data_9H0X
# 
_entry.id   9H0X 
# 
_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   9H0X         pdb_00009h0x 10.2210/pdb9h0x/pdb 
WWPDB D_1292142200 ?            ?                   
# 
_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                        9H0X 
_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@helmholtz-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})-2-(2-methylpropyl)-~{N}-[4-[[4-[(2-methylpropylsulfonylamino)methyl]-1,2,3-triazol-1-yl]methyl]phenyl]-~{N}'-oxidanyl-propanediamide
;
480.581   1   ?        ? ? ? 
3 non-polymer syn 'ZINC ION' 65.409    1   ?        ? ? ? 
4 water       nat water 18.015    401 ?        ? ? ? 
# 
_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})-2-(2-methylpropyl)-~{N}-[4-[[4-[(2-methylpropylsulfonylamino)methyl]-1,2,3-triazol-1-yl]methyl]phenyl]-~{N}'-oxidanyl-propanediamide
;
A1IRK 
3 'ZINC ION' ZN    
4 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 
A1IRK non-polymer         . 
;(2~{R})-2-(2-methylpropyl)-~{N}-[4-[[4-[(2-methylpropylsulfonylamino)methyl]-1,2,3-triazol-1-yl]methyl]phenyl]-~{N}'-oxidanyl-propanediamide
;
? 'C21 H32 N6 O5 S' 480.581 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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  71  ASP ASP 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  75  THR THR 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 ?   ?   ?   A . n 
A 1 336 ASP 336 336 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IRK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IRK 
_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 A1IRK 1   401 401 A1IRK AAA A . 
C 3 ZN    1   402 1   ZN    ZN  A . 
D 4 HOH   1   501 328 HOH   HOH A . 
D 4 HOH   2   502 122 HOH   HOH A . 
D 4 HOH   3   503 373 HOH   HOH A . 
D 4 HOH   4   504 167 HOH   HOH A . 
D 4 HOH   5   505 191 HOH   HOH A . 
D 4 HOH   6   506 339 HOH   HOH A . 
D 4 HOH   7   507 109 HOH   HOH A . 
D 4 HOH   8   508 127 HOH   HOH A . 
D 4 HOH   9   509 302 HOH   HOH A . 
D 4 HOH   10  510 330 HOH   HOH A . 
D 4 HOH   11  511 345 HOH   HOH A . 
D 4 HOH   12  512 142 HOH   HOH A . 
D 4 HOH   13  513 285 HOH   HOH A . 
D 4 HOH   14  514 259 HOH   HOH A . 
D 4 HOH   15  515 126 HOH   HOH A . 
D 4 HOH   16  516 324 HOH   HOH A . 
D 4 HOH   17  517 194 HOH   HOH A . 
D 4 HOH   18  518 55  HOH   HOH A . 
D 4 HOH   19  519 123 HOH   HOH A . 
D 4 HOH   20  520 91  HOH   HOH A . 
D 4 HOH   21  521 201 HOH   HOH A . 
D 4 HOH   22  522 129 HOH   HOH A . 
D 4 HOH   23  523 88  HOH   HOH A . 
D 4 HOH   24  524 130 HOH   HOH A . 
D 4 HOH   25  525 166 HOH   HOH A . 
D 4 HOH   26  526 303 HOH   HOH A . 
D 4 HOH   27  527 372 HOH   HOH A . 
D 4 HOH   28  528 133 HOH   HOH A . 
D 4 HOH   29  529 204 HOH   HOH A . 
D 4 HOH   30  530 401 HOH   HOH A . 
D 4 HOH   31  531 348 HOH   HOH A . 
D 4 HOH   32  532 49  HOH   HOH A . 
D 4 HOH   33  533 44  HOH   HOH A . 
D 4 HOH   34  534 274 HOH   HOH A . 
D 4 HOH   35  535 251 HOH   HOH A . 
D 4 HOH   36  536 292 HOH   HOH A . 
D 4 HOH   37  537 333 HOH   HOH A . 
D 4 HOH   38  538 25  HOH   HOH A . 
D 4 HOH   39  539 114 HOH   HOH A . 
D 4 HOH   40  540 180 HOH   HOH A . 
D 4 HOH   41  541 12  HOH   HOH A . 
D 4 HOH   42  542 389 HOH   HOH A . 
D 4 HOH   43  543 311 HOH   HOH A . 
D 4 HOH   44  544 159 HOH   HOH A . 
D 4 HOH   45  545 82  HOH   HOH A . 
D 4 HOH   46  546 335 HOH   HOH A . 
D 4 HOH   47  547 231 HOH   HOH A . 
D 4 HOH   48  548 249 HOH   HOH A . 
D 4 HOH   49  549 6   HOH   HOH A . 
D 4 HOH   50  550 95  HOH   HOH A . 
D 4 HOH   51  551 247 HOH   HOH A . 
D 4 HOH   52  552 343 HOH   HOH A . 
D 4 HOH   53  553 211 HOH   HOH A . 
D 4 HOH   54  554 42  HOH   HOH A . 
D 4 HOH   55  555 131 HOH   HOH A . 
D 4 HOH   56  556 408 HOH   HOH A . 
D 4 HOH   57  557 89  HOH   HOH A . 
D 4 HOH   58  558 36  HOH   HOH A . 
D 4 HOH   59  559 33  HOH   HOH A . 
D 4 HOH   60  560 257 HOH   HOH A . 
D 4 HOH   61  561 1   HOH   HOH A . 
D 4 HOH   62  562 75  HOH   HOH A . 
D 4 HOH   63  563 15  HOH   HOH A . 
D 4 HOH   64  564 115 HOH   HOH A . 
D 4 HOH   65  565 22  HOH   HOH A . 
D 4 HOH   66  566 50  HOH   HOH A . 
D 4 HOH   67  567 236 HOH   HOH A . 
D 4 HOH   68  568 294 HOH   HOH A . 
D 4 HOH   69  569 56  HOH   HOH A . 
D 4 HOH   70  570 17  HOH   HOH A . 
D 4 HOH   71  571 92  HOH   HOH A . 
D 4 HOH   72  572 51  HOH   HOH A . 
D 4 HOH   73  573 265 HOH   HOH A . 
D 4 HOH   74  574 245 HOH   HOH A . 
D 4 HOH   75  575 396 HOH   HOH A . 
D 4 HOH   76  576 325 HOH   HOH A . 
D 4 HOH   77  577 266 HOH   HOH A . 
D 4 HOH   78  578 11  HOH   HOH A . 
D 4 HOH   79  579 215 HOH   HOH A . 
D 4 HOH   80  580 137 HOH   HOH A . 
D 4 HOH   81  581 193 HOH   HOH A . 
D 4 HOH   82  582 297 HOH   HOH A . 
D 4 HOH   83  583 262 HOH   HOH A . 
D 4 HOH   84  584 173 HOH   HOH A . 
D 4 HOH   85  585 162 HOH   HOH A . 
D 4 HOH   86  586 124 HOH   HOH A . 
D 4 HOH   87  587 62  HOH   HOH A . 
D 4 HOH   88  588 14  HOH   HOH A . 
D 4 HOH   89  589 316 HOH   HOH A . 
D 4 HOH   90  590 312 HOH   HOH A . 
D 4 HOH   91  591 379 HOH   HOH A . 
D 4 HOH   92  592 117 HOH   HOH A . 
D 4 HOH   93  593 98  HOH   HOH A . 
D 4 HOH   94  594 314 HOH   HOH A . 
D 4 HOH   95  595 45  HOH   HOH A . 
D 4 HOH   96  596 278 HOH   HOH A . 
D 4 HOH   97  597 225 HOH   HOH A . 
D 4 HOH   98  598 149 HOH   HOH A . 
D 4 HOH   99  599 181 HOH   HOH A . 
D 4 HOH   100 600 2   HOH   HOH A . 
D 4 HOH   101 601 47  HOH   HOH A . 
D 4 HOH   102 602 144 HOH   HOH A . 
D 4 HOH   103 603 246 HOH   HOH A . 
D 4 HOH   104 604 299 HOH   HOH A . 
D 4 HOH   105 605 152 HOH   HOH A . 
D 4 HOH   106 606 31  HOH   HOH A . 
D 4 HOH   107 607 64  HOH   HOH A . 
D 4 HOH   108 608 38  HOH   HOH A . 
D 4 HOH   109 609 28  HOH   HOH A . 
D 4 HOH   110 610 68  HOH   HOH A . 
D 4 HOH   111 611 368 HOH   HOH A . 
D 4 HOH   112 612 93  HOH   HOH A . 
D 4 HOH   113 613 61  HOH   HOH A . 
D 4 HOH   114 614 334 HOH   HOH A . 
D 4 HOH   115 615 286 HOH   HOH A . 
D 4 HOH   116 616 155 HOH   HOH A . 
D 4 HOH   117 617 216 HOH   HOH A . 
D 4 HOH   118 618 192 HOH   HOH A . 
D 4 HOH   119 619 29  HOH   HOH A . 
D 4 HOH   120 620 18  HOH   HOH A . 
D 4 HOH   121 621 244 HOH   HOH A . 
D 4 HOH   122 622 223 HOH   HOH A . 
D 4 HOH   123 623 221 HOH   HOH A . 
D 4 HOH   124 624 143 HOH   HOH A . 
D 4 HOH   125 625 10  HOH   HOH A . 
D 4 HOH   126 626 197 HOH   HOH A . 
D 4 HOH   127 627 97  HOH   HOH A . 
D 4 HOH   128 628 232 HOH   HOH A . 
D 4 HOH   129 629 35  HOH   HOH A . 
D 4 HOH   130 630 119 HOH   HOH A . 
D 4 HOH   131 631 118 HOH   HOH A . 
D 4 HOH   132 632 27  HOH   HOH A . 
D 4 HOH   133 633 63  HOH   HOH A . 
D 4 HOH   134 634 250 HOH   HOH A . 
D 4 HOH   135 635 48  HOH   HOH A . 
D 4 HOH   136 636 121 HOH   HOH A . 
D 4 HOH   137 637 39  HOH   HOH A . 
D 4 HOH   138 638 264 HOH   HOH A . 
D 4 HOH   139 639 306 HOH   HOH A . 
D 4 HOH   140 640 32  HOH   HOH A . 
D 4 HOH   141 641 187 HOH   HOH A . 
D 4 HOH   142 642 9   HOH   HOH A . 
D 4 HOH   143 643 78  HOH   HOH A . 
D 4 HOH   144 644 315 HOH   HOH A . 
D 4 HOH   145 645 189 HOH   HOH A . 
D 4 HOH   146 646 161 HOH   HOH A . 
D 4 HOH   147 647 7   HOH   HOH A . 
D 4 HOH   148 648 52  HOH   HOH A . 
D 4 HOH   149 649 374 HOH   HOH A . 
D 4 HOH   150 650 128 HOH   HOH A . 
D 4 HOH   151 651 273 HOH   HOH A . 
D 4 HOH   152 652 165 HOH   HOH A . 
D 4 HOH   153 653 30  HOH   HOH A . 
D 4 HOH   154 654 261 HOH   HOH A . 
D 4 HOH   155 655 267 HOH   HOH A . 
D 4 HOH   156 656 58  HOH   HOH A . 
D 4 HOH   157 657 212 HOH   HOH A . 
D 4 HOH   158 658 164 HOH   HOH A . 
D 4 HOH   159 659 230 HOH   HOH A . 
D 4 HOH   160 660 300 HOH   HOH A . 
D 4 HOH   161 661 66  HOH   HOH A . 
D 4 HOH   162 662 139 HOH   HOH A . 
D 4 HOH   163 663 26  HOH   HOH A . 
D 4 HOH   164 664 136 HOH   HOH A . 
D 4 HOH   165 665 16  HOH   HOH A . 
D 4 HOH   166 666 203 HOH   HOH A . 
D 4 HOH   167 667 220 HOH   HOH A . 
D 4 HOH   168 668 84  HOH   HOH A . 
D 4 HOH   169 669 79  HOH   HOH A . 
D 4 HOH   170 670 404 HOH   HOH A . 
D 4 HOH   171 671 272 HOH   HOH A . 
D 4 HOH   172 672 148 HOH   HOH A . 
D 4 HOH   173 673 269 HOH   HOH A . 
D 4 HOH   174 674 37  HOH   HOH A . 
D 4 HOH   175 675 363 HOH   HOH A . 
D 4 HOH   176 676 402 HOH   HOH A . 
D 4 HOH   177 677 65  HOH   HOH A . 
D 4 HOH   178 678 227 HOH   HOH A . 
D 4 HOH   179 679 256 HOH   HOH A . 
D 4 HOH   180 680 304 HOH   HOH A . 
D 4 HOH   181 681 8   HOH   HOH A . 
D 4 HOH   182 682 138 HOH   HOH A . 
D 4 HOH   183 683 4   HOH   HOH A . 
D 4 HOH   184 684 125 HOH   HOH A . 
D 4 HOH   185 685 287 HOH   HOH A . 
D 4 HOH   186 686 177 HOH   HOH A . 
D 4 HOH   187 687 3   HOH   HOH A . 
D 4 HOH   188 688 175 HOH   HOH A . 
D 4 HOH   189 689 83  HOH   HOH A . 
D 4 HOH   190 690 157 HOH   HOH A . 
D 4 HOH   191 691 60  HOH   HOH A . 
D 4 HOH   192 692 275 HOH   HOH A . 
D 4 HOH   193 693 34  HOH   HOH A . 
D 4 HOH   194 694 40  HOH   HOH A . 
D 4 HOH   195 695 195 HOH   HOH A . 
D 4 HOH   196 696 5   HOH   HOH A . 
D 4 HOH   197 697 178 HOH   HOH A . 
D 4 HOH   198 698 13  HOH   HOH A . 
D 4 HOH   199 699 321 HOH   HOH A . 
D 4 HOH   200 700 399 HOH   HOH A . 
D 4 HOH   201 701 19  HOH   HOH A . 
D 4 HOH   202 702 140 HOH   HOH A . 
D 4 HOH   203 703 407 HOH   HOH A . 
D 4 HOH   204 704 20  HOH   HOH A . 
D 4 HOH   205 705 72  HOH   HOH A . 
D 4 HOH   206 706 135 HOH   HOH A . 
D 4 HOH   207 707 243 HOH   HOH A . 
D 4 HOH   208 708 99  HOH   HOH A . 
D 4 HOH   209 709 41  HOH   HOH A . 
D 4 HOH   210 710 226 HOH   HOH A . 
D 4 HOH   211 711 168 HOH   HOH A . 
D 4 HOH   212 712 107 HOH   HOH A . 
D 4 HOH   213 713 209 HOH   HOH A . 
D 4 HOH   214 714 394 HOH   HOH A . 
D 4 HOH   215 715 308 HOH   HOH A . 
D 4 HOH   216 716 222 HOH   HOH A . 
D 4 HOH   217 717 239 HOH   HOH A . 
D 4 HOH   218 718 102 HOH   HOH A . 
D 4 HOH   219 719 190 HOH   HOH A . 
D 4 HOH   220 720 412 HOH   HOH A . 
D 4 HOH   221 721 224 HOH   HOH A . 
D 4 HOH   222 722 24  HOH   HOH A . 
D 4 HOH   223 723 196 HOH   HOH A . 
D 4 HOH   224 724 85  HOH   HOH A . 
D 4 HOH   225 725 69  HOH   HOH A . 
D 4 HOH   226 726 57  HOH   HOH A . 
D 4 HOH   227 727 70  HOH   HOH A . 
D 4 HOH   228 728 349 HOH   HOH A . 
D 4 HOH   229 729 106 HOH   HOH A . 
D 4 HOH   230 730 205 HOH   HOH A . 
D 4 HOH   231 731 346 HOH   HOH A . 
D 4 HOH   232 732 90  HOH   HOH A . 
D 4 HOH   233 733 398 HOH   HOH A . 
D 4 HOH   234 734 77  HOH   HOH A . 
D 4 HOH   235 735 111 HOH   HOH A . 
D 4 HOH   236 736 355 HOH   HOH A . 
D 4 HOH   237 737 151 HOH   HOH A . 
D 4 HOH   238 738 54  HOH   HOH A . 
D 4 HOH   239 739 80  HOH   HOH A . 
D 4 HOH   240 740 81  HOH   HOH A . 
D 4 HOH   241 741 290 HOH   HOH A . 
D 4 HOH   242 742 163 HOH   HOH A . 
D 4 HOH   243 743 67  HOH   HOH A . 
D 4 HOH   244 744 337 HOH   HOH A . 
D 4 HOH   245 745 357 HOH   HOH A . 
D 4 HOH   246 746 120 HOH   HOH A . 
D 4 HOH   247 747 46  HOH   HOH A . 
D 4 HOH   248 748 113 HOH   HOH A . 
D 4 HOH   249 749 309 HOH   HOH A . 
D 4 HOH   250 750 53  HOH   HOH A . 
D 4 HOH   251 751 43  HOH   HOH A . 
D 4 HOH   252 752 23  HOH   HOH A . 
D 4 HOH   253 753 352 HOH   HOH A . 
D 4 HOH   254 754 320 HOH   HOH A . 
D 4 HOH   255 755 248 HOH   HOH A . 
D 4 HOH   256 756 96  HOH   HOH A . 
D 4 HOH   257 757 322 HOH   HOH A . 
D 4 HOH   258 758 369 HOH   HOH A . 
D 4 HOH   259 759 391 HOH   HOH A . 
D 4 HOH   260 760 207 HOH   HOH A . 
D 4 HOH   261 761 351 HOH   HOH A . 
D 4 HOH   262 762 103 HOH   HOH A . 
D 4 HOH   263 763 279 HOH   HOH A . 
D 4 HOH   264 764 293 HOH   HOH A . 
D 4 HOH   265 765 73  HOH   HOH A . 
D 4 HOH   266 766 108 HOH   HOH A . 
D 4 HOH   267 767 234 HOH   HOH A . 
D 4 HOH   268 768 21  HOH   HOH A . 
D 4 HOH   269 769 141 HOH   HOH A . 
D 4 HOH   270 770 365 HOH   HOH A . 
D 4 HOH   271 771 336 HOH   HOH A . 
D 4 HOH   272 772 409 HOH   HOH A . 
D 4 HOH   273 773 382 HOH   HOH A . 
D 4 HOH   274 774 101 HOH   HOH A . 
D 4 HOH   275 775 280 HOH   HOH A . 
D 4 HOH   276 776 132 HOH   HOH A . 
D 4 HOH   277 777 206 HOH   HOH A . 
D 4 HOH   278 778 153 HOH   HOH A . 
D 4 HOH   279 779 74  HOH   HOH A . 
D 4 HOH   280 780 358 HOH   HOH A . 
D 4 HOH   281 781 214 HOH   HOH A . 
D 4 HOH   282 782 353 HOH   HOH A . 
D 4 HOH   283 783 258 HOH   HOH A . 
D 4 HOH   284 784 387 HOH   HOH A . 
D 4 HOH   285 785 323 HOH   HOH A . 
D 4 HOH   286 786 383 HOH   HOH A . 
D 4 HOH   287 787 158 HOH   HOH A . 
D 4 HOH   288 788 146 HOH   HOH A . 
D 4 HOH   289 789 377 HOH   HOH A . 
D 4 HOH   290 790 183 HOH   HOH A . 
D 4 HOH   291 791 116 HOH   HOH A . 
D 4 HOH   292 792 176 HOH   HOH A . 
D 4 HOH   293 793 375 HOH   HOH A . 
D 4 HOH   294 794 110 HOH   HOH A . 
D 4 HOH   295 795 329 HOH   HOH A . 
D 4 HOH   296 796 366 HOH   HOH A . 
D 4 HOH   297 797 202 HOH   HOH A . 
D 4 HOH   298 798 414 HOH   HOH A . 
D 4 HOH   299 799 86  HOH   HOH A . 
D 4 HOH   300 800 147 HOH   HOH A . 
D 4 HOH   301 801 301 HOH   HOH A . 
D 4 HOH   302 802 277 HOH   HOH A . 
D 4 HOH   303 803 200 HOH   HOH A . 
D 4 HOH   304 804 386 HOH   HOH A . 
D 4 HOH   305 805 298 HOH   HOH A . 
D 4 HOH   306 806 360 HOH   HOH A . 
D 4 HOH   307 807 342 HOH   HOH A . 
D 4 HOH   308 808 317 HOH   HOH A . 
D 4 HOH   309 809 188 HOH   HOH A . 
D 4 HOH   310 810 310 HOH   HOH A . 
D 4 HOH   311 811 288 HOH   HOH A . 
D 4 HOH   312 812 364 HOH   HOH A . 
D 4 HOH   313 813 186 HOH   HOH A . 
D 4 HOH   314 814 255 HOH   HOH A . 
D 4 HOH   315 815 350 HOH   HOH A . 
D 4 HOH   316 816 154 HOH   HOH A . 
D 4 HOH   317 817 276 HOH   HOH A . 
D 4 HOH   318 818 388 HOH   HOH A . 
D 4 HOH   319 819 228 HOH   HOH A . 
D 4 HOH   320 820 104 HOH   HOH A . 
D 4 HOH   321 821 313 HOH   HOH A . 
D 4 HOH   322 822 134 HOH   HOH A . 
D 4 HOH   323 823 112 HOH   HOH A . 
D 4 HOH   324 824 390 HOH   HOH A . 
D 4 HOH   325 825 150 HOH   HOH A . 
D 4 HOH   326 826 105 HOH   HOH A . 
D 4 HOH   327 827 381 HOH   HOH A . 
D 4 HOH   328 828 156 HOH   HOH A . 
D 4 HOH   329 829 242 HOH   HOH A . 
D 4 HOH   330 830 403 HOH   HOH A . 
D 4 HOH   331 831 284 HOH   HOH A . 
D 4 HOH   332 832 71  HOH   HOH A . 
D 4 HOH   333 833 331 HOH   HOH A . 
D 4 HOH   334 834 307 HOH   HOH A . 
D 4 HOH   335 835 281 HOH   HOH A . 
D 4 HOH   336 836 169 HOH   HOH A . 
D 4 HOH   337 837 252 HOH   HOH A . 
D 4 HOH   338 838 347 HOH   HOH A . 
D 4 HOH   339 839 182 HOH   HOH A . 
D 4 HOH   340 840 282 HOH   HOH A . 
D 4 HOH   341 841 218 HOH   HOH A . 
D 4 HOH   342 842 208 HOH   HOH A . 
D 4 HOH   343 843 361 HOH   HOH A . 
D 4 HOH   344 844 326 HOH   HOH A . 
D 4 HOH   345 845 413 HOH   HOH A . 
D 4 HOH   346 846 237 HOH   HOH A . 
D 4 HOH   347 847 171 HOH   HOH A . 
D 4 HOH   348 848 289 HOH   HOH A . 
D 4 HOH   349 849 241 HOH   HOH A . 
D 4 HOH   350 850 229 HOH   HOH A . 
D 4 HOH   351 851 362 HOH   HOH A . 
D 4 HOH   352 852 395 HOH   HOH A . 
D 4 HOH   353 853 145 HOH   HOH A . 
D 4 HOH   354 854 238 HOH   HOH A . 
D 4 HOH   355 855 59  HOH   HOH A . 
D 4 HOH   356 856 406 HOH   HOH A . 
D 4 HOH   357 857 376 HOH   HOH A . 
D 4 HOH   358 858 359 HOH   HOH A . 
D 4 HOH   359 859 384 HOH   HOH A . 
D 4 HOH   360 860 367 HOH   HOH A . 
D 4 HOH   361 861 210 HOH   HOH A . 
D 4 HOH   362 862 94  HOH   HOH A . 
D 4 HOH   363 863 170 HOH   HOH A . 
D 4 HOH   364 864 199 HOH   HOH A . 
D 4 HOH   365 865 174 HOH   HOH A . 
D 4 HOH   366 866 268 HOH   HOH A . 
D 4 HOH   367 867 305 HOH   HOH A . 
D 4 HOH   368 868 271 HOH   HOH A . 
D 4 HOH   369 869 380 HOH   HOH A . 
D 4 HOH   370 870 378 HOH   HOH A . 
D 4 HOH   371 871 235 HOH   HOH A . 
D 4 HOH   372 872 344 HOH   HOH A . 
D 4 HOH   373 873 240 HOH   HOH A . 
D 4 HOH   374 874 295 HOH   HOH A . 
D 4 HOH   375 875 356 HOH   HOH A . 
D 4 HOH   376 876 185 HOH   HOH A . 
D 4 HOH   377 877 213 HOH   HOH A . 
D 4 HOH   378 878 263 HOH   HOH A . 
D 4 HOH   379 879 283 HOH   HOH A . 
D 4 HOH   380 880 405 HOH   HOH A . 
D 4 HOH   381 881 179 HOH   HOH A . 
D 4 HOH   382 882 233 HOH   HOH A . 
D 4 HOH   383 883 370 HOH   HOH A . 
D 4 HOH   384 884 160 HOH   HOH A . 
D 4 HOH   385 885 260 HOH   HOH A . 
D 4 HOH   386 886 318 HOH   HOH A . 
D 4 HOH   387 887 100 HOH   HOH A . 
D 4 HOH   388 888 296 HOH   HOH A . 
D 4 HOH   389 889 172 HOH   HOH A . 
D 4 HOH   390 890 184 HOH   HOH A . 
D 4 HOH   391 891 254 HOH   HOH A . 
D 4 HOH   392 892 397 HOH   HOH A . 
D 4 HOH   393 893 217 HOH   HOH A . 
D 4 HOH   394 894 76  HOH   HOH A . 
D 4 HOH   395 895 270 HOH   HOH A . 
D 4 HOH   396 896 400 HOH   HOH A . 
D 4 HOH   397 897 198 HOH   HOH A . 
D 4 HOH   398 898 87  HOH   HOH A . 
D 4 HOH   399 899 410 HOH   HOH A . 
D 4 HOH   400 900 319 HOH   HOH A . 
D 4 HOH   401 901 219 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 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H0X 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.914 
_cell.length_a_esd                 ? 
_cell.length_b                     74.950 
_cell.length_b_esd                 ? 
_cell.length_c                     76.129 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H0X 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H0X 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.62 
_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 
_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    'JSCG+ condition F16: 0.1 M HEPES pH 7, 30% Jeff-M-600' 
_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         2022-07-15 
_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   1.033202 
_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        1.033202 
_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                                       9H0X 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.36 
_reflns.d_resolution_low                               47.08 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     72913 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.86 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.083 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       776332 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_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                                    1.36 
_reflns_shell.d_res_low                                     1.44 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           113983 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10514 
_reflns_shell.percent_possible_obs                          99.2 
_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                               10.8 
_reflns_shell.pdbx_chi_squared                              0.64 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.6 
_reflns_shell.pdbx_Rrim_I_all                               0.895 
_reflns_shell.pdbx_Rpim_I_all                               0.266 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.863 
_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                                  0.853 
_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                                 9H0X 
_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                            1.36 
_refine.ls_d_res_low                             47.08 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     72837 
_refine.ls_number_reflns_R_free                  3518 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.06 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1493 
_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                       0.1484 
_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                          1.35 
_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                 16.02 
_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                            0.10 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2603 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             402 
_refine_hist.number_atoms_total               3039 
_refine_hist.d_res_high                       1.36 
_refine_hist.d_res_low                        47.08 
# 
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' ? 0.016  ? 2780 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.448  ? 3772 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.943 ? 1044 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.101  ? 370  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.017  ? 507  ? 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' 1.36 1.38  . . 138 2732 99.00  . . . . 0.2267 . . . . . . . . . . . 0.2539 
'X-RAY DIFFRACTION' 1.38 1.40  . . 125 2741 99.00  . . . . 0.2168 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 1.40 1.42  . . 133 2768 99.00  . . . . 0.2088 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 1.42 1.45  . . 135 2727 99.00  . . . . 0.1967 . . . . . . . . . . . 0.2411 
'X-RAY DIFFRACTION' 1.45 1.47  . . 131 2746 99.00  . . . . 0.1890 . . . . . . . . . . . 0.2006 
'X-RAY DIFFRACTION' 1.47 1.50  . . 125 2774 99.00  . . . . 0.1745 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 1.50 1.52  . . 147 2736 100.00 . . . . 0.1718 . . . . . . . . . . . 0.1812 
'X-RAY DIFFRACTION' 1.52 1.55  . . 147 2750 99.00  . . . . 0.1657 . . . . . . . . . . . 0.1886 
'X-RAY DIFFRACTION' 1.55 1.58  . . 123 2750 99.00  . . . . 0.1554 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 1.58 1.62  . . 117 2755 98.00  . . . . 0.1515 . . . . . . . . . . . 0.1786 
'X-RAY DIFFRACTION' 1.62 1.66  . . 139 2718 98.00  . . . . 0.1490 . . . . . . . . . . . 0.1766 
'X-RAY DIFFRACTION' 1.66 1.70  . . 151 2762 99.00  . . . . 0.1491 . . . . . . . . . . . 0.1802 
'X-RAY DIFFRACTION' 1.70 1.74  . . 126 2755 99.00  . . . . 0.1442 . . . . . . . . . . . 0.1623 
'X-RAY DIFFRACTION' 1.74 1.79  . . 137 2752 99.00  . . . . 0.1439 . . . . . . . . . . . 0.1604 
'X-RAY DIFFRACTION' 1.79 1.85  . . 166 2757 100.00 . . . . 0.1475 . . . . . . . . . . . 0.1862 
'X-RAY DIFFRACTION' 1.85 1.92  . . 146 2776 99.00  . . . . 0.1492 . . . . . . . . . . . 0.1490 
'X-RAY DIFFRACTION' 1.92 1.99  . . 135 2787 100.00 . . . . 0.1453 . . . . . . . . . . . 0.1588 
'X-RAY DIFFRACTION' 1.99 2.09  . . 150 2774 100.00 . . . . 0.1424 . . . . . . . . . . . 0.1603 
'X-RAY DIFFRACTION' 2.09 2.20  . . 147 2741 98.00  . . . . 0.1353 . . . . . . . . . . . 0.1755 
'X-RAY DIFFRACTION' 2.20 2.33  . . 122 2782 98.00  . . . . 0.1375 . . . . . . . . . . . 0.1520 
'X-RAY DIFFRACTION' 2.33 2.51  . . 138 2815 99.00  . . . . 0.1357 . . . . . . . . . . . 0.1517 
'X-RAY DIFFRACTION' 2.51 2.77  . . 174 2783 100.00 . . . . 0.1487 . . . . . . . . . . . 0.1793 
'X-RAY DIFFRACTION' 2.77 3.17  . . 162 2820 99.00  . . . . 0.1529 . . . . . . . . . . . 0.1601 
'X-RAY DIFFRACTION' 3.17 3.99  . . 159 2849 99.00  . . . . 0.1345 . . . . . . . . . . . 0.1406 
'X-RAY DIFFRACTION' 3.99 47.08 . . 145 2969 98.00  . . . . 0.1487 . . . . . . . . . . . 0.1636 
# 
_struct.entry_id                     9H0X 
_struct.title                        'ProA in complex with inhibitor 6' 
_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        9H0X 
_struct_keywords.text            'inhibitor, ProA, Legionella pneumophila, 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 4 ? 
# 
_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              9H0X 
_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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  14460 ? 
# 
_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 
# 
_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 34  ? VAL A 36  ? SER A 34  VAL A 36  5 ? 3  
HELX_P HELX_P2  AA2 SER A 95  ? GLY A 116 ? SER A 95  GLY A 116 1 ? 22 
HELX_P HELX_P3  AA3 SER A 164 ? HIS A 180 ? SER A 164 HIS A 180 1 ? 17 
HELX_P HELX_P4  AA4 PHE A 186 ? GLY A 210 ? PHE A 186 GLY A 210 1 ? 25 
HELX_P HELX_P5  AA5 GLY A 217 ? MET A 221 ? GLY A 217 MET A 221 5 ? 5  
HELX_P HELX_P6  AA6 LYS A 222 ? GLY A 226 ? LYS A 222 GLY A 226 5 ? 5  
HELX_P HELX_P7  AA7 LYS A 235 ? GLY A 240 ? LYS A 235 GLY A 240 5 ? 6  
HELX_P HELX_P8  AA8 VAL A 245 ? TYR A 249 ? VAL A 245 TYR A 249 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 254 ? SER A 259 ? ASP A 254 SER A 259 1 ? 6  
HELX_P HELX_P10 AB1 SER A 259 ? ASN A 271 ? SER A 259 ASN A 271 1 ? 13 
HELX_P HELX_P11 AB2 ASN A 276 ? TYR A 291 ? ASN A 276 TYR A 291 1 ? 16 
HELX_P HELX_P12 AB3 THR A 297 ? GLY A 313 ? THR A 297 GLY A 313 1 ? 17 
HELX_P HELX_P13 AB4 ASN A 315 ? VAL A 326 ? ASN A 315 VAL A 326 1 ? 12 
# 
_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 ? ? ? ? ? ? ? 2.071 ? ? 
disulf2 disulf ? ? A CYS   303 SG  A ? ? 1_555 A CYS 333 SG A ? A CYS   303 A CYS 333 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
disulf3 disulf ? ? A CYS   303 SG  B ? ? 1_555 A CYS 333 SG B ? A CYS   303 A CYS 333 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc1 metalc ? ? A HIS   170 NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS   170 A ZN  402 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc2 metalc ? ? A HIS   174 NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS   174 A ZN  402 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc3 metalc ? ? A GLU   194 OE2 ? ? ? 1_555 C ZN  .   ZN ? ? A GLU   194 A ZN  402 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc4 metalc ? ? B A1IRK .   O1  ? ? ? 1_555 C ZN  .   ZN ? ? A A1IRK 401 A ZN  402 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc5 metalc ? ? B A1IRK .   O5  ? ? ? 1_555 C ZN  .   ZN ? ? A A1IRK 401 A ZN  402 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
# 
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 ? C ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS   174 ? A HIS   174 ? 1_555 97.5  ? 
2  NE2 ? A HIS   170 ? A HIS   170 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 OE2 ? A GLU   194 ? A GLU   194 ? 1_555 125.5 ? 
3  NE2 ? A HIS   174 ? A HIS   174 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 OE2 ? A GLU   194 ? A GLU   194 ? 1_555 90.8  ? 
4  NE2 ? A HIS   170 ? A HIS   170 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O1  ? B A1IRK .   ? A A1IRK 401 ? 1_555 106.2 ? 
5  NE2 ? A HIS   174 ? A HIS   174 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O1  ? B A1IRK .   ? A A1IRK 401 ? 1_555 93.6  ? 
6  OE2 ? A GLU   194 ? A GLU   194 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O1  ? B A1IRK .   ? A A1IRK 401 ? 1_555 127.0 ? 
7  NE2 ? A HIS   170 ? A HIS   170 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O5  ? B A1IRK .   ? A A1IRK 401 ? 1_555 90.2  ? 
8  NE2 ? A HIS   174 ? A HIS   174 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O5  ? B A1IRK .   ? A A1IRK 401 ? 1_555 169.0 ? 
9  OE2 ? A GLU   194 ? A GLU   194 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O5  ? B A1IRK .   ? A A1IRK 401 ? 1_555 91.1  ? 
10 O1  ? B A1IRK .   ? A A1IRK 401 ? 1_555 ZN ? C ZN . ? A ZN 402 ? 1_555 O5  ? B A1IRK .   ? A A1IRK 401 ? 1_555 76.6  ? 
# 
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 A CYS A 333 A CYS A 303 ? 1_555 CYS A 333 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 303 B CYS A 333 B 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 GLY A 7   ? N GLY A 7   O LEU A 28  ? O LEU A 28  
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                   9H0X 
_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 856 ? ? O A HOH 880 ? ? 1.86 
2 1 O A HOH 676 ? ? O A HOH 764 ? ? 1.86 
3 1 O A HOH 506 ? ? O A HOH 575 ? ? 1.88 
4 1 O A HOH 758 ? ? O A HOH 892 ? ? 1.99 
5 1 O A HOH 546 ? ? O A HOH 798 ? ? 2.09 
6 1 O A HOH 808 ? ? O A HOH 821 ? ? 2.14 
7 1 O A HOH 644 ? ? O A HOH 827 ? ? 2.15 
8 1 O A HOH 622 ? ? O A HOH 841 ? ? 2.16 
9 1 O A HOH 767 ? ? O A HOH 841 ? ? 2.19 
# 
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  ? ? -140.41 -65.16  
2  1 ASP A 88  ? ? -152.35 63.95   
3  1 SER A 95  ? ? -167.54 87.22   
4  1 GLU A 141 ? ? -98.38  59.87   
5  1 LYS A 148 ? ? -143.64 -17.07  
6  1 ASP A 156 ? ? -158.72 -124.70 
7  1 HIS A 180 ? ? -117.61 -97.75  
8  1 TYR A 185 ? ? -85.63  47.62   
9  1 LYS A 235 ? ? -158.60 83.18   
10 1 MET A 241 ? ? -141.03 -32.19  
# 
_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     238 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.154 
_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         -13.9156 
_pdbx_refine_tls.origin_y         14.4324 
_pdbx_refine_tls.origin_z         -17.2370 
_pdbx_refine_tls.T[1][1]          0.1133 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0097 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0100 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0878 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0036 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1105 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.1473 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.4787 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.5174 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7300 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2791 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.3245 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0284 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0629 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0011 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0675 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0136 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0332 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0248 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0125 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0092 
_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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 900 ? 5.87 . 
2 1 O ? A HOH 901 ? 6.13 . 
# 
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 THR 72  ? A THR 72  
3 1 Y 1 A GLN 73  ? A GLN 73  
4 1 Y 1 A SER 74  ? A SER 74  
5 1 Y 1 A VAL 335 ? A VAL 335 
6 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 
A1IRK C1   C  Y N 1   
A1IRK C2   C  Y N 2   
A1IRK C3   C  Y N 3   
A1IRK C4   C  Y N 4   
A1IRK C5   C  Y N 5   
A1IRK C6   C  Y N 6   
A1IRK C8   C  N R 7   
A1IRK C9   C  N N 8   
A1IRK C10  C  N N 9   
A1IRK C11  C  Y N 10  
A1IRK C12  C  Y N 11  
A1IRK C13  C  N N 12  
A1IRK C14  C  N N 13  
A1IRK C15  C  N N 14  
A1IRK C16  C  N N 15  
A1IRK C17  C  N N 16  
A1IRK C18  C  N N 17  
A1IRK C19  C  N N 18  
A1IRK C20  C  N N 19  
A1IRK C21  C  N N 20  
A1IRK C7   C  N N 21  
A1IRK N1   N  N N 22  
A1IRK N2   N  N N 23  
A1IRK N3   N  Y N 24  
A1IRK N4   N  Y N 25  
A1IRK N5   N  Y N 26  
A1IRK N6   N  N N 27  
A1IRK O1   O  N N 28  
A1IRK O2   O  N N 29  
A1IRK O3   O  N N 30  
A1IRK O4   O  N N 31  
A1IRK O5   O  N N 32  
A1IRK S1   S  N N 33  
A1IRK H3   H  N N 34  
A1IRK H4   H  N N 35  
A1IRK H5   H  N N 36  
A1IRK H6   H  N N 37  
A1IRK H1   H  N N 38  
A1IRK H10  H  N N 39  
A1IRK H9   H  N N 40  
A1IRK H11  H  N N 41  
A1IRK H12  H  N N 42  
A1IRK H13  H  N N 43  
A1IRK H16  H  N N 44  
A1IRK H15  H  N N 45  
A1IRK H17  H  N N 46  
A1IRK H18  H  N N 47  
A1IRK H19  H  N N 48  
A1IRK H20  H  N N 49  
A1IRK H23  H  N N 50  
A1IRK H21  H  N N 51  
A1IRK H22  H  N N 52  
A1IRK H25  H  N N 53  
A1IRK H24  H  N N 54  
A1IRK H26  H  N N 55  
A1IRK H28  H  N N 56  
A1IRK H27  H  N N 57  
A1IRK H29  H  N N 58  
A1IRK H30  H  N N 59  
A1IRK H32  H  N N 60  
A1IRK H31  H  N N 61  
A1IRK H7   H  N N 62  
A1IRK H8   H  N N 63  
A1IRK H14  H  N N 64  
A1IRK H2   H  N N 65  
ALA   N    N  N N 66  
ALA   CA   C  N S 67  
ALA   C    C  N N 68  
ALA   O    O  N N 69  
ALA   CB   C  N N 70  
ALA   OXT  O  N N 71  
ALA   H    H  N N 72  
ALA   H2   H  N N 73  
ALA   HA   H  N N 74  
ALA   HB1  H  N N 75  
ALA   HB2  H  N N 76  
ALA   HB3  H  N N 77  
ALA   HXT  H  N N 78  
ARG   N    N  N N 79  
ARG   CA   C  N S 80  
ARG   C    C  N N 81  
ARG   O    O  N N 82  
ARG   CB   C  N N 83  
ARG   CG   C  N N 84  
ARG   CD   C  N N 85  
ARG   NE   N  N N 86  
ARG   CZ   C  N N 87  
ARG   NH1  N  N N 88  
ARG   NH2  N  N N 89  
ARG   OXT  O  N N 90  
ARG   H    H  N N 91  
ARG   H2   H  N N 92  
ARG   HA   H  N N 93  
ARG   HB2  H  N N 94  
ARG   HB3  H  N N 95  
ARG   HG2  H  N N 96  
ARG   HG3  H  N N 97  
ARG   HD2  H  N N 98  
ARG   HD3  H  N N 99  
ARG   HE   H  N N 100 
ARG   HH11 H  N N 101 
ARG   HH12 H  N N 102 
ARG   HH21 H  N N 103 
ARG   HH22 H  N N 104 
ARG   HXT  H  N N 105 
ASN   N    N  N N 106 
ASN   CA   C  N S 107 
ASN   C    C  N N 108 
ASN   O    O  N N 109 
ASN   CB   C  N N 110 
ASN   CG   C  N N 111 
ASN   OD1  O  N N 112 
ASN   ND2  N  N N 113 
ASN   OXT  O  N N 114 
ASN   H    H  N N 115 
ASN   H2   H  N N 116 
ASN   HA   H  N N 117 
ASN   HB2  H  N N 118 
ASN   HB3  H  N N 119 
ASN   HD21 H  N N 120 
ASN   HD22 H  N N 121 
ASN   HXT  H  N N 122 
ASP   N    N  N N 123 
ASP   CA   C  N S 124 
ASP   C    C  N N 125 
ASP   O    O  N N 126 
ASP   CB   C  N N 127 
ASP   CG   C  N N 128 
ASP   OD1  O  N N 129 
ASP   OD2  O  N N 130 
ASP   OXT  O  N N 131 
ASP   H    H  N N 132 
ASP   H2   H  N N 133 
ASP   HA   H  N N 134 
ASP   HB2  H  N N 135 
ASP   HB3  H  N N 136 
ASP   HD2  H  N N 137 
ASP   HXT  H  N N 138 
CYS   N    N  N N 139 
CYS   CA   C  N R 140 
CYS   C    C  N N 141 
CYS   O    O  N N 142 
CYS   CB   C  N N 143 
CYS   SG   S  N N 144 
CYS   OXT  O  N N 145 
CYS   H    H  N N 146 
CYS   H2   H  N N 147 
CYS   HA   H  N N 148 
CYS   HB2  H  N N 149 
CYS   HB3  H  N N 150 
CYS   HG   H  N N 151 
CYS   HXT  H  N N 152 
GLN   N    N  N N 153 
GLN   CA   C  N S 154 
GLN   C    C  N N 155 
GLN   O    O  N N 156 
GLN   CB   C  N N 157 
GLN   CG   C  N N 158 
GLN   CD   C  N N 159 
GLN   OE1  O  N N 160 
GLN   NE2  N  N N 161 
GLN   OXT  O  N N 162 
GLN   H    H  N N 163 
GLN   H2   H  N N 164 
GLN   HA   H  N N 165 
GLN   HB2  H  N N 166 
GLN   HB3  H  N N 167 
GLN   HG2  H  N N 168 
GLN   HG3  H  N N 169 
GLN   HE21 H  N N 170 
GLN   HE22 H  N N 171 
GLN   HXT  H  N N 172 
GLU   N    N  N N 173 
GLU   CA   C  N S 174 
GLU   C    C  N N 175 
GLU   O    O  N N 176 
GLU   CB   C  N N 177 
GLU   CG   C  N N 178 
GLU   CD   C  N N 179 
GLU   OE1  O  N N 180 
GLU   OE2  O  N N 181 
GLU   OXT  O  N N 182 
GLU   H    H  N N 183 
GLU   H2   H  N N 184 
GLU   HA   H  N N 185 
GLU   HB2  H  N N 186 
GLU   HB3  H  N N 187 
GLU   HG2  H  N N 188 
GLU   HG3  H  N N 189 
GLU   HE2  H  N N 190 
GLU   HXT  H  N N 191 
GLY   N    N  N N 192 
GLY   CA   C  N N 193 
GLY   C    C  N N 194 
GLY   O    O  N N 195 
GLY   OXT  O  N N 196 
GLY   H    H  N N 197 
GLY   H2   H  N N 198 
GLY   HA2  H  N N 199 
GLY   HA3  H  N N 200 
GLY   HXT  H  N N 201 
HIS   N    N  N N 202 
HIS   CA   C  N S 203 
HIS   C    C  N N 204 
HIS   O    O  N N 205 
HIS   CB   C  N N 206 
HIS   CG   C  Y N 207 
HIS   ND1  N  Y N 208 
HIS   CD2  C  Y N 209 
HIS   CE1  C  Y N 210 
HIS   NE2  N  Y N 211 
HIS   OXT  O  N N 212 
HIS   H    H  N N 213 
HIS   H2   H  N N 214 
HIS   HA   H  N N 215 
HIS   HB2  H  N N 216 
HIS   HB3  H  N N 217 
HIS   HD1  H  N N 218 
HIS   HD2  H  N N 219 
HIS   HE1  H  N N 220 
HIS   HE2  H  N N 221 
HIS   HXT  H  N N 222 
HOH   O    O  N N 223 
HOH   H1   H  N N 224 
HOH   H2   H  N N 225 
ILE   N    N  N N 226 
ILE   CA   C  N S 227 
ILE   C    C  N N 228 
ILE   O    O  N N 229 
ILE   CB   C  N S 230 
ILE   CG1  C  N N 231 
ILE   CG2  C  N N 232 
ILE   CD1  C  N N 233 
ILE   OXT  O  N N 234 
ILE   H    H  N N 235 
ILE   H2   H  N N 236 
ILE   HA   H  N N 237 
ILE   HB   H  N N 238 
ILE   HG12 H  N N 239 
ILE   HG13 H  N N 240 
ILE   HG21 H  N N 241 
ILE   HG22 H  N N 242 
ILE   HG23 H  N N 243 
ILE   HD11 H  N N 244 
ILE   HD12 H  N N 245 
ILE   HD13 H  N N 246 
ILE   HXT  H  N N 247 
LEU   N    N  N N 248 
LEU   CA   C  N S 249 
LEU   C    C  N N 250 
LEU   O    O  N N 251 
LEU   CB   C  N N 252 
LEU   CG   C  N N 253 
LEU   CD1  C  N N 254 
LEU   CD2  C  N N 255 
LEU   OXT  O  N N 256 
LEU   H    H  N N 257 
LEU   H2   H  N N 258 
LEU   HA   H  N N 259 
LEU   HB2  H  N N 260 
LEU   HB3  H  N N 261 
LEU   HG   H  N N 262 
LEU   HD11 H  N N 263 
LEU   HD12 H  N N 264 
LEU   HD13 H  N N 265 
LEU   HD21 H  N N 266 
LEU   HD22 H  N N 267 
LEU   HD23 H  N N 268 
LEU   HXT  H  N N 269 
LYS   N    N  N N 270 
LYS   CA   C  N S 271 
LYS   C    C  N N 272 
LYS   O    O  N N 273 
LYS   CB   C  N N 274 
LYS   CG   C  N N 275 
LYS   CD   C  N N 276 
LYS   CE   C  N N 277 
LYS   NZ   N  N N 278 
LYS   OXT  O  N N 279 
LYS   H    H  N N 280 
LYS   H2   H  N N 281 
LYS   HA   H  N N 282 
LYS   HB2  H  N N 283 
LYS   HB3  H  N N 284 
LYS   HG2  H  N N 285 
LYS   HG3  H  N N 286 
LYS   HD2  H  N N 287 
LYS   HD3  H  N N 288 
LYS   HE2  H  N N 289 
LYS   HE3  H  N N 290 
LYS   HZ1  H  N N 291 
LYS   HZ2  H  N N 292 
LYS   HZ3  H  N N 293 
LYS   HXT  H  N N 294 
MET   N    N  N N 295 
MET   CA   C  N S 296 
MET   C    C  N N 297 
MET   O    O  N N 298 
MET   CB   C  N N 299 
MET   CG   C  N N 300 
MET   SD   S  N N 301 
MET   CE   C  N N 302 
MET   OXT  O  N N 303 
MET   H    H  N N 304 
MET   H2   H  N N 305 
MET   HA   H  N N 306 
MET   HB2  H  N N 307 
MET   HB3  H  N N 308 
MET   HG2  H  N N 309 
MET   HG3  H  N N 310 
MET   HE1  H  N N 311 
MET   HE2  H  N N 312 
MET   HE3  H  N N 313 
MET   HXT  H  N N 314 
PHE   N    N  N N 315 
PHE   CA   C  N S 316 
PHE   C    C  N N 317 
PHE   O    O  N N 318 
PHE   CB   C  N N 319 
PHE   CG   C  Y N 320 
PHE   CD1  C  Y N 321 
PHE   CD2  C  Y N 322 
PHE   CE1  C  Y N 323 
PHE   CE2  C  Y N 324 
PHE   CZ   C  Y N 325 
PHE   OXT  O  N N 326 
PHE   H    H  N N 327 
PHE   H2   H  N N 328 
PHE   HA   H  N N 329 
PHE   HB2  H  N N 330 
PHE   HB3  H  N N 331 
PHE   HD1  H  N N 332 
PHE   HD2  H  N N 333 
PHE   HE1  H  N N 334 
PHE   HE2  H  N N 335 
PHE   HZ   H  N N 336 
PHE   HXT  H  N N 337 
PRO   N    N  N N 338 
PRO   CA   C  N S 339 
PRO   C    C  N N 340 
PRO   O    O  N N 341 
PRO   CB   C  N N 342 
PRO   CG   C  N N 343 
PRO   CD   C  N N 344 
PRO   OXT  O  N N 345 
PRO   H    H  N N 346 
PRO   HA   H  N N 347 
PRO   HB2  H  N N 348 
PRO   HB3  H  N N 349 
PRO   HG2  H  N N 350 
PRO   HG3  H  N N 351 
PRO   HD2  H  N N 352 
PRO   HD3  H  N N 353 
PRO   HXT  H  N N 354 
SER   N    N  N N 355 
SER   CA   C  N S 356 
SER   C    C  N N 357 
SER   O    O  N N 358 
SER   CB   C  N N 359 
SER   OG   O  N N 360 
SER   OXT  O  N N 361 
SER   H    H  N N 362 
SER   H2   H  N N 363 
SER   HA   H  N N 364 
SER   HB2  H  N N 365 
SER   HB3  H  N N 366 
SER   HG   H  N N 367 
SER   HXT  H  N N 368 
THR   N    N  N N 369 
THR   CA   C  N S 370 
THR   C    C  N N 371 
THR   O    O  N N 372 
THR   CB   C  N R 373 
THR   OG1  O  N N 374 
THR   CG2  C  N N 375 
THR   OXT  O  N N 376 
THR   H    H  N N 377 
THR   H2   H  N N 378 
THR   HA   H  N N 379 
THR   HB   H  N N 380 
THR   HG1  H  N N 381 
THR   HG21 H  N N 382 
THR   HG22 H  N N 383 
THR   HG23 H  N N 384 
THR   HXT  H  N N 385 
TRP   N    N  N N 386 
TRP   CA   C  N S 387 
TRP   C    C  N N 388 
TRP   O    O  N N 389 
TRP   CB   C  N N 390 
TRP   CG   C  Y N 391 
TRP   CD1  C  Y N 392 
TRP   CD2  C  Y N 393 
TRP   NE1  N  Y N 394 
TRP   CE2  C  Y N 395 
TRP   CE3  C  Y N 396 
TRP   CZ2  C  Y N 397 
TRP   CZ3  C  Y N 398 
TRP   CH2  C  Y N 399 
TRP   OXT  O  N N 400 
TRP   H    H  N N 401 
TRP   H2   H  N N 402 
TRP   HA   H  N N 403 
TRP   HB2  H  N N 404 
TRP   HB3  H  N N 405 
TRP   HD1  H  N N 406 
TRP   HE1  H  N N 407 
TRP   HE3  H  N N 408 
TRP   HZ2  H  N N 409 
TRP   HZ3  H  N N 410 
TRP   HH2  H  N N 411 
TRP   HXT  H  N N 412 
TYR   N    N  N N 413 
TYR   CA   C  N S 414 
TYR   C    C  N N 415 
TYR   O    O  N N 416 
TYR   CB   C  N N 417 
TYR   CG   C  Y N 418 
TYR   CD1  C  Y N 419 
TYR   CD2  C  Y N 420 
TYR   CE1  C  Y N 421 
TYR   CE2  C  Y N 422 
TYR   CZ   C  Y N 423 
TYR   OH   O  N N 424 
TYR   OXT  O  N N 425 
TYR   H    H  N N 426 
TYR   H2   H  N N 427 
TYR   HA   H  N N 428 
TYR   HB2  H  N N 429 
TYR   HB3  H  N N 430 
TYR   HD1  H  N N 431 
TYR   HD2  H  N N 432 
TYR   HE1  H  N N 433 
TYR   HE2  H  N N 434 
TYR   HH   H  N N 435 
TYR   HXT  H  N N 436 
VAL   N    N  N N 437 
VAL   CA   C  N S 438 
VAL   C    C  N N 439 
VAL   O    O  N N 440 
VAL   CB   C  N N 441 
VAL   CG1  C  N N 442 
VAL   CG2  C  N N 443 
VAL   OXT  O  N N 444 
VAL   H    H  N N 445 
VAL   H2   H  N N 446 
VAL   HA   H  N N 447 
VAL   HB   H  N N 448 
VAL   HG11 H  N N 449 
VAL   HG12 H  N N 450 
VAL   HG13 H  N N 451 
VAL   HG21 H  N N 452 
VAL   HG22 H  N N 453 
VAL   HG23 H  N N 454 
VAL   HXT  H  N N 455 
ZN    ZN   ZN N N 456 
# 
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 
A1IRK C17 C15  sing N N 1   
A1IRK C16 C15  sing N N 2   
A1IRK C15 C14  sing N N 3   
A1IRK C14 C8   sing N N 4   
A1IRK C8  C9   sing N N 5   
A1IRK C8  C7   sing N N 6   
A1IRK N2  O1   sing N N 7   
A1IRK N2  C9   sing N N 8   
A1IRK C9  O5   doub N N 9   
A1IRK C7  O4   doub N N 10  
A1IRK C7  N1   sing N N 11  
A1IRK N1  C3   sing N N 12  
A1IRK C21 C19  sing N N 13  
A1IRK C3  C2   doub Y N 14  
A1IRK C3  C4   sing Y N 15  
A1IRK C20 C19  sing N N 16  
A1IRK C2  C1   sing Y N 17  
A1IRK C19 C18  sing N N 18  
A1IRK C4  C5   doub Y N 19  
A1IRK C1  C6   doub Y N 20  
A1IRK O3  S1   doub N N 21  
A1IRK C18 S1   sing N N 22  
A1IRK C5  C6   sing Y N 23  
A1IRK C6  C10  sing N N 24  
A1IRK N6  S1   sing N N 25  
A1IRK N6  C13  sing N N 26  
A1IRK S1  O2   doub N N 27  
A1IRK C11 C12  doub Y N 28  
A1IRK C11 N3   sing Y N 29  
A1IRK C10 N3   sing N N 30  
A1IRK C13 C12  sing N N 31  
A1IRK C12 N5   sing Y N 32  
A1IRK N3  N4   sing Y N 33  
A1IRK N5  N4   doub Y N 34  
A1IRK C1  H3   sing N N 35  
A1IRK C2  H4   sing N N 36  
A1IRK C4  H5   sing N N 37  
A1IRK C5  H6   sing N N 38  
A1IRK C8  H1   sing N N 39  
A1IRK C10 H10  sing N N 40  
A1IRK C10 H9   sing N N 41  
A1IRK C11 H11  sing N N 42  
A1IRK C13 H12  sing N N 43  
A1IRK C13 H13  sing N N 44  
A1IRK C14 H16  sing N N 45  
A1IRK C14 H15  sing N N 46  
A1IRK C15 H17  sing N N 47  
A1IRK C16 H18  sing N N 48  
A1IRK C16 H19  sing N N 49  
A1IRK C16 H20  sing N N 50  
A1IRK C17 H23  sing N N 51  
A1IRK C17 H21  sing N N 52  
A1IRK C17 H22  sing N N 53  
A1IRK C18 H25  sing N N 54  
A1IRK C18 H24  sing N N 55  
A1IRK C19 H26  sing N N 56  
A1IRK C20 H28  sing N N 57  
A1IRK C20 H27  sing N N 58  
A1IRK C20 H29  sing N N 59  
A1IRK C21 H30  sing N N 60  
A1IRK C21 H32  sing N N 61  
A1IRK C21 H31  sing N N 62  
A1IRK N1  H7   sing N N 63  
A1IRK N2  H8   sing N N 64  
A1IRK N6  H14  sing N N 65  
A1IRK O1  H2   sing N N 66  
ALA   N   CA   sing N N 67  
ALA   N   H    sing N N 68  
ALA   N   H2   sing N N 69  
ALA   CA  C    sing N N 70  
ALA   CA  CB   sing N N 71  
ALA   CA  HA   sing N N 72  
ALA   C   O    doub N N 73  
ALA   C   OXT  sing N N 74  
ALA   CB  HB1  sing N N 75  
ALA   CB  HB2  sing N N 76  
ALA   CB  HB3  sing N N 77  
ALA   OXT HXT  sing N N 78  
ARG   N   CA   sing N N 79  
ARG   N   H    sing N N 80  
ARG   N   H2   sing N N 81  
ARG   CA  C    sing N N 82  
ARG   CA  CB   sing N N 83  
ARG   CA  HA   sing N N 84  
ARG   C   O    doub N N 85  
ARG   C   OXT  sing N N 86  
ARG   CB  CG   sing N N 87  
ARG   CB  HB2  sing N N 88  
ARG   CB  HB3  sing N N 89  
ARG   CG  CD   sing N N 90  
ARG   CG  HG2  sing N N 91  
ARG   CG  HG3  sing N N 92  
ARG   CD  NE   sing N N 93  
ARG   CD  HD2  sing N N 94  
ARG   CD  HD3  sing N N 95  
ARG   NE  CZ   sing N N 96  
ARG   NE  HE   sing N N 97  
ARG   CZ  NH1  sing N N 98  
ARG   CZ  NH2  doub N N 99  
ARG   NH1 HH11 sing N N 100 
ARG   NH1 HH12 sing N N 101 
ARG   NH2 HH21 sing N N 102 
ARG   NH2 HH22 sing N N 103 
ARG   OXT HXT  sing N N 104 
ASN   N   CA   sing N N 105 
ASN   N   H    sing N N 106 
ASN   N   H2   sing N N 107 
ASN   CA  C    sing N N 108 
ASN   CA  CB   sing N N 109 
ASN   CA  HA   sing N N 110 
ASN   C   O    doub N N 111 
ASN   C   OXT  sing N N 112 
ASN   CB  CG   sing N N 113 
ASN   CB  HB2  sing N N 114 
ASN   CB  HB3  sing N N 115 
ASN   CG  OD1  doub N N 116 
ASN   CG  ND2  sing N N 117 
ASN   ND2 HD21 sing N N 118 
ASN   ND2 HD22 sing N N 119 
ASN   OXT HXT  sing N N 120 
ASP   N   CA   sing N N 121 
ASP   N   H    sing N N 122 
ASP   N   H2   sing N N 123 
ASP   CA  C    sing N N 124 
ASP   CA  CB   sing N N 125 
ASP   CA  HA   sing N N 126 
ASP   C   O    doub N N 127 
ASP   C   OXT  sing N N 128 
ASP   CB  CG   sing N N 129 
ASP   CB  HB2  sing N N 130 
ASP   CB  HB3  sing N N 131 
ASP   CG  OD1  doub N N 132 
ASP   CG  OD2  sing N N 133 
ASP   OD2 HD2  sing N N 134 
ASP   OXT HXT  sing N N 135 
CYS   N   CA   sing N N 136 
CYS   N   H    sing N N 137 
CYS   N   H2   sing N N 138 
CYS   CA  C    sing N N 139 
CYS   CA  CB   sing N N 140 
CYS   CA  HA   sing N N 141 
CYS   C   O    doub N N 142 
CYS   C   OXT  sing N N 143 
CYS   CB  SG   sing N N 144 
CYS   CB  HB2  sing N N 145 
CYS   CB  HB3  sing N N 146 
CYS   SG  HG   sing N N 147 
CYS   OXT HXT  sing N N 148 
GLN   N   CA   sing N N 149 
GLN   N   H    sing N N 150 
GLN   N   H2   sing N N 151 
GLN   CA  C    sing N N 152 
GLN   CA  CB   sing N N 153 
GLN   CA  HA   sing N N 154 
GLN   C   O    doub N N 155 
GLN   C   OXT  sing N N 156 
GLN   CB  CG   sing N N 157 
GLN   CB  HB2  sing N N 158 
GLN   CB  HB3  sing N N 159 
GLN   CG  CD   sing N N 160 
GLN   CG  HG2  sing N N 161 
GLN   CG  HG3  sing N N 162 
GLN   CD  OE1  doub N N 163 
GLN   CD  NE2  sing N N 164 
GLN   NE2 HE21 sing N N 165 
GLN   NE2 HE22 sing N N 166 
GLN   OXT HXT  sing N N 167 
GLU   N   CA   sing N N 168 
GLU   N   H    sing N N 169 
GLU   N   H2   sing N N 170 
GLU   CA  C    sing N N 171 
GLU   CA  CB   sing N N 172 
GLU   CA  HA   sing N N 173 
GLU   C   O    doub N N 174 
GLU   C   OXT  sing N N 175 
GLU   CB  CG   sing N N 176 
GLU   CB  HB2  sing N N 177 
GLU   CB  HB3  sing N N 178 
GLU   CG  CD   sing N N 179 
GLU   CG  HG2  sing N N 180 
GLU   CG  HG3  sing N N 181 
GLU   CD  OE1  doub N N 182 
GLU   CD  OE2  sing N N 183 
GLU   OE2 HE2  sing N N 184 
GLU   OXT HXT  sing N N 185 
GLY   N   CA   sing N N 186 
GLY   N   H    sing N N 187 
GLY   N   H2   sing N N 188 
GLY   CA  C    sing N N 189 
GLY   CA  HA2  sing N N 190 
GLY   CA  HA3  sing N N 191 
GLY   C   O    doub N N 192 
GLY   C   OXT  sing N N 193 
GLY   OXT HXT  sing N N 194 
HIS   N   CA   sing N N 195 
HIS   N   H    sing N N 196 
HIS   N   H2   sing N N 197 
HIS   CA  C    sing N N 198 
HIS   CA  CB   sing N N 199 
HIS   CA  HA   sing N N 200 
HIS   C   O    doub N N 201 
HIS   C   OXT  sing N N 202 
HIS   CB  CG   sing N N 203 
HIS   CB  HB2  sing N N 204 
HIS   CB  HB3  sing N N 205 
HIS   CG  ND1  sing Y N 206 
HIS   CG  CD2  doub Y N 207 
HIS   ND1 CE1  doub Y N 208 
HIS   ND1 HD1  sing N N 209 
HIS   CD2 NE2  sing Y N 210 
HIS   CD2 HD2  sing N N 211 
HIS   CE1 NE2  sing Y N 212 
HIS   CE1 HE1  sing N N 213 
HIS   NE2 HE2  sing N N 214 
HIS   OXT HXT  sing N N 215 
HOH   O   H1   sing N N 216 
HOH   O   H2   sing N N 217 
ILE   N   CA   sing N N 218 
ILE   N   H    sing N N 219 
ILE   N   H2   sing N N 220 
ILE   CA  C    sing N N 221 
ILE   CA  CB   sing N N 222 
ILE   CA  HA   sing N N 223 
ILE   C   O    doub N N 224 
ILE   C   OXT  sing N N 225 
ILE   CB  CG1  sing N N 226 
ILE   CB  CG2  sing N N 227 
ILE   CB  HB   sing N N 228 
ILE   CG1 CD1  sing N N 229 
ILE   CG1 HG12 sing N N 230 
ILE   CG1 HG13 sing N N 231 
ILE   CG2 HG21 sing N N 232 
ILE   CG2 HG22 sing N N 233 
ILE   CG2 HG23 sing N N 234 
ILE   CD1 HD11 sing N N 235 
ILE   CD1 HD12 sing N N 236 
ILE   CD1 HD13 sing N N 237 
ILE   OXT HXT  sing N N 238 
LEU   N   CA   sing N N 239 
LEU   N   H    sing N N 240 
LEU   N   H2   sing N N 241 
LEU   CA  C    sing N N 242 
LEU   CA  CB   sing N N 243 
LEU   CA  HA   sing N N 244 
LEU   C   O    doub N N 245 
LEU   C   OXT  sing N N 246 
LEU   CB  CG   sing N N 247 
LEU   CB  HB2  sing N N 248 
LEU   CB  HB3  sing N N 249 
LEU   CG  CD1  sing N N 250 
LEU   CG  CD2  sing N N 251 
LEU   CG  HG   sing N N 252 
LEU   CD1 HD11 sing N N 253 
LEU   CD1 HD12 sing N N 254 
LEU   CD1 HD13 sing N N 255 
LEU   CD2 HD21 sing N N 256 
LEU   CD2 HD22 sing N N 257 
LEU   CD2 HD23 sing N N 258 
LEU   OXT HXT  sing N N 259 
LYS   N   CA   sing N N 260 
LYS   N   H    sing N N 261 
LYS   N   H2   sing N N 262 
LYS   CA  C    sing N N 263 
LYS   CA  CB   sing N N 264 
LYS   CA  HA   sing N N 265 
LYS   C   O    doub N N 266 
LYS   C   OXT  sing N N 267 
LYS   CB  CG   sing N N 268 
LYS   CB  HB2  sing N N 269 
LYS   CB  HB3  sing N N 270 
LYS   CG  CD   sing N N 271 
LYS   CG  HG2  sing N N 272 
LYS   CG  HG3  sing N N 273 
LYS   CD  CE   sing N N 274 
LYS   CD  HD2  sing N N 275 
LYS   CD  HD3  sing N N 276 
LYS   CE  NZ   sing N N 277 
LYS   CE  HE2  sing N N 278 
LYS   CE  HE3  sing N N 279 
LYS   NZ  HZ1  sing N N 280 
LYS   NZ  HZ2  sing N N 281 
LYS   NZ  HZ3  sing N N 282 
LYS   OXT HXT  sing N N 283 
MET   N   CA   sing N N 284 
MET   N   H    sing N N 285 
MET   N   H2   sing N N 286 
MET   CA  C    sing N N 287 
MET   CA  CB   sing N N 288 
MET   CA  HA   sing N N 289 
MET   C   O    doub N N 290 
MET   C   OXT  sing N N 291 
MET   CB  CG   sing N N 292 
MET   CB  HB2  sing N N 293 
MET   CB  HB3  sing N N 294 
MET   CG  SD   sing N N 295 
MET   CG  HG2  sing N N 296 
MET   CG  HG3  sing N N 297 
MET   SD  CE   sing N N 298 
MET   CE  HE1  sing N N 299 
MET   CE  HE2  sing N N 300 
MET   CE  HE3  sing N N 301 
MET   OXT HXT  sing N N 302 
PHE   N   CA   sing N N 303 
PHE   N   H    sing N N 304 
PHE   N   H2   sing N N 305 
PHE   CA  C    sing N N 306 
PHE   CA  CB   sing N N 307 
PHE   CA  HA   sing N N 308 
PHE   C   O    doub N N 309 
PHE   C   OXT  sing N N 310 
PHE   CB  CG   sing N N 311 
PHE   CB  HB2  sing N N 312 
PHE   CB  HB3  sing N N 313 
PHE   CG  CD1  doub Y N 314 
PHE   CG  CD2  sing Y N 315 
PHE   CD1 CE1  sing Y N 316 
PHE   CD1 HD1  sing N N 317 
PHE   CD2 CE2  doub Y N 318 
PHE   CD2 HD2  sing N N 319 
PHE   CE1 CZ   doub Y N 320 
PHE   CE1 HE1  sing N N 321 
PHE   CE2 CZ   sing Y N 322 
PHE   CE2 HE2  sing N N 323 
PHE   CZ  HZ   sing N N 324 
PHE   OXT HXT  sing N N 325 
PRO   N   CA   sing N N 326 
PRO   N   CD   sing N N 327 
PRO   N   H    sing N N 328 
PRO   CA  C    sing N N 329 
PRO   CA  CB   sing N N 330 
PRO   CA  HA   sing N N 331 
PRO   C   O    doub N N 332 
PRO   C   OXT  sing N N 333 
PRO   CB  CG   sing N N 334 
PRO   CB  HB2  sing N N 335 
PRO   CB  HB3  sing N N 336 
PRO   CG  CD   sing N N 337 
PRO   CG  HG2  sing N N 338 
PRO   CG  HG3  sing N N 339 
PRO   CD  HD2  sing N N 340 
PRO   CD  HD3  sing N N 341 
PRO   OXT HXT  sing N N 342 
SER   N   CA   sing N N 343 
SER   N   H    sing N N 344 
SER   N   H2   sing N N 345 
SER   CA  C    sing N N 346 
SER   CA  CB   sing N N 347 
SER   CA  HA   sing N N 348 
SER   C   O    doub N N 349 
SER   C   OXT  sing N N 350 
SER   CB  OG   sing N N 351 
SER   CB  HB2  sing N N 352 
SER   CB  HB3  sing N N 353 
SER   OG  HG   sing N N 354 
SER   OXT HXT  sing N N 355 
THR   N   CA   sing N N 356 
THR   N   H    sing N N 357 
THR   N   H2   sing N N 358 
THR   CA  C    sing N N 359 
THR   CA  CB   sing N N 360 
THR   CA  HA   sing N N 361 
THR   C   O    doub N N 362 
THR   C   OXT  sing N N 363 
THR   CB  OG1  sing N N 364 
THR   CB  CG2  sing N N 365 
THR   CB  HB   sing N N 366 
THR   OG1 HG1  sing N N 367 
THR   CG2 HG21 sing N N 368 
THR   CG2 HG22 sing N N 369 
THR   CG2 HG23 sing N N 370 
THR   OXT HXT  sing N N 371 
TRP   N   CA   sing N N 372 
TRP   N   H    sing N N 373 
TRP   N   H2   sing N N 374 
TRP   CA  C    sing N N 375 
TRP   CA  CB   sing N N 376 
TRP   CA  HA   sing N N 377 
TRP   C   O    doub N N 378 
TRP   C   OXT  sing N N 379 
TRP   CB  CG   sing N N 380 
TRP   CB  HB2  sing N N 381 
TRP   CB  HB3  sing N N 382 
TRP   CG  CD1  doub Y N 383 
TRP   CG  CD2  sing Y N 384 
TRP   CD1 NE1  sing Y N 385 
TRP   CD1 HD1  sing N N 386 
TRP   CD2 CE2  doub Y N 387 
TRP   CD2 CE3  sing Y N 388 
TRP   NE1 CE2  sing Y N 389 
TRP   NE1 HE1  sing N N 390 
TRP   CE2 CZ2  sing Y N 391 
TRP   CE3 CZ3  doub Y N 392 
TRP   CE3 HE3  sing N N 393 
TRP   CZ2 CH2  doub Y N 394 
TRP   CZ2 HZ2  sing N N 395 
TRP   CZ3 CH2  sing Y N 396 
TRP   CZ3 HZ3  sing N N 397 
TRP   CH2 HH2  sing N N 398 
TRP   OXT HXT  sing N N 399 
TYR   N   CA   sing N N 400 
TYR   N   H    sing N N 401 
TYR   N   H2   sing N N 402 
TYR   CA  C    sing N N 403 
TYR   CA  CB   sing N N 404 
TYR   CA  HA   sing N N 405 
TYR   C   O    doub N N 406 
TYR   C   OXT  sing N N 407 
TYR   CB  CG   sing N N 408 
TYR   CB  HB2  sing N N 409 
TYR   CB  HB3  sing N N 410 
TYR   CG  CD1  doub Y N 411 
TYR   CG  CD2  sing Y N 412 
TYR   CD1 CE1  sing Y N 413 
TYR   CD1 HD1  sing N N 414 
TYR   CD2 CE2  doub Y N 415 
TYR   CD2 HD2  sing N N 416 
TYR   CE1 CZ   doub Y N 417 
TYR   CE1 HE1  sing N N 418 
TYR   CE2 CZ   sing Y N 419 
TYR   CE2 HE2  sing N N 420 
TYR   CZ  OH   sing N N 421 
TYR   OH  HH   sing N N 422 
TYR   OXT HXT  sing N N 423 
VAL   N   CA   sing N N 424 
VAL   N   H    sing N N 425 
VAL   N   H2   sing N N 426 
VAL   CA  C    sing N N 427 
VAL   CA  CB   sing N N 428 
VAL   CA  HA   sing N N 429 
VAL   C   O    doub N N 430 
VAL   C   OXT  sing N N 431 
VAL   CB  CG1  sing N N 432 
VAL   CB  CG2  sing N N 433 
VAL   CB  HB   sing N N 434 
VAL   CG1 HG11 sing N N 435 
VAL   CG1 HG12 sing N N 436 
VAL   CG1 HG13 sing N N 437 
VAL   CG2 HG21 sing N N 438 
VAL   CG2 HG22 sing N N 439 
VAL   CG2 HG23 sing N N 440 
VAL   OXT HXT  sing N N 441 
# 
_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.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6YZE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H0X 
_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]   0.016691 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013342 
_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]   0.013136 
_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  
H  
N  
O  
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   ? 5.863   24.978  -33.721 1.00 48.62  ? 2   LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 2   ? 6.230   26.078  -34.616 1.00 54.94  ? 2   LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 2   ? 5.127   26.400  -35.628 1.00 54.05  ? 2   LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 2   ? 4.794   27.570  -35.803 1.00 59.59  ? 2   LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 2   ? 7.539   25.779  -35.347 1.00 53.22  ? 2   LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 2   ? 7.742   26.515  -36.670 1.00 49.25  ? 2   LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 2   ? 8.905   25.909  -37.428 1.00 56.56  ? 2   LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 2   ? 9.353   26.796  -38.591 1.00 54.70  ? 2   LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 2   ? 10.774  26.499  -38.953 1.00 57.83  ? 2   LYS   A NZ   1 
ATOM   10   H  HA   . LYS   A 1 2   ? 6.361   26.869  -34.070 1.00 65.93  ? 2   LYS   A HA   1 
ATOM   11   H  HB2  . LYS   A 1 2   ? 8.276   26.025  -34.765 1.00 63.86  ? 2   LYS   A HB2  1 
ATOM   12   H  HB3  . LYS   A 1 2   ? 7.571   24.829  -35.538 1.00 63.86  ? 2   LYS   A HB3  1 
ATOM   13   H  HG2  . LYS   A 1 2   ? 6.942   26.437  -37.213 1.00 59.09  ? 2   LYS   A HG2  1 
ATOM   14   H  HG3  . LYS   A 1 2   ? 7.936   27.449  -36.498 1.00 59.09  ? 2   LYS   A HG3  1 
ATOM   15   H  HD2  . LYS   A 1 2   ? 9.656   25.797  -36.825 1.00 67.87  ? 2   LYS   A HD2  1 
ATOM   16   H  HD3  . LYS   A 1 2   ? 8.638   25.049  -37.788 1.00 67.87  ? 2   LYS   A HD3  1 
ATOM   17   H  HE2  . LYS   A 1 2   ? 8.793   26.626  -39.365 1.00 65.64  ? 2   LYS   A HE2  1 
ATOM   18   H  HE3  . LYS   A 1 2   ? 9.287   27.729  -38.333 1.00 65.64  ? 2   LYS   A HE3  1 
ATOM   19   H  HZ1  . LYS   A 1 2   ? 11.305  26.662  -38.259 1.00 69.39  ? 2   LYS   A HZ1  1 
ATOM   20   H  HZ2  . LYS   A 1 2   ? 10.856  25.643  -39.186 1.00 69.39  ? 2   LYS   A HZ2  1 
ATOM   21   H  HZ3  . LYS   A 1 2   ? 11.027  27.009  -39.637 1.00 69.39  ? 2   LYS   A HZ3  1 
ATOM   22   N  N    . VAL   A 1 3   ? 4.603   25.390  -36.333 1.00 36.11  ? 3   VAL   A N    1 
ATOM   23   C  CA   . VAL   A 1 3   ? 3.440   25.594  -37.193 1.00 39.08  ? 3   VAL   A CA   1 
ATOM   24   C  C    . VAL   A 1 3   ? 2.334   24.652  -36.742 1.00 36.63  ? 3   VAL   A C    1 
ATOM   25   O  O    . VAL   A 1 3   ? 2.603   23.558  -36.224 1.00 32.55  ? 3   VAL   A O    1 
ATOM   26   C  CB   . VAL   A 1 3   ? 3.704   25.367  -38.701 1.00 35.68  ? 3   VAL   A CB   1 
ATOM   27   C  CG1  . VAL   A 1 3   ? 4.563   26.509  -39.263 1.00 37.86  ? 3   VAL   A CG1  1 
ATOM   28   C  CG2  . VAL   A 1 3   ? 4.326   24.025  -38.962 1.00 44.48  ? 3   VAL   A CG2  1 
ATOM   29   H  H    . VAL   A 1 3   ? 4.904   24.584  -36.326 1.00 43.33  ? 3   VAL   A H    1 
ATOM   30   H  HA   . VAL   A 1 3   ? 3.171   26.519  -37.081 1.00 46.90  ? 3   VAL   A HA   1 
ATOM   31   H  HB   . VAL   A 1 3   ? 2.853   25.370  -39.168 1.00 42.81  ? 3   VAL   A HB   1 
ATOM   32   H  HG11 . VAL   A 1 3   ? 4.732   26.343  -40.203 1.00 45.43  ? 3   VAL   A HG11 1 
ATOM   33   H  HG12 . VAL   A 1 3   ? 4.086   27.346  -39.154 1.00 45.43  ? 3   VAL   A HG12 1 
ATOM   34   H  HG13 . VAL   A 1 3   ? 5.402   26.541  -38.777 1.00 45.43  ? 3   VAL   A HG13 1 
ATOM   35   H  HG21 . VAL   A 1 3   ? 4.483   23.930  -39.914 1.00 53.38  ? 3   VAL   A HG21 1 
ATOM   36   H  HG22 . VAL   A 1 3   ? 5.167   23.968  -38.481 1.00 53.38  ? 3   VAL   A HG22 1 
ATOM   37   H  HG23 . VAL   A 1 3   ? 3.722   23.332  -38.655 1.00 53.38  ? 3   VAL   A HG23 1 
ATOM   38   N  N    . GLN   A 1 4   ? 1.083   25.072  -36.932 1.00 30.04  ? 4   GLN   A N    1 
ATOM   39   C  CA   . GLN   A 1 4   ? -0.041  24.171  -36.718 1.00 30.66  ? 4   GLN   A CA   1 
ATOM   40   C  C    . GLN   A 1 4   ? -0.014  23.079  -37.787 1.00 30.57  ? 4   GLN   A C    1 
ATOM   41   O  O    . GLN   A 1 4   ? 0.377   23.313  -38.932 1.00 29.67  ? 4   GLN   A O    1 
ATOM   42   C  CB   . GLN   A 1 4   ? -1.379  24.911  -36.750 1.00 33.44  ? 4   GLN   A CB   1 
ATOM   43   C  CG   . GLN   A 1 4   ? -1.510  25.988  -35.663 1.00 42.70  ? 4   GLN   A CG   1 
ATOM   44   C  CD   . GLN   A 1 4   ? -2.889  26.653  -35.614 1.00 46.25  ? 4   GLN   A CD   1 
ATOM   45   O  OE1  . GLN   A 1 4   ? -3.488  26.974  -36.646 1.00 55.14  ? 4   GLN   A OE1  1 
ATOM   46   N  NE2  . GLN   A 1 4   ? -3.392  26.864  -34.403 1.00 55.02  ? 4   GLN   A NE2  1 
ATOM   47   H  H    . GLN   A 1 4   ? 0.864   25.866  -37.181 1.00 36.04  ? 4   GLN   A H    1 
ATOM   48   H  HA   . GLN   A 1 4   ? 0.027   23.768  -35.838 1.00 36.79  ? 4   GLN   A HA   1 
ATOM   49   H  HB2  . GLN   A 1 4   ? -1.475  25.345  -37.612 1.00 40.12  ? 4   GLN   A HB2  1 
ATOM   50   H  HB3  . GLN   A 1 4   ? -2.094  24.269  -36.620 1.00 40.12  ? 4   GLN   A HB3  1 
ATOM   51   H  HG2  . GLN   A 1 4   ? -1.348  25.580  -34.798 1.00 51.24  ? 4   GLN   A HG2  1 
ATOM   52   H  HG3  . GLN   A 1 4   ? -0.854  26.682  -35.830 1.00 51.24  ? 4   GLN   A HG3  1 
ATOM   53   H  HE21 . GLN   A 1 4   ? -2.946  26.631  -33.706 1.00 66.02  ? 4   GLN   A HE21 1 
ATOM   54   H  HE22 . GLN   A 1 4   ? -4.163  27.234  -34.316 1.00 66.02  ? 4   GLN   A HE22 1 
ATOM   55   N  N    . ALA   A 1 5   ? -0.480  21.888  -37.406 1.00 27.96  ? 5   ALA   A N    1 
ATOM   56   C  CA   . ALA   A 1 5   ? -0.607  20.771  -38.341 1.00 23.31  ? 5   ALA   A CA   1 
ATOM   57   C  C    . ALA   A 1 5   ? -1.778  19.915  -37.865 1.00 22.95  ? 5   ALA   A C    1 
ATOM   58   O  O    . ALA   A 1 5   ? -2.352  20.163  -36.809 1.00 23.45  ? 5   ALA   A O    1 
ATOM   59   C  CB   . ALA   A 1 5   ? 0.670   19.945  -38.447 1.00 28.59  ? 5   ALA   A CB   1 
ATOM   60   H  H    . ALA   A 1 5   ? -0.730  21.701  -36.605 1.00 33.55  ? 5   ALA   A H    1 
ATOM   61   H  HA   . ALA   A 1 5   ? -0.790  21.127  -39.224 1.00 27.97  ? 5   ALA   A HA   1 
ATOM   62   H  HB1  . ALA   A 1 5   ? 0.525   19.220  -39.075 1.00 34.30  ? 5   ALA   A HB1  1 
ATOM   63   H  HB2  . ALA   A 1 5   ? 1.390   20.515  -38.759 1.00 34.30  ? 5   ALA   A HB2  1 
ATOM   64   H  HB3  . ALA   A 1 5   ? 0.887   19.586  -37.572 1.00 34.30  ? 5   ALA   A HB3  1 
ATOM   65   N  N    . LYS   A 1 6   ? -2.121  18.892  -38.657 1.00 26.26  ? 6   LYS   A N    1 
ATOM   66   C  CA   . LYS   A 1 6   ? -3.250  18.022  -38.335 1.00 24.41  ? 6   LYS   A CA   1 
ATOM   67   C  C    . LYS   A 1 6   ? -2.722  16.594  -38.171 1.00 21.88  ? 6   LYS   A C    1 
ATOM   68   O  O    . LYS   A 1 6   ? -1.798  16.163  -38.859 1.00 23.52  ? 6   LYS   A O    1 
ATOM   69   C  CB   . LYS   A 1 6   ? -4.288  18.023  -39.469 1.00 26.87  ? 6   LYS   A CB   1 
ATOM   70   C  CG   . LYS   A 1 6   ? -5.084  19.338  -39.638 1.00 32.89  ? 6   LYS   A CG   1 
ATOM   71   C  CD   . LYS   A 1 6   ? -5.994  19.576  -38.432 1.00 37.10  ? 6   LYS   A CD   1 
ATOM   72   C  CE   . LYS   A 1 6   ? -6.977  20.723  -38.699 1.00 39.69  ? 6   LYS   A CE   1 
ATOM   73   N  NZ   . LYS   A 1 6   ? -7.448  21.370  -37.437 1.00 49.71  ? 6   LYS   A NZ   1 
ATOM   74   H  H    . LYS   A 1 6   ? -1.712  18.685  -39.385 1.00 31.51  ? 6   LYS   A H    1 
ATOM   75   H  HA   . LYS   A 1 6   ? -3.676  18.321  -37.516 1.00 29.29  ? 6   LYS   A HA   1 
ATOM   76   H  HB2  . LYS   A 1 6   ? -3.826  17.855  -40.306 1.00 32.24  ? 6   LYS   A HB2  1 
ATOM   77   H  HB3  . LYS   A 1 6   ? -4.930  17.316  -39.297 1.00 32.24  ? 6   LYS   A HB3  1 
ATOM   78   H  HG2  . LYS   A 1 6   ? -4.467  20.083  -39.711 1.00 39.46  ? 6   LYS   A HG2  1 
ATOM   79   H  HG3  . LYS   A 1 6   ? -5.635  19.284  -40.435 1.00 39.46  ? 6   LYS   A HG3  1 
ATOM   80   H  HD2  . LYS   A 1 6   ? -6.504  18.771  -38.250 1.00 44.52  ? 6   LYS   A HD2  1 
ATOM   81   H  HD3  . LYS   A 1 6   ? -5.454  19.808  -37.661 1.00 44.52  ? 6   LYS   A HD3  1 
ATOM   82   H  HE2  . LYS   A 1 6   ? -6.538  21.399  -39.238 1.00 47.63  ? 6   LYS   A HE2  1 
ATOM   83   H  HE3  . LYS   A 1 6   ? -7.751  20.376  -39.168 1.00 47.63  ? 6   LYS   A HE3  1 
ATOM   84   H  HZ1  . LYS   A 1 6   ? -8.006  22.037  -37.627 1.00 59.65  ? 6   LYS   A HZ1  1 
ATOM   85   H  HZ2  . LYS   A 1 6   ? -7.873  20.774  -36.930 1.00 59.65  ? 6   LYS   A HZ2  1 
ATOM   86   H  HZ3  . LYS   A 1 6   ? -6.755  21.694  -36.983 1.00 59.65  ? 6   LYS   A HZ3  1 
ATOM   87   N  N    . GLY   A 1 7   ? -3.328  15.876  -37.233 1.00 21.97  ? 7   GLY   A N    1 
ATOM   88   C  CA   . GLY   A 1 7   ? -2.945  14.503  -37.004 1.00 22.48  ? 7   GLY   A CA   1 
ATOM   89   C  C    . GLY   A 1 7   ? -4.064  13.514  -37.298 1.00 18.75  ? 7   GLY   A C    1 
ATOM   90   O  O    . GLY   A 1 7   ? -5.217  13.689  -36.898 1.00 20.61  ? 7   GLY   A O    1 
ATOM   91   H  H    . GLY   A 1 7   ? -3.958  16.165  -36.724 1.00 26.36  ? 7   GLY   A H    1 
ATOM   92   H  HA2  . GLY   A 1 7   ? -2.191  14.284  -37.573 1.00 26.98  ? 7   GLY   A HA2  1 
ATOM   93   H  HA3  . GLY   A 1 7   ? -2.683  14.396  -36.077 1.00 26.98  ? 7   GLY   A HA3  1 
ATOM   94   N  N    . MET   A 1 8   ? -3.687  12.468  -38.022 1.00 20.42  ? 8   MET   A N    1 
ATOM   95   C  CA   A MET   A 1 8   ? -4.591  11.377  -38.356 0.47 22.73  ? 8   MET   A CA   1 
ATOM   96   C  CA   B MET   A 1 8   ? -4.596  11.380  -38.348 0.20 22.75  ? 8   MET   A CA   1 
ATOM   97   C  CA   C MET   A 1 8   ? -4.585  11.376  -38.364 0.33 22.75  ? 8   MET   A CA   1 
ATOM   98   C  C    . MET   A 1 8   ? -4.183  10.138  -37.570 1.00 17.77  ? 8   MET   A C    1 
ATOM   99   O  O    . MET   A 1 8   ? -2.995  9.837   -37.461 1.00 20.96  ? 8   MET   A O    1 
ATOM   100  C  CB   A MET   A 1 8   ? -4.490  11.106  -39.869 0.47 27.97  ? 8   MET   A CB   1 
ATOM   101  C  CB   B MET   A 1 8   ? -4.543  11.100  -39.854 0.20 27.91  ? 8   MET   A CB   1 
ATOM   102  C  CB   C MET   A 1 8   ? -4.457  11.087  -39.875 0.33 27.94  ? 8   MET   A CB   1 
ATOM   103  C  CG   A MET   A 1 8   ? -5.411  10.051  -40.423 0.47 27.64  ? 8   MET   A CG   1 
ATOM   104  C  CG   B MET   A 1 8   ? -5.824  10.546  -40.436 0.20 28.37  ? 8   MET   A CG   1 
ATOM   105  C  CG   C MET   A 1 8   ? -5.277  9.928   -40.391 0.33 27.27  ? 8   MET   A CG   1 
ATOM   106  S  SD   A MET   A 1 8   ? -5.392  10.086  -42.248 0.47 33.54  ? 8   MET   A SD   1 
ATOM   107  S  SD   B MET   A 1 8   ? -5.937  10.862  -42.211 0.20 31.07  ? 8   MET   A SD   1 
ATOM   108  S  SD   C MET   A 1 8   ? -5.448  9.924   -42.194 0.33 33.72  ? 8   MET   A SD   1 
ATOM   109  C  CE   A MET   A 1 8   ? -6.243  11.643  -42.586 0.47 32.23  ? 8   MET   A CE   1 
ATOM   110  C  CE   B MET   A 1 8   ? -4.514  9.961   -42.788 0.20 28.19  ? 8   MET   A CE   1 
ATOM   111  C  CE   C MET   A 1 8   ? -3.863  10.546  -42.629 0.33 28.80  ? 8   MET   A CE   1 
ATOM   112  H  H    A MET   A 1 8   ? -2.894  12.366  -38.339 0.47 24.50  ? 8   MET   A H    1 
ATOM   113  H  H    B MET   A 1 8   ? -2.895  12.365  -38.342 0.20 24.50  ? 8   MET   A H    1 
ATOM   114  H  HA   A MET   A 1 8   ? -5.510  11.594  -38.132 0.47 27.28  ? 8   MET   A HA   1 
ATOM   115  H  HA   B MET   A 1 8   ? -5.507  11.611  -38.108 0.20 27.30  ? 8   MET   A HA   1 
ATOM   116  H  HB2  A MET   A 1 8   ? -4.689  11.932  -40.337 0.47 33.56  ? 8   MET   A HB2  1 
ATOM   117  H  HB2  B MET   A 1 8   ? -4.348  11.931  -40.315 0.20 33.49  ? 8   MET   A HB2  1 
ATOM   118  H  HB2  C MET   A 1 8   ? -4.739  11.878  -40.361 0.33 33.53  ? 8   MET   A HB2  1 
ATOM   119  H  HB3  A MET   A 1 8   ? -3.583  10.824  -40.065 0.47 33.56  ? 8   MET   A HB3  1 
ATOM   120  H  HB3  B MET   A 1 8   ? -3.841  10.453  -40.023 0.20 33.49  ? 8   MET   A HB3  1 
ATOM   121  H  HB3  C MET   A 1 8   ? -3.527  10.891  -40.069 0.33 33.53  ? 8   MET   A HB3  1 
ATOM   122  H  HG2  A MET   A 1 8   ? -5.117  9.176   -40.127 0.47 33.17  ? 8   MET   A HG2  1 
ATOM   123  H  HG2  B MET   A 1 8   ? -5.851  9.587   -40.294 0.20 34.04  ? 8   MET   A HG2  1 
ATOM   124  H  HG2  C MET   A 1 8   ? -4.847  9.098   -40.130 0.33 32.72  ? 8   MET   A HG2  1 
ATOM   125  H  HG3  A MET   A 1 8   ? -6.317  10.218  -40.119 0.47 33.17  ? 8   MET   A HG3  1 
ATOM   126  H  HG3  B MET   A 1 8   ? -6.582  10.967  -40.001 0.20 34.04  ? 8   MET   A HG3  1 
ATOM   127  H  HG3  C MET   A 1 8   ? -6.166  9.976   -40.007 0.33 32.72  ? 8   MET   A HG3  1 
ATOM   128  H  HE1  A MET   A 1 8   ? -6.483  11.674  -43.526 0.47 38.68  ? 8   MET   A HE1  1 
ATOM   129  H  HE1  B MET   A 1 8   ? -4.787  9.064   -43.036 0.20 33.83  ? 8   MET   A HE1  1 
ATOM   130  H  HE1  C MET   A 1 8   ? -3.671  10.307  -43.550 0.33 34.56  ? 8   MET   A HE1  1 
ATOM   131  H  HE2  A MET   A 1 8   ? -7.043  11.691  -42.039 0.47 38.68  ? 8   MET   A HE2  1 
ATOM   132  H  HE2  B MET   A 1 8   ? -4.141  10.418  -43.558 0.20 33.83  ? 8   MET   A HE2  1 
ATOM   133  H  HE2  C MET   A 1 8   ? -3.865  11.511  -42.532 0.33 34.56  ? 8   MET   A HE2  1 
ATOM   134  H  HE3  A MET   A 1 8   ? -5.650  12.380  -42.371 0.47 38.68  ? 8   MET   A HE3  1 
ATOM   135  H  HE3  B MET   A 1 8   ? -3.855  9.922   -42.077 0.20 33.83  ? 8   MET   A HE3  1 
ATOM   136  H  HE3  C MET   A 1 8   ? -3.198  10.156  -42.041 0.33 34.56  ? 8   MET   A HE3  1 
ATOM   137  N  N    . GLY   A 1 9   ? -5.151  9.417   -37.048 1.00 19.12  ? 9   GLY   A N    1 
ATOM   138  C  CA   . GLY   A 1 9   ? -4.796  8.254   -36.254 1.00 17.91  ? 9   GLY   A CA   1 
ATOM   139  C  C    . GLY   A 1 9   ? -6.028  7.642   -35.644 1.00 19.09  ? 9   GLY   A C    1 
ATOM   140  O  O    . GLY   A 1 9   ? -7.177  7.991   -36.004 1.00 21.13  ? 9   GLY   A O    1 
ATOM   141  H  H    . GLY   A 1 9   ? -5.993  9.571   -37.132 1.00 22.94  ? 9   GLY   A H    1 
ATOM   142  H  HA2  . GLY   A 1 9   ? -4.362  7.593   -36.815 1.00 21.50  ? 9   GLY   A HA2  1 
ATOM   143  H  HA3  . GLY   A 1 9   ? -4.190  8.513   -35.543 1.00 21.50  ? 9   GLY   A HA3  1 
ATOM   144  N  N    . PHE   A 1 10  ? -5.807  6.761   -34.666 1.00 15.85  ? 10  PHE   A N    1 
ATOM   145  C  CA   . PHE   A 1 10  ? -6.885  5.951   -34.140 1.00 16.80  ? 10  PHE   A CA   1 
ATOM   146  C  C    . PHE   A 1 10  ? -7.133  6.238   -32.673 1.00 15.81  ? 10  PHE   A C    1 
ATOM   147  O  O    . PHE   A 1 10  ? -6.337  6.863   -31.971 1.00 15.57  ? 10  PHE   A O    1 
ATOM   148  C  CB   . PHE   A 1 10  ? -6.549  4.484   -34.435 1.00 17.57  ? 10  PHE   A CB   1 
ATOM   149  C  CG   . PHE   A 1 10  ? -6.373  4.260   -35.893 1.00 18.18  ? 10  PHE   A CG   1 
ATOM   150  C  CD1  . PHE   A 1 10  ? -7.481  4.166   -36.714 1.00 20.33  ? 10  PHE   A CD1  1 
ATOM   151  C  CD2  . PHE   A 1 10  ? -5.104  4.289   -36.515 1.00 18.67  ? 10  PHE   A CD2  1 
ATOM   152  C  CE1  . PHE   A 1 10  ? -7.341  4.041   -38.070 1.00 21.74  ? 10  PHE   A CE1  1 
ATOM   153  C  CE2  . PHE   A 1 10  ? -4.969  4.157   -37.869 1.00 22.49  ? 10  PHE   A CE2  1 
ATOM   154  C  CZ   . PHE   A 1 10  ? -6.093  4.039   -38.652 1.00 22.01  ? 10  PHE   A CZ   1 
ATOM   155  H  H    . PHE   A 1 10  ? -5.041  6.621   -34.299 1.00 19.02  ? 10  PHE   A H    1 
ATOM   156  H  HA   . PHE   A 1 10  ? -7.734  6.168   -34.555 1.00 20.16  ? 10  PHE   A HA   1 
ATOM   157  H  HB2  . PHE   A 1 10  ? -5.723  4.246   -33.986 1.00 21.08  ? 10  PHE   A HB2  1 
ATOM   158  H  HB3  . PHE   A 1 10  ? -7.272  3.918   -34.122 1.00 21.08  ? 10  PHE   A HB3  1 
ATOM   159  H  HD1  . PHE   A 1 10  ? -8.332  4.187   -36.340 1.00 24.40  ? 10  PHE   A HD1  1 
ATOM   160  H  HD2  . PHE   A 1 10  ? -4.344  4.400   -35.992 1.00 22.40  ? 10  PHE   A HD2  1 
ATOM   161  H  HE1  . PHE   A 1 10  ? -8.097  3.958   -38.605 1.00 26.09  ? 10  PHE   A HE1  1 
ATOM   162  H  HE2  . PHE   A 1 10  ? -4.124  4.147   -38.258 1.00 26.99  ? 10  PHE   A HE2  1 
ATOM   163  H  HZ   . PHE   A 1 10  ? -6.011  3.958   -39.574 1.00 26.41  ? 10  PHE   A HZ   1 
ATOM   164  N  N    . GLY   A 1 11  ? -8.286  5.791   -32.195 1.00 15.58  ? 11  GLY   A N    1 
ATOM   165  C  CA   . GLY   A 1 11  ? -8.696  5.856   -30.822 1.00 15.14  ? 11  GLY   A CA   1 
ATOM   166  C  C    . GLY   A 1 11  ? -9.660  4.743   -30.453 1.00 14.67  ? 11  GLY   A C    1 
ATOM   167  O  O    . GLY   A 1 11  ? -10.002 3.906   -31.282 1.00 15.60  ? 11  GLY   A O    1 
ATOM   168  H  H    . GLY   A 1 11  ? -8.885  5.420   -32.690 1.00 18.69  ? 11  GLY   A H    1 
ATOM   169  H  HA2  . GLY   A 1 11  ? -7.915  5.785   -30.250 1.00 18.17  ? 11  GLY   A HA2  1 
ATOM   170  H  HA3  . GLY   A 1 11  ? -9.133  6.706   -30.656 1.00 18.17  ? 11  GLY   A HA3  1 
ATOM   171  N  N    . GLY   A 1 12  ? -10.087 4.744   -29.200 1.00 15.94  ? 12  GLY   A N    1 
ATOM   172  C  CA   . GLY   A 1 12  ? -10.982 3.705   -28.735 1.00 15.70  ? 12  GLY   A CA   1 
ATOM   173  C  C    . GLY   A 1 12  ? -10.255 2.544   -28.127 1.00 15.90  ? 12  GLY   A C    1 
ATOM   174  O  O    . GLY   A 1 12  ? -9.049  2.559   -27.866 1.00 15.53  ? 12  GLY   A O    1 
ATOM   175  H  H    . GLY   A 1 12  ? -9.874  5.329   -28.608 1.00 19.13  ? 12  GLY   A H    1 
ATOM   176  H  HA2  . GLY   A 1 12  ? -11.580 4.074   -28.066 1.00 18.83  ? 12  GLY   A HA2  1 
ATOM   177  H  HA3  . GLY   A 1 12  ? -11.508 3.377   -29.482 1.00 18.83  ? 12  GLY   A HA3  1 
ATOM   178  N  N    . ASN   A 1 13  ? -10.994 1.465   -27.932 1.00 15.95  ? 13  ASN   A N    1 
ATOM   179  C  CA   . ASN   A 1 13  ? -10.428 0.264   -27.312 1.00 16.98  ? 13  ASN   A CA   1 
ATOM   180  C  C    . ASN   A 1 13  ? -11.218 -0.965  -27.734 1.00 17.47  ? 13  ASN   A C    1 
ATOM   181  O  O    . ASN   A 1 13  ? -12.169 -0.891  -28.521 1.00 18.42  ? 13  ASN   A O    1 
ATOM   182  C  CB   . ASN   A 1 13  ? -10.295 0.439   -25.771 1.00 15.17  ? 13  ASN   A CB   1 
ATOM   183  C  CG   . ASN   A 1 13  ? -11.630 0.510   -25.075 1.00 14.89  ? 13  ASN   A CG   1 
ATOM   184  O  OD1  . ASN   A 1 13  ? -12.541 -0.232  -25.468 1.00 17.29  ? 13  ASN   A OD1  1 
ATOM   185  N  ND2  . ASN   A 1 13  ? -11.735 1.309   -24.030 1.00 15.37  ? 13  ASN   A ND2  1 
ATOM   186  H  H    . ASN   A 1 13  ? -11.824 1.396   -28.148 1.00 19.15  ? 13  ASN   A H    1 
ATOM   187  H  HA   . ASN   A 1 13  ? -9.535  0.123   -27.664 1.00 20.37  ? 13  ASN   A HA   1 
ATOM   188  H  HB2  . ASN   A 1 13  ? -9.807  -0.316  -25.408 1.00 18.20  ? 13  ASN   A HB2  1 
ATOM   189  H  HB3  . ASN   A 1 13  ? -9.817  1.263   -25.586 1.00 18.20  ? 13  ASN   A HB3  1 
ATOM   190  H  HD21 . ASN   A 1 13  ? -12.483 1.372   -23.611 1.00 18.44  ? 13  ASN   A HD21 1 
ATOM   191  H  HD22 . ASN   A 1 13  ? -11.055 1.766   -23.769 1.00 18.44  ? 13  ASN   A HD22 1 
ATOM   192  N  N    . ARG   A 1 14  ? -10.762 -2.122  -27.278 1.00 17.21  ? 14  ARG   A N    1 
ATOM   193  C  CA   . ARG   A 1 14  ? -11.323 -3.371  -27.761 1.00 21.36  ? 14  ARG   A CA   1 
ATOM   194  C  C    . ARG   A 1 14  ? -12.740 -3.591  -27.307 1.00 24.42  ? 14  ARG   A C    1 
ATOM   195  O  O    . ARG   A 1 14  ? -13.447 -4.382  -27.963 1.00 29.37  ? 14  ARG   A O    1 
ATOM   196  C  CB   . ARG   A 1 14  ? -10.428 -4.511  -27.300 1.00 24.56  ? 14  ARG   A CB   1 
ATOM   197  C  CG   . ARG   A 1 14  ? -9.150  -4.468  -28.048 1.00 22.15  ? 14  ARG   A CG   1 
ATOM   198  C  CD   . ARG   A 1 14  ? -8.070  -5.332  -27.392 1.00 32.77  ? 14  ARG   A CD   1 
ATOM   199  N  NE   . ARG   A 1 14  ? -6.823  -5.196  -28.128 1.00 31.94  ? 14  ARG   A NE   1 
ATOM   200  C  CZ   . ARG   A 1 14  ? -5.826  -6.067  -28.085 1.00 35.09  ? 14  ARG   A CZ   1 
ATOM   201  N  NH1  . ARG   A 1 14  ? -5.848  -7.096  -27.257 1.00 38.94  ? 14  ARG   A NH1  1 
ATOM   202  N  NH2  . ARG   A 1 14  ? -4.786  -5.892  -28.890 1.00 36.47  ? 14  ARG   A NH2  1 
ATOM   203  H  H    . ARG   A 1 14  ? -10.135 -2.210  -26.695 1.00 20.65  ? 14  ARG   A H    1 
ATOM   204  H  HA   . ARG   A 1 14  ? -11.345 -3.365  -28.731 1.00 25.63  ? 14  ARG   A HA   1 
ATOM   205  H  HB2  . ARG   A 1 14  ? -10.241 -4.419  -26.353 1.00 29.47  ? 14  ARG   A HB2  1 
ATOM   206  H  HB3  . ARG   A 1 14  ? -10.863 -5.361  -27.472 1.00 29.47  ? 14  ARG   A HB3  1 
ATOM   207  H  HG2  . ARG   A 1 14  ? -9.295  -4.799  -28.948 1.00 26.58  ? 14  ARG   A HG2  1 
ATOM   208  H  HG3  . ARG   A 1 14  ? -8.828  -3.554  -28.079 1.00 26.58  ? 14  ARG   A HG3  1 
ATOM   209  H  HD2  . ARG   A 1 14  ? -7.927  -5.040  -26.478 1.00 39.32  ? 14  ARG   A HD2  1 
ATOM   210  H  HD3  . ARG   A 1 14  ? -8.341  -6.263  -27.404 1.00 39.32  ? 14  ARG   A HD3  1 
ATOM   211  H  HE   . ARG   A 1 14  ? -6.727  -4.501  -28.626 1.00 38.33  ? 14  ARG   A HE   1 
ATOM   212  H  HH11 . ARG   A 1 14  ? -6.519  -7.212  -26.731 1.00 46.72  ? 14  ARG   A HH11 1 
ATOM   213  H  HH12 . ARG   A 1 14  ? -5.191  -7.651  -27.244 1.00 46.72  ? 14  ARG   A HH12 1 
ATOM   214  H  HH21 . ARG   A 1 14  ? -4.767  -5.221  -29.428 1.00 43.76  ? 14  ARG   A HH21 1 
ATOM   215  H  HH22 . ARG   A 1 14  ? -4.131  -6.449  -28.874 1.00 43.76  ? 14  ARG   A HH22 1 
ATOM   216  N  N    . LYS   A 1 15  ? -13.185 -2.918  -26.264 1.00 21.91  ? 15  LYS   A N    1 
ATOM   217  C  CA   . LYS   A 1 15  ? -14.562 -3.064  -25.801 1.00 26.68  ? 15  LYS   A CA   1 
ATOM   218  C  C    . LYS   A 1 15  ? -15.531 -2.150  -26.536 1.00 23.40  ? 15  LYS   A C    1 
ATOM   219  O  O    . LYS   A 1 15  ? -16.574 -2.617  -27.014 1.00 28.47  ? 15  LYS   A O    1 
ATOM   220  C  CB   . LYS   A 1 15  ? -14.690 -2.745  -24.330 1.00 27.47  ? 15  LYS   A CB   1 
ATOM   221  C  CG   . LYS   A 1 15  ? -16.114 -2.997  -23.769 1.00 30.11  ? 15  LYS   A CG   1 
ATOM   222  C  CD   . LYS   A 1 15  ? -16.080 -3.011  -22.282 1.00 33.87  ? 15  LYS   A CD   1 
ATOM   223  C  CE   . LYS   A 1 15  ? -17.469 -2.989  -21.692 1.00 32.04  ? 15  LYS   A CE   1 
ATOM   224  N  NZ   . LYS   A 1 15  ? -17.394 -2.647  -20.263 1.00 34.08  ? 15  LYS   A NZ   1 
ATOM   225  H  H    . LYS   A 1 15  ? -12.712 -2.368  -25.802 1.00 26.29  ? 15  LYS   A H    1 
ATOM   226  H  HA   . LYS   A 1 15  ? -14.797 -3.992  -25.955 1.00 32.02  ? 15  LYS   A HA   1 
ATOM   227  H  HB2  . LYS   A 1 15  ? -14.071 -3.303  -23.834 1.00 32.97  ? 15  LYS   A HB2  1 
ATOM   228  H  HB3  . LYS   A 1 15  ? -14.477 -1.809  -24.193 1.00 32.97  ? 15  LYS   A HB3  1 
ATOM   229  H  HG2  . LYS   A 1 15  ? -16.710 -2.289  -24.060 1.00 36.13  ? 15  LYS   A HG2  1 
ATOM   230  H  HG3  . LYS   A 1 15  ? -16.441 -3.855  -24.081 1.00 36.13  ? 15  LYS   A HG3  1 
ATOM   231  H  HD2  . LYS   A 1 15  ? -15.633 -3.817  -21.979 1.00 40.65  ? 15  LYS   A HD2  1 
ATOM   232  H  HD3  . LYS   A 1 15  ? -15.602 -2.228  -21.965 1.00 40.65  ? 15  LYS   A HD3  1 
ATOM   233  H  HE2  . LYS   A 1 15  ? -18.008 -2.321  -22.145 1.00 38.45  ? 15  LYS   A HE2  1 
ATOM   234  H  HE3  . LYS   A 1 15  ? -17.878 -3.863  -21.783 1.00 38.45  ? 15  LYS   A HE3  1 
ATOM   235  H  HZ1  . LYS   A 1 15  ? -18.211 -2.639  -19.909 1.00 40.89  ? 15  LYS   A HZ1  1 
ATOM   236  H  HZ2  . LYS   A 1 15  ? -16.898 -3.248  -19.832 1.00 40.89  ? 15  LYS   A HZ2  1 
ATOM   237  H  HZ3  . LYS   A 1 15  ? -17.027 -1.843  -20.161 1.00 40.89  ? 15  LYS   A HZ3  1 
ATOM   238  N  N    . ILE   A 1 16  ? -15.243 -0.874  -26.623 1.00 22.32  ? 16  ILE   A N    1 
ATOM   239  C  CA   . ILE   A 1 16  ? -16.200 0.038   -27.260 1.00 27.48  ? 16  ILE   A CA   1 
ATOM   240  C  C    . ILE   A 1 16  ? -15.990 0.150   -28.745 1.00 25.58  ? 16  ILE   A C    1 
ATOM   241  O  O    . ILE   A 1 16  ? -16.856 0.712   -29.443 1.00 30.77  ? 16  ILE   A O    1 
ATOM   242  C  CB   . ILE   A 1 16  ? -16.143 1.420   -26.606 1.00 32.35  ? 16  ILE   A CB   1 
ATOM   243  C  CG1  . ILE   A 1 16  ? -14.749 2.058   -26.754 1.00 25.58  ? 16  ILE   A CG1  1 
ATOM   244  C  CG2  . ILE   A 1 16  ? -16.517 1.269   -25.179 1.00 36.55  ? 16  ILE   A CG2  1 
ATOM   245  C  CD1  . ILE   A 1 16  ? -14.789 3.515   -26.735 1.00 32.22  ? 16  ILE   A CD1  1 
ATOM   246  H  H    . ILE   A 1 16  ? -14.521 -0.507  -26.333 1.00 26.78  ? 16  ILE   A H    1 
ATOM   247  H  HA   . ILE   A 1 16  ? -17.094 -0.314  -27.128 1.00 32.97  ? 16  ILE   A HA   1 
ATOM   248  H  HB   . ILE   A 1 16  ? -16.765 2.015   -27.053 1.00 38.82  ? 16  ILE   A HB   1 
ATOM   249  H  HG12 . ILE   A 1 16  ? -14.188 1.764   -26.019 1.00 30.70  ? 16  ILE   A HG12 1 
ATOM   250  H  HG13 . ILE   A 1 16  ? -14.363 1.780   -27.599 1.00 30.70  ? 16  ILE   A HG13 1 
ATOM   251  H  HG21 . ILE   A 1 16  ? -16.478 2.137   -24.749 1.00 43.86  ? 16  ILE   A HG21 1 
ATOM   252  H  HG22 . ILE   A 1 16  ? -17.418 0.913   -25.125 1.00 43.86  ? 16  ILE   A HG22 1 
ATOM   253  H  HG23 . ILE   A 1 16  ? -15.895 0.660   -24.752 1.00 43.86  ? 16  ILE   A HG23 1 
ATOM   254  H  HD11 . ILE   A 1 16  ? -13.886 3.857   -26.824 1.00 38.66  ? 16  ILE   A HD11 1 
ATOM   255  H  HD12 . ILE   A 1 16  ? -15.335 3.826   -27.474 1.00 38.66  ? 16  ILE   A HD12 1 
ATOM   256  H  HD13 . ILE   A 1 16  ? -15.172 3.810   -25.894 1.00 38.66  ? 16  ILE   A HD13 1 
ATOM   257  N  N    . GLY   A 1 17  ? -14.913 -0.418  -29.266 1.00 23.05  ? 17  GLY   A N    1 
ATOM   258  C  CA   . GLY   A 1 17  ? -14.549 -0.327  -30.658 1.00 24.04  ? 17  GLY   A CA   1 
ATOM   259  C  C    . GLY   A 1 17  ? -13.526 0.776   -30.912 1.00 20.15  ? 17  GLY   A C    1 
ATOM   260  O  O    . GLY   A 1 17  ? -13.361 1.717   -30.130 1.00 20.92  ? 17  GLY   A O    1 
ATOM   261  H  H    . GLY   A 1 17  ? -14.354 -0.883  -28.807 1.00 27.66  ? 17  GLY   A H    1 
ATOM   262  H  HA2  . GLY   A 1 17  ? -14.168 -1.171  -30.947 1.00 28.85  ? 17  GLY   A HA2  1 
ATOM   263  H  HA3  . GLY   A 1 17  ? -15.340 -0.139  -31.186 1.00 28.85  ? 17  GLY   A HA3  1 
ATOM   264  N  N    . GLU   A 1 18  ? -12.855 0.638   -32.035 1.00 20.93  ? 18  GLU   A N    1 
ATOM   265  C  CA   . GLU   A 1 18  ? -11.807 1.574   -32.440 1.00 20.74  ? 18  GLU   A CA   1 
ATOM   266  C  C    . GLU   A 1 18  ? -12.357 2.449   -33.556 1.00 22.89  ? 18  GLU   A C    1 
ATOM   267  O  O    . GLU   A 1 18  ? -13.255 2.041   -34.316 1.00 26.71  ? 18  GLU   A O    1 
ATOM   268  C  CB   . GLU   A 1 18  ? -10.540 0.792   -32.780 1.00 27.82  ? 18  GLU   A CB   1 
ATOM   269  C  CG   . GLU   A 1 18  ? -10.010 0.201   -31.462 1.00 25.93  ? 18  GLU   A CG   1 
ATOM   270  C  CD   . GLU   A 1 18  ? -8.700  -0.532  -31.488 1.00 31.27  ? 18  GLU   A CD   1 
ATOM   271  O  OE1  . GLU   A 1 18  ? -8.049  -0.539  -32.557 1.00 32.87  ? 18  GLU   A OE1  1 
ATOM   272  O  OE2  . GLU   A 1 18  ? -8.383  -1.123  -30.393 1.00 32.71  ? 18  GLU   A OE2  1 
ATOM   273  H  H    . GLU   A 1 18  ? -12.985 -0.000  -32.597 1.00 25.11  ? 18  GLU   A H    1 
ATOM   274  H  HA   . GLU   A 1 18  ? -11.539 2.195   -31.744 1.00 24.89  ? 18  GLU   A HA   1 
ATOM   275  H  HB2  . GLU   A 1 18  ? -10.742 0.073   -33.399 1.00 33.39  ? 18  GLU   A HB2  1 
ATOM   276  H  HB3  . GLU   A 1 18  ? -9.871  1.381   -33.163 1.00 33.39  ? 18  GLU   A HB3  1 
ATOM   277  H  HG2  . GLU   A 1 18  ? -9.906  0.932   -30.833 1.00 31.12  ? 18  GLU   A HG2  1 
ATOM   278  H  HG3  . GLU   A 1 18  ? -10.672 -0.427  -31.133 1.00 31.12  ? 18  GLU   A HG3  1 
ATOM   279  N  N    . TYR   A 1 19  ? -11.830 3.644   -33.680 1.00 19.75  ? 19  TYR   A N    1 
ATOM   280  C  CA   . TYR   A 1 19  ? -12.311 4.628   -34.633 1.00 19.30  ? 19  TYR   A CA   1 
ATOM   281  C  C    . TYR   A 1 19  ? -11.130 5.474   -35.083 1.00 21.03  ? 19  TYR   A C    1 
ATOM   282  O  O    . TYR   A 1 19  ? -10.029 5.373   -34.513 1.00 18.85  ? 19  TYR   A O    1 
ATOM   283  C  CB   . TYR   A 1 19  ? -13.405 5.524   -34.002 1.00 18.83  ? 19  TYR   A CB   1 
ATOM   284  C  CG   . TYR   A 1 19  ? -13.094 5.954   -32.593 1.00 19.25  ? 19  TYR   A CG   1 
ATOM   285  C  CD1  . TYR   A 1 19  ? -12.232 7.045   -32.335 1.00 19.43  ? 19  TYR   A CD1  1 
ATOM   286  C  CD2  . TYR   A 1 19  ? -13.626 5.313   -31.508 1.00 19.47  ? 19  TYR   A CD2  1 
ATOM   287  C  CE1  . TYR   A 1 19  ? -11.901 7.439   -31.045 1.00 18.65  ? 19  TYR   A CE1  1 
ATOM   288  C  CE2  . TYR   A 1 19  ? -13.309 5.734   -30.227 1.00 21.34  ? 19  TYR   A CE2  1 
ATOM   289  C  CZ   . TYR   A 1 19  ? -12.452 6.797   -30.014 1.00 18.41  ? 19  TYR   A CZ   1 
ATOM   290  O  OH   . TYR   A 1 19  ? -12.185 7.146   -28.713 1.00 20.32  ? 19  TYR   A OH   1 
ATOM   291  H  H    . TYR   A 1 19  ? -11.168 3.925   -33.208 1.00 23.70  ? 19  TYR   A H    1 
ATOM   292  H  HA   . TYR   A 1 19  ? -12.685 4.176   -35.405 1.00 23.15  ? 19  TYR   A HA   1 
ATOM   293  H  HB2  . TYR   A 1 19  ? -13.503 6.324   -34.542 1.00 22.60  ? 19  TYR   A HB2  1 
ATOM   294  H  HB3  . TYR   A 1 19  ? -14.240 5.031   -33.984 1.00 22.60  ? 19  TYR   A HB3  1 
ATOM   295  H  HD1  . TYR   A 1 19  ? -11.875 7.515   -33.054 1.00 23.31  ? 19  TYR   A HD1  1 
ATOM   296  H  HD2  . TYR   A 1 19  ? -14.202 4.594   -31.631 1.00 23.37  ? 19  TYR   A HD2  1 
ATOM   297  H  HE1  . TYR   A 1 19  ? -11.306 8.139   -30.902 1.00 22.38  ? 19  TYR   A HE1  1 
ATOM   298  H  HE2  . TYR   A 1 19  ? -13.680 5.293   -29.497 1.00 25.61  ? 19  TYR   A HE2  1 
ATOM   299  H  HH   . TYR   A 1 19  ? -11.654 7.797   -28.693 1.00 24.38  ? 19  TYR   A HH   1 
ATOM   300  N  N    . GLN   A 1 20  ? -11.344 6.341   -36.076 1.00 19.98  ? 20  GLN   A N    1 
ATOM   301  C  CA   . GLN   A 1 20  ? -10.283 7.064   -36.751 1.00 20.74  ? 20  GLN   A CA   1 
ATOM   302  C  C    . GLN   A 1 20  ? -10.529 8.571   -36.671 1.00 25.76  ? 20  GLN   A C    1 
ATOM   303  O  O    . GLN   A 1 20  ? -11.553 9.075   -37.151 1.00 23.82  ? 20  GLN   A O    1 
ATOM   304  C  CB   . GLN   A 1 20  ? -10.114 6.631   -38.212 1.00 24.17  ? 20  GLN   A CB   1 
ATOM   305  C  CG   . GLN   A 1 20  ? -8.939  7.331   -38.883 1.00 25.67  ? 20  GLN   A CG   1 
ATOM   306  C  CD   . GLN   A 1 20  ? -8.869  7.109   -40.363 1.00 36.34  ? 20  GLN   A CD   1 
ATOM   307  O  OE1  . GLN   A 1 20  ? -9.038  6.000   -40.830 1.00 36.02  ? 20  GLN   A OE1  1 
ATOM   308  N  NE2  . GLN   A 1 20  ? -8.570  8.164   -41.104 1.00 45.23  ? 20  GLN   A NE2  1 
ATOM   309  H  H    . GLN   A 1 20  ? -12.126 6.528   -36.381 1.00 23.98  ? 20  GLN   A H    1 
ATOM   310  H  HA   . GLN   A 1 20  ? -9.458  6.868   -36.280 1.00 24.88  ? 20  GLN   A HA   1 
ATOM   311  H  HB2  . GLN   A 1 20  ? -9.956  5.674   -38.244 1.00 29.01  ? 20  GLN   A HB2  1 
ATOM   312  H  HB3  . GLN   A 1 20  ? -10.920 6.851   -38.705 1.00 29.01  ? 20  GLN   A HB3  1 
ATOM   313  H  HG2  . GLN   A 1 20  ? -9.016  8.286   -38.730 1.00 30.80  ? 20  GLN   A HG2  1 
ATOM   314  H  HG3  . GLN   A 1 20  ? -8.114  6.999   -38.494 1.00 30.80  ? 20  GLN   A HG3  1 
ATOM   315  H  HE21 . GLN   A 1 20  ? -8.428  8.926   -40.730 1.00 54.28  ? 20  GLN   A HE21 1 
ATOM   316  H  HE22 . GLN   A 1 20  ? -8.517  8.088   -41.959 1.00 54.28  ? 20  GLN   A HE22 1 
ATOM   317  N  N    . PHE   A 1 21  ? -9.564  9.293   -36.110 1.00 20.42  ? 21  PHE   A N    1 
ATOM   318  C  CA   . PHE   A 1 21  ? -9.483  10.738  -36.235 1.00 20.18  ? 21  PHE   A CA   1 
ATOM   319  C  C    . PHE   A 1 21  ? -9.081  11.068  -37.656 1.00 23.37  ? 21  PHE   A C    1 
ATOM   320  O  O    . PHE   A 1 21  ? -8.027  10.650  -38.127 1.00 22.23  ? 21  PHE   A O    1 
ATOM   321  C  CB   . PHE   A 1 21  ? -8.430  11.241  -35.256 1.00 18.48  ? 21  PHE   A CB   1 
ATOM   322  C  CG   . PHE   A 1 21  ? -8.813  10.964  -33.857 1.00 16.76  ? 21  PHE   A CG   1 
ATOM   323  C  CD1  . PHE   A 1 21  ? -9.790  11.705  -33.216 1.00 17.77  ? 21  PHE   A CD1  1 
ATOM   324  C  CD2  . PHE   A 1 21  ? -8.198  9.922   -33.102 1.00 17.69  ? 21  PHE   A CD2  1 
ATOM   325  C  CE1  . PHE   A 1 21  ? -10.149 11.434  -31.919 1.00 18.34  ? 21  PHE   A CE1  1 
ATOM   326  C  CE2  . PHE   A 1 21  ? -8.553  9.674   -31.827 1.00 16.39  ? 21  PHE   A CE2  1 
ATOM   327  C  CZ   . PHE   A 1 21  ? -9.532  10.412  -31.227 1.00 15.70  ? 21  PHE   A CZ   1 
ATOM   328  H  H    . PHE   A 1 21  ? -8.927  8.958   -35.639 1.00 24.51  ? 21  PHE   A H    1 
ATOM   329  H  HA   . PHE   A 1 21  ? -10.332 11.164  -36.038 1.00 24.21  ? 21  PHE   A HA   1 
ATOM   330  H  HB2  . PHE   A 1 21  ? -7.587  10.796  -35.435 1.00 22.18  ? 21  PHE   A HB2  1 
ATOM   331  H  HB3  . PHE   A 1 21  ? -8.327  12.200  -35.360 1.00 22.18  ? 21  PHE   A HB3  1 
ATOM   332  H  HD1  . PHE   A 1 21  ? -10.211 12.398  -33.671 1.00 21.33  ? 21  PHE   A HD1  1 
ATOM   333  H  HD2  . PHE   A 1 21  ? -7.536  9.403   -33.499 1.00 21.23  ? 21  PHE   A HD2  1 
ATOM   334  H  HE1  . PHE   A 1 21  ? -10.811 11.941  -31.506 1.00 22.01  ? 21  PHE   A HE1  1 
ATOM   335  H  HE2  . PHE   A 1 21  ? -8.130  8.995   -31.353 1.00 19.67  ? 21  PHE   A HE2  1 
ATOM   336  H  HZ   . PHE   A 1 21  ? -9.782  10.227  -30.351 1.00 18.84  ? 21  PHE   A HZ   1 
ATOM   337  N  N    . GLY   A 1 22  ? -9.971  11.752  -38.376 1.00 24.24  ? 22  GLY   A N    1 
ATOM   338  C  CA   . GLY   A 1 22  ? -9.835  11.940  -39.798 1.00 27.75  ? 22  GLY   A CA   1 
ATOM   339  C  C    . GLY   A 1 22  ? -10.884 11.237  -40.618 1.00 29.83  ? 22  GLY   A C    1 
ATOM   340  O  O    . GLY   A 1 22  ? -10.957 11.493  -41.827 1.00 33.74  ? 22  GLY   A O    1 
ATOM   341  H  H    . GLY   A 1 22  ? -10.674 12.120  -38.046 1.00 29.08  ? 22  GLY   A H    1 
ATOM   342  H  HA2  . GLY   A 1 22  ? -9.888  12.889  -39.995 1.00 33.30  ? 22  GLY   A HA2  1 
ATOM   343  H  HA3  . GLY   A 1 22  ? -8.967  11.609  -40.076 1.00 33.30  ? 22  GLY   A HA3  1 
ATOM   344  N  N    . LYS   A 1 23  ? -11.752 10.460  -39.999 1.00 26.49  ? 23  LYS   A N    1 
ATOM   345  C  CA   . LYS   A 1 23  ? -12.847 9.780   -40.701 1.00 29.19  ? 23  LYS   A CA   1 
ATOM   346  C  C    . LYS   A 1 23  ? -14.105 9.812   -39.861 1.00 32.42  ? 23  LYS   A C    1 
ATOM   347  O  O    . LYS   A 1 23  ? -15.080 10.440  -40.249 1.00 36.12  ? 23  LYS   A O    1 
ATOM   348  C  CB   . LYS   A 1 23  ? -12.468 8.335   -41.006 1.00 30.28  ? 23  LYS   A CB   1 
ATOM   349  C  CG   . LYS   A 1 23  ? -13.414 7.604   -41.950 1.00 36.54  ? 23  LYS   A CG   1 
ATOM   350  C  CD   . LYS   A 1 23  ? -13.082 6.091   -41.967 1.00 40.99  ? 23  LYS   A CD   1 
ATOM   351  C  CE   . LYS   A 1 23  ? -11.609 5.851   -42.285 1.00 51.34  ? 23  LYS   A CE   1 
ATOM   352  N  NZ   . LYS   A 1 23  ? -11.230 6.342   -43.651 1.00 64.96  ? 23  LYS   A NZ   1 
ATOM   353  H  H    . LYS   A 1 23  ? -11.737 10.301  -39.154 1.00 31.78  ? 23  LYS   A H    1 
ATOM   354  H  HA   . LYS   A 1 23  ? -13.017 10.235  -41.541 1.00 35.03  ? 23  LYS   A HA   1 
ATOM   355  H  HB2  . LYS   A 1 23  ? -11.588 8.329   -41.414 1.00 36.34  ? 23  LYS   A HB2  1 
ATOM   356  H  HB3  . LYS   A 1 23  ? -12.451 7.840   -40.172 1.00 36.34  ? 23  LYS   A HB3  1 
ATOM   357  H  HG2  . LYS   A 1 23  ? -14.329 7.718   -41.650 1.00 43.85  ? 23  LYS   A HG2  1 
ATOM   358  H  HG3  . LYS   A 1 23  ? -13.313 7.954   -42.849 1.00 43.85  ? 23  LYS   A HG3  1 
ATOM   359  H  HD2  . LYS   A 1 23  ? -13.273 5.710   -41.096 1.00 49.19  ? 23  LYS   A HD2  1 
ATOM   360  H  HD3  . LYS   A 1 23  ? -13.617 5.651   -42.646 1.00 49.19  ? 23  LYS   A HD3  1 
ATOM   361  H  HE2  . LYS   A 1 23  ? -11.064 6.321   -41.634 1.00 61.60  ? 23  LYS   A HE2  1 
ATOM   362  H  HE3  . LYS   A 1 23  ? -11.427 4.900   -42.246 1.00 61.60  ? 23  LYS   A HE3  1 
ATOM   363  H  HZ1  . LYS   A 1 23  ? -10.362 6.205   -43.793 1.00 77.95  ? 23  LYS   A HZ1  1 
ATOM   364  H  HZ2  . LYS   A 1 23  ? -11.696 5.907   -44.271 1.00 77.95  ? 23  LYS   A HZ2  1 
ATOM   365  H  HZ3  . LYS   A 1 23  ? -11.400 7.213   -43.720 1.00 77.95  ? 23  LYS   A HZ3  1 
ATOM   366  N  N    . ASP   A 1 24  ? -14.092 9.142   -38.699 1.00 25.84  ? 24  ASP   A N    1 
ATOM   367  C  CA   . ASP   A 1 24  ? -15.227 9.084   -37.790 1.00 29.87  ? 24  ASP   A CA   1 
ATOM   368  C  C    . ASP   A 1 24  ? -15.300 10.322  -36.918 1.00 30.88  ? 24  ASP   A C    1 
ATOM   369  O  O    . ASP   A 1 24  ? -16.391 10.791  -36.592 1.00 28.67  ? 24  ASP   A O    1 
ATOM   370  C  CB   . ASP   A 1 24  ? -15.111 7.851   -36.883 1.00 29.29  ? 24  ASP   A CB   1 
ATOM   371  C  CG   . ASP   A 1 24  ? -14.856 6.595   -37.688 1.00 35.00  ? 24  ASP   A CG   1 
ATOM   372  O  OD1  . ASP   A 1 24  ? -15.744 6.254   -38.488 1.00 35.92  ? 24  ASP   A OD1  1 
ATOM   373  O  OD2  . ASP   A 1 24  ? -13.767 5.991   -37.617 1.00 26.29  ? 24  ASP   A OD2  1 
ATOM   374  H  H    . ASP   A 1 24  ? -13.412 8.700   -38.411 1.00 31.01  ? 24  ASP   A H    1 
ATOM   375  H  HA   . ASP   A 1 24  ? -16.037 9.017   -38.318 1.00 35.84  ? 24  ASP   A HA   1 
ATOM   376  H  HB2  . ASP   A 1 24  ? -14.372 7.974   -36.266 1.00 35.15  ? 24  ASP   A HB2  1 
ATOM   377  H  HB3  . ASP   A 1 24  ? -15.938 7.736   -36.390 1.00 35.15  ? 24  ASP   A HB3  1 
ATOM   378  N  N    . LEU   A 1 25  ? -14.150 10.849  -36.525 1.00 24.42  ? 25  LEU   A N    1 
ATOM   379  C  CA   . LEU   A 1 25  ? -14.039 12.001  -35.646 1.00 21.80  ? 25  LEU   A CA   1 
ATOM   380  C  C    . LEU   A 1 25  ? -13.145 12.997  -36.339 1.00 22.26  ? 25  LEU   A C    1 
ATOM   381  O  O    . LEU   A 1 25  ? -12.466 12.664  -37.300 1.00 23.61  ? 25  LEU   A O    1 
ATOM   382  C  CB   . LEU   A 1 25  ? -13.431 11.622  -34.279 1.00 24.45  ? 25  LEU   A CB   1 
ATOM   383  C  CG   . LEU   A 1 25  ? -14.286 10.695  -33.440 1.00 28.53  ? 25  LEU   A CG   1 
ATOM   384  C  CD1  . LEU   A 1 25  ? -13.635 10.318  -32.101 1.00 28.88  ? 25  LEU   A CD1  1 
ATOM   385  C  CD2  . LEU   A 1 25  ? -15.632 11.355  -33.131 1.00 36.21  ? 25  LEU   A CD2  1 
ATOM   386  H  H    . LEU   A 1 25  ? -13.385 10.540  -36.768 1.00 29.30  ? 25  LEU   A H    1 
ATOM   387  H  HA   . LEU   A 1 25  ? -14.915 12.380  -35.474 1.00 26.16  ? 25  LEU   A HA   1 
ATOM   388  H  HB2  . LEU   A 1 25  ? -12.582 11.178  -34.433 1.00 29.34  ? 25  LEU   A HB2  1 
ATOM   389  H  HB3  . LEU   A 1 25  ? -13.292 12.435  -33.768 1.00 29.34  ? 25  LEU   A HB3  1 
ATOM   390  H  HG   . LEU   A 1 25  ? -14.402 9.885   -33.960 1.00 34.23  ? 25  LEU   A HG   1 
ATOM   391  H  HD11 . LEU   A 1 25  ? -14.241 9.745   -31.606 1.00 34.66  ? 25  LEU   A HD11 1 
ATOM   392  H  HD12 . LEU   A 1 25  ? -12.804 9.849   -32.276 1.00 34.66  ? 25  LEU   A HD12 1 
ATOM   393  H  HD13 . LEU   A 1 25  ? -13.458 11.128  -31.597 1.00 34.66  ? 25  LEU   A HD13 1 
ATOM   394  H  HD21 . LEU   A 1 25  ? -16.154 10.759  -32.571 1.00 43.46  ? 25  LEU   A HD21 1 
ATOM   395  H  HD22 . LEU   A 1 25  ? -15.474 12.191  -32.666 1.00 43.46  ? 25  LEU   A HD22 1 
ATOM   396  H  HD23 . LEU   A 1 25  ? -16.101 11.521  -33.963 1.00 43.46  ? 25  LEU   A HD23 1 
ATOM   397  N  N    . PRO   A 1 26  ? -13.049 14.221  -35.816 1.00 23.83  ? 26  PRO   A N    1 
ATOM   398  C  CA   . PRO   A 1 26  ? -12.188 15.195  -36.486 1.00 23.25  ? 26  PRO   A CA   1 
ATOM   399  C  C    . PRO   A 1 26  ? -10.707 14.804  -36.466 1.00 24.41  ? 26  PRO   A C    1 
ATOM   400  O  O    . PRO   A 1 26  ? -10.231 14.087  -35.562 1.00 23.64  ? 26  PRO   A O    1 
ATOM   401  C  CB   . PRO   A 1 26  ? -12.427 16.488  -35.665 1.00 27.90  ? 26  PRO   A CB   1 
ATOM   402  C  CG   . PRO   A 1 26  ? -13.766 16.275  -34.941 1.00 32.52  ? 26  PRO   A CG   1 
ATOM   403  C  CD   . PRO   A 1 26  ? -13.762 14.787  -34.647 1.00 31.04  ? 26  PRO   A CD   1 
ATOM   404  H  HA   . PRO   A 1 26  ? -12.470 15.309  -37.407 1.00 27.90  ? 26  PRO   A HA   1 
ATOM   405  H  HB2  . PRO   A 1 26  ? -11.706 16.610  -35.028 1.00 33.48  ? 26  PRO   A HB2  1 
ATOM   406  H  HB3  . PRO   A 1 26  ? -12.475 17.252  -36.262 1.00 33.48  ? 26  PRO   A HB3  1 
ATOM   407  H  HG2  . PRO   A 1 26  ? -13.795 16.797  -34.124 1.00 39.03  ? 26  PRO   A HG2  1 
ATOM   408  H  HG3  . PRO   A 1 26  ? -14.506 16.521  -35.518 1.00 39.03  ? 26  PRO   A HG3  1 
ATOM   409  H  HD2  . PRO   A 1 26  ? -13.285 14.597  -33.825 1.00 37.24  ? 26  PRO   A HD2  1 
ATOM   410  H  HD3  . PRO   A 1 26  ? -14.667 14.442  -34.593 1.00 37.24  ? 26  PRO   A HD3  1 
ATOM   411  N  N    . LEU   A 1 27  ? -9.958  15.381  -37.376 1.00 24.02  ? 27  LEU   A N    1 
ATOM   412  C  CA   . LEU   A 1 27  ? -8.503  15.340  -37.308 1.00 26.13  ? 27  LEU   A CA   1 
ATOM   413  C  C    . LEU   A 1 27  ? -8.039  16.058  -36.033 1.00 22.75  ? 27  LEU   A C    1 
ATOM   414  O  O    . LEU   A 1 27  ? -8.709  16.946  -35.486 1.00 23.81  ? 27  LEU   A O    1 
ATOM   415  C  CB   . LEU   A 1 27  ? -7.894  16.054  -38.492 1.00 26.97  ? 27  LEU   A CB   1 
ATOM   416  C  CG   . LEU   A 1 27  ? -7.894  15.233  -39.790 1.00 26.40  ? 27  LEU   A CG   1 
ATOM   417  C  CD1  . LEU   A 1 27  ? -7.663  16.206  -40.928 1.00 32.25  ? 27  LEU   A CD1  1 
ATOM   418  C  CD2  . LEU   A 1 27  ? -6.877  14.151  -39.932 1.00 27.57  ? 27  LEU   A CD2  1 
ATOM   419  H  H    . LEU   A 1 27  ? -10.263 15.811  -38.055 1.00 28.82  ? 27  LEU   A H    1 
ATOM   420  H  HA   . LEU   A 1 27  ? -8.204  14.417  -37.310 1.00 31.36  ? 27  LEU   A HA   1 
ATOM   421  H  HB2  . LEU   A 1 27  ? -8.399  16.865  -38.657 1.00 32.37  ? 27  LEU   A HB2  1 
ATOM   422  H  HB3  . LEU   A 1 27  ? -6.973  16.273  -38.282 1.00 32.37  ? 27  LEU   A HB3  1 
ATOM   423  H  HG   . LEU   A 1 27  ? -8.744  14.767  -39.797 1.00 31.68  ? 27  LEU   A HG   1 
ATOM   424  H  HD11 . LEU   A 1 27  ? -7.668  15.718  -41.766 1.00 38.70  ? 27  LEU   A HD11 1 
ATOM   425  H  HD12 . LEU   A 1 27  ? -8.373  16.867  -40.927 1.00 38.70  ? 27  LEU   A HD12 1 
ATOM   426  H  HD13 . LEU   A 1 27  ? -6.805  16.641  -40.803 1.00 38.70  ? 27  LEU   A HD13 1 
ATOM   427  H  HD21 . LEU   A 1 27  ? -6.969  13.745  -40.808 1.00 33.09  ? 27  LEU   A HD21 1 
ATOM   428  H  HD22 . LEU   A 1 27  ? -5.991  14.535  -39.837 1.00 33.09  ? 27  LEU   A HD22 1 
ATOM   429  H  HD23 . LEU   A 1 27  ? -7.025  13.486  -39.242 1.00 33.09  ? 27  LEU   A HD23 1 
ATOM   430  N  N    . LEU   A 1 28  ? -6.950  15.549  -35.439 1.00 20.65  ? 28  LEU   A N    1 
ATOM   431  C  CA   . LEU   A 1 28  ? -6.394  16.135  -34.228 1.00 18.19  ? 28  LEU   A CA   1 
ATOM   432  C  C    . LEU   A 1 28  ? -5.593  17.396  -34.539 1.00 18.88  ? 28  LEU   A C    1 
ATOM   433  O  O    . LEU   A 1 28  ? -4.927  17.506  -35.560 1.00 21.56  ? 28  LEU   A O    1 
ATOM   434  C  CB   . LEU   A 1 28  ? -5.457  15.121  -33.573 1.00 18.51  ? 28  LEU   A CB   1 
ATOM   435  C  CG   . LEU   A 1 28  ? -6.134  13.831  -33.151 1.00 18.60  ? 28  LEU   A CG   1 
ATOM   436  C  CD1  . LEU   A 1 28  ? -5.055  12.775  -32.785 1.00 24.22  ? 28  LEU   A CD1  1 
ATOM   437  C  CD2  . LEU   A 1 28  ? -7.050  14.037  -31.993 1.00 21.91  ? 28  LEU   A CD2  1 
ATOM   438  H  H    . LEU   A 1 28  ? -6.518  14.862  -35.724 1.00 24.78  ? 28  LEU   A H    1 
ATOM   439  H  HA   . LEU   A 1 28  ? -7.114  16.373  -33.624 1.00 21.83  ? 28  LEU   A HA   1 
ATOM   440  H  HB2  . LEU   A 1 28  ? -4.756  14.894  -34.204 1.00 22.22  ? 28  LEU   A HB2  1 
ATOM   441  H  HB3  . LEU   A 1 28  ? -5.070  15.524  -32.780 1.00 22.22  ? 28  LEU   A HB3  1 
ATOM   442  H  HG   . LEU   A 1 28  ? -6.671  13.509  -33.892 1.00 22.32  ? 28  LEU   A HG   1 
ATOM   443  H  HD11 . LEU   A 1 28  ? -5.496  11.955  -32.512 1.00 29.06  ? 28  LEU   A HD11 1 
ATOM   444  H  HD12 . LEU   A 1 28  ? -4.498  12.609  -33.561 1.00 29.06  ? 28  LEU   A HD12 1 
ATOM   445  H  HD13 . LEU   A 1 28  ? -4.513  13.117  -32.056 1.00 29.06  ? 28  LEU   A HD13 1 
ATOM   446  H  HD21 . LEU   A 1 28  ? -7.435  13.184  -31.739 1.00 26.29  ? 28  LEU   A HD21 1 
ATOM   447  H  HD22 . LEU   A 1 28  ? -6.545  14.406  -31.252 1.00 26.29  ? 28  LEU   A HD22 1 
ATOM   448  H  HD23 . LEU   A 1 28  ? -7.753  14.653  -32.253 1.00 26.29  ? 28  LEU   A HD23 1 
ATOM   449  N  N    . GLU   A 1 29  ? -5.642  18.341  -33.601 1.00 20.04  ? 29  GLU   A N    1 
ATOM   450  C  CA   . GLU   A 1 29  ? -4.874  19.576  -33.762 1.00 19.63  ? 29  GLU   A CA   1 
ATOM   451  C  C    . GLU   A 1 29  ? -3.514  19.434  -33.096 1.00 19.05  ? 29  GLU   A C    1 
ATOM   452  O  O    . GLU   A 1 29  ? -3.437  19.304  -31.871 1.00 18.49  ? 29  GLU   A O    1 
ATOM   453  C  CB   . GLU   A 1 29  ? -5.652  20.745  -33.146 1.00 25.96  ? 29  GLU   A CB   1 
ATOM   454  C  CG   . GLU   A 1 29  ? -6.996  21.091  -33.843 1.00 37.36  ? 29  GLU   A CG   1 
ATOM   455  C  CD   . GLU   A 1 29  ? -7.933  21.974  -33.004 1.00 49.40  ? 29  GLU   A CD   1 
ATOM   456  O  OE1  . GLU   A 1 29  ? -7.604  22.290  -31.834 1.00 51.54  ? 29  GLU   A OE1  1 
ATOM   457  O  OE2  . GLU   A 1 29  ? -9.025  22.319  -33.517 1.00 57.79  ? 29  GLU   A OE2  1 
ATOM   458  H  H    . GLU   A 1 29  ? -6.102  18.291  -32.877 1.00 24.05  ? 29  GLU   A H    1 
ATOM   459  H  HA   . GLU   A 1 29  ? -4.725  19.737  -34.707 1.00 23.56  ? 29  GLU   A HA   1 
ATOM   460  H  HB2  . GLU   A 1 29  ? -5.853  20.525  -32.223 1.00 31.15  ? 29  GLU   A HB2  1 
ATOM   461  H  HB3  . GLU   A 1 29  ? -5.094  21.537  -33.184 1.00 31.15  ? 29  GLU   A HB3  1 
ATOM   462  H  HG2  . GLU   A 1 29  ? -6.805  21.565  -34.667 1.00 44.83  ? 29  GLU   A HG2  1 
ATOM   463  H  HG3  . GLU   A 1 29  ? -7.466  20.265  -34.037 1.00 44.83  ? 29  GLU   A HG3  1 
ATOM   464  N  N    . ILE   A 1 30  ? -2.458  19.387  -33.890 1.00 19.85  ? 30  ILE   A N    1 
ATOM   465  C  CA   . ILE   A 1 30  ? -1.098  19.199  -33.393 1.00 20.32  ? 30  ILE   A CA   1 
ATOM   466  C  C    . ILE   A 1 30  ? -0.187  20.340  -33.837 1.00 20.30  ? 30  ILE   A C    1 
ATOM   467  O  O    . ILE   A 1 30  ? -0.632  21.298  -34.516 1.00 23.69  ? 30  ILE   A O    1 
ATOM   468  C  CB   . ILE   A 1 30  ? -0.545  17.823  -33.845 1.00 19.31  ? 30  ILE   A CB   1 
ATOM   469  C  CG1  . ILE   A 1 30  ? -0.528  17.716  -35.349 1.00 21.55  ? 30  ILE   A CG1  1 
ATOM   470  C  CG2  . ILE   A 1 30  ? -1.398  16.672  -33.263 1.00 20.60  ? 30  ILE   A CG2  1 
ATOM   471  C  CD1  . ILE   A 1 30  ? 0.282   16.516  -35.906 1.00 24.54  ? 30  ILE   A CD1  1 
ATOM   472  H  H    . ILE   A 1 30  ? -2.499  19.464  -34.745 1.00 23.82  ? 30  ILE   A H    1 
ATOM   473  H  HA   . ILE   A 1 30  ? -1.119  19.229  -32.424 1.00 24.38  ? 30  ILE   A HA   1 
ATOM   474  H  HB   . ILE   A 1 30  ? 0.363   17.754  -33.511 1.00 23.17  ? 30  ILE   A HB   1 
ATOM   475  H  HG12 . ILE   A 1 30  ? -1.441  17.621  -35.661 1.00 25.86  ? 30  ILE   A HG12 1 
ATOM   476  H  HG13 . ILE   A 1 30  ? -0.135  18.525  -35.711 1.00 25.86  ? 30  ILE   A HG13 1 
ATOM   477  H  HG21 . ILE   A 1 30  ? -0.997  15.825  -33.513 1.00 24.72  ? 30  ILE   A HG21 1 
ATOM   478  H  HG22 . ILE   A 1 30  ? -1.422  16.755  -32.297 1.00 24.72  ? 30  ILE   A HG22 1 
ATOM   479  H  HG23 . ILE   A 1 30  ? -2.296  16.732  -33.623 1.00 24.72  ? 30  ILE   A HG23 1 
ATOM   480  H  HD11 . ILE   A 1 30  ? 0.288   16.561  -36.875 1.00 29.45  ? 30  ILE   A HD11 1 
ATOM   481  H  HD12 . ILE   A 1 30  ? 1.190   16.563  -35.568 1.00 29.45  ? 30  ILE   A HD12 1 
ATOM   482  H  HD13 . ILE   A 1 30  ? -0.136  15.690  -35.615 1.00 29.45  ? 30  ILE   A HD13 1 
ATOM   483  N  N    . THR   A 1 31  ? 1.093   20.245  -33.531 1.00 20.89  ? 31  THR   A N    1 
ATOM   484  C  CA   . THR   A 1 31  ? 2.053   21.276  -33.898 1.00 21.49  ? 31  THR   A CA   1 
ATOM   485  C  C    . THR   A 1 31  ? 3.285   20.614  -34.496 1.00 26.78  ? 31  THR   A C    1 
ATOM   486  O  O    . THR   A 1 31  ? 3.506   19.423  -34.296 1.00 23.51  ? 31  THR   A O    1 
ATOM   487  C  CB   . THR   A 1 31  ? 2.412   22.191  -32.742 1.00 31.72  ? 31  THR   A CB   1 
ATOM   488  O  OG1  . THR   A 1 31  ? 2.660   21.418  -31.570 1.00 36.21  ? 31  THR   A OG1  1 
ATOM   489  C  CG2  . THR   A 1 31  ? 1.262   23.123  -32.394 1.00 31.34  ? 31  THR   A CG2  1 
ATOM   490  H  H    . THR   A 1 31  ? 1.439   19.583  -33.104 1.00 25.06  ? 31  THR   A H    1 
ATOM   491  H  HA   . THR   A 1 31  ? 1.665   21.850  -34.577 1.00 25.79  ? 31  THR   A HA   1 
ATOM   492  H  HB   . THR   A 1 31  ? 3.192   22.705  -33.004 1.00 38.06  ? 31  THR   A HB   1 
ATOM   493  H  HG1  . THR   A 1 31  ? 2.801   21.925  -30.915 1.00 43.46  ? 31  THR   A HG1  1 
ATOM   494  H  HG21 . THR   A 1 31  ? 1.488   23.652  -31.613 1.00 37.61  ? 31  THR   A HG21 1 
ATOM   495  H  HG22 . THR   A 1 31  ? 1.083   23.721  -33.137 1.00 37.61  ? 31  THR   A HG22 1 
ATOM   496  H  HG23 . THR   A 1 31  ? 0.463   22.607  -32.205 1.00 37.61  ? 31  THR   A HG23 1 
ATOM   497  N  N    . ARG   A 1 32  ? 4.052   21.360  -35.319 1.00 25.16  ? 32  ARG   A N    1 
ATOM   498  C  CA   . ARG   A 1 32  ? 5.225   20.798  -35.937 1.00 27.87  ? 32  ARG   A CA   1 
ATOM   499  C  C    . ARG   A 1 32  ? 6.363   21.805  -35.960 1.00 33.41  ? 32  ARG   A C    1 
ATOM   500  O  O    . ARG   A 1 32  ? 6.140   22.996  -36.206 1.00 35.68  ? 32  ARG   A O    1 
ATOM   501  C  CB   . ARG   A 1 32  ? 4.903   20.481  -37.395 1.00 31.61  ? 32  ARG   A CB   1 
ATOM   502  C  CG   . ARG   A 1 32  ? 6.041   19.756  -38.146 1.00 34.98  ? 32  ARG   A CG   1 
ATOM   503  C  CD   . ARG   A 1 32  ? 5.545   19.224  -39.493 1.00 35.15  ? 32  ARG   A CD   1 
ATOM   504  N  NE   . ARG   A 1 32  ? 6.496   18.316  -40.146 1.00 34.57  ? 32  ARG   A NE   1 
ATOM   505  C  CZ   . ARG   A 1 32  ? 7.457   18.677  -40.993 1.00 42.03  ? 32  ARG   A CZ   1 
ATOM   506  N  NH1  . ARG   A 1 32  ? 7.652   19.942  -41.330 1.00 39.70  ? 32  ARG   A NH1  1 
ATOM   507  N  NH2  . ARG   A 1 32  ? 8.244   17.740  -41.513 1.00 39.13  ? 32  ARG   A NH2  1 
ATOM   508  H  H    . ARG   A 1 32  ? 3.898   22.182  -35.521 1.00 30.19  ? 32  ARG   A H    1 
ATOM   509  H  HA   . ARG   A 1 32  ? 5.509   20.020  -35.433 1.00 33.45  ? 32  ARG   A HA   1 
ATOM   510  H  HB2  . ARG   A 1 32  ? 4.119   19.910  -37.423 1.00 37.93  ? 32  ARG   A HB2  1 
ATOM   511  H  HB3  . ARG   A 1 32  ? 4.725   21.313  -37.861 1.00 37.93  ? 32  ARG   A HB3  1 
ATOM   512  H  HG2  . ARG   A 1 32  ? 6.769   20.375  -38.308 1.00 41.97  ? 32  ARG   A HG2  1 
ATOM   513  H  HG3  . ARG   A 1 32  ? 6.354   19.007  -37.615 1.00 41.97  ? 32  ARG   A HG3  1 
ATOM   514  H  HD2  . ARG   A 1 32  ? 4.718   18.737  -39.353 1.00 42.18  ? 32  ARG   A HD2  1 
ATOM   515  H  HD3  . ARG   A 1 32  ? 5.393   19.973  -40.090 1.00 42.18  ? 32  ARG   A HD3  1 
ATOM   516  H  HE   . ARG   A 1 32  ? 6.426   17.478  -39.965 1.00 41.49  ? 32  ARG   A HE   1 
ATOM   517  H  HH11 . ARG   A 1 32  ? 7.150   20.557  -40.998 1.00 47.64  ? 32  ARG   A HH11 1 
ATOM   518  H  HH12 . ARG   A 1 32  ? 8.280   20.149  -41.880 1.00 47.64  ? 32  ARG   A HH12 1 
ATOM   519  H  HH21 . ARG   A 1 32  ? 8.128   16.915  -41.300 1.00 46.96  ? 32  ARG   A HH21 1 
ATOM   520  H  HH22 . ARG   A 1 32  ? 8.869   17.959  -42.061 1.00 46.96  ? 32  ARG   A HH22 1 
ATOM   521  N  N    . ASP   A 1 33  ? 7.571   21.325  -35.659 1.00 28.99  ? 33  ASP   A N    1 
ATOM   522  C  CA   . ASP   A 1 33  ? 8.798   22.118  -35.780 1.00 31.70  ? 33  ASP   A CA   1 
ATOM   523  C  C    . ASP   A 1 33  ? 9.621   21.542  -36.923 1.00 37.30  ? 33  ASP   A C    1 
ATOM   524  O  O    . ASP   A 1 33  ? 10.233  20.473  -36.783 1.00 32.45  ? 33  ASP   A O    1 
ATOM   525  C  CB   . ASP   A 1 33  ? 9.597   22.102  -34.472 1.00 37.81  ? 33  ASP   A CB   1 
ATOM   526  C  CG   . ASP   A 1 33  ? 10.912  22.883  -34.571 1.00 40.16  ? 33  ASP   A CG   1 
ATOM   527  O  OD1  . ASP   A 1 33  ? 11.219  23.397  -35.657 1.00 43.67  ? 33  ASP   A OD1  1 
ATOM   528  O  OD2  . ASP   A 1 33  ? 11.610  23.013  -33.544 1.00 53.83  ? 33  ASP   A OD2  1 
ATOM   529  H  H    . ASP   A 1 33  ? 7.709   20.525  -35.375 1.00 34.78  ? 33  ASP   A H    1 
ATOM   530  H  HA   . ASP   A 1 33  ? 8.567   23.037  -35.989 1.00 38.04  ? 33  ASP   A HA   1 
ATOM   531  H  HB2  . ASP   A 1 33  ? 9.062   22.503  -33.769 1.00 45.38  ? 33  ASP   A HB2  1 
ATOM   532  H  HB3  . ASP   A 1 33  ? 9.811   21.184  -34.243 1.00 45.38  ? 33  ASP   A HB3  1 
ATOM   533  N  N    . SER   A 1 34  ? 9.671   22.275  -38.046 1.00 34.46  ? 34  SER   A N    1 
ATOM   534  C  CA   . SER   A 1 34  ? 10.295  21.724  -39.241 1.00 42.31  ? 34  SER   A CA   1 
ATOM   535  C  C    . SER   A 1 34  ? 11.804  21.580  -39.066 1.00 36.41  ? 34  SER   A C    1 
ATOM   536  O  O    . SER   A 1 34  ? 12.425  20.726  -39.717 1.00 44.04  ? 34  SER   A O    1 
ATOM   537  C  CB   . SER   A 1 34  ? 9.971   22.608  -40.456 1.00 41.67  ? 34  SER   A CB   1 
ATOM   538  O  OG   . SER   A 1 34  ? 10.447  23.927  -40.220 1.00 46.29  ? 34  SER   A OG   1 
ATOM   539  H  H    . SER   A 1 34  ? 9.358   23.072  -38.133 1.00 41.35  ? 34  SER   A H    1 
ATOM   540  H  HA   . SER   A 1 34  ? 9.930   20.841  -39.410 1.00 50.77  ? 34  SER   A HA   1 
ATOM   541  H  HB2  . SER   A 1 34  ? 10.406  22.245  -41.243 1.00 50.00  ? 34  SER   A HB2  1 
ATOM   542  H  HB3  . SER   A 1 34  ? 9.010   22.633  -40.589 1.00 50.00  ? 34  SER   A HB3  1 
ATOM   543  H  HG   . SER   A 1 34  ? 11.285  23.922  -40.154 1.00 55.55  ? 34  SER   A HG   1 
ATOM   544  N  N    . SER   A 1 35  ? 12.420  22.423  -38.215 1.00 35.54  ? 35  SER   A N    1 
ATOM   545  C  CA   . SER   A 1 35  ? 13.877  22.369  -38.039 1.00 39.51  ? 35  SER   A CA   1 
ATOM   546  C  C    . SER   A 1 35  ? 14.370  20.990  -37.599 1.00 34.35  ? 35  SER   A C    1 
ATOM   547  O  O    . SER   A 1 35  ? 15.536  20.651  -37.861 1.00 36.43  ? 35  SER   A O    1 
ATOM   548  C  CB   . SER   A 1 35  ? 14.350  23.491  -37.104 1.00 42.08  ? 35  SER   A CB   1 
ATOM   549  O  OG   . SER   A 1 35  ? 14.197  23.094  -35.732 1.00 38.31  ? 35  SER   A OG   1 
ATOM   550  H  H    . SER   A 1 35  ? 12.023  23.019  -37.739 1.00 42.64  ? 35  SER   A H    1 
ATOM   551  H  HA   . SER   A 1 35  ? 14.304  22.540  -38.893 1.00 47.41  ? 35  SER   A HA   1 
ATOM   552  H  HB2  . SER   A 1 35  ? 15.286  23.677  -37.279 1.00 50.50  ? 35  SER   A HB2  1 
ATOM   553  H  HB3  . SER   A 1 35  ? 13.817  24.286  -37.267 1.00 50.50  ? 35  SER   A HB3  1 
ATOM   554  H  HG   . SER   A 1 35  ? 13.406  22.849  -35.590 1.00 45.97  ? 35  SER   A HG   1 
ATOM   555  N  N    . VAL   A 1 36  ? 13.495  20.170  -37.001 1.00 38.82  ? 36  VAL   A N    1 
ATOM   556  C  CA   . VAL   A 1 36  ? 13.865  18.833  -36.529 1.00 36.98  ? 36  VAL   A CA   1 
ATOM   557  C  C    . VAL   A 1 36  ? 12.920  17.749  -37.052 1.00 35.70  ? 36  VAL   A C    1 
ATOM   558  O  O    . VAL   A 1 36  ? 12.994  16.586  -36.628 1.00 32.66  ? 36  VAL   A O    1 
ATOM   559  C  CB   . VAL   A 1 36  ? 13.947  18.782  -34.983 1.00 38.50  ? 36  VAL   A CB   1 
ATOM   560  C  CG1  . VAL   A 1 36  ? 15.198  19.501  -34.474 1.00 43.65  ? 36  VAL   A CG1  1 
ATOM   561  C  CG2  . VAL   A 1 36  ? 12.684  19.386  -34.332 1.00 37.99  ? 36  VAL   A CG2  1 
ATOM   562  H  H    . VAL   A 1 36  ? 12.671  20.370  -36.855 1.00 46.59  ? 36  VAL   A H    1 
ATOM   563  H  HA   . VAL   A 1 36  ? 14.738  18.642  -36.906 1.00 44.37  ? 36  VAL   A HA   1 
ATOM   564  H  HB   . VAL   A 1 36  ? 14.003  17.850  -34.721 1.00 46.20  ? 36  VAL   A HB   1 
ATOM   565  H  HG11 . VAL   A 1 36  ? 15.218  19.453  -33.505 1.00 52.38  ? 36  VAL   A HG11 1 
ATOM   566  H  HG12 . VAL   A 1 36  ? 15.984  19.067  -34.842 1.00 52.38  ? 36  VAL   A HG12 1 
ATOM   567  H  HG13 . VAL   A 1 36  ? 15.168  20.428  -34.759 1.00 52.38  ? 36  VAL   A HG13 1 
ATOM   568  H  HG21 . VAL   A 1 36  ? 12.730  19.257  -33.372 1.00 45.58  ? 36  VAL   A HG21 1 
ATOM   569  H  HG22 . VAL   A 1 36  ? 12.645  20.333  -34.537 1.00 45.58  ? 36  VAL   A HG22 1 
ATOM   570  H  HG23 . VAL   A 1 36  ? 11.900  18.938  -34.689 1.00 45.58  ? 36  VAL   A HG23 1 
ATOM   571  N  N    . GLU   A 1 37  ? 12.037  18.103  -37.979 1.00 33.77  ? 37  GLU   A N    1 
ATOM   572  C  CA   . GLU   A 1 37  ? 11.044  17.174  -38.520 1.00 38.74  ? 37  GLU   A CA   1 
ATOM   573  C  C    . GLU   A 1 37  ? 10.287  16.434  -37.415 1.00 32.80  ? 37  GLU   A C    1 
ATOM   574  O  O    . GLU   A 1 37  ? 10.136  15.215  -37.459 1.00 30.36  ? 37  GLU   A O    1 
ATOM   575  C  CB   . GLU   A 1 37  ? 11.699  16.154  -39.427 1.00 36.30  ? 37  GLU   A CB   1 
ATOM   576  C  CG   . GLU   A 1 37  ? 12.199  16.730  -40.759 1.00 43.09  ? 37  GLU   A CG   1 
ATOM   577  C  CD   . GLU   A 1 37  ? 12.407  15.661  -41.816 1.00 55.07  ? 37  GLU   A CD   1 
ATOM   578  O  OE1  . GLU   A 1 37  ? 13.330  14.830  -41.627 1.00 50.45  ? 37  GLU   A OE1  1 
ATOM   579  O  OE2  . GLU   A 1 37  ? 11.657  15.659  -42.826 1.00 63.03  ? 37  GLU   A OE2  1 
ATOM   580  H  H    . GLU   A 1 37  ? 11.990  18.892  -38.319 1.00 40.52  ? 37  GLU   A H    1 
ATOM   581  H  HA   . GLU   A 1 37  ? 10.408  17.706  -39.023 1.00 46.48  ? 37  GLU   A HA   1 
ATOM   582  H  HB2  . GLU   A 1 37  ? 12.462  15.772  -38.965 1.00 43.56  ? 37  GLU   A HB2  1 
ATOM   583  H  HB3  . GLU   A 1 37  ? 11.053  15.459  -39.630 1.00 43.56  ? 37  GLU   A HB3  1 
ATOM   584  H  HG2  . GLU   A 1 37  ? 11.545  17.363  -41.096 1.00 51.71  ? 37  GLU   A HG2  1 
ATOM   585  H  HG3  . GLU   A 1 37  ? 13.048  17.176  -40.612 1.00 51.71  ? 37  GLU   A HG3  1 
ATOM   586  N  N    . MET   A 1 38  ? 9.821   17.175  -36.422 1.00 29.88  ? 38  MET   A N    1 
ATOM   587  C  CA   . MET   A 1 38  ? 9.131   16.568  -35.294 1.00 24.76  ? 38  MET   A CA   1 
ATOM   588  C  C    . MET   A 1 38  ? 7.768   17.214  -35.124 1.00 27.98  ? 38  MET   A C    1 
ATOM   589  O  O    . MET   A 1 38  ? 7.622   18.425  -35.331 1.00 28.36  ? 38  MET   A O    1 
ATOM   590  C  CB   . MET   A 1 38  ? 9.874   16.778  -33.981 1.00 31.47  ? 38  MET   A CB   1 
ATOM   591  C  CG   . MET   A 1 38  ? 11.225  16.107  -33.921 1.00 41.25  ? 38  MET   A CG   1 
ATOM   592  S  SD   . MET   A 1 38  ? 11.078  14.305  -33.846 1.00 66.11  ? 38  MET   A SD   1 
ATOM   593  C  CE   . MET   A 1 38  ? 12.834  13.866  -33.825 1.00 45.32  ? 38  MET   A CE   1 
ATOM   594  H  H    . MET   A 1 38  ? 9.893   18.031  -36.379 1.00 35.86  ? 38  MET   A H    1 
ATOM   595  H  HA   . MET   A 1 38  ? 9.059   15.618  -35.477 1.00 29.71  ? 38  MET   A HA   1 
ATOM   596  H  HB2  . MET   A 1 38  ? 10.012  17.729  -33.851 1.00 37.76  ? 38  MET   A HB2  1 
ATOM   597  H  HB3  . MET   A 1 38  ? 9.335   16.419  -33.259 1.00 37.76  ? 38  MET   A HB3  1 
ATOM   598  H  HG2  . MET   A 1 38  ? 11.732  16.338  -34.716 1.00 49.50  ? 38  MET   A HG2  1 
ATOM   599  H  HG3  . MET   A 1 38  ? 11.697  16.407  -33.128 1.00 49.50  ? 38  MET   A HG3  1 
ATOM   600  H  HE1  . MET   A 1 38  ? 12.918  12.901  -33.776 1.00 54.38  ? 38  MET   A HE1  1 
ATOM   601  H  HE2  . MET   A 1 38  ? 13.251  14.193  -34.638 1.00 54.38  ? 38  MET   A HE2  1 
ATOM   602  H  HE3  . MET   A 1 38  ? 13.253  14.274  -33.051 1.00 54.38  ? 38  MET   A HE3  1 
ATOM   603  N  N    . CYS   A 1 39  ? 6.766   16.412  -34.747 1.00 22.17  ? 39  CYS   A N    1 
ATOM   604  C  CA   . CYS   A 1 39  ? 5.432   16.893  -34.438 1.00 21.17  ? 39  CYS   A CA   1 
ATOM   605  C  C    . CYS   A 1 39  ? 5.223   16.712  -32.938 1.00 19.84  ? 39  CYS   A C    1 
ATOM   606  O  O    . CYS   A 1 39  ? 5.921   15.922  -32.284 1.00 21.55  ? 39  CYS   A O    1 
ATOM   607  C  CB   . CYS   A 1 39  ? 4.360   16.088  -35.148 1.00 20.31  ? 39  CYS   A CB   1 
ATOM   608  S  SG   . CYS   A 1 39  ? 4.127   16.587  -36.871 1.00 26.99  ? 39  CYS   A SG   1 
ATOM   609  H  H    . CYS   A 1 39  ? 6.846   15.559  -34.663 1.00 26.61  ? 39  CYS   A H    1 
ATOM   610  H  HA   . CYS   A 1 39  ? 5.346   17.819  -34.710 1.00 25.41  ? 39  CYS   A HA   1 
ATOM   611  H  HB2  . CYS   A 1 39  ? 4.612   15.151  -35.140 1.00 24.37  ? 39  CYS   A HB2  1 
ATOM   612  H  HB3  . CYS   A 1 39  ? 3.517   16.208  -34.685 1.00 24.37  ? 39  CYS   A HB3  1 
ATOM   613  N  N    . PHE   A 1 40  ? 4.270   17.459  -32.397 1.00 18.98  ? 40  PHE   A N    1 
ATOM   614  C  CA   . PHE   A 1 40  ? 4.029   17.495  -30.958 1.00 17.42  ? 40  PHE   A CA   1 
ATOM   615  C  C    . PHE   A 1 40  ? 2.545   17.400  -30.713 1.00 17.65  ? 40  PHE   A C    1 
ATOM   616  O  O    . PHE   A 1 40  ? 1.745   18.002  -31.436 1.00 18.55  ? 40  PHE   A O    1 
ATOM   617  C  CB   . PHE   A 1 40  ? 4.542   18.811  -30.351 1.00 22.25  ? 40  PHE   A CB   1 
ATOM   618  C  CG   . PHE   A 1 40  ? 5.993   19.079  -30.671 1.00 22.84  ? 40  PHE   A CG   1 
ATOM   619  C  CD1  . PHE   A 1 40  ? 6.325   19.718  -31.833 1.00 28.75  ? 40  PHE   A CD1  1 
ATOM   620  C  CD2  . PHE   A 1 40  ? 6.990   18.627  -29.832 1.00 23.93  ? 40  PHE   A CD2  1 
ATOM   621  C  CE1  . PHE   A 1 40  ? 7.667   19.908  -32.173 1.00 29.33  ? 40  PHE   A CE1  1 
ATOM   622  C  CE2  . PHE   A 1 40  ? 8.343   18.813  -30.131 1.00 26.22  ? 40  PHE   A CE2  1 
ATOM   623  C  CZ   . PHE   A 1 40  ? 8.677   19.475  -31.287 1.00 29.07  ? 40  PHE   A CZ   1 
ATOM   624  H  H    . PHE   A 1 40  ? 3.741   17.963  -32.849 1.00 22.77  ? 40  PHE   A H    1 
ATOM   625  H  HA   . PHE   A 1 40  ? 4.478   16.749  -30.530 1.00 20.90  ? 40  PHE   A HA   1 
ATOM   626  H  HB2  . PHE   A 1 40  ? 4.016   19.546  -30.704 1.00 26.70  ? 40  PHE   A HB2  1 
ATOM   627  H  HB3  . PHE   A 1 40  ? 4.450   18.770  -29.387 1.00 26.70  ? 40  PHE   A HB3  1 
ATOM   628  H  HD1  . PHE   A 1 40  ? 5.655   20.026  -32.400 1.00 34.50  ? 40  PHE   A HD1  1 
ATOM   629  H  HD2  . PHE   A 1 40  ? 6.756   18.186  -29.047 1.00 28.72  ? 40  PHE   A HD2  1 
ATOM   630  H  HE1  . PHE   A 1 40  ? 7.894   20.318  -32.977 1.00 35.20  ? 40  PHE   A HE1  1 
ATOM   631  H  HE2  . PHE   A 1 40  ? 9.003   18.495  -29.559 1.00 31.47  ? 40  PHE   A HE2  1 
ATOM   632  H  HZ   . PHE   A 1 40  ? 9.571   19.639  -31.487 1.00 34.88  ? 40  PHE   A HZ   1 
ATOM   633  N  N    . MET   A 1 41  ? 2.161   16.607  -29.710 1.00 17.20  ? 41  MET   A N    1 
ATOM   634  C  CA   . MET   A 1 41  ? 0.745   16.408  -29.358 1.00 14.91  ? 41  MET   A CA   1 
ATOM   635  C  C    . MET   A 1 41  ? 0.312   17.577  -28.467 1.00 15.53  ? 41  MET   A C    1 
ATOM   636  O  O    . MET   A 1 41  ? 0.069   17.458  -27.264 1.00 15.60  ? 41  MET   A O    1 
ATOM   637  C  CB   . MET   A 1 41  ? 0.599   15.081  -28.595 1.00 15.59  ? 41  MET   A CB   1 
ATOM   638  C  CG   . MET   A 1 41  ? 0.917   13.913  -29.467 1.00 15.84  ? 41  MET   A CG   1 
ATOM   639  S  SD   . MET   A 1 41  ? -0.240  13.589  -30.798 1.00 17.66  ? 41  MET   A SD   1 
ATOM   640  C  CE   . MET   A 1 41  ? -1.614  12.923  -29.853 1.00 17.88  ? 41  MET   A CE   1 
ATOM   641  H  H    . MET   A 1 41  ? 2.705   16.167  -29.210 1.00 20.64  ? 41  MET   A H    1 
ATOM   642  H  HA   . MET   A 1 41  ? 0.206   16.380  -30.164 1.00 17.89  ? 41  MET   A HA   1 
ATOM   643  H  HB2  . MET   A 1 41  ? 1.209   15.076  -27.841 1.00 18.71  ? 41  MET   A HB2  1 
ATOM   644  H  HB3  . MET   A 1 41  ? -0.315  14.990  -28.283 1.00 18.71  ? 41  MET   A HB3  1 
ATOM   645  H  HG2  . MET   A 1 41  ? 1.785   14.064  -29.873 1.00 19.01  ? 41  MET   A HG2  1 
ATOM   646  H  HG3  . MET   A 1 41  ? 0.945   13.118  -28.912 1.00 19.01  ? 41  MET   A HG3  1 
ATOM   647  H  HE1  . MET   A 1 41  ? -2.339  12.705  -30.460 1.00 21.46  ? 41  MET   A HE1  1 
ATOM   648  H  HE2  . MET   A 1 41  ? -1.320  12.123  -29.389 1.00 21.46  ? 41  MET   A HE2  1 
ATOM   649  H  HE3  . MET   A 1 41  ? -1.908  13.588  -29.212 1.00 21.46  ? 41  MET   A HE3  1 
ATOM   650  N  N    . GLU   A 1 42  ? 0.282   18.747  -29.078 1.00 16.18  ? 42  GLU   A N    1 
ATOM   651  C  CA   . GLU   A 1 42  ? -0.035  19.964  -28.357 1.00 17.20  ? 42  GLU   A CA   1 
ATOM   652  C  C    . GLU   A 1 42  ? -0.616  20.976  -29.333 1.00 17.98  ? 42  GLU   A C    1 
ATOM   653  O  O    . GLU   A 1 42  ? -0.205  21.069  -30.494 1.00 19.18  ? 42  GLU   A O    1 
ATOM   654  C  CB   . GLU   A 1 42  ? 1.237   20.525  -27.734 1.00 20.34  ? 42  GLU   A CB   1 
ATOM   655  C  CG   . GLU   A 1 42  ? 1.037   21.857  -27.083 1.00 22.65  ? 42  GLU   A CG   1 
ATOM   656  C  CD   . GLU   A 1 42  ? 2.259   22.358  -26.322 1.00 26.85  ? 42  GLU   A CD   1 
ATOM   657  O  OE1  . GLU   A 1 42  ? 3.389   21.933  -26.638 1.00 33.83  ? 42  GLU   A OE1  1 
ATOM   658  O  OE2  . GLU   A 1 42  ? 2.069   23.226  -25.441 1.00 25.54  ? 42  GLU   A OE2  1 
ATOM   659  H  H    . GLU   A 1 42  ? 0.443   18.863  -29.915 1.00 19.42  ? 42  GLU   A H    1 
ATOM   660  H  HA   . GLU   A 1 42  ? -0.697  19.795  -27.668 1.00 20.64  ? 42  GLU   A HA   1 
ATOM   661  H  HB2  . GLU   A 1 42  ? 1.554   19.906  -27.057 1.00 24.40  ? 42  GLU   A HB2  1 
ATOM   662  H  HB3  . GLU   A 1 42  ? 1.907   20.629  -28.427 1.00 24.40  ? 42  GLU   A HB3  1 
ATOM   663  H  HG2  . GLU   A 1 42  ? 0.826   22.511  -27.768 1.00 27.18  ? 42  GLU   A HG2  1 
ATOM   664  H  HG3  . GLU   A 1 42  ? 0.303   21.790  -26.452 1.00 27.18  ? 42  GLU   A HG3  1 
ATOM   665  N  N    . ASN   A 1 43  ? -1.578  21.725  -28.818 1.00 17.12  ? 43  ASN   A N    1 
ATOM   666  C  CA   . ASN   A 1 43  ? -2.112  22.930  -29.441 1.00 17.87  ? 43  ASN   A CA   1 
ATOM   667  C  C    . ASN   A 1 43  ? -2.290  23.962  -28.347 1.00 19.41  ? 43  ASN   A C    1 
ATOM   668  O  O    . ASN   A 1 43  ? -2.000  23.699  -27.174 1.00 18.87  ? 43  ASN   A O    1 
ATOM   669  C  CB   . ASN   A 1 43  ? -3.376  22.586  -30.221 1.00 19.02  ? 43  ASN   A CB   1 
ATOM   670  C  CG   . ASN   A 1 43  ? -4.393  21.898  -29.401 1.00 17.93  ? 43  ASN   A CG   1 
ATOM   671  O  OD1  . ASN   A 1 43  ? -4.939  22.484  -28.450 1.00 18.56  ? 43  ASN   A OD1  1 
ATOM   672  N  ND2  . ASN   A 1 43  ? -4.660  20.617  -29.677 1.00 17.12  ? 43  ASN   A ND2  1 
ATOM   673  H  H    . ASN   A 1 43  ? -1.960  21.549  -28.068 1.00 20.54  ? 43  ASN   A H    1 
ATOM   674  H  HA   . ASN   A 1 43  ? -1.497  23.321  -30.080 1.00 21.44  ? 43  ASN   A HA   1 
ATOM   675  H  HB2  . ASN   A 1 43  ? -3.770  23.405  -30.560 1.00 22.82  ? 43  ASN   A HB2  1 
ATOM   676  H  HB3  . ASN   A 1 43  ? -3.141  22.001  -30.958 1.00 22.82  ? 43  ASN   A HB3  1 
ATOM   677  H  HD21 . ASN   A 1 43  ? -5.248  20.191  -29.215 1.00 20.55  ? 43  ASN   A HD21 1 
ATOM   678  H  HD22 . ASN   A 1 43  ? -4.244  20.218  -30.315 1.00 20.55  ? 43  ASN   A HD22 1 
ATOM   679  N  N    . THR   A 1 44  ? -2.832  25.125  -28.690 1.00 20.21  ? 44  THR   A N    1 
ATOM   680  C  CA   . THR   A 1 44  ? -2.911  26.175  -27.693 1.00 19.95  ? 44  THR   A CA   1 
ATOM   681  C  C    . THR   A 1 44  ? -3.697  25.710  -26.497 1.00 21.58  ? 44  THR   A C    1 
ATOM   682  O  O    . THR   A 1 44  ? -3.352  26.020  -25.349 1.00 21.31  ? 44  THR   A O    1 
ATOM   683  C  CB   . THR   A 1 44  ? -3.607  27.385  -28.319 1.00 25.98  ? 44  THR   A CB   1 
ATOM   684  O  OG1  . THR   A 1 44  ? -2.767  27.893  -29.346 1.00 31.03  ? 44  THR   A OG1  1 
ATOM   685  C  CG2  . THR   A 1 44  ? -3.881  28.478  -27.285 1.00 27.75  ? 44  THR   A CG2  1 
ATOM   686  H  H    . THR   A 1 44  ? -3.149  25.322  -29.465 1.00 24.25  ? 44  THR   A H    1 
ATOM   687  H  HA   . THR   A 1 44  ? -2.019  26.423  -27.403 1.00 23.94  ? 44  THR   A HA   1 
ATOM   688  H  HB   . THR   A 1 44  ? -4.467  27.120  -28.682 1.00 31.18  ? 44  THR   A HB   1 
ATOM   689  H  HG1  . THR   A 1 44  ? -3.127  28.559  -29.709 1.00 37.24  ? 44  THR   A HG1  1 
ATOM   690  H  HG21 . THR   A 1 44  ? -4.127  29.303  -27.731 1.00 33.30  ? 44  THR   A HG21 1 
ATOM   691  H  HG22 . THR   A 1 44  ? -4.608  28.207  -26.701 1.00 33.30  ? 44  THR   A HG22 1 
ATOM   692  H  HG23 . THR   A 1 44  ? -3.088  28.633  -26.749 1.00 33.30  ? 44  THR   A HG23 1 
ATOM   693  N  N    . ASP   A 1 45  ? -4.767  24.961  -26.719 1.00 17.78  ? 45  ASP   A N    1 
ATOM   694  C  CA   . ASP   A 1 45  ? -5.694  24.631  -25.652 1.00 16.75  ? 45  ASP   A CA   1 
ATOM   695  C  C    . ASP   A 1 45  ? -5.357  23.368  -24.843 1.00 14.11  ? 45  ASP   A C    1 
ATOM   696  O  O    . ASP   A 1 45  ? -5.782  23.246  -23.676 1.00 15.43  ? 45  ASP   A O    1 
ATOM   697  C  CB   . ASP   A 1 45  ? -7.120  24.464  -26.182 1.00 18.40  ? 45  ASP   A CB   1 
ATOM   698  C  CG   . ASP   A 1 45  ? -7.719  25.793  -26.686 1.00 34.20  ? 45  ASP   A CG   1 
ATOM   699  O  OD1  . ASP   A 1 45  ? -7.229  26.903  -26.327 1.00 34.22  ? 45  ASP   A OD1  1 
ATOM   700  O  OD2  . ASP   A 1 45  ? -8.651  25.713  -27.496 1.00 32.25  ? 45  ASP   A OD2  1 
ATOM   701  H  H    . ASP   A 1 45  ? -4.978  24.629  -27.483 1.00 21.34  ? 45  ASP   A H    1 
ATOM   702  H  HA   . ASP   A 1 45  ? -5.660  25.388  -25.046 1.00 20.10  ? 45  ASP   A HA   1 
ATOM   703  H  HB2  . ASP   A 1 45  ? -7.112  23.837  -26.923 1.00 22.08  ? 45  ASP   A HB2  1 
ATOM   704  H  HB3  . ASP   A 1 45  ? -7.687  24.129  -25.470 1.00 22.08  ? 45  ASP   A HB3  1 
ATOM   705  N  N    . VAL   A 1 46  ? -4.634  22.424  -25.438 1.00 14.26  ? 46  VAL   A N    1 
ATOM   706  C  CA   . VAL   A 1 46  ? -4.436  21.099  -24.854 1.00 13.17  ? 46  VAL   A CA   1 
ATOM   707  C  C    . VAL   A 1 46  ? -3.038  20.606  -25.182 1.00 13.14  ? 46  VAL   A C    1 
ATOM   708  O  O    . VAL   A 1 46  ? -2.586  20.728  -26.321 1.00 14.55  ? 46  VAL   A O    1 
ATOM   709  C  CB   . VAL   A 1 46  ? -5.434  20.052  -25.433 1.00 13.18  ? 46  VAL   A CB   1 
ATOM   710  C  CG1  . VAL   A 1 46  ? -5.315  18.761  -24.723 1.00 13.24  ? 46  VAL   A CG1  1 
ATOM   711  C  CG2  . VAL   A 1 46  ? -6.844  20.566  -25.335 1.00 16.08  ? 46  VAL   A CG2  1 
ATOM   712  H  H    . VAL   A 1 46  ? -4.239  22.528  -26.196 1.00 17.12  ? 46  VAL   A H    1 
ATOM   713  H  HA   . VAL   A 1 46  ? -4.549  21.190  -23.895 1.00 15.81  ? 46  VAL   A HA   1 
ATOM   714  H  HB   . VAL   A 1 46  ? -5.219  19.905  -26.367 1.00 15.82  ? 46  VAL   A HB   1 
ATOM   715  H  HG11 . VAL   A 1 46  ? -6.040  18.179  -25.002 1.00 15.89  ? 46  VAL   A HG11 1 
ATOM   716  H  HG12 . VAL   A 1 46  ? -4.462  18.356  -24.944 1.00 15.89  ? 46  VAL   A HG12 1 
ATOM   717  H  HG13 . VAL   A 1 46  ? -5.368  18.919  -23.767 1.00 15.89  ? 46  VAL   A HG13 1 
ATOM   718  H  HG21 . VAL   A 1 46  ? -7.456  19.862  -25.604 1.00 19.30  ? 46  VAL   A HG21 1 
ATOM   719  H  HG22 . VAL   A 1 46  ? -7.022  20.826  -24.417 1.00 19.30  ? 46  VAL   A HG22 1 
ATOM   720  H  HG23 . VAL   A 1 46  ? -6.942  21.332  -25.921 1.00 19.30  ? 46  VAL   A HG23 1 
ATOM   721  N  N    . LYS   A 1 47  ? -2.354  20.036  -24.166 1.00 14.30  ? 47  LYS   A N    1 
ATOM   722  C  CA   . LYS   A 1 47  ? -1.067  19.372  -24.363 1.00 13.72  ? 47  LYS   A CA   1 
ATOM   723  C  C    . LYS   A 1 47  ? -1.191  17.957  -23.811 1.00 13.48  ? 47  LYS   A C    1 
ATOM   724  O  O    . LYS   A 1 47  ? -1.713  17.763  -22.695 1.00 13.98  ? 47  LYS   A O    1 
ATOM   725  C  CB   . LYS   A 1 47  ? 0.066   20.103  -23.591 1.00 15.20  ? 47  LYS   A CB   1 
ATOM   726  C  CG   . LYS   A 1 47  ? 1.360   19.281  -23.533 1.00 16.95  ? 47  LYS   A CG   1 
ATOM   727  C  CD   . LYS   A 1 47  ? 2.541   20.119  -23.051 1.00 19.54  ? 47  LYS   A CD   1 
ATOM   728  C  CE   . LYS   A 1 47  ? 2.349   20.650  -21.669 1.00 18.59  ? 47  LYS   A CE   1 
ATOM   729  N  NZ   . LYS   A 1 47  ? 3.632   21.387  -21.217 1.00 24.10  ? 47  LYS   A NZ   1 
ATOM   730  H  H    . LYS   A 1 47  ? -2.627  20.026  -23.350 1.00 17.17  ? 47  LYS   A H    1 
ATOM   731  H  HA   . LYS   A 1 47  ? -0.845  19.353  -25.307 1.00 16.46  ? 47  LYS   A HA   1 
ATOM   732  H  HB2  . LYS   A 1 47  ? 0.262   20.943  -24.036 1.00 18.24  ? 47  LYS   A HB2  1 
ATOM   733  H  HB3  . LYS   A 1 47  ? -0.226  20.270  -22.682 1.00 18.24  ? 47  LYS   A HB3  1 
ATOM   734  H  HG2  . LYS   A 1 47  ? 1.242   18.540  -22.918 1.00 20.34  ? 47  LYS   A HG2  1 
ATOM   735  H  HG3  . LYS   A 1 47  ? 1.567   18.946  -24.420 1.00 20.34  ? 47  LYS   A HG3  1 
ATOM   736  H  HD2  . LYS   A 1 47  ? 3.340   19.570  -23.052 1.00 23.45  ? 47  LYS   A HD2  1 
ATOM   737  H  HD3  . LYS   A 1 47  ? 2.656   20.875  -23.648 1.00 23.45  ? 47  LYS   A HD3  1 
ATOM   738  H  HE2  . LYS   A 1 47  ? 1.607   21.275  -21.657 1.00 22.31  ? 47  LYS   A HE2  1 
ATOM   739  H  HE3  . LYS   A 1 47  ? 2.176   19.917  -21.057 1.00 22.31  ? 47  LYS   A HE3  1 
ATOM   740  H  HZ1  . LYS   A 1 47  ? 3.519   21.722  -20.400 1.00 28.92  ? 47  LYS   A HZ1  1 
ATOM   741  H  HZ2  . LYS   A 1 47  ? 4.320   20.823  -21.205 1.00 28.92  ? 47  LYS   A HZ2  1 
ATOM   742  H  HZ3  . LYS   A 1 47  ? 3.815   22.053  -21.779 1.00 28.92  ? 47  LYS   A HZ3  1 
ATOM   743  N  N    . VAL   A 1 48  ? -0.710  16.965  -24.575 1.00 13.03  ? 48  VAL   A N    1 
ATOM   744  C  CA   . VAL   A 1 48  ? -0.611  15.597  -24.089 1.00 12.60  ? 48  VAL   A CA   1 
ATOM   745  C  C    . VAL   A 1 48  ? 0.849   15.278  -23.774 1.00 13.20  ? 48  VAL   A C    1 
ATOM   746  O  O    . VAL   A 1 48  ? 1.733   15.482  -24.623 1.00 14.21  ? 48  VAL   A O    1 
ATOM   747  C  CB   . VAL   A 1 48  ? -1.136  14.605  -25.127 1.00 13.09  ? 48  VAL   A CB   1 
ATOM   748  C  CG1  . VAL   A 1 48  ? -0.842  13.187  -24.663 1.00 15.70  ? 48  VAL   A CG1  1 
ATOM   749  C  CG2  . VAL   A 1 48  ? -2.649  14.797  -25.274 1.00 16.82  ? 48  VAL   A CG2  1 
ATOM   750  H  H    . VAL   A 1 48  ? -0.434  17.070  -25.383 1.00 15.64  ? 48  VAL   A H    1 
ATOM   751  H  HA   . VAL   A 1 48  ? -1.128  15.523  -23.272 1.00 15.12  ? 48  VAL   A HA   1 
ATOM   752  H  HB   . VAL   A 1 48  ? -0.706  14.752  -25.984 1.00 15.71  ? 48  VAL   A HB   1 
ATOM   753  H  HG11 . VAL   A 1 48  ? -1.389  12.569  -25.172 1.00 18.84  ? 48  VAL   A HG11 1 
ATOM   754  H  HG12 . VAL   A 1 48  ? 0.097   12.995  -24.810 1.00 18.84  ? 48  VAL   A HG12 1 
ATOM   755  H  HG13 . VAL   A 1 48  ? -1.051  13.114  -23.719 1.00 18.84  ? 48  VAL   A HG13 1 
ATOM   756  H  HG21 . VAL   A 1 48  ? -2.990  14.145  -25.906 1.00 20.18  ? 48  VAL   A HG21 1 
ATOM   757  H  HG22 . VAL   A 1 48  ? -3.069  14.670  -24.409 1.00 20.18  ? 48  VAL   A HG22 1 
ATOM   758  H  HG23 . VAL   A 1 48  ? -2.823  15.694  -25.598 1.00 20.18  ? 48  VAL   A HG23 1 
ATOM   759  N  N    . VAL   A 1 49  ? 1.084   14.788  -22.557 1.00 12.98  ? 49  VAL   A N    1 
ATOM   760  C  CA   . VAL   A 1 49  ? 2.391   14.319  -22.085 1.00 13.53  ? 49  VAL   A CA   1 
ATOM   761  C  C    . VAL   A 1 49  ? 2.365   12.787  -22.056 1.00 13.38  ? 49  VAL   A C    1 
ATOM   762  O  O    . VAL   A 1 49  ? 1.462   12.210  -21.442 1.00 13.67  ? 49  VAL   A O    1 
ATOM   763  C  CB   . VAL   A 1 49  ? 2.654   14.887  -20.679 1.00 14.00  ? 49  VAL   A CB   1 
ATOM   764  C  CG1  . VAL   A 1 49  ? 3.932   14.371  -20.099 1.00 16.57  ? 49  VAL   A CG1  1 
ATOM   765  C  CG2  . VAL   A 1 49  ? 2.641   16.404  -20.680 1.00 15.34  ? 49  VAL   A CG2  1 
ATOM   766  H  H    . VAL   A 1 49  ? 0.473   14.712  -21.956 1.00 15.58  ? 49  VAL   A H    1 
ATOM   767  H  HA   . VAL   A 1 49  ? 3.097   14.594  -22.691 1.00 16.24  ? 49  VAL   A HA   1 
ATOM   768  H  HB   . VAL   A 1 49  ? 1.932   14.583  -20.108 1.00 16.80  ? 49  VAL   A HB   1 
ATOM   769  H  HG11 . VAL   A 1 49  ? 4.124   14.852  -19.279 1.00 19.88  ? 49  VAL   A HG11 1 
ATOM   770  H  HG12 . VAL   A 1 49  ? 3.835   13.424  -19.912 1.00 19.88  ? 49  VAL   A HG12 1 
ATOM   771  H  HG13 . VAL   A 1 49  ? 4.648   14.510  -20.738 1.00 19.88  ? 49  VAL   A HG13 1 
ATOM   772  H  HG21 . VAL   A 1 49  ? 2.839   16.722  -19.786 1.00 18.40  ? 49  VAL   A HG21 1 
ATOM   773  H  HG22 . VAL   A 1 49  ? 3.312   16.725  -21.302 1.00 18.40  ? 49  VAL   A HG22 1 
ATOM   774  H  HG23 . VAL   A 1 49  ? 1.762   16.711  -20.954 1.00 18.40  ? 49  VAL   A HG23 1 
ATOM   775  N  N    . ASP   A 1 50  ? 3.330   12.135  -22.681 1.00 13.98  ? 50  ASP   A N    1 
ATOM   776  C  CA   . ASP   A 1 50  ? 3.479   10.696  -22.592 1.00 15.30  ? 50  ASP   A CA   1 
ATOM   777  C  C    . ASP   A 1 50  ? 4.367   10.442  -21.360 1.00 15.04  ? 50  ASP   A C    1 
ATOM   778  O  O    . ASP   A 1 50  ? 5.597   10.625  -21.419 1.00 16.11  ? 50  ASP   A O    1 
ATOM   779  C  CB   . ASP   A 1 50  ? 4.103   10.115  -23.857 1.00 17.01  ? 50  ASP   A CB   1 
ATOM   780  C  CG   . ASP   A 1 50  ? 4.274   8.626   -23.796 1.00 16.97  ? 50  ASP   A CG   1 
ATOM   781  O  OD1  . ASP   A 1 50  ? 4.035   7.977   -22.779 1.00 16.66  ? 50  ASP   A OD1  1 
ATOM   782  O  OD2  . ASP   A 1 50  ? 4.809   8.048   -24.812 1.00 20.63  ? 50  ASP   A OD2  1 
ATOM   783  H  H    . ASP   A 1 50  ? 3.925   12.513  -23.174 1.00 16.77  ? 50  ASP   A H    1 
ATOM   784  H  HA   . ASP   A 1 50  ? 2.615   10.267  -22.487 1.00 18.36  ? 50  ASP   A HA   1 
ATOM   785  H  HB2  . ASP   A 1 50  ? 3.531   10.320  -24.614 1.00 20.41  ? 50  ASP   A HB2  1 
ATOM   786  H  HB3  . ASP   A 1 50  ? 4.979   10.511  -23.987 1.00 20.41  ? 50  ASP   A HB3  1 
ATOM   787  N  N    . MET   A 1 51  ? 3.768   9.920   -20.289 1.00 14.75  ? 51  MET   A N    1 
ATOM   788  C  CA   . MET   A 1 51  ? 4.548   9.682   -19.088 1.00 14.43  ? 51  MET   A CA   1 
ATOM   789  C  C    . MET   A 1 51  ? 5.441   8.437   -19.235 1.00 15.82  ? 51  MET   A C    1 
ATOM   790  O  O    . MET   A 1 51  ? 6.324   8.227   -18.366 1.00 17.29  ? 51  MET   A O    1 
ATOM   791  C  CB   . MET   A 1 51  ? 3.623   9.407   -17.900 1.00 15.60  ? 51  MET   A CB   1 
ATOM   792  C  CG   . MET   A 1 51  ? 2.759   10.642  -17.635 1.00 14.85  ? 51  MET   A CG   1 
ATOM   793  S  SD   . MET   A 1 51  ? 3.651   12.080  -17.006 1.00 18.30  ? 51  MET   A SD   1 
ATOM   794  C  CE   . MET   A 1 51  ? 4.216   11.392  -15.396 1.00 17.88  ? 51  MET   A CE   1 
ATOM   795  H  H    . MET   A 1 51  ? 2.938   9.703   -20.240 1.00 17.70  ? 51  MET   A H    1 
ATOM   796  H  HA   . MET   A 1 51  ? 5.071   10.479  -18.911 1.00 17.32  ? 51  MET   A HA   1 
ATOM   797  H  HB2  . MET   A 1 51  ? 3.044   8.655   -18.102 1.00 18.72  ? 51  MET   A HB2  1 
ATOM   798  H  HB3  . MET   A 1 51  ? 4.151   9.216   -17.110 1.00 18.72  ? 51  MET   A HB3  1 
ATOM   799  H  HG2  . MET   A 1 51  ? 2.335   10.905  -18.467 1.00 17.82  ? 51  MET   A HG2  1 
ATOM   800  H  HG3  . MET   A 1 51  ? 2.085   10.409  -16.978 1.00 17.82  ? 51  MET   A HG3  1 
ATOM   801  H  HE1  . MET   A 1 51  ? 4.720   12.071  -14.921 1.00 21.45  ? 51  MET   A HE1  1 
ATOM   802  H  HE2  . MET   A 1 51  ? 3.441   11.130  -14.874 1.00 21.45  ? 51  MET   A HE2  1 
ATOM   803  H  HE3  . MET   A 1 51  ? 4.778   10.619  -15.562 1.00 21.45  ? 51  MET   A HE3  1 
ATOM   804  N  N    . GLY   A 1 52  ? 5.237   7.580   -20.231 1.00 16.41  ? 52  GLY   A N    1 
ATOM   805  C  CA   . GLY   A 1 52  ? 6.100   6.416   -20.421 1.00 17.71  ? 52  GLY   A CA   1 
ATOM   806  C  C    . GLY   A 1 52  ? 6.093   5.418   -19.275 1.00 15.96  ? 52  GLY   A C    1 
ATOM   807  O  O    . GLY   A 1 52  ? 7.118   4.759   -19.000 1.00 19.20  ? 52  GLY   A O    1 
ATOM   808  H  H    . GLY   A 1 52  ? 4.606   7.649   -20.811 1.00 19.69  ? 52  GLY   A H    1 
ATOM   809  H  HA2  . GLY   A 1 52  ? 5.818   5.947   -21.222 1.00 21.26  ? 52  GLY   A HA2  1 
ATOM   810  H  HA3  . GLY   A 1 52  ? 7.013   6.722   -20.540 1.00 21.26  ? 52  GLY   A HA3  1 
ATOM   811  N  N    . HIS   A 1 53  ? 4.976   5.308   -18.575 1.00 16.00  ? 53  HIS   A N    1 
ATOM   812  C  CA   . HIS   A 1 53  ? 4.755   4.409   -17.439 1.00 15.75  ? 53  HIS   A CA   1 
ATOM   813  C  C    . HIS   A 1 53  ? 5.556   4.871   -16.219 1.00 19.59  ? 53  HIS   A C    1 
ATOM   814  O  O    . HIS   A 1 53  ? 5.621   4.147   -15.238 1.00 20.47  ? 53  HIS   A O    1 
ATOM   815  C  CB   . HIS   A 1 53  ? 4.965   2.929   -17.775 1.00 18.45  ? 53  HIS   A CB   1 
ATOM   816  C  CG   . HIS   A 1 53  ? 3.993   2.489   -18.818 1.00 18.55  ? 53  HIS   A CG   1 
ATOM   817  N  ND1  . HIS   A 1 53  ? 4.356   1.645   -19.845 1.00 25.31  ? 53  HIS   A ND1  1 
ATOM   818  C  CD2  . HIS   A 1 53  ? 2.676   2.741   -18.968 1.00 17.52  ? 53  HIS   A CD2  1 
ATOM   819  C  CE1  . HIS   A 1 53  ? 3.305   1.467   -20.630 1.00 25.43  ? 53  HIS   A CE1  1 
ATOM   820  N  NE2  . HIS   A 1 53  ? 2.284   2.129   -20.131 1.00 21.76  ? 53  HIS   A NE2  1 
ATOM   821  H  H    . HIS   A 1 53  ? 4.277   5.777   -18.749 1.00 19.19  ? 53  HIS   A H    1 
ATOM   822  H  HA   . HIS   A 1 53  ? 3.820   4.439   -17.185 1.00 18.90  ? 53  HIS   A HA   1 
ATOM   823  H  HB2  . HIS   A 1 53  ? 5.864   2.797   -18.114 1.00 22.14  ? 53  HIS   A HB2  1 
ATOM   824  H  HB3  . HIS   A 1 53  ? 4.829   2.393   -16.978 1.00 22.14  ? 53  HIS   A HB3  1 
ATOM   825  H  HD1  . HIS   A 1 53  ? 5.134   1.294   -19.957 1.00 30.37  ? 53  HIS   A HD1  1 
ATOM   826  H  HD2  . HIS   A 1 53  ? 2.137   3.234   -18.393 1.00 21.03  ? 53  HIS   A HD2  1 
ATOM   827  H  HE1  . HIS   A 1 53  ? 3.290   0.956   -21.407 1.00 30.51  ? 53  HIS   A HE1  1 
ATOM   828  H  HE2  . HIS   A 1 53  ? 1.499   2.172   -20.478 1.00 26.11  ? 53  HIS   A HE2  1 
ATOM   829  N  N    . LYS   A 1 54  ? 6.107   6.078   -16.225 1.00 16.55  ? 54  LYS   A N    1 
ATOM   830  C  CA   . LYS   A 1 54  ? 6.737   6.652   -15.035 1.00 17.79  ? 54  LYS   A CA   1 
ATOM   831  C  C    . LYS   A 1 54  ? 5.719   7.480   -14.248 1.00 17.04  ? 54  LYS   A C    1 
ATOM   832  O  O    . LYS   A 1 54  ? 4.584   7.743   -14.648 1.00 15.92  ? 54  LYS   A O    1 
ATOM   833  C  CB   . LYS   A 1 54  ? 7.907   7.522   -15.501 1.00 18.98  ? 54  LYS   A CB   1 
ATOM   834  C  CG   . LYS   A 1 54  ? 8.997   6.687   -16.191 1.00 25.83  ? 54  LYS   A CG   1 
ATOM   835  C  CD   . LYS   A 1 54  ? 10.176  7.500   -16.604 1.00 32.69  ? 54  LYS   A CD   1 
ATOM   836  C  CE   . LYS   A 1 54  ? 11.194  6.603   -17.304 1.00 47.39  ? 54  LYS   A CE   1 
ATOM   837  N  NZ   . LYS   A 1 54  ? 11.954  5.788   -16.303 1.00 49.11  ? 54  LYS   A NZ   1 
ATOM   838  H  H    . LYS   A 1 54  ? 6.131   6.594   -16.912 1.00 19.86  ? 54  LYS   A H    1 
ATOM   839  H  HA   . LYS   A 1 54  ? 7.066   5.958   -14.442 1.00 21.35  ? 54  LYS   A HA   1 
ATOM   840  H  HB2  . LYS   A 1 54  ? 7.583   8.182   -16.133 1.00 22.78  ? 54  LYS   A HB2  1 
ATOM   841  H  HB3  . LYS   A 1 54  ? 8.302   7.964   -14.733 1.00 22.78  ? 54  LYS   A HB3  1 
ATOM   842  H  HG2  . LYS   A 1 54  ? 9.306   6.002   -15.578 1.00 30.99  ? 54  LYS   A HG2  1 
ATOM   843  H  HG3  . LYS   A 1 54  ? 8.623   6.276   -16.987 1.00 30.99  ? 54  LYS   A HG3  1 
ATOM   844  H  HD2  . LYS   A 1 54  ? 9.897   8.196   -17.220 1.00 39.23  ? 54  LYS   A HD2  1 
ATOM   845  H  HD3  . LYS   A 1 54  ? 10.593  7.896   -15.823 1.00 39.23  ? 54  LYS   A HD3  1 
ATOM   846  H  HE2  . LYS   A 1 54  ? 10.733  5.999   -17.907 1.00 56.86  ? 54  LYS   A HE2  1 
ATOM   847  H  HE3  . LYS   A 1 54  ? 11.823  7.150   -17.799 1.00 56.86  ? 54  LYS   A HE3  1 
ATOM   848  H  HZ1  . LYS   A 1 54  ? 12.548  5.271   -16.718 1.00 58.94  ? 54  LYS   A HZ1  1 
ATOM   849  H  HZ2  . LYS   A 1 54  ? 12.384  6.324   -15.737 1.00 58.94  ? 54  LYS   A HZ2  1 
ATOM   850  H  HZ3  . LYS   A 1 54  ? 11.395  5.271   -15.842 1.00 58.94  ? 54  LYS   A HZ3  1 
ATOM   851  N  N    . TYR   A 1 55  ? 6.174   7.904   -13.050 1.00 17.82  ? 55  TYR   A N    1 
ATOM   852  C  CA   . TYR   A 1 55  ? 5.374   8.677   -12.118 1.00 19.91  ? 55  TYR   A CA   1 
ATOM   853  C  C    . TYR   A 1 55  ? 5.720   10.159  -12.111 1.00 17.88  ? 55  TYR   A C    1 
ATOM   854  O  O    . TYR   A 1 55  ? 5.039   10.928  -11.427 1.00 18.21  ? 55  TYR   A O    1 
ATOM   855  C  CB   . TYR   A 1 55  ? 5.500   8.055   -10.704 1.00 18.96  ? 55  TYR   A CB   1 
ATOM   856  C  CG   . TYR   A 1 55  ? 4.894   6.653   -10.646 1.00 18.90  ? 55  TYR   A CG   1 
ATOM   857  C  CD1  . TYR   A 1 55  ? 3.594   6.452   -10.354 1.00 19.92  ? 55  TYR   A CD1  1 
ATOM   858  C  CD2  . TYR   A 1 55  ? 5.664   5.557   -10.963 1.00 23.26  ? 55  TYR   A CD2  1 
ATOM   859  C  CE1  . TYR   A 1 55  ? 3.020   5.139   -10.355 1.00 21.98  ? 55  TYR   A CE1  1 
ATOM   860  C  CE2  . TYR   A 1 55  ? 5.110   4.254   -10.998 1.00 23.75  ? 55  TYR   A CE2  1 
ATOM   861  C  CZ   . TYR   A 1 55  ? 3.784   4.090   -10.706 1.00 22.68  ? 55  TYR   A CZ   1 
ATOM   862  O  OH   . TYR   A 1 55  ? 3.275   2.816   -10.758 1.00 25.50  ? 55  TYR   A OH   1 
ATOM   863  H  H    . TYR   A 1 55  ? 6.968   7.745   -12.760 1.00 21.39  ? 55  TYR   A H    1 
ATOM   864  H  HA   . TYR   A 1 55  ? 4.440   8.627   -12.373 1.00 23.89  ? 55  TYR   A HA   1 
ATOM   865  H  HB2  . TYR   A 1 55  ? 6.438   7.992   -10.465 1.00 22.75  ? 55  TYR   A HB2  1 
ATOM   866  H  HB3  . TYR   A 1 55  ? 5.033   8.616   -10.066 1.00 22.75  ? 55  TYR   A HB3  1 
ATOM   867  H  HD1  . TYR   A 1 55  ? 3.057   7.182   -10.146 1.00 23.91  ? 55  TYR   A HD1  1 
ATOM   868  H  HD2  . TYR   A 1 55  ? 6.566   5.674   -11.158 1.00 27.91  ? 55  TYR   A HD2  1 
ATOM   869  H  HE1  . TYR   A 1 55  ? 2.130   5.014   -10.116 1.00 26.38  ? 55  TYR   A HE1  1 
ATOM   870  H  HE2  . TYR   A 1 55  ? 5.639   3.521   -11.216 1.00 28.50  ? 55  TYR   A HE2  1 
ATOM   871  H  HH   . TYR   A 1 55  ? 3.889   2.267   -10.924 1.00 30.60  ? 55  TYR   A HH   1 
ATOM   872  N  N    . TYR   A 1 56  ? 6.750   10.570  -12.851 1.00 18.30  ? 56  TYR   A N    1 
ATOM   873  C  CA   . TYR   A 1 56  ? 7.204   11.951  -12.917 1.00 20.19  ? 56  TYR   A CA   1 
ATOM   874  C  C    . TYR   A 1 56  ? 7.587   12.264  -14.348 1.00 19.72  ? 56  TYR   A C    1 
ATOM   875  O  O    . TYR   A 1 56  ? 7.949   11.347  -15.071 1.00 20.05  ? 56  TYR   A O    1 
ATOM   876  C  CB   . TYR   A 1 56  ? 8.456   12.194  -12.009 1.00 19.37  ? 56  TYR   A CB   1 
ATOM   877  C  CG   . TYR   A 1 56  ? 8.165   11.755  -10.586 1.00 21.23  ? 56  TYR   A CG   1 
ATOM   878  C  CD1  . TYR   A 1 56  ? 7.478   12.590  -9.773  1.00 21.32  ? 56  TYR   A CD1  1 
ATOM   879  C  CD2  . TYR   A 1 56  ? 8.613   10.542  -10.100 1.00 22.98  ? 56  TYR   A CD2  1 
ATOM   880  C  CE1  . TYR   A 1 56  ? 7.163   12.205  -8.444  1.00 21.06  ? 56  TYR   A CE1  1 
ATOM   881  C  CE2  . TYR   A 1 56  ? 8.267   10.126  -8.817  1.00 24.35  ? 56  TYR   A CE2  1 
ATOM   882  C  CZ   . TYR   A 1 56  ? 7.563   10.982  -8.014  1.00 20.67  ? 56  TYR   A CZ   1 
ATOM   883  O  OH   . TYR   A 1 56  ? 7.261   10.567  -6.724  1.00 24.46  ? 56  TYR   A OH   1 
ATOM   884  H  H    . TYR   A 1 56  ? 7.220   10.042  -13.342 1.00 21.96  ? 56  TYR   A H    1 
ATOM   885  H  HA   . TYR   A 1 56  ? 6.488   12.539  -12.631 1.00 24.23  ? 56  TYR   A HA   1 
ATOM   886  H  HB2  . TYR   A 1 56  ? 9.206   11.680  -12.346 1.00 23.25  ? 56  TYR   A HB2  1 
ATOM   887  H  HB3  . TYR   A 1 56  ? 8.676   13.139  -12.004 1.00 23.25  ? 56  TYR   A HB3  1 
ATOM   888  H  HD1  . TYR   A 1 56  ? 7.209   13.423  -10.088 1.00 25.59  ? 56  TYR   A HD1  1 
ATOM   889  H  HD2  . TYR   A 1 56  ? 9.148   10.000  -10.633 1.00 27.57  ? 56  TYR   A HD2  1 
ATOM   890  H  HE1  . TYR   A 1 56  ? 6.695   12.778  -7.880  1.00 25.27  ? 56  TYR   A HE1  1 
ATOM   891  H  HE2  . TYR   A 1 56  ? 8.510   9.281   -8.512  1.00 29.22  ? 56  TYR   A HE2  1 
ATOM   892  H  HH   . TYR   A 1 56  ? 7.595   9.810   -6.579  1.00 29.35  ? 56  TYR   A HH   1 
ATOM   893  N  N    . SER   A 1 57  ? 7.490   13.542  -14.742 1.00 18.93  ? 57  SER   A N    1 
ATOM   894  C  CA   . SER   A 1 57  ? 7.844   13.937  -16.108 1.00 19.62  ? 57  SER   A CA   1 
ATOM   895  C  C    . SER   A 1 57  ? 8.219   15.405  -16.110 1.00 19.62  ? 57  SER   A C    1 
ATOM   896  O  O    . SER   A 1 57  ? 7.695   16.182  -15.318 1.00 21.28  ? 57  SER   A O    1 
ATOM   897  C  CB   . SER   A 1 57  ? 6.615   13.720  -17.008 1.00 17.98  ? 57  SER   A CB   1 
ATOM   898  O  OG   . SER   A 1 57  ? 6.821   14.314  -18.284 1.00 21.22  ? 57  SER   A OG   1 
ATOM   899  H  H    . SER   A 1 57  ? 7.224   14.189  -14.241 1.00 22.72  ? 57  SER   A H    1 
ATOM   900  H  HA   . SER   A 1 57  ? 8.606   13.434  -16.434 1.00 23.55  ? 57  SER   A HA   1 
ATOM   901  H  HB2  . SER   A 1 57  ? 6.469   12.768  -17.121 1.00 21.58  ? 57  SER   A HB2  1 
ATOM   902  H  HB3  . SER   A 1 57  ? 5.840   14.127  -16.590 1.00 21.58  ? 57  SER   A HB3  1 
ATOM   903  H  HG   . SER   A 1 57  ? 7.524   14.012  -18.632 1.00 25.46  ? 57  SER   A HG   1 
ATOM   904  N  N    . ASN   A 1 58  ? 9.037   15.785  -17.083 1.00 19.63  ? 58  ASN   A N    1 
ATOM   905  C  CA   . ASN   A 1 58  ? 9.242   17.199  -17.361 1.00 20.83  ? 58  ASN   A CA   1 
ATOM   906  C  C    . ASN   A 1 58  ? 8.080   17.888  -18.079 1.00 20.11  ? 58  ASN   A C    1 
ATOM   907  O  O    . ASN   A 1 58  ? 8.172   19.091  -18.311 1.00 23.14  ? 58  ASN   A O    1 
ATOM   908  C  CB   . ASN   A 1 58  ? 10.529  17.421  -18.145 1.00 23.11  ? 58  ASN   A CB   1 
ATOM   909  C  CG   . ASN   A 1 58  ? 10.539  16.742  -19.495 1.00 24.16  ? 58  ASN   A CG   1 
ATOM   910  O  OD1  . ASN   A 1 58  ? 9.496   16.380  -20.048 1.00 22.99  ? 58  ASN   A OD1  1 
ATOM   911  N  ND2  . ASN   A 1 58  ? 11.745  16.539  -20.039 1.00 25.81  ? 58  ASN   A ND2  1 
ATOM   912  H  H    . ASN   A 1 58  ? 9.480   15.249  -17.589 1.00 23.55  ? 58  ASN   A H    1 
ATOM   913  H  HA   . ASN   A 1 58  ? 9.337   17.636  -16.501 1.00 25.00  ? 58  ASN   A HA   1 
ATOM   914  H  HB2  . ASN   A 1 58  ? 10.646  18.373  -18.290 1.00 27.73  ? 58  ASN   A HB2  1 
ATOM   915  H  HB3  . ASN   A 1 58  ? 11.273  17.070  -17.631 1.00 27.73  ? 58  ASN   A HB3  1 
ATOM   916  H  HD21 . ASN   A 1 58  ? 12.454  16.791  -19.622 1.00 30.97  ? 58  ASN   A HD21 1 
ATOM   917  H  HD22 . ASN   A 1 58  ? 11.812  16.157  -20.807 1.00 30.97  ? 58  ASN   A HD22 1 
ATOM   918  N  N    . ASN   A 1 59  ? 7.032   17.177  -18.471 1.00 18.77  ? 59  ASN   A N    1 
ATOM   919  C  CA   . ASN   A 1 59  ? 5.811   17.756  -19.030 1.00 18.85  ? 59  ASN   A CA   1 
ATOM   920  C  C    . ASN   A 1 59  ? 6.011   18.343  -20.437 1.00 18.59  ? 59  ASN   A C    1 
ATOM   921  O  O    . ASN   A 1 59  ? 5.126   19.036  -20.966 1.00 20.12  ? 59  ASN   A O    1 
ATOM   922  C  CB   . ASN   A 1 59  ? 5.125   18.751  -18.105 1.00 19.59  ? 59  ASN   A CB   1 
ATOM   923  C  CG   . ASN   A 1 59  ? 4.161   18.081  -17.185 1.00 21.67  ? 59  ASN   A CG   1 
ATOM   924  O  OD1  . ASN   A 1 59  ? 4.060   16.870  -17.142 1.00 22.38  ? 59  ASN   A OD1  1 
ATOM   925  N  ND2  . ASN   A 1 59  ? 3.425   18.869  -16.494 1.00 26.05  ? 59  ASN   A ND2  1 
ATOM   926  H  H    . ASN   A 1 59  ? 7.001   16.319  -18.423 1.00 22.53  ? 59  ASN   A H    1 
ATOM   927  H  HA   . ASN   A 1 59  ? 5.182   17.023  -19.123 1.00 22.62  ? 59  ASN   A HA   1 
ATOM   928  H  HB2  . ASN   A 1 59  ? 5.795   19.201  -17.567 1.00 23.51  ? 59  ASN   A HB2  1 
ATOM   929  H  HB3  . ASN   A 1 59  ? 4.637   19.398  -18.638 1.00 23.51  ? 59  ASN   A HB3  1 
ATOM   930  H  HD21 . ASN   A 1 59  ? 2.848   18.546  -15.944 1.00 31.26  ? 59  ASN   A HD21 1 
ATOM   931  H  HD22 . ASN   A 1 59  ? 3.508   19.721  -16.580 1.00 31.26  ? 59  ASN   A HD22 1 
ATOM   932  N  N    . LYS   A 1 60  ? 7.096   18.030  -21.095 1.00 18.07  ? 60  LYS   A N    1 
ATOM   933  C  CA   . LYS   A 1 60  ? 7.215   18.324  -22.501 1.00 19.07  ? 60  LYS   A CA   1 
ATOM   934  C  C    . LYS   A 1 60  ? 6.170   17.507  -23.241 1.00 19.35  ? 60  LYS   A C    1 
ATOM   935  O  O    . LYS   A 1 60  ? 5.882   16.365  -22.881 1.00 18.51  ? 60  LYS   A O    1 
ATOM   936  C  CB   . LYS   A 1 60  ? 8.632   18.004  -23.023 1.00 21.29  ? 60  LYS   A CB   1 
ATOM   937  C  CG   . LYS   A 1 60  ? 9.731   18.733  -22.308 1.00 26.76  ? 60  LYS   A CG   1 
ATOM   938  C  CD   . LYS   A 1 60  ? 11.087  18.592  -22.993 1.00 31.55  ? 60  LYS   A CD   1 
ATOM   939  C  CE   . LYS   A 1 60  ? 12.099  19.641  -22.496 1.00 40.79  ? 60  LYS   A CE   1 
ATOM   940  N  NZ   . LYS   A 1 60  ? 11.532  20.685  -21.576 1.00 57.11  ? 60  LYS   A NZ   1 
ATOM   941  H  H    . LYS   A 1 60  ? 7.784   17.645  -20.753 1.00 21.68  ? 60  LYS   A H    1 
ATOM   942  H  HA   . LYS   A 1 60  ? 7.070   19.267  -22.672 1.00 22.89  ? 60  LYS   A HA   1 
ATOM   943  H  HB2  . LYS   A 1 60  ? 8.794   17.053  -22.918 1.00 25.55  ? 60  LYS   A HB2  1 
ATOM   944  H  HB3  . LYS   A 1 60  ? 8.680   18.247  -23.960 1.00 25.55  ? 60  LYS   A HB3  1 
ATOM   945  H  HG2  . LYS   A 1 60  ? 9.511   19.677  -22.273 1.00 32.11  ? 60  LYS   A HG2  1 
ATOM   946  H  HG3  . LYS   A 1 60  ? 9.812   18.377  -21.409 1.00 32.11  ? 60  LYS   A HG3  1 
ATOM   947  H  HD2  . LYS   A 1 60  ? 11.449  17.711  -22.806 1.00 37.86  ? 60  LYS   A HD2  1 
ATOM   948  H  HD3  . LYS   A 1 60  ? 10.976  18.709  -23.949 1.00 37.86  ? 60  LYS   A HD3  1 
ATOM   949  H  HE2  . LYS   A 1 60  ? 12.805  19.182  -22.014 1.00 48.95  ? 60  LYS   A HE2  1 
ATOM   950  H  HE3  . LYS   A 1 60  ? 12.468  20.101  -23.265 1.00 48.95  ? 60  LYS   A HE3  1 
ATOM   951  H  HZ1  . LYS   A 1 60  ? 12.167  21.264  -21.345 1.00 68.54  ? 60  LYS   A HZ1  1 
ATOM   952  H  HZ2  . LYS   A 1 60  ? 10.875  21.125  -21.984 1.00 68.54  ? 60  LYS   A HZ2  1 
ATOM   953  H  HZ3  . LYS   A 1 60  ? 11.210  20.300  -20.841 1.00 68.54  ? 60  LYS   A HZ3  1 
ATOM   954  N  N    . PRO   A 1 61  ? 5.596   18.065  -24.304 1.00 18.33  ? 61  PRO   A N    1 
ATOM   955  C  CA   . PRO   A 1 61  ? 4.603   17.329  -25.084 1.00 17.31  ? 61  PRO   A CA   1 
ATOM   956  C  C    . PRO   A 1 61  ? 5.189   16.089  -25.717 1.00 16.91  ? 61  PRO   A C    1 
ATOM   957  O  O    . PRO   A 1 61  ? 6.354   16.049  -26.110 1.00 18.63  ? 61  PRO   A O    1 
ATOM   958  C  CB   . PRO   A 1 61  ? 4.181   18.368  -26.149 1.00 19.35  ? 61  PRO   A CB   1 
ATOM   959  C  CG   . PRO   A 1 61  ? 5.347   19.215  -26.294 1.00 22.62  ? 61  PRO   A CG   1 
ATOM   960  C  CD   . PRO   A 1 61  ? 5.885   19.379  -24.901 1.00 20.50  ? 61  PRO   A CD   1 
ATOM   961  H  HA   . PRO   A 1 61  ? 3.844   17.075  -24.537 1.00 20.77  ? 61  PRO   A HA   1 
ATOM   962  H  HB2  . PRO   A 1 61  ? 3.965   17.923  -26.983 1.00 23.22  ? 61  PRO   A HB2  1 
ATOM   963  H  HB3  . PRO   A 1 61  ? 3.416   18.876  -25.835 1.00 23.22  ? 61  PRO   A HB3  1 
ATOM   964  H  HG2  . PRO   A 1 61  ? 5.999   18.784  -26.868 1.00 27.15  ? 61  PRO   A HG2  1 
ATOM   965  H  HG3  . PRO   A 1 61  ? 5.089   20.071  -26.669 1.00 27.15  ? 61  PRO   A HG3  1 
ATOM   966  H  HD2  . PRO   A 1 61  ? 6.839   19.557  -24.912 1.00 24.60  ? 61  PRO   A HD2  1 
ATOM   967  H  HD3  . PRO   A 1 61  ? 5.422   20.088  -24.428 1.00 24.60  ? 61  PRO   A HD3  1 
ATOM   968  N  N    . MET   A 1 62  ? 4.335   15.087  -25.878 1.00 16.53  ? 62  MET   A N    1 
ATOM   969  C  CA   . MET   A 1 62  ? 4.725   13.878  -26.603 1.00 15.62  ? 62  MET   A CA   1 
ATOM   970  C  C    . MET   A 1 62  ? 5.161   14.380  -28.014 1.00 19.55  ? 62  MET   A C    1 
ATOM   971  O  O    . MET   A 1 62  ? 4.475   15.181  -28.670 1.00 16.84  ? 62  MET   A O    1 
ATOM   972  C  CB   . MET   A 1 62  ? 3.420   13.059  -26.871 1.00 15.53  ? 62  MET   A CB   1 
ATOM   973  C  CG   . MET   A 1 62  ? 3.676   11.846  -27.695 1.00 16.14  ? 62  MET   A CG   1 
ATOM   974  S  SD   . MET   A 1 62  ? 2.268   10.720  -27.542 1.00 17.88  ? 62  MET   A SD   1 
ATOM   975  C  CE   . MET   A 1 62  ? 2.668   9.449   -28.679 1.00 22.52  ? 62  MET   A CE   1 
ATOM   976  H  H    . MET   A 1 62  ? 3.528   15.078  -25.581 1.00 19.83  ? 62  MET   A H    1 
ATOM   977  H  HA   . MET   A 1 62  ? 5.390   13.355  -26.128 1.00 18.74  ? 62  MET   A HA   1 
ATOM   978  H  HB2  . MET   A 1 62  ? 3.044   12.775  -26.023 1.00 18.63  ? 62  MET   A HB2  1 
ATOM   979  H  HB3  . MET   A 1 62  ? 2.786   13.619  -27.345 1.00 18.63  ? 62  MET   A HB3  1 
ATOM   980  H  HG2  . MET   A 1 62  ? 3.780   12.095  -28.627 1.00 19.37  ? 62  MET   A HG2  1 
ATOM   981  H  HG3  . MET   A 1 62  ? 4.476   11.395  -27.381 1.00 19.37  ? 62  MET   A HG3  1 
ATOM   982  H  HE1  . MET   A 1 62  ? 1.995   8.753   -28.625 1.00 27.02  ? 62  MET   A HE1  1 
ATOM   983  H  HE2  . MET   A 1 62  ? 2.689   9.821   -29.575 1.00 27.02  ? 62  MET   A HE2  1 
ATOM   984  H  HE3  . MET   A 1 62  ? 3.538   9.085   -28.452 1.00 27.02  ? 62  MET   A HE3  1 
ATOM   985  N  N    . GLN   A 1 63  ? 6.243   13.857  -28.505 1.00 17.02  ? 63  GLN   A N    1 
ATOM   986  C  CA   . GLN   A 1 63  ? 6.841   14.303  -29.765 1.00 17.85  ? 63  GLN   A CA   1 
ATOM   987  C  C    . GLN   A 1 63  ? 7.166   13.083  -30.611 1.00 19.03  ? 63  GLN   A C    1 
ATOM   988  O  O    . GLN   A 1 63  ? 7.603   12.048  -30.094 1.00 21.04  ? 63  GLN   A O    1 
ATOM   989  C  CB   . GLN   A 1 63  ? 8.110   15.176  -29.485 1.00 23.49  ? 63  GLN   A CB   1 
ATOM   990  C  CG   . GLN   A 1 63  ? 9.262   14.443  -28.855 1.00 27.67  ? 63  GLN   A CG   1 
ATOM   991  C  CD   . GLN   A 1 63  ? 10.495  15.331  -28.749 1.00 35.00  ? 63  GLN   A CD   1 
ATOM   992  O  OE1  . GLN   A 1 63  ? 10.385  16.506  -28.394 1.00 32.38  ? 63  GLN   A OE1  1 
ATOM   993  N  NE2  . GLN   A 1 63  ? 11.665  14.787  -29.085 1.00 42.98  ? 63  GLN   A NE2  1 
ATOM   994  H  H    . GLN   A 1 63  ? 6.679   13.219  -28.127 1.00 20.43  ? 63  GLN   A H    1 
ATOM   995  H  HA   . GLN   A 1 63  ? 6.223   14.847  -30.277 1.00 21.42  ? 63  GLN   A HA   1 
ATOM   996  H  HB2  . GLN   A 1 63  ? 8.424   15.540  -30.328 1.00 28.18  ? 63  GLN   A HB2  1 
ATOM   997  H  HB3  . GLN   A 1 63  ? 7.861   15.896  -28.885 1.00 28.18  ? 63  GLN   A HB3  1 
ATOM   998  H  HG2  . GLN   A 1 63  ? 9.012   14.160  -27.962 1.00 33.21  ? 63  GLN   A HG2  1 
ATOM   999  H  HG3  . GLN   A 1 63  ? 9.487   13.672  -29.398 1.00 33.21  ? 63  GLN   A HG3  1 
ATOM   1000 H  HE21 . GLN   A 1 63  ? 11.699  13.968  -29.348 1.00 51.57  ? 63  GLN   A HE21 1 
ATOM   1001 H  HE22 . GLN   A 1 63  ? 12.386  15.254  -29.039 1.00 51.57  ? 63  GLN   A HE22 1 
ATOM   1002 N  N    . PHE   A 1 64  ? 6.981   13.225  -31.918 1.00 18.72  ? 64  PHE   A N    1 
ATOM   1003 C  CA   . PHE   A 1 64  ? 7.139   12.088  -32.820 1.00 21.62  ? 64  PHE   A CA   1 
ATOM   1004 C  C    . PHE   A 1 64  ? 7.612   12.586  -34.172 1.00 21.71  ? 64  PHE   A C    1 
ATOM   1005 O  O    . PHE   A 1 64  ? 7.291   13.692  -34.571 1.00 23.29  ? 64  PHE   A O    1 
ATOM   1006 C  CB   . PHE   A 1 64  ? 5.817   11.286  -32.911 1.00 20.98  ? 64  PHE   A CB   1 
ATOM   1007 C  CG   . PHE   A 1 64  ? 4.601   12.086  -33.358 1.00 19.22  ? 64  PHE   A CG   1 
ATOM   1008 C  CD1  . PHE   A 1 64  ? 3.960   12.943  -32.491 1.00 19.66  ? 64  PHE   A CD1  1 
ATOM   1009 C  CD2  . PHE   A 1 64  ? 4.055   11.952  -34.639 1.00 21.95  ? 64  PHE   A CD2  1 
ATOM   1010 C  CE1  . PHE   A 1 64  ? 2.832   13.656  -32.898 1.00 22.31  ? 64  PHE   A CE1  1 
ATOM   1011 C  CE2  . PHE   A 1 64  ? 2.955   12.668  -35.034 1.00 23.66  ? 64  PHE   A CE2  1 
ATOM   1012 C  CZ   . PHE   A 1 64  ? 2.337   13.529  -34.139 1.00 23.19  ? 64  PHE   A CZ   1 
ATOM   1013 H  H    . PHE   A 1 64  ? 6.766   13.962  -32.304 1.00 22.46  ? 64  PHE   A H    1 
ATOM   1014 H  HA   . PHE   A 1 64  ? 7.827   11.483  -32.501 1.00 25.95  ? 64  PHE   A HA   1 
ATOM   1015 H  HB2  . PHE   A 1 64  ? 5.940   10.566  -33.549 1.00 25.18  ? 64  PHE   A HB2  1 
ATOM   1016 H  HB3  . PHE   A 1 64  ? 5.619   10.923  -32.034 1.00 25.18  ? 64  PHE   A HB3  1 
ATOM   1017 H  HD1  . PHE   A 1 64  ? 4.283   13.048  -31.625 1.00 23.59  ? 64  PHE   A HD1  1 
ATOM   1018 H  HD2  . PHE   A 1 64  ? 4.450   11.362  -35.240 1.00 26.34  ? 64  PHE   A HD2  1 
ATOM   1019 H  HE1  . PHE   A 1 64  ? 2.415   14.231  -32.298 1.00 26.77  ? 64  PHE   A HE1  1 
ATOM   1020 H  HE2  . PHE   A 1 64  ? 2.623   12.576  -35.898 1.00 28.39  ? 64  PHE   A HE2  1 
ATOM   1021 H  HZ   . PHE   A 1 64  ? 1.587   14.015  -34.397 1.00 27.83  ? 64  PHE   A HZ   1 
ATOM   1022 N  N    . THR   A 1 65  ? 8.361   11.746  -34.853 1.00 22.29  ? 65  THR   A N    1 
ATOM   1023 C  CA   . THR   A 1 65  ? 8.801   12.090  -36.210 1.00 23.61  ? 65  THR   A CA   1 
ATOM   1024 C  C    . THR   A 1 65  ? 7.599   12.240  -37.128 1.00 24.61  ? 65  THR   A C    1 
ATOM   1025 O  O    . THR   A 1 65  ? 6.651   11.448  -37.102 1.00 25.38  ? 65  THR   A O    1 
ATOM   1026 C  CB   . THR   A 1 65  ? 9.681   10.970  -36.707 1.00 23.03  ? 65  THR   A CB   1 
ATOM   1027 O  OG1  . THR   A 1 65  ? 10.900  10.967  -35.949 1.00 28.30  ? 65  THR   A OG1  1 
ATOM   1028 C  CG2  . THR   A 1 65  ? 10.023  11.162  -38.200 1.00 30.33  ? 65  THR   A CG2  1 
ATOM   1029 H  H    . THR   A 1 65  ? 8.630   10.981  -34.568 1.00 26.75  ? 65  THR   A H    1 
ATOM   1030 H  HA   . THR   A 1 65  ? 9.291   12.927  -36.211 1.00 28.33  ? 65  THR   A HA   1 
ATOM   1031 H  HB   . THR   A 1 65  ? 9.218   10.123  -36.607 1.00 27.64  ? 65  THR   A HB   1 
ATOM   1032 H  HG1  . THR   A 1 65  ? 11.212  11.745  -35.904 1.00 33.96  ? 65  THR   A HG1  1 
ATOM   1033 H  HG21 . THR   A 1 65  ? 10.753  10.576  -38.451 1.00 36.40  ? 65  THR   A HG21 1 
ATOM   1034 H  HG22 . THR   A 1 65  ? 9.249   10.953  -38.747 1.00 36.40  ? 65  THR   A HG22 1 
ATOM   1035 H  HG23 . THR   A 1 65  ? 10.286  12.081  -38.365 1.00 36.40  ? 65  THR   A HG23 1 
ATOM   1036 N  N    . CYS   A 1 66  ? 7.599   13.292  -37.943 1.00 28.71  ? 66  CYS   A N    1 
ATOM   1037 C  CA   . CYS   A 1 66  ? 6.499   13.482  -38.883 1.00 25.69  ? 66  CYS   A CA   1 
ATOM   1038 C  C    . CYS   A 1 66  ? 7.111   13.994  -40.172 1.00 36.42  ? 66  CYS   A C    1 
ATOM   1039 O  O    . CYS   A 1 66  ? 7.728   15.065  -40.168 1.00 31.82  ? 66  CYS   A O    1 
ATOM   1040 C  CB   . CYS   A 1 66  ? 5.399   14.414  -38.463 1.00 27.98  ? 66  CYS   A CB   1 
ATOM   1041 S  SG   . CYS   A 1 66  ? 5.855   15.994  -37.847 1.00 32.53  ? 66  CYS   A SG   1 
ATOM   1042 H  H    . CYS   A 1 66  ? 8.211   13.896  -37.969 1.00 34.45  ? 66  CYS   A H    1 
ATOM   1043 H  HA   . CYS   A 1 66  ? 6.071   12.616  -38.982 1.00 30.83  ? 66  CYS   A HA   1 
ATOM   1044 H  HB2  . CYS   A 1 66  ? 4.832   14.569  -39.235 1.00 33.58  ? 66  CYS   A HB2  1 
ATOM   1045 H  HB3  . CYS   A 1 66  ? 4.892   13.977  -37.761 1.00 33.58  ? 66  CYS   A HB3  1 
ATOM   1046 N  N    . LYS   A 1 67  ? 6.951   13.221  -41.241 1.00 34.28  ? 67  LYS   A N    1 
ATOM   1047 C  CA   . LYS   A 1 67  ? 7.584   13.442  -42.538 1.00 41.65  ? 67  LYS   A CA   1 
ATOM   1048 C  C    . LYS   A 1 67  ? 6.534   13.280  -43.616 1.00 28.54  ? 67  LYS   A C    1 
ATOM   1049 O  O    . LYS   A 1 67  ? 5.482   12.680  -43.419 1.00 30.07  ? 67  LYS   A O    1 
ATOM   1050 C  CB   . LYS   A 1 67  ? 8.694   12.415  -42.781 1.00 559.13 ? 67  LYS   A CB   1 
ATOM   1051 C  CG   . LYS   A 1 67  ? 9.903   12.676  -41.905 1.00 51.88  ? 67  LYS   A CG   1 
ATOM   1052 C  CD   . LYS   A 1 67  ? 11.144  11.996  -42.399 1.00 52.60  ? 67  LYS   A CD   1 
ATOM   1053 C  CE   . LYS   A 1 67  ? 11.167  10.538  -42.011 1.00 50.48  ? 67  LYS   A CE   1 
ATOM   1054 N  NZ   . LYS   A 1 67  ? 12.518  9.937   -42.223 1.00 57.01  ? 67  LYS   A NZ   1 
ATOM   1055 H  H    . LYS   A 1 67  ? 6.453   12.520  -41.240 1.00 41.14  ? 67  LYS   A H    1 
ATOM   1056 H  HA   . LYS   A 1 67  ? 7.958   14.336  -42.579 1.00 49.98  ? 67  LYS   A HA   1 
ATOM   1057 H  HB2  . LYS   A 1 67  ? 8.358   11.528  -42.580 1.00 670.96 ? 67  LYS   A HB2  1 
ATOM   1058 H  HB3  . LYS   A 1 67  ? 8.974   12.461  -43.709 1.00 670.96 ? 67  LYS   A HB3  1 
ATOM   1059 H  HG2  . LYS   A 1 67  ? 10.075  13.631  -41.881 1.00 62.26  ? 67  LYS   A HG2  1 
ATOM   1060 H  HG3  . LYS   A 1 67  ? 9.720   12.350  -41.010 1.00 62.26  ? 67  LYS   A HG3  1 
ATOM   1061 H  HD2  . LYS   A 1 67  ? 11.179  12.054  -43.367 1.00 63.12  ? 67  LYS   A HD2  1 
ATOM   1062 H  HD3  . LYS   A 1 67  ? 11.923  12.426  -42.013 1.00 63.12  ? 67  LYS   A HD3  1 
ATOM   1063 H  HE2  . LYS   A 1 67  ? 10.939  10.452  -41.072 1.00 60.57  ? 67  LYS   A HE2  1 
ATOM   1064 H  HE3  . LYS   A 1 67  ? 10.527  10.050  -42.553 1.00 60.57  ? 67  LYS   A HE3  1 
ATOM   1065 H  HZ1  . LYS   A 1 67  ? 12.510  9.078   -41.987 1.00 68.41  ? 67  LYS   A HZ1  1 
ATOM   1066 H  HZ2  . LYS   A 1 67  ? 12.747  9.998   -43.081 1.00 68.41  ? 67  LYS   A HZ2  1 
ATOM   1067 H  HZ3  . LYS   A 1 67  ? 13.123  10.366  -41.732 1.00 68.41  ? 67  LYS   A HZ3  1 
ATOM   1068 N  N    . GLU   A 1 68  ? 6.831   13.914  -44.744 1.00 28.15  ? 68  GLU   A N    1 
ATOM   1069 C  CA   . GLU   A 1 68  ? 6.023   13.737  -45.934 1.00 33.69  ? 68  GLU   A CA   1 
ATOM   1070 C  C    . GLU   A 1 68  ? 6.126   12.293  -46.417 1.00 29.08  ? 68  GLU   A C    1 
ATOM   1071 O  O    . GLU   A 1 68  ? 7.178   11.664  -46.310 1.00 29.16  ? 68  GLU   A O    1 
ATOM   1072 C  CB   . GLU   A 1 68  ? 6.587   14.625  -47.063 1.00 34.56  ? 68  GLU   A CB   1 
ATOM   1073 C  CG   . GLU   A 1 68  ? 6.501   16.118  -46.810 1.00 41.48  ? 68  GLU   A CG   1 
ATOM   1074 C  CD   . GLU   A 1 68  ? 5.118   16.687  -47.087 1.00 41.42  ? 68  GLU   A CD   1 
ATOM   1075 O  OE1  . GLU   A 1 68  ? 4.745   16.878  -48.279 1.00 43.22  ? 68  GLU   A OE1  1 
ATOM   1076 O  OE2  . GLU   A 1 68  ? 4.408   16.929  -46.090 1.00 47.72  ? 68  GLU   A OE2  1 
ATOM   1077 H  H    . GLU   A 1 68  ? 7.496   14.450  -44.843 1.00 33.78  ? 68  GLU   A H    1 
ATOM   1078 H  HA   . GLU   A 1 68  ? 5.100   13.968  -45.741 1.00 40.43  ? 68  GLU   A HA   1 
ATOM   1079 H  HB2  . GLU   A 1 68  ? 7.523   14.404  -47.188 1.00 41.47  ? 68  GLU   A HB2  1 
ATOM   1080 H  HB3  . GLU   A 1 68  ? 6.091   14.439  -47.876 1.00 41.47  ? 68  GLU   A HB3  1 
ATOM   1081 H  HG2  . GLU   A 1 68  ? 6.716   16.294  -45.880 1.00 49.78  ? 68  GLU   A HG2  1 
ATOM   1082 H  HG3  . GLU   A 1 68  ? 7.133   16.573  -47.388 1.00 49.78  ? 68  GLU   A HG3  1 
ATOM   1083 N  N    . THR   A 1 69  ? 5.049   11.825  -47.048 1.00 26.74  ? 69  THR   A N    1 
ATOM   1084 C  CA   . THR   A 1 69  ? 4.927   10.471  -47.557 1.00 27.58  ? 69  THR   A CA   1 
ATOM   1085 C  C    . THR   A 1 69  ? 4.269   10.495  -48.920 1.00 31.61  ? 69  THR   A C    1 
ATOM   1086 O  O    . THR   A 1 69  ? 3.689   11.510  -49.317 1.00 34.56  ? 69  THR   A O    1 
ATOM   1087 C  CB   . THR   A 1 69  ? 4.096   9.607   -46.588 1.00 34.97  ? 69  THR   A CB   1 
ATOM   1088 O  OG1  . THR   A 1 69  ? 2.725   10.067  -46.586 1.00 37.24  ? 69  THR   A OG1  1 
ATOM   1089 C  CG2  . THR   A 1 69  ? 4.686   9.649   -45.179 1.00 37.74  ? 69  THR   A CG2  1 
ATOM   1090 H  H    . THR   A 1 69  ? 4.347   12.299  -47.196 1.00 32.09  ? 69  THR   A H    1 
ATOM   1091 H  HA   . THR   A 1 69  ? 5.807   10.078  -47.667 1.00 33.10  ? 69  THR   A HA   1 
ATOM   1092 H  HB   . THR   A 1 69  ? 4.112   8.681   -46.877 1.00 41.96  ? 69  THR   A HB   1 
ATOM   1093 H  HG1  . THR   A 1 69  ? 2.273   9.620   -46.037 1.00 44.69  ? 69  THR   A HG1  1 
ATOM   1094 H  HG21 . THR   A 1 69  ? 4.177   9.071   -44.589 1.00 45.29  ? 69  THR   A HG21 1 
ATOM   1095 H  HG22 . THR   A 1 69  ? 5.608   9.348   -45.196 1.00 45.29  ? 69  THR   A HG22 1 
ATOM   1096 H  HG23 . THR   A 1 69  ? 4.657   10.555  -44.834 1.00 45.29  ? 69  THR   A HG23 1 
ATOM   1097 N  N    . PRO   A 1 70  ? 4.372   9.408   -49.674 1.00 32.41  ? 70  PRO   A N    1 
ATOM   1098 C  CA   . PRO   A 1 70  ? 3.731   9.370   -50.996 1.00 36.00  ? 70  PRO   A CA   1 
ATOM   1099 C  C    . PRO   A 1 70  ? 2.215   9.498   -50.889 1.00 39.52  ? 70  PRO   A C    1 
ATOM   1100 O  O    . PRO   A 1 70  ? 1.587   8.996   -49.954 1.00 45.95  ? 70  PRO   A O    1 
ATOM   1101 C  CB   . PRO   A 1 70  ? 4.168   8.011   -51.549 1.00 39.50  ? 70  PRO   A CB   1 
ATOM   1102 C  CG   . PRO   A 1 70  ? 5.459   7.720   -50.791 1.00 41.30  ? 70  PRO   A CG   1 
ATOM   1103 C  CD   . PRO   A 1 70  ? 5.175   8.198   -49.428 1.00 35.71  ? 70  PRO   A CD   1 
ATOM   1104 H  HA   . PRO   A 1 70  ? 4.066   10.077  -51.569 1.00 43.20  ? 70  PRO   A HA   1 
ATOM   1105 H  HB2  . PRO   A 1 70  ? 3.492   7.340   -51.365 1.00 47.39  ? 70  PRO   A HB2  1 
ATOM   1106 H  HB3  . PRO   A 1 70  ? 4.325   8.071   -52.504 1.00 47.39  ? 70  PRO   A HB3  1 
ATOM   1107 H  HG2  . PRO   A 1 70  ? 5.646   6.769   -50.799 1.00 49.56  ? 70  PRO   A HG2  1 
ATOM   1108 H  HG3  . PRO   A 1 70  ? 6.198   8.207   -51.188 1.00 49.56  ? 70  PRO   A HG3  1 
ATOM   1109 H  HD2  . PRO   A 1 70  ? 4.668   7.540   -48.927 1.00 42.85  ? 70  PRO   A HD2  1 
ATOM   1110 H  HD3  . PRO   A 1 70  ? 5.995   8.414   -48.957 1.00 42.85  ? 70  PRO   A HD3  1 
ATOM   1111 N  N    . ASP   A 1 71  ? 1.622   10.195  -51.851 1.00 52.03  ? 71  ASP   A N    1 
ATOM   1112 C  CA   . ASP   A 1 71  ? 0.171   10.449  -51.806 1.00 52.19  ? 71  ASP   A CA   1 
ATOM   1113 C  C    . ASP   A 1 71  ? -0.650  9.384   -52.557 1.00 46.35  ? 71  ASP   A C    1 
ATOM   1114 O  O    . ASP   A 1 71  ? -0.105  8.430   -53.131 1.00 49.92  ? 71  ASP   A O    1 
ATOM   1115 C  CB   . ASP   A 1 71  ? -0.122  11.889  -52.302 1.00 45.47  ? 71  ASP   A CB   1 
ATOM   1116 C  CG   . ASP   A 1 71  ? 0.124   12.042  -53.789 1.00 40.40  ? 71  ASP   A CG   1 
ATOM   1117 O  OD1  . ASP   A 1 71  ? 0.444   11.018  -54.429 1.00 53.64  ? 71  ASP   A OD1  1 
ATOM   1118 O  OD2  . ASP   A 1 71  ? 0.036   13.180  -54.323 1.00 42.09  ? 71  ASP   A OD2  1 
ATOM   1119 H  H    . ASP   A 1 71  ? 2.025   10.529  -52.534 1.00 62.44  ? 71  ASP   A H    1 
ATOM   1120 H  HA   . ASP   A 1 71  ? -0.135  10.388  -50.888 1.00 62.63  ? 71  ASP   A HA   1 
ATOM   1121 H  HB2  . ASP   A 1 71  ? -1.052  12.103  -52.126 1.00 54.57  ? 71  ASP   A HB2  1 
ATOM   1122 H  HB3  . ASP   A 1 71  ? 0.456   12.511  -51.834 1.00 54.57  ? 71  ASP   A HB3  1 
ATOM   1123 N  N    . THR   A 1 75  ? -2.472  23.817  -43.888 1.00 45.47  ? 75  THR   A N    1 
ATOM   1124 C  CA   . THR   A 1 75  ? -1.740  22.923  -42.998 1.00 46.08  ? 75  THR   A CA   1 
ATOM   1125 C  C    . THR   A 1 75  ? -1.567  21.547  -43.643 1.00 47.18  ? 75  THR   A C    1 
ATOM   1126 O  O    . THR   A 1 75  ? -2.277  21.179  -44.572 1.00 48.67  ? 75  THR   A O    1 
ATOM   1127 C  CB   . THR   A 1 75  ? -2.437  22.731  -41.609 1.00 65.20  ? 75  THR   A CB   1 
ATOM   1128 O  OG1  . THR   A 1 75  ? -3.780  22.254  -41.787 1.00 69.78  ? 75  THR   A OG1  1 
ATOM   1129 C  CG2  . THR   A 1 75  ? -2.445  24.042  -40.808 1.00 57.85  ? 75  THR   A CG2  1 
ATOM   1130 H  HA   . THR   A 1 75  ? -0.868  23.315  -42.832 1.00 55.30  ? 75  THR   A HA   1 
ATOM   1131 H  HB   . THR   A 1 75  ? -1.939  22.075  -41.096 1.00 78.24  ? 75  THR   A HB   1 
ATOM   1132 H  HG1  . THR   A 1 75  ? -4.202  22.770  -42.298 1.00 83.73  ? 75  THR   A HG1  1 
ATOM   1133 H  HG21 . THR   A 1 75  ? -2.872  23.903  -39.948 1.00 69.42  ? 75  THR   A HG21 1 
ATOM   1134 H  HG22 . THR   A 1 75  ? -1.536  24.348  -40.663 1.00 69.42  ? 75  THR   A HG22 1 
ATOM   1135 H  HG23 . THR   A 1 75  ? -2.933  24.725  -41.295 1.00 69.42  ? 75  THR   A HG23 1 
ATOM   1136 N  N    . LYS   A 1 76  ? -0.604  20.794  -43.133 1.00 33.11  ? 76  LYS   A N    1 
ATOM   1137 C  CA   . LYS   A 1 76  ? -0.308  19.439  -43.585 1.00 30.72  ? 76  LYS   A CA   1 
ATOM   1138 C  C    . LYS   A 1 76  ? -0.807  18.472  -42.504 1.00 31.23  ? 76  LYS   A C    1 
ATOM   1139 O  O    . LYS   A 1 76  ? -0.972  18.831  -41.313 1.00 27.92  ? 76  LYS   A O    1 
ATOM   1140 C  CB   . LYS   A 1 76  ? 1.198   19.290  -43.804 1.00 32.28  ? 76  LYS   A CB   1 
ATOM   1141 C  CG   . LYS   A 1 76  ? 1.737   20.292  -44.806 1.00 31.67  ? 76  LYS   A CG   1 
ATOM   1142 C  CD   . LYS   A 1 76  ? 2.953   19.756  -45.541 1.00 29.38  ? 76  LYS   A CD   1 
ATOM   1143 C  CE   . LYS   A 1 76  ? 3.303   20.662  -46.713 1.00 33.46  ? 76  LYS   A CE   1 
ATOM   1144 N  NZ   . LYS   A 1 76  ? 4.569   20.270  -47.210 1.00 29.48  ? 76  LYS   A NZ   1 
ATOM   1145 H  H    . LYS   A 1 76  ? -0.086  21.055  -42.498 1.00 39.73  ? 76  LYS   A H    1 
ATOM   1146 H  HA   . LYS   A 1 76  ? -0.746  19.225  -44.424 1.00 36.86  ? 76  LYS   A HA   1 
ATOM   1147 H  HB2  . LYS   A 1 76  ? 1.656   19.429  -42.961 1.00 38.73  ? 76  LYS   A HB2  1 
ATOM   1148 H  HB3  . LYS   A 1 76  ? 1.383   18.399  -44.139 1.00 38.73  ? 76  LYS   A HB3  1 
ATOM   1149 H  HG2  . LYS   A 1 76  ? 1.050   20.491  -45.461 1.00 38.00  ? 76  LYS   A HG2  1 
ATOM   1150 H  HG3  . LYS   A 1 76  ? 1.996   21.102  -44.340 1.00 38.00  ? 76  LYS   A HG3  1 
ATOM   1151 H  HD2  . LYS   A 1 76  ? 3.712   19.724  -44.937 1.00 35.26  ? 76  LYS   A HD2  1 
ATOM   1152 H  HD3  . LYS   A 1 76  ? 2.763   18.868  -45.882 1.00 35.26  ? 76  LYS   A HD3  1 
ATOM   1153 H  HE2  . LYS   A 1 76  ? 2.641   20.568  -47.416 1.00 40.15  ? 76  LYS   A HE2  1 
ATOM   1154 H  HE3  . LYS   A 1 76  ? 3.347   21.585  -46.419 1.00 40.15  ? 76  LYS   A HE3  1 
ATOM   1155 H  HZ1  . LYS   A 1 76  ? 4.801   20.789  -47.895 1.00 35.38  ? 76  LYS   A HZ1  1 
ATOM   1156 H  HZ2  . LYS   A 1 76  ? 5.183   20.344  -46.571 1.00 35.38  ? 76  LYS   A HZ2  1 
ATOM   1157 H  HZ3  . LYS   A 1 76  ? 4.539   19.424  -47.486 1.00 35.38  ? 76  LYS   A HZ3  1 
ATOM   1158 N  N    . THR   A 1 77  ? -1.076  17.246  -42.943 1.00 27.63  ? 77  THR   A N    1 
ATOM   1159 C  CA   . THR   A 1 77  ? -1.558  16.161  -42.074 1.00 26.67  ? 77  THR   A CA   1 
ATOM   1160 C  C    . THR   A 1 77  ? -0.514  15.065  -41.967 1.00 28.56  ? 77  THR   A C    1 
ATOM   1161 O  O    . THR   A 1 77  ? 0.133   14.675  -42.942 1.00 32.73  ? 77  THR   A O    1 
ATOM   1162 C  CB   . THR   A 1 77  ? -2.869  15.558  -42.650 1.00 28.95  ? 77  THR   A CB   1 
ATOM   1163 O  OG1  . THR   A 1 77  ? -3.903  16.561  -42.730 1.00 34.18  ? 77  THR   A OG1  1 
ATOM   1164 C  CG2  . THR   A 1 77  ? -3.413  14.418  -41.806 1.00 31.22  ? 77  THR   A CG2  1 
ATOM   1165 H  H    . THR   A 1 77  ? -0.985  17.005  -43.764 1.00 33.16  ? 77  THR   A H    1 
ATOM   1166 H  HA   . THR   A 1 77  ? -1.723  16.510  -41.184 1.00 32.00  ? 77  THR   A HA   1 
ATOM   1167 H  HB   . THR   A 1 77  ? -2.650  15.217  -43.531 1.00 34.74  ? 77  THR   A HB   1 
ATOM   1168 H  HG1  . THR   A 1 77  ? -4.198  16.732  -41.963 1.00 41.02  ? 77  THR   A HG1  1 
ATOM   1169 H  HG21 . THR   A 1 77  ? -4.282  14.144  -42.139 1.00 37.47  ? 77  THR   A HG21 1 
ATOM   1170 H  HG22 . THR   A 1 77  ? -2.808  13.661  -41.842 1.00 37.47  ? 77  THR   A HG22 1 
ATOM   1171 H  HG23 . THR   A 1 77  ? -3.506  14.704  -40.883 1.00 37.47  ? 77  THR   A HG23 1 
ATOM   1172 N  N    . TYR   A 1 78  ? -0.397  14.521  -40.764 1.00 25.52  ? 78  TYR   A N    1 
ATOM   1173 C  CA   . TYR   A 1 78  ? 0.568   13.465  -40.496 1.00 22.47  ? 78  TYR   A CA   1 
ATOM   1174 C  C    . TYR   A 1 78  ? -0.113  12.375  -39.661 1.00 22.87  ? 78  TYR   A C    1 
ATOM   1175 O  O    . TYR   A 1 78  ? -1.004  12.650  -38.842 1.00 23.43  ? 78  TYR   A O    1 
ATOM   1176 C  CB   . TYR   A 1 78  ? 1.827   13.985  -39.746 1.00 23.66  ? 78  TYR   A CB   1 
ATOM   1177 C  CG   . TYR   A 1 78  ? 2.480   15.181  -40.455 1.00 25.11  ? 78  TYR   A CG   1 
ATOM   1178 C  CD1  . TYR   A 1 78  ? 2.016   16.452  -40.234 1.00 27.76  ? 78  TYR   A CD1  1 
ATOM   1179 C  CD2  . TYR   A 1 78  ? 3.549   15.012  -41.348 1.00 25.98  ? 78  TYR   A CD2  1 
ATOM   1180 C  CE1  . TYR   A 1 78  ? 2.589   17.556  -40.898 1.00 31.56  ? 78  TYR   A CE1  1 
ATOM   1181 C  CE2  . TYR   A 1 78  ? 4.129   16.107  -42.031 1.00 26.71  ? 78  TYR   A CE2  1 
ATOM   1182 C  CZ   . TYR   A 1 78  ? 3.646   17.366  -41.775 1.00 29.70  ? 78  TYR   A CZ   1 
ATOM   1183 O  OH   . TYR   A 1 78  ? 4.178   18.500  -42.414 1.00 32.54  ? 78  TYR   A OH   1 
ATOM   1184 H  H    . TYR   A 1 78  ? -0.869  14.748  -40.082 1.00 30.62  ? 78  TYR   A H    1 
ATOM   1185 H  HA   . TYR   A 1 78  ? 0.865   13.083  -41.337 1.00 26.96  ? 78  TYR   A HA   1 
ATOM   1186 H  HB2  . TYR   A 1 78  ? 1.570   14.266  -38.853 1.00 28.39  ? 78  TYR   A HB2  1 
ATOM   1187 H  HB3  . TYR   A 1 78  ? 2.482   13.271  -39.693 1.00 28.39  ? 78  TYR   A HB3  1 
ATOM   1188 H  HD1  . TYR   A 1 78  ? 1.315   16.587  -39.639 1.00 33.32  ? 78  TYR   A HD1  1 
ATOM   1189 H  HD2  . TYR   A 1 78  ? 3.885   14.158  -41.496 1.00 31.18  ? 78  TYR   A HD2  1 
ATOM   1190 H  HE1  . TYR   A 1 78  ? 2.257   18.412  -40.748 1.00 37.87  ? 78  TYR   A HE1  1 
ATOM   1191 H  HE2  . TYR   A 1 78  ? 4.821   15.977  -42.638 1.00 32.05  ? 78  TYR   A HE2  1 
ATOM   1192 H  HH   . TYR   A 1 78  ? 4.894   18.300  -42.805 1.00 39.05  ? 78  TYR   A HH   1 
ATOM   1193 N  N    . TYR   A 1 79  ? 0.375   11.139  -39.839 1.00 21.96  ? 79  TYR   A N    1 
ATOM   1194 C  CA   . TYR   A 1 79  ? -0.099  10.078  -38.929 1.00 20.26  ? 79  TYR   A CA   1 
ATOM   1195 C  C    . TYR   A 1 79  ? 0.572   10.168  -37.572 1.00 20.31  ? 79  TYR   A C    1 
ATOM   1196 O  O    . TYR   A 1 79  ? 1.755   10.459  -37.477 1.00 20.86  ? 79  TYR   A O    1 
ATOM   1197 C  CB   . TYR   A 1 79  ? 0.214   8.689   -39.483 1.00 22.95  ? 79  TYR   A CB   1 
ATOM   1198 C  CG   . TYR   A 1 79  ? -0.875  8.184   -40.408 1.00 24.82  ? 79  TYR   A CG   1 
ATOM   1199 C  CD1  . TYR   A 1 79  ? -0.812  8.476   -41.766 1.00 33.66  ? 79  TYR   A CD1  1 
ATOM   1200 C  CD2  . TYR   A 1 79  ? -1.957  7.465   -39.952 1.00 28.48  ? 79  TYR   A CD2  1 
ATOM   1201 C  CE1  . TYR   A 1 79  ? -1.795  8.045   -42.632 1.00 39.11  ? 79  TYR   A CE1  1 
ATOM   1202 C  CE2  . TYR   A 1 79  ? -2.939  7.016   -40.804 1.00 35.56  ? 79  TYR   A CE2  1 
ATOM   1203 C  CZ   . TYR   A 1 79  ? -2.859  7.326   -42.154 1.00 40.26  ? 79  TYR   A CZ   1 
ATOM   1204 O  OH   . TYR   A 1 79  ? -3.828  6.900   -43.041 1.00 44.78  ? 79  TYR   A OH   1 
ATOM   1205 H  H    . TYR   A 1 79  ? 0.943   10.902  -40.439 1.00 26.35  ? 79  TYR   A H    1 
ATOM   1206 H  HA   . TYR   A 1 79  ? -1.057  10.193  -38.836 1.00 24.31  ? 79  TYR   A HA   1 
ATOM   1207 H  HB2  . TYR   A 1 79  ? 1.044   8.725   -39.983 1.00 27.55  ? 79  TYR   A HB2  1 
ATOM   1208 H  HB3  . TYR   A 1 79  ? 0.298   8.064   -38.745 1.00 27.55  ? 79  TYR   A HB3  1 
ATOM   1209 H  HD1  . TYR   A 1 79  ? -0.095  8.970   -42.096 1.00 40.39  ? 79  TYR   A HD1  1 
ATOM   1210 H  HD2  . TYR   A 1 79  ? -2.026  7.278   -39.044 1.00 34.18  ? 79  TYR   A HD2  1 
ATOM   1211 H  HE1  . TYR   A 1 79  ? -1.736  8.242   -43.539 1.00 46.93  ? 79  TYR   A HE1  1 
ATOM   1212 H  HE2  . TYR   A 1 79  ? -3.648  6.510   -40.478 1.00 42.67  ? 79  TYR   A HE2  1 
ATOM   1213 H  HH   . TYR   A 1 79  ? -4.433  6.487   -42.630 1.00 53.74  ? 79  TYR   A HH   1 
ATOM   1214 N  N    . THR   A 1 80  ? -0.198  9.911   -36.525 1.00 18.06  ? 80  THR   A N    1 
ATOM   1215 C  CA   . THR   A 1 80  ? 0.342   10.027  -35.168 1.00 17.45  ? 80  THR   A CA   1 
ATOM   1216 C  C    . THR   A 1 80  ? 1.136   8.787   -34.767 1.00 16.96  ? 80  THR   A C    1 
ATOM   1217 O  O    . THR   A 1 80  ? 1.172   7.776   -35.449 1.00 18.54  ? 80  THR   A O    1 
ATOM   1218 C  CB   . THR   A 1 80  ? -0.817  10.220  -34.182 1.00 18.98  ? 80  THR   A CB   1 
ATOM   1219 O  OG1  . THR   A 1 80  ? -1.679  9.080   -34.227 1.00 19.62  ? 80  THR   A OG1  1 
ATOM   1220 C  CG2  . THR   A 1 80  ? -1.620  11.480  -34.530 1.00 21.06  ? 80  THR   A CG2  1 
ATOM   1221 H  H    . THR   A 1 80  ? -1.023  9.673   -36.567 1.00 21.67  ? 80  THR   A H    1 
ATOM   1222 H  HA   . THR   A 1 80  ? 0.944   10.786  -35.137 1.00 20.94  ? 80  THR   A HA   1 
ATOM   1223 H  HB   . THR   A 1 80  ? -0.463  10.324  -33.285 1.00 22.78  ? 80  THR   A HB   1 
ATOM   1224 H  HG1  . THR   A 1 80  ? -1.268  8.399   -33.959 1.00 23.55  ? 80  THR   A HG1  1 
ATOM   1225 H  HG21 . THR   A 1 80  ? -2.347  11.595  -33.898 1.00 25.27  ? 80  THR   A HG21 1 
ATOM   1226 H  HG22 . THR   A 1 80  ? -1.046  12.261  -34.494 1.00 25.27  ? 80  THR   A HG22 1 
ATOM   1227 H  HG23 . THR   A 1 80  ? -1.989  11.402  -35.424 1.00 25.27  ? 80  THR   A HG23 1 
ATOM   1228 N  N    . GLY   A 1 81  ? 1.788   8.905   -33.615 1.00 17.80  ? 81  GLY   A N    1 
ATOM   1229 C  CA   . GLY   A 1 81  ? 2.465   7.780   -33.021 1.00 18.08  ? 81  GLY   A CA   1 
ATOM   1230 C  C    . GLY   A 1 81  ? 3.942   7.755   -33.341 1.00 18.09  ? 81  GLY   A C    1 
ATOM   1231 O  O    . GLY   A 1 81  ? 4.415   8.301   -34.335 1.00 18.80  ? 81  GLY   A O    1 
ATOM   1232 H  H    . GLY   A 1 81  ? 1.848   9.634   -33.162 1.00 21.36  ? 81  GLY   A H    1 
ATOM   1233 H  HA2  . GLY   A 1 81  ? 2.363   7.817   -32.057 1.00 21.69  ? 81  GLY   A HA2  1 
ATOM   1234 H  HA3  . GLY   A 1 81  ? 2.068   6.958   -33.349 1.00 21.69  ? 81  GLY   A HA3  1 
ATOM   1235 N  N    . TYR   A 1 82  ? 4.690   7.053   -32.499 1.00 19.29  ? 82  TYR   A N    1 
ATOM   1236 C  CA   . TYR   A 1 82  ? 6.119   6.972   -32.720 1.00 18.81  ? 82  TYR   A CA   1 
ATOM   1237 C  C    . TYR   A 1 82  ? 6.508   6.171   -33.950 1.00 23.41  ? 82  TYR   A C    1 
ATOM   1238 O  O    . TYR   A 1 82  ? 7.652   6.275   -34.376 1.00 23.17  ? 82  TYR   A O    1 
ATOM   1239 C  CB   . TYR   A 1 82  ? 6.759   6.294   -31.479 1.00 19.93  ? 82  TYR   A CB   1 
ATOM   1240 C  CG   . TYR   A 1 82  ? 6.609   7.092   -30.199 1.00 18.50  ? 82  TYR   A CG   1 
ATOM   1241 C  CD1  . TYR   A 1 82  ? 6.909   8.458   -30.133 1.00 19.04  ? 82  TYR   A CD1  1 
ATOM   1242 C  CD2  . TYR   A 1 82  ? 6.097   6.512   -29.064 1.00 19.62  ? 82  TYR   A CD2  1 
ATOM   1243 C  CE1  . TYR   A 1 82  ? 6.744   9.177   -28.975 1.00 18.61  ? 82  TYR   A CE1  1 
ATOM   1244 C  CE2  . TYR   A 1 82  ? 5.919   7.238   -27.905 1.00 19.92  ? 82  TYR   A CE2  1 
ATOM   1245 C  CZ   . TYR   A 1 82  ? 6.280   8.547   -27.869 1.00 18.23  ? 82  TYR   A CZ   1 
ATOM   1246 O  OH   . TYR   A 1 82  ? 6.102   9.305   -26.737 1.00 19.91  ? 82  TYR   A OH   1 
ATOM   1247 H  H    . TYR   A 1 82  ? 4.399   6.627   -31.811 1.00 23.15  ? 82  TYR   A H    1 
ATOM   1248 H  HA   . TYR   A 1 82  ? 6.460   7.872   -32.843 1.00 22.57  ? 82  TYR   A HA   1 
ATOM   1249 H  HB2  . TYR   A 1 82  ? 6.336   5.432   -31.341 1.00 23.91  ? 82  TYR   A HB2  1 
ATOM   1250 H  HB3  . TYR   A 1 82  ? 7.708   6.176   -31.643 1.00 23.91  ? 82  TYR   A HB3  1 
ATOM   1251 H  HD1  . TYR   A 1 82  ? 7.228   8.889   -30.893 1.00 22.85  ? 82  TYR   A HD1  1 
ATOM   1252 H  HD2  . TYR   A 1 82  ? 5.866   5.611   -29.077 1.00 23.54  ? 82  TYR   A HD2  1 
ATOM   1253 H  HE1  . TYR   A 1 82  ? 6.949   10.084  -28.950 1.00 22.33  ? 82  TYR   A HE1  1 
ATOM   1254 H  HE2  . TYR   A 1 82  ? 5.554   6.834   -27.151 1.00 23.91  ? 82  TYR   A HE2  1 
ATOM   1255 H  HH   . TYR   A 1 82  ? 5.768   8.836   -26.126 1.00 23.89  ? 82  TYR   A HH   1 
ATOM   1256 N  N    . SER   A 1 83  ? 5.599   5.386   -34.538 1.00 21.07  ? 83  SER   A N    1 
ATOM   1257 C  CA   . SER   A 1 83  ? 5.811   4.659   -35.790 1.00 22.70  ? 83  SER   A CA   1 
ATOM   1258 C  C    . SER   A 1 83  ? 5.028   5.259   -36.947 1.00 22.52  ? 83  SER   A C    1 
ATOM   1259 O  O    . SER   A 1 83  ? 4.961   4.648   -38.009 1.00 25.08  ? 83  SER   A O    1 
ATOM   1260 C  CB   . SER   A 1 83  ? 5.398   3.210   -35.597 1.00 26.73  ? 83  SER   A CB   1 
ATOM   1261 O  OG   . SER   A 1 83  ? 6.237   2.533   -34.681 1.00 33.87  ? 83  SER   A OG   1 
ATOM   1262 H  H    . SER   A 1 83  ? 4.814   5.253   -34.213 1.00 25.28  ? 83  SER   A H    1 
ATOM   1263 H  HA   . SER   A 1 83  ? 6.753   4.692   -36.021 1.00 27.23  ? 83  SER   A HA   1 
ATOM   1264 H  HB2  . SER   A 1 83  ? 4.489   3.188   -35.259 1.00 32.08  ? 83  SER   A HB2  1 
ATOM   1265 H  HB3  . SER   A 1 83  ? 5.444   2.757   -36.454 1.00 32.08  ? 83  SER   A HB3  1 
ATOM   1266 H  HG   . SER   A 1 83  ? 5.995   1.731   -34.608 1.00 40.64  ? 83  SER   A HG   1 
ATOM   1267 N  N    . ALA   A 1 84  ? 4.400   6.420   -36.764 1.00 21.91  ? 84  ALA   A N    1 
ATOM   1268 C  CA   . ALA   A 1 84  ? 3.755   7.133   -37.867 1.00 22.87  ? 84  ALA   A CA   1 
ATOM   1269 C  C    . ALA   A 1 84  ? 2.696   6.255   -38.536 1.00 22.23  ? 84  ALA   A C    1 
ATOM   1270 O  O    . ALA   A 1 84  ? 2.536   6.228   -39.753 1.00 22.73  ? 84  ALA   A O    1 
ATOM   1271 C  CB   . ALA   A 1 84  ? 4.767   7.665   -38.884 1.00 27.05  ? 84  ALA   A CB   1 
ATOM   1272 H  H    . ALA   A 1 84  ? 4.332   6.818   -36.004 1.00 26.29  ? 84  ALA   A H    1 
ATOM   1273 H  HA   . ALA   A 1 84  ? 3.303   7.909   -37.501 1.00 27.44  ? 84  ALA   A HA   1 
ATOM   1274 H  HB1  . ALA   A 1 84  ? 4.294   8.161   -39.570 1.00 32.46  ? 84  ALA   A HB1  1 
ATOM   1275 H  HB2  . ALA   A 1 84  ? 5.396   8.247   -38.428 1.00 32.46  ? 84  ALA   A HB2  1 
ATOM   1276 H  HB3  . ALA   A 1 84  ? 5.239   6.917   -39.281 1.00 32.46  ? 84  ALA   A HB3  1 
ATOM   1277 N  N    . ASP   A 1 85  ? 1.942   5.543   -37.704 1.00 20.06  ? 85  ASP   A N    1 
ATOM   1278 C  CA   . ASP   A 1 85  ? 0.884   4.630   -38.168 1.00 19.64  ? 85  ASP   A CA   1 
ATOM   1279 C  C    . ASP   A 1 85  ? -0.478  4.902   -37.546 1.00 19.15  ? 85  ASP   A C    1 
ATOM   1280 O  O    . ASP   A 1 85  ? -1.419  4.169   -37.819 1.00 20.63  ? 85  ASP   A O    1 
ATOM   1281 C  CB   . ASP   A 1 85  ? 1.323   3.176   -37.930 1.00 21.80  ? 85  ASP   A CB   1 
ATOM   1282 C  CG   . ASP   A 1 85  ? 1.479   2.816   -36.446 1.00 25.05  ? 85  ASP   A CG   1 
ATOM   1283 O  OD1  . ASP   A 1 85  ? 1.314   3.700   -35.595 1.00 22.68  ? 85  ASP   A OD1  1 
ATOM   1284 O  OD2  . ASP   A 1 85  ? 1.881   1.659   -36.151 1.00 28.39  ? 85  ASP   A OD2  1 
ATOM   1285 H  H    . ASP   A 1 85  ? 2.019   5.567   -36.847 1.00 24.07  ? 85  ASP   A H    1 
ATOM   1286 H  HA   . ASP   A 1 85  ? 0.760   4.737   -39.124 1.00 23.57  ? 85  ASP   A HA   1 
ATOM   1287 H  HB2  . ASP   A 1 85  ? 0.657   2.582   -38.310 1.00 26.16  ? 85  ASP   A HB2  1 
ATOM   1288 H  HB3  . ASP   A 1 85  ? 2.180   3.033   -38.361 1.00 26.16  ? 85  ASP   A HB3  1 
ATOM   1289 N  N    . GLY   A 1 86  ? -0.603  5.932   -36.719 1.00 17.60  ? 86  GLY   A N    1 
ATOM   1290 C  CA   . GLY   A 1 86  ? -1.839  6.305   -36.094 1.00 17.95  ? 86  GLY   A CA   1 
ATOM   1291 C  C    . GLY   A 1 86  ? -2.081  5.669   -34.743 1.00 16.25  ? 86  GLY   A C    1 
ATOM   1292 O  O    . GLY   A 1 86  ? -3.106  5.968   -34.116 1.00 16.13  ? 86  GLY   A O    1 
ATOM   1293 H  H    . GLY   A 1 86  ? 0.050   6.447   -36.501 1.00 21.12  ? 86  GLY   A H    1 
ATOM   1294 H  HA2  . GLY   A 1 86  ? -1.850  7.268   -35.975 1.00 21.55  ? 86  GLY   A HA2  1 
ATOM   1295 H  HA3  . GLY   A 1 86  ? -2.572  6.051   -36.677 1.00 21.55  ? 86  GLY   A HA3  1 
ATOM   1296 N  N    . TYR   A 1 87  ? -1.175  4.793   -34.297 1.00 17.27  ? 87  TYR   A N    1 
ATOM   1297 C  CA   . TYR   A 1 87  ? -1.391  3.997   -33.090 1.00 16.01  ? 87  TYR   A CA   1 
ATOM   1298 C  C    . TYR   A 1 87  ? -0.436  4.392   -31.970 1.00 16.75  ? 87  TYR   A C    1 
ATOM   1299 O  O    . TYR   A 1 87  ? 0.640   4.946   -32.188 1.00 18.64  ? 87  TYR   A O    1 
ATOM   1300 C  CB   . TYR   A 1 87  ? -1.263  2.475   -33.363 1.00 16.85  ? 87  TYR   A CB   1 
ATOM   1301 C  CG   . TYR   A 1 87  ? -2.422  1.922   -34.137 1.00 16.92  ? 87  TYR   A CG   1 
ATOM   1302 C  CD1  . TYR   A 1 87  ? -3.587  1.648   -33.477 1.00 18.23  ? 87  TYR   A CD1  1 
ATOM   1303 C  CD2  . TYR   A 1 87  ? -2.367  1.768   -35.508 1.00 19.54  ? 87  TYR   A CD2  1 
ATOM   1304 C  CE1  . TYR   A 1 87  ? -4.719  1.195   -34.175 1.00 19.69  ? 87  TYR   A CE1  1 
ATOM   1305 C  CE2  . TYR   A 1 87  ? -3.471  1.294   -36.233 1.00 22.72  ? 87  TYR   A CE2  1 
ATOM   1306 C  CZ   . TYR   A 1 87  ? -4.625  1.026   -35.547 1.00 23.34  ? 87  TYR   A CZ   1 
ATOM   1307 O  OH   . TYR   A 1 87  ? -5.736  0.600   -36.273 1.00 23.24  ? 87  TYR   A OH   1 
ATOM   1308 H  H    . TYR   A 1 87  ? -0.422  4.642   -34.683 1.00 20.72  ? 87  TYR   A H    1 
ATOM   1309 H  HA   . TYR   A 1 87  ? -2.294  4.177   -32.786 1.00 19.21  ? 87  TYR   A HA   1 
ATOM   1310 H  HB2  . TYR   A 1 87  ? -0.455  2.314   -33.876 1.00 20.23  ? 87  TYR   A HB2  1 
ATOM   1311 H  HB3  . TYR   A 1 87  ? -1.216  2.005   -32.516 1.00 20.23  ? 87  TYR   A HB3  1 
ATOM   1312 H  HD1  . TYR   A 1 87  ? -3.631  1.763   -32.556 1.00 21.87  ? 87  TYR   A HD1  1 
ATOM   1313 H  HD2  . TYR   A 1 87  ? -1.583  1.982   -35.960 1.00 23.45  ? 87  TYR   A HD2  1 
ATOM   1314 H  HE1  . TYR   A 1 87  ? -5.513  1.013   -33.726 1.00 23.62  ? 87  TYR   A HE1  1 
ATOM   1315 H  HE2  . TYR   A 1 87  ? -3.420  1.167   -37.152 1.00 27.27  ? 87  TYR   A HE2  1 
ATOM   1316 H  HH   . TYR   A 1 87  ? -6.349  0.366   -35.748 1.00 27.89  ? 87  TYR   A HH   1 
ATOM   1317 N  N    . ASP   A 1 88  ? -0.847  4.105   -30.745 1.00 15.82  ? 88  ASP   A N    1 
ATOM   1318 C  CA   . ASP   A 1 88  ? -0.003  4.192   -29.567 1.00 15.55  ? 88  ASP   A CA   1 
ATOM   1319 C  C    . ASP   A 1 88  ? -0.570  3.172   -28.575 1.00 14.79  ? 88  ASP   A C    1 
ATOM   1320 O  O    . ASP   A 1 88  ? -1.136  3.540   -27.563 1.00 14.92  ? 88  ASP   A O    1 
ATOM   1321 C  CB   . ASP   A 1 88  ? -0.096  5.606   -29.013 1.00 17.19  ? 88  ASP   A CB   1 
ATOM   1322 C  CG   . ASP   A 1 88  ? 0.789   5.841   -27.756 1.00 17.38  ? 88  ASP   A CG   1 
ATOM   1323 O  OD1  . ASP   A 1 88  ? 1.699   4.999   -27.449 1.00 22.39  ? 88  ASP   A OD1  1 
ATOM   1324 O  OD2  . ASP   A 1 88  ? 0.404   6.688   -26.924 1.00 18.23  ? 88  ASP   A OD2  1 
ATOM   1325 H  H    . ASP   A 1 88  ? -1.647  3.846   -30.563 1.00 18.98  ? 88  ASP   A H    1 
ATOM   1326 H  HA   . ASP   A 1 88  ? 0.925   3.989   -29.765 1.00 18.65  ? 88  ASP   A HA   1 
ATOM   1327 H  HB2  . ASP   A 1 88  ? 0.191   6.231   -29.698 1.00 20.63  ? 88  ASP   A HB2  1 
ATOM   1328 H  HB3  . ASP   A 1 88  ? -1.017  5.785   -28.765 1.00 20.63  ? 88  ASP   A HB3  1 
ATOM   1329 N  N    . ARG   A 1 89  ? -0.512  1.894   -28.951 1.00 16.55  ? 89  ARG   A N    1 
ATOM   1330 C  CA   . ARG   A 1 89  ? -1.328  0.870   -28.304 1.00 15.34  ? 89  ARG   A CA   1 
ATOM   1331 C  C    . ARG   A 1 89  ? -0.873  0.625   -26.868 1.00 16.47  ? 89  ARG   A C    1 
ATOM   1332 O  O    . ARG   A 1 89  ? 0.343   0.612   -26.599 1.00 18.54  ? 89  ARG   A O    1 
ATOM   1333 C  CB   . ARG   A 1 89  ? -1.267  -0.435  -29.058 1.00 16.76  ? 89  ARG   A CB   1 
ATOM   1334 C  CG   . ARG   A 1 89  ? -2.096  -0.443  -30.377 1.00 18.96  ? 89  ARG   A CG   1 
ATOM   1335 C  CD   . ARG   A 1 89  ? -1.999  -1.780  -31.057 1.00 21.60  ? 89  ARG   A CD   1 
ATOM   1336 N  NE   . ARG   A 1 89  ? -2.767  -1.842  -32.326 1.00 22.20  ? 89  ARG   A NE   1 
ATOM   1337 C  CZ   . ARG   A 1 89  ? -2.238  -1.729  -33.503 1.00 23.86  ? 89  ARG   A CZ   1 
ATOM   1338 N  NH1  . ARG   A 1 89  ? -0.999  -1.313  -33.645 1.00 25.18  ? 89  ARG   A NH1  1 
ATOM   1339 N  NH2  . ARG   A 1 89  ? -2.984  -1.981  -34.572 1.00 24.36  ? 89  ARG   A NH2  1 
ATOM   1340 H  H    . ARG   A 1 89  ? -0.007  1.593   -29.579 1.00 19.86  ? 89  ARG   A H    1 
ATOM   1341 H  HA   . ARG   A 1 89  ? -2.246  1.185   -28.296 1.00 18.41  ? 89  ARG   A HA   1 
ATOM   1342 H  HB2  . ARG   A 1 89  ? -0.343  -0.618  -29.289 1.00 20.11  ? 89  ARG   A HB2  1 
ATOM   1343 H  HB3  . ARG   A 1 89  ? -1.613  -1.140  -28.488 1.00 20.11  ? 89  ARG   A HB3  1 
ATOM   1344 H  HG2  . ARG   A 1 89  ? -3.029  -0.266  -30.175 1.00 22.76  ? 89  ARG   A HG2  1 
ATOM   1345 H  HG3  . ARG   A 1 89  ? -1.753  0.235   -30.980 1.00 22.76  ? 89  ARG   A HG3  1 
ATOM   1346 H  HD2  . ARG   A 1 89  ? -1.069  -1.963  -31.262 1.00 25.92  ? 89  ARG   A HD2  1 
ATOM   1347 H  HD3  . ARG   A 1 89  ? -2.349  -2.462  -30.463 1.00 25.92  ? 89  ARG   A HD3  1 
ATOM   1348 H  HE   . ARG   A 1 89  ? -3.617  -1.961  -32.276 1.00 26.64  ? 89  ARG   A HE   1 
ATOM   1349 H  HH11 . ARG   A 1 89  ? -0.531  -1.113  -32.952 1.00 30.22  ? 89  ARG   A HH11 1 
ATOM   1350 H  HH12 . ARG   A 1 89  ? -0.657  -1.241  -34.430 1.00 30.22  ? 89  ARG   A HH12 1 
ATOM   1351 H  HH21 . ARG   A 1 89  ? -3.806  -2.216  -34.477 1.00 29.23  ? 89  ARG   A HH21 1 
ATOM   1352 H  HH22 . ARG   A 1 89  ? -2.645  -1.910  -35.360 1.00 29.23  ? 89  ARG   A HH22 1 
ATOM   1353 N  N    . ASP   A 1 90  ? -1.832  0.416   -25.962 1.00 15.94  ? 90  ASP   A N    1 
ATOM   1354 C  CA   . ASP   A 1 90  ? -1.489  0.005   -24.613 1.00 14.83  ? 90  ASP   A CA   1 
ATOM   1355 C  C    . ASP   A 1 90  ? -2.705  -0.635  -23.991 1.00 14.92  ? 90  ASP   A C    1 
ATOM   1356 O  O    . ASP   A 1 90  ? -3.783  -0.050  -24.021 1.00 14.23  ? 90  ASP   A O    1 
ATOM   1357 C  CB   . ASP   A 1 90  ? -1.022  1.201   -23.813 1.00 16.63  ? 90  ASP   A CB   1 
ATOM   1358 C  CG   . ASP   A 1 90  ? -0.275  0.771   -22.549 1.00 22.73  ? 90  ASP   A CG   1 
ATOM   1359 O  OD1  . ASP   A 1 90  ? -0.903  0.171   -21.655 1.00 23.57  ? 90  ASP   A OD1  1 
ATOM   1360 O  OD2  . ASP   A 1 90  ? 0.915   1.200   -22.441 1.00 30.34  ? 90  ASP   A OD2  1 
ATOM   1361 H  H    . ASP   A 1 90  ? -2.674  0.506   -26.109 1.00 19.13  ? 90  ASP   A H    1 
ATOM   1362 H  HA   . ASP   A 1 90  ? -0.778  -0.655  -24.620 1.00 17.79  ? 90  ASP   A HA   1 
ATOM   1363 H  HB2  . ASP   A 1 90  ? -0.422  1.736   -24.355 1.00 19.96  ? 90  ASP   A HB2  1 
ATOM   1364 H  HB3  . ASP   A 1 90  ? -1.791  1.730   -23.548 1.00 19.96  ? 90  ASP   A HB3  1 
ATOM   1365 N  N    . ASN   A 1 91  ? -2.537  -1.852  -23.482 1.00 15.57  ? 91  ASN   A N    1 
ATOM   1366 C  CA   . ASN   A 1 91  ? -3.546  -2.500  -22.643 1.00 15.36  ? 91  ASN   A CA   1 
ATOM   1367 C  C    . ASN   A 1 91  ? -4.928  -2.507  -23.290 1.00 15.20  ? 91  ASN   A C    1 
ATOM   1368 O  O    . ASN   A 1 91  ? -5.931  -2.297  -22.636 1.00 16.22  ? 91  ASN   A O    1 
ATOM   1369 C  CB   . ASN   A 1 91  ? -3.585  -1.930  -21.229 1.00 16.02  ? 91  ASN   A CB   1 
ATOM   1370 C  CG   . ASN   A 1 91  ? -4.431  -2.752  -20.306 1.00 15.81  ? 91  ASN   A CG   1 
ATOM   1371 O  OD1  . ASN   A 1 91  ? -4.545  -3.953  -20.439 1.00 18.92  ? 91  ASN   A OD1  1 
ATOM   1372 N  ND2  . ASN   A 1 91  ? -5.044  -2.108  -19.327 1.00 16.78  ? 91  ASN   A ND2  1 
ATOM   1373 H  H    . ASN   A 1 91  ? -1.836  -2.332  -23.608 1.00 18.69  ? 91  ASN   A H    1 
ATOM   1374 H  HA   . ASN   A 1 91  ? -3.279  -3.429  -22.561 1.00 18.43  ? 91  ASN   A HA   1 
ATOM   1375 H  HB2  . ASN   A 1 91  ? -2.684  -1.907  -20.871 1.00 19.22  ? 91  ASN   A HB2  1 
ATOM   1376 H  HB3  . ASN   A 1 91  ? -3.954  -1.033  -21.258 1.00 19.22  ? 91  ASN   A HB3  1 
ATOM   1377 H  HD21 . ASN   A 1 91  ? -5.540  -2.540  -18.773 1.00 20.13  ? 91  ASN   A HD21 1 
ATOM   1378 H  HD22 . ASN   A 1 91  ? -4.945  -1.258  -19.244 1.00 20.13  ? 91  ASN   A HD22 1 
ATOM   1379 N  N    . GLY   A 1 92  ? -4.965  -2.753  -24.603 1.00 15.56  ? 92  GLY   A N    1 
ATOM   1380 C  CA   . GLY   A 1 92  ? -6.234  -2.920  -25.297 1.00 16.36  ? 92  GLY   A CA   1 
ATOM   1381 C  C    . GLY   A 1 92  ? -6.841  -1.654  -25.844 1.00 15.30  ? 92  GLY   A C    1 
ATOM   1382 O  O    . GLY   A 1 92  ? -7.908  -1.732  -26.459 1.00 16.61  ? 92  GLY   A O    1 
ATOM   1383 H  H    . GLY   A 1 92  ? -4.271  -2.827  -25.105 1.00 18.68  ? 92  GLY   A H    1 
ATOM   1384 H  HA2  . GLY   A 1 92  ? -6.101  -3.527  -26.042 1.00 19.63  ? 92  GLY   A HA2  1 
ATOM   1385 H  HA3  . GLY   A 1 92  ? -6.874  -3.311  -24.681 1.00 19.63  ? 92  GLY   A HA3  1 
ATOM   1386 N  N    . ALA   A 1 93  ? -6.190  -0.521  -25.680 1.00 14.74  ? 93  ALA   A N    1 
ATOM   1387 C  CA   . ALA   A 1 93  ? -6.570  0.754   -26.320 1.00 14.56  ? 93  ALA   A CA   1 
ATOM   1388 C  C    . ALA   A 1 93  ? -5.691  1.075   -27.512 1.00 14.37  ? 93  ALA   A C    1 
ATOM   1389 O  O    . ALA   A 1 93  ? -4.497  0.732   -27.542 1.00 15.59  ? 93  ALA   A O    1 
ATOM   1390 C  CB   . ALA   A 1 93  ? -6.457  1.898   -25.321 1.00 15.30  ? 93  ALA   A CB   1 
ATOM   1391 H  H    . ALA   A 1 93  ? -5.491  -0.447  -25.184 1.00 17.69  ? 93  ALA   A H    1 
ATOM   1392 H  HA   . ALA   A 1 93  ? -7.483  0.670   -26.637 1.00 17.48  ? 93  ALA   A HA   1 
ATOM   1393 H  HB1  . ALA   A 1 93  ? -6.700  2.727   -25.762 1.00 18.36  ? 93  ALA   A HB1  1 
ATOM   1394 H  HB2  . ALA   A 1 93  ? -7.058  1.730   -24.579 1.00 18.36  ? 93  ALA   A HB2  1 
ATOM   1395 H  HB3  . ALA   A 1 93  ? -5.543  1.949   -25.002 1.00 18.36  ? 93  ALA   A HB3  1 
ATOM   1396 N  N    . ALA   A 1 94  ? -6.298  1.641   -28.558 1.00 15.47  ? 94  ALA   A N    1 
ATOM   1397 C  CA   . ALA   A 1 94  ? -5.578  1.984   -29.781 1.00 15.08  ? 94  ALA   A CA   1 
ATOM   1398 C  C    . ALA   A 1 94  ? -4.553  3.091   -29.590 1.00 14.42  ? 94  ALA   A C    1 
ATOM   1399 O  O    . ALA   A 1 94  ? -3.452  2.979   -30.154 1.00 15.25  ? 94  ALA   A O    1 
ATOM   1400 C  CB   . ALA   A 1 94  ? -6.554  2.383   -30.889 1.00 15.97  ? 94  ALA   A CB   1 
ATOM   1401 H  H    . ALA   A 1 94  ? -7.134  1.839   -28.584 1.00 18.56  ? 94  ALA   A H    1 
ATOM   1402 H  HA   . ALA   A 1 94  ? -5.098  1.185   -30.048 1.00 18.09  ? 94  ALA   A HA   1 
ATOM   1403 H  HB1  . ALA   A 1 94  ? -6.052  2.592   -31.692 1.00 19.17  ? 94  ALA   A HB1  1 
ATOM   1404 H  HB2  . ALA   A 1 94  ? -7.158  1.643   -31.059 1.00 19.17  ? 94  ALA   A HB2  1 
ATOM   1405 H  HB3  . ALA   A 1 94  ? -7.057  3.161   -30.601 1.00 19.17  ? 94  ALA   A HB3  1 
ATOM   1406 N  N    . SER   A 1 95  ? -4.915  4.143   -28.868 1.00 13.57  ? 95  SER   A N    1 
ATOM   1407 C  CA   . SER   A 1 95  ? -4.028  5.299   -28.711 1.00 14.66  ? 95  SER   A CA   1 
ATOM   1408 C  C    . SER   A 1 95  ? -4.579  6.176   -27.604 1.00 14.03  ? 95  SER   A C    1 
ATOM   1409 O  O    . SER   A 1 95  ? -5.299  7.153   -27.861 1.00 13.74  ? 95  SER   A O    1 
ATOM   1410 C  CB   . SER   A 1 95  ? -3.904  6.116   -30.001 1.00 14.91  ? 95  SER   A CB   1 
ATOM   1411 O  OG   . SER   A 1 95  ? -3.040  7.213   -29.749 1.00 15.72  ? 95  SER   A OG   1 
ATOM   1412 H  H    . SER   A 1 95  ? -5.667  4.216   -28.457 1.00 16.29  ? 95  SER   A H    1 
ATOM   1413 H  HA   . SER   A 1 95  ? -3.138  4.986   -28.487 1.00 17.59  ? 95  SER   A HA   1 
ATOM   1414 H  HB2  . SER   A 1 95  ? -3.530  5.561   -30.704 1.00 17.90  ? 95  SER   A HB2  1 
ATOM   1415 H  HB3  . SER   A 1 95  ? -4.778  6.442   -30.266 1.00 17.90  ? 95  SER   A HB3  1 
ATOM   1416 H  HG   . SER   A 1 95  ? -2.239  6.972   -29.827 1.00 18.86  ? 95  SER   A HG   1 
ATOM   1417 N  N    . PRO   A 1 96  ? -4.220  5.914   -26.355 1.00 12.57  ? 96  PRO   A N    1 
ATOM   1418 C  CA   . PRO   A 1 96  ? -4.656  6.797   -25.294 1.00 13.60  ? 96  PRO   A CA   1 
ATOM   1419 C  C    . PRO   A 1 96  ? -4.228  8.229   -25.488 1.00 13.12  ? 96  PRO   A C    1 
ATOM   1420 O  O    . PRO   A 1 96  ? -4.952  9.117   -25.010 1.00 12.67  ? 96  PRO   A O    1 
ATOM   1421 C  CB   . PRO   A 1 96  ? -4.047  6.142   -24.022 1.00 13.47  ? 96  PRO   A CB   1 
ATOM   1422 C  CG   . PRO   A 1 96  ? -4.004  4.663   -24.423 1.00 14.94  ? 96  PRO   A CG   1 
ATOM   1423 C  CD   . PRO   A 1 96  ? -3.540  4.710   -25.834 1.00 14.23  ? 96  PRO   A CD   1 
ATOM   1424 H  HA   . PRO   A 1 96  ? -5.622  6.779   -25.212 1.00 16.32  ? 96  PRO   A HA   1 
ATOM   1425 H  HB2  . PRO   A 1 96  ? -3.160  6.492   -23.847 1.00 16.17  ? 96  PRO   A HB2  1 
ATOM   1426 H  HB3  . PRO   A 1 96  ? -4.619  6.289   -23.253 1.00 16.17  ? 96  PRO   A HB3  1 
ATOM   1427 H  HG2  . PRO   A 1 96  ? -3.380  4.178   -23.861 1.00 17.93  ? 96  PRO   A HG2  1 
ATOM   1428 H  HG3  . PRO   A 1 96  ? -4.888  4.268   -24.354 1.00 17.93  ? 96  PRO   A HG3  1 
ATOM   1429 H  HD2  . PRO   A 1 96  ? -2.576  4.807   -25.881 1.00 17.07  ? 96  PRO   A HD2  1 
ATOM   1430 H  HD3  . PRO   A 1 96  ? -3.817  3.916   -26.319 1.00 17.07  ? 96  PRO   A HD3  1 
ATOM   1431 N  N    . THR   A 1 97  ? -3.062  8.468   -26.050 1.00 12.65  ? 97  THR   A N    1 
ATOM   1432 C  CA   . THR   A 1 97  ? -2.601  9.822   -26.308 1.00 12.42  ? 97  THR   A CA   1 
ATOM   1433 C  C    . THR   A 1 97  ? -3.470  10.552  -27.329 1.00 12.21  ? 97  THR   A C    1 
ATOM   1434 O  O    . THR   A 1 97  ? -3.805  11.736  -27.102 1.00 13.34  ? 97  THR   A O    1 
ATOM   1435 C  CB   . THR   A 1 97  ? -1.113  9.815   -26.670 1.00 12.79  ? 97  THR   A CB   1 
ATOM   1436 O  OG1  . THR   A 1 97  ? -0.892  8.885   -27.722 1.00 14.70  ? 97  THR   A OG1  1 
ATOM   1437 C  CG2  . THR   A 1 97  ? -0.263  9.442   -25.443 1.00 15.11  ? 97  THR   A CG2  1 
ATOM   1438 H  H    . THR   A 1 97  ? -2.507  7.859   -26.297 1.00 15.18  ? 97  THR   A H    1 
ATOM   1439 H  HA   . THR   A 1 97  ? -2.680  10.341  -25.492 1.00 14.90  ? 97  THR   A HA   1 
ATOM   1440 H  HB   . THR   A 1 97  ? -0.838  10.697  -26.964 1.00 15.35  ? 97  THR   A HB   1 
ATOM   1441 H  HG1  . THR   A 1 97  ? -1.059  8.106   -27.456 1.00 17.64  ? 97  THR   A HG1  1 
ATOM   1442 H  HG21 . THR   A 1 97  ? 0.653   9.269   -25.714 1.00 18.14  ? 97  THR   A HG21 1 
ATOM   1443 H  HG22 . THR   A 1 97  ? -0.269  10.170  -24.802 1.00 18.14  ? 97  THR   A HG22 1 
ATOM   1444 H  HG23 . THR   A 1 97  ? -0.621  8.646   -25.020 1.00 18.14  ? 97  THR   A HG23 1 
ATOM   1445 N  N    . ASN   A 1 98  ? -3.875  9.908   -28.432 1.00 12.68  ? 98  ASN   A N    1 
ATOM   1446 C  CA   . ASN   A 1 98  ? -4.811  10.575  -29.337 1.00 12.60  ? 98  ASN   A CA   1 
ATOM   1447 C  C    . ASN   A 1 98  ? -6.130  10.848  -28.628 1.00 12.98  ? 98  ASN   A C    1 
ATOM   1448 O  O    . ASN   A 1 98  ? -6.710  11.941  -28.767 1.00 14.02  ? 98  ASN   A O    1 
ATOM   1449 C  CB   . ASN   A 1 98  ? -5.100  9.675   -30.539 1.00 13.09  ? 98  ASN   A CB   1 
ATOM   1450 C  CG   . ASN   A 1 98  ? -4.000  9.610   -31.481 1.00 14.65  ? 98  ASN   A CG   1 
ATOM   1451 O  OD1  . ASN   A 1 98  ? -3.005  10.330  -31.402 1.00 15.70  ? 98  ASN   A OD1  1 
ATOM   1452 N  ND2  . ASN   A 1 98  ? -4.156  8.719   -32.485 1.00 14.88  ? 98  ASN   A ND2  1 
ATOM   1453 H  H    . ASN   A 1 98  ? -3.631  9.118   -28.668 1.00 15.21  ? 98  ASN   A H    1 
ATOM   1454 H  HA   . ASN   A 1 98  ? -4.410  11.406  -29.636 1.00 15.12  ? 98  ASN   A HA   1 
ATOM   1455 H  HB2  . ASN   A 1 98  ? -5.276  8.775   -30.223 1.00 15.71  ? 98  ASN   A HB2  1 
ATOM   1456 H  HB3  . ASN   A 1 98  ? -5.876  10.018  -31.010 1.00 15.71  ? 98  ASN   A HB3  1 
ATOM   1457 H  HD21 . ASN   A 1 98  ? -3.542  8.628   -33.079 1.00 17.86  ? 98  ASN   A HD21 1 
ATOM   1458 H  HD22 . ASN   A 1 98  ? -4.871  8.242   -32.529 1.00 17.86  ? 98  ASN   A HD22 1 
ATOM   1459 N  N    . ASP   A 1 99  ? -6.666  9.868   -27.898 1.00 12.55  ? 99  ASP   A N    1 
ATOM   1460 C  CA   . ASP   A 1 99  ? -7.937  10.049  -27.178 1.00 13.45  ? 99  ASP   A CA   1 
ATOM   1461 C  C    . ASP   A 1 99  ? -7.863  11.212  -26.207 1.00 13.76  ? 99  ASP   A C    1 
ATOM   1462 O  O    . ASP   A 1 99  ? -8.879  11.893  -25.969 1.00 14.09  ? 99  ASP   A O    1 
ATOM   1463 C  CB   . ASP   A 1 99  ? -8.399  8.765   -26.514 1.00 14.22  ? 99  ASP   A CB   1 
ATOM   1464 C  CG   . ASP   A 1 99  ? -9.169  7.867   -27.459 1.00 17.50  ? 99  ASP   A CG   1 
ATOM   1465 O  OD1  . ASP   A 1 99  ? -9.834  8.384   -28.379 1.00 19.13  ? 99  ASP   A OD1  1 
ATOM   1466 O  OD2  . ASP   A 1 99  ? -9.066  6.664   -27.328 1.00 16.81  ? 99  ASP   A OD2  1 
ATOM   1467 H  H    . ASP   A 1 99  ? -6.317  9.088   -27.799 1.00 15.06  ? 99  ASP   A H    1 
ATOM   1468 H  HA   . ASP   A 1 99  ? -8.624  10.262  -27.829 1.00 16.14  ? 99  ASP   A HA   1 
ATOM   1469 H  HB2  . ASP   A 1 99  ? -7.624  8.275   -26.198 1.00 17.06  ? 99  ASP   A HB2  1 
ATOM   1470 H  HB3  . ASP   A 1 99  ? -8.980  8.986   -25.769 1.00 17.06  ? 99  ASP   A HB3  1 
ATOM   1471 N  N    . ALA   A 1 100 ? -6.733  11.408  -25.533 1.00 13.21  ? 100 ALA   A N    1 
ATOM   1472 C  CA   . ALA   A 1 100 ? -6.636  12.495  -24.572 1.00 12.41  ? 100 ALA   A CA   1 
ATOM   1473 C  C    . ALA   A 1 100 ? -6.615  13.834  -25.254 1.00 12.28  ? 100 ALA   A C    1 
ATOM   1474 O  O    . ALA   A 1 100 ? -7.200  14.787  -24.721 1.00 12.93  ? 100 ALA   A O    1 
ATOM   1475 C  CB   . ALA   A 1 100 ? -5.375  12.269  -23.742 1.00 14.43  ? 100 ALA   A CB   1 
ATOM   1476 H  H    . ALA   A 1 100 ? -6.021  10.932  -25.613 1.00 15.86  ? 100 ALA   A H    1 
ATOM   1477 H  HA   . ALA   A 1 100 ? -7.408  12.500  -23.985 1.00 14.90  ? 100 ALA   A HA   1 
ATOM   1478 H  HB1  . ALA   A 1 100 ? -5.294  12.981  -23.090 1.00 17.32  ? 100 ALA   A HB1  1 
ATOM   1479 H  HB2  . ALA   A 1 100 ? -5.443  11.413  -23.291 1.00 17.32  ? 100 ALA   A HB2  1 
ATOM   1480 H  HB3  . ALA   A 1 100 ? -4.604  12.271  -24.332 1.00 17.32  ? 100 ALA   A HB3  1 
ATOM   1481 N  N    . LEU   A 1 101 ? -5.894  13.951  -26.366 1.00 12.49  ? 101 LEU   A N    1 
ATOM   1482 C  CA   . LEU   A 1 101 ? -5.821  15.230  -27.111 1.00 13.58  ? 101 LEU   A CA   1 
ATOM   1483 C  C    . LEU   A 1 101 ? -7.246  15.588  -27.545 1.00 15.53  ? 101 LEU   A C    1 
ATOM   1484 O  O    . LEU   A 1 101 ? -7.641  16.753  -27.370 1.00 14.83  ? 101 LEU   A O    1 
ATOM   1485 C  CB   . LEU   A 1 101 ? -4.872  15.095  -28.299 1.00 13.72  ? 101 LEU   A CB   1 
ATOM   1486 C  CG   . LEU   A 1 101 ? -4.520  16.395  -29.030 1.00 16.15  ? 101 LEU   A CG   1 
ATOM   1487 C  CD1  . LEU   A 1 101 ? -3.883  17.420  -28.105 1.00 17.25  ? 101 LEU   A CD1  1 
ATOM   1488 C  CD2  . LEU   A 1 101 ? -3.603  16.094  -30.200 1.00 17.32  ? 101 LEU   A CD2  1 
ATOM   1489 H  H    . LEU   A 1 101 ? -5.427  13.260  -26.713 1.00 14.98  ? 101 LEU   A H    1 
ATOM   1490 H  HA   . LEU   A 1 101 ? -5.485  15.930  -26.497 1.00 16.30  ? 101 LEU   A HA   1 
ATOM   1491 H  HB2  . LEU   A 1 101 ? -4.036  14.683  -27.979 1.00 16.46  ? 101 LEU   A HB2  1 
ATOM   1492 H  HB3  . LEU   A 1 101 ? -5.279  14.476  -28.948 1.00 16.46  ? 101 LEU   A HB3  1 
ATOM   1493 H  HG   . LEU   A 1 101 ? -5.358  16.784  -29.389 1.00 19.38  ? 101 LEU   A HG   1 
ATOM   1494 H  HD11 . LEU   A 1 101 ? -3.575  18.180  -28.628 1.00 20.71  ? 101 LEU   A HD11 1 
ATOM   1495 H  HD12 . LEU   A 1 101 ? -4.536  17.722  -27.452 1.00 20.71  ? 101 LEU   A HD12 1 
ATOM   1496 H  HD13 . LEU   A 1 101 ? -3.127  17.017  -27.646 1.00 20.71  ? 101 LEU   A HD13 1 
ATOM   1497 H  HD21 . LEU   A 1 101 ? -3.431  16.911  -30.697 1.00 20.78  ? 101 LEU   A HD21 1 
ATOM   1498 H  HD22 . LEU   A 1 101 ? -2.762  15.735  -29.869 1.00 20.78  ? 101 LEU   A HD22 1 
ATOM   1499 H  HD23 . LEU   A 1 101 ? -4.025  15.442  -30.785 1.00 20.78  ? 101 LEU   A HD23 1 
ATOM   1500 N  N    . TYR   A 1 102 ? -7.992  14.606  -28.047 1.00 14.52  ? 102 TYR   A N    1 
ATOM   1501 C  CA   . TYR   A 1 102 ? -9.385  14.832  -28.511 1.00 15.14  ? 102 TYR   A CA   1 
ATOM   1502 C  C    . TYR   A 1 102 ? -10.291 15.111  -27.319 1.00 15.10  ? 102 TYR   A C    1 
ATOM   1503 O  O    . TYR   A 1 102 ? -11.140 15.995  -27.432 1.00 17.19  ? 102 TYR   A O    1 
ATOM   1504 C  CB   . TYR   A 1 102 ? -9.906  13.621  -29.283 1.00 17.06  ? 102 TYR   A CB   1 
ATOM   1505 C  CG   . TYR   A 1 102 ? -11.339 13.804  -29.759 1.00 17.23  ? 102 TYR   A CG   1 
ATOM   1506 C  CD1  . TYR   A 1 102 ? -11.654 14.765  -30.710 1.00 21.21  ? 102 TYR   A CD1  1 
ATOM   1507 C  CD2  . TYR   A 1 102 ? -12.374 13.041  -29.237 1.00 18.98  ? 102 TYR   A CD2  1 
ATOM   1508 C  CE1  . TYR   A 1 102 ? -12.955 14.949  -31.143 1.00 22.61  ? 102 TYR   A CE1  1 
ATOM   1509 C  CE2  . TYR   A 1 102 ? -13.680 13.211  -29.666 1.00 20.69  ? 102 TYR   A CE2  1 
ATOM   1510 C  CZ   . TYR   A 1 102 ? -13.969 14.168  -30.622 1.00 23.55  ? 102 TYR   A CZ   1 
ATOM   1511 O  OH   . TYR   A 1 102 ? -15.250 14.350  -31.051 1.00 33.40  ? 102 TYR   A OH   1 
ATOM   1512 H  H    . TYR   A 1 102 ? -7.684  13.761  -28.106 1.00 17.42  ? 102 TYR   A H    1 
ATOM   1513 H  HA   . TYR   A 1 102 ? -9.395  15.622  -29.112 1.00 18.16  ? 102 TYR   A HA   1 
ATOM   1514 H  HB2  . TYR   A 1 102 ? -9.325  13.470  -30.061 1.00 20.47  ? 102 TYR   A HB2  1 
ATOM   1515 H  HB3  . TYR   A 1 102 ? -9.858  12.830  -28.702 1.00 20.47  ? 102 TYR   A HB3  1 
ATOM   1516 H  HD1  . TYR   A 1 102 ? -10.967 15.301  -31.072 1.00 25.45  ? 102 TYR   A HD1  1 
ATOM   1517 H  HD2  . TYR   A 1 102 ? -12.183 12.382  -28.589 1.00 22.78  ? 102 TYR   A HD2  1 
ATOM   1518 H  HE1  . TYR   A 1 102 ? -13.149 15.601  -31.795 1.00 27.14  ? 102 TYR   A HE1  1 
ATOM   1519 H  HE2  . TYR   A 1 102 ? -14.369 12.679  -29.309 1.00 24.82  ? 102 TYR   A HE2  1 
ATOM   1520 H  HH   . TYR   A 1 102 ? -15.264 14.913  -31.698 1.00 40.08  ? 102 TYR   A HH   1 
ATOM   1521 N  N    . ALA   A 1 103 ? -10.136 14.369  -26.224 1.00 14.49  ? 103 ALA   A N    1 
ATOM   1522 C  CA   . ALA   A 1 103 ? -10.966 14.555  -25.014 1.00 15.28  ? 103 ALA   A CA   1 
ATOM   1523 C  C    . ALA   A 1 103 ? -10.840 16.008  -24.564 1.00 16.86  ? 103 ALA   A C    1 
ATOM   1524 O  O    . ALA   A 1 103 ? -11.870 16.609  -24.298 1.00 18.80  ? 103 ALA   A O    1 
ATOM   1525 C  CB   . ALA   A 1 103 ? -10.563 13.596  -23.919 1.00 16.46  ? 103 ALA   A CB   1 
ATOM   1526 H  H    . ALA   A 1 103 ? -9.514  13.721  -26.153 1.00 17.39  ? 103 ALA   A H    1 
ATOM   1527 H  HA   . ALA   A 1 103 ? -11.916 14.387  -25.260 1.00 18.33  ? 103 ALA   A HA   1 
ATOM   1528 H  HB1  . ALA   A 1 103 ? -11.078 13.782  -23.116 1.00 19.75  ? 103 ALA   A HB1  1 
ATOM   1529 H  HB2  . ALA   A 1 103 ? -10.733 12.683  -24.205 1.00 19.75  ? 103 ALA   A HB2  1 
ATOM   1530 H  HB3  . ALA   A 1 103 ? -9.616  13.702  -23.726 1.00 19.75  ? 103 ALA   A HB3  1 
ATOM   1531 N  N    . GLY   A 1 104 ? -9.625  16.555  -24.501 1.00 14.51  ? 104 GLY   A N    1 
ATOM   1532 C  CA   . GLY   A 1 104 ? -9.428  17.931  -24.056 1.00 14.96  ? 104 GLY   A CA   1 
ATOM   1533 C  C    . GLY   A 1 104 ? -10.117 18.909  -24.981 1.00 15.50  ? 104 GLY   A C    1 
ATOM   1534 O  O    . GLY   A 1 104 ? -10.689 19.890  -24.495 1.00 16.29  ? 104 GLY   A O    1 
ATOM   1535 H  H    . GLY   A 1 104 ? -8.907  16.133  -24.717 1.00 17.41  ? 104 GLY   A H    1 
ATOM   1536 H  HA2  . GLY   A 1 104 ? -9.791  18.039  -23.163 1.00 17.95  ? 104 GLY   A HA2  1 
ATOM   1537 H  HA3  . GLY   A 1 104 ? -8.480  18.135  -24.038 1.00 17.95  ? 104 GLY   A HA3  1 
ATOM   1538 N  N    . TYR   A 1 105 ? -10.094 18.660  -26.290 1.00 13.99  ? 105 TYR   A N    1 
ATOM   1539 C  CA   . TYR   A 1 105 ? -10.799 19.498  -27.236 1.00 16.46  ? 105 TYR   A CA   1 
ATOM   1540 C  C    . TYR   A 1 105 ? -12.286 19.528  -26.914 1.00 16.10  ? 105 TYR   A C    1 
ATOM   1541 O  O    . TYR   A 1 105 ? -12.894 20.618  -26.820 1.00 17.46  ? 105 TYR   A O    1 
ATOM   1542 C  CB   . TYR   A 1 105 ? -10.576 18.988  -28.679 1.00 18.45  ? 105 TYR   A CB   1 
ATOM   1543 C  CG   . TYR   A 1 105 ? -11.290 19.796  -29.723 1.00 22.28  ? 105 TYR   A CG   1 
ATOM   1544 C  CD1  . TYR   A 1 105 ? -12.647 19.588  -29.969 1.00 28.44  ? 105 TYR   A CD1  1 
ATOM   1545 C  CD2  . TYR   A 1 105 ? -10.640 20.803  -30.419 1.00 27.82  ? 105 TYR   A CD2  1 
ATOM   1546 C  CE1  . TYR   A 1 105 ? -13.338 20.379  -30.937 1.00 32.75  ? 105 TYR   A CE1  1 
ATOM   1547 C  CE2  . TYR   A 1 105 ? -11.304 21.586  -31.382 1.00 35.23  ? 105 TYR   A CE2  1 
ATOM   1548 C  CZ   . TYR   A 1 105 ? -12.646 21.371  -31.614 1.00 34.35  ? 105 TYR   A CZ   1 
ATOM   1549 O  OH   . TYR   A 1 105 ? -13.304 22.139  -32.561 1.00 57.06  ? 105 TYR   A OH   1 
ATOM   1550 H  H    . TYR   A 1 105 ? -9.671  18.005  -26.653 1.00 16.79  ? 105 TYR   A H    1 
ATOM   1551 H  HA   . TYR   A 1 105 ? -10.445 20.399  -27.179 1.00 19.76  ? 105 TYR   A HA   1 
ATOM   1552 H  HB2  . TYR   A 1 105 ? -9.627  19.021  -28.878 1.00 22.14  ? 105 TYR   A HB2  1 
ATOM   1553 H  HB3  . TYR   A 1 105 ? -10.897 18.075  -28.741 1.00 22.14  ? 105 TYR   A HB3  1 
ATOM   1554 H  HD1  . TYR   A 1 105 ? -13.106 18.930  -29.499 1.00 34.12  ? 105 TYR   A HD1  1 
ATOM   1555 H  HD2  . TYR   A 1 105 ? -9.742  20.966  -30.245 1.00 33.38  ? 105 TYR   A HD2  1 
ATOM   1556 H  HE1  . TYR   A 1 105 ? -14.239 20.230  -31.112 1.00 39.30  ? 105 TYR   A HE1  1 
ATOM   1557 H  HE2  . TYR   A 1 105 ? -10.843 22.240  -31.855 1.00 42.28  ? 105 TYR   A HE2  1 
ATOM   1558 H  HH   . TYR   A 1 105 ? -12.775 22.698  -32.896 1.00 68.47  ? 105 TYR   A HH   1 
ATOM   1559 N  N    . VAL   A 1 106 ? -12.887 18.373  -26.661 1.00 15.24  ? 106 VAL   A N    1 
ATOM   1560 C  CA   . VAL   A 1 106 ? -14.330 18.315  -26.490 1.00 15.90  ? 106 VAL   A CA   1 
ATOM   1561 C  C    . VAL   A 1 106 ? -14.713 19.032  -25.215 1.00 15.59  ? 106 VAL   A C    1 
ATOM   1562 O  O    . VAL   A 1 106 ? -15.698 19.794  -25.181 1.00 16.45  ? 106 VAL   A O    1 
ATOM   1563 C  CB   . VAL   A 1 106 ? -14.779 16.855  -26.477 1.00 16.87  ? 106 VAL   A CB   1 
ATOM   1564 C  CG1  . VAL   A 1 106 ? -16.273 16.791  -26.067 1.00 19.74  ? 106 VAL   A CG1  1 
ATOM   1565 C  CG2  . VAL   A 1 106 ? -14.587 16.189  -27.779 1.00 17.41  ? 106 VAL   A CG2  1 
ATOM   1566 H  H    . VAL   A 1 106 ? -12.486 17.616  -26.584 1.00 18.29  ? 106 VAL   A H    1 
ATOM   1567 H  HA   . VAL   A 1 106 ? -14.769 18.760  -27.231 1.00 19.08  ? 106 VAL   A HA   1 
ATOM   1568 H  HB   . VAL   A 1 106 ? -14.230 16.375  -25.837 1.00 20.25  ? 106 VAL   A HB   1 
ATOM   1569 H  HG11 . VAL   A 1 106 ? -16.601 15.889  -26.209 1.00 23.68  ? 106 VAL   A HG11 1 
ATOM   1570 H  HG12 . VAL   A 1 106 ? -16.353 17.027  -25.129 1.00 23.68  ? 106 VAL   A HG12 1 
ATOM   1571 H  HG13 . VAL   A 1 106 ? -16.777 17.416  -26.610 1.00 23.68  ? 106 VAL   A HG13 1 
ATOM   1572 H  HG21 . VAL   A 1 106 ? -14.908 15.276  -27.718 1.00 20.89  ? 106 VAL   A HG21 1 
ATOM   1573 H  HG22 . VAL   A 1 106 ? -15.087 16.670  -28.457 1.00 20.89  ? 106 VAL   A HG22 1 
ATOM   1574 H  HG23 . VAL   A 1 106 ? -13.642 16.193  -28.000 1.00 20.89  ? 106 VAL   A HG23 1 
ATOM   1575 N  N    . ILE   A 1 107 ? -13.977 18.836  -24.138 1.00 14.20  ? 107 ILE   A N    1 
ATOM   1576 C  CA   . ILE   A 1 107 ? -14.375 19.419  -22.859 1.00 14.43  ? 107 ILE   A CA   1 
ATOM   1577 C  C    . ILE   A 1 107 ? -14.229 20.924  -22.909 1.00 14.61  ? 107 ILE   A C    1 
ATOM   1578 O  O    . ILE   A 1 107 ? -15.119 21.646  -22.402 1.00 15.65  ? 107 ILE   A O    1 
ATOM   1579 C  CB   . ILE   A 1 107 ? -13.594 18.840  -21.663 1.00 15.64  ? 107 ILE   A CB   1 
ATOM   1580 C  CG1  . ILE   A 1 107 ? -13.647 17.321  -21.691 1.00 19.27  ? 107 ILE   A CG1  1 
ATOM   1581 C  CG2  . ILE   A 1 107 ? -14.137 19.415  -20.346 1.00 18.91  ? 107 ILE   A CG2  1 
ATOM   1582 C  CD1  . ILE   A 1 107 ? -15.024 16.752  -21.759 1.00 36.61  ? 107 ILE   A CD1  1 
ATOM   1583 H  H    . ILE   A 1 107 ? -13.251 18.375  -24.114 1.00 17.04  ? 107 ILE   A H    1 
ATOM   1584 H  HA   . ILE   A 1 107 ? -15.305 19.180  -22.726 1.00 17.31  ? 107 ILE   A HA   1 
ATOM   1585 H  HB   . ILE   A 1 107 ? -12.662 19.100  -21.732 1.00 18.77  ? 107 ILE   A HB   1 
ATOM   1586 H  HG12 . ILE   A 1 107 ? -13.162 17.008  -22.471 1.00 23.13  ? 107 ILE   A HG12 1 
ATOM   1587 H  HG13 . ILE   A 1 107 ? -13.229 16.982  -20.883 1.00 23.13  ? 107 ILE   A HG13 1 
ATOM   1588 H  HG21 . ILE   A 1 107 ? -13.627 19.048  -19.607 1.00 22.69  ? 107 ILE   A HG21 1 
ATOM   1589 H  HG22 . ILE   A 1 107 ? -14.047 20.381  -20.362 1.00 22.69  ? 107 ILE   A HG22 1 
ATOM   1590 H  HG23 . ILE   A 1 107 ? -15.072 19.171  -20.256 1.00 22.69  ? 107 ILE   A HG23 1 
ATOM   1591 H  HD11 . ILE   A 1 107 ? -14.966 15.784  -21.756 1.00 43.94  ? 107 ILE   A HD11 1 
ATOM   1592 H  HD12 . ILE   A 1 107 ? -15.529 17.056  -20.989 1.00 43.94  ? 107 ILE   A HD12 1 
ATOM   1593 H  HD13 . ILE   A 1 107 ? -15.451 17.056  -22.575 1.00 43.94  ? 107 ILE   A HD13 1 
ATOM   1594 N  N    . LYS   A 1 108 ? -13.145 21.426  -23.494 1.00 16.56  ? 108 LYS   A N    1 
ATOM   1595 C  CA   . LYS   A 1 108 ? -12.962 22.856  -23.695 1.00 16.91  ? 108 LYS   A CA   1 
ATOM   1596 C  C    . LYS   A 1 108 ? -14.145 23.399  -24.479 1.00 16.52  ? 108 LYS   A C    1 
ATOM   1597 O  O    . LYS   A 1 108 ? -14.729 24.449  -24.131 1.00 17.30  ? 108 LYS   A O    1 
ATOM   1598 C  CB   . LYS   A 1 108 ? -11.629 23.085  -24.397 1.00 19.67  ? 108 LYS   A CB   1 
ATOM   1599 C  CG   . LYS   A 1 108 ? -11.304 24.464  -24.933 1.00 28.59  ? 108 LYS   A CG   1 
ATOM   1600 C  CD   . LYS   A 1 108 ? -10.651 25.339  -23.871 1.00 36.35  ? 108 LYS   A CD   1 
ATOM   1601 C  CE   . LYS   A 1 108 ? -10.550 26.786  -24.342 1.00 34.40  ? 108 LYS   A CE   1 
ATOM   1602 N  NZ   . LYS   A 1 108 ? -11.915 27.449  -24.589 1.00 45.86  ? 108 LYS   A NZ   1 
ATOM   1603 H  H    . LYS   A 1 108 ? -12.491 20.952  -23.789 1.00 19.87  ? 108 LYS   A H    1 
ATOM   1604 H  HA   . LYS   A 1 108 ? -12.921 23.337  -22.854 1.00 20.29  ? 108 LYS   A HA   1 
ATOM   1605 H  HB2  . LYS   A 1 108 ? -10.927 22.865  -23.765 1.00 23.61  ? 108 LYS   A HB2  1 
ATOM   1606 H  HB3  . LYS   A 1 108 ? -11.593 22.482  -25.156 1.00 23.61  ? 108 LYS   A HB3  1 
ATOM   1607 H  HG2  . LYS   A 1 108 ? -10.690 24.382  -25.679 1.00 34.31  ? 108 LYS   A HG2  1 
ATOM   1608 H  HG3  . LYS   A 1 108 ? -12.122 24.897  -25.223 1.00 34.31  ? 108 LYS   A HG3  1 
ATOM   1609 H  HD2  . LYS   A 1 108 ? -11.185 25.317  -23.061 1.00 43.62  ? 108 LYS   A HD2  1 
ATOM   1610 H  HD3  . LYS   A 1 108 ? -9.757  25.013  -23.688 1.00 43.62  ? 108 LYS   A HD3  1 
ATOM   1611 H  HE2  . LYS   A 1 108 ? -10.087 27.304  -23.665 1.00 41.28  ? 108 LYS   A HE2  1 
ATOM   1612 H  HE3  . LYS   A 1 108 ? -10.053 26.811  -25.175 1.00 41.28  ? 108 LYS   A HE3  1 
ATOM   1613 H  HZ1  . LYS   A 1 108 ? -11.801 28.291  -24.852 1.00 55.04  ? 108 LYS   A HZ1  1 
ATOM   1614 H  HZ2  . LYS   A 1 108 ? -12.358 27.006  -25.221 1.00 55.04  ? 108 LYS   A HZ2  1 
ATOM   1615 H  HZ3  . LYS   A 1 108 ? -12.396 27.442  -23.841 1.00 55.04  ? 108 LYS   A HZ3  1 
ATOM   1616 N  N    . HIS   A 1 109 ? -14.492 22.752  -25.577 1.00 15.59  ? 109 HIS   A N    1 
ATOM   1617 C  CA   . HIS   A 1 109 ? -15.568 23.274  -26.417 1.00 16.98  ? 109 HIS   A CA   1 
ATOM   1618 C  C    . HIS   A 1 109 ? -16.940 23.177  -25.747 1.00 15.63  ? 109 HIS   A C    1 
ATOM   1619 O  O    . HIS   A 1 109 ? -17.791 24.035  -26.040 1.00 17.24  ? 109 HIS   A O    1 
ATOM   1620 C  CB   . HIS   A 1 109 ? -15.501 22.669  -27.823 1.00 17.45  ? 109 HIS   A CB   1 
ATOM   1621 C  CG   . HIS   A 1 109 ? -14.353 23.217  -28.607 1.00 20.22  ? 109 HIS   A CG   1 
ATOM   1622 N  ND1  . HIS   A 1 109 ? -14.508 24.095  -29.653 1.00 29.42  ? 109 HIS   A ND1  1 
ATOM   1623 C  CD2  . HIS   A 1 109 ? -13.018 23.097  -28.401 1.00 24.80  ? 109 HIS   A CD2  1 
ATOM   1624 C  CE1  . HIS   A 1 109 ? -13.310 24.429  -30.115 1.00 34.46  ? 109 HIS   A CE1  1 
ATOM   1625 N  NE2  . HIS   A 1 109 ? -12.390 23.856  -29.355 1.00 30.00  ? 109 HIS   A NE2  1 
ATOM   1626 H  H    . HIS   A 1 109 ? -14.131 22.024  -25.859 1.00 18.71  ? 109 HIS   A H    1 
ATOM   1627 H  HA   . HIS   A 1 109 ? -15.435 24.225  -26.552 1.00 20.37  ? 109 HIS   A HA   1 
ATOM   1628 H  HB2  . HIS   A 1 109 ? -15.390 21.708  -27.752 1.00 20.94  ? 109 HIS   A HB2  1 
ATOM   1629 H  HB3  . HIS   A 1 109 ? -16.320 22.875  -28.299 1.00 20.94  ? 109 HIS   A HB3  1 
ATOM   1630 H  HD2  . HIS   A 1 109 ? -12.605 22.593  -27.738 1.00 29.76  ? 109 HIS   A HD2  1 
ATOM   1631 H  HE1  . HIS   A 1 109 ? -13.145 24.974  -30.850 1.00 41.35  ? 109 HIS   A HE1  1 
ATOM   1632 H  HE2  . HIS   A 1 109 ? -11.539 23.945  -29.444 1.00 36.00  ? 109 HIS   A HE2  1 
ATOM   1633 N  N    . MET   A 1 110 ? -17.205 22.163  -24.938 1.00 14.81  ? 110 MET   A N    1 
ATOM   1634 C  CA   A MET   A 1 110 ? -18.480 22.093  -24.224 0.41 14.25  ? 110 MET   A CA   1 
ATOM   1635 C  CA   B MET   A 1 110 ? -18.483 22.101  -24.232 0.59 14.17  ? 110 MET   A CA   1 
ATOM   1636 C  C    . MET   A 1 110 ? -18.668 23.313  -23.341 1.00 14.94  ? 110 MET   A C    1 
ATOM   1637 O  O    . MET   A 1 110 ? -19.725 23.961  -23.361 1.00 15.13  ? 110 MET   A O    1 
ATOM   1638 C  CB   A MET   A 1 110 ? -18.525 20.837  -23.374 0.41 16.23  ? 110 MET   A CB   1 
ATOM   1639 C  CB   B MET   A 1 110 ? -18.516 20.819  -23.446 0.59 16.11  ? 110 MET   A CB   1 
ATOM   1640 C  CG   A MET   A 1 110 ? -19.911 20.623  -22.700 0.41 16.42  ? 110 MET   A CG   1 
ATOM   1641 C  CG   B MET   A 1 110 ? -19.868 20.606  -22.764 0.59 16.38  ? 110 MET   A CG   1 
ATOM   1642 S  SD   A MET   A 1 110 ? -20.218 21.439  -21.119 0.41 16.01  ? 110 MET   A SD   1 
ATOM   1643 S  SD   B MET   A 1 110 ? -19.840 19.262  -21.618 0.59 17.61  ? 110 MET   A SD   1 
ATOM   1644 C  CE   A MET   A 1 110 ? -19.075 20.505  -20.116 0.41 20.90  ? 110 MET   A CE   1 
ATOM   1645 C  CE   B MET   A 1 110 ? -18.912 19.995  -20.281 0.59 21.48  ? 110 MET   A CE   1 
ATOM   1646 H  H    A MET   A 1 110 ? -16.672 21.506  -24.782 0.41 17.78  ? 110 MET   A H    1 
ATOM   1647 H  H    B MET   A 1 110 ? -16.673 21.506  -24.779 0.59 17.78  ? 110 MET   A H    1 
ATOM   1648 H  HA   A MET   A 1 110 ? -19.197 22.050  -24.876 0.41 17.10  ? 110 MET   A HA   1 
ATOM   1649 H  HA   B MET   A 1 110 ? -19.219 22.091  -24.864 0.59 17.00  ? 110 MET   A HA   1 
ATOM   1650 H  HB2  A MET   A 1 110 ? -18.341 20.068  -23.936 0.41 19.48  ? 110 MET   A HB2  1 
ATOM   1651 H  HB2  B MET   A 1 110 ? -18.356 20.073  -24.045 0.59 19.34  ? 110 MET   A HB2  1 
ATOM   1652 H  HB3  A MET   A 1 110 ? -17.856 20.905  -22.675 0.41 19.48  ? 110 MET   A HB3  1 
ATOM   1653 H  HB3  B MET   A 1 110 ? -17.830 20.847  -22.760 0.59 19.34  ? 110 MET   A HB3  1 
ATOM   1654 H  HG2  A MET   A 1 110 ? -20.591 20.943  -23.313 0.41 19.70  ? 110 MET   A HG2  1 
ATOM   1655 H  HG2  B MET   A 1 110 ? -20.108 21.411  -22.279 0.59 19.66  ? 110 MET   A HG2  1 
ATOM   1656 H  HG3  A MET   A 1 110 ? -20.022 19.672  -22.547 0.41 19.70  ? 110 MET   A HG3  1 
ATOM   1657 H  HG3  B MET   A 1 110 ? -20.537 20.413  -23.439 0.59 19.66  ? 110 MET   A HG3  1 
ATOM   1658 H  HE1  A MET   A 1 110 ? -19.157 20.792  -19.193 0.41 25.08  ? 110 MET   A HE1  1 
ATOM   1659 H  HE1  B MET   A 1 110 ? -18.892 19.376  -19.534 0.59 25.78  ? 110 MET   A HE1  1 
ATOM   1660 H  HE2  A MET   A 1 110 ? -19.289 19.561  -20.189 0.41 25.08  ? 110 MET   A HE2  1 
ATOM   1661 H  HE2  B MET   A 1 110 ? -18.009 20.177  -20.585 0.59 25.78  ? 110 MET   A HE2  1 
ATOM   1662 H  HE3  A MET   A 1 110 ? -18.173 20.665  -20.434 0.41 25.08  ? 110 MET   A HE3  1 
ATOM   1663 H  HE3  B MET   A 1 110 ? -19.344 20.822  -20.013 0.59 25.78  ? 110 MET   A HE3  1 
ATOM   1664 N  N    . TYR   A 1 111 ? -17.684 23.614  -22.489 1.00 14.38  ? 111 TYR   A N    1 
ATOM   1665 C  CA   . TYR   A 1 111 ? -17.843 24.744  -21.587 1.00 14.32  ? 111 TYR   A CA   1 
ATOM   1666 C  C    . TYR   A 1 111 ? -17.965 26.036  -22.379 1.00 15.55  ? 111 TYR   A C    1 
ATOM   1667 O  O    . TYR   A 1 111 ? -18.732 26.921  -21.988 1.00 15.90  ? 111 TYR   A O    1 
ATOM   1668 C  CB   . TYR   A 1 111 ? -16.663 24.794  -20.609 1.00 15.12  ? 111 TYR   A CB   1 
ATOM   1669 C  CG   . TYR   A 1 111 ? -16.832 23.839  -19.427 1.00 13.47  ? 111 TYR   A CG   1 
ATOM   1670 C  CD1  . TYR   A 1 111 ? -17.765 24.067  -18.439 1.00 14.13  ? 111 TYR   A CD1  1 
ATOM   1671 C  CD2  . TYR   A 1 111 ? -16.085 22.693  -19.291 1.00 13.32  ? 111 TYR   A CD2  1 
ATOM   1672 C  CE1  . TYR   A 1 111 ? -17.932 23.201  -17.353 1.00 14.62  ? 111 TYR   A CE1  1 
ATOM   1673 C  CE2  . TYR   A 1 111 ? -16.237 21.822  -18.227 1.00 12.88  ? 111 TYR   A CE2  1 
ATOM   1674 C  CZ   . TYR   A 1 111 ? -17.164 22.105  -17.271 1.00 13.99  ? 111 TYR   A CZ   1 
ATOM   1675 O  OH   . TYR   A 1 111 ? -17.392 21.276  -16.189 1.00 15.95  ? 111 TYR   A OH   1 
ATOM   1676 H  H    . TYR   A 1 111 ? -16.939 23.190  -22.418 1.00 17.25  ? 111 TYR   A H    1 
ATOM   1677 H  HA   . TYR   A 1 111 ? -18.651 24.639  -21.060 1.00 17.19  ? 111 TYR   A HA   1 
ATOM   1678 H  HB2  . TYR   A 1 111 ? -15.852 24.548  -21.080 1.00 18.14  ? 111 TYR   A HB2  1 
ATOM   1679 H  HB3  . TYR   A 1 111 ? -16.583 25.694  -20.257 1.00 18.14  ? 111 TYR   A HB3  1 
ATOM   1680 H  HD1  . TYR   A 1 111 ? -18.303 24.824  -18.497 1.00 16.95  ? 111 TYR   A HD1  1 
ATOM   1681 H  HD2  . TYR   A 1 111 ? -15.451 22.495  -19.942 1.00 15.99  ? 111 TYR   A HD2  1 
ATOM   1682 H  HE1  . TYR   A 1 111 ? -18.567 23.383  -16.698 1.00 17.54  ? 111 TYR   A HE1  1 
ATOM   1683 H  HE2  . TYR   A 1 111 ? -15.714 21.055  -18.165 1.00 15.46  ? 111 TYR   A HE2  1 
ATOM   1684 H  HH   . TYR   A 1 111 ? -16.863 20.624  -16.210 1.00 19.14  ? 111 TYR   A HH   1 
ATOM   1685 N  N    . HIS   A 1 112 ? -17.247 26.180  -23.473 1.00 14.54  ? 112 HIS   A N    1 
ATOM   1686 C  CA   . HIS   A 1 112 ? -17.371 27.382  -24.273 1.00 16.46  ? 112 HIS   A CA   1 
ATOM   1687 C  C    . HIS   A 1 112 ? -18.727 27.470  -24.984 1.00 17.83  ? 112 HIS   A C    1 
ATOM   1688 O  O    . HIS   A 1 112 ? -19.415 28.494  -24.877 1.00 19.13  ? 112 HIS   A O    1 
ATOM   1689 C  CB   . HIS   A 1 112 ? -16.256 27.438  -25.310 1.00 19.25  ? 112 HIS   A CB   1 
ATOM   1690 C  CG   . HIS   A 1 112 ? -16.344 28.662  -26.174 1.00 23.51  ? 112 HIS   A CG   1 
ATOM   1691 N  ND1  . HIS   A 1 112 ? -16.932 28.674  -27.421 1.00 35.75  ? 112 HIS   A ND1  1 
ATOM   1692 C  CD2  . HIS   A 1 112 ? -16.006 29.942  -25.904 1.00 29.06  ? 112 HIS   A CD2  1 
ATOM   1693 C  CE1  . HIS   A 1 112 ? -16.894 29.907  -27.916 1.00 29.51  ? 112 HIS   A CE1  1 
ATOM   1694 N  NE2  . HIS   A 1 112 ? -16.339 30.694  -27.013 1.00 32.35  ? 112 HIS   A NE2  1 
ATOM   1695 H  H    . HIS   A 1 112 ? -16.684 25.604  -23.774 1.00 17.44  ? 112 HIS   A H    1 
ATOM   1696 H  HA   . HIS   A 1 112 ? -17.292 28.139  -23.672 1.00 19.75  ? 112 HIS   A HA   1 
ATOM   1697 H  HB2  . HIS   A 1 112 ? -15.399 27.450  -24.855 1.00 23.10  ? 112 HIS   A HB2  1 
ATOM   1698 H  HB3  . HIS   A 1 112 ? -16.316 26.658  -25.884 1.00 23.10  ? 112 HIS   A HB3  1 
ATOM   1699 H  HD1  . HIS   A 1 112 ? -17.271 27.990  -27.817 1.00 42.91  ? 112 HIS   A HD1  1 
ATOM   1700 H  HD2  . HIS   A 1 112 ? -15.621 30.257  -25.119 1.00 34.87  ? 112 HIS   A HD2  1 
ATOM   1701 H  HE1  . HIS   A 1 112 ? -17.204 30.169  -28.752 1.00 35.41  ? 112 HIS   A HE1  1 
ATOM   1702 N  N    . ASP   A 1 113 ? -19.138 26.410  -25.680 1.00 16.14  ? 113 ASP   A N    1 
ATOM   1703 C  CA   . ASP   A 1 113 ? -20.348 26.461  -26.482 1.00 16.90  ? 113 ASP   A CA   1 
ATOM   1704 C  C    . ASP   A 1 113 ? -21.595 26.512  -25.624 1.00 19.72  ? 113 ASP   A C    1 
ATOM   1705 O  O    . ASP   A 1 113 ? -22.537 27.189  -26.007 1.00 20.56  ? 113 ASP   A O    1 
ATOM   1706 C  CB   . ASP   A 1 113 ? -20.423 25.263  -27.414 1.00 18.11  ? 113 ASP   A CB   1 
ATOM   1707 C  CG   . ASP   A 1 113 ? -19.419 25.306  -28.546 1.00 23.83  ? 113 ASP   A CG   1 
ATOM   1708 O  OD1  . ASP   A 1 113 ? -18.802 26.358  -28.796 1.00 26.28  ? 113 ASP   A OD1  1 
ATOM   1709 O  OD2  . ASP   A 1 113 ? -19.221 24.211  -29.121 1.00 23.26  ? 113 ASP   A OD2  1 
ATOM   1710 H  H    . ASP   A 1 113 ? -18.731 25.652  -25.703 1.00 19.36  ? 113 ASP   A H    1 
ATOM   1711 H  HA   . ASP   A 1 113 ? -20.310 27.269  -27.018 1.00 20.27  ? 113 ASP   A HA   1 
ATOM   1712 H  HB2  . ASP   A 1 113 ? -20.256 24.457  -26.901 1.00 21.73  ? 113 ASP   A HB2  1 
ATOM   1713 H  HB3  . ASP   A 1 113 ? -21.310 25.228  -27.807 1.00 21.73  ? 113 ASP   A HB3  1 
ATOM   1714 N  N    . TRP   A 1 114 ? -21.650 25.793  -24.520 1.00 16.15  ? 114 TRP   A N    1 
ATOM   1715 C  CA   . TRP   A 1 114 ? -22.859 25.780  -23.706 1.00 15.94  ? 114 TRP   A CA   1 
ATOM   1716 C  C    . TRP   A 1 114 ? -22.928 26.905  -22.696 1.00 18.30  ? 114 TRP   A C    1 
ATOM   1717 O  O    . TRP   A 1 114 ? -24.040 27.316  -22.355 1.00 18.31  ? 114 TRP   A O    1 
ATOM   1718 C  CB   . TRP   A 1 114 ? -22.985 24.486  -22.947 1.00 16.33  ? 114 TRP   A CB   1 
ATOM   1719 C  CG   . TRP   A 1 114 ? -23.517 23.351  -23.794 1.00 15.48  ? 114 TRP   A CG   1 
ATOM   1720 C  CD1  . TRP   A 1 114 ? -23.786 23.347  -25.123 1.00 19.36  ? 114 TRP   A CD1  1 
ATOM   1721 C  CD2  . TRP   A 1 114 ? -23.796 22.055  -23.289 1.00 14.85  ? 114 TRP   A CD2  1 
ATOM   1722 N  NE1  . TRP   A 1 114 ? -24.251 22.108  -25.485 1.00 17.53  ? 114 TRP   A NE1  1 
ATOM   1723 C  CE2  . TRP   A 1 114 ? -24.268 21.297  -24.374 1.00 17.07  ? 114 TRP   A CE2  1 
ATOM   1724 C  CE3  . TRP   A 1 114 ? -23.694 21.453  -22.042 1.00 16.88  ? 114 TRP   A CE3  1 
ATOM   1725 C  CZ2  . TRP   A 1 114 ? -24.660 19.965  -24.217 1.00 19.20  ? 114 TRP   A CZ2  1 
ATOM   1726 C  CZ3  . TRP   A 1 114 ? -24.107 20.137  -21.912 1.00 19.40  ? 114 TRP   A CZ3  1 
ATOM   1727 C  CH2  . TRP   A 1 114 ? -24.538 19.401  -22.991 1.00 20.15  ? 114 TRP   A CH2  1 
ATOM   1728 H  H    . TRP   A 1 114 ? -21.008 25.307  -24.218 1.00 19.38  ? 114 TRP   A H    1 
ATOM   1729 H  HA   . TRP   A 1 114 ? -23.607 25.862  -24.318 1.00 19.12  ? 114 TRP   A HA   1 
ATOM   1730 H  HB2  . TRP   A 1 114 ? -22.110 24.228  -22.617 1.00 19.59  ? 114 TRP   A HB2  1 
ATOM   1731 H  HB3  . TRP   A 1 114 ? -23.595 24.616  -22.203 1.00 19.59  ? 114 TRP   A HB3  1 
ATOM   1732 H  HD1  . TRP   A 1 114 ? -23.673 24.069  -25.698 1.00 23.23  ? 114 TRP   A HD1  1 
ATOM   1733 H  HE1  . TRP   A 1 114 ? -24.492 21.876  -26.277 1.00 21.03  ? 114 TRP   A HE1  1 
ATOM   1734 H  HE3  . TRP   A 1 114 ? -23.357 21.922  -21.312 1.00 20.25  ? 114 TRP   A HE3  1 
ATOM   1735 H  HZ2  . TRP   A 1 114 ? -24.996 19.479  -24.935 1.00 23.03  ? 114 TRP   A HZ2  1 
ATOM   1736 H  HZ3  . TRP   A 1 114 ? -24.093 19.741  -21.071 1.00 23.29  ? 114 TRP   A HZ3  1 
ATOM   1737 H  HH2  . TRP   A 1 114 ? -24.749 18.502  -22.878 1.00 24.18  ? 114 TRP   A HH2  1 
ATOM   1738 N  N    . TYR   A 1 115 ? -21.786 27.391  -22.202 1.00 16.15  ? 115 TYR   A N    1 
ATOM   1739 C  CA   . TYR   A 1 115 ? -21.749 28.357  -21.090 1.00 17.69  ? 115 TYR   A CA   1 
ATOM   1740 C  C    . TYR   A 1 115 ? -20.944 29.608  -21.363 1.00 20.20  ? 115 TYR   A C    1 
ATOM   1741 O  O    . TYR   A 1 115 ? -20.987 30.537  -20.534 1.00 21.62  ? 115 TYR   A O    1 
ATOM   1742 C  CB   . TYR   A 1 115 ? -21.259 27.677  -19.794 1.00 16.52  ? 115 TYR   A CB   1 
ATOM   1743 C  CG   . TYR   A 1 115 ? -22.180 26.557  -19.456 1.00 16.78  ? 115 TYR   A CG   1 
ATOM   1744 C  CD1  . TYR   A 1 115 ? -23.505 26.806  -19.064 1.00 18.11  ? 115 TYR   A CD1  1 
ATOM   1745 C  CD2  . TYR   A 1 115 ? -21.812 25.249  -19.597 1.00 15.45  ? 115 TYR   A CD2  1 
ATOM   1746 C  CE1  . TYR   A 1 115 ? -24.374 25.781  -18.846 1.00 17.48  ? 115 TYR   A CE1  1 
ATOM   1747 C  CE2  . TYR   A 1 115 ? -22.699 24.209  -19.376 1.00 14.70  ? 115 TYR   A CE2  1 
ATOM   1748 C  CZ   . TYR   A 1 115 ? -23.999 24.507  -19.026 1.00 14.95  ? 115 TYR   A CZ   1 
ATOM   1749 O  OH   . TYR   A 1 115 ? -24.895 23.477  -18.887 1.00 16.14  ? 115 TYR   A OH   1 
ATOM   1750 H  H    . TYR   A 1 115 ? -21.006 27.176  -22.494 1.00 19.38  ? 115 TYR   A H    1 
ATOM   1751 H  HA   . TYR   A 1 115 ? -22.655 28.659  -20.919 1.00 21.23  ? 115 TYR   A HA   1 
ATOM   1752 H  HB2  . TYR   A 1 115 ? -20.365 27.323  -19.925 1.00 19.82  ? 115 TYR   A HB2  1 
ATOM   1753 H  HB3  . TYR   A 1 115 ? -21.259 28.317  -19.065 1.00 19.82  ? 115 TYR   A HB3  1 
ATOM   1754 H  HD1  . TYR   A 1 115 ? -23.794 27.683  -18.953 1.00 21.73  ? 115 TYR   A HD1  1 
ATOM   1755 H  HD2  . TYR   A 1 115 ? -20.939 25.050  -19.850 1.00 18.54  ? 115 TYR   A HD2  1 
ATOM   1756 H  HE1  . TYR   A 1 115 ? -25.241 25.967  -18.567 1.00 20.97  ? 115 TYR   A HE1  1 
ATOM   1757 H  HE2  . TYR   A 1 115 ? -22.423 23.325  -19.462 1.00 17.64  ? 115 TYR   A HE2  1 
ATOM   1758 H  HH   . TYR   A 1 115 ? -25.658 23.782  -18.711 1.00 19.37  ? 115 TYR   A HH   1 
ATOM   1759 N  N    . GLY   A 1 116 ? -20.207 29.677  -22.461 1.00 17.49  ? 116 GLY   A N    1 
ATOM   1760 C  CA   . GLY   A 1 116 ? -19.375 30.825  -22.755 1.00 19.87  ? 116 GLY   A CA   1 
ATOM   1761 C  C    . GLY   A 1 116 ? -18.262 31.045  -21.763 1.00 22.11  ? 116 GLY   A C    1 
ATOM   1762 O  O    . GLY   A 1 116 ? -17.790 32.188  -21.630 1.00 27.08  ? 116 GLY   A O    1 
ATOM   1763 H  H    . GLY   A 1 116 ? -20.171 29.061  -23.060 1.00 20.99  ? 116 GLY   A H    1 
ATOM   1764 H  HA2  . GLY   A 1 116 ? -18.976 30.708  -23.632 1.00 23.85  ? 116 GLY   A HA2  1 
ATOM   1765 H  HA3  . GLY   A 1 116 ? -19.930 31.621  -22.764 1.00 23.85  ? 116 GLY   A HA3  1 
ATOM   1766 N  N    . VAL   A 1 117 ? -17.731 29.985  -21.185 1.00 20.62  ? 117 VAL   A N    1 
ATOM   1767 C  CA   . VAL   A 1 117 ? -16.659 30.095  -20.189 1.00 23.23  ? 117 VAL   A CA   1 
ATOM   1768 C  C    . VAL   A 1 117 ? -15.502 29.160  -20.547 1.00 21.68  ? 117 VAL   A C    1 
ATOM   1769 O  O    . VAL   A 1 117 ? -15.655 28.170  -21.263 1.00 18.80  ? 117 VAL   A O    1 
ATOM   1770 C  CB   . VAL   A 1 117 ? -17.119 29.802  -18.758 1.00 22.92  ? 117 VAL   A CB   1 
ATOM   1771 C  CG1  . VAL   A 1 117 ? -18.176 30.858  -18.335 1.00 31.25  ? 117 VAL   A CG1  1 
ATOM   1772 C  CG2  . VAL   A 1 117 ? -17.594 28.432  -18.604 1.00 20.74  ? 117 VAL   A CG2  1 
ATOM   1773 H  H    . VAL   A 1 117 ? -17.971 29.176  -21.349 1.00 24.74  ? 117 VAL   A H    1 
ATOM   1774 H  HA   . VAL   A 1 117 ? -16.337 31.009  -20.230 1.00 27.87  ? 117 VAL   A HA   1 
ATOM   1775 H  HB   . VAL   A 1 117 ? -16.363 29.873  -18.154 1.00 27.50  ? 117 VAL   A HB   1 
ATOM   1776 H  HG11 . VAL   A 1 117 ? -18.467 30.669  -17.429 1.00 37.50  ? 117 VAL   A HG11 1 
ATOM   1777 H  HG12 . VAL   A 1 117 ? -17.775 31.740  -18.376 1.00 37.50  ? 117 VAL   A HG12 1 
ATOM   1778 H  HG13 . VAL   A 1 117 ? -18.931 30.809  -18.941 1.00 37.50  ? 117 VAL   A HG13 1 
ATOM   1779 H  HG21 . VAL   A 1 117 ? -17.871 28.295  -17.684 1.00 24.89  ? 117 VAL   A HG21 1 
ATOM   1780 H  HG22 . VAL   A 1 117 ? -18.346 28.289  -19.200 1.00 24.89  ? 117 VAL   A HG22 1 
ATOM   1781 H  HG23 . VAL   A 1 117 ? -16.874 27.821  -18.827 1.00 24.89  ? 117 VAL   A HG23 1 
ATOM   1782 N  N    . GLU   A 1 118 ? -14.329 29.507  -20.022 1.00 20.24  ? 118 GLU   A N    1 
ATOM   1783 C  CA   . GLU   A 1 118 ? -13.159 28.646  -20.072 1.00 21.41  ? 118 GLU   A CA   1 
ATOM   1784 C  C    . GLU   A 1 118 ? -13.316 27.459  -19.125 1.00 17.74  ? 118 GLU   A C    1 
ATOM   1785 O  O    . GLU   A 1 118 ? -13.785 27.567  -17.983 1.00 19.98  ? 118 GLU   A O    1 
ATOM   1786 C  CB   . GLU   A 1 118 ? -11.937 29.468  -19.623 1.00 21.35  ? 118 GLU   A CB   1 
ATOM   1787 C  CG   . GLU   A 1 118 ? -11.543 30.521  -20.616 1.00 25.60  ? 118 GLU   A CG   1 
ATOM   1788 C  CD   . GLU   A 1 118 ? -10.988 29.969  -21.897 1.00 32.40  ? 118 GLU   A CD   1 
ATOM   1789 O  OE1  . GLU   A 1 118 ? -10.613 28.807  -21.926 1.00 32.84  ? 118 GLU   A OE1  1 
ATOM   1790 O  OE2  . GLU   A 1 118 ? -10.915 30.707  -22.919 1.00 44.58  ? 118 GLU   A OE2  1 
ATOM   1791 H  H    . GLU   A 1 118 ? -14.183 30.255  -19.622 1.00 24.29  ? 118 GLU   A H    1 
ATOM   1792 H  HA   . GLU   A 1 118 ? -13.036 28.307  -20.972 1.00 25.69  ? 118 GLU   A HA   1 
ATOM   1793 H  HB2  . GLU   A 1 118 ? -12.145 29.910  -18.785 1.00 25.62  ? 118 GLU   A HB2  1 
ATOM   1794 H  HB3  . GLU   A 1 118 ? -11.182 28.871  -19.505 1.00 25.62  ? 118 GLU   A HB3  1 
ATOM   1795 H  HG2  . GLU   A 1 118 ? -12.326 31.050  -20.837 1.00 30.71  ? 118 GLU   A HG2  1 
ATOM   1796 H  HG3  . GLU   A 1 118 ? -10.862 31.086  -20.218 1.00 30.71  ? 118 GLU   A HG3  1 
ATOM   1797 N  N    . ALA   A 1 119 ? -12.912 26.267  -19.587 1.00 15.53  ? 119 ALA   A N    1 
ATOM   1798 C  CA   . ALA   A 1 119 ? -12.867 25.111  -18.710 1.00 13.87  ? 119 ALA   A CA   1 
ATOM   1799 C  C    . ALA   A 1 119 ? -11.893 25.347  -17.543 1.00 14.70  ? 119 ALA   A C    1 
ATOM   1800 O  O    . ALA   A 1 119 ? -12.201 25.013  -16.402 1.00 14.76  ? 119 ALA   A O    1 
ATOM   1801 C  CB   . ALA   A 1 119 ? -12.495 23.833  -19.487 1.00 15.98  ? 119 ALA   A CB   1 
ATOM   1802 H  H    . ALA   A 1 119 ? -12.663 26.112  -20.395 1.00 18.63  ? 119 ALA   A H    1 
ATOM   1803 H  HA   . ALA   A 1 119 ? -13.755 24.970  -18.347 1.00 16.65  ? 119 ALA   A HA   1 
ATOM   1804 H  HB1  . ALA   A 1 119 ? -12.494 23.081  -18.875 1.00 19.18  ? 119 ALA   A HB1  1 
ATOM   1805 H  HB2  . ALA   A 1 119 ? -13.149 23.688  -20.188 1.00 19.18  ? 119 ALA   A HB2  1 
ATOM   1806 H  HB3  . ALA   A 1 119 ? -11.613 23.945  -19.875 1.00 19.18  ? 119 ALA   A HB3  1 
ATOM   1807 N  N    . LEU   A 1 120 ? -10.716 25.910  -17.837 1.00 14.84  ? 120 LEU   A N    1 
ATOM   1808 C  CA   . LEU   A 1 120 ? -9.697  26.170  -16.842 1.00 14.83  ? 120 LEU   A CA   1 
ATOM   1809 C  C    . LEU   A 1 120 ? -9.124  27.549  -17.059 1.00 14.82  ? 120 LEU   A C    1 
ATOM   1810 O  O    . LEU   A 1 120 ? -8.894  27.951  -18.212 1.00 16.06  ? 120 LEU   A O    1 
ATOM   1811 C  CB   . LEU   A 1 120 ? -8.538  25.158  -16.931 1.00 13.93  ? 120 LEU   A CB   1 
ATOM   1812 C  CG   . LEU   A 1 120 ? -8.896  23.725  -16.661 1.00 14.68  ? 120 LEU   A CG   1 
ATOM   1813 C  CD1  . LEU   A 1 120 ? -7.639  22.831  -16.827 1.00 17.00  ? 120 LEU   A CD1  1 
ATOM   1814 C  CD2  . LEU   A 1 120 ? -9.448  23.444  -15.290 1.00 16.00  ? 120 LEU   A CD2  1 
ATOM   1815 H  H    . LEU   A 1 120 ? -10.488 26.153  -18.630 1.00 17.80  ? 120 LEU   A H    1 
ATOM   1816 H  HA   . LEU   A 1 120 ? -10.104 26.118  -15.963 1.00 17.80  ? 120 LEU   A HA   1 
ATOM   1817 H  HB2  . LEU   A 1 120 ? -8.169  25.198  -17.827 1.00 16.72  ? 120 LEU   A HB2  1 
ATOM   1818 H  HB3  . LEU   A 1 120 ? -7.863  25.412  -16.283 1.00 16.72  ? 120 LEU   A HB3  1 
ATOM   1819 H  HG   . LEU   A 1 120 ? -9.597  23.518  -17.299 1.00 17.62  ? 120 LEU   A HG   1 
ATOM   1820 H  HD11 . LEU   A 1 120 ? -7.871  21.916  -16.606 1.00 20.39  ? 120 LEU   A HD11 1 
ATOM   1821 H  HD12 . LEU   A 1 120 ? -7.335  22.882  -17.747 1.00 20.39  ? 120 LEU   A HD12 1 
ATOM   1822 H  HD13 . LEU   A 1 120 ? -6.944  23.150  -16.230 1.00 20.39  ? 120 LEU   A HD13 1 
ATOM   1823 H  HD21 . LEU   A 1 120 ? -9.611  22.492  -15.204 1.00 19.20  ? 120 LEU   A HD21 1 
ATOM   1824 H  HD22 . LEU   A 1 120 ? -8.803  23.731  -14.625 1.00 19.20  ? 120 LEU   A HD22 1 
ATOM   1825 H  HD23 . LEU   A 1 120 ? -10.278 23.933  -15.177 1.00 19.20  ? 120 LEU   A HD23 1 
ATOM   1826 N  N    . THR   A 1 121 ? -8.805  28.252  -15.963 1.00 15.55  ? 121 THR   A N    1 
ATOM   1827 C  CA   A THR   A 1 121 ? -8.194  29.571  -16.070 0.56 18.13  ? 121 THR   A CA   1 
ATOM   1828 C  CA   B THR   A 1 121 ? -8.205  29.575  -16.064 0.44 18.18  ? 121 THR   A CA   1 
ATOM   1829 C  C    . THR   A 1 121 ? -7.065  29.669  -15.060 1.00 17.38  ? 121 THR   A C    1 
ATOM   1830 O  O    . THR   A 1 121 ? -7.118  29.047  -13.996 1.00 18.74  ? 121 THR   A O    1 
ATOM   1831 C  CB   A THR   A 1 121 ? -9.188  30.721  -15.796 0.56 22.92  ? 121 THR   A CB   1 
ATOM   1832 C  CB   B THR   A 1 121 ? -9.285  30.640  -15.734 0.44 22.86  ? 121 THR   A CB   1 
ATOM   1833 O  OG1  A THR   A 1 121 ? -9.690  30.647  -14.464 0.56 23.22  ? 121 THR   A OG1  1 
ATOM   1834 O  OG1  B THR   A 1 121 ? -10.159 30.809  -16.864 0.44 26.01  ? 121 THR   A OG1  1 
ATOM   1835 C  CG2  A THR   A 1 121 ? -10.399 30.637  -16.726 0.56 25.38  ? 121 THR   A CG2  1 
ATOM   1836 C  CG2  B THR   A 1 121 ? -8.702  31.981  -15.403 0.44 25.43  ? 121 THR   A CG2  1 
ATOM   1837 H  HA   . THR   A 1 121 ? -7.850  29.675  -16.971 1.00 21.82  ? 121 THR   A HA   1 
ATOM   1838 H  HB   A THR   A 1 121 ? -8.714  31.556  -15.938 0.56 27.51  ? 121 THR   A HB   1 
ATOM   1839 H  HB   B THR   A 1 121 ? -9.770  30.325  -14.956 0.44 27.43  ? 121 THR   A HB   1 
ATOM   1840 H  HG1  A THR   A 1 121 ? -10.052 29.900  -14.335 0.56 27.87  ? 121 THR   A HG1  1 
ATOM   1841 H  HG1  B THR   A 1 121 ? -10.447 30.062  -17.119 0.44 31.21  ? 121 THR   A HG1  1 
ATOM   1842 H  HG21 A THR   A 1 121 ? -11.058 31.302  -16.473 0.56 30.46  ? 121 THR   A HG21 1 
ATOM   1843 H  HG21 B THR   A 1 121 ? -8.404  31.994  -14.479 0.44 30.51  ? 121 THR   A HG21 1 
ATOM   1844 H  HG22 A THR   A 1 121 ? -10.125 30.798  -17.642 0.56 30.46  ? 121 THR   A HG22 1 
ATOM   1845 H  HG22 B THR   A 1 121 ? -7.944  32.165  -15.980 0.44 30.51  ? 121 THR   A HG22 1 
ATOM   1846 H  HG23 A THR   A 1 121 ? -10.801 29.756  -16.667 0.56 30.46  ? 121 THR   A HG23 1 
ATOM   1847 H  HG23 B THR   A 1 121 ? -9.369  32.673  -15.529 0.44 30.51  ? 121 THR   A HG23 1 
ATOM   1848 N  N    . LYS   A 1 122 ? -6.051  30.442  -15.389 1.00 18.71  ? 122 LYS   A N    1 
ATOM   1849 C  CA   . LYS   A 1 122 ? -4.946  30.696  -14.480 1.00 20.62  ? 122 LYS   A CA   1 
ATOM   1850 C  C    . LYS   A 1 122 ? -5.372  31.696  -13.415 1.00 21.44  ? 122 LYS   A C    1 
ATOM   1851 O  O    . LYS   A 1 122 ? -6.335  32.418  -13.573 1.00 22.19  ? 122 LYS   A O    1 
ATOM   1852 C  CB   . LYS   A 1 122 ? -3.754  31.294  -15.228 1.00 24.20  ? 122 LYS   A CB   1 
ATOM   1853 C  CG   . LYS   A 1 122 ? -3.353  30.522  -16.458 1.00 26.28  ? 122 LYS   A CG   1 
ATOM   1854 C  CD   . LYS   A 1 122 ? -2.237  31.226  -17.268 1.00 33.11  ? 122 LYS   A CD   1 
ATOM   1855 C  CE   . LYS   A 1 122 ? -1.279  30.251  -17.919 1.00 39.87  ? 122 LYS   A CE   1 
ATOM   1856 N  NZ   . LYS   A 1 122 ? -0.326  30.988  -18.835 1.00 53.15  ? 122 LYS   A NZ   1 
ATOM   1857 H  H    . LYS   A 1 122 ? -5.973  30.840  -16.147 1.00 22.45  ? 122 LYS   A H    1 
ATOM   1858 H  HA   . LYS   A 1 122 ? -4.686  29.855  -14.073 1.00 24.75  ? 122 LYS   A HA   1 
ATOM   1859 H  HB2  . LYS   A 1 122 ? -3.981  32.195  -15.506 1.00 29.04  ? 122 LYS   A HB2  1 
ATOM   1860 H  HB3  . LYS   A 1 122 ? -2.990  31.313  -14.630 1.00 29.04  ? 122 LYS   A HB3  1 
ATOM   1861 H  HG2  . LYS   A 1 122 ? -3.024  29.649  -16.191 1.00 31.53  ? 122 LYS   A HG2  1 
ATOM   1862 H  HG3  . LYS   A 1 122 ? -4.126  30.423  -17.036 1.00 31.53  ? 122 LYS   A HG3  1 
ATOM   1863 H  HD2  . LYS   A 1 122 ? -2.644  31.759  -17.970 1.00 39.73  ? 122 LYS   A HD2  1 
ATOM   1864 H  HD3  . LYS   A 1 122 ? -1.726  31.796  -16.673 1.00 39.73  ? 122 LYS   A HD3  1 
ATOM   1865 H  HE2  . LYS   A 1 122 ? -0.764  29.796  -17.235 1.00 47.85  ? 122 LYS   A HE2  1 
ATOM   1866 H  HE3  . LYS   A 1 122 ? -1.777  29.606  -18.444 1.00 47.85  ? 122 LYS   A HE3  1 
ATOM   1867 H  HZ1  . LYS   A 1 122 ? 0.237   30.413  -19.214 1.00 63.78  ? 122 LYS   A HZ1  1 
ATOM   1868 H  HZ2  . LYS   A 1 122 ? -0.781  31.411  -19.472 1.00 63.78  ? 122 LYS   A HZ2  1 
ATOM   1869 H  HZ3  . LYS   A 1 122 ? 0.142   31.586  -18.370 1.00 63.78  ? 122 LYS   A HZ3  1 
ATOM   1870 N  N    . SER   A 1 123 ? -4.566  31.796  -12.337 1.00 24.30  ? 123 SER   A N    1 
ATOM   1871 C  CA   . SER   A 1 123 ? -4.837  32.743  -11.266 1.00 28.47  ? 123 SER   A CA   1 
ATOM   1872 C  C    . SER   A 1 123 ? -4.844  34.177  -11.769 1.00 28.39  ? 123 SER   A C    1 
ATOM   1873 O  O    . SER   A 1 123 ? -5.617  34.995  -11.268 1.00 35.55  ? 123 SER   A O    1 
ATOM   1874 C  CB   . SER   A 1 123 ? -3.748  32.578  -10.192 1.00 37.59  ? 123 SER   A CB   1 
ATOM   1875 O  OG   . SER   A 1 123 ? -3.633  31.220  -9.803  1.00 50.54  ? 123 SER   A OG   1 
ATOM   1876 H  H    . SER   A 1 123 ? -3.859  31.323  -12.212 1.00 29.16  ? 123 SER   A H    1 
ATOM   1877 H  HA   . SER   A 1 123 ? -5.709  32.560  -10.883 1.00 34.16  ? 123 SER   A HA   1 
ATOM   1878 H  HB2  . SER   A 1 123 ? -2.899  32.877  -10.554 1.00 45.11  ? 123 SER   A HB2  1 
ATOM   1879 H  HB3  . SER   A 1 123 ? -3.984  33.111  -9.417  1.00 45.11  ? 123 SER   A HB3  1 
ATOM   1880 H  HG   . SER   A 1 123 ? -3.027  31.136  -9.228  1.00 60.65  ? 123 SER   A HG   1 
ATOM   1881 N  N    . ASP   A 1 124 ? -4.055  34.462  -12.795 1.00 27.99  ? 124 ASP   A N    1 
ATOM   1882 C  CA   . ASP   A 1 124 ? -3.951  35.810  -13.358 1.00 33.21  ? 124 ASP   A CA   1 
ATOM   1883 C  C    . ASP   A 1 124 ? -5.110  36.152  -14.284 1.00 30.00  ? 124 ASP   A C    1 
ATOM   1884 O  O    . ASP   A 1 124 ? -5.095  37.259  -14.841 1.00 31.36  ? 124 ASP   A O    1 
ATOM   1885 C  CB   . ASP   A 1 124 ? -2.598  36.023  -14.084 1.00 34.11  ? 124 ASP   A CB   1 
ATOM   1886 C  CG   . ASP   A 1 124 ? -2.609  35.520  -15.540 1.00 35.68  ? 124 ASP   A CG   1 
ATOM   1887 O  OD1  . ASP   A 1 124 ? -3.391  34.638  -15.856 1.00 36.23  ? 124 ASP   A OD1  1 
ATOM   1888 O  OD2  . ASP   A 1 124 ? -1.818  35.990  -16.396 1.00 44.31  ? 124 ASP   A OD2  1 
ATOM   1889 H  H    . ASP   A 1 124 ? -3.557  33.885  -13.194 1.00 33.59  ? 124 ASP   A H    1 
ATOM   1890 H  HA   . ASP   A 1 124 ? -3.962  36.441  -12.622 1.00 39.86  ? 124 ASP   A HA   1 
ATOM   1891 H  HB2  . ASP   A 1 124 ? -2.394  36.971  -14.097 1.00 40.93  ? 124 ASP   A HB2  1 
ATOM   1892 H  HB3  . ASP   A 1 124 ? -1.905  35.540  -13.607 1.00 40.93  ? 124 ASP   A HB3  1 
ATOM   1893 N  N    . GLY   A 1 125 ? -6.032  35.212  -14.531 1.00 28.95  ? 125 GLY   A N    1 
ATOM   1894 C  CA   . GLY   A 1 125 ? -7.255  35.455  -15.278 1.00 32.13  ? 125 GLY   A CA   1 
ATOM   1895 C  C    . GLY   A 1 125 ? -7.287  34.856  -16.673 1.00 32.38  ? 125 GLY   A C    1 
ATOM   1896 O  O    . GLY   A 1 125 ? -8.381  34.604  -17.204 1.00 35.46  ? 125 GLY   A O    1 
ATOM   1897 H  H    . GLY   A 1 125 ? -5.961  34.399  -14.261 1.00 34.74  ? 125 GLY   A H    1 
ATOM   1898 H  HA2  . GLY   A 1 125 ? -8.001  35.084  -14.782 1.00 38.56  ? 125 GLY   A HA2  1 
ATOM   1899 H  HA3  . GLY   A 1 125 ? -7.379  36.413  -15.367 1.00 38.56  ? 125 GLY   A HA3  1 
ATOM   1900 N  N    . SER   A 1 126 ? -6.156  34.555  -17.231 1.00 30.37  ? 126 SER   A N    1 
ATOM   1901 C  CA   . SER   A 1 126 ? -6.103  34.083  -18.610 1.00 33.06  ? 126 SER   A CA   1 
ATOM   1902 C  C    . SER   A 1 126 ? -6.490  32.607  -18.761 1.00 31.02  ? 126 SER   A C    1 
ATOM   1903 O  O    . SER   A 1 126 ? -6.540  31.849  -17.794 1.00 25.55  ? 126 SER   A O    1 
ATOM   1904 C  CB   . SER   A 1 126 ? -4.694  34.303  -19.139 1.00 36.88  ? 126 SER   A CB   1 
ATOM   1905 O  OG   . SER   A 1 126 ? -3.729  33.647  -18.358 1.00 45.81  ? 126 SER   A OG   1 
ATOM   1906 H  H    . SER   A 1 126 ? -5.390  34.611  -16.844 1.00 36.45  ? 126 SER   A H    1 
ATOM   1907 H  HA   . SER   A 1 126 ? -6.746  34.582  -19.137 1.00 39.67  ? 126 SER   A HA   1 
ATOM   1908 H  HB2  . SER   A 1 126 ? -4.645  33.960  -20.045 1.00 44.26  ? 126 SER   A HB2  1 
ATOM   1909 H  HB3  . SER   A 1 126 ? -4.505  35.254  -19.133 1.00 44.26  ? 126 SER   A HB3  1 
ATOM   1910 H  HG   . SER   A 1 126 ? -2.963  33.781  -18.675 1.00 54.97  ? 126 SER   A HG   1 
ATOM   1911 N  N    . PRO   A 1 127 ? -6.816  32.150  -19.989 1.00 24.25  ? 127 PRO   A N    1 
ATOM   1912 C  CA   . PRO   A 1 127 ? -7.118  30.714  -20.241 1.00 22.94  ? 127 PRO   A CA   1 
ATOM   1913 C  C    . PRO   A 1 127 ? -5.947  29.852  -19.794 1.00 25.26  ? 127 PRO   A C    1 
ATOM   1914 O  O    . PRO   A 1 127 ? -4.781  30.265  -19.973 1.00 24.13  ? 127 PRO   A O    1 
ATOM   1915 C  CB   . PRO   A 1 127 ? -7.366  30.642  -21.743 1.00 24.75  ? 127 PRO   A CB   1 
ATOM   1916 C  CG   . PRO   A 1 127 ? -7.850  32.039  -22.078 1.00 30.73  ? 127 PRO   A CG   1 
ATOM   1917 C  CD   . PRO   A 1 127 ? -6.997  32.940  -21.249 1.00 29.04  ? 127 PRO   A CD   1 
ATOM   1918 H  HA   . PRO   A 1 127 ? -7.928  30.454  -19.754 1.00 27.53  ? 127 PRO   A HA   1 
ATOM   1919 H  HB2  . PRO   A 1 127 ? -6.542  30.432  -22.224 1.00 29.70  ? 127 PRO   A HB2  1 
ATOM   1920 H  HB3  . PRO   A 1 127 ? -8.045  29.973  -21.956 1.00 29.70  ? 127 PRO   A HB3  1 
ATOM   1921 H  HG2  . PRO   A 1 127 ? -7.734  32.231  -23.030 1.00 36.88  ? 127 PRO   A HG2  1 
ATOM   1922 H  HG3  . PRO   A 1 127 ? -8.793  32.147  -21.845 1.00 36.88  ? 127 PRO   A HG3  1 
ATOM   1923 H  HD2  . PRO   A 1 127 ? -6.137  33.112  -21.677 1.00 34.85  ? 127 PRO   A HD2  1 
ATOM   1924 H  HD3  . PRO   A 1 127 ? -7.445  33.788  -21.067 1.00 34.85  ? 127 PRO   A HD3  1 
ATOM   1925 N  N    . MET   A 1 128 ? -6.239  28.685  -19.225 1.00 19.62  ? 128 MET   A N    1 
ATOM   1926 C  CA   . MET   A 1 128 ? -5.192  27.751  -18.745 1.00 20.86  ? 128 MET   A CA   1 
ATOM   1927 C  C    . MET   A 1 128 ? -5.192  26.514  -19.651 1.00 15.43  ? 128 MET   A C    1 
ATOM   1928 O  O    . MET   A 1 128 ? -6.270  25.915  -19.834 1.00 17.67  ? 128 MET   A O    1 
ATOM   1929 C  CB   . MET   A 1 128 ? -5.467  27.361  -17.293 1.00 18.23  ? 128 MET   A CB   1 
ATOM   1930 C  CG   . MET   A 1 128 ? -4.562  26.283  -16.754 1.00 17.40  ? 128 MET   A CG   1 
ATOM   1931 S  SD   . MET   A 1 128 ? -4.787  26.109  -14.975 1.00 22.22  ? 128 MET   A SD   1 
ATOM   1932 C  CE   . MET   A 1 128 ? -3.766  24.654  -14.717 1.00 26.70  ? 128 MET   A CE   1 
ATOM   1933 H  H    . MET   A 1 128 ? -7.091  28.411  -19.121 1.00 23.55  ? 128 MET   A H    1 
ATOM   1934 H  HA   . MET   A 1 128 ? -4.309  28.194  -18.807 1.00 25.03  ? 128 MET   A HA   1 
ATOM   1935 H  HB2  . MET   A 1 128 ? -5.371  28.161  -16.734 1.00 21.88  ? 128 MET   A HB2  1 
ATOM   1936 H  HB3  . MET   A 1 128 ? -6.397  27.059  -17.222 1.00 21.88  ? 128 MET   A HB3  1 
ATOM   1937 H  HG2  . MET   A 1 128 ? -4.767  25.430  -17.187 1.00 20.89  ? 128 MET   A HG2  1 
ATOM   1938 H  HG3  . MET   A 1 128 ? -3.631  26.509  -16.941 1.00 20.89  ? 128 MET   A HG3  1 
ATOM   1939 H  HE1  . MET   A 1 128 ? -3.808  24.388  -13.779 1.00 32.05  ? 128 MET   A HE1  1 
ATOM   1940 H  HE2  . MET   A 1 128 ? -4.094  23.927  -15.278 1.00 32.05  ? 128 MET   A HE2  1 
ATOM   1941 H  HE3  . MET   A 1 128 ? -2.843  24.858  -14.958 1.00 32.05  ? 128 MET   A HE3  1 
ATOM   1942 N  N    . GLN   A 1 129 ? -4.028  26.147  -20.180 1.00 15.14  ? 129 GLN   A N    1 
ATOM   1943 C  CA   . GLN   A 1 129 ? -3.917  24.983  -21.091 1.00 15.81  ? 129 GLN   A CA   1 
ATOM   1944 C  C    . GLN   A 1 129 ? -4.255  23.695  -20.335 1.00 16.25  ? 129 GLN   A C    1 
ATOM   1945 O  O    . GLN   A 1 129 ? -3.805  23.554  -19.185 1.00 15.44  ? 129 GLN   A O    1 
ATOM   1946 C  CB   . GLN   A 1 129 ? -2.518  24.860  -21.691 1.00 15.88  ? 129 GLN   A CB   1 
ATOM   1947 C  CG   . GLN   A 1 129 ? -2.372  23.715  -22.688 1.00 16.75  ? 129 GLN   A CG   1 
ATOM   1948 C  CD   . GLN   A 1 129 ? -0.973  23.595  -23.248 1.00 19.97  ? 129 GLN   A CD   1 
ATOM   1949 O  OE1  . GLN   A 1 129 ? 0.005   23.466  -22.506 1.00 19.56  ? 129 GLN   A OE1  1 
ATOM   1950 N  NE2  . GLN   A 1 129 ? -0.865  23.644  -24.567 1.00 18.15  ? 129 GLN   A NE2  1 
ATOM   1951 H  H    . GLN   A 1 129 ? -3.263  26.580  -19.985 1.00 18.17  ? 129 GLN   A H    1 
ATOM   1952 H  HA   . GLN   A 1 129 ? -4.570  25.099  -21.827 1.00 18.98  ? 129 GLN   A HA   1 
ATOM   1953 H  HB2  . GLN   A 1 129 ? -2.293  25.701  -22.139 1.00 19.06  ? 129 GLN   A HB2  1 
ATOM   1954 H  HB3  . GLN   A 1 129 ? -1.877  24.729  -20.962 1.00 19.06  ? 129 GLN   A HB3  1 
ATOM   1955 H  HG2  . GLN   A 1 129 ? -2.606  22.869  -22.252 1.00 20.10  ? 129 GLN   A HG2  1 
ATOM   1956 H  HG3  . GLN   A 1 129 ? -2.999  23.851  -23.429 1.00 20.10  ? 129 GLN   A HG3  1 
ATOM   1957 H  HE21 . GLN   A 1 129 ? -1.593  23.723  -25.068 1.00 21.78  ? 129 GLN   A HE21 1 
ATOM   1958 H  HE22 . GLN   A 1 129 ? -0.066  23.594  -24.947 1.00 21.78  ? 129 GLN   A HE22 1 
ATOM   1959 N  N    . LEU   A 1 130 ? -5.031  22.810  -20.949 1.00 13.32  ? 130 LEU   A N    1 
ATOM   1960 C  CA   . LEU   A 1 130 ? -5.388  21.510  -20.400 1.00 12.73  ? 130 LEU   A CA   1 
ATOM   1961 C  C    . LEU   A 1 130 ? -4.200  20.584  -20.622 1.00 14.25  ? 130 LEU   A C    1 
ATOM   1962 O  O    . LEU   A 1 130 ? -3.867  20.309  -21.771 1.00 14.97  ? 130 LEU   A O    1 
ATOM   1963 C  CB   . LEU   A 1 130 ? -6.632  20.963  -21.091 1.00 13.26  ? 130 LEU   A CB   1 
ATOM   1964 C  CG   . LEU   A 1 130 ? -7.942  21.455  -20.617 1.00 14.77  ? 130 LEU   A CG   1 
ATOM   1965 C  CD1  . LEU   A 1 130 ? -8.173  22.865  -20.802 1.00 17.70  ? 130 LEU   A CD1  1 
ATOM   1966 C  CD2  . LEU   A 1 130 ? -9.093  20.602  -21.312 1.00 15.03  ? 130 LEU   A CD2  1 
ATOM   1967 H  H    . LEU   A 1 130 ? -5.368  22.938  -21.729 1.00 15.98  ? 130 LEU   A H    1 
ATOM   1968 H  HA   . LEU   A 1 130 ? -5.577  21.585  -19.451 1.00 15.27  ? 130 LEU   A HA   1 
ATOM   1969 H  HB2  . LEU   A 1 130 ? -6.571  21.187  -22.033 1.00 15.91  ? 130 LEU   A HB2  1 
ATOM   1970 H  HB3  . LEU   A 1 130 ? -6.635  20.000  -20.978 1.00 15.91  ? 130 LEU   A HB3  1 
ATOM   1971 H  HG   . LEU   A 1 130 ? -7.956  21.339  -19.654 1.00 17.72  ? 130 LEU   A HG   1 
ATOM   1972 H  HD11 . LEU   A 1 130 ? -9.069  23.080  -20.499 1.00 21.24  ? 130 LEU   A HD11 1 
ATOM   1973 H  HD12 . LEU   A 1 130 ? -7.521  23.362  -20.284 1.00 21.24  ? 130 LEU   A HD12 1 
ATOM   1974 H  HD13 . LEU   A 1 130 ? -8.081  23.080  -21.743 1.00 21.24  ? 130 LEU   A HD13 1 
ATOM   1975 H  HD21 . LEU   A 1 130 ? -9.955  20.916  -20.995 1.00 18.03  ? 130 LEU   A HD21 1 
ATOM   1976 H  HD22 . LEU   A 1 130 ? -9.033  20.715  -22.274 1.00 18.03  ? 130 LEU   A HD22 1 
ATOM   1977 H  HD23 . LEU   A 1 130 ? -8.977  19.667  -21.081 1.00 18.03  ? 130 LEU   A HD23 1 
ATOM   1978 N  N    . VAL   A 1 131 ? -3.546  20.129  -19.562 1.00 12.30  ? 131 VAL   A N    1 
ATOM   1979 C  CA   . VAL   A 1 131 ? -2.368  19.252  -19.638 1.00 12.24  ? 131 VAL   A CA   1 
ATOM   1980 C  C    . VAL   A 1 131 ? -2.823  17.855  -19.249 1.00 12.97  ? 131 VAL   A C    1 
ATOM   1981 O  O    . VAL   A 1 131 ? -3.272  17.619  -18.099 1.00 13.06  ? 131 VAL   A O    1 
ATOM   1982 C  CB   . VAL   A 1 131 ? -1.222  19.756  -18.753 1.00 13.74  ? 131 VAL   A CB   1 
ATOM   1983 C  CG1  . VAL   A 1 131 ? -0.089  18.768  -18.851 1.00 15.76  ? 131 VAL   A CG1  1 
ATOM   1984 C  CG2  . VAL   A 1 131 ? -0.821  21.175  -19.155 1.00 15.35  ? 131 VAL   A CG2  1 
ATOM   1985 H  H    . VAL   A 1 131 ? -3.769  20.318  -18.753 1.00 14.76  ? 131 VAL   A H    1 
ATOM   1986 H  HA   . VAL   A 1 131 ? -2.031  19.223  -20.547 1.00 14.69  ? 131 VAL   A HA   1 
ATOM   1987 H  HB   . VAL   A 1 131 ? -1.491  19.816  -17.822 1.00 16.49  ? 131 VAL   A HB   1 
ATOM   1988 H  HG11 . VAL   A 1 131 ? 0.682   19.124  -18.380 1.00 18.91  ? 131 VAL   A HG11 1 
ATOM   1989 H  HG12 . VAL   A 1 131 ? -0.364  17.930  -18.448 1.00 18.91  ? 131 VAL   A HG12 1 
ATOM   1990 H  HG13 . VAL   A 1 131 ? 0.130   18.630  -19.786 1.00 18.91  ? 131 VAL   A HG13 1 
ATOM   1991 H  HG21 . VAL   A 1 131 ? -0.080  21.463  -18.600 1.00 18.41  ? 131 VAL   A HG21 1 
ATOM   1992 H  HG22 . VAL   A 1 131 ? -0.556  21.176  -20.088 1.00 18.41  ? 131 VAL   A HG22 1 
ATOM   1993 H  HG23 . VAL   A 1 131 ? -1.580  21.766  -19.027 1.00 18.41  ? 131 VAL   A HG23 1 
ATOM   1994 N  N    . MET   A 1 132 ? -2.751  16.935  -20.192 1.00 11.89  ? 132 MET   A N    1 
ATOM   1995 C  CA   . MET   A 1 132 ? -3.231  15.566  -20.064 1.00 12.21  ? 132 MET   A CA   1 
ATOM   1996 C  C    . MET   A 1 132 ? -2.022  14.652  -19.978 1.00 12.40  ? 132 MET   A C    1 
ATOM   1997 O  O    . MET   A 1 132 ? -1.325  14.465  -20.984 1.00 13.23  ? 132 MET   A O    1 
ATOM   1998 C  CB   . MET   A 1 132 ? -4.130  15.156  -21.245 1.00 14.44  ? 132 MET   A CB   1 
ATOM   1999 C  CG   . MET   A 1 132 ? -5.136  16.194  -21.660 1.00 14.84  ? 132 MET   A CG   1 
ATOM   2000 S  SD   . MET   A 1 132 ? -6.575  16.285  -20.540 1.00 16.30  ? 132 MET   A SD   1 
ATOM   2001 C  CE   . MET   A 1 132 ? -7.590  14.985  -21.182 1.00 19.88  ? 132 MET   A CE   1 
ATOM   2002 H  H    . MET   A 1 132 ? -2.408  17.087  -20.966 1.00 14.27  ? 132 MET   A H    1 
ATOM   2003 H  HA   . MET   A 1 132 ? -3.759  15.503  -19.253 1.00 14.66  ? 132 MET   A HA   1 
ATOM   2004 H  HB2  . MET   A 1 132 ? -3.566  14.972  -22.012 1.00 17.32  ? 132 MET   A HB2  1 
ATOM   2005 H  HB3  . MET   A 1 132 ? -4.620  14.357  -20.995 1.00 17.32  ? 132 MET   A HB3  1 
ATOM   2006 H  HG2  . MET   A 1 132 ? -4.706  17.064  -21.665 1.00 17.80  ? 132 MET   A HG2  1 
ATOM   2007 H  HG3  . MET   A 1 132 ? -5.462  15.980  -22.548 1.00 17.80  ? 132 MET   A HG3  1 
ATOM   2008 H  HE1  . MET   A 1 132 ? -8.428  14.967  -20.693 1.00 23.86  ? 132 MET   A HE1  1 
ATOM   2009 H  HE2  . MET   A 1 132 ? -7.759  15.151  -22.122 1.00 23.86  ? 132 MET   A HE2  1 
ATOM   2010 H  HE3  . MET   A 1 132 ? -7.127  14.139  -21.074 1.00 23.86  ? 132 MET   A HE3  1 
ATOM   2011 N  N    . ARG   A 1 133 ? -1.750  14.082  -18.808 1.00 12.83  ? 133 ARG   A N    1 
ATOM   2012 C  CA   . ARG   A 1 133 ? -0.626  13.188  -18.586 1.00 11.64  ? 133 ARG   A CA   1 
ATOM   2013 C  C    . ARG   A 1 133 ? -1.110  11.768  -18.764 1.00 12.40  ? 133 ARG   A C    1 
ATOM   2014 O  O    . ARG   A 1 133 ? -1.917  11.277  -17.962 1.00 12.88  ? 133 ARG   A O    1 
ATOM   2015 C  CB   . ARG   A 1 133 ? -0.005  13.380  -17.213 1.00 12.46  ? 133 ARG   A CB   1 
ATOM   2016 C  CG   . ARG   A 1 133 ? 0.472   14.828  -16.929 1.00 15.65  ? 133 ARG   A CG   1 
ATOM   2017 C  CD   . ARG   A 1 133 ? 1.403   14.904  -15.720 1.00 17.46  ? 133 ARG   A CD   1 
ATOM   2018 N  NE   . ARG   A 1 133 ? 0.807   14.347  -14.529 1.00 16.68  ? 133 ARG   A NE   1 
ATOM   2019 C  CZ   . ARG   A 1 133 ? 1.446   14.065  -13.385 1.00 18.23  ? 133 ARG   A CZ   1 
ATOM   2020 N  NH1  . ARG   A 1 133 ? 2.697   14.377  -13.213 1.00 20.63  ? 133 ARG   A NH1  1 
ATOM   2021 N  NH2  . ARG   A 1 133 ? 0.781   13.479  -12.381 1.00 19.17  ? 133 ARG   A NH2  1 
ATOM   2022 H  H    . ARG   A 1 133 ? -2.223  14.204  -18.100 1.00 15.40  ? 133 ARG   A H    1 
ATOM   2023 H  HA   . ARG   A 1 133 ? 0.059   13.382  -19.244 1.00 13.96  ? 133 ARG   A HA   1 
ATOM   2024 H  HB2  . ARG   A 1 133 ? -0.664  13.149  -16.540 1.00 14.95  ? 133 ARG   A HB2  1 
ATOM   2025 H  HB3  . ARG   A 1 133 ? 0.766   12.796  -17.137 1.00 14.95  ? 133 ARG   A HB3  1 
ATOM   2026 H  HG2  . ARG   A 1 133 ? 0.954   15.163  -17.701 1.00 18.78  ? 133 ARG   A HG2  1 
ATOM   2027 H  HG3  . ARG   A 1 133 ? -0.299  15.389  -16.751 1.00 18.78  ? 133 ARG   A HG3  1 
ATOM   2028 H  HD2  . ARG   A 1 133 ? 2.213   14.407  -15.913 1.00 20.95  ? 133 ARG   A HD2  1 
ATOM   2029 H  HD3  . ARG   A 1 133 ? 1.617   15.833  -15.543 1.00 20.95  ? 133 ARG   A HD3  1 
ATOM   2030 H  HE   . ARG   A 1 133 ? -0.036  14.179  -14.556 1.00 20.01  ? 133 ARG   A HE   1 
ATOM   2031 H  HH11 . ARG   A 1 133 ? 3.089   14.188  -12.471 1.00 24.75  ? 133 ARG   A HH11 1 
ATOM   2032 H  HH12 . ARG   A 1 133 ? 3.132   14.772  -13.841 1.00 24.75  ? 133 ARG   A HH12 1 
ATOM   2033 H  HH21 . ARG   A 1 133 ? 1.186   13.296  -11.645 1.00 23.01  ? 133 ARG   A HH21 1 
ATOM   2034 H  HH22 . ARG   A 1 133 ? -0.052  13.285  -12.473 1.00 23.01  ? 133 ARG   A HH22 1 
ATOM   2035 N  N    . VAL   A 1 134 ? -0.649  11.122  -19.793 1.00 11.70  ? 134 VAL   A N    1 
ATOM   2036 C  CA   . VAL   A 1 134 ? -1.159  9.816   -20.237 1.00 12.65  ? 134 VAL   A CA   1 
ATOM   2037 C  C    . VAL   A 1 134 ? -0.082  8.757   -19.993 1.00 12.43  ? 134 VAL   A C    1 
ATOM   2038 O  O    . VAL   A 1 134 ? 1.106   9.052   -19.971 1.00 13.35  ? 134 VAL   A O    1 
ATOM   2039 C  CB   . VAL   A 1 134 ? -1.621  9.906   -21.719 1.00 14.38  ? 134 VAL   A CB   1 
ATOM   2040 C  CG1  . VAL   A 1 134 ? -2.192  8.654   -22.328 1.00 16.26  ? 134 VAL   A CG1  1 
ATOM   2041 C  CG2  . VAL   A 1 134 ? -2.646  11.059  -21.826 1.00 16.67  ? 134 VAL   A CG2  1 
ATOM   2042 H  H    . VAL   A 1 134 ? -0.010  11.416  -20.289 1.00 14.04  ? 134 VAL   A H    1 
ATOM   2043 H  HA   . VAL   A 1 134 ? -1.921  9.533   -19.707 1.00 15.18  ? 134 VAL   A HA   1 
ATOM   2044 H  HB   . VAL   A 1 134 ? -0.820  10.062  -22.243 1.00 17.25  ? 134 VAL   A HB   1 
ATOM   2045 H  HG11 . VAL   A 1 134 ? -2.518  8.856   -23.219 1.00 19.51  ? 134 VAL   A HG11 1 
ATOM   2046 H  HG12 . VAL   A 1 134 ? -1.495  7.980   -22.376 1.00 19.51  ? 134 VAL   A HG12 1 
ATOM   2047 H  HG13 . VAL   A 1 134 ? -2.921  8.336   -21.773 1.00 19.51  ? 134 VAL   A HG13 1 
ATOM   2048 H  HG21 . VAL   A 1 134 ? -3.011  11.075  -22.724 1.00 20.00  ? 134 VAL   A HG21 1 
ATOM   2049 H  HG22 . VAL   A 1 134 ? -3.356  10.911  -21.182 1.00 20.00  ? 134 VAL   A HG22 1 
ATOM   2050 H  HG23 . VAL   A 1 134 ? -2.198  11.898  -21.637 1.00 20.00  ? 134 VAL   A HG23 1 
ATOM   2051 N  N    . HIS   A 1 135 ? -0.477  7.499   -19.941 1.00 12.70  ? 135 HIS   A N    1 
ATOM   2052 C  CA   . HIS   A 1 135 ? 0.421   6.386   -19.678 1.00 13.56  ? 135 HIS   A CA   1 
ATOM   2053 C  C    . HIS   A 1 135 ? 1.125   6.562   -18.325 1.00 14.56  ? 135 HIS   A C    1 
ATOM   2054 O  O    . HIS   A 1 135 ? 2.298   6.216   -18.161 1.00 14.57  ? 135 HIS   A O    1 
ATOM   2055 C  CB   . HIS   A 1 135 ? 1.457   6.166   -20.780 1.00 14.09  ? 135 HIS   A CB   1 
ATOM   2056 C  CG   . HIS   A 1 135 ? 0.902   5.983   -22.153 1.00 14.01  ? 135 HIS   A CG   1 
ATOM   2057 N  ND1  . HIS   A 1 135 ? 0.153   4.880   -22.489 1.00 18.28  ? 135 HIS   A ND1  1 
ATOM   2058 C  CD2  . HIS   A 1 135 ? 1.049   6.706   -23.263 1.00 14.86  ? 135 HIS   A CD2  1 
ATOM   2059 C  CE1  . HIS   A 1 135 ? -0.156  4.953   -23.779 1.00 17.20  ? 135 HIS   A CE1  1 
ATOM   2060 N  NE2  . HIS   A 1 135 ? 0.404   6.029   -24.288 1.00 15.18  ? 135 HIS   A NE2  1 
ATOM   2061 H  H    . HIS   A 1 135 ? -1.292  7.252   -20.060 1.00 15.24  ? 135 HIS   A H    1 
ATOM   2062 H  HA   . HIS   A 1 135 ? -0.129  5.588   -19.650 1.00 16.27  ? 135 HIS   A HA   1 
ATOM   2063 H  HB2  . HIS   A 1 135 ? 2.045   6.938   -20.806 1.00 16.91  ? 135 HIS   A HB2  1 
ATOM   2064 H  HB3  . HIS   A 1 135 ? 1.967   5.369   -20.566 1.00 16.91  ? 135 HIS   A HB3  1 
ATOM   2065 H  HD1  . HIS   A 1 135 ? -0.076  4.247   -21.953 1.00 21.94  ? 135 HIS   A HD1  1 
ATOM   2066 H  HD2  . HIS   A 1 135 ? 1.501   7.515   -23.337 1.00 17.83  ? 135 HIS   A HD2  1 
ATOM   2067 H  HE1  . HIS   A 1 135 ? -0.683  4.344   -24.245 1.00 20.64  ? 135 HIS   A HE1  1 
ATOM   2068 H  HE2  . HIS   A 1 135 ? 0.376   6.271   -25.113 1.00 18.21  ? 135 HIS   A HE2  1 
ATOM   2069 N  N    . TYR   A 1 136 ? 0.405   7.120   -17.363 1.00 13.02  ? 136 TYR   A N    1 
ATOM   2070 C  CA   . TYR   A 1 136 ? 0.982   7.341   -16.033 1.00 13.13  ? 136 TYR   A CA   1 
ATOM   2071 C  C    . TYR   A 1 136 ? 1.163   6.027   -15.287 1.00 13.35  ? 136 TYR   A C    1 
ATOM   2072 O  O    . TYR   A 1 136 ? 0.186   5.268   -15.147 1.00 14.88  ? 136 TYR   A O    1 
ATOM   2073 C  CB   . TYR   A 1 136 ? 0.052   8.257   -15.247 1.00 14.94  ? 136 TYR   A CB   1 
ATOM   2074 C  CG   . TYR   A 1 136 ? 0.441   8.453   -13.825 1.00 14.58  ? 136 TYR   A CG   1 
ATOM   2075 C  CD1  . TYR   A 1 136 ? 1.374   9.420   -13.475 1.00 15.35  ? 136 TYR   A CD1  1 
ATOM   2076 C  CD2  . TYR   A 1 136 ? -0.156  7.734   -12.785 1.00 16.00  ? 136 TYR   A CD2  1 
ATOM   2077 C  CE1  . TYR   A 1 136 ? 1.704   9.650   -12.100 1.00 17.32  ? 136 TYR   A CE1  1 
ATOM   2078 C  CE2  . TYR   A 1 136 ? 0.141   7.988   -11.442 1.00 17.90  ? 136 TYR   A CE2  1 
ATOM   2079 C  CZ   . TYR   A 1 136 ? 1.080   8.883   -11.129 1.00 17.05  ? 136 TYR   A CZ   1 
ATOM   2080 O  OH   . TYR   A 1 136 ? 1.406   9.128   -9.793  1.00 20.78  ? 136 TYR   A OH   1 
ATOM   2081 H  H    . TYR   A 1 136 ? -0.411  7.380   -17.447 1.00 15.62  ? 136 TYR   A H    1 
ATOM   2082 H  HA   . TYR   A 1 136 ? 1.857   7.750   -16.120 1.00 15.76  ? 136 TYR   A HA   1 
ATOM   2083 H  HB2  . TYR   A 1 136 ? 0.044   9.129   -15.672 1.00 17.92  ? 136 TYR   A HB2  1 
ATOM   2084 H  HB3  . TYR   A 1 136 ? -0.840  7.875   -15.257 1.00 17.92  ? 136 TYR   A HB3  1 
ATOM   2085 H  HD1  . TYR   A 1 136 ? 1.787   9.922   -14.139 1.00 18.42  ? 136 TYR   A HD1  1 
ATOM   2086 H  HD2  . TYR   A 1 136 ? -0.770  7.067   -12.992 1.00 19.20  ? 136 TYR   A HD2  1 
ATOM   2087 H  HE1  . TYR   A 1 136 ? 2.326   10.301  -11.864 1.00 20.78  ? 136 TYR   A HE1  1 
ATOM   2088 H  HE2  . TYR   A 1 136 ? -0.314  7.534   -10.770 1.00 21.48  ? 136 TYR   A HE2  1 
ATOM   2089 H  HH   . TYR   A 1 136 ? 1.984   9.735   -9.745  1.00 24.94  ? 136 TYR   A HH   1 
ATOM   2090 N  N    . GLY   A 1 137 ? 2.341   5.788   -14.750 1.00 14.07  ? 137 GLY   A N    1 
ATOM   2091 C  CA   . GLY   A 1 137 ? 2.540   4.686   -13.823 1.00 14.93  ? 137 GLY   A CA   1 
ATOM   2092 C  C    . GLY   A 1 137 ? 2.503   3.333   -14.513 1.00 17.72  ? 137 GLY   A C    1 
ATOM   2093 O  O    . GLY   A 1 137 ? 2.403   3.217   -15.736 1.00 17.19  ? 137 GLY   A O    1 
ATOM   2094 H  H    . GLY   A 1 137 ? 3.050   6.250   -14.904 1.00 16.89  ? 137 GLY   A H    1 
ATOM   2095 H  HA2  . GLY   A 1 137 ? 3.402   4.784   -13.388 1.00 17.91  ? 137 GLY   A HA2  1 
ATOM   2096 H  HA3  . GLY   A 1 137 ? 1.843   4.704   -13.149 1.00 17.91  ? 137 GLY   A HA3  1 
ATOM   2097 N  N    . GLN   A 1 138 ? 2.639   2.288   -13.683 1.00 16.72  ? 138 GLN   A N    1 
ATOM   2098 C  CA   . GLN   A 1 138 ? 2.650   0.904   -14.129 1.00 18.72  ? 138 GLN   A CA   1 
ATOM   2099 C  C    . GLN   A 1 138 ? 1.402   0.233   -13.585 1.00 20.01  ? 138 GLN   A C    1 
ATOM   2100 O  O    . GLN   A 1 138 ? 1.242   0.055   -12.367 1.00 21.34  ? 138 GLN   A O    1 
ATOM   2101 C  CB   . GLN   A 1 138 ? 3.902   0.166   -13.660 1.00 25.29  ? 138 GLN   A CB   1 
ATOM   2102 C  CG   . GLN   A 1 138 ? 4.245   -1.067  -14.566 1.00 37.15  ? 138 GLN   A CG   1 
ATOM   2103 C  CD   . GLN   A 1 138 ? 4.716   -0.718  -16.007 1.00 50.49  ? 138 GLN   A CD   1 
ATOM   2104 O  OE1  . GLN   A 1 138 ? 3.888   -0.672  -16.936 1.00 37.13  ? 138 GLN   A OE1  1 
ATOM   2105 N  NE2  . GLN   A 1 138 ? 6.031   -0.499  -16.199 1.00 47.19  ? 138 GLN   A NE2  1 
ATOM   2106 H  H    . GLN   A 1 138 ? 2.728   2.367   -12.831 1.00 20.07  ? 138 GLN   A H    1 
ATOM   2107 H  HA   . GLN   A 1 138 ? 2.635   0.885   -15.099 1.00 22.46  ? 138 GLN   A HA   1 
ATOM   2108 H  HB2  . GLN   A 1 138 ? 4.657   0.776   -13.682 1.00 30.35  ? 138 GLN   A HB2  1 
ATOM   2109 H  HB3  . GLN   A 1 138 ? 3.761   -0.154  -12.755 1.00 30.35  ? 138 GLN   A HB3  1 
ATOM   2110 H  HG2  . GLN   A 1 138 ? 4.958   -1.571  -14.142 1.00 44.58  ? 138 GLN   A HG2  1 
ATOM   2111 H  HG3  . GLN   A 1 138 ? 3.452   -1.619  -14.646 1.00 44.58  ? 138 GLN   A HG3  1 
ATOM   2112 H  HE21 . GLN   A 1 138 ? 6.578   -0.555  -15.537 1.00 56.63  ? 138 GLN   A HE21 1 
ATOM   2113 H  HE22 . GLN   A 1 138 ? 6.325   -0.304  -16.984 1.00 56.63  ? 138 GLN   A HE22 1 
ATOM   2114 N  N    . GLY   A 1 139 ? 0.472   -0.122  -14.473 1.00 18.80  ? 139 GLY   A N    1 
ATOM   2115 C  CA   . GLY   A 1 139 ? -0.773  -0.798  -14.063 1.00 19.81  ? 139 GLY   A CA   1 
ATOM   2116 C  C    . GLY   A 1 139 ? -1.628  0.093   -13.183 1.00 17.07  ? 139 GLY   A C    1 
ATOM   2117 O  O    . GLY   A 1 139 ? -2.322  -0.450  -12.305 1.00 20.18  ? 139 GLY   A O    1 
ATOM   2118 H  H    . GLY   A 1 139 ? 0.559   0.049   -15.358 1.00 22.56  ? 139 GLY   A H    1 
ATOM   2119 H  HA2  . GLY   A 1 139 ? -1.274  -1.055  -14.861 1.00 23.77  ? 139 GLY   A HA2  1 
ATOM   2120 H  HA3  . GLY   A 1 139 ? -0.545  -1.621  -13.572 1.00 23.77  ? 139 GLY   A HA3  1 
ATOM   2121 N  N    . TYR   A 1 140 ? -1.607  1.407   -13.416 1.00 16.30  ? 140 TYR   A N    1 
ATOM   2122 C  CA   . TYR   A 1 140 ? -2.351  2.374   -12.565 1.00 15.03  ? 140 TYR   A CA   1 
ATOM   2123 C  C    . TYR   A 1 140 ? -3.810  2.404   -12.994 1.00 14.79  ? 140 TYR   A C    1 
ATOM   2124 O  O    . TYR   A 1 140 ? -4.096  2.909   -14.084 1.00 15.47  ? 140 TYR   A O    1 
ATOM   2125 C  CB   . TYR   A 1 140 ? -1.658  3.734   -12.671 1.00 16.16  ? 140 TYR   A CB   1 
ATOM   2126 C  CG   . TYR   A 1 140 ? -2.198  4.761   -11.689 1.00 14.68  ? 140 TYR   A CG   1 
ATOM   2127 C  CD1  . TYR   A 1 140 ? -1.886  4.685   -10.338 1.00 17.44  ? 140 TYR   A CD1  1 
ATOM   2128 C  CD2  . TYR   A 1 140 ? -3.003  5.808   -12.114 1.00 13.90  ? 140 TYR   A CD2  1 
ATOM   2129 C  CE1  . TYR   A 1 140 ? -2.373  5.612   -9.435  1.00 16.44  ? 140 TYR   A CE1  1 
ATOM   2130 C  CE2  . TYR   A 1 140 ? -3.484  6.751   -11.223 1.00 16.47  ? 140 TYR   A CE2  1 
ATOM   2131 C  CZ   . TYR   A 1 140 ? -3.169  6.650   -9.880  1.00 17.53  ? 140 TYR   A CZ   1 
ATOM   2132 O  OH   . TYR   A 1 140 ? -3.648  7.568   -8.996  1.00 18.15  ? 140 TYR   A OH   1 
ATOM   2133 H  H    . TYR   A 1 140 ? -1.164  1.756   -14.120 1.00 19.56  ? 140 TYR   A H    1 
ATOM   2134 H  HA   . TYR   A 1 140 ? -2.302  2.068   -11.622 1.00 18.03  ? 140 TYR   A HA   1 
ATOM   2135 H  HB2  . TYR   A 1 140 ? -0.697  3.609   -12.509 1.00 19.40  ? 140 TYR   A HB2  1 
ATOM   2136 H  HB3  . TYR   A 1 140 ? -1.773  4.075   -13.585 1.00 19.40  ? 140 TYR   A HB3  1 
ATOM   2137 H  HD1  . TYR   A 1 140 ? -1.343  3.978   -10.028 1.00 20.93  ? 140 TYR   A HD1  1 
ATOM   2138 H  HD2  . TYR   A 1 140 ? -3.220  5.884   -13.029 1.00 16.68  ? 140 TYR   A HD2  1 
ATOM   2139 H  HE1  . TYR   A 1 140 ? -2.153  5.543   -8.522  1.00 19.73  ? 140 TYR   A HE1  1 
ATOM   2140 H  HE2  . TYR   A 1 140 ? -4.034  7.454   -11.526 1.00 19.77  ? 140 TYR   A HE2  1 
ATOM   2141 H  HH   . TYR   A 1 140 ? -3.603  7.257   -8.200  1.00 21.78  ? 140 TYR   A HH   1 
ATOM   2142 N  N    . GLU   A 1 141 ? -4.715  1.917   -12.144 1.00 16.50  ? 141 GLU   A N    1 
ATOM   2143 C  CA   . GLU   A 1 141 ? -6.158  1.821   -12.488 1.00 16.18  ? 141 GLU   A CA   1 
ATOM   2144 C  C    . GLU   A 1 141 ? -6.908  3.017   -11.892 1.00 17.10  ? 141 GLU   A C    1 
ATOM   2145 O  O    . GLU   A 1 141 ? -7.834  2.796   -11.092 1.00 18.57  ? 141 GLU   A O    1 
ATOM   2146 C  CB   . GLU   A 1 141 ? -6.694  0.490   -11.969 1.00 20.54  ? 141 GLU   A CB   1 
ATOM   2147 C  CG   . GLU   A 1 141 ? -5.936  -0.705  -12.534 1.00 26.31  ? 141 GLU   A CG   1 
ATOM   2148 C  CD   . GLU   A 1 141 ? -6.751  -1.978  -12.501 1.00 42.99  ? 141 GLU   A CD   1 
ATOM   2149 O  OE1  . GLU   A 1 141 ? -7.127  -2.439  -11.405 1.00 34.58  ? 141 GLU   A OE1  1 
ATOM   2150 O  OE2  . GLU   A 1 141 ? -7.026  -2.489  -13.597 1.00 32.48  ? 141 GLU   A OE2  1 
ATOM   2151 H  H    . GLU   A 1 141 ? -4.487  1.658   -11.312 1.00 19.80  ? 141 GLU   A H    1 
ATOM   2152 H  HA   . GLU   A 1 141 ? -6.253  1.842   -13.474 1.00 19.42  ? 141 GLU   A HA   1 
ATOM   2153 H  HB2  . GLU   A 1 141 ? -6.625  0.478   -10.992 1.00 24.65  ? 141 GLU   A HB2  1 
ATOM   2154 H  HB3  . GLU   A 1 141 ? -7.641  0.412   -12.206 1.00 24.65  ? 141 GLU   A HB3  1 
ATOM   2155 H  HG2  . GLU   A 1 141 ? -5.682  -0.516  -13.463 1.00 31.57  ? 141 GLU   A HG2  1 
ATOM   2156 H  HG3  . GLU   A 1 141 ? -5.115  -0.842  -12.017 1.00 31.57  ? 141 GLU   A HG3  1 
ATOM   2157 N  N    . ASN   A 1 142 ? -6.536  4.235   -12.278 1.00 15.79  ? 142 ASN   A N    1 
ATOM   2158 C  CA   . ASN   A 1 142 ? -7.173  5.449   -11.768 1.00 13.82  ? 142 ASN   A CA   1 
ATOM   2159 C  C    . ASN   A 1 142 ? -6.777  6.602   -12.676 1.00 13.52  ? 142 ASN   A C    1 
ATOM   2160 O  O    . ASN   A 1 142 ? -5.928  6.478   -13.575 1.00 13.25  ? 142 ASN   A O    1 
ATOM   2161 C  CB   . ASN   A 1 142 ? -6.742  5.699   -10.321 1.00 15.36  ? 142 ASN   A CB   1 
ATOM   2162 C  CG   . ASN   A 1 142 ? -7.538  6.766   -9.623  1.00 14.86  ? 142 ASN   A CG   1 
ATOM   2163 O  OD1  . ASN   A 1 142 ? -8.741  6.849   -9.770  1.00 14.47  ? 142 ASN   A OD1  1 
ATOM   2164 N  ND2  . ASN   A 1 142 ? -6.872  7.604   -8.870  1.00 17.37  ? 142 ASN   A ND2  1 
ATOM   2165 H  H    . ASN   A 1 142 ? -5.911  4.387   -12.849 1.00 18.95  ? 142 ASN   A H    1 
ATOM   2166 H  HA   . ASN   A 1 142 ? -8.140  5.369   -11.799 1.00 16.58  ? 142 ASN   A HA   1 
ATOM   2167 H  HB2  . ASN   A 1 142 ? -6.846  4.876   -9.818  1.00 18.43  ? 142 ASN   A HB2  1 
ATOM   2168 H  HB3  . ASN   A 1 142 ? -5.812  5.974   -10.317 1.00 18.43  ? 142 ASN   A HB3  1 
ATOM   2169 H  HD21 . ASN   A 1 142 ? -7.287  8.231   -8.452  1.00 20.84  ? 142 ASN   A HD21 1 
ATOM   2170 H  HD22 . ASN   A 1 142 ? -6.019  7.528   -8.793  1.00 20.84  ? 142 ASN   A HD22 1 
ATOM   2171 N  N    . ALA   A 1 143 ? -7.432  7.733   -12.425 1.00 12.33  ? 143 ALA   A N    1 
ATOM   2172 C  CA   . ALA   A 1 143 ? -7.166  9.017   -13.073 1.00 12.85  ? 143 ALA   A CA   1 
ATOM   2173 C  C    . ALA   A 1 143 ? -7.491  10.084  -12.029 1.00 13.23  ? 143 ALA   A C    1 
ATOM   2174 O  O    . ALA   A 1 143 ? -8.340  9.849   -11.157 1.00 13.38  ? 143 ALA   A O    1 
ATOM   2175 C  CB   . ALA   A 1 143 ? -8.007  9.220   -14.335 1.00 12.55  ? 143 ALA   A CB   1 
ATOM   2176 H  H    . ALA   A 1 143 ? -8.071  7.787   -11.852 1.00 14.80  ? 143 ALA   A H    1 
ATOM   2177 H  HA   . ALA   A 1 143 ? -6.239  9.084   -13.351 1.00 15.42  ? 143 ALA   A HA   1 
ATOM   2178 H  HB1  . ALA   A 1 143 ? -7.768  10.068  -14.741 1.00 15.05  ? 143 ALA   A HB1  1 
ATOM   2179 H  HB2  . ALA   A 1 143 ? -7.827  8.495   -14.955 1.00 15.05  ? 143 ALA   A HB2  1 
ATOM   2180 H  HB3  . ALA   A 1 143 ? -8.946  9.222   -14.093 1.00 15.05  ? 143 ALA   A HB3  1 
ATOM   2181 N  N    . TYR   A 1 144 ? -6.866  11.242  -12.112 1.00 11.88  ? 144 TYR   A N    1 
ATOM   2182 C  CA   . TYR   A 1 144 ? -7.084  12.253  -11.075 1.00 12.29  ? 144 TYR   A CA   1 
ATOM   2183 C  C    . TYR   A 1 144 ? -6.660  13.630  -11.558 1.00 13.17  ? 144 TYR   A C    1 
ATOM   2184 O  O    . TYR   A 1 144 ? -5.859  13.797  -12.482 1.00 13.17  ? 144 TYR   A O    1 
ATOM   2185 C  CB   . TYR   A 1 144 ? -6.336  11.872  -9.778  1.00 12.57  ? 144 TYR   A CB   1 
ATOM   2186 C  CG   . TYR   A 1 144 ? -4.860  11.788  -9.872  1.00 13.07  ? 144 TYR   A CG   1 
ATOM   2187 C  CD1  . TYR   A 1 144 ? -4.033  12.901  -9.609  1.00 15.06  ? 144 TYR   A CD1  1 
ATOM   2188 C  CD2  . TYR   A 1 144 ? -4.227  10.614  -10.168 1.00 14.91  ? 144 TYR   A CD2  1 
ATOM   2189 C  CE1  . TYR   A 1 144 ? -2.680  12.832  -9.664  1.00 16.73  ? 144 TYR   A CE1  1 
ATOM   2190 C  CE2  . TYR   A 1 144 ? -2.823  10.549  -10.213 1.00 17.01  ? 144 TYR   A CE2  1 
ATOM   2191 C  CZ   . TYR   A 1 144 ? -2.083  11.676  -9.927  1.00 16.56  ? 144 TYR   A CZ   1 
ATOM   2192 O  OH   . TYR   A 1 144 ? -0.674  11.534  -10.021 1.00 21.25  ? 144 TYR   A OH   1 
ATOM   2193 H  H    . TYR   A 1 144 ? -6.322  11.469  -12.739 1.00 14.25  ? 144 TYR   A H    1 
ATOM   2194 H  HA   . TYR   A 1 144 ? -8.036  12.309  -10.897 1.00 14.75  ? 144 TYR   A HA   1 
ATOM   2195 H  HB2  . TYR   A 1 144 ? -6.541  12.539  -9.104  1.00 15.08  ? 144 TYR   A HB2  1 
ATOM   2196 H  HB3  . TYR   A 1 144 ? -6.653  11.001  -9.491  1.00 15.08  ? 144 TYR   A HB3  1 
ATOM   2197 H  HD1  . TYR   A 1 144 ? -4.431  13.712  -9.390  1.00 18.07  ? 144 TYR   A HD1  1 
ATOM   2198 H  HD2  . TYR   A 1 144 ? -4.729  9.851   -10.343 1.00 17.90  ? 144 TYR   A HD2  1 
ATOM   2199 H  HE1  . TYR   A 1 144 ? -2.169  13.595  -9.517  1.00 20.08  ? 144 TYR   A HE1  1 
ATOM   2200 H  HE2  . TYR   A 1 144 ? -2.397  9.752   -10.433 1.00 20.41  ? 144 TYR   A HE2  1 
ATOM   2201 H  HH   . TYR   A 1 144 ? -0.298  12.258  -9.823  1.00 25.50  ? 144 TYR   A HH   1 
ATOM   2202 N  N    . TRP   A 1 145 ? -7.170  14.630  -10.829 1.00 11.30  ? 145 TRP   A N    1 
ATOM   2203 C  CA   . TRP   A 1 145 ? -6.788  16.040  -10.929 1.00 11.30  ? 145 TRP   A CA   1 
ATOM   2204 C  C    . TRP   A 1 145 ? -5.883  16.370  -9.759  1.00 12.32  ? 145 TRP   A C    1 
ATOM   2205 O  O    . TRP   A 1 145 ? -6.200  16.032  -8.619  1.00 13.09  ? 145 TRP   A O    1 
ATOM   2206 C  CB   . TRP   A 1 145 ? -8.058  16.918  -10.886 1.00 11.43  ? 145 TRP   A CB   1 
ATOM   2207 C  CG   . TRP   A 1 145 ? -7.845  18.371  -10.525 1.00 12.01  ? 145 TRP   A CG   1 
ATOM   2208 C  CD1  . TRP   A 1 145 ? -8.051  18.900  -9.304  1.00 13.42  ? 145 TRP   A CD1  1 
ATOM   2209 C  CD2  . TRP   A 1 145 ? -7.456  19.434  -11.398 1.00 11.97  ? 145 TRP   A CD2  1 
ATOM   2210 N  NE1  . TRP   A 1 145 ? -7.789  20.247  -9.340  1.00 14.66  ? 145 TRP   A NE1  1 
ATOM   2211 C  CE2  . TRP   A 1 145 ? -7.402  20.597  -10.599 1.00 13.10  ? 145 TRP   A CE2  1 
ATOM   2212 C  CE3  . TRP   A 1 145 ? -7.080  19.519  -12.733 1.00 14.08  ? 145 TRP   A CE3  1 
ATOM   2213 C  CZ2  . TRP   A 1 145 ? -7.030  21.854  -11.125 1.00 14.69  ? 145 TRP   A CZ2  1 
ATOM   2214 C  CZ3  . TRP   A 1 145 ? -6.739  20.813  -13.257 1.00 13.14  ? 145 TRP   A CZ3  1 
ATOM   2215 C  CH2  . TRP   A 1 145 ? -6.692  21.913  -12.433 1.00 14.59  ? 145 TRP   A CH2  1 
ATOM   2216 H  H    . TRP   A 1 145 ? -7.778  14.507  -10.233 1.00 13.56  ? 145 TRP   A H    1 
ATOM   2217 H  HA   . TRP   A 1 145 ? -6.310  16.218  -11.755 1.00 13.56  ? 145 TRP   A HA   1 
ATOM   2218 H  HB2  . TRP   A 1 145 ? -8.472  16.898  -11.763 1.00 13.71  ? 145 TRP   A HB2  1 
ATOM   2219 H  HB3  . TRP   A 1 145 ? -8.663  16.545  -10.226 1.00 13.71  ? 145 TRP   A HB3  1 
ATOM   2220 H  HD1  . TRP   A 1 145 ? -8.328  18.426  -8.554  1.00 16.10  ? 145 TRP   A HD1  1 
ATOM   2221 H  HE1  . TRP   A 1 145 ? -7.859  20.785  -8.673  1.00 17.59  ? 145 TRP   A HE1  1 
ATOM   2222 H  HE3  . TRP   A 1 145 ? -7.050  18.761  -13.272 1.00 16.89  ? 145 TRP   A HE3  1 
ATOM   2223 H  HZ2  . TRP   A 1 145 ? -7.018  22.614  -10.590 1.00 17.62  ? 145 TRP   A HZ2  1 
ATOM   2224 H  HZ3  . TRP   A 1 145 ? -6.548  20.907  -14.163 1.00 15.77  ? 145 TRP   A HZ3  1 
ATOM   2225 H  HH2  . TRP   A 1 145 ? -6.418  22.728  -12.789 1.00 17.51  ? 145 TRP   A HH2  1 
ATOM   2226 N  N    . ASP   A 1 146 ? -4.775  17.065  -10.005 1.00 11.80  ? 146 ASP   A N    1 
ATOM   2227 C  CA   . ASP   A 1 146 ? -3.781  17.318  -8.978  1.00 14.50  ? 146 ASP   A CA   1 
ATOM   2228 C  C    . ASP   A 1 146 ? -3.640  18.793  -8.606  1.00 14.60  ? 146 ASP   A C    1 
ATOM   2229 O  O    . ASP   A 1 146 ? -2.711  19.147  -7.865  1.00 16.69  ? 146 ASP   A O    1 
ATOM   2230 C  CB   . ASP   A 1 146 ? -2.415  16.744  -9.382  1.00 15.59  ? 146 ASP   A CB   1 
ATOM   2231 C  CG   . ASP   A 1 146 ? -1.750  17.554  -10.434 1.00 17.10  ? 146 ASP   A CG   1 
ATOM   2232 O  OD1  . ASP   A 1 146 ? -2.410  18.465  -11.004 1.00 16.50  ? 146 ASP   A OD1  1 
ATOM   2233 O  OD2  . ASP   A 1 146 ? -0.575  17.293  -10.708 1.00 20.47  ? 146 ASP   A OD2  1 
ATOM   2234 H  H    . ASP   A 1 146 ? -4.579  17.404  -10.770 1.00 14.17  ? 146 ASP   A H    1 
ATOM   2235 H  HA   . ASP   A 1 146 ? -4.073  16.851  -8.179  1.00 17.40  ? 146 ASP   A HA   1 
ATOM   2236 H  HB2  . ASP   A 1 146 ? -1.836  16.725  -8.604  1.00 18.71  ? 146 ASP   A HB2  1 
ATOM   2237 H  HB3  . ASP   A 1 146 ? -2.537  15.845  -9.726  1.00 18.71  ? 146 ASP   A HB3  1 
ATOM   2238 N  N    . GLY   A 1 147 ? -4.503  19.652  -9.157  1.00 14.12  ? 147 GLY   A N    1 
ATOM   2239 C  CA   . GLY   A 1 147 ? -4.476  21.100  -8.863  1.00 16.01  ? 147 GLY   A CA   1 
ATOM   2240 C  C    . GLY   A 1 147 ? -4.022  21.918  -10.056 1.00 16.55  ? 147 GLY   A C    1 
ATOM   2241 O  O    . GLY   A 1 147 ? -4.239  23.141  -10.040 1.00 19.60  ? 147 GLY   A O    1 
ATOM   2242 H  H    . GLY   A 1 147 ? -5.124  19.384  -9.756  1.00 16.95  ? 147 GLY   A H    1 
ATOM   2243 H  HA2  . GLY   A 1 147 ? -5.380  21.387  -8.597  1.00 19.21  ? 147 GLY   A HA2  1 
ATOM   2244 H  HA3  . GLY   A 1 147 ? -3.873  21.268  -8.104  1.00 19.21  ? 147 GLY   A HA3  1 
ATOM   2245 N  N    . LYS   A 1 148 ? -3.394  21.283  -11.048 1.00 15.32  ? 148 LYS   A N    1 
ATOM   2246 C  CA   . LYS   A 1 148 ? -2.918  22.000  -12.261 1.00 16.25  ? 148 LYS   A CA   1 
ATOM   2247 C  C    . LYS   A 1 148 ? -3.062  21.159  -13.538 1.00 17.01  ? 148 LYS   A C    1 
ATOM   2248 O  O    . LYS   A 1 148 ? -2.977  21.753  -14.623 1.00 15.98  ? 148 LYS   A O    1 
ATOM   2249 C  CB   . LYS   A 1 148 ? -1.445  22.387  -12.096 1.00 17.61  ? 148 LYS   A CB   1 
ATOM   2250 C  CG   . LYS   A 1 148 ? -0.461  21.228  -12.166 1.00 20.04  ? 148 LYS   A CG   1 
ATOM   2251 C  CD   . LYS   A 1 148 ? 0.977   21.638  -11.882 1.00 29.88  ? 148 LYS   A CD   1 
ATOM   2252 C  CE   . LYS   A 1 148 ? 1.923   20.495  -12.045 1.00 41.29  ? 148 LYS   A CE   1 
ATOM   2253 N  NZ   . LYS   A 1 148 ? 3.284   20.867  -11.654 1.00 53.64  ? 148 LYS   A NZ   1 
ATOM   2254 H  H    . LYS   A 1 148 ? -3.180  20.411  -10.977 1.00 18.38  ? 148 LYS   A H    1 
ATOM   2255 H  HA   . LYS   A 1 148 ? -3.455  22.824  -12.369 1.00 19.50  ? 148 LYS   A HA   1 
ATOM   2256 H  HB2  . LYS   A 1 148 ? -1.211  23.033  -12.795 1.00 21.13  ? 148 LYS   A HB2  1 
ATOM   2257 H  HB3  . LYS   A 1 148 ? -1.335  22.833  -11.230 1.00 21.13  ? 148 LYS   A HB3  1 
ATOM   2258 H  HG2  . LYS   A 1 148 ? -0.733  20.544  -11.517 1.00 24.05  ? 148 LYS   A HG2  1 
ATOM   2259 H  HG3  . LYS   A 1 148 ? -0.505  20.828  -13.062 1.00 24.05  ? 148 LYS   A HG3  1 
ATOM   2260 H  HD2  . LYS   A 1 148 ? 1.234   22.358  -12.498 1.00 35.86  ? 148 LYS   A HD2  1 
ATOM   2261 H  HD3  . LYS   A 1 148 ? 1.040   21.980  -10.965 1.00 35.86  ? 148 LYS   A HD3  1 
ATOM   2262 H  HE2  . LYS   A 1 148 ? 1.627   19.744  -11.501 1.00 49.55  ? 148 LYS   A HE2  1 
ATOM   2263 H  HE3  . LYS   A 1 148 ? 1.930   20.214  -12.976 1.00 49.55  ? 148 LYS   A HE3  1 
ATOM   2264 H  HZ1  . LYS   A 1 148 ? 3.829   20.147  -11.726 1.00 64.37  ? 148 LYS   A HZ1  1 
ATOM   2265 H  HZ2  . LYS   A 1 148 ? 3.586   21.527  -12.195 1.00 64.37  ? 148 LYS   A HZ2  1 
ATOM   2266 H  HZ3  . LYS   A 1 148 ? 3.285   21.158  -10.796 1.00 64.37  ? 148 LYS   A HZ3  1 
ATOM   2267 N  N    . GLN   A 1 149 ? -3.238  19.844  -13.429 1.00 13.20  ? 149 GLN   A N    1 
ATOM   2268 C  CA   . GLN   A 1 149 ? -3.266  18.986  -14.637 1.00 13.65  ? 149 GLN   A CA   1 
ATOM   2269 C  C    . GLN   A 1 149 ? -4.101  17.728  -14.400 1.00 12.12  ? 149 GLN   A C    1 
ATOM   2270 O  O    . GLN   A 1 149 ? -4.537  17.522  -13.256 1.00 13.36  ? 149 GLN   A O    1 
ATOM   2271 C  CB   . GLN   A 1 149 ? -1.837  18.631  -15.045 1.00 13.45  ? 149 GLN   A CB   1 
ATOM   2272 C  CG   . GLN   A 1 149 ? -1.147  17.678  -14.076 1.00 16.71  ? 149 GLN   A CG   1 
ATOM   2273 C  CD   . GLN   A 1 149 ? 0.348   17.882  -14.016 1.00 23.90  ? 149 GLN   A CD   1 
ATOM   2274 O  OE1  . GLN   A 1 149 ? 0.913   18.650  -14.795 1.00 23.93  ? 149 GLN   A OE1  1 
ATOM   2275 N  NE2  . GLN   A 1 149 ? 1.005   17.190  -13.099 1.00 20.62  ? 149 GLN   A NE2  1 
ATOM   2276 H  H    . GLN   A 1 149 ? -3.315  19.430  -12.632 1.00 15.84  ? 149 GLN   A H    1 
ATOM   2277 H  HA   . GLN   A 1 149 ? -3.684  19.497  -15.374 1.00 16.38  ? 149 GLN   A HA   1 
ATOM   2278 H  HB2  . GLN   A 1 149 ? -1.852  18.225  -15.936 1.00 16.14  ? 149 GLN   A HB2  1 
ATOM   2279 H  HB3  . GLN   A 1 149 ? -1.321  19.461  -15.104 1.00 16.14  ? 149 GLN   A HB3  1 
ATOM   2280 H  HG2  . GLN   A 1 149 ? -1.518  17.802  -13.182 1.00 20.06  ? 149 GLN   A HG2  1 
ATOM   2281 H  HG3  . GLN   A 1 149 ? -1.328  16.753  -14.348 1.00 20.06  ? 149 GLN   A HG3  1 
ATOM   2282 H  HE21 . GLN   A 1 149 ? 0.556   16.708  -12.506 1.00 24.75  ? 149 GLN   A HE21 1 
ATOM   2283 H  HE22 . GLN   A 1 149 ? 1.891   17.210  -13.081 1.00 24.75  ? 149 GLN   A HE22 1 
ATOM   2284 N  N    . MET   A 1 150 ? -4.261  16.902  -15.425 1.00 11.67  ? 150 MET   A N    1 
ATOM   2285 C  CA   . MET   A 1 150 ? -5.106  15.713  -15.419 1.00 11.98  ? 150 MET   A CA   1 
ATOM   2286 C  C    . MET   A 1 150 ? -4.172  14.549  -15.664 1.00 12.30  ? 150 MET   A C    1 
ATOM   2287 O  O    . MET   A 1 150 ? -3.344  14.626  -16.564 1.00 15.13  ? 150 MET   A O    1 
ATOM   2288 C  CB   . MET   A 1 150 ? -6.224  15.802  -16.427 1.00 13.29  ? 150 MET   A CB   1 
ATOM   2289 C  CG   . MET   A 1 150 ? -7.327  16.803  -16.016 1.00 14.48  ? 150 MET   A CG   1 
ATOM   2290 S  SD   . MET   A 1 150 ? -6.985  18.566  -16.167 1.00 14.28  ? 150 MET   A SD   1 
ATOM   2291 C  CE   . MET   A 1 150 ? -6.419  18.727  -17.826 1.00 14.95  ? 150 MET   A CE   1 
ATOM   2292 H  H    . MET   A 1 150 ? -3.890  17.024  -16.191 1.00 14.01  ? 150 MET   A H    1 
ATOM   2293 H  HA   . MET   A 1 150 ? -5.570  15.593  -14.576 1.00 14.38  ? 150 MET   A HA   1 
ATOM   2294 H  HB2  . MET   A 1 150 ? -5.859  16.092  -17.278 1.00 15.95  ? 150 MET   A HB2  1 
ATOM   2295 H  HB3  . MET   A 1 150 ? -6.633  14.928  -16.522 1.00 15.95  ? 150 MET   A HB3  1 
ATOM   2296 H  HG2  . MET   A 1 150 ? -8.106  16.625  -16.568 1.00 17.38  ? 150 MET   A HG2  1 
ATOM   2297 H  HG3  . MET   A 1 150 ? -7.538  16.641  -15.083 1.00 17.38  ? 150 MET   A HG3  1 
ATOM   2298 H  HE1  . MET   A 1 150 ? -6.250  19.664  -18.012 1.00 17.94  ? 150 MET   A HE1  1 
ATOM   2299 H  HE2  . MET   A 1 150 ? -5.601  18.217  -17.932 1.00 17.94  ? 150 MET   A HE2  1 
ATOM   2300 H  HE3  . MET   A 1 150 ? -7.101  18.388  -18.427 1.00 17.94  ? 150 MET   A HE3  1 
ATOM   2301 N  N    . THR   A 1 151 ? -4.294  13.467  -14.937 1.00 11.73  ? 151 THR   A N    1 
ATOM   2302 C  CA   . THR   A 1 151 ? -3.411  12.289  -15.035 1.00 12.13  ? 151 THR   A CA   1 
ATOM   2303 C  C    . THR   A 1 151 ? -4.239  11.049  -15.195 1.00 12.03  ? 151 THR   A C    1 
ATOM   2304 O  O    . THR   A 1 151 ? -5.208  10.838  -14.467 1.00 13.28  ? 151 THR   A O    1 
ATOM   2305 C  CB   . THR   A 1 151 ? -2.560  12.202  -13.769 1.00 14.48  ? 151 THR   A CB   1 
ATOM   2306 O  OG1  . THR   A 1 151 ? -1.785  13.426  -13.598 1.00 14.18  ? 151 THR   A OG1  1 
ATOM   2307 C  CG2  . THR   A 1 151 ? -1.581  11.040  -13.772 1.00 14.74  ? 151 THR   A CG2  1 
ATOM   2308 H  H    . THR   A 1 151 ? -4.907  13.367  -14.342 1.00 14.07  ? 151 THR   A H    1 
ATOM   2309 H  HA   . THR   A 1 151 ? -2.839  12.353  -15.816 1.00 14.56  ? 151 THR   A HA   1 
ATOM   2310 H  HB   . THR   A 1 151 ? -3.179  12.067  -13.035 1.00 17.38  ? 151 THR   A HB   1 
ATOM   2311 H  HG1  . THR   A 1 151 ? -1.754  13.635  -12.785 1.00 17.01  ? 151 THR   A HG1  1 
ATOM   2312 H  HG21 . THR   A 1 151 ? -1.044  11.056  -12.965 1.00 17.69  ? 151 THR   A HG21 1 
ATOM   2313 H  HG22 . THR   A 1 151 ? -2.064  10.199  -13.812 1.00 17.69  ? 151 THR   A HG22 1 
ATOM   2314 H  HG23 . THR   A 1 151 ? -0.994  11.102  -14.542 1.00 17.69  ? 151 THR   A HG23 1 
ATOM   2315 N  N    . PHE   A 1 152 ? -3.847  10.215  -16.160 1.00 11.71  ? 152 PHE   A N    1 
ATOM   2316 C  CA   . PHE   A 1 152 ? -4.591  9.020   -16.540 1.00 11.65  ? 152 PHE   A CA   1 
ATOM   2317 C  C    . PHE   A 1 152 ? -3.670  7.819   -16.573 1.00 12.92  ? 152 PHE   A C    1 
ATOM   2318 O  O    . PHE   A 1 152 ? -2.684  7.786   -17.317 1.00 13.47  ? 152 PHE   A O    1 
ATOM   2319 C  CB   . PHE   A 1 152 ? -5.185  9.259   -17.938 1.00 12.87  ? 152 PHE   A CB   1 
ATOM   2320 C  CG   . PHE   A 1 152 ? -6.001  10.533  -18.060 1.00 11.50  ? 152 PHE   A CG   1 
ATOM   2321 C  CD1  . PHE   A 1 152 ? -7.333  10.539  -17.751 1.00 12.12  ? 152 PHE   A CD1  1 
ATOM   2322 C  CD2  . PHE   A 1 152 ? -5.406  11.710  -18.458 1.00 12.49  ? 152 PHE   A CD2  1 
ATOM   2323 C  CE1  . PHE   A 1 152 ? -8.068  11.722  -17.834 1.00 14.17  ? 152 PHE   A CE1  1 
ATOM   2324 C  CE2  . PHE   A 1 152 ? -6.136  12.881  -18.573 1.00 13.18  ? 152 PHE   A CE2  1 
ATOM   2325 C  CZ   . PHE   A 1 152 ? -7.460  12.878  -18.267 1.00 14.17  ? 152 PHE   A CZ   1 
ATOM   2326 H  H    . PHE   A 1 152 ? -3.130  10.327  -16.622 1.00 14.05  ? 152 PHE   A H    1 
ATOM   2327 H  HA   . PHE   A 1 152 ? -5.281  8.827   -15.887 1.00 13.98  ? 152 PHE   A HA   1 
ATOM   2328 H  HB2  . PHE   A 1 152 ? -4.459  9.313   -18.579 1.00 15.44  ? 152 PHE   A HB2  1 
ATOM   2329 H  HB3  . PHE   A 1 152 ? -5.768  8.516   -18.159 1.00 15.44  ? 152 PHE   A HB3  1 
ATOM   2330 H  HD1  . PHE   A 1 152 ? -7.750  9.752   -17.486 1.00 14.54  ? 152 PHE   A HD1  1 
ATOM   2331 H  HD2  . PHE   A 1 152 ? -4.497  11.718  -18.654 1.00 14.98  ? 152 PHE   A HD2  1 
ATOM   2332 H  HE1  . PHE   A 1 152 ? -8.967  11.729  -17.598 1.00 17.01  ? 152 PHE   A HE1  1 
ATOM   2333 H  HE2  . PHE   A 1 152 ? -5.723  13.664  -18.858 1.00 15.82  ? 152 PHE   A HE2  1 
ATOM   2334 H  HZ   . PHE   A 1 152 ? -7.957  13.660  -18.350 1.00 17.01  ? 152 PHE   A HZ   1 
ATOM   2335 N  N    . GLY   A 1 153 ? -4.012  6.803   -15.809 1.00 12.60  ? 153 GLY   A N    1 
ATOM   2336 C  CA   . GLY   A 1 153 ? -3.326  5.531   -15.921 1.00 13.73  ? 153 GLY   A CA   1 
ATOM   2337 C  C    . GLY   A 1 153 ? -3.716  4.741   -17.153 1.00 12.61  ? 153 GLY   A C    1 
ATOM   2338 O  O    . GLY   A 1 153 ? -4.658  5.043   -17.876 1.00 13.27  ? 153 GLY   A O    1 
ATOM   2339 H  H    . GLY   A 1 153 ? -4.638  6.821   -15.219 1.00 15.12  ? 153 GLY   A H    1 
ATOM   2340 H  HA2  . GLY   A 1 153 ? -2.369  5.689   -15.955 1.00 16.48  ? 153 GLY   A HA2  1 
ATOM   2341 H  HA3  . GLY   A 1 153 ? -3.529  4.992   -15.141 1.00 16.48  ? 153 GLY   A HA3  1 
ATOM   2342 N  N    . ASP   A 1 154 ? -2.947  3.689   -17.392 1.00 13.58  ? 154 ASP   A N    1 
ATOM   2343 C  CA   . ASP   A 1 154 ? -3.188  2.734   -18.483 1.00 13.93  ? 154 ASP   A CA   1 
ATOM   2344 C  C    . ASP   A 1 154 ? -4.029  1.561   -18.019 1.00 15.33  ? 154 ASP   A C    1 
ATOM   2345 O  O    . ASP   A 1 154 ? -4.313  0.676   -18.840 1.00 16.55  ? 154 ASP   A O    1 
ATOM   2346 C  CB   . ASP   A 1 154 ? -1.860  2.277   -19.126 1.00 15.23  ? 154 ASP   A CB   1 
ATOM   2347 C  CG   . ASP   A 1 154 ? -1.421  3.191   -20.276 1.00 17.40  ? 154 ASP   A CG   1 
ATOM   2348 O  OD1  . ASP   A 1 154 ? -2.206  3.917   -20.879 1.00 19.41  ? 154 ASP   A OD1  1 
ATOM   2349 O  OD2  . ASP   A 1 154 ? -0.231  3.148   -20.696 1.00 24.66  ? 154 ASP   A OD2  1 
ATOM   2350 H  H    . ASP   A 1 154 ? -2.253  3.493   -16.924 1.00 16.29  ? 154 ASP   A H    1 
ATOM   2351 H  HA   . ASP   A 1 154 ? -3.672  3.171   -19.201 1.00 16.71  ? 154 ASP   A HA   1 
ATOM   2352 H  HB2  . ASP   A 1 154 ? -1.163  2.284   -18.452 1.00 18.27  ? 154 ASP   A HB2  1 
ATOM   2353 H  HB3  . ASP   A 1 154 ? -1.971  1.380   -19.479 1.00 18.27  ? 154 ASP   A HB3  1 
ATOM   2354 N  N    . GLY   A 1 155 ? -4.491  1.527   -16.803 1.00 15.37  ? 155 GLY   A N    1 
ATOM   2355 C  CA   . GLY   A 1 155 ? -5.277  0.406   -16.318 1.00 16.53  ? 155 GLY   A CA   1 
ATOM   2356 C  C    . GLY   A 1 155 ? -4.426  -0.820  -16.105 1.00 19.48  ? 155 GLY   A C    1 
ATOM   2357 O  O    . GLY   A 1 155 ? -3.200  -0.793  -16.174 1.00 20.62  ? 155 GLY   A O    1 
ATOM   2358 H  H    . GLY   A 1 155 ? -4.367  2.145   -16.219 1.00 18.45  ? 155 GLY   A H    1 
ATOM   2359 H  HA2  . GLY   A 1 155 ? -5.693  0.643   -15.475 1.00 19.83  ? 155 GLY   A HA2  1 
ATOM   2360 H  HA3  . GLY   A 1 155 ? -5.969  0.193   -16.963 1.00 19.83  ? 155 GLY   A HA3  1 
ATOM   2361 N  N    . ASP   A 1 156 ? -5.125  -1.936  -15.898 1.00 22.61  ? 156 ASP   A N    1 
ATOM   2362 C  CA   . ASP   A 1 156 ? -4.504  -3.236  -15.671 1.00 24.33  ? 156 ASP   A CA   1 
ATOM   2363 C  C    . ASP   A 1 156 ? -5.555  -4.285  -16.011 1.00 25.70  ? 156 ASP   A C    1 
ATOM   2364 O  O    . ASP   A 1 156 ? -6.096  -4.227  -17.126 1.00 26.67  ? 156 ASP   A O    1 
ATOM   2365 C  CB   . ASP   A 1 156 ? -3.944  -3.332  -14.263 1.00 29.74  ? 156 ASP   A CB   1 
ATOM   2366 C  CG   . ASP   A 1 156 ? -2.684  -4.226  -14.203 1.00 46.28  ? 156 ASP   A CG   1 
ATOM   2367 O  OD1  . ASP   A 1 156 ? -2.327  -4.828  -15.240 1.00 51.66  ? 156 ASP   A OD1  1 
ATOM   2368 O  OD2  . ASP   A 1 156 ? -2.048  -4.327  -13.129 1.00 49.68  ? 156 ASP   A OD2  1 
ATOM   2369 H  H    . ASP   A 1 156 ? -5.984  -1.966  -15.884 1.00 27.13  ? 156 ASP   A H    1 
ATOM   2370 H  HA   . ASP   A 1 156 ? -3.727  -3.391  -16.231 1.00 29.19  ? 156 ASP   A HA   1 
ATOM   2371 H  HB2  . ASP   A 1 156 ? -3.702  -2.445  -13.955 1.00 35.68  ? 156 ASP   A HB2  1 
ATOM   2372 H  HB3  . ASP   A 1 156 ? -4.616  -3.714  -13.678 1.00 35.68  ? 156 ASP   A HB3  1 
ATOM   2373 N  N    . THR   A 1 157 ? -5.871  -5.205  -15.075 1.00 29.31  ? 157 THR   A N    1 
ATOM   2374 C  CA   . THR   A 1 157 ? -6.724  -6.352  -15.399 1.00 33.00  ? 157 THR   A CA   1 
ATOM   2375 C  C    . THR   A 1 157 ? -8.202  -5.984  -15.385 1.00 30.56  ? 157 THR   A C    1 
ATOM   2376 O  O    . THR   A 1 157 ? -9.012  -6.651  -16.036 1.00 36.40  ? 157 THR   A O    1 
ATOM   2377 C  CB   . THR   A 1 157 ? -6.485  -7.530  -14.433 1.00 32.72  ? 157 THR   A CB   1 
ATOM   2378 O  OG1  . THR   A 1 157 ? -6.906  -7.173  -13.114 1.00 37.86  ? 157 THR   A OG1  1 
ATOM   2379 C  CG2  . THR   A 1 157 ? -5.030  -7.899  -14.415 1.00 35.54  ? 157 THR   A CG2  1 
ATOM   2380 H  H    . THR   A 1 157 ? -5.605  -5.182  -14.258 1.00 35.18  ? 157 THR   A H    1 
ATOM   2381 H  HA   . THR   A 1 157 ? -6.479  -6.653  -16.288 1.00 39.60  ? 157 THR   A HA   1 
ATOM   2382 H  HB   . THR   A 1 157 ? -6.995  -8.301  -14.729 1.00 39.26  ? 157 THR   A HB   1 
ATOM   2383 H  HG1  . THR   A 1 157 ? -6.678  -7.769  -12.568 1.00 45.43  ? 157 THR   A HG1  1 
ATOM   2384 H  HG21 . THR   A 1 157 ? -4.888  -8.663  -13.835 1.00 42.64  ? 157 THR   A HG21 1 
ATOM   2385 H  HG22 . THR   A 1 157 ? -4.733  -8.124  -15.310 1.00 42.64  ? 157 THR   A HG22 1 
ATOM   2386 H  HG23 . THR   A 1 157 ? -4.503  -7.153  -14.087 1.00 42.64  ? 157 THR   A HG23 1 
ATOM   2387 N  N    . MET   A 1 158 ? -8.587  -4.971  -14.618 1.00 29.27  ? 158 MET   A N    1 
ATOM   2388 C  CA   . MET   A 1 158 ? -9.984  -4.601  -14.476 1.00 27.14  ? 158 MET   A CA   1 
ATOM   2389 C  C    . MET   A 1 158 ? -10.382 -3.485  -15.435 1.00 23.73  ? 158 MET   A C    1 
ATOM   2390 O  O    . MET   A 1 158 ? -11.574 -3.370  -15.774 1.00 25.51  ? 158 MET   A O    1 
ATOM   2391 C  CB   . MET   A 1 158 ? -10.251 -4.192  -13.024 1.00 32.76  ? 158 MET   A CB   1 
ATOM   2392 C  CG   . MET   A 1 158 ? -11.424 -3.265  -12.783 1.00 49.97  ? 158 MET   A CG   1 
ATOM   2393 S  SD   . MET   A 1 158 ? -12.120 -3.339  -11.097 1.00 138.44 ? 158 MET   A SD   1 
ATOM   2394 C  CE   . MET   A 1 158 ? -10.973 -2.288  -10.191 1.00 45.06  ? 158 MET   A CE   1 
ATOM   2395 H  H    . MET   A 1 158 ? -8.049  -4.477  -14.163 1.00 35.13  ? 158 MET   A H    1 
ATOM   2396 H  HA   . MET   A 1 158 ? -10.556 -5.362  -14.660 1.00 32.56  ? 158 MET   A HA   1 
ATOM   2397 H  HB2  . MET   A 1 158 ? -10.417 -4.998  -12.510 1.00 39.32  ? 158 MET   A HB2  1 
ATOM   2398 H  HB3  . MET   A 1 158 ? -9.460  -3.741  -12.688 1.00 39.32  ? 158 MET   A HB3  1 
ATOM   2399 H  HG2  . MET   A 1 158 ? -11.134 -2.353  -12.939 1.00 59.96  ? 158 MET   A HG2  1 
ATOM   2400 H  HG3  . MET   A 1 158 ? -12.134 -3.498  -13.402 1.00 59.96  ? 158 MET   A HG3  1 
ATOM   2401 H  HE1  . MET   A 1 158 ? -11.245 -2.253  -9.261  1.00 54.08  ? 158 MET   A HE1  1 
ATOM   2402 H  HE2  . MET   A 1 158 ? -10.080 -2.661  -10.262 1.00 54.08  ? 158 MET   A HE2  1 
ATOM   2403 H  HE3  . MET   A 1 158 ? -10.990 -1.398  -10.575 1.00 54.08  ? 158 MET   A HE3  1 
ATOM   2404 N  N    . MET   A 1 159 ? -9.435  -2.597  -15.790 1.00 20.95  ? 159 MET   A N    1 
ATOM   2405 C  CA   . MET   A 1 159 ? -9.729  -1.430  -16.614 1.00 18.13  ? 159 MET   A CA   1 
ATOM   2406 C  C    . MET   A 1 159 ? -8.776  -1.315  -17.823 1.00 19.39  ? 159 MET   A C    1 
ATOM   2407 O  O    . MET   A 1 159 ? -7.570  -1.574  -17.716 1.00 18.98  ? 159 MET   A O    1 
ATOM   2408 C  CB   . MET   A 1 159 ? -9.664  -0.090  -15.878 1.00 20.15  ? 159 MET   A CB   1 
ATOM   2409 C  CG   . MET   A 1 159 ? -10.706 0.016   -14.745 1.00 27.25  ? 159 MET   A CG   1 
ATOM   2410 S  SD   . MET   A 1 159 ? -10.297 1.386   -13.618 1.00 39.80  ? 159 MET   A SD   1 
ATOM   2411 C  CE   . MET   A 1 159 ? -11.737 1.359   -12.545 1.00 47.99  ? 159 MET   A CE   1 
ATOM   2412 H  H    . MET   A 1 159 ? -8.609  -2.658  -15.559 1.00 25.15  ? 159 MET   A H    1 
ATOM   2413 H  HA   . MET   A 1 159 ? -10.641 -1.580  -16.908 1.00 21.76  ? 159 MET   A HA   1 
ATOM   2414 H  HB2  . MET   A 1 159 ? -8.782  0.014   -15.487 1.00 24.18  ? 159 MET   A HB2  1 
ATOM   2415 H  HB3  . MET   A 1 159 ? -9.832  0.627   -16.510 1.00 24.18  ? 159 MET   A HB3  1 
ATOM   2416 H  HG2  . MET   A 1 159 ? -11.583 0.181   -15.126 1.00 32.70  ? 159 MET   A HG2  1 
ATOM   2417 H  HG3  . MET   A 1 159 ? -10.716 -0.810  -14.237 1.00 32.70  ? 159 MET   A HG3  1 
ATOM   2418 H  HE1  . MET   A 1 159 ? -11.638 2.045   -11.866 1.00 57.59  ? 159 MET   A HE1  1 
ATOM   2419 H  HE2  . MET   A 1 159 ? -12.530 1.532   -13.076 1.00 57.59  ? 159 MET   A HE2  1 
ATOM   2420 H  HE3  . MET   A 1 159 ? -11.803 0.487   -12.126 1.00 57.59  ? 159 MET   A HE3  1 
ATOM   2421 N  N    . TYR   A 1 160 ? -9.314  -0.862  -18.960 1.00 15.54  ? 160 TYR   A N    1 
ATOM   2422 C  CA   . TYR   A 1 160 ? -8.553  -0.318  -20.068 1.00 15.92  ? 160 TYR   A CA   1 
ATOM   2423 C  C    . TYR   A 1 160 ? -7.914  1.002   -19.639 1.00 15.70  ? 160 TYR   A C    1 
ATOM   2424 O  O    . TYR   A 1 160 ? -8.288  1.595   -18.602 1.00 15.64  ? 160 TYR   A O    1 
ATOM   2425 C  CB   . TYR   A 1 160 ? -9.512  -0.054  -21.247 1.00 15.58  ? 160 TYR   A CB   1 
ATOM   2426 C  CG   . TYR   A 1 160 ? -10.012 -1.303  -21.896 1.00 15.80  ? 160 TYR   A CG   1 
ATOM   2427 C  CD1  . TYR   A 1 160 ? -9.240  -1.971  -22.812 1.00 17.71  ? 160 TYR   A CD1  1 
ATOM   2428 C  CD2  . TYR   A 1 160 ? -11.267 -1.819  -21.603 1.00 17.51  ? 160 TYR   A CD2  1 
ATOM   2429 C  CE1  . TYR   A 1 160 ? -9.709  -3.118  -23.424 1.00 21.54  ? 160 TYR   A CE1  1 
ATOM   2430 C  CE2  . TYR   A 1 160 ? -11.705 -2.963  -22.189 1.00 19.37  ? 160 TYR   A CE2  1 
ATOM   2431 C  CZ   . TYR   A 1 160 ? -10.933 -3.633  -23.042 1.00 19.40  ? 160 TYR   A CZ   1 
ATOM   2432 O  OH   . TYR   A 1 160 ? -11.382 -4.797  -23.657 1.00 22.92  ? 160 TYR   A OH   1 
ATOM   2433 H  H    . TYR   A 1 160 ? -10.160 -0.862  -19.114 1.00 18.64  ? 160 TYR   A H    1 
ATOM   2434 H  HA   . TYR   A 1 160 ? -7.858  -0.940  -20.338 1.00 19.11  ? 160 TYR   A HA   1 
ATOM   2435 H  HB2  . TYR   A 1 160 ? -10.281 0.440   -20.921 1.00 18.69  ? 160 TYR   A HB2  1 
ATOM   2436 H  HB3  . TYR   A 1 160 ? -9.046  0.465   -21.921 1.00 18.69  ? 160 TYR   A HB3  1 
ATOM   2437 H  HD1  . TYR   A 1 160 ? -8.394  -1.649  -23.022 1.00 21.25  ? 160 TYR   A HD1  1 
ATOM   2438 H  HD2  . TYR   A 1 160 ? -11.815 -1.376  -20.997 1.00 21.01  ? 160 TYR   A HD2  1 
ATOM   2439 H  HE1  . TYR   A 1 160 ? -9.207  -3.537  -24.085 1.00 25.85  ? 160 TYR   A HE1  1 
ATOM   2440 H  HE2  . TYR   A 1 160 ? -12.556 -3.282  -21.992 1.00 23.25  ? 160 TYR   A HE2  1 
ATOM   2441 H  HH   . TYR   A 1 160 ? -10.802 -5.080  -24.194 1.00 27.51  ? 160 TYR   A HH   1 
ATOM   2442 N  N    . PRO   A 1 161 ? -7.045  1.566   -20.463 1.00 13.87  ? 161 PRO   A N    1 
ATOM   2443 C  CA   . PRO   A 1 161 ? -6.519  2.914   -20.195 1.00 12.72  ? 161 PRO   A CA   1 
ATOM   2444 C  C    . PRO   A 1 161 ? -7.650  3.883   -19.929 1.00 13.86  ? 161 PRO   A C    1 
ATOM   2445 O  O    . PRO   A 1 161 ? -8.673  3.884   -20.621 1.00 13.48  ? 161 PRO   A O    1 
ATOM   2446 C  CB   . PRO   A 1 161 ? -5.721  3.222   -21.468 1.00 13.58  ? 161 PRO   A CB   1 
ATOM   2447 C  CG   . PRO   A 1 161 ? -5.156  1.839   -21.895 1.00 13.47  ? 161 PRO   A CG   1 
ATOM   2448 C  CD   . PRO   A 1 161 ? -6.391  0.966   -21.644 1.00 13.33  ? 161 PRO   A CD   1 
ATOM   2449 H  HA   . PRO   A 1 161 ? -5.911  2.934   -19.439 1.00 15.26  ? 161 PRO   A HA   1 
ATOM   2450 H  HB2  . PRO   A 1 161 ? -6.305  3.588   -22.150 1.00 16.30  ? 161 PRO   A HB2  1 
ATOM   2451 H  HB3  . PRO   A 1 161 ? -5.006  3.848   -21.273 1.00 16.30  ? 161 PRO   A HB3  1 
ATOM   2452 H  HG2  . PRO   A 1 161 ? -4.893  1.840   -22.828 1.00 16.16  ? 161 PRO   A HG2  1 
ATOM   2453 H  HG3  . PRO   A 1 161 ? -4.406  1.579   -21.338 1.00 16.16  ? 161 PRO   A HG3  1 
ATOM   2454 H  HD2  . PRO   A 1 161 ? -6.985  0.991   -22.410 1.00 15.99  ? 161 PRO   A HD2  1 
ATOM   2455 H  HD3  . PRO   A 1 161 ? -6.127  0.051   -21.458 1.00 15.99  ? 161 PRO   A HD3  1 
ATOM   2456 N  N    . LEU   A 1 162 ? -7.443  4.750   -18.952 1.00 12.52  ? 162 LEU   A N    1 
ATOM   2457 C  CA   . LEU   A 1 162 ? -8.524  5.598   -18.435 1.00 14.65  ? 162 LEU   A CA   1 
ATOM   2458 C  C    . LEU   A 1 162 ? -8.635  6.885   -19.198 1.00 15.33  ? 162 LEU   A C    1 
ATOM   2459 O  O    . LEU   A 1 162 ? -8.600  7.966   -18.650 1.00 20.02  ? 162 LEU   A O    1 
ATOM   2460 C  CB   . LEU   A 1 162 ? -8.254  5.861   -16.957 1.00 15.76  ? 162 LEU   A CB   1 
ATOM   2461 C  CG   . LEU   A 1 162 ? -8.468  4.735   -15.978 1.00 16.39  ? 162 LEU   A CG   1 
ATOM   2462 C  CD1  . LEU   A 1 162 ? -9.818  4.084   -16.161 1.00 24.99  ? 162 LEU   A CD1  1 
ATOM   2463 C  CD2  . LEU   A 1 162 ? -7.475  3.698   -15.987 1.00 17.52  ? 162 LEU   A CD2  1 
ATOM   2464 H  H    . LEU   A 1 162 ? -6.684  4.872   -18.565 1.00 15.03  ? 162 LEU   A H    1 
ATOM   2465 H  HA   . LEU   A 1 162 ? -9.373  5.138   -18.528 1.00 17.58  ? 162 LEU   A HA   1 
ATOM   2466 H  HB2  . LEU   A 1 162 ? -7.326  6.129   -16.871 1.00 18.91  ? 162 LEU   A HB2  1 
ATOM   2467 H  HB3  . LEU   A 1 162 ? -8.836  6.585   -16.677 1.00 18.91  ? 162 LEU   A HB3  1 
ATOM   2468 H  HG   . LEU   A 1 162 ? -8.404  5.174   -15.115 1.00 19.67  ? 162 LEU   A HG   1 
ATOM   2469 H  HD11 . LEU   A 1 162 ? -10.028 3.564   -15.370 1.00 29.99  ? 162 LEU   A HD11 1 
ATOM   2470 H  HD12 . LEU   A 1 162 ? -10.487 4.774   -16.290 1.00 29.99  ? 162 LEU   A HD12 1 
ATOM   2471 H  HD13 . LEU   A 1 162 ? -9.786  3.504   -16.939 1.00 29.99  ? 162 LEU   A HD13 1 
ATOM   2472 H  HD21 . LEU   A 1 162 ? -7.634  3.100   -15.240 1.00 21.02  ? 162 LEU   A HD21 1 
ATOM   2473 H  HD22 . LEU   A 1 162 ? -7.538  3.208   -16.822 1.00 21.02  ? 162 LEU   A HD22 1 
ATOM   2474 H  HD23 . LEU   A 1 162 ? -6.596  4.101   -15.906 1.00 21.02  ? 162 LEU   A HD23 1 
ATOM   2475 N  N    . VAL   A 1 163 ? -8.760  6.805   -20.490 1.00 17.73  ? 163 VAL   A N    1 
ATOM   2476 C  CA   . VAL   A 1 163 ? -8.811  7.982   -21.332 1.00 15.89  ? 163 VAL   A CA   1 
ATOM   2477 C  C    . VAL   A 1 163 ? -10.004 7.740   -22.199 1.00 18.29  ? 163 VAL   A C    1 
ATOM   2478 O  O    . VAL   A 1 163 ? -9.999  6.813   -23.010 1.00 20.96  ? 163 VAL   A O    1 
ATOM   2479 C  CB   . VAL   A 1 163 ? -7.581  8.169   -22.196 1.00 16.96  ? 163 VAL   A CB   1 
ATOM   2480 C  CG1  . VAL   A 1 163 ? -7.744  9.521   -22.942 1.00 22.29  ? 163 VAL   A CG1  1 
ATOM   2481 C  CG2  . VAL   A 1 163 ? -6.283  8.273   -21.384 1.00 17.99  ? 163 VAL   A CG2  1 
ATOM   2482 H  H    . VAL   A 1 163 ? -8.821  6.064   -20.922 1.00 21.28  ? 163 VAL   A H    1 
ATOM   2483 H  HA   . VAL   A 1 163 ? -8.902  8.783   -20.793 1.00 19.06  ? 163 VAL   A HA   1 
ATOM   2484 H  HB   . VAL   A 1 163 ? -7.508  7.400   -22.783 1.00 20.35  ? 163 VAL   A HB   1 
ATOM   2485 H  HG11 . VAL   A 1 163 ? -6.940  9.698   -23.454 1.00 26.75  ? 163 VAL   A HG11 1 
ATOM   2486 H  HG12 . VAL   A 1 163 ? -8.509  9.463   -23.537 1.00 26.75  ? 163 VAL   A HG12 1 
ATOM   2487 H  HG13 . VAL   A 1 163 ? -7.884  10.226  -22.291 1.00 26.75  ? 163 VAL   A HG13 1 
ATOM   2488 H  HG21 . VAL   A 1 163 ? -5.540  8.412   -21.992 1.00 21.59  ? 163 VAL   A HG21 1 
ATOM   2489 H  HG22 . VAL   A 1 163 ? -6.353  9.022   -20.771 1.00 21.59  ? 163 VAL   A HG22 1 
ATOM   2490 H  HG23 . VAL   A 1 163 ? -6.154  7.450   -20.886 1.00 21.59  ? 163 VAL   A HG23 1 
ATOM   2491 N  N    . SER   A 1 164 ? -11.068 8.420   -21.921 1.00 15.72  ? 164 SER   A N    1 
ATOM   2492 C  CA   . SER   A 1 164 ? -12.339 8.469   -22.658 1.00 16.45  ? 164 SER   A CA   1 
ATOM   2493 C  C    . SER   A 1 164 ? -12.881 9.863   -22.534 1.00 15.33  ? 164 SER   A C    1 
ATOM   2494 O  O    . SER   A 1 164 ? -12.431 10.653  -21.683 1.00 14.74  ? 164 SER   A O    1 
ATOM   2495 C  CB   . SER   A 1 164 ? -13.295 7.401   -22.192 1.00 17.03  ? 164 SER   A CB   1 
ATOM   2496 O  OG   . SER   A 1 164 ? -13.814 7.868   -20.905 1.00 17.74  ? 164 SER   A OG   1 
ATOM   2497 H  H    . SER   A 1 164 ? -11.110 8.932   -21.231 1.00 18.87  ? 164 SER   A H    1 
ATOM   2498 H  HA   . SER   A 1 164 ? -12.197 8.299   -23.603 1.00 19.73  ? 164 SER   A HA   1 
ATOM   2499 H  HB2  . SER   A 1 164 ? -14.019 7.297   -22.829 1.00 20.44  ? 164 SER   A HB2  1 
ATOM   2500 H  HB3  . SER   A 1 164 ? -12.828 6.558   -22.080 1.00 20.44  ? 164 SER   A HB3  1 
ATOM   2501 H  HG   . SER   A 1 164 ? -14.445 7.374   -20.653 1.00 21.28  ? 164 SER   A HG   1 
ATOM   2502 N  N    . LEU   A 1 165 ? -13.899 10.196  -23.320 1.00 15.15  ? 165 LEU   A N    1 
ATOM   2503 C  CA   A LEU   A 1 165 ? -14.486 11.522  -23.184 0.51 14.00  ? 165 LEU   A CA   1 
ATOM   2504 C  CA   B LEU   A 1 165 ? -14.474 11.513  -23.188 0.49 13.98  ? 165 LEU   A CA   1 
ATOM   2505 C  C    . LEU   A 1 165 ? -15.027 11.740  -21.788 1.00 14.32  ? 165 LEU   A C    1 
ATOM   2506 O  O    . LEU   A 1 165 ? -14.845 12.800  -21.185 1.00 15.03  ? 165 LEU   A O    1 
ATOM   2507 C  CB   A LEU   A 1 165 ? -15.655 11.743  -24.152 0.51 18.47  ? 165 LEU   A CB   1 
ATOM   2508 C  CB   B LEU   A 1 165 ? -15.569 11.688  -24.229 0.49 18.74  ? 165 LEU   A CB   1 
ATOM   2509 C  CG   A LEU   A 1 165 ? -15.344 11.997  -25.614 0.51 17.50  ? 165 LEU   A CG   1 
ATOM   2510 C  CG   B LEU   A 1 165 ? -16.249 13.015  -24.252 0.49 16.81  ? 165 LEU   A CG   1 
ATOM   2511 C  CD1  A LEU   A 1 165 ? -16.619 12.441  -26.382 0.51 14.83  ? 165 LEU   A CD1  1 
ATOM   2512 C  CD1  B LEU   A 1 165 ? -15.262 14.179  -24.306 0.49 17.35  ? 165 LEU   A CD1  1 
ATOM   2513 C  CD2  A LEU   A 1 165 ? -14.246 12.998  -25.765 0.51 19.26  ? 165 LEU   A CD2  1 
ATOM   2514 C  CD2  B LEU   A 1 165 ? -17.245 13.067  -25.412 0.49 18.99  ? 165 LEU   A CD2  1 
ATOM   2515 H  H    A LEU   A 1 165 ? -14.256 9.691   -23.918 0.51 18.18  ? 165 LEU   A H    1 
ATOM   2516 H  H    B LEU   A 1 165 ? -14.259 9.691   -23.915 0.49 18.18  ? 165 LEU   A H    1 
ATOM   2517 H  HA   . LEU   A 1 165 ? -13.778 12.152  -23.392 1.00 16.77  ? 165 LEU   A HA   1 
ATOM   2518 H  HB2  A LEU   A 1 165 ? -16.214 10.951  -24.122 0.51 22.16  ? 165 LEU   A HB2  1 
ATOM   2519 H  HB2  B LEU   A 1 165 ? -15.177 11.552  -25.106 0.49 22.49  ? 165 LEU   A HB2  1 
ATOM   2520 H  HB3  A LEU   A 1 165 ? -16.154 12.513  -23.838 0.51 22.16  ? 165 LEU   A HB3  1 
ATOM   2521 H  HB3  B LEU   A 1 165 ? -16.252 11.019  -24.064 0.49 22.49  ? 165 LEU   A HB3  1 
ATOM   2522 H  HG   A LEU   A 1 165 ? -15.035 11.168  -26.012 0.51 21.00  ? 165 LEU   A HG   1 
ATOM   2523 H  HG   B LEU   A 1 165 ? -16.736 13.124  -23.420 0.49 20.17  ? 165 LEU   A HG   1 
ATOM   2524 H  HD11 A LEU   A 1 165 ? -16.396 12.570  -27.317 0.51 17.80  ? 165 LEU   A HD11 1 
ATOM   2525 H  HD11 B LEU   A 1 165 ? -15.743 15.009  -24.160 0.49 20.82  ? 165 LEU   A HD11 1 
ATOM   2526 H  HD12 A LEU   A 1 165 ? -17.296 11.751  -26.296 0.51 17.80  ? 165 LEU   A HD12 1 
ATOM   2527 H  HD12 B LEU   A 1 165 ? -14.593 14.059  -23.614 0.49 20.82  ? 165 LEU   A HD12 1 
ATOM   2528 H  HD13 A LEU   A 1 165 ? -16.944 13.271  -26.001 0.51 17.80  ? 165 LEU   A HD13 1 
ATOM   2529 H  HD13 B LEU   A 1 165 ? -14.837 14.193  -25.178 0.49 20.82  ? 165 LEU   A HD13 1 
ATOM   2530 H  HD21 A LEU   A 1 165 ? -14.171 13.246  -26.700 0.51 23.11  ? 165 LEU   A HD21 1 
ATOM   2531 H  HD21 B LEU   A 1 165 ? -17.737 13.902  -25.369 0.49 22.79  ? 165 LEU   A HD21 1 
ATOM   2532 H  HD22 A LEU   A 1 165 ? -14.456 13.780  -25.231 0.51 23.11  ? 165 LEU   A HD22 1 
ATOM   2533 H  HD22 B LEU   A 1 165 ? -16.757 13.014  -26.249 0.49 22.79  ? 165 LEU   A HD22 1 
ATOM   2534 H  HD23 A LEU   A 1 165 ? -13.414 12.603  -25.460 0.51 23.11  ? 165 LEU   A HD23 1 
ATOM   2535 H  HD23 B LEU   A 1 165 ? -17.857 12.319  -25.338 0.49 22.79  ? 165 LEU   A HD23 1 
ATOM   2536 N  N    . GLY   A 1 166 ? -15.728 10.758  -21.236 1.00 13.83  ? 166 GLY   A N    1 
ATOM   2537 C  CA   . GLY   A 1 166 ? -16.327 10.940  -19.926 1.00 14.31  ? 166 GLY   A CA   1 
ATOM   2538 C  C    . GLY   A 1 166 ? -15.278 11.086  -18.841 1.00 14.25  ? 166 GLY   A C    1 
ATOM   2539 O  O    . GLY   A 1 166 ? -15.370 11.954  -17.971 1.00 14.24  ? 166 GLY   A O    1 
ATOM   2540 H  H    . GLY   A 1 166 ? -15.868 9.988   -21.593 1.00 16.60  ? 166 GLY   A H    1 
ATOM   2541 H  HA2  . GLY   A 1 166 ? -16.878 11.738  -19.931 1.00 17.17  ? 166 GLY   A HA2  1 
ATOM   2542 H  HA3  . GLY   A 1 166 ? -16.883 10.174  -19.716 1.00 17.17  ? 166 GLY   A HA3  1 
ATOM   2543 N  N    . VAL   A 1 167 ? -14.239 10.237  -18.880 1.00 13.59  ? 167 VAL   A N    1 
ATOM   2544 C  CA   . VAL   A 1 167 ? -13.200 10.340  -17.850 1.00 13.99  ? 167 VAL   A CA   1 
ATOM   2545 C  C    . VAL   A 1 167 ? -12.467 11.662  -17.997 1.00 13.14  ? 167 VAL   A C    1 
ATOM   2546 O  O    . VAL   A 1 167 ? -12.157 12.347  -16.999 1.00 13.45  ? 167 VAL   A O    1 
ATOM   2547 C  CB   . VAL   A 1 167 ? -12.201 9.155   -17.888 1.00 14.19  ? 167 VAL   A CB   1 
ATOM   2548 C  CG1  . VAL   A 1 167 ? -11.121 9.344   -16.853 1.00 17.39  ? 167 VAL   A CG1  1 
ATOM   2549 C  CG2  . VAL   A 1 167 ? -12.889 7.849   -17.595 1.00 19.95  ? 167 VAL   A CG2  1 
ATOM   2550 H  H    . VAL   A 1 167 ? -14.119 9.620   -19.467 1.00 16.31  ? 167 VAL   A H    1 
ATOM   2551 H  HA   . VAL   A 1 167 ? -13.648 10.301  -16.990 1.00 16.79  ? 167 VAL   A HA   1 
ATOM   2552 H  HB   . VAL   A 1 167 ? -11.819 9.128   -18.779 1.00 17.03  ? 167 VAL   A HB   1 
ATOM   2553 H  HG11 . VAL   A 1 167 ? -10.629 8.514   -16.756 1.00 20.86  ? 167 VAL   A HG11 1 
ATOM   2554 H  HG12 . VAL   A 1 167 ? -10.524 10.050  -17.146 1.00 20.86  ? 167 VAL   A HG12 1 
ATOM   2555 H  HG13 . VAL   A 1 167 ? -11.531 9.587   -16.009 1.00 20.86  ? 167 VAL   A HG13 1 
ATOM   2556 H  HG21 . VAL   A 1 167 ? -12.235 7.133   -17.628 1.00 23.95  ? 167 VAL   A HG21 1 
ATOM   2557 H  HG22 . VAL   A 1 167 ? -13.288 7.892   -16.712 1.00 23.95  ? 167 VAL   A HG22 1 
ATOM   2558 H  HG23 . VAL   A 1 167 ? -13.577 7.698   -18.262 1.00 23.95  ? 167 VAL   A HG23 1 
ATOM   2559 N  N    . GLY   A 1 168 ? -12.142 12.063  -19.211 1.00 14.16  ? 168 GLY   A N    1 
ATOM   2560 C  CA   . GLY   A 1 168 ? -11.537 13.368  -19.417 1.00 14.52  ? 168 GLY   A CA   1 
ATOM   2561 C  C    . GLY   A 1 168 ? -12.394 14.512  -18.931 1.00 12.74  ? 168 GLY   A C    1 
ATOM   2562 O  O    . GLY   A 1 168 ? -11.896 15.401  -18.228 1.00 14.70  ? 168 GLY   A O    1 
ATOM   2563 H  H    . GLY   A 1 168 ? -12.259 11.605  -19.929 1.00 16.99  ? 168 GLY   A H    1 
ATOM   2564 H  HA2  . GLY   A 1 168 ? -10.691 13.403  -18.945 1.00 17.42  ? 168 GLY   A HA2  1 
ATOM   2565 H  HA3  . GLY   A 1 168 ? -11.375 13.495  -20.365 1.00 17.42  ? 168 GLY   A HA3  1 
ATOM   2566 N  N    . GLY   A 1 169 ? -13.682 14.494  -19.207 1.00 12.88  ? 169 GLY   A N    1 
ATOM   2567 C  CA   . GLY   A 1 169 ? -14.581 15.517  -18.731 1.00 13.18  ? 169 GLY   A CA   1 
ATOM   2568 C  C    . GLY   A 1 169 ? -14.660 15.546  -17.222 1.00 13.66  ? 169 GLY   A C    1 
ATOM   2569 O  O    . GLY   A 1 169 ? -14.678 16.621  -16.593 1.00 13.96  ? 169 GLY   A O    1 
ATOM   2570 H  H    . GLY   A 1 169 ? -14.068 13.887  -19.679 1.00 15.45  ? 169 GLY   A H    1 
ATOM   2571 H  HA2  . GLY   A 1 169 ? -14.274 16.384  -19.039 1.00 15.81  ? 169 GLY   A HA2  1 
ATOM   2572 H  HA3  . GLY   A 1 169 ? -15.470 15.353  -19.082 1.00 15.81  ? 169 GLY   A HA3  1 
ATOM   2573 N  N    . HIS   A 1 170 ? -14.660 14.376  -16.585 1.00 12.79  ? 170 HIS   A N    1 
ATOM   2574 C  CA   . HIS   A 1 170 ? -14.650 14.273  -15.143 1.00 11.92  ? 170 HIS   A CA   1 
ATOM   2575 C  C    . HIS   A 1 170 ? -13.430 14.967  -14.587 1.00 11.40  ? 170 HIS   A C    1 
ATOM   2576 O  O    . HIS   A 1 170 ? -13.513 15.776  -13.673 1.00 11.92  ? 170 HIS   A O    1 
ATOM   2577 C  CB   . HIS   A 1 170 ? -14.705 12.785  -14.742 1.00 12.15  ? 170 HIS   A CB   1 
ATOM   2578 C  CG   . HIS   A 1 170 ? -14.647 12.534  -13.287 1.00 11.92  ? 170 HIS   A CG   1 
ATOM   2579 N  ND1  . HIS   A 1 170 ? -15.700 12.069  -12.524 1.00 11.61  ? 170 HIS   A ND1  1 
ATOM   2580 C  CD2  . HIS   A 1 170 ? -13.619 12.671  -12.445 1.00 12.77  ? 170 HIS   A CD2  1 
ATOM   2581 C  CE1  . HIS   A 1 170 ? -15.303 11.952  -11.285 1.00 11.11  ? 170 HIS   A CE1  1 
ATOM   2582 N  NE2  . HIS   A 1 170 ? -14.055 12.348  -11.217 1.00 11.75  ? 170 HIS   A NE2  1 
ATOM   2583 H  H    . HIS   A 1 170 ? -14.665 13.612  -16.980 1.00 15.35  ? 170 HIS   A H    1 
ATOM   2584 H  HA   . HIS   A 1 170 ? -15.432 14.703  -14.762 1.00 14.30  ? 170 HIS   A HA   1 
ATOM   2585 H  HB2  . HIS   A 1 170 ? -15.537 12.408  -15.070 1.00 14.59  ? 170 HIS   A HB2  1 
ATOM   2586 H  HB3  . HIS   A 1 170 ? -13.951 12.328  -15.147 1.00 14.59  ? 170 HIS   A HB3  1 
ATOM   2587 H  HD1  . HIS   A 1 170 ? -16.488 11.887  -12.816 1.00 13.93  ? 170 HIS   A HD1  1 
ATOM   2588 H  HD2  . HIS   A 1 170 ? -12.758 12.940  -12.669 1.00 15.32  ? 170 HIS   A HD2  1 
ATOM   2589 H  HE1  . HIS   A 1 170 ? -15.817 11.642  -10.575 1.00 13.33  ? 170 HIS   A HE1  1 
ATOM   2590 N  N    . GLU   A 1 171 ? -12.247 14.612  -15.067 1.00 11.08  ? 171 GLU   A N    1 
ATOM   2591 C  CA   . GLU   A 1 171 ? -11.030 15.114  -14.442 1.00 10.96  ? 171 GLU   A CA   1 
ATOM   2592 C  C    . GLU   A 1 171 ? -10.851 16.599  -14.661 1.00 10.57  ? 171 GLU   A C    1 
ATOM   2593 O  O    . GLU   A 1 171 ? -10.478 17.322  -13.732 1.00 11.46  ? 171 GLU   A O    1 
ATOM   2594 C  CB   . GLU   A 1 171 ? -9.766  14.356  -14.912 1.00 13.08  ? 171 GLU   A CB   1 
ATOM   2595 C  CG   . GLU   A 1 171 ? -9.812  12.875  -14.653 1.00 16.19  ? 171 GLU   A CG   1 
ATOM   2596 C  CD   . GLU   A 1 171 ? -10.071 12.398  -13.312 1.00 21.06  ? 171 GLU   A CD   1 
ATOM   2597 O  OE1  . GLU   A 1 171 ? -10.065 13.143  -12.334 1.00 18.58  ? 171 GLU   A OE1  1 
ATOM   2598 O  OE2  . GLU   A 1 171 ? -10.465 11.193  -13.258 1.00 20.08  ? 171 GLU   A OE2  1 
ATOM   2599 H  H    . GLU   A 1 171 ? -12.121 14.092  -15.740 1.00 13.30  ? 171 GLU   A H    1 
ATOM   2600 H  HA   . GLU   A 1 171 ? -11.125 14.946  -13.491 1.00 13.15  ? 171 GLU   A HA   1 
ATOM   2601 H  HB2  . GLU   A 1 171 ? -9.663  14.485  -15.868 1.00 15.69  ? 171 GLU   A HB2  1 
ATOM   2602 H  HB3  . GLU   A 1 171 ? -8.997  14.714  -14.443 1.00 15.69  ? 171 GLU   A HB3  1 
ATOM   2603 H  HG2  . GLU   A 1 171 ? -10.511 12.503  -15.213 1.00 19.43  ? 171 GLU   A HG2  1 
ATOM   2604 H  HG3  . GLU   A 1 171 ? -8.951  12.509  -14.909 1.00 19.43  ? 171 GLU   A HG3  1 
ATOM   2605 N  N    . VAL   A 1 172 ? -11.078 17.094  -15.871 1.00 11.24  ? 172 VAL   A N    1 
ATOM   2606 C  CA   . VAL   A 1 172 ? -10.966 18.522  -16.125 1.00 11.60  ? 172 VAL   A CA   1 
ATOM   2607 C  C    . VAL   A 1 172 ? -11.920 19.285  -15.233 1.00 10.82  ? 172 VAL   A C    1 
ATOM   2608 O  O    . VAL   A 1 172 ? -11.633 20.369  -14.723 1.00 12.08  ? 172 VAL   A O    1 
ATOM   2609 C  CB   . VAL   A 1 172 ? -11.241 18.822  -17.599 1.00 12.30  ? 172 VAL   A CB   1 
ATOM   2610 C  CG1  . VAL   A 1 172 ? -11.344 20.331  -17.810 1.00 14.47  ? 172 VAL   A CG1  1 
ATOM   2611 C  CG2  . VAL   A 1 172 ? -10.156 18.205  -18.512 1.00 12.60  ? 172 VAL   A CG2  1 
ATOM   2612 H  H    . VAL   A 1 172 ? -11.299 16.627  -16.559 1.00 13.49  ? 172 VAL   A H    1 
ATOM   2613 H  HA   . VAL   A 1 172 ? -10.059 18.800  -15.920 1.00 13.92  ? 172 VAL   A HA   1 
ATOM   2614 H  HB   . VAL   A 1 172 ? -12.086 18.417  -17.851 1.00 14.76  ? 172 VAL   A HB   1 
ATOM   2615 H  HG11 . VAL   A 1 172 ? -11.306 20.521  -18.760 1.00 17.37  ? 172 VAL   A HG11 1 
ATOM   2616 H  HG12 . VAL   A 1 172 ? -12.186 20.644  -17.444 1.00 17.37  ? 172 VAL   A HG12 1 
ATOM   2617 H  HG13 . VAL   A 1 172 ? -10.605 20.765  -17.356 1.00 17.37  ? 172 VAL   A HG13 1 
ATOM   2618 H  HG21 . VAL   A 1 172 ? -10.418 18.324  -19.438 1.00 15.12  ? 172 VAL   A HG21 1 
ATOM   2619 H  HG22 . VAL   A 1 172 ? -9.312  18.653  -18.347 1.00 15.12  ? 172 VAL   A HG22 1 
ATOM   2620 H  HG23 . VAL   A 1 172 ? -10.074 17.260  -18.310 1.00 15.12  ? 172 VAL   A HG23 1 
ATOM   2621 N  N    . SER   A 1 173 ? -13.109 18.706  -15.017 1.00 10.43  ? 173 SER   A N    1 
ATOM   2622 C  CA   . SER   A 1 173 ? -14.137 19.410  -14.266 1.00 11.47  ? 173 SER   A CA   1 
ATOM   2623 C  C    . SER   A 1 173 ? -13.801 19.490  -12.783 1.00 11.34  ? 173 SER   A C    1 
ATOM   2624 O  O    . SER   A 1 173 ? -14.341 20.349  -12.084 1.00 11.67  ? 173 SER   A O    1 
ATOM   2625 C  CB   . SER   A 1 173 ? -15.494 18.780  -14.512 1.00 12.01  ? 173 SER   A CB   1 
ATOM   2626 O  OG   . SER   A 1 173 ? -15.863 19.009  -15.860 1.00 12.14  ? 173 SER   A OG   1 
ATOM   2627 H  H    . SER   A 1 173 ? -13.334 17.923  -15.291 1.00 12.52  ? 173 SER   A H    1 
ATOM   2628 H  HA   . SER   A 1 173 ? -14.205 20.323  -14.587 1.00 13.76  ? 173 SER   A HA   1 
ATOM   2629 H  HB2  . SER   A 1 173 ? -15.443 17.825  -14.347 1.00 14.41  ? 173 SER   A HB2  1 
ATOM   2630 H  HB3  . SER   A 1 173 ? -16.150 19.184  -13.922 1.00 14.41  ? 173 SER   A HB3  1 
ATOM   2631 H  HG   . SER   A 1 173 ? -15.277 18.699  -16.376 1.00 14.57  ? 173 SER   A HG   1 
ATOM   2632 N  N    . HIS   A 1 174 ? -12.870 18.680  -12.245 1.00 10.27  ? 174 HIS   A N    1 
ATOM   2633 C  CA   . HIS   A 1 174 ? -12.353 18.927  -10.906 1.00 10.98  ? 174 HIS   A CA   1 
ATOM   2634 C  C    . HIS   A 1 174 ? -11.651 20.274  -10.851 1.00 10.71  ? 174 HIS   A C    1 
ATOM   2635 O  O    . HIS   A 1 174 ? -11.707 20.979  -9.848  1.00 11.64  ? 174 HIS   A O    1 
ATOM   2636 C  CB   . HIS   A 1 174 ? -11.372 17.839  -10.490 1.00 11.64  ? 174 HIS   A CB   1 
ATOM   2637 C  CG   . HIS   A 1 174 ? -12.003 16.599  -9.961  1.00 10.63  ? 174 HIS   A CG   1 
ATOM   2638 N  ND1  . HIS   A 1 174 ? -12.930 16.578  -8.941  1.00 12.20  ? 174 HIS   A ND1  1 
ATOM   2639 C  CD2  . HIS   A 1 174 ? -11.822 15.322  -10.325 1.00 10.52  ? 174 HIS   A CD2  1 
ATOM   2640 C  CE1  . HIS   A 1 174 ? -13.275 15.331  -8.703  1.00 12.57  ? 174 HIS   A CE1  1 
ATOM   2641 N  NE2  . HIS   A 1 174 ? -12.600 14.531  -9.517  1.00 13.47  ? 174 HIS   A NE2  1 
ATOM   2642 H  H    . HIS   A 1 174 ? -12.532 17.993  -12.636 1.00 12.33  ? 174 HIS   A H    1 
ATOM   2643 H  HA   . HIS   A 1 174 ? -13.098 18.915  -10.285 1.00 13.18  ? 174 HIS   A HA   1 
ATOM   2644 H  HB2  . HIS   A 1 174 ? -10.843 17.589  -11.264 1.00 13.97  ? 174 HIS   A HB2  1 
ATOM   2645 H  HB3  . HIS   A 1 174 ? -10.796 18.192  -9.795  1.00 13.97  ? 174 HIS   A HB3  1 
ATOM   2646 H  HD1  . HIS   A 1 174 ? -13.234 17.268  -8.527  1.00 14.63  ? 174 HIS   A HD1  1 
ATOM   2647 H  HD2  . HIS   A 1 174 ? -11.266 15.023  -11.008 1.00 12.63  ? 174 HIS   A HD2  1 
ATOM   2648 H  HE1  . HIS   A 1 174 ? -13.892 15.054  -8.065  1.00 15.09  ? 174 HIS   A HE1  1 
ATOM   2649 N  N    . GLY   A 1 175 ? -10.955 20.646  -11.935 1.00 11.14  ? 175 GLY   A N    1 
ATOM   2650 C  CA   . GLY   A 1 175 ? -10.333 21.949  -11.998 1.00 13.43  ? 175 GLY   A CA   1 
ATOM   2651 C  C    . GLY   A 1 175 ? -11.364 23.064  -12.103 1.00 11.33  ? 175 GLY   A C    1 
ATOM   2652 O  O    . GLY   A 1 175 ? -11.226 24.107  -11.463 1.00 13.21  ? 175 GLY   A O    1 
ATOM   2653 H  H    . GLY   A 1 175 ? -10.835 20.160  -12.635 1.00 13.37  ? 175 GLY   A H    1 
ATOM   2654 H  HA2  . GLY   A 1 175 ? -9.804  22.093  -11.198 1.00 16.12  ? 175 GLY   A HA2  1 
ATOM   2655 H  HA3  . GLY   A 1 175 ? -9.751  21.992  -12.773 1.00 16.12  ? 175 GLY   A HA3  1 
ATOM   2656 N  N    . PHE   A 1 176 ? -12.397 22.849  -12.917 1.00 12.04  ? 176 PHE   A N    1 
ATOM   2657 C  CA   . PHE   A 1 176 ? -13.490 23.808  -13.004 1.00 12.58  ? 176 PHE   A CA   1 
ATOM   2658 C  C    . PHE   A 1 176 ? -14.087 24.077  -11.627 1.00 12.23  ? 176 PHE   A C    1 
ATOM   2659 O  O    . PHE   A 1 176 ? -14.225 25.226  -11.184 1.00 12.58  ? 176 PHE   A O    1 
ATOM   2660 C  CB   . PHE   A 1 176 ? -14.536 23.310  -13.979 1.00 12.63  ? 176 PHE   A CB   1 
ATOM   2661 C  CG   . PHE   A 1 176 ? -15.674 24.302  -14.189 1.00 12.69  ? 176 PHE   A CG   1 
ATOM   2662 C  CD1  . PHE   A 1 176 ? -15.575 25.252  -15.162 1.00 13.29  ? 176 PHE   A CD1  1 
ATOM   2663 C  CD2  . PHE   A 1 176 ? -16.813 24.278  -13.407 1.00 14.47  ? 176 PHE   A CD2  1 
ATOM   2664 C  CE1  . PHE   A 1 176 ? -16.585 26.181  -15.367 1.00 14.83  ? 176 PHE   A CE1  1 
ATOM   2665 C  CE2  . PHE   A 1 176 ? -17.814 25.233  -13.631 1.00 14.29  ? 176 PHE   A CE2  1 
ATOM   2666 C  CZ   . PHE   A 1 176 ? -17.685 26.178  -14.602 1.00 15.36  ? 176 PHE   A CZ   1 
ATOM   2667 H  H    . PHE   A 1 176 ? -12.488 22.160  -13.424 1.00 14.45  ? 176 PHE   A H    1 
ATOM   2668 H  HA   . PHE   A 1 176 ? -13.153 24.651  -13.346 1.00 15.10  ? 176 PHE   A HA   1 
ATOM   2669 H  HB2  . PHE   A 1 176 ? -14.115 23.150  -14.838 1.00 15.15  ? 176 PHE   A HB2  1 
ATOM   2670 H  HB3  . PHE   A 1 176 ? -14.916 22.485  -13.638 1.00 15.15  ? 176 PHE   A HB3  1 
ATOM   2671 H  HD1  . PHE   A 1 176 ? -14.816 25.277  -15.698 1.00 15.95  ? 176 PHE   A HD1  1 
ATOM   2672 H  HD2  . PHE   A 1 176 ? -16.915 23.637  -12.741 1.00 17.36  ? 176 PHE   A HD2  1 
ATOM   2673 H  HE1  . PHE   A 1 176 ? -16.498 26.813  -16.043 1.00 17.80  ? 176 PHE   A HE1  1 
ATOM   2674 H  HE2  . PHE   A 1 176 ? -18.582 25.221  -13.107 1.00 17.15  ? 176 PHE   A HE2  1 
ATOM   2675 H  HZ   . PHE   A 1 176 ? -18.351 26.814  -14.733 1.00 18.43  ? 176 PHE   A HZ   1 
ATOM   2676 N  N    . THR   A 1 177 ? -14.334 23.015  -10.864 1.00 11.56  ? 177 THR   A N    1 
ATOM   2677 C  CA   . THR   A 1 177 ? -14.867 23.177  -9.512  1.00 10.97  ? 177 THR   A CA   1 
ATOM   2678 C  C    . THR   A 1 177 ? -13.868 23.901  -8.626  1.00 10.99  ? 177 THR   A C    1 
ATOM   2679 O  O    . THR   A 1 177 ? -14.240 24.813  -7.896  1.00 12.79  ? 177 THR   A O    1 
ATOM   2680 C  CB   . THR   A 1 177 ? -15.253 21.809  -8.942  1.00 11.28  ? 177 THR   A CB   1 
ATOM   2681 O  OG1  . THR   A 1 177 ? -16.342 21.355  -9.721  1.00 12.15  ? 177 THR   A OG1  1 
ATOM   2682 C  CG2  . THR   A 1 177 ? -15.613 21.852  -7.467  1.00 13.01  ? 177 THR   A CG2  1 
ATOM   2683 H  H    . THR   A 1 177 ? -14.204 22.199  -11.101 1.00 13.87  ? 177 THR   A H    1 
ATOM   2684 H  HA   . THR   A 1 177 ? -15.674 23.715  -9.539  1.00 13.16  ? 177 THR   A HA   1 
ATOM   2685 H  HB   . THR   A 1 177 ? -14.502 21.196  -8.984  1.00 13.53  ? 177 THR   A HB   1 
ATOM   2686 H  HG1  . THR   A 1 177 ? -16.549 20.572  -9.497  1.00 14.58  ? 177 THR   A HG1  1 
ATOM   2687 H  HG21 . THR   A 1 177 ? -15.931 20.982  -7.178  1.00 15.61  ? 177 THR   A HG21 1 
ATOM   2688 H  HG22 . THR   A 1 177 ? -14.834 22.093  -6.942  1.00 15.61  ? 177 THR   A HG22 1 
ATOM   2689 H  HG23 . THR   A 1 177 ? -16.311 22.509  -7.315  1.00 15.61  ? 177 THR   A HG23 1 
ATOM   2690 N  N    . GLU   A 1 178 ? -12.601 23.493  -8.622  1.00 11.31  ? 178 GLU   A N    1 
ATOM   2691 C  CA   A GLU   A 1 178 ? -11.616 24.136  -7.762  0.49 13.37  ? 178 GLU   A CA   1 
ATOM   2692 C  CA   B GLU   A 1 178 ? -11.615 24.136  -7.763  0.51 13.37  ? 178 GLU   A CA   1 
ATOM   2693 C  C    . GLU   A 1 178 ? -11.570 25.636  -7.989  1.00 14.00  ? 178 GLU   A C    1 
ATOM   2694 O  O    . GLU   A 1 178 ? -11.368 26.398  -7.045  1.00 14.91  ? 178 GLU   A O    1 
ATOM   2695 C  CB   A GLU   A 1 178 ? -10.248 23.513  -8.006  0.49 13.51  ? 178 GLU   A CB   1 
ATOM   2696 C  CB   B GLU   A 1 178 ? -10.248 23.512  -8.010  0.51 13.53  ? 178 GLU   A CB   1 
ATOM   2697 C  CG   A GLU   A 1 178 ? -9.130  24.045  -7.101  0.49 14.18  ? 178 GLU   A CG   1 
ATOM   2698 C  CG   B GLU   A 1 178 ? -9.114  24.065  -7.132  0.51 14.18  ? 178 GLU   A CG   1 
ATOM   2699 C  CD   A GLU   A 1 178 ? -7.845  23.284  -7.345  0.49 21.38  ? 178 GLU   A CD   1 
ATOM   2700 C  CD   B GLU   A 1 178 ? -7.838  23.288  -7.374  0.51 21.37  ? 178 GLU   A CD   1 
ATOM   2701 O  OE1  A GLU   A 1 178 ? -7.785  22.062  -7.064  0.49 21.38  ? 178 GLU   A OE1  1 
ATOM   2702 O  OE1  B GLU   A 1 178 ? -7.785  22.070  -7.082  0.51 21.39  ? 178 GLU   A OE1  1 
ATOM   2703 O  OE2  A GLU   A 1 178 ? -6.885  23.913  -7.818  0.49 34.53  ? 178 GLU   A OE2  1 
ATOM   2704 O  OE2  B GLU   A 1 178 ? -6.879  23.901  -7.866  0.51 34.53  ? 178 GLU   A OE2  1 
ATOM   2705 H  H    A GLU   A 1 178 ? -12.290 22.851  -9.103  0.49 13.57  ? 178 GLU   A H    1 
ATOM   2706 H  H    B GLU   A 1 178 ? -12.291 22.851  -9.103  0.51 13.57  ? 178 GLU   A H    1 
ATOM   2707 H  HA   . GLU   A 1 178 ? -11.861 23.989  -6.835  1.00 16.05  ? 178 GLU   A HA   1 
ATOM   2708 H  HB2  A GLU   A 1 178 ? -10.315 22.557  -7.857  0.49 16.21  ? 178 GLU   A HB2  1 
ATOM   2709 H  HB2  B GLU   A 1 178 ? -10.310 22.559  -7.839  0.51 16.24  ? 178 GLU   A HB2  1 
ATOM   2710 H  HB3  A GLU   A 1 178 ? -9.989  23.688  -8.924  0.49 16.21  ? 178 GLU   A HB3  1 
ATOM   2711 H  HB3  B GLU   A 1 178 ? -10.002 23.668  -8.935  0.51 16.24  ? 178 GLU   A HB3  1 
ATOM   2712 H  HG2  A GLU   A 1 178 ? -8.975  24.983  -7.293  0.49 17.01  ? 178 GLU   A HG2  1 
ATOM   2713 H  HG2  B GLU   A 1 178 ? -8.957  24.997  -7.351  0.51 17.02  ? 178 GLU   A HG2  1 
ATOM   2714 H  HG3  A GLU   A 1 178 ? -9.384  23.934  -6.171  0.49 17.01  ? 178 GLU   A HG3  1 
ATOM   2715 H  HG3  B GLU   A 1 178 ? -9.355  23.981  -6.196  0.51 17.02  ? 178 GLU   A HG3  1 
ATOM   2716 N  N    . GLN   A 1 179 ? -11.775 26.059  -9.236  1.00 12.69  ? 179 GLN   A N    1 
ATOM   2717 C  CA   . GLN   A 1 179 ? -11.550 27.457  -9.682  1.00 13.12  ? 179 GLN   A CA   1 
ATOM   2718 C  C    . GLN   A 1 179 ? -12.859 28.250  -9.553  1.00 13.94  ? 179 GLN   A C    1 
ATOM   2719 O  O    . GLN   A 1 179 ? -12.820 29.471  -9.796  1.00 17.08  ? 179 GLN   A O    1 
ATOM   2720 C  CB   . GLN   A 1 179 ? -10.996 27.423  -11.106 1.00 14.05  ? 179 GLN   A CB   1 
ATOM   2721 C  CG   . GLN   A 1 179 ? -9.575  26.873  -11.179 1.00 14.23  ? 179 GLN   A CG   1 
ATOM   2722 C  CD   . GLN   A 1 179 ? -9.056  26.715  -12.591 1.00 16.91  ? 179 GLN   A CD   1 
ATOM   2723 O  OE1  . GLN   A 1 179 ? -9.724  27.065  -13.567 1.00 16.16  ? 179 GLN   A OE1  1 
ATOM   2724 N  NE2  . GLN   A 1 179 ? -7.846  26.190  -12.711 1.00 20.98  ? 179 GLN   A NE2  1 
ATOM   2725 H  H    . GLN   A 1 179 ? -12.088 25.503  -9.873  1.00 15.23  ? 179 GLN   A H    1 
ATOM   2726 H  HA   . GLN   A 1 179 ? -10.870 27.868  -9.092  1.00 15.75  ? 179 GLN   A HA   1 
ATOM   2727 H  HB2  . GLN   A 1 179 ? -11.584 26.867  -11.658 1.00 16.85  ? 179 GLN   A HB2  1 
ATOM   2728 H  HB3  . GLN   A 1 179 ? -11.008 28.330  -11.474 1.00 16.85  ? 179 GLN   A HB3  1 
ATOM   2729 H  HG2  . GLN   A 1 179 ? -8.973  27.474  -10.692 1.00 17.08  ? 179 GLN   A HG2  1 
ATOM   2730 H  HG3  . GLN   A 1 179 ? -9.543  25.999  -10.735 1.00 17.08  ? 179 GLN   A HG3  1 
ATOM   2731 H  HE21 . GLN   A 1 179 ? -7.489  26.080  -13.517 1.00 25.18  ? 179 GLN   A HE21 1 
ATOM   2732 H  HE22 . GLN   A 1 179 ? -7.397  25.948  -11.986 1.00 25.18  ? 179 GLN   A HE22 1 
ATOM   2733 N  N    . HIS   A 1 180 ? -13.960 27.593  -9.183  1.00 13.87  ? 180 HIS   A N    1 
ATOM   2734 C  CA   . HIS   A 1 180 ? -15.278 28.258  -8.995  1.00 13.38  ? 180 HIS   A CA   1 
ATOM   2735 C  C    . HIS   A 1 180 ? -15.764 28.141  -7.545  1.00 13.03  ? 180 HIS   A C    1 
ATOM   2736 O  O    . HIS   A 1 180 ? -15.311 28.940  -6.707  1.00 17.04  ? 180 HIS   A O    1 
ATOM   2737 C  CB   . HIS   A 1 180 ? -16.275 27.736  -10.035 1.00 14.22  ? 180 HIS   A CB   1 
ATOM   2738 C  CG   . HIS   A 1 180 ? -15.984 28.238  -11.406 1.00 14.48  ? 180 HIS   A CG   1 
ATOM   2739 N  ND1  . HIS   A 1 180 ? -15.167 27.590  -12.304 1.00 15.27  ? 180 HIS   A ND1  1 
ATOM   2740 C  CD2  . HIS   A 1 180 ? -16.399 29.349  -12.020 1.00 15.66  ? 180 HIS   A CD2  1 
ATOM   2741 C  CE1  . HIS   A 1 180 ? -15.104 28.292  -13.423 1.00 15.78  ? 180 HIS   A CE1  1 
ATOM   2742 N  NE2  . HIS   A 1 180 ? -15.845 29.364  -13.272 1.00 17.43  ? 180 HIS   A NE2  1 
ATOM   2743 H  H    . HIS   A 1 180 ? -13.968 26.704  -9.034  1.00 16.65  ? 180 HIS   A H    1 
ATOM   2744 H  HA   . HIS   A 1 180 ? -15.151 29.220  -9.164  1.00 16.06  ? 180 HIS   A HA   1 
ATOM   2745 H  HB2  . HIS   A 1 180 ? -16.243 26.755  -10.039 1.00 17.07  ? 180 HIS   A HB2  1 
ATOM   2746 H  HB3  . HIS   A 1 180 ? -17.179 28.017  -9.777  1.00 17.07  ? 180 HIS   A HB3  1 
ATOM   2747 H  HD1  . HIS   A 1 180 ? -14.754 26.828  -12.161 1.00 18.33  ? 180 HIS   A HD1  1 
ATOM   2748 H  HD2  . HIS   A 1 180 ? -16.969 30.002  -11.664 1.00 18.80  ? 180 HIS   A HD2  1 
ATOM   2749 H  HE1  . HIS   A 1 180 ? -14.617 28.061  -14.194 1.00 18.93  ? 180 HIS   A HE1  1 
ATOM   2750 N  N    . SER   A 1 181 ? -16.636 27.176  -7.247  1.00 12.62  ? 181 SER   A N    1 
ATOM   2751 C  CA   . SER   A 1 181 ? -17.154 26.967  -5.871  1.00 14.29  ? 181 SER   A CA   1 
ATOM   2752 C  C    . SER   A 1 181 ? -16.010 26.622  -4.915  1.00 14.09  ? 181 SER   A C    1 
ATOM   2753 O  O    . SER   A 1 181 ? -16.101 27.013  -3.736  1.00 14.75  ? 181 SER   A O    1 
ATOM   2754 C  CB   . SER   A 1 181 ? -18.194 25.878  -5.837  1.00 13.68  ? 181 SER   A CB   1 
ATOM   2755 O  OG   . SER   A 1 181 ? -17.628 24.628  -6.204  1.00 14.11  ? 181 SER   A OG   1 
ATOM   2756 H  H    . SER   A 1 181 ? -16.983 26.631  -7.876  1.00 15.14  ? 181 SER   A H    1 
ATOM   2757 H  HA   . SER   A 1 181 ? -17.572 27.810  -5.565  1.00 17.15  ? 181 SER   A HA   1 
ATOM   2758 H  HB2  . SER   A 1 181 ? -18.564 25.814  -4.937  1.00 16.41  ? 181 SER   A HB2  1 
ATOM   2759 H  HB3  . SER   A 1 181 ? -18.918 26.100  -6.449  1.00 16.41  ? 181 SER   A HB3  1 
ATOM   2760 H  HG   . SER   A 1 181 ? -17.329 24.671  -6.993  1.00 16.93  ? 181 SER   A HG   1 
ATOM   2761 N  N    . GLY   A 1 182 ? -14.988 25.900  -5.380  1.00 12.63  ? 182 GLY   A N    1 
ATOM   2762 C  CA   . GLY   A 1 182 ? -13.941 25.451  -4.486  1.00 12.57  ? 182 GLY   A CA   1 
ATOM   2763 C  C    . GLY   A 1 182 ? -14.367 24.380  -3.516  1.00 12.41  ? 182 GLY   A C    1 
ATOM   2764 O  O    . GLY   A 1 182 ? -13.695 24.205  -2.481  1.00 14.11  ? 182 GLY   A O    1 
ATOM   2765 H  H    . GLY   A 1 182 ? -14.917 25.633  -6.194  1.00 15.15  ? 182 GLY   A H    1 
ATOM   2766 H  HA2  . GLY   A 1 182 ? -13.208 25.099  -5.015  1.00 15.09  ? 182 GLY   A HA2  1 
ATOM   2767 H  HA3  . GLY   A 1 182 ? -13.623 26.209  -3.971  1.00 15.09  ? 182 GLY   A HA3  1 
ATOM   2768 N  N    . LEU   A 1 183 ? -15.397 23.604  -3.857  1.00 13.21  ? 183 LEU   A N    1 
ATOM   2769 C  CA   . LEU   A 1 183 ? -15.834 22.507  -2.986  1.00 12.29  ? 183 LEU   A CA   1 
ATOM   2770 C  C    . LEU   A 1 183 ? -14.627 21.688  -2.519  1.00 13.31  ? 183 LEU   A C    1 
ATOM   2771 O  O    . LEU   A 1 183 ? -13.872 21.146  -3.348  1.00 13.16  ? 183 LEU   A O    1 
ATOM   2772 C  CB   . LEU   A 1 183 ? -16.776 21.599  -3.743  1.00 11.67  ? 183 LEU   A CB   1 
ATOM   2773 C  CG   . LEU   A 1 183 ? -18.193 22.111  -4.069  1.00 13.38  ? 183 LEU   A CG   1 
ATOM   2774 C  CD1  . LEU   A 1 183 ? -18.854 21.280  -5.153  1.00 12.38  ? 183 LEU   A CD1  1 
ATOM   2775 C  CD2  . LEU   A 1 183 ? -19.031 22.162  -2.822  1.00 14.76  ? 183 LEU   A CD2  1 
ATOM   2776 H  H    . LEU   A 1 183 ? -15.856 23.689  -4.580  1.00 15.85  ? 183 LEU   A H    1 
ATOM   2777 H  HA   . LEU   A 1 183 ? -16.295 22.877  -2.217  1.00 14.75  ? 183 LEU   A HA   1 
ATOM   2778 H  HB2  . LEU   A 1 183 ? -16.358 21.386  -4.592  1.00 14.01  ? 183 LEU   A HB2  1 
ATOM   2779 H  HB3  . LEU   A 1 183 ? -16.889 20.791  -3.217  1.00 14.01  ? 183 LEU   A HB3  1 
ATOM   2780 H  HG   . LEU   A 1 183 ? -18.124 23.013  -4.418  1.00 16.06  ? 183 LEU   A HG   1 
ATOM   2781 H  HD11 . LEU   A 1 183 ? -19.756 21.608  -5.297  1.00 14.86  ? 183 LEU   A HD11 1 
ATOM   2782 H  HD12 . LEU   A 1 183 ? -18.339 21.360  -5.971  1.00 14.86  ? 183 LEU   A HD12 1 
ATOM   2783 H  HD13 . LEU   A 1 183 ? -18.881 20.353  -4.869  1.00 14.86  ? 183 LEU   A HD13 1 
ATOM   2784 H  HD21 . LEU   A 1 183 ? -19.910 22.506  -3.046  1.00 17.71  ? 183 LEU   A HD21 1 
ATOM   2785 H  HD22 . LEU   A 1 183 ? -19.109 21.266  -2.458  1.00 17.71  ? 183 LEU   A HD22 1 
ATOM   2786 H  HD23 . LEU   A 1 183 ? -18.602 22.745  -2.177  1.00 17.71  ? 183 LEU   A HD23 1 
ATOM   2787 N  N    . GLU   A 1 184 ? -14.475 21.560  -1.218  1.00 14.34  ? 184 GLU   A N    1 
ATOM   2788 C  CA   . GLU   A 1 184 ? -13.303 20.907  -0.657  1.00 14.77  ? 184 GLU   A CA   1 
ATOM   2789 C  C    . GLU   A 1 184 ? -13.456 19.396  -0.727  1.00 15.50  ? 184 GLU   A C    1 
ATOM   2790 O  O    . GLU   A 1 184 ? -14.563 18.861  -0.606  1.00 14.72  ? 184 GLU   A O    1 
ATOM   2791 C  CB   . GLU   A 1 184 ? -13.069 21.375  0.771   1.00 17.16  ? 184 GLU   A CB   1 
ATOM   2792 C  CG   . GLU   A 1 184 ? -12.863 22.892  0.924   1.00 20.93  ? 184 GLU   A CG   1 
ATOM   2793 C  CD   . GLU   A 1 184 ? -11.586 23.457  0.353   1.00 42.22  ? 184 GLU   A CD   1 
ATOM   2794 O  OE1  . GLU   A 1 184 ? -10.836 22.770  -0.402  1.00 45.89  ? 184 GLU   A OE1  1 
ATOM   2795 O  OE2  . GLU   A 1 184 ? -11.316 24.629  0.738   1.00 46.07  ? 184 GLU   A OE2  1 
ATOM   2796 H  H    . GLU   A 1 184 ? -15.036 21.843  -0.631  1.00 17.21  ? 184 GLU   A H    1 
ATOM   2797 H  HA   . GLU   A 1 184 ? -12.512 21.141  -1.168  1.00 17.73  ? 184 GLU   A HA   1 
ATOM   2798 H  HB2  . GLU   A 1 184 ? -13.840 21.129  1.306   1.00 20.59  ? 184 GLU   A HB2  1 
ATOM   2799 H  HB3  . GLU   A 1 184 ? -12.275 20.936  1.114   1.00 20.59  ? 184 GLU   A HB3  1 
ATOM   2800 H  HG2  . GLU   A 1 184 ? -13.597 23.342  0.478   1.00 25.12  ? 184 GLU   A HG2  1 
ATOM   2801 H  HG3  . GLU   A 1 184 ? -12.870 23.104  1.870   1.00 25.12  ? 184 GLU   A HG3  1 
ATOM   2802 N  N    . TYR   A 1 185 ? -12.333 18.686  -0.910  1.00 14.45  ? 185 TYR   A N    1 
ATOM   2803 C  CA   . TYR   A 1 185 ? -12.338 17.263  -1.301  1.00 12.92  ? 185 TYR   A CA   1 
ATOM   2804 C  C    . TYR   A 1 185 ? -12.461 16.289  -0.125  1.00 13.92  ? 185 TYR   A C    1 
ATOM   2805 O  O    . TYR   A 1 185 ? -11.697 15.311  0.006   1.00 15.07  ? 185 TYR   A O    1 
ATOM   2806 C  CB   . TYR   A 1 185 ? -11.124 16.973  -2.157  1.00 13.40  ? 185 TYR   A CB   1 
ATOM   2807 C  CG   . TYR   A 1 185 ? -11.288 15.814  -3.074  1.00 12.75  ? 185 TYR   A CG   1 
ATOM   2808 C  CD1  . TYR   A 1 185 ? -12.101 15.927  -4.153  1.00 13.69  ? 185 TYR   A CD1  1 
ATOM   2809 C  CD2  . TYR   A 1 185 ? -10.627 14.612  -2.856  1.00 13.84  ? 185 TYR   A CD2  1 
ATOM   2810 C  CE1  . TYR   A 1 185 ? -12.244 14.885  -5.084  1.00 13.53  ? 185 TYR   A CE1  1 
ATOM   2811 C  CE2  . TYR   A 1 185 ? -10.774 13.567  -3.748  1.00 14.03  ? 185 TYR   A CE2  1 
ATOM   2812 C  CZ   . TYR   A 1 185 ? -11.567 13.702  -4.838  1.00 14.19  ? 185 TYR   A CZ   1 
ATOM   2813 O  OH   . TYR   A 1 185 ? -11.696 12.627  -5.703  1.00 14.75  ? 185 TYR   A OH   1 
ATOM   2814 H  H    . TYR   A 1 185 ? -11.542 19.008  -0.813  1.00 17.35  ? 185 TYR   A H    1 
ATOM   2815 H  HA   . TYR   A 1 185 ? -13.138 17.099  -1.823  1.00 15.51  ? 185 TYR   A HA   1 
ATOM   2816 H  HB2  . TYR   A 1 185 ? -10.935 17.754  -2.700  1.00 16.08  ? 185 TYR   A HB2  1 
ATOM   2817 H  HB3  . TYR   A 1 185 ? -10.372 16.784  -1.574  1.00 16.08  ? 185 TYR   A HB3  1 
ATOM   2818 H  HD1  . TYR   A 1 185 ? -12.578 16.715  -4.280  1.00 16.43  ? 185 TYR   A HD1  1 
ATOM   2819 H  HD2  . TYR   A 1 185 ? -10.084 14.510  -2.108  1.00 16.60  ? 185 TYR   A HD2  1 
ATOM   2820 H  HE1  . TYR   A 1 185 ? -12.775 14.986  -5.841  1.00 16.24  ? 185 TYR   A HE1  1 
ATOM   2821 H  HE2  . TYR   A 1 185 ? -10.326 12.766  -3.599  1.00 16.84  ? 185 TYR   A HE2  1 
ATOM   2822 H  HH   . TYR   A 1 185 ? -12.163 12.846  -6.366  1.00 17.70  ? 185 TYR   A HH   1 
ATOM   2823 N  N    . PHE   A 1 186 ? -13.409 16.543  0.777   1.00 13.28  ? 186 PHE   A N    1 
ATOM   2824 C  CA   . PHE   A 1 186 ? -13.707 15.666  1.899   1.00 13.63  ? 186 PHE   A CA   1 
ATOM   2825 C  C    . PHE   A 1 186 ? -15.136 15.980  2.332   1.00 13.78  ? 186 PHE   A C    1 
ATOM   2826 O  O    . PHE   A 1 186 ? -15.707 17.013  1.992   1.00 13.87  ? 186 PHE   A O    1 
ATOM   2827 C  CB   . PHE   A 1 186 ? -12.701 15.846  3.055   1.00 14.64  ? 186 PHE   A CB   1 
ATOM   2828 C  CG   . PHE   A 1 186 ? -12.795 17.178  3.724   1.00 15.63  ? 186 PHE   A CG   1 
ATOM   2829 C  CD1  . PHE   A 1 186 ? -12.141 18.281  3.234   1.00 16.96  ? 186 PHE   A CD1  1 
ATOM   2830 C  CD2  . PHE   A 1 186 ? -13.558 17.340  4.847   1.00 18.56  ? 186 PHE   A CD2  1 
ATOM   2831 C  CE1  . PHE   A 1 186 ? -12.253 19.522  3.906   1.00 18.33  ? 186 PHE   A CE1  1 
ATOM   2832 C  CE2  . PHE   A 1 186 ? -13.667 18.575  5.533   1.00 19.65  ? 186 PHE   A CE2  1 
ATOM   2833 C  CZ   . PHE   A 1 186 ? -13.027 19.676  4.982   1.00 18.25  ? 186 PHE   A CZ   1 
ATOM   2834 H  H    . PHE   A 1 186 ? -13.910 17.242  0.758   1.00 15.94  ? 186 PHE   A H    1 
ATOM   2835 H  HA   . PHE   A 1 186 ? -13.654 14.737  1.626   1.00 16.35  ? 186 PHE   A HA   1 
ATOM   2836 H  HB2  . PHE   A 1 186 ? -12.868 15.164  3.724   1.00 17.57  ? 186 PHE   A HB2  1 
ATOM   2837 H  HB3  . PHE   A 1 186 ? -11.801 15.752  2.704   1.00 17.57  ? 186 PHE   A HB3  1 
ATOM   2838 H  HD1  . PHE   A 1 186 ? -11.626 18.214  2.462   1.00 20.35  ? 186 PHE   A HD1  1 
ATOM   2839 H  HD2  . PHE   A 1 186 ? -14.026 16.606  5.176   1.00 22.27  ? 186 PHE   A HD2  1 
ATOM   2840 H  HE1  . PHE   A 1 186 ? -11.773 20.252  3.587   1.00 22.00  ? 186 PHE   A HE1  1 
ATOM   2841 H  HE2  . PHE   A 1 186 ? -14.151 18.645  6.324   1.00 23.58  ? 186 PHE   A HE2  1 
ATOM   2842 H  HZ   . PHE   A 1 186 ? -13.136 20.518  5.362   1.00 21.90  ? 186 PHE   A HZ   1 
ATOM   2843 N  N    . GLY   A 1 187 ? -15.691 15.073  3.135   1.00 15.12  ? 187 GLY   A N    1 
ATOM   2844 C  CA   . GLY   A 1 187 ? -17.043 15.305  3.660   1.00 14.72  ? 187 GLY   A CA   1 
ATOM   2845 C  C    . GLY   A 1 187 ? -18.114 15.425  2.588   1.00 13.79  ? 187 GLY   A C    1 
ATOM   2846 O  O    . GLY   A 1 187 ? -18.001 14.938  1.468   1.00 13.19  ? 187 GLY   A O    1 
ATOM   2847 H  H    . GLY   A 1 187 ? -15.322 14.338  3.385   1.00 18.14  ? 187 GLY   A H    1 
ATOM   2848 H  HA2  . GLY   A 1 187 ? -17.285 14.568  4.242   1.00 17.66  ? 187 GLY   A HA2  1 
ATOM   2849 H  HA3  . GLY   A 1 187 ? -17.043 16.127  4.174   1.00 17.66  ? 187 GLY   A HA3  1 
ATOM   2850 N  N    . GLN   A 1 188 ? -19.166 16.138  2.928   1.00 13.85  ? 188 GLN   A N    1 
ATOM   2851 C  CA   . GLN   A 1 188 ? -20.273 16.325  1.995   1.00 13.34  ? 188 GLN   A CA   1 
ATOM   2852 C  C    . GLN   A 1 188 ? -19.872 17.145  0.775   1.00 12.90  ? 188 GLN   A C    1 
ATOM   2853 O  O    . GLN   A 1 188 ? -20.222 16.823  -0.354  1.00 12.59  ? 188 GLN   A O    1 
ATOM   2854 C  CB   . GLN   A 1 188 ? -21.451 16.950  2.718   1.00 13.57  ? 188 GLN   A CB   1 
ATOM   2855 C  CG   . GLN   A 1 188 ? -22.102 15.997  3.745   1.00 13.77  ? 188 GLN   A CG   1 
ATOM   2856 C  CD   . GLN   A 1 188 ? -23.190 16.642  4.476   1.00 16.13  ? 188 GLN   A CD   1 
ATOM   2857 O  OE1  . GLN   A 1 188 ? -24.017 17.309  3.953   1.00 14.28  ? 188 GLN   A OE1  1 
ATOM   2858 N  NE2  . GLN   A 1 188 ? -23.181 16.482  5.796   1.00 26.60  ? 188 GLN   A NE2  1 
ATOM   2859 H  H    . GLN   A 1 188 ? -19.271 16.527  3.688   1.00 16.62  ? 188 GLN   A H    1 
ATOM   2860 H  HA   . GLN   A 1 188 ? -20.548 15.456  1.665   1.00 16.00  ? 188 GLN   A HA   1 
ATOM   2861 H  HB2  . GLN   A 1 188 ? -21.147 17.739  3.193   1.00 16.28  ? 188 GLN   A HB2  1 
ATOM   2862 H  HB3  . GLN   A 1 188 ? -22.127 17.194  2.066   1.00 16.28  ? 188 GLN   A HB3  1 
ATOM   2863 H  HG2  . GLN   A 1 188 ? -22.463 15.226  3.281   1.00 16.53  ? 188 GLN   A HG2  1 
ATOM   2864 H  HG3  . GLN   A 1 188 ? -21.431 15.714  4.386   1.00 16.53  ? 188 GLN   A HG3  1 
ATOM   2865 H  HE21 . GLN   A 1 188 ? -22.558 16.021  6.169   1.00 31.92  ? 188 GLN   A HE21 1 
ATOM   2866 H  HE22 . GLN   A 1 188 ? -23.798 16.840  6.277   1.00 31.92  ? 188 GLN   A HE22 1 
ATOM   2867 N  N    . SER   A 1 189 ? -19.044 18.173  0.987   1.00 13.25  ? 189 SER   A N    1 
ATOM   2868 C  CA   . SER   A 1 189 ? -18.612 18.969  -0.158  1.00 12.37  ? 189 SER   A CA   1 
ATOM   2869 C  C    . SER   A 1 189 ? -17.803 18.153  -1.130  1.00 10.85  ? 189 SER   A C    1 
ATOM   2870 O  O    . SER   A 1 189 ? -17.859 18.384  -2.340  1.00 11.71  ? 189 SER   A O    1 
ATOM   2871 C  CB   . SER   A 1 189 ? -17.834 20.198  0.308   1.00 12.64  ? 189 SER   A CB   1 
ATOM   2872 O  OG   . SER   A 1 189 ? -16.656 19.864  1.005   1.00 15.00  ? 189 SER   A OG   1 
ATOM   2873 H  H    . SER   A 1 189 ? -18.733 18.417  1.751   1.00 15.90  ? 189 SER   A H    1 
ATOM   2874 H  HA   . SER   A 1 189 ? -19.399 19.288  -0.627  1.00 14.85  ? 189 SER   A HA   1 
ATOM   2875 H  HB2  . SER   A 1 189 ? -17.593 20.724  -0.471  1.00 15.17  ? 189 SER   A HB2  1 
ATOM   2876 H  HB3  . SER   A 1 189 ? -18.404 20.719  0.896   1.00 15.17  ? 189 SER   A HB3  1 
ATOM   2877 H  HG   . SER   A 1 189 ? -16.144 19.422  0.507   1.00 18.00  ? 189 SER   A HG   1 
ATOM   2878 N  N    . GLY   A 1 190 ? -17.019 17.227  -0.599  1.00 11.68  ? 190 GLY   A N    1 
ATOM   2879 C  CA   . GLY   A 1 190 ? -16.208 16.380  -1.453  1.00 12.81  ? 190 GLY   A CA   1 
ATOM   2880 C  C    . GLY   A 1 190 ? -17.048 15.427  -2.278  1.00 11.77  ? 190 GLY   A C    1 
ATOM   2881 O  O    . GLY   A 1 190 ? -16.741 15.145  -3.438  1.00 12.03  ? 190 GLY   A O    1 
ATOM   2882 H  H    . GLY   A 1 190 ? -16.939 17.071  0.243   1.00 14.02  ? 190 GLY   A H    1 
ATOM   2883 H  HA2  . GLY   A 1 190 ? -15.690 16.934  -2.058  1.00 15.37  ? 190 GLY   A HA2  1 
ATOM   2884 H  HA3  . GLY   A 1 190 ? -15.601 15.858  -0.905  1.00 15.37  ? 190 GLY   A HA3  1 
ATOM   2885 N  N    . GLY   A 1 191 ? -18.132 14.906  -1.668  1.00 12.66  ? 191 GLY   A N    1 
ATOM   2886 C  CA   . GLY   A 1 191 ? -19.065 14.129  -2.452  1.00 10.66  ? 191 GLY   A CA   1 
ATOM   2887 C  C    . GLY   A 1 191 ? -19.707 14.956  -3.557  1.00 10.88  ? 191 GLY   A C    1 
ATOM   2888 O  O    . GLY   A 1 191 ? -19.892 14.478  -4.675  1.00 11.54  ? 191 GLY   A O    1 
ATOM   2889 H  H    . GLY   A 1 191 ? -18.329 14.994  -0.835  1.00 15.19  ? 191 GLY   A H    1 
ATOM   2890 H  HA2  . GLY   A 1 191 ? -18.600 13.381  -2.858  1.00 12.79  ? 191 GLY   A HA2  1 
ATOM   2891 H  HA3  . GLY   A 1 191 ? -19.767 13.789  -1.875  1.00 12.79  ? 191 GLY   A HA3  1 
ATOM   2892 N  N    . MET   A 1 192 ? -20.069 16.208  -3.269  1.00 10.71  ? 192 MET   A N    1 
ATOM   2893 C  CA   . MET   A 1 192 ? -20.588 17.087  -4.324  1.00 10.07  ? 192 MET   A CA   1 
ATOM   2894 C  C    . MET   A 1 192 ? -19.556 17.375  -5.417  1.00 10.36  ? 192 MET   A C    1 
ATOM   2895 O  O    . MET   A 1 192 ? -19.898 17.463  -6.592  1.00 10.74  ? 192 MET   A O    1 
ATOM   2896 C  CB   . MET   A 1 192 ? -21.019 18.413  -3.724  1.00 11.17  ? 192 MET   A CB   1 
ATOM   2897 C  CG   . MET   A 1 192 ? -22.251 18.325  -2.828  1.00 10.48  ? 192 MET   A CG   1 
ATOM   2898 S  SD   . MET   A 1 192 ? -22.656 19.853  -1.947  1.00 13.69  ? 192 MET   A SD   1 
ATOM   2899 C  CE   . MET   A 1 192 ? -22.959 20.993  -3.276  1.00 14.52  ? 192 MET   A CE   1 
ATOM   2900 H  H    . MET   A 1 192 ? -20.026 16.568  -2.489  1.00 12.85  ? 192 MET   A H    1 
ATOM   2901 H  HA   . MET   A 1 192 ? -21.350 16.631  -4.715  1.00 12.08  ? 192 MET   A HA   1 
ATOM   2902 H  HB2  . MET   A 1 192 ? -20.290 18.763  -3.188  1.00 13.40  ? 192 MET   A HB2  1 
ATOM   2903 H  HB3  . MET   A 1 192 ? -21.224 19.027  -4.446  1.00 13.40  ? 192 MET   A HB3  1 
ATOM   2904 H  HG2  . MET   A 1 192 ? -23.016 18.093  -3.377  1.00 12.58  ? 192 MET   A HG2  1 
ATOM   2905 H  HG3  . MET   A 1 192 ? -22.099 17.636  -2.162  1.00 12.58  ? 192 MET   A HG3  1 
ATOM   2906 H  HE1  . MET   A 1 192 ? -23.211 21.852  -2.903  1.00 17.42  ? 192 MET   A HE1  1 
ATOM   2907 H  HE2  . MET   A 1 192 ? -22.151 21.085  -3.803  1.00 17.42  ? 192 MET   A HE2  1 
ATOM   2908 H  HE3  . MET   A 1 192 ? -23.678 20.649  -3.829  1.00 17.42  ? 192 MET   A HE3  1 
ATOM   2909 N  N    . ASN   A 1 193 ? -18.285 17.521  -5.002  1.00 10.52  ? 193 ASN   A N    1 
ATOM   2910 C  CA   . ASN   A 1 193 ? -17.194 17.769  -5.961  1.00 10.78  ? 193 ASN   A CA   1 
ATOM   2911 C  C    . ASN   A 1 193 ? -17.089 16.594  -6.940  1.00 10.48  ? 193 ASN   A C    1 
ATOM   2912 O  O    . ASN   A 1 193 ? -17.164 16.753  -8.156  1.00 10.24  ? 193 ASN   A O    1 
ATOM   2913 C  CB   . ASN   A 1 193 ? -15.912 17.979  -5.143  1.00 12.27  ? 193 ASN   A CB   1 
ATOM   2914 C  CG   . ASN   A 1 193 ? -14.695 18.289  -5.973  1.00 11.36  ? 193 ASN   A CG   1 
ATOM   2915 O  OD1  . ASN   A 1 193 ? -14.527 17.662  -7.017  1.00 12.97  ? 193 ASN   A OD1  1 
ATOM   2916 N  ND2  . ASN   A 1 193 ? -13.884 19.205  -5.548  1.00 12.37  ? 193 ASN   A ND2  1 
ATOM   2917 H  H    . ASN   A 1 193 ? -18.031 17.480  -4.181  1.00 12.62  ? 193 ASN   A H    1 
ATOM   2918 H  HA   . ASN   A 1 193 ? -17.346 18.563  -6.497  1.00 12.93  ? 193 ASN   A HA   1 
ATOM   2919 H  HB2  . ASN   A 1 193 ? -16.050 18.721  -4.534  1.00 14.72  ? 193 ASN   A HB2  1 
ATOM   2920 H  HB3  . ASN   A 1 193 ? -15.727 17.169  -4.642  1.00 14.72  ? 193 ASN   A HB3  1 
ATOM   2921 H  HD21 . ASN   A 1 193 ? -13.181 19.402  -6.004  1.00 14.85  ? 193 ASN   A HD21 1 
ATOM   2922 H  HD22 . ASN   A 1 193 ? -14.048 19.617  -4.812  1.00 14.85  ? 193 ASN   A HD22 1 
ATOM   2923 N  N    . GLU   A 1 194 ? -17.009 15.387  -6.372  1.00 9.87   ? 194 GLU   A N    1 
ATOM   2924 C  CA   . GLU   A 1 194 ? -16.982 14.206  -7.216  1.00 10.21  ? 194 GLU   A CA   1 
ATOM   2925 C  C    . GLU   A 1 194 ? -18.202 14.101  -8.097  1.00 10.37  ? 194 GLU   A C    1 
ATOM   2926 O  O    . GLU   A 1 194 ? -18.111 13.794  -9.298  1.00 10.82  ? 194 GLU   A O    1 
ATOM   2927 C  CB   . GLU   A 1 194 ? -16.843 13.002  -6.281  1.00 11.13  ? 194 GLU   A CB   1 
ATOM   2928 C  CG   . GLU   A 1 194 ? -15.431 12.523  -6.099  1.00 12.22  ? 194 GLU   A CG   1 
ATOM   2929 C  CD   . GLU   A 1 194 ? -14.818 12.137  -7.405  1.00 12.83  ? 194 GLU   A CD   1 
ATOM   2930 O  OE1  . GLU   A 1 194 ? -15.400 11.423  -8.222  1.00 14.28  ? 194 GLU   A OE1  1 
ATOM   2931 O  OE2  . GLU   A 1 194 ? -13.624 12.507  -7.588  1.00 13.36  ? 194 GLU   A OE2  1 
ATOM   2932 H  H    . GLU   A 1 194 ? -16.971 15.236  -5.526  1.00 11.84  ? 194 GLU   A H    1 
ATOM   2933 H  HA   . GLU   A 1 194 ? -16.231 14.237  -7.829  1.00 12.25  ? 194 GLU   A HA   1 
ATOM   2934 H  HB2  . GLU   A 1 194 ? -17.186 13.246  -5.408  1.00 13.36  ? 194 GLU   A HB2  1 
ATOM   2935 H  HB3  . GLU   A 1 194 ? -17.359 12.265  -6.646  1.00 13.36  ? 194 GLU   A HB3  1 
ATOM   2936 H  HG2  . GLU   A 1 194 ? -14.898 13.233  -5.708  1.00 14.67  ? 194 GLU   A HG2  1 
ATOM   2937 H  HG3  . GLU   A 1 194 ? -15.427 11.746  -5.517  1.00 14.67  ? 194 GLU   A HG3  1 
ATOM   2938 N  N    . SER   A 1 195 ? -19.381 14.379  -7.532  1.00 9.78   ? 195 SER   A N    1 
ATOM   2939 C  CA   A SER   A 1 195 ? -20.599 14.297  -8.321  0.52 10.86  ? 195 SER   A CA   1 
ATOM   2940 C  CA   B SER   A 1 195 ? -20.581 14.289  -8.332  0.48 10.92  ? 195 SER   A CA   1 
ATOM   2941 C  C    . SER   A 1 195 ? -20.574 15.251  -9.493  1.00 9.51   ? 195 SER   A C    1 
ATOM   2942 O  O    . SER   A 1 195 ? -20.975 14.897  -10.581 1.00 10.34  ? 195 SER   A O    1 
ATOM   2943 C  CB   A SER   A 1 195 ? -21.833 14.625  -7.477  0.52 11.15  ? 195 SER   A CB   1 
ATOM   2944 C  CB   B SER   A 1 195 ? -21.803 14.511  -7.463  0.48 11.14  ? 195 SER   A CB   1 
ATOM   2945 O  OG   A SER   A 1 195 ? -22.063 13.705  -6.441  0.52 9.45   ? 195 SER   A OG   1 
ATOM   2946 O  OG   B SER   A 1 195 ? -22.911 14.469  -8.286  0.48 11.92  ? 195 SER   A OG   1 
ATOM   2947 H  H    A SER   A 1 195 ? -19.494 14.612  -6.712  0.52 11.74  ? 195 SER   A H    1 
ATOM   2948 H  H    B SER   A 1 195 ? -19.499 14.613  -6.713  0.48 11.74  ? 195 SER   A H    1 
ATOM   2949 H  HA   A SER   A 1 195 ? -20.660 13.382  -8.638  0.52 13.03  ? 195 SER   A HA   1 
ATOM   2950 H  HA   B SER   A 1 195 ? -20.622 13.394  -8.703  0.48 13.10  ? 195 SER   A HA   1 
ATOM   2951 H  HB2  A SER   A 1 195 ? -21.709 15.503  -7.084  0.52 13.38  ? 195 SER   A HB2  1 
ATOM   2952 H  HB2  B SER   A 1 195 ? -21.863 13.810  -6.795  0.48 13.37  ? 195 SER   A HB2  1 
ATOM   2953 H  HB3  A SER   A 1 195 ? -22.609 14.629  -8.059  0.52 13.38  ? 195 SER   A HB3  1 
ATOM   2954 H  HB3  B SER   A 1 195 ? -21.747 15.377  -7.031  0.48 13.37  ? 195 SER   A HB3  1 
ATOM   2955 H  HG   A SER   A 1 195 ? -22.168 12.935  -6.759  0.52 11.34  ? 195 SER   A HG   1 
ATOM   2956 H  HG   B SER   A 1 195 ? -23.019 13.691  -8.583  0.48 14.31  ? 195 SER   A HG   1 
ATOM   2957 N  N    . PHE   A 1 196 ? -20.183 16.504  -9.260  1.00 9.69   ? 196 PHE   A N    1 
ATOM   2958 C  CA   . PHE   A 1 196 ? -20.174 17.458  -10.362 1.00 10.30  ? 196 PHE   A CA   1 
ATOM   2959 C  C    . PHE   A 1 196 ? -19.326 16.932  -11.514 1.00 9.18   ? 196 PHE   A C    1 
ATOM   2960 O  O    . PHE   A 1 196 ? -19.665 17.091  -12.681 1.00 10.26  ? 196 PHE   A O    1 
ATOM   2961 C  CB   . PHE   A 1 196 ? -19.684 18.836  -9.891  1.00 10.24  ? 196 PHE   A CB   1 
ATOM   2962 C  CG   . PHE   A 1 196 ? -19.683 19.840  -10.994 1.00 10.22  ? 196 PHE   A CG   1 
ATOM   2963 C  CD1  . PHE   A 1 196 ? -20.871 20.500  -11.344 1.00 11.53  ? 196 PHE   A CD1  1 
ATOM   2964 C  CD2  . PHE   A 1 196 ? -18.593 20.077  -11.819 1.00 11.18  ? 196 PHE   A CD2  1 
ATOM   2965 C  CE1  . PHE   A 1 196 ? -20.955 21.381  -12.439 1.00 12.68  ? 196 PHE   A CE1  1 
ATOM   2966 C  CE2  . PHE   A 1 196 ? -18.644 20.936  -12.894 1.00 11.62  ? 196 PHE   A CE2  1 
ATOM   2967 C  CZ   . PHE   A 1 196 ? -19.837 21.579  -13.219 1.00 11.31  ? 196 PHE   A CZ   1 
ATOM   2968 H  H    . PHE   A 1 196 ? -19.927 16.814  -8.500  1.00 11.62  ? 196 PHE   A H    1 
ATOM   2969 H  HA   . PHE   A 1 196 ? -21.082 17.582  -10.681 1.00 12.36  ? 196 PHE   A HA   1 
ATOM   2970 H  HB2  . PHE   A 1 196 ? -20.269 19.159  -9.188  1.00 12.29  ? 196 PHE   A HB2  1 
ATOM   2971 H  HB3  . PHE   A 1 196 ? -18.777 18.754  -9.556  1.00 12.29  ? 196 PHE   A HB3  1 
ATOM   2972 H  HD1  . PHE   A 1 196 ? -21.633 20.349  -10.833 1.00 13.84  ? 196 PHE   A HD1  1 
ATOM   2973 H  HD2  . PHE   A 1 196 ? -17.794 19.636  -11.639 1.00 13.41  ? 196 PHE   A HD2  1 
ATOM   2974 H  HE1  . PHE   A 1 196 ? -21.751 21.821  -12.632 1.00 15.22  ? 196 PHE   A HE1  1 
ATOM   2975 H  HE2  . PHE   A 1 196 ? -17.881 21.087  -13.403 1.00 13.95  ? 196 PHE   A HE2  1 
ATOM   2976 H  HZ   . PHE   A 1 196 ? -19.878 22.140  -13.960 1.00 13.57  ? 196 PHE   A HZ   1 
ATOM   2977 N  N    . SER   A 1 197 ? -18.180 16.345  -11.160 1.00 10.37  ? 197 SER   A N    1 
ATOM   2978 C  CA   . SER   A 1 197 ? -17.352 15.768  -12.218 1.00 10.82  ? 197 SER   A CA   1 
ATOM   2979 C  C    . SER   A 1 197 ? -18.039 14.601  -12.949 1.00 9.67   ? 197 SER   A C    1 
ATOM   2980 O  O    . SER   A 1 197 ? -17.822 14.449  -14.174 1.00 10.47  ? 197 SER   A O    1 
ATOM   2981 C  CB   . SER   A 1 197 ? -16.011 15.358  -11.621 1.00 10.39  ? 197 SER   A CB   1 
ATOM   2982 O  OG   . SER   A 1 197 ? -15.127 16.485  -11.467 1.00 11.37  ? 197 SER   A OG   1 
ATOM   2983 H  H    . SER   A 1 197 ? -17.877 16.271  -10.359 1.00 12.44  ? 197 SER   A H    1 
ATOM   2984 H  HA   . SER   A 1 197 ? -17.195 16.439  -12.900 1.00 12.99  ? 197 SER   A HA   1 
ATOM   2985 H  HB2  . SER   A 1 197 ? -16.165 14.962  -10.749 1.00 12.47  ? 197 SER   A HB2  1 
ATOM   2986 H  HB3  . SER   A 1 197 ? -15.591 14.711  -12.210 1.00 12.47  ? 197 SER   A HB3  1 
ATOM   2987 H  HG   . SER   A 1 197 ? -15.059 16.898  -12.196 1.00 13.65  ? 197 SER   A HG   1 
ATOM   2988 N  N    . ASP   A 1 198 ? -18.809 13.767  -12.237 1.00 9.88   ? 198 ASP   A N    1 
ATOM   2989 C  CA   . ASP   A 1 198 ? -19.588 12.728  -12.933 1.00 10.33  ? 198 ASP   A CA   1 
ATOM   2990 C  C    . ASP   A 1 198 ? -20.685 13.330  -13.801 1.00 11.89  ? 198 ASP   A C    1 
ATOM   2991 O  O    . ASP   A 1 198 ? -20.985 12.810  -14.875 1.00 11.28  ? 198 ASP   A O    1 
ATOM   2992 C  CB   . ASP   A 1 198 ? -20.153 11.758  -11.900 1.00 11.90  ? 198 ASP   A CB   1 
ATOM   2993 C  CG   . ASP   A 1 198 ? -19.128 10.843  -11.313 1.00 11.23  ? 198 ASP   A CG   1 
ATOM   2994 O  OD1  . ASP   A 1 198 ? -17.980 10.697  -11.850 1.00 12.98  ? 198 ASP   A OD1  1 
ATOM   2995 O  OD2  . ASP   A 1 198 ? -19.440 10.176  -10.266 1.00 12.96  ? 198 ASP   A OD2  1 
ATOM   2996 H  H    . ASP   A 1 198 ? -18.897 13.780  -11.382 1.00 11.86  ? 198 ASP   A H    1 
ATOM   2997 H  HA   . ASP   A 1 198 ? -19.008 12.230  -13.530 1.00 12.39  ? 198 ASP   A HA   1 
ATOM   2998 H  HB2  . ASP   A 1 198 ? -20.545 12.268  -11.175 1.00 14.28  ? 198 ASP   A HB2  1 
ATOM   2999 H  HB3  . ASP   A 1 198 ? -20.830 11.209  -12.325 1.00 14.28  ? 198 ASP   A HB3  1 
ATOM   3000 N  N    . MET   A 1 199 ? -21.296 14.420  -13.339 1.00 10.37  ? 199 MET   A N    1 
ATOM   3001 C  CA   . MET   A 1 199 ? -22.281 15.108  -14.159 1.00 11.08  ? 199 MET   A CA   1 
ATOM   3002 C  C    . MET   A 1 199 ? -21.653 15.617  -15.432 1.00 10.58  ? 199 MET   A C    1 
ATOM   3003 O  O    . MET   A 1 199 ? -22.239 15.500  -16.514 1.00 11.66  ? 199 MET   A O    1 
ATOM   3004 C  CB   . MET   A 1 199 ? -22.989 16.271  -13.436 1.00 11.66  ? 199 MET   A CB   1 
ATOM   3005 C  CG   . MET   A 1 199 ? -23.666 15.937  -12.139 1.00 11.33  ? 199 MET   A CG   1 
ATOM   3006 S  SD   . MET   A 1 199 ? -24.072 17.470  -11.270 1.00 13.20  ? 199 MET   A SD   1 
ATOM   3007 C  CE   . MET   A 1 199 ? -24.158 16.961  -9.563  1.00 15.36  ? 199 MET   A CE   1 
ATOM   3008 H  H    . MET   A 1 199 ? -21.159 14.773  -12.567 1.00 12.45  ? 199 MET   A H    1 
ATOM   3009 H  HA   . MET   A 1 199 ? -22.974 14.455  -14.345 1.00 13.30  ? 199 MET   A HA   1 
ATOM   3010 H  HB2  . MET   A 1 199 ? -22.327 16.954  -13.245 1.00 14.00  ? 199 MET   A HB2  1 
ATOM   3011 H  HB3  . MET   A 1 199 ? -23.669 16.626  -14.030 1.00 14.00  ? 199 MET   A HB3  1 
ATOM   3012 H  HG2  . MET   A 1 199 ? -24.485 15.445  -12.311 1.00 13.60  ? 199 MET   A HG2  1 
ATOM   3013 H  HG3  . MET   A 1 199 ? -23.072 15.408  -11.583 1.00 13.60  ? 199 MET   A HG3  1 
ATOM   3014 H  HE1  . MET   A 1 199 ? -24.337 17.738  -9.010  1.00 18.43  ? 199 MET   A HE1  1 
ATOM   3015 H  HE2  . MET   A 1 199 ? -24.871 16.312  -9.462  1.00 18.43  ? 199 MET   A HE2  1 
ATOM   3016 H  HE3  . MET   A 1 199 ? -23.310 16.563  -9.309  1.00 18.43  ? 199 MET   A HE3  1 
ATOM   3017 N  N    . ALA   A 1 200 ? -20.441 16.177  -15.309 1.00 10.69  ? 200 ALA   A N    1 
ATOM   3018 C  CA   . ALA   A 1 200 ? -19.756 16.726  -16.465 1.00 10.72  ? 200 ALA   A CA   1 
ATOM   3019 C  C    . ALA   A 1 200 ? -19.369 15.638  -17.432 1.00 10.58  ? 200 ALA   A C    1 
ATOM   3020 O  O    . ALA   A 1 200 ? -19.322 15.880  -18.642 1.00 12.42  ? 200 ALA   A O    1 
ATOM   3021 C  CB   . ALA   A 1 200 ? -18.521 17.482  -16.022 1.00 12.47  ? 200 ALA   A CB   1 
ATOM   3022 H  H    . ALA   A 1 200 ? -20.005 16.248  -14.570 1.00 12.83  ? 200 ALA   A H    1 
ATOM   3023 H  HA   . ALA   A 1 200 ? -20.348 17.347  -16.918 1.00 12.86  ? 200 ALA   A HA   1 
ATOM   3024 H  HB1  . ALA   A 1 200 ? -18.067 17.832  -16.805 1.00 14.96  ? 200 ALA   A HB1  1 
ATOM   3025 H  HB2  . ALA   A 1 200 ? -18.789 18.212  -15.441 1.00 14.96  ? 200 ALA   A HB2  1 
ATOM   3026 H  HB3  . ALA   A 1 200 ? -17.935 16.876  -15.543 1.00 14.96  ? 200 ALA   A HB3  1 
ATOM   3027 N  N    . ALA   A 1 201 ? -19.060 14.450  -16.954 1.00 11.91  ? 201 ALA   A N    1 
ATOM   3028 C  CA   . ALA   A 1 201 ? -18.812 13.309  -17.852 1.00 12.68  ? 201 ALA   A CA   1 
ATOM   3029 C  C    . ALA   A 1 201 ? -20.025 13.064  -18.737 1.00 12.50  ? 201 ALA   A C    1 
ATOM   3030 O  O    . ALA   A 1 201 ? -19.922 12.803  -19.937 1.00 13.60  ? 201 ALA   A O    1 
ATOM   3031 C  CB   . ALA   A 1 201 ? -18.467 12.060  -17.039 1.00 12.86  ? 201 ALA   A CB   1 
ATOM   3032 H  H    . ALA   A 1 201 ? -18.984 14.264  -16.118 1.00 14.29  ? 201 ALA   A H    1 
ATOM   3033 H  HA   . ALA   A 1 201 ? -18.050 13.506  -18.419 1.00 15.21  ? 201 ALA   A HA   1 
ATOM   3034 H  HB1  . ALA   A 1 201 ? -18.285 11.327  -17.648 1.00 15.43  ? 201 ALA   A HB1  1 
ATOM   3035 H  HB2  . ALA   A 1 201 ? -17.683 12.243  -16.497 1.00 15.43  ? 201 ALA   A HB2  1 
ATOM   3036 H  HB3  . ALA   A 1 201 ? -19.219 11.837  -16.468 1.00 15.43  ? 201 ALA   A HB3  1 
ATOM   3037 N  N    . GLN   A 1 202 ? -21.203 13.038  -18.127 1.00 12.24  ? 202 GLN   A N    1 
ATOM   3038 C  CA   . GLN   A 1 202 ? -22.442 12.858  -18.884 1.00 12.02  ? 202 GLN   A CA   1 
ATOM   3039 C  C    . GLN   A 1 202 ? -22.660 13.992  -19.862 1.00 12.23  ? 202 GLN   A C    1 
ATOM   3040 O  O    . GLN   A 1 202 ? -23.076 13.751  -20.983 1.00 13.36  ? 202 GLN   A O    1 
ATOM   3041 C  CB   . GLN   A 1 202 ? -23.640 12.785  -17.920 1.00 12.28  ? 202 GLN   A CB   1 
ATOM   3042 C  CG   . GLN   A 1 202 ? -23.572 11.684  -16.883 1.00 13.12  ? 202 GLN   A CG   1 
ATOM   3043 C  CD   . GLN   A 1 202 ? -23.409 10.372  -17.435 1.00 14.73  ? 202 GLN   A CD   1 
ATOM   3044 O  OE1  . GLN   A 1 202 ? -24.121 9.913   -18.326 1.00 15.22  ? 202 GLN   A OE1  1 
ATOM   3045 N  NE2  . GLN   A 1 202 ? -22.410 9.676   -16.897 1.00 19.17  ? 202 GLN   A NE2  1 
ATOM   3046 H  H    . GLN   A 1 202 ? -21.316 13.121  -17.279 1.00 14.69  ? 202 GLN   A H    1 
ATOM   3047 H  HA   . GLN   A 1 202 ? -22.379 12.025  -19.378 1.00 14.43  ? 202 GLN   A HA   1 
ATOM   3048 H  HB2  . GLN   A 1 202 ? -23.700 13.628  -17.444 1.00 14.74  ? 202 GLN   A HB2  1 
ATOM   3049 H  HB3  . GLN   A 1 202 ? -24.444 12.641  -18.443 1.00 14.74  ? 202 GLN   A HB3  1 
ATOM   3050 H  HG2  . GLN   A 1 202 ? -22.817 11.853  -16.298 1.00 15.75  ? 202 GLN   A HG2  1 
ATOM   3051 H  HG3  . GLN   A 1 202 ? -24.396 11.688  -16.371 1.00 15.75  ? 202 GLN   A HG3  1 
ATOM   3052 H  HE21 . GLN   A 1 202 ? -21.930 10.025  -16.274 1.00 23.00  ? 202 GLN   A HE21 1 
ATOM   3053 H  HE22 . GLN   A 1 202 ? -22.245 8.878   -17.172 1.00 23.00  ? 202 GLN   A HE22 1 
ATOM   3054 N  N    . ALA   A 1 203 ? -22.415 15.226  -19.407 1.00 11.79  ? 203 ALA   A N    1 
ATOM   3055 C  CA   . ALA   A 1 203 ? -22.574 16.376  -20.280 1.00 12.15  ? 203 ALA   A CA   1 
ATOM   3056 C  C    . ALA   A 1 203 ? -21.659 16.280  -21.500 1.00 13.78  ? 203 ALA   A C    1 
ATOM   3057 O  O    . ALA   A 1 203 ? -22.054 16.611  -22.616 1.00 13.67  ? 203 ALA   A O    1 
ATOM   3058 C  CB   . ALA   A 1 203 ? -22.310 17.623  -19.490 1.00 14.25  ? 203 ALA   A CB   1 
ATOM   3059 H  H    . ALA   A 1 203 ? -22.160 15.416  -18.608 1.00 14.15  ? 203 ALA   A H    1 
ATOM   3060 H  HA   . ALA   A 1 203 ? -23.484 16.413  -20.613 1.00 14.57  ? 203 ALA   A HA   1 
ATOM   3061 H  HB1  . ALA   A 1 203 ? -22.429 18.394  -20.067 1.00 17.10  ? 203 ALA   A HB1  1 
ATOM   3062 H  HB2  . ALA   A 1 203 ? -22.933 17.666  -18.749 1.00 17.10  ? 203 ALA   A HB2  1 
ATOM   3063 H  HB3  . ALA   A 1 203 ? -21.399 17.598  -19.156 1.00 17.10  ? 203 ALA   A HB3  1 
ATOM   3064 N  N    . ALA   A 1 204 ? -20.411 15.886  -21.292 1.00 12.70  ? 204 ALA   A N    1 
ATOM   3065 C  CA   . ALA   A 1 204 ? -19.486 15.793  -22.419 1.00 13.44  ? 204 ALA   A CA   1 
ATOM   3066 C  C    . ALA   A 1 204 ? -19.966 14.799  -23.429 1.00 14.47  ? 204 ALA   A C    1 
ATOM   3067 O  O    . ALA   A 1 204 ? -19.916 15.063  -24.648 1.00 15.21  ? 204 ALA   A O    1 
ATOM   3068 C  CB   . ALA   A 1 204 ? -18.094 15.380  -21.899 1.00 14.60  ? 204 ALA   A CB   1 
ATOM   3069 H  H    . ALA   A 1 204 ? -20.079 15.672  -20.528 1.00 15.24  ? 204 ALA   A H    1 
ATOM   3070 H  HA   . ALA   A 1 204 ? -19.421 16.659  -22.851 1.00 16.12  ? 204 ALA   A HA   1 
ATOM   3071 H  HB1  . ALA   A 1 204 ? -17.484 15.308  -22.650 1.00 17.51  ? 204 ALA   A HB1  1 
ATOM   3072 H  HB2  . ALA   A 1 204 ? -17.776 16.054  -21.278 1.00 17.51  ? 204 ALA   A HB2  1 
ATOM   3073 H  HB3  . ALA   A 1 204 ? -18.166 14.524  -21.449 1.00 17.51  ? 204 ALA   A HB3  1 
ATOM   3074 N  N    . GLU   A 1 205 ? -20.488 13.649  -22.962 1.00 13.01  ? 205 GLU   A N    1 
ATOM   3075 C  CA   . GLU   A 1 205 ? -21.012 12.650  -23.882 1.00 13.45  ? 205 GLU   A CA   1 
ATOM   3076 C  C    . GLU   A 1 205 ? -22.216 13.191  -24.654 1.00 14.62  ? 205 GLU   A C    1 
ATOM   3077 O  O    . GLU   A 1 205 ? -22.327 13.028  -25.875 1.00 15.75  ? 205 GLU   A O    1 
ATOM   3078 C  CB   . GLU   A 1 205 ? -21.427 11.399  -23.063 1.00 15.48  ? 205 GLU   A CB   1 
ATOM   3079 C  CG   . GLU   A 1 205 ? -20.240 10.577  -22.590 1.00 18.04  ? 205 GLU   A CG   1 
ATOM   3080 C  CD   . GLU   A 1 205 ? -20.664 9.347   -21.793 1.00 33.72  ? 205 GLU   A CD   1 
ATOM   3081 O  OE1  . GLU   A 1 205 ? -21.867 8.972   -21.703 1.00 23.42  ? 205 GLU   A OE1  1 
ATOM   3082 O  OE2  . GLU   A 1 205 ? -19.769 8.723   -21.215 1.00 22.85  ? 205 GLU   A OE2  1 
ATOM   3083 H  H    . GLU   A 1 205 ? -20.544 13.435  -22.131 1.00 15.61  ? 205 GLU   A H    1 
ATOM   3084 H  HA   . GLU   A 1 205 ? -20.328 12.408  -24.525 1.00 16.14  ? 205 GLU   A HA   1 
ATOM   3085 H  HB2  . GLU   A 1 205 ? -21.923 11.685  -22.280 1.00 18.57  ? 205 GLU   A HB2  1 
ATOM   3086 H  HB3  . GLU   A 1 205 ? -21.983 10.830  -23.617 1.00 18.57  ? 205 GLU   A HB3  1 
ATOM   3087 H  HG2  . GLU   A 1 205 ? -19.735 10.276  -23.362 1.00 21.65  ? 205 GLU   A HG2  1 
ATOM   3088 H  HG3  . GLU   A 1 205 ? -19.680 11.127  -22.021 1.00 21.65  ? 205 GLU   A HG3  1 
ATOM   3089 N  N    . TYR   A 1 206 ? -23.169 13.835  -23.950 1.00 13.80  ? 206 TYR   A N    1 
ATOM   3090 C  CA   . TYR   A 1 206 ? -24.355 14.364  -24.591 1.00 15.03  ? 206 TYR   A CA   1 
ATOM   3091 C  C    . TYR   A 1 206 ? -23.989 15.476  -25.585 1.00 14.51  ? 206 TYR   A C    1 
ATOM   3092 O  O    . TYR   A 1 206 ? -24.512 15.543  -26.696 1.00 15.50  ? 206 TYR   A O    1 
ATOM   3093 C  CB   . TYR   A 1 206 ? -25.330 14.882  -23.515 1.00 16.91  ? 206 TYR   A CB   1 
ATOM   3094 C  CG   . TYR   A 1 206 ? -26.659 15.192  -24.100 1.00 17.30  ? 206 TYR   A CG   1 
ATOM   3095 C  CD1  . TYR   A 1 206 ? -26.917 16.401  -24.719 1.00 17.04  ? 206 TYR   A CD1  1 
ATOM   3096 C  CD2  . TYR   A 1 206 ? -27.635 14.215  -24.118 1.00 20.83  ? 206 TYR   A CD2  1 
ATOM   3097 C  CE1  . TYR   A 1 206 ? -28.147 16.647  -25.340 1.00 22.29  ? 206 TYR   A CE1  1 
ATOM   3098 C  CE2  . TYR   A 1 206 ? -28.870 14.450  -24.707 1.00 24.85  ? 206 TYR   A CE2  1 
ATOM   3099 C  CZ   . TYR   A 1 206 ? -29.086 15.645  -25.364 1.00 22.11  ? 206 TYR   A CZ   1 
ATOM   3100 O  OH   . TYR   A 1 206 ? -30.359 15.877  -25.901 1.00 32.48  ? 206 TYR   A OH   1 
ATOM   3101 H  H    . TYR   A 1 206 ? -23.140 13.972  -23.102 1.00 16.56  ? 206 TYR   A H    1 
ATOM   3102 H  HA   . TYR   A 1 206 ? -24.801 13.660  -25.086 1.00 18.04  ? 206 TYR   A HA   1 
ATOM   3103 H  HB2  . TYR   A 1 206 ? -25.446 14.202  -22.832 1.00 20.29  ? 206 TYR   A HB2  1 
ATOM   3104 H  HB3  . TYR   A 1 206 ? -24.972 15.692  -23.119 1.00 20.29  ? 206 TYR   A HB3  1 
ATOM   3105 H  HD1  . TYR   A 1 206 ? -26.263 17.063  -24.721 1.00 20.45  ? 206 TYR   A HD1  1 
ATOM   3106 H  HD2  . TYR   A 1 206 ? -27.463 13.388  -23.730 1.00 24.99  ? 206 TYR   A HD2  1 
ATOM   3107 H  HE1  . TYR   A 1 206 ? -28.325 17.473  -25.730 1.00 26.75  ? 206 TYR   A HE1  1 
ATOM   3108 H  HE2  . TYR   A 1 206 ? -29.544 13.810  -24.660 1.00 29.81  ? 206 TYR   A HE2  1 
ATOM   3109 H  HH   . TYR   A 1 206 ? -30.866 15.230  -25.729 1.00 38.98  ? 206 TYR   A HH   1 
ATOM   3110 N  N    . TYR   A 1 207 ? -23.093 16.355  -25.165 1.00 14.05  ? 207 TYR   A N    1 
ATOM   3111 C  CA   . TYR   A 1 207 ? -22.624 17.412  -26.068 1.00 14.95  ? 207 TYR   A CA   1 
ATOM   3112 C  C    . TYR   A 1 207 ? -22.011 16.811  -27.340 1.00 16.77  ? 207 TYR   A C    1 
ATOM   3113 O  O    . TYR   A 1 207 ? -22.290 17.290  -28.458 1.00 18.23  ? 207 TYR   A O    1 
ATOM   3114 C  CB   . TYR   A 1 207 ? -21.589 18.251  -25.297 1.00 15.65  ? 207 TYR   A CB   1 
ATOM   3115 C  CG   . TYR   A 1 207 ? -20.777 19.199  -26.150 1.00 16.23  ? 207 TYR   A CG   1 
ATOM   3116 C  CD1  . TYR   A 1 207 ? -21.252 20.422  -26.493 1.00 18.48  ? 207 TYR   A CD1  1 
ATOM   3117 C  CD2  . TYR   A 1 207 ? -19.535 18.867  -26.634 1.00 18.30  ? 207 TYR   A CD2  1 
ATOM   3118 C  CE1  . TYR   A 1 207 ? -20.528 21.275  -27.301 1.00 20.25  ? 207 TYR   A CE1  1 
ATOM   3119 C  CE2  . TYR   A 1 207 ? -18.810 19.745  -27.415 1.00 19.25  ? 207 TYR   A CE2  1 
ATOM   3120 C  CZ   . TYR   A 1 207 ? -19.294 20.929  -27.745 1.00 17.59  ? 207 TYR   A CZ   1 
ATOM   3121 O  OH   . TYR   A 1 207 ? -18.602 21.809  -28.575 1.00 21.55  ? 207 TYR   A OH   1 
ATOM   3122 H  H    . TYR   A 1 207 ? -22.743 16.369  -24.379 1.00 16.86  ? 207 TYR   A H    1 
ATOM   3123 H  HA   . TYR   A 1 207 ? -23.357 17.982  -26.347 1.00 17.94  ? 207 TYR   A HA   1 
ATOM   3124 H  HB2  . TYR   A 1 207 ? -22.056 18.783  -24.634 1.00 18.78  ? 207 TYR   A HB2  1 
ATOM   3125 H  HB3  . TYR   A 1 207 ? -20.968 17.648  -24.859 1.00 18.78  ? 207 TYR   A HB3  1 
ATOM   3126 H  HD1  . TYR   A 1 207 ? -22.084 20.692  -26.177 1.00 22.17  ? 207 TYR   A HD1  1 
ATOM   3127 H  HD2  . TYR   A 1 207 ? -19.175 18.034  -26.432 1.00 21.96  ? 207 TYR   A HD2  1 
ATOM   3128 H  HE1  . TYR   A 1 207 ? -20.890 22.096  -27.543 1.00 24.31  ? 207 TYR   A HE1  1 
ATOM   3129 H  HE2  . TYR   A 1 207 ? -17.965 19.498  -27.715 1.00 23.09  ? 207 TYR   A HE2  1 
ATOM   3130 H  HH   . TYR   A 1 207 ? -19.062 22.499  -28.710 1.00 25.86  ? 207 TYR   A HH   1 
ATOM   3131 N  N    . SER   A 1 208 ? -21.192 15.763  -27.193 1.00 15.71  ? 208 SER   A N    1 
ATOM   3132 C  CA   . SER   A 1 208 ? -20.490 15.215  -28.359 1.00 17.68  ? 208 SER   A CA   1 
ATOM   3133 C  C    . SER   A 1 208 ? -21.385 14.435  -29.295 1.00 22.40  ? 208 SER   A C    1 
ATOM   3134 O  O    . SER   A 1 208 ? -21.335 14.638  -30.517 1.00 20.87  ? 208 SER   A O    1 
ATOM   3135 C  CB   . SER   A 1 208 ? -19.382 14.334  -27.808 1.00 20.63  ? 208 SER   A CB   1 
ATOM   3136 O  OG   . SER   A 1 208 ? -18.343 14.332  -28.813 1.00 45.47  ? 208 SER   A OG   1 
ATOM   3137 H  H    . SER   A 1 208 ? -21.029 15.362  -26.450 1.00 18.85  ? 208 SER   A H    1 
ATOM   3138 H  HA   . SER   A 1 208 ? -20.135 15.938  -28.900 1.00 21.22  ? 208 SER   A HA   1 
ATOM   3139 H  HB2  . SER   A 1 208 ? -19.043 14.701  -26.976 1.00 24.76  ? 208 SER   A HB2  1 
ATOM   3140 H  HB3  . SER   A 1 208 ? -19.710 13.433  -27.663 1.00 24.76  ? 208 SER   A HB3  1 
ATOM   3141 H  HG   . SER   A 1 208 ? -17.714 13.827  -28.576 1.00 54.56  ? 208 SER   A HG   1 
ATOM   3142 N  N    . VAL   A 1 209 ? -22.264 13.574  -28.782 1.00 18.98  ? 209 VAL   A N    1 
ATOM   3143 C  CA   . VAL   A 1 209 ? -22.957 12.584  -29.599 1.00 22.68  ? 209 VAL   A CA   1 
ATOM   3144 C  C    . VAL   A 1 209 ? -24.442 12.505  -29.306 1.00 23.26  ? 209 VAL   A C    1 
ATOM   3145 O  O    . VAL   A 1 209 ? -25.156 11.712  -29.937 1.00 26.12  ? 209 VAL   A O    1 
ATOM   3146 C  CB   . VAL   A 1 209 ? -22.336 11.180  -29.490 1.00 29.41  ? 209 VAL   A CB   1 
ATOM   3147 C  CG1  . VAL   A 1 209 ? -20.918 11.162  -30.054 1.00 37.02  ? 209 VAL   A CG1  1 
ATOM   3148 C  CG2  . VAL   A 1 209 ? -22.379 10.661  -28.087 1.00 27.60  ? 209 VAL   A CG2  1 
ATOM   3149 H  H    . VAL   A 1 209 ? -22.477 13.545  -27.950 1.00 22.78  ? 209 VAL   A H    1 
ATOM   3150 H  HA   . VAL   A 1 209 ? -22.859 12.868  -30.521 1.00 27.22  ? 209 VAL   A HA   1 
ATOM   3151 H  HB   . VAL   A 1 209 ? -22.870 10.574  -30.027 1.00 35.29  ? 209 VAL   A HB   1 
ATOM   3152 H  HG11 . VAL   A 1 209 ? -20.556 10.266  -29.970 1.00 44.43  ? 209 VAL   A HG11 1 
ATOM   3153 H  HG12 . VAL   A 1 209 ? -20.946 11.422  -30.988 1.00 44.43  ? 209 VAL   A HG12 1 
ATOM   3154 H  HG13 . VAL   A 1 209 ? -20.371 11.788  -29.553 1.00 44.43  ? 209 VAL   A HG13 1 
ATOM   3155 H  HG21 . VAL   A 1 209 ? -21.985 9.775   -28.066 1.00 33.11  ? 209 VAL   A HG21 1 
ATOM   3156 H  HG22 . VAL   A 1 209 ? -21.876 11.260  -27.514 1.00 33.11  ? 209 VAL   A HG22 1 
ATOM   3157 H  HG23 . VAL   A 1 209 ? -23.303 10.620  -27.794 1.00 33.11  ? 209 VAL   A HG23 1 
ATOM   3158 N  N    . GLY   A 1 210 ? -24.954 13.314  -28.409 1.00 19.98  ? 210 GLY   A N    1 
ATOM   3159 C  CA   . GLY   A 1 210 ? -26.357 13.386  -28.180 1.00 19.43  ? 210 GLY   A CA   1 
ATOM   3160 C  C    . GLY   A 1 210 ? -26.967 12.269  -27.385 1.00 20.16  ? 210 GLY   A C    1 
ATOM   3161 O  O    . GLY   A 1 210 ? -28.183 12.099  -27.381 1.00 24.16  ? 210 GLY   A O    1 
ATOM   3162 H  H    . GLY   A 1 210 ? -24.491 13.841  -27.911 1.00 23.98  ? 210 GLY   A H    1 
ATOM   3163 H  HA2  . GLY   A 1 210 ? -26.546 14.212  -27.708 1.00 23.32  ? 210 GLY   A HA2  1 
ATOM   3164 H  HA3  . GLY   A 1 210 ? -26.805 13.405  -29.040 1.00 23.32  ? 210 GLY   A HA3  1 
ATOM   3165 N  N    . LYS   A 1 211 ? -26.135 11.504  -26.699 1.00 19.36  ? 211 LYS   A N    1 
ATOM   3166 C  CA   . LYS   A 1 211 ? -26.567 10.388  -25.867 1.00 20.77  ? 211 LYS   A CA   1 
ATOM   3167 C  C    . LYS   A 1 211 ? -25.516 10.257  -24.766 1.00 18.32  ? 211 LYS   A C    1 
ATOM   3168 O  O    . LYS   A 1 211 ? -24.335 10.513  -24.969 1.00 18.89  ? 211 LYS   A O    1 
ATOM   3169 C  CB   . LYS   A 1 211 ? -26.652 9.067   -26.622 1.00 26.41  ? 211 LYS   A CB   1 
ATOM   3170 C  CG   . LYS   A 1 211 ? -25.423 8.662   -27.338 1.00 35.88  ? 211 LYS   A CG   1 
ATOM   3171 C  CD   . LYS   A 1 211 ? -25.465 7.216   -27.890 1.00 41.95  ? 211 LYS   A CD   1 
ATOM   3172 C  CE   . LYS   A 1 211 ? -24.117 6.834   -28.541 1.00 45.82  ? 211 LYS   A CE   1 
ATOM   3173 N  NZ   . LYS   A 1 211 ? -24.292 6.022   -29.793 1.00 52.06  ? 211 LYS   A NZ   1 
ATOM   3174 H  H    . LYS   A 1 211 ? -25.282 11.612  -26.698 1.00 23.24  ? 211 LYS   A H    1 
ATOM   3175 H  HA   . LYS   A 1 211 ? -27.450 10.568  -25.509 1.00 24.93  ? 211 LYS   A HA   1 
ATOM   3176 H  HB2  . LYS   A 1 211 ? -26.860 8.366   -25.985 1.00 31.70  ? 211 LYS   A HB2  1 
ATOM   3177 H  HB3  . LYS   A 1 211 ? -27.360 9.138   -27.281 1.00 31.70  ? 211 LYS   A HB3  1 
ATOM   3178 H  HG2  . LYS   A 1 211 ? -25.288 9.260   -28.089 1.00 43.05  ? 211 LYS   A HG2  1 
ATOM   3179 H  HG3  . LYS   A 1 211 ? -24.672 8.721   -26.727 1.00 43.05  ? 211 LYS   A HG3  1 
ATOM   3180 H  HD2  . LYS   A 1 211 ? -25.642 6.597   -27.164 1.00 50.34  ? 211 LYS   A HD2  1 
ATOM   3181 H  HD3  . LYS   A 1 211 ? -26.162 7.147   -28.562 1.00 50.34  ? 211 LYS   A HD3  1 
ATOM   3182 H  HE2  . LYS   A 1 211 ? -23.636 7.643   -28.773 1.00 54.99  ? 211 LYS   A HE2  1 
ATOM   3183 H  HE3  . LYS   A 1 211 ? -23.599 6.308   -27.912 1.00 54.99  ? 211 LYS   A HE3  1 
ATOM   3184 H  HZ1  . LYS   A 1 211 ? -23.496 5.816   -30.136 1.00 62.47  ? 211 LYS   A HZ1  1 
ATOM   3185 H  HZ2  . LYS   A 1 211 ? -24.730 5.269   -29.610 1.00 62.47  ? 211 LYS   A HZ2  1 
ATOM   3186 H  HZ3  . LYS   A 1 211 ? -24.754 6.486   -30.395 1.00 62.47  ? 211 LYS   A HZ3  1 
ATOM   3187 N  N    . ASN   A 1 212 ? -25.954 9.817   -23.596 1.00 17.36  ? 212 ASN   A N    1 
ATOM   3188 C  CA   . ASN   A 1 212 ? -25.080 9.586   -22.449 1.00 16.32  ? 212 ASN   A CA   1 
ATOM   3189 C  C    . ASN   A 1 212 ? -25.564 8.324   -21.756 1.00 17.93  ? 212 ASN   A C    1 
ATOM   3190 O  O    . ASN   A 1 212 ? -26.734 8.006   -21.805 1.00 20.28  ? 212 ASN   A O    1 
ATOM   3191 C  CB   . ASN   A 1 212 ? -25.039 10.782  -21.507 1.00 16.44  ? 212 ASN   A CB   1 
ATOM   3192 C  CG   . ASN   A 1 212 ? -26.392 11.127  -20.908 1.00 17.71  ? 212 ASN   A CG   1 
ATOM   3193 O  OD1  . ASN   A 1 212 ? -27.280 11.627  -21.597 1.00 20.18  ? 212 ASN   A OD1  1 
ATOM   3194 N  ND2  . ASN   A 1 212 ? -26.523 10.947  -19.596 1.00 17.46  ? 212 ASN   A ND2  1 
ATOM   3195 H  H    . ASN   A 1 212 ? -26.779 9.639   -23.433 1.00 20.84  ? 212 ASN   A H    1 
ATOM   3196 H  HA   . ASN   A 1 212 ? -24.163 9.444   -22.729 1.00 19.58  ? 212 ASN   A HA   1 
ATOM   3197 H  HB2  . ASN   A 1 212 ? -24.432 10.585  -20.777 1.00 19.73  ? 212 ASN   A HB2  1 
ATOM   3198 H  HB3  . ASN   A 1 212 ? -24.726 11.558  -21.999 1.00 19.73  ? 212 ASN   A HB3  1 
ATOM   3199 H  HD21 . ASN   A 1 212 ? -27.270 11.129  -19.209 1.00 20.95  ? 212 ASN   A HD21 1 
ATOM   3200 H  HD22 . ASN   A 1 212 ? -25.861 10.650  -19.134 1.00 20.95  ? 212 ASN   A HD22 1 
ATOM   3201 N  N    . SER   A 1 213 ? -24.632 7.676   -21.051 1.00 17.98  ? 213 SER   A N    1 
ATOM   3202 C  CA   . SER   A 1 213 ? -24.873 6.339   -20.535 1.00 19.42  ? 213 SER   A CA   1 
ATOM   3203 C  C    . SER   A 1 213 ? -25.515 6.313   -19.152 1.00 16.81  ? 213 SER   A C    1 
ATOM   3204 O  O    . SER   A 1 213 ? -26.028 5.262   -18.760 1.00 19.97  ? 213 SER   A O    1 
ATOM   3205 C  CB   . SER   A 1 213 ? -23.538 5.595   -20.441 1.00 17.47  ? 213 SER   A CB   1 
ATOM   3206 O  OG   . SER   A 1 213 ? -22.713 6.241   -19.494 1.00 19.11  ? 213 SER   A OG   1 
ATOM   3207 H  H    . SER   A 1 213 ? -23.856 7.994   -20.862 1.00 21.57  ? 213 SER   A H    1 
ATOM   3208 H  HA   . SER   A 1 213 ? -25.470 5.880   -21.146 1.00 23.31  ? 213 SER   A HA   1 
ATOM   3209 H  HB2  . SER   A 1 213 ? -23.697 4.681   -20.160 1.00 20.97  ? 213 SER   A HB2  1 
ATOM   3210 H  HB3  . SER   A 1 213 ? -23.102 5.605   -21.308 1.00 20.97  ? 213 SER   A HB3  1 
ATOM   3211 H  HG   . SER   A 1 213 ? -21.988 5.824   -19.413 1.00 22.93  ? 213 SER   A HG   1 
ATOM   3212 N  N    . TRP   A 1 214 ? -25.469 7.416   -18.408 1.00 14.49  ? 214 TRP   A N    1 
ATOM   3213 C  CA   . TRP   A 1 214 ? -25.864 7.488   -17.008 1.00 15.34  ? 214 TRP   A CA   1 
ATOM   3214 C  C    . TRP   A 1 214 ? -24.972 6.612   -16.175 1.00 16.69  ? 214 TRP   A C    1 
ATOM   3215 O  O    . TRP   A 1 214 ? -25.274 6.313   -15.027 1.00 16.88  ? 214 TRP   A O    1 
ATOM   3216 C  CB   . TRP   A 1 214 ? -27.325 7.201   -16.814 1.00 16.51  ? 214 TRP   A CB   1 
ATOM   3217 C  CG   . TRP   A 1 214 ? -28.203 8.294   -17.382 1.00 15.95  ? 214 TRP   A CG   1 
ATOM   3218 C  CD1  . TRP   A 1 214 ? -29.161 8.139   -18.350 1.00 21.91  ? 214 TRP   A CD1  1 
ATOM   3219 C  CD2  . TRP   A 1 214 ? -28.233 9.663   -16.989 1.00 14.78  ? 214 TRP   A CD2  1 
ATOM   3220 N  NE1  . TRP   A 1 214 ? -29.779 9.342   -18.570 1.00 21.32  ? 214 TRP   A NE1  1 
ATOM   3221 C  CE2  . TRP   A 1 214 ? -29.233 10.287  -17.761 1.00 19.05  ? 214 TRP   A CE2  1 
ATOM   3222 C  CE3  . TRP   A 1 214 ? -27.511 10.424  -16.106 1.00 15.87  ? 214 TRP   A CE3  1 
ATOM   3223 C  CZ2  . TRP   A 1 214 ? -29.522 11.643  -17.622 1.00 20.61  ? 214 TRP   A CZ2  1 
ATOM   3224 C  CZ3  . TRP   A 1 214 ? -27.838 11.782  -15.982 1.00 18.35  ? 214 TRP   A CZ3  1 
ATOM   3225 C  CH2  . TRP   A 1 214 ? -28.821 12.341  -16.753 1.00 19.09  ? 214 TRP   A CH2  1 
ATOM   3226 H  H    . TRP   A 1 214 ? -25.197 8.174   -18.711 1.00 17.39  ? 214 TRP   A H    1 
ATOM   3227 H  HA   . TRP   A 1 214 ? -25.757 8.394   -16.680 1.00 18.41  ? 214 TRP   A HA   1 
ATOM   3228 H  HB2  . TRP   A 1 214 ? -27.548 6.370   -17.262 1.00 19.82  ? 214 TRP   A HB2  1 
ATOM   3229 H  HB3  . TRP   A 1 214 ? -27.511 7.126   -15.865 1.00 19.82  ? 214 TRP   A HB3  1 
ATOM   3230 H  HD1  . TRP   A 1 214 ? -29.360 7.343   -18.788 1.00 26.29  ? 214 TRP   A HD1  1 
ATOM   3231 H  HE1  . TRP   A 1 214 ? -30.414 9.477   -19.134 1.00 25.59  ? 214 TRP   A HE1  1 
ATOM   3232 H  HE3  . TRP   A 1 214 ? -26.824 10.050  -15.603 1.00 19.04  ? 214 TRP   A HE3  1 
ATOM   3233 H  HZ2  . TRP   A 1 214 ? -30.191 12.044  -18.129 1.00 24.73  ? 214 TRP   A HZ2  1 
ATOM   3234 H  HZ3  . TRP   A 1 214 ? -27.380 12.309  -15.368 1.00 22.01  ? 214 TRP   A HZ3  1 
ATOM   3235 H  HH2  . TRP   A 1 214 ? -29.001 13.249  -16.660 1.00 22.91  ? 214 TRP   A HH2  1 
ATOM   3236 N  N    . GLN   A 1 215 ? -23.783 6.312   -16.677 1.00 15.71  ? 215 GLN   A N    1 
ATOM   3237 C  CA   . GLN   A 1 215 ? -22.816 5.476   -15.976 1.00 15.28  ? 215 GLN   A CA   1 
ATOM   3238 C  C    . GLN   A 1 215 ? -21.458 6.122   -16.087 1.00 15.06  ? 215 GLN   A C    1 
ATOM   3239 O  O    . GLN   A 1 215 ? -21.227 6.963   -16.984 1.00 17.71  ? 215 GLN   A O    1 
ATOM   3240 C  CB   . GLN   A 1 215 ? -22.764 4.102   -16.563 1.00 15.61  ? 215 GLN   A CB   1 
ATOM   3241 C  CG   . GLN   A 1 215 ? -24.056 3.331   -16.441 1.00 17.65  ? 215 GLN   A CG   1 
ATOM   3242 C  CD   . GLN   A 1 215 ? -24.051 1.984   -17.053 1.00 21.67  ? 215 GLN   A CD   1 
ATOM   3243 O  OE1  . GLN   A 1 215 ? -23.059 1.568   -17.714 1.00 23.18  ? 215 GLN   A OE1  1 
ATOM   3244 N  NE2  . GLN   A 1 215 ? -25.139 1.265   -16.865 1.00 24.58  ? 215 GLN   A NE2  1 
ATOM   3245 H  H    . GLN   A 1 215 ? -23.504 6.588   -17.443 1.00 18.85  ? 215 GLN   A H    1 
ATOM   3246 H  HA   . GLN   A 1 215 ? -23.057 5.401   -15.039 1.00 18.34  ? 215 GLN   A HA   1 
ATOM   3247 H  HB2  . GLN   A 1 215 ? -22.553 4.175   -17.507 1.00 18.73  ? 215 GLN   A HB2  1 
ATOM   3248 H  HB3  . GLN   A 1 215 ? -22.074 3.595   -16.108 1.00 18.73  ? 215 GLN   A HB3  1 
ATOM   3249 H  HG2  . GLN   A 1 215 ? -24.258 3.219   -15.499 1.00 21.18  ? 215 GLN   A HG2  1 
ATOM   3250 H  HG3  . GLN   A 1 215 ? -24.759 3.841   -16.873 1.00 21.18  ? 215 GLN   A HG3  1 
ATOM   3251 H  HE21 . GLN   A 1 215 ? -25.794 1.588   -16.410 1.00 29.50  ? 215 GLN   A HE21 1 
ATOM   3252 H  HE22 . GLN   A 1 215 ? -25.194 0.474   -17.197 1.00 29.50  ? 215 GLN   A HE22 1 
ATOM   3253 N  N    . ILE   A 1 216 ? -20.565 5.767   -15.197 1.00 13.68  ? 216 ILE   A N    1 
ATOM   3254 C  CA   . ILE   A 1 216 ? -19.191 6.233   -15.219 1.00 14.25  ? 216 ILE   A CA   1 
ATOM   3255 C  C    . ILE   A 1 216 ? -18.319 5.031   -15.459 1.00 14.20  ? 216 ILE   A C    1 
ATOM   3256 O  O    . ILE   A 1 216 ? -18.389 4.044   -14.737 1.00 15.25  ? 216 ILE   A O    1 
ATOM   3257 C  CB   . ILE   A 1 216 ? -18.774 6.933   -13.924 1.00 15.16  ? 216 ILE   A CB   1 
ATOM   3258 C  CG1  . ILE   A 1 216 ? -19.679 8.142   -13.640 1.00 15.57  ? 216 ILE   A CG1  1 
ATOM   3259 C  CG2  . ILE   A 1 216 ? -17.314 7.299   -13.967 1.00 17.10  ? 216 ILE   A CG2  1 
ATOM   3260 C  CD1  . ILE   A 1 216 ? -19.563 9.274   -14.648 1.00 17.60  ? 216 ILE   A CD1  1 
ATOM   3261 H  H    . ILE   A 1 216 ? -20.733 5.235   -14.542 1.00 16.41  ? 216 ILE   A H    1 
ATOM   3262 H  HA   . ILE   A 1 216 ? -19.089 6.868   -15.946 1.00 17.10  ? 216 ILE   A HA   1 
ATOM   3263 H  HB   . ILE   A 1 216 ? -18.893 6.316   -13.186 1.00 18.19  ? 216 ILE   A HB   1 
ATOM   3264 H  HG12 . ILE   A 1 216 ? -20.602 7.843   -13.641 1.00 18.69  ? 216 ILE   A HG12 1 
ATOM   3265 H  HG13 . ILE   A 1 216 ? -19.448 8.501   -12.769 1.00 18.69  ? 216 ILE   A HG13 1 
ATOM   3266 H  HG21 . ILE   A 1 216 ? -17.117 7.895   -13.228 1.00 20.52  ? 216 ILE   A HG21 1 
ATOM   3267 H  HG22 . ILE   A 1 216 ? -16.784 6.491   -13.892 1.00 20.52  ? 216 ILE   A HG22 1 
ATOM   3268 H  HG23 . ILE   A 1 216 ? -17.124 7.742   -14.809 1.00 20.52  ? 216 ILE   A HG23 1 
ATOM   3269 H  HD11 . ILE   A 1 216 ? -20.163 9.991   -14.388 1.00 21.12  ? 216 ILE   A HD11 1 
ATOM   3270 H  HD12 . ILE   A 1 216 ? -18.648 9.596   -14.657 1.00 21.12  ? 216 ILE   A HD12 1 
ATOM   3271 H  HD13 . ILE   A 1 216 ? -19.805 8.941   -15.526 1.00 21.12  ? 216 ILE   A HD13 1 
ATOM   3272 N  N    . GLY   A 1 217 ? -17.482 5.140   -16.498 1.00 15.78  ? 217 GLY   A N    1 
ATOM   3273 C  CA   . GLY   A 1 217 ? -16.531 4.100   -16.817 1.00 17.84  ? 217 GLY   A CA   1 
ATOM   3274 C  C    . GLY   A 1 217 ? -16.967 2.842   -17.558 1.00 18.57  ? 217 GLY   A C    1 
ATOM   3275 O  O    . GLY   A 1 217 ? -16.126 1.968   -17.691 1.00 18.05  ? 217 GLY   A O    1 
ATOM   3276 H  H    . GLY   A 1 217 ? -17.454 5.816   -17.030 1.00 18.94  ? 217 GLY   A H    1 
ATOM   3277 H  HA2  . GLY   A 1 217 ? -15.835 4.503   -17.359 1.00 21.41  ? 217 GLY   A HA2  1 
ATOM   3278 H  HA3  . GLY   A 1 217 ? -16.144 3.798   -15.980 1.00 21.41  ? 217 GLY   A HA3  1 
ATOM   3279 N  N    . PRO   A 1 218 ? -18.189 2.654   -18.071 1.00 17.26  ? 218 PRO   A N    1 
ATOM   3280 C  CA   . PRO   A 1 218 ? -18.468 1.390   -18.764 1.00 17.30  ? 218 PRO   A CA   1 
ATOM   3281 C  C    . PRO   A 1 218 ? -17.537 1.176   -19.965 1.00 18.67  ? 218 PRO   A C    1 
ATOM   3282 O  O    . PRO   A 1 218 ? -17.092 0.044   -20.191 1.00 19.98  ? 218 PRO   A O    1 
ATOM   3283 C  CB   . PRO   A 1 218 ? -19.941 1.505   -19.183 1.00 21.27  ? 218 PRO   A CB   1 
ATOM   3284 C  CG   . PRO   A 1 218 ? -20.169 2.936   -19.302 1.00 17.36  ? 218 PRO   A CG   1 
ATOM   3285 C  CD   . PRO   A 1 218 ? -19.327 3.579   -18.161 1.00 18.29  ? 218 PRO   A CD   1 
ATOM   3286 H  HA   . PRO   A 1 218 ? -18.396 0.644   -18.149 1.00 20.76  ? 218 PRO   A HA   1 
ATOM   3287 H  HB2  . PRO   A 1 218 ? -20.082 1.057   -20.032 1.00 25.52  ? 218 PRO   A HB2  1 
ATOM   3288 H  HB3  . PRO   A 1 218 ? -20.512 1.115   -18.503 1.00 25.52  ? 218 PRO   A HB3  1 
ATOM   3289 H  HG2  . PRO   A 1 218 ? -19.870 3.247   -20.170 1.00 20.83  ? 218 PRO   A HG2  1 
ATOM   3290 H  HG3  . PRO   A 1 218 ? -21.113 3.130   -19.187 1.00 20.83  ? 218 PRO   A HG3  1 
ATOM   3291 H  HD2  . PRO   A 1 218 ? -19.035 4.472   -18.402 1.00 21.94  ? 218 PRO   A HD2  1 
ATOM   3292 H  HD3  . PRO   A 1 218 ? -19.825 3.605   -17.329 1.00 21.94  ? 218 PRO   A HD3  1 
ATOM   3293 N  N    . GLU   A 1 219 ? -17.148 2.253   -20.637 1.00 16.89  ? 219 GLU   A N    1 
ATOM   3294 C  CA   . GLU   A 1 219 ? -16.290 2.138   -21.811 1.00 17.32  ? 219 GLU   A CA   1 
ATOM   3295 C  C    . GLU   A 1 219 ? -14.883 1.745   -21.459 1.00 19.45  ? 219 GLU   A C    1 
ATOM   3296 O  O    . GLU   A 1 219 ? -14.170 1.311   -22.379 1.00 21.40  ? 219 GLU   A O    1 
ATOM   3297 C  CB   . GLU   A 1 219 ? -16.284 3.475   -22.567 1.00 21.05  ? 219 GLU   A CB   1 
ATOM   3298 C  CG   . GLU   A 1 219 ? -15.656 4.651   -21.828 1.00 22.82  ? 219 GLU   A CG   1 
ATOM   3299 C  CD   . GLU   A 1 219 ? -16.527 5.384   -20.801 1.00 27.41  ? 219 GLU   A CD   1 
ATOM   3300 O  OE1  . GLU   A 1 219 ? -17.640 4.915   -20.408 1.00 22.68  ? 219 GLU   A OE1  1 
ATOM   3301 O  OE2  . GLU   A 1 219 ? -16.094 6.489   -20.433 1.00 22.50  ? 219 GLU   A OE2  1 
ATOM   3302 H  H    . GLU   A 1 219 ? -17.366 3.060   -20.435 1.00 20.26  ? 219 GLU   A H    1 
ATOM   3303 H  HA   . GLU   A 1 219 ? -16.647 1.457   -22.402 1.00 20.78  ? 219 GLU   A HA   1 
ATOM   3304 H  HB2  . GLU   A 1 219 ? -15.787 3.356   -23.392 1.00 25.26  ? 219 GLU   A HB2  1 
ATOM   3305 H  HB3  . GLU   A 1 219 ? -17.202 3.717   -22.764 1.00 25.26  ? 219 GLU   A HB3  1 
ATOM   3306 H  HG2  . GLU   A 1 219 ? -14.877 4.322   -21.351 1.00 27.39  ? 219 GLU   A HG2  1 
ATOM   3307 H  HG3  . GLU   A 1 219 ? -15.387 5.309   -22.488 1.00 27.39  ? 219 GLU   A HG3  1 
ATOM   3308 N  N    . ILE   A 1 220 ? -14.477 1.799   -20.191 1.00 18.15  ? 220 ILE   A N    1 
ATOM   3309 C  CA   . ILE   A 1 220 ? -13.134 1.412   -19.789 1.00 18.28  ? 220 ILE   A CA   1 
ATOM   3310 C  C    . ILE   A 1 220 ? -13.088 0.201   -18.868 1.00 21.14  ? 220 ILE   A C    1 
ATOM   3311 O  O    . ILE   A 1 220 ? -12.006 -0.206  -18.460 1.00 19.10  ? 220 ILE   A O    1 
ATOM   3312 C  CB   . ILE   A 1 220 ? -12.262 2.566   -19.285 1.00 19.04  ? 220 ILE   A CB   1 
ATOM   3313 C  CG1  . ILE   A 1 220 ? -12.927 3.345   -18.145 1.00 18.66  ? 220 ILE   A CG1  1 
ATOM   3314 C  CG2  . ILE   A 1 220 ? -11.966 3.545   -20.455 1.00 20.29  ? 220 ILE   A CG2  1 
ATOM   3315 C  CD1  . ILE   A 1 220 ? -12.936 2.592   -16.819 1.00 23.16  ? 220 ILE   A CD1  1 
ATOM   3316 H  H    . ILE   A 1 220 ? -14.972 2.062   -19.538 1.00 21.78  ? 220 ILE   A H    1 
ATOM   3317 H  HA   . ILE   A 1 220 ? -12.691 1.129   -20.605 1.00 21.94  ? 220 ILE   A HA   1 
ATOM   3318 H  HB   . ILE   A 1 220 ? -11.443 2.174   -18.942 1.00 22.84  ? 220 ILE   A HB   1 
ATOM   3319 H  HG12 . ILE   A 1 220 ? -12.446 4.177   -18.012 1.00 22.39  ? 220 ILE   A HG12 1 
ATOM   3320 H  HG13 . ILE   A 1 220 ? -13.848 3.530   -18.389 1.00 22.39  ? 220 ILE   A HG13 1 
ATOM   3321 H  HG21 . ILE   A 1 220 ? -11.464 4.302   -20.114 1.00 24.34  ? 220 ILE   A HG21 1 
ATOM   3322 H  HG22 . ILE   A 1 220 ? -11.447 3.082   -21.131 1.00 24.34  ? 220 ILE   A HG22 1 
ATOM   3323 H  HG23 . ILE   A 1 220 ? -12.806 3.848   -20.833 1.00 24.34  ? 220 ILE   A HG23 1 
ATOM   3324 H  HD11 . ILE   A 1 220 ? -13.146 3.213   -16.104 1.00 27.79  ? 220 ILE   A HD11 1 
ATOM   3325 H  HD12 . ILE   A 1 220 ? -13.606 1.892   -16.858 1.00 27.79  ? 220 ILE   A HD12 1 
ATOM   3326 H  HD13 . ILE   A 1 220 ? -12.060 2.202   -16.671 1.00 27.79  ? 220 ILE   A HD13 1 
ATOM   3327 N  N    . MET   A 1 221 ? -14.220 -0.409  -18.538 1.00 21.05  ? 221 MET   A N    1 
ATOM   3328 C  CA   . MET   A 1 221 ? -14.194 -1.619  -17.732 1.00 21.80  ? 221 MET   A CA   1 
ATOM   3329 C  C    . MET   A 1 221 ? -13.942 -2.818  -18.623 1.00 22.70  ? 221 MET   A C    1 
ATOM   3330 O  O    . MET   A 1 221 ? -14.596 -2.988  -19.666 1.00 22.11  ? 221 MET   A O    1 
ATOM   3331 C  CB   . MET   A 1 221 ? -15.505 -1.841  -16.945 1.00 23.48  ? 221 MET   A CB   1 
ATOM   3332 C  CG   . MET   A 1 221 ? -15.875 -0.763  -15.947 1.00 31.02  ? 221 MET   A CG   1 
ATOM   3333 S  SD   . MET   A 1 221 ? -14.595 -0.349  -14.717 1.00 59.11  ? 221 MET   A SD   1 
ATOM   3334 C  CE   . MET   A 1 221 ? -14.282 -1.999  -14.171 1.00 32.07  ? 221 MET   A CE   1 
ATOM   3335 H  H    . MET   A 1 221 ? -15.006 -0.144  -18.766 1.00 25.26  ? 221 MET   A H    1 
ATOM   3336 H  HA   . MET   A 1 221 ? -13.486 -1.517  -17.078 1.00 26.16  ? 221 MET   A HA   1 
ATOM   3337 H  HB2  . MET   A 1 221 ? -16.234 -1.903  -17.582 1.00 28.18  ? 221 MET   A HB2  1 
ATOM   3338 H  HB3  . MET   A 1 221 ? -15.424 -2.672  -16.452 1.00 28.18  ? 221 MET   A HB3  1 
ATOM   3339 H  HG2  . MET   A 1 221 ? -16.076 0.050   -16.438 1.00 37.22  ? 221 MET   A HG2  1 
ATOM   3340 H  HG3  . MET   A 1 221 ? -16.659 -1.058  -15.458 1.00 37.22  ? 221 MET   A HG3  1 
ATOM   3341 H  HE1  . MET   A 1 221 ? -13.600 -1.980  -13.482 1.00 38.48  ? 221 MET   A HE1  1 
ATOM   3342 H  HE2  . MET   A 1 221 ? -15.102 -2.375  -13.814 1.00 38.48  ? 221 MET   A HE2  1 
ATOM   3343 H  HE3  . MET   A 1 221 ? -13.976 -2.528  -14.924 1.00 38.48  ? 221 MET   A HE3  1 
ATOM   3344 N  N    . LYS   A 1 222 ? -13.001 -3.673  -18.232 1.00 23.20  ? 222 LYS   A N    1 
ATOM   3345 C  CA   . LYS   A 1 222 ? -12.767 -4.893  -18.988 1.00 23.89  ? 222 LYS   A CA   1 
ATOM   3346 C  C    . LYS   A 1 222 ? -13.921 -5.885  -18.793 1.00 29.04  ? 222 LYS   A C    1 
ATOM   3347 O  O    . LYS   A 1 222 ? -14.467 -6.016  -17.695 1.00 28.26  ? 222 LYS   A O    1 
ATOM   3348 C  CB   . LYS   A 1 222 ? -11.474 -5.551  -18.536 1.00 25.85  ? 222 LYS   A CB   1 
ATOM   3349 C  CG   . LYS   A 1 222 ? -10.229 -4.723  -18.814 1.00 26.81  ? 222 LYS   A CG   1 
ATOM   3350 C  CD   . LYS   A 1 222 ? -9.422  -5.261  -19.947 1.00 29.79  ? 222 LYS   A CD   1 
ATOM   3351 C  CE   . LYS   A 1 222 ? -8.134  -4.428  -20.188 1.00 32.63  ? 222 LYS   A CE   1 
ATOM   3352 N  NZ   . LYS   A 1 222 ? -6.926  -5.148  -19.649 1.00 38.88  ? 222 LYS   A NZ   1 
ATOM   3353 H  H    . LYS   A 1 222 ? -12.495 -3.570  -17.545 1.00 27.84  ? 222 LYS   A H    1 
ATOM   3354 H  HA   . LYS   A 1 222 ? -12.699 -4.669  -19.929 1.00 28.66  ? 222 LYS   A HA   1 
ATOM   3355 H  HB2  . LYS   A 1 222 ? -11.520 -5.704  -17.579 1.00 31.03  ? 222 LYS   A HB2  1 
ATOM   3356 H  HB3  . LYS   A 1 222 ? -11.376 -6.396  -19.002 1.00 31.03  ? 222 LYS   A HB3  1 
ATOM   3357 H  HG2  . LYS   A 1 222 ? -10.495 -3.817  -19.039 1.00 32.18  ? 222 LYS   A HG2  1 
ATOM   3358 H  HG3  . LYS   A 1 222 ? -9.669  -4.717  -18.022 1.00 32.18  ? 222 LYS   A HG3  1 
ATOM   3359 H  HD2  . LYS   A 1 222 ? -9.159  -6.174  -19.748 1.00 35.75  ? 222 LYS   A HD2  1 
ATOM   3360 H  HD3  . LYS   A 1 222 ? -9.953  -5.239  -20.758 1.00 35.75  ? 222 LYS   A HD3  1 
ATOM   3361 H  HE2  . LYS   A 1 222 ? -8.011  -4.288  -21.140 1.00 39.16  ? 222 LYS   A HE2  1 
ATOM   3362 H  HE3  . LYS   A 1 222 ? -8.211  -3.574  -19.735 1.00 39.16  ? 222 LYS   A HE3  1 
ATOM   3363 H  HZ1  . LYS   A 1 222 ? -6.195  -4.661  -19.787 1.00 46.65  ? 222 LYS   A HZ1  1 
ATOM   3364 H  HZ2  . LYS   A 1 222 ? -7.020  -5.288  -18.775 1.00 46.65  ? 222 LYS   A HZ2  1 
ATOM   3365 H  HZ3  . LYS   A 1 222 ? -6.832  -5.933  -20.059 1.00 46.65  ? 222 LYS   A HZ3  1 
ATOM   3366 N  N    . GLU   A 1 223 ? -14.318 -6.559  -19.877 1.00 30.28  ? 223 GLU   A N    1 
ATOM   3367 C  CA   . GLU   A 1 223 ? -15.505 -7.422  -19.797 1.00 43.29  ? 223 GLU   A CA   1 
ATOM   3368 C  C    . GLU   A 1 223 ? -15.287 -8.552  -18.790 1.00 43.38  ? 223 GLU   A C    1 
ATOM   3369 O  O    . GLU   A 1 223 ? -16.200 -8.923  -18.038 1.00 44.64  ? 223 GLU   A O    1 
ATOM   3370 C  CB   . GLU   A 1 223 ? -15.862 -7.958  -21.192 1.00 44.73  ? 223 GLU   A CB   1 
ATOM   3371 C  CG   . GLU   A 1 223 ? -17.078 -8.924  -21.278 1.00 52.78  ? 223 GLU   A CG   1 
ATOM   3372 C  CD   . GLU   A 1 223 ? -18.348 -8.412  -20.583 1.00 58.79  ? 223 GLU   A CD   1 
ATOM   3373 O  OE1  . GLU   A 1 223 ? -18.854 -7.334  -20.970 1.00 63.48  ? 223 GLU   A OE1  1 
ATOM   3374 O  OE2  . GLU   A 1 223 ? -18.857 -9.108  -19.671 1.00 57.34  ? 223 GLU   A OE2  1 
ATOM   3375 H  H    . GLU   A 1 223 ? -13.933 -6.535  -20.646 1.00 36.34  ? 223 GLU   A H    1 
ATOM   3376 H  HA   . GLU   A 1 223 ? -16.264 -6.902  -19.491 1.00 51.95  ? 223 GLU   A HA   1 
ATOM   3377 H  HB2  . GLU   A 1 223 ? -16.061 -7.201  -21.764 1.00 53.68  ? 223 GLU   A HB2  1 
ATOM   3378 H  HB3  . GLU   A 1 223 ? -15.093 -8.440  -21.535 1.00 53.68  ? 223 GLU   A HB3  1 
ATOM   3379 H  HG2  . GLU   A 1 223 ? -17.293 -9.069  -22.212 1.00 63.34  ? 223 GLU   A HG2  1 
ATOM   3380 H  HG3  . GLU   A 1 223 ? -16.835 -9.765  -20.860 1.00 63.34  ? 223 GLU   A HG3  1 
ATOM   3381 N  N    . ASP   A 1 224 ? -14.069 -9.076  -18.720 1.00 35.49  ? 224 ASP   A N    1 
ATOM   3382 C  CA   . ASP   A 1 224 ? -13.771 -10.134 -17.761 1.00 43.91  ? 224 ASP   A CA   1 
ATOM   3383 C  C    . ASP   A 1 224 ? -13.822 -9.670  -16.309 1.00 42.95  ? 224 ASP   A C    1 
ATOM   3384 O  O    . ASP   A 1 224 ? -13.755 -10.519 -15.414 1.00 48.53  ? 224 ASP   A O    1 
ATOM   3385 C  CB   . ASP   A 1 224 ? -12.398 -10.749 -18.075 1.00 45.56  ? 224 ASP   A CB   1 
ATOM   3386 C  CG   . ASP   A 1 224 ? -11.253 -9.730  -17.953 1.00 54.25  ? 224 ASP   A CG   1 
ATOM   3387 O  OD1  . ASP   A 1 224 ? -11.065 -9.158  -16.850 1.00 59.46  ? 224 ASP   A OD1  1 
ATOM   3388 O  OD2  . ASP   A 1 224 ? -10.546 -9.498  -18.966 1.00 58.57  ? 224 ASP   A OD2  1 
ATOM   3389 H  H    . ASP   A 1 224 ? -13.404 -8.839  -19.211 1.00 42.59  ? 224 ASP   A H    1 
ATOM   3390 H  HA   . ASP   A 1 224 ? -14.439 -10.830 -17.857 1.00 52.69  ? 224 ASP   A HA   1 
ATOM   3391 H  HB2  . ASP   A 1 224 ? -12.225 -11.472 -17.451 1.00 54.68  ? 224 ASP   A HB2  1 
ATOM   3392 H  HB3  . ASP   A 1 224 ? -12.403 -11.089 -18.983 1.00 54.68  ? 224 ASP   A HB3  1 
ATOM   3393 N  N    . SER   A 1 225 ? -13.964 -8.367  -16.046 1.00 38.30  ? 225 SER   A N    1 
ATOM   3394 C  CA   . SER   A 1 225 ? -13.925 -7.889  -14.671 1.00 37.07  ? 225 SER   A CA   1 
ATOM   3395 C  C    . SER   A 1 225 ? -15.204 -8.214  -13.895 1.00 40.71  ? 225 SER   A C    1 
ATOM   3396 O  O    . SER   A 1 225 ? -15.176 -8.213  -12.664 1.00 38.09  ? 225 SER   A O    1 
ATOM   3397 C  CB   . SER   A 1 225 ? -13.703 -6.368  -14.622 1.00 39.25  ? 225 SER   A CB   1 
ATOM   3398 O  OG   . SER   A 1 225 ? -14.907 -5.642  -14.898 1.00 35.12  ? 225 SER   A OG   1 
ATOM   3399 H  H    . SER   A 1 225 ? -14.082 -7.754  -16.638 1.00 45.96  ? 225 SER   A H    1 
ATOM   3400 H  HA   . SER   A 1 225 ? -13.174 -8.324  -14.237 1.00 44.48  ? 225 SER   A HA   1 
ATOM   3401 H  HB2  . SER   A 1 225 ? -13.390 -6.127  -13.736 1.00 47.10  ? 225 SER   A HB2  1 
ATOM   3402 H  HB3  . SER   A 1 225 ? -13.037 -6.129  -15.286 1.00 47.10  ? 225 SER   A HB3  1 
ATOM   3403 H  HG   . SER   A 1 225 ? -15.200 -5.848  -15.658 1.00 42.15  ? 225 SER   A HG   1 
ATOM   3404 N  N    . GLY   A 1 226 ? -16.325 -8.436  -14.579 1.00 41.34  ? 226 GLY   A N    1 
ATOM   3405 C  CA   . GLY   A 1 226 ? -17.607 -8.619  -13.929 1.00 40.32  ? 226 GLY   A CA   1 
ATOM   3406 C  C    . GLY   A 1 226 ? -18.377 -7.360  -13.574 1.00 40.19  ? 226 GLY   A C    1 
ATOM   3407 O  O    . GLY   A 1 226 ? -19.492 -7.468  -13.044 1.00 43.37  ? 226 GLY   A O    1 
ATOM   3408 H  H    . GLY   A 1 226 ? -16.363 -8.484  -15.437 1.00 49.61  ? 226 GLY   A H    1 
ATOM   3409 H  HA2  . GLY   A 1 226 ? -18.172 -9.147  -14.515 1.00 48.38  ? 226 GLY   A HA2  1 
ATOM   3410 H  HA3  . GLY   A 1 226 ? -17.462 -9.110  -13.105 1.00 48.38  ? 226 GLY   A HA3  1 
ATOM   3411 N  N    . TYR   A 1 227 ? -17.827 -6.173  -13.829 1.00 38.09  ? 227 TYR   A N    1 
ATOM   3412 C  CA   . TYR   A 1 227 ? -18.500 -4.903  -13.550 1.00 43.37  ? 227 TYR   A CA   1 
ATOM   3413 C  C    . TYR   A 1 227 ? -18.876 -4.239  -14.861 1.00 28.12  ? 227 TYR   A C    1 
ATOM   3414 O  O    . TYR   A 1 227 ? -18.020 -4.061  -15.732 1.00 33.92  ? 227 TYR   A O    1 
ATOM   3415 C  CB   . TYR   A 1 227 ? -17.608 -3.968  -12.726 1.00 41.92  ? 227 TYR   A CB   1 
ATOM   3416 C  CG   . TYR   A 1 227 ? -17.127 -4.645  -11.469 1.00 41.17  ? 227 TYR   A CG   1 
ATOM   3417 C  CD1  . TYR   A 1 227 ? -17.985 -4.798  -10.388 1.00 42.87  ? 227 TYR   A CD1  1 
ATOM   3418 C  CD2  . TYR   A 1 227 ? -15.840 -5.168  -11.374 1.00 49.56  ? 227 TYR   A CD2  1 
ATOM   3419 C  CE1  . TYR   A 1 227 ? -17.576 -5.439  -9.229  1.00 45.57  ? 227 TYR   A CE1  1 
ATOM   3420 C  CE2  . TYR   A 1 227 ? -15.416 -5.813  -10.220 1.00 51.19  ? 227 TYR   A CE2  1 
ATOM   3421 C  CZ   . TYR   A 1 227 ? -16.292 -5.944  -9.150  1.00 47.74  ? 227 TYR   A CZ   1 
ATOM   3422 O  OH   . TYR   A 1 227 ? -15.902 -6.582  -7.991  1.00 54.20  ? 227 TYR   A OH   1 
ATOM   3423 H  H    . TYR   A 1 227 ? -17.044 -6.075  -14.172 1.00 45.71  ? 227 TYR   A H    1 
ATOM   3424 H  HA   . TYR   A 1 227 ? -19.310 -5.083  -13.047 1.00 52.05  ? 227 TYR   A HA   1 
ATOM   3425 H  HB2  . TYR   A 1 227 ? -16.835 -3.713  -13.253 1.00 50.31  ? 227 TYR   A HB2  1 
ATOM   3426 H  HB3  . TYR   A 1 227 ? -18.114 -3.179  -12.476 1.00 50.31  ? 227 TYR   A HB3  1 
ATOM   3427 H  HD1  . TYR   A 1 227 ? -18.851 -4.465  -10.442 1.00 51.44  ? 227 TYR   A HD1  1 
ATOM   3428 H  HD2  . TYR   A 1 227 ? -15.257 -5.084  -12.093 1.00 59.48  ? 227 TYR   A HD2  1 
ATOM   3429 H  HE1  . TYR   A 1 227 ? -18.160 -5.529  -8.512  1.00 54.69  ? 227 TYR   A HE1  1 
ATOM   3430 H  HE2  . TYR   A 1 227 ? -14.553 -6.155  -10.165 1.00 61.43  ? 227 TYR   A HE2  1 
ATOM   3431 H  HH   . TYR   A 1 227 ? -15.113 -6.861  -8.069  1.00 65.04  ? 227 TYR   A HH   1 
ATOM   3432 N  N    . ASP   A 1 228 ? -20.159 -3.910  -15.025 1.00 24.19  ? 228 ASP   A N    1 
ATOM   3433 C  CA   . ASP   A 1 228 ? -20.551 -3.179  -16.227 1.00 24.97  ? 228 ASP   A CA   1 
ATOM   3434 C  C    . ASP   A 1 228 ? -19.977 -1.774  -16.235 1.00 24.94  ? 228 ASP   A C    1 
ATOM   3435 O  O    . ASP   A 1 228 ? -19.696 -1.221  -17.289 1.00 23.49  ? 228 ASP   A O    1 
ATOM   3436 C  CB   . ASP   A 1 228 ? -22.070 -3.099  -16.370 1.00 29.10  ? 228 ASP   A CB   1 
ATOM   3437 C  CG   . ASP   A 1 228 ? -22.728 -4.461  -16.405 1.00 37.24  ? 228 ASP   A CG   1 
ATOM   3438 O  OD1  . ASP   A 1 228 ? -22.008 -5.466  -16.592 1.00 43.47  ? 228 ASP   A OD1  1 
ATOM   3439 O  OD2  . ASP   A 1 228 ? -23.959 -4.541  -16.241 1.00 43.83  ? 228 ASP   A OD2  1 
ATOM   3440 H  H    . ASP   A 1 228 ? -20.796 -4.092  -14.477 1.00 29.02  ? 228 ASP   A H    1 
ATOM   3441 H  HA   . ASP   A 1 228 ? -20.205 -3.674  -16.985 1.00 29.97  ? 228 ASP   A HA   1 
ATOM   3442 H  HB2  . ASP   A 1 228 ? -22.433 -2.610  -15.615 1.00 34.92  ? 228 ASP   A HB2  1 
ATOM   3443 H  HB3  . ASP   A 1 228 ? -22.286 -2.640  -17.197 1.00 34.92  ? 228 ASP   A HB3  1 
ATOM   3444 N  N    . ALA   A 1 229 ? -19.892 -1.141  -15.074 1.00 21.65  ? 229 ALA   A N    1 
ATOM   3445 C  CA   . ALA   A 1 229 ? -19.442 0.242   -14.969 1.00 17.95  ? 229 ALA   A CA   1 
ATOM   3446 C  C    . ALA   A 1 229 ? -18.795 0.412   -13.604 1.00 17.14  ? 229 ALA   A C    1 
ATOM   3447 O  O    . ALA   A 1 229 ? -18.914 -0.460  -12.727 1.00 19.21  ? 229 ALA   A O    1 
ATOM   3448 C  CB   . ALA   A 1 229 ? -20.607 1.215   -15.135 1.00 19.59  ? 229 ALA   A CB   1 
ATOM   3449 H  H    . ALA   A 1 229 ? -20.094 -1.496  -14.317 1.00 25.97  ? 229 ALA   A H    1 
ATOM   3450 H  HA   . ALA   A 1 229 ? -18.787 0.432   -15.659 1.00 21.54  ? 229 ALA   A HA   1 
ATOM   3451 H  HB1  . ALA   A 1 229 ? -20.278 2.122   -15.033 1.00 23.50  ? 229 ALA   A HB1  1 
ATOM   3452 H  HB2  . ALA   A 1 229 ? -20.991 1.100   -16.018 1.00 23.50  ? 229 ALA   A HB2  1 
ATOM   3453 H  HB3  . ALA   A 1 229 ? -21.274 1.027   -14.456 1.00 23.50  ? 229 ALA   A HB3  1 
ATOM   3454 N  N    . LEU   A 1 230 ? -18.112 1.531   -13.432 1.00 16.82  ? 230 LEU   A N    1 
ATOM   3455 C  CA   . LEU   A 1 230 ? -17.570 1.888   -12.122 1.00 17.39  ? 230 LEU   A CA   1 
ATOM   3456 C  C    . LEU   A 1 230 ? -18.642 2.485   -11.230 1.00 16.08  ? 230 LEU   A C    1 
ATOM   3457 O  O    . LEU   A 1 230 ? -18.750 2.099   -10.063 1.00 17.39  ? 230 LEU   A O    1 
ATOM   3458 C  CB   . LEU   A 1 230 ? -16.435 2.886   -12.304 1.00 18.57  ? 230 LEU   A CB   1 
ATOM   3459 C  CG   . LEU   A 1 230 ? -15.688 3.226   -11.029 1.00 24.90  ? 230 LEU   A CG   1 
ATOM   3460 C  CD1  . LEU   A 1 230 ? -14.992 2.012   -10.401 1.00 30.97  ? 230 LEU   A CD1  1 
ATOM   3461 C  CD2  . LEU   A 1 230 ? -14.677 4.332   -11.326 1.00 26.89  ? 230 LEU   A CD2  1 
ATOM   3462 H  H    . LEU   A 1 230 ? -17.945 2.104   -14.052 1.00 20.18  ? 230 LEU   A H    1 
ATOM   3463 H  HA   . LEU   A 1 230 ? -17.224 1.090   -11.691 1.00 20.86  ? 230 LEU   A HA   1 
ATOM   3464 H  HB2  . LEU   A 1 230 ? -15.794 2.514   -12.930 1.00 22.28  ? 230 LEU   A HB2  1 
ATOM   3465 H  HB3  . LEU   A 1 230 ? -16.803 3.711   -12.658 1.00 22.28  ? 230 LEU   A HB3  1 
ATOM   3466 H  HG   . LEU   A 1 230 ? -16.330 3.531   -10.369 1.00 29.88  ? 230 LEU   A HG   1 
ATOM   3467 H  HD11 . LEU   A 1 230 ? -14.500 2.301   -9.616  1.00 37.17  ? 230 LEU   A HD11 1 
ATOM   3468 H  HD12 . LEU   A 1 230 ? -15.664 1.359   -10.148 1.00 37.17  ? 230 LEU   A HD12 1 
ATOM   3469 H  HD13 . LEU   A 1 230 ? -14.383 1.626   -11.050 1.00 37.17  ? 230 LEU   A HD13 1 
ATOM   3470 H  HD21 . LEU   A 1 230 ? -14.188 4.539   -10.514 1.00 32.27  ? 230 LEU   A HD21 1 
ATOM   3471 H  HD22 . LEU   A 1 230 ? -14.065 4.024   -12.012 1.00 32.27  ? 230 LEU   A HD22 1 
ATOM   3472 H  HD23 . LEU   A 1 230 ? -15.152 5.119   -11.636 1.00 32.27  ? 230 LEU   A HD23 1 
ATOM   3473 N  N    . ARG   A 1 231 ? -19.437 3.412   -11.741 1.00 14.53  ? 231 ARG   A N    1 
ATOM   3474 C  CA   . ARG   A 1 231 ? -20.549 4.011   -10.997 1.00 14.13  ? 231 ARG   A CA   1 
ATOM   3475 C  C    . ARG   A 1 231 ? -21.772 4.068   -11.882 1.00 13.27  ? 231 ARG   A C    1 
ATOM   3476 O  O    . ARG   A 1 231 ? -21.672 4.152   -13.125 1.00 13.09  ? 231 ARG   A O    1 
ATOM   3477 C  CB   . ARG   A 1 231 ? -20.240 5.427   -10.511 1.00 13.58  ? 231 ARG   A CB   1 
ATOM   3478 C  CG   . ARG   A 1 231 ? -19.252 5.499   -9.389  1.00 12.73  ? 231 ARG   A CG   1 
ATOM   3479 C  CD   . ARG   A 1 231 ? -18.985 6.927   -8.901  1.00 13.12  ? 231 ARG   A CD   1 
ATOM   3480 N  NE   . ARG   A 1 231 ? -18.176 7.701   -9.836  1.00 12.45  ? 231 ARG   A NE   1 
ATOM   3481 C  CZ   . ARG   A 1 231 ? -16.841 7.702   -9.853  1.00 13.67  ? 231 ARG   A CZ   1 
ATOM   3482 N  NH1  . ARG   A 1 231 ? -16.153 6.861   -9.146  1.00 15.04  ? 231 ARG   A NH1  1 
ATOM   3483 N  NH2  . ARG   A 1 231 ? -16.209 8.626   -10.555 1.00 13.57  ? 231 ARG   A NH2  1 
ATOM   3484 H  H    . ARG   A 1 231 ? -19.356 3.723   -12.539 1.00 17.43  ? 231 ARG   A H    1 
ATOM   3485 H  HA   . ARG   A 1 231 ? -20.729 3.454   -10.223 1.00 16.96  ? 231 ARG   A HA   1 
ATOM   3486 H  HB2  . ARG   A 1 231 ? -19.877 5.935   -11.253 1.00 16.30  ? 231 ARG   A HB2  1 
ATOM   3487 H  HB3  . ARG   A 1 231 ? -21.064 5.834   -10.201 1.00 16.30  ? 231 ARG   A HB3  1 
ATOM   3488 H  HG2  . ARG   A 1 231 ? -19.592 4.988   -8.638  1.00 15.27  ? 231 ARG   A HG2  1 
ATOM   3489 H  HG3  . ARG   A 1 231 ? -18.408 5.126   -9.689  1.00 15.27  ? 231 ARG   A HG3  1 
ATOM   3490 H  HD2  . ARG   A 1 231 ? -19.832 7.385   -8.786  1.00 15.75  ? 231 ARG   A HD2  1 
ATOM   3491 H  HD3  . ARG   A 1 231 ? -18.511 6.888   -8.055  1.00 15.75  ? 231 ARG   A HD3  1 
ATOM   3492 H  HE   . ARG   A 1 231 ? -18.586 8.188   -10.415 1.00 14.93  ? 231 ARG   A HE   1 
ATOM   3493 H  HH11 . ARG   A 1 231 ? -16.557 6.284   -8.652  1.00 18.04  ? 231 ARG   A HH11 1 
ATOM   3494 H  HH12 . ARG   A 1 231 ? -15.294 6.879   -9.171  1.00 18.04  ? 231 ARG   A HH12 1 
ATOM   3495 H  HH21 . ARG   A 1 231 ? -16.657 9.215   -10.993 1.00 16.28  ? 231 ARG   A HH21 1 
ATOM   3496 H  HH22 . ARG   A 1 231 ? -15.349 8.638   -10.574 1.00 16.28  ? 231 ARG   A HH22 1 
ATOM   3497 N  N    . TYR   A 1 232 ? -22.938 4.121   -11.238 1.00 14.50  ? 232 TYR   A N    1 
ATOM   3498 C  CA   . TYR   A 1 232 ? -24.254 4.152   -11.874 1.00 14.64  ? 232 TYR   A CA   1 
ATOM   3499 C  C    . TYR   A 1 232 ? -24.992 5.352   -11.318 1.00 16.26  ? 232 TYR   A C    1 
ATOM   3500 O  O    . TYR   A 1 232 ? -25.133 5.466   -10.111 1.00 18.90  ? 232 TYR   A O    1 
ATOM   3501 C  CB   . TYR   A 1 232 ? -25.047 2.907   -11.561 1.00 15.43  ? 232 TYR   A CB   1 
ATOM   3502 C  CG   . TYR   A 1 232 ? -24.327 1.622   -11.943 1.00 17.31  ? 232 TYR   A CG   1 
ATOM   3503 C  CD1  . TYR   A 1 232 ? -23.399 1.011   -11.075 1.00 18.20  ? 232 TYR   A CD1  1 
ATOM   3504 C  CD2  . TYR   A 1 232 ? -24.517 1.054   -13.182 1.00 19.54  ? 232 TYR   A CD2  1 
ATOM   3505 C  CE1  . TYR   A 1 232 ? -22.773 -0.163  -11.424 1.00 19.84  ? 232 TYR   A CE1  1 
ATOM   3506 C  CE2  . TYR   A 1 232 ? -23.847 -0.078  -13.530 1.00 22.52  ? 232 TYR   A CE2  1 
ATOM   3507 C  CZ   . TYR   A 1 232 ? -22.986 -0.664  -12.653 1.00 21.04  ? 232 TYR   A CZ   1 
ATOM   3508 O  OH   . TYR   A 1 232 ? -22.300 -1.820  -13.034 1.00 28.66  ? 232 TYR   A OH   1 
ATOM   3509 H  H    . TYR   A 1 232 ? -22.996 4.140   -10.380 1.00 17.40  ? 232 TYR   A H    1 
ATOM   3510 H  HA   . TYR   A 1 232 ? -24.150 4.227   -12.836 1.00 17.57  ? 232 TYR   A HA   1 
ATOM   3511 H  HB2  . TYR   A 1 232 ? -25.222 2.879   -10.608 1.00 18.51  ? 232 TYR   A HB2  1 
ATOM   3512 H  HB3  . TYR   A 1 232 ? -25.883 2.937   -12.052 1.00 18.51  ? 232 TYR   A HB3  1 
ATOM   3513 H  HD1  . TYR   A 1 232 ? -23.208 1.407   -10.256 1.00 21.84  ? 232 TYR   A HD1  1 
ATOM   3514 H  HD2  . TYR   A 1 232 ? -25.107 1.446   -13.784 1.00 23.44  ? 232 TYR   A HD2  1 
ATOM   3515 H  HE1  . TYR   A 1 232 ? -22.214 -0.600  -10.823 1.00 23.81  ? 232 TYR   A HE1  1 
ATOM   3516 H  HE2  . TYR   A 1 232 ? -23.977 -0.452  -14.372 1.00 27.02  ? 232 TYR   A HE2  1 
ATOM   3517 H  HH   . TYR   A 1 232 ? -22.617 -2.119  -13.752 1.00 34.40  ? 232 TYR   A HH   1 
ATOM   3518 N  N    . MET   A 1 233 ? -25.439 6.259   -12.128 1.00 13.63  ? 233 MET   A N    1 
ATOM   3519 C  CA   . MET   A 1 233 ? -26.089 7.459   -11.621 1.00 13.48  ? 233 MET   A CA   1 
ATOM   3520 C  C    . MET   A 1 233 ? -27.579 7.272   -11.431 1.00 15.14  ? 233 MET   A C    1 
ATOM   3521 O  O    . MET   A 1 233 ? -28.159 8.003   -10.603 1.00 16.14  ? 233 MET   A O    1 
ATOM   3522 C  CB   . MET   A 1 233 ? -25.803 8.601   -12.610 1.00 16.16  ? 233 MET   A CB   1 
ATOM   3523 C  CG   . MET   A 1 233 ? -24.305 8.878   -12.707 1.00 15.59  ? 233 MET   A CG   1 
ATOM   3524 S  SD   . MET   A 1 233 ? -23.911 10.309  -13.753 1.00 17.86  ? 233 MET   A SD   1 
ATOM   3525 C  CE   . MET   A 1 233 ? -24.085 11.672  -12.667 1.00 14.07  ? 233 MET   A CE   1 
ATOM   3526 H  H    . MET   A 1 233 ? -25.385 6.219   -12.986 1.00 16.35  ? 233 MET   A H    1 
ATOM   3527 H  HA   . MET   A 1 233 ? -25.724 7.712   -10.758 1.00 16.18  ? 233 MET   A HA   1 
ATOM   3528 H  HB2  . MET   A 1 233 ? -26.128 8.355   -13.490 1.00 19.39  ? 233 MET   A HB2  1 
ATOM   3529 H  HB3  . MET   A 1 233 ? -26.246 9.409   -12.307 1.00 19.39  ? 233 MET   A HB3  1 
ATOM   3530 H  HG2  . MET   A 1 233 ? -23.959 9.053   -11.818 1.00 18.71  ? 233 MET   A HG2  1 
ATOM   3531 H  HG3  . MET   A 1 233 ? -23.866 8.101   -13.087 1.00 18.71  ? 233 MET   A HG3  1 
ATOM   3532 H  HE1  . MET   A 1 233 ? -23.901 12.490  -13.155 1.00 16.88  ? 233 MET   A HE1  1 
ATOM   3533 H  HE2  . MET   A 1 233 ? -24.992 11.689  -12.324 1.00 16.88  ? 233 MET   A HE2  1 
ATOM   3534 H  HE3  . MET   A 1 233 ? -23.456 11.575  -11.935 1.00 16.88  ? 233 MET   A HE3  1 
ATOM   3535 N  N    . ASP   A 1 234 ? -28.213 6.309   -12.105 1.00 15.09  ? 234 ASP   A N    1 
ATOM   3536 C  CA   . ASP   A 1 234 ? -29.632 6.014   -11.889 1.00 16.18  ? 234 ASP   A CA   1 
ATOM   3537 C  C    . ASP   A 1 234 ? -29.910 5.439   -10.508 1.00 17.71  ? 234 ASP   A C    1 
ATOM   3538 O  O    . ASP   A 1 234 ? -30.980 5.670   -9.938  1.00 19.68  ? 234 ASP   A O    1 
ATOM   3539 C  CB   . ASP   A 1 234 ? -30.201 5.154   -13.017 1.00 18.46  ? 234 ASP   A CB   1 
ATOM   3540 C  CG   . ASP   A 1 234 ? -29.654 3.754   -12.998 1.00 22.08  ? 234 ASP   A CG   1 
ATOM   3541 O  OD1  . ASP   A 1 234 ? -28.412 3.635   -12.890 1.00 24.30  ? 234 ASP   A OD1  1 
ATOM   3542 O  OD2  . ASP   A 1 234 ? -30.418 2.784   -13.094 1.00 35.96  ? 234 ASP   A OD2  1 
ATOM   3543 H  H    . ASP   A 1 234 ? -27.843 5.807   -12.697 1.00 18.11  ? 234 ASP   A H    1 
ATOM   3544 H  HA   . ASP   A 1 234 ? -30.122 6.850   -11.930 1.00 19.41  ? 234 ASP   A HA   1 
ATOM   3545 H  HB2  . ASP   A 1 234 ? -31.165 5.103   -12.922 1.00 22.16  ? 234 ASP   A HB2  1 
ATOM   3546 H  HB3  . ASP   A 1 234 ? -29.973 5.556   -13.870 1.00 22.16  ? 234 ASP   A HB3  1 
ATOM   3547 N  N    . LYS   A 1 235 ? -28.964 4.653   -9.956  1.00 16.73  ? 235 LYS   A N    1 
ATOM   3548 C  CA   . LYS   A 1 235 ? -29.112 3.915   -8.698  1.00 15.90  ? 235 LYS   A CA   1 
ATOM   3549 C  C    . LYS   A 1 235 ? -27.700 3.649   -8.233  1.00 14.53  ? 235 LYS   A C    1 
ATOM   3550 O  O    . LYS   A 1 235 ? -27.139 2.591   -8.514  1.00 15.47  ? 235 LYS   A O    1 
ATOM   3551 C  CB   . LYS   A 1 235 ? -29.919 2.632   -8.865  1.00 19.65  ? 235 LYS   A CB   1 
ATOM   3552 C  CG   . LYS   A 1 235 ? -30.247 2.006   -7.508  1.00 24.46  ? 235 LYS   A CG   1 
ATOM   3553 C  CD   . LYS   A 1 235 ? -31.022 0.692   -7.655  1.00 26.92  ? 235 LYS   A CD   1 
ATOM   3554 C  CE   . LYS   A 1 235 ? -31.204 -0.058  -6.353  1.00 37.34  ? 235 LYS   A CE   1 
ATOM   3555 N  NZ   . LYS   A 1 235 ? -32.651 -0.090  -5.945  1.00 52.72  ? 235 LYS   A NZ   1 
ATOM   3556 H  H    . LYS   A 1 235 ? -28.191 4.529   -10.314 1.00 20.07  ? 235 LYS   A H    1 
ATOM   3557 H  HA   . LYS   A 1 235 ? -29.610 4.420   -8.037  1.00 19.08  ? 235 LYS   A HA   1 
ATOM   3558 H  HB2  . LYS   A 1 235 ? -30.752 2.832   -9.321  1.00 23.59  ? 235 LYS   A HB2  1 
ATOM   3559 H  HB3  . LYS   A 1 235 ? -29.404 1.993   -9.382  1.00 23.59  ? 235 LYS   A HB3  1 
ATOM   3560 H  HG2  . LYS   A 1 235 ? -29.421 1.820   -7.034  1.00 29.35  ? 235 LYS   A HG2  1 
ATOM   3561 H  HG3  . LYS   A 1 235 ? -30.792 2.623   -6.995  1.00 29.35  ? 235 LYS   A HG3  1 
ATOM   3562 H  HD2  . LYS   A 1 235 ? -31.903 0.887   -8.009  1.00 32.31  ? 235 LYS   A HD2  1 
ATOM   3563 H  HD3  . LYS   A 1 235 ? -30.540 0.112   -8.265  1.00 32.31  ? 235 LYS   A HD3  1 
ATOM   3564 H  HE2  . LYS   A 1 235 ? -30.895 -0.972  -6.461  1.00 44.81  ? 235 LYS   A HE2  1 
ATOM   3565 H  HE3  . LYS   A 1 235 ? -30.697 0.382   -5.652  1.00 44.81  ? 235 LYS   A HE3  1 
ATOM   3566 H  HZ1  . LYS   A 1 235 ? -32.738 -0.514  -5.167  1.00 63.26  ? 235 LYS   A HZ1  1 
ATOM   3567 H  HZ2  . LYS   A 1 235 ? -32.961 0.739   -5.858  1.00 63.26  ? 235 LYS   A HZ2  1 
ATOM   3568 H  HZ3  . LYS   A 1 235 ? -33.131 -0.515  -6.562  1.00 63.26  ? 235 LYS   A HZ3  1 
ATOM   3569 N  N    . PRO   A 1 236 ? -27.081 4.624   -7.562  1.00 13.35  ? 236 PRO   A N    1 
ATOM   3570 C  CA   . PRO   A 1 236 ? -25.663 4.485   -7.187  1.00 12.86  ? 236 PRO   A CA   1 
ATOM   3571 C  C    . PRO   A 1 236 ? -25.346 3.232   -6.437  1.00 13.96  ? 236 PRO   A C    1 
ATOM   3572 O  O    . PRO   A 1 236 ? -24.265 2.663   -6.660  1.00 14.32  ? 236 PRO   A O    1 
ATOM   3573 C  CB   . PRO   A 1 236 ? -25.412 5.760   -6.382  1.00 13.37  ? 236 PRO   A CB   1 
ATOM   3574 C  CG   . PRO   A 1 236 ? -26.312 6.795   -7.069  1.00 14.78  ? 236 PRO   A CG   1 
ATOM   3575 C  CD   . PRO   A 1 236 ? -27.563 6.013   -7.357  1.00 15.08  ? 236 PRO   A CD   1 
ATOM   3576 H  HA   . PRO   A 1 236 ? -25.103 4.500   -7.979  1.00 15.43  ? 236 PRO   A HA   1 
ATOM   3577 H  HB2  . PRO   A 1 236 ? -25.669 5.630   -5.455  1.00 16.05  ? 236 PRO   A HB2  1 
ATOM   3578 H  HB3  . PRO   A 1 236 ? -24.478 6.014   -6.435  1.00 16.05  ? 236 PRO   A HB3  1 
ATOM   3579 H  HG2  . PRO   A 1 236 ? -26.489 7.540   -6.474  1.00 17.73  ? 236 PRO   A HG2  1 
ATOM   3580 H  HG3  . PRO   A 1 236 ? -25.898 7.115   -7.886  1.00 17.73  ? 236 PRO   A HG3  1 
ATOM   3581 H  HD2  . PRO   A 1 236 ? -28.174 6.056   -6.605  1.00 18.09  ? 236 PRO   A HD2  1 
ATOM   3582 H  HD3  . PRO   A 1 236 ? -27.998 6.346   -8.158  1.00 18.09  ? 236 PRO   A HD3  1 
ATOM   3583 N  N    . SER   A 1 237 ? -26.256 2.768   -5.590  1.00 15.14  ? 237 SER   A N    1 
ATOM   3584 C  CA   . SER   A 1 237 ? -26.027 1.585   -4.724  1.00 15.34  ? 237 SER   A CA   1 
ATOM   3585 C  C    . SER   A 1 237 ? -25.832 0.314   -5.558  1.00 16.60  ? 237 SER   A C    1 
ATOM   3586 O  O    . SER   A 1 237 ? -25.426 -0.682  -4.994  1.00 18.49  ? 237 SER   A O    1 
ATOM   3587 C  CB   . SER   A 1 237 ? -27.178 1.455   -3.751  1.00 17.52  ? 237 SER   A CB   1 
ATOM   3588 O  OG   . SER   A 1 237 ? -28.397 1.219   -4.432  1.00 19.21  ? 237 SER   A OG   1 
ATOM   3589 H  H    . SER   A 1 237 ? -27.074 3.141   -5.516  1.00 18.17  ? 237 SER   A H    1 
ATOM   3590 H  HA   . SER   A 1 237 ? -25.199 1.740   -4.207  1.00 18.40  ? 237 SER   A HA   1 
ATOM   3591 H  HB2  . SER   A 1 237 ? -27.000 0.718   -3.138  1.00 21.02  ? 237 SER   A HB2  1 
ATOM   3592 H  HB3  . SER   A 1 237 ? -27.251 2.276   -3.229  1.00 21.02  ? 237 SER   A HB3  1 
ATOM   3593 H  HG   . SER   A 1 237 ? -29.024 1.188   -3.866  1.00 23.05  ? 237 SER   A HG   1 
ATOM   3594 N  N    . ARG   A 1 238 ? -26.106 0.380   -6.852  1.00 16.46  ? 238 ARG   A N    1 
ATOM   3595 C  CA   A ARG   A 1 238 ? -25.805 -0.830  -7.693  0.57 18.12  ? 238 ARG   A CA   1 
ATOM   3596 C  CA   B ARG   A 1 238 ? -25.808 -0.831  -7.691  0.43 18.21  ? 238 ARG   A CA   1 
ATOM   3597 C  C    . ARG   A 1 238 ? -24.309 -1.256  -7.698  1.00 17.09  ? 238 ARG   A C    1 
ATOM   3598 O  O    . ARG   A 1 238 ? -23.902 -2.410  -7.970  1.00 21.10  ? 238 ARG   A O    1 
ATOM   3599 C  CB   A ARG   A 1 238 ? -26.198 -0.520  -9.137  0.57 18.09  ? 238 ARG   A CB   1 
ATOM   3600 C  CB   B ARG   A 1 238 ? -26.220 -0.538  -9.133  0.43 18.21  ? 238 ARG   A CB   1 
ATOM   3601 C  CG   A ARG   A 1 238 ? -27.699 -0.496  -9.374  0.57 20.95  ? 238 ARG   A CG   1 
ATOM   3602 C  CG   B ARG   A 1 238 ? -26.468 -1.820  -9.912  0.43 21.14  ? 238 ARG   A CG   1 
ATOM   3603 C  CD   A ARG   A 1 238 ? -28.021 0.012   -10.762 0.57 23.52  ? 238 ARG   A CD   1 
ATOM   3604 C  CD   B ARG   A 1 238 ? -26.376 -1.612  -11.402 0.43 23.71  ? 238 ARG   A CD   1 
ATOM   3605 N  NE   A ARG   A 1 238 ? -27.475 -0.856  -11.811 0.57 30.27  ? 238 ARG   A NE   1 
ATOM   3606 N  NE   B ARG   A 1 238 ? -27.513 -0.852  -11.924 0.43 30.21  ? 238 ARG   A NE   1 
ATOM   3607 C  CZ   A ARG   A 1 238 ? -27.540 -0.591  -13.108 0.57 31.74  ? 238 ARG   A CZ   1 
ATOM   3608 C  CZ   B ARG   A 1 238 ? -27.632 -0.486  -13.189 0.43 31.48  ? 238 ARG   A CZ   1 
ATOM   3609 N  NH1  A ARG   A 1 238 ? -28.083 0.535   -13.533 0.57 32.59  ? 238 ARG   A NH1  1 
ATOM   3610 N  NH1  B ARG   A 1 238 ? -27.113 -1.228  -14.150 0.43 29.89  ? 238 ARG   A NH1  1 
ATOM   3611 N  NH2  A ARG   A 1 238 ? -27.035 -1.442  -13.982 0.57 29.78  ? 238 ARG   A NH2  1 
ATOM   3612 N  NH2  B ARG   A 1 238 ? -28.243 0.644   -13.485 0.43 32.45  ? 238 ARG   A NH2  1 
ATOM   3613 H  H    . ARG   A 1 238 ? -26.560 1.155   -7.072  1.00 19.75  ? 238 ARG   A H    1 
ATOM   3614 H  HA   . ARG   A 1 238 ? -26.443 -1.601  -7.408  1.00 21.85  ? 238 ARG   A HA   1 
ATOM   3615 H  HB2  A ARG   A 1 238 ? -25.825 0.353   -9.384  0.57 21.70  ? 238 ARG   A HB2  1 
ATOM   3616 H  HB2  B ARG   A 1 238 ? -27.038 0.002   -9.133  0.43 21.85  ? 238 ARG   A HB2  1 
ATOM   3617 H  HB3  A ARG   A 1 238 ? -25.795 -1.194  -9.725  0.57 21.70  ? 238 ARG   A HB3  1 
ATOM   3618 H  HB3  B ARG   A 1 238 ? -25.514 -0.023  -9.575  0.43 21.85  ? 238 ARG   A HB3  1 
ATOM   3619 H  HG2  A ARG   A 1 238 ? -28.060 -1.403  -9.272  0.57 25.14  ? 238 ARG   A HG2  1 
ATOM   3620 H  HG2  B ARG   A 1 238 ? -25.813 -2.497  -9.645  0.43 25.37  ? 238 ARG   A HG2  1 
ATOM   3621 H  HG3  A ARG   A 1 238 ? -28.127 0.086   -8.710  0.57 25.14  ? 238 ARG   A HG3  1 
ATOM   3622 H  HG3  B ARG   A 1 238 ? -27.362 -2.162  -9.693  0.43 25.37  ? 238 ARG   A HG3  1 
ATOM   3623 H  HD2  A ARG   A 1 238 ? -28.992 0.073   -10.865 0.57 28.23  ? 238 ARG   A HD2  1 
ATOM   3624 H  HD2  B ARG   A 1 238 ? -25.550 -1.134  -11.603 0.43 28.46  ? 238 ARG   A HD2  1 
ATOM   3625 H  HD3  A ARG   A 1 238 ? -27.649 0.913   -10.863 0.57 28.23  ? 238 ARG   A HD3  1 
ATOM   3626 H  HD3  B ARG   A 1 238 ? -26.338 -2.483  -11.846 0.43 28.46  ? 238 ARG   A HD3  1 
ATOM   3627 H  HE   A ARG   A 1 238 ? -27.083 -1.594  -11.569 0.57 36.33  ? 238 ARG   A HE   1 
ATOM   3628 H  HE   B ARG   A 1 238 ? -28.145 -0.624  -11.371 0.43 36.25  ? 238 ARG   A HE   1 
ATOM   3629 H  HH11 A ARG   A 1 238 ? -28.016 1.274   -13.053 0.57 39.11  ? 238 ARG   A HH11 1 
ATOM   3630 H  HH11 B ARG   A 1 238 ? -26.987 -0.874  -14.950 0.43 35.87  ? 238 ARG   A HH11 1 
ATOM   3631 H  HH12 A ARG   A 1 238 ? -28.494 0.551   -14.315 0.57 39.11  ? 238 ARG   A HH12 1 
ATOM   3632 H  HH12 B ARG   A 1 238 ? -26.886 -2.067  -13.993 0.43 35.87  ? 238 ARG   A HH12 1 
ATOM   3633 H  HH21 A ARG   A 1 238 ? -27.019 -1.230  -14.840 0.57 35.73  ? 238 ARG   A HH21 1 
ATOM   3634 H  HH21 B ARG   A 1 238 ? -28.395 0.854   -14.330 0.43 38.94  ? 238 ARG   A HH21 1 
ATOM   3635 H  HH22 A ARG   A 1 238 ? -26.709 -2.214  -13.703 0.57 35.73  ? 238 ARG   A HH22 1 
ATOM   3636 H  HH22 B ARG   A 1 238 ? -28.497 1.185   -12.834 0.43 38.94  ? 238 ARG   A HH22 1 
ATOM   3637 N  N    . ASP   A 1 239 ? -23.424 -0.321  -7.337  1.00 17.22  ? 239 ASP   A N    1 
ATOM   3638 C  CA   . ASP   A 1 239 ? -21.963 -0.619  -7.298  1.00 19.39  ? 239 ASP   A CA   1 
ATOM   3639 C  C    . ASP   A 1 239 ? -21.553 -1.219  -5.946  1.00 21.09  ? 239 ASP   A C    1 
ATOM   3640 O  O    . ASP   A 1 239 ? -20.367 -1.489  -5.789  1.00 21.15  ? 239 ASP   A O    1 
ATOM   3641 C  CB   . ASP   A 1 239 ? -21.124 0.610   -7.631  1.00 17.76  ? 239 ASP   A CB   1 
ATOM   3642 C  CG   . ASP   A 1 239 ? -21.136 1.699   -6.585  1.00 15.80  ? 239 ASP   A CG   1 
ATOM   3643 O  OD1  . ASP   A 1 239 ? -21.857 1.513   -5.632  1.00 19.14  ? 239 ASP   A OD1  1 
ATOM   3644 O  OD2  . ASP   A 1 239 ? -20.450 2.707   -6.770  1.00 18.46  ? 239 ASP   A OD2  1 
ATOM   3645 H  H    . ASP   A 1 239 ? -23.680 0.509   -7.093  1.00 20.67  ? 239 ASP   A H    1 
ATOM   3646 H  HA   . ASP   A 1 239 ? -21.765 -1.278  -8.000  1.00 23.27  ? 239 ASP   A HA   1 
ATOM   3647 H  HB2  . ASP   A 1 239 ? -20.194 0.335   -7.775  1.00 21.31  ? 239 ASP   A HB2  1 
ATOM   3648 H  HB3  . ASP   A 1 239 ? -21.457 0.993   -8.470  1.00 21.31  ? 239 ASP   A HB3  1 
ATOM   3649 N  N    . GLY   A 1 240 ? -22.476 -1.401  -4.992  1.00 17.35  ? 240 GLY   A N    1 
ATOM   3650 C  CA   . GLY   A 1 240 ? -22.158 -2.003  -3.726  1.00 19.94  ? 240 GLY   A CA   1 
ATOM   3651 C  C    . GLY   A 1 240 ? -21.510 -1.118  -2.689  1.00 19.96  ? 240 GLY   A C    1 
ATOM   3652 O  O    . GLY   A 1 240 ? -21.155 -1.659  -1.626  1.00 24.00  ? 240 GLY   A O    1 
ATOM   3653 H  H    . GLY   A 1 240 ? -23.308 -1.198  -5.071  1.00 20.82  ? 240 GLY   A H    1 
ATOM   3654 H  HA2  . GLY   A 1 240 ? -22.980 -2.343  -3.339  1.00 23.92  ? 240 GLY   A HA2  1 
ATOM   3655 H  HA3  . GLY   A 1 240 ? -21.554 -2.744  -3.888  1.00 23.92  ? 240 GLY   A HA3  1 
ATOM   3656 N  N    . MET   A 1 241 ? -21.290 0.157   -2.948  1.00 20.17  ? 241 MET   A N    1 
ATOM   3657 C  CA   . MET   A 1 241 ? -20.592 1.061   -2.024  1.00 21.83  ? 241 MET   A CA   1 
ATOM   3658 C  C    . MET   A 1 241 ? -21.190 2.451   -1.973  1.00 18.69  ? 241 MET   A C    1 
ATOM   3659 O  O    . MET   A 1 241 ? -21.197 3.073   -0.907  1.00 19.49  ? 241 MET   A O    1 
ATOM   3660 C  CB   . MET   A 1 241 ? -19.137 1.178   -2.480  1.00 29.38  ? 241 MET   A CB   1 
ATOM   3661 C  CG   . MET   A 1 241 ? -18.588 -0.147  -3.028  1.00 43.31  ? 241 MET   A CG   1 
ATOM   3662 S  SD   . MET   A 1 241 ? -16.793 -0.235  -3.097  1.00 85.72  ? 241 MET   A SD   1 
ATOM   3663 C  CE   . MET   A 1 241 ? -16.572 -1.958  -2.674  1.00 44.20  ? 241 MET   A CE   1 
ATOM   3664 H  H    . MET   A 1 241 ? -21.540 0.545   -3.673  1.00 24.21  ? 241 MET   A H    1 
ATOM   3665 H  HA   . MET   A 1 241 ? -20.615 0.696   -1.126  1.00 26.19  ? 241 MET   A HA   1 
ATOM   3666 H  HB2  . MET   A 1 241 ? -19.077 1.844   -3.183  1.00 35.25  ? 241 MET   A HB2  1 
ATOM   3667 H  HB3  . MET   A 1 241 ? -18.588 1.443   -1.725  1.00 35.25  ? 241 MET   A HB3  1 
ATOM   3668 H  HG2  . MET   A 1 241 ? -18.896 -0.869  -2.458  1.00 51.97  ? 241 MET   A HG2  1 
ATOM   3669 H  HG3  . MET   A 1 241 ? -18.923 -0.271  -3.930  1.00 51.97  ? 241 MET   A HG3  1 
ATOM   3670 H  HE1  . MET   A 1 241 ? -15.623 -2.152  -2.628  1.00 53.04  ? 241 MET   A HE1  1 
ATOM   3671 H  HE2  . MET   A 1 241 ? -16.987 -2.127  -1.814  1.00 53.04  ? 241 MET   A HE2  1 
ATOM   3672 H  HE3  . MET   A 1 241 ? -16.990 -2.506  -3.357  1.00 53.04  ? 241 MET   A HE3  1 
ATOM   3673 N  N    . SER   A 1 242 ? -21.744 2.960   -3.051  1.00 14.97  ? 242 SER   A N    1 
ATOM   3674 C  CA   . SER   A 1 242 ? -22.275 4.308   -3.122  1.00 13.29  ? 242 SER   A CA   1 
ATOM   3675 C  C    . SER   A 1 242 ? -23.657 4.362   -2.533  1.00 15.45  ? 242 SER   A C    1 
ATOM   3676 O  O    . SER   A 1 242 ? -24.381 3.374   -2.466  1.00 17.54  ? 242 SER   A O    1 
ATOM   3677 C  CB   . SER   A 1 242 ? -22.293 4.750   -4.563  1.00 15.11  ? 242 SER   A CB   1 
ATOM   3678 O  OG   . SER   A 1 242 ? -20.935 4.893   -5.057  1.00 15.46  ? 242 SER   A OG   1 
ATOM   3679 H  H    . SER   A 1 242 ? -21.830 2.529   -3.790  1.00 17.96  ? 242 SER   A H    1 
ATOM   3680 H  HA   . SER   A 1 242 ? -21.723 4.922   -2.613  1.00 15.95  ? 242 SER   A HA   1 
ATOM   3681 H  HB2  . SER   A 1 242 ? -22.758 4.086   -5.095  1.00 18.13  ? 242 SER   A HB2  1 
ATOM   3682 H  HB3  . SER   A 1 242 ? -22.747 5.605   -4.628  1.00 18.13  ? 242 SER   A HB3  1 
ATOM   3683 H  HG   . SER   A 1 242 ? -20.550 4.146   -5.058  1.00 18.55  ? 242 SER   A HG   1 
ATOM   3684 N  N    . ILE   A 1 243 ? -24.036 5.563   -2.122  1.00 15.14  ? 243 ILE   A N    1 
ATOM   3685 C  CA   . ILE   A 1 243 ? -25.329 5.798   -1.491  1.00 16.24  ? 243 ILE   A CA   1 
ATOM   3686 C  C    . ILE   A 1 243 ? -26.285 6.515   -2.424  1.00 13.33  ? 243 ILE   A C    1 
ATOM   3687 O  O    . ILE   A 1 243 ? -25.906 7.300   -3.294  1.00 14.58  ? 243 ILE   A O    1 
ATOM   3688 C  CB   . ILE   A 1 243 ? -25.182 6.551   -0.159  1.00 14.82  ? 243 ILE   A CB   1 
ATOM   3689 C  CG1  . ILE   A 1 243 ? -24.462 7.861   -0.329  1.00 15.27  ? 243 ILE   A CG1  1 
ATOM   3690 C  CG2  . ILE   A 1 243 ? -24.528 5.623   0.817   1.00 15.81  ? 243 ILE   A CG2  1 
ATOM   3691 C  CD1  . ILE   A 1 243 ? -24.546 8.765   0.910   1.00 16.40  ? 243 ILE   A CD1  1 
ATOM   3692 H  H    . ILE   A 1 243 ? -23.554 6.271   -2.198  1.00 18.17  ? 243 ILE   A H    1 
ATOM   3693 H  HA   . ILE   A 1 243 ? -25.728 4.931   -1.321  1.00 19.49  ? 243 ILE   A HA   1 
ATOM   3694 H  HB   . ILE   A 1 243 ? -26.053 6.804   0.186   1.00 17.79  ? 243 ILE   A HB   1 
ATOM   3695 H  HG12 . ILE   A 1 243 ? -23.525 7.683   -0.505  1.00 18.32  ? 243 ILE   A HG12 1 
ATOM   3696 H  HG13 . ILE   A 1 243 ? -24.855 8.340   -1.075  1.00 18.32  ? 243 ILE   A HG13 1 
ATOM   3697 H  HG21 . ILE   A 1 243 ? -24.482 6.056   1.684   1.00 18.98  ? 243 ILE   A HG21 1 
ATOM   3698 H  HG22 . ILE   A 1 243 ? -25.053 4.810   0.880   1.00 18.98  ? 243 ILE   A HG22 1 
ATOM   3699 H  HG23 . ILE   A 1 243 ? -23.633 5.415   0.504   1.00 18.98  ? 243 ILE   A HG23 1 
ATOM   3700 H  HD11 . ILE   A 1 243 ? -24.132 9.618   0.707   1.00 19.68  ? 243 ILE   A HD11 1 
ATOM   3701 H  HD12 . ILE   A 1 243 ? -25.479 8.897   1.141   1.00 19.68  ? 243 ILE   A HD12 1 
ATOM   3702 H  HD13 . ILE   A 1 243 ? -24.080 8.337   1.645   1.00 19.68  ? 243 ILE   A HD13 1 
ATOM   3703 N  N    . ASP   A 1 244 ? -27.571 6.295   -2.202  1.00 14.54  ? 244 ASP   A N    1 
ATOM   3704 C  CA   . ASP   A 1 244 ? -28.641 6.774   -3.088  1.00 17.19  ? 244 ASP   A CA   1 
ATOM   3705 C  C    . ASP   A 1 244 ? -29.336 8.012   -2.527  1.00 16.24  ? 244 ASP   A C    1 
ATOM   3706 O  O    . ASP   A 1 244 ? -30.033 8.710   -3.273  1.00 17.02  ? 244 ASP   A O    1 
ATOM   3707 C  CB   . ASP   A 1 244 ? -29.726 5.687   -3.279  1.00 18.27  ? 244 ASP   A CB   1 
ATOM   3708 C  CG   . ASP   A 1 244 ? -29.233 4.448   -3.995  1.00 17.68  ? 244 ASP   A CG   1 
ATOM   3709 O  OD1  . ASP   A 1 244 ? -28.204 4.533   -4.646  1.00 18.59  ? 244 ASP   A OD1  1 
ATOM   3710 O  OD2  . ASP   A 1 244 ? -29.885 3.376   -3.849  1.00 21.29  ? 244 ASP   A OD2  1 
ATOM   3711 H  H    . ASP   A 1 244 ? -27.868 5.857   -1.525  1.00 17.45  ? 244 ASP   A H    1 
ATOM   3712 H  HA   . ASP   A 1 244 ? -28.256 6.973   -3.956  1.00 20.63  ? 244 ASP   A HA   1 
ATOM   3713 H  HB2  . ASP   A 1 244 ? -30.050 5.414   -2.406  1.00 21.92  ? 244 ASP   A HB2  1 
ATOM   3714 H  HB3  . ASP   A 1 244 ? -30.453 6.061   -3.801  1.00 21.92  ? 244 ASP   A HB3  1 
ATOM   3715 N  N    . VAL   A 1 245 ? -29.197 8.266   -1.232  1.00 15.66  ? 245 VAL   A N    1 
ATOM   3716 C  CA   . VAL   A 1 245 ? -29.908 9.346   -0.551  1.00 17.27  ? 245 VAL   A CA   1 
ATOM   3717 C  C    . VAL   A 1 245 ? -28.988 9.922   0.513   1.00 16.10  ? 245 VAL   A C    1 
ATOM   3718 O  O    . VAL   A 1 245 ? -28.171 9.221   1.111   1.00 15.88  ? 245 VAL   A O    1 
ATOM   3719 C  CB   . VAL   A 1 245 ? -31.219 8.892   0.105   1.00 16.89  ? 245 VAL   A CB   1 
ATOM   3720 C  CG1  . VAL   A 1 245 ? -32.233 8.409   -0.939  1.00 21.69  ? 245 VAL   A CG1  1 
ATOM   3721 C  CG2  . VAL   A 1 245 ? -30.979 7.773   1.097   1.00 21.30  ? 245 VAL   A CG2  1 
ATOM   3722 H  H    . VAL   A 1 245 ? -28.682 7.816   -0.710  1.00 18.79  ? 245 VAL   A H    1 
ATOM   3723 H  HA   . VAL   A 1 245 ? -30.123 10.025  -1.209  1.00 20.73  ? 245 VAL   A HA   1 
ATOM   3724 H  HB   . VAL   A 1 245 ? -31.583 9.662   0.569   1.00 20.27  ? 245 VAL   A HB   1 
ATOM   3725 H  HG11 . VAL   A 1 245 ? -33.088 8.265   -0.505  1.00 26.02  ? 245 VAL   A HG11 1 
ATOM   3726 H  HG12 . VAL   A 1 245 ? -32.322 9.085   -1.629  1.00 26.02  ? 245 VAL   A HG12 1 
ATOM   3727 H  HG13 . VAL   A 1 245 ? -31.915 7.579   -1.328  1.00 26.02  ? 245 VAL   A HG13 1 
ATOM   3728 H  HG21 . VAL   A 1 245 ? -31.833 7.397   1.362   1.00 25.56  ? 245 VAL   A HG21 1 
ATOM   3729 H  HG22 . VAL   A 1 245 ? -30.433 7.090   0.677   1.00 25.56  ? 245 VAL   A HG22 1 
ATOM   3730 H  HG23 . VAL   A 1 245 ? -30.521 8.132   1.873   1.00 25.56  ? 245 VAL   A HG23 1 
ATOM   3731 N  N    . ALA   A 1 246 ? -29.236 11.202  0.846   1.00 16.49  ? 246 ALA   A N    1 
ATOM   3732 C  CA   . ALA   A 1 246 ? -28.397 11.863  1.832   1.00 16.79  ? 246 ALA   A CA   1 
ATOM   3733 C  C    . ALA   A 1 246 ? -28.543 11.281  3.214   1.00 20.88  ? 246 ALA   A C    1 
ATOM   3734 O  O    . ALA   A 1 246 ? -27.572 11.333  3.991   1.00 19.82  ? 246 ALA   A O    1 
ATOM   3735 C  CB   . ALA   A 1 246 ? -28.706 13.335  1.857   1.00 17.42  ? 246 ALA   A CB   1 
ATOM   3736 H  H    . ALA   A 1 246 ? -29.867 11.687  0.520   1.00 19.78  ? 246 ALA   A H    1 
ATOM   3737 H  HA   . ALA   A 1 246 ? -27.470 11.751  1.571   1.00 20.14  ? 246 ALA   A HA   1 
ATOM   3738 H  HB1  . ALA   A 1 246 ? -28.129 13.768  2.506   1.00 20.90  ? 246 ALA   A HB1  1 
ATOM   3739 H  HB2  . ALA   A 1 246 ? -28.549 13.706  0.975   1.00 20.90  ? 246 ALA   A HB2  1 
ATOM   3740 H  HB3  . ALA   A 1 246 ? -29.635 13.458  2.108   1.00 20.90  ? 246 ALA   A HB3  1 
ATOM   3741 N  N    . ASP   A 1 247 ? -29.655 10.621  3.510   1.00 17.18  ? 247 ASP   A N    1 
ATOM   3742 C  CA   . ASP   A 1 247 ? -29.855 10.029  4.827   1.00 20.21  ? 247 ASP   A CA   1 
ATOM   3743 C  C    . ASP   A 1 247 ? -28.926 8.856   5.088   1.00 21.00  ? 247 ASP   A C    1 
ATOM   3744 O  O    . ASP   A 1 247 ? -28.786 8.431   6.236   1.00 22.48  ? 247 ASP   A O    1 
ATOM   3745 C  CB   . ASP   A 1 247 ? -31.314 9.597   4.996   1.00 23.34  ? 247 ASP   A CB   1 
ATOM   3746 C  CG   . ASP   A 1 247 ? -32.259 10.770  5.296   1.00 33.44  ? 247 ASP   A CG   1 
ATOM   3747 O  OD1  . ASP   A 1 247 ? -31.807 11.937  5.421   1.00 36.54  ? 247 ASP   A OD1  1 
ATOM   3748 O  OD2  . ASP   A 1 247 ? -33.479 10.515  5.315   1.00 40.23  ? 247 ASP   A OD2  1 
ATOM   3749 H  H    . ASP   A 1 247 ? -30.311 10.501  2.966   1.00 20.62  ? 247 ASP   A H    1 
ATOM   3750 H  HA   . ASP   A 1 247 ? -29.673 10.702  5.502   1.00 24.25  ? 247 ASP   A HA   1 
ATOM   3751 H  HB2  . ASP   A 1 247 ? -31.614 9.175   4.176   1.00 28.01  ? 247 ASP   A HB2  1 
ATOM   3752 H  HB3  . ASP   A 1 247 ? -31.373 8.970   5.733   1.00 28.01  ? 247 ASP   A HB3  1 
ATOM   3753 N  N    . ASP   A 1 248 ? -28.264 8.312   4.066   1.00 17.37  ? 248 ASP   A N    1 
ATOM   3754 C  CA   . ASP   A 1 248 ? -27.299 7.234   4.231   1.00 19.47  ? 248 ASP   A CA   1 
ATOM   3755 C  C    . ASP   A 1 248 ? -25.853 7.721   4.300   1.00 18.72  ? 248 ASP   A C    1 
ATOM   3756 O  O    . ASP   A 1 248 ? -24.941 6.893   4.417   1.00 20.36  ? 248 ASP   A O    1 
ATOM   3757 C  CB   . ASP   A 1 248 ? -27.500 6.204   3.116   1.00 21.04  ? 248 ASP   A CB   1 
ATOM   3758 C  CG   . ASP   A 1 248 ? -28.826 5.443   3.263   1.00 24.89  ? 248 ASP   A CG   1 
ATOM   3759 O  OD1  . ASP   A 1 248 ? -29.387 5.372   4.364   1.00 29.72  ? 248 ASP   A OD1  1 
ATOM   3760 O  OD2  . ASP   A 1 248 ? -29.324 4.953   2.251   1.00 27.35  ? 248 ASP   A OD2  1 
ATOM   3761 H  H    . ASP   A 1 248 ? -28.362 8.559   3.248   1.00 20.84  ? 248 ASP   A H    1 
ATOM   3762 H  HA   . ASP   A 1 248 ? -27.459 6.779   5.073   1.00 23.37  ? 248 ASP   A HA   1 
ATOM   3763 H  HB2  . ASP   A 1 248 ? -27.506 6.659   2.260   1.00 25.25  ? 248 ASP   A HB2  1 
ATOM   3764 H  HB3  . ASP   A 1 248 ? -26.777 5.559   3.144   1.00 25.25  ? 248 ASP   A HB3  1 
ATOM   3765 N  N    . TYR   A 1 249 ? -25.634 9.024   4.264   1.00 16.87  ? 249 TYR   A N    1 
ATOM   3766 C  CA   . TYR   A 1 249 ? -24.287 9.576   4.390   1.00 16.05  ? 249 TYR   A CA   1 
ATOM   3767 C  C    . TYR   A 1 249 ? -23.804 9.471   5.832   1.00 19.78  ? 249 TYR   A C    1 
ATOM   3768 O  O    . TYR   A 1 249 ? -24.590 9.591   6.791   1.00 20.00  ? 249 TYR   A O    1 
ATOM   3769 C  CB   . TYR   A 1 249 ? -24.288 11.051  3.995   1.00 16.92  ? 249 TYR   A CB   1 
ATOM   3770 C  CG   . TYR   A 1 249 ? -22.956 11.688  4.230   1.00 16.27  ? 249 TYR   A CG   1 
ATOM   3771 C  CD1  . TYR   A 1 249 ? -21.937 11.562  3.309   1.00 16.20  ? 249 TYR   A CD1  1 
ATOM   3772 C  CD2  . TYR   A 1 249 ? -22.694 12.382  5.411   1.00 17.41  ? 249 TYR   A CD2  1 
ATOM   3773 C  CE1  . TYR   A 1 249 ? -20.673 12.072  3.572   1.00 17.46  ? 249 TYR   A CE1  1 
ATOM   3774 C  CE2  . TYR   A 1 249 ? -21.411 12.891  5.680   1.00 17.34  ? 249 TYR   A CE2  1 
ATOM   3775 C  CZ   . TYR   A 1 249 ? -20.442 12.729  4.715   1.00 17.61  ? 249 TYR   A CZ   1 
ATOM   3776 O  OH   . TYR   A 1 249 ? -19.172 13.191  4.944   1.00 19.37  ? 249 TYR   A OH   1 
ATOM   3777 H  H    . TYR   A 1 249 ? -26.247 9.619   4.168   1.00 20.24  ? 249 TYR   A H    1 
ATOM   3778 H  HA   . TYR   A 1 249 ? -23.684 9.085   3.810   1.00 19.26  ? 249 TYR   A HA   1 
ATOM   3779 H  HB2  . TYR   A 1 249 ? -24.500 11.129  3.052   1.00 20.30  ? 249 TYR   A HB2  1 
ATOM   3780 H  HB3  . TYR   A 1 249 ? -24.949 11.523  4.524   1.00 20.30  ? 249 TYR   A HB3  1 
ATOM   3781 H  HD1  . TYR   A 1 249 ? -22.098 11.129  2.502   1.00 19.44  ? 249 TYR   A HD1  1 
ATOM   3782 H  HD2  . TYR   A 1 249 ? -23.377 12.509  6.029   1.00 20.89  ? 249 TYR   A HD2  1 
ATOM   3783 H  HE1  . TYR   A 1 249 ? -19.987 11.958  2.955   1.00 20.95  ? 249 TYR   A HE1  1 
ATOM   3784 H  HE2  . TYR   A 1 249 ? -21.223 13.323  6.482   1.00 20.81  ? 249 TYR   A HE2  1 
ATOM   3785 H  HH   . TYR   A 1 249 ? -19.145 13.607  5.674   1.00 23.25  ? 249 TYR   A HH   1 
ATOM   3786 N  N    . TYR   A 1 250 ? -22.499 9.248   5.999   1.00 17.55  ? 250 TYR   A N    1 
ATOM   3787 C  CA   . TYR   A 1 250 ? -21.884 9.300   7.320   1.00 18.33  ? 250 TYR   A CA   1 
ATOM   3788 C  C    . TYR   A 1 250 ? -20.482 9.855   7.163   1.00 20.02  ? 250 TYR   A C    1 
ATOM   3789 O  O    . TYR   A 1 250 ? -19.825 9.658   6.149   1.00 18.45  ? 250 TYR   A O    1 
ATOM   3790 C  CB   . TYR   A 1 250 ? -21.931 7.961   8.031   1.00 21.25  ? 250 TYR   A CB   1 
ATOM   3791 C  CG   . TYR   A 1 250 ? -21.265 6.848   7.302   1.00 20.75  ? 250 TYR   A CG   1 
ATOM   3792 C  CD1  . TYR   A 1 250 ? -19.905 6.625   7.453   1.00 22.34  ? 250 TYR   A CD1  1 
ATOM   3793 C  CD2  . TYR   A 1 250 ? -21.977 6.011   6.462   1.00 23.79  ? 250 TYR   A CD2  1 
ATOM   3794 C  CE1  . TYR   A 1 250 ? -19.270 5.576   6.800   1.00 21.09  ? 250 TYR   A CE1  1 
ATOM   3795 C  CE2  . TYR   A 1 250 ? -21.339 4.971   5.780   1.00 25.78  ? 250 TYR   A CE2  1 
ATOM   3796 C  CZ   . TYR   A 1 250 ? -19.965 4.760   5.994   1.00 25.71  ? 250 TYR   A CZ   1 
ATOM   3797 O  OH   . TYR   A 1 250 ? -19.320 3.737   5.366   1.00 32.51  ? 250 TYR   A OH   1 
ATOM   3798 H  H    . TYR   A 1 250 ? -21.952 9.065   5.361   1.00 21.05  ? 250 TYR   A H    1 
ATOM   3799 H  HA   . TYR   A 1 250 ? -22.365 9.910   7.902   1.00 22.00  ? 250 TYR   A HA   1 
ATOM   3800 H  HB2  . TYR   A 1 250 ? -21.490 8.053   8.890   1.00 25.50  ? 250 TYR   A HB2  1 
ATOM   3801 H  HB3  . TYR   A 1 250 ? -22.859 7.712   8.159   1.00 25.50  ? 250 TYR   A HB3  1 
ATOM   3802 H  HD1  . TYR   A 1 250 ? -19.408 7.187   8.003   1.00 26.81  ? 250 TYR   A HD1  1 
ATOM   3803 H  HD2  . TYR   A 1 250 ? -22.891 6.141   6.349   1.00 28.54  ? 250 TYR   A HD2  1 
ATOM   3804 H  HE1  . TYR   A 1 250 ? -18.358 5.439   6.922   1.00 25.31  ? 250 TYR   A HE1  1 
ATOM   3805 H  HE2  . TYR   A 1 250 ? -21.815 4.428   5.195   1.00 30.94  ? 250 TYR   A HE2  1 
ATOM   3806 H  HH   . TYR   A 1 250 ? -19.867 3.288   4.913   1.00 39.01  ? 250 TYR   A HH   1 
ATOM   3807 N  N    . GLY   A 1 251 ? -19.989 10.468  8.230   1.00 23.09  ? 251 GLY   A N    1 
ATOM   3808 C  CA   . GLY   A 1 251 ? -18.635 10.965  8.200   1.00 24.03  ? 251 GLY   A CA   1 
ATOM   3809 C  C    . GLY   A 1 251 ? -17.637 9.849   8.006   1.00 27.13  ? 251 GLY   A C    1 
ATOM   3810 O  O    . GLY   A 1 251 ? -17.668 8.836   8.715   1.00 28.68  ? 251 GLY   A O    1 
ATOM   3811 H  H    . GLY   A 1 251 ? -20.414 10.603  8.965   1.00 27.71  ? 251 GLY   A H    1 
ATOM   3812 H  HA2  . GLY   A 1 251 ? -18.538 11.597  7.470   1.00 28.84  ? 251 GLY   A HA2  1 
ATOM   3813 H  HA3  . GLY   A 1 251 ? -18.437 11.416  9.036   1.00 28.84  ? 251 GLY   A HA3  1 
ATOM   3814 N  N    . GLY   A 1 252 ? -16.714 10.057  7.089   1.00 23.03  ? 252 GLY   A N    1 
ATOM   3815 C  CA   . GLY   A 1 252 ? -15.725 9.075   6.715   1.00 22.82  ? 252 GLY   A CA   1 
ATOM   3816 C  C    . GLY   A 1 252 ? -16.045 8.317   5.440   1.00 22.39  ? 252 GLY   A C    1 
ATOM   3817 O  O    . GLY   A 1 252 ? -15.152 7.662   4.867   1.00 23.85  ? 252 GLY   A O    1 
ATOM   3818 H  H    . GLY   A 1 252 ? -16.639 10.793  6.651   1.00 27.64  ? 252 GLY   A H    1 
ATOM   3819 H  HA2  . GLY   A 1 252 ? -14.873 9.522   6.590   1.00 27.39  ? 252 GLY   A HA2  1 
ATOM   3820 H  HA3  . GLY   A 1 252 ? -15.640 8.428   7.433   1.00 27.39  ? 252 GLY   A HA3  1 
ATOM   3821 N  N    . LEU   A 1 253 ? -17.293 8.384   4.969   1.00 18.10  ? 253 LEU   A N    1 
ATOM   3822 C  CA   . LEU   A 1 253 ? -17.619 7.727   3.710   1.00 17.66  ? 253 LEU   A CA   1 
ATOM   3823 C  C    . LEU   A 1 253 ? -16.812 8.424   2.619   1.00 16.06  ? 253 LEU   A C    1 
ATOM   3824 O  O    . LEU   A 1 253 ? -16.822 9.654   2.528   1.00 16.74  ? 253 LEU   A O    1 
ATOM   3825 C  CB   . LEU   A 1 253 ? -19.135 7.837   3.444   1.00 17.75  ? 253 LEU   A CB   1 
ATOM   3826 C  CG   . LEU   A 1 253 ? -19.637 7.176   2.180   1.00 17.13  ? 253 LEU   A CG   1 
ATOM   3827 C  CD1  . LEU   A 1 253 ? -19.415 5.695   2.159   1.00 17.53  ? 253 LEU   A CD1  1 
ATOM   3828 C  CD2  . LEU   A 1 253 ? -21.143 7.473   2.036   1.00 19.21  ? 253 LEU   A CD2  1 
ATOM   3829 H  H    . LEU   A 1 253 ? -17.947 8.792   5.351   1.00 21.71  ? 253 LEU   A H    1 
ATOM   3830 H  HA   . LEU   A 1 253 ? -17.404 6.781   3.725   1.00 21.19  ? 253 LEU   A HA   1 
ATOM   3831 H  HB2  . LEU   A 1 253 ? -19.603 7.426   4.188   1.00 21.30  ? 253 LEU   A HB2  1 
ATOM   3832 H  HB3  . LEU   A 1 253 ? -19.365 8.777   3.386   1.00 21.30  ? 253 LEU   A HB3  1 
ATOM   3833 H  HG   . LEU   A 1 253 ? -19.136 7.535   1.431   1.00 20.56  ? 253 LEU   A HG   1 
ATOM   3834 H  HD11 . LEU   A 1 253 ? -19.818 5.326   1.357   1.00 21.04  ? 253 LEU   A HD11 1 
ATOM   3835 H  HD12 . LEU   A 1 253 ? -18.461 5.519   2.160   1.00 21.04  ? 253 LEU   A HD12 1 
ATOM   3836 H  HD13 . LEU   A 1 253 ? -19.824 5.303   2.946   1.00 21.04  ? 253 LEU   A HD13 1 
ATOM   3837 H  HD21 . LEU   A 1 253 ? -21.471 7.053   1.225   1.00 23.05  ? 253 LEU   A HD21 1 
ATOM   3838 H  HD22 . LEU   A 1 253 ? -21.610 7.115   2.807   1.00 23.05  ? 253 LEU   A HD22 1 
ATOM   3839 H  HD23 . LEU   A 1 253 ? -21.272 8.433   1.987   1.00 23.05  ? 253 LEU   A HD23 1 
ATOM   3840 N  N    . ASP   A 1 254 ? -16.161 7.653   1.770   1.00 15.94  ? 254 ASP   A N    1 
ATOM   3841 C  CA   . ASP   A 1 254 ? -15.294 8.236   0.756   1.00 14.19  ? 254 ASP   A CA   1 
ATOM   3842 C  C    . ASP   A 1 254 ? -16.095 9.070   -0.237  1.00 13.56  ? 254 ASP   A C    1 
ATOM   3843 O  O    . ASP   A 1 254 ? -17.234 8.719   -0.611  1.00 13.86  ? 254 ASP   A O    1 
ATOM   3844 C  CB   . ASP   A 1 254 ? -14.583 7.133   -0.044  1.00 15.82  ? 254 ASP   A CB   1 
ATOM   3845 C  CG   . ASP   A 1 254 ? -13.549 7.679   -1.017  1.00 16.66  ? 254 ASP   A CG   1 
ATOM   3846 O  OD1  . ASP   A 1 254 ? -12.489 8.112   -0.515  1.00 22.45  ? 254 ASP   A OD1  1 
ATOM   3847 O  OD2  . ASP   A 1 254 ? -13.751 7.699   -2.213  1.00 16.38  ? 254 ASP   A OD2  1 
ATOM   3848 H  H    . ASP   A 1 254 ? -16.200 6.794   1.757   1.00 19.13  ? 254 ASP   A H    1 
ATOM   3849 H  HA   . ASP   A 1 254 ? -14.642 8.796   1.206   1.00 17.03  ? 254 ASP   A HA   1 
ATOM   3850 H  HB2  . ASP   A 1 254 ? -14.129 6.539   0.574   1.00 18.99  ? 254 ASP   A HB2  1 
ATOM   3851 H  HB3  . ASP   A 1 254 ? -15.243 6.639   -0.555  1.00 18.99  ? 254 ASP   A HB3  1 
ATOM   3852 N  N    . VAL   A 1 255 ? -15.477 10.121  -0.787  1.00 12.90  ? 255 VAL   A N    1 
ATOM   3853 C  CA   . VAL   A 1 255 ? -16.098 11.037  -1.715  1.00 13.17  ? 255 VAL   A CA   1 
ATOM   3854 C  C    . VAL   A 1 255 ? -16.582 10.315  -2.950  1.00 11.87  ? 255 VAL   A C    1 
ATOM   3855 O  O    . VAL   A 1 255 ? -17.488 10.809  -3.631  1.00 12.78  ? 255 VAL   A O    1 
ATOM   3856 C  CB   . VAL   A 1 255 ? -15.130 12.205  -2.047  1.00 13.98  ? 255 VAL   A CB   1 
ATOM   3857 C  CG1  . VAL   A 1 255 ? -14.893 13.045  -0.859  1.00 14.28  ? 255 VAL   A CG1  1 
ATOM   3858 C  CG2  . VAL   A 1 255 ? -13.840 11.735  -2.712  1.00 13.42  ? 255 VAL   A CG2  1 
ATOM   3859 H  H    . VAL   A 1 255 ? -14.658 10.327  -0.625  1.00 15.48  ? 255 VAL   A H    1 
ATOM   3860 H  HA   . VAL   A 1 255 ? -16.880 11.424  -1.291  1.00 15.80  ? 255 VAL   A HA   1 
ATOM   3861 H  HB   . VAL   A 1 255 ? -15.560 12.767  -2.711  1.00 16.77  ? 255 VAL   A HB   1 
ATOM   3862 H  HG11 . VAL   A 1 255 ? -14.360 13.813  -1.117  1.00 17.13  ? 255 VAL   A HG11 1 
ATOM   3863 H  HG12 . VAL   A 1 255 ? -15.746 13.337  -0.503  1.00 17.13  ? 255 VAL   A HG12 1 
ATOM   3864 H  HG13 . VAL   A 1 255 ? -14.418 12.523  -0.193  1.00 17.13  ? 255 VAL   A HG13 1 
ATOM   3865 H  HG21 . VAL   A 1 255 ? -13.318 12.510  -2.972  1.00 16.11  ? 255 VAL   A HG21 1 
ATOM   3866 H  HG22 . VAL   A 1 255 ? -13.338 11.195  -2.082  1.00 16.11  ? 255 VAL   A HG22 1 
ATOM   3867 H  HG23 . VAL   A 1 255 ? -14.062 11.208  -3.495  1.00 16.11  ? 255 VAL   A HG23 1 
ATOM   3868 N  N    . HIS   A 1 256 ? -15.963 9.208   -3.376  1.00 12.59  ? 256 HIS   A N    1 
ATOM   3869 C  CA   . HIS   A 1 256 ? -16.391 8.490   -4.583  1.00 12.84  ? 256 HIS   A CA   1 
ATOM   3870 C  C    . HIS   A 1 256 ? -17.601 7.594   -4.338  1.00 12.99  ? 256 HIS   A C    1 
ATOM   3871 O  O    . HIS   A 1 256 ? -18.134 7.035   -5.322  1.00 13.86  ? 256 HIS   A O    1 
ATOM   3872 C  CB   . HIS   A 1 256 ? -15.224 7.648   -5.120  1.00 14.11  ? 256 HIS   A CB   1 
ATOM   3873 C  CG   . HIS   A 1 256 ? -14.018 8.425   -5.499  1.00 13.43  ? 256 HIS   A CG   1 
ATOM   3874 N  ND1  . HIS   A 1 256 ? -12.987 8.643   -4.628  1.00 14.27  ? 256 HIS   A ND1  1 
ATOM   3875 C  CD2  . HIS   A 1 256 ? -13.696 9.023   -6.664  1.00 13.01  ? 256 HIS   A CD2  1 
ATOM   3876 C  CE1  . HIS   A 1 256 ? -12.048 9.337   -5.274  1.00 16.56  ? 256 HIS   A CE1  1 
ATOM   3877 N  NE2  . HIS   A 1 256 ? -12.450 9.581   -6.488  1.00 16.36  ? 256 HIS   A NE2  1 
ATOM   3878 H  H    . HIS   A 1 256 ? -15.288 8.851   -2.981  1.00 15.11  ? 256 HIS   A H    1 
ATOM   3879 H  HA   . HIS   A 1 256 ? -16.636 9.135   -5.265  1.00 15.41  ? 256 HIS   A HA   1 
ATOM   3880 H  HB2  . HIS   A 1 256 ? -14.960 7.015   -4.434  1.00 16.93  ? 256 HIS   A HB2  1 
ATOM   3881 H  HB3  . HIS   A 1 256 ? -15.525 7.173   -5.910  1.00 16.93  ? 256 HIS   A HB3  1 
ATOM   3882 H  HD1  . HIS   A 1 256 ? -12.950 8.380   -3.810  1.00 17.12  ? 256 HIS   A HD1  1 
ATOM   3883 H  HD2  . HIS   A 1 256 ? -14.214 9.052   -7.435  1.00 15.61  ? 256 HIS   A HD2  1 
ATOM   3884 H  HE1  . HIS   A 1 256 ? -11.233 9.605   -4.913  1.00 19.87  ? 256 HIS   A HE1  1 
ATOM   3885 N  N    . TYR   A 1 257 ? -18.066 7.538   -3.118  1.00 12.98  ? 257 TYR   A N    1 
ATOM   3886 C  CA   . TYR   A 1 257 ? -19.279 6.797   -2.732  1.00 13.45  ? 257 TYR   A CA   1 
ATOM   3887 C  C    . TYR   A 1 257 ? -20.361 7.756   -2.292  1.00 13.33  ? 257 TYR   A C    1 
ATOM   3888 O  O    . TYR   A 1 257 ? -21.558 7.579   -2.609  1.00 13.98  ? 257 TYR   A O    1 
ATOM   3889 C  CB   . TYR   A 1 257 ? -18.982 5.778   -1.644  1.00 13.30  ? 257 TYR   A CB   1 
ATOM   3890 C  CG   . TYR   A 1 257 ? -17.840 4.847   -1.996  1.00 14.66  ? 257 TYR   A CG   1 
ATOM   3891 C  CD1  . TYR   A 1 257 ? -17.669 4.362   -3.252  1.00 16.98  ? 257 TYR   A CD1  1 
ATOM   3892 C  CD2  . TYR   A 1 257 ? -16.946 4.451   -1.035  1.00 19.46  ? 257 TYR   A CD2  1 
ATOM   3893 C  CE1  . TYR   A 1 257 ? -16.537 3.537   -3.606  1.00 20.53  ? 257 TYR   A CE1  1 
ATOM   3894 C  CE2  . TYR   A 1 257 ? -15.822 3.627   -1.368  1.00 22.95  ? 257 TYR   A CE2  1 
ATOM   3895 C  CZ   . TYR   A 1 257 ? -15.695 3.177   -2.624  1.00 20.49  ? 257 TYR   A CZ   1 
ATOM   3896 O  OH   . TYR   A 1 257 ? -14.610 2.340   -3.019  1.00 34.00  ? 257 TYR   A OH   1 
ATOM   3897 H  H    . TYR   A 1 257 ? -17.693 7.933   -2.452  1.00 15.58  ? 257 TYR   A H    1 
ATOM   3898 H  HA   . TYR   A 1 257 ? -19.607 6.269   -3.476  1.00 16.14  ? 257 TYR   A HA   1 
ATOM   3899 H  HB2  . TYR   A 1 257 ? -18.745 6.248   -0.829  1.00 15.96  ? 257 TYR   A HB2  1 
ATOM   3900 H  HB3  . TYR   A 1 257 ? -19.774 5.237   -1.496  1.00 15.96  ? 257 TYR   A HB3  1 
ATOM   3901 H  HD1  . TYR   A 1 257 ? -18.299 4.567   -3.905  1.00 20.38  ? 257 TYR   A HD1  1 
ATOM   3902 H  HD2  . TYR   A 1 257 ? -17.071 4.720   -0.154  1.00 23.35  ? 257 TYR   A HD2  1 
ATOM   3903 H  HE1  . TYR   A 1 257 ? -16.397 3.264   -4.484  1.00 24.64  ? 257 TYR   A HE1  1 
ATOM   3904 H  HE2  . TYR   A 1 257 ? -15.190 3.408   -0.722  1.00 27.54  ? 257 TYR   A HE2  1 
ATOM   3905 H  HH   . TYR   A 1 257 ? -14.118 2.177   -2.358  1.00 40.79  ? 257 TYR   A HH   1 
ATOM   3906 N  N    . SER   A 1 258 ? -20.019 8.825   -1.557  1.00 12.62  ? 258 SER   A N    1 
ATOM   3907 C  CA   . SER   A 1 258 ? -21.008 9.841   -1.213  1.00 11.65  ? 258 SER   A CA   1 
ATOM   3908 C  C    . SER   A 1 258 ? -21.406 10.676  -2.406  1.00 12.28  ? 258 SER   A C    1 
ATOM   3909 O  O    . SER   A 1 258 ? -22.436 11.366  -2.320  1.00 12.81  ? 258 SER   A O    1 
ATOM   3910 C  CB   . SER   A 1 258 ? -20.464 10.726  -0.123  1.00 13.57  ? 258 SER   A CB   1 
ATOM   3911 O  OG   . SER   A 1 258 ? -19.382 11.490  -0.616  1.00 14.64  ? 258 SER   A OG   1 
ATOM   3912 H  H    . SER   A 1 258 ? -19.229 8.978   -1.253  1.00 15.14  ? 258 SER   A H    1 
ATOM   3913 H  HA   . SER   A 1 258 ? -21.807 9.410   -0.872  1.00 13.97  ? 258 SER   A HA   1 
ATOM   3914 H  HB2  . SER   A 1 258 ? -21.164 11.324  0.182   1.00 16.28  ? 258 SER   A HB2  1 
ATOM   3915 H  HB3  . SER   A 1 258 ? -20.155 10.174  0.612   1.00 16.28  ? 258 SER   A HB3  1 
ATOM   3916 H  HG   . SER   A 1 258 ? -19.061 11.964  -0.000  1.00 17.57  ? 258 SER   A HG   1 
ATOM   3917 N  N    . SER   A 1 259 ? -20.644 10.616  -3.510  1.00 11.38  ? 259 SER   A N    1 
ATOM   3918 C  CA   . SER   A 1 259 ? -21.047 11.218  -4.750  1.00 10.96  ? 259 SER   A CA   1 
ATOM   3919 C  C    . SER   A 1 259 ? -22.382 10.656  -5.242  1.00 10.48  ? 259 SER   A C    1 
ATOM   3920 O  O    . SER   A 1 259 ? -22.992 11.258  -6.136  1.00 11.47  ? 259 SER   A O    1 
ATOM   3921 C  CB   . SER   A 1 259 ? -19.951 11.033  -5.807  1.00 12.05  ? 259 SER   A CB   1 
ATOM   3922 O  OG   . SER   A 1 259 ? -19.713 9.666   -6.013  1.00 12.96  ? 259 SER   A OG   1 
ATOM   3923 H  H    . SER   A 1 259 ? -19.880 10.223  -3.550  1.00 13.66  ? 259 SER   A H    1 
ATOM   3924 H  HA   . SER   A 1 259 ? -21.159 12.173  -4.623  1.00 13.15  ? 259 SER   A HA   1 
ATOM   3925 H  HB2  . SER   A 1 259 ? -20.239 11.435  -6.641  1.00 14.46  ? 259 SER   A HB2  1 
ATOM   3926 H  HB3  . SER   A 1 259 ? -19.134 11.457  -5.499  1.00 14.46  ? 259 SER   A HB3  1 
ATOM   3927 H  HG   . SER   A 1 259 ? -19.507 9.298   -5.286  1.00 15.55  ? 259 SER   A HG   1 
ATOM   3928 N  N    . GLY   A 1 260 ? -22.812 9.513   -4.764  1.00 11.91  ? 260 GLY   A N    1 
ATOM   3929 C  CA   . GLY   A 1 260 ? -24.089 8.956   -5.170  1.00 11.07  ? 260 GLY   A CA   1 
ATOM   3930 C  C    . GLY   A 1 260 ? -25.223 9.913   -4.935  1.00 11.77  ? 260 GLY   A C    1 
ATOM   3931 O  O    . GLY   A 1 260 ? -26.205 9.914   -5.681  1.00 12.41  ? 260 GLY   A O    1 
ATOM   3932 H  H    . GLY   A 1 260 ? -22.384 9.029   -4.196  1.00 14.29  ? 260 GLY   A H    1 
ATOM   3933 H  HA2  . GLY   A 1 260 ? -24.060 8.740   -6.116  1.00 13.28  ? 260 GLY   A HA2  1 
ATOM   3934 H  HA3  . GLY   A 1 260 ? -24.261 8.145   -4.666  1.00 13.28  ? 260 GLY   A HA3  1 
ATOM   3935 N  N    . VAL   A 1 261 ? -25.165 10.709  -3.867  1.00 11.99  ? 261 VAL   A N    1 
ATOM   3936 C  CA   . VAL   A 1 261 ? -26.305 11.577  -3.566  1.00 12.26  ? 261 VAL   A CA   1 
ATOM   3937 C  C    . VAL   A 1 261 ? -26.576 12.556  -4.705  1.00 11.36  ? 261 VAL   A C    1 
ATOM   3938 O  O    . VAL   A 1 261 ? -27.682 12.609  -5.241  1.00 12.46  ? 261 VAL   A O    1 
ATOM   3939 C  CB   . VAL   A 1 261 ? -26.067 12.328  -2.247  1.00 11.93  ? 261 VAL   A CB   1 
ATOM   3940 C  CG1  . VAL   A 1 261 ? -27.260 13.264  -1.944  1.00 13.56  ? 261 VAL   A CG1  1 
ATOM   3941 C  CG2  . VAL   A 1 261 ? -25.832 11.329  -1.117  1.00 15.36  ? 261 VAL   A CG2  1 
ATOM   3942 H  H    . VAL   A 1 261 ? -24.503 10.764  -3.321  1.00 14.39  ? 261 VAL   A H    1 
ATOM   3943 H  HA   . VAL   A 1 261 ? -27.089 11.014  -3.473  1.00 14.71  ? 261 VAL   A HA   1 
ATOM   3944 H  HB   . VAL   A 1 261 ? -25.274 12.882  -2.321  1.00 14.32  ? 261 VAL   A HB   1 
ATOM   3945 H  HG11 . VAL   A 1 261 ? -27.169 13.610  -1.042  1.00 16.27  ? 261 VAL   A HG11 1 
ATOM   3946 H  HG12 . VAL   A 1 261 ? -27.257 13.996  -2.581  1.00 16.27  ? 261 VAL   A HG12 1 
ATOM   3947 H  HG13 . VAL   A 1 261 ? -28.085 12.760  -2.023  1.00 16.27  ? 261 VAL   A HG13 1 
ATOM   3948 H  HG21 . VAL   A 1 261 ? -25.740 11.813  -0.282  1.00 18.43  ? 261 VAL   A HG21 1 
ATOM   3949 H  HG22 . VAL   A 1 261 ? -26.588 10.724  -1.068  1.00 18.43  ? 261 VAL   A HG22 1 
ATOM   3950 H  HG23 . VAL   A 1 261 ? -25.020 10.830  -1.300  1.00 18.43  ? 261 VAL   A HG23 1 
ATOM   3951 N  N    . TYR   A 1 262 ? -25.582 13.350  -5.091  1.00 10.71  ? 262 TYR   A N    1 
ATOM   3952 C  CA   . TYR   A 1 262 ? -25.748 14.338  -6.143  1.00 9.90   ? 262 TYR   A CA   1 
ATOM   3953 C  C    . TYR   A 1 262 ? -25.795 13.683  -7.510  1.00 10.38  ? 262 TYR   A C    1 
ATOM   3954 O  O    . TYR   A 1 262 ? -26.396 14.227  -8.431  1.00 11.65  ? 262 TYR   A O    1 
ATOM   3955 C  CB   . TYR   A 1 262 ? -24.725 15.460  -6.028  1.00 12.39  ? 262 TYR   A CB   1 
ATOM   3956 C  CG   . TYR   A 1 262 ? -25.226 16.649  -5.198  1.00 11.18  ? 262 TYR   A CG   1 
ATOM   3957 C  CD1  . TYR   A 1 262 ? -25.514 16.493  -3.856  1.00 13.17  ? 262 TYR   A CD1  1 
ATOM   3958 C  CD2  . TYR   A 1 262 ? -25.442 17.868  -5.751  1.00 12.00  ? 262 TYR   A CD2  1 
ATOM   3959 C  CE1  . TYR   A 1 262 ? -26.044 17.547  -3.079  1.00 12.10  ? 262 TYR   A CE1  1 
ATOM   3960 C  CE2  . TYR   A 1 262 ? -25.907 18.939  -4.948  1.00 12.99  ? 262 TYR   A CE2  1 
ATOM   3961 C  CZ   . TYR   A 1 262 ? -26.234 18.722  -3.659  1.00 12.28  ? 262 TYR   A CZ   1 
ATOM   3962 O  OH   . TYR   A 1 262 ? -26.706 19.836  -2.958  1.00 14.31  ? 262 TYR   A OH   1 
ATOM   3963 H  H    . TYR   A 1 262 ? -24.791 13.335  -4.753  1.00 12.86  ? 262 TYR   A H    1 
ATOM   3964 H  HA   . TYR   A 1 262 ? -26.595 14.798  -6.035  1.00 11.88  ? 262 TYR   A HA   1 
ATOM   3965 H  HB2  . TYR   A 1 262 ? -23.926 15.114  -5.601  1.00 14.87  ? 262 TYR   A HB2  1 
ATOM   3966 H  HB3  . TYR   A 1 262 ? -24.513 15.785  -6.917  1.00 14.87  ? 262 TYR   A HB3  1 
ATOM   3967 H  HD1  . TYR   A 1 262 ? -25.355 15.670  -3.453  1.00 15.80  ? 262 TYR   A HD1  1 
ATOM   3968 H  HD2  . TYR   A 1 262 ? -25.284 18.002  -6.658  1.00 14.40  ? 262 TYR   A HD2  1 
ATOM   3969 H  HE1  . TYR   A 1 262 ? -26.254 17.419  -2.182  1.00 14.52  ? 262 TYR   A HE1  1 
ATOM   3970 H  HE2  . TYR   A 1 262 ? -25.987 19.792  -5.310  1.00 15.59  ? 262 TYR   A HE2  1 
ATOM   3971 H  HH   . TYR   A 1 262 ? -26.784 19.651  -2.143  1.00 17.17  ? 262 TYR   A HH   1 
ATOM   3972 N  N    . ASN   A 1 263 ? -25.196 12.494  -7.693  1.00 10.37  ? 263 ASN   A N    1 
ATOM   3973 C  CA   . ASN   A 1 263 ? -25.314 11.796  -8.963  1.00 11.15  ? 263 ASN   A CA   1 
ATOM   3974 C  C    . ASN   A 1 263 ? -26.752 11.381  -9.186  1.00 11.97  ? 263 ASN   A C    1 
ATOM   3975 O  O    . ASN   A 1 263 ? -27.318 11.572  -10.272 1.00 12.54  ? 263 ASN   A O    1 
ATOM   3976 C  CB   . ASN   A 1 263 ? -24.417 10.576  -8.975  1.00 11.68  ? 263 ASN   A CB   1 
ATOM   3977 C  CG   . ASN   A 1 263 ? -22.989 10.902  -9.240  1.00 13.14  ? 263 ASN   A CG   1 
ATOM   3978 O  OD1  . ASN   A 1 263 ? -22.622 12.055  -9.407  1.00 13.88  ? 263 ASN   A OD1  1 
ATOM   3979 N  ND2  . ASN   A 1 263 ? -22.150 9.872   -9.328  1.00 13.87  ? 263 ASN   A ND2  1 
ATOM   3980 H  H    . ASN   A 1 263 ? -24.725 12.084  -7.102  1.00 12.45  ? 263 ASN   A H    1 
ATOM   3981 H  HA   . ASN   A 1 263 ? -25.030 12.384  -9.680  1.00 13.38  ? 263 ASN   A HA   1 
ATOM   3982 H  HB2  . ASN   A 1 263 ? -24.467 10.140  -8.110  1.00 14.01  ? 263 ASN   A HB2  1 
ATOM   3983 H  HB3  . ASN   A 1 263 ? -24.718 9.971   -9.670  1.00 14.01  ? 263 ASN   A HB3  1 
ATOM   3984 H  HD21 . ASN   A 1 263 ? -21.315 10.009  -9.480  1.00 16.64  ? 263 ASN   A HD21 1 
ATOM   3985 H  HD22 . ASN   A 1 263 ? -22.444 9.069   -9.232  1.00 16.64  ? 263 ASN   A HD22 1 
ATOM   3986 N  N    . HIS   A 1 264 ? -27.370 10.822  -8.152  1.00 11.05  ? 264 HIS   A N    1 
ATOM   3987 C  CA   . HIS   A 1 264 ? -28.757 10.401  -8.225  1.00 12.11  ? 264 HIS   A CA   1 
ATOM   3988 C  C    . HIS   A 1 264 ? -29.654 11.608  -8.411  1.00 12.12  ? 264 HIS   A C    1 
ATOM   3989 O  O    . HIS   A 1 264 ? -30.587 11.576  -9.218  1.00 12.94  ? 264 HIS   A O    1 
ATOM   3990 C  CB   . HIS   A 1 264 ? -29.080 9.581   -6.976  1.00 12.08  ? 264 HIS   A CB   1 
ATOM   3991 C  CG   . HIS   A 1 264 ? -30.328 8.823   -7.059  1.00 13.74  ? 264 HIS   A CG   1 
ATOM   3992 N  ND1  . HIS   A 1 264 ? -30.961 8.343   -5.941  1.00 16.77  ? 264 HIS   A ND1  1 
ATOM   3993 C  CD2  . HIS   A 1 264 ? -31.028 8.395   -8.128  1.00 15.63  ? 264 HIS   A CD2  1 
ATOM   3994 C  CE1  . HIS   A 1 264 ? -32.063 7.695   -6.320  1.00 19.64  ? 264 HIS   A CE1  1 
ATOM   3995 N  NE2  . HIS   A 1 264 ? -32.105 7.685   -7.647  1.00 18.17  ? 264 HIS   A NE2  1 
ATOM   3996 H  H    . HIS   A 1 264 ? -27.003 10.675  -7.388  1.00 13.26  ? 264 HIS   A H    1 
ATOM   3997 H  HA   . HIS   A 1 264 ? -28.920 9.821   -8.985  1.00 14.54  ? 264 HIS   A HA   1 
ATOM   3998 H  HB2  . HIS   A 1 264 ? -28.361 8.948   -6.827  1.00 14.49  ? 264 HIS   A HB2  1 
ATOM   3999 H  HB3  . HIS   A 1 264 ? -29.153 10.185  -6.220  1.00 14.49  ? 264 HIS   A HB3  1 
ATOM   4000 H  HD1  . HIS   A 1 264 ? -30.691 8.443   -5.131  1.00 20.13  ? 264 HIS   A HD1  1 
ATOM   4001 H  HD2  . HIS   A 1 264 ? -30.822 8.549   -9.021  1.00 18.76  ? 264 HIS   A HD2  1 
ATOM   4002 H  HE1  . HIS   A 1 264 ? -32.694 7.315   -5.752  1.00 23.56  ? 264 HIS   A HE1  1 
ATOM   4003 N  N    . LEU   A 1 265 ? -29.347 12.695  -7.688  1.00 12.62  ? 265 LEU   A N    1 
ATOM   4004 C  CA   . LEU   A 1 265 ? -30.102 13.935  -7.836  1.00 13.03  ? 265 LEU   A CA   1 
ATOM   4005 C  C    . LEU   A 1 265 ? -30.073 14.427  -9.274  1.00 13.00  ? 265 LEU   A C    1 
ATOM   4006 O  O    . LEU   A 1 265 ? -31.096 14.832  -9.824  1.00 13.62  ? 265 LEU   A O    1 
ATOM   4007 C  CB   . LEU   A 1 265 ? -29.517 14.948  -6.866  1.00 12.13  ? 265 LEU   A CB   1 
ATOM   4008 C  CG   . LEU   A 1 265 ? -30.060 16.354  -6.960  1.00 13.08  ? 265 LEU   A CG   1 
ATOM   4009 C  CD1  . LEU   A 1 265 ? -31.550 16.439  -6.736  1.00 14.93  ? 265 LEU   A CD1  1 
ATOM   4010 C  CD2  . LEU   A 1 265 ? -29.321 17.239  -5.947  1.00 14.24  ? 265 LEU   A CD2  1 
ATOM   4011 H  H    . LEU   A 1 265 ? -28.712 12.735  -7.110  1.00 15.14  ? 265 LEU   A H    1 
ATOM   4012 H  HA   . LEU   A 1 265 ? -31.037 13.801  -7.617  1.00 15.63  ? 265 LEU   A HA   1 
ATOM   4013 H  HB2  . LEU   A 1 265 ? -29.688 14.635  -5.964  1.00 14.56  ? 265 LEU   A HB2  1 
ATOM   4014 H  HB3  . LEU   A 1 265 ? -28.562 15.000  -7.024  1.00 14.56  ? 265 LEU   A HB3  1 
ATOM   4015 H  HG   . LEU   A 1 265 ? -29.913 16.673  -7.864  1.00 15.70  ? 265 LEU   A HG   1 
ATOM   4016 H  HD11 . LEU   A 1 265 ? -31.825 17.367  -6.789  1.00 17.92  ? 265 LEU   A HD11 1 
ATOM   4017 H  HD12 . LEU   A 1 265 ? -32.002 15.920  -7.420  1.00 17.92  ? 265 LEU   A HD12 1 
ATOM   4018 H  HD13 . LEU   A 1 265 ? -31.758 16.082  -5.858  1.00 17.92  ? 265 LEU   A HD13 1 
ATOM   4019 H  HD21 . LEU   A 1 265 ? -29.740 18.114  -5.928  1.00 17.09  ? 265 LEU   A HD21 1 
ATOM   4020 H  HD22 . LEU   A 1 265 ? -29.373 16.828  -5.071  1.00 17.09  ? 265 LEU   A HD22 1 
ATOM   4021 H  HD23 . LEU   A 1 265 ? -28.394 17.323  -6.219  1.00 17.09  ? 265 LEU   A HD23 1 
ATOM   4022 N  N    . PHE   A 1 266 ? -28.895 14.402  -9.890  1.00 11.66  ? 266 PHE   A N    1 
ATOM   4023 C  CA   . PHE   A 1 266 ? -28.774 14.876  -11.263 1.00 11.18  ? 266 PHE   A CA   1 
ATOM   4024 C  C    . PHE   A 1 266 ? -29.587 14.036  -12.226 1.00 11.33  ? 266 PHE   A C    1 
ATOM   4025 O  O    . PHE   A 1 266 ? -30.307 14.566  -13.088 1.00 13.77  ? 266 PHE   A O    1 
ATOM   4026 C  CB   . PHE   A 1 266 ? -27.290 14.883  -11.641 1.00 12.34  ? 266 PHE   A CB   1 
ATOM   4027 C  CG   . PHE   A 1 266 ? -26.991 15.378  -13.039 1.00 12.24  ? 266 PHE   A CG   1 
ATOM   4028 C  CD1  . PHE   A 1 266 ? -27.122 16.713  -13.370 1.00 13.44  ? 266 PHE   A CD1  1 
ATOM   4029 C  CD2  . PHE   A 1 266 ? -26.491 14.512  -14.006 1.00 14.94  ? 266 PHE   A CD2  1 
ATOM   4030 C  CE1  . PHE   A 1 266 ? -26.789 17.187  -14.626 1.00 15.34  ? 266 PHE   A CE1  1 
ATOM   4031 C  CE2  . PHE   A 1 266 ? -26.133 15.019  -15.290 1.00 15.23  ? 266 PHE   A CE2  1 
ATOM   4032 C  CZ   . PHE   A 1 266 ? -26.336 16.330  -15.559 1.00 14.23  ? 266 PHE   A CZ   1 
ATOM   4033 H  H    . PHE   A 1 266 ? -28.161 14.120  -9.541  1.00 13.99  ? 266 PHE   A H    1 
ATOM   4034 H  HA   . PHE   A 1 266 ? -29.121 15.779  -11.331 1.00 13.41  ? 266 PHE   A HA   1 
ATOM   4035 H  HB2  . PHE   A 1 266 ? -26.818 15.460  -11.021 1.00 14.81  ? 266 PHE   A HB2  1 
ATOM   4036 H  HB3  . PHE   A 1 266 ? -26.952 13.976  -11.575 1.00 14.81  ? 266 PHE   A HB3  1 
ATOM   4037 H  HD1  . PHE   A 1 266 ? -27.442 17.309  -12.732 1.00 16.12  ? 266 PHE   A HD1  1 
ATOM   4038 H  HD2  . PHE   A 1 266 ? -26.391 13.607  -13.816 1.00 17.93  ? 266 PHE   A HD2  1 
ATOM   4039 H  HE1  . PHE   A 1 266 ? -26.877 18.091  -14.824 1.00 18.41  ? 266 PHE   A HE1  1 
ATOM   4040 H  HE2  . PHE   A 1 266 ? -25.764 14.457  -15.933 1.00 18.27  ? 266 PHE   A HE2  1 
ATOM   4041 H  HZ   . PHE   A 1 266 ? -26.157 16.647  -16.415 1.00 17.08  ? 266 PHE   A HZ   1 
ATOM   4042 N  N    . TYR   A 1 267 ? -29.544 12.716  -12.060 1.00 12.25  ? 267 TYR   A N    1 
ATOM   4043 C  CA   . TYR   A 1 267 ? -30.321 11.829  -12.880 1.00 12.76  ? 267 TYR   A CA   1 
ATOM   4044 C  C    . TYR   A 1 267 ? -31.805 12.117  -12.701 1.00 12.67  ? 267 TYR   A C    1 
ATOM   4045 O  O    . TYR   A 1 267 ? -32.580 12.190  -13.658 1.00 14.35  ? 267 TYR   A O    1 
ATOM   4046 C  CB   . TYR   A 1 267 ? -30.031 10.367  -12.467 1.00 14.40  ? 267 TYR   A CB   1 
ATOM   4047 C  CG   . TYR   A 1 267 ? -30.855 9.392   -13.170 1.00 13.97  ? 267 TYR   A CG   1 
ATOM   4048 C  CD1  . TYR   A 1 267 ? -30.454 8.892   -14.425 1.00 15.88  ? 267 TYR   A CD1  1 
ATOM   4049 C  CD2  . TYR   A 1 267 ? -32.015 8.894   -12.633 1.00 15.93  ? 267 TYR   A CD2  1 
ATOM   4050 C  CE1  . TYR   A 1 267 ? -31.225 7.961   -15.093 1.00 18.31  ? 267 TYR   A CE1  1 
ATOM   4051 C  CE2  . TYR   A 1 267 ? -32.795 7.976   -13.342 1.00 18.21  ? 267 TYR   A CE2  1 
ATOM   4052 C  CZ   . TYR   A 1 267 ? -32.371 7.538   -14.555 1.00 16.36  ? 267 TYR   A CZ   1 
ATOM   4053 O  OH   . TYR   A 1 267 ? -33.156 6.565   -15.201 1.00 25.24  ? 267 TYR   A OH   1 
ATOM   4054 H  H    . TYR   A 1 267 ? -29.065 12.315  -11.470 1.00 14.70  ? 267 TYR   A H    1 
ATOM   4055 H  HA   . TYR   A 1 267 ? -30.077 11.952  -13.811 1.00 15.31  ? 267 TYR   A HA   1 
ATOM   4056 H  HB2  . TYR   A 1 267 ? -29.102 10.166  -12.660 1.00 17.28  ? 267 TYR   A HB2  1 
ATOM   4057 H  HB3  . TYR   A 1 267 ? -30.202 10.271  -11.517 1.00 17.28  ? 267 TYR   A HB3  1 
ATOM   4058 H  HD1  . TYR   A 1 267 ? -29.662 9.192   -14.808 1.00 19.05  ? 267 TYR   A HD1  1 
ATOM   4059 H  HD2  . TYR   A 1 267 ? -32.285 9.170   -11.787 1.00 19.12  ? 267 TYR   A HD2  1 
ATOM   4060 H  HE1  . TYR   A 1 267 ? -30.946 7.630   -15.916 1.00 21.97  ? 267 TYR   A HE1  1 
ATOM   4061 H  HE2  . TYR   A 1 267 ? -33.597 7.668   -12.986 1.00 21.86  ? 267 TYR   A HE2  1 
ATOM   4062 H  HH   . TYR   A 1 267 ? -33.793 6.334   -14.705 1.00 30.29  ? 267 TYR   A HH   1 
ATOM   4063 N  N    . ILE   A 1 268 ? -32.249 12.228  -11.437 1.00 12.74  ? 268 ILE   A N    1 
ATOM   4064 C  CA   . ILE   A 1 268 ? -33.675 12.459  -11.159 1.00 13.83  ? 268 ILE   A CA   1 
ATOM   4065 C  C    . ILE   A 1 268 ? -34.150 13.766  -11.793 1.00 14.41  ? 268 ILE   A C    1 
ATOM   4066 O  O    . ILE   A 1 268 ? -35.213 13.820  -12.426 1.00 16.07  ? 268 ILE   A O    1 
ATOM   4067 C  CB   . ILE   A 1 268 ? -33.925 12.434  -9.639  1.00 15.06  ? 268 ILE   A CB   1 
ATOM   4068 C  CG1  . ILE   A 1 268 ? -33.773 11.016  -9.082  1.00 15.59  ? 268 ILE   A CG1  1 
ATOM   4069 C  CG2  . ILE   A 1 268 ? -35.296 12.939  -9.300  1.00 15.65  ? 268 ILE   A CG2  1 
ATOM   4070 C  CD1  . ILE   A 1 268 ? -33.555 10.966  -7.568  1.00 19.16  ? 268 ILE   A CD1  1 
ATOM   4071 H  H    . ILE   A 1 268 ? -31.754 12.173  -10.737 1.00 15.29  ? 268 ILE   A H    1 
ATOM   4072 H  HA   . ILE   A 1 268 ? -34.189 11.743  -11.564 1.00 16.59  ? 268 ILE   A HA   1 
ATOM   4073 H  HB   . ILE   A 1 268 ? -33.260 13.016  -9.239  1.00 18.07  ? 268 ILE   A HB   1 
ATOM   4074 H  HG12 . ILE   A 1 268 ? -34.579 10.516  -9.282  1.00 18.70  ? 268 ILE   A HG12 1 
ATOM   4075 H  HG13 . ILE   A 1 268 ? -33.008 10.596  -9.505  1.00 18.70  ? 268 ILE   A HG13 1 
ATOM   4076 H  HG21 . ILE   A 1 268 ? -35.503 12.701  -8.383  1.00 18.78  ? 268 ILE   A HG21 1 
ATOM   4077 H  HG22 . ILE   A 1 268 ? -35.312 13.904  -9.403  1.00 18.78  ? 268 ILE   A HG22 1 
ATOM   4078 H  HG23 . ILE   A 1 268 ? -35.940 12.532  -9.901  1.00 18.78  ? 268 ILE   A HG23 1 
ATOM   4079 H  HD11 . ILE   A 1 268 ? -33.395 10.047  -7.302  1.00 22.99  ? 268 ILE   A HD11 1 
ATOM   4080 H  HD12 . ILE   A 1 268 ? -32.788 11.514  -7.340  1.00 22.99  ? 268 ILE   A HD12 1 
ATOM   4081 H  HD13 . ILE   A 1 268 ? -34.348 11.305  -7.123  1.00 22.99  ? 268 ILE   A HD13 1 
ATOM   4082 N  N    . LEU   A 1 269 ? -33.366 14.841  -11.618 1.00 14.02  ? 269 LEU   A N    1 
ATOM   4083 C  CA   . LEU   A 1 269 ? -33.746 16.159  -12.150 1.00 13.66  ? 269 LEU   A CA   1 
ATOM   4084 C  C    . LEU   A 1 269 ? -33.808 16.161  -13.671 1.00 13.79  ? 269 LEU   A C    1 
ATOM   4085 O  O    . LEU   A 1 269 ? -34.775 16.645  -14.250 1.00 15.39  ? 269 LEU   A O    1 
ATOM   4086 C  CB   . LEU   A 1 269 ? -32.769 17.203  -11.624 1.00 14.32  ? 269 LEU   A CB   1 
ATOM   4087 C  CG   . LEU   A 1 269 ? -33.041 18.635  -12.168 1.00 13.68  ? 269 LEU   A CG   1 
ATOM   4088 C  CD1  . LEU   A 1 269 ? -34.464 19.088  -11.764 1.00 16.13  ? 269 LEU   A CD1  1 
ATOM   4089 C  CD2  . LEU   A 1 269 ? -31.976 19.562  -11.624 1.00 15.56  ? 269 LEU   A CD2  1 
ATOM   4090 H  H    . LEU   A 1 269 ? -32.615 14.836  -11.198 1.00 16.83  ? 269 LEU   A H    1 
ATOM   4091 H  HA   . LEU   A 1 269 ? -34.636 16.391  -11.840 1.00 16.39  ? 269 LEU   A HA   1 
ATOM   4092 H  HB2  . LEU   A 1 269 ? -32.836 17.234  -10.657 1.00 17.18  ? 269 LEU   A HB2  1 
ATOM   4093 H  HB3  . LEU   A 1 269 ? -31.871 16.950  -11.887 1.00 17.18  ? 269 LEU   A HB3  1 
ATOM   4094 H  HG   . LEU   A 1 269 ? -33.002 18.658  -13.137 1.00 16.41  ? 269 LEU   A HG   1 
ATOM   4095 H  HD11 . LEU   A 1 269 ? -34.582 20.017  -12.015 1.00 19.35  ? 269 LEU   A HD11 1 
ATOM   4096 H  HD12 . LEU   A 1 269 ? -35.114 18.535  -12.225 1.00 19.35  ? 269 LEU   A HD12 1 
ATOM   4097 H  HD13 . LEU   A 1 269 ? -34.566 18.988  -10.805 1.00 19.35  ? 269 LEU   A HD13 1 
ATOM   4098 H  HD21 . LEU   A 1 269 ? -32.154 20.464  -11.934 1.00 18.68  ? 269 LEU   A HD21 1 
ATOM   4099 H  HD22 . LEU   A 1 269 ? -31.998 19.534  -10.655 1.00 18.68  ? 269 LEU   A HD22 1 
ATOM   4100 H  HD23 . LEU   A 1 269 ? -31.108 19.269  -11.944 1.00 18.68  ? 269 LEU   A HD23 1 
ATOM   4101 N  N    . ALA   A 1 270 ? -32.804 15.560  -14.321 1.00 13.26  ? 270 ALA   A N    1 
ATOM   4102 C  CA   . ALA   A 1 270 ? -32.775 15.500  -15.773 1.00 13.60  ? 270 ALA   A CA   1 
ATOM   4103 C  C    . ALA   A 1 270 ? -33.890 14.683  -16.358 1.00 17.04  ? 270 ALA   A C    1 
ATOM   4104 O  O    . ALA   A 1 270 ? -34.231 14.881  -17.534 1.00 18.47  ? 270 ALA   A O    1 
ATOM   4105 C  CB   . ALA   A 1 270 ? -31.470 14.849  -16.182 1.00 15.76  ? 270 ALA   A CB   1 
ATOM   4106 H  H    . ALA   A 1 270 ? -32.132 15.182  -13.940 1.00 15.91  ? 270 ALA   A H    1 
ATOM   4107 H  HA   . ALA   A 1 270 ? -32.849 16.402  -16.121 1.00 16.32  ? 270 ALA   A HA   1 
ATOM   4108 H  HB1  . ALA   A 1 270 ? -31.428 14.809  -17.150 1.00 18.91  ? 270 ALA   A HB1  1 
ATOM   4109 H  HB2  . ALA   A 1 270 ? -30.733 15.378  -15.840 1.00 18.91  ? 270 ALA   A HB2  1 
ATOM   4110 H  HB3  . ALA   A 1 270 ? -31.434 13.954  -15.811 1.00 18.91  ? 270 ALA   A HB3  1 
ATOM   4111 N  N    . ASN   A 1 271 ? -34.508 13.808  -15.580 1.00 15.12  ? 271 ASN   A N    1 
ATOM   4112 C  CA   . ASN   A 1 271 ? -35.588 12.964  -16.038 1.00 19.23  ? 271 ASN   A CA   1 
ATOM   4113 C  C    . ASN   A 1 271 ? -36.963 13.412  -15.548 1.00 19.76  ? 271 ASN   A C    1 
ATOM   4114 O  O    . ASN   A 1 271 ? -37.958 12.711  -15.794 1.00 22.09  ? 271 ASN   A O    1 
ATOM   4115 C  CB   . ASN   A 1 271 ? -35.286 11.535  -15.600 1.00 19.47  ? 271 ASN   A CB   1 
ATOM   4116 C  CG   . ASN   A 1 271 ? -34.284 10.862  -16.486 1.00 22.18  ? 271 ASN   A CG   1 
ATOM   4117 O  OD1  . ASN   A 1 271 ? -34.638 10.454  -17.622 1.00 27.33  ? 271 ASN   A OD1  1 
ATOM   4118 N  ND2  . ASN   A 1 271 ? -33.061 10.784  -16.092 1.00 20.34  ? 271 ASN   A ND2  1 
ATOM   4119 H  H    . ASN   A 1 271 ? -34.309 13.683  -14.753 1.00 18.15  ? 271 ASN   A H    1 
ATOM   4120 H  HA   . ASN   A 1 271 ? -35.638 12.992  -17.006 1.00 23.08  ? 271 ASN   A HA   1 
ATOM   4121 H  HB2  . ASN   A 1 271 ? -34.929 11.549  -14.698 1.00 23.37  ? 271 ASN   A HB2  1 
ATOM   4122 H  HB3  . ASN   A 1 271 ? -36.106 11.016  -15.624 1.00 23.37  ? 271 ASN   A HB3  1 
ATOM   4123 H  HD21 . ASN   A 1 271 ? -32.473 10.401  -16.589 1.00 24.41  ? 271 ASN   A HD21 1 
ATOM   4124 H  HD22 . ASN   A 1 271 ? -32.832 11.115  -15.332 1.00 24.41  ? 271 ASN   A HD22 1 
ATOM   4125 N  N    . GLN   A 1 272 ? -37.062 14.562  -14.887 1.00 17.75  ? 272 GLN   A N    1 
ATOM   4126 C  CA   . GLN   A 1 272 ? -38.380 15.087  -14.566 1.00 18.79  ? 272 GLN   A CA   1 
ATOM   4127 C  C    . GLN   A 1 272 ? -39.126 15.448  -15.856 1.00 20.68  ? 272 GLN   A C    1 
ATOM   4128 O  O    . GLN   A 1 272 ? -38.521 15.824  -16.858 1.00 20.22  ? 272 GLN   A O    1 
ATOM   4129 C  CB   . GLN   A 1 272 ? -38.287 16.322  -13.670 1.00 17.73  ? 272 GLN   A CB   1 
ATOM   4130 C  CG   . GLN   A 1 272 ? -37.764 16.080  -12.274 1.00 17.87  ? 272 GLN   A CG   1 
ATOM   4131 C  CD   . GLN   A 1 272 ? -38.649 15.290  -11.354 1.00 21.40  ? 272 GLN   A CD   1 
ATOM   4132 O  OE1  . GLN   A 1 272 ? -39.790 14.958  -11.653 1.00 24.85  ? 272 GLN   A OE1  1 
ATOM   4133 N  NE2  . GLN   A 1 272 ? -38.115 15.011  -10.147 1.00 22.02  ? 272 GLN   A NE2  1 
ATOM   4134 H  H    . GLN   A 1 272 ? -36.399 15.043  -14.622 1.00 21.30  ? 272 GLN   A H    1 
ATOM   4135 H  HA   . GLN   A 1 272 ? -38.882 14.411  -14.084 1.00 22.54  ? 272 GLN   A HA   1 
ATOM   4136 H  HB2  . GLN   A 1 272 ? -37.693 16.961  -14.094 1.00 21.28  ? 272 GLN   A HB2  1 
ATOM   4137 H  HB3  . GLN   A 1 272 ? -39.175 16.702  -13.583 1.00 21.28  ? 272 GLN   A HB3  1 
ATOM   4138 H  HG2  . GLN   A 1 272 ? -36.926 15.597  -12.346 1.00 21.44  ? 272 GLN   A HG2  1 
ATOM   4139 H  HG3  . GLN   A 1 272 ? -37.616 16.942  -11.854 1.00 21.44  ? 272 GLN   A HG3  1 
ATOM   4140 H  HE21 . GLN   A 1 272 ? -37.322 15.283  -9.954  1.00 26.42  ? 272 GLN   A HE21 1 
ATOM   4141 H  HE22 . GLN   A 1 272 ? -38.568 14.562  -9.570  1.00 26.42  ? 272 GLN   A HE22 1 
ATOM   4142 N  N    . PRO   A 1 273 ? -40.457 15.391  -15.857 1.00 23.31  ? 273 PRO   A N    1 
ATOM   4143 C  CA   . PRO   A 1 273 ? -41.197 15.895  -17.032 1.00 23.94  ? 273 PRO   A CA   1 
ATOM   4144 C  C    . PRO   A 1 273 ? -40.779 17.337  -17.306 1.00 22.16  ? 273 PRO   A C    1 
ATOM   4145 O  O    . PRO   A 1 273 ? -40.622 18.145  -16.388 1.00 24.12  ? 273 PRO   A O    1 
ATOM   4146 C  CB   . PRO   A 1 273 ? -42.677 15.770  -16.627 1.00 26.01  ? 273 PRO   A CB   1 
ATOM   4147 C  CG   . PRO   A 1 273 ? -42.662 14.686  -15.562 1.00 27.46  ? 273 PRO   A CG   1 
ATOM   4148 C  CD   . PRO   A 1 273 ? -41.352 14.923  -14.795 1.00 22.91  ? 273 PRO   A CD   1 
ATOM   4149 H  HA   . PRO   A 1 273 ? -41.055 15.343  -17.816 1.00 28.73  ? 273 PRO   A HA   1 
ATOM   4150 H  HB2  . PRO   A 1 273 ? -43.000 16.612  -16.268 1.00 31.21  ? 273 PRO   A HB2  1 
ATOM   4151 H  HB3  . PRO   A 1 273 ? -43.214 15.507  -17.390 1.00 31.21  ? 273 PRO   A HB3  1 
ATOM   4152 H  HG2  . PRO   A 1 273 ? -43.430 14.781  -14.978 1.00 32.95  ? 273 PRO   A HG2  1 
ATOM   4153 H  HG3  . PRO   A 1 273 ? -42.668 13.810  -15.979 1.00 32.95  ? 273 PRO   A HG3  1 
ATOM   4154 H  HD2  . PRO   A 1 273 ? -41.466 15.599  -14.109 1.00 27.49  ? 273 PRO   A HD2  1 
ATOM   4155 H  HD3  . PRO   A 1 273 ? -41.025 14.100  -14.399 1.00 27.49  ? 273 PRO   A HD3  1 
ATOM   4156 N  N    . ASN   A 1 274 ? -40.528 17.625  -18.565 1.00 24.09  ? 274 ASN   A N    1 
ATOM   4157 C  CA   . ASN   A 1 274 ? -40.187 18.950  -19.069 1.00 26.63  ? 274 ASN   A CA   1 
ATOM   4158 C  C    . ASN   A 1 274 ? -38.732 19.282  -18.793 1.00 20.16  ? 274 ASN   A C    1 
ATOM   4159 O  O    . ASN   A 1 274 ? -38.339 20.419  -19.029 1.00 24.39  ? 274 ASN   A O    1 
ATOM   4160 C  CB   . ASN   A 1 274 ? -41.063 20.072  -18.510 1.00 27.08  ? 274 ASN   A CB   1 
ATOM   4161 C  CG   . ASN   A 1 274 ? -42.525 19.796  -18.702 1.00 34.39  ? 274 ASN   A CG   1 
ATOM   4162 O  OD1  . ASN   A 1 274 ? -42.936 19.427  -19.792 1.00 33.82  ? 274 ASN   A OD1  1 
ATOM   4163 N  ND2  . ASN   A 1 274 ? -43.296 19.914  -17.625 1.00 36.46  ? 274 ASN   A ND2  1 
ATOM   4164 H  H    . ASN   A 1 274 ? -40.549 17.034  -19.189 1.00 28.91  ? 274 ASN   A H    1 
ATOM   4165 H  HA   . ASN   A 1 274 ? -40.332 18.940  -20.028 1.00 31.95  ? 274 ASN   A HA   1 
ATOM   4166 H  HB2  . ASN   A 1 274 ? -40.894 20.164  -17.559 1.00 32.50  ? 274 ASN   A HB2  1 
ATOM   4167 H  HB3  . ASN   A 1 274 ? -40.848 20.901  -18.967 1.00 32.50  ? 274 ASN   A HB3  1 
ATOM   4168 H  HD21 . ASN   A 1 274 ? -42.950 20.139  -16.870 1.00 43.75  ? 274 ASN   A HD21 1 
ATOM   4169 H  HD22 . ASN   A 1 274 ? -44.142 19.767  -17.683 1.00 43.75  ? 274 ASN   A HD22 1 
ATOM   4170 N  N    . TRP   A 1 275 ? -37.934 18.348  -18.284 1.00 20.13  ? 275 TRP   A N    1 
ATOM   4171 C  CA   . TRP   A 1 275 ? -36.510 18.563  -18.097 1.00 16.77  ? 275 TRP   A CA   1 
ATOM   4172 C  C    . TRP   A 1 275 ? -35.709 17.674  -19.036 1.00 17.70  ? 275 TRP   A C    1 
ATOM   4173 O  O    . TRP   A 1 275 ? -36.230 16.808  -19.729 1.00 20.22  ? 275 TRP   A O    1 
ATOM   4174 C  CB   . TRP   A 1 275 ? -36.150 18.251  -16.630 1.00 17.65  ? 275 TRP   A CB   1 
ATOM   4175 C  CG   . TRP   A 1 275 ? -36.530 19.396  -15.720 1.00 17.44  ? 275 TRP   A CG   1 
ATOM   4176 C  CD1  . TRP   A 1 275 ? -37.830 19.707  -15.317 1.00 18.77  ? 275 TRP   A CD1  1 
ATOM   4177 C  CD2  . TRP   A 1 275 ? -35.690 20.340  -15.107 1.00 15.97  ? 275 TRP   A CD2  1 
ATOM   4178 N  NE1  . TRP   A 1 275 ? -37.812 20.802  -14.519 1.00 17.79  ? 275 TRP   A NE1  1 
ATOM   4179 C  CE2  . TRP   A 1 275 ? -36.518 21.228  -14.383 1.00 15.91  ? 275 TRP   A CE2  1 
ATOM   4180 C  CE3  . TRP   A 1 275 ? -34.320 20.579  -15.128 1.00 14.97  ? 275 TRP   A CE3  1 
ATOM   4181 C  CZ2  . TRP   A 1 275 ? -35.986 22.294  -13.629 1.00 15.94  ? 275 TRP   A CZ2  1 
ATOM   4182 C  CZ3  . TRP   A 1 275 ? -33.799 21.657  -14.404 1.00 15.26  ? 275 TRP   A CZ3  1 
ATOM   4183 C  CH2  . TRP   A 1 275 ? -34.634 22.514  -13.686 1.00 14.43  ? 275 TRP   A CH2  1 
ATOM   4184 H  H    . TRP   A 1 275 ? -38.203 17.569  -18.036 1.00 24.15  ? 275 TRP   A H    1 
ATOM   4185 H  HA   . TRP   A 1 275 ? -36.281 19.483  -18.303 1.00 20.13  ? 275 TRP   A HA   1 
ATOM   4186 H  HB2  . TRP   A 1 275 ? -36.630 17.458  -16.343 1.00 21.18  ? 275 TRP   A HB2  1 
ATOM   4187 H  HB3  . TRP   A 1 275 ? -35.194 18.105  -16.558 1.00 21.18  ? 275 TRP   A HB3  1 
ATOM   4188 H  HD1  . TRP   A 1 275 ? -38.594 19.235  -15.560 1.00 22.52  ? 275 TRP   A HD1  1 
ATOM   4189 H  HE1  . TRP   A 1 275 ? -38.500 21.169  -14.157 1.00 21.35  ? 275 TRP   A HE1  1 
ATOM   4190 H  HE3  . TRP   A 1 275 ? -33.755 20.027  -15.619 1.00 17.97  ? 275 TRP   A HE3  1 
ATOM   4191 H  HZ2  . TRP   A 1 275 ? -36.537 22.833  -13.108 1.00 19.13  ? 275 TRP   A HZ2  1 
ATOM   4192 H  HZ3  . TRP   A 1 275 ? -32.881 21.805  -14.402 1.00 18.31  ? 275 TRP   A HZ3  1 
ATOM   4193 H  HH2  . TRP   A 1 275 ? -34.269 23.244  -13.240 1.00 17.31  ? 275 TRP   A HH2  1 
ATOM   4194 N  N    . ASN   A 1 276 ? -34.421 17.941  -19.081 1.00 17.00  ? 276 ASN   A N    1 
ATOM   4195 C  CA   . ASN   A 1 276 ? -33.471 17.144  -19.853 1.00 17.55  ? 276 ASN   A CA   1 
ATOM   4196 C  C    . ASN   A 1 276 ? -32.112 17.347  -19.219 1.00 17.07  ? 276 ASN   A C    1 
ATOM   4197 O  O    . ASN   A 1 276 ? -31.950 18.110  -18.258 1.00 15.61  ? 276 ASN   A O    1 
ATOM   4198 C  CB   . ASN   A 1 276 ? -33.458 17.532  -21.333 1.00 16.66  ? 276 ASN   A CB   1 
ATOM   4199 C  CG   . ASN   A 1 276 ? -33.249 19.009  -21.551 1.00 19.65  ? 276 ASN   A CG   1 
ATOM   4200 O  OD1  . ASN   A 1 276 ? -32.554 19.646  -20.848 1.00 19.35  ? 276 ASN   A OD1  1 
ATOM   4201 N  ND2  . ASN   A 1 276 ? -33.902 19.551  -22.568 1.00 26.38  ? 276 ASN   A ND2  1 
ATOM   4202 H  H    . ASN   A 1 276 ? -34.054 18.597  -18.662 1.00 20.40  ? 276 ASN   A H    1 
ATOM   4203 H  HA   . ASN   A 1 276 ? -33.724 16.209  -19.803 1.00 21.06  ? 276 ASN   A HA   1 
ATOM   4204 H  HB2  . ASN   A 1 276 ? -32.736 17.059  -21.776 1.00 19.99  ? 276 ASN   A HB2  1 
ATOM   4205 H  HB3  . ASN   A 1 276 ? -34.308 17.287  -21.731 1.00 19.99  ? 276 ASN   A HB3  1 
ATOM   4206 H  HD21 . ASN   A 1 276 ? -34.411 19.064  -23.061 1.00 31.65  ? 276 ASN   A HD21 1 
ATOM   4207 H  HD22 . ASN   A 1 276 ? -33.817 20.391  -22.735 1.00 31.65  ? 276 ASN   A HD22 1 
ATOM   4208 N  N    . LEU   A 1 277 ? -31.107 16.656  -19.744 1.00 14.84  ? 277 LEU   A N    1 
ATOM   4209 C  CA   . LEU   A 1 277 ? -29.767 16.723  -19.204 1.00 14.93  ? 277 LEU   A CA   1 
ATOM   4210 C  C    . LEU   A 1 277 ? -29.222 18.143  -19.235 1.00 13.99  ? 277 LEU   A C    1 
ATOM   4211 O  O    . LEU   A 1 277 ? -28.607 18.601  -18.260 1.00 13.80  ? 277 LEU   A O    1 
ATOM   4212 C  CB   . LEU   A 1 277 ? -28.832 15.740  -19.945 1.00 15.59  ? 277 LEU   A CB   1 
ATOM   4213 C  CG   . LEU   A 1 277 ? -27.372 15.833  -19.490 1.00 19.29  ? 277 LEU   A CG   1 
ATOM   4214 C  CD1  . LEU   A 1 277 ? -26.688 14.450  -19.648 1.00 24.07  ? 277 LEU   A CD1  1 
ATOM   4215 C  CD2  . LEU   A 1 277 ? -26.574 16.874  -20.251 1.00 17.38  ? 277 LEU   A CD2  1 
ATOM   4216 H  H    . LEU   A 1 277 ? -31.180 16.134  -20.423 1.00 17.81  ? 277 LEU   A H    1 
ATOM   4217 H  HA   . LEU   A 1 277 ? -29.795 16.444  -18.276 1.00 17.91  ? 277 LEU   A HA   1 
ATOM   4218 H  HB2  . LEU   A 1 277 ? -29.138 14.834  -19.782 1.00 18.71  ? 277 LEU   A HB2  1 
ATOM   4219 H  HB3  . LEU   A 1 277 ? -28.861 15.935  -20.895 1.00 18.71  ? 277 LEU   A HB3  1 
ATOM   4220 H  HG   . LEU   A 1 277 ? -27.377 16.108  -18.559 1.00 23.15  ? 277 LEU   A HG   1 
ATOM   4221 H  HD11 . LEU   A 1 277 ? -25.758 14.524  -19.381 1.00 28.88  ? 277 LEU   A HD11 1 
ATOM   4222 H  HD12 . LEU   A 1 277 ? -27.143 13.805  -19.085 1.00 28.88  ? 277 LEU   A HD12 1 
ATOM   4223 H  HD13 . LEU   A 1 277 ? -26.743 14.174  -20.577 1.00 28.88  ? 277 LEU   A HD13 1 
ATOM   4224 H  HD21 . LEU   A 1 277 ? -25.935 16.424  -20.825 1.00 20.85  ? 277 LEU   A HD21 1 
ATOM   4225 H  HD22 . LEU   A 1 277 ? -27.182 17.408  -20.786 1.00 20.85  ? 277 LEU   A HD22 1 
ATOM   4226 H  HD23 . LEU   A 1 277 ? -26.108 17.441  -19.616 1.00 20.85  ? 277 LEU   A HD23 1 
ATOM   4227 N  N    . ARG   A 1 278 ? -29.426 18.831  -20.368 1.00 14.85  ? 278 ARG   A N    1 
ATOM   4228 C  CA   . ARG   A 1 278 ? -28.861 20.168  -20.485 1.00 15.49  ? 278 ARG   A CA   1 
ATOM   4229 C  C    . ARG   A 1 278 ? -29.421 21.116  -19.437 1.00 14.62  ? 278 ARG   A C    1 
ATOM   4230 O  O    . ARG   A 1 278 ? -28.660 21.885  -18.846 1.00 15.11  ? 278 ARG   A O    1 
ATOM   4231 C  CB   . ARG   A 1 278 ? -29.136 20.719  -21.855 1.00 17.30  ? 278 ARG   A CB   1 
ATOM   4232 C  CG   . ARG   A 1 278 ? -28.180 20.107  -22.901 1.00 20.84  ? 278 ARG   A CG   1 
ATOM   4233 C  CD   . ARG   A 1 278 ? -28.149 20.890  -24.221 1.00 27.52  ? 278 ARG   A CD   1 
ATOM   4234 N  NE   . ARG   A 1 278 ? -27.517 22.186  -24.008 1.00 24.05  ? 278 ARG   A NE   1 
ATOM   4235 C  CZ   . ARG   A 1 278 ? -27.394 23.108  -24.949 1.00 29.95  ? 278 ARG   A CZ   1 
ATOM   4236 N  NH1  . ARG   A 1 278 ? -27.776 22.864  -26.199 1.00 27.95  ? 278 ARG   A NH1  1 
ATOM   4237 N  NH2  . ARG   A 1 278 ? -26.867 24.287  -24.631 1.00 28.81  ? 278 ARG   A NH2  1 
ATOM   4238 H  H    . ARG   A 1 278 ? -29.870 18.553  -21.050 1.00 17.82  ? 278 ARG   A H    1 
ATOM   4239 H  HA   . ARG   A 1 278 ? -27.902 20.101  -20.353 1.00 18.59  ? 278 ARG   A HA   1 
ATOM   4240 H  HB2  . ARG   A 1 278 ? -30.048 20.509  -22.110 1.00 20.76  ? 278 ARG   A HB2  1 
ATOM   4241 H  HB3  . ARG   A 1 278 ? -29.007 21.681  -21.847 1.00 20.76  ? 278 ARG   A HB3  1 
ATOM   4242 H  HG2  . ARG   A 1 278 ? -27.281 20.097  -22.538 1.00 25.01  ? 278 ARG   A HG2  1 
ATOM   4243 H  HG3  . ARG   A 1 278 ? -28.468 19.202  -23.098 1.00 25.01  ? 278 ARG   A HG3  1 
ATOM   4244 H  HD2  . ARG   A 1 278 ? -27.638 20.398  -24.882 1.00 33.02  ? 278 ARG   A HD2  1 
ATOM   4245 H  HD3  . ARG   A 1 278 ? -29.054 21.033  -24.539 1.00 33.02  ? 278 ARG   A HD3  1 
ATOM   4246 H  HE   . ARG   A 1 278 ? -27.205 22.361  -23.226 1.00 28.85  ? 278 ARG   A HE   1 
ATOM   4247 H  HH11 . ARG   A 1 278 ? -27.691 23.472  -26.801 1.00 33.54  ? 278 ARG   A HH11 1 
ATOM   4248 H  HH12 . ARG   A 1 278 ? -28.107 22.098  -26.406 1.00 33.54  ? 278 ARG   A HH12 1 
ATOM   4249 H  HH21 . ARG   A 1 278 ? -26.611 24.440  -23.824 1.00 34.57  ? 278 ARG   A HH21 1 
ATOM   4250 H  HH22 . ARG   A 1 278 ? -26.781 24.896  -25.232 1.00 34.57  ? 278 ARG   A HH22 1 
ATOM   4251 N  N    . MET   A 1 279 ? -30.726 21.095  -19.206 1.00 15.40  ? 279 MET   A N    1 
ATOM   4252 C  CA   A MET   A 1 279 ? -31.297 21.987  -18.206 0.56 16.53  ? 279 MET   A CA   1 
ATOM   4253 C  CA   B MET   A 1 279 ? -31.290 21.987  -18.204 0.44 16.62  ? 279 MET   A CA   1 
ATOM   4254 C  C    . MET   A 1 279 ? -30.751 21.647  -16.826 1.00 14.45  ? 279 MET   A C    1 
ATOM   4255 O  O    . MET   A 1 279 ? -30.466 22.535  -16.007 1.00 14.14  ? 279 MET   A O    1 
ATOM   4256 C  CB   A MET   A 1 279 ? -32.821 21.837  -18.210 0.56 17.08  ? 279 MET   A CB   1 
ATOM   4257 C  CB   B MET   A 1 279 ? -32.809 21.861  -18.162 0.44 17.26  ? 279 MET   A CB   1 
ATOM   4258 C  CG   A MET   A 1 279 ? -33.473 22.440  -19.421 0.56 17.16  ? 279 MET   A CG   1 
ATOM   4259 C  CG   B MET   A 1 279 ? -33.510 22.435  -19.313 0.44 17.26  ? 279 MET   A CG   1 
ATOM   4260 S  SD   A MET   A 1 279 ? -35.242 22.074  -19.532 0.56 22.03  ? 279 MET   A SD   1 
ATOM   4261 S  SD   B MET   A 1 279 ? -35.271 22.054  -19.135 0.44 20.15  ? 279 MET   A SD   1 
ATOM   4262 C  CE   A MET   A 1 279 ? -35.724 22.915  -18.020 0.56 16.19  ? 279 MET   A CE   1 
ATOM   4263 C  CE   B MET   A 1 279 ? -35.778 22.913  -20.576 0.44 16.26  ? 279 MET   A CE   1 
ATOM   4264 H  H    A MET   A 1 279 ? -31.292 20.585  -19.605 0.56 18.48  ? 279 MET   A H    1 
ATOM   4265 H  H    B MET   A 1 279 ? -31.294 20.586  -19.604 0.44 18.48  ? 279 MET   A H    1 
ATOM   4266 H  HA   A MET   A 1 279 ? -31.075 22.905  -18.427 0.56 19.84  ? 279 MET   A HA   1 
ATOM   4267 H  HA   B MET   A 1 279 ? -31.058 22.896  -18.454 0.44 19.94  ? 279 MET   A HA   1 
ATOM   4268 H  HB2  A MET   A 1 279 ? -33.043 20.893  -18.191 0.56 20.50  ? 279 MET   A HB2  1 
ATOM   4269 H  HB2  B MET   A 1 279 ? -33.038 20.920  -18.122 0.44 20.72  ? 279 MET   A HB2  1 
ATOM   4270 H  HB3  A MET   A 1 279 ? -33.181 22.279  -17.426 0.56 20.50  ? 279 MET   A HB3  1 
ATOM   4271 H  HB3  B MET   A 1 279 ? -33.133 22.316  -17.369 0.44 20.72  ? 279 MET   A HB3  1 
ATOM   4272 H  HG2  A MET   A 1 279 ? -33.369 23.404  -19.387 0.56 20.60  ? 279 MET   A HG2  1 
ATOM   4273 H  HG2  B MET   A 1 279 ? -33.391 23.398  -19.333 0.44 20.72  ? 279 MET   A HG2  1 
ATOM   4274 H  HG3  A MET   A 1 279 ? -33.045 22.089  -20.218 0.56 20.60  ? 279 MET   A HG3  1 
ATOM   4275 H  HG3  B MET   A 1 279 ? -33.179 22.043  -20.137 0.44 20.72  ? 279 MET   A HG3  1 
ATOM   4276 H  HE1  A MET   A 1 279 ? -36.692 22.918  -17.955 0.56 19.43  ? 279 MET   A HE1  1 
ATOM   4277 H  HE1  B MET   A 1 279 ? -36.730 22.779  -20.704 0.44 19.51  ? 279 MET   A HE1  1 
ATOM   4278 H  HE2  A MET   A 1 279 ? -35.343 22.445  -17.262 0.56 19.43  ? 279 MET   A HE2  1 
ATOM   4279 H  HE2  B MET   A 1 279 ? -35.589 23.857  -20.463 0.44 19.51  ? 279 MET   A HE2  1 
ATOM   4280 H  HE3  A MET   A 1 279 ? -35.391 23.826  -18.046 0.56 19.43  ? 279 MET   A HE3  1 
ATOM   4281 H  HE3  B MET   A 1 279 ? -35.289 22.566  -21.339 0.44 19.51  ? 279 MET   A HE3  1 
ATOM   4282 N  N    . ALA   A 1 280 ? -30.659 20.356  -16.489 1.00 13.94  ? 280 ALA   A N    1 
ATOM   4283 C  CA   . ALA   A 1 280 ? -30.140 19.945  -15.208 1.00 14.63  ? 280 ALA   A CA   1 
ATOM   4284 C  C    . ALA   A 1 280 ? -28.702 20.388  -15.044 1.00 12.87  ? 280 ALA   A C    1 
ATOM   4285 O  O    . ALA   A 1 280 ? -28.289 20.890  -13.990 1.00 13.38  ? 280 ALA   A O    1 
ATOM   4286 C  CB   . ALA   A 1 280 ? -30.236 18.436  -15.064 1.00 13.44  ? 280 ALA   A CB   1 
ATOM   4287 H  H    . ALA   A 1 280 ? -30.895 19.702  -16.995 1.00 16.73  ? 280 ALA   A H    1 
ATOM   4288 H  HA   . ALA   A 1 280 ? -30.674 20.353  -14.508 1.00 17.56  ? 280 ALA   A HA   1 
ATOM   4289 H  HB1  . ALA   A 1 280 ? -29.849 18.174  -14.214 1.00 16.12  ? 280 ALA   A HB1  1 
ATOM   4290 H  HB2  . ALA   A 1 280 ? -31.170 18.174  -15.097 1.00 16.12  ? 280 ALA   A HB2  1 
ATOM   4291 H  HB3  . ALA   A 1 280 ? -29.750 18.017  -15.792 1.00 16.12  ? 280 ALA   A HB3  1 
ATOM   4292 N  N    . PHE   A 1 281 ? -27.895 20.227  -16.104 1.00 12.11  ? 281 PHE   A N    1 
ATOM   4293 C  CA   . PHE   A 1 281 ? -26.498 20.642  -15.990 1.00 12.20  ? 281 PHE   A CA   1 
ATOM   4294 C  C    . PHE   A 1 281 ? -26.395 22.160  -15.932 1.00 11.81  ? 281 PHE   A C    1 
ATOM   4295 O  O    . PHE   A 1 281 ? -25.511 22.685  -15.214 1.00 12.68  ? 281 PHE   A O    1 
ATOM   4296 C  CB   . PHE   A 1 281 ? -25.676 20.045  -17.158 1.00 11.85  ? 281 PHE   A CB   1 
ATOM   4297 C  CG   . PHE   A 1 281 ? -24.176 20.080  -16.947 1.00 11.96  ? 281 PHE   A CG   1 
ATOM   4298 C  CD1  . PHE   A 1 281 ? -23.610 19.483  -15.870 1.00 14.18  ? 281 PHE   A CD1  1 
ATOM   4299 C  CD2  . PHE   A 1 281 ? -23.358 20.732  -17.844 1.00 13.27  ? 281 PHE   A CD2  1 
ATOM   4300 C  CE1  . PHE   A 1 281 ? -22.208 19.485  -15.633 1.00 12.55  ? 281 PHE   A CE1  1 
ATOM   4301 C  CE2  . PHE   A 1 281 ? -21.953 20.725  -17.617 1.00 13.12  ? 281 PHE   A CE2  1 
ATOM   4302 C  CZ   . PHE   A 1 281 ? -21.438 20.121  -16.560 1.00 13.32  ? 281 PHE   A CZ   1 
ATOM   4303 H  H    . PHE   A 1 281 ? -28.124 19.896  -16.864 1.00 14.54  ? 281 PHE   A H    1 
ATOM   4304 H  HA   . PHE   A 1 281 ? -26.108 20.293  -15.173 1.00 14.64  ? 281 PHE   A HA   1 
ATOM   4305 H  HB2  . PHE   A 1 281 ? -25.935 19.118  -17.277 1.00 14.22  ? 281 PHE   A HB2  1 
ATOM   4306 H  HB3  . PHE   A 1 281 ? -25.871 20.550  -17.963 1.00 14.22  ? 281 PHE   A HB3  1 
ATOM   4307 H  HD1  . PHE   A 1 281 ? -24.164 19.052  -15.259 1.00 17.01  ? 281 PHE   A HD1  1 
ATOM   4308 H  HD2  . PHE   A 1 281 ? -23.717 21.167  -18.583 1.00 15.92  ? 281 PHE   A HD2  1 
ATOM   4309 H  HE1  . PHE   A 1 281 ? -21.837 19.075  -14.886 1.00 15.06  ? 281 PHE   A HE1  1 
ATOM   4310 H  HE2  . PHE   A 1 281 ? -21.390 21.153  -18.221 1.00 15.75  ? 281 PHE   A HE2  1 
ATOM   4311 H  HZ   . PHE   A 1 281 ? -20.515 20.130  -16.445 1.00 15.99  ? 281 PHE   A HZ   1 
ATOM   4312 N  N    . ASP   A 1 282 ? -27.290 22.895  -16.600 1.00 12.57  ? 282 ASP   A N    1 
ATOM   4313 C  CA   . ASP   A 1 282 ? -27.274 24.354  -16.496 1.00 14.08  ? 282 ASP   A CA   1 
ATOM   4314 C  C    . ASP   A 1 282 ? -27.425 24.769  -15.024 1.00 12.85  ? 282 ASP   A C    1 
ATOM   4315 O  O    . ASP   A 1 282 ? -26.771 25.697  -14.545 1.00 13.48  ? 282 ASP   A O    1 
ATOM   4316 C  CB   . ASP   A 1 282 ? -28.443 24.972  -17.217 1.00 14.20  ? 282 ASP   A CB   1 
ATOM   4317 C  CG   . ASP   A 1 282 ? -28.424 24.820  -18.714 1.00 17.78  ? 282 ASP   A CG   1 
ATOM   4318 O  OD1  . ASP   A 1 282 ? -27.359 24.572  -19.344 1.00 17.52  ? 282 ASP   A OD1  1 
ATOM   4319 O  OD2  . ASP   A 1 282 ? -29.537 25.025  -19.329 1.00 17.63  ? 282 ASP   A OD2  1 
ATOM   4320 H  H    . ASP   A 1 282 ? -27.905 22.579  -17.111 1.00 15.09  ? 282 ASP   A H    1 
ATOM   4321 H  HA   . ASP   A 1 282 ? -26.443 24.664  -16.889 1.00 16.89  ? 282 ASP   A HA   1 
ATOM   4322 H  HB2  . ASP   A 1 282 ? -29.257 24.555  -16.894 1.00 17.04  ? 282 ASP   A HB2  1 
ATOM   4323 H  HB3  . ASP   A 1 282 ? -28.456 25.922  -17.022 1.00 17.04  ? 282 ASP   A HB3  1 
ATOM   4324 N  N    . VAL   A 1 283 ? -28.293 24.095  -14.284 1.00 12.35  ? 283 VAL   A N    1 
ATOM   4325 C  CA   . VAL   A 1 283 ? -28.487 24.428  -12.872 1.00 13.10  ? 283 VAL   A CA   1 
ATOM   4326 C  C    . VAL   A 1 283 ? -27.218 24.155  -12.072 1.00 11.71  ? 283 VAL   A C    1 
ATOM   4327 O  O    . VAL   A 1 283 ? -26.820 24.964  -11.233 1.00 12.84  ? 283 VAL   A O    1 
ATOM   4328 C  CB   . VAL   A 1 283 ? -29.680 23.623  -12.299 1.00 12.94  ? 283 VAL   A CB   1 
ATOM   4329 C  CG1  . VAL   A 1 283 ? -29.826 23.744  -10.779 1.00 14.11  ? 283 VAL   A CG1  1 
ATOM   4330 C  CG2  . VAL   A 1 283 ? -30.957 24.071  -12.941 1.00 14.76  ? 283 VAL   A CG2  1 
ATOM   4331 H  H    . VAL   A 1 283 ? -28.781 23.445  -14.568 1.00 14.82  ? 283 VAL   A H    1 
ATOM   4332 H  HA   . VAL   A 1 283 ? -28.684 25.375  -12.807 1.00 15.72  ? 283 VAL   A HA   1 
ATOM   4333 H  HB   . VAL   A 1 283 ? -29.502 22.690  -12.497 1.00 15.52  ? 283 VAL   A HB   1 
ATOM   4334 H  HG11 . VAL   A 1 283 ? -30.683 23.374  -10.514 1.00 16.93  ? 283 VAL   A HG11 1 
ATOM   4335 H  HG12 . VAL   A 1 283 ? -29.107 23.252  -10.353 1.00 16.93  ? 283 VAL   A HG12 1 
ATOM   4336 H  HG13 . VAL   A 1 283 ? -29.779 24.680  -10.531 1.00 16.93  ? 283 VAL   A HG13 1 
ATOM   4337 H  HG21 . VAL   A 1 283 ? -31.688 23.531  -12.602 1.00 17.71  ? 283 VAL   A HG21 1 
ATOM   4338 H  HG22 . VAL   A 1 283 ? -31.108 25.005  -12.726 1.00 17.71  ? 283 VAL   A HG22 1 
ATOM   4339 H  HG23 . VAL   A 1 283 ? -30.883 23.961  -13.902 1.00 17.71  ? 283 VAL   A HG23 1 
ATOM   4340 N  N    . MET   A 1 284 ? -26.626 22.973  -12.251 1.00 11.50  ? 284 MET   A N    1 
ATOM   4341 C  CA   . MET   A 1 284 ? -25.400 22.594  -11.548 1.00 11.13  ? 284 MET   A CA   1 
ATOM   4342 C  C    . MET   A 1 284 ? -24.242 23.493  -11.870 1.00 11.43  ? 284 MET   A C    1 
ATOM   4343 O  O    . MET   A 1 284 ? -23.511 23.882  -10.965 1.00 12.05  ? 284 MET   A O    1 
ATOM   4344 C  CB   . MET   A 1 284 ? -25.086 21.110  -11.844 1.00 12.87  ? 284 MET   A CB   1 
ATOM   4345 C  CG   . MET   A 1 284 ? -26.198 20.162  -11.477 1.00 12.87  ? 284 MET   A CG   1 
ATOM   4346 S  SD   . MET   A 1 284 ? -26.537 20.138  -9.677  1.00 13.83  ? 284 MET   A SD   1 
ATOM   4347 C  CE   . MET   A 1 284 ? -27.523 18.623  -9.558  1.00 15.94  ? 284 MET   A CE   1 
ATOM   4348 H  H    . MET   A 1 284 ? -26.918 22.363  -12.782 1.00 13.80  ? 284 MET   A H    1 
ATOM   4349 H  HA   . MET   A 1 284 ? -25.550 22.682  -10.594 1.00 13.36  ? 284 MET   A HA   1 
ATOM   4350 H  HB2  . MET   A 1 284 ? -24.917 21.012  -12.794 1.00 15.45  ? 284 MET   A HB2  1 
ATOM   4351 H  HB3  . MET   A 1 284 ? -24.299 20.852  -11.339 1.00 15.45  ? 284 MET   A HB3  1 
ATOM   4352 H  HG2  . MET   A 1 284 ? -27.010 20.435  -11.932 1.00 15.44  ? 284 MET   A HG2  1 
ATOM   4353 H  HG3  . MET   A 1 284 ? -25.951 19.264  -11.748 1.00 15.44  ? 284 MET   A HG3  1 
ATOM   4354 H  HE1  . MET   A 1 284 ? -27.796 18.495  -8.636  1.00 19.12  ? 284 MET   A HE1  1 
ATOM   4355 H  HE2  . MET   A 1 284 ? -28.305 18.709  -10.126 1.00 19.12  ? 284 MET   A HE2  1 
ATOM   4356 H  HE3  . MET   A 1 284 ? -26.984 17.871  -9.850  1.00 19.12  ? 284 MET   A HE3  1 
ATOM   4357 N  N    . VAL   A 1 285 ? -24.060 23.823  -13.148 1.00 12.43  ? 285 VAL   A N    1 
ATOM   4358 C  CA   . VAL   A 1 285 ? -22.966 24.711  -13.522 1.00 11.79  ? 285 VAL   A CA   1 
ATOM   4359 C  C    . VAL   A 1 285 ? -23.146 26.074  -12.860 1.00 11.80  ? 285 VAL   A C    1 
ATOM   4360 O  O    . VAL   A 1 285 ? -22.203 26.641  -12.303 1.00 12.77  ? 285 VAL   A O    1 
ATOM   4361 C  CB   . VAL   A 1 285 ? -22.827 24.827  -15.046 1.00 12.53  ? 285 VAL   A CB   1 
ATOM   4362 C  CG1  . VAL   A 1 285 ? -21.889 25.942  -15.448 1.00 13.95  ? 285 VAL   A CG1  1 
ATOM   4363 C  CG2  . VAL   A 1 285 ? -22.391 23.482  -15.628 1.00 13.90  ? 285 VAL   A CG2  1 
ATOM   4364 H  H    . VAL   A 1 285 ? -24.546 23.550  -13.803 1.00 14.91  ? 285 VAL   A H    1 
ATOM   4365 H  HA   . VAL   A 1 285 ? -22.140 24.323  -13.195 1.00 14.15  ? 285 VAL   A HA   1 
ATOM   4366 H  HB   . VAL   A 1 285 ? -23.691 25.057  -15.421 1.00 15.04  ? 285 VAL   A HB   1 
ATOM   4367 H  HG11 . VAL   A 1 285 ? -21.506 25.736  -16.315 1.00 16.75  ? 285 VAL   A HG11 1 
ATOM   4368 H  HG12 . VAL   A 1 285 ? -22.389 26.772  -15.496 1.00 16.75  ? 285 VAL   A HG12 1 
ATOM   4369 H  HG13 . VAL   A 1 285 ? -21.185 26.018  -14.785 1.00 16.75  ? 285 VAL   A HG13 1 
ATOM   4370 H  HG21 . VAL   A 1 285 ? -22.394 23.541  -16.596 1.00 16.69  ? 285 VAL   A HG21 1 
ATOM   4371 H  HG22 . VAL   A 1 285 ? -21.497 23.276  -15.312 1.00 16.69  ? 285 VAL   A HG22 1 
ATOM   4372 H  HG23 . VAL   A 1 285 ? -23.012 22.796  -15.337 1.00 16.69  ? 285 VAL   A HG23 1 
ATOM   4373 N  N    . LYS   A 1 286 ? -24.356 26.637  -12.927 1.00 11.61  ? 286 LYS   A N    1 
ATOM   4374 C  CA   . LYS   A 1 286 ? -24.606 27.935  -12.343 1.00 13.49  ? 286 LYS   A CA   1 
ATOM   4375 C  C    . LYS   A 1 286 ? -24.425 27.903  -10.845 1.00 13.32  ? 286 LYS   A C    1 
ATOM   4376 O  O    . LYS   A 1 286 ? -23.887 28.859  -10.261 1.00 13.82  ? 286 LYS   A O    1 
ATOM   4377 C  CB   . LYS   A 1 286 ? -25.990 28.448  -12.753 1.00 14.20  ? 286 LYS   A CB   1 
ATOM   4378 C  CG   . LYS   A 1 286 ? -26.252 29.837  -12.219 1.00 17.76  ? 286 LYS   A CG   1 
ATOM   4379 C  CD   . LYS   A 1 286 ? -27.527 30.456  -12.811 1.00 22.54  ? 286 LYS   A CD   1 
ATOM   4380 C  CE   . LYS   A 1 286 ? -27.361 30.991  -14.222 1.00 26.30  ? 286 LYS   A CE   1 
ATOM   4381 N  NZ   . LYS   A 1 286 ? -26.281 32.012  -14.333 1.00 34.12  ? 286 LYS   A NZ   1 
ATOM   4382 H  H    . LYS   A 1 286 ? -25.042 26.282  -13.307 1.00 13.93  ? 286 LYS   A H    1 
ATOM   4383 H  HA   . LYS   A 1 286 ? -23.963 28.572  -12.692 1.00 16.18  ? 286 LYS   A HA   1 
ATOM   4384 H  HB2  . LYS   A 1 286 ? -26.047 28.478  -13.721 1.00 17.04  ? 286 LYS   A HB2  1 
ATOM   4385 H  HB3  . LYS   A 1 286 ? -26.669 27.853  -12.399 1.00 17.04  ? 286 LYS   A HB3  1 
ATOM   4386 H  HG2  . LYS   A 1 286 ? -26.357 29.793  -11.256 1.00 21.31  ? 286 LYS   A HG2  1 
ATOM   4387 H  HG3  . LYS   A 1 286 ? -25.504 30.411  -12.446 1.00 21.31  ? 286 LYS   A HG3  1 
ATOM   4388 H  HD2  . LYS   A 1 286 ? -28.221 29.779  -12.834 1.00 27.04  ? 286 LYS   A HD2  1 
ATOM   4389 H  HD3  . LYS   A 1 286 ? -27.804 31.196  -12.248 1.00 27.04  ? 286 LYS   A HD3  1 
ATOM   4390 H  HE2  . LYS   A 1 286 ? -27.140 30.255  -14.814 1.00 31.56  ? 286 LYS   A HE2  1 
ATOM   4391 H  HE3  . LYS   A 1 286 ? -28.193 31.404  -14.502 1.00 31.56  ? 286 LYS   A HE3  1 
ATOM   4392 H  HZ1  . LYS   A 1 286 ? -25.493 31.644  -14.145 1.00 40.95  ? 286 LYS   A HZ1  1 
ATOM   4393 H  HZ2  . LYS   A 1 286 ? -26.256 32.341  -15.160 1.00 40.95  ? 286 LYS   A HZ2  1 
ATOM   4394 H  HZ3  . LYS   A 1 286 ? -26.432 32.679  -13.763 1.00 40.95  ? 286 LYS   A HZ3  1 
ATOM   4395 N  N    . ALA   A 1 287 ? -24.889 26.851  -10.192 1.00 12.92  ? 287 ALA   A N    1 
ATOM   4396 C  CA   . ALA   A 1 287 ? -24.655 26.717  -8.753  1.00 12.05  ? 287 ALA   A CA   1 
ATOM   4397 C  C    . ALA   A 1 287 ? -23.176 26.646  -8.439  1.00 12.53  ? 287 ALA   A C    1 
ATOM   4398 O  O    . ALA   A 1 287 ? -22.701 27.325  -7.520  1.00 13.13  ? 287 ALA   A O    1 
ATOM   4399 C  CB   . ALA   A 1 287 ? -25.407 25.513  -8.223  1.00 13.95  ? 287 ALA   A CB   1 
ATOM   4400 H  H    . ALA   A 1 287 ? -25.336 26.208  -10.546 1.00 15.50  ? 287 ALA   A H    1 
ATOM   4401 H  HA   . ALA   A 1 287 ? -25.002 27.498  -8.295  1.00 14.46  ? 287 ALA   A HA   1 
ATOM   4402 H  HB1  . ALA   A 1 287 ? -25.267 25.451  -7.266  1.00 16.74  ? 287 ALA   A HB1  1 
ATOM   4403 H  HB2  . ALA   A 1 287 ? -26.352 25.622  -8.413  1.00 16.74  ? 287 ALA   A HB2  1 
ATOM   4404 H  HB3  . ALA   A 1 287 ? -25.071 24.715  -8.660  1.00 16.74  ? 287 ALA   A HB3  1 
ATOM   4405 N  N    . ASN   A 1 288 ? -22.400 25.892  -9.227  1.00 11.97  ? 288 ASN   A N    1 
ATOM   4406 C  CA   . ASN   A 1 288 ? -20.958 25.815  -8.980  1.00 11.59  ? 288 ASN   A CA   1 
ATOM   4407 C  C    . ASN   A 1 288 ? -20.326 27.194  -9.148  1.00 13.37  ? 288 ASN   A C    1 
ATOM   4408 O  O    . ASN   A 1 288 ? -19.486 27.611  -8.340  1.00 14.09  ? 288 ASN   A O    1 
ATOM   4409 C  CB   . ASN   A 1 288 ? -20.414 24.775  -9.956  1.00 11.87  ? 288 ASN   A CB   1 
ATOM   4410 C  CG   . ASN   A 1 288 ? -19.067 24.199  -9.554  1.00 13.24  ? 288 ASN   A CG   1 
ATOM   4411 O  OD1  . ASN   A 1 288 ? -18.256 24.827  -8.851  1.00 13.79  ? 288 ASN   A OD1  1 
ATOM   4412 N  ND2  . ASN   A 1 288 ? -18.775 23.014  -10.069 1.00 12.45  ? 288 ASN   A ND2  1 
ATOM   4413 H  H    . ASN   A 1 288 ? -22.678 25.426  -9.894  1.00 14.36  ? 288 ASN   A H    1 
ATOM   4414 H  HA   . ASN   A 1 288 ? -20.738 25.534  -8.079  1.00 13.91  ? 288 ASN   A HA   1 
ATOM   4415 H  HB2  . ASN   A 1 288 ? -21.045 24.040  -10.011 1.00 14.25  ? 288 ASN   A HB2  1 
ATOM   4416 H  HB3  . ASN   A 1 288 ? -20.310 25.189  -10.827 1.00 14.25  ? 288 ASN   A HB3  1 
ATOM   4417 H  HD21 . ASN   A 1 288 ? -18.026 22.636  -9.879  1.00 14.94  ? 288 ASN   A HD21 1 
ATOM   4418 H  HD22 . ASN   A 1 288 ? -19.334 22.623  -10.593 1.00 14.94  ? 288 ASN   A HD22 1 
ATOM   4419 N  N    . MET   A 1 289 ? -20.753 27.938  -10.150 1.00 12.72  ? 289 MET   A N    1 
ATOM   4420 C  CA   A MET   A 1 289 ? -20.129 29.228  -10.413 0.15 13.90  ? 289 MET   A CA   1 
ATOM   4421 C  CA   B MET   A 1 289 ? -20.138 29.229  -10.416 0.42 13.89  ? 289 MET   A CA   1 
ATOM   4422 C  CA   C MET   A 1 289 ? -20.127 29.229  -10.406 0.43 13.90  ? 289 MET   A CA   1 
ATOM   4423 C  C    . MET   A 1 289 ? -20.544 30.284  -9.386  1.00 14.92  ? 289 MET   A C    1 
ATOM   4424 O  O    . MET   A 1 289 ? -19.739 31.146  -9.023  1.00 16.88  ? 289 MET   A O    1 
ATOM   4425 C  CB   A MET   A 1 289 ? -20.475 29.671  -11.843 0.15 15.79  ? 289 MET   A CB   1 
ATOM   4426 C  CB   B MET   A 1 289 ? -20.575 29.735  -11.792 0.42 15.74  ? 289 MET   A CB   1 
ATOM   4427 C  CB   C MET   A 1 289 ? -20.518 29.747  -11.785 0.43 15.75  ? 289 MET   A CB   1 
ATOM   4428 C  CG   A MET   A 1 289 ? -19.860 28.758  -12.913 0.15 15.84  ? 289 MET   A CG   1 
ATOM   4429 C  CG   B MET   A 1 289 ? -20.080 28.933  -12.934 0.42 15.30  ? 289 MET   A CG   1 
ATOM   4430 C  CG   C MET   A 1 289 ? -20.027 28.941  -12.917 0.43 15.37  ? 289 MET   A CG   1 
ATOM   4431 S  SD   A MET   A 1 289 ? -20.209 29.064  -14.668 0.15 18.46  ? 289 MET   A SD   1 
ATOM   4432 S  SD   B MET   A 1 289 ? -20.731 29.408  -14.540 0.42 19.73  ? 289 MET   A SD   1 
ATOM   4433 S  SD   C MET   A 1 289 ? -20.495 29.498  -14.565 0.43 19.30  ? 289 MET   A SD   1 
ATOM   4434 C  CE   A MET   A 1 289 ? -21.569 30.213  -14.520 0.15 14.47  ? 289 MET   A CE   1 
ATOM   4435 C  CE   B MET   A 1 289 ? -19.842 30.945  -14.767 0.42 17.85  ? 289 MET   A CE   1 
ATOM   4436 C  CE   C MET   A 1 289 ? -22.222 29.699  -14.388 0.43 11.66  ? 289 MET   A CE   1 
ATOM   4437 H  H    A MET   A 1 289 ? -21.392 27.728  -10.686 0.15 15.26  ? 289 MET   A H    1 
ATOM   4438 H  H    B MET   A 1 289 ? -21.390 27.725  -10.687 0.42 15.26  ? 289 MET   A H    1 
ATOM   4439 H  HA   A MET   A 1 289 ? -19.165 29.131  -10.352 0.15 16.68  ? 289 MET   A HA   1 
ATOM   4440 H  HA   B MET   A 1 289 ? -19.177 29.098  -10.394 0.42 16.66  ? 289 MET   A HA   1 
ATOM   4441 H  HB2  A MET   A 1 289 ? -21.438 29.656  -11.954 0.15 18.95  ? 289 MET   A HB2  1 
ATOM   4442 H  HB2  B MET   A 1 289 ? -21.544 29.729  -11.829 0.42 18.89  ? 289 MET   A HB2  1 
ATOM   4443 H  HB2  C MET   A 1 289 ? -21.486 29.767  -11.842 0.43 18.90  ? 289 MET   A HB2  1 
ATOM   4444 H  HB3  A MET   A 1 289 ? -20.138 30.569  -11.986 0.15 18.95  ? 289 MET   A HB3  1 
ATOM   4445 H  HB3  B MET   A 1 289 ? -20.244 30.640  -11.906 0.42 18.89  ? 289 MET   A HB3  1 
ATOM   4446 H  HB3  C MET   A 1 289 ? -20.161 30.642  -11.890 0.43 18.90  ? 289 MET   A HB3  1 
ATOM   4447 H  HG2  A MET   A 1 289 ? -18.896 28.809  -12.817 0.15 19.00  ? 289 MET   A HG2  1 
ATOM   4448 H  HG2  B MET   A 1 289 ? -19.115 29.021  -12.975 0.42 18.37  ? 289 MET   A HG2  1 
ATOM   4449 H  HG2  C MET   A 1 289 ? -19.058 28.935  -12.885 0.43 18.44  ? 289 MET   A HG2  1 
ATOM   4450 H  HG3  A MET   A 1 289 ? -20.164 27.855  -12.731 0.15 19.00  ? 289 MET   A HG3  1 
ATOM   4451 H  HG3  B MET   A 1 289 ? -20.323 28.006  -12.785 0.42 18.37  ? 289 MET   A HG3  1 
ATOM   4452 H  HG3  C MET   A 1 289 ? -20.368 28.038  -12.815 0.43 18.44  ? 289 MET   A HG3  1 
ATOM   4453 H  HE1  A MET   A 1 289 ? -21.915 30.409  -15.405 0.15 17.36  ? 289 MET   A HE1  1 
ATOM   4454 H  HE1  B MET   A 1 289 ? -20.057 31.307  -15.641 0.42 21.42  ? 289 MET   A HE1  1 
ATOM   4455 H  HE1  C MET   A 1 289 ? -22.524 30.387  -15.001 0.43 14.00  ? 289 MET   A HE1  1 
ATOM   4456 H  HE2  A MET   A 1 289 ? -22.264 29.812  -13.975 0.15 17.36  ? 289 MET   A HE2  1 
ATOM   4457 H  HE2  B MET   A 1 289 ? -20.110 31.570  -14.075 0.42 21.42  ? 289 MET   A HE2  1 
ATOM   4458 H  HE2  C MET   A 1 289 ? -22.660 28.858  -14.592 0.43 14.00  ? 289 MET   A HE2  1 
ATOM   4459 H  HE3  A MET   A 1 289 ? -21.250 31.028  -14.102 0.15 17.36  ? 289 MET   A HE3  1 
ATOM   4460 H  HE3  B MET   A 1 289 ? -18.890 30.771  -14.706 0.42 21.42  ? 289 MET   A HE3  1 
ATOM   4461 H  HE3  C MET   A 1 289 ? -22.417 29.960  -13.474 0.43 14.00  ? 289 MET   A HE3  1 
ATOM   4462 N  N    . ASP   A 1 290 ? -21.825 30.277  -8.938  1.00 14.64  ? 290 ASP   A N    1 
ATOM   4463 C  CA   . ASP   A 1 290 ? -22.350 31.445  -8.264  1.00 15.58  ? 290 ASP   A CA   1 
ATOM   4464 C  C    . ASP   A 1 290 ? -22.828 31.236  -6.836  1.00 15.39  ? 290 ASP   A C    1 
ATOM   4465 O  O    . ASP   A 1 290 ? -23.018 32.232  -6.124  1.00 18.97  ? 290 ASP   A O    1 
ATOM   4466 C  CB   . ASP   A 1 290 ? -23.543 32.016  -9.071  1.00 17.62  ? 290 ASP   A CB   1 
ATOM   4467 C  CG   . ASP   A 1 290 ? -23.163 32.559  -10.433 1.00 25.20  ? 290 ASP   A CG   1 
ATOM   4468 O  OD1  . ASP   A 1 290 ? -21.984 32.821  -10.698 1.00 27.51  ? 290 ASP   A OD1  1 
ATOM   4469 O  OD2  . ASP   A 1 290 ? -24.092 32.802  -11.250 1.00 30.20  ? 290 ASP   A OD2  1 
ATOM   4470 H  H    . ASP   A 1 290 ? -22.374 29.620  -9.020  1.00 17.57  ? 290 ASP   A H    1 
ATOM   4471 H  HA   . ASP   A 1 290 ? -21.633 32.097  -8.222  1.00 18.70  ? 290 ASP   A HA   1 
ATOM   4472 H  HB2  . ASP   A 1 290 ? -24.194 31.309  -9.207  1.00 21.15  ? 290 ASP   A HB2  1 
ATOM   4473 H  HB3  . ASP   A 1 290 ? -23.943 32.741  -8.566  1.00 21.15  ? 290 ASP   A HB3  1 
ATOM   4474 N  N    . TYR   A 1 291 ? -23.063 30.010  -6.393  1.00 14.23  ? 291 TYR   A N    1 
ATOM   4475 C  CA   . TYR   A 1 291 ? -23.728 29.776  -5.105  1.00 14.16  ? 291 TYR   A CA   1 
ATOM   4476 C  C    . TYR   A 1 291 ? -23.022 28.807  -4.175  1.00 15.35  ? 291 TYR   A C    1 
ATOM   4477 O  O    . TYR   A 1 291 ? -22.927 29.098  -2.989  1.00 16.84  ? 291 TYR   A O    1 
ATOM   4478 C  CB   . TYR   A 1 291 ? -25.190 29.315  -5.302  1.00 14.39  ? 291 TYR   A CB   1 
ATOM   4479 C  CG   . TYR   A 1 291 ? -26.005 30.399  -5.921  1.00 16.31  ? 291 TYR   A CG   1 
ATOM   4480 C  CD1  . TYR   A 1 291 ? -26.317 31.558  -5.213  1.00 18.14  ? 291 TYR   A CD1  1 
ATOM   4481 C  CD2  . TYR   A 1 291 ? -26.407 30.334  -7.243  1.00 16.10  ? 291 TYR   A CD2  1 
ATOM   4482 C  CE1  . TYR   A 1 291 ? -27.021 32.602  -5.809  1.00 23.72  ? 291 TYR   A CE1  1 
ATOM   4483 C  CE2  . TYR   A 1 291 ? -27.093 31.372  -7.856  1.00 16.66  ? 291 TYR   A CE2  1 
ATOM   4484 C  CZ   . TYR   A 1 291 ? -27.354 32.481  -7.149  1.00 19.10  ? 291 TYR   A CZ   1 
ATOM   4485 O  OH   . TYR   A 1 291 ? -28.081 33.547  -7.682  1.00 24.43  ? 291 TYR   A OH   1 
ATOM   4486 H  H    . TYR   A 1 291 ? -22.850 29.291  -6.815  1.00 17.07  ? 291 TYR   A H    1 
ATOM   4487 H  HA   . TYR   A 1 291 ? -23.737 30.634  -4.653  1.00 17.00  ? 291 TYR   A HA   1 
ATOM   4488 H  HB2  . TYR   A 1 291 ? -25.208 28.542  -5.888  1.00 17.26  ? 291 TYR   A HB2  1 
ATOM   4489 H  HB3  . TYR   A 1 291 ? -25.577 29.089  -4.442  1.00 17.26  ? 291 TYR   A HB3  1 
ATOM   4490 H  HD1  . TYR   A 1 291 ? -26.050 31.636  -4.326  1.00 21.77  ? 291 TYR   A HD1  1 
ATOM   4491 H  HD2  . TYR   A 1 291 ? -26.210 29.570  -7.736  1.00 19.32  ? 291 TYR   A HD2  1 
ATOM   4492 H  HE1  . TYR   A 1 291 ? -27.261 33.357  -5.322  1.00 28.46  ? 291 TYR   A HE1  1 
ATOM   4493 H  HE2  . TYR   A 1 291 ? -27.367 31.301  -8.742  1.00 19.99  ? 291 TYR   A HE2  1 
ATOM   4494 H  HH   . TYR   A 1 291 ? -28.211 33.424  -8.503  1.00 29.32  ? 291 TYR   A HH   1 
ATOM   4495 N  N    . TRP   A 1 292 ? -22.511 27.678  -4.658  1.00 14.22  ? 292 TRP   A N    1 
ATOM   4496 C  CA   . TRP   A 1 292 ? -21.920 26.681  -3.769  1.00 12.61  ? 292 TRP   A CA   1 
ATOM   4497 C  C    . TRP   A 1 292 ? -20.659 27.256  -3.144  1.00 14.71  ? 292 TRP   A C    1 
ATOM   4498 O  O    . TRP   A 1 292 ? -19.875 27.947  -3.810  1.00 14.07  ? 292 TRP   A O    1 
ATOM   4499 C  CB   . TRP   A 1 292 ? -21.600 25.429  -4.574  1.00 13.00  ? 292 TRP   A CB   1 
ATOM   4500 C  CG   . TRP   A 1 292 ? -22.788 24.651  -5.027  1.00 11.10  ? 292 TRP   A CG   1 
ATOM   4501 C  CD1  . TRP   A 1 292 ? -24.044 24.722  -4.536  1.00 13.06  ? 292 TRP   A CD1  1 
ATOM   4502 C  CD2  . TRP   A 1 292 ? -22.755 23.602  -5.981  1.00 11.46  ? 292 TRP   A CD2  1 
ATOM   4503 N  NE1  . TRP   A 1 292 ? -24.842 23.777  -5.179  1.00 12.37  ? 292 TRP   A NE1  1 
ATOM   4504 C  CE2  . TRP   A 1 292 ? -24.061 23.079  -6.072  1.00 12.20  ? 292 TRP   A CE2  1 
ATOM   4505 C  CE3  . TRP   A 1 292 ? -21.738 23.036  -6.815  1.00 12.97  ? 292 TRP   A CE3  1 
ATOM   4506 C  CZ2  . TRP   A 1 292 ? -24.383 22.067  -6.941  1.00 12.43  ? 292 TRP   A CZ2  1 
ATOM   4507 C  CZ3  . TRP   A 1 292 ? -22.073 22.042  -7.672  1.00 13.07  ? 292 TRP   A CZ3  1 
ATOM   4508 C  CH2  . TRP   A 1 292 ? -23.356 21.550  -7.763  1.00 12.64  ? 292 TRP   A CH2  1 
ATOM   4509 H  H    . TRP   A 1 292 ? -22.494 27.465  -5.491  1.00 17.07  ? 292 TRP   A H    1 
ATOM   4510 H  HA   . TRP   A 1 292 ? -22.531 26.437  -3.056  1.00 15.13  ? 292 TRP   A HA   1 
ATOM   4511 H  HB2  . TRP   A 1 292 ? -21.104 25.691  -5.365  1.00 15.60  ? 292 TRP   A HB2  1 
ATOM   4512 H  HB3  . TRP   A 1 292 ? -21.060 24.840  -4.024  1.00 15.60  ? 292 TRP   A HB3  1 
ATOM   4513 H  HD1  . TRP   A 1 292 ? -24.332 25.308  -3.874  1.00 15.67  ? 292 TRP   A HD1  1 
ATOM   4514 H  HE1  . TRP   A 1 292 ? -25.681 23.651  -5.041  1.00 14.85  ? 292 TRP   A HE1  1 
ATOM   4515 H  HE3  . TRP   A 1 292 ? -20.862 23.346  -6.769  1.00 15.56  ? 292 TRP   A HE3  1 
ATOM   4516 H  HZ2  . TRP   A 1 292 ? -25.249 21.731  -6.988  1.00 14.91  ? 292 TRP   A HZ2  1 
ATOM   4517 H  HZ3  . TRP   A 1 292 ? -21.414 21.679  -8.219  1.00 15.69  ? 292 TRP   A HZ3  1 
ATOM   4518 H  HH2  . TRP   A 1 292 ? -23.548 20.873  -8.370  1.00 15.17  ? 292 TRP   A HH2  1 
ATOM   4519 N  N    . THR   A 1 293 ? -20.424 26.902  -1.880  1.00 15.46  ? 293 THR   A N    1 
ATOM   4520 C  CA   . THR   A 1 293 ? -19.284 27.405  -1.122  1.00 15.28  ? 293 THR   A CA   1 
ATOM   4521 C  C    . THR   A 1 293 ? -18.350 26.243  -0.793  1.00 15.19  ? 293 THR   A C    1 
ATOM   4522 O  O    . THR   A 1 293 ? -18.718 25.070  -0.957  1.00 13.76  ? 293 THR   A O    1 
ATOM   4523 C  CB   . THR   A 1 293 ? -19.746 28.073  0.182   1.00 17.18  ? 293 THR   A CB   1 
ATOM   4524 O  OG1  . THR   A 1 293 ? -20.207 27.034  1.079   1.00 19.04  ? 293 THR   A OG1  1 
ATOM   4525 C  CG2  . THR   A 1 293 ? -20.870 29.077  -0.017  1.00 19.96  ? 293 THR   A CG2  1 
ATOM   4526 H  H    . THR   A 1 293 ? -20.923 26.362  -1.434  1.00 18.55  ? 293 THR   A H    1 
ATOM   4527 H  HA   . THR   A 1 293 ? -18.804 28.073  -1.636  1.00 18.33  ? 293 THR   A HA   1 
ATOM   4528 H  HB   . THR   A 1 293 ? -18.999 28.568  0.553   1.00 20.61  ? 293 THR   A HB   1 
ATOM   4529 H  HG1  . THR   A 1 293 ? -20.530 27.378  1.775   1.00 22.85  ? 293 THR   A HG1  1 
ATOM   4530 H  HG21 . THR   A 1 293 ? -21.073 29.518  0.823   1.00 23.95  ? 293 THR   A HG21 1 
ATOM   4531 H  HG22 . THR   A 1 293 ? -20.605 29.746  -0.668  1.00 23.95  ? 293 THR   A HG22 1 
ATOM   4532 H  HG23 . THR   A 1 293 ? -21.666 28.625  -0.336  1.00 23.95  ? 293 THR   A HG23 1 
ATOM   4533 N  N    . PRO   A 1 294 ? -17.106 26.529  -0.411  1.00 14.04  ? 294 PRO   A N    1 
ATOM   4534 C  CA   . PRO   A 1 294 ? -16.125 25.449  -0.289  1.00 15.02  ? 294 PRO   A CA   1 
ATOM   4535 C  C    . PRO   A 1 294 ? -16.478 24.335  0.678   1.00 14.01  ? 294 PRO   A C    1 
ATOM   4536 O  O    . PRO   A 1 294 ? -16.159 23.158  0.398   1.00 16.12  ? 294 PRO   A O    1 
ATOM   4537 C  CB   . PRO   A 1 294 ? -14.846 26.182  0.134   1.00 16.05  ? 294 PRO   A CB   1 
ATOM   4538 C  CG   . PRO   A 1 294 ? -15.026 27.574  -0.512  1.00 17.30  ? 294 PRO   A CG   1 
ATOM   4539 C  CD   . PRO   A 1 294 ? -16.459 27.861  -0.289  1.00 15.85  ? 294 PRO   A CD   1 
ATOM   4540 H  HA   . PRO   A 1 294 ? -16.008 25.051  -1.165  1.00 18.02  ? 294 PRO   A HA   1 
ATOM   4541 H  HB2  . PRO   A 1 294 ? -14.793 26.242  1.101   1.00 19.26  ? 294 PRO   A HB2  1 
ATOM   4542 H  HB3  . PRO   A 1 294 ? -14.063 25.727  -0.213  1.00 19.26  ? 294 PRO   A HB3  1 
ATOM   4543 H  HG2  . PRO   A 1 294 ? -14.462 28.228  -0.070  1.00 20.76  ? 294 PRO   A HG2  1 
ATOM   4544 H  HG3  . PRO   A 1 294 ? -14.815 27.538  -1.458  1.00 20.76  ? 294 PRO   A HG3  1 
ATOM   4545 H  HD2  . PRO   A 1 294 ? -16.602 28.232  0.596   1.00 19.02  ? 294 PRO   A HD2  1 
ATOM   4546 H  HD3  . PRO   A 1 294 ? -16.797 28.470  -0.963  1.00 19.02  ? 294 PRO   A HD3  1 
ATOM   4547 N  N    . TYR   A 1 295 ? -17.162 24.627  1.770   1.00 14.10  ? 295 TYR   A N    1 
ATOM   4548 C  CA   . TYR   A 1 295 ? -17.517 23.627  2.761   1.00 14.17  ? 295 TYR   A CA   1 
ATOM   4549 C  C    . TYR   A 1 295 ? -19.014 23.261  2.684   1.00 14.95  ? 295 TYR   A C    1 
ATOM   4550 O  O    . TYR   A 1 295 ? -19.571 22.809  3.689   1.00 14.64  ? 295 TYR   A O    1 
ATOM   4551 C  CB   . TYR   A 1 295 ? -17.109 24.068  4.163   1.00 16.52  ? 295 TYR   A CB   1 
ATOM   4552 C  CG   . TYR   A 1 295 ? -15.652 24.350  4.287   1.00 18.87  ? 295 TYR   A CG   1 
ATOM   4553 C  CD1  . TYR   A 1 295 ? -14.720 23.342  4.297   1.00 18.19  ? 295 TYR   A CD1  1 
ATOM   4554 C  CD2  . TYR   A 1 295 ? -15.210 25.666  4.334   1.00 29.26  ? 295 TYR   A CD2  1 
ATOM   4555 C  CE1  . TYR   A 1 295 ? -13.340 23.639  4.451   1.00 25.95  ? 295 TYR   A CE1  1 
ATOM   4556 C  CE2  . TYR   A 1 295 ? -13.861 25.971  4.452   1.00 31.91  ? 295 TYR   A CE2  1 
ATOM   4557 C  CZ   . TYR   A 1 295 ? -12.952 24.959  4.506   1.00 31.92  ? 295 TYR   A CZ   1 
ATOM   4558 O  OH   . TYR   A 1 295 ? -11.603 25.254  4.653   1.00 42.64  ? 295 TYR   A OH   1 
ATOM   4559 H  H    . TYR   A 1 295 ? -17.440 25.417  1.963   1.00 16.92  ? 295 TYR   A H    1 
ATOM   4560 H  HA   . TYR   A 1 295 ? -17.015 22.817  2.580   1.00 17.01  ? 295 TYR   A HA   1 
ATOM   4561 H  HB2  . TYR   A 1 295 ? -17.591 24.878  4.390   1.00 19.83  ? 295 TYR   A HB2  1 
ATOM   4562 H  HB3  . TYR   A 1 295 ? -17.331 23.363  4.791   1.00 19.83  ? 295 TYR   A HB3  1 
ATOM   4563 H  HD1  . TYR   A 1 295 ? -14.994 22.458  4.202   1.00 21.83  ? 295 TYR   A HD1  1 
ATOM   4564 H  HD2  . TYR   A 1 295 ? -15.831 26.356  4.285   1.00 35.11  ? 295 TYR   A HD2  1 
ATOM   4565 H  HE1  . TYR   A 1 295 ? -12.711 22.957  4.514   1.00 31.14  ? 295 TYR   A HE1  1 
ATOM   4566 H  HE2  . TYR   A 1 295 ? -13.581 26.857  4.494   1.00 38.30  ? 295 TYR   A HE2  1 
ATOM   4567 H  HH   . TYR   A 1 295 ? -11.160 24.544  4.727   1.00 51.17  ? 295 TYR   A HH   1 
ATOM   4568 N  N    . SER   A 1 296 ? -19.636 23.411  1.512   1.00 13.64  ? 296 SER   A N    1 
ATOM   4569 C  CA   . SER   A 1 296 ? -21.059 23.185  1.376   1.00 12.41  ? 296 SER   A CA   1 
ATOM   4570 C  C    . SER   A 1 296 ? -21.454 21.850  1.951   1.00 13.65  ? 296 SER   A C    1 
ATOM   4571 O  O    . SER   A 1 296 ? -20.817 20.822  1.707   1.00 15.83  ? 296 SER   A O    1 
ATOM   4572 C  CB   . SER   A 1 296 ? -21.400 23.162  -0.088  1.00 14.34  ? 296 SER   A CB   1 
ATOM   4573 O  OG   . SER   A 1 296 ? -22.812 23.135  -0.315  1.00 14.75  ? 296 SER   A OG   1 
ATOM   4574 H  H    . SER   A 1 296 ? -19.247 23.644  0.781   1.00 16.37  ? 296 SER   A H    1 
ATOM   4575 H  HA   . SER   A 1 296 ? -21.538 23.889  1.840   1.00 14.89  ? 296 SER   A HA   1 
ATOM   4576 H  HB2  . SER   A 1 296 ? -21.035 23.959  -0.504  1.00 17.21  ? 296 SER   A HB2  1 
ATOM   4577 H  HB3  . SER   A 1 296 ? -21.007 22.370  -0.486  1.00 17.21  ? 296 SER   A HB3  1 
ATOM   4578 H  HG   . SER   A 1 296 ? -23.146 22.449  0.037   1.00 17.70  ? 296 SER   A HG   1 
ATOM   4579 N  N    . THR   A 1 297 ? -22.582 21.842  2.656   1.00 13.19  ? 297 THR   A N    1 
ATOM   4580 C  CA   . THR   A 1 297 ? -23.282 20.602  2.976   1.00 13.55  ? 297 THR   A CA   1 
ATOM   4581 C  C    . THR   A 1 297 ? -24.196 20.258  1.786   1.00 11.80  ? 297 THR   A C    1 
ATOM   4582 O  O    . THR   A 1 297 ? -24.470 21.071  0.917   1.00 12.61  ? 297 THR   A O    1 
ATOM   4583 C  CB   . THR   A 1 297 ? -24.126 20.743  4.236   1.00 15.23  ? 297 THR   A CB   1 
ATOM   4584 O  OG1  . THR   A 1 297 ? -25.143 21.726  3.952   1.00 14.86  ? 297 THR   A OG1  1 
ATOM   4585 C  CG2  . THR   A 1 297 ? -23.283 21.166  5.441   1.00 16.41  ? 297 THR   A CG2  1 
ATOM   4586 H  H    . THR   A 1 297 ? -22.965 22.548  2.963   1.00 15.82  ? 297 THR   A H    1 
ATOM   4587 H  HA   . THR   A 1 297 ? -22.638 19.895  3.140   1.00 16.26  ? 297 THR   A HA   1 
ATOM   4588 H  HB   . THR   A 1 297 ? -24.526 19.894  4.481   1.00 18.28  ? 297 THR   A HB   1 
ATOM   4589 H  HG1  . THR   A 1 297 ? -25.590 21.884  4.645   1.00 17.83  ? 297 THR   A HG1  1 
ATOM   4590 H  HG21 . THR   A 1 297 ? -23.836 21.200  6.237   1.00 19.70  ? 297 THR   A HG21 1 
ATOM   4591 H  HG22 . THR   A 1 297 ? -22.565 20.530  5.584   1.00 19.70  ? 297 THR   A HG22 1 
ATOM   4592 H  HG23 . THR   A 1 297 ? -22.900 22.044  5.286   1.00 19.70  ? 297 THR   A HG23 1 
ATOM   4593 N  N    . PHE   A 1 298 ? -24.704 19.022  1.774   1.00 12.90  ? 298 PHE   A N    1 
ATOM   4594 C  CA   . PHE   A 1 298 ? -25.679 18.651  0.742   1.00 13.27  ? 298 PHE   A CA   1 
ATOM   4595 C  C    . PHE   A 1 298 ? -26.908 19.575  0.766   1.00 12.94  ? 298 PHE   A C    1 
ATOM   4596 O  O    . PHE   A 1 298 ? -27.391 19.985  -0.295  1.00 13.03  ? 298 PHE   A O    1 
ATOM   4597 C  CB   . PHE   A 1 298 ? -26.173 17.228  0.969   1.00 13.69  ? 298 PHE   A CB   1 
ATOM   4598 C  CG   . PHE   A 1 298 ? -25.143 16.133  0.742   1.00 12.32  ? 298 PHE   A CG   1 
ATOM   4599 C  CD1  . PHE   A 1 298 ? -24.174 16.196  -0.217  1.00 14.06  ? 298 PHE   A CD1  1 
ATOM   4600 C  CD2  . PHE   A 1 298 ? -25.183 15.025  1.517   1.00 15.36  ? 298 PHE   A CD2  1 
ATOM   4601 C  CE1  . PHE   A 1 298 ? -23.258 15.143  -0.426  1.00 13.73  ? 298 PHE   A CE1  1 
ATOM   4602 C  CE2  . PHE   A 1 298 ? -24.253 13.972  1.339   1.00 16.77  ? 298 PHE   A CE2  1 
ATOM   4603 C  CZ   . PHE   A 1 298 ? -23.305 14.068  0.362   1.00 15.67  ? 298 PHE   A CZ   1 
ATOM   4604 H  H    . PHE   A 1 298 ? -24.509 18.399  2.334   1.00 15.47  ? 298 PHE   A H    1 
ATOM   4605 H  HA   . PHE   A 1 298 ? -25.231 18.716  -0.116  1.00 15.93  ? 298 PHE   A HA   1 
ATOM   4606 H  HB2  . PHE   A 1 298 ? -26.476 17.153  1.887   1.00 16.42  ? 298 PHE   A HB2  1 
ATOM   4607 H  HB3  . PHE   A 1 298 ? -26.911 17.060  0.361   1.00 16.42  ? 298 PHE   A HB3  1 
ATOM   4608 H  HD1  . PHE   A 1 298 ? -24.116 16.956  -0.750  1.00 16.87  ? 298 PHE   A HD1  1 
ATOM   4609 H  HD2  . PHE   A 1 298 ? -25.833 14.954  2.179   1.00 18.43  ? 298 PHE   A HD2  1 
ATOM   4610 H  HE1  . PHE   A 1 298 ? -22.627 15.198  -1.108  1.00 16.48  ? 298 PHE   A HE1  1 
ATOM   4611 H  HE2  . PHE   A 1 298 ? -24.287 13.220  1.885   1.00 20.12  ? 298 PHE   A HE2  1 
ATOM   4612 H  HZ   . PHE   A 1 298 ? -22.689 13.380  0.246   1.00 18.80  ? 298 PHE   A HZ   1 
ATOM   4613 N  N    . ASP   A 1 299 ? -27.407 19.906  1.963   1.00 12.58  ? 299 ASP   A N    1 
ATOM   4614 C  CA   . ASP   A 1 299 ? -28.561 20.797  2.074   1.00 13.68  ? 299 ASP   A CA   1 
ATOM   4615 C  C    . ASP   A 1 299 ? -28.242 22.192  1.542   1.00 13.92  ? 299 ASP   A C    1 
ATOM   4616 O  O    . ASP   A 1 299 ? -29.047 22.803  0.847   1.00 14.64  ? 299 ASP   A O    1 
ATOM   4617 C  CB   . ASP   A 1 299 ? -29.061 20.874  3.517   1.00 13.35  ? 299 ASP   A CB   1 
ATOM   4618 C  CG   . ASP   A 1 299 ? -29.758 19.610  4.010   1.00 15.65  ? 299 ASP   A CG   1 
ATOM   4619 O  OD1  . ASP   A 1 299 ? -30.010 18.657  3.217   1.00 17.33  ? 299 ASP   A OD1  1 
ATOM   4620 O  OD2  . ASP   A 1 299 ? -30.055 19.571  5.242   1.00 19.26  ? 299 ASP   A OD2  1 
ATOM   4621 H  H    . ASP   A 1 299 ? -27.098 19.630  2.717   1.00 15.09  ? 299 ASP   A H    1 
ATOM   4622 H  HA   . ASP   A 1 299 ? -29.277 20.422  1.537   1.00 16.41  ? 299 ASP   A HA   1 
ATOM   4623 H  HB2  . ASP   A 1 299 ? -28.303 21.037  4.100   1.00 16.02  ? 299 ASP   A HB2  1 
ATOM   4624 H  HB3  . ASP   A 1 299 ? -29.696 21.605  3.586   1.00 16.02  ? 299 ASP   A HB3  1 
ATOM   4625 N  N    . GLU   A 1 300 ? -27.095 22.750  1.935   1.00 12.86  ? 300 GLU   A N    1 
ATOM   4626 C  CA   . GLU   A 1 300 ? -26.754 24.068  1.432   1.00 13.92  ? 300 GLU   A CA   1 
ATOM   4627 C  C    . GLU   A 1 300 ? -26.608 24.015  -0.077  1.00 12.35  ? 300 GLU   A C    1 
ATOM   4628 O  O    . GLU   A 1 300 ? -26.963 24.975  -0.784  1.00 14.33  ? 300 GLU   A O    1 
ATOM   4629 C  CB   . GLU   A 1 300 ? -25.440 24.530  2.057   1.00 15.64  ? 300 GLU   A CB   1 
ATOM   4630 C  CG   . GLU   A 1 300 ? -25.594 25.008  3.485   1.00 16.92  ? 300 GLU   A CG   1 
ATOM   4631 C  CD   . GLU   A 1 300 ? -24.307 25.039  4.248   1.00 16.81  ? 300 GLU   A CD   1 
ATOM   4632 O  OE1  . GLU   A 1 300 ? -23.214 24.704  3.760   1.00 17.48  ? 300 GLU   A OE1  1 
ATOM   4633 O  OE2  . GLU   A 1 300 ? -24.353 25.421  5.453   1.00 18.78  ? 300 GLU   A OE2  1 
ATOM   4634 H  H    . GLU   A 1 300 ? -26.523 22.396  2.471   1.00 15.43  ? 300 GLU   A H    1 
ATOM   4635 H  HA   . GLU   A 1 300 ? -27.446 24.705  1.671   1.00 16.70  ? 300 GLU   A HA   1 
ATOM   4636 H  HB2  . GLU   A 1 300 ? -24.814 23.789  2.057   1.00 18.77  ? 300 GLU   A HB2  1 
ATOM   4637 H  HB3  . GLU   A 1 300 ? -25.084 25.265  1.533   1.00 18.77  ? 300 GLU   A HB3  1 
ATOM   4638 H  HG2  . GLU   A 1 300 ? -25.956 25.908  3.477   1.00 20.31  ? 300 GLU   A HG2  1 
ATOM   4639 H  HG3  . GLU   A 1 300 ? -26.201 24.412  3.951   1.00 20.31  ? 300 GLU   A HG3  1 
ATOM   4640 N  N    . GLY   A 1 301 ? -26.113 22.910  -0.624  1.00 13.03  ? 301 GLY   A N    1 
ATOM   4641 C  CA   . GLY   A 1 301 ? -25.978 22.781  -2.072  1.00 12.83  ? 301 GLY   A CA   1 
ATOM   4642 C  C    . GLY   A 1 301 ? -27.319 22.783  -2.767  1.00 12.57  ? 301 GLY   A C    1 
ATOM   4643 O  O    . GLY   A 1 301 ? -27.454 23.336  -3.871  1.00 13.09  ? 301 GLY   A O    1 
ATOM   4644 H  H    . GLY   A 1 301 ? -25.849 22.222  -0.182  1.00 15.64  ? 301 GLY   A H    1 
ATOM   4645 H  HA2  . GLY   A 1 301 ? -25.452 23.520  -2.414  1.00 15.40  ? 301 GLY   A HA2  1 
ATOM   4646 H  HA3  . GLY   A 1 301 ? -25.525 21.948  -2.280  1.00 15.40  ? 301 GLY   A HA3  1 
ATOM   4647 N  N    . GLY   A 1 302 ? -28.332 22.197  -2.121  1.00 13.30  ? 302 GLY   A N    1 
ATOM   4648 C  CA   . GLY   A 1 302 ? -29.698 22.192  -2.673  1.00 14.15  ? 302 GLY   A CA   1 
ATOM   4649 C  C    . GLY   A 1 302 ? -30.251 23.598  -2.689  1.00 12.66  ? 302 GLY   A C    1 
ATOM   4650 O  O    . GLY   A 1 302 ? -30.982 23.928  -3.632  1.00 13.98  ? 302 GLY   A O    1 
ATOM   4651 H  H    . GLY   A 1 302 ? -28.224 21.794  -1.316  1.00 15.96  ? 302 GLY   A H    1 
ATOM   4652 H  HA2  . GLY   A 1 302 ? -29.681 21.828  -3.590  1.00 16.98  ? 302 GLY   A HA2  1 
ATOM   4653 H  HA3  . GLY   A 1 302 ? -30.273 21.611  -2.121  1.00 16.98  ? 302 GLY   A HA3  1 
ATOM   4654 N  N    . CYS   A 1 303 ? -29.935 24.394  -1.667  1.00 13.82  ? 303 CYS   A N    1 
ATOM   4655 C  CA   A CYS   A 1 303 ? -30.320 25.909  -1.717  0.44 14.91  ? 303 CYS   A CA   1 
ATOM   4656 C  CA   B CYS   A 1 303 ? -30.347 25.826  -1.681  0.56 15.01  ? 303 CYS   A CA   1 
ATOM   4657 C  C    . CYS   A 1 303 ? -29.662 26.620  -2.822  1.00 14.82  ? 303 CYS   A C    1 
ATOM   4658 O  O    . CYS   A 1 303 ? -30.232 27.563  -3.436  1.00 15.69  ? 303 CYS   A O    1 
ATOM   4659 C  CB   A CYS   A 1 303 ? -29.940 26.631  -0.430  0.44 15.67  ? 303 CYS   A CB   1 
ATOM   4660 C  CB   B CYS   A 1 303 ? -30.025 26.489  -0.348  0.56 15.66  ? 303 CYS   A CB   1 
ATOM   4661 S  SG   A CYS   A 1 303 ? -30.712 26.111  1.101   0.44 16.77  ? 303 CYS   A SG   1 
ATOM   4662 S  SG   B CYS   A 1 303 ? -30.885 28.064  -0.097  0.56 21.38  ? 303 CYS   A SG   1 
ATOM   4663 H  H    A CYS   A 1 303 ? -29.477 24.280  -0.973  0.44 16.58  ? 303 CYS   A H    1 
ATOM   4664 H  H    B CYS   A 1 303 ? -29.133 24.305  -1.264  0.56 16.58  ? 303 CYS   A H    1 
ATOM   4665 H  HA   A CYS   A 1 303 ? -31.285 25.944  -1.806  0.44 17.89  ? 303 CYS   A HA   1 
ATOM   4666 H  HA   B CYS   A 1 303 ? -31.323 25.853  -1.828  0.56 18.01  ? 303 CYS   A HA   1 
ATOM   4667 H  HB2  A CYS   A 1 303 ? -28.984 26.526  -0.307  0.44 18.80  ? 303 CYS   A HB2  1 
ATOM   4668 H  HB2  B CYS   A 1 303 ? -30.270 25.879  0.382   0.56 18.79  ? 303 CYS   A HB2  1 
ATOM   4669 H  HB3  A CYS   A 1 303 ? -30.159 27.569  -0.545  0.44 18.80  ? 303 CYS   A HB3  1 
ATOM   4670 H  HB3  B CYS   A 1 303 ? -29.057 26.651  -0.296  0.56 18.79  ? 303 CYS   A HB3  1 
ATOM   4671 N  N    . GLY   A 1 304 ? -28.425 26.228  -3.138  1.00 12.99  ? 304 GLY   A N    1 
ATOM   4672 C  CA   . GLY   A 1 304 ? -27.684 26.864  -4.244  1.00 13.59  ? 304 GLY   A CA   1 
ATOM   4673 C  C    . GLY   A 1 304 ? -28.294 26.485  -5.577  1.00 14.52  ? 304 GLY   A C    1 
ATOM   4674 O  O    . GLY   A 1 304 ? -28.251 27.328  -6.478  1.00 15.02  ? 304 GLY   A O    1 
ATOM   4675 H  H    . GLY   A 1 304 ? -28.009 25.555  -2.698  1.00 15.59  ? 304 GLY   A H    1 
ATOM   4676 H  HA2  . GLY   A 1 304 ? -27.705 27.844  -4.133  1.00 16.31  ? 304 GLY   A HA2  1 
ATOM   4677 H  HA3  . GLY   A 1 304 ? -26.743 26.571  -4.216  1.00 16.31  ? 304 GLY   A HA3  1 
ATOM   4678 N  N    . MET   A 1 305 ? -28.811 25.260  -5.724  1.00 12.53  ? 305 MET   A N    1 
ATOM   4679 C  CA   . MET   A 1 305 ? -29.496 24.850  -6.942  1.00 13.28  ? 305 MET   A CA   1 
ATOM   4680 C  C    . MET   A 1 305 ? -30.816 25.601  -7.110  1.00 13.11  ? 305 MET   A C    1 
ATOM   4681 O  O    . MET   A 1 305 ? -31.212 25.934  -8.230  1.00 13.63  ? 305 MET   A O    1 
ATOM   4682 C  CB   . MET   A 1 305 ? -29.787 23.355  -6.858  1.00 13.70  ? 305 MET   A CB   1 
ATOM   4683 C  CG   . MET   A 1 305 ? -28.586 22.468  -7.081  1.00 13.81  ? 305 MET   A CG   1 
ATOM   4684 S  SD   . MET   A 1 305 ? -28.913 20.735  -6.752  1.00 14.38  ? 305 MET   A SD   1 
ATOM   4685 C  CE   . MET   A 1 305 ? -30.004 20.394  -8.114  1.00 16.21  ? 305 MET   A CE   1 
ATOM   4686 H  H    . MET   A 1 305 ? -28.745 24.648  -5.124  1.00 15.04  ? 305 MET   A H    1 
ATOM   4687 H  HA   . MET   A 1 305 ? -28.922 25.032  -7.703  1.00 15.94  ? 305 MET   A HA   1 
ATOM   4688 H  HB2  . MET   A 1 305 ? -30.136 23.157  -5.975  1.00 16.44  ? 305 MET   A HB2  1 
ATOM   4689 H  HB3  . MET   A 1 305 ? -30.446 23.130  -7.533  1.00 16.44  ? 305 MET   A HB3  1 
ATOM   4690 H  HG2  . MET   A 1 305 ? -28.305 22.547  -8.006  1.00 16.57  ? 305 MET   A HG2  1 
ATOM   4691 H  HG3  . MET   A 1 305 ? -27.871 22.754  -6.492  1.00 16.57  ? 305 MET   A HG3  1 
ATOM   4692 H  HE1  . MET   A 1 305 ? -30.273 19.463  -8.077  1.00 19.45  ? 305 MET   A HE1  1 
ATOM   4693 H  HE2  . MET   A 1 305 ? -30.783 20.967  -8.045  1.00 19.45  ? 305 MET   A HE2  1 
ATOM   4694 H  HE3  . MET   A 1 305 ? -29.536 20.570  -8.945  1.00 19.45  ? 305 MET   A HE3  1 
ATOM   4695 N  N    . LEU   A 1 306 ? -31.535 25.821  -5.998  1.00 12.70  ? 306 LEU   A N    1 
ATOM   4696 C  CA   . LEU   A 1 306 ? -32.778 26.565  -6.082  1.00 14.33  ? 306 LEU   A CA   1 
ATOM   4697 C  C    . LEU   A 1 306 ? -32.533 27.992  -6.548  1.00 14.52  ? 306 LEU   A C    1 
ATOM   4698 O  O    . LEU   A 1 306 ? -33.239 28.502  -7.408  1.00 15.51  ? 306 LEU   A O    1 
ATOM   4699 C  CB   . LEU   A 1 306 ? -33.471 26.559  -4.730  1.00 15.15  ? 306 LEU   A CB   1 
ATOM   4700 C  CG   . LEU   A 1 306 ? -34.120 25.238  -4.382  1.00 15.77  ? 306 LEU   A CG   1 
ATOM   4701 C  CD1  . LEU   A 1 306 ? -34.545 25.116  -2.920  1.00 18.24  ? 306 LEU   A CD1  1 
ATOM   4702 C  CD2  . LEU   A 1 306 ? -35.350 25.003  -5.236  1.00 19.08  ? 306 LEU   A CD2  1 
ATOM   4703 H  H    . LEU   A 1 306 ? -31.323 25.553  -5.209  1.00 15.24  ? 306 LEU   A H    1 
ATOM   4704 H  HA   . LEU   A 1 306 ? -33.362 26.135  -6.726  1.00 17.20  ? 306 LEU   A HA   1 
ATOM   4705 H  HB2  . LEU   A 1 306 ? -32.815 26.757  -4.043  1.00 18.18  ? 306 LEU   A HB2  1 
ATOM   4706 H  HB3  . LEU   A 1 306 ? -34.164 27.238  -4.733  1.00 18.18  ? 306 LEU   A HB3  1 
ATOM   4707 H  HG   . LEU   A 1 306 ? -33.440 24.567  -4.550  1.00 18.92  ? 306 LEU   A HG   1 
ATOM   4708 H  HD11 . LEU   A 1 306 ? -34.968 24.254  -2.784  1.00 21.88  ? 306 LEU   A HD11 1 
ATOM   4709 H  HD12 . LEU   A 1 306 ? -33.760 25.192  -2.355  1.00 21.88  ? 306 LEU   A HD12 1 
ATOM   4710 H  HD13 . LEU   A 1 306 ? -35.172 25.827  -2.713  1.00 21.88  ? 306 LEU   A HD13 1 
ATOM   4711 H  HD21 . LEU   A 1 306 ? -35.797 24.198  -4.930  1.00 22.89  ? 306 LEU   A HD21 1 
ATOM   4712 H  HD22 . LEU   A 1 306 ? -35.944 25.764  -5.150  1.00 22.89  ? 306 LEU   A HD22 1 
ATOM   4713 H  HD23 . LEU   A 1 306 ? -35.077 24.899  -6.161  1.00 22.89  ? 306 LEU   A HD23 1 
ATOM   4714 N  N    . SER   A 1 307 ? -31.468 28.627  -6.026  1.00 14.00  ? 307 SER   A N    1 
ATOM   4715 C  CA   . SER   A 1 307 ? -31.164 29.986  -6.463  1.00 15.76  ? 307 SER   A CA   1 
ATOM   4716 C  C    . SER   A 1 307 ? -30.721 30.013  -7.919  1.00 13.92  ? 307 SER   A C    1 
ATOM   4717 O  O    . SER   A 1 307 ? -31.098 30.915  -8.671  1.00 17.23  ? 307 SER   A O    1 
ATOM   4718 C  CB   . SER   A 1 307 ? -30.049 30.538  -5.610  1.00 17.15  ? 307 SER   A CB   1 
ATOM   4719 O  OG   . SER   A 1 307 ? -30.464 30.698  -4.270  1.00 19.70  ? 307 SER   A OG   1 
ATOM   4720 H  H    . SER   A 1 307 ? -30.931 28.300  -5.440  1.00 16.80  ? 307 SER   A H    1 
ATOM   4721 H  HA   . SER   A 1 307 ? -31.961 30.531  -6.365  1.00 18.91  ? 307 SER   A HA   1 
ATOM   4722 H  HB2  . SER   A 1 307 ? -29.299 29.923  -5.636  1.00 20.58  ? 307 SER   A HB2  1 
ATOM   4723 H  HB3  . SER   A 1 307 ? -29.782 31.401  -5.962  1.00 20.58  ? 307 SER   A HB3  1 
ATOM   4724 H  HG   . SER   A 1 307 ? -29.816 30.944  -3.796  1.00 23.64  ? 307 SER   A HG   1 
ATOM   4725 N  N    . ALA   A 1 308 ? -29.950 29.030  -8.347  1.00 14.31  ? 308 ALA   A N    1 
ATOM   4726 C  CA   . ALA   A 1 308 ? -29.534 28.941  -9.746  1.00 14.68  ? 308 ALA   A CA   1 
ATOM   4727 C  C    . ALA   A 1 308 ? -30.727 28.748  -10.664 1.00 15.15  ? 308 ALA   A C    1 
ATOM   4728 O  O    . ALA   A 1 308 ? -30.860 29.402  -11.712 1.00 16.08  ? 308 ALA   A O    1 
ATOM   4729 C  CB   . ALA   A 1 308 ? -28.537 27.800  -9.925  1.00 15.34  ? 308 ALA   A CB   1 
ATOM   4730 H  H    . ALA   A 1 308 ? -29.648 28.396  -7.851  1.00 17.18  ? 308 ALA   A H    1 
ATOM   4731 H  HA   . ALA   A 1 308 ? -29.096 29.771  -9.989  1.00 17.61  ? 308 ALA   A HA   1 
ATOM   4732 H  HB1  . ALA   A 1 308 ? -28.263 27.763  -10.855 1.00 18.41  ? 308 ALA   A HB1  1 
ATOM   4733 H  HB2  . ALA   A 1 308 ? -27.766 27.963  -9.360  1.00 18.41  ? 308 ALA   A HB2  1 
ATOM   4734 H  HB3  . ALA   A 1 308 ? -28.962 26.966  -9.672  1.00 18.41  ? 308 ALA   A HB3  1 
ATOM   4735 N  N    . ALA   A 1 309 ? -31.615 27.828  -10.317 1.00 15.52  ? 309 ALA   A N    1 
ATOM   4736 C  CA   . ALA   A 1 309 ? -32.810 27.600  -11.116 1.00 15.61  ? 309 ALA   A CA   1 
ATOM   4737 C  C    . ALA   A 1 309 ? -33.673 28.850  -11.196 1.00 17.16  ? 309 ALA   A C    1 
ATOM   4738 O  O    . ALA   A 1 309 ? -34.246 29.121  -12.264 1.00 17.89  ? 309 ALA   A O    1 
ATOM   4739 C  CB   . ALA   A 1 309 ? -33.598 26.449  -10.501 1.00 16.08  ? 309 ALA   A CB   1 
ATOM   4740 H  H    . ALA   A 1 309 ? -31.551 27.323  -9.625  1.00 18.62  ? 309 ALA   A H    1 
ATOM   4741 H  HA   . ALA   A 1 309 ? -32.553 27.363  -12.021 1.00 18.73  ? 309 ALA   A HA   1 
ATOM   4742 H  HB1  . ALA   A 1 309 ? -34.386 26.281  -11.041 1.00 19.30  ? 309 ALA   A HB1  1 
ATOM   4743 H  HB2  . ALA   A 1 309 ? -33.037 25.658  -10.479 1.00 19.30  ? 309 ALA   A HB2  1 
ATOM   4744 H  HB3  . ALA   A 1 309 ? -33.861 26.693  -9.599  1.00 19.30  ? 309 ALA   A HB3  1 
ATOM   4745 N  N    . LYS   A 1 310 ? -33.789 29.619  -10.105 1.00 16.45  ? 310 LYS   A N    1 
ATOM   4746 C  CA   . LYS   A 1 310 ? -34.539 30.883  -10.152 1.00 18.19  ? 310 LYS   A CA   1 
ATOM   4747 C  C    . LYS   A 1 310 ? -33.901 31.833  -11.162 1.00 21.38  ? 310 LYS   A C    1 
ATOM   4748 O  O    . LYS   A 1 310 ? -34.590 32.427  -11.999 1.00 21.98  ? 310 LYS   A O    1 
ATOM   4749 C  CB   . LYS   A 1 310 ? -34.592 31.492  -8.760  1.00 23.23  ? 310 LYS   A CB   1 
ATOM   4750 C  CG   . LYS   A 1 310 ? -35.532 32.657  -8.675  1.00 24.86  ? 310 LYS   A CG   1 
ATOM   4751 C  CD   . LYS   A 1 310 ? -35.921 32.859  -7.191  1.00 33.62  ? 310 LYS   A CD   1 
ATOM   4752 C  CE   . LYS   A 1 310 ? -36.590 34.203  -6.949  1.00 44.71  ? 310 LYS   A CE   1 
ATOM   4753 N  NZ   . LYS   A 1 310 ? -35.579 35.271  -6.734  1.00 48.88  ? 310 LYS   A NZ   1 
ATOM   4754 H  H    . LYS   A 1 310 ? -33.448 29.436  -9.337  1.00 19.74  ? 310 LYS   A H    1 
ATOM   4755 H  HA   . LYS   A 1 310 ? -35.453 30.721  -10.433 1.00 21.82  ? 310 LYS   A HA   1 
ATOM   4756 H  HB2  . LYS   A 1 310 ? -34.891 30.817  -8.131  1.00 27.88  ? 310 LYS   A HB2  1 
ATOM   4757 H  HB3  . LYS   A 1 310 ? -33.705 31.803  -8.517  1.00 27.88  ? 310 LYS   A HB3  1 
ATOM   4758 H  HG2  . LYS   A 1 310 ? -35.098 33.460  -9.002  1.00 29.84  ? 310 LYS   A HG2  1 
ATOM   4759 H  HG3  . LYS   A 1 310 ? -36.332 32.477  -9.192  1.00 29.84  ? 310 LYS   A HG3  1 
ATOM   4760 H  HD2  . LYS   A 1 310 ? -36.541 32.162  -6.926  1.00 40.35  ? 310 LYS   A HD2  1 
ATOM   4761 H  HD3  . LYS   A 1 310 ? -35.121 32.818  -6.644  1.00 40.35  ? 310 LYS   A HD3  1 
ATOM   4762 H  HE2  . LYS   A 1 310 ? -37.128 34.439  -7.722  1.00 53.65  ? 310 LYS   A HE2  1 
ATOM   4763 H  HE3  . LYS   A 1 310 ? -37.151 34.147  -6.160  1.00 53.65  ? 310 LYS   A HE3  1 
ATOM   4764 H  HZ1  . LYS   A 1 310 ? -35.985 36.052  -6.603  1.00 58.65  ? 310 LYS   A HZ1  1 
ATOM   4765 H  HZ2  . LYS   A 1 310 ? -35.082 35.081  -6.021  1.00 58.65  ? 310 LYS   A HZ2  1 
ATOM   4766 H  HZ3  . LYS   A 1 310 ? -35.050 35.337  -7.447  1.00 58.65  ? 310 LYS   A HZ3  1 
ATOM   4767 N  N    . ASP   A 1 311 ? -32.578 31.961  -11.116 1.00 19.02  ? 311 ASP   A N    1 
ATOM   4768 C  CA   . ASP   A 1 311 ? -31.887 32.813  -12.095 1.00 19.33  ? 311 ASP   A CA   1 
ATOM   4769 C  C    . ASP   A 1 311 ? -32.160 32.372  -13.516 1.00 19.90  ? 311 ASP   A C    1 
ATOM   4770 O  O    . ASP   A 1 311 ? -32.254 33.223  -14.412 1.00 21.92  ? 311 ASP   A O    1 
ATOM   4771 C  CB   . ASP   A 1 311 ? -30.377 32.694  -11.851 1.00 20.08  ? 311 ASP   A CB   1 
ATOM   4772 C  CG   . ASP   A 1 311 ? -29.896 33.384  -10.587 1.00 26.40  ? 311 ASP   A CG   1 
ATOM   4773 O  OD1  . ASP   A 1 311 ? -30.616 34.180  -9.984  1.00 26.27  ? 311 ASP   A OD1  1 
ATOM   4774 O  OD2  . ASP   A 1 311 ? -28.734 33.095  -10.174 1.00 26.95  ? 311 ASP   A OD2  1 
ATOM   4775 H  H    . ASP   A 1 311 ? -32.063 31.578  -10.543 1.00 22.82  ? 311 ASP   A H    1 
ATOM   4776 H  HA   . ASP   A 1 311 ? -32.194 33.726  -11.985 1.00 23.20  ? 311 ASP   A HA   1 
ATOM   4777 H  HB2  . ASP   A 1 311 ? -30.147 31.754  -11.778 1.00 24.10  ? 311 ASP   A HB2  1 
ATOM   4778 H  HB3  . ASP   A 1 311 ? -29.908 33.093  -12.601 1.00 24.10  ? 311 ASP   A HB3  1 
ATOM   4779 N  N    . LEU   A 1 312 ? -32.210 31.067  -13.790 1.00 18.04  ? 312 LEU   A N    1 
ATOM   4780 C  CA   . LEU   A 1 312 ? -32.396 30.509  -15.123 1.00 19.46  ? 312 LEU   A CA   1 
ATOM   4781 C  C    . LEU   A 1 312 ? -33.843 30.502  -15.559 1.00 22.17  ? 312 LEU   A C    1 
ATOM   4782 O  O    . LEU   A 1 312 ? -34.090 30.207  -16.716 1.00 23.40  ? 312 LEU   A O    1 
ATOM   4783 C  CB   . LEU   A 1 312 ? -31.869 29.073  -15.116 1.00 18.93  ? 312 LEU   A CB   1 
ATOM   4784 C  CG   . LEU   A 1 312 ? -30.356 28.956  -15.003 1.00 18.51  ? 312 LEU   A CG   1 
ATOM   4785 C  CD1  . LEU   A 1 312 ? -29.987 27.555  -14.657 1.00 20.22  ? 312 LEU   A CD1  1 
ATOM   4786 C  CD2  . LEU   A 1 312 ? -29.650 29.296  -16.248 1.00 24.97  ? 312 LEU   A CD2  1 
ATOM   4787 H  H    . LEU   A 1 312 ? -32.135 30.457  -13.188 1.00 21.65  ? 312 LEU   A H    1 
ATOM   4788 H  HA   . LEU   A 1 312 ? -31.899 31.034  -15.770 1.00 23.36  ? 312 LEU   A HA   1 
ATOM   4789 H  HB2  . LEU   A 1 312 ? -32.257 28.606  -14.359 1.00 22.72  ? 312 LEU   A HB2  1 
ATOM   4790 H  HB3  . LEU   A 1 312 ? -32.136 28.642  -15.943 1.00 22.72  ? 312 LEU   A HB3  1 
ATOM   4791 H  HG   . LEU   A 1 312 ? -30.080 29.584  -14.318 1.00 22.21  ? 312 LEU   A HG   1 
ATOM   4792 H  HD11 . LEU   A 1 312 ? -29.022 27.488  -14.598 1.00 24.26  ? 312 LEU   A HD11 1 
ATOM   4793 H  HD12 . LEU   A 1 312 ? -30.387 27.325  -13.803 1.00 24.26  ? 312 LEU   A HD12 1 
ATOM   4794 H  HD13 . LEU   A 1 312 ? -30.319 26.961  -15.348 1.00 24.26  ? 312 LEU   A HD13 1 
ATOM   4795 H  HD21 . LEU   A 1 312 ? -28.703 29.120  -16.132 1.00 29.96  ? 312 LEU   A HD21 1 
ATOM   4796 H  HD22 . LEU   A 1 312 ? -30.001 28.751  -16.970 1.00 29.96  ? 312 LEU   A HD22 1 
ATOM   4797 H  HD23 . LEU   A 1 312 ? -29.790 30.235  -16.445 1.00 29.96  ? 312 LEU   A HD23 1 
ATOM   4798 N  N    . GLY   A 1 313 ? -34.781 30.793  -14.669 1.00 19.76  ? 313 GLY   A N    1 
ATOM   4799 C  CA   . GLY   A 1 313 ? -36.200 30.752  -14.964 1.00 23.67  ? 313 GLY   A CA   1 
ATOM   4800 C  C    . GLY   A 1 313 ? -36.770 29.357  -15.018 1.00 23.36  ? 313 GLY   A C    1 
ATOM   4801 O  O    . GLY   A 1 313 ? -37.828 29.172  -15.639 1.00 25.12  ? 313 GLY   A O    1 
ATOM   4802 H  H    . GLY   A 1 313 ? -34.614 31.025  -13.858 1.00 23.71  ? 313 GLY   A H    1 
ATOM   4803 H  HA2  . GLY   A 1 313 ? -36.678 31.246  -14.279 1.00 28.40  ? 313 GLY   A HA2  1 
ATOM   4804 H  HA3  . GLY   A 1 313 ? -36.355 31.174  -15.824 1.00 28.40  ? 313 GLY   A HA3  1 
ATOM   4805 N  N    . TYR   A 1 314 ? -36.132 28.376  -14.358 1.00 18.61  ? 314 TYR   A N    1 
ATOM   4806 C  CA   . TYR   A 1 314 ? -36.601 27.002  -14.383 1.00 22.39  ? 314 TYR   A CA   1 
ATOM   4807 C  C    . TYR   A 1 314 ? -37.514 26.749  -13.184 1.00 20.56  ? 314 TYR   A C    1 
ATOM   4808 O  O    . TYR   A 1 314 ? -37.513 27.490  -12.202 1.00 22.59  ? 314 TYR   A O    1 
ATOM   4809 C  CB   . TYR   A 1 314 ? -35.436 26.004  -14.391 1.00 17.84  ? 314 TYR   A CB   1 
ATOM   4810 C  CG   . TYR   A 1 314 ? -34.539 26.074  -15.631 1.00 17.86  ? 314 TYR   A CG   1 
ATOM   4811 C  CD1  . TYR   A 1 314 ? -34.941 26.655  -16.805 1.00 18.73  ? 314 TYR   A CD1  1 
ATOM   4812 C  CD2  . TYR   A 1 314 ? -33.297 25.497  -15.598 1.00 17.29  ? 314 TYR   A CD2  1 
ATOM   4813 C  CE1  . TYR   A 1 314 ? -34.076 26.625  -17.933 1.00 19.22  ? 314 TYR   A CE1  1 
ATOM   4814 C  CE2  . TYR   A 1 314 ? -32.452 25.462  -16.680 1.00 18.41  ? 314 TYR   A CE2  1 
ATOM   4815 C  CZ   . TYR   A 1 314 ? -32.856 26.046  -17.834 1.00 20.48  ? 314 TYR   A CZ   1 
ATOM   4816 O  OH   . TYR   A 1 314 ? -32.047 26.065  -18.972 1.00 21.56  ? 314 TYR   A OH   1 
ATOM   4817 H  H    . TYR   A 1 314 ? -35.421 28.493  -13.889 1.00 22.33  ? 314 TYR   A H    1 
ATOM   4818 H  HA   . TYR   A 1 314 ? -37.104 26.850  -15.199 1.00 26.87  ? 314 TYR   A HA   1 
ATOM   4819 H  HB2  . TYR   A 1 314 ? -34.878 26.176  -13.617 1.00 21.40  ? 314 TYR   A HB2  1 
ATOM   4820 H  HB3  . TYR   A 1 314 ? -35.799 25.106  -14.344 1.00 21.40  ? 314 TYR   A HB3  1 
ATOM   4821 H  HD1  . TYR   A 1 314 ? -35.774 27.066  -16.864 1.00 22.47  ? 314 TYR   A HD1  1 
ATOM   4822 H  HD2  . TYR   A 1 314 ? -33.011 25.110  -14.803 1.00 20.74  ? 314 TYR   A HD2  1 
ATOM   4823 H  HE1  . TYR   A 1 314 ? -34.347 27.003  -18.738 1.00 23.07  ? 314 TYR   A HE1  1 
ATOM   4824 H  HE2  . TYR   A 1 314 ? -31.622 25.047  -16.622 1.00 22.09  ? 314 TYR   A HE2  1 
ATOM   4825 H  HH   . TYR   A 1 314 ? -31.307 25.704  -18.805 1.00 25.87  ? 314 TYR   A HH   1 
ATOM   4826 N  N    . ASN   A 1 315 ? -38.269 25.658  -13.258 1.00 19.97  ? 315 ASN   A N    1 
ATOM   4827 C  CA   . ASN   A 1 315 ? -39.320 25.396  -12.286 1.00 19.30  ? 315 ASN   A CA   1 
ATOM   4828 C  C    . ASN   A 1 315 ? -38.772 24.915  -10.954 1.00 20.43  ? 315 ASN   A C    1 
ATOM   4829 O  O    . ASN   A 1 315 ? -38.116 23.875  -10.885 1.00 19.44  ? 315 ASN   A O    1 
ATOM   4830 C  CB   . ASN   A 1 315 ? -40.266 24.343  -12.857 1.00 20.08  ? 315 ASN   A CB   1 
ATOM   4831 C  CG   . ASN   A 1 315 ? -41.455 24.110  -11.975 1.00 23.16  ? 315 ASN   A CG   1 
ATOM   4832 O  OD1  . ASN   A 1 315 ? -41.305 23.519  -10.931 1.00 23.43  ? 315 ASN   A OD1  1 
ATOM   4833 N  ND2  . ASN   A 1 315 ? -42.630 24.524  -12.399 1.00 30.16  ? 315 ASN   A ND2  1 
ATOM   4834 H  H    . ASN   A 1 315 ? -38.191 25.053  -13.864 1.00 23.97  ? 315 ASN   A H    1 
ATOM   4835 H  HA   . ASN   A 1 315 ? -39.790 26.227  -12.116 1.00 23.16  ? 315 ASN   A HA   1 
ATOM   4836 H  HB2  . ASN   A 1 315 ? -40.587 24.639  -13.723 1.00 24.09  ? 315 ASN   A HB2  1 
ATOM   4837 H  HB3  . ASN   A 1 315 ? -39.790 23.503  -12.949 1.00 24.09  ? 315 ASN   A HB3  1 
ATOM   4838 H  HD21 . ASN   A 1 315 ? -43.329 24.404  -11.914 1.00 36.19  ? 315 ASN   A HD21 1 
ATOM   4839 H  HD22 . ASN   A 1 315 ? -42.698 24.914  -13.163 1.00 36.19  ? 315 ASN   A HD22 1 
ATOM   4840 N  N    . LEU   A 1 316 ? -38.989 25.705  -9.898  1.00 20.05  ? 316 LEU   A N    1 
ATOM   4841 C  CA   . LEU   A 1 316 ? -38.392 25.416  -8.569  1.00 19.02  ? 316 LEU   A CA   1 
ATOM   4842 C  C    . LEU   A 1 316 ? -39.080 24.227  -7.891  1.00 19.98  ? 316 LEU   A C    1 
ATOM   4843 O  O    . LEU   A 1 316 ? -38.445 23.633  -7.024  1.00 19.87  ? 316 LEU   A O    1 
ATOM   4844 C  CB   . LEU   A 1 316 ? -38.493 26.672  -7.706  1.00 20.40  ? 316 LEU   A CB   1 
ATOM   4845 C  CG   . LEU   A 1 316 ? -37.789 27.919  -8.250  1.00 32.85  ? 316 LEU   A CG   1 
ATOM   4846 C  CD1  . LEU   A 1 316 ? -37.850 29.039  -7.232  1.00 38.13  ? 316 LEU   A CD1  1 
ATOM   4847 C  CD2  . LEU   A 1 316 ? -36.350 27.645  -8.647  1.00 28.97  ? 316 LEU   A CD2  1 
ATOM   4848 H  H    . LEU   A 1 316 ? -39.532 26.424  -9.940  1.00 24.05  ? 316 LEU   A H    1 
ATOM   4849 H  HA   . LEU   A 1 316 ? -37.437 25.188  -8.701  1.00 22.82  ? 316 LEU   A HA   1 
ATOM   4850 H  HB2  . LEU   A 1 316 ? -39.446 26.883  -7.583  1.00 24.48  ? 316 LEU   A HB2  1 
ATOM   4851 H  HB3  . LEU   A 1 316 ? -38.115 26.465  -6.820  1.00 24.48  ? 316 LEU   A HB3  1 
ATOM   4852 H  HG   . LEU   A 1 316 ? -38.276 28.218  -9.060  1.00 39.42  ? 316 LEU   A HG   1 
ATOM   4853 H  HD11 . LEU   A 1 316 ? -37.406 29.827  -7.589  1.00 45.75  ? 316 LEU   A HD11 1 
ATOM   4854 H  HD12 . LEU   A 1 316 ? -38.778 29.250  -7.037  1.00 45.75  ? 316 LEU   A HD12 1 
ATOM   4855 H  HD13 . LEU   A 1 316 ? -37.403 28.759  -6.416  1.00 45.75  ? 316 LEU   A HD13 1 
ATOM   4856 H  HD21 . LEU   A 1 316 ? -35.902 28.484  -8.842  1.00 34.77  ? 316 LEU   A HD21 1 
ATOM   4857 H  HD22 . LEU   A 1 316 ? -35.892 27.196  -7.917  1.00 34.77  ? 316 LEU   A HD22 1 
ATOM   4858 H  HD23 . LEU   A 1 316 ? -36.332 27.077  -9.436  1.00 34.77  ? 316 LEU   A HD23 1 
ATOM   4859 N  N    . ASP   A 1 317 ? -40.328 23.925  -8.246  1.00 18.23  ? 317 ASP   A N    1 
ATOM   4860 C  CA   . ASP   A 1 317 ? -41.051 22.766  -7.660  1.00 20.20  ? 317 ASP   A CA   1 
ATOM   4861 C  C    . ASP   A 1 317 ? -40.442 21.473  -8.200  1.00 19.63  ? 317 ASP   A C    1 
ATOM   4862 O  O    . ASP   A 1 317 ? -40.535 20.463  -7.502  1.00 22.53  ? 317 ASP   A O    1 
ATOM   4863 C  CB   . ASP   A 1 317 ? -42.546 22.828  -7.931  1.00 21.04  ? 317 ASP   A CB   1 
ATOM   4864 C  CG   . ASP   A 1 317 ? -43.371 23.636  -6.940  1.00 27.79  ? 317 ASP   A CG   1 
ATOM   4865 O  OD1  . ASP   A 1 317 ? -42.799 24.108  -5.938  1.00 26.74  ? 317 ASP   A OD1  1 
ATOM   4866 O  OD2  . ASP   A 1 317 ? -44.589 23.770  -7.170  1.00 47.99  ? 317 ASP   A OD2  1 
ATOM   4867 H  H    . ASP   A 1 317 ? -40.769 24.400  -8.873  1.00 21.87  ? 317 ASP   A H    1 
ATOM   4868 H  HA   . ASP   A 1 317 ? -40.914 22.780  -6.688  1.00 24.24  ? 317 ASP   A HA   1 
ATOM   4869 H  HB2  . ASP   A 1 317 ? -42.687 23.214  -8.820  1.00 25.25  ? 317 ASP   A HB2  1 
ATOM   4870 H  HB3  . ASP   A 1 317 ? -42.895 21.913  -7.944  1.00 25.25  ? 317 ASP   A HB3  1 
ATOM   4871 N  N    . ASP   A 1 318 ? -39.861 21.506  -9.398  1.00 18.88  ? 318 ASP   A N    1 
ATOM   4872 C  CA   . ASP   A 1 318 ? -39.198 20.308  -9.976  1.00 19.27  ? 318 ASP   A CA   1 
ATOM   4873 C  C    . ASP   A 1 318 ? -37.871 20.106  -9.251  1.00 18.74  ? 318 ASP   A C    1 
ATOM   4874 O  O    . ASP   A 1 318 ? -37.542 18.963  -9.007  1.00 16.62  ? 318 ASP   A O    1 
ATOM   4875 C  CB   . ASP   A 1 318 ? -39.053 20.413  -11.483 1.00 20.50  ? 318 ASP   A CB   1 
ATOM   4876 C  CG   . ASP   A 1 318 ? -40.385 20.362  -12.212 1.00 25.69  ? 318 ASP   A CG   1 
ATOM   4877 O  OD1  . ASP   A 1 318 ? -41.189 19.471  -11.882 1.00 29.92  ? 318 ASP   A OD1  1 
ATOM   4878 O  OD2  . ASP   A 1 318 ? -40.605 21.210  -13.091 1.00 28.07  ? 318 ASP   A OD2  1 
ATOM   4879 H  H    . ASP   A 1 318 ? -39.824 22.263  -9.887  1.00 22.66  ? 318 ASP   A H    1 
ATOM   4880 H  HA   . ASP   A 1 318 ? -39.765 19.527  -9.791  1.00 23.13  ? 318 ASP   A HA   1 
ATOM   4881 H  HB2  . ASP   A 1 318 ? -38.610 21.259  -11.703 1.00 24.60  ? 318 ASP   A HB2  1 
ATOM   4882 H  HB3  . ASP   A 1 318 ? -38.491 19.678  -11.805 1.00 24.60  ? 318 ASP   A HB3  1 
ATOM   4883 N  N    . ILE   A 1 319 ? -37.161 21.172  -8.898  1.00 16.73  ? 319 ILE   A N    1 
ATOM   4884 C  CA   . ILE   A 1 319 ? -35.941 21.043  -8.117  1.00 16.04  ? 319 ILE   A CA   1 
ATOM   4885 C  C    . ILE   A 1 319 ? -36.270 20.454  -6.738  1.00 14.79  ? 319 ILE   A C    1 
ATOM   4886 O  O    . ILE   A 1 319 ? -35.595 19.537  -6.244  1.00 14.00  ? 319 ILE   A O    1 
ATOM   4887 C  CB   . ILE   A 1 319 ? -35.264 22.420  -7.955  1.00 16.02  ? 319 ILE   A CB   1 
ATOM   4888 C  CG1  . ILE   A 1 319 ? -34.866 23.061  -9.302  1.00 18.76  ? 319 ILE   A CG1  1 
ATOM   4889 C  CG2  . ILE   A 1 319 ? -34.061 22.342  -7.043  1.00 17.28  ? 319 ILE   A CG2  1 
ATOM   4890 C  CD1  . ILE   A 1 319 ? -33.657 22.469  -9.913  1.00 17.28  ? 319 ILE   A CD1  1 
ATOM   4891 H  H    . ILE   A 1 319 ? -37.379 21.981  -9.093  1.00 20.08  ? 319 ILE   A H    1 
ATOM   4892 H  HA   . ILE   A 1 319 ? -35.335 20.448  -8.585  1.00 19.24  ? 319 ILE   A HA   1 
ATOM   4893 H  HB   . ILE   A 1 319 ? -35.934 22.992  -7.551  1.00 19.23  ? 319 ILE   A HB   1 
ATOM   4894 H  HG12 . ILE   A 1 319 ? -35.598 22.950  -9.928  1.00 22.51  ? 319 ILE   A HG12 1 
ATOM   4895 H  HG13 . ILE   A 1 319 ? -34.692 24.004  -9.158  1.00 22.51  ? 319 ILE   A HG13 1 
ATOM   4896 H  HG21 . ILE   A 1 319 ? -33.545 23.158  -7.131  1.00 20.73  ? 319 ILE   A HG21 1 
ATOM   4897 H  HG22 . ILE   A 1 319 ? -34.366 22.241  -6.127  1.00 20.73  ? 319 ILE   A HG22 1 
ATOM   4898 H  HG23 . ILE   A 1 319 ? -33.520 21.579  -7.298  1.00 20.73  ? 319 ILE   A HG23 1 
ATOM   4899 H  HD11 . ILE   A 1 319 ? -33.556 22.815  -10.813 1.00 20.74  ? 319 ILE   A HD11 1 
ATOM   4900 H  HD12 . ILE   A 1 319 ? -32.883 22.707  -9.378  1.00 20.74  ? 319 ILE   A HD12 1 
ATOM   4901 H  HD13 . ILE   A 1 319 ? -33.757 21.504  -9.939  1.00 20.74  ? 319 ILE   A HD13 1 
ATOM   4902 N  N    . LYS   A 1 320 ? -37.316 20.985  -6.095  1.00 14.88  ? 320 LYS   A N    1 
ATOM   4903 C  CA   . LYS   A 1 320 ? -37.675 20.545  -4.755  1.00 14.45  ? 320 LYS   A CA   1 
ATOM   4904 C  C    . LYS   A 1 320 ? -38.092 19.096  -4.750  1.00 14.36  ? 320 LYS   A C    1 
ATOM   4905 O  O    . LYS   A 1 320 ? -37.717 18.362  -3.830  1.00 14.32  ? 320 LYS   A O    1 
ATOM   4906 C  CB   . LYS   A 1 320 ? -38.767 21.454  -4.231  1.00 15.07  ? 320 LYS   A CB   1 
ATOM   4907 C  CG   . LYS   A 1 320 ? -38.276 22.855  -3.825  1.00 16.22  ? 320 LYS   A CG   1 
ATOM   4908 C  CD   . LYS   A 1 320 ? -39.438 23.769  -3.453  1.00 18.03  ? 320 LYS   A CD   1 
ATOM   4909 C  CE   . LYS   A 1 320 ? -38.793 25.065  -3.059  1.00 18.75  ? 320 LYS   A CE   1 
ATOM   4910 N  NZ   . LYS   A 1 320 ? -39.905 25.966  -2.651  1.00 21.80  ? 320 LYS   A NZ   1 
ATOM   4911 H  H    . LYS   A 1 320 ? -37.828 21.598  -6.415  1.00 17.86  ? 320 LYS   A H    1 
ATOM   4912 H  HA   . LYS   A 1 320 ? -36.913 20.614  -4.158  1.00 17.34  ? 320 LYS   A HA   1 
ATOM   4913 H  HB2  . LYS   A 1 320 ? -39.437 21.565  -4.923  1.00 18.08  ? 320 LYS   A HB2  1 
ATOM   4914 H  HB3  . LYS   A 1 320 ? -39.164 21.042  -3.448  1.00 18.08  ? 320 LYS   A HB3  1 
ATOM   4915 H  HG2  . LYS   A 1 320 ? -37.690 22.779  -3.057  1.00 19.47  ? 320 LYS   A HG2  1 
ATOM   4916 H  HG3  . LYS   A 1 320 ? -37.799 23.256  -4.569  1.00 19.47  ? 320 LYS   A HG3  1 
ATOM   4917 H  HD2  . LYS   A 1 320 ? -40.027 23.908  -4.212  1.00 21.64  ? 320 LYS   A HD2  1 
ATOM   4918 H  HD3  . LYS   A 1 320 ? -39.939 23.406  -2.706  1.00 21.64  ? 320 LYS   A HD3  1 
ATOM   4919 H  HE2  . LYS   A 1 320 ? -38.187 24.932  -2.313  1.00 22.49  ? 320 LYS   A HE2  1 
ATOM   4920 H  HE3  . LYS   A 1 320 ? -38.316 25.452  -3.810  1.00 22.49  ? 320 LYS   A HE3  1 
ATOM   4921 H  HZ1  . LYS   A 1 320 ? -40.463 26.089  -3.333  1.00 26.16  ? 320 LYS   A HZ1  1 
ATOM   4922 H  HZ2  . LYS   A 1 320 ? -40.354 25.606  -1.972  1.00 26.16  ? 320 LYS   A HZ2  1 
ATOM   4923 H  HZ3  . LYS   A 1 320 ? -39.580 26.754  -2.397  1.00 26.16  ? 320 LYS   A HZ3  1 
ATOM   4924 N  N    . LYS   A 1 321 ? -38.858 18.656  -5.738  1.00 15.04  ? 321 LYS   A N    1 
ATOM   4925 C  CA   . LYS   A 1 321 ? -39.217 17.247  -5.795  1.00 15.59  ? 321 LYS   A CA   1 
ATOM   4926 C  C    . LYS   A 1 321 ? -37.972 16.372  -5.898  1.00 15.89  ? 321 LYS   A C    1 
ATOM   4927 O  O    . LYS   A 1 321 ? -37.878 15.331  -5.240  1.00 16.33  ? 321 LYS   A O    1 
ATOM   4928 C  CB   . LYS   A 1 321 ? -40.142 16.977  -6.982  1.00 16.27  ? 321 LYS   A CB   1 
ATOM   4929 C  CG   . LYS   A 1 321 ? -40.636 15.541  -7.088  1.00 20.07  ? 321 LYS   A CG   1 
ATOM   4930 C  CD   . LYS   A 1 321 ? -41.646 15.345  -8.205  1.00 25.67  ? 321 LYS   A CD   1 
ATOM   4931 C  CE   . LYS   A 1 321 ? -42.056 13.868  -8.166  1.00 35.72  ? 321 LYS   A CE   1 
ATOM   4932 N  NZ   . LYS   A 1 321 ? -43.301 13.611  -8.913  1.00 45.18  ? 321 LYS   A NZ   1 
ATOM   4933 H  H    . LYS   A 1 321 ? -39.177 19.140  -6.374  1.00 18.04  ? 321 LYS   A H    1 
ATOM   4934 H  HA   . LYS   A 1 321 ? -39.695 17.020  -4.982  1.00 18.71  ? 321 LYS   A HA   1 
ATOM   4935 H  HB2  . LYS   A 1 321 ? -40.921 17.549  -6.902  1.00 19.52  ? 321 LYS   A HB2  1 
ATOM   4936 H  HB3  . LYS   A 1 321 ? -39.662 17.182  -7.799  1.00 19.52  ? 321 LYS   A HB3  1 
ATOM   4937 H  HG2  . LYS   A 1 321 ? -39.880 14.959  -7.262  1.00 24.08  ? 321 LYS   A HG2  1 
ATOM   4938 H  HG3  . LYS   A 1 321 ? -41.062 15.291  -6.253  1.00 24.08  ? 321 LYS   A HG3  1 
ATOM   4939 H  HD2  . LYS   A 1 321 ? -42.425 15.904  -8.061  1.00 30.81  ? 321 LYS   A HD2  1 
ATOM   4940 H  HD3  . LYS   A 1 321 ? -41.245 15.549  -9.065  1.00 30.81  ? 321 LYS   A HD3  1 
ATOM   4941 H  HE2  . LYS   A 1 321 ? -41.351 13.332  -8.562  1.00 42.87  ? 321 LYS   A HE2  1 
ATOM   4942 H  HE3  . LYS   A 1 321 ? -42.198 13.602  -7.244  1.00 42.87  ? 321 LYS   A HE3  1 
ATOM   4943 H  HZ1  . LYS   A 1 321 ? -43.513 12.748  -8.864  1.00 54.22  ? 321 LYS   A HZ1  1 
ATOM   4944 H  HZ2  . LYS   A 1 321 ? -43.967 14.092  -8.570  1.00 54.22  ? 321 LYS   A HZ2  1 
ATOM   4945 H  HZ3  . LYS   A 1 321 ? -43.195 13.833  -9.768  1.00 54.22  ? 321 LYS   A HZ3  1 
ATOM   4946 N  N    . SER   A 1 322 ? -37.008 16.809  -6.712  1.00 14.31  ? 322 SER   A N    1 
ATOM   4947 C  CA   . SER   A 1 322 ? -35.784 16.026  -6.896  1.00 13.80  ? 322 SER   A CA   1 
ATOM   4948 C  C    . SER   A 1 322 ? -34.975 15.977  -5.615  1.00 14.45  ? 322 SER   A C    1 
ATOM   4949 O  O    . SER   A 1 322 ? -34.465 14.921  -5.225  1.00 14.53  ? 322 SER   A O    1 
ATOM   4950 C  CB   . SER   A 1 322 ? -34.971 16.627  -8.046  1.00 14.42  ? 322 SER   A CB   1 
ATOM   4951 O  OG   . SER   A 1 322 ? -35.763 16.627  -9.246  1.00 15.35  ? 322 SER   A OG   1 
ATOM   4952 H  H    . SER   A 1 322 ? -37.037 17.541  -7.161  1.00 17.18  ? 322 SER   A H    1 
ATOM   4953 H  HA   . SER   A 1 322 ? -36.011 15.112  -7.131  1.00 16.56  ? 322 SER   A HA   1 
ATOM   4954 H  HB2  . SER   A 1 322 ? -34.725 17.538  -7.823  1.00 17.30  ? 322 SER   A HB2  1 
ATOM   4955 H  HB3  . SER   A 1 322 ? -34.173 16.093  -8.188  1.00 17.30  ? 322 SER   A HB3  1 
ATOM   4956 H  HG   . SER   A 1 322 ? -36.451 17.097  -9.136  1.00 18.41  ? 322 SER   A HG   1 
ATOM   4957 N  N    . LEU   A 1 323 ? -34.815 17.124  -4.947  1.00 13.09  ? 323 LEU   A N    1 
ATOM   4958 C  CA   . LEU   A 1 323 ? -34.094 17.159  -3.654  1.00 12.69  ? 323 LEU   A CA   1 
ATOM   4959 C  C    . LEU   A 1 323 ? -34.772 16.255  -2.638  1.00 14.62  ? 323 LEU   A C    1 
ATOM   4960 O  O    . LEU   A 1 323 ? -34.103 15.513  -1.912  1.00 15.00  ? 323 LEU   A O    1 
ATOM   4961 C  CB   . LEU   A 1 323 ? -34.078 18.617  -3.098  1.00 13.09  ? 323 LEU   A CB   1 
ATOM   4962 C  CG   . LEU   A 1 323 ? -33.229 19.602  -3.884  1.00 13.49  ? 323 LEU   A CG   1 
ATOM   4963 C  CD1  . LEU   A 1 323 ? -33.375 21.016  -3.315  1.00 14.40  ? 323 LEU   A CD1  1 
ATOM   4964 C  CD2  . LEU   A 1 323 ? -31.809 19.227  -3.905  1.00 15.14  ? 323 LEU   A CD2  1 
ATOM   4965 H  H    . LEU   A 1 323 ? -35.107 17.889  -5.209  1.00 15.71  ? 323 LEU   A H    1 
ATOM   4966 H  HA   . LEU   A 1 323 ? -33.182 16.860  -3.797  1.00 15.23  ? 323 LEU   A HA   1 
ATOM   4967 H  HB2  . LEU   A 1 323 ? -34.987 18.954  -3.098  1.00 15.71  ? 323 LEU   A HB2  1 
ATOM   4968 H  HB3  . LEU   A 1 323 ? -33.732 18.595  -2.192  1.00 15.71  ? 323 LEU   A HB3  1 
ATOM   4969 H  HG   . LEU   A 1 323 ? -33.549 19.588  -4.800  1.00 16.19  ? 323 LEU   A HG   1 
ATOM   4970 H  HD11 . LEU   A 1 323 ? -32.833 21.625  -3.840  1.00 17.28  ? 323 LEU   A HD11 1 
ATOM   4971 H  HD12 . LEU   A 1 323 ? -34.307 21.280  -3.359  1.00 17.28  ? 323 LEU   A HD12 1 
ATOM   4972 H  HD13 . LEU   A 1 323 ? -33.075 21.017  -2.392  1.00 17.28  ? 323 LEU   A HD13 1 
ATOM   4973 H  HD21 . LEU   A 1 323 ? -31.302 19.936  -4.330  1.00 18.17  ? 323 LEU   A HD21 1 
ATOM   4974 H  HD22 . LEU   A 1 323 ? -31.503 19.100  -2.994  1.00 18.17  ? 323 LEU   A HD22 1 
ATOM   4975 H  HD23 . LEU   A 1 323 ? -31.708 18.402  -4.406  1.00 18.17  ? 323 LEU   A HD23 1 
ATOM   4976 N  N    . SER   A 1 324 ? -36.080 16.308  -2.586  1.00 14.59  ? 324 SER   A N    1 
ATOM   4977 C  CA   . SER   A 1 324 ? -36.807 15.460  -1.641  1.00 17.12  ? 324 SER   A CA   1 
ATOM   4978 C  C    . SER   A 1 324 ? -36.566 13.982  -1.909  1.00 16.04  ? 324 SER   A C    1 
ATOM   4979 O  O    . SER   A 1 324 ? -36.458 13.185  -0.970  1.00 18.04  ? 324 SER   A O    1 
ATOM   4980 C  CB   . SER   A 1 324 ? -38.302 15.764  -1.665  1.00 17.53  ? 324 SER   A CB   1 
ATOM   4981 O  OG   . SER   A 1 324 ? -38.589 17.033  -1.031  1.00 22.27  ? 324 SER   A OG   1 
ATOM   4982 H  H    . SER   A 1 324 ? -36.575 16.815  -3.074  1.00 17.51  ? 324 SER   A H    1 
ATOM   4983 H  HA   . SER   A 1 324 ? -36.480 15.666  -0.751  1.00 20.55  ? 324 SER   A HA   1 
ATOM   4984 H  HB2  . SER   A 1 324 ? -38.601 15.798  -2.587  1.00 21.03  ? 324 SER   A HB2  1 
ATOM   4985 H  HB3  . SER   A 1 324 ? -38.773 15.062  -1.189  1.00 21.03  ? 324 SER   A HB3  1 
ATOM   4986 H  HG   . SER   A 1 324 ? -39.417 17.177  -1.040  1.00 26.72  ? 324 SER   A HG   1 
ATOM   4987 N  N    . GLU   A 1 325 ? -36.488 13.589  -3.186  1.00 16.79  ? 325 GLU   A N    1 
ATOM   4988 C  CA   . GLU   A 1 325 ? -36.291 12.184  -3.515  1.00 16.74  ? 325 GLU   A CA   1 
ATOM   4989 C  C    . GLU   A 1 325 ? -34.947 11.697  -3.042  1.00 16.28  ? 325 GLU   A C    1 
ATOM   4990 O  O    . GLU   A 1 325 ? -34.831 10.505  -2.727  1.00 19.10  ? 325 GLU   A O    1 
ATOM   4991 C  CB   . GLU   A 1 325 ? -36.417 11.997  -5.027  1.00 20.70  ? 325 GLU   A CB   1 
ATOM   4992 C  CG   . GLU   A 1 325 ? -37.833 12.036  -5.514  1.00 27.92  ? 325 GLU   A CG   1 
ATOM   4993 C  CD   . GLU   A 1 325 ? -37.923 11.754  -6.979  1.00 38.23  ? 325 GLU   A CD   1 
ATOM   4994 O  OE1  . GLU   A 1 325 ? -37.337 10.735  -7.384  1.00 27.60  ? 325 GLU   A OE1  1 
ATOM   4995 O  OE2  . GLU   A 1 325 ? -38.542 12.572  -7.700  1.00 35.37  ? 325 GLU   A OE2  1 
ATOM   4996 H  H    . GLU   A 1 325 ? -36.545 14.111  -3.867  1.00 20.14  ? 325 GLU   A H    1 
ATOM   4997 H  HA   . GLU   A 1 325 ? -36.976 11.652  -3.080  1.00 20.08  ? 325 GLU   A HA   1 
ATOM   4998 H  HB2  . GLU   A 1 325 ? -35.929 12.706  -5.473  1.00 24.84  ? 325 GLU   A HB2  1 
ATOM   4999 H  HB3  . GLU   A 1 325 ? -36.043 11.135  -5.268  1.00 24.84  ? 325 GLU   A HB3  1 
ATOM   5000 H  HG2  . GLU   A 1 325 ? -38.352 11.365  -5.043  1.00 33.51  ? 325 GLU   A HG2  1 
ATOM   5001 H  HG3  . GLU   A 1 325 ? -38.203 12.917  -5.351  1.00 33.51  ? 325 GLU   A HG3  1 
ATOM   5002 N  N    . VAL   A 1 326 ? -33.940 12.574  -2.903  1.00 14.79  ? 326 VAL   A N    1 
ATOM   5003 C  CA   . VAL   A 1 326 ? -32.633 12.172  -2.366  1.00 14.48  ? 326 VAL   A CA   1 
ATOM   5004 C  C    . VAL   A 1 326 ? -32.476 12.573  -0.894  1.00 15.15  ? 326 VAL   A C    1 
ATOM   5005 O  O    . VAL   A 1 326 ? -31.380 12.591  -0.365  1.00 16.86  ? 326 VAL   A O    1 
ATOM   5006 C  CB   . VAL   A 1 326 ? -31.442 12.637  -3.213  1.00 13.94  ? 326 VAL   A CB   1 
ATOM   5007 C  CG1  . VAL   A 1 326 ? -31.525 12.040  -4.585  1.00 16.24  ? 326 VAL   A CG1  1 
ATOM   5008 C  CG2  . VAL   A 1 326 ? -31.370 14.141  -3.323  1.00 14.47  ? 326 VAL   A CG2  1 
ATOM   5009 H  H    . VAL   A 1 326 ? -33.992 13.407  -3.113  1.00 17.75  ? 326 VAL   A H    1 
ATOM   5010 H  HA   . VAL   A 1 326 ? -32.614 11.203  -2.405  1.00 17.38  ? 326 VAL   A HA   1 
ATOM   5011 H  HB   . VAL   A 1 326 ? -30.633 12.338  -2.770  1.00 16.73  ? 326 VAL   A HB   1 
ATOM   5012 H  HG11 . VAL   A 1 326 ? -30.783 12.366  -5.117  1.00 19.49  ? 326 VAL   A HG11 1 
ATOM   5013 H  HG12 . VAL   A 1 326 ? -31.481 11.073  -4.512  1.00 19.49  ? 326 VAL   A HG12 1 
ATOM   5014 H  HG13 . VAL   A 1 326 ? -32.365 12.302  -4.993  1.00 19.49  ? 326 VAL   A HG13 1 
ATOM   5015 H  HG21 . VAL   A 1 326 ? -30.588 14.383  -3.843  1.00 17.36  ? 326 VAL   A HG21 1 
ATOM   5016 H  HG22 . VAL   A 1 326 ? -32.172 14.465  -3.762  1.00 17.36  ? 326 VAL   A HG22 1 
ATOM   5017 H  HG23 . VAL   A 1 326 ? -31.305 14.521  -2.432  1.00 17.36  ? 326 VAL   A HG23 1 
ATOM   5018 N  N    . THR   A 1 327 ? -33.564 12.871  -0.255  1.00 14.69  ? 327 THR   A N    1 
ATOM   5019 C  CA   . THR   A 1 327 ? -33.684 13.235  1.163   1.00 16.36  ? 327 THR   A CA   1 
ATOM   5020 C  C    . THR   A 1 327 ? -32.851 14.457  1.561   1.00 16.83  ? 327 THR   A C    1 
ATOM   5021 O  O    . THR   A 1 327 ? -32.374 14.563  2.716   1.00 19.74  ? 327 THR   A O    1 
ATOM   5022 C  CB   . THR   A 1 327 ? -33.493 12.071  2.154   1.00 17.21  ? 327 THR   A CB   1 
ATOM   5023 O  OG1  . THR   A 1 327 ? -32.109 11.737  2.257   1.00 20.09  ? 327 THR   A OG1  1 
ATOM   5024 C  CG2  . THR   A 1 327 ? -34.273 10.867  1.732   1.00 19.73  ? 327 THR   A CG2  1 
ATOM   5025 H  H    . THR   A 1 327 ? -34.334 12.876  -0.638  1.00 17.63  ? 327 THR   A H    1 
ATOM   5026 H  HA   . THR   A 1 327 ? -34.613 13.496  1.262   1.00 19.63  ? 327 THR   A HA   1 
ATOM   5027 H  HB   . THR   A 1 327 ? -33.820 12.344  3.025   1.00 20.66  ? 327 THR   A HB   1 
ATOM   5028 H  HG1  . THR   A 1 327 ? -31.786 11.610  1.492   1.00 24.11  ? 327 THR   A HG1  1 
ATOM   5029 H  HG21 . THR   A 1 327 ? -34.181 10.164  2.394   1.00 23.68  ? 327 THR   A HG21 1 
ATOM   5030 H  HG22 . THR   A 1 327 ? -35.212 11.094  1.643   1.00 23.68  ? 327 THR   A HG22 1 
ATOM   5031 H  HG23 . THR   A 1 327 ? -33.945 10.541  0.879   1.00 23.68  ? 327 THR   A HG23 1 
ATOM   5032 N  N    . ILE   A 1 328 ? -32.703 15.427  0.684   1.00 14.72  ? 328 ILE   A N    1 
ATOM   5033 C  CA   . ILE   A 1 328 ? -32.090 16.720  1.019   1.00 14.77  ? 328 ILE   A CA   1 
ATOM   5034 C  C    . ILE   A 1 328 ? -33.200 17.620  1.525   1.00 15.95  ? 328 ILE   A C    1 
ATOM   5035 O  O    . ILE   A 1 328 ? -34.261 17.723  0.895   1.00 17.56  ? 328 ILE   A O    1 
ATOM   5036 C  CB   . ILE   A 1 328 ? -31.391 17.311  -0.216  1.00 14.76  ? 328 ILE   A CB   1 
ATOM   5037 C  CG1  . ILE   A 1 328 ? -30.084 16.512  -0.447  1.00 15.42  ? 328 ILE   A CG1  1 
ATOM   5038 C  CG2  . ILE   A 1 328 ? -31.171 18.805  -0.031  1.00 18.43  ? 328 ILE   A CG2  1 
ATOM   5039 C  CD1  . ILE   A 1 328 ? -29.344 16.791  -1.720  1.00 15.30  ? 328 ILE   A CD1  1 
ATOM   5040 H  H    . ILE   A 1 328 ? -32.953 15.371  -0.137  1.00 17.67  ? 328 ILE   A H    1 
ATOM   5041 H  HA   . ILE   A 1 328 ? -31.424 16.623  1.718   1.00 17.72  ? 328 ILE   A HA   1 
ATOM   5042 H  HB   . ILE   A 1 328 ? -31.940 17.225  -1.010  1.00 17.71  ? 328 ILE   A HB   1 
ATOM   5043 H  HG12 . ILE   A 1 328 ? -29.477 16.710  0.283   1.00 18.51  ? 328 ILE   A HG12 1 
ATOM   5044 H  HG13 . ILE   A 1 328 ? -30.305 15.568  -0.448  1.00 18.51  ? 328 ILE   A HG13 1 
ATOM   5045 H  HG21 . ILE   A 1 328 ? -30.517 19.111  -0.679  1.00 22.12  ? 328 ILE   A HG21 1 
ATOM   5046 H  HG22 . ILE   A 1 328 ? -32.013 19.267  -0.167  1.00 22.12  ? 328 ILE   A HG22 1 
ATOM   5047 H  HG23 . ILE   A 1 328 ? -30.846 18.968  0.869   1.00 22.12  ? 328 ILE   A HG23 1 
ATOM   5048 H  HD11 . ILE   A 1 328 ? -28.652 16.121  -1.836  1.00 18.36  ? 328 ILE   A HD11 1 
ATOM   5049 H  HD12 . ILE   A 1 328 ? -29.968 16.754  -2.462  1.00 18.36  ? 328 ILE   A HD12 1 
ATOM   5050 H  HD13 . ILE   A 1 328 ? -28.945 17.673  -1.667  1.00 18.36  ? 328 ILE   A HD13 1 
ATOM   5051 N  N    . ASN   A 1 329 ? -32.959 18.310  2.613   1.00 13.86  ? 329 ASN   A N    1 
ATOM   5052 C  CA   . ASN   A 1 329 ? -33.905 19.221  3.243   1.00 14.54  ? 329 ASN   A CA   1 
ATOM   5053 C  C    . ASN   A 1 329 ? -33.608 20.637  2.776   1.00 13.94  ? 329 ASN   A C    1 
ATOM   5054 O  O    . ASN   A 1 329 ? -32.445 21.068  2.734   1.00 16.85  ? 329 ASN   A O    1 
ATOM   5055 C  CB   . ASN   A 1 329 ? -33.716 19.143  4.778   1.00 15.88  ? 329 ASN   A CB   1 
ATOM   5056 C  CG   . ASN   A 1 329 ? -34.719 20.017  5.500   1.00 18.14  ? 329 ASN   A CG   1 
ATOM   5057 O  OD1  . ASN   A 1 329 ? -34.572 21.259  5.588   1.00 20.17  ? 329 ASN   A OD1  1 
ATOM   5058 N  ND2  . ASN   A 1 329 ? -35.673 19.372  6.104   1.00 18.68  ? 329 ASN   A ND2  1 
ATOM   5059 H  H    . ASN   A 1 329 ? -32.212 18.271  3.037   1.00 16.63  ? 329 ASN   A H    1 
ATOM   5060 H  HA   . ASN   A 1 329 ? -34.820 18.999  3.010   1.00 17.44  ? 329 ASN   A HA   1 
ATOM   5061 H  HB2  . ASN   A 1 329 ? -33.842 18.227  5.071   1.00 19.05  ? 329 ASN   A HB2  1 
ATOM   5062 H  HB3  . ASN   A 1 329 ? -32.824 19.446  5.008   1.00 19.05  ? 329 ASN   A HB3  1 
ATOM   5063 H  HD21 . ASN   A 1 329 ? -36.279 19.804  6.535   1.00 22.41  ? 329 ASN   A HD21 1 
ATOM   5064 H  HD22 . ASN   A 1 329 ? -35.698 18.513  6.072   1.00 22.41  ? 329 ASN   A HD22 1 
ATOM   5065 N  N    . TYR   A 1 330 ? -34.667 21.373  2.466   1.00 14.22  ? 330 TYR   A N    1 
ATOM   5066 C  CA   . TYR   A 1 330 ? -34.591 22.746  1.958   1.00 13.77  ? 330 TYR   A CA   1 
ATOM   5067 C  C    . TYR   A 1 330 ? -35.513 23.660  2.763   1.00 17.44  ? 330 TYR   A C    1 
ATOM   5068 O  O    . TYR   A 1 330 ? -35.866 24.738  2.290   1.00 17.50  ? 330 TYR   A O    1 
ATOM   5069 C  CB   . TYR   A 1 330 ? -34.844 22.866  0.442   1.00 15.05  ? 330 TYR   A CB   1 
ATOM   5070 C  CG   . TYR   A 1 330 ? -36.032 22.053  -0.014  1.00 13.66  ? 330 TYR   A CG   1 
ATOM   5071 C  CD1  . TYR   A 1 330 ? -37.327 22.541  -0.026  1.00 14.55  ? 330 TYR   A CD1  1 
ATOM   5072 C  CD2  . TYR   A 1 330 ? -35.837 20.721  -0.369  1.00 14.36  ? 330 TYR   A CD2  1 
ATOM   5073 C  CE1  . TYR   A 1 330 ? -38.413 21.722  -0.376  1.00 15.51  ? 330 TYR   A CE1  1 
ATOM   5074 C  CE2  . TYR   A 1 330 ? -36.923 19.932  -0.759  1.00 14.28  ? 330 TYR   A CE2  1 
ATOM   5075 C  CZ   . TYR   A 1 330 ? -38.165 20.439  -0.779  1.00 14.68  ? 330 TYR   A CZ   1 
ATOM   5076 O  OH   . TYR   A 1 330 ? -39.265 19.659  -1.125  1.00 17.57  ? 330 TYR   A OH   1 
ATOM   5077 H  H    . TYR   A 1 330 ? -35.477 21.093  2.543   1.00 17.07  ? 330 TYR   A H    1 
ATOM   5078 H  HA   . TYR   A 1 330 ? -33.678 23.055  2.064   1.00 16.53  ? 330 TYR   A HA   1 
ATOM   5079 H  HB2  . TYR   A 1 330 ? -35.013 23.796  0.222   1.00 18.06  ? 330 TYR   A HB2  1 
ATOM   5080 H  HB3  . TYR   A 1 330 ? -34.061 22.549  -0.035  1.00 18.06  ? 330 TYR   A HB3  1 
ATOM   5081 H  HD1  . TYR   A 1 330 ? -37.481 23.429  0.203   1.00 17.47  ? 330 TYR   A HD1  1 
ATOM   5082 H  HD2  . TYR   A 1 330 ? -34.982 20.356  -0.346  1.00 17.24  ? 330 TYR   A HD2  1 
ATOM   5083 H  HE1  . TYR   A 1 330 ? -39.284 22.046  -0.334  1.00 18.61  ? 330 TYR   A HE1  1 
ATOM   5084 H  HE2  . TYR   A 1 330 ? -36.784 19.046  -1.007  1.00 17.13  ? 330 TYR   A HE2  1 
ATOM   5085 H  HH   . TYR   A 1 330 ? -39.008 18.914  -1.417  1.00 21.08  ? 330 TYR   A HH   1 
ATOM   5086 N  N    . GLN   A 1 331 ? -35.948 23.258  3.983   1.00 15.97  ? 331 GLN   A N    1 
ATOM   5087 C  CA   . GLN   A 1 331 ? -36.926 24.055  4.722   1.00 17.40  ? 331 GLN   A CA   1 
ATOM   5088 C  C    . GLN   A 1 331 ? -36.360 25.412  5.093   1.00 23.24  ? 331 GLN   A C    1 
ATOM   5089 O  O    . GLN   A 1 331 ? -37.153 26.355  5.231   1.00 27.85  ? 331 GLN   A O    1 
ATOM   5090 C  CB   . GLN   A 1 331 ? -37.525 23.233  5.941   1.00 19.63  ? 331 GLN   A CB   1 
ATOM   5091 C  CG   . GLN   A 1 331 ? -38.320 21.975  5.411   1.00 24.47  ? 331 GLN   A CG   1 
ATOM   5092 C  CD   . GLN   A 1 331 ? -39.078 21.165  6.479   1.00 24.65  ? 331 GLN   A CD   1 
ATOM   5093 O  OE1  . GLN   A 1 331 ? -39.499 21.711  7.459   1.00 19.25  ? 331 GLN   A OE1  1 
ATOM   5094 N  NE2  . GLN   A 1 331 ? -39.386 19.875  6.158   1.00 33.33  ? 331 GLN   A NE2  1 
ATOM   5095 H  H    . GLN   A 1 331 ? -35.692 22.542  4.385   1.00 19.16  ? 331 GLN   A H    1 
ATOM   5096 H  HA   . GLN   A 1 331 ? -37.704 24.239  4.172   1.00 20.88  ? 331 GLN   A HA   1 
ATOM   5097 H  HB2  . GLN   A 1 331 ? -36.804 22.927  6.513   1.00 23.55  ? 331 GLN   A HB2  1 
ATOM   5098 H  HB3  . GLN   A 1 331 ? -38.133 23.795  6.446   1.00 23.55  ? 331 GLN   A HB3  1 
ATOM   5099 H  HG2  . GLN   A 1 331 ? -38.974 22.279  4.763   1.00 29.37  ? 331 GLN   A HG2  1 
ATOM   5100 H  HG3  . GLN   A 1 331 ? -37.689 21.372  4.988   1.00 29.37  ? 331 GLN   A HG3  1 
ATOM   5101 H  HE21 . GLN   A 1 331 ? -39.157 19.556  5.393   1.00 40.00  ? 331 GLN   A HE21 1 
ATOM   5102 H  HE22 . GLN   A 1 331 ? -39.809 19.381  6.720   1.00 40.00  ? 331 GLN   A HE22 1 
ATOM   5103 N  N    . SER   A 1 332 ? -35.032 25.539  5.183   1.00 20.91  ? 332 SER   A N    1 
ATOM   5104 C  CA   . SER   A 1 332 ? -34.369 26.806  5.590   1.00 29.06  ? 332 SER   A CA   1 
ATOM   5105 C  C    . SER   A 1 332 ? -33.964 27.638  4.364   1.00 26.83  ? 332 SER   A C    1 
ATOM   5106 O  O    . SER   A 1 332 ? -33.464 28.763  4.566   1.00 27.71  ? 332 SER   A O    1 
ATOM   5107 C  CB   . SER   A 1 332 ? -33.171 26.520  6.460   1.00 29.33  ? 332 SER   A CB   1 
ATOM   5108 O  OG   . SER   A 1 332 ? -31.993 26.347  5.687   1.00 31.50  ? 332 SER   A OG   1 
ATOM   5109 H  H    . SER   A 1 332 ? -34.472 24.863  4.977   1.00 25.09  ? 332 SER   A H    1 
ATOM   5110 H  HA   . SER   A 1 332 ? -35.015 27.335  6.121   1.00 34.88  ? 332 SER   A HA   1 
ATOM   5111 H  HB2  . SER   A 1 332 ? -33.043 27.260  7.083   1.00 35.19  ? 332 SER   A HB2  1 
ATOM   5112 H  HB3  . SER   A 1 332 ? -33.338 25.712  6.980   1.00 35.19  ? 332 SER   A HB3  1 
ATOM   5113 H  HG   . SER   A 1 332 ? -32.110 25.703  5.154   1.00 37.80  ? 332 SER   A HG   1 
ATOM   5114 N  N    . CYS   A 1 333 ? -34.168 27.118  3.151   1.00 21.15  ? 333 CYS   A N    1 
ATOM   5115 C  CA   A CYS   A 1 333 ? -33.699 27.875  1.908   0.53 23.27  ? 333 CYS   A CA   1 
ATOM   5116 C  CA   B CYS   A 1 333 ? -33.702 27.855  1.939   0.47 23.28  ? 333 CYS   A CA   1 
ATOM   5117 C  C    . CYS   A 1 333 ? -34.578 29.073  1.536   1.00 31.60  ? 333 CYS   A C    1 
ATOM   5118 O  O    . CYS   A 1 333 ? -35.572 28.976  0.741   1.00 28.17  ? 333 CYS   A O    1 
ATOM   5119 C  CB   A CYS   A 1 333 ? -33.668 26.945  0.714   0.53 19.85  ? 333 CYS   A CB   1 
ATOM   5120 C  CB   B CYS   A 1 333 ? -33.582 26.914  0.745   0.47 19.84  ? 333 CYS   A CB   1 
ATOM   5121 S  SG   A CYS   A 1 333 ? -32.622 25.567  0.750   0.53 19.50  ? 333 CYS   A SG   1 
ATOM   5122 S  SG   B CYS   A 1 333 ? -32.796 27.692  -0.691  0.47 19.37  ? 333 CYS   A SG   1 
ATOM   5123 H  H    A CYS   A 1 333 ? -34.612 26.443  2.918   0.53 25.38  ? 333 CYS   A H    1 
ATOM   5124 H  H    B CYS   A 1 333 ? -34.952 26.709  2.974   0.47 25.38  ? 333 CYS   A H    1 
ATOM   5125 H  HA   A CYS   A 1 333 ? -32.817 28.218  2.122   0.53 27.92  ? 333 CYS   A HA   1 
ATOM   5126 H  HA   B CYS   A 1 333 ? -32.791 28.189  2.131   0.47 27.94  ? 333 CYS   A HA   1 
ATOM   5127 H  HB2  A CYS   A 1 333 ? -34.567 26.603  0.588   0.53 23.82  ? 333 CYS   A HB2  1 
ATOM   5128 H  HB2  B CYS   A 1 333 ? -33.051 26.129  1.006   0.47 23.80  ? 333 CYS   A HB2  1 
ATOM   5129 H  HB3  A CYS   A 1 333 ? -33.402 27.470  -0.057  0.53 23.82  ? 333 CYS   A HB3  1 
ATOM   5130 H  HB3  B CYS   A 1 333 ? -34.477 26.602  0.485   0.47 23.80  ? 333 CYS   A HB3  1 
ATOM   5131 N  N    . TYR   A 1 334 ? -34.315 30.206  2.190   1.00 31.44  ? 334 TYR   A N    1 
ATOM   5132 C  CA   . TYR   A 1 334 ? -35.053 31.469  1.913   1.00 39.46  ? 334 TYR   A CA   1 
ATOM   5133 C  C    . TYR   A 1 334 ? -34.051 32.620  1.926   1.00 40.28  ? 334 TYR   A C    1 
ATOM   5134 O  O    . TYR   A 1 334 ? -33.312 32.732  2.900   1.00 40.56  ? 334 TYR   A O    1 
ATOM   5135 C  CB   . TYR   A 1 334 ? -36.157 31.702  2.948   1.00 36.40  ? 334 TYR   A CB   1 
ATOM   5136 C  CG   . TYR   A 1 334 ? -37.361 30.783  2.799   1.00 31.01  ? 334 TYR   A CG   1 
ATOM   5137 C  CD1  . TYR   A 1 334 ? -38.400 31.106  1.937   1.00 31.69  ? 334 TYR   A CD1  1 
ATOM   5138 C  CD2  . TYR   A 1 334 ? -37.461 29.603  3.524   1.00 27.28  ? 334 TYR   A CD2  1 
ATOM   5139 C  CE1  . TYR   A 1 334 ? -39.500 30.280  1.792   1.00 27.27  ? 334 TYR   A CE1  1 
ATOM   5140 C  CE2  . TYR   A 1 334 ? -38.557 28.768  3.389   1.00 28.55  ? 334 TYR   A CE2  1 
ATOM   5141 C  CZ   . TYR   A 1 334 ? -39.579 29.108  2.522   1.00 26.85  ? 334 TYR   A CZ   1 
ATOM   5142 O  OH   . TYR   A 1 334 ? -40.663 28.292  2.385   1.00 26.42  ? 334 TYR   A OH   1 
ATOM   5143 H  H    . TYR   A 1 334 ? -33.698 30.240  2.847   1.00 37.72  ? 334 TYR   A H    1 
ATOM   5144 H  HA   . TYR   A 1 334 ? -35.465 31.414  1.011   1.00 47.35  ? 334 TYR   A HA   1 
ATOM   5145 H  HB2  . TYR   A 1 334 ? -35.773 31.577  3.843   1.00 43.68  ? 334 TYR   A HB2  1 
ATOM   5146 H  HB3  . TYR   A 1 334 ? -36.459 32.634  2.876   1.00 43.68  ? 334 TYR   A HB3  1 
ATOM   5147 H  HD1  . TYR   A 1 334 ? -38.353 31.904  1.434   1.00 38.03  ? 334 TYR   A HD1  1 
ATOM   5148 H  HD2  . TYR   A 1 334 ? -36.766 29.363  4.116   1.00 32.73  ? 334 TYR   A HD2  1 
ATOM   5149 H  HE1  . TYR   A 1 334 ? -40.195 30.514  1.202   1.00 32.72  ? 334 TYR   A HE1  1 
ATOM   5150 H  HE2  . TYR   A 1 334 ? -38.608 27.971  3.886   1.00 34.26  ? 334 TYR   A HE2  1 
ATOM   5151 H  HH   . TYR   A 1 334 ? -40.578 27.610  2.898   1.00 31.70  ? 334 TYR   A HH   1 
HETATM 5152 C  C1   . A1IRK B 2 .   ? -12.821 5.027   -5.794  1.00 20.13  ? 401 A1IRK A C1   1 
HETATM 5153 C  C2   . A1IRK B 2 .   ? -12.697 5.648   -7.022  1.00 18.97  ? 401 A1IRK A C2   1 
HETATM 5154 C  C3   . A1IRK B 2 .   ? -11.550 6.377   -7.320  1.00 16.36  ? 401 A1IRK A C3   1 
HETATM 5155 C  C4   . A1IRK B 2 .   ? -10.578 6.515   -6.342  1.00 18.60  ? 401 A1IRK A C4   1 
HETATM 5156 C  C5   . A1IRK B 2 .   ? -10.739 5.932   -5.100  1.00 21.55  ? 401 A1IRK A C5   1 
HETATM 5157 C  C6   . A1IRK B 2 .   ? -11.868 5.188   -4.811  1.00 19.83  ? 401 A1IRK A C6   1 
HETATM 5158 C  C8   . A1IRK B 2 .   ? -11.640 8.366   -10.556 1.00 18.22  ? 401 A1IRK A C8   1 
HETATM 5159 C  C9   . A1IRK B 2 .   ? -11.808 9.842   -10.078 1.00 23.09  ? 401 A1IRK A C9   1 
HETATM 5160 C  C10  . A1IRK B 2 .   ? -12.069 4.583   -3.443  1.00 28.29  ? 401 A1IRK A C10  1 
HETATM 5161 C  C11  . A1IRK B 2 .   ? -10.825 2.407   -3.797  1.00 31.80  ? 401 A1IRK A C11  1 
HETATM 5162 C  C12  . A1IRK B 2 .   ? -9.735  1.874   -3.169  1.00 38.69  ? 401 A1IRK A C12  1 
HETATM 5163 C  C13  . A1IRK B 2 .   ? -8.992  0.604   -3.434  1.00 48.20  ? 401 A1IRK A C13  1 
HETATM 5164 C  C14  . A1IRK B 2 .   ? -12.331 8.189   -11.924 1.00 22.17  ? 401 A1IRK A C14  1 
HETATM 5165 C  C15  . A1IRK B 2 .   ? -12.231 6.788   -12.526 1.00 28.98  ? 401 A1IRK A C15  1 
HETATM 5166 C  C16  . A1IRK B 2 .   ? -10.807 6.384   -12.864 1.00 28.12  ? 401 A1IRK A C16  1 
HETATM 5167 C  C17  . A1IRK B 2 .   ? -13.079 6.674   -13.774 1.00 24.95  ? 401 A1IRK A C17  1 
HETATM 5168 C  C18  . A1IRK B 2 .   ? -6.893  3.072   -5.225  1.00 53.59  ? 401 A1IRK A C18  1 
HETATM 5169 C  C19  . A1IRK B 2 .   ? -7.042  3.062   -6.747  1.00 45.34  ? 401 A1IRK A C19  1 
HETATM 5170 C  C20  . A1IRK B 2 .   ? -8.094  4.074   -7.185  1.00 39.89  ? 401 A1IRK A C20  1 
HETATM 5171 C  C21  . A1IRK B 2 .   ? -5.705  3.322   -7.419  1.00 33.54  ? 401 A1IRK A C21  1 
HETATM 5172 C  C7   . A1IRK B 2 .   ? -12.206 7.449   -9.480  1.00 18.27  ? 401 A1IRK A C7   1 
HETATM 5173 N  N1   . A1IRK B 2 .   ? -11.317 7.002   -8.560  1.00 16.39  ? 401 A1IRK A N1   1 
HETATM 5174 N  N2   . A1IRK B 2 .   ? -10.843 10.678  -10.442 1.00 25.69  ? 401 A1IRK A N2   1 
HETATM 5175 N  N3   . A1IRK B 2 .   ? -11.057 3.568   -3.163  1.00 31.40  ? 401 A1IRK A N3   1 
HETATM 5176 N  N4   . A1IRK B 2 .   ? -10.167 3.762   -2.177  1.00 44.55  ? 401 A1IRK A N4   1 
HETATM 5177 N  N5   . A1IRK B 2 .   ? -9.358  2.730   -2.184  1.00 44.04  ? 401 A1IRK A N5   1 
HETATM 5178 N  N6   . A1IRK B 2 .   ? -8.071  0.662   -4.567  1.00 54.74  ? 401 A1IRK A N6   1 
HETATM 5179 O  O1   . A1IRK B 2 .   ? -10.977 12.030  -10.121 1.00 17.11  ? 401 A1IRK A O1   1 
HETATM 5180 O  O2   . A1IRK B 2 .   ? -6.335  1.669   -3.106  1.00 64.56  ? 401 A1IRK A O2   1 
HETATM 5181 O  O3   . A1IRK B 2 .   ? -5.706  0.744   -5.310  1.00 61.84  ? 401 A1IRK A O3   1 
HETATM 5182 O  O4   . A1IRK B 2 .   ? -13.419 7.223   -9.414  1.00 21.38  ? 401 A1IRK A O4   1 
HETATM 5183 O  O5   . A1IRK B 2 .   ? -12.811 10.227  -9.462  1.00 23.73  ? 401 A1IRK A O5   1 
HETATM 5184 S  S1   . A1IRK B 2 .   ? -6.631  1.471   -4.493  1.00 137.88 ? 401 A1IRK A S1   1 
HETATM 5185 H  H3   . A1IRK B 2 .   ? -13.693 4.401   -5.612  1.00 24.15  ? 401 A1IRK A H3   1 
HETATM 5186 H  H4   . A1IRK B 2 .   ? -13.514 5.546   -7.734  1.00 22.76  ? 401 A1IRK A H4   1 
HETATM 5187 H  H5   . A1IRK B 2 .   ? -9.669  7.084   -6.535  1.00 22.32  ? 401 A1IRK A H5   1 
HETATM 5188 H  H6   . A1IRK B 2 .   ? -9.963  6.066   -4.347  1.00 25.87  ? 401 A1IRK A H6   1 
HETATM 5189 H  H1   . A1IRK B 2 .   ? -10.596 8.066   -10.633 1.00 21.86  ? 401 A1IRK A H1   1 
HETATM 5190 H  H10  . A1IRK B 2 .   ? -13.060 4.139   -3.362  1.00 33.95  ? 401 A1IRK A H10  1 
HETATM 5191 H  H9   . A1IRK B 2 .   ? -12.032 5.353   -2.674  1.00 33.95  ? 401 A1IRK A H9   1 
HETATM 5192 H  H11  . A1IRK B 2 .   ? -11.413 2.023   -4.629  1.00 38.16  ? 401 A1IRK A H11  1 
HETATM 5193 H  H12  . A1IRK B 2 .   ? -8.463  0.344   -2.518  1.00 57.84  ? 401 A1IRK A H12  1 
HETATM 5194 H  H13  . A1IRK B 2 .   ? -9.736  -0.178  -3.581  1.00 57.84  ? 401 A1IRK A H13  1 
HETATM 5195 H  H16  . A1IRK B 2 .   ? -13.389 8.436   -11.854 1.00 26.60  ? 401 A1IRK A H16  1 
HETATM 5196 H  H15  . A1IRK B 2 .   ? -11.920 8.885   -12.654 1.00 26.60  ? 401 A1IRK A H15  1 
HETATM 5197 H  H17  . A1IRK B 2 .   ? -12.594 6.101   -11.764 1.00 34.78  ? 401 A1IRK A H17  1 
HETATM 5198 H  H18  . A1IRK B 2 .   ? -10.333 7.099   -13.536 1.00 33.74  ? 401 A1IRK A H18  1 
HETATM 5199 H  H19  . A1IRK B 2 .   ? -10.768 5.412   -13.353 1.00 33.74  ? 401 A1IRK A H19  1 
HETATM 5200 H  H20  . A1IRK B 2 .   ? -10.183 6.320   -11.974 1.00 33.74  ? 401 A1IRK A H20  1 
HETATM 5201 H  H23  . A1IRK B 2 .   ? -12.757 7.361   -14.555 1.00 29.94  ? 401 A1IRK A H23  1 
HETATM 5202 H  H21  . A1IRK B 2 .   ? -14.128 6.894   -13.579 1.00 29.94  ? 401 A1IRK A H21  1 
HETATM 5203 H  H22  . A1IRK B 2 .   ? -13.045 5.675   -14.205 1.00 29.94  ? 401 A1IRK A H22  1 
HETATM 5204 H  H25  . A1IRK B 2 .   ? -7.766  3.570   -4.805  1.00 64.31  ? 401 A1IRK A H25  1 
HETATM 5205 H  H24  . A1IRK B 2 .   ? -6.095  3.768   -4.970  1.00 64.31  ? 401 A1IRK A H24  1 
HETATM 5206 H  H26  . A1IRK B 2 .   ? -7.393  2.079   -7.060  1.00 54.41  ? 401 A1IRK A H26  1 
HETATM 5207 H  H28  . A1IRK B 2 .   ? -7.807  5.093   -6.929  1.00 47.87  ? 401 A1IRK A H28  1 
HETATM 5208 H  H27  . A1IRK B 2 .   ? -9.057  3.886   -6.713  1.00 47.87  ? 401 A1IRK A H27  1 
HETATM 5209 H  H29  . A1IRK B 2 .   ? -8.257  4.049   -8.262  1.00 47.87  ? 401 A1IRK A H29  1 
HETATM 5210 H  H30  . A1IRK B 2 .   ? -5.331  4.319   -7.191  1.00 40.25  ? 401 A1IRK A H30  1 
HETATM 5211 H  H32  . A1IRK B 2 .   ? -5.781  3.244   -8.503  1.00 40.25  ? 401 A1IRK A H32  1 
HETATM 5212 H  H31  . A1IRK B 2 .   ? -4.949  2.609   -7.094  1.00 40.25  ? 401 A1IRK A H31  1 
HETATM 5213 H  H7   . A1IRK B 2 .   ? -10.330 7.122   -8.767  1.00 19.67  ? 401 A1IRK A H7   1 
HETATM 5214 H  H8   . A1IRK B 2 .   ? -9.858  10.458  -10.547 1.00 30.82  ? 401 A1IRK A H8   1 
HETATM 5215 H  H14  . A1IRK B 2 .   ? -8.415  0.160   -5.379  1.00 65.69  ? 401 A1IRK A H14  1 
HETATM 5216 H  H2   . A1IRK B 2 .   ? -10.107 12.278  -9.713  1.00 20.53  ? 401 A1IRK A H2   1 
HETATM 5217 ZN ZN   . ZN    C 3 .   ? -12.906 12.441  -9.527  1.00 13.46  ? 402 ZN    A ZN   1 
HETATM 5218 O  O    . HOH   D 4 .   ? -38.941 23.632  8.686   1.00 24.16  ? 501 HOH   A O    1 
HETATM 5219 O  O    . HOH   D 4 .   ? -10.108 23.543  3.917   1.00 32.04  ? 502 HOH   A O    1 
HETATM 5220 O  O    . HOH   D 4 .   ? -9.431  25.574  1.895   1.00 37.07  ? 503 HOH   A O    1 
HETATM 5221 O  O    . HOH   D 4 .   ? -13.054 3.960   -38.758 1.00 39.59  ? 504 HOH   A O    1 
HETATM 5222 O  O    . HOH   D 4 .   ? -14.119 1.293   -5.251  1.00 37.33  ? 505 HOH   A O    1 
HETATM 5223 O  O    . HOH   D 4 .   ? -6.394  -3.204  -29.606 1.00 40.76  ? 506 HOH   A O    1 
HETATM 5224 O  O    . HOH   D 4 .   ? 0.211   -0.751  -19.580 1.00 29.51  ? 507 HOH   A O    1 
HETATM 5225 O  O    . HOH   D 4 .   ? -20.494 2.484   3.499   1.00 39.96  ? 508 HOH   A O    1 
HETATM 5226 O  O    . HOH   D 4 .   ? -13.709 -5.880  -29.994 1.00 41.27  ? 509 HOH   A O    1 
HETATM 5227 O  O    . HOH   D 4 .   ? -17.213 12.525  -30.199 1.00 30.81  ? 510 HOH   A O    1 
HETATM 5228 O  O    . HOH   D 4 .   ? 0.835   2.243   -10.217 1.00 35.74  ? 511 HOH   A O    1 
HETATM 5229 O  O    . HOH   D 4 .   ? -10.479 27.199  -28.515 1.00 43.83  ? 512 HOH   A O    1 
HETATM 5230 O  O    . HOH   D 4 .   ? -41.397 13.035  -11.085 1.00 45.14  ? 513 HOH   A O    1 
HETATM 5231 O  O    . HOH   D 4 .   ? -8.011  28.679  -28.015 1.00 45.10  ? 514 HOH   A O    1 
HETATM 5232 O  O    . HOH   D 4 .   ? -42.047 18.368  -14.063 1.00 31.92  ? 515 HOH   A O    1 
HETATM 5233 O  O    . HOH   D 4 .   ? -20.837 -3.027  -11.240 1.00 43.63  ? 516 HOH   A O    1 
HETATM 5234 O  O    . HOH   D 4 .   ? -31.290 3.235   2.327   1.00 38.19  ? 517 HOH   A O    1 
HETATM 5235 O  O    . HOH   D 4 .   ? -30.890 17.341  6.318   1.00 24.11  ? 518 HOH   A O    1 
HETATM 5236 O  O    . HOH   D 4 .   ? -10.557 3.971   -40.190 1.00 33.49  ? 519 HOH   A O    1 
HETATM 5237 O  O    . HOH   D 4 .   ? 0.994   15.781  -9.263  1.00 29.26  ? 520 HOH   A O    1 
HETATM 5238 O  O    . HOH   D 4 .   ? 6.311   22.147  -40.896 1.00 45.23  ? 521 HOH   A O    1 
HETATM 5239 O  O    . HOH   D 4 .   ? 2.185   2.467   -26.456 1.00 31.77  ? 522 HOH   A O    1 
HETATM 5240 O  O    . HOH   D 4 .   ? -23.944 31.037  -1.539  1.00 29.28  ? 523 HOH   A O    1 
HETATM 5241 O  O    . HOH   D 4 .   ? -26.581 26.030  6.708   1.00 29.99  ? 524 HOH   A O    1 
HETATM 5242 O  O    . HOH   D 4 .   ? -42.096 21.582  -15.224 1.00 33.75  ? 525 HOH   A O    1 
HETATM 5243 O  O    . HOH   D 4 .   ? -28.478 6.047   -21.592 1.00 41.04  ? 526 HOH   A O    1 
HETATM 5244 O  O    . HOH   D 4 .   ? -38.365 29.235  -18.216 1.00 43.74  ? 527 HOH   A O    1 
HETATM 5245 O  O    . HOH   D 4 .   ? -30.566 2.419   -1.492  1.00 33.17  ? 528 HOH   A O    1 
HETATM 5246 O  O    . HOH   D 4 .   ? -9.299  29.924  -24.847 1.00 40.96  ? 529 HOH   A O    1 
HETATM 5247 O  O    . HOH   D 4 .   ? 6.201   18.255  -44.088 1.00 33.92  ? 530 HOH   A O    1 
HETATM 5248 O  O    . HOH   D 4 .   ? -24.976 -3.599  -13.996 1.00 40.96  ? 531 HOH   A O    1 
HETATM 5249 O  O    . HOH   D 4 .   ? 3.195   11.009  -9.317  1.00 25.52  ? 532 HOH   A O    1 
HETATM 5250 O  O    . HOH   D 4 .   ? -17.921 2.547   -7.519  1.00 19.27  ? 533 HOH   A O    1 
HETATM 5251 O  O    . HOH   D 4 .   ? -9.877  13.665  -42.876 1.00 40.04  ? 534 HOH   A O    1 
HETATM 5252 O  O    . HOH   D 4 .   ? 2.682   1.202   -33.665 1.00 38.95  ? 535 HOH   A O    1 
HETATM 5253 O  O    . HOH   D 4 .   ? -15.672 31.553  -7.019  1.00 42.04  ? 536 HOH   A O    1 
HETATM 5254 O  O    . HOH   D 4 .   ? -5.989  15.923  -44.247 1.00 43.36  ? 537 HOH   A O    1 
HETATM 5255 O  O    . HOH   D 4 .   ? -17.628 12.175  1.260   1.00 16.69  ? 538 HOH   A O    1 
HETATM 5256 O  O    . HOH   D 4 .   ? -31.562 22.200  0.232   1.00 27.71  ? 539 HOH   A O    1 
HETATM 5257 O  O    . HOH   D 4 .   ? -30.247 11.144  -26.004 1.00 36.75  ? 540 HOH   A O    1 
HETATM 5258 O  O    . HOH   D 4 .   ? -3.137  6.311   -20.186 1.00 16.03  ? 541 HOH   A O    1 
HETATM 5259 O  O    . HOH   D 4 .   ? -23.394 31.994  -13.692 1.00 33.63  ? 542 HOH   A O    1 
HETATM 5260 O  O    . HOH   D 4 .   ? -3.577  32.077  -21.520 1.00 37.14  ? 543 HOH   A O    1 
HETATM 5261 O  O    . HOH   D 4 .   ? 9.860   10.621  -30.071 1.00 34.12  ? 544 HOH   A O    1 
HETATM 5262 O  O    . HOH   D 4 .   ? 4.547   15.934  -14.686 1.00 28.19  ? 545 HOH   A O    1 
HETATM 5263 O  O    . HOH   D 4 .   ? -18.742 14.630  7.157   1.00 27.75  ? 546 HOH   A O    1 
HETATM 5264 O  O    . HOH   D 4 .   ? 3.717   3.830   -28.762 1.00 39.43  ? 547 HOH   A O    1 
HETATM 5265 O  O    . HOH   D 4 .   ? 4.335   22.202  -29.131 1.00 37.50  ? 548 HOH   A O    1 
HETATM 5266 O  O    . HOH   D 4 .   ? -3.307  15.132  -12.197 1.00 15.65  ? 549 HOH   A O    1 
HETATM 5267 O  O    . HOH   D 4 .   ? -16.273 19.827  3.660   1.00 23.83  ? 550 HOH   A O    1 
HETATM 5268 O  O    . HOH   D 4 .   ? -9.378  19.257  -36.677 1.00 38.19  ? 551 HOH   A O    1 
HETATM 5269 O  O    . HOH   D 4 .   ? 8.679   9.447   -46.071 1.00 40.99  ? 552 HOH   A O    1 
HETATM 5270 O  O    . HOH   D 4 .   ? -0.947  27.122  -24.867 1.00 34.02  ? 553 HOH   A O    1 
HETATM 5271 O  O    . HOH   D 4 .   ? -20.155 6.140   -20.571 1.00 21.81  ? 554 HOH   A O    1 
HETATM 5272 O  O    . HOH   D 4 .   ? 1.340   13.260  -9.573  1.00 27.15  ? 555 HOH   A O    1 
HETATM 5273 O  O    . HOH   D 4 .   ? 7.557   2.827   -13.914 1.00 37.50  ? 556 HOH   A O    1 
HETATM 5274 O  O    . HOH   D 4 .   ? -24.613 1.637   -0.421  1.00 25.27  ? 557 HOH   A O    1 
HETATM 5275 O  O    . HOH   D 4 .   ? -28.302 4.389   -0.177  1.00 20.63  ? 558 HOH   A O    1 
HETATM 5276 O  O    . HOH   D 4 .   ? -12.298 26.896  -14.347 1.00 17.15  ? 559 HOH   A O    1 
HETATM 5277 O  O    . HOH   D 4 .   ? -38.874 11.494  -10.152 1.00 35.20  ? 560 HOH   A O    1 
HETATM 5278 O  O    . HOH   D 4 .   ? -7.269  4.647   -27.341 1.00 16.37  ? 561 HOH   A O    1 
HETATM 5279 O  O    . HOH   D 4 .   ? -25.746 -2.095  -2.709  1.00 28.42  ? 562 HOH   A O    1 
HETATM 5280 O  O    . HOH   D 4 .   ? -39.823 17.067  1.377   1.00 19.52  ? 563 HOH   A O    1 
HETATM 5281 O  O    . HOH   D 4 .   ? -4.247  24.183  -7.274  1.00 35.39  ? 564 HOH   A O    1 
HETATM 5282 O  O    . HOH   D 4 .   ? -0.641  2.778   -15.825 1.00 15.74  ? 565 HOH   A O    1 
HETATM 5283 O  O    . HOH   D 4 .   ? -21.038 24.455  5.356   1.00 20.58  ? 566 HOH   A O    1 
HETATM 5284 O  O    . HOH   D 4 .   ? -26.529 3.092   -20.310 1.00 35.44  ? 567 HOH   A O    1 
HETATM 5285 O  O    . HOH   D 4 .   ? -4.890  4.561   -42.167 1.00 41.56  ? 568 HOH   A O    1 
HETATM 5286 O  O    . HOH   D 4 .   ? -22.772 26.818  1.938   1.00 21.65  ? 569 HOH   A O    1 
HETATM 5287 O  O    . HOH   D 4 .   ? -11.221 12.665  0.375   1.00 18.80  ? 570 HOH   A O    1 
HETATM 5288 O  O    . HOH   D 4 .   ? -8.148  0.598   -35.027 1.00 32.93  ? 571 HOH   A O    1 
HETATM 5289 O  O    . HOH   D 4 .   ? 7.313   12.472  -20.217 1.00 23.39  ? 572 HOH   A O    1 
HETATM 5290 O  O    . HOH   D 4 .   ? 4.918   0.706   -10.269 1.00 41.34  ? 573 HOH   A O    1 
HETATM 5291 O  O    . HOH   D 4 .   ? -38.141 28.109  7.060   1.00 26.34  ? 574 HOH   A O    1 
HETATM 5292 O  O    . HOH   D 4 .   ? -5.801  -1.874  -30.802 1.00 39.91  ? 575 HOH   A O    1 
HETATM 5293 O  O    . HOH   D 4 .   ? -6.750  27.847  -23.820 1.00 46.49  ? 576 HOH   A O    1 
HETATM 5294 O  O    . HOH   D 4 .   ? 9.510   5.041   -20.271 1.00 38.66  ? 577 HOH   A O    1 
HETATM 5295 O  O    . HOH   D 4 .   ? -0.573  9.612   -30.329 1.00 16.16  ? 578 HOH   A O    1 
HETATM 5296 O  O    . HOH   D 4 .   ? 4.145   11.266  -38.509 1.00 30.89  ? 579 HOH   A O    1 
HETATM 5297 O  O    . HOH   D 4 .   ? 8.405   14.453  -21.639 1.00 34.38  ? 580 HOH   A O    1 
HETATM 5298 O  O    . HOH   D 4 .   ? -37.314 32.534  -12.059 1.00 33.01  ? 581 HOH   A O    1 
HETATM 5299 O  O    . HOH   D 4 .   ? -9.312  -6.562  -23.850 1.00 40.60  ? 582 HOH   A O    1 
HETATM 5300 O  O    . HOH   D 4 .   ? -19.511 0.891   -28.834 1.00 38.10  ? 583 HOH   A O    1 
HETATM 5301 O  O    . HOH   D 4 .   ? -14.056 29.798  -16.433 1.00 34.51  ? 584 HOH   A O    1 
HETATM 5302 O  O    . HOH   D 4 .   ? -1.338  -1.760  -17.922 1.00 35.22  ? 585 HOH   A O    1 
HETATM 5303 O  O    . HOH   D 4 .   ? -16.093 31.152  -15.323 1.00 35.23  ? 586 HOH   A O    1 
HETATM 5304 O  O    . HOH   D 4 .   ? -29.921 12.331  -21.625 1.00 27.07  ? 587 HOH   A O    1 
HETATM 5305 O  O    . HOH   D 4 .   ? -13.785 26.448  -22.523 1.00 18.59  ? 588 HOH   A O    1 
HETATM 5306 O  O    . HOH   D 4 .   ? 2.113   -1.379  -27.214 1.00 39.11  ? 589 HOH   A O    1 
HETATM 5307 O  O    . HOH   D 4 .   ? -13.446 -6.211  -22.552 1.00 30.39  ? 590 HOH   A O    1 
HETATM 5308 O  O    . HOH   D 4 .   ? -17.575 -4.963  -18.276 1.00 42.19  ? 591 HOH   A O    1 
HETATM 5309 O  O    . HOH   D 4 .   ? 7.837   9.432   -22.449 1.00 30.62  ? 592 HOH   A O    1 
HETATM 5310 O  O    . HOH   D 4 .   ? -11.552 25.850  -2.027  1.00 27.77  ? 593 HOH   A O    1 
HETATM 5311 O  O    . HOH   D 4 .   ? -17.118 2.213   4.788   1.00 39.23  ? 594 HOH   A O    1 
HETATM 5312 O  O    . HOH   D 4 .   ? -11.920 22.297  -4.889  1.00 24.90  ? 595 HOH   A O    1 
HETATM 5313 O  O    . HOH   D 4 .   ? 7.371   7.293   -24.196 1.00 32.47  ? 596 HOH   A O    1 
HETATM 5314 O  O    . HOH   D 4 .   ? -41.177 26.156  -5.107  1.00 36.23  ? 597 HOH   A O    1 
HETATM 5315 O  O    . HOH   D 4 .   ? -12.955 6.175   -26.266 1.00 36.48  ? 598 HOH   A O    1 
HETATM 5316 O  O    . HOH   D 4 .   ? 6.889   0.650   -20.188 1.00 35.46  ? 599 HOH   A O    1 
HETATM 5317 O  O    . HOH   D 4 .   ? -4.197  21.612  -17.078 1.00 13.99  ? 600 HOH   A O    1 
HETATM 5318 O  O    . HOH   D 4 .   ? -18.289 27.013  3.044   1.00 20.59  ? 601 HOH   A O    1 
HETATM 5319 O  O    . HOH   D 4 .   ? -2.451  7.318   -6.537  1.00 29.26  ? 602 HOH   A O    1 
HETATM 5320 O  O    . HOH   D 4 .   ? -10.137 11.223  -7.476  1.00 26.24  ? 603 HOH   A O    1 
HETATM 5321 O  O    . HOH   D 4 .   ? -20.357 -2.211  -19.766 1.00 34.83  ? 604 HOH   A O    1 
HETATM 5322 O  O    . HOH   D 4 .   ? -34.042 7.076   -9.499  1.00 35.59  ? 605 HOH   A O    1 
HETATM 5323 O  O    . HOH   D 4 .   ? -1.479  24.452  -18.027 1.00 18.31  ? 606 HOH   A O    1 
HETATM 5324 O  O    . HOH   D 4 .   ? -17.013 30.890  -8.762  1.00 23.55  ? 607 HOH   A O    1 
HETATM 5325 O  O    . HOH   D 4 .   ? -17.118 7.485   -18.079 1.00 21.05  ? 608 HOH   A O    1 
HETATM 5326 O  O    . HOH   D 4 .   ? -23.122 25.852  -0.642  1.00 17.24  ? 609 HOH   A O    1 
HETATM 5327 O  O    . HOH   D 4 .   ? 1.237   21.124  -15.961 1.00 24.80  ? 610 HOH   A O    1 
HETATM 5328 O  O    . HOH   D 4 .   ? -11.662 8.719   2.042   1.00 35.34  ? 611 HOH   A O    1 
HETATM 5329 O  O    . HOH   D 4 .   ? -9.700  20.726  -5.601  1.00 24.61  ? 612 HOH   A O    1 
HETATM 5330 O  O    . HOH   D 4 .   ? -26.515 22.311  6.269   1.00 21.87  ? 613 HOH   A O    1 
HETATM 5331 O  O    . HOH   D 4 .   ? 8.248   8.404   -5.325  1.00 46.15  ? 614 HOH   A O    1 
HETATM 5332 O  O    . HOH   D 4 .   ? -38.355 17.093  -21.467 1.00 38.25  ? 615 HOH   A O    1 
HETATM 5333 O  O    . HOH   D 4 .   ? -28.682 30.409  -2.182  1.00 29.04  ? 616 HOH   A O    1 
HETATM 5334 O  O    . HOH   D 4 .   ? -17.770 9.987   -7.949  1.00 14.51  ? 617 HOH   A O    1 
HETATM 5335 O  O    . HOH   D 4 .   ? -22.821 30.762  -18.481 1.00 36.10  ? 618 HOH   A O    1 
HETATM 5336 O  O    . HOH   D 4 .   ? 8.563   17.640  -26.654 1.00 24.61  ? 619 HOH   A O    1 
HETATM 5337 O  O    . HOH   D 4 .   ? -19.743 29.391  -6.162  1.00 17.33  ? 620 HOH   A O    1 
HETATM 5338 O  O    . HOH   D 4 .   ? -34.412 8.185   -4.170  1.00 32.27  ? 621 HOH   A O    1 
HETATM 5339 O  O    . HOH   D 4 .   ? -9.236  1.312   -9.228  1.00 37.31  ? 622 HOH   A O    1 
HETATM 5340 O  O    . HOH   D 4 .   ? -32.654 23.898  4.586   1.00 30.96  ? 623 HOH   A O    1 
HETATM 5341 O  O    . HOH   D 4 .   ? -32.442 3.872   -4.778  1.00 32.55  ? 624 HOH   A O    1 
HETATM 5342 O  O    . HOH   D 4 .   ? -21.306 7.280   -6.405  1.00 16.30  ? 625 HOH   A O    1 
HETATM 5343 O  O    . HOH   D 4 .   ? -15.791 18.644  -9.758  1.00 12.23  ? 626 HOH   A O    1 
HETATM 5344 O  O    . HOH   D 4 .   ? -26.631 22.976  -21.508 1.00 28.18  ? 627 HOH   A O    1 
HETATM 5345 O  O    . HOH   D 4 .   ? -17.217 24.166  -31.030 1.00 38.37  ? 628 HOH   A O    1 
HETATM 5346 O  O    . HOH   D 4 .   ? -1.824  2.078   -39.590 1.00 25.13  ? 629 HOH   A O    1 
HETATM 5347 O  O    . HOH   D 4 .   ? 2.733   23.836  -22.815 1.00 29.88  ? 630 HOH   A O    1 
HETATM 5348 O  O    . HOH   D 4 .   ? -5.753  0.865   -39.032 1.00 31.69  ? 631 HOH   A O    1 
HETATM 5349 O  O    . HOH   D 4 .   ? -16.947 11.591  4.522   1.00 20.69  ? 632 HOH   A O    1 
HETATM 5350 O  O    . HOH   D 4 .   ? -12.375 28.784  -6.053  1.00 25.80  ? 633 HOH   A O    1 
HETATM 5351 O  O    . HOH   D 4 .   ? -37.379 14.179  -18.777 1.00 36.55  ? 634 HOH   A O    1 
HETATM 5352 O  O    . HOH   D 4 .   ? -37.185 11.870  -12.369 1.00 25.09  ? 635 HOH   A O    1 
HETATM 5353 O  O    . HOH   D 4 .   ? 7.164   18.789  -14.524 1.00 39.00  ? 636 HOH   A O    1 
HETATM 5354 O  O    . HOH   D 4 .   ? 3.682   5.619   -25.547 1.00 22.87  ? 637 HOH   A O    1 
HETATM 5355 O  O    . HOH   D 4 .   ? -33.106 35.409  -9.939  1.00 40.72  ? 638 HOH   A O    1 
HETATM 5356 O  O    . HOH   D 4 .   ? -30.600 15.777  4.475   1.00 42.99  ? 639 HOH   A O    1 
HETATM 5357 O  O    . HOH   D 4 .   ? -0.767  23.017  -15.734 1.00 19.30  ? 640 HOH   A O    1 
HETATM 5358 O  O    . HOH   D 4 .   ? -38.141 30.117  -11.552 1.00 31.17  ? 641 HOH   A O    1 
HETATM 5359 O  O    . HOH   D 4 .   ? -22.517 3.964   -8.387  1.00 15.30  ? 642 HOH   A O    1 
HETATM 5360 O  O    . HOH   D 4 .   ? 3.075   4.270   -33.519 1.00 27.14  ? 643 HOH   A O    1 
HETATM 5361 O  O    . HOH   D 4 .   ? 14.152  16.862  -18.681 1.00 38.82  ? 644 HOH   A O    1 
HETATM 5362 O  O    . HOH   D 4 .   ? 3.518   0.316   -37.959 1.00 35.85  ? 645 HOH   A O    1 
HETATM 5363 O  O    . HOH   D 4 .   ? -33.190 15.166  5.310   1.00 34.10  ? 646 HOH   A O    1 
HETATM 5364 O  O    . HOH   D 4 .   ? -7.015  19.060  -28.804 1.00 17.06  ? 647 HOH   A O    1 
HETATM 5365 O  O    . HOH   D 4 .   ? 6.690   8.943   -35.876 1.00 25.94  ? 648 HOH   A O    1 
HETATM 5366 O  O    . HOH   D 4 .   ? -27.461 2.302   -15.715 1.00 38.22  ? 649 HOH   A O    1 
HETATM 5367 O  O    . HOH   D 4 .   ? -16.458 29.767  -3.452  1.00 25.59  ? 650 HOH   A O    1 
HETATM 5368 O  O    . HOH   D 4 .   ? -26.744 8.262   8.134   1.00 44.23  ? 651 HOH   A O    1 
HETATM 5369 O  O    . HOH   D 4 .   ? -12.951 30.968  -12.157 1.00 35.24  ? 652 HOH   A O    1 
HETATM 5370 O  O    . HOH   D 4 .   ? -17.137 8.434   -22.155 1.00 20.67  ? 653 HOH   A O    1 
HETATM 5371 O  O    . HOH   D 4 .   ? -31.889 33.108  -4.394  1.00 38.71  ? 654 HOH   A O    1 
HETATM 5372 O  O    . HOH   D 4 .   ? -13.224 1.091   -0.926  1.00 37.07  ? 655 HOH   A O    1 
HETATM 5373 O  O    . HOH   D 4 .   ? 4.459   13.657  -11.148 1.00 22.66  ? 656 HOH   A O    1 
HETATM 5374 O  O    . HOH   D 4 .   ? -22.275 7.069   -23.723 1.00 36.98  ? 657 HOH   A O    1 
HETATM 5375 O  O    . HOH   D 4 .   ? -36.417 9.007   -0.963  1.00 33.53  ? 658 HOH   A O    1 
HETATM 5376 O  O    . HOH   D 4 .   ? 5.337   10.954  -40.883 1.00 33.24  ? 659 HOH   A O    1 
HETATM 5377 O  O    . HOH   D 4 .   ? -9.469  23.782  -29.362 1.00 46.58  ? 660 HOH   A O    1 
HETATM 5378 O  O    . HOH   D 4 .   ? -19.455 8.738   -18.423 1.00 21.29  ? 661 HOH   A O    1 
HETATM 5379 O  O    . HOH   D 4 .   ? -4.480  27.775  -23.466 1.00 32.35  ? 662 HOH   A O    1 
HETATM 5380 O  O    . HOH   D 4 .   ? 1.597   10.772  -31.516 1.00 17.35  ? 663 HOH   A O    1 
HETATM 5381 O  O    . HOH   D 4 .   ? -26.506 26.000  -21.998 1.00 30.64  ? 664 HOH   A O    1 
HETATM 5382 O  O    . HOH   D 4 .   ? 5.627   13.593  -23.418 1.00 18.85  ? 665 HOH   A O    1 
HETATM 5383 O  O    . HOH   D 4 .   ? 2.826   12.019  -44.098 1.00 35.38  ? 666 HOH   A O    1 
HETATM 5384 O  O    . HOH   D 4 .   ? 1.250   22.198  -41.376 1.00 35.23  ? 667 HOH   A O    1 
HETATM 5385 O  O    . HOH   D 4 .   ? 0.308   -0.692  -36.161 1.00 26.44  ? 668 HOH   A O    1 
HETATM 5386 O  O    . HOH   D 4 .   ? -28.501 16.318  3.724   1.00 27.20  ? 669 HOH   A O    1 
HETATM 5387 O  O    . HOH   D 4 .   ? -17.201 20.810  -30.825 1.00 46.33  ? 670 HOH   A O    1 
HETATM 5388 O  O    . HOH   D 4 .   ? -29.771 9.790   8.519   1.00 43.59  ? 671 HOH   A O    1 
HETATM 5389 O  O    . HOH   D 4 .   ? -25.538 29.164  -20.815 1.00 31.05  ? 672 HOH   A O    1 
HETATM 5390 O  O    . HOH   D 4 .   ? -18.073 -1.672  -7.443  1.00 38.03  ? 673 HOH   A O    1 
HETATM 5391 O  O    . HOH   D 4 .   ? -11.541 19.855  -7.249  1.00 18.16  ? 674 HOH   A O    1 
HETATM 5392 O  O    . HOH   D 4 .   ? -2.611  23.120  -33.607 1.00 33.32  ? 675 HOH   A O    1 
HETATM 5393 O  O    . HOH   D 4 .   ? -21.911 18.905  -30.764 1.00 40.08  ? 676 HOH   A O    1 
HETATM 5394 O  O    . HOH   D 4 .   ? -14.506 12.590  3.851   1.00 25.85  ? 677 HOH   A O    1 
HETATM 5395 O  O    . HOH   D 4 .   ? -41.153 15.785  -20.641 1.00 39.77  ? 678 HOH   A O    1 
HETATM 5396 O  O    . HOH   D 4 .   ? -33.191 26.347  -21.560 1.00 33.96  ? 679 HOH   A O    1 
HETATM 5397 O  O    . HOH   D 4 .   ? 0.572   7.470   -7.636  1.00 37.79  ? 680 HOH   A O    1 
HETATM 5398 O  O    . HOH   D 4 .   ? -7.672  21.692  -28.511 1.00 21.13  ? 681 HOH   A O    1 
HETATM 5399 O  O    . HOH   D 4 .   ? -12.308 29.570  -14.764 1.00 30.20  ? 682 HOH   A O    1 
HETATM 5400 O  O    . HOH   D 4 .   ? -16.770 5.072   -7.019  1.00 15.70  ? 683 HOH   A O    1 
HETATM 5401 O  O    . HOH   D 4 .   ? -6.400  25.541  -10.145 1.00 32.31  ? 684 HOH   A O    1 
HETATM 5402 O  O    . HOH   D 4 .   ? -23.736 33.654  -3.761  1.00 40.31  ? 685 HOH   A O    1 
HETATM 5403 O  O    . HOH   D 4 .   ? 7.615   21.406  -19.880 1.00 39.23  ? 686 HOH   A O    1 
HETATM 5404 O  O    . HOH   D 4 .   ? -23.034 13.799  -3.682  1.00 13.86  ? 687 HOH   A O    1 
HETATM 5405 O  O    . HOH   D 4 .   ? -18.961 -0.979  -9.919  1.00 36.43  ? 688 HOH   A O    1 
HETATM 5406 O  O    . HOH   D 4 .   ? -7.408  25.708  -22.446 1.00 30.58  ? 689 HOH   A O    1 
HETATM 5407 O  O    . HOH   D 4 .   ? -22.197 8.736   -25.629 1.00 29.16  ? 690 HOH   A O    1 
HETATM 5408 O  O    . HOH   D 4 .   ? -19.142 19.550  3.643   1.00 19.91  ? 691 HOH   A O    1 
HETATM 5409 O  O    . HOH   D 4 .   ? -1.686  27.774  -19.974 1.00 31.90  ? 692 HOH   A O    1 
HETATM 5410 O  O    . HOH   D 4 .   ? 7.488   11.807  -26.612 1.00 21.99  ? 693 HOH   A O    1 
HETATM 5411 O  O    . HOH   D 4 .   ? 0.704   24.205  -19.829 1.00 22.40  ? 694 HOH   A O    1 
HETATM 5412 O  O    . HOH   D 4 .   ? 5.028   2.147   -39.405 1.00 45.09  ? 695 HOH   A O    1 
HETATM 5413 O  O    . HOH   D 4 .   ? -26.673 18.300  4.377   1.00 15.35  ? 696 HOH   A O    1 
HETATM 5414 O  O    . HOH   D 4 .   ? -20.902 30.502  -26.282 1.00 34.86  ? 697 HOH   A O    1 
HETATM 5415 O  O    . HOH   D 4 .   ? -0.938  7.483   -31.960 1.00 18.93  ? 698 HOH   A O    1 
HETATM 5416 O  O    . HOH   D 4 .   ? -19.015 8.523   11.231  1.00 42.08  ? 699 HOH   A O    1 
HETATM 5417 O  O    . HOH   D 4 .   ? -2.428  29.711  -11.929 1.00 43.62  ? 700 HOH   A O    1 
HETATM 5418 O  O    . HOH   D 4 .   ? -9.329  2.903   -23.243 1.00 16.18  ? 701 HOH   A O    1 
HETATM 5419 O  O    . HOH   D 4 .   ? -3.969  0.907   -9.557  1.00 27.37  ? 702 HOH   A O    1 
HETATM 5420 O  O    . HOH   D 4 .   ? -10.679 5.185   -25.283 1.00 42.30  ? 703 HOH   A O    1 
HETATM 5421 O  O    . HOH   D 4 .   ? 6.226   15.117  -12.691 1.00 24.82  ? 704 HOH   A O    1 
HETATM 5422 O  O    . HOH   D 4 .   ? -10.168 26.309  -4.430  1.00 24.55  ? 705 HOH   A O    1 
HETATM 5423 O  O    . HOH   D 4 .   ? -9.708  17.474  -32.838 1.00 30.89  ? 706 HOH   A O    1 
HETATM 5424 O  O    . HOH   D 4 .   ? 2.905   2.775   -23.802 1.00 33.32  ? 707 HOH   A O    1 
HETATM 5425 O  O    . HOH   D 4 .   ? 8.021   10.510  -17.890 1.00 33.37  ? 708 HOH   A O    1 
HETATM 5426 O  O    . HOH   D 4 .   ? -14.679 8.368   -25.412 1.00 22.18  ? 709 HOH   A O    1 
HETATM 5427 O  O    . HOH   D 4 .   ? -20.134 -0.889  0.963   1.00 34.48  ? 710 HOH   A O    1 
HETATM 5428 O  O    . HOH   D 4 .   ? -26.071 27.759  -16.442 1.00 17.93  ? 711 HOH   A O    1 
HETATM 5429 O  O    . HOH   D 4 .   ? 8.715   14.801  -24.993 1.00 31.93  ? 712 HOH   A O    1 
HETATM 5430 O  O    . HOH   D 4 .   ? -38.387 24.533  -15.923 1.00 30.26  ? 713 HOH   A O    1 
HETATM 5431 O  O    . HOH   D 4 .   ? -37.353 13.714  1.733   1.00 33.26  ? 714 HOH   A O    1 
HETATM 5432 O  O    . HOH   D 4 .   ? 3.139   3.942   -41.428 1.00 40.43  ? 715 HOH   A O    1 
HETATM 5433 O  O    . HOH   D 4 .   ? 2.708   13.533  -47.204 1.00 38.73  ? 716 HOH   A O    1 
HETATM 5434 O  O    . HOH   D 4 .   ? -33.487 13.200  -19.784 1.00 33.97  ? 717 HOH   A O    1 
HETATM 5435 O  O    . HOH   D 4 .   ? -35.877 16.529  5.535   1.00 29.04  ? 718 HOH   A O    1 
HETATM 5436 O  O    . HOH   D 4 .   ? -36.109 29.890  -18.784 1.00 33.87  ? 719 HOH   A O    1 
HETATM 5437 O  O    . HOH   D 4 .   ? 10.051  11.179  -17.073 1.00 49.40  ? 720 HOH   A O    1 
HETATM 5438 O  O    . HOH   D 4 .   ? 0.757   27.786  -37.933 1.00 40.52  ? 721 HOH   A O    1 
HETATM 5439 O  O    . HOH   D 4 .   ? -23.003 7.193   -8.571  1.00 15.86  ? 722 HOH   A O    1 
HETATM 5440 O  O    . HOH   D 4 .   ? -32.253 29.898  -18.956 1.00 32.03  ? 723 HOH   A O    1 
HETATM 5441 O  O    . HOH   D 4 .   ? 8.766   9.079   -33.746 1.00 27.83  ? 724 HOH   A O    1 
HETATM 5442 O  O    . HOH   D 4 .   ? 3.088   7.845   -42.118 1.00 30.68  ? 725 HOH   A O    1 
HETATM 5443 O  O    . HOH   D 4 .   ? 3.087   5.591   -30.546 1.00 26.95  ? 726 HOH   A O    1 
HETATM 5444 O  O    . HOH   D 4 .   ? -19.210 17.136  5.674   1.00 24.19  ? 727 HOH   A O    1 
HETATM 5445 O  O    . HOH   D 4 .   ? 12.388  13.341  -36.805 1.00 41.02  ? 728 HOH   A O    1 
HETATM 5446 O  O    . HOH   D 4 .   ? -4.376  -2.129  -28.162 1.00 26.90  ? 729 HOH   A O    1 
HETATM 5447 O  O    . HOH   D 4 .   ? -19.224 21.274  6.162   1.00 39.41  ? 730 HOH   A O    1 
HETATM 5448 O  O    . HOH   D 4 .   ? -8.636  30.364  -11.741 1.00 33.27  ? 731 HOH   A O    1 
HETATM 5449 O  O    . HOH   D 4 .   ? 3.782   21.287  -41.567 1.00 37.34  ? 732 HOH   A O    1 
HETATM 5450 O  O    . HOH   D 4 .   ? -5.245  28.140  -11.913 1.00 35.59  ? 733 HOH   A O    1 
HETATM 5451 O  O    . HOH   D 4 .   ? 0.813   0.721   -17.274 1.00 23.41  ? 734 HOH   A O    1 
HETATM 5452 O  O    . HOH   D 4 .   ? -11.437 10.460  -25.615 1.00 28.41  ? 735 HOH   A O    1 
HETATM 5453 O  O    . HOH   D 4 .   ? -15.550 17.049  -32.216 1.00 52.46  ? 736 HOH   A O    1 
HETATM 5454 O  O    . HOH   D 4 .   ? -19.487 1.901   1.199   1.00 34.08  ? 737 HOH   A O    1 
HETATM 5455 O  O    . HOH   D 4 .   ? -25.242 26.993  -2.092  1.00 17.94  ? 738 HOH   A O    1 
HETATM 5456 O  O    . HOH   D 4 .   ? 10.651  13.656  -18.353 1.00 31.81  ? 739 HOH   A O    1 
HETATM 5457 O  O    . HOH   D 4 .   ? -9.586  26.324  -20.677 1.00 24.64  ? 740 HOH   A O    1 
HETATM 5458 O  O    . HOH   D 4 .   ? -43.646 21.018  -11.281 1.00 42.53  ? 741 HOH   A O    1 
HETATM 5459 O  O    . HOH   D 4 .   ? 1.082   25.894  -26.282 1.00 39.40  ? 742 HOH   A O    1 
HETATM 5460 O  O    . HOH   D 4 .   ? -7.457  17.848  -31.307 1.00 21.64  ? 743 HOH   A O    1 
HETATM 5461 O  O    . HOH   D 4 .   ? 2.845   22.070  -18.439 1.00 29.97  ? 744 HOH   A O    1 
HETATM 5462 O  O    . HOH   D 4 .   ? -12.139 -8.522  -21.271 1.00 42.49  ? 745 HOH   A O    1 
HETATM 5463 O  O    . HOH   D 4 .   ? -2.869  -2.107  -37.537 1.00 25.52  ? 746 HOH   A O    1 
HETATM 5464 O  O    . HOH   D 4 .   ? -15.690 4.786   2.388   1.00 21.93  ? 747 HOH   A O    1 
HETATM 5465 O  O    . HOH   D 4 .   ? -13.284 26.805  -27.146 1.00 28.84  ? 748 HOH   A O    1 
HETATM 5466 O  O    . HOH   D 4 .   ? -25.094 12.102  -32.882 1.00 44.06  ? 749 HOH   A O    1 
HETATM 5467 O  O    . HOH   D 4 .   ? 2.504   10.605  -41.842 1.00 27.52  ? 750 HOH   A O    1 
HETATM 5468 O  O    . HOH   D 4 .   ? -31.566 14.495  -21.735 1.00 24.70  ? 751 HOH   A O    1 
HETATM 5469 O  O    . HOH   D 4 .   ? -30.501 17.629  -22.867 1.00 21.94  ? 752 HOH   A O    1 
HETATM 5470 O  O    . HOH   D 4 .   ? -35.884 17.930  -24.125 1.00 39.91  ? 753 HOH   A O    1 
HETATM 5471 O  O    . HOH   D 4 .   ? -32.772 6.617   -18.175 1.00 42.58  ? 754 HOH   A O    1 
HETATM 5472 O  O    . HOH   D 4 .   ? -7.898  5.138   -24.343 1.00 24.02  ? 755 HOH   A O    1 
HETATM 5473 O  O    . HOH   D 4 .   ? -14.168 32.103  -18.523 1.00 32.94  ? 756 HOH   A O    1 
HETATM 5474 O  O    . HOH   D 4 .   ? 0.255   34.147  -15.245 1.00 37.37  ? 757 HOH   A O    1 
HETATM 5475 O  O    . HOH   D 4 .   ? -24.549 3.970   3.849   1.00 35.40  ? 758 HOH   A O    1 
HETATM 5476 O  O    . HOH   D 4 .   ? -19.477 34.099  -8.513  1.00 43.60  ? 759 HOH   A O    1 
HETATM 5477 O  O    . HOH   D 4 .   ? -40.859 28.053  -10.169 1.00 31.27  ? 760 HOH   A O    1 
HETATM 5478 O  O    . HOH   D 4 .   ? -2.975  -5.452  -18.348 1.00 43.06  ? 761 HOH   A O    1 
HETATM 5479 O  O    . HOH   D 4 .   ? -23.734 16.387  -31.066 1.00 31.33  ? 762 HOH   A O    1 
HETATM 5480 O  O    . HOH   D 4 .   ? -21.797 10.801  10.627  1.00 40.69  ? 763 HOH   A O    1 
HETATM 5481 O  O    . HOH   D 4 .   ? -20.213 18.221  -30.447 1.00 34.85  ? 764 HOH   A O    1 
HETATM 5482 O  O    . HOH   D 4 .   ? 4.117   4.960   -22.574 1.00 25.96  ? 765 HOH   A O    1 
HETATM 5483 O  O    . HOH   D 4 .   ? -31.754 33.508  -7.253  1.00 30.59  ? 766 HOH   A O    1 
HETATM 5484 O  O    . HOH   D 4 .   ? -10.261 4.102   -9.795  1.00 49.79  ? 767 HOH   A O    1 
HETATM 5485 O  O    . HOH   D 4 .   ? 8.991   7.208   -12.068 1.00 20.76  ? 768 HOH   A O    1 
HETATM 5486 O  O    . HOH   D 4 .   ? -24.973 18.156  7.636   1.00 40.03  ? 769 HOH   A O    1 
HETATM 5487 O  O    . HOH   D 4 .   ? -2.566  25.494  -31.772 1.00 32.49  ? 770 HOH   A O    1 
HETATM 5488 O  O    . HOH   D 4 .   ? 1.550   1.157   -31.117 1.00 25.99  ? 771 HOH   A O    1 
HETATM 5489 O  O    . HOH   D 4 .   ? -31.966 10.886  -20.102 1.00 40.09  ? 772 HOH   A O    1 
HETATM 5490 O  O    . HOH   D 4 .   ? -4.417  22.395  -36.262 1.00 45.15  ? 773 HOH   A O    1 
HETATM 5491 O  O    . HOH   D 4 .   ? 18.415  20.602  -36.733 1.00 40.87  ? 774 HOH   A O    1 
HETATM 5492 O  O    . HOH   D 4 .   ? -21.104 15.860  8.005   1.00 42.49  ? 775 HOH   A O    1 
HETATM 5493 O  O    . HOH   D 4 .   ? 3.987   17.969  -12.807 1.00 27.12  ? 776 HOH   A O    1 
HETATM 5494 O  O    . HOH   D 4 .   ? -31.353 18.718  -25.118 1.00 36.56  ? 777 HOH   A O    1 
HETATM 5495 O  O    . HOH   D 4 .   ? -17.790 17.207  -29.865 1.00 32.47  ? 778 HOH   A O    1 
HETATM 5496 O  O    . HOH   D 4 .   ? -2.713  -3.491  -26.628 1.00 25.84  ? 779 HOH   A O    1 
HETATM 5497 O  O    . HOH   D 4 .   ? 11.134  7.794   -40.417 1.00 47.29  ? 780 HOH   A O    1 
HETATM 5498 O  O    . HOH   D 4 .   ? -13.974 9.513   -27.712 1.00 34.93  ? 781 HOH   A O    1 
HETATM 5499 O  O    . HOH   D 4 .   ? 11.060  10.932  -15.047 1.00 45.64  ? 782 HOH   A O    1 
HETATM 5500 O  O    . HOH   D 4 .   ? -32.631 4.377   -7.599  1.00 37.64  ? 783 HOH   A O    1 
HETATM 5501 O  O    . HOH   D 4 .   ? 3.401   22.246  -14.485 1.00 37.72  ? 784 HOH   A O    1 
HETATM 5502 O  O    . HOH   D 4 .   ? 11.960  14.962  -22.759 1.00 35.87  ? 785 HOH   A O    1 
HETATM 5503 O  O    . HOH   D 4 .   ? -26.677 11.943  7.032   1.00 43.49  ? 786 HOH   A O    1 
HETATM 5504 O  O    . HOH   D 4 .   ? -29.174 10.201  -23.680 1.00 32.64  ? 787 HOH   A O    1 
HETATM 5505 O  O    . HOH   D 4 .   ? -29.961 28.325  -19.689 1.00 49.24  ? 788 HOH   A O    1 
HETATM 5506 O  O    . HOH   D 4 .   ? -17.407 -2.826  -30.081 1.00 41.83  ? 789 HOH   A O    1 
HETATM 5507 O  O    . HOH   D 4 .   ? -22.931 2.373   1.678   1.00 36.20  ? 790 HOH   A O    1 
HETATM 5508 O  O    . HOH   D 4 .   ? -17.505 31.049  -5.701  1.00 30.20  ? 791 HOH   A O    1 
HETATM 5509 O  O    . HOH   D 4 .   ? 6.530   22.201  -22.483 1.00 35.35  ? 792 HOH   A O    1 
HETATM 5510 O  O    . HOH   D 4 .   ? -36.159 15.786  2.734   1.00 40.78  ? 793 HOH   A O    1 
HETATM 5511 O  O    . HOH   D 4 .   ? 8.318   7.213   -37.459 1.00 32.66  ? 794 HOH   A O    1 
HETATM 5512 O  O    . HOH   D 4 .   ? -13.144 11.047  1.417   1.00 28.32  ? 795 HOH   A O    1 
HETATM 5513 O  O    . HOH   D 4 .   ? 1.238   -3.675  -13.451 1.00 43.24  ? 796 HOH   A O    1 
HETATM 5514 O  O    . HOH   D 4 .   ? -32.913 14.714  -23.934 1.00 35.34  ? 797 HOH   A O    1 
HETATM 5515 O  O    . HOH   D 4 .   ? -16.851 13.785  7.408   1.00 36.72  ? 798 HOH   A O    1 
HETATM 5516 O  O    . HOH   D 4 .   ? -27.002 19.476  6.832   1.00 26.71  ? 799 HOH   A O    1 
HETATM 5517 O  O    . HOH   D 4 .   ? -22.113 18.670  8.258   1.00 44.22  ? 800 HOH   A O    1 
HETATM 5518 O  O    . HOH   D 4 .   ? -15.818 4.304   5.424   1.00 38.05  ? 801 HOH   A O    1 
HETATM 5519 O  O    . HOH   D 4 .   ? -23.280 14.132  8.349   1.00 40.16  ? 802 HOH   A O    1 
HETATM 5520 O  O    . HOH   D 4 .   ? -29.285 25.075  3.463   1.00 34.57  ? 803 HOH   A O    1 
HETATM 5521 O  O    . HOH   D 4 .   ? 0.837   -3.111  -16.246 1.00 45.31  ? 804 HOH   A O    1 
HETATM 5522 O  O    . HOH   D 4 .   ? -14.330 27.808  -29.633 1.00 46.86  ? 805 HOH   A O    1 
HETATM 5523 O  O    . HOH   D 4 .   ? 11.003  13.964  -14.511 1.00 43.12  ? 806 HOH   A O    1 
HETATM 5524 O  O    . HOH   D 4 .   ? -33.945 16.991  -25.031 1.00 39.61  ? 807 HOH   A O    1 
HETATM 5525 O  O    . HOH   D 4 .   ? -34.743 30.527  -4.892  1.00 45.96  ? 808 HOH   A O    1 
HETATM 5526 O  O    . HOH   D 4 .   ? 0.741   25.032  -29.068 1.00 38.24  ? 809 HOH   A O    1 
HETATM 5527 O  O    . HOH   D 4 .   ? 13.494  14.733  -17.477 1.00 42.24  ? 810 HOH   A O    1 
HETATM 5528 O  O    . HOH   D 4 .   ? -20.323 31.561  -3.258  1.00 48.09  ? 811 HOH   A O    1 
HETATM 5529 O  O    . HOH   D 4 .   ? 11.387  17.097  -14.680 1.00 41.33  ? 812 HOH   A O    1 
HETATM 5530 O  O    . HOH   D 4 .   ? -24.785 5.890   -24.198 1.00 38.03  ? 813 HOH   A O    1 
HETATM 5531 O  O    . HOH   D 4 .   ? -19.624 0.172   -22.797 1.00 35.50  ? 814 HOH   A O    1 
HETATM 5532 O  O    . HOH   D 4 .   ? -3.065  -5.893  -25.248 1.00 43.96  ? 815 HOH   A O    1 
HETATM 5533 O  O    . HOH   D 4 .   ? -0.186  -3.006  -26.607 1.00 35.18  ? 816 HOH   A O    1 
HETATM 5534 O  O    . HOH   D 4 .   ? 9.518   8.012   -25.993 1.00 41.49  ? 817 HOH   A O    1 
HETATM 5535 O  O    . HOH   D 4 .   ? -24.061 29.577  -16.178 1.00 25.38  ? 818 HOH   A O    1 
HETATM 5536 O  O    . HOH   D 4 .   ? 1.701   7.165   -44.374 1.00 46.92  ? 819 HOH   A O    1 
HETATM 5537 O  O    . HOH   D 4 .   ? 7.987   12.106  -23.964 1.00 29.27  ? 820 HOH   A O    1 
HETATM 5538 O  O    . HOH   D 4 .   ? -34.771 29.758  -2.891  1.00 41.28  ? 821 HOH   A O    1 
HETATM 5539 O  O    . HOH   D 4 .   ? 3.456   17.120  -10.191 1.00 32.57  ? 822 HOH   A O    1 
HETATM 5540 O  O    . HOH   D 4 .   ? -25.164 14.635  -32.432 1.00 37.55  ? 823 HOH   A O    1 
HETATM 5541 O  O    . HOH   D 4 .   ? -17.826 32.471  -12.154 1.00 32.34  ? 824 HOH   A O    1 
HETATM 5542 O  O    . HOH   D 4 .   ? -26.604 29.158  -1.424  1.00 29.83  ? 825 HOH   A O    1 
HETATM 5543 O  O    . HOH   D 4 .   ? -20.431 4.790   -23.081 1.00 32.67  ? 826 HOH   A O    1 
HETATM 5544 O  O    . HOH   D 4 .   ? 13.804  18.617  -17.495 1.00 43.79  ? 827 HOH   A O    1 
HETATM 5545 O  O    . HOH   D 4 .   ? 8.212   16.450  -11.482 1.00 33.55  ? 828 HOH   A O    1 
HETATM 5546 O  O    . HOH   D 4 .   ? -18.117 30.861  -1.917  1.00 41.54  ? 829 HOH   A O    1 
HETATM 5547 O  O    . HOH   D 4 .   ? -20.452 20.766  -31.865 1.00 47.33  ? 830 HOH   A O    1 
HETATM 5548 O  O    . HOH   D 4 .   ? -41.868 28.370  -12.635 1.00 38.96  ? 831 HOH   A O    1 
HETATM 5549 O  O    . HOH   D 4 .   ? -27.285 28.463  -18.789 1.00 24.90  ? 832 HOH   A O    1 
HETATM 5550 O  O    . HOH   D 4 .   ? -7.145  4.616   -43.991 1.00 48.02  ? 833 HOH   A O    1 
HETATM 5551 O  O    . HOH   D 4 .   ? -21.949 32.362  -24.779 1.00 38.00  ? 834 HOH   A O    1 
HETATM 5552 O  O    . HOH   D 4 .   ? 6.384   3.574   -22.700 1.00 40.04  ? 835 HOH   A O    1 
HETATM 5553 O  O    . HOH   D 4 .   ? -20.519 22.831  7.558   1.00 29.54  ? 836 HOH   A O    1 
HETATM 5554 O  O    . HOH   D 4 .   ? -18.647 10.432  -28.000 1.00 41.82  ? 837 HOH   A O    1 
HETATM 5555 O  O    . HOH   D 4 .   ? -21.622 30.077  -28.618 1.00 45.85  ? 838 HOH   A O    1 
HETATM 5556 O  O    . HOH   D 4 .   ? 10.043  10.839  -27.146 1.00 34.43  ? 839 HOH   A O    1 
HETATM 5557 O  O    . HOH   D 4 .   ? -18.826 12.394  -32.721 1.00 44.36  ? 840 HOH   A O    1 
HETATM 5558 O  O    . HOH   D 4 .   ? -10.956 2.434   -8.551  1.00 46.81  ? 841 HOH   A O    1 
HETATM 5559 O  O    . HOH   D 4 .   ? -38.294 26.106  -18.251 1.00 40.40  ? 842 HOH   A O    1 
HETATM 5560 O  O    . HOH   D 4 .   ? 13.878  13.779  -22.109 1.00 52.30  ? 843 HOH   A O    1 
HETATM 5561 O  O    . HOH   D 4 .   ? -1.089  27.184  -17.574 1.00 36.93  ? 844 HOH   A O    1 
HETATM 5562 O  O    . HOH   D 4 .   ? 11.139  12.557  -20.920 1.00 48.15  ? 845 HOH   A O    1 
HETATM 5563 O  O    . HOH   D 4 .   ? 5.488   7.128   -42.490 1.00 42.07  ? 846 HOH   A O    1 
HETATM 5564 O  O    . HOH   D 4 .   ? 9.773   13.647  -23.161 1.00 38.93  ? 847 HOH   A O    1 
HETATM 5565 O  O    . HOH   D 4 .   ? 10.491  15.172  -12.366 1.00 43.94  ? 848 HOH   A O    1 
HETATM 5566 O  O    . HOH   D 4 .   ? -28.466 24.103  5.797   1.00 30.94  ? 849 HOH   A O    1 
HETATM 5567 O  O    . HOH   D 4 .   ? 5.602   3.846   -26.368 1.00 37.65  ? 850 HOH   A O    1 
HETATM 5568 O  O    . HOH   D 4 .   ? -29.082 16.559  8.020   1.00 50.27  ? 851 HOH   A O    1 
HETATM 5569 O  O    . HOH   D 4 .   ? -16.360 0.653   -6.505  1.00 39.51  ? 852 HOH   A O    1 
HETATM 5570 O  O    . HOH   D 4 .   ? 10.846  8.985   -12.986 1.00 35.94  ? 853 HOH   A O    1 
HETATM 5571 O  O    . HOH   D 4 .   ? -17.032 2.312   2.038   1.00 29.08  ? 854 HOH   A O    1 
HETATM 5572 O  O    . HOH   D 4 .   ? -1.018  -0.413  -38.541 1.00 26.22  ? 855 HOH   A O    1 
HETATM 5573 O  O    . HOH   D 4 .   ? -1.912  15.388  -5.938  1.00 38.87  ? 856 HOH   A O    1 
HETATM 5574 O  O    . HOH   D 4 .   ? -44.585 17.793  -13.957 1.00 38.38  ? 857 HOH   A O    1 
HETATM 5575 O  O    . HOH   D 4 .   ? -35.969 9.558   -12.238 1.00 39.62  ? 858 HOH   A O    1 
HETATM 5576 O  O    . HOH   D 4 .   ? 2.006   24.264  -43.005 1.00 45.76  ? 859 HOH   A O    1 
HETATM 5577 O  O    . HOH   D 4 .   ? 0.527   17.913  -48.555 1.00 37.25  ? 860 HOH   A O    1 
HETATM 5578 O  O    . HOH   D 4 .   ? -33.580 5.934   -3.412  1.00 30.76  ? 861 HOH   A O    1 
HETATM 5579 O  O    . HOH   D 4 .   ? -17.394 8.054   -24.835 1.00 26.97  ? 862 HOH   A O    1 
HETATM 5580 O  O    . HOH   D 4 .   ? -19.532 26.849  5.404   1.00 25.22  ? 863 HOH   A O    1 
HETATM 5581 O  O    . HOH   D 4 .   ? -19.401 9.762   -25.889 1.00 30.29  ? 864 HOH   A O    1 
HETATM 5582 O  O    . HOH   D 4 .   ? -8.306  19.424  -3.594  1.00 38.01  ? 865 HOH   A O    1 
HETATM 5583 O  O    . HOH   D 4 .   ? -12.066 28.611  -2.973  1.00 37.11  ? 866 HOH   A O    1 
HETATM 5584 O  O    . HOH   D 4 .   ? -41.851 28.662  -5.576  1.00 50.53  ? 867 HOH   A O    1 
HETATM 5585 O  O    . HOH   D 4 .   ? 7.088   22.465  -29.024 1.00 40.94  ? 868 HOH   A O    1 
HETATM 5586 O  O    . HOH   D 4 .   ? 1.016   4.920   -7.522  1.00 44.63  ? 869 HOH   A O    1 
HETATM 5587 O  O    . HOH   D 4 .   ? -20.913 2.216   -23.063 1.00 46.97  ? 870 HOH   A O    1 
HETATM 5588 O  O    . HOH   D 4 .   ? -16.397 10.298  -28.986 1.00 45.60  ? 871 HOH   A O    1 
HETATM 5589 O  O    . HOH   D 4 .   ? -26.579 9.222   10.821  1.00 42.93  ? 872 HOH   A O    1 
HETATM 5590 O  O    . HOH   D 4 .   ? 9.566   4.491   -12.702 1.00 38.40  ? 873 HOH   A O    1 
HETATM 5591 O  O    . HOH   D 4 .   ? -24.056 28.981  2.580   1.00 40.06  ? 874 HOH   A O    1 
HETATM 5592 O  O    . HOH   D 4 .   ? 2.280   0.077   -40.366 1.00 47.29  ? 875 HOH   A O    1 
HETATM 5593 O  O    . HOH   D 4 .   ? 8.816   20.508  -26.981 1.00 34.61  ? 876 HOH   A O    1 
HETATM 5594 O  O    . HOH   D 4 .   ? -16.713 29.172  3.253   1.00 36.90  ? 877 HOH   A O    1 
HETATM 5595 O  O    . HOH   D 4 .   ? -16.505 20.791  6.376   1.00 34.92  ? 878 HOH   A O    1 
HETATM 5596 O  O    . HOH   D 4 .   ? 10.339  8.229   -31.263 1.00 41.03  ? 879 HOH   A O    1 
HETATM 5597 O  O    . HOH   D 4 .   ? -0.186  15.319  -6.616  1.00 34.12  ? 880 HOH   A O    1 
HETATM 5598 O  O    . HOH   D 4 .   ? 8.230   22.002  -24.535 1.00 44.50  ? 881 HOH   A O    1 
HETATM 5599 O  O    . HOH   D 4 .   ? -9.442  11.483  -1.387  1.00 30.50  ? 882 HOH   A O    1 
HETATM 5600 O  O    . HOH   D 4 .   ? 13.585  17.061  -15.803 1.00 36.13  ? 883 HOH   A O    1 
HETATM 5601 O  O    . HOH   D 4 .   ? 0.241   25.133  -14.454 1.00 31.34  ? 884 HOH   A O    1 
HETATM 5602 O  O    . HOH   D 4 .   ? 18.443  21.610  -34.225 1.00 41.50  ? 885 HOH   A O    1 
HETATM 5603 O  O    . HOH   D 4 .   ? -13.154 3.950   1.823   1.00 41.61  ? 886 HOH   A O    1 
HETATM 5604 O  O    . HOH   D 4 .   ? -18.544 5.538   -25.053 1.00 36.34  ? 887 HOH   A O    1 
HETATM 5605 O  O    . HOH   D 4 .   ? 8.647   8.041   -39.872 1.00 41.79  ? 888 HOH   A O    1 
HETATM 5606 O  O    . HOH   D 4 .   ? 5.582   1.946   -24.506 1.00 35.93  ? 889 HOH   A O    1 
HETATM 5607 O  O    . HOH   D 4 .   ? 8.855   6.410   -9.287  1.00 36.93  ? 890 HOH   A O    1 
HETATM 5608 O  O    . HOH   D 4 .   ? -19.168 9.648   -32.764 1.00 41.98  ? 891 HOH   A O    1 
HETATM 5609 O  O    . HOH   D 4 .   ? -23.749 2.155   3.757   1.00 46.24  ? 892 HOH   A O    1 
HETATM 5610 O  O    . HOH   D 4 .   ? 1.436   -4.501  -24.900 1.00 36.41  ? 893 HOH   A O    1 
HETATM 5611 O  O    . HOH   D 4 .   ? 4.865   15.129  -8.743  1.00 24.76  ? 894 HOH   A O    1 
HETATM 5612 O  O    . HOH   D 4 .   ? -33.702 4.981   -0.842  1.00 41.78  ? 895 HOH   A O    1 
HETATM 5613 O  O    . HOH   D 4 .   ? -1.398  27.885  -14.796 1.00 42.09  ? 896 HOH   A O    1 
HETATM 5614 O  O    . HOH   D 4 .   ? -7.360  17.323  -2.708  1.00 18.55  ? 897 HOH   A O    1 
HETATM 5615 O  O    . HOH   D 4 .   ? -22.486 21.376  8.821   1.00 26.34  ? 898 HOH   A O    1 
HETATM 5616 O  O    . HOH   D 4 .   ? -17.451 8.336   -30.686 1.00 38.87  ? 899 HOH   A O    1 
HETATM 5617 O  O    . HOH   D 4 .   ? -18.677 23.988  9.366   1.00 40.41  ? 900 HOH   A O    1 
HETATM 5618 O  O    . HOH   D 4 .   ? -7.133  11.088  -0.306  1.00 29.30  ? 901 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   ? 0.6007 0.6057 0.6411 -0.0353 0.1586  0.0549  2   LYS   A N   
2    C  CA  . LYS   A 2   ? 0.6857 0.6801 0.7218 -0.0368 0.1682  0.0614  2   LYS   A CA  
3    C  C   . LYS   A 2   ? 0.6887 0.6649 0.7002 -0.0263 0.1694  0.0712  2   LYS   A C   
4    O  O   . LYS   A 2   ? 0.7657 0.7255 0.7730 -0.0277 0.1738  0.0760  2   LYS   A O   
5    C  CB  . LYS   A 2   ? 0.6565 0.6660 0.6997 -0.0379 0.1754  0.0609  2   LYS   A CB  
6    C  CG  . LYS   A 2   ? 0.6137 0.6125 0.6449 -0.0345 0.1855  0.0699  2   LYS   A CG  
7    C  CD  . LYS   A 2   ? 0.6991 0.7151 0.7347 -0.0333 0.1912  0.0692  2   LYS   A CD  
8    C  CE  . LYS   A 2   ? 0.6809 0.6878 0.7095 -0.0328 0.2028  0.0772  2   LYS   A CE  
9    N  NZ  . LYS   A 2   ? 0.7097 0.7358 0.7516 -0.0370 0.2094  0.0744  2   LYS   A NZ  
22   N  N   . VAL   A 3   ? 0.4656 0.4453 0.4609 -0.0151 0.1657  0.0737  3   VAL   A N   
23   C  CA  . VAL   A 3   ? 0.5158 0.4814 0.4878 -0.0041 0.1641  0.0814  3   VAL   A CA  
24   C  C   . VAL   A 3   ? 0.4872 0.4544 0.4500 0.0023  0.1533  0.0788  3   VAL   A C   
25   O  O   . VAL   A 3   ? 0.4289 0.4094 0.3986 0.0017  0.1483  0.0723  3   VAL   A O   
26   C  CB  . VAL   A 3   ? 0.4772 0.4445 0.4338 0.0053  0.1694  0.0872  3   VAL   A CB  
27   C  CG1 . VAL   A 3   ? 0.5052 0.4662 0.4671 0.0002  0.1811  0.0920  3   VAL   A CG1 
28   C  CG2 . VAL   A 3   ? 0.5824 0.5676 0.5402 0.0087  0.1674  0.0823  3   VAL   A CG2 
38   N  N   . GLN   A 4   ? 0.4132 0.3673 0.3608 0.0088  0.1493  0.0835  4   GLN   A N   
39   C  CA  . GLN   A 4   ? 0.4243 0.3804 0.3603 0.0161  0.1391  0.0816  4   GLN   A CA  
40   C  C   . GLN   A 4   ? 0.4246 0.3906 0.3465 0.0262  0.1362  0.0808  4   GLN   A C   
41   O  O   . GLN   A 4   ? 0.4162 0.3818 0.3294 0.0312  0.1426  0.0856  4   GLN   A O   
42   C  CB  . GLN   A 4   ? 0.4683 0.4104 0.3917 0.0215  0.1349  0.0864  4   GLN   A CB  
43   C  CG  . GLN   A 4   ? 0.5848 0.5162 0.5212 0.0123  0.1361  0.0858  4   GLN   A CG  
44   C  CD  . GLN   A 4   ? 0.6380 0.5569 0.5625 0.0187  0.1314  0.0898  4   GLN   A CD  
45   O  OE1 . GLN   A 4   ? 0.7576 0.6717 0.6660 0.0289  0.1321  0.0957  4   GLN   A OE1 
46   N  NE2 . GLN   A 4   ? 0.7475 0.6623 0.6805 0.0131  0.1266  0.0862  4   GLN   A NE2 
55   N  N   . ALA   A 5   ? 0.3886 0.3634 0.3104 0.0288  0.1226  0.0721  5   ALA   A N   
56   C  CA  . ALA   A 5   ? 0.3315 0.3145 0.2397 0.0382  0.1181  0.0692  5   ALA   A CA  
57   C  C   . ALA   A 5   ? 0.3278 0.3123 0.2317 0.0411  0.1029  0.0620  5   ALA   A C   
58   O  O   . ALA   A 5   ? 0.3328 0.3132 0.2451 0.0359  0.0967  0.0597  5   ALA   A O   
59   C  CB  . ALA   A 5   ? 0.3909 0.3865 0.3088 0.0362  0.1211  0.0642  5   ALA   A CB  
65   N  N   . LYS   A 6   ? 0.3721 0.3627 0.2631 0.0493  0.0974  0.0580  6   LYS   A N   
66   C  CA  . LYS   A 6   ? 0.3494 0.3418 0.2362 0.0518  0.0838  0.0505  6   LYS   A CA  
67   C  C   . LYS   A 6   ? 0.3129 0.3136 0.2050 0.0513  0.0784  0.0409  6   LYS   A C   
68   O  O   . LYS   A 6   ? 0.3324 0.3387 0.2224 0.0543  0.0841  0.0403  6   LYS   A O   
69   C  CB  . LYS   A 6   ? 0.3877 0.3800 0.2532 0.0624  0.0811  0.0527  6   LYS   A CB  
70   C  CG  . LYS   A 6   ? 0.4696 0.4531 0.3268 0.0656  0.0846  0.0622  6   LYS   A CG  
71   C  CD  . LYS   A 6   ? 0.5212 0.5005 0.3879 0.0600  0.0763  0.0595  6   LYS   A CD  
72   C  CE  . LYS   A 6   ? 0.5602 0.5318 0.4160 0.0658  0.0781  0.0679  6   LYS   A CE  
73   N  NZ  . LYS   A 6   ? 0.6854 0.6498 0.5535 0.0587  0.0754  0.0681  6   LYS   A NZ  
87   N  N   . GLY   A 7   ? 0.3117 0.3124 0.2107 0.0478  0.0680  0.0336  7   GLY   A N   
88   C  CA  . GLY   A 7   ? 0.3150 0.3208 0.2183 0.0479  0.0629  0.0248  7   GLY   A CA  
89   C  C   . GLY   A 7   ? 0.2712 0.2768 0.1644 0.0520  0.0531  0.0176  7   GLY   A C   
90   O  O   . GLY   A 7   ? 0.2962 0.2987 0.1880 0.0507  0.0465  0.0166  7   GLY   A O   
94   N  N   . MET   A 8   ? 0.2933 0.3027 0.1798 0.0569  0.0528  0.0118  8   MET   A N   
95   C  CA  A MET   A 8   ? 0.3254 0.3348 0.2034 0.0600  0.0443  0.0029  8   MET   A CA  
96   C  CA  B MET   A 8   ? 0.3256 0.3350 0.2037 0.0600  0.0443  0.0029  8   MET   A CA  
97   C  CA  C MET   A 8   ? 0.3256 0.3351 0.2036 0.0601  0.0444  0.0029  8   MET   A CA  
98   C  C   . MET   A 8   ? 0.2599 0.2675 0.1478 0.0568  0.0406  -0.0048 8   MET   A C   
99   O  O   . MET   A 8   ? 0.2975 0.3073 0.1915 0.0572  0.0457  -0.0046 8   MET   A O   
100  C  CB  A MET   A 8   ? 0.3958 0.4100 0.2568 0.0690  0.0472  0.0015  8   MET   A CB  
101  C  CB  B MET   A 8   ? 0.3951 0.4092 0.2560 0.0689  0.0469  0.0013  8   MET   A CB  
102  C  CB  C MET   A 8   ? 0.3954 0.4096 0.2565 0.0690  0.0474  0.0014  8   MET   A CB  
103  C  CG  A MET   A 8   ? 0.3946 0.4102 0.2453 0.0725  0.0390  -0.0089 8   MET   A CG  
104  C  CG  B MET   A 8   ? 0.4044 0.4202 0.2533 0.0726  0.0383  -0.0060 8   MET   A CG  
105  C  CG  C MET   A 8   ? 0.3897 0.4051 0.2413 0.0723  0.0393  -0.0095 8   MET   A CG  
106  S  SD  A MET   A 8   ? 0.4743 0.4973 0.3026 0.0841  0.0426  -0.0091 8   MET   A SD  
107  S  SD  B MET   A 8   ? 0.4437 0.4667 0.2700 0.0842  0.0421  -0.0040 8   MET   A SD  
108  S  SD  C MET   A 8   ? 0.4765 0.4993 0.3054 0.0837  0.0416  -0.0106 8   MET   A SD  
109  C  CE  A MET   A 8   ? 0.4602 0.4846 0.2799 0.0874  0.0440  0.0019  8   MET   A CE  
110  C  CE  B MET   A 8   ? 0.4071 0.4321 0.2319 0.0877  0.0488  -0.0078 8   MET   A CE  
111  C  CE  C MET   A 8   ? 0.4134 0.4378 0.2429 0.0866  0.0550  -0.0011 8   MET   A CE  
137  N  N   . GLY   A 9   ? 0.2779 0.2816 0.1670 0.0542  0.0324  -0.0115 9   GLY   A N   
138  C  CA  . GLY   A 9   ? 0.2612 0.2608 0.1587 0.0517  0.0297  -0.0177 9   GLY   A CA  
139  C  C   . GLY   A 9   ? 0.2774 0.2716 0.1764 0.0476  0.0216  -0.0237 9   GLY   A C   
140  O  O   . GLY   A 9   ? 0.3047 0.3006 0.1976 0.0474  0.0173  -0.0248 9   GLY   A O   
144  N  N   . PHE   A 10  ? 0.2355 0.2237 0.1432 0.0445  0.0198  -0.0272 10  PHE   A N   
145  C  CA  . PHE   A 10  ? 0.2492 0.2309 0.1583 0.0405  0.0135  -0.0338 10  PHE   A CA  
146  C  C   . PHE   A 10  ? 0.2339 0.2120 0.1547 0.0346  0.0114  -0.0299 10  PHE   A C   
147  O  O   . PHE   A 10  ? 0.2276 0.2079 0.1562 0.0337  0.0145  -0.0237 10  PHE   A O   
148  C  CB  . PHE   A 10  ? 0.2622 0.2373 0.1679 0.0432  0.0137  -0.0422 10  PHE   A CB  
149  C  CG  . PHE   A 10  ? 0.2727 0.2521 0.1659 0.0492  0.0154  -0.0466 10  PHE   A CG  
150  C  CD1 . PHE   A 10  ? 0.3021 0.2843 0.1862 0.0493  0.0108  -0.0529 10  PHE   A CD1 
151  C  CD2 . PHE   A 10  ? 0.2787 0.2619 0.1686 0.0554  0.0218  -0.0442 10  PHE   A CD2 
152  C  CE1 . PHE   A 10  ? 0.3223 0.3101 0.1937 0.0557  0.0121  -0.0569 10  PHE   A CE1 
153  C  CE2 . PHE   A 10  ? 0.3299 0.3177 0.2070 0.0615  0.0237  -0.0478 10  PHE   A CE2 
154  C  CZ  . PHE   A 10  ? 0.3264 0.3164 0.1936 0.0619  0.0187  -0.0541 10  PHE   A CZ  
164  N  N   . GLY   A 11  ? 0.2319 0.2055 0.1543 0.0302  0.0063  -0.0342 11  GLY   A N   
165  C  CA  . GLY   A 11  ? 0.2247 0.1941 0.1566 0.0249  0.0041  -0.0318 11  GLY   A CA  
166  C  C   . GLY   A 11  ? 0.2210 0.1825 0.1538 0.0210  0.0005  -0.0390 11  GLY   A C   
167  O  O   . GLY   A 11  ? 0.2356 0.1948 0.1622 0.0219  -0.0006 -0.0468 11  GLY   A O   
171  N  N   . GLY   A 12  ? 0.2359 0.1932 0.1766 0.0165  -0.0010 -0.0366 12  GLY   A N   
172  C  CA  . GLY   A 12  ? 0.2349 0.1838 0.1777 0.0119  -0.0030 -0.0424 12  GLY   A CA  
173  C  C   . GLY   A 12  ? 0.2410 0.1780 0.1853 0.0135  0.0002  -0.0435 12  GLY   A C   
174  O  O   . GLY   A 12  ? 0.2360 0.1728 0.1811 0.0182  0.0033  -0.0392 12  GLY   A O   
178  N  N   . ASN   A 13  ? 0.2450 0.1717 0.1896 0.0096  -0.0001 -0.0496 13  ASN   A N   
179  C  CA  . ASN   A 13  ? 0.2627 0.1748 0.2076 0.0115  0.0037  -0.0502 13  ASN   A CA  
180  C  C   . ASN   A 13  ? 0.2735 0.1740 0.2161 0.0074  0.0042  -0.0600 13  ASN   A C   
181  O  O   . ASN   A 13  ? 0.2842 0.1902 0.2254 0.0030  0.0009  -0.0671 13  ASN   A O   
182  C  CB  . ASN   A 13  ? 0.2388 0.1475 0.1902 0.0107  0.0047  -0.0424 13  ASN   A CB  
183  C  CG  . ASN   A 13  ? 0.2343 0.1411 0.1905 0.0031  0.0026  -0.0428 13  ASN   A CG  
184  O  OD1 . ASN   A 13  ? 0.2669 0.1676 0.2226 -0.0019 0.0024  -0.0502 13  ASN   A OD1 
185  N  ND2 . ASN   A 13  ? 0.2370 0.1487 0.1981 0.0020  0.0016  -0.0359 13  ASN   A ND2 
192  N  N   . ARG   A 14  ? 0.2760 0.1605 0.2175 0.0095  0.0086  -0.0609 14  ARG   A N   
193  C  CA  . ARG   A 14  ? 0.3340 0.2047 0.2728 0.0059  0.0105  -0.0710 14  ARG   A CA  
194  C  C   . ARG   A 14  ? 0.3719 0.2392 0.3167 -0.0042 0.0092  -0.0749 14  ARG   A C   
195  O  O   . ARG   A 14  ? 0.4368 0.2981 0.3808 -0.0095 0.0093  -0.0857 14  ARG   A O   
196  C  CB  . ARG   A 14  ? 0.3816 0.2339 0.3174 0.0117  0.0166  -0.0696 14  ARG   A CB  
197  C  CG  . ARG   A 14  ? 0.3516 0.2085 0.2815 0.0211  0.0179  -0.0691 14  ARG   A CG  
198  C  CD  . ARG   A 14  ? 0.4914 0.3344 0.4192 0.0295  0.0235  -0.0646 14  ARG   A CD  
199  N  NE  . ARG   A 14  ? 0.4799 0.3306 0.4032 0.0388  0.0248  -0.0641 14  ARG   A NE  
200  C  CZ  . ARG   A 14  ? 0.5246 0.3651 0.4438 0.0477  0.0296  -0.0636 14  ARG   A CZ  
201  N  NH1 . ARG   A 14  ? 0.5800 0.4010 0.4983 0.0496  0.0339  -0.0622 14  ARG   A NH1 
202  N  NH2 . ARG   A 14  ? 0.5400 0.3900 0.4557 0.0555  0.0306  -0.0642 14  ARG   A NH2 
216  N  N   . LYS   A 15  ? 0.3364 0.2085 0.2876 -0.0073 0.0080  -0.0675 15  LYS   A N   
217  C  CA  . LYS   A 15  ? 0.3950 0.2659 0.3529 -0.0170 0.0071  -0.0708 15  LYS   A CA  
218  C  C   . LYS   A 15  ? 0.3463 0.2363 0.3066 -0.0212 0.0008  -0.0753 15  LYS   A C   
219  O  O   . LYS   A 15  ? 0.4091 0.3004 0.3723 -0.0284 -0.0007 -0.0850 15  LYS   A O   
220  C  CB  . LYS   A 15  ? 0.4042 0.2724 0.3672 -0.0179 0.0089  -0.0609 15  LYS   A CB  
221  C  CG  . LYS   A 15  ? 0.4358 0.3019 0.4064 -0.0281 0.0094  -0.0640 15  LYS   A CG  
222  C  CD  . LYS   A 15  ? 0.4851 0.3435 0.4584 -0.0276 0.0131  -0.0543 15  LYS   A CD  
223  C  CE  . LYS   A 15  ? 0.4585 0.3190 0.4400 -0.0372 0.0135  -0.0558 15  LYS   A CE  
224  N  NZ  . LYS   A 15  ? 0.4846 0.3427 0.4675 -0.0352 0.0159  -0.0451 15  LYS   A NZ  
238  N  N   . ILE   A 16  ? 0.3279 0.2328 0.2873 -0.0170 -0.0027 -0.0687 16  ILE   A N   
239  C  CA  . ILE   A 16  ? 0.3869 0.3094 0.3477 -0.0197 -0.0084 -0.0717 16  ILE   A CA  
240  C  C   . ILE   A 16  ? 0.3626 0.2937 0.3155 -0.0156 -0.0112 -0.0782 16  ILE   A C   
241  O  O   . ILE   A 16  ? 0.4237 0.3693 0.3763 -0.0170 -0.0160 -0.0825 16  ILE   A O   
242  C  CB  . ILE   A 16  ? 0.4443 0.3772 0.4077 -0.0173 -0.0103 -0.0615 16  ILE   A CB  
243  C  CG1 . ILE   A 16  ? 0.3598 0.2942 0.3181 -0.0093 -0.0087 -0.0542 16  ILE   A CG1 
244  C  CG2 . ILE   A 16  ? 0.4974 0.4232 0.4679 -0.0215 -0.0080 -0.0565 16  ILE   A CG2 
245  C  CD1 . ILE   A 16  ? 0.4394 0.3865 0.3983 -0.0071 -0.0111 -0.0476 16  ILE   A CD1 
257  N  N   . GLY   A 17  ? 0.3355 0.2587 0.2817 -0.0101 -0.0081 -0.0795 17  GLY   A N   
258  C  CA  . GLY   A 17  ? 0.3484 0.2793 0.2858 -0.0050 -0.0098 -0.0848 17  GLY   A CA  
259  C  C   . GLY   A 17  ? 0.2978 0.2371 0.2305 0.0029  -0.0090 -0.0753 17  GLY   A C   
260  O  O   . GLY   A 17  ? 0.3048 0.2481 0.2419 0.0033  -0.0089 -0.0658 17  GLY   A O   
264  N  N   . GLU   A 18  ? 0.3098 0.2517 0.2337 0.0089  -0.0081 -0.0787 18  GLU   A N   
265  C  CA  . GLU   A 18  ? 0.3065 0.2559 0.2257 0.0162  -0.0060 -0.0706 18  GLU   A CA  
266  C  C   . GLU   A 18  ? 0.3311 0.2954 0.2431 0.0189  -0.0096 -0.0718 18  GLU   A C   
267  O  O   . GLU   A 18  ? 0.3793 0.3484 0.2873 0.0173  -0.0135 -0.0814 18  GLU   A O   
268  C  CB  . GLU   A 18  ? 0.4004 0.3418 0.3150 0.0220  -0.0011 -0.0719 18  GLU   A CB  
269  C  CG  . GLU   A 18  ? 0.3782 0.3069 0.3003 0.0208  0.0021  -0.0676 18  GLU   A CG  
270  C  CD  . GLU   A 18  ? 0.4493 0.3701 0.3689 0.0274  0.0072  -0.0669 18  GLU   A CD  
271  O  OE1 . GLU   A 18  ? 0.4704 0.3960 0.3826 0.0331  0.0089  -0.0694 18  GLU   A OE1 
272  O  OE2 . GLU   A 18  ? 0.4694 0.3793 0.3941 0.0272  0.0096  -0.0638 18  GLU   A OE2 
279  N  N   . TYR   A 19  ? 0.2895 0.2614 0.1996 0.0232  -0.0080 -0.0624 19  TYR   A N   
280  C  CA  . TYR   A 19  ? 0.2819 0.2668 0.1844 0.0270  -0.0103 -0.0608 19  TYR   A CA  
281  C  C   . TYR   A 19  ? 0.3046 0.2924 0.2020 0.0336  -0.0049 -0.0520 19  TYR   A C   
282  O  O   . TYR   A 19  ? 0.2773 0.2593 0.1797 0.0339  -0.0002 -0.0474 19  TYR   A O   
283  C  CB  . TYR   A 19  ? 0.2722 0.2630 0.1804 0.0232  -0.0142 -0.0568 19  TYR   A CB  
284  C  CG  . TYR   A 19  ? 0.2760 0.2604 0.1949 0.0193  -0.0120 -0.0486 19  TYR   A CG  
285  C  CD1 . TYR   A 19  ? 0.2776 0.2631 0.1974 0.0222  -0.0079 -0.0384 19  TYR   A CD1 
286  C  CD2 . TYR   A 19  ? 0.2781 0.2557 0.2061 0.0127  -0.0135 -0.0512 19  TYR   A CD2 
287  C  CE1 . TYR   A 19  ? 0.2661 0.2470 0.1955 0.0187  -0.0063 -0.0322 19  TYR   A CE1 
288  C  CE2 . TYR   A 19  ? 0.3006 0.2735 0.2368 0.0102  -0.0116 -0.0438 19  TYR   A CE2 
289  C  CZ  . TYR   A 19  ? 0.2625 0.2378 0.1993 0.0132  -0.0085 -0.0348 19  TYR   A CZ  
290  O  OH  . TYR   A 19  ? 0.2851 0.2567 0.2303 0.0104  -0.0073 -0.0292 19  TYR   A OH  
300  N  N   . GLN   A 20  ? 0.2912 0.2888 0.1792 0.0389  -0.0051 -0.0492 20  GLN   A N   
301  C  CA  . GLN   A 20  ? 0.3020 0.3025 0.1833 0.0453  0.0011  -0.0418 20  GLN   A CA  
302  C  C   . GLN   A 20  ? 0.3642 0.3694 0.2450 0.0468  0.0026  -0.0313 20  GLN   A C   
303  O  O   . GLN   A 20  ? 0.3394 0.3515 0.2140 0.0491  -0.0014 -0.0316 20  GLN   A O   
304  C  CB  . GLN   A 20  ? 0.3485 0.3545 0.2155 0.0525  0.0017  -0.0476 20  GLN   A CB  
305  C  CG  . GLN   A 20  ? 0.3687 0.3772 0.2293 0.0590  0.0095  -0.0393 20  GLN   A CG  
306  C  CD  . GLN   A 20  ? 0.5070 0.5223 0.3514 0.0672  0.0104  -0.0435 20  GLN   A CD  
307  O  OE1 . GLN   A 20  ? 0.5047 0.5194 0.3445 0.0681  0.0073  -0.0545 20  GLN   A OE1 
308  N  NE2 . GLN   A 20  ? 0.6208 0.6418 0.4561 0.0736  0.0153  -0.0347 20  GLN   A NE2 
317  N  N   . PHE   A 21  ? 0.2957 0.2975 0.1828 0.0458  0.0086  -0.0225 21  PHE   A N   
318  C  CA  . PHE   A 21  ? 0.2926 0.2965 0.1777 0.0479  0.0127  -0.0122 21  PHE   A CA  
319  C  C   . PHE   A 21  ? 0.3361 0.3450 0.2069 0.0562  0.0173  -0.0096 21  PHE   A C   
320  O  O   . PHE   A 21  ? 0.3225 0.3313 0.1910 0.0586  0.0224  -0.0102 21  PHE   A O   
321  C  CB  . PHE   A 21  ? 0.2686 0.2678 0.1657 0.0434  0.0182  -0.0058 21  PHE   A CB  
322  C  CG  . PHE   A 21  ? 0.2441 0.2390 0.1536 0.0365  0.0139  -0.0078 21  PHE   A CG  
323  C  CD1 . PHE   A 21  ? 0.2561 0.2504 0.1689 0.0336  0.0106  -0.0051 21  PHE   A CD1 
324  C  CD2 . PHE   A 21  ? 0.2545 0.2456 0.1721 0.0334  0.0133  -0.0123 21  PHE   A CD2 
325  C  CE1 . PHE   A 21  ? 0.2609 0.2516 0.1843 0.0276  0.0070  -0.0068 21  PHE   A CE1 
326  C  CE2 . PHE   A 21  ? 0.2361 0.2232 0.1635 0.0280  0.0098  -0.0133 21  PHE   A CE2 
327  C  CZ  . PHE   A 21  ? 0.2264 0.2134 0.1567 0.0248  0.0067  -0.0107 21  PHE   A CZ  
337  N  N   . GLY   A 22  ? 0.3489 0.3630 0.2090 0.0614  0.0154  -0.0071 22  GLY   A N   
338  C  CA  . GLY   A 22  ? 0.3970 0.4170 0.2405 0.0707  0.0184  -0.0057 22  GLY   A CA  
339  C  C   . GLY   A 22  ? 0.4240 0.4527 0.2568 0.0752  0.0103  -0.0154 22  GLY   A C   
340  O  O   . GLY   A 22  ? 0.4764 0.5120 0.2935 0.0843  0.0118  -0.0142 22  GLY   A O   
344  N  N   . LYS   A 23  ? 0.3787 0.4083 0.2194 0.0693  0.0023  -0.0247 23  LYS   A N   
345  C  CA  . LYS   A 23  ? 0.4122 0.4518 0.2453 0.0719  -0.0060 -0.0358 23  LYS   A CA  
346  C  C   . LYS   A 23  ? 0.4489 0.4913 0.2918 0.0659  -0.0134 -0.0392 23  LYS   A C   
347  O  O   . LYS   A 23  ? 0.4944 0.5467 0.3314 0.0706  -0.0175 -0.0381 23  LYS   A O   
348  C  CB  . LYS   A 23  ? 0.4268 0.4643 0.2595 0.0698  -0.0075 -0.0480 23  LYS   A CB  
349  C  CG  . LYS   A 23  ? 0.5055 0.5541 0.3289 0.0728  -0.0150 -0.0610 23  LYS   A CG  
350  C  CD  . LYS   A 23  ? 0.5629 0.6051 0.3894 0.0683  -0.0161 -0.0741 23  LYS   A CD  
351  C  CE  . LYS   A 23  ? 0.6979 0.7325 0.5201 0.0721  -0.0078 -0.0704 23  LYS   A CE  
352  N  NZ  . LYS   A 23  ? 0.8734 0.9170 0.6778 0.0833  -0.0046 -0.0674 23  LYS   A NZ  
366  N  N   . ASP   A 24  ? 0.3633 0.3975 0.2210 0.0563  -0.0147 -0.0430 24  ASP   A N   
367  C  CA  . ASP   A 24  ? 0.4101 0.4461 0.2786 0.0496  -0.0206 -0.0462 24  ASP   A CA  
368  C  C   . ASP   A 24  ? 0.4220 0.4547 0.2966 0.0487  -0.0180 -0.0346 24  ASP   A C   
369  O  O   . ASP   A 24  ? 0.3909 0.4298 0.2685 0.0481  -0.0225 -0.0343 24  ASP   A O   
370  C  CB  . ASP   A 24  ? 0.4020 0.4286 0.2825 0.0403  -0.0216 -0.0539 24  ASP   A CB  
371  C  CG  . ASP   A 24  ? 0.4764 0.5025 0.3511 0.0409  -0.0225 -0.0654 24  ASP   A CG  
372  O  OD1 . ASP   A 24  ? 0.4864 0.5232 0.3553 0.0425  -0.0282 -0.0748 24  ASP   A OD1 
373  O  OD2 . ASP   A 24  ? 0.3691 0.3855 0.2442 0.0408  -0.0177 -0.0655 24  ASP   A OD2 
378  N  N   . LEU   A 25  ? 0.3424 0.3659 0.2195 0.0484  -0.0108 -0.0256 25  LEU   A N   
379  C  CA  . LEU   A 25  ? 0.3088 0.3272 0.1925 0.0466  -0.0074 -0.0154 25  LEU   A CA  
380  C  C   . LEU   A 25  ? 0.3181 0.3344 0.1932 0.0530  0.0004  -0.0057 25  LEU   A C   
381  O  O   . LEU   A 25  ? 0.3376 0.3556 0.2039 0.0576  0.0036  -0.0067 25  LEU   A O   
382  C  CB  . LEU   A 25  ? 0.3407 0.3496 0.2388 0.0382  -0.0057 -0.0152 25  LEU   A CB  
383  C  CG  . LEU   A 25  ? 0.3895 0.3979 0.2966 0.0315  -0.0117 -0.0231 25  LEU   A CG  
384  C  CD1 . LEU   A 25  ? 0.3930 0.3921 0.3122 0.0248  -0.0096 -0.0218 25  LEU   A CD1 
385  C  CD2 . LEU   A 25  ? 0.4840 0.4989 0.3930 0.0311  -0.0164 -0.0222 25  LEU   A CD2 
397  N  N   . PRO   A 26  ? 0.3385 0.3500 0.2168 0.0527  0.0046  0.0039  26  PRO   A N   
398  C  CA  . PRO   A 26  ? 0.3349 0.3429 0.2056 0.0579  0.0135  0.0136  26  PRO   A CA  
399  C  C   . PRO   A 26  ? 0.3496 0.3532 0.2247 0.0549  0.0201  0.0140  26  PRO   A C   
400  O  O   . PRO   A 26  ? 0.3368 0.3375 0.2238 0.0481  0.0187  0.0095  26  PRO   A O   
401  C  CB  . PRO   A 26  ? 0.3941 0.3954 0.2705 0.0559  0.0165  0.0220  26  PRO   A CB  
402  C  CG  . PRO   A 26  ? 0.4495 0.4549 0.3314 0.0534  0.0077  0.0170  26  PRO   A CG  
403  C  CD  . PRO   A 26  ? 0.4275 0.4361 0.3157 0.0479  0.0020  0.0062  26  PRO   A CD  
411  N  N   . LEU   A 27  ? 0.3478 0.3507 0.2140 0.0604  0.0280  0.0206  27  LEU   A N   
412  C  CA  . LEU   A 27  ? 0.3736 0.3734 0.2458 0.0575  0.0360  0.0230  27  LEU   A CA  
413  C  C   . LEU   A 27  ? 0.3279 0.3211 0.2155 0.0493  0.0393  0.0273  27  LEU   A C   
414  O  O   . LEU   A 27  ? 0.3419 0.3309 0.2319 0.0477  0.0385  0.0314  27  LEU   A O   
415  C  CB  . LEU   A 27  ? 0.3883 0.3882 0.2482 0.0645  0.0453  0.0309  27  LEU   A CB  
416  C  CG  . LEU   A 27  ? 0.3836 0.3910 0.2286 0.0727  0.0441  0.0262  27  LEU   A CG  
417  C  CD1 . LEU   A 27  ? 0.4628 0.4698 0.2927 0.0813  0.0529  0.0362  27  LEU   A CD1 
418  C  CD2 . LEU   A 27  ? 0.3964 0.4063 0.2451 0.0713  0.0456  0.0199  27  LEU   A CD2 
430  N  N   . LEU   A 28  ? 0.2974 0.2907 0.1966 0.0439  0.0416  0.0246  28  LEU   A N   
431  C  CA  . LEU   A 28  ? 0.2624 0.2521 0.1768 0.0362  0.0441  0.0269  28  LEU   A CA  
432  C  C   . LEU   A 28  ? 0.2719 0.2582 0.1873 0.0354  0.0550  0.0355  28  LEU   A C   
433  O  O   . LEU   A 28  ? 0.3077 0.2958 0.2159 0.0396  0.0622  0.0389  28  LEU   A O   
434  C  CB  . LEU   A 28  ? 0.2616 0.2549 0.1870 0.0323  0.0429  0.0210  28  LEU   A CB  
435  C  CG  . LEU   A 28  ? 0.2624 0.2563 0.1881 0.0322  0.0337  0.0128  28  LEU   A CG  
436  C  CD1 . LEU   A 28  ? 0.3301 0.3268 0.2633 0.0312  0.0342  0.0080  28  LEU   A CD1 
437  C  CD2 . LEU   A 28  ? 0.3032 0.2937 0.2356 0.0274  0.0278  0.0119  28  LEU   A CD2 
449  N  N   . GLU   A 29  ? 0.2852 0.2660 0.2101 0.0295  0.0567  0.0386  29  GLU   A N   
450  C  CA  . GLU   A 29  ? 0.2807 0.2564 0.2089 0.0269  0.0678  0.0460  29  GLU   A CA  
451  C  C   . GLU   A 29  ? 0.2662 0.2470 0.2107 0.0194  0.0718  0.0430  29  GLU   A C   
452  O  O   . GLU   A 29  ? 0.2543 0.2367 0.2115 0.0133  0.0670  0.0384  29  GLU   A O   
453  C  CB  . GLU   A 29  ? 0.3636 0.3297 0.2930 0.0246  0.0683  0.0503  29  GLU   A CB  
454  C  CG  . GLU   A 29  ? 0.5148 0.4768 0.4279 0.0332  0.0653  0.0545  29  GLU   A CG  
455  C  CD  . GLU   A 29  ? 0.6689 0.6232 0.5847 0.0315  0.0630  0.0566  29  GLU   A CD  
456  O  OE1 . GLU   A 29  ? 0.6923 0.6438 0.6221 0.0233  0.0629  0.0541  29  GLU   A OE1 
457  O  OE2 . GLU   A 29  ? 0.7801 0.7322 0.6836 0.0391  0.0606  0.0602  29  GLU   A OE2 
464  N  N   . ILE   A 30  ? 0.2750 0.2602 0.2190 0.0206  0.0800  0.0450  30  ILE   A N   
465  C  CA  . ILE   A 30  ? 0.2728 0.2664 0.2328 0.0145  0.0841  0.0418  30  ILE   A CA  
466  C  C   . ILE   A 30  ? 0.2717 0.2632 0.2364 0.0106  0.0976  0.0482  30  ILE   A C   
467  O  O   . ILE   A 30  ? 0.3215 0.3026 0.2758 0.0131  0.1043  0.0561  30  ILE   A O   
468  C  CB  . ILE   A 30  ? 0.2574 0.2610 0.2152 0.0194  0.0812  0.0364  30  ILE   A CB  
469  C  CG1 . ILE   A 30  ? 0.2912 0.2946 0.2330 0.0274  0.0867  0.0406  30  ILE   A CG1 
470  C  CG2 . ILE   A 30  ? 0.2745 0.2784 0.2299 0.0216  0.0687  0.0296  30  ILE   A CG2 
471  C  CD1 . ILE   A 30  ? 0.3263 0.3395 0.2668 0.0321  0.0869  0.0357  30  ILE   A CD1 
483  N  N   . THR   A 31  ? 0.2709 0.2722 0.2505 0.0050  0.1024  0.0452  31  THR   A N   
484  C  CA  . THR   A 31  ? 0.2762 0.2770 0.2633 -0.0004 0.1161  0.0502  31  THR   A CA  
485  C  C   . THR   A 31  ? 0.3370 0.3517 0.3289 0.0011  0.1215  0.0484  31  THR   A C   
486  O  O   . THR   A 31  ? 0.2916 0.3165 0.2853 0.0047  0.1140  0.0420  31  THR   A O   
487  C  CB  . THR   A 31  ? 0.4002 0.3996 0.4053 -0.0117 0.1181  0.0478  31  THR   A CB  
488  O  OG1 . THR   A 31  ? 0.4490 0.4599 0.4670 -0.0148 0.1080  0.0387  31  THR   A OG1 
489  C  CG2 . THR   A 31  ? 0.4031 0.3861 0.4016 -0.0125 0.1167  0.0517  31  THR   A CG2 
497  N  N   . ARG   A 32  ? 0.3163 0.3305 0.3090 -0.0007 0.1355  0.0546  32  ARG   A N   
498  C  CA  . ARG   A 32  ? 0.3444 0.3727 0.3419 0.0010  0.1418  0.0533  32  ARG   A CA  
499  C  C   . ARG   A 32  ? 0.4080 0.4401 0.4214 -0.0086 0.1561  0.0560  32  ARG   A C   
500  O  O   . ARG   A 32  ? 0.4422 0.4607 0.4528 -0.0125 0.1624  0.0621  32  ARG   A O   
501  C  CB  . ARG   A 32  ? 0.4004 0.4246 0.3759 0.0121  0.1460  0.0593  32  ARG   A CB  
502  C  CG  . ARG   A 32  ? 0.4376 0.4764 0.4149 0.0160  0.1521  0.0578  32  ARG   A CG  
503  C  CD  . ARG   A 32  ? 0.4489 0.4844 0.4021 0.0285  0.1528  0.0616  32  ARG   A CD  
504  N  NE  . ARG   A 32  ? 0.4370 0.4863 0.3903 0.0338  0.1563  0.0584  32  ARG   A NE  
505  C  CZ  . ARG   A 32  ? 0.5292 0.5834 0.4844 0.0331  0.1654  0.0615  32  ARG   A CZ  
506  N  NH1 . ARG   A 32  ? 0.5018 0.5477 0.4590 0.0272  0.1731  0.0683  32  ARG   A NH1 
507  N  NH2 . ARG   A 32  ? 0.4883 0.5552 0.4434 0.0384  0.1664  0.0573  32  ARG   A NH2 
521  N  N   . ASP   A 33  ? 0.3400 0.3907 0.3706 -0.0124 0.1578  0.0499  33  ASP   A N   
522  C  CA  . ASP   A 33  ? 0.3663 0.4250 0.4131 -0.0215 0.1679  0.0499  33  ASP   A CA  
523  C  C   . ASP   A 33  ? 0.4354 0.5047 0.4770 -0.0150 0.1737  0.0516  33  ASP   A C   
524  O  O   . ASP   A 33  ? 0.3659 0.4527 0.4143 -0.0111 0.1712  0.0459  33  ASP   A O   
525  C  CB  . ASP   A 33  ? 0.4297 0.5047 0.5024 -0.0314 0.1646  0.0404  33  ASP   A CB  
526  C  CG  . ASP   A 33  ? 0.4502 0.5358 0.5399 -0.0409 0.1721  0.0387  33  ASP   A CG  
527  O  OD1 . ASP   A 33  ? 0.4994 0.5790 0.5811 -0.0399 0.1807  0.0453  33  ASP   A OD1 
528  O  OD2 . ASP   A 33  ? 0.6115 0.7115 0.7222 -0.0493 0.1690  0.0307  33  ASP   A OD2 
533  N  N   . SER   A 34  ? 0.4068 0.4658 0.4367 -0.0136 0.1815  0.0592  34  SER   A N   
534  C  CA  . SER   A 34  ? 0.5064 0.5734 0.5277 -0.0062 0.1867  0.0614  34  SER   A CA  
535  C  C   . SER   A 34  ? 0.4174 0.5060 0.4599 -0.0126 0.1918  0.0560  34  SER   A C   
536  O  O   . SER   A 34  ? 0.5107 0.6121 0.5505 -0.0059 0.1935  0.0543  34  SER   A O   
537  C  CB  . SER   A 34  ? 0.5095 0.5602 0.5135 -0.0029 0.1941  0.0712  34  SER   A CB  
538  O  OG  . SER   A 34  ? 0.5660 0.6106 0.5823 -0.0139 0.2015  0.0738  34  SER   A OG  
544  N  N   . SER   A 35  ? 0.3977 0.4913 0.4612 -0.0253 0.1940  0.0528  35  SER   A N   
545  C  CA  . SER   A 35  ? 0.4333 0.5497 0.5181 -0.0318 0.1984  0.0474  35  SER   A CA  
546  C  C   . SER   A 35  ? 0.3579 0.4965 0.4509 -0.0258 0.1920  0.0393  35  SER   A C   
547  O  O   . SER   A 35  ? 0.3737 0.5326 0.4780 -0.0260 0.1961  0.0361  35  SER   A O   
548  C  CB  . SER   A 35  ? 0.4586 0.5764 0.5639 -0.0461 0.1998  0.0441  35  SER   A CB  
549  O  OG  . SER   A 35  ? 0.4033 0.5302 0.5222 -0.0492 0.1896  0.0356  35  SER   A OG  
555  N  N   . VAL   A 36  ? 0.4178 0.5526 0.5046 -0.0194 0.1826  0.0364  36  VAL   A N   
556  C  CA  . VAL   A 36  ? 0.3862 0.5392 0.4796 -0.0121 0.1763  0.0291  36  VAL   A CA  
557  C  C   . VAL   A 36  ? 0.3810 0.5236 0.4518 0.0019  0.1712  0.0311  36  VAL   A C   
558  O  O   . VAL   A 36  ? 0.3393 0.4909 0.4108 0.0093  0.1623  0.0250  36  VAL   A O   
559  C  CB  . VAL   A 36  ? 0.3953 0.5587 0.5087 -0.0184 0.1683  0.0211  36  VAL   A CB  
560  C  CG1 . VAL   A 36  ? 0.4462 0.6285 0.5838 -0.0298 0.1712  0.0164  36  VAL   A CG1 
561  C  CG2 . VAL   A 36  ? 0.3979 0.5406 0.5049 -0.0227 0.1635  0.0231  36  VAL   A CG2 
571  N  N   . GLU   A 37  ? 0.3704 0.4935 0.4192 0.0059  0.1734  0.0386  37  GLU   A N   
572  C  CA  . GLU   A 37  ? 0.4444 0.5573 0.4701 0.0185  0.1674  0.0398  37  GLU   A CA  
573  C  C   . GLU   A 37  ? 0.3702 0.4795 0.3964 0.0197  0.1509  0.0328  37  GLU   A C   
574  O  O   . GLU   A 37  ? 0.3411 0.4527 0.3597 0.0285  0.1428  0.0279  37  GLU   A O   
575  C  CB  . GLU   A 37  ? 0.4125 0.5358 0.4310 0.0284  0.1689  0.0374  37  GLU   A CB  
576  C  CG  . GLU   A 37  ? 0.5020 0.6231 0.5121 0.0286  0.1785  0.0431  37  GLU   A CG  
577  C  CD  . GLU   A 37  ? 0.6575 0.7825 0.6526 0.0406  0.1780  0.0412  37  GLU   A CD  
578  O  OE1 . GLU   A 37  ? 0.5900 0.7312 0.5958 0.0434  0.1776  0.0350  37  GLU   A OE1 
579  O  OE2 . GLU   A 37  ? 0.7700 0.8820 0.7428 0.0474  0.1776  0.0455  37  GLU   A OE2 
586  N  N   . MET   A 38  ? 0.3326 0.4353 0.3674 0.0109  0.1468  0.0324  38  MET   A N   
587  C  CA  . MET   A 38  ? 0.2682 0.3679 0.3046 0.0114  0.1323  0.0264  38  MET   A CA  
588  C  C   . MET   A 38  ? 0.3195 0.3996 0.3442 0.0093  0.1278  0.0303  38  MET   A C   
589  O  O   . MET   A 38  ? 0.3269 0.3986 0.3520 0.0032  0.1358  0.0363  38  MET   A O   
590  C  CB  . MET   A 38  ? 0.3406 0.4544 0.4007 0.0030  0.1294  0.0203  38  MET   A CB  
591  C  CG  . MET   A 38  ? 0.4520 0.5886 0.5265 0.0053  0.1319  0.0152  38  MET   A CG  
592  S  SD  . MET   A 38  ? 0.7695 0.9088 0.8335 0.0191  0.1207  0.0098  38  MET   A SD  
593  C  CE  . MET   A 38  ? 0.4899 0.6582 0.5737 0.0211  0.1267  0.0051  38  MET   A CE  
603  N  N   . CYS   A 39  ? 0.2519 0.3243 0.2663 0.0144  0.1157  0.0271  39  CYS   A N   
604  C  CA  . CYS   A 39  ? 0.2477 0.3041 0.2527 0.0130  0.1098  0.0296  39  CYS   A CA  
605  C  C   . CYS   A 39  ? 0.2260 0.2846 0.2433 0.0080  0.0999  0.0237  39  CYS   A C   
606  O  O   . CYS   A 39  ? 0.2401 0.3109 0.2679 0.0088  0.0957  0.0178  39  CYS   A O   
607  C  CB  . CYS   A 39  ? 0.2468 0.2940 0.2309 0.0223  0.1032  0.0296  39  CYS   A CB  
608  S  SG  . CYS   A 39  ? 0.3402 0.3809 0.3044 0.0290  0.1132  0.0379  39  CYS   A SG  
613  N  N   . PHE   A 40  ? 0.2197 0.2665 0.2349 0.0036  0.0966  0.0257  40  PHE   A N   
614  C  CA  . PHE   A 40  ? 0.1958 0.2439 0.2221 -0.0016 0.0884  0.0209  40  PHE   A CA  
615  C  C   . PHE   A 40  ? 0.2075 0.2417 0.2214 0.0008  0.0801  0.0218  40  PHE   A C   
616  O  O   . PHE   A 40  ? 0.2268 0.2496 0.2283 0.0026  0.0829  0.0274  40  PHE   A O   
617  C  CB  . PHE   A 40  ? 0.2513 0.3011 0.2930 -0.0122 0.0947  0.0214  40  PHE   A CB  
618  C  CG  . PHE   A 40  ? 0.2493 0.3136 0.3050 -0.0162 0.1045  0.0206  40  PHE   A CG  
619  C  CD1 . PHE   A 40  ? 0.3270 0.3874 0.3780 -0.0165 0.1167  0.0271  40  PHE   A CD1 
620  C  CD2 . PHE   A 40  ? 0.2513 0.3339 0.3241 -0.0187 0.1015  0.0134  40  PHE   A CD2 
621  C  CE1 . PHE   A 40  ? 0.3250 0.3999 0.3895 -0.0203 0.1266  0.0262  40  PHE   A CE1 
622  C  CE2 . PHE   A 40  ? 0.2700 0.3691 0.3572 -0.0222 0.1103  0.0118  40  PHE   A CE2 
623  C  CZ  . PHE   A 40  ? 0.3085 0.4036 0.3924 -0.0238 0.1231  0.0181  40  PHE   A CZ  
633  N  N   . MET   A 41  ? 0.2004 0.2361 0.2169 0.0017  0.0700  0.0167  41  MET   A N   
634  C  CA  . MET   A 41  ? 0.1785 0.2029 0.1851 0.0034  0.0618  0.0167  41  MET   A CA  
635  C  C   . MET   A 41  ? 0.1860 0.2049 0.1993 -0.0037 0.0616  0.0179  41  MET   A C   
636  O  O   . MET   A 41  ? 0.1841 0.2044 0.2043 -0.0066 0.0552  0.0142  41  MET   A O   
637  C  CB  . MET   A 41  ? 0.1858 0.2134 0.1933 0.0069  0.0527  0.0110  41  MET   A CB  
638  C  CG  . MET   A 41  ? 0.1907 0.2208 0.1904 0.0142  0.0529  0.0092  41  MET   A CG  
639  S  SD  . MET   A 41  ? 0.2239 0.2435 0.2035 0.0202  0.0520  0.0111  41  MET   A SD  
640  C  CE  . MET   A 41  ? 0.2306 0.2418 0.2070 0.0196  0.0412  0.0075  41  MET   A CE  
650  N  N   . GLU   A 42  ? 0.1971 0.2095 0.2082 -0.0064 0.0698  0.0234  42  GLU   A N   
651  C  CA  . GLU   A 42  ? 0.2102 0.2158 0.2275 -0.0132 0.0716  0.0247  42  GLU   A CA  
652  C  C   . GLU   A 42  ? 0.2282 0.2207 0.2342 -0.0116 0.0790  0.0326  42  GLU   A C   
653  O  O   . GLU   A 42  ? 0.2458 0.2380 0.2451 -0.0082 0.0867  0.0373  42  GLU   A O   
654  C  CB  . GLU   A 42  ? 0.2405 0.2559 0.2762 -0.0215 0.0769  0.0213  42  GLU   A CB  
655  C  CG  . GLU   A 42  ? 0.2702 0.2775 0.3128 -0.0294 0.0804  0.0218  42  GLU   A CG  
656  C  CD  . GLU   A 42  ? 0.3129 0.3319 0.3755 -0.0387 0.0842  0.0159  42  GLU   A CD  
657  O  OE1 . GLU   A 42  ? 0.3938 0.4269 0.4649 -0.0392 0.0878  0.0137  42  GLU   A OE1 
658  O  OE2 . GLU   A 42  ? 0.2952 0.3098 0.3653 -0.0454 0.0840  0.0132  42  GLU   A OE2 
665  N  N   . ASN   A 43  ? 0.2217 0.2036 0.2250 -0.0131 0.0768  0.0344  43  ASN   A N   
666  C  CA  . ASN   A 43  ? 0.2387 0.2067 0.2335 -0.0122 0.0844  0.0421  43  ASN   A CA  
667  C  C   . ASN   A 43  ? 0.2574 0.2183 0.2618 -0.0197 0.0852  0.0405  43  ASN   A C   
668  O  O   . ASN   A 43  ? 0.2440 0.2123 0.2608 -0.0251 0.0794  0.0333  43  ASN   A O   
669  C  CB  . ASN   A 43  ? 0.2613 0.2237 0.2376 -0.0025 0.0797  0.0461  43  ASN   A CB  
670  C  CG  . ASN   A 43  ? 0.2472 0.2113 0.2225 -0.0010 0.0677  0.0411  43  ASN   A CG  
671  O  OD1 . ASN   A 43  ? 0.2555 0.2143 0.2355 -0.0046 0.0650  0.0400  43  ASN   A OD1 
672  N  ND2 . ASN   A 43  ? 0.2365 0.2078 0.2064 0.0038  0.0605  0.0373  43  ASN   A ND2 
679  N  N   . THR   A 44  ? 0.2747 0.2207 0.2723 -0.0191 0.0919  0.0471  44  THR   A N   
680  C  CA  . THR   A 44  ? 0.2711 0.2089 0.2781 -0.0265 0.0940  0.0451  44  THR   A CA  
681  C  C   . THR   A 44  ? 0.2896 0.2309 0.2993 -0.0266 0.0820  0.0389  44  THR   A C   
682  O  O   . THR   A 44  ? 0.2810 0.2250 0.3035 -0.0340 0.0802  0.0325  44  THR   A O   
683  C  CB  . THR   A 44  ? 0.3576 0.2764 0.3532 -0.0231 0.1024  0.0541  44  THR   A CB  
684  O  OG1 . THR   A 44  ? 0.4235 0.3380 0.4176 -0.0240 0.1154  0.0604  44  THR   A OG1 
685  C  CG2 . THR   A 44  ? 0.3812 0.2887 0.3844 -0.0296 0.1043  0.0519  44  THR   A CG2 
693  N  N   . ASP   A 45  ? 0.2452 0.1874 0.2431 -0.0185 0.0737  0.0400  45  ASP   A N   
694  C  CA  . ASP   A 45  ? 0.2314 0.1748 0.2303 -0.0181 0.0636  0.0356  45  ASP   A CA  
695  C  C   . ASP   A 45  ? 0.1907 0.1481 0.1972 -0.0197 0.0547  0.0281  45  ASP   A C   
696  O  O   . ASP   A 45  ? 0.2053 0.1644 0.2166 -0.0218 0.0482  0.0235  45  ASP   A O   
697  C  CB  . ASP   A 45  ? 0.2589 0.1974 0.2429 -0.0093 0.0590  0.0399  45  ASP   A CB  
698  C  CG  . ASP   A 45  ? 0.4667 0.3903 0.4423 -0.0061 0.0663  0.0475  45  ASP   A CG  
699  O  OD1 . ASP   A 45  ? 0.4680 0.3821 0.4500 -0.0118 0.0742  0.0485  45  ASP   A OD1 
700  O  OD2 . ASP   A 45  ? 0.4474 0.3688 0.4094 0.0026  0.0646  0.0523  45  ASP   A OD2 
705  N  N   . VAL   A 46  ? 0.1897 0.1562 0.1961 -0.0177 0.0545  0.0270  46  VAL   A N   
706  C  CA  . VAL   A 46  ? 0.1710 0.1484 0.1812 -0.0167 0.0464  0.0213  46  VAL   A CA  
707  C  C   . VAL   A 46  ? 0.1645 0.1526 0.1821 -0.0181 0.0501  0.0191  46  VAL   A C   
708  O  O   . VAL   A 46  ? 0.1840 0.1716 0.1973 -0.0161 0.0569  0.0229  46  VAL   A O   
709  C  CB  . VAL   A 46  ? 0.1754 0.1522 0.1732 -0.0094 0.0401  0.0220  46  VAL   A CB  
710  C  CG1 . VAL   A 46  ? 0.1724 0.1568 0.1739 -0.0087 0.0329  0.0166  46  VAL   A CG1 
711  C  CG2 . VAL   A 46  ? 0.2175 0.1859 0.2076 -0.0071 0.0372  0.0247  46  VAL   A CG2 
721  N  N   . LYS   A 47  ? 0.1721 0.1708 0.2006 -0.0207 0.0458  0.0131  47  LYS   A N   
722  C  CA  . LYS   A 47  ? 0.1579 0.1695 0.1939 -0.0205 0.0477  0.0102  47  LYS   A CA  
723  C  C   . LYS   A 47  ? 0.1535 0.1710 0.1878 -0.0155 0.0392  0.0065  47  LYS   A C   
724  O  O   . LYS   A 47  ? 0.1594 0.1765 0.1953 -0.0161 0.0327  0.0039  47  LYS   A O   
725  C  CB  . LYS   A 47  ? 0.1678 0.1891 0.2207 -0.0283 0.0512  0.0058  47  LYS   A CB  
726  C  CG  . LYS   A 47  ? 0.1810 0.2196 0.2433 -0.0271 0.0511  0.0017  47  LYS   A CG  
727  C  CD  . LYS   A 47  ? 0.2041 0.2545 0.2840 -0.0354 0.0562  -0.0029 47  LYS   A CD  
728  C  CE  . LYS   A 47  ? 0.1886 0.2411 0.2766 -0.0406 0.0511  -0.0083 47  LYS   A CE  
729  N  NZ  . LYS   A 47  ? 0.2470 0.3146 0.3542 -0.0493 0.0557  -0.0148 47  LYS   A NZ  
743  N  N   . VAL   A 48  ? 0.1475 0.1697 0.1779 -0.0102 0.0398  0.0065  48  VAL   A N   
744  C  CA  . VAL   A 48  ? 0.1408 0.1678 0.1703 -0.0051 0.0335  0.0031  48  VAL   A CA  
745  C  C   . VAL   A 48  ? 0.1394 0.1817 0.1806 -0.0049 0.0352  -0.0004 48  VAL   A C   
746  O  O   . VAL   A 48  ? 0.1489 0.1975 0.1935 -0.0051 0.0419  0.0004  48  VAL   A O   
747  C  CB  . VAL   A 48  ? 0.1534 0.1741 0.1699 0.0013  0.0325  0.0043  48  VAL   A CB  
748  C  CG1 . VAL   A 48  ? 0.1854 0.2096 0.2017 0.0065  0.0278  0.0008  48  VAL   A CG1 
749  C  CG2 . VAL   A 48  ? 0.2080 0.2168 0.2142 0.0014  0.0291  0.0064  48  VAL   A CG2 
759  N  N   . VAL   A 49  ? 0.1322 0.1816 0.1796 -0.0040 0.0295  -0.0041 49  VAL   A N   
760  C  CA  . VAL   A 49  ? 0.1300 0.1962 0.1881 -0.0018 0.0292  -0.0079 49  VAL   A CA  
761  C  C   . VAL   A 49  ? 0.1310 0.1958 0.1816 0.0075  0.0251  -0.0083 49  VAL   A C   
762  O  O   . VAL   A 49  ? 0.1403 0.1957 0.1836 0.0099  0.0197  -0.0078 49  VAL   A O   
763  C  CB  . VAL   A 49  ? 0.1292 0.2047 0.1982 -0.0061 0.0254  -0.0120 49  VAL   A CB  
764  C  CG1 . VAL   A 49  ? 0.1515 0.2467 0.2313 -0.0027 0.0238  -0.0164 49  VAL   A CG1 
765  C  CG2 . VAL   A 49  ? 0.1440 0.2183 0.2204 -0.0157 0.0300  -0.0124 49  VAL   A CG2 
775  N  N   . ASP   A 50  ? 0.1351 0.2084 0.1875 0.0125  0.0282  -0.0091 50  ASP   A N   
776  C  CA  . ASP   A 50  ? 0.1543 0.2264 0.2005 0.0218  0.0252  -0.0099 50  ASP   A CA  
777  C  C   . ASP   A 50  ? 0.1423 0.2302 0.1989 0.0250  0.0216  -0.0129 50  ASP   A C   
778  O  O   . ASP   A 50  ? 0.1460 0.2520 0.2139 0.0257  0.0243  -0.0154 50  ASP   A O   
779  C  CB  . ASP   A 50  ? 0.1767 0.2505 0.2192 0.0270  0.0305  -0.0096 50  ASP   A CB  
780  C  CG  . ASP   A 50  ? 0.1794 0.2500 0.2153 0.0369  0.0281  -0.0107 50  ASP   A CG  
781  O  OD1 . ASP   A 50  ? 0.1770 0.2446 0.2115 0.0406  0.0231  -0.0111 50  ASP   A OD1 
782  O  OD2 . ASP   A 50  ? 0.2267 0.2984 0.2588 0.0422  0.0324  -0.0111 50  ASP   A OD2 
787  N  N   . MET   A 51  ? 0.1419 0.2242 0.1942 0.0279  0.0156  -0.0127 51  MET   A N   
788  C  CA  . MET   A 51  ? 0.1302 0.2279 0.1902 0.0322  0.0116  -0.0153 51  MET   A CA  
789  C  C   . MET   A 51  ? 0.1460 0.2504 0.2047 0.0436  0.0121  -0.0155 51  MET   A C   
790  O  O   . MET   A 51  ? 0.1563 0.2780 0.2225 0.0490  0.0092  -0.0178 51  MET   A O   
791  C  CB  . MET   A 51  ? 0.1502 0.2388 0.2038 0.0335  0.0058  -0.0140 51  MET   A CB  
792  C  CG  . MET   A 51  ? 0.1420 0.2250 0.1973 0.0233  0.0051  -0.0142 51  MET   A CG  
793  S  SD  . MET   A 51  ? 0.1731 0.2767 0.2454 0.0153  0.0053  -0.0195 51  MET   A SD  
794  C  CE  . MET   A 51  ? 0.1618 0.2807 0.2367 0.0239  -0.0019 -0.0223 51  MET   A CE  
804  N  N   . GLY   A 52  ? 0.1608 0.2529 0.2098 0.0484  0.0151  -0.0137 52  GLY   A N   
805  C  CA  . GLY   A 52  ? 0.1763 0.2733 0.2235 0.0598  0.0163  -0.0141 52  GLY   A CA  
806  C  C   . GLY   A 52  ? 0.1565 0.2511 0.1989 0.0694  0.0118  -0.0128 52  GLY   A C   
807  O  O   . GLY   A 52  ? 0.1921 0.2995 0.2378 0.0795  0.0117  -0.0136 52  GLY   A O   
811  N  N   . HIS   A 53  ? 0.1646 0.2439 0.1993 0.0671  0.0084  -0.0106 53  HIS   A N   
812  C  CA  . HIS   A 53  ? 0.1657 0.2389 0.1937 0.0755  0.0050  -0.0081 53  HIS   A CA  
813  C  C   . HIS   A 53  ? 0.2037 0.2994 0.2412 0.0785  0.0007  -0.0097 53  HIS   A C   
814  O  O   . HIS   A 53  ? 0.2168 0.3118 0.2490 0.0877  -0.0020 -0.0074 53  HIS   A O   
815  C  CB  . HIS   A 53  ? 0.2073 0.2683 0.2254 0.0872  0.0076  -0.0062 53  HIS   A CB  
816  C  CG  . HIS   A 53  ? 0.2195 0.2577 0.2278 0.0830  0.0108  -0.0059 53  HIS   A CG  
817  N  ND1 . HIS   A 53  ? 0.3091 0.3403 0.3122 0.0888  0.0150  -0.0071 53  HIS   A ND1 
818  C  CD2 . HIS   A 53  ? 0.2137 0.2357 0.2164 0.0743  0.0102  -0.0053 53  HIS   A CD2 
819  C  CE1 . HIS   A 53  ? 0.3195 0.3320 0.3146 0.0829  0.0165  -0.0079 53  HIS   A CE1 
820  N  NE2 . HIS   A 53  ? 0.2746 0.2822 0.2698 0.0741  0.0136  -0.0068 53  HIS   A NE2 
829  N  N   . LYS   A 54  ? 0.1544 0.2692 0.2052 0.0707  0.0002  -0.0137 54  LYS   A N   
830  C  CA  . LYS   A 54  ? 0.1595 0.2963 0.2201 0.0714  -0.0046 -0.0169 54  LYS   A CA  
831  C  C   . LYS   A 54  ? 0.1529 0.2825 0.2119 0.0627  -0.0079 -0.0169 54  LYS   A C   
832  O  O   . LYS   A 54  ? 0.1474 0.2576 0.1998 0.0555  -0.0064 -0.0146 54  LYS   A O   
833  C  CB  . LYS   A 54  ? 0.1607 0.3222 0.2382 0.0663  -0.0025 -0.0225 54  LYS   A CB  
834  C  CG  . LYS   A 54  ? 0.2432 0.4150 0.3231 0.0762  0.0007  -0.0227 54  LYS   A CG  
835  C  CD  . LYS   A 54  ? 0.3154 0.5134 0.4132 0.0711  0.0034  -0.0282 54  LYS   A CD  
836  C  CE  . LYS   A 54  ? 0.4978 0.7056 0.5971 0.0820  0.0069  -0.0281 54  LYS   A CE  
837  N  NZ  . LYS   A 54  ? 0.5137 0.7384 0.6140 0.0963  0.0019  -0.0288 54  LYS   A NZ  
851  N  N   . TYR   A 55  ? 0.1545 0.3025 0.2201 0.0642  -0.0129 -0.0203 55  TYR   A N   
852  C  CA  . TYR   A 55  ? 0.1823 0.3272 0.2469 0.0578  -0.0165 -0.0213 55  TYR   A CA  
853  C  C   . TYR   A 55  ? 0.1468 0.3065 0.2260 0.0456  -0.0165 -0.0280 55  TYR   A C   
854  O  O   . TYR   A 55  ? 0.1522 0.3084 0.2311 0.0393  -0.0190 -0.0296 55  TYR   A O   
855  C  CB  . TYR   A 55  ? 0.1697 0.3222 0.2285 0.0688  -0.0220 -0.0202 55  TYR   A CB  
856  C  CG  . TYR   A 55  ? 0.1815 0.3127 0.2239 0.0793  -0.0206 -0.0124 55  TYR   A CG  
857  C  CD1 . TYR   A 55  ? 0.2056 0.3145 0.2368 0.0767  -0.0200 -0.0078 55  TYR   A CD1 
858  C  CD2 . TYR   A 55  ? 0.2370 0.3704 0.2764 0.0911  -0.0189 -0.0101 55  TYR   A CD2 
859  C  CE1 . TYR   A 55  ? 0.2435 0.3311 0.2606 0.0850  -0.0174 -0.0011 55  TYR   A CE1 
860  C  CE2 . TYR   A 55  ? 0.2557 0.3665 0.2802 0.1000  -0.0162 -0.0032 55  TYR   A CE2 
861  C  CZ  . TYR   A 55  ? 0.2533 0.3412 0.2674 0.0959  -0.0153 0.0010  55  TYR   A CZ  
862  O  OH  . TYR   A 55  ? 0.3009 0.3663 0.3018 0.1035  -0.0118 0.0070  55  TYR   A OH  
872  N  N   . TYR   A 56  ? 0.1426 0.3179 0.2347 0.0422  -0.0133 -0.0320 56  TYR   A N   
873  C  CA  . TYR   A 56  ? 0.1569 0.3459 0.2643 0.0301  -0.0117 -0.0387 56  TYR   A CA  
874  C  C   . TYR   A 56  ? 0.1498 0.3365 0.2630 0.0242  -0.0041 -0.0380 56  TYR   A C   
875  O  O   . TYR   A 56  ? 0.1559 0.3411 0.2650 0.0318  -0.0017 -0.0348 56  TYR   A O   
876  C  CB  . TYR   A 56  ? 0.1309 0.3523 0.2529 0.0326  -0.0162 -0.0468 56  TYR   A CB  
877  C  CG  . TYR   A 56  ? 0.1557 0.3812 0.2698 0.0411  -0.0239 -0.0470 56  TYR   A CG  
878  C  CD1 . TYR   A 56  ? 0.1583 0.3801 0.2718 0.0342  -0.0269 -0.0499 56  TYR   A CD1 
879  C  CD2 . TYR   A 56  ? 0.1775 0.4107 0.2849 0.0565  -0.0273 -0.0441 56  TYR   A CD2 
880  C  CE1 . TYR   A 56  ? 0.1566 0.3819 0.2614 0.0425  -0.0336 -0.0497 56  TYR   A CE1 
881  C  CE2 . TYR   A 56  ? 0.1977 0.4322 0.2955 0.0651  -0.0335 -0.0428 56  TYR   A CE2 
882  C  CZ  . TYR   A 56  ? 0.1523 0.3838 0.2493 0.0577  -0.0365 -0.0458 56  TYR   A CZ  
883  O  OH  . TYR   A 56  ? 0.2027 0.4370 0.2896 0.0670  -0.0423 -0.0444 56  TYR   A OH  
893  N  N   . SER   A 57  ? 0.1375 0.3227 0.2592 0.0114  0.0000  -0.0407 57  SER   A N   
894  C  CA  . SER   A 57  ? 0.1456 0.3280 0.2720 0.0057  0.0083  -0.0393 57  SER   A CA  
895  C  C   . SER   A 57  ? 0.1378 0.3285 0.2792 -0.0078 0.0124  -0.0448 57  SER   A C   
896  O  O   . SER   A 57  ? 0.1596 0.3466 0.3023 -0.0139 0.0096  -0.0478 57  SER   A O   
897  C  CB  . SER   A 57  ? 0.1396 0.2938 0.2500 0.0054  0.0113  -0.0318 57  SER   A CB  
898  O  OG  . SER   A 57  ? 0.1809 0.3309 0.2943 -0.0007 0.0195  -0.0300 57  SER   A OG  
904  N  N   . ASN   A 58  ? 0.1319 0.3305 0.2833 -0.0125 0.0200  -0.0457 58  ASN   A N   
905  C  CA  . ASN   A 58  ? 0.1429 0.3422 0.3064 -0.0263 0.0267  -0.0490 58  ASN   A CA  
906  C  C   . ASN   A 58  ? 0.1470 0.3180 0.2990 -0.0321 0.0318  -0.0425 58  ASN   A C   
907  O  O   . ASN   A 58  ? 0.1836 0.3515 0.3440 -0.0430 0.0383  -0.0443 58  ASN   A O   
908  C  CB  . ASN   A 58  ? 0.1605 0.3782 0.3394 -0.0300 0.0345  -0.0518 58  ASN   A CB  
909  C  CG  . ASN   A 58  ? 0.1801 0.3884 0.3494 -0.0239 0.0405  -0.0443 58  ASN   A CG  
910  O  OD1 . ASN   A 58  ? 0.1790 0.3639 0.3307 -0.0200 0.0405  -0.0371 58  ASN   A OD1 
911  N  ND2 . ASN   A 58  ? 0.1903 0.4186 0.3716 -0.0229 0.0455  -0.0466 58  ASN   A ND2 
918  N  N   . ASN   A 59  ? 0.1427 0.2940 0.2766 -0.0250 0.0297  -0.0353 59  ASN   A N   
919  C  CA  . ASN   A 59  ? 0.1559 0.2824 0.2779 -0.0287 0.0328  -0.0294 59  ASN   A CA  
920  C  C   . ASN   A 59  ? 0.1552 0.2743 0.2770 -0.0330 0.0433  -0.0249 59  ASN   A C   
921  O  O   . ASN   A 59  ? 0.1836 0.2840 0.2970 -0.0365 0.0471  -0.0201 59  ASN   A O   
922  C  CB  . ASN   A 59  ? 0.1672 0.2865 0.2908 -0.0357 0.0303  -0.0321 59  ASN   A CB  
923  C  CG  . ASN   A 59  ? 0.1995 0.3119 0.3121 -0.0293 0.0214  -0.0311 59  ASN   A CG  
924  O  OD1 . ASN   A 59  ? 0.2109 0.3239 0.3155 -0.0201 0.0172  -0.0288 59  ASN   A OD1 
925  N  ND2 . ASN   A 59  ? 0.2582 0.3622 0.3696 -0.0342 0.0196  -0.0326 59  ASN   A ND2 
932  N  N   . LYS   A 60  ? 0.1414 0.2744 0.2707 -0.0317 0.0482  -0.0257 60  LYS   A N   
933  C  CA  . LYS   A 60  ? 0.1581 0.2833 0.2834 -0.0330 0.0579  -0.0202 60  LYS   A CA  
934  C  C   . LYS   A 60  ? 0.1743 0.2817 0.2793 -0.0243 0.0557  -0.0136 60  LYS   A C   
935  O  O   . LYS   A 60  ? 0.1661 0.2735 0.2637 -0.0161 0.0483  -0.0140 60  LYS   A O   
936  C  CB  . LYS   A 60  ? 0.1751 0.3212 0.3127 -0.0320 0.0634  -0.0227 60  LYS   A CB  
937  C  CG  . LYS   A 60  ? 0.2298 0.3974 0.3896 -0.0408 0.0654  -0.0307 60  LYS   A CG  
938  C  CD  . LYS   A 60  ? 0.2792 0.4673 0.4522 -0.0412 0.0729  -0.0326 60  LYS   A CD  
939  C  CE  . LYS   A 60  ? 0.3818 0.5891 0.5788 -0.0537 0.0778  -0.0407 60  LYS   A CE  
940  N  NZ  . LYS   A 60  ? 0.5900 0.7888 0.7912 -0.0635 0.0754  -0.0447 60  LYS   A NZ  
954  N  N   . PRO   A 61  ? 0.1697 0.2615 0.2651 -0.0259 0.0623  -0.0074 61  PRO   A N   
955  C  CA  . PRO   A 61  ? 0.1681 0.2451 0.2446 -0.0181 0.0600  -0.0022 61  PRO   A CA  
956  C  C   . PRO   A 61  ? 0.1617 0.2464 0.2343 -0.0095 0.0598  -0.0026 61  PRO   A C   
957  O  O   . PRO   A 61  ? 0.1757 0.2746 0.2577 -0.0096 0.0655  -0.0041 61  PRO   A O   
958  C  CB  . PRO   A 61  ? 0.2007 0.2642 0.2703 -0.0216 0.0689  0.0041  61  PRO   A CB  
959  C  CG  . PRO   A 61  ? 0.2336 0.3077 0.3183 -0.0291 0.0781  0.0028  61  PRO   A CG  
960  C  CD  . PRO   A 61  ? 0.1968 0.2844 0.2979 -0.0345 0.0729  -0.0049 61  PRO   A CD  
968  N  N   . MET   A 62  ? 0.1649 0.2396 0.2235 -0.0021 0.0539  -0.0015 62  MET   A N   
969  C  CA  . MET   A 62  ? 0.1546 0.2323 0.2065 0.0066  0.0542  -0.0018 62  MET   A CA  
970  C  C   . MET   A 62  ? 0.2054 0.2833 0.2542 0.0062  0.0642  0.0019  62  MET   A C   
971  O  O   . MET   A 62  ? 0.1775 0.2439 0.2184 0.0034  0.0681  0.0065  62  MET   A O   
972  C  CB  . MET   A 62  ? 0.1646 0.2258 0.1995 0.0120  0.0484  -0.0005 62  MET   A CB  
973  C  CG  . MET   A 62  ? 0.1753 0.2363 0.2016 0.0205  0.0490  -0.0016 62  MET   A CG  
974  S  SD  . MET   A 62  ? 0.2079 0.2521 0.2194 0.0251  0.0408  -0.0029 62  MET   A SD  
975  C  CE  . MET   A 62  ? 0.2703 0.3134 0.2720 0.0342  0.0431  -0.0051 62  MET   A CE  
985  N  N   . GLN   A 63  ? 0.1676 0.2581 0.2210 0.0102  0.0684  0.0005  63  GLN   A N   
986  C  CA  . GLN   A 63  ? 0.1776 0.2711 0.2296 0.0100  0.0789  0.0039  63  GLN   A CA  
987  C  C   . GLN   A 63  ? 0.1947 0.2906 0.2375 0.0202  0.0795  0.0029  63  GLN   A C   
988  O  O   . GLN   A 63  ? 0.2167 0.3200 0.2628 0.0259  0.0746  -0.0014 63  GLN   A O   
989  C  CB  . GLN   A 63  ? 0.2365 0.3472 0.3087 0.0023  0.0864  0.0024  63  GLN   A CB  
990  C  CG  . GLN   A 63  ? 0.2778 0.4096 0.3641 0.0055  0.0839  -0.0035 63  GLN   A CG  
991  C  CD  . GLN   A 63  ? 0.3575 0.5082 0.4643 -0.0028 0.0921  -0.0057 63  GLN   A CD  
992  O  OE1 . GLN   A 63  ? 0.3224 0.4705 0.4374 -0.0131 0.0952  -0.0054 63  GLN   A OE1 
993  N  NE2 . GLN   A 63  ? 0.4493 0.6189 0.5648 0.0016  0.0960  -0.0082 63  GLN   A NE2 
1002 N  N   . PHE   A 64  ? 0.1970 0.2865 0.2276 0.0230  0.0859  0.0070  64  PHE   A N   
1003 C  CA  . PHE   A 64  ? 0.2377 0.3272 0.2568 0.0329  0.0863  0.0055  64  PHE   A CA  
1004 C  C   . PHE   A 64  ? 0.2398 0.3319 0.2534 0.0343  0.0974  0.0099  64  PHE   A C   
1005 O  O   . PHE   A 64  ? 0.2626 0.3487 0.2737 0.0291  0.1031  0.0154  64  PHE   A O   
1006 C  CB  . PHE   A 64  ? 0.2406 0.3137 0.2429 0.0377  0.0778  0.0040  64  PHE   A CB  
1007 C  CG  . PHE   A 64  ? 0.2267 0.2862 0.2174 0.0347  0.0774  0.0083  64  PHE   A CG  
1008 C  CD1 . PHE   A 64  ? 0.2322 0.2863 0.2283 0.0274  0.0742  0.0102  64  PHE   A CD1 
1009 C  CD2 . PHE   A 64  ? 0.2693 0.3218 0.2428 0.0401  0.0798  0.0103  64  PHE   A CD2 
1010 C  CE1 . PHE   A 64  ? 0.2735 0.3156 0.2587 0.0259  0.0737  0.0143  64  PHE   A CE1 
1011 C  CE2 . PHE   A 64  ? 0.2980 0.3400 0.2608 0.0387  0.0790  0.0143  64  PHE   A CE2 
1012 C  CZ  . PHE   A 64  ? 0.2918 0.3285 0.2608 0.0317  0.0760  0.0165  64  PHE   A CZ  
1022 N  N   . THR   A 65  ? 0.2453 0.3455 0.2562 0.0419  0.1008  0.0078  65  THR   A N   
1023 C  CA  . THR   A 65  ? 0.2636 0.3664 0.2670 0.0448  0.1117  0.0120  65  THR   A CA  
1024 C  C   . THR   A 65  ? 0.2890 0.3754 0.2708 0.0481  0.1107  0.0156  65  THR   A C   
1025 O  O   . THR   A 65  ? 0.3061 0.3823 0.2759 0.0526  0.1019  0.0121  65  THR   A O   
1026 C  CB  . THR   A 65  ? 0.2532 0.3665 0.2555 0.0540  0.1137  0.0079  65  THR   A CB  
1027 O  OG1 . THR   A 65  ? 0.3066 0.4387 0.3301 0.0515  0.1158  0.0052  65  THR   A OG1 
1028 C  CG2 . THR   A 65  ? 0.3489 0.4639 0.3397 0.0589  0.1245  0.0119  65  THR   A CG2 
1036 N  N   . CYS   A 66  ? 0.3434 0.4273 0.3202 0.0458  0.1202  0.0227  66  CYS   A N   
1037 C  CA  . CYS   A 66  ? 0.3167 0.3873 0.2721 0.0505  0.1196  0.0266  66  CYS   A CA  
1038 C  C   . CYS   A 66  ? 0.4540 0.5285 0.4015 0.0541  0.1327  0.0329  66  CYS   A C   
1039 O  O   . CYS   A 66  ? 0.3913 0.4689 0.3489 0.0475  0.1429  0.0389  66  CYS   A O   
1040 C  CB  . CYS   A 66  ? 0.3509 0.4091 0.3033 0.0451  0.1161  0.0308  66  CYS   A CB  
1041 S  SG  . CYS   A 66  ? 0.4031 0.4611 0.3719 0.0335  0.1247  0.0371  66  CYS   A SG  
1046 N  N   . LYS   A 67  ? 0.4328 0.5069 0.3629 0.0642  0.1328  0.0312  67  LYS   A N   
1047 C  CA  . LYS   A 67  ? 0.5277 0.6069 0.4480 0.0699  0.1447  0.0361  67  LYS   A CA  
1048 C  C   . LYS   A 67  ? 0.3731 0.4422 0.2690 0.0777  0.1402  0.0370  67  LYS   A C   
1049 O  O   . LYS   A 67  ? 0.3981 0.4608 0.2837 0.0814  0.1305  0.0322  67  LYS   A O   
1050 C  CB  . LYS   A 67  ? 7.0754 7.1674 7.0016 0.0746  0.1462  0.0300  67  LYS   A CB  
1051 C  CG  . LYS   A 67  ? 0.6379 0.7440 0.5893 0.0673  0.1514  0.0293  67  LYS   A CG  
1052 C  CD  . LYS   A 67  ? 0.6405 0.7602 0.5978 0.0715  0.1555  0.0255  67  LYS   A CD  
1053 C  CE  . LYS   A 67  ? 0.6130 0.7360 0.5689 0.0797  0.1474  0.0167  67  LYS   A CE  
1054 N  NZ  . LYS   A 67  ? 0.6871 0.8253 0.6536 0.0829  0.1514  0.0129  67  LYS   A NZ  
1068 N  N   . GLU   A 68  ? 0.3712 0.4392 0.2592 0.0794  0.1471  0.0432  68  GLU   A N   
1069 C  CA  . GLU   A 68  ? 0.4509 0.5129 0.3165 0.0880  0.1434  0.0438  68  GLU   A CA  
1070 C  C   . GLU   A 68  ? 0.3935 0.4605 0.2509 0.0961  0.1377  0.0340  68  GLU   A C   
1071 O  O   . GLU   A 68  ? 0.3883 0.4642 0.2554 0.0965  0.1410  0.0300  68  GLU   A O   
1072 C  CB  . GLU   A 68  ? 0.4636 0.5253 0.3241 0.0890  0.1535  0.0524  68  GLU   A CB  
1073 C  CG  . GLU   A 68  ? 0.5519 0.6058 0.4184 0.0817  0.1602  0.0624  68  GLU   A CG  
1074 C  CD  . GLU   A 68  ? 0.5604 0.6023 0.4112 0.0857  0.1547  0.0667  68  GLU   A CD  
1075 O  OE1 . GLU   A 68  ? 0.5898 0.6288 0.4237 0.0937  0.1553  0.0705  68  GLU   A OE1 
1076 O  OE2 . GLU   A 68  ? 0.6403 0.6767 0.4963 0.0811  0.1495  0.0661  68  GLU   A OE2 
1083 N  N   . THR   A 69  ? 0.3718 0.4334 0.2110 0.1028  0.1295  0.0302  69  THR   A N   
1084 C  CA  . THR   A 69  ? 0.3849 0.4485 0.2146 0.1099  0.1229  0.0198  69  THR   A CA  
1085 C  C   . THR   A 69  ? 0.4431 0.5050 0.2530 0.1173  0.1204  0.0202  69  THR   A C   
1086 O  O   . THR   A 69  ? 0.4841 0.5421 0.2869 0.1176  0.1218  0.0281  69  THR   A O   
1087 C  CB  . THR   A 69  ? 0.4794 0.5385 0.3106 0.1089  0.1123  0.0106  69  THR   A CB  
1088 O  OG1 . THR   A 69  ? 0.5138 0.5661 0.3350 0.1086  0.1053  0.0119  69  THR   A OG1 
1089 C  CG2 . THR   A 69  ? 0.5073 0.5686 0.3581 0.1023  0.1144  0.0109  69  THR   A CG2 
1097 N  N   . PRO   A 70  ? 0.4552 0.5199 0.2561 0.1238  0.1170  0.0118  70  PRO   A N   
1098 C  CA  . PRO   A 70  ? 0.5070 0.5717 0.2892 0.1313  0.1140  0.0110  70  PRO   A CA  
1099 C  C   . PRO   A 70  ? 0.5560 0.6160 0.3295 0.1317  0.1036  0.0085  70  PRO   A C   
1100 O  O   . PRO   A 70  ? 0.6370 0.6934 0.4156 0.1278  0.0960  0.0018  70  PRO   A O   
1101 C  CB  . PRO   A 70  ? 0.5516 0.6197 0.3293 0.1366  0.1116  0.0002  70  PRO   A CB  
1102 C  CG  . PRO   A 70  ? 0.5677 0.6394 0.3621 0.1330  0.1184  0.0003  70  PRO   A CG  
1103 C  CD  . PRO   A 70  ? 0.4936 0.5619 0.3012 0.1253  0.1167  0.0030  70  PRO   A CD  
1111 N  N   . ASP   A 71  ? 0.7187 0.7792 0.4792 0.1368  0.1035  0.0140  71  ASP   A N   
1112 C  CA  . ASP   A 71  ? 0.7238 0.7821 0.4770 0.1377  0.0938  0.0125  71  ASP   A CA  
1113 C  C   . ASP   A 71  ? 0.6524 0.7148 0.3937 0.1432  0.0835  0.0001  71  ASP   A C   
1114 O  O   . ASP   A 71  ? 0.6978 0.7632 0.4356 0.1464  0.0839  -0.0074 71  ASP   A O   
1115 C  CB  . ASP   A 71  ? 0.6414 0.6977 0.3886 0.1404  0.0990  0.0258  71  ASP   A CB  
1116 C  CG  . ASP   A 71  ? 0.5803 0.6412 0.3134 0.1496  0.1030  0.0291  71  ASP   A CG  
1117 O  OD1 . ASP   A 71  ? 0.7482 0.8144 0.4757 0.1537  0.1010  0.0205  71  ASP   A OD1 
1118 O  OD2 . ASP   A 71  ? 0.6044 0.6631 0.3319 0.1532  0.1087  0.0404  71  ASP   A OD2 
1123 N  N   . THR   A 75  ? 0.6458 0.6019 0.4798 0.0795  0.1361  0.1039  75  THR   A N   
1124 C  CA  . THR   A 75  ? 0.6463 0.6105 0.4940 0.0706  0.1348  0.0965  75  THR   A CA  
1125 C  C   . THR   A 75  ? 0.6585 0.6363 0.4980 0.0767  0.1296  0.0898  75  THR   A C   
1126 O  O   . THR   A 75  ? 0.6814 0.6629 0.5049 0.0869  0.1240  0.0889  75  THR   A O   
1127 C  CB  . THR   A 75  ? 0.8862 0.8488 0.7423 0.0648  0.1270  0.0919  75  THR   A CB  
1128 O  OG1 . THR   A 75  ? 0.9478 0.9131 0.7903 0.0732  0.1158  0.0891  75  THR   A OG1 
1129 C  CG2 . THR   A 75  ? 0.7938 0.7432 0.6612 0.0570  0.1324  0.0967  75  THR   A CG2 
1136 N  N   . LYS   A 76  ? 0.4737 0.4593 0.3251 0.0704  0.1315  0.0843  76  LYS   A N   
1137 C  CA  . LYS   A 76  ? 0.4411 0.4388 0.2872 0.0753  0.1273  0.0766  76  LYS   A CA  
1138 C  C   . LYS   A 76  ? 0.4447 0.4464 0.2954 0.0728  0.1179  0.0679  76  LYS   A C   
1139 O  O   . LYS   A 76  ? 0.3995 0.3968 0.2645 0.0643  0.1151  0.0669  76  LYS   A O   
1140 C  CB  . LYS   A 76  ? 0.4551 0.4593 0.3120 0.0711  0.1369  0.0765  76  LYS   A CB  
1141 C  CG  . LYS   A 76  ? 0.4503 0.4496 0.3033 0.0726  0.1471  0.0854  76  LYS   A CG  
1142 C  CD  . LYS   A 76  ? 0.4174 0.4266 0.2723 0.0739  0.1537  0.0838  76  LYS   A CD  
1143 C  CE  . LYS   A 76  ? 0.4735 0.4775 0.3202 0.0776  0.1631  0.0927  76  LYS   A CE  
1144 N  NZ  . LYS   A 76  ? 0.4181 0.4317 0.2703 0.0765  0.1705  0.0915  76  LYS   A NZ  
1158 N  N   . THR   A 77  ? 0.3997 0.4091 0.2411 0.0791  0.1104  0.0596  77  THR   A N   
1159 C  CA  . THR   A 77  ? 0.3837 0.3959 0.2337 0.0754  0.0970  0.0482  77  THR   A CA  
1160 C  C   . THR   A 77  ? 0.4021 0.4220 0.2609 0.0741  0.0973  0.0407  77  THR   A C   
1161 O  O   . THR   A 77  ? 0.4560 0.4814 0.3060 0.0803  0.1031  0.0406  77  THR   A O   
1162 C  CB  . THR   A 77  ? 0.4176 0.4313 0.2509 0.0832  0.0864  0.0427  77  THR   A CB  
1163 O  OG1 . THR   A 77  ? 0.4885 0.4967 0.3135 0.0858  0.0853  0.0495  77  THR   A OG1 
1164 C  CG2 . THR   A 77  ? 0.4431 0.4583 0.2850 0.0789  0.0739  0.0310  77  THR   A CG2 
1172 N  N   . TYR   A 78  ? 0.3581 0.3783 0.2332 0.0668  0.0907  0.0343  78  TYR   A N   
1173 C  CA  . TYR   A 78  ? 0.3141 0.3411 0.1986 0.0661  0.0904  0.0274  78  TYR   A CA  
1174 C  C   . TYR   A 78  ? 0.3186 0.3431 0.2072 0.0643  0.0780  0.0179  78  TYR   A C   
1175 O  O   . TYR   A 78  ? 0.3261 0.3452 0.2188 0.0596  0.0713  0.0176  78  TYR   A O   
1176 C  CB  . TYR   A 78  ? 0.3210 0.3527 0.2252 0.0586  0.0980  0.0305  78  TYR   A CB  
1177 C  CG  . TYR   A 78  ? 0.3396 0.3720 0.2423 0.0582  0.1116  0.0404  78  TYR   A CG  
1178 C  CD1 . TYR   A 78  ? 0.3758 0.3999 0.2791 0.0538  0.1152  0.0481  78  TYR   A CD1 
1179 C  CD2 . TYR   A 78  ? 0.3488 0.3893 0.2491 0.0624  0.1215  0.0422  78  TYR   A CD2 
1180 C  CE1 . TYR   A 78  ? 0.4252 0.4473 0.3264 0.0533  0.1290  0.0577  78  TYR   A CE1 
1181 C  CE2 . TYR   A 78  ? 0.3587 0.3989 0.2571 0.0618  0.1354  0.0519  78  TYR   A CE2 
1182 C  CZ  . TYR   A 78  ? 0.3997 0.4299 0.2989 0.0569  0.1392  0.0596  78  TYR   A CZ  
1183 O  OH  . TYR   A 78  ? 0.4366 0.4627 0.3369 0.0541  0.1495  0.0679  78  TYR   A OH  
1193 N  N   . TYR   A 79  ? 0.3061 0.3341 0.1941 0.0680  0.0761  0.0104  79  TYR   A N   
1194 C  CA  . TYR   A 79  ? 0.2840 0.3080 0.1778 0.0656  0.0663  0.0021  79  TYR   A CA  
1195 C  C   . TYR   A 79  ? 0.2776 0.3033 0.1907 0.0588  0.0661  0.0028  79  TYR   A C   
1196 O  O   . TYR   A 79  ? 0.2790 0.3121 0.2016 0.0579  0.0732  0.0056  79  TYR   A O   
1197 C  CB  . TYR   A 79  ? 0.3201 0.3450 0.2071 0.0719  0.0648  -0.0064 79  TYR   A CB  
1198 C  CG  . TYR   A 79  ? 0.3506 0.3722 0.2204 0.0769  0.0594  -0.0121 79  TYR   A CG  
1199 C  CD1 . TYR   A 79  ? 0.4662 0.4923 0.3204 0.0840  0.0643  -0.0102 79  TYR   A CD1 
1200 C  CD2 . TYR   A 79  ? 0.3994 0.4145 0.2683 0.0744  0.0499  -0.0195 79  TYR   A CD2 
1201 C  CE1 . TYR   A 79  ? 0.5407 0.5663 0.3789 0.0890  0.0588  -0.0162 79  TYR   A CE1 
1202 C  CE2 . TYR   A 79  ? 0.4940 0.5083 0.3486 0.0782  0.0448  -0.0260 79  TYR   A CE2 
1203 C  CZ  . TYR   A 79  ? 0.5568 0.5771 0.3958 0.0857  0.0488  -0.0246 79  TYR   A CZ  
1204 O  OH  . TYR   A 79  ? 0.6184 0.6405 0.4427 0.0901  0.0432  -0.0320 79  TYR   A OH  
1214 N  N   . THR   A 80  ? 0.2492 0.2691 0.1679 0.0543  0.0580  -0.0001 80  THR   A N   
1215 C  CA  . THR   A 80  ? 0.2352 0.2571 0.1708 0.0485  0.0569  0.0004  80  THR   A CA  
1216 C  C   . THR   A 80  ? 0.2262 0.2508 0.1673 0.0519  0.0557  -0.0052 80  THR   A C   
1217 O  O   . THR   A 80  ? 0.2499 0.2725 0.1820 0.0580  0.0552  -0.0102 80  THR   A O   
1218 C  CB  . THR   A 80  ? 0.2561 0.2707 0.1945 0.0432  0.0491  -0.0001 80  THR   A CB  
1219 O  OG1 . THR   A 80  ? 0.2689 0.2769 0.1998 0.0457  0.0421  -0.0067 80  THR   A OG1 
1220 C  CG2 . THR   A 80  ? 0.2851 0.2968 0.2182 0.0410  0.0504  0.0058  80  THR   A CG2 
1228 N  N   . GLY   A 81  ? 0.2303 0.2598 0.1862 0.0482  0.0552  -0.0045 81  GLY   A N   
1229 C  CA  . GLY   A 81  ? 0.2312 0.2630 0.1927 0.0521  0.0533  -0.0090 81  GLY   A CA  
1230 C  C   . GLY   A 81  ? 0.2244 0.2696 0.1932 0.0557  0.0605  -0.0084 81  GLY   A C   
1231 O  O   . GLY   A 81  ? 0.2325 0.2836 0.1984 0.0568  0.0676  -0.0056 81  GLY   A O   
1235 N  N   . TYR   A 82  ? 0.2347 0.2854 0.2128 0.0585  0.0588  -0.0109 82  TYR   A N   
1236 C  CA  . TYR   A 82  ? 0.2206 0.2867 0.2074 0.0626  0.0651  -0.0110 82  TYR   A CA  
1237 C  C   . TYR   A 82  ? 0.2827 0.3484 0.2586 0.0711  0.0697  -0.0136 82  TYR   A C   
1238 O  O   . TYR   A 82  ? 0.2729 0.3524 0.2550 0.0743  0.0765  -0.0129 82  TYR   A O   
1239 C  CB  . TYR   A 82  ? 0.2289 0.3015 0.2268 0.0656  0.0612  -0.0134 82  TYR   A CB  
1240 C  CG  . TYR   A 82  ? 0.2053 0.2822 0.2153 0.0579  0.0571  -0.0117 82  TYR   A CG  
1241 C  CD1 . TYR   A 82  ? 0.2056 0.2921 0.2260 0.0495  0.0610  -0.0087 82  TYR   A CD1 
1242 C  CD2 . TYR   A 82  ? 0.2217 0.2916 0.2320 0.0588  0.0498  -0.0130 82  TYR   A CD2 
1243 C  CE1 . TYR   A 82  ? 0.1955 0.2852 0.2263 0.0425  0.0572  -0.0082 82  TYR   A CE1 
1244 C  CE2 . TYR   A 82  ? 0.2210 0.2949 0.2410 0.0523  0.0460  -0.0118 82  TYR   A CE2 
1245 C  CZ  . TYR   A 82  ? 0.1927 0.2771 0.2230 0.0444  0.0495  -0.0100 82  TYR   A CZ  
1246 O  OH  . TYR   A 82  ? 0.2095 0.2976 0.2493 0.0377  0.0458  -0.0098 82  TYR   A OH  
1256 N  N   . SER   A 83  ? 0.2629 0.3142 0.2234 0.0748  0.0663  -0.0171 83  SER   A N   
1257 C  CA  . SER   A 83  ? 0.2884 0.3378 0.2361 0.0828  0.0702  -0.0206 83  SER   A CA  
1258 C  C   . SER   A 83  ? 0.2922 0.3371 0.2263 0.0814  0.0720  -0.0191 83  SER   A C   
1259 O  O   . SER   A 83  ? 0.3300 0.3719 0.2509 0.0878  0.0738  -0.0230 83  SER   A O   
1260 C  CB  . SER   A 83  ? 0.3465 0.3826 0.2866 0.0885  0.0651  -0.0273 83  SER   A CB  
1261 O  OG  . SER   A 83  ? 0.4322 0.4723 0.3823 0.0929  0.0647  -0.0282 83  SER   A OG  
1267 N  N   . ALA   A 84  ? 0.2841 0.3283 0.2200 0.0740  0.0712  -0.0139 84  ALA   A N   
1268 C  CA  . ALA   A 84  ? 0.3013 0.3432 0.2243 0.0740  0.0738  -0.0109 84  ALA   A CA  
1269 C  C   . ALA   A 84  ? 0.3023 0.3337 0.2088 0.0782  0.0680  -0.0175 84  ALA   A C   
1270 O  O   . ALA   A 84  ? 0.3130 0.3451 0.2053 0.0834  0.0708  -0.0185 84  ALA   A O   
1271 C  CB  . ALA   A 84  ? 0.3513 0.4040 0.2726 0.0775  0.0845  -0.0066 84  ALA   A CB  
1277 N  N   . ASP   A 85  ? 0.2772 0.2992 0.1856 0.0757  0.0599  -0.0223 85  ASP   A N   
1278 C  CA  . ASP   A 85  ? 0.2796 0.2913 0.1752 0.0779  0.0539  -0.0302 85  ASP   A CA  
1279 C  C   . ASP   A 85  ? 0.2757 0.2800 0.1718 0.0711  0.0463  -0.0306 85  ASP   A C   
1280 O  O   . ASP   A 85  ? 0.2996 0.2966 0.1877 0.0713  0.0410  -0.0377 85  ASP   A O   
1281 C  CB  . ASP   A 85  ? 0.3090 0.3143 0.2050 0.0826  0.0530  -0.0376 85  ASP   A CB  
1282 C  CG  . ASP   A 85  ? 0.3472 0.3481 0.2566 0.0792  0.0498  -0.0367 85  ASP   A CG  
1283 O  OD1 . ASP   A 85  ? 0.3129 0.3171 0.2319 0.0729  0.0482  -0.0309 85  ASP   A OD1 
1284 O  OD2 . ASP   A 85  ? 0.3914 0.3859 0.3012 0.0838  0.0497  -0.0414 85  ASP   A OD2 
1289 N  N   . GLY   A 86  ? 0.2520 0.2588 0.1580 0.0650  0.0458  -0.0237 86  GLY   A N   
1290 C  CA  . GLY   A 86  ? 0.2578 0.2592 0.1651 0.0590  0.0394  -0.0232 86  GLY   A CA  
1291 C  C   . GLY   A 86  ? 0.2352 0.2297 0.1523 0.0548  0.0344  -0.0256 86  GLY   A C   
1292 O  O   . GLY   A 86  ? 0.2344 0.2248 0.1537 0.0496  0.0294  -0.0251 86  GLY   A O   
1296 N  N   . TYR   A 87  ? 0.2468 0.2402 0.1691 0.0579  0.0362  -0.0278 87  TYR   A N   
1297 C  CA  . TYR   A 87  ? 0.2314 0.2166 0.1603 0.0560  0.0321  -0.0300 87  TYR   A CA  
1298 C  C   . TYR   A 87  ? 0.2341 0.2262 0.1763 0.0551  0.0338  -0.0248 87  TYR   A C   
1299 O  O   . TYR   A 87  ? 0.2525 0.2558 0.1999 0.0570  0.0388  -0.0215 87  TYR   A O   
1300 C  CB  . TYR   A 87  ? 0.2474 0.2229 0.1701 0.0614  0.0321  -0.0375 87  TYR   A CB  
1301 C  CG  . TYR   A 87  ? 0.2547 0.2218 0.1665 0.0601  0.0287  -0.0448 87  TYR   A CG  
1302 C  CD1 . TYR   A 87  ? 0.2736 0.2320 0.1870 0.0541  0.0235  -0.0473 87  TYR   A CD1 
1303 C  CD2 . TYR   A 87  ? 0.2907 0.2607 0.1912 0.0647  0.0307  -0.0493 87  TYR   A CD2 
1304 C  CE1 . TYR   A 87  ? 0.2965 0.2498 0.2017 0.0519  0.0199  -0.0551 87  TYR   A CE1 
1305 C  CE2 . TYR   A 87  ? 0.3359 0.3007 0.2268 0.0633  0.0267  -0.0574 87  TYR   A CE2 
1306 C  CZ  . TYR   A 87  ? 0.3452 0.3023 0.2393 0.0566  0.0212  -0.0604 87  TYR   A CZ  
1307 O  OH  . TYR   A 87  ? 0.3474 0.3020 0.2336 0.0545  0.0170  -0.0693 87  TYR   A OH  
1317 N  N   . ASP   A 88  ? 0.2223 0.2085 0.1703 0.0521  0.0297  -0.0245 88  ASP   A N   
1318 C  CA  . ASP   A 88  ? 0.2130 0.2053 0.1724 0.0527  0.0299  -0.0213 88  ASP   A CA  
1319 C  C   . ASP   A 88  ? 0.2078 0.1876 0.1665 0.0532  0.0260  -0.0233 88  ASP   A C   
1320 O  O   . ASP   A 88  ? 0.2085 0.1866 0.1719 0.0485  0.0226  -0.0208 88  ASP   A O   
1321 C  CB  . ASP   A 88  ? 0.2283 0.2289 0.1960 0.0460  0.0294  -0.0162 88  ASP   A CB  
1322 C  CG  . ASP   A 88  ? 0.2234 0.2333 0.2038 0.0459  0.0290  -0.0138 88  ASP   A CG  
1323 O  OD1 . ASP   A 88  ? 0.2847 0.2981 0.2678 0.0524  0.0301  -0.0152 88  ASP   A OD1 
1324 O  OD2 . ASP   A 88  ? 0.2314 0.2433 0.2179 0.0400  0.0265  -0.0113 88  ASP   A OD2 
1329 N  N   . ARG   A 89  ? 0.2358 0.2054 0.1875 0.0587  0.0271  -0.0279 89  ARG   A N   
1330 C  CA  . ARG   A 89  ? 0.2271 0.1804 0.1754 0.0580  0.0246  -0.0305 89  ARG   A CA  
1331 C  C   . ARG   A 89  ? 0.2391 0.1923 0.1944 0.0605  0.0238  -0.0263 89  ARG   A C   
1332 O  O   . ARG   A 89  ? 0.2604 0.2236 0.2206 0.0668  0.0260  -0.0240 89  ARG   A O   
1333 C  CB  . ARG   A 89  ? 0.2521 0.1932 0.1914 0.0635  0.0270  -0.0368 89  ARG   A CB  
1334 C  CG  . ARG   A 89  ? 0.2841 0.2221 0.2144 0.0603  0.0263  -0.0431 89  ARG   A CG  
1335 C  CD  . ARG   A 89  ? 0.3246 0.2498 0.2463 0.0655  0.0288  -0.0506 89  ARG   A CD  
1336 N  NE  . ARG   A 89  ? 0.3356 0.2595 0.2483 0.0631  0.0275  -0.0581 89  ARG   A NE  
1337 C  CZ  . ARG   A 89  ? 0.3565 0.2876 0.2626 0.0679  0.0300  -0.0607 89  ARG   A CZ  
1338 N  NH1 . ARG   A 89  ? 0.3685 0.3110 0.2774 0.0739  0.0341  -0.0558 89  ARG   A NH1 
1339 N  NH2 . ARG   A 89  ? 0.3667 0.2953 0.2634 0.0665  0.0284  -0.0687 89  ARG   A NH2 
1353 N  N   . ASP   A 90  ? 0.2357 0.1789 0.1911 0.0561  0.0209  -0.0253 90  ASP   A N   
1354 C  CA  . ASP   A 90  ? 0.2212 0.1619 0.1803 0.0599  0.0204  -0.0213 90  ASP   A CA  
1355 C  C   . ASP   A 90  ? 0.2293 0.1529 0.1847 0.0557  0.0192  -0.0219 90  ASP   A C   
1356 O  O   . ASP   A 90  ? 0.2205 0.1435 0.1767 0.0473  0.0165  -0.0226 90  ASP   A O   
1357 C  CB  . ASP   A 90  ? 0.2353 0.1929 0.2039 0.0577  0.0183  -0.0166 90  ASP   A CB  
1358 C  CG  . ASP   A 90  ? 0.3103 0.2709 0.2825 0.0647  0.0179  -0.0130 90  ASP   A CG  
1359 O  OD1 . ASP   A 90  ? 0.3260 0.2744 0.2950 0.0651  0.0170  -0.0112 90  ASP   A OD1 
1360 O  OD2 . ASP   A 90  ? 0.3987 0.3763 0.3779 0.0691  0.0185  -0.0119 90  ASP   A OD2 
1365 N  N   . ASN   A 91  ? 0.2437 0.1531 0.1950 0.0617  0.0217  -0.0216 91  ASN   A N   
1366 C  CA  . ASN   A 91  ? 0.2473 0.1401 0.1961 0.0583  0.0219  -0.0206 91  ASN   A CA  
1367 C  C   . ASN   A 91  ? 0.2487 0.1333 0.1955 0.0482  0.0207  -0.0261 91  ASN   A C   
1368 O  O   . ASN   A 91  ? 0.2622 0.1431 0.2111 0.0416  0.0191  -0.0247 91  ASN   A O   
1369 C  CB  . ASN   A 91  ? 0.2518 0.1512 0.2056 0.0579  0.0196  -0.0139 91  ASN   A CB  
1370 C  CG  . ASN   A 91  ? 0.2563 0.1377 0.2065 0.0567  0.0214  -0.0117 91  ASN   A CG  
1371 O  OD1 . ASN   A 91  ? 0.3039 0.1669 0.2480 0.0598  0.0257  -0.0134 91  ASN   A OD1 
1372 N  ND2 . ASN   A 91  ? 0.2660 0.1517 0.2197 0.0520  0.0189  -0.0077 91  ASN   A ND2 
1379 N  N   . GLY   A 92  ? 0.2553 0.1384 0.1977 0.0477  0.0215  -0.0328 92  GLY   A N   
1380 C  CA  . GLY   A 92  ? 0.2684 0.1447 0.2085 0.0392  0.0201  -0.0396 92  GLY   A CA  
1381 C  C   . GLY   A 92  ? 0.2489 0.1407 0.1918 0.0328  0.0156  -0.0402 92  GLY   A C   
1382 O  O   . GLY   A 92  ? 0.2668 0.1563 0.2080 0.0265  0.0137  -0.0462 92  GLY   A O   
1386 N  N   . ALA   A 93  ? 0.2353 0.1427 0.1823 0.0346  0.0142  -0.0346 93  ALA   A N   
1387 C  CA  . ALA   A 93  ? 0.2279 0.1492 0.1763 0.0304  0.0113  -0.0342 93  ALA   A CA  
1388 C  C   . ALA   A 93  ? 0.2236 0.1539 0.1683 0.0351  0.0131  -0.0355 93  ALA   A C   
1389 O  O   . ALA   A 93  ? 0.2384 0.1705 0.1833 0.0419  0.0163  -0.0342 93  ALA   A O   
1390 C  CB  . ALA   A 93  ? 0.2314 0.1626 0.1872 0.0283  0.0095  -0.0271 93  ALA   A CB  
1396 N  N   . ALA   A 94  ? 0.2370 0.1731 0.1776 0.0325  0.0114  -0.0384 94  ALA   A N   
1397 C  CA  . ALA   A 94  ? 0.2310 0.1755 0.1664 0.0371  0.0138  -0.0394 94  ALA   A CA  
1398 C  C   . ALA   A 94  ? 0.2167 0.1737 0.1577 0.0390  0.0162  -0.0321 94  ALA   A C   
1399 O  O   . ALA   A 94  ? 0.2258 0.1879 0.1656 0.0446  0.0201  -0.0319 94  ALA   A O   
1400 C  CB  . ALA   A 94  ? 0.2434 0.1917 0.1719 0.0346  0.0112  -0.0435 94  ALA   A CB  
1406 N  N   . SER   A 95  ? 0.2021 0.1642 0.1494 0.0342  0.0142  -0.0270 95  SER   A N   
1407 C  CA  . SER   A 95  ? 0.2099 0.1835 0.1634 0.0344  0.0168  -0.0210 95  SER   A CA  
1408 C  C   . SER   A 95  ? 0.1991 0.1742 0.1598 0.0287  0.0140  -0.0169 95  SER   A C   
1409 O  O   . SER   A 95  ? 0.1950 0.1725 0.1546 0.0251  0.0129  -0.0149 95  SER   A O   
1410 C  CB  . SER   A 95  ? 0.2127 0.1933 0.1607 0.0355  0.0197  -0.0198 95  SER   A CB  
1411 O  OG  . SER   A 95  ? 0.2172 0.2073 0.1728 0.0344  0.0232  -0.0142 95  SER   A OG  
1417 N  N   . PRO   A 96  ? 0.1786 0.1530 0.1461 0.0287  0.0130  -0.0154 96  PRO   A N   
1418 C  CA  . PRO   A 96  ? 0.1886 0.1655 0.1626 0.0238  0.0106  -0.0119 96  PRO   A CA  
1419 C  C   . PRO   A 96  ? 0.1777 0.1642 0.1564 0.0211  0.0128  -0.0083 96  PRO   A C   
1420 O  O   . PRO   A 96  ? 0.1713 0.1577 0.1523 0.0166  0.0109  -0.0062 96  PRO   A O   
1421 C  CB  . PRO   A 96  ? 0.1854 0.1618 0.1646 0.0265  0.0098  -0.0111 96  PRO   A CB  
1422 C  CG  . PRO   A 96  ? 0.2096 0.1759 0.1822 0.0314  0.0109  -0.0147 96  PRO   A CG  
1423 C  CD  . PRO   A 96  ? 0.2008 0.1708 0.1689 0.0339  0.0138  -0.0169 96  PRO   A CD  
1431 N  N   . THR   A 97  ? 0.1683 0.1628 0.1495 0.0237  0.0171  -0.0076 97  THR   A N   
1432 C  CA  . THR   A 97  ? 0.1611 0.1634 0.1472 0.0205  0.0207  -0.0042 97  THR   A CA  
1433 C  C   . THR   A 97  ? 0.1625 0.1609 0.1405 0.0191  0.0219  -0.0023 97  THR   A C   
1434 O  O   . THR   A 97  ? 0.1759 0.1746 0.1566 0.0149  0.0227  0.0011  97  THR   A O   
1435 C  CB  . THR   A 97  ? 0.1605 0.1733 0.1522 0.0234  0.0259  -0.0041 97  THR   A CB  
1436 O  OG1 . THR   A 97  ? 0.1882 0.1987 0.1716 0.0292  0.0278  -0.0064 97  THR   A OG1 
1437 C  CG2 . THR   A 97  ? 0.1841 0.2043 0.1859 0.0246  0.0241  -0.0054 97  THR   A CG2 
1445 N  N   . ASN   A 98  ? 0.1731 0.1678 0.1407 0.0228  0.0219  -0.0045 98  ASN   A N   
1446 C  CA  . ASN   A 98  ? 0.1758 0.1682 0.1346 0.0227  0.0219  -0.0028 98  ASN   A CA  
1447 C  C   . ASN   A 98  ? 0.1821 0.1698 0.1413 0.0189  0.0165  -0.0028 98  ASN   A C   
1448 O  O   . ASN   A 98  ? 0.1958 0.1835 0.1535 0.0174  0.0170  0.0010  98  ASN   A O   
1449 C  CB  . ASN   A 98  ? 0.1865 0.1771 0.1339 0.0276  0.0213  -0.0071 98  ASN   A CB  
1450 C  CG  . ASN   A 98  ? 0.2055 0.2011 0.1499 0.0321  0.0273  -0.0064 98  ASN   A CG  
1451 O  OD1 . ASN   A 98  ? 0.2148 0.2161 0.1657 0.0313  0.0327  -0.0022 98  ASN   A OD1 
1452 N  ND2 . ASN   A 98  ? 0.2124 0.2065 0.1466 0.0369  0.0268  -0.0112 98  ASN   A ND2 
1459 N  N   . ASP   A 99  ? 0.1777 0.1609 0.1383 0.0179  0.0118  -0.0068 99  ASP   A N   
1460 C  CA  . ASP   A 99  ? 0.1899 0.1695 0.1517 0.0141  0.0071  -0.0070 99  ASP   A CA  
1461 C  C   . ASP   A 99  ? 0.1906 0.1721 0.1599 0.0106  0.0077  -0.0025 99  ASP   A C   
1462 O  O   . ASP   A 99  ? 0.1954 0.1757 0.1642 0.0084  0.0055  -0.0009 99  ASP   A O   
1463 C  CB  . ASP   A 99  ? 0.2013 0.1749 0.1641 0.0132  0.0037  -0.0115 99  ASP   A CB  
1464 C  CG  . ASP   A 99  ? 0.2465 0.2168 0.2015 0.0143  0.0017  -0.0173 99  ASP   A CG  
1465 O  OD1 . ASP   A 99  ? 0.2679 0.2420 0.2170 0.0151  0.0006  -0.0178 99  ASP   A OD1 
1466 O  OD2 . ASP   A 99  ? 0.2401 0.2043 0.1944 0.0150  0.0014  -0.0215 99  ASP   A OD2 
1471 N  N   . ALA   A 100 ? 0.1800 0.1650 0.1571 0.0099  0.0101  -0.0011 100 ALA   A N   
1472 C  CA  . ALA   A 100 ? 0.1666 0.1537 0.1513 0.0059  0.0105  0.0017  100 ALA   A CA  
1473 C  C   . ALA   A 100 ? 0.1652 0.1530 0.1486 0.0048  0.0148  0.0057  100 ALA   A C   
1474 O  O   . ALA   A 100 ? 0.1735 0.1590 0.1590 0.0019  0.0143  0.0078  100 ALA   A O   
1475 C  CB  . ALA   A 100 ? 0.1872 0.1803 0.1808 0.0059  0.0116  0.0008  100 ALA   A CB  
1481 N  N   . LEU   A 101 ? 0.1681 0.1583 0.1481 0.0073  0.0197  0.0070  101 LEU   A N   
1482 C  CA  . LEU   A 101 ? 0.1831 0.1723 0.1605 0.0069  0.0254  0.0119  101 LEU   A CA  
1483 C  C   . LEU   A 101 ? 0.2127 0.1967 0.1807 0.0088  0.0226  0.0137  101 LEU   A C   
1484 O  O   . LEU   A 101 ? 0.2049 0.1853 0.1734 0.0073  0.0246  0.0177  101 LEU   A O   
1485 C  CB  . LEU   A 101 ? 0.1849 0.1777 0.1586 0.0102  0.0314  0.0132  101 LEU   A CB  
1486 C  CG  . LEU   A 101 ? 0.2168 0.2081 0.1887 0.0096  0.0395  0.0192  101 LEU   A CG  
1487 C  CD1 . LEU   A 101 ? 0.2264 0.2182 0.2110 0.0029  0.0433  0.0204  101 LEU   A CD1 
1488 C  CD2 . LEU   A 101 ? 0.2316 0.2273 0.1991 0.0135  0.0456  0.0202  101 LEU   A CD2 
1500 N  N   . TYR   A 102 ? 0.2024 0.1863 0.1629 0.0122  0.0180  0.0103  102 TYR   A N   
1501 C  CA  . TYR   A 102 ? 0.2134 0.1959 0.1657 0.0145  0.0143  0.0107  102 TYR   A CA  
1502 C  C   . TYR   A 102 ? 0.2118 0.1922 0.1698 0.0108  0.0100  0.0103  102 TYR   A C   
1503 O  O   . TYR   A 102 ? 0.2398 0.2189 0.1945 0.0121  0.0097  0.0134  102 TYR   A O   
1504 C  CB  . TYR   A 102 ? 0.2395 0.2242 0.1843 0.0178  0.0102  0.0052  102 TYR   A CB  
1505 C  CG  . TYR   A 102 ? 0.2434 0.2301 0.1810 0.0202  0.0057  0.0043  102 TYR   A CG  
1506 C  CD1 . TYR   A 102 ? 0.2963 0.2846 0.2249 0.0253  0.0082  0.0091  102 TYR   A CD1 
1507 C  CD2 . TYR   A 102 ? 0.2645 0.2520 0.2047 0.0177  -0.0005 -0.0012 102 TYR   A CD2 
1508 C  CE1 . TYR   A 102 ? 0.3149 0.3074 0.2370 0.0287  0.0037  0.0082  102 TYR   A CE1 
1509 C  CE2 . TYR   A 102 ? 0.2862 0.2784 0.2214 0.0197  -0.0048 -0.0028 102 TYR   A CE2 
1510 C  CZ  . TYR   A 102 ? 0.3243 0.3200 0.2505 0.0257  -0.0032 0.0017  102 TYR   A CZ  
1511 O  OH  . TYR   A 102 ? 0.4484 0.4510 0.3696 0.0290  -0.0079 0.0000  102 TYR   A OH  
1521 N  N   . ALA   A 103 ? 0.2017 0.1817 0.1673 0.0074  0.0070  0.0069  103 ALA   A N   
1522 C  CA  . ALA   A 103 ? 0.2104 0.1888 0.1813 0.0041  0.0033  0.0064  103 ALA   A CA  
1523 C  C   . ALA   A 103 ? 0.2299 0.2065 0.2042 0.0024  0.0065  0.0109  103 ALA   A C   
1524 O  O   . ALA   A 103 ? 0.2554 0.2305 0.2285 0.0025  0.0047  0.0122  103 ALA   A O   
1525 C  CB  . ALA   A 103 ? 0.2233 0.2013 0.2007 0.0016  0.0012  0.0033  103 ALA   A CB  
1531 N  N   . GLY   A 104 ? 0.1985 0.1754 0.1774 0.0008  0.0115  0.0126  104 GLY   A N   
1532 C  CA  . GLY   A 104 ? 0.2038 0.1775 0.1870 -0.0020 0.0154  0.0158  104 GLY   A CA  
1533 C  C   . GLY   A 104 ? 0.2151 0.1840 0.1900 0.0014  0.0185  0.0208  104 GLY   A C   
1534 O  O   . GLY   A 104 ? 0.2263 0.1905 0.2020 0.0006  0.0193  0.0230  104 GLY   A O   
1538 N  N   . TYR   A 105 ? 0.1985 0.1686 0.1646 0.0061  0.0204  0.0226  105 TYR   A N   
1539 C  CA  . TYR   A 105 ? 0.2344 0.2008 0.1904 0.0114  0.0230  0.0278  105 TYR   A CA  
1540 C  C   . TYR   A 105 ? 0.2305 0.1977 0.1834 0.0137  0.0168  0.0270  105 TYR   A C   
1541 O  O   . TYR   A 105 ? 0.2503 0.2125 0.2007 0.0157  0.0188  0.0313  105 TYR   A O   
1542 C  CB  . TYR   A 105 ? 0.2618 0.2317 0.2075 0.0170  0.0246  0.0288  105 TYR   A CB  
1543 C  CG  . TYR   A 105 ? 0.3152 0.2828 0.2485 0.0242  0.0271  0.0346  105 TYR   A CG  
1544 C  CD1 . TYR   A 105 ? 0.3940 0.3658 0.3206 0.0290  0.0206  0.0331  105 TYR   A CD1 
1545 C  CD2 . TYR   A 105 ? 0.3890 0.3504 0.3175 0.0264  0.0363  0.0417  105 TYR   A CD2 
1546 C  CE1 . TYR   A 105 ? 0.4531 0.4241 0.3672 0.0374  0.0226  0.0389  105 TYR   A CE1 
1547 C  CE2 . TYR   A 105 ? 0.4883 0.4466 0.4037 0.0346  0.0393  0.0484  105 TYR   A CE2 
1548 C  CZ  . TYR   A 105 ? 0.4779 0.4414 0.3859 0.0406  0.0320  0.0469  105 TYR   A CZ  
1549 O  OH  . TYR   A 105 ? 0.7706 0.7326 0.6647 0.0502  0.0344  0.0536  105 TYR   A OH  
1559 N  N   . VAL   A 106 ? 0.2174 0.1903 0.1714 0.0131  0.0100  0.0214  106 VAL   A N   
1560 C  CA  . VAL   A 106 ? 0.2255 0.2016 0.1772 0.0151  0.0044  0.0199  106 VAL   A CA  
1561 C  C   . VAL   A 106 ? 0.2203 0.1927 0.1792 0.0118  0.0041  0.0209  106 VAL   A C   
1562 O  O   . VAL   A 106 ? 0.2323 0.2043 0.1883 0.0151  0.0033  0.0234  106 VAL   A O   
1563 C  CB  . VAL   A 106 ? 0.2353 0.2175 0.1882 0.0136  -0.0016 0.0130  106 VAL   A CB  
1564 C  CG1 . VAL   A 106 ? 0.2696 0.2566 0.2237 0.0138  -0.0071 0.0107  106 VAL   A CG1 
1565 C  CG2 . VAL   A 106 ? 0.2435 0.2297 0.1883 0.0175  -0.0019 0.0109  106 VAL   A CG2 
1575 N  N   . ILE   A 107 ? 0.2005 0.1708 0.1681 0.0062  0.0046  0.0189  107 ILE   A N   
1576 C  CA  . ILE   A 107 ? 0.2022 0.1700 0.1760 0.0032  0.0037  0.0187  107 ILE   A CA  
1577 C  C   . ILE   A 107 ? 0.2074 0.1678 0.1800 0.0043  0.0092  0.0236  107 ILE   A C   
1578 O  O   . ILE   A 107 ? 0.2214 0.1794 0.1938 0.0057  0.0085  0.0248  107 ILE   A O   
1579 C  CB  . ILE   A 107 ? 0.2144 0.1831 0.1969 -0.0021 0.0026  0.0151  107 ILE   A CB  
1580 C  CG1 . ILE   A 107 ? 0.2589 0.2319 0.2415 -0.0025 -0.0014 0.0112  107 ILE   A CG1 
1581 C  CG2 . ILE   A 107 ? 0.2547 0.2217 0.2420 -0.0043 0.0012  0.0145  107 ILE   A CG2 
1582 C  CD1 . ILE   A 107 ? 0.4784 0.4543 0.4584 -0.0013 -0.0059 0.0093  107 ILE   A CD1 
1594 N  N   . LYS   A 108 ? 0.2335 0.1899 0.2056 0.0037  0.0154  0.0262  108 LYS   A N   
1595 C  CA  . LYS   A 108 ? 0.2417 0.1887 0.2120 0.0044  0.0224  0.0313  108 LYS   A CA  
1596 C  C   . LYS   A 108 ? 0.2411 0.1858 0.2008 0.0123  0.0223  0.0361  108 LYS   A C   
1597 O  O   . LYS   A 108 ? 0.2538 0.1913 0.2121 0.0143  0.0245  0.0390  108 LYS   A O   
1598 C  CB  . LYS   A 108 ? 0.2773 0.2218 0.2484 0.0025  0.0295  0.0334  108 LYS   A CB  
1599 C  CG  . LYS   A 108 ? 0.3951 0.3284 0.3629 0.0033  0.0389  0.0396  108 LYS   A CG  
1600 C  CD  . LYS   A 108 ? 0.4919 0.4189 0.4705 -0.0043 0.0430  0.0373  108 LYS   A CD  
1601 C  CE  . LYS   A 108 ? 0.4732 0.3856 0.4481 -0.0034 0.0531  0.0436  108 LYS   A CE  
1602 N  NZ  . LYS   A 108 ? 0.6247 0.5293 0.5887 0.0049  0.0525  0.0489  108 LYS   A NZ  
1616 N  N   . HIS   A 109 ? 0.2301 0.1809 0.1815 0.0177  0.0199  0.0369  109 HIS   A N   
1617 C  CA  . HIS   A 109 ? 0.2511 0.2023 0.1916 0.0266  0.0196  0.0414  109 HIS   A CA  
1618 C  C   . HIS   A 109 ? 0.2315 0.1884 0.1738 0.0284  0.0129  0.0388  109 HIS   A C   
1619 O  O   . HIS   A 109 ? 0.2549 0.2096 0.1907 0.0355  0.0139  0.0432  109 HIS   A O   
1620 C  CB  . HIS   A 109 ? 0.2583 0.2159 0.1889 0.0323  0.0190  0.0424  109 HIS   A CB  
1621 C  CG  . HIS   A 109 ? 0.2974 0.2474 0.2236 0.0330  0.0280  0.0478  109 HIS   A CG  
1622 N  ND1 . HIS   A 109 ? 0.4198 0.3644 0.3338 0.0413  0.0338  0.0557  109 HIS   A ND1 
1623 C  CD2 . HIS   A 109 ? 0.3541 0.3009 0.2874 0.0263  0.0329  0.0469  109 HIS   A CD2 
1624 C  CE1 . HIS   A 109 ? 0.4860 0.4239 0.3995 0.0391  0.0425  0.0595  109 HIS   A CE1 
1625 N  NE2 . HIS   A 109 ? 0.4246 0.3645 0.3507 0.0298  0.0419  0.0538  109 HIS   A NE2 
1633 N  N   . MET   A 110 ? 0.2162 0.1803 0.1663 0.0232  0.0067  0.0322  110 MET   A N   
1634 C  CA  A MET   A 110 ? 0.2061 0.1760 0.1592 0.0241  0.0014  0.0298  110 MET   A CA  
1635 C  CA  B MET   A 110 ? 0.2052 0.1750 0.1582 0.0242  0.0014  0.0298  110 MET   A CA  
1636 C  C   . MET   A 110 ? 0.2170 0.1780 0.1726 0.0242  0.0049  0.0328  110 MET   A C   
1637 O  O   . MET   A 110 ? 0.2201 0.1824 0.1722 0.0302  0.0041  0.0351  110 MET   A O   
1638 C  CB  A MET   A 110 ? 0.2264 0.2025 0.1880 0.0174  -0.0037 0.0231  110 MET   A CB  
1639 C  CB  B MET   A 110 ? 0.2250 0.2012 0.1861 0.0176  -0.0037 0.0231  110 MET   A CB  
1640 C  CG  A MET   A 110 ? 0.2249 0.2087 0.1901 0.0177  -0.0087 0.0203  110 MET   A CG  
1641 C  CG  B MET   A 110 ? 0.2246 0.2083 0.1895 0.0178  -0.0086 0.0203  110 MET   A CG  
1642 S  SD  A MET   A 110 ? 0.2194 0.1978 0.1913 0.0152  -0.0074 0.0209  110 MET   A SD  
1643 S  SD  B MET   A 110 ? 0.2359 0.2231 0.2103 0.0097  -0.0123 0.0141  110 MET   A SD  
1644 C  CE  A MET   A 110 ? 0.2797 0.2553 0.2591 0.0067  -0.0075 0.0169  110 MET   A CE  
1645 C  CE  B MET   A 110 ? 0.2864 0.2637 0.2661 0.0056  -0.0084 0.0157  110 MET   A CE  
1664 N  N   . TYR   A 111 ? 0.2103 0.1634 0.1725 0.0177  0.0085  0.0319  111 TYR   A N   
1665 C  CA  . TYR   A 111 ? 0.2116 0.1561 0.1766 0.0171  0.0117  0.0332  111 TYR   A CA  
1666 C  C   . TYR   A 111 ? 0.2334 0.1674 0.1900 0.0237  0.0182  0.0402  111 TYR   A C   
1667 O  O   . TYR   A 111 ? 0.2402 0.1690 0.1950 0.0278  0.0195  0.0422  111 TYR   A O   
1668 C  CB  . TYR   A 111 ? 0.2203 0.1601 0.1940 0.0087  0.0140  0.0297  111 TYR   A CB  
1669 C  CG  . TYR   A 111 ? 0.1944 0.1422 0.1754 0.0041  0.0081  0.0238  111 TYR   A CG  
1670 C  CD1 . TYR   A 111 ? 0.2015 0.1506 0.1846 0.0048  0.0055  0.0222  111 TYR   A CD1 
1671 C  CD2 . TYR   A 111 ? 0.1891 0.1429 0.1741 -0.0001 0.0055  0.0204  111 TYR   A CD2 
1672 C  CE1 . TYR   A 111 ? 0.2037 0.1594 0.1922 0.0011  0.0011  0.0178  111 TYR   A CE1 
1673 C  CE2 . TYR   A 111 ? 0.1800 0.1394 0.1701 -0.0032 0.0011  0.0162  111 TYR   A CE2 
1674 C  CZ  . TYR   A 111 ? 0.1932 0.1534 0.1848 -0.0027 -0.0009 0.0152  111 TYR   A CZ  
1675 O  OH  . TYR   A 111 ? 0.2151 0.1803 0.2106 -0.0052 -0.0044 0.0120  111 TYR   A OH  
1685 N  N   . HIS   A 112 ? 0.2238 0.1538 0.1747 0.0256  0.0230  0.0443  112 HIS   A N   
1686 C  CA  . HIS   A 112 ? 0.2551 0.1738 0.1965 0.0328  0.0302  0.0521  112 HIS   A CA  
1687 C  C   . HIS   A 112 ? 0.2736 0.1989 0.2049 0.0441  0.0265  0.0557  112 HIS   A C   
1688 O  O   . HIS   A 112 ? 0.2941 0.2119 0.2208 0.0506  0.0294  0.0601  112 HIS   A O   
1689 C  CB  . HIS   A 112 ? 0.2936 0.2073 0.2307 0.0322  0.0369  0.0561  112 HIS   A CB  
1690 C  CG  . HIS   A 112 ? 0.3556 0.2560 0.2816 0.0401  0.0457  0.0653  112 HIS   A CG  
1691 N  ND1 . HIS   A 112 ? 0.5141 0.4180 0.4264 0.0512  0.0457  0.0713  112 HIS   A ND1 
1692 C  CD2 . HIS   A 112 ? 0.4318 0.3145 0.3579 0.0391  0.0549  0.0696  112 HIS   A CD2 
1693 C  CE1 . HIS   A 112 ? 0.4431 0.3313 0.3466 0.0574  0.0552  0.0801  112 HIS   A CE1 
1694 N  NE2 . HIS   A 112 ? 0.4809 0.3551 0.3930 0.0497  0.0613  0.0792  112 HIS   A NE2 
1702 N  N   . ASP   A 113 ? 0.2483 0.1883 0.1765 0.0469  0.0200  0.0532  113 ASP   A N   
1703 C  CA  . ASP   A 113 ? 0.2578 0.2074 0.1767 0.0579  0.0160  0.0556  113 ASP   A CA  
1704 C  C   . ASP   A 113 ? 0.2894 0.2466 0.2133 0.0596  0.0105  0.0525  113 ASP   A C   
1705 O  O   . ASP   A 113 ? 0.3018 0.2610 0.2184 0.0698  0.0103  0.0567  113 ASP   A O   
1706 C  CB  . ASP   A 113 ? 0.2694 0.2338 0.1848 0.0591  0.0102  0.0518  113 ASP   A CB  
1707 C  CG  . ASP   A 113 ? 0.3466 0.3057 0.2533 0.0612  0.0159  0.0562  113 ASP   A CG  
1708 O  OD1 . ASP   A 113 ? 0.3842 0.3286 0.2858 0.0635  0.0249  0.0637  113 ASP   A OD1 
1709 O  OD2 . ASP   A 113 ? 0.3360 0.3056 0.2420 0.0597  0.0116  0.0514  113 ASP   A OD2 
1714 N  N   . TRP   A 114 ? 0.2387 0.2009 0.1740 0.0508  0.0061  0.0456  114 TRP   A N   
1715 C  CA  . TRP   A 114 ? 0.2315 0.2022 0.1719 0.0522  0.0012  0.0426  114 TRP   A CA  
1716 C  C   . TRP   A 114 ? 0.2648 0.2230 0.2077 0.0522  0.0059  0.0448  114 TRP   A C   
1717 O  O   . TRP   A 114 ? 0.2632 0.2264 0.2060 0.0581  0.0039  0.0452  114 TRP   A O   
1718 C  CB  . TRP   A 114 ? 0.2294 0.2108 0.1802 0.0433  -0.0048 0.0346  114 TRP   A CB  
1719 C  CG  . TRP   A 114 ? 0.2136 0.2110 0.1633 0.0443  -0.0110 0.0304  114 TRP   A CG  
1720 C  CD1 . TRP   A 114 ? 0.2635 0.2679 0.2040 0.0521  -0.0124 0.0323  114 TRP   A CD1 
1721 C  CD2 . TRP   A 114 ? 0.1995 0.2069 0.1579 0.0368  -0.0162 0.0230  114 TRP   A CD2 
1722 N  NE1 . TRP   A 114 ? 0.2343 0.2537 0.1780 0.0493  -0.0188 0.0252  114 TRP   A NE1 
1723 C  CE2 . TRP   A 114 ? 0.2244 0.2448 0.1794 0.0396  -0.0208 0.0197  114 TRP   A CE2 
1724 C  CE3 . TRP   A 114 ? 0.2223 0.2285 0.1904 0.0284  -0.0171 0.0191  114 TRP   A CE3 
1725 C  CZ2 . TRP   A 114 ? 0.2454 0.2764 0.2076 0.0331  -0.0257 0.0119  114 TRP   A CZ2 
1726 C  CZ3 . TRP   A 114 ? 0.2490 0.2652 0.2231 0.0229  -0.0215 0.0127  114 TRP   A CZ3 
1727 C  CH2 . TRP   A 114 ? 0.2556 0.2829 0.2271 0.0246  -0.0255 0.0090  114 TRP   A CH2 
1738 N  N   . TYR   A 115 ? 0.2416 0.1848 0.1873 0.0459  0.0118  0.0455  115 TYR   A N   
1739 C  CA  . TYR   A 115 ? 0.2638 0.1951 0.2133 0.0438  0.0159  0.0453  115 TYR   A CA  
1740 C  C   . TYR   A 115 ? 0.3037 0.2152 0.2486 0.0448  0.0254  0.0506  115 TYR   A C   
1741 O  O   . TYR   A 115 ? 0.3248 0.2248 0.2718 0.0440  0.0294  0.0502  115 TYR   A O   
1742 C  CB  . TYR   A 115 ? 0.2443 0.1785 0.2048 0.0332  0.0129  0.0381  115 TYR   A CB  
1743 C  CG  . TYR   A 115 ? 0.2406 0.1916 0.2054 0.0326  0.0052  0.0338  115 TYR   A CG  
1744 C  CD1 . TYR   A 115 ? 0.2550 0.2131 0.2200 0.0382  0.0025  0.0336  115 TYR   A CD1 
1745 C  CD2 . TYR   A 115 ? 0.2195 0.1797 0.1880 0.0271  0.0009  0.0300  115 TYR   A CD2 
1746 C  CE1 . TYR   A 115 ? 0.2401 0.2142 0.2098 0.0370  -0.0037 0.0296  115 TYR   A CE1 
1747 C  CE2 . TYR   A 115 ? 0.2040 0.1782 0.1764 0.0261  -0.0051 0.0260  115 TYR   A CE2 
1748 C  CZ  . TYR   A 115 ? 0.2044 0.1859 0.1777 0.0308  -0.0073 0.0259  115 TYR   A CZ  
1749 O  OH  . TYR   A 115 ? 0.2129 0.2092 0.1912 0.0291  -0.0126 0.0217  115 TYR   A OH  
1759 N  N   . GLY   A 116 ? 0.2731 0.1796 0.2119 0.0460  0.0299  0.0552  116 GLY   A N   
1760 C  CA  . GLY   A 116 ? 0.3109 0.1979 0.2462 0.0457  0.0403  0.0604  116 GLY   A CA  
1761 C  C   . GLY   A 116 ? 0.3385 0.2170 0.2847 0.0337  0.0439  0.0550  116 GLY   A C   
1762 O  O   . GLY   A 116 ? 0.4075 0.2683 0.3532 0.0322  0.0528  0.0575  116 GLY   A O   
1766 N  N   . VAL   A 117 ? 0.3126 0.2028 0.2679 0.0253  0.0382  0.0481  117 VAL   A N   
1767 C  CA  . VAL   A 117 ? 0.3434 0.2296 0.3095 0.0144  0.0402  0.0419  117 VAL   A CA  
1768 C  C   . VAL   A 117 ? 0.3195 0.2137 0.2905 0.0079  0.0393  0.0395  117 VAL   A C   
1769 O  O   . VAL   A 117 ? 0.2806 0.1855 0.2482 0.0108  0.0348  0.0405  117 VAL   A O   
1770 C  CB  . VAL   A 117 ? 0.3349 0.2277 0.3082 0.0109  0.0340  0.0349  117 VAL   A CB  
1771 C  CG1 . VAL   A 117 ? 0.4449 0.3285 0.4139 0.0173  0.0361  0.0368  117 VAL   A CG1 
1772 C  CG2 . VAL   A 117 ? 0.3011 0.2108 0.2761 0.0111  0.0252  0.0320  117 VAL   A CG2 
1782 N  N   . GLU   A 118 ? 0.3000 0.1894 0.2797 -0.0008 0.0436  0.0356  118 GLU   A N   
1783 C  CA  . GLU   A 118 ? 0.3092 0.2081 0.2961 -0.0074 0.0423  0.0318  118 GLU   A CA  
1784 C  C   . GLU   A 118 ? 0.2562 0.1694 0.2486 -0.0098 0.0328  0.0254  118 GLU   A C   
1785 O  O   . GLU   A 118 ? 0.2829 0.1974 0.2788 -0.0111 0.0292  0.0212  118 GLU   A O   
1786 C  CB  . GLU   A 118 ? 0.3078 0.1992 0.3041 -0.0164 0.0495  0.0282  118 GLU   A CB  
1787 C  CG  . GLU   A 118 ? 0.3681 0.2445 0.3600 -0.0156 0.0606  0.0348  118 GLU   A CG  
1788 C  CD  . GLU   A 118 ? 0.4543 0.3350 0.4418 -0.0134 0.0633  0.0399  118 GLU   A CD  
1789 O  OE1 . GLU   A 118 ? 0.4540 0.3491 0.4446 -0.0147 0.0573  0.0366  118 GLU   A OE1 
1790 O  OE2 . GLU   A 118 ? 0.6151 0.4838 0.5949 -0.0097 0.0722  0.0477  118 GLU   A OE2 
1797 N  N   . ALA   A 119 ? 0.2244 0.1483 0.2172 -0.0100 0.0291  0.0246  119 ALA   A N   
1798 C  CA  . ALA   A 119 ? 0.1979 0.1334 0.1959 -0.0124 0.0217  0.0191  119 ALA   A CA  
1799 C  C   . ALA   A 119 ? 0.2043 0.1419 0.2125 -0.0195 0.0220  0.0130  119 ALA   A C   
1800 O  O   . ALA   A 119 ? 0.2024 0.1450 0.2136 -0.0204 0.0171  0.0088  119 ALA   A O   
1801 C  CB  . ALA   A 119 ? 0.2224 0.1664 0.2185 -0.0111 0.0189  0.0194  119 ALA   A CB  
1807 N  N   . LEU   A 120 ? 0.2051 0.1400 0.2187 -0.0243 0.0280  0.0122  120 LEU   A N   
1808 C  CA  . LEU   A 120 ? 0.1999 0.1393 0.2243 -0.0313 0.0284  0.0052  120 LEU   A CA  
1809 C  C   . LEU   A 120 ? 0.2020 0.1305 0.2306 -0.0363 0.0373  0.0051  120 LEU   A C   
1810 O  O   . LEU   A 120 ? 0.2214 0.1424 0.2464 -0.0354 0.0442  0.0108  120 LEU   A O   
1811 C  CB  . LEU   A 120 ? 0.1821 0.1346 0.2127 -0.0336 0.0264  0.0023  120 LEU   A CB  
1812 C  CG  . LEU   A 120 ? 0.1895 0.1514 0.2169 -0.0294 0.0187  0.0019  120 LEU   A CG  
1813 C  CD1 . LEU   A 120 ? 0.2130 0.1864 0.2463 -0.0307 0.0180  -0.0005 120 LEU   A CD1 
1814 C  CD2 . LEU   A 120 ? 0.2046 0.1706 0.2329 -0.0289 0.0126  -0.0020 120 LEU   A CD2 
1826 N  N   . THR   A 121 ? 0.2090 0.1366 0.2453 -0.0420 0.0377  -0.0018 121 THR   A N   
1827 C  CA  A THR   A 121 ? 0.2436 0.1598 0.2855 -0.0484 0.0469  -0.0034 121 THR   A CA  
1828 C  CA  B THR   A 121 ? 0.2442 0.1604 0.2861 -0.0484 0.0468  -0.0034 121 THR   A CA  
1829 C  C   . THR   A 121 ? 0.2258 0.1530 0.2816 -0.0571 0.0456  -0.0140 121 THR   A C   
1830 O  O   . THR   A 121 ? 0.2381 0.1775 0.2963 -0.0565 0.0374  -0.0198 121 THR   A O   
1831 C  CB  A THR   A 121 ? 0.3119 0.2111 0.3480 -0.0462 0.0504  -0.0018 121 THR   A CB  
1832 C  CB  B THR   A 121 ? 0.3109 0.2109 0.3465 -0.0456 0.0494  -0.0018 121 THR   A CB  
1833 O  OG1 A THR   A 121 ? 0.3135 0.2177 0.3512 -0.0461 0.0437  -0.0084 121 THR   A OG1 
1834 O  OG1 B THR   A 121 ? 0.3585 0.2478 0.3820 -0.0376 0.0528  0.0083  121 THR   A OG1 
1835 C  CG2 A THR   A 121 ? 0.3503 0.2414 0.3727 -0.0362 0.0506  0.0081  121 THR   A CG2 
1836 C  CG2 B THR   A 121 ? 0.3451 0.2330 0.3880 -0.0534 0.0578  -0.0066 121 THR   A CG2 
1848 N  N   . LYS   A 122 ? 0.2408 0.1644 0.3056 -0.0649 0.0538  -0.0165 122 LYS   A N   
1849 C  CA  . LYS   A 122 ? 0.2563 0.1913 0.3359 -0.0742 0.0532  -0.0278 122 LYS   A CA  
1850 C  C   . LYS   A 122 ? 0.2690 0.1973 0.3483 -0.0755 0.0521  -0.0339 122 LYS   A C   
1851 O  O   . LYS   A 122 ? 0.2871 0.1985 0.3574 -0.0716 0.0553  -0.0292 122 LYS   A O   
1852 C  CB  . LYS   A 122 ? 0.2989 0.2348 0.3856 -0.0795 0.0611  -0.0277 122 LYS   A CB  
1853 C  CG  . LYS   A 122 ? 0.3245 0.2639 0.4100 -0.0777 0.0646  -0.0205 122 LYS   A CG  
1854 C  CD  . LYS   A 122 ? 0.4092 0.3478 0.5009 -0.0826 0.0738  -0.0196 122 LYS   A CD  
1855 C  CE  . LYS   A 122 ? 0.4876 0.4418 0.5857 -0.0837 0.0745  -0.0188 122 LYS   A CE  
1856 N  NZ  . LYS   A 122 ? 0.6555 0.6063 0.7577 -0.0877 0.0845  -0.0164 122 LYS   A NZ  
1870 N  N   . SER   A 123 ? 0.2971 0.2398 0.3865 -0.0807 0.0478  -0.0448 123 SER   A N   
1871 C  CA  . SER   A 123 ? 0.3513 0.2894 0.4411 -0.0825 0.0468  -0.0520 123 SER   A CA  
1872 C  C   . SER   A 123 ? 0.3569 0.2765 0.4452 -0.0850 0.0564  -0.0497 123 SER   A C   
1873 O  O   . SER   A 123 ? 0.4536 0.3606 0.5366 -0.0833 0.0575  -0.0508 123 SER   A O   
1874 C  CB  . SER   A 123 ? 0.4560 0.4151 0.5572 -0.0876 0.0412  -0.0640 123 SER   A CB  
1875 O  OG  . SER   A 123 ? 0.6135 0.5908 0.7159 -0.0844 0.0327  -0.0655 123 SER   A OG  
1881 N  N   . ASP   A 124 ? 0.3515 0.2685 0.4435 -0.0882 0.0638  -0.0458 124 ASP   A N   
1882 C  CA  . ASP   A 124 ? 0.4239 0.3233 0.5148 -0.0906 0.0740  -0.0433 124 ASP   A CA  
1883 C  C   . ASP   A 124 ? 0.3947 0.2737 0.4714 -0.0826 0.0790  -0.0313 124 ASP   A C   
1884 O  O   . ASP   A 124 ? 0.4180 0.2813 0.4922 -0.0832 0.0880  -0.0278 124 ASP   A O   
1885 C  CB  . ASP   A 124 ? 0.4300 0.3351 0.5307 -0.0972 0.0807  -0.0441 124 ASP   A CB  
1886 C  CG  . ASP   A 124 ? 0.4535 0.3541 0.5481 -0.0931 0.0856  -0.0326 124 ASP   A CG  
1887 O  OD1 . ASP   A 124 ? 0.4632 0.3640 0.5492 -0.0863 0.0813  -0.0262 124 ASP   A OD1 
1888 O  OD2 . ASP   A 124 ? 0.5627 0.4599 0.6610 -0.0967 0.0941  -0.0300 124 ASP   A OD2 
1893 N  N   . GLY   A 125 ? 0.3841 0.2639 0.4520 -0.0752 0.0740  -0.0249 125 GLY   A N   
1894 C  CA  . GLY   A 125 ? 0.4346 0.2979 0.4884 -0.0662 0.0770  -0.0143 125 GLY   A CA  
1895 C  C   . GLY   A 125 ? 0.4404 0.3024 0.4875 -0.0613 0.0801  -0.0037 125 GLY   A C   
1896 O  O   . GLY   A 125 ? 0.4859 0.3406 0.5210 -0.0524 0.0792  0.0046  125 GLY   A O   
1900 N  N   . SER   A 126 ? 0.4098 0.2803 0.4640 -0.0663 0.0831  -0.0042 126 SER   A N   
1901 C  CA  . SER   A 126 ? 0.4467 0.3154 0.4940 -0.0616 0.0872  0.0056  126 SER   A CA  
1902 C  C   . SER   A 126 ? 0.4184 0.2980 0.4622 -0.0574 0.0800  0.0082  126 SER   A C   
1903 O  O   . SER   A 126 ? 0.3434 0.2344 0.3929 -0.0596 0.0721  0.0016  126 SER   A O   
1904 C  CB  . SER   A 126 ? 0.4901 0.3643 0.5470 -0.0687 0.0938  0.0037  126 SER   A CB  
1905 O  OG  . SER   A 126 ? 0.5922 0.4854 0.6629 -0.0761 0.0885  -0.0059 126 SER   A OG  
1911 N  N   . PRO   A 127 ? 0.3372 0.2134 0.3708 -0.0506 0.0827  0.0180  127 PRO   A N   
1912 C  CA  . PRO   A 127 ? 0.3177 0.2068 0.3471 -0.0455 0.0748  0.0200  127 PRO   A CA  
1913 C  C   . PRO   A 127 ? 0.3364 0.2447 0.3786 -0.0519 0.0707  0.0123  127 PRO   A C   
1914 O  O   . PRO   A 127 ? 0.3182 0.2281 0.3708 -0.0598 0.0779  0.0096  127 PRO   A O   
1915 C  CB  . PRO   A 127 ? 0.3468 0.2296 0.3638 -0.0380 0.0802  0.0306  127 PRO   A CB  
1916 C  CG  . PRO   A 127 ? 0.4313 0.2950 0.4414 -0.0352 0.0882  0.0359  127 PRO   A CG  
1917 C  CD  . PRO   A 127 ? 0.4059 0.2687 0.4289 -0.0449 0.0913  0.0275  127 PRO   A CD  
1925 N  N   . MET   A 128 ? 0.2605 0.1830 0.3020 -0.0485 0.0597  0.0089  128 MET   A N   
1926 C  CA  . MET   A 128 ? 0.2664 0.2078 0.3184 -0.0523 0.0548  0.0022  128 MET   A CA  
1927 C  C   . MET   A 128 ? 0.1972 0.1465 0.2424 -0.0457 0.0516  0.0068  128 MET   A C   
1928 O  O   . MET   A 128 ? 0.2300 0.1772 0.2643 -0.0385 0.0461  0.0105  128 MET   A O   
1929 C  CB  . MET   A 128 ? 0.2288 0.1792 0.2849 -0.0529 0.0455  -0.0053 128 MET   A CB  
1930 C  CG  . MET   A 128 ? 0.2091 0.1790 0.2732 -0.0539 0.0393  -0.0111 128 MET   A CG  
1931 S  SD  . MET   A 128 ? 0.2655 0.2447 0.3339 -0.0547 0.0303  -0.0198 128 MET   A SD  
1932 C  CE  . MET   A 128 ? 0.3134 0.3141 0.3872 -0.0523 0.0240  -0.0232 128 MET   A CE  
1942 N  N   . GLN   A 129 ? 0.1884 0.1469 0.2401 -0.0484 0.0551  0.0059  129 GLN   A N   
1943 C  CA  . GLN   A 129 ? 0.1967 0.1623 0.2419 -0.0422 0.0529  0.0096  129 GLN   A CA  
1944 C  C   . GLN   A 129 ? 0.1991 0.1753 0.2431 -0.0381 0.0421  0.0059  129 GLN   A C   
1945 O  O   . GLN   A 129 ? 0.1826 0.1680 0.2358 -0.0415 0.0378  -0.0008 129 GLN   A O   
1946 C  CB  . GLN   A 129 ? 0.1916 0.1665 0.2455 -0.0459 0.0591  0.0086  129 GLN   A CB  
1947 C  CG  . GLN   A 129 ? 0.2030 0.1840 0.2494 -0.0391 0.0578  0.0121  129 GLN   A CG  
1948 C  CD  . GLN   A 129 ? 0.2372 0.2287 0.2928 -0.0423 0.0642  0.0109  129 GLN   A CD  
1949 O  OE1 . GLN   A 129 ? 0.2229 0.2280 0.2924 -0.0473 0.0630  0.0042  129 GLN   A OE1 
1950 N  NE2 . GLN   A 129 ? 0.2185 0.2051 0.2661 -0.0389 0.0712  0.0174  129 GLN   A NE2 
1959 N  N   . LEU   A 130 ? 0.1662 0.1408 0.1990 -0.0309 0.0382  0.0098  130 LEU   A N   
1960 C  CA  . LEU   A 130 ? 0.1571 0.1390 0.1876 -0.0270 0.0295  0.0072  130 LEU   A CA  
1961 C  C   . LEU   A 130 ? 0.1706 0.1644 0.2064 -0.0264 0.0294  0.0047  130 LEU   A C   
1962 O  O   . LEU   A 130 ? 0.1811 0.1749 0.2129 -0.0239 0.0333  0.0078  130 LEU   A O   
1963 C  CB  . LEU   A 130 ? 0.1702 0.1458 0.1879 -0.0207 0.0264  0.0114  130 LEU   A CB  
1964 C  CG  . LEU   A 130 ? 0.1934 0.1615 0.2063 -0.0195 0.0235  0.0127  130 LEU   A CG  
1965 C  CD1 . LEU   A 130 ? 0.2340 0.1923 0.2461 -0.0212 0.0294  0.0157  130 LEU   A CD1 
1966 C  CD2 . LEU   A 130 ? 0.2006 0.1676 0.2028 -0.0133 0.0192  0.0152  130 LEU   A CD2 
1978 N  N   . VAL   A 131 ? 0.1395 0.1441 0.1839 -0.0278 0.0252  -0.0007 131 VAL   A N   
1979 C  CA  . VAL   A 131 ? 0.1323 0.1501 0.1826 -0.0262 0.0248  -0.0034 131 VAL   A CA  
1980 C  C   . VAL   A 131 ? 0.1433 0.1625 0.1872 -0.0198 0.0178  -0.0037 131 VAL   A C   
1981 O  O   . VAL   A 131 ? 0.1440 0.1641 0.1881 -0.0191 0.0123  -0.0058 131 VAL   A O   
1982 C  CB  . VAL   A 131 ? 0.1422 0.1729 0.2070 -0.0316 0.0255  -0.0096 131 VAL   A CB  
1983 C  CG1 . VAL   A 131 ? 0.1609 0.2066 0.2312 -0.0281 0.0245  -0.0120 131 VAL   A CG1 
1984 C  CG2 . VAL   A 131 ? 0.1614 0.1883 0.2333 -0.0393 0.0337  -0.0096 131 VAL   A CG2 
1994 N  N   . MET   A 132 ? 0.1320 0.1502 0.1696 -0.0149 0.0185  -0.0015 132 MET   A N   
1995 C  CA  . MET   A 132 ? 0.1392 0.1553 0.1696 -0.0091 0.0135  -0.0015 132 MET   A CA  
1996 C  C   . MET   A 132 ? 0.1363 0.1633 0.1714 -0.0053 0.0133  -0.0039 132 MET   A C   
1997 O  O   . MET   A 132 ? 0.1458 0.1760 0.1810 -0.0037 0.0175  -0.0033 132 MET   A O   
1998 C  CB  . MET   A 132 ? 0.1744 0.1807 0.1934 -0.0061 0.0142  0.0016  132 MET   A CB  
1999 C  CG  . MET   A 132 ? 0.1839 0.1817 0.1981 -0.0086 0.0158  0.0047  132 MET   A CG  
2000 S  SD  . MET   A 132 ? 0.2052 0.1970 0.2170 -0.0096 0.0099  0.0044  132 MET   A SD  
2001 C  CE  . MET   A 132 ? 0.2556 0.2424 0.2573 -0.0052 0.0063  0.0044  132 MET   A CE  
2011 N  N   . ARG   A 133 ? 0.1386 0.1719 0.1771 -0.0029 0.0088  -0.0064 133 ARG   A N   
2012 C  CA  . ARG   A 133 ? 0.1183 0.1628 0.1610 0.0024  0.0080  -0.0085 133 ARG   A CA  
2013 C  C   . ARG   A 133 ? 0.1343 0.1700 0.1669 0.0093  0.0059  -0.0068 133 ARG   A C   
2014 O  O   . ARG   A 133 ? 0.1444 0.1730 0.1719 0.0109  0.0021  -0.0059 133 ARG   A O   
2015 C  CB  . ARG   A 133 ? 0.1216 0.1790 0.1728 0.0024  0.0044  -0.0120 133 ARG   A CB  
2016 C  CG  . ARG   A 133 ? 0.1554 0.2214 0.2180 -0.0058 0.0065  -0.0154 133 ARG   A CG  
2017 C  CD  . ARG   A 133 ? 0.1688 0.2529 0.2416 -0.0051 0.0029  -0.0209 133 ARG   A CD  
2018 N  NE  . ARG   A 133 ? 0.1616 0.2437 0.2283 -0.0003 -0.0033 -0.0207 133 ARG   A NE  
2019 C  CZ  . ARG   A 133 ? 0.1749 0.2718 0.2459 0.0038  -0.0079 -0.0244 133 ARG   A CZ  
2020 N  NH1 . ARG   A 133 ? 0.1946 0.3113 0.2779 0.0029  -0.0078 -0.0297 133 ARG   A NH1 
2021 N  NH2 . ARG   A 133 ? 0.1911 0.2834 0.2539 0.0091  -0.0125 -0.0226 133 ARG   A NH2 
2035 N  N   . VAL   A 134 ? 0.1267 0.1618 0.1562 0.0130  0.0089  -0.0064 134 VAL   A N   
2036 C  CA  . VAL   A 134 ? 0.1458 0.1698 0.1651 0.0186  0.0081  -0.0056 134 VAL   A CA  
2037 C  C   . VAL   A 134 ? 0.1401 0.1711 0.1611 0.0266  0.0082  -0.0068 134 VAL   A C   
2038 O  O   . VAL   A 134 ? 0.1440 0.1898 0.1736 0.0278  0.0099  -0.0083 134 VAL   A O   
2039 C  CB  . VAL   A 134 ? 0.1724 0.1890 0.1848 0.0173  0.0114  -0.0048 134 VAL   A CB  
2040 C  CG1 . VAL   A 134 ? 0.2034 0.2087 0.2057 0.0217  0.0109  -0.0057 134 VAL   A CG1 
2041 C  CG2 . VAL   A 134 ? 0.2036 0.2150 0.2147 0.0108  0.0112  -0.0031 134 VAL   A CG2 
2051 N  N   . HIS   A 135 ? 0.1499 0.1700 0.1626 0.0322  0.0071  -0.0063 135 HIS   A N   
2052 C  CA  . HIS   A 135 ? 0.1600 0.1832 0.1720 0.0413  0.0075  -0.0066 135 HIS   A CA  
2053 C  C   . HIS   A 135 ? 0.1658 0.2026 0.1850 0.0445  0.0045  -0.0066 135 HIS   A C   
2054 O  O   . HIS   A 135 ? 0.1599 0.2097 0.1840 0.0511  0.0049  -0.0076 135 HIS   A O   
2055 C  CB  . HIS   A 135 ? 0.1636 0.1943 0.1775 0.0452  0.0117  -0.0082 135 HIS   A CB  
2056 C  CG  . HIS   A 135 ? 0.1689 0.1887 0.1749 0.0434  0.0147  -0.0089 135 HIS   A CG  
2057 N  ND1 . HIS   A 135 ? 0.2319 0.2352 0.2275 0.0463  0.0145  -0.0097 135 HIS   A ND1 
2058 C  CD2 . HIS   A 135 ? 0.1781 0.2018 0.1847 0.0398  0.0181  -0.0093 135 HIS   A CD2 
2059 C  CE1 . HIS   A 135 ? 0.2214 0.2204 0.2116 0.0445  0.0169  -0.0113 135 HIS   A CE1 
2060 N  NE2 . HIS   A 135 ? 0.1898 0.2010 0.1858 0.0413  0.0193  -0.0105 135 HIS   A NE2 
2069 N  N   . TYR   A 136 ? 0.1466 0.1817 0.1664 0.0401  0.0012  -0.0057 136 TYR   A N   
2070 C  CA  . TYR   A 136 ? 0.1416 0.1903 0.1671 0.0431  -0.0023 -0.0063 136 TYR   A CA  
2071 C  C   . TYR   A 136 ? 0.1482 0.1924 0.1666 0.0540  -0.0035 -0.0038 136 TYR   A C   
2072 O  O   . TYR   A 136 ? 0.1769 0.2028 0.1855 0.0551  -0.0030 -0.0009 136 TYR   A O   
2073 C  CB  . TYR   A 136 ? 0.1651 0.2111 0.1913 0.0359  -0.0051 -0.0062 136 TYR   A CB  
2074 C  CG  . TYR   A 136 ? 0.1553 0.2135 0.1850 0.0390  -0.0092 -0.0072 136 TYR   A CG  
2075 C  CD1 . TYR   A 136 ? 0.1544 0.2327 0.1960 0.0360  -0.0106 -0.0117 136 TYR   A CD1 
2076 C  CD2 . TYR   A 136 ? 0.1787 0.2291 0.2001 0.0444  -0.0115 -0.0040 136 TYR   A CD2 
2077 C  CE1 . TYR   A 136 ? 0.1739 0.2656 0.2186 0.0390  -0.0152 -0.0140 136 TYR   A CE1 
2078 C  CE2 . TYR   A 136 ? 0.1981 0.2606 0.2214 0.0478  -0.0155 -0.0050 136 TYR   A CE2 
2079 C  CZ  . TYR   A 136 ? 0.1767 0.2600 0.2111 0.0456  -0.0177 -0.0102 136 TYR   A CZ  
2080 O  OH  . TYR   A 136 ? 0.2187 0.3161 0.2548 0.0494  -0.0224 -0.0124 136 TYR   A OH  
2090 N  N   . GLY   A 137 ? 0.1501 0.2110 0.1736 0.0618  -0.0049 -0.0049 137 GLY   A N   
2091 C  CA  . GLY   A 137 ? 0.1642 0.2224 0.1805 0.0734  -0.0063 -0.0017 137 GLY   A CA  
2092 C  C   . GLY   A 137 ? 0.2084 0.2498 0.2152 0.0810  -0.0022 0.0010  137 GLY   A C   
2093 O  O   . GLY   A 137 ? 0.2044 0.2383 0.2104 0.0776  0.0011  -0.0005 137 GLY   A O   
2097 N  N   . GLN   A 138 ? 0.2003 0.2359 0.1992 0.0922  -0.0024 0.0049  138 GLN   A N   
2098 C  CA  . GLN   A 138 ? 0.2348 0.2525 0.2239 0.1009  0.0020  0.0076  138 GLN   A CA  
2099 C  C   . GLN   A 138 ? 0.2631 0.2563 0.2410 0.0999  0.0036  0.0121  138 GLN   A C   
2100 O  O   . GLN   A 138 ? 0.2814 0.2745 0.2550 0.1051  0.0020  0.0161  138 GLN   A O   
2101 C  CB  . GLN   A 138 ? 0.3143 0.3438 0.3028 0.1163  0.0019  0.0092  138 GLN   A CB  
2102 C  CG  . GLN   A 138 ? 0.4718 0.4866 0.4532 0.1248  0.0073  0.0100  138 GLN   A CG  
2103 C  CD  . GLN   A 138 ? 0.6363 0.6577 0.6245 0.1197  0.0096  0.0047  138 GLN   A CD  
2104 O  OE1 . GLN   A 138 ? 0.4733 0.4792 0.4583 0.1107  0.0120  0.0029  138 GLN   A OE1 
2105 N  NE2 . GLN   A 138 ? 0.5836 0.6286 0.5807 0.1259  0.0091  0.0023  138 GLN   A NE2 
2114 N  N   . GLY   A 139 ? 0.2558 0.2291 0.2292 0.0930  0.0070  0.0110  139 GLY   A N   
2115 C  CA  . GLY   A 139 ? 0.2794 0.2293 0.2438 0.0903  0.0095  0.0143  139 GLY   A CA  
2116 C  C   . GLY   A 139 ? 0.2426 0.1965 0.2093 0.0826  0.0061  0.0157  139 GLY   A C   
2117 O  O   . GLY   A 139 ? 0.2887 0.2296 0.2484 0.0845  0.0078  0.0202  139 GLY   A O   
2121 N  N   . TYR   A 140 ? 0.2245 0.1946 0.2003 0.0743  0.0023  0.0120  140 TYR   A N   
2122 C  CA  . TYR   A 140 ? 0.2057 0.1811 0.1842 0.0674  -0.0009 0.0126  140 TYR   A CA  
2123 C  C   . TYR   A 140 ? 0.2091 0.1682 0.1848 0.0575  0.0007  0.0123  140 TYR   A C   
2124 O  O   . TYR   A 140 ? 0.2163 0.1757 0.1956 0.0502  0.0007  0.0086  140 TYR   A O   
2125 C  CB  . TYR   A 140 ? 0.2090 0.2067 0.1984 0.0630  -0.0047 0.0085  140 TYR   A CB  
2126 C  CG  . TYR   A 140 ? 0.1868 0.1919 0.1791 0.0576  -0.0083 0.0083  140 TYR   A CG  
2127 C  CD1 . TYR   A 140 ? 0.2198 0.2330 0.2100 0.0644  -0.0108 0.0104  140 TYR   A CD1 
2128 C  CD2 . TYR   A 140 ? 0.1759 0.1799 0.1723 0.0466  -0.0089 0.0060  140 TYR   A CD2 
2129 C  CE1 . TYR   A 140 ? 0.2042 0.2241 0.1964 0.0599  -0.0140 0.0095  140 TYR   A CE1 
2130 C  CE2 . TYR   A 140 ? 0.2057 0.2156 0.2045 0.0423  -0.0117 0.0054  140 TYR   A CE2 
2131 C  CZ  . TYR   A 140 ? 0.2171 0.2349 0.2139 0.0486  -0.0143 0.0068  140 TYR   A CZ  
2132 O  OH  . TYR   A 140 ? 0.2226 0.2461 0.2210 0.0446  -0.0170 0.0056  140 TYR   A OH  
2142 N  N   . GLU   A 141 ? 0.2368 0.1835 0.2065 0.0575  0.0022  0.0162  141 GLU   A N   
2143 C  CA  . GLU   A 141 ? 0.2382 0.1703 0.2062 0.0482  0.0041  0.0155  141 GLU   A CA  
2144 C  C   . GLU   A 141 ? 0.2455 0.1863 0.2178 0.0411  0.0008  0.0153  141 GLU   A C   
2145 O  O   . GLU   A 141 ? 0.2680 0.2007 0.2368 0.0394  0.0022  0.0184  141 GLU   A O   
2146 C  CB  . GLU   A 141 ? 0.3030 0.2150 0.2625 0.0520  0.0092  0.0198  141 GLU   A CB  
2147 C  CG  . GLU   A 141 ? 0.3812 0.2826 0.3358 0.0599  0.0131  0.0199  141 GLU   A CG  
2148 C  CD  . GLU   A 141 ? 0.6031 0.4797 0.5506 0.0593  0.0195  0.0219  141 GLU   A CD  
2149 O  OE1 . GLU   A 141 ? 0.5014 0.3690 0.4434 0.0626  0.0225  0.0278  141 GLU   A OE1 
2150 O  OE2 . GLU   A 141 ? 0.4735 0.3396 0.4209 0.0551  0.0219  0.0171  141 GLU   A OE2 
2157 N  N   . ASN   A 142 ? 0.2216 0.1773 0.2011 0.0371  -0.0027 0.0119  142 ASN   A N   
2158 C  CA  . ASN   A 142 ? 0.1927 0.1561 0.1763 0.0308  -0.0055 0.0112  142 ASN   A CA  
2159 C  C   . ASN   A 142 ? 0.1829 0.1571 0.1737 0.0257  -0.0073 0.0072  142 ASN   A C   
2160 O  O   . ASN   A 142 ? 0.1776 0.1555 0.1705 0.0274  -0.0064 0.0053  142 ASN   A O   
2161 C  CB  . ASN   A 142 ? 0.2094 0.1819 0.1921 0.0362  -0.0077 0.0134  142 ASN   A CB  
2162 C  CG  . ASN   A 142 ? 0.2008 0.1780 0.1857 0.0306  -0.0099 0.0128  142 ASN   A CG  
2163 O  OD1 . ASN   A 142 ? 0.1992 0.1677 0.1830 0.0249  -0.0086 0.0134  142 ASN   A OD1 
2164 N  ND2 . ASN   A 142 ? 0.2264 0.2183 0.2151 0.0323  -0.0132 0.0109  142 ASN   A ND2 
2171 N  N   . ALA   A 143 ? 0.1654 0.1438 0.1595 0.0196  -0.0091 0.0062  143 ALA   A N   
2172 C  CA  . ALA   A 143 ? 0.1669 0.1540 0.1674 0.0145  -0.0100 0.0033  143 ALA   A CA  
2173 C  C   . ALA   A 143 ? 0.1686 0.1620 0.1720 0.0118  -0.0123 0.0027  143 ALA   A C   
2174 O  O   . ALA   A 143 ? 0.1734 0.1620 0.1729 0.0122  -0.0128 0.0047  143 ALA   A O   
2175 C  CB  . ALA   A 143 ? 0.1657 0.1457 0.1652 0.0093  -0.0086 0.0025  143 ALA   A CB  
2181 N  N   . TYR   A 144 ? 0.1459 0.1494 0.1560 0.0088  -0.0131 -0.0002 144 TYR   A N   
2182 C  CA  . TYR   A 144 ? 0.1482 0.1575 0.1611 0.0064  -0.0151 -0.0019 144 TYR   A CA  
2183 C  C   . TYR   A 144 ? 0.1550 0.1701 0.1753 0.0007  -0.0143 -0.0053 144 TYR   A C   
2184 O  O   . TYR   A 144 ? 0.1524 0.1711 0.1770 -0.0005 -0.0122 -0.0064 144 TYR   A O   
2185 C  CB  . TYR   A 144 ? 0.1487 0.1676 0.1613 0.0124  -0.0178 -0.0026 144 TYR   A CB  
2186 C  CG  . TYR   A 144 ? 0.1488 0.1809 0.1671 0.0157  -0.0186 -0.0055 144 TYR   A CG  
2187 C  CD1 . TYR   A 144 ? 0.1661 0.2124 0.1937 0.0121  -0.0199 -0.0110 144 TYR   A CD1 
2188 C  CD2 . TYR   A 144 ? 0.1731 0.2049 0.1886 0.0224  -0.0177 -0.0034 144 TYR   A CD2 
2189 C  CE1 . TYR   A 144 ? 0.1800 0.2412 0.2146 0.0147  -0.0207 -0.0143 144 TYR   A CE1 
2190 C  CE2 . TYR   A 144 ? 0.1926 0.2394 0.2143 0.0263  -0.0186 -0.0063 144 TYR   A CE2 
2191 C  CZ  . TYR   A 144 ? 0.1784 0.2408 0.2101 0.0221  -0.0203 -0.0119 144 TYR   A CZ  
2192 O  OH  . TYR   A 144 ? 0.2295 0.3089 0.2689 0.0258  -0.0209 -0.0152 144 TYR   A OH  
2202 N  N   . TRP   A 145 ? 0.1305 0.1464 0.1523 -0.0026 -0.0153 -0.0070 145 TRP   A N   
2203 C  CA  . TRP   A 145 ? 0.1266 0.1470 0.1556 -0.0082 -0.0142 -0.0109 145 TRP   A CA  
2204 C  C   . TRP   A 145 ? 0.1333 0.1672 0.1678 -0.0075 -0.0170 -0.0161 145 TRP   A C   
2205 O  O   . TRP   A 145 ? 0.1435 0.1798 0.1738 -0.0037 -0.0201 -0.0162 145 TRP   A O   
2206 C  CB  . TRP   A 145 ? 0.1323 0.1433 0.1585 -0.0117 -0.0133 -0.0098 145 TRP   A CB  
2207 C  CG  . TRP   A 145 ? 0.1370 0.1503 0.1691 -0.0167 -0.0122 -0.0142 145 TRP   A CG  
2208 C  CD1 . TRP   A 145 ? 0.1535 0.1702 0.1861 -0.0170 -0.0145 -0.0177 145 TRP   A CD1 
2209 C  CD2 . TRP   A 145 ? 0.1357 0.1461 0.1730 -0.0218 -0.0080 -0.0153 145 TRP   A CD2 
2210 N  NE1 . TRP   A 145 ? 0.1676 0.1834 0.2061 -0.0226 -0.0121 -0.0219 145 TRP   A NE1 
2211 C  CE2 . TRP   A 145 ? 0.1481 0.1598 0.1899 -0.0257 -0.0077 -0.0202 145 TRP   A CE2 
2212 C  CE3 . TRP   A 145 ? 0.1631 0.1703 0.2016 -0.0233 -0.0039 -0.0128 145 TRP   A CE3 
2213 C  CZ2 . TRP   A 145 ? 0.1677 0.1751 0.2152 -0.0316 -0.0028 -0.0223 145 TRP   A CZ2 
2214 C  CZ3 . TRP   A 145 ? 0.1508 0.1542 0.1944 -0.0287 0.0012  -0.0141 145 TRP   A CZ3 
2215 C  CH2 . TRP   A 145 ? 0.1675 0.1708 0.2159 -0.0329 0.0018  -0.0188 145 TRP   A CH2 
2226 N  N   . ASP   A 146 ? 0.1204 0.1639 0.1642 -0.0111 -0.0158 -0.0207 146 ASP   A N   
2227 C  CA  . ASP   A 146 ? 0.1468 0.2067 0.1974 -0.0105 -0.0190 -0.0272 146 ASP   A CA  
2228 C  C   . ASP   A 146 ? 0.1444 0.2073 0.2028 -0.0182 -0.0181 -0.0338 146 ASP   A C   
2229 O  O   . ASP   A 146 ? 0.1632 0.2416 0.2295 -0.0193 -0.0205 -0.0410 146 ASP   A O   
2230 C  CB  . ASP   A 146 ? 0.1539 0.2273 0.2111 -0.0079 -0.0189 -0.0289 146 ASP   A CB  
2231 C  CG  . ASP   A 146 ? 0.1694 0.2443 0.2361 -0.0150 -0.0140 -0.0312 146 ASP   A CG  
2232 O  OD1 . ASP   A 146 ? 0.1661 0.2287 0.2323 -0.0211 -0.0102 -0.0299 146 ASP   A OD1 
2233 O  OD2 . ASP   A 146 ? 0.2050 0.2933 0.2793 -0.0141 -0.0135 -0.0338 146 ASP   A OD2 
2238 N  N   . GLY   A 147 ? 0.1438 0.1923 0.2004 -0.0232 -0.0143 -0.0318 147 GLY   A N   
2239 C  CA  . GLY   A 147 ? 0.1660 0.2130 0.2291 -0.0305 -0.0121 -0.0376 147 GLY   A CA  
2240 C  C   . GLY   A 147 ? 0.1726 0.2140 0.2424 -0.0372 -0.0054 -0.0374 147 GLY   A C   
2241 O  O   . GLY   A 147 ? 0.2127 0.2464 0.2857 -0.0431 -0.0018 -0.0402 147 GLY   A O   
2245 N  N   . LYS   A 148 ? 0.1555 0.1997 0.2269 -0.0359 -0.0032 -0.0341 148 LYS   A N   
2246 C  CA  . LYS   A 148 ? 0.1672 0.2062 0.2441 -0.0415 0.0042  -0.0328 148 LYS   A CA  
2247 C  C   . LYS   A 148 ? 0.1808 0.2143 0.2511 -0.0372 0.0065  -0.0252 148 LYS   A C   
2248 O  O   . LYS   A 148 ? 0.1702 0.1960 0.2411 -0.0404 0.0130  -0.0222 148 LYS   A O   
2249 C  CB  . LYS   A 148 ? 0.1740 0.2294 0.2656 -0.0470 0.0058  -0.0403 148 LYS   A CB  
2250 C  CG  . LYS   A 148 ? 0.1982 0.2702 0.2931 -0.0419 0.0028  -0.0409 148 LYS   A CG  
2251 C  CD  . LYS   A 148 ? 0.3108 0.4027 0.4218 -0.0472 0.0038  -0.0496 148 LYS   A CD  
2252 C  CE  . LYS   A 148 ? 0.4488 0.5574 0.5628 -0.0408 0.0013  -0.0494 148 LYS   A CE  
2253 N  NZ  . LYS   A 148 ? 0.5920 0.7234 0.7226 -0.0454 0.0012  -0.0587 148 LYS   A NZ  
2267 N  N   . GLN   A 149 ? 0.1337 0.1704 0.1976 -0.0301 0.0019  -0.0225 149 GLN   A N   
2268 C  CA  . GLN   A 149 ? 0.1427 0.1751 0.2009 -0.0261 0.0039  -0.0170 149 GLN   A CA  
2269 C  C   . GLN   A 149 ? 0.1281 0.1560 0.1762 -0.0193 -0.0007 -0.0135 149 GLN   A C   
2270 O  O   . GLN   A 149 ? 0.1441 0.1734 0.1901 -0.0174 -0.0051 -0.0149 149 GLN   A O   
2271 C  CB  . GLN   A 149 ? 0.1329 0.1788 0.1995 -0.0260 0.0059  -0.0195 149 GLN   A CB  
2272 C  CG  . GLN   A 149 ? 0.1683 0.2289 0.2378 -0.0207 0.0003  -0.0229 149 GLN   A CG  
2273 C  CD  . GLN   A 149 ? 0.2488 0.3279 0.3315 -0.0229 0.0017  -0.0285 149 GLN   A CD  
2274 O  OE1 . GLN   A 149 ? 0.2462 0.3266 0.3364 -0.0290 0.0078  -0.0295 149 GLN   A OE1 
2275 N  NE2 . GLN   A 149 ? 0.2012 0.2955 0.2869 -0.0176 -0.0035 -0.0320 149 GLN   A NE2 
2284 N  N   . MET   A 150 ? 0.1261 0.1491 0.1682 -0.0158 0.0006  -0.0097 150 MET   A N   
2285 C  CA  . MET   A 150 ? 0.1354 0.1516 0.1683 -0.0106 -0.0024 -0.0067 150 MET   A CA  
2286 C  C   . MET   A 150 ? 0.1371 0.1597 0.1704 -0.0055 -0.0027 -0.0070 150 MET   A C   
2287 O  O   . MET   A 150 ? 0.1706 0.1973 0.2071 -0.0059 0.0008  -0.0073 150 MET   A O   
2288 C  CB  . MET   A 150 ? 0.1584 0.1629 0.1837 -0.0111 -0.0008 -0.0030 150 MET   A CB  
2289 C  CG  . MET   A 150 ? 0.1762 0.1742 0.1999 -0.0142 -0.0012 -0.0022 150 MET   A CG  
2290 S  SD  . MET   A 150 ? 0.1720 0.1690 0.2018 -0.0199 0.0035  -0.0032 150 MET   A SD  
2291 C  CE  . MET   A 150 ? 0.1816 0.1764 0.2100 -0.0199 0.0094  -0.0002 150 MET   A CE  
2301 N  N   . THR   A 151 ? 0.1313 0.1537 0.1605 -0.0003 -0.0060 -0.0065 151 THR   A N   
2302 C  CA  . THR   A 151 ? 0.1350 0.1623 0.1636 0.0062  -0.0062 -0.0065 151 THR   A CA  
2303 C  C   . THR   A 151 ? 0.1411 0.1559 0.1600 0.0103  -0.0067 -0.0035 151 THR   A C   
2304 O  O   . THR   A 151 ? 0.1608 0.1686 0.1752 0.0101  -0.0086 -0.0020 151 THR   A O   
2305 C  CB  . THR   A 151 ? 0.1586 0.1993 0.1924 0.0096  -0.0093 -0.0090 151 THR   A CB  
2306 O  OG1 . THR   A 151 ? 0.1469 0.2003 0.1914 0.0042  -0.0088 -0.0134 151 THR   A OG1 
2307 C  CG2 . THR   A 151 ? 0.1599 0.2071 0.1931 0.0179  -0.0096 -0.0088 151 THR   A CG2 
2315 N  N   . PHE   A 152 ? 0.1389 0.1508 0.1550 0.0137  -0.0045 -0.0031 152 PHE   A N   
2316 C  CA  . PHE   A 152 ? 0.1455 0.1442 0.1530 0.0165  -0.0041 -0.0016 152 PHE   A CA  
2317 C  C   . PHE   A 152 ? 0.1620 0.1614 0.1675 0.0243  -0.0031 -0.0016 152 PHE   A C   
2318 O  O   . PHE   A 152 ? 0.1656 0.1721 0.1741 0.0266  -0.0010 -0.0029 152 PHE   A O   
2319 C  CB  . PHE   A 152 ? 0.1641 0.1565 0.1684 0.0129  -0.0020 -0.0020 152 PHE   A CB  
2320 C  CG  . PHE   A 152 ? 0.1464 0.1385 0.1521 0.0066  -0.0024 -0.0015 152 PHE   A CG  
2321 C  CD1 . PHE   A 152 ? 0.1579 0.1425 0.1600 0.0041  -0.0042 -0.0007 152 PHE   A CD1 
2322 C  CD2 . PHE   A 152 ? 0.1547 0.1540 0.1658 0.0036  -0.0003 -0.0017 152 PHE   A CD2 
2323 C  CE1 . PHE   A 152 ? 0.1836 0.1682 0.1867 -0.0003 -0.0045 0.0000  152 PHE   A CE1 
2324 C  CE2 . PHE   A 152 ? 0.1641 0.1611 0.1756 -0.0012 0.0001  -0.0007 152 PHE   A CE2 
2325 C  CZ  . PHE   A 152 ? 0.1804 0.1704 0.1876 -0.0025 -0.0022 0.0002  152 PHE   A CZ  
2335 N  N   . GLY   A 153 ? 0.1625 0.1538 0.1625 0.0289  -0.0037 0.0004  153 GLY   A N   
2336 C  CA  . GLY   A 153 ? 0.1795 0.1669 0.1755 0.0371  -0.0019 0.0010  153 GLY   A CA  
2337 C  C   . GLY   A 153 ? 0.1714 0.1461 0.1617 0.0368  0.0010  -0.0004 153 GLY   A C   
2338 O  O   . GLY   A 153 ? 0.1824 0.1509 0.1709 0.0305  0.0011  -0.0017 153 GLY   A O   
2342 N  N   . ASP   A 154 ? 0.1857 0.1573 0.1728 0.0446  0.0032  -0.0004 154 ASP   A N   
2343 C  CA  . ASP   A 154 ? 0.1967 0.1552 0.1774 0.0458  0.0063  -0.0026 154 ASP   A CA  
2344 C  C   . ASP   A 154 ? 0.2232 0.1627 0.1966 0.0471  0.0079  -0.0014 154 ASP   A C   
2345 O  O   . ASP   A 154 ? 0.2448 0.1713 0.2129 0.0475  0.0107  -0.0042 154 ASP   A O   
2346 C  CB  . ASP   A 154 ? 0.2107 0.1758 0.1921 0.0536  0.0087  -0.0040 154 ASP   A CB  
2347 C  CG  . ASP   A 154 ? 0.2328 0.2095 0.2187 0.0497  0.0094  -0.0066 154 ASP   A CG  
2348 O  OD1 . ASP   A 154 ? 0.2589 0.2342 0.2446 0.0422  0.0088  -0.0077 154 ASP   A OD1 
2349 O  OD2 . ASP   A 154 ? 0.3201 0.3076 0.3094 0.0550  0.0114  -0.0075 154 ASP   A OD2 
2354 N  N   . GLY   A 155 ? 0.2250 0.1614 0.1977 0.0472  0.0069  0.0022  155 GLY   A N   
2355 C  CA  . GLY   A 155 ? 0.2482 0.1656 0.2142 0.0481  0.0099  0.0041  155 GLY   A CA  
2356 C  C   . GLY   A 155 ? 0.2904 0.1991 0.2507 0.0591  0.0135  0.0063  155 GLY   A C   
2357 O  O   . GLY   A 155 ? 0.3005 0.2204 0.2625 0.0669  0.0130  0.0066  155 GLY   A O   
2361 N  N   . ASP   A 156 ? 0.3392 0.2269 0.2929 0.0594  0.0178  0.0075  156 ASP   A N   
2362 C  CA  . ASP   A 156 ? 0.3681 0.2417 0.3144 0.0701  0.0227  0.0102  156 ASP   A CA  
2363 C  C   . ASP   A 156 ? 0.3956 0.2441 0.3367 0.0649  0.0280  0.0081  156 ASP   A C   
2364 O  O   . ASP   A 156 ? 0.4082 0.2540 0.3512 0.0569  0.0276  0.0013  156 ASP   A O   
2365 C  CB  . ASP   A 156 ? 0.4360 0.3142 0.3796 0.0799  0.0224  0.0175  156 ASP   A CB  
2366 C  CG  . ASP   A 156 ? 0.6478 0.5242 0.5862 0.0947  0.0251  0.0201  156 ASP   A CG  
2367 O  OD1 . ASP   A 156 ? 0.7191 0.5880 0.6558 0.0967  0.0279  0.0161  156 ASP   A OD1 
2368 O  OD2 . ASP   A 156 ? 0.6895 0.5729 0.6252 0.1050  0.0244  0.0258  156 ASP   A OD2 
2373 N  N   . THR   A 157 ? 0.4495 0.2802 0.3841 0.0690  0.0331  0.0136  157 THR   A N   
2374 C  CA  . THR   A 157 ? 0.5064 0.3109 0.4364 0.0645  0.0397  0.0112  157 THR   A CA  
2375 C  C   . THR   A 157 ? 0.4748 0.2767 0.4096 0.0502  0.0392  0.0084  157 THR   A C   
2376 O  O   . THR   A 157 ? 0.5539 0.3405 0.4888 0.0425  0.0428  0.0026  157 THR   A O   
2377 C  CB  . THR   A 157 ? 0.5122 0.2974 0.4334 0.0742  0.0468  0.0188  157 THR   A CB  
2378 O  OG1 . THR   A 157 ? 0.5762 0.3654 0.4967 0.0743  0.0464  0.0261  157 THR   A OG1 
2379 C  CG2 . THR   A 157 ? 0.5468 0.3391 0.4643 0.0885  0.0465  0.0215  157 THR   A CG2 
2387 N  N   . MET   A 158 ? 0.4521 0.2687 0.3913 0.0468  0.0350  0.0118  158 MET   A N   
2388 C  CA  . MET   A 158 ? 0.4238 0.2395 0.3678 0.0346  0.0347  0.0099  158 MET   A CA  
2389 C  C   . MET   A 158 ? 0.3723 0.2056 0.3238 0.0260  0.0281  0.0032  158 MET   A C   
2390 O  O   . MET   A 158 ? 0.3940 0.2256 0.3497 0.0156  0.0279  -0.0013 158 MET   A O   
2391 C  CB  . MET   A 158 ? 0.4940 0.3138 0.4370 0.0366  0.0347  0.0179  158 MET   A CB  
2392 C  CG  . MET   A 158 ? 0.7064 0.5361 0.6561 0.0260  0.0316  0.0165  158 MET   A CG  
2393 S  SD  . MET   A 158 ? 1.8298 1.6542 1.7763 0.0269  0.0357  0.0254  158 MET   A SD  
2394 C  CE  . MET   A 158 ? 0.6405 0.4864 0.5853 0.0374  0.0292  0.0305  158 MET   A CE  
2404 N  N   . MET   A 159 ? 0.3305 0.1816 0.2841 0.0304  0.0230  0.0028  159 MET   A N   
2405 C  CA  . MET   A 159 ? 0.2873 0.1547 0.2469 0.0237  0.0175  -0.0018 159 MET   A CA  
2406 C  C   . MET   A 159 ? 0.3011 0.1754 0.2603 0.0273  0.0160  -0.0061 159 MET   A C   
2407 O  O   . MET   A 159 ? 0.2959 0.1725 0.2529 0.0364  0.0170  -0.0038 159 MET   A O   
2408 C  CB  . MET   A 159 ? 0.3055 0.1904 0.2697 0.0230  0.0128  0.0018  159 MET   A CB  
2409 C  CG  . MET   A 159 ? 0.3963 0.2776 0.3613 0.0189  0.0137  0.0056  159 MET   A CG  
2410 S  SD  . MET   A 159 ? 0.5481 0.4478 0.5162 0.0215  0.0091  0.0102  159 MET   A SD  
2411 C  CE  . MET   A 159 ? 0.6539 0.5473 0.6221 0.0159  0.0112  0.0133  159 MET   A CE  
2421 N  N   . TYR   A 160 ? 0.2499 0.1293 0.2111 0.0208  0.0137  -0.0121 160 TYR   A N   
2422 C  CA  . TYR   A 160 ? 0.2509 0.1417 0.2124 0.0231  0.0117  -0.0151 160 TYR   A CA  
2423 C  C   . TYR   A 160 ? 0.2405 0.1490 0.2069 0.0246  0.0084  -0.0109 160 TYR   A C   
2424 O  O   . TYR   A 160 ? 0.2374 0.1501 0.2069 0.0225  0.0067  -0.0070 160 TYR   A O   
2425 C  CB  . TYR   A 160 ? 0.2458 0.1386 0.2074 0.0157  0.0097  -0.0218 160 TYR   A CB  
2426 C  CG  . TYR   A 160 ? 0.2551 0.1326 0.2126 0.0136  0.0126  -0.0284 160 TYR   A CG  
2427 C  CD1 . TYR   A 160 ? 0.2824 0.1554 0.2350 0.0188  0.0147  -0.0325 160 TYR   A CD1 
2428 C  CD2 . TYR   A 160 ? 0.2794 0.1474 0.2385 0.0061  0.0136  -0.0313 160 TYR   A CD2 
2429 C  CE1 . TYR   A 160 ? 0.3372 0.1953 0.2859 0.0165  0.0175  -0.0399 160 TYR   A CE1 
2430 C  CE2 . TYR   A 160 ? 0.3086 0.1624 0.2651 0.0032  0.0166  -0.0385 160 TYR   A CE2 
2431 C  CZ  . TYR   A 160 ? 0.3128 0.1606 0.2638 0.0084  0.0187  -0.0428 160 TYR   A CZ  
2432 O  OH  . TYR   A 160 ? 0.3635 0.1959 0.3117 0.0051  0.0220  -0.0513 160 TYR   A OH  
2442 N  N   . PRO   A 161 ? 0.2133 0.1328 0.1808 0.0272  0.0077  -0.0121 161 PRO   A N   
2443 C  CA  . PRO   A 161 ? 0.1914 0.1272 0.1647 0.0265  0.0053  -0.0092 161 PRO   A CA  
2444 C  C   . PRO   A 161 ? 0.2038 0.1428 0.1799 0.0190  0.0025  -0.0086 161 PRO   A C   
2445 O  O   . PRO   A 161 ? 0.2010 0.1362 0.1750 0.0141  0.0017  -0.0117 161 PRO   A O   
2446 C  CB  . PRO   A 161 ? 0.1999 0.1434 0.1728 0.0286  0.0064  -0.0117 161 PRO   A CB  
2447 C  CG  . PRO   A 161 ? 0.2036 0.1371 0.1710 0.0352  0.0096  -0.0142 161 PRO   A CG  
2448 C  CD  . PRO   A 161 ? 0.2086 0.1258 0.1720 0.0312  0.0099  -0.0162 161 PRO   A CD  
2456 N  N   . LEU   A 162 ? 0.1825 0.1300 0.1633 0.0186  0.0008  -0.0051 162 LEU   A N   
2457 C  CA  . LEU   A 162 ? 0.2081 0.1573 0.1913 0.0126  -0.0015 -0.0040 162 LEU   A CA  
2458 C  C   . LEU   A 162 ? 0.2129 0.1708 0.1985 0.0090  -0.0026 -0.0046 162 LEU   A C   
2459 O  O   . LEU   A 162 ? 0.2686 0.2335 0.2584 0.0071  -0.0038 -0.0027 162 LEU   A O   
2460 C  CB  . LEU   A 162 ? 0.2199 0.1729 0.2058 0.0145  -0.0025 -0.0004 162 LEU   A CB  
2461 C  CG  . LEU   A 162 ? 0.2326 0.1756 0.2147 0.0179  -0.0011 0.0019  162 LEU   A CG  
2462 C  CD1 . LEU   A 162 ? 0.3465 0.2772 0.3259 0.0129  0.0003  0.0007  162 LEU   A CD1 
2463 C  CD2 . LEU   A 162 ? 0.2493 0.1882 0.2282 0.0254  0.0012  0.0026  162 LEU   A CD2 
2475 N  N   . VAL   A 163 ? 0.2447 0.2018 0.2271 0.0086  -0.0019 -0.0072 163 VAL   A N   
2476 C  CA  . VAL   A 163 ? 0.2189 0.1831 0.2017 0.0067  -0.0019 -0.0069 163 VAL   A CA  
2477 C  C   . VAL   A 163 ? 0.2522 0.2125 0.2302 0.0043  -0.0033 -0.0099 163 VAL   A C   
2478 O  O   . VAL   A 163 ? 0.2889 0.2449 0.2624 0.0059  -0.0026 -0.0136 163 VAL   A O   
2479 C  CB  . VAL   A 163 ? 0.2306 0.2005 0.2133 0.0100  0.0009  -0.0069 163 VAL   A CB  
2480 C  CG1 . VAL   A 163 ? 0.2962 0.2717 0.2789 0.0077  0.0018  -0.0051 163 VAL   A CG1 
2481 C  CG2 . VAL   A 163 ? 0.2394 0.2159 0.2283 0.0127  0.0020  -0.0053 163 VAL   A CG2 
2491 N  N   . SER   A 164 ? 0.2188 0.1806 0.1980 0.0008  -0.0054 -0.0090 164 SER   A N   
2492 C  CA  . SER   A 164 ? 0.2288 0.1911 0.2050 -0.0015 -0.0075 -0.0119 164 SER   A CA  
2493 C  C   . SER   A 164 ? 0.2122 0.1803 0.1900 -0.0027 -0.0086 -0.0085 164 SER   A C   
2494 O  O   . SER   A 164 ? 0.2029 0.1724 0.1847 -0.0031 -0.0078 -0.0049 164 SER   A O   
2495 C  CB  . SER   A 164 ? 0.2380 0.1941 0.2150 -0.0047 -0.0087 -0.0153 164 SER   A CB  
2496 O  OG  . SER   A 164 ? 0.2452 0.2017 0.2270 -0.0072 -0.0094 -0.0119 164 SER   A OG  
2502 N  N   . LEU   A 165 ? 0.2098 0.1815 0.1844 -0.0030 -0.0106 -0.0101 165 LEU   A N   
2503 C  CA  A LEU   A 165 ? 0.1936 0.1695 0.1689 -0.0030 -0.0112 -0.0065 165 LEU   A CA  
2504 C  CA  B LEU   A 165 ? 0.1933 0.1692 0.1686 -0.0029 -0.0112 -0.0065 165 LEU   A CA  
2505 C  C   . LEU   A 165 ? 0.1960 0.1708 0.1772 -0.0060 -0.0122 -0.0050 165 LEU   A C   
2506 O  O   . LEU   A 165 ? 0.2040 0.1796 0.1876 -0.0059 -0.0113 -0.0013 165 LEU   A O   
2507 C  CB  A LEU   A 165 ? 0.2498 0.2314 0.2206 -0.0017 -0.0139 -0.0087 165 LEU   A CB  
2508 C  CB  B LEU   A 165 ? 0.2534 0.2348 0.2239 -0.0015 -0.0138 -0.0088 165 LEU   A CB  
2509 C  CG  A LEU   A 165 ? 0.2390 0.2240 0.2019 0.0029  -0.0131 -0.0088 165 LEU   A CG  
2510 C  CG  B LEU   A 165 ? 0.2278 0.2134 0.1974 0.0004  -0.0143 -0.0049 165 LEU   A CG  
2511 C  CD1 A LEU   A 165 ? 0.2041 0.1970 0.1624 0.0055  -0.0165 -0.0101 165 LEU   A CD1 
2512 C  CD1 B LEU   A 165 ? 0.2360 0.2189 0.2044 0.0026  -0.0100 0.0010  165 LEU   A CD1 
2513 C  CD2 A LEU   A 165 ? 0.2624 0.2455 0.2239 0.0054  -0.0086 -0.0029 165 LEU   A CD2 
2514 C  CD2 B LEU   A 165 ? 0.2549 0.2481 0.2186 0.0036  -0.0172 -0.0075 165 LEU   A CD2 
2536 N  N   . GLY   A 166 ? 0.1899 0.1624 0.1734 -0.0089 -0.0137 -0.0080 166 GLY   A N   
2537 C  CA  . GLY   A 166 ? 0.1945 0.1665 0.1828 -0.0113 -0.0141 -0.0063 166 GLY   A CA  
2538 C  C   . GLY   A 166 ? 0.1940 0.1629 0.1845 -0.0106 -0.0123 -0.0031 166 GLY   A C   
2539 O  O   . GLY   A 166 ? 0.1925 0.1631 0.1856 -0.0109 -0.0124 -0.0006 166 GLY   A O   
2543 N  N   . VAL   A 167 ? 0.1873 0.1523 0.1768 -0.0090 -0.0108 -0.0037 167 VAL   A N   
2544 C  CA  . VAL   A 167 ? 0.1916 0.1565 0.1835 -0.0073 -0.0098 -0.0013 167 VAL   A CA  
2545 C  C   . VAL   A 167 ? 0.1783 0.1487 0.1722 -0.0067 -0.0092 0.0004  167 VAL   A C   
2546 O  O   . VAL   A 167 ? 0.1802 0.1532 0.1776 -0.0071 -0.0093 0.0017  167 VAL   A O   
2547 C  CB  . VAL   A 167 ? 0.1961 0.1568 0.1863 -0.0043 -0.0082 -0.0021 167 VAL   A CB  
2548 C  CG1 . VAL   A 167 ? 0.2345 0.1986 0.2275 -0.0016 -0.0079 0.0001  167 VAL   A CG1 
2549 C  CG2 . VAL   A 167 ? 0.2725 0.2249 0.2609 -0.0053 -0.0076 -0.0035 167 VAL   A CG2 
2559 N  N   . GLY   A 168 ? 0.1914 0.1635 0.1831 -0.0058 -0.0080 0.0002  168 GLY   A N   
2560 C  CA  . GLY   A 168 ? 0.1941 0.1696 0.1879 -0.0060 -0.0060 0.0022  168 GLY   A CA  
2561 C  C   . GLY   A 168 ? 0.1712 0.1466 0.1662 -0.0077 -0.0066 0.0038  168 GLY   A C   
2562 O  O   . GLY   A 168 ? 0.1943 0.1709 0.1933 -0.0090 -0.0054 0.0046  168 GLY   A O   
2566 N  N   . GLY   A 169 ? 0.1742 0.1489 0.1662 -0.0077 -0.0084 0.0037  169 GLY   A N   
2567 C  CA  . GLY   A 169 ? 0.1776 0.1525 0.1705 -0.0082 -0.0090 0.0053  169 GLY   A CA  
2568 C  C   . GLY   A 169 ? 0.1824 0.1572 0.1795 -0.0100 -0.0099 0.0049  169 GLY   A C   
2569 O  O   . GLY   A 169 ? 0.1855 0.1601 0.1847 -0.0106 -0.0091 0.0058  169 GLY   A O   
2573 N  N   . HIS   A 170 ? 0.1713 0.1456 0.1691 -0.0105 -0.0112 0.0036  170 HIS   A N   
2574 C  CA  . HIS   A 170 ? 0.1593 0.1339 0.1596 -0.0111 -0.0118 0.0038  170 HIS   A CA  
2575 C  C   . HIS   A 170 ? 0.1510 0.1281 0.1542 -0.0108 -0.0110 0.0035  170 HIS   A C   
2576 O  O   . HIS   A 170 ? 0.1564 0.1349 0.1616 -0.0115 -0.0113 0.0032  170 HIS   A O   
2577 C  CB  . HIS   A 170 ? 0.1637 0.1354 0.1628 -0.0107 -0.0121 0.0033  170 HIS   A CB  
2578 C  CG  . HIS   A 170 ? 0.1605 0.1322 0.1601 -0.0099 -0.0122 0.0044  170 HIS   A CG  
2579 N  ND1 . HIS   A 170 ? 0.1575 0.1271 0.1565 -0.0109 -0.0119 0.0053  170 HIS   A ND1 
2580 C  CD2 . HIS   A 170 ? 0.1700 0.1446 0.1706 -0.0077 -0.0124 0.0046  170 HIS   A CD2 
2581 C  CE1 . HIS   A 170 ? 0.1512 0.1215 0.1495 -0.0088 -0.0117 0.0067  170 HIS   A CE1 
2582 N  NE2 . HIS   A 170 ? 0.1578 0.1318 0.1570 -0.0067 -0.0125 0.0059  170 HIS   A NE2 
2590 N  N   . GLU   A 171 ? 0.1461 0.1247 0.1502 -0.0098 -0.0100 0.0029  171 GLU   A N   
2591 C  CA  . GLU   A 171 ? 0.1413 0.1251 0.1500 -0.0100 -0.0096 0.0015  171 GLU   A CA  
2592 C  C   . GLU   A 171 ? 0.1352 0.1194 0.1470 -0.0127 -0.0075 0.0010  171 GLU   A C   
2593 O  O   . GLU   A 171 ? 0.1440 0.1315 0.1599 -0.0142 -0.0078 -0.0011 171 GLU   A O   
2594 C  CB  . GLU   A 171 ? 0.1666 0.1538 0.1765 -0.0079 -0.0087 0.0007  171 GLU   A CB  
2595 C  CG  . GLU   A 171 ? 0.2081 0.1927 0.2144 -0.0044 -0.0098 0.0013  171 GLU   A CG  
2596 C  CD  . GLU   A 171 ? 0.2701 0.2548 0.2753 -0.0026 -0.0115 0.0019  171 GLU   A CD  
2597 O  OE1 . GLU   A 171 ? 0.2365 0.2255 0.2440 -0.0033 -0.0127 0.0012  171 GLU   A OE1 
2598 O  OE2 . GLU   A 171 ? 0.2611 0.2396 0.2621 -0.0004 -0.0112 0.0033  171 GLU   A OE2 
2605 N  N   . VAL   A 172 ? 0.1456 0.1263 0.1553 -0.0131 -0.0051 0.0028  172 VAL   A N   
2606 C  CA  . VAL   A 172 ? 0.1503 0.1285 0.1620 -0.0153 -0.0019 0.0033  172 VAL   A CA  
2607 C  C   . VAL   A 172 ? 0.1414 0.1168 0.1529 -0.0159 -0.0030 0.0031  172 VAL   A C   
2608 O  O   . VAL   A 172 ? 0.1566 0.1306 0.1716 -0.0183 -0.0011 0.0015  172 VAL   A O   
2609 C  CB  . VAL   A 172 ? 0.1623 0.1362 0.1690 -0.0138 0.0011  0.0066  172 VAL   A CB  
2610 C  CG1 . VAL   A 172 ? 0.1915 0.1598 0.1986 -0.0152 0.0054  0.0085  172 VAL   A CG1 
2611 C  CG2 . VAL   A 172 ? 0.1650 0.1420 0.1720 -0.0131 0.0032  0.0066  172 VAL   A CG2 
2621 N  N   . SER   A 173 ? 0.1381 0.1126 0.1457 -0.0140 -0.0058 0.0041  173 SER   A N   
2622 C  CA  . SER   A 173 ? 0.1520 0.1246 0.1590 -0.0138 -0.0065 0.0042  173 SER   A CA  
2623 C  C   . SER   A 173 ? 0.1484 0.1241 0.1586 -0.0149 -0.0080 0.0012  173 SER   A C   
2624 O  O   . SER   A 173 ? 0.1530 0.1270 0.1634 -0.0151 -0.0077 0.0003  173 SER   A O   
2625 C  CB  . SER   A 173 ? 0.1600 0.1329 0.1633 -0.0118 -0.0086 0.0058  173 SER   A CB  
2626 O  OG  . SER   A 173 ? 0.1634 0.1348 0.1632 -0.0099 -0.0075 0.0080  173 SER   A OG  
2632 N  N   . HIS   A 174 ? 0.1324 0.1133 0.1447 -0.0149 -0.0095 -0.0006 174 HIS   A N   
2633 C  CA  . HIS   A 174 ? 0.1388 0.1247 0.1538 -0.0153 -0.0110 -0.0041 174 HIS   A CA  
2634 C  C   . HIS   A 174 ? 0.1336 0.1195 0.1537 -0.0188 -0.0088 -0.0076 174 HIS   A C   
2635 O  O   . HIS   A 174 ? 0.1445 0.1317 0.1661 -0.0197 -0.0095 -0.0111 174 HIS   A O   
2636 C  CB  . HIS   A 174 ? 0.1446 0.1372 0.1606 -0.0134 -0.0130 -0.0050 174 HIS   A CB  
2637 C  CG  . HIS   A 174 ? 0.1337 0.1254 0.1447 -0.0100 -0.0147 -0.0024 174 HIS   A CG  
2638 N  ND1 . HIS   A 174 ? 0.1548 0.1458 0.1628 -0.0088 -0.0156 -0.0017 174 HIS   A ND1 
2639 C  CD2 . HIS   A 174 ? 0.1337 0.1240 0.1422 -0.0076 -0.0147 -0.0003 174 HIS   A CD2 
2640 C  CE1 . HIS   A 174 ? 0.1616 0.1505 0.1657 -0.0063 -0.0157 0.0011  174 HIS   A CE1 
2641 N  NE2 . HIS   A 174 ? 0.1732 0.1611 0.1775 -0.0055 -0.0152 0.0019  174 HIS   A NE2 
2649 N  N   . GLY   A 175 ? 0.1388 0.1228 0.1616 -0.0209 -0.0056 -0.0070 175 GLY   A N   
2650 C  CA  . GLY   A 175 ? 0.1668 0.1487 0.1950 -0.0252 -0.0019 -0.0100 175 GLY   A CA  
2651 C  C   . GLY   A 175 ? 0.1448 0.1162 0.1696 -0.0252 0.0007  -0.0083 175 GLY   A C   
2652 O  O   . GLY   A 175 ? 0.1683 0.1370 0.1964 -0.0280 0.0024  -0.0122 175 GLY   A O   
2656 N  N   . PHE   A 176 ? 0.1577 0.1237 0.1762 -0.0217 0.0011  -0.0030 176 PHE   A N   
2657 C  CA  . PHE   A 176 ? 0.1686 0.1263 0.1833 -0.0198 0.0031  -0.0008 176 PHE   A CA  
2658 C  C   . PHE   A 176 ? 0.1636 0.1225 0.1784 -0.0194 0.0006  -0.0042 176 PHE   A C   
2659 O  O   . PHE   A 176 ? 0.1698 0.1226 0.1855 -0.0204 0.0032  -0.0065 176 PHE   A O   
2660 C  CB  . PHE   A 176 ? 0.1717 0.1281 0.1800 -0.0153 0.0022  0.0045  176 PHE   A CB  
2661 C  CG  . PHE   A 176 ? 0.1764 0.1256 0.1803 -0.0117 0.0043  0.0073  176 PHE   A CG  
2662 C  CD1 . PHE   A 176 ? 0.1878 0.1284 0.1888 -0.0103 0.0094  0.0108  176 PHE   A CD1 
2663 C  CD2 . PHE   A 176 ? 0.1986 0.1500 0.2010 -0.0092 0.0016  0.0068  176 PHE   A CD2 
2664 C  CE1 . PHE   A 176 ? 0.2113 0.1448 0.2075 -0.0056 0.0116  0.0140  176 PHE   A CE1 
2665 C  CE2 . PHE   A 176 ? 0.1996 0.1452 0.1983 -0.0049 0.0037  0.0094  176 PHE   A CE2 
2666 C  CZ  . PHE   A 176 ? 0.2173 0.1538 0.2125 -0.0027 0.0085  0.0130  176 PHE   A CZ  
2676 N  N   . THR   A 177 ? 0.1528 0.1194 0.1669 -0.0179 -0.0038 -0.0050 177 THR   A N   
2677 C  CA  . THR   A 177 ? 0.1448 0.1138 0.1581 -0.0169 -0.0059 -0.0079 177 THR   A CA  
2678 C  C   . THR   A 177 ? 0.1428 0.1140 0.1608 -0.0203 -0.0056 -0.0145 177 THR   A C   
2679 O  O   . THR   A 177 ? 0.1668 0.1347 0.1845 -0.0205 -0.0048 -0.0177 177 THR   A O   
2680 C  CB  . THR   A 177 ? 0.1472 0.1231 0.1581 -0.0146 -0.0096 -0.0065 177 THR   A CB  
2681 O  OG1 . THR   A 177 ? 0.1599 0.1338 0.1678 -0.0125 -0.0094 -0.0020 177 THR   A OG1 
2682 C  CG2 . THR   A 177 ? 0.1684 0.1482 0.1778 -0.0131 -0.0114 -0.0092 177 THR   A CG2 
2690 N  N   . GLU   A 178 ? 0.1429 0.1210 0.1656 -0.0228 -0.0066 -0.0173 178 GLU   A N   
2691 C  CA  A GLU   A 178 ? 0.1654 0.1488 0.1939 -0.0264 -0.0070 -0.0249 178 GLU   A CA  
2692 C  CA  B GLU   A 178 ? 0.1654 0.1488 0.1939 -0.0264 -0.0070 -0.0249 178 GLU   A CA  
2693 C  C   . GLU   A 178 ? 0.1755 0.1491 0.2072 -0.0306 -0.0021 -0.0279 178 GLU   A C   
2694 O  O   . GLU   A 178 ? 0.1859 0.1604 0.2202 -0.0329 -0.0023 -0.0349 178 GLU   A O   
2695 C  CB  A GLU   A 178 ? 0.1619 0.1552 0.1961 -0.0282 -0.0081 -0.0269 178 GLU   A CB  
2696 C  CB  B GLU   A 178 ? 0.1622 0.1555 0.1965 -0.0282 -0.0081 -0.0269 178 GLU   A CB  
2697 C  CG  A GLU   A 178 ? 0.1645 0.1679 0.2063 -0.0320 -0.0096 -0.0361 178 GLU   A CG  
2698 C  CG  B GLU   A 178 ? 0.1646 0.1678 0.2066 -0.0322 -0.0094 -0.0361 178 GLU   A CG  
2699 C  CD  A GLU   A 178 ? 0.2496 0.2654 0.2972 -0.0324 -0.0112 -0.0376 178 GLU   A CD  
2700 C  CD  B GLU   A 178 ? 0.2495 0.2652 0.2972 -0.0325 -0.0111 -0.0375 178 GLU   A CD  
2701 O  OE1 A GLU   A 178 ? 0.2486 0.2716 0.2922 -0.0269 -0.0150 -0.0347 178 GLU   A OE1 
2702 O  OE1 B GLU   A 178 ? 0.2487 0.2716 0.2923 -0.0270 -0.0149 -0.0347 178 GLU   A OE1 
2703 O  OE2 A GLU   A 178 ? 0.4125 0.4307 0.4689 -0.0381 -0.0080 -0.0415 178 GLU   A OE2 
2704 O  OE2 B GLU   A 178 ? 0.4125 0.4305 0.4689 -0.0381 -0.0079 -0.0413 178 GLU   A OE2 
2716 N  N   . GLN   A 179 ? 0.1627 0.1261 0.1934 -0.0311 0.0027  -0.0228 179 GLN   A N   
2717 C  CA  . GLN   A 179 ? 0.1712 0.1226 0.2048 -0.0352 0.0092  -0.0243 179 GLN   A CA  
2718 C  C   . GLN   A 179 ? 0.1876 0.1272 0.2147 -0.0313 0.0112  -0.0218 179 GLN   A C   
2719 O  O   . GLN   A 179 ? 0.2314 0.1584 0.2594 -0.0335 0.0172  -0.0228 179 GLN   A O   
2720 C  CB  . GLN   A 179 ? 0.1839 0.1311 0.2187 -0.0367 0.0139  -0.0192 179 GLN   A CB  
2721 C  CG  . GLN   A 179 ? 0.1796 0.1386 0.2226 -0.0411 0.0131  -0.0230 179 GLN   A CG  
2722 C  CD  . GLN   A 179 ? 0.2144 0.1705 0.2577 -0.0417 0.0178  -0.0176 179 GLN   A CD  
2723 O  OE1 . GLN   A 179 ? 0.2107 0.1556 0.2475 -0.0388 0.0218  -0.0108 179 GLN   A OE1 
2724 N  NE2 . GLN   A 179 ? 0.2597 0.2271 0.3104 -0.0449 0.0173  -0.0205 179 GLN   A NE2 
2733 N  N   . HIS   A 180 ? 0.1876 0.1309 0.2086 -0.0256 0.0070  -0.0187 180 HIS   A N   
2734 C  CA  . HIS   A 180 ? 0.1860 0.1212 0.2013 -0.0208 0.0084  -0.0164 180 HIS   A CA  
2735 C  C   . HIS   A 180 ? 0.1798 0.1213 0.1940 -0.0192 0.0046  -0.0212 180 HIS   A C   
2736 O  O   . HIS   A 180 ? 0.2304 0.1698 0.2473 -0.0222 0.0056  -0.0285 180 HIS   A O   
2737 C  CB  . HIS   A 180 ? 0.1988 0.1332 0.2085 -0.0153 0.0081  -0.0081 180 HIS   A CB  
2738 C  CG  . HIS   A 180 ? 0.2055 0.1309 0.2139 -0.0152 0.0131  -0.0033 180 HIS   A CG  
2739 N  ND1 . HIS   A 180 ? 0.2137 0.1428 0.2238 -0.0173 0.0133  -0.0011 180 HIS   A ND1 
2740 C  CD2 . HIS   A 180 ? 0.2260 0.1384 0.2307 -0.0124 0.0187  0.0001  180 HIS   A CD2 
2741 C  CE1 . HIS   A 180 ? 0.2244 0.1434 0.2316 -0.0160 0.0190  0.0036  180 HIS   A CE1 
2742 N  NE2 . HIS   A 180 ? 0.2502 0.1585 0.2537 -0.0128 0.0224  0.0048  180 HIS   A NE2 
2750 N  N   . SER   A 181 ? 0.1733 0.1224 0.1836 -0.0149 0.0007  -0.0178 181 SER   A N   
2751 C  CA  . SER   A 181 ? 0.1931 0.1487 0.2012 -0.0126 -0.0023 -0.0213 181 SER   A CA  
2752 C  C   . SER   A 181 ? 0.1866 0.1511 0.1977 -0.0158 -0.0054 -0.0278 181 SER   A C   
2753 O  O   . SER   A 181 ? 0.1944 0.1618 0.2041 -0.0149 -0.0066 -0.0334 181 SER   A O   
2754 C  CB  . SER   A 181 ? 0.1843 0.1465 0.1889 -0.0084 -0.0047 -0.0158 181 SER   A CB  
2755 O  OG  . SER   A 181 ? 0.1872 0.1559 0.1930 -0.0098 -0.0072 -0.0135 181 SER   A OG  
2761 N  N   . GLY   A 182 ? 0.1649 0.1351 0.1797 -0.0184 -0.0068 -0.0274 182 GLY   A N   
2762 C  CA  . GLY   A 182 ? 0.1596 0.1411 0.1770 -0.0198 -0.0105 -0.0331 182 GLY   A CA  
2763 C  C   . GLY   A 182 ? 0.1564 0.1468 0.1683 -0.0149 -0.0143 -0.0313 182 GLY   A C   
2764 O  O   . GLY   A 182 ? 0.1748 0.1748 0.1866 -0.0142 -0.0175 -0.0366 182 GLY   A O   
2768 N  N   . LEU   A 183 ? 0.1687 0.1569 0.1763 -0.0116 -0.0140 -0.0241 183 LEU   A N   
2769 C  CA  . LEU   A 183 ? 0.1567 0.1514 0.1590 -0.0074 -0.0162 -0.0213 183 LEU   A CA  
2770 C  C   . LEU   A 183 ? 0.1663 0.1704 0.1691 -0.0065 -0.0193 -0.0232 183 LEU   A C   
2771 O  O   . LEU   A 183 ? 0.1631 0.1679 0.1692 -0.0080 -0.0196 -0.0215 183 LEU   A O   
2772 C  CB  . LEU   A 183 ? 0.1505 0.1420 0.1511 -0.0061 -0.0150 -0.0138 183 LEU   A CB  
2773 C  CG  . LEU   A 183 ? 0.1742 0.1605 0.1737 -0.0051 -0.0126 -0.0111 183 LEU   A CG  
2774 C  CD1 . LEU   A 183 ? 0.1618 0.1467 0.1620 -0.0054 -0.0120 -0.0055 183 LEU   A CD1 
2775 C  CD2 . LEU   A 183 ? 0.1918 0.1816 0.1872 -0.0018 -0.0124 -0.0117 183 LEU   A CD2 
2787 N  N   . GLU   A 184 ? 0.1781 0.1899 0.1768 -0.0030 -0.0216 -0.0262 184 GLU   A N   
2788 C  CA  . GLU   A 184 ? 0.1801 0.2027 0.1785 -0.0006 -0.0250 -0.0286 184 GLU   A CA  
2789 C  C   . GLU   A 184 ? 0.1909 0.2136 0.1843 0.0038  -0.0249 -0.0208 184 GLU   A C   
2790 O  O   . GLU   A 184 ? 0.1845 0.2017 0.1730 0.0058  -0.0226 -0.0150 184 GLU   A O   
2791 C  CB  . GLU   A 184 ? 0.2085 0.2403 0.2032 0.0024  -0.0278 -0.0354 184 GLU   A CB  
2792 C  CG  . GLU   A 184 ? 0.2549 0.2856 0.2548 -0.0025 -0.0276 -0.0448 184 GLU   A CG  
2793 C  CD  . GLU   A 184 ? 0.5199 0.5545 0.5298 -0.0085 -0.0283 -0.0514 184 GLU   A CD  
2794 O  OE1 . GLU   A 184 ? 0.5640 0.6017 0.5780 -0.0093 -0.0287 -0.0485 184 GLU   A OE1 
2795 O  OE2 . GLU   A 184 ? 0.5672 0.6022 0.5811 -0.0125 -0.0282 -0.0605 184 GLU   A OE2 
2802 N  N   . TYR   A 185 ? 0.1751 0.2040 0.1701 0.0055  -0.0269 -0.0208 185 TYR   A N   
2803 C  CA  . TYR   A 185 ? 0.1579 0.1837 0.1494 0.0089  -0.0258 -0.0134 185 TYR   A CA  
2804 C  C   . TYR   A 185 ? 0.1726 0.2019 0.1546 0.0167  -0.0262 -0.0094 185 TYR   A C   
2805 O  O   . TYR   A 185 ? 0.1869 0.2199 0.1660 0.0218  -0.0272 -0.0067 185 TYR   A O   
2806 C  CB  . TYR   A 185 ? 0.1608 0.1902 0.1582 0.0077  -0.0269 -0.0147 185 TYR   A CB  
2807 C  CG  . TYR   A 185 ? 0.1556 0.1772 0.1516 0.0086  -0.0246 -0.0081 185 TYR   A CG  
2808 C  CD1 . TYR   A 185 ? 0.1702 0.1818 0.1682 0.0039  -0.0219 -0.0055 185 TYR   A CD1 
2809 C  CD2 . TYR   A 185 ? 0.1698 0.1941 0.1618 0.0146  -0.0252 -0.0048 185 TYR   A CD2 
2810 C  CE1 . TYR   A 185 ? 0.1708 0.1755 0.1679 0.0041  -0.0200 -0.0009 185 TYR   A CE1 
2811 C  CE2 . TYR   A 185 ? 0.1757 0.1911 0.1665 0.0150  -0.0226 0.0003  185 TYR   A CE2 
2812 C  CZ  . TYR   A 185 ? 0.1799 0.1859 0.1733 0.0094  -0.0202 0.0017  185 TYR   A CZ  
2813 O  OH  . TYR   A 185 ? 0.1902 0.1880 0.1822 0.0096  -0.0179 0.0056  185 TYR   A OH  
2823 N  N   . PHE   A 186 ? 0.1667 0.1949 0.1430 0.0185  -0.0251 -0.0086 186 PHE   A N   
2824 C  CA  . PHE   A 186 ? 0.1739 0.2038 0.1400 0.0260  -0.0240 -0.0036 186 PHE   A CA  
2825 C  C   . PHE   A 186 ? 0.1788 0.2031 0.1416 0.0249  -0.0205 -0.0012 186 PHE   A C   
2826 O  O   . PHE   A 186 ? 0.1791 0.2012 0.1468 0.0199  -0.0203 -0.0050 186 PHE   A O   
2827 C  CB  . PHE   A 186 ? 0.1835 0.2277 0.1451 0.0325  -0.0285 -0.0085 186 PHE   A CB  
2828 C  CG  . PHE   A 186 ? 0.1933 0.2444 0.1563 0.0305  -0.0310 -0.0171 186 PHE   A CG  
2829 C  CD1 . PHE   A 186 ? 0.2055 0.2607 0.1782 0.0242  -0.0336 -0.0260 186 PHE   A CD1 
2830 C  CD2 . PHE   A 186 ? 0.2327 0.2853 0.1870 0.0349  -0.0299 -0.0166 186 PHE   A CD2 
2831 C  CE1 . PHE   A 186 ? 0.2210 0.2808 0.1947 0.0222  -0.0352 -0.0347 186 PHE   A CE1 
2832 C  CE2 . PHE   A 186 ? 0.2445 0.3031 0.1992 0.0336  -0.0320 -0.0254 186 PHE   A CE2 
2833 C  CZ  . PHE   A 186 ? 0.2226 0.2835 0.1875 0.0267  -0.0346 -0.0346 186 PHE   A CZ  
2843 N  N   . GLY   A 187 ? 0.1994 0.2216 0.1533 0.0303  -0.0173 0.0054  187 GLY   A N   
2844 C  CA  . GLY   A 187 ? 0.1966 0.2153 0.1474 0.0298  -0.0134 0.0078  187 GLY   A CA  
2845 C  C   . GLY   A 187 ? 0.1851 0.1955 0.1435 0.0225  -0.0103 0.0096  187 GLY   A C   
2846 O  O   . GLY   A 187 ? 0.1775 0.1822 0.1413 0.0186  -0.0098 0.0113  187 GLY   A O   
2850 N  N   . GLN   A 188 ? 0.1855 0.1964 0.1442 0.0213  -0.0084 0.0085  188 GLN   A N   
2851 C  CA  . GLN   A 188 ? 0.1783 0.1842 0.1442 0.0157  -0.0058 0.0098  188 GLN   A CA  
2852 C  C   . GLN   A 188 ? 0.1707 0.1748 0.1446 0.0109  -0.0089 0.0052  188 GLN   A C   
2853 O  O   . GLN   A 188 ? 0.1665 0.1662 0.1457 0.0069  -0.0080 0.0071  188 GLN   A O   
2854 C  CB  . GLN   A 188 ? 0.1809 0.1895 0.1451 0.0169  -0.0031 0.0094  188 GLN   A CB  
2855 C  CG  . GLN   A 188 ? 0.1857 0.1947 0.1428 0.0206  0.0021  0.0158  188 GLN   A CG  
2856 C  CD  . GLN   A 188 ? 0.2147 0.2278 0.1703 0.0222  0.0049  0.0152  188 GLN   A CD  
2857 O  OE1 . GLN   A 188 ? 0.1889 0.2026 0.1509 0.0191  0.0055  0.0132  188 GLN   A OE1 
2858 N  NE2 . GLN   A 188 ? 0.3493 0.3663 0.2951 0.0284  0.0069  0.0168  188 GLN   A NE2 
2867 N  N   . SER   A 189 ? 0.1737 0.1814 0.1482 0.0114  -0.0124 -0.0012 189 SER   A N   
2868 C  CA  . SER   A 189 ? 0.1613 0.1659 0.1429 0.0068  -0.0141 -0.0049 189 SER   A CA  
2869 C  C   . SER   A 189 ? 0.1418 0.1442 0.1264 0.0049  -0.0150 -0.0027 189 SER   A C   
2870 O  O   . SER   A 189 ? 0.1523 0.1505 0.1420 0.0012  -0.0147 -0.0026 189 SER   A O   
2871 C  CB  . SER   A 189 ? 0.1633 0.1712 0.1458 0.0067  -0.0166 -0.0127 189 SER   A CB  
2872 O  OG  . SER   A 189 ? 0.1915 0.2069 0.1716 0.0092  -0.0197 -0.0157 189 SER   A OG  
2878 N  N   . GLY   A 190 ? 0.1526 0.1582 0.1332 0.0083  -0.0160 -0.0011 190 GLY   A N   
2879 C  CA  . GLY   A 190 ? 0.1668 0.1705 0.1496 0.0075  -0.0166 0.0009  190 GLY   A CA  
2880 C  C   . GLY   A 190 ? 0.1559 0.1519 0.1395 0.0053  -0.0135 0.0063  190 GLY   A C   
2881 O  O   . GLY   A 190 ? 0.1590 0.1516 0.1465 0.0025  -0.0137 0.0066  190 GLY   A O   
2885 N  N   . GLY   A 191 ? 0.1690 0.1629 0.1490 0.0063  -0.0103 0.0103  191 GLY   A N   
2886 C  CA  . GLY   A 191 ? 0.1448 0.1328 0.1276 0.0028  -0.0072 0.0138  191 GLY   A CA  
2887 C  C   . GLY   A 191 ? 0.1454 0.1334 0.1347 -0.0017 -0.0080 0.0112  191 GLY   A C   
2888 O  O   . GLY   A 191 ? 0.1536 0.1384 0.1463 -0.0049 -0.0077 0.0118  191 GLY   A O   
2892 N  N   . MET   A 192 ? 0.1417 0.1331 0.1320 -0.0014 -0.0090 0.0083  192 MET   A N   
2893 C  CA  . MET   A 192 ? 0.1322 0.1231 0.1274 -0.0039 -0.0096 0.0065  192 MET   A CA  
2894 C  C   . MET   A 192 ? 0.1359 0.1243 0.1334 -0.0056 -0.0116 0.0047  192 MET   A C   
2895 O  O   . MET   A 192 ? 0.1403 0.1270 0.1406 -0.0074 -0.0116 0.0051  192 MET   A O   
2896 C  CB  . MET   A 192 ? 0.1456 0.1386 0.1403 -0.0022 -0.0096 0.0037  192 MET   A CB  
2897 C  CG  . MET   A 192 ? 0.1362 0.1327 0.1294 -0.0004 -0.0071 0.0055  192 MET   A CG  
2898 S  SD  . MET   A 192 ? 0.1769 0.1753 0.1681 0.0029  -0.0069 0.0015  192 MET   A SD  
2899 C  CE  . MET   A 192 ? 0.1871 0.1817 0.1829 0.0019  -0.0074 0.0001  192 MET   A CE  
2909 N  N   . ASN   A 193 ? 0.1379 0.1275 0.1343 -0.0045 -0.0132 0.0024  193 ASN   A N   
2910 C  CA  . ASN   A 193 ? 0.1406 0.1290 0.1400 -0.0063 -0.0144 0.0006  193 ASN   A CA  
2911 C  C   . ASN   A 193 ? 0.1375 0.1232 0.1373 -0.0072 -0.0139 0.0035  193 ASN   A C   
2912 O  O   . ASN   A 193 ? 0.1347 0.1180 0.1365 -0.0091 -0.0137 0.0036  193 ASN   A O   
2913 C  CB  . ASN   A 193 ? 0.1579 0.1512 0.1571 -0.0049 -0.0162 -0.0029 193 ASN   A CB  
2914 C  CG  . ASN   A 193 ? 0.1446 0.1388 0.1482 -0.0071 -0.0169 -0.0054 193 ASN   A CG  
2915 O  OD1 . ASN   A 193 ? 0.1656 0.1570 0.1701 -0.0079 -0.0162 -0.0030 193 ASN   A OD1 
2916 N  ND2 . ASN   A 193 ? 0.1551 0.1533 0.1617 -0.0082 -0.0178 -0.0105 193 ASN   A ND2 
2923 N  N   . GLU   A 194 ? 0.1310 0.1163 0.1277 -0.0053 -0.0134 0.0059  194 GLU   A N   
2924 C  CA  . GLU   A 194 ? 0.1368 0.1178 0.1334 -0.0063 -0.0124 0.0080  194 GLU   A CA  
2925 C  C   . GLU   A 194 ? 0.1387 0.1176 0.1376 -0.0095 -0.0113 0.0085  194 GLU   A C   
2926 O  O   . GLU   A 194 ? 0.1446 0.1215 0.1449 -0.0112 -0.0116 0.0079  194 GLU   A O   
2927 C  CB  . GLU   A 194 ? 0.1507 0.1295 0.1428 -0.0032 -0.0108 0.0111  194 GLU   A CB  
2928 C  CG  . GLU   A 194 ? 0.1647 0.1449 0.1548 0.0007  -0.0120 0.0110  194 GLU   A CG  
2929 C  CD  . GLU   A 194 ? 0.1725 0.1500 0.1651 -0.0008 -0.0122 0.0101  194 GLU   A CD  
2930 O  OE1 . GLU   A 194 ? 0.1929 0.1642 0.1857 -0.0031 -0.0105 0.0110  194 GLU   A OE1 
2931 O  OE2 . GLU   A 194 ? 0.1769 0.1594 0.1713 0.0007  -0.0141 0.0078  194 GLU   A OE2 
2938 N  N   . SER   A 195 ? 0.1305 0.1113 0.1298 -0.0100 -0.0102 0.0092  195 SER   A N   
2939 C  CA  A SER   A 195 ? 0.1427 0.1246 0.1453 -0.0128 -0.0097 0.0089  195 SER   A CA  
2940 C  CA  B SER   A 195 ? 0.1434 0.1253 0.1460 -0.0128 -0.0097 0.0089  195 SER   A CA  
2941 C  C   . SER   A 195 ? 0.1245 0.1081 0.1289 -0.0129 -0.0116 0.0072  195 SER   A C   
2942 O  O   . SER   A 195 ? 0.1343 0.1185 0.1401 -0.0145 -0.0121 0.0064  195 SER   A O   
2943 C  CB  A SER   A 195 ? 0.1446 0.1307 0.1484 -0.0127 -0.0081 0.0097  195 SER   A CB  
2944 C  CB  B SER   A 195 ? 0.1446 0.1303 0.1483 -0.0128 -0.0079 0.0098  195 SER   A CB  
2945 O  OG  A SER   A 195 ? 0.1243 0.1086 0.1261 -0.0126 -0.0051 0.0122  195 SER   A OG  
2946 O  OG  B SER   A 195 ? 0.1518 0.1413 0.1598 -0.0153 -0.0080 0.0088  195 SER   A OG  
2957 N  N   . PHE   A 196 ? 0.1267 0.1108 0.1305 -0.0111 -0.0122 0.0064  196 PHE   A N   
2958 C  CA  . PHE   A 196 ? 0.1344 0.1180 0.1388 -0.0106 -0.0127 0.0059  196 PHE   A CA  
2959 C  C   . PHE   A 196 ? 0.1212 0.1025 0.1250 -0.0115 -0.0132 0.0057  196 PHE   A C   
2960 O  O   . PHE   A 196 ? 0.1348 0.1167 0.1382 -0.0111 -0.0136 0.0059  196 PHE   A O   
2961 C  CB  . PHE   A 196 ? 0.1346 0.1161 0.1384 -0.0092 -0.0122 0.0048  196 PHE   A CB  
2962 C  CG  . PHE   A 196 ? 0.1354 0.1140 0.1389 -0.0081 -0.0113 0.0053  196 PHE   A CG  
2963 C  CD1 . PHE   A 196 ? 0.1519 0.1317 0.1547 -0.0054 -0.0109 0.0065  196 PHE   A CD1 
2964 C  CD2 . PHE   A 196 ? 0.1488 0.1238 0.1521 -0.0090 -0.0105 0.0053  196 PHE   A CD2 
2965 C  CE1 . PHE   A 196 ? 0.1681 0.1447 0.1689 -0.0029 -0.0098 0.0082  196 PHE   A CE1 
2966 C  CE2 . PHE   A 196 ? 0.1562 0.1276 0.1578 -0.0074 -0.0087 0.0070  196 PHE   A CE2 
2967 C  CZ  . PHE   A 196 ? 0.1528 0.1245 0.1525 -0.0039 -0.0084 0.0088  196 PHE   A CZ  
2977 N  N   . SER   A 197 ? 0.1370 0.1166 0.1404 -0.0118 -0.0132 0.0054  197 SER   A N   
2978 C  CA  . SER   A 197 ? 0.1435 0.1214 0.1464 -0.0122 -0.0132 0.0051  197 SER   A CA  
2979 C  C   . SER   A 197 ? 0.1293 0.1065 0.1315 -0.0134 -0.0135 0.0049  197 SER   A C   
2980 O  O   . SER   A 197 ? 0.1399 0.1167 0.1411 -0.0133 -0.0137 0.0042  197 SER   A O   
2981 C  CB  . SER   A 197 ? 0.1380 0.1159 0.1410 -0.0114 -0.0132 0.0046  197 SER   A CB  
2982 O  OG  . SER   A 197 ? 0.1492 0.1287 0.1542 -0.0115 -0.0130 0.0031  197 SER   A OG  
2988 N  N   . ASP   A 198 ? 0.1319 0.1088 0.1347 -0.0146 -0.0129 0.0053  198 ASP   A N   
2989 C  CA  . ASP   A 198 ? 0.1374 0.1138 0.1412 -0.0171 -0.0127 0.0038  198 ASP   A CA  
2990 C  C   . ASP   A 198 ? 0.1545 0.1371 0.1600 -0.0176 -0.0143 0.0022  198 ASP   A C   
2991 O  O   . ASP   A 198 ? 0.1463 0.1305 0.1519 -0.0188 -0.0153 -0.0003 198 ASP   A O   
2992 C  CB  . ASP   A 198 ? 0.1579 0.1317 0.1626 -0.0189 -0.0104 0.0048  198 ASP   A CB  
2993 C  CG  . ASP   A 198 ? 0.1527 0.1196 0.1542 -0.0173 -0.0087 0.0066  198 ASP   A CG  
2994 O  OD1 . ASP   A 198 ? 0.1763 0.1409 0.1758 -0.0152 -0.0095 0.0061  198 ASP   A OD1 
2995 O  OD2 . ASP   A 198 ? 0.1762 0.1396 0.1767 -0.0173 -0.0060 0.0089  198 ASP   A OD2 
3000 N  N   . MET   A 199 ? 0.1337 0.1203 0.1402 -0.0160 -0.0146 0.0034  199 MET   A N   
3001 C  CA  . MET   A 199 ? 0.1401 0.1335 0.1475 -0.0146 -0.0161 0.0026  199 MET   A CA  
3002 C  C   . MET   A 199 ? 0.1353 0.1277 0.1390 -0.0120 -0.0171 0.0027  199 MET   A C   
3003 O  O   . MET   A 199 ? 0.1475 0.1452 0.1504 -0.0111 -0.0188 0.0011  199 MET   A O   
3004 C  CB  . MET   A 199 ? 0.1460 0.1427 0.1544 -0.0121 -0.0158 0.0041  199 MET   A CB  
3005 C  CG  . MET   A 199 ? 0.1401 0.1388 0.1515 -0.0137 -0.0143 0.0044  199 MET   A CG  
3006 S  SD  . MET   A 199 ? 0.1636 0.1636 0.1742 -0.0095 -0.0135 0.0059  199 MET   A SD  
3007 C  CE  . MET   A 199 ? 0.1911 0.1903 0.2023 -0.0110 -0.0112 0.0066  199 MET   A CE  
3017 N  N   . ALA   A 200 ? 0.1395 0.1259 0.1408 -0.0108 -0.0157 0.0045  200 ALA   A N   
3018 C  CA  . ALA   A 200 ? 0.1416 0.1262 0.1393 -0.0085 -0.0152 0.0055  200 ALA   A CA  
3019 C  C   . ALA   A 200 ? 0.1405 0.1253 0.1364 -0.0094 -0.0160 0.0035  200 ALA   A C   
3020 O  O   . ALA   A 200 ? 0.1644 0.1508 0.1566 -0.0070 -0.0162 0.0036  200 ALA   A O   
3021 C  CB  . ALA   A 200 ? 0.1657 0.1448 0.1633 -0.0085 -0.0129 0.0070  200 ALA   A CB  
3027 N  N   . ALA   A 201 ? 0.1574 0.1399 0.1551 -0.0123 -0.0159 0.0017  201 ALA   A N   
3028 C  CA  . ALA   A 201 ? 0.1681 0.1496 0.1641 -0.0132 -0.0164 -0.0011 201 ALA   A CA  
3029 C  C   . ALA   A 201 ? 0.1636 0.1518 0.1595 -0.0136 -0.0187 -0.0043 201 ALA   A C   
3030 O  O   . ALA   A 201 ? 0.1781 0.1683 0.1704 -0.0122 -0.0198 -0.0066 201 ALA   A O   
3031 C  CB  . ALA   A 201 ? 0.1715 0.1477 0.1693 -0.0157 -0.0152 -0.0021 201 ALA   A CB  
3037 N  N   . GLN   A 202 ? 0.1573 0.1502 0.1575 -0.0156 -0.0196 -0.0053 202 GLN   A N   
3038 C  CA  . GLN   A 202 ? 0.1508 0.1534 0.1527 -0.0161 -0.0223 -0.0092 202 GLN   A CA  
3039 C  C   . GLN   A 202 ? 0.1529 0.1618 0.1502 -0.0103 -0.0240 -0.0076 202 GLN   A C   
3040 O  O   . GLN   A 202 ? 0.1656 0.1816 0.1605 -0.0088 -0.0266 -0.0110 202 GLN   A O   
3041 C  CB  . GLN   A 202 ? 0.1500 0.1581 0.1586 -0.0191 -0.0222 -0.0099 202 GLN   A CB  
3042 C  CG  . GLN   A 202 ? 0.1616 0.1629 0.1741 -0.0244 -0.0193 -0.0105 202 GLN   A CG  
3043 C  CD  . GLN   A 202 ? 0.1831 0.1803 0.1960 -0.0283 -0.0188 -0.0149 202 GLN   A CD  
3044 O  OE1 . GLN   A 202 ? 0.1864 0.1906 0.2015 -0.0306 -0.0209 -0.0206 202 GLN   A OE1 
3045 N  NE2 . GLN   A 202 ? 0.2441 0.2296 0.2546 -0.0289 -0.0159 -0.0129 202 GLN   A NE2 
3054 N  N   . ALA   A 203 ? 0.1487 0.1548 0.1443 -0.0068 -0.0225 -0.0025 203 ALA   A N   
3055 C  CA  . ALA   A 203 ? 0.1541 0.1632 0.1442 -0.0004 -0.0228 0.0004  203 ALA   A CA  
3056 C  C   . ALA   A 203 ? 0.1780 0.1842 0.1613 0.0021  -0.0222 0.0008  203 ALA   A C   
3057 O  O   . ALA   A 203 ? 0.1764 0.1886 0.1542 0.0071  -0.0236 0.0009  203 ALA   A O   
3058 C  CB  . ALA   A 203 ? 0.1830 0.1859 0.1727 0.0019  -0.0200 0.0052  203 ALA   A CB  
3064 N  N   . ALA   A 204 ? 0.1672 0.1650 0.1503 -0.0005 -0.0197 0.0014  204 ALA   A N   
3065 C  CA  . ALA   A 204 ? 0.1793 0.1748 0.1564 0.0019  -0.0183 0.0019  204 ALA   A CA  
3066 C  C   . ALA   A 204 ? 0.1911 0.1932 0.1656 0.0021  -0.0215 -0.0034 204 ALA   A C   
3067 O  O   . ALA   A 204 ? 0.2016 0.2074 0.1688 0.0070  -0.0218 -0.0030 204 ALA   A O   
3068 C  CB  . ALA   A 204 ? 0.1959 0.1835 0.1752 -0.0012 -0.0154 0.0025  204 ALA   A CB  
3074 N  N   . GLU   A 205 ? 0.1701 0.1741 0.1501 -0.0030 -0.0235 -0.0088 205 GLU   A N   
3075 C  CA  . GLU   A 205 ? 0.1740 0.1843 0.1528 -0.0041 -0.0265 -0.0156 205 GLU   A CA  
3076 C  C   . GLU   A 205 ? 0.1851 0.2088 0.1618 0.0000  -0.0303 -0.0174 205 GLU   A C   
3077 O  O   . GLU   A 205 ? 0.1992 0.2296 0.1697 0.0036  -0.0326 -0.0206 205 GLU   A O   
3078 C  CB  . GLU   A 205 ? 0.1979 0.2057 0.1843 -0.0114 -0.0267 -0.0206 205 GLU   A CB  
3079 C  CG  . GLU   A 205 ? 0.2345 0.2300 0.2209 -0.0138 -0.0234 -0.0200 205 GLU   A CG  
3080 C  CD  . GLU   A 205 ? 0.4327 0.4233 0.4252 -0.0201 -0.0224 -0.0238 205 GLU   A CD  
3081 O  OE1 . GLU   A 205 ? 0.2984 0.2953 0.2961 -0.0242 -0.0240 -0.0282 205 GLU   A OE1 
3082 O  OE2 . GLU   A 205 ? 0.2985 0.2787 0.2908 -0.0209 -0.0194 -0.0221 205 GLU   A OE2 
3089 N  N   . TYR   A 206 ? 0.1712 0.2004 0.1527 0.0003  -0.0314 -0.0156 206 TYR   A N   
3090 C  CA  . TYR   A 206 ? 0.1824 0.2262 0.1626 0.0052  -0.0352 -0.0171 206 TYR   A CA  
3091 C  C   . TYR   A 206 ? 0.1794 0.2234 0.1485 0.0147  -0.0344 -0.0114 206 TYR   A C   
3092 O  O   . TYR   A 206 ? 0.1901 0.2453 0.1534 0.0203  -0.0377 -0.0138 206 TYR   A O   
3093 C  CB  . TYR   A 206 ? 0.2020 0.2505 0.1898 0.0042  -0.0354 -0.0155 206 TYR   A CB  
3094 C  CG  . TYR   A 206 ? 0.2007 0.2671 0.1895 0.0086  -0.0399 -0.0186 206 TYR   A CG  
3095 C  CD1 . TYR   A 206 ? 0.1984 0.2696 0.1795 0.0188  -0.0406 -0.0135 206 TYR   A CD1 
3096 C  CD2 . TYR   A 206 ? 0.2383 0.3174 0.2356 0.0029  -0.0433 -0.0272 206 TYR   A CD2 
3097 C  CE1 . TYR   A 206 ? 0.2585 0.3487 0.2399 0.0245  -0.0453 -0.0166 206 TYR   A CE1 
3098 C  CE2 . TYR   A 206 ? 0.2817 0.3810 0.2812 0.0070  -0.0481 -0.0314 206 TYR   A CE2 
3099 C  CZ  . TYR   A 206 ? 0.2480 0.3534 0.2388 0.0185  -0.0496 -0.0261 206 TYR   A CZ  
3100 O  OH  . TYR   A 206 ? 0.3711 0.4988 0.3643 0.0238  -0.0548 -0.0303 206 TYR   A OH  
3110 N  N   . TYR   A 207 ? 0.1786 0.2103 0.1449 0.0165  -0.0297 -0.0039 207 TYR   A N   
3111 C  CA  . TYR   A 207 ? 0.1945 0.2231 0.1503 0.0248  -0.0270 0.0025  207 TYR   A CA  
3112 C  C   . TYR   A 207 ? 0.2197 0.2500 0.1676 0.0270  -0.0273 0.0001  207 TYR   A C   
3113 O  O   . TYR   A 207 ? 0.2393 0.2760 0.1775 0.0353  -0.0282 0.0020  207 TYR   A O   
3114 C  CB  . TYR   A 207 ? 0.2082 0.2217 0.1647 0.0234  -0.0210 0.0092  207 TYR   A CB  
3115 C  CG  . TYR   A 207 ? 0.2211 0.2273 0.1681 0.0294  -0.0160 0.0159  207 TYR   A CG  
3116 C  CD1 . TYR   A 207 ? 0.2521 0.2572 0.1927 0.0373  -0.0139 0.0220  207 TYR   A CD1 
3117 C  CD2 . TYR   A 207 ? 0.2504 0.2503 0.1946 0.0277  -0.0125 0.0165  207 TYR   A CD2 
3118 C  CE1 . TYR   A 207 ? 0.2805 0.2773 0.2118 0.0428  -0.0080 0.0288  207 TYR   A CE1 
3119 C  CE2 . TYR   A 207 ? 0.2673 0.2606 0.2033 0.0328  -0.0068 0.0230  207 TYR   A CE2 
3120 C  CZ  . TYR   A 207 ? 0.2493 0.2402 0.1787 0.0400  -0.0043 0.0293  207 TYR   A CZ  
3121 O  OH  . TYR   A 207 ? 0.3053 0.2880 0.2255 0.0453  0.0026  0.0367  207 TYR   A OH  
3131 N  N   . SER   A 208 ? 0.2071 0.2318 0.1580 0.0207  -0.0265 -0.0039 208 SER   A N   
3132 C  CA  . SER   A 208 ? 0.2346 0.2596 0.1777 0.0231  -0.0261 -0.0061 208 SER   A CA  
3133 C  C   . SER   A 208 ? 0.2907 0.3294 0.2309 0.0247  -0.0319 -0.0143 208 SER   A C   
3134 O  O   . SER   A 208 ? 0.2729 0.3174 0.2025 0.0319  -0.0325 -0.0141 208 SER   A O   
3135 C  CB  . SER   A 208 ? 0.2736 0.2886 0.2216 0.0165  -0.0234 -0.0080 208 SER   A CB  
3136 O  OG  . SER   A 208 ? 0.5920 0.6039 0.5316 0.0204  -0.0201 -0.0062 208 SER   A OG  
3142 N  N   . VAL   A 209 ? 0.2423 0.2874 0.1915 0.0185  -0.0360 -0.0220 209 VAL   A N   
3143 C  CA  . VAL   A 209 ? 0.2853 0.3424 0.2341 0.0172  -0.0411 -0.0323 209 VAL   A CA  
3144 C  C   . VAL   A 209 ? 0.2849 0.3569 0.2418 0.0151  -0.0462 -0.0378 209 VAL   A C   
3145 O  O   . VAL   A 209 ? 0.3164 0.4010 0.2750 0.0132  -0.0510 -0.0478 209 VAL   A O   
3146 C  CB  . VAL   A 209 ? 0.3721 0.4208 0.3245 0.0096  -0.0400 -0.0393 209 VAL   A CB  
3147 C  CG1 . VAL   A 209 ? 0.4749 0.5132 0.4186 0.0131  -0.0357 -0.0356 209 VAL   A CG1 
3148 C  CG2 . VAL   A 209 ? 0.3482 0.3881 0.3122 0.0010  -0.0380 -0.0394 209 VAL   A CG2 
3158 N  N   . GLY   A 210 ? 0.2416 0.3140 0.2037 0.0156  -0.0454 -0.0323 210 GLY   A N   
3159 C  CA  . GLY   A 210 ? 0.2267 0.3152 0.1964 0.0151  -0.0498 -0.0366 210 GLY   A CA  
3160 C  C   . GLY   A 210 ? 0.2308 0.3215 0.2139 0.0039  -0.0507 -0.0446 210 GLY   A C   
3161 O  O   . GLY   A 210 ? 0.2734 0.3807 0.2641 0.0022  -0.0546 -0.0508 210 GLY   A O   
3165 N  N   . LYS   A 211 ? 0.2250 0.2994 0.2113 -0.0034 -0.0465 -0.0444 211 LYS   A N   
3166 C  CA  . LYS   A 211 ? 0.2398 0.3117 0.2377 -0.0140 -0.0454 -0.0505 211 LYS   A CA  
3167 C  C   . LYS   A 211 ? 0.2152 0.2671 0.2136 -0.0171 -0.0396 -0.0437 211 LYS   A C   
3168 O  O   . LYS   A 211 ? 0.2286 0.2697 0.2193 -0.0134 -0.0372 -0.0386 211 LYS   A O   
3169 C  CB  . LYS   A 211 ? 0.3101 0.3841 0.3094 -0.0197 -0.0472 -0.0618 211 LYS   A CB  
3170 C  CG  . LYS   A 211 ? 0.4371 0.4994 0.4266 -0.0173 -0.0455 -0.0617 211 LYS   A CG  
3171 C  CD  . LYS   A 211 ? 0.5139 0.5745 0.5056 -0.0241 -0.0462 -0.0736 211 LYS   A CD  
3172 C  CE  . LYS   A 211 ? 0.5707 0.6183 0.5520 -0.0206 -0.0437 -0.0726 211 LYS   A CE  
3173 N  NZ  . LYS   A 211 ? 0.6488 0.7034 0.6259 -0.0210 -0.0471 -0.0845 211 LYS   A NZ  
3187 N  N   . ASN   A 212 ? 0.2012 0.2496 0.2089 -0.0239 -0.0372 -0.0438 212 ASN   A N   
3188 C  CA  . ASN   A 212 ? 0.1933 0.2248 0.2018 -0.0266 -0.0321 -0.0380 212 ASN   A CA  
3189 C  C   . ASN   A 212 ? 0.2125 0.2394 0.2295 -0.0358 -0.0295 -0.0430 212 ASN   A C   
3190 O  O   . ASN   A 212 ? 0.2358 0.2741 0.2607 -0.0404 -0.0311 -0.0490 212 ASN   A O   
3191 C  CB  . ASN   A 212 ? 0.1953 0.2255 0.2037 -0.0228 -0.0307 -0.0295 212 ASN   A CB  
3192 C  CG  . ASN   A 212 ? 0.2048 0.2470 0.2213 -0.0244 -0.0318 -0.0305 212 ASN   A CG  
3193 O  OD1 . ASN   A 212 ? 0.2308 0.2880 0.2480 -0.0211 -0.0357 -0.0331 212 ASN   A OD1 
3194 N  ND2 . ASN   A 212 ? 0.2018 0.2381 0.2236 -0.0284 -0.0283 -0.0276 212 ASN   A ND2 
3201 N  N   . SER   A 213 ? 0.2190 0.2294 0.2346 -0.0378 -0.0250 -0.0398 213 SER   A N   
3202 C  CA  . SER   A 213 ? 0.2384 0.2399 0.2596 -0.0456 -0.0212 -0.0439 213 SER   A CA  
3203 C  C   . SER   A 213 ? 0.2036 0.2034 0.2317 -0.0496 -0.0175 -0.0401 213 SER   A C   
3204 O  O   . SER   A 213 ? 0.2432 0.2380 0.2775 -0.0570 -0.0138 -0.0438 213 SER   A O   
3205 C  CB  . SER   A 213 ? 0.2218 0.2056 0.2367 -0.0443 -0.0176 -0.0416 213 SER   A CB  
3206 O  OG  . SER   A 213 ? 0.2457 0.2231 0.2572 -0.0397 -0.0157 -0.0325 213 SER   A OG  
3212 N  N   . TRP   A 214 ? 0.1735 0.1765 0.2005 -0.0450 -0.0178 -0.0328 214 TRP   A N   
3213 C  CA  . TRP   A 214 ? 0.1838 0.1841 0.2150 -0.0470 -0.0140 -0.0280 214 TRP   A CA  
3214 C  C   . TRP   A 214 ? 0.2079 0.1906 0.2358 -0.0480 -0.0087 -0.0241 214 TRP   A C   
3215 O  O   . TRP   A 214 ? 0.2111 0.1890 0.2415 -0.0503 -0.0044 -0.0206 214 TRP   A O   
3216 C  CB  . TRP   A 214 ? 0.1914 0.2030 0.2330 -0.0534 -0.0133 -0.0327 214 TRP   A CB  
3217 C  CG  . TRP   A 214 ? 0.1770 0.2078 0.2213 -0.0498 -0.0186 -0.0346 214 TRP   A CG  
3218 C  CD1 . TRP   A 214 ? 0.2452 0.2919 0.2953 -0.0523 -0.0225 -0.0428 214 TRP   A CD1 
3219 C  CD2 . TRP   A 214 ? 0.1613 0.1976 0.2026 -0.0427 -0.0203 -0.0286 214 TRP   A CD2 
3220 N  NE1 . TRP   A 214 ? 0.2326 0.2947 0.2829 -0.0461 -0.0265 -0.0412 214 TRP   A NE1 
3221 C  CE2 . TRP   A 214 ? 0.2081 0.2629 0.2529 -0.0403 -0.0249 -0.0325 214 TRP   A CE2 
3222 C  CE3 . TRP   A 214 ? 0.1798 0.2076 0.2156 -0.0380 -0.0185 -0.0210 214 TRP   A CE3 
3223 C  CZ2 . TRP   A 214 ? 0.2261 0.2885 0.2686 -0.0328 -0.0268 -0.0280 214 TRP   A CZ2 
3224 C  CZ3 . TRP   A 214 ? 0.2090 0.2447 0.2433 -0.0317 -0.0205 -0.0176 214 TRP   A CZ3 
3225 C  CH2 . TRP   A 214 ? 0.2121 0.2638 0.2495 -0.0291 -0.0243 -0.0208 214 TRP   A CH2 
3236 N  N   . GLN   A 215 ? 0.2008 0.1742 0.2218 -0.0447 -0.0090 -0.0236 215 GLN   A N   
3237 C  CA  . GLN   A 215 ? 0.2022 0.1595 0.2189 -0.0437 -0.0044 -0.0197 215 GLN   A CA  
3238 C  C   . GLN   A 215 ? 0.2025 0.1576 0.2121 -0.0364 -0.0063 -0.0155 215 GLN   A C   
3239 O  O   . GLN   A 215 ? 0.2341 0.1971 0.2417 -0.0333 -0.0103 -0.0167 215 GLN   A O   
3240 C  CB  . GLN   A 215 ? 0.2096 0.1568 0.2266 -0.0480 -0.0017 -0.0253 215 GLN   A CB  
3241 C  CG  . GLN   A 215 ? 0.2323 0.1806 0.2578 -0.0569 0.0013  -0.0306 215 GLN   A CG  
3242 C  CD  . GLN   A 215 ? 0.2865 0.2237 0.3129 -0.0622 0.0045  -0.0374 215 GLN   A CD  
3243 O  OE1 . GLN   A 215 ? 0.3108 0.2395 0.3306 -0.0586 0.0040  -0.0388 215 GLN   A OE1 
3244 N  NE2 . GLN   A 215 ? 0.3206 0.2576 0.3557 -0.0712 0.0082  -0.0423 215 GLN   A NE2 
3253 N  N   . ILE   A 216 ? 0.1896 0.1347 0.1953 -0.0332 -0.0032 -0.0104 216 ILE   A N   
3254 C  CA  . ILE   A 216 ? 0.1991 0.1429 0.1996 -0.0269 -0.0045 -0.0071 216 ILE   A CA  
3255 C  C   . ILE   A 216 ? 0.2036 0.1356 0.2002 -0.0252 -0.0017 -0.0078 216 ILE   A C   
3256 O  O   . ILE   A 216 ? 0.2208 0.1421 0.2165 -0.0259 0.0027  -0.0060 216 ILE   A O   
3257 C  CB  . ILE   A 216 ? 0.2105 0.1558 0.2098 -0.0232 -0.0042 -0.0012 216 ILE   A CB  
3258 C  CG1 . ILE   A 216 ? 0.2110 0.1668 0.2139 -0.0244 -0.0064 -0.0007 216 ILE   A CG1 
3259 C  CG2 . ILE   A 216 ? 0.2363 0.1816 0.2319 -0.0175 -0.0053 0.0009  216 ILE   A CG2 
3260 C  CD1 . ILE   A 216 ? 0.2339 0.1980 0.2368 -0.0229 -0.0102 -0.0024 216 ILE   A CD1 
3272 N  N   . GLY   A 217 ? 0.2242 0.1575 0.2179 -0.0222 -0.0036 -0.0100 217 GLY   A N   
3273 C  CA  . GLY   A 217 ? 0.2551 0.1782 0.2446 -0.0192 -0.0011 -0.0108 217 GLY   A CA  
3274 C  C   . GLY   A 217 ? 0.2677 0.1812 0.2567 -0.0231 0.0013  -0.0169 217 GLY   A C   
3275 O  O   . GLY   A 217 ? 0.2659 0.1691 0.2508 -0.0195 0.0040  -0.0169 217 GLY   A O   
3279 N  N   . PRO   A 218 ? 0.2487 0.1653 0.2420 -0.0299 0.0005  -0.0227 218 PRO   A N   
3280 C  CA  . PRO   A 218 ? 0.2525 0.1591 0.2457 -0.0339 0.0031  -0.0297 218 PRO   A CA  
3281 C  C   . PRO   A 218 ? 0.2721 0.1777 0.2597 -0.0296 0.0016  -0.0337 218 PRO   A C   
3282 O  O   . PRO   A 218 ? 0.2943 0.1863 0.2786 -0.0289 0.0053  -0.0365 218 PRO   A O   
3283 C  CB  . PRO   A 218 ? 0.2973 0.2133 0.2975 -0.0420 0.0010  -0.0364 218 PRO   A CB  
3284 C  CG  . PRO   A 218 ? 0.2420 0.1745 0.2432 -0.0395 -0.0042 -0.0338 218 PRO   A CG  
3285 C  CD  . PRO   A 218 ? 0.2553 0.1856 0.2539 -0.0338 -0.0031 -0.0242 218 PRO   A CD  
3293 N  N   . GLU   A 219 ? 0.2459 0.1642 0.2315 -0.0258 -0.0028 -0.0329 219 GLU   A N   
3294 C  CA  . GLU   A 219 ? 0.2530 0.1720 0.2330 -0.0214 -0.0037 -0.0363 219 GLU   A CA  
3295 C  C   . GLU   A 219 ? 0.2842 0.1947 0.2601 -0.0148 -0.0006 -0.0317 219 GLU   A C   
3296 O  O   . GLU   A 219 ? 0.3113 0.2193 0.2826 -0.0112 0.0001  -0.0352 219 GLU   A O   
3297 C  CB  . GLU   A 219 ? 0.2955 0.2300 0.2743 -0.0189 -0.0082 -0.0353 219 GLU   A CB  
3298 C  CG  . GLU   A 219 ? 0.3158 0.2558 0.2955 -0.0152 -0.0086 -0.0270 219 GLU   A CG  
3299 C  CD  . GLU   A 219 ? 0.3706 0.3153 0.3556 -0.0183 -0.0097 -0.0233 219 GLU   A CD  
3300 O  OE1 . GLU   A 219 ? 0.3099 0.2532 0.2988 -0.0235 -0.0095 -0.0259 219 GLU   A OE1 
3301 O  OE2 . GLU   A 219 ? 0.3064 0.2568 0.2917 -0.0155 -0.0106 -0.0182 219 GLU   A OE2 
3308 N  N   . ILE   A 220 ? 0.2687 0.1752 0.2458 -0.0124 0.0015  -0.0247 220 ILE   A N   
3309 C  CA  . ILE   A 220 ? 0.2734 0.1743 0.2470 -0.0051 0.0040  -0.0205 220 ILE   A CA  
3310 C  C   . ILE   A 220 ? 0.3156 0.2003 0.2873 -0.0037 0.0090  -0.0182 220 ILE   A C   
3311 O  O   . ILE   A 220 ? 0.2925 0.1725 0.2608 0.0036  0.0112  -0.0144 220 ILE   A O   
3312 C  CB  . ILE   A 220 ? 0.2786 0.1911 0.2536 -0.0005 0.0019  -0.0146 220 ILE   A CB  
3313 C  CG1 . ILE   A 220 ? 0.2709 0.1884 0.2498 -0.0034 0.0005  -0.0104 220 ILE   A CG1 
3314 C  CG2 . ILE   A 220 ? 0.2905 0.2149 0.2653 -0.0002 -0.0009 -0.0168 220 ILE   A CG2 
3315 C  CD1 . ILE   A 220 ? 0.3314 0.2393 0.3093 -0.0015 0.0037  -0.0060 220 ILE   A CD1 
3327 N  N   . MET   A 221 ? 0.3166 0.1927 0.2905 -0.0103 0.0114  -0.0202 221 MET   A N   
3328 C  CA  . MET   A 221 ? 0.3331 0.1910 0.3042 -0.0090 0.0176  -0.0175 221 MET   A CA  
3329 C  C   . MET   A 221 ? 0.3505 0.1941 0.3179 -0.0086 0.0212  -0.0238 221 MET   A C   
3330 O  O   . MET   A 221 ? 0.3419 0.1868 0.3113 -0.0149 0.0198  -0.0325 221 MET   A O   
3331 C  CB  . MET   A 221 ? 0.3546 0.2075 0.3301 -0.0168 0.0204  -0.0168 221 MET   A CB  
3332 C  CG  . MET   A 221 ? 0.4449 0.3100 0.4236 -0.0171 0.0178  -0.0108 221 MET   A CG  
3333 S  SD  . MET   A 221 ? 0.8016 0.6693 0.7752 -0.0061 0.0177  -0.0009 221 MET   A SD  
3334 C  CE  . MET   A 221 ? 0.4691 0.3131 0.4361 -0.0018 0.0261  0.0024  221 MET   A CE  
3344 N  N   . LYS   A 222 ? 0.3633 0.1933 0.3248 -0.0008 0.0258  -0.0199 222 LYS   A N   
3345 C  CA  . LYS   A 222 ? 0.3790 0.1924 0.3362 0.0001  0.0303  -0.0258 222 LYS   A CA  
3346 C  C   . LYS   A 222 ? 0.4494 0.2452 0.4087 -0.0088 0.0360  -0.0298 222 LYS   A C   
3347 O  O   . LYS   A 222 ? 0.4411 0.2306 0.4019 -0.0112 0.0396  -0.0240 222 LYS   A O   
3348 C  CB  . LYS   A 222 ? 0.4098 0.2127 0.3598 0.0122  0.0343  -0.0198 222 LYS   A CB  
3349 C  CG  . LYS   A 222 ? 0.4165 0.2368 0.3656 0.0208  0.0295  -0.0173 222 LYS   A CG  
3350 C  CD  . LYS   A 222 ? 0.4567 0.2735 0.4017 0.0258  0.0305  -0.0228 222 LYS   A CD  
3351 C  CE  . LYS   A 222 ? 0.4864 0.3218 0.4317 0.0341  0.0268  -0.0199 222 LYS   A CE  
3352 N  NZ  . LYS   A 222 ? 0.5693 0.3980 0.5098 0.0465  0.0305  -0.0147 222 LYS   A NZ  
3366 N  N   . GLU   A 223 ? 0.4674 0.2560 0.4271 -0.0144 0.0371  -0.0404 223 GLU   A N   
3367 C  CA  . GLU   A 223 ? 0.6333 0.4130 0.5987 -0.0246 0.0408  -0.0452 223 GLU   A CA  
3368 C  C   . GLU   A 223 ? 0.6409 0.4038 0.6035 -0.0205 0.0481  -0.0373 223 GLU   A C   
3369 O  O   . GLU   A 223 ? 0.6563 0.4161 0.6237 -0.0267 0.0514  -0.0347 223 GLU   A O   
3370 C  CB  . GLU   A 223 ? 0.6507 0.4314 0.6176 -0.0300 0.0387  -0.0581 223 GLU   A CB  
3371 C  CG  . GLU   A 223 ? 0.7517 0.5281 0.7258 -0.0404 0.0410  -0.0641 223 GLU   A CG  
3372 C  CD  . GLU   A 223 ? 0.8211 0.6081 0.8045 -0.0494 0.0401  -0.0623 223 GLU   A CD  
3373 O  OE1 . GLU   A 223 ? 0.8731 0.6782 0.8606 -0.0531 0.0339  -0.0659 223 GLU   A OE1 
3374 O  OE2 . GLU   A 223 ? 0.8049 0.5825 0.7911 -0.0524 0.0459  -0.0574 223 GLU   A OE2 
3381 N  N   . ASP   A 224 ? 0.5470 0.3000 0.5015 -0.0094 0.0508  -0.0330 224 ASP   A N   
3382 C  CA  . ASP   A 224 ? 0.6600 0.3978 0.6104 -0.0039 0.0577  -0.0250 224 ASP   A CA  
3383 C  C   . ASP   A 224 ? 0.6474 0.3880 0.5967 -0.0004 0.0592  -0.0135 224 ASP   A C   
3384 O  O   . ASP   A 224 ? 0.7232 0.4521 0.6688 0.0033  0.0653  -0.0065 224 ASP   A O   
3385 C  CB  . ASP   A 224 ? 0.6866 0.4160 0.6286 0.0084  0.0597  -0.0233 224 ASP   A CB  
3386 C  CG  . ASP   A 224 ? 0.7942 0.5353 0.7318 0.0192  0.0554  -0.0182 224 ASP   A CG  
3387 O  OD1 . ASP   A 224 ? 0.8586 0.6054 0.7952 0.0238  0.0549  -0.0090 224 ASP   A OD1 
3388 O  OD2 . ASP   A 224 ? 0.8481 0.5937 0.7835 0.0232  0.0527  -0.0238 224 ASP   A OD2 
3393 N  N   . SER   A 225 ? 0.5826 0.3380 0.5346 -0.0015 0.0541  -0.0114 225 SER   A N   
3394 C  CA  . SER   A 225 ? 0.5665 0.3254 0.5165 0.0030  0.0550  -0.0008 225 SER   A CA  
3395 C  C   . SER   A 225 ? 0.6119 0.3680 0.5669 -0.0059 0.0591  0.0011  225 SER   A C   
3396 O  O   . SER   A 225 ? 0.5804 0.3351 0.5319 -0.0012 0.0621  0.0103  225 SER   A O   
3397 C  CB  . SER   A 225 ? 0.5884 0.3633 0.5396 0.0044  0.0485  0.0004  225 SER   A CB  
3398 O  OG  . SER   A 225 ? 0.5292 0.3160 0.4893 -0.0075 0.0449  -0.0049 225 SER   A OG  
3404 N  N   . GLY   A 226 ? 0.6169 0.3740 0.5800 -0.0182 0.0591  -0.0076 226 GLY   A N   
3405 C  CA  . GLY   A 226 ? 0.6015 0.3591 0.5712 -0.0273 0.0625  -0.0068 226 GLY   A CA  
3406 C  C   . GLY   A 226 ? 0.5922 0.3666 0.5682 -0.0327 0.0581  -0.0062 226 GLY   A C   
3407 O  O   . GLY   A 226 ? 0.6298 0.4064 0.6119 -0.0403 0.0611  -0.0058 226 GLY   A O   
3411 N  N   . TYR   A 227 ? 0.5622 0.3481 0.5369 -0.0289 0.0517  -0.0060 227 TYR   A N   
3412 C  CA  . TYR   A 227 ? 0.6220 0.4236 0.6023 -0.0336 0.0475  -0.0057 227 TYR   A CA  
3413 C  C   . TYR   A 227 ? 0.4222 0.2374 0.4087 -0.0401 0.0406  -0.0162 227 TYR   A C   
3414 O  O   . TYR   A 227 ? 0.4955 0.3148 0.4784 -0.0350 0.0361  -0.0194 227 TYR   A O   
3415 C  CB  . TYR   A 227 ? 0.6029 0.4127 0.5772 -0.0234 0.0441  0.0031  227 TYR   A CB  
3416 C  CG  . TYR   A 227 ? 0.6010 0.3965 0.5669 -0.0152 0.0509  0.0134  227 TYR   A CG  
3417 C  CD1 . TYR   A 227 ? 0.6221 0.4171 0.5895 -0.0182 0.0553  0.0186  227 TYR   A CD1 
3418 C  CD2 . TYR   A 227 ? 0.7128 0.5005 0.6698 -0.0036 0.0519  0.0176  227 TYR   A CD2 
3419 C  CE1 . TYR   A 227 ? 0.6619 0.4483 0.6212 -0.0098 0.0606  0.0279  227 TYR   A CE1 
3420 C  CE2 . TYR   A 227 ? 0.7384 0.5187 0.6879 0.0051  0.0567  0.0267  227 TYR   A CE2 
3421 C  CZ  . TYR   A 227 ? 0.6948 0.4742 0.6450 0.0019  0.0611  0.0318  227 TYR   A CZ  
3422 O  OH  . TYR   A 227 ? 0.7818 0.5542 0.7234 0.0109  0.0662  0.0408  227 TYR   A OH  
3432 N  N   . ASP   A 228 ? 0.3658 0.1915 0.3617 -0.0503 0.0392  -0.0215 228 ASP   A N   
3433 C  CA  . ASP   A 228 ? 0.3679 0.2120 0.3691 -0.0543 0.0312  -0.0305 228 ASP   A CA  
3434 C  C   . ASP   A 228 ? 0.3622 0.2244 0.3609 -0.0470 0.0235  -0.0261 228 ASP   A C   
3435 O  O   . ASP   A 228 ? 0.3404 0.2136 0.3385 -0.0454 0.0175  -0.0309 228 ASP   A O   
3436 C  CB  . ASP   A 228 ? 0.4130 0.2672 0.4254 -0.0657 0.0310  -0.0372 228 ASP   A CB  
3437 C  CG  . ASP   A 228 ? 0.5179 0.3628 0.5341 -0.0713 0.0362  -0.0407 228 ASP   A CG  
3438 O  OD1 . ASP   A 228 ? 0.6043 0.4330 0.6145 -0.0677 0.0400  -0.0405 228 ASP   A OD1 
3439 O  OD2 . ASP   A 228 ? 0.5954 0.4491 0.6208 -0.0792 0.0370  -0.0437 228 ASP   A OD2 
3444 N  N   . ALA   A 229 ? 0.3195 0.1856 0.3173 -0.0432 0.0239  -0.0174 229 ALA   A N   
3445 C  CA  . ALA   A 229 ? 0.2676 0.1501 0.2642 -0.0376 0.0173  -0.0137 229 ALA   A CA  
3446 C  C   . ALA   A 229 ? 0.2604 0.1389 0.2519 -0.0306 0.0197  -0.0040 229 ALA   A C   
3447 O  O   . ALA   A 229 ? 0.2921 0.1568 0.2811 -0.0304 0.0263  0.0003  229 ALA   A O   
3448 C  CB  . ALA   A 229 ? 0.2802 0.1797 0.2843 -0.0432 0.0132  -0.0167 229 ALA   A CB  
3454 N  N   . LEU   A 230 ? 0.2529 0.1434 0.2427 -0.0249 0.0147  -0.0010 230 LEU   A N   
3455 C  CA  . LEU   A 230 ? 0.2612 0.1524 0.2469 -0.0185 0.0155  0.0068  230 LEU   A CA  
3456 C  C   . LEU   A 230 ? 0.2412 0.1391 0.2307 -0.0222 0.0160  0.0091  230 LEU   A C   
3457 O  O   . LEU   A 230 ? 0.2610 0.1524 0.2472 -0.0200 0.0205  0.0149  230 LEU   A O   
3458 C  CB  . LEU   A 230 ? 0.2730 0.1754 0.2570 -0.0122 0.0100  0.0077  230 LEU   A CB  
3459 C  CG  . LEU   A 230 ? 0.3538 0.2589 0.3336 -0.0050 0.0099  0.0140  230 LEU   A CG  
3460 C  CD1 . LEU   A 230 ? 0.4374 0.3291 0.4102 0.0017  0.0149  0.0187  230 LEU   A CD1 
3461 C  CD2 . LEU   A 230 ? 0.3743 0.2925 0.3551 -0.0012 0.0045  0.0129  230 LEU   A CD2 
3473 N  N   . ARG   A 231 ? 0.2153 0.1259 0.2108 -0.0269 0.0119  0.0051  231 ARG   A N   
3474 C  CA  . ARG   A 231 ? 0.2063 0.1246 0.2062 -0.0304 0.0124  0.0065  231 ARG   A CA  
3475 C  C   . ARG   A 231 ? 0.1903 0.1157 0.1983 -0.0383 0.0111  -0.0001 231 ARG   A C   
3476 O  O   . ARG   A 231 ? 0.1863 0.1156 0.1956 -0.0396 0.0074  -0.0057 231 ARG   A O   
3477 C  CB  . ARG   A 231 ? 0.1956 0.1260 0.1946 -0.0259 0.0078  0.0090  231 ARG   A CB  
3478 C  CG  . ARG   A 231 ? 0.1878 0.1155 0.1802 -0.0186 0.0086  0.0147  231 ARG   A CG  
3479 C  CD  . ARG   A 231 ? 0.1889 0.1284 0.1813 -0.0154 0.0042  0.0155  231 ARG   A CD  
3480 N  NE  . ARG   A 231 ? 0.1780 0.1235 0.1714 -0.0139 -0.0005 0.0124  231 ARG   A NE  
3481 C  CZ  . ARG   A 231 ? 0.1946 0.1400 0.1849 -0.0089 -0.0020 0.0131  231 ARG   A CZ  
3482 N  NH1 . ARG   A 231 ? 0.2156 0.1548 0.2009 -0.0042 0.0004  0.0164  231 ARG   A NH1 
3483 N  NH2 . ARG   A 231 ? 0.1903 0.1426 0.1825 -0.0084 -0.0055 0.0107  231 ARG   A NH2 
3497 N  N   . TYR   A 232 ? 0.2027 0.1322 0.2160 -0.0429 0.0138  0.0005  232 TYR   A N   
3498 C  CA  . TYR   A 232 ? 0.1982 0.1374 0.2208 -0.0506 0.0130  -0.0058 232 TYR   A CA  
3499 C  C   . TYR   A 232 ? 0.2128 0.1664 0.2388 -0.0495 0.0106  -0.0040 232 TYR   A C   
3500 O  O   . TYR   A 232 ? 0.2473 0.1990 0.2717 -0.0478 0.0142  0.0016  232 TYR   A O   
3501 C  CB  . TYR   A 232 ? 0.2095 0.1395 0.2372 -0.0583 0.0203  -0.0074 232 TYR   A CB  
3502 C  CG  . TYR   A 232 ? 0.2409 0.1527 0.2643 -0.0591 0.0243  -0.0086 232 TYR   A CG  
3503 C  CD1 . TYR   A 232 ? 0.2605 0.1561 0.2750 -0.0532 0.0294  -0.0011 232 TYR   A CD1 
3504 C  CD2 . TYR   A 232 ? 0.2679 0.1792 0.2951 -0.0643 0.0228  -0.0175 232 TYR   A CD2 
3505 C  CE1 . TYR   A 232 ? 0.2885 0.1667 0.2987 -0.0529 0.0336  -0.0020 232 TYR   A CE1 
3506 C  CE2 . TYR   A 232 ? 0.3130 0.2070 0.3358 -0.0644 0.0267  -0.0190 232 TYR   A CE2 
3507 C  CZ  . TYR   A 232 ? 0.3025 0.1797 0.3170 -0.0585 0.0322  -0.0110 232 TYR   A CZ  
3508 O  OH  . TYR   A 232 ? 0.4069 0.2657 0.4165 -0.0575 0.0364  -0.0124 232 TYR   A OH  
3518 N  N   . MET   A 233 ? 0.1736 0.1410 0.2031 -0.0493 0.0050  -0.0080 233 MET   A N   
3519 C  CA  . MET   A 233 ? 0.1668 0.1468 0.1987 -0.0469 0.0029  -0.0060 233 MET   A CA  
3520 C  C   . MET   A 233 ? 0.1811 0.1712 0.2230 -0.0531 0.0052  -0.0091 233 MET   A C   
3521 O  O   . MET   A 233 ? 0.1907 0.1882 0.2343 -0.0512 0.0060  -0.0060 233 MET   A O   
3522 C  CB  . MET   A 233 ? 0.1984 0.1874 0.2283 -0.0423 -0.0037 -0.0079 233 MET   A CB  
3523 C  CG  . MET   A 233 ? 0.1968 0.1773 0.2184 -0.0367 -0.0052 -0.0048 233 MET   A CG  
3524 S  SD  . MET   A 233 ? 0.2239 0.2125 0.2424 -0.0313 -0.0109 -0.0055 233 MET   A SD  
3525 C  CE  . MET   A 233 ? 0.1746 0.1675 0.1925 -0.0271 -0.0110 -0.0012 233 MET   A CE  
3535 N  N   . ASP   A 234 ? 0.1778 0.1688 0.2266 -0.0606 0.0067  -0.0153 234 ASP   A N   
3536 C  CA  . ASP   A 234 ? 0.1842 0.1859 0.2445 -0.0679 0.0097  -0.0191 234 ASP   A CA  
3537 C  C   . ASP   A 234 ? 0.2062 0.1991 0.2674 -0.0707 0.0182  -0.0134 234 ASP   A C   
3538 O  O   . ASP   A 234 ? 0.2251 0.2288 0.2939 -0.0736 0.0209  -0.0133 234 ASP   A O   
3539 C  CB  . ASP   A 234 ? 0.2090 0.2152 0.2774 -0.0759 0.0088  -0.0288 234 ASP   A CB  
3540 C  CG  . ASP   A 234 ? 0.2620 0.2485 0.3283 -0.0810 0.0146  -0.0297 234 ASP   A CG  
3541 O  OD1 . ASP   A 234 ? 0.2987 0.2705 0.3543 -0.0752 0.0148  -0.0248 234 ASP   A OD1 
3542 O  OD2 . ASP   A 234 ? 0.4351 0.4205 0.5106 -0.0906 0.0193  -0.0354 234 ASP   A OD2 
3547 N  N   . LYS   A 235 ? 0.2030 0.1765 0.2561 -0.0692 0.0230  -0.0083 235 LYS   A N   
3548 C  CA  . LYS   A 235 ? 0.1970 0.1587 0.2485 -0.0710 0.0322  -0.0020 235 LYS   A CA  
3549 C  C   . LYS   A 235 ? 0.1896 0.1346 0.2279 -0.0633 0.0331  0.0047  235 LYS   A C   
3550 O  O   . LYS   A 235 ? 0.2077 0.1372 0.2428 -0.0649 0.0366  0.0044  235 LYS   A O   
3551 C  CB  . LYS   A 235 ? 0.2435 0.1991 0.3042 -0.0820 0.0396  -0.0063 235 LYS   A CB  
3552 C  CG  . LYS   A 235 ? 0.3084 0.2532 0.3678 -0.0837 0.0503  0.0013  235 LYS   A CG  
3553 C  CD  . LYS   A 235 ? 0.3392 0.2763 0.4075 -0.0946 0.0583  -0.0027 235 LYS   A CD  
3554 C  CE  . LYS   A 235 ? 0.4771 0.4011 0.5405 -0.0935 0.0684  0.0061  235 LYS   A CE  
3555 N  NZ  . LYS   A 235 ? 0.6633 0.6010 0.7388 -0.1006 0.0727  0.0042  235 LYS   A NZ  
3569 N  N   . PRO   A 236 ? 0.1761 0.1246 0.2067 -0.0547 0.0298  0.0099  236 PRO   A N   
3570 C  CA  . PRO   A 236 ? 0.1777 0.1144 0.1966 -0.0467 0.0292  0.0151  236 PRO   A CA  
3571 C  C   . PRO   A 236 ? 0.1994 0.1183 0.2126 -0.0462 0.0376  0.0207  236 PRO   A C   
3572 O  O   . PRO   A 236 ? 0.2102 0.1175 0.2164 -0.0419 0.0375  0.0223  236 PRO   A O   
3573 C  CB  . PRO   A 236 ? 0.1825 0.1287 0.1969 -0.0396 0.0254  0.0187  236 PRO   A CB  
3574 C  CG  . PRO   A 236 ? 0.1919 0.1547 0.2148 -0.0425 0.0203  0.0132  236 PRO   A CG  
3575 C  CD  . PRO   A 236 ? 0.1916 0.1567 0.2245 -0.0515 0.0249  0.0096  236 PRO   A CD  
3583 N  N   . SER   A 237 ? 0.2144 0.1306 0.2303 -0.0502 0.0454  0.0241  237 SER   A N   
3584 C  CA  . SER   A 237 ? 0.2255 0.1229 0.2344 -0.0488 0.0552  0.0313  237 SER   A CA  
3585 C  C   . SER   A 237 ? 0.2463 0.1274 0.2570 -0.0542 0.0593  0.0279  237 SER   A C   
3586 O  O   . SER   A 237 ? 0.2789 0.1416 0.2821 -0.0515 0.0671  0.0340  237 SER   A O   
3587 C  CB  . SER   A 237 ? 0.2511 0.1506 0.2639 -0.0531 0.0632  0.0351  237 SER   A CB  
3588 O  OG  . SER   A 237 ? 0.2653 0.1719 0.2928 -0.0649 0.0652  0.0278  237 SER   A OG  
3594 N  N   . ARG   A 238 ? 0.2394 0.1273 0.2588 -0.0607 0.0541  0.0185  238 ARG   A N   
3595 C  CA  A ARG   A 238 ? 0.2655 0.1372 0.2856 -0.0652 0.0576  0.0141  238 ARG   A CA  
3596 C  CA  B ARG   A 238 ? 0.2667 0.1383 0.2867 -0.0652 0.0576  0.0141  238 ARG   A CA  
3597 C  C   . ARG   A 238 ? 0.2617 0.1187 0.2689 -0.0552 0.0569  0.0187  238 ARG   A C   
3598 O  O   . ARG   A 238 ? 0.3187 0.1607 0.3224 -0.0545 0.0607  0.0182  238 ARG   A O   
3599 C  CB  A ARG   A 238 ? 0.2577 0.1422 0.2872 -0.0716 0.0502  0.0027  238 ARG   A CB  
3600 C  CB  B ARG   A 238 ? 0.2592 0.1436 0.2889 -0.0718 0.0504  0.0026  238 ARG   A CB  
3601 C  CG  A ARG   A 238 ? 0.2848 0.1829 0.3284 -0.0823 0.0513  -0.0040 238 ARG   A CG  
3602 C  CG  B ARG   A 238 ? 0.2982 0.1732 0.3317 -0.0779 0.0532  -0.0040 238 ARG   A CG  
3603 C  CD  A ARG   A 238 ? 0.3095 0.2234 0.3608 -0.0864 0.0427  -0.0148 238 ARG   A CD  
3604 C  CD  B ARG   A 238 ? 0.3266 0.2101 0.3644 -0.0809 0.0456  -0.0144 238 ARG   A CD  
3605 N  NE  A ARG   A 238 ? 0.3990 0.3034 0.4478 -0.0871 0.0412  -0.0208 238 ARG   A NE  
3606 N  NE  B ARG   A 238 ? 0.3977 0.3031 0.4471 -0.0875 0.0406  -0.0217 238 ARG   A NE  
3607 C  CZ  A ARG   A 238 ? 0.4129 0.3279 0.4653 -0.0892 0.0340  -0.0301 238 ARG   A CZ  
3608 C  CZ  B ARG   A 238 ? 0.4083 0.3259 0.4617 -0.0896 0.0332  -0.0309 238 ARG   A CZ  
3609 N  NH1 A ARG   A 238 ? 0.4147 0.3511 0.4725 -0.0893 0.0270  -0.0337 238 ARG   A NH1 
3610 N  NH1 B ARG   A 238 ? 0.3920 0.3016 0.4422 -0.0895 0.0318  -0.0365 238 ARG   A NH1 
3611 N  NH2 A ARG   A 238 ? 0.3923 0.2978 0.4414 -0.0893 0.0334  -0.0351 238 ARG   A NH2 
3612 N  NH2 B ARG   A 238 ? 0.4116 0.3507 0.4707 -0.0897 0.0268  -0.0338 238 ARG   A NH2 
3637 N  N   . ASP   A 239 ? 0.2629 0.1286 0.2628 -0.0452 0.0504  0.0228  239 ASP   A N   
3638 C  CA  . ASP   A 239 ? 0.2973 0.1534 0.2862 -0.0349 0.0490  0.0268  239 ASP   A CA  
3639 C  C   . ASP   A 239 ? 0.3266 0.1697 0.3048 -0.0270 0.0564  0.0373  239 ASP   A C   
3640 O  O   . ASP   A 239 ? 0.3327 0.1693 0.3016 -0.0173 0.0554  0.0412  239 ASP   A O   
3641 C  CB  . ASP   A 239 ? 0.2718 0.1438 0.2590 -0.0286 0.0388  0.0251  239 ASP   A CB  
3642 C  CG  . ASP   A 239 ? 0.2436 0.1283 0.2284 -0.0236 0.0360  0.0297  239 ASP   A CG  
3643 O  OD1 . ASP   A 239 ? 0.2869 0.1692 0.2710 -0.0248 0.0416  0.0341  239 ASP   A OD1 
3644 O  OD2 . ASP   A 239 ? 0.2738 0.1701 0.2575 -0.0191 0.0287  0.0282  239 ASP   A OD2 
3649 N  N   . GLY   A 240 ? 0.2799 0.1203 0.2589 -0.0301 0.0635  0.0421  240 GLY   A N   
3650 C  CA  . GLY   A 240 ? 0.3196 0.1501 0.2877 -0.0218 0.0700  0.0518  240 GLY   A CA  
3651 C  C   . GLY   A 240 ? 0.3202 0.1595 0.2787 -0.0108 0.0666  0.0586  240 GLY   A C   
3652 O  O   . GLY   A 240 ? 0.3773 0.2094 0.3252 -0.0022 0.0715  0.0667  240 GLY   A O   
3656 N  N   . MET   A 241 ? 0.3151 0.1740 0.2773 -0.0098 0.0565  0.0538  241 MET   A N   
3657 C  CA  . MET   A 241 ? 0.3346 0.2056 0.2891 0.0003  0.0512  0.0574  241 MET   A CA  
3658 C  C   . MET   A 241 ? 0.2862 0.1765 0.2475 -0.0033 0.0449  0.0528  241 MET   A C   
3659 O  O   . MET   A 241 ? 0.2954 0.1937 0.2513 0.0023  0.0442  0.0562  241 MET   A O   
3660 C  CB  . MET   A 241 ? 0.4310 0.3043 0.3810 0.0082  0.0445  0.0558  241 MET   A CB  
3661 C  CG  . MET   A 241 ? 0.6149 0.4695 0.5612 0.0100  0.0495  0.0574  241 MET   A CG  
3662 S  SD  . MET   A 241 ? 1.1542 1.0108 1.0920 0.0232  0.0441  0.0589  241 MET   A SD  
3663 C  CE  . MET   A 241 ? 0.6408 0.4708 0.5676 0.0297  0.0555  0.0675  241 MET   A CE  
3673 N  N   . SER   A 242 ? 0.2328 0.1307 0.2051 -0.0117 0.0407  0.0451  242 SER   A N   
3674 C  CA  . SER   A 242 ? 0.2039 0.1188 0.1823 -0.0141 0.0347  0.0408  242 SER   A CA  
3675 C  C   . SER   A 242 ? 0.2285 0.1468 0.2117 -0.0194 0.0402  0.0421  242 SER   A C   
3676 O  O   . SER   A 242 ? 0.2573 0.1661 0.2432 -0.0249 0.0481  0.0440  242 SER   A O   
3677 C  CB  . SER   A 242 ? 0.2221 0.1431 0.2090 -0.0195 0.0286  0.0330  242 SER   A CB  
3678 O  OG  . SER   A 242 ? 0.2282 0.1485 0.2108 -0.0140 0.0235  0.0318  242 SER   A OG  
3684 N  N   . ILE   A 243 ? 0.2194 0.1517 0.2042 -0.0180 0.0362  0.0407  243 ILE   A N   
3685 C  CA  . ILE   A 243 ? 0.2297 0.1684 0.2190 -0.0218 0.0408  0.0418  243 ILE   A CA  
3686 C  C   . ILE   A 243 ? 0.1845 0.1357 0.1861 -0.0288 0.0369  0.0347  243 ILE   A C   
3687 O  O   . ILE   A 243 ? 0.1972 0.1551 0.2015 -0.0283 0.0294  0.0297  243 ILE   A O   
3688 C  CB  . ILE   A 243 ? 0.2124 0.1575 0.1933 -0.0138 0.0406  0.0458  243 ILE   A CB  
3689 C  CG1 . ILE   A 243 ? 0.2150 0.1705 0.1945 -0.0092 0.0314  0.0414  243 ILE   A CG1 
3690 C  CG2 . ILE   A 243 ? 0.2330 0.1661 0.2017 -0.0070 0.0464  0.0537  243 ILE   A CG2 
3691 C  CD1 . ILE   A 243 ? 0.2287 0.1927 0.2018 -0.0029 0.0307  0.0429  243 ILE   A CD1 
3703 N  N   . ASP   A 244 ? 0.1959 0.1514 0.2051 -0.0349 0.0424  0.0346  244 ASP   A N   
3704 C  CA  . ASP   A 244 ? 0.2208 0.1896 0.2429 -0.0417 0.0396  0.0278  244 ASP   A CA  
3705 C  C   . ASP   A 244 ? 0.2031 0.1868 0.2271 -0.0386 0.0376  0.0274  244 ASP   A C   
3706 O  O   . ASP   A 244 ? 0.2058 0.2023 0.2384 -0.0410 0.0333  0.0221  244 ASP   A O   
3707 C  CB  . ASP   A 244 ? 0.2318 0.1984 0.2640 -0.0518 0.0474  0.0264  244 ASP   A CB  
3708 C  CG  . ASP   A 244 ? 0.2293 0.1808 0.2616 -0.0564 0.0498  0.0250  244 ASP   A CG  
3709 O  OD1 . ASP   A 244 ? 0.2442 0.1909 0.2712 -0.0526 0.0440  0.0234  244 ASP   A OD1 
3710 O  OD2 . ASP   A 244 ? 0.2758 0.2196 0.3134 -0.0640 0.0585  0.0255  244 ASP   A OD2 
3715 N  N   . VAL   A 245 ? 0.1990 0.1815 0.2146 -0.0326 0.0408  0.0329  245 VAL   A N   
3716 C  CA  . VAL   A 245 ? 0.2148 0.2101 0.2314 -0.0293 0.0403  0.0327  245 VAL   A CA  
3717 C  C   . VAL   A 245 ? 0.2053 0.1977 0.2087 -0.0199 0.0387  0.0363  245 VAL   A C   
3718 O  O   . VAL   A 245 ? 0.2092 0.1910 0.2031 -0.0162 0.0413  0.0411  245 VAL   A O   
3719 C  CB  . VAL   A 245 ? 0.2061 0.2066 0.2291 -0.0339 0.0491  0.0350  245 VAL   A CB  
3720 C  CG1 . VAL   A 245 ? 0.2594 0.2669 0.2978 -0.0440 0.0502  0.0296  245 VAL   A CG1 
3721 C  CG2 . VAL   A 245 ? 0.2691 0.2562 0.2841 -0.0333 0.0583  0.0426  245 VAL   A CG2 
3731 N  N   . ALA   A 246 ? 0.2070 0.2096 0.2098 -0.0155 0.0350  0.0338  246 ALA   A N   
3732 C  CA  . ALA   A 246 ? 0.2150 0.2167 0.2061 -0.0071 0.0327  0.0352  246 ALA   A CA  
3733 C  C   . ALA   A 246 ? 0.2707 0.2695 0.2530 -0.0032 0.0399  0.0415  246 ALA   A C   
3734 O  O   . ALA   A 246 ? 0.2624 0.2577 0.2331 0.0038  0.0384  0.0436  246 ALA   A O   
3735 C  CB  . ALA   A 246 ? 0.2191 0.2307 0.2119 -0.0040 0.0281  0.0304  246 ALA   A CB  
3741 N  N   . ASP   A 247 ? 0.2218 0.2218 0.2091 -0.0076 0.0481  0.0449  247 ASP   A N   
3742 C  CA  . ASP   A 247 ? 0.2644 0.2608 0.2426 -0.0037 0.0565  0.0521  247 ASP   A CA  
3743 C  C   . ASP   A 247 ? 0.2826 0.2641 0.2512 -0.0013 0.0598  0.0583  247 ASP   A C   
3744 O  O   . ASP   A 247 ? 0.3066 0.2838 0.2636 0.0048  0.0658  0.0650  247 ASP   A O   
3745 C  CB  . ASP   A 247 ? 0.2992 0.3007 0.2869 -0.0103 0.0655  0.0541  247 ASP   A CB  
3746 C  CG  . ASP   A 247 ? 0.4202 0.4376 0.4129 -0.0086 0.0643  0.0503  247 ASP   A CG  
3747 O  OD1 . ASP   A 247 ? 0.4594 0.4819 0.4472 -0.0022 0.0571  0.0463  247 ASP   A OD1 
3748 O  OD2 . ASP   A 247 ? 0.5002 0.5251 0.5031 -0.0142 0.0708  0.0507  247 ASP   A OD2 
3753 N  N   . ASP   A 248 ? 0.2382 0.2116 0.2101 -0.0049 0.0565  0.0564  248 ASP   A N   
3754 C  CA  . ASP   A 248 ? 0.2728 0.2317 0.2354 -0.0014 0.0591  0.0619  248 ASP   A CA  
3755 C  C   . ASP   A 248 ? 0.2661 0.2256 0.2195 0.0070  0.0505  0.0602  248 ASP   A C   
3756 O  O   . ASP   A 248 ? 0.2930 0.2422 0.2383 0.0116  0.0517  0.0644  248 ASP   A O   
3757 C  CB  . ASP   A 248 ? 0.2929 0.2417 0.2649 -0.0105 0.0621  0.0608  248 ASP   A CB  
3758 C  CG  . ASP   A 248 ? 0.3397 0.2860 0.3199 -0.0190 0.0727  0.0634  248 ASP   A CG  
3759 O  OD1 . ASP   A 248 ? 0.4022 0.3496 0.3775 -0.0163 0.0801  0.0691  248 ASP   A OD1 
3760 O  OD2 . ASP   A 248 ? 0.3676 0.3119 0.3596 -0.0286 0.0737  0.0590  248 ASP   A OD2 
3765 N  N   . TYR   A 249 ? 0.2383 0.2095 0.1929 0.0094  0.0426  0.0540  249 TYR   A N   
3766 C  CA  . TYR   A 249 ? 0.2295 0.2034 0.1770 0.0164  0.0348  0.0512  249 TYR   A CA  
3767 C  C   . TYR   A 249 ? 0.2811 0.2564 0.2140 0.0266  0.0367  0.0560  249 TYR   A C   
3768 O  O   . TYR   A 249 ? 0.2843 0.2630 0.2126 0.0290  0.0419  0.0592  249 TYR   A O   
3769 C  CB  . TYR   A 249 ? 0.2349 0.2197 0.1883 0.0151  0.0271  0.0430  249 TYR   A CB  
3770 C  CG  . TYR   A 249 ? 0.2273 0.2161 0.1748 0.0212  0.0199  0.0392  249 TYR   A CG  
3771 C  CD1 . TYR   A 249 ? 0.2263 0.2123 0.1769 0.0199  0.0150  0.0366  249 TYR   A CD1 
3772 C  CD2 . TYR   A 249 ? 0.2421 0.2385 0.1809 0.0283  0.0181  0.0378  249 TYR   A CD2 
3773 C  CE1 . TYR   A 249 ? 0.2419 0.2332 0.1882 0.0251  0.0088  0.0328  249 TYR   A CE1 
3774 C  CE2 . TYR   A 249 ? 0.2410 0.2428 0.1751 0.0335  0.0114  0.0333  249 TYR   A CE2 
3775 C  CZ  . TYR   A 249 ? 0.2436 0.2429 0.1825 0.0312  0.0070  0.0309  249 TYR   A CZ  
3776 O  OH  . TYR   A 249 ? 0.2646 0.2708 0.2007 0.0356  0.0007  0.0260  249 TYR   A OH  
3786 N  N   . TYR   A 250 ? 0.2559 0.2299 0.1809 0.0335  0.0324  0.0564  250 TYR   A N   
3787 C  CA  . TYR   A 250 ? 0.2690 0.2479 0.1796 0.0446  0.0320  0.0593  250 TYR   A CA  
3788 C  C   . TYR   A 250 ? 0.2884 0.2750 0.1974 0.0492  0.0224  0.0532  250 TYR   A C   
3789 O  O   . TYR   A 250 ? 0.2674 0.2507 0.1830 0.0458  0.0189  0.0507  250 TYR   A O   
3790 C  CB  . TYR   A 250 ? 0.3134 0.2813 0.2128 0.0504  0.0409  0.0702  250 TYR   A CB  
3791 C  CG  . TYR   A 250 ? 0.3111 0.2663 0.2109 0.0501  0.0424  0.0739  250 TYR   A CG  
3792 C  CD1 . TYR   A 250 ? 0.3333 0.2903 0.2252 0.0591  0.0373  0.0741  250 TYR   A CD1 
3793 C  CD2 . TYR   A 250 ? 0.3511 0.2933 0.2594 0.0410  0.0489  0.0764  250 TYR   A CD2 
3794 C  CE1 . TYR   A 250 ? 0.3217 0.2666 0.2133 0.0600  0.0391  0.0777  250 TYR   A CE1 
3795 C  CE2 . TYR   A 250 ? 0.3808 0.3100 0.2888 0.0410  0.0506  0.0791  250 TYR   A CE2 
3796 C  CZ  . TYR   A 250 ? 0.3826 0.3128 0.2814 0.0513  0.0458  0.0802  250 TYR   A CZ  
3797 O  OH  . TYR   A 250 ? 0.4733 0.3907 0.3711 0.0526  0.0478  0.0831  250 TYR   A OH  
3807 N  N   . GLY   A 251 ? 0.3267 0.3242 0.2265 0.0575  0.0187  0.0508  251 GLY   A N   
3808 C  CA  . GLY   A 251 ? 0.3358 0.3427 0.2347 0.0618  0.0099  0.0442  251 GLY   A CA  
3809 C  C   . GLY   A 251 ? 0.3784 0.3800 0.2724 0.0675  0.0100  0.0494  251 GLY   A C   
3810 O  O   . GLY   A 251 ? 0.4040 0.3993 0.2864 0.0752  0.0158  0.0585  251 GLY   A O   
3814 N  N   . GLY   A 252 ? 0.3228 0.3272 0.2250 0.0645  0.0040  0.0439  252 GLY   A N   
3815 C  CA  . GLY   A 252 ? 0.3225 0.3225 0.2222 0.0694  0.0036  0.0476  252 GLY   A CA  
3816 C  C   . GLY   A 252 ? 0.3192 0.3044 0.2271 0.0616  0.0077  0.0504  252 GLY   A C   
3817 O  O   . GLY   A 252 ? 0.3387 0.3204 0.2471 0.0642  0.0064  0.0515  252 GLY   A O   
3821 N  N   . LEU   A 253 ? 0.2652 0.2425 0.1798 0.0523  0.0123  0.0511  253 LEU   A N   
3822 C  CA  . LEU   A 253 ? 0.2609 0.2261 0.1840 0.0443  0.0153  0.0520  253 LEU   A CA  
3823 C  C   . LEU   A 253 ? 0.2353 0.2070 0.1680 0.0402  0.0079  0.0441  253 LEU   A C   
3824 O  O   . LEU   A 253 ? 0.2387 0.2206 0.1769 0.0369  0.0028  0.0373  253 LEU   A O   
3825 C  CB  . LEU   A 253 ? 0.2615 0.2218 0.1913 0.0351  0.0205  0.0525  253 LEU   A CB  
3826 C  CG  . LEU   A 253 ? 0.2541 0.2037 0.1931 0.0261  0.0236  0.0522  253 LEU   A CG  
3827 C  CD1 . LEU   A 253 ? 0.2661 0.2004 0.1995 0.0287  0.0302  0.0591  253 LEU   A CD1 
3828 C  CD2 . LEU   A 253 ? 0.2776 0.2280 0.2243 0.0177  0.0275  0.0513  253 LEU   A CD2 
3840 N  N   . ASP   A 254 ? 0.2354 0.2001 0.1700 0.0401  0.0080  0.0450  254 ASP   A N   
3841 C  CA  . ASP   A 254 ? 0.2085 0.1795 0.1512 0.0371  0.0018  0.0382  254 ASP   A CA  
3842 C  C   . ASP   A 254 ? 0.1968 0.1683 0.1502 0.0267  0.0006  0.0331  254 ASP   A C   
3843 O  O   . ASP   A 254 ? 0.2022 0.1658 0.1586 0.0208  0.0050  0.0350  254 ASP   A O   
3844 C  CB  . ASP   A 254 ? 0.2323 0.1942 0.1747 0.0389  0.0034  0.0407  254 ASP   A CB  
3845 C  CG  . ASP   A 254 ? 0.2379 0.2075 0.1878 0.0371  -0.0025 0.0343  254 ASP   A CG  
3846 O  OD1 . ASP   A 254 ? 0.3075 0.2896 0.2560 0.0431  -0.0072 0.0317  254 ASP   A OD1 
3847 O  OD2 . ASP   A 254 ? 0.2334 0.1984 0.1904 0.0303  -0.0024 0.0317  254 ASP   A OD2 
3852 N  N   . VAL   A 255 ? 0.1833 0.1636 0.1431 0.0242  -0.0051 0.0265  255 VAL   A N   
3853 C  CA  . VAL   A 255 ? 0.1836 0.1648 0.1520 0.0163  -0.0065 0.0220  255 VAL   A CA  
3854 C  C   . VAL   A 255 ? 0.1688 0.1407 0.1416 0.0109  -0.0039 0.0232  255 VAL   A C   
3855 O  O   . VAL   A 255 ? 0.1785 0.1501 0.1569 0.0050  -0.0037 0.0212  255 VAL   A O   
3856 C  CB  . VAL   A 255 ? 0.1890 0.1797 0.1624 0.0154  -0.0119 0.0154  255 VAL   A CB  
3857 C  CG1 . VAL   A 255 ? 0.1906 0.1908 0.1611 0.0189  -0.0144 0.0124  255 VAL   A CG1 
3858 C  CG2 . VAL   A 255 ? 0.1809 0.1729 0.1561 0.0174  -0.0138 0.0145  255 VAL   A CG2 
3868 N  N   . HIS   A 256 ? 0.1809 0.1460 0.1516 0.0131  -0.0023 0.0256  256 HIS   A N   
3869 C  CA  . HIS   A 256 ? 0.1857 0.1419 0.1603 0.0078  0.0000  0.0254  256 HIS   A CA  
3870 C  C   . HIS   A 256 ? 0.1911 0.1379 0.1646 0.0047  0.0060  0.0291  256 HIS   A C   
3871 O  O   . HIS   A 256 ? 0.2028 0.1432 0.1806 -0.0009 0.0078  0.0275  256 HIS   A O   
3872 C  CB  . HIS   A 256 ? 0.2039 0.1557 0.1764 0.0117  -0.0002 0.0259  256 HIS   A CB  
3873 C  CG  . HIS   A 256 ? 0.1911 0.1527 0.1664 0.0138  -0.0052 0.0220  256 HIS   A CG  
3874 N  ND1 . HIS   A 256 ? 0.1999 0.1701 0.1721 0.0205  -0.0077 0.0220  256 HIS   A ND1 
3875 C  CD2 . HIS   A 256 ? 0.1826 0.1476 0.1640 0.0098  -0.0076 0.0177  256 HIS   A CD2 
3876 C  CE1 . HIS   A 256 ? 0.2243 0.2029 0.2020 0.0196  -0.0114 0.0174  256 HIS   A CE1 
3877 N  NE2 . HIS   A 256 ? 0.2214 0.1962 0.2042 0.0134  -0.0110 0.0153  256 HIS   A NE2 
3885 N  N   . TYR   A 257 ? 0.1925 0.1395 0.1612 0.0075  0.0089  0.0330  257 TYR   A N   
3886 C  CA  . TYR   A 257 ? 0.2011 0.1404 0.1695 0.0040  0.0156  0.0368  257 TYR   A CA  
3887 C  C   . TYR   A 257 ? 0.1954 0.1435 0.1675 0.0007  0.0153  0.0353  257 TYR   A C   
3888 O  O   . TYR   A 257 ? 0.2020 0.1490 0.1802 -0.0059 0.0187  0.0346  257 TYR   A O   
3889 C  CB  . TYR   A 257 ? 0.2056 0.1360 0.1639 0.0109  0.0212  0.0441  257 TYR   A CB  
3890 C  CG  . TYR   A 257 ? 0.2273 0.1491 0.1808 0.0161  0.0216  0.0460  257 TYR   A CG  
3891 C  CD1 . TYR   A 257 ? 0.2571 0.1725 0.2157 0.0116  0.0213  0.0426  257 TYR   A CD1 
3892 C  CD2 . TYR   A 257 ? 0.2917 0.2127 0.2349 0.0267  0.0223  0.0511  257 TYR   A CD2 
3893 C  CE1 . TYR   A 257 ? 0.3060 0.2140 0.2601 0.0175  0.0215  0.0440  257 TYR   A CE1 
3894 C  CE2 . TYR   A 257 ? 0.3396 0.2541 0.2784 0.0330  0.0223  0.0529  257 TYR   A CE2 
3895 C  CZ  . TYR   A 257 ? 0.3089 0.2163 0.2533 0.0280  0.0224  0.0494  257 TYR   A CZ  
3896 O  OH  . TYR   A 257 ? 0.4836 0.3841 0.4240 0.0345  0.0228  0.0508  257 TYR   A OH  
3906 N  N   . SER   A 258 ? 0.1841 0.1420 0.1534 0.0051  0.0114  0.0340  258 SER   A N   
3907 C  CA  . SER   A 258 ? 0.1679 0.1339 0.1407 0.0027  0.0110  0.0319  258 SER   A CA  
3908 C  C   . SER   A 258 ? 0.1714 0.1420 0.1532 -0.0030 0.0072  0.0264  258 SER   A C   
3909 O  O   . SER   A 258 ? 0.1748 0.1511 0.1607 -0.0054 0.0076  0.0249  258 SER   A O   
3910 C  CB  . SER   A 258 ? 0.1916 0.1656 0.1584 0.0091  0.0079  0.0310  258 SER   A CB  
3911 O  OG  . SER   A 258 ? 0.2029 0.1818 0.1716 0.0101  0.0018  0.0261  258 SER   A OG  
3917 N  N   . SER   A 259 ? 0.1598 0.1285 0.1443 -0.0043 0.0039  0.0237  259 SER   A N   
3918 C  CA  . SER   A 259 ? 0.1510 0.1228 0.1426 -0.0090 0.0011  0.0195  259 SER   A CA  
3919 C  C   . SER   A 259 ? 0.1433 0.1144 0.1406 -0.0148 0.0044  0.0194  259 SER   A C   
3920 O  O   . SER   A 259 ? 0.1521 0.1287 0.1551 -0.0178 0.0020  0.0160  259 SER   A O   
3921 C  CB  . SER   A 259 ? 0.1656 0.1345 0.1576 -0.0089 -0.0017 0.0175  259 SER   A CB  
3922 O  OG  . SER   A 259 ? 0.1806 0.1410 0.1707 -0.0093 0.0013  0.0197  259 SER   A OG  
3928 N  N   . GLY   A 260 ? 0.1638 0.1286 0.1600 -0.0164 0.0097  0.0226  260 GLY   A N   
3929 C  CA  . GLY   A 260 ? 0.1506 0.1160 0.1539 -0.0230 0.0133  0.0215  260 GLY   A CA  
3930 C  C   . GLY   A 260 ? 0.1540 0.1309 0.1625 -0.0243 0.0127  0.0199  260 GLY   A C   
3931 O  O   . GLY   A 260 ? 0.1573 0.1403 0.1738 -0.0293 0.0125  0.0165  260 GLY   A O   
3935 N  N   . VAL   A 261 ? 0.1570 0.1377 0.1609 -0.0194 0.0126  0.0220  261 VAL   A N   
3936 C  CA  . VAL   A 261 ? 0.1554 0.1465 0.1639 -0.0198 0.0130  0.0207  261 VAL   A CA  
3937 C  C   . VAL   A 261 ? 0.1398 0.1383 0.1537 -0.0204 0.0077  0.0160  261 VAL   A C   
3938 O  O   . VAL   A 261 ? 0.1485 0.1549 0.1700 -0.0238 0.0080  0.0138  261 VAL   A O   
3939 C  CB  . VAL   A 261 ? 0.1529 0.1461 0.1543 -0.0136 0.0134  0.0228  261 VAL   A CB  
3940 C  CG1 . VAL   A 261 ? 0.1686 0.1723 0.1744 -0.0132 0.0140  0.0213  261 VAL   A CG1 
3941 C  CG2 . VAL   A 261 ? 0.2009 0.1874 0.1952 -0.0115 0.0189  0.0284  261 VAL   A CG2 
3951 N  N   . TYR   A 262 ? 0.1334 0.1300 0.1436 -0.0170 0.0031  0.0146  262 TYR   A N   
3952 C  CA  . TYR   A 262 ? 0.1204 0.1219 0.1338 -0.0165 -0.0010 0.0114  262 TYR   A CA  
3953 C  C   . TYR   A 262 ? 0.1252 0.1265 0.1426 -0.0203 -0.0026 0.0092  262 TYR   A C   
3954 O  O   . TYR   A 262 ? 0.1379 0.1458 0.1590 -0.0203 -0.0051 0.0068  262 TYR   A O   
3955 C  CB  . TYR   A 262 ? 0.1545 0.1533 0.1631 -0.0122 -0.0040 0.0106  262 TYR   A CB  
3956 C  CG  . TYR   A 262 ? 0.1382 0.1411 0.1456 -0.0085 -0.0036 0.0101  262 TYR   A CG  
3957 C  CD1 . TYR   A 262 ? 0.1638 0.1682 0.1683 -0.0068 -0.0008 0.0117  262 TYR   A CD1 
3958 C  CD2 . TYR   A 262 ? 0.1476 0.1524 0.1560 -0.0061 -0.0055 0.0083  262 TYR   A CD2 
3959 C  CE1 . TYR   A 262 ? 0.1494 0.1578 0.1526 -0.0031 -0.0001 0.0106  262 TYR   A CE1 
3960 C  CE2 . TYR   A 262 ? 0.1599 0.1670 0.1668 -0.0023 -0.0046 0.0075  262 TYR   A CE2 
3961 C  CZ  . TYR   A 262 ? 0.1508 0.1602 0.1555 -0.0011 -0.0021 0.0083  262 TYR   A CZ  
3962 O  OH  . TYR   A 262 ? 0.1764 0.1879 0.1793 0.0030  -0.0012 0.0067  262 TYR   A OH  
3972 N  N   . ASN   A 263 ? 0.1281 0.1218 0.1442 -0.0230 -0.0012 0.0098  263 ASN   A N   
3973 C  CA  . ASN   A 263 ? 0.1369 0.1303 0.1565 -0.0269 -0.0024 0.0067  263 ASN   A CA  
3974 C  C   . ASN   A 263 ? 0.1418 0.1435 0.1695 -0.0318 -0.0007 0.0042  263 ASN   A C   
3975 O  O   . ASN   A 263 ? 0.1449 0.1546 0.1771 -0.0332 -0.0038 0.0001  263 ASN   A O   
3976 C  CB  . ASN   A 263 ? 0.1484 0.1306 0.1646 -0.0282 -0.0004 0.0078  263 ASN   A CB  
3977 C  CG  . ASN   A 263 ? 0.1705 0.1478 0.1810 -0.0241 -0.0031 0.0085  263 ASN   A CG  
3978 O  OD1 . ASN   A 263 ? 0.1789 0.1602 0.1883 -0.0210 -0.0061 0.0081  263 ASN   A OD1 
3979 N  ND2 . ASN   A 263 ? 0.1837 0.1521 0.1911 -0.0240 -0.0015 0.0093  263 ASN   A ND2 
3986 N  N   . HIS   A 264 ? 0.1296 0.1307 0.1594 -0.0342 0.0043  0.0063  264 HIS   A N   
3987 C  CA  . HIS   A 264 ? 0.1370 0.1472 0.1761 -0.0398 0.0069  0.0037  264 HIS   A CA  
3988 C  C   . HIS   A 264 ? 0.1307 0.1558 0.1741 -0.0369 0.0038  0.0019  264 HIS   A C   
3989 O  O   . HIS   A 264 ? 0.1344 0.1713 0.1858 -0.0398 0.0019  -0.0027 264 HIS   A O   
3990 C  CB  . HIS   A 264 ? 0.1384 0.1428 0.1776 -0.0425 0.0143  0.0077  264 HIS   A CB  
3991 C  CG  . HIS   A 264 ? 0.1539 0.1647 0.2037 -0.0503 0.0188  0.0049  264 HIS   A CG  
3992 N  ND1 . HIS   A 264 ? 0.1920 0.2016 0.2438 -0.0529 0.0263  0.0086  264 HIS   A ND1 
3993 C  CD2 . HIS   A 264 ? 0.1720 0.1907 0.2312 -0.0567 0.0172  -0.0017 264 HIS   A CD2 
3994 C  CE1 . HIS   A 264 ? 0.2217 0.2389 0.2854 -0.0613 0.0295  0.0041  264 HIS   A CE1 
3995 N  NE2 . HIS   A 264 ? 0.1997 0.2227 0.2682 -0.0639 0.0238  -0.0027 264 HIS   A NE2 
4003 N  N   . LEU   A 265 ? 0.1389 0.1638 0.1767 -0.0305 0.0029  0.0050  265 LEU   A N   
4004 C  CA  . LEU   A 265 ? 0.1394 0.1759 0.1797 -0.0261 0.0003  0.0039  265 LEU   A CA  
4005 C  C   . LEU   A 265 ? 0.1371 0.1786 0.1783 -0.0243 -0.0050 0.0007  265 LEU   A C   
4006 O  O   . LEU   A 265 ? 0.1386 0.1935 0.1856 -0.0232 -0.0069 -0.0019 265 LEU   A O   
4007 C  CB  . LEU   A 265 ? 0.1323 0.1637 0.1650 -0.0199 0.0005  0.0070  265 LEU   A CB  
4008 C  CG  . LEU   A 265 ? 0.1418 0.1806 0.1746 -0.0140 -0.0016 0.0063  265 LEU   A CG  
4009 C  CD1 . LEU   A 265 ? 0.1578 0.2110 0.1986 -0.0142 0.0004  0.0052  265 LEU   A CD1 
4010 C  CD2 . LEU   A 265 ? 0.1616 0.1928 0.1866 -0.0090 -0.0010 0.0082  265 LEU   A CD2 
4022 N  N   . PHE   A 266 ? 0.1254 0.1571 0.1604 -0.0232 -0.0074 0.0010  266 PHE   A N   
4023 C  CA  . PHE   A 266 ? 0.1184 0.1537 0.1525 -0.0207 -0.0118 -0.0012 266 PHE   A CA  
4024 C  C   . PHE   A 266 ? 0.1148 0.1600 0.1558 -0.0253 -0.0134 -0.0061 266 PHE   A C   
4025 O  O   . PHE   A 266 ? 0.1408 0.1981 0.1842 -0.0224 -0.0168 -0.0086 266 PHE   A O   
4026 C  CB  . PHE   A 266 ? 0.1398 0.1626 0.1665 -0.0195 -0.0129 0.0003  266 PHE   A CB  
4027 C  CG  . PHE   A 266 ? 0.1389 0.1634 0.1627 -0.0164 -0.0164 -0.0010 266 PHE   A CG  
4028 C  CD1 . PHE   A 266 ? 0.1543 0.1811 0.1751 -0.0102 -0.0178 0.0007  266 PHE   A CD1 
4029 C  CD2 . PHE   A 266 ? 0.1743 0.1962 0.1972 -0.0191 -0.0177 -0.0034 266 PHE   A CD2 
4030 C  CE1 . PHE   A 266 ? 0.1798 0.2067 0.1963 -0.0065 -0.0200 0.0008  266 PHE   A CE1 
4031 C  CE2 . PHE   A 266 ? 0.1789 0.2021 0.1975 -0.0153 -0.0205 -0.0039 266 PHE   A CE2 
4032 C  CZ  . PHE   A 266 ? 0.1664 0.1925 0.1819 -0.0091 -0.0215 -0.0015 266 PHE   A CZ  
4042 N  N   . TYR   A 267 ? 0.1268 0.1675 0.1711 -0.0323 -0.0107 -0.0079 267 TYR   A N   
4043 C  CA  . TYR   A 267 ? 0.1278 0.1773 0.1798 -0.0382 -0.0116 -0.0140 267 TYR   A CA  
4044 C  C   . TYR   A 267 ? 0.1173 0.1849 0.1791 -0.0393 -0.0115 -0.0167 267 TYR   A C   
4045 O  O   . TYR   A 267 ? 0.1318 0.2145 0.1991 -0.0394 -0.0154 -0.0221 267 TYR   A O   
4046 C  CB  . TYR   A 267 ? 0.1516 0.1898 0.2056 -0.0459 -0.0067 -0.0148 267 TYR   A CB  
4047 C  CG  . TYR   A 267 ? 0.1406 0.1864 0.2038 -0.0536 -0.0066 -0.0221 267 TYR   A CG  
4048 C  CD1 . TYR   A 267 ? 0.1657 0.2103 0.2273 -0.0551 -0.0101 -0.0275 267 TYR   A CD1 
4049 C  CD2 . TYR   A 267 ? 0.1590 0.2134 0.2329 -0.0602 -0.0026 -0.0246 267 TYR   A CD2 
4050 C  CE1 . TYR   A 267 ? 0.1911 0.2432 0.2615 -0.0629 -0.0101 -0.0360 267 TYR   A CE1 
4051 C  CE2 . TYR   A 267 ? 0.1818 0.2445 0.2658 -0.0686 -0.0024 -0.0330 267 TYR   A CE2 
4052 C  CZ  . TYR   A 267 ? 0.1595 0.2207 0.2414 -0.0698 -0.0065 -0.0389 267 TYR   A CZ  
4053 O  OH  . TYR   A 267 ? 0.2657 0.3351 0.3584 -0.0791 -0.0061 -0.0486 267 TYR   A OH  
4063 N  N   . ILE   A 268 ? 0.1173 0.1850 0.1817 -0.0399 -0.0069 -0.0133 268 ILE   A N   
4064 C  CA  . ILE   A 268 ? 0.1216 0.2074 0.1963 -0.0410 -0.0059 -0.0157 268 ILE   A CA  
4065 C  C   . ILE   A 268 ? 0.1248 0.2241 0.1985 -0.0322 -0.0113 -0.0162 268 ILE   A C   
4066 O  O   . ILE   A 268 ? 0.1366 0.2550 0.2189 -0.0325 -0.0140 -0.0212 268 ILE   A O   
4067 C  CB  . ILE   A 268 ? 0.1383 0.2202 0.2136 -0.0418 0.0006  -0.0109 268 ILE   A CB  
4068 C  CG1 . ILE   A 268 ? 0.1477 0.2189 0.2256 -0.0506 0.0070  -0.0104 268 ILE   A CG1 
4069 C  CG2 . ILE   A 268 ? 0.1363 0.2374 0.2210 -0.0407 0.0016  -0.0124 268 ILE   A CG2 
4070 C  CD1 . ILE   A 268 ? 0.1979 0.2594 0.2707 -0.0493 0.0134  -0.0037 268 ILE   A CD1 
4082 N  N   . LEU   A 269 ? 0.1266 0.2163 0.1899 -0.0242 -0.0126 -0.0112 269 LEU   A N   
4083 C  CA  . LEU   A 269 ? 0.1199 0.2185 0.1806 -0.0148 -0.0163 -0.0104 269 LEU   A CA  
4084 C  C   . LEU   A 269 ? 0.1191 0.2257 0.1791 -0.0126 -0.0218 -0.0140 269 LEU   A C   
4085 O  O   . LEU   A 269 ? 0.1323 0.2563 0.1964 -0.0079 -0.0249 -0.0164 269 LEU   A O   
4086 C  CB  . LEU   A 269 ? 0.1370 0.2201 0.1869 -0.0084 -0.0154 -0.0048 269 LEU   A CB  
4087 C  CG  . LEU   A 269 ? 0.1290 0.2163 0.1743 0.0019  -0.0179 -0.0030 269 LEU   A CG  
4088 C  CD1 . LEU   A 269 ? 0.1518 0.2565 0.2044 0.0057  -0.0173 -0.0041 269 LEU   A CD1 
4089 C  CD2 . LEU   A 269 ? 0.1619 0.2318 0.1976 0.0060  -0.0161 0.0013  269 LEU   A CD2 
4101 N  N   . ALA   A 270 ? 0.1179 0.2132 0.1727 -0.0157 -0.0229 -0.0148 270 ALA   A N   
4102 C  CA  . ALA   A 270 ? 0.1206 0.2229 0.1732 -0.0134 -0.0279 -0.0184 270 ALA   A CA  
4103 C  C   . ALA   A 270 ? 0.1541 0.2758 0.2176 -0.0185 -0.0304 -0.0263 270 ALA   A C   
4104 O  O   . ALA   A 270 ? 0.1684 0.3027 0.2308 -0.0142 -0.0355 -0.0300 270 ALA   A O   
4105 C  CB  . ALA   A 270 ? 0.1556 0.2416 0.2015 -0.0167 -0.0275 -0.0180 270 ALA   A CB  
4111 N  N   . ASN   A 271 ? 0.1250 0.2506 0.1990 -0.0273 -0.0268 -0.0293 271 ASN   A N   
4112 C  CA  . ASN   A 271 ? 0.1666 0.3108 0.2533 -0.0342 -0.0283 -0.0381 271 ASN   A CA  
4113 C  C   . ASN   A 271 ? 0.1626 0.3280 0.2602 -0.0328 -0.0278 -0.0396 271 ASN   A C   
4114 O  O   . ASN   A 271 ? 0.1816 0.3652 0.2924 -0.0398 -0.0284 -0.0475 271 ASN   A O   
4115 C  CB  . ASN   A 271 ? 0.1720 0.3043 0.2636 -0.0464 -0.0233 -0.0409 271 ASN   A CB  
4116 C  CG  . ASN   A 271 ? 0.2128 0.3325 0.2974 -0.0485 -0.0251 -0.0434 271 ASN   A CG  
4117 O  OD1 . ASN   A 271 ? 0.2730 0.4046 0.3609 -0.0504 -0.0297 -0.0515 271 ASN   A OD1 
4118 N  ND2 . ASN   A 271 ? 0.1999 0.2981 0.2748 -0.0473 -0.0225 -0.0375 271 ASN   A ND2 
4125 N  N   . GLN   A 272 ? 0.1389 0.3035 0.2320 -0.0242 -0.0267 -0.0330 272 GLN   A N   
4126 C  CA  . GLN   A 272 ? 0.1414 0.3281 0.2442 -0.0208 -0.0269 -0.0345 272 GLN   A CA  
4127 C  C   . GLN   A 272 ? 0.1566 0.3667 0.2623 -0.0145 -0.0342 -0.0401 272 GLN   A C   
4128 O  O   . GLN   A 272 ? 0.1557 0.3614 0.2510 -0.0080 -0.0388 -0.0392 272 GLN   A O   
4129 C  CB  . GLN   A 272 ? 0.1329 0.3124 0.2285 -0.0113 -0.0244 -0.0266 272 GLN   A CB  
4130 C  CG  . GLN   A 272 ? 0.1412 0.3031 0.2346 -0.0160 -0.0175 -0.0217 272 GLN   A CG  
4131 C  CD  . GLN   A 272 ? 0.1786 0.3498 0.2846 -0.0245 -0.0120 -0.0240 272 GLN   A CD  
4132 O  OE1 . GLN   A 272 ? 0.2105 0.4039 0.3297 -0.0278 -0.0127 -0.0299 272 GLN   A OE1 
4133 N  NE2 . GLN   A 272 ? 0.1933 0.3479 0.2952 -0.0278 -0.0058 -0.0191 272 GLN   A NE2 
4142 N  N   . PRO   A 273 ? 0.1765 0.4131 0.2959 -0.0152 -0.0354 -0.0457 273 PRO   A N   
4143 C  CA  . PRO   A 273 ? 0.1762 0.4368 0.2967 -0.0064 -0.0428 -0.0503 273 PRO   A CA  
4144 C  C   . PRO   A 273 ? 0.1610 0.4146 0.2665 0.0097  -0.0451 -0.0419 273 PRO   A C   
4145 O  O   . PRO   A 273 ? 0.1913 0.4331 0.2919 0.0150  -0.0408 -0.0345 273 PRO   A O   
4146 C  CB  . PRO   A 273 ? 0.1917 0.4715 0.3251 -0.0086 -0.0407 -0.0543 273 PRO   A CB  
4147 C  CG  . PRO   A 273 ? 0.2087 0.4815 0.3533 -0.0235 -0.0336 -0.0561 273 PRO   A CG  
4148 C  CD  . PRO   A 273 ? 0.1632 0.4100 0.2971 -0.0231 -0.0298 -0.0477 273 PRO   A CD  
4156 N  N   . ASN   A 274 ? 0.1874 0.4442 0.2839 0.0172  -0.0508 -0.0427 274 ASN   A N   
4157 C  CA  . ASN   A 274 ? 0.2263 0.4773 0.3080 0.0330  -0.0529 -0.0350 274 ASN   A CA  
4158 C  C   . ASN   A 274 ? 0.1602 0.3780 0.2278 0.0330  -0.0487 -0.0269 274 ASN   A C   
4159 O  O   . ASN   A 274 ? 0.2214 0.4287 0.2766 0.0446  -0.0482 -0.0196 274 ASN   A O   
4160 C  CB  . ASN   A 274 ? 0.2294 0.4881 0.3115 0.0438  -0.0510 -0.0304 274 ASN   A CB  
4161 C  CG  . ASN   A 274 ? 0.3109 0.5924 0.4033 0.0426  -0.0520 -0.0371 274 ASN   A CG  
4162 O  OD1 . ASN   A 274 ? 0.3005 0.5926 0.3919 0.0428  -0.0559 -0.0426 274 ASN   A OD1 
4163 N  ND2 . ASN   A 274 ? 0.3310 0.6206 0.4336 0.0408  -0.0482 -0.0370 274 ASN   A ND2 
4170 N  N   . TRP   A 275 ? 0.1648 0.3659 0.2340 0.0207  -0.0453 -0.0281 275 TRP   A N   
4171 C  CA  . TRP   A 275 ? 0.1358 0.3086 0.1928 0.0202  -0.0421 -0.0217 275 TRP   A CA  
4172 C  C   . TRP   A 275 ? 0.1509 0.3175 0.2040 0.0147  -0.0444 -0.0253 275 TRP   A C   
4173 O  O   . TRP   A 275 ? 0.1753 0.3576 0.2353 0.0099  -0.0482 -0.0334 275 TRP   A O   
4174 C  CB  . TRP   A 275 ? 0.1507 0.3086 0.2114 0.0122  -0.0359 -0.0192 275 TRP   A CB  
4175 C  CG  . TRP   A 275 ? 0.1491 0.3054 0.2082 0.0198  -0.0329 -0.0138 275 TRP   A CG  
4176 C  CD1 . TRP   A 275 ? 0.1563 0.3324 0.2244 0.0233  -0.0329 -0.0156 275 TRP   A CD1 
4177 C  CD2 . TRP   A 275 ? 0.1407 0.2764 0.1897 0.0246  -0.0294 -0.0071 275 TRP   A CD2 
4178 N  NE1 . TRP   A 275 ? 0.1486 0.3160 0.2115 0.0308  -0.0296 -0.0100 275 TRP   A NE1 
4179 C  CE2 . TRP   A 275 ? 0.1371 0.2795 0.1882 0.0315  -0.0274 -0.0050 275 TRP   A CE2 
4180 C  CE3 . TRP   A 275 ? 0.1390 0.2521 0.1777 0.0241  -0.0277 -0.0030 275 TRP   A CE3 
4181 C  CZ2 . TRP   A 275 ? 0.1459 0.2710 0.1888 0.0370  -0.0236 0.0004  275 TRP   A CZ2 
4182 C  CZ3 . TRP   A 275 ? 0.1501 0.2478 0.1818 0.0291  -0.0241 0.0021  275 TRP   A CZ3 
4183 C  CH2 . TRP   A 275 ? 0.1372 0.2403 0.1706 0.0355  -0.0222 0.0036  275 TRP   A CH2 
4194 N  N   . ASN   A 276 ? 0.1532 0.2974 0.1952 0.0157  -0.0421 -0.0198 276 ASN   A N   
4195 C  CA  . ASN   A 276 ? 0.1650 0.2999 0.2020 0.0110  -0.0432 -0.0222 276 ASN   A CA  
4196 C  C   . ASN   A 276 ? 0.1697 0.2794 0.1993 0.0091  -0.0385 -0.0159 276 ASN   A C   
4197 O  O   . ASN   A 276 ? 0.1548 0.2554 0.1831 0.0115  -0.0350 -0.0106 276 ASN   A O   
4198 C  CB  . ASN   A 276 ? 0.1538 0.2971 0.1821 0.0198  -0.0479 -0.0228 276 ASN   A CB  
4199 C  CG  . ASN   A 276 ? 0.1976 0.3345 0.2146 0.0327  -0.0467 -0.0141 276 ASN   A CG  
4200 O  OD1 . ASN   A 276 ? 0.2012 0.3203 0.2139 0.0335  -0.0421 -0.0078 276 ASN   A OD1 
4201 N  ND2 . ASN   A 276 ? 0.2791 0.4316 0.2914 0.0432  -0.0509 -0.0143 276 ASN   A ND2 
4208 N  N   . LEU   A 277 ? 0.1465 0.2457 0.1717 0.0051  -0.0384 -0.0171 277 LEU   A N   
4209 C  CA  . LEU   A 277 ? 0.1566 0.2346 0.1760 0.0029  -0.0344 -0.0122 277 LEU   A CA  
4210 C  C   . LEU   A 277 ? 0.1509 0.2194 0.1613 0.0116  -0.0325 -0.0049 277 LEU   A C   
4211 O  O   . LEU   A 277 ? 0.1531 0.2088 0.1625 0.0106  -0.0288 -0.0009 277 LEU   A O   
4212 C  CB  . LEU   A 277 ? 0.1685 0.2393 0.1846 -0.0016 -0.0349 -0.0152 277 LEU   A CB  
4213 C  CG  . LEU   A 277 ? 0.2238 0.2751 0.2342 -0.0028 -0.0311 -0.0104 277 LEU   A CG  
4214 C  CD1 . LEU   A 277 ? 0.2861 0.3308 0.2977 -0.0099 -0.0305 -0.0145 277 LEU   A CD1 
4215 C  CD2 . LEU   A 277 ? 0.2050 0.2497 0.2055 0.0046  -0.0304 -0.0052 277 LEU   A CD2 
4227 N  N   . ARG   A 278 ? 0.1621 0.2366 0.1656 0.0201  -0.0347 -0.0033 278 ARG   A N   
4228 C  CA  . ARG   A 278 ? 0.1771 0.2398 0.1715 0.0281  -0.0316 0.0041  278 ARG   A CA  
4229 C  C   . ARG   A 278 ? 0.1659 0.2269 0.1627 0.0314  -0.0292 0.0073  278 ARG   A C   
4230 O  O   . ARG   A 278 ? 0.1786 0.2239 0.1717 0.0320  -0.0250 0.0116  278 ARG   A O   
4231 C  CB  . ARG   A 278 ? 0.2005 0.2705 0.1862 0.0379  -0.0338 0.0060  278 ARG   A CB  
4232 C  CG  . ARG   A 278 ? 0.2490 0.3144 0.2283 0.0363  -0.0343 0.0049  278 ARG   A CG  
4233 C  CD  . ARG   A 278 ? 0.3370 0.4045 0.3041 0.0476  -0.0346 0.0094  278 ARG   A CD  
4234 N  NE  . ARG   A 278 ? 0.3011 0.3516 0.2610 0.0530  -0.0286 0.0181  278 ARG   A NE  
4235 C  CZ  . ARG   A 278 ? 0.3810 0.4277 0.3292 0.0634  -0.0263 0.0245  278 ARG   A CZ  
4236 N  NH1 . ARG   A 278 ? 0.3537 0.4134 0.2948 0.0703  -0.0301 0.0234  278 ARG   A NH1 
4237 N  NH2 . ARG   A 278 ? 0.3740 0.4034 0.3172 0.0670  -0.0198 0.0319  278 ARG   A NH2 
4251 N  N   . MET   A 279 ? 0.1682 0.2455 0.1714 0.0336  -0.0316 0.0046  279 MET   A N   
4252 C  CA  A MET   A 279 ? 0.1822 0.2585 0.1875 0.0375  -0.0291 0.0074  279 MET   A CA  
4253 C  CA  B MET   A 279 ? 0.1833 0.2595 0.1886 0.0375  -0.0291 0.0074  279 MET   A CA  
4254 C  C   . MET   A 279 ? 0.1581 0.2232 0.1679 0.0291  -0.0257 0.0069  279 MET   A C   
4255 O  O   . MET   A 279 ? 0.1588 0.2127 0.1660 0.0315  -0.0221 0.0102  279 MET   A O   
4256 C  CB  A MET   A 279 ? 0.1789 0.2781 0.1922 0.0405  -0.0324 0.0036  279 MET   A CB  
4257 C  CB  B MET   A 279 ? 0.1813 0.2800 0.1947 0.0405  -0.0323 0.0038  279 MET   A CB  
4258 C  CG  A MET   A 279 ? 0.1774 0.2895 0.1853 0.0519  -0.0359 0.0048  279 MET   A CG  
4259 C  CG  B MET   A 279 ? 0.1784 0.2905 0.1870 0.0515  -0.0357 0.0047  279 MET   A CG  
4260 S  SD  A MET   A 279 ? 0.2243 0.3688 0.2440 0.0545  -0.0410 -0.0016 279 MET   A SD  
4261 S  SD  B MET   A 279 ? 0.2004 0.3431 0.2222 0.0527  -0.0399 -0.0016 279 MET   A SD  
4262 C  CE  A MET   A 279 ? 0.1507 0.2900 0.1744 0.0568  -0.0361 0.0019  279 MET   A CE  
4263 C  CE  B MET   A 279 ? 0.1502 0.3053 0.1622 0.0685  -0.0440 0.0012  279 MET   A CE  
4282 N  N   . ALA   A 280 ? 0.1483 0.2165 0.1648 0.0195  -0.0265 0.0026  280 ALA   A N   
4283 C  CA  . ALA   A 280 ? 0.1593 0.2177 0.1788 0.0127  -0.0233 0.0027  280 ALA   A CA  
4284 C  C   . ALA   A 280 ? 0.1455 0.1855 0.1578 0.0124  -0.0208 0.0060  280 ALA   A C   
4285 O  O   . ALA   A 280 ? 0.1553 0.1863 0.1667 0.0120  -0.0180 0.0076  280 ALA   A O   
4286 C  CB  . ALA   A 280 ? 0.1403 0.2034 0.1668 0.0034  -0.0239 -0.0018 280 ALA   A CB  
4292 N  N   . PHE   A 281 ? 0.1393 0.1744 0.1466 0.0126  -0.0218 0.0065  281 PHE   A N   
4293 C  CA  . PHE   A 281 ? 0.1473 0.1667 0.1493 0.0117  -0.0191 0.0092  281 PHE   A CA  
4294 C  C   . PHE   A 281 ? 0.1468 0.1583 0.1436 0.0184  -0.0163 0.0132  281 PHE   A C   
4295 O  O   . PHE   A 281 ? 0.1622 0.1618 0.1578 0.0165  -0.0133 0.0142  281 PHE   A O   
4296 C  CB  . PHE   A 281 ? 0.1450 0.1620 0.1432 0.0104  -0.0202 0.0086  281 PHE   A CB  
4297 C  CG  . PHE   A 281 ? 0.1516 0.1555 0.1473 0.0073  -0.0175 0.0101  281 PHE   A CG  
4298 C  CD1 . PHE   A 281 ? 0.1799 0.1796 0.1792 0.0018  -0.0166 0.0086  281 PHE   A CD1 
4299 C  CD2 . PHE   A 281 ? 0.1725 0.1694 0.1621 0.0104  -0.0156 0.0130  281 PHE   A CD2 
4300 C  CE1 . PHE   A 281 ? 0.1628 0.1532 0.1608 -0.0007 -0.0147 0.0092  281 PHE   A CE1 
4301 C  CE2 . PHE   A 281 ? 0.1741 0.1611 0.1633 0.0067  -0.0129 0.0136  281 PHE   A CE2 
4302 C  CZ  . PHE   A 281 ? 0.1758 0.1609 0.1695 0.0016  -0.0130 0.0114  281 PHE   A CZ  
4312 N  N   . ASP   A 282 ? 0.1554 0.1730 0.1493 0.0263  -0.0170 0.0152  282 ASP   A N   
4313 C  CA  . ASP   A 282 ? 0.1795 0.1873 0.1680 0.0333  -0.0133 0.0194  282 ASP   A CA  
4314 C  C   . ASP   A 282 ? 0.1642 0.1677 0.1564 0.0314  -0.0111 0.0181  282 ASP   A C   
4315 O  O   . ASP   A 282 ? 0.1778 0.1674 0.1669 0.0320  -0.0073 0.0195  282 ASP   A O   
4316 C  CB  . ASP   A 282 ? 0.1789 0.1964 0.1643 0.0434  -0.0147 0.0217  282 ASP   A CB  
4317 C  CG  . ASP   A 282 ? 0.2245 0.2472 0.2040 0.0482  -0.0168 0.0234  282 ASP   A CG  
4318 O  OD1 . ASP   A 282 ? 0.2253 0.2397 0.2006 0.0452  -0.0156 0.0244  282 ASP   A OD1 
4319 O  OD2 . ASP   A 282 ? 0.2184 0.2551 0.1965 0.0564  -0.0196 0.0238  282 ASP   A OD2 
4324 N  N   . VAL   A 283 ? 0.1517 0.1670 0.1505 0.0290  -0.0132 0.0151  283 VAL   A N   
4325 C  CA  . VAL   A 283 ? 0.1613 0.1739 0.1626 0.0278  -0.0110 0.0139  283 VAL   A CA  
4326 C  C   . VAL   A 283 ? 0.1474 0.1488 0.1485 0.0209  -0.0095 0.0125  283 VAL   A C   
4327 O  O   . VAL   A 283 ? 0.1655 0.1578 0.1647 0.0215  -0.0068 0.0120  283 VAL   A O   
4328 C  CB  . VAL   A 283 ? 0.1513 0.1801 0.1602 0.0261  -0.0128 0.0113  283 VAL   A CB  
4329 C  CG1 . VAL   A 283 ? 0.1660 0.1929 0.1770 0.0243  -0.0103 0.0101  283 VAL   A CG1 
4330 C  CG2 . VAL   A 283 ? 0.1695 0.2115 0.1796 0.0338  -0.0144 0.0120  283 VAL   A CG2 
4340 N  N   . MET   A 284 ? 0.1435 0.1468 0.1468 0.0146  -0.0113 0.0111  284 MET   A N   
4341 C  CA  . MET   A 284 ? 0.1415 0.1367 0.1446 0.0090  -0.0104 0.0098  284 MET   A CA  
4342 C  C   . MET   A 284 ? 0.1507 0.1337 0.1499 0.0095  -0.0083 0.0106  284 MET   A C   
4343 O  O   . MET   A 284 ? 0.1606 0.1373 0.1598 0.0073  -0.0067 0.0088  284 MET   A O   
4344 C  CB  . MET   A 284 ? 0.1613 0.1607 0.1670 0.0036  -0.0124 0.0086  284 MET   A CB  
4345 C  CG  . MET   A 284 ? 0.1560 0.1661 0.1668 0.0015  -0.0134 0.0073  284 MET   A CG  
4346 S  SD  . MET   A 284 ? 0.1675 0.1782 0.1799 0.0005  -0.0110 0.0069  284 MET   A SD  
4347 C  CE  . MET   A 284 ? 0.1885 0.2095 0.2074 -0.0045 -0.0109 0.0059  284 MET   A CE  
4357 N  N   . VAL   A 285 ? 0.1653 0.1456 0.1612 0.0121  -0.0078 0.0131  285 VAL   A N   
4358 C  CA  . VAL   A 285 ? 0.1625 0.1305 0.1552 0.0120  -0.0044 0.0144  285 VAL   A CA  
4359 C  C   . VAL   A 285 ? 0.1660 0.1252 0.1571 0.0152  -0.0009 0.0144  285 VAL   A C   
4360 O  O   . VAL   A 285 ? 0.1810 0.1312 0.1728 0.0118  0.0018  0.0123  285 VAL   A O   
4361 C  CB  . VAL   A 285 ? 0.1738 0.1404 0.1620 0.0153  -0.0038 0.0180  285 VAL   A CB  
4362 C  CG1 . VAL   A 285 ? 0.1976 0.1504 0.1823 0.0160  0.0015  0.0204  285 VAL   A CG1 
4363 C  CG2 . VAL   A 285 ? 0.1884 0.1617 0.1782 0.0113  -0.0068 0.0166  285 VAL   A CG2 
4373 N  N   . LYS   A 286 ? 0.1633 0.1254 0.1525 0.0219  -0.0006 0.0163  286 LYS   A N   
4374 C  CA  . LYS   A 286 ? 0.1910 0.1436 0.1779 0.0260  0.0032  0.0163  286 LYS   A CA  
4375 C  C   . LYS   A 286 ? 0.1878 0.1403 0.1780 0.0219  0.0030  0.0114  286 LYS   A C   
4376 O  O   . LYS   A 286 ? 0.1983 0.1395 0.1875 0.0210  0.0064  0.0090  286 LYS   A O   
4377 C  CB  . LYS   A 286 ? 0.1993 0.1570 0.1833 0.0354  0.0032  0.0196  286 LYS   A CB  
4378 C  CG  . LYS   A 286 ? 0.2495 0.1952 0.2301 0.0408  0.0079  0.0199  286 LYS   A CG  
4379 C  CD  . LYS   A 286 ? 0.3100 0.2598 0.2865 0.0522  0.0084  0.0242  286 LYS   A CD  
4380 C  CE  . LYS   A 286 ? 0.3624 0.3050 0.3317 0.0585  0.0109  0.0303  286 LYS   A CE  
4381 N  NZ  . LYS   A 286 ? 0.4705 0.3906 0.4354 0.0568  0.0177  0.0319  286 LYS   A NZ  
4395 N  N   . ALA   A 287 ? 0.1774 0.1421 0.1713 0.0195  -0.0005 0.0096  287 ALA   A N   
4396 C  CA  . ALA   A 287 ? 0.1655 0.1311 0.1611 0.0163  -0.0007 0.0053  287 ALA   A CA  
4397 C  C   . ALA   A 287 ? 0.1735 0.1327 0.1699 0.0102  -0.0005 0.0022  287 ALA   A C   
4398 O  O   . ALA   A 287 ? 0.1830 0.1368 0.1790 0.0090  0.0010  -0.0019 287 ALA   A O   
4399 C  CB  . ALA   A 287 ? 0.1841 0.1630 0.1829 0.0149  -0.0034 0.0052  287 ALA   A CB  
4405 N  N   . ASN   A 288 ? 0.1656 0.1259 0.1632 0.0066  -0.0019 0.0036  288 ASN   A N   
4406 C  CA  . ASN   A 288 ? 0.1615 0.1180 0.1608 0.0012  -0.0017 0.0005  288 ASN   A CA  
4407 C  C   . ASN   A 288 ? 0.1882 0.1326 0.1870 0.0006  0.0025  -0.0012 288 ASN   A C   
4408 O  O   . ASN   A 288 ? 0.1975 0.1392 0.1986 -0.0031 0.0032  -0.0065 288 ASN   A O   
4409 C  CB  . ASN   A 288 ? 0.1635 0.1237 0.1639 -0.0012 -0.0034 0.0028  288 ASN   A CB  
4410 C  CG  . ASN   A 288 ? 0.1794 0.1413 0.1825 -0.0060 -0.0046 -0.0002 288 ASN   A CG  
4411 O  OD1 . ASN   A 288 ? 0.1866 0.1458 0.1915 -0.0084 -0.0036 -0.0044 288 ASN   A OD1 
4412 N  ND2 . ASN   A 288 ? 0.1676 0.1343 0.1713 -0.0073 -0.0066 0.0014  288 ASN   A ND2 
4419 N  N   . MET   A 289 ? 0.1835 0.1204 0.1793 0.0045  0.0057  0.0029  289 MET   A N   
4420 C  CA  A MET   A 289 ? 0.2035 0.1261 0.1986 0.0037  0.0112  0.0022  289 MET   A CA  
4421 C  CA  B MET   A 289 ? 0.2033 0.1259 0.1984 0.0038  0.0112  0.0023  289 MET   A CA  
4422 C  CA  C MET   A 289 ? 0.2035 0.1260 0.1985 0.0037  0.0112  0.0022  289 MET   A CA  
4423 C  C   . MET   A 289 ? 0.2191 0.1345 0.2132 0.0055  0.0137  -0.0018 289 MET   A C   
4424 O  O   . MET   A 289 ? 0.2467 0.1521 0.2427 0.0015  0.0173  -0.0063 289 MET   A O   
4425 C  CB  A MET   A 289 ? 0.2313 0.1471 0.2215 0.0087  0.0146  0.0091  289 MET   A CB  
4426 C  CB  B MET   A 289 ? 0.2309 0.1464 0.2209 0.0093  0.0147  0.0091  289 MET   A CB  
4427 C  CB  C MET   A 289 ? 0.2310 0.1463 0.2212 0.0090  0.0148  0.0090  289 MET   A CB  
4428 C  CG  A MET   A 289 ? 0.2300 0.1512 0.2206 0.0065  0.0130  0.0121  289 MET   A CG  
4429 C  CG  B MET   A 289 ? 0.2239 0.1440 0.2136 0.0079  0.0135  0.0127  289 MET   A CG  
4430 C  CG  C MET   A 289 ? 0.2248 0.1446 0.2146 0.0077  0.0136  0.0125  289 MET   A CG  
4431 S  SD  A MET   A 289 ? 0.2671 0.1836 0.2505 0.0133  0.0161  0.0202  289 MET   A SD  
4432 S  SD  B MET   A 289 ? 0.2843 0.1994 0.2660 0.0164  0.0165  0.0210  289 MET   A SD  
4433 S  SD  C MET   A 289 ? 0.2794 0.1925 0.2614 0.0154  0.0174  0.0208  289 MET   A SD  
4434 C  CE  A MET   A 289 ? 0.2207 0.1307 0.1984 0.0228  0.0186  0.0233  289 MET   A CE  
4435 C  CE  B MET   A 289 ? 0.2682 0.1620 0.2481 0.0150  0.0260  0.0222  289 MET   A CE  
4436 C  CE  C MET   A 289 ? 0.1819 0.1011 0.1601 0.0247  0.0149  0.0230  289 MET   A CE  
4462 N  N   . ASP   A 290 ? 0.2148 0.1351 0.2063 0.0116  0.0121  -0.0006 290 ASP   A N   
4463 C  CA  . ASP   A 290 ? 0.2306 0.1418 0.2196 0.0155  0.0156  -0.0031 290 ASP   A CA  
4464 C  C   . ASP   A 290 ? 0.2253 0.1444 0.2150 0.0159  0.0130  -0.0083 290 ASP   A C   
4465 O  O   . ASP   A 290 ? 0.2741 0.1848 0.2618 0.0179  0.0160  -0.0123 290 ASP   A O   
4466 C  CB  . ASP   A 290 ? 0.2594 0.1669 0.2433 0.0250  0.0180  0.0034  290 ASP   A CB  
4467 C  CG  . ASP   A 290 ? 0.3602 0.2563 0.3408 0.0269  0.0223  0.0091  290 ASP   A CG  
4468 O  OD1 . ASP   A 290 ? 0.3920 0.2789 0.3743 0.0206  0.0254  0.0076  290 ASP   A OD1 
4469 O  OD2 . ASP   A 290 ? 0.4251 0.3216 0.4008 0.0356  0.0232  0.0152  290 ASP   A OD2 
4474 N  N   . TYR   A 291 ? 0.2050 0.1389 0.1965 0.0145  0.0082  -0.0081 291 TYR   A N   
4475 C  CA  . TYR   A 291 ? 0.2018 0.1438 0.1925 0.0165  0.0066  -0.0113 291 TYR   A CA  
4476 C  C   . TYR   A 291 ? 0.2132 0.1644 0.2056 0.0116  0.0030  -0.0149 291 TYR   A C   
4477 O  O   . TYR   A 291 ? 0.2323 0.1846 0.2230 0.0118  0.0029  -0.0202 291 TYR   A O   
4478 C  CB  . TYR   A 291 ? 0.2014 0.1535 0.1918 0.0224  0.0057  -0.0064 291 TYR   A CB  
4479 C  CG  . TYR   A 291 ? 0.2291 0.1739 0.2168 0.0297  0.0091  -0.0036 291 TYR   A CG  
4480 C  CD1 . TYR   A 291 ? 0.2563 0.1922 0.2409 0.0340  0.0126  -0.0069 291 TYR   A CD1 
4481 C  CD2 . TYR   A 291 ? 0.2263 0.1719 0.2136 0.0331  0.0090  0.0022  291 TYR   A CD2 
4482 C  CE1 . TYR   A 291 ? 0.3310 0.2580 0.3121 0.0419  0.0164  -0.0037 291 TYR   A CE1 
4483 C  CE2 . TYR   A 291 ? 0.2371 0.1754 0.2205 0.0413  0.0123  0.0056  291 TYR   A CE2 
4484 C  CZ  . TYR   A 291 ? 0.2723 0.2006 0.2527 0.0456  0.0162  0.0029  291 TYR   A CZ  
4485 O  OH  . TYR   A 291 ? 0.3443 0.2641 0.3200 0.0552  0.0202  0.0066  291 TYR   A OH  
4495 N  N   . TRP   A 292 ? 0.1961 0.1536 0.1908 0.0080  0.0003  -0.0122 292 TRP   A N   
4496 C  CA  . TRP   A 292 ? 0.1726 0.1387 0.1676 0.0051  -0.0028 -0.0144 292 TRP   A CA  
4497 C  C   . TRP   A 292 ? 0.2001 0.1630 0.1959 0.0015  -0.0031 -0.0214 292 TRP   A C   
4498 O  O   . TRP   A 292 ? 0.1938 0.1487 0.1922 -0.0017 -0.0014 -0.0232 292 TRP   A O   
4499 C  CB  . TRP   A 292 ? 0.1753 0.1463 0.1724 0.0025  -0.0049 -0.0101 292 TRP   A CB  
4500 C  CG  . TRP   A 292 ? 0.1491 0.1260 0.1466 0.0047  -0.0052 -0.0050 292 TRP   A CG  
4501 C  CD1 . TRP   A 292 ? 0.1725 0.1542 0.1694 0.0084  -0.0042 -0.0038 292 TRP   A CD1 
4502 C  CD2 . TRP   A 292 ? 0.1519 0.1321 0.1515 0.0026  -0.0066 -0.0014 292 TRP   A CD2 
4503 N  NE1 . TRP   A 292 ? 0.1606 0.1493 0.1601 0.0081  -0.0049 0.0001  292 TRP   A NE1 
4504 C  CE2 . TRP   A 292 ? 0.1586 0.1457 0.1594 0.0045  -0.0065 0.0014  292 TRP   A CE2 
4505 C  CE3 . TRP   A 292 ? 0.1712 0.1495 0.1721 -0.0007 -0.0078 -0.0006 292 TRP   A CE3 
4506 C  CZ2 . TRP   A 292 ? 0.1591 0.1507 0.1624 0.0027  -0.0077 0.0039  292 TRP   A CZ2 
4507 C  CZ3 . TRP   A 292 ? 0.1709 0.1528 0.1730 -0.0017 -0.0089 0.0024  292 TRP   A CZ3 
4508 C  CH2 . TRP   A 292 ? 0.1629 0.1511 0.1663 -0.0004 -0.0089 0.0043  292 TRP   A CH2 
4519 N  N   . THR   A 293 ? 0.2079 0.1781 0.2015 0.0019  -0.0053 -0.0254 293 THR   A N   
4520 C  CA  . THR   A 293 ? 0.2050 0.1759 0.1995 -0.0010 -0.0066 -0.0336 293 THR   A CA  
4521 C  C   . THR   A 293 ? 0.2003 0.1816 0.1953 -0.0025 -0.0105 -0.0337 293 THR   A C   
4522 O  O   . THR   A 293 ? 0.1810 0.1673 0.1744 -0.0007 -0.0115 -0.0273 293 THR   A O   
4523 C  CB  . THR   A 293 ? 0.2302 0.2022 0.2202 0.0023  -0.0062 -0.0395 293 THR   A CB  
4524 O  OG1 . THR   A 293 ? 0.2518 0.2347 0.2369 0.0061  -0.0083 -0.0368 293 THR   A OG1 
4525 C  CG2 . THR   A 293 ? 0.2691 0.2317 0.2573 0.0058  -0.0022 -0.0386 293 THR   A CG2 
4533 N  N   . PRO   A 294 ? 0.1836 0.1685 0.1814 -0.0059 -0.0124 -0.0408 294 PRO   A N   
4534 C  CA  . PRO   A 294 ? 0.1922 0.1873 0.1911 -0.0064 -0.0160 -0.0403 294 PRO   A CA  
4535 C  C   . PRO   A 294 ? 0.1786 0.1829 0.1707 -0.0010 -0.0183 -0.0370 294 PRO   A C   
4536 O  O   . PRO   A 294 ? 0.2042 0.2126 0.1959 0.0001  -0.0196 -0.0318 294 PRO   A O   
4537 C  CB  . PRO   A 294 ? 0.2022 0.2017 0.2060 -0.0106 -0.0177 -0.0505 294 PRO   A CB  
4538 C  CG  . PRO   A 294 ? 0.2211 0.2070 0.2291 -0.0149 -0.0131 -0.0535 294 PRO   A CG  
4539 C  CD  . PRO   A 294 ? 0.2071 0.1862 0.2089 -0.0101 -0.0108 -0.0497 294 PRO   A CD  
4547 N  N   . TYR   A 295 ? 0.1810 0.1875 0.1673 0.0030  -0.0182 -0.0392 295 TYR   A N   
4548 C  CA  . TYR   A 295 ? 0.1818 0.1963 0.1605 0.0086  -0.0192 -0.0355 295 TYR   A CA  
4549 C  C   . TYR   A 295 ? 0.1941 0.2044 0.1696 0.0112  -0.0155 -0.0280 295 TYR   A C   
4550 O  O   . TYR   A 295 ? 0.1907 0.2060 0.1595 0.0159  -0.0147 -0.0259 295 TYR   A O   
4551 C  CB  . TYR   A 295 ? 0.2105 0.2336 0.1838 0.0120  -0.0218 -0.0435 295 TYR   A CB  
4552 C  CG  . TYR   A 295 ? 0.2363 0.2669 0.2140 0.0093  -0.0259 -0.0518 295 TYR   A CG  
4553 C  CD1 . TYR   A 295 ? 0.2247 0.2642 0.2023 0.0110  -0.0290 -0.0496 295 TYR   A CD1 
4554 C  CD2 . TYR   A 295 ? 0.3669 0.3952 0.3497 0.0046  -0.0261 -0.0621 295 TYR   A CD2 
4555 C  CE1 . TYR   A 295 ? 0.3178 0.3675 0.3007 0.0087  -0.0331 -0.0584 295 TYR   A CE1 
4556 C  CE2 . TYR   A 295 ? 0.3956 0.4325 0.3844 0.0009  -0.0296 -0.0710 295 TYR   A CE2 
4557 C  CZ  . TYR   A 295 ? 0.3917 0.4404 0.3809 0.0030  -0.0333 -0.0692 295 TYR   A CZ  
4558 O  OH  . TYR   A 295 ? 0.5212 0.5815 0.5174 -0.0004 -0.0371 -0.0787 295 TYR   A OH  
4568 N  N   . SER   A 296 ? 0.1783 0.1811 0.1588 0.0084  -0.0132 -0.0239 296 SER   A N   
4569 C  CA  . SER   A 296 ? 0.1635 0.1648 0.1431 0.0104  -0.0101 -0.0183 296 SER   A CA  
4570 C  C   . SER   A 296 ? 0.1788 0.1855 0.1542 0.0128  -0.0091 -0.0124 296 SER   A C   
4571 O  O   . SER   A 296 ? 0.2061 0.2138 0.1815 0.0119  -0.0102 -0.0092 296 SER   A O   
4572 C  CB  . SER   A 296 ? 0.1880 0.1836 0.1734 0.0073  -0.0090 -0.0144 296 SER   A CB  
4573 O  OG  . SER   A 296 ? 0.1927 0.1888 0.1789 0.0091  -0.0064 -0.0104 296 SER   A OG  
4579 N  N   . THR   A 297 ? 0.1732 0.1825 0.1453 0.0161  -0.0061 -0.0103 297 THR   A N   
4580 C  CA  . THR   A 297 ? 0.1775 0.1899 0.1475 0.0172  -0.0031 -0.0034 297 THR   A CA  
4581 C  C   . THR   A 297 ? 0.1536 0.1638 0.1311 0.0135  -0.0012 0.0008  297 THR   A C   
4582 O  O   . THR   A 297 ? 0.1630 0.1706 0.1454 0.0120  -0.0020 -0.0011 297 THR   A O   
4583 C  CB  . THR   A 297 ? 0.1991 0.2165 0.1630 0.0220  0.0000  -0.0029 297 THR   A CB  
4584 O  OG1 . THR   A 297 ? 0.1933 0.2102 0.1611 0.0222  0.0018  -0.0049 297 THR   A OG1 
4585 C  CG2 . THR   A 297 ? 0.2156 0.2369 0.1712 0.0265  -0.0024 -0.0083 297 THR   A CG2 
4593 N  N   . PHE   A 298 ? 0.1669 0.1782 0.1449 0.0122  0.0017  0.0066  298 PHE   A N   
4594 C  CA  . PHE   A 298 ? 0.1690 0.1807 0.1547 0.0083  0.0034  0.0092  298 PHE   A CA  
4595 C  C   . PHE   A 298 ? 0.1619 0.1786 0.1510 0.0101  0.0051  0.0078  298 PHE   A C   
4596 O  O   . PHE   A 298 ? 0.1608 0.1782 0.1559 0.0086  0.0040  0.0071  298 PHE   A O   
4597 C  CB  . PHE   A 298 ? 0.1739 0.1862 0.1600 0.0062  0.0076  0.0147  298 PHE   A CB  
4598 C  CG  . PHE   A 298 ? 0.1594 0.1656 0.1429 0.0047  0.0069  0.0171  298 PHE   A CG  
4599 C  CD1 . PHE   A 298 ? 0.1822 0.1844 0.1676 0.0029  0.0028  0.0150  298 PHE   A CD1 
4600 C  CD2 . PHE   A 298 ? 0.2003 0.2043 0.1790 0.0058  0.0111  0.0220  298 PHE   A CD2 
4601 C  CE1 . PHE   A 298 ? 0.1805 0.1776 0.1636 0.0024  0.0025  0.0173  298 PHE   A CE1 
4602 C  CE2 . PHE   A 298 ? 0.2214 0.2188 0.1969 0.0057  0.0111  0.0248  298 PHE   A CE2 
4603 C  CZ  . PHE   A 298 ? 0.2076 0.2021 0.1856 0.0041  0.0064  0.0220  298 PHE   A CZ  
4613 N  N   . ASP   A 299 ? 0.1576 0.1783 0.1420 0.0141  0.0078  0.0075  299 ASP   A N   
4614 C  CA  . ASP   A 299 ? 0.1688 0.1948 0.1560 0.0170  0.0098  0.0060  299 ASP   A CA  
4615 C  C   . ASP   A 299 ? 0.1734 0.1946 0.1609 0.0191  0.0067  0.0012  299 ASP   A C   
4616 O  O   . ASP   A 299 ? 0.1803 0.2034 0.1726 0.0203  0.0070  0.0010  299 ASP   A O   
4617 C  CB  . ASP   A 299 ? 0.1651 0.1960 0.1462 0.0215  0.0136  0.0064  299 ASP   A CB  
4618 C  CG  . ASP   A 299 ? 0.1923 0.2280 0.1741 0.0197  0.0190  0.0123  299 ASP   A CG  
4619 O  OD1 . ASP   A 299 ? 0.2114 0.2471 0.2000 0.0142  0.0200  0.0155  299 ASP   A OD1 
4620 O  OD2 . ASP   A 299 ? 0.2391 0.2784 0.2143 0.0238  0.0228  0.0135  299 ASP   A OD2 
4625 N  N   . GLU   A 300 ? 0.1637 0.1790 0.1459 0.0199  0.0041  -0.0030 300 GLU   A N   
4626 C  CA  . GLU   A 300 ? 0.1791 0.1876 0.1620 0.0209  0.0025  -0.0076 300 GLU   A CA  
4627 C  C   . GLU   A 300 ? 0.1586 0.1632 0.1473 0.0177  0.0009  -0.0055 300 GLU   A C   
4628 O  O   . GLU   A 300 ? 0.1845 0.1850 0.1750 0.0197  0.0013  -0.0063 300 GLU   A O   
4629 C  CB  . GLU   A 300 ? 0.2041 0.2080 0.1821 0.0206  0.0000  -0.0133 300 GLU   A CB  
4630 C  CG  . GLU   A 300 ? 0.2215 0.2287 0.1927 0.0251  0.0012  -0.0176 300 GLU   A CG  
4631 C  CD  . GLU   A 300 ? 0.2216 0.2293 0.1880 0.0246  -0.0020 -0.0230 300 GLU   A CD  
4632 O  OE1 . GLU   A 300 ? 0.2299 0.2359 0.1985 0.0209  -0.0049 -0.0237 300 GLU   A OE1 
4633 O  OE2 . GLU   A 300 ? 0.2475 0.2589 0.2072 0.0287  -0.0016 -0.0275 300 GLU   A OE2 
4640 N  N   . GLY   A 301 ? 0.1664 0.1716 0.1572 0.0135  -0.0006 -0.0025 301 GLY   A N   
4641 C  CA  . GLY   A 301 ? 0.1632 0.1657 0.1586 0.0108  -0.0021 -0.0008 301 GLY   A CA  
4642 C  C   . GLY   A 301 ? 0.1563 0.1647 0.1564 0.0122  -0.0009 0.0018  301 GLY   A C   
4643 O  O   . GLY   A 301 ? 0.1630 0.1692 0.1651 0.0132  -0.0019 0.0021  301 GLY   A O   
4647 N  N   . GLY   A 302 ? 0.1622 0.1792 0.1641 0.0127  0.0014  0.0035  302 GLY   A N   
4648 C  CA  . GLY   A 302 ? 0.1677 0.1941 0.1757 0.0141  0.0025  0.0049  302 GLY   A CA  
4649 C  C   . GLY   A 302 ? 0.1494 0.1753 0.1562 0.0206  0.0031  0.0033  302 GLY   A C   
4650 O  O   . GLY   A 302 ? 0.1632 0.1940 0.1740 0.0231  0.0024  0.0041  302 GLY   A O   
4654 N  N   . CYS   A 303 ? 0.1678 0.1884 0.1689 0.0238  0.0045  0.0007  303 CYS   A N   
4655 C  CA  A CYS   A 303 ? 0.1840 0.1998 0.1828 0.0307  0.0057  -0.0015 303 CYS   A CA  
4656 C  CA  B CYS   A 303 ? 0.1849 0.2014 0.1839 0.0304  0.0057  -0.0014 303 CYS   A CA  
4657 C  C   . CYS   A 303 ? 0.1867 0.1919 0.1844 0.0310  0.0042  -0.0015 303 CYS   A C   
4658 O  O   . CYS   A 303 ? 0.1986 0.2014 0.1961 0.0367  0.0053  -0.0007 303 CYS   A O   
4659 C  CB  A CYS   A 303 ? 0.1976 0.2077 0.1900 0.0332  0.0074  -0.0057 303 CYS   A CB  
4660 C  CB  B CYS   A 303 ? 0.1968 0.2085 0.1895 0.0330  0.0075  -0.0054 303 CYS   A CB  
4661 S  SG  A CYS   A 303 ? 0.2087 0.2296 0.1990 0.0353  0.0104  -0.0059 303 CYS   A SG  
4662 S  SG  B CYS   A 303 ? 0.2714 0.2795 0.2614 0.0420  0.0106  -0.0080 303 CYS   A SG  
4671 N  N   . GLY   A 304 ? 0.1661 0.1645 0.1629 0.0255  0.0022  -0.0021 304 GLY   A N   
4672 C  CA  . GLY   A 304 ? 0.1775 0.1654 0.1734 0.0251  0.0016  -0.0017 304 GLY   A CA  
4673 C  C   . GLY   A 304 ? 0.1863 0.1799 0.1855 0.0262  0.0003  0.0024  304 GLY   A C   
4674 O  O   . GLY   A 304 ? 0.1957 0.1822 0.1929 0.0299  0.0011  0.0039  304 GLY   A O   
4678 N  N   . MET   A 305 ? 0.1557 0.1611 0.1594 0.0232  -0.0014 0.0040  305 MET   A N   
4679 C  CA  . MET   A 305 ? 0.1612 0.1748 0.1686 0.0241  -0.0032 0.0064  305 MET   A CA  
4680 C  C   . MET   A 305 ? 0.1559 0.1774 0.1647 0.0318  -0.0022 0.0073  305 MET   A C   
4681 O  O   . MET   A 305 ? 0.1616 0.1860 0.1703 0.0362  -0.0035 0.0092  305 MET   A O   
4682 C  CB  . MET   A 305 ? 0.1613 0.1852 0.1741 0.0181  -0.0044 0.0065  305 MET   A CB  
4683 C  CG  . MET   A 305 ? 0.1652 0.1826 0.1769 0.0118  -0.0057 0.0064  305 MET   A CG  
4684 S  SD  . MET   A 305 ? 0.1681 0.1935 0.1849 0.0051  -0.0055 0.0067  305 MET   A SD  
4685 C  CE  . MET   A 305 ? 0.1850 0.2227 0.2083 0.0051  -0.0076 0.0062  305 MET   A CE  
4695 N  N   . LEU   A 306 ? 0.1487 0.1754 0.1585 0.0343  0.0000  0.0061  306 LEU   A N   
4696 C  CA  . LEU   A 306 ? 0.1660 0.2012 0.1774 0.0425  0.0012  0.0068  306 LEU   A CA  
4697 C  C   . LEU   A 306 ? 0.1750 0.1968 0.1797 0.0502  0.0027  0.0078  306 LEU   A C   
4698 O  O   . LEU   A 306 ? 0.1861 0.2126 0.1908 0.0575  0.0023  0.0101  306 LEU   A O   
4699 C  CB  . LEU   A 306 ? 0.1736 0.2155 0.1865 0.0438  0.0041  0.0051  306 LEU   A CB  
4700 C  CG  . LEU   A 306 ? 0.1737 0.2311 0.1943 0.0380  0.0042  0.0052  306 LEU   A CG  
4701 C  CD1 . LEU   A 306 ? 0.2036 0.2652 0.2241 0.0381  0.0081  0.0042  306 LEU   A CD1 
4702 C  CD2 . LEU   A 306 ? 0.2069 0.2821 0.2358 0.0405  0.0028  0.0057  306 LEU   A CD2 
4714 N  N   . SER   A 307 ? 0.1760 0.1809 0.1751 0.0484  0.0046  0.0059  307 SER   A N   
4715 C  CA  . SER   A 307 ? 0.2056 0.1947 0.1985 0.0545  0.0073  0.0068  307 SER   A CA  
4716 C  C   . SER   A 307 ? 0.1844 0.1688 0.1756 0.0549  0.0062  0.0106  307 SER   A C   
4717 O  O   . SER   A 307 ? 0.2295 0.2085 0.2166 0.0632  0.0081  0.0139  307 SER   A O   
4718 C  CB  . SER   A 307 ? 0.2297 0.2031 0.2187 0.0503  0.0096  0.0026  307 SER   A CB  
4719 O  OG  . SER   A 307 ? 0.2611 0.2378 0.2497 0.0517  0.0110  -0.0012 307 SER   A OG  
4725 N  N   . ALA   A 308 ? 0.1880 0.1744 0.1815 0.0470  0.0034  0.0106  308 ALA   A N   
4726 C  CA  . ALA   A 308 ? 0.1942 0.1778 0.1857 0.0474  0.0023  0.0141  308 ALA   A CA  
4727 C  C   . ALA   A 308 ? 0.1947 0.1932 0.1877 0.0542  -0.0002 0.0169  308 ALA   A C   
4728 O  O   . ALA   A 308 ? 0.2095 0.2042 0.1974 0.0614  0.0006  0.0208  308 ALA   A O   
4729 C  CB  . ALA   A 308 ? 0.2013 0.1860 0.1955 0.0378  -0.0003 0.0128  308 ALA   A CB  
4735 N  N   . ALA   A 309 ? 0.1910 0.2076 0.1910 0.0522  -0.0029 0.0150  309 ALA   A N   
4736 C  CA  . ALA   A 309 ? 0.1850 0.2196 0.1884 0.0580  -0.0058 0.0161  309 ALA   A CA  
4737 C  C   . ALA   A 309 ? 0.2059 0.2406 0.2055 0.0705  -0.0035 0.0187  309 ALA   A C   
4738 O  O   . ALA   A 309 ? 0.2132 0.2557 0.2108 0.0786  -0.0053 0.0214  309 ALA   A O   
4739 C  CB  . ALA   A 309 ? 0.1816 0.2346 0.1948 0.0522  -0.0077 0.0127  309 ALA   A CB  
4745 N  N   . LYS   A 310 ? 0.2002 0.2267 0.1981 0.0732  0.0003  0.0177  310 LYS   A N   
4746 C  CA  . LYS   A 310 ? 0.2248 0.2481 0.2180 0.0860  0.0033  0.0201  310 LYS   A CA  
4747 C  C   . LYS   A 310 ? 0.2746 0.2797 0.2581 0.0921  0.0058  0.0249  310 LYS   A C   
4748 O  O   . LYS   A 310 ? 0.2822 0.2912 0.2616 0.1036  0.0059  0.0291  310 LYS   A O   
4749 C  CB  . LYS   A 310 ? 0.2918 0.3068 0.2842 0.0865  0.0073  0.0172  310 LYS   A CB  
4750 C  CG  . LYS   A 310 ? 0.3140 0.3281 0.3026 0.1000  0.0106  0.0191  310 LYS   A CG  
4751 C  CD  . LYS   A 310 ? 0.4238 0.4392 0.4145 0.0997  0.0133  0.0148  310 LYS   A CD  
4752 C  CE  . LYS   A 310 ? 0.5687 0.5762 0.5537 0.1130  0.0179  0.0159  310 LYS   A CE  
4753 N  NZ  . LYS   A 310 ? 0.6343 0.6126 0.6102 0.1130  0.0228  0.0151  310 LYS   A NZ  
4767 N  N   . ASP   A 311 ? 0.2523 0.2382 0.2321 0.0847  0.0080  0.0245  311 ASP   A N   
4768 C  CA  . ASP   A 311 ? 0.2653 0.2329 0.2363 0.0891  0.0116  0.0293  311 ASP   A CA  
4769 C  C   . ASP   A 311 ? 0.2695 0.2482 0.2386 0.0935  0.0081  0.0336  311 ASP   A C   
4770 O  O   . ASP   A 311 ? 0.3008 0.2709 0.2614 0.1036  0.0110  0.0394  311 ASP   A O   
4771 C  CB  . ASP   A 311 ? 0.2804 0.2315 0.2511 0.0777  0.0136  0.0270  311 ASP   A CB  
4772 C  CG  . ASP   A 311 ? 0.3653 0.3018 0.3359 0.0741  0.0177  0.0224  311 ASP   A CG  
4773 O  OD1 . ASP   A 311 ? 0.3654 0.2988 0.3340 0.0813  0.0205  0.0217  311 ASP   A OD1 
4774 O  OD2 . ASP   A 311 ? 0.3741 0.3031 0.3468 0.0638  0.0179  0.0187  311 ASP   A OD2 
4779 N  N   . LEU   A 312 ? 0.2379 0.2340 0.2136 0.0863  0.0024  0.0310  312 LEU   A N   
4780 C  CA  . LEU   A 312 ? 0.2524 0.2606 0.2266 0.0891  -0.0017 0.0333  312 LEU   A CA  
4781 C  C   . LEU   A 312 ? 0.2786 0.3090 0.2549 0.0994  -0.0054 0.0339  312 LEU   A C   
4782 O  O   . LEU   A 312 ? 0.2914 0.3327 0.2650 0.1040  -0.0089 0.0356  312 LEU   A O   
4783 C  CB  . LEU   A 312 ? 0.2404 0.2574 0.2216 0.0763  -0.0060 0.0288  312 LEU   A CB  
4784 C  CG  . LEU   A 312 ? 0.2419 0.2406 0.2208 0.0672  -0.0034 0.0286  312 LEU   A CG  
4785 C  CD1 . LEU   A 312 ? 0.2581 0.2656 0.2445 0.0558  -0.0071 0.0239  312 LEU   A CD1 
4786 C  CD2 . LEU   A 312 ? 0.3296 0.3187 0.3004 0.0703  -0.0017 0.0332  312 LEU   A CD2 
4798 N  N   . GLY   A 313 ? 0.2437 0.2823 0.2247 0.1033  -0.0048 0.0320  313 GLY   A N   
4799 C  CA  . GLY   A 313 ? 0.2836 0.3467 0.2689 0.1127  -0.0084 0.0316  313 GLY   A CA  
4800 C  C   . GLY   A 313 ? 0.2671 0.3560 0.2645 0.1043  -0.0144 0.0257  313 GLY   A C   
4801 O  O   . GLY   A 313 ? 0.2802 0.3926 0.2817 0.1111  -0.0187 0.0246  313 GLY   A O   
4805 N  N   . TYR   A 314 ? 0.2059 0.2916 0.2095 0.0899  -0.0147 0.0216  314 TYR   A N   
4806 C  CA  . TYR   A 314 ? 0.2431 0.3496 0.2582 0.0807  -0.0191 0.0160  314 TYR   A CA  
4807 C  C   . TYR   A 314 ? 0.2122 0.3315 0.2374 0.0781  -0.0177 0.0127  314 TYR   A C   
4808 O  O   . TYR   A 314 ? 0.2421 0.3512 0.2649 0.0811  -0.0134 0.0141  314 TYR   A O   
4809 C  CB  . TYR   A 314 ? 0.1889 0.2845 0.2043 0.0676  -0.0195 0.0141  314 TYR   A CB  
4810 C  CG  . TYR   A 314 ? 0.1954 0.2812 0.2020 0.0691  -0.0209 0.0168  314 TYR   A CG  
4811 C  CD1 . TYR   A 314 ? 0.2065 0.2985 0.2065 0.0803  -0.0229 0.0199  314 TYR   A CD1 
4812 C  CD2 . TYR   A 314 ? 0.1936 0.2650 0.1982 0.0596  -0.0200 0.0164  314 TYR   A CD2 
4813 C  CE1 . TYR   A 314 ? 0.2186 0.3018 0.2100 0.0812  -0.0235 0.0225  314 TYR   A CE1 
4814 C  CE2 . TYR   A 314 ? 0.2130 0.2763 0.2103 0.0601  -0.0207 0.0185  314 TYR   A CE2 
4815 C  CZ  . TYR   A 314 ? 0.2396 0.3085 0.2301 0.0708  -0.0222 0.0217  314 TYR   A CZ  
4816 O  OH  . TYR   A 314 ? 0.2587 0.3199 0.2406 0.0725  -0.0223 0.0245  314 TYR   A OH  
4826 N  N   . ASN   A 315 ? 0.1934 0.3350 0.2304 0.0717  -0.0209 0.0077  315 ASN   A N   
4827 C  CA  . ASN   A 315 ? 0.1757 0.3339 0.2237 0.0700  -0.0192 0.0047  315 ASN   A CA  
4828 C  C   . ASN   A 315 ? 0.1937 0.3393 0.2434 0.0598  -0.0147 0.0041  315 ASN   A C   
4829 O  O   . ASN   A 315 ? 0.1822 0.3224 0.2341 0.0486  -0.0150 0.0023  315 ASN   A O   
4830 C  CB  . ASN   A 315 ? 0.1718 0.3580 0.2330 0.0650  -0.0235 -0.0011 315 ASN   A CB  
4831 C  CG  . ASN   A 315 ? 0.1999 0.4062 0.2739 0.0636  -0.0213 -0.0042 315 ASN   A CG  
4832 O  OD1 . ASN   A 315 ? 0.2036 0.4046 0.2820 0.0543  -0.0172 -0.0051 315 ASN   A OD1 
4833 N  ND2 . ASN   A 315 ? 0.2784 0.5089 0.3585 0.0729  -0.0238 -0.0058 315 ASN   A ND2 
4840 N  N   . LEU   A 316 ? 0.1915 0.3312 0.2389 0.0648  -0.0105 0.0057  316 LEU   A N   
4841 C  CA  . LEU   A 316 ? 0.1833 0.3098 0.2294 0.0573  -0.0061 0.0055  316 LEU   A CA  
4842 C  C   . LEU   A 316 ? 0.1862 0.3289 0.2442 0.0482  -0.0046 0.0024  316 LEU   A C   
4843 O  O   . LEU   A 316 ? 0.1887 0.3209 0.2453 0.0403  -0.0017 0.0025  316 LEU   A O   
4844 C  CB  . LEU   A 316 ? 0.2063 0.3229 0.2457 0.0663  -0.0021 0.0072  316 LEU   A CB  
4845 C  CG  . LEU   A 316 ? 0.3746 0.4715 0.4021 0.0748  -0.0019 0.0103  316 LEU   A CG  
4846 C  CD1 . LEU   A 316 ? 0.4472 0.5326 0.4688 0.0817  0.0028  0.0106  316 LEU   A CD1 
4847 C  CD2 . LEU   A 316 ? 0.3338 0.4118 0.3551 0.0675  -0.0028 0.0111  316 LEU   A CD2 
4859 N  N   . ASP   A 317 ? 0.1519 0.3195 0.2212 0.0495  -0.0059 -0.0002 317 ASP   A N   
4860 C  CA  . ASP   A 317 ? 0.1671 0.3508 0.2495 0.0396  -0.0034 -0.0034 317 ASP   A CA  
4861 C  C   . ASP   A 317 ? 0.1601 0.3400 0.2456 0.0275  -0.0052 -0.0056 317 ASP   A C   
4862 O  O   . ASP   A 317 ? 0.1943 0.3755 0.2863 0.0176  -0.0013 -0.0067 317 ASP   A O   
4863 C  CB  . ASP   A 317 ? 0.1636 0.3769 0.2589 0.0439  -0.0043 -0.0066 317 ASP   A CB  
4864 C  CG  . ASP   A 317 ? 0.2460 0.4671 0.3428 0.0521  0.0002  -0.0054 317 ASP   A CG  
4865 O  OD1 . ASP   A 317 ? 0.2419 0.4446 0.3293 0.0538  0.0043  -0.0024 317 ASP   A OD1 
4866 O  OD2 . ASP   A 317 ? 0.4898 0.7365 0.5973 0.0569  -0.0006 -0.0080 317 ASP   A OD2 
4871 N  N   . ASP   A 318 ? 0.1539 0.3289 0.2346 0.0287  -0.0104 -0.0059 318 ASP   A N   
4872 C  CA  . ASP   A 318 ? 0.1601 0.3298 0.2424 0.0180  -0.0122 -0.0083 318 ASP   A CA  
4873 C  C   . ASP   A 318 ? 0.1650 0.3092 0.2377 0.0135  -0.0091 -0.0048 318 ASP   A C   
4874 O  O   . ASP   A 318 ? 0.1385 0.2785 0.2145 0.0037  -0.0073 -0.0060 318 ASP   A O   
4875 C  CB  . ASP   A 318 ? 0.1748 0.3494 0.2546 0.0216  -0.0184 -0.0101 318 ASP   A CB  
4876 C  CG  . ASP   A 318 ? 0.2272 0.4309 0.3180 0.0248  -0.0222 -0.0151 318 ASP   A CG  
4877 O  OD1 . ASP   A 318 ? 0.2709 0.4907 0.3754 0.0164  -0.0206 -0.0199 318 ASP   A OD1 
4878 O  OD2 . ASP   A 318 ? 0.2568 0.4671 0.3425 0.0359  -0.0264 -0.0140 318 ASP   A OD2 
4883 N  N   . ILE   A 319 ? 0.1486 0.2770 0.2101 0.0206  -0.0084 -0.0010 319 ILE   A N   
4884 C  CA  . ILE   A 319 ? 0.1494 0.2570 0.2028 0.0169  -0.0059 0.0014  319 ILE   A CA  
4885 C  C   . ILE   A 319 ? 0.1318 0.2412 0.1889 0.0121  -0.0007 0.0018  319 ILE   A C   
4886 O  O   . ILE   A 319 ? 0.1254 0.2255 0.1811 0.0049  0.0014  0.0025  319 ILE   A O   
4887 C  CB  . ILE   A 319 ? 0.1578 0.2506 0.2004 0.0253  -0.0057 0.0041  319 ILE   A CB  
4888 C  CG1 . ILE   A 319 ? 0.1958 0.2841 0.2330 0.0307  -0.0094 0.0052  319 ILE   A CG1 
4889 C  CG2 . ILE   A 319 ? 0.1821 0.2569 0.2175 0.0216  -0.0035 0.0053  319 ILE   A CG2 
4890 C  CD1 . ILE   A 319 ? 0.1824 0.2588 0.2156 0.0249  -0.0112 0.0054  319 ILE   A CD1 
4902 N  N   . LYS   A 320 ? 0.1276 0.2489 0.1889 0.0168  0.0020  0.0016  320 LYS   A N   
4903 C  CA  . LYS   A 320 ? 0.1207 0.2440 0.1842 0.0136  0.0077  0.0025  320 LYS   A CA  
4904 C  C   . LYS   A 320 ? 0.1135 0.2450 0.1870 0.0030  0.0103  0.0012  320 LYS   A C   
4905 O  O   . LYS   A 320 ? 0.1165 0.2397 0.1878 -0.0022 0.0149  0.0034  320 LYS   A O   
4906 C  CB  . LYS   A 320 ? 0.1233 0.2594 0.1898 0.0217  0.0100  0.0023  320 LYS   A CB  
4907 C  CG  . LYS   A 320 ? 0.1461 0.2692 0.2011 0.0315  0.0098  0.0037  320 LYS   A CG  
4908 C  CD  . LYS   A 320 ? 0.1636 0.2999 0.2216 0.0408  0.0119  0.0032  320 LYS   A CD  
4909 C  CE  . LYS   A 320 ? 0.1824 0.3015 0.2283 0.0491  0.0123  0.0039  320 LYS   A CE  
4910 N  NZ  . LYS   A 320 ? 0.2167 0.3470 0.2645 0.0590  0.0149  0.0034  320 LYS   A NZ  
4924 N  N   . LYS   A 321 ? 0.1132 0.2607 0.1975 -0.0001 0.0077  -0.0024 321 LYS   A N   
4925 C  CA  . LYS   A 321 ? 0.1147 0.2683 0.2093 -0.0115 0.0105  -0.0048 321 LYS   A CA  
4926 C  C   . LYS   A 321 ? 0.1276 0.2611 0.2152 -0.0180 0.0106  -0.0033 321 LYS   A C   
4927 O  O   . LYS   A 321 ? 0.1345 0.2620 0.2240 -0.0255 0.0161  -0.0019 321 LYS   A O   
4928 C  CB  . LYS   A 321 ? 0.1120 0.2868 0.2192 -0.0139 0.0064  -0.0107 321 LYS   A CB  
4929 C  CG  . LYS   A 321 ? 0.1533 0.3358 0.2734 -0.0268 0.0098  -0.0148 321 LYS   A CG  
4930 C  CD  . LYS   A 321 ? 0.2114 0.4187 0.3453 -0.0290 0.0053  -0.0224 321 LYS   A CD  
4931 C  CE  . LYS   A 321 ? 0.3329 0.5445 0.4799 -0.0437 0.0101  -0.0271 321 LYS   A CE  
4932 N  NZ  . LYS   A 321 ? 0.4371 0.6780 0.6016 -0.0477 0.0075  -0.0357 321 LYS   A NZ  
4946 N  N   . SER   A 322 ? 0.1140 0.2367 0.1931 -0.0143 0.0051  -0.0031 322 SER   A N   
4947 C  CA  . SER   A 322 ? 0.1156 0.2206 0.1882 -0.0193 0.0048  -0.0019 322 SER   A CA  
4948 C  C   . SER   A 322 ? 0.1320 0.2214 0.1954 -0.0185 0.0090  0.0028  322 SER   A C   
4949 O  O   . SER   A 322 ? 0.1369 0.2165 0.1988 -0.0243 0.0124  0.0044  322 SER   A O   
4950 C  CB  . SER   A 322 ? 0.1278 0.2265 0.1935 -0.0147 -0.0016 -0.0026 322 SER   A CB  
4951 O  OG  . SER   A 322 ? 0.1317 0.2465 0.2049 -0.0145 -0.0058 -0.0071 322 SER   A OG  
4957 N  N   . LEU   A 323 ? 0.1181 0.2048 0.1746 -0.0107 0.0089  0.0049  323 LEU   A N   
4958 C  CA  . LEU   A 323 ? 0.1200 0.1948 0.1674 -0.0090 0.0124  0.0084  323 LEU   A CA  
4959 C  C   . LEU   A 323 ? 0.1416 0.2207 0.1931 -0.0135 0.0194  0.0104  323 LEU   A C   
4960 O  O   . LEU   A 323 ? 0.1521 0.2201 0.1976 -0.0158 0.0228  0.0136  323 LEU   A O   
4961 C  CB  . LEU   A 323 ? 0.1274 0.2015 0.1684 -0.0001 0.0115  0.0085  323 LEU   A CB  
4962 C  CG  . LEU   A 323 ? 0.1374 0.2028 0.1724 0.0045  0.0064  0.0075  323 LEU   A CG  
4963 C  CD1 . LEU   A 323 ? 0.1511 0.2150 0.1809 0.0127  0.0068  0.0070  323 LEU   A CD1 
4964 C  CD2 . LEU   A 323 ? 0.1654 0.2165 0.1935 0.0019  0.0048  0.0083  323 LEU   A CD2 
4976 N  N   . SER   A 324 ? 0.1326 0.2277 0.1940 -0.0143 0.0220  0.0090  324 SER   A N   
4977 C  CA  . SER   A 324 ? 0.1614 0.2613 0.2278 -0.0192 0.0300  0.0111  324 SER   A CA  
4978 C  C   . SER   A 324 ? 0.1488 0.2415 0.2191 -0.0289 0.0332  0.0117  324 SER   A C   
4979 O  O   . SER   A 324 ? 0.1777 0.2628 0.2449 -0.0319 0.0402  0.0160  324 SER   A O   
4980 C  CB  . SER   A 324 ? 0.1552 0.2765 0.2342 -0.0191 0.0322  0.0086  324 SER   A CB  
4981 O  OG  . SER   A 324 ? 0.2154 0.3413 0.2894 -0.0093 0.0319  0.0092  324 SER   A OG  
4987 N  N   . GLU   A 325 ? 0.1557 0.2502 0.2320 -0.0336 0.0286  0.0075  325 GLU   A N   
4988 C  CA  . GLU   A 325 ? 0.1563 0.2431 0.2366 -0.0431 0.0318  0.0069  325 GLU   A CA  
4989 C  C   . GLU   A 325 ? 0.1619 0.2274 0.2292 -0.0417 0.0330  0.0118  325 GLU   A C   
4990 O  O   . GLU   A 325 ? 0.2007 0.2566 0.2685 -0.0478 0.0392  0.0140  325 GLU   A O   
4991 C  CB  . GLU   A 325 ? 0.2017 0.2953 0.2896 -0.0469 0.0256  0.0004  325 GLU   A CB  
4992 C  CG  . GLU   A 325 ? 0.2804 0.3969 0.3837 -0.0506 0.0254  -0.0053 325 GLU   A CG  
4993 C  CD  . GLU   A 325 ? 0.4063 0.5303 0.5160 -0.0543 0.0191  -0.0122 325 GLU   A CD  
4994 O  OE1 . GLU   A 325 ? 0.2760 0.3878 0.3849 -0.0609 0.0200  -0.0137 325 GLU   A OE1 
4995 O  OE2 . GLU   A 325 ? 0.3628 0.5042 0.4771 -0.0494 0.0133  -0.0161 325 GLU   A OE2 
5002 N  N   . VAL   A 326 ? 0.1494 0.2073 0.2052 -0.0337 0.0281  0.0135  326 VAL   A N   
5003 C  CA  . VAL   A 326 ? 0.1553 0.1959 0.1990 -0.0314 0.0288  0.0177  326 VAL   A CA  
5004 C  C   . VAL   A 326 ? 0.1676 0.2057 0.2022 -0.0253 0.0326  0.0224  326 VAL   A C   
5005 O  O   . VAL   A 326 ? 0.1965 0.2241 0.2201 -0.0209 0.0316  0.0251  326 VAL   A O   
5006 C  CB  . VAL   A 326 ? 0.1529 0.1862 0.1906 -0.0281 0.0214  0.0158  326 VAL   A CB  
5007 C  CG1 . VAL   A 326 ? 0.1793 0.2138 0.2241 -0.0339 0.0185  0.0117  326 VAL   A CG1 
5008 C  CG2 . VAL   A 326 ? 0.1586 0.1976 0.1935 -0.0212 0.0162  0.0141  326 VAL   A CG2 
5018 N  N   . THR   A 327 ? 0.1567 0.2057 0.1959 -0.0248 0.0369  0.0229  327 THR   A N   
5019 C  CA  . THR   A 327 ? 0.1803 0.2297 0.2116 -0.0191 0.0415  0.0268  327 THR   A CA  
5020 C  C   . THR   A 327 ? 0.1907 0.2373 0.2113 -0.0103 0.0358  0.0257  327 THR   A C   
5021 O  O   . THR   A 327 ? 0.2327 0.2747 0.2425 -0.0051 0.0381  0.0287  327 THR   A O   
5022 C  CB  . THR   A 327 ? 0.1964 0.2360 0.2216 -0.0208 0.0498  0.0333  327 THR   A CB  
5023 O  OG1 . THR   A 327 ? 0.2413 0.2668 0.2552 -0.0175 0.0471  0.0356  327 THR   A OG1 
5024 C  CG2 . THR   A 327 ? 0.2244 0.2644 0.2608 -0.0306 0.0562  0.0338  327 THR   A CG2 
5032 N  N   . ILE   A 328 ? 0.1623 0.2119 0.1853 -0.0083 0.0291  0.0212  328 ILE   A N   
5033 C  CA  . ILE   A 328 ? 0.1662 0.2136 0.1812 -0.0009 0.0247  0.0191  328 ILE   A CA  
5034 C  C   . ILE   A 328 ? 0.1765 0.2351 0.1943 0.0034  0.0269  0.0178  328 ILE   A C   
5035 O  O   . ILE   A 328 ? 0.1898 0.2594 0.2178 0.0017  0.0273  0.0163  328 ILE   A O   
5036 C  CB  . ILE   A 328 ? 0.1672 0.2104 0.1833 -0.0009 0.0177  0.0157  328 ILE   A CB  
5037 C  CG1 . ILE   A 328 ? 0.1811 0.2128 0.1921 -0.0034 0.0159  0.0170  328 ILE   A CG1 
5038 C  CG2 . ILE   A 328 ? 0.2154 0.2581 0.2269 0.0058  0.0146  0.0127  328 ILE   A CG2 
5039 C  CD1 . ILE   A 328 ? 0.1805 0.2079 0.1930 -0.0046 0.0103  0.0144  328 ILE   A CD1 
5051 N  N   . ASN   A 329 ? 0.1536 0.2105 0.1624 0.0096  0.0279  0.0177  329 ASN   A N   
5052 C  CA  . ASN   A 329 ? 0.1590 0.2250 0.1683 0.0151  0.0304  0.0162  329 ASN   A CA  
5053 C  C   . ASN   A 329 ? 0.1531 0.2162 0.1603 0.0204  0.0251  0.0116  329 ASN   A C   
5054 O  O   . ASN   A 329 ? 0.1958 0.2484 0.1960 0.0216  0.0210  0.0095  329 ASN   A O   
5055 C  CB  . ASN   A 329 ? 0.1801 0.2445 0.1787 0.0195  0.0348  0.0183  329 ASN   A CB  
5056 C  CG  . ASN   A 329 ? 0.2056 0.2796 0.2041 0.0254  0.0382  0.0167  329 ASN   A CG  
5057 O  OD1 . ASN   A 329 ? 0.2332 0.3055 0.2277 0.0314  0.0350  0.0122  329 ASN   A OD1 
5058 N  ND2 . ASN   A 329 ? 0.2083 0.2911 0.2103 0.0241  0.0454  0.0204  329 ASN   A ND2 
5065 N  N   . TYR   A 330 ? 0.1515 0.2240 0.1648 0.0238  0.0257  0.0100  330 TYR   A N   
5066 C  CA  . TYR   A 330 ? 0.1475 0.2166 0.1592 0.0296  0.0220  0.0064  330 TYR   A CA  
5067 C  C   . TYR   A 330 ? 0.1921 0.2682 0.2024 0.0372  0.0255  0.0048  330 TYR   A C   
5068 O  O   . TYR   A 330 ? 0.1926 0.2686 0.2037 0.0429  0.0241  0.0026  330 TYR   A O   
5069 C  CB  . TYR   A 330 ? 0.1602 0.2321 0.1797 0.0283  0.0182  0.0061  330 TYR   A CB  
5070 C  CG  . TYR   A 330 ? 0.1333 0.2213 0.1645 0.0246  0.0201  0.0074  330 TYR   A CG  
5071 C  CD1 . TYR   A 330 ? 0.1373 0.2403 0.1754 0.0293  0.0220  0.0066  330 TYR   A CD1 
5072 C  CD2 . TYR   A 330 ? 0.1404 0.2290 0.1764 0.0160  0.0204  0.0090  330 TYR   A CD2 
5073 C  CE1 . TYR   A 330 ? 0.1395 0.2597 0.1902 0.0248  0.0240  0.0069  330 TYR   A CE1 
5074 C  CE2 . TYR   A 330 ? 0.1303 0.2338 0.1783 0.0112  0.0226  0.0090  330 TYR   A CE2 
5075 C  CZ  . TYR   A 330 ? 0.1274 0.2472 0.1831 0.0152  0.0240  0.0076  330 TYR   A CZ  
5076 O  OH  . TYR   A 330 ? 0.1536 0.2909 0.2230 0.0097  0.0263  0.0066  330 TYR   A OH  
5086 N  N   . GLN   A 331 ? 0.1724 0.2543 0.1800 0.0381  0.0308  0.0063  331 GLN   A N   
5087 C  CA  . GLN   A 331 ? 0.1879 0.2783 0.1949 0.0455  0.0347  0.0048  331 GLN   A CA  
5088 C  C   . GLN   A 331 ? 0.2688 0.3481 0.2660 0.0527  0.0326  0.0000  331 GLN   A C   
5089 O  O   . GLN   A 331 ? 0.3255 0.4093 0.3234 0.0600  0.0345  -0.0021 331 GLN   A O   
5090 C  CB  . GLN   A 331 ? 0.2134 0.3129 0.2194 0.0447  0.0419  0.0081  331 GLN   A CB  
5091 C  CG  . GLN   A 331 ? 0.2665 0.3777 0.2856 0.0366  0.0451  0.0121  331 GLN   A CG  
5092 C  CD  . GLN   A 331 ? 0.2652 0.3859 0.2856 0.0350  0.0538  0.0161  331 GLN   A CD  
5093 O  OE1 . GLN   A 331 ? 0.1972 0.3223 0.2122 0.0416  0.0578  0.0156  331 GLN   A OE1 
5094 N  NE2 . GLN   A 331 ? 0.3707 0.4956 0.4002 0.0260  0.0574  0.0197  331 GLN   A NE2 
5103 N  N   . SER   A 332 ? 0.2465 0.3120 0.2358 0.0507  0.0290  -0.0023 332 SER   A N   
5104 C  CA  . SER   A 332 ? 0.3566 0.4105 0.3372 0.0559  0.0272  -0.0082 332 SER   A CA  
5105 C  C   . SER   A 332 ? 0.3308 0.3745 0.3140 0.0560  0.0235  -0.0100 332 SER   A C   
5106 O  O   . SER   A 332 ? 0.3478 0.3800 0.3251 0.0596  0.0229  -0.0152 332 SER   A O   
5107 C  CB  . SER   A 332 ? 0.3653 0.4124 0.3365 0.0538  0.0256  -0.0107 332 SER   A CB  
5108 O  OG  . SER   A 332 ? 0.3958 0.4335 0.3677 0.0483  0.0208  -0.0113 332 SER   A OG  
5114 N  N   . CYS   A 333 ? 0.2551 0.3021 0.2464 0.0522  0.0215  -0.0062 333 CYS   A N   
5115 C  CA  A CYS   A 333 ? 0.2851 0.3215 0.2775 0.0527  0.0183  -0.0069 333 CYS   A CA  
5116 C  CA  B CYS   A 333 ? 0.2853 0.3219 0.2776 0.0527  0.0183  -0.0069 333 CYS   A CA  
5117 C  C   . CYS   A 333 ? 0.3905 0.4266 0.3836 0.0615  0.0200  -0.0076 333 CYS   A C   
5118 O  O   . CYS   A 333 ? 0.3411 0.3882 0.3411 0.0645  0.0200  -0.0045 333 CYS   A O   
5119 C  CB  A CYS   A 333 ? 0.2378 0.2789 0.2375 0.0470  0.0155  -0.0029 333 CYS   A CB  
5120 C  CB  B CYS   A 333 ? 0.2380 0.2784 0.2373 0.0466  0.0154  -0.0030 333 CYS   A CB  
5121 S  SG  A CYS   A 333 ? 0.2341 0.2731 0.2336 0.0376  0.0134  -0.0013 333 CYS   A SG  
5122 S  SG  B CYS   A 333 ? 0.2369 0.2637 0.2353 0.0469  0.0120  -0.0031 333 CYS   A SG  
5131 N  N   . TYR   A 334 ? 0.3946 0.4195 0.3803 0.0666  0.0219  -0.0122 334 TYR   A N   
5132 C  CA  . TYR   A 334 ? 0.4981 0.5187 0.4825 0.0763  0.0244  -0.0131 334 TYR   A CA  
5133 C  C   . TYR   A 334 ? 0.5181 0.5170 0.4952 0.0771  0.0248  -0.0179 334 TYR   A C   
5134 O  O   . TYR   A 334 ? 0.5255 0.5182 0.4973 0.0742  0.0250  -0.0234 334 TYR   A O   
5135 C  CB  . TYR   A 334 ? 0.4559 0.4875 0.4396 0.0834  0.0285  -0.0144 334 TYR   A CB  
5136 C  CG  . TYR   A 334 ? 0.3770 0.4311 0.3701 0.0835  0.0293  -0.0099 334 TYR   A CG  
5137 C  CD1 . TYR   A 334 ? 0.3802 0.4442 0.3798 0.0900  0.0295  -0.0071 334 TYR   A CD1 
5138 C  CD2 . TYR   A 334 ? 0.3250 0.3907 0.3207 0.0773  0.0303  -0.0085 334 TYR   A CD2 
5139 C  CE1 . TYR   A 334 ? 0.3132 0.3997 0.3231 0.0893  0.0302  -0.0042 334 TYR   A CE1 
5140 C  CE2 . TYR   A 334 ? 0.3312 0.4167 0.3368 0.0761  0.0321  -0.0049 334 TYR   A CE2 
5141 C  CZ  . TYR   A 334 ? 0.3033 0.4002 0.3168 0.0816  0.0318  -0.0034 334 TYR   A CZ  
5142 O  OH  . TYR   A 334 ? 0.2867 0.4054 0.3117 0.0795  0.0334  -0.0011 334 TYR   A OH  
5152 C  C1  . A1IRK B .   ? 0.2888 0.2244 0.2515 0.0257  0.0035  0.0308  401 A1IRK A C1  
5153 C  C2  . A1IRK B .   ? 0.2701 0.2105 0.2401 0.0200  0.0004  0.0252  401 A1IRK A C2  
5154 C  C3  . A1IRK B .   ? 0.2320 0.1844 0.2053 0.0224  -0.0040 0.0219  401 A1IRK A C3  
5155 C  C4  . A1IRK B .   ? 0.2581 0.2199 0.2286 0.0301  -0.0063 0.0231  401 A1IRK A C4  
5156 C  C5  . A1IRK B .   ? 0.2992 0.2579 0.2618 0.0365  -0.0042 0.0283  401 A1IRK A C5  
5157 C  C6  . A1IRK B .   ? 0.2835 0.2282 0.2416 0.0345  0.0012  0.0327  401 A1IRK A C6  
5158 C  C8  . A1IRK B .   ? 0.2471 0.2092 0.2360 0.0074  -0.0086 0.0107  401 A1IRK A C8  
5159 C  C9  . A1IRK B .   ? 0.3044 0.2759 0.2971 0.0048  -0.0112 0.0091  401 A1IRK A C9  
5160 C  C10 . A1IRK B .   ? 0.3954 0.3356 0.3438 0.0418  0.0046  0.0394  401 A1IRK A C10 
5161 C  C11 . A1IRK B .   ? 0.4494 0.3710 0.3877 0.0547  0.0107  0.0461  401 A1IRK A C11 
5162 C  C12 . A1IRK B .   ? 0.5382 0.4629 0.4690 0.0674  0.0104  0.0499  401 A1IRK A C12 
5163 C  C13 . A1IRK B .   ? 0.6648 0.5774 0.5891 0.0764  0.0144  0.0540  401 A1IRK A C13 
5164 C  C14 . A1IRK B .   ? 0.2986 0.2551 0.2886 0.0025  -0.0077 0.0085  401 A1IRK A C14 
5165 C  C15 . A1IRK B .   ? 0.3895 0.3356 0.3761 0.0040  -0.0049 0.0085  401 A1IRK A C15 
5166 C  C16 . A1IRK B .   ? 0.3783 0.3263 0.3638 0.0097  -0.0048 0.0082  401 A1IRK A C16 
5167 C  C17 . A1IRK B .   ? 0.3393 0.2818 0.3270 -0.0014 -0.0047 0.0051  401 A1IRK A C17 
5168 C  C18 . A1IRK B .   ? 0.7092 0.6683 0.6588 0.0689  -0.0026 0.0350  401 A1IRK A C18 
5169 C  C19 . A1IRK B .   ? 0.6045 0.5572 0.5610 0.0605  -0.0015 0.0306  401 A1IRK A C19 
5170 C  C20 . A1IRK B .   ? 0.5330 0.4866 0.4960 0.0481  -0.0028 0.0268  401 A1IRK A C20 
5171 C  C21 . A1IRK B .   ? 0.4485 0.4150 0.4109 0.0639  -0.0047 0.0264  401 A1IRK A C21 
5172 C  C7  . A1IRK B .   ? 0.2521 0.2066 0.2357 0.0101  -0.0062 0.0147  401 A1IRK A C7  
5173 N  N1  . A1IRK B .   ? 0.2288 0.1855 0.2085 0.0175  -0.0061 0.0173  401 A1IRK A N1  
5174 N  N2  . A1IRK B .   ? 0.3330 0.3129 0.3300 0.0046  -0.0129 0.0064  401 A1IRK A N2  
5175 N  N3  . A1IRK B .   ? 0.4386 0.3747 0.3796 0.0525  0.0063  0.0437  401 A1IRK A N3  
5176 N  N4  . A1IRK B .   ? 0.6030 0.5512 0.5387 0.0625  0.0030  0.0451  401 A1IRK A N4  
5177 N  N5  . A1IRK B .   ? 0.6005 0.5428 0.5300 0.0719  0.0053  0.0491  401 A1IRK A N5  
5178 N  N6  . A1IRK B .   ? 0.7435 0.6619 0.6744 0.0762  0.0112  0.0486  401 A1IRK A N6  
5179 O  O1  . A1IRK B .   ? 0.2211 0.2071 0.2218 0.0015  -0.0144 0.0043  401 A1IRK A O1  
5180 O  O2  . A1IRK B .   ? 0.8562 0.8111 0.7856 0.0917  0.0010  0.0475  401 A1IRK A O2  
5181 O  O3  . A1IRK B .   ? 0.8242 0.7650 0.7604 0.0882  0.0044  0.0434  401 A1IRK A O3  
5182 O  O4  . A1IRK B .   ? 0.2937 0.2419 0.2769 0.0059  -0.0042 0.0155  401 A1IRK A O4  
5183 O  O5  . A1IRK B .   ? 0.3129 0.2836 0.3052 0.0025  -0.0112 0.0099  401 A1IRK A O5  
5184 S  S1  . A1IRK B .   ? 1.7863 1.7302 1.7222 0.0826  0.0033  0.0440  401 A1IRK A S1  
5217 ZN ZN  . ZN    C .   ? 0.1774 0.1580 0.1759 -0.0020 -0.0138 0.0060  402 ZN    A ZN  
5218 O  O   . HOH   D .   ? 0.2690 0.3846 0.2645 0.0566  0.0557  0.0090  501 HOH   A O   
5219 O  O   . HOH   D .   ? 0.3806 0.4553 0.3816 0.0022  -0.0409 -0.0719 502 HOH   A O   
5220 O  O   . HOH   D .   ? 0.4426 0.4995 0.4664 -0.0173 -0.0338 -0.0805 503 HOH   A O   
5221 O  O   . HOH   D .   ? 0.5428 0.5526 0.4086 0.0427  -0.0166 -0.0830 504 HOH   A O   
5222 O  O   . HOH   D .   ? 0.5285 0.4144 0.4755 0.0287  0.0238  0.0444  505 HOH   A O   
5223 O  O   . HOH   D .   ? 0.5804 0.4655 0.5028 0.0399  0.0193  -0.0627 506 HOH   A O   
5224 O  O   . HOH   D .   ? 0.4002 0.3511 0.3699 0.0803  0.0168  -0.0042 507 HOH   A O   
5225 O  O   . HOH   D .   ? 0.5696 0.4635 0.4852 0.0333  0.0569  0.0814  508 HOH   A O   
5226 O  O   . HOH   D .   ? 0.5936 0.4460 0.5286 -0.0115 0.0098  -0.1085 509 HOH   A O   
5227 O  O   . HOH   D .   ? 0.4091 0.4203 0.3412 0.0204  -0.0198 -0.0155 510 HOH   A O   
5228 O  O   . HOH   D .   ? 0.4504 0.4741 0.4336 0.0962  -0.0083 0.0147  511 HOH   A O   
5229 O  O   . HOH   D .   ? 0.6075 0.5112 0.5465 0.0174  0.0692  0.0654  512 HOH   A O   
5230 O  O   . HOH   D .   ? 0.4504 0.6666 0.5982 -0.0488 -0.0046 -0.0398 513 HOH   A O   
5231 O  O   . HOH   D .   ? 0.6218 0.5102 0.5816 -0.0006 0.0896  0.0656  514 HOH   A O   
5232 O  O   . HOH   D .   ? 0.2802 0.5346 0.3982 0.0115  -0.0310 -0.0326 515 HOH   A O   
5233 O  O   . HOH   D .   ? 0.6127 0.4400 0.6052 -0.0439 0.0480  0.0042  516 HOH   A O   
5234 O  O   . HOH   D .   ? 0.5023 0.4380 0.5109 -0.0462 0.0936  0.0619  517 HOH   A O   
5235 O  O   . HOH   D .   ? 0.3003 0.3426 0.2732 0.0211  0.0346  0.0253  518 HOH   A O   
5236 O  O   . HOH   D .   ? 0.4723 0.4794 0.3207 0.0574  -0.0042 -0.0765 519 HOH   A O   
5237 O  O   . HOH   D .   ? 0.3050 0.4247 0.3822 0.0001  -0.0221 -0.0382 520 HOH   A O   
5238 O  O   . HOH   D .   ? 0.5832 0.5992 0.5359 0.0194  0.1750  0.0790  521 HOH   A O   
5239 O  O   . HOH   D .   ? 0.4100 0.4093 0.3879 0.0667  0.0284  -0.0186 522 HOH   A O   
5240 O  O   . HOH   D .   ? 0.3952 0.3374 0.3799 0.0195  0.0079  -0.0281 523 HOH   A O   
5241 O  O   . HOH   D .   ? 0.3893 0.4070 0.3431 0.0380  0.0056  -0.0262 524 HOH   A O   
5242 O  O   . HOH   D .   ? 0.3123 0.5659 0.4041 0.0498  -0.0375 -0.0204 525 HOH   A O   
5243 O  O   . HOH   D .   ? 0.4898 0.5358 0.5339 -0.0579 -0.0289 -0.0647 526 HOH   A O   
5244 O  O   . HOH   D .   ? 0.5122 0.6459 0.5037 0.1270  -0.0263 0.0280  527 HOH   A O   
5245 O  O   . HOH   D .   ? 0.4336 0.3632 0.4635 -0.0629 0.0778  0.0403  528 HOH   A O   
5246 O  O   . HOH   D .   ? 0.5674 0.4441 0.5446 -0.0104 0.0804  0.0536  529 HOH   A O   
5247 O  O   . HOH   D .   ? 0.4487 0.4895 0.3504 0.0575  0.1637  0.0696  530 HOH   A O   
5248 O  O   . HOH   D .   ? 0.5546 0.4164 0.5854 -0.0804 0.0423  -0.0297 531 HOH   A O   
5249 O  O   . HOH   D .   ? 0.2561 0.3958 0.3178 0.0412  -0.0264 -0.0263 532 HOH   A O   
5250 O  O   . HOH   D .   ? 0.2879 0.1815 0.2627 -0.0065 0.0225  0.0280  533 HOH   A O   
5251 O  O   . HOH   D .   ? 0.5629 0.5950 0.3636 0.0961  0.0290  0.0095  534 HOH   A O   
5252 O  O   . HOH   D .   ? 0.5183 0.5118 0.4498 0.0829  0.0469  -0.0366 535 HOH   A O   
5253 O  O   . HOH   D .   ? 0.5570 0.4674 0.5729 -0.0235 0.0170  -0.0314 536 HOH   A O   
5254 O  O   . HOH   D .   ? 0.6114 0.6289 0.4074 0.1015  0.0697  0.0420  537 HOH   A O   
5255 O  O   . HOH   D .   ? 0.2285 0.2205 0.1851 0.0229  -0.0039 0.0237  538 HOH   A O   
5256 O  O   . HOH   D .   ? 0.3350 0.3772 0.3405 0.0204  0.0115  0.0055  539 HOH   A O   
5257 O  O   . HOH   D .   ? 0.4176 0.5438 0.4347 -0.0125 -0.0564 -0.0619 540 HOH   A O   
5258 O  O   . HOH   D .   ? 0.2091 0.1962 0.2040 0.0290  0.0048  -0.0054 541 HOH   A O   
5259 O  O   . HOH   D .   ? 0.4689 0.3684 0.4405 0.0360  0.0228  0.0249  542 HOH   A O   
5260 O  O   . HOH   D .   ? 0.4880 0.3818 0.5413 -0.0640 0.0971  0.0162  543 HOH   A O   
5261 O  O   . HOH   D .   ? 0.3666 0.5014 0.4282 0.0377  0.0778  -0.0077 544 HOH   A O   
5262 O  O   . HOH   D .   ? 0.2750 0.4122 0.3838 -0.0108 0.0030  -0.0366 545 HOH   A O   
5263 O  O   . HOH   D .   ? 0.3689 0.3940 0.2915 0.0467  -0.0043 0.0180  546 HOH   A O   
5264 O  O   . HOH   D .   ? 0.4973 0.5221 0.4788 0.0669  0.0386  -0.0187 547 HOH   A O   
5265 O  O   . HOH   D .   ? 0.4439 0.4751 0.5057 -0.0353 0.1075  0.0248  548 HOH   A O   
5266 O  O   . HOH   D .   ? 0.1681 0.2145 0.2121 -0.0043 -0.0116 -0.0155 549 HOH   A O   
5267 O  O   . HOH   D .   ? 0.3028 0.3338 0.2689 0.0196  -0.0228 -0.0207 550 HOH   A O   
5268 O  O   . HOH   D .   ? 0.5333 0.5140 0.4037 0.0589  0.0490  0.0489  551 HOH   A O   
5269 O  O   . HOH   D .   ? 0.5296 0.6200 0.4079 0.1036  0.1389  0.0149  552 HOH   A O   
5270 O  O   . HOH   D .   ? 0.4293 0.3818 0.4814 -0.0524 0.0947  0.0252  553 HOH   A O   
5271 O  O   . HOH   D .   ? 0.2889 0.2535 0.2864 -0.0300 -0.0151 -0.0296 554 HOH   A O   
5272 O  O   . HOH   D .   ? 0.2835 0.4009 0.3473 0.0186  -0.0234 -0.0287 555 HOH   A O   
5273 O  O   . HOH   D .   ? 0.4225 0.5459 0.4564 0.1139  -0.0056 -0.0064 556 HOH   A O   
5274 O  O   . HOH   D .   ? 0.3684 0.2526 0.3393 -0.0193 0.0668  0.0602  557 HOH   A O   
5275 O  O   . HOH   D .   ? 0.2824 0.2178 0.2836 -0.0360 0.0633  0.0485  558 HOH   A O   
5276 O  O   . HOH   D .   ? 0.2332 0.1666 0.2517 -0.0261 0.0195  0.0006  559 HOH   A O   
5277 O  O   . HOH   D .   ? 0.3511 0.5081 0.4783 -0.0591 0.0042  -0.0304 560 HOH   A O   
5278 O  O   . HOH   D .   ? 0.2381 0.1932 0.1909 0.0225  0.0064  -0.0257 561 HOH   A O   
5279 O  O   . HOH   D .   ? 0.4151 0.2593 0.4053 -0.0444 0.0831  0.0496  562 HOH   A O   
5280 O  O   . HOH   D .   ? 0.1772 0.3139 0.2506 -0.0058 0.0460  0.0143  563 HOH   A O   
5281 O  O   . HOH   D .   ? 0.4065 0.4540 0.4840 -0.0457 -0.0097 -0.0565 564 HOH   A O   
5282 O  O   . HOH   D .   ? 0.2061 0.1961 0.1959 0.0644  0.0025  0.0030  565 HOH   A O   
5283 O  O   . HOH   D .   ? 0.2685 0.2847 0.2289 0.0223  -0.0114 -0.0335 566 HOH   A O   
5284 O  O   . HOH   D .   ? 0.4388 0.4291 0.4787 -0.0690 -0.0129 -0.0625 567 HOH   A O   
5285 O  O   . HOH   D .   ? 0.5794 0.5888 0.4107 0.0832  0.0296  -0.0540 568 HOH   A O   
5286 O  O   . HOH   D .   ? 0.2857 0.2733 0.2637 0.0157  -0.0043 -0.0299 569 HOH   A O   
5287 O  O   . HOH   D .   ? 0.2402 0.2679 0.2063 0.0350  -0.0243 0.0060  570 HOH   A O   
5288 O  O   . HOH   D .   ? 0.4691 0.4172 0.3649 0.0396  0.0070  -0.0734 571 HOH   A O   
5289 O  O   . HOH   D .   ? 0.2149 0.3589 0.3150 0.0138  0.0255  -0.0236 572 HOH   A O   
5290 O  O   . HOH   D .   ? 0.5034 0.5737 0.4938 0.1339  -0.0097 0.0131  573 HOH   A O   
5291 O  O   . HOH   D .   ? 0.3091 0.3959 0.2957 0.0764  0.0414  -0.0084 574 HOH   A O   
5292 O  O   . HOH   D .   ? 0.5632 0.4705 0.4827 0.0432  0.0180  -0.0607 575 HOH   A O   
5293 O  O   . HOH   D .   ? 0.6162 0.5281 0.6223 -0.0273 0.0722  0.0363  576 HOH   A O   
5294 O  O   . HOH   D .   ? 0.4193 0.5648 0.4847 0.0842  0.0191  -0.0188 577 HOH   A O   
5295 O  O   . HOH   D .   ? 0.2100 0.2239 0.1800 0.0328  0.0375  -0.0038 578 HOH   A O   
5296 O  O   . HOH   D .   ? 0.3968 0.4485 0.3284 0.0601  0.0935  0.0131  579 HOH   A O   
5297 O  O   . HOH   D .   ? 0.3436 0.4997 0.4630 -0.0026 0.0407  -0.0250 580 HOH   A O   
5298 O  O   . HOH   D .   ? 0.4054 0.4559 0.3931 0.1221  0.0020  0.0292  581 HOH   A O   
5299 O  O   . HOH   D .   ? 0.5996 0.4072 0.5359 0.0226  0.0312  -0.0503 582 HOH   A O   
5300 O  O   . HOH   D .   ? 0.5060 0.4674 0.4742 -0.0309 -0.0221 -0.0903 583 HOH   A O   
5301 O  O   . HOH   D .   ? 0.4721 0.3668 0.4723 -0.0147 0.0362  0.0165  584 HOH   A O   
5302 O  O   . HOH   D .   ? 0.4850 0.4081 0.4452 0.0795  0.0173  0.0016  585 HOH   A O   
5303 O  O   . HOH   D .   ? 0.4879 0.3699 0.4809 -0.0059 0.0361  0.0168  586 HOH   A O   
5304 O  O   . HOH   D .   ? 0.3018 0.3945 0.3322 -0.0192 -0.0413 -0.0390 587 HOH   A O   
5305 O  O   . HOH   D .   ? 0.2726 0.1909 0.2430 0.0049  0.0345  0.0387  588 HOH   A O   
5306 O  O   . HOH   D .   ? 0.5248 0.4829 0.4784 0.0862  0.0331  -0.0280 589 HOH   A O   
5307 O  O   . HOH   D .   ? 0.4648 0.2704 0.4196 -0.0106 0.0290  -0.0557 590 HOH   A O   
5308 O  O   . HOH   D .   ? 0.6026 0.4169 0.5836 -0.0377 0.0332  -0.0376 591 HOH   A O   
5309 O  O   . HOH   D .   ? 0.3183 0.4501 0.3949 0.0387  0.0309  -0.0181 592 HOH   A O   
5310 O  O   . HOH   D .   ? 0.3407 0.3483 0.3660 -0.0238 -0.0179 -0.0543 593 HOH   A O   
5311 O  O   . HOH   D .   ? 0.5666 0.4701 0.4538 0.0668  0.0460  0.0880  594 HOH   A O   
5312 O  O   . HOH   D .   ? 0.3073 0.3117 0.3271 -0.0170 -0.0175 -0.0279 595 HOH   A O   
5313 O  O   . HOH   D .   ? 0.3588 0.4654 0.4097 0.0541  0.0345  -0.0152 596 HOH   A O   
5314 O  O   . HOH   D .   ? 0.3863 0.5439 0.4462 0.0669  0.0070  0.0030  597 HOH   A O   
5315 O  O   . HOH   D .   ? 0.4892 0.4486 0.4481 0.0017  -0.0087 -0.0293 598 HOH   A O   
5316 O  O   . HOH   D .   ? 0.4264 0.4842 0.4368 0.1097  0.0191  -0.0089 599 HOH   A O   
5317 O  O   . HOH   D .   ? 0.1584 0.1613 0.2119 -0.0354 0.0203  -0.0084 600 HOH   A O   
5318 O  O   . HOH   D .   ? 0.2674 0.2656 0.2493 0.0052  -0.0147 -0.0513 601 HOH   A O   
5319 O  O   . HOH   D .   ? 0.3566 0.4045 0.3507 0.0610  -0.0232 0.0061  602 HOH   A O   
5320 O  O   . HOH   D .   ? 0.3359 0.3307 0.3303 0.0123  -0.0167 0.0065  603 HOH   A O   
5321 O  O   . HOH   D .   ? 0.4824 0.3573 0.4836 -0.0546 0.0143  -0.0521 604 HOH   A O   
5322 O  O   . HOH   D .   ? 0.4027 0.4536 0.4960 -0.0778 0.0203  -0.0191 605 HOH   A O   
5323 O  O   . HOH   D .   ? 0.2027 0.2086 0.2846 -0.0558 0.0424  -0.0143 606 HOH   A O   
5324 O  O   . HOH   D .   ? 0.3265 0.2344 0.3341 -0.0141 0.0177  -0.0158 607 HOH   A O   
5325 O  O   . HOH   D .   ? 0.2845 0.2380 0.2772 -0.0186 -0.0105 -0.0108 608 HOH   A O   
5326 O  O   . HOH   D .   ? 0.2281 0.2117 0.2153 0.0114  -0.0039 -0.0179 609 HOH   A O   
5327 O  O   . HOH   D .   ? 0.2568 0.3262 0.3594 -0.0460 0.0222  -0.0306 610 HOH   A O   
5328 O  O   . HOH   D .   ? 0.4679 0.4725 0.4026 0.0588  -0.0124 0.0314  611 HOH   A O   
5329 O  O   . HOH   D .   ? 0.2962 0.3161 0.3228 -0.0162 -0.0202 -0.0278 612 HOH   A O   
5330 O  O   . HOH   D .   ? 0.2827 0.3095 0.2388 0.0321  0.0076  -0.0064 613 HOH   A O   
5331 O  O   . HOH   D .   ? 0.4819 0.7243 0.5474 0.0966  -0.0466 -0.0365 614 HOH   A O   
5332 O  O   . HOH   D .   ? 0.3832 0.6186 0.4515 0.0215  -0.0598 -0.0445 615 HOH   A O   
5333 O  O   . HOH   D .   ? 0.3832 0.3520 0.3683 0.0408  0.0104  -0.0112 616 HOH   A O   
5334 O  O   . HOH   D .   ? 0.1994 0.1604 0.1913 -0.0081 -0.0047 0.0147  617 HOH   A O   
5335 O  O   . HOH   D .   ? 0.5027 0.4118 0.4572 0.0468  0.0227  0.0434  618 HOH   A O   
5336 O  O   . HOH   D .   ? 0.2329 0.3575 0.3446 -0.0232 0.0835  -0.0064 619 HOH   A O   
5337 O  O   . HOH   D .   ? 0.2418 0.1752 0.2416 -0.0022 0.0060  -0.0173 620 HOH   A O   
5338 O  O   . HOH   D .   ? 0.3703 0.4096 0.4461 -0.0635 0.0421  0.0091  621 HOH   A O   
5339 O  O   . HOH   D .   ? 0.5179 0.4258 0.4741 0.0432  0.0099  0.0283  622 HOH   A O   
5340 O  O   . HOH   D .   ? 0.3803 0.4305 0.3657 0.0378  0.0222  0.0004  623 HOH   A O   
5341 O  O   . HOH   D .   ? 0.3975 0.3748 0.4643 -0.0798 0.0577  0.0123  624 HOH   A O   
5342 O  O   . HOH   D .   ? 0.2270 0.1717 0.2208 -0.0181 0.0113  0.0219  625 HOH   A O   
5343 O  O   . HOH   D .   ? 0.1592 0.1399 0.1657 -0.0118 -0.0127 0.0004  626 HOH   A O   
5344 O  O   . HOH   D .   ? 0.3588 0.3835 0.3284 0.0429  -0.0206 0.0214  627 HOH   A O   
5345 O  O   . HOH   D .   ? 0.5350 0.4962 0.4268 0.0625  0.0231  0.0585  628 HOH   A O   
5346 O  O   . HOH   D .   ? 0.3673 0.3555 0.2322 0.0812  0.0391  -0.0566 629 HOH   A O   
5347 O  O   . HOH   D .   ? 0.3356 0.3665 0.4334 -0.0588 0.0754  -0.0029 630 HOH   A O   
5348 O  O   . HOH   D .   ? 0.4576 0.4276 0.3189 0.0649  0.0180  -0.0775 631 HOH   A O   
5349 O  O   . HOH   D .   ? 0.2839 0.2874 0.2148 0.0433  -0.0027 0.0300  632 HOH   A O   
5350 O  O   . HOH   D .   ? 0.3307 0.2865 0.3632 -0.0349 0.0032  -0.0427 633 HOH   A O   
5351 O  O   . HOH   D .   ? 0.3671 0.5647 0.4569 -0.0178 -0.0445 -0.0493 634 HOH   A O   
5352 O  O   . HOH   D .   ? 0.2333 0.3772 0.3429 -0.0511 -0.0091 -0.0332 635 HOH   A O   
5353 O  O   . HOH   D .   ? 0.3816 0.5620 0.5382 -0.0366 0.0129  -0.0567 636 HOH   A O   
5354 O  O   . HOH   D .   ? 0.2732 0.3152 0.2805 0.0545  0.0298  -0.0128 637 HOH   A O   
5355 O  O   . HOH   D .   ? 0.5459 0.4909 0.5103 0.1062  0.0229  0.0263  638 HOH   A O   
5356 O  O   . HOH   D .   ? 0.5379 0.5720 0.5234 0.0093  0.0334  0.0283  639 HOH   A O   
5357 O  O   . HOH   D .   ? 0.2015 0.2381 0.2937 -0.0526 0.0260  -0.0271 640 HOH   A O   
5358 O  O   . HOH   D .   ? 0.3609 0.4526 0.3707 0.1045  -0.0059 0.0204  641 HOH   A O   
5359 O  O   . HOH   D .   ? 0.2198 0.1387 0.2228 -0.0344 0.0222  0.0155  642 HOH   A O   
5360 O  O   . HOH   D .   ? 0.3546 0.3745 0.3022 0.0705  0.0508  -0.0230 643 HOH   A O   
5361 O  O   . HOH   D .   ? 0.3237 0.6095 0.5420 -0.0267 0.0412  -0.0636 644 HOH   A O   
5362 O  O   . HOH   D .   ? 0.4888 0.4881 0.3851 0.1011  0.0601  -0.0493 645 HOH   A O   
5363 O  O   . HOH   D .   ? 0.4162 0.4665 0.4130 0.0055  0.0479  0.0335  646 HOH   A O   
5364 O  O   . HOH   D .   ? 0.2378 0.2108 0.1995 0.0090  0.0399  0.0296  647 HOH   A O   
5365 O  O   . HOH   D .   ? 0.3126 0.3880 0.2852 0.0615  0.0865  -0.0012 648 HOH   A O   
5366 O  O   . HOH   D .   ? 0.4788 0.4424 0.5309 -0.0789 0.0084  -0.0414 649 HOH   A O   
5367 O  O   . HOH   D .   ? 0.3388 0.2843 0.3492 -0.0171 0.0013  -0.0424 650 HOH   A O   
5368 O  O   . HOH   D .   ? 0.5948 0.5660 0.5197 0.0264  0.0634  0.0733  651 HOH   A O   
5369 O  O   . HOH   D .   ? 0.4724 0.3716 0.4950 -0.0322 0.0317  -0.0108 652 HOH   A O   
5370 O  O   . HOH   D .   ? 0.2777 0.2476 0.2603 -0.0138 -0.0160 -0.0196 653 HOH   A O   
5371 O  O   . HOH   D .   ? 0.5087 0.4721 0.4900 0.0711  0.0182  0.0000  654 HOH   A O   
5372 O  O   . HOH   D .   ? 0.5323 0.4268 0.4493 0.0593  0.0278  0.0651  655 HOH   A O   
5373 O  O   . HOH   D .   ? 0.2029 0.3609 0.2970 0.0153  -0.0178 -0.0386 656 HOH   A O   
5374 O  O   . HOH   D .   ? 0.4697 0.4700 0.4652 -0.0286 -0.0269 -0.0447 657 HOH   A O   
5375 O  O   . HOH   D .   ? 0.3794 0.4376 0.4571 -0.0581 0.0593  0.0204  658 HOH   A O   
5376 O  O   . HOH   D .   ? 0.4293 0.4916 0.3421 0.0735  0.1092  0.0156  659 HOH   A O   
5377 O  O   . HOH   D .   ? 0.6303 0.5679 0.5716 0.0170  0.0551  0.0528  660 HOH   A O   
5378 O  O   . HOH   D .   ? 0.2803 0.2499 0.2787 -0.0231 -0.0148 -0.0135 661 HOH   A O   
5379 O  O   . HOH   D .   ? 0.4251 0.3505 0.4537 -0.0411 0.0787  0.0281  662 HOH   A O   
5380 O  O   . HOH   D .   ? 0.2161 0.2486 0.1944 0.0338  0.0527  0.0015  663 HOH   A O   
5381 O  O   . HOH   D .   ? 0.4038 0.4044 0.3559 0.0616  -0.0100 0.0365  664 HOH   A O   
5382 O  O   . HOH   D .   ? 0.1788 0.2816 0.2559 0.0045  0.0408  -0.0119 665 HOH   A O   
5383 O  O   . HOH   D .   ? 0.4816 0.5288 0.3338 0.0907  0.1115  0.0255  666 HOH   A O   
5384 O  O   . HOH   D .   ? 0.4890 0.4689 0.3806 0.0465  0.1475  0.0872  667 HOH   A O   
5385 O  O   . HOH   D .   ? 0.3819 0.3452 0.2775 0.0846  0.0422  -0.0577 668 HOH   A O   
5386 O  O   . HOH   D .   ? 0.3435 0.3671 0.3228 0.0111  0.0225  0.0234  669 HOH   A O   
5387 O  O   . HOH   D .   ? 0.6227 0.6099 0.5277 0.0502  0.0061  0.0366  670 HOH   A O   
5388 O  O   . HOH   D .   ? 0.5722 0.5678 0.5162 0.0167  0.0708  0.0677  671 HOH   A O   
5389 O  O   . HOH   D .   ? 0.4272 0.3814 0.3712 0.0674  0.0075  0.0478  672 HOH   A O   
5390 O  O   . HOH   D .   ? 0.5488 0.3840 0.5122 -0.0068 0.0459  0.0352  673 HOH   A O   
5391 O  O   . HOH   D .   ? 0.2234 0.2249 0.2418 -0.0144 -0.0164 -0.0152 674 HOH   A O   
5392 O  O   . HOH   D .   ? 0.4536 0.4106 0.4018 0.0114  0.1015  0.0629  675 HOH   A O   
5393 O  O   . HOH   D .   ? 0.5247 0.5621 0.4361 0.0556  -0.0233 0.0140  676 HOH   A O   
5394 O  O   . HOH   D .   ? 0.3407 0.3614 0.2800 0.0444  -0.0153 0.0172  677 HOH   A O   
5395 O  O   . HOH   D .   ? 0.3792 0.6513 0.4804 0.0057  -0.0571 -0.0597 678 HOH   A O   
5396 O  O   . HOH   D .   ? 0.4108 0.4990 0.3804 0.0931  -0.0294 0.0275  679 HOH   A O   
5397 O  O   . HOH   D .   ? 0.4456 0.5312 0.4592 0.0675  -0.0259 -0.0030 680 HOH   A O   
5398 O  O   . HOH   D .   ? 0.2954 0.2516 0.2561 0.0068  0.0491  0.0396  681 HOH   A O   
5399 O  O   . HOH   D .   ? 0.4081 0.3137 0.4258 -0.0287 0.0337  0.0025  682 HOH   A O   
5400 O  O   . HOH   D .   ? 0.2329 0.1553 0.2084 0.0006  0.0102  0.0264  683 HOH   A O   
5401 O  O   . HOH   D .   ? 0.3884 0.3865 0.4527 -0.0484 0.0063  -0.0375 684 HOH   A O   
5402 O  O   . HOH   D .   ? 0.5480 0.4521 0.5315 0.0225  0.0189  -0.0245 685 HOH   A O   
5403 O  O   . HOH   D .   ? 0.3976 0.5343 0.5588 -0.0615 0.0579  -0.0376 686 HOH   A O   
5404 O  O   . HOH   D .   ? 0.1808 0.1692 0.1767 -0.0082 0.0002  0.0164  687 HOH   A O   
5405 O  O   . HOH   D .   ? 0.5177 0.3683 0.4980 -0.0228 0.0369  0.0173  688 HOH   A O   
5406 O  O   . HOH   D .   ? 0.4058 0.3405 0.4155 -0.0249 0.0515  0.0261  689 HOH   A O   
5407 O  O   . HOH   D .   ? 0.3690 0.3872 0.3519 -0.0163 -0.0325 -0.0427 690 HOH   A O   
5408 O  O   . HOH   D .   ? 0.2581 0.2776 0.2207 0.0198  -0.0139 -0.0098 691 HOH   A O   
5409 O  O   . HOH   D .   ? 0.3897 0.3533 0.4690 -0.0672 0.0707  -0.0028 692 HOH   A O   
5410 O  O   . HOH   D .   ? 0.2179 0.3321 0.2855 0.0215  0.0560  -0.0093 693 HOH   A O   
5411 O  O   . HOH   D .   ? 0.2452 0.2664 0.3396 -0.0596 0.0554  -0.0123 694 HOH   A O   
5412 O  O   . HOH   D .   ? 0.5955 0.6244 0.4931 0.1043  0.0736  -0.0385 695 HOH   A O   
5413 O  O   . HOH   D .   ? 0.1978 0.2198 0.1656 0.0195  0.0126  0.0135  696 HOH   A O   
5414 O  O   . HOH   D .   ? 0.5058 0.4107 0.4081 0.0758  0.0374  0.0764  697 HOH   A O   
5415 O  O   . HOH   D .   ? 0.2548 0.2598 0.2044 0.0438  0.0361  -0.0126 698 HOH   A O   
5416 O  O   . HOH   D .   ? 0.5816 0.5783 0.4389 0.0887  0.0279  0.0708  699 HOH   A O   
5417 O  O   . HOH   D .   ? 0.5198 0.5092 0.6285 -0.0844 0.0375  -0.0547 700 HOH   A O   
5418 O  O   . HOH   D .   ? 0.2407 0.1687 0.2053 0.0125  0.0027  -0.0229 701 HOH   A O   
5419 O  O   . HOH   D .   ? 0.3780 0.3263 0.3357 0.0776  0.0026  0.0266  702 HOH   A O   
5420 O  O   . HOH   D .   ? 0.5655 0.5145 0.5271 0.0071  -0.0026 -0.0252 703 HOH   A O   
5421 O  O   . HOH   D .   ? 0.2137 0.3938 0.3356 0.0002  -0.0080 -0.0471 704 HOH   A O   
5422 O  O   . HOH   D .   ? 0.2982 0.2971 0.3375 -0.0340 -0.0109 -0.0516 705 HOH   A O   
5423 O  O   . HOH   D .   ? 0.4263 0.4083 0.3391 0.0350  0.0303  0.0292  706 HOH   A O   
5424 O  O   . HOH   D .   ? 0.4196 0.4333 0.4130 0.0688  0.0230  -0.0135 707 HOH   A O   
5425 O  O   . HOH   D .   ? 0.3348 0.4992 0.4341 0.0342  0.0111  -0.0273 708 HOH   A O   
5426 O  O   . HOH   D .   ? 0.3020 0.2738 0.2671 -0.0022 -0.0132 -0.0222 709 HOH   A O   
5427 O  O   . HOH   D .   ? 0.5140 0.3581 0.4382 0.0214  0.0703  0.0814  710 HOH   A O   
5428 O  O   . HOH   D .   ? 0.2466 0.2142 0.2203 0.0445  0.0001  0.0292  711 HOH   A O   
5429 O  O   . HOH   D .   ? 0.3212 0.4630 0.4291 -0.0034 0.0616  -0.0149 712 HOH   A O   
5430 O  O   . HOH   D .   ? 0.3155 0.4810 0.3532 0.0717  -0.0317 0.0033  713 HOH   A O   
5431 O  O   . HOH   D .   ? 0.3712 0.4625 0.4300 -0.0236 0.0532  0.0239  714 HOH   A O   
5432 O  O   . HOH   D .   ? 0.5453 0.5747 0.4162 0.1001  0.0731  -0.0338 715 HOH   A O   
5433 O  O   . HOH   D .   ? 0.5351 0.5805 0.3561 0.1027  0.1224  0.0410  716 HOH   A O   
5434 O  O   . HOH   D .   ? 0.3655 0.5009 0.4242 -0.0211 -0.0418 -0.0421 717 HOH   A O   
5435 O  O   . HOH   D .   ? 0.3368 0.4163 0.3503 0.0078  0.0535  0.0293  718 HOH   A O   
5436 O  O   . HOH   D .   ? 0.4090 0.4962 0.3815 0.1239  -0.0193 0.0366  719 HOH   A O   
5437 O  O   . HOH   D .   ? 0.5131 0.7239 0.6401 0.0331  0.0099  -0.0374 720 HOH   A O   
5438 O  O   . HOH   D .   ? 0.5595 0.4828 0.4973 0.0102  0.1629  0.0973  721 HOH   A O   
5439 O  O   . HOH   D .   ? 0.2141 0.1659 0.2226 -0.0308 0.0093  0.0120  722 HOH   A O   
5440 O  O   . HOH   D .   ? 0.4113 0.4358 0.3700 0.1019  -0.0085 0.0418  723 HOH   A O   
5441 O  O   . HOH   D .   ? 0.3135 0.4183 0.3256 0.0563  0.0868  -0.0040 724 HOH   A O   
5442 O  O   . HOH   D .   ? 0.4163 0.4609 0.2887 0.0909  0.0870  -0.0070 725 HOH   A O   
5443 O  O   . HOH   D .   ? 0.3402 0.3686 0.3153 0.0580  0.0438  -0.0157 726 HOH   A O   
5444 O  O   . HOH   D .   ? 0.3170 0.3424 0.2597 0.0328  -0.0096 0.0030  727 HOH   A O   
5445 O  O   . HOH   D .   ? 0.4545 0.6051 0.4991 0.0365  0.1406  0.0148  728 HOH   A O   
5446 O  O   . HOH   D .   ? 0.3959 0.2976 0.3283 0.0498  0.0217  -0.0459 729 HOH   A O   
5447 O  O   . HOH   D .   ? 0.5051 0.5370 0.4555 0.0280  -0.0161 -0.0228 730 HOH   A O   
5448 O  O   . HOH   D .   ? 0.4271 0.3552 0.4817 -0.0558 0.0329  -0.0294 731 HOH   A O   
5449 O  O   . HOH   D .   ? 0.5009 0.5034 0.4145 0.0391  0.1587  0.0810  732 HOH   A O   
5450 O  O   . HOH   D .   ? 0.4326 0.4086 0.5110 -0.0643 0.0262  -0.0388 733 HOH   A O   
5451 O  O   . HOH   D .   ? 0.3089 0.2895 0.2911 0.0810  0.0095  0.0015  734 HOH   A O   
5452 O  O   . HOH   D .   ? 0.3800 0.3549 0.3447 0.0055  -0.0038 -0.0085 735 HOH   A O   
5453 O  O   . HOH   D .   ? 0.6957 0.6972 0.6003 0.0426  -0.0003 0.0168  736 HOH   A O   
5454 O  O   . HOH   D .   ? 0.4942 0.3790 0.4219 0.0262  0.0505  0.0724  737 HOH   A O   
5455 O  O   . HOH   D .   ? 0.2378 0.2161 0.2278 0.0178  0.0005  -0.0120 738 HOH   A O   
5456 O  O   . HOH   D .   ? 0.2795 0.4987 0.4304 0.0073  0.0234  -0.0424 739 HOH   A O   
5457 O  O   . HOH   D .   ? 0.3346 0.2611 0.3405 -0.0218 0.0420  0.0233  740 HOH   A O   
5458 O  O   . HOH   D .   ? 0.4117 0.6743 0.5298 0.0345  -0.0197 -0.0206 741 HOH   A O   
5459 O  O   . HOH   D .   ? 0.4866 0.4638 0.5466 -0.0518 0.1021  0.0255  742 HOH   A O   
5460 O  O   . HOH   D .   ? 0.3022 0.2807 0.2395 0.0224  0.0392  0.0300  743 HOH   A O   
5461 O  O   . HOH   D .   ? 0.3178 0.3881 0.4327 -0.0550 0.0420  -0.0263 744 HOH   A O   
5462 O  O   . HOH   D .   ? 0.6361 0.3979 0.5803 0.0026  0.0440  -0.0464 745 HOH   A O   
5463 O  O   . HOH   D .   ? 0.3858 0.3252 0.2588 0.0753  0.0308  -0.0814 746 HOH   A O   
5464 O  O   . HOH   D .   ? 0.3264 0.2644 0.2426 0.0534  0.0207  0.0617  747 HOH   A O   
5465 O  O   . HOH   D .   ? 0.4159 0.3278 0.3521 0.0250  0.0498  0.0595  748 HOH   A O   
5466 O  O   . HOH   D .   ? 0.5453 0.6511 0.4777 0.0317  -0.0570 -0.0520 749 HOH   A O   
5467 O  O   . HOH   D .   ? 0.3752 0.4181 0.2525 0.0806  0.0938  0.0116  750 HOH   A O   
5468 O  O   . HOH   D .   ? 0.2628 0.3822 0.2934 -0.0039 -0.0459 -0.0338 751 HOH   A O   
5469 O  O   . HOH   D .   ? 0.2416 0.3480 0.2440 0.0233  -0.0449 -0.0150 752 HOH   A O   
5470 O  O   . HOH   D .   ? 0.4274 0.6337 0.4554 0.0396  -0.0640 -0.0348 753 HOH   A O   
5471 O  O   . HOH   D .   ? 0.4821 0.5671 0.5685 -0.0745 -0.0204 -0.0632 754 HOH   A O   
5472 O  O   . HOH   D .   ? 0.3314 0.2832 0.2982 0.0160  0.0029  -0.0180 755 HOH   A O   
5473 O  O   . HOH   D .   ? 0.4685 0.3284 0.4546 -0.0071 0.0558  0.0316  756 HOH   A O   
5474 O  O   . HOH   D .   ? 0.4495 0.3972 0.5731 -0.1055 0.0806  -0.0470 757 HOH   A O   
5475 O  O   . HOH   D .   ? 0.4967 0.4105 0.4378 0.0082  0.0661  0.0754  758 HOH   A O   
5476 O  O   . HOH   D .   ? 0.5975 0.4679 0.5914 0.0012  0.0306  -0.0128 759 HOH   A O   
5477 O  O   . HOH   D .   ? 0.3294 0.4857 0.3729 0.0944  -0.0092 0.0095  760 HOH   A O   
5478 O  O   . HOH   D .   ? 0.6164 0.4671 0.5525 0.0836  0.0318  -0.0003 761 HOH   A O   
5479 O  O   . HOH   D .   ? 0.3991 0.4687 0.3225 0.0471  -0.0394 -0.0098 762 HOH   A O   
5480 O  O   . HOH   D .   ? 0.5532 0.5575 0.4355 0.0662  0.0299  0.0579  763 HOH   A O   
5481 O  O   . HOH   D .   ? 0.4618 0.4848 0.3775 0.0464  -0.0179 0.0134  764 HOH   A O   
5482 O  O   . HOH   D .   ? 0.3062 0.3564 0.3238 0.0609  0.0208  -0.0116 765 HOH   A O   
5483 O  O   . HOH   D .   ? 0.4098 0.3650 0.3877 0.0777  0.0178  0.0111  766 HOH   A O   
5484 O  O   . HOH   D .   ? 0.6624 0.5956 0.6337 0.0264  0.0010  0.0200  767 HOH   A O   
5485 O  O   . HOH   D .   ? 0.1672 0.3712 0.2505 0.0846  -0.0182 -0.0275 768 HOH   A O   
5486 O  O   . HOH   D .   ? 0.5181 0.5463 0.4567 0.0353  0.0117  0.0122  769 HOH   A O   
5487 O  O   . HOH   D .   ? 0.4427 0.3795 0.4123 -0.0052 0.1102  0.0647  770 HOH   A O   
5488 O  O   . HOH   D .   ? 0.3543 0.3354 0.2980 0.0736  0.0374  -0.0326 771 HOH   A O   
5489 O  O   . HOH   D .   ? 0.4526 0.5611 0.5095 -0.0365 -0.0378 -0.0488 772 HOH   A O   
5490 O  O   . HOH   D .   ? 0.6188 0.5754 0.5212 0.0373  0.0969  0.0715  773 HOH   A O   
5491 O  O   . HOH   D .   ? 0.3931 0.6097 0.5500 -0.0388 0.1982  0.0222  774 HOH   A O   
5492 O  O   . HOH   D .   ? 0.5552 0.5817 0.4775 0.0443  0.0025  0.0169  775 HOH   A O   
5493 O  O   . HOH   D .   ? 0.2571 0.3976 0.3758 -0.0244 -0.0014 -0.0471 776 HOH   A O   
5494 O  O   . HOH   D .   ? 0.4239 0.5540 0.4112 0.0438  -0.0519 -0.0138 777 HOH   A O   
5495 O  O   . HOH   D .   ? 0.4347 0.4406 0.3583 0.0345  -0.0106 0.0120  778 HOH   A O   
5496 O  O   . HOH   D .   ? 0.3858 0.2759 0.3201 0.0643  0.0275  -0.0390 779 HOH   A O   
5497 O  O   . HOH   D .   ? 0.5708 0.6936 0.5323 0.0913  0.1274  -0.0009 780 HOH   A O   
5498 O  O   . HOH   D .   ? 0.4646 0.4463 0.4161 0.0068  -0.0115 -0.0201 781 HOH   A O   
5499 O  O   . HOH   D .   ? 0.4499 0.6959 0.5885 0.0420  -0.0011 -0.0453 782 HOH   A O   
5500 O  O   . HOH   D .   ? 0.4507 0.4488 0.5307 -0.0851 0.0410  -0.0061 783 HOH   A O   
5501 O  O   . HOH   D .   ? 0.3977 0.5029 0.5327 -0.0588 0.0220  -0.0494 784 HOH   A O   
5502 O  O   . HOH   D .   ? 0.3296 0.5433 0.4899 -0.0074 0.0574  -0.0337 785 HOH   A O   
5503 O  O   . HOH   D .   ? 0.5702 0.5709 0.5115 0.0238  0.0404  0.0490  786 HOH   A O   
5504 O  O   . HOH   D .   ? 0.3745 0.4653 0.4004 -0.0266 -0.0450 -0.0547 787 HOH   A O   
5505 O  O   . HOH   D .   ? 0.6332 0.6456 0.5922 0.0816  -0.0093 0.0386  788 HOH   A O   
5506 O  O   . HOH   D .   ? 0.5740 0.4875 0.5279 -0.0295 -0.0099 -0.1101 789 HOH   A O   
5507 O  O   . HOH   D .   ? 0.5135 0.4036 0.4583 0.0049  0.0627  0.0715  790 HOH   A O   
5508 O  O   . HOH   D .   ? 0.4069 0.3262 0.4144 -0.0136 0.0113  -0.0305 791 HOH   A O   
5509 O  O   . HOH   D .   ? 0.3696 0.4659 0.5075 -0.0615 0.0757  -0.0191 792 HOH   A O   
5510 O  O   . HOH   D .   ? 0.4766 0.5598 0.5132 -0.0060 0.0458  0.0240  793 HOH   A O   
5511 O  O   . HOH   D .   ? 0.3963 0.4846 0.3599 0.0794  0.0957  -0.0074 794 HOH   A O   
5512 O  O   . HOH   D .   ? 0.3725 0.3810 0.3224 0.0406  -0.0149 0.0206  795 HOH   A O   
5513 O  O   . HOH   D .   ? 0.5870 0.5216 0.5342 0.1265  0.0176  0.0228  796 HOH   A O   
5514 O  O   . HOH   D .   ? 0.3861 0.5425 0.4141 0.0067  -0.0568 -0.0435 797 HOH   A O   
5515 O  O   . HOH   D .   ? 0.4826 0.5141 0.3985 0.0553  -0.0096 0.0185  798 HOH   A O   
5516 O  O   . HOH   D .   ? 0.3440 0.3747 0.2961 0.0311  0.0151  0.0092  799 HOH   A O   
5517 O  O   . HOH   D .   ? 0.5726 0.6061 0.5015 0.0411  -0.0007 0.0014  800 HOH   A O   
5518 O  O   . HOH   D .   ? 0.5390 0.4801 0.4266 0.0747  0.0278  0.0761  801 HOH   A O   
5519 O  O   . HOH   D .   ? 0.5302 0.5460 0.4499 0.0427  0.0185  0.0337  802 HOH   A O   
5520 O  O   . HOH   D .   ? 0.4381 0.4595 0.4159 0.0328  0.0105  -0.0089 803 HOH   A O   
5521 O  O   . HOH   D .   ? 0.6117 0.5430 0.5669 0.1083  0.0193  0.0103  804 HOH   A O   
5522 O  O   . HOH   D .   ? 0.6569 0.5616 0.5619 0.0474  0.0575  0.0761  805 HOH   A O   
5523 O  O   . HOH   D .   ? 0.4052 0.6632 0.5701 0.0109  0.0015  -0.0578 806 HOH   A O   
5524 O  O   . HOH   D .   ? 0.4369 0.6164 0.4517 0.0327  -0.0623 -0.0351 807 HOH   A O   
5525 O  O   . HOH   D .   ? 0.5741 0.5980 0.5741 0.0730  0.0110  0.0060  808 HOH   A O   
5526 O  O   . HOH   D .   ? 0.4840 0.4553 0.5137 -0.0343 0.1098  0.0411  809 HOH   A O   
5527 O  O   . HOH   D .   ? 0.3730 0.6607 0.5711 -0.0017 0.0248  -0.0608 810 HOH   A O   
5528 O  O   . HOH   D .   ? 0.6359 0.5601 0.6313 0.0009  0.0091  -0.0340 811 HOH   A O   
5529 O  O   . HOH   D .   ? 0.3694 0.6354 0.5655 -0.0231 0.0118  -0.0708 812 HOH   A O   
5530 O  O   . HOH   D .   ? 0.4718 0.4914 0.4817 -0.0408 -0.0313 -0.0622 813 HOH   A O   
5531 O  O   . HOH   D .   ? 0.4798 0.3971 0.4721 -0.0432 -0.0039 -0.0600 814 HOH   A O   
5532 O  O   . HOH   D .   ? 0.6312 0.4808 0.5583 0.0705  0.0340  -0.0386 815 HOH   A O   
5533 O  O   . HOH   D .   ? 0.4935 0.4091 0.4340 0.0796  0.0308  -0.0327 816 HOH   A O   
5534 O  O   . HOH   D .   ? 0.4574 0.5947 0.5244 0.0538  0.0489  -0.0168 817 HOH   A O   
5535 O  O   . HOH   D .   ? 0.3547 0.2864 0.3233 0.0405  0.0120  0.0319  818 HOH   A O   
5536 O  O   . HOH   D .   ? 0.6360 0.6774 0.4695 0.1045  0.0828  -0.0152 819 HOH   A O   
5537 O  O   . HOH   D .   ? 0.2962 0.4305 0.3852 0.0173  0.0449  -0.0163 820 HOH   A O   
5538 O  O   . HOH   D .   ? 0.5120 0.5428 0.5138 0.0663  0.0130  0.0013  821 HOH   A O   
5539 O  O   . HOH   D .   ? 0.3254 0.4779 0.4341 -0.0122 -0.0165 -0.0512 822 HOH   A O   
5540 O  O   . HOH   D .   ? 0.4671 0.5682 0.3913 0.0461  -0.0521 -0.0305 823 HOH   A O   
5541 O  O   . HOH   D .   ? 0.4525 0.3291 0.4471 -0.0030 0.0323  0.0043  824 HOH   A O   
5542 O  O   . HOH   D .   ? 0.3927 0.3624 0.3782 0.0281  0.0059  -0.0160 825 HOH   A O   
5543 O  O   . HOH   D .   ? 0.4269 0.3948 0.4196 -0.0322 -0.0183 -0.0457 826 HOH   A O   
5544 O  O   . HOH   D .   ? 0.3872 0.6644 0.6122 -0.0436 0.0384  -0.0708 827 HOH   A O   
5545 O  O   . HOH   D .   ? 0.2971 0.5261 0.4514 -0.0090 -0.0114 -0.0658 828 HOH   A O   
5546 O  O   . HOH   D .   ? 0.5455 0.4853 0.5473 -0.0094 0.0028  -0.0472 829 HOH   A O   
5547 O  O   . HOH   D .   ? 0.6295 0.6470 0.5219 0.0674  -0.0094 0.0318  830 HOH   A O   
5548 O  O   . HOH   D .   ? 0.4174 0.6024 0.4604 0.1110  -0.0184 0.0109  831 HOH   A O   
5549 O  O   . HOH   D .   ? 0.3367 0.3130 0.2965 0.0638  -0.0007 0.0382  832 HOH   A O   
5550 O  O   . HOH   D .   ? 0.6656 0.6885 0.4706 0.0893  0.0176  -0.0666 833 HOH   A O   
5551 O  O   . HOH   D .   ? 0.5514 0.4366 0.4559 0.0811  0.0430  0.0787  834 HOH   A O   
5552 O  O   . HOH   D .   ? 0.4758 0.5465 0.4992 0.0799  0.0247  -0.0137 835 HOH   A O   
5553 O  O   . HOH   D .   ? 0.3818 0.4156 0.3250 0.0327  -0.0134 -0.0304 836 HOH   A O   
5554 O  O   . HOH   D .   ? 0.5423 0.5502 0.4965 0.0038  -0.0258 -0.0283 837 HOH   A O   
5555 O  O   . HOH   D .   ? 0.6458 0.5688 0.5275 0.0938  0.0339  0.0829  838 HOH   A O   
5556 O  O   . HOH   D .   ? 0.3577 0.5081 0.4425 0.0319  0.0635  -0.0141 839 HOH   A O   
5557 O  O   . HOH   D .   ? 0.5787 0.6146 0.4921 0.0323  -0.0284 -0.0246 840 HOH   A O   
5558 O  O   . HOH   D .   ? 0.6353 0.5475 0.5958 0.0317  0.0085  0.0281  841 HOH   A O   
5559 O  O   . HOH   D .   ? 0.4516 0.6161 0.4673 0.0968  -0.0358 0.0118  842 HOH   A O   
5560 O  O   . HOH   D .   ? 0.5168 0.7744 0.6959 0.0047  0.0532  -0.0420 843 HOH   A O   
5561 O  O   . HOH   D .   ? 0.4389 0.4287 0.5355 -0.0724 0.0560  -0.0203 844 HOH   A O   
5562 O  O   . HOH   D .   ? 0.4936 0.7025 0.6335 0.0162  0.0363  -0.0340 845 HOH   A O   
5563 O  O   . HOH   D .   ? 0.5514 0.6124 0.4346 0.0982  0.1004  -0.0080 846 HOH   A O   
5564 O  O   . HOH   D .   ? 0.3954 0.5658 0.5178 0.0050  0.0497  -0.0238 847 HOH   A O   
5565 O  O   . HOH   D .   ? 0.4104 0.6782 0.5810 0.0028  -0.0089 -0.0681 848 HOH   A O   
5566 O  O   . HOH   D .   ? 0.3949 0.4223 0.3583 0.0355  0.0116  -0.0098 849 HOH   A O   
5567 O  O   . HOH   D .   ? 0.4577 0.5094 0.4636 0.0728  0.0359  -0.0162 850 HOH   A O   
5568 O  O   . HOH   D .   ? 0.6421 0.6762 0.5917 0.0298  0.0344  0.0294  851 HOH   A O   
5569 O  O   . HOH   D .   ? 0.5576 0.4278 0.5159 0.0086  0.0307  0.0384  852 HOH   A O   
5570 O  O   . HOH   D .   ? 0.3328 0.5810 0.4517 0.0687  -0.0143 -0.0409 853 HOH   A O   
5571 O  O   . HOH   D .   ? 0.4314 0.3303 0.3433 0.0481  0.0398  0.0744  854 HOH   A O   
5572 O  O   . HOH   D .   ? 0.3859 0.3528 0.2577 0.0849  0.0398  -0.0678 855 HOH   A O   
5573 O  O   . HOH   D .   ? 0.4429 0.5438 0.4902 0.0108  -0.0323 -0.0330 856 HOH   A O   
5574 O  O   . HOH   D .   ? 0.3373 0.6386 0.4824 0.0065  -0.0307 -0.0436 857 HOH   A O   
5575 O  O   . HOH   D .   ? 0.4284 0.5408 0.5363 -0.0671 -0.0016 -0.0349 858 HOH   A O   
5576 O  O   . HOH   D .   ? 0.6298 0.5940 0.5150 0.0480  0.1661  0.1025  859 HOH   A O   
5577 O  O   . HOH   D .   ? 0.5335 0.5515 0.3306 0.1078  0.1314  0.0753  860 HOH   A O   
5578 O  O   . HOH   D .   ? 0.3648 0.3710 0.4331 -0.0707 0.0556  0.0164  861 HOH   A O   
5579 O  O   . HOH   D .   ? 0.3580 0.3366 0.3304 -0.0102 -0.0192 -0.0288 862 HOH   A O   
5580 O  O   . HOH   D .   ? 0.3274 0.3371 0.2938 0.0163  -0.0148 -0.0536 863 HOH   A O   
5581 O  O   . HOH   D .   ? 0.3933 0.3946 0.3631 -0.0065 -0.0258 -0.0292 864 HOH   A O   
5582 O  O   . HOH   D .   ? 0.4584 0.5037 0.4823 -0.0068 -0.0282 -0.0328 865 HOH   A O   
5583 O  O   . HOH   D .   ? 0.4667 0.4453 0.4980 -0.0330 -0.0069 -0.0595 866 HOH   A O   
5584 O  O   . HOH   D .   ? 0.5730 0.7254 0.6217 0.0929  0.0074  0.0059  867 HOH   A O   
5585 O  O   . HOH   D .   ? 0.4646 0.5288 0.5619 -0.0477 0.1210  0.0169  868 HOH   A O   
5586 O  O   . HOH   D .   ? 0.5433 0.6131 0.5394 0.0896  -0.0218 0.0076  869 HOH   A O   
5587 O  O   . HOH   D .   ? 0.6128 0.5615 0.6103 -0.0431 -0.0127 -0.0582 870 HOH   A O   
5588 O  O   . HOH   D .   ? 0.5967 0.5952 0.5409 0.0095  -0.0192 -0.0245 871 HOH   A O   
5589 O  O   . HOH   D .   ? 0.5826 0.5684 0.4803 0.0464  0.0651  0.0776  872 HOH   A O   
5590 O  O   . HOH   D .   ? 0.4024 0.5903 0.4662 0.1126  -0.0139 -0.0176 873 HOH   A O   
5591 O  O   . HOH   D .   ? 0.5235 0.5009 0.4977 0.0225  0.0010  -0.0368 874 HOH   A O   
5592 O  O   . HOH   D .   ? 0.6452 0.6397 0.5117 0.1050  0.0592  -0.0600 875 HOH   A O   
5593 O  O   . HOH   D .   ? 0.3578 0.4717 0.4855 -0.0455 0.1024  -0.0031 876 HOH   A O   
5594 O  O   . HOH   D .   ? 0.4735 0.4648 0.4638 -0.0038 -0.0147 -0.0711 877 HOH   A O   
5595 O  O   . HOH   D .   ? 0.4432 0.4892 0.3942 0.0295  -0.0253 -0.0304 878 HOH   A O   
5596 O  O   . HOH   D .   ? 0.4614 0.5932 0.5044 0.0591  0.0782  -0.0111 879 HOH   A O   
5597 O  O   . HOH   D .   ? 0.3717 0.4922 0.4325 0.0107  -0.0320 -0.0380 880 HOH   A O   
5598 O  O   . HOH   D .   ? 0.4782 0.5889 0.6238 -0.0614 0.0933  -0.0139 881 HOH   A O   
5599 O  O   . HOH   D .   ? 0.3861 0.4133 0.3596 0.0366  -0.0249 0.0069  882 HOH   A O   
5600 O  O   . HOH   D .   ? 0.2886 0.5810 0.5033 -0.0246 0.0205  -0.0737 883 HOH   A O   
5601 O  O   . HOH   D .   ? 0.3441 0.3875 0.4590 -0.0693 0.0309  -0.0420 884 HOH   A O   
5602 O  O   . HOH   D .   ? 0.3884 0.6110 0.5774 -0.0563 0.1857  0.0112  885 HOH   A O   
5603 O  O   . HOH   D .   ? 0.5760 0.5174 0.4874 0.0678  0.0145  0.0614  886 HOH   A O   
5604 O  O   . HOH   D .   ? 0.4776 0.4489 0.4544 -0.0197 -0.0199 -0.0441 887 HOH   A O   
5605 O  O   . HOH   D .   ? 0.5169 0.6098 0.4613 0.0846  0.1115  -0.0010 888 HOH   A O   
5606 O  O   . HOH   D .   ? 0.4417 0.4807 0.4429 0.0863  0.0299  -0.0157 889 HOH   A O   
5607 O  O   . HOH   D .   ? 0.3726 0.5888 0.4419 0.1044  -0.0302 -0.0249 890 HOH   A O   
5608 O  O   . HOH   D .   ? 0.5457 0.5821 0.4675 0.0206  -0.0340 -0.0460 891 HOH   A O   
5609 O  O   . HOH   D .   ? 0.6457 0.5339 0.5775 0.0120  0.0745  0.0837  892 HOH   A O   
5610 O  O   . HOH   D .   ? 0.5110 0.4201 0.4522 0.0996  0.0350  -0.0254 893 HOH   A O   
5611 O  O   . HOH   D .   ? 0.2157 0.4028 0.3224 0.0099  -0.0275 -0.0532 894 HOH   A O   
5612 O  O   . HOH   D .   ? 0.5147 0.5024 0.5703 -0.0676 0.0748  0.0327  895 HOH   A O   
5613 O  O   . HOH   D .   ? 0.4981 0.4962 0.6051 -0.0787 0.0447  -0.0376 896 HOH   A O   
5614 O  O   . HOH   D .   ? 0.2096 0.2696 0.2258 0.0064  -0.0329 -0.0283 897 HOH   A O   
5615 O  O   . HOH   D .   ? 0.3443 0.3819 0.2747 0.0415  -0.0042 -0.0156 898 HOH   A O   
5616 O  O   . HOH   D .   ? 0.5108 0.5183 0.4479 0.0087  -0.0258 -0.0433 899 HOH   A O   
5617 O  O   . HOH   D .   ? 0.5167 0.5670 0.4515 0.0374  -0.0222 -0.0504 900 HOH   A O   
5618 O  O   . HOH   D .   ? 0.3624 0.4166 0.3342 0.0512  -0.0318 0.0028  901 HOH   A O   
# 
