647 HOH   A O    1 
HETATM 5434 O  O    . HOH   N 7 .   ? 26.436  4.223   15.383  1.00 30.15 ? 648 HOH   A O    1 
HETATM 5435 O  O    . HOH   N 7 .   ? 42.108  16.396  32.923  1.00 46.46 ? 649 HOH   A O    1 
HETATM 5436 O  O    . HOH   N 7 .   ? 26.659  -12.210 12.120  1.00 30.50 ? 650 HOH   A O    1 
HETATM 5437 O  O    . HOH   N 7 .   ? 24.523  -9.908  20.869  1.00 36.29 ? 651 HOH   A O    1 
HETATM 5438 O  O    . HOH   N 7 .   ? 17.268  -20.475 18.788  1.00 43.87 ? 652 HOH   A O    1 
HETATM 5439 O  O    . HOH   N 7 .   ? 17.642  -21.562 9.784   1.00 36.59 ? 653 HOH   A O    1 
HETATM 5440 O  O    . HOH   N 7 .   ? 27.054  4.066   31.496  1.00 18.11 ? 654 HOH   A O    1 
HETATM 5441 O  O    . HOH   N 7 .   ? 36.388  -1.692  20.054  1.00 27.74 ? 655 HOH   A O    1 
HETATM 5442 O  O    . HOH   N 7 .   ? 32.025  8.604   17.053  1.00 40.65 ? 656 HOH   A O    1 
HETATM 5443 O  O    . HOH   N 7 .   ? 10.618  -20.764 21.201  1.00 44.98 ? 657 HOH   A O    1 
HETATM 5444 O  O    . HOH   N 7 .   ? 15.651  3.821   3.814   1.00 39.63 ? 658 HOH   A O    1 
HETATM 5445 O  O    . HOH   N 7 .   ? -3.765  -12.107 -3.224  1.00 38.12 ? 659 HOH   A O    1 
HETATM 5446 O  O    . HOH   N 7 .   ? 39.319  11.273  20.701  1.00 49.41 ? 660 HOH   A O    1 
HETATM 5447 O  O    . HOH   N 7 .   ? 4.426   -24.470 15.440  1.00 37.31 ? 661 HOH   A O    1 
HETATM 5448 O  O    . HOH   N 7 .   ? 4.763   -16.804 27.829  1.00 44.60 ? 662 HOH   A O    1 
HETATM 5449 O  O    . HOH   N 7 .   ? 28.529  2.557   19.356  1.00 25.67 ? 663 HOH   A O    1 
HETATM 5450 O  O    . HOH   N 7 .   ? 26.300  3.814   18.002  1.00 23.06 ? 664 HOH   A O    1 
HETATM 5451 O  O    . HOH   N 7 .   ? -0.432  -8.849  26.050  1.00 40.92 ? 665 HOH   A O    1 
HETATM 5452 O  O    . HOH   N 7 .   ? 4.052   4.960   32.795  1.00 42.46 ? 666 HOH   A O    1 
HETATM 5453 O  O    . HOH   N 7 .   ? 32.005  1.789   12.417  1.00 41.78 ? 667 HOH   A O    1 
HETATM 5454 O  O    . HOH   N 7 .   ? 15.356  -19.649 22.388  1.00 43.74 ? 668 HOH   A O    1 
HETATM 5455 O  O    . HOH   N 7 .   ? 4.675   -14.572 17.401  1.00 17.31 ? 669 HOH   A O    1 
HETATM 5456 O  O    . HOH   N 7 .   ? 2.314   -7.357  -2.027  1.00 21.17 ? 670 HOH   A O    1 
HETATM 5457 O  O    . HOH   N 7 .   ? 25.218  7.273   34.569  1.00 26.53 ? 671 HOH   A O    1 
HETATM 5458 O  O    . HOH   N 7 .   ? 19.490  -19.066 10.170  1.00 29.17 ? 672 HOH   A O    1 
HETATM 5459 O  O    . HOH   N 7 .   ? 9.758   -8.331  40.375  1.00 43.69 ? 673 HOH   A O    1 
HETATM 5460 O  O    . HOH   N 7 .   ? 7.819   12.457  24.309  1.00 40.64 ? 674 HOH   A O    1 
HETATM 5461 O  O    . HOH   N 7 .   ? 26.215  17.915  32.482  1.00 52.23 ? 675 HOH   A O    1 
HETATM 5462 O  O    . HOH   N 7 .   ? 2.870   7.125   28.156  1.00 40.12 ? 676 HOH   A O    1 
HETATM 5463 O  O    . HOH   N 7 .   ? 1.341   -24.353 10.612  1.00 39.52 ? 677 HOH   A O    1 
HETATM 5464 O  O    . HOH   N 7 .   ? -3.229  -0.764  -0.188  1.00 25.06 ? 678 HOH   A O    1 
HETATM 5465 O  O    . HOH   N 7 .   ? 17.626  18.349  20.372  1.00 44.90 ? 679 HOH   A O    1 
HETATM 5466 O  O    . HOH   N 7 .   ? 38.936  12.204  16.957  1.00 40.82 ? 680 HOH   A O    1 
HETATM 5467 O  O    . HOH   N 7 .   ? 11.239  3.961   35.579  1.00 24.79 ? 681 HOH   A O    1 
HETATM 5468 O  O    . HOH   N 7 .   ? 8.925   -22.539 24.190  1.00 53.12 ? 682 HOH   A O    1 
HETATM 5469 O  O    . HOH   N 7 .   ? 26.070  2.483   8.404   1.00 34.94 ? 683 HOH   A O    1 
HETATM 5470 O  O    . HOH   N 7 .   ? 28.873  13.644  34.340  1.00 29.90 ? 684 HOH   A O    1 
HETATM 5471 O  O    . HOH   N 7 .   ? 11.877  -21.019 -8.128  1.00 33.77 ? 685 HOH   A O    1 
HETATM 5472 O  O    . HOH   N 7 .   ? 6.196   -16.415 -10.114 1.00 41.72 ? 686 HOH   A O    1 
HETATM 5473 O  O    . HOH   N 7 .   ? 21.479  6.973   11.098  1.00 34.65 ? 687 HOH   A O    1 
HETATM 5474 O  O    . HOH   N 7 .   ? 20.030  -11.620 -5.088  1.00 39.86 ? 688 HOH   A O    1 
HETATM 5475 O  O    . HOH   N 7 .   ? 8.202   -26.708 6.841   1.00 36.21 ? 689 HOH   A O    1 
HETATM 5476 O  O    . HOH   N 7 .   ? -6.631  -4.444  14.351  1.00 31.03 ? 690 HOH   A O    1 
HETATM 5477 O  O    . HOH   N 7 .   ? 9.580   -26.071 15.304  1.00 41.03 ? 691 HOH   A O    1 
HETATM 5478 O  O    . HOH   N 7 .   ? 22.642  14.191  30.158  1.00 32.07 ? 692 HOH   A O    1 
HETATM 5479 O  O    . HOH   N 7 .   ? 41.243  8.718   28.670  1.00 43.72 ? 693 HOH   A O    1 
HETATM 5480 O  O    . HOH   N 7 .   ? 36.923  7.304   34.726  1.00 39.20 ? 694 HOH   A O    1 
HETATM 5481 O  O    . HOH   N 7 .   ? 20.513  -11.476 -2.562  1.00 39.21 ? 695 HOH   A O    1 
HETATM 5482 O  O    . HOH   N 7 .   ? 0.612   -27.024 3.092   1.00 35.13 ? 696 HOH   A O    1 
HETATM 5483 O  O    . HOH   N 7 .   ? -2.071  -23.223 -0.489  1.00 47.40 ? 697 HOH   A O    1 
HETATM 5484 O  O    . HOH   N 7 .   ? -6.960  -17.767 22.560  1.00 48.63 ? 698 HOH   A O    1 
HETATM 5485 O  O    . HOH   N 7 .   ? 31.421  -3.466  13.117  1.00 42.72 ? 699 HOH   A O    1 
HETATM 5486 O  O    . HOH   N 7 .   ? 40.093  -5.803  26.752  1.00 35.65 ? 700 HOH   A O    1 
HETATM 5487 O  O    . HOH   N 7 .   ? 24.716  3.859   37.961  1.00 28.52 ? 701 HOH   A O    1 
HETATM 5488 O  O    . HOH   N 7 .   ? 40.732  17.831  27.173  1.00 49.02 ? 702 HOH   A O    1 
HETATM 5489 O  O    . HOH   N 7 .   ? 20.391  -9.678  22.310  1.00 29.07 ? 703 HOH   A O    1 
HETATM 5490 O  O    . HOH   N 7 .   ? -6.165  -21.612 -3.199  1.00 39.09 ? 704 HOH   A O    1 
HETATM 5491 O  O    . HOH   N 7 .   ? 3.708   0.172   31.790  1.00 27.82 ? 705 HOH   A O    1 
HETATM 5492 O  O    . HOH   N 7 .   ? 20.468  -0.083  -2.004  1.00 42.20 ? 706 HOH   A O    1 
HETATM 5493 O  O    . HOH   N 7 .   ? 18.257  13.783  15.170  1.00 34.77 ? 707 HOH   A O    1 
HETATM 5494 O  O    . HOH   N 7 .   ? -8.881  -17.591 -0.186  1.00 42.48 ? 708 HOH   A O    1 
HETATM 5495 O  O    . HOH   N 7 .   ? 6.692   8.985   7.778   1.00 43.70 ? 709 HOH   A O    1 
HETATM 5496 O  O    . HOH   N 7 .   ? -9.145  -10.521 3.440   1.00 33.79 ? 710 HOH   A O    1 
HETATM 5497 O  O    . HOH   N 7 .   ? 37.299  7.833   31.956  1.00 34.98 ? 711 HOH   A O    1 
HETATM 5498 O  O    . HOH   N 7 .   ? 21.143  15.319  16.960  1.00 43.33 ? 712 HOH   A O    1 
HETATM 5499 O  O    . HOH   N 7 .   ? 14.607  17.821  28.552  1.00 43.12 ? 713 HOH   A O    1 
HETATM 5500 O  O    . HOH   N 7 .   ? 16.241  1.113   39.966  1.00 40.75 ? 714 HOH   A O    1 
HETATM 5501 O  O    . HOH   N 7 .   ? -13.019 -15.031 11.784  1.00 38.09 ? 715 HOH   A O    1 
HETATM 5502 O  O    . HOH   N 7 .   ? 39.658  -1.921  25.764  1.00 38.80 ? 716 HOH   A O    1 
HETATM 5503 O  O    . HOH   N 7 .   ? 38.113  12.320  38.627  1.00 52.27 ? 717 HOH   A O    1 
HETATM 5504 O  O    . HOH   N 7 .   ? -9.652  -8.307  7.595   1.00 46.47 ? 718 HOH   A O    1 
HETATM 5505 O  O    . HOH   N 7 .   ? 30.700  -11.459 23.567  1.00 48.01 ? 719 HOH   A O    1 
HETATM 5506 O  O    . HOH   N 7 .   ? 6.011   2.260   -1.252  1.00 36.66 ? 720 HOH   A O    1 
HETATM 5507 O  O    . HOH   N 7 .   ? 11.141  1.169   -3.666  1.00 44.74 ? 721 HOH   A O    1 
HETATM 5508 O  O    . HOH   N 7 .   ? 32.144  12.088  36.414  1.00 34.23 ? 722 HOH   A O    1 
HETATM 5509 O  O    . HOH   N 7 .   ? 36.103  11.588  33.750  1.00 40.65 ? 723 HOH   A O    1 
HETATM 5510 O  O    . HOH   N 7 .   ? 19.582  -14.665 21.259  1.00 50.06 ? 724 HOH   A O    1 
HETATM 5511 O  O    . HOH   N 7 .   ? -1.952  -2.284  18.940  1.00 34.31 ? 725 HOH   A O    1 
HETATM 5512 O  O    . HOH   N 7 .   ? 10.501  10.800  8.265   1.00 39.89 ? 726 HOH   A O    1 
HETATM 5513 O  O    . HOH   N 7 .   ? 26.935  -11.265 35.189  1.00 43.18 ? 727 HOH   A O    1 
HETATM 5514 O  O    . HOH   N 7 .   ? 15.350  9.879   38.139  1.00 46.83 ? 728 HOH   A O    1 
HETATM 5515 O  O    . HOH   N 7 .   ? 11.741  -20.795 26.304  1.00 43.04 ? 729 HOH   A O    1 
HETATM 5516 O  O    . HOH   N 7 .   ? 12.707  -20.820 20.636  1.00 46.24 ? 730 HOH   A O    1 
HETATM 5517 O  O    . HOH   N 7 .   ? 13.443  17.261  18.841  1.00 47.00 ? 731 HOH   A O    1 
HETATM 5518 O  O    . HOH   N 7 .   ? 6.213   -19.036 -10.465 1.00 42.46 ? 732 HOH   A O    1 
HETATM 5519 O  O    . HOH   N 7 .   ? 18.844  13.321  11.249  1.00 41.02 ? 733 HOH   A O    1 
HETATM 5520 O  O    . HOH   N 7 .   ? 1.581   2.664   26.568  1.00 44.08 ? 734 HOH   A O    1 
HETATM 5521 O  O    . HOH   N 7 .   ? 5.345   12.345  39.171  1.00 47.38 ? 735 HOH   A O    1 
HETATM 5522 O  O    . HOH   N 7 .   ? -7.698  -19.994 -4.874  1.00 40.80 ? 736 HOH   A O    1 
HETATM 5523 O  O    . HOH   N 7 .   ? 12.246  -18.857 37.168  1.00 42.88 ? 737 HOH   A O    1 
HETATM 5524 O  O    . HOH   N 7 .   ? 20.190  17.870  19.928  1.00 42.58 ? 738 HOH   A O    1 
HETATM 5525 O  O    . HOH   N 7 .   ? 18.174  6.160   35.545  1.00 37.96 ? 739 HOH   A O    1 
HETATM 5526 O  O    . HOH   N 7 .   ? 21.186  -14.149 20.384  1.00 40.42 ? 740 HOH   A O    1 
HETATM 5527 O  O    . HOH   N 7 .   ? 17.227  8.209   34.277  1.00 32.30 ? 741 HOH   A O    1 
HETATM 5528 O  O    . HOH   N 7 .   ? 19.664  -1.783  39.707  1.00 39.35 ? 742 HOH   A O    1 
HETATM 5529 O  O    . HOH   N 7 .   ? 6.793   -14.021 -8.698  1.00 38.56 ? 743 HOH   A O    1 
HETATM 5530 O  O    . HOH   N 7 .   ? 5.631   -18.582 29.660  1.00 47.30 ? 744 HOH   A O    1 
HETATM 5531 O  O    . HOH   N 7 .   ? 6.647   0.419   -3.039  1.00 37.26 ? 745 HOH   A O    1 
HETATM 5532 O  O    . HOH   N 7 .   ? -11.776 -17.344 12.937  1.00 45.86 ? 746 HOH   A O    1 
HETATM 5533 O  O    . HOH   N 7 .   ? 15.470  -17.787 25.000  1.00 46.10 ? 747 HOH   A O    1 
HETATM 5534 O  O    . HOH   N 7 .   ? 21.421  -27.154 3.591   1.00 44.91 ? 748 HOH   A O    1 
HETATM 5535 O  O    . HOH   N 7 .   ? 9.714   1.556   39.019  1.00 49.05 ? 749 HOH   A O    1 
HETATM 5536 O  O    . HOH   N 7 .   ? 3.446   -28.972 3.710   1.00 46.62 ? 750 HOH   A O    1 
HETATM 5537 O  O    . HOH   N 7 .   ? 24.177  2.819   41.003  1.00 47.11 ? 751 HOH   A O    1 
HETATM 5538 O  O    . HOH   N 7 .   ? -4.749  -19.950 18.461  1.00 39.97 ? 752 HOH   A O    1 
HETATM 5539 O  O    . HOH   N 7 .   ? -7.730  -12.141 1.713   1.00 28.68 ? 753 HOH   A O    1 
HETATM 5540 O  O    . HOH   N 7 .   ? -1.679  -23.433 -11.243 1.00 41.20 ? 754 HOH   A O    1 
HETATM 5541 O  O    . HOH   N 7 .   ? 11.288  5.663   37.936  1.00 46.46 ? 755 HOH   A O    1 
HETATM 5542 O  O    . HOH   N 7 .   ? 0.856   -3.389  26.447  1.00 43.70 ? 756 HOH   A O    1 
HETATM 5543 O  O    . HOH   N 7 .   ? 19.388  1.019   40.060  1.00 40.00 ? 757 HOH   A O    1 
HETATM 5544 O  O    . HOH   N 7 .   ? 12.619  -22.767 18.171  1.00 45.89 ? 758 HOH   A O    1 
HETATM 5545 O  O    . HOH   N 7 .   ? 2.231   -7.491  -4.698  1.00 33.28 ? 759 HOH   A O    1 
HETATM 5546 O  O    . HOH   N 7 .   ? 39.147  1.825   18.837  1.00 41.53 ? 760 HOH   A O    1 
HETATM 5547 O  O    . HOH   N 7 .   ? 31.481  -7.504  32.521  1.00 42.29 ? 761 HOH   A O    1 
HETATM 5548 O  O    . HOH   N 7 .   ? -0.674  -8.201  -4.466  1.00 49.23 ? 762 HOH   A O    1 
HETATM 5549 O  O    . HOH   N 7 .   ? 12.663  1.680   -1.377  1.00 37.38 ? 763 HOH   A O    1 
HETATM 5550 O  O    . HOH   N 7 .   ? 2.867   -2.739  37.575  1.00 47.70 ? 764 HOH   A O    1 
HETATM 5551 O  O    . HOH   N 7 .   ? 19.841  -16.998 21.364  1.00 54.65 ? 765 HOH   A O    1 
HETATM 5552 O  O    . HOH   N 7 .   ? -6.106  -11.688 -2.660  1.00 41.99 ? 766 HOH   A O    1 
HETATM 5553 O  O    . HOH   N 7 .   ? 21.899  -11.344 20.609  1.00 39.45 ? 767 HOH   A O    1 
HETATM 5554 O  O    . HOH   N 7 .   ? -3.387  3.193   13.072  1.00 42.14 ? 768 HOH   A O    1 
HETATM 5555 O  O    . HOH   N 7 .   ? 4.279   1.565   16.648  1.00 37.06 ? 769 HOH   A O    1 
HETATM 5556 O  O    . HOH   N 7 .   ? 18.020  -13.899 23.765  1.00 33.53 ? 770 HOH   A O    1 
HETATM 5557 O  O    . HOH   N 7 .   ? -2.167  -24.099 -8.836  1.00 36.04 ? 771 HOH   A O    1 
HETATM 5558 O  O    . HOH   N 7 .   ? 14.198  -22.117 19.064  1.00 57.55 ? 772 HOH   A O    1 
HETATM 5559 O  O    . HOH   N 7 .   ? 17.347  10.107  36.234  1.00 39.76 ? 773 HOH   A O    1 
HETATM 5560 O  O    . HOH   N 7 .   ? -5.330  -2.216  -1.000  1.00 41.24 ? 774 HOH   A O    1 
HETATM 5561 O  O    . HOH   N 7 .   ? 0.233   -0.502  23.129  1.00 31.19 ? 775 HOH   A O    1 
HETATM 5562 O  O    . HOH   N 7 .   ? 18.415  6.922   38.220  1.00 49.41 ? 776 HOH   A O    1 
HETATM 5563 O  O    . HOH   N 7 .   ? 1.189   -12.107 26.137  1.00 41.18 ? 777 HOH   A O    1 
HETATM 5564 O  O    . HOH   N 7 .   ? -5.494  -24.643 3.774   1.00 48.15 ? 778 HOH   A O    1 
HETATM 5565 O  O    . HOH   N 7 .   ? 3.133   2.282   19.915  1.00 35.41 ? 779 HOH   A O    1 
HETATM 5566 O  O    . HOH   N 7 .   ? 3.438   -6.762  -8.772  1.00 47.14 ? 780 HOH   A O    1 
HETATM 5567 O  O    . HOH   N 7 .   ? 20.336  -10.964 24.663  1.00 39.58 ? 781 HOH   A O    1 
HETATM 5568 O  O    . HOH   N 7 .   ? 25.042  -11.266 24.958  1.00 54.17 ? 782 HOH   A O    1 
HETATM 5569 O  O    . HOH   N 7 .   ? -0.692  -0.714  20.447  1.00 37.66 ? 783 HOH   A O    1 
HETATM 5570 O  O    . HOH   N 7 .   ? 3.844   -3.686  -7.669  1.00 43.09 ? 784 HOH   A O    1 
HETATM 5571 O  O    . HOH   N 7 .   ? -8.783  -6.234  0.621   1.00 40.25 ? 785 HOH   A O    1 
HETATM 5572 O  O    . HOH   N 7 .   ? 0.227   -24.693 12.634  1.00 39.20 ? 786 HOH   A O    1 
HETATM 5573 O  O    . HOH   N 7 .   ? 31.861  0.633   40.006  1.00 51.47 ? 787 HOH   A O    1 
HETATM 5574 O  O    . HOH   N 7 .   ? -10.135 -8.099  2.624   1.00 39.60 ? 788 HOH   A O    1 
HETATM 5575 O  O    . HOH   N 7 .   ? 21.763  2.139   41.303  1.00 48.93 ? 789 HOH   A O    1 
HETATM 5576 O  O    . HOH   N 7 .   ? -7.069  -18.362 18.504  1.00 34.08 ? 790 HOH   A O    1 
HETATM 5577 O  O    . HOH   N 7 .   ? 43.258  5.099   21.169  1.00 44.04 ? 791 HOH   A O    1 
HETATM 5578 O  O    . HOH   N 7 .   ? 37.357  9.964   35.708  1.00 40.73 ? 792 HOH   A O    1 
HETATM 5579 O  O    . HOH   N 7 .   ? 28.135  -10.480 24.932  1.00 47.73 ? 793 HOH   A O    1 
HETATM 5580 O  O    . HOH   N 7 .   ? 17.132  -16.756 25.074  1.00 45.01 ? 794 HOH   A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . LYS   A 2   ? 0.6120 0.6010 0.7078 -0.1946 -0.0560 0.0574  2   LYS   A N   
2    C  CA  . LYS   A 2   ? 0.5249 0.5307 0.6216 -0.1844 -0.0505 0.0489  2   LYS   A CA  
3    C  C   . LYS   A 2   ? 0.5607 0.5993 0.6511 -0.1897 -0.0400 0.0495  2   LYS   A C   
4    O  O   . LYS   A 2   ? 0.6292 0.6712 0.7093 -0.1979 -0.0374 0.0597  2   LYS   A O   
5    C  CB  . LYS   A 2   ? 0.5664 0.5524 0.6581 -0.1725 -0.0539 0.0522  2   LYS   A CB  
6    C  CG  . LYS   A 2   ? 0.6001 0.5696 0.7015 -0.1601 -0.0603 0.0419  2   LYS   A CG  
7    C  CD  . LYS   A 2   ? 0.5333 0.4857 0.6304 -0.1482 -0.0627 0.0445  2   LYS   A CD  
8    C  CE  . LYS   A 2   ? 0.5677 0.4903 0.6711 -0.1401 -0.0723 0.0417  2   LYS   A CE  
9    N  NZ  . LYS   A 2   ? 0.5850 0.4961 0.6878 -0.1260 -0.0737 0.0390  2   LYS   A NZ  
22   N  N   . VAL   A 3   ? 0.4658 0.5300 0.5625 -0.1845 -0.0345 0.0376  3   VAL   A N   
23   C  CA  . VAL   A 3   ? 0.4682 0.5671 0.5619 -0.1872 -0.0244 0.0343  3   VAL   A CA  
24   C  C   . VAL   A 3   ? 0.3992 0.5094 0.4915 -0.1748 -0.0204 0.0283  3   VAL   A C   
25   O  O   . VAL   A 3   ? 0.4527 0.5411 0.5438 -0.1601 -0.0246 0.0261  3   VAL   A O   
26   C  CB  . VAL   A 3   ? 0.4265 0.5502 0.5312 -0.1918 -0.0215 0.0236  3   VAL   A CB  
27   C  CG1 . VAL   A 3   ? 0.4833 0.5956 0.5902 -0.2049 -0.0256 0.0295  3   VAL   A CG1 
28   C  CG2 . VAL   A 3   ? 0.5015 0.6316 0.6178 -0.1813 -0.0244 0.0095  3   VAL   A CG2 
38   N  N   . GLN   A 4   ? 0.3972 0.5365 0.4874 -0.1737 -0.0118 0.0237  4   GLN   A N   
39   C  CA  . GLN   A 4   ? 0.4006 0.5487 0.4889 -0.1562 -0.0076 0.0157  4   GLN   A CA  
40   C  C   . GLN   A 4   ? 0.3336 0.4958 0.4325 -0.1438 -0.0077 0.0002  4   GLN   A C   
41   O  O   . GLN   A 4   ? 0.3604 0.5456 0.4691 -0.1529 -0.0061 -0.0059 4   GLN   A O   
42   C  CB  . GLN   A 4   ? 0.4486 0.6218 0.5315 -0.1616 0.0006  0.0169  4   GLN   A CB  
43   C  CG  . GLN   A 4   ? 0.6449 0.8008 0.7130 -0.1694 -0.0001 0.0320  4   GLN   A CG  
44   C  CD  . GLN   A 4   ? 0.8273 1.0032 0.8868 -0.1686 0.0075  0.0311  4   GLN   A CD  
45   O  OE1 . GLN   A 4   ? 0.8565 1.0230 0.9081 -0.1637 0.0077  0.0362  4   GLN   A OE1 
46   N  NE2 . GLN   A 4   ? 0.6420 0.8462 0.7034 -0.1734 0.0134  0.0237  4   GLN   A NE2 
55   N  N   . ALA   A 5   ? 0.3054 0.4545 0.4025 -0.1247 -0.0100 -0.0053 5   ALA   A N   
56   C  CA  . ALA   A 5   ? 0.2375 0.3974 0.3424 -0.1118 -0.0116 -0.0187 5   ALA   A CA  
57   C  C   . ALA   A 5   ? 0.2912 0.4515 0.3911 -0.0941 -0.0097 -0.0233 5   ALA   A C   
58   O  O   . ALA   A 5   ? 0.3011 0.4549 0.3926 -0.0933 -0.0065 -0.0166 5   ALA   A O   
59   C  CB  . ALA   A 5   ? 0.3334 0.4728 0.4406 -0.1088 -0.0188 -0.0204 5   ALA   A CB  
65   N  N   . LYS   A 6   ? 0.2358 0.4037 0.3406 -0.0812 -0.0123 -0.0337 6   LYS   A N   
66   C  CA  . LYS   A 6   ? 0.2179 0.3837 0.3183 -0.0647 -0.0123 -0.0376 6   LYS   A CA  
67   C  C   . LYS   A 6   ? 0.2366 0.3842 0.3328 -0.0527 -0.0185 -0.0400 6   LYS   A C   
68   O  O   . LYS   A 6   ? 0.2617 0.4111 0.3633 -0.0537 -0.0229 -0.0450 6   LYS   A O   
69   C  CB  . LYS   A 6   ? 0.2215 0.4165 0.3319 -0.0594 -0.0107 -0.0485 6   LYS   A CB  
70   C  CG  . LYS   A 6   ? 0.2917 0.5097 0.4058 -0.0689 -0.0035 -0.0489 6   LYS   A CG  
71   C  CD  . LYS   A 6   ? 0.3882 0.5966 0.4921 -0.0646 0.0002  -0.0432 6   LYS   A CD  
72   C  CE  . LYS   A 6   ? 0.4905 0.7244 0.5971 -0.0760 0.0076  -0.0442 6   LYS   A CE  
73   N  NZ  . LYS   A 6   ? 0.4851 0.7230 0.5887 -0.0666 0.0106  -0.0474 6   LYS   A NZ  
87   N  N   . GLY   A 7   ? 0.2198 0.3517 0.3061 -0.0419 -0.0186 -0.0371 7   GLY   A N   
88   C  CA  . GLY   A 7   ? 0.2122 0.3274 0.2918 -0.0319 -0.0235 -0.0384 7   GLY   A CA  
89   C  C   . GLY   A 7   ? 0.1706 0.2899 0.2479 -0.0184 -0.0262 -0.0431 7   GLY   A C   
90   O  O   . GLY   A 7   ? 0.2085 0.3287 0.2831 -0.0136 -0.0235 -0.0414 7   GLY   A O   
94   N  N   . MET   A 8   ? 0.2039 0.3252 0.2821 -0.0124 -0.0323 -0.0488 8   MET   A N   
95   C  CA  . MET   A 8   ? 0.2163 0.3379 0.2910 0.0003  -0.0375 -0.0519 8   MET   A CA  
96   C  C   . MET   A 8   ? 0.2050 0.3055 0.2650 0.0053  -0.0403 -0.0478 8   MET   A C   
97   O  O   . MET   A 8   ? 0.2199 0.3139 0.2772 0.0012  -0.0415 -0.0483 8   MET   A O   
98   C  CB  . MET   A 8   ? 0.2909 0.4310 0.3763 0.0031  -0.0438 -0.0610 8   MET   A CB  
99   C  CG  . MET   A 8   ? 0.2910 0.4298 0.3732 0.0162  -0.0518 -0.0637 8   MET   A CG  
100  S  SD  . MET   A 8   ? 0.3492 0.5140 0.4483 0.0193  -0.0595 -0.0755 8   MET   A SD  
101  C  CE  . MET   A 8   ? 0.4646 0.6464 0.5768 0.0258  -0.0583 -0.0811 8   MET   A CE  
111  N  N   . GLY   A 9   ? 0.2044 0.2953 0.2553 0.0137  -0.0415 -0.0444 9   GLY   A N   
112  C  CA  . GLY   A 9   ? 0.2184 0.2922 0.2544 0.0173  -0.0438 -0.0406 9   GLY   A CA  
113  C  C   . GLY   A 9   ? 0.2318 0.2952 0.2586 0.0244  -0.0444 -0.0356 9   GLY   A C   
114  O  O   . GLY   A 9   ? 0.2313 0.3010 0.2643 0.0292  -0.0456 -0.0369 9   GLY   A O   
118  N  N   . PHE   A 10  ? 0.2175 0.2654 0.2302 0.0248  -0.0434 -0.0307 10  PHE   A N   
119  C  CA  . PHE   A 10  ? 0.1927 0.2293 0.1946 0.0305  -0.0452 -0.0253 10  PHE   A CA  
120  C  C   . PHE   A 10  ? 0.2024 0.2279 0.1987 0.0274  -0.0377 -0.0200 10  PHE   A C   
121  O  O   . PHE   A 10  ? 0.2110 0.2357 0.2102 0.0216  -0.0321 -0.0202 10  PHE   A O   
122  C  CB  . PHE   A 10  ? 0.2375 0.2681 0.2259 0.0331  -0.0520 -0.0239 10  PHE   A CB  
123  C  CG  . PHE   A 10  ? 0.2620 0.3037 0.2563 0.0367  -0.0607 -0.0291 10  PHE   A CG  
124  C  CD1 . PHE   A 10  ? 0.2656 0.3105 0.2653 0.0444  -0.0681 -0.0297 10  PHE   A CD1 
125  C  CD2 . PHE   A 10  ? 0.2489 0.2990 0.2461 0.0327  -0.0618 -0.0346 10  PHE   A CD2 
126  C  CE1 . PHE   A 10  ? 0.3106 0.3674 0.3181 0.0484  -0.0768 -0.0355 10  PHE   A CE1 
127  C  CE2 . PHE   A 10  ? 0.2890 0.3511 0.2929 0.0359  -0.0700 -0.0400 10  PHE   A CE2 
128  C  CZ  . PHE   A 10  ? 0.2907 0.3568 0.3001 0.0439  -0.0775 -0.0404 10  PHE   A CZ  
138  N  N   . GLY   A 11  ? 0.2078 0.2244 0.1973 0.0317  -0.0386 -0.0154 11  GLY   A N   
139  C  CA  . GLY   A 11  ? 0.2297 0.2359 0.2131 0.0295  -0.0325 -0.0105 11  GLY   A CA  
140  C  C   . GLY   A 11  ? 0.2147 0.2090 0.1858 0.0333  -0.0363 -0.0051 11  GLY   A C   
141  O  O   . GLY   A 11  ? 0.2357 0.2287 0.2028 0.0376  -0.0444 -0.0046 11  GLY   A O   
145  N  N   . GLY   A 12  ? 0.2329 0.2181 0.1982 0.0311  -0.0311 -0.0008 12  GLY   A N   
146  C  CA  . GLY   A 12  ? 0.2472 0.2201 0.2005 0.0327  -0.0340 0.0053  12  GLY   A CA  
147  C  C   . GLY   A 12  ? 0.2558 0.2232 0.1939 0.0277  -0.0325 0.0085  12  GLY   A C   
148  O  O   . GLY   A 12  ? 0.2507 0.2237 0.1886 0.0239  -0.0284 0.0048  12  GLY   A O   
152  N  N   . ASN   A 13  ? 0.2704 0.2270 0.1955 0.0274  -0.0362 0.0151  13  ASN   A N   
153  C  CA  . ASN   A 13  ? 0.2833 0.2368 0.1919 0.0212  -0.0344 0.0184  13  ASN   A CA  
154  C  C   . ASN   A 13  ? 0.3119 0.2545 0.2056 0.0212  -0.0434 0.0266  13  ASN   A C   
155  O  O   . ASN   A 13  ? 0.3270 0.2632 0.2250 0.0272  -0.0519 0.0290  13  ASN   A O   
156  C  CB  . ASN   A 13  ? 0.2511 0.2033 0.1580 0.0159  -0.0247 0.0188  13  ASN   A CB  
157  C  CG  . ASN   A 13  ? 0.2851 0.2271 0.1926 0.0167  -0.0243 0.0241  13  ASN   A CG  
158  O  OD1 . ASN   A 13  ? 0.3080 0.2397 0.2076 0.0177  -0.0312 0.0304  13  ASN   A OD1 
159  N  ND2 . ASN   A 13  ? 0.2837 0.2278 0.1994 0.0155  -0.0168 0.0219  13  ASN   A ND2 
166  N  N   . ARG   A 14  ? 0.3307 0.2718 0.2067 0.0140  -0.0422 0.0307  14  ARG   A N   
167  C  CA  . ARG   A 14  ? 0.3707 0.3013 0.2292 0.0119  -0.0518 0.0401  14  ARG   A CA  
168  C  C   . ARG   A 14  ? 0.4073 0.3214 0.2646 0.0131  -0.0560 0.0482  14  ARG   A C   
169  O  O   . ARG   A 14  ? 0.4643 0.3664 0.3148 0.0155  -0.0679 0.0554  14  ARG   A O   
170  C  CB  . ARG   A 14  ? 0.4251 0.3594 0.2632 0.0015  -0.0480 0.0431  14  ARG   A CB  
171  C  CG  . ARG   A 14  ? 0.5866 0.5360 0.4214 -0.0007 -0.0463 0.0355  14  ARG   A CG  
172  C  CD  . ARG   A 14  ? 0.7790 0.7305 0.5888 -0.0110 -0.0467 0.0409  14  ARG   A CD  
173  N  NE  . ARG   A 14  ? 0.8811 0.8496 0.6893 -0.0168 -0.0366 0.0309  14  ARG   A NE  
174  C  CZ  . ARG   A 14  ? 0.8071 0.7882 0.6214 -0.0145 -0.0363 0.0205  14  ARG   A CZ  
175  N  NH1 . ARG   A 14  ? 0.8233 0.8036 0.6447 -0.0075 -0.0451 0.0194  14  ARG   A NH1 
176  N  NH2 . ARG   A 14  ? 0.8392 0.8347 0.6539 -0.0192 -0.0273 0.0101  14  ARG   A NH2 
190  N  N   . LYS   A 15  ? 0.4013 0.3139 0.2652 0.0113  -0.0474 0.0471  15  LYS   A N   
191  C  CA  . LYS   A 15  ? 0.4437 0.3406 0.3069 0.0117  -0.0510 0.0538  15  LYS   A CA  
192  C  C   . LYS   A 15  ? 0.4106 0.3037 0.2911 0.0226  -0.0580 0.0502  15  LYS   A C   
193  O  O   . LYS   A 15  ? 0.4574 0.3362 0.3357 0.0263  -0.0692 0.0557  15  LYS   A O   
194  C  CB  . LYS   A 15  ? 0.3694 0.2678 0.2347 0.0062  -0.0396 0.0528  15  LYS   A CB  
195  C  CG  . LYS   A 15  ? 0.4427 0.3257 0.3094 0.0064  -0.0427 0.0583  15  LYS   A CG  
196  C  CD  . LYS   A 15  ? 0.4347 0.3208 0.3020 -0.0002 -0.0316 0.0574  15  LYS   A CD  
197  C  CE  . LYS   A 15  ? 0.4669 0.3380 0.3363 -0.0005 -0.0346 0.0620  15  LYS   A CE  
198  N  NZ  . LYS   A 15  ? 0.4998 0.3755 0.3685 -0.0082 -0.0240 0.0612  15  LYS   A NZ  
212  N  N   . ILE   A 16  ? 0.3835 0.2893 0.2814 0.0275  -0.0521 0.0407  16  ILE   A N   
213  C  CA  . ILE   A 16  ? 0.3821 0.2885 0.2971 0.0367  -0.0569 0.0354  16  ILE   A CA  
214  C  C   . ILE   A 16  ? 0.3473 0.2609 0.2693 0.0437  -0.0655 0.0311  16  ILE   A C   
215  O  O   . ILE   A 16  ? 0.3863 0.3006 0.3220 0.0520  -0.0720 0.0263  16  ILE   A O   
216  C  CB  . ILE   A 16  ? 0.3549 0.2727 0.2842 0.0371  -0.0464 0.0282  16  ILE   A CB  
217  C  CG1 . ILE   A 16  ? 0.3605 0.2946 0.2960 0.0361  -0.0409 0.0220  16  ILE   A CG1 
218  C  CG2 . ILE   A 16  ? 0.4219 0.3340 0.3448 0.0303  -0.0384 0.0320  16  ILE   A CG2 
219  C  CD1 . ILE   A 16  ? 0.3913 0.3347 0.3376 0.0345  -0.0314 0.0172  16  ILE   A CD1 
231  N  N   . GLY   A 17  ? 0.3347 0.2546 0.2483 0.0407  -0.0662 0.0315  17  GLY   A N   
232  C  CA  . GLY   A 17  ? 0.3650 0.2930 0.2850 0.0466  -0.0745 0.0271  17  GLY   A CA  
233  C  C   . GLY   A 17  ? 0.2881 0.2351 0.2213 0.0466  -0.0670 0.0175  17  GLY   A C   
234  O  O   . GLY   A 17  ? 0.3133 0.2663 0.2535 0.0436  -0.0567 0.0142  17  GLY   A O   
238  N  N   . GLU   A 18  ? 0.3453 0.3012 0.2817 0.0496  -0.0733 0.0137  18  GLU   A N   
239  C  CA  . GLU   A 18  ? 0.3073 0.2807 0.2561 0.0489  -0.0683 0.0050  18  GLU   A CA  
240  C  C   . GLU   A 18  ? 0.3058 0.2898 0.2745 0.0562  -0.0719 -0.0026 18  GLU   A C   
241  O  O   . GLU   A 18  ? 0.4078 0.3876 0.3802 0.0637  -0.0824 -0.0026 18  GLU   A O   
242  C  CB  . GLU   A 18  ? 0.4017 0.3801 0.3420 0.0468  -0.0730 0.0043  18  GLU   A CB  
243  C  CG  . GLU   A 18  ? 0.4066 0.4004 0.3567 0.0435  -0.0671 -0.0038 18  GLU   A CG  
244  C  CD  . GLU   A 18  ? 0.4833 0.4818 0.4242 0.0413  -0.0721 -0.0053 18  GLU   A CD  
245  O  OE1 . GLU   A 18  ? 0.4858 0.4789 0.4105 0.0358  -0.0694 -0.0017 18  GLU   A OE1 
246  O  OE2 . GLU   A 18  ? 0.4179 0.4272 0.3681 0.0447  -0.0782 -0.0109 18  GLU   A OE2 
253  N  N   . TYR   A 19  ? 0.2686 0.2666 0.2505 0.0537  -0.0636 -0.0091 19  TYR   A N   
254  C  CA  . TYR   A 19  ? 0.2490 0.2623 0.2500 0.0586  -0.0651 -0.0177 19  TYR   A CA  
255  C  C   . TYR   A 19  ? 0.2487 0.2790 0.2583 0.0533  -0.0600 -0.0236 19  TYR   A C   
256  O  O   . TYR   A 19  ? 0.2631 0.2910 0.2651 0.0465  -0.0550 -0.0212 19  TYR   A O   
257  C  CB  . TYR   A 19  ? 0.2679 0.2816 0.2767 0.0598  -0.0596 -0.0193 19  TYR   A CB  
258  C  CG  . TYR   A 19  ? 0.2397 0.2474 0.2410 0.0520  -0.0489 -0.0144 19  TYR   A CG  
259  C  CD1 . TYR   A 19  ? 0.2626 0.2814 0.2693 0.0452  -0.0406 -0.0167 19  TYR   A CD1 
260  C  CD2 . TYR   A 19  ? 0.2668 0.2574 0.2557 0.0511  -0.0480 -0.0070 19  TYR   A CD2 
261  C  CE1 . TYR   A 19  ? 0.2500 0.2624 0.2509 0.0390  -0.0325 -0.0122 19  TYR   A CE1 
262  C  CE2 . TYR   A 19  ? 0.2615 0.2479 0.2450 0.0446  -0.0388 -0.0035 19  TYR   A CE2 
263  C  CZ  . TYR   A 19  ? 0.2460 0.2431 0.2359 0.0392  -0.0316 -0.0062 19  TYR   A CZ  
264  O  OH  . TYR   A 19  ? 0.2752 0.2672 0.2608 0.0338  -0.0242 -0.0027 19  TYR   A OH  
274  N  N   . GLN   A 20  ? 0.2432 0.2916 0.2699 0.0560  -0.0615 -0.0322 20  GLN   A N   
275  C  CA  . GLN   A 20  ? 0.2415 0.3069 0.2775 0.0504  -0.0583 -0.0379 20  GLN   A CA  
276  C  C   . GLN   A 20  ? 0.2025 0.2839 0.2520 0.0457  -0.0501 -0.0428 20  GLN   A C   
277  O  O   . GLN   A 20  ? 0.2308 0.3235 0.2919 0.0507  -0.0514 -0.0491 20  GLN   A O   
278  C  CB  . GLN   A 20  ? 0.2678 0.3446 0.3116 0.0559  -0.0683 -0.0444 20  GLN   A CB  
279  C  CG  . GLN   A 20  ? 0.2729 0.3656 0.3247 0.0488  -0.0656 -0.0497 20  GLN   A CG  
280  C  CD  . GLN   A 20  ? 0.3747 0.4843 0.4393 0.0544  -0.0747 -0.0584 20  GLN   A CD  
281  O  OE1 . GLN   A 20  ? 0.3761 0.4799 0.4377 0.0634  -0.0856 -0.0581 20  GLN   A OE1 
282  N  NE2 . GLN   A 20  ? 0.4370 0.5673 0.5157 0.0484  -0.0711 -0.0659 20  GLN   A NE2 
291  N  N   . PHE   A 21  ? 0.1937 0.2766 0.2417 0.0358  -0.0423 -0.0405 21  PHE   A N   
292  C  CA  . PHE   A 21  ? 0.1900 0.2900 0.2494 0.0283  -0.0354 -0.0440 21  PHE   A CA  
293  C  C   . PHE   A 21  ? 0.2018 0.3232 0.2750 0.0275  -0.0389 -0.0528 21  PHE   A C   
294  O  O   . PHE   A 21  ? 0.2193 0.3403 0.2914 0.0247  -0.0418 -0.0533 21  PHE   A O   
295  C  CB  . PHE   A 21  ? 0.1928 0.2843 0.2459 0.0180  -0.0287 -0.0375 21  PHE   A CB  
296  C  CG  . PHE   A 21  ? 0.1873 0.2602 0.2287 0.0188  -0.0253 -0.0300 21  PHE   A CG  
297  C  CD1 . PHE   A 21  ? 0.1944 0.2692 0.2369 0.0184  -0.0207 -0.0286 21  PHE   A CD1 
298  C  CD2 . PHE   A 21  ? 0.2112 0.2668 0.2407 0.0200  -0.0268 -0.0254 21  PHE   A CD2 
299  C  CE1 . PHE   A 21  ? 0.2092 0.2679 0.2418 0.0192  -0.0180 -0.0222 21  PHE   A CE1 
300  C  CE2 . PHE   A 21  ? 0.1810 0.2220 0.2010 0.0205  -0.0236 -0.0195 21  PHE   A CE2 
301  C  CZ  . PHE   A 21  ? 0.2084 0.2502 0.2302 0.0201  -0.0194 -0.0176 21  PHE   A CZ  
311  N  N   . GLY   A 22  ? 0.1934 0.3347 0.2804 0.0304  -0.0389 -0.0611 22  GLY   A N   
312  C  CA  . GLY   A 22  ? 0.1885 0.3524 0.2907 0.0318  -0.0432 -0.0714 22  GLY   A CA  
313  C  C   . GLY   A 22  ? 0.1566 0.3253 0.2672 0.0457  -0.0528 -0.0790 22  GLY   A C   
314  O  O   . GLY   A 22  ? 0.1956 0.3861 0.3218 0.0484  -0.0571 -0.0895 22  GLY   A O   
318  N  N   . LYS   A 23  ? 0.1910 0.3395 0.2922 0.0544  -0.0572 -0.0741 23  LYS   A N   
319  C  CA  . LYS   A 23  ? 0.2193 0.3679 0.3285 0.0684  -0.0684 -0.0803 23  LYS   A CA  
320  C  C   . LYS   A 23  ? 0.2659 0.4013 0.3714 0.0736  -0.0674 -0.0779 23  LYS   A C   
321  O  O   . LYS   A 23  ? 0.2730 0.4234 0.3943 0.0800  -0.0688 -0.0886 23  LYS   A O   
322  C  CB  . LYS   A 23  ? 0.2815 0.4135 0.3801 0.0740  -0.0798 -0.0748 23  LYS   A CB  
323  C  CG  . LYS   A 23  ? 0.3764 0.5063 0.4829 0.0881  -0.0942 -0.0798 23  LYS   A CG  
324  C  CD  . LYS   A 23  ? 0.5735 0.6836 0.6646 0.0921  -0.1057 -0.0713 23  LYS   A CD  
325  C  CE  . LYS   A 23  ? 0.6934 0.8041 0.7948 0.1056  -0.1221 -0.0767 23  LYS   A CE  
326  N  NZ  . LYS   A 23  ? 0.8724 0.9733 0.9795 0.1139  -0.1256 -0.0784 23  LYS   A NZ  
340  N  N   . ASP   A 24  ? 0.2088 0.3189 0.2957 0.0712  -0.0652 -0.0658 24  ASP   A N   
341  C  CA  . ASP   A 24  ? 0.2153 0.3113 0.2976 0.0750  -0.0642 -0.0628 24  ASP   A CA  
342  C  C   . ASP   A 24  ? 0.2668 0.3727 0.3512 0.0667  -0.0516 -0.0638 24  ASP   A C   
343  O  O   . ASP   A 24  ? 0.2945 0.4034 0.3850 0.0705  -0.0503 -0.0686 24  ASP   A O   
344  C  CB  . ASP   A 24  ? 0.3094 0.3764 0.3709 0.0743  -0.0668 -0.0496 24  ASP   A CB  
345  C  CG  . ASP   A 24  ? 0.3634 0.4192 0.4197 0.0815  -0.0801 -0.0469 24  ASP   A CG  
346  O  OD1 . ASP   A 24  ? 0.3957 0.4516 0.4618 0.0919  -0.0908 -0.0522 24  ASP   A OD1 
347  O  OD2 . ASP   A 24  ? 0.2962 0.3452 0.3397 0.0766  -0.0804 -0.0404 24  ASP   A OD2 
352  N  N   . LEU   A 25  ? 0.2133 0.3233 0.2924 0.0555  -0.0433 -0.0592 25  LEU   A N   
353  C  CA  . LEU   A 25  ? 0.1911 0.3080 0.2690 0.0457  -0.0324 -0.0572 25  LEU   A CA  
354  C  C   . LEU   A 25  ? 0.1902 0.3289 0.2764 0.0362  -0.0278 -0.0611 25  LEU   A C   
355  O  O   . LEU   A 25  ? 0.2113 0.3550 0.3014 0.0365  -0.0324 -0.0635 25  LEU   A O   
356  C  CB  . LEU   A 25  ? 0.2332 0.3272 0.2940 0.0403  -0.0283 -0.0448 25  LEU   A CB  
357  C  CG  . LEU   A 25  ? 0.2821 0.3562 0.3340 0.0466  -0.0305 -0.0402 25  LEU   A CG  
358  C  CD1 . LEU   A 25  ? 0.3018 0.3565 0.3382 0.0411  -0.0268 -0.0294 25  LEU   A CD1 
359  C  CD2 . LEU   A 25  ? 0.3117 0.3945 0.3705 0.0480  -0.0268 -0.0455 25  LEU   A CD2 
371  N  N   . PRO   A 26  ? 0.1679 0.3199 0.2564 0.0266  -0.0191 -0.0613 26  PRO   A N   
372  C  CA  . PRO   A 26  ? 0.1680 0.3393 0.2629 0.0151  -0.0147 -0.0631 26  PRO   A CA  
373  C  C   . PRO   A 26  ? 0.1857 0.3421 0.2723 0.0086  -0.0156 -0.0546 26  PRO   A C   
374  O  O   . PRO   A 26  ? 0.2206 0.3530 0.2947 0.0107  -0.0170 -0.0463 26  PRO   A O   
375  C  CB  . PRO   A 26  ? 0.2068 0.3884 0.3000 0.0050  -0.0057 -0.0611 26  PRO   A CB  
376  C  CG  . PRO   A 26  ? 0.2094 0.3885 0.3032 0.0147  -0.0063 -0.0654 26  PRO   A CG  
377  C  CD  . PRO   A 26  ? 0.1881 0.3386 0.2727 0.0248  -0.0133 -0.0594 26  PRO   A CD  
385  N  N   . LEU   A 27  ? 0.1953 0.3680 0.2898 0.0001  -0.0146 -0.0578 27  LEU   A N   
386  C  CA  . LEU   A 27  ? 0.1896 0.3508 0.2787 -0.0082 -0.0149 -0.0510 27  LEU   A CA  
387  C  C   . LEU   A 27  ? 0.2245 0.3712 0.3035 -0.0173 -0.0096 -0.0403 27  LEU   A C   
388  O  O   . LEU   A 27  ? 0.2082 0.3615 0.2861 -0.0214 -0.0044 -0.0385 27  LEU   A O   
389  C  CB  . LEU   A 27  ? 0.1877 0.3718 0.2891 -0.0172 -0.0144 -0.0571 27  LEU   A CB  
390  C  CG  . LEU   A 27  ? 0.1759 0.3723 0.2877 -0.0085 -0.0215 -0.0674 27  LEU   A CG  
391  C  CD1 . LEU   A 27  ? 0.2459 0.4711 0.3724 -0.0190 -0.0192 -0.0749 27  LEU   A CD1 
392  C  CD2 . LEU   A 27  ? 0.2435 0.4205 0.3479 -0.0030 -0.0286 -0.0645 27  LEU   A CD2 
404  N  N   . LEU   A 28  ? 0.1988 0.3262 0.2709 -0.0201 -0.0116 -0.0340 28  LEU   A N   
405  C  CA  . LEU   A 28  ? 0.1829 0.2940 0.2469 -0.0273 -0.0087 -0.0243 28  LEU   A CA  
406  C  C   . LEU   A 28  ? 0.1825 0.3024 0.2515 -0.0425 -0.0066 -0.0210 28  LEU   A C   
407  O  O   . LEU   A 28  ? 0.2060 0.3375 0.2831 -0.0474 -0.0084 -0.0256 28  LEU   A O   
408  C  CB  . LEU   A 28  ? 0.1899 0.2781 0.2467 -0.0230 -0.0124 -0.0211 28  LEU   A CB  
409  C  CG  . LEU   A 28  ? 0.1904 0.2675 0.2394 -0.0105 -0.0146 -0.0221 28  LEU   A CG  
410  C  CD1 . LEU   A 28  ? 0.2119 0.2735 0.2552 -0.0084 -0.0180 -0.0216 28  LEU   A CD1 
411  C  CD2 . LEU   A 28  ? 0.2353 0.3043 0.2778 -0.0083 -0.0109 -0.0171 28  LEU   A CD2 
423  N  N   . GLU   A 29  ? 0.2283 0.3421 0.2918 -0.0504 -0.0034 -0.0126 29  GLU   A N   
424  C  CA  . GLU   A 29  ? 0.2487 0.3675 0.3144 -0.0666 -0.0023 -0.0066 29  GLU   A CA  
425  C  C   . GLU   A 29  ? 0.2088 0.3031 0.2722 -0.0700 -0.0073 -0.0002 29  GLU   A C   
426  O  O   . GLU   A 29  ? 0.2317 0.3062 0.2884 -0.0666 -0.0085 0.0058  29  GLU   A O   
427  C  CB  . GLU   A 29  ? 0.3776 0.5029 0.4377 -0.0743 0.0025  -0.0001 29  GLU   A CB  
428  C  CG  . GLU   A 29  ? 0.4552 0.5970 0.5155 -0.0661 0.0068  -0.0071 29  GLU   A CG  
429  C  CD  . GLU   A 29  ? 0.5800 0.7535 0.6510 -0.0688 0.0099  -0.0177 29  GLU   A CD  
430  O  OE1 . GLU   A 29  ? 0.5142 0.6977 0.5919 -0.0777 0.0091  -0.0191 29  GLU   A OE1 
431  O  OE2 . GLU   A 29  ? 0.6230 0.8121 0.6969 -0.0620 0.0129  -0.0255 29  GLU   A OE2 
438  N  N   . ILE   A 30  ? 0.2768 0.3732 0.3472 -0.0767 -0.0105 -0.0025 30  ILE   A N   
439  C  CA  . ILE   A 30  ? 0.2785 0.3527 0.3496 -0.0794 -0.0161 0.0009  30  ILE   A CA  
440  C  C   . ILE   A 30  ? 0.2560 0.3328 0.3322 -0.0969 -0.0179 0.0064  30  ILE   A C   
441  O  O   . ILE   A 30  ? 0.2806 0.3774 0.3582 -0.1075 -0.0138 0.0083  30  ILE   A O   
442  C  CB  . ILE   A 30  ? 0.2220 0.2920 0.2962 -0.0694 -0.0199 -0.0084 30  ILE   A CB  
443  C  CG1 . ILE   A 30  ? 0.2457 0.3386 0.3285 -0.0716 -0.0199 -0.0168 30  ILE   A CG1 
444  C  CG2 . ILE   A 30  ? 0.2436 0.3083 0.3105 -0.0542 -0.0188 -0.0115 30  ILE   A CG2 
445  C  CD1 . ILE   A 30  ? 0.2801 0.3690 0.3664 -0.0657 -0.0251 -0.0249 30  ILE   A CD1 
457  N  N   . THR   A 31  ? 0.2705 0.3273 0.3499 -0.1004 -0.0243 0.0085  31  THR   A N   
458  C  CA  . THR   A 31  ? 0.3203 0.3747 0.4050 -0.1174 -0.0278 0.0144  31  THR   A CA  
459  C  C   . THR   A 31  ? 0.3175 0.3656 0.4112 -0.1165 -0.0335 0.0063  31  THR   A C   
460  O  O   . THR   A 31  ? 0.2838 0.3218 0.3775 -0.1034 -0.0359 -0.0012 31  THR   A O   
461  C  CB  . THR   A 31  ? 0.3966 0.4276 0.4768 -0.1252 -0.0325 0.0275  31  THR   A CB  
462  O  OG1 . THR   A 31  ? 0.3982 0.4077 0.4755 -0.1117 -0.0356 0.0266  31  THR   A OG1 
463  C  CG2 . THR   A 31  ? 0.3849 0.4278 0.4567 -0.1338 -0.0274 0.0371  31  THR   A CG2 
471  N  N   . ARG   A 32  ? 0.3034 0.3584 0.4043 -0.1315 -0.0355 0.0075  32  ARG   A N   
472  C  CA  . ARG   A 32  ? 0.3016 0.3529 0.4120 -0.1320 -0.0409 -0.0011 32  ARG   A CA  
473  C  C   . ARG   A 32  ? 0.3727 0.4102 0.4890 -0.1498 -0.0472 0.0066  32  ARG   A C   
474  O  O   . ARG   A 32  ? 0.4087 0.4534 0.5230 -0.1657 -0.0453 0.0168  32  ARG   A O   
475  C  CB  . ARG   A 32  ? 0.3228 0.4037 0.4395 -0.1306 -0.0372 -0.0120 32  ARG   A CB  
476  C  CG  . ARG   A 32  ? 0.3545 0.4357 0.4816 -0.1332 -0.0428 -0.0211 32  ARG   A CG  
477  C  CD  . ARG   A 32  ? 0.3485 0.4561 0.4802 -0.1248 -0.0405 -0.0336 32  ARG   A CD  
478  N  NE  . ARG   A 32  ? 0.3398 0.4461 0.4791 -0.1228 -0.0464 -0.0439 32  ARG   A NE  
479  C  CZ  . ARG   A 32  ? 0.3769 0.4977 0.5274 -0.1341 -0.0484 -0.0488 32  ARG   A CZ  
480  N  NH1 . ARG   A 32  ? 0.4010 0.5375 0.5565 -0.1504 -0.0448 -0.0435 32  ARG   A NH1 
481  N  NH2 . ARG   A 32  ? 0.3797 0.5007 0.5362 -0.1298 -0.0539 -0.0596 32  ARG   A NH2 
495  N  N   . ASP   A 33  ? 0.3710 0.3886 0.4943 -0.1475 -0.0551 0.0016  33  ASP   A N   
496  C  CA  . ASP   A 33  ? 0.4037 0.4074 0.5356 -0.1634 -0.0628 0.0058  33  ASP   A CA  
497  C  C   . ASP   A 33  ? 0.3764 0.3962 0.5184 -0.1654 -0.0635 -0.0068 33  ASP   A C   
498  O  O   . ASP   A 33  ? 0.4269 0.4384 0.5740 -0.1552 -0.0680 -0.0182 33  ASP   A O   
499  C  CB  . ASP   A 33  ? 0.4090 0.3781 0.5436 -0.1588 -0.0723 0.0075  33  ASP   A CB  
500  C  CG  . ASP   A 33  ? 0.4838 0.4377 0.6221 -0.1683 -0.0768 0.0111  33  ASP   A CG  
501  O  OD1 . ASP   A 33  ? 0.4739 0.4436 0.6151 -0.1803 -0.0739 0.0113  33  ASP   A OD1 
502  O  OD2 . ASP   A 33  ? 0.5438 0.4707 0.6829 -0.1635 -0.0838 0.0131  33  ASP   A OD2 
507  N  N   . SER   A 34  ? 0.4385 0.4832 0.5837 -0.1792 -0.0591 -0.0053 34  SER   A N   
508  C  CA  . SER   A 34  ? 0.4216 0.4876 0.5768 -0.1800 -0.0588 -0.0182 34  SER   A CA  
509  C  C   . SER   A 34  ? 0.4719 0.5195 0.6368 -0.1845 -0.0671 -0.0232 34  SER   A C   
510  O  O   . SER   A 34  ? 0.4936 0.5521 0.6671 -0.1816 -0.0701 -0.0362 34  SER   A O   
511  C  CB  . SER   A 34  ? 0.5401 0.6358 0.6969 -0.1904 -0.0507 -0.0161 34  SER   A CB  
512  O  OG  . SER   A 34  ? 0.6658 0.7829 0.8159 -0.1844 -0.0432 -0.0162 34  SER   A OG  
518  N  N   . SER   A 35  ? 0.4800 0.5003 0.6427 -0.1897 -0.0705 -0.0140 35  SER   A N   
519  C  CA  . SER   A 35  ? 0.5185 0.5209 0.6892 -0.1929 -0.0773 -0.0195 35  SER   A CA  
520  C  C   . SER   A 35  ? 0.5075 0.4978 0.6818 -0.1789 -0.0838 -0.0327 35  SER   A C   
521  O  O   . SER   A 35  ? 0.5192 0.5085 0.7012 -0.1795 -0.0880 -0.0435 35  SER   A O   
522  C  CB  . SER   A 35  ? 0.5272 0.5015 0.6929 -0.1994 -0.0808 -0.0062 35  SER   A CB  
523  O  OG  . SER   A 35  ? 0.6664 0.6138 0.8291 -0.1871 -0.0869 -0.0062 35  SER   A OG  
529  N  N   . VAL   A 36  ? 0.4855 0.4675 0.6545 -0.1658 -0.0844 -0.0325 36  VAL   A N   
530  C  CA  . VAL   A 36  ? 0.4482 0.4189 0.6200 -0.1504 -0.0893 -0.0454 36  VAL   A CA  
531  C  C   . VAL   A 36  ? 0.3968 0.3896 0.5621 -0.1359 -0.0829 -0.0540 36  VAL   A C   
532  O  O   . VAL   A 36  ? 0.4407 0.4283 0.6035 -0.1216 -0.0841 -0.0642 36  VAL   A O   
533  C  CB  . VAL   A 36  ? 0.5162 0.4584 0.6837 -0.1425 -0.0925 -0.0400 36  VAL   A CB  
534  C  CG1 . VAL   A 36  ? 0.5797 0.4993 0.7502 -0.1498 -0.0980 -0.0348 36  VAL   A CG1 
535  C  CG2 . VAL   A 36  ? 0.4687 0.4115 0.6271 -0.1425 -0.0880 -0.0265 36  VAL   A CG2 
545  N  N   . GLU   A 37  ? 0.3718 0.3900 0.5324 -0.1385 -0.0754 -0.0502 37  GLU   A N   
546  C  CA  . GLU   A 37  ? 0.3658 0.4042 0.5183 -0.1240 -0.0693 -0.0567 37  GLU   A CA  
547  C  C   . GLU   A 37  ? 0.3734 0.3982 0.5151 -0.1090 -0.0674 -0.0555 37  GLU   A C   
548  O  O   . GLU   A 37  ? 0.3393 0.3679 0.4756 -0.0957 -0.0670 -0.0645 37  GLU   A O   
549  C  CB  . GLU   A 37  ? 0.4403 0.4930 0.5983 -0.1194 -0.0723 -0.0714 37  GLU   A CB  
550  C  CG  . GLU   A 37  ? 0.4151 0.4855 0.5847 -0.1341 -0.0735 -0.0736 37  GLU   A CG  
551  C  CD  . GLU   A 37  ? 0.5377 0.6258 0.7124 -0.1285 -0.0765 -0.0882 37  GLU   A CD  
552  O  OE1 . GLU   A 37  ? 0.5412 0.6186 0.7145 -0.1198 -0.0813 -0.0976 37  GLU   A OE1 
553  O  OE2 . GLU   A 37  ? 0.5750 0.6896 0.7547 -0.1321 -0.0741 -0.0910 37  GLU   A OE2 
560  N  N   . MET   A 38  ? 0.3601 0.3694 0.4982 -0.1124 -0.0666 -0.0437 38  MET   A N   
561  C  CA  A MET   A 38  ? 0.3449 0.3417 0.4738 -0.1002 -0.0646 -0.0412 38  MET   A CA  
562  C  CA  B MET   A 38  ? 0.3455 0.3422 0.4745 -0.1002 -0.0646 -0.0411 38  MET   A CA  
563  C  C   . MET   A 38  ? 0.2925 0.2991 0.4125 -0.1004 -0.0574 -0.0305 38  MET   A C   
564  O  O   . MET   A 38  ? 0.3251 0.3364 0.4464 -0.1134 -0.0560 -0.0209 38  MET   A O   
565  C  CB  A MET   A 38  ? 0.3808 0.3492 0.5147 -0.1021 -0.0714 -0.0380 38  MET   A CB  
566  C  CB  B MET   A 38  ? 0.3807 0.3489 0.5146 -0.1024 -0.0715 -0.0376 38  MET   A CB  
567  C  CG  A MET   A 38  ? 0.3856 0.3426 0.5130 -0.0883 -0.0702 -0.0395 38  MET   A CG  
568  C  CG  B MET   A 38  ? 0.4075 0.3629 0.5499 -0.0973 -0.0785 -0.0509 38  MET   A CG  
569  S  SD  A MET   A 38  ? 0.4000 0.3661 0.5229 -0.0725 -0.0682 -0.0561 38  MET   A SD  
570  S  SD  B MET   A 38  ? 0.4847 0.4489 0.6196 -0.0790 -0.0751 -0.0658 38  MET   A SD  
571  C  CE  A MET   A 38  ? 0.4632 0.4319 0.5981 -0.0786 -0.0750 -0.0686 38  MET   A CE  
572  C  CE  B MET   A 38  ? 0.4082 0.3703 0.5302 -0.0699 -0.0682 -0.0564 38  MET   A CE  
591  N  N   . CYS   A 39  ? 0.3178 0.3279 0.4283 -0.0869 -0.0528 -0.0322 39  CYS   A N   
592  C  CA  . CYS   A 39  ? 0.2872 0.3056 0.3894 -0.0851 -0.0463 -0.0240 39  CYS   A CA  
593  C  C   . CYS   A 39  ? 0.2742 0.2740 0.3699 -0.0778 -0.0462 -0.0193 39  CYS   A C   
594  O  O   . CYS   A 39  ? 0.2830 0.2690 0.3797 -0.0705 -0.0497 -0.0253 39  CYS   A O   
595  C  CB  . CYS   A 39  ? 0.2683 0.3078 0.3657 -0.0758 -0.0417 -0.0301 39  CYS   A CB  
596  S  SG  . CYS   A 39  ? 0.2711 0.3394 0.3769 -0.0850 -0.0398 -0.0333 39  CYS   A SG  
601  N  N   . PHE   A 40  ? 0.2506 0.2518 0.3404 -0.0800 -0.0422 -0.0094 40  PHE   A N   
602  C  CA  . PHE   A 40  ? 0.2625 0.2474 0.3468 -0.0739 -0.0422 -0.0042 40  PHE   A CA  
603  C  C   . PHE   A 40  ? 0.2587 0.2558 0.3336 -0.0673 -0.0351 -0.0017 40  PHE   A C   
604  O  O   . PHE   A 40  ? 0.2744 0.2886 0.3481 -0.0728 -0.0310 0.0013  40  PHE   A O   
605  C  CB  . PHE   A 40  ? 0.3213 0.2910 0.4088 -0.0856 -0.0471 0.0070  40  PHE   A CB  
606  C  CG  . PHE   A 40  ? 0.3313 0.2887 0.4296 -0.0942 -0.0552 0.0051  40  PHE   A CG  
607  C  CD1 . PHE   A 40  ? 0.3411 0.3094 0.4439 -0.1078 -0.0557 0.0072  40  PHE   A CD1 
608  C  CD2 . PHE   A 40  ? 0.3709 0.3072 0.4760 -0.0888 -0.0624 -0.0001 40  PHE   A CD2 
609  C  CE1 . PHE   A 40  ? 0.4505 0.4064 0.5635 -0.1163 -0.0636 0.0054  40  PHE   A CE1 
610  C  CE2 . PHE   A 40  ? 0.4006 0.3246 0.5169 -0.0963 -0.0707 -0.0030 40  PHE   A CE2 
611  C  CZ  . PHE   A 40  ? 0.4215 0.3542 0.5413 -0.1103 -0.0715 0.0004  40  PHE   A CZ  
621  N  N   . MET   A 41  ? 0.2445 0.2341 0.3137 -0.0560 -0.0336 -0.0039 41  MET   A N   
622  C  CA  . MET   A 41  ? 0.2164 0.2145 0.2769 -0.0495 -0.0276 -0.0015 41  MET   A CA  
623  C  C   . MET   A 41  ? 0.2206 0.2132 0.2788 -0.0560 -0.0269 0.0093  41  MET   A C   
624  O  O   . MET   A 41  ? 0.2567 0.2390 0.3110 -0.0503 -0.0265 0.0117  41  MET   A O   
625  C  CB  . MET   A 41  ? 0.2487 0.2401 0.3035 -0.0373 -0.0265 -0.0068 41  MET   A CB  
626  C  CG  . MET   A 41  ? 0.2562 0.2545 0.3099 -0.0314 -0.0273 -0.0163 41  MET   A CG  
627  S  SD  . MET   A 41  ? 0.2266 0.2458 0.2775 -0.0291 -0.0244 -0.0178 41  MET   A SD  
628  C  CE  . MET   A 41  ? 0.2503 0.2669 0.2907 -0.0203 -0.0199 -0.0141 41  MET   A CE  
638  N  N   . GLU   A 42  ? 0.2693 0.2697 0.3297 -0.0682 -0.0269 0.0155  42  GLU   A N   
639  C  CA  . GLU   A 42  ? 0.2796 0.2745 0.3363 -0.0765 -0.0274 0.0270  42  GLU   A CA  
640  C  C   . GLU   A 42  ? 0.2792 0.2939 0.3344 -0.0888 -0.0234 0.0317  42  GLU   A C   
641  O  O   . GLU   A 42  ? 0.2750 0.3034 0.3356 -0.0939 -0.0226 0.0269  42  GLU   A O   
642  C  CB  . GLU   A 42  ? 0.2940 0.2664 0.3558 -0.0825 -0.0359 0.0326  42  GLU   A CB  
643  C  CG  . GLU   A 42  ? 0.3707 0.3345 0.4281 -0.0914 -0.0387 0.0460  42  GLU   A CG  
644  C  CD  . GLU   A 42  ? 0.4418 0.3806 0.5055 -0.0967 -0.0495 0.0521  42  GLU   A CD  
645  O  OE1 . GLU   A 42  ? 0.4580 0.3862 0.5308 -0.0927 -0.0543 0.0443  42  GLU   A OE1 
646  O  OE2 . GLU   A 42  ? 0.4721 0.4017 0.5320 -0.1049 -0.0539 0.0644  42  GLU   A OE2 
653  N  N   . ASN   A 43  ? 0.2855 0.3051 0.3336 -0.0927 -0.0204 0.0391  43  ASN   A N   
654  C  CA  . ASN   A 43  ? 0.2867 0.3257 0.3321 -0.1065 -0.0166 0.0444  43  ASN   A CA  
655  C  C   . ASN   A 43  ? 0.3402 0.3687 0.3776 -0.1142 -0.0190 0.0574  43  ASN   A C   
656  O  O   . ASN   A 43  ? 0.3086 0.3148 0.3449 -0.1081 -0.0244 0.0613  43  ASN   A O   
657  C  CB  . ASN   A 43  ? 0.2889 0.3543 0.3336 -0.1007 -0.0084 0.0355  43  ASN   A CB  
658  C  CG  . ASN   A 43  ? 0.3045 0.3651 0.3439 -0.0866 -0.0061 0.0328  43  ASN   A CG  
659  O  OD1 . ASN   A 43  ? 0.2656 0.3229 0.2981 -0.0886 -0.0051 0.0395  43  ASN   A OD1 
660  N  ND2 . ASN   A 43  ? 0.2705 0.3316 0.3128 -0.0732 -0.0053 0.0232  43  ASN   A ND2 
667  N  N   . THR   A 44  ? 0.3435 0.3896 0.3753 -0.1279 -0.0154 0.0636  44  THR   A N   
668  C  CA  . THR   A 44  ? 0.3851 0.4216 0.4077 -0.1372 -0.0189 0.0775  44  THR   A CA  
669  C  C   . THR   A 44  ? 0.3786 0.4058 0.3965 -0.1236 -0.0185 0.0768  44  THR   A C   
670  O  O   . THR   A 44  ? 0.4218 0.4278 0.4368 -0.1237 -0.0256 0.0858  44  THR   A O   
671  C  CB  . THR   A 44  ? 0.4549 0.5157 0.4692 -0.1494 -0.0133 0.0804  44  THR   A CB  
672  O  OG1 . THR   A 44  ? 0.5281 0.6185 0.5444 -0.1464 -0.0035 0.0698  44  THR   A OG1 
673  C  CG2 . THR   A 44  ? 0.4417 0.5054 0.4583 -0.1607 -0.0153 0.0819  44  THR   A CG2 
681  N  N   . ASP   A 45  ? 0.3149 0.3564 0.3332 -0.1114 -0.0114 0.0658  45  ASP   A N   
682  C  CA  . ASP   A 45  ? 0.2928 0.3308 0.3059 -0.1009 -0.0095 0.0648  45  ASP   A CA  
683  C  C   . ASP   A 45  ? 0.3081 0.3264 0.3255 -0.0854 -0.0124 0.0596  45  ASP   A C   
684  O  O   . ASP   A 45  ? 0.2983 0.3068 0.3120 -0.0794 -0.0137 0.0621  45  ASP   A O   
685  C  CB  . ASP   A 45  ? 0.3610 0.4253 0.3727 -0.0972 -0.0007 0.0556  45  ASP   A CB  
686  C  CG  . ASP   A 45  ? 0.4582 0.5453 0.4646 -0.1125 0.0033  0.0596  45  ASP   A CG  
687  O  OD1 . ASP   A 45  ? 0.5049 0.5846 0.5063 -0.1265 -0.0012 0.0720  45  ASP   A OD1 
688  O  OD2 . ASP   A 45  ? 0.4333 0.5459 0.4413 -0.1115 0.0104  0.0502  45  ASP   A OD2 
693  N  N   . VAL   A 46  ? 0.2707 0.2847 0.2953 -0.0795 -0.0135 0.0521  46  VAL   A N   
694  C  CA  . VAL   A 46  ? 0.2448 0.2452 0.2723 -0.0655 -0.0148 0.0454  46  VAL   A CA  
695  C  C   . VAL   A 46  ? 0.2551 0.2425 0.2902 -0.0656 -0.0204 0.0428  46  VAL   A C   
696  O  O   . VAL   A 46  ? 0.2586 0.2541 0.2978 -0.0713 -0.0205 0.0402  46  VAL   A O   
697  C  CB  . VAL   A 46  ? 0.2383 0.2516 0.2649 -0.0550 -0.0087 0.0354  46  VAL   A CB  
698  C  CG1 . VAL   A 46  ? 0.2649 0.2651 0.2920 -0.0426 -0.0098 0.0298  46  VAL   A CG1 
699  C  CG2 . VAL   A 46  ? 0.2728 0.3001 0.2937 -0.0550 -0.0035 0.0360  46  VAL   A CG2 
709  N  N   . LYS   A 47  ? 0.2475 0.2164 0.2856 -0.0589 -0.0251 0.0419  47  LYS   A N   
710  C  CA  . LYS   A 47  ? 0.2507 0.2081 0.2970 -0.0560 -0.0301 0.0359  47  LYS   A CA  
711  C  C   . LYS   A 47  ? 0.2513 0.2065 0.2972 -0.0426 -0.0275 0.0263  47  LYS   A C   
712  O  O   . LYS   A 47  ? 0.2539 0.2040 0.2973 -0.0368 -0.0266 0.0272  47  LYS   A O   
713  C  CB  . LYS   A 47  ? 0.2937 0.2307 0.3461 -0.0608 -0.0394 0.0420  47  LYS   A CB  
714  C  CG  . LYS   A 47  ? 0.2861 0.2104 0.3484 -0.0549 -0.0447 0.0329  47  LYS   A CG  
715  C  CD  . LYS   A 47  ? 0.3120 0.2161 0.3834 -0.0612 -0.0557 0.0380  47  LYS   A CD  
716  C  CE  . LYS   A 47  ? 0.3920 0.2827 0.4639 -0.0589 -0.0611 0.0450  47  LYS   A CE  
717  N  NZ  . LYS   A 47  ? 0.4091 0.2770 0.4918 -0.0632 -0.0740 0.0490  47  LYS   A NZ  
731  N  N   . VAL   A 48  ? 0.2522 0.2116 0.3002 -0.0385 -0.0266 0.0173  48  VAL   A N   
732  C  CA  . VAL   A 48  ? 0.2261 0.1837 0.2725 -0.0279 -0.0247 0.0086  48  VAL   A CA  
733  C  C   . VAL   A 48  ? 0.2491 0.1946 0.3044 -0.0264 -0.0305 0.0022  48  VAL   A C   
734  O  O   . VAL   A 48  ? 0.2604 0.2045 0.3218 -0.0314 -0.0345 -0.0001 48  VAL   A O   
735  C  CB  . VAL   A 48  ? 0.2295 0.2006 0.2705 -0.0237 -0.0204 0.0028  48  VAL   A CB  
736  C  CG1 . VAL   A 48  ? 0.2440 0.2125 0.2825 -0.0154 -0.0197 -0.0057 48  VAL   A CG1 
737  C  CG2 . VAL   A 48  ? 0.2455 0.2272 0.2796 -0.0226 -0.0153 0.0069  48  VAL   A CG2 
747  N  N   . VAL   A 49  ? 0.2663 0.2043 0.3233 -0.0196 -0.0310 -0.0019 49  VAL   A N   
748  C  CA  . VAL   A 49  ? 0.2629 0.1914 0.3299 -0.0163 -0.0362 -0.0109 49  VAL   A CA  
749  C  C   . VAL   A 49  ? 0.2366 0.1738 0.2986 -0.0088 -0.0313 -0.0218 49  VAL   A C   
750  O  O   . VAL   A 49  ? 0.2622 0.2052 0.3159 -0.0046 -0.0256 -0.0209 49  VAL   A O   
751  C  CB  . VAL   A 49  ? 0.2780 0.1933 0.3529 -0.0144 -0.0414 -0.0085 49  VAL   A CB  
752  C  CG1 . VAL   A 49  ? 0.3175 0.2253 0.4047 -0.0087 -0.0464 -0.0213 49  VAL   A CG1 
753  C  CG2 . VAL   A 49  ? 0.3014 0.2069 0.3790 -0.0234 -0.0476 0.0041  49  VAL   A CG2 
763  N  N   . ASP   A 50  ? 0.2736 0.2122 0.3399 -0.0081 -0.0335 -0.0317 50  ASP   A N   
764  C  CA  . ASP   A 50  ? 0.2446 0.1917 0.3058 -0.0023 -0.0297 -0.0427 50  ASP   A CA  
765  C  C   . ASP   A 50  ? 0.2583 0.1994 0.3302 0.0023  -0.0324 -0.0524 50  ASP   A C   
766  O  O   . ASP   A 50  ? 0.2627 0.1963 0.3473 0.0018  -0.0389 -0.0596 50  ASP   A O   
767  C  CB  . ASP   A 50  ? 0.2346 0.1883 0.2949 -0.0040 -0.0312 -0.0496 50  ASP   A CB  
768  C  CG  . ASP   A 50  ? 0.2750 0.2391 0.3272 0.0006  -0.0275 -0.0601 50  ASP   A CG  
769  O  OD1 . ASP   A 50  ? 0.2729 0.2392 0.3221 0.0045  -0.0238 -0.0637 50  ASP   A OD1 
770  O  OD2 . ASP   A 50  ? 0.2879 0.2588 0.3374 -0.0006 -0.0289 -0.0656 50  ASP   A OD2 
775  N  N   . MET   A 51  ? 0.2871 0.2318 0.3554 0.0068  -0.0277 -0.0536 51  MET   A N   
776  C  CA  A MET   A 51  ? 0.2650 0.2070 0.3454 0.0118  -0.0301 -0.0644 51  MET   A CA  
777  C  CA  B MET   A 51  ? 0.2648 0.2070 0.3450 0.0118  -0.0299 -0.0644 51  MET   A CA  
778  C  C   . MET   A 51  ? 0.2908 0.2429 0.3724 0.0146  -0.0284 -0.0809 51  MET   A C   
779  O  O   . MET   A 51  ? 0.3149 0.2669 0.4096 0.0190  -0.0309 -0.0934 51  MET   A O   
780  C  CB  A MET   A 51  ? 0.2830 0.2280 0.3599 0.0148  -0.0253 -0.0610 51  MET   A CB  
781  C  CB  B MET   A 51  ? 0.2830 0.2290 0.3594 0.0150  -0.0248 -0.0617 51  MET   A CB  
782  C  CG  A MET   A 51  ? 0.3137 0.2500 0.3895 0.0121  -0.0272 -0.0459 51  MET   A CG  
783  C  CG  B MET   A 51  ? 0.3169 0.2551 0.3914 0.0126  -0.0260 -0.0470 51  MET   A CG  
784  S  SD  A MET   A 51  ? 0.3155 0.2463 0.4011 0.0163  -0.0297 -0.0450 51  MET   A SD  
785  S  SD  B MET   A 51  ? 0.2930 0.2131 0.3854 0.0120  -0.0376 -0.0434 51  MET   A SD  
786  C  CE  A MET   A 51  ? 0.3101 0.2335 0.4177 0.0214  -0.0387 -0.0599 51  MET   A CE  
787  C  CE  B MET   A 51  ? 0.3068 0.2288 0.4128 0.0205  -0.0388 -0.0566 51  MET   A CE  
806  N  N   . GLY   A 52  ? 0.2867 0.2488 0.3556 0.0124  -0.0247 -0.0820 52  GLY   A N   
807  C  CA  . GLY   A 52  ? 0.2987 0.2720 0.3667 0.0139  -0.0233 -0.0975 52  GLY   A CA  
808  C  C   . GLY   A 52  ? 0.3060 0.2912 0.3718 0.0173  -0.0174 -0.1075 52  GLY   A C   
809  O  O   . GLY   A 52  ? 0.3193 0.3128 0.3920 0.0194  -0.0177 -0.1241 52  GLY   A O   
813  N  N   . HIS   A 53  ? 0.3094 0.2970 0.3663 0.0173  -0.0118 -0.0988 53  HIS   A N   
814  C  CA  . HIS   A 53  ? 0.3147 0.3144 0.3696 0.0191  -0.0054 -0.1067 53  HIS   A CA  
815  C  C   . HIS   A 53  ? 0.2869 0.2850 0.3633 0.0243  -0.0089 -0.1190 53  HIS   A C   
816  O  O   . HIS   A 53  ? 0.3162 0.3282 0.3952 0.0261  -0.0039 -0.1307 53  HIS   A O   
817  C  CB  . HIS   A 53  ? 0.3064 0.3233 0.3471 0.0164  0.0001  -0.1156 53  HIS   A CB  
818  C  CG  . HIS   A 53  ? 0.3207 0.3383 0.3404 0.0120  0.0022  -0.1026 53  HIS   A CG  
819  N  ND1 . HIS   A 53  ? 0.4021 0.4266 0.4111 0.0094  0.0012  -0.1060 53  HIS   A ND1 
820  C  CD2 . HIS   A 53  ? 0.3185 0.3302 0.3270 0.0103  0.0041  -0.0870 53  HIS   A CD2 
821  C  CE1 . HIS   A 53  ? 0.4917 0.5139 0.4843 0.0068  0.0018  -0.0924 53  HIS   A CE1 
822  N  NE2 . HIS   A 53  ? 0.3687 0.3831 0.3613 0.0075  0.0036  -0.0812 53  HIS   A NE2 
830  N  N   . LYS   A 54  ? 0.3005 0.2817 0.3923 0.0264  -0.0176 -0.1152 54  LYS   A N   
831  C  CA  . LYS   A 54  ? 0.3397 0.3154 0.4540 0.0323  -0.0237 -0.1251 54  LYS   A CA  
832  C  C   . LYS   A 54  ? 0.3341 0.3030 0.4494 0.0333  -0.0237 -0.1129 54  LYS   A C   
833  O  O   . LYS   A 54  ? 0.3084 0.2731 0.4093 0.0289  -0.0210 -0.0964 54  LYS   A O   
834  C  CB  . LYS   A 54  ? 0.3036 0.2621 0.4343 0.0333  -0.0353 -0.1271 54  LYS   A CB  
835  C  CG  . LYS   A 54  ? 0.3946 0.3580 0.5259 0.0320  -0.0366 -0.1392 54  LYS   A CG  
836  C  CD  . LYS   A 54  ? 0.4921 0.4766 0.6269 0.0354  -0.0317 -0.1583 54  LYS   A CD  
837  C  CE  . LYS   A 54  ? 0.5228 0.5102 0.6656 0.0353  -0.0365 -0.1686 54  LYS   A CE  
838  N  NZ  . LYS   A 54  ? 0.5510 0.5602 0.7003 0.0383  -0.0328 -0.1849 54  LYS   A NZ  
852  N  N   . TYR   A 55  ? 0.3555 0.3238 0.4885 0.0391  -0.0276 -0.1216 55  TYR   A N   
853  C  CA  . TYR   A 55  ? 0.4095 0.3725 0.5451 0.0406  -0.0286 -0.1115 55  TYR   A CA  
854  C  C   . TYR   A 55  ? 0.4146 0.3551 0.5630 0.0416  -0.0414 -0.1024 55  TYR   A C   
855  O  O   . TYR   A 55  ? 0.4871 0.4213 0.6394 0.0429  -0.0447 -0.0941 55  TYR   A O   
856  C  CB  . TYR   A 55  ? 0.3912 0.3706 0.5379 0.0459  -0.0247 -0.1274 55  TYR   A CB  
857  C  CG  . TYR   A 55  ? 0.3724 0.3741 0.5025 0.0420  -0.0115 -0.1327 55  TYR   A CG  
858  C  CD1 . TYR   A 55  ? 0.3386 0.3547 0.4662 0.0412  -0.0073 -0.1476 55  TYR   A CD1 
859  C  CD2 . TYR   A 55  ? 0.3573 0.3652 0.4736 0.0383  -0.0038 -0.1225 55  TYR   A CD2 
860  C  CE1 . TYR   A 55  ? 0.3417 0.3777 0.4521 0.0360  0.0041  -0.1508 55  TYR   A CE1 
861  C  CE2 . TYR   A 55  ? 0.3487 0.3748 0.4491 0.0333  0.0071  -0.1257 55  TYR   A CE2 
862  C  CZ  . TYR   A 55  ? 0.3359 0.3760 0.4325 0.0317  0.0110  -0.1391 55  TYR   A CZ  
863  O  OH  . TYR   A 55  ? 0.4578 0.5156 0.5367 0.0253  0.0212  -0.1408 55  TYR   A OH  
873  N  N   . TYR   A 56  ? 0.4008 0.3303 0.5545 0.0398  -0.0487 -0.1029 56  TYR   A N   
874  C  CA  . TYR   A 56  ? 0.4745 0.3848 0.6355 0.0373  -0.0606 -0.0901 56  TYR   A CA  
875  C  C   . TYR   A 56  ? 0.3619 0.2625 0.5168 0.0307  -0.0628 -0.0845 56  TYR   A C   
876  O  O   . TYR   A 56  ? 0.4174 0.3276 0.5666 0.0302  -0.0569 -0.0941 56  TYR   A O   
877  C  CB  . TYR   A 56  ? 0.5750 0.4845 0.7550 0.0419  -0.0703 -0.0980 56  TYR   A CB  
878  C  CG  . TYR   A 56  ? 0.7096 0.6257 0.8974 0.0435  -0.0712 -0.1129 56  TYR   A CG  
879  C  CD1 . TYR   A 56  ? 0.7277 0.6313 0.9173 0.0392  -0.0779 -0.1089 56  TYR   A CD1 
880  C  CD2 . TYR   A 56  ? 0.7031 0.6396 0.8961 0.0483  -0.0652 -0.1311 56  TYR   A CD2 
881  C  CE1 . TYR   A 56  ? 0.7786 0.6887 0.9754 0.0407  -0.0789 -0.1229 56  TYR   A CE1 
882  C  CE2 . TYR   A 56  ? 0.7231 0.6676 0.9227 0.0493  -0.0659 -0.1449 56  TYR   A CE2 
883  C  CZ  . TYR   A 56  ? 0.8403 0.7710 1.0422 0.0460  -0.0730 -0.1410 56  TYR   A CZ  
884  O  OH  . TYR   A 56  ? 0.9016 0.8404 1.1104 0.0472  -0.0739 -0.1551 56  TYR   A OH  
894  N  N   . SER   A 57  ? 0.4079 0.2925 0.5629 0.0250  -0.0708 -0.0692 57  SER   A N   
895  C  CA  . SER   A 57  ? 0.3695 0.2460 0.5201 0.0173  -0.0733 -0.0633 57  SER   A CA  
896  C  C   . SER   A 57  ? 0.4064 0.2674 0.5601 0.0112  -0.0835 -0.0482 57  SER   A C   
897  O  O   . SER   A 57  ? 0.4492 0.3056 0.6030 0.0114  -0.0872 -0.0384 57  SER   A O   
898  C  CB  . SER   A 57  ? 0.3766 0.2640 0.5071 0.0118  -0.0627 -0.0547 57  SER   A CB  
899  O  OG  . SER   A 57  ? 0.3766 0.2578 0.5022 0.0028  -0.0654 -0.0443 57  SER   A OG  
905  N  N   . ASN   A 58  ? 0.4418 0.2960 0.5975 0.0052  -0.0882 -0.0465 58  ASN   A N   
906  C  CA  . ASN   A 58  ? 0.4943 0.3350 0.6498 -0.0032 -0.0968 -0.0308 58  ASN   A CA  
907  C  C   . ASN   A 58  ? 0.4486 0.2889 0.5888 -0.0135 -0.0926 -0.0141 58  ASN   A C   
908  O  O   . ASN   A 58  ? 0.4527 0.2849 0.5894 -0.0222 -0.0982 -0.0001 58  ASN   A O   
909  C  CB  . ASN   A 58  ? 0.4747 0.3085 0.6380 -0.0070 -0.1033 -0.0348 58  ASN   A CB  
910  C  CG  . ASN   A 58  ? 0.5490 0.3904 0.7071 -0.0109 -0.0968 -0.0415 58  ASN   A CG  
911  O  OD1 . ASN   A 58  ? 0.5082 0.3559 0.6547 -0.0158 -0.0896 -0.0361 58  ASN   A OD1 
912  N  ND2 . ASN   A 58  ? 0.5502 0.3915 0.7178 -0.0093 -0.1002 -0.0535 58  ASN   A ND2 
919  N  N   . ASN   A 59  ? 0.3944 0.2446 0.5254 -0.0131 -0.0830 -0.0157 59  ASN   A N   
920  C  CA  . ASN   A 59  ? 0.4041 0.2625 0.5192 -0.0212 -0.0763 -0.0014 59  ASN   A CA  
921  C  C   . ASN   A 59  ? 0.3932 0.2519 0.5044 -0.0328 -0.0772 0.0057  59  ASN   A C   
922  O  O   . ASN   A 59  ? 0.3954 0.2600 0.4959 -0.0414 -0.0739 0.0184  59  ASN   A O   
923  C  CB  . ASN   A 59  ? 0.3962 0.2472 0.5085 -0.0231 -0.0802 0.0118  59  ASN   A CB  
924  C  CG  . ASN   A 59  ? 0.4287 0.2852 0.5423 -0.0124 -0.0765 0.0052  59  ASN   A CG  
925  O  OD1 . ASN   A 59  ? 0.3789 0.2497 0.4887 -0.0060 -0.0672 -0.0054 59  ASN   A OD1 
926  N  ND2 . ASN   A 59  ? 0.4668 0.3172 0.5836 -0.0105 -0.0826 0.0112  59  ASN   A ND2 
933  N  N   . LYS   A 60  ? 0.3788 0.2338 0.4987 -0.0336 -0.0809 -0.0036 60  LYS   A N   
934  C  CA  . LYS   A 60  ? 0.3901 0.2501 0.5063 -0.0442 -0.0799 0.0006  60  LYS   A CA  
935  C  C   . LYS   A 60  ? 0.3776 0.2610 0.4805 -0.0428 -0.0675 -0.0014 60  LYS   A C   
936  O  O   . LYS   A 60  ? 0.3946 0.2878 0.4936 -0.0329 -0.0611 -0.0106 60  LYS   A O   
937  C  CB  . LYS   A 60  ? 0.4761 0.3276 0.6056 -0.0444 -0.0869 -0.0109 60  LYS   A CB  
938  C  CG  . LYS   A 60  ? 0.5289 0.3648 0.6660 -0.0457 -0.0969 -0.0059 60  LYS   A CG  
939  C  CD  . LYS   A 60  ? 0.5539 0.3855 0.7027 -0.0436 -0.1022 -0.0183 60  LYS   A CD  
940  C  CE  . LYS   A 60  ? 0.7035 0.5207 0.8628 -0.0393 -0.1126 -0.0176 60  LYS   A CE  
941  N  NZ  . LYS   A 60  ? 0.8017 0.6089 0.9553 -0.0486 -0.1182 0.0013  60  LYS   A NZ  
955  N  N   . PRO   A 61  ? 0.3321 0.2251 0.4282 -0.0527 -0.0643 0.0070  61  PRO   A N   
956  C  CA  . PRO   A 61  ? 0.3431 0.2577 0.4287 -0.0504 -0.0541 0.0043  61  PRO   A CA  
957  C  C   . PRO   A 61  ? 0.3207 0.2427 0.4086 -0.0443 -0.0525 -0.0096 61  PRO   A C   
958  O  O   . PRO   A 61  ? 0.3279 0.2427 0.4253 -0.0467 -0.0585 -0.0162 61  PRO   A O   
959  C  CB  . PRO   A 61  ? 0.3161 0.2394 0.3985 -0.0634 -0.0530 0.0142  61  PRO   A CB  
960  C  CG  . PRO   A 61  ? 0.3385 0.2447 0.4313 -0.0732 -0.0632 0.0177  61  PRO   A CG  
961  C  CD  . PRO   A 61  ? 0.3955 0.2813 0.4938 -0.0672 -0.0702 0.0187  61  PRO   A CD  
969  N  N   . MET   A 62  ? 0.3023 0.2383 0.3810 -0.0369 -0.0450 -0.0141 62  MET   A N   
970  C  CA  . MET   A 62  ? 0.2764 0.2222 0.3536 -0.0326 -0.0434 -0.0252 62  MET   A CA  
971  C  C   . MET   A 62  ? 0.2664 0.2184 0.3482 -0.0411 -0.0459 -0.0254 62  MET   A C   
972  O  O   . MET   A 62  ? 0.2922 0.2530 0.3716 -0.0479 -0.0436 -0.0175 62  MET   A O   
973  C  CB  . MET   A 62  ? 0.2627 0.2223 0.3276 -0.0260 -0.0360 -0.0257 62  MET   A CB  
974  C  CG  . MET   A 62  ? 0.3062 0.2738 0.3669 -0.0203 -0.0351 -0.0365 62  MET   A CG  
975  S  SD  . MET   A 62  ? 0.2704 0.2501 0.3159 -0.0138 -0.0286 -0.0340 62  MET   A SD  
976  C  CE  . MET   A 62  ? 0.2998 0.2906 0.3411 -0.0115 -0.0304 -0.0433 62  MET   A CE  
986  N  N   . GLN   A 63  ? 0.2667 0.2163 0.3557 -0.0411 -0.0504 -0.0355 63  GLN   A N   
987  C  CA  . GLN   A 63  ? 0.2848 0.2404 0.3796 -0.0497 -0.0534 -0.0368 63  GLN   A CA  
988  C  C   . GLN   A 63  ? 0.3022 0.2707 0.3945 -0.0445 -0.0525 -0.0486 63  GLN   A C   
989  O  O   . GLN   A 63  ? 0.3260 0.2925 0.4166 -0.0368 -0.0528 -0.0583 63  GLN   A O   
990  C  CB  . GLN   A 63  ? 0.3745 0.3126 0.4824 -0.0574 -0.0620 -0.0367 63  GLN   A CB  
991  C  CG  . GLN   A 63  ? 0.4754 0.4028 0.5915 -0.0510 -0.0672 -0.0500 63  GLN   A CG  
992  C  CD  . GLN   A 63  ? 0.6204 0.5280 0.7511 -0.0587 -0.0773 -0.0491 63  GLN   A CD  
993  O  OE1 . GLN   A 63  ? 0.4667 0.3642 0.5991 -0.0678 -0.0805 -0.0358 63  GLN   A OE1 
994  N  NE2 . GLN   A 63  ? 0.7147 0.6169 0.8556 -0.0561 -0.0829 -0.0632 63  GLN   A NE2 
1003 N  N   . PHE   A 64  ? 0.3034 0.2869 0.3955 -0.0492 -0.0515 -0.0482 64  PHE   A N   
1004 C  CA  . PHE   A 64  ? 0.3066 0.3042 0.3953 -0.0444 -0.0514 -0.0578 64  PHE   A CA  
1005 C  C   . PHE   A 64  ? 0.2943 0.3024 0.3914 -0.0533 -0.0544 -0.0597 64  PHE   A C   
1006 O  O   . PHE   A 64  ? 0.2970 0.3090 0.3985 -0.0624 -0.0534 -0.0518 64  PHE   A O   
1007 C  CB  . PHE   A 64  ? 0.2497 0.2590 0.3254 -0.0361 -0.0461 -0.0555 64  PHE   A CB  
1008 C  CG  . PHE   A 64  ? 0.2320 0.2515 0.3068 -0.0393 -0.0424 -0.0465 64  PHE   A CG  
1009 C  CD1 . PHE   A 64  ? 0.2813 0.2938 0.3546 -0.0417 -0.0392 -0.0369 64  PHE   A CD1 
1010 C  CD2 . PHE   A 64  ? 0.2766 0.3141 0.3523 -0.0395 -0.0424 -0.0490 64  PHE   A CD2 
1011 C  CE1 . PHE   A 64  ? 0.2848 0.3091 0.3572 -0.0448 -0.0354 -0.0305 64  PHE   A CE1 
1012 C  CE2 . PHE   A 64  ? 0.2441 0.2936 0.3207 -0.0419 -0.0389 -0.0434 64  PHE   A CE2 
1013 C  CZ  . PHE   A 64  ? 0.2572 0.3005 0.3319 -0.0448 -0.0350 -0.0344 64  PHE   A CZ  
1023 N  N   . THR   A 65  ? 0.2971 0.3118 0.3964 -0.0515 -0.0579 -0.0709 65  THR   A N   
1024 C  CA  . THR   A 65  ? 0.2754 0.3015 0.3840 -0.0598 -0.0614 -0.0748 65  THR   A CA  
1025 C  C   . THR   A 65  ? 0.3274 0.3741 0.4331 -0.0594 -0.0578 -0.0713 65  THR   A C   
1026 O  O   . THR   A 65  ? 0.2794 0.3336 0.3749 -0.0493 -0.0557 -0.0723 65  THR   A O   
1027 C  CB  . THR   A 65  ? 0.3262 0.3550 0.4367 -0.0565 -0.0663 -0.0887 65  THR   A CB  
1028 O  OG1 . THR   A 65  ? 0.3981 0.4079 0.5160 -0.0586 -0.0702 -0.0929 65  THR   A OG1 
1029 C  CG2 . THR   A 65  ? 0.3251 0.3693 0.4443 -0.0635 -0.0698 -0.0940 65  THR   A CG2 
1037 N  N   . CYS   A 66  ? 0.3385 0.3944 0.4531 -0.0704 -0.0574 -0.0673 66  CYS   A N   
1038 C  CA  . CYS   A 66  ? 0.2758 0.3554 0.3915 -0.0706 -0.0544 -0.0668 66  CYS   A CA  
1039 C  C   . CYS   A 66  ? 0.3356 0.4278 0.4646 -0.0823 -0.0577 -0.0718 66  CYS   A C   
1040 O  O   . CYS   A 66  ? 0.3552 0.4430 0.4908 -0.0956 -0.0572 -0.0656 66  CYS   A O   
1041 C  CB  . CYS   A 66  ? 0.3040 0.3859 0.4162 -0.0726 -0.0483 -0.0564 66  CYS   A CB  
1042 S  SG  . CYS   A 66  ? 0.3139 0.3811 0.4307 -0.0885 -0.0477 -0.0451 66  CYS   A SG  
1047 N  N   . LYS   A 67  ? 0.4079 0.5142 0.5402 -0.0782 -0.0615 -0.0822 67  LYS   A N   
1048 C  CA  . LYS   A 67  ? 0.4721 0.5907 0.6181 -0.0893 -0.0653 -0.0886 67  LYS   A CA  
1049 C  C   . LYS   A 67  ? 0.5202 0.6667 0.6739 -0.0938 -0.0621 -0.0889 67  LYS   A C   
1050 O  O   . LYS   A 67  ? 0.4951 0.6537 0.6438 -0.0830 -0.0599 -0.0894 67  LYS   A O   
1051 C  CB  . LYS   A 67  ? 0.4783 0.5995 0.6245 -0.0828 -0.0718 -0.1009 67  LYS   A CB  
1052 C  CG  . LYS   A 67  ? 0.5513 0.6492 0.6922 -0.0792 -0.0748 -0.1041 67  LYS   A CG  
1053 C  CD  . LYS   A 67  ? 0.6566 0.7588 0.8005 -0.0773 -0.0815 -0.1176 67  LYS   A CD  
1054 C  CE  . LYS   A 67  ? 0.7557 0.8758 0.8915 -0.0665 -0.0833 -0.1231 67  LYS   A CE  
1055 N  NZ  . LYS   A 67  ? 0.8650 0.9892 1.0017 -0.0651 -0.0900 -0.1360 67  LYS   A NZ  
1069 N  N   . GLU   A 68  ? 0.5638 0.7208 0.7301 -0.1093 -0.0623 -0.0895 68  GLU   A N   
1070 C  CA  . GLU   A 68  ? 0.5347 0.7228 0.7109 -0.1151 -0.0588 -0.0921 68  GLU   A CA  
1071 C  C   . GLU   A 68  ? 0.5495 0.7573 0.7286 -0.1021 -0.0629 -0.1039 68  GLU   A C   
1072 O  O   . GLU   A 68  ? 0.4181 0.6470 0.5999 -0.0961 -0.0602 -0.1059 68  GLU   A O   
1073 C  CB  . GLU   A 68  ? 0.5412 0.7371 0.7304 -0.1354 -0.0593 -0.0919 68  GLU   A CB  
1074 C  CG  . GLU   A 68  ? 0.5939 0.8218 0.7924 -0.1396 -0.0553 -0.0955 68  GLU   A CG  
1075 C  CD  . GLU   A 68  ? 0.6399 0.8694 0.8450 -0.1577 -0.0536 -0.0897 68  GLU   A CD  
1076 O  OE1 . GLU   A 68  ? 0.5880 0.8064 0.7981 -0.1637 -0.0595 -0.0922 68  GLU   A OE1 
1077 O  OE2 . GLU   A 68  ? 0.6471 0.8889 0.8520 -0.1656 -0.0464 -0.0832 68  GLU   A OE2 
1084 N  N   . THR   A 69  ? 0.5206 0.7220 0.6994 -0.0975 -0.0700 -0.1117 69  THR   A N   
1085 C  CA  . THR   A 69  ? 0.5754 0.7928 0.7548 -0.0851 -0.0759 -0.1220 69  THR   A CA  
1086 C  C   . THR   A 69  ? 0.6299 0.8282 0.7920 -0.0703 -0.0784 -0.1204 69  THR   A C   
1087 O  O   . THR   A 69  ? 0.6077 0.7889 0.7646 -0.0708 -0.0816 -0.1228 69  THR   A O   
1088 C  CB  . THR   A 69  ? 0.4856 0.7109 0.6749 -0.0917 -0.0815 -0.1311 69  THR   A CB  
1089 O  OG1 . THR   A 69  ? 0.5432 0.7811 0.7435 -0.1052 -0.0765 -0.1277 69  THR   A OG1 
1090 C  CG2 . THR   A 69  ? 0.4144 0.6540 0.6020 -0.0788 -0.0875 -0.1393 69  THR   A CG2 
1098 N  N   . PRO   A 70  ? 0.6128 0.8132 0.7660 -0.0578 -0.0771 -0.1167 70  PRO   A N   
1099 C  CA  . PRO   A 70  ? 0.6626 0.8450 0.7976 -0.0452 -0.0789 -0.1137 70  PRO   A CA  
1100 C  C   . PRO   A 70  ? 0.6442 0.8307 0.7748 -0.0389 -0.0875 -0.1225 70  PRO   A C   
1101 O  O   . PRO   A 70  ? 0.5809 0.7877 0.7233 -0.0407 -0.0926 -0.1306 70  PRO   A O   
1102 C  CB  . PRO   A 70  ? 0.5542 0.7416 0.6847 -0.0357 -0.0763 -0.1083 70  PRO   A CB  
1103 C  CG  . PRO   A 70  ? 0.5578 0.7733 0.7054 -0.0384 -0.0772 -0.1144 70  PRO   A CG  
1104 C  CD  . PRO   A 70  ? 0.5245 0.7452 0.6845 -0.0549 -0.0739 -0.1159 70  PRO   A CD  
1112 N  N   . LYS   A 76  ? 0.4028 0.6598 0.5520 -0.1200 -0.0097 -0.0564 76  LYS   A N   
1113 C  CA  . LYS   A 76  ? 0.3729 0.6268 0.5269 -0.1046 -0.0165 -0.0660 76  LYS   A CA  
1114 C  C   . LYS   A 76  ? 0.2539 0.4800 0.3949 -0.0878 -0.0195 -0.0620 76  LYS   A C   
1115 O  O   . LYS   A 76  ? 0.2977 0.5037 0.4273 -0.0895 -0.0171 -0.0516 76  LYS   A O   
1116 C  CB  . LYS   A 76  ? 0.4300 0.6766 0.5894 -0.1130 -0.0219 -0.0670 76  LYS   A CB  
1117 C  CG  . LYS   A 76  ? 0.5010 0.7699 0.6742 -0.1078 -0.0263 -0.0809 76  LYS   A CG  
1118 C  CD  . LYS   A 76  ? 0.4002 0.7016 0.5836 -0.1132 -0.0206 -0.0873 76  LYS   A CD  
1119 C  CE  . LYS   A 76  ? 0.5280 0.8440 0.7225 -0.1106 -0.0247 -0.0977 76  LYS   A CE  
1120 N  NZ  . LYS   A 76  ? 0.4836 0.7956 0.6806 -0.1279 -0.0244 -0.0933 76  LYS   A NZ  
1133 N  N   . THR   A 77  ? 0.2850 0.5107 0.4275 -0.0723 -0.0251 -0.0699 77  THR   A N   
1134 C  CA  . THR   A 77  ? 0.2755 0.4802 0.4062 -0.0566 -0.0279 -0.0674 77  THR   A CA  
1135 C  C   . THR   A 77  ? 0.2417 0.4286 0.3676 -0.0509 -0.0349 -0.0686 77  THR   A C   
1136 O  O   . THR   A 77  ? 0.2495 0.4482 0.3836 -0.0504 -0.0398 -0.0767 77  THR   A O   
1137 C  CB  . THR   A 77  ? 0.2852 0.5055 0.4202 -0.0428 -0.0290 -0.0751 77  THR   A CB  
1138 O  OG1 . THR   A 77  ? 0.2854 0.5269 0.4268 -0.0489 -0.0220 -0.0767 77  THR   A OG1 
1139 C  CG2 . THR   A 77  ? 0.3119 0.5095 0.4335 -0.0287 -0.0317 -0.0707 77  THR   A CG2 
1147 N  N   . TYR   A 78  ? 0.2393 0.3997 0.3520 -0.0465 -0.0352 -0.0615 78  TYR   A N   
1148 C  CA  . TYR   A 78  ? 0.2331 0.3762 0.3397 -0.0428 -0.0405 -0.0627 78  TYR   A CA  
1149 C  C   . TYR   A 78  ? 0.2248 0.3516 0.3175 -0.0300 -0.0414 -0.0597 78  TYR   A C   
1150 O  O   . TYR   A 78  ? 0.2237 0.3437 0.3105 -0.0275 -0.0371 -0.0535 78  TYR   A O   
1151 C  CB  . TYR   A 78  ? 0.2453 0.3717 0.3517 -0.0541 -0.0398 -0.0576 78  TYR   A CB  
1152 C  CG  . TYR   A 78  ? 0.2251 0.3650 0.3437 -0.0694 -0.0387 -0.0580 78  TYR   A CG  
1153 C  CD1 . TYR   A 78  ? 0.2742 0.4222 0.4020 -0.0744 -0.0434 -0.0655 78  TYR   A CD1 
1154 C  CD2 . TYR   A 78  ? 0.2766 0.4221 0.3968 -0.0798 -0.0331 -0.0508 78  TYR   A CD2 
1155 C  CE1 . TYR   A 78  ? 0.2970 0.4581 0.4362 -0.0899 -0.0423 -0.0657 78  TYR   A CE1 
1156 C  CE2 . TYR   A 78  ? 0.3416 0.5007 0.4715 -0.0958 -0.0319 -0.0503 78  TYR   A CE2 
1157 C  CZ  . TYR   A 78  ? 0.3542 0.5206 0.4939 -0.1011 -0.0364 -0.0576 78  TYR   A CZ  
1158 O  OH  . TYR   A 78  ? 0.3638 0.5440 0.5134 -0.1185 -0.0352 -0.0568 78  TYR   A OH  
1168 N  N   . TYR   A 79  ? 0.2196 0.3411 0.3068 -0.0230 -0.0471 -0.0640 79  TYR   A N   
1169 C  CA  . TYR   A 79  ? 0.2063 0.3118 0.2787 -0.0136 -0.0479 -0.0605 79  TYR   A CA  
1170 C  C   . TYR   A 79  ? 0.2221 0.3079 0.2881 -0.0174 -0.0441 -0.0554 79  TYR   A C   
1171 O  O   . TYR   A 79  ? 0.2386 0.3190 0.3093 -0.0246 -0.0450 -0.0574 79  TYR   A O   
1172 C  CB  . TYR   A 79  ? 0.2431 0.3497 0.3097 -0.0071 -0.0551 -0.0662 79  TYR   A CB  
1173 C  CG  . TYR   A 79  ? 0.3180 0.4371 0.3856 0.0017  -0.0605 -0.0688 79  TYR   A CG  
1174 C  CD1 . TYR   A 79  ? 0.3478 0.4594 0.4057 0.0106  -0.0612 -0.0637 79  TYR   A CD1 
1175 C  CD2 . TYR   A 79  ? 0.3703 0.5083 0.4498 0.0013  -0.0659 -0.0766 79  TYR   A CD2 
1176 C  CE1 . TYR   A 79  ? 0.4398 0.5603 0.4998 0.0194  -0.0681 -0.0661 79  TYR   A CE1 
1177 C  CE2 . TYR   A 79  ? 0.3777 0.5268 0.4601 0.0106  -0.0724 -0.0797 79  TYR   A CE2 
1178 C  CZ  . TYR   A 79  ? 0.4285 0.5679 0.5013 0.0200  -0.0740 -0.0743 79  TYR   A CZ  
1179 O  OH  . TYR   A 79  ? 0.4913 0.6394 0.5683 0.0299  -0.0823 -0.0774 79  TYR   A OH  
1189 N  N   . THR   A 80  ? 0.1941 0.2691 0.2504 -0.0123 -0.0408 -0.0494 80  THR   A N   
1190 C  CA  . THR   A 80  ? 0.1782 0.2359 0.2293 -0.0143 -0.0376 -0.0452 80  THR   A CA  
1191 C  C   . THR   A 80  ? 0.2243 0.2737 0.2674 -0.0106 -0.0404 -0.0499 80  THR   A C   
1192 O  O   . THR   A 80  ? 0.2190 0.2750 0.2576 -0.0065 -0.0448 -0.0547 80  THR   A O   
1193 C  CB  . THR   A 80  ? 0.2199 0.2711 0.2639 -0.0102 -0.0331 -0.0381 80  THR   A CB  
1194 O  OG1 . THR   A 80  ? 0.2336 0.2846 0.2676 -0.0012 -0.0349 -0.0383 80  THR   A OG1 
1195 C  CG2 . THR   A 80  ? 0.2344 0.2962 0.2857 -0.0141 -0.0299 -0.0348 80  THR   A CG2 
1203 N  N   . GLY   A 81  ? 0.2374 0.2733 0.2788 -0.0123 -0.0382 -0.0490 81  GLY   A N   
1204 C  CA  . GLY   A 81  ? 0.2416 0.2716 0.2755 -0.0090 -0.0394 -0.0546 81  GLY   A CA  
1205 C  C   . GLY   A 81  ? 0.2417 0.2708 0.2841 -0.0136 -0.0431 -0.0632 81  GLY   A C   
1206 O  O   . GLY   A 81  ? 0.2402 0.2760 0.2922 -0.0187 -0.0462 -0.0657 81  GLY   A O   
1210 N  N   . TYR   A 82  ? 0.2556 0.2772 0.2952 -0.0120 -0.0428 -0.0690 82  TYR   A N   
1211 C  CA  . TYR   A 82  ? 0.2439 0.2636 0.2922 -0.0153 -0.0468 -0.0794 82  TYR   A CA  
1212 C  C   . TYR   A 82  ? 0.2832 0.3156 0.3293 -0.0153 -0.0513 -0.0871 82  TYR   A C   
1213 O  O   . TYR   A 82  ? 0.2503 0.2833 0.3065 -0.0196 -0.0555 -0.0953 82  TYR   A O   
1214 C  CB  . TYR   A 82  ? 0.2356 0.2481 0.2811 -0.0120 -0.0452 -0.0862 82  TYR   A CB  
1215 C  CG  . TYR   A 82  ? 0.2421 0.2417 0.2929 -0.0119 -0.0424 -0.0807 82  TYR   A CG  
1216 C  CD1 . TYR   A 82  ? 0.2747 0.2651 0.3376 -0.0174 -0.0445 -0.0744 82  TYR   A CD1 
1217 C  CD2 . TYR   A 82  ? 0.2508 0.2482 0.2940 -0.0070 -0.0381 -0.0812 82  TYR   A CD2 
1218 C  CE1 . TYR   A 82  ? 0.2507 0.2290 0.3178 -0.0172 -0.0432 -0.0687 82  TYR   A CE1 
1219 C  CE2 . TYR   A 82  ? 0.2619 0.2484 0.3109 -0.0064 -0.0363 -0.0767 82  TYR   A CE2 
1220 C  CZ  . TYR   A 82  ? 0.2833 0.2597 0.3441 -0.0111 -0.0394 -0.0703 82  TYR   A CZ  
1221 O  OH  . TYR   A 82  ? 0.2951 0.2602 0.3612 -0.0107 -0.0391 -0.0649 82  TYR   A OH  
1231 N  N   . SER   A 83  ? 0.2720 0.3138 0.3054 -0.0106 -0.0516 -0.0846 83  SER   A N   
1232 C  CA  . SER   A 83  ? 0.3191 0.3739 0.3499 -0.0101 -0.0571 -0.0904 83  SER   A CA  
1233 C  C   . SER   A 83  ? 0.3043 0.3689 0.3404 -0.0102 -0.0594 -0.0853 83  SER   A C   
1234 O  O   . SER   A 83  ? 0.2980 0.3742 0.3316 -0.0082 -0.0648 -0.0890 83  SER   A O   
1235 C  CB  . SER   A 83  ? 0.3670 0.4259 0.3791 -0.0049 -0.0580 -0.0919 83  SER   A CB  
1236 O  OG  . SER   A 83  ? 0.4222 0.4761 0.4298 -0.0052 -0.0550 -0.0985 83  SER   A OG  
1242 N  N   . ALA   A 84  ? 0.2516 0.3135 0.2954 -0.0124 -0.0557 -0.0777 84  ALA   A N   
1243 C  CA  . ALA   A 84  ? 0.2518 0.3262 0.3037 -0.0135 -0.0570 -0.0751 84  ALA   A CA  
1244 C  C   . ALA   A 84  ? 0.2492 0.3322 0.2921 -0.0052 -0.0608 -0.0739 84  ALA   A C   
1245 O  O   . ALA   A 84  ? 0.2785 0.3757 0.3277 -0.0043 -0.0658 -0.0778 84  ALA   A O   
1246 C  CB  . ALA   A 84  ? 0.2959 0.3799 0.3620 -0.0210 -0.0607 -0.0821 84  ALA   A CB  
1252 N  N   . ASP   A 85  ? 0.2344 0.3085 0.2631 0.0006  -0.0590 -0.0685 85  ASP   A N   
1253 C  CA  . ASP   A 85  ? 0.2770 0.3545 0.2954 0.0082  -0.0637 -0.0654 85  ASP   A CA  
1254 C  C   . ASP   A 85  ? 0.2397 0.3110 0.2551 0.0124  -0.0602 -0.0570 85  ASP   A C   
1255 O  O   . ASP   A 85  ? 0.2793 0.3495 0.2858 0.0189  -0.0646 -0.0533 85  ASP   A O   
1256 C  CB  . ASP   A 85  ? 0.3381 0.4109 0.3389 0.0105  -0.0667 -0.0665 85  ASP   A CB  
1257 C  CG  . ASP   A 85  ? 0.3353 0.3957 0.3273 0.0086  -0.0598 -0.0645 85  ASP   A CG  
1258 O  OD1 . ASP   A 85  ? 0.2933 0.3466 0.2922 0.0067  -0.0536 -0.0609 85  ASP   A OD1 
1259 O  OD2 . ASP   A 85  ? 0.3949 0.4539 0.3728 0.0088  -0.0606 -0.0666 85  ASP   A OD2 
1264 N  N   . GLY   A 86  ? 0.2404 0.3069 0.2626 0.0086  -0.0532 -0.0536 86  GLY   A N   
1265 C  CA  . GLY   A 86  ? 0.2024 0.2636 0.2220 0.0120  -0.0495 -0.0466 86  GLY   A CA  
1266 C  C   . GLY   A 86  ? 0.2305 0.2770 0.2364 0.0135  -0.0458 -0.0412 86  GLY   A C   
1267 O  O   . GLY   A 86  ? 0.2383 0.2795 0.2420 0.0160  -0.0427 -0.0355 86  GLY   A O   
1271 N  N   . TYR   A 87  ? 0.2305 0.2718 0.2280 0.0118  -0.0456 -0.0439 87  TYR   A N   
1272 C  CA  . TYR   A 87  ? 0.2437 0.2747 0.2276 0.0129  -0.0423 -0.0402 87  TYR   A CA  
1273 C  C   . TYR   A 87  ? 0.2330 0.2582 0.2207 0.0086  -0.0368 -0.0434 87  TYR   A C   
1274 O  O   . TYR   A 87  ? 0.2699 0.2973 0.2682 0.0048  -0.0374 -0.0493 87  TYR   A O   
1275 C  CB  . TYR   A 87  ? 0.2413 0.2737 0.2094 0.0148  -0.0472 -0.0412 87  TYR   A CB  
1276 C  CG  . TYR   A 87  ? 0.2615 0.2947 0.2234 0.0201  -0.0539 -0.0358 87  TYR   A CG  
1277 C  CD1 . TYR   A 87  ? 0.2533 0.2773 0.2074 0.0230  -0.0530 -0.0276 87  TYR   A CD1 
1278 C  CD2 . TYR   A 87  ? 0.2962 0.3389 0.2614 0.0226  -0.0621 -0.0393 87  TYR   A CD2 
1279 C  CE1 . TYR   A 87  ? 0.2739 0.2965 0.2240 0.0285  -0.0608 -0.0230 87  TYR   A CE1 
1280 C  CE2 . TYR   A 87  ? 0.3122 0.3548 0.2737 0.0287  -0.0701 -0.0349 87  TYR   A CE2 
1281 C  CZ  . TYR   A 87  ? 0.2936 0.3251 0.2477 0.0318  -0.0696 -0.0266 87  TYR   A CZ  
1282 O  OH  . TYR   A 87  ? 0.3711 0.4000 0.3228 0.0383  -0.0791 -0.0225 87  TYR   A OH  
1292 N  N   . ASP   A 88  ? 0.2358 0.2531 0.2158 0.0093  -0.0321 -0.0397 88  ASP   A N   
1293 C  CA  . ASP   A 88  ? 0.2297 0.2418 0.2128 0.0068  -0.0277 -0.0437 88  ASP   A CA  
1294 C  C   . ASP   A 88  ? 0.2645 0.2734 0.2332 0.0081  -0.0241 -0.0408 88  ASP   A C   
1295 O  O   . ASP   A 88  ? 0.2550 0.2579 0.2248 0.0083  -0.0196 -0.0368 88  ASP   A O   
1296 C  CB  . ASP   A 88  ? 0.2250 0.2314 0.2212 0.0048  -0.0250 -0.0407 88  ASP   A CB  
1297 C  CG  . ASP   A 88  ? 0.2562 0.2559 0.2571 0.0035  -0.0221 -0.0448 88  ASP   A CG  
1298 O  OD1 . ASP   A 88  ? 0.2930 0.2950 0.2920 0.0035  -0.0225 -0.0535 88  ASP   A OD1 
1299 O  OD2 . ASP   A 88  ? 0.2763 0.2694 0.2841 0.0026  -0.0200 -0.0403 88  ASP   A OD2 
1304 N  N   . ARG   A 89  ? 0.2917 0.3052 0.2464 0.0082  -0.0265 -0.0422 89  ARG   A N   
1305 C  CA  . ARG   A 89  ? 0.2603 0.2710 0.1989 0.0080  -0.0242 -0.0365 89  ARG   A CA  
1306 C  C   . ARG   A 89  ? 0.2591 0.2700 0.1966 0.0054  -0.0174 -0.0411 89  ARG   A C   
1307 O  O   . ARG   A 89  ? 0.2855 0.3015 0.2289 0.0041  -0.0160 -0.0515 89  ARG   A O   
1308 C  CB  . ARG   A 89  ? 0.2951 0.3109 0.2171 0.0072  -0.0295 -0.0357 89  ARG   A CB  
1309 C  CG  . ARG   A 89  ? 0.3532 0.3692 0.2753 0.0108  -0.0377 -0.0310 89  ARG   A CG  
1310 C  CD  . ARG   A 89  ? 0.4101 0.4285 0.3128 0.0098  -0.0439 -0.0280 89  ARG   A CD  
1311 N  NE  . ARG   A 89  ? 0.4177 0.4365 0.3218 0.0144  -0.0536 -0.0242 89  ARG   A NE  
1312 C  CZ  . ARG   A 89  ? 0.4084 0.4361 0.3204 0.0159  -0.0590 -0.0306 89  ARG   A CZ  
1313 N  NH1 . ARG   A 89  ? 0.5066 0.5422 0.4259 0.0128  -0.0562 -0.0408 89  ARG   A NH1 
1314 N  NH2 . ARG   A 89  ? 0.4583 0.4871 0.3723 0.0208  -0.0683 -0.0274 89  ARG   A NH2 
1328 N  N   . ASP   A 90  ? 0.2703 0.2761 0.2009 0.0050  -0.0135 -0.0342 90  ASP   A N   
1329 C  CA  . ASP   A 90  ? 0.2642 0.2728 0.1919 0.0022  -0.0069 -0.0385 90  ASP   A CA  
1330 C  C   . ASP   A 90  ? 0.2759 0.2800 0.1902 0.0002  -0.0044 -0.0289 90  ASP   A C   
1331 O  O   . ASP   A 90  ? 0.2779 0.2732 0.1950 0.0026  -0.0055 -0.0205 90  ASP   A O   
1332 C  CB  . ASP   A 90  ? 0.3095 0.3152 0.2554 0.0038  -0.0036 -0.0434 90  ASP   A CB  
1333 C  CG  . ASP   A 90  ? 0.4102 0.4229 0.3574 0.0020  0.0017  -0.0530 90  ASP   A CG  
1334 O  OD1 . ASP   A 90  ? 0.3720 0.3857 0.3116 -0.0001 0.0065  -0.0497 90  ASP   A OD1 
1335 O  OD2 . ASP   A 90  ? 0.4790 0.4971 0.4350 0.0024  0.0009  -0.0647 90  ASP   A OD2 
1340 N  N   . ASN   A 91  ? 0.3074 0.3183 0.2072 -0.0050 -0.0012 -0.0307 91  ASN   A N   
1341 C  CA  . ASN   A 91  ? 0.3070 0.3144 0.1943 -0.0091 0.0022  -0.0224 91  ASN   A CA  
1342 C  C   . ASN   A 91  ? 0.3063 0.3008 0.1874 -0.0071 -0.0035 -0.0092 91  ASN   A C   
1343 O  O   . ASN   A 91  ? 0.3226 0.3093 0.2045 -0.0072 -0.0014 -0.0027 91  ASN   A O   
1344 C  CB  . ASN   A 91  ? 0.3051 0.3138 0.2038 -0.0093 0.0096  -0.0264 91  ASN   A CB  
1345 C  CG  . ASN   A 91  ? 0.2892 0.2981 0.1748 -0.0155 0.0142  -0.0205 91  ASN   A CG  
1346 O  OD1 . ASN   A 91  ? 0.3224 0.3362 0.1895 -0.0221 0.0142  -0.0177 91  ASN   A OD1 
1347 N  ND2 . ASN   A 91  ? 0.2996 0.3045 0.1945 -0.0145 0.0183  -0.0190 91  ASN   A ND2 
1354 N  N   . GLY   A 92  ? 0.3132 0.3060 0.1883 -0.0052 -0.0114 -0.0060 92  GLY   A N   
1355 C  CA  . GLY   A 92  ? 0.3512 0.3324 0.2202 -0.0027 -0.0186 0.0051  92  GLY   A CA  
1356 C  C   . GLY   A 92  ? 0.3149 0.2907 0.2010 0.0048  -0.0216 0.0058  92  GLY   A C   
1357 O  O   . GLY   A 92  ? 0.3175 0.2847 0.2017 0.0082  -0.0281 0.0129  92  GLY   A O   
1361 N  N   . ALA   A 93  ? 0.2945 0.2754 0.1973 0.0070  -0.0176 -0.0017 93  ALA   A N   
1362 C  CA  . ALA   A 93  ? 0.2915 0.2708 0.2098 0.0123  -0.0198 -0.0018 93  ALA   A CA  
1363 C  C   . ALA   A 93  ? 0.2896 0.2766 0.2149 0.0141  -0.0244 -0.0076 93  ALA   A C   
1364 O  O   . ALA   A 93  ? 0.2914 0.2850 0.2165 0.0116  -0.0231 -0.0145 93  ALA   A O   
1365 C  CB  . ALA   A 93  ? 0.2490 0.2280 0.1805 0.0121  -0.0131 -0.0042 93  ALA   A CB  
1371 N  N   . ALA   A 94  ? 0.2760 0.2635 0.2092 0.0185  -0.0296 -0.0062 94  ALA   A N   
1372 C  CA  . ALA   A 94  ? 0.2461 0.2422 0.1869 0.0200  -0.0344 -0.0117 94  ALA   A CA  
1373 C  C   . ALA   A 94  ? 0.2340 0.2355 0.1892 0.0174  -0.0300 -0.0181 94  ALA   A C   
1374 O  O   . ALA   A 94  ? 0.2353 0.2431 0.1935 0.0157  -0.0319 -0.0244 94  ALA   A O   
1375 C  CB  . ALA   A 94  ? 0.2653 0.2629 0.2128 0.0255  -0.0408 -0.0097 94  ALA   A CB  
1381 N  N   . SER   A 95  ? 0.2359 0.2346 0.2002 0.0168  -0.0252 -0.0163 95  SER   A N   
1382 C  CA  . SER   A 95  ? 0.2157 0.2170 0.1931 0.0136  -0.0223 -0.0201 95  SER   A CA  
1383 C  C   . SER   A 95  ? 0.2157 0.2114 0.1975 0.0125  -0.0172 -0.0160 95  SER   A C   
1384 O  O   . SER   A 95  ? 0.2190 0.2170 0.2075 0.0127  -0.0167 -0.0132 95  SER   A O   
1385 C  CB  . SER   A 95  ? 0.1999 0.2099 0.1884 0.0132  -0.0258 -0.0225 95  SER   A CB  
1386 O  OG  . SER   A 95  ? 0.2210 0.2316 0.2207 0.0082  -0.0239 -0.0248 95  SER   A OG  
1392 N  N   . PRO   A 96  ? 0.2262 0.2164 0.2048 0.0113  -0.0133 -0.0164 96  PRO   A N   
1393 C  CA  . PRO   A 96  ? 0.2279 0.2132 0.2116 0.0104  -0.0093 -0.0128 96  PRO   A CA  
1394 C  C   . PRO   A 96  ? 0.2330 0.2194 0.2293 0.0073  -0.0099 -0.0125 96  PRO   A C   
1395 O  O   . PRO   A 96  ? 0.2276 0.2126 0.2271 0.0063  -0.0079 -0.0077 96  PRO   A O   
1396 C  CB  . PRO   A 96  ? 0.2546 0.2366 0.2354 0.0096  -0.0062 -0.0162 96  PRO   A CB  
1397 C  CG  . PRO   A 96  ? 0.2409 0.2259 0.2086 0.0102  -0.0072 -0.0182 96  PRO   A CG  
1398 C  CD  . PRO   A 96  ? 0.2545 0.2445 0.2244 0.0106  -0.0123 -0.0207 96  PRO   A CD  
1406 N  N   . THR   A 97  ? 0.2048 0.1937 0.2076 0.0048  -0.0128 -0.0170 97  THR   A N   
1407 C  CA  . THR   A 97  ? 0.2062 0.1950 0.2200 -0.0002 -0.0140 -0.0153 97  THR   A CA  
1408 C  C   . THR   A 97  ? 0.2170 0.2148 0.2332 -0.0017 -0.0141 -0.0119 97  THR   A C   
1409 O  O   . THR   A 97  ? 0.2057 0.2044 0.2267 -0.0060 -0.0128 -0.0074 97  THR   A O   
1410 C  CB  . THR   A 97  ? 0.2175 0.2054 0.2383 -0.0031 -0.0176 -0.0215 97  THR   A CB  
1411 O  OG1 . THR   A 97  ? 0.2177 0.2127 0.2337 -0.0009 -0.0198 -0.0268 97  THR   A OG1 
1412 C  CG2 . THR   A 97  ? 0.2538 0.2332 0.2771 -0.0020 -0.0177 -0.0260 97  THR   A CG2 
1420 N  N   . ASN   A 98  ? 0.1835 0.1892 0.1967 0.0016  -0.0160 -0.0145 98  ASN   A N   
1421 C  CA  . ASN   A 98  ? 0.1848 0.2014 0.2020 0.0016  -0.0161 -0.0135 98  ASN   A CA  
1422 C  C   . ASN   A 98  ? 0.2177 0.2324 0.2316 0.0039  -0.0127 -0.0090 98  ASN   A C   
1423 O  O   . ASN   A 98  ? 0.1899 0.2118 0.2090 0.0006  -0.0105 -0.0072 98  ASN   A O   
1424 C  CB  . ASN   A 98  ? 0.1792 0.2033 0.1944 0.0067  -0.0203 -0.0177 98  ASN   A CB  
1425 C  CG  . ASN   A 98  ? 0.1908 0.2217 0.2118 0.0037  -0.0240 -0.0231 98  ASN   A CG  
1426 O  OD1 . ASN   A 98  ? 0.2170 0.2471 0.2445 -0.0028 -0.0234 -0.0238 98  ASN   A OD1 
1427 N  ND2 . ASN   A 98  ? 0.2175 0.2548 0.2365 0.0084  -0.0288 -0.0268 98  ASN   A ND2 
1434 N  N   . ASP   A 99  ? 0.2045 0.2108 0.2093 0.0089  -0.0121 -0.0075 99  ASP   A N   
1435 C  CA  . ASP   A 99  ? 0.1890 0.1926 0.1909 0.0111  -0.0093 -0.0039 99  ASP   A CA  
1436 C  C   . ASP   A 99  ? 0.2258 0.2270 0.2312 0.0063  -0.0057 -0.0002 99  ASP   A C   
1437 O  O   . ASP   A 99  ? 0.2024 0.2074 0.2090 0.0059  -0.0035 0.0018  99  ASP   A O   
1438 C  CB  . ASP   A 99  ? 0.1936 0.1875 0.1849 0.0153  -0.0096 -0.0023 99  ASP   A CB  
1439 C  CG  . ASP   A 99  ? 0.2482 0.2432 0.2349 0.0206  -0.0144 -0.0032 99  ASP   A CG  
1440 O  OD1 . ASP   A 99  ? 0.2537 0.2572 0.2473 0.0229  -0.0169 -0.0056 99  ASP   A OD1 
1441 O  OD2 . ASP   A 99  ? 0.2393 0.2273 0.2157 0.0220  -0.0163 -0.0019 99  ASP   A OD2 
1446 N  N   . ALA   A 100 ? 0.1899 0.1850 0.1974 0.0026  -0.0058 0.0001  100 ALA   A N   
1447 C  CA  . ALA   A 100 ? 0.1975 0.1886 0.2085 -0.0018 -0.0044 0.0044  100 ALA   A CA  
1448 C  C   . ALA   A 100 ? 0.2084 0.2083 0.2253 -0.0085 -0.0046 0.0069  100 ALA   A C   
1449 O  O   . ALA   A 100 ? 0.2079 0.2095 0.2248 -0.0119 -0.0029 0.0115  100 ALA   A O   
1450 C  CB  . ALA   A 100 ? 0.2206 0.2022 0.2347 -0.0031 -0.0062 0.0031  100 ALA   A CB  
1456 N  N   . LEU   A 101 ? 0.2009 0.2076 0.2225 -0.0114 -0.0068 0.0040  101 LEU   A N   
1457 C  CA  . LEU   A 101 ? 0.1790 0.1967 0.2060 -0.0194 -0.0065 0.0060  101 LEU   A CA  
1458 C  C   . LEU   A 101 ? 0.2084 0.2401 0.2347 -0.0180 -0.0032 0.0049  101 LEU   A C   
1459 O  O   . LEU   A 101 ? 0.2043 0.2435 0.2313 -0.0244 -0.0009 0.0085  101 LEU   A O   
1460 C  CB  . LEU   A 101 ? 0.2179 0.2414 0.2509 -0.0225 -0.0094 0.0016  101 LEU   A CB  
1461 C  CG  . LEU   A 101 ? 0.2175 0.2510 0.2567 -0.0338 -0.0095 0.0042  101 LEU   A CG  
1462 C  CD1 . LEU   A 101 ? 0.2536 0.2757 0.2927 -0.0421 -0.0109 0.0126  101 LEU   A CD1 
1463 C  CD2 . LEU   A 101 ? 0.2148 0.2534 0.2606 -0.0364 -0.0128 -0.0012 101 LEU   A CD2 
1475 N  N   . TYR   A 102 ? 0.2061 0.2412 0.2309 -0.0095 -0.0036 -0.0003 102 TYR   A N   
1476 C  CA  . TYR   A 102 ? 0.1578 0.2050 0.1840 -0.0063 -0.0016 -0.0033 102 TYR   A CA  
1477 C  C   . TYR   A 102 ? 0.2033 0.2449 0.2244 -0.0057 0.0015  0.0007  102 TYR   A C   
1478 O  O   . TYR   A 102 ? 0.2138 0.2672 0.2368 -0.0088 0.0043  0.0001  102 TYR   A O   
1479 C  CB  . TYR   A 102 ? 0.2277 0.2757 0.2538 0.0033  -0.0049 -0.0090 102 TYR   A CB  
1480 C  CG  . TYR   A 102 ? 0.2170 0.2767 0.2473 0.0080  -0.0044 -0.0140 102 TYR   A CG  
1481 C  CD1 . TYR   A 102 ? 0.2553 0.3363 0.2952 0.0048  -0.0030 -0.0198 102 TYR   A CD1 
1482 C  CD2 . TYR   A 102 ? 0.2341 0.2843 0.2595 0.0151  -0.0052 -0.0136 102 TYR   A CD2 
1483 C  CE1 . TYR   A 102 ? 0.2637 0.3572 0.3094 0.0097  -0.0026 -0.0267 102 TYR   A CE1 
1484 C  CE2 . TYR   A 102 ? 0.2576 0.3174 0.2885 0.0200  -0.0055 -0.0195 102 TYR   A CE2 
1485 C  CZ  . TYR   A 102 ? 0.2951 0.3770 0.3367 0.0179  -0.0043 -0.0268 102 TYR   A CZ  
1486 O  OH  . TYR   A 102 ? 0.3528 0.4459 0.4017 0.0235  -0.0048 -0.0350 102 TYR   A OH  
1496 N  N   . ALA   A 103 ? 0.1919 0.2174 0.2068 -0.0021 0.0010  0.0039  103 ALA   A N   
1497 C  CA  . ALA   A 103 ? 0.2044 0.2250 0.2153 -0.0015 0.0035  0.0072  103 ALA   A CA  
1498 C  C   . ALA   A 103 ? 0.2407 0.2651 0.2526 -0.0101 0.0051  0.0123  103 ALA   A C   
1499 O  O   . ALA   A 103 ? 0.2240 0.2549 0.2346 -0.0116 0.0076  0.0131  103 ALA   A O   
1500 C  CB  . ALA   A 103 ? 0.2247 0.2294 0.2299 0.0023  0.0031  0.0092  103 ALA   A CB  
1506 N  N   . GLY   A 104 ? 0.1990 0.2187 0.2129 -0.0161 0.0031  0.0160  104 GLY   A N   
1507 C  CA  . GLY   A 104 ? 0.2072 0.2289 0.2212 -0.0254 0.0029  0.0226  104 GLY   A CA  
1508 C  C   . GLY   A 104 ? 0.2185 0.2601 0.2338 -0.0320 0.0057  0.0215  104 GLY   A C   
1509 O  O   . GLY   A 104 ? 0.2462 0.2939 0.2581 -0.0380 0.0074  0.0257  104 GLY   A O   
1513 N  N   . TYR   A 105 ? 0.2000 0.2538 0.2204 -0.0313 0.0063  0.0152  105 TYR   A N   
1514 C  CA  . TYR   A 105 ? 0.1883 0.2652 0.2120 -0.0368 0.0096  0.0113  105 TYR   A CA  
1515 C  C   . TYR   A 105 ? 0.1992 0.2845 0.2208 -0.0321 0.0129  0.0072  105 TYR   A C   
1516 O  O   . TYR   A 105 ? 0.2202 0.3192 0.2398 -0.0395 0.0161  0.0085  105 TYR   A O   
1517 C  CB  . TYR   A 105 ? 0.2415 0.3301 0.2730 -0.0338 0.0088  0.0029  105 TYR   A CB  
1518 C  CG  . TYR   A 105 ? 0.2608 0.3771 0.2984 -0.0390 0.0125  -0.0037 105 TYR   A CG  
1519 C  CD1 . TYR   A 105 ? 0.2438 0.3736 0.2849 -0.0316 0.0147  -0.0127 105 TYR   A CD1 
1520 C  CD2 . TYR   A 105 ? 0.2895 0.4193 0.3302 -0.0520 0.0138  -0.0015 105 TYR   A CD2 
1521 C  CE1 . TYR   A 105 ? 0.3078 0.4661 0.3563 -0.0362 0.0184  -0.0210 105 TYR   A CE1 
1522 C  CE2 . TYR   A 105 ? 0.2753 0.4341 0.3219 -0.0581 0.0181  -0.0086 105 TYR   A CE2 
1523 C  CZ  . TYR   A 105 ? 0.3096 0.4838 0.3606 -0.0497 0.0207  -0.0192 105 TYR   A CZ  
1524 O  OH  . TYR   A 105 ? 0.3164 0.5225 0.3750 -0.0554 0.0253  -0.0285 105 TYR   A OH  
1534 N  N   . VAL   A 106 ? 0.2138 0.2910 0.2355 -0.0204 0.0118  0.0023  106 VAL   A N   
1535 C  CA  . VAL   A 106 ? 0.1891 0.2723 0.2105 -0.0149 0.0139  -0.0028 106 VAL   A CA  
1536 C  C   . VAL   A 106 ? 0.2144 0.2934 0.2289 -0.0198 0.0158  0.0037  106 VAL   A C   
1537 O  O   . VAL   A 106 ? 0.2183 0.3122 0.2324 -0.0229 0.0189  0.0006  106 VAL   A O   
1538 C  CB  . VAL   A 106 ? 0.2473 0.3173 0.2688 -0.0028 0.0109  -0.0066 106 VAL   A CB  
1539 C  CG1 . VAL   A 106 ? 0.2627 0.3328 0.2831 0.0023  0.0120  -0.0102 106 VAL   A CG1 
1540 C  CG2 . VAL   A 106 ? 0.2576 0.3352 0.2864 0.0026  0.0078  -0.0140 106 VAL   A CG2 
1550 N  N   . ILE   A 107 ? 0.2030 0.2631 0.2125 -0.0204 0.0137  0.0117  107 ILE   A N   
1551 C  CA  . ILE   A 107 ? 0.1991 0.2543 0.2030 -0.0236 0.0143  0.0175  107 ILE   A CA  
1552 C  C   . ILE   A 107 ? 0.2045 0.2721 0.2057 -0.0359 0.0152  0.0230  107 ILE   A C   
1553 O  O   . ILE   A 107 ? 0.2404 0.3173 0.2375 -0.0396 0.0172  0.0236  107 ILE   A O   
1554 C  CB  . ILE   A 107 ? 0.1874 0.2212 0.1891 -0.0207 0.0111  0.0233  107 ILE   A CB  
1555 C  CG1 . ILE   A 107 ? 0.2241 0.2480 0.2261 -0.0105 0.0110  0.0184  107 ILE   A CG1 
1556 C  CG2 . ILE   A 107 ? 0.2444 0.2740 0.2417 -0.0242 0.0105  0.0293  107 ILE   A CG2 
1557 C  CD1 . ILE   A 107 ? 0.2585 0.2668 0.2603 -0.0082 0.0085  0.0208  107 ILE   A CD1 
1569 N  N   . LYS   A 108 ? 0.2210 0.2892 0.2239 -0.0433 0.0134  0.0273  108 LYS   A N   
1570 C  CA  . LYS   A 108 ? 0.2331 0.3124 0.2322 -0.0572 0.0137  0.0341  108 LYS   A CA  
1571 C  C   . LYS   A 108 ? 0.2458 0.3527 0.2451 -0.0613 0.0194  0.0267  108 LYS   A C   
1572 O  O   . LYS   A 108 ? 0.2472 0.3652 0.2398 -0.0700 0.0212  0.0305  108 LYS   A O   
1573 C  CB  . LYS   A 108 ? 0.2976 0.3727 0.3002 -0.0640 0.0107  0.0382  108 LYS   A CB  
1574 C  CG  . LYS   A 108 ? 0.3411 0.4281 0.3403 -0.0805 0.0107  0.0457  108 LYS   A CG  
1575 C  CD  . LYS   A 108 ? 0.3434 0.4151 0.3351 -0.0883 0.0052  0.0593  108 LYS   A CD  
1576 C  CE  . LYS   A 108 ? 0.4126 0.4969 0.3986 -0.1066 0.0049  0.0681  108 LYS   A CE  
1577 N  NZ  . LYS   A 108 ? 0.4847 0.5959 0.4644 -0.1127 0.0116  0.0647  108 LYS   A NZ  
1591 N  N   . HIS   A 109 ? 0.2358 0.3555 0.2432 -0.0551 0.0219  0.0154  109 HIS   A N   
1592 C  CA  . HIS   A 109 ? 0.2287 0.3775 0.2394 -0.0584 0.0271  0.0057  109 HIS   A CA  
1593 C  C   . HIS   A 109 ? 0.2640 0.4174 0.2736 -0.0510 0.0293  -0.0013 109 HIS   A C   
1594 O  O   . HIS   A 109 ? 0.2503 0.4270 0.2589 -0.0570 0.0336  -0.0066 109 HIS   A O   
1595 C  CB  . HIS   A 109 ? 0.2736 0.4344 0.2956 -0.0539 0.0275  -0.0045 109 HIS   A CB  
1596 C  CG  . HIS   A 109 ? 0.2499 0.4144 0.2731 -0.0652 0.0268  0.0012  109 HIS   A CG  
1597 N  ND1 . HIS   A 109 ? 0.3077 0.4984 0.3318 -0.0790 0.0310  0.0000  109 HIS   A ND1 
1598 C  CD2 . HIS   A 109 ? 0.2810 0.4260 0.3041 -0.0663 0.0222  0.0086  109 HIS   A CD2 
1599 C  CE1 . HIS   A 109 ? 0.3189 0.5050 0.3438 -0.0881 0.0287  0.0068  109 HIS   A CE1 
1600 N  NE2 . HIS   A 109 ? 0.2983 0.4562 0.3230 -0.0801 0.0231  0.0117  109 HIS   A NE2 
1608 N  N   . MET   A 110 ? 0.2461 0.3784 0.2552 -0.0396 0.0264  -0.0012 110 MET   A N   
1609 C  CA  A MET   A 110 ? 0.2386 0.3729 0.2463 -0.0341 0.0278  -0.0066 110 MET   A CA  
1610 C  CA  B MET   A 110 ? 0.2382 0.3725 0.2458 -0.0341 0.0278  -0.0067 110 MET   A CA  
1611 C  C   . MET   A 110 ? 0.2864 0.4260 0.2843 -0.0444 0.0292  0.0008  110 MET   A C   
1612 O  O   . MET   A 110 ? 0.2719 0.4318 0.2687 -0.0476 0.0329  -0.0060 110 MET   A O   
1613 C  CB  A MET   A 110 ? 0.2360 0.3453 0.2439 -0.0224 0.0242  -0.0058 110 MET   A CB  
1614 C  CB  B MET   A 110 ? 0.2354 0.3447 0.2432 -0.0224 0.0243  -0.0058 110 MET   A CB  
1615 C  CG  A MET   A 110 ? 0.2665 0.3751 0.2746 -0.0157 0.0248  -0.0123 110 MET   A CG  
1616 C  CG  B MET   A 110 ? 0.2662 0.3756 0.2741 -0.0161 0.0250  -0.0123 110 MET   A CG  
1617 S  SD  A MET   A 110 ? 0.2799 0.3591 0.2830 -0.0095 0.0216  -0.0050 110 MET   A SD  
1618 S  SD  B MET   A 110 ? 0.2653 0.3664 0.2630 -0.0217 0.0250  -0.0031 110 MET   A SD  
1619 C  CE  A MET   A 110 ? 0.2967 0.3717 0.2912 -0.0201 0.0211  0.0080  110 MET   A CE  
1620 C  CE  B MET   A 110 ? 0.2894 0.3616 0.2848 -0.0181 0.0208  0.0073  110 MET   A CE  
1639 N  N   . TYR   A 111 ? 0.2486 0.3709 0.2394 -0.0499 0.0257  0.0143  111 TYR   A N   
1640 C  CA  . TYR   A 111 ? 0.2532 0.3785 0.2341 -0.0597 0.0251  0.0229  111 TYR   A CA  
1641 C  C   . TYR   A 111 ? 0.2734 0.4239 0.2496 -0.0745 0.0284  0.0245  111 TYR   A C   
1642 O  O   . TYR   A 111 ? 0.2740 0.4381 0.2421 -0.0820 0.0301  0.0259  111 TYR   A O   
1643 C  CB  . TYR   A 111 ? 0.2689 0.3691 0.2459 -0.0612 0.0189  0.0363  111 TYR   A CB  
1644 C  CG  . TYR   A 111 ? 0.2487 0.3302 0.2265 -0.0508 0.0165  0.0361  111 TYR   A CG  
1645 C  CD1 . TYR   A 111 ? 0.2727 0.3571 0.2456 -0.0507 0.0167  0.0360  111 TYR   A CD1 
1646 C  CD2 . TYR   A 111 ? 0.2454 0.3081 0.2288 -0.0417 0.0143  0.0352  111 TYR   A CD2 
1647 C  CE1 . TYR   A 111 ? 0.2660 0.3349 0.2407 -0.0420 0.0148  0.0352  111 TYR   A CE1 
1648 C  CE2 . TYR   A 111 ? 0.2412 0.2894 0.2254 -0.0336 0.0129  0.0346  111 TYR   A CE2 
1649 C  CZ  . TYR   A 111 ? 0.2172 0.2685 0.1975 -0.0338 0.0132  0.0346  111 TYR   A CZ  
1650 O  OH  . TYR   A 111 ? 0.2338 0.2724 0.2156 -0.0268 0.0121  0.0335  111 TYR   A OH  
1660 N  N   . HIS   A 112 ? 0.2286 0.3870 0.2092 -0.0798 0.0295  0.0241  112 HIS   A N   
1661 C  CA  . HIS   A 112 ? 0.2582 0.4429 0.2342 -0.0956 0.0333  0.0253  112 HIS   A CA  
1662 C  C   . HIS   A 112 ? 0.2783 0.4928 0.2594 -0.0928 0.0397  0.0084  112 HIS   A C   
1663 O  O   . HIS   A 112 ? 0.2840 0.5126 0.2581 -0.1000 0.0399  0.0065  112 HIS   A O   
1664 C  CB  . HIS   A 112 ? 0.2922 0.4774 0.2727 -0.1025 0.0325  0.0289  112 HIS   A CB  
1665 C  CG  . HIS   A 112 ? 0.2999 0.5054 0.2765 -0.1143 0.0336  0.0270  112 HIS   A CG  
1666 N  ND1 . HIS   A 112 ? 0.4265 0.6569 0.4118 -0.1133 0.0386  0.0127  112 HIS   A ND1 
1667 C  CD2 . HIS   A 112 ? 0.3750 0.5788 0.3401 -0.1270 0.0296  0.0372  112 HIS   A CD2 
1668 C  CE1 . HIS   A 112 ? 0.4255 0.6697 0.4038 -0.1257 0.0384  0.0142  112 HIS   A CE1 
1669 N  NE2 . HIS   A 112 ? 0.4401 0.6687 0.4058 -0.1346 0.0330  0.0294  112 HIS   A NE2 
1677 N  N   . ASP   A 113 ? 0.2669 0.4848 0.2609 -0.0798 0.0414  -0.0052 113 ASP   A N   
1678 C  CA  . ASP   A 113 ? 0.2938 0.5404 0.2965 -0.0758 0.0465  -0.0234 113 ASP   A CA  
1679 C  C   . ASP   A 113 ? 0.2670 0.5162 0.2660 -0.0711 0.0471  -0.0294 113 ASP   A C   
1680 O  O   . ASP   A 113 ? 0.2918 0.5606 0.2902 -0.0743 0.0483  -0.0390 113 ASP   A O   
1681 C  CB  . ASP   A 113 ? 0.2893 0.5319 0.3073 -0.0611 0.0448  -0.0348 113 ASP   A CB  
1682 C  CG  . ASP   A 113 ? 0.3134 0.5656 0.3380 -0.0665 0.0453  -0.0349 113 ASP   A CG  
1683 O  OD1 . ASP   A 113 ? 0.2977 0.5531 0.3145 -0.0815 0.0461  -0.0238 113 ASP   A OD1 
1684 O  OD2 . ASP   A 113 ? 0.2751 0.5253 0.3120 -0.0550 0.0429  -0.0442 113 ASP   A OD2 
1689 N  N   . TRP   A 114 ? 0.2660 0.4899 0.2621 -0.0626 0.0437  -0.0240 114 TRP   A N   
1690 C  CA  . TRP   A 114 ? 0.2933 0.5194 0.2877 -0.0574 0.0443  -0.0308 114 TRP   A CA  
1691 C  C   . TRP   A 114 ? 0.3618 0.5924 0.3413 -0.0697 0.0447  -0.0206 114 TRP   A C   
1692 O  O   . TRP   A 114 ? 0.3261 0.5678 0.3040 -0.0691 0.0453  -0.0289 114 TRP   A O   
1693 C  CB  . TRP   A 114 ? 0.2945 0.4904 0.2928 -0.0428 0.0395  -0.0303 114 TRP   A CB  
1694 C  CG  . TRP   A 114 ? 0.3312 0.5240 0.3433 -0.0295 0.0380  -0.0425 114 TRP   A CG  
1695 C  CD1 . TRP   A 114 ? 0.3452 0.5579 0.3681 -0.0279 0.0399  -0.0537 114 TRP   A CD1 
1696 C  CD2 . TRP   A 114 ? 0.3558 0.5242 0.3724 -0.0164 0.0336  -0.0443 114 TRP   A CD2 
1697 N  NE1 . TRP   A 114 ? 0.3877 0.5884 0.4216 -0.0136 0.0357  -0.0621 114 TRP   A NE1 
1698 C  CE2 . TRP   A 114 ? 0.3217 0.4946 0.3510 -0.0070 0.0319  -0.0558 114 TRP   A CE2 
1699 C  CE3 . TRP   A 114 ? 0.3579 0.5020 0.3691 -0.0123 0.0306  -0.0372 114 TRP   A CE3 
1700 C  CZ2 . TRP   A 114 ? 0.4247 0.5764 0.4596 0.0056  0.0266  -0.0588 114 TRP   A CZ2 
1701 C  CZ3 . TRP   A 114 ? 0.3703 0.4953 0.3872 -0.0007 0.0267  -0.0408 114 TRP   A CZ3 
1702 C  CH2 . TRP   A 114 ? 0.3354 0.4632 0.3631 0.0078  0.0243  -0.0506 114 TRP   A CH2 
1713 N  N   . TYR   A 115 ? 0.3400 0.5562 0.3094 -0.0793 0.0411  -0.0029 115 TYR   A N   
1714 C  CA  . TYR   A 115 ? 0.3104 0.5208 0.2669 -0.0875 0.0370  0.0082  115 TYR   A CA  
1715 C  C   . TYR   A 115 ? 0.3729 0.5847 0.3211 -0.1018 0.0330  0.0199  115 TYR   A C   
1716 O  O   . TYR   A 115 ? 0.4062 0.6145 0.3441 -0.1093 0.0284  0.0291  115 TYR   A O   
1717 C  CB  . TYR   A 115 ? 0.3311 0.5130 0.2847 -0.0812 0.0323  0.0185  115 TYR   A CB  
1718 C  CG  . TYR   A 115 ? 0.2885 0.4625 0.2522 -0.0653 0.0332  0.0056  115 TYR   A CG  
1719 C  CD1 . TYR   A 115 ? 0.3427 0.5309 0.3065 -0.0627 0.0359  -0.0055 115 TYR   A CD1 
1720 C  CD2 . TYR   A 115 ? 0.2849 0.4383 0.2577 -0.0540 0.0311  0.0043  115 TYR   A CD2 
1721 C  CE1 . TYR   A 115 ? 0.2914 0.4718 0.2647 -0.0494 0.0359  -0.0170 115 TYR   A CE1 
1722 C  CE2 . TYR   A 115 ? 0.2623 0.4082 0.2430 -0.0412 0.0313  -0.0062 115 TYR   A CE2 
1723 C  CZ  . TYR   A 115 ? 0.2946 0.4531 0.2758 -0.0390 0.0334  -0.0166 115 TYR   A CZ  
1724 O  OH  . TYR   A 115 ? 0.2771 0.4268 0.2664 -0.0272 0.0326  -0.0266 115 TYR   A OH  
1734 N  N   . GLY   A 116 ? 0.2893 0.5068 0.2419 -0.1058 0.0342  0.0192  116 GLY   A N   
1735 C  CA  . GLY   A 116 ? 0.3169 0.5339 0.2616 -0.1196 0.0299  0.0305  116 GLY   A CA  
1736 C  C   . GLY   A 116 ? 0.4320 0.6210 0.3697 -0.1228 0.0219  0.0485  116 GLY   A C   
1737 O  O   . GLY   A 116 ? 0.4598 0.6476 0.3883 -0.1337 0.0165  0.0584  116 GLY   A O   
1741 N  N   . VAL   A 117 ? 0.3610 0.5279 0.3036 -0.1134 0.0203  0.0525  117 VAL   A N   
1742 C  CA  . VAL   A 117 ? 0.4838 0.6228 0.4227 -0.1142 0.0116  0.0674  117 VAL   A CA  
1743 C  C   . VAL   A 117 ? 0.3904 0.5110 0.3375 -0.1097 0.0100  0.0709  117 VAL   A C   
1744 O  O   . VAL   A 117 ? 0.3666 0.4938 0.3221 -0.1035 0.0160  0.0620  117 VAL   A O   
1745 C  CB  . VAL   A 117 ? 0.4646 0.5932 0.4008 -0.1069 0.0094  0.0692  117 VAL   A CB  
1746 C  CG1 . VAL   A 117 ? 0.5032 0.6522 0.4325 -0.1106 0.0117  0.0634  117 VAL   A CG1 
1747 C  CG2 . VAL   A 117 ? 0.4299 0.5517 0.3747 -0.0934 0.0138  0.0611  117 VAL   A CG2 
1757 N  N   . GLU   A 118 ? 0.3688 0.4668 0.3146 -0.1129 0.0011  0.0832  118 GLU   A N   
1758 C  CA  . GLU   A 118 ? 0.3635 0.4404 0.3176 -0.1076 -0.0021 0.0864  118 GLU   A CA  
1759 C  C   . GLU   A 118 ? 0.3305 0.3943 0.2902 -0.0931 -0.0019 0.0815  118 GLU   A C   
1760 O  O   . GLU   A 118 ? 0.3823 0.4435 0.3378 -0.0901 -0.0036 0.0829  118 GLU   A O   
1761 C  CB  . GLU   A 118 ? 0.3851 0.4407 0.3383 -0.1127 -0.0131 0.0981  118 GLU   A CB  
1762 C  CG  . GLU   A 118 ? 0.5388 0.6023 0.4884 -0.1253 -0.0147 0.1020  118 GLU   A CG  
1763 C  CD  . GLU   A 118 ? 0.5517 0.6220 0.5088 -0.1265 -0.0096 0.0962  118 GLU   A CD  
1764 O  OE1 . GLU   A 118 ? 0.4789 0.5354 0.4451 -0.1189 -0.0101 0.0943  118 GLU   A OE1 
1765 O  OE2 . GLU   A 118 ? 0.4845 0.5747 0.4387 -0.1355 -0.0055 0.0934  118 GLU   A OE2 
1772 N  N   . ALA   A 119 ? 0.3069 0.3629 0.2765 -0.0826 -0.0002 0.0733  119 ALA   A N   
1773 C  CA  . ALA   A 119 ? 0.2996 0.3401 0.2748 -0.0684 -0.0012 0.0682  119 ALA   A CA  
1774 C  C   . ALA   A 119 ? 0.3108 0.3298 0.2865 -0.0680 -0.0101 0.0776  119 ALA   A C   
1775 O  O   . ALA   A 119 ? 0.3150 0.3272 0.2913 -0.0610 -0.0115 0.0764  119 ALA   A O   
1776 C  CB  . ALA   A 119 ? 0.2654 0.3015 0.2492 -0.0594 0.0013  0.0594  119 ALA   A CB  
1782 N  N   . LEU   A 120 ? 0.2831 0.2916 0.2598 -0.0757 -0.0166 0.0865  120 LEU   A N   
1783 C  CA  . LEU   A 120 ? 0.3034 0.2899 0.2835 -0.0748 -0.0269 0.0947  120 LEU   A CA  
1784 C  C   . LEU   A 120 ? 0.3943 0.3781 0.3690 -0.0877 -0.0342 0.1060  120 LEU   A C   
1785 O  O   . LEU   A 120 ? 0.3761 0.3700 0.3482 -0.0964 -0.0314 0.1066  120 LEU   A O   
1786 C  CB  . LEU   A 120 ? 0.2827 0.2533 0.2745 -0.0659 -0.0294 0.0889  120 LEU   A CB  
1787 C  CG  . LEU   A 120 ? 0.2678 0.2390 0.2653 -0.0522 -0.0233 0.0762  120 LEU   A CG  
1788 C  CD1 . LEU   A 120 ? 0.2899 0.2491 0.2970 -0.0467 -0.0255 0.0710  120 LEU   A CD1 
1789 C  CD2 . LEU   A 120 ? 0.3193 0.2863 0.3172 -0.0454 -0.0248 0.0754  120 LEU   A CD2 
1801 N  N   . THR   A 121 ? 0.3886 0.3601 0.3632 -0.0867 -0.0435 0.1118  121 THR   A N   
1802 C  CA  . THR   A 121 ? 0.4822 0.4489 0.4532 -0.0960 -0.0522 0.1204  121 THR   A CA  
1803 C  C   . THR   A 121 ? 0.4606 0.4044 0.4408 -0.0899 -0.0644 0.1234  121 THR   A C   
1804 O  O   . THR   A 121 ? 0.4546 0.3899 0.4422 -0.0790 -0.0661 0.1191  121 THR   A O   
1805 C  CB  . THR   A 121 ? 0.5419 0.5241 0.5001 -0.1049 -0.0519 0.1254  121 THR   A CB  
1806 O  OG1 . THR   A 121 ? 0.5281 0.5045 0.4868 -0.0984 -0.0563 0.1265  121 THR   A OG1 
1807 C  CG2 . THR   A 121 ? 0.4841 0.4921 0.4348 -0.1095 -0.0398 0.1196  121 THR   A CG2 
1815 N  N   . LYS   A 122 ? 0.4419 0.3765 0.4223 -0.0971 -0.0735 0.1305  122 LYS   A N   
1816 C  CA  . LYS   A 122 ? 0.5649 0.4782 0.5556 -0.0917 -0.0865 0.1328  122 LYS   A CA  
1817 C  C   . LYS   A 122 ? 0.6166 0.5295 0.6027 -0.0924 -0.0933 0.1386  122 LYS   A C   
1818 O  O   . LYS   A 122 ? 0.6071 0.5363 0.5818 -0.0971 -0.0871 0.1403  122 LYS   A O   
1819 C  CB  . LYS   A 122 ? 0.5711 0.4746 0.5636 -0.0999 -0.0942 0.1385  122 LYS   A CB  
1820 C  CG  . LYS   A 122 ? 0.6334 0.5390 0.6294 -0.1012 -0.0875 0.1334  122 LYS   A CG  
1821 C  CD  . LYS   A 122 ? 0.6666 0.5574 0.6688 -0.1058 -0.0969 0.1370  122 LYS   A CD  
1822 C  CE  . LYS   A 122 ? 0.6923 0.5891 0.6951 -0.1107 -0.0898 0.1335  122 LYS   A CE  
1823 N  NZ  . LYS   A 122 ? 0.6944 0.6101 0.6837 -0.1246 -0.0837 0.1393  122 LYS   A NZ  
1837 N  N   . SER   A 123 ? 0.6932 0.5891 0.6887 -0.0877 -0.1058 0.1406  123 SER   A N   
1838 C  CA  . SER   A 123 ? 0.6919 0.5858 0.6848 -0.0877 -0.1139 0.1460  123 SER   A CA  
1839 C  C   . SER   A 123 ? 0.6850 0.5871 0.6625 -0.1033 -0.1170 0.1578  123 SER   A C   
1840 O  O   . SER   A 123 ? 0.7206 0.6283 0.6912 -0.1056 -0.1197 0.1621  123 SER   A O   
1841 C  CB  . SER   A 123 ? 0.7579 0.6321 0.7658 -0.0797 -0.1273 0.1447  123 SER   A CB  
1842 O  OG  . SER   A 123 ? 0.9140 0.7836 0.9363 -0.0657 -0.1238 0.1324  123 SER   A OG  
1848 N  N   . ASP   A 124 ? 0.6654 0.5693 0.6376 -0.1139 -0.1166 0.1625  124 ASP   A N   
1849 C  CA  . ASP   A 124 ? 0.6485 0.5606 0.6061 -0.1302 -0.1202 0.1739  124 ASP   A CA  
1850 C  C   . ASP   A 124 ? 0.6207 0.5584 0.5655 -0.1385 -0.1061 0.1716  124 ASP   A C   
1851 O  O   . ASP   A 124 ? 0.6948 0.6427 0.6276 -0.1531 -0.1075 0.1794  124 ASP   A O   
1852 C  CB  . ASP   A 124 ? 0.6895 0.5866 0.6497 -0.1380 -0.1312 0.1817  124 ASP   A CB  
1853 C  CG  . ASP   A 124 ? 0.8102 0.7055 0.7761 -0.1377 -0.1258 0.1767  124 ASP   A CG  
1854 O  OD1 . ASP   A 124 ? 0.7011 0.6061 0.6697 -0.1307 -0.1136 0.1668  124 ASP   A OD1 
1855 O  OD2 . ASP   A 124 ? 0.9870 0.8707 0.9545 -0.1448 -0.1343 0.1830  124 ASP   A OD2 
1860 N  N   . GLY   A 125 ? 0.7096 0.6581 0.6570 -0.1302 -0.0936 0.1610  125 GLY   A N   
1861 C  CA  . GLY   A 125 ? 0.6296 0.6034 0.5670 -0.1365 -0.0808 0.1568  125 GLY   A CA  
1862 C  C   . GLY   A 125 ? 0.6591 0.6400 0.5973 -0.1412 -0.0737 0.1533  125 GLY   A C   
1863 O  O   . GLY   A 125 ? 0.5350 0.5379 0.4677 -0.1444 -0.0624 0.1472  125 GLY   A O   
1867 N  N   . SER   A 126 ? 0.6134 0.5773 0.5592 -0.1414 -0.0803 0.1562  126 SER   A N   
1868 C  CA  . SER   A 126 ? 0.5743 0.5444 0.5217 -0.1459 -0.0740 0.1527  126 SER   A CA  
1869 C  C   . SER   A 126 ? 0.6040 0.5782 0.5595 -0.1344 -0.0636 0.1410  126 SER   A C   
1870 O  O   . SER   A 126 ? 0.4819 0.4442 0.4455 -0.1220 -0.0650 0.1367  126 SER   A O   
1871 C  CB  . SER   A 126 ? 0.5885 0.5378 0.5426 -0.1488 -0.0846 0.1585  126 SER   A CB  
1872 O  OG  . SER   A 126 ? 0.6962 0.6244 0.6646 -0.1353 -0.0900 0.1540  126 SER   A OG  
1878 N  N   . PRO   A 127 ? 0.4931 0.4854 0.4467 -0.1388 -0.0534 0.1353  127 PRO   A N   
1879 C  CA  . PRO   A 127 ? 0.4656 0.4623 0.4270 -0.1289 -0.0442 0.1247  127 PRO   A CA  
1880 C  C   . PRO   A 127 ? 0.4194 0.3927 0.3936 -0.1195 -0.0496 0.1227  127 PRO   A C   
1881 O  O   . PRO   A 127 ? 0.4739 0.4324 0.4524 -0.1229 -0.0578 0.1271  127 PRO   A O   
1882 C  CB  . PRO   A 127 ? 0.5560 0.5742 0.5150 -0.1376 -0.0356 0.1204  127 PRO   A CB  
1883 C  CG  . PRO   A 127 ? 0.4791 0.5147 0.4253 -0.1492 -0.0353 0.1251  127 PRO   A CG  
1884 C  CD  . PRO   A 127 ? 0.5836 0.5980 0.5273 -0.1529 -0.0487 0.1371  127 PRO   A CD  
1892 N  N   . MET   A 128 ? 0.3935 0.3639 0.3739 -0.1079 -0.0452 0.1153  128 MET   A N   
1893 C  CA  A MET   A 128 ? 0.4003 0.3511 0.3933 -0.0980 -0.0495 0.1110  128 MET   A CA  
1894 C  CA  B MET   A 128 ? 0.4029 0.3536 0.3958 -0.0980 -0.0495 0.1110  128 MET   A CA  
1895 C  C   . MET   A 128 ? 0.3547 0.3136 0.3525 -0.0957 -0.0409 0.1030  128 MET   A C   
1896 O  O   . MET   A 128 ? 0.3542 0.3287 0.3489 -0.0918 -0.0320 0.0971  128 MET   A O   
1897 C  CB  A MET   A 128 ? 0.4090 0.3490 0.4057 -0.0865 -0.0529 0.1092  128 MET   A CB  
1898 C  CB  B MET   A 128 ? 0.4113 0.3506 0.4085 -0.0862 -0.0530 0.1090  128 MET   A CB  
1899 C  CG  A MET   A 128 ? 0.4455 0.3652 0.4559 -0.0763 -0.0595 0.1042  128 MET   A CG  
1900 C  CG  B MET   A 128 ? 0.4519 0.3698 0.4629 -0.0769 -0.0610 0.1049  128 MET   A CG  
1901 S  SD  A MET   A 128 ? 0.5749 0.4855 0.5898 -0.0650 -0.0648 0.1025  128 MET   A SD  
1902 S  SD  B MET   A 128 ? 0.4340 0.3455 0.4528 -0.0615 -0.0597 0.0966  128 MET   A SD  
1903 C  CE  A MET   A 128 ? 0.4460 0.3624 0.4644 -0.0545 -0.0544 0.0919  128 MET   A CE  
1904 C  CE  B MET   A 128 ? 0.4825 0.3979 0.4934 -0.0631 -0.0636 0.1037  128 MET   A CE  
1923 N  N   . GLN   A 129 ? 0.3467 0.2965 0.3527 -0.0969 -0.0440 0.1010  129 GLN   A N   
1924 C  CA  . GLN   A 129 ? 0.3447 0.3020 0.3570 -0.0910 -0.0372 0.0898  129 GLN   A CA  
1925 C  C   . GLN   A 129 ? 0.3490 0.3022 0.3656 -0.0743 -0.0343 0.0793  129 GLN   A C   
1926 O  O   . GLN   A 129 ? 0.3235 0.2603 0.3450 -0.0678 -0.0406 0.0798  129 GLN   A O   
1927 C  CB  . GLN   A 129 ? 0.3515 0.2965 0.3727 -0.0947 -0.0431 0.0893  129 GLN   A CB  
1928 C  CG  . GLN   A 129 ? 0.3575 0.3128 0.3843 -0.0886 -0.0368 0.0766  129 GLN   A CG  
1929 C  CD  . GLN   A 129 ? 0.3386 0.2807 0.3748 -0.0921 -0.0435 0.0753  129 GLN   A CD  
1930 O  OE1 . GLN   A 129 ? 0.3612 0.2818 0.4044 -0.0885 -0.0523 0.0763  129 GLN   A OE1 
1931 N  NE2 . GLN   A 129 ? 0.3274 0.2829 0.3654 -0.0983 -0.0398 0.0716  129 GLN   A NE2 
1940 N  N   . LEU   A 130 ? 0.2903 0.2590 0.3058 -0.0676 -0.0254 0.0694  130 LEU   A N   
1941 C  CA  . LEU   A 130 ? 0.2447 0.2102 0.2629 -0.0536 -0.0223 0.0599  130 LEU   A CA  
1942 C  C   . LEU   A 130 ? 0.2925 0.2471 0.3193 -0.0483 -0.0254 0.0532  130 LEU   A C   
1943 O  O   . LEU   A 130 ? 0.2808 0.2420 0.3097 -0.0504 -0.0236 0.0490  130 LEU   A O   
1944 C  CB  . LEU   A 130 ? 0.2472 0.2304 0.2613 -0.0490 -0.0135 0.0526  130 LEU   A CB  
1945 C  CG  . LEU   A 130 ? 0.3312 0.3232 0.3385 -0.0480 -0.0096 0.0541  130 LEU   A CG  
1946 C  CD1 . LEU   A 130 ? 0.3694 0.3681 0.3711 -0.0606 -0.0113 0.0638  130 LEU   A CD1 
1947 C  CD2 . LEU   A 130 ? 0.2964 0.3035 0.3022 -0.0426 -0.0025 0.0455  130 LEU   A CD2 
1959 N  N   . VAL   A 131 ? 0.2609 0.2008 0.2936 -0.0416 -0.0302 0.0510  131 VAL   A N   
1960 C  CA  . VAL   A 131 ? 0.2722 0.2033 0.3136 -0.0363 -0.0331 0.0427  131 VAL   A CA  
1961 C  C   . VAL   A 131 ? 0.2769 0.2129 0.3169 -0.0253 -0.0271 0.0329  131 VAL   A C   
1962 O  O   . VAL   A 131 ? 0.2547 0.1875 0.2949 -0.0199 -0.0268 0.0319  131 VAL   A O   
1963 C  CB  . VAL   A 131 ? 0.3228 0.2351 0.3738 -0.0367 -0.0435 0.0452  131 VAL   A CB  
1964 C  CG1 . VAL   A 131 ? 0.2959 0.2013 0.3570 -0.0299 -0.0459 0.0336  131 VAL   A CG1 
1965 C  CG2 . VAL   A 131 ? 0.3327 0.2383 0.3835 -0.0495 -0.0504 0.0570  131 VAL   A CG2 
1975 N  N   . MET   A 132 ? 0.2412 0.1854 0.2792 -0.0230 -0.0227 0.0261  132 MET   A N   
1976 C  CA  . MET   A 132 ? 0.2189 0.1689 0.2525 -0.0148 -0.0170 0.0186  132 MET   A CA  
1977 C  C   . MET   A 132 ? 0.2778 0.2231 0.3169 -0.0107 -0.0191 0.0094  132 MET   A C   
1978 O  O   . MET   A 132 ? 0.2605 0.2083 0.3012 -0.0127 -0.0202 0.0061  132 MET   A O   
1979 C  CB  . MET   A 132 ? 0.2388 0.2017 0.2653 -0.0150 -0.0119 0.0180  132 MET   A CB  
1980 C  CG  . MET   A 132 ? 0.2607 0.2318 0.2832 -0.0198 -0.0096 0.0247  132 MET   A CG  
1981 S  SD  . MET   A 132 ? 0.2525 0.2254 0.2688 -0.0150 -0.0054 0.0259  132 MET   A SD  
1982 C  CE  . MET   A 132 ? 0.2477 0.2288 0.2587 -0.0084 -0.0009 0.0193  132 MET   A CE  
1992 N  N   . ARG   A 133 ? 0.2668 0.2072 0.3095 -0.0051 -0.0194 0.0043  133 ARG   A N   
1993 C  CA  . ARG   A 133 ? 0.2480 0.1856 0.2973 -0.0012 -0.0214 -0.0062 133 ARG   A CA  
1994 C  C   . ARG   A 133 ? 0.2520 0.1990 0.2927 0.0034  -0.0148 -0.0128 133 ARG   A C   
1995 O  O   . ARG   A 133 ? 0.2547 0.2044 0.2909 0.0061  -0.0107 -0.0123 133 ARG   A O   
1996 C  CB  . ARG   A 133 ? 0.2542 0.1823 0.3151 0.0017  -0.0267 -0.0091 133 ARG   A CB  
1997 C  CG  . ARG   A 133 ? 0.2868 0.2038 0.3533 -0.0036 -0.0343 0.0008  133 ARG   A CG  
1998 C  CD  . ARG   A 133 ? 0.3065 0.2109 0.3880 -0.0006 -0.0432 -0.0039 133 ARG   A CD  
1999 N  NE  . ARG   A 133 ? 0.2979 0.2047 0.3832 0.0065  -0.0416 -0.0093 133 ARG   A NE  
2000 C  CZ  . ARG   A 133 ? 0.3360 0.2374 0.4359 0.0125  -0.0472 -0.0191 133 ARG   A CZ  
2001 N  NH1 . ARG   A 133 ? 0.3233 0.2125 0.4361 0.0123  -0.0567 -0.0226 133 ARG   A NH1 
2002 N  NH2 . ARG   A 133 ? 0.3166 0.2256 0.4195 0.0187  -0.0436 -0.0263 133 ARG   A NH2 
2016 N  N   . VAL   A 134 ? 0.2469 0.1984 0.2851 0.0034  -0.0144 -0.0186 134 VAL   A N   
2017 C  CA  A VAL   A 134 ? 0.2485 0.2087 0.2755 0.0058  -0.0095 -0.0223 134 VAL   A CA  
2018 C  CA  B VAL   A 134 ? 0.2480 0.2081 0.2750 0.0059  -0.0093 -0.0223 134 VAL   A CA  
2019 C  C   . VAL   A 134 ? 0.2419 0.2049 0.2715 0.0081  -0.0097 -0.0342 134 VAL   A C   
2020 O  O   . VAL   A 134 ? 0.2457 0.2043 0.2869 0.0081  -0.0143 -0.0405 134 VAL   A O   
2021 C  CB  A VAL   A 134 ? 0.2833 0.2485 0.3042 0.0035  -0.0098 -0.0188 134 VAL   A CB  
2022 C  CB  B VAL   A 134 ? 0.2899 0.2554 0.3096 0.0040  -0.0091 -0.0184 134 VAL   A CB  
2023 C  CG1 A VAL   A 134 ? 0.2296 0.2015 0.2381 0.0060  -0.0066 -0.0200 134 VAL   A CG1 
2024 C  CG1 B VAL   A 134 ? 0.3290 0.2948 0.3473 0.0018  -0.0083 -0.0090 134 VAL   A CG1 
2025 C  CG2 A VAL   A 134 ? 0.3339 0.2988 0.3555 0.0004  -0.0099 -0.0093 134 VAL   A CG2 
2026 C  CG2 B VAL   A 134 ? 0.3001 0.2655 0.3266 0.0014  -0.0136 -0.0227 134 VAL   A CG2 
2045 N  N   . HIS   A 135 ? 0.2286 0.1994 0.2473 0.0095  -0.0050 -0.0375 135 HIS   A N   
2046 C  CA  . HIS   A 135 ? 0.2538 0.2314 0.2723 0.0107  -0.0036 -0.0496 135 HIS   A CA  
2047 C  C   . HIS   A 135 ? 0.2612 0.2377 0.2931 0.0134  -0.0040 -0.0579 135 HIS   A C   
2048 O  O   . HIS   A 135 ? 0.2549 0.2345 0.2954 0.0149  -0.0060 -0.0702 135 HIS   A O   
2049 C  CB  . HIS   A 135 ? 0.2719 0.2519 0.2926 0.0097  -0.0075 -0.0564 135 HIS   A CB  
2050 C  CG  . HIS   A 135 ? 0.2539 0.2360 0.2650 0.0078  -0.0087 -0.0500 135 HIS   A CG  
2051 N  ND1 . HIS   A 135 ? 0.2821 0.2707 0.2774 0.0077  -0.0061 -0.0476 135 HIS   A ND1 
2052 C  CD2 . HIS   A 135 ? 0.2642 0.2439 0.2801 0.0058  -0.0130 -0.0470 135 HIS   A CD2 
2053 C  CE1 . HIS   A 135 ? 0.2605 0.2502 0.2525 0.0070  -0.0093 -0.0433 135 HIS   A CE1 
2054 N  NE2 . HIS   A 135 ? 0.2366 0.2223 0.2412 0.0057  -0.0129 -0.0434 135 HIS   A NE2 
2063 N  N   . TYR   A 136 ? 0.2461 0.2188 0.2810 0.0144  -0.0028 -0.0524 136 TYR   A N   
2064 C  CA  . TYR   A 136 ? 0.2421 0.2145 0.2910 0.0178  -0.0041 -0.0605 136 TYR   A CA  
2065 C  C   . TYR   A 136 ? 0.2499 0.2366 0.2954 0.0186  0.0021  -0.0719 136 TYR   A C   
2066 O  O   . TYR   A 136 ? 0.2438 0.2375 0.2750 0.0160  0.0084  -0.0677 136 TYR   A O   
2067 C  CB  . TYR   A 136 ? 0.2501 0.2160 0.3023 0.0183  -0.0049 -0.0510 136 TYR   A CB  
2068 C  CG  . TYR   A 136 ? 0.2622 0.2294 0.3282 0.0224  -0.0062 -0.0588 136 TYR   A CG  
2069 C  CD1 . TYR   A 136 ? 0.2781 0.2355 0.3618 0.0255  -0.0149 -0.0623 136 TYR   A CD1 
2070 C  CD2 . TYR   A 136 ? 0.2592 0.2373 0.3215 0.0229  0.0005  -0.0623 136 TYR   A CD2 
2071 C  CE1 . TYR   A 136 ? 0.2941 0.2530 0.3925 0.0305  -0.0175 -0.0702 136 TYR   A CE1 
2072 C  CE2 . TYR   A 136 ? 0.2841 0.2657 0.3608 0.0269  -0.0008 -0.0705 136 TYR   A CE2 
2073 C  CZ  . TYR   A 136 ? 0.2971 0.2693 0.3924 0.0314  -0.0101 -0.0748 136 TYR   A CZ  
2074 O  OH  . TYR   A 136 ? 0.3557 0.3320 0.4672 0.0366  -0.0126 -0.0840 136 TYR   A OH  
2084 N  N   . GLY   A 137 ? 0.2782 0.2696 0.3374 0.0218  0.0000  -0.0869 137 GLY   A N   
2085 C  CA  . GLY   A 137 ? 0.2595 0.2675 0.3191 0.0225  0.0062  -0.1000 137 GLY   A CA  
2086 C  C   . GLY   A 137 ? 0.2507 0.2724 0.2924 0.0178  0.0125  -0.1036 137 GLY   A C   
2087 O  O   . GLY   A 137 ? 0.2736 0.2917 0.3040 0.0152  0.0110  -0.0975 137 GLY   A O   
2091 N  N   . GLN   A 138 ? 0.2594 0.2982 0.2985 0.0161  0.0193  -0.1137 138 GLN   A N   
2092 C  CA  . GLN   A 138 ? 0.2683 0.3224 0.2890 0.0102  0.0255  -0.1176 138 GLN   A CA  
2093 C  C   . GLN   A 138 ? 0.2988 0.3582 0.3036 0.0043  0.0327  -0.1079 138 GLN   A C   
2094 O  O   . GLN   A 138 ? 0.3278 0.3970 0.3394 0.0041  0.0373  -0.1138 138 GLN   A O   
2095 C  CB  . GLN   A 138 ? 0.3826 0.4553 0.4138 0.0115  0.0278  -0.1397 138 GLN   A CB  
2096 C  CG  . GLN   A 138 ? 0.4143 0.4789 0.4676 0.0186  0.0193  -0.1508 138 GLN   A CG  
2097 C  CD  . GLN   A 138 ? 0.6672 0.7506 0.7324 0.0206  0.0206  -0.1740 138 GLN   A CD  
2098 O  OE1 . GLN   A 138 ? 0.6396 0.7207 0.7284 0.0264  0.0146  -0.1813 138 GLN   A OE1 
2099 N  NE2 . GLN   A 138 ? 0.6047 0.7062 0.6530 0.0140  0.0266  -0.1778 138 GLN   A NE2 
2108 N  N   . GLY   A 139 ? 0.2923 0.3449 0.2772 -0.0002 0.0327  -0.0932 139 GLY   A N   
2109 C  CA  . GLY   A 139 ? 0.2838 0.3378 0.2529 -0.0062 0.0379  -0.0826 139 GLY   A CA  
2110 C  C   . GLY   A 139 ? 0.3067 0.3523 0.2852 -0.0038 0.0382  -0.0758 139 GLY   A C   
2111 O  O   . GLY   A 139 ? 0.3055 0.3581 0.2789 -0.0084 0.0439  -0.0743 139 GLY   A O   
2115 N  N   . TYR   A 140 ? 0.2870 0.3182 0.2781 0.0023  0.0321  -0.0711 140 TYR   A N   
2116 C  CA  . TYR   A 140 ? 0.2728 0.2967 0.2738 0.0050  0.0313  -0.0657 140 TYR   A CA  
2117 C  C   . TYR   A 140 ? 0.2531 0.2670 0.2403 0.0020  0.0316  -0.0499 140 TYR   A C   
2118 O  O   . TYR   A 140 ? 0.2320 0.2354 0.2144 0.0032  0.0273  -0.0416 140 TYR   A O   
2119 C  CB  . TYR   A 140 ? 0.2739 0.2874 0.2933 0.0115  0.0239  -0.0674 140 TYR   A CB  
2120 C  CG  . TYR   A 140 ? 0.2729 0.2803 0.3034 0.0143  0.0220  -0.0628 140 TYR   A CG  
2121 C  CD1 . TYR   A 140 ? 0.3443 0.3610 0.3872 0.0162  0.0240  -0.0722 140 TYR   A CD1 
2122 C  CD2 . TYR   A 140 ? 0.2487 0.2427 0.2772 0.0147  0.0181  -0.0498 140 TYR   A CD2 
2123 C  CE1 . TYR   A 140 ? 0.3617 0.3730 0.4144 0.0189  0.0212  -0.0678 140 TYR   A CE1 
2124 C  CE2 . TYR   A 140 ? 0.3179 0.3072 0.3547 0.0166  0.0160  -0.0454 140 TYR   A CE2 
2125 C  CZ  . TYR   A 140 ? 0.3291 0.3262 0.3777 0.0188  0.0171  -0.0539 140 TYR   A CZ  
2126 O  OH  . TYR   A 140 ? 0.4681 0.4605 0.5244 0.0207  0.0139  -0.0490 140 TYR   A OH  
2136 N  N   . GLU   A 141 ? 0.2483 0.2661 0.2303 -0.0018 0.0365  -0.0469 141 GLU   A N   
2137 C  CA  . GLU   A 141 ? 0.2317 0.2400 0.2007 -0.0050 0.0367  -0.0335 141 GLU   A CA  
2138 C  C   . GLU   A 141 ? 0.2347 0.2357 0.2141 -0.0017 0.0349  -0.0287 141 GLU   A C   
2139 O  O   . GLU   A 141 ? 0.2434 0.2455 0.2209 -0.0047 0.0381  -0.0257 141 GLU   A O   
2140 C  CB  . GLU   A 141 ? 0.2571 0.2734 0.2114 -0.0132 0.0426  -0.0322 141 GLU   A CB  
2141 C  CG  . GLU   A 141 ? 0.3013 0.3268 0.2427 -0.0179 0.0443  -0.0365 141 GLU   A CG  
2142 C  CD  . GLU   A 141 ? 0.3990 0.4267 0.3196 -0.0278 0.0477  -0.0290 141 GLU   A CD  
2143 O  OE1 . GLU   A 141 ? 0.3851 0.4240 0.3053 -0.0338 0.0540  -0.0327 141 GLU   A OE1 
2144 O  OE2 . GLU   A 141 ? 0.3246 0.3445 0.2294 -0.0302 0.0438  -0.0205 141 GLU   A OE2 
2151 N  N   . ASN   A 142 ? 0.2183 0.2122 0.2084 0.0037  0.0295  -0.0280 142 ASN   A N   
2152 C  CA  . ASN   A 142 ? 0.2060 0.1931 0.2043 0.0062  0.0269  -0.0225 142 ASN   A CA  
2153 C  C   . ASN   A 142 ? 0.2276 0.2064 0.2318 0.0095  0.0207  -0.0191 142 ASN   A C   
2154 O  O   . ASN   A 142 ? 0.2340 0.2122 0.2373 0.0100  0.0185  -0.0214 142 ASN   A O   
2155 C  CB  . ASN   A 142 ? 0.2210 0.2144 0.2333 0.0080  0.0277  -0.0297 142 ASN   A CB  
2156 C  CG  . ASN   A 142 ? 0.2149 0.2065 0.2275 0.0069  0.0287  -0.0239 142 ASN   A CG  
2157 O  OD1 . ASN   A 142 ? 0.2163 0.1995 0.2236 0.0068  0.0267  -0.0149 142 ASN   A OD1 
2158 N  ND2 . ASN   A 142 ? 0.2645 0.2653 0.2849 0.0065  0.0316  -0.0304 142 ASN   A ND2 
2165 N  N   . ALA   A 143 ? 0.2130 0.1866 0.2228 0.0107  0.0179  -0.0135 143 ALA   A N   
2166 C  CA  . ALA   A 143 ? 0.1927 0.1596 0.2085 0.0119  0.0122  -0.0093 143 ALA   A CA  
2167 C  C   . ALA   A 143 ? 0.2025 0.1675 0.2284 0.0132  0.0092  -0.0078 143 ALA   A C   
2168 O  O   . ALA   A 143 ? 0.2116 0.1806 0.2382 0.0132  0.0121  -0.0091 143 ALA   A O   
2169 C  CB  . ALA   A 143 ? 0.2050 0.1689 0.2117 0.0103  0.0120  -0.0013 143 ALA   A CB  
2175 N  N   . TYR   A 144 ? 0.2056 0.1644 0.2392 0.0136  0.0028  -0.0048 144 TYR   A N   
2176 C  CA  . TYR   A 144 ? 0.2099 0.1658 0.2522 0.0146  -0.0018 -0.0023 144 TYR   A CA  
2177 C  C   . TYR   A 144 ? 0.2388 0.1867 0.2833 0.0121  -0.0088 0.0059  144 TYR   A C   
2178 O  O   . TYR   A 144 ? 0.2327 0.1769 0.2769 0.0103  -0.0111 0.0068  144 TYR   A O   
2179 C  CB  . TYR   A 144 ? 0.2274 0.1855 0.2838 0.0190  -0.0042 -0.0124 144 TYR   A CB  
2180 C  CG  . TYR   A 144 ? 0.2582 0.2109 0.3252 0.0213  -0.0102 -0.0182 144 TYR   A CG  
2181 C  CD1 . TYR   A 144 ? 0.2735 0.2313 0.3400 0.0222  -0.0068 -0.0275 144 TYR   A CD1 
2182 C  CD2 . TYR   A 144 ? 0.2877 0.2299 0.3656 0.0224  -0.0202 -0.0147 144 TYR   A CD2 
2183 C  CE1 . TYR   A 144 ? 0.3061 0.2589 0.3835 0.0245  -0.0127 -0.0342 144 TYR   A CE1 
2184 C  CE2 . TYR   A 144 ? 0.3081 0.2433 0.3970 0.0244  -0.0268 -0.0203 144 TYR   A CE2 
2185 C  CZ  . TYR   A 144 ? 0.3024 0.2432 0.3917 0.0258  -0.0229 -0.0307 144 TYR   A CZ  
2186 O  OH  . TYR   A 144 ? 0.3587 0.2921 0.4603 0.0280  -0.0301 -0.0374 144 TYR   A OH  
2196 N  N   . TRP   A 145 ? 0.2109 0.1571 0.2569 0.0111  -0.0123 0.0120  145 TRP   A N   
2197 C  CA  . TRP   A 145 ? 0.2101 0.1490 0.2580 0.0074  -0.0201 0.0209  145 TRP   A CA  
2198 C  C   . TRP   A 145 ? 0.2531 0.1848 0.3150 0.0111  -0.0289 0.0188  145 TRP   A C   
2199 O  O   . TRP   A 145 ? 0.2336 0.1697 0.3016 0.0156  -0.0281 0.0130  145 TRP   A O   
2200 C  CB  . TRP   A 145 ? 0.2184 0.1620 0.2566 0.0032  -0.0182 0.0292  145 TRP   A CB  
2201 C  CG  . TRP   A 145 ? 0.2092 0.1474 0.2486 -0.0009 -0.0265 0.0385  145 TRP   A CG  
2202 C  CD1 . TRP   A 145 ? 0.2439 0.1810 0.2868 0.0002  -0.0314 0.0412  145 TRP   A CD1 
2203 C  CD2 . TRP   A 145 ? 0.2781 0.2119 0.3139 -0.0080 -0.0312 0.0472  145 TRP   A CD2 
2204 N  NE1 . TRP   A 145 ? 0.2667 0.1978 0.3074 -0.0058 -0.0397 0.0519  145 TRP   A NE1 
2205 C  CE2 . TRP   A 145 ? 0.2452 0.1743 0.2812 -0.0115 -0.0394 0.0560  145 TRP   A CE2 
2206 C  CE3 . TRP   A 145 ? 0.2687 0.2026 0.3011 -0.0124 -0.0296 0.0486  145 TRP   A CE3 
2207 C  CZ2 . TRP   A 145 ? 0.3089 0.2329 0.3403 -0.0204 -0.0458 0.0671  145 TRP   A CZ2 
2208 C  CZ3 . TRP   A 145 ? 0.2639 0.1940 0.2933 -0.0211 -0.0353 0.0585  145 TRP   A CZ3 
2209 C  CH2 . TRP   A 145 ? 0.3013 0.2263 0.3296 -0.0256 -0.0432 0.0681  145 TRP   A CH2 
2220 N  N   . ASP   A 146 ? 0.2520 0.1726 0.3199 0.0092  -0.0381 0.0231  146 ASP   A N   
2221 C  CA  . ASP   A 146 ? 0.2783 0.1896 0.3623 0.0139  -0.0486 0.0198  146 ASP   A CA  
2222 C  C   . ASP   A 146 ? 0.3191 0.2183 0.4034 0.0090  -0.0602 0.0329  146 ASP   A C   
2223 O  O   . ASP   A 146 ? 0.3200 0.2071 0.4178 0.0122  -0.0719 0.0322  146 ASP   A O   
2224 C  CB  . ASP   A 146 ? 0.3281 0.2347 0.4227 0.0175  -0.0508 0.0096  146 ASP   A CB  
2225 C  CG  . ASP   A 146 ? 0.2996 0.1954 0.3918 0.0112  -0.0561 0.0170  146 ASP   A CG  
2226 O  OD1 . ASP   A 146 ? 0.3146 0.2105 0.3944 0.0033  -0.0551 0.0291  146 ASP   A OD1 
2227 O  OD2 . ASP   A 146 ? 0.3640 0.2532 0.4664 0.0136  -0.0604 0.0095  146 ASP   A OD2 
2232 N  N   . GLY   A 147 ? 0.2707 0.1734 0.3405 0.0011  -0.0578 0.0445  147 GLY   A N   
2233 C  CA  . GLY   A 147 ? 0.3127 0.2061 0.3791 -0.0059 -0.0680 0.0583  147 GLY   A CA  
2234 C  C   . GLY   A 147 ? 0.3499 0.2373 0.4099 -0.0155 -0.0703 0.0669  147 GLY   A C   
2235 O  O   . GLY   A 147 ? 0.3472 0.2348 0.3984 -0.0242 -0.0746 0.0779  147 GLY   A O   
2239 N  N   . LYS   A 148 ? 0.3302 0.2180 0.3929 -0.0146 -0.0658 0.0598  148 LYS   A N   
2240 C  CA  . LYS   A 148 ? 0.3736 0.2573 0.4315 -0.0242 -0.0677 0.0670  148 LYS   A CA  
2241 C  C   . LYS   A 148 ? 0.3010 0.1956 0.3544 -0.0245 -0.0571 0.0599  148 LYS   A C   
2242 O  O   . LYS   A 148 ? 0.3443 0.2401 0.3925 -0.0334 -0.0568 0.0656  148 LYS   A O   
2243 C  CB  . LYS   A 148 ? 0.3516 0.2224 0.4205 -0.0237 -0.0785 0.0654  148 LYS   A CB  
2244 C  CG  . LYS   A 148 ? 0.3896 0.2555 0.4729 -0.0144 -0.0787 0.0509  148 LYS   A CG  
2245 C  CD  . LYS   A 148 ? 0.4794 0.3343 0.5754 -0.0124 -0.0904 0.0479  148 LYS   A CD  
2246 C  CE  . LYS   A 148 ? 0.6485 0.4991 0.7519 -0.0118 -0.0906 0.0395  148 LYS   A CE  
2247 N  NZ  . LYS   A 148 ? 0.7181 0.5576 0.8333 -0.0112 -0.1026 0.0378  148 LYS   A NZ  
2261 N  N   . GLN   A 149 ? 0.2737 0.1770 0.3284 -0.0161 -0.0487 0.0481  149 GLN   A N   
2262 C  CA  . GLN   A 149 ? 0.2823 0.1941 0.3334 -0.0156 -0.0407 0.0413  149 GLN   A CA  
2263 C  C   . GLN   A 149 ? 0.2593 0.1813 0.3074 -0.0079 -0.0318 0.0323  149 GLN   A C   
2264 O  O   . GLN   A 149 ? 0.2553 0.1774 0.3064 -0.0030 -0.0318 0.0298  149 GLN   A O   
2265 C  CB  . GLN   A 149 ? 0.3336 0.2360 0.3949 -0.0146 -0.0460 0.0354  149 GLN   A CB  
2266 C  CG  . GLN   A 149 ? 0.3044 0.2016 0.3782 -0.0051 -0.0489 0.0240  149 GLN   A CG  
2267 C  CD  . GLN   A 149 ? 0.3616 0.2438 0.4489 -0.0052 -0.0596 0.0214  149 GLN   A CD  
2268 O  OE1 . GLN   A 149 ? 0.3703 0.2477 0.4567 -0.0122 -0.0625 0.0257  149 GLN   A OE1 
2269 N  NE2 . GLN   A 149 ? 0.3569 0.2326 0.4583 0.0027  -0.0656 0.0129  149 GLN   A NE2 
2278 N  N   . MET   A 150 ? 0.2472 0.1776 0.2892 -0.0077 -0.0248 0.0280  150 MET   A N   
2279 C  CA  . MET   A 150 ? 0.2358 0.1751 0.2720 -0.0026 -0.0167 0.0217  150 MET   A CA  
2280 C  C   . MET   A 150 ? 0.2425 0.1821 0.2818 0.0012  -0.0153 0.0120  150 MET   A C   
2281 O  O   . MET   A 150 ? 0.2412 0.1801 0.2811 -0.0013 -0.0169 0.0112  150 MET   A O   
2282 C  CB  . MET   A 150 ? 0.2495 0.1983 0.2753 -0.0058 -0.0112 0.0256  150 MET   A CB  
2283 C  CG  . MET   A 150 ? 0.2370 0.1891 0.2585 -0.0089 -0.0110 0.0326  150 MET   A CG  
2284 S  SD  . MET   A 150 ? 0.2575 0.2066 0.2795 -0.0185 -0.0177 0.0435  150 MET   A SD  
2285 C  CE  . MET   A 150 ? 0.2684 0.2234 0.2890 -0.0241 -0.0162 0.0432  150 MET   A CE  
2295 N  N   . THR   A 151 ? 0.2154 0.1574 0.2563 0.0065  -0.0122 0.0044  151 THR   A N   
2296 C  CA  . THR   A 151 ? 0.2111 0.1553 0.2550 0.0096  -0.0110 -0.0060 151 THR   A CA  
2297 C  C   . THR   A 151 ? 0.2046 0.1576 0.2379 0.0111  -0.0033 -0.0093 151 THR   A C   
2298 O  O   . THR   A 151 ? 0.2375 0.1933 0.2677 0.0119  0.0001  -0.0078 151 THR   A O   
2299 C  CB  . THR   A 151 ? 0.2559 0.1958 0.3139 0.0136  -0.0158 -0.0137 151 THR   A CB  
2300 O  OG1 . THR   A 151 ? 0.2599 0.1883 0.3271 0.0116  -0.0249 -0.0085 151 THR   A OG1 
2301 C  CG2 . THR   A 151 ? 0.2527 0.1971 0.3146 0.0165  -0.0145 -0.0264 151 THR   A CG2 
2309 N  N   . PHE   A 152 ? 0.2160 0.1728 0.2435 0.0109  -0.0014 -0.0132 152 PHE   A N   
2310 C  CA  . PHE   A 152 ? 0.2201 0.1831 0.2350 0.0108  0.0042  -0.0135 152 PHE   A CA  
2311 C  C   . PHE   A 152 ? 0.2410 0.2095 0.2540 0.0116  0.0058  -0.0230 152 PHE   A C   
2312 O  O   . PHE   A 152 ? 0.2243 0.1925 0.2407 0.0115  0.0027  -0.0273 152 PHE   A O   
2313 C  CB  . PHE   A 152 ? 0.2215 0.1848 0.2285 0.0092  0.0038  -0.0071 152 PHE   A CB  
2314 C  CG  . PHE   A 152 ? 0.2046 0.1658 0.2134 0.0074  0.0025  0.0007  152 PHE   A CG  
2315 C  CD1 . PHE   A 152 ? 0.2243 0.1867 0.2278 0.0077  0.0054  0.0050  152 PHE   A CD1 
2316 C  CD2 . PHE   A 152 ? 0.2218 0.1805 0.2375 0.0046  -0.0017 0.0033  152 PHE   A CD2 
2317 C  CE1 . PHE   A 152 ? 0.2429 0.2060 0.2476 0.0057  0.0045  0.0108  152 PHE   A CE1 
2318 C  CE2 . PHE   A 152 ? 0.2305 0.1899 0.2463 0.0014  -0.0025 0.0105  152 PHE   A CE2 
2319 C  CZ  . PHE   A 152 ? 0.2183 0.1809 0.2286 0.0022  0.0009  0.0136  152 PHE   A CZ  
2329 N  N   . GLY   A 153 ? 0.2185 0.1931 0.2254 0.0114  0.0108  -0.0264 153 GLY   A N   
2330 C  CA  . GLY   A 153 ? 0.2390 0.2218 0.2411 0.0106  0.0133  -0.0352 153 GLY   A CA  
2331 C  C   . GLY   A 153 ? 0.2305 0.2145 0.2176 0.0084  0.0135  -0.0311 153 GLY   A C   
2332 O  O   . GLY   A 153 ? 0.2369 0.2157 0.2180 0.0082  0.0121  -0.0221 153 GLY   A O   
2336 N  N   . ASP   A 154 ? 0.2645 0.2563 0.2461 0.0070  0.0147  -0.0388 154 ASP   A N   
2337 C  CA  . ASP   A 154 ? 0.2765 0.2700 0.2425 0.0047  0.0139  -0.0350 154 ASP   A CA  
2338 C  C   . ASP   A 154 ? 0.2711 0.2683 0.2213 0.0005  0.0183  -0.0312 154 ASP   A C   
2339 O  O   . ASP   A 154 ? 0.2789 0.2769 0.2144 -0.0021 0.0168  -0.0272 154 ASP   A O   
2340 C  CB  . ASP   A 154 ? 0.2870 0.2873 0.2528 0.0044  0.0119  -0.0443 154 ASP   A CB  
2341 C  CG  . ASP   A 154 ? 0.2883 0.2830 0.2629 0.0067  0.0060  -0.0436 154 ASP   A CG  
2342 O  OD1 . ASP   A 154 ? 0.2748 0.2633 0.2482 0.0074  0.0036  -0.0344 154 ASP   A OD1 
2343 O  OD2 . ASP   A 154 ? 0.3672 0.3655 0.3484 0.0071  0.0036  -0.0529 154 ASP   A OD2 
2348 N  N   . GLY   A 155 ? 0.2523 0.2513 0.2054 -0.0008 0.0229  -0.0315 155 GLY   A N   
2349 C  CA  . GLY   A 155 ? 0.2658 0.2683 0.2045 -0.0066 0.0274  -0.0273 155 GLY   A CA  
2350 C  C   . GLY   A 155 ? 0.3136 0.3299 0.2431 -0.0117 0.0309  -0.0355 155 GLY   A C   
2351 O  O   . GLY   A 155 ? 0.2986 0.3220 0.2360 -0.0094 0.0302  -0.0463 155 GLY   A O   
2355 N  N   . ASP   A 156 ? 0.2778 0.2982 0.1909 -0.0192 0.0346  -0.0309 156 ASP   A N   
2356 C  CA  . ASP   A 156 ? 0.3223 0.3587 0.2231 -0.0264 0.0388  -0.0381 156 ASP   A CA  
2357 C  C   . ASP   A 156 ? 0.3791 0.4115 0.2558 -0.0351 0.0382  -0.0255 156 ASP   A C   
2358 O  O   . ASP   A 156 ? 0.3595 0.3803 0.2270 -0.0334 0.0310  -0.0163 156 ASP   A O   
2359 C  CB  . ASP   A 156 ? 0.3586 0.4118 0.2708 -0.0280 0.0463  -0.0518 156 ASP   A CB  
2360 C  CG  . ASP   A 156 ? 0.3807 0.4552 0.2841 -0.0348 0.0514  -0.0634 156 ASP   A CG  
2361 O  OD1 . ASP   A 156 ? 0.4621 0.5375 0.3488 -0.0385 0.0487  -0.0601 156 ASP   A OD1 
2362 O  OD2 . ASP   A 156 ? 0.4672 0.5586 0.3806 -0.0363 0.0579  -0.0764 156 ASP   A OD2 
2367 N  N   . THR   A 157 ? 0.3674 0.4083 0.2346 -0.0443 0.0445  -0.0245 157 THR   A N   
2368 C  CA  . THR   A 157 ? 0.4001 0.4367 0.2426 -0.0548 0.0433  -0.0117 157 THR   A CA  
2369 C  C   . THR   A 157 ? 0.3696 0.3866 0.2111 -0.0541 0.0397  0.0022  157 THR   A C   
2370 O  O   . THR   A 157 ? 0.4596 0.4649 0.2829 -0.0595 0.0343  0.0153  157 THR   A O   
2371 C  CB  . THR   A 157 ? 0.4019 0.4594 0.2340 -0.0672 0.0525  -0.0176 157 THR   A CB  
2372 O  OG1 . THR   A 157 ? 0.4744 0.5334 0.3180 -0.0682 0.0581  -0.0189 157 THR   A OG1 
2373 C  CG2 . THR   A 157 ? 0.4623 0.5427 0.3010 -0.0664 0.0574  -0.0359 157 THR   A CG2 
2381 N  N   . MET   A 158 ? 0.3323 0.3448 0.1924 -0.0477 0.0414  -0.0003 158 MET   A N   
2382 C  CA  . MET   A 158 ? 0.3523 0.3486 0.2125 -0.0475 0.0387  0.0107  158 MET   A CA  
2383 C  C   . MET   A 158 ? 0.3386 0.3190 0.2086 -0.0367 0.0310  0.0150  158 MET   A C   
2384 O  O   . MET   A 158 ? 0.3343 0.2996 0.2004 -0.0362 0.0262  0.0249  158 MET   A O   
2385 C  CB  . MET   A 158 ? 0.4297 0.4333 0.3029 -0.0488 0.0457  0.0051  158 MET   A CB  
2386 C  CG  . MET   A 158 ? 0.5334 0.5552 0.3996 -0.0602 0.0543  -0.0002 158 MET   A CG  
2387 S  SD  . MET   A 158 ? 0.5858 0.5984 0.4284 -0.0748 0.0540  0.0153  158 MET   A SD  
2388 C  CE  . MET   A 158 ? 0.5289 0.5405 0.3876 -0.0746 0.0584  0.0139  158 MET   A CE  
2398 N  N   . MET   A 159 ? 0.3229 0.3073 0.2060 -0.0285 0.0297  0.0072  159 MET   A N   
2399 C  CA  . MET   A 159 ? 0.2900 0.2637 0.1842 -0.0194 0.0240  0.0097  159 MET   A CA  
2400 C  C   . MET   A 159 ? 0.2748 0.2508 0.1706 -0.0149 0.0196  0.0059  159 MET   A C   
2401 O  O   . MET   A 159 ? 0.2920 0.2795 0.1892 -0.0160 0.0223  -0.0030 159 MET   A O   
2402 C  CB  . MET   A 159 ? 0.2887 0.2647 0.2016 -0.0147 0.0272  0.0041  159 MET   A CB  
2403 C  CG  . MET   A 159 ? 0.3305 0.3052 0.2444 -0.0184 0.0312  0.0067  159 MET   A CG  
2404 S  SD  . MET   A 159 ? 0.3450 0.3237 0.2800 -0.0130 0.0337  0.0002  159 MET   A SD  
2405 C  CE  . MET   A 159 ? 0.3518 0.3371 0.2844 -0.0206 0.0403  -0.0006 159 MET   A CE  
2415 N  N   . TYR   A 160 ? 0.2869 0.2530 0.1839 -0.0097 0.0128  0.0114  160 TYR   A N   
2416 C  CA  . TYR   A 160 ? 0.3060 0.2744 0.2088 -0.0046 0.0083  0.0076  160 TYR   A CA  
2417 C  C   . TYR   A 160 ? 0.2666 0.2386 0.1879 -0.0005 0.0109  0.0008  160 TYR   A C   
2418 O  O   . TYR   A 160 ? 0.2682 0.2395 0.1970 -0.0005 0.0148  0.0005  160 TYR   A O   
2419 C  CB  . TYR   A 160 ? 0.2848 0.2437 0.1863 0.0000  0.0005  0.0144  160 TYR   A CB  
2420 C  CG  . TYR   A 160 ? 0.2924 0.2453 0.1761 -0.0033 -0.0051 0.0218  160 TYR   A CG  
2421 C  CD1 . TYR   A 160 ? 0.3319 0.2896 0.2061 -0.0047 -0.0090 0.0206  160 TYR   A CD1 
2422 C  CD2 . TYR   A 160 ? 0.3041 0.2453 0.1803 -0.0053 -0.0074 0.0305  160 TYR   A CD2 
2423 C  CE1 . TYR   A 160 ? 0.3730 0.3243 0.2292 -0.0084 -0.0153 0.0289  160 TYR   A CE1 
2424 C  CE2 . TYR   A 160 ? 0.3195 0.2524 0.1788 -0.0090 -0.0142 0.0389  160 TYR   A CE2 
2425 C  CZ  . TYR   A 160 ? 0.3560 0.2941 0.2048 -0.0106 -0.0183 0.0386  160 TYR   A CZ  
2426 O  OH  . TYR   A 160 ? 0.4100 0.3392 0.2404 -0.0149 -0.0262 0.0483  160 TYR   A OH  
2436 N  N   . PRO   A 161 ? 0.2534 0.2287 0.1825 0.0027  0.0080  -0.0040 161 PRO   A N   
2437 C  CA  . PRO   A 161 ? 0.2841 0.2599 0.2299 0.0056  0.0088  -0.0080 161 PRO   A CA  
2438 C  C   . PRO   A 161 ? 0.2527 0.2224 0.2041 0.0076  0.0086  -0.0019 161 PRO   A C   
2439 O  O   . PRO   A 161 ? 0.2561 0.2215 0.2035 0.0092  0.0056  0.0035  161 PRO   A O   
2440 C  CB  . PRO   A 161 ? 0.2415 0.2197 0.1917 0.0075  0.0042  -0.0113 161 PRO   A CB  
2441 C  CG  . PRO   A 161 ? 0.2560 0.2394 0.1934 0.0051  0.0033  -0.0142 161 PRO   A CG  
2442 C  CD  . PRO   A 161 ? 0.2554 0.2346 0.1779 0.0026  0.0038  -0.0063 161 PRO   A CD  
2450 N  N   . LEU   A 162 ? 0.2306 0.2004 0.1917 0.0077  0.0115  -0.0037 162 LEU   A N   
2451 C  CA  . LEU   A 162 ? 0.2276 0.1933 0.1924 0.0085  0.0123  0.0014  162 LEU   A CA  
2452 C  C   . LEU   A 162 ? 0.2587 0.2242 0.2326 0.0103  0.0094  0.0030  162 LEU   A C   
2453 O  O   . LEU   A 162 ? 0.3019 0.2670 0.2842 0.0100  0.0097  0.0036  162 LEU   A O   
2454 C  CB  . LEU   A 162 ? 0.2429 0.2102 0.2128 0.0073  0.0162  -0.0011 162 LEU   A CB  
2455 C  CG  . LEU   A 162 ? 0.2503 0.2203 0.2118 0.0039  0.0205  -0.0023 162 LEU   A CG  
2456 C  CD1 . LEU   A 162 ? 0.2589 0.2370 0.2202 0.0024  0.0224  -0.0106 162 LEU   A CD1 
2457 C  CD2 . LEU   A 162 ? 0.3086 0.2789 0.2756 0.0032  0.0235  -0.0017 162 LEU   A CD2 
2469 N  N   . VAL   A 163 ? 0.2431 0.2097 0.2150 0.0115  0.0060  0.0038  163 VAL   A N   
2470 C  CA  . VAL   A 163 ? 0.2635 0.2331 0.2431 0.0119  0.0038  0.0048  163 VAL   A CA  
2471 C  C   . VAL   A 163 ? 0.2990 0.2691 0.2751 0.0144  0.0020  0.0073  163 VAL   A C   
2472 O  O   . VAL   A 163 ? 0.3005 0.2706 0.2713 0.0164  -0.0013 0.0068  163 VAL   A O   
2473 C  CB  . VAL   A 163 ? 0.2553 0.2284 0.2393 0.0110  0.0010  0.0011  163 VAL   A CB  
2474 C  CG1 . VAL   A 163 ? 0.2951 0.2729 0.2868 0.0094  -0.0007 0.0026  163 VAL   A CG1 
2475 C  CG2 . VAL   A 163 ? 0.3265 0.2978 0.3154 0.0094  0.0016  -0.0030 163 VAL   A CG2 
2485 N  N   . SER   A 164 ? 0.2831 0.2536 0.2622 0.0147  0.0034  0.0094  164 SER   A N   
2486 C  CA  . SER   A 164 ? 0.2520 0.2245 0.2313 0.0178  0.0013  0.0096  164 SER   A CA  
2487 C  C   . SER   A 164 ? 0.2395 0.2184 0.2257 0.0162  0.0034  0.0097  164 SER   A C   
2488 O  O   . SER   A 164 ? 0.2445 0.2235 0.2332 0.0127  0.0057  0.0114  164 SER   A O   
2489 C  CB  . SER   A 164 ? 0.2543 0.2182 0.2258 0.0198  0.0005  0.0118  164 SER   A CB  
2490 O  OG  . SER   A 164 ? 0.2602 0.2209 0.2312 0.0175  0.0045  0.0136  164 SER   A OG  
2496 N  N   . LEU   A 165 ? 0.2277 0.2124 0.2172 0.0189  0.0019  0.0073  165 LEU   A N   
2497 C  CA  . LEU   A 165 ? 0.2313 0.2246 0.2259 0.0168  0.0044  0.0065  165 LEU   A CA  
2498 C  C   . LEU   A 165 ? 0.2127 0.1998 0.2042 0.0153  0.0071  0.0094  165 LEU   A C   
2499 O  O   . LEU   A 165 ? 0.2307 0.2221 0.2243 0.0112  0.0093  0.0113  165 LEU   A O   
2500 C  CB  . LEU   A 165 ? 0.2407 0.2423 0.2402 0.0210  0.0025  0.0011  165 LEU   A CB  
2501 C  CG  . LEU   A 165 ? 0.2880 0.3013 0.2939 0.0222  0.0000  -0.0036 165 LEU   A CG  
2502 C  CD1 . LEU   A 165 ? 0.3243 0.3468 0.3372 0.0277  -0.0020 -0.0109 165 LEU   A CD1 
2503 C  CD2 . LEU   A 165 ? 0.3752 0.3998 0.3849 0.0149  0.0030  -0.0026 165 LEU   A CD2 
2515 N  N   . GLY   A 166 ? 0.2191 0.1963 0.2055 0.0181  0.0065  0.0101  166 GLY   A N   
2516 C  CA  . GLY   A 166 ? 0.2409 0.2134 0.2253 0.0166  0.0090  0.0120  166 GLY   A CA  
2517 C  C   . GLY   A 166 ? 0.2366 0.2067 0.2206 0.0130  0.0113  0.0147  166 GLY   A C   
2518 O  O   . GLY   A 166 ? 0.2390 0.2114 0.2255 0.0107  0.0128  0.0160  166 GLY   A O   
2522 N  N   . VAL   A 167 ? 0.2190 0.1852 0.2004 0.0129  0.0109  0.0149  167 VAL   A N   
2523 C  CA  . VAL   A 167 ? 0.2346 0.1995 0.2181 0.0106  0.0123  0.0153  167 VAL   A CA  
2524 C  C   . VAL   A 167 ? 0.2205 0.1897 0.2108 0.0083  0.0110  0.0164  167 VAL   A C   
2525 O  O   . VAL   A 167 ? 0.2172 0.1856 0.2112 0.0066  0.0110  0.0178  167 VAL   A O   
2526 C  CB  . VAL   A 167 ? 0.2278 0.1898 0.2075 0.0108  0.0124  0.0133  167 VAL   A CB  
2527 C  CG1 . VAL   A 167 ? 0.2416 0.2042 0.2271 0.0094  0.0132  0.0111  167 VAL   A CG1 
2528 C  CG2 . VAL   A 167 ? 0.2667 0.2240 0.2377 0.0107  0.0136  0.0141  167 VAL   A CG2 
2538 N  N   . GLY   A 168 ? 0.2159 0.1899 0.2080 0.0077  0.0093  0.0160  168 GLY   A N   
2539 C  CA  . GLY   A 168 ? 0.2009 0.1788 0.1981 0.0034  0.0078  0.0184  168 GLY   A CA  
2540 C  C   . GLY   A 168 ? 0.2115 0.1944 0.2090 0.0007  0.0086  0.0213  168 GLY   A C   
2541 O  O   . GLY   A 168 ? 0.2082 0.1899 0.2081 -0.0031 0.0069  0.0253  168 GLY   A O   
2545 N  N   . GLY   A 169 ? 0.1876 0.1757 0.1828 0.0027  0.0105  0.0192  169 GLY   A N   
2546 C  CA  . GLY   A 169 ? 0.1915 0.1863 0.1864 0.0000  0.0116  0.0205  169 GLY   A CA  
2547 C  C   . GLY   A 169 ? 0.1869 0.1754 0.1811 -0.0003 0.0116  0.0231  169 GLY   A C   
2548 O  O   . GLY   A 169 ? 0.1972 0.1892 0.1916 -0.0043 0.0106  0.0267  169 GLY   A O   
2552 N  N   . HIS   A 170 ? 0.1660 0.1463 0.1592 0.0034  0.0124  0.0214  170 HIS   A N   
2553 C  CA  . HIS   A 170 ? 0.1774 0.1534 0.1717 0.0034  0.0126  0.0224  170 HIS   A CA  
2554 C  C   . HIS   A 170 ? 0.1898 0.1633 0.1890 0.0013  0.0093  0.0254  170 HIS   A C   
2555 O  O   . HIS   A 170 ? 0.1998 0.1740 0.2010 -0.0006 0.0072  0.0283  170 HIS   A O   
2556 C  CB  . HIS   A 170 ? 0.1975 0.1675 0.1896 0.0062  0.0146  0.0195  170 HIS   A CB  
2557 C  CG  . HIS   A 170 ? 0.1841 0.1522 0.1783 0.0059  0.0156  0.0189  170 HIS   A CG  
2558 N  ND1 . HIS   A 170 ? 0.1786 0.1462 0.1707 0.0058  0.0177  0.0179  170 HIS   A ND1 
2559 C  CD2 . HIS   A 170 ? 0.1794 0.1469 0.1796 0.0058  0.0142  0.0185  170 HIS   A CD2 
2560 C  CE1 . HIS   A 170 ? 0.1656 0.1336 0.1616 0.0051  0.0183  0.0168  170 HIS   A CE1 
2561 N  NE2 . HIS   A 170 ? 0.2022 0.1706 0.2037 0.0057  0.0160  0.0167  170 HIS   A NE2 
2569 N  N   . GLU   A 171 ? 0.1968 0.1668 0.1984 0.0016  0.0077  0.0246  171 GLU   A N   
2570 C  CA  . GLU   A 171 ? 0.1880 0.1531 0.1962 0.0006  0.0033  0.0263  171 GLU   A CA  
2571 C  C   . GLU   A 171 ? 0.2003 0.1668 0.2089 -0.0049 -0.0008 0.0330  171 GLU   A C   
2572 O  O   . GLU   A 171 ? 0.2198 0.1824 0.2321 -0.0064 -0.0054 0.0369  171 GLU   A O   
2573 C  CB  . GLU   A 171 ? 0.2205 0.1816 0.2317 0.0024  0.0025  0.0223  171 GLU   A CB  
2574 C  CG  . GLU   A 171 ? 0.2195 0.1803 0.2292 0.0061  0.0062  0.0161  171 GLU   A CG  
2575 C  CD  . GLU   A 171 ? 0.2169 0.1774 0.2315 0.0078  0.0066  0.0136  171 GLU   A CD  
2576 O  OE1 . GLU   A 171 ? 0.2268 0.1855 0.2478 0.0075  0.0024  0.0160  171 GLU   A OE1 
2577 O  OE2 . GLU   A 171 ? 0.2278 0.1906 0.2396 0.0090  0.0108  0.0093  171 GLU   A OE2 
2584 N  N   . VAL   A 172 ? 0.1952 0.1681 0.2003 -0.0085 0.0004  0.0345  172 VAL   A N   
2585 C  CA  . VAL   A 172 ? 0.1964 0.1732 0.2001 -0.0160 -0.0026 0.0414  172 VAL   A CA  
2586 C  C   . VAL   A 172 ? 0.2084 0.1893 0.2085 -0.0180 -0.0029 0.0448  172 VAL   A C   
2587 O  O   . VAL   A 172 ? 0.2181 0.1971 0.2176 -0.0234 -0.0079 0.0520  172 VAL   A O   
2588 C  CB  . VAL   A 172 ? 0.1939 0.1816 0.1947 -0.0199 0.0002  0.0405  172 VAL   A CB  
2589 C  CG1 . VAL   A 172 ? 0.2520 0.2478 0.2493 -0.0296 -0.0015 0.0476  172 VAL   A CG1 
2590 C  CG2 . VAL   A 172 ? 0.2426 0.2263 0.2474 -0.0191 -0.0010 0.0380  172 VAL   A CG2 
2600 N  N   . SER   A 173 ? 0.1895 0.1756 0.1869 -0.0141 0.0017  0.0401  173 SER   A N   
2601 C  CA  . SER   A 173 ? 0.1767 0.1687 0.1706 -0.0161 0.0018  0.0419  173 SER   A CA  
2602 C  C   . SER   A 173 ? 0.1963 0.1804 0.1938 -0.0141 -0.0022 0.0440  173 SER   A C   
2603 O  O   . SER   A 173 ? 0.2023 0.1906 0.1970 -0.0171 -0.0043 0.0474  173 SER   A O   
2604 C  CB  . SER   A 173 ? 0.1981 0.1975 0.1895 -0.0127 0.0073  0.0350  173 SER   A CB  
2605 O  OG  . SER   A 173 ? 0.2191 0.2280 0.2091 -0.0144 0.0098  0.0324  173 SER   A OG  
2611 N  N   . HIS   A 174 ? 0.2132 0.1879 0.2173 -0.0093 -0.0038 0.0414  174 HIS   A N   
2612 C  CA  . HIS   A 174 ? 0.2064 0.1751 0.2169 -0.0076 -0.0093 0.0430  174 HIS   A CA  
2613 C  C   . HIS   A 174 ? 0.2138 0.1783 0.2245 -0.0131 -0.0174 0.0520  174 HIS   A C   
2614 O  O   . HIS   A 174 ? 0.2233 0.1865 0.2350 -0.0143 -0.0232 0.0565  174 HIS   A O   
2615 C  CB  . HIS   A 174 ? 0.2111 0.1731 0.2301 -0.0018 -0.0093 0.0368  174 HIS   A CB  
2616 C  CG  . HIS   A 174 ? 0.1979 0.1633 0.2174 0.0022  -0.0036 0.0298  174 HIS   A CG  
2617 N  ND1 . HIS   A 174 ? 0.1881 0.1577 0.2074 0.0025  -0.0028 0.0291  174 HIS   A ND1 
2618 C  CD2 . HIS   A 174 ? 0.1866 0.1518 0.2058 0.0050  0.0014  0.0236  174 HIS   A CD2 
2619 C  CE1 . HIS   A 174 ? 0.2204 0.1918 0.2400 0.0048  0.0027  0.0230  174 HIS   A CE1 
2620 N  NE2 . HIS   A 174 ? 0.1809 0.1497 0.1998 0.0061  0.0052  0.0201  174 HIS   A NE2 
2628 N  N   . GLY   A 175 ? 0.2297 0.1919 0.2392 -0.0172 -0.0187 0.0552  175 GLY   A N   
2629 C  CA  . GLY   A 175 ? 0.2141 0.1717 0.2220 -0.0247 -0.0266 0.0653  175 GLY   A CA  
2630 C  C   . GLY   A 175 ? 0.2314 0.2002 0.2284 -0.0328 -0.0257 0.0718  175 GLY   A C   
2631 O  O   . GLY   A 175 ? 0.2490 0.2147 0.2433 -0.0380 -0.0332 0.0807  175 GLY   A O   
2635 N  N   . PHE   A 176 ? 0.2036 0.1863 0.1944 -0.0339 -0.0172 0.0671  176 PHE   A N   
2636 C  CA  . PHE   A 176 ? 0.2142 0.2111 0.1954 -0.0412 -0.0154 0.0705  176 PHE   A CA  
2637 C  C   . PHE   A 176 ? 0.2092 0.2059 0.1892 -0.0395 -0.0188 0.0720  176 PHE   A C   
2638 O  O   . PHE   A 176 ? 0.2197 0.2199 0.1928 -0.0470 -0.0239 0.0803  176 PHE   A O   
2639 C  CB  . PHE   A 176 ? 0.2366 0.2485 0.2150 -0.0399 -0.0061 0.0616  176 PHE   A CB  
2640 C  CG  . PHE   A 176 ? 0.2291 0.2594 0.1988 -0.0474 -0.0034 0.0623  176 PHE   A CG  
2641 C  CD1 . PHE   A 176 ? 0.2306 0.2677 0.1973 -0.0457 -0.0020 0.0589  176 PHE   A CD1 
2642 C  CD2 . PHE   A 176 ? 0.2430 0.2853 0.2075 -0.0573 -0.0020 0.0657  176 PHE   A CD2 
2643 C  CE1 . PHE   A 176 ? 0.2620 0.3181 0.2206 -0.0529 0.0007  0.0579  176 PHE   A CE1 
2644 C  CE2 . PHE   A 176 ? 0.2538 0.3163 0.2100 -0.0653 0.0012  0.0651  176 PHE   A CE2 
2645 C  CZ  . PHE   A 176 ? 0.2710 0.3405 0.2241 -0.0628 0.0025  0.0608  176 PHE   A CZ  
2655 N  N   . THR   A 177 ? 0.2079 0.2004 0.1942 -0.0304 -0.0166 0.0645  177 THR   A N   
2656 C  CA  . THR   A 177 ? 0.1990 0.1921 0.1860 -0.0284 -0.0199 0.0648  177 THR   A CA  
2657 C  C   . THR   A 177 ? 0.2293 0.2114 0.2203 -0.0296 -0.0311 0.0734  177 THR   A C   
2658 O  O   . THR   A 177 ? 0.2164 0.2016 0.2026 -0.0336 -0.0367 0.0794  177 THR   A O   
2659 C  CB  . THR   A 177 ? 0.2042 0.1956 0.1981 -0.0197 -0.0149 0.0549  177 THR   A CB  
2660 O  OG1 . THR   A 177 ? 0.2129 0.2131 0.2025 -0.0191 -0.0066 0.0483  177 THR   A OG1 
2661 C  CG2 . THR   A 177 ? 0.2002 0.1924 0.1972 -0.0175 -0.0186 0.0543  177 THR   A CG2 
2669 N  N   . GLU   A 178 ? 0.2387 0.2077 0.2388 -0.0260 -0.0353 0.0735  178 GLU   A N   
2670 C  CA  . GLU   A 178 ? 0.2504 0.2068 0.2573 -0.0255 -0.0475 0.0802  178 GLU   A CA  
2671 C  C   . GLU   A 178 ? 0.2785 0.2340 0.2749 -0.0366 -0.0551 0.0940  178 GLU   A C   
2672 O  O   . GLU   A 178 ? 0.3031 0.2525 0.2998 -0.0383 -0.0659 0.1018  178 GLU   A O   
2673 C  CB  . GLU   A 178 ? 0.2390 0.1827 0.2576 -0.0203 -0.0501 0.0764  178 GLU   A CB  
2674 C  CG  . GLU   A 178 ? 0.2872 0.2157 0.3162 -0.0183 -0.0638 0.0812  178 GLU   A CG  
2675 C  CD  . GLU   A 178 ? 0.3982 0.3168 0.4403 -0.0120 -0.0649 0.0737  178 GLU   A CD  
2676 O  OE1 . GLU   A 178 ? 0.3511 0.2743 0.4009 -0.0040 -0.0583 0.0616  178 GLU   A OE1 
2677 O  OE2 . GLU   A 178 ? 0.5432 0.4494 0.5878 -0.0157 -0.0730 0.0799  178 GLU   A OE2 
2684 N  N   . GLN   A 179 ? 0.2553 0.2174 0.2425 -0.0448 -0.0501 0.0973  179 GLN   A N   
2685 C  CA  . GLN   A 179 ? 0.2707 0.2332 0.2469 -0.0580 -0.0566 0.1111  179 GLN   A CA  
2686 C  C   . GLN   A 179 ? 0.2775 0.2586 0.2397 -0.0653 -0.0529 0.1134  179 GLN   A C   
2687 O  O   . GLN   A 179 ? 0.3191 0.3058 0.2732 -0.0752 -0.0561 0.1193  179 GLN   A O   
2688 C  CB  . GLN   A 179 ? 0.3048 0.2681 0.2804 -0.0629 -0.0522 0.1104  179 GLN   A CB  
2689 C  CG  . GLN   A 179 ? 0.3140 0.2589 0.3030 -0.0570 -0.0578 0.1083  179 GLN   A CG  
2690 C  CD  . GLN   A 179 ? 0.4116 0.3581 0.4020 -0.0588 -0.0513 0.1048  179 GLN   A CD  
2691 O  OE1 . GLN   A 179 ? 0.4251 0.3878 0.4079 -0.0634 -0.0420 0.1022  179 GLN   A OE1 
2692 N  NE2 . GLN   A 179 ? 0.3916 0.3234 0.3931 -0.0541 -0.0560 0.1019  179 GLN   A NE2 
2701 N  N   . HIS   A 180 ? 0.2566 0.2489 0.2192 -0.0590 -0.0452 0.1033  180 HIS   A N   
2702 C  CA  . HIS   A 180 ? 0.2719 0.2829 0.2227 -0.0649 -0.0417 0.1031  180 HIS   A CA  
2703 C  C   . HIS   A 180 ? 0.2314 0.2411 0.1855 -0.0586 -0.0461 0.1008  180 HIS   A C   
2704 O  O   . HIS   A 180 ? 0.2953 0.2970 0.2478 -0.0615 -0.0577 0.1110  180 HIS   A O   
2705 C  CB  . HIS   A 180 ? 0.2601 0.2884 0.2082 -0.0645 -0.0286 0.0918  180 HIS   A CB  
2706 C  CG  . HIS   A 180 ? 0.2677 0.3038 0.2102 -0.0737 -0.0252 0.0951  180 HIS   A CG  
2707 N  ND1 . HIS   A 180 ? 0.3019 0.3299 0.2517 -0.0709 -0.0230 0.0929  180 HIS   A ND1 
2708 C  CD2 . HIS   A 180 ? 0.3062 0.3592 0.2368 -0.0862 -0.0235 0.0995  180 HIS   A CD2 
2709 C  CE1 . HIS   A 180 ? 0.3284 0.3680 0.2715 -0.0815 -0.0202 0.0963  180 HIS   A CE1 
2710 N  NE2 . HIS   A 180 ? 0.3317 0.3869 0.2646 -0.0900 -0.0201 0.0985  180 HIS   A NE2 
2718 N  N   . SER   A 181 ? 0.2236 0.2401 0.1827 -0.0507 -0.0381 0.0883  181 SER   A N   
2719 C  CA  . SER   A 181 ? 0.2393 0.2567 0.2026 -0.0453 -0.0413 0.0847  181 SER   A CA  
2720 C  C   . SER   A 181 ? 0.2716 0.2720 0.2480 -0.0381 -0.0506 0.0870  181 SER   A C   
2721 O  O   . SER   A 181 ? 0.2657 0.2655 0.2442 -0.0368 -0.0586 0.0896  181 SER   A O   
2722 C  CB  . SER   A 181 ? 0.2265 0.2519 0.1938 -0.0389 -0.0311 0.0710  181 SER   A CB  
2723 O  OG  . SER   A 181 ? 0.2361 0.2519 0.2136 -0.0313 -0.0263 0.0645  181 SER   A OG  
2729 N  N   . GLY   A 182 ? 0.2357 0.2243 0.2217 -0.0330 -0.0497 0.0846  182 GLY   A N   
2730 C  CA  . GLY   A 182 ? 0.2469 0.2221 0.2477 -0.0250 -0.0573 0.0832  182 GLY   A CA  
2731 C  C   . GLY   A 182 ? 0.2440 0.2234 0.2552 -0.0163 -0.0531 0.0716  182 GLY   A C   
2732 O  O   . GLY   A 182 ? 0.2364 0.2100 0.2601 -0.0104 -0.0607 0.0698  182 GLY   A O   
2736 N  N   . LEU   A 183 ? 0.2182 0.2076 0.2255 -0.0157 -0.0417 0.0634  183 LEU   A N   
2737 C  CA  . LEU   A 183 ? 0.2136 0.2071 0.2294 -0.0096 -0.0369 0.0530  183 LEU   A CA  
2738 C  C   . LEU   A 183 ? 0.1951 0.1804 0.2261 -0.0023 -0.0394 0.0480  183 LEU   A C   
2739 O  O   . LEU   A 183 ? 0.2135 0.1925 0.2471 -0.0005 -0.0364 0.0461  183 LEU   A O   
2740 C  CB  . LEU   A 183 ? 0.2114 0.2108 0.2219 -0.0098 -0.0249 0.0457  183 LEU   A CB  
2741 C  CG  . LEU   A 183 ? 0.2146 0.2254 0.2140 -0.0149 -0.0211 0.0453  183 LEU   A CG  
2742 C  CD1 . LEU   A 183 ? 0.1988 0.2115 0.1947 -0.0142 -0.0113 0.0389  183 LEU   A CD1 
2743 C  CD2 . LEU   A 183 ? 0.2191 0.2373 0.2203 -0.0145 -0.0226 0.0415  183 LEU   A CD2 
2755 N  N   . GLU   A 184 ? 0.2043 0.1916 0.2462 0.0019  -0.0450 0.0445  184 GLU   A N   
2756 C  CA  . GLU   A 184 ? 0.2121 0.1948 0.2708 0.0092  -0.0483 0.0378  184 GLU   A CA  
2757 C  C   . GLU   A 184 ? 0.1870 0.1751 0.2494 0.0117  -0.0364 0.0267  184 GLU   A C   
2758 O  O   . GLU   A 184 ? 0.2010 0.1965 0.2573 0.0092  -0.0284 0.0234  184 GLU   A O   
2759 C  CB  . GLU   A 184 ? 0.2010 0.1867 0.2713 0.0131  -0.0583 0.0365  184 GLU   A CB  
2760 C  CG  . GLU   A 184 ? 0.2505 0.2268 0.3195 0.0115  -0.0733 0.0484  184 GLU   A CG  
2761 C  CD  . GLU   A 184 ? 0.3282 0.2906 0.4083 0.0158  -0.0816 0.0494  184 GLU   A CD  
2762 O  OE1 . GLU   A 184 ? 0.4113 0.3746 0.5059 0.0226  -0.0782 0.0379  184 GLU   A OE1 
2763 O  OE2 . GLU   A 184 ? 0.3840 0.3351 0.4583 0.0117  -0.0917 0.0615  184 GLU   A OE2 
2770 N  N   . TYR   A 185 ? 0.2237 0.2077 0.2961 0.0161  -0.0358 0.0210  185 TYR   A N   
2771 C  CA  . TYR   A 185 ? 0.1827 0.1704 0.2542 0.0165  -0.0245 0.0129  185 TYR   A CA  
2772 C  C   . TYR   A 185 ? 0.2065 0.2048 0.2894 0.0192  -0.0205 0.0018  185 TYR   A C   
2773 O  O   . TYR   A 185 ? 0.2128 0.2142 0.3048 0.0222  -0.0174 -0.0068 185 TYR   A O   
2774 C  CB  . TYR   A 185 ? 0.1976 0.1775 0.2716 0.0185  -0.0250 0.0119  185 TYR   A CB  
2775 C  CG  . TYR   A 185 ? 0.2107 0.1920 0.2766 0.0166  -0.0143 0.0083  185 TYR   A CG  
2776 C  CD1 . TYR   A 185 ? 0.1835 0.1638 0.2346 0.0120  -0.0089 0.0137  185 TYR   A CD1 
2777 C  CD2 . TYR   A 185 ? 0.2123 0.1966 0.2857 0.0195  -0.0104 -0.0010 185 TYR   A CD2 
2778 C  CE1 . TYR   A 185 ? 0.1990 0.1791 0.2431 0.0108  -0.0010 0.0110  185 TYR   A CE1 
2779 C  CE2 . TYR   A 185 ? 0.2153 0.2004 0.2797 0.0172  -0.0018 -0.0032 185 TYR   A CE2 
2780 C  CZ  . TYR   A 185 ? 0.2013 0.1832 0.2511 0.0131  0.0022  0.0035  185 TYR   A CZ  
2781 O  OH  . TYR   A 185 ? 0.2181 0.1997 0.2594 0.0112  0.0091  0.0019  185 TYR   A OH  
2791 N  N   . PHE   A 186 ? 0.1955 0.2012 0.2774 0.0171  -0.0198 0.0016  186 PHE   A N   
2792 C  CA  . PHE   A 186 ? 0.1773 0.1950 0.2684 0.0174  -0.0150 -0.0081 186 PHE   A CA  
2793 C  C   . PHE   A 186 ? 0.1876 0.2100 0.2716 0.0131  -0.0138 -0.0055 186 PHE   A C   
2794 O  O   . PHE   A 186 ? 0.1927 0.2108 0.2674 0.0113  -0.0184 0.0027  186 PHE   A O   
2795 C  CB  . PHE   A 186 ? 0.2019 0.2256 0.3131 0.0238  -0.0228 -0.0156 186 PHE   A CB  
2796 C  CG  . PHE   A 186 ? 0.2500 0.2677 0.3658 0.0271  -0.0368 -0.0086 186 PHE   A CG  
2797 C  CD1 . PHE   A 186 ? 0.3872 0.4091 0.4995 0.0249  -0.0411 -0.0042 186 PHE   A CD1 
2798 C  CD2 . PHE   A 186 ? 0.4069 0.4143 0.5299 0.0319  -0.0464 -0.0061 186 PHE   A CD2 
2799 C  CE1 . PHE   A 186 ? 0.4393 0.4557 0.5540 0.0270  -0.0548 0.0033  186 PHE   A CE1 
2800 C  CE2 . PHE   A 186 ? 0.4279 0.4279 0.5540 0.0339  -0.0607 0.0020  186 PHE   A CE2 
2801 C  CZ  . PHE   A 186 ? 0.3421 0.3468 0.4633 0.0313  -0.0649 0.0072  186 PHE   A CZ  
2811 N  N   . GLY   A 187 ? 0.1878 0.2200 0.2760 0.0107  -0.0073 -0.0130 187 GLY   A N   
2812 C  CA  . GLY   A 187 ? 0.1757 0.2129 0.2596 0.0067  -0.0063 -0.0125 187 GLY   A CA  
2813 C  C   . GLY   A 187 ? 0.1683 0.1980 0.2351 0.0024  -0.0026 -0.0060 187 GLY   A C   
2814 O  O   . GLY   A 187 ? 0.2027 0.2249 0.2610 0.0013  0.0025  -0.0039 187 GLY   A O   
2818 N  N   . GLN   A 188 ? 0.1822 0.2151 0.2446 0.0001  -0.0056 -0.0040 188 GLN   A N   
2819 C  CA  . GLN   A 188 ? 0.1789 0.2075 0.2274 -0.0035 -0.0023 -0.0006 188 GLN   A CA  
2820 C  C   . GLN   A 188 ? 0.1816 0.2036 0.2212 -0.0026 -0.0051 0.0070  188 GLN   A C   
2821 O  O   . GLN   A 188 ? 0.1859 0.2029 0.2167 -0.0040 -0.0002 0.0082  188 GLN   A O   
2822 C  CB  . GLN   A 188 ? 0.1921 0.2283 0.2393 -0.0062 -0.0049 -0.0023 188 GLN   A CB  
2823 C  CG  . GLN   A 188 ? 0.1799 0.2224 0.2347 -0.0088 -0.0011 -0.0100 188 GLN   A CG  
2824 C  CD  . GLN   A 188 ? 0.1980 0.2490 0.2528 -0.0109 -0.0055 -0.0120 188 GLN   A CD  
2825 O  OE1 . GLN   A 188 ? 0.2135 0.2638 0.2588 -0.0133 -0.0047 -0.0115 188 GLN   A OE1 
2826 N  NE2 . GLN   A 188 ? 0.2663 0.3270 0.3330 -0.0100 -0.0097 -0.0160 188 GLN   A NE2 
2835 N  N   . SER   A 189 ? 0.1965 0.2185 0.2386 -0.0008 -0.0136 0.0123  189 SER   A N   
2836 C  CA  . SER   A 189 ? 0.1921 0.2080 0.2257 -0.0016 -0.0162 0.0202  189 SER   A CA  
2837 C  C   . SER   A 189 ? 0.1690 0.1771 0.2031 0.0003  -0.0115 0.0195  189 SER   A C   
2838 O  O   . SER   A 189 ? 0.1802 0.1845 0.2055 -0.0015 -0.0094 0.0234  189 SER   A O   
2839 C  CB  . SER   A 189 ? 0.2027 0.2173 0.2396 -0.0007 -0.0276 0.0272  189 SER   A CB  
2840 O  OG  . SER   A 189 ? 0.2064 0.2180 0.2580 0.0047  -0.0320 0.0239  189 SER   A OG  
2846 N  N   . GLY   A 190 ? 0.1890 0.1965 0.2335 0.0037  -0.0096 0.0138  190 GLY   A N   
2847 C  CA  . GLY   A 190 ? 0.1802 0.1817 0.2246 0.0052  -0.0052 0.0123  190 GLY   A CA  
2848 C  C   . GLY   A 190 ? 0.1672 0.1671 0.2025 0.0025  0.0035  0.0104  190 GLY   A C   
2849 O  O   . GLY   A 190 ? 0.1679 0.1622 0.1974 0.0026  0.0059  0.0124  190 GLY   A O   
2853 N  N   . GLY   A 191 ? 0.1813 0.1854 0.2157 0.0001  0.0073  0.0067  191 GLY   A N   
2854 C  CA  . GLY   A 191 ? 0.1767 0.1768 0.2024 -0.0025 0.0132  0.0060  191 GLY   A CA  
2855 C  C   . GLY   A 191 ? 0.1859 0.1838 0.2027 -0.0028 0.0120  0.0099  191 GLY   A C   
2856 O  O   . GLY   A 191 ? 0.1918 0.1844 0.2029 -0.0026 0.0149  0.0105  191 GLY   A O   
2860 N  N   . MET   A 192 ? 0.1865 0.1900 0.2023 -0.0037 0.0075  0.0123  192 MET   A N   
2861 C  CA  . MET   A 192 ? 0.1912 0.1967 0.1989 -0.0052 0.0069  0.0152  192 MET   A CA  
2862 C  C   . MET   A 192 ? 0.1895 0.1907 0.1952 -0.0044 0.0058  0.0200  192 MET   A C   
2863 O  O   . MET   A 192 ? 0.1821 0.1837 0.1822 -0.0051 0.0080  0.0203  192 MET   A O   
2864 C  CB  . MET   A 192 ? 0.2059 0.2203 0.2115 -0.0078 0.0021  0.0174  192 MET   A CB  
2865 C  CG  . MET   A 192 ? 0.2187 0.2387 0.2259 -0.0090 0.0027  0.0119  192 MET   A CG  
2866 S  SD  . MET   A 192 ? 0.2123 0.2442 0.2157 -0.0126 -0.0038 0.0147  192 MET   A SD  
2867 C  CE  . MET   A 192 ? 0.2638 0.3018 0.2558 -0.0161 -0.0027 0.0175  192 MET   A CE  
2877 N  N   . ASN   A 193 ? 0.1940 0.1918 0.2054 -0.0029 0.0018  0.0230  193 ASN   A N   
2878 C  CA  . ASN   A 193 ? 0.1854 0.1779 0.1962 -0.0025 0.0000  0.0271  193 ASN   A CA  
2879 C  C   . ASN   A 193 ? 0.1879 0.1759 0.1969 -0.0007 0.0058  0.0238  193 ASN   A C   
2880 O  O   . ASN   A 193 ? 0.1862 0.1736 0.1901 -0.0017 0.0069  0.0255  193 ASN   A O   
2881 C  CB  . ASN   A 193 ? 0.1936 0.1822 0.2139 -0.0001 -0.0062 0.0286  193 ASN   A CB  
2882 C  CG  . ASN   A 193 ? 0.1999 0.1815 0.2213 0.0002  -0.0093 0.0324  193 ASN   A CG  
2883 O  OD1 . ASN   A 193 ? 0.2018 0.1808 0.2203 0.0006  -0.0049 0.0308  193 ASN   A OD1 
2884 N  ND2 . ASN   A 193 ? 0.1955 0.1732 0.2213 -0.0002 -0.0181 0.0379  193 ASN   A ND2 
2891 N  N   . GLU   A 194 ? 0.1716 0.1577 0.1842 0.0011  0.0092  0.0189  194 GLU   A N   
2892 C  CA  . GLU   A 194 ? 0.1981 0.1796 0.2069 0.0018  0.0140  0.0166  194 GLU   A CA  
2893 C  C   . GLU   A 194 ? 0.1907 0.1718 0.1923 0.0010  0.0162  0.0164  194 GLU   A C   
2894 O  O   . GLU   A 194 ? 0.1848 0.1630 0.1826 0.0019  0.0171  0.0169  194 GLU   A O   
2895 C  CB  . GLU   A 194 ? 0.1891 0.1708 0.2013 0.0015  0.0175  0.0120  194 GLU   A CB  
2896 C  CG  . GLU   A 194 ? 0.1786 0.1605 0.1966 0.0032  0.0178  0.0092  194 GLU   A CG  
2897 C  CD  . GLU   A 194 ? 0.1671 0.1443 0.1813 0.0044  0.0178  0.0107  194 GLU   A CD  
2898 O  OE1 . GLU   A 194 ? 0.1996 0.1735 0.2060 0.0033  0.0211  0.0109  194 GLU   A OE1 
2899 O  OE2 . GLU   A 194 ? 0.2068 0.1829 0.2261 0.0063  0.0138  0.0115  194 GLU   A OE2 
2906 N  N   . SER   A 195 ? 0.1934 0.1782 0.1941 -0.0004 0.0164  0.0147  195 SER   A N   
2907 C  CA  . SER   A 195 ? 0.1914 0.1760 0.1877 -0.0002 0.0178  0.0122  195 SER   A CA  
2908 C  C   . SER   A 195 ? 0.1917 0.1817 0.1854 -0.0001 0.0166  0.0136  195 SER   A C   
2909 O  O   . SER   A 195 ? 0.1917 0.1802 0.1834 0.0017  0.0175  0.0116  195 SER   A O   
2910 C  CB  . SER   A 195 ? 0.1951 0.1837 0.1923 -0.0017 0.0177  0.0087  195 SER   A CB  
2911 O  OG  . SER   A 195 ? 0.2204 0.2052 0.2204 -0.0029 0.0192  0.0070  195 SER   A OG  
2917 N  N   . PHE   A 196 ? 0.1904 0.1873 0.1840 -0.0026 0.0140  0.0172  196 PHE   A N   
2918 C  CA  . PHE   A 196 ? 0.1783 0.1825 0.1687 -0.0046 0.0135  0.0189  196 PHE   A CA  
2919 C  C   . PHE   A 196 ? 0.1749 0.1739 0.1655 -0.0029 0.0141  0.0201  196 PHE   A C   
2920 O  O   . PHE   A 196 ? 0.1836 0.1876 0.1729 -0.0027 0.0153  0.0178  196 PHE   A O   
2921 C  CB  . PHE   A 196 ? 0.1980 0.2080 0.1867 -0.0093 0.0096  0.0250  196 PHE   A CB  
2922 C  CG  . PHE   A 196 ? 0.1627 0.1822 0.1469 -0.0137 0.0096  0.0272  196 PHE   A CG  
2923 C  CD1 . PHE   A 196 ? 0.1937 0.2269 0.1742 -0.0164 0.0117  0.0228  196 PHE   A CD1 
2924 C  CD2 . PHE   A 196 ? 0.1923 0.2085 0.1767 -0.0156 0.0080  0.0323  196 PHE   A CD2 
2925 C  CE1 . PHE   A 196 ? 0.1994 0.2451 0.1760 -0.0215 0.0128  0.0235  196 PHE   A CE1 
2926 C  CE2 . PHE   A 196 ? 0.2002 0.2270 0.1807 -0.0211 0.0086  0.0341  196 PHE   A CE2 
2927 C  CZ  . PHE   A 196 ? 0.2011 0.2436 0.1775 -0.0243 0.0114  0.0296  196 PHE   A CZ  
2937 N  N   . SER   A 197 ? 0.1850 0.1756 0.1784 -0.0015 0.0132  0.0224  197 SER   A N   
2938 C  CA  . SER   A 197 ? 0.1864 0.1724 0.1799 0.0000  0.0135  0.0228  197 SER   A CA  
2939 C  C   . SER   A 197 ? 0.2019 0.1844 0.1932 0.0032  0.0160  0.0186  197 SER   A C   
2940 O  O   . SER   A 197 ? 0.1870 0.1701 0.1773 0.0044  0.0159  0.0179  197 SER   A O   
2941 C  CB  . SER   A 197 ? 0.1828 0.1621 0.1806 0.0010  0.0118  0.0243  197 SER   A CB  
2942 O  OG  . SER   A 197 ? 0.2091 0.1888 0.2096 -0.0015 0.0073  0.0290  197 SER   A OG  
2948 N  N   . ASP   A 198 ? 0.1864 0.1647 0.1769 0.0043  0.0174  0.0161  198 ASP   A N   
2949 C  CA  . ASP   A 198 ? 0.2059 0.1783 0.1937 0.0068  0.0180  0.0136  198 ASP   A CA  
2950 C  C   . ASP   A 198 ? 0.2390 0.2173 0.2276 0.0085  0.0171  0.0096  198 ASP   A C   
2951 O  O   . ASP   A 198 ? 0.2101 0.1857 0.1983 0.0116  0.0157  0.0074  198 ASP   A O   
2952 C  CB  . ASP   A 198 ? 0.2046 0.1700 0.1911 0.0059  0.0192  0.0128  198 ASP   A CB  
2953 C  CG  . ASP   A 198 ? 0.2079 0.1695 0.1936 0.0043  0.0209  0.0146  198 ASP   A CG  
2954 O  OD1 . ASP   A 198 ? 0.2109 0.1722 0.1960 0.0051  0.0207  0.0157  198 ASP   A OD1 
2955 O  OD2 . ASP   A 198 ? 0.2047 0.1643 0.1905 0.0018  0.0227  0.0139  198 ASP   A OD2 
2960 N  N   . MET   A 199 ? 0.1847 0.1725 0.1747 0.0066  0.0174  0.0078  199 MET   A N   
2961 C  CA  . MET   A 199 ? 0.2034 0.2011 0.1951 0.0078  0.0172  0.0021  199 MET   A CA  
2962 C  C   . MET   A 199 ? 0.2021 0.2077 0.1946 0.0075  0.0171  0.0025  199 MET   A C   
2963 O  O   . MET   A 199 ? 0.1979 0.2081 0.1934 0.0108  0.0164  -0.0032 199 MET   A O   
2964 C  CB  . MET   A 199 ? 0.2020 0.2115 0.1937 0.0042  0.0179  0.0002  199 MET   A CB  
2965 C  CG  . MET   A 199 ? 0.1980 0.2026 0.1901 0.0040  0.0178  -0.0015 199 MET   A CG  
2966 S  SD  . MET   A 199 ? 0.2078 0.2281 0.1981 -0.0011 0.0178  -0.0021 199 MET   A SD  
2967 C  CE  . MET   A 199 ? 0.2026 0.2149 0.1942 -0.0019 0.0171  -0.0009 199 MET   A CE  
2977 N  N   . ALA   A 200 ? 0.1869 0.1940 0.1778 0.0036  0.0171  0.0087  200 ALA   A N   
2978 C  CA  . ALA   A 200 ? 0.1927 0.2070 0.1844 0.0017  0.0169  0.0097  200 ALA   A CA  
2979 C  C   . ALA   A 200 ? 0.1965 0.2036 0.1896 0.0062  0.0159  0.0083  200 ALA   A C   
2980 O  O   . ALA   A 200 ? 0.2037 0.2188 0.1992 0.0065  0.0156  0.0056  200 ALA   A O   
2981 C  CB  . ALA   A 200 ? 0.2098 0.2236 0.2000 -0.0038 0.0157  0.0174  200 ALA   A CB  
2987 N  N   . ALA   A 201 ? 0.1964 0.1898 0.1875 0.0090  0.0152  0.0100  201 ALA   A N   
2988 C  CA  . ALA   A 201 ? 0.2031 0.1896 0.1935 0.0129  0.0135  0.0090  201 ALA   A CA  
2989 C  C   . ALA   A 201 ? 0.2092 0.1987 0.2025 0.0175  0.0116  0.0028  201 ALA   A C   
2990 O  O   . ALA   A 201 ? 0.2148 0.2075 0.2105 0.0203  0.0094  0.0003  201 ALA   A O   
2991 C  CB  . ALA   A 201 ? 0.1978 0.1711 0.1838 0.0135  0.0136  0.0118  201 ALA   A CB  
2997 N  N   . GLN   A 202 ? 0.2040 0.1926 0.1984 0.0188  0.0115  -0.0007 202 GLN   A N   
2998 C  CA  . GLN   A 202 ? 0.2308 0.2222 0.2304 0.0241  0.0086  -0.0085 202 GLN   A CA  
2999 C  C   . GLN   A 202 ? 0.2242 0.2353 0.2299 0.0239  0.0098  -0.0147 202 GLN   A C   
3000 O  O   . GLN   A 202 ? 0.2225 0.2384 0.2342 0.0288  0.0069  -0.0209 202 GLN   A O   
3001 C  CB  . GLN   A 202 ? 0.2094 0.1971 0.2100 0.0246  0.0085  -0.0119 202 GLN   A CB  
3002 C  CG  . GLN   A 202 ? 0.2198 0.1906 0.2147 0.0230  0.0082  -0.0059 202 GLN   A CG  
3003 C  CD  . GLN   A 202 ? 0.2604 0.2160 0.2515 0.0255  0.0041  -0.0024 202 GLN   A CD  
3004 O  OE1 . GLN   A 202 ? 0.2395 0.1906 0.2341 0.0308  -0.0012 -0.0064 202 GLN   A OE1 
3005 N  NE2 . GLN   A 202 ? 0.3024 0.2511 0.2867 0.0219  0.0059  0.0046  202 GLN   A NE2 
3014 N  N   . ALA   A 203 ? 0.2262 0.2499 0.2306 0.0177  0.0137  -0.0133 203 ALA   A N   
3015 C  CA  . ALA   A 203 ? 0.2069 0.2519 0.2157 0.0150  0.0157  -0.0188 203 ALA   A CA  
3016 C  C   . ALA   A 203 ? 0.2375 0.2865 0.2485 0.0147  0.0149  -0.0176 203 ALA   A C   
3017 O  O   . ALA   A 203 ? 0.2526 0.3170 0.2706 0.0163  0.0148  -0.0255 203 ALA   A O   
3018 C  CB  . ALA   A 203 ? 0.2168 0.2724 0.2208 0.0065  0.0192  -0.0146 203 ALA   A CB  
3024 N  N   . ALA   A 204 ? 0.2187 0.2553 0.2249 0.0128  0.0142  -0.0090 204 ALA   A N   
3025 C  CA  . ALA   A 204 ? 0.2123 0.2519 0.2209 0.0125  0.0129  -0.0083 204 ALA   A CA  
3026 C  C   . ALA   A 204 ? 0.2623 0.2996 0.2759 0.0208  0.0088  -0.0148 204 ALA   A C   
3027 O  O   . ALA   A 204 ? 0.2418 0.2921 0.2621 0.0218  0.0079  -0.0203 204 ALA   A O   
3028 C  CB  . ALA   A 204 ? 0.2250 0.2507 0.2283 0.0099  0.0123  0.0004  204 ALA   A CB  
3034 N  N   . GLU   A 205 ? 0.2172 0.2381 0.2281 0.0263  0.0057  -0.0140 205 GLU   A N   
3035 C  CA  . GLU   A 205 ? 0.2357 0.2514 0.2508 0.0343  -0.0003 -0.0189 205 GLU   A CA  
3036 C  C   . GLU   A 205 ? 0.2551 0.2866 0.2814 0.0388  -0.0016 -0.0306 205 GLU   A C   
3037 O  O   . GLU   A 205 ? 0.2547 0.2939 0.2890 0.0439  -0.0055 -0.0371 205 GLU   A O   
3038 C  CB  . GLU   A 205 ? 0.2579 0.2523 0.2668 0.0374  -0.0037 -0.0147 205 GLU   A CB  
3039 C  CG  . GLU   A 205 ? 0.2481 0.2294 0.2469 0.0337  -0.0029 -0.0053 205 GLU   A CG  
3040 C  CD  . GLU   A 205 ? 0.2856 0.2481 0.2770 0.0347  -0.0057 -0.0008 205 GLU   A CD  
3041 O  OE1 . GLU   A 205 ? 0.2988 0.2548 0.2929 0.0386  -0.0098 -0.0039 205 GLU   A OE1 
3042 O  OE2 . GLU   A 205 ? 0.2587 0.2134 0.2418 0.0308  -0.0040 0.0057  205 GLU   A OE2 
3049 N  N   . TYR   A 206 ? 0.2421 0.2800 0.2700 0.0373  0.0015  -0.0347 206 TYR   A N   
3050 C  CA  . TYR   A 206 ? 0.3175 0.3733 0.3568 0.0413  0.0010  -0.0481 206 TYR   A CA  
3051 C  C   . TYR   A 206 ? 0.3315 0.4127 0.3770 0.0376  0.0045  -0.0536 206 TYR   A C   
3052 O  O   . TYR   A 206 ? 0.3663 0.4611 0.4239 0.0435  0.0016  -0.0651 206 TYR   A O   
3053 C  CB  . TYR   A 206 ? 0.2838 0.3433 0.3214 0.0384  0.0047  -0.0508 206 TYR   A CB  
3054 C  CG  . TYR   A 206 ? 0.3987 0.4687 0.4479 0.0449  0.0023  -0.0658 206 TYR   A CG  
3055 C  CD1 . TYR   A 206 ? 0.3939 0.4461 0.4484 0.0541  -0.0054 -0.0698 206 TYR   A CD1 
3056 C  CD2 . TYR   A 206 ? 0.5190 0.6167 0.5739 0.0416  0.0073  -0.0763 206 TYR   A CD2 
3057 C  CE1 . TYR   A 206 ? 0.5245 0.5849 0.5918 0.0611  -0.0088 -0.0850 206 TYR   A CE1 
3058 C  CE2 . TYR   A 206 ? 0.5572 0.6665 0.6244 0.0482  0.0052  -0.0925 206 TYR   A CE2 
3059 C  CZ  . TYR   A 206 ? 0.6301 0.7200 0.7045 0.0586  -0.0033 -0.0973 206 TYR   A CZ  
3060 O  OH  . TYR   A 206 ? 0.7874 0.8872 0.8761 0.0662  -0.0067 -0.1148 206 TYR   A OH  
3070 N  N   . TYR   A 207 ? 0.2901 0.3779 0.3285 0.0276  0.0099  -0.0456 207 TYR   A N   
3071 C  CA  . TYR   A 207 ? 0.3028 0.4142 0.3459 0.0217  0.0133  -0.0492 207 TYR   A CA  
3072 C  C   . TYR   A 207 ? 0.3240 0.4356 0.3741 0.0269  0.0088  -0.0520 207 TYR   A C   
3073 O  O   . TYR   A 207 ? 0.3733 0.5069 0.4344 0.0279  0.0091  -0.0625 207 TYR   A O   
3074 C  CB  . TYR   A 207 ? 0.3569 0.4688 0.3900 0.0096  0.0178  -0.0374 207 TYR   A CB  
3075 C  CG  . TYR   A 207 ? 0.3301 0.4649 0.3664 0.0008  0.0213  -0.0390 207 TYR   A CG  
3076 C  CD1 . TYR   A 207 ? 0.3169 0.4502 0.3558 -0.0001 0.0193  -0.0364 207 TYR   A CD1 
3077 C  CD2 . TYR   A 207 ? 0.3459 0.5049 0.3821 -0.0077 0.0265  -0.0431 207 TYR   A CD2 
3078 C  CE1 . TYR   A 207 ? 0.3499 0.5044 0.3923 -0.0094 0.0224  -0.0378 207 TYR   A CE1 
3079 C  CE2 . TYR   A 207 ? 0.2804 0.4614 0.3186 -0.0179 0.0300  -0.0438 207 TYR   A CE2 
3080 C  CZ  . TYR   A 207 ? 0.3596 0.5378 0.4015 -0.0187 0.0279  -0.0411 207 TYR   A CZ  
3081 O  OH  . TYR   A 207 ? 0.3739 0.5740 0.4184 -0.0298 0.0313  -0.0417 207 TYR   A OH  
3091 N  N   . SER   A 208 ? 0.3117 0.4008 0.3557 0.0299  0.0046  -0.0434 208 SER   A N   
3092 C  CA  . SER   A 208 ? 0.2963 0.3850 0.3448 0.0337  -0.0001 -0.0446 208 SER   A CA  
3093 C  C   . SER   A 208 ? 0.3843 0.4742 0.4436 0.0454  -0.0073 -0.0552 208 SER   A C   
3094 O  O   . SER   A 208 ? 0.3267 0.4332 0.3972 0.0483  -0.0096 -0.0637 208 SER   A O   
3095 C  CB  . SER   A 208 ? 0.3831 0.4485 0.4206 0.0330  -0.0023 -0.0330 208 SER   A CB  
3096 O  OG  . SER   A 208 ? 0.4027 0.4692 0.4426 0.0346  -0.0062 -0.0332 208 SER   A OG  
3102 N  N   . VAL   A 209 ? 0.3610 0.4332 0.4184 0.0521  -0.0117 -0.0549 209 VAL   A N   
3103 C  CA  . VAL   A 209 ? 0.3242 0.3912 0.3913 0.0638  -0.0214 -0.0629 209 VAL   A CA  
3104 C  C   . VAL   A 209 ? 0.3697 0.4369 0.4449 0.0701  -0.0237 -0.0726 209 VAL   A C   
3105 O  O   . VAL   A 209 ? 0.4175 0.4761 0.5015 0.0805  -0.0334 -0.0790 209 VAL   A O   
3106 C  CB  . VAL   A 209 ? 0.4069 0.4463 0.4638 0.0673  -0.0289 -0.0523 209 VAL   A CB  
3107 C  CG1 . VAL   A 209 ? 0.4574 0.4988 0.5095 0.0635  -0.0286 -0.0465 209 VAL   A CG1 
3108 C  CG2 . VAL   A 209 ? 0.3639 0.3822 0.4068 0.0628  -0.0261 -0.0417 209 VAL   A CG2 
3118 N  N   . GLY   A 210 ? 0.2954 0.3721 0.3685 0.0640  -0.0159 -0.0743 210 GLY   A N   
3119 C  CA  . GLY   A 210 ? 0.3082 0.3875 0.3898 0.0696  -0.0179 -0.0854 210 GLY   A CA  
3120 C  C   . GLY   A 210 ? 0.4366 0.4862 0.5124 0.0739  -0.0241 -0.0796 210 GLY   A C   
3121 O  O   . GLY   A 210 ? 0.4252 0.4729 0.5103 0.0804  -0.0284 -0.0897 210 GLY   A O   
3125 N  N   . LYS   A 211 ? 0.3391 0.3663 0.4003 0.0699  -0.0246 -0.0642 211 LYS   A N   
3126 C  CA  . LYS   A 211 ? 0.3654 0.3653 0.4191 0.0713  -0.0295 -0.0570 211 LYS   A CA  
3127 C  C   . LYS   A 211 ? 0.3130 0.3016 0.3501 0.0620  -0.0236 -0.0422 211 LYS   A C   
3128 O  O   . LYS   A 211 ? 0.3047 0.3008 0.3369 0.0572  -0.0192 -0.0369 211 LYS   A O   
3129 C  CB  . LYS   A 211 ? 0.3814 0.3622 0.4378 0.0798  -0.0420 -0.0558 211 LYS   A CB  
3130 C  CG  . LYS   A 211 ? 0.5670 0.5566 0.6268 0.0829  -0.0455 -0.0565 211 LYS   A CG  
3131 C  CD  . LYS   A 211 ? 0.5935 0.5640 0.6558 0.0918  -0.0597 -0.0550 211 LYS   A CD  
3132 C  CE  . LYS   A 211 ? 0.7584 0.7057 0.8017 0.0864  -0.0621 -0.0381 211 LYS   A CE  
3133 N  NZ  . LYS   A 211 ? 0.9207 0.8793 0.9558 0.0796  -0.0545 -0.0323 211 LYS   A NZ  
3147 N  N   . ASN   A 212 ? 0.3364 0.3070 0.3661 0.0597  -0.0240 -0.0363 212 ASN   A N   
3148 C  CA  . ASN   A 212 ? 0.2826 0.2444 0.2988 0.0513  -0.0182 -0.0244 212 ASN   A CA  
3149 C  C   . ASN   A 212 ? 0.2881 0.2256 0.2967 0.0507  -0.0231 -0.0174 212 ASN   A C   
3150 O  O   . ASN   A 212 ? 0.3198 0.2472 0.3339 0.0554  -0.0296 -0.0219 212 ASN   A O   
3151 C  CB  . ASN   A 212 ? 0.2379 0.2141 0.2540 0.0453  -0.0096 -0.0261 212 ASN   A CB  
3152 C  CG  . ASN   A 212 ? 0.3276 0.3033 0.3489 0.0470  -0.0102 -0.0332 212 ASN   A CG  
3153 O  OD1 . ASN   A 212 ? 0.3299 0.3174 0.3623 0.0522  -0.0124 -0.0450 212 ASN   A OD1 
3154 N  ND2 . ASN   A 212 ? 0.2928 0.2573 0.3075 0.0423  -0.0081 -0.0276 212 ASN   A ND2 
3161 N  N   . SER   A 213 ? 0.2702 0.1988 0.2666 0.0444  -0.0200 -0.0068 213 SER   A N   
3162 C  CA  . SER   A 213 ? 0.2835 0.1905 0.2702 0.0419  -0.0245 0.0015  213 SER   A CA  
3163 C  C   . SER   A 213 ? 0.2767 0.1767 0.2610 0.0367  -0.0212 0.0031  213 SER   A C   
3164 O  O   . SER   A 213 ? 0.3048 0.1866 0.2827 0.0340  -0.0257 0.0089  213 SER   A O   
3165 C  CB  . SER   A 213 ? 0.3060 0.2098 0.2805 0.0365  -0.0220 0.0107  213 SER   A CB  
3166 O  OG  . SER   A 213 ? 0.2891 0.2026 0.2614 0.0304  -0.0126 0.0120  213 SER   A OG  
3172 N  N   . TRP   A 214 ? 0.2497 0.1635 0.2380 0.0343  -0.0139 -0.0011 214 TRP   A N   
3173 C  CA  . TRP   A 214 ? 0.2691 0.1800 0.2552 0.0286  -0.0096 0.0004  214 TRP   A CA  
3174 C  C   . TRP   A 214 ? 0.2881 0.1917 0.2633 0.0211  -0.0060 0.0099  214 TRP   A C   
3175 O  O   . TRP   A 214 ? 0.2760 0.1738 0.2486 0.0158  -0.0040 0.0120  214 TRP   A O   
3176 C  CB  . TRP   A 214 ? 0.2674 0.1659 0.2582 0.0307  -0.0155 -0.0037 214 TRP   A CB  
3177 C  CG  . TRP   A 214 ? 0.2752 0.1860 0.2786 0.0373  -0.0170 -0.0160 214 TRP   A CG  
3178 C  CD1 . TRP   A 214 ? 0.3322 0.2385 0.3448 0.0452  -0.0251 -0.0238 214 TRP   A CD1 
3179 C  CD2 . TRP   A 214 ? 0.2552 0.1866 0.2634 0.0361  -0.0104 -0.0227 214 TRP   A CD2 
3180 N  NE1 . TRP   A 214 ? 0.3227 0.2479 0.3462 0.0492  -0.0230 -0.0364 214 TRP   A NE1 
3181 C  CE2 . TRP   A 214 ? 0.3069 0.2476 0.3267 0.0429  -0.0138 -0.0352 214 TRP   A CE2 
3182 C  CE3 . TRP   A 214 ? 0.2792 0.2220 0.2832 0.0300  -0.0027 -0.0195 214 TRP   A CE3 
3183 C  CZ2 . TRP   A 214 ? 0.3216 0.2845 0.3468 0.0424  -0.0088 -0.0441 214 TRP   A CZ2 
3184 C  CZ3 . TRP   A 214 ? 0.2995 0.2616 0.3085 0.0297  0.0009  -0.0267 214 TRP   A CZ3 
3185 C  CH2 . TRP   A 214 ? 0.3292 0.3018 0.3476 0.0352  -0.0015 -0.0387 214 TRP   A CH2 
3196 N  N   . GLN   A 215 ? 0.2587 0.1642 0.2281 0.0203  -0.0051 0.0143  215 GLN   A N   
3197 C  CA  . GLN   A 215 ? 0.2572 0.1601 0.2172 0.0135  -0.0010 0.0210  215 GLN   A CA  
3198 C  C   . GLN   A 215 ? 0.2443 0.1609 0.2057 0.0136  0.0038  0.0201  215 GLN   A C   
3199 O  O   . GLN   A 215 ? 0.2597 0.1848 0.2269 0.0182  0.0028  0.0165  215 GLN   A O   
3200 C  CB  . GLN   A 215 ? 0.2736 0.1623 0.2232 0.0117  -0.0064 0.0277  215 GLN   A CB  
3201 C  CG  . GLN   A 215 ? 0.2978 0.1692 0.2456 0.0108  -0.0130 0.0302  215 GLN   A CG  
3202 C  CD  . GLN   A 215 ? 0.3304 0.1863 0.2663 0.0081  -0.0200 0.0387  215 GLN   A CD  
3203 O  OE1 . GLN   A 215 ? 0.3697 0.2292 0.2982 0.0072  -0.0196 0.0419  215 GLN   A OE1 
3204 N  NE2 . GLN   A 215 ? 0.3840 0.2215 0.3173 0.0062  -0.0272 0.0425  215 GLN   A NE2 
3213 N  N   . ILE   A 216 ? 0.2298 0.1493 0.1872 0.0083  0.0089  0.0226  216 ILE   A N   
3214 C  CA  . ILE   A 216 ? 0.2039 0.1338 0.1632 0.0082  0.0124  0.0216  216 ILE   A CA  
3215 C  C   . ILE   A 216 ? 0.2591 0.1859 0.2095 0.0055  0.0123  0.0246  216 ILE   A C   
3216 O  O   . ILE   A 216 ? 0.2607 0.1834 0.2039 0.0000  0.0143  0.0274  216 ILE   A O   
3217 C  CB  . ILE   A 216 ? 0.2233 0.1609 0.1877 0.0054  0.0173  0.0199  216 ILE   A CB  
3218 C  CG1 . ILE   A 216 ? 0.2157 0.1571 0.1869 0.0071  0.0170  0.0172  216 ILE   A CG1 
3219 C  CG2 . ILE   A 216 ? 0.2455 0.1910 0.2133 0.0058  0.0191  0.0186  216 ILE   A CG2 
3220 C  CD1 . ILE   A 216 ? 0.2334 0.1825 0.2097 0.0108  0.0154  0.0149  216 ILE   A CD1 
3232 N  N   . GLY   A 217 ? 0.2389 0.1689 0.1893 0.0086  0.0101  0.0239  217 GLY   A N   
3233 C  CA  . GLY   A 217 ? 0.2645 0.1945 0.2070 0.0062  0.0102  0.0253  217 GLY   A CA  
3234 C  C   . GLY   A 217 ? 0.3024 0.2223 0.2330 0.0047  0.0053  0.0304  217 GLY   A C   
3235 O  O   . GLY   A 217 ? 0.3060 0.2277 0.2280 0.0012  0.0059  0.0317  217 GLY   A O   
3239 N  N   . PRO   A 218 ? 0.2618 0.1709 0.1913 0.0071  -0.0006 0.0332  218 PRO   A N   
3240 C  CA  . PRO   A 218 ? 0.2831 0.1806 0.2005 0.0053  -0.0073 0.0395  218 PRO   A CA  
3241 C  C   . PRO   A 218 ? 0.3062 0.2082 0.2207 0.0082  -0.0108 0.0388  218 PRO   A C   
3242 O  O   . PRO   A 218 ? 0.3316 0.2295 0.2330 0.0040  -0.0135 0.0438  218 PRO   A O   
3243 C  CB  . PRO   A 218 ? 0.3101 0.1953 0.2318 0.0099  -0.0148 0.0404  218 PRO   A CB  
3244 C  CG  . PRO   A 218 ? 0.3004 0.1958 0.2371 0.0162  -0.0126 0.0326  218 PRO   A CG  
3245 C  CD  . PRO   A 218 ? 0.2623 0.1691 0.2016 0.0119  -0.0030 0.0303  218 PRO   A CD  
3253 N  N   . GLU   A 219 ? 0.2935 0.2051 0.2195 0.0144  -0.0107 0.0328  219 GLU   A N   
3254 C  CA  . GLU   A 219 ? 0.2900 0.2066 0.2155 0.0175  -0.0146 0.0312  219 GLU   A CA  
3255 C  C   . GLU   A 219 ? 0.3306 0.2549 0.2497 0.0125  -0.0097 0.0303  219 GLU   A C   
3256 O  O   . GLU   A 219 ? 0.3482 0.2754 0.2634 0.0136  -0.0134 0.0297  219 GLU   A O   
3257 C  CB  . GLU   A 219 ? 0.2825 0.2092 0.2227 0.0236  -0.0148 0.0246  219 GLU   A CB  
3258 C  CG  . GLU   A 219 ? 0.2859 0.2231 0.2343 0.0216  -0.0070 0.0207  219 GLU   A CG  
3259 C  CD  . GLU   A 219 ? 0.2782 0.2150 0.2323 0.0212  -0.0035 0.0200  219 GLU   A CD  
3260 O  OE1 . GLU   A 219 ? 0.2990 0.2264 0.2498 0.0212  -0.0056 0.0225  219 GLU   A OE1 
3261 O  OE2 . GLU   A 219 ? 0.2861 0.2315 0.2477 0.0203  0.0009  0.0174  219 GLU   A OE2 
3268 N  N   . ILE   A 220 ? 0.2928 0.2212 0.2117 0.0076  -0.0021 0.0290  220 ILE   A N   
3269 C  CA  . ILE   A 220 ? 0.3080 0.2452 0.2233 0.0036  0.0024  0.0257  220 ILE   A CA  
3270 C  C   . ILE   A 220 ? 0.2861 0.2227 0.1889 -0.0043 0.0061  0.0284  220 ILE   A C   
3271 O  O   . ILE   A 220 ? 0.2999 0.2460 0.1995 -0.0079 0.0102  0.0241  220 ILE   A O   
3272 C  CB  . ILE   A 220 ? 0.3877 0.3340 0.3167 0.0053  0.0075  0.0191  220 ILE   A CB  
3273 C  CG1 . ILE   A 220 ? 0.3114 0.2568 0.2470 0.0045  0.0115  0.0193  220 ILE   A CG1 
3274 C  CG2 . ILE   A 220 ? 0.3318 0.2813 0.2705 0.0106  0.0039  0.0166  220 ILE   A CG2 
3275 C  CD1 . ILE   A 220 ? 0.3663 0.3140 0.2974 -0.0012 0.0168  0.0188  220 ILE   A CD1 
3287 N  N   . MET   A 221 ? 0.3069 0.2334 0.2023 -0.0078 0.0046  0.0351  221 MET   A N   
3288 C  CA  . MET   A 221 ? 0.3532 0.2802 0.2352 -0.0174 0.0082  0.0386  221 MET   A CA  
3289 C  C   . MET   A 221 ? 0.3452 0.2676 0.2100 -0.0211 0.0021  0.0448  221 MET   A C   
3290 O  O   . MET   A 221 ? 0.3771 0.2871 0.2387 -0.0173 -0.0071 0.0507  221 MET   A O   
3291 C  CB  . MET   A 221 ? 0.3759 0.2929 0.2564 -0.0213 0.0083  0.0441  221 MET   A CB  
3292 C  CG  . MET   A 221 ? 0.4081 0.3311 0.3026 -0.0200 0.0148  0.0385  221 MET   A CG  
3293 S  SD  . MET   A 221 ? 0.3759 0.3180 0.2787 -0.0217 0.0241  0.0286  221 MET   A SD  
3294 C  CE  . MET   A 221 ? 0.4120 0.3599 0.2968 -0.0348 0.0286  0.0314  221 MET   A CE  
3304 N  N   . LYS   A 222 ? 0.3283 0.2616 0.1825 -0.0284 0.0066  0.0428  222 LYS   A N   
3305 C  CA  . LYS   A 222 ? 0.3393 0.2697 0.1749 -0.0332 0.0007  0.0491  222 LYS   A CA  
3306 C  C   . LYS   A 222 ? 0.4158 0.3300 0.2364 -0.0404 -0.0048 0.0620  222 LYS   A C   
3307 O  O   . LYS   A 222 ? 0.4367 0.3485 0.2569 -0.0466 -0.0002 0.0644  222 LYS   A O   
3308 C  CB  . LYS   A 222 ? 0.4061 0.3545 0.2330 -0.0409 0.0078  0.0429  222 LYS   A CB  
3309 C  CG  . LYS   A 222 ? 0.4347 0.3973 0.2760 -0.0342 0.0116  0.0299  222 LYS   A CG  
3310 C  CD  . LYS   A 222 ? 0.4963 0.4633 0.3296 -0.0329 0.0063  0.0282  222 LYS   A CD  
3311 C  CE  . LYS   A 222 ? 0.3664 0.3474 0.2145 -0.0279 0.0105  0.0144  222 LYS   A CE  
3312 N  NZ  . LYS   A 222 ? 0.4716 0.4689 0.3097 -0.0341 0.0142  0.0068  222 LYS   A NZ  
3326 N  N   . GLU   A 223 ? 0.4070 0.3097 0.2154 -0.0400 -0.0157 0.0704  223 GLU   A N   
3327 C  CA  . GLU   A 223 ? 0.5317 0.4147 0.3265 -0.0460 -0.0241 0.0839  223 GLU   A CA  
3328 C  C   . GLU   A 223 ? 0.5077 0.3972 0.2884 -0.0608 -0.0180 0.0885  223 GLU   A C   
3329 O  O   . GLU   A 223 ? 0.5601 0.4382 0.3402 -0.0651 -0.0217 0.0957  223 GLU   A O   
3330 C  CB  . GLU   A 223 ? 0.5991 0.4699 0.3864 -0.0410 -0.0385 0.0909  223 GLU   A CB  
3331 C  CG  . GLU   A 223 ? 0.5957 0.4646 0.4026 -0.0255 -0.0442 0.0839  223 GLU   A CG  
3332 C  CD  . GLU   A 223 ? 0.6270 0.5121 0.4376 -0.0207 -0.0428 0.0755  223 GLU   A CD  
3333 O  OE1 . GLU   A 223 ? 0.4996 0.4019 0.3131 -0.0238 -0.0317 0.0671  223 GLU   A OE1 
3334 O  OE2 . GLU   A 223 ? 0.5645 0.4452 0.3766 -0.0134 -0.0534 0.0764  223 GLU   A OE2 
3341 N  N   . ASP   A 224 ? 0.4522 0.3623 0.2260 -0.0678 -0.0086 0.0820  224 ASP   A N   
3342 C  CA  . ASP   A 224 ? 0.4322 0.3541 0.1985 -0.0807 -0.0015 0.0827  224 ASP   A CA  
3343 C  C   . ASP   A 224 ? 0.4560 0.3925 0.2318 -0.0846 0.0117  0.0736  224 ASP   A C   
3344 O  O   . ASP   A 224 ? 0.4715 0.4241 0.2436 -0.0947 0.0193  0.0702  224 ASP   A O   
3345 C  CB  . ASP   A 224 ? 0.4906 0.4283 0.2436 -0.0868 -0.0002 0.0805  224 ASP   A CB  
3346 C  CG  . ASP   A 224 ? 0.6356 0.5855 0.3911 -0.0799 0.0020  0.0701  224 ASP   A CG  
3347 O  OD1 . ASP   A 224 ? 0.5302 0.4864 0.2977 -0.0748 0.0088  0.0607  224 ASP   A OD1 
3348 O  OD2 . ASP   A 224 ? 0.7194 0.6734 0.4650 -0.0800 -0.0032 0.0709  224 ASP   A OD2 
3353 N  N   . SER   A 225 ? 0.4211 0.3533 0.2100 -0.0769 0.0141  0.0690  225 SER   A N   
3354 C  CA  . SER   A 225 ? 0.4341 0.3814 0.2364 -0.0786 0.0256  0.0590  225 SER   A CA  
3355 C  C   . SER   A 225 ? 0.4237 0.3648 0.2262 -0.0866 0.0273  0.0648  225 SER   A C   
3356 O  O   . SER   A 225 ? 0.4692 0.4262 0.2781 -0.0923 0.0368  0.0576  225 SER   A O   
3357 C  CB  . SER   A 225 ? 0.3891 0.3367 0.2157 -0.0638 0.0261  0.0496  225 SER   A CB  
3358 O  OG  . SER   A 225 ? 0.3811 0.3091 0.2141 -0.0574 0.0189  0.0562  225 SER   A OG  
3364 N  N   . GLY   A 226 ? 0.4464 0.3658 0.2462 -0.0855 0.0174  0.0757  226 GLY   A N   
3365 C  CA  . GLY   A 226 ? 0.4795 0.3910 0.2835 -0.0908 0.0175  0.0799  226 GLY   A CA  
3366 C  C   . GLY   A 226 ? 0.4496 0.3524 0.2682 -0.0834 0.0182  0.0769  226 GLY   A C   
3367 O  O   . GLY   A 226 ? 0.4735 0.3710 0.2970 -0.0876 0.0188  0.0790  226 GLY   A O   
3371 N  N   . TYR   A 227 ? 0.4090 0.3125 0.2377 -0.0716 0.0179  0.0707  227 TYR   A N   
3372 C  CA  . TYR   A 227 ? 0.3845 0.2840 0.2326 -0.0613 0.0175  0.0653  227 TYR   A CA  
3373 C  C   . TYR   A 227 ? 0.4002 0.2857 0.2529 -0.0494 0.0072  0.0672  227 TYR   A C   
3374 O  O   . TYR   A 227 ? 0.4647 0.3555 0.3171 -0.0435 0.0053  0.0645  227 TYR   A O   
3375 C  CB  . TYR   A 227 ? 0.3814 0.3012 0.2454 -0.0559 0.0263  0.0525  227 TYR   A CB  
3376 C  CG  . TYR   A 227 ? 0.4545 0.3914 0.3186 -0.0657 0.0364  0.0475  227 TYR   A CG  
3377 C  CD1 . TYR   A 227 ? 0.5404 0.4778 0.4116 -0.0698 0.0400  0.0466  227 TYR   A CD1 
3378 C  CD2 . TYR   A 227 ? 0.4421 0.3966 0.2999 -0.0709 0.0422  0.0423  227 TYR   A CD2 
3379 C  CE1 . TYR   A 227 ? 0.5587 0.5144 0.4318 -0.0787 0.0492  0.0407  227 TYR   A CE1 
3380 C  CE2 . TYR   A 227 ? 0.4722 0.4458 0.3320 -0.0796 0.0517  0.0355  227 TYR   A CE2 
3381 C  CZ  . TYR   A 227 ? 0.5528 0.5272 0.4206 -0.0834 0.0552  0.0348  227 TYR   A CZ  
3382 O  OH  . TYR   A 227 ? 0.6322 0.6281 0.5036 -0.0920 0.0647  0.0268  227 TYR   A OH  
3392 N  N   . ASP   A 228 ? 0.3997 0.2687 0.2579 -0.0457 0.0007  0.0706  228 ASP   A N   
3393 C  CA  . ASP   A 228 ? 0.3803 0.2400 0.2464 -0.0334 -0.0083 0.0695  228 ASP   A CA  
3394 C  C   . ASP   A 228 ? 0.3583 0.2314 0.2423 -0.0231 -0.0039 0.0587  228 ASP   A C   
3395 O  O   . ASP   A 228 ? 0.3561 0.2291 0.2461 -0.0139 -0.0089 0.0559  228 ASP   A O   
3396 C  CB  . ASP   A 228 ? 0.4064 0.2452 0.2747 -0.0316 -0.0176 0.0743  228 ASP   A CB  
3397 C  CG  . ASP   A 228 ? 0.5729 0.3965 0.4259 -0.0404 -0.0249 0.0857  228 ASP   A CG  
3398 O  OD1 . ASP   A 228 ? 0.6289 0.4572 0.4699 -0.0443 -0.0261 0.0899  228 ASP   A OD1 
3399 O  OD2 . ASP   A 228 ? 0.7363 0.5487 0.5938 -0.0422 -0.0291 0.0879  228 ASP   A OD2 
3404 N  N   . ALA   A 229 ? 0.3030 0.1876 0.1955 -0.0249 0.0048  0.0529  229 ALA   A N   
3405 C  CA  . ALA   A 229 ? 0.2908 0.1865 0.1989 -0.0168 0.0083  0.0444  229 ALA   A CA  
3406 C  C   . ALA   A 229 ? 0.2979 0.2073 0.2111 -0.0212 0.0174  0.0396  229 ALA   A C   
3407 O  O   . ALA   A 229 ? 0.3227 0.2331 0.2297 -0.0301 0.0213  0.0417  229 ALA   A O   
3408 C  CB  . ALA   A 229 ? 0.3156 0.2040 0.2340 -0.0104 0.0039  0.0424  229 ALA   A CB  
3414 N  N   . LEU   A 230 ? 0.2843 0.2047 0.2095 -0.0153 0.0202  0.0329  230 LEU   A N   
3415 C  CA  . LEU   A 230 ? 0.2918 0.2239 0.2255 -0.0173 0.0267  0.0277  230 LEU   A CA  
3416 C  C   . LEU   A 230 ? 0.2952 0.2239 0.2344 -0.0185 0.0271  0.0277  230 LEU   A C   
3417 O  O   . LEU   A 230 ? 0.2943 0.2280 0.2342 -0.0246 0.0316  0.0264  230 LEU   A O   
3418 C  CB  . LEU   A 230 ? 0.2930 0.2344 0.2375 -0.0108 0.0274  0.0221  230 LEU   A CB  
3419 C  CG  . LEU   A 230 ? 0.3236 0.2701 0.2658 -0.0094 0.0274  0.0200  230 LEU   A CG  
3420 C  CD1 . LEU   A 230 ? 0.3347 0.2870 0.2885 -0.0036 0.0266  0.0157  230 LEU   A CD1 
3421 C  CD2 . LEU   A 230 ? 0.3194 0.2746 0.2571 -0.0158 0.0326  0.0169  230 LEU   A CD2 
3433 N  N   . ARG   A 231 ? 0.2667 0.1889 0.2105 -0.0129 0.0226  0.0279  231 ARG   A N   
3434 C  CA  . ARG   A 231 ? 0.2397 0.1596 0.1895 -0.0133 0.0224  0.0264  231 ARG   A CA  
3435 C  C   . ARG   A 231 ? 0.2400 0.1477 0.1893 -0.0093 0.0157  0.0278  231 ARG   A C   
3436 O  O   . ARG   A 231 ? 0.2457 0.1505 0.1940 -0.0040 0.0115  0.0282  231 ARG   A O   
3437 C  CB  . ARG   A 231 ? 0.2207 0.1522 0.1818 -0.0093 0.0246  0.0212  231 ARG   A CB  
3438 C  CG  . ARG   A 231 ? 0.2317 0.1745 0.1974 -0.0124 0.0296  0.0183  231 ARG   A CG  
3439 C  CD  . ARG   A 231 ? 0.2119 0.1636 0.1881 -0.0081 0.0294  0.0148  231 ARG   A CD  
3440 N  NE  . ARG   A 231 ? 0.2004 0.1543 0.1783 -0.0033 0.0273  0.0149  231 ARG   A NE  
3441 C  CZ  . ARG   A 231 ? 0.1994 0.1585 0.1801 -0.0025 0.0283  0.0132  231 ARG   A CZ  
3442 N  NH1 . ARG   A 231 ? 0.2298 0.1932 0.2104 -0.0057 0.0318  0.0106  231 ARG   A NH1 
3443 N  NH2 . ARG   A 231 ? 0.1942 0.1550 0.1784 0.0012  0.0257  0.0133  231 ARG   A NH2 
3457 N  N   . TYR   A 232 ? 0.2648 0.1662 0.2163 -0.0116 0.0145  0.0273  232 TYR   A N   
3458 C  CA  . TYR   A 232 ? 0.2641 0.1539 0.2182 -0.0075 0.0078  0.0263  232 TYR   A CA  
3459 C  C   . TYR   A 232 ? 0.2731 0.1709 0.2377 -0.0046 0.0091  0.0193  232 TYR   A C   
3460 O  O   . TYR   A 232 ? 0.2814 0.1843 0.2483 -0.0093 0.0131  0.0181  232 TYR   A O   
3461 C  CB  . TYR   A 232 ? 0.2854 0.1582 0.2320 -0.0142 0.0040  0.0320  232 TYR   A CB  
3462 C  CG  . TYR   A 232 ? 0.3260 0.1922 0.2594 -0.0197 0.0031  0.0402  232 TYR   A CG  
3463 C  CD1 . TYR   A 232 ? 0.3774 0.2322 0.3054 -0.0157 -0.0048 0.0441  232 TYR   A CD1 
3464 C  CD2 . TYR   A 232 ? 0.3528 0.2268 0.2794 -0.0289 0.0100  0.0429  232 TYR   A CD2 
3465 C  CE1 . TYR   A 232 ? 0.3926 0.2420 0.3067 -0.0215 -0.0062 0.0520  232 TYR   A CE1 
3466 C  CE2 . TYR   A 232 ? 0.3712 0.2420 0.2844 -0.0349 0.0098  0.0496  232 TYR   A CE2 
3467 C  CZ  . TYR   A 232 ? 0.4366 0.2946 0.3426 -0.0315 0.0015  0.0548  232 TYR   A CZ  
3468 O  OH  . TYR   A 232 ? 0.5177 0.3731 0.4087 -0.0382 0.0007  0.0620  232 TYR   A OH  
3478 N  N   . MET   A 233 ? 0.2642 0.1651 0.2352 0.0028  0.0058  0.0140  233 MET   A N   
3479 C  CA  . MET   A 233 ? 0.2549 0.1661 0.2343 0.0048  0.0072  0.0070  233 MET   A CA  
3480 C  C   . MET   A 233 ? 0.2757 0.1772 0.2593 0.0054  0.0027  0.0026  233 MET   A C   
3481 O  O   . MET   A 233 ? 0.2685 0.1775 0.2575 0.0046  0.0044  -0.0028 233 MET   A O   
3482 C  CB  . MET   A 233 ? 0.2335 0.1575 0.2175 0.0109  0.0073  0.0027  233 MET   A CB  
3483 C  CG  . MET   A 233 ? 0.2870 0.2207 0.2686 0.0095  0.0115  0.0064  233 MET   A CG  
3484 S  SD  . MET   A 233 ? 0.2654 0.2137 0.2515 0.0140  0.0115  0.0028  233 MET   A SD  
3485 C  CE  . MET   A 233 ? 0.2248 0.1865 0.2146 0.0110  0.0147  0.0000  233 MET   A CE  
3495 N  N   . ASP   A 234 ? 0.2739 0.1581 0.2552 0.0066  -0.0040 0.0048  234 ASP   A N   
3496 C  CA  . ASP   A 234 ? 0.2706 0.1431 0.2574 0.0073  -0.0097 0.0001  234 ASP   A CA  
3497 C  C   . ASP   A 234 ? 0.2936 0.1586 0.2770 -0.0021 -0.0075 0.0040  234 ASP   A C   
3498 O  O   . ASP   A 234 ? 0.3346 0.1976 0.3245 -0.0029 -0.0091 -0.0020 234 ASP   A O   
3499 C  CB  . ASP   A 234 ? 0.3477 0.2014 0.3339 0.0117  -0.0195 0.0020  234 ASP   A CB  
3500 C  CG  . ASP   A 234 ? 0.3350 0.1736 0.3083 0.0047  -0.0213 0.0146  234 ASP   A CG  
3501 O  OD1 . ASP   A 234 ? 0.3756 0.2229 0.3415 0.0022  -0.0158 0.0199  234 ASP   A OD1 
3502 O  OD2 . ASP   A 234 ? 0.4442 0.2618 0.4145 0.0016  -0.0287 0.0191  234 ASP   A OD2 
3507 N  N   . LYS   A 235 ? 0.2781 0.1405 0.2519 -0.0097 -0.0039 0.0131  235 LYS   A N   
3508 C  CA  . LYS   A 235 ? 0.2785 0.1370 0.2489 -0.0202 -0.0007 0.0169  235 LYS   A CA  
3509 C  C   . LYS   A 235 ? 0.2831 0.1541 0.2474 -0.0254 0.0071  0.0216  235 LYS   A C   
3510 O  O   . LYS   A 235 ? 0.3194 0.1838 0.2734 -0.0310 0.0074  0.0292  235 LYS   A O   
3511 C  CB  . LYS   A 235 ? 0.3482 0.1830 0.3123 -0.0261 -0.0078 0.0237  235 LYS   A CB  
3512 C  CG  . LYS   A 235 ? 0.3875 0.2186 0.3485 -0.0387 -0.0046 0.0273  235 LYS   A CG  
3513 C  CD  . LYS   A 235 ? 0.4503 0.2555 0.4036 -0.0456 -0.0129 0.0359  235 LYS   A CD  
3514 C  CE  . LYS   A 235 ? 0.6624 0.4653 0.6088 -0.0613 -0.0086 0.0424  235 LYS   A CE  
3515 N  NZ  . LYS   A 235 ? 0.7328 0.5085 0.6758 -0.0684 -0.0183 0.0486  235 LYS   A NZ  
3529 N  N   . PRO   A 236 ? 0.2610 0.1505 0.2313 -0.0236 0.0130  0.0167  236 PRO   A N   
3530 C  CA  . PRO   A 236 ? 0.2342 0.1361 0.2015 -0.0265 0.0194  0.0190  236 PRO   A CA  
3531 C  C   . PRO   A 236 ? 0.2658 0.1656 0.2264 -0.0375 0.0230  0.0238  236 PRO   A C   
3532 O  O   . PRO   A 236 ? 0.2531 0.1580 0.2075 -0.0402 0.0265  0.0268  236 PRO   A O   
3533 C  CB  . PRO   A 236 ? 0.2400 0.1586 0.2169 -0.0235 0.0228  0.0128  236 PRO   A CB  
3534 C  CG  . PRO   A 236 ? 0.2431 0.1609 0.2251 -0.0164 0.0184  0.0080  236 PRO   A CG  
3535 C  CD  . PRO   A 236 ? 0.2648 0.1649 0.2448 -0.0178 0.0130  0.0086  236 PRO   A CD  
3543 N  N   . SER   A 237 ? 0.2706 0.1642 0.2322 -0.0447 0.0225  0.0240  237 SER   A N   
3544 C  CA  . SER   A 237 ? 0.2730 0.1671 0.2284 -0.0572 0.0267  0.0282  237 SER   A CA  
3545 C  C   . SER   A 237 ? 0.2729 0.1534 0.2138 -0.0631 0.0241  0.0376  237 SER   A C   
3546 O  O   . SER   A 237 ? 0.3343 0.2180 0.2674 -0.0748 0.0285  0.0418  237 SER   A O   
3547 C  CB  . SER   A 237 ? 0.3149 0.2035 0.2749 -0.0642 0.0257  0.0266  237 SER   A CB  
3548 O  OG  . SER   A 237 ? 0.3283 0.1952 0.2866 -0.0626 0.0171  0.0290  237 SER   A OG  
3554 N  N   . ARG   A 238 ? 0.3394 0.2064 0.2761 -0.0558 0.0170  0.0408  238 ARG   A N   
3555 C  CA  . ARG   A 238 ? 0.3247 0.1797 0.2468 -0.0607 0.0135  0.0503  238 ARG   A CA  
3556 C  C   . ARG   A 238 ? 0.3569 0.2283 0.2720 -0.0649 0.0211  0.0511  238 ARG   A C   
3557 O  O   . ARG   A 238 ? 0.3934 0.2598 0.2944 -0.0741 0.0208  0.0590  238 ARG   A O   
3558 C  CB  . ARG   A 238 ? 0.3606 0.2024 0.2827 -0.0497 0.0044  0.0513  238 ARG   A CB  
3559 C  CG  . ARG   A 238 ? 0.5327 0.3600 0.4396 -0.0537 -0.0017 0.0617  238 ARG   A CG  
3560 C  CD  . ARG   A 238 ? 0.6156 0.4300 0.5254 -0.0419 -0.0121 0.0615  238 ARG   A CD  
3561 N  NE  . ARG   A 238 ? 0.6087 0.4063 0.5269 -0.0378 -0.0207 0.0591  238 ARG   A NE  
3562 C  CZ  . ARG   A 238 ? 0.5665 0.3697 0.4997 -0.0273 -0.0216 0.0484  238 ARG   A CZ  
3563 N  NH1 . ARG   A 238 ? 0.5458 0.3693 0.4863 -0.0199 -0.0154 0.0409  238 ARG   A NH1 
3564 N  NH2 . ARG   A 238 ? 0.6523 0.4406 0.5933 -0.0247 -0.0294 0.0452  238 ARG   A NH2 
3578 N  N   . ASP   A 239 ? 0.3158 0.2068 0.2405 -0.0588 0.0273  0.0430  239 ASP   A N   
3579 C  CA  . ASP   A 239 ? 0.3326 0.2397 0.2533 -0.0615 0.0338  0.0415  239 ASP   A CA  
3580 C  C   . ASP   A 239 ? 0.3371 0.2590 0.2582 -0.0729 0.0420  0.0390  239 ASP   A C   
3581 O  O   . ASP   A 239 ? 0.3634 0.3010 0.2824 -0.0757 0.0479  0.0357  239 ASP   A O   
3582 C  CB  . ASP   A 239 ? 0.2842 0.2036 0.2158 -0.0497 0.0352  0.0341  239 ASP   A CB  
3583 C  CG  . ASP   A 239 ? 0.2734 0.2058 0.2199 -0.0466 0.0387  0.0262  239 ASP   A CG  
3584 O  OD1 . ASP   A 239 ? 0.2910 0.2256 0.2407 -0.0532 0.0410  0.0250  239 ASP   A OD1 
3585 O  OD2 . ASP   A 239 ? 0.2783 0.2177 0.2332 -0.0377 0.0382  0.0218  239 ASP   A OD2 
3590 N  N   . GLY   A 240 ? 0.3202 0.2388 0.2447 -0.0796 0.0425  0.0393  240 GLY   A N   
3591 C  CA  . GLY   A 240 ? 0.3575 0.2908 0.2824 -0.0920 0.0501  0.0369  240 GLY   A CA  
3592 C  C   . GLY   A 240 ? 0.3278 0.2825 0.2699 -0.0879 0.0558  0.0256  240 GLY   A C   
3593 O  O   . GLY   A 240 ? 0.3624 0.3317 0.3079 -0.0978 0.0621  0.0219  240 GLY   A O   
3597 N  N   . MET   A 241 ? 0.2996 0.2573 0.2529 -0.0744 0.0532  0.0202  241 MET   A N   
3598 C  CA  B MET   A 241 ? 0.3203 0.2967 0.2898 -0.0700 0.0566  0.0104  241 MET   A CA  
3599 C  CA  C MET   A 241 ? 0.3203 0.2969 0.2898 -0.0696 0.0566  0.0103  241 MET   A CA  
3600 C  C   . MET   A 241 ? 0.2823 0.2546 0.2618 -0.0591 0.0513  0.0079  241 MET   A C   
3601 O  O   . MET   A 241 ? 0.2853 0.2687 0.2768 -0.0580 0.0522  0.0018  241 MET   A O   
3602 C  CB  B MET   A 241 ? 0.3293 0.3225 0.3032 -0.0660 0.0606  0.0041  241 MET   A CB  
3603 C  CB  C MET   A 241 ? 0.3288 0.3201 0.3016 -0.0648 0.0599  0.0048  241 MET   A CB  
3604 C  CG  B MET   A 241 ? 0.3772 0.3897 0.3689 -0.0626 0.0631  -0.0061 241 MET   A CG  
3605 C  CG  C MET   A 241 ? 0.3983 0.4105 0.3883 -0.0617 0.0631  -0.0059 241 MET   A CG  
3606 S  SD  B MET   A 241 ? 0.3993 0.4374 0.3974 -0.0667 0.0709  -0.0164 241 MET   A SD  
3607 S  SD  C MET   A 241 ? 0.4630 0.4934 0.4573 -0.0755 0.0708  -0.0114 241 MET   A SD  
3608 C  CE  B MET   A 241 ? 0.2894 0.3438 0.3114 -0.0591 0.0693  -0.0274 241 MET   A CE  
3609 C  CE  C MET   A 241 ? 0.3226 0.3588 0.3015 -0.0851 0.0769  -0.0093 241 MET   A CE  
3628 N  N   . SER   A 242 ? 0.2425 0.2012 0.2174 -0.0515 0.0458  0.0119  242 SER   A N   
3629 C  CA  . SER   A 242 ? 0.2247 0.1819 0.2075 -0.0426 0.0414  0.0094  242 SER   A CA  
3630 C  C   . SER   A 242 ? 0.2358 0.1864 0.2210 -0.0462 0.0392  0.0088  242 SER   A C   
3631 O  O   . SER   A 242 ? 0.2589 0.1993 0.2377 -0.0545 0.0391  0.0125  242 SER   A O   
3632 C  CB  . SER   A 242 ? 0.2298 0.1769 0.2075 -0.0348 0.0369  0.0127  242 SER   A CB  
3633 O  OG  . SER   A 242 ? 0.2326 0.1867 0.2101 -0.0310 0.0384  0.0122  242 SER   A OG  
3639 N  N   . ILE   A 243 ? 0.2210 0.1769 0.2149 -0.0405 0.0368  0.0043  243 ILE   A N   
3640 C  CA  . ILE   A 243 ? 0.2411 0.1939 0.2391 -0.0433 0.0347  0.0015  243 ILE   A CA  
3641 C  C   . ILE   A 243 ? 0.2501 0.1932 0.2470 -0.0366 0.0292  0.0009  243 ILE   A C   
3642 O  O   . ILE   A 243 ? 0.2429 0.1882 0.2392 -0.0291 0.0276  0.0011  243 ILE   A O   
3643 C  CB  . ILE   A 243 ? 0.2234 0.1931 0.2328 -0.0434 0.0362  -0.0047 243 ILE   A CB  
3644 C  CG1 . ILE   A 243 ? 0.2190 0.1982 0.2332 -0.0342 0.0340  -0.0064 243 ILE   A CG1 
3645 C  CG2 . ILE   A 243 ? 0.2317 0.2123 0.2444 -0.0514 0.0418  -0.0063 243 ILE   A CG2 
3646 C  CD1 . ILE   A 243 ? 0.2254 0.2184 0.2501 -0.0333 0.0325  -0.0116 243 ILE   A CD1 
3658 N  N   . ASP   A 244 ? 0.2458 0.1792 0.2435 -0.0398 0.0263  -0.0008 244 ASP   A N   
3659 C  CA  . ASP   A 244 ? 0.2348 0.1588 0.2328 -0.0339 0.0208  -0.0035 244 ASP   A CA  
3660 C  C   . ASP   A 244 ? 0.2511 0.1857 0.2569 -0.0307 0.0194  -0.0114 244 ASP   A C   
3661 O  O   . ASP   A 244 ? 0.2580 0.1918 0.2650 -0.0245 0.0160  -0.0156 244 ASP   A O   
3662 C  CB  . ASP   A 244 ? 0.2769 0.1806 0.2715 -0.0387 0.0166  -0.0012 244 ASP   A CB  
3663 C  CG  . ASP   A 244 ? 0.2751 0.1662 0.2595 -0.0422 0.0162  0.0078  244 ASP   A CG  
3664 O  OD1 . ASP   A 244 ? 0.2974 0.1939 0.2777 -0.0381 0.0181  0.0107  244 ASP   A OD1 
3665 O  OD2 . ASP   A 244 ? 0.3360 0.2115 0.3160 -0.0500 0.0135  0.0122  244 ASP   A OD2 
3670 N  N   . VAL   A 245 ? 0.2345 0.1803 0.2458 -0.0352 0.0218  -0.0142 245 VAL   A N   
3671 C  CA  . VAL   A 245 ? 0.2251 0.1820 0.2428 -0.0332 0.0199  -0.0214 245 VAL   A CA  
3672 C  C   . VAL   A 245 ? 0.2548 0.2290 0.2772 -0.0340 0.0224  -0.0216 245 VAL   A C   
3673 O  O   . VAL   A 245 ? 0.2390 0.2163 0.2626 -0.0377 0.0258  -0.0186 245 VAL   A O   
3674 C  CB  . VAL   A 245 ? 0.2851 0.2346 0.3069 -0.0385 0.0176  -0.0267 245 VAL   A CB  
3675 C  CG1 . VAL   A 245 ? 0.3180 0.2485 0.3371 -0.0365 0.0131  -0.0272 245 VAL   A CG1 
3676 C  CG2 . VAL   A 245 ? 0.3032 0.2523 0.3269 -0.0483 0.0208  -0.0243 245 VAL   A CG2 
3686 N  N   . ALA   A 246 ? 0.2281 0.2145 0.2538 -0.0305 0.0199  -0.0258 246 ALA   A N   
3687 C  CA  . ALA   A 246 ? 0.2260 0.2276 0.2567 -0.0299 0.0198  -0.0255 246 ALA   A CA  
3688 C  C   . ALA   A 246 ? 0.2332 0.2408 0.2717 -0.0361 0.0214  -0.0287 246 ALA   A C   
3689 O  O   . ALA   A 246 ? 0.2689 0.2869 0.3133 -0.0360 0.0223  -0.0282 246 ALA   A O   
3690 C  CB  . ALA   A 246 ? 0.2118 0.2244 0.2422 -0.0262 0.0158  -0.0282 246 ALA   A CB  
3696 N  N   . ASP   A 247 ? 0.2189 0.2205 0.2590 -0.0417 0.0215  -0.0327 247 ASP   A N   
3697 C  CA  . ASP   A 247 ? 0.2488 0.2576 0.2970 -0.0490 0.0232  -0.0363 247 ASP   A CA  
3698 C  C   . ASP   A 247 ? 0.2337 0.2419 0.2823 -0.0545 0.0286  -0.0326 247 ASP   A C   
3699 O  O   . ASP   A 247 ? 0.2726 0.2917 0.3293 -0.0606 0.0309  -0.0361 247 ASP   A O   
3700 C  CB  . ASP   A 247 ? 0.2900 0.2901 0.3394 -0.0549 0.0216  -0.0411 247 ASP   A CB  
3701 C  CG  . ASP   A 247 ? 0.3343 0.3425 0.3866 -0.0515 0.0169  -0.0483 247 ASP   A CG  
3702 O  OD1 . ASP   A 247 ? 0.4004 0.4233 0.4542 -0.0466 0.0148  -0.0490 247 ASP   A OD1 
3703 O  OD2 . ASP   A 247 ? 0.4211 0.4205 0.4741 -0.0542 0.0147  -0.0534 247 ASP   A OD2 
3708 N  N   . ASP   A 248 ? 0.2391 0.2369 0.2794 -0.0530 0.0306  -0.0265 248 ASP   A N   
3709 C  CA  . ASP   A 248 ? 0.2451 0.2442 0.2840 -0.0587 0.0360  -0.0234 248 ASP   A CA  
3710 C  C   . ASP   A 248 ? 0.2269 0.2397 0.2704 -0.0529 0.0374  -0.0238 248 ASP   A C   
3711 O  O   . ASP   A 248 ? 0.2497 0.2664 0.2925 -0.0564 0.0422  -0.0228 248 ASP   A O   
3712 C  CB  . ASP   A 248 ? 0.2584 0.2384 0.2852 -0.0613 0.0366  -0.0165 248 ASP   A CB  
3713 C  CG  . ASP   A 248 ? 0.3405 0.3050 0.3644 -0.0687 0.0344  -0.0158 248 ASP   A CG  
3714 O  OD1 . ASP   A 248 ? 0.3537 0.3240 0.3850 -0.0742 0.0343  -0.0209 248 ASP   A OD1 
3715 O  OD2 . ASP   A 248 ? 0.3950 0.3409 0.4100 -0.0692 0.0320  -0.0104 248 ASP   A OD2 
3720 N  N   . TYR   A 249 ? 0.2240 0.2441 0.2721 -0.0446 0.0330  -0.0255 249 TYR   A N   
3721 C  CA  . TYR   A 249 ? 0.2071 0.2376 0.2610 -0.0384 0.0322  -0.0259 249 TYR   A CA  
3722 C  C   . TYR   A 249 ? 0.2295 0.2775 0.2971 -0.0412 0.0339  -0.0326 249 TYR   A C   
3723 O  O   . TYR   A 249 ? 0.2670 0.3224 0.3413 -0.0453 0.0332  -0.0373 249 TYR   A O   
3724 C  CB  . TYR   A 249 ? 0.2452 0.2770 0.2991 -0.0304 0.0256  -0.0244 249 TYR   A CB  
3725 C  CG  . TYR   A 249 ? 0.2304 0.2702 0.2913 -0.0241 0.0225  -0.0242 249 TYR   A CG  
3726 C  CD1 . TYR   A 249 ? 0.2390 0.2728 0.2956 -0.0204 0.0234  -0.0203 249 TYR   A CD1 
3727 C  CD2 . TYR   A 249 ? 0.2531 0.3061 0.3260 -0.0217 0.0177  -0.0283 249 TYR   A CD2 
3728 C  CE1 . TYR   A 249 ? 0.2137 0.2531 0.2782 -0.0146 0.0197  -0.0208 249 TYR   A CE1 
3729 C  CE2 . TYR   A 249 ? 0.2403 0.2984 0.3213 -0.0153 0.0132  -0.0282 249 TYR   A CE2 
3730 C  CZ  . TYR   A 249 ? 0.2696 0.3203 0.3465 -0.0119 0.0142  -0.0246 249 TYR   A CZ  
3731 O  OH  . TYR   A 249 ? 0.3008 0.3547 0.3868 -0.0055 0.0087  -0.0252 249 TYR   A OH  
3741 N  N   . TYR   A 250 ? 0.2093 0.2651 0.2821 -0.0390 0.0362  -0.0345 250 TYR   A N   
3742 C  CA  . TYR   A 250 ? 0.2105 0.2859 0.2994 -0.0392 0.0370  -0.0429 250 TYR   A CA  
3743 C  C   . TYR   A 250 ? 0.2674 0.3470 0.3633 -0.0296 0.0331  -0.0441 250 TYR   A C   
3744 O  O   . TYR   A 250 ? 0.2361 0.3046 0.3231 -0.0258 0.0327  -0.0387 250 TYR   A O   
3745 C  CB  . TYR   A 250 ? 0.2248 0.3089 0.3150 -0.0500 0.0459  -0.0472 250 TYR   A CB  
3746 C  CG  . TYR   A 250 ? 0.2682 0.3432 0.3454 -0.0543 0.0518  -0.0423 250 TYR   A CG  
3747 C  CD1 . TYR   A 250 ? 0.2895 0.3461 0.3508 -0.0603 0.0531  -0.0342 250 TYR   A CD1 
3748 C  CD2 . TYR   A 250 ? 0.2421 0.3280 0.3235 -0.0528 0.0555  -0.0467 250 TYR   A CD2 
3749 C  CE1 . TYR   A 250 ? 0.2796 0.3275 0.3282 -0.0644 0.0572  -0.0288 250 TYR   A CE1 
3750 C  CE2 . TYR   A 250 ? 0.3400 0.4189 0.4081 -0.0576 0.0608  -0.0423 250 TYR   A CE2 
3751 C  CZ  . TYR   A 250 ? 0.3280 0.3876 0.3791 -0.0636 0.0613  -0.0326 250 TYR   A CZ  
3752 O  OH  . TYR   A 250 ? 0.3192 0.3712 0.3563 -0.0683 0.0651  -0.0273 250 TYR   A OH  
3762 N  N   . GLY   A 251 ? 0.3150 0.4105 0.4281 -0.0254 0.0292  -0.0518 251 GLY   A N   
3763 C  CA  . GLY   A 251 ? 0.3008 0.3981 0.4230 -0.0151 0.0221  -0.0529 251 GLY   A CA  
3764 C  C   . GLY   A 251 ? 0.2981 0.3957 0.4209 -0.0131 0.0263  -0.0554 251 GLY   A C   
3765 O  O   . GLY   A 251 ? 0.3929 0.4852 0.5190 -0.0049 0.0201  -0.0539 251 GLY   A O   
3769 N  N   . GLY   A 252 ? 0.2485 0.3525 0.3679 -0.0212 0.0362  -0.0592 252 GLY   A N   
3770 C  CA  . GLY   A 252 ? 0.2586 0.3653 0.3770 -0.0208 0.0410  -0.0625 252 GLY   A CA  
3771 C  C   . GLY   A 252 ? 0.2289 0.3177 0.3273 -0.0233 0.0441  -0.0527 252 GLY   A C   
3772 O  O   . GLY   A 252 ? 0.2721 0.3628 0.3668 -0.0244 0.0487  -0.0549 252 GLY   A O   
3776 N  N   . LEU   A 253 ? 0.2101 0.2825 0.2958 -0.0241 0.0414  -0.0429 253 LEU   A N   
3777 C  CA  . LEU   A 253 ? 0.2121 0.2679 0.2801 -0.0261 0.0435  -0.0343 253 LEU   A CA  
3778 C  C   . LEU   A 253 ? 0.1929 0.2403 0.2599 -0.0171 0.0380  -0.0309 253 LEU   A C   
3779 O  O   . LEU   A 253 ? 0.2175 0.2618 0.2890 -0.0110 0.0307  -0.0286 253 LEU   A O   
3780 C  CB  . LEU   A 253 ? 0.2248 0.2682 0.2824 -0.0298 0.0424  -0.0275 253 LEU   A CB  
3781 C  CG  . LEU   A 253 ? 0.2978 0.3242 0.3385 -0.0328 0.0440  -0.0195 253 LEU   A CG  
3782 C  CD1 . LEU   A 253 ? 0.2489 0.2773 0.2831 -0.0417 0.0510  -0.0197 253 LEU   A CD1 
3783 C  CD2 . LEU   A 253 ? 0.2502 0.2673 0.2864 -0.0347 0.0413  -0.0162 253 LEU   A CD2 
3795 N  N   . ASP   A 254 ? 0.1823 0.2268 0.2432 -0.0172 0.0412  -0.0305 254 ASP   A N   
3796 C  CA  . ASP   A 254 ? 0.1940 0.2306 0.2542 -0.0099 0.0363  -0.0277 254 ASP   A CA  
3797 C  C   . ASP   A 254 ? 0.1930 0.2144 0.2418 -0.0084 0.0325  -0.0179 254 ASP   A C   
3798 O  O   . ASP   A 254 ? 0.1884 0.2033 0.2271 -0.0131 0.0349  -0.0137 254 ASP   A O   
3799 C  CB  . ASP   A 254 ? 0.1987 0.2361 0.2534 -0.0114 0.0411  -0.0299 254 ASP   A CB  
3800 C  CG  . ASP   A 254 ? 0.2000 0.2302 0.2559 -0.0042 0.0360  -0.0284 254 ASP   A CG  
3801 O  OD1 . ASP   A 254 ? 0.2319 0.2680 0.3025 0.0018  0.0314  -0.0345 254 ASP   A OD1 
3802 O  OD2 . ASP   A 254 ? 0.1919 0.2103 0.2352 -0.0046 0.0358  -0.0213 254 ASP   A OD2 
3807 N  N   . VAL   A 255 ? 0.1881 0.2043 0.2391 -0.0023 0.0263  -0.0149 255 VAL   A N   
3808 C  CA  . VAL   A 255 ? 0.1604 0.1662 0.2019 -0.0013 0.0228  -0.0069 255 VAL   A CA  
3809 C  C   . VAL   A 255 ? 0.1720 0.1690 0.2001 -0.0040 0.0270  -0.0030 255 VAL   A C   
3810 O  O   . VAL   A 255 ? 0.1911 0.1820 0.2118 -0.0044 0.0258  0.0014  255 VAL   A O   
3811 C  CB  . VAL   A 255 ? 0.1765 0.1789 0.2222 0.0040  0.0157  -0.0038 255 VAL   A CB  
3812 C  CG1 . VAL   A 255 ? 0.1871 0.1954 0.2452 0.0069  0.0089  -0.0056 255 VAL   A CG1 
3813 C  CG2 . VAL   A 255 ? 0.1927 0.1933 0.2407 0.0063  0.0166  -0.0065 255 VAL   A CG2 
3823 N  N   . HIS   A 256 ? 0.1847 0.1821 0.2099 -0.0056 0.0312  -0.0052 256 HIS   A N   
3824 C  CA  . HIS   A 256 ? 0.1957 0.1842 0.2080 -0.0080 0.0336  -0.0010 256 HIS   A CA  
3825 C  C   . HIS   A 256 ? 0.2097 0.1944 0.2148 -0.0141 0.0367  0.0007  256 HIS   A C   
3826 O  O   . HIS   A 256 ? 0.2006 0.1759 0.1953 -0.0158 0.0370  0.0049  256 HIS   A O   
3827 C  CB  . HIS   A 256 ? 0.1910 0.1822 0.2018 -0.0083 0.0363  -0.0039 256 HIS   A CB  
3828 C  CG  . HIS   A 256 ? 0.2065 0.1976 0.2235 -0.0024 0.0322  -0.0050 256 HIS   A CG  
3829 N  ND1 . HIS   A 256 ? 0.1952 0.1941 0.2254 0.0008  0.0304  -0.0114 256 HIS   A ND1 
3830 C  CD2 . HIS   A 256 ? 0.1966 0.1803 0.2093 0.0005  0.0290  -0.0008 256 HIS   A CD2 
3831 C  CE1 . HIS   A 256 ? 0.2100 0.2042 0.2432 0.0052  0.0256  -0.0103 256 HIS   A CE1 
3832 N  NE2 . HIS   A 256 ? 0.2120 0.1978 0.2344 0.0045  0.0252  -0.0037 256 HIS   A NE2 
3841 N  N   . TYR   A 257 ? 0.1940 0.1853 0.2051 -0.0174 0.0382  -0.0025 257 TYR   A N   
3842 C  CA  . TYR   A 257 ? 0.1806 0.1677 0.1866 -0.0239 0.0403  -0.0011 257 TYR   A CA  
3843 C  C   . TYR   A 257 ? 0.2125 0.1984 0.2224 -0.0225 0.0369  -0.0013 257 TYR   A C   
3844 O  O   . TYR   A 257 ? 0.2069 0.1835 0.2111 -0.0247 0.0359  0.0010  257 TYR   A O   
3845 C  CB  . TYR   A 257 ? 0.2088 0.2070 0.2187 -0.0310 0.0458  -0.0057 257 TYR   A CB  
3846 C  CG  . TYR   A 257 ? 0.1981 0.2005 0.2031 -0.0336 0.0499  -0.0069 257 TYR   A CG  
3847 C  CD1 . TYR   A 257 ? 0.2210 0.2121 0.2128 -0.0345 0.0495  -0.0009 257 TYR   A CD1 
3848 C  CD2 . TYR   A 257 ? 0.1982 0.2175 0.2129 -0.0346 0.0537  -0.0151 257 TYR   A CD2 
3849 C  CE1 . TYR   A 257 ? 0.2347 0.2311 0.2210 -0.0373 0.0530  -0.0023 257 TYR   A CE1 
3850 C  CE2 . TYR   A 257 ? 0.2370 0.2628 0.2475 -0.0372 0.0578  -0.0179 257 TYR   A CE2 
3851 C  CZ  . TYR   A 257 ? 0.2644 0.2785 0.2596 -0.0390 0.0576  -0.0110 257 TYR   A CZ  
3852 O  OH  . TYR   A 257 ? 0.2847 0.3061 0.2742 -0.0421 0.0614  -0.0139 257 TYR   A OH  
3862 N  N   . SER   A 258 ? 0.2005 0.1957 0.2204 -0.0186 0.0342  -0.0044 258 SER   A N   
3863 C  CA  . SER   A 258 ? 0.1914 0.1871 0.2134 -0.0173 0.0305  -0.0045 258 SER   A CA  
3864 C  C   . SER   A 258 ? 0.2070 0.1957 0.2225 -0.0132 0.0272  -0.0006 258 SER   A C   
3865 O  O   . SER   A 258 ? 0.1959 0.1849 0.2106 -0.0129 0.0248  -0.0014 258 SER   A O   
3866 C  CB  . SER   A 258 ? 0.2023 0.2097 0.2357 -0.0146 0.0273  -0.0078 258 SER   A CB  
3867 O  OG  . SER   A 258 ? 0.1933 0.2005 0.2284 -0.0091 0.0236  -0.0055 258 SER   A OG  
3873 N  N   . SER   A 259 ? 0.1976 0.1816 0.2087 -0.0105 0.0272  0.0023  259 SER   A N   
3874 C  CA  . SER   A 259 ? 0.1842 0.1630 0.1894 -0.0075 0.0250  0.0051  259 SER   A CA  
3875 C  C   . SER   A 259 ? 0.1954 0.1661 0.1952 -0.0090 0.0253  0.0045  259 SER   A C   
3876 O  O   . SER   A 259 ? 0.2018 0.1711 0.1992 -0.0063 0.0232  0.0042  259 SER   A O   
3877 C  CB  . SER   A 259 ? 0.1905 0.1659 0.1926 -0.0050 0.0252  0.0078  259 SER   A CB  
3878 O  OG  . SER   A 259 ? 0.1878 0.1581 0.1857 -0.0076 0.0284  0.0079  259 SER   A OG  
3884 N  N   . GLY   A 260 ? 0.1881 0.1535 0.1865 -0.0136 0.0275  0.0040  260 GLY   A N   
3885 C  CA  . GLY   A 260 ? 0.2007 0.1556 0.1951 -0.0150 0.0260  0.0037  260 GLY   A CA  
3886 C  C   . GLY   A 260 ? 0.2228 0.1809 0.2211 -0.0135 0.0234  -0.0008 260 GLY   A C   
3887 O  O   . GLY   A 260 ? 0.2183 0.1694 0.2151 -0.0114 0.0208  -0.0029 260 GLY   A O   
3891 N  N   . VAL   A 261 ? 0.2057 0.1753 0.2096 -0.0142 0.0236  -0.0033 261 VAL   A N   
3892 C  CA  . VAL   A 261 ? 0.2087 0.1832 0.2152 -0.0138 0.0212  -0.0083 261 VAL   A CA  
3893 C  C   . VAL   A 261 ? 0.2003 0.1780 0.2042 -0.0091 0.0192  -0.0096 261 VAL   A C   
3894 O  O   . VAL   A 261 ? 0.2115 0.1859 0.2155 -0.0076 0.0175  -0.0145 261 VAL   A O   
3895 C  CB  . VAL   A 261 ? 0.1873 0.1745 0.1995 -0.0154 0.0207  -0.0099 261 VAL   A CB  
3896 C  CG1 . VAL   A 261 ? 0.2353 0.2296 0.2488 -0.0154 0.0181  -0.0154 261 VAL   A CG1 
3897 C  CG2 . VAL   A 261 ? 0.2157 0.2032 0.2325 -0.0204 0.0232  -0.0106 261 VAL   A CG2 
3907 N  N   . TYR   A 262 ? 0.1894 0.1742 0.1920 -0.0071 0.0190  -0.0060 262 TYR   A N   
3908 C  CA  . TYR   A 262 ? 0.1761 0.1671 0.1762 -0.0044 0.0178  -0.0071 262 TYR   A CA  
3909 C  C   . TYR   A 262 ? 0.1903 0.1731 0.1881 -0.0012 0.0180  -0.0069 262 TYR   A C   
3910 O  O   . TYR   A 262 ? 0.1911 0.1791 0.1888 0.0012  0.0171  -0.0110 262 TYR   A O   
3911 C  CB  . TYR   A 262 ? 0.1974 0.1979 0.1964 -0.0049 0.0166  -0.0022 262 TYR   A CB  
3912 C  CG  . TYR   A 262 ? 0.2099 0.2224 0.2090 -0.0074 0.0144  -0.0039 262 TYR   A CG  
3913 C  CD1 . TYR   A 262 ? 0.1949 0.2088 0.1980 -0.0093 0.0135  -0.0059 262 TYR   A CD1 
3914 C  CD2 . TYR   A 262 ? 0.2202 0.2441 0.2150 -0.0087 0.0132  -0.0038 262 TYR   A CD2 
3915 C  CE1 . TYR   A 262 ? 0.1780 0.2033 0.1806 -0.0115 0.0106  -0.0075 262 TYR   A CE1 
3916 C  CE2 . TYR   A 262 ? 0.2056 0.2413 0.1985 -0.0119 0.0108  -0.0049 262 TYR   A CE2 
3917 C  CZ  . TYR   A 262 ? 0.1797 0.2157 0.1765 -0.0129 0.0091  -0.0067 262 TYR   A CZ  
3918 O  OH  . TYR   A 262 ? 0.2103 0.2586 0.2045 -0.0161 0.0060  -0.0078 262 TYR   A OH  
3928 N  N   . ASN   A 263 ? 0.1969 0.1686 0.1930 -0.0014 0.0189  -0.0030 263 ASN   A N   
3929 C  CA  . ASN   A 263 ? 0.1992 0.1622 0.1929 0.0017  0.0177  -0.0027 263 ASN   A CA  
3930 C  C   . ASN   A 263 ? 0.2162 0.1715 0.2118 0.0031  0.0150  -0.0082 263 ASN   A C   
3931 O  O   . ASN   A 263 ? 0.1994 0.1546 0.1966 0.0076  0.0124  -0.0124 263 ASN   A O   
3932 C  CB  . ASN   A 263 ? 0.2119 0.1651 0.2016 0.0001  0.0189  0.0029  263 ASN   A CB  
3933 C  CG  . ASN   A 263 ? 0.1868 0.1458 0.1758 0.0007  0.0204  0.0066  263 ASN   A CG  
3934 O  OD1 . ASN   A 263 ? 0.2187 0.1871 0.2097 0.0018  0.0200  0.0065  263 ASN   A OD1 
3935 N  ND2 . ASN   A 263 ? 0.2151 0.1682 0.2007 -0.0004 0.0216  0.0099  263 ASN   A ND2 
3942 N  N   . HIS   A 264 ? 0.2038 0.1528 0.2004 -0.0007 0.0149  -0.0090 264 HIS   A N   
3943 C  CA  . HIS   A 264 ? 0.2000 0.1394 0.1996 0.0000  0.0112  -0.0145 264 HIS   A CA  
3944 C  C   . HIS   A 264 ? 0.2263 0.1781 0.2313 0.0034  0.0101  -0.0239 264 HIS   A C   
3945 O  O   . HIS   A 264 ? 0.2319 0.1801 0.2410 0.0079  0.0063  -0.0308 264 HIS   A O   
3946 C  CB  . HIS   A 264 ? 0.2258 0.1578 0.2255 -0.0066 0.0120  -0.0128 264 HIS   A CB  
3947 C  CG  . HIS   A 264 ? 0.2584 0.1747 0.2602 -0.0074 0.0073  -0.0159 264 HIS   A CG  
3948 N  ND1 . HIS   A 264 ? 0.2814 0.1921 0.2851 -0.0140 0.0072  -0.0166 264 HIS   A ND1 
3949 C  CD2 . HIS   A 264 ? 0.2665 0.1706 0.2698 -0.0026 0.0014  -0.0185 264 HIS   A CD2 
3950 C  CE1 . HIS   A 264 ? 0.3207 0.2147 0.3264 -0.0136 0.0013  -0.0191 264 HIS   A CE1 
3951 N  NE2 . HIS   A 264 ? 0.2870 0.1764 0.2930 -0.0062 -0.0027 -0.0204 264 HIS   A NE2 
3959 N  N   . LEU   A 265 ? 0.2167 0.1841 0.2218 0.0013  0.0127  -0.0248 265 LEU   A N   
3960 C  CA  . LEU   A 265 ? 0.2317 0.2144 0.2397 0.0029  0.0123  -0.0333 265 LEU   A CA  
3961 C  C   . LEU   A 265 ? 0.2202 0.2103 0.2285 0.0076  0.0119  -0.0365 265 LEU   A C   
3962 O  O   . LEU   A 265 ? 0.2138 0.2109 0.2269 0.0108  0.0103  -0.0469 265 LEU   A O   
3963 C  CB  . LEU   A 265 ? 0.1993 0.1967 0.2049 -0.0011 0.0143  -0.0305 265 LEU   A CB  
3964 C  CG  . LEU   A 265 ? 0.1733 0.1899 0.1781 -0.0016 0.0143  -0.0367 265 LEU   A CG  
3965 C  CD1 . LEU   A 265 ? 0.2135 0.2330 0.2233 -0.0008 0.0127  -0.0486 265 LEU   A CD1 
3966 C  CD2 . LEU   A 265 ? 0.2344 0.2615 0.2354 -0.0060 0.0145  -0.0306 265 LEU   A CD2 
3978 N  N   . PHE   A 266 ? 0.2030 0.1936 0.2075 0.0078  0.0134  -0.0290 266 PHE   A N   
3979 C  CA  . PHE   A 266 ? 0.2039 0.2029 0.2091 0.0113  0.0134  -0.0317 266 PHE   A CA  
3980 C  C   . PHE   A 266 ? 0.2285 0.2171 0.2393 0.0174  0.0095  -0.0381 266 PHE   A C   
3981 O  O   . PHE   A 266 ? 0.2245 0.2237 0.2411 0.0214  0.0083  -0.0479 266 PHE   A O   
3982 C  CB  . PHE   A 266 ? 0.1965 0.1949 0.1969 0.0098  0.0151  -0.0218 266 PHE   A CB  
3983 C  CG  . PHE   A 266 ? 0.2251 0.2324 0.2265 0.0123  0.0153  -0.0236 266 PHE   A CG  
3984 C  CD1 . PHE   A 266 ? 0.2418 0.2689 0.2432 0.0099  0.0171  -0.0274 266 PHE   A CD1 
3985 C  CD2 . PHE   A 266 ? 0.2299 0.2271 0.2316 0.0158  0.0136  -0.0210 266 PHE   A CD2 
3986 C  CE1 . PHE   A 266 ? 0.2268 0.2642 0.2297 0.0109  0.0178  -0.0294 266 PHE   A CE1 
3987 C  CE2 . PHE   A 266 ? 0.2531 0.2599 0.2568 0.0179  0.0136  -0.0232 266 PHE   A CE2 
3988 C  CZ  . PHE   A 266 ? 0.2193 0.2465 0.2242 0.0152  0.0160  -0.0276 266 PHE   A CZ  
3998 N  N   . TYR   A 267 ? 0.2358 0.2042 0.2452 0.0178  0.0068  -0.0328 267 TYR   A N   
3999 C  CA  . TYR   A 267 ? 0.2588 0.2131 0.2728 0.0232  0.0009  -0.0371 267 TYR   A CA  
4000 C  C   . TYR   A 267 ? 0.2496 0.2054 0.2721 0.0259  -0.0023 -0.0494 267 TYR   A C   
4001 O  O   . TYR   A 267 ? 0.2714 0.2291 0.3021 0.0327  -0.0066 -0.0592 267 TYR   A O   
4002 C  CB  . TYR   A 267 ? 0.2419 0.1742 0.2503 0.0203  -0.0013 -0.0274 267 TYR   A CB  
4003 C  CG  . TYR   A 267 ? 0.2644 0.1778 0.2759 0.0246  -0.0093 -0.0292 267 TYR   A CG  
4004 C  CD1 . TYR   A 267 ? 0.2699 0.1785 0.2814 0.0299  -0.0136 -0.0275 267 TYR   A CD1 
4005 C  CD2 . TYR   A 267 ? 0.3011 0.2005 0.3162 0.0233  -0.0138 -0.0324 267 TYR   A CD2 
4006 C  CE1 . TYR   A 267 ? 0.3181 0.2078 0.3327 0.0342  -0.0228 -0.0284 267 TYR   A CE1 
4007 C  CE2 . TYR   A 267 ? 0.3289 0.2078 0.3472 0.0272  -0.0231 -0.0331 267 TYR   A CE2 
4008 C  CZ  . TYR   A 267 ? 0.3363 0.2104 0.3543 0.0330  -0.0279 -0.0308 267 TYR   A CZ  
4009 O  OH  . TYR   A 267 ? 0.3880 0.2406 0.4094 0.0374  -0.0389 -0.0307 267 TYR   A OH  
4019 N  N   . ILE   A 268 ? 0.2275 0.1834 0.2495 0.0211  -0.0007 -0.0504 268 ILE   A N   
4020 C  CA  . ILE   A 268 ? 0.2471 0.2041 0.2774 0.0232  -0.0040 -0.0630 268 ILE   A CA  
4021 C  C   . ILE   A 268 ? 0.2517 0.2333 0.2875 0.0269  -0.0022 -0.0755 268 ILE   A C   
4022 O  O   . ILE   A 268 ? 0.2614 0.2449 0.3073 0.0331  -0.0065 -0.0888 268 ILE   A O   
4023 C  CB  . ILE   A 268 ? 0.2485 0.2039 0.2770 0.0165  -0.0022 -0.0617 268 ILE   A CB  
4024 C  CG1 . ILE   A 268 ? 0.2816 0.2129 0.3067 0.0122  -0.0046 -0.0521 268 ILE   A CG1 
4025 C  CG2 . ILE   A 268 ? 0.2839 0.2461 0.3209 0.0182  -0.0047 -0.0765 268 ILE   A CG2 
4026 C  CD1 . ILE   A 268 ? 0.2810 0.2139 0.3029 0.0042  -0.0009 -0.0477 268 ILE   A CD1 
4038 N  N   . LEU   A 269 ? 0.2275 0.2288 0.2571 0.0227  0.0037  -0.0719 269 LEU   A N   
4039 C  CA  . LEU   A 269 ? 0.2164 0.2439 0.2488 0.0235  0.0063  -0.0829 269 LEU   A CA  
4040 C  C   . LEU   A 269 ? 0.2305 0.2637 0.2696 0.0301  0.0047  -0.0897 269 LEU   A C   
4041 O  O   . LEU   A 269 ? 0.2484 0.2957 0.2970 0.0346  0.0034  -0.1054 269 LEU   A O   
4042 C  CB  . LEU   A 269 ? 0.2050 0.2491 0.2274 0.0161  0.0118  -0.0745 269 LEU   A CB  
4043 C  CG  . LEU   A 269 ? 0.2011 0.2742 0.2229 0.0140  0.0152  -0.0830 269 LEU   A CG  
4044 C  CD1 . LEU   A 269 ? 0.2500 0.3350 0.2775 0.0147  0.0144  -0.0986 269 LEU   A CD1 
4045 C  CD2 . LEU   A 269 ? 0.2510 0.3349 0.2614 0.0057  0.0186  -0.0711 269 LEU   A CD2 
4057 N  N   . ALA   A 270 ? 0.2394 0.2630 0.2750 0.0312  0.0043  -0.0794 270 ALA   A N   
4058 C  CA  . ALA   A 270 ? 0.2012 0.2305 0.2437 0.0375  0.0022  -0.0852 270 ALA   A CA  
4059 C  C   . ALA   A 270 ? 0.2646 0.2822 0.3199 0.0467  -0.0057 -0.0970 270 ALA   A C   
4060 O  O   . ALA   A 270 ? 0.2949 0.3233 0.3601 0.0533  -0.0081 -0.1076 270 ALA   A O   
4061 C  CB  . ALA   A 270 ? 0.2442 0.2621 0.2801 0.0368  0.0023  -0.0713 270 ALA   A CB  
4067 N  N   . ASN   A 271 ? 0.2656 0.2612 0.3216 0.0470  -0.0104 -0.0955 271 ASN   A N   
4068 C  CA  . ASN   A 271 ? 0.3029 0.2816 0.3707 0.0551  -0.0199 -0.1048 271 ASN   A CA  
4069 C  C   . ASN   A 271 ? 0.3537 0.3394 0.4315 0.0570  -0.0217 -0.1211 271 ASN   A C   
4070 O  O   . ASN   A 271 ? 0.3857 0.3538 0.4741 0.0632  -0.0307 -0.1289 271 ASN   A O   
4071 C  CB  . ASN   A 271 ? 0.3261 0.2722 0.3874 0.0530  -0.0253 -0.0906 271 ASN   A CB  
4072 C  CG  . ASN   A 271 ? 0.3631 0.2994 0.4191 0.0549  -0.0276 -0.0795 271 ASN   A CG  
4073 O  OD1 . ASN   A 271 ? 0.3973 0.3290 0.4620 0.0632  -0.0350 -0.0852 271 ASN   A OD1 
4074 N  ND2 . ASN   A 271 ? 0.3287 0.2644 0.3716 0.0477  -0.0215 -0.0651 271 ASN   A ND2 
4081 N  N   . GLN   A 272 ? 0.2747 0.2849 0.3494 0.0517  -0.0142 -0.1266 272 GLN   A N   
4082 C  CA  . GLN   A 272 ? 0.2754 0.2979 0.3604 0.0541  -0.0156 -0.1453 272 GLN   A CA  
4083 C  C   . GLN   A 272 ? 0.3082 0.3482 0.4073 0.0618  -0.0187 -0.1599 272 GLN   A C   
4084 O  O   . GLN   A 272 ? 0.3228 0.3741 0.4217 0.0637  -0.0166 -0.1582 272 GLN   A O   
4085 C  CB  . GLN   A 272 ? 0.2832 0.3305 0.3593 0.0453  -0.0071 -0.1460 272 GLN   A CB  
4086 C  CG  . GLN   A 272 ? 0.2722 0.3053 0.3364 0.0369  -0.0051 -0.1307 272 GLN   A CG  
4087 C  CD  . GLN   A 272 ? 0.3482 0.3542 0.4175 0.0378  -0.0117 -0.1312 272 GLN   A CD  
4088 O  OE1 . GLN   A 272 ? 0.3962 0.4036 0.4756 0.0406  -0.0155 -0.1464 272 GLN   A OE1 
4089 N  NE2 . GLN   A 272 ? 0.4667 0.4481 0.5295 0.0350  -0.0134 -0.1151 272 GLN   A NE2 
4098 N  N   . PRO   A 273 ? 0.3171 0.3614 0.4288 0.0649  -0.0242 -0.1721 273 PRO   A N   
4099 C  CA  . PRO   A 273 ? 0.3232 0.3852 0.4500 0.0711  -0.0284 -0.1845 273 PRO   A CA  
4100 C  C   . PRO   A 273 ? 0.2507 0.3492 0.3744 0.0668  -0.0194 -0.1893 273 PRO   A C   
4101 O  O   . PRO   A 273 ? 0.3934 0.5098 0.5076 0.0589  -0.0114 -0.1894 273 PRO   A O   
4102 C  CB  . PRO   A 273 ? 0.3342 0.3973 0.4735 0.0732  -0.0341 -0.1973 273 PRO   A CB  
4103 C  CG  . PRO   A 273 ? 0.3536 0.3876 0.4853 0.0698  -0.0360 -0.1883 273 PRO   A CG  
4104 C  CD  . PRO   A 273 ? 0.3281 0.3627 0.4422 0.0625  -0.0269 -0.1765 273 PRO   A CD  
4112 N  N   . ASN   A 274 ? 0.3411 0.4494 0.4710 0.0707  -0.0208 -0.1913 274 ASN   A N   
4113 C  CA  . ASN   A 274 ? 0.5378 0.6820 0.6660 0.0653  -0.0129 -0.1960 274 ASN   A CA  
4114 C  C   . ASN   A 274 ? 0.4604 0.6058 0.5711 0.0585  -0.0043 -0.1814 274 ASN   A C   
4115 O  O   . ASN   A 274 ? 0.4899 0.6610 0.5980 0.0533  0.0015  -0.1821 274 ASN   A O   
4116 C  CB  . ASN   A 274 ? 0.5916 0.7655 0.7211 0.0589  -0.0081 -0.2073 274 ASN   A CB  
4117 C  CG  . ASN   A 274 ? 0.6952 0.9043 0.8304 0.0556  -0.0047 -0.2166 274 ASN   A CG  
4118 O  OD1 . ASN   A 274 ? 0.7860 1.0142 0.9086 0.0461  0.0037  -0.2102 274 ASN   A OD1 
4119 N  ND2 . ASN   A 274 ? 0.6769 0.8938 0.8308 0.0628  -0.0118 -0.2309 274 ASN   A ND2 
4126 N  N   . TRP   A 275 ? 0.2797 0.3993 0.3796 0.0578  -0.0038 -0.1689 275 TRP   A N   
4127 C  CA  . TRP   A 275 ? 0.2743 0.3951 0.3585 0.0516  0.0040  -0.1555 275 TRP   A CA  
4128 C  C   . TRP   A 275 ? 0.2820 0.3855 0.3666 0.0562  0.0004  -0.1452 275 TRP   A C   
4129 O  O   . TRP   A 275 ? 0.3033 0.3873 0.3984 0.0655  -0.0084 -0.1491 275 TRP   A O   
4130 C  CB  . TRP   A 275 ? 0.2722 0.3747 0.3436 0.0450  0.0051  -0.1422 275 TRP   A CB  
4131 C  CG  . TRP   A 275 ? 0.2330 0.3574 0.2978 0.0370  0.0107  -0.1467 275 TRP   A CG  
4132 C  CD1 . TRP   A 275 ? 0.2868 0.4215 0.3589 0.0384  0.0095  -0.1627 275 TRP   A CD1 
4133 C  CD2 . TRP   A 275 ? 0.2141 0.3508 0.2631 0.0257  0.0171  -0.1337 275 TRP   A CD2 
4134 N  NE1 . TRP   A 275 ? 0.2494 0.4044 0.3104 0.0288  0.0153  -0.1615 275 TRP   A NE1 
4135 C  CE2 . TRP   A 275 ? 0.2045 0.3601 0.2510 0.0209  0.0196  -0.1432 275 TRP   A CE2 
4136 C  CE3 . TRP   A 275 ? 0.2325 0.3657 0.2698 0.0195  0.0201  -0.1156 275 TRP   A CE3 
4137 C  CZ2 . TRP   A 275 ? 0.2257 0.3959 0.2576 0.0100  0.0242  -0.1336 275 TRP   A CZ2 
4138 C  CZ3 . TRP   A 275 ? 0.2372 0.3833 0.2614 0.0091  0.0242  -0.1066 275 TRP   A CZ3 
4139 C  CH2 . TRP   A 275 ? 0.2497 0.4138 0.2708 0.0044  0.0260  -0.1148 275 TRP   A CH2 
4150 N  N   . ASN   A 276 ? 0.2465 0.3565 0.3201 0.0491  0.0059  -0.1317 276 ASN   A N   
4151 C  CA  . ASN   A 276 ? 0.2280 0.3210 0.2995 0.0517  0.0028  -0.1198 276 ASN   A CA  
4152 C  C   . ASN   A 276 ? 0.2148 0.3016 0.2696 0.0418  0.0080  -0.1004 276 ASN   A C   
4153 O  O   . ASN   A 276 ? 0.2117 0.3066 0.2579 0.0339  0.0128  -0.0965 276 ASN   A O   
4154 C  CB  . ASN   A 276 ? 0.2254 0.3382 0.3073 0.0561  0.0027  -0.1294 276 ASN   A CB  
4155 C  CG  . ASN   A 276 ? 0.2646 0.4128 0.3435 0.0473  0.0117  -0.1337 276 ASN   A CG  
4156 O  OD1 . ASN   A 276 ? 0.2680 0.4208 0.3327 0.0366  0.0176  -0.1221 276 ASN   A OD1 
4157 N  ND2 . ASN   A 276 ? 0.3429 0.5144 0.4342 0.0500  0.0111  -0.1481 276 ASN   A ND2 
4164 N  N   . LEU   A 277 ? 0.2520 0.3244 0.3032 0.0428  0.0061  -0.0892 277 LEU   A N   
4165 C  CA  . LEU   A 277 ? 0.2501 0.3151 0.2880 0.0349  0.0098  -0.0722 277 LEU   A CA  
4166 C  C   . LEU   A 277 ? 0.2315 0.3211 0.2639 0.0259  0.0165  -0.0706 277 LEU   A C   
4167 O  O   . LEU   A 277 ? 0.2058 0.2935 0.2281 0.0184  0.0194  -0.0605 277 LEU   A O   
4168 C  CB  . LEU   A 277 ? 0.2405 0.2910 0.2771 0.0379  0.0066  -0.0639 277 LEU   A CB  
4169 C  CG  . LEU   A 277 ? 0.2989 0.3418 0.3239 0.0308  0.0099  -0.0484 277 LEU   A CG  
4170 C  CD1 . LEU   A 277 ? 0.4486 0.4675 0.4699 0.0339  0.0057  -0.0398 277 LEU   A CD1 
4171 C  CD2 . LEU   A 277 ? 0.3664 0.4280 0.3899 0.0254  0.0139  -0.0463 277 LEU   A CD2 
4183 N  N   . ARG   A 278 ? 0.2045 0.3173 0.2435 0.0260  0.0185  -0.0798 278 ARG   A N   
4184 C  CA  . ARG   A 278 ? 0.2361 0.3723 0.2685 0.0154  0.0246  -0.0767 278 ARG   A CA  
4185 C  C   . ARG   A 278 ? 0.2057 0.3547 0.2320 0.0088  0.0279  -0.0790 278 ARG   A C   
4186 O  O   . ARG   A 278 ? 0.2169 0.3697 0.2317 -0.0010 0.0306  -0.0678 278 ARG   A O   
4187 C  CB  . ARG   A 278 ? 0.2385 0.4006 0.2803 0.0159  0.0267  -0.0883 278 ARG   A CB  
4188 C  CG  . ARG   A 278 ? 0.2974 0.4844 0.3310 0.0027  0.0331  -0.0840 278 ARG   A CG  
4189 C  CD  . ARG   A 278 ? 0.4843 0.6969 0.5262 0.0008  0.0359  -0.0928 278 ARG   A CD  
4190 N  NE  . ARG   A 278 ? 0.4617 0.6955 0.4931 -0.0144 0.0417  -0.0859 278 ARG   A NE  
4191 C  CZ  . ARG   A 278 ? 0.5239 0.7825 0.5587 -0.0211 0.0452  -0.0905 278 ARG   A CZ  
4192 N  NH1 . ARG   A 278 ? 0.5310 0.7948 0.5797 -0.0135 0.0430  -0.1005 278 ARG   A NH1 
4193 N  NH2 . ARG   A 278 ? 0.6336 0.9052 0.6566 -0.0361 0.0475  -0.0826 278 ARG   A NH2 
4207 N  N   . MET   A 279 ? 0.2129 0.3682 0.2469 0.0141  0.0268  -0.0936 279 MET   A N   
4208 C  CA  A MET   A 279 ? 0.2408 0.4097 0.2688 0.0078  0.0297  -0.0971 279 MET   A CA  
4209 C  CA  B MET   A 279 ? 0.2414 0.4103 0.2694 0.0078  0.0297  -0.0971 279 MET   A CA  
4210 C  C   . MET   A 279 ? 0.2161 0.3633 0.2339 0.0046  0.0280  -0.0828 279 MET   A C   
4211 O  O   . MET   A 279 ? 0.2089 0.3652 0.2161 -0.0044 0.0303  -0.0761 279 MET   A O   
4212 C  CB  A MET   A 279 ? 0.2341 0.4124 0.2744 0.0153  0.0281  -0.1174 279 MET   A CB  
4213 C  CB  B MET   A 279 ? 0.2331 0.4108 0.2736 0.0155  0.0279  -0.1172 279 MET   A CB  
4214 C  CG  A MET   A 279 ? 0.2702 0.4833 0.3177 0.0134  0.0318  -0.1333 279 MET   A CG  
4215 C  CG  B MET   A 279 ? 0.2600 0.4689 0.3101 0.0160  0.0310  -0.1333 279 MET   A CG  
4216 S  SD  A MET   A 279 ? 0.3456 0.5618 0.4105 0.0220  0.0256  -0.1535 279 MET   A SD  
4217 S  SD  B MET   A 279 ? 0.3650 0.5782 0.4315 0.0238  0.0249  -0.1530 279 MET   A SD  
4218 C  CE  A MET   A 279 ? 0.3018 0.4989 0.3827 0.0360  0.0181  -0.1583 279 MET   A CE  
4219 C  CE  B MET   A 279 ? 0.3510 0.5728 0.4053 0.0144  0.0283  -0.1513 279 MET   A CE  
4238 N  N   . ALA   A 280 ? 0.2107 0.3299 0.2314 0.0115  0.0236  -0.0783 280 ALA   A N   
4239 C  CA  . ALA   A 280 ? 0.2196 0.3200 0.2324 0.0085  0.0224  -0.0660 280 ALA   A CA  
4240 C  C   . ALA   A 280 ? 0.2111 0.3103 0.2140 0.0012  0.0240  -0.0504 280 ALA   A C   
4241 O  O   . ALA   A 280 ? 0.2118 0.3117 0.2072 -0.0049 0.0243  -0.0428 280 ALA   A O   
4242 C  CB  . ALA   A 280 ? 0.2405 0.3132 0.2578 0.0157  0.0179  -0.0637 280 ALA   A CB  
4248 N  N   . PHE   A 281 ? 0.1907 0.2881 0.1946 0.0020  0.0243  -0.0460 281 PHE   A N   
4249 C  CA  . PHE   A 281 ? 0.2055 0.3001 0.2017 -0.0046 0.0249  -0.0321 281 PHE   A CA  
4250 C  C   . PHE   A 281 ? 0.1945 0.3110 0.1834 -0.0147 0.0274  -0.0299 281 PHE   A C   
4251 O  O   . PHE   A 281 ? 0.2093 0.3213 0.1903 -0.0212 0.0261  -0.0179 281 PHE   A O   
4252 C  CB  . PHE   A 281 ? 0.2176 0.3062 0.2171 -0.0017 0.0243  -0.0293 281 PHE   A CB  
4253 C  CG  . PHE   A 281 ? 0.1887 0.2665 0.1823 -0.0062 0.0234  -0.0155 281 PHE   A CG  
4254 C  CD1 . PHE   A 281 ? 0.2208 0.2802 0.2115 -0.0053 0.0214  -0.0077 281 PHE   A CD1 
4255 C  CD2 . PHE   A 281 ? 0.2163 0.3027 0.2088 -0.0113 0.0244  -0.0114 281 PHE   A CD2 
4256 C  CE1 . PHE   A 281 ? 0.2411 0.2913 0.2288 -0.0084 0.0200  0.0029  281 PHE   A CE1 
4257 C  CE2 . PHE   A 281 ? 0.2126 0.2875 0.2012 -0.0149 0.0225  0.0002  281 PHE   A CE2 
4258 C  CZ  . PHE   A 281 ? 0.2141 0.2708 0.2007 -0.0129 0.0201  0.0068  281 PHE   A CZ  
4268 N  N   . ASP   A 282 ? 0.1978 0.3385 0.1892 -0.0166 0.0305  -0.0416 282 ASP   A N   
4269 C  CA  . ASP   A 282 ? 0.1998 0.3638 0.1822 -0.0282 0.0332  -0.0394 282 ASP   A CA  
4270 C  C   . ASP   A 282 ? 0.2180 0.3779 0.1918 -0.0326 0.0310  -0.0329 282 ASP   A C   
4271 O  O   . ASP   A 282 ? 0.2112 0.3745 0.1744 -0.0422 0.0298  -0.0209 282 ASP   A O   
4272 C  CB  . ASP   A 282 ? 0.2060 0.3997 0.1933 -0.0291 0.0374  -0.0565 282 ASP   A CB  
4273 C  CG  . ASP   A 282 ? 0.2992 0.5054 0.2948 -0.0275 0.0398  -0.0633 282 ASP   A CG  
4274 O  OD1 . ASP   A 282 ? 0.2878 0.4840 0.2822 -0.0292 0.0389  -0.0528 282 ASP   A OD1 
4275 O  OD2 . ASP   A 282 ? 0.2924 0.5209 0.2966 -0.0247 0.0426  -0.0806 282 ASP   A OD2 
4280 N  N   . VAL   A 283 ? 0.1953 0.3481 0.1737 -0.0259 0.0298  -0.0409 283 VAL   A N   
4281 C  CA  . VAL   A 283 ? 0.2161 0.3663 0.1879 -0.0294 0.0275  -0.0366 283 VAL   A CA  
4282 C  C   . VAL   A 283 ? 0.2093 0.3382 0.1771 -0.0304 0.0235  -0.0203 283 VAL   A C   
4283 O  O   . VAL   A 283 ? 0.2103 0.3416 0.1694 -0.0375 0.0207  -0.0108 283 VAL   A O   
4284 C  CB  . VAL   A 283 ? 0.1888 0.3337 0.1686 -0.0217 0.0268  -0.0492 283 VAL   A CB  
4285 C  CG1 . VAL   A 283 ? 0.2101 0.3484 0.1850 -0.0242 0.0238  -0.0441 283 VAL   A CG1 
4286 C  CG2 . VAL   A 283 ? 0.2275 0.3961 0.2123 -0.0208 0.0299  -0.0671 283 VAL   A CG2 
4296 N  N   . MET   A 284 ? 0.2080 0.3160 0.1823 -0.0233 0.0225  -0.0176 284 MET   A N   
4297 C  CA  . MET   A 284 ? 0.1830 0.2721 0.1558 -0.0232 0.0191  -0.0048 284 MET   A CA  
4298 C  C   . MET   A 284 ? 0.2140 0.3062 0.1803 -0.0307 0.0173  0.0069  284 MET   A C   
4299 O  O   . MET   A 284 ? 0.1952 0.2803 0.1577 -0.0340 0.0129  0.0169  284 MET   A O   
4300 C  CB  . MET   A 284 ? 0.1757 0.2464 0.1559 -0.0151 0.0194  -0.0063 284 MET   A CB  
4301 C  CG  . MET   A 284 ? 0.2205 0.2824 0.2064 -0.0088 0.0195  -0.0147 284 MET   A CG  
4302 S  SD  . MET   A 284 ? 0.2135 0.2709 0.1986 -0.0104 0.0174  -0.0134 284 MET   A SD  
4303 C  CE  . MET   A 284 ? 0.2118 0.2560 0.2044 -0.0039 0.0176  -0.0227 284 MET   A CE  
4313 N  N   . VAL   A 285 ? 0.2015 0.3036 0.1674 -0.0335 0.0200  0.0056  285 VAL   A N   
4314 C  CA  . VAL   A 285 ? 0.2057 0.3093 0.1657 -0.0418 0.0179  0.0173  285 VAL   A CA  
4315 C  C   . VAL   A 285 ? 0.2088 0.3257 0.1579 -0.0523 0.0157  0.0237  285 VAL   A C   
4316 O  O   . VAL   A 285 ? 0.2283 0.3363 0.1721 -0.0577 0.0100  0.0367  285 VAL   A O   
4317 C  CB  . VAL   A 285 ? 0.1898 0.3042 0.1524 -0.0435 0.0218  0.0132  285 VAL   A CB  
4318 C  CG1 . VAL   A 285 ? 0.2128 0.3336 0.1677 -0.0553 0.0201  0.0246  285 VAL   A CG1 
4319 C  CG2 . VAL   A 285 ? 0.2149 0.3129 0.1864 -0.0339 0.0219  0.0106  285 VAL   A CG2 
4329 N  N   . LYS   A 286 ? 0.2183 0.3567 0.1641 -0.0554 0.0193  0.0142  286 LYS   A N   
4330 C  CA  . LYS   A 286 ? 0.2353 0.3892 0.1686 -0.0666 0.0174  0.0198  286 LYS   A CA  
4331 C  C   . LYS   A 286 ? 0.2049 0.3457 0.1357 -0.0650 0.0109  0.0267  286 LYS   A C   
4332 O  O   . LYS   A 286 ? 0.2348 0.3756 0.1557 -0.0736 0.0050  0.0392  286 LYS   A O   
4333 C  CB  . LYS   A 286 ? 0.2415 0.4237 0.1730 -0.0694 0.0234  0.0051  286 LYS   A CB  
4334 C  CG  . LYS   A 286 ? 0.3360 0.5377 0.2529 -0.0819 0.0220  0.0096  286 LYS   A CG  
4335 C  CD  . LYS   A 286 ? 0.3953 0.6241 0.3147 -0.0869 0.0265  -0.0030 286 LYS   A CD  
4336 C  CE  . LYS   A 286 ? 0.4568 0.6969 0.3662 -0.1006 0.0222  0.0064  286 LYS   A CE  
4337 N  NZ  . LYS   A 286 ? 0.5594 0.7921 0.4647 -0.1090 0.0187  0.0209  286 LYS   A NZ  
4351 N  N   . ALA   A 287 ? 0.2118 0.3407 0.1518 -0.0546 0.0111  0.0192  287 ALA   A N   
4352 C  CA  . ALA   A 287 ? 0.2152 0.3319 0.1553 -0.0525 0.0050  0.0248  287 ALA   A CA  
4353 C  C   . ALA   A 287 ? 0.2365 0.3340 0.1781 -0.0523 -0.0014 0.0387  287 ALA   A C   
4354 O  O   . ALA   A 287 ? 0.2292 0.3228 0.1662 -0.0561 -0.0088 0.0483  287 ALA   A O   
4355 C  CB  . ALA   A 287 ? 0.2322 0.3400 0.1828 -0.0424 0.0072  0.0140  287 ALA   A CB  
4361 N  N   . ASN   A 288 ? 0.2280 0.3132 0.1764 -0.0476 0.0006  0.0391  288 ASN   A N   
4362 C  CA  . ASN   A 288 ? 0.2191 0.2868 0.1705 -0.0470 -0.0054 0.0500  288 ASN   A CA  
4363 C  C   . ASN   A 288 ? 0.2286 0.3004 0.1697 -0.0582 -0.0112 0.0629  288 ASN   A C   
4364 O  O   . ASN   A 288 ? 0.2523 0.3124 0.1932 -0.0596 -0.0201 0.0733  288 ASN   A O   
4365 C  CB  . ASN   A 288 ? 0.2113 0.2694 0.1700 -0.0415 -0.0014 0.0468  288 ASN   A CB  
4366 C  CG  . ASN   A 288 ? 0.2196 0.2580 0.1856 -0.0368 -0.0065 0.0527  288 ASN   A CG  
4367 O  OD1 . ASN   A 288 ? 0.2449 0.2765 0.2102 -0.0397 -0.0142 0.0619  288 ASN   A OD1 
4368 N  ND2 . ASN   A 288 ? 0.2317 0.2616 0.2050 -0.0298 -0.0026 0.0469  288 ASN   A ND2 
4375 N  N   . MET   A 289 ? 0.2217 0.3111 0.1546 -0.0667 -0.0068 0.0621  289 MET   A N   
4376 C  CA  A MET   A 289 ? 0.2692 0.3629 0.1911 -0.0796 -0.0117 0.0754  289 MET   A CA  
4377 C  CA  B MET   A 289 ? 0.2695 0.3631 0.1914 -0.0796 -0.0117 0.0754  289 MET   A CA  
4378 C  C   . MET   A 289 ? 0.2911 0.3920 0.2016 -0.0874 -0.0182 0.0831  289 MET   A C   
4379 O  O   . MET   A 289 ? 0.2807 0.3718 0.1874 -0.0935 -0.0274 0.0959  289 MET   A O   
4380 C  CB  A MET   A 289 ? 0.2745 0.3888 0.1914 -0.0874 -0.0039 0.0708  289 MET   A CB  
4381 C  CB  B MET   A 289 ? 0.2751 0.3890 0.1922 -0.0874 -0.0039 0.0710  289 MET   A CB  
4382 C  CG  A MET   A 289 ? 0.2389 0.3459 0.1652 -0.0827 0.0000  0.0673  289 MET   A CG  
4383 C  CG  B MET   A 289 ? 0.2404 0.3461 0.1669 -0.0827 -0.0003 0.0679  289 MET   A CG  
4384 S  SD  A MET   A 289 ? 0.3336 0.4692 0.2565 -0.0910 0.0092  0.0590  289 MET   A SD  
4385 S  SD  B MET   A 289 ? 0.2909 0.4216 0.2142 -0.0922 0.0077  0.0626  289 MET   A SD  
4386 C  CE  A MET   A 289 ? 0.3122 0.4463 0.2283 -0.1048 0.0014  0.0722  289 MET   A CE  
4387 C  CE  B MET   A 289 ? 0.2492 0.4051 0.1729 -0.0883 0.0158  0.0447  289 MET   A CE  
4406 N  N   . ASP   A 290 ? 0.2468 0.3631 0.1547 -0.0859 -0.0143 0.0731  290 ASP   A N   
4407 C  CA  . ASP   A 290 ? 0.2878 0.4182 0.1832 -0.0952 -0.0185 0.0776  290 ASP   A CA  
4408 C  C   . ASP   A 290 ? 0.2735 0.4003 0.1698 -0.0898 -0.0238 0.0762  290 ASP   A C   
4409 O  O   . ASP   A 290 ? 0.3193 0.4525 0.2065 -0.0970 -0.0302 0.0827  290 ASP   A O   
4410 C  CB  . ASP   A 290 ? 0.3076 0.4656 0.1998 -0.1004 -0.0094 0.0647  290 ASP   A CB  
4411 C  CG  . ASP   A 290 ? 0.3724 0.5384 0.2647 -0.1083 -0.0063 0.0659  290 ASP   A CG  
4412 O  OD1 . ASP   A 290 ? 0.3729 0.5227 0.2667 -0.1105 -0.0113 0.0770  290 ASP   A OD1 
4413 O  OD2 . ASP   A 290 ? 0.4704 0.6593 0.3630 -0.1115 0.0010  0.0540  290 ASP   A OD2 
4418 N  N   . TYR   A 291 ? 0.2762 0.3916 0.1870 -0.0767 -0.0214 0.0663  291 TYR   A N   
4419 C  CA  . TYR   A 291 ? 0.2593 0.3751 0.1729 -0.0721 -0.0249 0.0617  291 TYR   A CA  
4420 C  C   . TYR   A 291 ? 0.2545 0.3493 0.1825 -0.0614 -0.0295 0.0622  291 TYR   A C   
4421 O  O   . TYR   A 291 ? 0.2810 0.3726 0.2098 -0.0605 -0.0377 0.0662  291 TYR   A O   
4422 C  CB  . TYR   A 291 ? 0.2705 0.4025 0.1861 -0.0692 -0.0157 0.0445  291 TYR   A CB  
4423 C  CG  . TYR   A 291 ? 0.2644 0.4224 0.1663 -0.0800 -0.0120 0.0417  291 TYR   A CG  
4424 C  CD1 . TYR   A 291 ? 0.3237 0.4944 0.2117 -0.0896 -0.0181 0.0485  291 TYR   A CD1 
4425 C  CD2 . TYR   A 291 ? 0.2544 0.4255 0.1567 -0.0815 -0.0030 0.0327  291 TYR   A CD2 
4426 C  CE1 . TYR   A 291 ? 0.3215 0.5156 0.2008 -0.0993 -0.0140 0.0445  291 TYR   A CE1 
4427 C  CE2 . TYR   A 291 ? 0.2746 0.4728 0.1656 -0.0919 0.0010  0.0285  291 TYR   A CE2 
4428 C  CZ  . TYR   A 291 ? 0.3319 0.5392 0.2153 -0.0999 -0.0044 0.0337  291 TYR   A CZ  
4429 O  OH  . TYR   A 291 ? 0.3562 0.5866 0.2370 -0.1085 -0.0006 0.0278  291 TYR   A OH  
4439 N  N   . TRP   A 292 ? 0.2366 0.3189 0.1758 -0.0535 -0.0245 0.0573  292 TRP   A N   
4440 C  CA  . TRP   A 292 ? 0.2343 0.3005 0.1871 -0.0442 -0.0273 0.0556  292 TRP   A CA  
4441 C  C   . TRP   A 292 ? 0.2351 0.2888 0.1902 -0.0446 -0.0388 0.0680  292 TRP   A C   
4442 O  O   . TRP   A 292 ? 0.2792 0.3280 0.2287 -0.0501 -0.0431 0.0784  292 TRP   A O   
4443 C  CB  . TRP   A 292 ? 0.2511 0.3077 0.2128 -0.0375 -0.0199 0.0494  292 TRP   A CB  
4444 C  CG  . TRP   A 292 ? 0.2177 0.2806 0.1817 -0.0340 -0.0109 0.0365  292 TRP   A CG  
4445 C  CD1 . TRP   A 292 ? 0.2119 0.2863 0.1742 -0.0346 -0.0087 0.0282  292 TRP   A CD1 
4446 C  CD2 . TRP   A 292 ? 0.1981 0.2551 0.1671 -0.0293 -0.0042 0.0306  292 TRP   A CD2 
4447 N  NE1 . TRP   A 292 ? 0.2018 0.2759 0.1686 -0.0302 -0.0015 0.0174  292 TRP   A NE1 
4448 C  CE2 . TRP   A 292 ? 0.2013 0.2648 0.1718 -0.0269 0.0011  0.0193  292 TRP   A CE2 
4449 C  CE3 . TRP   A 292 ? 0.2197 0.2662 0.1922 -0.0268 -0.0029 0.0336  292 TRP   A CE3 
4450 C  CZ2 . TRP   A 292 ? 0.2161 0.2745 0.1912 -0.0221 0.0066  0.0121  292 TRP   A CZ2 
4451 C  CZ3 . TRP   A 292 ? 0.2152 0.2585 0.1912 -0.0223 0.0032  0.0263  292 TRP   A CZ3 
4452 C  CH2 . TRP   A 292 ? 0.1823 0.2309 0.1595 -0.0199 0.0075  0.0162  292 TRP   A CH2 
4463 N  N   . THR   A 293 ? 0.2403 0.2887 0.2048 -0.0388 -0.0444 0.0663  293 THR   A N   
4464 C  CA  . THR   A 293 ? 0.2406 0.2774 0.2107 -0.0371 -0.0571 0.0757  293 THR   A CA  
4465 C  C   . THR   A 293 ? 0.2370 0.2604 0.2245 -0.0273 -0.0567 0.0704  293 THR   A C   
4466 O  O   . THR   A 293 ? 0.2338 0.2583 0.2277 -0.0224 -0.0469 0.0598  293 THR   A O   
4467 C  CB  . THR   A 293 ? 0.3200 0.3642 0.2887 -0.0381 -0.0654 0.0770  293 THR   A CB  
4468 O  OG1 . THR   A 293 ? 0.3294 0.3757 0.3114 -0.0302 -0.0616 0.0650  293 THR   A OG1 
4469 C  CG2 . THR   A 293 ? 0.3131 0.3749 0.2642 -0.0479 -0.0635 0.0787  293 THR   A CG2 
4477 N  N   . PRO   A 294 ? 0.2344 0.2449 0.2296 -0.0246 -0.0674 0.0774  294 PRO   A N   
4478 C  CA  . PRO   A 294 ? 0.2494 0.2492 0.2610 -0.0158 -0.0660 0.0708  294 PRO   A CA  
4479 C  C   . PRO   A 294 ? 0.2016 0.2070 0.2262 -0.0085 -0.0616 0.0584  294 PRO   A C   
4480 O  O   . PRO   A 294 ? 0.2092 0.2118 0.2423 -0.0036 -0.0542 0.0502  294 PRO   A O   
4481 C  CB  . PRO   A 294 ? 0.2465 0.2324 0.2647 -0.0144 -0.0809 0.0802  294 PRO   A CB  
4482 C  CG  . PRO   A 294 ? 0.3043 0.2906 0.3047 -0.0254 -0.0870 0.0946  294 PRO   A CG  
4483 C  CD  . PRO   A 294 ? 0.2495 0.2535 0.2384 -0.0302 -0.0815 0.0918  294 PRO   A CD  
4491 N  N   . TYR   A 295 ? 0.2355 0.2498 0.2613 -0.0085 -0.0658 0.0567  295 TYR   A N   
4492 C  CA  . TYR   A 295 ? 0.2286 0.2499 0.2670 -0.0031 -0.0615 0.0448  295 TYR   A CA  
4493 C  C   . TYR   A 295 ? 0.2267 0.2594 0.2567 -0.0071 -0.0518 0.0385  295 TYR   A C   
4494 O  O   . TYR   A 295 ? 0.2616 0.3024 0.2987 -0.0055 -0.0510 0.0312  295 TYR   A O   
4495 C  CB  . TYR   A 295 ? 0.2500 0.2730 0.3005 0.0011  -0.0743 0.0451  295 TYR   A CB  
4496 C  CG  . TYR   A 295 ? 0.2767 0.2872 0.3397 0.0069  -0.0838 0.0480  295 TYR   A CG  
4497 C  CD1 . TYR   A 295 ? 0.2688 0.2785 0.3497 0.0144  -0.0804 0.0371  295 TYR   A CD1 
4498 C  CD2 . TYR   A 295 ? 0.2299 0.2292 0.2864 0.0041  -0.0958 0.0613  295 TYR   A CD2 
4499 C  CE1 . TYR   A 295 ? 0.2465 0.2454 0.3402 0.0203  -0.0888 0.0375  295 TYR   A CE1 
4500 C  CE2 . TYR   A 295 ? 0.2521 0.2377 0.3211 0.0095  -0.1053 0.0634  295 TYR   A CE2 
4501 C  CZ  . TYR   A 295 ? 0.2790 0.2647 0.3674 0.0184  -0.1018 0.0505  295 TYR   A CZ  
4502 O  OH  . TYR   A 295 ? 0.2921 0.2652 0.3950 0.0246  -0.1114 0.0502  295 TYR   A OH  
4512 N  N   . SER   A 296 ? 0.2202 0.2539 0.2369 -0.0119 -0.0445 0.0403  296 SER   A N   
4513 C  CA  . SER   A 296 ? 0.1988 0.2424 0.2086 -0.0151 -0.0363 0.0335  296 SER   A CA  
4514 C  C   . SER   A 296 ? 0.2200 0.2643 0.2404 -0.0114 -0.0296 0.0226  296 SER   A C   
4515 O  O   . SER   A 296 ? 0.2204 0.2576 0.2485 -0.0078 -0.0253 0.0196  296 SER   A O   
4516 C  CB  . SER   A 296 ? 0.2141 0.2572 0.2130 -0.0185 -0.0288 0.0343  296 SER   A CB  
4517 O  OG  . SER   A 296 ? 0.2261 0.2788 0.2193 -0.0210 -0.0226 0.0270  296 SER   A OG  
4523 N  N   . THR   A 297 ? 0.2228 0.2765 0.2428 -0.0134 -0.0284 0.0166  297 THR   A N   
4524 C  CA  . THR   A 297 ? 0.2143 0.2684 0.2408 -0.0126 -0.0206 0.0068  297 THR   A CA  
4525 C  C   . THR   A 297 ? 0.1926 0.2441 0.2101 -0.0147 -0.0126 0.0039  297 THR   A C   
4526 O  O   . THR   A 297 ? 0.2181 0.2722 0.2254 -0.0170 -0.0129 0.0075  297 THR   A O   
4527 C  CB  . THR   A 297 ? 0.2367 0.3012 0.2673 -0.0144 -0.0229 0.0008  297 THR   A CB  
4528 O  OG1 . THR   A 297 ? 0.2450 0.3179 0.2641 -0.0185 -0.0256 0.0020  297 THR   A OG1 
4529 C  CG2 . THR   A 297 ? 0.2778 0.3462 0.3198 -0.0114 -0.0317 0.0020  297 THR   A CG2 
4537 N  N   . PHE   A 298 ? 0.2049 0.2522 0.2267 -0.0145 -0.0059 -0.0030 298 PHE   A N   
4538 C  CA  . PHE   A 298 ? 0.1775 0.2215 0.1928 -0.0156 -0.0003 -0.0069 298 PHE   A CA  
4539 C  C   . PHE   A 298 ? 0.2053 0.2599 0.2145 -0.0184 -0.0018 -0.0110 298 PHE   A C   
4540 O  O   . PHE   A 298 ? 0.1992 0.2561 0.2014 -0.0190 0.0003  -0.0123 298 PHE   A O   
4541 C  CB  . PHE   A 298 ? 0.2027 0.2390 0.2234 -0.0160 0.0051  -0.0127 298 PHE   A CB  
4542 C  CG  . PHE   A 298 ? 0.2120 0.2395 0.2364 -0.0144 0.0082  -0.0099 298 PHE   A CG  
4543 C  CD1 . PHE   A 298 ? 0.1989 0.2209 0.2194 -0.0118 0.0086  -0.0045 298 PHE   A CD1 
4544 C  CD2 . PHE   A 298 ? 0.2275 0.2537 0.2592 -0.0164 0.0110  -0.0134 298 PHE   A CD2 
4545 C  CE1 . PHE   A 298 ? 0.2082 0.2236 0.2318 -0.0106 0.0116  -0.0032 298 PHE   A CE1 
4546 C  CE2 . PHE   A 298 ? 0.2322 0.2532 0.2664 -0.0159 0.0144  -0.0118 298 PHE   A CE2 
4547 C  CZ  . PHE   A 298 ? 0.2009 0.2164 0.2309 -0.0127 0.0146  -0.0070 298 PHE   A CZ  
4557 N  N   . ASP   A 299 ? 0.2089 0.2718 0.2216 -0.0203 -0.0052 -0.0147 299 ASP   A N   
4558 C  CA  . ASP   A 299 ? 0.2181 0.2932 0.2249 -0.0234 -0.0069 -0.0199 299 ASP   A CA  
4559 C  C   . ASP   A 299 ? 0.2173 0.3016 0.2132 -0.0257 -0.0107 -0.0132 299 ASP   A C   
4560 O  O   . ASP   A 299 ? 0.2454 0.3386 0.2335 -0.0281 -0.0086 -0.0173 299 ASP   A O   
4561 C  CB  . ASP   A 299 ? 0.2029 0.2857 0.2160 -0.0252 -0.0107 -0.0246 299 ASP   A CB  
4562 C  CG  . ASP   A 299 ? 0.2641 0.3404 0.2862 -0.0257 -0.0064 -0.0329 299 ASP   A CG  
4563 O  OD1 . ASP   A 299 ? 0.2462 0.3115 0.2684 -0.0248 -0.0011 -0.0351 299 ASP   A OD1 
4564 O  OD2 . ASP   A 299 ? 0.2905 0.3724 0.3201 -0.0273 -0.0089 -0.0366 299 ASP   A OD2 
4569 N  N   . GLU   A 300 ? 0.2227 0.3059 0.2182 -0.0255 -0.0167 -0.0032 300 GLU   A N   
4570 C  CA  . GLU   A 300 ? 0.2016 0.2915 0.1855 -0.0294 -0.0211 0.0055  300 GLU   A CA  
4571 C  C   . GLU   A 300 ? 0.2356 0.3224 0.2135 -0.0299 -0.0154 0.0070  300 GLU   A C   
4572 O  O   . GLU   A 300 ? 0.2396 0.3374 0.2066 -0.0350 -0.0152 0.0086  300 GLU   A O   
4573 C  CB  . GLU   A 300 ? 0.2267 0.3112 0.2136 -0.0284 -0.0301 0.0163  300 GLU   A CB  
4574 C  CG  . GLU   A 300 ? 0.2438 0.3359 0.2342 -0.0289 -0.0381 0.0157  300 GLU   A CG  
4575 C  CD  . GLU   A 300 ? 0.3512 0.4360 0.3506 -0.0251 -0.0476 0.0233  300 GLU   A CD  
4576 O  OE1 . GLU   A 300 ? 0.2679 0.3409 0.2714 -0.0219 -0.0477 0.0285  300 GLU   A OE1 
4577 O  OE2 . GLU   A 300 ? 0.3621 0.4534 0.3655 -0.0249 -0.0557 0.0232  300 GLU   A OE2 
4584 N  N   . GLY   A 301 ? 0.2177 0.2914 0.2024 -0.0253 -0.0107 0.0060  301 GLY   A N   
4585 C  CA  . GLY   A 301 ? 0.2154 0.2868 0.1959 -0.0252 -0.0058 0.0065  301 GLY   A CA  
4586 C  C   . GLY   A 301 ? 0.2235 0.3045 0.2007 -0.0262 -0.0007 -0.0039 301 GLY   A C   
4587 O  O   . GLY   A 301 ? 0.2089 0.2969 0.1803 -0.0282 0.0018  -0.0042 301 GLY   A O   
4591 N  N   . GLY   A 302 ? 0.2117 0.2939 0.1938 -0.0249 0.0004  -0.0134 302 GLY   A N   
4592 C  CA  . GLY   A 302 ? 0.2133 0.3050 0.1943 -0.0253 0.0039  -0.0252 302 GLY   A CA  
4593 C  C   . GLY   A 302 ? 0.2232 0.3359 0.1943 -0.0312 0.0023  -0.0266 302 GLY   A C   
4594 O  O   . GLY   A 302 ? 0.2194 0.3439 0.1873 -0.0323 0.0059  -0.0338 302 GLY   A O   
4598 N  N   . CYS   A 303 ? 0.2534 0.3725 0.2196 -0.0353 -0.0033 -0.0201 303 CYS   A N   
4599 C  CA  . CYS   A 303 ? 0.2662 0.4055 0.2199 -0.0428 -0.0055 -0.0186 303 CYS   A CA  
4600 C  C   . CYS   A 303 ? 0.2496 0.3935 0.1949 -0.0468 -0.0037 -0.0111 303 CYS   A C   
4601 O  O   . CYS   A 303 ? 0.2464 0.4093 0.1834 -0.0523 -0.0008 -0.0159 303 CYS   A O   
4602 C  CB  . CYS   A 303 ? 0.2743 0.4160 0.2237 -0.0463 -0.0139 -0.0096 303 CYS   A CB  
4603 S  SG  . CYS   A 303 ? 0.2897 0.4268 0.2507 -0.0423 -0.0170 -0.0168 303 CYS   A SG  
4608 N  N   . GLY   A 304 ? 0.2288 0.3569 0.1764 -0.0448 -0.0055 0.0003  304 GLY   A N   
4609 C  CA  . GLY   A 304 ? 0.2449 0.3758 0.1856 -0.0490 -0.0040 0.0076  304 GLY   A CA  
4610 C  C   . GLY   A 304 ? 0.2243 0.3617 0.1680 -0.0468 0.0040  -0.0033 304 GLY   A C   
4611 O  O   . GLY   A 304 ? 0.2341 0.3868 0.1704 -0.0529 0.0067  -0.0033 304 GLY   A O   
4615 N  N   . MET   A 305 ? 0.2091 0.3357 0.1641 -0.0384 0.0073  -0.0129 305 MET   A N   
4616 C  CA  . MET   A 305 ? 0.2010 0.3320 0.1611 -0.0347 0.0130  -0.0245 305 MET   A CA  
4617 C  C   . MET   A 305 ? 0.1812 0.3364 0.1377 -0.0383 0.0155  -0.0374 305 MET   A C   
4618 O  O   . MET   A 305 ? 0.2047 0.3753 0.1604 -0.0400 0.0196  -0.0442 305 MET   A O   
4619 C  CB  . MET   A 305 ? 0.1766 0.2888 0.1482 -0.0260 0.0138  -0.0306 305 MET   A CB  
4620 C  CG  . MET   A 305 ? 0.1927 0.2849 0.1681 -0.0222 0.0133  -0.0212 305 MET   A CG  
4621 S  SD  . MET   A 305 ? 0.2129 0.2841 0.1989 -0.0145 0.0143  -0.0269 305 MET   A SD  
4622 C  CE  . MET   A 305 ? 0.2526 0.3301 0.2431 -0.0102 0.0171  -0.0406 305 MET   A CE  
4632 N  N   . LEU   A 306 ? 0.2160 0.3767 0.1715 -0.0397 0.0131  -0.0422 306 LEU   A N   
4633 C  CA  . LEU   A 306 ? 0.2284 0.4134 0.1807 -0.0432 0.0153  -0.0562 306 LEU   A CA  
4634 C  C   . LEU   A 306 ? 0.2336 0.4423 0.1713 -0.0540 0.0161  -0.0506 306 LEU   A C   
4635 O  O   . LEU   A 306 ? 0.2425 0.4741 0.1786 -0.0570 0.0209  -0.0623 306 LEU   A O   
4636 C  CB  . LEU   A 306 ? 0.2241 0.4091 0.1777 -0.0431 0.0117  -0.0612 306 LEU   A CB  
4637 C  CG  . LEU   A 306 ? 0.2533 0.4205 0.2216 -0.0343 0.0120  -0.0713 306 LEU   A CG  
4638 C  CD1 . LEU   A 306 ? 0.2717 0.4371 0.2413 -0.0355 0.0079  -0.0732 306 LEU   A CD1 
4639 C  CD2 . LEU   A 306 ? 0.2848 0.4592 0.2616 -0.0294 0.0156  -0.0895 306 LEU   A CD2 
4651 N  N   . SER   A 307 ? 0.2405 0.4446 0.1678 -0.0605 0.0110  -0.0330 307 SER   A N   
4652 C  CA  . SER   A 307 ? 0.2581 0.4820 0.1698 -0.0727 0.0108  -0.0248 307 SER   A CA  
4653 C  C   . SER   A 307 ? 0.2622 0.4913 0.1748 -0.0743 0.0164  -0.0248 307 SER   A C   
4654 O  O   . SER   A 307 ? 0.2650 0.5154 0.1748 -0.0815 0.0196  -0.0287 307 SER   A O   
4655 C  CB  . SER   A 307 ? 0.2828 0.4954 0.1847 -0.0785 0.0022  -0.0045 307 SER   A CB  
4656 O  OG  . SER   A 307 ? 0.2810 0.4928 0.1818 -0.0778 -0.0035 -0.0048 307 SER   A OG  
4662 N  N   . ALA   A 308 ? 0.2305 0.4368 0.1527 -0.0667 0.0164  -0.0197 308 ALA   A N   
4663 C  CA  . ALA   A 308 ? 0.2256 0.4357 0.1502 -0.0674 0.0211  -0.0202 308 ALA   A CA  
4664 C  C   . ALA   A 308 ? 0.2534 0.4832 0.1859 -0.0637 0.0279  -0.0408 308 ALA   A C   
4665 O  O   . ALA   A 308 ? 0.2456 0.4942 0.1781 -0.0692 0.0313  -0.0445 308 ALA   A O   
4666 C  CB  . ALA   A 308 ? 0.2598 0.4415 0.1941 -0.0588 0.0194  -0.0130 308 ALA   A CB  
4672 N  N   . ALA   A 309 ? 0.2214 0.4436 0.1655 -0.0535 0.0280  -0.0541 309 ALA   A N   
4673 C  CA  . ALA   A 309 ? 0.2621 0.5003 0.2164 -0.0482 0.0327  -0.0750 309 ALA   A CA  
4674 C  C   . ALA   A 309 ? 0.2640 0.5308 0.2157 -0.0564 0.0338  -0.0827 309 ALA   A C   
4675 O  O   . ALA   A 309 ? 0.2364 0.5201 0.1975 -0.0563 0.0364  -0.0936 309 ALA   A O   
4676 C  CB  . ALA   A 309 ? 0.2289 0.4490 0.1964 -0.0367 0.0304  -0.0857 309 ALA   A CB  
4682 N  N   . LYS   A 310 ? 0.2639 0.5357 0.2053 -0.0633 0.0307  -0.0765 310 LYS   A N   
4683 C  CA  . LYS   A 310 ? 0.2493 0.5472 0.1891 -0.0720 0.0312  -0.0814 310 LYS   A CA  
4684 C  C   . LYS   A 310 ? 0.2577 0.5693 0.1925 -0.0824 0.0326  -0.0727 310 LYS   A C   
4685 O  O   . LYS   A 310 ? 0.2746 0.6104 0.2155 -0.0864 0.0354  -0.0835 310 LYS   A O   
4686 C  CB  . LYS   A 310 ? 0.2708 0.5692 0.1995 -0.0777 0.0268  -0.0741 310 LYS   A CB  
4687 C  CG  . LYS   A 310 ? 0.3183 0.6442 0.2440 -0.0874 0.0275  -0.0783 310 LYS   A CG  
4688 C  CD  . LYS   A 310 ? 0.4381 0.7643 0.3548 -0.0911 0.0229  -0.0737 310 LYS   A CD  
4689 C  CE  . LYS   A 310 ? 0.6563 0.9743 0.5568 -0.1007 0.0171  -0.0506 310 LYS   A CE  
4690 N  NZ  . LYS   A 310 ? 0.6200 0.9604 0.5119 -0.1140 0.0165  -0.0457 310 LYS   A NZ  
4704 N  N   . ASP   A 311 ? 0.2384 0.5349 0.1635 -0.0869 0.0301  -0.0539 311 ASP   A N   
4705 C  CA  . ASP   A 311 ? 0.2630 0.5697 0.1837 -0.0974 0.0305  -0.0451 311 ASP   A CA  
4706 C  C   . ASP   A 311 ? 0.2472 0.5641 0.1806 -0.0929 0.0355  -0.0582 311 ASP   A C   
4707 O  O   . ASP   A 311 ? 0.2847 0.6228 0.2187 -0.1015 0.0372  -0.0611 311 ASP   A O   
4708 C  CB  . ASP   A 311 ? 0.2686 0.5527 0.1797 -0.1011 0.0260  -0.0235 311 ASP   A CB  
4709 C  CG  . ASP   A 311 ? 0.2995 0.5742 0.1984 -0.1067 0.0190  -0.0086 311 ASP   A CG  
4710 O  OD1 . ASP   A 311 ? 0.3256 0.6159 0.2202 -0.1123 0.0179  -0.0118 311 ASP   A OD1 
4711 O  OD2 . ASP   A 311 ? 0.3533 0.6050 0.2478 -0.1056 0.0139  0.0066  311 ASP   A OD2 
4716 N  N   . LEU   A 312 ? 0.2327 0.5349 0.1766 -0.0799 0.0372  -0.0663 312 LEU   A N   
4717 C  CA  . LEU   A 312 ? 0.2322 0.5399 0.1892 -0.0737 0.0405  -0.0779 312 LEU   A CA  
4718 C  C   . LEU   A 312 ? 0.2369 0.5639 0.2085 -0.0680 0.0421  -0.1003 312 LEU   A C   
4719 O  O   . LEU   A 312 ? 0.2754 0.6122 0.2588 -0.0642 0.0437  -0.1113 312 LEU   A O   
4720 C  CB  . LEU   A 312 ? 0.2412 0.5228 0.2033 -0.0620 0.0406  -0.0756 312 LEU   A CB  
4721 C  CG  . LEU   A 312 ? 0.2284 0.4907 0.1803 -0.0658 0.0391  -0.0554 312 LEU   A CG  
4722 C  CD1 . LEU   A 312 ? 0.2592 0.4972 0.2156 -0.0543 0.0392  -0.0544 312 LEU   A CD1 
4723 C  CD2 . LEU   A 312 ? 0.3251 0.5956 0.2777 -0.0722 0.0404  -0.0509 312 LEU   A CD2 
4735 N  N   . GLY   A 313 ? 0.2289 0.5614 0.2010 -0.0670 0.0411  -0.1078 313 GLY   A N   
4736 C  CA  . GLY   A 313 ? 0.2868 0.6353 0.2747 -0.0607 0.0416  -0.1294 313 GLY   A CA  
4737 C  C   . GLY   A 313 ? 0.2733 0.6018 0.2755 -0.0450 0.0399  -0.1409 313 GLY   A C   
4738 O  O   . GLY   A 313 ? 0.3108 0.6496 0.3291 -0.0383 0.0390  -0.1590 313 GLY   A O   
4742 N  N   . TYR   A 314 ? 0.2132 0.5134 0.2106 -0.0392 0.0388  -0.1308 314 TYR   A N   
4743 C  CA  . TYR   A 314 ? 0.2146 0.4926 0.2246 -0.0252 0.0365  -0.1396 314 TYR   A CA  
4744 C  C   . TYR   A 314 ? 0.2762 0.5477 0.2894 -0.0213 0.0338  -0.1479 314 TYR   A C   
4745 O  O   . TYR   A 314 ? 0.2646 0.5430 0.2666 -0.0290 0.0339  -0.1426 314 TYR   A O   
4746 C  CB  . TYR   A 314 ? 0.2275 0.4805 0.2303 -0.0223 0.0368  -0.1252 314 TYR   A CB  
4747 C  CG  . TYR   A 314 ? 0.2286 0.4846 0.2322 -0.0237 0.0389  -0.1192 314 TYR   A CG  
4748 C  CD1 . TYR   A 314 ? 0.2334 0.5143 0.2406 -0.0297 0.0404  -0.1243 314 TYR   A CD1 
4749 C  CD2 . TYR   A 314 ? 0.2560 0.4910 0.2570 -0.0196 0.0393  -0.1087 314 TYR   A CD2 
4750 C  CE1 . TYR   A 314 ? 0.3067 0.5900 0.3150 -0.0313 0.0419  -0.1192 314 TYR   A CE1 
4751 C  CE2 . TYR   A 314 ? 0.2462 0.4838 0.2484 -0.0209 0.0409  -0.1034 314 TYR   A CE2 
4752 C  CZ  . TYR   A 314 ? 0.2795 0.5407 0.2853 -0.0267 0.0420  -0.1086 314 TYR   A CZ  
4753 O  OH  . TYR   A 314 ? 0.2718 0.5353 0.2791 -0.0284 0.0434  -0.1037 314 TYR   A OH  
4763 N  N   . ASN   A 315 ? 0.2434 0.5008 0.2725 -0.0096 0.0304  -0.1607 315 ASN   A N   
4764 C  CA  . ASN   A 315 ? 0.2321 0.4814 0.2669 -0.0057 0.0270  -0.1698 315 ASN   A CA  
4765 C  C   . ASN   A 315 ? 0.2219 0.4510 0.2441 -0.0076 0.0263  -0.1587 315 ASN   A C   
4766 O  O   . ASN   A 315 ? 0.2717 0.4766 0.2923 -0.0030 0.0255  -0.1515 315 ASN   A O   
4767 C  CB  . ASN   A 315 ? 0.2774 0.5105 0.3320 0.0070  0.0217  -0.1830 315 ASN   A CB  
4768 C  CG  . ASN   A 315 ? 0.2895 0.5202 0.3535 0.0100  0.0177  -0.1953 315 ASN   A CG  
4769 O  OD1 . ASN   A 315 ? 0.2711 0.4785 0.3329 0.0121  0.0150  -0.1921 315 ASN   A OD1 
4770 N  ND2 . ASN   A 315 ? 0.3145 0.5700 0.3894 0.0096  0.0174  -0.2095 315 ASN   A ND2 
4777 N  N   . LEU   A 316 ? 0.2519 0.4916 0.2666 -0.0143 0.0262  -0.1585 316 LEU   A N   
4778 C  CA  . LEU   A 316 ? 0.2475 0.4713 0.2505 -0.0171 0.0247  -0.1488 316 LEU   A CA  
4779 C  C   . LEU   A 316 ? 0.2435 0.4420 0.2584 -0.0093 0.0200  -0.1558 316 LEU   A C   
4780 O  O   . LEU   A 316 ? 0.2693 0.4436 0.2824 -0.0094 0.0173  -0.1417 316 LEU   A O   
4781 C  CB  . LEU   A 316 ? 0.2577 0.5016 0.2487 -0.0274 0.0247  -0.1444 316 LEU   A CB  
4782 C  CG  . LEU   A 316 ? 0.3009 0.5655 0.2793 -0.0377 0.0275  -0.1324 316 LEU   A CG  
4783 C  CD1 . LEU   A 316 ? 0.4194 0.6970 0.3843 -0.0478 0.0256  -0.1247 316 LEU   A CD1 
4784 C  CD2 . LEU   A 316 ? 0.3363 0.5882 0.3061 -0.0388 0.0287  -0.1168 316 LEU   A CD2 
4796 N  N   . ASP   A 317 ? 0.2426 0.4438 0.2729 -0.0033 0.0178  -0.1728 317 ASP   A N   
4797 C  CA  . ASP   A 317 ? 0.2392 0.4151 0.2802 0.0028  0.0126  -0.1793 317 ASP   A CA  
4798 C  C   . ASP   A 317 ? 0.2848 0.4299 0.3309 0.0093  0.0100  -0.1711 317 ASP   A C   
4799 O  O   . ASP   A 317 ? 0.2885 0.4074 0.3365 0.0098  0.0064  -0.1632 317 ASP   A O   
4800 C  CB  . ASP   A 317 ? 0.2485 0.4323 0.3066 0.0077  0.0093  -0.1959 317 ASP   A CB  
4801 C  CG  . ASP   A 317 ? 0.2814 0.4939 0.3361 0.0009  0.0113  -0.2022 317 ASP   A CG  
4802 O  OD1 . ASP   A 317 ? 0.2572 0.4685 0.3024 -0.0049 0.0111  -0.1977 317 ASP   A OD1 
4803 O  OD2 . ASP   A 317 ? 0.3404 0.5774 0.4025 0.0010  0.0128  -0.2121 317 ASP   A OD2 
4808 N  N   . ASP   A 318 ? 0.2412 0.3893 0.2895 0.0133  0.0116  -0.1703 318 ASP   A N   
4809 C  CA  . ASP   A 318 ? 0.2515 0.3708 0.3042 0.0190  0.0085  -0.1598 318 ASP   A CA  
4810 C  C   . ASP   A 318 ? 0.3015 0.4062 0.3417 0.0130  0.0100  -0.1369 318 ASP   A C   
4811 O  O   . ASP   A 318 ? 0.3101 0.3876 0.3520 0.0151  0.0069  -0.1274 318 ASP   A O   
4812 C  CB  . ASP   A 318 ? 0.2624 0.3913 0.3200 0.0241  0.0098  -0.1638 318 ASP   A CB  
4813 C  CG  . ASP   A 318 ? 0.3419 0.4788 0.4169 0.0312  0.0055  -0.1811 318 ASP   A CG  
4814 O  OD1 . ASP   A 318 ? 0.3377 0.4566 0.4231 0.0360  -0.0010 -0.1872 318 ASP   A OD1 
4815 O  OD2 . ASP   A 318 ? 0.2951 0.4537 0.3742 0.0317  0.0074  -0.1855 318 ASP   A OD2 
4820 N  N   . ILE   A 319 ? 0.2663 0.3892 0.2940 0.0052  0.0143  -0.1283 319 ILE   A N   
4821 C  CA  . ILE   A 319 ? 0.2514 0.3623 0.2691 0.0002  0.0148  -0.1085 319 ILE   A CA  
4822 C  C   . ILE   A 319 ? 0.2210 0.3199 0.2391 -0.0022 0.0122  -0.1063 319 ILE   A C   
4823 O  O   . ILE   A 319 ? 0.2350 0.3129 0.2532 -0.0021 0.0109  -0.0953 319 ILE   A O   
4824 C  CB  . ILE   A 319 ? 0.2876 0.4207 0.2929 -0.0074 0.0182  -0.1007 319 ILE   A CB  
4825 C  CG1 . ILE   A 319 ? 0.3013 0.4427 0.3066 -0.0060 0.0210  -0.0999 319 ILE   A CG1 
4826 C  CG2 . ILE   A 319 ? 0.3126 0.4349 0.3094 -0.0122 0.0171  -0.0826 319 ILE   A CG2 
4827 C  CD1 . ILE   A 319 ? 0.3289 0.4983 0.3242 -0.0141 0.0246  -0.0993 319 ILE   A CD1 
4839 N  N   . LYS   A 320 ? 0.2167 0.3308 0.2355 -0.0048 0.0116  -0.1177 320 LYS   A N   
4840 C  CA  . LYS   A 320 ? 0.2584 0.3637 0.2787 -0.0075 0.0089  -0.1174 320 LYS   A CA  
4841 C  C   . LYS   A 320 ? 0.2469 0.3247 0.2777 -0.0030 0.0057  -0.1193 320 LYS   A C   
4842 O  O   . LYS   A 320 ? 0.2464 0.3087 0.2770 -0.0058 0.0045  -0.1104 320 LYS   A O   
4843 C  CB  . LYS   A 320 ? 0.2617 0.3894 0.2821 -0.0103 0.0085  -0.1325 320 LYS   A CB  
4844 C  CG  . LYS   A 320 ? 0.2562 0.4087 0.2628 -0.0178 0.0103  -0.1265 320 LYS   A CG  
4845 C  CD  . LYS   A 320 ? 0.2943 0.4733 0.2994 -0.0211 0.0104  -0.1430 320 LYS   A CD  
4846 C  CE  . LYS   A 320 ? 0.2880 0.4914 0.2766 -0.0299 0.0117  -0.1346 320 LYS   A CE  
4847 N  NZ  . LYS   A 320 ? 0.3301 0.5648 0.3144 -0.0342 0.0132  -0.1507 320 LYS   A NZ  
4861 N  N   . LYS   A 321 ? 0.2578 0.3297 0.2981 0.0035  0.0036  -0.1310 321 LYS   A N   
4862 C  CA  . LYS   A 321 ? 0.2675 0.3108 0.3167 0.0069  -0.0011 -0.1312 321 LYS   A CA  
4863 C  C   . LYS   A 321 ? 0.2749 0.2987 0.3186 0.0061  -0.0002 -0.1129 321 LYS   A C   
4864 O  O   . LYS   A 321 ? 0.2888 0.2929 0.3332 0.0030  -0.0020 -0.1058 321 LYS   A O   
4865 C  CB  . LYS   A 321 ? 0.2833 0.3232 0.3445 0.0153  -0.0052 -0.1467 321 LYS   A CB  
4866 C  CG  . LYS   A 321 ? 0.3422 0.3494 0.4111 0.0190  -0.0116 -0.1439 321 LYS   A CG  
4867 C  CD  . LYS   A 321 ? 0.4935 0.4969 0.5768 0.0283  -0.0179 -0.1612 321 LYS   A CD  
4868 C  CE  . LYS   A 321 ? 0.6114 0.5791 0.7013 0.0314  -0.0263 -0.1563 321 LYS   A CE  
4869 N  NZ  . LYS   A 321 ? 0.6073 0.5627 0.6919 0.0339  -0.0267 -0.1421 321 LYS   A NZ  
4883 N  N   . SER   A 322 ? 0.2550 0.2861 0.2929 0.0076  0.0029  -0.1056 322 SER   A N   
4884 C  CA  . SER   A 322 ? 0.2447 0.2597 0.2774 0.0069  0.0039  -0.0897 322 SER   A CA  
4885 C  C   . SER   A 322 ? 0.2607 0.2754 0.2868 0.0002  0.0062  -0.0781 322 SER   A C   
4886 O  O   . SER   A 322 ? 0.2653 0.2627 0.2907 -0.0018 0.0060  -0.0691 322 SER   A O   
4887 C  CB  . SER   A 322 ? 0.2365 0.2618 0.2653 0.0096  0.0065  -0.0859 322 SER   A CB  
4888 O  OG  . SER   A 322 ? 0.2573 0.2862 0.2940 0.0163  0.0042  -0.0979 322 SER   A OG  
4894 N  N   . LEU   A 323 ? 0.2328 0.2674 0.2544 -0.0035 0.0081  -0.0785 323 LEU   A N   
4895 C  CA  . LEU   A 323 ? 0.2339 0.2695 0.2516 -0.0087 0.0089  -0.0692 323 LEU   A CA  
4896 C  C   . LEU   A 323 ? 0.2559 0.2795 0.2795 -0.0115 0.0070  -0.0720 323 LEU   A C   
4897 O  O   . LEU   A 323 ? 0.2428 0.2575 0.2663 -0.0146 0.0078  -0.0634 323 LEU   A O   
4898 C  CB  . LEU   A 323 ? 0.2566 0.3151 0.2685 -0.0122 0.0091  -0.0701 323 LEU   A CB  
4899 C  CG  . LEU   A 323 ? 0.2281 0.2984 0.2321 -0.0127 0.0108  -0.0629 323 LEU   A CG  
4900 C  CD1 . LEU   A 323 ? 0.2464 0.3402 0.2436 -0.0175 0.0101  -0.0660 323 LEU   A CD1 
4901 C  CD2 . LEU   A 323 ? 0.2462 0.3071 0.2470 -0.0134 0.0110  -0.0483 323 LEU   A CD2 
4913 N  N   . SER   A 324 ? 0.2530 0.2772 0.2826 -0.0109 0.0046  -0.0849 324 SER   A N   
4914 C  CA  A SER   A 324 ? 0.2538 0.2664 0.2894 -0.0147 0.0024  -0.0877 324 SER   A CA  
4915 C  CA  B SER   A 324 ? 0.2534 0.2659 0.2891 -0.0146 0.0024  -0.0879 324 SER   A CA  
4916 C  C   . SER   A 324 ? 0.2781 0.2657 0.3157 -0.0151 0.0017  -0.0806 324 SER   A C   
4917 O  O   . SER   A 324 ? 0.2726 0.2512 0.3116 -0.0209 0.0019  -0.0760 324 SER   A O   
4918 C  CB  A SER   A 324 ? 0.2883 0.3051 0.3310 -0.0136 -0.0009 -0.1041 324 SER   A CB  
4919 C  CB  B SER   A 324 ? 0.2878 0.3046 0.3306 -0.0132 -0.0009 -0.1045 324 SER   A CB  
4920 O  OG  A SER   A 324 ? 0.3555 0.3711 0.4017 -0.0070 -0.0024 -0.1127 324 SER   A OG  
4921 O  OG  B SER   A 324 ? 0.3652 0.3756 0.4133 -0.0185 -0.0030 -0.1077 324 SER   A OG  
4932 N  N   . GLU   A 325 ? 0.2682 0.2455 0.3053 -0.0098 0.0006  -0.0795 325 GLU   A N   
4933 C  CA  . GLU   A 325 ? 0.2740 0.2273 0.3109 -0.0107 -0.0012 -0.0717 325 GLU   A CA  
4934 C  C   . GLU   A 325 ? 0.2603 0.2116 0.2903 -0.0150 0.0031  -0.0577 325 GLU   A C   
4935 O  O   . GLU   A 325 ? 0.3837 0.3180 0.4124 -0.0193 0.0025  -0.0510 325 GLU   A O   
4936 C  CB  . GLU   A 325 ? 0.3142 0.2587 0.3526 -0.0032 -0.0046 -0.0744 325 GLU   A CB  
4937 C  CG  . GLU   A 325 ? 0.3967 0.3348 0.4452 0.0008  -0.0107 -0.0887 325 GLU   A CG  
4938 C  CD  . GLU   A 325 ? 0.5173 0.4485 0.5700 0.0095  -0.0151 -0.0931 325 GLU   A CD  
4939 O  OE1 . GLU   A 325 ? 0.4536 0.3743 0.5011 0.0106  -0.0153 -0.0824 325 GLU   A OE1 
4940 O  OE2 . GLU   A 325 ? 0.6175 0.5557 0.6796 0.0154  -0.0187 -0.1087 325 GLU   A OE2 
4947 N  N   . VAL   A 326 ? 0.2591 0.2272 0.2849 -0.0145 0.0068  -0.0536 326 VAL   A N   
4948 C  CA  . VAL   A 326 ? 0.2632 0.2317 0.2853 -0.0181 0.0103  -0.0431 326 VAL   A CA  
4949 C  C   . VAL   A 326 ? 0.2719 0.2530 0.2969 -0.0228 0.0115  -0.0440 326 VAL   A C   
4950 O  O   . VAL   A 326 ? 0.2527 0.2399 0.2767 -0.0242 0.0138  -0.0376 326 VAL   A O   
4951 C  CB  . VAL   A 326 ? 0.2560 0.2308 0.2727 -0.0140 0.0123  -0.0367 326 VAL   A CB  
4952 C  CG1 . VAL   A 326 ? 0.2946 0.2566 0.3091 -0.0096 0.0109  -0.0352 326 VAL   A CG1 
4953 C  CG2 . VAL   A 326 ? 0.2860 0.2798 0.3015 -0.0117 0.0122  -0.0400 326 VAL   A CG2 
4963 N  N   . THR   A 327 ? 0.2499 0.2352 0.2798 -0.0249 0.0093  -0.0528 327 THR   A N   
4964 C  CA  . THR   A 327 ? 0.2490 0.2464 0.2829 -0.0295 0.0092  -0.0553 327 THR   A CA  
4965 C  C   . THR   A 327 ? 0.2305 0.2460 0.2618 -0.0277 0.0093  -0.0519 327 THR   A C   
4966 O  O   . THR   A 327 ? 0.2892 0.3125 0.3240 -0.0305 0.0093  -0.0495 327 THR   A O   
4967 C  CB  . THR   A 327 ? 0.2295 0.2186 0.2672 -0.0364 0.0112  -0.0515 327 THR   A CB  
4968 O  OG1 . THR   A 327 ? 0.2576 0.2493 0.2931 -0.0364 0.0145  -0.0428 327 THR   A OG1 
4969 C  CG2 . THR   A 327 ? 0.2454 0.2134 0.2834 -0.0394 0.0100  -0.0518 327 THR   A CG2 
4977 N  N   . ILE   A 328 ? 0.2457 0.2688 0.2716 -0.0234 0.0086  -0.0522 328 ILE   A N   
4978 C  CA  . ILE   A 328 ? 0.2210 0.2607 0.2429 -0.0230 0.0070  -0.0488 328 ILE   A CA  
4979 C  C   . ILE   A 328 ? 0.2685 0.3226 0.2903 -0.0249 0.0042  -0.0578 328 ILE   A C   
4980 O  O   . ILE   A 328 ? 0.2900 0.3449 0.3122 -0.0239 0.0042  -0.0673 328 ILE   A O   
4981 C  CB  . ILE   A 328 ? 0.2471 0.2885 0.2620 -0.0195 0.0080  -0.0434 328 ILE   A CB  
4982 C  CG1 . ILE   A 328 ? 0.2527 0.2839 0.2676 -0.0182 0.0098  -0.0337 328 ILE   A CG1 
4983 C  CG2 . ILE   A 328 ? 0.2759 0.3348 0.2846 -0.0207 0.0054  -0.0414 328 ILE   A CG2 
4984 C  CD1 . ILE   A 328 ? 0.2903 0.3188 0.2998 -0.0149 0.0111  -0.0293 328 ILE   A CD1 
4996 N  N   . ASN   A 329 ? 0.2499 0.3161 0.2719 -0.0272 0.0013  -0.0555 329 ASN   A N   
4997 C  CA  . ASN   A 329 ? 0.3014 0.3831 0.3226 -0.0299 -0.0021 -0.0634 329 ASN   A CA  
4998 C  C   . ASN   A 329 ? 0.3083 0.4046 0.3188 -0.0298 -0.0037 -0.0609 329 ASN   A C   
4999 O  O   . ASN   A 329 ? 0.3517 0.4538 0.3573 -0.0305 -0.0068 -0.0512 329 ASN   A O   
5000 C  CB  . ASN   A 329 ? 0.2758 0.3635 0.3028 -0.0326 -0.0056 -0.0617 329 ASN   A CB  
5001 C  CG  . ASN   A 329 ? 0.4368 0.5420 0.4617 -0.0355 -0.0102 -0.0685 329 ASN   A CG  
5002 O  OD1 . ASN   A 329 ? 0.3984 0.5131 0.4163 -0.0360 -0.0104 -0.0743 329 ASN   A OD1 
5003 N  ND2 . ASN   A 329 ? 0.5257 0.6373 0.5571 -0.0375 -0.0141 -0.0684 329 ASN   A ND2 
5010 N  N   . TYR   A 330 ? 0.2390 0.3416 0.2460 -0.0293 -0.0019 -0.0699 330 TYR   A N   
5011 C  CA  . TYR   A 330 ? 0.2464 0.3666 0.2425 -0.0312 -0.0024 -0.0689 330 TYR   A CA  
5012 C  C   . TYR   A 330 ? 0.2658 0.4061 0.2573 -0.0357 -0.0057 -0.0766 330 TYR   A C   
5013 O  O   . TYR   A 330 ? 0.2724 0.4300 0.2526 -0.0394 -0.0068 -0.0744 330 TYR   A O   
5014 C  CB  . TYR   A 330 ? 0.2379 0.3579 0.2331 -0.0283 0.0018  -0.0753 330 TYR   A CB  
5015 C  CG  . TYR   A 330 ? 0.2583 0.3788 0.2611 -0.0261 0.0029  -0.0923 330 TYR   A CG  
5016 C  CD1 . TYR   A 330 ? 0.2558 0.3969 0.2557 -0.0287 0.0022  -0.1048 330 TYR   A CD1 
5017 C  CD2 . TYR   A 330 ? 0.2809 0.3807 0.2934 -0.0216 0.0038  -0.0959 330 TYR   A CD2 
5018 C  CE1 . TYR   A 330 ? 0.2987 0.4402 0.3074 -0.0259 0.0024  -0.1221 330 TYR   A CE1 
5019 C  CE2 . TYR   A 330 ? 0.3057 0.4032 0.3265 -0.0191 0.0030  -0.1115 330 TYR   A CE2 
5020 C  CZ  . TYR   A 330 ? 0.2899 0.4083 0.3097 -0.0208 0.0023  -0.1253 330 TYR   A CZ  
5021 O  OH  . TYR   A 330 ? 0.3251 0.4421 0.3547 -0.0177 0.0007  -0.1429 330 TYR   A OH  
5031 N  N   . GLN   A 331 ? 0.2688 0.4081 0.2683 -0.0363 -0.0075 -0.0855 331 GLN   A N   
5032 C  CA  . GLN   A 331 ? 0.3039 0.4628 0.2993 -0.0407 -0.0113 -0.0929 331 GLN   A CA  
5033 C  C   . GLN   A 331 ? 0.3015 0.4697 0.2885 -0.0442 -0.0170 -0.0799 331 GLN   A C   
5034 O  O   . GLN   A 331 ? 0.3512 0.5389 0.3271 -0.0489 -0.0202 -0.0806 331 GLN   A O   
5035 C  CB  . GLN   A 331 ? 0.2873 0.4397 0.2948 -0.0408 -0.0123 -0.1039 331 GLN   A CB  
5036 C  CG  . GLN   A 331 ? 0.3625 0.5064 0.3778 -0.0378 -0.0089 -0.1183 331 GLN   A CG  
5037 C  CD  . GLN   A 331 ? 0.4112 0.5299 0.4333 -0.0336 -0.0057 -0.1128 331 GLN   A CD  
5038 O  OE1 . GLN   A 331 ? 0.3617 0.4695 0.3844 -0.0335 -0.0052 -0.0999 331 GLN   A OE1 
5039 N  NE2 . GLN   A 331 ? 0.3603 0.4706 0.3882 -0.0301 -0.0043 -0.1233 331 GLN   A NE2 
5048 N  N   . SER   A 332 ? 0.3345 0.4890 0.3261 -0.0420 -0.0187 -0.0677 332 SER   A N   
5049 C  CA  . SER   A 332 ? 0.4678 0.6274 0.4539 -0.0437 -0.0258 -0.0547 332 SER   A CA  
5050 C  C   . SER   A 332 ? 0.4996 0.6696 0.4698 -0.0474 -0.0274 -0.0463 332 SER   A C   
5051 O  O   . SER   A 332 ? 0.4502 0.6306 0.4117 -0.0514 -0.0349 -0.0383 332 SER   A O   
5052 C  CB  . SER   A 332 ? 0.4338 0.5762 0.4296 -0.0394 -0.0262 -0.0454 332 SER   A CB  
5053 O  OG  . SER   A 332 ? 0.5016 0.6307 0.4975 -0.0363 -0.0202 -0.0418 332 SER   A OG  
5059 N  N   . CYS   A 333 ? 0.3234 0.4912 0.2897 -0.0467 -0.0209 -0.0475 333 CYS   A N   
5060 C  CA  . CYS   A 333 ? 0.3361 0.5144 0.2877 -0.0516 -0.0214 -0.0392 333 CYS   A CA  
5061 C  C   . CYS   A 333 ? 0.3934 0.5964 0.3319 -0.0591 -0.0240 -0.0440 333 CYS   A C   
5062 O  O   . CYS   A 333 ? 0.3956 0.6092 0.3194 -0.0659 -0.0276 -0.0334 333 CYS   A O   
5063 C  CB  . CYS   A 333 ? 0.3077 0.4822 0.2598 -0.0493 -0.0134 -0.0432 333 CYS   A CB  
5064 S  SG  . CYS   A 333 ? 0.2883 0.4356 0.2538 -0.0412 -0.0099 -0.0390 333 CYS   A SG  
5069 N  N   . TYR   A 334 ? 0.3805 0.5933 0.3234 -0.0589 -0.0222 -0.0600 334 TYR   A N   
5070 C  CA  . TYR   A 334 ? 0.4326 0.6713 0.3639 -0.0659 -0.0236 -0.0682 334 TYR   A CA  
5071 C  C   . TYR   A 334 ? 0.4015 0.6468 0.3303 -0.0689 -0.0327 -0.0649 334 TYR   A C   
5072 O  O   . TYR   A 334 ? 0.5342 0.8004 0.4561 -0.0740 -0.0343 -0.0748 334 TYR   A O   
5073 C  CB  . TYR   A 334 ? 0.4341 0.6798 0.3733 -0.0631 -0.0168 -0.0895 334 TYR   A CB  
5074 C  CG  . TYR   A 334 ? 0.3971 0.6394 0.3387 -0.0600 -0.0092 -0.0933 334 TYR   A CG  
5075 C  CD1 . TYR   A 334 ? 0.4205 0.6844 0.3496 -0.0659 -0.0057 -0.0949 334 TYR   A CD1 
5076 C  CD2 . TYR   A 334 ? 0.3869 0.6052 0.3427 -0.0518 -0.0058 -0.0941 334 TYR   A CD2 
5077 C  CE1 . TYR   A 334 ? 0.4005 0.6635 0.3335 -0.0628 0.0010  -0.0995 334 TYR   A CE1 
5078 C  CE2 . TYR   A 334 ? 0.3941 0.6096 0.3525 -0.0485 0.0000  -0.0975 334 TYR   A CE2 
5079 C  CZ  . TYR   A 334 ? 0.3757 0.6138 0.3236 -0.0535 0.0033  -0.1006 334 TYR   A CZ  
5080 O  OH  . TYR   A 334 ? 0.4278 0.6656 0.3797 -0.0501 0.0088  -0.1050 334 TYR   A OH  
5090 N  N   . VAL   A 335 ? 0.5110 0.7405 0.4455 -0.0659 -0.0390 -0.0517 335 VAL   A N   
5091 C  CA  . VAL   A 335 ? 0.5826 0.8162 0.5176 -0.0673 -0.0492 -0.0472 335 VAL   A CA  
5092 C  C   . VAL   A 335 ? 0.6144 0.8598 0.5555 -0.0678 -0.0485 -0.0649 335 VAL   A C   
5093 O  O   . VAL   A 335 ? 0.5538 0.7878 0.5110 -0.0627 -0.0442 -0.0749 335 VAL   A O   
5094 C  CB  . VAL   A 335 ? 0.4999 0.7460 0.4157 -0.0751 -0.0584 -0.0325 335 VAL   A CB  
5095 C  CG1 . VAL   A 335 ? 0.6182 0.8517 0.5281 -0.0755 -0.0585 -0.0161 335 VAL   A CG1 
5096 C  CG2 . VAL   A 335 ? 0.6063 0.8749 0.5078 -0.0826 -0.0553 -0.0399 335 VAL   A CG2 
5106 C  C1  . A1IRL B .   ? 0.2912 0.3006 0.2977 -0.0151 0.0469  -0.0163 401 A1IRL A C1  
5107 C  C2  . A1IRL B .   ? 0.2665 0.2885 0.2827 -0.0178 0.0501  -0.0228 401 A1IRL A C2  
5108 C  C3  . A1IRL B .   ? 0.2246 0.2575 0.2581 -0.0122 0.0482  -0.0322 401 A1IRL A C3  
5109 C  C4  . A1IRL B .   ? 0.2418 0.2707 0.2818 -0.0046 0.0428  -0.0339 401 A1IRL A C4  
5110 C  C5  . A1IRL B .   ? 0.2002 0.2166 0.2297 -0.0033 0.0404  -0.0270 401 A1IRL A C5  
5111 C  C6  . A1IRL B .   ? 0.2420 0.2497 0.2550 -0.0082 0.0427  -0.0185 401 A1IRL A C6  
5112 C  C10 . A1IRL B .   ? 0.2882 0.2803 0.2596 -0.0149 0.0440  -0.0076 401 A1IRL A C10 
5113 C  C11 . A1IRL B .   ? 0.2646 0.2461 0.2381 -0.0052 0.0356  -0.0051 401 A1IRL A C11 
5114 C  C12 . A1IRL B .   ? 0.2291 0.2026 0.2257 0.0029  0.0277  0.0016  401 A1IRL A C12 
5115 C  C13 . A1IRL B .   ? 0.1776 0.1489 0.1812 0.0065  0.0227  0.0023  401 A1IRL A C13 
5116 C  C14 . A1IRL B .   ? 0.1855 0.1517 0.1820 0.0065  0.0211  0.0085  401 A1IRL A C14 
5117 C  C15 . A1IRL B .   ? 0.1979 0.1611 0.1839 0.0056  0.0225  0.0097  401 A1IRL A C15 
5118 C  C16 . A1IRL B .   ? 0.2253 0.1897 0.2104 0.0061  0.0220  0.0065  401 A1IRL A C16 
5119 C  C17 . A1IRL B .   ? 0.2144 0.1746 0.1972 0.0068  0.0201  0.0137  401 A1IRL A C17 
5120 C  C7  . A1IRL B .   ? 0.3893 0.3777 0.3825 -0.0068 0.0387  -0.0068 401 A1IRL A C7  
5121 C  C8  . A1IRL B .   ? 0.3548 0.3404 0.3472 -0.0031 0.0358  -0.0074 401 A1IRL A C8  
5122 C  C9  . A1IRL B .   ? 0.2266 0.2162 0.2089 -0.0069 0.0391  -0.0099 401 A1IRL A C9  
5123 N  N1  . A1IRL B .   ? 0.2701 0.2681 0.2765 -0.0052 0.0393  -0.0139 401 A1IRL A N1  
5124 N  N2  . A1IRL B .   ? 0.3929 0.3696 0.3843 0.0007  0.0309  -0.0018 401 A1IRL A N2  
5125 O  O1  . A1IRL B .   ? 0.4246 0.4073 0.4079 -0.0110 0.0400  -0.0013 401 A1IRL A O1  
5126 O  O2  . A1IRL B .   ? 0.2291 0.2083 0.2563 0.0105  0.0190  -0.0072 401 A1IRL A O2  
5127 O  O3  . A1IRL B .   ? 0.2481 0.2157 0.2689 0.0103  0.0123  0.0048  401 A1IRL A O3  
5128 O  O4  . A1IRL B .   ? 0.1734 0.1467 0.1901 0.0078  0.0178  0.0052  401 A1IRL A O4  
5129 O  O5  . A1IRL B .   ? 0.2147 0.1867 0.2094 0.0013  0.0285  0.0045  401 A1IRL A O5  
5130 P  P1  . A1IRL B .   ? 0.2003 0.1729 0.2180 0.0090  0.0178  0.0016  401 A1IRL A P1  
5131 CL CL1 . A1IRL B .   ? 0.2775 0.3291 0.3254 -0.0150 0.0518  -0.0421 401 A1IRL A CL1 
5132 CL CL2 . A1IRL B .   ? 0.3028 0.3412 0.3661 0.0034  0.0376  -0.0450 401 A1IRL A CL2 
5158 O  O6  . BU3   C .   ? 0.2749 0.3113 0.3327 0.0014  -0.0288 0.0105  402 BU3   A O6  
5159 C  C3  . BU3   C .   ? 0.3697 0.4090 0.4419 0.0061  -0.0379 0.0091  402 BU3   A C3  
5160 C  C4  . BU3   C .   ? 0.3577 0.3884 0.4377 0.0110  -0.0410 0.0101  402 BU3   A C4  
5161 C  C2  . BU3   C .   ? 0.3889 0.4396 0.4723 0.0062  -0.0339 -0.0014 402 BU3   A C2  
5162 O  O5  . BU3   C .   ? 0.3388 0.3892 0.4242 0.0051  -0.0229 -0.0081 402 BU3   A O5  
5163 C  C1  . BU3   C .   ? 0.3825 0.4407 0.4583 0.0014  -0.0337 -0.0019 402 BU3   A C1  
5174 O  O6  . BU3   D .   ? 0.5739 0.5415 0.4656 0.0205  -0.0492 0.0139  403 BU3   A O6  
5175 C  C3  . BU3   D .   ? 0.6092 0.5858 0.5030 0.0225  -0.0552 0.0089  403 BU3   A C3  
5176 C  C4  . BU3   D .   ? 0.5833 0.5536 0.4645 0.0248  -0.0677 0.0158  403 BU3   A C4  
5177 C  C2  . BU3   D .   ? 0.5447 0.5319 0.4356 0.0172  -0.0498 0.0013  403 BU3   A C2  
5178 O  O5  . BU3   D .   ? 0.6384 0.6316 0.5205 0.0168  -0.0576 -0.0002 403 BU3   A O5  
5179 C  C1  . BU3   D .   ? 0.5678 0.5542 0.4485 0.0104  -0.0410 0.0017  403 BU3   A C1  
5190 C  C1  . GOL   E .   ? 0.4614 0.5533 0.5505 0.0274  -0.0089 -0.1975 404 GOL   A C1  
5191 O  O1  . GOL   E .   ? 0.6317 0.7073 0.7168 0.0301  -0.0087 -0.1869 404 GOL   A O1  
5192 C  C2  . GOL   E .   ? 0.4697 0.5875 0.5700 0.0318  -0.0090 -0.2107 404 GOL   A C2  
5193 O  O2  . GOL   E .   ? 0.4722 0.6070 0.5674 0.0316  -0.0042 -0.2071 404 GOL   A O2  
5194 C  C3  . GOL   E .   ? 0.5437 0.6400 0.6618 0.0408  -0.0182 -0.2175 404 GOL   A C3  
5195 O  O3  . GOL   E .   ? 0.4959 0.6178 0.6273 0.0444  -0.0193 -0.2330 404 GOL   A O3  
5203 O  O6  . BU3   F .   ? 0.5212 0.5695 0.6448 0.0351  -0.0108 -0.1902 405 BU3   A O6  
5204 C  C3  . BU3   F .   ? 0.5567 0.6214 0.6636 0.0301  -0.0047 -0.1962 405 BU3   A C3  
5205 C  C4  . BU3   F .   ? 0.4752 0.5518 0.5962 0.0319  -0.0082 -0.2115 405 BU3   A C4  
5206 C  C2  . BU3   F .   ? 0.6128 0.6661 0.7010 0.0260  -0.0052 -0.1861 405 BU3   A C2  
5207 O  O5  . BU3   F .   ? 0.5462 0.5831 0.6465 0.0277  -0.0148 -0.1856 405 BU3   A O5  
5208 C  C1  . BU3   F .   ? 0.4799 0.5229 0.5548 0.0239  -0.0022 -0.1681 405 BU3   A C1  
5219 C  C1  . GOL   G .   ? 0.4253 0.6816 0.4931 0.0108  0.0243  -0.1841 406 GOL   A C1  
5220 O  O1  . GOL   G .   ? 0.3469 0.5857 0.3987 0.0074  0.0270  -0.1669 406 GOL   A O1  
5221 C  C2  . GOL   G .   ? 0.4437 0.6861 0.5284 0.0230  0.0186  -0.1915 406 GOL   A C2  
5222 O  O2  . GOL   G .   ? 0.6249 0.8382 0.7065 0.0287  0.0167  -0.1810 406 GOL   A O2  
5223 C  C3  . GOL   G .   ? 0.5273 0.7665 0.6285 0.0305  0.0120  -0.2073 406 GOL   A C3  
5224 O  O3  . GOL   G .   ? 0.5848 0.7949 0.6820 0.0337  0.0092  -0.2017 406 GOL   A O3  
5232 O  O6  . BU3   H .   ? 0.3124 0.2954 0.2994 0.0282  -0.0086 0.0032  407 BU3   A O6  
5233 C  C3  . BU3   H .   ? 0.4214 0.4148 0.4145 0.0287  -0.0111 -0.0006 407 BU3   A C3  
5234 C  C4  . BU3   H .   ? 0.4342 0.4335 0.4305 0.0224  -0.0074 -0.0003 407 BU3   A C4  
5235 C  C2  . BU3   H .   ? 0.4236 0.4290 0.4269 0.0327  -0.0133 -0.0067 407 BU3   A C2  
5236 O  O5  . BU3   H .   ? 0.4207 0.4194 0.4235 0.0380  -0.0161 -0.0075 407 BU3   A O5  
5237 C  C1  . BU3   H .   ? 0.3874 0.4025 0.3969 0.0355  -0.0184 -0.0116 407 BU3   A C1  
5248 O  O6  . BU3   I .   ? 0.5013 0.7159 0.4853 -0.0434 -0.0036 -0.1379 408 BU3   A O6  
5249 C  C3  . BU3   I .   ? 0.4921 0.7229 0.4773 -0.0422 0.0000  -0.1549 408 BU3   A C3  
5250 C  C4  . BU3   I .   ? 0.2789 0.4938 0.2721 -0.0353 0.0038  -0.1548 408 BU3   A C4  
5251 C  C2  . BU3   I .   ? 0.5280 0.7874 0.5012 -0.0484 0.0023  -0.1525 408 BU3   A C2  
5252 O  O5  . BU3   I .   ? 0.6722 0.9449 0.6410 -0.0535 -0.0010 -0.1531 408 BU3   A O5  
5253 C  C1  . BU3   I .   ? 0.4542 0.7263 0.4365 -0.0450 0.0078  -0.1650 408 BU3   A C1  
5264 C  C1  . GOL   J .   ? 0.3357 0.5889 0.3583 -0.0959 0.0432  -0.0135 409 GOL   A C1  
5265 O  O1  . GOL   J .   ? 0.6550 0.8916 0.6838 -0.0777 0.0403  -0.0198 409 GOL   A O1  
5266 C  C2  . GOL   J .   ? 0.5316 0.8136 0.5598 -0.0955 0.0466  -0.0297 409 GOL   A C2  
5267 O  O2  . GOL   J .   ? 0.4626 0.7539 0.4832 -0.1103 0.0469  -0.0250 409 GOL   A O2  
5268 C  C3  . GOL   J .   ? 0.4251 0.7148 0.4717 -0.0822 0.0462  -0.0436 409 GOL   A C3  
5269 O  O3  . GOL   J .   ? 0.5346 0.8267 0.5874 -0.0680 0.0464  -0.0551 409 GOL   A O3  
5276 ZN ZN  . ZN    K .   ? 0.1950 0.1657 0.2088 0.0069  0.0137  0.0132  410 ZN    A ZN  
5277 S  S   . SO4   L .   ? 1.3412 1.1016 1.2639 -0.0559 -0.0332 0.0661  411 SO4   A S   
5278 O  O1  . SO4   L .   ? 1.0697 0.8259 0.9864 -0.0499 -0.0396 0.0709  411 SO4   A O1  
5279 O  O2  . SO4   L .   ? 1.1651 0.9204 1.1030 -0.0457 -0.0378 0.0553  411 SO4   A O2  
5280 O  O3  . SO4   L .   ? 1.1697 0.9225 1.0878 -0.0678 -0.0343 0.0727  411 SO4   A O3  
5281 O  O4  . SO4   L .   ? 1.0286 0.8072 0.9475 -0.0605 -0.0215 0.0645  411 SO4   A O4  
5282 S  S   . SO4   M .   ? 0.9846 0.8483 1.1317 0.0203  -0.0857 -0.0197 412 SO4   A S   
5283 O  O1  . SO4   M .   ? 0.7810 0.6532 0.9273 0.0253  -0.0812 -0.0213 412 SO4   A O1  
5284 O  O2  . SO4   M .   ? 0.5679 0.4387 0.7141 0.0220  -0.0779 -0.0317 412 SO4   A O2  
5285 O  O3  . SO4   M .   ? 0.5332 0.3891 0.6672 0.0098  -0.0872 -0.0018 412 SO4   A O3  
5286 O  O4  . SO4   M .   ? 0.8255 0.6826 0.9878 0.0233  -0.0973 -0.0243 412 SO4   A O4  
# 
