data_9D5Z
# 
_entry.id   9D5Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9D5Z         pdb_00009d5z 10.2210/pdb9d5z/pdb 
WWPDB D_1000287325 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        9D5Z 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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                 1 
_pdbx_contact_author.email              l.halabelian@utoronto.ca 
_pdbx_contact_author.name_first         Levon 
_pdbx_contact_author.name_last          Halabelian 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4361-3619 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kimani, S.'                           1  ? 
'Dong, A.'                             2  ? 
'Hoffmann, L.'                         3  ? 
'Nemec, V.'                            4  ? 
'Ackloo, S.'                           5  ? 
'Muller-Knapp, S.'                     6  ? 
'Knapp, S.'                            7  ? 
'Arrowsmith, C.H.'                     8  ? 
'Edwards, A.M.'                        9  ? 
'Halabelian, L.'                       10 ? 
'Structural Genomics Consortium (SGC)' 11 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of the human WDR5 in complex with LH168 compound' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kimani, S.'                           1  ? 
primary 'Dong, A.'                             2  ? 
primary 'Hoffmann, L.'                         3  ? 
primary 'Nemec, V.'                            4  ? 
primary 'Ackloo, S.'                           5  ? 
primary 'Muller-Knapp, S.'                     6  ? 
primary 'Knapp, S.'                            7  ? 
primary 'Arrowsmith, C.H.'                     8  ? 
primary 'Edwards, A.M.'                        9  ? 
primary 'Halabelian, L.'                       10 ? 
primary 'Structural Genomics Consortium (SGC)' 11 ? 
# 
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 'WD repeat-containing protein 5' 34289.887 2   ? ? 'UNP residues 23-334' ? 
2 non-polymer syn 
;(3P)-N-[(2S)-1-(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)-1-oxopentan-2-yl]-3-[1-ethyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]-5-[(1H-imidazol-1-yl)methyl]benzamide
;
584.656   2   ? ? ?                     ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    5   ? ? ?                     ? 
4 water       nat water 18.015    474 ? ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BMP2-induced 3-kb gene protein' 
# 
_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       
;GTQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLL
VSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRD
GSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCI
FANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GTQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLL
VSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRD
GSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCI
FANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(3P)-N-[(2S)-1-(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)-1-oxopentan-2-yl]-3-[1-ethyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]-5-[(1H-imidazol-1-yl)methyl]benzamide
;
A1A16 
3 1,2-ETHANEDIOL EDO   
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   THR n 
1 3   GLN n 
1 4   SER n 
1 5   LYS n 
1 6   PRO n 
1 7   THR n 
1 8   PRO n 
1 9   VAL n 
1 10  LYS n 
1 11  PRO n 
1 12  ASN n 
1 13  TYR n 
1 14  ALA n 
1 15  LEU n 
1 16  LYS n 
1 17  PHE n 
1 18  THR n 
1 19  LEU n 
1 20  ALA n 
1 21  GLY n 
1 22  HIS n 
1 23  THR n 
1 24  LYS n 
1 25  ALA n 
1 26  VAL n 
1 27  SER n 
1 28  SER n 
1 29  VAL n 
1 30  LYS n 
1 31  PHE n 
1 32  SER n 
1 33  PRO n 
1 34  ASN n 
1 35  GLY n 
1 36  GLU n 
1 37  TRP n 
1 38  LEU n 
1 39  ALA n 
1 40  SER n 
1 41  SER n 
1 42  SER n 
1 43  ALA n 
1 44  ASP n 
1 45  LYS n 
1 46  LEU n 
1 47  ILE n 
1 48  LYS n 
1 49  ILE n 
1 50  TRP n 
1 51  GLY n 
1 52  ALA n 
1 53  TYR n 
1 54  ASP n 
1 55  GLY n 
1 56  LYS n 
1 57  PHE n 
1 58  GLU n 
1 59  LYS n 
1 60  THR n 
1 61  ILE n 
1 62  SER n 
1 63  GLY n 
1 64  HIS n 
1 65  LYS n 
1 66  LEU n 
1 67  GLY n 
1 68  ILE n 
1 69  SER n 
1 70  ASP n 
1 71  VAL n 
1 72  ALA n 
1 73  TRP n 
1 74  SER n 
1 75  SER n 
1 76  ASP n 
1 77  SER n 
1 78  ASN n 
1 79  LEU n 
1 80  LEU n 
1 81  VAL n 
1 82  SER n 
1 83  ALA n 
1 84  SER n 
1 85  ASP n 
1 86  ASP n 
1 87  LYS n 
1 88  THR n 
1 89  LEU n 
1 90  LYS n 
1 91  ILE n 
1 92  TRP n 
1 93  ASP n 
1 94  VAL n 
1 95  SER n 
1 96  SER n 
1 97  GLY n 
1 98  LYS n 
1 99  CYS n 
1 100 LEU n 
1 101 LYS n 
1 102 THR n 
1 103 LEU n 
1 104 LYS n 
1 105 GLY n 
1 106 HIS n 
1 107 SER n 
1 108 ASN n 
1 109 TYR n 
1 110 VAL n 
1 111 PHE n 
1 112 CYS n 
1 113 CYS n 
1 114 ASN n 
1 115 PHE n 
1 116 ASN n 
1 117 PRO n 
1 118 GLN n 
1 119 SER n 
1 120 ASN n 
1 121 LEU n 
1 122 ILE n 
1 123 VAL n 
1 124 SER n 
1 125 GLY n 
1 126 SER n 
1 127 PHE n 
1 128 ASP n 
1 129 GLU n 
1 130 SER n 
1 131 VAL n 
1 132 ARG n 
1 133 ILE n 
1 134 TRP n 
1 135 ASP n 
1 136 VAL n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 LYS n 
1 141 CYS n 
1 142 LEU n 
1 143 LYS n 
1 144 THR n 
1 145 LEU n 
1 146 PRO n 
1 147 ALA n 
1 148 HIS n 
1 149 SER n 
1 150 ASP n 
1 151 PRO n 
1 152 VAL n 
1 153 SER n 
1 154 ALA n 
1 155 VAL n 
1 156 HIS n 
1 157 PHE n 
1 158 ASN n 
1 159 ARG n 
1 160 ASP n 
1 161 GLY n 
1 162 SER n 
1 163 LEU n 
1 164 ILE n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 SER n 
1 169 TYR n 
1 170 ASP n 
1 171 GLY n 
1 172 LEU n 
1 173 CYS n 
1 174 ARG n 
1 175 ILE n 
1 176 TRP n 
1 177 ASP n 
1 178 THR n 
1 179 ALA n 
1 180 SER n 
1 181 GLY n 
1 182 GLN n 
1 183 CYS n 
1 184 LEU n 
1 185 LYS n 
1 186 THR n 
1 187 LEU n 
1 188 ILE n 
1 189 ASP n 
1 190 ASP n 
1 191 ASP n 
1 192 ASN n 
1 193 PRO n 
1 194 PRO n 
1 195 VAL n 
1 196 SER n 
1 197 PHE n 
1 198 VAL n 
1 199 LYS n 
1 200 PHE n 
1 201 SER n 
1 202 PRO n 
1 203 ASN n 
1 204 GLY n 
1 205 LYS n 
1 206 TYR n 
1 207 ILE n 
1 208 LEU n 
1 209 ALA n 
1 210 ALA n 
1 211 THR n 
1 212 LEU n 
1 213 ASP n 
1 214 ASN n 
1 215 THR n 
1 216 LEU n 
1 217 LYS n 
1 218 LEU n 
1 219 TRP n 
1 220 ASP n 
1 221 TYR n 
1 222 SER n 
1 223 LYS n 
1 224 GLY n 
1 225 LYS n 
1 226 CYS n 
1 227 LEU n 
1 228 LYS n 
1 229 THR n 
1 230 TYR n 
1 231 THR n 
1 232 GLY n 
1 233 HIS n 
1 234 LYS n 
1 235 ASN n 
1 236 GLU n 
1 237 LYS n 
1 238 TYR n 
1 239 CYS n 
1 240 ILE n 
1 241 PHE n 
1 242 ALA n 
1 243 ASN n 
1 244 PHE n 
1 245 SER n 
1 246 VAL n 
1 247 THR n 
1 248 GLY n 
1 249 GLY n 
1 250 LYS n 
1 251 TRP n 
1 252 ILE n 
1 253 VAL n 
1 254 SER n 
1 255 GLY n 
1 256 SER n 
1 257 GLU n 
1 258 ASP n 
1 259 ASN n 
1 260 LEU n 
1 261 VAL n 
1 262 TYR n 
1 263 ILE n 
1 264 TRP n 
1 265 ASN n 
1 266 LEU n 
1 267 GLN n 
1 268 THR n 
1 269 LYS n 
1 270 GLU n 
1 271 ILE n 
1 272 VAL n 
1 273 GLN n 
1 274 LYS n 
1 275 LEU n 
1 276 GLN n 
1 277 GLY n 
1 278 HIS n 
1 279 THR n 
1 280 ASP n 
1 281 VAL n 
1 282 VAL n 
1 283 ILE n 
1 284 SER n 
1 285 THR n 
1 286 ALA n 
1 287 CYS n 
1 288 HIS n 
1 289 PRO n 
1 290 THR n 
1 291 GLU n 
1 292 ASN n 
1 293 ILE n 
1 294 ILE n 
1 295 ALA n 
1 296 SER n 
1 297 ALA n 
1 298 ALA n 
1 299 LEU n 
1 300 GLU n 
1 301 ASN n 
1 302 ASP n 
1 303 LYS n 
1 304 THR n 
1 305 ILE n 
1 306 LYS n 
1 307 LEU n 
1 308 TRP n 
1 309 LYS n 
1 310 SER n 
1 311 ASP n 
1 312 CYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   312 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'WDR5, BIG3' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
A1A16 non-polymer         . 
;(3P)-N-[(2S)-1-(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)-1-oxopentan-2-yl]-3-[1-ethyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]-5-[(1H-imidazol-1-yl)methyl]benzamide
;
?                 'C29 H31 F3 N6 O2 S' 584.656 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'           62.068  
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 
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 
# 
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   GLY 1   23  ?   ?   ?   A . n 
A 1 2   THR 2   24  ?   ?   ?   A . n 
A 1 3   GLN 3   25  ?   ?   ?   A . n 
A 1 4   SER 4   26  ?   ?   ?   A . n 
A 1 5   LYS 5   27  ?   ?   ?   A . n 
A 1 6   PRO 6   28  ?   ?   ?   A . n 
A 1 7   THR 7   29  ?   ?   ?   A . n 
A 1 8   PRO 8   30  ?   ?   ?   A . n 
A 1 9   VAL 9   31  31  VAL VAL A . n 
A 1 10  LYS 10  32  32  LYS LYS A . n 
A 1 11  PRO 11  33  33  PRO PRO A . n 
A 1 12  ASN 12  34  34  ASN ASN A . n 
A 1 13  TYR 13  35  35  TYR TYR A . n 
A 1 14  ALA 14  36  36  ALA ALA A . n 
A 1 15  LEU 15  37  37  LEU LEU A . n 
A 1 16  LYS 16  38  38  LYS LYS A . n 
A 1 17  PHE 17  39  39  PHE PHE A . n 
A 1 18  THR 18  40  40  THR THR A . n 
A 1 19  LEU 19  41  41  LEU LEU A . n 
A 1 20  ALA 20  42  42  ALA ALA A . n 
A 1 21  GLY 21  43  43  GLY GLY A . n 
A 1 22  HIS 22  44  44  HIS HIS A . n 
A 1 23  THR 23  45  45  THR THR A . n 
A 1 24  LYS 24  46  46  LYS LYS A . n 
A 1 25  ALA 25  47  47  ALA ALA A . n 
A 1 26  VAL 26  48  48  VAL VAL A . n 
A 1 27  SER 27  49  49  SER SER A . n 
A 1 28  SER 28  50  50  SER SER A . n 
A 1 29  VAL 29  51  51  VAL VAL A . n 
A 1 30  LYS 30  52  52  LYS LYS A . n 
A 1 31  PHE 31  53  53  PHE PHE A . n 
A 1 32  SER 32  54  54  SER SER A . n 
A 1 33  PRO 33  55  55  PRO PRO A . n 
A 1 34  ASN 34  56  56  ASN ASN A . n 
A 1 35  GLY 35  57  57  GLY GLY A . n 
A 1 36  GLU 36  58  58  GLU GLU A . n 
A 1 37  TRP 37  59  59  TRP TRP A . n 
A 1 38  LEU 38  60  60  LEU LEU A . n 
A 1 39  ALA 39  61  61  ALA ALA A . n 
A 1 40  SER 40  62  62  SER SER A . n 
A 1 41  SER 41  63  63  SER SER A . n 
A 1 42  SER 42  64  64  SER SER A . n 
A 1 43  ALA 43  65  65  ALA ALA A . n 
A 1 44  ASP 44  66  66  ASP ASP A . n 
A 1 45  LYS 45  67  67  LYS LYS A . n 
A 1 46  LEU 46  68  68  LEU LEU A . n 
A 1 47  ILE 47  69  69  ILE ILE A . n 
A 1 48  LYS 48  70  70  LYS LYS A . n 
A 1 49  ILE 49  71  71  ILE ILE A . n 
A 1 50  TRP 50  72  72  TRP TRP A . n 
A 1 51  GLY 51  73  73  GLY GLY A . n 
A 1 52  ALA 52  74  74  ALA ALA A . n 
A 1 53  TYR 53  75  75  TYR TYR A . n 
A 1 54  ASP 54  76  76  ASP ASP A . n 
A 1 55  GLY 55  77  77  GLY GLY A . n 
A 1 56  LYS 56  78  78  LYS LYS A . n 
A 1 57  PHE 57  79  79  PHE PHE A . n 
A 1 58  GLU 58  80  80  GLU GLU A . n 
A 1 59  LYS 59  81  81  LYS LYS A . n 
A 1 60  THR 60  82  82  THR THR A . n 
A 1 61  ILE 61  83  83  ILE ILE A . n 
A 1 62  SER 62  84  84  SER SER A . n 
A 1 63  GLY 63  85  85  GLY GLY A . n 
A 1 64  HIS 64  86  86  HIS HIS A . n 
A 1 65  LYS 65  87  87  LYS LYS A . n 
A 1 66  LEU 66  88  88  LEU LEU A . n 
A 1 67  GLY 67  89  89  GLY GLY A . n 
A 1 68  ILE 68  90  90  ILE ILE A . n 
A 1 69  SER 69  91  91  SER SER A . n 
A 1 70  ASP 70  92  92  ASP ASP A . n 
A 1 71  VAL 71  93  93  VAL VAL A . n 
A 1 72  ALA 72  94  94  ALA ALA A . n 
A 1 73  TRP 73  95  95  TRP TRP A . n 
A 1 74  SER 74  96  96  SER SER A . n 
A 1 75  SER 75  97  97  SER SER A . n 
A 1 76  ASP 76  98  98  ASP ASP A . n 
A 1 77  SER 77  99  99  SER SER A . n 
A 1 78  ASN 78  100 100 ASN ASN A . n 
A 1 79  LEU 79  101 101 LEU LEU A . n 
A 1 80  LEU 80  102 102 LEU LEU A . n 
A 1 81  VAL 81  103 103 VAL VAL A . n 
A 1 82  SER 82  104 104 SER SER A . n 
A 1 83  ALA 83  105 105 ALA ALA A . n 
A 1 84  SER 84  106 106 SER SER A . n 
A 1 85  ASP 85  107 107 ASP ASP A . n 
A 1 86  ASP 86  108 108 ASP ASP A . n 
A 1 87  LYS 87  109 109 LYS LYS A . n 
A 1 88  THR 88  110 110 THR THR A . n 
A 1 89  LEU 89  111 111 LEU LEU A . n 
A 1 90  LYS 90  112 112 LYS LYS A . n 
A 1 91  ILE 91  113 113 ILE ILE A . n 
A 1 92  TRP 92  114 114 TRP TRP A . n 
A 1 93  ASP 93  115 115 ASP ASP A . n 
A 1 94  VAL 94  116 116 VAL VAL A . n 
A 1 95  SER 95  117 117 SER SER A . n 
A 1 96  SER 96  118 118 SER SER A . n 
A 1 97  GLY 97  119 119 GLY GLY A . n 
A 1 98  LYS 98  120 120 LYS LYS A . n 
A 1 99  CYS 99  121 121 CYS CYS A . n 
A 1 100 LEU 100 122 122 LEU LEU A . n 
A 1 101 LYS 101 123 123 LYS LYS A . n 
A 1 102 THR 102 124 124 THR THR A . n 
A 1 103 LEU 103 125 125 LEU LEU A . n 
A 1 104 LYS 104 126 126 LYS LYS A . n 
A 1 105 GLY 105 127 127 GLY GLY A . n 
A 1 106 HIS 106 128 128 HIS HIS A . n 
A 1 107 SER 107 129 129 SER SER A . n 
A 1 108 ASN 108 130 130 ASN ASN A . n 
A 1 109 TYR 109 131 131 TYR TYR A . n 
A 1 110 VAL 110 132 132 VAL VAL A . n 
A 1 111 PHE 111 133 133 PHE PHE A . n 
A 1 112 CYS 112 134 134 CYS CYS A . n 
A 1 113 CYS 113 135 135 CYS CYS A . n 
A 1 114 ASN 114 136 136 ASN ASN A . n 
A 1 115 PHE 115 137 137 PHE PHE A . n 
A 1 116 ASN 116 138 138 ASN ASN A . n 
A 1 117 PRO 117 139 139 PRO PRO A . n 
A 1 118 GLN 118 140 140 GLN GLN A . n 
A 1 119 SER 119 141 141 SER SER A . n 
A 1 120 ASN 120 142 142 ASN ASN A . n 
A 1 121 LEU 121 143 143 LEU LEU A . n 
A 1 122 ILE 122 144 144 ILE ILE A . n 
A 1 123 VAL 123 145 145 VAL VAL A . n 
A 1 124 SER 124 146 146 SER SER A . n 
A 1 125 GLY 125 147 147 GLY GLY A . n 
A 1 126 SER 126 148 148 SER SER A . n 
A 1 127 PHE 127 149 149 PHE PHE A . n 
A 1 128 ASP 128 150 150 ASP ASP A . n 
A 1 129 GLU 129 151 151 GLU GLU A . n 
A 1 130 SER 130 152 152 SER SER A . n 
A 1 131 VAL 131 153 153 VAL VAL A . n 
A 1 132 ARG 132 154 154 ARG ARG A . n 
A 1 133 ILE 133 155 155 ILE ILE A . n 
A 1 134 TRP 134 156 156 TRP TRP A . n 
A 1 135 ASP 135 157 157 ASP ASP A . n 
A 1 136 VAL 136 158 158 VAL VAL A . n 
A 1 137 LYS 137 159 159 LYS LYS A . n 
A 1 138 THR 138 160 160 THR THR A . n 
A 1 139 GLY 139 161 161 GLY GLY A . n 
A 1 140 LYS 140 162 162 LYS LYS A . n 
A 1 141 CYS 141 163 163 CYS CYS A . n 
A 1 142 LEU 142 164 164 LEU LEU A . n 
A 1 143 LYS 143 165 165 LYS LYS A . n 
A 1 144 THR 144 166 166 THR THR A . n 
A 1 145 LEU 145 167 167 LEU LEU A . n 
A 1 146 PRO 146 168 168 PRO PRO A . n 
A 1 147 ALA 147 169 169 ALA ALA A . n 
A 1 148 HIS 148 170 170 HIS HIS A . n 
A 1 149 SER 149 171 171 SER SER A . n 
A 1 150 ASP 150 172 172 ASP ASP A . n 
A 1 151 PRO 151 173 173 PRO PRO A . n 
A 1 152 VAL 152 174 174 VAL VAL A . n 
A 1 153 SER 153 175 175 SER SER A . n 
A 1 154 ALA 154 176 176 ALA ALA A . n 
A 1 155 VAL 155 177 177 VAL VAL A . n 
A 1 156 HIS 156 178 178 HIS HIS A . n 
A 1 157 PHE 157 179 179 PHE PHE A . n 
A 1 158 ASN 158 180 180 ASN ASN A . n 
A 1 159 ARG 159 181 181 ARG ARG A . n 
A 1 160 ASP 160 182 182 ASP ASP A . n 
A 1 161 GLY 161 183 183 GLY GLY A . n 
A 1 162 SER 162 184 184 SER SER A . n 
A 1 163 LEU 163 185 185 LEU LEU A . n 
A 1 164 ILE 164 186 186 ILE ILE A . n 
A 1 165 VAL 165 187 187 VAL VAL A . n 
A 1 166 SER 166 188 188 SER SER A . n 
A 1 167 SER 167 189 189 SER SER A . n 
A 1 168 SER 168 190 190 SER SER A . n 
A 1 169 TYR 169 191 191 TYR TYR A . n 
A 1 170 ASP 170 192 192 ASP ASP A . n 
A 1 171 GLY 171 193 193 GLY GLY A . n 
A 1 172 LEU 172 194 194 LEU LEU A . n 
A 1 173 CYS 173 195 195 CYS CYS A . n 
A 1 174 ARG 174 196 196 ARG ARG A . n 
A 1 175 ILE 175 197 197 ILE ILE A . n 
A 1 176 TRP 176 198 198 TRP TRP A . n 
A 1 177 ASP 177 199 199 ASP ASP A . n 
A 1 178 THR 178 200 200 THR THR A . n 
A 1 179 ALA 179 201 201 ALA ALA A . n 
A 1 180 SER 180 202 202 SER SER A . n 
A 1 181 GLY 181 203 203 GLY GLY A . n 
A 1 182 GLN 182 204 204 GLN GLN A . n 
A 1 183 CYS 183 205 205 CYS CYS A . n 
A 1 184 LEU 184 206 206 LEU LEU A . n 
A 1 185 LYS 185 207 207 LYS LYS A . n 
A 1 186 THR 186 208 208 THR THR A . n 
A 1 187 LEU 187 209 209 LEU LEU A . n 
A 1 188 ILE 188 210 210 ILE ILE A . n 
A 1 189 ASP 189 211 ?   ?   ?   A . n 
A 1 190 ASP 190 212 ?   ?   ?   A . n 
A 1 191 ASP 191 213 213 ASP ASP A . n 
A 1 192 ASN 192 214 214 ASN ASN A . n 
A 1 193 PRO 193 215 215 PRO PRO A . n 
A 1 194 PRO 194 216 216 PRO PRO A . n 
A 1 195 VAL 195 217 217 VAL VAL A . n 
A 1 196 SER 196 218 218 SER SER A . n 
A 1 197 PHE 197 219 219 PHE PHE A . n 
A 1 198 VAL 198 220 220 VAL VAL A . n 
A 1 199 LYS 199 221 221 LYS LYS A . n 
A 1 200 PHE 200 222 222 PHE PHE A . n 
A 1 201 SER 201 223 223 SER SER A . n 
A 1 202 PRO 202 224 224 PRO PRO A . n 
A 1 203 ASN 203 225 225 ASN ASN A . n 
A 1 204 GLY 204 226 226 GLY GLY A . n 
A 1 205 LYS 205 227 227 LYS LYS A . n 
A 1 206 TYR 206 228 228 TYR TYR A . n 
A 1 207 ILE 207 229 229 ILE ILE A . n 
A 1 208 LEU 208 230 230 LEU LEU A . n 
A 1 209 ALA 209 231 231 ALA ALA A . n 
A 1 210 ALA 210 232 232 ALA ALA A . n 
A 1 211 THR 211 233 233 THR THR A . n 
A 1 212 LEU 212 234 234 LEU LEU A . n 
A 1 213 ASP 213 235 235 ASP ASP A . n 
A 1 214 ASN 214 236 236 ASN ASN A . n 
A 1 215 THR 215 237 237 THR THR A . n 
A 1 216 LEU 216 238 238 LEU LEU A . n 
A 1 217 LYS 217 239 239 LYS LYS A . n 
A 1 218 LEU 218 240 240 LEU LEU A . n 
A 1 219 TRP 219 241 241 TRP TRP A . n 
A 1 220 ASP 220 242 242 ASP ASP A . n 
A 1 221 TYR 221 243 243 TYR TYR A . n 
A 1 222 SER 222 244 244 SER SER A . n 
A 1 223 LYS 223 245 245 LYS LYS A . n 
A 1 224 GLY 224 246 246 GLY GLY A . n 
A 1 225 LYS 225 247 247 LYS LYS A . n 
A 1 226 CYS 226 248 248 CYS CYS A . n 
A 1 227 LEU 227 249 249 LEU LEU A . n 
A 1 228 LYS 228 250 250 LYS LYS A . n 
A 1 229 THR 229 251 251 THR THR A . n 
A 1 230 TYR 230 252 252 TYR TYR A . n 
A 1 231 THR 231 253 253 THR THR A . n 
A 1 232 GLY 232 254 254 GLY GLY A . n 
A 1 233 HIS 233 255 255 HIS HIS A . n 
A 1 234 LYS 234 256 256 LYS LYS A . n 
A 1 235 ASN 235 257 257 ASN ASN A . n 
A 1 236 GLU 236 258 258 GLU GLU A . n 
A 1 237 LYS 237 259 259 LYS LYS A . n 
A 1 238 TYR 238 260 260 TYR TYR A . n 
A 1 239 CYS 239 261 261 CYS CYS A . n 
A 1 240 ILE 240 262 262 ILE ILE A . n 
A 1 241 PHE 241 263 263 PHE PHE A . n 
A 1 242 ALA 242 264 264 ALA ALA A . n 
A 1 243 ASN 243 265 265 ASN ASN A . n 
A 1 244 PHE 244 266 266 PHE PHE A . n 
A 1 245 SER 245 267 267 SER SER A . n 
A 1 246 VAL 246 268 268 VAL VAL A . n 
A 1 247 THR 247 269 269 THR THR A . n 
A 1 248 GLY 248 270 270 GLY GLY A . n 
A 1 249 GLY 249 271 271 GLY GLY A . n 
A 1 250 LYS 250 272 272 LYS LYS A . n 
A 1 251 TRP 251 273 273 TRP TRP A . n 
A 1 252 ILE 252 274 274 ILE ILE A . n 
A 1 253 VAL 253 275 275 VAL VAL A . n 
A 1 254 SER 254 276 276 SER SER A . n 
A 1 255 GLY 255 277 277 GLY GLY A . n 
A 1 256 SER 256 278 278 SER SER A . n 
A 1 257 GLU 257 279 279 GLU GLU A . n 
A 1 258 ASP 258 280 280 ASP ASP A . n 
A 1 259 ASN 259 281 281 ASN ASN A . n 
A 1 260 LEU 260 282 282 LEU LEU A . n 
A 1 261 VAL 261 283 283 VAL VAL A . n 
A 1 262 TYR 262 284 284 TYR TYR A . n 
A 1 263 ILE 263 285 285 ILE ILE A . n 
A 1 264 TRP 264 286 286 TRP TRP A . n 
A 1 265 ASN 265 287 287 ASN ASN A . n 
A 1 266 LEU 266 288 288 LEU LEU A . n 
A 1 267 GLN 267 289 289 GLN GLN A . n 
A 1 268 THR 268 290 290 THR THR A . n 
A 1 269 LYS 269 291 291 LYS LYS A . n 
A 1 270 GLU 270 292 292 GLU GLU A . n 
A 1 271 ILE 271 293 293 ILE ILE A . n 
A 1 272 VAL 272 294 294 VAL VAL A . n 
A 1 273 GLN 273 295 295 GLN GLN A . n 
A 1 274 LYS 274 296 296 LYS LYS A . n 
A 1 275 LEU 275 297 297 LEU LEU A . n 
A 1 276 GLN 276 298 298 GLN GLN A . n 
A 1 277 GLY 277 299 299 GLY GLY A . n 
A 1 278 HIS 278 300 300 HIS HIS A . n 
A 1 279 THR 279 301 301 THR THR A . n 
A 1 280 ASP 280 302 302 ASP ASP A . n 
A 1 281 VAL 281 303 303 VAL VAL A . n 
A 1 282 VAL 282 304 304 VAL VAL A . n 
A 1 283 ILE 283 305 305 ILE ILE A . n 
A 1 284 SER 284 306 306 SER SER A . n 
A 1 285 THR 285 307 307 THR THR A . n 
A 1 286 ALA 286 308 308 ALA ALA A . n 
A 1 287 CYS 287 309 309 CYS CYS A . n 
A 1 288 HIS 288 310 310 HIS HIS A . n 
A 1 289 PRO 289 311 311 PRO PRO A . n 
A 1 290 THR 290 312 312 THR THR A . n 
A 1 291 GLU 291 313 313 GLU GLU A . n 
A 1 292 ASN 292 314 314 ASN ASN A . n 
A 1 293 ILE 293 315 315 ILE ILE A . n 
A 1 294 ILE 294 316 316 ILE ILE A . n 
A 1 295 ALA 295 317 317 ALA ALA A . n 
A 1 296 SER 296 318 318 SER SER A . n 
A 1 297 ALA 297 319 319 ALA ALA A . n 
A 1 298 ALA 298 320 320 ALA ALA A . n 
A 1 299 LEU 299 321 321 LEU LEU A . n 
A 1 300 GLU 300 322 322 GLU GLU A . n 
A 1 301 ASN 301 323 323 ASN ASN A . n 
A 1 302 ASP 302 324 324 ASP ASP A . n 
A 1 303 LYS 303 325 325 LYS LYS A . n 
A 1 304 THR 304 326 326 THR THR A . n 
A 1 305 ILE 305 327 327 ILE ILE A . n 
A 1 306 LYS 306 328 328 LYS LYS A . n 
A 1 307 LEU 307 329 329 LEU LEU A . n 
A 1 308 TRP 308 330 330 TRP TRP A . n 
A 1 309 LYS 309 331 331 LYS LYS A . n 
A 1 310 SER 310 332 332 SER SER A . n 
A 1 311 ASP 311 333 333 ASP ASP A . n 
A 1 312 CYS 312 334 334 CYS CYS A . n 
B 1 1   GLY 1   23  ?   ?   ?   B . n 
B 1 2   THR 2   24  ?   ?   ?   B . n 
B 1 3   GLN 3   25  ?   ?   ?   B . n 
B 1 4   SER 4   26  ?   ?   ?   B . n 
B 1 5   LYS 5   27  ?   ?   ?   B . n 
B 1 6   PRO 6   28  ?   ?   ?   B . n 
B 1 7   THR 7   29  ?   ?   ?   B . n 
B 1 8   PRO 8   30  ?   ?   ?   B . n 
B 1 9   VAL 9   31  31  VAL VAL B . n 
B 1 10  LYS 10  32  32  LYS LYS B . n 
B 1 11  PRO 11  33  33  PRO PRO B . n 
B 1 12  ASN 12  34  34  ASN ASN B . n 
B 1 13  TYR 13  35  35  TYR TYR B . n 
B 1 14  ALA 14  36  36  ALA ALA B . n 
B 1 15  LEU 15  37  37  LEU LEU B . n 
B 1 16  LYS 16  38  38  LYS LYS B . n 
B 1 17  PHE 17  39  39  PHE PHE B . n 
B 1 18  THR 18  40  40  THR THR B . n 
B 1 19  LEU 19  41  41  LEU LEU B . n 
B 1 20  ALA 20  42  42  ALA ALA B . n 
B 1 21  GLY 21  43  43  GLY GLY B . n 
B 1 22  HIS 22  44  44  HIS HIS B . n 
B 1 23  THR 23  45  45  THR THR B . n 
B 1 24  LYS 24  46  46  LYS LYS B . n 
B 1 25  ALA 25  47  47  ALA ALA B . n 
B 1 26  VAL 26  48  48  VAL VAL B . n 
B 1 27  SER 27  49  49  SER SER B . n 
B 1 28  SER 28  50  50  SER SER B . n 
B 1 29  VAL 29  51  51  VAL VAL B . n 
B 1 30  LYS 30  52  52  LYS LYS B . n 
B 1 31  PHE 31  53  53  PHE PHE B . n 
B 1 32  SER 32  54  54  SER SER B . n 
B 1 33  PRO 33  55  55  PRO PRO B . n 
B 1 34  ASN 34  56  56  ASN ASN B . n 
B 1 35  GLY 35  57  57  GLY GLY B . n 
B 1 36  GLU 36  58  58  GLU GLU B . n 
B 1 37  TRP 37  59  59  TRP TRP B . n 
B 1 38  LEU 38  60  60  LEU LEU B . n 
B 1 39  ALA 39  61  61  ALA ALA B . n 
B 1 40  SER 40  62  62  SER SER B . n 
B 1 41  SER 41  63  63  SER SER B . n 
B 1 42  SER 42  64  64  SER SER B . n 
B 1 43  ALA 43  65  65  ALA ALA B . n 
B 1 44  ASP 44  66  66  ASP ASP B . n 
B 1 45  LYS 45  67  67  LYS LYS B . n 
B 1 46  LEU 46  68  68  LEU LEU B . n 
B 1 47  ILE 47  69  69  ILE ILE B . n 
B 1 48  LYS 48  70  70  LYS LYS B . n 
B 1 49  ILE 49  71  71  ILE ILE B . n 
B 1 50  TRP 50  72  72  TRP TRP B . n 
B 1 51  GLY 51  73  73  GLY GLY B . n 
B 1 52  ALA 52  74  74  ALA ALA B . n 
B 1 53  TYR 53  75  75  TYR TYR B . n 
B 1 54  ASP 54  76  76  ASP ASP B . n 
B 1 55  GLY 55  77  77  GLY GLY B . n 
B 1 56  LYS 56  78  78  LYS LYS B . n 
B 1 57  PHE 57  79  79  PHE PHE B . n 
B 1 58  GLU 58  80  80  GLU GLU B . n 
B 1 59  LYS 59  81  81  LYS LYS B . n 
B 1 60  THR 60  82  82  THR THR B . n 
B 1 61  ILE 61  83  83  ILE ILE B . n 
B 1 62  SER 62  84  84  SER SER B . n 
B 1 63  GLY 63  85  85  GLY GLY B . n 
B 1 64  HIS 64  86  86  HIS HIS B . n 
B 1 65  LYS 65  87  87  LYS LYS B . n 
B 1 66  LEU 66  88  88  LEU LEU B . n 
B 1 67  GLY 67  89  89  GLY GLY B . n 
B 1 68  ILE 68  90  90  ILE ILE B . n 
B 1 69  SER 69  91  91  SER SER B . n 
B 1 70  ASP 70  92  92  ASP ASP B . n 
B 1 71  VAL 71  93  93  VAL VAL B . n 
B 1 72  ALA 72  94  94  ALA ALA B . n 
B 1 73  TRP 73  95  95  TRP TRP B . n 
B 1 74  SER 74  96  96  SER SER B . n 
B 1 75  SER 75  97  97  SER SER B . n 
B 1 76  ASP 76  98  98  ASP ASP B . n 
B 1 77  SER 77  99  99  SER SER B . n 
B 1 78  ASN 78  100 100 ASN ASN B . n 
B 1 79  LEU 79  101 101 LEU LEU B . n 
B 1 80  LEU 80  102 102 LEU LEU B . n 
B 1 81  VAL 81  103 103 VAL VAL B . n 
B 1 82  SER 82  104 104 SER SER B . n 
B 1 83  ALA 83  105 105 ALA ALA B . n 
B 1 84  SER 84  106 106 SER SER B . n 
B 1 85  ASP 85  107 107 ASP ASP B . n 
B 1 86  ASP 86  108 108 ASP ASP B . n 
B 1 87  LYS 87  109 109 LYS LYS B . n 
B 1 88  THR 88  110 110 THR THR B . n 
B 1 89  LEU 89  111 111 LEU LEU B . n 
B 1 90  LYS 90  112 112 LYS LYS B . n 
B 1 91  ILE 91  113 113 ILE ILE B . n 
B 1 92  TRP 92  114 114 TRP TRP B . n 
B 1 93  ASP 93  115 115 ASP ASP B . n 
B 1 94  VAL 94  116 116 VAL VAL B . n 
B 1 95  SER 95  117 117 SER SER B . n 
B 1 96  SER 96  118 118 SER SER B . n 
B 1 97  GLY 97  119 119 GLY GLY B . n 
B 1 98  LYS 98  120 120 LYS LYS B . n 
B 1 99  CYS 99  121 121 CYS CYS B . n 
B 1 100 LEU 100 122 122 LEU LEU B . n 
B 1 101 LYS 101 123 123 LYS LYS B . n 
B 1 102 THR 102 124 124 THR THR B . n 
B 1 103 LEU 103 125 125 LEU LEU B . n 
B 1 104 LYS 104 126 126 LYS LYS B . n 
B 1 105 GLY 105 127 127 GLY GLY B . n 
B 1 106 HIS 106 128 128 HIS HIS B . n 
B 1 107 SER 107 129 129 SER SER B . n 
B 1 108 ASN 108 130 130 ASN ASN B . n 
B 1 109 TYR 109 131 131 TYR TYR B . n 
B 1 110 VAL 110 132 132 VAL VAL B . n 
B 1 111 PHE 111 133 133 PHE PHE B . n 
B 1 112 CYS 112 134 134 CYS CYS B . n 
B 1 113 CYS 113 135 135 CYS CYS B . n 
B 1 114 ASN 114 136 136 ASN ASN B . n 
B 1 115 PHE 115 137 137 PHE PHE B . n 
B 1 116 ASN 116 138 138 ASN ASN B . n 
B 1 117 PRO 117 139 139 PRO PRO B . n 
B 1 118 GLN 118 140 140 GLN GLN B . n 
B 1 119 SER 119 141 141 SER SER B . n 
B 1 120 ASN 120 142 142 ASN ASN B . n 
B 1 121 LEU 121 143 143 LEU LEU B . n 
B 1 122 ILE 122 144 144 ILE ILE B . n 
B 1 123 VAL 123 145 145 VAL VAL B . n 
B 1 124 SER 124 146 146 SER SER B . n 
B 1 125 GLY 125 147 147 GLY GLY B . n 
B 1 126 SER 126 148 148 SER SER B . n 
B 1 127 PHE 127 149 149 PHE PHE B . n 
B 1 128 ASP 128 150 150 ASP ASP B . n 
B 1 129 GLU 129 151 151 GLU GLU B . n 
B 1 130 SER 130 152 152 SER SER B . n 
B 1 131 VAL 131 153 153 VAL VAL B . n 
B 1 132 ARG 132 154 154 ARG ARG B . n 
B 1 133 ILE 133 155 155 ILE ILE B . n 
B 1 134 TRP 134 156 156 TRP TRP B . n 
B 1 135 ASP 135 157 157 ASP ASP B . n 
B 1 136 VAL 136 158 158 VAL VAL B . n 
B 1 137 LYS 137 159 159 LYS LYS B . n 
B 1 138 THR 138 160 160 THR THR B . n 
B 1 139 GLY 139 161 161 GLY GLY B . n 
B 1 140 LYS 140 162 162 LYS LYS B . n 
B 1 141 CYS 141 163 163 CYS CYS B . n 
B 1 142 LEU 142 164 164 LEU LEU B . n 
B 1 143 LYS 143 165 165 LYS LYS B . n 
B 1 144 THR 144 166 166 THR THR B . n 
B 1 145 LEU 145 167 167 LEU LEU B . n 
B 1 146 PRO 146 168 168 PRO PRO B . n 
B 1 147 ALA 147 169 169 ALA ALA B . n 
B 1 148 HIS 148 170 170 HIS HIS B . n 
B 1 149 SER 149 171 171 SER SER B . n 
B 1 150 ASP 150 172 172 ASP ASP B . n 
B 1 151 PRO 151 173 173 PRO PRO B . n 
B 1 152 VAL 152 174 174 VAL VAL B . n 
B 1 153 SER 153 175 175 SER SER B . n 
B 1 154 ALA 154 176 176 ALA ALA B . n 
B 1 155 VAL 155 177 177 VAL VAL B . n 
B 1 156 HIS 156 178 178 HIS HIS B . n 
B 1 157 PHE 157 179 179 PHE PHE B . n 
B 1 158 ASN 158 180 180 ASN ASN B . n 
B 1 159 ARG 159 181 181 ARG ARG B . n 
B 1 160 ASP 160 182 182 ASP ASP B . n 
B 1 161 GLY 161 183 183 GLY GLY B . n 
B 1 162 SER 162 184 184 SER SER B . n 
B 1 163 LEU 163 185 185 LEU LEU B . n 
B 1 164 ILE 164 186 186 ILE ILE B . n 
B 1 165 VAL 165 187 187 VAL VAL B . n 
B 1 166 SER 166 188 188 SER SER B . n 
B 1 167 SER 167 189 189 SER SER B . n 
B 1 168 SER 168 190 190 SER SER B . n 
B 1 169 TYR 169 191 191 TYR TYR B . n 
B 1 170 ASP 170 192 192 ASP ASP B . n 
B 1 171 GLY 171 193 193 GLY GLY B . n 
B 1 172 LEU 172 194 194 LEU LEU B . n 
B 1 173 CYS 173 195 195 CYS CYS B . n 
B 1 174 ARG 174 196 196 ARG ARG B . n 
B 1 175 ILE 175 197 197 ILE ILE B . n 
B 1 176 TRP 176 198 198 TRP TRP B . n 
B 1 177 ASP 177 199 199 ASP ASP B . n 
B 1 178 THR 178 200 200 THR THR B . n 
B 1 179 ALA 179 201 201 ALA ALA B . n 
B 1 180 SER 180 202 202 SER SER B . n 
B 1 181 GLY 181 203 203 GLY GLY B . n 
B 1 182 GLN 182 204 204 GLN GLN B . n 
B 1 183 CYS 183 205 205 CYS CYS B . n 
B 1 184 LEU 184 206 206 LEU LEU B . n 
B 1 185 LYS 185 207 207 LYS LYS B . n 
B 1 186 THR 186 208 208 THR THR B . n 
B 1 187 LEU 187 209 209 LEU LEU B . n 
B 1 188 ILE 188 210 210 ILE ILE B . n 
B 1 189 ASP 189 211 ?   ?   ?   B . n 
B 1 190 ASP 190 212 ?   ?   ?   B . n 
B 1 191 ASP 191 213 213 ASP ASP B . n 
B 1 192 ASN 192 214 214 ASN ASN B . n 
B 1 193 PRO 193 215 215 PRO PRO B . n 
B 1 194 PRO 194 216 216 PRO PRO B . n 
B 1 195 VAL 195 217 217 VAL VAL B . n 
B 1 196 SER 196 218 218 SER SER B . n 
B 1 197 PHE 197 219 219 PHE PHE B . n 
B 1 198 VAL 198 220 220 VAL VAL B . n 
B 1 199 LYS 199 221 221 LYS LYS B . n 
B 1 200 PHE 200 222 222 PHE PHE B . n 
B 1 201 SER 201 223 223 SER SER B . n 
B 1 202 PRO 202 224 224 PRO PRO B . n 
B 1 203 ASN 203 225 225 ASN ASN B . n 
B 1 204 GLY 204 226 226 GLY GLY B . n 
B 1 205 LYS 205 227 227 LYS LYS B . n 
B 1 206 TYR 206 228 228 TYR TYR B . n 
B 1 207 ILE 207 229 229 ILE ILE B . n 
B 1 208 LEU 208 230 230 LEU LEU B . n 
B 1 209 ALA 209 231 231 ALA ALA B . n 
B 1 210 ALA 210 232 232 ALA ALA B . n 
B 1 211 THR 211 233 233 THR THR B . n 
B 1 212 LEU 212 234 234 LEU LEU B . n 
B 1 213 ASP 213 235 235 ASP ASP B . n 
B 1 214 ASN 214 236 236 ASN ASN B . n 
B 1 215 THR 215 237 237 THR THR B . n 
B 1 216 LEU 216 238 238 LEU LEU B . n 
B 1 217 LYS 217 239 239 LYS LYS B . n 
B 1 218 LEU 218 240 240 LEU LEU B . n 
B 1 219 TRP 219 241 241 TRP TRP B . n 
B 1 220 ASP 220 242 242 ASP ASP B . n 
B 1 221 TYR 221 243 243 TYR TYR B . n 
B 1 222 SER 222 244 244 SER SER B . n 
B 1 223 LYS 223 245 245 LYS LYS B . n 
B 1 224 GLY 224 246 246 GLY GLY B . n 
B 1 225 LYS 225 247 247 LYS LYS B . n 
B 1 226 CYS 226 248 248 CYS CYS B . n 
B 1 227 LEU 227 249 249 LEU LEU B . n 
B 1 228 LYS 228 250 250 LYS LYS B . n 
B 1 229 THR 229 251 251 THR THR B . n 
B 1 230 TYR 230 252 252 TYR TYR B . n 
B 1 231 THR 231 253 253 THR THR B . n 
B 1 232 GLY 232 254 254 GLY GLY B . n 
B 1 233 HIS 233 255 255 HIS HIS B . n 
B 1 234 LYS 234 256 256 LYS LYS B . n 
B 1 235 ASN 235 257 257 ASN ASN B . n 
B 1 236 GLU 236 258 258 GLU GLU B . n 
B 1 237 LYS 237 259 259 LYS LYS B . n 
B 1 238 TYR 238 260 260 TYR TYR B . n 
B 1 239 CYS 239 261 261 CYS CYS B . n 
B 1 240 ILE 240 262 262 ILE ILE B . n 
B 1 241 PHE 241 263 263 PHE PHE B . n 
B 1 242 ALA 242 264 264 ALA ALA B . n 
B 1 243 ASN 243 265 265 ASN ASN B . n 
B 1 244 PHE 244 266 266 PHE PHE B . n 
B 1 245 SER 245 267 267 SER SER B . n 
B 1 246 VAL 246 268 268 VAL VAL B . n 
B 1 247 THR 247 269 269 THR THR B . n 
B 1 248 GLY 248 270 270 GLY GLY B . n 
B 1 249 GLY 249 271 271 GLY GLY B . n 
B 1 250 LYS 250 272 272 LYS LYS B . n 
B 1 251 TRP 251 273 273 TRP TRP B . n 
B 1 252 ILE 252 274 274 ILE ILE B . n 
B 1 253 VAL 253 275 275 VAL VAL B . n 
B 1 254 SER 254 276 276 SER SER B . n 
B 1 255 GLY 255 277 277 GLY GLY B . n 
B 1 256 SER 256 278 278 SER SER B . n 
B 1 257 GLU 257 279 279 GLU GLU B . n 
B 1 258 ASP 258 280 280 ASP ASP B . n 
B 1 259 ASN 259 281 281 ASN ASN B . n 
B 1 260 LEU 260 282 282 LEU LEU B . n 
B 1 261 VAL 261 283 283 VAL VAL B . n 
B 1 262 TYR 262 284 284 TYR TYR B . n 
B 1 263 ILE 263 285 285 ILE ILE B . n 
B 1 264 TRP 264 286 286 TRP TRP B . n 
B 1 265 ASN 265 287 287 ASN ASN B . n 
B 1 266 LEU 266 288 288 LEU LEU B . n 
B 1 267 GLN 267 289 289 GLN GLN B . n 
B 1 268 THR 268 290 290 THR THR B . n 
B 1 269 LYS 269 291 291 LYS LYS B . n 
B 1 270 GLU 270 292 292 GLU GLU B . n 
B 1 271 ILE 271 293 293 ILE ILE B . n 
B 1 272 VAL 272 294 294 VAL VAL B . n 
B 1 273 GLN 273 295 295 GLN GLN B . n 
B 1 274 LYS 274 296 296 LYS LYS B . n 
B 1 275 LEU 275 297 297 LEU LEU B . n 
B 1 276 GLN 276 298 298 GLN GLN B . n 
B 1 277 GLY 277 299 299 GLY GLY B . n 
B 1 278 HIS 278 300 300 HIS HIS B . n 
B 1 279 THR 279 301 301 THR THR B . n 
B 1 280 ASP 280 302 302 ASP ASP B . n 
B 1 281 VAL 281 303 303 VAL VAL B . n 
B 1 282 VAL 282 304 304 VAL VAL B . n 
B 1 283 ILE 283 305 305 ILE ILE B . n 
B 1 284 SER 284 306 306 SER SER B . n 
B 1 285 THR 285 307 307 THR THR B . n 
B 1 286 ALA 286 308 308 ALA ALA B . n 
B 1 287 CYS 287 309 309 CYS CYS B . n 
B 1 288 HIS 288 310 310 HIS HIS B . n 
B 1 289 PRO 289 311 311 PRO PRO B . n 
B 1 290 THR 290 312 312 THR THR B . n 
B 1 291 GLU 291 313 313 GLU GLU B . n 
B 1 292 ASN 292 314 314 ASN ASN B . n 
B 1 293 ILE 293 315 315 ILE ILE B . n 
B 1 294 ILE 294 316 316 ILE ILE B . n 
B 1 295 ALA 295 317 317 ALA ALA B . n 
B 1 296 SER 296 318 318 SER SER B . n 
B 1 297 ALA 297 319 319 ALA ALA B . n 
B 1 298 ALA 298 320 320 ALA ALA B . n 
B 1 299 LEU 299 321 321 LEU LEU B . n 
B 1 300 GLU 300 322 322 GLU GLU B . n 
B 1 301 ASN 301 323 323 ASN ASN B . n 
B 1 302 ASP 302 324 324 ASP ASP B . n 
B 1 303 LYS 303 325 325 LYS LYS B . n 
B 1 304 THR 304 326 326 THR THR B . n 
B 1 305 ILE 305 327 327 ILE ILE B . n 
B 1 306 LYS 306 328 328 LYS LYS B . n 
B 1 307 LEU 307 329 329 LEU LEU B . n 
B 1 308 TRP 308 330 330 TRP TRP B . n 
B 1 309 LYS 309 331 331 LYS LYS B . n 
B 1 310 SER 310 332 332 SER SER B . n 
B 1 311 ASP 311 333 333 ASP ASP B . n 
B 1 312 CYS 312 334 334 CYS CYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A16 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A16 
_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 
C 2 A1A16 1   401 401 A1A16 LIG A . 
D 3 EDO   1   402 402 EDO   EDO A . 
E 3 EDO   1   403 403 EDO   EDO A . 
F 2 A1A16 1   401 401 A1A16 LIG B . 
G 3 EDO   1   402 402 EDO   EDO B . 
H 3 EDO   1   403 403 EDO   EDO B . 
I 3 EDO   1   404 404 EDO   EDO B . 
J 4 HOH   1   501 353 HOH   HOH A . 
J 4 HOH   2   502 284 HOH   HOH A . 
J 4 HOH   3   503 364 HOH   HOH A . 
J 4 HOH   4   504 374 HOH   HOH A . 
J 4 HOH   5   505 55  HOH   HOH A . 
J 4 HOH   6   506 444 HOH   HOH A . 
J 4 HOH   7   507 10  HOH   HOH A . 
J 4 HOH   8   508 198 HOH   HOH A . 
J 4 HOH   9   509 495 HOH   HOH A . 
J 4 HOH   10  510 449 HOH   HOH A . 
J 4 HOH   11  511 381 HOH   HOH A . 
J 4 HOH   12  512 92  HOH   HOH A . 
J 4 HOH   13  513 177 HOH   HOH A . 
J 4 HOH   14  514 462 HOH   HOH A . 
J 4 HOH   15  515 413 HOH   HOH A . 
J 4 HOH   16  516 328 HOH   HOH A . 
J 4 HOH   17  517 471 HOH   HOH A . 
J 4 HOH   18  518 325 HOH   HOH A . 
J 4 HOH   19  519 125 HOH   HOH A . 
J 4 HOH   20  520 105 HOH   HOH A . 
J 4 HOH   21  521 65  HOH   HOH A . 
J 4 HOH   22  522 47  HOH   HOH A . 
J 4 HOH   23  523 396 HOH   HOH A . 
J 4 HOH   24  524 221 HOH   HOH A . 
J 4 HOH   25  525 6   HOH   HOH A . 
J 4 HOH   26  526 408 HOH   HOH A . 
J 4 HOH   27  527 184 HOH   HOH A . 
J 4 HOH   28  528 195 HOH   HOH A . 
J 4 HOH   29  529 58  HOH   HOH A . 
J 4 HOH   30  530 188 HOH   HOH A . 
J 4 HOH   31  531 185 HOH   HOH A . 
J 4 HOH   32  532 135 HOH   HOH A . 
J 4 HOH   33  533 93  HOH   HOH A . 
J 4 HOH   34  534 104 HOH   HOH A . 
J 4 HOH   35  535 151 HOH   HOH A . 
J 4 HOH   36  536 136 HOH   HOH A . 
J 4 HOH   37  537 169 HOH   HOH A . 
J 4 HOH   38  538 83  HOH   HOH A . 
J 4 HOH   39  539 258 HOH   HOH A . 
J 4 HOH   40  540 2   HOH   HOH A . 
J 4 HOH   41  541 127 HOH   HOH A . 
J 4 HOH   42  542 214 HOH   HOH A . 
J 4 HOH   43  543 360 HOH   HOH A . 
J 4 HOH   44  544 378 HOH   HOH A . 
J 4 HOH   45  545 39  HOH   HOH A . 
J 4 HOH   46  546 9   HOH   HOH A . 
J 4 HOH   47  547 179 HOH   HOH A . 
J 4 HOH   48  548 161 HOH   HOH A . 
J 4 HOH   49  549 112 HOH   HOH A . 
J 4 HOH   50  550 79  HOH   HOH A . 
J 4 HOH   51  551 203 HOH   HOH A . 
J 4 HOH   52  552 326 HOH   HOH A . 
J 4 HOH   53  553 108 HOH   HOH A . 
J 4 HOH   54  554 131 HOH   HOH A . 
J 4 HOH   55  555 226 HOH   HOH A . 
J 4 HOH   56  556 292 HOH   HOH A . 
J 4 HOH   57  557 121 HOH   HOH A . 
J 4 HOH   58  558 29  HOH   HOH A . 
J 4 HOH   59  559 273 HOH   HOH A . 
J 4 HOH   60  560 140 HOH   HOH A . 
J 4 HOH   61  561 229 HOH   HOH A . 
J 4 HOH   62  562 111 HOH   HOH A . 
J 4 HOH   63  563 254 HOH   HOH A . 
J 4 HOH   64  564 98  HOH   HOH A . 
J 4 HOH   65  565 12  HOH   HOH A . 
J 4 HOH   66  566 156 HOH   HOH A . 
J 4 HOH   67  567 4   HOH   HOH A . 
J 4 HOH   68  568 137 HOH   HOH A . 
J 4 HOH   69  569 397 HOH   HOH A . 
J 4 HOH   70  570 441 HOH   HOH A . 
J 4 HOH   71  571 146 HOH   HOH A . 
J 4 HOH   72  572 69  HOH   HOH A . 
J 4 HOH   73  573 358 HOH   HOH A . 
J 4 HOH   74  574 395 HOH   HOH A . 
J 4 HOH   75  575 85  HOH   HOH A . 
J 4 HOH   76  576 387 HOH   HOH A . 
J 4 HOH   77  577 48  HOH   HOH A . 
J 4 HOH   78  578 459 HOH   HOH A . 
J 4 HOH   79  579 193 HOH   HOH A . 
J 4 HOH   80  580 213 HOH   HOH A . 
J 4 HOH   81  581 468 HOH   HOH A . 
J 4 HOH   82  582 464 HOH   HOH A . 
J 4 HOH   83  583 100 HOH   HOH A . 
J 4 HOH   84  584 61  HOH   HOH A . 
J 4 HOH   85  585 425 HOH   HOH A . 
J 4 HOH   86  586 28  HOH   HOH A . 
J 4 HOH   87  587 165 HOH   HOH A . 
J 4 HOH   88  588 22  HOH   HOH A . 
J 4 HOH   89  589 384 HOH   HOH A . 
J 4 HOH   90  590 113 HOH   HOH A . 
J 4 HOH   91  591 250 HOH   HOH A . 
J 4 HOH   92  592 175 HOH   HOH A . 
J 4 HOH   93  593 54  HOH   HOH A . 
J 4 HOH   94  594 376 HOH   HOH A . 
J 4 HOH   95  595 350 HOH   HOH A . 
J 4 HOH   96  596 386 HOH   HOH A . 
J 4 HOH   97  597 126 HOH   HOH A . 
J 4 HOH   98  598 327 HOH   HOH A . 
J 4 HOH   99  599 110 HOH   HOH A . 
J 4 HOH   100 600 472 HOH   HOH A . 
J 4 HOH   101 601 355 HOH   HOH A . 
J 4 HOH   102 602 178 HOH   HOH A . 
J 4 HOH   103 603 201 HOH   HOH A . 
J 4 HOH   104 604 189 HOH   HOH A . 
J 4 HOH   105 605 162 HOH   HOH A . 
J 4 HOH   106 606 439 HOH   HOH A . 
J 4 HOH   107 607 324 HOH   HOH A . 
J 4 HOH   108 608 248 HOH   HOH A . 
J 4 HOH   109 609 231 HOH   HOH A . 
J 4 HOH   110 610 26  HOH   HOH A . 
J 4 HOH   111 611 103 HOH   HOH A . 
J 4 HOH   112 612 246 HOH   HOH A . 
J 4 HOH   113 613 377 HOH   HOH A . 
J 4 HOH   114 614 35  HOH   HOH A . 
J 4 HOH   115 615 56  HOH   HOH A . 
J 4 HOH   116 616 145 HOH   HOH A . 
J 4 HOH   117 617 34  HOH   HOH A . 
J 4 HOH   118 618 247 HOH   HOH A . 
J 4 HOH   119 619 50  HOH   HOH A . 
J 4 HOH   120 620 73  HOH   HOH A . 
J 4 HOH   121 621 86  HOH   HOH A . 
J 4 HOH   122 622 432 HOH   HOH A . 
J 4 HOH   123 623 11  HOH   HOH A . 
J 4 HOH   124 624 279 HOH   HOH A . 
J 4 HOH   125 625 31  HOH   HOH A . 
J 4 HOH   126 626 470 HOH   HOH A . 
J 4 HOH   127 627 465 HOH   HOH A . 
J 4 HOH   128 628 74  HOH   HOH A . 
J 4 HOH   129 629 466 HOH   HOH A . 
J 4 HOH   130 630 223 HOH   HOH A . 
J 4 HOH   131 631 211 HOH   HOH A . 
J 4 HOH   132 632 133 HOH   HOH A . 
J 4 HOH   133 633 365 HOH   HOH A . 
J 4 HOH   134 634 157 HOH   HOH A . 
J 4 HOH   135 635 1   HOH   HOH A . 
J 4 HOH   136 636 215 HOH   HOH A . 
J 4 HOH   137 637 150 HOH   HOH A . 
J 4 HOH   138 638 57  HOH   HOH A . 
J 4 HOH   139 639 496 HOH   HOH A . 
J 4 HOH   140 640 23  HOH   HOH A . 
J 4 HOH   141 641 16  HOH   HOH A . 
J 4 HOH   142 642 399 HOH   HOH A . 
J 4 HOH   143 643 19  HOH   HOH A . 
J 4 HOH   144 644 90  HOH   HOH A . 
J 4 HOH   145 645 43  HOH   HOH A . 
J 4 HOH   146 646 400 HOH   HOH A . 
J 4 HOH   147 647 301 HOH   HOH A . 
J 4 HOH   148 648 336 HOH   HOH A . 
J 4 HOH   149 649 346 HOH   HOH A . 
J 4 HOH   150 650 18  HOH   HOH A . 
J 4 HOH   151 651 66  HOH   HOH A . 
J 4 HOH   152 652 20  HOH   HOH A . 
J 4 HOH   153 653 14  HOH   HOH A . 
J 4 HOH   154 654 45  HOH   HOH A . 
J 4 HOH   155 655 280 HOH   HOH A . 
J 4 HOH   156 656 139 HOH   HOH A . 
J 4 HOH   157 657 356 HOH   HOH A . 
J 4 HOH   158 658 366 HOH   HOH A . 
J 4 HOH   159 659 268 HOH   HOH A . 
J 4 HOH   160 660 371 HOH   HOH A . 
J 4 HOH   161 661 75  HOH   HOH A . 
J 4 HOH   162 662 158 HOH   HOH A . 
J 4 HOH   163 663 269 HOH   HOH A . 
J 4 HOH   164 664 390 HOH   HOH A . 
J 4 HOH   165 665 82  HOH   HOH A . 
J 4 HOH   166 666 114 HOH   HOH A . 
J 4 HOH   167 667 36  HOH   HOH A . 
J 4 HOH   168 668 67  HOH   HOH A . 
J 4 HOH   169 669 264 HOH   HOH A . 
J 4 HOH   170 670 317 HOH   HOH A . 
J 4 HOH   171 671 59  HOH   HOH A . 
J 4 HOH   172 672 294 HOH   HOH A . 
J 4 HOH   173 673 455 HOH   HOH A . 
J 4 HOH   174 674 331 HOH   HOH A . 
J 4 HOH   175 675 38  HOH   HOH A . 
J 4 HOH   176 676 329 HOH   HOH A . 
J 4 HOH   177 677 33  HOH   HOH A . 
J 4 HOH   178 678 216 HOH   HOH A . 
J 4 HOH   179 679 467 HOH   HOH A . 
J 4 HOH   180 680 230 HOH   HOH A . 
J 4 HOH   181 681 375 HOH   HOH A . 
J 4 HOH   182 682 316 HOH   HOH A . 
J 4 HOH   183 683 141 HOH   HOH A . 
J 4 HOH   184 684 224 HOH   HOH A . 
J 4 HOH   185 685 37  HOH   HOH A . 
J 4 HOH   186 686 392 HOH   HOH A . 
J 4 HOH   187 687 174 HOH   HOH A . 
J 4 HOH   188 688 306 HOH   HOH A . 
J 4 HOH   189 689 372 HOH   HOH A . 
J 4 HOH   190 690 282 HOH   HOH A . 
J 4 HOH   191 691 342 HOH   HOH A . 
J 4 HOH   192 692 97  HOH   HOH A . 
J 4 HOH   193 693 276 HOH   HOH A . 
J 4 HOH   194 694 344 HOH   HOH A . 
J 4 HOH   195 695 349 HOH   HOH A . 
J 4 HOH   196 696 450 HOH   HOH A . 
J 4 HOH   197 697 149 HOH   HOH A . 
J 4 HOH   198 698 153 HOH   HOH A . 
J 4 HOH   199 699 461 HOH   HOH A . 
J 4 HOH   200 700 296 HOH   HOH A . 
J 4 HOH   201 701 442 HOH   HOH A . 
J 4 HOH   202 702 409 HOH   HOH A . 
J 4 HOH   203 703 266 HOH   HOH A . 
J 4 HOH   204 704 438 HOH   HOH A . 
J 4 HOH   205 705 265 HOH   HOH A . 
J 4 HOH   206 706 312 HOH   HOH A . 
J 4 HOH   207 707 458 HOH   HOH A . 
J 4 HOH   208 708 259 HOH   HOH A . 
J 4 HOH   209 709 117 HOH   HOH A . 
J 4 HOH   210 710 236 HOH   HOH A . 
J 4 HOH   211 711 469 HOH   HOH A . 
J 4 HOH   212 712 148 HOH   HOH A . 
J 4 HOH   213 713 435 HOH   HOH A . 
J 4 HOH   214 714 402 HOH   HOH A . 
J 4 HOH   215 715 299 HOH   HOH A . 
J 4 HOH   216 716 403 HOH   HOH A . 
J 4 HOH   217 717 77  HOH   HOH A . 
J 4 HOH   218 718 452 HOH   HOH A . 
J 4 HOH   219 719 89  HOH   HOH A . 
J 4 HOH   220 720 42  HOH   HOH A . 
J 4 HOH   221 721 460 HOH   HOH A . 
J 4 HOH   222 722 204 HOH   HOH A . 
J 4 HOH   223 723 393 HOH   HOH A . 
J 4 HOH   224 724 68  HOH   HOH A . 
J 4 HOH   225 725 451 HOH   HOH A . 
J 4 HOH   226 726 222 HOH   HOH A . 
J 4 HOH   227 727 241 HOH   HOH A . 
J 4 HOH   228 728 430 HOH   HOH A . 
J 4 HOH   229 729 132 HOH   HOH A . 
J 4 HOH   230 730 420 HOH   HOH A . 
J 4 HOH   231 731 456 HOH   HOH A . 
J 4 HOH   232 732 428 HOH   HOH A . 
J 4 HOH   233 733 305 HOH   HOH A . 
J 4 HOH   234 734 289 HOH   HOH A . 
J 4 HOH   235 735 489 HOH   HOH A . 
J 4 HOH   236 736 238 HOH   HOH A . 
J 4 HOH   237 737 426 HOH   HOH A . 
J 4 HOH   238 738 423 HOH   HOH A . 
J 4 HOH   239 739 251 HOH   HOH A . 
J 4 HOH   240 740 283 HOH   HOH A . 
J 4 HOH   241 741 443 HOH   HOH A . 
J 4 HOH   242 742 433 HOH   HOH A . 
J 4 HOH   243 743 431 HOH   HOH A . 
J 4 HOH   244 744 419 HOH   HOH A . 
J 4 HOH   245 745 418 HOH   HOH A . 
J 4 HOH   246 746 257 HOH   HOH A . 
J 4 HOH   247 747 267 HOH   HOH A . 
J 4 HOH   248 748 197 HOH   HOH A . 
J 4 HOH   249 749 427 HOH   HOH A . 
J 4 HOH   250 750 277 HOH   HOH A . 
J 4 HOH   251 751 304 HOH   HOH A . 
J 4 HOH   252 752 302 HOH   HOH A . 
J 4 HOH   253 753 434 HOH   HOH A . 
J 4 HOH   254 754 463 HOH   HOH A . 
J 4 HOH   255 755 288 HOH   HOH A . 
J 4 HOH   256 756 244 HOH   HOH A . 
J 4 HOH   257 757 343 HOH   HOH A . 
J 4 HOH   258 758 457 HOH   HOH A . 
J 4 HOH   259 759 440 HOH   HOH A . 
J 4 HOH   260 760 424 HOH   HOH A . 
J 4 HOH   261 761 290 HOH   HOH A . 
J 4 HOH   262 762 308 HOH   HOH A . 
J 4 HOH   263 763 181 HOH   HOH A . 
J 4 HOH   264 764 446 HOH   HOH A . 
J 4 HOH   265 765 315 HOH   HOH A . 
J 4 HOH   266 766 116 HOH   HOH A . 
J 4 HOH   267 767 445 HOH   HOH A . 
J 4 HOH   268 768 485 HOH   HOH A . 
K 4 HOH   1   501 199 HOH   HOH B . 
K 4 HOH   2   502 295 HOH   HOH B . 
K 4 HOH   3   503 437 HOH   HOH B . 
K 4 HOH   4   504 7   HOH   HOH B . 
K 4 HOH   5   505 486 HOH   HOH B . 
K 4 HOH   6   506 362 HOH   HOH B . 
K 4 HOH   7   507 115 HOH   HOH B . 
K 4 HOH   8   508 345 HOH   HOH B . 
K 4 HOH   9   509 478 HOH   HOH B . 
K 4 HOH   10  510 318 HOH   HOH B . 
K 4 HOH   11  511 274 HOH   HOH B . 
K 4 HOH   12  512 357 HOH   HOH B . 
K 4 HOH   13  513 109 HOH   HOH B . 
K 4 HOH   14  514 71  HOH   HOH B . 
K 4 HOH   15  515 21  HOH   HOH B . 
K 4 HOH   16  516 411 HOH   HOH B . 
K 4 HOH   17  517 398 HOH   HOH B . 
K 4 HOH   18  518 191 HOH   HOH B . 
K 4 HOH   19  519 172 HOH   HOH B . 
K 4 HOH   20  520 202 HOH   HOH B . 
K 4 HOH   21  521 491 HOH   HOH B . 
K 4 HOH   22  522 130 HOH   HOH B . 
K 4 HOH   23  523 475 HOH   HOH B . 
K 4 HOH   24  524 119 HOH   HOH B . 
K 4 HOH   25  525 8   HOH   HOH B . 
K 4 HOH   26  526 5   HOH   HOH B . 
K 4 HOH   27  527 483 HOH   HOH B . 
K 4 HOH   28  528 298 HOH   HOH B . 
K 4 HOH   29  529 271 HOH   HOH B . 
K 4 HOH   30  530 207 HOH   HOH B . 
K 4 HOH   31  531 81  HOH   HOH B . 
K 4 HOH   32  532 218 HOH   HOH B . 
K 4 HOH   33  533 415 HOH   HOH B . 
K 4 HOH   34  534 24  HOH   HOH B . 
K 4 HOH   35  535 256 HOH   HOH B . 
K 4 HOH   36  536 389 HOH   HOH B . 
K 4 HOH   37  537 180 HOH   HOH B . 
K 4 HOH   38  538 334 HOH   HOH B . 
K 4 HOH   39  539 160 HOH   HOH B . 
K 4 HOH   40  540 106 HOH   HOH B . 
K 4 HOH   41  541 155 HOH   HOH B . 
K 4 HOH   42  542 319 HOH   HOH B . 
K 4 HOH   43  543 453 HOH   HOH B . 
K 4 HOH   44  544 41  HOH   HOH B . 
K 4 HOH   45  545 102 HOH   HOH B . 
K 4 HOH   46  546 253 HOH   HOH B . 
K 4 HOH   47  547 196 HOH   HOH B . 
K 4 HOH   48  548 60  HOH   HOH B . 
K 4 HOH   49  549 414 HOH   HOH B . 
K 4 HOH   50  550 382 HOH   HOH B . 
K 4 HOH   51  551 187 HOH   HOH B . 
K 4 HOH   52  552 293 HOH   HOH B . 
K 4 HOH   53  553 94  HOH   HOH B . 
K 4 HOH   54  554 78  HOH   HOH B . 
K 4 HOH   55  555 118 HOH   HOH B . 
K 4 HOH   56  556 80  HOH   HOH B . 
K 4 HOH   57  557 101 HOH   HOH B . 
K 4 HOH   58  558 186 HOH   HOH B . 
K 4 HOH   59  559 194 HOH   HOH B . 
K 4 HOH   60  560 341 HOH   HOH B . 
K 4 HOH   61  561 49  HOH   HOH B . 
K 4 HOH   62  562 164 HOH   HOH B . 
K 4 HOH   63  563 170 HOH   HOH B . 
K 4 HOH   64  564 128 HOH   HOH B . 
K 4 HOH   65  565 200 HOH   HOH B . 
K 4 HOH   66  566 167 HOH   HOH B . 
K 4 HOH   67  567 330 HOH   HOH B . 
K 4 HOH   68  568 252 HOH   HOH B . 
K 4 HOH   69  569 480 HOH   HOH B . 
K 4 HOH   70  570 219 HOH   HOH B . 
K 4 HOH   71  571 338 HOH   HOH B . 
K 4 HOH   72  572 210 HOH   HOH B . 
K 4 HOH   73  573 321 HOH   HOH B . 
K 4 HOH   74  574 163 HOH   HOH B . 
K 4 HOH   75  575 144 HOH   HOH B . 
K 4 HOH   76  576 17  HOH   HOH B . 
K 4 HOH   77  577 129 HOH   HOH B . 
K 4 HOH   78  578 260 HOH   HOH B . 
K 4 HOH   79  579 190 HOH   HOH B . 
K 4 HOH   80  580 51  HOH   HOH B . 
K 4 HOH   81  581 183 HOH   HOH B . 
K 4 HOH   82  582 96  HOH   HOH B . 
K 4 HOH   83  583 87  HOH   HOH B . 
K 4 HOH   84  584 152 HOH   HOH B . 
K 4 HOH   85  585 235 HOH   HOH B . 
K 4 HOH   86  586 76  HOH   HOH B . 
K 4 HOH   87  587 333 HOH   HOH B . 
K 4 HOH   88  588 84  HOH   HOH B . 
K 4 HOH   89  589 270 HOH   HOH B . 
K 4 HOH   90  590 122 HOH   HOH B . 
K 4 HOH   91  591 347 HOH   HOH B . 
K 4 HOH   92  592 320 HOH   HOH B . 
K 4 HOH   93  593 123 HOH   HOH B . 
K 4 HOH   94  594 159 HOH   HOH B . 
K 4 HOH   95  595 15  HOH   HOH B . 
K 4 HOH   96  596 335 HOH   HOH B . 
K 4 HOH   97  597 348 HOH   HOH B . 
K 4 HOH   98  598 25  HOH   HOH B . 
K 4 HOH   99  599 30  HOH   HOH B . 
K 4 HOH   100 600 91  HOH   HOH B . 
K 4 HOH   101 601 154 HOH   HOH B . 
K 4 HOH   102 602 3   HOH   HOH B . 
K 4 HOH   103 603 46  HOH   HOH B . 
K 4 HOH   104 604 143 HOH   HOH B . 
K 4 HOH   105 605 352 HOH   HOH B . 
K 4 HOH   106 606 243 HOH   HOH B . 
K 4 HOH   107 607 407 HOH   HOH B . 
K 4 HOH   108 608 209 HOH   HOH B . 
K 4 HOH   109 609 134 HOH   HOH B . 
K 4 HOH   110 610 173 HOH   HOH B . 
K 4 HOH   111 611 410 HOH   HOH B . 
K 4 HOH   112 612 272 HOH   HOH B . 
K 4 HOH   113 613 220 HOH   HOH B . 
K 4 HOH   114 614 373 HOH   HOH B . 
K 4 HOH   115 615 138 HOH   HOH B . 
K 4 HOH   116 616 72  HOH   HOH B . 
K 4 HOH   117 617 206 HOH   HOH B . 
K 4 HOH   118 618 354 HOH   HOH B . 
K 4 HOH   119 619 332 HOH   HOH B . 
K 4 HOH   120 620 369 HOH   HOH B . 
K 4 HOH   121 621 263 HOH   HOH B . 
K 4 HOH   122 622 487 HOH   HOH B . 
K 4 HOH   123 623 205 HOH   HOH B . 
K 4 HOH   124 624 52  HOH   HOH B . 
K 4 HOH   125 625 212 HOH   HOH B . 
K 4 HOH   126 626 53  HOH   HOH B . 
K 4 HOH   127 627 227 HOH   HOH B . 
K 4 HOH   128 628 124 HOH   HOH B . 
K 4 HOH   129 629 239 HOH   HOH B . 
K 4 HOH   130 630 44  HOH   HOH B . 
K 4 HOH   131 631 240 HOH   HOH B . 
K 4 HOH   132 632 368 HOH   HOH B . 
K 4 HOH   133 633 490 HOH   HOH B . 
K 4 HOH   134 634 261 HOH   HOH B . 
K 4 HOH   135 635 13  HOH   HOH B . 
K 4 HOH   136 636 168 HOH   HOH B . 
K 4 HOH   137 637 228 HOH   HOH B . 
K 4 HOH   138 638 323 HOH   HOH B . 
K 4 HOH   139 639 40  HOH   HOH B . 
K 4 HOH   140 640 166 HOH   HOH B . 
K 4 HOH   141 641 351 HOH   HOH B . 
K 4 HOH   142 642 394 HOH   HOH B . 
K 4 HOH   143 643 488 HOH   HOH B . 
K 4 HOH   144 644 70  HOH   HOH B . 
K 4 HOH   145 645 473 HOH   HOH B . 
K 4 HOH   146 646 32  HOH   HOH B . 
K 4 HOH   147 647 370 HOH   HOH B . 
K 4 HOH   148 648 448 HOH   HOH B . 
K 4 HOH   149 649 171 HOH   HOH B . 
K 4 HOH   150 650 64  HOH   HOH B . 
K 4 HOH   151 651 311 HOH   HOH B . 
K 4 HOH   152 652 379 HOH   HOH B . 
K 4 HOH   153 653 383 HOH   HOH B . 
K 4 HOH   154 654 401 HOH   HOH B . 
K 4 HOH   155 655 481 HOH   HOH B . 
K 4 HOH   156 656 107 HOH   HOH B . 
K 4 HOH   157 657 242 HOH   HOH B . 
K 4 HOH   158 658 62  HOH   HOH B . 
K 4 HOH   159 659 176 HOH   HOH B . 
K 4 HOH   160 660 63  HOH   HOH B . 
K 4 HOH   161 661 406 HOH   HOH B . 
K 4 HOH   162 662 340 HOH   HOH B . 
K 4 HOH   163 663 27  HOH   HOH B . 
K 4 HOH   164 664 245 HOH   HOH B . 
K 4 HOH   165 665 182 HOH   HOH B . 
K 4 HOH   166 666 232 HOH   HOH B . 
K 4 HOH   167 667 363 HOH   HOH B . 
K 4 HOH   168 668 416 HOH   HOH B . 
K 4 HOH   169 669 367 HOH   HOH B . 
K 4 HOH   170 670 476 HOH   HOH B . 
K 4 HOH   171 671 285 HOH   HOH B . 
K 4 HOH   172 672 497 HOH   HOH B . 
K 4 HOH   173 673 249 HOH   HOH B . 
K 4 HOH   174 674 492 HOH   HOH B . 
K 4 HOH   175 675 300 HOH   HOH B . 
K 4 HOH   176 676 493 HOH   HOH B . 
K 4 HOH   177 677 412 HOH   HOH B . 
K 4 HOH   178 678 310 HOH   HOH B . 
K 4 HOH   179 679 447 HOH   HOH B . 
K 4 HOH   180 680 234 HOH   HOH B . 
K 4 HOH   181 681 339 HOH   HOH B . 
K 4 HOH   182 682 95  HOH   HOH B . 
K 4 HOH   183 683 99  HOH   HOH B . 
K 4 HOH   184 684 429 HOH   HOH B . 
K 4 HOH   185 685 142 HOH   HOH B . 
K 4 HOH   186 686 314 HOH   HOH B . 
K 4 HOH   187 687 286 HOH   HOH B . 
K 4 HOH   188 688 88  HOH   HOH B . 
K 4 HOH   189 689 454 HOH   HOH B . 
K 4 HOH   190 690 361 HOH   HOH B . 
K 4 HOH   191 691 421 HOH   HOH B . 
K 4 HOH   192 692 477 HOH   HOH B . 
K 4 HOH   193 693 482 HOH   HOH B . 
K 4 HOH   194 694 494 HOH   HOH B . 
K 4 HOH   195 695 225 HOH   HOH B . 
K 4 HOH   196 696 359 HOH   HOH B . 
K 4 HOH   197 697 474 HOH   HOH B . 
K 4 HOH   198 698 287 HOH   HOH B . 
K 4 HOH   199 699 388 HOH   HOH B . 
K 4 HOH   200 700 484 HOH   HOH B . 
K 4 HOH   201 701 422 HOH   HOH B . 
K 4 HOH   202 702 208 HOH   HOH B . 
K 4 HOH   203 703 275 HOH   HOH B . 
K 4 HOH   204 704 479 HOH   HOH B . 
K 4 HOH   205 705 303 HOH   HOH B . 
K 4 HOH   206 706 385 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 32  ? NZ  ? A LYS 10  NZ  
2  1 Y 1 A LYS 78  ? NZ  ? A LYS 56  NZ  
3  1 Y 1 A LYS 87  ? CE  ? A LYS 65  CE  
4  1 Y 1 A LYS 87  ? NZ  ? A LYS 65  NZ  
5  1 Y 1 A LYS 120 ? NZ  ? A LYS 98  NZ  
6  1 Y 1 A LYS 126 ? NZ  ? A LYS 104 NZ  
7  1 Y 1 A LYS 159 ? CD  ? A LYS 137 CD  
8  1 Y 1 A LYS 159 ? CE  ? A LYS 137 CE  
9  1 Y 1 A LYS 159 ? NZ  ? A LYS 137 NZ  
10 1 Y 1 A LYS 162 ? CD  ? A LYS 140 CD  
11 1 Y 1 A LYS 162 ? CE  ? A LYS 140 CE  
12 1 Y 1 A LYS 162 ? NZ  ? A LYS 140 NZ  
13 1 Y 1 A LYS 207 ? CE  ? A LYS 185 CE  
14 1 Y 1 A LYS 207 ? NZ  ? A LYS 185 NZ  
15 1 Y 1 A ILE 210 ? CG1 ? A ILE 188 CG1 
16 1 Y 1 A ILE 210 ? CG2 ? A ILE 188 CG2 
17 1 Y 1 A ILE 210 ? CD1 ? A ILE 188 CD1 
18 1 Y 1 A LYS 227 ? CD  ? A LYS 205 CD  
19 1 Y 1 A LYS 227 ? CE  ? A LYS 205 CE  
20 1 Y 1 A LYS 227 ? NZ  ? A LYS 205 NZ  
21 1 Y 1 A SER 244 ? OG  ? A SER 222 OG  
22 1 Y 1 A LYS 245 ? CE  ? A LYS 223 CE  
23 1 Y 1 A LYS 245 ? NZ  ? A LYS 223 NZ  
24 1 Y 1 A LYS 247 ? CG  ? A LYS 225 CG  
25 1 Y 1 A LYS 247 ? CD  ? A LYS 225 CD  
26 1 Y 1 A LYS 247 ? CE  ? A LYS 225 CE  
27 1 Y 1 A LYS 247 ? NZ  ? A LYS 225 NZ  
28 1 Y 1 B VAL 31  ? CG1 ? B VAL 9   CG1 
29 1 Y 1 B VAL 31  ? CG2 ? B VAL 9   CG2 
30 1 Y 1 B LYS 32  ? CD  ? B LYS 10  CD  
31 1 Y 1 B LYS 32  ? CE  ? B LYS 10  CE  
32 1 Y 1 B LYS 32  ? NZ  ? B LYS 10  NZ  
33 1 Y 1 B LYS 78  ? CG  ? B LYS 56  CG  
34 1 Y 1 B LYS 78  ? CD  ? B LYS 56  CD  
35 1 Y 1 B LYS 78  ? CE  ? B LYS 56  CE  
36 1 Y 1 B LYS 78  ? NZ  ? B LYS 56  NZ  
37 1 Y 1 B LYS 87  ? CE  ? B LYS 65  CE  
38 1 Y 1 B LYS 87  ? NZ  ? B LYS 65  NZ  
39 1 Y 1 B LYS 120 ? CG  ? B LYS 98  CG  
40 1 Y 1 B LYS 120 ? CD  ? B LYS 98  CD  
41 1 Y 1 B LYS 120 ? CE  ? B LYS 98  CE  
42 1 Y 1 B LYS 120 ? NZ  ? B LYS 98  NZ  
43 1 Y 1 B LYS 159 ? CD  ? B LYS 137 CD  
44 1 Y 1 B LYS 159 ? CE  ? B LYS 137 CE  
45 1 Y 1 B LYS 159 ? NZ  ? B LYS 137 NZ  
46 1 Y 1 B LYS 162 ? CG  ? B LYS 140 CG  
47 1 Y 1 B LYS 162 ? CD  ? B LYS 140 CD  
48 1 Y 1 B LYS 162 ? CE  ? B LYS 140 CE  
49 1 Y 1 B LYS 162 ? NZ  ? B LYS 140 NZ  
50 1 Y 1 B LYS 207 ? CD  ? B LYS 185 CD  
51 1 Y 1 B LYS 207 ? CE  ? B LYS 185 CE  
52 1 Y 1 B LYS 207 ? NZ  ? B LYS 185 NZ  
53 1 Y 1 B ILE 210 ? CG1 ? B ILE 188 CG1 
54 1 Y 1 B ILE 210 ? CG2 ? B ILE 188 CG2 
55 1 Y 1 B ILE 210 ? CD1 ? B ILE 188 CD1 
56 1 Y 1 B LYS 227 ? CD  ? B LYS 205 CD  
57 1 Y 1 B LYS 227 ? CE  ? B LYS 205 CE  
58 1 Y 1 B LYS 227 ? NZ  ? B LYS 205 NZ  
59 1 Y 1 B LYS 239 ? CE  ? B LYS 217 CE  
60 1 Y 1 B LYS 239 ? NZ  ? B LYS 217 NZ  
61 1 Y 1 B SER 244 ? OG  ? B SER 222 OG  
62 1 Y 1 B LYS 245 ? CG  ? B LYS 223 CG  
63 1 Y 1 B LYS 245 ? CD  ? B LYS 223 CD  
64 1 Y 1 B LYS 245 ? CE  ? B LYS 223 CE  
65 1 Y 1 B LYS 245 ? NZ  ? B LYS 223 NZ  
66 1 Y 1 B LYS 247 ? CG  ? B LYS 225 CG  
67 1 Y 1 B LYS 247 ? CD  ? B LYS 225 CD  
68 1 Y 1 B LYS 247 ? CE  ? B LYS 225 CE  
69 1 Y 1 B LYS 247 ? NZ  ? B LYS 225 NZ  
70 1 Y 1 B GLU 292 ? CG  ? B GLU 270 CG  
71 1 Y 1 B GLU 292 ? CD  ? B GLU 270 CD  
72 1 Y 1 B GLU 292 ? OE1 ? B GLU 270 OE1 
73 1 Y 1 B GLU 292 ? OE2 ? B GLU 270 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement     ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0425 1 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        2 
? phasing        ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        3 
# 
_cell.angle_alpha                  110.41 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.22 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  112.20 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D5Z 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.951 
_cell.length_a_esd                 ? 
_cell.length_b                     61.185 
_cell.length_b_esd                 ? 
_cell.length_c                     64.605 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9D5Z 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9D5Z 
_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             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.79 
_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              ? 
_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    '20% PEG3350, 0.2 M Ammonium formate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-25 
_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   1.18049 
_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                        'CLSI BEAMLINE 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.18049 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D5Z 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               50.00 
_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                                     63599 
_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                           94.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.225 
_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                                0.055 
_reflns.pdbx_Rpim_I_all                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       218124 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.046 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
_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 
1.70 1.73  ? ? ? ? ? ? 2681 ? ? ? ? ? ? ? ? ? ? ? 3.2 0.700 ? ? 0.376 0.200 ? 1  1 0.936 0.983 ? 80.6 ? 0.316 ? ? ? ? ? ? ? ? ? 
1.73 1.76  ? ? ? ? ? ? 2898 ? ? ? ? ? ? ? ? ? ? ? 3.2 0.713 ? ? 0.336 0.182 ? 2  1 0.950 0.987 ? 85.0 ? 0.280 ? ? ? ? ? ? ? ? ? 
1.76 1.79  ? ? ? ? ? ? 3089 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.715 ? ? 0.289 0.154 ? 3  1 0.965 0.991 ? 90.3 ? 0.243 ? ? ? ? ? ? ? ? ? 
1.79 1.83  ? ? ? ? ? ? 3057 ? ? ? ? ? ? ? ? ? ? ? 3.5 0.721 ? ? 0.279 0.147 ? 4  1 0.973 0.993 ? 92.9 ? 0.236 ? ? ? ? ? ? ? ? ? 
1.83 1.87  ? ? ? ? ? ? 3217 ? ? ? ? ? ? ? ? ? ? ? 3.5 0.721 ? ? 0.232 0.122 ? 5  1 0.979 0.995 ? 93.7 ? 0.196 ? ? ? ? ? ? ? ? ? 
1.87 1.91  ? ? ? ? ? ? 3172 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.722 ? ? 0.185 0.099 ? 6  1 0.986 0.997 ? 94.0 ? 0.155 ? ? ? ? ? ? ? ? ? 
1.91 1.96  ? ? ? ? ? ? 3182 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.740 ? ? 0.159 0.085 ? 7  1 0.988 0.997 ? 94.1 ? 0.133 ? ? ? ? ? ? ? ? ? 
1.96 2.02  ? ? ? ? ? ? 3198 ? ? ? ? ? ? ? ? ? ? ? 3.5 0.739 ? ? 0.137 0.071 ? 8  1 0.992 0.998 ? 95.0 ? 0.116 ? ? ? ? ? ? ? ? ? 
2.02 2.07  ? ? ? ? ? ? 3179 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.785 ? ? 0.124 0.066 ? 9  1 0.992 0.998 ? 94.4 ? 0.104 ? ? ? ? ? ? ? ? ? 
2.07 2.14  ? ? ? ? ? ? 3221 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.830 ? ? 0.111 0.060 ? 10 1 0.993 0.998 ? 94.3 ? 0.093 ? ? ? ? ? ? ? ? ? 
2.14 2.22  ? ? ? ? ? ? 3185 ? ? ? ? ? ? ? ? ? ? ? 3.6 0.738 ? ? 0.093 0.048 ? 11 1 0.995 0.999 ? 94.9 ? 0.079 ? ? ? ? ? ? ? ? ? 
2.22 2.31  ? ? ? ? ? ? 3252 ? ? ? ? ? ? ? ? ? ? ? 3.6 0.769 ? ? 0.090 0.047 ? 12 1 0.995 0.999 ? 95.7 ? 0.076 ? ? ? ? ? ? ? ? ? 
2.31 2.41  ? ? ? ? ? ? 3216 ? ? ? ? ? ? ? ? ? ? ? 3.3 1.166 ? ? 0.080 0.044 ? 13 1 0.994 0.998 ? 96.3 ? 0.066 ? ? ? ? ? ? ? ? ? 
2.41 2.54  ? ? ? ? ? ? 3287 ? ? ? ? ? ? ? ? ? ? ? 3.6 0.969 ? ? 0.067 0.035 ? 14 1 0.996 0.999 ? 96.5 ? 0.057 ? ? ? ? ? ? ? ? ? 
2.54 2.70  ? ? ? ? ? ? 3264 ? ? ? ? ? ? ? ? ? ? ? 3.4 1.294 ? ? 0.057 0.031 ? 15 1 0.996 0.999 ? 96.8 ? 0.048 ? ? ? ? ? ? ? ? ? 
2.70 2.91  ? ? ? ? ? ? 3292 ? ? ? ? ? ? ? ? ? ? ? 3.6 1.288 ? ? 0.047 0.025 ? 16 1 0.997 0.999 ? 96.8 ? 0.040 ? ? ? ? ? ? ? ? ? 
2.91 3.20  ? ? ? ? ? ? 3274 ? ? ? ? ? ? ? ? ? ? ? 3.5 0.994 ? ? 0.041 0.022 ? 17 1 0.998 0.999 ? 97.3 ? 0.035 ? ? ? ? ? ? ? ? ? 
3.20 3.66  ? ? ? ? ? ? 3298 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.758 ? ? 0.033 0.017 ? 18 1 0.998 1.000 ? 97.5 ? 0.028 ? ? ? ? ? ? ? ? ? 
3.66 4.61  ? ? ? ? ? ? 3306 ? ? ? ? ? ? ? ? ? ? ? 3.5 2.544 ? ? 0.031 0.016 ? 19 1 0.997 0.999 ? 97.8 ? 0.026 ? ? ? ? ? ? ? ? ? 
4.61 50.00 ? ? ? ? ? ? 3331 ? ? ? ? ? ? ? ? ? ? ? 3.5 6.029 ? ? 0.036 0.020 ? 20 1 0.996 0.999 ? 98.5 ? 0.031 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.06 
_refine.aniso_B[1][2]                            -0.25 
_refine.aniso_B[1][3]                            -0.91 
_refine.aniso_B[2][2]                            1.88 
_refine.aniso_B[2][3]                            0.31 
_refine.aniso_B[3][3]                            -1.67 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.816 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.973 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9D5Z 
_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                            1.70 
_refine.ls_d_res_low                             42.89 
_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                     62385 
_refine.ls_number_reflns_R_free                  1212 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.93 
_refine.ls_percent_reflns_R_free                 1.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14033 
_refine.ls_R_factor_R_free                       0.18872 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.13940 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.145 
_refine.pdbx_overall_ESU_R_Free                  0.096 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             4.530 
_refine.overall_SU_ML                            0.065 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        42.89 
_refine_hist.number_atoms_solvent             474 
_refine_hist.number_atoms_total               5185 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4711 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  0.012  4919  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4499  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.305  1.776  6702  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.475  1.769  10404 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.353  5.000  622   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.241  5.000  8     ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.541 10.000 761   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.065  0.200  747   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  5878  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1084  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.280  2.420  2461  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.272  2.420  2461  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.527  4.340  3086  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.527  4.341  3087  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.589  2.596  2458  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.589  2.598  2459  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.921  4.696  3615  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 12.649 25.57  5356  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 11.381 23.13  5233  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 2.240  3.000  9418  ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.70 
_refine_ls_shell.d_res_low                        1.743 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             85 
_refine_ls_shell.number_reflns_R_work             3885 
_refine_ls_shell.percent_reflns_obs               79.16 
_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                  0.203 
_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                  0.240 
# 
_struct.entry_id                     9D5Z 
_struct.title                        'Crystal structure of the human WDR5 in complex with LH168 compound' 
_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        9D5Z 
_struct_keywords.text            'WD-repeat, WDR, WDR5, SGC, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    WDR5_HUMAN 
_struct_ref.pdbx_db_accession          P61964 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLLV
SASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDG
SLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIF
ANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC
;
_struct_ref.pdbx_align_begin           24 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9D5Z A 2 ? 312 ? P61964 24 ? 334 ? 24 334 
2 1 9D5Z B 2 ? 312 ? P61964 24 ? 334 ? 24 334 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9D5Z GLY A 1 ? UNP P61964 ? ? 'expression tag' 23 1 
2 9D5Z GLY B 1 ? UNP P61964 ? ? 'expression tag' 23 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,J   
2 1 B,F,G,H,I,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? 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 ALA A 14  ? LEU A 19  ? ALA A 36  LEU A 41  
AA1 2 ILE A 305 ? LYS A 309 ? ILE A 327 LYS A 331 
AA1 3 ILE A 293 ? ALA A 298 ? ILE A 315 ALA A 320 
AA1 4 VAL A 282 ? CYS A 287 ? VAL A 304 CYS A 309 
AA2 1 VAL A 26  ? PHE A 31  ? VAL A 48  PHE A 53  
AA2 2 TRP A 37  ? SER A 42  ? TRP A 59  SER A 64  
AA2 3 LEU A 46  ? GLY A 51  ? LEU A 68  GLY A 73  
AA2 4 PHE A 57  ? SER A 62  ? PHE A 79  SER A 84  
AA3 1 ILE A 68  ? TRP A 73  ? ILE A 90  TRP A 95  
AA3 2 LEU A 79  ? SER A 84  ? LEU A 101 SER A 106 
AA3 3 THR A 88  ? ASP A 93  ? THR A 110 ASP A 115 
AA3 4 CYS A 99  ? LYS A 104 ? CYS A 121 LYS A 126 
AA4 1 VAL A 110 ? PHE A 115 ? VAL A 132 PHE A 137 
AA4 2 LEU A 121 ? SER A 126 ? LEU A 143 SER A 148 
AA4 3 VAL A 131 ? ASP A 135 ? VAL A 153 ASP A 157 
AA4 4 CYS A 141 ? LEU A 145 ? CYS A 163 LEU A 167 
AA5 1 VAL A 152 ? PHE A 157 ? VAL A 174 PHE A 179 
AA5 2 LEU A 163 ? SER A 168 ? LEU A 185 SER A 190 
AA5 3 CYS A 173 ? ASP A 177 ? CYS A 195 ASP A 199 
AA5 4 CYS A 183 ? LEU A 187 ? CYS A 205 LEU A 209 
AA6 1 VAL A 195 ? PHE A 200 ? VAL A 217 PHE A 222 
AA6 2 TYR A 206 ? THR A 211 ? TYR A 228 THR A 233 
AA6 3 THR A 215 ? ASP A 220 ? THR A 237 ASP A 242 
AA6 4 LYS A 225 ? TYR A 230 ? LYS A 247 TYR A 252 
AA7 1 ALA A 242 ? SER A 245 ? ALA A 264 SER A 267 
AA7 2 TRP A 251 ? SER A 254 ? TRP A 273 SER A 276 
AA7 3 VAL A 261 ? ASN A 265 ? VAL A 283 ASN A 287 
AA7 4 ILE A 271 ? LEU A 275 ? ILE A 293 LEU A 297 
AA8 1 ALA B 14  ? LEU B 19  ? ALA B 36  LEU B 41  
AA8 2 ILE B 305 ? LYS B 309 ? ILE B 327 LYS B 331 
AA8 3 ILE B 293 ? ALA B 298 ? ILE B 315 ALA B 320 
AA8 4 VAL B 282 ? CYS B 287 ? VAL B 304 CYS B 309 
AA9 1 VAL B 26  ? PHE B 31  ? VAL B 48  PHE B 53  
AA9 2 TRP B 37  ? SER B 42  ? TRP B 59  SER B 64  
AA9 3 ILE B 47  ? GLY B 51  ? ILE B 69  GLY B 73  
AA9 4 PHE B 57  ? ILE B 61  ? PHE B 79  ILE B 83  
AB1 1 ILE B 68  ? TRP B 73  ? ILE B 90  TRP B 95  
AB1 2 LEU B 79  ? SER B 84  ? LEU B 101 SER B 106 
AB1 3 THR B 88  ? ASP B 93  ? THR B 110 ASP B 115 
AB1 4 CYS B 99  ? LYS B 104 ? CYS B 121 LYS B 126 
AB2 1 VAL B 110 ? PHE B 115 ? VAL B 132 PHE B 137 
AB2 2 LEU B 121 ? SER B 126 ? LEU B 143 SER B 148 
AB2 3 VAL B 131 ? ASP B 135 ? VAL B 153 ASP B 157 
AB2 4 CYS B 141 ? LEU B 145 ? CYS B 163 LEU B 167 
AB3 1 VAL B 152 ? PHE B 157 ? VAL B 174 PHE B 179 
AB3 2 LEU B 163 ? SER B 168 ? LEU B 185 SER B 190 
AB3 3 CYS B 173 ? ASP B 177 ? CYS B 195 ASP B 199 
AB3 4 CYS B 183 ? LEU B 187 ? CYS B 205 LEU B 209 
AB4 1 VAL B 195 ? PHE B 200 ? VAL B 217 PHE B 222 
AB4 2 TYR B 206 ? THR B 211 ? TYR B 228 THR B 233 
AB4 3 THR B 215 ? ASP B 220 ? THR B 237 ASP B 242 
AB4 4 LYS B 225 ? TYR B 230 ? LYS B 247 TYR B 252 
AB5 1 ALA B 242 ? SER B 245 ? ALA B 264 SER B 267 
AB5 2 TRP B 251 ? SER B 254 ? TRP B 273 SER B 276 
AB5 3 VAL B 261 ? ASN B 265 ? VAL B 283 ASN B 287 
AB5 4 ILE B 271 ? LEU B 275 ? ILE B 293 LEU B 297 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 19  ? N LEU A 41  O ILE A 305 ? O ILE A 327 
AA1 2 3 O TRP A 308 ? O TRP A 330 N ILE A 294 ? N ILE A 316 
AA1 3 4 O ALA A 295 ? O ALA A 317 N ALA A 286 ? N ALA A 308 
AA2 1 2 N LYS A 30  ? N LYS A 52  O ALA A 39  ? O ALA A 61  
AA2 2 3 N SER A 40  ? N SER A 62  O LYS A 48  ? O LYS A 70  
AA2 3 4 N ILE A 49  ? N ILE A 71  O GLU A 58  ? O GLU A 80  
AA3 1 2 N ALA A 72  ? N ALA A 94  O VAL A 81  ? O VAL A 103 
AA3 2 3 N LEU A 80  ? N LEU A 102 O TRP A 92  ? O TRP A 114 
AA3 3 4 N LEU A 89  ? N LEU A 111 O LEU A 103 ? O LEU A 125 
AA4 1 2 N ASN A 114 ? N ASN A 136 O VAL A 123 ? O VAL A 145 
AA4 2 3 N ILE A 122 ? N ILE A 144 O TRP A 134 ? O TRP A 156 
AA4 3 4 N VAL A 131 ? N VAL A 153 O LEU A 145 ? O LEU A 167 
AA5 1 2 N HIS A 156 ? N HIS A 178 O VAL A 165 ? O VAL A 187 
AA5 2 3 N ILE A 164 ? N ILE A 186 O TRP A 176 ? O TRP A 198 
AA5 3 4 N ILE A 175 ? N ILE A 197 O LEU A 184 ? O LEU A 206 
AA6 1 2 N LYS A 199 ? N LYS A 221 O LEU A 208 ? O LEU A 230 
AA6 2 3 N ILE A 207 ? N ILE A 229 O TRP A 219 ? O TRP A 241 
AA6 3 4 N LEU A 218 ? N LEU A 240 O LEU A 227 ? O LEU A 249 
AA7 1 2 N SER A 245 ? N SER A 267 O TRP A 251 ? O TRP A 273 
AA7 2 3 N SER A 254 ? N SER A 276 O TYR A 262 ? O TYR A 284 
AA7 3 4 N ILE A 263 ? N ILE A 285 O VAL A 272 ? O VAL A 294 
AA8 1 2 N LEU B 19  ? N LEU B 41  O ILE B 305 ? O ILE B 327 
AA8 2 3 O TRP B 308 ? O TRP B 330 N ILE B 294 ? N ILE B 316 
AA8 3 4 O ALA B 295 ? O ALA B 317 N ALA B 286 ? N ALA B 308 
AA9 1 2 N LYS B 30  ? N LYS B 52  O ALA B 39  ? O ALA B 61  
AA9 2 3 N SER B 40  ? N SER B 62  O LYS B 48  ? O LYS B 70  
AA9 3 4 N ILE B 47  ? N ILE B 69  O ILE B 61  ? O ILE B 83  
AB1 1 2 N SER B 69  ? N SER B 91  O ALA B 83  ? O ALA B 105 
AB1 2 3 N LEU B 80  ? N LEU B 102 O TRP B 92  ? O TRP B 114 
AB1 3 4 N LEU B 89  ? N LEU B 111 O LEU B 103 ? O LEU B 125 
AB2 1 2 N ASN B 114 ? N ASN B 136 O VAL B 123 ? O VAL B 145 
AB2 2 3 N ILE B 122 ? N ILE B 144 O TRP B 134 ? O TRP B 156 
AB2 3 4 N VAL B 131 ? N VAL B 153 O LEU B 145 ? O LEU B 167 
AB3 1 2 N HIS B 156 ? N HIS B 178 O VAL B 165 ? O VAL B 187 
AB3 2 3 N ILE B 164 ? N ILE B 186 O TRP B 176 ? O TRP B 198 
AB3 3 4 N ILE B 175 ? N ILE B 197 O LEU B 184 ? O LEU B 206 
AB4 1 2 N LYS B 199 ? N LYS B 221 O LEU B 208 ? O LEU B 230 
AB4 2 3 N ILE B 207 ? N ILE B 229 O TRP B 219 ? O TRP B 241 
AB4 3 4 N LEU B 218 ? N LEU B 240 O LEU B 227 ? O LEU B 249 
AB5 1 2 N ASN B 243 ? N ASN B 265 O VAL B 253 ? O VAL B 275 
AB5 2 3 N SER B 254 ? N SER B 276 O TYR B 262 ? O TYR B 284 
AB5 3 4 N VAL B 261 ? N VAL B 283 O LEU B 275 ? O LEU B 297 
# 
_pdbx_entry_details.entry_id                   9D5Z 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 B HOH 503 ? ? O B HOH 676 ? ? 2.02 
2 1 O A HOH 594 ? ? O A HOH 629 ? ? 2.14 
# 
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 67  ? ? 81.46   8.75   
2  1 LYS A 109 ? ? 82.04   8.35   
3  1 GLU A 151 ? ? 82.03   8.14   
4  1 LEU A 234 ? ? -83.10  35.74  
5  1 ASN A 257 ? ? -156.99 89.05  
6  1 ASN A 257 ? ? -156.99 88.95  
7  1 LYS A 259 ? ? -134.09 -47.58 
8  1 ASN A 281 ? ? 80.59   17.38  
9  1 LYS A 291 ? ? 81.12   5.01   
10 1 ASP A 324 ? ? -125.03 -65.54 
11 1 LYS B 67  ? ? 81.51   7.01   
12 1 GLU B 80  ? ? -101.77 -60.34 
13 1 LYS B 109 ? ? 83.38   8.50   
14 1 GLU B 151 ? ? 85.57   3.54   
15 1 LEU B 234 ? ? -83.58  40.34  
16 1 ASP B 324 ? ? -130.10 -68.71 
# 
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 GLY 23  ? A GLY 1   
2  1 Y 1 A THR 24  ? A THR 2   
3  1 Y 1 A GLN 25  ? A GLN 3   
4  1 Y 1 A SER 26  ? A SER 4   
5  1 Y 1 A LYS 27  ? A LYS 5   
6  1 Y 1 A PRO 28  ? A PRO 6   
7  1 Y 1 A THR 29  ? A THR 7   
8  1 Y 1 A PRO 30  ? A PRO 8   
9  1 Y 1 A ASP 211 ? A ASP 189 
10 1 Y 1 A ASP 212 ? A ASP 190 
11 1 Y 1 B GLY 23  ? B GLY 1   
12 1 Y 1 B THR 24  ? B THR 2   
13 1 Y 1 B GLN 25  ? B GLN 3   
14 1 Y 1 B SER 26  ? B SER 4   
15 1 Y 1 B LYS 27  ? B LYS 5   
16 1 Y 1 B PRO 28  ? B PRO 6   
17 1 Y 1 B THR 29  ? B THR 7   
18 1 Y 1 B PRO 30  ? B PRO 8   
19 1 Y 1 B ASP 211 ? B ASP 189 
20 1 Y 1 B ASP 212 ? B ASP 190 
# 
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 
A1A16 C4   C N S 1   
A1A16 C5   C N N 2   
A1A16 C7   C N N 3   
A1A16 C8   C N N 4   
A1A16 C10  C Y N 5   
A1A16 C13  C Y N 6   
A1A16 C17  C N N 7   
A1A16 C20  C Y N 8   
A1A16 C21  C Y N 9   
A1A16 C22  C Y N 10  
A1A16 C24  C N N 11  
A1A16 C28  C N N 12  
A1A16 C1   C N N 13  
A1A16 C2   C N N 14  
A1A16 C3   C N N 15  
A1A16 N6   N N N 16  
A1A16 C9   C N N 17  
A1A16 C11  C Y N 18  
A1A16 S12  S Y N 19  
A1A16 C14  C Y N 20  
A1A16 O15  O N N 21  
A1A16 N16  N N N 22  
A1A16 C18  C Y N 23  
A1A16 C19  C Y N 24  
A1A16 N23  N Y N 25  
A1A16 C25  C N N 26  
A1A16 N26  N Y N 27  
A1A16 C27  C Y N 28  
A1A16 F29  F N N 29  
A1A16 F30  F N N 30  
A1A16 F31  F N N 31  
A1A16 C32  C Y N 32  
A1A16 C33  C Y N 33  
A1A16 C34  C N N 34  
A1A16 N35  N Y N 35  
A1A16 C36  C Y N 36  
A1A16 N37  N Y N 37  
A1A16 C38  C Y N 38  
A1A16 C39  C Y N 39  
A1A16 C40  C Y N 40  
A1A16 O41  O N N 41  
A1A16 H1   H N N 42  
A1A16 H2   H N N 43  
A1A16 H3   H N N 44  
A1A16 H4   H N N 45  
A1A16 H5   H N N 46  
A1A16 H6   H N N 47  
A1A16 H7   H N N 48  
A1A16 H8   H N N 49  
A1A16 H9   H N N 50  
A1A16 H10  H N N 51  
A1A16 H11  H N N 52  
A1A16 H12  H N N 53  
A1A16 H13  H N N 54  
A1A16 H14  H N N 55  
A1A16 H15  H N N 56  
A1A16 H16  H N N 57  
A1A16 H17  H N N 58  
A1A16 H18  H N N 59  
A1A16 H19  H N N 60  
A1A16 H20  H N N 61  
A1A16 H21  H N N 62  
A1A16 H22  H N N 63  
A1A16 H23  H N N 64  
A1A16 H24  H N N 65  
A1A16 H25  H N N 66  
A1A16 H26  H N N 67  
A1A16 H27  H N N 68  
A1A16 H28  H N N 69  
A1A16 H29  H N N 70  
A1A16 H30  H N N 71  
A1A16 H31  H N N 72  
ALA   N    N N N 73  
ALA   CA   C N S 74  
ALA   C    C N N 75  
ALA   O    O N N 76  
ALA   CB   C N N 77  
ALA   OXT  O N N 78  
ALA   H    H N N 79  
ALA   H2   H N N 80  
ALA   HA   H N N 81  
ALA   HB1  H N N 82  
ALA   HB2  H N N 83  
ALA   HB3  H N N 84  
ALA   HXT  H N N 85  
ARG   N    N N N 86  
ARG   CA   C N S 87  
ARG   C    C N N 88  
ARG   O    O N N 89  
ARG   CB   C N N 90  
ARG   CG   C N N 91  
ARG   CD   C N N 92  
ARG   NE   N N N 93  
ARG   CZ   C N N 94  
ARG   NH1  N N N 95  
ARG   NH2  N N N 96  
ARG   OXT  O N N 97  
ARG   H    H N N 98  
ARG   H2   H N N 99  
ARG   HA   H N N 100 
ARG   HB2  H N N 101 
ARG   HB3  H N N 102 
ARG   HG2  H N N 103 
ARG   HG3  H N N 104 
ARG   HD2  H N N 105 
ARG   HD3  H N N 106 
ARG   HE   H N N 107 
ARG   HH11 H N N 108 
ARG   HH12 H N N 109 
ARG   HH21 H N N 110 
ARG   HH22 H N N 111 
ARG   HXT  H N N 112 
ASN   N    N N N 113 
ASN   CA   C N S 114 
ASN   C    C N N 115 
ASN   O    O N N 116 
ASN   CB   C N N 117 
ASN   CG   C N N 118 
ASN   OD1  O N N 119 
ASN   ND2  N N N 120 
ASN   OXT  O N N 121 
ASN   H    H N N 122 
ASN   H2   H N N 123 
ASN   HA   H N N 124 
ASN   HB2  H N N 125 
ASN   HB3  H N N 126 
ASN   HD21 H N N 127 
ASN   HD22 H N N 128 
ASN   HXT  H N N 129 
ASP   N    N N N 130 
ASP   CA   C N S 131 
ASP   C    C N N 132 
ASP   O    O N N 133 
ASP   CB   C N N 134 
ASP   CG   C N N 135 
ASP   OD1  O N N 136 
ASP   OD2  O N N 137 
ASP   OXT  O N N 138 
ASP   H    H N N 139 
ASP   H2   H N N 140 
ASP   HA   H N N 141 
ASP   HB2  H N N 142 
ASP   HB3  H N N 143 
ASP   HD2  H N N 144 
ASP   HXT  H N N 145 
CYS   N    N N N 146 
CYS   CA   C N R 147 
CYS   C    C N N 148 
CYS   O    O N N 149 
CYS   CB   C N N 150 
CYS   SG   S N N 151 
CYS   OXT  O N N 152 
CYS   H    H N N 153 
CYS   H2   H N N 154 
CYS   HA   H N N 155 
CYS   HB2  H N N 156 
CYS   HB3  H N N 157 
CYS   HG   H N N 158 
CYS   HXT  H N N 159 
EDO   C1   C N N 160 
EDO   O1   O N N 161 
EDO   C2   C N N 162 
EDO   O2   O N N 163 
EDO   H11  H N N 164 
EDO   H12  H N N 165 
EDO   HO1  H N N 166 
EDO   H21  H N N 167 
EDO   H22  H N N 168 
EDO   HO2  H N N 169 
GLN   N    N N N 170 
GLN   CA   C N S 171 
GLN   C    C N N 172 
GLN   O    O N N 173 
GLN   CB   C N N 174 
GLN   CG   C N N 175 
GLN   CD   C N N 176 
GLN   OE1  O N N 177 
GLN   NE2  N N N 178 
GLN   OXT  O N N 179 
GLN   H    H N N 180 
GLN   H2   H N N 181 
GLN   HA   H N N 182 
GLN   HB2  H N N 183 
GLN   HB3  H N N 184 
GLN   HG2  H N N 185 
GLN   HG3  H N N 186 
GLN   HE21 H N N 187 
GLN   HE22 H N N 188 
GLN   HXT  H N N 189 
GLU   N    N N N 190 
GLU   CA   C N S 191 
GLU   C    C N N 192 
GLU   O    O N N 193 
GLU   CB   C N N 194 
GLU   CG   C N N 195 
GLU   CD   C N N 196 
GLU   OE1  O N N 197 
GLU   OE2  O N N 198 
GLU   OXT  O N N 199 
GLU   H    H N N 200 
GLU   H2   H N N 201 
GLU   HA   H N N 202 
GLU   HB2  H N N 203 
GLU   HB3  H N N 204 
GLU   HG2  H N N 205 
GLU   HG3  H N N 206 
GLU   HE2  H N N 207 
GLU   HXT  H N N 208 
GLY   N    N N N 209 
GLY   CA   C N N 210 
GLY   C    C N N 211 
GLY   O    O N N 212 
GLY   OXT  O N N 213 
GLY   H    H N N 214 
GLY   H2   H N N 215 
GLY   HA2  H N N 216 
GLY   HA3  H N N 217 
GLY   HXT  H N N 218 
HIS   N    N N N 219 
HIS   CA   C N S 220 
HIS   C    C N N 221 
HIS   O    O N N 222 
HIS   CB   C N N 223 
HIS   CG   C Y N 224 
HIS   ND1  N Y N 225 
HIS   CD2  C Y N 226 
HIS   CE1  C Y N 227 
HIS   NE2  N Y N 228 
HIS   OXT  O N N 229 
HIS   H    H N N 230 
HIS   H2   H N N 231 
HIS   HA   H N N 232 
HIS   HB2  H N N 233 
HIS   HB3  H N N 234 
HIS   HD1  H N N 235 
HIS   HD2  H N N 236 
HIS   HE1  H N N 237 
HIS   HE2  H N N 238 
HIS   HXT  H N N 239 
HOH   O    O N N 240 
HOH   H1   H N N 241 
HOH   H2   H N N 242 
ILE   N    N N N 243 
ILE   CA   C N S 244 
ILE   C    C N N 245 
ILE   O    O N N 246 
ILE   CB   C N S 247 
ILE   CG1  C N N 248 
ILE   CG2  C N N 249 
ILE   CD1  C N N 250 
ILE   OXT  O N N 251 
ILE   H    H N N 252 
ILE   H2   H N N 253 
ILE   HA   H N N 254 
ILE   HB   H N N 255 
ILE   HG12 H N N 256 
ILE   HG13 H N N 257 
ILE   HG21 H N N 258 
ILE   HG22 H N N 259 
ILE   HG23 H N N 260 
ILE   HD11 H N N 261 
ILE   HD12 H N N 262 
ILE   HD13 H N N 263 
ILE   HXT  H N N 264 
LEU   N    N N N 265 
LEU   CA   C N S 266 
LEU   C    C N N 267 
LEU   O    O N N 268 
LEU   CB   C N N 269 
LEU   CG   C N N 270 
LEU   CD1  C N N 271 
LEU   CD2  C N N 272 
LEU   OXT  O N N 273 
LEU   H    H N N 274 
LEU   H2   H N N 275 
LEU   HA   H N N 276 
LEU   HB2  H N N 277 
LEU   HB3  H N N 278 
LEU   HG   H N N 279 
LEU   HD11 H N N 280 
LEU   HD12 H N N 281 
LEU   HD13 H N N 282 
LEU   HD21 H N N 283 
LEU   HD22 H N N 284 
LEU   HD23 H N N 285 
LEU   HXT  H N N 286 
LYS   N    N N N 287 
LYS   CA   C N S 288 
LYS   C    C N N 289 
LYS   O    O N N 290 
LYS   CB   C N N 291 
LYS   CG   C N N 292 
LYS   CD   C N N 293 
LYS   CE   C N N 294 
LYS   NZ   N N N 295 
LYS   OXT  O N N 296 
LYS   H    H N N 297 
LYS   H2   H N N 298 
LYS   HA   H N N 299 
LYS   HB2  H N N 300 
LYS   HB3  H N N 301 
LYS   HG2  H N N 302 
LYS   HG3  H N N 303 
LYS   HD2  H N N 304 
LYS   HD3  H N N 305 
LYS   HE2  H N N 306 
LYS   HE3  H N N 307 
LYS   HZ1  H N N 308 
LYS   HZ2  H N N 309 
LYS   HZ3  H N N 310 
LYS   HXT  H N N 311 
PHE   N    N N N 312 
PHE   CA   C N S 313 
PHE   C    C N N 314 
PHE   O    O N N 315 
PHE   CB   C N N 316 
PHE   CG   C Y N 317 
PHE   CD1  C Y N 318 
PHE   CD2  C Y N 319 
PHE   CE1  C Y N 320 
PHE   CE2  C Y N 321 
PHE   CZ   C Y N 322 
PHE   OXT  O N N 323 
PHE   H    H N N 324 
PHE   H2   H N N 325 
PHE   HA   H N N 326 
PHE   HB2  H N N 327 
PHE   HB3  H N N 328 
PHE   HD1  H N N 329 
PHE   HD2  H N N 330 
PHE   HE1  H N N 331 
PHE   HE2  H N N 332 
PHE   HZ   H N N 333 
PHE   HXT  H N N 334 
PRO   N    N N N 335 
PRO   CA   C N S 336 
PRO   C    C N N 337 
PRO   O    O N N 338 
PRO   CB   C N N 339 
PRO   CG   C N N 340 
PRO   CD   C N N 341 
PRO   OXT  O N N 342 
PRO   H    H N N 343 
PRO   HA   H N N 344 
PRO   HB2  H N N 345 
PRO   HB3  H N N 346 
PRO   HG2  H N N 347 
PRO   HG3  H N N 348 
PRO   HD2  H N N 349 
PRO   HD3  H N N 350 
PRO   HXT  H N N 351 
SER   N    N N N 352 
SER   CA   C N S 353 
SER   C    C N N 354 
SER   O    O N N 355 
SER   CB   C N N 356 
SER   OG   O N N 357 
SER   OXT  O N N 358 
SER   H    H N N 359 
SER   H2   H N N 360 
SER   HA   H N N 361 
SER   HB2  H N N 362 
SER   HB3  H N N 363 
SER   HG   H N N 364 
SER   HXT  H N N 365 
THR   N    N N N 366 
THR   CA   C N S 367 
THR   C    C N N 368 
THR   O    O N N 369 
THR   CB   C N R 370 
THR   OG1  O N N 371 
THR   CG2  C N N 372 
THR   OXT  O N N 373 
THR   H    H N N 374 
THR   H2   H N N 375 
THR   HA   H N N 376 
THR   HB   H N N 377 
THR   HG1  H N N 378 
THR   HG21 H N N 379 
THR   HG22 H N N 380 
THR   HG23 H N N 381 
THR   HXT  H N N 382 
TRP   N    N N N 383 
TRP   CA   C N S 384 
TRP   C    C N N 385 
TRP   O    O N N 386 
TRP   CB   C N N 387 
TRP   CG   C Y N 388 
TRP   CD1  C Y N 389 
TRP   CD2  C Y N 390 
TRP   NE1  N Y N 391 
TRP   CE2  C Y N 392 
TRP   CE3  C Y N 393 
TRP   CZ2  C Y N 394 
TRP   CZ3  C Y N 395 
TRP   CH2  C Y N 396 
TRP   OXT  O N N 397 
TRP   H    H N N 398 
TRP   H2   H N N 399 
TRP   HA   H N N 400 
TRP   HB2  H N N 401 
TRP   HB3  H N N 402 
TRP   HD1  H N N 403 
TRP   HE1  H N N 404 
TRP   HE3  H N N 405 
TRP   HZ2  H N N 406 
TRP   HZ3  H N N 407 
TRP   HH2  H N N 408 
TRP   HXT  H N N 409 
TYR   N    N N N 410 
TYR   CA   C N S 411 
TYR   C    C N N 412 
TYR   O    O N N 413 
TYR   CB   C N N 414 
TYR   CG   C Y N 415 
TYR   CD1  C Y N 416 
TYR   CD2  C Y N 417 
TYR   CE1  C Y N 418 
TYR   CE2  C Y N 419 
TYR   CZ   C Y N 420 
TYR   OH   O N N 421 
TYR   OXT  O N N 422 
TYR   H    H N N 423 
TYR   H2   H N N 424 
TYR   HA   H N N 425 
TYR   HB2  H N N 426 
TYR   HB3  H N N 427 
TYR   HD1  H N N 428 
TYR   HD2  H N N 429 
TYR   HE1  H N N 430 
TYR   HE2  H N N 431 
TYR   HH   H N N 432 
TYR   HXT  H N N 433 
VAL   N    N N N 434 
VAL   CA   C N S 435 
VAL   C    C N N 436 
VAL   O    O N N 437 
VAL   CB   C N N 438 
VAL   CG1  C N N 439 
VAL   CG2  C N N 440 
VAL   OXT  O N N 441 
VAL   H    H N N 442 
VAL   H2   H N N 443 
VAL   HA   H N N 444 
VAL   HB   H N N 445 
VAL   HG11 H N N 446 
VAL   HG12 H N N 447 
VAL   HG13 H N N 448 
VAL   HG21 H N N 449 
VAL   HG22 H N N 450 
VAL   HG23 H N N 451 
VAL   HXT  H N N 452 
# 
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 
A1A16 C38 N37  sing Y N 1   
A1A16 C38 C39  doub Y N 2   
A1A16 N37 C36  doub Y N 3   
A1A16 C39 N35  sing Y N 4   
A1A16 C36 N35  sing Y N 5   
A1A16 N35 C34  sing N N 6   
A1A16 C34 C33  sing N N 7   
A1A16 F31 C28  sing N N 8   
A1A16 C25 C24  sing N N 9   
A1A16 C32 C33  doub Y N 10  
A1A16 C32 C20  sing Y N 11  
A1A16 C33 C40  sing Y N 12  
A1A16 F29 C28  sing N N 13  
A1A16 C28 C27  sing N N 14  
A1A16 C28 F30  sing N N 15  
A1A16 N26 C27  doub Y N 16  
A1A16 N26 N23  sing Y N 17  
A1A16 C27 C21  sing Y N 18  
A1A16 N23 C24  sing N N 19  
A1A16 N23 C22  sing Y N 20  
A1A16 C21 C22  doub Y N 21  
A1A16 C21 C20  sing N N 22  
A1A16 C20 C19  doub Y N 23  
A1A16 C40 C18  doub Y N 24  
A1A16 C19 C18  sing Y N 25  
A1A16 C18 C17  sing N N 26  
A1A16 C17 O41  doub N N 27  
A1A16 C17 N16  sing N N 28  
A1A16 N16 C4   sing N N 29  
A1A16 O15 C5   doub N N 30  
A1A16 C14 C13  doub Y N 31  
A1A16 C14 C10  sing Y N 32  
A1A16 C13 S12  sing Y N 33  
A1A16 C5  C4   sing N N 34  
A1A16 C5  N6   sing N N 35  
A1A16 C10 C9   sing N N 36  
A1A16 C10 C11  doub Y N 37  
A1A16 C9  N6   sing N N 38  
A1A16 C4  C3   sing N N 39  
A1A16 S12 C11  sing Y N 40  
A1A16 N6  C7   sing N N 41  
A1A16 C11 C8   sing N N 42  
A1A16 C8  C7   sing N N 43  
A1A16 C3  C2   sing N N 44  
A1A16 C2  C1   sing N N 45  
A1A16 C4  H1   sing N N 46  
A1A16 C7  H2   sing N N 47  
A1A16 C7  H3   sing N N 48  
A1A16 C8  H4   sing N N 49  
A1A16 C8  H5   sing N N 50  
A1A16 C13 H6   sing N N 51  
A1A16 C22 H7   sing N N 52  
A1A16 C24 H8   sing N N 53  
A1A16 C24 H9   sing N N 54  
A1A16 C1  H10  sing N N 55  
A1A16 C1  H11  sing N N 56  
A1A16 C1  H12  sing N N 57  
A1A16 C2  H13  sing N N 58  
A1A16 C2  H14  sing N N 59  
A1A16 C3  H15  sing N N 60  
A1A16 C3  H16  sing N N 61  
A1A16 C9  H17  sing N N 62  
A1A16 C9  H18  sing N N 63  
A1A16 C14 H19  sing N N 64  
A1A16 N16 H20  sing N N 65  
A1A16 C19 H21  sing N N 66  
A1A16 C25 H22  sing N N 67  
A1A16 C25 H23  sing N N 68  
A1A16 C25 H24  sing N N 69  
A1A16 C32 H25  sing N N 70  
A1A16 C34 H26  sing N N 71  
A1A16 C34 H27  sing N N 72  
A1A16 C36 H28  sing N N 73  
A1A16 C38 H29  sing N N 74  
A1A16 C39 H30  sing N N 75  
A1A16 C40 H31  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
EDO   C1  O1   sing N N 159 
EDO   C1  C2   sing N N 160 
EDO   C1  H11  sing N N 161 
EDO   C1  H12  sing N N 162 
EDO   O1  HO1  sing N N 163 
EDO   C2  O2   sing N N 164 
EDO   C2  H21  sing N N 165 
EDO   C2  H22  sing N N 166 
EDO   O2  HO2  sing N N 167 
GLN   N   CA   sing N N 168 
GLN   N   H    sing N N 169 
GLN   N   H2   sing N N 170 
GLN   CA  C    sing N N 171 
GLN   CA  CB   sing N N 172 
GLN   CA  HA   sing N N 173 
GLN   C   O    doub N N 174 
GLN   C   OXT  sing N N 175 
GLN   CB  CG   sing N N 176 
GLN   CB  HB2  sing N N 177 
GLN   CB  HB3  sing N N 178 
GLN   CG  CD   sing N N 179 
GLN   CG  HG2  sing N N 180 
GLN   CG  HG3  sing N N 181 
GLN   CD  OE1  doub N N 182 
GLN   CD  NE2  sing N N 183 
GLN   NE2 HE21 sing N N 184 
GLN   NE2 HE22 sing N N 185 
GLN   OXT HXT  sing N N 186 
GLU   N   CA   sing N N 187 
GLU   N   H    sing N N 188 
GLU   N   H2   sing N N 189 
GLU   CA  C    sing N N 190 
GLU   CA  CB   sing N N 191 
GLU   CA  HA   sing N N 192 
GLU   C   O    doub N N 193 
GLU   C   OXT  sing N N 194 
GLU   CB  CG   sing N N 195 
GLU   CB  HB2  sing N N 196 
GLU   CB  HB3  sing N N 197 
GLU   CG  CD   sing N N 198 
GLU   CG  HG2  sing N N 199 
GLU   CG  HG3  sing N N 200 
GLU   CD  OE1  doub N N 201 
GLU   CD  OE2  sing N N 202 
GLU   OE2 HE2  sing N N 203 
GLU   OXT HXT  sing N N 204 
GLY   N   CA   sing N N 205 
GLY   N   H    sing N N 206 
GLY   N   H2   sing N N 207 
GLY   CA  C    sing N N 208 
GLY   CA  HA2  sing N N 209 
GLY   CA  HA3  sing N N 210 
GLY   C   O    doub N N 211 
GLY   C   OXT  sing N N 212 
GLY   OXT HXT  sing N N 213 
HIS   N   CA   sing N N 214 
HIS   N   H    sing N N 215 
HIS   N   H2   sing N N 216 
HIS   CA  C    sing N N 217 
HIS   CA  CB   sing N N 218 
HIS   CA  HA   sing N N 219 
HIS   C   O    doub N N 220 
HIS   C   OXT  sing N N 221 
HIS   CB  CG   sing N N 222 
HIS   CB  HB2  sing N N 223 
HIS   CB  HB3  sing N N 224 
HIS   CG  ND1  sing Y N 225 
HIS   CG  CD2  doub Y N 226 
HIS   ND1 CE1  doub Y N 227 
HIS   ND1 HD1  sing N N 228 
HIS   CD2 NE2  sing Y N 229 
HIS   CD2 HD2  sing N N 230 
HIS   CE1 NE2  sing Y N 231 
HIS   CE1 HE1  sing N N 232 
HIS   NE2 HE2  sing N N 233 
HIS   OXT HXT  sing N N 234 
HOH   O   H1   sing N N 235 
HOH   O   H2   sing N N 236 
ILE   N   CA   sing N N 237 
ILE   N   H    sing N N 238 
ILE   N   H2   sing N N 239 
ILE   CA  C    sing N N 240 
ILE   CA  CB   sing N N 241 
ILE   CA  HA   sing N N 242 
ILE   C   O    doub N N 243 
ILE   C   OXT  sing N N 244 
ILE   CB  CG1  sing N N 245 
ILE   CB  CG2  sing N N 246 
ILE   CB  HB   sing N N 247 
ILE   CG1 CD1  sing N N 248 
ILE   CG1 HG12 sing N N 249 
ILE   CG1 HG13 sing N N 250 
ILE   CG2 HG21 sing N N 251 
ILE   CG2 HG22 sing N N 252 
ILE   CG2 HG23 sing N N 253 
ILE   CD1 HD11 sing N N 254 
ILE   CD1 HD12 sing N N 255 
ILE   CD1 HD13 sing N N 256 
ILE   OXT HXT  sing N N 257 
LEU   N   CA   sing N N 258 
LEU   N   H    sing N N 259 
LEU   N   H2   sing N N 260 
LEU   CA  C    sing N N 261 
LEU   CA  CB   sing N N 262 
LEU   CA  HA   sing N N 263 
LEU   C   O    doub N N 264 
LEU   C   OXT  sing N N 265 
LEU   CB  CG   sing N N 266 
LEU   CB  HB2  sing N N 267 
LEU   CB  HB3  sing N N 268 
LEU   CG  CD1  sing N N 269 
LEU   CG  CD2  sing N N 270 
LEU   CG  HG   sing N N 271 
LEU   CD1 HD11 sing N N 272 
LEU   CD1 HD12 sing N N 273 
LEU   CD1 HD13 sing N N 274 
LEU   CD2 HD21 sing N N 275 
LEU   CD2 HD22 sing N N 276 
LEU   CD2 HD23 sing N N 277 
LEU   OXT HXT  sing N N 278 
LYS   N   CA   sing N N 279 
LYS   N   H    sing N N 280 
LYS   N   H2   sing N N 281 
LYS   CA  C    sing N N 282 
LYS   CA  CB   sing N N 283 
LYS   CA  HA   sing N N 284 
LYS   C   O    doub N N 285 
LYS   C   OXT  sing N N 286 
LYS   CB  CG   sing N N 287 
LYS   CB  HB2  sing N N 288 
LYS   CB  HB3  sing N N 289 
LYS   CG  CD   sing N N 290 
LYS   CG  HG2  sing N N 291 
LYS   CG  HG3  sing N N 292 
LYS   CD  CE   sing N N 293 
LYS   CD  HD2  sing N N 294 
LYS   CD  HD3  sing N N 295 
LYS   CE  NZ   sing N N 296 
LYS   CE  HE2  sing N N 297 
LYS   CE  HE3  sing N N 298 
LYS   NZ  HZ1  sing N N 299 
LYS   NZ  HZ2  sing N N 300 
LYS   NZ  HZ3  sing N N 301 
LYS   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   'Other private' 
_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   3SMR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D5Z 
_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]   0.021299 
_atom_sites.fract_transf_matrix[1][2]   0.008693 
_atom_sites.fract_transf_matrix[1][3]   0.004122 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017653 
_atom_sites.fract_transf_matrix[2][3]   0.007375 
_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]   0.016779 
_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 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . VAL   A 1 9   ? 2.350   54.655 -16.333 1.00 58.89 ? 31  VAL   A N   1 
ATOM   2    C CA  . VAL   A 1 9   ? 1.461   53.622 -16.953 1.00 56.70 ? 31  VAL   A CA  1 
ATOM   3    C C   . VAL   A 1 9   ? 1.255   52.485 -15.950 1.00 49.33 ? 31  VAL   A C   1 
ATOM   4    O O   . VAL   A 1 9   ? 2.202   51.994 -15.334 1.00 47.22 ? 31  VAL   A O   1 
ATOM   5    C CB  . VAL   A 1 9   ? 1.945   53.070 -18.314 1.00 58.91 ? 31  VAL   A CB  1 
ATOM   6    C CG1 . VAL   A 1 9   ? 1.986   54.144 -19.391 1.00 60.25 ? 31  VAL   A CG1 1 
ATOM   7    C CG2 . VAL   A 1 9   ? 3.298   52.382 -18.227 1.00 61.98 ? 31  VAL   A CG2 1 
ATOM   8    N N   . LYS   A 1 10  ? -0.012  52.090 -15.786 1.00 42.41 ? 32  LYS   A N   1 
ATOM   9    C CA  . LYS   A 1 10  ? -0.375  50.900 -15.038 1.00 37.63 ? 32  LYS   A CA  1 
ATOM   10   C C   . LYS   A 1 10  ? -1.097  49.957 -16.002 1.00 34.01 ? 32  LYS   A C   1 
ATOM   11   O O   . LYS   A 1 10  ? -1.757  50.417 -16.935 1.00 34.28 ? 32  LYS   A O   1 
ATOM   12   C CB  . LYS   A 1 10  ? -1.226  51.310 -13.827 1.00 40.85 ? 32  LYS   A CB  1 
ATOM   13   C CG  . LYS   A 1 10  ? -0.615  52.364 -12.874 1.00 42.87 ? 32  LYS   A CG  1 
ATOM   14   C CD  . LYS   A 1 10  ? -1.393  52.576 -11.573 1.00 45.15 ? 32  LYS   A CD  1 
ATOM   15   C CE  . LYS   A 1 10  ? -0.753  53.513 -10.581 1.00 43.13 ? 32  LYS   A CE  1 
ATOM   16   N N   . PRO   A 1 11  ? -1.003  48.618 -15.828 1.00 29.60 ? 33  PRO   A N   1 
ATOM   17   C CA  . PRO   A 1 11  ? -1.759  47.695 -16.671 1.00 28.52 ? 33  PRO   A CA  1 
ATOM   18   C C   . PRO   A 1 11  ? -3.220  47.711 -16.232 1.00 28.53 ? 33  PRO   A C   1 
ATOM   19   O O   . PRO   A 1 11  ? -3.568  48.315 -15.219 1.00 28.53 ? 33  PRO   A O   1 
ATOM   20   C CB  . PRO   A 1 11  ? -1.051  46.354 -16.453 1.00 28.38 ? 33  PRO   A CB  1 
ATOM   21   C CG  . PRO   A 1 11  ? -0.518  46.444 -15.037 1.00 28.50 ? 33  PRO   A CG  1 
ATOM   22   C CD  . PRO   A 1 11  ? -0.207  47.918 -14.804 1.00 29.37 ? 33  PRO   A CD  1 
ATOM   23   N N   . ASN   A 1 12  ? -4.080  47.082 -17.031 1.00 29.65 ? 34  ASN   A N   1 
ATOM   24   C CA  . ASN   A 1 12  ? -5.502  47.060 -16.731 1.00 28.21 ? 34  ASN   A CA  1 
ATOM   25   C C   . ASN   A 1 12  ? -6.034  45.659 -17.029 1.00 25.99 ? 34  ASN   A C   1 
ATOM   26   O O   . ASN   A 1 12  ? -7.017  45.491 -17.749 1.00 26.54 ? 34  ASN   A O   1 
ATOM   27   C CB  . ASN   A 1 12  ? -6.234  48.185 -17.456 1.00 30.25 ? 34  ASN   A CB  1 
ATOM   28   C CG  . ASN   A 1 12  ? -6.231  47.981 -18.953 1.00 31.86 ? 34  ASN   A CG  1 
ATOM   29   O OD1 . ASN   A 1 12  ? -5.372  47.278 -19.498 1.00 33.15 ? 34  ASN   A OD1 1 
ATOM   30   N ND2 . ASN   A 1 12  ? -7.189  48.578 -19.636 1.00 34.12 ? 34  ASN   A ND2 1 
ATOM   31   N N   . TYR   A 1 13  ? -5.354  44.652 -16.475 1.00 22.96 ? 35  TYR   A N   1 
ATOM   32   C CA  . TYR   A 1 13  ? -5.826  43.282 -16.539 1.00 23.26 ? 35  TYR   A CA  1 
ATOM   33   C C   . TYR   A 1 13  ? -7.274  43.198 -16.057 1.00 23.99 ? 35  TYR   A C   1 
ATOM   34   O O   . TYR   A 1 13  ? -7.629  43.716 -14.996 1.00 23.52 ? 35  TYR   A O   1 
ATOM   35   C CB  . TYR   A 1 13  ? -4.890  42.399 -15.711 1.00 22.90 ? 35  TYR   A CB  1 
ATOM   36   C CG  . TYR   A 1 13  ? -3.608  42.102 -16.469 1.00 21.82 ? 35  TYR   A CG  1 
ATOM   37   C CD1 . TYR   A 1 13  ? -3.566  41.071 -17.398 1.00 20.72 ? 35  TYR   A CD1 1 
ATOM   38   C CD2 . TYR   A 1 13  ? -2.472  42.890 -16.318 1.00 21.88 ? 35  TYR   A CD2 1 
ATOM   39   C CE1 . TYR   A 1 13  ? -2.423  40.805 -18.129 1.00 20.17 ? 35  TYR   A CE1 1 
ATOM   40   C CE2 . TYR   A 1 13  ? -1.312  42.611 -17.020 1.00 21.99 ? 35  TYR   A CE2 1 
ATOM   41   C CZ  . TYR   A 1 13  ? -1.296  41.580 -17.947 1.00 21.44 ? 35  TYR   A CZ  1 
ATOM   42   O OH  . TYR   A 1 13  ? -0.182  41.291 -18.688 1.00 23.25 ? 35  TYR   A OH  1 
ATOM   43   N N   . ALA   A 1 14  ? -8.096  42.519 -16.852 1.00 22.87 ? 36  ALA   A N   1 
ATOM   44   C CA  . ALA   A 1 14  ? -9.479  42.232 -16.514 1.00 24.76 ? 36  ALA   A CA  1 
ATOM   45   C C   . ALA   A 1 14  ? -9.727  40.755 -16.787 1.00 23.10 ? 36  ALA   A C   1 
ATOM   46   O O   . ALA   A 1 14  ? -9.070  40.190 -17.652 1.00 23.06 ? 36  ALA   A O   1 
ATOM   47   C CB  . ALA   A 1 14  ? -10.411 43.100 -17.328 1.00 26.52 ? 36  ALA   A CB  1 
ATOM   48   N N   . LEU   A 1 15  ? -10.680 40.161 -16.059 1.00 23.32 ? 37  LEU   A N   1 
ATOM   49   C CA  . LEU   A 1 15  ? -10.975 38.744 -16.163 1.00 22.38 ? 37  LEU   A CA  1 
ATOM   50   C C   . LEU   A 1 15  ? -11.635 38.444 -17.504 1.00 20.69 ? 37  LEU   A C   1 
ATOM   51   O O   . LEU   A 1 15  ? -12.605 39.098 -17.883 1.00 22.47 ? 37  LEU   A O   1 
ATOM   52   C CB  . LEU   A 1 15  ? -11.867 38.346 -14.986 1.00 23.66 ? 37  LEU   A CB  1 
ATOM   53   C CG  . LEU   A 1 15  ? -12.227 36.864 -14.872 1.00 23.48 ? 37  LEU   A CG  1 
ATOM   54   C CD1 . LEU   A 1 15  ? -10.997 35.978 -14.670 1.00 22.16 ? 37  LEU   A CD1 1 
ATOM   55   C CD2 . LEU   A 1 15  ? -13.243 36.673 -13.744 1.00 24.39 ? 37  LEU   A CD2 1 
ATOM   56   N N   . LYS   A 1 16  ? -11.090 37.449 -18.211 1.00 20.09 ? 38  LYS   A N   1 
ATOM   57   C CA  . LYS   A 1 16  ? -11.635 36.993 -19.471 1.00 19.99 ? 38  LYS   A CA  1 
ATOM   58   C C   . LYS   A 1 16  ? -12.305 35.632 -19.317 1.00 20.30 ? 38  LYS   A C   1 
ATOM   59   O O   . LYS   A 1 16  ? -13.365 35.417 -19.883 1.00 22.38 ? 38  LYS   A O   1 
ATOM   60   C CB  . LYS   A 1 16  ? -10.507 36.916 -20.503 1.00 21.90 ? 38  LYS   A CB  1 
ATOM   61   C CG  . LYS   A 1 16  ? -9.859  38.264 -20.720 1.00 24.14 ? 38  LYS   A CG  1 
ATOM   62   C CD  . LYS   A 1 16  ? -10.786 39.315 -21.327 1.00 26.36 ? 38  LYS   A CD  1 
ATOM   63   C CE  . LYS   A 1 16  ? -11.197 38.948 -22.723 1.00 29.91 ? 38  LYS   A CE  1 
ATOM   64   N NZ  . LYS   A 1 16  ? -11.630 40.141 -23.436 1.00 33.55 ? 38  LYS   A NZ  1 
ATOM   65   N N   . PHE   A 1 17  ? -11.646 34.697 -18.624 1.00 19.63 ? 39  PHE   A N   1 
ATOM   66   C CA  . PHE   A 1 17  ? -12.180 33.348 -18.490 1.00 19.37 ? 39  PHE   A CA  1 
ATOM   67   C C   . PHE   A 1 17  ? -11.855 32.788 -17.117 1.00 18.98 ? 39  PHE   A C   1 
ATOM   68   O O   . PHE   A 1 17  ? -10.790 33.074 -16.574 1.00 19.68 ? 39  PHE   A O   1 
ATOM   69   C CB  . PHE   A 1 17  ? -11.615 32.387 -19.542 1.00 19.72 ? 39  PHE   A CB  1 
ATOM   70   C CG  . PHE   A 1 17  ? -11.903 32.854 -20.960 1.00 19.02 ? 39  PHE   A CG  1 
ATOM   71   C CD1 . PHE   A 1 17  ? -13.162 32.680 -21.523 1.00 19.76 ? 39  PHE   A CD1 1 
ATOM   72   C CD2 . PHE   A 1 17  ? -10.926 33.497 -21.713 1.00 19.88 ? 39  PHE   A CD2 1 
ATOM   73   C CE1 . PHE   A 1 17  ? -13.444 33.144 -22.803 1.00 20.90 ? 39  PHE   A CE1 1 
ATOM   74   C CE2 . PHE   A 1 17  ? -11.208 33.959 -22.993 1.00 20.34 ? 39  PHE   A CE2 1 
ATOM   75   C CZ  . PHE   A 1 17  ? -12.467 33.772 -23.540 1.00 20.69 ? 39  PHE   A CZ  1 
ATOM   76   N N   . THR   A 1 18  ? -12.770 31.948 -16.620 1.00 19.19 ? 40  THR   A N   1 
ATOM   77   C CA  . THR   A 1 18  ? -12.506 31.079 -15.483 1.00 20.08 ? 40  THR   A CA  1 
ATOM   78   C C   . THR   A 1 18  ? -12.594 29.632 -15.958 1.00 20.72 ? 40  THR   A C   1 
ATOM   79   O O   . THR   A 1 18  ? -13.610 29.235 -16.530 1.00 22.67 ? 40  THR   A O   1 
ATOM   80   C CB  . THR   A 1 18  ? -13.491 31.325 -14.348 1.00 20.80 ? 40  THR   A CB  1 
ATOM   81   O OG1 . THR   A 1 18  ? -13.323 32.692 -13.989 1.00 21.26 ? 40  THR   A OG1 1 
ATOM   82   C CG2 . THR   A 1 18  ? -13.221 30.422 -13.155 1.00 21.88 ? 40  THR   A CG2 1 
ATOM   83   N N   . LEU   A 1 19  ? -11.524 28.869 -15.701 1.00 20.05 ? 41  LEU   A N   1 
ATOM   84   C CA  . LEU   A 1 19  ? -11.369 27.516 -16.205 1.00 21.09 ? 41  LEU   A CA  1 
ATOM   85   C C   . LEU   A 1 19  ? -11.571 26.540 -15.054 1.00 20.82 ? 41  LEU   A C   1 
ATOM   86   O O   . LEU   A 1 19  ? -10.718 26.457 -14.167 1.00 20.87 ? 41  LEU   A O   1 
ATOM   87   C CB  . LEU   A 1 19  ? -9.996  27.289 -16.836 1.00 22.16 ? 41  LEU   A CB  1 
ATOM   88   C CG  . LEU   A 1 19  ? -9.428  28.417 -17.693 1.00 23.57 ? 41  LEU   A CG  1 
ATOM   89   C CD1 . LEU   A 1 19  ? -8.185  27.957 -18.434 1.00 23.76 ? 41  LEU   A CD1 1 
ATOM   90   C CD2 . LEU   A 1 19  ? -10.443 29.001 -18.629 1.00 23.82 ? 41  LEU   A CD2 1 
ATOM   91   N N   . ALA   A 1 20  ? -12.690 25.809 -15.102 1.00 21.26 ? 42  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? -13.024 24.831 -14.087 1.00 20.50 ? 42  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? -12.856 23.425 -14.645 1.00 21.31 ? 42  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? -13.140 23.144 -15.822 1.00 20.55 ? 42  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? -14.441 25.017 -13.597 1.00 22.39 ? 42  ALA   A CB  1 
ATOM   96   N N   . GLY   A 1 21  ? -12.467 22.524 -13.747 1.00 21.12 ? 43  GLY   A N   1 
ATOM   97   C CA  . GLY   A 1 21  ? -12.369 21.119 -14.105 1.00 21.63 ? 43  GLY   A CA  1 
ATOM   98   C C   . GLY   A 1 21  ? -11.533 20.320 -13.120 1.00 20.75 ? 43  GLY   A C   1 
ATOM   99   O O   . GLY   A 1 21  ? -11.806 19.138 -12.925 1.00 22.73 ? 43  GLY   A O   1 
ATOM   100  N N   . HIS   A 1 22  ? -10.479 20.926 -12.563 1.00 20.25 ? 44  HIS   A N   1 
ATOM   101  C CA  . HIS   A 1 22  ? -9.684  20.225 -11.568 1.00 19.94 ? 44  HIS   A CA  1 
ATOM   102  C C   . HIS   A 1 22  ? -10.556 19.977 -10.338 1.00 19.79 ? 44  HIS   A C   1 
ATOM   103  O O   . HIS   A 1 22  ? -11.443 20.775 -10.016 1.00 20.73 ? 44  HIS   A O   1 
ATOM   104  C CB  . HIS   A 1 22  ? -8.391  20.982 -11.255 1.00 18.87 ? 44  HIS   A CB  1 
ATOM   105  C CG  . HIS   A 1 22  ? -7.353  20.867 -12.313 1.00 17.56 ? 44  HIS   A CG  1 
ATOM   106  N ND1 . HIS   A 1 22  ? -6.796  19.656 -12.661 1.00 17.13 ? 44  HIS   A ND1 1 
ATOM   107  C CD2 . HIS   A 1 22  ? -6.727  21.798 -13.050 1.00 18.49 ? 44  HIS   A CD2 1 
ATOM   108  C CE1 . HIS   A 1 22  ? -5.873  19.871 -13.600 1.00 18.18 ? 44  HIS   A CE1 1 
ATOM   109  N NE2 . HIS   A 1 22  ? -5.826  21.165 -13.862 1.00 17.70 ? 44  HIS   A NE2 1 
ATOM   110  N N   . THR   A 1 23  ? -10.328 18.839 -9.671  1.00 20.14 ? 45  THR   A N   1 
ATOM   111  C CA  . THR   A 1 23  ? -11.180 18.434 -8.558  1.00 20.41 ? 45  THR   A CA  1 
ATOM   112  C C   . THR   A 1 23  ? -10.435 18.584 -7.239  1.00 19.54 ? 45  THR   A C   1 
ATOM   113  O O   . THR   A 1 23  ? -10.985 18.255 -6.191  1.00 19.22 ? 45  THR   A O   1 
ATOM   114  C CB  . THR   A 1 23  ? -11.676 17.005 -8.755  1.00 22.28 ? 45  THR   A CB  1 
ATOM   115  O OG1 . THR   A 1 23  ? -10.552 16.135 -8.801  1.00 21.73 ? 45  THR   A OG1 1 
ATOM   116  C CG2 . THR   A 1 23  ? -12.471 16.851 -10.038 1.00 24.85 ? 45  THR   A CG2 1 
ATOM   117  N N   . LYS   A 1 24  ? -9.182  19.050 -7.315  1.00 20.20 ? 46  LYS   A N   1 
ATOM   118  C CA  . LYS   A 1 24  ? -8.402  19.446 -6.151  1.00 19.78 ? 46  LYS   A CA  1 
ATOM   119  C C   . LYS   A 1 24  ? -7.637  20.713 -6.519  1.00 19.94 ? 46  LYS   A C   1 
ATOM   120  O O   . LYS   A 1 24  ? -7.742  21.206 -7.648  1.00 21.27 ? 46  LYS   A O   1 
ATOM   121  C CB  . LYS   A 1 24  ? -7.479  18.313 -5.679  1.00 21.02 ? 46  LYS   A CB  1 
ATOM   122  C CG  . LYS   A 1 24  ? -8.153  17.080 -5.124  1.00 21.74 ? 46  LYS   A CG  1 
ATOM   123  C CD  . LYS   A 1 24  ? -7.165  16.120 -4.475  1.00 21.22 ? 46  LYS   A CD  1 
ATOM   124  C CE  . LYS   A 1 24  ? -7.792  14.894 -3.899  1.00 21.56 ? 46  LYS   A CE  1 
ATOM   125  N NZ  . LYS   A 1 24  ? -6.772  14.034 -3.271  1.00 20.79 ? 46  LYS   A NZ  1 
ATOM   126  N N   . ALA   A 1 25  ? -6.872  21.237 -5.559  1.00 20.48 ? 47  ALA   A N   1 
ATOM   127  C CA  . ALA   A 1 25  ? -6.053  22.417 -5.761  1.00 19.66 ? 47  ALA   A CA  1 
ATOM   128  C C   . ALA   A 1 25  ? -5.272  22.328 -7.075  1.00 19.09 ? 47  ALA   A C   1 
ATOM   129  O O   . ALA   A 1 25  ? -4.792  21.262 -7.447  1.00 18.77 ? 47  ALA   A O   1 
ATOM   130  C CB  . ALA   A 1 25  ? -5.101  22.563 -4.583  1.00 20.34 ? 47  ALA   A CB  1 
ATOM   131  N N   . VAL   A 1 26  ? -5.171  23.464 -7.781  1.00 19.78 ? 48  VAL   A N   1 
ATOM   132  C CA  . VAL   A 1 26  ? -4.278  23.595 -8.925  1.00 19.43 ? 48  VAL   A CA  1 
ATOM   133  C C   . VAL   A 1 26  ? -2.902  23.963 -8.388  1.00 19.42 ? 48  VAL   A C   1 
ATOM   134  O O   . VAL   A 1 26  ? -2.809  24.774 -7.469  1.00 20.41 ? 48  VAL   A O   1 
ATOM   135  C CB  . VAL   A 1 26  ? -4.806  24.657 -9.904  1.00 19.70 ? 48  VAL   A CB  1 
ATOM   136  C CG1 . VAL   A 1 26  ? -3.940  24.797 -11.148 1.00 19.47 ? 48  VAL   A CG1 1 
ATOM   137  C CG2 . VAL   A 1 26  ? -6.266  24.384 -10.268 1.00 20.61 ? 48  VAL   A CG2 1 
ATOM   138  N N   . SER   A 1 27  ? -1.855  23.333 -8.938  1.00 17.65 ? 49  SER   A N   1 
ATOM   139  C CA  . SER   A 1 27  ? -0.495  23.504 -8.432  1.00 17.82 ? 49  SER   A CA  1 
ATOM   140  C C   . SER   A 1 27  ? 0.346   24.433 -9.307  1.00 17.51 ? 49  SER   A C   1 
ATOM   141  O O   . SER   A 1 27  ? 1.211   25.147 -8.801  1.00 17.66 ? 49  SER   A O   1 
ATOM   142  C CB  . SER   A 1 27  ? 0.198   22.171 -8.281  1.00 17.62 ? 49  SER   A CB  1 
ATOM   143  O OG  . SER   A 1 27  ? 0.113   21.368 -9.458  1.00 17.62 ? 49  SER   A OG  1 
ATOM   144  N N   . SER   A 1 28  ? 0.135   24.389 -10.627 1.00 16.81 ? 50  SER   A N   1 
ATOM   145  C CA  . SER   A 1 28  ? 0.994   25.109 -11.553 1.00 17.53 ? 50  SER   A CA  1 
ATOM   146  C C   . SER   A 1 28  ? 0.261   25.340 -12.864 1.00 16.82 ? 50  SER   A C   1 
ATOM   147  O O   . SER   A 1 28  ? -0.406  24.439 -13.370 1.00 18.17 ? 50  SER   A O   1 
ATOM   148  C CB  . SER   A 1 28  ? 2.285   24.345 -11.781 1.00 18.28 ? 50  SER   A CB  1 
ATOM   149  O OG  . SER   A 1 28  ? 3.258   25.132 -12.448 1.00 20.34 ? 50  SER   A OG  1 
ATOM   150  N N   . VAL   A 1 29  ? 0.401   26.552 -13.404 1.00 15.98 ? 51  VAL   A N   1 
ATOM   151  C CA  . VAL   A 1 29  ? -0.013  26.829 -14.773 1.00 15.09 ? 51  VAL   A CA  1 
ATOM   152  C C   . VAL   A 1 29  ? 1.169   27.379 -15.561 1.00 14.94 ? 51  VAL   A C   1 
ATOM   153  O O   . VAL   A 1 29  ? 1.979   28.140 -15.039 1.00 14.99 ? 51  VAL   A O   1 
ATOM   154  C CB  . VAL   A 1 29  ? -1.230  27.767 -14.847 1.00 16.04 ? 51  VAL   A CB  1 
ATOM   155  C CG1 . VAL   A 1 29  ? -2.470  27.104 -14.257 1.00 17.05 ? 51  VAL   A CG1 1 
ATOM   156  C CG2 . VAL   A 1 29  ? -0.968  29.116 -14.204 1.00 16.42 ? 51  VAL   A CG2 1 
ATOM   157  N N   . LYS   A 1 30  ? 1.217   27.014 -16.847 1.00 15.34 ? 52  LYS   A N   1 
ATOM   158  C CA  . LYS   A 1 30  ? 2.298   27.429 -17.724 1.00 15.27 ? 52  LYS   A CA  1 
ATOM   159  C C   . LYS   A 1 30  ? 1.774   27.542 -19.148 1.00 15.21 ? 52  LYS   A C   1 
ATOM   160  O O   . LYS   A 1 30  ? 1.089   26.648 -19.642 1.00 14.86 ? 52  LYS   A O   1 
ATOM   161  C CB  . LYS   A 1 30  ? 3.413   26.387 -17.785 1.00 16.14 ? 52  LYS   A CB  1 
ATOM   162  C CG  . LYS   A 1 30  ? 4.133   26.023 -16.494 1.00 17.36 ? 52  LYS   A CG  1 
ATOM   163  C CD  . LYS   A 1 30  ? 4.981   27.106 -15.833 1.00 17.61 ? 52  LYS   A CD  1 
ATOM   164  C CE  . LYS   A 1 30  ? 5.591   26.621 -14.551 1.00 17.95 ? 52  LYS   A CE  1 
ATOM   165  N NZ  . LYS   A 1 30  ? 6.600   25.574 -14.729 1.00 17.98 ? 52  LYS   A NZ  1 
ATOM   166  N N   . PHE   A 1 31  ? 2.141   28.628 -19.815 1.00 15.67 ? 53  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 31  ? 1.802   28.799 -21.215 1.00 15.81 ? 53  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 31  ? 2.801   28.074 -22.098 1.00 14.95 ? 53  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 31  ? 3.994   28.105 -21.831 1.00 15.34 ? 53  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 31  ? 1.822   30.263 -21.649 1.00 15.60 ? 53  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 31  ? 0.627   31.051 -21.138 1.00 16.83 ? 53  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 31  ? -0.627  30.878 -21.705 1.00 16.66 ? 53  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 31  ? 0.756   31.930 -20.063 1.00 17.57 ? 53  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 31  ? -1.717  31.594 -21.235 1.00 17.36 ? 53  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 31  ? -0.339  32.652 -19.615 1.00 17.75 ? 53  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 31  ? -1.568  32.484 -20.207 1.00 18.15 ? 53  PHE   A CZ  1 
ATOM   177  N N   . SER   A 1 32  ? 2.308   27.464 -23.181 1.00 15.29 ? 54  SER   A N   1 
ATOM   178  C CA  . SER   A 1 32  ? 3.197   26.895 -24.176 1.00 14.83 ? 54  SER   A CA  1 
ATOM   179  C C   . SER   A 1 32  ? 4.053   27.996 -24.794 1.00 15.37 ? 54  SER   A C   1 
ATOM   180  O O   . SER   A 1 32  ? 3.602   29.133 -24.956 1.00 15.74 ? 54  SER   A O   1 
ATOM   181  C CB  . SER   A 1 32  ? 2.448   26.139 -25.228 1.00 14.90 ? 54  SER   A CB  1 
ATOM   182  O OG  . SER   A 1 32  ? 1.536   26.961 -25.941 1.00 14.84 ? 54  SER   A OG  1 
ATOM   183  N N   . PRO   A 1 33  ? 5.314   27.700 -25.180 1.00 16.01 ? 55  PRO   A N   1 
ATOM   184  C CA  . PRO   A 1 33  ? 6.157   28.697 -25.846 1.00 16.31 ? 55  PRO   A CA  1 
ATOM   185  C C   . PRO   A 1 33  ? 5.568   29.336 -27.109 1.00 16.02 ? 55  PRO   A C   1 
ATOM   186  O O   . PRO   A 1 33  ? 5.851   30.500 -27.399 1.00 17.76 ? 55  PRO   A O   1 
ATOM   187  C CB  . PRO   A 1 33  ? 7.427   27.889 -26.135 1.00 16.46 ? 55  PRO   A CB  1 
ATOM   188  C CG  . PRO   A 1 33  ? 7.502   26.914 -24.992 1.00 17.25 ? 55  PRO   A CG  1 
ATOM   189  C CD  . PRO   A 1 33  ? 6.066   26.492 -24.806 1.00 15.75 ? 55  PRO   A CD  1 
ATOM   190  N N   . ASN   A 1 34  ? 4.729   28.577 -27.831 1.00 16.29 ? 56  ASN   A N   1 
ATOM   191  C CA  . ASN   A 1 34  ? 4.113   29.059 -29.053 1.00 16.55 ? 56  ASN   A CA  1 
ATOM   192  C C   . ASN   A 1 34  ? 2.851   29.876 -28.773 1.00 16.72 ? 56  ASN   A C   1 
ATOM   193  O O   . ASN   A 1 34  ? 2.212   30.359 -29.714 1.00 17.33 ? 56  ASN   A O   1 
ATOM   194  C CB  . ASN   A 1 34  ? 3.845   27.938 -30.050 1.00 17.18 ? 56  ASN   A CB  1 
ATOM   195  C CG  . ASN   A 1 34  ? 2.750   27.003 -29.624 1.00 17.09 ? 56  ASN   A CG  1 
ATOM   196  O OD1 . ASN   A 1 34  ? 2.121   27.193 -28.577 1.00 16.61 ? 56  ASN   A OD1 1 
ATOM   197  N ND2 . ASN   A 1 34  ? 2.479   26.016 -30.458 1.00 17.59 ? 56  ASN   A ND2 1 
ATOM   198  N N   . GLY   A 1 35  ? 2.487   30.003 -27.494 1.00 15.84 ? 57  GLY   A N   1 
ATOM   199  C CA  . GLY   A 1 35  ? 1.411   30.871 -27.061 1.00 16.08 ? 57  GLY   A CA  1 
ATOM   200  C C   . GLY   A 1 35  ? 0.025   30.229 -27.133 1.00 15.43 ? 57  GLY   A C   1 
ATOM   201  O O   . GLY   A 1 35  ? -0.930  30.826 -26.663 1.00 16.58 ? 57  GLY   A O   1 
ATOM   202  N N   . GLU   A 1 36  ? -0.095  29.028 -27.715 1.00 15.50 ? 58  GLU   A N   1 
ATOM   203  C CA  . GLU   A 1 36  ? -1.389  28.473 -28.088 1.00 15.96 ? 58  GLU   A CA  1 
ATOM   204  C C   . GLU   A 1 36  ? -2.152  27.944 -26.877 1.00 16.18 ? 58  GLU   A C   1 
ATOM   205  O O   . GLU   A 1 36  ? -3.388  27.988 -26.837 1.00 16.28 ? 58  GLU   A O   1 
ATOM   206  C CB  . GLU   A 1 36  ? -1.117  27.372 -29.109 1.00 17.37 ? 58  GLU   A CB  1 
ATOM   207  C CG  . GLU   A 1 36  ? -2.383  26.757 -29.672 1.00 18.52 ? 58  GLU   A CG  1 
ATOM   208  C CD  . GLU   A 1 36  ? -2.116  25.681 -30.700 1.00 19.98 ? 58  GLU   A CD  1 
ATOM   209  O OE1 . GLU   A 1 36  ? -0.950  25.449 -31.077 1.00 21.79 ? 58  GLU   A OE1 1 
ATOM   210  O OE2 . GLU   A 1 36  ? -3.120  25.058 -31.092 1.00 21.51 ? 58  GLU   A OE2 1 
ATOM   211  N N   . TRP   A 1 37  ? -1.404  27.409 -25.902 1.00 15.54 ? 59  TRP   A N   1 
ATOM   212  C CA  . TRP   A 1 37  ? -1.983  26.573 -24.865 1.00 16.23 ? 59  TRP   A CA  1 
ATOM   213  C C   . TRP   A 1 37  ? -1.588  27.061 -23.474 1.00 15.77 ? 59  TRP   A C   1 
ATOM   214  O O   . TRP   A 1 37  ? -0.524  27.634 -23.273 1.00 15.56 ? 59  TRP   A O   1 
ATOM   215  C CB  . TRP   A 1 37  ? -1.522  25.118 -25.019 1.00 17.50 ? 59  TRP   A CB  1 
ATOM   216  C CG  . TRP   A 1 37  ? -1.873  24.457 -26.329 1.00 19.57 ? 59  TRP   A CG  1 
ATOM   217  C CD1 . TRP   A 1 37  ? -0.990  23.976 -27.248 1.00 20.19 ? 59  TRP   A CD1 1 
ATOM   218  C CD2 . TRP   A 1 37  ? -3.196  24.175 -26.848 1.00 22.51 ? 59  TRP   A CD2 1 
ATOM   219  N NE1 . TRP   A 1 37  ? -1.670  23.438 -28.312 1.00 24.33 ? 59  TRP   A NE1 1 
ATOM   220  C CE2 . TRP   A 1 37  ? -3.019  23.542 -28.097 1.00 24.18 ? 59  TRP   A CE2 1 
ATOM   221  C CE3 . TRP   A 1 37  ? -4.501  24.400 -26.396 1.00 25.03 ? 59  TRP   A CE3 1 
ATOM   222  C CZ2 . TRP   A 1 37  ? -4.093  23.133 -28.891 1.00 27.74 ? 59  TRP   A CZ2 1 
ATOM   223  C CZ3 . TRP   A 1 37  ? -5.569  23.986 -27.175 1.00 27.57 ? 59  TRP   A CZ3 1 
ATOM   224  C CH2 . TRP   A 1 37  ? -5.366  23.358 -28.410 1.00 28.21 ? 59  TRP   A CH2 1 
ATOM   225  N N   . LEU   A 1 38  ? -2.473  26.791 -22.514 1.00 15.67 ? 60  LEU   A N   1 
ATOM   226  C CA  . LEU   A 1 38  ? -2.117  26.767 -21.107 1.00 16.09 ? 60  LEU   A CA  1 
ATOM   227  C C   . LEU   A 1 38  ? -2.161  25.311 -20.647 1.00 16.25 ? 60  LEU   A C   1 
ATOM   228  O O   . LEU   A 1 38  ? -3.152  24.621 -20.907 1.00 16.48 ? 60  LEU   A O   1 
ATOM   229  C CB  . LEU   A 1 38  ? -3.093  27.626 -20.301 1.00 16.69 ? 60  LEU   A CB  1 
ATOM   230  C CG  . LEU   A 1 38  ? -2.734  27.794 -18.823 1.00 17.78 ? 60  LEU   A CG  1 
ATOM   231  C CD1 . LEU   A 1 38  ? -1.614  28.787 -18.709 1.00 18.19 ? 60  LEU   A CD1 1 
ATOM   232  C CD2 . LEU   A 1 38  ? -3.929  28.178 -17.993 1.00 18.40 ? 60  LEU   A CD2 1 
ATOM   233  N N   . ALA   A 1 39  ? -1.105  24.856 -19.951 1.00 15.98 ? 61  ALA   A N   1 
ATOM   234  C CA  . ALA   A 1 39  ? -1.151  23.597 -19.217 1.00 16.05 ? 61  ALA   A CA  1 
ATOM   235  C C   . ALA   A 1 39  ? -1.327  23.876 -17.724 1.00 16.36 ? 61  ALA   A C   1 
ATOM   236  O O   . ALA   A 1 39  ? -0.705  24.798 -17.180 1.00 17.15 ? 61  ALA   A O   1 
ATOM   237  C CB  . ALA   A 1 39  ? 0.104   22.784 -19.471 1.00 15.42 ? 61  ALA   A CB  1 
ATOM   238  N N   . SER   A 1 40  ? -2.181  23.075 -17.075 1.00 16.20 ? 62  SER   A N   1 
ATOM   239  C CA  . SER   A 1 40  ? -2.359  23.119 -15.631 1.00 16.66 ? 62  SER   A CA  1 
ATOM   240  C C   . SER   A 1 40  ? -2.079  21.745 -15.023 1.00 16.19 ? 62  SER   A C   1 
ATOM   241  O O   . SER   A 1 40  ? -2.470  20.719 -15.576 1.00 16.56 ? 62  SER   A O   1 
ATOM   242  C CB  . SER   A 1 40  ? -3.760  23.597 -15.268 1.00 16.69 ? 62  SER   A CB  1 
ATOM   243  O OG  . SER   A 1 40  ? -4.751  22.731 -15.803 1.00 16.48 ? 62  SER   A OG  1 
ATOM   244  N N   . SER   A 1 41  ? -1.438  21.745 -13.855 1.00 16.16 ? 63  SER   A N   1 
ATOM   245  C CA  . SER   A 1 41  ? -1.254  20.553 -13.050 1.00 16.41 ? 63  SER   A CA  1 
ATOM   246  C C   . SER   A 1 41  ? -2.014  20.726 -11.732 1.00 16.90 ? 63  SER   A C   1 
ATOM   247  O O   . SER   A 1 41  ? -2.283  21.843 -11.307 1.00 16.75 ? 63  SER   A O   1 
ATOM   248  C CB  . SER   A 1 41  ? 0.218   20.299 -12.835 1.00 16.42 ? 63  SER   A CB  1 
ATOM   249  O OG  . SER   A 1 41  ? 0.839   21.338 -12.095 1.00 16.52 ? 63  SER   A OG  1 
ATOM   250  N N   . SER   A 1 42  ? -2.321  19.616 -11.057 1.00 17.68 ? 64  SER   A N   1 
ATOM   251  C CA  . SER   A 1 42  ? -3.162  19.657 -9.866  1.00 18.08 ? 64  SER   A CA  1 
ATOM   252  C C   . SER   A 1 42  ? -2.816  18.521 -8.908  1.00 18.16 ? 64  SER   A C   1 
ATOM   253  O O   . SER   A 1 42  ? -2.291  17.494 -9.325  1.00 17.57 ? 64  SER   A O   1 
ATOM   254  C CB  . SER   A 1 42  ? -4.615  19.604 -10.285 1.00 18.13 ? 64  SER   A CB  1 
ATOM   255  O OG  . SER   A 1 42  ? -5.495  19.478 -9.182  1.00 18.96 ? 64  SER   A OG  1 
ATOM   256  N N   . ALA   A 1 43  ? -3.157  18.724 -7.625  1.00 19.16 ? 65  ALA   A N   1 
ATOM   257  C CA  . ALA   A 1 43  ? -3.208  17.660 -6.625  1.00 19.80 ? 65  ALA   A CA  1 
ATOM   258  C C   . ALA   A 1 43  ? -4.112  16.496 -7.047  1.00 19.79 ? 65  ALA   A C   1 
ATOM   259  O O   . ALA   A 1 43  ? -3.990  15.407 -6.485  1.00 20.32 ? 65  ALA   A O   1 
ATOM   260  C CB  . ALA   A 1 43  ? -3.663  18.230 -5.299  1.00 19.39 ? 65  ALA   A CB  1 
ATOM   261  N N   . ASP   A 1 44  ? -4.998  16.710 -8.036  1.00 19.55 ? 66  ASP   A N   1 
ATOM   262  C CA  . ASP   A 1 44  ? -5.931  15.684 -8.499  1.00 18.53 ? 66  ASP   A CA  1 
ATOM   263  C C   . ASP   A 1 44  ? -5.259  14.669 -9.429  1.00 18.81 ? 66  ASP   A C   1 
ATOM   264  O O   . ASP   A 1 44  ? -5.922  13.772 -9.952  1.00 19.23 ? 66  ASP   A O   1 
ATOM   265  C CB  . ASP   A 1 44  ? -7.172  16.296 -9.124  1.00 19.00 ? 66  ASP   A CB  1 
ATOM   266  C CG  . ASP   A 1 44  ? -6.974  16.995 -10.464 1.00 18.98 ? 66  ASP   A CG  1 
ATOM   267  O OD1 . ASP   A 1 44  ? -5.852  16.926 -11.026 1.00 18.44 ? 66  ASP   A OD1 1 
ATOM   268  O OD2 . ASP   A 1 44  ? -7.954  17.588 -10.956 1.00 20.33 ? 66  ASP   A OD2 1 
ATOM   269  N N   . LYS   A 1 45  ? -3.941  14.797 -9.611  1.00 18.77 ? 67  LYS   A N   1 
ATOM   270  C CA  . LYS   A 1 45  ? -3.134  13.825 -10.336 1.00 19.54 ? 67  LYS   A CA  1 
ATOM   271  C C   . LYS   A 1 45  ? -3.243  14.051 -11.845 1.00 19.20 ? 67  LYS   A C   1 
ATOM   272  O O   . LYS   A 1 45  ? -2.751  13.231 -12.627 1.00 18.79 ? 67  LYS   A O   1 
ATOM   273  C CB  . LYS   A 1 45  ? -3.482  12.358 -10.043 1.00 20.76 ? 67  LYS   A CB  1 
ATOM   274  C CG  . LYS   A 1 45  ? -3.692  11.938 -8.602  1.00 22.99 ? 67  LYS   A CG  1 
ATOM   275  C CD  . LYS   A 1 45  ? -4.305  10.545 -8.576  1.00 26.23 ? 67  LYS   A CD  1 
ATOM   276  C CE  . LYS   A 1 45  ? -4.663  10.078 -7.226  1.00 28.70 ? 67  LYS   A CE  1 
ATOM   277  N NZ  . LYS   A 1 45  ? -4.987  8.661  -7.359  1.00 32.59 ? 67  LYS   A NZ  1 
ATOM   278  N N   . LEU   A 1 46  ? -3.874  15.160 -12.260 1.00 19.06 ? 68  LEU   A N   1 
ATOM   279  C CA  . LEU   A 1 46  ? -4.120  15.408 -13.679 1.00 19.13 ? 68  LEU   A CA  1 
ATOM   280  C C   . LEU   A 1 46  ? -3.358  16.626 -14.184 1.00 18.37 ? 68  LEU   A C   1 
ATOM   281  O O   . LEU   A 1 46  ? -3.155  17.601 -13.462 1.00 17.36 ? 68  LEU   A O   1 
ATOM   282  C CB  . LEU   A 1 46  ? -5.605  15.603 -13.989 1.00 20.00 ? 68  LEU   A CB  1 
ATOM   283  C CG  . LEU   A 1 46  ? -6.547  14.520 -13.465 1.00 21.32 ? 68  LEU   A CG  1 
ATOM   284  C CD1 . LEU   A 1 46  ? -7.974  14.947 -13.729 1.00 22.87 ? 68  LEU   A CD1 1 
ATOM   285  C CD2 . LEU   A 1 46  ? -6.272  13.159 -14.063 1.00 22.78 ? 68  LEU   A CD2 1 
ATOM   286  N N   . ILE   A 1 47  ? -3.050  16.568 -15.487 1.00 17.94 ? 69  ILE   A N   1 
ATOM   287  C CA  . ILE   A 1 47  ? -2.709  17.732 -16.286 1.00 17.80 ? 69  ILE   A CA  1 
ATOM   288  C C   . ILE   A 1 47  ? -3.892  18.052 -17.195 1.00 16.98 ? 69  ILE   A C   1 
ATOM   289  O O   . ILE   A 1 47  ? -4.463  17.157 -17.812 1.00 16.26 ? 69  ILE   A O   1 
ATOM   290  C CB  . ILE   A 1 47  ? -1.450  17.446 -17.118 1.00 18.61 ? 69  ILE   A CB  1 
ATOM   291  C CG1 . ILE   A 1 47  ? -0.230  17.146 -16.250 1.00 20.86 ? 69  ILE   A CG1 1 
ATOM   292  C CG2 . ILE   A 1 47  ? -1.186  18.586 -18.101 1.00 18.90 ? 69  ILE   A CG2 1 
ATOM   293  C CD1 . ILE   A 1 47  ? 0.904   16.494 -17.011 1.00 22.48 ? 69  ILE   A CD1 1 
ATOM   294  N N   . LYS   A 1 48  ? -4.241  19.333 -17.304 1.00 16.34 ? 70  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 48  ? -5.231  19.757 -18.276 1.00 17.15 ? 70  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 48  ? -4.635  20.805 -19.211 1.00 17.47 ? 70  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 48  ? -3.795  21.623 -18.806 1.00 16.93 ? 70  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 48  ? -6.503  20.242 -17.574 1.00 17.85 ? 70  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 48  ? -7.289  19.112 -16.907 1.00 19.17 ? 70  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 48  ? -8.458  19.561 -16.041 1.00 20.16 ? 70  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 48  ? -9.107  18.417 -15.319 1.00 20.02 ? 70  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 48  ? -9.889  17.610 -16.251 1.00 21.79 ? 70  LYS   A NZ  1 
ATOM   303  N N   . ILE   A 1 49  ? -5.082  20.738 -20.476 1.00 17.12 ? 71  ILE   A N   1 
ATOM   304  C CA  . ILE   A 1 49  ? -4.656  21.632 -21.537 1.00 17.48 ? 71  ILE   A CA  1 
ATOM   305  C C   . ILE   A 1 49  ? -5.849  22.473 -21.947 1.00 16.54 ? 71  ILE   A C   1 
ATOM   306  O O   . ILE   A 1 49  ? -6.927  21.915 -22.167 1.00 17.18 ? 71  ILE   A O   1 
ATOM   307  C CB  . ILE   A 1 49  ? -4.140  20.849 -22.757 1.00 18.32 ? 71  ILE   A CB  1 
ATOM   308  C CG1 . ILE   A 1 49  ? -3.047  19.868 -22.372 1.00 18.83 ? 71  ILE   A CG1 1 
ATOM   309  C CG2 . ILE   A 1 49  ? -3.690  21.811 -23.853 1.00 19.74 ? 71  ILE   A CG2 1 
ATOM   310  C CD1 . ILE   A 1 49  ? -1.873  20.516 -21.661 1.00 19.01 ? 71  ILE   A CD1 1 
ATOM   311  N N   . TRP   A 1 50  ? -5.616  23.784 -22.055 1.00 16.34 ? 72  TRP   A N   1 
ATOM   312  C CA  . TRP   A 1 50  ? -6.653  24.763 -22.335 1.00 16.99 ? 72  TRP   A CA  1 
ATOM   313  C C   . TRP   A 1 50  ? -6.180  25.722 -23.426 1.00 16.82 ? 72  TRP   A C   1 
ATOM   314  O O   . TRP   A 1 50  ? -5.013  26.055 -23.468 1.00 17.20 ? 72  TRP   A O   1 
ATOM   315  C CB  . TRP   A 1 50  ? -6.959  25.581 -21.072 1.00 17.07 ? 72  TRP   A CB  1 
ATOM   316  C CG  . TRP   A 1 50  ? -7.041  24.809 -19.784 1.00 17.36 ? 72  TRP   A CG  1 
ATOM   317  C CD1 . TRP   A 1 50  ? -6.006  24.417 -18.981 1.00 17.85 ? 72  TRP   A CD1 1 
ATOM   318  C CD2 . TRP   A 1 50  ? -8.247  24.445 -19.089 1.00 18.41 ? 72  TRP   A CD2 1 
ATOM   319  N NE1 . TRP   A 1 50  ? -6.481  23.793 -17.864 1.00 18.11 ? 72  TRP   A NE1 1 
ATOM   320  C CE2 . TRP   A 1 50  ? -7.849  23.786 -17.903 1.00 18.27 ? 72  TRP   A CE2 1 
ATOM   321  C CE3 . TRP   A 1 50  ? -9.610  24.585 -19.368 1.00 18.87 ? 72  TRP   A CE3 1 
ATOM   322  C CZ2 . TRP   A 1 50  ? -8.767  23.285 -16.989 1.00 19.40 ? 72  TRP   A CZ2 1 
ATOM   323  C CZ3 . TRP   A 1 50  ? -10.512 24.111 -18.442 1.00 19.71 ? 72  TRP   A CZ3 1 
ATOM   324  C CH2 . TRP   A 1 50  ? -10.096 23.473 -17.271 1.00 19.52 ? 72  TRP   A CH2 1 
ATOM   325  N N   . GLY   A 1 51  ? -7.099  26.207 -24.273 1.00 17.65 ? 73  GLY   A N   1 
ATOM   326  C CA  . GLY   A 1 51  ? -6.755  27.229 -25.251 1.00 17.39 ? 73  GLY   A CA  1 
ATOM   327  C C   . GLY   A 1 51  ? -6.433  28.551 -24.552 1.00 16.94 ? 73  GLY   A C   1 
ATOM   328  O O   . GLY   A 1 51  ? -7.213  29.005 -23.710 1.00 16.08 ? 73  GLY   A O   1 
ATOM   329  N N   . ALA   A 1 52  ? -5.297  29.174 -24.911 1.00 16.00 ? 74  ALA   A N   1 
ATOM   330  C CA  . ALA   A 1 52  ? -4.832  30.373 -24.225 1.00 16.59 ? 74  ALA   A CA  1 
ATOM   331  C C   . ALA   A 1 52  ? -5.732  31.586 -24.479 1.00 17.01 ? 74  ALA   A C   1 
ATOM   332  O O   . ALA   A 1 52  ? -5.743  32.531 -23.672 1.00 17.77 ? 74  ALA   A O   1 
ATOM   333  C CB  . ALA   A 1 52  ? -3.413  30.689 -24.637 1.00 16.91 ? 74  ALA   A CB  1 
ATOM   334  N N   . TYR   A 1 53  ? -6.415  31.608 -25.627 1.00 16.63 ? 75  TYR   A N   1 
ATOM   335  C CA  . TYR   A 1 53  ? -7.087  32.813 -26.091 1.00 16.69 ? 75  TYR   A CA  1 
ATOM   336  C C   . TYR   A 1 53  ? -8.605  32.735 -25.922 1.00 17.38 ? 75  TYR   A C   1 
ATOM   337  O O   . TYR   A 1 53  ? -9.264  33.776 -25.810 1.00 18.18 ? 75  TYR   A O   1 
ATOM   338  C CB  . TYR   A 1 53  ? -6.711  33.059 -27.553 1.00 16.75 ? 75  TYR   A CB  1 
ATOM   339  C CG  . TYR   A 1 53  ? -5.208  33.102 -27.780 1.00 16.01 ? 75  TYR   A CG  1 
ATOM   340  C CD1 . TYR   A 1 53  ? -4.412  34.072 -27.171 1.00 16.00 ? 75  TYR   A CD1 1 
ATOM   341  C CD2 . TYR   A 1 53  ? -4.582  32.178 -28.603 1.00 16.28 ? 75  TYR   A CD2 1 
ATOM   342  C CE1 . TYR   A 1 53  ? -3.043  34.102 -27.362 1.00 16.44 ? 75  TYR   A CE1 1 
ATOM   343  C CE2 . TYR   A 1 53  ? -3.221  32.229 -28.839 1.00 16.49 ? 75  TYR   A CE2 1 
ATOM   344  C CZ  . TYR   A 1 53  ? -2.448  33.191 -28.220 1.00 15.85 ? 75  TYR   A CZ  1 
ATOM   345  O OH  . TYR   A 1 53  ? -1.101  33.214 -28.456 1.00 16.37 ? 75  TYR   A OH  1 
ATOM   346  N N   . ASP   A 1 54  ? -9.156  31.516 -25.952 1.00 17.46 ? 76  ASP   A N   1 
ATOM   347  C CA  . ASP   A 1 54  ? -10.583 31.297 -25.783 1.00 18.52 ? 76  ASP   A CA  1 
ATOM   348  C C   . ASP   A 1 54  ? -10.897 30.535 -24.502 1.00 18.56 ? 76  ASP   A C   1 
ATOM   349  O O   . ASP   A 1 54  ? -12.063 30.276 -24.233 1.00 20.55 ? 76  ASP   A O   1 
ATOM   350  C CB  . ASP   A 1 54  ? -11.172 30.557 -26.971 1.00 18.34 ? 76  ASP   A CB  1 
ATOM   351  C CG  . ASP   A 1 54  ? -10.578 29.186 -27.277 1.00 19.02 ? 76  ASP   A CG  1 
ATOM   352  O OD1 . ASP   A 1 54  ? -9.749  28.683 -26.477 1.00 19.22 ? 76  ASP   A OD1 1 
ATOM   353  O OD2 . ASP   A 1 54  ? -10.970 28.618 -28.307 1.00 20.55 ? 76  ASP   A OD2 1 
ATOM   354  N N   . GLY   A 1 55  ? -9.863  30.126 -23.753 1.00 18.89 ? 77  GLY   A N   1 
ATOM   355  C CA  . GLY   A 1 55  ? -10.030 29.395 -22.501 1.00 19.41 ? 77  GLY   A CA  1 
ATOM   356  C C   . GLY   A 1 55  ? -10.636 27.995 -22.665 1.00 19.40 ? 77  GLY   A C   1 
ATOM   357  O O   . GLY   A 1 55  ? -11.006 27.367 -21.679 1.00 20.69 ? 77  GLY   A O   1 
ATOM   358  N N   . LYS   A 1 56  ? -10.705 27.468 -23.890 1.00 19.78 ? 78  LYS   A N   1 
ATOM   359  C CA  . LYS   A 1 56  ? -11.473 26.250 -24.132 1.00 19.55 ? 78  LYS   A CA  1 
ATOM   360  C C   . LYS   A 1 56  ? -10.700 25.022 -23.650 1.00 19.59 ? 78  LYS   A C   1 
ATOM   361  O O   . LYS   A 1 56  ? -9.549  24.797 -24.017 1.00 19.97 ? 78  LYS   A O   1 
ATOM   362  C CB  . LYS   A 1 56  ? -11.795 26.104 -25.621 1.00 21.39 ? 78  LYS   A CB  1 
ATOM   363  C CG  . LYS   A 1 56  ? -12.626 24.898 -26.016 1.00 24.36 ? 78  LYS   A CG  1 
ATOM   364  C CD  . LYS   A 1 56  ? -12.931 24.808 -27.510 1.00 27.14 ? 78  LYS   A CD  1 
ATOM   365  C CE  . LYS   A 1 56  ? -13.136 23.398 -27.982 1.00 32.76 ? 78  LYS   A CE  1 
ATOM   366  N N   . PHE   A 1 57  ? -11.358 24.197 -22.847 1.00 19.83 ? 79  PHE   A N   1 
ATOM   367  C CA  . PHE   A 1 57  ? -10.768 22.943 -22.421 1.00 20.43 ? 79  PHE   A CA  1 
ATOM   368  C C   . PHE   A 1 57  ? -10.474 22.078 -23.647 1.00 21.45 ? 79  PHE   A C   1 
ATOM   369  O O   . PHE   A 1 57  ? -11.331 21.892 -24.519 1.00 22.37 ? 79  PHE   A O   1 
ATOM   370  C CB  . PHE   A 1 57  ? -11.706 22.217 -21.454 1.00 20.23 ? 79  PHE   A CB  1 
ATOM   371  C CG  . PHE   A 1 57  ? -11.255 20.795 -21.167 1.00 21.16 ? 79  PHE   A CG  1 
ATOM   372  C CD1 . PHE   A 1 57  ? -10.176 20.554 -20.321 1.00 19.34 ? 79  PHE   A CD1 1 
ATOM   373  C CD2 . PHE   A 1 57  ? -11.884 19.714 -21.781 1.00 22.35 ? 79  PHE   A CD2 1 
ATOM   374  C CE1 . PHE   A 1 57  ? -9.749  19.259 -20.092 1.00 20.23 ? 79  PHE   A CE1 1 
ATOM   375  C CE2 . PHE   A 1 57  ? -11.440 18.424 -21.559 1.00 22.84 ? 79  PHE   A CE2 1 
ATOM   376  C CZ  . PHE   A 1 57  ? -10.390 18.198 -20.699 1.00 22.12 ? 79  PHE   A CZ  1 
ATOM   377  N N   . GLU   A 1 58  ? -9.248  21.536 -23.688 1.00 20.26 ? 80  GLU   A N   1 
ATOM   378  C CA  . GLU   A 1 58  ? -8.796  20.729 -24.804 1.00 21.35 ? 80  GLU   A CA  1 
ATOM   379  C C   . GLU   A 1 58  ? -8.729  19.253 -24.410 1.00 19.70 ? 80  GLU   A C   1 
ATOM   380  O O   . GLU   A 1 58  ? -9.321  18.417 -25.078 1.00 20.11 ? 80  GLU   A O   1 
ATOM   381  C CB  . GLU   A 1 58  ? -7.430  21.183 -25.304 1.00 22.73 ? 80  GLU   A CB  1 
ATOM   382  C CG  . GLU   A 1 58  ? -6.948  20.367 -26.500 1.00 27.61 ? 80  GLU   A CG  1 
ATOM   383  C CD  . GLU   A 1 58  ? -7.678  20.684 -27.786 1.00 30.24 ? 80  GLU   A CD  1 
ATOM   384  O OE1 . GLU   A 1 58  ? -8.484  21.651 -27.806 1.00 30.68 ? 80  GLU   A OE1 1 
ATOM   385  O OE2 . GLU   A 1 58  ? -7.425  19.957 -28.775 1.00 35.14 ? 80  GLU   A OE2 1 
ATOM   386  N N   . LYS   A 1 59  ? -7.974  18.918 -23.358 1.00 19.32 ? 81  LYS   A N   1 
ATOM   387  C CA  . LYS   A 1 59  ? -7.833  17.510 -22.985 1.00 19.74 ? 81  LYS   A CA  1 
ATOM   388  C C   . LYS   A 1 59  ? -7.247  17.355 -21.589 1.00 19.43 ? 81  LYS   A C   1 
ATOM   389  O O   . LYS   A 1 59  ? -6.695  18.299 -21.022 1.00 18.53 ? 81  LYS   A O   1 
ATOM   390  C CB  . LYS   A 1 59  ? -6.930  16.724 -23.940 1.00 21.38 ? 81  LYS   A CB  1 
ATOM   391  C CG  . LYS   A 1 59  ? -5.472  17.137 -23.911 1.00 22.56 ? 81  LYS   A CG  1 
ATOM   392  C CD  . LYS   A 1 59  ? -4.579  16.334 -24.850 1.00 25.31 ? 81  LYS   A CD  1 
ATOM   393  C CE  . LYS   A 1 59  ? -4.760  16.717 -26.278 1.00 27.64 ? 81  LYS   A CE  1 
ATOM   394  N NZ  . LYS   A 1 59  ? -3.931  15.861 -27.118 1.00 28.65 ? 81  LYS   A NZ  1 
ATOM   395  N N   . THR   A 1 60  ? -7.444  16.146 -21.044 1.00 19.41 ? 82  THR   A N   1 
ATOM   396  C CA  . THR   A 1 60  ? -6.848  15.731 -19.787 1.00 19.88 ? 82  THR   A CA  1 
ATOM   397  C C   . THR   A 1 60  ? -5.756  14.713 -20.087 1.00 19.66 ? 82  THR   A C   1 
ATOM   398  O O   . THR   A 1 60  ? -5.924  13.833 -20.930 1.00 21.91 ? 82  THR   A O   1 
ATOM   399  C CB  . THR   A 1 60  ? -7.903  15.129 -18.866 1.00 20.76 ? 82  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 60  ? -8.856  16.156 -18.619 1.00 20.81 ? 82  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 60  ? -7.310  14.654 -17.550 1.00 21.61 ? 82  THR   A CG2 1 
ATOM   402  N N   . ILE   A 1 61  ? -4.654  14.840 -19.360 1.00 18.92 ? 83  ILE   A N   1 
ATOM   403  C CA  . ILE   A 1 61  ? -3.513  13.948 -19.470 1.00 19.89 ? 83  ILE   A CA  1 
ATOM   404  C C   . ILE   A 1 61  ? -3.328  13.306 -18.097 1.00 19.84 ? 83  ILE   A C   1 
ATOM   405  O O   . ILE   A 1 61  ? -3.206  14.013 -17.092 1.00 20.44 ? 83  ILE   A O   1 
ATOM   406  C CB  . ILE   A 1 61  ? -2.267  14.714 -19.972 1.00 19.76 ? 83  ILE   A CB  1 
ATOM   407  C CG1 . ILE   A 1 61  ? -2.464  15.226 -21.413 1.00 20.06 ? 83  ILE   A CG1 1 
ATOM   408  C CG2 . ILE   A 1 61  ? -1.009  13.853 -19.871 1.00 20.87 ? 83  ILE   A CG2 1 
ATOM   409  C CD1 . ILE   A 1 61  ? -1.307  16.052 -21.943 1.00 20.34 ? 83  ILE   A CD1 1 
ATOM   410  N N   A SER   A 1 62  ? -3.302  11.971 -18.064 0.70 20.62 ? 84  SER   A N   1 
ATOM   411  N N   B SER   A 1 62  ? -3.367  11.964 -18.062 0.30 20.29 ? 84  SER   A N   1 
ATOM   412  C CA  A SER   A 1 62  ? -3.352  11.249 -16.803 0.70 20.69 ? 84  SER   A CA  1 
ATOM   413  C CA  B SER   A 1 62  ? -3.404  11.203 -16.819 0.30 20.23 ? 84  SER   A CA  1 
ATOM   414  C C   A SER   A 1 62  ? -2.327  10.122 -16.801 0.70 19.83 ? 84  SER   A C   1 
ATOM   415  C C   B SER   A 1 62  ? -2.290  10.162 -16.804 0.30 19.64 ? 84  SER   A C   1 
ATOM   416  O O   A SER   A 1 62  ? -1.956  9.610  -17.858 0.70 19.90 ? 84  SER   A O   1 
ATOM   417  O O   B SER   A 1 62  ? -1.821  9.741  -17.860 0.30 19.64 ? 84  SER   A O   1 
ATOM   418  C CB  A SER   A 1 62  ? -4.730  10.712 -16.561 0.70 21.28 ? 84  SER   A CB  1 
ATOM   419  C CB  B SER   A 1 62  ? -4.730  10.507 -16.636 0.30 20.48 ? 84  SER   A CB  1 
ATOM   420  O OG  A SER   A 1 62  ? -5.104  9.831  -17.613 0.70 21.56 ? 84  SER   A OG  1 
ATOM   421  O OG  B SER   A 1 62  ? -5.827  11.366 -16.907 0.30 20.82 ? 84  SER   A OG  1 
ATOM   422  N N   . GLY   A 1 63  ? -1.912  9.719  -15.597 1.00 19.60 ? 85  GLY   A N   1 
ATOM   423  C CA  . GLY   A 1 63  ? -1.003  8.596  -15.447 1.00 20.51 ? 85  GLY   A CA  1 
ATOM   424  C C   . GLY   A 1 63  ? -0.251  8.603  -14.120 1.00 20.40 ? 85  GLY   A C   1 
ATOM   425  O O   . GLY   A 1 63  ? 0.084   7.538  -13.612 1.00 22.83 ? 85  GLY   A O   1 
ATOM   426  N N   . HIS   A 1 64  ? 0.024   9.784  -13.558 1.00 20.13 ? 86  HIS   A N   1 
ATOM   427  C CA  . HIS   A 1 64  ? 0.604   9.831  -12.227 1.00 19.74 ? 86  HIS   A CA  1 
ATOM   428  C C   . HIS   A 1 64  ? -0.330  9.173  -11.215 1.00 21.44 ? 86  HIS   A C   1 
ATOM   429  O O   . HIS   A 1 64  ? -1.552  9.291  -11.317 1.00 22.39 ? 86  HIS   A O   1 
ATOM   430  C CB  . HIS   A 1 64  ? 0.935   11.254 -11.786 1.00 18.73 ? 86  HIS   A CB  1 
ATOM   431  C CG  . HIS   A 1 64  ? 2.184   11.799 -12.385 1.00 18.64 ? 86  HIS   A CG  1 
ATOM   432  N ND1 . HIS   A 1 64  ? 3.413   11.239 -12.106 1.00 18.41 ? 86  HIS   A ND1 1 
ATOM   433  C CD2 . HIS   A 1 64  ? 2.408   12.779 -13.272 1.00 18.24 ? 86  HIS   A CD2 1 
ATOM   434  C CE1 . HIS   A 1 64  ? 4.353   11.917 -12.753 1.00 18.48 ? 86  HIS   A CE1 1 
ATOM   435  N NE2 . HIS   A 1 64  ? 3.769   12.849 -13.480 1.00 18.16 ? 86  HIS   A NE2 1 
ATOM   436  N N   . LYS   A 1 65  ? 0.291   8.530  -10.218 1.00 22.83 ? 87  LYS   A N   1 
ATOM   437  C CA  . LYS   A 1 65  ? -0.412  7.795  -9.176  1.00 24.45 ? 87  LYS   A CA  1 
ATOM   438  C C   . LYS   A 1 65  ? -0.751  8.704  -7.998  1.00 22.56 ? 87  LYS   A C   1 
ATOM   439  O O   . LYS   A 1 65  ? -1.618  8.368  -7.184  1.00 22.97 ? 87  LYS   A O   1 
ATOM   440  C CB  . LYS   A 1 65  ? 0.455   6.624  -8.684  1.00 28.55 ? 87  LYS   A CB  1 
ATOM   441  C CG  . LYS   A 1 65  ? 0.681   5.471  -9.664  1.00 31.82 ? 87  LYS   A CG  1 
ATOM   442  C CD  . LYS   A 1 65  ? 1.831   4.554  -9.247  1.00 33.58 ? 87  LYS   A CD  1 
ATOM   443  N N   . LEU   A 1 66  ? -0.017  9.817  -7.874  1.00 20.65 ? 88  LEU   A N   1 
ATOM   444  C CA  . LEU   A 1 66  ? -0.260  10.812 -6.845  1.00 20.83 ? 88  LEU   A CA  1 
ATOM   445  C C   . LEU   A 1 66  ? -0.258  12.198 -7.487  1.00 19.98 ? 88  LEU   A C   1 
ATOM   446  O O   . LEU   A 1 66  ? -0.085  12.328 -8.698  1.00 21.02 ? 88  LEU   A O   1 
ATOM   447  C CB  . LEU   A 1 66  ? 0.780   10.698 -5.730  1.00 21.44 ? 88  LEU   A CB  1 
ATOM   448  C CG  . LEU   A 1 66  ? 0.747   9.407  -4.911  1.00 21.37 ? 88  LEU   A CG  1 
ATOM   449  C CD1 . LEU   A 1 66  ? 2.012   9.292  -4.048  1.00 22.36 ? 88  LEU   A CD1 1 
ATOM   450  C CD2 . LEU   A 1 66  ? -0.530  9.326  -4.066  1.00 21.36 ? 88  LEU   A CD2 1 
ATOM   451  N N   . GLY   A 1 67  ? -0.515  13.218 -6.667  1.00 18.71 ? 89  GLY   A N   1 
ATOM   452  C CA  . GLY   A 1 67  ? -0.643  14.591 -7.127  1.00 18.67 ? 89  GLY   A CA  1 
ATOM   453  C C   . GLY   A 1 67  ? 0.603   15.118 -7.834  1.00 18.69 ? 89  GLY   A C   1 
ATOM   454  O O   . GLY   A 1 67  ? 1.711   14.610 -7.654  1.00 18.88 ? 89  GLY   A O   1 
ATOM   455  N N   . ILE   A 1 68  ? 0.383   16.159 -8.638  1.00 17.94 ? 90  ILE   A N   1 
ATOM   456  C CA  . ILE   A 1 68  ? 1.429   16.796 -9.424  1.00 17.84 ? 90  ILE   A CA  1 
ATOM   457  C C   . ILE   A 1 68  ? 1.641   18.199 -8.867  1.00 17.74 ? 90  ILE   A C   1 
ATOM   458  O O   . ILE   A 1 68  ? 0.655   18.925 -8.692  1.00 18.02 ? 90  ILE   A O   1 
ATOM   459  C CB  . ILE   A 1 68  ? 1.022   16.856 -10.906 1.00 17.93 ? 90  ILE   A CB  1 
ATOM   460  C CG1 . ILE   A 1 68  ? 0.660   15.476 -11.460 1.00 18.44 ? 90  ILE   A CG1 1 
ATOM   461  C CG2 . ILE   A 1 68  ? 2.095   17.565 -11.747 1.00 18.59 ? 90  ILE   A CG2 1 
ATOM   462  C CD1 . ILE   A 1 68  ? 0.020   15.509 -12.846 1.00 19.37 ? 90  ILE   A CD1 1 
ATOM   463  N N   . SER   A 1 69  ? 2.910   18.565 -8.637  1.00 17.15 ? 91  SER   A N   1 
ATOM   464  C CA  . SER   A 1 69  ? 3.273   19.879 -8.120  1.00 17.47 ? 91  SER   A CA  1 
ATOM   465  C C   . SER   A 1 69  ? 3.585   20.866 -9.245  1.00 17.04 ? 91  SER   A C   1 
ATOM   466  O O   . SER   A 1 69  ? 3.486   22.077 -9.043  1.00 17.15 ? 91  SER   A O   1 
ATOM   467  C CB  . SER   A 1 69  ? 4.453   19.782 -7.186  1.00 19.09 ? 91  SER   A CB  1 
ATOM   468  O OG  . SER   A 1 69  ? 4.130   19.126 -5.960  1.00 20.58 ? 91  SER   A OG  1 
ATOM   469  N N   . ASP   A 1 70  ? 4.031   20.381 -10.407 1.00 16.56 ? 92  ASP   A N   1 
ATOM   470  C CA  . ASP   A 1 70  ? 4.558   21.281 -11.427 1.00 16.76 ? 92  ASP   A CA  1 
ATOM   471  C C   . ASP   A 1 70  ? 4.532   20.588 -12.784 1.00 16.20 ? 92  ASP   A C   1 
ATOM   472  O O   . ASP   A 1 70  ? 4.499   19.355 -12.878 1.00 15.82 ? 92  ASP   A O   1 
ATOM   473  C CB  . ASP   A 1 70  ? 5.970   21.741 -11.053 1.00 17.49 ? 92  ASP   A CB  1 
ATOM   474  C CG  . ASP   A 1 70  ? 6.528   22.991 -11.734 1.00 18.45 ? 92  ASP   A CG  1 
ATOM   475  O OD1 . ASP   A 1 70  ? 5.731   23.731 -12.364 1.00 18.85 ? 92  ASP   A OD1 1 
ATOM   476  O OD2 . ASP   A 1 70  ? 7.755   23.247 -11.581 1.00 18.23 ? 92  ASP   A OD2 1 
ATOM   477  N N   . VAL   A 1 71  ? 4.506   21.416 -13.823 1.00 16.58 ? 93  VAL   A N   1 
ATOM   478  C CA  . VAL   A 1 71  ? 4.545   20.981 -15.205 1.00 17.32 ? 93  VAL   A CA  1 
ATOM   479  C C   . VAL   A 1 71  ? 5.335   22.029 -15.989 1.00 16.54 ? 93  VAL   A C   1 
ATOM   480  O O   . VAL   A 1 71  ? 5.403   23.185 -15.576 1.00 16.37 ? 93  VAL   A O   1 
ATOM   481  C CB  . VAL   A 1 71  ? 3.089   20.837 -15.703 1.00 18.71 ? 93  VAL   A CB  1 
ATOM   482  C CG1 . VAL   A 1 71  ? 2.376   22.180 -15.727 1.00 19.20 ? 93  VAL   A CG1 1 
ATOM   483  C CG2 . VAL   A 1 71  ? 2.987   20.170 -17.067 1.00 19.94 ? 93  VAL   A CG2 1 
ATOM   484  N N   . ALA   A 1 72  ? 5.936   21.618 -17.111 1.00 15.89 ? 94  ALA   A N   1 
ATOM   485  C CA  . ALA   A 1 72  ? 6.753   22.507 -17.931 1.00 15.60 ? 94  ALA   A CA  1 
ATOM   486  C C   . ALA   A 1 72  ? 6.740   22.009 -19.363 1.00 14.87 ? 94  ALA   A C   1 
ATOM   487  O O   . ALA   A 1 72  ? 6.637   20.812 -19.574 1.00 14.43 ? 94  ALA   A O   1 
ATOM   488  C CB  . ALA   A 1 72  ? 8.183   22.585 -17.413 1.00 15.24 ? 94  ALA   A CB  1 
ATOM   489  N N   . TRP   A 1 73  ? 6.878   22.951 -20.305 1.00 15.31 ? 95  TRP   A N   1 
ATOM   490  C CA  . TRP   A 1 73  ? 6.810   22.690 -21.730 1.00 15.27 ? 95  TRP   A CA  1 
ATOM   491  C C   . TRP   A 1 73  ? 8.196   22.632 -22.353 1.00 15.59 ? 95  TRP   A C   1 
ATOM   492  O O   . TRP   A 1 73  ? 9.094   23.394 -21.981 1.00 16.41 ? 95  TRP   A O   1 
ATOM   493  C CB  . TRP   A 1 73  ? 6.086   23.840 -22.431 1.00 15.12 ? 95  TRP   A CB  1 
ATOM   494  C CG  . TRP   A 1 73  ? 4.629   24.014 -22.125 1.00 15.01 ? 95  TRP   A CG  1 
ATOM   495  C CD1 . TRP   A 1 73  ? 4.061   24.772 -21.140 1.00 16.00 ? 95  TRP   A CD1 1 
ATOM   496  C CD2 . TRP   A 1 73  ? 3.541   23.495 -22.920 1.00 15.18 ? 95  TRP   A CD2 1 
ATOM   497  N NE1 . TRP   A 1 73  ? 2.691   24.732 -21.243 1.00 15.69 ? 95  TRP   A NE1 1 
ATOM   498  C CE2 . TRP   A 1 73  ? 2.343   23.956 -22.324 1.00 15.42 ? 95  TRP   A CE2 1 
ATOM   499  C CE3 . TRP   A 1 73  ? 3.461   22.677 -24.052 1.00 15.32 ? 95  TRP   A CE3 1 
ATOM   500  C CZ2 . TRP   A 1 73  ? 1.091   23.616 -22.825 1.00 15.98 ? 95  TRP   A CZ2 1 
ATOM   501  C CZ3 . TRP   A 1 73  ? 2.213   22.344 -24.550 1.00 16.23 ? 95  TRP   A CZ3 1 
ATOM   502  C CH2 . TRP   A 1 73  ? 1.044   22.802 -23.939 1.00 15.44 ? 95  TRP   A CH2 1 
ATOM   503  N N   . SER   A 1 74  ? 8.315   21.814 -23.403 1.00 16.56 ? 96  SER   A N   1 
ATOM   504  C CA  . SER   A 1 74  ? 9.471   21.870 -24.274 1.00 16.71 ? 96  SER   A CA  1 
ATOM   505  C C   . SER   A 1 74  ? 9.381   23.102 -25.172 1.00 18.27 ? 96  SER   A C   1 
ATOM   506  O O   . SER   A 1 74  ? 8.312   23.680 -25.390 1.00 18.53 ? 96  SER   A O   1 
ATOM   507  C CB  . SER   A 1 74  ? 9.596   20.616 -25.108 1.00 17.14 ? 96  SER   A CB  1 
ATOM   508  O OG  . SER   A 1 74  ? 8.469   20.490 -25.969 1.00 16.55 ? 96  SER   A OG  1 
ATOM   509  N N   . SER   A 1 75  ? 10.526  23.472 -25.737 1.00 18.84 ? 97  SER   A N   1 
ATOM   510  C CA  . SER   A 1 75  ? 10.626  24.691 -26.533 1.00 20.11 ? 97  SER   A CA  1 
ATOM   511  C C   . SER   A 1 75  ? 9.716   24.672 -27.755 1.00 19.77 ? 97  SER   A C   1 
ATOM   512  O O   . SER   A 1 75  ? 9.256   25.730 -28.181 1.00 21.69 ? 97  SER   A O   1 
ATOM   513  C CB  . SER   A 1 75  ? 12.047  24.950 -26.942 1.00 20.67 ? 97  SER   A CB  1 
ATOM   514  O OG  . SER   A 1 75  ? 12.806  25.317 -25.802 1.00 23.45 ? 97  SER   A OG  1 
ATOM   515  N N   . ASP   A 1 76  ? 9.474   23.485 -28.320 1.00 19.30 ? 98  ASP   A N   1 
ATOM   516  C CA  . ASP   A 1 76  ? 8.674   23.358 -29.529 1.00 19.14 ? 98  ASP   A CA  1 
ATOM   517  C C   . ASP   A 1 76  ? 7.191   23.186 -29.204 1.00 18.42 ? 98  ASP   A C   1 
ATOM   518  O O   . ASP   A 1 76  ? 6.386   22.953 -30.108 1.00 18.52 ? 98  ASP   A O   1 
ATOM   519  C CB  . ASP   A 1 76  ? 9.186   22.202 -30.367 1.00 21.06 ? 98  ASP   A CB  1 
ATOM   520  C CG  . ASP   A 1 76  ? 8.963   20.816 -29.784 1.00 21.21 ? 98  ASP   A CG  1 
ATOM   521  O OD1 . ASP   A 1 76  ? 8.469   20.715 -28.637 1.00 21.14 ? 98  ASP   A OD1 1 
ATOM   522  O OD2 . ASP   A 1 76  ? 9.244   19.839 -30.517 1.00 23.38 ? 98  ASP   A OD2 1 
ATOM   523  N N   . SER   A 1 77  ? 6.844   23.256 -27.916 1.00 17.36 ? 99  SER   A N   1 
ATOM   524  C CA  . SER   A 1 77  ? 5.466   23.171 -27.456 1.00 17.55 ? 99  SER   A CA  1 
ATOM   525  C C   . SER   A 1 77  ? 4.852   21.792 -27.695 1.00 18.18 ? 99  SER   A C   1 
ATOM   526  O O   . SER   A 1 77  ? 3.627   21.659 -27.575 1.00 18.72 ? 99  SER   A O   1 
ATOM   527  C CB  . SER   A 1 77  ? 4.585   24.227 -28.061 1.00 17.53 ? 99  SER   A CB  1 
ATOM   528  O OG  . SER   A 1 77  ? 5.095   25.529 -27.866 1.00 19.42 ? 99  SER   A OG  1 
ATOM   529  N N   . ASN   A 1 78  ? 5.681   20.767 -27.964 1.00 18.04 ? 100 ASN   A N   1 
ATOM   530  C CA  . ASN   A 1 78  ? 5.174   19.435 -28.265 1.00 18.87 ? 100 ASN   A CA  1 
ATOM   531  C C   . ASN   A 1 78  ? 5.215   18.476 -27.073 1.00 18.57 ? 100 ASN   A C   1 
ATOM   532  O O   . ASN   A 1 78  ? 4.463   17.497 -27.070 1.00 18.67 ? 100 ASN   A O   1 
ATOM   533  C CB  . ASN   A 1 78  ? 5.917   18.767 -29.409 1.00 20.22 ? 100 ASN   A CB  1 
ATOM   534  C CG  . ASN   A 1 78  ? 5.605   19.430 -30.728 1.00 22.05 ? 100 ASN   A CG  1 
ATOM   535  O OD1 . ASN   A 1 78  ? 4.459   19.822 -30.993 1.00 23.01 ? 100 ASN   A OD1 1 
ATOM   536  N ND2 . ASN   A 1 78  ? 6.608   19.549 -31.575 1.00 23.82 ? 100 ASN   A ND2 1 
ATOM   537  N N   . LEU   A 1 79  ? 6.097   18.729 -26.093 1.00 17.44 ? 101 LEU   A N   1 
ATOM   538  C CA  . LEU   A 1 79  ? 6.206   17.886 -24.906 1.00 17.37 ? 101 LEU   A CA  1 
ATOM   539  C C   . LEU   A 1 79  ? 5.895   18.681 -23.630 1.00 16.37 ? 101 LEU   A C   1 
ATOM   540  O O   . LEU   A 1 79  ? 6.097   19.896 -23.544 1.00 14.73 ? 101 LEU   A O   1 
ATOM   541  C CB  . LEU   A 1 79  ? 7.610   17.284 -24.796 1.00 18.70 ? 101 LEU   A CB  1 
ATOM   542  C CG  . LEU   A 1 79  ? 8.149   16.535 -26.021 1.00 20.46 ? 101 LEU   A CG  1 
ATOM   543  C CD1 . LEU   A 1 79  ? 9.573   16.025 -25.736 1.00 20.58 ? 101 LEU   A CD1 1 
ATOM   544  C CD2 . LEU   A 1 79  ? 7.240   15.394 -26.441 1.00 21.86 ? 101 LEU   A CD2 1 
ATOM   545  N N   . LEU   A 1 80  ? 5.435   17.949 -22.616 1.00 16.00 ? 102 LEU   A N   1 
ATOM   546  C CA  . LEU   A 1 80  ? 5.373   18.416 -21.242 1.00 17.19 ? 102 LEU   A CA  1 
ATOM   547  C C   . LEU   A 1 80  ? 6.212   17.497 -20.364 1.00 17.40 ? 102 LEU   A C   1 
ATOM   548  O O   . LEU   A 1 80  ? 6.384   16.323 -20.679 1.00 18.22 ? 102 LEU   A O   1 
ATOM   549  C CB  . LEU   A 1 80  ? 3.941   18.389 -20.735 1.00 17.85 ? 102 LEU   A CB  1 
ATOM   550  C CG  . LEU   A 1 80  ? 2.978   19.409 -21.320 1.00 20.02 ? 102 LEU   A CG  1 
ATOM   551  C CD1 . LEU   A 1 80  ? 1.585   18.999 -20.951 1.00 22.34 ? 102 LEU   A CD1 1 
ATOM   552  C CD2 . LEU   A 1 80  ? 3.323   20.795 -20.802 1.00 21.99 ? 102 LEU   A CD2 1 
ATOM   553  N N   . VAL   A 1 81  ? 6.688   18.040 -19.246 1.00 16.41 ? 103 VAL   A N   1 
ATOM   554  C CA  . VAL   A 1 81  ? 7.207   17.235 -18.158 1.00 16.34 ? 103 VAL   A CA  1 
ATOM   555  C C   . VAL   A 1 81  ? 6.405   17.602 -16.911 1.00 16.04 ? 103 VAL   A C   1 
ATOM   556  O O   . VAL   A 1 81  ? 6.073   18.763 -16.720 1.00 16.34 ? 103 VAL   A O   1 
ATOM   557  C CB  . VAL   A 1 81  ? 8.726   17.394 -17.943 1.00 15.99 ? 103 VAL   A CB  1 
ATOM   558  C CG1 . VAL   A 1 81  ? 9.116   18.823 -17.612 1.00 16.43 ? 103 VAL   A CG1 1 
ATOM   559  C CG2 . VAL   A 1 81  ? 9.252   16.465 -16.855 1.00 15.57 ? 103 VAL   A CG2 1 
ATOM   560  N N   . SER   A 1 82  ? 6.103   16.601 -16.081 1.00 15.87 ? 104 SER   A N   1 
ATOM   561  C CA  . SER   A 1 82  ? 5.398   16.802 -14.828 1.00 15.70 ? 104 SER   A CA  1 
ATOM   562  C C   . SER   A 1 82  ? 6.222   16.248 -13.675 1.00 15.94 ? 104 SER   A C   1 
ATOM   563  O O   . SER   A 1 82  ? 6.933   15.266 -13.847 1.00 16.70 ? 104 SER   A O   1 
ATOM   564  C CB  . SER   A 1 82  ? 4.052   16.152 -14.866 1.00 16.03 ? 104 SER   A CB  1 
ATOM   565  O OG  . SER   A 1 82  ? 4.180   14.795 -15.258 1.00 16.75 ? 104 SER   A OG  1 
ATOM   566  N N   . ALA   A 1 83  ? 6.076   16.877 -12.501 1.00 17.20 ? 105 ALA   A N   1 
ATOM   567  C CA  . ALA   A 1 83  ? 6.739   16.454 -11.274 1.00 15.89 ? 105 ALA   A CA  1 
ATOM   568  C C   . ALA   A 1 83  ? 5.686   16.038 -10.253 1.00 16.20 ? 105 ALA   A C   1 
ATOM   569  O O   . ALA   A 1 83  ? 4.830   16.860 -9.946  1.00 17.07 ? 105 ALA   A O   1 
ATOM   570  C CB  . ALA   A 1 83  ? 7.536   17.621 -10.717 1.00 15.96 ? 105 ALA   A CB  1 
ATOM   571  N N   . SER   A 1 84  ? 5.816   14.831 -9.675  1.00 15.37 ? 106 SER   A N   1 
ATOM   572  C CA  . SER   A 1 84  ? 4.756   14.226 -8.885  1.00 16.41 ? 106 SER   A CA  1 
ATOM   573  C C   . SER   A 1 84  ? 5.239   13.728 -7.525  1.00 17.40 ? 106 SER   A C   1 
ATOM   574  O O   . SER   A 1 84  ? 6.408   13.368 -7.313  1.00 17.47 ? 106 SER   A O   1 
ATOM   575  C CB  . SER   A 1 84  ? 4.114   13.101 -9.664  1.00 16.38 ? 106 SER   A CB  1 
ATOM   576  O OG  . SER   A 1 84  ? 3.120   12.416 -8.920  1.00 17.25 ? 106 SER   A OG  1 
ATOM   577  N N   . ASP   A 1 85  ? 4.269   13.662 -6.618  1.00 18.51 ? 107 ASP   A N   1 
ATOM   578  C CA  . ASP   A 1 85  ? 4.472   13.087 -5.296  1.00 19.00 ? 107 ASP   A CA  1 
ATOM   579  C C   . ASP   A 1 85  ? 4.749   11.586 -5.386  1.00 19.29 ? 107 ASP   A C   1 
ATOM   580  O O   . ASP   A 1 85  ? 5.168   10.989 -4.381  1.00 20.09 ? 107 ASP   A O   1 
ATOM   581  C CB  . ASP   A 1 85  ? 3.301   13.402 -4.374  1.00 19.20 ? 107 ASP   A CB  1 
ATOM   582  C CG  . ASP   A 1 85  ? 3.336   14.773 -3.715  1.00 20.50 ? 107 ASP   A CG  1 
ATOM   583  O OD1 . ASP   A 1 85  ? 4.139   15.621 -4.173  1.00 20.75 ? 107 ASP   A OD1 1 
ATOM   584  O OD2 . ASP   A 1 85  ? 2.573   14.976 -2.717  1.00 22.36 ? 107 ASP   A OD2 1 
ATOM   585  N N   . ASP   A 1 86  ? 4.545   10.988 -6.572  1.00 17.97 ? 108 ASP   A N   1 
ATOM   586  C CA  . ASP   A 1 86  ? 4.876   9.583  -6.771  1.00 19.04 ? 108 ASP   A CA  1 
ATOM   587  C C   . ASP   A 1 86  ? 6.391   9.377  -6.946  1.00 18.33 ? 108 ASP   A C   1 
ATOM   588  O O   . ASP   A 1 86  ? 6.832   8.261  -7.204  1.00 18.86 ? 108 ASP   A O   1 
ATOM   589  C CB  . ASP   A 1 86  ? 4.033   8.986  -7.886  1.00 19.68 ? 108 ASP   A CB  1 
ATOM   590  C CG  . ASP   A 1 86  ? 4.363   9.495  -9.285  1.00 19.63 ? 108 ASP   A CG  1 
ATOM   591  O OD1 . ASP   A 1 86  ? 5.378   10.220 -9.416  1.00 18.53 ? 108 ASP   A OD1 1 
ATOM   592  O OD2 . ASP   A 1 86  ? 3.595   9.174  -10.226 1.00 20.34 ? 108 ASP   A OD2 1 
ATOM   593  N N   . LYS   A 1 87  ? 7.169   10.456 -6.815  1.00 18.33 ? 109 LYS   A N   1 
ATOM   594  C CA  . LYS   A 1 87  ? 8.621   10.449 -6.785  1.00 18.56 ? 109 LYS   A CA  1 
ATOM   595  C C   . LYS   A 1 87  ? 9.182   10.399 -8.199  1.00 18.20 ? 109 LYS   A C   1 
ATOM   596  O O   . LYS   A 1 87  ? 10.392  10.245 -8.343  1.00 17.94 ? 109 LYS   A O   1 
ATOM   597  C CB  . LYS   A 1 87  ? 9.211   9.317  -5.940  1.00 20.69 ? 109 LYS   A CB  1 
ATOM   598  C CG  . LYS   A 1 87  ? 8.664   9.259  -4.523  1.00 22.66 ? 109 LYS   A CG  1 
ATOM   599  C CD  . LYS   A 1 87  ? 9.385   8.220  -3.668  1.00 26.33 ? 109 LYS   A CD  1 
ATOM   600  C CE  . LYS   A 1 87  ? 8.644   7.881  -2.437  1.00 30.96 ? 109 LYS   A CE  1 
ATOM   601  N NZ  . LYS   A 1 87  ? 9.275   6.706  -1.845  1.00 36.44 ? 109 LYS   A NZ  1 
ATOM   602  N N   . THR   A 1 88  ? 8.310   10.544 -9.213  1.00 17.96 ? 110 THR   A N   1 
ATOM   603  C CA  . THR   A 1 88  ? 8.739   10.499 -10.604 1.00 18.08 ? 110 THR   A CA  1 
ATOM   604  C C   . THR   A 1 88  ? 8.439   11.826 -11.292 1.00 17.89 ? 110 THR   A C   1 
ATOM   605  O O   . THR   A 1 88  ? 7.630   12.627 -10.836 1.00 16.72 ? 110 THR   A O   1 
ATOM   606  C CB  . THR   A 1 88  ? 8.074   9.358  -11.387 1.00 18.62 ? 110 THR   A CB  1 
ATOM   607  O OG1 . THR   A 1 88  ? 6.745   9.742  -11.739 1.00 18.34 ? 110 THR   A OG1 1 
ATOM   608  C CG2 . THR   A 1 88  ? 8.109   8.025  -10.659 1.00 19.62 ? 110 THR   A CG2 1 
ATOM   609  N N   . LEU   A 1 89  ? 9.141   12.031 -12.406 1.00 17.54 ? 111 LEU   A N   1 
ATOM   610  C CA  . LEU   A 1 89  ? 8.662   12.891 -13.462 1.00 16.37 ? 111 LEU   A CA  1 
ATOM   611  C C   . LEU   A 1 89  ? 8.173   12.035 -14.624 1.00 16.91 ? 111 LEU   A C   1 
ATOM   612  O O   . LEU   A 1 89  ? 8.626   10.912 -14.847 1.00 17.89 ? 111 LEU   A O   1 
ATOM   613  C CB  . LEU   A 1 89  ? 9.723   13.887 -13.908 1.00 15.80 ? 111 LEU   A CB  1 
ATOM   614  C CG  . LEU   A 1 89  ? 10.335  14.717 -12.778 1.00 15.48 ? 111 LEU   A CG  1 
ATOM   615  C CD1 . LEU   A 1 89  ? 11.699  14.167 -12.387 1.00 15.55 ? 111 LEU   A CD1 1 
ATOM   616  C CD2 . LEU   A 1 89  ? 10.404  16.184 -13.154 1.00 15.55 ? 111 LEU   A CD2 1 
ATOM   617  N N   . LYS   A 1 90  ? 7.248   12.604 -15.388 1.00 17.00 ? 112 LYS   A N   1 
ATOM   618  C CA  . LYS   A 1 90  ? 6.822   11.985 -16.631 1.00 17.57 ? 112 LYS   A CA  1 
ATOM   619  C C   . LYS   A 1 90  ? 6.965   12.996 -17.758 1.00 16.84 ? 112 LYS   A C   1 
ATOM   620  O O   . LYS   A 1 90  ? 6.661   14.178 -17.592 1.00 17.26 ? 112 LYS   A O   1 
ATOM   621  C CB  . LYS   A 1 90  ? 5.387   11.464 -16.513 1.00 18.16 ? 112 LYS   A CB  1 
ATOM   622  C CG  . LYS   A 1 90  ? 5.327   10.186 -15.693 1.00 18.49 ? 112 LYS   A CG  1 
ATOM   623  C CD  . LYS   A 1 90  ? 3.905   9.711  -15.409 1.00 19.06 ? 112 LYS   A CD  1 
ATOM   624  C CE  . LYS   A 1 90  ? 3.831   8.467  -14.571 1.00 20.36 ? 112 LYS   A CE  1 
ATOM   625  N NZ  . LYS   A 1 90  ? 4.275   7.258  -15.282 1.00 21.63 ? 112 LYS   A NZ  1 
ATOM   626  N N   . ILE   A 1 91  ? 7.445   12.500 -18.894 1.00 16.91 ? 113 ILE   A N   1 
ATOM   627  C CA  . ILE   A 1 91  ? 7.438   13.236 -20.139 1.00 17.49 ? 113 ILE   A CA  1 
ATOM   628  C C   . ILE   A 1 91  ? 6.236   12.782 -20.960 1.00 17.88 ? 113 ILE   A C   1 
ATOM   629  O O   . ILE   A 1 91  ? 6.046   11.591 -21.197 1.00 18.19 ? 113 ILE   A O   1 
ATOM   630  C CB  . ILE   A 1 91  ? 8.751   12.997 -20.898 1.00 17.90 ? 113 ILE   A CB  1 
ATOM   631  C CG1 . ILE   A 1 91  ? 9.974   13.335 -20.043 1.00 18.07 ? 113 ILE   A CG1 1 
ATOM   632  C CG2 . ILE   A 1 91  ? 8.723   13.747 -22.218 1.00 18.13 ? 113 ILE   A CG2 1 
ATOM   633  C CD1 . ILE   A 1 91  ? 11.316  13.123 -20.726 1.00 17.77 ? 113 ILE   A CD1 1 
ATOM   634  N N   . TRP   A 1 92  ? 5.495   13.772 -21.464 1.00 16.74 ? 114 TRP   A N   1 
ATOM   635  C CA  . TRP   A 1 92  ? 4.248   13.542 -22.159 1.00 17.34 ? 114 TRP   A CA  1 
ATOM   636  C C   . TRP   A 1 92  ? 4.349   14.097 -23.569 1.00 18.60 ? 114 TRP   A C   1 
ATOM   637  O O   . TRP   A 1 92  ? 4.892   15.182 -23.765 1.00 19.52 ? 114 TRP   A O   1 
ATOM   638  C CB  . TRP   A 1 92  ? 3.092   14.237 -21.439 1.00 17.38 ? 114 TRP   A CB  1 
ATOM   639  C CG  . TRP   A 1 92  ? 2.994   13.908 -19.986 1.00 18.14 ? 114 TRP   A CG  1 
ATOM   640  C CD1 . TRP   A 1 92  ? 3.553   14.584 -18.944 1.00 18.88 ? 114 TRP   A CD1 1 
ATOM   641  C CD2 . TRP   A 1 92  ? 2.262   12.808 -19.415 1.00 18.63 ? 114 TRP   A CD2 1 
ATOM   642  N NE1 . TRP   A 1 92  ? 3.214   13.982 -17.763 1.00 18.12 ? 114 TRP   A NE1 1 
ATOM   643  C CE2 . TRP   A 1 92  ? 2.431   12.894 -18.019 1.00 18.56 ? 114 TRP   A CE2 1 
ATOM   644  C CE3 . TRP   A 1 92  ? 1.484   11.776 -19.947 1.00 18.60 ? 114 TRP   A CE3 1 
ATOM   645  C CZ2 . TRP   A 1 92  ? 1.827   12.000 -17.145 1.00 18.88 ? 114 TRP   A CZ2 1 
ATOM   646  C CZ3 . TRP   A 1 92  ? 0.891   10.890 -19.082 1.00 18.57 ? 114 TRP   A CZ3 1 
ATOM   647  C CH2 . TRP   A 1 92  ? 1.051   11.008 -17.698 1.00 19.08 ? 114 TRP   A CH2 1 
ATOM   648  N N   . ASP   A 1 93  ? 3.763   13.354 -24.507 1.00 19.82 ? 115 ASP   A N   1 
ATOM   649  C CA  . ASP   A 1 93  ? 3.454   13.884 -25.817 1.00 21.34 ? 115 ASP   A CA  1 
ATOM   650  C C   . ASP   A 1 93  ? 2.112   14.603 -25.734 1.00 22.10 ? 115 ASP   A C   1 
ATOM   651  O O   . ASP   A 1 93  ? 1.082   13.980 -25.461 1.00 22.78 ? 115 ASP   A O   1 
ATOM   652  C CB  . ASP   A 1 93  ? 3.466   12.787 -26.864 1.00 23.23 ? 115 ASP   A CB  1 
ATOM   653  C CG  . ASP   A 1 93  ? 3.244   13.290 -28.281 1.00 25.83 ? 115 ASP   A CG  1 
ATOM   654  O OD1 . ASP   A 1 93  ? 2.105   13.613 -28.614 1.00 27.75 ? 115 ASP   A OD1 1 
ATOM   655  O OD2 . ASP   A 1 93  ? 4.227   13.407 -29.015 1.00 31.84 ? 115 ASP   A OD2 1 
ATOM   656  N N   . VAL   A 1 94  ? 2.125   15.915 -25.987 1.00 20.94 ? 116 VAL   A N   1 
ATOM   657  C CA  . VAL   A 1 94  ? 0.928   16.715 -25.787 1.00 22.56 ? 116 VAL   A CA  1 
ATOM   658  C C   . VAL   A 1 94  ? -0.172  16.301 -26.768 1.00 22.15 ? 116 VAL   A C   1 
ATOM   659  O O   . VAL   A 1 94  ? -1.336  16.240 -26.395 1.00 23.44 ? 116 VAL   A O   1 
ATOM   660  C CB  . VAL   A 1 94  ? 1.249   18.217 -25.871 1.00 25.24 ? 116 VAL   A CB  1 
ATOM   661  C CG1 . VAL   A 1 94  ? -0.019  19.061 -25.742 1.00 27.83 ? 116 VAL   A CG1 1 
ATOM   662  C CG2 . VAL   A 1 94  ? 2.241   18.617 -24.788 1.00 25.90 ? 116 VAL   A CG2 1 
ATOM   663  N N   A SER   A 1 95  ? 0.188   16.005 -28.018 0.70 22.48 ? 117 SER   A N   1 
ATOM   664  N N   B SER   A 1 95  ? 0.206   16.002 -28.013 0.30 21.97 ? 117 SER   A N   1 
ATOM   665  C CA  A SER   A 1 95  ? -0.826  15.716 -29.019 0.70 24.37 ? 117 SER   A CA  1 
ATOM   666  C CA  B SER   A 1 95  ? -0.766  15.694 -29.049 0.30 22.55 ? 117 SER   A CA  1 
ATOM   667  C C   A SER   A 1 95  ? -1.515  14.379 -28.732 0.70 24.34 ? 117 SER   A C   1 
ATOM   668  C C   B SER   A 1 95  ? -1.496  14.382 -28.754 0.30 23.25 ? 117 SER   A C   1 
ATOM   669  O O   A SER   A 1 95  ? -2.727  14.279 -28.900 0.70 26.87 ? 117 SER   A O   1 
ATOM   670  O O   B SER   A 1 95  ? -2.709  14.306 -28.935 0.30 24.37 ? 117 SER   A O   1 
ATOM   671  C CB  A SER   A 1 95  ? -0.265  15.752 -30.415 0.70 26.45 ? 117 SER   A CB  1 
ATOM   672  C CB  B SER   A 1 95  ? -0.118  15.663 -30.406 0.30 22.59 ? 117 SER   A CB  1 
ATOM   673  O OG  A SER   A 1 95  ? 0.709   14.732 -30.585 0.70 30.32 ? 117 SER   A OG  1 
ATOM   674  O OG  B SER   A 1 95  ? -0.984  15.081 -31.367 0.30 22.33 ? 117 SER   A OG  1 
ATOM   675  N N   . SER   A 1 96  ? -0.757  13.355 -28.312 1.00 23.53 ? 118 SER   A N   1 
ATOM   676  C CA  . SER   A 1 96  ? -1.327  12.024 -28.091 1.00 24.17 ? 118 SER   A CA  1 
ATOM   677  C C   . SER   A 1 96  ? -1.797  11.830 -26.652 1.00 24.06 ? 118 SER   A C   1 
ATOM   678  O O   . SER   A 1 96  ? -2.578  10.918 -26.368 1.00 25.47 ? 118 SER   A O   1 
ATOM   679  C CB  . SER   A 1 96  ? -0.339  10.934 -28.442 1.00 24.94 ? 118 SER   A CB  1 
ATOM   680  O OG  . SER   A 1 96  ? 0.721   10.866 -27.496 1.00 23.96 ? 118 SER   A OG  1 
ATOM   681  N N   . GLY   A 1 97  ? -1.252  12.629 -25.733 1.00 23.11 ? 119 GLY   A N   1 
ATOM   682  C CA  . GLY   A 1 97  ? -1.543  12.478 -24.318 1.00 23.45 ? 119 GLY   A CA  1 
ATOM   683  C C   . GLY   A 1 97  ? -0.782  11.321 -23.673 1.00 23.53 ? 119 GLY   A C   1 
ATOM   684  O O   . GLY   A 1 97  ? -0.967  11.056 -22.490 1.00 24.32 ? 119 GLY   A O   1 
ATOM   685  N N   . LYS   A 1 98  ? 0.122   10.682 -24.424 1.00 24.75 ? 120 LYS   A N   1 
ATOM   686  C CA  . LYS   A 1 98  ? 0.801   9.479  -23.972 1.00 24.79 ? 120 LYS   A CA  1 
ATOM   687  C C   . LYS   A 1 98  ? 2.038   9.845  -23.162 1.00 22.31 ? 120 LYS   A C   1 
ATOM   688  O O   . LYS   A 1 98  ? 2.743   10.791 -23.478 1.00 21.73 ? 120 LYS   A O   1 
ATOM   689  C CB  . LYS   A 1 98  ? 1.163   8.590  -25.168 1.00 28.90 ? 120 LYS   A CB  1 
ATOM   690  C CG  . LYS   A 1 98  ? -0.055  7.974  -25.860 1.00 33.33 ? 120 LYS   A CG  1 
ATOM   691  C CD  . LYS   A 1 98  ? 0.205   6.778  -26.773 1.00 37.62 ? 120 LYS   A CD  1 
ATOM   692  C CE  . LYS   A 1 98  ? -0.931  6.521  -27.742 1.00 39.91 ? 120 LYS   A CE  1 
ATOM   693  N N   . CYS   A 1 99  ? 2.294   9.067  -22.111 1.00 20.82 ? 121 CYS   A N   1 
ATOM   694  C CA  . CYS   A 1 99  ? 3.534   9.170  -21.365 1.00 21.30 ? 121 CYS   A CA  1 
ATOM   695  C C   . CYS   A 1 99  ? 4.655   8.494  -22.161 1.00 21.98 ? 121 CYS   A C   1 
ATOM   696  O O   . CYS   A 1 99  ? 4.602   7.293  -22.415 1.00 23.70 ? 121 CYS   A O   1 
ATOM   697  C CB  . CYS   A 1 99  ? 3.353   8.540  -19.993 1.00 22.61 ? 121 CYS   A CB  1 
ATOM   698  S SG  . CYS   A 1 99  ? 4.885   8.415  -19.053 1.00 23.36 ? 121 CYS   A SG  1 
ATOM   699  N N   . LEU   A 1 100 ? 5.666   9.272  -22.554 1.00 21.09 ? 122 LEU   A N   1 
ATOM   700  C CA  . LEU   A 1 100 ? 6.795   8.752  -23.310 1.00 22.33 ? 122 LEU   A CA  1 
ATOM   701  C C   . LEU   A 1 100 ? 7.850   8.131  -22.402 1.00 23.07 ? 122 LEU   A C   1 
ATOM   702  O O   . LEU   A 1 100 ? 8.487   7.152  -22.795 1.00 24.16 ? 122 LEU   A O   1 
ATOM   703  C CB  . LEU   A 1 100 ? 7.393   9.889  -24.128 1.00 22.96 ? 122 LEU   A CB  1 
ATOM   704  C CG  . LEU   A 1 100 ? 6.450   10.545 -25.136 1.00 22.64 ? 122 LEU   A CG  1 
ATOM   705  C CD1 . LEU   A 1 100 ? 7.203   11.682 -25.806 1.00 22.63 ? 122 LEU   A CD1 1 
ATOM   706  C CD2 . LEU   A 1 100 ? 5.917   9.515  -26.136 1.00 24.12 ? 122 LEU   A CD2 1 
ATOM   707  N N   . LYS   A 1 101 ? 8.102   8.771  -21.248 1.00 21.82 ? 123 LYS   A N   1 
ATOM   708  C CA  . LYS   A 1 101 ? 9.128   8.336  -20.314 1.00 22.22 ? 123 LYS   A CA  1 
ATOM   709  C C   . LYS   A 1 101 ? 8.672   8.635  -18.892 1.00 20.98 ? 123 LYS   A C   1 
ATOM   710  O O   . LYS   A 1 101 ? 7.988   9.637  -18.653 1.00 20.57 ? 123 LYS   A O   1 
ATOM   711  C CB  . LYS   A 1 101 ? 10.465  9.066  -20.485 1.00 22.95 ? 123 LYS   A CB  1 
ATOM   712  C CG  . LYS   A 1 101 ? 11.228  8.814  -21.767 1.00 26.45 ? 123 LYS   A CG  1 
ATOM   713  C CD  . LYS   A 1 101 ? 11.743  7.384  -21.826 1.00 29.46 ? 123 LYS   A CD  1 
ATOM   714  C CE  . LYS   A 1 101 ? 12.723  7.138  -22.901 1.00 32.88 ? 123 LYS   A CE  1 
ATOM   715  N NZ  . LYS   A 1 101 ? 12.051  6.747  -24.131 1.00 36.72 ? 123 LYS   A NZ  1 
ATOM   716  N N   . THR   A 1 102 ? 9.082   7.764  -17.959 1.00 20.84 ? 124 THR   A N   1 
ATOM   717  C CA  . THR   A 1 102 ? 8.984   8.029  -16.539 1.00 20.41 ? 124 THR   A CA  1 
ATOM   718  C C   . THR   A 1 102 ? 10.404  8.117  -15.986 1.00 20.87 ? 124 THR   A C   1 
ATOM   719  O O   . THR   A 1 102 ? 11.213  7.196  -16.150 1.00 22.55 ? 124 THR   A O   1 
ATOM   720  C CB  . THR   A 1 102 ? 8.164   6.955  -15.822 1.00 21.10 ? 124 THR   A CB  1 
ATOM   721  O OG1 . THR   A 1 102 ? 6.904   6.838  -16.479 1.00 20.52 ? 124 THR   A OG1 1 
ATOM   722  C CG2 . THR   A 1 102 ? 7.970   7.282  -14.350 1.00 20.70 ? 124 THR   A CG2 1 
ATOM   723  N N   . LEU   A 1 103 ? 10.692  9.266  -15.364 1.00 20.04 ? 125 LEU   A N   1 
ATOM   724  C CA  . LEU   A 1 103 ? 12.010  9.590  -14.853 1.00 19.28 ? 125 LEU   A CA  1 
ATOM   725  C C   . LEU   A 1 103 ? 12.064  9.209  -13.374 1.00 18.90 ? 125 LEU   A C   1 
ATOM   726  O O   . LEU   A 1 103 ? 11.462  9.883  -12.537 1.00 18.01 ? 125 LEU   A O   1 
ATOM   727  C CB  . LEU   A 1 103 ? 12.279  11.079 -15.048 1.00 19.76 ? 125 LEU   A CB  1 
ATOM   728  C CG  . LEU   A 1 103 ? 12.087  11.646 -16.465 1.00 22.17 ? 125 LEU   A CG  1 
ATOM   729  C CD1 . LEU   A 1 103 ? 12.625  13.071 -16.614 1.00 20.62 ? 125 LEU   A CD1 1 
ATOM   730  C CD2 . LEU   A 1 103 ? 12.666  10.757 -17.513 1.00 24.01 ? 125 LEU   A CD2 1 
ATOM   731  N N   . LYS   A 1 104 ? 12.859  8.176  -13.069 1.00 19.23 ? 126 LYS   A N   1 
ATOM   732  C CA  . LYS   A 1 104 ? 12.926  7.596  -11.741 1.00 19.69 ? 126 LYS   A CA  1 
ATOM   733  C C   . LYS   A 1 104 ? 14.319  7.808  -11.175 1.00 20.90 ? 126 LYS   A C   1 
ATOM   734  O O   . LYS   A 1 104 ? 15.326  7.655  -11.884 1.00 21.53 ? 126 LYS   A O   1 
ATOM   735  C CB  . LYS   A 1 104 ? 12.604  6.098  -11.814 1.00 22.47 ? 126 LYS   A CB  1 
ATOM   736  C CG  . LYS   A 1 104 ? 11.224  5.732  -12.346 1.00 25.30 ? 126 LYS   A CG  1 
ATOM   737  C CD  . LYS   A 1 104 ? 10.985  4.227  -12.508 1.00 29.10 ? 126 LYS   A CD  1 
ATOM   738  C CE  . LYS   A 1 104 ? 9.585   3.904  -12.938 1.00 33.76 ? 126 LYS   A CE  1 
ATOM   739  N N   . GLY   A 1 105 ? 14.367  8.133  -9.883  1.00 20.21 ? 127 GLY   A N   1 
ATOM   740  C CA  . GLY   A 1 105 ? 15.634  8.345  -9.209  1.00 20.75 ? 127 GLY   A CA  1 
ATOM   741  C C   . GLY   A 1 105 ? 15.495  9.168  -7.930  1.00 20.10 ? 127 GLY   A C   1 
ATOM   742  O O   . GLY   A 1 105 ? 16.207  8.902  -6.955  1.00 20.85 ? 127 GLY   A O   1 
ATOM   743  N N   . HIS   A 1 106 ? 14.604  10.170 -7.920  1.00 19.05 ? 128 HIS   A N   1 
ATOM   744  C CA  . HIS   A 1 106 ? 14.377  10.918 -6.685  1.00 18.56 ? 128 HIS   A CA  1 
ATOM   745  C C   . HIS   A 1 106 ? 13.814  9.973  -5.619  1.00 18.70 ? 128 HIS   A C   1 
ATOM   746  O O   . HIS   A 1 106 ? 13.092  9.034  -5.955  1.00 18.78 ? 128 HIS   A O   1 
ATOM   747  C CB  . HIS   A 1 106 ? 13.435  12.103 -6.908  1.00 18.03 ? 128 HIS   A CB  1 
ATOM   748  C CG  . HIS   A 1 106 ? 14.053  13.311 -7.518  1.00 17.52 ? 128 HIS   A CG  1 
ATOM   749  N ND1 . HIS   A 1 106 ? 15.096  13.985 -6.927  1.00 16.62 ? 128 HIS   A ND1 1 
ATOM   750  C CD2 . HIS   A 1 106 ? 13.782  13.965 -8.678  1.00 17.04 ? 128 HIS   A CD2 1 
ATOM   751  C CE1 . HIS   A 1 106 ? 15.413  15.026 -7.696  1.00 17.22 ? 128 HIS   A CE1 1 
ATOM   752  N NE2 . HIS   A 1 106 ? 14.624  15.027 -8.766  1.00 16.39 ? 128 HIS   A NE2 1 
ATOM   753  N N   . SER   A 1 107 ? 14.139  10.239 -4.340  1.00 18.32 ? 129 SER   A N   1 
ATOM   754  C CA  . SER   A 1 107 ? 13.751  9.381  -3.228  1.00 20.26 ? 129 SER   A CA  1 
ATOM   755  C C   . SER   A 1 107 ? 12.634  10.021 -2.404  1.00 20.29 ? 129 SER   A C   1 
ATOM   756  O O   . SER   A 1 107 ? 12.311  9.556  -1.312  1.00 20.89 ? 129 SER   A O   1 
ATOM   757  C CB  . SER   A 1 107 ? 14.948  9.069  -2.373  1.00 20.68 ? 129 SER   A CB  1 
ATOM   758  O OG  . SER   A 1 107 ? 15.510  10.260 -1.843  1.00 19.51 ? 129 SER   A OG  1 
ATOM   759  N N   . ASN   A 1 108 ? 12.040  11.096 -2.932  1.00 20.30 ? 130 ASN   A N   1 
ATOM   760  C CA  . ASN   A 1 108 ? 10.928  11.767 -2.281  1.00 20.38 ? 130 ASN   A CA  1 
ATOM   761  C C   . ASN   A 1 108 ? 10.188  12.552 -3.362  1.00 19.31 ? 130 ASN   A C   1 
ATOM   762  O O   . ASN   A 1 108 ? 10.561  12.491 -4.526  1.00 19.50 ? 130 ASN   A O   1 
ATOM   763  C CB  . ASN   A 1 108 ? 11.424  12.620 -1.123  1.00 20.11 ? 130 ASN   A CB  1 
ATOM   764  C CG  . ASN   A 1 108 ? 10.390  12.884 -0.051  1.00 22.13 ? 130 ASN   A CG  1 
ATOM   765  O OD1 . ASN   A 1 108 ? 9.172   12.906 -0.286  1.00 22.90 ? 130 ASN   A OD1 1 
ATOM   766  N ND2 . ASN   A 1 108 ? 10.876  13.173 1.139   1.00 23.64 ? 130 ASN   A ND2 1 
ATOM   767  N N   . TYR   A 1 109 ? 9.135   13.266 -2.957  1.00 18.93 ? 131 TYR   A N   1 
ATOM   768  C CA  . TYR   A 1 109 ? 8.293   14.000 -3.878  1.00 19.21 ? 131 TYR   A CA  1 
ATOM   769  C C   . TYR   A 1 109 ? 9.136   14.841 -4.829  1.00 17.67 ? 131 TYR   A C   1 
ATOM   770  O O   . TYR   A 1 109 ? 10.080  15.510 -4.406  1.00 16.58 ? 131 TYR   A O   1 
ATOM   771  C CB  . TYR   A 1 109 ? 7.376   14.976 -3.143  1.00 20.17 ? 131 TYR   A CB  1 
ATOM   772  C CG  . TYR   A 1 109 ? 6.529   14.393 -2.021  1.00 21.93 ? 131 TYR   A CG  1 
ATOM   773  C CD1 . TYR   A 1 109 ? 6.060   13.086 -2.068  1.00 22.69 ? 131 TYR   A CD1 1 
ATOM   774  C CD2 . TYR   A 1 109 ? 6.170   15.173 -0.929  1.00 25.46 ? 131 TYR   A CD2 1 
ATOM   775  C CE1 . TYR   A 1 109 ? 5.270   12.567 -1.058  1.00 25.57 ? 131 TYR   A CE1 1 
ATOM   776  C CE2 . TYR   A 1 109 ? 5.372   14.664 0.085   1.00 28.60 ? 131 TYR   A CE2 1 
ATOM   777  C CZ  . TYR   A 1 109 ? 4.918   13.361 0.014   1.00 28.91 ? 131 TYR   A CZ  1 
ATOM   778  O OH  . TYR   A 1 109 ? 4.127   12.836 0.991   1.00 35.80 ? 131 TYR   A OH  1 
ATOM   779  N N   . VAL   A 1 110 ? 8.755   14.855 -6.107  1.00 17.18 ? 132 VAL   A N   1 
ATOM   780  C CA  . VAL   A 1 110 ? 9.384   15.787 -7.037  1.00 16.13 ? 132 VAL   A CA  1 
ATOM   781  C C   . VAL   A 1 110 ? 8.520   17.047 -7.073  1.00 15.80 ? 132 VAL   A C   1 
ATOM   782  O O   . VAL   A 1 110 ? 7.318   16.960 -7.282  1.00 16.48 ? 132 VAL   A O   1 
ATOM   783  C CB  . VAL   A 1 110 ? 9.608   15.207 -8.443  1.00 16.36 ? 132 VAL   A CB  1 
ATOM   784  C CG1 . VAL   A 1 110 ? 10.585  16.066 -9.243  1.00 16.90 ? 132 VAL   A CG1 1 
ATOM   785  C CG2 . VAL   A 1 110 ? 10.113  13.769 -8.407  1.00 17.75 ? 132 VAL   A CG2 1 
ATOM   786  N N   . PHE   A 1 111 ? 9.142   18.209 -6.843  1.00 15.35 ? 133 PHE   A N   1 
ATOM   787  C CA  . PHE   A 1 111 ? 8.400   19.435 -6.607  1.00 16.49 ? 133 PHE   A CA  1 
ATOM   788  C C   . PHE   A 1 111 ? 8.429   20.392 -7.798  1.00 16.42 ? 133 PHE   A C   1 
ATOM   789  O O   . PHE   A 1 111 ? 7.468   21.118 -8.027  1.00 17.15 ? 133 PHE   A O   1 
ATOM   790  C CB  . PHE   A 1 111 ? 8.999   20.142 -5.392  1.00 18.38 ? 133 PHE   A CB  1 
ATOM   791  C CG  . PHE   A 1 111 ? 8.121   21.269 -4.878  1.00 20.20 ? 133 PHE   A CG  1 
ATOM   792  C CD1 . PHE   A 1 111 ? 6.839   21.008 -4.389  1.00 21.86 ? 133 PHE   A CD1 1 
ATOM   793  C CD2 . PHE   A 1 111 ? 8.586   22.577 -4.851  1.00 21.41 ? 133 PHE   A CD2 1 
ATOM   794  C CE1 . PHE   A 1 111 ? 6.043   22.038 -3.908  1.00 22.48 ? 133 PHE   A CE1 1 
ATOM   795  C CE2 . PHE   A 1 111 ? 7.782   23.605 -4.370  1.00 22.52 ? 133 PHE   A CE2 1 
ATOM   796  C CZ  . PHE   A 1 111 ? 6.532   23.330 -3.866  1.00 22.81 ? 133 PHE   A CZ  1 
ATOM   797  N N   . CYS   A 1 112 ? 9.530   20.433 -8.542  1.00 15.83 ? 134 CYS   A N   1 
ATOM   798  C CA  . CYS   A 1 112 ? 9.701   21.455 -9.565  1.00 15.83 ? 134 CYS   A CA  1 
ATOM   799  C C   . CYS   A 1 112 ? 10.472  20.877 -10.747 1.00 14.90 ? 134 CYS   A C   1 
ATOM   800  O O   . CYS   A 1 112 ? 11.292  19.984 -10.581 1.00 15.50 ? 134 CYS   A O   1 
ATOM   801  C CB  . CYS   A 1 112 ? 10.369  22.691 -8.968  1.00 16.31 ? 134 CYS   A CB  1 
ATOM   802  S SG  . CYS   A 1 112 ? 11.881  22.339 -8.029  1.00 16.41 ? 134 CYS   A SG  1 
ATOM   803  N N   . CYS   A 1 113 ? 10.225  21.430 -11.936 1.00 14.40 ? 135 CYS   A N   1 
ATOM   804  C CA  . CYS   A 1 113 ? 10.815  20.912 -13.159 1.00 15.00 ? 135 CYS   A CA  1 
ATOM   805  C C   . CYS   A 1 113 ? 10.823  21.979 -14.247 1.00 15.14 ? 135 CYS   A C   1 
ATOM   806  O O   . CYS   A 1 113 ? 10.017  22.910 -14.229 1.00 15.67 ? 135 CYS   A O   1 
ATOM   807  C CB  . CYS   A 1 113 ? 10.089  19.663 -13.641 1.00 15.59 ? 135 CYS   A CB  1 
ATOM   808  S SG  . CYS   A 1 113 ? 8.305   19.877 -13.895 1.00 16.12 ? 135 CYS   A SG  1 
ATOM   809  N N   . ASN   A 1 114 ? 11.738  21.801 -15.209 1.00 15.41 ? 136 ASN   A N   1 
ATOM   810  C CA  . ASN   A 1 114 ? 11.873  22.689 -16.350 1.00 16.21 ? 136 ASN   A CA  1 
ATOM   811  C C   . ASN   A 1 114 ? 12.735  22.004 -17.406 1.00 16.50 ? 136 ASN   A C   1 
ATOM   812  O O   . ASN   A 1 114 ? 13.666  21.272 -17.057 1.00 16.76 ? 136 ASN   A O   1 
ATOM   813  C CB  . ASN   A 1 114 ? 12.491  24.037 -15.971 1.00 17.01 ? 136 ASN   A CB  1 
ATOM   814  C CG  . ASN   A 1 114 ? 11.466  25.125 -15.732 1.00 17.55 ? 136 ASN   A CG  1 
ATOM   815  O OD1 . ASN   A 1 114 ? 10.570  25.329 -16.563 1.00 19.17 ? 136 ASN   A OD1 1 
ATOM   816  N ND2 . ASN   A 1 114 ? 11.602  25.866 -14.636 1.00 17.70 ? 136 ASN   A ND2 1 
ATOM   817  N N   . PHE   A 1 115 ? 12.409  22.257 -18.685 1.00 16.89 ? 137 PHE   A N   1 
ATOM   818  C CA  . PHE   A 1 115 ? 13.284  21.920 -19.792 1.00 16.62 ? 137 PHE   A CA  1 
ATOM   819  C C   . PHE   A 1 115 ? 14.310  23.026 -19.980 1.00 16.92 ? 137 PHE   A C   1 
ATOM   820  O O   . PHE   A 1 115 ? 14.055  24.189 -19.665 1.00 17.19 ? 137 PHE   A O   1 
ATOM   821  C CB  . PHE   A 1 115 ? 12.522  21.815 -21.118 1.00 17.22 ? 137 PHE   A CB  1 
ATOM   822  C CG  . PHE   A 1 115 ? 11.652  20.593 -21.337 1.00 16.78 ? 137 PHE   A CG  1 
ATOM   823  C CD1 . PHE   A 1 115 ? 10.341  20.542 -20.855 1.00 16.11 ? 137 PHE   A CD1 1 
ATOM   824  C CD2 . PHE   A 1 115 ? 12.140  19.500 -22.037 1.00 17.23 ? 137 PHE   A CD2 1 
ATOM   825  C CE1 . PHE   A 1 115 ? 9.560   19.422 -21.064 1.00 16.17 ? 137 PHE   A CE1 1 
ATOM   826  C CE2 . PHE   A 1 115 ? 11.336  18.396 -22.268 1.00 17.03 ? 137 PHE   A CE2 1 
ATOM   827  C CZ  . PHE   A 1 115 ? 10.054  18.358 -21.781 1.00 16.54 ? 137 PHE   A CZ  1 
ATOM   828  N N   . ASN   A 1 116 ? 15.448  22.667 -20.572 1.00 17.56 ? 138 ASN   A N   1 
ATOM   829  C CA  . ASN   A 1 116 ? 16.372  23.668 -21.078 1.00 17.30 ? 138 ASN   A CA  1 
ATOM   830  C C   . ASN   A 1 116 ? 15.864  24.210 -22.420 1.00 18.66 ? 138 ASN   A C   1 
ATOM   831  O O   . ASN   A 1 116 ? 14.948  23.670 -23.038 1.00 19.09 ? 138 ASN   A O   1 
ATOM   832  C CB  . ASN   A 1 116 ? 17.806  23.148 -21.091 1.00 17.07 ? 138 ASN   A CB  1 
ATOM   833  C CG  . ASN   A 1 116 ? 18.043  22.050 -22.096 1.00 17.36 ? 138 ASN   A CG  1 
ATOM   834  O OD1 . ASN   A 1 116 ? 17.116  21.361 -22.534 1.00 17.28 ? 138 ASN   A OD1 1 
ATOM   835  N ND2 . ASN   A 1 116 ? 19.304  21.824 -22.412 1.00 18.67 ? 138 ASN   A ND2 1 
ATOM   836  N N   . PRO   A 1 117 ? 16.433  25.331 -22.915 1.00 20.01 ? 139 PRO   A N   1 
ATOM   837  C CA  . PRO   A 1 117 ? 16.039  25.881 -24.217 1.00 20.84 ? 139 PRO   A CA  1 
ATOM   838  C C   . PRO   A 1 117 ? 16.115  24.908 -25.398 1.00 20.85 ? 139 PRO   A C   1 
ATOM   839  O O   . PRO   A 1 117 ? 15.183  24.824 -26.194 1.00 21.39 ? 139 PRO   A O   1 
ATOM   840  C CB  . PRO   A 1 117 ? 17.020  27.054 -24.357 1.00 21.10 ? 139 PRO   A CB  1 
ATOM   841  C CG  . PRO   A 1 117 ? 17.215  27.504 -22.928 1.00 20.72 ? 139 PRO   A CG  1 
ATOM   842  C CD  . PRO   A 1 117 ? 17.384  26.190 -22.193 1.00 20.19 ? 139 PRO   A CD  1 
ATOM   843  N N   . GLN   A 1 118 ? 17.208  24.140 -25.472 1.00 20.09 ? 140 GLN   A N   1 
ATOM   844  C CA  . GLN   A 1 118 ? 17.360  23.114 -26.491 1.00 20.37 ? 140 GLN   A CA  1 
ATOM   845  C C   . GLN   A 1 118 ? 16.294  22.034 -26.319 1.00 20.00 ? 140 GLN   A C   1 
ATOM   846  O O   . GLN   A 1 118 ? 15.858  21.440 -27.306 1.00 21.57 ? 140 GLN   A O   1 
ATOM   847  C CB  . GLN   A 1 118 ? 18.763  22.516 -26.415 1.00 21.11 ? 140 GLN   A CB  1 
ATOM   848  C CG  . GLN   A 1 118 ? 19.046  21.473 -27.493 1.00 22.93 ? 140 GLN   A CG  1 
ATOM   849  C CD  . GLN   A 1 118 ? 20.470  20.971 -27.482 1.00 23.81 ? 140 GLN   A CD  1 
ATOM   850  O OE1 . GLN   A 1 118 ? 21.377  21.634 -26.977 1.00 27.95 ? 140 GLN   A OE1 1 
ATOM   851  N NE2 . GLN   A 1 118 ? 20.686  19.792 -28.040 1.00 25.73 ? 140 GLN   A NE2 1 
ATOM   852  N N   . SER   A 1 119 ? 15.928  21.783 -25.051 1.00 19.55 ? 141 SER   A N   1 
ATOM   853  C CA  . SER   A 1 119 ? 14.914  20.831 -24.623 1.00 18.71 ? 141 SER   A CA  1 
ATOM   854  C C   . SER   A 1 119 ? 15.402  19.388 -24.762 1.00 19.02 ? 141 SER   A C   1 
ATOM   855  O O   . SER   A 1 119 ? 14.589  18.472 -24.824 1.00 19.77 ? 141 SER   A O   1 
ATOM   856  C CB  . SER   A 1 119 ? 13.573  21.048 -25.296 1.00 18.55 ? 141 SER   A CB  1 
ATOM   857  O OG  . SER   A 1 119 ? 12.946  22.209 -24.781 1.00 18.03 ? 141 SER   A OG  1 
ATOM   858  N N   . ASN   A 1 120 ? 16.729  19.199 -24.734 1.00 18.34 ? 142 ASN   A N   1 
ATOM   859  C CA  . ASN   A 1 120 ? 17.332  17.879 -24.653 1.00 19.62 ? 142 ASN   A CA  1 
ATOM   860  C C   . ASN   A 1 120 ? 17.493  17.455 -23.194 1.00 18.43 ? 142 ASN   A C   1 
ATOM   861  O O   . ASN   A 1 120 ? 17.737  16.283 -22.928 1.00 18.23 ? 142 ASN   A O   1 
ATOM   862  C CB  . ASN   A 1 120 ? 18.661  17.834 -25.393 1.00 19.78 ? 142 ASN   A CB  1 
ATOM   863  C CG  . ASN   A 1 120 ? 19.675  18.778 -24.784 1.00 21.23 ? 142 ASN   A CG  1 
ATOM   864  O OD1 . ASN   A 1 120 ? 19.390  19.961 -24.559 1.00 21.61 ? 142 ASN   A OD1 1 
ATOM   865  N ND2 . ASN   A 1 120 ? 20.865  18.278 -24.507 1.00 22.55 ? 142 ASN   A ND2 1 
ATOM   866  N N   . LEU   A 1 121 ? 17.349  18.411 -22.259 1.00 18.70 ? 143 LEU   A N   1 
ATOM   867  C CA  . LEU   A 1 121 ? 17.523  18.184 -20.834 1.00 17.41 ? 143 LEU   A CA  1 
ATOM   868  C C   . LEU   A 1 121 ? 16.279  18.649 -20.090 1.00 16.95 ? 143 LEU   A C   1 
ATOM   869  O O   . LEU   A 1 121 ? 15.565  19.547 -20.529 1.00 16.30 ? 143 LEU   A O   1 
ATOM   870  C CB  . LEU   A 1 121 ? 18.721  18.939 -20.267 1.00 17.99 ? 143 LEU   A CB  1 
ATOM   871  C CG  . LEU   A 1 121 ? 20.094  18.586 -20.841 1.00 18.42 ? 143 LEU   A CG  1 
ATOM   872  C CD1 . LEU   A 1 121 ? 21.095  19.456 -20.122 1.00 19.90 ? 143 LEU   A CD1 1 
ATOM   873  C CD2 . LEU   A 1 121 ? 20.435  17.116 -20.692 1.00 18.84 ? 143 LEU   A CD2 1 
ATOM   874  N N   . ILE   A 1 122 ? 16.051  17.995 -18.957 1.00 17.40 ? 144 ILE   A N   1 
ATOM   875  C CA  . ILE   A 1 122 ? 15.112  18.418 -17.936 1.00 16.52 ? 144 ILE   A CA  1 
ATOM   876  C C   . ILE   A 1 122 ? 15.888  18.522 -16.633 1.00 15.67 ? 144 ILE   A C   1 
ATOM   877  O O   . ILE   A 1 122 ? 16.740  17.680 -16.343 1.00 16.11 ? 144 ILE   A O   1 
ATOM   878  C CB  . ILE   A 1 122 ? 13.964  17.405 -17.814 1.00 16.92 ? 144 ILE   A CB  1 
ATOM   879  C CG1 . ILE   A 1 122 ? 13.054  17.488 -19.031 1.00 16.74 ? 144 ILE   A CG1 1 
ATOM   880  C CG2 . ILE   A 1 122 ? 13.185  17.576 -16.508 1.00 16.79 ? 144 ILE   A CG2 1 
ATOM   881  C CD1 . ILE   A 1 122 ? 12.186  16.264 -19.221 1.00 16.78 ? 144 ILE   A CD1 1 
ATOM   882  N N   . VAL   A 1 123 ? 15.555  19.541 -15.859 1.00 15.31 ? 145 VAL   A N   1 
ATOM   883  C CA  . VAL   A 1 123 ? 16.035  19.689 -14.499 1.00 15.63 ? 145 VAL   A CA  1 
ATOM   884  C C   . VAL   A 1 123 ? 14.849  19.554 -13.551 1.00 15.64 ? 145 VAL   A C   1 
ATOM   885  O O   . VAL   A 1 123 ? 13.740  20.026 -13.847 1.00 15.36 ? 145 VAL   A O   1 
ATOM   886  C CB  . VAL   A 1 123 ? 16.775  21.027 -14.291 1.00 15.89 ? 145 VAL   A CB  1 
ATOM   887  C CG1 . VAL   A 1 123 ? 15.861  22.239 -14.476 1.00 16.01 ? 145 VAL   A CG1 1 
ATOM   888  C CG2 . VAL   A 1 123 ? 17.450  21.088 -12.921 1.00 16.93 ? 145 VAL   A CG2 1 
ATOM   889  N N   . SER   A 1 124 ? 15.122  18.911 -12.413 1.00 15.04 ? 146 SER   A N   1 
ATOM   890  C CA  . SER   A 1 124 ? 14.120  18.665 -11.389 1.00 15.54 ? 146 SER   A CA  1 
ATOM   891  C C   . SER   A 1 124 ? 14.680  18.998 -10.011 1.00 16.21 ? 146 SER   A C   1 
ATOM   892  O O   . SER   A 1 124 ? 15.880  18.862 -9.792  1.00 16.07 ? 146 SER   A O   1 
ATOM   893  C CB  . SER   A 1 124 ? 13.647  17.234 -11.414 1.00 15.87 ? 146 SER   A CB  1 
ATOM   894  O OG  . SER   A 1 124 ? 14.695  16.305 -11.154 1.00 16.02 ? 146 SER   A OG  1 
ATOM   895  N N   . GLY   A 1 125 ? 13.776  19.378 -9.093  1.00 16.31 ? 147 GLY   A N   1 
ATOM   896  C CA  . GLY   A 1 125 ? 14.083  19.554 -7.684  1.00 17.17 ? 147 GLY   A CA  1 
ATOM   897  C C   . GLY   A 1 125 ? 13.104  18.768 -6.821  1.00 16.98 ? 147 GLY   A C   1 
ATOM   898  O O   . GLY   A 1 125 ? 11.938  18.604 -7.183  1.00 17.52 ? 147 GLY   A O   1 
ATOM   899  N N   . SER   A 1 126 ? 13.596  18.281 -5.678  1.00 16.53 ? 148 SER   A N   1 
ATOM   900  C CA  . SER   A 1 126 ? 12.846  17.331 -4.874  1.00 16.76 ? 148 SER   A CA  1 
ATOM   901  C C   . SER   A 1 126 ? 12.939  17.650 -3.380  1.00 16.56 ? 148 SER   A C   1 
ATOM   902  O O   . SER   A 1 126 ? 13.824  18.366 -2.908  1.00 16.58 ? 148 SER   A O   1 
ATOM   903  C CB  . SER   A 1 126 ? 13.309  15.922 -5.198  1.00 16.55 ? 148 SER   A CB  1 
ATOM   904  O OG  . SER   A 1 126 ? 12.762  14.945 -4.322  1.00 16.81 ? 148 SER   A OG  1 
ATOM   905  N N   . PHE   A 1 127 ? 11.973  17.104 -2.636  1.00 17.12 ? 149 PHE   A N   1 
ATOM   906  C CA  . PHE   A 1 127 ? 12.024  17.096 -1.185  1.00 18.12 ? 149 PHE   A CA  1 
ATOM   907  C C   . PHE   A 1 127 ? 13.230  16.305 -0.696  1.00 17.46 ? 149 PHE   A C   1 
ATOM   908  O O   . PHE   A 1 127 ? 13.590  16.452 0.457   1.00 18.51 ? 149 PHE   A O   1 
ATOM   909  C CB  . PHE   A 1 127 ? 10.688  16.567 -0.660  1.00 18.97 ? 149 PHE   A CB  1 
ATOM   910  C CG  . PHE   A 1 127 ? 9.671   17.688 -0.540  1.00 22.47 ? 149 PHE   A CG  1 
ATOM   911  C CD1 . PHE   A 1 127 ? 9.043   18.199 -1.667  1.00 24.44 ? 149 PHE   A CD1 1 
ATOM   912  C CD2 . PHE   A 1 127 ? 9.362   18.247 0.701   1.00 26.56 ? 149 PHE   A CD2 1 
ATOM   913  C CE1 . PHE   A 1 127 ? 8.123   19.227 -1.560  1.00 25.52 ? 149 PHE   A CE1 1 
ATOM   914  C CE2 . PHE   A 1 127 ? 8.445   19.285 0.794   1.00 27.73 ? 149 PHE   A CE2 1 
ATOM   915  C CZ  . PHE   A 1 127 ? 7.838   19.775 -0.339  1.00 26.06 ? 149 PHE   A CZ  1 
ATOM   916  N N   . ASP   A 1 128 ? 13.832  15.483 -1.566  1.00 17.96 ? 150 ASP   A N   1 
ATOM   917  C CA  . ASP   A 1 128 ? 15.003  14.690 -1.243  1.00 18.48 ? 150 ASP   A CA  1 
ATOM   918  C C   . ASP   A 1 128 ? 16.273  15.550 -1.180  1.00 19.13 ? 150 ASP   A C   1 
ATOM   919  O O   . ASP   A 1 128 ? 17.348  15.015 -0.901  1.00 19.35 ? 150 ASP   A O   1 
ATOM   920  C CB  . ASP   A 1 128 ? 15.108  13.480 -2.162  1.00 18.27 ? 150 ASP   A CB  1 
ATOM   921  C CG  . ASP   A 1 128 ? 15.609  13.736 -3.574  1.00 16.74 ? 150 ASP   A CG  1 
ATOM   922  O OD1 . ASP   A 1 128 ? 15.998  14.886 -3.866  1.00 16.74 ? 150 ASP   A OD1 1 
ATOM   923  O OD2 . ASP   A 1 128 ? 15.571  12.798 -4.383  1.00 17.77 ? 150 ASP   A OD2 1 
ATOM   924  N N   . GLU   A 1 129 ? 16.132  16.860 -1.450  1.00 19.33 ? 151 GLU   A N   1 
ATOM   925  C CA  . GLU   A 1 129 ? 17.153  17.880 -1.273  1.00 19.00 ? 151 GLU   A CA  1 
ATOM   926  C C   . GLU   A 1 129 ? 18.127  17.919 -2.452  1.00 19.00 ? 151 GLU   A C   1 
ATOM   927  O O   . GLU   A 1 129 ? 19.111  18.651 -2.391  1.00 19.13 ? 151 GLU   A O   1 
ATOM   928  C CB  . GLU   A 1 129 ? 17.921  17.728 0.048   1.00 19.41 ? 151 GLU   A CB  1 
ATOM   929  C CG  . GLU   A 1 129 ? 16.982  17.551 1.238   1.00 19.71 ? 151 GLU   A CG  1 
ATOM   930  C CD  . GLU   A 1 129 ? 17.594  17.542 2.615   1.00 20.31 ? 151 GLU   A CD  1 
ATOM   931  O OE1 . GLU   A 1 129 ? 18.838  17.502 2.738   1.00 21.77 ? 151 GLU   A OE1 1 
ATOM   932  O OE2 . GLU   A 1 129 ? 16.779  17.551 3.567   1.00 21.36 ? 151 GLU   A OE2 1 
ATOM   933  N N   . SER   A 1 130 ? 17.828  17.169 -3.520  1.00 17.96 ? 152 SER   A N   1 
ATOM   934  C CA  . SER   A 1 130 ? 18.702  17.079 -4.672  1.00 18.88 ? 152 SER   A CA  1 
ATOM   935  C C   . SER   A 1 130 ? 18.092  17.807 -5.864  1.00 18.50 ? 152 SER   A C   1 
ATOM   936  O O   . SER   A 1 130 ? 16.881  18.014 -5.935  1.00 18.57 ? 152 SER   A O   1 
ATOM   937  C CB  . SER   A 1 130 ? 18.985  15.630 -5.029  1.00 20.25 ? 152 SER   A CB  1 
ATOM   938  O OG  . SER   A 1 130 ? 17.895  15.027 -5.714  1.00 19.98 ? 152 SER   A OG  1 
ATOM   939  N N   . VAL   A 1 131 ? 18.972  18.178 -6.796  1.00 19.22 ? 153 VAL   A N   1 
ATOM   940  C CA  . VAL   A 1 131 ? 18.585  18.615 -8.121  1.00 17.95 ? 153 VAL   A CA  1 
ATOM   941  C C   . VAL   A 1 131 ? 19.067  17.543 -9.091  1.00 17.32 ? 153 VAL   A C   1 
ATOM   942  O O   . VAL   A 1 131 ? 20.200  17.110 -8.979  1.00 17.09 ? 153 VAL   A O   1 
ATOM   943  C CB  . VAL   A 1 131 ? 19.189  19.998 -8.432  1.00 18.36 ? 153 VAL   A CB  1 
ATOM   944  C CG1 . VAL   A 1 131 ? 19.131  20.327 -9.925  1.00 18.07 ? 153 VAL   A CG1 1 
ATOM   945  C CG2 . VAL   A 1 131 ? 18.546  21.102 -7.591  1.00 17.63 ? 153 VAL   A CG2 1 
ATOM   946  N N   . ARG   A 1 132 ? 18.203  17.076 -10.003 1.00 17.95 ? 154 ARG   A N   1 
ATOM   947  C CA  A ARG   A 1 132 ? 18.617  16.085 -10.984 0.50 18.27 ? 154 ARG   A CA  1 
ATOM   948  C CA  B ARG   A 1 132 ? 18.601  16.078 -10.985 0.50 18.31 ? 154 ARG   A CA  1 
ATOM   949  C C   . ARG   A 1 132 ? 18.507  16.674 -12.389 1.00 18.18 ? 154 ARG   A C   1 
ATOM   950  O O   . ARG   A 1 132 ? 17.640  17.500 -12.660 1.00 17.17 ? 154 ARG   A O   1 
ATOM   951  C CB  A ARG   A 1 132 ? 17.837  14.781 -10.789 0.50 18.91 ? 154 ARG   A CB  1 
ATOM   952  C CB  B ARG   A 1 132 ? 17.782  14.795 -10.800 0.50 19.39 ? 154 ARG   A CB  1 
ATOM   953  C CG  A ARG   A 1 132 ? 18.293  13.977 -9.575  0.50 19.64 ? 154 ARG   A CG  1 
ATOM   954  C CG  B ARG   A 1 132 ? 18.358  13.846 -9.752  0.50 20.31 ? 154 ARG   A CG  1 
ATOM   955  C CD  A ARG   A 1 132 ? 17.498  12.683 -9.413  0.50 19.75 ? 154 ARG   A CD  1 
ATOM   956  C CD  B ARG   A 1 132 ? 17.444  12.658 -9.433  0.50 20.92 ? 154 ARG   A CD  1 
ATOM   957  N NE  A ARG   A 1 132 ? 17.992  11.820 -8.331  0.50 20.25 ? 154 ARG   A NE  1 
ATOM   958  N NE  B ARG   A 1 132 ? 18.174  11.516 -8.866  0.50 22.04 ? 154 ARG   A NE  1 
ATOM   959  C CZ  A ARG   A 1 132 ? 18.553  10.624 -8.512  0.50 20.10 ? 154 ARG   A CZ  1 
ATOM   960  C CZ  B ARG   A 1 132 ? 18.542  11.324 -7.595  0.50 21.66 ? 154 ARG   A CZ  1 
ATOM   961  N NH1 A ARG   A 1 132 ? 18.795  10.158 -9.732  0.50 20.24 ? 154 ARG   A NH1 1 
ATOM   962  N NH1 B ARG   A 1 132 ? 18.088  12.076 -6.604  0.50 21.90 ? 154 ARG   A NH1 1 
ATOM   963  N NH2 A ARG   A 1 132 ? 18.852  9.887  -7.462  0.50 20.01 ? 154 ARG   A NH2 1 
ATOM   964  N NH2 B ARG   A 1 132 ? 19.365  10.335 -7.314  0.50 22.06 ? 154 ARG   A NH2 1 
ATOM   965  N N   . ILE   A 1 133 ? 19.454  16.277 -13.253 1.00 18.34 ? 155 ILE   A N   1 
ATOM   966  C CA  . ILE   A 1 133 ? 19.467  16.657 -14.656 1.00 17.83 ? 155 ILE   A CA  1 
ATOM   967  C C   . ILE   A 1 133 ? 19.248  15.384 -15.476 1.00 18.15 ? 155 ILE   A C   1 
ATOM   968  O O   . ILE   A 1 133 ? 19.965  14.399 -15.301 1.00 18.97 ? 155 ILE   A O   1 
ATOM   969  C CB  . ILE   A 1 133 ? 20.766  17.394 -15.047 1.00 18.78 ? 155 ILE   A CB  1 
ATOM   970  C CG1 . ILE   A 1 133 ? 21.029  18.632 -14.168 1.00 18.84 ? 155 ILE   A CG1 1 
ATOM   971  C CG2 . ILE   A 1 133 ? 20.743  17.753 -16.539 1.00 18.83 ? 155 ILE   A CG2 1 
ATOM   972  C CD1 . ILE   A 1 133 ? 22.385  19.287 -14.397 1.00 20.58 ? 155 ILE   A CD1 1 
ATOM   973  N N   . TRP   A 1 134 ? 18.241  15.420 -16.364 1.00 16.82 ? 156 TRP   A N   1 
ATOM   974  C CA  . TRP   A 1 134 ? 17.778  14.231 -17.056 1.00 17.73 ? 156 TRP   A CA  1 
ATOM   975  C C   . TRP   A 1 134 ? 17.917  14.392 -18.566 1.00 18.30 ? 156 TRP   A C   1 
ATOM   976  O O   . TRP   A 1 134 ? 17.666  15.467 -19.105 1.00 17.31 ? 156 TRP   A O   1 
ATOM   977  C CB  . TRP   A 1 134 ? 16.303  13.998 -16.731 1.00 18.01 ? 156 TRP   A CB  1 
ATOM   978  C CG  . TRP   A 1 134 ? 15.952  13.994 -15.277 1.00 17.98 ? 156 TRP   A CG  1 
ATOM   979  C CD1 . TRP   A 1 134 ? 15.649  15.054 -14.473 1.00 17.65 ? 156 TRP   A CD1 1 
ATOM   980  C CD2 . TRP   A 1 134 ? 15.756  12.818 -14.481 1.00 17.35 ? 156 TRP   A CD2 1 
ATOM   981  N NE1 . TRP   A 1 134 ? 15.329  14.623 -13.221 1.00 16.62 ? 156 TRP   A NE1 1 
ATOM   982  C CE2 . TRP   A 1 134 ? 15.371  13.259 -13.202 1.00 17.54 ? 156 TRP   A CE2 1 
ATOM   983  C CE3 . TRP   A 1 134 ? 15.873  11.449 -14.721 1.00 18.06 ? 156 TRP   A CE3 1 
ATOM   984  C CZ2 . TRP   A 1 134 ? 15.109  12.367 -12.171 1.00 17.97 ? 156 TRP   A CZ2 1 
ATOM   985  C CZ3 . TRP   A 1 134 ? 15.602  10.570 -13.694 1.00 17.53 ? 156 TRP   A CZ3 1 
ATOM   986  C CH2 . TRP   A 1 134 ? 15.231  11.027 -12.444 1.00 17.44 ? 156 TRP   A CH2 1 
ATOM   987  N N   . ASP   A 1 135 ? 18.253  13.284 -19.230 1.00 19.37 ? 157 ASP   A N   1 
ATOM   988  C CA  . ASP   A 1 135 ? 18.250  13.201 -20.674 1.00 21.04 ? 157 ASP   A CA  1 
ATOM   989  C C   . ASP   A 1 135 ? 16.833  12.917 -21.175 1.00 20.19 ? 157 ASP   A C   1 
ATOM   990  O O   . ASP   A 1 135 ? 16.257  11.873 -20.875 1.00 20.01 ? 157 ASP   A O   1 
ATOM   991  C CB  . ASP   A 1 135 ? 19.191  12.114 -21.156 1.00 23.15 ? 157 ASP   A CB  1 
ATOM   992  C CG  . ASP   A 1 135 ? 19.416  12.126 -22.659 1.00 26.11 ? 157 ASP   A CG  1 
ATOM   993  O OD1 . ASP   A 1 135 ? 20.229  12.946 -23.112 1.00 30.64 ? 157 ASP   A OD1 1 
ATOM   994  O OD2 . ASP   A 1 135 ? 18.706  11.386 -23.363 1.00 29.43 ? 157 ASP   A OD2 1 
ATOM   995  N N   . VAL   A 1 136 ? 16.283  13.846 -21.965 1.00 19.48 ? 158 VAL   A N   1 
ATOM   996  C CA  . VAL   A 1 136 ? 14.911  13.740 -22.452 1.00 19.42 ? 158 VAL   A CA  1 
ATOM   997  C C   . VAL   A 1 136 ? 14.745  12.501 -23.334 1.00 21.08 ? 158 VAL   A C   1 
ATOM   998  O O   . VAL   A 1 136 ? 13.748  11.786 -23.203 1.00 21.19 ? 158 VAL   A O   1 
ATOM   999  C CB  . VAL   A 1 136 ? 14.460  15.021 -23.193 1.00 18.70 ? 158 VAL   A CB  1 
ATOM   1000 C CG1 . VAL   A 1 136 ? 13.126  14.833 -23.915 1.00 18.81 ? 158 VAL   A CG1 1 
ATOM   1001 C CG2 . VAL   A 1 136 ? 14.389  16.228 -22.263 1.00 17.87 ? 158 VAL   A CG2 1 
ATOM   1002 N N   . LYS   A 1 137 ? 15.712  12.254 -24.234 1.00 22.55 ? 159 LYS   A N   1 
ATOM   1003 C CA  . LYS   A 1 137 ? 15.599  11.173 -25.208 1.00 24.93 ? 159 LYS   A CA  1 
ATOM   1004 C C   . LYS   A 1 137 ? 15.625  9.801  -24.530 1.00 26.01 ? 159 LYS   A C   1 
ATOM   1005 O O   . LYS   A 1 137 ? 14.851  8.937  -24.922 1.00 26.25 ? 159 LYS   A O   1 
ATOM   1006 C CB  . LYS   A 1 137 ? 16.690  11.174 -26.286 1.00 27.68 ? 159 LYS   A CB  1 
ATOM   1007 C CG  . LYS   A 1 137 ? 16.226  10.728 -27.677 1.00 32.60 ? 159 LYS   A CG  1 
ATOM   1008 N N   . THR   A 1 138 ? 16.522  9.582  -23.557 1.00 26.03 ? 160 THR   A N   1 
ATOM   1009 C CA  . THR   A 1 138 ? 16.660  8.256  -22.960 1.00 26.24 ? 160 THR   A CA  1 
ATOM   1010 C C   . THR   A 1 138 ? 15.844  8.149  -21.673 1.00 25.69 ? 160 THR   A C   1 
ATOM   1011 O O   . THR   A 1 138 ? 15.539  7.050  -21.230 1.00 28.60 ? 160 THR   A O   1 
ATOM   1012 C CB  . THR   A 1 138 ? 18.120  7.906  -22.671 1.00 27.41 ? 160 THR   A CB  1 
ATOM   1013 O OG1 . THR   A 1 138 ? 18.592  8.848  -21.713 1.00 28.53 ? 160 THR   A OG1 1 
ATOM   1014 C CG2 . THR   A 1 138 ? 18.976  7.874  -23.926 1.00 29.46 ? 160 THR   A CG2 1 
ATOM   1015 N N   . GLY   A 1 139 ? 15.564  9.280  -21.033 1.00 23.43 ? 161 GLY   A N   1 
ATOM   1016 C CA  . GLY   A 1 139 ? 14.830  9.274  -19.781 1.00 25.19 ? 161 GLY   A CA  1 
ATOM   1017 C C   . GLY   A 1 139 ? 15.722  8.879  -18.610 1.00 26.00 ? 161 GLY   A C   1 
ATOM   1018 O O   . GLY   A 1 139 ? 15.228  8.622  -17.525 1.00 28.27 ? 161 GLY   A O   1 
ATOM   1019 N N   . LYS   A 1 140 ? 17.042  8.857  -18.834 1.00 25.46 ? 162 LYS   A N   1 
ATOM   1020 C CA  . LYS   A 1 140 ? 17.986  8.517  -17.782 1.00 26.20 ? 162 LYS   A CA  1 
ATOM   1021 C C   . LYS   A 1 140 ? 18.469  9.790  -17.090 1.00 24.15 ? 162 LYS   A C   1 
ATOM   1022 O O   . LYS   A 1 140 ? 18.574  10.862 -17.703 1.00 23.00 ? 162 LYS   A O   1 
ATOM   1023 C CB  . LYS   A 1 140 ? 19.163  7.729  -18.365 1.00 27.50 ? 162 LYS   A CB  1 
ATOM   1024 C CG  . LYS   A 1 140 ? 18.787  6.394  -19.020 1.00 30.17 ? 162 LYS   A CG  1 
ATOM   1025 N N   . CYS   A 1 141 ? 18.748  9.643  -15.789 1.00 22.26 ? 163 CYS   A N   1 
ATOM   1026 C CA  . CYS   A 1 141 ? 19.360  10.698 -15.009 1.00 21.01 ? 163 CYS   A CA  1 
ATOM   1027 C C   . CYS   A 1 141 ? 20.831  10.804 -15.405 1.00 21.67 ? 163 CYS   A C   1 
ATOM   1028 O O   . CYS   A 1 141 ? 21.559  9.817  -15.342 1.00 23.36 ? 163 CYS   A O   1 
ATOM   1029 C CB  . CYS   A 1 141 ? 19.209  10.432 -13.516 1.00 20.78 ? 163 CYS   A CB  1 
ATOM   1030 S SG  . CYS   A 1 141 ? 19.809  11.809 -12.510 1.00 23.37 ? 163 CYS   A SG  1 
ATOM   1031 N N   . LEU   A 1 142 ? 21.255  12.007 -15.801 1.00 21.56 ? 164 LEU   A N   1 
ATOM   1032 C CA  . LEU   A 1 142 ? 22.641  12.276 -16.160 1.00 22.19 ? 164 LEU   A CA  1 
ATOM   1033 C C   . LEU   A 1 142 ? 23.452  12.687 -14.937 1.00 21.95 ? 164 LEU   A C   1 
ATOM   1034 O O   . LEU   A 1 142 ? 24.598  12.271 -14.777 1.00 24.65 ? 164 LEU   A O   1 
ATOM   1035 C CB  . LEU   A 1 142 ? 22.682  13.369 -17.226 1.00 22.61 ? 164 LEU   A CB  1 
ATOM   1036 C CG  . LEU   A 1 142 ? 22.069  12.988 -18.576 1.00 24.84 ? 164 LEU   A CG  1 
ATOM   1037 C CD1 . LEU   A 1 142 ? 21.999  14.209 -19.450 1.00 25.67 ? 164 LEU   A CD1 1 
ATOM   1038 C CD2 . LEU   A 1 142 ? 22.854  11.887 -19.252 1.00 27.63 ? 164 LEU   A CD2 1 
ATOM   1039 N N   . LYS   A 1 143 ? 22.871  13.541 -14.092 1.00 21.72 ? 165 LYS   A N   1 
ATOM   1040 C CA  . LYS   A 1 143 ? 23.562  14.014 -12.904 1.00 22.38 ? 165 LYS   A CA  1 
ATOM   1041 C C   . LYS   A 1 143 ? 22.578  14.187 -11.753 1.00 21.63 ? 165 LYS   A C   1 
ATOM   1042 O O   . LYS   A 1 143 ? 21.432  14.586 -11.969 1.00 21.14 ? 165 LYS   A O   1 
ATOM   1043 C CB  . LYS   A 1 143 ? 24.251  15.365 -13.096 1.00 22.82 ? 165 LYS   A CB  1 
ATOM   1044 C CG  . LYS   A 1 143 ? 25.295  15.369 -14.182 1.00 25.23 ? 165 LYS   A CG  1 
ATOM   1045 C CD  . LYS   A 1 143 ? 26.056  16.680 -14.294 1.00 28.03 ? 165 LYS   A CD  1 
ATOM   1046 C CE  . LYS   A 1 143 ? 27.330  16.496 -15.062 1.00 29.71 ? 165 LYS   A CE  1 
ATOM   1047 N NZ  . LYS   A 1 143 ? 27.108  16.170 -16.475 1.00 31.12 ? 165 LYS   A NZ  1 
ATOM   1048 N N   . THR   A 1 144 ? 23.077  13.895 -10.547 1.00 22.20 ? 166 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 144 ? 22.407  14.203 -9.294  1.00 22.47 ? 166 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 144 ? 23.286  15.196 -8.542  1.00 21.60 ? 166 THR   A C   1 
ATOM   1051 O O   . THR   A 1 144 ? 24.438  14.892 -8.210  1.00 21.24 ? 166 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 144 ? 22.181  12.943 -8.458  1.00 23.74 ? 166 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 144 ? 21.424  12.040 -9.257  1.00 25.31 ? 166 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 144 ? 21.434  13.243 -7.171  1.00 22.79 ? 166 THR   A CG2 1 
ATOM   1055 N N   . LEU   A 1 145 ? 22.741  16.399 -8.332  1.00 20.36 ? 167 LEU   A N   1 
ATOM   1056 C CA  . LEU   A 1 145 ? 23.444  17.460 -7.631  1.00 21.29 ? 167 LEU   A CA  1 
ATOM   1057 C C   . LEU   A 1 145 ? 23.019  17.447 -6.167  1.00 21.00 ? 167 LEU   A C   1 
ATOM   1058 O O   . LEU   A 1 145 ? 21.826  17.536 -5.887  1.00 20.94 ? 167 LEU   A O   1 
ATOM   1059 C CB  . LEU   A 1 145 ? 23.143  18.826 -8.241  1.00 21.62 ? 167 LEU   A CB  1 
ATOM   1060 C CG  . LEU   A 1 145 ? 23.241  18.958 -9.765  1.00 23.78 ? 167 LEU   A CG  1 
ATOM   1061 C CD1 . LEU   A 1 145 ? 23.093  20.404 -10.181 1.00 23.37 ? 167 LEU   A CD1 1 
ATOM   1062 C CD2 . LEU   A 1 145 ? 24.493  18.332 -10.313 1.00 25.62 ? 167 LEU   A CD2 1 
ATOM   1063 N N   . PRO   A 1 146 ? 23.957  17.322 -5.200  1.00 22.72 ? 168 PRO   A N   1 
ATOM   1064 C CA  . PRO   A 1 146 ? 23.620  17.438 -3.778  1.00 23.43 ? 168 PRO   A CA  1 
ATOM   1065 C C   . PRO   A 1 146 ? 23.397  18.909 -3.428  1.00 22.63 ? 168 PRO   A C   1 
ATOM   1066 O O   . PRO   A 1 146 ? 24.219  19.545 -2.785  1.00 23.42 ? 168 PRO   A O   1 
ATOM   1067 C CB  . PRO   A 1 146 ? 24.853  16.807 -3.108  1.00 25.45 ? 168 PRO   A CB  1 
ATOM   1068 C CG  . PRO   A 1 146 ? 26.001  17.137 -4.040  1.00 26.03 ? 168 PRO   A CG  1 
ATOM   1069 C CD  . PRO   A 1 146 ? 25.394  17.063 -5.423  1.00 24.54 ? 168 PRO   A CD  1 
ATOM   1070 N N   . ALA   A 1 147 ? 22.278  19.455 -3.913  1.00 20.91 ? 169 ALA   A N   1 
ATOM   1071 C CA  . ALA   A 1 147 ? 22.157  20.881 -4.130  1.00 19.85 ? 169 ALA   A CA  1 
ATOM   1072 C C   . ALA   A 1 147 ? 21.920  21.658 -2.842  1.00 19.25 ? 169 ALA   A C   1 
ATOM   1073 O O   . ALA   A 1 147 ? 22.402  22.786 -2.712  1.00 19.93 ? 169 ALA   A O   1 
ATOM   1074 C CB  . ALA   A 1 147 ? 21.073  21.148 -5.139  1.00 20.31 ? 169 ALA   A CB  1 
ATOM   1075 N N   . HIS   A 1 148 ? 21.178  21.059 -1.913  1.00 18.78 ? 170 HIS   A N   1 
ATOM   1076 C CA  . HIS   A 1 148 ? 20.637  21.790 -0.786  1.00 18.88 ? 170 HIS   A CA  1 
ATOM   1077 C C   . HIS   A 1 148 ? 20.537  20.869 0.423   1.00 19.32 ? 170 HIS   A C   1 
ATOM   1078 O O   . HIS   A 1 148 ? 20.774  19.664 0.310   1.00 19.27 ? 170 HIS   A O   1 
ATOM   1079 C CB  . HIS   A 1 148 ? 19.267  22.374 -1.144  1.00 18.59 ? 170 HIS   A CB  1 
ATOM   1080 C CG  . HIS   A 1 148 ? 19.356  23.460 -2.148  1.00 18.65 ? 170 HIS   A CG  1 
ATOM   1081 N ND1 . HIS   A 1 148 ? 19.778  24.700 -1.730  1.00 19.27 ? 170 HIS   A ND1 1 
ATOM   1082 C CD2 . HIS   A 1 148 ? 19.175  23.544 -3.483  1.00 19.06 ? 170 HIS   A CD2 1 
ATOM   1083 C CE1 . HIS   A 1 148 ? 19.819  25.518 -2.780  1.00 19.59 ? 170 HIS   A CE1 1 
ATOM   1084 N NE2 . HIS   A 1 148 ? 19.442  24.840 -3.850  1.00 19.43 ? 170 HIS   A NE2 1 
ATOM   1085 N N   . SER   A 1 149 ? 20.199  21.472 1.574   1.00 20.02 ? 171 SER   A N   1 
ATOM   1086 C CA  . SER   A 1 149 ? 20.072  20.749 2.829   1.00 20.82 ? 171 SER   A CA  1 
ATOM   1087 C C   . SER   A 1 149 ? 18.629  20.776 3.336   1.00 20.04 ? 171 SER   A C   1 
ATOM   1088 O O   . SER   A 1 149 ? 18.382  20.565 4.521   1.00 21.00 ? 171 SER   A O   1 
ATOM   1089 C CB  . SER   A 1 149 ? 21.040  21.285 3.872   1.00 21.83 ? 171 SER   A CB  1 
ATOM   1090 O OG  . SER   A 1 149 ? 20.780  22.642 4.182   1.00 21.38 ? 171 SER   A OG  1 
ATOM   1091 N N   . ASP   A 1 150 ? 17.682  20.974 2.419   1.00 20.23 ? 172 ASP   A N   1 
ATOM   1092 C CA  . ASP   A 1 150 ? 16.256  20.957 2.700   1.00 20.36 ? 172 ASP   A CA  1 
ATOM   1093 C C   . ASP   A 1 150 ? 15.543  20.888 1.351   1.00 19.80 ? 172 ASP   A C   1 
ATOM   1094 O O   . ASP   A 1 150 ? 16.199  20.957 0.311   1.00 18.17 ? 172 ASP   A O   1 
ATOM   1095 C CB  . ASP   A 1 150 ? 15.808  22.196 3.468   1.00 22.50 ? 172 ASP   A CB  1 
ATOM   1096 C CG  . ASP   A 1 150 ? 15.934  22.159 4.984   1.00 24.55 ? 172 ASP   A CG  1 
ATOM   1097 O OD1 . ASP   A 1 150 ? 15.460  21.164 5.581   1.00 26.20 ? 172 ASP   A OD1 1 
ATOM   1098 O OD2 . ASP   A 1 150 ? 16.475  23.146 5.562   1.00 26.63 ? 172 ASP   A OD2 1 
ATOM   1099 N N   . PRO   A 1 151 ? 14.202  20.725 1.314   1.00 19.27 ? 173 PRO   A N   1 
ATOM   1100 C CA  . PRO   A 1 151 ? 13.478  20.645 0.045   1.00 18.75 ? 173 PRO   A CA  1 
ATOM   1101 C C   . PRO   A 1 151 ? 13.807  21.767 -0.934  1.00 18.60 ? 173 PRO   A C   1 
ATOM   1102 O O   . PRO   A 1 151 ? 13.994  22.924 -0.547  1.00 19.26 ? 173 PRO   A O   1 
ATOM   1103 C CB  . PRO   A 1 151 ? 12.019  20.656 0.489   1.00 19.02 ? 173 PRO   A CB  1 
ATOM   1104 C CG  . PRO   A 1 151 ? 12.072  19.953 1.827   1.00 19.38 ? 173 PRO   A CG  1 
ATOM   1105 C CD  . PRO   A 1 151 ? 13.320  20.528 2.479   1.00 19.75 ? 173 PRO   A CD  1 
ATOM   1106 N N   . VAL   A 1 152 ? 13.900  21.372 -2.204  1.00 17.24 ? 174 VAL   A N   1 
ATOM   1107 C CA  . VAL   A 1 152 ? 14.189  22.293 -3.281  1.00 17.30 ? 174 VAL   A CA  1 
ATOM   1108 C C   . VAL   A 1 152 ? 12.875  22.846 -3.833  1.00 17.10 ? 174 VAL   A C   1 
ATOM   1109 O O   . VAL   A 1 152 ? 12.026  22.093 -4.312  1.00 18.40 ? 174 VAL   A O   1 
ATOM   1110 C CB  . VAL   A 1 152 ? 14.992  21.578 -4.374  1.00 17.11 ? 174 VAL   A CB  1 
ATOM   1111 C CG1 . VAL   A 1 152 ? 15.329  22.550 -5.504  1.00 16.86 ? 174 VAL   A CG1 1 
ATOM   1112 C CG2 . VAL   A 1 152 ? 16.241  20.905 -3.811  1.00 17.94 ? 174 VAL   A CG2 1 
ATOM   1113 N N   . SER   A 1 153 ? 12.751  24.173 -3.819  1.00 17.01 ? 175 SER   A N   1 
ATOM   1114 C CA  . SER   A 1 153 ? 11.496  24.848 -4.134  1.00 16.91 ? 175 SER   A CA  1 
ATOM   1115 C C   . SER   A 1 153 ? 11.400  25.210 -5.614  1.00 16.03 ? 175 SER   A C   1 
ATOM   1116 O O   . SER   A 1 153 ? 10.288  25.319 -6.149  1.00 16.29 ? 175 SER   A O   1 
ATOM   1117 C CB  . SER   A 1 153 ? 11.314  26.069 -3.268  1.00 17.40 ? 175 SER   A CB  1 
ATOM   1118 O OG  . SER   A 1 153 ? 12.489  26.867 -3.291  1.00 18.66 ? 175 SER   A OG  1 
ATOM   1119 N N   . ALA   A 1 154 ? 12.540  25.421 -6.283  1.00 16.20 ? 176 ALA   A N   1 
ATOM   1120 C CA  . ALA   A 1 154 ? 12.495  25.791 -7.694  1.00 15.68 ? 176 ALA   A CA  1 
ATOM   1121 C C   . ALA   A 1 154 ? 13.799  25.431 -8.390  1.00 15.47 ? 176 ALA   A C   1 
ATOM   1122 O O   . ALA   A 1 154 ? 14.843  25.403 -7.757  1.00 15.23 ? 176 ALA   A O   1 
ATOM   1123 C CB  . ALA   A 1 154 ? 12.229  27.265 -7.858  1.00 15.42 ? 176 ALA   A CB  1 
ATOM   1124 N N   . VAL   A 1 155 ? 13.696  25.203 -9.704  1.00 15.86 ? 177 VAL   A N   1 
ATOM   1125 C CA  . VAL   A 1 155 ? 14.827  24.990 -10.591 1.00 15.91 ? 177 VAL   A CA  1 
ATOM   1126 C C   . VAL   A 1 155 ? 14.494  25.625 -11.933 1.00 16.10 ? 177 VAL   A C   1 
ATOM   1127 O O   . VAL   A 1 155 ? 13.369  25.497 -12.414 1.00 16.83 ? 177 VAL   A O   1 
ATOM   1128 C CB  . VAL   A 1 155 ? 15.183  23.502 -10.796 1.00 16.95 ? 177 VAL   A CB  1 
ATOM   1129 C CG1 . VAL   A 1 155 ? 15.813  22.902 -9.544  1.00 17.51 ? 177 VAL   A CG1 1 
ATOM   1130 C CG2 . VAL   A 1 155 ? 13.975  22.672 -11.268 1.00 16.77 ? 177 VAL   A CG2 1 
ATOM   1131 N N   . HIS   A 1 156 ? 15.479  26.287 -12.543 1.00 16.49 ? 178 HIS   A N   1 
ATOM   1132 C CA  . HIS   A 1 156 ? 15.248  26.996 -13.787 1.00 16.58 ? 178 HIS   A CA  1 
ATOM   1133 C C   . HIS   A 1 156 ? 16.568  27.098 -14.556 1.00 17.17 ? 178 HIS   A C   1 
ATOM   1134 O O   . HIS   A 1 156 ? 17.620  27.397 -13.975 1.00 18.37 ? 178 HIS   A O   1 
ATOM   1135 C CB  . HIS   A 1 156 ? 14.627  28.361 -13.468 1.00 16.92 ? 178 HIS   A CB  1 
ATOM   1136 C CG  . HIS   A 1 156 ? 14.187  29.164 -14.659 1.00 17.63 ? 178 HIS   A CG  1 
ATOM   1137 N ND1 . HIS   A 1 156 ? 14.683  30.420 -14.963 1.00 19.37 ? 178 HIS   A ND1 1 
ATOM   1138 C CD2 . HIS   A 1 156 ? 13.321  28.853 -15.637 1.00 18.23 ? 178 HIS   A CD2 1 
ATOM   1139 C CE1 . HIS   A 1 156 ? 14.079  30.860 -16.059 1.00 20.02 ? 178 HIS   A CE1 1 
ATOM   1140 N NE2 . HIS   A 1 156 ? 13.254  29.912 -16.495 1.00 19.25 ? 178 HIS   A NE2 1 
ATOM   1141 N N   . PHE   A 1 157 ? 16.499  26.870 -15.872 1.00 17.35 ? 179 PHE   A N   1 
ATOM   1142 C CA  . PHE   A 1 157 ? 17.627  27.145 -16.749 1.00 17.77 ? 179 PHE   A CA  1 
ATOM   1143 C C   . PHE   A 1 157 ? 17.623  28.600 -17.198 1.00 18.78 ? 179 PHE   A C   1 
ATOM   1144 O O   . PHE   A 1 157 ? 16.559  29.202 -17.358 1.00 19.97 ? 179 PHE   A O   1 
ATOM   1145 C CB  . PHE   A 1 157 ? 17.565  26.299 -18.013 1.00 17.96 ? 179 PHE   A CB  1 
ATOM   1146 C CG  . PHE   A 1 157 ? 17.893  24.831 -17.810 1.00 17.29 ? 179 PHE   A CG  1 
ATOM   1147 C CD1 . PHE   A 1 157 ? 19.215  24.414 -17.771 1.00 17.21 ? 179 PHE   A CD1 1 
ATOM   1148 C CD2 . PHE   A 1 157 ? 16.887  23.877 -17.703 1.00 17.03 ? 179 PHE   A CD2 1 
ATOM   1149 C CE1 . PHE   A 1 157 ? 19.527  23.075 -17.625 1.00 16.97 ? 179 PHE   A CE1 1 
ATOM   1150 C CE2 . PHE   A 1 157 ? 17.209  22.537 -17.581 1.00 16.27 ? 179 PHE   A CE2 1 
ATOM   1151 C CZ  . PHE   A 1 157 ? 18.527  22.139 -17.547 1.00 16.90 ? 179 PHE   A CZ  1 
ATOM   1152 N N   . ASN   A 1 158 ? 18.828  29.135 -17.432 1.00 18.15 ? 180 ASN   A N   1 
ATOM   1153 C CA  . ASN   A 1 158 ? 18.980  30.446 -18.043 1.00 18.79 ? 180 ASN   A CA  1 
ATOM   1154 C C   . ASN   A 1 158 ? 18.760  30.345 -19.556 1.00 19.82 ? 180 ASN   A C   1 
ATOM   1155 O O   . ASN   A 1 158 ? 18.435  29.281 -20.089 1.00 18.73 ? 180 ASN   A O   1 
ATOM   1156 C CB  . ASN   A 1 158 ? 20.332  31.060 -17.684 1.00 19.81 ? 180 ASN   A CB  1 
ATOM   1157 C CG  . ASN   A 1 158 ? 21.493  30.375 -18.366 1.00 19.82 ? 180 ASN   A CG  1 
ATOM   1158 O OD1 . ASN   A 1 158 ? 21.358  29.260 -18.890 1.00 18.95 ? 180 ASN   A OD1 1 
ATOM   1159 N ND2 . ASN   A 1 158 ? 22.644  31.038 -18.386 1.00 21.44 ? 180 ASN   A ND2 1 
ATOM   1160 N N   . ARG   A 1 159 ? 18.972  31.472 -20.242 1.00 21.06 ? 181 ARG   A N   1 
ATOM   1161 C CA  . ARG   A 1 159 ? 18.480  31.683 -21.594 1.00 23.25 ? 181 ARG   A CA  1 
ATOM   1162 C C   . ARG   A 1 159 ? 19.029  30.657 -22.574 1.00 23.22 ? 181 ARG   A C   1 
ATOM   1163 O O   . ARG   A 1 159 ? 18.343  30.330 -23.547 1.00 23.09 ? 181 ARG   A O   1 
ATOM   1164 C CB  . ARG   A 1 159 ? 18.866  33.082 -22.081 1.00 27.56 ? 181 ARG   A CB  1 
ATOM   1165 C CG  . ARG   A 1 159 ? 18.477  33.358 -23.524 1.00 31.72 ? 181 ARG   A CG  1 
ATOM   1166 C CD  . ARG   A 1 159 ? 18.625  34.833 -23.848 1.00 33.98 ? 181 ARG   A CD  1 
ATOM   1167 N NE  . ARG   A 1 159 ? 19.978  35.326 -23.567 1.00 37.94 ? 181 ARG   A NE  1 
ATOM   1168 C CZ  . ARG   A 1 159 ? 20.345  36.603 -23.660 1.00 42.43 ? 181 ARG   A CZ  1 
ATOM   1169 N NH1 . ARG   A 1 159 ? 21.600  36.942 -23.412 1.00 44.77 ? 181 ARG   A NH1 1 
ATOM   1170 N NH2 . ARG   A 1 159 ? 19.464  37.533 -24.013 1.00 42.17 ? 181 ARG   A NH2 1 
ATOM   1171 N N   . ASP   A 1 160 ? 20.271  30.200 -22.358 1.00 21.87 ? 182 ASP   A N   1 
ATOM   1172 C CA  . ASP   A 1 160 ? 20.866  29.235 -23.273 1.00 21.62 ? 182 ASP   A CA  1 
ATOM   1173 C C   . ASP   A 1 160 ? 21.047  27.869 -22.619 1.00 20.94 ? 182 ASP   A C   1 
ATOM   1174 O O   . ASP   A 1 160 ? 21.622  26.970 -23.222 1.00 23.19 ? 182 ASP   A O   1 
ATOM   1175 C CB  . ASP   A 1 160 ? 22.213  29.710 -23.791 1.00 22.60 ? 182 ASP   A CB  1 
ATOM   1176 C CG  . ASP   A 1 160 ? 23.358  29.652 -22.796 1.00 22.70 ? 182 ASP   A CG  1 
ATOM   1177 O OD1 . ASP   A 1 160 ? 23.075  29.855 -21.598 1.00 22.72 ? 182 ASP   A OD1 1 
ATOM   1178 O OD2 . ASP   A 1 160 ? 24.527  29.443 -23.244 1.00 24.94 ? 182 ASP   A OD2 1 
ATOM   1179 N N   . GLY   A 1 161 ? 20.620  27.726 -21.370 1.00 19.52 ? 183 GLY   A N   1 
ATOM   1180 C CA  . GLY   A 1 161 ? 20.697  26.446 -20.687 1.00 19.54 ? 183 GLY   A CA  1 
ATOM   1181 C C   . GLY   A 1 161 ? 22.060  26.169 -20.054 1.00 19.96 ? 183 GLY   A C   1 
ATOM   1182 O O   . GLY   A 1 161 ? 22.267  25.071 -19.539 1.00 19.32 ? 183 GLY   A O   1 
ATOM   1183 N N   . SER   A 1 162 ? 22.981  27.147 -20.098 1.00 20.75 ? 184 SER   A N   1 
ATOM   1184 C CA  . SER   A 1 162 ? 24.327  26.951 -19.571 1.00 19.73 ? 184 SER   A CA  1 
ATOM   1185 C C   . SER   A 1 162 ? 24.330  26.893 -18.048 1.00 19.56 ? 184 SER   A C   1 
ATOM   1186 O O   . SER   A 1 162 ? 25.263  26.345 -17.468 1.00 20.22 ? 184 SER   A O   1 
ATOM   1187 C CB  . SER   A 1 162 ? 25.290  28.005 -20.052 1.00 20.50 ? 184 SER   A CB  1 
ATOM   1188 O OG  . SER   A 1 162 ? 24.844  29.321 -19.763 1.00 20.97 ? 184 SER   A OG  1 
ATOM   1189 N N   . LEU   A 1 163 ? 23.318  27.504 -17.415 1.00 19.58 ? 185 LEU   A N   1 
ATOM   1190 C CA  . LEU   A 1 163 ? 23.229  27.567 -15.966 1.00 19.53 ? 185 LEU   A CA  1 
ATOM   1191 C C   . LEU   A 1 163 ? 21.864  27.083 -15.500 1.00 18.94 ? 185 LEU   A C   1 
ATOM   1192 O O   . LEU   A 1 163 ? 20.864  27.269 -16.182 1.00 19.95 ? 185 LEU   A O   1 
ATOM   1193 C CB  . LEU   A 1 163 ? 23.423  28.999 -15.475 1.00 20.70 ? 185 LEU   A CB  1 
ATOM   1194 C CG  . LEU   A 1 163 ? 24.703  29.720 -15.901 1.00 22.03 ? 185 LEU   A CG  1 
ATOM   1195 C CD1 . LEU   A 1 163 ? 24.649  31.124 -15.319 1.00 22.10 ? 185 LEU   A CD1 1 
ATOM   1196 C CD2 . LEU   A 1 163 ? 25.947  28.988 -15.428 1.00 22.99 ? 185 LEU   A CD2 1 
ATOM   1197 N N   . ILE   A 1 164 ? 21.856  26.569 -14.266 1.00 18.75 ? 186 ILE   A N   1 
ATOM   1198 C CA  . ILE   A 1 164 ? 20.653  26.274 -13.517 1.00 18.71 ? 186 ILE   A CA  1 
ATOM   1199 C C   . ILE   A 1 164 ? 20.667  27.106 -12.243 1.00 18.67 ? 186 ILE   A C   1 
ATOM   1200 O O   . ILE   A 1 164 ? 21.697  27.177 -11.577 1.00 19.19 ? 186 ILE   A O   1 
ATOM   1201 C CB  . ILE   A 1 164 ? 20.612  24.776 -13.182 1.00 18.02 ? 186 ILE   A CB  1 
ATOM   1202 C CG1 . ILE   A 1 164 ? 20.490  23.918 -14.435 1.00 18.04 ? 186 ILE   A CG1 1 
ATOM   1203 C CG2 . ILE   A 1 164 ? 19.509  24.487 -12.173 1.00 17.56 ? 186 ILE   A CG2 1 
ATOM   1204 C CD1 . ILE   A 1 164 ? 20.995  22.497 -14.265 1.00 18.19 ? 186 ILE   A CD1 1 
ATOM   1205 N N   . VAL   A 1 165 ? 19.527  27.729 -11.921 1.00 18.31 ? 187 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 19.352  28.340 -10.610 1.00 18.14 ? 187 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 18.401  27.457 -9.796  1.00 17.96 ? 187 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 17.412  26.942 -10.328 1.00 17.42 ? 187 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 18.858  29.800 -10.670 1.00 19.62 ? 187 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 17.473  29.926 -11.293 1.00 20.64 ? 187 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 18.895  30.455 -9.288  1.00 19.78 ? 187 VAL   A CG2 1 
ATOM   1212 N N   . SER   A 1 166 ? 18.737  27.251 -8.514  1.00 17.67 ? 188 SER   A N   1 
ATOM   1213 C CA  . SER   A 1 166 ? 17.914  26.459 -7.601  1.00 18.09 ? 188 SER   A CA  1 
ATOM   1214 C C   . SER   A 1 166 ? 17.684  27.241 -6.314  1.00 18.40 ? 188 SER   A C   1 
ATOM   1215 O O   . SER   A 1 166 ? 18.470  28.128 -5.957  1.00 19.65 ? 188 SER   A O   1 
ATOM   1216 C CB  . SER   A 1 166 ? 18.530  25.114 -7.298  1.00 19.01 ? 188 SER   A CB  1 
ATOM   1217 O OG  . SER   A 1 166 ? 19.751  25.276 -6.587  1.00 19.01 ? 188 SER   A OG  1 
ATOM   1218 N N   . SER   A 1 167 ? 16.612  26.880 -5.605  1.00 16.98 ? 189 SER   A N   1 
ATOM   1219 C CA  . SER   A 1 167 ? 16.286  27.510 -4.339  1.00 17.65 ? 189 SER   A CA  1 
ATOM   1220 C C   . SER   A 1 167 ? 15.791  26.449 -3.367  1.00 16.82 ? 189 SER   A C   1 
ATOM   1221 O O   . SER   A 1 167 ? 15.327  25.397 -3.791  1.00 17.10 ? 189 SER   A O   1 
ATOM   1222 C CB  . SER   A 1 167 ? 15.256  28.600 -4.511  1.00 17.88 ? 189 SER   A CB  1 
ATOM   1223 O OG  . SER   A 1 167 ? 14.105  28.086 -5.150  1.00 17.44 ? 189 SER   A OG  1 
ATOM   1224 N N   . SER   A 1 168 ? 15.876  26.743 -2.065  1.00 16.98 ? 190 SER   A N   1 
ATOM   1225 C CA  . SER   A 1 168 ? 15.507  25.759 -1.066  1.00 17.04 ? 190 SER   A CA  1 
ATOM   1226 C C   . SER   A 1 168 ? 14.997  26.414 0.214   1.00 17.72 ? 190 SER   A C   1 
ATOM   1227 O O   . SER   A 1 168 ? 15.329  27.559 0.524   1.00 18.44 ? 190 SER   A O   1 
ATOM   1228 C CB  . SER   A 1 168 ? 16.698  24.857 -0.801  1.00 17.28 ? 190 SER   A CB  1 
ATOM   1229 O OG  . SER   A 1 168 ? 16.527  24.065 0.365   1.00 18.47 ? 190 SER   A OG  1 
ATOM   1230 N N   . TYR   A 1 169 ? 14.238  25.626 0.984   1.00 18.20 ? 191 TYR   A N   1 
ATOM   1231 C CA  . TYR   A 1 169 ? 13.896  25.962 2.356   1.00 20.51 ? 191 TYR   A CA  1 
ATOM   1232 C C   . TYR   A 1 169 ? 15.147  26.230 3.202   1.00 21.10 ? 191 TYR   A C   1 
ATOM   1233 O O   . TYR   A 1 169 ? 15.078  26.932 4.226   1.00 23.01 ? 191 TYR   A O   1 
ATOM   1234 C CB  . TYR   A 1 169 ? 13.042  24.817 2.896   1.00 22.12 ? 191 TYR   A CB  1 
ATOM   1235 C CG  . TYR   A 1 169 ? 12.368  25.114 4.227   1.00 26.01 ? 191 TYR   A CG  1 
ATOM   1236 C CD1 . TYR   A 1 169 ? 13.015  24.864 5.436   1.00 30.80 ? 191 TYR   A CD1 1 
ATOM   1237 C CD2 . TYR   A 1 169 ? 11.091  25.641 4.271   1.00 28.70 ? 191 TYR   A CD2 1 
ATOM   1238 C CE1 . TYR   A 1 169 ? 12.412  25.151 6.645   1.00 31.93 ? 191 TYR   A CE1 1 
ATOM   1239 C CE2 . TYR   A 1 169 ? 10.469  25.923 5.474   1.00 31.31 ? 191 TYR   A CE2 1 
ATOM   1240 C CZ  . TYR   A 1 169 ? 11.134  25.677 6.660   1.00 33.60 ? 191 TYR   A CZ  1 
ATOM   1241 O OH  . TYR   A 1 169 ? 10.536  25.950 7.845   1.00 38.58 ? 191 TYR   A OH  1 
ATOM   1242 N N   . ASP   A 1 170 ? 16.305  25.704 2.769   1.00 21.50 ? 192 ASP   A N   1 
ATOM   1243 C CA  . ASP   A 1 170 ? 17.551  25.909 3.495   1.00 21.75 ? 192 ASP   A CA  1 
ATOM   1244 C C   . ASP   A 1 170 ? 17.941  27.393 3.527   1.00 22.47 ? 192 ASP   A C   1 
ATOM   1245 O O   . ASP   A 1 170 ? 18.829  27.772 4.289   1.00 24.56 ? 192 ASP   A O   1 
ATOM   1246 C CB  . ASP   A 1 170 ? 18.667  24.994 3.001   1.00 21.47 ? 192 ASP   A CB  1 
ATOM   1247 C CG  . ASP   A 1 170 ? 19.235  25.298 1.622   1.00 21.32 ? 192 ASP   A CG  1 
ATOM   1248 O OD1 . ASP   A 1 170 ? 18.817  26.306 1.011   1.00 20.33 ? 192 ASP   A OD1 1 
ATOM   1249 O OD2 . ASP   A 1 170 ? 20.082  24.504 1.158   1.00 20.86 ? 192 ASP   A OD2 1 
ATOM   1250 N N   . GLY   A 1 171 ? 17.302  28.235 2.704   1.00 21.93 ? 193 GLY   A N   1 
ATOM   1251 C CA  . GLY   A 1 171 ? 17.554  29.667 2.732   1.00 23.40 ? 193 GLY   A CA  1 
ATOM   1252 C C   . GLY   A 1 171 ? 18.550  30.105 1.659   1.00 23.75 ? 193 GLY   A C   1 
ATOM   1253 O O   . GLY   A 1 171 ? 18.954  31.271 1.604   1.00 24.72 ? 193 GLY   A O   1 
ATOM   1254 N N   . LEU   A 1 172 ? 18.912  29.172 0.778   1.00 23.51 ? 194 LEU   A N   1 
ATOM   1255 C CA  . LEU   A 1 172 ? 19.930  29.450 -0.218  1.00 23.68 ? 194 LEU   A CA  1 
ATOM   1256 C C   . LEU   A 1 172 ? 19.349  29.481 -1.618  1.00 22.64 ? 194 LEU   A C   1 
ATOM   1257 O O   . LEU   A 1 172 ? 18.423  28.732 -1.932  1.00 21.79 ? 194 LEU   A O   1 
ATOM   1258 C CB  . LEU   A 1 172 ? 21.011  28.382 -0.162  1.00 25.02 ? 194 LEU   A CB  1 
ATOM   1259 C CG  . LEU   A 1 172 ? 21.763  28.260 1.159   1.00 26.03 ? 194 LEU   A CG  1 
ATOM   1260 C CD1 . LEU   A 1 172 ? 22.771  27.164 0.960   1.00 26.46 ? 194 LEU   A CD1 1 
ATOM   1261 C CD2 . LEU   A 1 172 ? 22.407  29.581 1.572   1.00 27.58 ? 194 LEU   A CD2 1 
ATOM   1262 N N   A CYS   A 1 173 ? 19.897  30.387 -2.431  0.50 23.43 ? 195 CYS   A N   1 
ATOM   1263 N N   B CYS   A 1 173 ? 19.951  30.337 -2.447  0.50 21.38 ? 195 CYS   A N   1 
ATOM   1264 C CA  A CYS   A 1 173 ? 19.852  30.277 -3.877  0.50 23.84 ? 195 CYS   A CA  1 
ATOM   1265 C CA  B CYS   A 1 173 ? 19.818  30.282 -3.890  0.50 20.24 ? 195 CYS   A CA  1 
ATOM   1266 C C   A CYS   A 1 173 ? 21.238  29.897 -4.372  0.50 22.57 ? 195 CYS   A C   1 
ATOM   1267 C C   B CYS   A 1 173 ? 21.196  29.996 -4.483  0.50 20.57 ? 195 CYS   A C   1 
ATOM   1268 O O   A CYS   A 1 173 ? 22.237  30.447 -3.907  0.50 22.48 ? 195 CYS   A O   1 
ATOM   1269 O O   B CYS   A 1 173 ? 22.156  30.715 -4.194  0.50 20.58 ? 195 CYS   A O   1 
ATOM   1270 C CB  A CYS   A 1 173 ? 19.455  31.588 -4.540  0.50 26.37 ? 195 CYS   A CB  1 
ATOM   1271 C CB  B CYS   A 1 173 ? 19.221  31.581 -4.421  0.50 19.60 ? 195 CYS   A CB  1 
ATOM   1272 S SG  A CYS   A 1 173 ? 17.742  32.055 -4.206  0.50 31.32 ? 195 CYS   A SG  1 
ATOM   1273 S SG  B CYS   A 1 173 ? 19.374  31.762 -6.215  0.50 18.69 ? 195 CYS   A SG  1 
ATOM   1274 N N   . ARG   A 1 174 ? 21.281  28.938 -5.299  1.00 20.92 ? 196 ARG   A N   1 
ATOM   1275 C CA  . ARG   A 1 174 ? 22.545  28.489 -5.874  1.00 21.26 ? 196 ARG   A CA  1 
ATOM   1276 C C   . ARG   A 1 174 ? 22.446  28.455 -7.390  1.00 20.86 ? 196 ARG   A C   1 
ATOM   1277 O O   . ARG   A 1 174 ? 21.388  28.141 -7.938  1.00 21.50 ? 196 ARG   A O   1 
ATOM   1278 C CB  . ARG   A 1 174 ? 22.921  27.100 -5.343  1.00 22.55 ? 196 ARG   A CB  1 
ATOM   1279 C CG  . ARG   A 1 174 ? 23.433  27.192 -3.915  1.00 22.98 ? 196 ARG   A CG  1 
ATOM   1280 C CD  . ARG   A 1 174 ? 23.918  25.883 -3.330  1.00 24.11 ? 196 ARG   A CD  1 
ATOM   1281 N NE  . ARG   A 1 174 ? 24.706  26.120 -2.114  1.00 25.91 ? 196 ARG   A NE  1 
ATOM   1282 C CZ  . ARG   A 1 174 ? 24.866  25.266 -1.099  1.00 28.77 ? 196 ARG   A CZ  1 
ATOM   1283 N NH1 . ARG   A 1 174 ? 25.667  25.580 -0.093  1.00 30.85 ? 196 ARG   A NH1 1 
ATOM   1284 N NH2 . ARG   A 1 174 ? 24.218  24.112 -1.078  1.00 28.59 ? 196 ARG   A NH2 1 
ATOM   1285 N N   . ILE   A 1 175 ? 23.571  28.766 -8.036  1.00 20.00 ? 197 ILE   A N   1 
ATOM   1286 C CA  . ILE   A 1 175 ? 23.690  28.711 -9.480  1.00 20.94 ? 197 ILE   A CA  1 
ATOM   1287 C C   . ILE   A 1 175 ? 24.706  27.634 -9.843  1.00 20.23 ? 197 ILE   A C   1 
ATOM   1288 O O   . ILE   A 1 175 ? 25.795  27.592 -9.287  1.00 22.54 ? 197 ILE   A O   1 
ATOM   1289 C CB  . ILE   A 1 175 ? 24.051  30.082 -10.067 1.00 23.49 ? 197 ILE   A CB  1 
ATOM   1290 C CG1 . ILE   A 1 175 ? 22.960  31.127 -9.762  1.00 23.57 ? 197 ILE   A CG1 1 
ATOM   1291 C CG2 . ILE   A 1 175 ? 24.315  29.957 -11.571 1.00 24.88 ? 197 ILE   A CG2 1 
ATOM   1292 C CD1 . ILE   A 1 175 ? 23.106  31.836 -8.425  1.00 25.42 ? 197 ILE   A CD1 1 
ATOM   1293 N N   . TRP   A 1 176 ? 24.325  26.792 -10.809 1.00 19.69 ? 198 TRP   A N   1 
ATOM   1294 C CA  . TRP   A 1 176 ? 25.035  25.581 -11.172 1.00 18.92 ? 198 TRP   A CA  1 
ATOM   1295 C C   . TRP   A 1 176 ? 25.436  25.654 -12.635 1.00 19.31 ? 198 TRP   A C   1 
ATOM   1296 O O   . TRP   A 1 176 ? 24.646  26.080 -13.472 1.00 20.96 ? 198 TRP   A O   1 
ATOM   1297 C CB  . TRP   A 1 176 ? 24.146  24.343 -10.973 1.00 18.03 ? 198 TRP   A CB  1 
ATOM   1298 C CG  . TRP   A 1 176 ? 23.569  24.262 -9.588  1.00 18.06 ? 198 TRP   A CG  1 
ATOM   1299 C CD1 . TRP   A 1 176 ? 22.405  24.816 -9.147  1.00 19.11 ? 198 TRP   A CD1 1 
ATOM   1300 C CD2 . TRP   A 1 176 ? 24.174  23.632 -8.449  1.00 19.39 ? 198 TRP   A CD2 1 
ATOM   1301 N NE1 . TRP   A 1 176 ? 22.246  24.585 -7.809  1.00 19.45 ? 198 TRP   A NE1 1 
ATOM   1302 C CE2 . TRP   A 1 176 ? 23.315  23.860 -7.355  1.00 19.70 ? 198 TRP   A CE2 1 
ATOM   1303 C CE3 . TRP   A 1 176 ? 25.363  22.918 -8.255  1.00 20.38 ? 198 TRP   A CE3 1 
ATOM   1304 C CZ2 . TRP   A 1 176 ? 23.605  23.389 -6.083  1.00 19.78 ? 198 TRP   A CZ2 1 
ATOM   1305 C CZ3 . TRP   A 1 176 ? 25.625  22.425 -7.006  1.00 20.38 ? 198 TRP   A CZ3 1 
ATOM   1306 C CH2 . TRP   A 1 176 ? 24.768  22.672 -5.937  1.00 21.19 ? 198 TRP   A CH2 1 
ATOM   1307 N N   . ASP   A 1 177 ? 26.650  25.199 -12.918 1.00 20.87 ? 199 ASP   A N   1 
ATOM   1308 C CA  . ASP   A 1 177 ? 27.099  24.988 -14.276 1.00 20.52 ? 199 ASP   A CA  1 
ATOM   1309 C C   . ASP   A 1 177 ? 26.451  23.709 -14.787 1.00 20.07 ? 199 ASP   A C   1 
ATOM   1310 O O   . ASP   A 1 177 ? 26.679  22.640 -14.226 1.00 20.34 ? 199 ASP   A O   1 
ATOM   1311 C CB  . ASP   A 1 177 ? 28.610  24.863 -14.331 1.00 22.24 ? 199 ASP   A CB  1 
ATOM   1312 C CG  . ASP   A 1 177 ? 29.161  24.624 -15.723 1.00 22.77 ? 199 ASP   A CG  1 
ATOM   1313 O OD1 . ASP   A 1 177 ? 29.047  25.557 -16.544 1.00 24.63 ? 199 ASP   A OD1 1 
ATOM   1314 O OD2 . ASP   A 1 177 ? 29.649  23.507 -15.970 1.00 23.93 ? 199 ASP   A OD2 1 
ATOM   1315 N N   . THR   A 1 178 ? 25.614  23.831 -15.824 1.00 19.73 ? 200 THR   A N   1 
ATOM   1316 C CA  . THR   A 1 178 ? 24.875  22.677 -16.329 1.00 19.75 ? 200 THR   A CA  1 
ATOM   1317 C C   . THR   A 1 178 ? 25.816  21.542 -16.733 1.00 20.68 ? 200 THR   A C   1 
ATOM   1318 O O   . THR   A 1 178 ? 25.586  20.377 -16.401 1.00 21.85 ? 200 THR   A O   1 
ATOM   1319 C CB  . THR   A 1 178 ? 23.987  23.075 -17.501 1.00 18.91 ? 200 THR   A CB  1 
ATOM   1320 O OG1 . THR   A 1 178 ? 23.072  24.042 -16.997 1.00 19.74 ? 200 THR   A OG1 1 
ATOM   1321 C CG2 . THR   A 1 178 ? 23.219  21.886 -18.046 1.00 19.39 ? 200 THR   A CG2 1 
ATOM   1322 N N   . ALA   A 1 179 ? 26.843  21.874 -17.515 1.00 22.33 ? 201 ALA   A N   1 
ATOM   1323 C CA  . ALA   A 1 179 ? 27.664  20.862 -18.155 1.00 24.11 ? 201 ALA   A CA  1 
ATOM   1324 C C   . ALA   A 1 179 ? 28.357  19.975 -17.117 1.00 24.64 ? 201 ALA   A C   1 
ATOM   1325 O O   . ALA   A 1 179 ? 28.481  18.768 -17.330 1.00 26.22 ? 201 ALA   A O   1 
ATOM   1326 C CB  . ALA   A 1 179 ? 28.662  21.548 -19.069 1.00 25.73 ? 201 ALA   A CB  1 
ATOM   1327 N N   . SER   A 1 180 ? 28.794  20.578 -15.999 1.00 24.14 ? 202 SER   A N   1 
ATOM   1328 C CA  . SER   A 1 180 ? 29.640  19.912 -15.015 1.00 24.86 ? 202 SER   A CA  1 
ATOM   1329 C C   . SER   A 1 180 ? 28.887  19.584 -13.731 1.00 23.77 ? 202 SER   A C   1 
ATOM   1330 O O   . SER   A 1 180 ? 29.339  18.744 -12.948 1.00 21.10 ? 202 SER   A O   1 
ATOM   1331 C CB  . SER   A 1 180 ? 30.838  20.752 -14.685 1.00 24.82 ? 202 SER   A CB  1 
ATOM   1332 O OG  . SER   A 1 180 ? 30.448  21.891 -13.932 1.00 23.24 ? 202 SER   A OG  1 
ATOM   1333 N N   . GLY   A 1 181 ? 27.775  20.286 -13.488 1.00 23.58 ? 203 GLY   A N   1 
ATOM   1334 C CA  . GLY   A 1 181 ? 27.039  20.119 -12.247 1.00 24.42 ? 203 GLY   A CA  1 
ATOM   1335 C C   . GLY   A 1 181 ? 27.707  20.823 -11.065 1.00 24.33 ? 203 GLY   A C   1 
ATOM   1336 O O   . GLY   A 1 181 ? 27.268  20.686 -9.927  1.00 24.32 ? 203 GLY   A O   1 
ATOM   1337 N N   . GLN   A 1 182 ? 28.761  21.603 -11.325 1.00 25.39 ? 204 GLN   A N   1 
ATOM   1338 C CA  . GLN   A 1 182 ? 29.456  22.296 -10.253 1.00 26.64 ? 204 GLN   A CA  1 
ATOM   1339 C C   . GLN   A 1 182 ? 28.726  23.585 -9.892  1.00 24.97 ? 204 GLN   A C   1 
ATOM   1340 O O   . GLN   A 1 182 ? 28.164  24.248 -10.758 1.00 26.44 ? 204 GLN   A O   1 
ATOM   1341 C CB  . GLN   A 1 182 ? 30.892  22.580 -10.681 1.00 30.37 ? 204 GLN   A CB  1 
ATOM   1342 C CG  . GLN   A 1 182 ? 31.770  21.334 -10.705 1.00 35.30 ? 204 GLN   A CG  1 
ATOM   1343 C CD  . GLN   A 1 182 ? 32.010  20.789 -9.317  1.00 38.86 ? 204 GLN   A CD  1 
ATOM   1344 O OE1 . GLN   A 1 182 ? 32.366  21.526 -8.387  1.00 48.19 ? 204 GLN   A OE1 1 
ATOM   1345 N NE2 . GLN   A 1 182 ? 31.784  19.498 -9.157  1.00 36.95 ? 204 GLN   A NE2 1 
ATOM   1346 N N   . CYS   A 1 183 ? 28.758  23.930 -8.602  1.00 25.46 ? 205 CYS   A N   1 
ATOM   1347 C CA  . CYS   A 1 183 ? 28.141  25.146 -8.106  1.00 25.41 ? 205 CYS   A CA  1 
ATOM   1348 C C   . CYS   A 1 183 ? 29.058  26.320 -8.425  1.00 27.09 ? 205 CYS   A C   1 
ATOM   1349 O O   . CYS   A 1 183 ? 30.232  26.301 -8.046  1.00 28.85 ? 205 CYS   A O   1 
ATOM   1350 C CB  . CYS   A 1 183 ? 27.937  25.080 -6.597  1.00 27.16 ? 205 CYS   A CB  1 
ATOM   1351 S SG  . CYS   A 1 183 ? 27.010  26.482 -5.918  1.00 29.03 ? 205 CYS   A SG  1 
ATOM   1352 N N   . LEU   A 1 184 ? 28.507  27.338 -9.101  1.00 26.35 ? 206 LEU   A N   1 
ATOM   1353 C CA  . LEU   A 1 184 ? 29.266  28.537 -9.405  1.00 26.80 ? 206 LEU   A CA  1 
ATOM   1354 C C   . LEU   A 1 184 ? 29.083  29.622 -8.349  1.00 26.58 ? 206 LEU   A C   1 
ATOM   1355 O O   . LEU   A 1 184 ? 29.967  30.458 -8.185  1.00 30.10 ? 206 LEU   A O   1 
ATOM   1356 C CB  . LEU   A 1 184 ? 28.892  29.068 -10.782 1.00 27.33 ? 206 LEU   A CB  1 
ATOM   1357 C CG  . LEU   A 1 184 ? 29.215  28.135 -11.950 1.00 28.73 ? 206 LEU   A CG  1 
ATOM   1358 C CD1 . LEU   A 1 184 ? 28.727  28.725 -13.259 1.00 28.35 ? 206 LEU   A CD1 1 
ATOM   1359 C CD2 . LEU   A 1 184 ? 30.697  27.865 -11.998 1.00 30.85 ? 206 LEU   A CD2 1 
ATOM   1360 N N   . LYS   A 1 185 ? 27.936  29.657 -7.677  1.00 27.54 ? 207 LYS   A N   1 
ATOM   1361 C CA  . LYS   A 1 185 ? 27.622  30.790 -6.822  1.00 27.86 ? 207 LYS   A CA  1 
ATOM   1362 C C   . LYS   A 1 185 ? 26.513  30.386 -5.863  1.00 27.33 ? 207 LYS   A C   1 
ATOM   1363 O O   . LYS   A 1 185 ? 25.547  29.739 -6.275  1.00 26.52 ? 207 LYS   A O   1 
ATOM   1364 C CB  . LYS   A 1 185 ? 27.168  32.006 -7.648  1.00 29.32 ? 207 LYS   A CB  1 
ATOM   1365 C CG  . LYS   A 1 185 ? 27.252  33.367 -6.961  1.00 32.02 ? 207 LYS   A CG  1 
ATOM   1366 C CD  . LYS   A 1 185 ? 27.555  34.543 -7.885  1.00 34.57 ? 207 LYS   A CD  1 
ATOM   1367 N N   . THR   A 1 186 ? 26.694  30.770 -4.597  1.00 28.24 ? 208 THR   A N   1 
ATOM   1368 C CA  . THR   A 1 186 ? 25.623  30.810 -3.621  1.00 29.33 ? 208 THR   A CA  1 
ATOM   1369 C C   . THR   A 1 186 ? 25.310  32.269 -3.286  1.00 31.64 ? 208 THR   A C   1 
ATOM   1370 O O   . THR   A 1 186 ? 26.214  33.003 -2.894  1.00 31.79 ? 208 THR   A O   1 
ATOM   1371 C CB  . THR   A 1 186 ? 26.061  30.041 -2.370  1.00 30.00 ? 208 THR   A CB  1 
ATOM   1372 O OG1 . THR   A 1 186 ? 26.316  28.681 -2.724  1.00 27.29 ? 208 THR   A OG1 1 
ATOM   1373 C CG2 . THR   A 1 186 ? 24.979  30.037 -1.306  1.00 30.96 ? 208 THR   A CG2 1 
ATOM   1374 N N   . LEU   A 1 187 ? 24.044  32.684 -3.442  1.00 34.88 ? 209 LEU   A N   1 
ATOM   1375 C CA  . LEU   A 1 187 ? 23.526  33.874 -2.776  1.00 40.80 ? 209 LEU   A CA  1 
ATOM   1376 C C   . LEU   A 1 187 ? 22.955  33.444 -1.415  1.00 44.68 ? 209 LEU   A C   1 
ATOM   1377 O O   . LEU   A 1 187 ? 22.007  32.639 -1.345  1.00 45.46 ? 209 LEU   A O   1 
ATOM   1378 C CB  . LEU   A 1 187 ? 22.444  34.610 -3.575  1.00 40.60 ? 209 LEU   A CB  1 
ATOM   1379 C CG  . LEU   A 1 187 ? 22.436  34.490 -5.107  1.00 38.69 ? 209 LEU   A CG  1 
ATOM   1380 C CD1 . LEU   A 1 187 ? 21.068  34.935 -5.624  1.00 36.69 ? 209 LEU   A CD1 1 
ATOM   1381 C CD2 . LEU   A 1 187 ? 23.531  35.301 -5.782  1.00 40.41 ? 209 LEU   A CD2 1 
ATOM   1382 N N   . ILE   A 1 188 ? 23.507  34.012 -0.338  1.00 48.91 ? 210 ILE   A N   1 
ATOM   1383 C CA  . ILE   A 1 188 ? 23.164  33.633 1.032   1.00 54.25 ? 210 ILE   A CA  1 
ATOM   1384 C C   . ILE   A 1 188 ? 22.394  34.782 1.710   1.00 60.77 ? 210 ILE   A C   1 
ATOM   1385 O O   . ILE   A 1 188 ? 22.933  35.921 1.709   1.00 68.87 ? 210 ILE   A O   1 
ATOM   1386 C CB  . ILE   A 1 188 ? 24.419  33.256 1.843   1.00 52.64 ? 210 ILE   A CB  1 
ATOM   1387 N N   . ASP   A 1 191 ? 20.977  37.188 6.235   1.00 62.07 ? 213 ASP   A N   1 
ATOM   1388 C CA  . ASP   A 1 191 ? 19.798  36.402 6.706   1.00 60.96 ? 213 ASP   A CA  1 
ATOM   1389 C C   . ASP   A 1 191 ? 19.509  35.289 5.695   1.00 58.34 ? 213 ASP   A C   1 
ATOM   1390 O O   . ASP   A 1 191 ? 19.989  35.334 4.556   1.00 60.51 ? 213 ASP   A O   1 
ATOM   1391 C CB  . ASP   A 1 191 ? 18.602  37.313 6.952   1.00 63.60 ? 213 ASP   A CB  1 
ATOM   1392 C CG  . ASP   A 1 191 ? 17.559  36.821 7.950   1.00 65.32 ? 213 ASP   A CG  1 
ATOM   1393 O OD1 . ASP   A 1 191 ? 17.819  35.811 8.644   1.00 66.09 ? 213 ASP   A OD1 1 
ATOM   1394 O OD2 . ASP   A 1 191 ? 16.488  37.456 8.028   1.00 66.89 ? 213 ASP   A OD2 1 
ATOM   1395 N N   . ASN   A 1 192 ? 18.731  34.284 6.125   1.00 49.59 ? 214 ASN   A N   1 
ATOM   1396 C CA  . ASN   A 1 192 ? 18.433  33.142 5.275   1.00 44.36 ? 214 ASN   A CA  1 
ATOM   1397 C C   . ASN   A 1 192 ? 17.027  32.613 5.562   1.00 37.04 ? 214 ASN   A C   1 
ATOM   1398 O O   . ASN   A 1 192 ? 16.857  31.452 5.919   1.00 35.66 ? 214 ASN   A O   1 
ATOM   1399 C CB  . ASN   A 1 192 ? 19.502  32.059 5.402   1.00 48.08 ? 214 ASN   A CB  1 
ATOM   1400 C CG  . ASN   A 1 192 ? 19.578  31.488 6.795   1.00 51.36 ? 214 ASN   A CG  1 
ATOM   1401 O OD1 . ASN   A 1 192 ? 19.086  32.096 7.754   1.00 55.09 ? 214 ASN   A OD1 1 
ATOM   1402 N ND2 . ASN   A 1 192 ? 20.197  30.326 6.928   1.00 53.90 ? 214 ASN   A ND2 1 
ATOM   1403 N N   . PRO   A 1 193 ? 15.961  33.415 5.346   1.00 31.99 ? 215 PRO   A N   1 
ATOM   1404 C CA  . PRO   A 1 193 ? 14.599  32.881 5.384   1.00 30.18 ? 215 PRO   A CA  1 
ATOM   1405 C C   . PRO   A 1 193 ? 14.429  31.844 4.276   1.00 26.83 ? 215 PRO   A C   1 
ATOM   1406 O O   . PRO   A 1 193 ? 15.123  31.905 3.265   1.00 25.50 ? 215 PRO   A O   1 
ATOM   1407 C CB  . PRO   A 1 193 ? 13.737  34.138 5.150   1.00 31.56 ? 215 PRO   A CB  1 
ATOM   1408 C CG  . PRO   A 1 193 ? 14.638  35.047 4.336   1.00 30.59 ? 215 PRO   A CG  1 
ATOM   1409 C CD  . PRO   A 1 193 ? 16.008  34.842 4.973   1.00 31.82 ? 215 PRO   A CD  1 
ATOM   1410 N N   . PRO   A 1 194 ? 13.517  30.854 4.399   1.00 25.84 ? 216 PRO   A N   1 
ATOM   1411 C CA  . PRO   A 1 194 ? 13.284  29.911 3.301   1.00 23.30 ? 216 PRO   A CA  1 
ATOM   1412 C C   . PRO   A 1 194 ? 13.112  30.631 1.971   1.00 23.12 ? 216 PRO   A C   1 
ATOM   1413 O O   . PRO   A 1 194 ? 12.373  31.612 1.885   1.00 21.72 ? 216 PRO   A O   1 
ATOM   1414 C CB  . PRO   A 1 194 ? 12.006  29.181 3.723   1.00 24.35 ? 216 PRO   A CB  1 
ATOM   1415 C CG  . PRO   A 1 194 ? 12.061  29.224 5.235   1.00 24.75 ? 216 PRO   A CG  1 
ATOM   1416 C CD  . PRO   A 1 194 ? 12.658  30.587 5.561   1.00 26.80 ? 216 PRO   A CD  1 
ATOM   1417 N N   . VAL   A 1 195 ? 13.831  30.152 0.949   1.00 21.32 ? 217 VAL   A N   1 
ATOM   1418 C CA  . VAL   A 1 195 ? 13.638  30.637 -0.405  1.00 21.16 ? 217 VAL   A CA  1 
ATOM   1419 C C   . VAL   A 1 195 ? 12.610  29.738 -1.088  1.00 20.41 ? 217 VAL   A C   1 
ATOM   1420 O O   . VAL   A 1 195 ? 12.865  28.551 -1.305  1.00 20.94 ? 217 VAL   A O   1 
ATOM   1421 C CB  . VAL   A 1 195 ? 14.951  30.676 -1.210  1.00 20.64 ? 217 VAL   A CB  1 
ATOM   1422 C CG1 . VAL   A 1 195 ? 14.744  31.343 -2.554  1.00 20.11 ? 217 VAL   A CG1 1 
ATOM   1423 C CG2 . VAL   A 1 195 ? 16.090  31.349 -0.448  1.00 21.21 ? 217 VAL   A CG2 1 
ATOM   1424 N N   . SER   A 1 196 ? 11.480  30.339 -1.476  1.00 20.72 ? 218 SER   A N   1 
ATOM   1425 C CA  . SER   A 1 196 ? 10.306  29.605 -1.941  1.00 19.76 ? 218 SER   A CA  1 
ATOM   1426 C C   . SER   A 1 196 ? 10.173  29.592 -3.465  1.00 18.90 ? 218 SER   A C   1 
ATOM   1427 O O   . SER   A 1 196 ? 9.369   28.834 -4.006  1.00 18.87 ? 218 SER   A O   1 
ATOM   1428 C CB  . SER   A 1 196 ? 9.055   30.174 -1.301  1.00 19.44 ? 218 SER   A CB  1 
ATOM   1429 O OG  . SER   A 1 196 ? 8.997   31.578 -1.492  1.00 20.62 ? 218 SER   A OG  1 
ATOM   1430 N N   . PHE   A 1 197 ? 10.937  30.424 -4.171  1.00 18.78 ? 219 PHE   A N   1 
ATOM   1431 C CA  . PHE   A 1 197 ? 10.854  30.459 -5.624  1.00 18.61 ? 219 PHE   A CA  1 
ATOM   1432 C C   . PHE   A 1 197 ? 12.077  31.184 -6.173  1.00 17.53 ? 219 PHE   A C   1 
ATOM   1433 O O   . PHE   A 1 197 ? 12.539  32.116 -5.546  1.00 19.22 ? 219 PHE   A O   1 
ATOM   1434 C CB  . PHE   A 1 197 ? 9.581   31.169 -6.095  1.00 19.61 ? 219 PHE   A CB  1 
ATOM   1435 C CG  . PHE   A 1 197 ? 9.444   31.107 -7.608  1.00 21.74 ? 219 PHE   A CG  1 
ATOM   1436 C CD1 . PHE   A 1 197 ? 9.099   29.913 -8.233  1.00 22.33 ? 219 PHE   A CD1 1 
ATOM   1437 C CD2 . PHE   A 1 197 ? 9.725   32.214 -8.403  1.00 23.09 ? 219 PHE   A CD2 1 
ATOM   1438 C CE1 . PHE   A 1 197 ? 9.034   29.830 -9.615  1.00 22.48 ? 219 PHE   A CE1 1 
ATOM   1439 C CE2 . PHE   A 1 197 ? 9.641   32.128 -9.782  1.00 22.89 ? 219 PHE   A CE2 1 
ATOM   1440 C CZ  . PHE   A 1 197 ? 9.293   30.942 -10.383 1.00 22.78 ? 219 PHE   A CZ  1 
ATOM   1441 N N   . VAL   A 1 198 ? 12.579  30.758 -7.335  1.00 17.76 ? 220 VAL   A N   1 
ATOM   1442 C CA  . VAL   A 1 198 ? 13.592  31.506 -8.073  1.00 18.83 ? 220 VAL   A CA  1 
ATOM   1443 C C   . VAL   A 1 198 ? 13.365  31.271 -9.556  1.00 18.90 ? 220 VAL   A C   1 
ATOM   1444 O O   . VAL   A 1 198 ? 12.865  30.225 -9.955  1.00 18.22 ? 220 VAL   A O   1 
ATOM   1445 C CB  . VAL   A 1 198 ? 15.072  31.165 -7.790  1.00 21.04 ? 220 VAL   A CB  1 
ATOM   1446 C CG1 . VAL   A 1 198 ? 15.541  31.701 -6.456  1.00 24.32 ? 220 VAL   A CG1 1 
ATOM   1447 C CG2 . VAL   A 1 198 ? 15.365  29.674 -7.884  1.00 20.09 ? 220 VAL   A CG2 1 
ATOM   1448 N N   A LYS   A 1 199 ? 13.712  32.269 -10.369 0.50 19.10 ? 221 LYS   A N   1 
ATOM   1449 N N   B LYS   A 1 199 ? 13.810  32.249 -10.347 0.50 18.64 ? 221 LYS   A N   1 
ATOM   1450 C CA  A LYS   A 1 199 ? 13.843  32.057 -11.798 0.50 19.55 ? 221 LYS   A CA  1 
ATOM   1451 C CA  B LYS   A 1 199 ? 13.744  32.186 -11.793 0.50 18.65 ? 221 LYS   A CA  1 
ATOM   1452 C C   A LYS   A 1 199 ? 14.696  33.175 -12.383 0.50 19.70 ? 221 LYS   A C   1 
ATOM   1453 C C   B LYS   A 1 199 ? 14.730  33.201 -12.364 0.50 19.24 ? 221 LYS   A C   1 
ATOM   1454 O O   A LYS   A 1 199 ? 14.693  34.299 -11.883 0.50 19.43 ? 221 LYS   A O   1 
ATOM   1455 O O   B LYS   A 1 199 ? 14.861  34.295 -11.822 0.50 19.30 ? 221 LYS   A O   1 
ATOM   1456 C CB  A LYS   A 1 199 ? 12.501  31.998 -12.535 0.50 19.69 ? 221 LYS   A CB  1 
ATOM   1457 C CB  B LYS   A 1 199 ? 12.325  32.542 -12.239 0.50 18.16 ? 221 LYS   A CB  1 
ATOM   1458 C CG  A LYS   A 1 199 ? 11.827  33.329 -12.791 0.50 20.68 ? 221 LYS   A CG  1 
ATOM   1459 C CG  B LYS   A 1 199 ? 12.004  32.187 -13.671 0.50 18.45 ? 221 LYS   A CG  1 
ATOM   1460 C CD  A LYS   A 1 199 ? 10.424  33.217 -13.377 0.50 20.73 ? 221 LYS   A CD  1 
ATOM   1461 C CD  B LYS   A 1 199 ? 10.590  32.532 -14.105 0.50 18.96 ? 221 LYS   A CD  1 
ATOM   1462 C CE  A LYS   A 1 199 ? 10.355  32.527 -14.704 0.50 21.99 ? 221 LYS   A CE  1 
ATOM   1463 C CE  B LYS   A 1 199 ? 10.235  31.859 -15.409 0.50 19.34 ? 221 LYS   A CE  1 
ATOM   1464 N NZ  A LYS   A 1 199 ? 8.960   32.403 -15.143 0.50 21.91 ? 221 LYS   A NZ  1 
ATOM   1465 N NZ  B LYS   A 1 199 ? 8.835   32.093 -15.765 0.50 20.13 ? 221 LYS   A NZ  1 
ATOM   1466 N N   . PHE   A 1 200 ? 15.411  32.837 -13.458 1.00 19.68 ? 222 PHE   A N   1 
ATOM   1467 C CA  . PHE   A 1 200 ? 16.171  33.802 -14.224 1.00 19.98 ? 222 PHE   A CA  1 
ATOM   1468 C C   . PHE   A 1 200 ? 15.253  34.775 -14.958 1.00 21.05 ? 222 PHE   A C   1 
ATOM   1469 O O   . PHE   A 1 200 ? 14.173  34.404 -15.396 1.00 21.27 ? 222 PHE   A O   1 
ATOM   1470 C CB  . PHE   A 1 200 ? 17.030  33.127 -15.292 1.00 20.55 ? 222 PHE   A CB  1 
ATOM   1471 C CG  . PHE   A 1 200 ? 18.316  32.515 -14.758 1.00 20.62 ? 222 PHE   A CG  1 
ATOM   1472 C CD1 . PHE   A 1 200 ? 19.403  33.324 -14.437 1.00 21.99 ? 222 PHE   A CD1 1 
ATOM   1473 C CD2 . PHE   A 1 200 ? 18.440  31.139 -14.607 1.00 20.43 ? 222 PHE   A CD2 1 
ATOM   1474 C CE1 . PHE   A 1 200 ? 20.583  32.773 -13.956 1.00 20.96 ? 222 PHE   A CE1 1 
ATOM   1475 C CE2 . PHE   A 1 200 ? 19.622  30.591 -14.141 1.00 21.59 ? 222 PHE   A CE2 1 
ATOM   1476 C CZ  . PHE   A 1 200 ? 20.697  31.411 -13.827 1.00 21.12 ? 222 PHE   A CZ  1 
ATOM   1477 N N   . SER   A 1 201 ? 15.736  36.010 -15.123 1.00 22.33 ? 223 SER   A N   1 
ATOM   1478 C CA  . SER   A 1 201 ? 15.157  36.969 -16.055 1.00 21.90 ? 223 SER   A CA  1 
ATOM   1479 C C   . SER   A 1 201 ? 15.317  36.434 -17.474 1.00 22.46 ? 223 SER   A C   1 
ATOM   1480 O O   . SER   A 1 201 ? 16.163  35.573 -17.722 1.00 21.59 ? 223 SER   A O   1 
ATOM   1481 C CB  . SER   A 1 201 ? 15.808  38.319 -15.909 1.00 22.19 ? 223 SER   A CB  1 
ATOM   1482 O OG  . SER   A 1 201 ? 17.151  38.276 -16.375 1.00 21.62 ? 223 SER   A OG  1 
ATOM   1483 N N   . PRO   A 1 202 ? 14.478  36.871 -18.435 1.00 23.20 ? 224 PRO   A N   1 
ATOM   1484 C CA  . PRO   A 1 202 ? 14.592  36.408 -19.818 1.00 24.99 ? 224 PRO   A CA  1 
ATOM   1485 C C   . PRO   A 1 202 ? 15.979  36.578 -20.424 1.00 25.33 ? 224 PRO   A C   1 
ATOM   1486 O O   . PRO   A 1 202 ? 16.401  35.728 -21.197 1.00 26.91 ? 224 PRO   A O   1 
ATOM   1487 C CB  . PRO   A 1 202 ? 13.521  37.219 -20.577 1.00 25.68 ? 224 PRO   A CB  1 
ATOM   1488 C CG  . PRO   A 1 202 ? 12.485  37.503 -19.513 1.00 25.71 ? 224 PRO   A CG  1 
ATOM   1489 C CD  . PRO   A 1 202 ? 13.285  37.705 -18.223 1.00 24.56 ? 224 PRO   A CD  1 
ATOM   1490 N N   . ASN   A 1 203 ? 16.702  37.631 -20.029 1.00 26.87 ? 225 ASN   A N   1 
ATOM   1491 C CA  . ASN   A 1 203 ? 18.011  37.885 -20.611 1.00 27.81 ? 225 ASN   A CA  1 
ATOM   1492 C C   . ASN   A 1 203 ? 19.109  37.148 -19.840 1.00 27.47 ? 225 ASN   A C   1 
ATOM   1493 O O   . ASN   A 1 203 ? 20.275  37.220 -20.223 1.00 29.42 ? 225 ASN   A O   1 
ATOM   1494 C CB  . ASN   A 1 203 ? 18.303  39.375 -20.764 1.00 31.12 ? 225 ASN   A CB  1 
ATOM   1495 C CG  . ASN   A 1 203 ? 18.480  40.100 -19.450 1.00 32.32 ? 225 ASN   A CG  1 
ATOM   1496 O OD1 . ASN   A 1 203 ? 18.399  39.495 -18.373 1.00 30.14 ? 225 ASN   A OD1 1 
ATOM   1497 N ND2 . ASN   A 1 203 ? 18.692  41.410 -19.523 1.00 35.27 ? 225 ASN   A ND2 1 
ATOM   1498 N N   . GLY   A 1 204 ? 18.745  36.477 -18.741 1.00 25.62 ? 226 GLY   A N   1 
ATOM   1499 C CA  . GLY   A 1 204 ? 19.671  35.634 -18.001 1.00 25.80 ? 226 GLY   A CA  1 
ATOM   1500 C C   . GLY   A 1 204 ? 20.544  36.408 -17.012 1.00 26.18 ? 226 GLY   A C   1 
ATOM   1501 O O   . GLY   A 1 204 ? 21.348  35.790 -16.318 1.00 25.79 ? 226 GLY   A O   1 
ATOM   1502 N N   . LYS   A 1 205 ? 20.377  37.739 -16.923 1.00 26.31 ? 227 LYS   A N   1 
ATOM   1503 C CA  . LYS   A 1 205 ? 21.280  38.579 -16.142 1.00 27.24 ? 227 LYS   A CA  1 
ATOM   1504 C C   . LYS   A 1 205 ? 20.853  38.644 -14.674 1.00 27.08 ? 227 LYS   A C   1 
ATOM   1505 O O   . LYS   A 1 205 ? 21.682  38.862 -13.782 1.00 28.67 ? 227 LYS   A O   1 
ATOM   1506 C CB  . LYS   A 1 205 ? 21.343  40.003 -16.717 1.00 28.47 ? 227 LYS   A CB  1 
ATOM   1507 C CG  . LYS   A 1 205 ? 21.887  40.135 -18.135 1.00 31.44 ? 227 LYS   A CG  1 
ATOM   1508 N N   . TYR   A 1 206 ? 19.550  38.478 -14.422 1.00 24.60 ? 228 TYR   A N   1 
ATOM   1509 C CA  . TYR   A 1 206 ? 18.998  38.675 -13.093 1.00 25.18 ? 228 TYR   A CA  1 
ATOM   1510 C C   . TYR   A 1 206 ? 18.315  37.396 -12.621 1.00 23.77 ? 228 TYR   A C   1 
ATOM   1511 O O   . TYR   A 1 206 ? 17.954  36.529 -13.416 1.00 22.98 ? 228 TYR   A O   1 
ATOM   1512 C CB  . TYR   A 1 206 ? 18.017  39.854 -13.083 1.00 26.34 ? 228 TYR   A CB  1 
ATOM   1513 C CG  . TYR   A 1 206 ? 18.550  41.105 -13.772 1.00 29.30 ? 228 TYR   A CG  1 
ATOM   1514 C CD1 . TYR   A 1 206 ? 19.617  41.816 -13.245 1.00 32.23 ? 228 TYR   A CD1 1 
ATOM   1515 C CD2 . TYR   A 1 206 ? 17.985  41.576 -14.954 1.00 32.93 ? 228 TYR   A CD2 1 
ATOM   1516 C CE1 . TYR   A 1 206 ? 20.116  42.948 -13.872 1.00 34.34 ? 228 TYR   A CE1 1 
ATOM   1517 C CE2 . TYR   A 1 206 ? 18.468  42.711 -15.588 1.00 34.08 ? 228 TYR   A CE2 1 
ATOM   1518 C CZ  . TYR   A 1 206 ? 19.546  43.394 -15.051 1.00 34.06 ? 228 TYR   A CZ  1 
ATOM   1519 O OH  . TYR   A 1 206 ? 20.039  44.514 -15.654 1.00 37.49 ? 228 TYR   A OH  1 
ATOM   1520 N N   . ILE   A 1 207 ? 18.157  37.304 -11.305 1.00 23.10 ? 229 ILE   A N   1 
ATOM   1521 C CA  . ILE   A 1 207 ? 17.396  36.239 -10.685 1.00 22.01 ? 229 ILE   A CA  1 
ATOM   1522 C C   . ILE   A 1 207 ? 16.353  36.885 -9.784  1.00 21.43 ? 229 ILE   A C   1 
ATOM   1523 O O   . ILE   A 1 207 ? 16.670  37.745 -8.970  1.00 22.20 ? 229 ILE   A O   1 
ATOM   1524 C CB  . ILE   A 1 207 ? 18.307  35.268 -9.920  1.00 22.22 ? 229 ILE   A CB  1 
ATOM   1525 C CG1 . ILE   A 1 207 ? 19.291  34.562 -10.861 1.00 23.17 ? 229 ILE   A CG1 1 
ATOM   1526 C CG2 . ILE   A 1 207 ? 17.479  34.265 -9.124  1.00 23.13 ? 229 ILE   A CG2 1 
ATOM   1527 C CD1 . ILE   A 1 207 ? 20.581  34.126 -10.188 1.00 24.20 ? 229 ILE   A CD1 1 
ATOM   1528 N N   . LEU   A 1 208 ? 15.106  36.456 -9.968  1.00 20.32 ? 230 LEU   A N   1 
ATOM   1529 C CA  . LEU   A 1 208 ? 13.999  36.823 -9.106  1.00 20.56 ? 230 LEU   A CA  1 
ATOM   1530 C C   . LEU   A 1 208 ? 13.845  35.730 -8.051  1.00 20.83 ? 230 LEU   A C   1 
ATOM   1531 O O   . LEU   A 1 208 ? 13.667  34.571 -8.401  1.00 21.55 ? 230 LEU   A O   1 
ATOM   1532 C CB  . LEU   A 1 208 ? 12.727  36.961 -9.938  1.00 21.04 ? 230 LEU   A CB  1 
ATOM   1533 C CG  . LEU   A 1 208 ? 11.455  37.414 -9.203  1.00 21.42 ? 230 LEU   A CG  1 
ATOM   1534 C CD1 . LEU   A 1 208 ? 11.562  38.816 -8.663  1.00 21.78 ? 230 LEU   A CD1 1 
ATOM   1535 C CD2 . LEU   A 1 208 ? 10.248  37.343 -10.118 1.00 22.43 ? 230 LEU   A CD2 1 
ATOM   1536 N N   . ALA   A 1 209 ? 13.889  36.117 -6.775  1.00 20.89 ? 231 ALA   A N   1 
ATOM   1537 C CA  . ALA   A 1 209 ? 13.805  35.187 -5.661  1.00 20.46 ? 231 ALA   A CA  1 
ATOM   1538 C C   . ALA   A 1 209 ? 12.715  35.603 -4.674  1.00 20.52 ? 231 ALA   A C   1 
ATOM   1539 O O   . ALA   A 1 209 ? 12.690  36.750 -4.219  1.00 22.82 ? 231 ALA   A O   1 
ATOM   1540 C CB  . ALA   A 1 209 ? 15.141  35.126 -4.950  1.00 20.32 ? 231 ALA   A CB  1 
ATOM   1541 N N   . ALA   A 1 210 ? 11.855  34.642 -4.309  1.00 19.90 ? 232 ALA   A N   1 
ATOM   1542 C CA  . ALA   A 1 210 ? 10.877  34.821 -3.243  1.00 20.48 ? 232 ALA   A CA  1 
ATOM   1543 C C   . ALA   A 1 210 ? 11.400  34.210 -1.946  1.00 20.85 ? 232 ALA   A C   1 
ATOM   1544 O O   . ALA   A 1 210 ? 11.943  33.106 -1.959  1.00 22.52 ? 232 ALA   A O   1 
ATOM   1545 C CB  . ALA   A 1 210 ? 9.571   34.156 -3.618  1.00 20.32 ? 232 ALA   A CB  1 
ATOM   1546 N N   . THR   A 1 211 ? 11.155  34.894 -0.825  1.00 22.32 ? 233 THR   A N   1 
ATOM   1547 C CA  . THR   A 1 211 ? 11.419  34.339 0.494   1.00 22.39 ? 233 THR   A CA  1 
ATOM   1548 C C   . THR   A 1 211 ? 10.125  34.384 1.312   1.00 22.69 ? 233 THR   A C   1 
ATOM   1549 O O   . THR   A 1 211 ? 9.239   35.194 1.034   1.00 22.97 ? 233 THR   A O   1 
ATOM   1550 C CB  . THR   A 1 211 ? 12.589  35.069 1.163   1.00 24.11 ? 233 THR   A CB  1 
ATOM   1551 O OG1 . THR   A 1 211 ? 12.485  36.483 1.009   1.00 24.09 ? 233 THR   A OG1 1 
ATOM   1552 C CG2 . THR   A 1 211 ? 13.929  34.640 0.590   1.00 25.42 ? 233 THR   A CG2 1 
ATOM   1553 N N   . LEU   A 1 212 ? 10.016  33.510 2.322   1.00 22.88 ? 234 LEU   A N   1 
ATOM   1554 C CA  . LEU   A 1 212 ? 8.781   33.356 3.079   1.00 23.78 ? 234 LEU   A CA  1 
ATOM   1555 C C   . LEU   A 1 212 ? 8.659   34.410 4.183   1.00 23.58 ? 234 LEU   A C   1 
ATOM   1556 O O   . LEU   A 1 212 ? 8.072   34.159 5.227   1.00 26.72 ? 234 LEU   A O   1 
ATOM   1557 C CB  . LEU   A 1 212 ? 8.672   31.927 3.614   1.00 24.80 ? 234 LEU   A CB  1 
ATOM   1558 C CG  . LEU   A 1 212 ? 8.453   30.839 2.560   1.00 26.34 ? 234 LEU   A CG  1 
ATOM   1559 C CD1 . LEU   A 1 212 ? 8.168   29.490 3.201   1.00 27.32 ? 234 LEU   A CD1 1 
ATOM   1560 C CD2 . LEU   A 1 212 ? 7.326   31.185 1.613   1.00 26.73 ? 234 LEU   A CD2 1 
ATOM   1561 N N   . ASP   A 1 213 ? 9.138   35.620 3.905   1.00 25.60 ? 235 ASP   A N   1 
ATOM   1562 C CA  . ASP   A 1 213 ? 8.929   36.797 4.734   1.00 26.65 ? 235 ASP   A CA  1 
ATOM   1563 C C   . ASP   A 1 213 ? 8.193   37.849 3.899   1.00 25.95 ? 235 ASP   A C   1 
ATOM   1564 O O   . ASP   A 1 213 ? 8.444   39.043 4.037   1.00 26.21 ? 235 ASP   A O   1 
ATOM   1565 C CB  . ASP   A 1 213 ? 10.267  37.345 5.212   1.00 28.30 ? 235 ASP   A CB  1 
ATOM   1566 C CG  . ASP   A 1 213 ? 11.283  37.624 4.107   1.00 29.02 ? 235 ASP   A CG  1 
ATOM   1567 O OD1 . ASP   A 1 213 ? 10.939  37.426 2.928   1.00 30.50 ? 235 ASP   A OD1 1 
ATOM   1568 O OD2 . ASP   A 1 213 ? 12.424  38.024 4.421   1.00 31.76 ? 235 ASP   A OD2 1 
ATOM   1569 N N   . ASN   A 1 214 ? 7.324   37.399 2.990   1.00 26.36 ? 236 ASN   A N   1 
ATOM   1570 C CA  . ASN   A 1 214 ? 6.481   38.292 2.211   1.00 26.13 ? 236 ASN   A CA  1 
ATOM   1571 C C   . ASN   A 1 214 ? 7.309   39.230 1.327   1.00 25.68 ? 236 ASN   A C   1 
ATOM   1572 O O   . ASN   A 1 214 ? 6.961   40.401 1.184   1.00 25.25 ? 236 ASN   A O   1 
ATOM   1573 C CB  . ASN   A 1 214 ? 5.578   39.120 3.120   1.00 26.96 ? 236 ASN   A CB  1 
ATOM   1574 C CG  . ASN   A 1 214 ? 4.877   38.282 4.163   1.00 27.33 ? 236 ASN   A CG  1 
ATOM   1575 O OD1 . ASN   A 1 214 ? 4.065   37.415 3.820   1.00 25.55 ? 236 ASN   A OD1 1 
ATOM   1576 N ND2 . ASN   A 1 214 ? 5.163   38.534 5.433   1.00 29.10 ? 236 ASN   A ND2 1 
ATOM   1577 N N   . THR   A 1 215 ? 8.375   38.702 0.706   1.00 25.63 ? 237 THR   A N   1 
ATOM   1578 C CA  . THR   A 1 215 ? 9.348   39.511 -0.016  1.00 25.09 ? 237 THR   A CA  1 
ATOM   1579 C C   . THR   A 1 215 ? 9.785   38.784 -1.289  1.00 24.09 ? 237 THR   A C   1 
ATOM   1580 O O   . THR   A 1 215 ? 10.075  37.581 -1.273  1.00 23.32 ? 237 THR   A O   1 
ATOM   1581 C CB  . THR   A 1 215 ? 10.547  39.800 0.887   1.00 25.35 ? 237 THR   A CB  1 
ATOM   1582 O OG1 . THR   A 1 215 ? 10.047  40.422 2.066   1.00 27.00 ? 237 THR   A OG1 1 
ATOM   1583 C CG2 . THR   A 1 215 ? 11.570  40.707 0.237   1.00 26.46 ? 237 THR   A CG2 1 
ATOM   1584 N N   . LEU   A 1 216 ? 9.815   39.545 -2.387  1.00 23.36 ? 238 LEU   A N   1 
ATOM   1585 C CA  . LEU   A 1 216 ? 10.471  39.173 -3.631  1.00 23.75 ? 238 LEU   A CA  1 
ATOM   1586 C C   . LEU   A 1 216 ? 11.677  40.080 -3.831  1.00 24.48 ? 238 LEU   A C   1 
ATOM   1587 O O   . LEU   A 1 216 ? 11.609  41.272 -3.533  1.00 26.66 ? 238 LEU   A O   1 
ATOM   1588 C CB  . LEU   A 1 216 ? 9.501   39.346 -4.802  1.00 24.89 ? 238 LEU   A CB  1 
ATOM   1589 C CG  . LEU   A 1 216 ? 8.454   38.248 -4.973  1.00 25.19 ? 238 LEU   A CG  1 
ATOM   1590 C CD1 . LEU   A 1 216 ? 7.279   38.775 -5.771  1.00 25.79 ? 238 LEU   A CD1 1 
ATOM   1591 C CD2 . LEU   A 1 216 ? 9.060   37.022 -5.664  1.00 25.27 ? 238 LEU   A CD2 1 
ATOM   1592 N N   . LYS   A 1 217 ? 12.767  39.521 -4.363  1.00 23.64 ? 239 LYS   A N   1 
ATOM   1593 C CA  . LYS   A 1 217 ? 13.948  40.325 -4.637  1.00 23.90 ? 239 LYS   A CA  1 
ATOM   1594 C C   . LYS   A 1 217 ? 14.480  40.023 -6.030  1.00 23.48 ? 239 LYS   A C   1 
ATOM   1595 O O   . LYS   A 1 217 ? 14.447  38.874 -6.465  1.00 24.65 ? 239 LYS   A O   1 
ATOM   1596 C CB  . LYS   A 1 217 ? 15.055  40.035 -3.627  1.00 25.03 ? 239 LYS   A CB  1 
ATOM   1597 C CG  . LYS   A 1 217 ? 14.737  40.498 -2.222  1.00 26.96 ? 239 LYS   A CG  1 
ATOM   1598 C CD  . LYS   A 1 217 ? 15.856  40.271 -1.213  1.00 28.70 ? 239 LYS   A CD  1 
ATOM   1599 C CE  . LYS   A 1 217 ? 15.548  40.964 0.076   1.00 33.06 ? 239 LYS   A CE  1 
ATOM   1600 N NZ  . LYS   A 1 217 ? 16.448  40.533 1.148   1.00 36.37 ? 239 LYS   A NZ  1 
ATOM   1601 N N   . LEU   A 1 218 ? 15.010  41.061 -6.686  1.00 23.30 ? 240 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 218 ? 15.697  40.909 -7.954  1.00 24.09 ? 240 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 218 ? 17.196  41.023 -7.723  1.00 24.50 ? 240 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 218 ? 17.650  42.040 -7.207  1.00 25.65 ? 240 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 218 ? 15.223  41.973 -8.937  1.00 25.12 ? 240 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 218 ? 15.724  41.793 -10.368 1.00 25.98 ? 240 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 218 ? 15.112  40.534 -10.998 1.00 26.04 ? 240 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 218 ? 15.391  43.049 -11.146 1.00 28.11 ? 240 LEU   A CD2 1 
ATOM   1609 N N   . TRP   A 1 219 ? 17.934  39.980 -8.127  1.00 24.51 ? 241 TRP   A N   1 
ATOM   1610 C CA  . TRP   A 1 219 ? 19.368  39.895 -7.902  1.00 26.22 ? 241 TRP   A CA  1 
ATOM   1611 C C   . TRP   A 1 219 ? 20.112  40.024 -9.223  1.00 27.04 ? 241 TRP   A C   1 
ATOM   1612 O O   . TRP   A 1 219 ? 19.712  39.433 -10.219 1.00 26.93 ? 241 TRP   A O   1 
ATOM   1613 C CB  . TRP   A 1 219 ? 19.744  38.563 -7.239  1.00 27.31 ? 241 TRP   A CB  1 
ATOM   1614 C CG  . TRP   A 1 219 ? 19.254  38.410 -5.827  1.00 29.08 ? 241 TRP   A CG  1 
ATOM   1615 C CD1 . TRP   A 1 219 ? 18.014  38.005 -5.427  1.00 30.45 ? 241 TRP   A CD1 1 
ATOM   1616 C CD2 . TRP   A 1 219 ? 20.016  38.629 -4.624  1.00 29.94 ? 241 TRP   A CD2 1 
ATOM   1617 N NE1 . TRP   A 1 219 ? 17.941  37.988 -4.063  1.00 30.55 ? 241 TRP   A NE1 1 
ATOM   1618 C CE2 . TRP   A 1 219 ? 19.153  38.351 -3.544  1.00 31.06 ? 241 TRP   A CE2 1 
ATOM   1619 C CE3 . TRP   A 1 219 ? 21.328  39.028 -4.356  1.00 31.12 ? 241 TRP   A CE3 1 
ATOM   1620 C CZ2 . TRP   A 1 219 ? 19.558  38.471 -2.220  1.00 33.30 ? 241 TRP   A CZ2 1 
ATOM   1621 C CZ3 . TRP   A 1 219 ? 21.731  39.144 -3.044  1.00 34.17 ? 241 TRP   A CZ3 1 
ATOM   1622 C CH2 . TRP   A 1 219 ? 20.857  38.863 -1.991  1.00 33.94 ? 241 TRP   A CH2 1 
ATOM   1623 N N   . ASP   A 1 220 ? 21.221  40.769 -9.209  1.00 28.69 ? 242 ASP   A N   1 
ATOM   1624 C CA  . ASP   A 1 220 ? 22.146  40.764 -10.325 1.00 30.14 ? 242 ASP   A CA  1 
ATOM   1625 C C   . ASP   A 1 220 ? 23.022  39.532 -10.156 1.00 31.73 ? 242 ASP   A C   1 
ATOM   1626 O O   . ASP   A 1 220 ? 23.715  39.400 -9.150  1.00 33.29 ? 242 ASP   A O   1 
ATOM   1627 C CB  . ASP   A 1 220 ? 22.925  42.067 -10.379 1.00 32.64 ? 242 ASP   A CB  1 
ATOM   1628 C CG  . ASP   A 1 220 ? 23.889  42.203 -11.545 1.00 34.23 ? 242 ASP   A CG  1 
ATOM   1629 O OD1 . ASP   A 1 220 ? 24.705  41.278 -11.729 1.00 33.61 ? 242 ASP   A OD1 1 
ATOM   1630 O OD2 . ASP   A 1 220 ? 23.809  43.235 -12.257 1.00 37.93 ? 242 ASP   A OD2 1 
ATOM   1631 N N   . TYR   A 1 221 ? 22.951  38.616 -11.126 1.00 31.60 ? 243 TYR   A N   1 
ATOM   1632 C CA  . TYR   A 1 221 ? 23.683  37.365 -11.032 1.00 31.76 ? 243 TYR   A CA  1 
ATOM   1633 C C   . TYR   A 1 221 ? 25.194  37.629 -11.067 1.00 32.88 ? 243 TYR   A C   1 
ATOM   1634 O O   . TYR   A 1 221 ? 25.917  37.099 -10.221 1.00 30.83 ? 243 TYR   A O   1 
ATOM   1635 C CB  . TYR   A 1 221 ? 23.227  36.349 -12.090 1.00 30.97 ? 243 TYR   A CB  1 
ATOM   1636 C CG  . TYR   A 1 221 ? 24.234  35.215 -12.194 1.00 31.07 ? 243 TYR   A CG  1 
ATOM   1637 C CD1 . TYR   A 1 221 ? 24.488  34.396 -11.102 1.00 30.63 ? 243 TYR   A CD1 1 
ATOM   1638 C CD2 . TYR   A 1 221 ? 24.988  35.020 -13.345 1.00 33.50 ? 243 TYR   A CD2 1 
ATOM   1639 C CE1 . TYR   A 1 221 ? 25.436  33.386 -11.160 1.00 33.38 ? 243 TYR   A CE1 1 
ATOM   1640 C CE2 . TYR   A 1 221 ? 25.947  34.019 -13.415 1.00 34.10 ? 243 TYR   A CE2 1 
ATOM   1641 C CZ  . TYR   A 1 221 ? 26.165  33.195 -12.323 1.00 34.42 ? 243 TYR   A CZ  1 
ATOM   1642 O OH  . TYR   A 1 221 ? 27.105  32.210 -12.403 1.00 37.79 ? 243 TYR   A OH  1 
ATOM   1643 N N   . SER   A 1 222 ? 25.656  38.446 -12.033 1.00 33.78 ? 244 SER   A N   1 
ATOM   1644 C CA  . SER   A 1 222 ? 27.070  38.748 -12.212 1.00 36.21 ? 244 SER   A CA  1 
ATOM   1645 C C   . SER   A 1 222 ? 27.709  39.260 -10.918 1.00 39.50 ? 244 SER   A C   1 
ATOM   1646 O O   . SER   A 1 222 ? 28.785  38.805 -10.529 1.00 42.64 ? 244 SER   A O   1 
ATOM   1647 C CB  . SER   A 1 222 ? 27.274  39.755 -13.334 1.00 37.59 ? 244 SER   A CB  1 
ATOM   1648 N N   . LYS   A 1 223 ? 27.038  40.215 -10.260 1.00 39.39 ? 245 LYS   A N   1 
ATOM   1649 C CA  . LYS   A 1 223 ? 27.605  40.951 -9.137  1.00 40.52 ? 245 LYS   A CA  1 
ATOM   1650 C C   . LYS   A 1 223 ? 27.204  40.339 -7.794  1.00 40.96 ? 245 LYS   A C   1 
ATOM   1651 O O   . LYS   A 1 223 ? 27.808  40.662 -6.775  1.00 42.63 ? 245 LYS   A O   1 
ATOM   1652 C CB  . LYS   A 1 223 ? 27.148  42.417 -9.173  1.00 41.42 ? 245 LYS   A CB  1 
ATOM   1653 C CG  . LYS   A 1 223 ? 27.488  43.193 -10.452 1.00 41.68 ? 245 LYS   A CG  1 
ATOM   1654 C CD  . LYS   A 1 223 ? 27.103  44.669 -10.414 1.00 43.27 ? 245 LYS   A CD  1 
ATOM   1655 N N   . GLY   A 1 224 ? 26.168  39.487 -7.785  1.00 39.03 ? 246 GLY   A N   1 
ATOM   1656 C CA  . GLY   A 1 224 ? 25.682  38.870 -6.559  1.00 39.06 ? 246 GLY   A CA  1 
ATOM   1657 C C   . GLY   A 1 224 ? 25.053  39.873 -5.588  1.00 38.38 ? 246 GLY   A C   1 
ATOM   1658 O O   . GLY   A 1 224 ? 25.140  39.678 -4.380  1.00 40.68 ? 246 GLY   A O   1 
ATOM   1659 N N   . LYS   A 1 225 ? 24.373  40.904 -6.118  1.00 36.16 ? 247 LYS   A N   1 
ATOM   1660 C CA  . LYS   A 1 225 ? 23.833  41.999 -5.321  1.00 34.04 ? 247 LYS   A CA  1 
ATOM   1661 C C   . LYS   A 1 225 ? 22.326  42.106 -5.560  1.00 33.15 ? 247 LYS   A C   1 
ATOM   1662 O O   . LYS   A 1 225 ? 21.857  41.879 -6.675  1.00 31.06 ? 247 LYS   A O   1 
ATOM   1663 C CB  . LYS   A 1 225 ? 24.481  43.334 -5.719  1.00 33.44 ? 247 LYS   A CB  1 
ATOM   1664 N N   . CYS   A 1 226 ? 21.574  42.466 -4.511  1.00 33.01 ? 248 CYS   A N   1 
ATOM   1665 C CA  . CYS   A 1 226 ? 20.137  42.706 -4.618  1.00 31.57 ? 248 CYS   A CA  1 
ATOM   1666 C C   . CYS   A 1 226 ? 19.875  44.097 -5.194  1.00 31.15 ? 248 CYS   A C   1 
ATOM   1667 O O   . CYS   A 1 226 ? 20.381  45.090 -4.664  1.00 33.47 ? 248 CYS   A O   1 
ATOM   1668 C CB  . CYS   A 1 226 ? 19.454  42.612 -3.258  1.00 32.91 ? 248 CYS   A CB  1 
ATOM   1669 S SG  . CYS   A 1 226 ? 17.664  42.883 -3.327  1.00 35.46 ? 248 CYS   A SG  1 
ATOM   1670 N N   . LEU   A 1 227 ? 19.090  44.154 -6.272  1.00 30.75 ? 249 LEU   A N   1 
ATOM   1671 C CA  . LEU   A 1 227 ? 18.837  45.382 -7.014  1.00 31.17 ? 249 LEU   A CA  1 
ATOM   1672 C C   . LEU   A 1 227 ? 17.485  45.977 -6.638  1.00 30.81 ? 249 LEU   A C   1 
ATOM   1673 O O   . LEU   A 1 227 ? 17.343  47.195 -6.596  1.00 33.32 ? 249 LEU   A O   1 
ATOM   1674 C CB  . LEU   A 1 227 ? 18.848  45.094 -8.513  1.00 33.33 ? 249 LEU   A CB  1 
ATOM   1675 C CG  . LEU   A 1 227 ? 20.193  44.759 -9.156  1.00 34.42 ? 249 LEU   A CG  1 
ATOM   1676 C CD1 . LEU   A 1 227 ? 19.951  44.641 -10.647 1.00 34.88 ? 249 LEU   A CD1 1 
ATOM   1677 C CD2 . LEU   A 1 227 ? 21.296  45.764 -8.867  1.00 34.60 ? 249 LEU   A CD2 1 
ATOM   1678 N N   . LYS   A 1 228 ? 16.480  45.113 -6.451  1.00 29.67 ? 250 LYS   A N   1 
ATOM   1679 C CA  . LYS   A 1 228 ? 15.119  45.553 -6.194  1.00 28.70 ? 250 LYS   A CA  1 
ATOM   1680 C C   . LYS   A 1 228 ? 14.480  44.637 -5.160  1.00 27.83 ? 250 LYS   A C   1 
ATOM   1681 O O   . LYS   A 1 228 ? 14.784  43.446 -5.113  1.00 27.08 ? 250 LYS   A O   1 
ATOM   1682 C CB  . LYS   A 1 228 ? 14.253  45.501 -7.458  1.00 28.31 ? 250 LYS   A CB  1 
ATOM   1683 C CG  . LYS   A 1 228 ? 14.752  46.316 -8.645  1.00 29.90 ? 250 LYS   A CG  1 
ATOM   1684 C CD  . LYS   A 1 228 ? 14.664  47.826 -8.474  1.00 31.36 ? 250 LYS   A CD  1 
ATOM   1685 C CE  . LYS   A 1 228 ? 15.277  48.535 -9.636  1.00 32.41 ? 250 LYS   A CE  1 
ATOM   1686 N NZ  . LYS   A 1 228 ? 15.182  49.989 -9.494  1.00 33.36 ? 250 LYS   A NZ  1 
ATOM   1687 N N   . THR   A 1 229 ? 13.558  45.210 -4.384  1.00 28.07 ? 251 THR   A N   1 
ATOM   1688 C CA  . THR   A 1 229 ? 12.747  44.481 -3.425  1.00 29.49 ? 251 THR   A CA  1 
ATOM   1689 C C   . THR   A 1 229 ? 11.276  44.808 -3.698  1.00 28.80 ? 251 THR   A C   1 
ATOM   1690 O O   . THR   A 1 229 ? 10.928  45.976 -3.861  1.00 30.52 ? 251 THR   A O   1 
ATOM   1691 C CB  . THR   A 1 229 ? 13.168  44.876 -2.006  1.00 32.62 ? 251 THR   A CB  1 
ATOM   1692 O OG1 . THR   A 1 229 ? 14.525  44.489 -1.795  1.00 34.22 ? 251 THR   A OG1 1 
ATOM   1693 C CG2 . THR   A 1 229 ? 12.334  44.182 -0.946  1.00 35.02 ? 251 THR   A CG2 1 
ATOM   1694 N N   . TYR   A 1 230 ? 10.424  43.775 -3.740  1.00 26.73 ? 252 TYR   A N   1 
ATOM   1695 C CA  . TYR   A 1 230 ? 8.996   43.928 -3.972  1.00 26.02 ? 252 TYR   A CA  1 
ATOM   1696 C C   . TYR   A 1 230 ? 8.234   43.357 -2.776  1.00 26.44 ? 252 TYR   A C   1 
ATOM   1697 O O   . TYR   A 1 230 ? 8.449   42.206 -2.392  1.00 25.52 ? 252 TYR   A O   1 
ATOM   1698 C CB  . TYR   A 1 230 ? 8.569   43.229 -5.271  1.00 25.04 ? 252 TYR   A CB  1 
ATOM   1699 C CG  . TYR   A 1 230 ? 9.479   43.562 -6.452  1.00 24.53 ? 252 TYR   A CG  1 
ATOM   1700 C CD1 . TYR   A 1 230 ? 9.271   44.699 -7.219  1.00 24.82 ? 252 TYR   A CD1 1 
ATOM   1701 C CD2 . TYR   A 1 230 ? 10.575  42.763 -6.774  1.00 25.71 ? 252 TYR   A CD2 1 
ATOM   1702 C CE1 . TYR   A 1 230 ? 10.095  45.012 -8.289  1.00 23.89 ? 252 TYR   A CE1 1 
ATOM   1703 C CE2 . TYR   A 1 230 ? 11.413  43.074 -7.834  1.00 24.07 ? 252 TYR   A CE2 1 
ATOM   1704 C CZ  . TYR   A 1 230 ? 11.176  44.206 -8.589  1.00 23.77 ? 252 TYR   A CZ  1 
ATOM   1705 O OH  . TYR   A 1 230 ? 12.005  44.544 -9.612  1.00 23.00 ? 252 TYR   A OH  1 
ATOM   1706 N N   . THR   A 1 231 ? 7.355   44.182 -2.193  1.00 27.42 ? 253 THR   A N   1 
ATOM   1707 C CA  . THR   A 1 231 ? 6.630   43.821 -0.980  1.00 27.31 ? 253 THR   A CA  1 
ATOM   1708 C C   . THR   A 1 231 ? 5.176   44.270 -1.111  1.00 27.41 ? 253 THR   A C   1 
ATOM   1709 O O   . THR   A 1 231 ? 4.797   44.873 -2.116  1.00 28.36 ? 253 THR   A O   1 
ATOM   1710 C CB  . THR   A 1 231 ? 7.297   44.438 0.249   1.00 27.84 ? 253 THR   A CB  1 
ATOM   1711 O OG1 . THR   A 1 231 ? 7.206   45.855 0.117   1.00 27.71 ? 253 THR   A OG1 1 
ATOM   1712 C CG2 . THR   A 1 231 ? 8.742   43.996 0.405   1.00 28.11 ? 253 THR   A CG2 1 
ATOM   1713 N N   . GLY   A 1 232 ? 4.378   43.961 -0.083  1.00 28.78 ? 254 GLY   A N   1 
ATOM   1714 C CA  . GLY   A 1 232 ? 2.973   44.332 -0.030  1.00 29.49 ? 254 GLY   A CA  1 
ATOM   1715 C C   . GLY   A 1 232 ? 2.059   43.116 -0.174  1.00 29.17 ? 254 GLY   A C   1 
ATOM   1716 O O   . GLY   A 1 232 ? 0.893   43.163 0.213   1.00 30.45 ? 254 GLY   A O   1 
ATOM   1717 N N   . HIS   A 1 233 ? 2.590   42.030 -0.741  1.00 27.78 ? 255 HIS   A N   1 
ATOM   1718 C CA  . HIS   A 1 233 ? 1.833   40.795 -0.896  1.00 26.49 ? 255 HIS   A CA  1 
ATOM   1719 C C   . HIS   A 1 233 ? 2.001   39.929 0.354   1.00 26.56 ? 255 HIS   A C   1 
ATOM   1720 O O   . HIS   A 1 233 ? 2.727   40.291 1.275   1.00 26.53 ? 255 HIS   A O   1 
ATOM   1721 C CB  . HIS   A 1 233 ? 2.279   40.059 -2.164  1.00 26.52 ? 255 HIS   A CB  1 
ATOM   1722 C CG  . HIS   A 1 233 ? 3.691   39.565 -2.125  1.00 28.26 ? 255 HIS   A CG  1 
ATOM   1723 N ND1 . HIS   A 1 233 ? 4.768   40.378 -1.838  1.00 28.78 ? 255 HIS   A ND1 1 
ATOM   1724 C CD2 . HIS   A 1 233 ? 4.206   38.346 -2.381  1.00 30.01 ? 255 HIS   A CD2 1 
ATOM   1725 C CE1 . HIS   A 1 233 ? 5.883   39.658 -1.898  1.00 30.45 ? 255 HIS   A CE1 1 
ATOM   1726 N NE2 . HIS   A 1 233 ? 5.564   38.424 -2.228  1.00 29.59 ? 255 HIS   A NE2 1 
ATOM   1727 N N   . LYS   A 1 234 ? 1.303   38.790 0.382   1.00 25.21 ? 256 LYS   A N   1 
ATOM   1728 C CA  . LYS   A 1 234 ? 1.388   37.854 1.488   1.00 25.21 ? 256 LYS   A CA  1 
ATOM   1729 C C   . LYS   A 1 234 ? 2.000   36.542 1.001   1.00 23.44 ? 256 LYS   A C   1 
ATOM   1730 O O   . LYS   A 1 234 ? 1.430   35.875 0.136   1.00 22.94 ? 256 LYS   A O   1 
ATOM   1731 C CB  . LYS   A 1 234 ? 0.018   37.556 2.108   1.00 27.47 ? 256 LYS   A CB  1 
ATOM   1732 C CG  . LYS   A 1 234 ? 0.081   36.806 3.431   1.00 32.90 ? 256 LYS   A CG  1 
ATOM   1733 C CD  . LYS   A 1 234 ? -1.278  36.635 4.102   1.00 37.79 ? 256 LYS   A CD  1 
ATOM   1734 C CE  . LYS   A 1 234 ? -1.196  35.751 5.299   1.00 41.68 ? 256 LYS   A CE  1 
ATOM   1735 N NZ  . LYS   A 1 234 ? -2.503  35.145 5.540   1.00 45.31 ? 256 LYS   A NZ  1 
ATOM   1736 N N   . ASN   A 1 235 ? 3.132   36.163 1.603   1.00 23.45 ? 257 ASN   A N   1 
ATOM   1737 C CA  . ASN   A 1 235 ? 3.835   34.947 1.232   1.00 23.36 ? 257 ASN   A CA  1 
ATOM   1738 C C   . ASN   A 1 235 ? 4.706   34.484 2.399   1.00 23.94 ? 257 ASN   A C   1 
ATOM   1739 O O   . ASN   A 1 235 ? 5.870   34.878 2.496   1.00 24.63 ? 257 ASN   A O   1 
ATOM   1740 C CB  . ASN   A 1 235 ? 4.626   35.164 -0.054  1.00 24.06 ? 257 ASN   A CB  1 
ATOM   1741 C CG  . ASN   A 1 235 ? 5.224   33.894 -0.613  1.00 23.57 ? 257 ASN   A CG  1 
ATOM   1742 O OD1 . ASN   A 1 235 ? 6.105   33.958 -1.474  1.00 25.16 ? 257 ASN   A OD1 1 
ATOM   1743 N ND2 . ASN   A 1 235 ? 4.765   32.739 -0.162  1.00 22.80 ? 257 ASN   A ND2 1 
ATOM   1744 N N   A GLU   A 1 236 ? 4.120   33.663 3.282   0.50 24.98 ? 258 GLU   A N   1 
ATOM   1745 N N   B GLU   A 1 236 ? 4.126   33.663 3.289   0.50 24.60 ? 258 GLU   A N   1 
ATOM   1746 C CA  A GLU   A 1 236 ? 4.818   33.161 4.455   0.50 25.27 ? 258 GLU   A CA  1 
ATOM   1747 C CA  B GLU   A 1 236 ? 4.835   33.143 4.451   0.50 24.51 ? 258 GLU   A CA  1 
ATOM   1748 C C   A GLU   A 1 236 ? 4.719   31.636 4.565   0.50 24.08 ? 258 GLU   A C   1 
ATOM   1749 C C   B GLU   A 1 236 ? 4.791   31.616 4.520   0.50 23.93 ? 258 GLU   A C   1 
ATOM   1750 O O   A GLU   A 1 236 ? 5.238   31.068 5.524   0.50 23.43 ? 258 GLU   A O   1 
ATOM   1751 O O   B GLU   A 1 236 ? 5.397   31.033 5.416   0.50 23.43 ? 258 GLU   A O   1 
ATOM   1752 C CB  A GLU   A 1 236 ? 4.281   33.863 5.710   0.50 27.47 ? 258 GLU   A CB  1 
ATOM   1753 C CB  B GLU   A 1 236 ? 4.236   33.664 5.760   0.50 26.39 ? 258 GLU   A CB  1 
ATOM   1754 C CG  A GLU   A 1 236 ? 2.779   33.685 5.935   0.50 28.18 ? 258 GLU   A CG  1 
ATOM   1755 C CG  B GLU   A 1 236 ? 4.286   35.181 5.892   0.50 25.93 ? 258 GLU   A CG  1 
ATOM   1756 C CD  A GLU   A 1 236 ? 2.218   34.295 7.212   0.50 29.91 ? 258 GLU   A CD  1 
ATOM   1757 C CD  B GLU   A 1 236 ? 3.755   35.740 7.197   0.50 27.40 ? 258 GLU   A CD  1 
ATOM   1758 O OE1 A GLU   A 1 236 ? 1.670   33.527 8.032   0.50 30.48 ? 258 GLU   A OE1 1 
ATOM   1759 O OE1 B GLU   A 1 236 ? 3.309   34.988 8.094   0.50 27.18 ? 258 GLU   A OE1 1 
ATOM   1760 O OE2 A GLU   A 1 236 ? 2.312   35.533 7.388   0.50 31.75 ? 258 GLU   A OE2 1 
ATOM   1761 O OE2 B GLU   A 1 236 ? 3.799   36.976 7.291   0.50 29.23 ? 258 GLU   A OE2 1 
ATOM   1762 N N   . LYS   A 1 237 ? 4.072   30.972 3.593   1.00 23.83 ? 259 LYS   A N   1 
ATOM   1763 C CA  . LYS   A 1 237 ? 3.743   29.559 3.729   1.00 24.25 ? 259 LYS   A CA  1 
ATOM   1764 C C   . LYS   A 1 237 ? 4.080   28.757 2.474   1.00 24.18 ? 259 LYS   A C   1 
ATOM   1765 O O   . LYS   A 1 237 ? 4.679   27.688 2.578   1.00 25.00 ? 259 LYS   A O   1 
ATOM   1766 C CB  . LYS   A 1 237 ? 2.264   29.388 4.096   1.00 26.87 ? 259 LYS   A CB  1 
ATOM   1767 C CG  . LYS   A 1 237 ? 1.852   27.949 4.374   1.00 31.21 ? 259 LYS   A CG  1 
ATOM   1768 C CD  . LYS   A 1 237 ? 0.455   27.799 4.966   1.00 34.17 ? 259 LYS   A CD  1 
ATOM   1769 C CE  . LYS   A 1 237 ? 0.174   26.374 5.285   1.00 38.44 ? 259 LYS   A CE  1 
ATOM   1770 N NZ  . LYS   A 1 237 ? -1.140  26.165 5.892   1.00 42.55 ? 259 LYS   A NZ  1 
ATOM   1771 N N   . TYR   A 1 238 ? 3.683   29.255 1.298   1.00 23.33 ? 260 TYR   A N   1 
ATOM   1772 C CA  . TYR   A 1 238 ? 3.708   28.453 0.083   1.00 22.57 ? 260 TYR   A CA  1 
ATOM   1773 C C   . TYR   A 1 238 ? 4.798   28.893 -0.890  1.00 21.37 ? 260 TYR   A C   1 
ATOM   1774 O O   . TYR   A 1 238 ? 5.260   30.031 -0.869  1.00 21.56 ? 260 TYR   A O   1 
ATOM   1775 C CB  . TYR   A 1 238 ? 2.358   28.572 -0.624  1.00 22.38 ? 260 TYR   A CB  1 
ATOM   1776 C CG  . TYR   A 1 238 ? 1.234   27.866 0.123   1.00 22.13 ? 260 TYR   A CG  1 
ATOM   1777 C CD1 . TYR   A 1 238 ? 1.057   26.495 0.034   1.00 22.79 ? 260 TYR   A CD1 1 
ATOM   1778 C CD2 . TYR   A 1 238 ? 0.357   28.579 0.920   1.00 22.77 ? 260 TYR   A CD2 1 
ATOM   1779 C CE1 . TYR   A 1 238 ? 0.031   25.850 0.703   1.00 23.47 ? 260 TYR   A CE1 1 
ATOM   1780 C CE2 . TYR   A 1 238 ? -0.673  27.954 1.596   1.00 24.38 ? 260 TYR   A CE2 1 
ATOM   1781 C CZ  . TYR   A 1 238 ? -0.827  26.585 1.496   1.00 24.43 ? 260 TYR   A CZ  1 
ATOM   1782 O OH  . TYR   A 1 238 ? -1.828  25.991 2.176   1.00 28.77 ? 260 TYR   A OH  1 
ATOM   1783 N N   . CYS   A 1 239 ? 5.195   27.948 -1.745  1.00 21.14 ? 261 CYS   A N   1 
ATOM   1784 C CA  . CYS   A 1 239 ? 6.067   28.229 -2.875  1.00 19.28 ? 261 CYS   A CA  1 
ATOM   1785 C C   . CYS   A 1 239 ? 5.214   28.756 -4.019  1.00 18.46 ? 261 CYS   A C   1 
ATOM   1786 O O   . CYS   A 1 239 ? 4.585   27.991 -4.736  1.00 19.90 ? 261 CYS   A O   1 
ATOM   1787 C CB  . CYS   A 1 239 ? 6.860   26.994 -3.284  1.00 19.02 ? 261 CYS   A CB  1 
ATOM   1788 S SG  . CYS   A 1 239 ? 7.920   26.376 -1.951  1.00 20.84 ? 261 CYS   A SG  1 
ATOM   1789 N N   . ILE   A 1 240 ? 5.172   30.078 -4.144  1.00 18.52 ? 262 ILE   A N   1 
ATOM   1790 C CA  . ILE   A 1 240 ? 4.308   30.740 -5.105  1.00 19.24 ? 262 ILE   A CA  1 
ATOM   1791 C C   . ILE   A 1 240 ? 5.143   31.157 -6.309  1.00 19.83 ? 262 ILE   A C   1 
ATOM   1792 O O   . ILE   A 1 240 ? 6.189   31.783 -6.158  1.00 20.55 ? 262 ILE   A O   1 
ATOM   1793 C CB  . ILE   A 1 240 ? 3.614   31.955 -4.475  1.00 20.66 ? 262 ILE   A CB  1 
ATOM   1794 C CG1 . ILE   A 1 240 ? 2.689   31.551 -3.346  1.00 21.77 ? 262 ILE   A CG1 1 
ATOM   1795 C CG2 . ILE   A 1 240 ? 2.881   32.757 -5.554  1.00 20.91 ? 262 ILE   A CG2 1 
ATOM   1796 C CD1 . ILE   A 1 240 ? 2.023   32.724 -2.640  1.00 22.58 ? 262 ILE   A CD1 1 
ATOM   1797 N N   . PHE   A 1 241 ? 4.645   30.841 -7.508  1.00 19.73 ? 263 PHE   A N   1 
ATOM   1798 C CA  . PHE   A 1 241 ? 5.331   31.219 -8.732  1.00 20.15 ? 263 PHE   A CA  1 
ATOM   1799 C C   . PHE   A 1 241 ? 5.243   32.728 -8.951  1.00 21.92 ? 263 PHE   A C   1 
ATOM   1800 O O   . PHE   A 1 241 ? 4.178   33.320 -8.787  1.00 25.80 ? 263 PHE   A O   1 
ATOM   1801 C CB  . PHE   A 1 241 ? 4.718   30.528 -9.951  1.00 19.56 ? 263 PHE   A CB  1 
ATOM   1802 C CG  . PHE   A 1 241 ? 4.939   29.026 -10.033 1.00 19.00 ? 263 PHE   A CG  1 
ATOM   1803 C CD1 . PHE   A 1 241 ? 4.033   28.145 -9.455  1.00 18.05 ? 263 PHE   A CD1 1 
ATOM   1804 C CD2 . PHE   A 1 241 ? 6.026   28.505 -10.727 1.00 18.48 ? 263 PHE   A CD2 1 
ATOM   1805 C CE1 . PHE   A 1 241 ? 4.228   26.777 -9.544  1.00 18.56 ? 263 PHE   A CE1 1 
ATOM   1806 C CE2 . PHE   A 1 241 ? 6.215   27.135 -10.814 1.00 19.10 ? 263 PHE   A CE2 1 
ATOM   1807 C CZ  . PHE   A 1 241 ? 5.317   26.277 -10.224 1.00 19.20 ? 263 PHE   A CZ  1 
ATOM   1808 N N   . ALA   A 1 242 ? 6.372   33.311 -9.381  1.00 20.17 ? 264 ALA   A N   1 
ATOM   1809 C CA  . ALA   A 1 242 ? 6.452   34.690 -9.824  1.00 20.00 ? 264 ALA   A CA  1 
ATOM   1810 C C   . ALA   A 1 242 ? 7.052   34.739 -11.229 1.00 18.92 ? 264 ALA   A C   1 
ATOM   1811 O O   . ALA   A 1 242 ? 7.613   33.760 -11.727 1.00 19.05 ? 264 ALA   A O   1 
ATOM   1812 C CB  . ALA   A 1 242 ? 7.267   35.513 -8.843  1.00 20.68 ? 264 ALA   A CB  1 
ATOM   1813 N N   . ASN   A 1 243 ? 6.908   35.900 -11.867 1.00 19.27 ? 265 ASN   A N   1 
ATOM   1814 C CA  . ASN   A 1 243 ? 7.182   36.043 -13.284 1.00 19.61 ? 265 ASN   A CA  1 
ATOM   1815 C C   . ASN   A 1 243 ? 7.662   37.451 -13.617 1.00 19.85 ? 265 ASN   A C   1 
ATOM   1816 O O   . ASN   A 1 243 ? 7.310   38.410 -12.932 1.00 20.14 ? 265 ASN   A O   1 
ATOM   1817 C CB  . ASN   A 1 243 ? 5.933   35.810 -14.120 1.00 20.74 ? 265 ASN   A CB  1 
ATOM   1818 C CG  . ASN   A 1 243 ? 5.210   34.548 -13.710 1.00 21.53 ? 265 ASN   A CG  1 
ATOM   1819 O OD1 . ASN   A 1 243 ? 4.390   34.567 -12.791 1.00 25.23 ? 265 ASN   A OD1 1 
ATOM   1820 N ND2 . ASN   A 1 243 ? 5.507   33.452 -14.373 1.00 21.56 ? 265 ASN   A ND2 1 
ATOM   1821 N N   . PHE   A 1 244 ? 8.479   37.515 -14.674 1.00 19.93 ? 266 PHE   A N   1 
ATOM   1822 C CA  . PHE   A 1 244 ? 8.722   38.702 -15.468 1.00 20.49 ? 266 PHE   A CA  1 
ATOM   1823 C C   . PHE   A 1 244 ? 7.662   38.797 -16.563 1.00 20.97 ? 266 PHE   A C   1 
ATOM   1824 O O   . PHE   A 1 244 ? 7.520   37.882 -17.376 1.00 22.05 ? 266 PHE   A O   1 
ATOM   1825 C CB  . PHE   A 1 244 ? 10.112  38.601 -16.105 1.00 19.93 ? 266 PHE   A CB  1 
ATOM   1826 C CG  . PHE   A 1 244 ? 11.256  38.536 -15.101 1.00 20.24 ? 266 PHE   A CG  1 
ATOM   1827 C CD1 . PHE   A 1 244 ? 11.628  37.337 -14.513 1.00 20.11 ? 266 PHE   A CD1 1 
ATOM   1828 C CD2 . PHE   A 1 244 ? 11.988  39.677 -14.789 1.00 22.09 ? 266 PHE   A CD2 1 
ATOM   1829 C CE1 . PHE   A 1 244 ? 12.662  37.297 -13.591 1.00 20.62 ? 266 PHE   A CE1 1 
ATOM   1830 C CE2 . PHE   A 1 244 ? 13.031  39.631 -13.877 1.00 21.64 ? 266 PHE   A CE2 1 
ATOM   1831 C CZ  . PHE   A 1 244 ? 13.386  38.437 -13.294 1.00 20.26 ? 266 PHE   A CZ  1 
ATOM   1832 N N   . SER   A 1 245 ? 6.911   39.901 -16.568 1.00 20.08 ? 267 SER   A N   1 
ATOM   1833 C CA  . SER   A 1 245 ? 6.007   40.219 -17.660 1.00 20.63 ? 267 SER   A CA  1 
ATOM   1834 C C   . SER   A 1 245 ? 6.731   41.195 -18.577 1.00 20.76 ? 267 SER   A C   1 
ATOM   1835 O O   . SER   A 1 245 ? 7.161   42.240 -18.095 1.00 21.42 ? 267 SER   A O   1 
ATOM   1836 C CB  . SER   A 1 245 ? 4.707   40.821 -17.150 1.00 21.39 ? 267 SER   A CB  1 
ATOM   1837 O OG  . SER   A 1 245 ? 3.806   41.090 -18.220 1.00 22.98 ? 267 SER   A OG  1 
ATOM   1838 N N   . VAL   A 1 246 ? 6.880   40.836 -19.863 1.00 20.67 ? 268 VAL   A N   1 
ATOM   1839 C CA  . VAL   A 1 246 ? 7.723   41.589 -20.787 1.00 22.70 ? 268 VAL   A CA  1 
ATOM   1840 C C   . VAL   A 1 246 ? 6.982   41.979 -22.074 1.00 22.48 ? 268 VAL   A C   1 
ATOM   1841 O O   . VAL   A 1 246 ? 7.571   42.644 -22.923 1.00 23.41 ? 268 VAL   A O   1 
ATOM   1842 C CB  . VAL   A 1 246 ? 9.008   40.803 -21.129 1.00 24.64 ? 268 VAL   A CB  1 
ATOM   1843 C CG1 . VAL   A 1 246 ? 9.840   40.514 -19.889 1.00 24.98 ? 268 VAL   A CG1 1 
ATOM   1844 C CG2 . VAL   A 1 246 ? 8.732   39.518 -21.897 1.00 26.52 ? 268 VAL   A CG2 1 
ATOM   1845 N N   . THR   A 1 247 ? 5.701   41.609 -22.230 1.00 21.65 ? 269 THR   A N   1 
ATOM   1846 C CA  . THR   A 1 247 ? 5.017   41.809 -23.504 1.00 21.64 ? 269 THR   A CA  1 
ATOM   1847 C C   . THR   A 1 247 ? 4.556   43.256 -23.675 1.00 22.64 ? 269 THR   A C   1 
ATOM   1848 O O   . THR   A 1 247 ? 4.440   43.750 -24.806 1.00 24.07 ? 269 THR   A O   1 
ATOM   1849 C CB  . THR   A 1 247 ? 3.862   40.808 -23.625 1.00 21.25 ? 269 THR   A CB  1 
ATOM   1850 O OG1 . THR   A 1 247 ? 3.063   40.841 -22.438 1.00 21.60 ? 269 THR   A OG1 1 
ATOM   1851 C CG2 . THR   A 1 247 ? 4.398   39.403 -23.833 1.00 21.89 ? 269 THR   A CG2 1 
ATOM   1852 N N   . GLY   A 1 248 ? 4.256   43.917 -22.560 1.00 22.99 ? 270 GLY   A N   1 
ATOM   1853 C CA  . GLY   A 1 248 ? 3.860   45.314 -22.561 1.00 24.91 ? 270 GLY   A CA  1 
ATOM   1854 C C   . GLY   A 1 248 ? 4.787   46.105 -21.651 1.00 25.56 ? 270 GLY   A C   1 
ATOM   1855 O O   . GLY   A 1 248 ? 5.991   46.175 -21.891 1.00 26.16 ? 270 GLY   A O   1 
ATOM   1856 N N   . GLY   A 1 249 ? 4.234   46.629 -20.559 1.00 26.70 ? 271 GLY   A N   1 
ATOM   1857 C CA  . GLY   A 1 249 ? 5.079   47.206 -19.527 1.00 26.88 ? 271 GLY   A CA  1 
ATOM   1858 C C   . GLY   A 1 249 ? 5.937   46.114 -18.894 1.00 26.69 ? 271 GLY   A C   1 
ATOM   1859 O O   . GLY   A 1 249 ? 5.588   44.937 -18.970 1.00 27.76 ? 271 GLY   A O   1 
ATOM   1860 N N   . LYS   A 1 250 ? 7.060   46.511 -18.277 1.00 26.27 ? 272 LYS   A N   1 
ATOM   1861 C CA  . LYS   A 1 250 ? 7.939   45.571 -17.601 1.00 25.95 ? 272 LYS   A CA  1 
ATOM   1862 C C   . LYS   A 1 250 ? 7.498   45.445 -16.149 1.00 26.06 ? 272 LYS   A C   1 
ATOM   1863 O O   . LYS   A 1 250 ? 7.789   46.316 -15.324 1.00 25.98 ? 272 LYS   A O   1 
ATOM   1864 C CB  . LYS   A 1 250 ? 9.406   45.985 -17.764 1.00 25.88 ? 272 LYS   A CB  1 
ATOM   1865 C CG  . LYS   A 1 250 ? 9.844   46.183 -19.215 1.00 28.64 ? 272 LYS   A CG  1 
ATOM   1866 C CD  . LYS   A 1 250 ? 9.455   45.039 -20.148 1.00 30.17 ? 272 LYS   A CD  1 
ATOM   1867 C CE  . LYS   A 1 250 ? 9.563   45.376 -21.605 1.00 33.50 ? 272 LYS   A CE  1 
ATOM   1868 N NZ  . LYS   A 1 250 ? 10.539  44.524 -22.281 1.00 36.03 ? 272 LYS   A NZ  1 
ATOM   1869 N N   . TRP   A 1 251 ? 6.783   44.349 -15.861 1.00 23.81 ? 273 TRP   A N   1 
ATOM   1870 C CA  . TRP   A 1 251 ? 6.265   44.107 -14.526 1.00 23.51 ? 273 TRP   A CA  1 
ATOM   1871 C C   . TRP   A 1 251 ? 6.910   42.869 -13.918 1.00 21.89 ? 273 TRP   A C   1 
ATOM   1872 O O   . TRP   A 1 251 ? 7.494   42.035 -14.613 1.00 21.23 ? 273 TRP   A O   1 
ATOM   1873 C CB  . TRP   A 1 251 ? 4.741   43.907 -14.514 1.00 24.29 ? 273 TRP   A CB  1 
ATOM   1874 C CG  . TRP   A 1 251 ? 3.953   44.712 -15.510 1.00 25.95 ? 273 TRP   A CG  1 
ATOM   1875 C CD1 . TRP   A 1 251 ? 3.214   44.210 -16.545 1.00 26.54 ? 273 TRP   A CD1 1 
ATOM   1876 C CD2 . TRP   A 1 251 ? 3.799   46.146 -15.552 1.00 27.12 ? 273 TRP   A CD2 1 
ATOM   1877 N NE1 . TRP   A 1 251 ? 2.618   45.233 -17.225 1.00 28.32 ? 273 TRP   A NE1 1 
ATOM   1878 C CE2 . TRP   A 1 251 ? 2.958   46.428 -16.645 1.00 28.29 ? 273 TRP   A CE2 1 
ATOM   1879 C CE3 . TRP   A 1 251 ? 4.292   47.211 -14.788 1.00 28.09 ? 273 TRP   A CE3 1 
ATOM   1880 C CZ2 . TRP   A 1 251 ? 2.596   47.729 -16.983 1.00 29.55 ? 273 TRP   A CZ2 1 
ATOM   1881 C CZ3 . TRP   A 1 251 ? 3.927   48.500 -15.119 1.00 29.49 ? 273 TRP   A CZ3 1 
ATOM   1882 C CH2 . TRP   A 1 251 ? 3.102   48.752 -16.212 1.00 29.75 ? 273 TRP   A CH2 1 
ATOM   1883 N N   . ILE   A 1 252 ? 6.698   42.761 -12.608 1.00 21.83 ? 274 ILE   A N   1 
ATOM   1884 C CA  . ILE   A 1 252 ? 6.828   41.529 -11.849 1.00 21.19 ? 274 ILE   A CA  1 
ATOM   1885 C C   . ILE   A 1 252 ? 5.414   41.094 -11.468 1.00 21.66 ? 274 ILE   A C   1 
ATOM   1886 O O   . ILE   A 1 252 ? 4.610   41.924 -11.044 1.00 22.42 ? 274 ILE   A O   1 
ATOM   1887 C CB  . ILE   A 1 252 ? 7.728   41.758 -10.624 1.00 22.05 ? 274 ILE   A CB  1 
ATOM   1888 C CG1 . ILE   A 1 252 ? 9.134   42.210 -11.029 1.00 22.43 ? 274 ILE   A CG1 1 
ATOM   1889 C CG2 . ILE   A 1 252 ? 7.774   40.518 -9.729  1.00 22.07 ? 274 ILE   A CG2 1 
ATOM   1890 C CD1 . ILE   A 1 252 ? 9.939   41.178 -11.788 1.00 23.35 ? 274 ILE   A CD1 1 
ATOM   1891 N N   . VAL   A 1 253 ? 5.110   39.800 -11.654 1.00 20.45 ? 275 VAL   A N   1 
ATOM   1892 C CA  . VAL   A 1 253 ? 3.805   39.255 -11.336 1.00 21.06 ? 275 VAL   A CA  1 
ATOM   1893 C C   . VAL   A 1 253 ? 3.984   38.098 -10.360 1.00 20.39 ? 275 VAL   A C   1 
ATOM   1894 O O   . VAL   A 1 253 ? 4.833   37.240 -10.574 1.00 20.95 ? 275 VAL   A O   1 
ATOM   1895 C CB  . VAL   A 1 253 ? 3.095   38.808 -12.636 1.00 21.22 ? 275 VAL   A CB  1 
ATOM   1896 C CG1 . VAL   A 1 253 ? 1.778   38.101 -12.361 1.00 22.41 ? 275 VAL   A CG1 1 
ATOM   1897 C CG2 . VAL   A 1 253 ? 2.880   39.976 -13.581 1.00 21.08 ? 275 VAL   A CG2 1 
ATOM   1898 N N   . SER   A 1 254 ? 3.156   38.067 -9.309  1.00 20.53 ? 276 SER   A N   1 
ATOM   1899 C CA  . SER   A 1 254 ? 3.181   36.966 -8.353  1.00 21.37 ? 276 SER   A CA  1 
ATOM   1900 C C   . SER   A 1 254 ? 1.766   36.666 -7.861  1.00 21.77 ? 276 SER   A C   1 
ATOM   1901 O O   . SER   A 1 254 ? 0.921   37.551 -7.802  1.00 22.85 ? 276 SER   A O   1 
ATOM   1902 C CB  . SER   A 1 254 ? 4.086   37.274 -7.191  1.00 22.23 ? 276 SER   A CB  1 
ATOM   1903 O OG  . SER   A 1 254 ? 4.208   36.162 -6.306  1.00 22.70 ? 276 SER   A OG  1 
ATOM   1904 N N   . GLY   A 1 255 ? 1.527   35.416 -7.456  1.00 21.00 ? 277 GLY   A N   1 
ATOM   1905 C CA  . GLY   A 1 255 ? 0.387   35.126 -6.600  1.00 20.99 ? 277 GLY   A CA  1 
ATOM   1906 C C   . GLY   A 1 255 ? 0.648   35.597 -5.170  1.00 22.13 ? 277 GLY   A C   1 
ATOM   1907 O O   . GLY   A 1 255 ? 1.699   36.165 -4.871  1.00 21.73 ? 277 GLY   A O   1 
ATOM   1908 N N   . SER   A 1 256 ? -0.311  35.318 -4.282  1.00 21.89 ? 278 SER   A N   1 
ATOM   1909 C CA  . SER   A 1 256 ? -0.283  35.814 -2.919  1.00 22.19 ? 278 SER   A CA  1 
ATOM   1910 C C   . SER   A 1 256 ? -1.262  34.995 -2.087  1.00 22.54 ? 278 SER   A C   1 
ATOM   1911 O O   . SER   A 1 256 ? -2.215  34.441 -2.639  1.00 22.46 ? 278 SER   A O   1 
ATOM   1912 C CB  . SER   A 1 256 ? -0.619  37.283 -2.904  1.00 23.12 ? 278 SER   A CB  1 
ATOM   1913 O OG  . SER   A 1 256 ? -0.619  37.819 -1.599  1.00 23.96 ? 278 SER   A OG  1 
ATOM   1914 N N   . GLU   A 1 257 ? -1.012  34.931 -0.773  1.00 21.36 ? 279 GLU   A N   1 
ATOM   1915 C CA  . GLU   A 1 257 ? -1.796  34.118 0.149   1.00 22.24 ? 279 GLU   A CA  1 
ATOM   1916 C C   . GLU   A 1 257 ? -3.036  34.860 0.645   1.00 23.39 ? 279 GLU   A C   1 
ATOM   1917 O O   . GLU   A 1 257 ? -3.767  34.328 1.489   1.00 23.49 ? 279 GLU   A O   1 
ATOM   1918 C CB  . GLU   A 1 257 ? -0.925  33.674 1.327   1.00 22.04 ? 279 GLU   A CB  1 
ATOM   1919 C CG  . GLU   A 1 257 ? 0.147   32.680 0.892   1.00 21.81 ? 279 GLU   A CG  1 
ATOM   1920 C CD  . GLU   A 1 257 ? 1.333   32.514 1.822   1.00 22.17 ? 279 GLU   A CD  1 
ATOM   1921 O OE1 . GLU   A 1 257 ? 1.330   33.080 2.949   1.00 21.52 ? 279 GLU   A OE1 1 
ATOM   1922 O OE2 . GLU   A 1 257 ? 2.273   31.795 1.391   1.00 23.20 ? 279 GLU   A OE2 1 
ATOM   1923 N N   . ASP   A 1 258 ? -3.250  36.086 0.147   1.00 24.32 ? 280 ASP   A N   1 
ATOM   1924 C CA  . ASP   A 1 258 ? -4.480  36.831 0.386   1.00 25.43 ? 280 ASP   A CA  1 
ATOM   1925 C C   . ASP   A 1 258 ? -5.421  36.712 -0.821  1.00 25.95 ? 280 ASP   A C   1 
ATOM   1926 O O   . ASP   A 1 258 ? -6.371  37.492 -0.955  1.00 26.16 ? 280 ASP   A O   1 
ATOM   1927 C CB  . ASP   A 1 258 ? -4.188  38.291 0.701   1.00 25.77 ? 280 ASP   A CB  1 
ATOM   1928 C CG  . ASP   A 1 258 ? -3.458  39.075 -0.388  1.00 26.20 ? 280 ASP   A CG  1 
ATOM   1929 O OD1 . ASP   A 1 258 ? -3.179  38.481 -1.448  1.00 25.16 ? 280 ASP   A OD1 1 
ATOM   1930 O OD2 . ASP   A 1 258 ? -3.158  40.277 -0.165  1.00 27.65 ? 280 ASP   A OD2 1 
ATOM   1931 N N   . ASN   A 1 259 ? -5.132  35.774 -1.732  1.00 26.00 ? 281 ASN   A N   1 
ATOM   1932 C CA  . ASN   A 1 259 ? -6.060  35.385 -2.788  1.00 25.69 ? 281 ASN   A CA  1 
ATOM   1933 C C   . ASN   A 1 259 ? -6.041  36.365 -3.966  1.00 26.09 ? 281 ASN   A C   1 
ATOM   1934 O O   . ASN   A 1 259 ? -6.954  36.324 -4.796  1.00 25.49 ? 281 ASN   A O   1 
ATOM   1935 C CB  . ASN   A 1 259 ? -7.490  35.224 -2.277  1.00 26.81 ? 281 ASN   A CB  1 
ATOM   1936 C CG  . ASN   A 1 259 ? -7.598  34.242 -1.135  1.00 26.93 ? 281 ASN   A CG  1 
ATOM   1937 O OD1 . ASN   A 1 259 ? -6.617  33.588 -0.763  1.00 27.79 ? 281 ASN   A OD1 1 
ATOM   1938 N ND2 . ASN   A 1 259 ? -8.792  34.103 -0.586  1.00 27.63 ? 281 ASN   A ND2 1 
ATOM   1939 N N   . LEU   A 1 260 ? -4.983  37.192 -4.057  1.00 25.06 ? 282 LEU   A N   1 
ATOM   1940 C CA  . LEU   A 1 260 ? -4.841  38.201 -5.099  1.00 24.71 ? 282 LEU   A CA  1 
ATOM   1941 C C   . LEU   A 1 260 ? -3.638  37.890 -5.982  1.00 23.48 ? 282 LEU   A C   1 
ATOM   1942 O O   . LEU   A 1 260 ? -2.662  37.286 -5.529  1.00 22.69 ? 282 LEU   A O   1 
ATOM   1943 C CB  . LEU   A 1 260 ? -4.648  39.581 -4.472  1.00 26.00 ? 282 LEU   A CB  1 
ATOM   1944 C CG  . LEU   A 1 260 ? -5.778  40.087 -3.569  1.00 26.90 ? 282 LEU   A CG  1 
ATOM   1945 C CD1 . LEU   A 1 260 ? -5.380  41.386 -2.883  1.00 26.81 ? 282 LEU   A CD1 1 
ATOM   1946 C CD2 . LEU   A 1 260 ? -7.064  40.272 -4.357  1.00 26.85 ? 282 LEU   A CD2 1 
ATOM   1947 N N   . VAL   A 1 261 ? -3.719  38.343 -7.240  1.00 22.39 ? 283 VAL   A N   1 
ATOM   1948 C CA  . VAL   A 1 261 ? -2.551  38.449 -8.100  1.00 22.95 ? 283 VAL   A CA  1 
ATOM   1949 C C   . VAL   A 1 261 ? -1.973  39.848 -7.909  1.00 22.90 ? 283 VAL   A C   1 
ATOM   1950 O O   . VAL   A 1 261 ? -2.702  40.830 -8.047  1.00 23.42 ? 283 VAL   A O   1 
ATOM   1951 C CB  . VAL   A 1 261 ? -2.843  38.217 -9.593  1.00 22.64 ? 283 VAL   A CB  1 
ATOM   1952 C CG1 . VAL   A 1 261 ? -1.585  38.389 -10.425 1.00 22.41 ? 283 VAL   A CG1 1 
ATOM   1953 C CG2 . VAL   A 1 261 ? -3.493  36.861 -9.861  1.00 23.22 ? 283 VAL   A CG2 1 
ATOM   1954 N N   . TYR   A 1 262 ? -0.671  39.919 -7.608  1.00 21.57 ? 284 TYR   A N   1 
ATOM   1955 C CA  . TYR   A 1 262 ? 0.024   41.192 -7.482  1.00 21.61 ? 284 TYR   A CA  1 
ATOM   1956 C C   . TYR   A 1 262 ? 0.848   41.467 -8.738  1.00 22.47 ? 284 TYR   A C   1 
ATOM   1957 O O   . TYR   A 1 262 ? 1.505   40.573 -9.281  1.00 21.20 ? 284 TYR   A O   1 
ATOM   1958 C CB  . TYR   A 1 262 ? 0.933   41.217 -6.249  1.00 22.34 ? 284 TYR   A CB  1 
ATOM   1959 C CG  . TYR   A 1 262 ? 0.199   41.493 -4.949  1.00 22.65 ? 284 TYR   A CG  1 
ATOM   1960 C CD1 . TYR   A 1 262 ? -0.659  40.545 -4.405  1.00 23.57 ? 284 TYR   A CD1 1 
ATOM   1961 C CD2 . TYR   A 1 262 ? 0.367   42.693 -4.260  1.00 24.30 ? 284 TYR   A CD2 1 
ATOM   1962 C CE1 . TYR   A 1 262 ? -1.338  40.790 -3.225  1.00 23.95 ? 284 TYR   A CE1 1 
ATOM   1963 C CE2 . TYR   A 1 262 ? -0.303  42.946 -3.074  1.00 24.53 ? 284 TYR   A CE2 1 
ATOM   1964 C CZ  . TYR   A 1 262 ? -1.157  41.988 -2.560  1.00 24.46 ? 284 TYR   A CZ  1 
ATOM   1965 O OH  . TYR   A 1 262 ? -1.852  42.200 -1.411  1.00 25.65 ? 284 TYR   A OH  1 
ATOM   1966 N N   . ILE   A 1 263 ? 0.829   42.741 -9.156  1.00 22.87 ? 285 ILE   A N   1 
ATOM   1967 C CA  . ILE   A 1 263 ? 1.662   43.220 -10.247 1.00 23.17 ? 285 ILE   A CA  1 
ATOM   1968 C C   . ILE   A 1 263 ? 2.403   44.470 -9.778  1.00 24.16 ? 285 ILE   A C   1 
ATOM   1969 O O   . ILE   A 1 263 ? 1.760   45.415 -9.300  1.00 25.21 ? 285 ILE   A O   1 
ATOM   1970 C CB  . ILE   A 1 263 ? 0.813   43.506 -11.498 1.00 23.09 ? 285 ILE   A CB  1 
ATOM   1971 C CG1 . ILE   A 1 263 ? -0.102  42.314 -11.831 1.00 23.72 ? 285 ILE   A CG1 1 
ATOM   1972 C CG2 . ILE   A 1 263 ? 1.708   43.896 -12.677 1.00 23.81 ? 285 ILE   A CG2 1 
ATOM   1973 C CD1 . ILE   A 1 263 ? -0.975  42.517 -13.052 1.00 24.29 ? 285 ILE   A CD1 1 
ATOM   1974 N N   . TRP   A 1 264 ? 3.742   44.441 -9.936  1.00 22.39 ? 286 TRP   A N   1 
ATOM   1975 C CA  . TRP   A 1 264 ? 4.617   45.554 -9.598  1.00 22.95 ? 286 TRP   A CA  1 
ATOM   1976 C C   . TRP   A 1 264 ? 5.289   46.088 -10.856 1.00 23.72 ? 286 TRP   A C   1 
ATOM   1977 O O   . TRP   A 1 264 ? 5.567   45.339 -11.792 1.00 23.34 ? 286 TRP   A O   1 
ATOM   1978 C CB  . TRP   A 1 264 ? 5.752   45.164 -8.640  1.00 22.94 ? 286 TRP   A CB  1 
ATOM   1979 C CG  . TRP   A 1 264 ? 5.383   44.691 -7.262  1.00 23.76 ? 286 TRP   A CG  1 
ATOM   1980 C CD1 . TRP   A 1 264 ? 5.388   45.421 -6.112  1.00 24.04 ? 286 TRP   A CD1 1 
ATOM   1981 C CD2 . TRP   A 1 264 ? 5.067   43.336 -6.878  1.00 22.77 ? 286 TRP   A CD2 1 
ATOM   1982 N NE1 . TRP   A 1 264 ? 5.056   44.625 -5.047  1.00 24.98 ? 286 TRP   A NE1 1 
ATOM   1983 C CE2 . TRP   A 1 264 ? 4.862   43.339 -5.486  1.00 23.41 ? 286 TRP   A CE2 1 
ATOM   1984 C CE3 . TRP   A 1 264 ? 4.931   42.133 -7.578  1.00 22.14 ? 286 TRP   A CE3 1 
ATOM   1985 C CZ2 . TRP   A 1 264 ? 4.520   42.183 -4.787  1.00 22.50 ? 286 TRP   A CZ2 1 
ATOM   1986 C CZ3 . TRP   A 1 264 ? 4.598   40.994 -6.889  1.00 22.21 ? 286 TRP   A CZ3 1 
ATOM   1987 C CH2 . TRP   A 1 264 ? 4.410   41.016 -5.507  1.00 22.37 ? 286 TRP   A CH2 1 
ATOM   1988 N N   . ASN   A 1 265 ? 5.644   47.373 -10.795 1.00 24.24 ? 287 ASN   A N   1 
ATOM   1989 C CA  . ASN   A 1 265 ? 6.587   47.965 -11.727 1.00 26.59 ? 287 ASN   A CA  1 
ATOM   1990 C C   . ASN   A 1 265 ? 7.993   47.484 -11.364 1.00 25.89 ? 287 ASN   A C   1 
ATOM   1991 O O   . ASN   A 1 265 ? 8.444   47.676 -10.239 1.00 26.80 ? 287 ASN   A O   1 
ATOM   1992 C CB  . ASN   A 1 265 ? 6.476   49.483 -11.690 1.00 28.77 ? 287 ASN   A CB  1 
ATOM   1993 C CG  . ASN   A 1 265 ? 7.403   50.169 -12.665 1.00 30.60 ? 287 ASN   A CG  1 
ATOM   1994 O OD1 . ASN   A 1 265 ? 8.608   49.888 -12.691 1.00 29.78 ? 287 ASN   A OD1 1 
ATOM   1995 N ND2 . ASN   A 1 265 ? 6.867   51.077 -13.466 1.00 33.16 ? 287 ASN   A ND2 1 
ATOM   1996 N N   . LEU   A 1 266 ? 8.684   46.852 -12.317 1.00 25.27 ? 288 LEU   A N   1 
ATOM   1997 C CA  . LEU   A 1 266 ? 9.954   46.200 -12.028 1.00 26.48 ? 288 LEU   A CA  1 
ATOM   1998 C C   . LEU   A 1 266 ? 10.977  47.224 -11.524 1.00 28.00 ? 288 LEU   A C   1 
ATOM   1999 O O   . LEU   A 1 266 ? 11.694  46.970 -10.558 1.00 29.11 ? 288 LEU   A O   1 
ATOM   2000 C CB  . LEU   A 1 266 ? 10.418  45.469 -13.291 1.00 26.96 ? 288 LEU   A CB  1 
ATOM   2001 C CG  . LEU   A 1 266 ? 11.685  44.612 -13.168 1.00 26.50 ? 288 LEU   A CG  1 
ATOM   2002 C CD1 . LEU   A 1 266 ? 11.666  43.494 -14.194 1.00 26.27 ? 288 LEU   A CD1 1 
ATOM   2003 C CD2 . LEU   A 1 266 ? 12.937  45.437 -13.365 1.00 26.87 ? 288 LEU   A CD2 1 
ATOM   2004 N N   . GLN   A 1 267 ? 11.053  48.378 -12.192 1.00 29.01 ? 289 GLN   A N   1 
ATOM   2005 C CA  . GLN   A 1 267 ? 12.061  49.376 -11.859 1.00 30.56 ? 289 GLN   A CA  1 
ATOM   2006 C C   . GLN   A 1 267 ? 11.700  50.146 -10.589 1.00 30.71 ? 289 GLN   A C   1 
ATOM   2007 O O   . GLN   A 1 267 ? 12.577  50.404 -9.763  1.00 31.15 ? 289 GLN   A O   1 
ATOM   2008 C CB  . GLN   A 1 267 ? 12.303  50.344 -13.022 1.00 33.36 ? 289 GLN   A CB  1 
ATOM   2009 C CG  . GLN   A 1 267 ? 12.926  49.699 -14.256 1.00 35.74 ? 289 GLN   A CG  1 
ATOM   2010 C CD  . GLN   A 1 267 ? 14.256  49.012 -14.010 1.00 35.87 ? 289 GLN   A CD  1 
ATOM   2011 O OE1 . GLN   A 1 267 ? 14.931  49.220 -12.994 1.00 36.73 ? 289 GLN   A OE1 1 
ATOM   2012 N NE2 . GLN   A 1 267 ? 14.660  48.185 -14.966 1.00 35.48 ? 289 GLN   A NE2 1 
ATOM   2013 N N   . THR   A 1 268 ? 10.429  50.540 -10.426 1.00 30.81 ? 290 THR   A N   1 
ATOM   2014 C CA  . THR   A 1 268 ? 10.089  51.457 -9.345  1.00 34.25 ? 290 THR   A CA  1 
ATOM   2015 C C   . THR   A 1 268 ? 9.674   50.699 -8.091  1.00 32.18 ? 290 THR   A C   1 
ATOM   2016 O O   . THR   A 1 268 ? 9.751   51.265 -7.000  1.00 32.58 ? 290 THR   A O   1 
ATOM   2017 C CB  . THR   A 1 268 ? 9.005   52.457 -9.753  1.00 34.74 ? 290 THR   A CB  1 
ATOM   2018 O OG1 . THR   A 1 268 ? 7.785   51.724 -9.838  1.00 34.46 ? 290 THR   A OG1 1 
ATOM   2019 C CG2 . THR   A 1 268 ? 9.348   53.174 -11.047 1.00 35.42 ? 290 THR   A CG2 1 
ATOM   2020 N N   . LYS   A 1 269 ? 9.199   49.459 -8.265  1.00 31.80 ? 291 LYS   A N   1 
ATOM   2021 C CA  . LYS   A 1 269 ? 8.820   48.580 -7.166  1.00 33.26 ? 291 LYS   A CA  1 
ATOM   2022 C C   . LYS   A 1 269 ? 7.416   48.905 -6.641  1.00 32.97 ? 291 LYS   A C   1 
ATOM   2023 O O   . LYS   A 1 269 ? 6.966   48.286 -5.676  1.00 32.58 ? 291 LYS   A O   1 
ATOM   2024 C CB  . LYS   A 1 269 ? 9.869   48.574 -6.046  1.00 35.04 ? 291 LYS   A CB  1 
ATOM   2025 C CG  . LYS   A 1 269 ? 11.272  48.224 -6.540  1.00 38.03 ? 291 LYS   A CG  1 
ATOM   2026 C CD  . LYS   A 1 269 ? 12.390  48.569 -5.571  1.00 39.61 ? 291 LYS   A CD  1 
ATOM   2027 C CE  . LYS   A 1 269 ? 12.530  50.047 -5.426  1.00 41.41 ? 291 LYS   A CE  1 
ATOM   2028 N NZ  . LYS   A 1 269 ? 13.429  50.361 -4.320  1.00 42.88 ? 291 LYS   A NZ  1 
ATOM   2029 N N   . GLU   A 1 270 ? 6.698   49.835 -7.287  1.00 31.93 ? 292 GLU   A N   1 
ATOM   2030 C CA  . GLU   A 1 270 ? 5.348   50.157 -6.848  1.00 33.15 ? 292 GLU   A CA  1 
ATOM   2031 C C   . GLU   A 1 270 ? 4.392   49.082 -7.354  1.00 29.91 ? 292 GLU   A C   1 
ATOM   2032 O O   . GLU   A 1 270 ? 4.518   48.635 -8.491  1.00 27.80 ? 292 GLU   A O   1 
ATOM   2033 C CB  . GLU   A 1 270 ? 4.705   51.418 -7.420  1.00 37.72 ? 292 GLU   A CB  1 
ATOM   2034 C CG  . GLU   A 1 270 ? 5.599   52.647 -7.520  1.00 43.55 ? 292 GLU   A CG  1 
ATOM   2035 C CD  . GLU   A 1 270 ? 4.976   53.520 -8.596  1.00 49.50 ? 292 GLU   A CD  1 
ATOM   2036 O OE1 . GLU   A 1 270 ? 3.827   53.978 -8.359  1.00 52.55 ? 292 GLU   A OE1 1 
ATOM   2037 O OE2 . GLU   A 1 270 ? 5.587   53.665 -9.690  1.00 53.68 ? 292 GLU   A OE2 1 
ATOM   2038 N N   . ILE   A 1 271 ? 3.420   48.721 -6.509  1.00 28.56 ? 293 ILE   A N   1 
ATOM   2039 C CA  . ILE   A 1 271 ? 2.293   47.904 -6.916  1.00 29.22 ? 293 ILE   A CA  1 
ATOM   2040 C C   . ILE   A 1 271 ? 1.484   48.713 -7.921  1.00 28.88 ? 293 ILE   A C   1 
ATOM   2041 O O   . ILE   A 1 271 ? 1.129   49.860 -7.657  1.00 30.46 ? 293 ILE   A O   1 
ATOM   2042 C CB  . ILE   A 1 271 ? 1.431   47.487 -5.709  1.00 29.87 ? 293 ILE   A CB  1 
ATOM   2043 C CG1 . ILE   A 1 271 ? 2.206   46.590 -4.735  1.00 31.88 ? 293 ILE   A CG1 1 
ATOM   2044 C CG2 . ILE   A 1 271 ? 0.136   46.821 -6.173  1.00 30.12 ? 293 ILE   A CG2 1 
ATOM   2045 C CD1 . ILE   A 1 271 ? 1.598   46.508 -3.347  1.00 33.61 ? 293 ILE   A CD1 1 
ATOM   2046 N N   . VAL   A 1 272 ? 1.205   48.108 -9.074  1.00 28.64 ? 294 VAL   A N   1 
ATOM   2047 C CA  . VAL   A 1 272 ? 0.469   48.803 -10.118 1.00 28.39 ? 294 VAL   A CA  1 
ATOM   2048 C C   . VAL   A 1 272 ? -0.900  48.164 -10.333 1.00 28.42 ? 294 VAL   A C   1 
ATOM   2049 O O   . VAL   A 1 272 ? -1.785  48.800 -10.896 1.00 29.04 ? 294 VAL   A O   1 
ATOM   2050 C CB  . VAL   A 1 272 ? 1.283   48.875 -11.420 1.00 29.51 ? 294 VAL   A CB  1 
ATOM   2051 C CG1 . VAL   A 1 272 ? 2.464   49.824 -11.257 1.00 30.58 ? 294 VAL   A CG1 1 
ATOM   2052 C CG2 . VAL   A 1 272 ? 1.752   47.506 -11.903 1.00 29.00 ? 294 VAL   A CG2 1 
ATOM   2053 N N   . GLN   A 1 273 ? -1.083  46.917 -9.896  1.00 26.61 ? 295 GLN   A N   1 
ATOM   2054 C CA  . GLN   A 1 273 ? -2.392  46.299 -9.978  1.00 27.91 ? 295 GLN   A CA  1 
ATOM   2055 C C   . GLN   A 1 273 ? -2.465  45.104 -9.036  1.00 26.79 ? 295 GLN   A C   1 
ATOM   2056 O O   . GLN   A 1 273 ? -1.469  44.423 -8.824  1.00 26.51 ? 295 GLN   A O   1 
ATOM   2057 C CB  . GLN   A 1 273 ? -2.718  45.850 -11.404 1.00 28.47 ? 295 GLN   A CB  1 
ATOM   2058 C CG  . GLN   A 1 273 ? -4.192  46.001 -11.745 1.00 29.34 ? 295 GLN   A CG  1 
ATOM   2059 C CD  . GLN   A 1 273 ? -4.590  45.502 -13.123 1.00 26.90 ? 295 GLN   A CD  1 
ATOM   2060 O OE1 . GLN   A 1 273 ? -3.779  45.228 -14.020 1.00 24.32 ? 295 GLN   A OE1 1 
ATOM   2061 N NE2 . GLN   A 1 273 ? -5.893  45.365 -13.293 1.00 27.03 ? 295 GLN   A NE2 1 
ATOM   2062 N N   . LYS   A 1 274 ? -3.670  44.886 -8.496  1.00 27.55 ? 296 LYS   A N   1 
ATOM   2063 C CA  . LYS   A 1 274 ? -4.003  43.718 -7.701  1.00 28.11 ? 296 LYS   A CA  1 
ATOM   2064 C C   . LYS   A 1 274 ? -5.254  43.102 -8.320  1.00 28.48 ? 296 LYS   A C   1 
ATOM   2065 O O   . LYS   A 1 274 ? -6.263  43.788 -8.441  1.00 32.64 ? 296 LYS   A O   1 
ATOM   2066 C CB  . LYS   A 1 274 ? -4.212  44.118 -6.235  1.00 28.96 ? 296 LYS   A CB  1 
ATOM   2067 C CG  . LYS   A 1 274 ? -2.901  44.420 -5.497  1.00 30.29 ? 296 LYS   A CG  1 
ATOM   2068 C CD  . LYS   A 1 274 ? -2.964  45.384 -4.311  1.00 33.39 ? 296 LYS   A CD  1 
ATOM   2069 C CE  . LYS   A 1 274 ? -3.813  44.891 -3.201  1.00 36.38 ? 296 LYS   A CE  1 
ATOM   2070 N NZ  . LYS   A 1 274 ? -3.735  45.779 -2.032  1.00 38.00 ? 296 LYS   A NZ  1 
ATOM   2071 N N   . LEU   A 1 275 ? -5.178  41.826 -8.720  1.00 25.61 ? 297 LEU   A N   1 
ATOM   2072 C CA  . LEU   A 1 275 ? -6.300  41.191 -9.402  1.00 26.15 ? 297 LEU   A CA  1 
ATOM   2073 C C   . LEU   A 1 275 ? -7.123  40.378 -8.405  1.00 26.12 ? 297 LEU   A C   1 
ATOM   2074 O O   . LEU   A 1 275 ? -6.627  39.413 -7.830  1.00 24.23 ? 297 LEU   A O   1 
ATOM   2075 C CB  . LEU   A 1 275 ? -5.825  40.310 -10.550 1.00 25.20 ? 297 LEU   A CB  1 
ATOM   2076 C CG  . LEU   A 1 275 ? -4.756  40.912 -11.469 1.00 26.65 ? 297 LEU   A CG  1 
ATOM   2077 C CD1 . LEU   A 1 275 ? -4.459  39.955 -12.606 1.00 26.70 ? 297 LEU   A CD1 1 
ATOM   2078 C CD2 . LEU   A 1 275 ? -5.156  42.268 -12.011 1.00 27.51 ? 297 LEU   A CD2 1 
ATOM   2079 N N   . GLN   A 1 276 ? -8.396  40.757 -8.252  1.00 26.46 ? 298 GLN   A N   1 
ATOM   2080 C CA  . GLN   A 1 276 ? -9.283  40.105 -7.301  1.00 28.82 ? 298 GLN   A CA  1 
ATOM   2081 C C   . GLN   A 1 276 ? -10.220 39.149 -8.050  1.00 27.25 ? 298 GLN   A C   1 
ATOM   2082 O O   . GLN   A 1 276 ? -10.648 39.439 -9.176  1.00 25.91 ? 298 GLN   A O   1 
ATOM   2083 C CB  . GLN   A 1 276 ? -9.980  41.214 -6.503  1.00 32.72 ? 298 GLN   A CB  1 
ATOM   2084 C CG  . GLN   A 1 276 ? -11.191 41.815 -7.198  1.00 38.35 ? 298 GLN   A CG  1 
ATOM   2085 C CD  . GLN   A 1 276 ? -12.437 40.985 -6.984  1.00 46.50 ? 298 GLN   A CD  1 
ATOM   2086 O OE1 . GLN   A 1 276 ? -12.470 40.093 -6.122  1.00 52.54 ? 298 GLN   A OE1 1 
ATOM   2087 N NE2 . GLN   A 1 276 ? -13.472 41.279 -7.763  1.00 51.75 ? 298 GLN   A NE2 1 
ATOM   2088 N N   . GLY   A 1 277 ? -10.549 38.019 -7.402  1.00 26.33 ? 299 GLY   A N   1 
ATOM   2089 C CA  . GLY   A 1 277 ? -11.508 37.063 -7.937  1.00 26.26 ? 299 GLY   A CA  1 
ATOM   2090 C C   . GLY   A 1 277 ? -11.344 35.667 -7.338  1.00 25.84 ? 299 GLY   A C   1 
ATOM   2091 O O   . GLY   A 1 277 ? -12.336 34.998 -7.069  1.00 25.98 ? 299 GLY   A O   1 
ATOM   2092 N N   . HIS   A 1 278 ? -10.089 35.217 -7.162  1.00 25.64 ? 300 HIS   A N   1 
ATOM   2093 C CA  . HIS   A 1 278 ? -9.838  33.904 -6.580  1.00 23.86 ? 300 HIS   A CA  1 
ATOM   2094 C C   . HIS   A 1 278 ? -10.360 33.853 -5.141  1.00 23.97 ? 300 HIS   A C   1 
ATOM   2095 O O   . HIS   A 1 278 ? -10.418 34.881 -4.467  1.00 24.00 ? 300 HIS   A O   1 
ATOM   2096 C CB  . HIS   A 1 278 ? -8.358  33.508 -6.676  1.00 22.78 ? 300 HIS   A CB  1 
ATOM   2097 C CG  . HIS   A 1 278 ? -7.931  33.096 -8.057  1.00 22.17 ? 300 HIS   A CG  1 
ATOM   2098 N ND1 . HIS   A 1 278 ? -8.369  31.925 -8.637  1.00 21.03 ? 300 HIS   A ND1 1 
ATOM   2099 C CD2 . HIS   A 1 278 ? -7.112  33.669 -8.954  1.00 21.26 ? 300 HIS   A CD2 1 
ATOM   2100 C CE1 . HIS   A 1 278 ? -7.821  31.809 -9.843  1.00 21.81 ? 300 HIS   A CE1 1 
ATOM   2101 N NE2 . HIS   A 1 278 ? -7.042  32.853 -10.046 1.00 21.51 ? 300 HIS   A NE2 1 
ATOM   2102 N N   . THR   A 1 279 ? -10.712 32.643 -4.683  1.00 23.21 ? 301 THR   A N   1 
ATOM   2103 C CA  . THR   A 1 279 ? -11.231 32.442 -3.337  1.00 23.16 ? 301 THR   A CA  1 
ATOM   2104 C C   . THR   A 1 279 ? -10.309 31.523 -2.526  1.00 22.60 ? 301 THR   A C   1 
ATOM   2105 O O   . THR   A 1 279 ? -10.694 31.010 -1.471  1.00 23.47 ? 301 THR   A O   1 
ATOM   2106 C CB  . THR   A 1 279 ? -12.658 31.911 -3.409  1.00 24.52 ? 301 THR   A CB  1 
ATOM   2107 O OG1 . THR   A 1 279 ? -12.580 30.667 -4.099  1.00 24.66 ? 301 THR   A OG1 1 
ATOM   2108 C CG2 . THR   A 1 279 ? -13.589 32.890 -4.106  1.00 25.57 ? 301 THR   A CG2 1 
ATOM   2109 N N   . ASP   A 1 280 ? -9.063  31.380 -2.976  1.00 22.28 ? 302 ASP   A N   1 
ATOM   2110 C CA  . ASP   A 1 280 ? -8.040  30.742 -2.167  1.00 21.36 ? 302 ASP   A CA  1 
ATOM   2111 C C   . ASP   A 1 280 ? -6.691  31.283 -2.616  1.00 22.19 ? 302 ASP   A C   1 
ATOM   2112 O O   . ASP   A 1 280 ? -6.607  32.097 -3.534  1.00 22.80 ? 302 ASP   A O   1 
ATOM   2113 C CB  . ASP   A 1 280 ? -8.144  29.222 -2.227  1.00 22.74 ? 302 ASP   A CB  1 
ATOM   2114 C CG  . ASP   A 1 280 ? -7.624  28.440 -1.024  1.00 21.60 ? 302 ASP   A CG  1 
ATOM   2115 O OD1 . ASP   A 1 280 ? -6.873  29.018 -0.211  1.00 21.01 ? 302 ASP   A OD1 1 
ATOM   2116 O OD2 . ASP   A 1 280 ? -8.007  27.252 -0.889  1.00 22.92 ? 302 ASP   A OD2 1 
ATOM   2117 N N   . VAL   A 1 281 ? -5.639  30.804 -1.958  1.00 22.53 ? 303 VAL   A N   1 
ATOM   2118 C CA  . VAL   A 1 281 ? -4.280  31.238 -2.241  1.00 21.96 ? 303 VAL   A CA  1 
ATOM   2119 C C   . VAL   A 1 281 ? -4.024  31.114 -3.739  1.00 21.00 ? 303 VAL   A C   1 
ATOM   2120 O O   . VAL   A 1 281 ? -4.285  30.076 -4.337  1.00 21.04 ? 303 VAL   A O   1 
ATOM   2121 C CB  . VAL   A 1 281 ? -3.267  30.401 -1.441  1.00 22.50 ? 303 VAL   A CB  1 
ATOM   2122 C CG1 . VAL   A 1 281 ? -1.828  30.668 -1.860  1.00 22.90 ? 303 VAL   A CG1 1 
ATOM   2123 C CG2 . VAL   A 1 281 ? -3.440  30.571 0.071   1.00 23.30 ? 303 VAL   A CG2 1 
ATOM   2124 N N   . VAL   A 1 282 ? -3.455  32.170 -4.315  1.00 20.65 ? 304 VAL   A N   1 
ATOM   2125 C CA  . VAL   A 1 282 ? -3.057  32.141 -5.704  1.00 19.67 ? 304 VAL   A CA  1 
ATOM   2126 C C   . VAL   A 1 282 ? -1.640  31.590 -5.744  1.00 20.14 ? 304 VAL   A C   1 
ATOM   2127 O O   . VAL   A 1 282 ? -0.667  32.303 -5.472  1.00 21.07 ? 304 VAL   A O   1 
ATOM   2128 C CB  . VAL   A 1 282 ? -3.174  33.509 -6.388  1.00 19.90 ? 304 VAL   A CB  1 
ATOM   2129 C CG1 . VAL   A 1 282 ? -2.741  33.432 -7.848  1.00 20.46 ? 304 VAL   A CG1 1 
ATOM   2130 C CG2 . VAL   A 1 282 ? -4.603  34.043 -6.267  1.00 19.36 ? 304 VAL   A CG2 1 
ATOM   2131 N N   . ILE   A 1 283 ? -1.562  30.294 -6.035  1.00 18.71 ? 305 ILE   A N   1 
ATOM   2132 C CA  . ILE   A 1 283 ? -0.332  29.544 -5.869  1.00 19.02 ? 305 ILE   A CA  1 
ATOM   2133 C C   . ILE   A 1 283 ? 0.558   29.742 -7.095  1.00 18.37 ? 305 ILE   A C   1 
ATOM   2134 O O   . ILE   A 1 283 ? 1.772   29.565 -7.010  1.00 19.16 ? 305 ILE   A O   1 
ATOM   2135 C CB  . ILE   A 1 283 ? -0.642  28.059 -5.615  1.00 19.30 ? 305 ILE   A CB  1 
ATOM   2136 C CG1 . ILE   A 1 283 ? 0.580   27.286 -5.149  1.00 20.16 ? 305 ILE   A CG1 1 
ATOM   2137 C CG2 . ILE   A 1 283 ? -1.266  27.400 -6.844  1.00 18.76 ? 305 ILE   A CG2 1 
ATOM   2138 C CD1 . ILE   A 1 283 ? 1.065   27.669 -3.770  1.00 21.12 ? 305 ILE   A CD1 1 
ATOM   2139 N N   . SER   A 1 284 ? -0.059  30.071 -8.239  1.00 17.87 ? 306 SER   A N   1 
ATOM   2140 C CA  . SER   A 1 284 ? 0.644   30.079 -9.510  1.00 17.44 ? 306 SER   A CA  1 
ATOM   2141 C C   . SER   A 1 284 ? 0.103   31.193 -10.405 1.00 17.51 ? 306 SER   A C   1 
ATOM   2142 O O   . SER   A 1 284 ? -1.100  31.424 -10.481 1.00 17.56 ? 306 SER   A O   1 
ATOM   2143 C CB  . SER   A 1 284 ? 0.534   28.717 -10.192 1.00 17.81 ? 306 SER   A CB  1 
ATOM   2144 O OG  . SER   A 1 284 ? 1.132   28.748 -11.486 1.00 17.18 ? 306 SER   A OG  1 
ATOM   2145 N N   . THR   A 1 285 ? 1.034   31.896 -11.047 1.00 17.09 ? 307 THR   A N   1 
ATOM   2146 C CA  . THR   A 1 285 ? 0.753   32.834 -12.112 1.00 17.55 ? 307 THR   A CA  1 
ATOM   2147 C C   . THR   A 1 285 ? 1.713   32.502 -13.247 1.00 17.37 ? 307 THR   A C   1 
ATOM   2148 O O   . THR   A 1 285 ? 2.787   31.947 -13.014 1.00 17.81 ? 307 THR   A O   1 
ATOM   2149 C CB  . THR   A 1 285 ? 0.932   34.275 -11.631 1.00 19.49 ? 307 THR   A CB  1 
ATOM   2150 O OG1 . THR   A 1 285 ? 2.248   34.332 -11.082 1.00 20.32 ? 307 THR   A OG1 1 
ATOM   2151 C CG2 . THR   A 1 285 ? -0.096  34.676 -10.586 1.00 20.50 ? 307 THR   A CG2 1 
ATOM   2152 N N   . ALA   A 1 286 ? 1.286   32.819 -14.463 1.00 16.64 ? 308 ALA   A N   1 
ATOM   2153 C CA  . ALA   A 1 286 ? 2.117   32.713 -15.645 1.00 17.30 ? 308 ALA   A CA  1 
ATOM   2154 C C   . ALA   A 1 286 ? 1.782   33.867 -16.581 1.00 17.19 ? 308 ALA   A C   1 
ATOM   2155 O O   . ALA   A 1 286 ? 0.628   34.318 -16.642 1.00 17.64 ? 308 ALA   A O   1 
ATOM   2156 C CB  . ALA   A 1 286 ? 1.916   31.390 -16.334 1.00 16.98 ? 308 ALA   A CB  1 
ATOM   2157 N N   . CYS   A 1 287 ? 2.801   34.296 -17.325 1.00 17.40 ? 309 CYS   A N   1 
ATOM   2158 C CA  . CYS   A 1 287 ? 2.693   35.400 -18.270 1.00 18.25 ? 309 CYS   A CA  1 
ATOM   2159 C C   . CYS   A 1 287 ? 2.848   34.866 -19.687 1.00 17.76 ? 309 CYS   A C   1 
ATOM   2160 O O   . CYS   A 1 287 ? 3.796   34.146 -19.994 1.00 18.43 ? 309 CYS   A O   1 
ATOM   2161 C CB  . CYS   A 1 287 ? 3.740   36.468 -17.990 1.00 19.13 ? 309 CYS   A CB  1 
ATOM   2162 S SG  . CYS   A 1 287 ? 3.478   37.275 -16.394 1.00 20.74 ? 309 CYS   A SG  1 
ATOM   2163 N N   . HIS   A 1 288 ? 1.890   35.232 -20.540 1.00 17.60 ? 310 HIS   A N   1 
ATOM   2164 C CA  . HIS   A 1 288 ? 1.861   34.779 -21.923 1.00 17.46 ? 310 HIS   A CA  1 
ATOM   2165 C C   . HIS   A 1 288 ? 3.107   35.273 -22.666 1.00 18.08 ? 310 HIS   A C   1 
ATOM   2166 O O   . HIS   A 1 288 ? 3.548   36.397 -22.442 1.00 19.78 ? 310 HIS   A O   1 
ATOM   2167 C CB  . HIS   A 1 288 ? 0.567   35.261 -22.580 1.00 17.04 ? 310 HIS   A CB  1 
ATOM   2168 C CG  . HIS   A 1 288 ? 0.326   34.646 -23.903 1.00 17.11 ? 310 HIS   A CG  1 
ATOM   2169 N ND1 . HIS   A 1 288 ? 0.875   35.095 -25.086 1.00 16.94 ? 310 HIS   A ND1 1 
ATOM   2170 C CD2 . HIS   A 1 288 ? -0.405  33.566 -24.208 1.00 16.45 ? 310 HIS   A CD2 1 
ATOM   2171 C CE1 . HIS   A 1 288 ? 0.477   34.299 -26.070 1.00 16.57 ? 310 HIS   A CE1 1 
ATOM   2172 N NE2 . HIS   A 1 288 ? -0.295  33.361 -25.563 1.00 16.50 ? 310 HIS   A NE2 1 
ATOM   2173 N N   . PRO   A 1 289 ? 3.706   34.472 -23.584 1.00 18.24 ? 311 PRO   A N   1 
ATOM   2174 C CA  . PRO   A 1 289 ? 4.939   34.870 -24.265 1.00 18.39 ? 311 PRO   A CA  1 
ATOM   2175 C C   . PRO   A 1 289 ? 4.837   36.063 -25.216 1.00 19.16 ? 311 PRO   A C   1 
ATOM   2176 O O   . PRO   A 1 289 ? 5.848   36.726 -25.414 1.00 21.72 ? 311 PRO   A O   1 
ATOM   2177 C CB  . PRO   A 1 289 ? 5.376   33.600 -25.006 1.00 18.27 ? 311 PRO   A CB  1 
ATOM   2178 C CG  . PRO   A 1 289 ? 4.075   32.830 -25.211 1.00 17.96 ? 311 PRO   A CG  1 
ATOM   2179 C CD  . PRO   A 1 289 ? 3.276   33.122 -23.966 1.00 17.82 ? 311 PRO   A CD  1 
ATOM   2180 N N   . THR   A 1 290 ? 3.649   36.357 -25.782 1.00 18.83 ? 312 THR   A N   1 
ATOM   2181 C CA  . THR   A 1 290 ? 3.539   37.436 -26.768 1.00 19.17 ? 312 THR   A CA  1 
ATOM   2182 C C   . THR   A 1 290 ? 2.418   38.433 -26.465 1.00 19.09 ? 312 THR   A C   1 
ATOM   2183 O O   . THR   A 1 290 ? 2.529   39.597 -26.840 1.00 20.28 ? 312 THR   A O   1 
ATOM   2184 C CB  . THR   A 1 290 ? 3.390   36.885 -28.190 1.00 18.97 ? 312 THR   A CB  1 
ATOM   2185 O OG1 . THR   A 1 290 ? 2.162   36.175 -28.331 1.00 18.42 ? 312 THR   A OG1 1 
ATOM   2186 C CG2 . THR   A 1 290 ? 4.536   35.974 -28.582 1.00 19.75 ? 312 THR   A CG2 1 
ATOM   2187 N N   . GLU   A 1 291 ? 1.333   38.003 -25.819 1.00 20.74 ? 313 GLU   A N   1 
ATOM   2188 C CA  . GLU   A 1 291 ? 0.225   38.885 -25.499 1.00 21.41 ? 313 GLU   A CA  1 
ATOM   2189 C C   . GLU   A 1 291 ? 0.257   39.244 -24.017 1.00 21.25 ? 313 GLU   A C   1 
ATOM   2190 O O   . GLU   A 1 291 ? 0.810   38.497 -23.208 1.00 19.67 ? 313 GLU   A O   1 
ATOM   2191 C CB  . GLU   A 1 291 ? -1.096  38.175 -25.782 1.00 23.06 ? 313 GLU   A CB  1 
ATOM   2192 C CG  . GLU   A 1 291 ? -1.340  37.918 -27.261 1.00 24.32 ? 313 GLU   A CG  1 
ATOM   2193 C CD  . GLU   A 1 291 ? -1.548  39.206 -28.038 1.00 26.53 ? 313 GLU   A CD  1 
ATOM   2194 O OE1 . GLU   A 1 291 ? -2.474  40.008 -27.717 1.00 29.43 ? 313 GLU   A OE1 1 
ATOM   2195 O OE2 . GLU   A 1 291 ? -0.768  39.390 -28.969 1.00 25.79 ? 313 GLU   A OE2 1 
ATOM   2196 N N   . ASN   A 1 292 ? -0.386  40.365 -23.676 1.00 21.51 ? 314 ASN   A N   1 
ATOM   2197 C CA  . ASN   A 1 292 ? -0.541  40.793 -22.290 1.00 21.64 ? 314 ASN   A CA  1 
ATOM   2198 C C   . ASN   A 1 292 ? -1.659  39.984 -21.633 1.00 21.01 ? 314 ASN   A C   1 
ATOM   2199 O O   . ASN   A 1 292 ? -2.770  40.489 -21.403 1.00 21.19 ? 314 ASN   A O   1 
ATOM   2200 C CB  . ASN   A 1 292 ? -0.840  42.286 -22.190 1.00 22.85 ? 314 ASN   A CB  1 
ATOM   2201 C CG  . ASN   A 1 292 ? 0.186   43.138 -22.901 1.00 22.98 ? 314 ASN   A CG  1 
ATOM   2202 O OD1 . ASN   A 1 292 ? 1.392   42.876 -22.829 1.00 24.71 ? 314 ASN   A OD1 1 
ATOM   2203 N ND2 . ASN   A 1 292 ? -0.269  44.163 -23.601 1.00 23.35 ? 314 ASN   A ND2 1 
ATOM   2204 N N   . ILE   A 1 293 ? -1.343  38.711 -21.361 1.00 19.12 ? 315 ILE   A N   1 
ATOM   2205 C CA  . ILE   A 1 293 ? -2.276  37.770 -20.757 1.00 19.85 ? 315 ILE   A CA  1 
ATOM   2206 C C   . ILE   A 1 293 ? -1.583  37.114 -19.565 1.00 19.17 ? 315 ILE   A C   1 
ATOM   2207 O O   . ILE   A 1 293 ? -0.439  36.663 -19.675 1.00 18.97 ? 315 ILE   A O   1 
ATOM   2208 C CB  . ILE   A 1 293 ? -2.751  36.721 -21.782 1.00 19.53 ? 315 ILE   A CB  1 
ATOM   2209 C CG1 . ILE   A 1 293 ? -3.568  37.364 -22.900 1.00 19.66 ? 315 ILE   A CG1 1 
ATOM   2210 C CG2 . ILE   A 1 293 ? -3.520  35.582 -21.114 1.00 20.11 ? 315 ILE   A CG2 1 
ATOM   2211 C CD1 . ILE   A 1 293 ? -3.910  36.438 -24.055 1.00 19.30 ? 315 ILE   A CD1 1 
ATOM   2212 N N   . ILE   A 1 294 ? -2.287  37.114 -18.425 1.00 19.06 ? 316 ILE   A N   1 
ATOM   2213 C CA  . ILE   A 1 294 ? -1.883  36.384 -17.240 1.00 17.75 ? 316 ILE   A CA  1 
ATOM   2214 C C   . ILE   A 1 294 ? -2.866  35.241 -17.016 1.00 18.19 ? 316 ILE   A C   1 
ATOM   2215 O O   . ILE   A 1 294 ? -4.078  35.415 -17.169 1.00 19.47 ? 316 ILE   A O   1 
ATOM   2216 C CB  . ILE   A 1 294 ? -1.819  37.313 -16.013 1.00 18.25 ? 316 ILE   A CB  1 
ATOM   2217 C CG1 . ILE   A 1 294 ? -0.711  38.349 -16.182 1.00 19.26 ? 316 ILE   A CG1 1 
ATOM   2218 C CG2 . ILE   A 1 294 ? -1.646  36.522 -14.713 1.00 18.09 ? 316 ILE   A CG2 1 
ATOM   2219 C CD1 . ILE   A 1 294 ? -0.750  39.458 -15.144 1.00 20.30 ? 316 ILE   A CD1 1 
ATOM   2220 N N   . ALA   A 1 295 ? -2.308  34.082 -16.646 1.00 18.24 ? 317 ALA   A N   1 
ATOM   2221 C CA  . ALA   A 1 295 ? -3.060  33.001 -16.041 1.00 18.39 ? 317 ALA   A CA  1 
ATOM   2222 C C   . ALA   A 1 295 ? -2.709  32.934 -14.562 1.00 18.23 ? 317 ALA   A C   1 
ATOM   2223 O O   . ALA   A 1 295 ? -1.535  33.017 -14.198 1.00 18.01 ? 317 ALA   A O   1 
ATOM   2224 C CB  . ALA   A 1 295 ? -2.744  31.687 -16.696 1.00 17.99 ? 317 ALA   A CB  1 
ATOM   2225 N N   . SER   A 1 296 ? -3.743  32.714 -13.744 1.00 18.26 ? 318 SER   A N   1 
ATOM   2226 C CA  . SER   A 1 296 ? -3.583  32.510 -12.316 1.00 18.04 ? 318 SER   A CA  1 
ATOM   2227 C C   . SER   A 1 296 ? -4.332  31.245 -11.903 1.00 18.12 ? 318 SER   A C   1 
ATOM   2228 O O   . SER   A 1 296 ? -5.272  30.828 -12.570 1.00 18.74 ? 318 SER   A O   1 
ATOM   2229 C CB  . SER   A 1 296 ? -4.063  33.717 -11.546 1.00 18.56 ? 318 SER   A CB  1 
ATOM   2230 O OG  . SER   A 1 296 ? -5.425  34.003 -11.844 1.00 18.62 ? 318 SER   A OG  1 
ATOM   2231 N N   . ALA   A 1 297 ? -3.894  30.629 -10.805 1.00 17.73 ? 319 ALA   A N   1 
ATOM   2232 C CA  . ALA   A 1 297 ? -4.518  29.409 -10.329 1.00 18.21 ? 319 ALA   A CA  1 
ATOM   2233 C C   . ALA   A 1 297 ? -4.464  29.367 -8.805  1.00 18.88 ? 319 ALA   A C   1 
ATOM   2234 O O   . ALA   A 1 297 ? -3.542  29.901 -8.188  1.00 18.96 ? 319 ALA   A O   1 
ATOM   2235 C CB  . ALA   A 1 297 ? -3.829  28.226 -10.961 1.00 18.97 ? 319 ALA   A CB  1 
ATOM   2236 N N   . ALA   A 1 298 ? -5.463  28.715 -8.205  1.00 19.73 ? 320 ALA   A N   1 
ATOM   2237 C CA  . ALA   A 1 298 ? -5.650  28.783 -6.760  1.00 20.59 ? 320 ALA   A CA  1 
ATOM   2238 C C   . ALA   A 1 298 ? -5.882  27.413 -6.125  1.00 20.92 ? 320 ALA   A C   1 
ATOM   2239 O O   . ALA   A 1 298 ? -6.166  26.419 -6.795  1.00 19.68 ? 320 ALA   A O   1 
ATOM   2240 C CB  . ALA   A 1 298 ? -6.773  29.748 -6.418  1.00 21.71 ? 320 ALA   A CB  1 
ATOM   2241 N N   . LEU   A 1 299 ? -5.759  27.406 -4.791  1.00 21.36 ? 321 LEU   A N   1 
ATOM   2242 C CA  . LEU   A 1 299 ? -5.773  26.191 -3.993  1.00 21.64 ? 321 LEU   A CA  1 
ATOM   2243 C C   . LEU   A 1 299 ? -7.214  25.713 -3.772  1.00 22.54 ? 321 LEU   A C   1 
ATOM   2244 O O   . LEU   A 1 299 ? -8.145  26.156 -4.446  1.00 22.12 ? 321 LEU   A O   1 
ATOM   2245 C CB  . LEU   A 1 299 ? -4.993  26.464 -2.704  1.00 22.08 ? 321 LEU   A CB  1 
ATOM   2246 C CG  . LEU   A 1 299 ? -3.500  26.791 -2.860  1.00 21.95 ? 321 LEU   A CG  1 
ATOM   2247 C CD1 . LEU   A 1 299 ? -2.794  26.799 -1.496  1.00 22.27 ? 321 LEU   A CD1 1 
ATOM   2248 C CD2 . LEU   A 1 299 ? -2.814  25.813 -3.780  1.00 21.45 ? 321 LEU   A CD2 1 
ATOM   2249 N N   . GLU   A 1 300 ? -7.384  24.781 -2.828  1.00 24.16 ? 322 GLU   A N   1 
ATOM   2250 C CA  . GLU   A 1 300 ? -8.500  23.847 -2.862  1.00 25.52 ? 322 GLU   A CA  1 
ATOM   2251 C C   . GLU   A 1 300 ? -9.858  24.496 -2.598  1.00 25.80 ? 322 GLU   A C   1 
ATOM   2252 O O   . GLU   A 1 300 ? -10.856 23.889 -2.964  1.00 27.42 ? 322 GLU   A O   1 
ATOM   2253 C CB  . GLU   A 1 300 ? -8.316  22.686 -1.892  1.00 29.34 ? 322 GLU   A CB  1 
ATOM   2254 C CG  . GLU   A 1 300 ? -7.911  23.144 -0.500  1.00 33.47 ? 322 GLU   A CG  1 
ATOM   2255 C CD  . GLU   A 1 300 ? -6.429  22.996 -0.165  1.00 36.71 ? 322 GLU   A CD  1 
ATOM   2256 O OE1 . GLU   A 1 300 ? -5.516  23.390 -0.976  1.00 34.97 ? 322 GLU   A OE1 1 
ATOM   2257 O OE2 . GLU   A 1 300 ? -6.210  22.474 0.971   1.00 39.65 ? 322 GLU   A OE2 1 
ATOM   2258 N N   . ASN   A 1 301 ? -9.925  25.691 -1.992  1.00 26.86 ? 323 ASN   A N   1 
ATOM   2259 C CA  . ASN   A 1 301 ? -11.210 26.365 -1.815  1.00 29.58 ? 323 ASN   A CA  1 
ATOM   2260 C C   . ASN   A 1 301 ? -11.706 26.963 -3.132  1.00 27.79 ? 323 ASN   A C   1 
ATOM   2261 O O   . ASN   A 1 301 ? -12.846 27.416 -3.199  1.00 32.44 ? 323 ASN   A O   1 
ATOM   2262 C CB  . ASN   A 1 301 ? -11.181 27.460 -0.748  1.00 33.80 ? 323 ASN   A CB  1 
ATOM   2263 C CG  . ASN   A 1 301 ? -12.555 28.029 -0.442  1.00 37.14 ? 323 ASN   A CG  1 
ATOM   2264 O OD1 . ASN   A 1 301 ? -13.514 27.279 -0.221  1.00 39.13 ? 323 ASN   A OD1 1 
ATOM   2265 N ND2 . ASN   A 1 301 ? -12.692 29.348 -0.440  1.00 39.10 ? 323 ASN   A ND2 1 
ATOM   2266 N N   . ASP   A 1 302 ? -10.865 26.938 -4.172  1.00 23.49 ? 324 ASP   A N   1 
ATOM   2267 C CA  . ASP   A 1 302 ? -11.142 27.620 -5.433  1.00 21.90 ? 324 ASP   A CA  1 
ATOM   2268 C C   . ASP   A 1 302 ? -11.047 26.607 -6.574  1.00 21.05 ? 324 ASP   A C   1 
ATOM   2269 O O   . ASP   A 1 302 ? -12.053 26.324 -7.214  1.00 20.83 ? 324 ASP   A O   1 
ATOM   2270 C CB  . ASP   A 1 302 ? -10.203 28.811 -5.577  1.00 22.63 ? 324 ASP   A CB  1 
ATOM   2271 C CG  . ASP   A 1 302 ? -10.304 29.615 -6.866  1.00 21.65 ? 324 ASP   A CG  1 
ATOM   2272 O OD1 . ASP   A 1 302 ? -10.415 28.995 -7.938  1.00 22.69 ? 324 ASP   A OD1 1 
ATOM   2273 O OD2 . ASP   A 1 302 ? -10.206 30.860 -6.789  1.00 22.90 ? 324 ASP   A OD2 1 
ATOM   2274 N N   . LYS   A 1 303 ? -9.839  26.073 -6.812  1.00 21.37 ? 325 LYS   A N   1 
ATOM   2275 C CA  . LYS   A 1 303 ? -9.579  25.003 -7.769  1.00 21.78 ? 325 LYS   A CA  1 
ATOM   2276 C C   . LYS   A 1 303 ? -9.754  25.469 -9.214  1.00 20.51 ? 325 LYS   A C   1 
ATOM   2277 O O   . LYS   A 1 303 ? -9.852  24.631 -10.109 1.00 19.67 ? 325 LYS   A O   1 
ATOM   2278 C CB  . LYS   A 1 303 ? -10.487 23.776 -7.590  1.00 24.70 ? 325 LYS   A CB  1 
ATOM   2279 C CG  . LYS   A 1 303 ? -10.506 23.176 -6.199  1.00 27.62 ? 325 LYS   A CG  1 
ATOM   2280 C CD  . LYS   A 1 303 ? -11.198 21.818 -6.164  1.00 31.28 ? 325 LYS   A CD  1 
ATOM   2281 C CE  . LYS   A 1 303 ? -12.671 21.898 -6.009  1.00 37.69 ? 325 LYS   A CE  1 
ATOM   2282 N NZ  . LYS   A 1 303 ? -13.043 22.026 -4.599  1.00 39.93 ? 325 LYS   A NZ  1 
ATOM   2283 N N   . THR   A 1 304 ? -9.803  26.784 -9.451  1.00 19.76 ? 326 THR   A N   1 
ATOM   2284 C CA  . THR   A 1 304 ? -9.997  27.267 -10.810 1.00 21.06 ? 326 THR   A CA  1 
ATOM   2285 C C   . THR   A 1 304 ? -8.746  28.003 -11.276 1.00 20.27 ? 326 THR   A C   1 
ATOM   2286 O O   . THR   A 1 304 ? -7.885  28.399 -10.489 1.00 20.23 ? 326 THR   A O   1 
ATOM   2287 C CB  . THR   A 1 304 ? -11.242 28.144 -10.986 1.00 21.95 ? 326 THR   A CB  1 
ATOM   2288 O OG1 . THR   A 1 304 ? -10.985 29.409 -10.381 1.00 23.09 ? 326 THR   A OG1 1 
ATOM   2289 C CG2 . THR   A 1 304 ? -12.511 27.484 -10.476 1.00 21.82 ? 326 THR   A CG2 1 
ATOM   2290 N N   . ILE   A 1 305 ? -8.699  28.165 -12.598 1.00 19.62 ? 327 ILE   A N   1 
ATOM   2291 C CA  . ILE   A 1 305 ? -7.688  28.944 -13.280 1.00 19.94 ? 327 ILE   A CA  1 
ATOM   2292 C C   . ILE   A 1 305 ? -8.396  30.154 -13.870 1.00 19.85 ? 327 ILE   A C   1 
ATOM   2293 O O   . ILE   A 1 305 ? -9.527  30.023 -14.342 1.00 20.15 ? 327 ILE   A O   1 
ATOM   2294 C CB  . ILE   A 1 305 ? -7.031  28.099 -14.377 1.00 20.19 ? 327 ILE   A CB  1 
ATOM   2295 C CG1 . ILE   A 1 305 ? -6.390  26.843 -13.799 1.00 21.11 ? 327 ILE   A CG1 1 
ATOM   2296 C CG2 . ILE   A 1 305 ? -6.035  28.924 -15.182 1.00 19.60 ? 327 ILE   A CG2 1 
ATOM   2297 C CD1 . ILE   A 1 305 ? -6.414  25.665 -14.747 1.00 21.94 ? 327 ILE   A CD1 1 
ATOM   2298 N N   . LYS   A 1 306 ? -7.742  31.315 -13.810 1.00 18.80 ? 328 LYS   A N   1 
ATOM   2299 C CA  . LYS   A 1 306 ? -8.311  32.509 -14.405 1.00 20.20 ? 328 LYS   A CA  1 
ATOM   2300 C C   . LYS   A 1 306 ? -7.352  33.037 -15.467 1.00 19.55 ? 328 LYS   A C   1 
ATOM   2301 O O   . LYS   A 1 306 ? -6.138  33.004 -15.288 1.00 19.14 ? 328 LYS   A O   1 
ATOM   2302 C CB  . LYS   A 1 306 ? -8.691  33.543 -13.347 1.00 21.76 ? 328 LYS   A CB  1 
ATOM   2303 C CG  . LYS   A 1 306 ? -9.897  33.095 -12.533 1.00 22.46 ? 328 LYS   A CG  1 
ATOM   2304 C CD  . LYS   A 1 306 ? -10.256 34.009 -11.369 1.00 22.99 ? 328 LYS   A CD  1 
ATOM   2305 C CE  . LYS   A 1 306 ? -11.346 33.418 -10.552 1.00 23.90 ? 328 LYS   A CE  1 
ATOM   2306 N NZ  . LYS   A 1 306 ? -12.676 33.483 -11.149 1.00 23.22 ? 328 LYS   A NZ  1 
ATOM   2307 N N   . LEU   A 1 307 ? -7.933  33.481 -16.579 1.00 18.87 ? 329 LEU   A N   1 
ATOM   2308 C CA  . LEU   A 1 307 ? -7.199  34.178 -17.627 1.00 19.12 ? 329 LEU   A CA  1 
ATOM   2309 C C   . LEU   A 1 307 ? -7.626  35.640 -17.659 1.00 19.89 ? 329 LEU   A C   1 
ATOM   2310 O O   . LEU   A 1 307 ? -8.819  35.939 -17.689 1.00 19.59 ? 329 LEU   A O   1 
ATOM   2311 C CB  . LEU   A 1 307 ? -7.457  33.518 -18.976 1.00 20.16 ? 329 LEU   A CB  1 
ATOM   2312 C CG  . LEU   A 1 307 ? -6.905  32.107 -19.128 1.00 20.68 ? 329 LEU   A CG  1 
ATOM   2313 C CD1 . LEU   A 1 307 ? -7.471  31.448 -20.368 1.00 21.28 ? 329 LEU   A CD1 1 
ATOM   2314 C CD2 . LEU   A 1 307 ? -5.388  32.162 -19.171 1.00 22.01 ? 329 LEU   A CD2 1 
ATOM   2315 N N   . TRP   A 1 308 ? -6.618  36.517 -17.706 1.00 20.26 ? 330 TRP   A N   1 
ATOM   2316 C CA  . TRP   A 1 308 ? -6.763  37.958 -17.584 1.00 20.59 ? 330 TRP   A CA  1 
ATOM   2317 C C   . TRP   A 1 308 ? -6.049  38.624 -18.752 1.00 21.24 ? 330 TRP   A C   1 
ATOM   2318 O O   . TRP   A 1 308 ? -4.976  38.162 -19.154 1.00 21.09 ? 330 TRP   A O   1 
ATOM   2319 C CB  . TRP   A 1 308 ? -6.117  38.474 -16.292 1.00 20.90 ? 330 TRP   A CB  1 
ATOM   2320 C CG  . TRP   A 1 308 ? -6.430  37.696 -15.047 1.00 21.03 ? 330 TRP   A CG  1 
ATOM   2321 C CD1 . TRP   A 1 308 ? -5.825  36.536 -14.653 1.00 20.82 ? 330 TRP   A CD1 1 
ATOM   2322 C CD2 . TRP   A 1 308 ? -7.341  38.067 -13.994 1.00 21.45 ? 330 TRP   A CD2 1 
ATOM   2323 N NE1 . TRP   A 1 308 ? -6.324  36.143 -13.448 1.00 21.28 ? 330 TRP   A NE1 1 
ATOM   2324 C CE2 . TRP   A 1 308 ? -7.240  37.063 -13.011 1.00 21.80 ? 330 TRP   A CE2 1 
ATOM   2325 C CE3 . TRP   A 1 308 ? -8.232  39.129 -13.791 1.00 21.36 ? 330 TRP   A CE3 1 
ATOM   2326 C CZ2 . TRP   A 1 308 ? -7.995  37.089 -11.839 1.00 21.79 ? 330 TRP   A CZ2 1 
ATOM   2327 C CZ3 . TRP   A 1 308 ? -8.968  39.162 -12.627 1.00 21.26 ? 330 TRP   A CZ3 1 
ATOM   2328 C CH2 . TRP   A 1 308 ? -8.849  38.153 -11.669 1.00 22.29 ? 330 TRP   A CH2 1 
ATOM   2329 N N   . LYS   A 1 309 ? -6.622  39.718 -19.265 1.00 21.83 ? 331 LYS   A N   1 
ATOM   2330 C CA  . LYS   A 1 309 ? -5.982  40.413 -20.376 1.00 22.99 ? 331 LYS   A CA  1 
ATOM   2331 C C   . LYS   A 1 309 ? -5.925  41.915 -20.122 1.00 22.43 ? 331 LYS   A C   1 
ATOM   2332 O O   . LYS   A 1 309 ? -6.856  42.513 -19.566 1.00 22.25 ? 331 LYS   A O   1 
ATOM   2333 C CB  . LYS   A 1 309 ? -6.668  40.113 -21.710 1.00 25.19 ? 331 LYS   A CB  1 
ATOM   2334 C CG  . LYS   A 1 309 ? -5.910  40.655 -22.912 1.00 28.67 ? 331 LYS   A CG  1 
ATOM   2335 C CD  . LYS   A 1 309 ? -6.533  40.255 -24.238 1.00 33.08 ? 331 LYS   A CD  1 
ATOM   2336 C CE  . LYS   A 1 309 ? -5.661  40.552 -25.418 1.00 36.97 ? 331 LYS   A CE  1 
ATOM   2337 N NZ  . LYS   A 1 309 ? -5.267  41.954 -25.485 1.00 40.89 ? 331 LYS   A NZ  1 
ATOM   2338 N N   . SER   A 1 310 ? -4.821  42.502 -20.602 1.00 23.02 ? 332 SER   A N   1 
ATOM   2339 C CA  . SER   A 1 310 ? -4.484  43.900 -20.391 1.00 24.80 ? 332 SER   A CA  1 
ATOM   2340 C C   . SER   A 1 310 ? -4.138  44.557 -21.726 1.00 26.27 ? 332 SER   A C   1 
ATOM   2341 O O   . SER   A 1 310 ? -3.708  43.886 -22.660 1.00 26.03 ? 332 SER   A O   1 
ATOM   2342 C CB  . SER   A 1 310 ? -3.334  44.040 -19.423 1.00 24.69 ? 332 SER   A CB  1 
ATOM   2343 O OG  . SER   A 1 310 ? -2.875  45.388 -19.335 1.00 26.03 ? 332 SER   A OG  1 
ATOM   2344 N N   . ASP   A 1 311 ? -4.311  45.878 -21.791 1.00 28.12 ? 333 ASP   A N   1 
ATOM   2345 C CA  . ASP   A 1 311 ? -3.897  46.652 -22.952 1.00 31.34 ? 333 ASP   A CA  1 
ATOM   2346 C C   . ASP   A 1 311 ? -2.395  46.957 -22.929 1.00 34.51 ? 333 ASP   A C   1 
ATOM   2347 O O   . ASP   A 1 311 ? -1.830  47.313 -23.966 1.00 36.25 ? 333 ASP   A O   1 
ATOM   2348 C CB  . ASP   A 1 311 ? -4.703  47.933 -23.056 1.00 33.03 ? 333 ASP   A CB  1 
ATOM   2349 C CG  . ASP   A 1 311 ? -6.199  47.715 -23.218 1.00 35.48 ? 333 ASP   A CG  1 
ATOM   2350 O OD1 . ASP   A 1 311 ? -6.574  46.799 -23.974 1.00 38.24 ? 333 ASP   A OD1 1 
ATOM   2351 O OD2 . ASP   A 1 311 ? -6.973  48.468 -22.601 1.00 37.71 ? 333 ASP   A OD2 1 
ATOM   2352 N N   . CYS   A 1 312 ? -1.753  46.847 -21.757 1.00 33.55 ? 334 CYS   A N   1 
ATOM   2353 C CA  . CYS   A 1 312 ? -0.317  47.083 -21.652 1.00 36.77 ? 334 CYS   A CA  1 
ATOM   2354 C C   . CYS   A 1 312 ? 0.300   46.243 -20.514 1.00 35.39 ? 334 CYS   A C   1 
ATOM   2355 O O   . CYS   A 1 312 ? -0.435  45.395 -19.961 1.00 30.42 ? 334 CYS   A O   1 
ATOM   2356 C CB  . CYS   A 1 312 ? -0.027  48.567 -21.458 1.00 39.79 ? 334 CYS   A CB  1 
ATOM   2357 S SG  . CYS   A 1 312 ? -0.584  49.223 -19.862 1.00 40.06 ? 334 CYS   A SG  1 
ATOM   2358 O OXT . CYS   A 1 312 ? 1.510   46.470 -20.222 1.00 35.62 ? 334 CYS   A OXT 1 
ATOM   2359 N N   . VAL   B 1 9   ? -18.527 4.124  -38.203 1.00 60.17 ? 31  VAL   B N   1 
ATOM   2360 C CA  . VAL   B 1 9   ? -19.098 5.362  -37.590 1.00 57.34 ? 31  VAL   B CA  1 
ATOM   2361 C C   . VAL   B 1 9   ? -19.592 6.265  -38.717 1.00 53.61 ? 31  VAL   B C   1 
ATOM   2362 O O   . VAL   B 1 9   ? -18.841 6.568  -39.637 1.00 55.64 ? 31  VAL   B O   1 
ATOM   2363 C CB  . VAL   B 1 9   ? -18.077 6.099  -36.698 1.00 56.04 ? 31  VAL   B CB  1 
ATOM   2364 N N   . LYS   B 1 10  ? -20.868 6.660  -38.648 1.00 46.40 ? 32  LYS   B N   1 
ATOM   2365 C CA  . LYS   B 1 10  ? -21.422 7.679  -39.527 1.00 42.07 ? 32  LYS   B CA  1 
ATOM   2366 C C   . LYS   B 1 10  ? -22.206 8.659  -38.657 1.00 39.28 ? 32  LYS   B C   1 
ATOM   2367 O O   . LYS   B 1 10  ? -22.857 8.243  -37.708 1.00 40.66 ? 32  LYS   B O   1 
ATOM   2368 C CB  . LYS   B 1 10  ? -22.324 7.086  -40.622 1.00 44.88 ? 32  LYS   B CB  1 
ATOM   2369 C CG  . LYS   B 1 10  ? -21.653 6.112  -41.591 1.00 44.85 ? 32  LYS   B CG  1 
ATOM   2370 N N   . PRO   B 1 11  ? -22.153 9.985  -38.926 1.00 36.86 ? 33  PRO   B N   1 
ATOM   2371 C CA  . PRO   B 1 11  ? -22.962 10.951 -38.181 1.00 35.19 ? 33  PRO   B CA  1 
ATOM   2372 C C   . PRO   B 1 11  ? -24.431 10.885 -38.598 1.00 35.54 ? 33  PRO   B C   1 
ATOM   2373 O O   . PRO   B 1 11  ? -24.765 10.274 -39.615 1.00 38.02 ? 33  PRO   B O   1 
ATOM   2374 C CB  . PRO   B 1 11  ? -22.309 12.294 -38.522 1.00 36.62 ? 33  PRO   B CB  1 
ATOM   2375 C CG  . PRO   B 1 11  ? -21.765 12.081 -39.915 1.00 35.51 ? 33  PRO   B CG  1 
ATOM   2376 C CD  . PRO   B 1 11  ? -21.375 10.607 -40.001 1.00 36.67 ? 33  PRO   B CD  1 
ATOM   2377 N N   . ASN   B 1 12  ? -25.304 11.515 -37.802 1.00 37.73 ? 34  ASN   B N   1 
ATOM   2378 C CA  . ASN   B 1 12  ? -26.735 11.529 -38.077 1.00 38.92 ? 34  ASN   B CA  1 
ATOM   2379 C C   . ASN   B 1 12  ? -27.280 12.947 -37.924 1.00 36.32 ? 34  ASN   B C   1 
ATOM   2380 O O   . ASN   B 1 12  ? -28.341 13.157 -37.333 1.00 36.74 ? 34  ASN   B O   1 
ATOM   2381 C CB  . ASN   B 1 12  ? -27.503 10.514 -37.228 1.00 41.88 ? 34  ASN   B CB  1 
ATOM   2382 C CG  . ASN   B 1 12  ? -27.313 10.679 -35.735 1.00 42.87 ? 34  ASN   B CG  1 
ATOM   2383 O OD1 . ASN   B 1 12  ? -26.392 11.363 -35.283 1.00 42.48 ? 34  ASN   B OD1 1 
ATOM   2384 N ND2 . ASN   B 1 12  ? -28.150 10.021 -34.942 1.00 45.96 ? 34  ASN   B ND2 1 
ATOM   2385 N N   . TYR   B 1 13  ? -26.561 13.917 -38.501 1.00 34.19 ? 35  TYR   B N   1 
ATOM   2386 C CA  . TYR   B 1 13  ? -27.022 15.292 -38.521 1.00 33.81 ? 35  TYR   B CA  1 
ATOM   2387 C C   . TYR   B 1 13  ? -28.480 15.343 -38.961 1.00 33.01 ? 35  TYR   B C   1 
ATOM   2388 O O   . TYR   B 1 13  ? -28.875 14.748 -39.962 1.00 32.25 ? 35  TYR   B O   1 
ATOM   2389 C CB  . TYR   B 1 13  ? -26.136 16.167 -39.405 1.00 31.19 ? 35  TYR   B CB  1 
ATOM   2390 C CG  . TYR   B 1 13  ? -24.861 16.527 -38.663 1.00 29.86 ? 35  TYR   B CG  1 
ATOM   2391 C CD1 . TYR   B 1 13  ? -24.845 17.568 -37.742 1.00 29.48 ? 35  TYR   B CD1 1 
ATOM   2392 C CD2 . TYR   B 1 13  ? -23.703 15.784 -38.830 1.00 30.26 ? 35  TYR   B CD2 1 
ATOM   2393 C CE1 . TYR   B 1 13  ? -23.706 17.875 -37.019 1.00 28.03 ? 35  TYR   B CE1 1 
ATOM   2394 C CE2 . TYR   B 1 13  ? -22.555 16.081 -38.115 1.00 29.73 ? 35  TYR   B CE2 1 
ATOM   2395 C CZ  . TYR   B 1 13  ? -22.555 17.132 -37.210 1.00 29.08 ? 35  TYR   B CZ  1 
ATOM   2396 O OH  . TYR   B 1 13  ? -21.424 17.424 -36.497 1.00 28.68 ? 35  TYR   B OH  1 
ATOM   2397 N N   . ALA   B 1 14  ? -29.261 16.074 -38.174 1.00 33.74 ? 36  ALA   B N   1 
ATOM   2398 C CA  . ALA   B 1 14  ? -30.671 16.250 -38.433 1.00 35.23 ? 36  ALA   B CA  1 
ATOM   2399 C C   . ALA   B 1 14  ? -31.008 17.711 -38.185 1.00 32.81 ? 36  ALA   B C   1 
ATOM   2400 O O   . ALA   B 1 14  ? -30.432 18.328 -37.293 1.00 30.95 ? 36  ALA   B O   1 
ATOM   2401 C CB  . ALA   B 1 14  ? -31.467 15.328 -37.536 1.00 36.92 ? 36  ALA   B CB  1 
ATOM   2402 N N   . LEU   B 1 15  ? -31.953 18.230 -38.970 1.00 33.45 ? 37  LEU   B N   1 
ATOM   2403 C CA  . LEU   B 1 15  ? -32.277 19.644 -38.958 1.00 32.47 ? 37  LEU   B CA  1 
ATOM   2404 C C   . LEU   B 1 15  ? -32.929 20.000 -37.633 1.00 32.29 ? 37  LEU   B C   1 
ATOM   2405 O O   . LEU   B 1 15  ? -33.837 19.303 -37.204 1.00 33.35 ? 37  LEU   B O   1 
ATOM   2406 C CB  . LEU   B 1 15  ? -33.227 19.949 -40.109 1.00 34.30 ? 37  LEU   B CB  1 
ATOM   2407 C CG  . LEU   B 1 15  ? -33.661 21.411 -40.235 1.00 33.70 ? 37  LEU   B CG  1 
ATOM   2408 C CD1 . LEU   B 1 15  ? -32.474 22.283 -40.603 1.00 33.44 ? 37  LEU   B CD1 1 
ATOM   2409 C CD2 . LEU   B 1 15  ? -34.757 21.513 -41.275 1.00 37.01 ? 37  LEU   B CD2 1 
ATOM   2410 N N   . LYS   B 1 16  ? -32.484 21.096 -37.014 1.00 34.21 ? 38  LYS   B N   1 
ATOM   2411 C CA  . LYS   B 1 16  ? -33.078 21.547 -35.765 1.00 35.54 ? 38  LYS   B CA  1 
ATOM   2412 C C   . LYS   B 1 16  ? -33.801 22.873 -35.973 1.00 35.31 ? 38  LYS   B C   1 
ATOM   2413 O O   . LYS   B 1 16  ? -34.866 23.086 -35.380 1.00 36.53 ? 38  LYS   B O   1 
ATOM   2414 C CB  . LYS   B 1 16  ? -32.029 21.621 -34.651 1.00 37.11 ? 38  LYS   B CB  1 
ATOM   2415 C CG  . LYS   B 1 16  ? -31.370 20.287 -34.308 1.00 41.41 ? 38  LYS   B CG  1 
ATOM   2416 C CD  . LYS   B 1 16  ? -32.281 19.154 -33.839 1.00 44.22 ? 38  LYS   B CD  1 
ATOM   2417 C CE  . LYS   B 1 16  ? -32.630 19.185 -32.391 1.00 47.82 ? 38  LYS   B CE  1 
ATOM   2418 N NZ  . LYS   B 1 16  ? -33.263 17.930 -31.955 1.00 49.29 ? 38  LYS   B NZ  1 
ATOM   2419 N N   . PHE   B 1 17  ? -33.214 23.743 -36.811 1.00 33.27 ? 39  PHE   B N   1 
ATOM   2420 C CA  . PHE   B 1 17  ? -33.731 25.084 -37.039 1.00 33.63 ? 39  PHE   B CA  1 
ATOM   2421 C C   . PHE   B 1 17  ? -33.382 25.562 -38.448 1.00 32.98 ? 39  PHE   B C   1 
ATOM   2422 O O   . PHE   B 1 17  ? -32.347 25.188 -39.001 1.00 33.27 ? 39  PHE   B O   1 
ATOM   2423 C CB  . PHE   B 1 17  ? -33.169 26.089 -36.024 1.00 32.34 ? 39  PHE   B CB  1 
ATOM   2424 C CG  . PHE   B 1 17  ? -33.422 25.707 -34.570 1.00 33.59 ? 39  PHE   B CG  1 
ATOM   2425 C CD1 . PHE   B 1 17  ? -34.662 25.934 -33.972 1.00 34.01 ? 39  PHE   B CD1 1 
ATOM   2426 C CD2 . PHE   B 1 17  ? -32.434 25.072 -33.823 1.00 34.00 ? 39  PHE   B CD2 1 
ATOM   2427 C CE1 . PHE   B 1 17  ? -34.892 25.563 -32.654 1.00 34.35 ? 39  PHE   B CE1 1 
ATOM   2428 C CE2 . PHE   B 1 17  ? -32.676 24.690 -32.511 1.00 34.78 ? 39  PHE   B CE2 1 
ATOM   2429 C CZ  . PHE   B 1 17  ? -33.902 24.938 -31.927 1.00 34.84 ? 39  PHE   B CZ  1 
ATOM   2430 N N   . THR   B 1 18  ? -34.287 26.385 -39.004 1.00 33.33 ? 40  THR   B N   1 
ATOM   2431 C CA  . THR   B 1 18  ? -34.043 27.197 -40.186 1.00 32.57 ? 40  THR   B CA  1 
ATOM   2432 C C   . THR   B 1 18  ? -34.114 28.664 -39.766 1.00 33.12 ? 40  THR   B C   1 
ATOM   2433 O O   . THR   B 1 18  ? -35.089 29.082 -39.142 1.00 33.99 ? 40  THR   B O   1 
ATOM   2434 C CB  . THR   B 1 18  ? -35.071 26.874 -41.272 1.00 32.23 ? 40  THR   B CB  1 
ATOM   2435 O OG1 . THR   B 1 18  ? -34.835 25.509 -41.612 1.00 32.56 ? 40  THR   B OG1 1 
ATOM   2436 C CG2 . THR   B 1 18  ? -34.908 27.726 -42.520 1.00 31.81 ? 40  THR   B CG2 1 
ATOM   2437 N N   . LEU   B 1 19  ? -33.077 29.432 -40.133 1.00 32.01 ? 41  LEU   B N   1 
ATOM   2438 C CA  . LEU   B 1 19  ? -32.931 30.816 -39.701 1.00 31.73 ? 41  LEU   B CA  1 
ATOM   2439 C C   . LEU   B 1 19  ? -33.159 31.744 -40.891 1.00 30.02 ? 41  LEU   B C   1 
ATOM   2440 O O   . LEU   B 1 19  ? -32.312 31.838 -41.786 1.00 32.58 ? 41  LEU   B O   1 
ATOM   2441 C CB  . LEU   B 1 19  ? -31.564 31.081 -39.069 1.00 32.17 ? 41  LEU   B CB  1 
ATOM   2442 C CG  . LEU   B 1 19  ? -31.022 30.024 -38.099 1.00 33.93 ? 41  LEU   B CG  1 
ATOM   2443 C CD1 . LEU   B 1 19  ? -29.804 30.599 -37.408 1.00 32.68 ? 41  LEU   B CD1 1 
ATOM   2444 C CD2 . LEU   B 1 19  ? -31.994 29.506 -37.074 1.00 33.26 ? 41  LEU   B CD2 1 
ATOM   2445 N N   . ALA   B 1 20  ? -34.306 32.434 -40.868 1.00 30.45 ? 42  ALA   B N   1 
ATOM   2446 C CA  . ALA   B 1 20  ? -34.720 33.347 -41.922 1.00 30.02 ? 42  ALA   B CA  1 
ATOM   2447 C C   . ALA   B 1 20  ? -34.550 34.786 -41.443 1.00 29.43 ? 42  ALA   B C   1 
ATOM   2448 O O   . ALA   B 1 20  ? -34.750 35.073 -40.261 1.00 28.06 ? 42  ALA   B O   1 
ATOM   2449 C CB  . ALA   B 1 20  ? -36.161 33.070 -42.287 1.00 32.16 ? 42  ALA   B CB  1 
ATOM   2450 N N   . GLY   B 1 21  ? -34.192 35.680 -42.371 1.00 28.30 ? 43  GLY   B N   1 
ATOM   2451 C CA  . GLY   B 1 21  ? -33.990 37.084 -42.043 1.00 29.30 ? 43  GLY   B CA  1 
ATOM   2452 C C   . GLY   B 1 21  ? -33.253 37.846 -43.145 1.00 28.48 ? 43  GLY   B C   1 
ATOM   2453 O O   . GLY   B 1 21  ? -33.603 38.986 -43.438 1.00 29.04 ? 43  GLY   B O   1 
ATOM   2454 N N   . HIS   B 1 22  ? -32.183 37.256 -43.700 1.00 27.82 ? 44  HIS   B N   1 
ATOM   2455 C CA  . HIS   B 1 22  ? -31.419 37.919 -44.750 1.00 26.02 ? 44  HIS   B CA  1 
ATOM   2456 C C   . HIS   B 1 22  ? -32.312 38.092 -45.979 1.00 26.33 ? 44  HIS   B C   1 
ATOM   2457 O O   . HIS   B 1 22  ? -33.167 37.246 -46.240 1.00 27.25 ? 44  HIS   B O   1 
ATOM   2458 C CB  . HIS   B 1 22  ? -30.116 37.169 -45.055 1.00 24.39 ? 44  HIS   B CB  1 
ATOM   2459 C CG  . HIS   B 1 22  ? -29.062 37.354 -44.023 1.00 22.61 ? 44  HIS   B CG  1 
ATOM   2460 N ND1 . HIS   B 1 22  ? -28.556 38.598 -43.717 1.00 21.93 ? 44  HIS   B ND1 1 
ATOM   2461 C CD2 . HIS   B 1 22  ? -28.457 36.489 -43.186 1.00 21.86 ? 44  HIS   B CD2 1 
ATOM   2462 C CE1 . HIS   B 1 22  ? -27.640 38.470 -42.752 1.00 22.01 ? 44  HIS   B CE1 1 
ATOM   2463 N NE2 . HIS   B 1 22  ? -27.580 37.200 -42.402 1.00 22.62 ? 44  HIS   B NE2 1 
ATOM   2464 N N   . THR   B 1 23  ? -32.117 39.202 -46.705 1.00 26.01 ? 45  THR   B N   1 
ATOM   2465 C CA  . THR   B 1 23  ? -32.972 39.572 -47.827 1.00 25.53 ? 45  THR   B CA  1 
ATOM   2466 C C   . THR   B 1 23  ? -32.259 39.355 -49.159 1.00 24.93 ? 45  THR   B C   1 
ATOM   2467 O O   . THR   B 1 23  ? -32.850 39.575 -50.220 1.00 25.58 ? 45  THR   B O   1 
ATOM   2468 C CB  . THR   B 1 23  ? -33.476 41.010 -47.683 1.00 27.12 ? 45  THR   B CB  1 
ATOM   2469 O OG1 . THR   B 1 23  ? -32.376 41.906 -47.719 1.00 27.45 ? 45  THR   B OG1 1 
ATOM   2470 C CG2 . THR   B 1 23  ? -34.256 41.216 -46.399 1.00 28.13 ? 45  THR   B CG2 1 
ATOM   2471 N N   . LYS   B 1 24  ? -30.993 38.934 -49.088 1.00 23.72 ? 46  LYS   B N   1 
ATOM   2472 C CA  . LYS   B 1 24  ? -30.274 38.434 -50.244 1.00 24.07 ? 46  LYS   B CA  1 
ATOM   2473 C C   . LYS   B 1 24  ? -29.504 37.197 -49.804 1.00 23.63 ? 46  LYS   B C   1 
ATOM   2474 O O   . LYS   B 1 24  ? -29.605 36.763 -48.653 1.00 22.76 ? 46  LYS   B O   1 
ATOM   2475 C CB  . LYS   B 1 24  ? -29.338 39.491 -50.852 1.00 23.95 ? 46  LYS   B CB  1 
ATOM   2476 C CG  . LYS   B 1 24  ? -30.004 40.746 -51.401 1.00 24.56 ? 46  LYS   B CG  1 
ATOM   2477 C CD  . LYS   B 1 24  ? -29.039 41.680 -52.121 1.00 24.16 ? 46  LYS   B CD  1 
ATOM   2478 C CE  . LYS   B 1 24  ? -29.697 42.864 -52.753 1.00 22.93 ? 46  LYS   B CE  1 
ATOM   2479 N NZ  . LYS   B 1 24  ? -28.732 43.710 -53.461 1.00 21.19 ? 46  LYS   B NZ  1 
ATOM   2480 N N   . ALA   B 1 25  ? -28.744 36.641 -50.747 1.00 23.25 ? 47  ALA   B N   1 
ATOM   2481 C CA  . ALA   B 1 25  ? -27.884 35.505 -50.471 1.00 23.08 ? 47  ALA   B CA  1 
ATOM   2482 C C   . ALA   B 1 25  ? -27.107 35.711 -49.169 1.00 22.04 ? 47  ALA   B C   1 
ATOM   2483 O O   . ALA   B 1 25  ? -26.624 36.806 -48.860 1.00 21.93 ? 47  ALA   B O   1 
ATOM   2484 C CB  . ALA   B 1 25  ? -26.948 35.289 -51.645 1.00 23.08 ? 47  ALA   B CB  1 
ATOM   2485 N N   . VAL   B 1 26  ? -26.975 34.624 -48.417 1.00 21.17 ? 48  VAL   B N   1 
ATOM   2486 C CA  . VAL   B 1 26  ? -26.078 34.584 -47.278 1.00 20.92 ? 48  VAL   B CA  1 
ATOM   2487 C C   . VAL   B 1 26  ? -24.702 34.217 -47.818 1.00 20.03 ? 48  VAL   B C   1 
ATOM   2488 O O   . VAL   B 1 26  ? -24.605 33.388 -48.718 1.00 21.97 ? 48  VAL   B O   1 
ATOM   2489 C CB  . VAL   B 1 26  ? -26.570 33.585 -46.207 1.00 21.79 ? 48  VAL   B CB  1 
ATOM   2490 C CG1 . VAL   B 1 26  ? -25.685 33.588 -44.960 1.00 20.62 ? 48  VAL   B CG1 1 
ATOM   2491 C CG2 . VAL   B 1 26  ? -28.017 33.847 -45.796 1.00 23.79 ? 48  VAL   B CG2 1 
ATOM   2492 N N   . SER   B 1 27  ? -23.647 34.859 -47.310 1.00 19.05 ? 49  SER   B N   1 
ATOM   2493 C CA  . SER   B 1 27  ? -22.300 34.632 -47.829 1.00 18.28 ? 49  SER   B CA  1 
ATOM   2494 C C   . SER   B 1 27  ? -21.437 33.772 -46.902 1.00 17.94 ? 49  SER   B C   1 
ATOM   2495 O O   . SER   B 1 27  ? -20.558 33.044 -47.367 1.00 17.25 ? 49  SER   B O   1 
ATOM   2496 C CB  . SER   B 1 27  ? -21.614 35.943 -48.108 1.00 17.84 ? 49  SER   B CB  1 
ATOM   2497 O OG  . SER   B 1 27  ? -21.730 36.810 -46.989 1.00 17.84 ? 49  SER   B OG  1 
ATOM   2498 N N   . SER   B 1 28  ? -21.638 33.879 -45.588 1.00 18.46 ? 50  SER   B N   1 
ATOM   2499 C CA  . SER   B 1 28  ? -20.729 33.245 -44.651 1.00 18.49 ? 50  SER   B CA  1 
ATOM   2500 C C   . SER   B 1 28  ? -21.446 33.080 -43.325 1.00 18.32 ? 50  SER   B C   1 
ATOM   2501 O O   . SER   B 1 28  ? -22.163 33.992 -42.932 1.00 20.21 ? 50  SER   B O   1 
ATOM   2502 C CB  . SER   B 1 28  ? -19.481 34.088 -44.474 1.00 20.32 ? 50  SER   B CB  1 
ATOM   2503 O OG  . SER   B 1 28  ? -18.510 33.441 -43.675 1.00 23.08 ? 50  SER   B OG  1 
ATOM   2504 N N   . VAL   B 1 29  ? -21.248 31.929 -42.667 1.00 17.65 ? 51  VAL   B N   1 
ATOM   2505 C CA  . VAL   B 1 29  ? -21.678 31.729 -41.292 1.00 17.51 ? 51  VAL   B CA  1 
ATOM   2506 C C   . VAL   B 1 29  ? -20.488 31.230 -40.474 1.00 16.13 ? 51  VAL   B C   1 
ATOM   2507 O O   . VAL   B 1 29  ? -19.673 30.457 -40.973 1.00 16.12 ? 51  VAL   B O   1 
ATOM   2508 C CB  . VAL   B 1 29  ? -22.883 30.771 -41.188 1.00 18.03 ? 51  VAL   B CB  1 
ATOM   2509 C CG1 . VAL   B 1 29  ? -24.102 31.358 -41.874 1.00 19.64 ? 51  VAL   B CG1 1 
ATOM   2510 C CG2 . VAL   B 1 29  ? -22.598 29.386 -41.756 1.00 18.43 ? 51  VAL   B CG2 1 
ATOM   2511 N N   . LYS   B 1 30  ? -20.411 31.671 -39.211 1.00 16.86 ? 52  LYS   B N   1 
ATOM   2512 C CA  . LYS   B 1 30  ? -19.305 31.338 -38.318 1.00 16.87 ? 52  LYS   B CA  1 
ATOM   2513 C C   . LYS   B 1 30  ? -19.816 31.273 -36.875 1.00 17.56 ? 52  LYS   B C   1 
ATOM   2514 O O   . LYS   B 1 30  ? -20.545 32.163 -36.440 1.00 17.57 ? 52  LYS   B O   1 
ATOM   2515 C CB  . LYS   B 1 30  ? -18.148 32.351 -38.351 1.00 18.12 ? 52  LYS   B CB  1 
ATOM   2516 C CG  . LYS   B 1 30  ? -17.510 32.679 -39.710 1.00 17.73 ? 52  LYS   B CG  1 
ATOM   2517 C CD  . LYS   B 1 30  ? -16.648 31.550 -40.252 1.00 18.88 ? 52  LYS   B CD  1 
ATOM   2518 C CE  . LYS   B 1 30  ? -16.020 31.875 -41.568 1.00 20.17 ? 52  LYS   B CE  1 
ATOM   2519 N NZ  . LYS   B 1 30  ? -15.043 32.962 -41.505 1.00 20.73 ? 52  LYS   B NZ  1 
ATOM   2520 N N   . PHE   B 1 31  ? -19.423 30.216 -36.143 1.00 18.14 ? 53  PHE   B N   1 
ATOM   2521 C CA  . PHE   B 1 31  ? -19.741 30.098 -34.724 1.00 19.40 ? 53  PHE   B CA  1 
ATOM   2522 C C   . PHE   B 1 31  ? -18.743 30.904 -33.902 1.00 19.86 ? 53  PHE   B C   1 
ATOM   2523 O O   . PHE   B 1 31  ? -17.536 30.845 -34.149 1.00 19.92 ? 53  PHE   B O   1 
ATOM   2524 C CB  . PHE   B 1 31  ? -19.760 28.656 -34.197 1.00 20.01 ? 53  PHE   B CB  1 
ATOM   2525 C CG  . PHE   B 1 31  ? -20.948 27.840 -34.686 1.00 20.14 ? 53  PHE   B CG  1 
ATOM   2526 C CD1 . PHE   B 1 31  ? -22.186 27.985 -34.078 1.00 21.48 ? 53  PHE   B CD1 1 
ATOM   2527 C CD2 . PHE   B 1 31  ? -20.831 26.943 -35.747 1.00 20.31 ? 53  PHE   B CD2 1 
ATOM   2528 C CE1 . PHE   B 1 31  ? -23.277 27.248 -34.497 1.00 21.91 ? 53  PHE   B CE1 1 
ATOM   2529 C CE2 . PHE   B 1 31  ? -21.931 26.200 -36.162 1.00 20.93 ? 53  PHE   B CE2 1 
ATOM   2530 C CZ  . PHE   B 1 31  ? -23.145 26.337 -35.516 1.00 21.86 ? 53  PHE   B CZ  1 
ATOM   2531 N N   . SER   B 1 32  ? -19.247 31.595 -32.866 1.00 19.42 ? 54  SER   B N   1 
ATOM   2532 C CA  . SER   B 1 32  ? -18.365 32.247 -31.909 1.00 19.62 ? 54  SER   B CA  1 
ATOM   2533 C C   . SER   B 1 32  ? -17.520 31.193 -31.192 1.00 19.00 ? 54  SER   B C   1 
ATOM   2534 O O   . SER   B 1 32  ? -17.984 30.070 -30.953 1.00 17.62 ? 54  SER   B O   1 
ATOM   2535 C CB  . SER   B 1 32  ? -19.123 33.092 -30.907 1.00 20.50 ? 54  SER   B CB  1 
ATOM   2536 O OG  . SER   B 1 32  ? -20.033 32.313 -30.135 1.00 19.10 ? 54  SER   B OG  1 
ATOM   2537 N N   . PRO   B 1 33  ? -16.240 31.500 -30.880 1.00 17.82 ? 55  PRO   B N   1 
ATOM   2538 C CA  . PRO   B 1 33  ? -15.385 30.603 -30.099 1.00 17.57 ? 55  PRO   B CA  1 
ATOM   2539 C C   . PRO   B 1 33  ? -15.957 30.121 -28.767 1.00 18.59 ? 55  PRO   B C   1 
ATOM   2540 O O   . PRO   B 1 33  ? -15.670 28.998 -28.370 1.00 19.48 ? 55  PRO   B O   1 
ATOM   2541 C CB  . PRO   B 1 33  ? -14.116 31.456 -29.926 1.00 18.16 ? 55  PRO   B CB  1 
ATOM   2542 C CG  . PRO   B 1 33  ? -14.075 32.224 -31.194 1.00 17.66 ? 55  PRO   B CG  1 
ATOM   2543 C CD  . PRO   B 1 33  ? -15.497 32.651 -31.399 1.00 17.36 ? 55  PRO   B CD  1 
ATOM   2544 N N   . ASN   B 1 34  ? -16.791 30.948 -28.120 1.00 19.43 ? 56  ASN   B N   1 
ATOM   2545 C CA  . ASN   B 1 34  ? -17.427 30.575 -26.862 1.00 20.46 ? 56  ASN   B CA  1 
ATOM   2546 C C   . ASN   B 1 34  ? -18.667 29.696 -27.071 1.00 21.23 ? 56  ASN   B C   1 
ATOM   2547 O O   . ASN   B 1 34  ? -19.305 29.287 -26.092 1.00 21.18 ? 56  ASN   B O   1 
ATOM   2548 C CB  . ASN   B 1 34  ? -17.749 31.804 -26.021 1.00 21.20 ? 56  ASN   B CB  1 
ATOM   2549 C CG  . ASN   B 1 34  ? -18.857 32.659 -26.591 1.00 21.95 ? 56  ASN   B CG  1 
ATOM   2550 O OD1 . ASN   B 1 34  ? -19.528 32.294 -27.572 1.00 21.86 ? 56  ASN   B OD1 1 
ATOM   2551 N ND2 . ASN   B 1 34  ? -19.043 33.821 -25.983 1.00 22.64 ? 56  ASN   B ND2 1 
ATOM   2552 N N   . GLY   B 1 35  ? -19.006 29.391 -28.328 1.00 21.63 ? 57  GLY   B N   1 
ATOM   2553 C CA  . GLY   B 1 35  ? -20.069 28.441 -28.626 1.00 22.20 ? 57  GLY   B CA  1 
ATOM   2554 C C   . GLY   B 1 35  ? -21.481 29.036 -28.556 1.00 22.47 ? 57  GLY   B C   1 
ATOM   2555 O O   . GLY   B 1 35  ? -22.443 28.339 -28.864 1.00 22.60 ? 57  GLY   B O   1 
ATOM   2556 N N   . GLU   B 1 36  ? -21.610 30.314 -28.173 1.00 22.41 ? 58  GLU   B N   1 
ATOM   2557 C CA  . GLU   B 1 36  ? -22.902 30.895 -27.824 1.00 23.00 ? 58  GLU   B CA  1 
ATOM   2558 C C   . GLU   B 1 36  ? -23.684 31.369 -29.044 1.00 21.80 ? 58  GLU   B C   1 
ATOM   2559 O O   . GLU   B 1 36  ? -24.915 31.384 -29.012 1.00 22.08 ? 58  GLU   B O   1 
ATOM   2560 C CB  . GLU   B 1 36  ? -22.761 32.146 -26.954 1.00 24.79 ? 58  GLU   B CB  1 
ATOM   2561 C CG  . GLU   B 1 36  ? -22.222 31.865 -25.558 1.00 26.98 ? 58  GLU   B CG  1 
ATOM   2562 C CD  . GLU   B 1 36  ? -22.358 33.036 -24.598 1.00 32.31 ? 58  GLU   B CD  1 
ATOM   2563 O OE1 . GLU   B 1 36  ? -21.417 33.251 -23.785 1.00 34.17 ? 58  GLU   B OE1 1 
ATOM   2564 O OE2 . GLU   B 1 36  ? -23.424 33.696 -24.648 1.00 37.33 ? 58  GLU   B OE2 1 
ATOM   2565 N N   . TRP   B 1 37  ? -22.959 31.827 -30.073 1.00 20.98 ? 59  TRP   B N   1 
ATOM   2566 C CA  . TRP   B 1 37  ? -23.549 32.559 -31.185 1.00 22.14 ? 59  TRP   B CA  1 
ATOM   2567 C C   . TRP   B 1 37  ? -23.131 31.980 -32.535 1.00 21.83 ? 59  TRP   B C   1 
ATOM   2568 O O   . TRP   B 1 37  ? -22.052 31.384 -32.692 1.00 22.31 ? 59  TRP   B O   1 
ATOM   2569 C CB  . TRP   B 1 37  ? -23.147 34.040 -31.136 1.00 23.21 ? 59  TRP   B CB  1 
ATOM   2570 C CG  . TRP   B 1 37  ? -23.336 34.695 -29.798 1.00 23.80 ? 59  TRP   B CG  1 
ATOM   2571 C CD1 . TRP   B 1 37  ? -22.381 35.095 -28.904 1.00 23.83 ? 59  TRP   B CD1 1 
ATOM   2572 C CD2 . TRP   B 1 37  ? -24.606 35.004 -29.202 1.00 24.77 ? 59  TRP   B CD2 1 
ATOM   2573 N NE1 . TRP   B 1 37  ? -22.972 35.652 -27.803 1.00 25.64 ? 59  TRP   B NE1 1 
ATOM   2574 C CE2 . TRP   B 1 37  ? -24.334 35.609 -27.957 1.00 25.12 ? 59  TRP   B CE2 1 
ATOM   2575 C CE3 . TRP   B 1 37  ? -25.933 34.832 -29.613 1.00 25.55 ? 59  TRP   B CE3 1 
ATOM   2576 C CZ2 . TRP   B 1 37  ? -25.356 36.035 -27.117 1.00 26.71 ? 59  TRP   B CZ2 1 
ATOM   2577 C CZ3 . TRP   B 1 37  ? -26.940 35.250 -28.775 1.00 26.71 ? 59  TRP   B CZ3 1 
ATOM   2578 C CH2 . TRP   B 1 37  ? -26.648 35.847 -27.551 1.00 26.53 ? 59  TRP   B CH2 1 
ATOM   2579 N N   . LEU   B 1 38  ? -24.023 32.196 -33.508 1.00 21.25 ? 60  LEU   B N   1 
ATOM   2580 C CA  . LEU   B 1 38  ? -23.699 32.124 -34.924 1.00 21.95 ? 60  LEU   B CA  1 
ATOM   2581 C C   . LEU   B 1 38  ? -23.793 33.529 -35.505 1.00 20.51 ? 60  LEU   B C   1 
ATOM   2582 O O   . LEU   B 1 38  ? -24.787 34.215 -35.278 1.00 21.43 ? 60  LEU   B O   1 
ATOM   2583 C CB  . LEU   B 1 38  ? -24.656 31.187 -35.660 1.00 23.05 ? 60  LEU   B CB  1 
ATOM   2584 C CG  . LEU   B 1 38  ? -24.329 30.923 -37.131 1.00 24.68 ? 60  LEU   B CG  1 
ATOM   2585 C CD1 . LEU   B 1 38  ? -23.188 29.940 -37.229 1.00 23.92 ? 60  LEU   B CD1 1 
ATOM   2586 C CD2 . LEU   B 1 38  ? -25.562 30.438 -37.881 1.00 25.80 ? 60  LEU   B CD2 1 
ATOM   2587 N N   . ALA   B 1 39  ? -22.766 33.917 -36.269 1.00 18.75 ? 61  ALA   B N   1 
ATOM   2588 C CA  . ALA   B 1 39  ? -22.793 35.134 -37.060 1.00 18.94 ? 61  ALA   B CA  1 
ATOM   2589 C C   . ALA   B 1 39  ? -23.002 34.773 -38.522 1.00 19.29 ? 61  ALA   B C   1 
ATOM   2590 O O   . ALA   B 1 39  ? -22.415 33.809 -39.026 1.00 19.90 ? 61  ALA   B O   1 
ATOM   2591 C CB  . ALA   B 1 39  ? -21.521 35.919 -36.881 1.00 18.61 ? 61  ALA   B CB  1 
ATOM   2592 N N   . SER   B 1 40  ? -23.807 35.590 -39.206 1.00 19.91 ? 62  SER   B N   1 
ATOM   2593 C CA  . SER   B 1 40  ? -24.002 35.429 -40.636 1.00 20.44 ? 62  SER   B CA  1 
ATOM   2594 C C   . SER   B 1 40  ? -23.736 36.756 -41.333 1.00 19.75 ? 62  SER   B C   1 
ATOM   2595 O O   . SER   B 1 40  ? -24.044 37.812 -40.796 1.00 20.64 ? 62  SER   B O   1 
ATOM   2596 C CB  . SER   B 1 40  ? -25.391 34.906 -40.945 1.00 21.02 ? 62  SER   B CB  1 
ATOM   2597 O OG  . SER   B 1 40  ? -26.374 35.794 -40.447 1.00 22.25 ? 62  SER   B OG  1 
ATOM   2598 N N   . SER   B 1 41  ? -23.148 36.680 -42.529 1.00 20.05 ? 63  SER   B N   1 
ATOM   2599 C CA  . SER   B 1 41  ? -22.988 37.839 -43.384 1.00 19.17 ? 63  SER   B CA  1 
ATOM   2600 C C   . SER   B 1 41  ? -23.788 37.588 -44.654 1.00 18.74 ? 63  SER   B C   1 
ATOM   2601 O O   . SER   B 1 41  ? -24.082 36.444 -44.986 1.00 18.45 ? 63  SER   B O   1 
ATOM   2602 C CB  . SER   B 1 41  ? -21.525 38.131 -43.700 1.00 18.95 ? 63  SER   B CB  1 
ATOM   2603 O OG  . SER   B 1 41  ? -20.911 37.041 -44.368 1.00 18.31 ? 63  SER   B OG  1 
ATOM   2604 N N   . SER   B 1 42  ? -24.103 38.664 -45.370 1.00 18.85 ? 64  SER   B N   1 
ATOM   2605 C CA  . SER   B 1 42  ? -24.982 38.565 -46.522 1.00 19.12 ? 64  SER   B CA  1 
ATOM   2606 C C   . SER   B 1 42  ? -24.659 39.637 -47.563 1.00 18.93 ? 64  SER   B C   1 
ATOM   2607 O O   . SER   B 1 42  ? -24.124 40.698 -47.267 1.00 18.65 ? 64  SER   B O   1 
ATOM   2608 C CB  . SER   B 1 42  ? -26.438 38.619 -46.092 1.00 19.41 ? 64  SER   B CB  1 
ATOM   2609 O OG  . SER   B 1 42  ? -27.317 38.667 -47.208 1.00 20.40 ? 64  SER   B OG  1 
ATOM   2610 N N   . ALA   B 1 43  ? -25.019 39.322 -48.803 1.00 19.11 ? 65  ALA   B N   1 
ATOM   2611 C CA  . ALA   B 1 43  ? -25.066 40.285 -49.892 1.00 20.16 ? 65  ALA   B CA  1 
ATOM   2612 C C   . ALA   B 1 43  ? -25.976 41.468 -49.562 1.00 20.26 ? 65  ALA   B C   1 
ATOM   2613 O O   . ALA   B 1 43  ? -25.854 42.519 -50.194 1.00 21.40 ? 65  ALA   B O   1 
ATOM   2614 C CB  . ALA   B 1 43  ? -25.505 39.584 -51.159 1.00 20.46 ? 65  ALA   B CB  1 
ATOM   2615 N N   . ASP   B 1 44  ? -26.869 41.301 -48.573 1.00 20.52 ? 66  ASP   B N   1 
ATOM   2616 C CA  . ASP   B 1 44  ? -27.811 42.339 -48.170 1.00 21.43 ? 66  ASP   B CA  1 
ATOM   2617 C C   . ASP   B 1 44  ? -27.153 43.430 -47.321 1.00 21.75 ? 66  ASP   B C   1 
ATOM   2618 O O   . ASP   B 1 44  ? -27.848 44.332 -46.853 1.00 20.63 ? 66  ASP   B O   1 
ATOM   2619 C CB  . ASP   B 1 44  ? -29.023 41.742 -47.463 1.00 21.84 ? 66  ASP   B CB  1 
ATOM   2620 C CG  . ASP   B 1 44  ? -28.767 41.131 -46.095 1.00 22.13 ? 66  ASP   B CG  1 
ATOM   2621 O OD1 . ASP   B 1 44  ? -27.632 41.260 -45.601 1.00 21.27 ? 66  ASP   B OD1 1 
ATOM   2622 O OD2 . ASP   B 1 44  ? -29.711 40.539 -45.543 1.00 23.27 ? 66  ASP   B OD2 1 
ATOM   2623 N N   . LYS   B 1 45  ? -25.828 43.351 -47.137 1.00 21.30 ? 67  LYS   B N   1 
ATOM   2624 C CA  . LYS   B 1 45  ? -25.031 44.358 -46.445 1.00 22.26 ? 67  LYS   B CA  1 
ATOM   2625 C C   . LYS   B 1 45  ? -25.092 44.207 -44.924 1.00 22.06 ? 67  LYS   B C   1 
ATOM   2626 O O   . LYS   B 1 45  ? -24.548 45.051 -44.203 1.00 22.93 ? 67  LYS   B O   1 
ATOM   2627 C CB  . LYS   B 1 45  ? -25.422 45.798 -46.774 1.00 24.88 ? 67  LYS   B CB  1 
ATOM   2628 C CG  . LYS   B 1 45  ? -25.592 46.121 -48.243 1.00 25.67 ? 67  LYS   B CG  1 
ATOM   2629 C CD  . LYS   B 1 45  ? -26.132 47.533 -48.370 1.00 30.09 ? 67  LYS   B CD  1 
ATOM   2630 C CE  . LYS   B 1 45  ? -26.320 47.940 -49.768 1.00 34.08 ? 67  LYS   B CE  1 
ATOM   2631 N NZ  . LYS   B 1 45  ? -26.746 49.338 -49.778 1.00 39.12 ? 67  LYS   B NZ  1 
ATOM   2632 N N   . LEU   B 1 46  ? -25.718 43.129 -44.435 1.00 21.81 ? 68  LEU   B N   1 
ATOM   2633 C CA  . LEU   B 1 46  ? -25.958 42.965 -43.009 1.00 22.78 ? 68  LEU   B CA  1 
ATOM   2634 C C   . LEU   B 1 46  ? -25.176 41.787 -42.431 1.00 22.17 ? 68  LEU   B C   1 
ATOM   2635 O O   . LEU   B 1 46  ? -24.887 40.802 -43.105 1.00 19.94 ? 68  LEU   B O   1 
ATOM   2636 C CB  . LEU   B 1 46  ? -27.450 42.747 -42.767 1.00 24.02 ? 68  LEU   B CB  1 
ATOM   2637 C CG  . LEU   B 1 46  ? -28.381 43.853 -43.261 1.00 26.38 ? 68  LEU   B CG  1 
ATOM   2638 C CD1 . LEU   B 1 46  ? -29.822 43.461 -42.938 1.00 26.89 ? 68  LEU   B CD1 1 
ATOM   2639 C CD2 . LEU   B 1 46  ? -28.006 45.212 -42.677 1.00 26.89 ? 68  LEU   B CD2 1 
ATOM   2640 N N   . ILE   B 1 47  ? -24.887 41.916 -41.138 1.00 22.34 ? 69  ILE   B N   1 
ATOM   2641 C CA  . ILE   B 1 47  ? -24.466 40.815 -40.298 1.00 21.84 ? 69  ILE   B CA  1 
ATOM   2642 C C   . ILE   B 1 47  ? -25.622 40.538 -39.343 1.00 22.16 ? 69  ILE   B C   1 
ATOM   2643 O O   . ILE   B 1 47  ? -26.179 41.462 -38.753 1.00 24.77 ? 69  ILE   B O   1 
ATOM   2644 C CB  . ILE   B 1 47  ? -23.187 41.171 -39.521 1.00 23.01 ? 69  ILE   B CB  1 
ATOM   2645 C CG1 . ILE   B 1 47  ? -22.013 41.446 -40.440 1.00 23.40 ? 69  ILE   B CG1 1 
ATOM   2646 C CG2 . ILE   B 1 47  ? -22.856 40.085 -38.497 1.00 22.46 ? 69  ILE   B CG2 1 
ATOM   2647 C CD1 . ILE   B 1 47  ? -20.953 42.317 -39.799 1.00 25.23 ? 69  ILE   B CD1 1 
ATOM   2648 N N   . LYS   B 1 48  ? -25.956 39.264 -39.167 1.00 22.99 ? 70  LYS   B N   1 
ATOM   2649 C CA  . LYS   B 1 48  ? -26.912 38.884 -38.144 1.00 24.01 ? 70  LYS   B CA  1 
ATOM   2650 C C   . LYS   B 1 48  ? -26.273 37.907 -37.157 1.00 24.81 ? 70  LYS   B C   1 
ATOM   2651 O O   . LYS   B 1 48  ? -25.420 37.096 -37.528 1.00 23.20 ? 70  LYS   B O   1 
ATOM   2652 C CB  . LYS   B 1 48  ? -28.188 38.379 -38.821 1.00 24.79 ? 70  LYS   B CB  1 
ATOM   2653 C CG  . LYS   B 1 48  ? -28.962 39.449 -39.567 1.00 25.51 ? 70  LYS   B CG  1 
ATOM   2654 C CD  . LYS   B 1 48  ? -30.144 38.901 -40.359 1.00 26.00 ? 70  LYS   B CD  1 
ATOM   2655 C CE  . LYS   B 1 48  ? -30.843 39.972 -41.145 1.00 26.94 ? 70  LYS   B CE  1 
ATOM   2656 N NZ  . LYS   B 1 48  ? -31.662 40.841 -40.288 1.00 27.13 ? 70  LYS   B NZ  1 
ATOM   2657 N N   . ILE   B 1 49  ? -26.727 38.024 -35.898 1.00 24.47 ? 71  ILE   B N   1 
ATOM   2658 C CA  . ILE   B 1 49  ? -26.278 37.210 -34.780 1.00 24.13 ? 71  ILE   B CA  1 
ATOM   2659 C C   . ILE   B 1 49  ? -27.464 36.383 -34.316 1.00 24.89 ? 71  ILE   B C   1 
ATOM   2660 O O   . ILE   B 1 49  ? -28.561 36.913 -34.138 1.00 26.30 ? 71  ILE   B O   1 
ATOM   2661 C CB  . ILE   B 1 49  ? -25.731 38.066 -33.628 1.00 24.14 ? 71  ILE   B CB  1 
ATOM   2662 C CG1 . ILE   B 1 49  ? -24.688 39.067 -34.098 1.00 23.41 ? 71  ILE   B CG1 1 
ATOM   2663 C CG2 . ILE   B 1 49  ? -25.211 37.181 -32.488 1.00 25.04 ? 71  ILE   B CG2 1 
ATOM   2664 C CD1 . ILE   B 1 49  ? -23.434 38.441 -34.680 1.00 23.46 ? 71  ILE   B CD1 1 
ATOM   2665 N N   . TRP   B 1 50  ? -27.217 35.083 -34.150 1.00 24.53 ? 72  TRP   B N   1 
ATOM   2666 C CA  . TRP   B 1 50  ? -28.249 34.126 -33.802 1.00 24.18 ? 72  TRP   B CA  1 
ATOM   2667 C C   . TRP   B 1 50  ? -27.748 33.271 -32.648 1.00 23.23 ? 72  TRP   B C   1 
ATOM   2668 O O   . TRP   B 1 50  ? -26.571 32.946 -32.594 1.00 23.77 ? 72  TRP   B O   1 
ATOM   2669 C CB  . TRP   B 1 50  ? -28.581 33.204 -34.980 1.00 24.34 ? 72  TRP   B CB  1 
ATOM   2670 C CG  . TRP   B 1 50  ? -28.702 33.863 -36.326 1.00 25.16 ? 72  TRP   B CG  1 
ATOM   2671 C CD1 . TRP   B 1 50  ? -27.666 34.206 -37.135 1.00 24.13 ? 72  TRP   B CD1 1 
ATOM   2672 C CD2 . TRP   B 1 50  ? -29.910 34.215 -37.034 1.00 25.47 ? 72  TRP   B CD2 1 
ATOM   2673 N NE1 . TRP   B 1 50  ? -28.130 34.759 -38.296 1.00 25.57 ? 72  TRP   B NE1 1 
ATOM   2674 C CE2 . TRP   B 1 50  ? -29.503 34.775 -38.265 1.00 25.31 ? 72  TRP   B CE2 1 
ATOM   2675 C CE3 . TRP   B 1 50  ? -31.276 34.110 -36.754 1.00 26.97 ? 72  TRP   B CE3 1 
ATOM   2676 C CZ2 . TRP   B 1 50  ? -30.412 35.226 -39.210 1.00 25.85 ? 72  TRP   B CZ2 1 
ATOM   2677 C CZ3 . TRP   B 1 50  ? -32.175 34.579 -37.683 1.00 28.14 ? 72  TRP   B CZ3 1 
ATOM   2678 C CH2 . TRP   B 1 50  ? -31.746 35.122 -38.893 1.00 27.33 ? 72  TRP   B CH2 1 
ATOM   2679 N N   . GLY   B 1 51  ? -28.659 32.858 -31.760 1.00 23.81 ? 73  GLY   B N   1 
ATOM   2680 C CA  . GLY   B 1 51  ? -28.331 31.860 -30.754 1.00 24.35 ? 73  GLY   B CA  1 
ATOM   2681 C C   . GLY   B 1 51  ? -27.924 30.538 -31.403 1.00 24.27 ? 73  GLY   B C   1 
ATOM   2682 O O   . GLY   B 1 51  ? -28.649 30.000 -32.234 1.00 25.54 ? 73  GLY   B O   1 
ATOM   2683 N N   . ALA   B 1 52  ? -26.752 30.022 -31.013 1.00 23.59 ? 74  ALA   B N   1 
ATOM   2684 C CA  . ALA   B 1 52  ? -26.185 28.816 -31.601 1.00 24.72 ? 74  ALA   B CA  1 
ATOM   2685 C C   . ALA   B 1 52  ? -27.018 27.575 -31.287 1.00 25.40 ? 74  ALA   B C   1 
ATOM   2686 O O   . ALA   B 1 52  ? -26.946 26.587 -32.019 1.00 25.99 ? 74  ALA   B O   1 
ATOM   2687 C CB  . ALA   B 1 52  ? -24.778 28.620 -31.082 1.00 25.92 ? 74  ALA   B CB  1 
ATOM   2688 N N   . TYR   B 1 53  ? -27.721 27.593 -30.146 1.00 24.84 ? 75  TYR   B N   1 
ATOM   2689 C CA  . TYR   B 1 53  ? -28.315 26.376 -29.624 1.00 26.38 ? 75  TYR   B CA  1 
ATOM   2690 C C   . TYR   B 1 53  ? -29.796 26.313 -29.977 1.00 27.65 ? 75  TYR   B C   1 
ATOM   2691 O O   . TYR   B 1 53  ? -30.319 25.223 -30.197 1.00 29.08 ? 75  TYR   B O   1 
ATOM   2692 C CB  . TYR   B 1 53  ? -28.083 26.252 -28.115 1.00 26.32 ? 75  TYR   B CB  1 
ATOM   2693 C CG  . TYR   B 1 53  ? -26.605 26.172 -27.746 1.00 25.67 ? 75  TYR   B CG  1 
ATOM   2694 C CD1 . TYR   B 1 53  ? -25.830 25.074 -28.105 1.00 26.85 ? 75  TYR   B CD1 1 
ATOM   2695 C CD2 . TYR   B 1 53  ? -25.983 27.192 -27.038 1.00 25.88 ? 75  TYR   B CD2 1 
ATOM   2696 C CE1 . TYR   B 1 53  ? -24.476 25.008 -27.806 1.00 26.36 ? 75  TYR   B CE1 1 
ATOM   2697 C CE2 . TYR   B 1 53  ? -24.639 27.121 -26.700 1.00 25.57 ? 75  TYR   B CE2 1 
ATOM   2698 C CZ  . TYR   B 1 53  ? -23.882 26.021 -27.071 1.00 25.83 ? 75  TYR   B CZ  1 
ATOM   2699 O OH  . TYR   B 1 53  ? -22.550 25.977 -26.746 1.00 25.73 ? 75  TYR   B OH  1 
ATOM   2700 N N   . ASP   B 1 54  ? -30.472 27.467 -29.976 1.00 27.54 ? 76  ASP   B N   1 
ATOM   2701 C CA  . ASP   B 1 54  ? -31.907 27.496 -30.211 1.00 30.41 ? 76  ASP   B CA  1 
ATOM   2702 C C   . ASP   B 1 54  ? -32.264 28.281 -31.473 1.00 29.99 ? 76  ASP   B C   1 
ATOM   2703 O O   . ASP   B 1 54  ? -33.443 28.382 -31.808 1.00 29.37 ? 76  ASP   B O   1 
ATOM   2704 C CB  . ASP   B 1 54  ? -32.647 28.071 -29.018 1.00 31.69 ? 76  ASP   B CB  1 
ATOM   2705 C CG  . ASP   B 1 54  ? -32.233 29.482 -28.619 1.00 32.92 ? 76  ASP   B CG  1 
ATOM   2706 O OD1 . ASP   B 1 54  ? -31.531 30.141 -29.415 1.00 32.20 ? 76  ASP   B OD1 1 
ATOM   2707 O OD2 . ASP   B 1 54  ? -32.600 29.891 -27.497 1.00 36.44 ? 76  ASP   B OD2 1 
ATOM   2708 N N   . GLY   B 1 55  ? -31.260 28.864 -32.148 1.00 30.73 ? 77  GLY   B N   1 
ATOM   2709 C CA  . GLY   B 1 55  ? -31.484 29.548 -33.411 1.00 30.63 ? 77  GLY   B CA  1 
ATOM   2710 C C   . GLY   B 1 55  ? -32.191 30.899 -33.273 1.00 31.25 ? 77  GLY   B C   1 
ATOM   2711 O O   . GLY   B 1 55  ? -32.563 31.490 -34.286 1.00 33.55 ? 77  GLY   B O   1 
ATOM   2712 N N   . LYS   B 1 56  ? -32.328 31.429 -32.050 1.00 30.42 ? 78  LYS   B N   1 
ATOM   2713 C CA  . LYS   B 1 56  ? -33.154 32.618 -31.850 1.00 30.31 ? 78  LYS   B CA  1 
ATOM   2714 C C   . LYS   B 1 56  ? -32.392 33.832 -32.375 1.00 29.73 ? 78  LYS   B C   1 
ATOM   2715 O O   . LYS   B 1 56  ? -31.205 34.002 -32.105 1.00 29.16 ? 78  LYS   B O   1 
ATOM   2716 C CB  . LYS   B 1 56  ? -33.615 32.799 -30.394 1.00 31.41 ? 78  LYS   B CB  1 
ATOM   2717 N N   . PHE   B 1 57  ? -33.087 34.675 -33.140 1.00 30.22 ? 79  PHE   B N   1 
ATOM   2718 C CA  . PHE   B 1 57  ? -32.470 35.861 -33.702 1.00 29.87 ? 79  PHE   B CA  1 
ATOM   2719 C C   . PHE   B 1 57  ? -32.079 36.776 -32.546 1.00 29.70 ? 79  PHE   B C   1 
ATOM   2720 O O   . PHE   B 1 57  ? -32.888 37.010 -31.656 1.00 30.40 ? 79  PHE   B O   1 
ATOM   2721 C CB  . PHE   B 1 57  ? -33.401 36.541 -34.710 1.00 31.37 ? 79  PHE   B CB  1 
ATOM   2722 C CG  . PHE   B 1 57  ? -32.935 37.933 -35.116 1.00 31.45 ? 79  PHE   B CG  1 
ATOM   2723 C CD1 . PHE   B 1 57  ? -31.929 38.101 -36.062 1.00 31.67 ? 79  PHE   B CD1 1 
ATOM   2724 C CD2 . PHE   B 1 57  ? -33.472 39.066 -34.516 1.00 32.18 ? 79  PHE   B CD2 1 
ATOM   2725 C CE1 . PHE   B 1 57  ? -31.492 39.374 -36.412 1.00 32.13 ? 79  PHE   B CE1 1 
ATOM   2726 C CE2 . PHE   B 1 57  ? -33.040 40.333 -34.872 1.00 31.90 ? 79  PHE   B CE2 1 
ATOM   2727 C CZ  . PHE   B 1 57  ? -32.051 40.486 -35.816 1.00 32.38 ? 79  PHE   B CZ  1 
ATOM   2728 N N   . GLU   B 1 58  ? -30.833 37.268 -32.557 1.00 30.61 ? 80  GLU   B N   1 
ATOM   2729 C CA  . GLU   B 1 58  ? -30.347 38.167 -31.521 1.00 31.64 ? 80  GLU   B CA  1 
ATOM   2730 C C   . GLU   B 1 58  ? -30.351 39.614 -32.025 1.00 31.52 ? 80  GLU   B C   1 
ATOM   2731 O O   . GLU   B 1 58  ? -31.022 40.455 -31.433 1.00 33.69 ? 80  GLU   B O   1 
ATOM   2732 C CB  . GLU   B 1 58  ? -28.980 37.710 -31.005 1.00 31.66 ? 80  GLU   B CB  1 
ATOM   2733 C CG  . GLU   B 1 58  ? -28.422 38.585 -29.881 1.00 34.64 ? 80  GLU   B CG  1 
ATOM   2734 C CD  . GLU   B 1 58  ? -29.149 38.556 -28.540 1.00 38.01 ? 80  GLU   B CD  1 
ATOM   2735 O OE1 . GLU   B 1 58  ? -29.982 37.651 -28.303 1.00 37.81 ? 80  GLU   B OE1 1 
ATOM   2736 O OE2 . GLU   B 1 58  ? -28.866 39.450 -27.706 1.00 41.20 ? 80  GLU   B OE2 1 
ATOM   2737 N N   . LYS   B 1 59  ? -29.602 39.917 -33.098 1.00 30.48 ? 81  LYS   B N   1 
ATOM   2738 C CA  . LYS   B 1 59  ? -29.478 41.291 -33.569 1.00 29.45 ? 81  LYS   B CA  1 
ATOM   2739 C C   . LYS   B 1 59  ? -28.925 41.355 -34.993 1.00 28.74 ? 81  LYS   B C   1 
ATOM   2740 O O   . LYS   B 1 59  ? -28.334 40.398 -35.490 1.00 27.77 ? 81  LYS   B O   1 
ATOM   2741 C CB  . LYS   B 1 59  ? -28.567 42.147 -32.682 1.00 29.91 ? 81  LYS   B CB  1 
ATOM   2742 C CG  . LYS   B 1 59  ? -27.094 41.728 -32.644 1.00 33.41 ? 81  LYS   B CG  1 
ATOM   2743 C CD  . LYS   B 1 59  ? -26.187 42.600 -31.774 1.00 35.91 ? 81  LYS   B CD  1 
ATOM   2744 C CE  . LYS   B 1 59  ? -26.339 42.327 -30.315 1.00 37.89 ? 81  LYS   B CE  1 
ATOM   2745 N NZ  . LYS   B 1 59  ? -25.372 43.107 -29.544 1.00 39.27 ? 81  LYS   B NZ  1 
ATOM   2746 N N   . THR   B 1 60  ? -29.136 42.524 -35.615 1.00 28.78 ? 82  THR   B N   1 
ATOM   2747 C CA  . THR   B 1 60  ? -28.550 42.898 -36.893 1.00 28.26 ? 82  THR   B CA  1 
ATOM   2748 C C   . THR   B 1 60  ? -27.475 43.954 -36.647 1.00 27.93 ? 82  THR   B C   1 
ATOM   2749 O O   . THR   B 1 60  ? -27.661 44.878 -35.857 1.00 28.03 ? 82  THR   B O   1 
ATOM   2750 C CB  . THR   B 1 60  ? -29.637 43.440 -37.826 1.00 28.86 ? 82  THR   B CB  1 
ATOM   2751 O OG1 . THR   B 1 60  ? -30.598 42.403 -38.028 1.00 28.47 ? 82  THR   B OG1 1 
ATOM   2752 C CG2 . THR   B 1 60  ? -29.087 43.859 -39.177 1.00 29.93 ? 82  THR   B CG2 1 
ATOM   2753 N N   . ILE   B 1 61  ? -26.340 43.793 -37.323 1.00 26.17 ? 83  ILE   B N   1 
ATOM   2754 C CA  . ILE   B 1 61  ? -25.266 44.767 -37.281 1.00 26.43 ? 83  ILE   B CA  1 
ATOM   2755 C C   . ILE   B 1 61  ? -25.092 45.327 -38.692 1.00 26.36 ? 83  ILE   B C   1 
ATOM   2756 O O   . ILE   B 1 61  ? -24.903 44.568 -39.646 1.00 24.99 ? 83  ILE   B O   1 
ATOM   2757 C CB  . ILE   B 1 61  ? -23.984 44.108 -36.747 1.00 26.27 ? 83  ILE   B CB  1 
ATOM   2758 C CG1 . ILE   B 1 61  ? -24.158 43.686 -35.283 1.00 27.19 ? 83  ILE   B CG1 1 
ATOM   2759 C CG2 . ILE   B 1 61  ? -22.784 45.034 -36.947 1.00 26.99 ? 83  ILE   B CG2 1 
ATOM   2760 C CD1 . ILE   B 1 61  ? -23.037 42.808 -34.745 1.00 27.51 ? 83  ILE   B CD1 1 
ATOM   2761 N N   . SER   B 1 62  ? -25.122 46.657 -38.805 1.00 26.59 ? 84  SER   B N   1 
ATOM   2762 C CA  . SER   B 1 62  ? -25.156 47.314 -40.098 1.00 27.14 ? 84  SER   B CA  1 
ATOM   2763 C C   . SER   B 1 62  ? -24.157 48.472 -40.138 1.00 25.46 ? 84  SER   B C   1 
ATOM   2764 O O   . SER   B 1 62  ? -23.770 49.022 -39.108 1.00 24.98 ? 84  SER   B O   1 
ATOM   2765 C CB  . SER   B 1 62  ? -26.560 47.775 -40.457 1.00 30.49 ? 84  SER   B CB  1 
ATOM   2766 O OG  . SER   B 1 62  ? -27.106 48.638 -39.472 1.00 34.06 ? 84  SER   B OG  1 
ATOM   2767 N N   . GLY   B 1 63  ? -23.763 48.842 -41.358 1.00 24.97 ? 85  GLY   B N   1 
ATOM   2768 C CA  . GLY   B 1 63  ? -22.867 49.966 -41.580 1.00 25.03 ? 85  GLY   B CA  1 
ATOM   2769 C C   . GLY   B 1 63  ? -22.155 49.887 -42.930 1.00 25.11 ? 85  GLY   B C   1 
ATOM   2770 O O   . GLY   B 1 63  ? -21.805 50.914 -43.501 1.00 28.81 ? 85  GLY   B O   1 
ATOM   2771 N N   . HIS   B 1 64  ? -21.869 48.679 -43.415 1.00 24.16 ? 86  HIS   B N   1 
ATOM   2772 C CA  . HIS   B 1 64  ? -21.268 48.549 -44.734 1.00 24.22 ? 86  HIS   B CA  1 
ATOM   2773 C C   . HIS   B 1 64  ? -22.222 49.075 -45.798 1.00 24.75 ? 86  HIS   B C   1 
ATOM   2774 O O   . HIS   B 1 64  ? -23.435 48.913 -45.700 1.00 25.89 ? 86  HIS   B O   1 
ATOM   2775 C CB  . HIS   B 1 64  ? -20.919 47.096 -45.068 1.00 21.88 ? 86  HIS   B CB  1 
ATOM   2776 C CG  . HIS   B 1 64  ? -19.651 46.598 -44.459 1.00 20.00 ? 86  HIS   B CG  1 
ATOM   2777 N ND1 . HIS   B 1 64  ? -18.425 47.116 -44.822 1.00 18.45 ? 86  HIS   B ND1 1 
ATOM   2778 C CD2 . HIS   B 1 64  ? -19.399 45.646 -43.544 1.00 19.36 ? 86  HIS   B CD2 1 
ATOM   2779 C CE1 . HIS   B 1 64  ? -17.467 46.470 -44.169 1.00 18.60 ? 86  HIS   B CE1 1 
ATOM   2780 N NE2 . HIS   B 1 64  ? -18.030 45.557 -43.401 1.00 18.75 ? 86  HIS   B NE2 1 
ATOM   2781 N N   . LYS   B 1 65  ? -21.653 49.648 -46.854 1.00 25.58 ? 87  LYS   B N   1 
ATOM   2782 C CA  . LYS   B 1 65  ? -22.462 50.334 -47.845 1.00 26.78 ? 87  LYS   B CA  1 
ATOM   2783 C C   . LYS   B 1 65  ? -22.710 49.426 -49.048 1.00 24.80 ? 87  LYS   B C   1 
ATOM   2784 O O   . LYS   B 1 65  ? -23.512 49.753 -49.916 1.00 25.03 ? 87  LYS   B O   1 
ATOM   2785 C CB  . LYS   B 1 65  ? -21.791 51.669 -48.183 1.00 31.34 ? 87  LYS   B CB  1 
ATOM   2786 C CG  . LYS   B 1 65  ? -22.021 52.776 -47.149 1.00 34.86 ? 87  LYS   B CG  1 
ATOM   2787 C CD  . LYS   B 1 65  ? -21.265 54.064 -47.461 1.00 38.56 ? 87  LYS   B CD  1 
ATOM   2788 N N   . LEU   B 1 66  ? -22.008 48.292 -49.096 1.00 23.31 ? 88  LEU   B N   1 
ATOM   2789 C CA  . LEU   B 1 66  ? -22.257 47.274 -50.096 1.00 21.77 ? 88  LEU   B CA  1 
ATOM   2790 C C   . LEU   B 1 66  ? -22.233 45.927 -49.393 1.00 20.61 ? 88  LEU   B C   1 
ATOM   2791 O O   . LEU   B 1 66  ? -21.993 45.863 -48.184 1.00 20.96 ? 88  LEU   B O   1 
ATOM   2792 C CB  . LEU   B 1 66  ? -21.210 47.365 -51.208 1.00 21.94 ? 88  LEU   B CB  1 
ATOM   2793 C CG  . LEU   B 1 66  ? -21.286 48.607 -52.101 1.00 21.85 ? 88  LEU   B CG  1 
ATOM   2794 C CD1 . LEU   B 1 66  ? -20.074 48.664 -53.019 1.00 21.89 ? 88  LEU   B CD1 1 
ATOM   2795 C CD2 . LEU   B 1 66  ? -22.570 48.635 -52.923 1.00 20.59 ? 88  LEU   B CD2 1 
ATOM   2796 N N   . GLY   B 1 67  ? -22.474 44.860 -50.158 1.00 19.84 ? 89  GLY   B N   1 
ATOM   2797 C CA  . GLY   B 1 67  ? -22.574 43.520 -49.598 1.00 19.18 ? 89  GLY   B CA  1 
ATOM   2798 C C   . GLY   B 1 67  ? -21.301 43.082 -48.869 1.00 18.96 ? 89  GLY   B C   1 
ATOM   2799 O O   . GLY   B 1 67  ? -20.211 43.619 -49.090 1.00 18.99 ? 89  GLY   B O   1 
ATOM   2800 N N   . ILE   B 1 68  ? -21.484 42.060 -48.026 1.00 18.34 ? 90  ILE   B N   1 
ATOM   2801 C CA  . ILE   B 1 68  ? -20.428 41.433 -47.248 1.00 17.93 ? 90  ILE   B CA  1 
ATOM   2802 C C   . ILE   B 1 68  ? -20.227 39.996 -47.727 1.00 17.38 ? 90  ILE   B C   1 
ATOM   2803 O O   . ILE   B 1 68  ? -21.189 39.225 -47.843 1.00 18.46 ? 90  ILE   B O   1 
ATOM   2804 C CB  . ILE   B 1 68  ? -20.804 41.461 -45.756 1.00 19.41 ? 90  ILE   B CB  1 
ATOM   2805 C CG1 . ILE   B 1 68  ? -21.205 42.878 -45.279 1.00 20.74 ? 90  ILE   B CG1 1 
ATOM   2806 C CG2 . ILE   B 1 68  ? -19.691 40.851 -44.892 1.00 19.93 ? 90  ILE   B CG2 1 
ATOM   2807 C CD1 . ILE   B 1 68  ? -21.811 42.901 -43.880 1.00 22.14 ? 90  ILE   B CD1 1 
ATOM   2808 N N   . SER   B 1 69  ? -18.958 39.620 -47.904 1.00 16.31 ? 91  SER   B N   1 
ATOM   2809 C CA  . SER   B 1 69  ? -18.579 38.304 -48.393 1.00 16.65 ? 91  SER   B CA  1 
ATOM   2810 C C   . SER   B 1 69  ? -18.227 37.381 -47.231 1.00 16.81 ? 91  SER   B C   1 
ATOM   2811 O O   . SER   B 1 69  ? -18.349 36.174 -47.369 1.00 17.59 ? 91  SER   B O   1 
ATOM   2812 C CB  . SER   B 1 69  ? -17.400 38.375 -49.362 1.00 17.47 ? 91  SER   B CB  1 
ATOM   2813 O OG  . SER   B 1 69  ? -17.756 38.998 -50.585 1.00 17.54 ? 91  SER   B OG  1 
ATOM   2814 N N   . ASP   B 1 70  ? -17.739 37.942 -46.110 1.00 16.69 ? 92  ASP   B N   1 
ATOM   2815 C CA  . ASP   B 1 70  ? -17.174 37.121 -45.051 1.00 16.73 ? 92  ASP   B CA  1 
ATOM   2816 C C   . ASP   B 1 70  ? -17.218 37.853 -43.711 1.00 16.75 ? 92  ASP   B C   1 
ATOM   2817 O O   . ASP   B 1 70  ? -17.249 39.078 -43.636 1.00 16.18 ? 92  ASP   B O   1 
ATOM   2818 C CB  . ASP   B 1 70  ? -15.755 36.683 -45.421 1.00 16.95 ? 92  ASP   B CB  1 
ATOM   2819 C CG  . ASP   B 1 70  ? -15.197 35.460 -44.705 1.00 16.75 ? 92  ASP   B CG  1 
ATOM   2820 O OD1 . ASP   B 1 70  ? -15.973 34.785 -43.991 1.00 17.17 ? 92  ASP   B OD1 1 
ATOM   2821 O OD2 . ASP   B 1 70  ? -13.981 35.170 -44.890 1.00 14.69 ? 92  ASP   B OD2 1 
ATOM   2822 N N   . VAL   B 1 71  ? -17.191 37.058 -42.646 1.00 16.36 ? 93  VAL   B N   1 
ATOM   2823 C CA  . VAL   B 1 71  ? -17.167 37.562 -41.285 1.00 17.03 ? 93  VAL   B CA  1 
ATOM   2824 C C   . VAL   B 1 71  ? -16.342 36.574 -40.456 1.00 16.87 ? 93  VAL   B C   1 
ATOM   2825 O O   . VAL   B 1 71  ? -16.309 35.386 -40.771 1.00 17.37 ? 93  VAL   B O   1 
ATOM   2826 C CB  . VAL   B 1 71  ? -18.614 37.750 -40.774 1.00 19.01 ? 93  VAL   B CB  1 
ATOM   2827 C CG1 . VAL   B 1 71  ? -19.366 36.427 -40.627 1.00 20.02 ? 93  VAL   B CG1 1 
ATOM   2828 C CG2 . VAL   B 1 71  ? -18.665 38.542 -39.478 1.00 21.01 ? 93  VAL   B CG2 1 
ATOM   2829 N N   . ALA   B 1 72  ? -15.730 37.056 -39.368 1.00 16.32 ? 94  ALA   B N   1 
ATOM   2830 C CA  . ALA   B 1 72  ? -14.904 36.236 -38.508 1.00 16.29 ? 94  ALA   B CA  1 
ATOM   2831 C C   . ALA   B 1 72  ? -14.902 36.808 -37.093 1.00 15.99 ? 94  ALA   B C   1 
ATOM   2832 O O   . ALA   B 1 72  ? -15.014 38.010 -36.899 1.00 16.91 ? 94  ALA   B O   1 
ATOM   2833 C CB  . ALA   B 1 72  ? -13.501 36.126 -39.053 1.00 16.72 ? 94  ALA   B CB  1 
ATOM   2834 N N   . TRP   B 1 73  ? -14.770 35.912 -36.114 1.00 16.59 ? 95  TRP   B N   1 
ATOM   2835 C CA  . TRP   B 1 73  ? -14.800 36.245 -34.699 1.00 16.91 ? 95  TRP   B CA  1 
ATOM   2836 C C   . TRP   B 1 73  ? -13.401 36.343 -34.108 1.00 16.23 ? 95  TRP   B C   1 
ATOM   2837 O O   . TRP   B 1 73  ? -12.536 35.526 -34.425 1.00 15.65 ? 95  TRP   B O   1 
ATOM   2838 C CB  . TRP   B 1 73  ? -15.513 35.146 -33.910 1.00 17.30 ? 95  TRP   B CB  1 
ATOM   2839 C CG  . TRP   B 1 73  ? -16.984 34.981 -34.166 1.00 18.32 ? 95  TRP   B CG  1 
ATOM   2840 C CD1 . TRP   B 1 73  ? -17.581 34.194 -35.111 1.00 19.02 ? 95  TRP   B CD1 1 
ATOM   2841 C CD2 . TRP   B 1 73  ? -18.050 35.557 -33.383 1.00 18.61 ? 95  TRP   B CD2 1 
ATOM   2842 N NE1 . TRP   B 1 73  ? -18.947 34.261 -34.996 1.00 18.14 ? 95  TRP   B NE1 1 
ATOM   2843 C CE2 . TRP   B 1 73  ? -19.262 35.092 -33.952 1.00 18.98 ? 95  TRP   B CE2 1 
ATOM   2844 C CE3 . TRP   B 1 73  ? -18.099 36.425 -32.285 1.00 18.10 ? 95  TRP   B CE3 1 
ATOM   2845 C CZ2 . TRP   B 1 73  ? -20.502 35.454 -33.433 1.00 19.38 ? 95  TRP   B CZ2 1 
ATOM   2846 C CZ3 . TRP   B 1 73  ? -19.332 36.781 -31.773 1.00 18.95 ? 95  TRP   B CZ3 1 
ATOM   2847 C CH2 . TRP   B 1 73  ? -20.511 36.293 -32.338 1.00 19.81 ? 95  TRP   B CH2 1 
ATOM   2848 N N   . SER   B 1 74  ? -13.244 37.240 -33.129 1.00 16.47 ? 96  SER   B N   1 
ATOM   2849 C CA  . SER   B 1 74  ? -12.077 37.209 -32.252 1.00 17.42 ? 96  SER   B CA  1 
ATOM   2850 C C   . SER   B 1 74  ? -12.180 36.015 -31.300 1.00 17.70 ? 96  SER   B C   1 
ATOM   2851 O O   . SER   B 1 74  ? -13.270 35.517 -31.023 1.00 17.54 ? 96  SER   B O   1 
ATOM   2852 C CB  . SER   B 1 74  ? -11.913 38.503 -31.496 1.00 18.06 ? 96  SER   B CB  1 
ATOM   2853 O OG  . SER   B 1 74  ? -13.033 38.736 -30.654 1.00 20.04 ? 96  SER   B OG  1 
ATOM   2854 N N   . SER   B 1 75  ? -11.035 35.590 -30.765 1.00 17.37 ? 97  SER   B N   1 
ATOM   2855 C CA  . SER   B 1 75  ? -10.973 34.429 -29.891 1.00 18.18 ? 97  SER   B CA  1 
ATOM   2856 C C   . SER   B 1 75  ? -11.806 34.599 -28.615 1.00 18.58 ? 97  SER   B C   1 
ATOM   2857 O O   . SER   B 1 75  ? -12.318 33.616 -28.085 1.00 19.22 ? 97  SER   B O   1 
ATOM   2858 C CB  . SER   B 1 75  ? -9.554  34.097 -29.578 1.00 18.75 ? 97  SER   B CB  1 
ATOM   2859 O OG  . SER   B 1 75  ? -8.914  33.549 -30.722 1.00 19.77 ? 97  SER   B OG  1 
ATOM   2860 N N   . ASP   B 1 76  ? -11.965 35.834 -28.122 1.00 18.24 ? 98  ASP   B N   1 
ATOM   2861 C CA  . ASP   B 1 76  ? -12.758 36.071 -26.922 1.00 18.98 ? 98  ASP   B CA  1 
ATOM   2862 C C   . ASP   B 1 76  ? -14.243 36.283 -27.232 1.00 19.01 ? 98  ASP   B C   1 
ATOM   2863 O O   . ASP   B 1 76  ? -15.020 36.615 -26.323 1.00 20.29 ? 98  ASP   B O   1 
ATOM   2864 C CB  . ASP   B 1 76  ? -12.202 37.234 -26.119 1.00 20.50 ? 98  ASP   B CB  1 
ATOM   2865 C CG  . ASP   B 1 76  ? -12.328 38.617 -26.739 1.00 21.47 ? 98  ASP   B CG  1 
ATOM   2866 O OD1 . ASP   B 1 76  ? -12.879 38.719 -27.866 1.00 21.78 ? 98  ASP   B OD1 1 
ATOM   2867 O OD2 . ASP   B 1 76  ? -11.855 39.585 -26.081 1.00 23.45 ? 98  ASP   B OD2 1 
ATOM   2868 N N   . SER   B 1 77  ? -14.628 36.101 -28.503 1.00 19.31 ? 99  SER   B N   1 
ATOM   2869 C CA  . SER   B 1 77  ? -16.005 36.212 -28.970 1.00 19.82 ? 99  SER   B CA  1 
ATOM   2870 C C   . SER   B 1 77  ? -16.589 37.622 -28.831 1.00 21.38 ? 99  SER   B C   1 
ATOM   2871 O O   . SER   B 1 77  ? -17.804 37.781 -28.989 1.00 22.48 ? 99  SER   B O   1 
ATOM   2872 C CB  . SER   B 1 77  ? -16.914 35.207 -28.278 1.00 19.89 ? 99  SER   B CB  1 
ATOM   2873 O OG  . SER   B 1 77  ? -16.471 33.863 -28.449 1.00 20.71 ? 99  SER   B OG  1 
ATOM   2874 N N   . ASN   B 1 78  ? -15.760 38.649 -28.567 1.00 21.75 ? 100 ASN   B N   1 
ATOM   2875 C CA  . ASN   B 1 78  ? -16.263 39.998 -28.324 1.00 23.18 ? 100 ASN   B CA  1 
ATOM   2876 C C   . ASN   B 1 78  ? -16.250 40.869 -29.585 1.00 23.33 ? 100 ASN   B C   1 
ATOM   2877 O O   . ASN   B 1 78  ? -16.971 41.865 -29.645 1.00 25.28 ? 100 ASN   B O   1 
ATOM   2878 C CB  . ASN   B 1 78  ? -15.490 40.703 -27.214 1.00 24.95 ? 100 ASN   B CB  1 
ATOM   2879 C CG  . ASN   B 1 78  ? -15.808 40.134 -25.851 1.00 26.90 ? 100 ASN   B CG  1 
ATOM   2880 O OD1 . ASN   B 1 78  ? -16.942 39.705 -25.604 1.00 26.69 ? 100 ASN   B OD1 1 
ATOM   2881 N ND2 . ASN   B 1 78  ? -14.837 40.127 -24.953 1.00 26.79 ? 100 ASN   B ND2 1 
ATOM   2882 N N   . LEU   B 1 79  ? -15.427 40.504 -30.576 1.00 20.67 ? 101 LEU   B N   1 
ATOM   2883 C CA  . LEU   B 1 79  ? -15.291 41.278 -31.806 1.00 20.69 ? 101 LEU   B CA  1 
ATOM   2884 C C   . LEU   B 1 79  ? -15.658 40.430 -33.017 1.00 19.68 ? 101 LEU   B C   1 
ATOM   2885 O O   . LEU   B 1 79  ? -15.444 39.220 -33.032 1.00 18.31 ? 101 LEU   B O   1 
ATOM   2886 C CB  . LEU   B 1 79  ? -13.855 41.778 -31.957 1.00 21.75 ? 101 LEU   B CB  1 
ATOM   2887 C CG  . LEU   B 1 79  ? -13.301 42.611 -30.801 1.00 22.46 ? 101 LEU   B CG  1 
ATOM   2888 C CD1 . LEU   B 1 79  ? -11.879 42.995 -31.114 1.00 24.08 ? 101 LEU   B CD1 1 
ATOM   2889 C CD2 . LEU   B 1 79  ? -14.137 43.851 -30.532 1.00 23.96 ? 101 LEU   B CD2 1 
ATOM   2890 N N   . LEU   B 1 80  ? -16.147 41.116 -34.054 1.00 20.17 ? 102 LEU   B N   1 
ATOM   2891 C CA  . LEU   B 1 80  ? -16.277 40.554 -35.388 1.00 20.22 ? 102 LEU   B CA  1 
ATOM   2892 C C   . LEU   B 1 80  ? -15.484 41.425 -36.347 1.00 19.71 ? 102 LEU   B C   1 
ATOM   2893 O O   . LEU   B 1 80  ? -15.335 42.626 -36.122 1.00 20.15 ? 102 LEU   B O   1 
ATOM   2894 C CB  . LEU   B 1 80  ? -17.734 40.508 -35.838 1.00 21.75 ? 102 LEU   B CB  1 
ATOM   2895 C CG  . LEU   B 1 80  ? -18.618 39.487 -35.117 1.00 24.48 ? 102 LEU   B CG  1 
ATOM   2896 C CD1 . LEU   B 1 80  ? -20.088 39.881 -35.219 1.00 26.47 ? 102 LEU   B CD1 1 
ATOM   2897 C CD2 . LEU   B 1 80  ? -18.419 38.101 -35.667 1.00 25.06 ? 102 LEU   B CD2 1 
ATOM   2898 N N   . VAL   B 1 81  ? -15.007 40.802 -37.421 1.00 18.46 ? 103 VAL   B N   1 
ATOM   2899 C CA  . VAL   B 1 81  ? -14.496 41.543 -38.560 1.00 17.89 ? 103 VAL   B CA  1 
ATOM   2900 C C   . VAL   B 1 81  ? -15.323 41.107 -39.762 1.00 17.86 ? 103 VAL   B C   1 
ATOM   2901 O O   . VAL   B 1 81  ? -15.648 39.938 -39.875 1.00 18.91 ? 103 VAL   B O   1 
ATOM   2902 C CB  . VAL   B 1 81  ? -12.984 41.370 -38.814 1.00 18.33 ? 103 VAL   B CB  1 
ATOM   2903 C CG1 . VAL   B 1 81  ? -12.590 39.922 -39.091 1.00 17.40 ? 103 VAL   B CG1 1 
ATOM   2904 C CG2 . VAL   B 1 81  ? -12.498 42.294 -39.929 1.00 18.48 ? 103 VAL   B CG2 1 
ATOM   2905 N N   . SER   B 1 82  ? -15.644 42.053 -40.654 1.00 17.83 ? 104 SER   B N   1 
ATOM   2906 C CA  . SER   B 1 82  ? -16.378 41.743 -41.866 1.00 17.44 ? 104 SER   B CA  1 
ATOM   2907 C C   . SER   B 1 82  ? -15.608 42.273 -43.062 1.00 17.37 ? 104 SER   B C   1 
ATOM   2908 O O   . SER   B 1 82  ? -14.924 43.281 -42.933 1.00 17.75 ? 104 SER   B O   1 
ATOM   2909 C CB  . SER   B 1 82  ? -17.755 42.342 -41.809 1.00 18.22 ? 104 SER   B CB  1 
ATOM   2910 O OG  . SER   B 1 82  ? -17.669 43.733 -41.539 1.00 18.68 ? 104 SER   B OG  1 
ATOM   2911 N N   . ALA   B 1 83  ? -15.772 41.609 -44.212 1.00 17.08 ? 105 ALA   B N   1 
ATOM   2912 C CA  . ALA   B 1 83  ? -15.116 41.977 -45.457 1.00 17.26 ? 105 ALA   B CA  1 
ATOM   2913 C C   . ALA   B 1 83  ? -16.182 42.299 -46.494 1.00 16.47 ? 105 ALA   B C   1 
ATOM   2914 O O   . ALA   B 1 83  ? -17.038 41.443 -46.733 1.00 15.96 ? 105 ALA   B O   1 
ATOM   2915 C CB  . ALA   B 1 83  ? -14.243 40.817 -45.916 1.00 17.35 ? 105 ALA   B CB  1 
ATOM   2916 N N   . SER   B 1 84  ? -16.088 43.485 -47.129 1.00 16.38 ? 106 SER   B N   1 
ATOM   2917 C CA  . SER   B 1 84  ? -17.167 44.033 -47.940 1.00 17.47 ? 106 SER   B CA  1 
ATOM   2918 C C   . SER   B 1 84  ? -16.707 44.453 -49.339 1.00 18.80 ? 106 SER   B C   1 
ATOM   2919 O O   . SER   B 1 84  ? -15.549 44.805 -49.600 1.00 18.50 ? 106 SER   B O   1 
ATOM   2920 C CB  . SER   B 1 84  ? -17.826 45.174 -47.214 1.00 18.18 ? 106 SER   B CB  1 
ATOM   2921 O OG  . SER   B 1 84  ? -18.778 45.874 -48.006 1.00 18.95 ? 106 SER   B OG  1 
ATOM   2922 N N   . ASP   B 1 85  ? -17.693 44.458 -50.232 1.00 20.25 ? 107 ASP   B N   1 
ATOM   2923 C CA  . ASP   B 1 85  ? -17.564 44.990 -51.579 1.00 20.23 ? 107 ASP   B CA  1 
ATOM   2924 C C   . ASP   B 1 85  ? -17.292 46.498 -51.566 1.00 20.47 ? 107 ASP   B C   1 
ATOM   2925 O O   . ASP   B 1 85  ? -16.883 47.037 -52.593 1.00 20.18 ? 107 ASP   B O   1 
ATOM   2926 C CB  . ASP   B 1 85  ? -18.778 44.608 -52.422 1.00 20.24 ? 107 ASP   B CB  1 
ATOM   2927 C CG  . ASP   B 1 85  ? -18.746 43.208 -53.020 1.00 19.73 ? 107 ASP   B CG  1 
ATOM   2928 O OD1 . ASP   B 1 85  ? -17.882 42.394 -52.603 1.00 19.93 ? 107 ASP   B OD1 1 
ATOM   2929 O OD2 . ASP   B 1 85  ? -19.551 42.952 -53.931 1.00 20.98 ? 107 ASP   B OD2 1 
ATOM   2930 N N   . ASP   B 1 86  ? -17.511 47.175 -50.424 1.00 19.76 ? 108 ASP   B N   1 
ATOM   2931 C CA  . ASP   B 1 86  ? -17.182 48.584 -50.295 1.00 20.91 ? 108 ASP   B CA  1 
ATOM   2932 C C   . ASP   B 1 86  ? -15.670 48.800 -50.147 1.00 20.42 ? 108 ASP   B C   1 
ATOM   2933 O O   . ASP   B 1 86  ? -15.241 49.938 -49.974 1.00 19.42 ? 108 ASP   B O   1 
ATOM   2934 C CB  . ASP   B 1 86  ? -17.976 49.233 -49.171 1.00 21.82 ? 108 ASP   B CB  1 
ATOM   2935 C CG  . ASP   B 1 86  ? -17.604 48.778 -47.766 1.00 21.87 ? 108 ASP   B CG  1 
ATOM   2936 O OD1 . ASP   B 1 86  ? -16.569 48.091 -47.638 1.00 21.60 ? 108 ASP   B OD1 1 
ATOM   2937 O OD2 . ASP   B 1 86  ? -18.360 49.094 -46.834 1.00 22.05 ? 108 ASP   B OD2 1 
ATOM   2938 N N   . LYS   B 1 87  ? -14.881 47.717 -50.195 1.00 20.11 ? 109 LYS   B N   1 
ATOM   2939 C CA  . LYS   B 1 87  ? -13.424 47.745 -50.262 1.00 21.05 ? 109 LYS   B CA  1 
ATOM   2940 C C   . LYS   B 1 87  ? -12.820 47.905 -48.866 1.00 20.69 ? 109 LYS   B C   1 
ATOM   2941 O O   . LYS   B 1 87  ? -11.605 48.085 -48.731 1.00 20.97 ? 109 LYS   B O   1 
ATOM   2942 C CB  . LYS   B 1 87  ? -12.890 48.817 -51.219 1.00 23.30 ? 109 LYS   B CB  1 
ATOM   2943 C CG  . LYS   B 1 87  ? -13.430 48.736 -52.631 1.00 24.48 ? 109 LYS   B CG  1 
ATOM   2944 C CD  . LYS   B 1 87  ? -12.841 49.881 -53.456 1.00 28.64 ? 109 LYS   B CD  1 
ATOM   2945 C CE  . LYS   B 1 87  ? -13.215 49.835 -54.896 1.00 32.93 ? 109 LYS   B CE  1 
ATOM   2946 N NZ  . LYS   B 1 87  ? -12.633 50.983 -55.590 1.00 37.13 ? 109 LYS   B NZ  1 
ATOM   2947 N N   . THR   B 1 88  ? -13.668 47.814 -47.836 1.00 19.63 ? 110 THR   B N   1 
ATOM   2948 C CA  . THR   B 1 88  ? -13.209 47.927 -46.464 1.00 20.17 ? 110 THR   B CA  1 
ATOM   2949 C C   . THR   B 1 88  ? -13.481 46.627 -45.722 1.00 19.33 ? 110 THR   B C   1 
ATOM   2950 O O   . THR   B 1 88  ? -14.319 45.814 -46.139 1.00 19.54 ? 110 THR   B O   1 
ATOM   2951 C CB  . THR   B 1 88  ? -13.888 49.092 -45.734 1.00 21.75 ? 110 THR   B CB  1 
ATOM   2952 O OG1 . THR   B 1 88  ? -15.192 48.689 -45.332 1.00 21.07 ? 110 THR   B OG1 1 
ATOM   2953 C CG2 . THR   B 1 88  ? -13.901 50.378 -46.546 1.00 22.82 ? 110 THR   B CG2 1 
ATOM   2954 N N   . LEU   B 1 89  ? -12.757 46.469 -44.608 1.00 18.35 ? 111 LEU   B N   1 
ATOM   2955 C CA  . LEU   B 1 89  ? -13.221 45.640 -43.508 1.00 18.38 ? 111 LEU   B CA  1 
ATOM   2956 C C   . LEU   B 1 89  ? -13.673 46.540 -42.360 1.00 19.96 ? 111 LEU   B C   1 
ATOM   2957 O O   . LEU   B 1 89  ? -13.194 47.668 -42.194 1.00 20.99 ? 111 LEU   B O   1 
ATOM   2958 C CB  . LEU   B 1 89  ? -12.149 44.655 -43.041 1.00 18.28 ? 111 LEU   B CB  1 
ATOM   2959 C CG  . LEU   B 1 89  ? -11.527 43.800 -44.145 1.00 18.24 ? 111 LEU   B CG  1 
ATOM   2960 C CD1 . LEU   B 1 89  ? -10.183 44.421 -44.554 1.00 19.18 ? 111 LEU   B CD1 1 
ATOM   2961 C CD2 . LEU   B 1 89  ? -11.392 42.356 -43.690 1.00 17.99 ? 111 LEU   B CD2 1 
ATOM   2962 N N   . LYS   B 1 90  ? -14.618 46.029 -41.570 1.00 19.20 ? 112 LYS   B N   1 
ATOM   2963 C CA  . LYS   B 1 90  ? -15.028 46.711 -40.359 1.00 20.38 ? 112 LYS   B CA  1 
ATOM   2964 C C   . LYS   B 1 90  ? -14.845 45.770 -39.181 1.00 20.22 ? 112 LYS   B C   1 
ATOM   2965 O O   . LYS   B 1 90  ? -15.159 44.586 -39.293 1.00 19.54 ? 112 LYS   B O   1 
ATOM   2966 C CB  . LYS   B 1 90  ? -16.459 47.219 -40.513 1.00 21.35 ? 112 LYS   B CB  1 
ATOM   2967 C CG  . LYS   B 1 90  ? -16.545 48.447 -41.387 1.00 21.87 ? 112 LYS   B CG  1 
ATOM   2968 C CD  . LYS   B 1 90  ? -17.974 48.891 -41.674 1.00 23.37 ? 112 LYS   B CD  1 
ATOM   2969 C CE  . LYS   B 1 90  ? -18.023 50.062 -42.611 1.00 24.92 ? 112 LYS   B CE  1 
ATOM   2970 N NZ  . LYS   B 1 90  ? -17.667 51.294 -41.902 1.00 26.89 ? 112 LYS   B NZ  1 
ATOM   2971 N N   . ILE   B 1 91  ? -14.337 46.327 -38.074 1.00 20.37 ? 113 ILE   B N   1 
ATOM   2972 C CA  . ILE   B 1 91  ? -14.261 45.624 -36.805 1.00 21.34 ? 113 ILE   B CA  1 
ATOM   2973 C C   . ILE   B 1 91  ? -15.431 46.091 -35.949 1.00 22.19 ? 113 ILE   B C   1 
ATOM   2974 O O   . ILE   B 1 91  ? -15.624 47.294 -35.802 1.00 23.58 ? 113 ILE   B O   1 
ATOM   2975 C CB  . ILE   B 1 91  ? -12.922 45.882 -36.098 1.00 22.42 ? 113 ILE   B CB  1 
ATOM   2976 C CG1 . ILE   B 1 91  ? -11.736 45.525 -36.998 1.00 23.11 ? 113 ILE   B CG1 1 
ATOM   2977 C CG2 . ILE   B 1 91  ? -12.890 45.147 -34.751 1.00 21.65 ? 113 ILE   B CG2 1 
ATOM   2978 C CD1 . ILE   B 1 91  ? -10.383 45.863 -36.400 1.00 22.55 ? 113 ILE   B CD1 1 
ATOM   2979 N N   . TRP   B 1 92  ? -16.190 45.130 -35.403 1.00 22.34 ? 114 TRP   B N   1 
ATOM   2980 C CA  . TRP   B 1 92  ? -17.415 45.411 -34.671 1.00 22.79 ? 114 TRP   B CA  1 
ATOM   2981 C C   . TRP   B 1 92  ? -17.298 44.945 -33.224 1.00 23.74 ? 114 TRP   B C   1 
ATOM   2982 O O   . TRP   B 1 92  ? -16.795 43.851 -32.959 1.00 22.50 ? 114 TRP   B O   1 
ATOM   2983 C CB  . TRP   B 1 92  ? -18.601 44.688 -35.320 1.00 22.75 ? 114 TRP   B CB  1 
ATOM   2984 C CG  . TRP   B 1 92  ? -18.741 44.921 -36.797 1.00 23.16 ? 114 TRP   B CG  1 
ATOM   2985 C CD1 . TRP   B 1 92  ? -18.167 44.190 -37.793 1.00 22.51 ? 114 TRP   B CD1 1 
ATOM   2986 C CD2 . TRP   B 1 92  ? -19.522 45.945 -37.444 1.00 23.57 ? 114 TRP   B CD2 1 
ATOM   2987 N NE1 . TRP   B 1 92  ? -18.519 44.692 -39.018 1.00 21.43 ? 114 TRP   B NE1 1 
ATOM   2988 C CE2 . TRP   B 1 92  ? -19.363 45.758 -38.834 1.00 23.31 ? 114 TRP   B CE2 1 
ATOM   2989 C CE3 . TRP   B 1 92  ? -20.336 46.988 -36.986 1.00 25.07 ? 114 TRP   B CE3 1 
ATOM   2990 C CZ2 . TRP   B 1 92  ? -19.983 46.590 -39.762 1.00 24.23 ? 114 TRP   B CZ2 1 
ATOM   2991 C CZ3 . TRP   B 1 92  ? -20.958 47.792 -37.906 1.00 25.18 ? 114 TRP   B CZ3 1 
ATOM   2992 C CH2 . TRP   B 1 92  ? -20.774 47.603 -39.271 1.00 25.88 ? 114 TRP   B CH2 1 
ATOM   2993 N N   . ASP   B 1 93  ? -17.805 45.778 -32.305 1.00 24.56 ? 115 ASP   B N   1 
ATOM   2994 C CA  . ASP   B 1 93  ? -18.111 45.344 -30.958 1.00 27.36 ? 115 ASP   B CA  1 
ATOM   2995 C C   . ASP   B 1 93  ? -19.451 44.620 -31.004 1.00 26.55 ? 115 ASP   B C   1 
ATOM   2996 O O   . ASP   B 1 93  ? -20.482 45.244 -31.253 1.00 28.11 ? 115 ASP   B O   1 
ATOM   2997 C CB  . ASP   B 1 93  ? -18.149 46.506 -29.981 1.00 29.69 ? 115 ASP   B CB  1 
ATOM   2998 C CG  . ASP   B 1 93  ? -18.271 46.066 -28.534 1.00 33.07 ? 115 ASP   B CG  1 
ATOM   2999 O OD1 . ASP   B 1 93  ? -19.385 45.708 -28.129 1.00 33.76 ? 115 ASP   B OD1 1 
ATOM   3000 O OD2 . ASP   B 1 93  ? -17.226 46.000 -27.861 1.00 38.30 ? 115 ASP   B OD2 1 
ATOM   3001 N N   . VAL   B 1 94  ? -19.417 43.310 -30.759 1.00 25.41 ? 116 VAL   B N   1 
ATOM   3002 C CA  . VAL   B 1 94  ? -20.594 42.470 -30.883 1.00 27.92 ? 116 VAL   B CA  1 
ATOM   3003 C C   . VAL   B 1 94  ? -21.694 42.928 -29.929 1.00 28.63 ? 116 VAL   B C   1 
ATOM   3004 O O   . VAL   B 1 94  ? -22.855 42.970 -30.325 1.00 30.07 ? 116 VAL   B O   1 
ATOM   3005 C CB  . VAL   B 1 94  ? -20.240 40.990 -30.660 1.00 30.27 ? 116 VAL   B CB  1 
ATOM   3006 C CG1 . VAL   B 1 94  ? -21.486 40.108 -30.626 1.00 33.98 ? 116 VAL   B CG1 1 
ATOM   3007 C CG2 . VAL   B 1 94  ? -19.280 40.495 -31.730 1.00 29.48 ? 116 VAL   B CG2 1 
ATOM   3008 N N   . SER   B 1 95  ? -21.336 43.254 -28.680 1.00 30.14 ? 117 SER   B N   1 
ATOM   3009 C CA  . SER   B 1 95  ? -22.331 43.579 -27.665 1.00 31.55 ? 117 SER   B CA  1 
ATOM   3010 C C   . SER   B 1 95  ? -23.093 44.863 -28.013 1.00 31.70 ? 117 SER   B C   1 
ATOM   3011 O O   . SER   B 1 95  ? -24.313 44.909 -27.878 1.00 34.59 ? 117 SER   B O   1 
ATOM   3012 C CB  . SER   B 1 95  ? -21.709 43.649 -26.291 1.00 35.98 ? 117 SER   B CB  1 
ATOM   3013 O OG  . SER   B 1 95  ? -20.943 44.834 -26.131 1.00 41.46 ? 117 SER   B OG  1 
ATOM   3014 N N   . SER   B 1 96  ? -22.385 45.897 -28.485 1.00 31.10 ? 118 SER   B N   1 
ATOM   3015 C CA  . SER   B 1 96  ? -22.994 47.186 -28.790 1.00 31.82 ? 118 SER   B CA  1 
ATOM   3016 C C   . SER   B 1 96  ? -23.477 47.265 -30.238 1.00 31.21 ? 118 SER   B C   1 
ATOM   3017 O O   . SER   B 1 96  ? -24.320 48.100 -30.568 1.00 31.14 ? 118 SER   B O   1 
ATOM   3018 C CB  . SER   B 1 96  ? -22.028 48.308 -28.510 1.00 31.14 ? 118 SER   B CB  1 
ATOM   3019 O OG  . SER   B 1 96  ? -20.941 48.295 -29.424 1.00 31.58 ? 118 SER   B OG  1 
ATOM   3020 N N   . GLY   B 1 97  ? -22.891 46.440 -31.111 1.00 31.94 ? 119 GLY   B N   1 
ATOM   3021 C CA  . GLY   B 1 97  ? -23.182 46.484 -32.539 1.00 31.40 ? 119 GLY   B CA  1 
ATOM   3022 C C   . GLY   B 1 97  ? -22.450 47.625 -33.247 1.00 31.97 ? 119 GLY   B C   1 
ATOM   3023 O O   . GLY   B 1 97  ? -22.689 47.858 -34.431 1.00 34.82 ? 119 GLY   B O   1 
ATOM   3024 N N   . LYS   B 1 98  ? -21.564 48.333 -32.531 1.00 31.68 ? 120 LYS   B N   1 
ATOM   3025 C CA  . LYS   B 1 98  ? -20.923 49.523 -33.073 1.00 31.49 ? 120 LYS   B CA  1 
ATOM   3026 C C   . LYS   B 1 98  ? -19.699 49.137 -33.900 1.00 29.74 ? 120 LYS   B C   1 
ATOM   3027 O O   . LYS   B 1 98  ? -18.962 48.219 -33.542 1.00 29.50 ? 120 LYS   B O   1 
ATOM   3028 C CB  . LYS   B 1 98  ? -20.495 50.495 -31.968 1.00 33.03 ? 120 LYS   B CB  1 
ATOM   3029 N N   . CYS   B 1 99  ? -19.478 49.864 -35.000 1.00 30.19 ? 121 CYS   B N   1 
ATOM   3030 C CA  . CYS   B 1 99  ? -18.251 49.740 -35.775 1.00 29.89 ? 121 CYS   B CA  1 
ATOM   3031 C C   . CYS   B 1 99  ? -17.121 50.464 -35.048 1.00 28.85 ? 121 CYS   B C   1 
ATOM   3032 O O   . CYS   B 1 99  ? -17.189 51.671 -34.883 1.00 29.85 ? 121 CYS   B O   1 
ATOM   3033 C CB  . CYS   B 1 99  ? -18.434 50.324 -37.172 1.00 30.20 ? 121 CYS   B CB  1 
ATOM   3034 S SG  . CYS   B 1 99  ? -16.905 50.422 -38.144 1.00 31.04 ? 121 CYS   B SG  1 
ATOM   3035 N N   . LEU   B 1 100 ? -16.092 49.721 -34.612 1.00 29.51 ? 122 LEU   B N   1 
ATOM   3036 C CA  . LEU   B 1 100 ? -14.967 50.287 -33.880 1.00 29.84 ? 122 LEU   B CA  1 
ATOM   3037 C C   . LEU   B 1 100 ? -13.925 50.882 -34.823 1.00 29.83 ? 122 LEU   B C   1 
ATOM   3038 O O   . LEU   B 1 100 ? -13.339 51.918 -34.510 1.00 30.40 ? 122 LEU   B O   1 
ATOM   3039 C CB  . LEU   B 1 100 ? -14.315 49.206 -33.029 1.00 29.54 ? 122 LEU   B CB  1 
ATOM   3040 C CG  . LEU   B 1 100 ? -15.209 48.560 -31.972 1.00 31.03 ? 122 LEU   B CG  1 
ATOM   3041 C CD1 . LEU   B 1 100 ? -14.435 47.435 -31.331 1.00 31.04 ? 122 LEU   B CD1 1 
ATOM   3042 C CD2 . LEU   B 1 100 ? -15.671 49.584 -30.944 1.00 32.59 ? 122 LEU   B CD2 1 
ATOM   3043 N N   . LYS   B 1 101 ? -13.632 50.164 -35.917 1.00 29.47 ? 123 LYS   B N   1 
ATOM   3044 C CA  . LYS   B 1 101 ? -12.635 50.582 -36.892 1.00 30.57 ? 123 LYS   B CA  1 
ATOM   3045 C C   . LYS   B 1 101 ? -13.108 50.184 -38.288 1.00 27.88 ? 123 LYS   B C   1 
ATOM   3046 O O   . LYS   B 1 101 ? -13.781 49.162 -38.456 1.00 25.42 ? 123 LYS   B O   1 
ATOM   3047 C CB  . LYS   B 1 101 ? -11.262 49.921 -36.700 1.00 31.66 ? 123 LYS   B CB  1 
ATOM   3048 C CG  . LYS   B 1 101 ? -10.477 50.279 -35.458 1.00 34.98 ? 123 LYS   B CG  1 
ATOM   3049 C CD  . LYS   B 1 101 ? -9.747  51.612 -35.562 1.00 37.13 ? 123 LYS   B CD  1 
ATOM   3050 C CE  . LYS   B 1 101 ? -8.873  51.887 -34.389 1.00 38.30 ? 123 LYS   B CE  1 
ATOM   3051 N NZ  . LYS   B 1 101 ? -9.682  52.139 -33.199 1.00 40.08 ? 123 LYS   B NZ  1 
ATOM   3052 N N   . THR   B 1 102 ? -12.736 51.016 -39.269 1.00 27.30 ? 124 THR   B N   1 
ATOM   3053 C CA  . THR   B 1 102 ? -12.870 50.694 -40.677 1.00 24.95 ? 124 THR   B CA  1 
ATOM   3054 C C   . THR   B 1 102 ? -11.463 50.566 -41.254 1.00 24.61 ? 124 THR   B C   1 
ATOM   3055 O O   . THR   B 1 102 ? -10.654 51.490 -41.161 1.00 26.91 ? 124 THR   B O   1 
ATOM   3056 C CB  . THR   B 1 102 ? -13.699 51.752 -41.407 1.00 25.37 ? 124 THR   B CB  1 
ATOM   3057 O OG1 . THR   B 1 102 ? -14.992 51.797 -40.804 1.00 24.27 ? 124 THR   B OG1 1 
ATOM   3058 C CG2 . THR   B 1 102 ? -13.854 51.404 -42.875 1.00 25.45 ? 124 THR   B CG2 1 
ATOM   3059 N N   . LEU   B 1 103 ? -11.188 49.389 -41.826 1.00 22.61 ? 125 LEU   B N   1 
ATOM   3060 C CA  . LEU   B 1 103 ? -9.882  49.044 -42.346 1.00 23.03 ? 125 LEU   B CA  1 
ATOM   3061 C C   . LEU   B 1 103 ? -9.858  49.357 -43.837 1.00 23.40 ? 125 LEU   B C   1 
ATOM   3062 O O   . LEU   B 1 103 ? -10.494 48.670 -44.635 1.00 23.57 ? 125 LEU   B O   1 
ATOM   3063 C CB  . LEU   B 1 103 ? -9.628  47.564 -42.062 1.00 24.09 ? 125 LEU   B CB  1 
ATOM   3064 C CG  . LEU   B 1 103 ? -9.752  47.105 -40.602 1.00 25.90 ? 125 LEU   B CG  1 
ATOM   3065 C CD1 . LEU   B 1 103 ? -9.064  45.761 -40.379 1.00 25.09 ? 125 LEU   B CD1 1 
ATOM   3066 C CD2 . LEU   B 1 103 ? -9.266  48.087 -39.587 1.00 28.04 ? 125 LEU   B CD2 1 
ATOM   3067 N N   . LYS   B 1 104 ? -9.083  50.379 -44.193 1.00 25.01 ? 126 LYS   B N   1 
ATOM   3068 C CA  . LYS   B 1 104 ? -9.043  50.900 -45.549 1.00 26.08 ? 126 LYS   B CA  1 
ATOM   3069 C C   . LYS   B 1 104 ? -7.661  50.652 -46.133 1.00 25.59 ? 126 LYS   B C   1 
ATOM   3070 O O   . LYS   B 1 104 ? -6.657  50.831 -45.448 1.00 26.24 ? 126 LYS   B O   1 
ATOM   3071 C CB  . LYS   B 1 104 ? -9.287  52.408 -45.565 1.00 30.02 ? 126 LYS   B CB  1 
ATOM   3072 C CG  . LYS   B 1 104 ? -10.619 52.842 -45.012 1.00 34.37 ? 126 LYS   B CG  1 
ATOM   3073 C CD  . LYS   B 1 104 ? -10.804 54.356 -45.133 1.00 39.08 ? 126 LYS   B CD  1 
ATOM   3074 C CE  . LYS   B 1 104 ? -11.737 54.924 -44.113 1.00 42.90 ? 126 LYS   B CE  1 
ATOM   3075 N NZ  . LYS   B 1 104 ? -13.115 54.498 -44.351 1.00 46.31 ? 126 LYS   B NZ  1 
ATOM   3076 N N   . GLY   B 1 105 ? -7.628  50.233 -47.399 1.00 24.84 ? 127 GLY   B N   1 
ATOM   3077 C CA  . GLY   B 1 105 ? -6.381  50.049 -48.120 1.00 24.61 ? 127 GLY   B CA  1 
ATOM   3078 C C   . GLY   B 1 105 ? -6.556  49.184 -49.364 1.00 23.23 ? 127 GLY   B C   1 
ATOM   3079 O O   . GLY   B 1 105 ? -5.895  49.409 -50.376 1.00 24.96 ? 127 GLY   B O   1 
ATOM   3080 N N   . HIS   B 1 106 ? -7.425  48.172 -49.289 1.00 21.90 ? 128 HIS   B N   1 
ATOM   3081 C CA  . HIS   B 1 106 ? -7.686  47.378 -50.474 1.00 21.06 ? 128 HIS   B CA  1 
ATOM   3082 C C   . HIS   B 1 106 ? -8.255  48.274 -51.570 1.00 22.07 ? 128 HIS   B C   1 
ATOM   3083 O O   . HIS   B 1 106 ? -8.981  49.236 -51.294 1.00 22.78 ? 128 HIS   B O   1 
ATOM   3084 C CB  . HIS   B 1 106 ? -8.635  46.222 -50.167 1.00 20.32 ? 128 HIS   B CB  1 
ATOM   3085 C CG  . HIS   B 1 106 ? -7.980  45.089 -49.483 1.00 19.53 ? 128 HIS   B CG  1 
ATOM   3086 N ND1 . HIS   B 1 106 ? -6.936  44.376 -50.036 1.00 19.12 ? 128 HIS   B ND1 1 
ATOM   3087 C CD2 . HIS   B 1 106 ? -8.221  44.542 -48.280 1.00 19.88 ? 128 HIS   B CD2 1 
ATOM   3088 C CE1 . HIS   B 1 106 ? -6.604  43.392 -49.201 1.00 19.94 ? 128 HIS   B CE1 1 
ATOM   3089 N NE2 . HIS   B 1 106 ? -7.362  43.481 -48.127 1.00 19.47 ? 128 HIS   B NE2 1 
ATOM   3090 N N   . SER   B 1 107 ? -7.915  47.947 -52.819 1.00 22.67 ? 129 SER   B N   1 
ATOM   3091 C CA  . SER   B 1 107 ? -8.374  48.740 -53.945 1.00 23.05 ? 129 SER   B CA  1 
ATOM   3092 C C   . SER   B 1 107 ? -9.514  48.046 -54.702 1.00 22.42 ? 129 SER   B C   1 
ATOM   3093 O O   . SER   B 1 107 ? -9.936  48.508 -55.766 1.00 23.31 ? 129 SER   B O   1 
ATOM   3094 C CB  . SER   B 1 107 ? -7.215  49.069 -54.840 1.00 23.82 ? 129 SER   B CB  1 
ATOM   3095 O OG  . SER   B 1 107 ? -6.605  47.888 -55.332 1.00 22.68 ? 129 SER   B OG  1 
ATOM   3096 N N   . ASN   B 1 108 ? -10.058 46.962 -54.141 1.00 21.33 ? 130 ASN   B N   1 
ATOM   3097 C CA  . ASN   B 1 108 ? -11.167 46.251 -54.759 1.00 20.41 ? 130 ASN   B CA  1 
ATOM   3098 C C   . ASN   B 1 108 ? -11.870 45.485 -53.642 1.00 18.86 ? 130 ASN   B C   1 
ATOM   3099 O O   . ASN   B 1 108 ? -11.517 45.631 -52.467 1.00 19.49 ? 130 ASN   B O   1 
ATOM   3100 C CB  . ASN   B 1 108 ? -10.660 45.362 -55.891 1.00 20.79 ? 130 ASN   B CB  1 
ATOM   3101 C CG  . ASN   B 1 108 ? -11.685 45.021 -56.953 1.00 23.78 ? 130 ASN   B CG  1 
ATOM   3102 O OD1 . ASN   B 1 108 ? -12.907 44.997 -56.724 1.00 24.37 ? 130 ASN   B OD1 1 
ATOM   3103 N ND2 . ASN   B 1 108 ? -11.183 44.671 -58.126 1.00 25.96 ? 130 ASN   B ND2 1 
ATOM   3104 N N   . TYR   B 1 109 ? -12.876 44.692 -54.017 1.00 17.72 ? 131 TYR   B N   1 
ATOM   3105 C CA  . TYR   B 1 109 ? -13.699 44.002 -53.046 1.00 17.55 ? 131 TYR   B CA  1 
ATOM   3106 C C   . TYR   B 1 109 ? -12.814 43.243 -52.069 1.00 16.39 ? 131 TYR   B C   1 
ATOM   3107 O O   . TYR   B 1 109 ? -11.875 42.572 -52.481 1.00 16.60 ? 131 TYR   B O   1 
ATOM   3108 C CB  . TYR   B 1 109 ? -14.652 43.011 -53.713 1.00 18.34 ? 131 TYR   B CB  1 
ATOM   3109 C CG  . TYR   B 1 109 ? -15.557 43.581 -54.799 1.00 20.46 ? 131 TYR   B CG  1 
ATOM   3110 C CD1 . TYR   B 1 109 ? -15.966 44.912 -54.795 1.00 19.62 ? 131 TYR   B CD1 1 
ATOM   3111 C CD2 . TYR   B 1 109 ? -16.028 42.765 -55.824 1.00 24.36 ? 131 TYR   B CD2 1 
ATOM   3112 C CE1 . TYR   B 1 109 ? -16.835 45.402 -55.754 1.00 22.30 ? 131 TYR   B CE1 1 
ATOM   3113 C CE2 . TYR   B 1 109 ? -16.874 43.253 -56.806 1.00 26.28 ? 131 TYR   B CE2 1 
ATOM   3114 C CZ  . TYR   B 1 109 ? -17.280 44.574 -56.766 1.00 24.49 ? 131 TYR   B CZ  1 
ATOM   3115 O OH  . TYR   B 1 109 ? -18.115 45.054 -57.732 1.00 29.27 ? 131 TYR   B OH  1 
ATOM   3116 N N   . VAL   B 1 110 ? -13.177 43.293 -50.785 1.00 16.22 ? 132 VAL   B N   1 
ATOM   3117 C CA  . VAL   B 1 110 ? -12.564 42.418 -49.797 1.00 16.12 ? 132 VAL   B CA  1 
ATOM   3118 C C   . VAL   B 1 110 ? -13.439 41.177 -49.673 1.00 15.72 ? 132 VAL   B C   1 
ATOM   3119 O O   . VAL   B 1 110 ? -14.628 41.269 -49.417 1.00 16.18 ? 132 VAL   B O   1 
ATOM   3120 C CB  . VAL   B 1 110 ? -12.330 43.071 -48.429 1.00 16.25 ? 132 VAL   B CB  1 
ATOM   3121 C CG1 . VAL   B 1 110 ? -11.389 42.223 -47.573 1.00 16.75 ? 132 VAL   B CG1 1 
ATOM   3122 C CG2 . VAL   B 1 110 ? -11.807 44.495 -48.558 1.00 16.85 ? 132 VAL   B CG2 1 
ATOM   3123 N N   . PHE   B 1 111 ? -12.818 40.007 -49.850 1.00 16.41 ? 133 PHE   B N   1 
ATOM   3124 C CA  . PHE   B 1 111 ? -13.554 38.775 -50.038 1.00 15.89 ? 133 PHE   B CA  1 
ATOM   3125 C C   . PHE   B 1 111 ? -13.484 37.885 -48.812 1.00 15.58 ? 133 PHE   B C   1 
ATOM   3126 O O   . PHE   B 1 111 ? -14.422 37.122 -48.580 1.00 16.83 ? 133 PHE   B O   1 
ATOM   3127 C CB  . PHE   B 1 111 ? -12.991 38.012 -51.241 1.00 17.29 ? 133 PHE   B CB  1 
ATOM   3128 C CG  . PHE   B 1 111 ? -13.820 36.814 -51.659 1.00 18.60 ? 133 PHE   B CG  1 
ATOM   3129 C CD1 . PHE   B 1 111 ? -15.115 36.992 -52.146 1.00 19.84 ? 133 PHE   B CD1 1 
ATOM   3130 C CD2 . PHE   B 1 111 ? -13.312 35.524 -51.589 1.00 20.44 ? 133 PHE   B CD2 1 
ATOM   3131 C CE1 . PHE   B 1 111 ? -15.875 35.911 -52.558 1.00 20.22 ? 133 PHE   B CE1 1 
ATOM   3132 C CE2 . PHE   B 1 111 ? -14.079 34.438 -51.999 1.00 21.19 ? 133 PHE   B CE2 1 
ATOM   3133 C CZ  . PHE   B 1 111 ? -15.350 34.638 -52.501 1.00 21.32 ? 133 PHE   B CZ  1 
ATOM   3134 N N   . CYS   B 1 112 ? -12.344 37.886 -48.104 1.00 14.82 ? 134 CYS   B N   1 
ATOM   3135 C CA  . CYS   B 1 112 ? -12.146 36.906 -47.051 1.00 14.65 ? 134 CYS   B CA  1 
ATOM   3136 C C   . CYS   B 1 112 ? -11.356 37.549 -45.924 1.00 14.88 ? 134 CYS   B C   1 
ATOM   3137 O O   . CYS   B 1 112 ? -10.552 38.444 -46.179 1.00 14.52 ? 134 CYS   B O   1 
ATOM   3138 C CB  . CYS   B 1 112 ? -11.449 35.657 -47.578 1.00 14.22 ? 134 CYS   B CB  1 
ATOM   3139 S SG  . CYS   B 1 112 ? -9.944  36.002 -48.525 1.00 15.65 ? 134 CYS   B SG  1 
ATOM   3140 N N   . CYS   B 1 113 ? -11.598 37.062 -44.700 1.00 14.22 ? 135 CYS   B N   1 
ATOM   3141 C CA  . CYS   B 1 113 ? -10.977 37.630 -43.510 1.00 13.91 ? 135 CYS   B CA  1 
ATOM   3142 C C   . CYS   B 1 113 ? -10.905 36.627 -42.371 1.00 14.09 ? 135 CYS   B C   1 
ATOM   3143 O O   . CYS   B 1 113 ? -11.662 35.657 -42.318 1.00 14.61 ? 135 CYS   B O   1 
ATOM   3144 C CB  . CYS   B 1 113 ? -11.696 38.905 -43.077 1.00 14.77 ? 135 CYS   B CB  1 
ATOM   3145 S SG  . CYS   B 1 113 ? -13.467 38.701 -42.765 1.00 16.48 ? 135 CYS   B SG  1 
ATOM   3146 N N   . ASN   B 1 114 ? -10.010 36.918 -41.427 1.00 14.28 ? 136 ASN   B N   1 
ATOM   3147 C CA  . ASN   B 1 114 ? -9.814  36.076 -40.259 1.00 14.53 ? 136 ASN   B CA  1 
ATOM   3148 C C   . ASN   B 1 114 ? -8.974  36.836 -39.240 1.00 14.67 ? 136 ASN   B C   1 
ATOM   3149 O O   . ASN   B 1 114 ? -8.035  37.540 -39.601 1.00 15.46 ? 136 ASN   B O   1 
ATOM   3150 C CB  . ASN   B 1 114 ? -9.171  34.731 -40.607 1.00 15.36 ? 136 ASN   B CB  1 
ATOM   3151 C CG  . ASN   B 1 114 ? -10.161 33.581 -40.692 1.00 16.17 ? 136 ASN   B CG  1 
ATOM   3152 O OD1 . ASN   B 1 114 ? -11.026 33.411 -39.818 1.00 16.95 ? 136 ASN   B OD1 1 
ATOM   3153 N ND2 . ASN   B 1 114 ? -10.068 32.783 -41.744 1.00 15.28 ? 136 ASN   B ND2 1 
ATOM   3154 N N   . PHE   B 1 115 ? -9.277  36.621 -37.962 1.00 14.62 ? 137 PHE   B N   1 
ATOM   3155 C CA  . PHE   B 1 115 ? -8.386  37.012 -36.881 1.00 14.62 ? 137 PHE   B CA  1 
ATOM   3156 C C   . PHE   B 1 115 ? -7.325  35.931 -36.697 1.00 14.96 ? 137 PHE   B C   1 
ATOM   3157 O O   . PHE   B 1 115 ? -7.587  34.768 -36.995 1.00 14.81 ? 137 PHE   B O   1 
ATOM   3158 C CB  . PHE   B 1 115 ? -9.163  37.097 -35.565 1.00 14.54 ? 137 PHE   B CB  1 
ATOM   3159 C CG  . PHE   B 1 115 ? -10.022 38.339 -35.378 1.00 15.39 ? 137 PHE   B CG  1 
ATOM   3160 C CD1 . PHE   B 1 115 ? -9.495  39.465 -34.757 1.00 15.67 ? 137 PHE   B CD1 1 
ATOM   3161 C CD2 . PHE   B 1 115 ? -11.350 38.374 -35.786 1.00 16.54 ? 137 PHE   B CD2 1 
ATOM   3162 C CE1 . PHE   B 1 115 ? -10.269 40.589 -34.563 1.00 16.65 ? 137 PHE   B CE1 1 
ATOM   3163 C CE2 . PHE   B 1 115 ? -12.120 39.509 -35.596 1.00 16.92 ? 137 PHE   B CE2 1 
ATOM   3164 C CZ  . PHE   B 1 115 ? -11.591 40.601 -34.960 1.00 16.87 ? 137 PHE   B CZ  1 
ATOM   3165 N N   . ASN   B 1 116 ? -6.163  36.298 -36.139 1.00 15.34 ? 138 ASN   B N   1 
ATOM   3166 C CA  . ASN   B 1 116 ? -5.233  35.295 -35.644 1.00 15.47 ? 138 ASN   B CA  1 
ATOM   3167 C C   . ASN   B 1 116 ? -5.768  34.800 -34.297 1.00 15.83 ? 138 ASN   B C   1 
ATOM   3168 O O   . ASN   B 1 116 ? -6.662  35.411 -33.702 1.00 15.62 ? 138 ASN   B O   1 
ATOM   3169 C CB  . ASN   B 1 116 ? -3.785  35.795 -35.636 1.00 16.11 ? 138 ASN   B CB  1 
ATOM   3170 C CG  . ASN   B 1 116 ? -3.551  37.001 -34.754 1.00 16.49 ? 138 ASN   B CG  1 
ATOM   3171 O OD1 . ASN   B 1 116 ? -4.497  37.624 -34.257 1.00 16.20 ? 138 ASN   B OD1 1 
ATOM   3172 N ND2 . ASN   B 1 116 ? -2.287  37.345 -34.541 1.00 17.37 ? 138 ASN   B ND2 1 
ATOM   3173 N N   . PRO   B 1 117 ? -5.270  33.654 -33.782 1.00 16.86 ? 139 PRO   B N   1 
ATOM   3174 C CA  . PRO   B 1 117 ? -5.682  33.175 -32.457 1.00 17.06 ? 139 PRO   B CA  1 
ATOM   3175 C C   . PRO   B 1 117 ? -5.587  34.247 -31.368 1.00 17.49 ? 139 PRO   B C   1 
ATOM   3176 O O   . PRO   B 1 117 ? -6.511  34.415 -30.570 1.00 17.41 ? 139 PRO   B O   1 
ATOM   3177 C CB  . PRO   B 1 117 ? -4.749  31.966 -32.228 1.00 17.11 ? 139 PRO   B CB  1 
ATOM   3178 C CG  . PRO   B 1 117 ? -4.466  31.472 -33.643 1.00 17.07 ? 139 PRO   B CG  1 
ATOM   3179 C CD  . PRO   B 1 117 ? -4.349  32.732 -34.475 1.00 17.00 ? 139 PRO   B CD  1 
ATOM   3180 N N   . GLN   B 1 118 ? -4.467  34.986 -31.361 1.00 17.69 ? 140 GLN   B N   1 
ATOM   3181 C CA  . GLN   B 1 118 ? -4.209  36.032 -30.380 1.00 17.24 ? 140 GLN   B CA  1 
ATOM   3182 C C   . GLN   B 1 118 ? -5.253  37.136 -30.501 1.00 17.42 ? 140 GLN   B C   1 
ATOM   3183 O O   . GLN   B 1 118 ? -5.572  37.791 -29.507 1.00 17.67 ? 140 GLN   B O   1 
ATOM   3184 C CB  . GLN   B 1 118 ? -2.829  36.660 -30.592 1.00 18.16 ? 140 GLN   B CB  1 
ATOM   3185 C CG  . GLN   B 1 118 ? -1.676  35.661 -30.627 1.00 18.68 ? 140 GLN   B CG  1 
ATOM   3186 C CD  . GLN   B 1 118 ? -1.287  35.287 -32.037 1.00 19.70 ? 140 GLN   B CD  1 
ATOM   3187 O OE1 . GLN   B 1 118 ? -2.051  34.659 -32.782 1.00 18.24 ? 140 GLN   B OE1 1 
ATOM   3188 N NE2 . GLN   B 1 118 ? -0.096  35.721 -32.437 1.00 21.93 ? 140 GLN   B NE2 1 
ATOM   3189 N N   . SER   B 1 119 ? -5.717  37.335 -31.748 1.00 16.85 ? 141 SER   B N   1 
ATOM   3190 C CA  . SER   B 1 119 ? -6.735  38.292 -32.157 1.00 17.55 ? 141 SER   B CA  1 
ATOM   3191 C C   . SER   B 1 119 ? -6.209  39.723 -32.050 1.00 18.79 ? 141 SER   B C   1 
ATOM   3192 O O   . SER   B 1 119 ? -6.984  40.670 -31.990 1.00 20.42 ? 141 SER   B O   1 
ATOM   3193 C CB  . SER   B 1 119 ? -8.057  38.062 -31.441 1.00 17.59 ? 141 SER   B CB  1 
ATOM   3194 O OG  . SER   B 1 119 ? -8.619  36.811 -31.834 1.00 16.96 ? 141 SER   B OG  1 
ATOM   3195 N N   . ASN   B 1 120 ? -4.880  39.877 -32.140 1.00 18.57 ? 142 ASN   B N   1 
ATOM   3196 C CA  . ASN   B 1 120 ? -4.267  41.187 -32.266 1.00 19.60 ? 142 ASN   B CA  1 
ATOM   3197 C C   . ASN   B 1 120 ? -4.118  41.565 -33.736 1.00 19.28 ? 142 ASN   B C   1 
ATOM   3198 O O   . ASN   B 1 120 ? -3.884  42.739 -34.025 1.00 20.12 ? 142 ASN   B O   1 
ATOM   3199 C CB  . ASN   B 1 120 ? -2.922  41.278 -31.564 1.00 20.43 ? 142 ASN   B CB  1 
ATOM   3200 C CG  . ASN   B 1 120 ? -1.857  40.423 -32.206 1.00 19.69 ? 142 ASN   B CG  1 
ATOM   3201 O OD1 . ASN   B 1 120 ? -2.100  39.263 -32.524 1.00 18.91 ? 142 ASN   B OD1 1 
ATOM   3202 N ND2 . ASN   B 1 120 ? -0.679  40.979 -32.428 1.00 21.79 ? 142 ASN   B ND2 1 
ATOM   3203 N N   . LEU   B 1 121 ? -4.291  40.589 -34.645 1.00 17.53 ? 143 LEU   B N   1 
ATOM   3204 C CA  . LEU   B 1 121 ? -4.167  40.824 -36.075 1.00 17.08 ? 143 LEU   B CA  1 
ATOM   3205 C C   . LEU   B 1 121 ? -5.410  40.320 -36.798 1.00 16.43 ? 143 LEU   B C   1 
ATOM   3206 O O   . LEU   B 1 121 ? -6.043  39.363 -36.368 1.00 15.91 ? 143 LEU   B O   1 
ATOM   3207 C CB  . LEU   B 1 121 ? -2.947  40.124 -36.678 1.00 17.94 ? 143 LEU   B CB  1 
ATOM   3208 C CG  . LEU   B 1 121 ? -1.578  40.483 -36.099 1.00 19.10 ? 143 LEU   B CG  1 
ATOM   3209 C CD1 . LEU   B 1 121 ? -0.525  39.633 -36.779 1.00 18.83 ? 143 LEU   B CD1 1 
ATOM   3210 C CD2 . LEU   B 1 121 ? -1.256  41.950 -36.247 1.00 19.63 ? 143 LEU   B CD2 1 
ATOM   3211 N N   . ILE   B 1 122 ? -5.684  40.951 -37.944 1.00 16.04 ? 144 ILE   B N   1 
ATOM   3212 C CA  . ILE   B 1 122 ? -6.605  40.440 -38.946 1.00 16.29 ? 144 ILE   B CA  1 
ATOM   3213 C C   . ILE   B 1 122 ? -5.849  40.261 -40.257 1.00 16.04 ? 144 ILE   B C   1 
ATOM   3214 O O   . ILE   B 1 122 ? -5.005  41.091 -40.605 1.00 16.84 ? 144 ILE   B O   1 
ATOM   3215 C CB  . ILE   B 1 122 ? -7.803  41.400 -39.086 1.00 17.45 ? 144 ILE   B CB  1 
ATOM   3216 C CG1 . ILE   B 1 122 ? -8.654  41.385 -37.834 1.00 17.68 ? 144 ILE   B CG1 1 
ATOM   3217 C CG2 . ILE   B 1 122 ? -8.652  41.077 -40.313 1.00 18.04 ? 144 ILE   B CG2 1 
ATOM   3218 C CD1 . ILE   B 1 122 ? -9.541  42.608 -37.709 1.00 18.86 ? 144 ILE   B CD1 1 
ATOM   3219 N N   . VAL   B 1 123 ? -6.173  39.176 -40.970 1.00 15.32 ? 145 VAL   B N   1 
ATOM   3220 C CA  . VAL   B 1 123 ? -5.720  38.972 -42.332 1.00 15.61 ? 145 VAL   B CA  1 
ATOM   3221 C C   . VAL   B 1 123 ? -6.927  39.081 -43.257 1.00 15.27 ? 145 VAL   B C   1 
ATOM   3222 O O   . VAL   B 1 123 ? -8.029  38.628 -42.917 1.00 14.16 ? 145 VAL   B O   1 
ATOM   3223 C CB  . VAL   B 1 123 ? -5.006  37.618 -42.489 1.00 15.09 ? 145 VAL   B CB  1 
ATOM   3224 C CG1 . VAL   B 1 123 ? -5.928  36.424 -42.264 1.00 14.97 ? 145 VAL   B CG1 1 
ATOM   3225 C CG2 . VAL   B 1 123 ? -4.287  37.514 -43.832 1.00 16.80 ? 145 VAL   B CG2 1 
ATOM   3226 N N   . SER   B 1 124 ? -6.689  39.658 -44.432 1.00 15.09 ? 146 SER   B N   1 
ATOM   3227 C CA  . SER   B 1 124 ? -7.723  39.825 -45.430 1.00 15.92 ? 146 SER   B CA  1 
ATOM   3228 C C   . SER   B 1 124 ? -7.163  39.456 -46.798 1.00 16.68 ? 146 SER   B C   1 
ATOM   3229 O O   . SER   B 1 124 ? -5.969  39.607 -47.060 1.00 17.02 ? 146 SER   B O   1 
ATOM   3230 C CB  . SER   B 1 124 ? -8.272  41.247 -45.436 1.00 15.98 ? 146 SER   B CB  1 
ATOM   3231 O OG  . SER   B 1 124 ? -7.256  42.196 -45.753 1.00 16.34 ? 146 SER   B OG  1 
ATOM   3232 N N   . GLY   B 1 125 ? -8.044  38.951 -47.660 1.00 16.80 ? 147 GLY   B N   1 
ATOM   3233 C CA  . GLY   B 1 125 ? -7.723  38.767 -49.066 1.00 16.62 ? 147 GLY   B CA  1 
ATOM   3234 C C   . GLY   B 1 125 ? -8.762  39.468 -49.930 1.00 16.30 ? 147 GLY   B C   1 
ATOM   3235 O O   . GLY   B 1 125 ? -9.922  39.569 -49.535 1.00 15.61 ? 147 GLY   B O   1 
ATOM   3236 N N   . SER   B 1 126 ? -8.316  39.981 -51.088 1.00 16.44 ? 148 SER   B N   1 
ATOM   3237 C CA  . SER   B 1 126 ? -9.147  40.841 -51.910 1.00 17.11 ? 148 SER   B CA  1 
ATOM   3238 C C   . SER   B 1 126 ? -9.084  40.467 -53.391 1.00 18.01 ? 148 SER   B C   1 
ATOM   3239 O O   . SER   B 1 126 ? -8.173  39.775 -53.863 1.00 17.01 ? 148 SER   B O   1 
ATOM   3240 C CB  . SER   B 1 126 ? -8.742  42.272 -51.646 1.00 17.80 ? 148 SER   B CB  1 
ATOM   3241 O OG  . SER   B 1 126 ? -9.237  43.177 -52.614 1.00 18.09 ? 148 SER   B OG  1 
ATOM   3242 N N   . PHE   B 1 127 ? -10.076 40.973 -54.135 1.00 17.47 ? 149 PHE   B N   1 
ATOM   3243 C CA  . PHE   B 1 127 ? -10.050 40.916 -55.580 1.00 19.16 ? 149 PHE   B CA  1 
ATOM   3244 C C   . PHE   B 1 127 ? -8.870  41.709 -56.132 1.00 18.78 ? 149 PHE   B C   1 
ATOM   3245 O O   . PHE   B 1 127 ? -8.510  41.497 -57.280 1.00 19.04 ? 149 PHE   B O   1 
ATOM   3246 C CB  . PHE   B 1 127 ? -11.392 41.391 -56.142 1.00 18.90 ? 149 PHE   B CB  1 
ATOM   3247 C CG  . PHE   B 1 127 ? -12.395 40.250 -56.203 1.00 20.52 ? 149 PHE   B CG  1 
ATOM   3248 C CD1 . PHE   B 1 127 ? -13.012 39.788 -55.048 1.00 22.15 ? 149 PHE   B CD1 1 
ATOM   3249 C CD2 . PHE   B 1 127 ? -12.716 39.637 -57.407 1.00 21.80 ? 149 PHE   B CD2 1 
ATOM   3250 C CE1 . PHE   B 1 127 ? -13.912 38.735 -55.089 1.00 23.40 ? 149 PHE   B CE1 1 
ATOM   3251 C CE2 . PHE   B 1 127 ? -13.646 38.600 -57.447 1.00 22.51 ? 149 PHE   B CE2 1 
ATOM   3252 C CZ  . PHE   B 1 127 ? -14.213 38.131 -56.279 1.00 23.31 ? 149 PHE   B CZ  1 
ATOM   3253 N N   . ASP   B 1 128 ? -8.256  42.571 -55.308 1.00 18.87 ? 150 ASP   B N   1 
ATOM   3254 C CA  . ASP   B 1 128 ? -7.095  43.341 -55.708 1.00 19.23 ? 150 ASP   B CA  1 
ATOM   3255 C C   . ASP   B 1 128 ? -5.814  42.503 -55.765 1.00 18.97 ? 150 ASP   B C   1 
ATOM   3256 O O   . ASP   B 1 128 ? -4.760  43.049 -56.084 1.00 20.41 ? 150 ASP   B O   1 
ATOM   3257 C CB  . ASP   B 1 128 ? -6.966  44.597 -54.857 1.00 19.51 ? 150 ASP   B CB  1 
ATOM   3258 C CG  . ASP   B 1 128 ? -6.474  44.421 -53.426 1.00 19.07 ? 150 ASP   B CG  1 
ATOM   3259 O OD1 . ASP   B 1 128 ? -6.061  43.293 -53.085 1.00 19.89 ? 150 ASP   B OD1 1 
ATOM   3260 O OD2 . ASP   B 1 128 ? -6.514  45.417 -52.660 1.00 18.80 ? 150 ASP   B OD2 1 
ATOM   3261 N N   . GLU   B 1 129 ? -5.900  41.214 -55.392 1.00 20.04 ? 151 GLU   B N   1 
ATOM   3262 C CA  . GLU   B 1 129 ? -4.857  40.213 -55.555 1.00 20.52 ? 151 GLU   B CA  1 
ATOM   3263 C C   . GLU   B 1 129 ? -3.875  40.239 -54.392 1.00 20.78 ? 151 GLU   B C   1 
ATOM   3264 O O   . GLU   B 1 129 ? -2.918  39.468 -54.394 1.00 21.89 ? 151 GLU   B O   1 
ATOM   3265 C CB  . GLU   B 1 129 ? -4.099  40.337 -56.879 1.00 21.47 ? 151 GLU   B CB  1 
ATOM   3266 C CG  . GLU   B 1 129 ? -5.074  40.359 -58.049 1.00 22.49 ? 151 GLU   B CG  1 
ATOM   3267 C CD  . GLU   B 1 129 ? -4.511  40.335 -59.450 1.00 22.41 ? 151 GLU   B CD  1 
ATOM   3268 O OE1 . GLU   B 1 129 ? -3.273  40.331 -59.618 1.00 23.18 ? 151 GLU   B OE1 1 
ATOM   3269 O OE2 . GLU   B 1 129 ? -5.355  40.303 -60.378 1.00 24.26 ? 151 GLU   B OE2 1 
ATOM   3270 N N   . SER   B 1 130 ? -4.142  41.088 -53.394 1.00 20.06 ? 152 SER   B N   1 
ATOM   3271 C CA  . SER   B 1 130 ? -3.279  41.197 -52.237 1.00 19.75 ? 152 SER   B CA  1 
ATOM   3272 C C   . SER   B 1 130 ? -3.896  40.504 -51.024 1.00 18.36 ? 152 SER   B C   1 
ATOM   3273 O O   . SER   B 1 130 ? -5.112  40.302 -50.918 1.00 17.34 ? 152 SER   B O   1 
ATOM   3274 C CB  . SER   B 1 130 ? -2.965  42.634 -51.921 1.00 21.38 ? 152 SER   B CB  1 
ATOM   3275 O OG  . SER   B 1 130 ? -4.057  43.277 -51.291 1.00 22.15 ? 152 SER   B OG  1 
ATOM   3276 N N   . VAL   B 1 131 ? -2.999  40.184 -50.089 1.00 18.26 ? 153 VAL   B N   1 
ATOM   3277 C CA  . VAL   B 1 131 ? -3.342  39.817 -48.725 1.00 18.52 ? 153 VAL   B CA  1 
ATOM   3278 C C   . VAL   B 1 131 ? -2.793  40.920 -47.829 1.00 19.34 ? 153 VAL   B C   1 
ATOM   3279 O O   . VAL   B 1 131 ? -1.637  41.301 -47.973 1.00 21.58 ? 153 VAL   B O   1 
ATOM   3280 C CB  . VAL   B 1 131 ? -2.717  38.450 -48.383 1.00 18.41 ? 153 VAL   B CB  1 
ATOM   3281 C CG1 . VAL   B 1 131 ? -2.795  38.129 -46.896 1.00 19.23 ? 153 VAL   B CG1 1 
ATOM   3282 C CG2 . VAL   B 1 131 ? -3.326  37.323 -49.212 1.00 17.99 ? 153 VAL   B CG2 1 
ATOM   3283 N N   A ARG   B 1 132 ? -3.626  41.430 -46.921 0.50 20.13 ? 154 ARG   B N   1 
ATOM   3284 N N   B ARG   B 1 132 ? -3.627  41.431 -46.921 0.50 20.01 ? 154 ARG   B N   1 
ATOM   3285 C CA  A ARG   B 1 132 ? -3.199  42.465 -45.997 0.50 20.47 ? 154 ARG   B CA  1 
ATOM   3286 C CA  B ARG   B 1 132 ? -3.213  42.473 -45.999 0.50 20.25 ? 154 ARG   B CA  1 
ATOM   3287 C C   A ARG   B 1 132 ? -3.294  41.936 -44.570 0.50 20.26 ? 154 ARG   B C   1 
ATOM   3288 C C   B ARG   B 1 132 ? -3.303  41.947 -44.569 0.50 20.19 ? 154 ARG   B C   1 
ATOM   3289 O O   A ARG   B 1 132 ? -4.168  41.128 -44.247 0.50 19.14 ? 154 ARG   B O   1 
ATOM   3290 O O   B ARG   B 1 132 ? -4.187  41.152 -44.240 0.50 19.10 ? 154 ARG   B O   1 
ATOM   3291 C CB  A ARG   B 1 132 ? -4.003  43.755 -46.201 0.50 21.44 ? 154 ARG   B CB  1 
ATOM   3292 C CB  B ARG   B 1 132 ? -4.035  43.752 -46.208 0.50 21.12 ? 154 ARG   B CB  1 
ATOM   3293 C CG  A ARG   B 1 132 ? -3.616  44.521 -47.461 0.50 22.31 ? 154 ARG   B CG  1 
ATOM   3294 C CG  B ARG   B 1 132 ? -3.570  44.603 -47.384 0.50 21.77 ? 154 ARG   B CG  1 
ATOM   3295 C CD  A ARG   B 1 132 ? -4.462  45.773 -47.639 0.50 24.23 ? 154 ARG   B CD  1 
ATOM   3296 C CD  B ARG   B 1 132 ? -4.425  45.852 -47.565 0.50 23.54 ? 154 ARG   B CD  1 
ATOM   3297 N NE  A ARG   B 1 132 ? -4.054  46.619 -48.765 0.50 26.29 ? 154 ARG   B NE  1 
ATOM   3298 N NE  B ARG   B 1 132 ? -3.707  46.947 -48.227 0.50 25.22 ? 154 ARG   B NE  1 
ATOM   3299 C CZ  A ARG   B 1 132 ? -3.454  47.802 -48.636 0.50 27.98 ? 154 ARG   B CZ  1 
ATOM   3300 C CZ  B ARG   B 1 132 ? -3.488  47.039 -49.538 0.50 26.55 ? 154 ARG   B CZ  1 
ATOM   3301 N NH1 A ARG   B 1 132 ? -3.080  48.240 -47.445 0.50 29.07 ? 154 ARG   B NH1 1 
ATOM   3302 N NH1 B ARG   B 1 132 ? -4.030  46.172 -50.377 0.50 26.70 ? 154 ARG   B NH1 1 
ATOM   3303 N NH2 A ARG   B 1 132 ? -3.226  48.543 -49.705 0.50 29.08 ? 154 ARG   B NH2 1 
ATOM   3304 N NH2 B ARG   B 1 132 ? -2.743  48.022 -50.005 0.50 28.18 ? 154 ARG   B NH2 1 
ATOM   3305 N N   . ILE   B 1 133 ? -2.367  42.412 -43.736 1.00 20.22 ? 155 ILE   B N   1 
ATOM   3306 C CA  . ILE   B 1 133 ? -2.345  42.113 -42.313 1.00 20.71 ? 155 ILE   B CA  1 
ATOM   3307 C C   . ILE   B 1 133 ? -2.544  43.439 -41.587 1.00 21.25 ? 155 ILE   B C   1 
ATOM   3308 O O   . ILE   B 1 133 ? -1.815  44.397 -41.844 1.00 22.21 ? 155 ILE   B O   1 
ATOM   3309 C CB  . ILE   B 1 133 ? -1.028  41.422 -41.907 1.00 22.31 ? 155 ILE   B CB  1 
ATOM   3310 C CG1 . ILE   B 1 133 ? -0.745  40.184 -42.764 1.00 21.08 ? 155 ILE   B CG1 1 
ATOM   3311 C CG2 . ILE   B 1 133 ? -1.025  41.079 -40.413 1.00 22.36 ? 155 ILE   B CG2 1 
ATOM   3312 C CD1 . ILE   B 1 133 ? 0.609   39.537 -42.505 1.00 21.79 ? 155 ILE   B CD1 1 
ATOM   3313 N N   . TRP   B 1 134 ? -3.521  43.460 -40.675 1.00 19.60 ? 156 TRP   B N   1 
ATOM   3314 C CA  . TRP   B 1 134 ? -3.995  44.663 -40.023 1.00 20.78 ? 156 TRP   B CA  1 
ATOM   3315 C C   . TRP   B 1 134 ? -3.811  44.516 -38.518 1.00 20.73 ? 156 TRP   B C   1 
ATOM   3316 O O   . TRP   B 1 134 ? -4.031  43.439 -37.957 1.00 19.02 ? 156 TRP   B O   1 
ATOM   3317 C CB  . TRP   B 1 134 ? -5.486  44.868 -40.307 1.00 20.47 ? 156 TRP   B CB  1 
ATOM   3318 C CG  . TRP   B 1 134 ? -5.891  44.799 -41.758 1.00 19.57 ? 156 TRP   B CG  1 
ATOM   3319 C CD1 . TRP   B 1 134 ? -6.190  43.693 -42.498 1.00 19.85 ? 156 TRP   B CD1 1 
ATOM   3320 C CD2 . TRP   B 1 134 ? -6.117  45.929 -42.618 1.00 19.88 ? 156 TRP   B CD2 1 
ATOM   3321 N NE1 . TRP   B 1 134 ? -6.553  44.046 -43.770 1.00 19.34 ? 156 TRP   B NE1 1 
ATOM   3322 C CE2 . TRP   B 1 134 ? -6.519  45.418 -43.869 1.00 19.89 ? 156 TRP   B CE2 1 
ATOM   3323 C CE3 . TRP   B 1 134 ? -6.000  47.312 -42.447 1.00 20.34 ? 156 TRP   B CE3 1 
ATOM   3324 C CZ2 . TRP   B 1 134 ? -6.832  46.261 -44.929 1.00 20.52 ? 156 TRP   B CZ2 1 
ATOM   3325 C CZ3 . TRP   B 1 134 ? -6.304  48.139 -43.498 1.00 20.92 ? 156 TRP   B CZ3 1 
ATOM   3326 C CH2 . TRP   B 1 134 ? -6.707  47.616 -44.722 1.00 20.85 ? 156 TRP   B CH2 1 
ATOM   3327 N N   . ASP   B 1 135 ? -3.476  45.633 -37.885 1.00 21.98 ? 157 ASP   B N   1 
ATOM   3328 C CA  . ASP   B 1 135 ? -3.466  45.753 -36.443 1.00 23.74 ? 157 ASP   B CA  1 
ATOM   3329 C C   . ASP   B 1 135 ? -4.886  46.027 -35.945 1.00 23.79 ? 157 ASP   B C   1 
ATOM   3330 O O   . ASP   B 1 135 ? -5.504  47.021 -36.314 1.00 25.13 ? 157 ASP   B O   1 
ATOM   3331 C CB  . ASP   B 1 135 ? -2.548  46.889 -36.027 1.00 24.97 ? 157 ASP   B CB  1 
ATOM   3332 C CG  . ASP   B 1 135 ? -2.340  46.951 -34.527 1.00 27.94 ? 157 ASP   B CG  1 
ATOM   3333 O OD1 . ASP   B 1 135 ? -1.573  46.120 -34.021 1.00 34.18 ? 157 ASP   B OD1 1 
ATOM   3334 O OD2 . ASP   B 1 135 ? -3.029  47.750 -33.878 1.00 33.40 ? 157 ASP   B OD2 1 
ATOM   3335 N N   . VAL   B 1 136 ? -5.393  45.154 -35.069 1.00 22.58 ? 158 VAL   B N   1 
ATOM   3336 C CA  . VAL   B 1 136 ? -6.752  45.287 -34.574 1.00 22.55 ? 158 VAL   B CA  1 
ATOM   3337 C C   . VAL   B 1 136 ? -6.908  46.557 -33.737 1.00 23.90 ? 158 VAL   B C   1 
ATOM   3338 O O   . VAL   B 1 136 ? -7.917  47.241 -33.844 1.00 25.95 ? 158 VAL   B O   1 
ATOM   3339 C CB  . VAL   B 1 136 ? -7.145  44.022 -33.793 1.00 21.14 ? 158 VAL   B CB  1 
ATOM   3340 C CG1 . VAL   B 1 136 ? -8.412  44.225 -32.963 1.00 21.83 ? 158 VAL   B CG1 1 
ATOM   3341 C CG2 . VAL   B 1 136 ? -7.291  42.830 -34.724 1.00 19.84 ? 158 VAL   B CG2 1 
ATOM   3342 N N   . LYS   B 1 137 ? -5.912  46.864 -32.902 1.00 26.10 ? 159 LYS   B N   1 
ATOM   3343 C CA  . LYS   B 1 137 ? -6.032  47.954 -31.946 1.00 29.96 ? 159 LYS   B CA  1 
ATOM   3344 C C   . LYS   B 1 137 ? -6.035  49.298 -32.669 1.00 30.00 ? 159 LYS   B C   1 
ATOM   3345 O O   . LYS   B 1 137 ? -6.818  50.169 -32.308 1.00 33.21 ? 159 LYS   B O   1 
ATOM   3346 C CB  . LYS   B 1 137 ? -4.940  47.878 -30.871 1.00 32.75 ? 159 LYS   B CB  1 
ATOM   3347 C CG  . LYS   B 1 137 ? -5.125  46.748 -29.857 1.00 36.41 ? 159 LYS   B CG  1 
ATOM   3348 N N   . THR   B 1 138 ? -5.175  49.477 -33.683 1.00 31.62 ? 160 THR   B N   1 
ATOM   3349 C CA  . THR   B 1 138 ? -5.068  50.774 -34.351 1.00 32.28 ? 160 THR   B CA  1 
ATOM   3350 C C   . THR   B 1 138 ? -5.912  50.805 -35.623 1.00 32.31 ? 160 THR   B C   1 
ATOM   3351 O O   . THR   B 1 138 ? -6.288  51.878 -36.082 1.00 34.16 ? 160 THR   B O   1 
ATOM   3352 C CB  . THR   B 1 138 ? -3.614  51.124 -34.683 1.00 31.87 ? 160 THR   B CB  1 
ATOM   3353 O OG1 . THR   B 1 138 ? -3.182  50.148 -35.629 1.00 31.63 ? 160 THR   B OG1 1 
ATOM   3354 C CG2 . THR   B 1 138 ? -2.718  51.127 -33.458 1.00 32.67 ? 160 THR   B CG2 1 
ATOM   3355 N N   . GLY   B 1 139 ? -6.143  49.645 -36.238 1.00 30.67 ? 161 GLY   B N   1 
ATOM   3356 C CA  . GLY   B 1 139 ? -6.843  49.594 -37.510 1.00 31.92 ? 161 GLY   B CA  1 
ATOM   3357 C C   . GLY   B 1 139 ? -5.922  49.909 -38.686 1.00 30.46 ? 161 GLY   B C   1 
ATOM   3358 O O   . GLY   B 1 139 ? -6.395  50.036 -39.814 1.00 34.38 ? 161 GLY   B O   1 
ATOM   3359 N N   . LYS   B 1 140 ? -4.612  50.036 -38.437 1.00 30.41 ? 162 LYS   B N   1 
ATOM   3360 C CA  . LYS   B 1 140 ? -3.677  50.354 -39.505 1.00 31.88 ? 162 LYS   B CA  1 
ATOM   3361 C C   . LYS   B 1 140 ? -3.293  49.052 -40.198 1.00 29.13 ? 162 LYS   B C   1 
ATOM   3362 O O   . LYS   B 1 140 ? -3.213  47.995 -39.569 1.00 27.97 ? 162 LYS   B O   1 
ATOM   3363 C CB  . LYS   B 1 140 ? -2.416  51.082 -39.029 1.00 32.34 ? 162 LYS   B CB  1 
ATOM   3364 N N   . CYS   B 1 141 ? -3.086  49.144 -41.510 1.00 27.30 ? 163 CYS   B N   1 
ATOM   3365 C CA  . CYS   B 1 141 ? -2.509  48.051 -42.265 1.00 27.50 ? 163 CYS   B CA  1 
ATOM   3366 C C   . CYS   B 1 141 ? -1.015  47.965 -41.948 1.00 27.73 ? 163 CYS   B C   1 
ATOM   3367 O O   . CYS   B 1 141 ? -0.294  48.953 -42.083 1.00 30.03 ? 163 CYS   B O   1 
ATOM   3368 C CB  . CYS   B 1 141 ? -2.745  48.245 -43.755 1.00 28.15 ? 163 CYS   B CB  1 
ATOM   3369 S SG  . CYS   B 1 141 ? -2.145  46.850 -44.729 1.00 29.39 ? 163 CYS   B SG  1 
ATOM   3370 N N   . LEU   B 1 142 ? -0.571  46.774 -41.527 1.00 27.50 ? 164 LEU   B N   1 
ATOM   3371 C CA  . LEU   B 1 142 ? 0.805   46.540 -41.129 1.00 28.00 ? 164 LEU   B CA  1 
ATOM   3372 C C   . LEU   B 1 142 ? 1.633   46.058 -42.308 1.00 27.27 ? 164 LEU   B C   1 
ATOM   3373 O O   . LEU   B 1 142 ? 2.788   46.448 -42.424 1.00 28.72 ? 164 LEU   B O   1 
ATOM   3374 C CB  . LEU   B 1 142 ? 0.878   45.526 -39.994 1.00 27.09 ? 164 LEU   B CB  1 
ATOM   3375 C CG  . LEU   B 1 142 ? 0.330   46.000 -38.649 1.00 29.59 ? 164 LEU   B CG  1 
ATOM   3376 C CD1 . LEU   B 1 142 ? 0.309   44.820 -37.690 1.00 30.69 ? 164 LEU   B CD1 1 
ATOM   3377 C CD2 . LEU   B 1 142 ? 1.129   47.161 -38.074 1.00 31.44 ? 164 LEU   B CD2 1 
ATOM   3378 N N   . LYS   B 1 143 ? 1.053   45.183 -43.138 1.00 27.76 ? 165 LYS   B N   1 
ATOM   3379 C CA  . LYS   B 1 143 ? 1.759   44.633 -44.283 1.00 28.62 ? 165 LYS   B CA  1 
ATOM   3380 C C   . LYS   B 1 143 ? 0.778   44.406 -45.425 1.00 27.47 ? 165 LYS   B C   1 
ATOM   3381 O O   . LYS   B 1 143 ? -0.385  44.069 -45.190 1.00 25.46 ? 165 LYS   B O   1 
ATOM   3382 C CB  . LYS   B 1 143 ? 2.465   43.312 -43.964 1.00 29.34 ? 165 LYS   B CB  1 
ATOM   3383 C CG  . LYS   B 1 143 ? 3.673   43.432 -43.052 1.00 31.70 ? 165 LYS   B CG  1 
ATOM   3384 C CD  . LYS   B 1 143 ? 4.353   42.097 -42.787 1.00 35.01 ? 165 LYS   B CD  1 
ATOM   3385 C CE  . LYS   B 1 143 ? 5.666   42.245 -42.069 1.00 36.82 ? 165 LYS   B CE  1 
ATOM   3386 N NZ  . LYS   B 1 143 ? 5.561   42.801 -40.715 1.00 37.49 ? 165 LYS   B NZ  1 
ATOM   3387 N N   . THR   B 1 144 ? 1.280   44.612 -46.652 1.00 26.70 ? 166 THR   B N   1 
ATOM   3388 C CA  . THR   B 1 144 ? 0.563   44.226 -47.858 1.00 26.08 ? 166 THR   B CA  1 
ATOM   3389 C C   . THR   B 1 144 ? 1.417   43.199 -48.591 1.00 26.38 ? 166 THR   B C   1 
ATOM   3390 O O   . THR   B 1 144 ? 2.520   43.525 -49.043 1.00 28.56 ? 166 THR   B O   1 
ATOM   3391 C CB  . THR   B 1 144 ? 0.301   45.447 -48.745 1.00 27.31 ? 166 THR   B CB  1 
ATOM   3392 O OG1 . THR   B 1 144 ? -0.400  46.432 -47.990 1.00 28.73 ? 166 THR   B OG1 1 
ATOM   3393 C CG2 . THR   B 1 144 ? -0.516  45.081 -49.969 1.00 27.35 ? 166 THR   B CG2 1 
ATOM   3394 N N   . LEU   B 1 145 ? 0.916   41.962 -48.673 1.00 25.83 ? 167 LEU   B N   1 
ATOM   3395 C CA  . LEU   B 1 145 ? 1.607   40.894 -49.368 1.00 25.24 ? 167 LEU   B CA  1 
ATOM   3396 C C   . LEU   B 1 145 ? 1.166   40.901 -50.829 1.00 25.85 ? 167 LEU   B C   1 
ATOM   3397 O O   . LEU   B 1 145 ? -0.024  40.821 -51.109 1.00 24.96 ? 167 LEU   B O   1 
ATOM   3398 C CB  . LEU   B 1 145 ? 1.304   39.558 -48.697 1.00 26.32 ? 167 LEU   B CB  1 
ATOM   3399 C CG  . LEU   B 1 145 ? 1.430   39.516 -47.170 1.00 27.44 ? 167 LEU   B CG  1 
ATOM   3400 C CD1 . LEU   B 1 145 ? 1.246   38.088 -46.646 1.00 27.68 ? 167 LEU   B CD1 1 
ATOM   3401 C CD2 . LEU   B 1 145 ? 2.742   40.097 -46.690 1.00 29.46 ? 167 LEU   B CD2 1 
ATOM   3402 N N   . PRO   B 1 146 ? 2.095   40.962 -51.811 1.00 27.76 ? 168 PRO   B N   1 
ATOM   3403 C CA  . PRO   B 1 146 ? 1.727   40.786 -53.217 1.00 27.79 ? 168 PRO   B CA  1 
ATOM   3404 C C   . PRO   B 1 146 ? 1.511   39.293 -53.467 1.00 25.65 ? 168 PRO   B C   1 
ATOM   3405 O O   . PRO   B 1 146 ? 2.315   38.624 -54.114 1.00 26.01 ? 168 PRO   B O   1 
ATOM   3406 C CB  . PRO   B 1 146 ? 2.955   41.374 -53.930 1.00 29.67 ? 168 PRO   B CB  1 
ATOM   3407 C CG  . PRO   B 1 146 ? 4.108   40.985 -53.037 1.00 29.27 ? 168 PRO   B CG  1 
ATOM   3408 C CD  . PRO   B 1 146 ? 3.543   41.155 -51.629 1.00 29.92 ? 168 PRO   B CD  1 
ATOM   3409 N N   . ALA   B 1 147 ? 0.406   38.765 -52.932 1.00 23.12 ? 169 ALA   B N   1 
ATOM   3410 C CA  . ALA   B 1 147 ? 0.299   37.341 -52.660 1.00 22.89 ? 169 ALA   B CA  1 
ATOM   3411 C C   . ALA   B 1 147 ? -0.023  36.525 -53.903 1.00 22.06 ? 169 ALA   B C   1 
ATOM   3412 O O   . ALA   B 1 147 ? 0.454   35.401 -54.024 1.00 22.52 ? 169 ALA   B O   1 
ATOM   3413 C CB  . ALA   B 1 147 ? -0.732  37.101 -51.609 1.00 22.67 ? 169 ALA   B CB  1 
ATOM   3414 N N   . HIS   B 1 148 ? -0.846  37.088 -54.796 1.00 21.29 ? 170 HIS   B N   1 
ATOM   3415 C CA  . HIS   B 1 148 ? -1.384  36.330 -55.908 1.00 20.79 ? 170 HIS   B CA  1 
ATOM   3416 C C   . HIS   B 1 148 ? -1.513  37.213 -57.144 1.00 21.24 ? 170 HIS   B C   1 
ATOM   3417 O O   . HIS   B 1 148 ? -1.299  38.427 -57.087 1.00 21.48 ? 170 HIS   B O   1 
ATOM   3418 C CB  . HIS   B 1 148 ? -2.723  35.726 -55.477 1.00 19.82 ? 170 HIS   B CB  1 
ATOM   3419 C CG  . HIS   B 1 148 ? -2.582  34.696 -54.415 1.00 19.12 ? 170 HIS   B CG  1 
ATOM   3420 N ND1 . HIS   B 1 148 ? -2.103  33.457 -54.757 1.00 18.75 ? 170 HIS   B ND1 1 
ATOM   3421 C CD2 . HIS   B 1 148 ? -2.802  34.656 -53.087 1.00 19.36 ? 170 HIS   B CD2 1 
ATOM   3422 C CE1 . HIS   B 1 148 ? -2.065  32.694 -53.673 1.00 20.14 ? 170 HIS   B CE1 1 
ATOM   3423 N NE2 . HIS   B 1 148 ? -2.486  33.395 -52.654 1.00 19.86 ? 170 HIS   B NE2 1 
ATOM   3424 N N   . SER   B 1 149 ? -1.895  36.577 -58.257 1.00 21.15 ? 171 SER   B N   1 
ATOM   3425 C CA  . SER   B 1 149 ? -2.035  37.256 -59.538 1.00 21.63 ? 171 SER   B CA  1 
ATOM   3426 C C   . SER   B 1 149 ? -3.471  37.157 -60.060 1.00 21.70 ? 171 SER   B C   1 
ATOM   3427 O O   . SER   B 1 149 ? -3.739  37.285 -61.260 1.00 21.62 ? 171 SER   B O   1 
ATOM   3428 C CB  . SER   B 1 149 ? -1.020  36.718 -60.529 1.00 21.02 ? 171 SER   B CB  1 
ATOM   3429 O OG  . SER   B 1 149 ? -1.221  35.340 -60.810 1.00 22.11 ? 171 SER   B OG  1 
ATOM   3430 N N   . ASP   B 1 150 ? -4.401  36.960 -59.125 1.00 22.49 ? 172 ASP   B N   1 
ATOM   3431 C CA  . ASP   B 1 150 ? -5.821  36.866 -59.393 1.00 21.27 ? 172 ASP   B CA  1 
ATOM   3432 C C   . ASP   B 1 150 ? -6.513  37.010 -58.039 1.00 20.29 ? 172 ASP   B C   1 
ATOM   3433 O O   . ASP   B 1 150 ? -5.845  37.064 -57.007 1.00 19.92 ? 172 ASP   B O   1 
ATOM   3434 C CB  . ASP   B 1 150 ? -6.189  35.560 -60.090 1.00 22.66 ? 172 ASP   B CB  1 
ATOM   3435 C CG  . ASP   B 1 150 ? -6.109  35.552 -61.609 1.00 23.85 ? 172 ASP   B CG  1 
ATOM   3436 O OD1 . ASP   B 1 150 ? -6.670  36.489 -62.217 1.00 25.15 ? 172 ASP   B OD1 1 
ATOM   3437 O OD2 . ASP   B 1 150 ? -5.512  34.594 -62.174 1.00 25.12 ? 172 ASP   B OD2 1 
ATOM   3438 N N   . PRO   B 1 151 ? -7.854  37.125 -57.992 1.00 19.71 ? 173 PRO   B N   1 
ATOM   3439 C CA  . PRO   B 1 151 ? -8.552  37.260 -56.713 1.00 19.43 ? 173 PRO   B CA  1 
ATOM   3440 C C   . PRO   B 1 151 ? -8.160  36.219 -55.670 1.00 18.42 ? 173 PRO   B C   1 
ATOM   3441 O O   . PRO   B 1 151 ? -7.937  35.044 -55.991 1.00 18.83 ? 173 PRO   B O   1 
ATOM   3442 C CB  . PRO   B 1 151 ? -10.031 37.174 -57.132 1.00 20.04 ? 173 PRO   B CB  1 
ATOM   3443 C CG  . PRO   B 1 151 ? -10.012 37.792 -58.524 1.00 20.50 ? 173 PRO   B CG  1 
ATOM   3444 C CD  . PRO   B 1 151 ? -8.749  37.243 -59.158 1.00 20.57 ? 173 PRO   B CD  1 
ATOM   3445 N N   . VAL   B 1 152 ? -8.095  36.682 -54.419 1.00 16.91 ? 174 VAL   B N   1 
ATOM   3446 C CA  . VAL   B 1 152 ? -7.743  35.845 -53.284 1.00 17.04 ? 174 VAL   B CA  1 
ATOM   3447 C C   . VAL   B 1 152 ? -9.034  35.268 -52.704 1.00 16.82 ? 174 VAL   B C   1 
ATOM   3448 O O   . VAL   B 1 152 ? -9.919  36.018 -52.279 1.00 17.12 ? 174 VAL   B O   1 
ATOM   3449 C CB  . VAL   B 1 152 ? -6.941  36.645 -52.240 1.00 17.25 ? 174 VAL   B CB  1 
ATOM   3450 C CG1 . VAL   B 1 152 ? -6.606  35.809 -51.012 1.00 17.60 ? 174 VAL   B CG1 1 
ATOM   3451 C CG2 . VAL   B 1 152 ? -5.676  37.239 -52.855 1.00 17.97 ? 174 VAL   B CG2 1 
ATOM   3452 N N   . SER   B 1 153 ? -9.129  33.931 -52.695 1.00 16.74 ? 175 SER   B N   1 
ATOM   3453 C CA  . SER   B 1 153 ? -10.355 33.254 -52.298 1.00 17.01 ? 175 SER   B CA  1 
ATOM   3454 C C   . SER   B 1 153 ? -10.430 32.992 -50.788 1.00 16.64 ? 175 SER   B C   1 
ATOM   3455 O O   . SER   B 1 153 ? -11.541 32.912 -50.225 1.00 16.81 ? 175 SER   B O   1 
ATOM   3456 C CB  . SER   B 1 153 ? -10.526 31.979 -53.094 1.00 17.82 ? 175 SER   B CB  1 
ATOM   3457 O OG  . SER   B 1 153 ? -9.355  31.190 -53.024 1.00 18.24 ? 175 SER   B OG  1 
ATOM   3458 N N   . ALA   B 1 154 ? -9.273  32.803 -50.131 1.00 15.59 ? 176 ALA   B N   1 
ATOM   3459 C CA  . ALA   B 1 154 ? -9.267  32.506 -48.704 1.00 15.15 ? 176 ALA   B CA  1 
ATOM   3460 C C   . ALA   B 1 154 ? -7.961  32.937 -48.043 1.00 15.19 ? 176 ALA   B C   1 
ATOM   3461 O O   . ALA   B 1 154 ? -6.903  32.936 -48.674 1.00 15.22 ? 176 ALA   B O   1 
ATOM   3462 C CB  . ALA   B 1 154 ? -9.506  31.032 -48.464 1.00 14.86 ? 176 ALA   B CB  1 
ATOM   3463 N N   . VAL   B 1 155 ? -8.076  33.259 -46.752 1.00 14.95 ? 177 VAL   B N   1 
ATOM   3464 C CA  . VAL   B 1 155 ? -6.939  33.551 -45.896 1.00 15.06 ? 177 VAL   B CA  1 
ATOM   3465 C C   . VAL   B 1 155 ? -7.231  32.971 -44.521 1.00 15.10 ? 177 VAL   B C   1 
ATOM   3466 O O   . VAL   B 1 155 ? -8.335  33.115 -44.008 1.00 15.52 ? 177 VAL   B O   1 
ATOM   3467 C CB  . VAL   B 1 155 ? -6.621  35.056 -45.790 1.00 15.37 ? 177 VAL   B CB  1 
ATOM   3468 C CG1 . VAL   B 1 155 ? -6.035  35.618 -47.076 1.00 16.03 ? 177 VAL   B CG1 1 
ATOM   3469 C CG2 . VAL   B 1 155 ? -7.820  35.874 -45.335 1.00 15.73 ? 177 VAL   B CG2 1 
ATOM   3470 N N   . HIS   B 1 156 ? -6.227  32.329 -43.925 1.00 15.77 ? 178 HIS   B N   1 
ATOM   3471 C CA  . HIS   B 1 156 ? -6.405  31.687 -42.629 1.00 15.48 ? 178 HIS   B CA  1 
ATOM   3472 C C   . HIS   B 1 156 ? -5.077  31.625 -41.878 1.00 16.37 ? 178 HIS   B C   1 
ATOM   3473 O O   . HIS   B 1 156 ? -4.043  31.308 -42.460 1.00 17.54 ? 178 HIS   B O   1 
ATOM   3474 C CB  . HIS   B 1 156 ? -6.944  30.273 -42.845 1.00 16.06 ? 178 HIS   B CB  1 
ATOM   3475 C CG  . HIS   B 1 156 ? -7.352  29.538 -41.615 1.00 17.01 ? 178 HIS   B CG  1 
ATOM   3476 N ND1 . HIS   B 1 156 ? -6.826  28.308 -41.274 1.00 18.21 ? 178 HIS   B ND1 1 
ATOM   3477 C CD2 . HIS   B 1 156 ? -8.192  29.870 -40.628 1.00 17.42 ? 178 HIS   B CD2 1 
ATOM   3478 C CE1 . HIS   B 1 156 ? -7.370  27.919 -40.134 1.00 17.72 ? 178 HIS   B CE1 1 
ATOM   3479 N NE2 . HIS   B 1 156 ? -8.206  28.853 -39.727 1.00 16.64 ? 178 HIS   B NE2 1 
ATOM   3480 N N   . PHE   B 1 157 ? -5.118  31.917 -40.579 1.00 16.70 ? 179 PHE   B N   1 
ATOM   3481 C CA  . PHE   B 1 157 ? -3.964  31.720 -39.705 1.00 17.04 ? 179 PHE   B CA  1 
ATOM   3482 C C   . PHE   B 1 157 ? -3.937  30.291 -39.172 1.00 17.90 ? 179 PHE   B C   1 
ATOM   3483 O O   . PHE   B 1 157 ? -4.986  29.688 -38.924 1.00 17.62 ? 179 PHE   B O   1 
ATOM   3484 C CB  . PHE   B 1 157 ? -3.973  32.634 -38.482 1.00 16.46 ? 179 PHE   B CB  1 
ATOM   3485 C CG  . PHE   B 1 157 ? -3.662  34.102 -38.739 1.00 15.87 ? 179 PHE   B CG  1 
ATOM   3486 C CD1 . PHE   B 1 157 ? -2.345  34.561 -38.749 1.00 17.06 ? 179 PHE   B CD1 1 
ATOM   3487 C CD2 . PHE   B 1 157 ? -4.686  35.019 -38.937 1.00 15.11 ? 179 PHE   B CD2 1 
ATOM   3488 C CE1 . PHE   B 1 157 ? -2.066  35.906 -38.938 1.00 16.26 ? 179 PHE   B CE1 1 
ATOM   3489 C CE2 . PHE   B 1 157 ? -4.402  36.357 -39.130 1.00 15.90 ? 179 PHE   B CE2 1 
ATOM   3490 C CZ  . PHE   B 1 157 ? -3.096  36.800 -39.128 1.00 16.27 ? 179 PHE   B CZ  1 
ATOM   3491 N N   . ASN   B 1 158 ? -2.724  29.777 -38.931 1.00 18.21 ? 180 ASN   B N   1 
ATOM   3492 C CA  . ASN   B 1 158 ? -2.597  28.486 -38.273 1.00 18.38 ? 180 ASN   B CA  1 
ATOM   3493 C C   . ASN   B 1 158 ? -2.821  28.654 -36.771 1.00 18.98 ? 180 ASN   B C   1 
ATOM   3494 O O   . ASN   B 1 158 ? -3.065  29.757 -36.289 1.00 17.36 ? 180 ASN   B O   1 
ATOM   3495 C CB  . ASN   B 1 158 ? -1.267  27.820 -38.598 1.00 18.65 ? 180 ASN   B CB  1 
ATOM   3496 C CG  . ASN   B 1 158 ? -0.109  28.506 -37.928 1.00 20.10 ? 180 ASN   B CG  1 
ATOM   3497 O OD1 . ASN   B 1 158 ? -0.214  29.667 -37.518 1.00 19.80 ? 180 ASN   B OD1 1 
ATOM   3498 N ND2 . ASN   B 1 158 ? 1.008   27.806 -37.811 1.00 23.68 ? 180 ASN   B ND2 1 
ATOM   3499 N N   . ARG   B 1 159 ? -2.731  27.522 -36.062 1.00 20.79 ? 181 ARG   B N   1 
ATOM   3500 C CA  . ARG   B 1 159 ? -3.170  27.370 -34.684 1.00 22.31 ? 181 ARG   B CA  1 
ATOM   3501 C C   . ARG   B 1 159 ? -2.457  28.313 -33.717 1.00 20.90 ? 181 ARG   B C   1 
ATOM   3502 O O   . ARG   B 1 159 ? -2.999  28.612 -32.652 1.00 20.83 ? 181 ARG   B O   1 
ATOM   3503 C CB  . ARG   B 1 159 ? -2.896  25.909 -34.302 1.00 26.66 ? 181 ARG   B CB  1 
ATOM   3504 C CG  . ARG   B 1 159 ? -1.421  25.529 -34.365 1.00 29.31 ? 181 ARG   B CG  1 
ATOM   3505 C CD  . ARG   B 1 159 ? -1.161  24.058 -34.091 1.00 32.70 ? 181 ARG   B CD  1 
ATOM   3506 N NE  . ARG   B 1 159 ? 0.252   23.727 -34.317 1.00 35.26 ? 181 ARG   B NE  1 
ATOM   3507 C CZ  . ARG   B 1 159 ? 1.140   23.474 -33.359 1.00 39.20 ? 181 ARG   B CZ  1 
ATOM   3508 N NH1 . ARG   B 1 159 ? 2.390   23.175 -33.668 1.00 41.26 ? 181 ARG   B NH1 1 
ATOM   3509 N NH2 . ARG   B 1 159 ? 0.787   23.519 -32.086 1.00 41.88 ? 181 ARG   B NH2 1 
ATOM   3510 N N   . ASP   B 1 160 ? -1.222  28.727 -34.028 1.00 19.78 ? 182 ASP   B N   1 
ATOM   3511 C CA  . ASP   B 1 160 ? -0.491  29.605 -33.122 1.00 19.95 ? 182 ASP   B CA  1 
ATOM   3512 C C   . ASP   B 1 160 ? -0.296  31.009 -33.700 1.00 18.66 ? 182 ASP   B C   1 
ATOM   3513 O O   . ASP   B 1 160 ? 0.343   31.851 -33.061 1.00 18.94 ? 182 ASP   B O   1 
ATOM   3514 C CB  . ASP   B 1 160 ? 0.803   28.958 -32.669 1.00 21.45 ? 182 ASP   B CB  1 
ATOM   3515 C CG  . ASP   B 1 160 ? 1.882   28.828 -33.726 1.00 22.60 ? 182 ASP   B CG  1 
ATOM   3516 O OD1 . ASP   B 1 160 ? 1.630   29.177 -34.908 1.00 22.87 ? 182 ASP   B OD1 1 
ATOM   3517 O OD2 . ASP   B 1 160 ? 2.964   28.367 -33.353 1.00 28.04 ? 182 ASP   B OD2 1 
ATOM   3518 N N   . GLY   B 1 161 ? -0.814  31.251 -34.911 1.00 18.91 ? 183 GLY   B N   1 
ATOM   3519 C CA  . GLY   B 1 161 ? -0.768  32.567 -35.542 1.00 19.69 ? 183 GLY   B CA  1 
ATOM   3520 C C   . GLY   B 1 161 ? 0.541   32.852 -36.292 1.00 20.22 ? 183 GLY   B C   1 
ATOM   3521 O O   . GLY   B 1 161 ? 0.683   33.919 -36.886 1.00 20.47 ? 183 GLY   B O   1 
ATOM   3522 N N   . SER   B 1 162 ? 1.499   31.911 -36.277 1.00 20.28 ? 184 SER   B N   1 
ATOM   3523 C CA  . SER   B 1 162 ? 2.812   32.151 -36.863 1.00 21.26 ? 184 SER   B CA  1 
ATOM   3524 C C   . SER   B 1 162 ? 2.774   32.092 -38.393 1.00 21.07 ? 184 SER   B C   1 
ATOM   3525 O O   . SER   B 1 162 ? 3.681   32.615 -39.046 1.00 22.28 ? 184 SER   B O   1 
ATOM   3526 C CB  . SER   B 1 162 ? 3.847   31.195 -36.325 1.00 22.19 ? 184 SER   B CB  1 
ATOM   3527 O OG  . SER   B 1 162 ? 3.512   29.847 -36.627 1.00 23.91 ? 184 SER   B OG  1 
ATOM   3528 N N   . LEU   B 1 163 ? 1.751   31.436 -38.963 1.00 21.66 ? 185 LEU   B N   1 
ATOM   3529 C CA  . LEU   B 1 163 ? 1.658   31.238 -40.401 1.00 20.52 ? 185 LEU   B CA  1 
ATOM   3530 C C   . LEU   B 1 163 ? 0.288   31.697 -40.875 1.00 20.03 ? 185 LEU   B C   1 
ATOM   3531 O O   . LEU   B 1 163 ? -0.685  31.624 -40.126 1.00 18.84 ? 185 LEU   B O   1 
ATOM   3532 C CB  . LEU   B 1 163 ? 1.821   29.777 -40.821 1.00 22.32 ? 185 LEU   B CB  1 
ATOM   3533 C CG  . LEU   B 1 163 ? 3.107   29.065 -40.410 1.00 23.87 ? 185 LEU   B CG  1 
ATOM   3534 C CD1 . LEU   B 1 163 ? 3.002   27.624 -40.849 1.00 25.71 ? 185 LEU   B CD1 1 
ATOM   3535 C CD2 . LEU   B 1 163 ? 4.314   29.745 -40.980 1.00 24.49 ? 185 LEU   B CD2 1 
ATOM   3536 N N   . ILE   B 1 164 ? 0.257   32.100 -42.148 1.00 18.99 ? 186 ILE   B N   1 
ATOM   3537 C CA  . ILE   B 1 164 ? -0.951  32.407 -42.894 1.00 18.40 ? 186 ILE   B CA  1 
ATOM   3538 C C   . ILE   B 1 164 ? -0.953  31.526 -44.137 1.00 17.99 ? 186 ILE   B C   1 
ATOM   3539 O O   . ILE   B 1 164 ? 0.074   31.367 -44.792 1.00 19.32 ? 186 ILE   B O   1 
ATOM   3540 C CB  . ILE   B 1 164 ? -0.986  33.891 -43.310 1.00 18.49 ? 186 ILE   B CB  1 
ATOM   3541 C CG1 . ILE   B 1 164 ? -1.118  34.810 -42.115 1.00 18.38 ? 186 ILE   B CG1 1 
ATOM   3542 C CG2 . ILE   B 1 164 ? -2.063  34.174 -44.367 1.00 18.88 ? 186 ILE   B CG2 1 
ATOM   3543 C CD1 . ILE   B 1 164 ? -0.699  36.235 -42.414 1.00 19.21 ? 186 ILE   B CD1 1 
ATOM   3544 N N   . VAL   B 1 165 ? -2.120  30.989 -44.492 1.00 16.58 ? 187 VAL   B N   1 
ATOM   3545 C CA  . VAL   B 1 165 ? -2.281  30.369 -45.802 1.00 17.50 ? 187 VAL   B CA  1 
ATOM   3546 C C   . VAL   B 1 165 ? -3.272  31.188 -46.629 1.00 17.58 ? 187 VAL   B C   1 
ATOM   3547 O O   . VAL   B 1 165 ? -4.280  31.671 -46.108 1.00 17.20 ? 187 VAL   B O   1 
ATOM   3548 C CB  . VAL   B 1 165 ? -2.716  28.896 -45.690 1.00 18.20 ? 187 VAL   B CB  1 
ATOM   3549 C CG1 . VAL   B 1 165 ? -4.092  28.725 -45.046 1.00 17.78 ? 187 VAL   B CG1 1 
ATOM   3550 C CG2 . VAL   B 1 165 ? -2.642  28.198 -47.042 1.00 18.83 ? 187 VAL   B CG2 1 
ATOM   3551 N N   . SER   B 1 166 ? -2.936  31.370 -47.917 1.00 17.61 ? 188 SER   B N   1 
ATOM   3552 C CA  . SER   B 1 166 ? -3.806  32.040 -48.868 1.00 18.44 ? 188 SER   B CA  1 
ATOM   3553 C C   . SER   B 1 166 ? -4.054  31.144 -50.077 1.00 18.93 ? 188 SER   B C   1 
ATOM   3554 O O   . SER   B 1 166 ? -3.198  30.328 -50.428 1.00 20.46 ? 188 SER   B O   1 
ATOM   3555 C CB  . SER   B 1 166 ? -3.221  33.360 -49.307 1.00 18.75 ? 188 SER   B CB  1 
ATOM   3556 O OG  . SER   B 1 166 ? -1.990  33.170 -49.992 1.00 20.03 ? 188 SER   B OG  1 
ATOM   3557 N N   . SER   B 1 167 ? -5.204  31.359 -50.734 1.00 18.65 ? 189 SER   B N   1 
ATOM   3558 C CA  . SER   B 1 167 ? -5.540  30.677 -51.973 1.00 17.88 ? 189 SER   B CA  1 
ATOM   3559 C C   . SER   B 1 167 ? -6.056  31.683 -52.988 1.00 17.60 ? 189 SER   B C   1 
ATOM   3560 O O   . SER   B 1 167 ? -6.559  32.731 -52.601 1.00 17.01 ? 189 SER   B O   1 
ATOM   3561 C CB  . SER   B 1 167 ? -6.547  29.588 -51.775 1.00 17.52 ? 189 SER   B CB  1 
ATOM   3562 O OG  . SER   B 1 167 ? -7.702  30.063 -51.101 1.00 16.94 ? 189 SER   B OG  1 
ATOM   3563 N N   . SER   B 1 168 ? -5.986  31.320 -54.277 1.00 17.61 ? 190 SER   B N   1 
ATOM   3564 C CA  . SER   B 1 168 ? -6.406  32.254 -55.310 1.00 18.14 ? 190 SER   B CA  1 
ATOM   3565 C C   . SER   B 1 168 ? -6.900  31.548 -56.568 1.00 18.52 ? 190 SER   B C   1 
ATOM   3566 O O   . SER   B 1 168 ? -6.597  30.382 -56.839 1.00 19.30 ? 190 SER   B O   1 
ATOM   3567 C CB  . SER   B 1 168 ? -5.261  33.201 -55.620 1.00 18.29 ? 190 SER   B CB  1 
ATOM   3568 O OG  . SER   B 1 168 ? -5.436  33.906 -56.834 1.00 19.27 ? 190 SER   B OG  1 
ATOM   3569 N N   . TYR   B 1 169 ? -7.657  32.315 -57.349 1.00 18.61 ? 191 TYR   B N   1 
ATOM   3570 C CA  . TYR   B 1 169 ? -8.052  31.914 -58.690 1.00 19.85 ? 191 TYR   B CA  1 
ATOM   3571 C C   . TYR   B 1 169 ? -6.846  31.615 -59.574 1.00 21.24 ? 191 TYR   B C   1 
ATOM   3572 O O   . TYR   B 1 169 ? -6.981  30.912 -60.582 1.00 23.52 ? 191 TYR   B O   1 
ATOM   3573 C CB  . TYR   B 1 169 ? -8.886  33.040 -59.295 1.00 21.66 ? 191 TYR   B CB  1 
ATOM   3574 C CG  . TYR   B 1 169 ? -9.534  32.678 -60.619 1.00 23.90 ? 191 TYR   B CG  1 
ATOM   3575 C CD1 . TYR   B 1 169 ? -10.778 32.066 -60.663 1.00 27.01 ? 191 TYR   B CD1 1 
ATOM   3576 C CD2 . TYR   B 1 169 ? -8.887  32.937 -61.829 1.00 25.94 ? 191 TYR   B CD2 1 
ATOM   3577 C CE1 . TYR   B 1 169 ? -11.382 31.748 -61.869 1.00 30.49 ? 191 TYR   B CE1 1 
ATOM   3578 C CE2 . TYR   B 1 169 ? -9.467  32.599 -63.036 1.00 29.37 ? 191 TYR   B CE2 1 
ATOM   3579 C CZ  . TYR   B 1 169 ? -10.716 32.004 -63.054 1.00 31.13 ? 191 TYR   B CZ  1 
ATOM   3580 O OH  . TYR   B 1 169 ? -11.261 31.688 -64.265 1.00 36.76 ? 191 TYR   B OH  1 
ATOM   3581 N N   . ASP   B 1 170 ? -5.677  32.156 -59.213 1.00 21.38 ? 192 ASP   B N   1 
ATOM   3582 C CA  . ASP   B 1 170 ? -4.461  31.945 -59.978 1.00 22.37 ? 192 ASP   B CA  1 
ATOM   3583 C C   . ASP   B 1 170 ? -4.002  30.483 -59.927 1.00 23.05 ? 192 ASP   B C   1 
ATOM   3584 O O   . ASP   B 1 170 ? -3.079  30.110 -60.656 1.00 24.29 ? 192 ASP   B O   1 
ATOM   3585 C CB  . ASP   B 1 170 ? -3.363  32.904 -59.540 1.00 22.42 ? 192 ASP   B CB  1 
ATOM   3586 C CG  . ASP   B 1 170 ? -2.763  32.698 -58.157 1.00 22.19 ? 192 ASP   B CG  1 
ATOM   3587 O OD1 . ASP   B 1 170 ? -3.134  31.714 -57.462 1.00 21.93 ? 192 ASP   B OD1 1 
ATOM   3588 O OD2 . ASP   B 1 170 ? -1.934  33.543 -57.776 1.00 23.08 ? 192 ASP   B OD2 1 
ATOM   3589 N N   . GLY   B 1 171 ? -4.595  29.682 -59.029 1.00 23.70 ? 193 GLY   B N   1 
ATOM   3590 C CA  . GLY   B 1 171 ? -4.326  28.255 -58.948 1.00 24.33 ? 193 GLY   B CA  1 
ATOM   3591 C C   . GLY   B 1 171 ? -3.298  27.901 -57.872 1.00 25.54 ? 193 GLY   B C   1 
ATOM   3592 O O   . GLY   B 1 171 ? -2.935  26.731 -57.717 1.00 27.15 ? 193 GLY   B O   1 
ATOM   3593 N N   . LEU   B 1 172 ? -2.857  28.902 -57.098 1.00 27.04 ? 194 LEU   B N   1 
ATOM   3594 C CA  . LEU   B 1 172 ? -1.846  28.681 -56.073 1.00 26.36 ? 194 LEU   B CA  1 
ATOM   3595 C C   . LEU   B 1 172 ? -2.462  28.661 -54.678 1.00 25.04 ? 194 LEU   B C   1 
ATOM   3596 O O   . LEU   B 1 172 ? -3.448  29.333 -54.411 1.00 23.51 ? 194 LEU   B O   1 
ATOM   3597 C CB  . LEU   B 1 172 ? -0.797  29.786 -56.127 1.00 27.25 ? 194 LEU   B CB  1 
ATOM   3598 C CG  . LEU   B 1 172 ? -0.065  29.986 -57.455 1.00 30.23 ? 194 LEU   B CG  1 
ATOM   3599 C CD1 . LEU   B 1 172 ? 0.938   31.114 -57.246 1.00 30.81 ? 194 LEU   B CD1 1 
ATOM   3600 C CD2 . LEU   B 1 172 ? 0.601   28.722 -57.949 1.00 30.98 ? 194 LEU   B CD2 1 
ATOM   3601 N N   A CYS   B 1 173 ? -1.888  27.826 -53.806 0.50 23.98 ? 195 CYS   B N   1 
ATOM   3602 N N   B CYS   B 1 173 ? -1.807  27.905 -53.802 0.50 25.75 ? 195 CYS   B N   1 
ATOM   3603 C CA  A CYS   B 1 173 ? -1.902  28.059 -52.370 0.50 23.58 ? 195 CYS   B CA  1 
ATOM   3604 C CA  B CYS   B 1 173 ? -1.930  28.078 -52.369 0.50 26.53 ? 195 CYS   B CA  1 
ATOM   3605 C C   A CYS   B 1 173 ? -0.513  28.526 -51.950 0.50 24.01 ? 195 CYS   B C   1 
ATOM   3606 C C   B CYS   B 1 173 ? -0.552  28.400 -51.796 0.50 25.98 ? 195 CYS   B C   1 
ATOM   3607 O O   A CYS   B 1 173 ? 0.485   28.031 -52.466 0.50 23.78 ? 195 CYS   B O   1 
ATOM   3608 O O   B CYS   B 1 173 ? 0.397   27.657 -52.030 0.50 26.84 ? 195 CYS   B O   1 
ATOM   3609 C CB  A CYS   B 1 173 ? -2.278  26.808 -51.583 0.50 23.21 ? 195 CYS   B CB  1 
ATOM   3610 C CB  B CYS   B 1 173 ? -2.525  26.824 -51.747 0.50 28.75 ? 195 CYS   B CB  1 
ATOM   3611 S SG  A CYS   B 1 173 ? -3.971  26.239 -51.890 0.50 22.49 ? 195 CYS   B SG  1 
ATOM   3612 S SG  B CYS   B 1 173 ? -2.233  26.726 -49.969 0.50 30.97 ? 195 CYS   B SG  1 
ATOM   3613 N N   . ARG   B 1 174 ? -0.457  29.497 -51.033 1.00 25.11 ? 196 ARG   B N   1 
ATOM   3614 C CA  . ARG   B 1 174 ? 0.810   29.953 -50.486 1.00 24.57 ? 196 ARG   B CA  1 
ATOM   3615 C C   . ARG   B 1 174 ? 0.747   30.017 -48.966 1.00 24.47 ? 196 ARG   B C   1 
ATOM   3616 O O   . ARG   B 1 174 ? -0.298  30.365 -48.396 1.00 22.49 ? 196 ARG   B O   1 
ATOM   3617 C CB  . ARG   B 1 174 ? 1.205   31.304 -51.073 1.00 26.07 ? 196 ARG   B CB  1 
ATOM   3618 C CG  . ARG   B 1 174 ? 1.685   31.124 -52.507 1.00 28.26 ? 196 ARG   B CG  1 
ATOM   3619 C CD  . ARG   B 1 174 ? 2.048   32.434 -53.149 1.00 29.20 ? 196 ARG   B CD  1 
ATOM   3620 N NE  . ARG   B 1 174 ? 2.856   32.170 -54.339 1.00 32.72 ? 196 ARG   B NE  1 
ATOM   3621 C CZ  . ARG   B 1 174 ? 3.087   33.037 -55.310 1.00 33.79 ? 196 ARG   B CZ  1 
ATOM   3622 N NH1 . ARG   B 1 174 ? 3.865   32.695 -56.323 1.00 36.07 ? 196 ARG   B NH1 1 
ATOM   3623 N NH2 . ARG   B 1 174 ? 2.554   34.244 -55.262 1.00 35.66 ? 196 ARG   B NH2 1 
ATOM   3624 N N   . ILE   B 1 175 ? 1.904   29.693 -48.356 1.00 24.21 ? 197 ILE   B N   1 
ATOM   3625 C CA  . ILE   B 1 175 ? 2.130   29.756 -46.917 1.00 24.93 ? 197 ILE   B CA  1 
ATOM   3626 C C   . ILE   B 1 175 ? 3.053   30.931 -46.637 1.00 23.89 ? 197 ILE   B C   1 
ATOM   3627 O O   . ILE   B 1 175 ? 4.114   31.037 -47.254 1.00 25.61 ? 197 ILE   B O   1 
ATOM   3628 C CB  . ILE   B 1 175 ? 2.794   28.471 -46.401 1.00 27.65 ? 197 ILE   B CB  1 
ATOM   3629 C CG1 . ILE   B 1 175 ? 2.056   27.241 -46.857 1.00 29.48 ? 197 ILE   B CG1 1 
ATOM   3630 C CG2 . ILE   B 1 175 ? 2.974   28.505 -44.878 1.00 30.10 ? 197 ILE   B CG2 1 
ATOM   3631 C CD1 . ILE   B 1 175 ? 0.711   27.070 -46.203 1.00 28.30 ? 197 ILE   B CD1 1 
ATOM   3632 N N   . TRP   B 1 176 ? 2.644   31.769 -45.683 1.00 23.83 ? 198 TRP   B N   1 
ATOM   3633 C CA  . TRP   B 1 176 ? 3.352   32.989 -45.349 1.00 23.83 ? 198 TRP   B CA  1 
ATOM   3634 C C   . TRP   B 1 176 ? 3.787   32.971 -43.885 1.00 23.74 ? 198 TRP   B C   1 
ATOM   3635 O O   . TRP   B 1 176 ? 3.035   32.548 -43.013 1.00 23.95 ? 198 TRP   B O   1 
ATOM   3636 C CB  . TRP   B 1 176 ? 2.452   34.202 -45.621 1.00 22.69 ? 198 TRP   B CB  1 
ATOM   3637 C CG  . TRP   B 1 176 ? 1.840   34.219 -46.992 1.00 23.27 ? 198 TRP   B CG  1 
ATOM   3638 C CD1 . TRP   B 1 176 ? 0.657   33.670 -47.387 1.00 23.31 ? 198 TRP   B CD1 1 
ATOM   3639 C CD2 . TRP   B 1 176 ? 2.418   34.821 -48.163 1.00 23.84 ? 198 TRP   B CD2 1 
ATOM   3640 N NE1 . TRP   B 1 176 ? 0.451   33.901 -48.714 1.00 23.75 ? 198 TRP   B NE1 1 
ATOM   3641 C CE2 . TRP   B 1 176 ? 1.517   34.597 -49.221 1.00 24.00 ? 198 TRP   B CE2 1 
ATOM   3642 C CE3 . TRP   B 1 176 ? 3.603   35.515 -48.410 1.00 25.67 ? 198 TRP   B CE3 1 
ATOM   3643 C CZ2 . TRP   B 1 176 ? 1.763   35.055 -50.510 1.00 25.05 ? 198 TRP   B CZ2 1 
ATOM   3644 C CZ3 . TRP   B 1 176 ? 3.848   35.960 -49.686 1.00 25.46 ? 198 TRP   B CZ3 1 
ATOM   3645 C CH2 . TRP   B 1 176 ? 2.943   35.728 -50.720 1.00 26.03 ? 198 TRP   B CH2 1 
ATOM   3646 N N   . ASP   B 1 177 ? 5.004   33.465 -43.632 1.00 25.73 ? 199 ASP   B N   1 
ATOM   3647 C CA  . ASP   B 1 177 ? 5.467   33.745 -42.284 1.00 26.84 ? 199 ASP   B CA  1 
ATOM   3648 C C   . ASP   B 1 177 ? 4.805   35.035 -41.825 1.00 26.35 ? 199 ASP   B C   1 
ATOM   3649 O O   . ASP   B 1 177 ? 5.029   36.079 -42.427 1.00 27.16 ? 199 ASP   B O   1 
ATOM   3650 C CB  . ASP   B 1 177 ? 6.968   33.956 -42.231 1.00 27.28 ? 199 ASP   B CB  1 
ATOM   3651 C CG  . ASP   B 1 177 ? 7.509   34.250 -40.841 1.00 27.51 ? 199 ASP   B CG  1 
ATOM   3652 O OD1 . ASP   B 1 177 ? 7.302   33.409 -39.946 1.00 29.50 ? 199 ASP   B OD1 1 
ATOM   3653 O OD2 . ASP   B 1 177 ? 8.092   35.329 -40.652 1.00 27.37 ? 199 ASP   B OD2 1 
ATOM   3654 N N   . THR   B 1 178 ? 3.975   34.961 -40.780 1.00 24.82 ? 200 THR   B N   1 
ATOM   3655 C CA  . THR   B 1 178 ? 3.207   36.119 -40.347 1.00 24.24 ? 200 THR   B CA  1 
ATOM   3656 C C   . THR   B 1 178 ? 4.129   37.297 -40.014 1.00 25.11 ? 200 THR   B C   1 
ATOM   3657 O O   . THR   B 1 178 ? 3.855   38.432 -40.399 1.00 23.95 ? 200 THR   B O   1 
ATOM   3658 C CB  . THR   B 1 178 ? 2.342   35.771 -39.138 1.00 22.45 ? 200 THR   B CB  1 
ATOM   3659 O OG1 . THR   B 1 178 ? 1.431   34.756 -39.556 1.00 21.82 ? 200 THR   B OG1 1 
ATOM   3660 C CG2 . THR   B 1 178 ? 1.604   36.990 -38.613 1.00 22.61 ? 200 THR   B CG2 1 
ATOM   3661 N N   . ALA   B 1 179 ? 5.203   37.038 -39.263 1.00 25.28 ? 201 ALA   B N   1 
ATOM   3662 C CA  . ALA   B 1 179 ? 5.968   38.124 -38.666 1.00 27.59 ? 201 ALA   B CA  1 
ATOM   3663 C C   . ALA   B 1 179 ? 6.685   38.950 -39.733 1.00 27.62 ? 201 ALA   B C   1 
ATOM   3664 O O   . ALA   B 1 179 ? 6.811   40.165 -39.580 1.00 31.37 ? 201 ALA   B O   1 
ATOM   3665 C CB  . ALA   B 1 179 ? 6.953   37.585 -37.648 1.00 28.50 ? 201 ALA   B CB  1 
ATOM   3666 N N   . SER   B 1 180 ? 7.157   38.278 -40.792 1.00 27.76 ? 202 SER   B N   1 
ATOM   3667 C CA  . SER   B 1 180 ? 7.992   38.890 -41.818 1.00 29.70 ? 202 SER   B CA  1 
ATOM   3668 C C   . SER   B 1 180 ? 7.226   39.154 -43.112 1.00 31.06 ? 202 SER   B C   1 
ATOM   3669 O O   . SER   B 1 180 ? 7.660   39.992 -43.898 1.00 30.20 ? 202 SER   B O   1 
ATOM   3670 C CB  . SER   B 1 180 ? 9.189   38.028 -42.125 1.00 29.86 ? 202 SER   B CB  1 
ATOM   3671 O OG  . SER   B 1 180 ? 8.781   36.840 -42.791 1.00 31.52 ? 202 SER   B OG  1 
ATOM   3672 N N   . GLY   B 1 181 ? 6.136   38.408 -43.350 1.00 32.33 ? 203 GLY   B N   1 
ATOM   3673 C CA  . GLY   B 1 181 ? 5.398   38.481 -44.602 1.00 31.44 ? 203 GLY   B CA  1 
ATOM   3674 C C   . GLY   B 1 181 ? 6.036   37.664 -45.728 1.00 31.50 ? 203 GLY   B C   1 
ATOM   3675 O O   . GLY   B 1 181 ? 5.622   37.796 -46.876 1.00 30.98 ? 203 GLY   B O   1 
ATOM   3676 N N   . GLN   B 1 182 ? 7.031   36.815 -45.430 1.00 32.00 ? 204 GLN   B N   1 
ATOM   3677 C CA  . GLN   B 1 182 ? 7.726   36.082 -46.484 1.00 34.25 ? 204 GLN   B CA  1 
ATOM   3678 C C   . GLN   B 1 182 ? 6.980   34.785 -46.819 1.00 32.97 ? 204 GLN   B C   1 
ATOM   3679 O O   . GLN   B 1 182 ? 6.439   34.126 -45.940 1.00 31.75 ? 204 GLN   B O   1 
ATOM   3680 C CB  . GLN   B 1 182 ? 9.185   35.798 -46.127 1.00 36.09 ? 204 GLN   B CB  1 
ATOM   3681 C CG  . GLN   B 1 182 ? 10.036  37.050 -45.922 1.00 40.32 ? 204 GLN   B CG  1 
ATOM   3682 C CD  . GLN   B 1 182 ? 10.013  37.997 -47.101 1.00 40.95 ? 204 GLN   B CD  1 
ATOM   3683 O OE1 . GLN   B 1 182 ? 9.563   39.142 -46.994 1.00 44.71 ? 204 GLN   B OE1 1 
ATOM   3684 N NE2 . GLN   B 1 182 ? 10.488  37.522 -48.242 1.00 39.90 ? 204 GLN   B NE2 1 
ATOM   3685 N N   . CYS   B 1 183 ? 6.969   34.426 -48.113 1.00 33.47 ? 205 CYS   B N   1 
ATOM   3686 C CA  . CYS   B 1 183 ? 6.336   33.201 -48.584 1.00 34.04 ? 205 CYS   B CA  1 
ATOM   3687 C C   . CYS   B 1 183 ? 7.267   32.020 -48.322 1.00 36.65 ? 205 CYS   B C   1 
ATOM   3688 O O   . CYS   B 1 183 ? 8.408   32.007 -48.798 1.00 40.19 ? 205 CYS   B O   1 
ATOM   3689 C CB  . CYS   B 1 183 ? 5.974   33.318 -50.064 1.00 35.03 ? 205 CYS   B CB  1 
ATOM   3690 S SG  . CYS   B 1 183 ? 5.165   31.852 -50.757 1.00 39.91 ? 205 CYS   B SG  1 
ATOM   3691 N N   . LEU   B 1 184 ? 6.778   31.037 -47.553 1.00 35.48 ? 206 LEU   B N   1 
ATOM   3692 C CA  . LEU   B 1 184 ? 7.567   29.863 -47.198 1.00 36.39 ? 206 LEU   B CA  1 
ATOM   3693 C C   . LEU   B 1 184 ? 7.295   28.682 -48.131 1.00 37.92 ? 206 LEU   B C   1 
ATOM   3694 O O   . LEU   B 1 184 ? 8.136   27.788 -48.233 1.00 41.94 ? 206 LEU   B O   1 
ATOM   3695 C CB  . LEU   B 1 184 ? 7.288   29.469 -45.753 1.00 38.80 ? 206 LEU   B CB  1 
ATOM   3696 C CG  . LEU   B 1 184 ? 7.437   30.579 -44.711 1.00 40.02 ? 206 LEU   B CG  1 
ATOM   3697 C CD1 . LEU   B 1 184 ? 6.974   30.088 -43.354 1.00 41.18 ? 206 LEU   B CD1 1 
ATOM   3698 C CD2 . LEU   B 1 184 ? 8.861   31.078 -44.640 1.00 42.39 ? 206 LEU   B CD2 1 
ATOM   3699 N N   . LYS   B 1 185 ? 6.126   28.654 -48.790 1.00 36.14 ? 207 LYS   B N   1 
ATOM   3700 C CA  . LYS   B 1 185 ? 5.776   27.553 -49.680 1.00 39.63 ? 207 LYS   B CA  1 
ATOM   3701 C C   . LYS   B 1 185 ? 4.700   28.003 -50.663 1.00 38.91 ? 207 LYS   B C   1 
ATOM   3702 O O   . LYS   B 1 185 ? 3.755   28.703 -50.292 1.00 36.91 ? 207 LYS   B O   1 
ATOM   3703 C CB  . LYS   B 1 185 ? 5.285   26.298 -48.941 1.00 42.72 ? 207 LYS   B CB  1 
ATOM   3704 C CG  . LYS   B 1 185 ? 5.879   24.972 -49.425 1.00 46.95 ? 207 LYS   B CG  1 
ATOM   3705 N N   . THR   B 1 186 ? 4.880   27.594 -51.926 1.00 40.10 ? 208 THR   B N   1 
ATOM   3706 C CA  . THR   B 1 186 ? 3.818   27.643 -52.916 1.00 40.75 ? 208 THR   B CA  1 
ATOM   3707 C C   . THR   B 1 186 ? 3.470   26.211 -53.320 1.00 43.51 ? 208 THR   B C   1 
ATOM   3708 O O   . THR   B 1 186 ? 4.366   25.431 -53.641 1.00 47.07 ? 208 THR   B O   1 
ATOM   3709 C CB  . THR   B 1 186 ? 4.265   28.470 -54.124 1.00 40.20 ? 208 THR   B CB  1 
ATOM   3710 O OG1 . THR   B 1 186 ? 4.562   29.799 -53.708 1.00 39.09 ? 208 THR   B OG1 1 
ATOM   3711 C CG2 . THR   B 1 186 ? 3.181   28.558 -55.179 1.00 41.07 ? 208 THR   B CG2 1 
ATOM   3712 N N   . LEU   B 1 187 ? 2.174   25.870 -53.320 1.00 44.06 ? 209 LEU   B N   1 
ATOM   3713 C CA  . LEU   B 1 187 ? 1.708   24.626 -53.922 1.00 49.41 ? 209 LEU   B CA  1 
ATOM   3714 C C   . LEU   B 1 187 ? 1.092   24.918 -55.288 1.00 49.45 ? 209 LEU   B C   1 
ATOM   3715 O O   . LEU   B 1 187 ? 0.067   25.605 -55.357 1.00 45.80 ? 209 LEU   B O   1 
ATOM   3716 C CB  . LEU   B 1 187 ? 0.703   23.928 -53.009 1.00 50.10 ? 209 LEU   B CB  1 
ATOM   3717 C CG  . LEU   B 1 187 ? 1.242   23.483 -51.649 1.00 54.82 ? 209 LEU   B CG  1 
ATOM   3718 C CD1 . LEU   B 1 187 ? 0.138   22.776 -50.892 1.00 56.08 ? 209 LEU   B CD1 1 
ATOM   3719 C CD2 . LEU   B 1 187 ? 2.465   22.593 -51.785 1.00 57.27 ? 209 LEU   B CD2 1 
ATOM   3720 N N   . ILE   B 1 188 ? 1.728   24.375 -56.345 1.00 53.86 ? 210 ILE   B N   1 
ATOM   3721 C CA  . ILE   B 1 188 ? 1.335   24.585 -57.735 1.00 54.62 ? 210 ILE   B CA  1 
ATOM   3722 C C   . ILE   B 1 188 ? 1.170   23.226 -58.443 1.00 56.22 ? 210 ILE   B C   1 
ATOM   3723 O O   . ILE   B 1 188 ? 1.551   22.205 -57.827 1.00 57.87 ? 210 ILE   B O   1 
ATOM   3724 C CB  . ILE   B 1 188 ? 2.350   25.470 -58.485 1.00 52.73 ? 210 ILE   B CB  1 
ATOM   3725 N N   . ASP   B 1 191 ? -0.636  20.928 -62.556 1.00 62.18 ? 213 ASP   B N   1 
ATOM   3726 C CA  . ASP   B 1 191 ? -1.791  21.707 -63.084 1.00 61.00 ? 213 ASP   B CA  1 
ATOM   3727 C C   . ASP   B 1 191 ? -2.176  22.753 -62.040 1.00 61.84 ? 213 ASP   B C   1 
ATOM   3728 O O   . ASP   B 1 191 ? -1.686  22.691 -60.907 1.00 62.63 ? 213 ASP   B O   1 
ATOM   3729 C CB  . ASP   B 1 191 ? -2.939  20.785 -63.472 1.00 64.20 ? 213 ASP   B CB  1 
ATOM   3730 C CG  . ASP   B 1 191 ? -4.040  21.392 -64.332 1.00 66.18 ? 213 ASP   B CG  1 
ATOM   3731 O OD1 . ASP   B 1 191 ? -4.078  22.636 -64.473 1.00 66.59 ? 213 ASP   B OD1 1 
ATOM   3732 O OD2 . ASP   B 1 191 ? -4.851  20.611 -64.867 1.00 70.73 ? 213 ASP   B OD2 1 
ATOM   3733 N N   . ASN   B 1 192 ? -3.050  23.696 -62.443 1.00 56.43 ? 214 ASN   B N   1 
ATOM   3734 C CA  . ASN   B 1 192 ? -3.407  24.837 -61.612 1.00 52.32 ? 214 ASN   B CA  1 
ATOM   3735 C C   . ASN   B 1 192 ? -4.853  25.293 -61.849 1.00 45.14 ? 214 ASN   B C   1 
ATOM   3736 O O   . ASN   B 1 192 ? -5.085  26.437 -62.235 1.00 42.66 ? 214 ASN   B O   1 
ATOM   3737 C CB  . ASN   B 1 192 ? -2.426  25.988 -61.823 1.00 54.45 ? 214 ASN   B CB  1 
ATOM   3738 C CG  . ASN   B 1 192 ? -2.396  26.465 -63.253 1.00 56.63 ? 214 ASN   B CG  1 
ATOM   3739 O OD1 . ASN   B 1 192 ? -2.775  25.726 -64.170 1.00 59.34 ? 214 ASN   B OD1 1 
ATOM   3740 N ND2 . ASN   B 1 192 ? -1.940  27.690 -63.463 1.00 58.84 ? 214 ASN   B ND2 1 
ATOM   3741 N N   . PRO   B 1 193 ? -5.885  24.473 -61.532 1.00 39.53 ? 215 PRO   B N   1 
ATOM   3742 C CA  . PRO   B 1 193 ? -7.266  24.955 -61.525 1.00 36.62 ? 215 PRO   B CA  1 
ATOM   3743 C C   . PRO   B 1 193 ? -7.420  25.990 -60.413 1.00 31.34 ? 215 PRO   B C   1 
ATOM   3744 O O   . PRO   B 1 193 ? -6.700  25.952 -59.424 1.00 29.61 ? 215 PRO   B O   1 
ATOM   3745 C CB  . PRO   B 1 193 ? -8.089  23.679 -61.262 1.00 39.29 ? 215 PRO   B CB  1 
ATOM   3746 C CG  . PRO   B 1 193 ? -7.160  22.826 -60.441 1.00 39.25 ? 215 PRO   B CG  1 
ATOM   3747 C CD  . PRO   B 1 193 ? -5.792  23.076 -61.075 1.00 40.26 ? 215 PRO   B CD  1 
ATOM   3748 N N   . PRO   B 1 194 ? -8.358  26.949 -60.539 1.00 28.12 ? 216 PRO   B N   1 
ATOM   3749 C CA  . PRO   B 1 194 ? -8.586  27.945 -59.494 1.00 25.52 ? 216 PRO   B CA  1 
ATOM   3750 C C   . PRO   B 1 194 ? -8.725  27.274 -58.135 1.00 23.32 ? 216 PRO   B C   1 
ATOM   3751 O O   . PRO   B 1 194 ? -9.358  26.229 -58.024 1.00 24.26 ? 216 PRO   B O   1 
ATOM   3752 C CB  . PRO   B 1 194 ? -9.893  28.608 -59.930 1.00 26.78 ? 216 PRO   B CB  1 
ATOM   3753 C CG  . PRO   B 1 194 ? -9.866  28.483 -61.432 1.00 28.48 ? 216 PRO   B CG  1 
ATOM   3754 C CD  . PRO   B 1 194 ? -9.260  27.114 -61.686 1.00 29.59 ? 216 PRO   B CD  1 
ATOM   3755 N N   . VAL   B 1 195 ? -8.112  27.881 -57.120 1.00 21.35 ? 217 VAL   B N   1 
ATOM   3756 C CA  . VAL   B 1 195 ? -8.281  27.418 -55.754 1.00 21.52 ? 217 VAL   B CA  1 
ATOM   3757 C C   . VAL   B 1 195 ? -9.310  28.326 -55.092 1.00 19.76 ? 217 VAL   B C   1 
ATOM   3758 O O   . VAL   B 1 195 ? -9.120  29.537 -55.026 1.00 19.83 ? 217 VAL   B O   1 
ATOM   3759 C CB  . VAL   B 1 195 ? -6.972  27.378 -54.950 1.00 22.74 ? 217 VAL   B CB  1 
ATOM   3760 C CG1 . VAL   B 1 195 ? -7.193  26.742 -53.583 1.00 22.08 ? 217 VAL   B CG1 1 
ATOM   3761 C CG2 . VAL   B 1 195 ? -5.870  26.658 -55.716 1.00 24.58 ? 217 VAL   B CG2 1 
ATOM   3762 N N   . SER   B 1 196 ? -10.400 27.712 -54.618 1.00 20.45 ? 218 SER   B N   1 
ATOM   3763 C CA  . SER   B 1 196 ? -11.603 28.427 -54.225 1.00 19.89 ? 218 SER   B CA  1 
ATOM   3764 C C   . SER   B 1 196 ? -11.709 28.523 -52.708 1.00 19.75 ? 218 SER   B C   1 
ATOM   3765 O O   . SER   B 1 196 ? -12.522 29.285 -52.188 1.00 17.97 ? 218 SER   B O   1 
ATOM   3766 C CB  . SER   B 1 196 ? -12.833 27.758 -54.811 1.00 21.34 ? 218 SER   B CB  1 
ATOM   3767 O OG  . SER   B 1 196 ? -12.806 26.350 -54.599 1.00 21.14 ? 218 SER   B OG  1 
ATOM   3768 N N   . PHE   B 1 197 ? -10.899 27.728 -52.001 1.00 20.04 ? 219 PHE   B N   1 
ATOM   3769 C CA  . PHE   B 1 197 ? -10.917 27.762 -50.552 1.00 19.95 ? 219 PHE   B CA  1 
ATOM   3770 C C   . PHE   B 1 197 ? -9.691  27.050 -49.996 1.00 19.19 ? 219 PHE   B C   1 
ATOM   3771 O O   . PHE   B 1 197 ? -9.254  26.069 -50.569 1.00 20.18 ? 219 PHE   B O   1 
ATOM   3772 C CB  . PHE   B 1 197 ? -12.183 27.097 -50.005 1.00 21.08 ? 219 PHE   B CB  1 
ATOM   3773 C CG  . PHE   B 1 197 ? -12.234 27.219 -48.495 1.00 22.24 ? 219 PHE   B CG  1 
ATOM   3774 C CD1 . PHE   B 1 197 ? -12.590 28.428 -47.905 1.00 22.57 ? 219 PHE   B CD1 1 
ATOM   3775 C CD2 . PHE   B 1 197 ? -11.901 26.146 -47.674 1.00 23.54 ? 219 PHE   B CD2 1 
ATOM   3776 C CE1 . PHE   B 1 197 ? -12.627 28.564 -46.532 1.00 23.02 ? 219 PHE   B CE1 1 
ATOM   3777 C CE2 . PHE   B 1 197 ? -11.946 26.284 -46.292 1.00 23.19 ? 219 PHE   B CE2 1 
ATOM   3778 C CZ  . PHE   B 1 197 ? -12.308 27.495 -45.728 1.00 23.14 ? 219 PHE   B CZ  1 
ATOM   3779 N N   . VAL   B 1 198 ? -9.157  27.551 -48.877 1.00 19.00 ? 220 VAL   B N   1 
ATOM   3780 C CA  . VAL   B 1 198 ? -8.118  26.858 -48.132 1.00 19.28 ? 220 VAL   B CA  1 
ATOM   3781 C C   . VAL   B 1 198 ? -8.227  27.184 -46.642 1.00 18.82 ? 220 VAL   B C   1 
ATOM   3782 O O   . VAL   B 1 198 ? -8.705  28.250 -46.267 1.00 19.54 ? 220 VAL   B O   1 
ATOM   3783 C CB  . VAL   B 1 198 ? -6.761  27.229 -48.764 1.00 20.43 ? 220 VAL   B CB  1 
ATOM   3784 C CG1 . VAL   B 1 198 ? -6.299  28.635 -48.424 1.00 20.34 ? 220 VAL   B CG1 1 
ATOM   3785 C CG2 . VAL   B 1 198 ? -5.688  26.212 -48.447 1.00 23.11 ? 220 VAL   B CG2 1 
ATOM   3786 N N   A LYS   B 1 199 ? -7.773  26.253 -45.801 0.50 18.69 ? 221 LYS   B N   1 
ATOM   3787 N N   B LYS   B 1 199 ? -7.777  26.232 -45.807 0.50 18.39 ? 221 LYS   B N   1 
ATOM   3788 C CA  A LYS   B 1 199 ? -7.572  26.537 -44.394 0.50 19.28 ? 221 LYS   B CA  1 
ATOM   3789 C CA  B LYS   B 1 199 ? -7.770  26.330 -44.353 0.50 18.67 ? 221 LYS   B CA  1 
ATOM   3790 C C   A LYS   B 1 199 ? -6.740  25.418 -43.782 0.50 19.15 ? 221 LYS   B C   1 
ATOM   3791 C C   B LYS   B 1 199 ? -6.665  25.408 -43.838 0.50 18.79 ? 221 LYS   B C   1 
ATOM   3792 O O   A LYS   B 1 199 ? -6.797  24.269 -44.226 0.50 19.07 ? 221 LYS   B O   1 
ATOM   3793 O O   B LYS   B 1 199 ? -6.405  24.377 -44.455 0.50 19.23 ? 221 LYS   B O   1 
ATOM   3794 C CB  A LYS   B 1 199 ? -8.889  26.618 -43.618 0.50 20.22 ? 221 LYS   B CB  1 
ATOM   3795 C CB  B LYS   B 1 199 ? -9.127  25.854 -43.810 0.50 18.98 ? 221 LYS   B CB  1 
ATOM   3796 C CG  A LYS   B 1 199 ? -9.444  25.265 -43.220 0.50 21.25 ? 221 LYS   B CG  1 
ATOM   3797 C CG  B LYS   B 1 199 ? -9.533  26.317 -42.410 0.50 19.46 ? 221 LYS   B CG  1 
ATOM   3798 C CD  A LYS   B 1 199 ? -10.801 25.333 -42.538 0.50 22.67 ? 221 LYS   B CD  1 
ATOM   3799 C CD  B LYS   B 1 199 ? -10.994 26.077 -42.044 0.50 20.05 ? 221 LYS   B CD  1 
ATOM   3800 C CE  A LYS   B 1 199 ? -10.813 26.185 -41.316 0.50 24.07 ? 221 LYS   B CE  1 
ATOM   3801 C CE  B LYS   B 1 199 ? -11.332 26.632 -40.684 0.50 20.14 ? 221 LYS   B CE  1 
ATOM   3802 N NZ  A LYS   B 1 199 ? -12.187 26.322 -40.827 0.50 24.89 ? 221 LYS   B NZ  1 
ATOM   3803 N NZ  B LYS   B 1 199 ? -12.764 26.527 -40.372 0.50 20.08 ? 221 LYS   B NZ  1 
ATOM   3804 N N   . PHE   B 1 200 ? -6.002  25.780 -42.734 1.00 18.95 ? 222 PHE   B N   1 
ATOM   3805 C CA  . PHE   B 1 200 ? -5.147  24.852 -42.013 1.00 19.67 ? 222 PHE   B CA  1 
ATOM   3806 C C   . PHE   B 1 200 ? -6.000  23.855 -41.238 1.00 20.23 ? 222 PHE   B C   1 
ATOM   3807 O O   . PHE   B 1 200 ? -7.103  24.178 -40.787 1.00 20.42 ? 222 PHE   B O   1 
ATOM   3808 C CB  . PHE   B 1 200 ? -4.261  25.558 -40.993 1.00 20.38 ? 222 PHE   B CB  1 
ATOM   3809 C CG  . PHE   B 1 200 ? -3.079  26.321 -41.557 1.00 20.01 ? 222 PHE   B CG  1 
ATOM   3810 C CD1 . PHE   B 1 200 ? -1.915  25.657 -41.925 1.00 22.18 ? 222 PHE   B CD1 1 
ATOM   3811 C CD2 . PHE   B 1 200 ? -3.116  27.704 -41.643 1.00 19.51 ? 222 PHE   B CD2 1 
ATOM   3812 C CE1 . PHE   B 1 200 ? -0.832  26.363 -42.420 1.00 21.91 ? 222 PHE   B CE1 1 
ATOM   3813 C CE2 . PHE   B 1 200 ? -2.023  28.407 -42.108 1.00 20.46 ? 222 PHE   B CE2 1 
ATOM   3814 C CZ  . PHE   B 1 200 ? -0.889  27.735 -42.516 1.00 21.44 ? 222 PHE   B CZ  1 
ATOM   3815 N N   . SER   B 1 201 ? -5.451  22.651 -41.062 1.00 22.24 ? 223 SER   B N   1 
ATOM   3816 C CA  . SER   B 1 201 ? -5.976  21.683 -40.116 1.00 24.53 ? 223 SER   B CA  1 
ATOM   3817 C C   . SER   B 1 201 ? -5.794  22.206 -38.688 1.00 25.55 ? 223 SER   B C   1 
ATOM   3818 O O   . SER   B 1 201 ? -4.938  23.053 -38.432 1.00 22.82 ? 223 SER   B O   1 
ATOM   3819 C CB  . SER   B 1 201 ? -5.314  20.328 -40.303 1.00 25.42 ? 223 SER   B CB  1 
ATOM   3820 O OG  . SER   B 1 201 ? -3.911  20.390 -40.067 1.00 26.01 ? 223 SER   B OG  1 
ATOM   3821 N N   . PRO   B 1 202 ? -6.605  21.759 -37.705 1.00 27.42 ? 224 PRO   B N   1 
ATOM   3822 C CA  . PRO   B 1 202 ? -6.398  22.183 -36.316 1.00 27.58 ? 224 PRO   B CA  1 
ATOM   3823 C C   . PRO   B 1 202 ? -4.959  22.038 -35.818 1.00 27.97 ? 224 PRO   B C   1 
ATOM   3824 O O   . PRO   B 1 202 ? -4.493  22.858 -35.030 1.00 27.77 ? 224 PRO   B O   1 
ATOM   3825 C CB  . PRO   B 1 202 ? -7.372  21.284 -35.548 1.00 29.43 ? 224 PRO   B CB  1 
ATOM   3826 C CG  . PRO   B 1 202 ? -8.499  21.048 -36.529 1.00 29.34 ? 224 PRO   B CG  1 
ATOM   3827 C CD  . PRO   B 1 202 ? -7.806  20.924 -37.879 1.00 27.87 ? 224 PRO   B CD  1 
ATOM   3828 N N   . ASN   B 1 203 ? -4.262  20.981 -36.260 1.00 29.31 ? 225 ASN   B N   1 
ATOM   3829 C CA  . ASN   B 1 203 ? -2.934  20.684 -35.747 1.00 32.79 ? 225 ASN   B CA  1 
ATOM   3830 C C   . ASN   B 1 203 ? -1.866  21.448 -36.534 1.00 31.04 ? 225 ASN   B C   1 
ATOM   3831 O O   . ASN   B 1 203 ? -0.688  21.380 -36.189 1.00 29.95 ? 225 ASN   B O   1 
ATOM   3832 C CB  . ASN   B 1 203 ? -2.681  19.179 -35.678 1.00 34.94 ? 225 ASN   B CB  1 
ATOM   3833 C CG  . ASN   B 1 203 ? -2.412  18.566 -37.034 1.00 35.86 ? 225 ASN   B CG  1 
ATOM   3834 O OD1 . ASN   B 1 203 ? -2.503  19.245 -38.065 1.00 35.80 ? 225 ASN   B OD1 1 
ATOM   3835 N ND2 . ASN   B 1 203 ? -2.062  17.288 -37.047 1.00 37.49 ? 225 ASN   B ND2 1 
ATOM   3836 N N   . GLY   B 1 204 ? -2.272  22.172 -37.586 1.00 29.97 ? 226 GLY   B N   1 
ATOM   3837 C CA  . GLY   B 1 204 ? -1.367  23.048 -38.307 1.00 29.56 ? 226 GLY   B CA  1 
ATOM   3838 C C   . GLY   B 1 204 ? -0.526  22.329 -39.362 1.00 30.39 ? 226 GLY   B C   1 
ATOM   3839 O O   . GLY   B 1 204 ? 0.157   23.001 -40.128 1.00 31.66 ? 226 GLY   B O   1 
ATOM   3840 N N   . LYS   B 1 205 ? -0.604  20.994 -39.447 1.00 30.47 ? 227 LYS   B N   1 
ATOM   3841 C CA  . LYS   B 1 205 ? 0.320   20.228 -40.281 1.00 30.97 ? 227 LYS   B CA  1 
ATOM   3842 C C   . LYS   B 1 205 ? -0.187  20.157 -41.725 1.00 32.72 ? 227 LYS   B C   1 
ATOM   3843 O O   . LYS   B 1 205 ? 0.590   19.961 -42.670 1.00 32.32 ? 227 LYS   B O   1 
ATOM   3844 C CB  . LYS   B 1 205 ? 0.531   18.836 -39.668 1.00 32.27 ? 227 LYS   B CB  1 
ATOM   3845 C CG  . LYS   B 1 205 ? 1.163   18.850 -38.278 1.00 34.53 ? 227 LYS   B CG  1 
ATOM   3846 N N   . TYR   B 1 206 ? -1.505  20.315 -41.890 1.00 31.20 ? 228 TYR   B N   1 
ATOM   3847 C CA  . TYR   B 1 206 ? -2.137  20.089 -43.172 1.00 29.99 ? 228 TYR   B CA  1 
ATOM   3848 C C   . TYR   B 1 206 ? -2.919  21.323 -43.594 1.00 27.33 ? 228 TYR   B C   1 
ATOM   3849 O O   . TYR   B 1 206 ? -3.234  22.200 -42.790 1.00 26.38 ? 228 TYR   B O   1 
ATOM   3850 C CB  . TYR   B 1 206 ? -3.110  18.911 -43.114 1.00 32.20 ? 228 TYR   B CB  1 
ATOM   3851 C CG  . TYR   B 1 206 ? -2.537  17.680 -42.432 1.00 34.63 ? 228 TYR   B CG  1 
ATOM   3852 C CD1 . TYR   B 1 206 ? -1.287  17.171 -42.790 1.00 35.98 ? 228 TYR   B CD1 1 
ATOM   3853 C CD2 . TYR   B 1 206 ? -3.242  17.039 -41.423 1.00 35.79 ? 228 TYR   B CD2 1 
ATOM   3854 C CE1 . TYR   B 1 206 ? -0.756  16.060 -42.156 1.00 37.47 ? 228 TYR   B CE1 1 
ATOM   3855 C CE2 . TYR   B 1 206 ? -2.725  15.919 -40.792 1.00 37.15 ? 228 TYR   B CE2 1 
ATOM   3856 C CZ  . TYR   B 1 206 ? -1.479  15.435 -41.154 1.00 38.85 ? 228 TYR   B CZ  1 
ATOM   3857 O OH  . TYR   B 1 206 ? -1.001  14.329 -40.513 1.00 41.26 ? 228 TYR   B OH  1 
ATOM   3858 N N   A ILE   B 1 207 ? -3.159  21.439 -44.901 0.50 25.57 ? 229 ILE   B N   1 
ATOM   3859 N N   B ILE   B 1 207 ? -3.305  21.291 -44.861 0.50 27.33 ? 229 ILE   B N   1 
ATOM   3860 C CA  A ILE   B 1 207 ? -4.138  22.387 -45.415 0.50 24.54 ? 229 ILE   B CA  1 
ATOM   3861 C CA  B ILE   B 1 207 ? -4.113  22.331 -45.458 0.50 27.17 ? 229 ILE   B CA  1 
ATOM   3862 C C   A ILE   B 1 207 ? -5.178  21.615 -46.221 0.50 24.78 ? 229 ILE   B C   1 
ATOM   3863 C C   B ILE   B 1 207 ? -5.178  21.666 -46.319 0.50 26.12 ? 229 ILE   B C   1 
ATOM   3864 O O   A ILE   B 1 207 ? -4.849  20.642 -46.898 0.50 25.58 ? 229 ILE   B O   1 
ATOM   3865 O O   B ILE   B 1 207 ? -4.863  20.819 -47.154 0.50 26.81 ? 229 ILE   B O   1 
ATOM   3866 C CB  A ILE   B 1 207 ? -3.499  23.522 -46.241 0.50 23.40 ? 229 ILE   B CB  1 
ATOM   3867 C CB  B ILE   B 1 207 ? -3.204  23.260 -46.268 0.50 28.64 ? 229 ILE   B CB  1 
ATOM   3868 C CG1 A ILE   B 1 207 ? -2.720  23.008 -47.454 0.50 23.38 ? 229 ILE   B CG1 1 
ATOM   3869 C CG1 B ILE   B 1 207 ? -2.194  23.946 -45.372 0.50 29.29 ? 229 ILE   B CG1 1 
ATOM   3870 C CG2 A ILE   B 1 207 ? -2.634  24.418 -45.356 0.50 22.94 ? 229 ILE   B CG2 1 
ATOM   3871 C CG2 B ILE   B 1 207 ? -4.026  24.261 -47.063 0.50 28.82 ? 229 ILE   B CG2 1 
ATOM   3872 C CD1 A ILE   B 1 207 ? -2.080  24.114 -48.268 0.50 23.68 ? 229 ILE   B CD1 1 
ATOM   3873 C CD1 B ILE   B 1 207 ? -1.047  24.556 -46.137 0.50 30.12 ? 229 ILE   B CD1 1 
ATOM   3874 N N   . LEU   B 1 208 ? -6.437  22.045 -46.082 1.00 23.92 ? 230 LEU   B N   1 
ATOM   3875 C CA  . LEU   B 1 208 ? -7.547  21.552 -46.867 1.00 23.91 ? 230 LEU   B CA  1 
ATOM   3876 C C   . LEU   B 1 208 ? -7.784  22.594 -47.950 1.00 22.77 ? 230 LEU   B C   1 
ATOM   3877 O O   . LEU   B 1 208 ? -7.959  23.755 -47.623 1.00 23.53 ? 230 LEU   B O   1 
ATOM   3878 C CB  . LEU   B 1 208 ? -8.752  21.408 -45.941 1.00 24.74 ? 230 LEU   B CB  1 
ATOM   3879 C CG  . LEU   B 1 208 ? -10.064 20.947 -46.581 1.00 26.04 ? 230 LEU   B CG  1 
ATOM   3880 C CD1 . LEU   B 1 208 ? -9.974  19.508 -47.052 1.00 28.48 ? 230 LEU   B CD1 1 
ATOM   3881 C CD2 . LEU   B 1 208 ? -11.227 21.132 -45.617 1.00 25.99 ? 230 LEU   B CD2 1 
ATOM   3882 N N   . ALA   B 1 209 ? -7.734  22.186 -49.221 1.00 24.50 ? 231 ALA   B N   1 
ATOM   3883 C CA  . ALA   B 1 209 ? -7.895  23.110 -50.337 1.00 24.43 ? 231 ALA   B CA  1 
ATOM   3884 C C   . ALA   B 1 209 ? -8.996  22.621 -51.271 1.00 25.53 ? 231 ALA   B C   1 
ATOM   3885 O O   . ALA   B 1 209 ? -9.006  21.446 -51.638 1.00 26.66 ? 231 ALA   B O   1 
ATOM   3886 C CB  . ALA   B 1 209 ? -6.600  23.264 -51.094 1.00 25.40 ? 231 ALA   B CB  1 
ATOM   3887 N N   . ALA   B 1 210 ? -9.882  23.546 -51.670 1.00 24.82 ? 232 ALA   B N   1 
ATOM   3888 C CA  . ALA   B 1 210 ? -10.909 23.272 -52.665 1.00 24.76 ? 232 ALA   B CA  1 
ATOM   3889 C C   . ALA   B 1 210 ? -10.451 23.832 -54.004 1.00 25.39 ? 232 ALA   B C   1 
ATOM   3890 O O   . ALA   B 1 210 ? -9.865  24.913 -54.041 1.00 24.27 ? 232 ALA   B O   1 
ATOM   3891 C CB  . ALA   B 1 210 ? -12.233 23.892 -52.295 1.00 23.23 ? 232 ALA   B CB  1 
ATOM   3892 N N   . THR   B 1 211 ? -10.729 23.088 -55.076 1.00 26.44 ? 233 THR   B N   1 
ATOM   3893 C CA  . THR   B 1 211 ? -10.527 23.584 -56.427 1.00 28.20 ? 233 THR   B CA  1 
ATOM   3894 C C   . THR   B 1 211 ? -11.847 23.475 -57.187 1.00 29.58 ? 233 THR   B C   1 
ATOM   3895 O O   . THR   B 1 211 ? -12.725 22.694 -56.820 1.00 30.65 ? 233 THR   B O   1 
ATOM   3896 C CB  . THR   B 1 211 ? -9.377  22.844 -57.122 1.00 29.93 ? 233 THR   B CB  1 
ATOM   3897 O OG1 . THR   B 1 211 ? -9.483  21.444 -56.878 1.00 27.92 ? 233 THR   B OG1 1 
ATOM   3898 C CG2 . THR   B 1 211 ? -8.020  23.294 -56.608 1.00 29.68 ? 233 THR   B CG2 1 
ATOM   3899 N N   . LEU   B 1 212 ? -11.985 24.274 -58.250 1.00 29.63 ? 234 LEU   B N   1 
ATOM   3900 C CA  . LEU   B 1 212 ? -13.242 24.319 -58.984 1.00 30.36 ? 234 LEU   B CA  1 
ATOM   3901 C C   . LEU   B 1 212 ? -13.325 23.188 -60.003 1.00 33.03 ? 234 LEU   B C   1 
ATOM   3902 O O   . LEU   B 1 212 ? -13.806 23.382 -61.121 1.00 35.38 ? 234 LEU   B O   1 
ATOM   3903 C CB  . LEU   B 1 212 ? -13.403 25.685 -59.632 1.00 30.93 ? 234 LEU   B CB  1 
ATOM   3904 C CG  . LEU   B 1 212 ? -13.557 26.849 -58.657 1.00 29.43 ? 234 LEU   B CG  1 
ATOM   3905 C CD1 . LEU   B 1 212 ? -13.917 28.051 -59.492 1.00 31.04 ? 234 LEU   B CD1 1 
ATOM   3906 C CD2 . LEU   B 1 212 ? -14.582 26.591 -57.561 1.00 28.71 ? 234 LEU   B CD2 1 
ATOM   3907 N N   . ASP   B 1 213 ? -12.857 22.008 -59.595 1.00 34.56 ? 235 ASP   B N   1 
ATOM   3908 C CA  . ASP   B 1 213 ? -13.033 20.776 -60.341 1.00 35.71 ? 235 ASP   B CA  1 
ATOM   3909 C C   . ASP   B 1 213 ? -13.747 19.768 -59.439 1.00 33.78 ? 235 ASP   B C   1 
ATOM   3910 O O   . ASP   B 1 213 ? -13.509 18.568 -59.549 1.00 35.56 ? 235 ASP   B O   1 
ATOM   3911 C CB  . ASP   B 1 213 ? -11.693 20.284 -60.871 1.00 38.14 ? 235 ASP   B CB  1 
ATOM   3912 C CG  . ASP   B 1 213 ? -10.594 20.127 -59.828 1.00 39.21 ? 235 ASP   B CG  1 
ATOM   3913 O OD1 . ASP   B 1 213 ? -10.885 20.334 -58.630 1.00 37.29 ? 235 ASP   B OD1 1 
ATOM   3914 O OD2 . ASP   B 1 213 ? -9.449  19.828 -60.220 1.00 44.46 ? 235 ASP   B OD2 1 
ATOM   3915 N N   . ASN   B 1 214 ? -14.609 20.265 -58.536 1.00 31.30 ? 236 ASN   B N   1 
ATOM   3916 C CA  . ASN   B 1 214 ? -15.426 19.412 -57.682 1.00 32.53 ? 236 ASN   B CA  1 
ATOM   3917 C C   . ASN   B 1 214 ? -14.550 18.561 -56.760 1.00 32.62 ? 236 ASN   B C   1 
ATOM   3918 O O   . ASN   B 1 214 ? -14.869 17.404 -56.504 1.00 33.95 ? 236 ASN   B O   1 
ATOM   3919 C CB  . ASN   B 1 214 ? -16.347 18.519 -58.508 1.00 33.19 ? 236 ASN   B CB  1 
ATOM   3920 C CG  . ASN   B 1 214 ? -17.029 19.279 -59.621 1.00 34.02 ? 236 ASN   B CG  1 
ATOM   3921 O OD1 . ASN   B 1 214 ? -17.923 20.093 -59.362 1.00 33.12 ? 236 ASN   B OD1 1 
ATOM   3922 N ND2 . ASN   B 1 214 ? -16.635 19.032 -60.863 1.00 36.51 ? 236 ASN   B ND2 1 
ATOM   3923 N N   . THR   B 1 215 ? -13.456 19.136 -56.250 1.00 32.84 ? 237 THR   B N   1 
ATOM   3924 C CA  . THR   B 1 215 ? -12.467 18.369 -55.500 1.00 33.55 ? 237 THR   B CA  1 
ATOM   3925 C C   . THR   B 1 215 ? -12.013 19.149 -54.269 1.00 31.00 ? 237 THR   B C   1 
ATOM   3926 O O   . THR   B 1 215 ? -11.705 20.332 -54.358 1.00 29.65 ? 237 THR   B O   1 
ATOM   3927 C CB  . THR   B 1 215 ? -11.274 18.041 -56.403 1.00 34.88 ? 237 THR   B CB  1 
ATOM   3928 O OG1 . THR   B 1 215 ? -11.779 17.298 -57.511 1.00 37.51 ? 237 THR   B OG1 1 
ATOM   3929 C CG2 . THR   B 1 215 ? -10.217 17.202 -55.710 1.00 37.69 ? 237 THR   B CG2 1 
ATOM   3930 N N   . LEU   B 1 216 ? -11.966 18.448 -53.128 1.00 30.27 ? 238 LEU   B N   1 
ATOM   3931 C CA  . LEU   B 1 216 ? -11.225 18.893 -51.962 1.00 28.92 ? 238 LEU   B CA  1 
ATOM   3932 C C   . LEU   B 1 216 ? -10.015 17.989 -51.788 1.00 29.81 ? 238 LEU   B C   1 
ATOM   3933 O O   . LEU   B 1 216 ? -10.136 16.777 -51.972 1.00 31.05 ? 238 LEU   B O   1 
ATOM   3934 C CB  . LEU   B 1 216 ? -12.116 18.826 -50.728 1.00 28.15 ? 238 LEU   B CB  1 
ATOM   3935 C CG  . LEU   B 1 216 ? -13.142 19.946 -50.580 1.00 28.09 ? 238 LEU   B CG  1 
ATOM   3936 C CD1 . LEU   B 1 216 ? -14.274 19.472 -49.712 1.00 29.61 ? 238 LEU   B CD1 1 
ATOM   3937 C CD2 . LEU   B 1 216 ? -12.484 21.161 -49.962 1.00 28.22 ? 238 LEU   B CD2 1 
ATOM   3938 N N   . LYS   B 1 217 ? -8.886  18.589 -51.389 1.00 29.16 ? 239 LYS   B N   1 
ATOM   3939 C CA  . LYS   B 1 217 ? -7.661  17.855 -51.114 1.00 30.86 ? 239 LYS   B CA  1 
ATOM   3940 C C   . LYS   B 1 217 ? -7.086  18.256 -49.755 1.00 30.22 ? 239 LYS   B C   1 
ATOM   3941 O O   . LYS   B 1 217 ? -7.081  19.431 -49.390 1.00 27.57 ? 239 LYS   B O   1 
ATOM   3942 C CB  . LYS   B 1 217 ? -6.606  18.096 -52.200 1.00 32.04 ? 239 LYS   B CB  1 
ATOM   3943 C CG  . LYS   B 1 217 ? -6.899  17.440 -53.535 1.00 33.93 ? 239 LYS   B CG  1 
ATOM   3944 C CD  . LYS   B 1 217 ? -5.915  17.791 -54.648 1.00 35.76 ? 239 LYS   B CD  1 
ATOM   3945 N N   . LEU   B 1 218 ? -6.597  17.251 -49.019 1.00 29.92 ? 240 LEU   B N   1 
ATOM   3946 C CA  . LEU   B 1 218 ? -5.844  17.465 -47.797 1.00 30.98 ? 240 LEU   B CA  1 
ATOM   3947 C C   . LEU   B 1 218 ? -4.355  17.326 -48.106 1.00 32.15 ? 240 LEU   B C   1 
ATOM   3948 O O   . LEU   B 1 218 ? -3.895  16.237 -48.446 1.00 34.09 ? 240 LEU   B O   1 
ATOM   3949 C CB  . LEU   B 1 218 ? -6.286  16.458 -46.739 1.00 31.02 ? 240 LEU   B CB  1 
ATOM   3950 C CG  . LEU   B 1 218 ? -5.744  16.703 -45.331 1.00 31.77 ? 240 LEU   B CG  1 
ATOM   3951 C CD1 . LEU   B 1 218 ? -6.350  17.957 -44.735 1.00 31.47 ? 240 LEU   B CD1 1 
ATOM   3952 C CD2 . LEU   B 1 218 ? -6.006  15.492 -44.466 1.00 33.15 ? 240 LEU   B CD2 1 
ATOM   3953 N N   . TRP   B 1 219 ? -3.620  18.438 -47.971 1.00 30.92 ? 241 TRP   B N   1 
ATOM   3954 C CA  . TRP   B 1 219 ? -2.203  18.503 -48.293 1.00 33.82 ? 241 TRP   B CA  1 
ATOM   3955 C C   . TRP   B 1 219 ? -1.352  18.525 -47.028 1.00 34.81 ? 241 TRP   B C   1 
ATOM   3956 O O   . TRP   B 1 219 ? -1.651  19.269 -46.101 1.00 33.80 ? 241 TRP   B O   1 
ATOM   3957 C CB  . TRP   B 1 219 ? -1.902  19.778 -49.090 1.00 35.28 ? 241 TRP   B CB  1 
ATOM   3958 C CG  . TRP   B 1 219 ? -2.425  19.795 -50.497 1.00 36.38 ? 241 TRP   B CG  1 
ATOM   3959 C CD1 . TRP   B 1 219 ? -3.656  20.199 -50.916 1.00 36.66 ? 241 TRP   B CD1 1 
ATOM   3960 C CD2 . TRP   B 1 219 ? -1.704  19.399 -51.677 1.00 39.11 ? 241 TRP   B CD2 1 
ATOM   3961 N NE1 . TRP   B 1 219 ? -3.759  20.081 -52.274 1.00 38.24 ? 241 TRP   B NE1 1 
ATOM   3962 C CE2 . TRP   B 1 219 ? -2.578  19.590 -52.769 1.00 40.21 ? 241 TRP   B CE2 1 
ATOM   3963 C CE3 . TRP   B 1 219 ? -0.418  18.903 -51.910 1.00 42.46 ? 241 TRP   B CE3 1 
ATOM   3964 C CZ2 . TRP   B 1 219 ? -2.198  19.296 -54.076 1.00 43.47 ? 241 TRP   B CZ2 1 
ATOM   3965 C CZ3 . TRP   B 1 219 ? -0.046  18.613 -53.204 1.00 44.46 ? 241 TRP   B CZ3 1 
ATOM   3966 C CH2 . TRP   B 1 219 ? -0.924  18.805 -54.269 1.00 44.62 ? 241 TRP   B CH2 1 
ATOM   3967 N N   . ASP   B 1 220 ? -0.271  17.736 -47.022 1.00 37.97 ? 242 ASP   B N   1 
ATOM   3968 C CA  . ASP   B 1 220 ? 0.900   18.074 -46.232 1.00 42.69 ? 242 ASP   B CA  1 
ATOM   3969 C C   . ASP   B 1 220 ? 1.731   19.055 -47.053 1.00 44.38 ? 242 ASP   B C   1 
ATOM   3970 O O   . ASP   B 1 220 ? 2.291   18.667 -48.072 1.00 44.35 ? 242 ASP   B O   1 
ATOM   3971 C CB  . ASP   B 1 220 ? 1.736   16.853 -45.887 1.00 44.01 ? 242 ASP   B CB  1 
ATOM   3972 C CG  . ASP   B 1 220 ? 2.939   17.137 -44.999 1.00 46.33 ? 242 ASP   B CG  1 
ATOM   3973 O OD1 . ASP   B 1 220 ? 3.634   18.149 -45.239 1.00 49.25 ? 242 ASP   B OD1 1 
ATOM   3974 O OD2 . ASP   B 1 220 ? 3.175   16.338 -44.086 1.00 49.95 ? 242 ASP   B OD2 1 
ATOM   3975 N N   . TYR   B 1 221 ? 1.807   20.313 -46.604 1.00 48.34 ? 243 TYR   B N   1 
ATOM   3976 C CA  . TYR   B 1 221 ? 2.402   21.386 -47.395 1.00 49.85 ? 243 TYR   B CA  1 
ATOM   3977 C C   . TYR   B 1 221 ? 3.904   21.499 -47.130 1.00 56.16 ? 243 TYR   B C   1 
ATOM   3978 O O   . TYR   B 1 221 ? 4.628   22.070 -47.950 1.00 59.87 ? 243 TYR   B O   1 
ATOM   3979 C CB  . TYR   B 1 221 ? 1.760   22.745 -47.101 1.00 47.36 ? 243 TYR   B CB  1 
ATOM   3980 C CG  . TYR   B 1 221 ? 1.937   23.155 -45.648 1.00 46.29 ? 243 TYR   B CG  1 
ATOM   3981 C CD1 . TYR   B 1 221 ? 3.043   23.892 -45.237 1.00 43.28 ? 243 TYR   B CD1 1 
ATOM   3982 C CD2 . TYR   B 1 221 ? 1.034   22.731 -44.682 1.00 47.44 ? 243 TYR   B CD2 1 
ATOM   3983 C CE1 . TYR   B 1 221 ? 3.229   24.224 -43.909 1.00 45.57 ? 243 TYR   B CE1 1 
ATOM   3984 C CE2 . TYR   B 1 221 ? 1.204   23.061 -43.352 1.00 48.46 ? 243 TYR   B CE2 1 
ATOM   3985 C CZ  . TYR   B 1 221 ? 2.302   23.810 -42.968 1.00 47.06 ? 243 TYR   B CZ  1 
ATOM   3986 O OH  . TYR   B 1 221 ? 2.435   24.135 -41.657 1.00 42.40 ? 243 TYR   B OH  1 
ATOM   3987 N N   . SER   B 1 222 ? 4.353   21.003 -45.968 1.00 56.23 ? 244 SER   B N   1 
ATOM   3988 C CA  . SER   B 1 222 ? 5.773   20.915 -45.672 1.00 59.49 ? 244 SER   B CA  1 
ATOM   3989 C C   . SER   B 1 222 ? 6.446   19.990 -46.686 1.00 62.95 ? 244 SER   B C   1 
ATOM   3990 O O   . SER   B 1 222 ? 7.370   20.409 -47.380 1.00 63.70 ? 244 SER   B O   1 
ATOM   3991 C CB  . SER   B 1 222 ? 6.010   20.458 -44.253 1.00 59.68 ? 244 SER   B CB  1 
ATOM   3992 N N   . LYS   B 1 223 ? 5.950   18.749 -46.794 1.00 64.18 ? 245 LYS   B N   1 
ATOM   3993 C CA  . LYS   B 1 223 ? 6.494   17.770 -47.730 1.00 64.57 ? 245 LYS   B CA  1 
ATOM   3994 C C   . LYS   B 1 223 ? 5.836   17.917 -49.105 1.00 65.11 ? 245 LYS   B C   1 
ATOM   3995 O O   . LYS   B 1 223 ? 6.350   17.392 -50.089 1.00 68.42 ? 245 LYS   B O   1 
ATOM   3996 C CB  . LYS   B 1 223 ? 6.351   16.340 -47.192 1.00 62.76 ? 245 LYS   B CB  1 
ATOM   3997 N N   . GLY   B 1 224 ? 4.690   18.614 -49.170 1.00 62.89 ? 246 GLY   B N   1 
ATOM   3998 C CA  . GLY   B 1 224 ? 4.066   18.973 -50.437 1.00 57.20 ? 246 GLY   B CA  1 
ATOM   3999 C C   . GLY   B 1 224 ? 3.385   17.784 -51.117 1.00 53.81 ? 246 GLY   B C   1 
ATOM   4000 O O   . GLY   B 1 224 ? 3.510   17.617 -52.326 1.00 57.40 ? 246 GLY   B O   1 
ATOM   4001 N N   . LYS   B 1 225 ? 2.637   16.990 -50.341 1.00 47.89 ? 247 LYS   B N   1 
ATOM   4002 C CA  . LYS   B 1 225 ? 1.995   15.780 -50.829 1.00 44.73 ? 247 LYS   B CA  1 
ATOM   4003 C C   . LYS   B 1 225 ? 0.501   15.830 -50.514 1.00 42.32 ? 247 LYS   B C   1 
ATOM   4004 O O   . LYS   B 1 225 ? 0.108   16.169 -49.400 1.00 42.57 ? 247 LYS   B O   1 
ATOM   4005 C CB  . LYS   B 1 225 ? 2.599   14.537 -50.165 1.00 43.01 ? 247 LYS   B CB  1 
ATOM   4006 N N   . CYS   B 1 226 ? -0.325  15.469 -51.499 1.00 44.69 ? 248 CYS   B N   1 
ATOM   4007 C CA  . CYS   B 1 226 ? -1.753  15.301 -51.277 1.00 43.68 ? 248 CYS   B CA  1 
ATOM   4008 C C   . CYS   B 1 226 ? -1.982  13.971 -50.562 1.00 44.00 ? 248 CYS   B C   1 
ATOM   4009 O O   . CYS   B 1 226 ? -1.576  12.929 -51.072 1.00 44.89 ? 248 CYS   B O   1 
ATOM   4010 C CB  . CYS   B 1 226 ? -2.517  15.365 -52.594 1.00 40.89 ? 248 CYS   B CB  1 
ATOM   4011 S SG  . CYS   B 1 226 ? -4.279  15.013 -52.394 1.00 42.69 ? 248 CYS   B SG  1 
ATOM   4012 N N   . LEU   B 1 227 ? -2.598  14.013 -49.371 1.00 41.54 ? 249 LEU   B N   1 
ATOM   4013 C CA  . LEU   B 1 227 ? -2.762  12.825 -48.542 1.00 43.13 ? 249 LEU   B CA  1 
ATOM   4014 C C   . LEU   B 1 227 ? -4.141  12.212 -48.774 1.00 42.95 ? 249 LEU   B C   1 
ATOM   4015 O O   . LEU   B 1 227 ? -4.305  10.990 -48.726 1.00 44.01 ? 249 LEU   B O   1 
ATOM   4016 C CB  . LEU   B 1 227 ? -2.578  13.157 -47.060 1.00 43.84 ? 249 LEU   B CB  1 
ATOM   4017 C CG  . LEU   B 1 227 ? -1.198  13.661 -46.624 1.00 45.73 ? 249 LEU   B CG  1 
ATOM   4018 C CD1 . LEU   B 1 227 ? -1.231  14.042 -45.149 1.00 47.40 ? 249 LEU   B CD1 1 
ATOM   4019 C CD2 . LEU   B 1 227 ? -0.090  12.650 -46.885 1.00 46.10 ? 249 LEU   B CD2 1 
ATOM   4020 N N   . LYS   B 1 228 ? -5.129  13.082 -48.990 1.00 38.92 ? 250 LYS   B N   1 
ATOM   4021 C CA  . LYS   B 1 228 ? -6.501  12.655 -49.187 1.00 40.25 ? 250 LYS   B CA  1 
ATOM   4022 C C   . LYS   B 1 228 ? -7.144  13.558 -50.231 1.00 39.08 ? 250 LYS   B C   1 
ATOM   4023 O O   . LYS   B 1 228 ? -6.805  14.740 -50.346 1.00 39.36 ? 250 LYS   B O   1 
ATOM   4024 C CB  . LYS   B 1 228 ? -7.318  12.724 -47.890 1.00 40.00 ? 250 LYS   B CB  1 
ATOM   4025 C CG  . LYS   B 1 228 ? -6.774  11.949 -46.687 1.00 42.51 ? 250 LYS   B CG  1 
ATOM   4026 C CD  . LYS   B 1 228 ? -6.884  10.431 -46.771 1.00 43.28 ? 250 LYS   B CD  1 
ATOM   4027 C CE  . LYS   B 1 228 ? -6.008  9.757  -45.777 1.00 43.77 ? 250 LYS   B CE  1 
ATOM   4028 N NZ  . LYS   B 1 228 ? -6.256  8.316  -45.758 1.00 45.23 ? 250 LYS   B NZ  1 
ATOM   4029 N N   . THR   B 1 229 ? -8.071  12.966 -50.986 1.00 39.63 ? 251 THR   B N   1 
ATOM   4030 C CA  . THR   B 1 229 ? -8.929  13.689 -51.902 1.00 37.78 ? 251 THR   B CA  1 
ATOM   4031 C C   . THR   B 1 229 ? -10.370 13.342 -51.541 1.00 36.32 ? 251 THR   B C   1 
ATOM   4032 O O   . THR   B 1 229 ? -10.656 12.179 -51.266 1.00 36.10 ? 251 THR   B O   1 
ATOM   4033 C CB  . THR   B 1 229 ? -8.576  13.258 -53.324 1.00 41.65 ? 251 THR   B CB  1 
ATOM   4034 O OG1 . THR   B 1 229 ? -7.209  13.605 -53.529 1.00 43.98 ? 251 THR   B OG1 1 
ATOM   4035 C CG2 . THR   B 1 229 ? -9.406  13.976 -54.367 1.00 43.61 ? 251 THR   B CG2 1 
ATOM   4036 N N   . TYR   B 1 230 ? -11.254 14.348 -51.540 1.00 32.59 ? 252 TYR   B N   1 
ATOM   4037 C CA  . TYR   B 1 230 ? -12.673 14.161 -51.257 1.00 32.45 ? 252 TYR   B CA  1 
ATOM   4038 C C   . TYR   B 1 230 ? -13.485 14.646 -52.459 1.00 31.52 ? 252 TYR   B C   1 
ATOM   4039 O O   . TYR   B 1 230 ? -13.345 15.800 -52.847 1.00 30.72 ? 252 TYR   B O   1 
ATOM   4040 C CB  . TYR   B 1 230 ? -13.043 14.926 -49.979 1.00 31.44 ? 252 TYR   B CB  1 
ATOM   4041 C CG  . TYR   B 1 230 ? -12.092 14.647 -48.824 1.00 31.93 ? 252 TYR   B CG  1 
ATOM   4042 C CD1 . TYR   B 1 230 ? -10.944 15.410 -48.661 1.00 31.92 ? 252 TYR   B CD1 1 
ATOM   4043 C CD2 . TYR   B 1 230 ? -12.301 13.600 -47.930 1.00 32.38 ? 252 TYR   B CD2 1 
ATOM   4044 C CE1 . TYR   B 1 230 ? -10.043 15.152 -47.645 1.00 32.23 ? 252 TYR   B CE1 1 
ATOM   4045 C CE2 . TYR   B 1 230 ? -11.410 13.337 -46.901 1.00 31.80 ? 252 TYR   B CE2 1 
ATOM   4046 C CZ  . TYR   B 1 230 ? -10.273 14.113 -46.763 1.00 30.86 ? 252 TYR   B CZ  1 
ATOM   4047 O OH  . TYR   B 1 230 ? -9.367  13.904 -45.764 1.00 34.13 ? 252 TYR   B OH  1 
ATOM   4048 N N   . THR   B 1 231 ? -14.330 13.770 -53.027 1.00 34.39 ? 253 THR   B N   1 
ATOM   4049 C CA  . THR   B 1 231 ? -15.105 14.077 -54.227 1.00 34.96 ? 253 THR   B CA  1 
ATOM   4050 C C   . THR   B 1 231 ? -16.541 13.577 -54.061 1.00 35.03 ? 253 THR   B C   1 
ATOM   4051 O O   . THR   B 1 231 ? -16.892 12.971 -53.048 1.00 34.79 ? 253 THR   B O   1 
ATOM   4052 C CB  . THR   B 1 231 ? -14.458 13.439 -55.457 1.00 37.35 ? 253 THR   B CB  1 
ATOM   4053 O OG1 . THR   B 1 231 ? -14.551 12.033 -55.255 1.00 38.30 ? 253 THR   B OG1 1 
ATOM   4054 C CG2 . THR   B 1 231 ? -13.014 13.860 -55.662 1.00 39.34 ? 253 THR   B CG2 1 
ATOM   4055 N N   . GLY   B 1 232 ? -17.366 13.846 -55.079 1.00 33.83 ? 254 GLY   B N   1 
ATOM   4056 C CA  . GLY   B 1 232 ? -18.759 13.426 -55.092 1.00 36.62 ? 254 GLY   B CA  1 
ATOM   4057 C C   . GLY   B 1 232 ? -19.710 14.615 -54.989 1.00 35.26 ? 254 GLY   B C   1 
ATOM   4058 O O   . GLY   B 1 232 ? -20.887 14.503 -55.308 1.00 37.15 ? 254 GLY   B O   1 
ATOM   4059 N N   . HIS   B 1 233 ? -19.180 15.744 -54.515 1.00 36.55 ? 255 HIS   B N   1 
ATOM   4060 C CA  . HIS   B 1 233 ? -19.899 17.004 -54.447 1.00 34.70 ? 255 HIS   B CA  1 
ATOM   4061 C C   . HIS   B 1 233 ? -19.719 17.766 -55.757 1.00 35.46 ? 255 HIS   B C   1 
ATOM   4062 O O   . HIS   B 1 233 ? -18.976 17.325 -56.645 1.00 37.03 ? 255 HIS   B O   1 
ATOM   4063 C CB  . HIS   B 1 233 ? -19.413 17.831 -53.246 1.00 33.80 ? 255 HIS   B CB  1 
ATOM   4064 C CG  . HIS   B 1 233 ? -17.969 18.213 -53.313 1.00 31.96 ? 255 HIS   B CG  1 
ATOM   4065 N ND1 . HIS   B 1 233 ? -17.518 19.511 -53.162 1.00 33.29 ? 255 HIS   B ND1 1 
ATOM   4066 C CD2 . HIS   B 1 233 ? -16.875 17.474 -53.559 1.00 30.34 ? 255 HIS   B CD2 1 
ATOM   4067 C CE1 . HIS   B 1 233 ? -16.200 19.542 -53.296 1.00 30.09 ? 255 HIS   B CE1 1 
ATOM   4068 N NE2 . HIS   B 1 233 ? -15.789 18.305 -53.517 1.00 33.36 ? 255 HIS   B NE2 1 
ATOM   4069 N N   . LYS   B 1 234 ? -20.418 18.909 -55.850 1.00 34.37 ? 256 LYS   B N   1 
ATOM   4070 C CA  . LYS   B 1 234 ? -20.388 19.787 -57.015 1.00 34.98 ? 256 LYS   B CA  1 
ATOM   4071 C C   . LYS   B 1 234 ? -19.806 21.147 -56.616 1.00 31.77 ? 256 LYS   B C   1 
ATOM   4072 O O   . LYS   B 1 234 ? -20.371 21.869 -55.796 1.00 30.86 ? 256 LYS   B O   1 
ATOM   4073 C CB  . LYS   B 1 234 ? -21.793 19.950 -57.609 1.00 37.94 ? 256 LYS   B CB  1 
ATOM   4074 C CG  . LYS   B 1 234 ? -21.900 20.764 -58.907 1.00 41.78 ? 256 LYS   B CG  1 
ATOM   4075 C CD  . LYS   B 1 234 ? -21.459 20.071 -60.192 1.00 46.49 ? 256 LYS   B CD  1 
ATOM   4076 C CE  . LYS   B 1 234 ? -21.739 20.901 -61.421 1.00 49.14 ? 256 LYS   B CE  1 
ATOM   4077 N NZ  . LYS   B 1 234 ? -21.387 20.179 -62.644 1.00 51.35 ? 256 LYS   B NZ  1 
ATOM   4078 N N   . ASN   B 1 235 ? -18.677 21.503 -57.233 1.00 29.52 ? 257 ASN   B N   1 
ATOM   4079 C CA  . ASN   B 1 235 ? -18.008 22.760 -56.942 1.00 27.95 ? 257 ASN   B CA  1 
ATOM   4080 C C   . ASN   B 1 235 ? -17.191 23.161 -58.167 1.00 28.77 ? 257 ASN   B C   1 
ATOM   4081 O O   . ASN   B 1 235 ? -16.036 22.767 -58.301 1.00 30.08 ? 257 ASN   B O   1 
ATOM   4082 C CB  . ASN   B 1 235 ? -17.156 22.648 -55.679 1.00 25.84 ? 257 ASN   B CB  1 
ATOM   4083 C CG  . ASN   B 1 235 ? -16.565 23.961 -55.218 1.00 27.09 ? 257 ASN   B CG  1 
ATOM   4084 O OD1 . ASN   B 1 235 ? -15.608 23.952 -54.433 1.00 25.79 ? 257 ASN   B OD1 1 
ATOM   4085 N ND2 . ASN   B 1 235 ? -17.088 25.090 -55.686 1.00 26.17 ? 257 ASN   B ND2 1 
ATOM   4086 N N   . GLU   B 1 236 ? -17.819 23.925 -59.065 1.00 29.94 ? 258 GLU   B N   1 
ATOM   4087 C CA  . GLU   B 1 236 ? -17.183 24.385 -60.288 1.00 30.61 ? 258 GLU   B CA  1 
ATOM   4088 C C   . GLU   B 1 236 ? -17.215 25.907 -60.421 1.00 27.89 ? 258 GLU   B C   1 
ATOM   4089 O O   . GLU   B 1 236 ? -16.598 26.441 -61.346 1.00 27.97 ? 258 GLU   B O   1 
ATOM   4090 C CB  . GLU   B 1 236 ? -17.891 23.757 -61.489 1.00 34.09 ? 258 GLU   B CB  1 
ATOM   4091 C CG  . GLU   B 1 236 ? -17.462 22.313 -61.724 1.00 37.50 ? 258 GLU   B CG  1 
ATOM   4092 C CD  . GLU   B 1 236 ? -18.146 21.573 -62.858 1.00 40.18 ? 258 GLU   B CD  1 
ATOM   4093 O OE1 . GLU   B 1 236 ? -19.235 22.015 -63.302 1.00 46.41 ? 258 GLU   B OE1 1 
ATOM   4094 O OE2 . GLU   B 1 236 ? -17.562 20.555 -63.298 1.00 38.64 ? 258 GLU   B OE2 1 
ATOM   4095 N N   . LYS   B 1 237 ? -17.932 26.594 -59.522 1.00 26.83 ? 259 LYS   B N   1 
ATOM   4096 C CA  . LYS   B 1 237 ? -18.261 28.003 -59.706 1.00 28.07 ? 259 LYS   B CA  1 
ATOM   4097 C C   . LYS   B 1 237 ? -17.926 28.876 -58.483 1.00 26.45 ? 259 LYS   B C   1 
ATOM   4098 O O   . LYS   B 1 237 ? -17.406 29.986 -58.642 1.00 25.52 ? 259 LYS   B O   1 
ATOM   4099 C CB  . LYS   B 1 237 ? -19.747 28.093 -60.075 1.00 31.72 ? 259 LYS   B CB  1 
ATOM   4100 C CG  . LYS   B 1 237 ? -20.247 29.503 -60.382 1.00 36.96 ? 259 LYS   B CG  1 
ATOM   4101 C CD  . LYS   B 1 237 ? -21.571 29.576 -61.139 1.00 39.48 ? 259 LYS   B CD  1 
ATOM   4102 C CE  . LYS   B 1 237 ? -22.058 30.990 -61.289 1.00 42.54 ? 259 LYS   B CE  1 
ATOM   4103 N NZ  . LYS   B 1 237 ? -23.508 31.069 -61.487 1.00 42.62 ? 259 LYS   B NZ  1 
ATOM   4104 N N   . TYR   B 1 238 ? -18.240 28.415 -57.266 1.00 25.12 ? 260 TYR   B N   1 
ATOM   4105 C CA  . TYR   B 1 238 ? -18.206 29.282 -56.090 1.00 24.83 ? 260 TYR   B CA  1 
ATOM   4106 C C   . TYR   B 1 238 ? -17.075 28.922 -55.130 1.00 23.57 ? 260 TYR   B C   1 
ATOM   4107 O O   . TYR   B 1 238 ? -16.577 27.795 -55.094 1.00 24.68 ? 260 TYR   B O   1 
ATOM   4108 C CB  . TYR   B 1 238 ? -19.515 29.229 -55.298 1.00 25.16 ? 260 TYR   B CB  1 
ATOM   4109 C CG  . TYR   B 1 238 ? -20.675 29.830 -56.074 1.00 26.33 ? 260 TYR   B CG  1 
ATOM   4110 C CD1 . TYR   B 1 238 ? -20.912 31.196 -56.056 1.00 26.91 ? 260 TYR   B CD1 1 
ATOM   4111 C CD2 . TYR   B 1 238 ? -21.508 29.031 -56.846 1.00 28.14 ? 260 TYR   B CD2 1 
ATOM   4112 C CE1 . TYR   B 1 238 ? -21.951 31.758 -56.776 1.00 29.28 ? 260 TYR   B CE1 1 
ATOM   4113 C CE2 . TYR   B 1 238 ? -22.566 29.576 -57.554 1.00 30.19 ? 260 TYR   B CE2 1 
ATOM   4114 C CZ  . TYR   B 1 238 ? -22.784 30.942 -57.521 1.00 30.06 ? 260 TYR   B CZ  1 
ATOM   4115 O OH  . TYR   B 1 238 ? -23.804 31.482 -58.241 1.00 32.13 ? 260 TYR   B OH  1 
ATOM   4116 N N   . CYS   B 1 239 ? -16.704 29.913 -54.318 1.00 22.07 ? 261 CYS   B N   1 
ATOM   4117 C CA  . CYS   B 1 239 ? -15.771 29.695 -53.226 1.00 19.50 ? 261 CYS   B CA  1 
ATOM   4118 C C   . CYS   B 1 239 ? -16.579 29.215 -52.027 1.00 20.09 ? 261 CYS   B C   1 
ATOM   4119 O O   . CYS   B 1 239 ? -17.228 30.013 -51.368 1.00 20.57 ? 261 CYS   B O   1 
ATOM   4120 C CB  . CYS   B 1 239 ? -15.015 30.974 -52.912 1.00 19.33 ? 261 CYS   B CB  1 
ATOM   4121 S SG  . CYS   B 1 239 ? -14.000 31.547 -54.297 1.00 19.63 ? 261 CYS   B SG  1 
ATOM   4122 N N   . ILE   B 1 240 ? -16.580 27.901 -51.803 1.00 19.98 ? 262 ILE   B N   1 
ATOM   4123 C CA  . ILE   B 1 240 ? -17.416 27.294 -50.784 1.00 20.79 ? 262 ILE   B CA  1 
ATOM   4124 C C   . ILE   B 1 240 ? -16.536 26.965 -49.592 1.00 20.38 ? 262 ILE   B C   1 
ATOM   4125 O O   . ILE   B 1 240 ? -15.466 26.393 -49.757 1.00 21.44 ? 262 ILE   B O   1 
ATOM   4126 C CB  . ILE   B 1 240 ? -18.126 26.050 -51.335 1.00 22.15 ? 262 ILE   B CB  1 
ATOM   4127 C CG1 . ILE   B 1 240 ? -19.045 26.410 -52.514 1.00 23.09 ? 262 ILE   B CG1 1 
ATOM   4128 C CG2 . ILE   B 1 240 ? -18.878 25.302 -50.229 1.00 22.16 ? 262 ILE   B CG2 1 
ATOM   4129 C CD1 . ILE   B 1 240 ? -19.827 25.238 -53.084 1.00 24.13 ? 262 ILE   B CD1 1 
ATOM   4130 N N   . PHE   B 1 241 ? -17.001 27.338 -48.400 1.00 22.37 ? 263 PHE   B N   1 
ATOM   4131 C CA  . PHE   B 1 241 ? -16.251 27.075 -47.184 1.00 21.70 ? 263 PHE   B CA  1 
ATOM   4132 C C   . PHE   B 1 241 ? -16.276 25.582 -46.917 1.00 24.17 ? 263 PHE   B C   1 
ATOM   4133 O O   . PHE   B 1 241 ? -17.293 24.944 -47.151 1.00 29.38 ? 263 PHE   B O   1 
ATOM   4134 C CB  . PHE   B 1 241 ? -16.853 27.822 -45.998 1.00 21.30 ? 263 PHE   B CB  1 
ATOM   4135 C CG  . PHE   B 1 241 ? -16.701 29.333 -46.020 1.00 19.20 ? 263 PHE   B CG  1 
ATOM   4136 C CD1 . PHE   B 1 241 ? -17.660 30.139 -46.629 1.00 18.78 ? 263 PHE   B CD1 1 
ATOM   4137 C CD2 . PHE   B 1 241 ? -15.630 29.943 -45.378 1.00 19.19 ? 263 PHE   B CD2 1 
ATOM   4138 C CE1 . PHE   B 1 241 ? -17.536 31.521 -46.615 1.00 18.73 ? 263 PHE   B CE1 1 
ATOM   4139 C CE2 . PHE   B 1 241 ? -15.510 31.326 -45.376 1.00 19.72 ? 263 PHE   B CE2 1 
ATOM   4140 C CZ  . PHE   B 1 241 ? -16.468 32.110 -45.972 1.00 19.92 ? 263 PHE   B CZ  1 
ATOM   4141 N N   . ALA   B 1 242 ? -15.152 25.049 -46.428 1.00 23.16 ? 264 ALA   B N   1 
ATOM   4142 C CA  . ALA   B 1 242 ? -15.111 23.695 -45.899 1.00 22.81 ? 264 ALA   B CA  1 
ATOM   4143 C C   . ALA   B 1 242 ? -14.527 23.718 -44.491 1.00 21.62 ? 264 ALA   B C   1 
ATOM   4144 O O   . ALA   B 1 242 ? -13.967 24.727 -44.054 1.00 22.12 ? 264 ALA   B O   1 
ATOM   4145 C CB  . ALA   B 1 242 ? -14.321 22.790 -46.814 1.00 24.33 ? 264 ALA   B CB  1 
ATOM   4146 N N   . ASN   B 1 243 ? -14.680 22.593 -43.786 1.00 21.36 ? 265 ASN   B N   1 
ATOM   4147 C CA  . ASN   B 1 243 ? -14.375 22.525 -42.367 1.00 21.32 ? 265 ASN   B CA  1 
ATOM   4148 C C   . ASN   B 1 243 ? -13.822 21.161 -41.969 1.00 21.83 ? 265 ASN   B C   1 
ATOM   4149 O O   . ASN   B 1 243 ? -14.145 20.141 -42.577 1.00 21.76 ? 265 ASN   B O   1 
ATOM   4150 C CB  . ASN   B 1 243 ? -15.607 22.715 -41.497 1.00 23.32 ? 265 ASN   B CB  1 
ATOM   4151 C CG  . ASN   B 1 243 ? -16.379 23.948 -41.886 1.00 24.49 ? 265 ASN   B CG  1 
ATOM   4152 O OD1 . ASN   B 1 243 ? -17.306 23.863 -42.692 1.00 31.16 ? 265 ASN   B OD1 1 
ATOM   4153 N ND2 . ASN   B 1 243 ? -15.990 25.090 -41.363 1.00 24.39 ? 265 ASN   B ND2 1 
ATOM   4154 N N   . PHE   B 1 244 ? -13.031 21.176 -40.885 1.00 21.65 ? 266 PHE   B N   1 
ATOM   4155 C CA  . PHE   B 1 244 ? -12.696 19.986 -40.126 1.00 21.34 ? 266 PHE   B CA  1 
ATOM   4156 C C   . PHE   B 1 244 ? -13.673 19.906 -38.962 1.00 21.81 ? 266 PHE   B C   1 
ATOM   4157 O O   . PHE   B 1 244 ? -13.697 20.807 -38.133 1.00 22.76 ? 266 PHE   B O   1 
ATOM   4158 C CB  . PHE   B 1 244 ? -11.269 20.082 -39.582 1.00 21.65 ? 266 PHE   B CB  1 
ATOM   4159 C CG  . PHE   B 1 244 ? -10.170 20.124 -40.626 1.00 21.42 ? 266 PHE   B CG  1 
ATOM   4160 C CD1 . PHE   B 1 244 ? -9.852  21.306 -41.291 1.00 23.05 ? 266 PHE   B CD1 1 
ATOM   4161 C CD2 . PHE   B 1 244 ? -9.456  18.981 -40.944 1.00 22.28 ? 266 PHE   B CD2 1 
ATOM   4162 C CE1 . PHE   B 1 244 ? -8.848  21.336 -42.249 1.00 23.58 ? 266 PHE   B CE1 1 
ATOM   4163 C CE2 . PHE   B 1 244 ? -8.459  19.017 -41.907 1.00 23.26 ? 266 PHE   B CE2 1 
ATOM   4164 C CZ  . PHE   B 1 244 ? -8.155  20.190 -42.553 1.00 23.74 ? 266 PHE   B CZ  1 
ATOM   4165 N N   . SER   B 1 245 ? -14.508 18.869 -38.928 1.00 21.91 ? 267 SER   B N   1 
ATOM   4166 C CA  . SER   B 1 245 ? -15.378 18.638 -37.785 1.00 22.61 ? 267 SER   B CA  1 
ATOM   4167 C C   . SER   B 1 245 ? -14.633 17.727 -36.818 1.00 23.70 ? 267 SER   B C   1 
ATOM   4168 O O   . SER   B 1 245 ? -14.182 16.674 -37.246 1.00 24.52 ? 267 SER   B O   1 
ATOM   4169 C CB  . SER   B 1 245 ? -16.671 17.998 -38.211 1.00 22.70 ? 267 SER   B CB  1 
ATOM   4170 O OG  . SER   B 1 245 ? -17.500 17.730 -37.094 1.00 24.17 ? 267 SER   B OG  1 
ATOM   4171 N N   . VAL   B 1 246 ? -14.467 18.142 -35.554 1.00 23.58 ? 268 VAL   B N   1 
ATOM   4172 C CA  . VAL   B 1 246 ? -13.600 17.415 -34.634 1.00 24.45 ? 268 VAL   B CA  1 
ATOM   4173 C C   . VAL   B 1 246 ? -14.270 17.145 -33.287 1.00 25.16 ? 268 VAL   B C   1 
ATOM   4174 O O   . VAL   B 1 246 ? -13.621 16.571 -32.413 1.00 26.32 ? 268 VAL   B O   1 
ATOM   4175 C CB  . VAL   B 1 246 ? -12.281 18.179 -34.415 1.00 25.15 ? 268 VAL   B CB  1 
ATOM   4176 C CG1 . VAL   B 1 246 ? -11.462 18.297 -35.693 1.00 25.82 ? 268 VAL   B CG1 1 
ATOM   4177 C CG2 . VAL   B 1 246 ? -12.534 19.550 -33.786 1.00 24.78 ? 268 VAL   B CG2 1 
ATOM   4178 N N   . THR   B 1 247 ? -15.526 17.562 -33.085 1.00 25.88 ? 269 THR   B N   1 
ATOM   4179 C CA  . THR   B 1 247 ? -16.145 17.431 -31.765 1.00 27.85 ? 269 THR   B CA  1 
ATOM   4180 C C   . THR   B 1 247 ? -16.539 15.981 -31.505 1.00 28.37 ? 269 THR   B C   1 
ATOM   4181 O O   . THR   B 1 247 ? -16.583 15.545 -30.355 1.00 29.05 ? 269 THR   B O   1 
ATOM   4182 C CB  . THR   B 1 247 ? -17.351 18.361 -31.637 1.00 27.49 ? 269 THR   B CB  1 
ATOM   4183 O OG1 . THR   B 1 247 ? -18.095 18.226 -32.846 1.00 27.37 ? 269 THR   B OG1 1 
ATOM   4184 C CG2 . THR   B 1 247 ? -16.945 19.809 -31.455 1.00 29.18 ? 269 THR   B CG2 1 
ATOM   4185 N N   . GLY   B 1 248 ? -16.871 15.253 -32.574 1.00 29.45 ? 270 GLY   B N   1 
ATOM   4186 C CA  . GLY   B 1 248 ? -17.189 13.841 -32.482 1.00 30.74 ? 270 GLY   B CA  1 
ATOM   4187 C C   . GLY   B 1 248 ? -16.300 13.041 -33.425 1.00 30.47 ? 270 GLY   B C   1 
ATOM   4188 O O   . GLY   B 1 248 ? -15.083 12.978 -33.249 1.00 30.56 ? 270 GLY   B O   1 
ATOM   4189 N N   . GLY   B 1 249 ? -16.911 12.452 -34.449 1.00 31.21 ? 271 GLY   B N   1 
ATOM   4190 C CA  . GLY   B 1 249 ? -16.137 11.798 -35.489 1.00 32.66 ? 271 GLY   B CA  1 
ATOM   4191 C C   . GLY   B 1 249 ? -15.289 12.831 -36.230 1.00 32.51 ? 271 GLY   B C   1 
ATOM   4192 O O   . GLY   B 1 249 ? -15.627 14.011 -36.213 1.00 32.60 ? 271 GLY   B O   1 
ATOM   4193 N N   . LYS   B 1 250 ? -14.187 12.381 -36.849 1.00 32.42 ? 272 LYS   B N   1 
ATOM   4194 C CA  A LYS   B 1 250 ? -13.302 13.274 -37.581 0.50 32.53 ? 272 LYS   B CA  1 
ATOM   4195 C CA  B LYS   B 1 250 ? -13.300 13.271 -37.581 0.50 32.36 ? 272 LYS   B CA  1 
ATOM   4196 C C   . LYS   B 1 250 ? -13.760 13.341 -39.036 1.00 32.45 ? 272 LYS   B C   1 
ATOM   4197 O O   . LYS   B 1 250 ? -13.449 12.453 -39.831 1.00 32.34 ? 272 LYS   B O   1 
ATOM   4198 C CB  A LYS   B 1 250 ? -11.836 12.857 -37.424 0.50 33.02 ? 272 LYS   B CB  1 
ATOM   4199 C CB  B LYS   B 1 250 ? -11.839 12.833 -37.432 0.50 32.65 ? 272 LYS   B CB  1 
ATOM   4200 C CG  A LYS   B 1 250 ? -11.329 12.839 -35.982 0.50 34.12 ? 272 LYS   B CG  1 
ATOM   4201 C CG  B LYS   B 1 250 ? -11.288 12.872 -36.004 0.50 33.46 ? 272 LYS   B CG  1 
ATOM   4202 C CD  A LYS   B 1 250 ? -11.885 13.963 -35.113 0.50 34.68 ? 272 LYS   B CD  1 
ATOM   4203 C CD  B LYS   B 1 250 ? -11.470 14.203 -35.281 0.50 34.22 ? 272 LYS   B CD  1 
ATOM   4204 C CE  A LYS   B 1 250 ? -11.504 13.848 -33.672 0.50 35.87 ? 272 LYS   B CE  1 
ATOM   4205 C CE  B LYS   B 1 250 ? -10.944 14.194 -33.877 0.50 35.00 ? 272 LYS   B CE  1 
ATOM   4206 N NZ  A LYS   B 1 250 ? -10.127 14.285 -33.428 0.50 36.49 ? 272 LYS   B NZ  1 
ATOM   4207 N NZ  B LYS   B 1 250 ? -11.719 13.340 -32.972 0.50 35.08 ? 272 LYS   B NZ  1 
ATOM   4208 N N   . TRP   B 1 251 ? -14.498 14.416 -39.367 1.00 30.40 ? 273 TRP   B N   1 
ATOM   4209 C CA  . TRP   B 1 251 ? -15.116 14.585 -40.675 1.00 29.84 ? 273 TRP   B CA  1 
ATOM   4210 C C   . TRP   B 1 251 ? -14.492 15.757 -41.425 1.00 28.18 ? 273 TRP   B C   1 
ATOM   4211 O O   . TRP   B 1 251 ? -13.840 16.613 -40.827 1.00 27.07 ? 273 TRP   B O   1 
ATOM   4212 C CB  . TRP   B 1 251 ? -16.624 14.844 -40.545 1.00 31.75 ? 273 TRP   B CB  1 
ATOM   4213 C CG  . TRP   B 1 251 ? -17.356 14.028 -39.513 1.00 31.38 ? 273 TRP   B CG  1 
ATOM   4214 C CD1 . TRP   B 1 251 ? -18.101 14.544 -38.496 1.00 32.31 ? 273 TRP   B CD1 1 
ATOM   4215 C CD2 . TRP   B 1 251 ? -17.475 12.592 -39.411 1.00 32.89 ? 273 TRP   B CD2 1 
ATOM   4216 N NE1 . TRP   B 1 251 ? -18.643 13.539 -37.743 1.00 32.49 ? 273 TRP   B NE1 1 
ATOM   4217 C CE2 . TRP   B 1 251 ? -18.280 12.333 -38.280 1.00 33.82 ? 273 TRP   B CE2 1 
ATOM   4218 C CE3 . TRP   B 1 251 ? -16.972 11.507 -40.139 1.00 33.84 ? 273 TRP   B CE3 1 
ATOM   4219 C CZ2 . TRP   B 1 251 ? -18.598 11.038 -37.871 1.00 34.26 ? 273 TRP   B CZ2 1 
ATOM   4220 C CZ3 . TRP   B 1 251 ? -17.278 10.225 -39.729 1.00 34.64 ? 273 TRP   B CZ3 1 
ATOM   4221 C CH2 . TRP   B 1 251 ? -18.087 9.997  -38.615 1.00 35.31 ? 273 TRP   B CH2 1 
ATOM   4222 N N   . ILE   B 1 252 ? -14.704 15.757 -42.748 1.00 26.11 ? 274 ILE   B N   1 
ATOM   4223 C CA  . ILE   B 1 252 ? -14.605 16.945 -43.579 1.00 26.09 ? 274 ILE   B CA  1 
ATOM   4224 C C   . ILE   B 1 252 ? -16.036 17.333 -43.926 1.00 26.82 ? 274 ILE   B C   1 
ATOM   4225 O O   . ILE   B 1 252 ? -16.835 16.466 -44.271 1.00 26.84 ? 274 ILE   B O   1 
ATOM   4226 C CB  . ILE   B 1 252 ? -13.778 16.675 -44.849 1.00 26.27 ? 274 ILE   B CB  1 
ATOM   4227 C CG1 . ILE   B 1 252 ? -12.344 16.249 -44.523 1.00 27.11 ? 274 ILE   B CG1 1 
ATOM   4228 C CG2 . ILE   B 1 252 ? -13.823 17.856 -45.822 1.00 26.00 ? 274 ILE   B CG2 1 
ATOM   4229 C CD1 . ILE   B 1 252 ? -11.511 17.275 -43.779 1.00 26.20 ? 274 ILE   B CD1 1 
ATOM   4230 N N   . VAL   B 1 253 ? -16.347 18.625 -43.796 1.00 26.14 ? 275 VAL   B N   1 
ATOM   4231 C CA  . VAL   B 1 253 ? -17.661 19.157 -44.119 1.00 26.88 ? 275 VAL   B CA  1 
ATOM   4232 C C   . VAL   B 1 253 ? -17.514 20.221 -45.206 1.00 26.99 ? 275 VAL   B C   1 
ATOM   4233 O O   . VAL   B 1 253 ? -16.617 21.054 -45.135 1.00 26.26 ? 275 VAL   B O   1 
ATOM   4234 C CB  . VAL   B 1 253 ? -18.320 19.740 -42.853 1.00 26.44 ? 275 VAL   B CB  1 
ATOM   4235 C CG1 . VAL   B 1 253 ? -19.695 20.327 -43.137 1.00 26.65 ? 275 VAL   B CG1 1 
ATOM   4236 C CG2 . VAL   B 1 253 ? -18.419 18.709 -41.736 1.00 25.70 ? 275 VAL   B CG2 1 
ATOM   4237 N N   . SER   B 1 254 ? -18.417 20.205 -46.194 1.00 26.70 ? 276 SER   B N   1 
ATOM   4238 C CA  . SER   B 1 254 ? -18.453 21.256 -47.197 1.00 26.03 ? 276 SER   B CA  1 
ATOM   4239 C C   . SER   B 1 254 ? -19.873 21.456 -47.721 1.00 27.16 ? 276 SER   B C   1 
ATOM   4240 O O   . SER   B 1 254 ? -20.670 20.530 -47.755 1.00 28.75 ? 276 SER   B O   1 
ATOM   4241 C CB  . SER   B 1 254 ? -17.508 20.955 -48.334 1.00 26.24 ? 276 SER   B CB  1 
ATOM   4242 O OG  . SER   B 1 254 ? -17.548 21.982 -49.319 1.00 26.47 ? 276 SER   B OG  1 
ATOM   4243 N N   . GLY   B 1 255 ? -20.169 22.689 -48.133 1.00 25.98 ? 277 GLY   B N   1 
ATOM   4244 C CA  . GLY   B 1 255 ? -21.297 22.972 -49.000 1.00 26.13 ? 277 GLY   B CA  1 
ATOM   4245 C C   . GLY   B 1 255 ? -21.072 22.424 -50.411 1.00 26.86 ? 277 GLY   B C   1 
ATOM   4246 O O   . GLY   B 1 255 ? -20.046 21.823 -50.712 1.00 25.44 ? 277 GLY   B O   1 
ATOM   4247 N N   . SER   B 1 256 ? -22.054 22.647 -51.283 1.00 27.82 ? 278 SER   B N   1 
ATOM   4248 C CA  . SER   B 1 256 ? -22.063 22.069 -52.615 1.00 29.27 ? 278 SER   B CA  1 
ATOM   4249 C C   . SER   B 1 256 ? -23.063 22.842 -53.466 1.00 30.11 ? 278 SER   B C   1 
ATOM   4250 O O   . SER   B 1 256 ? -24.009 23.427 -52.940 1.00 30.67 ? 278 SER   B O   1 
ATOM   4251 C CB  . SER   B 1 256 ? -22.406 20.584 -52.568 1.00 29.42 ? 278 SER   B CB  1 
ATOM   4252 O OG  . SER   B 1 256 ? -22.292 19.985 -53.853 1.00 32.03 ? 278 SER   B OG  1 
ATOM   4253 N N   . GLU   B 1 257 ? -22.847 22.821 -54.784 1.00 32.27 ? 279 GLU   B N   1 
ATOM   4254 C CA  . GLU   B 1 257 ? -23.679 23.570 -55.711 1.00 31.26 ? 279 GLU   B CA  1 
ATOM   4255 C C   . GLU   B 1 257 ? -24.924 22.767 -56.106 1.00 33.97 ? 279 GLU   B C   1 
ATOM   4256 O O   . GLU   B 1 257 ? -25.743 23.255 -56.885 1.00 36.22 ? 279 GLU   B O   1 
ATOM   4257 C CB  . GLU   B 1 257 ? -22.834 23.984 -56.917 1.00 30.64 ? 279 GLU   B CB  1 
ATOM   4258 C CG  . GLU   B 1 257 ? -21.749 25.005 -56.589 1.00 30.17 ? 279 GLU   B CG  1 
ATOM   4259 C CD  . GLU   B 1 257 ? -20.595 25.100 -57.577 1.00 29.55 ? 279 GLU   B CD  1 
ATOM   4260 O OE1 . GLU   B 1 257 ? -20.631 24.465 -58.659 1.00 27.95 ? 279 GLU   B OE1 1 
ATOM   4261 O OE2 . GLU   B 1 257 ? -19.630 25.809 -57.230 1.00 28.97 ? 279 GLU   B OE2 1 
ATOM   4262 N N   . ASP   B 1 258 ? -25.071 21.549 -55.566 1.00 34.09 ? 280 ASP   B N   1 
ATOM   4263 C CA  . ASP   B 1 258 ? -26.268 20.748 -55.762 1.00 36.49 ? 280 ASP   B CA  1 
ATOM   4264 C C   . ASP   B 1 258 ? -27.176 20.878 -54.540 1.00 36.24 ? 280 ASP   B C   1 
ATOM   4265 O O   . ASP   B 1 258 ? -28.079 20.060 -54.354 1.00 37.24 ? 280 ASP   B O   1 
ATOM   4266 C CB  . ASP   B 1 258 ? -25.904 19.304 -56.059 1.00 38.41 ? 280 ASP   B CB  1 
ATOM   4267 C CG  . ASP   B 1 258 ? -25.175 18.567 -54.946 1.00 39.12 ? 280 ASP   B CG  1 
ATOM   4268 O OD1 . ASP   B 1 258 ? -24.870 19.204 -53.923 1.00 35.94 ? 280 ASP   B OD1 1 
ATOM   4269 O OD2 . ASP   B 1 258 ? -24.918 17.358 -55.117 1.00 39.52 ? 280 ASP   B OD2 1 
ATOM   4270 N N   . ASN   B 1 259 ? -26.890 21.891 -53.707 1.00 36.85 ? 281 ASN   B N   1 
ATOM   4271 C CA  . ASN   B 1 259 ? -27.748 22.348 -52.623 1.00 35.69 ? 281 ASN   B CA  1 
ATOM   4272 C C   . ASN   B 1 259 ? -27.658 21.421 -51.411 1.00 34.89 ? 281 ASN   B C   1 
ATOM   4273 O O   . ASN   B 1 259 ? -28.502 21.510 -50.523 1.00 34.85 ? 281 ASN   B O   1 
ATOM   4274 C CB  . ASN   B 1 259 ? -29.203 22.503 -53.055 1.00 35.66 ? 281 ASN   B CB  1 
ATOM   4275 C CG  . ASN   B 1 259 ? -29.360 23.344 -54.301 1.00 36.16 ? 281 ASN   B CG  1 
ATOM   4276 O OD1 . ASN   B 1 259 ? -28.391 23.947 -54.780 1.00 37.58 ? 281 ASN   B OD1 1 
ATOM   4277 N ND2 . ASN   B 1 259 ? -30.578 23.408 -54.824 1.00 37.12 ? 281 ASN   B ND2 1 
ATOM   4278 N N   . LEU   B 1 260 ? -26.625 20.570 -51.349 1.00 33.98 ? 282 LEU   B N   1 
ATOM   4279 C CA  . LEU   B 1 260 ? -26.466 19.661 -50.225 1.00 33.48 ? 282 LEU   B CA  1 
ATOM   4280 C C   . LEU   B 1 260 ? -25.257 20.063 -49.390 1.00 33.51 ? 282 LEU   B C   1 
ATOM   4281 O O   . LEU   B 1 260 ? -24.304 20.647 -49.895 1.00 35.76 ? 282 LEU   B O   1 
ATOM   4282 C CB  . LEU   B 1 260 ? -26.298 18.218 -50.693 1.00 34.37 ? 282 LEU   B CB  1 
ATOM   4283 C CG  . LEU   B 1 260 ? -27.410 17.660 -51.583 1.00 34.64 ? 282 LEU   B CG  1 
ATOM   4284 C CD1 . LEU   B 1 260 ? -27.014 16.296 -52.128 1.00 36.99 ? 282 LEU   B CD1 1 
ATOM   4285 C CD2 . LEU   B 1 260 ? -28.724 17.569 -50.822 1.00 36.22 ? 282 LEU   B CD2 1 
ATOM   4286 N N   . VAL   B 1 261 ? -25.312 19.719 -48.102 1.00 32.80 ? 283 VAL   B N   1 
ATOM   4287 C CA  . VAL   B 1 261 ? -24.124 19.655 -47.269 1.00 32.83 ? 283 VAL   B CA  1 
ATOM   4288 C C   . VAL   B 1 261 ? -23.547 18.244 -47.377 1.00 33.61 ? 283 VAL   B C   1 
ATOM   4289 O O   . VAL   B 1 261 ? -24.266 17.275 -47.151 1.00 35.93 ? 283 VAL   B O   1 
ATOM   4290 C CB  . VAL   B 1 261 ? -24.417 19.998 -45.798 1.00 31.75 ? 283 VAL   B CB  1 
ATOM   4291 C CG1 . VAL   B 1 261 ? -23.174 19.810 -44.936 1.00 32.13 ? 283 VAL   B CG1 1 
ATOM   4292 C CG2 . VAL   B 1 261 ? -24.987 21.400 -45.630 1.00 33.45 ? 283 VAL   B CG2 1 
ATOM   4293 N N   . TYR   B 1 262 ? -22.245 18.152 -47.694 1.00 31.58 ? 284 TYR   B N   1 
ATOM   4294 C CA  . TYR   B 1 262 ? -21.519 16.890 -47.767 1.00 31.22 ? 284 TYR   B CA  1 
ATOM   4295 C C   . TYR   B 1 262 ? -20.621 16.716 -46.546 1.00 29.19 ? 284 TYR   B C   1 
ATOM   4296 O O   . TYR   B 1 262 ? -19.935 17.649 -46.162 1.00 28.05 ? 284 TYR   B O   1 
ATOM   4297 C CB  . TYR   B 1 262 ? -20.620 16.821 -49.004 1.00 32.43 ? 284 TYR   B CB  1 
ATOM   4298 C CG  . TYR   B 1 262 ? -21.387 16.471 -50.268 1.00 33.56 ? 284 TYR   B CG  1 
ATOM   4299 C CD1 . TYR   B 1 262 ? -22.298 17.362 -50.823 1.00 34.08 ? 284 TYR   B CD1 1 
ATOM   4300 C CD2 . TYR   B 1 262 ? -21.213 15.242 -50.889 1.00 35.27 ? 284 TYR   B CD2 1 
ATOM   4301 C CE1 . TYR   B 1 262 ? -23.019 17.038 -51.960 1.00 35.57 ? 284 TYR   B CE1 1 
ATOM   4302 C CE2 . TYR   B 1 262 ? -21.919 14.909 -52.031 1.00 36.22 ? 284 TYR   B CE2 1 
ATOM   4303 C CZ  . TYR   B 1 262 ? -22.831 15.803 -52.558 1.00 35.32 ? 284 TYR   B CZ  1 
ATOM   4304 O OH  . TYR   B 1 262 ? -23.538 15.445 -53.658 1.00 36.21 ? 284 TYR   B OH  1 
ATOM   4305 N N   . ILE   B 1 263 ? -20.573 15.484 -46.022 1.00 29.30 ? 285 ILE   B N   1 
ATOM   4306 C CA  . ILE   B 1 263 ? -19.735 15.114 -44.896 1.00 28.91 ? 285 ILE   B CA  1 
ATOM   4307 C C   . ILE   B 1 263 ? -18.966 13.854 -45.288 1.00 30.79 ? 285 ILE   B C   1 
ATOM   4308 O O   . ILE   B 1 263 ? -19.582 12.877 -45.709 1.00 32.89 ? 285 ILE   B O   1 
ATOM   4309 C CB  . ILE   B 1 263 ? -20.586 14.888 -43.629 1.00 28.97 ? 285 ILE   B CB  1 
ATOM   4310 C CG1 . ILE   B 1 263 ? -21.577 16.037 -43.391 1.00 28.91 ? 285 ILE   B CG1 1 
ATOM   4311 C CG2 . ILE   B 1 263 ? -19.692 14.627 -42.411 1.00 27.07 ? 285 ILE   B CG2 1 
ATOM   4312 C CD1 . ILE   B 1 263 ? -22.374 15.927 -42.101 1.00 30.73 ? 285 ILE   B CD1 1 
ATOM   4313 N N   . TRP   B 1 264 ? -17.629 13.909 -45.192 1.00 31.18 ? 286 TRP   B N   1 
ATOM   4314 C CA  . TRP   B 1 264 ? -16.761 12.774 -45.470 1.00 32.35 ? 286 TRP   B CA  1 
ATOM   4315 C C   . TRP   B 1 264 ? -16.074 12.309 -44.187 1.00 33.61 ? 286 TRP   B C   1 
ATOM   4316 O O   . TRP   B 1 264 ? -15.721 13.116 -43.332 1.00 33.32 ? 286 TRP   B O   1 
ATOM   4317 C CB  . TRP   B 1 264 ? -15.667 13.123 -46.491 1.00 33.07 ? 286 TRP   B CB  1 
ATOM   4318 C CG  . TRP   B 1 264 ? -16.113 13.520 -47.874 1.00 32.96 ? 286 TRP   B CG  1 
ATOM   4319 C CD1 . TRP   B 1 264 ? -16.173 12.710 -48.967 1.00 34.53 ? 286 TRP   B CD1 1 
ATOM   4320 C CD2 . TRP   B 1 264 ? -16.513 14.832 -48.330 1.00 33.74 ? 286 TRP   B CD2 1 
ATOM   4321 N NE1 . TRP   B 1 264 ? -16.582 13.418 -50.064 1.00 34.46 ? 286 TRP   B NE1 1 
ATOM   4322 C CE2 . TRP   B 1 264 ? -16.806 14.717 -49.708 1.00 34.10 ? 286 TRP   B CE2 1 
ATOM   4323 C CE3 . TRP   B 1 264 ? -16.661 16.084 -47.720 1.00 32.92 ? 286 TRP   B CE3 1 
ATOM   4324 C CZ2 . TRP   B 1 264 ? -17.232 15.800 -50.474 1.00 34.70 ? 286 TRP   B CZ2 1 
ATOM   4325 C CZ3 . TRP   B 1 264 ? -17.079 17.152 -48.481 1.00 33.15 ? 286 TRP   B CZ3 1 
ATOM   4326 C CH2 . TRP   B 1 264 ? -17.367 17.009 -49.835 1.00 33.21 ? 286 TRP   B CH2 1 
ATOM   4327 N N   . ASN   B 1 265 ? -15.806 11.004 -44.112 1.00 35.20 ? 287 ASN   B N   1 
ATOM   4328 C CA  . ASN   B 1 265 ? -14.808 10.468 -43.204 1.00 36.69 ? 287 ASN   B CA  1 
ATOM   4329 C C   . ASN   B 1 265 ? -13.437 10.966 -43.660 1.00 35.92 ? 287 ASN   B C   1 
ATOM   4330 O O   . ASN   B 1 265 ? -13.046 10.764 -44.805 1.00 37.25 ? 287 ASN   B O   1 
ATOM   4331 C CB  . ASN   B 1 265 ? -14.920 8.949  -43.155 1.00 38.79 ? 287 ASN   B CB  1 
ATOM   4332 C CG  . ASN   B 1 265 ? -13.831 8.279  -42.350 1.00 38.70 ? 287 ASN   B CG  1 
ATOM   4333 O OD1 . ASN   B 1 265 ? -12.650 8.629  -42.460 1.00 39.81 ? 287 ASN   B OD1 1 
ATOM   4334 N ND2 . ASN   B 1 265 ? -14.201 7.286  -41.561 1.00 41.00 ? 287 ASN   B ND2 1 
ATOM   4335 N N   . LEU   B 1 266 ? -12.708 11.625 -42.757 1.00 36.73 ? 288 LEU   B N   1 
ATOM   4336 C CA  . LEU   B 1 266 ? -11.470 12.297 -43.122 1.00 35.13 ? 288 LEU   B CA  1 
ATOM   4337 C C   . LEU   B 1 266 ? -10.432 11.288 -43.607 1.00 37.07 ? 288 LEU   B C   1 
ATOM   4338 O O   . LEU   B 1 266 ? -9.712  11.561 -44.567 1.00 36.79 ? 288 LEU   B O   1 
ATOM   4339 C CB  . LEU   B 1 266 ? -10.966 13.096 -41.923 1.00 35.32 ? 288 LEU   B CB  1 
ATOM   4340 C CG  . LEU   B 1 266 ? -9.737  13.980 -42.161 1.00 35.49 ? 288 LEU   B CG  1 
ATOM   4341 C CD1 . LEU   B 1 266 ? -9.784  15.181 -41.234 1.00 34.62 ? 288 LEU   B CD1 1 
ATOM   4342 C CD2 . LEU   B 1 266 ? -8.427  13.230 -41.961 1.00 36.41 ? 288 LEU   B CD2 1 
ATOM   4343 N N   . GLN   B 1 267 ? -10.360 10.129 -42.939 1.00 38.30 ? 289 GLN   B N   1 
ATOM   4344 C CA  . GLN   B 1 267 ? -9.355  9.125  -43.245 1.00 40.81 ? 289 GLN   B CA  1 
ATOM   4345 C C   . GLN   B 1 267 ? -9.756  8.260  -44.443 1.00 41.15 ? 289 GLN   B C   1 
ATOM   4346 O O   . GLN   B 1 267 ? -8.906  7.974  -45.284 1.00 41.00 ? 289 GLN   B O   1 
ATOM   4347 C CB  . GLN   B 1 267 ? -9.065  8.223  -42.041 1.00 40.66 ? 289 GLN   B CB  1 
ATOM   4348 C CG  . GLN   B 1 267 ? -8.371  8.941  -40.890 1.00 42.73 ? 289 GLN   B CG  1 
ATOM   4349 C CD  . GLN   B 1 267 ? -7.043  9.567  -41.265 1.00 44.87 ? 289 GLN   B CD  1 
ATOM   4350 O OE1 . GLN   B 1 267 ? -6.396  9.197  -42.251 1.00 50.72 ? 289 GLN   B OE1 1 
ATOM   4351 N NE2 . GLN   B 1 267 ? -6.609  10.521 -40.455 1.00 46.42 ? 289 GLN   B NE2 1 
ATOM   4352 N N   . THR   B 1 268 ? -11.018 7.805  -44.508 1.00 41.98 ? 290 THR   B N   1 
ATOM   4353 C CA  . THR   B 1 268 ? -11.411 6.850  -45.541 1.00 41.28 ? 290 THR   B CA  1 
ATOM   4354 C C   . THR   B 1 268 ? -11.825 7.589  -46.811 1.00 41.23 ? 290 THR   B C   1 
ATOM   4355 O O   . THR   B 1 268 ? -11.763 7.013  -47.895 1.00 41.36 ? 290 THR   B O   1 
ATOM   4356 C CB  . THR   B 1 268 ? -12.532 5.918  -45.073 1.00 44.59 ? 290 THR   B CB  1 
ATOM   4357 O OG1 . THR   B 1 268 ? -13.704 6.720  -44.949 1.00 42.32 ? 290 THR   B OG1 1 
ATOM   4358 C CG2 . THR   B 1 268 ? -12.178 5.173  -43.797 1.00 45.82 ? 290 THR   B CG2 1 
ATOM   4359 N N   . LYS   B 1 269 ? -12.278 8.842  -46.659 1.00 40.81 ? 291 LYS   B N   1 
ATOM   4360 C CA  . LYS   B 1 269 ? -12.651 9.701  -47.772 1.00 41.29 ? 291 LYS   B CA  1 
ATOM   4361 C C   . LYS   B 1 269 ? -14.032 9.334  -48.309 1.00 41.63 ? 291 LYS   B C   1 
ATOM   4362 O O   . LYS   B 1 269 ? -14.435 9.872  -49.332 1.00 44.38 ? 291 LYS   B O   1 
ATOM   4363 C CB  . LYS   B 1 269 ? -11.651 9.666  -48.936 1.00 42.07 ? 291 LYS   B CB  1 
ATOM   4364 C CG  . LYS   B 1 269 ? -10.214 10.025 -48.576 1.00 42.14 ? 291 LYS   B CG  1 
ATOM   4365 C CD  . LYS   B 1 269 ? -9.174  9.555  -49.589 1.00 44.85 ? 291 LYS   B CD  1 
ATOM   4366 C CE  . LYS   B 1 269 ? -8.900  8.080  -49.492 1.00 46.32 ? 291 LYS   B CE  1 
ATOM   4367 N NZ  . LYS   B 1 269 ? -8.111  7.553  -50.613 1.00 46.67 ? 291 LYS   B NZ  1 
ATOM   4368 N N   . GLU   B 1 270 ? -14.753 8.440  -47.621 1.00 41.93 ? 292 GLU   B N   1 
ATOM   4369 C CA  . GLU   B 1 270 ? -16.095 8.037  -48.020 1.00 42.86 ? 292 GLU   B CA  1 
ATOM   4370 C C   . GLU   B 1 270 ? -17.091 9.087  -47.533 1.00 40.77 ? 292 GLU   B C   1 
ATOM   4371 O O   . GLU   B 1 270 ? -16.960 9.605  -46.428 1.00 39.72 ? 292 GLU   B O   1 
ATOM   4372 C CB  . GLU   B 1 270 ? -16.451 6.665  -47.435 1.00 42.87 ? 292 GLU   B CB  1 
ATOM   4373 N N   . ILE   B 1 271 ? -18.075 9.413  -48.375 1.00 38.86 ? 293 ILE   B N   1 
ATOM   4374 C CA  . ILE   B 1 271 ? -19.195 10.239 -47.952 1.00 39.17 ? 293 ILE   B CA  1 
ATOM   4375 C C   . ILE   B 1 271 ? -20.005 9.455  -46.926 1.00 40.69 ? 293 ILE   B C   1 
ATOM   4376 O O   . ILE   B 1 271 ? -20.460 8.341  -47.209 1.00 43.52 ? 293 ILE   B O   1 
ATOM   4377 C CB  . ILE   B 1 271 ? -20.080 10.653 -49.137 1.00 41.03 ? 293 ILE   B CB  1 
ATOM   4378 C CG1 . ILE   B 1 271 ? -19.320 11.554 -50.109 1.00 43.10 ? 293 ILE   B CG1 1 
ATOM   4379 C CG2 . ILE   B 1 271 ? -21.376 11.307 -48.650 1.00 39.87 ? 293 ILE   B CG2 1 
ATOM   4380 C CD1 . ILE   B 1 271 ? -19.927 11.610 -51.501 1.00 43.66 ? 293 ILE   B CD1 1 
ATOM   4381 N N   . VAL   B 1 272 ? -20.208 10.080 -45.766 1.00 39.70 ? 294 VAL   B N   1 
ATOM   4382 C CA  . VAL   B 1 272 ? -20.871 9.435  -44.651 1.00 39.54 ? 294 VAL   B CA  1 
ATOM   4383 C C   . VAL   B 1 272 ? -22.236 10.083 -44.436 1.00 39.30 ? 294 VAL   B C   1 
ATOM   4384 O O   . VAL   B 1 272 ? -23.106 9.454  -43.845 1.00 41.56 ? 294 VAL   B O   1 
ATOM   4385 C CB  . VAL   B 1 272 ? -19.998 9.439  -43.380 1.00 39.79 ? 294 VAL   B CB  1 
ATOM   4386 C CG1 . VAL   B 1 272 ? -18.787 8.534  -43.554 1.00 40.20 ? 294 VAL   B CG1 1 
ATOM   4387 C CG2 . VAL   B 1 272 ? -19.564 10.838 -42.961 1.00 38.03 ? 294 VAL   B CG2 1 
ATOM   4388 N N   . GLN   B 1 273 ? -22.443 11.313 -44.934 1.00 38.09 ? 295 GLN   B N   1 
ATOM   4389 C CA  . GLN   B 1 273 ? -23.779 11.892 -44.921 1.00 36.83 ? 295 GLN   B CA  1 
ATOM   4390 C C   . GLN   B 1 273 ? -23.907 13.007 -45.961 1.00 37.16 ? 295 GLN   B C   1 
ATOM   4391 O O   . GLN   B 1 273 ? -22.927 13.670 -46.295 1.00 37.79 ? 295 GLN   B O   1 
ATOM   4392 C CB  . GLN   B 1 273 ? -24.103 12.392 -43.512 1.00 38.03 ? 295 GLN   B CB  1 
ATOM   4393 C CG  . GLN   B 1 273 ? -25.588 12.376 -43.175 1.00 39.36 ? 295 GLN   B CG  1 
ATOM   4394 C CD  . GLN   B 1 273 ? -25.910 12.875 -41.782 1.00 36.82 ? 295 GLN   B CD  1 
ATOM   4395 O OE1 . GLN   B 1 273 ? -25.032 13.178 -40.956 1.00 34.24 ? 295 GLN   B OE1 1 
ATOM   4396 N NE2 . GLN   B 1 273 ? -27.205 12.995 -41.530 1.00 36.43 ? 295 GLN   B NE2 1 
ATOM   4397 N N   . LYS   B 1 274 ? -25.138 13.190 -46.456 1.00 36.63 ? 296 LYS   B N   1 
ATOM   4398 C CA  . LYS   B 1 274 ? -25.519 14.312 -47.299 1.00 37.15 ? 296 LYS   B CA  1 
ATOM   4399 C C   . LYS   B 1 274 ? -26.775 14.932 -46.702 1.00 38.01 ? 296 LYS   B C   1 
ATOM   4400 O O   . LYS   B 1 274 ? -27.777 14.236 -46.497 1.00 40.66 ? 296 LYS   B O   1 
ATOM   4401 C CB  . LYS   B 1 274 ? -25.860 13.891 -48.731 1.00 39.15 ? 296 LYS   B CB  1 
ATOM   4402 C CG  . LYS   B 1 274 ? -24.712 13.365 -49.567 1.00 41.36 ? 296 LYS   B CG  1 
ATOM   4403 C CD  . LYS   B 1 274 ? -25.161 12.888 -50.945 1.00 45.19 ? 296 LYS   B CD  1 
ATOM   4404 C CE  . LYS   B 1 274 ? -24.129 12.016 -51.581 1.00 48.38 ? 296 LYS   B CE  1 
ATOM   4405 N NZ  . LYS   B 1 274 ? -24.530 11.544 -52.910 1.00 52.35 ? 296 LYS   B NZ  1 
ATOM   4406 N N   . LEU   B 1 275 ? -26.709 16.231 -46.406 1.00 33.72 ? 297 LEU   B N   1 
ATOM   4407 C CA  . LEU   B 1 275 ? -27.804 16.900 -45.728 1.00 35.51 ? 297 LEU   B CA  1 
ATOM   4408 C C   . LEU   B 1 275 ? -28.633 17.665 -46.758 1.00 36.79 ? 297 LEU   B C   1 
ATOM   4409 O O   . LEU   B 1 275 ? -28.157 18.615 -47.384 1.00 36.03 ? 297 LEU   B O   1 
ATOM   4410 C CB  . LEU   B 1 275 ? -27.289 17.812 -44.618 1.00 33.66 ? 297 LEU   B CB  1 
ATOM   4411 C CG  . LEU   B 1 275 ? -26.145 17.272 -43.750 1.00 33.69 ? 297 LEU   B CG  1 
ATOM   4412 C CD1 . LEU   B 1 275 ? -25.880 18.279 -42.653 1.00 33.95 ? 297 LEU   B CD1 1 
ATOM   4413 C CD2 . LEU   B 1 275 ? -26.428 15.903 -43.163 1.00 33.73 ? 297 LEU   B CD2 1 
ATOM   4414 N N   . GLN   B 1 276 ? -29.893 17.239 -46.893 1.00 39.39 ? 298 GLN   B N   1 
ATOM   4415 C CA  . GLN   B 1 276 ? -30.828 17.788 -47.857 1.00 40.62 ? 298 GLN   B CA  1 
ATOM   4416 C C   . GLN   B 1 276 ? -31.740 18.791 -47.153 1.00 40.75 ? 298 GLN   B C   1 
ATOM   4417 O O   . GLN   B 1 276 ? -32.140 18.560 -46.015 1.00 40.23 ? 298 GLN   B O   1 
ATOM   4418 C CB  . GLN   B 1 276 ? -31.542 16.561 -48.430 1.00 45.42 ? 298 GLN   B CB  1 
ATOM   4419 C CG  . GLN   B 1 276 ? -32.343 16.835 -49.698 1.00 51.42 ? 298 GLN   B CG  1 
ATOM   4420 C CD  . GLN   B 1 276 ? -33.759 17.304 -49.439 1.00 59.10 ? 298 GLN   B CD  1 
ATOM   4421 O OE1 . GLN   B 1 276 ? -34.279 17.232 -48.319 1.00 65.04 ? 298 GLN   B OE1 1 
ATOM   4422 N NE2 . GLN   B 1 276 ? -34.404 17.774 -50.497 1.00 64.28 ? 298 GLN   B NE2 1 
ATOM   4423 N N   . GLY   B 1 277 ? -32.067 19.909 -47.824 1.00 40.12 ? 299 GLY   B N   1 
ATOM   4424 C CA  . GLY   B 1 277 ? -33.010 20.871 -47.268 1.00 39.45 ? 299 GLY   B CA  1 
ATOM   4425 C C   . GLY   B 1 277 ? -32.950 22.229 -47.963 1.00 37.11 ? 299 GLY   B C   1 
ATOM   4426 O O   . GLY   B 1 277 ? -33.982 22.852 -48.210 1.00 37.23 ? 299 GLY   B O   1 
ATOM   4427 N N   . HIS   B 1 278 ? -31.732 22.707 -48.232 1.00 34.50 ? 300 HIS   B N   1 
ATOM   4428 C CA  . HIS   B 1 278 ? -31.548 24.019 -48.827 1.00 33.73 ? 300 HIS   B CA  1 
ATOM   4429 C C   . HIS   B 1 278 ? -32.107 24.000 -50.247 1.00 34.54 ? 300 HIS   B C   1 
ATOM   4430 O O   . HIS   B 1 278 ? -32.181 22.938 -50.869 1.00 35.94 ? 300 HIS   B O   1 
ATOM   4431 C CB  . HIS   B 1 278 ? -30.078 24.453 -48.772 1.00 32.05 ? 300 HIS   B CB  1 
ATOM   4432 C CG  . HIS   B 1 278 ? -29.629 25.002 -47.455 1.00 30.02 ? 300 HIS   B CG  1 
ATOM   4433 N ND1 . HIS   B 1 278 ? -30.106 26.193 -46.947 1.00 30.65 ? 300 HIS   B ND1 1 
ATOM   4434 C CD2 . HIS   B 1 278 ? -28.751 24.543 -46.550 1.00 30.13 ? 300 HIS   B CD2 1 
ATOM   4435 C CE1 . HIS   B 1 278 ? -29.514 26.445 -45.786 1.00 30.03 ? 300 HIS   B CE1 1 
ATOM   4436 N NE2 . HIS   B 1 278 ? -28.696 25.447 -45.518 1.00 29.30 ? 300 HIS   B NE2 1 
ATOM   4437 N N   . THR   B 1 279 ? -32.498 25.184 -50.745 1.00 33.48 ? 301 THR   B N   1 
ATOM   4438 C CA  . THR   B 1 279 ? -33.069 25.314 -52.077 1.00 33.36 ? 301 THR   B CA  1 
ATOM   4439 C C   . THR   B 1 279 ? -32.147 26.129 -52.987 1.00 32.62 ? 301 THR   B C   1 
ATOM   4440 O O   . THR   B 1 279 ? -32.571 26.577 -54.049 1.00 32.81 ? 301 THR   B O   1 
ATOM   4441 C CB  . THR   B 1 279 ? -34.467 25.929 -51.978 1.00 34.74 ? 301 THR   B CB  1 
ATOM   4442 O OG1 . THR   B 1 279 ? -34.311 27.177 -51.311 1.00 34.90 ? 301 THR   B OG1 1 
ATOM   4443 C CG2 . THR   B 1 279 ? -35.447 25.041 -51.230 1.00 35.69 ? 301 THR   B CG2 1 
ATOM   4444 N N   . ASP   B 1 280 ? -30.875 26.291 -52.601 1.00 30.97 ? 302 ASP   B N   1 
ATOM   4445 C CA  . ASP   B 1 280 ? -29.880 26.881 -53.485 1.00 31.24 ? 302 ASP   B CA  1 
ATOM   4446 C C   . ASP   B 1 280 ? -28.502 26.432 -53.001 1.00 29.61 ? 302 ASP   B C   1 
ATOM   4447 O O   . ASP   B 1 280 ? -28.404 25.713 -52.010 1.00 32.05 ? 302 ASP   B O   1 
ATOM   4448 C CB  . ASP   B 1 280 ? -30.040 28.395 -53.565 1.00 32.20 ? 302 ASP   B CB  1 
ATOM   4449 C CG  . ASP   B 1 280 ? -29.499 29.096 -54.805 1.00 31.81 ? 302 ASP   B CG  1 
ATOM   4450 O OD1 . ASP   B 1 280 ? -28.724 28.470 -55.564 1.00 32.58 ? 302 ASP   B OD1 1 
ATOM   4451 O OD2 . ASP   B 1 280 ? -29.863 30.272 -55.008 1.00 31.76 ? 302 ASP   B OD2 1 
ATOM   4452 N N   . VAL   B 1 281 ? -27.458 26.839 -53.734 1.00 27.68 ? 303 VAL   B N   1 
ATOM   4453 C CA  . VAL   B 1 281 ? -26.075 26.488 -53.444 1.00 25.85 ? 303 VAL   B CA  1 
ATOM   4454 C C   . VAL   B 1 281 ? -25.808 26.685 -51.957 1.00 24.85 ? 303 VAL   B C   1 
ATOM   4455 O O   . VAL   B 1 281 ? -26.111 27.742 -51.409 1.00 24.51 ? 303 VAL   B O   1 
ATOM   4456 C CB  . VAL   B 1 281 ? -25.097 27.345 -54.270 1.00 27.21 ? 303 VAL   B CB  1 
ATOM   4457 C CG1 . VAL   B 1 281 ? -23.641 27.176 -53.828 1.00 26.71 ? 303 VAL   B CG1 1 
ATOM   4458 C CG2 . VAL   B 1 281 ? -25.246 27.119 -55.773 1.00 27.54 ? 303 VAL   B CG2 1 
ATOM   4459 N N   . VAL   B 1 282 ? -25.219 25.664 -51.329 1.00 24.43 ? 304 VAL   B N   1 
ATOM   4460 C CA  . VAL   B 1 282 ? -24.782 25.775 -49.950 1.00 23.82 ? 304 VAL   B CA  1 
ATOM   4461 C C   . VAL   B 1 282 ? -23.375 26.356 -49.987 1.00 22.93 ? 304 VAL   B C   1 
ATOM   4462 O O   . VAL   B 1 282 ? -22.406 25.649 -50.253 1.00 23.52 ? 304 VAL   B O   1 
ATOM   4463 C CB  . VAL   B 1 282 ? -24.837 24.447 -49.176 1.00 24.94 ? 304 VAL   B CB  1 
ATOM   4464 C CG1 . VAL   B 1 282 ? -24.389 24.613 -47.732 1.00 25.52 ? 304 VAL   B CG1 1 
ATOM   4465 C CG2 . VAL   B 1 282 ? -26.225 23.828 -49.257 1.00 26.33 ? 304 VAL   B CG2 1 
ATOM   4466 N N   . ILE   B 1 283 ? -23.291 27.662 -49.730 1.00 22.21 ? 305 ILE   B N   1 
ATOM   4467 C CA  . ILE   B 1 283 ? -22.069 28.417 -49.950 1.00 22.32 ? 305 ILE   B CA  1 
ATOM   4468 C C   . ILE   B 1 283 ? -21.157 28.319 -48.731 1.00 20.26 ? 305 ILE   B C   1 
ATOM   4469 O O   . ILE   B 1 283 ? -19.947 28.475 -48.856 1.00 20.67 ? 305 ILE   B O   1 
ATOM   4470 C CB  . ILE   B 1 283 ? -22.387 29.876 -50.315 1.00 21.83 ? 305 ILE   B CB  1 
ATOM   4471 C CG1 . ILE   B 1 283 ? -21.159 30.598 -50.873 1.00 22.85 ? 305 ILE   B CG1 1 
ATOM   4472 C CG2 . ILE   B 1 283 ? -23.007 30.646 -49.152 1.00 22.84 ? 305 ILE   B CG2 1 
ATOM   4473 C CD1 . ILE   B 1 283 ? -20.773 30.166 -52.272 1.00 23.09 ? 305 ILE   B CD1 1 
ATOM   4474 N N   . SER   B 1 284 ? -21.742 28.091 -47.552 1.00 20.80 ? 306 SER   B N   1 
ATOM   4475 C CA  . SER   B 1 284 ? -20.993 28.176 -46.313 1.00 20.39 ? 306 SER   B CA  1 
ATOM   4476 C C   . SER   B 1 284 ? -21.485 27.114 -45.335 1.00 20.56 ? 306 SER   B C   1 
ATOM   4477 O O   . SER   B 1 284 ? -22.689 26.899 -45.194 1.00 21.11 ? 306 SER   B O   1 
ATOM   4478 C CB  . SER   B 1 284 ? -21.101 29.562 -45.735 1.00 20.07 ? 306 SER   B CB  1 
ATOM   4479 O OG  . SER   B 1 284 ? -20.453 29.659 -44.472 1.00 20.05 ? 306 SER   B OG  1 
ATOM   4480 N N   . THR   B 1 285 ? -20.525 26.428 -44.709 1.00 20.49 ? 307 THR   B N   1 
ATOM   4481 C CA  . THR   B 1 285 ? -20.771 25.554 -43.572 1.00 20.47 ? 307 THR   B CA  1 
ATOM   4482 C C   . THR   B 1 285 ? -19.823 25.968 -42.450 1.00 20.43 ? 307 THR   B C   1 
ATOM   4483 O O   . THR   B 1 285 ? -18.763 26.548 -42.705 1.00 20.97 ? 307 THR   B O   1 
ATOM   4484 C CB  . THR   B 1 285 ? -20.592 24.078 -43.934 1.00 21.57 ? 307 THR   B CB  1 
ATOM   4485 O OG1 . THR   B 1 285 ? -19.310 23.940 -44.535 1.00 21.95 ? 307 THR   B OG1 1 
ATOM   4486 C CG2 . THR   B 1 285 ? -21.615 23.574 -44.938 1.00 21.85 ? 307 THR   B CG2 1 
ATOM   4487 N N   . ALA   B 1 286 ? -20.242 25.670 -41.213 1.00 19.74 ? 308 ALA   B N   1 
ATOM   4488 C CA  . ALA   B 1 286 ? -19.453 25.930 -40.026 1.00 19.52 ? 308 ALA   B CA  1 
ATOM   4489 C C   . ALA   B 1 286 ? -19.776 24.862 -38.989 1.00 20.50 ? 308 ALA   B C   1 
ATOM   4490 O O   . ALA   B 1 286 ? -20.918 24.391 -38.901 1.00 20.44 ? 308 ALA   B O   1 
ATOM   4491 C CB  . ALA   B 1 286 ? -19.740 27.309 -39.478 1.00 19.95 ? 308 ALA   B CB  1 
ATOM   4492 N N   . CYS   B 1 287 ? -18.763 24.563 -38.174 1.00 21.36 ? 309 CYS   B N   1 
ATOM   4493 C CA  . CYS   B 1 287 ? -18.822 23.509 -37.176 1.00 20.95 ? 309 CYS   B CA  1 
ATOM   4494 C C   . CYS   B 1 287 ? -18.678 24.127 -35.794 1.00 20.29 ? 309 CYS   B C   1 
ATOM   4495 O O   . CYS   B 1 287 ? -17.766 24.913 -35.560 1.00 20.68 ? 309 CYS   B O   1 
ATOM   4496 C CB  . CYS   B 1 287 ? -17.716 22.490 -37.390 1.00 22.14 ? 309 CYS   B CB  1 
ATOM   4497 S SG  . CYS   B 1 287 ? -17.880 21.577 -38.943 1.00 23.83 ? 309 CYS   B SG  1 
ATOM   4498 N N   . HIS   B 1 288 ? -19.595 23.757 -34.898 1.00 19.73 ? 310 HIS   B N   1 
ATOM   4499 C CA  . HIS   B 1 288 ? -19.621 24.287 -33.541 1.00 20.85 ? 310 HIS   B CA  1 
ATOM   4500 C C   . HIS   B 1 288 ? -18.374 23.867 -32.761 1.00 20.92 ? 310 HIS   B C   1 
ATOM   4501 O O   . HIS   B 1 288 ? -17.844 22.767 -32.945 1.00 21.22 ? 310 HIS   B O   1 
ATOM   4502 C CB  . HIS   B 1 288 ? -20.934 23.865 -32.877 1.00 20.22 ? 310 HIS   B CB  1 
ATOM   4503 C CG  . HIS   B 1 288 ? -21.202 24.541 -31.582 1.00 20.52 ? 310 HIS   B CG  1 
ATOM   4504 N ND1 . HIS   B 1 288 ? -20.679 24.096 -30.384 1.00 20.47 ? 310 HIS   B ND1 1 
ATOM   4505 C CD2 . HIS   B 1 288 ? -21.922 25.635 -31.298 1.00 20.33 ? 310 HIS   B CD2 1 
ATOM   4506 C CE1 . HIS   B 1 288 ? -21.097 24.902 -29.406 1.00 21.40 ? 310 HIS   B CE1 1 
ATOM   4507 N NE2 . HIS   B 1 288 ? -21.850 25.847 -29.940 1.00 20.83 ? 310 HIS   B NE2 1 
ATOM   4508 N N   . PRO   B 1 289 ? -17.827 24.729 -31.876 1.00 21.39 ? 311 PRO   B N   1 
ATOM   4509 C CA  . PRO   B 1 289 ? -16.566 24.398 -31.203 1.00 22.08 ? 311 PRO   B CA  1 
ATOM   4510 C C   . PRO   B 1 289 ? -16.601 23.250 -30.193 1.00 21.71 ? 311 PRO   B C   1 
ATOM   4511 O O   . PRO   B 1 289 ? -15.559 22.659 -29.933 1.00 21.78 ? 311 PRO   B O   1 
ATOM   4512 C CB  . PRO   B 1 289 ? -16.149 25.726 -30.547 1.00 21.25 ? 311 PRO   B CB  1 
ATOM   4513 C CG  . PRO   B 1 289 ? -17.459 26.456 -30.343 1.00 20.17 ? 311 PRO   B CG  1 
ATOM   4514 C CD  . PRO   B 1 289 ? -18.275 26.103 -31.596 1.00 20.37 ? 311 PRO   B CD  1 
ATOM   4515 N N   . THR   B 1 290 ? -17.765 22.935 -29.607 1.00 22.69 ? 312 THR   B N   1 
ATOM   4516 C CA  . THR   B 1 290 ? -17.824 21.895 -28.582 1.00 22.80 ? 312 THR   B CA  1 
ATOM   4517 C C   . THR   B 1 290 ? -18.882 20.822 -28.873 1.00 24.71 ? 312 THR   B C   1 
ATOM   4518 O O   . THR   B 1 290 ? -18.704 19.665 -28.472 1.00 26.09 ? 312 THR   B O   1 
ATOM   4519 C CB  . THR   B 1 290 ? -18.032 22.493 -27.186 1.00 22.76 ? 312 THR   B CB  1 
ATOM   4520 O OG1 . THR   B 1 290 ? -19.230 23.272 -27.158 1.00 22.12 ? 312 THR   B OG1 1 
ATOM   4521 C CG2 . THR   B 1 290 ? -16.829 23.296 -26.726 1.00 22.76 ? 312 THR   B CG2 1 
ATOM   4522 N N   . GLU   B 1 291 ? -19.986 21.192 -29.526 1.00 24.42 ? 313 GLU   B N   1 
ATOM   4523 C CA  . GLU   B 1 291 ? -21.061 20.259 -29.824 1.00 25.15 ? 313 GLU   B CA  1 
ATOM   4524 C C   . GLU   B 1 291 ? -21.035 19.825 -31.287 1.00 24.45 ? 313 GLU   B C   1 
ATOM   4525 O O   . GLU   B 1 291 ? -20.515 20.533 -32.140 1.00 24.35 ? 313 GLU   B O   1 
ATOM   4526 C CB  . GLU   B 1 291 ? -22.402 20.928 -29.532 1.00 26.32 ? 313 GLU   B CB  1 
ATOM   4527 C CG  . GLU   B 1 291 ? -22.615 21.227 -28.054 1.00 27.68 ? 313 GLU   B CG  1 
ATOM   4528 C CD  . GLU   B 1 291 ? -22.818 20.001 -27.182 1.00 27.64 ? 313 GLU   B CD  1 
ATOM   4529 O OE1 . GLU   B 1 291 ? -23.519 19.035 -27.585 1.00 26.65 ? 313 GLU   B OE1 1 
ATOM   4530 O OE2 . GLU   B 1 291 ? -22.287 20.036 -26.051 1.00 28.31 ? 313 GLU   B OE2 1 
ATOM   4531 N N   . ASN   B 1 292 ? -21.638 18.658 -31.570 1.00 27.96 ? 314 ASN   B N   1 
ATOM   4532 C CA  . ASN   B 1 292 ? -21.750 18.144 -32.923 1.00 28.64 ? 314 ASN   B CA  1 
ATOM   4533 C C   . ASN   B 1 292 ? -22.907 18.878 -33.602 1.00 28.37 ? 314 ASN   B C   1 
ATOM   4534 O O   . ASN   B 1 292 ? -23.969 18.300 -33.839 1.00 29.09 ? 314 ASN   B O   1 
ATOM   4535 C CB  . ASN   B 1 292 ? -21.917 16.627 -32.951 1.00 30.11 ? 314 ASN   B CB  1 
ATOM   4536 C CG  . ASN   B 1 292 ? -20.819 15.886 -32.225 1.00 31.00 ? 314 ASN   B CG  1 
ATOM   4537 O OD1 . ASN   B 1 292 ? -19.628 16.147 -32.433 1.00 31.34 ? 314 ASN   B OD1 1 
ATOM   4538 N ND2 . ASN   B 1 292 ? -21.203 14.951 -31.369 1.00 32.13 ? 314 ASN   B ND2 1 
ATOM   4539 N N   . ILE   B 1 293 ? -22.668 20.165 -33.889 1.00 27.96 ? 315 ILE   B N   1 
ATOM   4540 C CA  . ILE   B 1 293 ? -23.633 21.054 -34.511 1.00 26.23 ? 315 ILE   B CA  1 
ATOM   4541 C C   . ILE   B 1 293 ? -22.961 21.667 -35.739 1.00 26.00 ? 315 ILE   B C   1 
ATOM   4542 O O   . ILE   B 1 293 ? -21.827 22.155 -35.654 1.00 26.01 ? 315 ILE   B O   1 
ATOM   4543 C CB  . ILE   B 1 293 ? -24.129 22.130 -33.519 1.00 26.73 ? 315 ILE   B CB  1 
ATOM   4544 C CG1 . ILE   B 1 293 ? -24.983 21.543 -32.409 1.00 27.92 ? 315 ILE   B CG1 1 
ATOM   4545 C CG2 . ILE   B 1 293 ? -24.899 23.237 -34.243 1.00 25.69 ? 315 ILE   B CG2 1 
ATOM   4546 C CD1 . ILE   B 1 293 ? -25.229 22.499 -31.253 1.00 26.73 ? 315 ILE   B CD1 1 
ATOM   4547 N N   . ILE   B 1 294 ? -23.679 21.617 -36.867 1.00 24.86 ? 316 ILE   B N   1 
ATOM   4548 C CA  . ILE   B 1 294 ? -23.299 22.283 -38.105 1.00 24.11 ? 316 ILE   B CA  1 
ATOM   4549 C C   . ILE   B 1 294 ? -24.299 23.387 -38.421 1.00 23.29 ? 316 ILE   B C   1 
ATOM   4550 O O   . ILE   B 1 294 ? -25.501 23.198 -38.266 1.00 23.60 ? 316 ILE   B O   1 
ATOM   4551 C CB  . ILE   B 1 294 ? -23.223 21.283 -39.271 1.00 24.90 ? 316 ILE   B CB  1 
ATOM   4552 C CG1 . ILE   B 1 294 ? -22.043 20.347 -39.097 1.00 26.62 ? 316 ILE   B CG1 1 
ATOM   4553 C CG2 . ILE   B 1 294 ? -23.185 21.992 -40.631 1.00 25.91 ? 316 ILE   B CG2 1 
ATOM   4554 C CD1 . ILE   B 1 294 ? -22.088 19.135 -40.009 1.00 27.32 ? 316 ILE   B CD1 1 
ATOM   4555 N N   . ALA   B 1 295 ? -23.765 24.512 -38.909 1.00 22.66 ? 317 ALA   B N   1 
ATOM   4556 C CA  . ALA   B 1 295 ? -24.554 25.540 -39.557 1.00 22.69 ? 317 ALA   B CA  1 
ATOM   4557 C C   . ALA   B 1 295 ? -24.241 25.520 -41.047 1.00 22.81 ? 317 ALA   B C   1 
ATOM   4558 O O   . ALA   B 1 295 ? -23.077 25.406 -41.431 1.00 23.11 ? 317 ALA   B O   1 
ATOM   4559 C CB  . ALA   B 1 295 ? -24.236 26.886 -38.960 1.00 22.65 ? 317 ALA   B CB  1 
ATOM   4560 N N   . SER   B 1 296 ? -25.281 25.638 -41.873 1.00 23.57 ? 318 SER   B N   1 
ATOM   4561 C CA  . SER   B 1 296 ? -25.121 25.762 -43.314 1.00 24.63 ? 318 SER   B CA  1 
ATOM   4562 C C   . SER   B 1 296 ? -25.900 26.976 -43.808 1.00 24.88 ? 318 SER   B C   1 
ATOM   4563 O O   . SER   B 1 296 ? -26.910 27.335 -43.210 1.00 26.90 ? 318 SER   B O   1 
ATOM   4564 C CB  . SER   B 1 296 ? -25.593 24.513 -44.004 1.00 24.65 ? 318 SER   B CB  1 
ATOM   4565 O OG  . SER   B 1 296 ? -26.961 24.277 -43.687 1.00 26.04 ? 318 SER   B OG  1 
ATOM   4566 N N   . ALA   B 1 297 ? -25.471 27.572 -44.926 1.00 24.57 ? 319 ALA   B N   1 
ATOM   4567 C CA  . ALA   B 1 297 ? -26.168 28.724 -45.483 1.00 23.49 ? 319 ALA   B CA  1 
ATOM   4568 C C   . ALA   B 1 297 ? -26.149 28.676 -47.009 1.00 23.21 ? 319 ALA   B C   1 
ATOM   4569 O O   . ALA   B 1 297 ? -25.236 28.118 -47.610 1.00 23.52 ? 319 ALA   B O   1 
ATOM   4570 C CB  . ALA   B 1 297 ? -25.562 30.011 -44.968 1.00 23.66 ? 319 ALA   B CB  1 
ATOM   4571 N N   . ALA   B 1 298 ? -27.163 29.295 -47.616 1.00 23.33 ? 320 ALA   B N   1 
ATOM   4572 C CA  . ALA   B 1 298 ? -27.396 29.174 -49.049 1.00 24.78 ? 320 ALA   B CA  1 
ATOM   4573 C C   . ALA   B 1 298 ? -27.647 30.521 -49.733 1.00 25.61 ? 320 ALA   B C   1 
ATOM   4574 O O   . ALA   B 1 298 ? -27.896 31.556 -49.098 1.00 25.97 ? 320 ALA   B O   1 
ATOM   4575 C CB  . ALA   B 1 298 ? -28.552 28.231 -49.302 1.00 25.04 ? 320 ALA   B CB  1 
ATOM   4576 N N   . LEU   B 1 299 ? -27.586 30.468 -51.070 1.00 25.97 ? 321 LEU   B N   1 
ATOM   4577 C CA  . LEU   B 1 299 ? -27.644 31.652 -51.913 1.00 25.53 ? 321 LEU   B CA  1 
ATOM   4578 C C   . LEU   B 1 299 ? -29.088 32.096 -52.169 1.00 27.01 ? 321 LEU   B C   1 
ATOM   4579 O O   . LEU   B 1 299 ? -30.005 31.709 -51.451 1.00 25.02 ? 321 LEU   B O   1 
ATOM   4580 C CB  . LEU   B 1 299 ? -26.868 31.318 -53.183 1.00 25.40 ? 321 LEU   B CB  1 
ATOM   4581 C CG  . LEU   B 1 299 ? -25.373 31.057 -52.999 1.00 24.48 ? 321 LEU   B CG  1 
ATOM   4582 C CD1 . LEU   B 1 299 ? -24.759 30.984 -54.388 1.00 25.30 ? 321 LEU   B CD1 1 
ATOM   4583 C CD2 . LEU   B 1 299 ? -24.686 32.142 -52.180 1.00 24.31 ? 321 LEU   B CD2 1 
ATOM   4584 N N   . GLU   B 1 300 ? -29.295 32.916 -53.211 1.00 29.30 ? 322 GLU   B N   1 
ATOM   4585 C CA  . GLU   B 1 300 ? -30.401 33.864 -53.214 1.00 31.04 ? 322 GLU   B CA  1 
ATOM   4586 C C   . GLU   B 1 300 ? -31.760 33.196 -53.436 1.00 31.48 ? 322 GLU   B C   1 
ATOM   4587 O O   . GLU   B 1 300 ? -32.763 33.866 -53.246 1.00 33.01 ? 322 GLU   B O   1 
ATOM   4588 C CB  . GLU   B 1 300 ? -30.219 35.017 -54.205 1.00 34.26 ? 322 GLU   B CB  1 
ATOM   4589 C CG  . GLU   B 1 300 ? -30.091 34.561 -55.652 1.00 35.78 ? 322 GLU   B CG  1 
ATOM   4590 C CD  . GLU   B 1 300 ? -28.674 34.356 -56.176 1.00 40.14 ? 322 GLU   B CD  1 
ATOM   4591 O OE1 . GLU   B 1 300 ? -27.758 33.875 -55.452 1.00 39.37 ? 322 GLU   B OE1 1 
ATOM   4592 O OE2 . GLU   B 1 300 ? -28.510 34.668 -57.381 1.00 44.47 ? 322 GLU   B OE2 1 
ATOM   4593 N N   . ASN   B 1 301 ? -31.827 31.927 -53.868 1.00 32.58 ? 323 ASN   B N   1 
ATOM   4594 C CA  . ASN   B 1 301 ? -33.122 31.255 -54.006 1.00 35.32 ? 323 ASN   B CA  1 
ATOM   4595 C C   . ASN   B 1 301 ? -33.577 30.710 -52.649 1.00 36.25 ? 323 ASN   B C   1 
ATOM   4596 O O   . ASN   B 1 301 ? -34.669 30.157 -52.531 1.00 38.52 ? 323 ASN   B O   1 
ATOM   4597 C CB  . ASN   B 1 301 ? -33.104 30.142 -55.054 1.00 37.69 ? 323 ASN   B CB  1 
ATOM   4598 C CG  . ASN   B 1 301 ? -34.489 29.609 -55.366 1.00 41.38 ? 323 ASN   B CG  1 
ATOM   4599 O OD1 . ASN   B 1 301 ? -35.380 30.373 -55.761 1.00 42.83 ? 323 ASN   B OD1 1 
ATOM   4600 N ND2 . ASN   B 1 301 ? -34.706 28.309 -55.205 1.00 42.74 ? 323 ASN   B ND2 1 
ATOM   4601 N N   . ASP   B 1 302 ? -32.737 30.889 -51.621 1.00 34.21 ? 324 ASP   B N   1 
ATOM   4602 C CA  . ASP   B 1 302 ? -32.928 30.252 -50.329 1.00 31.72 ? 324 ASP   B CA  1 
ATOM   4603 C C   . ASP   B 1 302 ? -32.816 31.323 -49.244 1.00 31.29 ? 324 ASP   B C   1 
ATOM   4604 O O   . ASP   B 1 302 ? -33.808 31.657 -48.588 1.00 30.99 ? 324 ASP   B O   1 
ATOM   4605 C CB  . ASP   B 1 302 ? -31.967 29.078 -50.185 1.00 31.73 ? 324 ASP   B CB  1 
ATOM   4606 C CG  . ASP   B 1 302 ? -32.051 28.322 -48.865 1.00 30.56 ? 324 ASP   B CG  1 
ATOM   4607 O OD1 . ASP   B 1 302 ? -32.225 28.984 -47.831 1.00 31.35 ? 324 ASP   B OD1 1 
ATOM   4608 O OD2 . ASP   B 1 302 ? -31.886 27.083 -48.873 1.00 32.46 ? 324 ASP   B OD2 1 
ATOM   4609 N N   . LYS   B 1 303 ? -31.596 31.851 -49.063 1.00 31.47 ? 325 LYS   B N   1 
ATOM   4610 C CA  . LYS   B 1 303 ? -31.332 32.953 -48.150 1.00 29.71 ? 325 LYS   B CA  1 
ATOM   4611 C C   . LYS   B 1 303 ? -31.445 32.528 -46.680 1.00 28.14 ? 325 LYS   B C   1 
ATOM   4612 O O   . LYS   B 1 303 ? -31.450 33.390 -45.807 1.00 27.42 ? 325 LYS   B O   1 
ATOM   4613 C CB  . LYS   B 1 303 ? -32.286 34.132 -48.398 1.00 30.80 ? 325 LYS   B CB  1 
ATOM   4614 C CG  . LYS   B 1 303 ? -32.359 34.662 -49.820 1.00 32.90 ? 325 LYS   B CG  1 
ATOM   4615 C CD  . LYS   B 1 303 ? -33.096 35.994 -49.939 1.00 35.61 ? 325 LYS   B CD  1 
ATOM   4616 C CE  . LYS   B 1 303 ? -33.270 36.459 -51.358 1.00 39.12 ? 325 LYS   B CE  1 
ATOM   4617 N NZ  . LYS   B 1 303 ? -34.362 35.764 -52.047 1.00 42.88 ? 325 LYS   B NZ  1 
ATOM   4618 N N   . THR   B 1 304 ? -31.539 31.219 -46.395 1.00 28.57 ? 326 THR   B N   1 
ATOM   4619 C CA  . THR   B 1 304 ? -31.664 30.758 -45.020 1.00 29.19 ? 326 THR   B CA  1 
ATOM   4620 C C   . THR   B 1 304 ? -30.352 30.144 -44.548 1.00 28.38 ? 326 THR   B C   1 
ATOM   4621 O O   . THR   B 1 304 ? -29.465 29.792 -45.332 1.00 27.37 ? 326 THR   B O   1 
ATOM   4622 C CB  . THR   B 1 304 ? -32.814 29.770 -44.813 1.00 29.52 ? 326 THR   B CB  1 
ATOM   4623 O OG1 . THR   B 1 304 ? -32.480 28.526 -45.423 1.00 29.79 ? 326 THR   B OG1 1 
ATOM   4624 C CG2 . THR   B 1 304 ? -34.127 30.322 -45.337 1.00 30.62 ? 326 THR   B CG2 1 
ATOM   4625 N N   . ILE   B 1 305 ? -30.286 30.059 -43.221 1.00 26.85 ? 327 ILE   B N   1 
ATOM   4626 C CA  . ILE   B 1 305 ? -29.282 29.323 -42.481 1.00 27.57 ? 327 ILE   B CA  1 
ATOM   4627 C C   . ILE   B 1 305 ? -29.981 28.145 -41.812 1.00 28.52 ? 327 ILE   B C   1 
ATOM   4628 O O   . ILE   B 1 305 ? -31.078 28.308 -41.286 1.00 30.97 ? 327 ILE   B O   1 
ATOM   4629 C CB  . ILE   B 1 305 ? -28.645 30.256 -41.442 1.00 26.13 ? 327 ILE   B CB  1 
ATOM   4630 C CG1 . ILE   B 1 305 ? -28.035 31.473 -42.114 1.00 27.38 ? 327 ILE   B CG1 1 
ATOM   4631 C CG2 . ILE   B 1 305 ? -27.631 29.503 -40.581 1.00 26.39 ? 327 ILE   B CG2 1 
ATOM   4632 C CD1 . ILE   B 1 305 ? -28.041 32.725 -41.269 1.00 27.20 ? 327 ILE   B CD1 1 
ATOM   4633 N N   . LYS   B 1 306 ? -29.347 26.970 -41.835 1.00 27.84 ? 328 LYS   B N   1 
ATOM   4634 C CA  . LYS   B 1 306 ? -29.894 25.812 -41.148 1.00 28.08 ? 328 LYS   B CA  1 
ATOM   4635 C C   . LYS   B 1 306 ? -28.910 25.331 -40.089 1.00 27.88 ? 328 LYS   B C   1 
ATOM   4636 O O   . LYS   B 1 306 ? -27.694 25.354 -40.295 1.00 26.61 ? 328 LYS   B O   1 
ATOM   4637 C CB  . LYS   B 1 306 ? -30.270 24.771 -42.203 1.00 29.35 ? 328 LYS   B CB  1 
ATOM   4638 C CG  . LYS   B 1 306 ? -31.549 25.145 -42.941 1.00 29.91 ? 328 LYS   B CG  1 
ATOM   4639 C CD  . LYS   B 1 306 ? -31.908 24.223 -44.097 1.00 31.35 ? 328 LYS   B CD  1 
ATOM   4640 C CE  . LYS   B 1 306 ? -33.003 24.785 -44.942 1.00 32.38 ? 328 LYS   B CE  1 
ATOM   4641 N NZ  . LYS   B 1 306 ? -34.310 24.719 -44.275 1.00 33.24 ? 328 LYS   B NZ  1 
ATOM   4642 N N   . LEU   B 1 307 ? -29.466 24.931 -38.941 1.00 27.53 ? 329 LEU   B N   1 
ATOM   4643 C CA  . LEU   B 1 307 ? -28.694 24.351 -37.856 1.00 27.44 ? 329 LEU   B CA  1 
ATOM   4644 C C   . LEU   B 1 307 ? -29.021 22.867 -37.753 1.00 27.54 ? 329 LEU   B C   1 
ATOM   4645 O O   . LEU   B 1 307 ? -30.201 22.490 -37.728 1.00 28.94 ? 329 LEU   B O   1 
ATOM   4646 C CB  . LEU   B 1 307 ? -28.995 25.078 -36.553 1.00 26.99 ? 329 LEU   B CB  1 
ATOM   4647 C CG  . LEU   B 1 307 ? -28.435 26.490 -36.414 1.00 29.05 ? 329 LEU   B CG  1 
ATOM   4648 C CD1 . LEU   B 1 307 ? -29.091 27.208 -35.248 1.00 29.06 ? 329 LEU   B CD1 1 
ATOM   4649 C CD2 . LEU   B 1 307 ? -26.917 26.431 -36.224 1.00 30.28 ? 329 LEU   B CD2 1 
ATOM   4650 N N   . TRP   B 1 308 ? -27.959 22.049 -37.685 1.00 27.76 ? 330 TRP   B N   1 
ATOM   4651 C CA  . TRP   B 1 308 ? -28.073 20.595 -37.692 1.00 29.63 ? 330 TRP   B CA  1 
ATOM   4652 C C   . TRP   B 1 308 ? -27.413 20.027 -36.442 1.00 29.49 ? 330 TRP   B C   1 
ATOM   4653 O O   . TRP   B 1 308 ? -26.410 20.571 -36.000 1.00 30.34 ? 330 TRP   B O   1 
ATOM   4654 C CB  . TRP   B 1 308 ? -27.393 20.028 -38.947 1.00 28.79 ? 330 TRP   B CB  1 
ATOM   4655 C CG  . TRP   B 1 308 ? -27.776 20.740 -40.215 1.00 29.51 ? 330 TRP   B CG  1 
ATOM   4656 C CD1 . TRP   B 1 308 ? -27.304 21.938 -40.667 1.00 30.08 ? 330 TRP   B CD1 1 
ATOM   4657 C CD2 . TRP   B 1 308 ? -28.723 20.277 -41.200 1.00 31.44 ? 330 TRP   B CD2 1 
ATOM   4658 N NE1 . TRP   B 1 308 ? -27.889 22.255 -41.866 1.00 30.75 ? 330 TRP   B NE1 1 
ATOM   4659 C CE2 . TRP   B 1 308 ? -28.772 21.262 -42.211 1.00 31.41 ? 330 TRP   B CE2 1 
ATOM   4660 C CE3 . TRP   B 1 308 ? -29.541 19.145 -41.315 1.00 33.81 ? 330 TRP   B CE3 1 
ATOM   4661 C CZ2 . TRP   B 1 308 ? -29.594 21.133 -43.327 1.00 31.60 ? 330 TRP   B CZ2 1 
ATOM   4662 C CZ3 . TRP   B 1 308 ? -30.354 19.022 -42.423 1.00 32.83 ? 330 TRP   B CZ3 1 
ATOM   4663 C CH2 . TRP   B 1 308 ? -30.386 20.007 -43.410 1.00 33.61 ? 330 TRP   B CH2 1 
ATOM   4664 N N   . LYS   B 1 309 ? -27.931 18.904 -35.922 1.00 29.89 ? 331 LYS   B N   1 
ATOM   4665 C CA  . LYS   B 1 309 ? -27.355 18.274 -34.742 1.00 31.62 ? 331 LYS   B CA  1 
ATOM   4666 C C   . LYS   B 1 309 ? -27.179 16.771 -34.964 1.00 32.31 ? 331 LYS   B C   1 
ATOM   4667 O O   . LYS   B 1 309 ? -28.082 16.095 -35.461 1.00 31.29 ? 331 LYS   B O   1 
ATOM   4668 C CB  . LYS   B 1 309 ? -28.226 18.516 -33.506 1.00 33.29 ? 331 LYS   B CB  1 
ATOM   4669 C CG  . LYS   B 1 309 ? -27.772 17.778 -32.246 1.00 35.35 ? 331 LYS   B CG  1 
ATOM   4670 C CD  . LYS   B 1 309 ? -26.490 18.331 -31.631 1.00 36.77 ? 331 LYS   B CD  1 
ATOM   4671 C CE  . LYS   B 1 309 ? -25.834 17.408 -30.645 1.00 38.49 ? 331 LYS   B CE  1 
ATOM   4672 N NZ  . LYS   B 1 309 ? -26.765 16.962 -29.618 1.00 41.24 ? 331 LYS   B NZ  1 
ATOM   4673 N N   . SER   B 1 310 ? -26.015 16.265 -34.542 1.00 32.28 ? 332 SER   B N   1 
ATOM   4674 C CA  . SER   B 1 310 ? -25.665 14.858 -34.666 1.00 34.50 ? 332 SER   B CA  1 
ATOM   4675 C C   . SER   B 1 310 ? -25.307 14.262 -33.306 1.00 36.49 ? 332 SER   B C   1 
ATOM   4676 O O   . SER   B 1 310 ? -24.872 14.960 -32.393 1.00 36.00 ? 332 SER   B O   1 
ATOM   4677 C CB  . SER   B 1 310 ? -24.535 14.674 -35.638 1.00 33.84 ? 332 SER   B CB  1 
ATOM   4678 O OG  . SER   B 1 310 ? -24.062 13.333 -35.636 1.00 34.45 ? 332 SER   B OG  1 
ATOM   4679 N N   . ASP   B 1 311 ? -25.447 12.939 -33.200 1.00 41.20 ? 333 ASP   B N   1 
ATOM   4680 C CA  . ASP   B 1 311 ? -25.105 12.224 -31.979 1.00 43.03 ? 333 ASP   B CA  1 
ATOM   4681 C C   . ASP   B 1 311 ? -23.619 11.857 -31.958 1.00 43.51 ? 333 ASP   B C   1 
ATOM   4682 O O   . ASP   B 1 311 ? -23.117 11.401 -30.931 1.00 45.85 ? 333 ASP   B O   1 
ATOM   4683 C CB  . ASP   B 1 311 ? -26.019 11.023 -31.774 1.00 43.80 ? 333 ASP   B CB  1 
ATOM   4684 C CG  . ASP   B 1 311 ? -27.497 11.358 -31.617 1.00 44.41 ? 333 ASP   B CG  1 
ATOM   4685 O OD1 . ASP   B 1 311 ? -27.806 12.387 -30.975 1.00 48.78 ? 333 ASP   B OD1 1 
ATOM   4686 O OD2 . ASP   B 1 311 ? -28.331 10.584 -32.117 1.00 42.73 ? 333 ASP   B OD2 1 
ATOM   4687 N N   . CYS   B 1 312 ? -22.903 12.039 -33.074 1.00 44.80 ? 334 CYS   B N   1 
ATOM   4688 C CA  . CYS   B 1 312 ? -21.475 11.752 -33.087 1.00 47.83 ? 334 CYS   B CA  1 
ATOM   4689 C C   . CYS   B 1 312 ? -20.772 12.496 -34.233 1.00 47.38 ? 334 CYS   B C   1 
ATOM   4690 O O   . CYS   B 1 312 ? -21.453 13.304 -34.913 1.00 41.89 ? 334 CYS   B O   1 
ATOM   4691 C CB  . CYS   B 1 312 ? -21.204 10.257 -33.220 1.00 52.52 ? 334 CYS   B CB  1 
ATOM   4692 S SG  . CYS   B 1 312 ? -21.569 9.599  -34.870 1.00 54.89 ? 334 CYS   B SG  1 
ATOM   4693 O OXT . CYS   B 1 312 ? -19.561 12.236 -34.402 1.00 50.73 ? 334 CYS   B OXT 1 
HETATM 4694 C C4  . A1A16 C 2 .   ? 4.433   23.643 0.924   1.00 26.47 ? 401 A1A16 A C4  1 
HETATM 4695 C C5  . A1A16 C 2 .   ? 5.871   23.239 0.584   1.00 25.79 ? 401 A1A16 A C5  1 
HETATM 4696 C C7  . A1A16 C 2 .   ? 6.768   24.921 2.205   1.00 24.90 ? 401 A1A16 A C7  1 
HETATM 4697 C C8  . A1A16 C 2 .   ? 7.396   26.238 1.780   1.00 25.52 ? 401 A1A16 A C8  1 
HETATM 4698 C C10 . A1A16 C 2 .   ? 9.178   24.739 0.807   1.00 24.05 ? 401 A1A16 A C10 1 
HETATM 4699 C C13 . A1A16 C 2 .   ? 11.035  25.991 0.332   1.00 24.61 ? 401 A1A16 A C13 1 
HETATM 4700 C C17 . A1A16 C 2 .   ? 3.866   24.359 -1.343  1.00 24.63 ? 401 A1A16 A C17 1 
HETATM 4701 C C20 . A1A16 C 2 .   ? 1.884   22.556 -4.040  1.00 23.02 ? 401 A1A16 A C20 1 
HETATM 4702 C C21 . A1A16 C 2 .   ? 1.128   21.293 -4.232  1.00 26.23 ? 401 A1A16 A C21 1 
HETATM 4703 C C22 . A1A16 C 2 .   ? 1.666   20.024 -4.185  1.00 29.78 ? 401 A1A16 A C22 1 
HETATM 4704 C C24 . A1A16 C 2 .   ? 0.678   17.703 -4.253  1.00 34.34 ? 401 A1A16 A C24 1 
HETATM 4705 C C28 . A1A16 C 2 .   ? -1.350  22.041 -4.603  1.00 29.56 ? 401 A1A16 A C28 1 
HETATM 4706 C C1  . A1A16 C 2 .   ? 2.368   24.514 3.183   1.00 33.10 ? 401 A1A16 A C1  1 
HETATM 4707 C C2  . A1A16 C 2 .   ? 2.384   23.243 2.426   1.00 30.13 ? 401 A1A16 A C2  1 
HETATM 4708 C C3  . A1A16 C 2 .   ? 3.777   22.832 2.038   1.00 29.61 ? 401 A1A16 A C3  1 
HETATM 4709 N N6  . A1A16 C 2 .   ? 6.899   23.893 1.169   1.00 24.86 ? 401 A1A16 A N6  1 
HETATM 4710 C C9  . A1A16 C 2 .   ? 8.281   23.533 0.852   1.00 25.64 ? 401 A1A16 A C9  1 
HETATM 4711 C C11 . A1A16 C 2 .   ? 8.760   25.954 1.234   1.00 24.64 ? 401 A1A16 A C11 1 
HETATM 4712 S S12 . A1A16 C 2 .   ? 9.972   27.135 1.002   1.00 25.96 ? 401 A1A16 A S12 1 
HETATM 4713 C C14 . A1A16 C 2 .   ? 10.495  24.767 0.286   1.00 24.09 ? 401 A1A16 A C14 1 
HETATM 4714 O O15 . A1A16 C 2 .   ? 6.059   22.343 -0.215  1.00 25.28 ? 401 A1A16 A O15 1 
HETATM 4715 N N16 . A1A16 C 2 .   ? 3.681   23.521 -0.310  1.00 25.09 ? 401 A1A16 A N16 1 
HETATM 4716 C C18 . A1A16 C 2 .   ? 3.182   24.015 -2.628  1.00 22.80 ? 401 A1A16 A C18 1 
HETATM 4717 C C19 . A1A16 C 2 .   ? 2.407   22.870 -2.789  1.00 22.90 ? 401 A1A16 A C19 1 
HETATM 4718 N N23 . A1A16 C 2 .   ? 0.641   19.166 -4.356  1.00 32.42 ? 401 A1A16 A N23 1 
HETATM 4719 C C25 . A1A16 C 2 .   ? 1.317   17.049 -5.420  1.00 32.73 ? 401 A1A16 A C25 1 
HETATM 4720 N N26 . A1A16 C 2 .   ? -0.543  19.794 -4.518  1.00 28.46 ? 401 A1A16 A N26 1 
HETATM 4721 C C27 . A1A16 C 2 .   ? -0.249  21.069 -4.443  1.00 27.59 ? 401 A1A16 A C27 1 
HETATM 4722 F F29 . A1A16 C 2 .   ? -0.911  23.254 -4.880  1.00 28.78 ? 401 A1A16 A F29 1 
HETATM 4723 F F30 . A1A16 C 2 .   ? -2.138  22.077 -3.481  1.00 29.93 ? 401 A1A16 A F30 1 
HETATM 4724 F F31 . A1A16 C 2 .   ? -2.086  21.758 -5.688  1.00 32.41 ? 401 A1A16 A F31 1 
HETATM 4725 C C32 . A1A16 C 2 .   ? 2.134   23.397 -5.120  1.00 21.65 ? 401 A1A16 A C32 1 
HETATM 4726 C C33 . A1A16 C 2 .   ? 2.911   24.543 -4.967  1.00 22.13 ? 401 A1A16 A C33 1 
HETATM 4727 C C34 . A1A16 C 2 .   ? 3.276   25.398 -6.156  1.00 21.79 ? 401 A1A16 A C34 1 
HETATM 4728 N N35 . A1A16 C 2 .   ? 4.610   25.077 -6.682  1.00 21.88 ? 401 A1A16 A N35 1 
HETATM 4729 C C36 . A1A16 C 2 .   ? 5.650   25.919 -6.811  1.00 20.16 ? 401 A1A16 A C36 1 
HETATM 4730 N N37 . A1A16 C 2 .   ? 6.696   25.336 -7.353  1.00 21.64 ? 401 A1A16 A N37 1 
HETATM 4731 C C38 . A1A16 C 2 .   ? 6.298   24.043 -7.582  1.00 20.97 ? 401 A1A16 A C38 1 
HETATM 4732 C C39 . A1A16 C 2 .   ? 5.025   23.863 -7.177  1.00 20.39 ? 401 A1A16 A C39 1 
HETATM 4733 C C40 . A1A16 C 2 .   ? 3.427   24.847 -3.717  1.00 22.40 ? 401 A1A16 A C40 1 
HETATM 4734 O O41 . A1A16 C 2 .   ? 4.558   25.371 -1.253  1.00 23.51 ? 401 A1A16 A O41 1 
HETATM 4735 C C1  . EDO   D 3 .   ? 16.974  46.256 -12.340 1.00 39.47 ? 402 EDO   A C1  1 
HETATM 4736 O O1  . EDO   D 3 .   ? 17.442  47.589 -12.278 1.00 39.86 ? 402 EDO   A O1  1 
HETATM 4737 C C2  . EDO   D 3 .   ? 17.427  45.529 -13.543 1.00 37.83 ? 402 EDO   A C2  1 
HETATM 4738 O O2  . EDO   D 3 .   ? 16.901  46.070 -14.732 1.00 39.00 ? 402 EDO   A O2  1 
HETATM 4739 C C1  . EDO   E 3 .   ? 7.274   49.814 -17.287 1.00 43.35 ? 403 EDO   A C1  1 
HETATM 4740 O O1  . EDO   E 3 .   ? 7.920   49.343 -18.443 1.00 39.22 ? 403 EDO   A O1  1 
HETATM 4741 C C2  . EDO   E 3 .   ? 5.979   50.444 -17.610 1.00 45.91 ? 403 EDO   A C2  1 
HETATM 4742 O O2  . EDO   E 3 .   ? 6.089   51.838 -17.770 1.00 50.23 ? 403 EDO   A O2  1 
HETATM 4743 C C4  . A1A16 F 2 .   ? -17.599 33.936 -57.288 1.00 25.73 ? 401 A1A16 B C4  1 
HETATM 4744 C C5  . A1A16 F 2 .   ? -16.173 34.389 -56.969 1.00 24.90 ? 401 A1A16 B C5  1 
HETATM 4745 C C7  . A1A16 F 2 .   ? -15.275 32.725 -58.591 1.00 26.07 ? 401 A1A16 B C7  1 
HETATM 4746 C C8  . A1A16 F 2 .   ? -14.591 31.436 -58.170 1.00 25.49 ? 401 A1A16 B C8  1 
HETATM 4747 C C10 . A1A16 F 2 .   ? -12.845 33.002 -57.214 1.00 23.58 ? 401 A1A16 B C10 1 
HETATM 4748 C C13 . A1A16 F 2 .   ? -10.959 31.796 -56.680 1.00 23.91 ? 401 A1A16 B C13 1 
HETATM 4749 C C17 . A1A16 F 2 .   ? -18.057 33.415 -54.956 1.00 22.32 ? 401 A1A16 B C17 1 
HETATM 4750 C C20 . A1A16 F 2 .   ? -19.942 35.382 -52.305 1.00 22.07 ? 401 A1A16 B C20 1 
HETATM 4751 C C21 . A1A16 F 2 .   ? -20.699 36.652 -52.172 1.00 25.41 ? 401 A1A16 B C21 1 
HETATM 4752 C C22 . A1A16 F 2 .   ? -20.174 37.898 -52.397 1.00 27.97 ? 401 A1A16 B C22 1 
HETATM 4753 C C24 . A1A16 F 2 .   ? -21.131 40.222 -52.508 1.00 31.47 ? 401 A1A16 B C24 1 
HETATM 4754 C C28 . A1A16 F 2 .   ? -23.185 35.962 -51.653 1.00 27.86 ? 401 A1A16 B C28 1 
HETATM 4755 C C1  . A1A16 F 2 .   ? -19.608 32.872 -59.325 1.00 30.66 ? 401 A1A16 B C1  1 
HETATM 4756 C C2  . A1A16 F 2 .   ? -19.615 34.227 -58.788 1.00 29.58 ? 401 A1A16 B C2  1 
HETATM 4757 C C3  . A1A16 F 2 .   ? -18.225 34.690 -58.459 1.00 27.97 ? 401 A1A16 B C3  1 
HETATM 4758 N N6  . A1A16 F 2 .   ? -15.139 33.763 -57.560 1.00 23.98 ? 401 A1A16 B N6  1 
HETATM 4759 C C9  . A1A16 F 2 .   ? -13.766 34.186 -57.290 1.00 23.90 ? 401 A1A16 B C9  1 
HETATM 4760 C C11 . A1A16 F 2 .   ? -13.243 31.762 -57.600 1.00 24.92 ? 401 A1A16 B C11 1 
HETATM 4761 S S12 . A1A16 F 2 .   ? -12.011 30.602 -57.314 1.00 26.72 ? 401 A1A16 B S12 1 
HETATM 4762 C C14 . A1A16 F 2 .   ? -11.525 33.021 -56.684 1.00 22.70 ? 401 A1A16 B C14 1 
HETATM 4763 O O15 . A1A16 F 2 .   ? -16.007 35.340 -56.227 1.00 24.93 ? 401 A1A16 B O15 1 
HETATM 4764 N N16 . A1A16 F 2 .   ? -18.339 34.134 -56.056 1.00 23.44 ? 401 A1A16 B N16 1 
HETATM 4765 C C18 . A1A16 F 2 .   ? -18.679 33.842 -53.665 1.00 21.89 ? 401 A1A16 B C18 1 
HETATM 4766 C C19 . A1A16 F 2 .   ? -19.448 34.998 -53.549 1.00 21.70 ? 401 A1A16 B C19 1 
HETATM 4767 N N23 . A1A16 F 2 .   ? -21.193 38.774 -52.294 1.00 30.06 ? 401 A1A16 B N23 1 
HETATM 4768 C C25 . A1A16 F 2 .   ? -20.732 40.920 -51.248 1.00 31.60 ? 401 A1A16 B C25 1 
HETATM 4769 N N26 . A1A16 F 2 .   ? -22.377 38.189 -52.007 1.00 28.38 ? 401 A1A16 B N26 1 
HETATM 4770 C C27 . A1A16 F 2 .   ? -22.080 36.904 -51.933 1.00 27.02 ? 401 A1A16 B C27 1 
HETATM 4771 F F29 . A1A16 F 2 .   ? -22.764 34.751 -51.251 1.00 26.69 ? 401 A1A16 B F29 1 
HETATM 4772 F F30 . A1A16 F 2 .   ? -23.950 35.796 -52.750 1.00 28.85 ? 401 A1A16 B F30 1 
HETATM 4773 F F31 . A1A16 F 2 .   ? -23.917 36.399 -50.630 1.00 30.04 ? 401 A1A16 B F31 1 
HETATM 4774 C C32 . A1A16 F 2 .   ? -19.664 34.604 -51.181 1.00 21.18 ? 401 A1A16 B C32 1 
HETATM 4775 C C33 . A1A16 F 2 .   ? -18.896 33.451 -51.288 1.00 20.64 ? 401 A1A16 B C33 1 
HETATM 4776 C C34 . A1A16 F 2 .   ? -18.521 32.653 -50.062 1.00 20.35 ? 401 A1A16 B C34 1 
HETATM 4777 N N35 . A1A16 F 2 .   ? -17.186 33.020 -49.559 1.00 20.02 ? 401 A1A16 B N35 1 
HETATM 4778 C C36 . A1A16 F 2 .   ? -16.115 32.213 -49.447 1.00 19.89 ? 401 A1A16 B C36 1 
HETATM 4779 N N37 . A1A16 F 2 .   ? -15.075 32.833 -48.940 1.00 21.95 ? 401 A1A16 B N37 1 
HETATM 4780 C C38 . A1A16 F 2 .   ? -15.505 34.117 -48.715 1.00 21.08 ? 401 A1A16 B C38 1 
HETATM 4781 C C39 . A1A16 F 2 .   ? -16.796 34.253 -49.091 1.00 21.07 ? 401 A1A16 B C39 1 
HETATM 4782 C C40 . A1A16 F 2 .   ? -18.409 33.075 -52.535 1.00 20.67 ? 401 A1A16 B C40 1 
HETATM 4783 O O41 . A1A16 F 2 .   ? -17.316 32.437 -54.997 1.00 21.87 ? 401 A1A16 B O41 1 
HETATM 4784 C C1  . EDO   G 3 .   ? 2.783   41.338 -37.726 1.00 43.16 ? 402 EDO   B C1  1 
HETATM 4785 O O1  . EDO   G 3 .   ? 3.115   42.680 -37.521 1.00 46.37 ? 402 EDO   B O1  1 
HETATM 4786 C C2  . EDO   G 3 .   ? 2.603   41.045 -39.167 1.00 42.09 ? 402 EDO   B C2  1 
HETATM 4787 O O2  . EDO   G 3 .   ? 3.816   40.809 -39.836 1.00 42.09 ? 402 EDO   B O2  1 
HETATM 4788 C C1  . EDO   H 3 .   ? -4.034  12.886 -42.224 1.00 43.64 ? 403 EDO   B C1  1 
HETATM 4789 O O1  . EDO   H 3 .   ? -4.491  12.488 -40.941 1.00 43.06 ? 403 EDO   B O1  1 
HETATM 4790 C C2  . EDO   H 3 .   ? -4.524  12.003 -43.310 1.00 42.59 ? 403 EDO   B C2  1 
HETATM 4791 O O2  . EDO   H 3 .   ? -4.175  10.648 -43.113 1.00 46.04 ? 403 EDO   B O2  1 
HETATM 4792 C C1  . EDO   I 3 .   ? -14.422 8.976  -37.810 1.00 48.94 ? 404 EDO   B C1  1 
HETATM 4793 O O1  . EDO   I 3 .   ? -13.744 9.519  -36.685 1.00 44.91 ? 404 EDO   B O1  1 
HETATM 4794 C C2  . EDO   I 3 .   ? -15.130 7.706  -37.507 1.00 51.11 ? 404 EDO   B C2  1 
HETATM 4795 O O2  . EDO   I 3 .   ? -14.742 7.115  -36.269 1.00 53.58 ? 404 EDO   B O2  1 
HETATM 4796 O O   . HOH   J 4 .   ? 0.757   37.834 -29.853 1.00 36.16 ? 501 HOH   A O   1 
HETATM 4797 O O   . HOH   J 4 .   ? 22.265  14.332 -23.054 1.00 43.04 ? 502 HOH   A O   1 
HETATM 4798 O O   . HOH   J 4 .   ? 2.230   16.552 -0.827  1.00 30.69 ? 503 HOH   A O   1 
HETATM 4799 O O   . HOH   J 4 .   ? -10.307 14.893 -10.956 1.00 49.70 ? 504 HOH   A O   1 
HETATM 4800 O O   . HOH   J 4 .   ? 8.942   25.087 -12.809 1.00 19.32 ? 505 HOH   A O   1 
HETATM 4801 O O   . HOH   J 4 .   ? 6.720   13.222 -29.367 1.00 42.49 ? 506 HOH   A O   1 
HETATM 4802 O O   . HOH   J 4 .   ? 8.242   26.268 -16.882 1.00 21.60 ? 507 HOH   A O   1 
HETATM 4803 O O   . HOH   J 4 .   ? 13.043  20.542 6.094   1.00 35.40 ? 508 HOH   A O   1 
HETATM 4804 O O   . HOH   J 4 .   ? -5.523  25.817 -30.699 1.00 40.54 ? 509 HOH   A O   1 
HETATM 4805 O O   . HOH   J 4 .   ? 12.732  17.618 -26.356 1.00 41.33 ? 510 HOH   A O   1 
HETATM 4806 O O   . HOH   J 4 .   ? -3.359  43.833 -25.194 1.00 37.94 ? 511 HOH   A O   1 
HETATM 4807 O O   . HOH   J 4 .   ? 4.728   16.709 -6.563  1.00 18.30 ? 512 HOH   A O   1 
HETATM 4808 O O   . HOH   J 4 .   ? 8.159   36.162 -24.462 1.00 38.75 ? 513 HOH   A O   1 
HETATM 4809 O O   . HOH   J 4 .   ? 18.324  47.900 -15.832 1.00 51.72 ? 514 HOH   A O   1 
HETATM 4810 O O   . HOH   J 4 .   ? -0.427  32.491 4.729   1.00 51.24 ? 515 HOH   A O   1 
HETATM 4811 O O   . HOH   J 4 .   ? -7.848  44.702 -6.632  1.00 48.15 ? 516 HOH   A O   1 
HETATM 4812 O O   . HOH   J 4 .   ? -8.601  22.179 1.878   1.00 38.11 ? 517 HOH   A O   1 
HETATM 4813 O O   . HOH   J 4 .   ? 26.641  30.650 -22.403 1.00 28.08 ? 518 HOH   A O   1 
HETATM 4814 O O   . HOH   J 4 .   ? 5.163   31.975 -20.265 1.00 31.52 ? 519 HOH   A O   1 
HETATM 4815 O O   . HOH   J 4 .   ? -8.378  12.965 -10.079 1.00 35.04 ? 520 HOH   A O   1 
HETATM 4816 O O   . HOH   J 4 .   ? 3.922   43.194 -19.912 1.00 22.75 ? 521 HOH   A O   1 
HETATM 4817 O O   . HOH   J 4 .   ? 14.848  10.384 0.657   1.00 29.45 ? 522 HOH   A O   1 
HETATM 4818 O O   . HOH   J 4 .   ? 24.169  39.271 -14.396 1.00 38.51 ? 523 HOH   A O   1 
HETATM 4819 O O   . HOH   J 4 .   ? 6.613   23.439 -32.649 1.00 40.06 ? 524 HOH   A O   1 
HETATM 4820 O O   . HOH   J 4 .   ? -0.170  31.499 -30.173 1.00 19.76 ? 525 HOH   A O   1 
HETATM 4821 O O   . HOH   J 4 .   ? -4.235  49.638 -11.178 1.00 50.47 ? 526 HOH   A O   1 
HETATM 4822 O O   . HOH   J 4 .   ? 14.814  34.071 -22.431 1.00 36.12 ? 527 HOH   A O   1 
HETATM 4823 O O   . HOH   J 4 .   ? 6.785   5.287  -18.571 1.00 33.49 ? 528 HOH   A O   1 
HETATM 4824 O O   . HOH   J 4 .   ? -15.143 34.201 -15.091 1.00 35.17 ? 529 HOH   A O   1 
HETATM 4825 O O   . HOH   J 4 .   ? 10.504  19.720 -32.804 1.00 33.58 ? 530 HOH   A O   1 
HETATM 4826 O O   . HOH   J 4 .   ? 22.221  24.495 3.030   1.00 26.44 ? 531 HOH   A O   1 
HETATM 4827 O O   . HOH   J 4 .   ? 19.147  23.308 6.116   1.00 29.10 ? 532 HOH   A O   1 
HETATM 4828 O O   . HOH   J 4 .   ? 22.792  33.887 -17.394 1.00 28.80 ? 533 HOH   A O   1 
HETATM 4829 O O   . HOH   J 4 .   ? 1.250   43.433 -19.171 1.00 26.67 ? 534 HOH   A O   1 
HETATM 4830 O O   . HOH   J 4 .   ? 8.264   31.590 -18.275 1.00 42.06 ? 535 HOH   A O   1 
HETATM 4831 O O   . HOH   J 4 .   ? 3.304   28.002 -12.755 1.00 24.13 ? 536 HOH   A O   1 
HETATM 4832 O O   . HOH   J 4 .   ? 21.684  22.850 -24.664 1.00 25.70 ? 537 HOH   A O   1 
HETATM 4833 O O   . HOH   J 4 .   ? 14.590  7.204  -15.401 1.00 28.25 ? 538 HOH   A O   1 
HETATM 4834 O O   . HOH   J 4 .   ? 22.744  42.759 -2.171  1.00 47.19 ? 539 HOH   A O   1 
HETATM 4835 O O   . HOH   J 4 .   ? 1.825   39.391 -18.617 1.00 21.58 ? 540 HOH   A O   1 
HETATM 4836 O O   . HOH   J 4 .   ? -14.445 30.874 -25.219 1.00 22.67 ? 541 HOH   A O   1 
HETATM 4837 O O   . HOH   J 4 .   ? 5.097   42.302 1.851   1.00 44.24 ? 542 HOH   A O   1 
HETATM 4838 O O   . HOH   J 4 .   ? 10.373  28.129 -28.277 1.00 30.72 ? 543 HOH   A O   1 
HETATM 4839 O O   . HOH   J 4 .   ? 7.395   45.501 -24.036 1.00 44.10 ? 544 HOH   A O   1 
HETATM 4840 O O   . HOH   J 4 .   ? 14.185  17.209 3.131   1.00 23.51 ? 545 HOH   A O   1 
HETATM 4841 O O   . HOH   J 4 .   ? 8.987   26.273 -8.312  1.00 20.14 ? 546 HOH   A O   1 
HETATM 4842 O O   . HOH   J 4 .   ? -10.152 14.442 -6.795  1.00 36.26 ? 547 HOH   A O   1 
HETATM 4843 O O   . HOH   J 4 .   ? -4.973  12.580 -23.073 1.00 34.00 ? 548 HOH   A O   1 
HETATM 4844 O O   . HOH   J 4 .   ? 27.194  19.152 -7.756  1.00 36.11 ? 549 HOH   A O   1 
HETATM 4845 O O   . HOH   J 4 .   ? 31.737  23.409 -17.619 1.00 30.56 ? 550 HOH   A O   1 
HETATM 4846 O O   . HOH   J 4 .   ? 7.175   35.380 -18.237 1.00 32.17 ? 551 HOH   A O   1 
HETATM 4847 O O   . HOH   J 4 .   ? -5.357  28.178 -28.628 1.00 24.12 ? 552 HOH   A O   1 
HETATM 4848 O O   . HOH   J 4 .   ? 17.971  7.306  -11.814 1.00 27.56 ? 553 HOH   A O   1 
HETATM 4849 O O   . HOH   J 4 .   ? 21.153  16.813 1.601   1.00 28.36 ? 554 HOH   A O   1 
HETATM 4850 O O   . HOH   J 4 .   ? 19.860  16.763 5.092   1.00 38.38 ? 555 HOH   A O   1 
HETATM 4851 O O   . HOH   J 4 .   ? 28.354  17.943 -19.867 1.00 47.20 ? 556 HOH   A O   1 
HETATM 4852 O O   . HOH   J 4 .   ? 6.976   32.037 -3.184  1.00 19.99 ? 557 HOH   A O   1 
HETATM 4853 O O   . HOH   J 4 .   ? 12.012  8.068  -8.205  1.00 21.79 ? 558 HOH   A O   1 
HETATM 4854 O O   . HOH   J 4 .   ? 6.246   34.672 -5.418  1.00 31.82 ? 559 HOH   A O   1 
HETATM 4855 O O   . HOH   J 4 .   ? 15.723  30.840 -23.802 1.00 32.30 ? 560 HOH   A O   1 
HETATM 4856 O O   . HOH   J 4 .   ? -15.678 34.061 -19.830 1.00 29.99 ? 561 HOH   A O   1 
HETATM 4857 O O   . HOH   J 4 .   ? 6.094   27.904 -20.165 1.00 29.50 ? 562 HOH   A O   1 
HETATM 4858 O O   . HOH   J 4 .   ? -6.414  32.531 1.701   1.00 40.38 ? 563 HOH   A O   1 
HETATM 4859 O O   . HOH   J 4 .   ? -13.145 26.854 -20.128 1.00 28.50 ? 564 HOH   A O   1 
HETATM 4860 O O   . HOH   J 4 .   ? 5.546   33.309 -17.062 1.00 24.63 ? 565 HOH   A O   1 
HETATM 4861 O O   . HOH   J 4 .   ? -3.164  10.584 -13.053 1.00 20.76 ? 566 HOH   A O   1 
HETATM 4862 O O   . HOH   J 4 .   ? 6.978   26.390 -29.601 1.00 18.83 ? 567 HOH   A O   1 
HETATM 4863 O O   . HOH   J 4 .   ? -13.745 35.889 -10.536 1.00 30.10 ? 568 HOH   A O   1 
HETATM 4864 O O   . HOH   J 4 .   ? 3.842   22.424 -31.389 1.00 40.48 ? 569 HOH   A O   1 
HETATM 4865 O O   . HOH   J 4 .   ? -1.901  6.244  -5.534  1.00 36.48 ? 570 HOH   A O   1 
HETATM 4866 O O   . HOH   J 4 .   ? 17.189  33.313 2.233   1.00 35.45 ? 571 HOH   A O   1 
HETATM 4867 O O   . HOH   J 4 .   ? -3.115  10.808 -20.863 1.00 25.49 ? 572 HOH   A O   1 
HETATM 4868 O O   . HOH   J 4 .   ? 7.224   46.884 -3.375  1.00 28.52 ? 573 HOH   A O   1 
HETATM 4869 O O   . HOH   J 4 .   ? 15.715  28.740 6.138   1.00 42.40 ? 574 HOH   A O   1 
HETATM 4870 O O   . HOH   J 4 .   ? 2.386   33.568 -29.029 1.00 23.90 ? 575 HOH   A O   1 
HETATM 4871 O O   . HOH   J 4 .   ? -1.344  50.956 -7.796  1.00 55.88 ? 576 HOH   A O   1 
HETATM 4872 O O   . HOH   J 4 .   ? 2.872   38.558 -20.955 1.00 20.98 ? 577 HOH   A O   1 
HETATM 4873 O O   . HOH   J 4 .   ? 15.605  44.454 -16.486 1.00 42.15 ? 578 HOH   A O   1 
HETATM 4874 O O   . HOH   J 4 .   ? 5.690   42.929 -27.074 1.00 31.99 ? 579 HOH   A O   1 
HETATM 4875 O O   . HOH   J 4 .   ? 21.216  8.557  -21.063 1.00 49.19 ? 580 HOH   A O   1 
HETATM 4876 O O   . HOH   J 4 .   ? -1.351  41.110 1.690   1.00 48.76 ? 581 HOH   A O   1 
HETATM 4877 O O   . HOH   J 4 .   ? 18.958  49.059 -7.746  1.00 41.96 ? 582 HOH   A O   1 
HETATM 4878 O O   . HOH   J 4 .   ? -11.213 15.011 -19.353 1.00 37.34 ? 583 HOH   A O   1 
HETATM 4879 O O   . HOH   J 4 .   ? 4.912   32.510 -28.979 1.00 23.51 ? 584 HOH   A O   1 
HETATM 4880 O O   . HOH   J 4 .   ? -14.942 39.060 -8.343  1.00 48.46 ? 585 HOH   A O   1 
HETATM 4881 O O   . HOH   J 4 .   ? -1.765  41.806 -25.796 1.00 24.38 ? 586 HOH   A O   1 
HETATM 4882 O O   . HOH   J 4 .   ? 9.491   17.334 -29.473 1.00 28.27 ? 587 HOH   A O   1 
HETATM 4883 O O   . HOH   J 4 .   ? 4.815   30.237 -13.640 1.00 21.33 ? 588 HOH   A O   1 
HETATM 4884 O O   . HOH   J 4 .   ? 5.363   8.982  -2.543  1.00 34.87 ? 589 HOH   A O   1 
HETATM 4885 O O   . HOH   J 4 .   ? -6.522  11.274 -19.544 1.00 32.43 ? 590 HOH   A O   1 
HETATM 4886 O O   . HOH   J 4 .   ? 2.704   9.293  -28.522 1.00 34.72 ? 591 HOH   A O   1 
HETATM 4887 O O   . HOH   J 4 .   ? 4.879   40.504 -27.898 1.00 29.95 ? 592 HOH   A O   1 
HETATM 4888 O O   . HOH   J 4 .   ? -5.136  13.161 -5.421  1.00 23.45 ? 593 HOH   A O   1 
HETATM 4889 O O   . HOH   J 4 .   ? 16.057  51.122 -7.161  1.00 50.36 ? 594 HOH   A O   1 
HETATM 4890 O O   . HOH   J 4 .   ? 11.402  4.481  -15.846 1.00 45.70 ? 595 HOH   A O   1 
HETATM 4891 O O   . HOH   J 4 .   ? 7.147   38.773 -26.696 1.00 39.91 ? 596 HOH   A O   1 
HETATM 4892 O O   . HOH   J 4 .   ? -14.077 21.944 -24.537 1.00 32.29 ? 597 HOH   A O   1 
HETATM 4893 O O   . HOH   J 4 .   ? 7.372   31.315 -13.183 1.00 22.94 ? 598 HOH   A O   1 
HETATM 4894 O O   . HOH   J 4 .   ? 18.041  14.311 -24.819 1.00 27.34 ? 599 HOH   A O   1 
HETATM 4895 O O   . HOH   J 4 .   ? -11.766 21.857 -1.344  1.00 48.72 ? 600 HOH   A O   1 
HETATM 4896 O O   . HOH   J 4 .   ? 0.791   13.036 -1.915  1.00 27.06 ? 601 HOH   A O   1 
HETATM 4897 O O   . HOH   J 4 .   ? 4.171   5.463  -13.196 1.00 53.54 ? 602 HOH   A O   1 
HETATM 4898 O O   . HOH   J 4 .   ? 19.108  13.332 -2.188  1.00 27.85 ? 603 HOH   A O   1 
HETATM 4899 O O   . HOH   J 4 .   ? 8.113   31.660 -26.334 1.00 28.96 ? 604 HOH   A O   1 
HETATM 4900 O O   . HOH   J 4 .   ? 32.408  27.785 -7.225  1.00 31.10 ? 605 HOH   A O   1 
HETATM 4901 O O   . HOH   J 4 .   ? 4.798   18.163 -3.324  1.00 30.26 ? 606 HOH   A O   1 
HETATM 4902 O O   . HOH   J 4 .   ? -7.660  26.110 1.603   1.00 37.40 ? 607 HOH   A O   1 
HETATM 4903 O O   . HOH   J 4 .   ? -9.056  24.181 -26.844 1.00 28.80 ? 608 HOH   A O   1 
HETATM 4904 O O   . HOH   J 4 .   ? 5.586   26.652 4.979   1.00 31.18 ? 609 HOH   A O   1 
HETATM 4905 O O   . HOH   J 4 .   ? 2.746   16.935 -29.167 1.00 22.96 ? 610 HOH   A O   1 
HETATM 4906 O O   . HOH   J 4 .   ? -9.544  37.497 -4.718  1.00 25.66 ? 611 HOH   A O   1 
HETATM 4907 O O   . HOH   J 4 .   ? -13.844 28.798 -22.711 1.00 39.30 ? 612 HOH   A O   1 
HETATM 4908 O O   . HOH   J 4 .   ? -9.763  42.187 -23.379 1.00 34.36 ? 613 HOH   A O   1 
HETATM 4909 O O   . HOH   J 4 .   ? -9.503  23.984 -12.787 1.00 21.89 ? 614 HOH   A O   1 
HETATM 4910 O O   . HOH   J 4 .   ? 21.693  23.023 -21.326 1.00 19.93 ? 615 HOH   A O   1 
HETATM 4911 O O   . HOH   J 4 .   ? 23.809  25.318 -22.725 1.00 42.76 ? 616 HOH   A O   1 
HETATM 4912 O O   . HOH   J 4 .   ? 17.349  33.273 -18.759 1.00 24.69 ? 617 HOH   A O   1 
HETATM 4913 O O   . HOH   J 4 .   ? 17.024  37.806 1.077   1.00 47.24 ? 618 HOH   A O   1 
HETATM 4914 O O   . HOH   J 4 .   ? 11.859  34.809 -16.899 1.00 25.76 ? 619 HOH   A O   1 
HETATM 4915 O O   . HOH   J 4 .   ? 9.523   42.295 -16.612 1.00 23.53 ? 620 HOH   A O   1 
HETATM 4916 O O   . HOH   J 4 .   ? -7.532  36.695 -7.501  1.00 23.46 ? 621 HOH   A O   1 
HETATM 4917 O O   . HOH   J 4 .   ? -13.965 36.740 -22.267 1.00 32.35 ? 622 HOH   A O   1 
HETATM 4918 O O   . HOH   J 4 .   ? 26.976  24.577 -18.790 1.00 25.87 ? 623 HOH   A O   1 
HETATM 4919 O O   . HOH   J 4 .   ? 10.592  4.432  -23.557 1.00 61.89 ? 624 HOH   A O   1 
HETATM 4920 O O   . HOH   J 4 .   ? 9.213   34.993 -16.166 1.00 20.09 ? 625 HOH   A O   1 
HETATM 4921 O O   . HOH   J 4 .   ? -5.479  27.181 1.382   1.00 48.53 ? 626 HOH   A O   1 
HETATM 4922 O O   . HOH   J 4 .   ? 19.156  48.620 -10.310 1.00 44.88 ? 627 HOH   A O   1 
HETATM 4923 O O   . HOH   J 4 .   ? 0.064   42.062 -29.185 1.00 39.52 ? 628 HOH   A O   1 
HETATM 4924 O O   . HOH   J 4 .   ? 16.215  49.596 -5.673  1.00 48.63 ? 629 HOH   A O   1 
HETATM 4925 O O   . HOH   J 4 .   ? -7.647  45.218 -10.424 1.00 37.22 ? 630 HOH   A O   1 
HETATM 4926 O O   . HOH   J 4 .   ? -11.707 41.664 -13.914 1.00 33.88 ? 631 HOH   A O   1 
HETATM 4927 O O   . HOH   J 4 .   ? -12.314 23.299 -10.910 1.00 22.75 ? 632 HOH   A O   1 
HETATM 4928 O O   . HOH   J 4 .   ? 29.281  31.624 -3.883  1.00 46.64 ? 633 HOH   A O   1 
HETATM 4929 O O   . HOH   J 4 .   ? -0.288  7.480  -18.645 1.00 27.05 ? 634 HOH   A O   1 
HETATM 4930 O O   . HOH   J 4 .   ? 12.511  10.964 -10.060 1.00 17.78 ? 635 HOH   A O   1 
HETATM 4931 O O   . HOH   J 4 .   ? 29.789  15.851 -17.302 1.00 52.70 ? 636 HOH   A O   1 
HETATM 4932 O O   . HOH   J 4 .   ? -0.989  13.168 -3.882  1.00 24.42 ? 637 HOH   A O   1 
HETATM 4933 O O   . HOH   J 4 .   ? -0.843  12.472 -14.570 1.00 19.21 ? 638 HOH   A O   1 
HETATM 4934 O O   . HOH   J 4 .   ? -11.066 15.325 -15.074 1.00 36.54 ? 639 HOH   A O   1 
HETATM 4935 O O   . HOH   J 4 .   ? 11.590  28.356 -11.658 1.00 20.83 ? 640 HOH   A O   1 
HETATM 4936 O O   . HOH   J 4 .   ? -13.822 24.931 -21.656 1.00 30.13 ? 641 HOH   A O   1 
HETATM 4937 O O   . HOH   J 4 .   ? 4.319   6.070  -24.971 1.00 50.99 ? 642 HOH   A O   1 
HETATM 4938 O O   . HOH   J 4 .   ? 13.447  37.387 -1.525  1.00 26.64 ? 643 HOH   A O   1 
HETATM 4939 O O   . HOH   J 4 .   ? -5.458  47.121 -8.461  1.00 34.35 ? 644 HOH   A O   1 
HETATM 4940 O O   . HOH   J 4 .   ? -9.255  14.419 -22.437 1.00 25.61 ? 645 HOH   A O   1 
HETATM 4941 O O   . HOH   J 4 .   ? 14.973  28.384 -19.603 1.00 50.83 ? 646 HOH   A O   1 
HETATM 4942 O O   . HOH   J 4 .   ? 26.911  30.994 -18.682 1.00 44.11 ? 647 HOH   A O   1 
HETATM 4943 O O   . HOH   J 4 .   ? 10.362  5.381  -18.923 1.00 33.95 ? 648 HOH   A O   1 
HETATM 4944 O O   . HOH   J 4 .   ? 25.801  12.986 -10.650 1.00 37.96 ? 649 HOH   A O   1 
HETATM 4945 O O   . HOH   J 4 .   ? 24.803  17.897 -17.630 1.00 31.65 ? 650 HOH   A O   1 
HETATM 4946 O O   . HOH   J 4 .   ? 5.699   38.316 -20.606 1.00 23.55 ? 651 HOH   A O   1 
HETATM 4947 O O   . HOH   J 4 .   ? -7.329  29.643 -27.717 1.00 17.86 ? 652 HOH   A O   1 
HETATM 4948 O O   . HOH   J 4 .   ? -7.424  34.703 -22.771 1.00 27.89 ? 653 HOH   A O   1 
HETATM 4949 O O   . HOH   J 4 .   ? 4.411   29.980 -18.639 1.00 20.94 ? 654 HOH   A O   1 
HETATM 4950 O O   . HOH   J 4 .   ? 6.159   20.951 -34.065 1.00 39.30 ? 655 HOH   A O   1 
HETATM 4951 O O   . HOH   J 4 .   ? 11.236  11.381 -24.579 1.00 32.57 ? 656 HOH   A O   1 
HETATM 4952 O O   . HOH   J 4 .   ? -10.660 30.000 -30.836 1.00 39.89 ? 657 HOH   A O   1 
HETATM 4953 O O   . HOH   J 4 .   ? -5.324  41.925 0.836   1.00 38.84 ? 658 HOH   A O   1 
HETATM 4954 O O   . HOH   J 4 .   ? -11.988 18.967 -26.077 1.00 57.64 ? 659 HOH   A O   1 
HETATM 4955 O O   . HOH   J 4 .   ? 23.943  21.848 0.717   1.00 42.31 ? 660 HOH   A O   1 
HETATM 4956 O O   . HOH   J 4 .   ? 0.208   7.260  -21.207 1.00 31.49 ? 661 HOH   A O   1 
HETATM 4957 O O   . HOH   J 4 .   ? 15.609  31.349 -19.075 1.00 26.76 ? 662 HOH   A O   1 
HETATM 4958 O O   . HOH   J 4 .   ? -15.136 37.941 -17.030 1.00 47.29 ? 663 HOH   A O   1 
HETATM 4959 O O   . HOH   J 4 .   ? -13.022 38.596 -10.636 1.00 42.66 ? 664 HOH   A O   1 
HETATM 4960 O O   . HOH   J 4 .   ? 11.567  21.474 -28.081 1.00 19.94 ? 665 HOH   A O   1 
HETATM 4961 O O   . HOH   J 4 .   ? -14.341 26.201 -17.469 1.00 28.58 ? 666 HOH   A O   1 
HETATM 4962 O O   . HOH   J 4 .   ? -15.163 31.573 -18.238 1.00 26.81 ? 667 HOH   A O   1 
HETATM 4963 O O   . HOH   J 4 .   ? 10.421  24.256 -19.424 1.00 18.71 ? 668 HOH   A O   1 
HETATM 4964 O O   . HOH   J 4 .   ? 4.202   52.243 -13.188 1.00 36.47 ? 669 HOH   A O   1 
HETATM 4965 O O   . HOH   J 4 .   ? 15.395  40.068 -19.084 1.00 36.08 ? 670 HOH   A O   1 
HETATM 4966 O O   . HOH   J 4 .   ? 21.529  17.246 -1.151  1.00 22.23 ? 671 HOH   A O   1 
HETATM 4967 O O   . HOH   J 4 .   ? -13.346 30.883 -9.469  1.00 43.34 ? 672 HOH   A O   1 
HETATM 4968 O O   . HOH   J 4 .   ? 23.684  19.295 0.094   1.00 43.28 ? 673 HOH   A O   1 
HETATM 4969 O O   . HOH   J 4 .   ? 18.392  7.083  -14.388 1.00 38.36 ? 674 HOH   A O   1 
HETATM 4970 O O   . HOH   J 4 .   ? 14.174  26.439 -17.773 1.00 20.02 ? 675 HOH   A O   1 
HETATM 4971 O O   . HOH   J 4 .   ? -6.538  19.928 -2.940  1.00 36.45 ? 676 HOH   A O   1 
HETATM 4972 O O   . HOH   J 4 .   ? 6.993   25.683 -19.194 1.00 19.29 ? 677 HOH   A O   1 
HETATM 4973 O O   . HOH   J 4 .   ? 26.503  13.275 -16.802 1.00 49.87 ? 678 HOH   A O   1 
HETATM 4974 O O   . HOH   J 4 .   ? 11.152  42.662 3.653   1.00 41.17 ? 679 HOH   A O   1 
HETATM 4975 O O   . HOH   J 4 .   ? 29.706  22.060 -6.509  1.00 34.99 ? 680 HOH   A O   1 
HETATM 4976 O O   . HOH   J 4 .   ? 9.859   48.428 -15.100 1.00 31.69 ? 681 HOH   A O   1 
HETATM 4977 O O   . HOH   J 4 .   ? 13.787  12.735 1.515   1.00 27.31 ? 682 HOH   A O   1 
HETATM 4978 O O   . HOH   J 4 .   ? 5.917   5.163  -20.816 1.00 41.39 ? 683 HOH   A O   1 
HETATM 4979 O O   . HOH   J 4 .   ? 22.334  32.738 -21.591 1.00 37.96 ? 684 HOH   A O   1 
HETATM 4980 O O   . HOH   J 4 .   ? 19.792  24.718 -24.097 1.00 23.18 ? 685 HOH   A O   1 
HETATM 4981 O O   . HOH   J 4 .   ? 19.662  26.052 6.581   1.00 36.81 ? 686 HOH   A O   1 
HETATM 4982 O O   . HOH   J 4 .   ? 1.929   6.714  -17.064 1.00 27.88 ? 687 HOH   A O   1 
HETATM 4983 O O   . HOH   J 4 .   ? 31.692  31.677 -10.316 1.00 43.36 ? 688 HOH   A O   1 
HETATM 4984 O O   . HOH   J 4 .   ? 26.903  28.100 0.983   1.00 42.28 ? 689 HOH   A O   1 
HETATM 4985 O O   . HOH   J 4 .   ? -0.975  45.818 -0.828  1.00 47.54 ? 690 HOH   A O   1 
HETATM 4986 O O   . HOH   J 4 .   ? 19.079  30.122 -26.477 1.00 41.01 ? 691 HOH   A O   1 
HETATM 4987 O O   . HOH   J 4 .   ? 16.250  36.649 -1.928  1.00 31.13 ? 692 HOH   A O   1 
HETATM 4988 O O   . HOH   J 4 .   ? 4.698   47.909 -2.194  1.00 30.50 ? 693 HOH   A O   1 
HETATM 4989 O O   . HOH   J 4 .   ? -9.442  32.431 1.881   1.00 52.33 ? 694 HOH   A O   1 
HETATM 4990 O O   . HOH   J 4 .   ? -10.940 36.247 -0.942  1.00 47.71 ? 695 HOH   A O   1 
HETATM 4991 O O   . HOH   J 4 .   ? 12.434  6.500  -1.120  1.00 55.95 ? 696 HOH   A O   1 
HETATM 4992 O O   . HOH   J 4 .   ? 1.808   45.336 -25.561 1.00 45.13 ? 697 HOH   A O   1 
HETATM 4993 O O   . HOH   J 4 .   ? 5.521   30.682 -22.594 1.00 28.14 ? 698 HOH   A O   1 
HETATM 4994 O O   . HOH   J 4 .   ? 12.153  47.513 -16.647 1.00 42.97 ? 699 HOH   A O   1 
HETATM 4995 O O   . HOH   J 4 .   ? 6.430   35.558 -20.810 1.00 35.17 ? 700 HOH   A O   1 
HETATM 4996 O O   . HOH   J 4 .   ? 1.959   11.126 -0.442  1.00 37.01 ? 701 HOH   A O   1 
HETATM 4997 O O   . HOH   J 4 .   ? 25.133  13.431 -5.535  1.00 38.52 ? 702 HOH   A O   1 
HETATM 4998 O O   . HOH   J 4 .   ? -5.059  12.761 -25.874 1.00 51.46 ? 703 HOH   A O   1 
HETATM 4999 O O   . HOH   J 4 .   ? -1.985  15.552 -4.084  1.00 36.59 ? 704 HOH   A O   1 
HETATM 5000 O O   . HOH   J 4 .   ? 29.049  32.127 -14.876 1.00 30.46 ? 705 HOH   A O   1 
HETATM 5001 O O   . HOH   J 4 .   ? 2.147   15.200 1.629   1.00 37.16 ? 706 HOH   A O   1 
HETATM 5002 O O   . HOH   J 4 .   ? 29.334  28.516 -3.664  1.00 46.04 ? 707 HOH   A O   1 
HETATM 5003 O O   . HOH   J 4 .   ? -14.208 29.168 -19.646 1.00 38.88 ? 708 HOH   A O   1 
HETATM 5004 O O   . HOH   J 4 .   ? 8.311   28.971 -16.064 1.00 31.81 ? 709 HOH   A O   1 
HETATM 5005 O O   . HOH   J 4 .   ? 4.212   31.862 -31.714 1.00 42.77 ? 710 HOH   A O   1 
HETATM 5006 O O   . HOH   J 4 .   ? -13.588 30.998 -7.164  1.00 46.08 ? 711 HOH   A O   1 
HETATM 5007 O O   . HOH   J 4 .   ? 29.284  25.211 -19.761 1.00 37.77 ? 712 HOH   A O   1 
HETATM 5008 O O   . HOH   J 4 .   ? 22.210  34.585 -20.160 1.00 41.61 ? 713 HOH   A O   1 
HETATM 5009 O O   . HOH   J 4 .   ? -8.762  26.199 -28.488 1.00 46.32 ? 714 HOH   A O   1 
HETATM 5010 O O   . HOH   J 4 .   ? 10.588  25.910 -10.507 1.00 16.60 ? 715 HOH   A O   1 
HETATM 5011 O O   . HOH   J 4 .   ? 24.359  42.020 -15.287 1.00 64.82 ? 716 HOH   A O   1 
HETATM 5012 O O   . HOH   J 4 .   ? 9.530   28.175 -13.447 1.00 30.54 ? 717 HOH   A O   1 
HETATM 5013 O O   . HOH   J 4 .   ? 13.308  8.220  1.630   1.00 39.85 ? 718 HOH   A O   1 
HETATM 5014 O O   . HOH   J 4 .   ? -16.866 30.146 -16.379 1.00 32.23 ? 719 HOH   A O   1 
HETATM 5015 O O   . HOH   J 4 .   ? 5.878   30.448 -16.223 1.00 23.67 ? 720 HOH   A O   1 
HETATM 5016 O O   . HOH   J 4 .   ? 17.068  44.339 -18.785 1.00 45.86 ? 721 HOH   A O   1 
HETATM 5017 O O   . HOH   J 4 .   ? 11.272  18.870 -27.731 1.00 28.97 ? 722 HOH   A O   1 
HETATM 5018 O O   . HOH   J 4 .   ? 8.671   40.515 -25.483 1.00 46.86 ? 723 HOH   A O   1 
HETATM 5019 O O   . HOH   J 4 .   ? -3.097  11.683 -4.707  1.00 22.75 ? 724 HOH   A O   1 
HETATM 5020 O O   . HOH   J 4 .   ? -2.005  7.490  -22.546 1.00 51.95 ? 725 HOH   A O   1 
HETATM 5021 O O   . HOH   J 4 .   ? 7.102   28.853 -30.707 1.00 34.18 ? 726 HOH   A O   1 
HETATM 5022 O O   . HOH   J 4 .   ? 13.928  4.717  -15.388 1.00 46.09 ? 727 HOH   A O   1 
HETATM 5023 O O   . HOH   J 4 .   ? -15.154 24.353 -23.446 1.00 36.35 ? 728 HOH   A O   1 
HETATM 5024 O O   . HOH   J 4 .   ? 25.473  23.561 -21.075 1.00 29.12 ? 729 HOH   A O   1 
HETATM 5025 O O   . HOH   J 4 .   ? 26.016  26.685 3.650   1.00 38.56 ? 730 HOH   A O   1 
HETATM 5026 O O   . HOH   J 4 .   ? 28.618  13.264 -14.318 1.00 51.03 ? 731 HOH   A O   1 
HETATM 5027 O O   . HOH   J 4 .   ? -8.415  37.008 -23.726 1.00 35.29 ? 732 HOH   A O   1 
HETATM 5028 O O   . HOH   J 4 .   ? 7.471   15.801 -30.634 1.00 39.62 ? 733 HOH   A O   1 
HETATM 5029 O O   . HOH   J 4 .   ? 2.820   38.626 -31.410 1.00 44.24 ? 734 HOH   A O   1 
HETATM 5030 O O   . HOH   J 4 .   ? 2.346   41.476 5.076   1.00 52.04 ? 735 HOH   A O   1 
HETATM 5031 O O   . HOH   J 4 .   ? 8.852   34.379 -26.722 1.00 43.50 ? 736 HOH   A O   1 
HETATM 5032 O O   . HOH   J 4 .   ? 25.545  37.467 -15.967 1.00 44.55 ? 737 HOH   A O   1 
HETATM 5033 O O   . HOH   J 4 .   ? -3.011  48.797 -6.812  1.00 49.52 ? 738 HOH   A O   1 
HETATM 5034 O O   . HOH   J 4 .   ? 14.787  41.714 -16.635 1.00 36.06 ? 739 HOH   A O   1 
HETATM 5035 O O   . HOH   J 4 .   ? 7.335   33.938 -29.289 1.00 39.43 ? 740 HOH   A O   1 
HETATM 5036 O O   . HOH   J 4 .   ? 3.645   9.075  -0.804  1.00 40.05 ? 741 HOH   A O   1 
HETATM 5037 O O   . HOH   J 4 .   ? 9.146   27.244 -32.119 1.00 53.51 ? 742 HOH   A O   1 
HETATM 5038 O O   . HOH   J 4 .   ? 7.751   31.356 -23.719 1.00 39.84 ? 743 HOH   A O   1 
HETATM 5039 O O   . HOH   J 4 .   ? -2.064  30.541 3.556   1.00 35.62 ? 744 HOH   A O   1 
HETATM 5040 O O   . HOH   J 4 .   ? -11.728 14.845 -12.970 1.00 38.56 ? 745 HOH   A O   1 
HETATM 5041 O O   . HOH   J 4 .   ? 6.780   3.350  -13.963 1.00 53.85 ? 746 HOH   A O   1 
HETATM 5042 O O   . HOH   J 4 .   ? -5.618  9.363  -12.811 1.00 30.95 ? 747 HOH   A O   1 
HETATM 5043 O O   . HOH   J 4 .   ? 12.930  45.169 -17.573 1.00 33.39 ? 748 HOH   A O   1 
HETATM 5044 O O   . HOH   J 4 .   ? 25.442  34.592 -17.197 1.00 34.95 ? 749 HOH   A O   1 
HETATM 5045 O O   . HOH   J 4 .   ? 8.154   34.317 -22.601 1.00 39.69 ? 750 HOH   A O   1 
HETATM 5046 O O   . HOH   J 4 .   ? 11.588  12.959 -26.811 1.00 33.28 ? 751 HOH   A O   1 
HETATM 5047 O O   . HOH   J 4 .   ? -16.226 30.763 -22.991 1.00 25.70 ? 752 HOH   A O   1 
HETATM 5048 O O   . HOH   J 4 .   ? -10.324 38.742 -2.388  1.00 42.43 ? 753 HOH   A O   1 
HETATM 5049 O O   . HOH   J 4 .   ? 17.595  34.662 -1.220  1.00 50.54 ? 754 HOH   A O   1 
HETATM 5050 O O   . HOH   J 4 .   ? 21.556  14.889 -2.153  1.00 38.64 ? 755 HOH   A O   1 
HETATM 5051 O O   . HOH   J 4 .   ? -6.661  47.313 -5.766  1.00 49.07 ? 756 HOH   A O   1 
HETATM 5052 O O   . HOH   J 4 .   ? 12.456  17.918 5.005   1.00 33.07 ? 757 HOH   A O   1 
HETATM 5053 O O   . HOH   J 4 .   ? 28.020  14.669 -11.535 1.00 57.47 ? 758 HOH   A O   1 
HETATM 5054 O O   . HOH   J 4 .   ? 31.310  23.299 -20.160 1.00 41.66 ? 759 HOH   A O   1 
HETATM 5055 O O   . HOH   J 4 .   ? -10.242 24.968 -30.893 1.00 38.24 ? 760 HOH   A O   1 
HETATM 5056 O O   . HOH   J 4 .   ? -15.207 26.824 -24.163 1.00 42.55 ? 761 HOH   A O   1 
HETATM 5057 O O   . HOH   J 4 .   ? 24.108  21.268 -21.552 1.00 31.80 ? 762 HOH   A O   1 
HETATM 5058 O O   . HOH   J 4 .   ? 10.704  5.525  -8.246  1.00 34.02 ? 763 HOH   A O   1 
HETATM 5059 O O   . HOH   J 4 .   ? 12.864  15.073 -27.692 1.00 34.09 ? 764 HOH   A O   1 
HETATM 5060 O O   . HOH   J 4 .   ? -8.710  18.941 -33.302 1.00 40.60 ? 765 HOH   A O   1 
HETATM 5061 O O   . HOH   J 4 .   ? 11.965  42.783 -17.608 1.00 27.60 ? 766 HOH   A O   1 
HETATM 5062 O O   . HOH   J 4 .   ? 9.109   12.856 -28.933 1.00 34.57 ? 767 HOH   A O   1 
HETATM 5063 O O   . HOH   J 4 .   ? -9.597  21.424 -33.044 1.00 41.43 ? 768 HOH   A O   1 
HETATM 5064 O O   . HOH   K 4 .   ? -26.398 8.828  -40.517 1.00 57.15 ? 501 HOH   B O   1 
HETATM 5065 O O   . HOH   K 4 .   ? -30.043 45.285 -46.953 1.00 40.94 ? 502 HOH   B O   1 
HETATM 5066 O O   . HOH   K 4 .   ? -2.409  40.738 -61.940 1.00 43.49 ? 503 HOH   B O   1 
HETATM 5067 O O   . HOH   K 4 .   ? -12.696 33.417 -43.609 1.00 16.67 ? 504 HOH   B O   1 
HETATM 5068 O O   . HOH   K 4 .   ? -7.809  19.305 -58.359 1.00 56.47 ? 505 HOH   B O   1 
HETATM 5069 O O   . HOH   K 4 .   ? -5.350  28.184 -31.781 1.00 34.13 ? 506 HOH   B O   1 
HETATM 5070 O O   . HOH   K 4 .   ? -19.903 41.222 -55.763 1.00 29.49 ? 507 HOH   B O   1 
HETATM 5071 O O   . HOH   K 4 .   ? -32.181 43.772 -45.983 1.00 45.75 ? 508 HOH   B O   1 
HETATM 5072 O O   . HOH   K 4 .   ? -20.017 38.183 -27.766 1.00 47.76 ? 509 HOH   B O   1 
HETATM 5073 O O   . HOH   K 4 .   ? -17.193 41.435 -50.036 1.00 18.95 ? 510 HOH   B O   1 
HETATM 5074 O O   . HOH   K 4 .   ? -4.944  38.250 -27.066 1.00 42.64 ? 511 HOH   B O   1 
HETATM 5075 O O   . HOH   K 4 .   ? 9.625   41.628 -44.078 1.00 42.58 ? 512 HOH   B O   1 
HETATM 5076 O O   . HOH   K 4 .   ? -17.299 15.737 -35.286 1.00 29.70 ? 513 HOH   B O   1 
HETATM 5077 O O   . HOH   K 4 .   ? -19.481 19.344 -36.748 1.00 24.16 ? 514 HOH   B O   1 
HETATM 5078 O O   . HOH   K 4 .   ? -13.408 32.495 -39.422 1.00 22.63 ? 515 HOH   B O   1 
HETATM 5079 O O   . HOH   K 4 .   ? -5.598  33.434 -64.486 1.00 33.77 ? 516 HOH   B O   1 
HETATM 5080 O O   . HOH   K 4 .   ? -13.602 22.575 -31.627 1.00 39.01 ? 517 HOH   B O   1 
HETATM 5081 O O   . HOH   K 4 .   ? 0.182   33.589 -59.508 1.00 28.90 ? 518 HOH   B O   1 
HETATM 5082 O O   . HOH   K 4 .   ? -28.237 24.951 -57.170 1.00 37.21 ? 519 HOH   B O   1 
HETATM 5083 O O   . HOH   K 4 .   ? -21.244 44.645 -54.947 1.00 24.14 ? 520 HOH   B O   1 
HETATM 5084 O O   . HOH   K 4 .   ? -16.354 15.413 -57.282 1.00 38.84 ? 521 HOH   B O   1 
HETATM 5085 O O   . HOH   K 4 .   ? -18.293 30.534 -43.303 1.00 27.91 ? 522 HOH   B O   1 
HETATM 5086 O O   . HOH   K 4 .   ? -23.941 51.729 -51.564 1.00 36.80 ? 523 HOH   B O   1 
HETATM 5087 O O   . HOH   K 4 .   ? -7.921  40.490 -59.910 1.00 23.37 ? 524 HOH   B O   1 
HETATM 5088 O O   . HOH   K 4 .   ? -21.658 28.091 -25.489 1.00 22.49 ? 525 HOH   B O   1 
HETATM 5089 O O   . HOH   K 4 .   ? -12.774 31.944 -48.058 1.00 19.09 ? 526 HOH   B O   1 
HETATM 5090 O O   . HOH   K 4 .   ? -9.188  37.080 -62.640 1.00 36.01 ? 527 HOH   B O   1 
HETATM 5091 O O   . HOH   K 4 .   ? -29.069 21.263 -47.974 1.00 34.41 ? 528 HOH   B O   1 
HETATM 5092 O O   . HOH   K 4 .   ? -16.312 27.098 -35.567 1.00 35.45 ? 529 HOH   B O   1 
HETATM 5093 O O   . HOH   K 4 .   ? -8.142  41.875 -29.966 1.00 31.48 ? 530 HOH   B O   1 
HETATM 5094 O O   . HOH   K 4 .   ? -20.803 22.052 -25.258 1.00 25.54 ? 531 HOH   B O   1 
HETATM 5095 O O   . HOH   K 4 .   ? -22.120 17.693 -24.874 1.00 55.01 ? 532 HOH   B O   1 
HETATM 5096 O O   . HOH   K 4 .   ? -29.762 13.270 -47.927 1.00 54.32 ? 533 HOH   B O   1 
HETATM 5097 O O   . HOH   K 4 .   ? 0.131   36.027 -35.410 1.00 18.84 ? 534 HOH   B O   1 
HETATM 5098 O O   . HOH   K 4 .   ? -16.740 48.943 -54.421 1.00 30.30 ? 535 HOH   B O   1 
HETATM 5099 O O   . HOH   K 4 .   ? -31.907 43.323 -49.905 1.00 47.03 ? 536 HOH   B O   1 
HETATM 5100 O O   . HOH   K 4 .   ? -6.342  29.233 -62.527 1.00 29.78 ? 537 HOH   B O   1 
HETATM 5101 O O   . HOH   K 4 .   ? -32.861 43.647 -37.428 1.00 43.89 ? 538 HOH   B O   1 
HETATM 5102 O O   . HOH   K 4 .   ? -14.764 25.850 -52.747 1.00 20.42 ? 539 HOH   B O   1 
HETATM 5103 O O   . HOH   K 4 .   ? -5.729  27.697 -37.298 1.00 31.98 ? 540 HOH   B O   1 
HETATM 5104 O O   . HOH   K 4 .   ? -4.018  51.228 -45.671 1.00 33.45 ? 541 HOH   B O   1 
HETATM 5105 O O   . HOH   K 4 .   ? -17.295 39.865 -53.263 1.00 29.29 ? 542 HOH   B O   1 
HETATM 5106 O O   . HOH   K 4 .   ? -28.911 18.526 -29.259 1.00 42.71 ? 543 HOH   B O   1 
HETATM 5107 O O   . HOH   K 4 .   ? -10.020 50.233 -48.995 1.00 22.90 ? 544 HOH   B O   1 
HETATM 5108 O O   . HOH   K 4 .   ? -24.955 47.758 -43.815 1.00 24.17 ? 545 HOH   B O   1 
HETATM 5109 O O   . HOH   K 4 .   ? -16.340 19.021 -27.372 1.00 33.90 ? 546 HOH   B O   1 
HETATM 5110 O O   . HOH   K 4 .   ? 5.715   28.659 -37.612 1.00 42.87 ? 547 HOH   B O   1 
HETATM 5111 O O   . HOH   K 4 .   ? -3.608  44.725 -32.231 1.00 25.94 ? 548 HOH   B O   1 
HETATM 5112 O O   . HOH   K 4 .   ? -19.001 49.893 -28.460 1.00 51.62 ? 549 HOH   B O   1 
HETATM 5113 O O   . HOH   K 4 .   ? -14.495 25.105 -63.075 1.00 42.54 ? 550 HOH   B O   1 
HETATM 5114 O O   . HOH   K 4 .   ? -9.626  28.225 -37.521 1.00 37.47 ? 551 HOH   B O   1 
HETATM 5115 O O   . HOH   K 4 .   ? -15.841 35.458 -24.027 1.00 43.82 ? 552 HOH   B O   1 
HETATM 5116 O O   . HOH   K 4 .   ? -19.055 25.896 -26.550 1.00 25.22 ? 553 HOH   B O   1 
HETATM 5117 O O   . HOH   K 4 .   ? -14.505 33.254 -26.542 1.00 19.32 ? 554 HOH   B O   1 
HETATM 5118 O O   . HOH   K 4 .   ? -15.315 16.422 -28.135 1.00 33.22 ? 555 HOH   B O   1 
HETATM 5119 O O   . HOH   K 4 .   ? 5.525   29.194 -33.067 1.00 41.34 ? 556 HOH   B O   1 
HETATM 5120 O O   . HOH   K 4 .   ? -2.877  34.507 -62.786 1.00 22.01 ? 557 HOH   B O   1 
HETATM 5121 O O   . HOH   K 4 .   ? -15.464 31.021 -35.885 1.00 36.10 ? 558 HOH   B O   1 
HETATM 5122 O O   . HOH   K 4 .   ? 8.234   42.988 -40.315 1.00 47.00 ? 559 HOH   B O   1 
HETATM 5123 O O   . HOH   K 4 .   ? -2.792  44.630 -55.082 1.00 44.44 ? 560 HOH   B O   1 
HETATM 5124 O O   . HOH   K 4 .   ? -16.883 28.436 -42.176 1.00 29.54 ? 561 HOH   B O   1 
HETATM 5125 O O   . HOH   K 4 .   ? -18.648 42.665 -27.663 1.00 29.46 ? 562 HOH   B O   1 
HETATM 5126 O O   . HOH   K 4 .   ? -7.199  51.425 -42.014 1.00 33.98 ? 563 HOH   B O   1 
HETATM 5127 O O   . HOH   K 4 .   ? -33.976 34.869 -45.175 1.00 28.27 ? 564 HOH   B O   1 
HETATM 5128 O O   . HOH   K 4 .   ? -19.824 15.290 -35.841 1.00 32.66 ? 565 HOH   B O   1 
HETATM 5129 O O   . HOH   K 4 .   ? -31.209 20.414 -50.486 1.00 38.38 ? 566 HOH   B O   1 
HETATM 5130 O O   . HOH   K 4 .   ? -36.729 24.005 -40.333 1.00 41.85 ? 567 HOH   B O   1 
HETATM 5131 O O   . HOH   K 4 .   ? -8.961  52.041 -39.074 1.00 50.22 ? 568 HOH   B O   1 
HETATM 5132 O O   . HOH   K 4 .   ? -8.359  53.488 -31.209 1.00 57.14 ? 569 HOH   B O   1 
HETATM 5133 O O   . HOH   K 4 .   ? -35.997 21.369 -49.343 1.00 49.99 ? 570 HOH   B O   1 
HETATM 5134 O O   . HOH   K 4 .   ? -36.108 30.212 -49.002 1.00 40.32 ? 571 HOH   B O   1 
HETATM 5135 O O   . HOH   K 4 .   ? -11.888 42.027 -27.341 1.00 29.96 ? 572 HOH   B O   1 
HETATM 5136 O O   . HOH   K 4 .   ? -22.749 17.143 -29.563 1.00 32.89 ? 573 HOH   B O   1 
HETATM 5137 O O   . HOH   K 4 .   ? -0.919  41.221 -58.504 1.00 30.44 ? 574 HOH   B O   1 
HETATM 5138 O O   . HOH   K 4 .   ? -22.644 23.914 -24.923 1.00 29.13 ? 575 HOH   B O   1 
HETATM 5139 O O   . HOH   K 4 .   ? -13.437 27.783 -29.434 1.00 21.39 ? 576 HOH   B O   1 
HETATM 5140 O O   . HOH   K 4 .   ? 1.688   39.933 -33.385 1.00 36.31 ? 577 HOH   B O   1 
HETATM 5141 O O   . HOH   K 4 .   ? 3.056   44.754 -51.457 1.00 46.65 ? 578 HOH   B O   1 
HETATM 5142 O O   . HOH   K 4 .   ? -28.326 47.207 -37.187 1.00 40.52 ? 579 HOH   B O   1 
HETATM 5143 O O   . HOH   K 4 .   ? -18.485 20.479 -34.405 1.00 22.12 ? 580 HOH   B O   1 
HETATM 5144 O O   . HOH   K 4 .   ? -22.077 51.152 -38.594 1.00 31.67 ? 581 HOH   B O   1 
HETATM 5145 O O   . HOH   K 4 .   ? -27.129 44.694 -51.343 1.00 25.10 ? 582 HOH   B O   1 
HETATM 5146 O O   . HOH   K 4 .   ? -16.354 26.864 -26.737 1.00 26.58 ? 583 HOH   B O   1 
HETATM 5147 O O   . HOH   K 4 .   ? 1.273   24.987 -38.542 1.00 42.61 ? 584 HOH   B O   1 
HETATM 5148 O O   . HOH   K 4 .   ? -3.376  51.610 -42.753 1.00 36.67 ? 585 HOH   B O   1 
HETATM 5149 O O   . HOH   K 4 .   ? -3.651  25.364 -37.548 1.00 24.39 ? 586 HOH   B O   1 
HETATM 5150 O O   . HOH   K 4 .   ? 10.525  33.805 -48.897 1.00 44.36 ? 587 HOH   B O   1 
HETATM 5151 O O   . HOH   K 4 .   ? 5.547   34.320 -37.890 1.00 27.20 ? 588 HOH   B O   1 
HETATM 5152 O O   . HOH   K 4 .   ? -4.549  24.498 -58.413 1.00 36.82 ? 589 HOH   B O   1 
HETATM 5153 O O   . HOH   K 4 .   ? -15.865 20.481 -34.965 1.00 22.58 ? 590 HOH   B O   1 
HETATM 5154 O O   . HOH   K 4 .   ? -14.459 46.221 -27.577 1.00 40.89 ? 591 HOH   B O   1 
HETATM 5155 O O   . HOH   K 4 .   ? -14.184 27.231 -42.840 1.00 24.56 ? 592 HOH   B O   1 
HETATM 5156 O O   . HOH   K 4 .   ? -23.048 44.782 -52.893 1.00 21.96 ? 593 HOH   B O   1 
HETATM 5157 O O   . HOH   K 4 .   ? -21.438 51.621 -35.946 1.00 36.00 ? 594 HOH   B O   1 
HETATM 5158 O O   . HOH   K 4 .   ? -7.473  32.513 -38.655 1.00 17.88 ? 595 HOH   B O   1 
HETATM 5159 O O   . HOH   K 4 .   ? -33.469 40.825 -52.653 1.00 39.93 ? 596 HOH   B O   1 
HETATM 5160 O O   . HOH   K 4 .   ? -14.046 10.984 -51.881 1.00 42.23 ? 597 HOH   B O   1 
HETATM 5161 O O   . HOH   K 4 .   ? -14.561 33.253 -36.994 1.00 20.32 ? 598 HOH   B O   1 
HETATM 5162 O O   . HOH   K 4 .   ? -10.042 30.121 -44.652 1.00 19.57 ? 599 HOH   B O   1 
HETATM 5163 O O   . HOH   K 4 .   ? -31.068 34.376 -43.202 1.00 27.45 ? 600 HOH   B O   1 
HETATM 5164 O O   . HOH   K 4 .   ? -28.725 24.484 -32.583 1.00 34.93 ? 601 HOH   B O   1 
HETATM 5165 O O   . HOH   K 4 .   ? -16.129 25.767 -38.637 1.00 27.09 ? 602 HOH   B O   1 
HETATM 5166 O O   . HOH   K 4 .   ? -9.412  47.492 -47.069 1.00 19.06 ? 603 HOH   B O   1 
HETATM 5167 O O   . HOH   K 4 .   ? -22.677 45.859 -42.261 1.00 25.99 ? 604 HOH   B O   1 
HETATM 5168 O O   . HOH   K 4 .   ? -34.392 16.857 -35.923 1.00 37.26 ? 605 HOH   B O   1 
HETATM 5169 O O   . HOH   K 4 .   ? -20.065 46.657 -56.468 1.00 32.70 ? 606 HOH   B O   1 
HETATM 5170 O O   . HOH   K 4 .   ? -4.542  44.694 -58.370 1.00 53.37 ? 607 HOH   B O   1 
HETATM 5171 O O   . HOH   K 4 .   ? -34.641 31.931 -36.148 1.00 37.94 ? 608 HOH   B O   1 
HETATM 5172 O O   . HOH   K 4 .   ? -26.723 10.850 -46.326 1.00 59.67 ? 609 HOH   B O   1 
HETATM 5173 O O   . HOH   K 4 .   ? -5.380  18.595 -37.293 1.00 35.69 ? 610 HOH   B O   1 
HETATM 5174 O O   . HOH   K 4 .   ? -0.986  24.940 -59.337 1.00 57.63 ? 611 HOH   B O   1 
HETATM 5175 O O   . HOH   K 4 .   ? -15.274 23.399 -50.242 1.00 33.63 ? 612 HOH   B O   1 
HETATM 5176 O O   . HOH   K 4 .   ? -17.988 53.117 -44.049 1.00 51.79 ? 613 HOH   B O   1 
HETATM 5177 O O   . HOH   K 4 .   ? -28.868 12.848 -44.271 1.00 51.29 ? 614 HOH   B O   1 
HETATM 5178 O O   . HOH   K 4 .   ? -9.318  23.939 -39.018 1.00 30.42 ? 615 HOH   B O   1 
HETATM 5179 O O   . HOH   K 4 .   ? -11.740 16.507 -38.698 1.00 28.41 ? 616 HOH   B O   1 
HETATM 5180 O O   . HOH   K 4 .   ? -16.800 31.038 -61.217 1.00 36.08 ? 617 HOH   B O   1 
HETATM 5181 O O   . HOH   K 4 .   ? -28.890 29.551 -28.433 1.00 28.70 ? 618 HOH   B O   1 
HETATM 5182 O O   . HOH   K 4 .   ? -18.919 18.048 -63.395 1.00 35.06 ? 619 HOH   B O   1 
HETATM 5183 O O   . HOH   K 4 .   ? -9.212  50.248 -57.910 1.00 36.56 ? 620 HOH   B O   1 
HETATM 5184 O O   . HOH   K 4 .   ? -30.647 34.772 -29.413 1.00 37.51 ? 621 HOH   B O   1 
HETATM 5185 O O   . HOH   K 4 .   ? -17.346 10.152 -52.983 1.00 38.59 ? 622 HOH   B O   1 
HETATM 5186 O O   . HOH   K 4 .   ? -26.630 32.174 -26.863 1.00 34.96 ? 623 HOH   B O   1 
HETATM 5187 O O   . HOH   K 4 .   ? -8.579  30.726 -30.391 1.00 31.48 ? 624 HOH   B O   1 
HETATM 5188 O O   . HOH   K 4 .   ? -35.903 32.363 -38.491 1.00 38.34 ? 625 HOH   B O   1 
HETATM 5189 O O   . HOH   K 4 .   ? -0.515  40.825 -55.728 1.00 29.40 ? 626 HOH   B O   1 
HETATM 5190 O O   . HOH   K 4 .   ? -1.116  48.059 -31.765 1.00 41.18 ? 627 HOH   B O   1 
HETATM 5191 O O   . HOH   K 4 .   ? -25.020 48.059 -36.092 1.00 28.78 ? 628 HOH   B O   1 
HETATM 5192 O O   . HOH   K 4 .   ? 2.506   33.337 -31.895 1.00 33.11 ? 629 HOH   B O   1 
HETATM 5193 O O   . HOH   K 4 .   ? -12.363 23.680 -39.648 1.00 20.14 ? 630 HOH   B O   1 
HETATM 5194 O O   . HOH   K 4 .   ? -24.071 20.410 -23.825 1.00 28.48 ? 631 HOH   B O   1 
HETATM 5195 O O   . HOH   K 4 .   ? -6.450  30.476 -36.568 1.00 40.52 ? 632 HOH   B O   1 
HETATM 5196 O O   . HOH   K 4 .   ? -23.315 8.146  -47.594 1.00 59.73 ? 633 HOH   B O   1 
HETATM 5197 O O   . HOH   K 4 .   ? -8.338  20.640 -54.348 1.00 29.88 ? 634 HOH   B O   1 
HETATM 5198 O O   . HOH   K 4 .   ? -15.012 53.542 -38.496 1.00 37.47 ? 635 HOH   B O   1 
HETATM 5199 O O   . HOH   K 4 .   ? -30.963 44.343 -34.290 1.00 37.07 ? 636 HOH   B O   1 
HETATM 5200 O O   . HOH   K 4 .   ? -5.715  14.416 -39.153 1.00 35.83 ? 637 HOH   B O   1 
HETATM 5201 O O   . HOH   K 4 .   ? -14.742 39.360 -22.151 1.00 44.19 ? 638 HOH   B O   1 
HETATM 5202 O O   . HOH   K 4 .   ? -9.885  37.825 -28.536 1.00 18.98 ? 639 HOH   B O   1 
HETATM 5203 O O   . HOH   K 4 .   ? -29.640 14.018 -34.144 1.00 50.75 ? 640 HOH   B O   1 
HETATM 5204 O O   . HOH   K 4 .   ? -18.134 8.244  -51.043 1.00 37.81 ? 641 HOH   B O   1 
HETATM 5205 O O   . HOH   K 4 .   ? -33.170 16.469 -40.961 1.00 41.77 ? 642 HOH   B O   1 
HETATM 5206 O O   . HOH   K 4 .   ? -21.612 11.686 -55.000 1.00 48.48 ? 643 HOH   B O   1 
HETATM 5207 O O   . HOH   K 4 .   ? -36.634 26.762 -37.299 1.00 36.43 ? 644 HOH   B O   1 
HETATM 5208 O O   . HOH   K 4 .   ? -24.273 42.459 -52.660 1.00 36.23 ? 645 HOH   B O   1 
HETATM 5209 O O   . HOH   K 4 .   ? -17.205 28.673 -37.289 1.00 24.10 ? 646 HOH   B O   1 
HETATM 5210 O O   . HOH   K 4 .   ? -11.460 10.295 -39.857 1.00 38.09 ? 647 HOH   B O   1 
HETATM 5211 O O   . HOH   K 4 .   ? -35.710 17.327 -33.460 1.00 37.60 ? 648 HOH   B O   1 
HETATM 5212 O O   . HOH   K 4 .   ? 7.860   36.363 -50.139 1.00 39.07 ? 649 HOH   B O   1 
HETATM 5213 O O   . HOH   K 4 .   ? -11.226 34.642 -36.959 1.00 18.95 ? 650 HOH   B O   1 
HETATM 5214 O O   A HOH   K 4 .   ? -17.531 34.085 -23.458 0.50 30.73 ? 651 HOH   B O   1 
HETATM 5215 O O   B HOH   K 4 .   ? -16.843 33.137 -22.450 0.50 24.49 ? 651 HOH   B O   1 
HETATM 5216 O O   . HOH   K 4 .   ? -14.380 23.622 -37.531 1.00 42.71 ? 652 HOH   B O   1 
HETATM 5217 O O   . HOH   K 4 .   ? -5.760  21.269 -54.109 1.00 36.48 ? 653 HOH   B O   1 
HETATM 5218 O O   . HOH   K 4 .   ? -14.208 20.857 -27.998 1.00 47.05 ? 654 HOH   B O   1 
HETATM 5219 O O   . HOH   K 4 .   ? 1.058   48.108 -46.015 1.00 48.54 ? 655 HOH   B O   1 
HETATM 5220 O O   . HOH   K 4 .   ? -19.955 51.951 -40.093 1.00 33.23 ? 656 HOH   B O   1 
HETATM 5221 O O   . HOH   K 4 .   ? -0.144  43.906 -32.124 1.00 44.61 ? 657 HOH   B O   1 
HETATM 5222 O O   . HOH   K 4 .   ? -8.256  45.008 -58.671 1.00 41.65 ? 658 HOH   B O   1 
HETATM 5223 O O   . HOH   K 4 .   ? -11.302 53.542 -38.499 1.00 37.35 ? 659 HOH   B O   1 
HETATM 5224 O O   . HOH   K 4 .   ? -15.979 28.471 -33.162 1.00 28.28 ? 660 HOH   B O   1 
HETATM 5225 O O   . HOH   K 4 .   ? 5.627   39.923 -49.005 1.00 50.45 ? 661 HOH   B O   1 
HETATM 5226 O O   . HOH   K 4 .   ? -8.932  32.903 -35.019 1.00 28.57 ? 662 HOH   B O   1 
HETATM 5227 O O   . HOH   K 4 .   ? -10.273 33.742 -33.480 1.00 36.13 ? 663 HOH   B O   1 
HETATM 5228 O O   . HOH   K 4 .   ? -19.811 40.365 -26.369 1.00 46.79 ? 664 HOH   B O   1 
HETATM 5229 O O   . HOH   K 4 .   ? -9.999  31.257 -37.920 1.00 46.80 ? 665 HOH   B O   1 
HETATM 5230 O O   . HOH   K 4 .   ? -2.205  31.878 -62.996 1.00 32.40 ? 666 HOH   B O   1 
HETATM 5231 O O   . HOH   K 4 .   ? -32.673 21.240 -54.158 1.00 37.26 ? 667 HOH   B O   1 
HETATM 5232 O O   . HOH   K 4 .   ? -30.904 15.263 -44.738 1.00 36.46 ? 668 HOH   B O   1 
HETATM 5233 O O   A HOH   K 4 .   ? -10.669 47.592 -32.445 0.50 24.24 ? 669 HOH   B O   1 
HETATM 5234 O O   B HOH   K 4 .   ? -10.159 46.753 -30.517 0.50 32.53 ? 669 HOH   B O   1 
HETATM 5235 O O   . HOH   K 4 .   ? -20.212 36.584 -56.447 1.00 35.91 ? 670 HOH   B O   1 
HETATM 5236 O O   . HOH   K 4 .   ? -32.662 43.680 -41.174 1.00 50.77 ? 671 HOH   B O   1 
HETATM 5237 O O   . HOH   K 4 .   ? -8.771  40.186 -26.433 1.00 48.97 ? 672 HOH   B O   1 
HETATM 5238 O O   . HOH   K 4 .   ? -13.468 29.573 -39.826 1.00 35.37 ? 673 HOH   B O   1 
HETATM 5239 O O   . HOH   K 4 .   ? -19.798 16.694 -28.217 1.00 49.56 ? 674 HOH   B O   1 
HETATM 5240 O O   . HOH   K 4 .   ? -11.029 32.448 -45.830 1.00 17.82 ? 675 HOH   B O   1 
HETATM 5241 O O   . HOH   K 4 .   ? -2.534  39.345 -63.394 1.00 85.24 ? 676 HOH   B O   1 
HETATM 5242 O O   . HOH   K 4 .   ? -9.092  11.425 -38.631 1.00 44.25 ? 677 HOH   B O   1 
HETATM 5243 O O   . HOH   K 4 .   ? 3.099   36.131 -32.454 1.00 42.20 ? 678 HOH   B O   1 
HETATM 5244 O O   . HOH   K 4 .   ? -35.209 16.205 -30.027 1.00 42.04 ? 679 HOH   B O   1 
HETATM 5245 O O   . HOH   K 4 .   ? -35.224 21.634 -44.738 1.00 46.88 ? 680 HOH   B O   1 
HETATM 5246 O O   . HOH   K 4 .   ? -9.326  52.200 -52.753 1.00 57.60 ? 681 HOH   B O   1 
HETATM 5247 O O   . HOH   K 4 .   ? -12.230 30.430 -42.674 1.00 35.15 ? 682 HOH   B O   1 
HETATM 5248 O O   . HOH   K 4 .   ? -15.831 28.143 -39.757 1.00 30.87 ? 683 HOH   B O   1 
HETATM 5249 O O   . HOH   K 4 .   ? -10.080 40.497 -29.044 1.00 34.27 ? 684 HOH   B O   1 
HETATM 5250 O O   . HOH   K 4 .   ? -25.149 46.237 -52.007 1.00 23.42 ? 685 HOH   B O   1 
HETATM 5251 O O   . HOH   K 4 .   ? -8.576  17.015 -35.286 1.00 49.55 ? 686 HOH   B O   1 
HETATM 5252 O O   . HOH   K 4 .   ? -7.835  26.157 -37.244 1.00 51.17 ? 687 HOH   B O   1 
HETATM 5253 O O   . HOH   K 4 .   ? -19.806 26.266 -23.860 1.00 28.71 ? 688 HOH   B O   1 
HETATM 5254 O O   . HOH   K 4 .   ? -22.559 42.841 -56.277 1.00 43.69 ? 689 HOH   B O   1 
HETATM 5255 O O   . HOH   K 4 .   ? -13.924 43.531 -26.450 1.00 45.27 ? 690 HOH   B O   1 
HETATM 5256 O O   . HOH   K 4 .   ? -29.766 45.670 -50.151 1.00 58.13 ? 691 HOH   B O   1 
HETATM 5257 O O   . HOH   K 4 .   ? -17.520 39.711 -55.730 1.00 40.68 ? 692 HOH   B O   1 
HETATM 5258 O O   . HOH   K 4 .   ? 1.504   44.728 -53.552 1.00 46.06 ? 693 HOH   B O   1 
HETATM 5259 O O   . HOH   K 4 .   ? -33.895 21.788 -30.408 1.00 32.74 ? 694 HOH   B O   1 
HETATM 5260 O O   . HOH   K 4 .   ? -13.420 28.616 -32.184 1.00 37.07 ? 695 HOH   B O   1 
HETATM 5261 O O   . HOH   K 4 .   ? -7.881  30.410 -34.813 1.00 36.64 ? 696 HOH   B O   1 
HETATM 5262 O O   . HOH   K 4 .   ? -27.591 48.659 -44.193 1.00 37.30 ? 697 HOH   B O   1 
HETATM 5263 O O   . HOH   K 4 .   ? -8.126  13.841 -37.912 1.00 36.88 ? 698 HOH   B O   1 
HETATM 5264 O O   . HOH   K 4 .   ? -7.906  43.846 -61.407 1.00 44.86 ? 699 HOH   B O   1 
HETATM 5265 O O   . HOH   K 4 .   ? -6.689  16.901 -39.280 1.00 35.34 ? 700 HOH   B O   1 
HETATM 5266 O O   . HOH   K 4 .   ? -7.516  29.580 -32.459 1.00 35.22 ? 701 HOH   B O   1 
HETATM 5267 O O   . HOH   K 4 .   ? -11.330 52.741 -48.868 1.00 36.89 ? 702 HOH   B O   1 
HETATM 5268 O O   . HOH   K 4 .   ? -19.459 21.755 -22.617 1.00 45.50 ? 703 HOH   B O   1 
HETATM 5269 O O   . HOH   K 4 .   ? -8.431  44.403 -29.361 1.00 43.39 ? 704 HOH   B O   1 
HETATM 5270 O O   . HOH   K 4 .   ? -9.244  16.336 -37.944 1.00 27.72 ? 705 HOH   B O   1 
HETATM 5271 O O   . HOH   K 4 .   ? -12.139 46.535 -28.129 1.00 40.39 ? 706 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . VAL   A 9   ? 0.7254 0.5397 0.9721 -0.0605 -0.0878 0.0962  31  VAL   A N   
2    C CA  . VAL   A 9   ? 0.7485 0.5001 0.9057 -0.0651 -0.0627 0.1010  31  VAL   A CA  
3    C C   . VAL   A 9   ? 0.6638 0.4207 0.7895 -0.0223 -0.1023 0.0452  31  VAL   A C   
4    O O   . VAL   A 9   ? 0.6390 0.3400 0.8151 -0.0460 -0.0775 -0.0025 31  VAL   A O   
5    C CB  . VAL   A 9   ? 0.8126 0.5184 0.9071 -0.0483 -0.0508 0.1183  31  VAL   A CB  
6    C CG1 . VAL   A 9   ? 0.8475 0.5300 0.9114 -0.0648 -0.0479 0.1413  31  VAL   A CG1 
7    C CG2 . VAL   A 9   ? 0.8378 0.5597 0.9575 -0.0184 -0.0435 0.1130  31  VAL   A CG2 
8    N N   . LYS   A 10  ? 0.6301 0.3303 0.6506 0.0210  -0.1105 0.0555  32  LYS   A N   
9    C CA  . LYS   A 10  ? 0.5642 0.3281 0.5373 0.0053  -0.1276 0.0018  32  LYS   A CA  
10   C C   . LYS   A 10  ? 0.5309 0.3191 0.4420 0.0462  -0.1175 0.0053  32  LYS   A C   
11   O O   . LYS   A 10  ? 0.5037 0.3192 0.4796 0.0363  -0.1340 0.0224  32  LYS   A O   
12   C CB  . LYS   A 10  ? 0.6231 0.3663 0.5624 0.0115  -0.1295 -0.0291 32  LYS   A CB  
13   C CG  . LYS   A 10  ? 0.6716 0.3826 0.5744 0.0244  -0.1199 -0.0634 32  LYS   A CG  
14   C CD  . LYS   A 10  ? 0.6857 0.4228 0.6070 0.0276  -0.0979 -0.0622 32  LYS   A CD  
15   C CE  . LYS   A 10  ? 0.6413 0.4284 0.5691 0.0144  -0.1158 -0.0707 32  LYS   A CE  
16   N N   . PRO   A 11  ? 0.4676 0.3132 0.3436 0.0471  -0.1150 -0.0023 33  PRO   A N   
17   C CA  . PRO   A 11  ? 0.4562 0.2941 0.3330 0.0670  -0.0926 -0.0003 33  PRO   A CA  
18   C C   . PRO   A 11  ? 0.4450 0.3292 0.3096 0.0571  -0.0945 -0.0185 33  PRO   A C   
19   O O   . PRO   A 11  ? 0.4369 0.3438 0.3033 0.0850  -0.0752 -0.0383 33  PRO   A O   
20   C CB  . PRO   A 11  ? 0.4592 0.2827 0.3364 0.0674  -0.0975 -0.0012 33  PRO   A CB  
21   C CG  . PRO   A 11  ? 0.4535 0.2897 0.3395 0.0698  -0.0960 0.0008  33  PRO   A CG  
22   C CD  . PRO   A 11  ? 0.4648 0.2992 0.3519 0.0525  -0.1000 -0.0020 33  PRO   A CD  
23   N N   . ASN   A 12  ? 0.4297 0.3640 0.3328 0.0505  -0.0910 -0.0303 34  ASN   A N   
24   C CA  . ASN   A 12  ? 0.4108 0.3521 0.3090 0.0583  -0.0838 -0.0237 34  ASN   A CA  
25   C C   . ASN   A 12  ? 0.3642 0.3349 0.2881 0.0696  -0.0865 -0.0373 34  ASN   A C   
26   O O   . ASN   A 12  ? 0.3694 0.3354 0.3034 0.1055  -0.0974 -0.0323 34  ASN   A O   
27   C CB  . ASN   A 12  ? 0.4319 0.3658 0.3516 0.0667  -0.0910 -0.0289 34  ASN   A CB  
28   C CG  . ASN   A 12  ? 0.4603 0.3922 0.3578 0.0731  -0.0957 -0.0196 34  ASN   A CG  
29   O OD1 . ASN   A 12  ? 0.4702 0.4170 0.3720 0.0836  -0.0997 -0.0456 34  ASN   A OD1 
30   N ND2 . ASN   A 12  ? 0.4736 0.4069 0.4156 0.0929  -0.1034 -0.0370 34  ASN   A ND2 
31   N N   . TYR   A 13  ? 0.3393 0.2959 0.2369 0.0488  -0.0710 -0.0246 35  TYR   A N   
32   C CA  . TYR   A 13  ? 0.3321 0.2988 0.2527 0.0461  -0.0518 -0.0228 35  TYR   A CA  
33   C C   . TYR   A 13  ? 0.3350 0.3028 0.2735 0.0624  -0.0462 -0.0228 35  TYR   A C   
34   O O   . TYR   A 13  ? 0.3112 0.2891 0.2931 0.0574  -0.0399 -0.0395 35  TYR   A O   
35   C CB  . TYR   A 13  ? 0.3316 0.2831 0.2552 0.0385  -0.0516 -0.0292 35  TYR   A CB  
36   C CG  . TYR   A 13  ? 0.3065 0.2887 0.2339 0.0275  -0.0527 -0.0226 35  TYR   A CG  
37   C CD1 . TYR   A 13  ? 0.2928 0.2668 0.2275 0.0430  -0.0446 -0.0096 35  TYR   A CD1 
38   C CD2 . TYR   A 13  ? 0.3112 0.2885 0.2316 0.0250  -0.0379 -0.0194 35  TYR   A CD2 
39   C CE1 . TYR   A 13  ? 0.2958 0.2716 0.1988 0.0354  -0.0414 -0.0055 35  TYR   A CE1 
40   C CE2 . TYR   A 13  ? 0.3172 0.2938 0.2244 0.0226  -0.0320 -0.0017 35  TYR   A CE2 
41   C CZ  . TYR   A 13  ? 0.3108 0.2753 0.2283 0.0263  -0.0379 -0.0025 35  TYR   A CZ  
42   O OH  . TYR   A 13  ? 0.3201 0.2996 0.2634 0.0229  -0.0388 0.0184  35  TYR   A OH  
43   N N   . ALA   A 14  ? 0.3184 0.2912 0.2594 0.0572  -0.0404 -0.0044 36  ALA   A N   
44   C CA  . ALA   A 14  ? 0.3289 0.3183 0.2935 0.0589  -0.0278 -0.0088 36  ALA   A CA  
45   C C   . ALA   A 14  ? 0.3075 0.3027 0.2672 0.0803  -0.0305 0.0071  36  ALA   A C   
46   O O   . ALA   A 14  ? 0.3285 0.3211 0.2264 0.0743  -0.0354 0.0069  36  ALA   A O   
47   C CB  . ALA   A 14  ? 0.3418 0.3281 0.3375 0.0460  -0.0313 0.0018  36  ALA   A CB  
48   N N   . LEU   A 15  ? 0.3192 0.3056 0.2611 0.0893  -0.0332 0.0232  37  LEU   A N   
49   C CA  . LEU   A 15  ? 0.2904 0.3137 0.2463 0.0921  -0.0247 0.0411  37  LEU   A CA  
50   C C   . LEU   A 15  ? 0.2604 0.2864 0.2391 0.0993  -0.0352 0.0599  37  LEU   A C   
51   O O   . LEU   A 15  ? 0.2817 0.3082 0.2638 0.1314  -0.0627 0.0302  37  LEU   A O   
52   C CB  . LEU   A 15  ? 0.2908 0.3460 0.2622 0.0849  -0.0064 0.0364  37  LEU   A CB  
53   C CG  . LEU   A 15  ? 0.2883 0.3487 0.2551 0.0806  0.0068  0.0353  37  LEU   A CG  
54   C CD1 . LEU   A 15  ? 0.2610 0.3495 0.2314 0.0660  0.0132  0.0330  37  LEU   A CD1 
55   C CD2 . LEU   A 15  ? 0.2997 0.3666 0.2601 0.0777  0.0110  0.0297  37  LEU   A CD2 
56   N N   . LYS   A 16  ? 0.2509 0.3044 0.2079 0.0715  -0.0300 0.0615  38  LYS   A N   
57   C CA  . LYS   A 16  ? 0.2470 0.3128 0.1994 0.0533  -0.0343 0.0630  38  LYS   A CA  
58   C C   . LYS   A 16  ? 0.2313 0.3469 0.1929 0.0338  -0.0327 0.0698  38  LYS   A C   
59   O O   . LYS   A 16  ? 0.2282 0.3910 0.2312 0.0252  -0.0581 0.0714  38  LYS   A O   
60   C CB  . LYS   A 16  ? 0.2760 0.3520 0.2038 0.0294  -0.0250 0.0570  38  LYS   A CB  
61   C CG  . LYS   A 16  ? 0.3084 0.3774 0.2312 0.0117  -0.0260 0.0523  38  LYS   A CG  
62   C CD  . LYS   A 16  ? 0.3487 0.3971 0.2557 0.0070  -0.0377 0.0502  38  LYS   A CD  
63   C CE  . LYS   A 16  ? 0.3989 0.4497 0.2877 0.0070  -0.0447 0.0324  38  LYS   A CE  
64   N NZ  . LYS   A 16  ? 0.4484 0.4921 0.3341 0.0038  -0.0410 0.0363  38  LYS   A NZ  
65   N N   . PHE   A 17  ? 0.2419 0.3269 0.1770 0.0269  -0.0280 0.0636  39  PHE   A N   
66   C CA  . PHE   A 17  ? 0.2205 0.3354 0.1799 0.0194  -0.0059 0.0591  39  PHE   A CA  
67   C C   . PHE   A 17  ? 0.2072 0.3364 0.1774 0.0258  -0.0084 0.0589  39  PHE   A C   
68   O O   . PHE   A 17  ? 0.2185 0.3412 0.1881 0.0196  -0.0195 0.0388  39  PHE   A O   
69   C CB  . PHE   A 17  ? 0.2293 0.3241 0.1958 0.0196  -0.0028 0.0519  39  PHE   A CB  
70   C CG  . PHE   A 17  ? 0.2242 0.3183 0.1799 0.0216  0.0108  0.0521  39  PHE   A CG  
71   C CD1 . PHE   A 17  ? 0.2183 0.3334 0.1991 0.0076  0.0268  0.0642  39  PHE   A CD1 
72   C CD2 . PHE   A 17  ? 0.2121 0.3368 0.2062 0.0161  0.0058  0.0521  39  PHE   A CD2 
73   C CE1 . PHE   A 17  ? 0.2272 0.3609 0.2057 0.0151  0.0162  0.0581  39  PHE   A CE1 
74   C CE2 . PHE   A 17  ? 0.2223 0.3583 0.1922 0.0131  0.0116  0.0516  39  PHE   A CE2 
75   C CZ  . PHE   A 17  ? 0.2217 0.3496 0.2146 0.0043  0.0149  0.0574  39  PHE   A CZ  
76   N N   . THR   A 18  ? 0.1872 0.3523 0.1894 0.0381  0.0100  0.0552  40  THR   A N   
77   C CA  . THR   A 18  ? 0.2068 0.3607 0.1954 0.0305  0.0158  0.0655  40  THR   A CA  
78   C C   . THR   A 18  ? 0.2211 0.3750 0.1911 0.0099  0.0042  0.0618  40  THR   A C   
79   O O   . THR   A 18  ? 0.2422 0.4037 0.2151 0.0051  -0.0151 0.0698  40  THR   A O   
80   C CB  . THR   A 18  ? 0.1924 0.3784 0.2191 0.0268  0.0260  0.0634  40  THR   A CB  
81   O OG1 . THR   A 18  ? 0.1906 0.3914 0.2254 0.0278  0.0383  0.0466  40  THR   A OG1 
82   C CG2 . THR   A 18  ? 0.2019 0.3931 0.2364 0.0230  0.0272  0.0712  40  THR   A CG2 
83   N N   . LEU   A 19  ? 0.2227 0.3597 0.1791 0.0110  -0.0010 0.0686  41  LEU   A N   
84   C CA  . LEU   A 19  ? 0.2327 0.3670 0.2014 0.0077  -0.0033 0.0747  41  LEU   A CA  
85   C C   . LEU   A 19  ? 0.2221 0.3577 0.2111 0.0054  -0.0188 0.0788  41  LEU   A C   
86   O O   . LEU   A 19  ? 0.2159 0.3492 0.2279 -0.0012 -0.0312 0.0740  41  LEU   A O   
87   C CB  . LEU   A 19  ? 0.2507 0.3713 0.2199 0.0067  0.0131  0.0718  41  LEU   A CB  
88   C CG  . LEU   A 19  ? 0.2782 0.3933 0.2239 -0.0021 0.0436  0.0681  41  LEU   A CG  
89   C CD1 . LEU   A 19  ? 0.3077 0.3971 0.1977 0.0014  0.0520  0.0649  41  LEU   A CD1 
90   C CD2 . LEU   A 19  ? 0.2642 0.4216 0.2191 -0.0096 0.0372  0.0611  41  LEU   A CD2 
91   N N   . ALA   A 20  ? 0.2051 0.3717 0.2310 0.0066  -0.0125 0.0715  42  ALA   A N   
92   C CA  . ALA   A 20  ? 0.1931 0.3744 0.2112 0.0081  -0.0039 0.0608  42  ALA   A CA  
93   C C   . ALA   A 20  ? 0.2204 0.3861 0.2032 -0.0027 -0.0032 0.0616  42  ALA   A C   
94   O O   . ALA   A 20  ? 0.2027 0.4001 0.1776 -0.0271 0.0070  0.0641  42  ALA   A O   
95   C CB  . ALA   A 20  ? 0.2083 0.3899 0.2525 0.0042  0.0237  0.0477  42  ALA   A CB  
96   N N   . GLY   A 21  ? 0.2244 0.3788 0.1990 0.0063  -0.0080 0.0542  43  GLY   A N   
97   C CA  . GLY   A 21  ? 0.2228 0.3713 0.2275 -0.0074 0.0000  0.0572  43  GLY   A CA  
98   C C   . GLY   A 21  ? 0.1967 0.3659 0.2257 -0.0031 0.0140  0.0642  43  GLY   A C   
99   O O   . GLY   A 21  ? 0.1784 0.4072 0.2777 -0.0238 0.0060  0.0753  43  GLY   A O   
100  N N   . HIS   A 22  ? 0.2094 0.3562 0.2038 -0.0017 0.0138  0.0727  44  HIS   A N   
101  C CA  . HIS   A 22  ? 0.1850 0.3572 0.2153 -0.0002 0.0114  0.0662  44  HIS   A CA  
102  C C   . HIS   A 22  ? 0.1818 0.3616 0.2084 -0.0041 0.0181  0.0701  44  HIS   A C   
103  O O   . HIS   A 22  ? 0.1995 0.3680 0.2198 -0.0096 -0.0150 0.0545  44  HIS   A O   
104  C CB  . HIS   A 22  ? 0.1621 0.3458 0.2088 0.0072  0.0232  0.0551  44  HIS   A CB  
105  C CG  . HIS   A 22  ? 0.1631 0.3272 0.1770 0.0117  0.0195  0.0424  44  HIS   A CG  
106  N ND1 . HIS   A 22  ? 0.1461 0.3350 0.1694 0.0055  0.0377  0.0278  44  HIS   A ND1 
107  C CD2 . HIS   A 22  ? 0.1785 0.3305 0.1933 0.0166  0.0325  0.0302  44  HIS   A CD2 
108  C CE1 . HIS   A 22  ? 0.1821 0.3357 0.1728 0.0068  0.0527  0.0251  44  HIS   A CE1 
109  N NE2 . HIS   A 22  ? 0.1757 0.3278 0.1689 0.0072  0.0438  0.0394  44  HIS   A NE2 
110  N N   . THR   A 23  ? 0.1730 0.3810 0.2111 -0.0056 0.0347  0.0761  45  THR   A N   
111  C CA  . THR   A 23  ? 0.1818 0.3849 0.2088 -0.0075 0.0368  0.0873  45  THR   A CA  
112  C C   . THR   A 23  ? 0.1812 0.3875 0.1735 -0.0091 0.0621  0.0905  45  THR   A C   
113  O O   . THR   A 23  ? 0.1803 0.3692 0.1807 -0.0217 0.0673  0.0923  45  THR   A O   
114  C CB  . THR   A 23  ? 0.1972 0.4048 0.2444 -0.0200 0.0433  0.0860  45  THR   A CB  
115  O OG1 . THR   A 23  ? 0.1794 0.3930 0.2531 -0.0102 0.0213  0.1047  45  THR   A OG1 
116  C CG2 . THR   A 23  ? 0.2274 0.4344 0.2824 -0.0186 0.0326  0.0902  45  THR   A CG2 
117  N N   . LYS   A 24  ? 0.1899 0.3816 0.1959 -0.0136 0.0462  0.0821  46  LYS   A N   
118  C CA  . LYS   A 24  ? 0.1742 0.3844 0.1927 0.0089  0.0478  0.0751  46  LYS   A CA  
119  C C   . LYS   A 24  ? 0.1759 0.3781 0.2033 0.0118  0.0451  0.0693  46  LYS   A C   
120  O O   . LYS   A 24  ? 0.1808 0.4002 0.2271 0.0080  0.0761  0.0894  46  LYS   A O   
121  C CB  . LYS   A 24  ? 0.2093 0.3870 0.2021 0.0014  0.0451  0.0865  46  LYS   A CB  
122  C CG  . LYS   A 24  ? 0.2329 0.3863 0.2067 0.0043  0.0373  0.0866  46  LYS   A CG  
123  C CD  . LYS   A 24  ? 0.2245 0.3896 0.1920 0.0058  0.0465  0.0904  46  LYS   A CD  
124  C CE  . LYS   A 24  ? 0.2383 0.3863 0.1946 0.0002  0.0428  0.1036  46  LYS   A CE  
125  N NZ  . LYS   A 24  ? 0.2256 0.3875 0.1766 -0.0096 0.0506  0.1089  46  LYS   A NZ  
126  N N   . ALA   A 25  ? 0.1910 0.3727 0.2144 0.0256  0.0489  0.0679  47  ALA   A N   
127  C CA  . ALA   A 25  ? 0.1778 0.3587 0.2102 0.0259  0.0435  0.0630  47  ALA   A CA  
128  C C   . ALA   A 25  ? 0.1746 0.3439 0.2068 0.0336  0.0396  0.0655  47  ALA   A C   
129  O O   . ALA   A 25  ? 0.1687 0.3325 0.2118 0.0438  0.0401  0.0645  47  ALA   A O   
130  C CB  . ALA   A 25  ? 0.1941 0.3686 0.2101 0.0418  0.0477  0.0643  47  ALA   A CB  
131  N N   . VAL   A 26  ? 0.1781 0.3429 0.2306 0.0144  0.0463  0.0619  48  VAL   A N   
132  C CA  . VAL   A 26  ? 0.1685 0.3481 0.2216 0.0158  0.0336  0.0578  48  VAL   A CA  
133  C C   . VAL   A 26  ? 0.1726 0.3456 0.2195 0.0148  0.0317  0.0320  48  VAL   A C   
134  O O   . VAL   A 26  ? 0.1652 0.3632 0.2470 0.0389  0.0416  -0.0135 48  VAL   A O   
135  C CB  . VAL   A 26  ? 0.1870 0.3348 0.2266 0.0077  0.0349  0.0739  48  VAL   A CB  
136  C CG1 . VAL   A 26  ? 0.1809 0.3264 0.2325 0.0201  0.0340  0.0622  48  VAL   A CG1 
137  C CG2 . VAL   A 26  ? 0.2069 0.3481 0.2281 -0.0019 0.0196  0.0952  48  VAL   A CG2 
138  N N   . SER   A 27  ? 0.1792 0.3137 0.1776 0.0181  0.0277  0.0393  49  SER   A N   
139  C CA  . SER   A 27  ? 0.1832 0.3129 0.1810 0.0132  0.0191  0.0375  49  SER   A CA  
140  C C   . SER   A 27  ? 0.2046 0.2898 0.1707 0.0093  0.0045  0.0379  49  SER   A C   
141  O O   . SER   A 27  ? 0.2089 0.3173 0.1447 -0.0019 0.0197  0.0241  49  SER   A O   
142  C CB  . SER   A 27  ? 0.1802 0.3131 0.1761 0.0159  0.0146  0.0602  49  SER   A CB  
143  O OG  . SER   A 27  ? 0.1640 0.3107 0.1947 0.0079  0.0196  0.0593  49  SER   A OG  
144  N N   . SER   A 28  ? 0.1922 0.2821 0.1641 0.0112  0.0138  0.0238  50  SER   A N   
145  C CA  . SER   A 28  ? 0.2096 0.2686 0.1876 0.0051  -0.0005 0.0341  50  SER   A CA  
146  C C   . SER   A 28  ? 0.2073 0.2584 0.1731 -0.0155 0.0064  0.0301  50  SER   A C   
147  O O   . SER   A 28  ? 0.2320 0.2755 0.1826 -0.0368 -0.0159 0.0335  50  SER   A O   
148  C CB  . SER   A 28  ? 0.2001 0.2908 0.2034 0.0092  0.0093  0.0420  50  SER   A CB  
149  O OG  . SER   A 28  ? 0.2446 0.3109 0.2169 0.0086  0.0047  0.0494  50  SER   A OG  
150  N N   . VAL   A 29  ? 0.1892 0.2420 0.1757 0.0003  0.0040  0.0285  51  VAL   A N   
151  C CA  . VAL   A 29  ? 0.1585 0.2450 0.1696 -0.0123 0.0015  0.0218  51  VAL   A CA  
152  C C   . VAL   A 29  ? 0.1518 0.2453 0.1702 -0.0100 -0.0003 0.0244  51  VAL   A C   
153  O O   . VAL   A 29  ? 0.1398 0.2526 0.1768 -0.0117 0.0020  0.0257  51  VAL   A O   
154  C CB  . VAL   A 29  ? 0.1637 0.2617 0.1841 -0.0086 0.0012  0.0301  51  VAL   A CB  
155  C CG1 . VAL   A 29  ? 0.1622 0.2722 0.2134 -0.0142 0.0105  0.0205  51  VAL   A CG1 
156  C CG2 . VAL   A 29  ? 0.1668 0.2678 0.1893 0.0060  -0.0030 0.0268  51  VAL   A CG2 
157  N N   . LYS   A 30  ? 0.1453 0.2544 0.1831 -0.0117 0.0121  0.0248  52  LYS   A N   
158  C CA  . LYS   A 30  ? 0.1554 0.2586 0.1661 -0.0107 0.0127  0.0254  52  LYS   A CA  
159  C C   . LYS   A 30  ? 0.1484 0.2545 0.1749 -0.0129 0.0068  0.0320  52  LYS   A C   
160  O O   . LYS   A 30  ? 0.1511 0.2401 0.1732 -0.0308 0.0241  0.0323  52  LYS   A O   
161  C CB  . LYS   A 30  ? 0.1531 0.2784 0.1817 -0.0049 0.0041  0.0231  52  LYS   A CB  
162  C CG  . LYS   A 30  ? 0.1750 0.2870 0.1973 -0.0081 -0.0069 0.0231  52  LYS   A CG  
163  C CD  . LYS   A 30  ? 0.1794 0.2836 0.2060 -0.0055 -0.0182 0.0220  52  LYS   A CD  
164  C CE  . LYS   A 30  ? 0.1903 0.2854 0.2062 -0.0033 -0.0299 0.0153  52  LYS   A CE  
165  N NZ  . LYS   A 30  ? 0.1933 0.2838 0.2061 -0.0019 -0.0484 0.0293  52  LYS   A NZ  
166  N N   . PHE   A 31  ? 0.1620 0.2531 0.1803 -0.0156 0.0112  0.0362  53  PHE   A N   
167  C CA  . PHE   A 31  ? 0.1726 0.2587 0.1693 -0.0089 0.0109  0.0325  53  PHE   A CA  
168  C C   . PHE   A 31  ? 0.1661 0.2462 0.1557 -0.0087 0.0117  0.0386  53  PHE   A C   
169  O O   . PHE   A 31  ? 0.1699 0.2636 0.1493 -0.0069 0.0158  0.0447  53  PHE   A O   
170  C CB  . PHE   A 31  ? 0.1795 0.2543 0.1587 -0.0070 0.0260  0.0418  53  PHE   A CB  
171  C CG  . PHE   A 31  ? 0.2030 0.2686 0.1679 -0.0026 0.0298  0.0398  53  PHE   A CG  
172  C CD1 . PHE   A 31  ? 0.2074 0.2679 0.1575 -0.0017 0.0216  0.0396  53  PHE   A CD1 
173  C CD2 . PHE   A 31  ? 0.2247 0.2667 0.1760 0.0086  0.0336  0.0340  53  PHE   A CD2 
174  C CE1 . PHE   A 31  ? 0.2088 0.2790 0.1717 -0.0034 0.0230  0.0346  53  PHE   A CE1 
175  C CE2 . PHE   A 31  ? 0.2081 0.2833 0.1827 0.0000  0.0388  0.0328  53  PHE   A CE2 
176  C CZ  . PHE   A 31  ? 0.2249 0.2793 0.1854 0.0068  0.0227  0.0328  53  PHE   A CZ  
177  N N   . SER   A 32  ? 0.1749 0.2472 0.1585 -0.0004 0.0132  0.0423  54  SER   A N   
178  C CA  . SER   A 32  ? 0.1693 0.2325 0.1614 -0.0035 0.0157  0.0369  54  SER   A CA  
179  C C   . SER   A 32  ? 0.1790 0.2352 0.1695 -0.0084 0.0056  0.0437  54  SER   A C   
180  O O   . SER   A 32  ? 0.1929 0.2183 0.1869 -0.0104 0.0024  0.0284  54  SER   A O   
181  C CB  . SER   A 32  ? 0.1687 0.2297 0.1674 -0.0106 0.0180  0.0318  54  SER   A CB  
182  O OG  . SER   A 32  ? 0.1523 0.2341 0.1775 -0.0107 0.0183  0.0235  54  SER   A OG  
183  N N   . PRO   A 33  ? 0.1903 0.2524 0.1656 -0.0168 0.0243  0.0694  55  PRO   A N   
184  C CA  . PRO   A 33  ? 0.1925 0.2518 0.1752 -0.0227 0.0180  0.0755  55  PRO   A CA  
185  C C   . PRO   A 33  ? 0.1835 0.2470 0.1783 -0.0184 0.0137  0.0724  55  PRO   A C   
186  O O   . PRO   A 33  ? 0.2048 0.2586 0.2114 -0.0175 0.0025  0.0770  55  PRO   A O   
187  C CB  . PRO   A 33  ? 0.1917 0.2649 0.1688 -0.0216 0.0268  0.0768  55  PRO   A CB  
188  C CG  . PRO   A 33  ? 0.2037 0.2695 0.1821 -0.0207 0.0145  0.0790  55  PRO   A CG  
189  C CD  . PRO   A 33  ? 0.1988 0.2383 0.1611 -0.0232 0.0352  0.0797  55  PRO   A CD  
190  N N   . ASN   A 34  ? 0.2019 0.2335 0.1835 -0.0194 0.0152  0.0599  56  ASN   A N   
191  C CA  . ASN   A 34  ? 0.2084 0.2376 0.1826 -0.0182 0.0101  0.0577  56  ASN   A CA  
192  C C   . ASN   A 34  ? 0.2124 0.2400 0.1829 -0.0185 0.0055  0.0622  56  ASN   A C   
193  O O   . ASN   A 34  ? 0.2158 0.2540 0.1886 -0.0115 -0.0084 0.0600  56  ASN   A O   
194  C CB  . ASN   A 34  ? 0.2138 0.2457 0.1930 -0.0150 0.0093  0.0505  56  ASN   A CB  
195  C CG  . ASN   A 34  ? 0.2238 0.2469 0.1786 -0.0195 0.0246  0.0347  56  ASN   A CG  
196  O OD1 . ASN   A 34  ? 0.2098 0.2554 0.1659 -0.0245 0.0301  0.0411  56  ASN   A OD1 
197  N ND2 . ASN   A 34  ? 0.2351 0.2455 0.1876 -0.0175 0.0453  0.0136  56  ASN   A ND2 
198  N N   . GLY   A 35  ? 0.2037 0.2319 0.1660 -0.0138 -0.0037 0.0697  57  GLY   A N   
199  C CA  . GLY   A 35  ? 0.2089 0.2295 0.1724 -0.0151 0.0022  0.0550  57  GLY   A CA  
200  C C   . GLY   A 35  ? 0.2025 0.2199 0.1637 -0.0168 0.0091  0.0590  57  GLY   A C   
201  O O   . GLY   A 35  ? 0.2201 0.2350 0.1747 -0.0097 0.0231  0.0555  57  GLY   A O   
202  N N   . GLU   A 36  ? 0.1961 0.2232 0.1696 -0.0092 0.0097  0.0615  58  GLU   A N   
203  C CA  . GLU   A 36  ? 0.2023 0.2206 0.1836 -0.0212 0.0031  0.0536  58  GLU   A CA  
204  C C   . GLU   A 36  ? 0.1919 0.2285 0.1941 -0.0210 0.0058  0.0433  58  GLU   A C   
205  O O   . GLU   A 36  ? 0.1802 0.2193 0.2191 -0.0110 0.0001  0.0399  58  GLU   A O   
206  C CB  . GLU   A 36  ? 0.2067 0.2351 0.2179 -0.0215 0.0013  0.0485  58  GLU   A CB  
207  C CG  . GLU   A 36  ? 0.2260 0.2630 0.2145 -0.0170 -0.0186 0.0468  58  GLU   A CG  
208  C CD  . GLU   A 36  ? 0.2349 0.3071 0.2170 -0.0175 -0.0114 0.0327  58  GLU   A CD  
209  O OE1 . GLU   A 36  ? 0.2294 0.3604 0.2381 -0.0215 -0.0056 0.0149  58  GLU   A OE1 
210  O OE2 . GLU   A 36  ? 0.2640 0.3233 0.2300 -0.0511 -0.0108 0.0301  58  GLU   A OE2 
211  N N   . TRP   A 37  ? 0.1864 0.2262 0.1776 -0.0290 0.0069  0.0500  59  TRP   A N   
212  C CA  . TRP   A 37  ? 0.2019 0.2390 0.1756 -0.0397 0.0146  0.0508  59  TRP   A CA  
213  C C   . TRP   A 37  ? 0.1849 0.2397 0.1745 -0.0306 0.0041  0.0501  59  TRP   A C   
214  O O   . TRP   A 37  ? 0.1731 0.2577 0.1604 -0.0318 0.0294  0.0420  59  TRP   A O   
215  C CB  . TRP   A 37  ? 0.2279 0.2378 0.1992 -0.0399 0.0138  0.0553  59  TRP   A CB  
216  C CG  . TRP   A 37  ? 0.2873 0.2433 0.2127 -0.0448 -0.0053 0.0641  59  TRP   A CG  
217  C CD1 . TRP   A 37  ? 0.3120 0.2464 0.2085 -0.0317 -0.0146 0.0568  59  TRP   A CD1 
218  C CD2 . TRP   A 37  ? 0.3216 0.2591 0.2746 -0.0491 -0.0047 0.0592  59  TRP   A CD2 
219  N NE1 . TRP   A 37  ? 0.3271 0.3110 0.2860 -0.0458 -0.0171 0.0307  59  TRP   A NE1 
220  C CE2 . TRP   A 37  ? 0.3410 0.2939 0.2837 -0.0526 -0.0006 0.0454  59  TRP   A CE2 
221  C CE3 . TRP   A 37  ? 0.3550 0.2960 0.2997 -0.0568 0.0163  0.0527  59  TRP   A CE3 
222  C CZ2 . TRP   A 37  ? 0.3666 0.3405 0.3467 -0.0473 0.0051  0.0295  59  TRP   A CZ2 
223  C CZ3 . TRP   A 37  ? 0.3901 0.3445 0.3128 -0.0515 0.0148  0.0252  59  TRP   A CZ3 
224  C CH2 . TRP   A 37  ? 0.3869 0.3479 0.3368 -0.0444 0.0355  0.0199  59  TRP   A CH2 
225  N N   . LEU   A 38  ? 0.1733 0.2570 0.1650 -0.0142 -0.0044 0.0526  60  LEU   A N   
226  C CA  . LEU   A 38  ? 0.1807 0.2575 0.1732 -0.0177 -0.0084 0.0391  60  LEU   A CA  
227  C C   . LEU   A 38  ? 0.1771 0.2643 0.1757 -0.0269 -0.0138 0.0567  60  LEU   A C   
228  O O   . LEU   A 38  ? 0.1678 0.2514 0.2068 -0.0348 -0.0282 0.0658  60  LEU   A O   
229  C CB  . LEU   A 38  ? 0.1868 0.2583 0.1888 -0.0094 -0.0132 0.0364  60  LEU   A CB  
230  C CG  . LEU   A 38  ? 0.2086 0.2716 0.1954 -0.0043 0.0026  0.0148  60  LEU   A CG  
231  C CD1 . LEU   A 38  ? 0.2101 0.2850 0.1959 -0.0073 0.0054  0.0188  60  LEU   A CD1 
232  C CD2 . LEU   A 38  ? 0.2083 0.2876 0.2030 -0.0081 0.0012  0.0169  60  LEU   A CD2 
233  N N   . ALA   A 39  ? 0.1658 0.2603 0.1810 -0.0213 0.0015  0.0660  61  ALA   A N   
234  C CA  . ALA   A 39  ? 0.1883 0.2588 0.1627 -0.0221 0.0005  0.0594  61  ALA   A CA  
235  C C   . ALA   A 39  ? 0.1885 0.2666 0.1663 -0.0233 0.0057  0.0590  61  ALA   A C   
236  O O   . ALA   A 39  ? 0.2142 0.2852 0.1520 -0.0245 0.0202  0.0428  61  ALA   A O   
237  C CB  . ALA   A 39  ? 0.1891 0.2422 0.1545 -0.0221 -0.0056 0.0644  61  ALA   A CB  
238  N N   . SER   A 40  ? 0.1755 0.2674 0.1724 -0.0244 0.0048  0.0549  62  SER   A N   
239  C CA  . SER   A 40  ? 0.1705 0.2768 0.1855 -0.0254 0.0093  0.0496  62  SER   A CA  
240  C C   . SER   A 40  ? 0.1649 0.2679 0.1821 -0.0195 0.0074  0.0515  62  SER   A C   
241  O O   . SER   A 40  ? 0.1997 0.2455 0.1836 -0.0022 0.0057  0.0566  62  SER   A O   
242  C CB  . SER   A 40  ? 0.1659 0.2859 0.1823 -0.0317 0.0196  0.0466  62  SER   A CB  
243  O OG  . SER   A 40  ? 0.1704 0.2848 0.1709 -0.0445 0.0145  0.0506  62  SER   A OG  
244  N N   . SER   A 41  ? 0.1672 0.2690 0.1774 -0.0189 0.0160  0.0520  63  SER   A N   
245  C CA  . SER   A 41  ? 0.1719 0.2657 0.1859 -0.0030 0.0169  0.0454  63  SER   A CA  
246  C C   . SER   A 41  ? 0.1695 0.2788 0.1938 0.0073  0.0243  0.0483  63  SER   A C   
247  O O   . SER   A 41  ? 0.1779 0.2777 0.1805 0.0223  0.0296  0.0412  63  SER   A O   
248  C CB  . SER   A 41  ? 0.1735 0.2591 0.1913 -0.0012 0.0218  0.0509  63  SER   A CB  
249  O OG  . SER   A 41  ? 0.1501 0.2825 0.1952 0.0082  0.0045  0.0419  63  SER   A OG  
250  N N   . SER   A 42  ? 0.1678 0.2908 0.2131 0.0043  0.0411  0.0517  64  SER   A N   
251  C CA  . SER   A 42  ? 0.1724 0.3115 0.2028 0.0156  0.0357  0.0558  64  SER   A CA  
252  C C   . SER   A 42  ? 0.1674 0.3203 0.2023 0.0091  0.0308  0.0596  64  SER   A C   
253  O O   . SER   A 42  ? 0.1505 0.3097 0.2073 0.0242  0.0098  0.0622  64  SER   A O   
254  C CB  . SER   A 42  ? 0.1667 0.3147 0.2074 0.0094  0.0396  0.0592  64  SER   A CB  
255  O OG  . SER   A 42  ? 0.1695 0.3332 0.2174 0.0271  0.0382  0.0662  64  SER   A OG  
256  N N   . ALA   A 43  ? 0.1927 0.3368 0.1985 -0.0010 0.0276  0.0703  65  ALA   A N   
257  C CA  . ALA   A 43  ? 0.2002 0.3526 0.1993 -0.0010 0.0259  0.0794  65  ALA   A CA  
258  C C   . ALA   A 43  ? 0.1870 0.3519 0.2128 -0.0081 0.0432  0.0994  65  ALA   A C   
259  O O   . ALA   A 43  ? 0.1885 0.3719 0.2114 -0.0095 0.0489  0.1194  65  ALA   A O   
260  C CB  . ALA   A 43  ? 0.1877 0.3570 0.1919 -0.0048 0.0410  0.0858  65  ALA   A CB  
261  N N   . ASP   A 44  ? 0.1928 0.3381 0.2118 -0.0013 0.0398  0.1164  66  ASP   A N   
262  C CA  . ASP   A 44  ? 0.1827 0.3210 0.2004 -0.0015 0.0384  0.1064  66  ASP   A CA  
263  C C   . ASP   A 44  ? 0.1857 0.3155 0.2134 -0.0132 0.0337  0.1049  66  ASP   A C   
264  O O   . ASP   A 44  ? 0.1936 0.3086 0.2285 -0.0049 0.0331  0.1021  66  ASP   A O   
265  C CB  . ASP   A 44  ? 0.1848 0.3309 0.2059 -0.0075 0.0355  0.1054  66  ASP   A CB  
266  C CG  . ASP   A 44  ? 0.1893 0.3174 0.2141 0.0031  0.0309  0.1107  66  ASP   A CG  
267  O OD1 . ASP   A 44  ? 0.1957 0.2818 0.2229 0.0208  0.0315  0.0787  66  ASP   A OD1 
268  O OD2 . ASP   A 44  ? 0.1945 0.3348 0.2432 0.0178  0.0282  0.0948  66  ASP   A OD2 
269  N N   . LYS   A 45  ? 0.1848 0.3050 0.2232 -0.0282 0.0405  0.1076  67  LYS   A N   
270  C CA  . LYS   A 45  ? 0.1925 0.3100 0.2397 -0.0260 0.0346  0.0992  67  LYS   A CA  
271  C C   . LYS   A 45  ? 0.1933 0.3074 0.2285 -0.0226 0.0381  0.0924  67  LYS   A C   
272  O O   . LYS   A 45  ? 0.1823 0.2912 0.2404 -0.0180 0.0368  0.0999  67  LYS   A O   
273  C CB  . LYS   A 45  ? 0.2193 0.3184 0.2508 -0.0304 0.0328  0.0932  67  LYS   A CB  
274  C CG  . LYS   A 45  ? 0.2676 0.3304 0.2755 -0.0462 0.0266  0.1131  67  LYS   A CG  
275  C CD  . LYS   A 45  ? 0.3321 0.3569 0.3076 -0.0632 0.0287  0.1212  67  LYS   A CD  
276  C CE  . LYS   A 45  ? 0.3887 0.3697 0.3319 -0.0834 0.0392  0.1295  67  LYS   A CE  
277  N NZ  . LYS   A 45  ? 0.4440 0.4068 0.3872 -0.0974 0.0450  0.1162  67  LYS   A NZ  
278  N N   . LEU   A 46  ? 0.2062 0.3032 0.2148 -0.0200 0.0337  0.0850  68  LEU   A N   
279  C CA  . LEU   A 46  ? 0.1991 0.3128 0.2148 -0.0247 0.0216  0.0838  68  LEU   A CA  
280  C C   . LEU   A 46  ? 0.1966 0.3051 0.1961 -0.0216 0.0149  0.0659  68  LEU   A C   
281  O O   . LEU   A 46  ? 0.1864 0.2891 0.1840 -0.0163 0.0127  0.0701  68  LEU   A O   
282  C CB  . LEU   A 46  ? 0.2015 0.3204 0.2379 -0.0262 0.0271  0.0918  68  LEU   A CB  
283  C CG  . LEU   A 46  ? 0.2115 0.3286 0.2700 -0.0325 0.0420  0.0872  68  LEU   A CG  
284  C CD1 . LEU   A 46  ? 0.2157 0.3508 0.3025 -0.0191 0.0454  0.0771  68  LEU   A CD1 
285  C CD2 . LEU   A 46  ? 0.2379 0.3468 0.2806 -0.0348 0.0410  0.0860  68  LEU   A CD2 
286  N N   . ILE   A 47  ? 0.1977 0.2887 0.1949 -0.0307 0.0310  0.0601  69  ILE   A N   
287  C CA  . ILE   A 47  ? 0.1979 0.2928 0.1856 -0.0321 0.0240  0.0535  69  ILE   A CA  
288  C C   . ILE   A 47  ? 0.1790 0.2700 0.1961 -0.0361 0.0221  0.0469  69  ILE   A C   
289  O O   . ILE   A 47  ? 0.1901 0.2521 0.1755 -0.0252 0.0220  0.0318  69  ILE   A O   
290  C CB  . ILE   A 47  ? 0.2023 0.3061 0.1986 -0.0260 0.0345  0.0444  69  ILE   A CB  
291  C CG1 . ILE   A 47  ? 0.2349 0.3557 0.2020 -0.0076 0.0231  0.0272  69  ILE   A CG1 
292  C CG2 . ILE   A 47  ? 0.1898 0.3260 0.2022 -0.0409 0.0590  0.0465  69  ILE   A CG2 
293  C CD1 . ILE   A 47  ? 0.2323 0.3888 0.2328 -0.0039 0.0141  0.0215  69  ILE   A CD1 
294  N N   . LYS   A 48  ? 0.1604 0.2642 0.1962 -0.0350 0.0115  0.0508  70  LYS   A N   
295  C CA  . LYS   A 48  ? 0.1683 0.2975 0.1855 -0.0293 0.0111  0.0565  70  LYS   A CA  
296  C C   . LYS   A 48  ? 0.1744 0.2918 0.1972 -0.0348 0.0050  0.0590  70  LYS   A C   
297  O O   . LYS   A 48  ? 0.1865 0.2927 0.1639 -0.0434 0.0081  0.0558  70  LYS   A O   
298  C CB  . LYS   A 48  ? 0.1575 0.3225 0.1982 -0.0288 0.0102  0.0723  70  LYS   A CB  
299  C CG  . LYS   A 48  ? 0.1721 0.3252 0.2310 -0.0288 0.0170  0.0805  70  LYS   A CG  
300  C CD  . LYS   A 48  ? 0.1792 0.3359 0.2507 -0.0330 0.0308  0.0864  70  LYS   A CD  
301  C CE  . LYS   A 48  ? 0.1772 0.3251 0.2582 -0.0366 0.0409  0.0814  70  LYS   A CE  
302  N NZ  . LYS   A 48  ? 0.1843 0.3384 0.3052 -0.0418 0.0516  0.0814  70  LYS   A NZ  
303  N N   . ILE   A 49  ? 0.1722 0.2838 0.1942 -0.0276 0.0053  0.0631  71  ILE   A N   
304  C CA  . ILE   A 49  ? 0.1668 0.2914 0.2058 -0.0157 0.0161  0.0714  71  ILE   A CA  
305  C C   . ILE   A 49  ? 0.1606 0.2754 0.1922 -0.0232 0.0127  0.0687  71  ILE   A C   
306  O O   . ILE   A 49  ? 0.1694 0.2673 0.2160 -0.0326 0.0000  0.0739  71  ILE   A O   
307  C CB  . ILE   A 49  ? 0.1830 0.3058 0.2071 -0.0124 0.0211  0.0834  71  ILE   A CB  
308  C CG1 . ILE   A 49  ? 0.1975 0.3115 0.2064 -0.0141 0.0193  0.0925  71  ILE   A CG1 
309  C CG2 . ILE   A 49  ? 0.2121 0.3045 0.2332 -0.0014 0.0179  0.0955  71  ILE   A CG2 
310  C CD1 . ILE   A 49  ? 0.2052 0.3057 0.2113 -0.0253 0.0132  0.0973  71  ILE   A CD1 
311  N N   . TRP   A 50  ? 0.1429 0.2701 0.2079 -0.0337 0.0184  0.0621  72  TRP   A N   
312  C CA  . TRP   A 50  ? 0.1693 0.2717 0.2045 -0.0288 0.0153  0.0607  72  TRP   A CA  
313  C C   . TRP   A 50  ? 0.1858 0.2676 0.1855 -0.0162 0.0110  0.0540  72  TRP   A C   
314  O O   . TRP   A 50  ? 0.1902 0.2726 0.1908 -0.0131 -0.0093 0.0422  72  TRP   A O   
315  C CB  . TRP   A 50  ? 0.1608 0.2900 0.1976 -0.0325 0.0146  0.0604  72  TRP   A CB  
316  C CG  . TRP   A 50  ? 0.1687 0.2847 0.2060 -0.0342 0.0183  0.0650  72  TRP   A CG  
317  C CD1 . TRP   A 50  ? 0.1789 0.2930 0.2061 -0.0255 0.0257  0.0723  72  TRP   A CD1 
318  C CD2 . TRP   A 50  ? 0.1821 0.3019 0.2152 -0.0300 0.0306  0.0665  72  TRP   A CD2 
319  N NE1 . TRP   A 50  ? 0.1904 0.2849 0.2128 -0.0275 0.0250  0.0706  72  TRP   A NE1 
320  C CE2 . TRP   A 50  ? 0.1889 0.2836 0.2213 -0.0198 0.0296  0.0664  72  TRP   A CE2 
321  C CE3 . TRP   A 50  ? 0.1860 0.2966 0.2340 -0.0254 0.0439  0.0709  72  TRP   A CE3 
322  C CZ2 . TRP   A 50  ? 0.2051 0.2913 0.2404 -0.0205 0.0360  0.0711  72  TRP   A CZ2 
323  C CZ3 . TRP   A 50  ? 0.1930 0.3062 0.2495 -0.0266 0.0487  0.0713  72  TRP   A CZ3 
324  C CH2 . TRP   A 50  ? 0.1958 0.3020 0.2436 -0.0281 0.0385  0.0664  72  TRP   A CH2 
325  N N   . GLY   A 51  ? 0.1952 0.2692 0.2061 -0.0047 0.0113  0.0562  73  GLY   A N   
326  C CA  . GLY   A 51  ? 0.1972 0.2618 0.2017 -0.0024 0.0075  0.0593  73  GLY   A CA  
327  C C   . GLY   A 51  ? 0.1932 0.2600 0.1903 -0.0054 0.0193  0.0623  73  GLY   A C   
328  O O   . GLY   A 51  ? 0.1943 0.2391 0.1775 0.0038  0.0260  0.0737  73  GLY   A O   
329  N N   . ALA   A 52  ? 0.1866 0.2583 0.1629 -0.0074 0.0256  0.0681  74  ALA   A N   
330  C CA  . ALA   A 52  ? 0.1920 0.2741 0.1641 -0.0104 0.0241  0.0606  74  ALA   A CA  
331  C C   . ALA   A 52  ? 0.1986 0.2750 0.1724 -0.0114 0.0128  0.0562  74  ALA   A C   
332  O O   . ALA   A 52  ? 0.2280 0.2859 0.1609 -0.0088 0.0090  0.0553  74  ALA   A O   
333  C CB  . ALA   A 52  ? 0.1747 0.2901 0.1777 -0.0114 0.0048  0.0544  74  ALA   A CB  
334  N N   . TYR   A 53  ? 0.1964 0.2546 0.1808 -0.0155 0.0008  0.0513  75  TYR   A N   
335  C CA  . TYR   A 53  ? 0.2068 0.2486 0.1787 -0.0100 0.0044  0.0542  75  TYR   A CA  
336  C C   . TYR   A 53  ? 0.2075 0.2557 0.1968 -0.0068 0.0034  0.0495  75  TYR   A C   
337  O O   . TYR   A 53  ? 0.2306 0.2652 0.1948 -0.0192 0.0031  0.0388  75  TYR   A O   
338  C CB  . TYR   A 53  ? 0.2113 0.2564 0.1687 -0.0044 -0.0063 0.0511  75  TYR   A CB  
339  C CG  . TYR   A 53  ? 0.2118 0.2494 0.1471 -0.0096 -0.0093 0.0543  75  TYR   A CG  
340  C CD1 . TYR   A 53  ? 0.2163 0.2518 0.1398 -0.0032 -0.0067 0.0412  75  TYR   A CD1 
341  C CD2 . TYR   A 53  ? 0.2198 0.2516 0.1471 -0.0086 -0.0184 0.0483  75  TYR   A CD2 
342  C CE1 . TYR   A 53  ? 0.2164 0.2515 0.1567 -0.0085 -0.0213 0.0478  75  TYR   A CE1 
343  C CE2 . TYR   A 53  ? 0.2107 0.2465 0.1691 -0.0003 -0.0233 0.0441  75  TYR   A CE2 
344  C CZ  . TYR   A 53  ? 0.2207 0.2276 0.1537 0.0003  -0.0238 0.0464  75  TYR   A CZ  
345  O OH  . TYR   A 53  ? 0.2336 0.2210 0.1673 -0.0261 -0.0132 0.0642  75  TYR   A OH  
346  N N   . ASP   A 54  ? 0.1996 0.2596 0.2041 -0.0082 -0.0054 0.0380  76  ASP   A N   
347  C CA  . ASP   A 54  ? 0.2048 0.2766 0.2222 -0.0022 -0.0017 0.0474  76  ASP   A CA  
348  C C   . ASP   A 54  ? 0.2138 0.2805 0.2110 -0.0035 -0.0134 0.0517  76  ASP   A C   
349  O O   . ASP   A 54  ? 0.2247 0.3266 0.2293 0.0090  -0.0279 0.0573  76  ASP   A O   
350  C CB  . ASP   A 54  ? 0.1954 0.2802 0.2209 -0.0097 0.0021  0.0492  76  ASP   A CB  
351  C CG  . ASP   A 54  ? 0.1918 0.2984 0.2325 -0.0043 0.0073  0.0383  76  ASP   A CG  
352  O OD1 . ASP   A 54  ? 0.1598 0.3076 0.2629 -0.0099 0.0098  0.0369  76  ASP   A OD1 
353  O OD2 . ASP   A 54  ? 0.1877 0.3419 0.2511 -0.0048 0.0080  0.0185  76  ASP   A OD2 
354  N N   . GLY   A 55  ? 0.2219 0.2892 0.2066 -0.0146 -0.0134 0.0722  77  GLY   A N   
355  C CA  . GLY   A 55  ? 0.2208 0.2908 0.2257 -0.0279 0.0014  0.0799  77  GLY   A CA  
356  C C   . GLY   A 55  ? 0.2260 0.2892 0.2218 -0.0353 -0.0049 0.0930  77  GLY   A C   
357  O O   . GLY   A 55  ? 0.2472 0.3316 0.2072 -0.0423 0.0198  0.0925  77  GLY   A O   
358  N N   . LYS   A 56  ? 0.2381 0.2849 0.2283 -0.0289 -0.0036 0.0976  78  LYS   A N   
359  C CA  . LYS   A 56  ? 0.2191 0.2788 0.2449 -0.0311 -0.0132 0.0947  78  LYS   A CA  
360  C C   . LYS   A 56  ? 0.1957 0.2913 0.2571 -0.0279 0.0013  0.1036  78  LYS   A C   
361  O O   . LYS   A 56  ? 0.1878 0.3108 0.2599 -0.0221 0.0103  0.1101  78  LYS   A O   
362  C CB  . LYS   A 56  ? 0.2716 0.2836 0.2575 -0.0286 -0.0257 0.0908  78  LYS   A CB  
363  C CG  . LYS   A 56  ? 0.3193 0.2873 0.3187 -0.0384 -0.0376 0.0800  78  LYS   A CG  
364  C CD  . LYS   A 56  ? 0.3944 0.2942 0.3424 -0.0383 -0.0643 0.0554  78  LYS   A CD  
365  C CE  . LYS   A 56  ? 0.4690 0.3377 0.4379 -0.0387 -0.0462 0.0336  78  LYS   A CE  
366  N N   . PHE   A 57  ? 0.1849 0.3067 0.2618 -0.0248 0.0019  0.1088  79  PHE   A N   
367  C CA  . PHE   A 57  ? 0.1944 0.3112 0.2704 -0.0187 -0.0013 0.1020  79  PHE   A CA  
368  C C   . PHE   A 57  ? 0.2046 0.3431 0.2670 -0.0267 -0.0229 0.0892  79  PHE   A C   
369  O O   . PHE   A 57  ? 0.2309 0.3641 0.2549 -0.0208 -0.0284 0.1099  79  PHE   A O   
370  C CB  . PHE   A 57  ? 0.1986 0.3084 0.2614 -0.0259 -0.0085 0.1014  79  PHE   A CB  
371  C CG  . PHE   A 57  ? 0.2185 0.3159 0.2693 -0.0174 -0.0171 0.0932  79  PHE   A CG  
372  C CD1 . PHE   A 57  ? 0.2076 0.3112 0.2158 -0.0299 -0.0070 0.0978  79  PHE   A CD1 
373  C CD2 . PHE   A 57  ? 0.2436 0.3135 0.2918 -0.0270 -0.0236 0.1122  79  PHE   A CD2 
374  C CE1 . PHE   A 57  ? 0.2134 0.3163 0.2389 -0.0304 -0.0165 0.0922  79  PHE   A CE1 
375  C CE2 . PHE   A 57  ? 0.2438 0.3089 0.3151 -0.0301 -0.0184 0.0994  79  PHE   A CE2 
376  C CZ  . PHE   A 57  ? 0.2527 0.3075 0.2799 -0.0288 -0.0182 0.1000  79  PHE   A CZ  
377  N N   . GLU   A 58  ? 0.2084 0.3069 0.2544 -0.0224 -0.0427 0.0916  80  GLU   A N   
378  C CA  . GLU   A 58  ? 0.2200 0.3394 0.2517 -0.0361 -0.0249 0.0909  80  GLU   A CA  
379  C C   . GLU   A 58  ? 0.1982 0.3112 0.2387 -0.0497 -0.0150 0.0767  80  GLU   A C   
380  O O   . GLU   A 58  ? 0.2194 0.3055 0.2389 -0.0788 -0.0271 0.0815  80  GLU   A O   
381  C CB  . GLU   A 58  ? 0.2228 0.3769 0.2639 -0.0471 -0.0203 0.0693  80  GLU   A CB  
382  C CG  . GLU   A 58  ? 0.3072 0.4377 0.3039 -0.0336 -0.0135 0.0547  80  GLU   A CG  
383  C CD  . GLU   A 58  ? 0.3505 0.4808 0.3176 -0.0210 -0.0314 0.0429  80  GLU   A CD  
384  O OE1 . GLU   A 58  ? 0.3372 0.4884 0.3398 -0.0223 -0.0493 0.0858  80  GLU   A OE1 
385  O OE2 . GLU   A 58  ? 0.4492 0.5229 0.3630 -0.0071 -0.0037 0.0099  80  GLU   A OE2 
386  N N   . LYS   A 59  ? 0.1949 0.3120 0.2271 -0.0515 -0.0058 0.0800  81  LYS   A N   
387  C CA  . LYS   A 59  ? 0.2135 0.3142 0.2221 -0.0495 -0.0016 0.0762  81  LYS   A CA  
388  C C   . LYS   A 59  ? 0.1947 0.3141 0.2292 -0.0526 -0.0068 0.0797  81  LYS   A C   
389  O O   . LYS   A 59  ? 0.1732 0.3111 0.2194 -0.0520 -0.0001 0.0854  81  LYS   A O   
390  C CB  . LYS   A 59  ? 0.2416 0.3268 0.2436 -0.0423 0.0011  0.0695  81  LYS   A CB  
391  C CG  . LYS   A 59  ? 0.2569 0.3420 0.2580 -0.0569 0.0089  0.0649  81  LYS   A CG  
392  C CD  . LYS   A 59  ? 0.2930 0.3703 0.2982 -0.0503 0.0065  0.0339  81  LYS   A CD  
393  C CE  . LYS   A 59  ? 0.3069 0.4339 0.3092 -0.0531 -0.0089 -0.0018 81  LYS   A CE  
394  N NZ  . LYS   A 59  ? 0.2997 0.4792 0.3094 -0.0466 -0.0055 -0.0275 81  LYS   A NZ  
395  N N   . THR   A 60  ? 0.2209 0.2976 0.2187 -0.0389 -0.0213 0.0691  82  THR   A N   
396  C CA  . THR   A 60  ? 0.2267 0.3112 0.2174 -0.0428 -0.0063 0.0747  82  THR   A CA  
397  C C   . THR   A 60  ? 0.2337 0.2960 0.2172 -0.0421 0.0054  0.0502  82  THR   A C   
398  O O   . THR   A 60  ? 0.2476 0.3440 0.2409 -0.0576 -0.0324 0.0304  82  THR   A O   
399  C CB  . THR   A 60  ? 0.2396 0.3219 0.2272 -0.0388 0.0049  0.0862  82  THR   A CB  
400  O OG1 . THR   A 60  ? 0.2085 0.3399 0.2420 -0.0410 0.0249  0.0970  82  THR   A OG1 
401  C CG2 . THR   A 60  ? 0.2516 0.3398 0.2296 -0.0414 0.0016  0.0833  82  THR   A CG2 
402  N N   . ILE   A 61  ? 0.2254 0.2835 0.2098 -0.0364 0.0149  0.0330  83  ILE   A N   
403  C CA  . ILE   A 61  ? 0.2367 0.2901 0.2288 -0.0360 0.0200  0.0503  83  ILE   A CA  
404  C C   . ILE   A 61  ? 0.2312 0.2863 0.2362 -0.0440 0.0200  0.0568  83  ILE   A C   
405  O O   . ILE   A 61  ? 0.2433 0.2979 0.2352 -0.0454 0.0051  0.0473  83  ILE   A O   
406  C CB  . ILE   A 61  ? 0.2318 0.2976 0.2211 -0.0260 0.0300  0.0569  83  ILE   A CB  
407  C CG1 . ILE   A 61  ? 0.2430 0.2968 0.2223 -0.0268 0.0559  0.0544  83  ILE   A CG1 
408  C CG2 . ILE   A 61  ? 0.2583 0.3097 0.2249 -0.0122 0.0266  0.0463  83  ILE   A CG2 
409  C CD1 . ILE   A 61  ? 0.2509 0.2945 0.2275 -0.0206 0.0692  0.0601  83  ILE   A CD1 
410  N N   A SER   A 62  ? 0.2453 0.2898 0.2484 -0.0407 0.0150  0.0602  84  SER   A N   
411  N N   B SER   A 62  ? 0.2354 0.2843 0.2510 -0.0366 0.0125  0.0577  84  SER   A N   
412  C CA  A SER   A 62  ? 0.2521 0.2935 0.2403 -0.0410 0.0059  0.0619  84  SER   A CA  
413  C CA  B SER   A 62  ? 0.2347 0.2794 0.2543 -0.0342 0.0085  0.0609  84  SER   A CA  
414  C C   A SER   A 62  ? 0.2291 0.2880 0.2362 -0.0487 0.0116  0.0728  84  SER   A C   
415  C C   B SER   A 62  ? 0.2238 0.2817 0.2406 -0.0399 0.0111  0.0688  84  SER   A C   
416  O O   A SER   A 62  ? 0.2258 0.2898 0.2404 -0.0551 0.0149  0.0757  84  SER   A O   
417  O O   B SER   A 62  ? 0.2204 0.2829 0.2430 -0.0488 0.0150  0.0694  84  SER   A O   
418  C CB  A SER   A 62  ? 0.2543 0.3022 0.2521 -0.0407 -0.0052 0.0589  84  SER   A CB  
419  C CB  B SER   A 62  ? 0.2303 0.2738 0.2740 -0.0268 0.0010  0.0581  84  SER   A CB  
420  O OG  A SER   A 62  ? 0.2568 0.3167 0.2456 -0.0463 -0.0141 0.0580  84  SER   A OG  
421  O OG  B SER   A 62  ? 0.2315 0.2600 0.2995 -0.0232 -0.0048 0.0541  84  SER   A OG  
422  N N   . GLY   A 63  ? 0.2226 0.2905 0.2316 -0.0397 0.0137  0.0682  85  GLY   A N   
423  C CA  . GLY   A 63  ? 0.2433 0.3019 0.2337 -0.0262 0.0171  0.0821  85  GLY   A CA  
424  C C   . GLY   A 63  ? 0.2250 0.2981 0.2517 -0.0033 0.0122  0.0884  85  GLY   A C   
425  O O   . GLY   A 63  ? 0.2744 0.2983 0.2946 -0.0028 0.0134  0.1056  85  GLY   A O   
426  N N   . HIS   A 64  ? 0.2198 0.3006 0.2440 0.0070  0.0279  0.0961  86  HIS   A N   
427  C CA  . HIS   A 64  ? 0.2215 0.3009 0.2276 0.0129  0.0440  0.0890  86  HIS   A CA  
428  C C   . HIS   A 64  ? 0.2491 0.2970 0.2682 -0.0027 0.0506  0.1069  86  HIS   A C   
429  O O   . HIS   A 64  ? 0.2537 0.3156 0.2812 -0.0161 0.0304  0.1136  86  HIS   A O   
430  C CB  . HIS   A 64  ? 0.2023 0.2926 0.2168 0.0225  0.0518  0.0744  86  HIS   A CB  
431  C CG  . HIS   A 64  ? 0.1754 0.2978 0.2350 0.0278  0.0401  0.0689  86  HIS   A CG  
432  N ND1 . HIS   A 64  ? 0.1703 0.3007 0.2285 0.0287  0.0335  0.0672  86  HIS   A ND1 
433  C CD2 . HIS   A 64  ? 0.1686 0.3009 0.2235 0.0399  0.0357  0.0634  86  HIS   A CD2 
434  C CE1 . HIS   A 64  ? 0.1781 0.3019 0.2219 0.0467  0.0367  0.0679  86  HIS   A CE1 
435  N NE2 . HIS   A 64  ? 0.1733 0.2950 0.2216 0.0515  0.0419  0.0651  86  HIS   A NE2 
436  N N   . LYS   A 65  ? 0.3013 0.3002 0.2660 0.0130  0.0614  0.1204  87  LYS   A N   
437  C CA  . LYS   A 65  ? 0.3466 0.3041 0.2781 0.0154  0.0712  0.1281  87  LYS   A CA  
438  C C   . LYS   A 65  ? 0.2926 0.3005 0.2638 0.0000  0.0765  0.1324  87  LYS   A C   
439  O O   . LYS   A 65  ? 0.2687 0.3060 0.2980 0.0079  0.0821  0.1236  87  LYS   A O   
440  C CB  . LYS   A 65  ? 0.4293 0.3253 0.3300 0.0558  0.0643  0.1256  87  LYS   A CB  
441  C CG  . LYS   A 65  ? 0.4913 0.3306 0.3871 0.0727  0.0665  0.1191  87  LYS   A CG  
442  C CD  . LYS   A 65  ? 0.5253 0.3291 0.4214 0.0839  0.0638  0.1299  87  LYS   A CD  
443  N N   . LEU   A 66  ? 0.2289 0.3376 0.2179 -0.0132 0.0708  0.1268  88  LEU   A N   
444  C CA  . LEU   A 66  ? 0.2124 0.3487 0.2301 -0.0099 0.0593  0.1190  88  LEU   A CA  
445  C C   . LEU   A 66  ? 0.2017 0.3445 0.2126 -0.0147 0.0531  0.1144  88  LEU   A C   
446  O O   . LEU   A 66  ? 0.2284 0.3538 0.2164 -0.0092 0.0775  0.1016  88  LEU   A O   
447  C CB  . LEU   A 66  ? 0.2119 0.3601 0.2426 -0.0123 0.0483  0.1342  88  LEU   A CB  
448  C CG  . LEU   A 66  ? 0.1941 0.3756 0.2420 -0.0313 0.0382  0.1487  88  LEU   A CG  
449  C CD1 . LEU   A 66  ? 0.1986 0.3896 0.2612 -0.0312 0.0399  0.1532  88  LEU   A CD1 
450  C CD2 . LEU   A 66  ? 0.2005 0.3725 0.2385 -0.0243 0.0398  0.1428  88  LEU   A CD2 
451  N N   . GLY   A 67  ? 0.1845 0.3402 0.1859 -0.0096 0.0380  0.1011  89  GLY   A N   
452  C CA  . GLY   A 67  ? 0.1674 0.3478 0.1940 -0.0102 0.0436  0.1041  89  GLY   A CA  
453  C C   . GLY   A 67  ? 0.1627 0.3472 0.2001 -0.0147 0.0395  0.0939  89  GLY   A C   
454  O O   . GLY   A 67  ? 0.1709 0.3419 0.2043 -0.0080 0.0384  0.1121  89  GLY   A O   
455  N N   . ILE   A 68  ? 0.1511 0.3154 0.2151 -0.0141 0.0490  0.0770  90  ILE   A N   
456  C CA  . ILE   A 68  ? 0.1733 0.3117 0.1925 -0.0124 0.0560  0.0700  90  ILE   A CA  
457  C C   . ILE   A 68  ? 0.1729 0.3127 0.1884 -0.0091 0.0529  0.0608  90  ILE   A C   
458  O O   . ILE   A 68  ? 0.1653 0.3275 0.1917 -0.0024 0.0477  0.0367  90  ILE   A O   
459  C CB  . ILE   A 68  ? 0.1634 0.3209 0.1967 -0.0043 0.0398  0.0690  90  ILE   A CB  
460  C CG1 . ILE   A 68  ? 0.1834 0.3268 0.1904 -0.0017 0.0261  0.0618  90  ILE   A CG1 
461  C CG2 . ILE   A 68  ? 0.1556 0.3206 0.2301 -0.0026 0.0472  0.0674  90  ILE   A CG2 
462  C CD1 . ILE   A 68  ? 0.1905 0.3318 0.2135 -0.0048 0.0104  0.0486  90  ILE   A CD1 
463  N N   . SER   A 69  ? 0.1676 0.3154 0.1685 -0.0011 0.0451  0.0569  91  SER   A N   
464  C CA  . SER   A 69  ? 0.1752 0.3148 0.1736 -0.0003 0.0373  0.0578  91  SER   A CA  
465  C C   . SER   A 69  ? 0.1805 0.2937 0.1730 0.0117  0.0275  0.0544  91  SER   A C   
466  O O   . SER   A 69  ? 0.2042 0.2949 0.1523 0.0102  0.0297  0.0545  91  SER   A O   
467  C CB  . SER   A 69  ? 0.1923 0.3443 0.1885 -0.0095 0.0284  0.0630  91  SER   A CB  
468  O OG  . SER   A 69  ? 0.2228 0.3715 0.1873 -0.0228 0.0381  0.0670  91  SER   A OG  
469  N N   . ASP   A 70  ? 0.1770 0.2688 0.1831 0.0006  0.0197  0.0406  92  ASP   A N   
470  C CA  . ASP   A 70  ? 0.1785 0.2705 0.1875 0.0038  0.0206  0.0373  92  ASP   A CA  
471  C C   . ASP   A 70  ? 0.1767 0.2533 0.1855 0.0032  0.0199  0.0427  92  ASP   A C   
472  O O   . ASP   A 70  ? 0.1803 0.2520 0.1687 0.0233  0.0219  0.0504  92  ASP   A O   
473  C CB  . ASP   A 70  ? 0.1845 0.2788 0.2011 -0.0112 0.0215  0.0362  92  ASP   A CB  
474  C CG  . ASP   A 70  ? 0.1867 0.3005 0.2138 -0.0125 0.0290  0.0357  92  ASP   A CG  
475  O OD1 . ASP   A 70  ? 0.2099 0.3077 0.1987 -0.0158 0.0254  0.0421  92  ASP   A OD1 
476  O OD2 . ASP   A 70  ? 0.1648 0.3124 0.2153 0.0065  0.0269  0.0427  92  ASP   A OD2 
477  N N   . VAL   A 71  ? 0.1902 0.2518 0.1879 0.0091  0.0176  0.0386  93  VAL   A N   
478  C CA  . VAL   A 71  ? 0.2056 0.2682 0.1841 0.0085  0.0275  0.0515  93  VAL   A CA  
479  C C   . VAL   A 71  ? 0.1889 0.2527 0.1865 -0.0002 0.0265  0.0409  93  VAL   A C   
480  O O   . VAL   A 71  ? 0.2068 0.2617 0.1534 0.0249  0.0332  0.0472  93  VAL   A O   
481  C CB  . VAL   A 71  ? 0.2163 0.2945 0.2000 0.0275  0.0217  0.0472  93  VAL   A CB  
482  C CG1 . VAL   A 71  ? 0.2253 0.2939 0.2100 0.0332  0.0224  0.0564  93  VAL   A CG1 
483  C CG2 . VAL   A 71  ? 0.2388 0.3125 0.2062 0.0336  0.0352  0.0512  93  VAL   A CG2 
484  N N   . ALA   A 72  ? 0.1865 0.2295 0.1875 -0.0081 0.0253  0.0423  94  ALA   A N   
485  C CA  . ALA   A 72  ? 0.1893 0.2192 0.1840 -0.0094 0.0211  0.0430  94  ALA   A CA  
486  C C   . ALA   A 72  ? 0.1641 0.2203 0.1805 -0.0084 0.0184  0.0481  94  ALA   A C   
487  O O   . ALA   A 72  ? 0.1727 0.2131 0.1625 -0.0172 0.0105  0.0331  94  ALA   A O   
488  C CB  . ALA   A 72  ? 0.1836 0.2050 0.1902 -0.0178 0.0274  0.0364  94  ALA   A CB  
489  N N   . TRP   A 73  ? 0.1712 0.2407 0.1698 -0.0183 0.0181  0.0569  95  TRP   A N   
490  C CA  . TRP   A 73  ? 0.1688 0.2502 0.1610 -0.0167 0.0147  0.0469  95  TRP   A CA  
491  C C   . TRP   A 73  ? 0.1666 0.2635 0.1620 -0.0182 0.0085  0.0463  95  TRP   A C   
492  O O   . TRP   A 73  ? 0.1886 0.2705 0.1642 -0.0242 0.0055  0.0426  95  TRP   A O   
493  C CB  . TRP   A 73  ? 0.1682 0.2546 0.1515 -0.0116 0.0125  0.0393  95  TRP   A CB  
494  C CG  . TRP   A 73  ? 0.1693 0.2569 0.1439 -0.0235 0.0391  0.0459  95  TRP   A CG  
495  C CD1 . TRP   A 73  ? 0.1805 0.2696 0.1576 -0.0211 0.0308  0.0373  95  TRP   A CD1 
496  C CD2 . TRP   A 73  ? 0.1684 0.2695 0.1388 -0.0215 0.0378  0.0423  95  TRP   A CD2 
497  N NE1 . TRP   A 73  ? 0.1737 0.2720 0.1504 -0.0138 0.0359  0.0351  95  TRP   A NE1 
498  C CE2 . TRP   A 73  ? 0.1717 0.2665 0.1476 -0.0152 0.0345  0.0393  95  TRP   A CE2 
499  C CE3 . TRP   A 73  ? 0.1623 0.2677 0.1519 -0.0218 0.0455  0.0410  95  TRP   A CE3 
500  C CZ2 . TRP   A 73  ? 0.1736 0.2737 0.1597 -0.0168 0.0339  0.0363  95  TRP   A CZ2 
501  C CZ3 . TRP   A 73  ? 0.1764 0.2821 0.1579 -0.0148 0.0315  0.0350  95  TRP   A CZ3 
502  C CH2 . TRP   A 73  ? 0.1663 0.2710 0.1493 -0.0257 0.0396  0.0373  95  TRP   A CH2 
503  N N   . SER   A 74  ? 0.1727 0.2726 0.1839 -0.0222 0.0079  0.0476  96  SER   A N   
504  C CA  . SER   A 74  ? 0.1739 0.2727 0.1882 -0.0322 0.0169  0.0520  96  SER   A CA  
505  C C   . SER   A 74  ? 0.1823 0.2884 0.2232 -0.0280 0.0250  0.0693  96  SER   A C   
506  O O   . SER   A 74  ? 0.1717 0.3017 0.2304 -0.0173 0.0260  0.0677  96  SER   A O   
507  C CB  . SER   A 74  ? 0.1910 0.2648 0.1951 -0.0371 0.0199  0.0528  96  SER   A CB  
508  O OG  . SER   A 74  ? 0.1930 0.2478 0.1880 -0.0452 0.0189  0.0390  96  SER   A OG  
509  N N   . SER   A 75  ? 0.1929 0.3092 0.2137 -0.0286 0.0386  0.0840  97  SER   A N   
510  C CA  . SER   A 75  ? 0.2234 0.3082 0.2323 -0.0339 0.0304  0.0898  97  SER   A CA  
511  C C   . SER   A 75  ? 0.2156 0.3126 0.2230 -0.0361 0.0318  0.0713  97  SER   A C   
512  O O   . SER   A 75  ? 0.2251 0.3525 0.2466 -0.0059 0.0381  0.0701  97  SER   A O   
513  C CB  . SER   A 75  ? 0.2217 0.3300 0.2337 -0.0347 0.0371  0.0908  97  SER   A CB  
514  O OG  . SER   A 75  ? 0.2635 0.3555 0.2720 -0.0456 0.0365  0.0602  97  SER   A OG  
515  N N   . ASP   A 76  ? 0.2167 0.3162 0.2003 -0.0303 0.0233  0.0588  98  ASP   A N   
516  C CA  . ASP   A 76  ? 0.2200 0.3073 0.1999 -0.0354 0.0196  0.0491  98  ASP   A CA  
517  C C   . ASP   A 76  ? 0.2078 0.3036 0.1883 -0.0194 0.0035  0.0461  98  ASP   A C   
518  O O   . ASP   A 76  ? 0.2114 0.3127 0.1796 -0.0235 0.0132  0.0427  98  ASP   A O   
519  C CB  . ASP   A 76  ? 0.2459 0.3308 0.2234 -0.0206 0.0039  0.0329  98  ASP   A CB  
520  C CG  . ASP   A 76  ? 0.2572 0.3270 0.2215 -0.0243 0.0237  0.0219  98  ASP   A CG  
521  O OD1 . ASP   A 76  ? 0.2612 0.3374 0.2044 -0.0166 0.0104  0.0215  98  ASP   A OD1 
522  O OD2 . ASP   A 76  ? 0.2875 0.3591 0.2417 0.0038  0.0469  0.0102  98  ASP   A OD2 
523  N N   . SER   A 77  ? 0.1916 0.2848 0.1829 -0.0214 0.0070  0.0536  99  SER   A N   
524  C CA  . SER   A 77  ? 0.2047 0.2945 0.1673 -0.0236 0.0141  0.0472  99  SER   A CA  
525  C C   . SER   A 77  ? 0.2069 0.3008 0.1828 -0.0257 0.0068  0.0468  99  SER   A C   
526  O O   . SER   A 77  ? 0.2071 0.3103 0.1937 -0.0218 -0.0017 0.0633  99  SER   A O   
527  C CB  . SER   A 77  ? 0.1997 0.2920 0.1743 -0.0254 0.0043  0.0422  99  SER   A CB  
528  O OG  . SER   A 77  ? 0.2432 0.2923 0.2022 -0.0194 -0.0110 0.0355  99  SER   A OG  
529  N N   . ASN   A 78  ? 0.2213 0.2992 0.1648 -0.0187 0.0218  0.0490  100 ASN   A N   
530  C CA  . ASN   A 78  ? 0.2296 0.3007 0.1866 -0.0277 0.0198  0.0507  100 ASN   A CA  
531  C C   . ASN   A 78  ? 0.2361 0.2805 0.1888 -0.0289 0.0295  0.0446  100 ASN   A C   
532  O O   . ASN   A 78  ? 0.2461 0.2558 0.2072 -0.0366 0.0380  0.0294  100 ASN   A O   
533  C CB  . ASN   A 78  ? 0.2610 0.3217 0.1855 -0.0296 0.0253  0.0493  100 ASN   A CB  
534  C CG  . ASN   A 78  ? 0.2771 0.3618 0.1987 -0.0084 0.0152  0.0506  100 ASN   A CG  
535  O OD1 . ASN   A 78  ? 0.3167 0.3600 0.1974 0.0285  0.0028  0.0345  100 ASN   A OD1 
536  N ND2 . ASN   A 78  ? 0.2889 0.3947 0.2213 0.0073  0.0377  0.0463  100 ASN   A ND2 
537  N N   . LEU   A 79  ? 0.2111 0.2626 0.1889 -0.0170 0.0252  0.0470  101 LEU   A N   
538  C CA  . LEU   A 79  ? 0.2174 0.2450 0.1976 -0.0112 0.0432  0.0483  101 LEU   A CA  
539  C C   . LEU   A 79  ? 0.2023 0.2320 0.1873 -0.0001 0.0328  0.0467  101 LEU   A C   
540  O O   . LEU   A 79  ? 0.1719 0.2288 0.1589 0.0099  0.0202  0.0261  101 LEU   A O   
541  C CB  . LEU   A 79  ? 0.2279 0.2585 0.2242 -0.0034 0.0605  0.0439  101 LEU   A CB  
542  C CG  . LEU   A 79  ? 0.2473 0.2809 0.2492 0.0034  0.0664  0.0210  101 LEU   A CG  
543  C CD1 . LEU   A 79  ? 0.2620 0.2900 0.2296 0.0138  0.0706  0.0242  101 LEU   A CD1 
544  C CD2 . LEU   A 79  ? 0.2704 0.2816 0.2784 0.0047  0.0759  0.0019  101 LEU   A CD2 
545  N N   . LEU   A 80  ? 0.2050 0.2223 0.1805 -0.0019 0.0371  0.0395  102 LEU   A N   
546  C CA  . LEU   A 80  ? 0.2189 0.2429 0.1911 0.0009  0.0346  0.0420  102 LEU   A CA  
547  C C   . LEU   A 80  ? 0.2257 0.2515 0.1839 0.0012  0.0241  0.0426  102 LEU   A C   
548  O O   . LEU   A 80  ? 0.2605 0.2580 0.1737 -0.0002 -0.0176 0.0614  102 LEU   A O   
549  C CB  . LEU   A 80  ? 0.2244 0.2493 0.2045 -0.0087 0.0513  0.0478  102 LEU   A CB  
550  C CG  . LEU   A 80  ? 0.2358 0.2609 0.2638 0.0056  0.0697  0.0437  102 LEU   A CG  
551  C CD1 . LEU   A 80  ? 0.2518 0.2801 0.3167 0.0074  0.0662  0.0529  102 LEU   A CD1 
552  C CD2 . LEU   A 80  ? 0.2557 0.2736 0.3061 0.0083  0.0679  0.0311  102 LEU   A CD2 
553  N N   . VAL   A 81  ? 0.1937 0.2410 0.1886 -0.0104 0.0228  0.0406  103 VAL   A N   
554  C CA  . VAL   A 81  ? 0.1946 0.2478 0.1784 -0.0063 0.0297  0.0406  103 VAL   A CA  
555  C C   . VAL   A 81  ? 0.1867 0.2418 0.1808 -0.0004 0.0286  0.0455  103 VAL   A C   
556  O O   . VAL   A 81  ? 0.2294 0.2316 0.1596 0.0038  0.0494  0.0675  103 VAL   A O   
557  C CB  . VAL   A 81  ? 0.1959 0.2378 0.1737 -0.0110 0.0229  0.0403  103 VAL   A CB  
558  C CG1 . VAL   A 81  ? 0.1952 0.2352 0.1936 -0.0128 0.0252  0.0436  103 VAL   A CG1 
559  C CG2 . VAL   A 81  ? 0.1853 0.2358 0.1704 -0.0064 0.0145  0.0325  103 VAL   A CG2 
560  N N   . SER   A 82  ? 0.1735 0.2471 0.1822 -0.0031 0.0350  0.0470  104 SER   A N   
561  C CA  . SER   A 82  ? 0.1707 0.2424 0.1835 -0.0051 0.0378  0.0427  104 SER   A CA  
562  C C   . SER   A 82  ? 0.1671 0.2475 0.1909 -0.0001 0.0402  0.0453  104 SER   A C   
563  O O   . SER   A 82  ? 0.1948 0.2275 0.2121 0.0050  0.0363  0.0343  104 SER   A O   
564  C CB  . SER   A 82  ? 0.1741 0.2570 0.1779 -0.0100 0.0383  0.0416  104 SER   A CB  
565  O OG  . SER   A 82  ? 0.1893 0.2667 0.1804 -0.0259 0.0603  0.0456  104 SER   A OG  
566  N N   . ALA   A 83  ? 0.1810 0.2728 0.1995 0.0041  0.0275  0.0431  105 ALA   A N   
567  C CA  . ALA   A 83  ? 0.1496 0.2680 0.1859 0.0034  0.0408  0.0530  105 ALA   A CA  
568  C C   . ALA   A 83  ? 0.1432 0.2681 0.2040 0.0094  0.0442  0.0580  105 ALA   A C   
569  O O   . ALA   A 83  ? 0.1536 0.2859 0.2090 0.0305  0.0608  0.0587  105 ALA   A O   
570  C CB  . ALA   A 83  ? 0.1460 0.2805 0.1798 0.0013  0.0420  0.0490  105 ALA   A CB  
571  N N   . SER   A 84  ? 0.1258 0.2521 0.2058 -0.0016 0.0374  0.0637  106 SER   A N   
572  C CA  . SER   A 84  ? 0.1451 0.2763 0.2019 0.0015  0.0468  0.0656  106 SER   A CA  
573  C C   . SER   A 84  ? 0.1692 0.2951 0.1967 0.0017  0.0475  0.0664  106 SER   A C   
574  O O   . SER   A 84  ? 0.1743 0.2877 0.2016 -0.0034 0.0204  0.0539  106 SER   A O   
575  C CB  . SER   A 84  ? 0.1565 0.2590 0.2069 -0.0113 0.0508  0.0700  106 SER   A CB  
576  O OG  . SER   A 84  ? 0.1648 0.2658 0.2246 -0.0117 0.0560  0.0727  106 SER   A OG  
577  N N   . ASP   A 85  ? 0.1805 0.3270 0.1958 0.0078  0.0487  0.0842  107 ASP   A N   
578  C CA  . ASP   A 85  ? 0.1864 0.3451 0.1904 0.0120  0.0475  0.0888  107 ASP   A CA  
579  C C   . ASP   A 85  ? 0.1917 0.3351 0.2060 -0.0005 0.0408  0.0999  107 ASP   A C   
580  O O   . ASP   A 85  ? 0.1928 0.3491 0.2213 0.0101  0.0278  0.1147  107 ASP   A O   
581  C CB  . ASP   A 85  ? 0.1773 0.3680 0.1840 0.0099  0.0523  0.0894  107 ASP   A CB  
582  C CG  . ASP   A 85  ? 0.1920 0.3964 0.1904 0.0119  0.0753  0.0769  107 ASP   A CG  
583  O OD1 . ASP   A 85  ? 0.1896 0.3901 0.2085 0.0131  0.0654  0.0743  107 ASP   A OD1 
584  O OD2 . ASP   A 85  ? 0.2182 0.4402 0.1911 0.0176  0.0915  0.0783  107 ASP   A OD2 
585  N N   . ASP   A 86  ? 0.1846 0.3067 0.1913 0.0034  0.0390  0.1033  108 ASP   A N   
586  C CA  . ASP   A 86  ? 0.2054 0.2978 0.2203 -0.0070 0.0423  0.0792  108 ASP   A CA  
587  C C   . ASP   A 86  ? 0.2082 0.2759 0.2123 0.0082  0.0245  0.0793  108 ASP   A C   
588  O O   . ASP   A 86  ? 0.1990 0.2711 0.2465 -0.0204 0.0345  0.0562  108 ASP   A O   
589  C CB  . ASP   A 86  ? 0.2243 0.2978 0.2256 -0.0046 0.0285  0.0791  108 ASP   A CB  
590  C CG  . ASP   A 86  ? 0.2357 0.2789 0.2310 -0.0265 0.0298  0.0729  108 ASP   A CG  
591  O OD1 . ASP   A 86  ? 0.2272 0.2550 0.2217 -0.0324 0.0201  0.0737  108 ASP   A OD1 
592  O OD2 . ASP   A 86  ? 0.2790 0.2333 0.2604 -0.0536 0.0191  0.0366  108 ASP   A OD2 
593  N N   . LYS   A 87  ? 0.2000 0.2870 0.2092 0.0042  0.0199  0.0805  109 LYS   A N   
594  C CA  . LYS   A 87  ? 0.2138 0.2789 0.2122 0.0138  0.0175  0.0848  109 LYS   A CA  
595  C C   . LYS   A 87  ? 0.2210 0.2577 0.2126 0.0081  0.0269  0.0812  109 LYS   A C   
596  O O   . LYS   A 87  ? 0.2249 0.2567 0.1999 0.0013  0.0321  0.0840  109 LYS   A O   
597  C CB  . LYS   A 87  ? 0.2416 0.2981 0.2462 0.0199  -0.0023 0.0874  109 LYS   A CB  
598  C CG  . LYS   A 87  ? 0.2566 0.3422 0.2620 0.0305  0.0066  0.1015  109 LYS   A CG  
599  C CD  . LYS   A 87  ? 0.3171 0.3860 0.2971 0.0488  -0.0160 0.1222  109 LYS   A CD  
600  C CE  . LYS   A 87  ? 0.3786 0.4458 0.3520 0.0554  -0.0062 0.1297  109 LYS   A CE  
601  N NZ  . LYS   A 87  ? 0.4834 0.4611 0.4400 0.0577  -0.0251 0.1353  109 LYS   A NZ  
602  N N   . THR   A 88  ? 0.2091 0.2476 0.2257 0.0085  0.0285  0.0627  110 THR   A N   
603  C CA  . THR   A 88  ? 0.2222 0.2451 0.2195 0.0025  0.0181  0.0635  110 THR   A CA  
604  C C   . THR   A 88  ? 0.2099 0.2544 0.2155 -0.0058 0.0160  0.0591  110 THR   A C   
605  O O   . THR   A 88  ? 0.1910 0.2667 0.1774 -0.0095 0.0279  0.0746  110 THR   A O   
606  C CB  . THR   A 88  ? 0.2135 0.2632 0.2307 0.0032  0.0272  0.0427  110 THR   A CB  
607  O OG1 . THR   A 88  ? 0.2066 0.2699 0.2204 -0.0182 0.0528  0.0426  110 THR   A OG1 
608  C CG2 . THR   A 88  ? 0.2261 0.2692 0.2502 0.0057  0.0257  0.0416  110 THR   A CG2 
609  N N   . LEU   A 89  ? 0.2003 0.2498 0.2163 -0.0190 0.0103  0.0569  111 LEU   A N   
610  C CA  . LEU   A 89  ? 0.1877 0.2284 0.2055 -0.0253 0.0133  0.0579  111 LEU   A CA  
611  C C   . LEU   A 89  ? 0.2098 0.2267 0.2057 -0.0231 0.0246  0.0534  111 LEU   A C   
612  O O   . LEU   A 89  ? 0.2255 0.2273 0.2266 -0.0181 0.0050  0.0456  111 LEU   A O   
613  C CB  . LEU   A 89  ? 0.1676 0.2309 0.2017 -0.0200 0.0115  0.0493  111 LEU   A CB  
614  C CG  . LEU   A 89  ? 0.1715 0.2235 0.1930 -0.0188 0.0121  0.0494  111 LEU   A CG  
615  C CD1 . LEU   A 89  ? 0.1728 0.2261 0.1918 -0.0171 0.0078  0.0462  111 LEU   A CD1 
616  C CD2 . LEU   A 89  ? 0.1743 0.2224 0.1939 -0.0249 0.0076  0.0535  111 LEU   A CD2 
617  N N   . LYS   A 90  ? 0.2099 0.2380 0.1980 -0.0258 0.0246  0.0493  112 LYS   A N   
618  C CA  . LYS   A 90  ? 0.2332 0.2296 0.2045 -0.0321 0.0357  0.0436  112 LYS   A CA  
619  C C   . LYS   A 90  ? 0.2251 0.2288 0.1858 -0.0242 0.0260  0.0347  112 LYS   A C   
620  O O   . LYS   A 90  ? 0.2416 0.2383 0.1756 -0.0192 0.0345  0.0247  112 LYS   A O   
621  C CB  . LYS   A 90  ? 0.2412 0.2384 0.2104 -0.0366 0.0521  0.0500  112 LYS   A CB  
622  C CG  . LYS   A 90  ? 0.2449 0.2454 0.2122 -0.0338 0.0513  0.0630  112 LYS   A CG  
623  C CD  . LYS   A 90  ? 0.2338 0.2547 0.2355 -0.0361 0.0467  0.0731  112 LYS   A CD  
624  C CE  . LYS   A 90  ? 0.2568 0.2560 0.2604 -0.0517 0.0566  0.0656  112 LYS   A CE  
625  N NZ  . LYS   A 90  ? 0.2711 0.2648 0.2860 -0.0644 0.0408  0.0532  112 LYS   A NZ  
626  N N   . ILE   A 91  ? 0.2349 0.2140 0.1936 -0.0193 0.0345  0.0318  113 ILE   A N   
627  C CA  . ILE   A 91  ? 0.2390 0.2307 0.1946 -0.0131 0.0157  0.0294  113 ILE   A CA  
628  C C   . ILE   A 91  ? 0.2432 0.2308 0.2051 -0.0260 0.0172  0.0287  113 ILE   A C   
629  O O   . ILE   A 91  ? 0.2601 0.2463 0.1847 -0.0303 0.0095  0.0253  113 ILE   A O   
630  C CB  . ILE   A 91  ? 0.2437 0.2276 0.2086 -0.0196 0.0295  0.0218  113 ILE   A CB  
631  C CG1 . ILE   A 91  ? 0.2490 0.2230 0.2144 -0.0171 0.0280  0.0217  113 ILE   A CG1 
632  C CG2 . ILE   A 91  ? 0.2400 0.2298 0.2189 -0.0204 0.0297  0.0276  113 ILE   A CG2 
633  C CD1 . ILE   A 91  ? 0.2448 0.2149 0.2154 -0.0145 0.0233  0.0134  113 ILE   A CD1 
634  N N   . TRP   A 92  ? 0.2203 0.2421 0.1736 -0.0244 0.0070  0.0309  114 TRP   A N   
635  C CA  . TRP   A 92  ? 0.2330 0.2474 0.1783 -0.0249 0.0119  0.0338  114 TRP   A CA  
636  C C   . TRP   A 92  ? 0.2490 0.2741 0.1835 -0.0321 0.0212  0.0436  114 TRP   A C   
637  O O   . TRP   A 92  ? 0.2496 0.2821 0.2097 -0.0304 0.0351  0.0464  114 TRP   A O   
638  C CB  . TRP   A 92  ? 0.2267 0.2462 0.1874 -0.0273 0.0158  0.0369  114 TRP   A CB  
639  C CG  . TRP   A 92  ? 0.2493 0.2461 0.1938 -0.0169 0.0243  0.0392  114 TRP   A CG  
640  C CD1 . TRP   A 92  ? 0.2631 0.2589 0.1950 -0.0233 0.0238  0.0453  114 TRP   A CD1 
641  C CD2 . TRP   A 92  ? 0.2383 0.2605 0.2089 -0.0207 0.0328  0.0355  114 TRP   A CD2 
642  N NE1 . TRP   A 92  ? 0.2447 0.2552 0.1885 -0.0111 0.0257  0.0470  114 TRP   A NE1 
643  C CE2 . TRP   A 92  ? 0.2493 0.2533 0.2026 -0.0130 0.0198  0.0461  114 TRP   A CE2 
644  C CE3 . TRP   A 92  ? 0.2386 0.2575 0.2103 -0.0075 0.0164  0.0369  114 TRP   A CE3 
645  C CZ2 . TRP   A 92  ? 0.2620 0.2631 0.1920 -0.0182 0.0181  0.0480  114 TRP   A CZ2 
646  C CZ3 . TRP   A 92  ? 0.2356 0.2628 0.2070 -0.0144 0.0153  0.0437  114 TRP   A CZ3 
647  C CH2 . TRP   A 92  ? 0.2573 0.2627 0.2049 -0.0264 0.0025  0.0493  114 TRP   A CH2 
648  N N   . ASP   A 93  ? 0.2748 0.2856 0.1926 -0.0375 0.0262  0.0299  115 ASP   A N   
649  C CA  . ASP   A 93  ? 0.2786 0.3302 0.2021 -0.0380 0.0034  0.0319  115 ASP   A CA  
650  C C   . ASP   A 93  ? 0.2923 0.3285 0.2187 -0.0389 0.0127  0.0176  115 ASP   A C   
651  O O   . ASP   A 93  ? 0.2847 0.3554 0.2252 -0.0526 0.0197  0.0323  115 ASP   A O   
652  C CB  . ASP   A 93  ? 0.2975 0.3474 0.2375 -0.0331 0.0081  0.0322  115 ASP   A CB  
653  C CG  . ASP   A 93  ? 0.3408 0.3855 0.2549 -0.0289 0.0107  0.0636  115 ASP   A CG  
654  O OD1 . ASP   A 93  ? 0.3629 0.4233 0.2680 -0.0203 -0.0097 0.0917  115 ASP   A OD1 
655  O OD2 . ASP   A 93  ? 0.4190 0.4929 0.2978 -0.0200 0.0257  0.0789  115 ASP   A OD2 
656  N N   . VAL   A 94  ? 0.2773 0.3130 0.2052 -0.0311 -0.0048 0.0219  116 VAL   A N   
657  C CA  . VAL   A 94  ? 0.2919 0.3226 0.2424 -0.0161 -0.0140 0.0058  116 VAL   A CA  
658  C C   . VAL   A 94  ? 0.2573 0.3308 0.2535 -0.0303 -0.0065 0.0274  116 VAL   A C   
659  O O   . VAL   A 94  ? 0.2625 0.3666 0.2615 -0.0441 -0.0045 0.0397  116 VAL   A O   
660  C CB  . VAL   A 94  ? 0.3131 0.3244 0.3215 0.0200  -0.0277 -0.0142 116 VAL   A CB  
661  C CG1 . VAL   A 94  ? 0.3494 0.3236 0.3844 0.0360  -0.0375 -0.0308 116 VAL   A CG1 
662  C CG2 . VAL   A 94  ? 0.3267 0.3300 0.3272 0.0337  -0.0183 -0.0247 116 VAL   A CG2 
663  N N   A SER   A 95  ? 0.2625 0.3360 0.2556 -0.0387 -0.0110 0.0157  117 SER   A N   
664  N N   B SER   A 95  ? 0.2477 0.3389 0.2479 -0.0408 -0.0144 0.0239  117 SER   A N   
665  C CA  A SER   A 95  ? 0.2657 0.3807 0.2792 -0.0391 -0.0104 0.0161  117 SER   A CA  
666  C CA  B SER   A 95  ? 0.2418 0.3603 0.2545 -0.0449 -0.0132 0.0261  117 SER   A CA  
667  C C   A SER   A 95  ? 0.2629 0.3846 0.2771 -0.0477 -0.0092 0.0178  117 SER   A C   
668  C C   B SER   A 95  ? 0.2558 0.3654 0.2618 -0.0527 -0.0111 0.0247  117 SER   A C   
669  O O   A SER   A 95  ? 0.2564 0.4420 0.3225 -0.0664 -0.0110 0.0116  117 SER   A O   
670  O O   B SER   A 95  ? 0.2532 0.3908 0.2819 -0.0606 -0.0108 0.0221  117 SER   A O   
671  C CB  A SER   A 95  ? 0.3008 0.4155 0.2887 -0.0210 -0.0009 0.0043  117 SER   A CB  
672  C CB  B SER   A 95  ? 0.2363 0.3703 0.2515 -0.0399 -0.0171 0.0227  117 SER   A CB  
673  O OG  A SER   A 95  ? 0.3689 0.4358 0.3471 -0.0109 0.0082  -0.0009 117 SER   A OG  
674  O OG  B SER   A 95  ? 0.2216 0.3755 0.2513 -0.0464 -0.0181 0.0292  117 SER   A OG  
675  N N   . SER   A 96  ? 0.2776 0.3561 0.2602 -0.0565 -0.0110 0.0303  118 SER   A N   
676  C CA  . SER   A 96  ? 0.2952 0.3522 0.2708 -0.0594 -0.0111 0.0312  118 SER   A CA  
677  C C   . SER   A 96  ? 0.2934 0.3466 0.2739 -0.0742 -0.0035 0.0462  118 SER   A C   
678  O O   . SER   A 96  ? 0.3433 0.3811 0.2433 -0.1169 -0.0228 0.0589  118 SER   A O   
679  C CB  . SER   A 96  ? 0.3112 0.3421 0.2941 -0.0568 -0.0117 0.0148  118 SER   A CB  
680  O OG  . SER   A 96  ? 0.2932 0.3137 0.3035 -0.0605 -0.0103 0.0130  118 SER   A OG  
681  N N   . GLY   A 97  ? 0.2836 0.3563 0.2381 -0.0648 -0.0125 0.0646  119 GLY   A N   
682  C CA  . GLY   A 97  ? 0.2870 0.3644 0.2393 -0.0587 0.0041  0.0629  119 GLY   A CA  
683  C C   . GLY   A 97  ? 0.3011 0.3589 0.2340 -0.0646 0.0090  0.0704  119 GLY   A C   
684  O O   . GLY   A 97  ? 0.2993 0.3801 0.2444 -0.0743 0.0104  0.0950  119 GLY   A O   
685  N N   . LYS   A 98  ? 0.3525 0.3415 0.2461 -0.0509 -0.0026 0.0577  120 LYS   A N   
686  C CA  . LYS   A 98  ? 0.3482 0.3157 0.2779 -0.0601 -0.0138 0.0561  120 LYS   A CA  
687  C C   . LYS   A 98  ? 0.3242 0.2626 0.2608 -0.0482 0.0005  0.0559  120 LYS   A C   
688  O O   . LYS   A 98  ? 0.3112 0.2643 0.2498 -0.0517 -0.0185 0.0587  120 LYS   A O   
689  C CB  . LYS   A 98  ? 0.4114 0.3492 0.3372 -0.0632 -0.0269 0.0343  120 LYS   A CB  
690  C CG  . LYS   A 98  ? 0.4493 0.4026 0.4142 -0.0719 -0.0706 0.0089  120 LYS   A CG  
691  C CD  . LYS   A 98  ? 0.5123 0.4343 0.4828 -0.0873 -0.0821 -0.0235 120 LYS   A CD  
692  C CE  . LYS   A 98  ? 0.4815 0.4700 0.5648 -0.1313 -0.1012 -0.0348 120 LYS   A CE  
693  N N   . CYS   A 99  ? 0.2855 0.2442 0.2611 -0.0357 0.0145  0.0539  121 CYS   A N   
694  C CA  . CYS   A 99  ? 0.2880 0.2445 0.2765 -0.0248 0.0146  0.0518  121 CYS   A CA  
695  C C   . CYS   A 99  ? 0.3121 0.2295 0.2935 -0.0141 0.0038  0.0341  121 CYS   A C   
696  O O   . CYS   A 99  ? 0.3537 0.2131 0.3335 -0.0376 0.0275  0.0195  121 CYS   A O   
697  C CB  . CYS   A 99  ? 0.2896 0.2788 0.2906 -0.0170 0.0165  0.0554  121 CYS   A CB  
698  S SG  . CYS   A 99  ? 0.2852 0.2948 0.3073 0.0006  0.0174  0.0464  121 CYS   A SG  
699  N N   . LEU   A 100 ? 0.2995 0.2278 0.2738 -0.0065 0.0051  0.0360  122 LEU   A N   
700  C CA  . LEU   A 100 ? 0.3153 0.2621 0.2709 -0.0052 0.0047  0.0293  122 LEU   A CA  
701  C C   . LEU   A 100 ? 0.3381 0.2621 0.2761 0.0112  -0.0010 0.0142  122 LEU   A C   
702  O O   . LEU   A 100 ? 0.3830 0.2845 0.2501 0.0223  -0.0132 -0.0140 122 LEU   A O   
703  C CB  . LEU   A 100 ? 0.3141 0.2750 0.2831 -0.0065 0.0128  0.0378  122 LEU   A CB  
704  C CG  . LEU   A 100 ? 0.3144 0.2840 0.2615 -0.0037 0.0221  0.0492  122 LEU   A CG  
705  C CD1 . LEU   A 100 ? 0.3185 0.3043 0.2370 -0.0044 0.0338  0.0525  122 LEU   A CD1 
706  C CD2 . LEU   A 100 ? 0.3176 0.3045 0.2941 0.0157  0.0193  0.0380  122 LEU   A CD2 
707  N N   . LYS   A 101 ? 0.3214 0.2507 0.2570 0.0115  0.0059  0.0271  123 LYS   A N   
708  C CA  . LYS   A 101 ? 0.3207 0.2572 0.2664 -0.0055 0.0027  0.0326  123 LYS   A CA  
709  C C   . LYS   A 101 ? 0.2911 0.2422 0.2636 -0.0067 0.0012  0.0333  123 LYS   A C   
710  O O   . LYS   A 101 ? 0.2760 0.2587 0.2467 0.0009  -0.0087 0.0391  123 LYS   A O   
711  C CB  . LYS   A 101 ? 0.3352 0.2748 0.2620 -0.0110 0.0191  0.0481  123 LYS   A CB  
712  C CG  . LYS   A 101 ? 0.3880 0.3360 0.2809 -0.0030 0.0324  0.0554  123 LYS   A CG  
713  C CD  . LYS   A 101 ? 0.4234 0.3811 0.3148 0.0104  0.0453  0.0365  123 LYS   A CD  
714  C CE  . LYS   A 101 ? 0.4447 0.4707 0.3337 -0.0142 0.0518  0.0555  123 LYS   A CE  
715  N NZ  . LYS   A 101 ? 0.5093 0.5152 0.3706 -0.0232 0.0685  0.0192  123 LYS   A NZ  
716  N N   . THR   A 102 ? 0.2800 0.2345 0.2772 0.0056  0.0133  0.0361  124 THR   A N   
717  C CA  . THR   A 102 ? 0.2601 0.2491 0.2663 -0.0040 0.0251  0.0468  124 THR   A CA  
718  C C   . THR   A 102 ? 0.2647 0.2700 0.2580 0.0137  0.0297  0.0397  124 THR   A C   
719  O O   . THR   A 102 ? 0.2968 0.2994 0.2604 0.0368  0.0236  0.0323  124 THR   A O   
720  C CB  . THR   A 102 ? 0.2493 0.2658 0.2865 -0.0103 0.0288  0.0542  124 THR   A CB  
721  O OG1 . THR   A 102 ? 0.2120 0.2598 0.3076 -0.0371 0.0444  0.0632  124 THR   A OG1 
722  C CG2 . THR   A 102 ? 0.2412 0.2643 0.2807 -0.0142 0.0328  0.0616  124 THR   A CG2 
723  N N   . LEU   A 103 ? 0.2505 0.2767 0.2341 0.0137  0.0367  0.0426  125 LEU   A N   
724  C CA  . LEU   A 103 ? 0.2441 0.2749 0.2134 0.0027  0.0309  0.0487  125 LEU   A CA  
725  C C   . LEU   A 103 ? 0.2417 0.2509 0.2255 0.0015  0.0326  0.0549  125 LEU   A C   
726  O O   . LEU   A 103 ? 0.2146 0.2330 0.2365 -0.0161 0.0281  0.0541  125 LEU   A O   
727  C CB  . LEU   A 103 ? 0.2542 0.2836 0.2128 0.0068  0.0393  0.0603  125 LEU   A CB  
728  C CG  . LEU   A 103 ? 0.2907 0.3162 0.2353 0.0053  0.0517  0.0688  125 LEU   A CG  
729  C CD1 . LEU   A 103 ? 0.2568 0.3099 0.2166 -0.0011 0.0584  0.0558  125 LEU   A CD1 
730  C CD2 . LEU   A 103 ? 0.3132 0.3344 0.2644 0.0127  0.0690  0.0564  125 LEU   A CD2 
731  N N   . LYS   A 104 ? 0.2620 0.2244 0.2440 0.0038  0.0274  0.0457  126 LYS   A N   
732  C CA  . LYS   A 104 ? 0.2524 0.2366 0.2590 0.0135  0.0217  0.0471  126 LYS   A CA  
733  C C   . LYS   A 104 ? 0.2585 0.2706 0.2649 0.0174  0.0254  0.0426  126 LYS   A C   
734  O O   . LYS   A 104 ? 0.2531 0.2944 0.2705 0.0255  0.0303  0.0257  126 LYS   A O   
735  C CB  . LYS   A 104 ? 0.3029 0.2454 0.3053 -0.0026 -0.0006 0.0555  126 LYS   A CB  
736  C CG  . LYS   A 104 ? 0.3266 0.2635 0.3710 -0.0046 -0.0317 0.0545  126 LYS   A CG  
737  C CD  . LYS   A 104 ? 0.3708 0.2935 0.4413 -0.0284 -0.0532 0.0335  126 LYS   A CD  
738  C CE  . LYS   A 104 ? 0.3987 0.4028 0.4812 -0.0333 -0.0703 0.0233  126 LYS   A CE  
739  N N   . GLY   A 105 ? 0.2271 0.2775 0.2633 0.0229  0.0336  0.0347  127 GLY   A N   
740  C CA  . GLY   A 105 ? 0.2193 0.2972 0.2718 0.0161  0.0164  0.0547  127 GLY   A CA  
741  C C   . GLY   A 105 ? 0.2044 0.2962 0.2628 0.0177  0.0110  0.0587  127 GLY   A C   
742  O O   . GLY   A 105 ? 0.1840 0.3151 0.2930 0.0550  -0.0043 0.0779  127 GLY   A O   
743  N N   . HIS   A 106 ? 0.1976 0.2690 0.2569 -0.0144 0.0168  0.0675  128 HIS   A N   
744  C CA  . HIS   A 106 ? 0.1928 0.2607 0.2515 -0.0150 0.0258  0.0804  128 HIS   A CA  
745  C C   . HIS   A 106 ? 0.2040 0.2681 0.2384 -0.0063 0.0140  0.0933  128 HIS   A C   
746  O O   . HIS   A 106 ? 0.2153 0.2678 0.2303 0.0050  0.0211  0.1056  128 HIS   A O   
747  C CB  . HIS   A 106 ? 0.1795 0.2482 0.2572 -0.0227 0.0206  0.0697  128 HIS   A CB  
748  C CG  . HIS   A 106 ? 0.1785 0.2370 0.2500 -0.0120 0.0144  0.0725  128 HIS   A CG  
749  N ND1 . HIS   A 106 ? 0.1649 0.2156 0.2508 -0.0138 0.0280  0.0668  128 HIS   A ND1 
750  C CD2 . HIS   A 106 ? 0.1636 0.2264 0.2574 -0.0167 0.0216  0.0702  128 HIS   A CD2 
751  C CE1 . HIS   A 106 ? 0.1635 0.2340 0.2565 -0.0098 0.0187  0.0744  128 HIS   A CE1 
752  N NE2 . HIS   A 106 ? 0.1539 0.2202 0.2485 -0.0067 0.0280  0.0697  128 HIS   A NE2 
753  N N   . SER   A 107 ? 0.1956 0.2670 0.2334 -0.0047 0.0001  0.1047  129 SER   A N   
754  C CA  . SER   A 107 ? 0.2257 0.3109 0.2330 -0.0019 0.0014  0.1052  129 SER   A CA  
755  C C   . SER   A 107 ? 0.2298 0.3239 0.2172 0.0072  0.0177  0.1216  129 SER   A C   
756  O O   . SER   A 107 ? 0.2260 0.3268 0.2408 0.0071  0.0542  0.1332  129 SER   A O   
757  C CB  . SER   A 107 ? 0.2366 0.3062 0.2430 -0.0039 -0.0082 0.1093  129 SER   A CB  
758  O OG  . SER   A 107 ? 0.1986 0.3067 0.2359 -0.0149 -0.0224 0.0924  129 SER   A OG  
759  N N   . ASN   A 108 ? 0.2383 0.3061 0.2266 0.0070  0.0193  0.1070  130 ASN   A N   
760  C CA  . ASN   A 108 ? 0.2291 0.3131 0.2322 0.0121  0.0095  0.1134  130 ASN   A CA  
761  C C   . ASN   A 108 ? 0.2124 0.2962 0.2250 -0.0007 0.0106  0.1030  130 ASN   A C   
762  O O   . ASN   A 108 ? 0.2268 0.2927 0.2212 0.0011  -0.0030 0.0814  130 ASN   A O   
763  C CB  . ASN   A 108 ? 0.2308 0.3234 0.2097 0.0254  0.0169  0.1132  130 ASN   A CB  
764  C CG  . ASN   A 108 ? 0.2452 0.3760 0.2195 0.0469  0.0059  0.0985  130 ASN   A CG  
765  O OD1 . ASN   A 108 ? 0.2308 0.4091 0.2299 0.0280  0.0313  0.0999  130 ASN   A OD1 
766  N ND2 . ASN   A 108 ? 0.2613 0.4023 0.2345 0.0816  -0.0151 0.0752  130 ASN   A ND2 
767  N N   . TYR   A 109 ? 0.1933 0.2939 0.2320 -0.0051 0.0056  0.0899  131 TYR   A N   
768  C CA  . TYR   A 109 ? 0.2003 0.3191 0.2103 0.0056  0.0297  0.0955  131 TYR   A CA  
769  C C   . TYR   A 109 ? 0.1816 0.2971 0.1927 0.0120  0.0299  0.0851  131 TYR   A C   
770  O O   . TYR   A 109 ? 0.1840 0.2677 0.1781 0.0128  0.0427  0.0755  131 TYR   A O   
771  C CB  . TYR   A 109 ? 0.1968 0.3550 0.2144 0.0093  0.0469  0.0842  131 TYR   A CB  
772  C CG  . TYR   A 109 ? 0.1940 0.3976 0.2413 0.0033  0.0607  0.0941  131 TYR   A CG  
773  C CD1 . TYR   A 109 ? 0.2000 0.4131 0.2488 -0.0061 0.0686  0.0963  131 TYR   A CD1 
774  C CD2 . TYR   A 109 ? 0.2546 0.4407 0.2717 -0.0151 0.0866  0.0797  131 TYR   A CD2 
775  C CE1 . TYR   A 109 ? 0.2388 0.4588 0.2740 -0.0147 0.0882  0.1005  131 TYR   A CE1 
776  C CE2 . TYR   A 109 ? 0.2911 0.4805 0.3150 -0.0269 0.1245  0.0775  131 TYR   A CE2 
777  C CZ  . TYR   A 109 ? 0.3071 0.4818 0.3095 -0.0274 0.1090  0.0861  131 TYR   A CZ  
778  O OH  . TYR   A 109 ? 0.3756 0.5985 0.3859 -0.0474 0.1723  0.0897  131 TYR   A OH  
779  N N   . VAL   A 110 ? 0.1735 0.2868 0.1922 0.0110  0.0244  0.0818  132 VAL   A N   
780  C CA  . VAL   A 110 ? 0.1693 0.2668 0.1768 0.0159  0.0160  0.0827  132 VAL   A CA  
781  C C   . VAL   A 110 ? 0.1628 0.2684 0.1692 0.0109  0.0243  0.0726  132 VAL   A C   
782  O O   . VAL   A 110 ? 0.1579 0.2875 0.1805 -0.0030 0.0233  0.0607  132 VAL   A O   
783  C CB  . VAL   A 110 ? 0.1856 0.2573 0.1785 0.0143  0.0145  0.0767  132 VAL   A CB  
784  C CG1 . VAL   A 110 ? 0.1883 0.2717 0.1819 0.0066  0.0162  0.0679  132 VAL   A CG1 
785  C CG2 . VAL   A 110 ? 0.1909 0.2747 0.2085 0.0134  0.0128  0.0716  132 VAL   A CG2 
786  N N   . PHE   A 111 ? 0.1620 0.2546 0.1665 0.0092  0.0291  0.0846  133 PHE   A N   
787  C CA  . PHE   A 111 ? 0.1716 0.2771 0.1777 0.0103  0.0396  0.0725  133 PHE   A CA  
788  C C   . PHE   A 111 ? 0.1656 0.2782 0.1799 0.0153  0.0361  0.0771  133 PHE   A C   
789  O O   . PHE   A 111 ? 0.1770 0.2841 0.1903 0.0152  0.0476  0.0882  133 PHE   A O   
790  C CB  . PHE   A 111 ? 0.1973 0.2972 0.2038 0.0056  0.0422  0.0591  133 PHE   A CB  
791  C CG  . PHE   A 111 ? 0.1941 0.3273 0.2461 0.0058  0.0492  0.0459  133 PHE   A CG  
792  C CD1 . PHE   A 111 ? 0.2122 0.3448 0.2733 -0.0174 0.0639  0.0416  133 PHE   A CD1 
793  C CD2 . PHE   A 111 ? 0.2160 0.3289 0.2684 -0.0054 0.0697  0.0439  133 PHE   A CD2 
794  C CE1 . PHE   A 111 ? 0.2062 0.3431 0.3048 -0.0041 0.0564  0.0464  133 PHE   A CE1 
795  C CE2 . PHE   A 111 ? 0.2149 0.3417 0.2987 -0.0024 0.0574  0.0349  133 PHE   A CE2 
796  C CZ  . PHE   A 111 ? 0.2162 0.3457 0.3045 -0.0061 0.0584  0.0403  133 PHE   A CZ  
797  N N   . CYS   A 112 ? 0.1584 0.2687 0.1740 0.0139  0.0266  0.0754  134 CYS   A N   
798  C CA  . CYS   A 112 ? 0.1633 0.2540 0.1842 -0.0013 0.0335  0.0617  134 CYS   A CA  
799  C C   . CYS   A 112 ? 0.1572 0.2409 0.1679 -0.0042 0.0226  0.0577  134 CYS   A C   
800  O O   . CYS   A 112 ? 0.1595 0.2525 0.1766 -0.0046 0.0219  0.0564  134 CYS   A O   
801  C CB  . CYS   A 112 ? 0.1751 0.2598 0.1846 0.0002  0.0264  0.0458  134 CYS   A CB  
802  S SG  . CYS   A 112 ? 0.1821 0.2595 0.1816 0.0002  0.0229  0.0268  134 CYS   A SG  
803  N N   . CYS   A 113 ? 0.1489 0.2369 0.1611 0.0002  0.0175  0.0551  135 CYS   A N   
804  C CA  . CYS   A 113 ? 0.1518 0.2392 0.1786 -0.0043 0.0241  0.0531  135 CYS   A CA  
805  C C   . CYS   A 113 ? 0.1633 0.2395 0.1721 -0.0053 0.0204  0.0549  135 CYS   A C   
806  O O   . CYS   A 113 ? 0.1804 0.2412 0.1737 -0.0092 0.0225  0.0525  135 CYS   A O   
807  C CB  . CYS   A 113 ? 0.1777 0.2440 0.1704 -0.0031 0.0131  0.0410  135 CYS   A CB  
808  S SG  . CYS   A 113 ? 0.1760 0.2553 0.1809 -0.0187 0.0109  0.0281  135 CYS   A SG  
809  N N   . ASN   A 114 ? 0.1610 0.2388 0.1856 -0.0174 0.0195  0.0509  136 ASN   A N   
810  C CA  . ASN   A 114 ? 0.1806 0.2537 0.1816 -0.0214 0.0126  0.0514  136 ASN   A CA  
811  C C   . ASN   A 114 ? 0.1864 0.2522 0.1881 -0.0243 0.0156  0.0508  136 ASN   A C   
812  O O   . ASN   A 114 ? 0.2001 0.2363 0.2004 -0.0178 0.0181  0.0542  136 ASN   A O   
813  C CB  . ASN   A 114 ? 0.2031 0.2554 0.1875 -0.0233 0.0142  0.0590  136 ASN   A CB  
814  C CG  . ASN   A 114 ? 0.2102 0.2675 0.1889 -0.0237 0.0105  0.0603  136 ASN   A CG  
815  O OD1 . ASN   A 114 ? 0.2630 0.2863 0.1787 -0.0157 -0.0166 0.0504  136 ASN   A OD1 
816  N ND2 . ASN   A 114 ? 0.2194 0.2681 0.1850 -0.0224 0.0025  0.0677  136 ASN   A ND2 
817  N N   . PHE   A 115 ? 0.1998 0.2534 0.1885 -0.0333 0.0305  0.0605  137 PHE   A N   
818  C CA  . PHE   A 115 ? 0.1999 0.2510 0.1806 -0.0260 0.0301  0.0651  137 PHE   A CA  
819  C C   . PHE   A 115 ? 0.1960 0.2506 0.1962 -0.0265 0.0322  0.0528  137 PHE   A C   
820  O O   . PHE   A 115 ? 0.1833 0.2488 0.2211 -0.0077 0.0356  0.0623  137 PHE   A O   
821  C CB  . PHE   A 115 ? 0.1953 0.2838 0.1750 -0.0207 0.0386  0.0592  137 PHE   A CB  
822  C CG  . PHE   A 115 ? 0.1899 0.2879 0.1595 -0.0109 0.0349  0.0473  137 PHE   A CG  
823  C CD1 . PHE   A 115 ? 0.1850 0.2857 0.1412 -0.0100 0.0342  0.0461  137 PHE   A CD1 
824  C CD2 . PHE   A 115 ? 0.1890 0.2979 0.1675 -0.0040 0.0433  0.0490  137 PHE   A CD2 
825  C CE1 . PHE   A 115 ? 0.1846 0.2895 0.1401 -0.0024 0.0348  0.0451  137 PHE   A CE1 
826  C CE2 . PHE   A 115 ? 0.1940 0.2934 0.1594 -0.0004 0.0368  0.0465  137 PHE   A CE2 
827  C CZ  . PHE   A 115 ? 0.1829 0.2846 0.1609 0.0019  0.0277  0.0480  137 PHE   A CZ  
828  N N   . ASN   A 116 ? 0.2037 0.2410 0.2225 -0.0353 0.0439  0.0511  138 ASN   A N   
829  C CA  . ASN   A 116 ? 0.1998 0.2490 0.2081 -0.0392 0.0497  0.0597  138 ASN   A CA  
830  C C   . ASN   A 116 ? 0.2218 0.2737 0.2133 -0.0487 0.0336  0.0584  138 ASN   A C   
831  O O   . ASN   A 116 ? 0.1972 0.3142 0.2139 -0.0518 0.0241  0.0647  138 ASN   A O   
832  C CB  . ASN   A 116 ? 0.2024 0.2384 0.2078 -0.0370 0.0607  0.0581  138 ASN   A CB  
833  C CG  . ASN   A 116 ? 0.1825 0.2630 0.2141 -0.0222 0.0699  0.0463  138 ASN   A CG  
834  O OD1 . ASN   A 116 ? 0.1789 0.2622 0.2152 -0.0188 0.0630  0.0501  138 ASN   A OD1 
835  N ND2 . ASN   A 116 ? 0.1871 0.2847 0.2375 -0.0126 0.0831  0.0161  138 ASN   A ND2 
836  N N   . PRO   A 117 ? 0.2464 0.2884 0.2253 -0.0494 0.0291  0.0717  139 PRO   A N   
837  C CA  . PRO   A 117 ? 0.2632 0.2941 0.2344 -0.0365 0.0222  0.0786  139 PRO   A CA  
838  C C   . PRO   A 117 ? 0.2606 0.3149 0.2166 -0.0349 0.0151  0.0761  139 PRO   A C   
839  O O   . PRO   A 117 ? 0.2762 0.3401 0.1964 -0.0456 0.0104  0.0899  139 PRO   A O   
840  C CB  . PRO   A 117 ? 0.2613 0.2911 0.2492 -0.0359 0.0210  0.0766  139 PRO   A CB  
841  C CG  . PRO   A 117 ? 0.2557 0.2910 0.2404 -0.0423 0.0245  0.0813  139 PRO   A CG  
842  C CD  . PRO   A 117 ? 0.2504 0.2926 0.2240 -0.0511 0.0270  0.0756  139 PRO   A CD  
843  N N   . GLN   A 118 ? 0.2489 0.3124 0.2018 -0.0287 0.0267  0.0647  140 GLN   A N   
844  C CA  . GLN   A 118 ? 0.2520 0.3338 0.1882 -0.0185 0.0228  0.0630  140 GLN   A CA  
845  C C   . GLN   A 118 ? 0.2430 0.3361 0.1806 -0.0236 0.0156  0.0609  140 GLN   A C   
846  O O   . GLN   A 118 ? 0.2967 0.3380 0.1847 -0.0188 0.0451  0.0615  140 GLN   A O   
847  C CB  . GLN   A 118 ? 0.2456 0.3505 0.2059 -0.0151 0.0233  0.0532  140 GLN   A CB  
848  C CG  . GLN   A 118 ? 0.2554 0.3757 0.2401 -0.0185 0.0205  0.0370  140 GLN   A CG  
849  C CD  . GLN   A 118 ? 0.2655 0.3888 0.2503 -0.0189 0.0394  0.0291  140 GLN   A CD  
850  O OE1 . GLN   A 118 ? 0.3006 0.4306 0.3306 -0.0246 0.0295  0.0110  140 GLN   A OE1 
851  N NE2 . GLN   A 118 ? 0.2837 0.4140 0.2796 -0.0225 0.0447  0.0118  140 GLN   A NE2 
852  N N   . SER   A 119 ? 0.2172 0.3319 0.1934 -0.0265 0.0261  0.0606  141 SER   A N   
853  C CA  . SER   A 119 ? 0.2212 0.2988 0.1909 -0.0286 0.0073  0.0547  141 SER   A CA  
854  C C   . SER   A 119 ? 0.2239 0.3012 0.1977 -0.0221 0.0185  0.0559  141 SER   A C   
855  O O   . SER   A 119 ? 0.2565 0.2940 0.2006 -0.0206 0.0158  0.0436  141 SER   A O   
856  C CB  . SER   A 119 ? 0.2157 0.2911 0.1980 -0.0280 0.0076  0.0564  141 SER   A CB  
857  O OG  . SER   A 119 ? 0.2067 0.2827 0.1957 -0.0357 0.0114  0.0467  141 SER   A OG  
858  N N   . ASN   A 120 ? 0.2156 0.2862 0.1949 -0.0272 0.0291  0.0675  142 ASN   A N   
859  C CA  . ASN   A 120 ? 0.2187 0.3104 0.2164 -0.0231 0.0381  0.0631  142 ASN   A CA  
860  C C   . ASN   A 120 ? 0.2159 0.2716 0.2127 -0.0094 0.0416  0.0616  142 ASN   A C   
861  O O   . ASN   A 120 ? 0.2348 0.2542 0.2034 -0.0050 0.0672  0.0584  142 ASN   A O   
862  C CB  . ASN   A 120 ? 0.2159 0.3378 0.1976 -0.0286 0.0358  0.0643  142 ASN   A CB  
863  C CG  . ASN   A 120 ? 0.2148 0.3571 0.2345 -0.0384 0.0402  0.0697  142 ASN   A CG  
864  O OD1 . ASN   A 120 ? 0.2043 0.3911 0.2254 -0.0533 0.0563  0.0547  142 ASN   A OD1 
865  N ND2 . ASN   A 120 ? 0.2313 0.3655 0.2597 -0.0276 0.0194  0.0775  142 ASN   A ND2 
866  N N   . LEU   A 121 ? 0.2237 0.2696 0.2171 -0.0093 0.0457  0.0671  143 LEU   A N   
867  C CA  . LEU   A 121 ? 0.1910 0.2527 0.2176 -0.0049 0.0454  0.0818  143 LEU   A CA  
868  C C   . LEU   A 121 ? 0.1869 0.2505 0.2065 -0.0156 0.0491  0.0729  143 LEU   A C   
869  O O   . LEU   A 121 ? 0.1579 0.2474 0.2139 -0.0158 0.0528  0.0688  143 LEU   A O   
870  C CB  . LEU   A 121 ? 0.1995 0.2734 0.2102 -0.0062 0.0439  0.0833  143 LEU   A CB  
871  C CG  . LEU   A 121 ? 0.1862 0.2917 0.2218 -0.0175 0.0388  0.0898  143 LEU   A CG  
872  C CD1 . LEU   A 121 ? 0.2159 0.2921 0.2479 -0.0345 0.0412  0.0916  143 LEU   A CD1 
873  C CD2 . LEU   A 121 ? 0.1937 0.2983 0.2237 -0.0272 0.0446  0.0787  143 LEU   A CD2 
874  N N   . ILE   A 122 ? 0.1926 0.2574 0.2108 -0.0131 0.0582  0.0693  144 ILE   A N   
875  C CA  . ILE   A 122 ? 0.1737 0.2503 0.2038 -0.0017 0.0465  0.0630  144 ILE   A CA  
876  C C   . ILE   A 122 ? 0.1538 0.2512 0.1902 0.0018  0.0522  0.0738  144 ILE   A C   
877  O O   . ILE   A 122 ? 0.1585 0.2727 0.1808 0.0222  0.0506  0.0627  144 ILE   A O   
878  C CB  . ILE   A 122 ? 0.1744 0.2665 0.2018 -0.0033 0.0463  0.0564  144 ILE   A CB  
879  C CG1 . ILE   A 122 ? 0.1862 0.2637 0.1861 0.0010  0.0425  0.0521  144 ILE   A CG1 
880  C CG2 . ILE   A 122 ? 0.1698 0.2685 0.1996 -0.0193 0.0469  0.0604  144 ILE   A CG2 
881  C CD1 . ILE   A 122 ? 0.1823 0.2681 0.1871 -0.0017 0.0536  0.0592  144 ILE   A CD1 
882  N N   . VAL   A 123 ? 0.1482 0.2447 0.1888 -0.0010 0.0305  0.0640  145 VAL   A N   
883  C CA  . VAL   A 123 ? 0.1383 0.2668 0.1887 0.0059  0.0238  0.0619  145 VAL   A CA  
884  C C   . VAL   A 123 ? 0.1395 0.2604 0.1943 -0.0008 0.0277  0.0529  145 VAL   A C   
885  O O   . VAL   A 123 ? 0.1445 0.2642 0.1748 0.0050  0.0309  0.0569  145 VAL   A O   
886  C CB  . VAL   A 123 ? 0.1357 0.2751 0.1927 0.0062  0.0146  0.0649  145 VAL   A CB  
887  C CG1 . VAL   A 123 ? 0.1285 0.2848 0.1950 0.0010  0.0096  0.0661  145 VAL   A CG1 
888  C CG2 . VAL   A 123 ? 0.1453 0.2933 0.2045 0.0138  0.0115  0.0691  145 VAL   A CG2 
889  N N   . SER   A 124 ? 0.1297 0.2635 0.1782 -0.0037 0.0361  0.0441  146 SER   A N   
890  C CA  . SER   A 124 ? 0.1317 0.2666 0.1920 -0.0067 0.0397  0.0500  146 SER   A CA  
891  C C   . SER   A 124 ? 0.1536 0.2739 0.1884 -0.0141 0.0398  0.0520  146 SER   A C   
892  O O   . SER   A 124 ? 0.1687 0.2615 0.1801 -0.0152 0.0309  0.0588  146 SER   A O   
893  C CB  . SER   A 124 ? 0.1298 0.2596 0.2133 -0.0061 0.0365  0.0493  146 SER   A CB  
894  O OG  . SER   A 124 ? 0.1627 0.2317 0.2139 -0.0049 0.0235  0.0525  146 SER   A OG  
895  N N   . GLY   A 125 ? 0.1468 0.2876 0.1853 -0.0090 0.0321  0.0439  147 GLY   A N   
896  C CA  . GLY   A 125 ? 0.1661 0.2937 0.1923 -0.0133 0.0318  0.0464  147 GLY   A CA  
897  C C   . GLY   A 125 ? 0.1764 0.2893 0.1795 -0.0085 0.0235  0.0567  147 GLY   A C   
898  O O   . GLY   A 125 ? 0.1867 0.2808 0.1980 -0.0255 0.0217  0.0613  147 GLY   A O   
899  N N   . SER   A 126 ? 0.1752 0.2832 0.1696 -0.0009 0.0182  0.0518  148 SER   A N   
900  C CA  . SER   A 126 ? 0.1566 0.3019 0.1784 -0.0033 0.0218  0.0562  148 SER   A CA  
901  C C   . SER   A 126 ? 0.1489 0.3016 0.1785 -0.0046 0.0160  0.0573  148 SER   A C   
902  O O   . SER   A 126 ? 0.1623 0.2849 0.1824 -0.0033 0.0233  0.0398  148 SER   A O   
903  C CB  . SER   A 126 ? 0.1633 0.2915 0.1739 -0.0008 0.0158  0.0607  148 SER   A CB  
904  O OG  . SER   A 126 ? 0.1492 0.3096 0.1796 0.0040  0.0405  0.0661  148 SER   A OG  
905  N N   . PHE   A 127 ? 0.1655 0.3191 0.1657 -0.0028 0.0206  0.0700  149 PHE   A N   
906  C CA  . PHE   A 127 ? 0.1751 0.3385 0.1746 -0.0026 0.0140  0.0686  149 PHE   A CA  
907  C C   . PHE   A 127 ? 0.1653 0.3383 0.1594 -0.0184 0.0047  0.0691  149 PHE   A C   
908  O O   . PHE   A 127 ? 0.1821 0.3584 0.1626 -0.0047 0.0060  0.0507  149 PHE   A O   
909  C CB  . PHE   A 127 ? 0.1793 0.3459 0.1953 -0.0041 0.0134  0.0706  149 PHE   A CB  
910  C CG  . PHE   A 127 ? 0.2343 0.3759 0.2436 0.0168  0.0241  0.0507  149 PHE   A CG  
911  C CD1 . PHE   A 127 ? 0.2796 0.3907 0.2582 0.0400  0.0239  0.0521  149 PHE   A CD1 
912  C CD2 . PHE   A 127 ? 0.2832 0.4186 0.3074 0.0456  0.0205  0.0110  149 PHE   A CD2 
913  C CE1 . PHE   A 127 ? 0.3199 0.3789 0.2707 0.0592  0.0249  0.0613  149 PHE   A CE1 
914  C CE2 . PHE   A 127 ? 0.3051 0.4168 0.3315 0.0531  0.0217  0.0166  149 PHE   A CE2 
915  C CZ  . PHE   A 127 ? 0.3131 0.3806 0.2963 0.0513  0.0379  0.0345  149 PHE   A CZ  
916  N N   . ASP   A 128 ? 0.1728 0.3329 0.1766 -0.0239 -0.0016 0.0691  150 ASP   A N   
917  C CA  . ASP   A 128 ? 0.1950 0.3299 0.1771 -0.0162 -0.0068 0.0719  150 ASP   A CA  
918  C C   . ASP   A 128 ? 0.1887 0.3452 0.1930 -0.0064 -0.0170 0.0688  150 ASP   A C   
919  O O   . ASP   A 128 ? 0.1707 0.3401 0.2242 -0.0107 -0.0280 0.0766  150 ASP   A O   
920  C CB  . ASP   A 128 ? 0.1915 0.3188 0.1837 -0.0168 -0.0041 0.0749  150 ASP   A CB  
921  C CG  . ASP   A 128 ? 0.1675 0.2874 0.1810 -0.0300 0.0028  0.0685  150 ASP   A CG  
922  O OD1 . ASP   A 128 ? 0.1691 0.2949 0.1720 -0.0392 0.0164  0.0659  150 ASP   A OD1 
923  O OD2 . ASP   A 128 ? 0.1715 0.2781 0.2255 -0.0331 0.0072  0.0707  150 ASP   A OD2 
924  N N   . GLU   A 129 ? 0.1976 0.3483 0.1884 0.0009  -0.0229 0.0576  151 GLU   A N   
925  C CA  . GLU   A 129 ? 0.1998 0.3330 0.1889 0.0000  -0.0019 0.0523  151 GLU   A CA  
926  C C   . GLU   A 129 ? 0.2010 0.3202 0.2004 -0.0058 0.0012  0.0533  151 GLU   A C   
927  O O   . GLU   A 129 ? 0.1902 0.3201 0.2163 -0.0136 0.0191  0.0268  151 GLU   A O   
928  C CB  . GLU   A 129 ? 0.2160 0.3380 0.1834 -0.0063 -0.0013 0.0716  151 GLU   A CB  
929  C CG  . GLU   A 129 ? 0.2064 0.3527 0.1897 -0.0014 -0.0020 0.0645  151 GLU   A CG  
930  C CD  . GLU   A 129 ? 0.2308 0.3482 0.1927 -0.0009 -0.0083 0.0740  151 GLU   A CD  
931  O OE1 . GLU   A 129 ? 0.2389 0.3701 0.2181 -0.0116 -0.0153 0.0761  151 GLU   A OE1 
932  O OE2 . GLU   A 129 ? 0.2452 0.3604 0.2059 0.0042  -0.0054 0.1024  151 GLU   A OE2 
933  N N   . SER   A 130 ? 0.1859 0.2937 0.2028 0.0015  0.0095  0.0467  152 SER   A N   
934  C CA  . SER   A 130 ? 0.1943 0.3051 0.2178 0.0099  0.0078  0.0487  152 SER   A CA  
935  C C   . SER   A 130 ? 0.1882 0.3071 0.2075 0.0038  0.0221  0.0560  152 SER   A C   
936  O O   . SER   A 130 ? 0.1911 0.3006 0.2138 0.0056  0.0116  0.0417  152 SER   A O   
937  C CB  . SER   A 130 ? 0.2207 0.3043 0.2442 0.0082  0.0001  0.0503  152 SER   A CB  
938  O OG  . SER   A 130 ? 0.2244 0.2959 0.2386 -0.0028 -0.0084 0.0664  152 SER   A OG  
939  N N   . VAL   A 131 ? 0.1813 0.3309 0.2179 -0.0024 0.0195  0.0576  153 VAL   A N   
940  C CA  . VAL   A 131 ? 0.1654 0.2998 0.2167 0.0128  0.0237  0.0717  153 VAL   A CA  
941  C C   . VAL   A 131 ? 0.1528 0.3007 0.2045 0.0131  0.0281  0.0698  153 VAL   A C   
942  O O   . VAL   A 131 ? 0.1461 0.2927 0.2102 0.0224  0.0358  0.0526  153 VAL   A O   
943  C CB  . VAL   A 131 ? 0.1746 0.3060 0.2168 0.0099  0.0349  0.0776  153 VAL   A CB  
944  C CG1 . VAL   A 131 ? 0.1631 0.3123 0.2111 0.0171  0.0156  0.0743  153 VAL   A CG1 
945  C CG2 . VAL   A 131 ? 0.1771 0.2889 0.2038 -0.0042 0.0371  0.0875  153 VAL   A CG2 
946  N N   . ARG   A 132 ? 0.1619 0.2945 0.2255 -0.0046 0.0328  0.0705  154 ARG   A N   
947  C CA  A ARG   A 132 ? 0.1791 0.2970 0.2178 -0.0037 0.0298  0.0737  154 ARG   A CA  
948  C CA  B ARG   A 132 ? 0.1796 0.2881 0.2278 -0.0003 0.0330  0.0753  154 ARG   A CA  
949  C C   . ARG   A 132 ? 0.1766 0.2905 0.2236 0.0020  0.0352  0.0722  154 ARG   A C   
950  O O   . ARG   A 132 ? 0.1782 0.2777 0.1962 0.0032  0.0430  0.0679  154 ARG   A O   
951  C CB  A ARG   A 132 ? 0.1968 0.3059 0.2155 -0.0147 0.0241  0.0804  154 ARG   A CB  
952  C CB  B ARG   A 132 ? 0.1997 0.2864 0.2506 -0.0056 0.0333  0.0792  154 ARG   A CB  
953  C CG  A ARG   A 132 ? 0.2059 0.3195 0.2206 -0.0157 0.0190  0.0858  154 ARG   A CG  
954  C CG  B ARG   A 132 ? 0.2082 0.2854 0.2777 -0.0005 0.0330  0.0860  154 ARG   A CG  
955  C CD  A ARG   A 132 ? 0.2082 0.3321 0.2102 -0.0256 0.0194  0.0864  154 ARG   A CD  
956  C CD  B ARG   A 132 ? 0.2159 0.2876 0.2913 -0.0043 0.0409  0.0846  154 ARG   A CD  
957  N NE  A ARG   A 132 ? 0.2121 0.3347 0.2225 -0.0289 0.0099  0.0868  154 ARG   A NE  
958  N NE  B ARG   A 132 ? 0.2316 0.2715 0.3340 -0.0020 0.0451  0.0827  154 ARG   A NE  
959  C CZ  A ARG   A 132 ? 0.2070 0.3373 0.2195 -0.0325 0.0087  0.0836  154 ARG   A CZ  
960  C CZ  B ARG   A 132 ? 0.2136 0.2611 0.3483 -0.0013 0.0411  0.0793  154 ARG   A CZ  
961  N NH1 A ARG   A 132 ? 0.2159 0.3454 0.2075 -0.0379 0.0189  0.0892  154 ARG   A NH1 
962  N NH1 B ARG   A 132 ? 0.1882 0.2620 0.3816 0.0018  0.0476  0.0691  154 ARG   A NH1 
963  N NH2 A ARG   A 132 ? 0.1992 0.3449 0.2162 -0.0304 0.0048  0.0794  154 ARG   A NH2 
964  N NH2 B ARG   A 132 ? 0.2241 0.2574 0.3564 0.0031  0.0458  0.0792  154 ARG   A NH2 
965  N N   . ILE   A 133 ? 0.1914 0.2888 0.2164 0.0134  0.0406  0.0672  155 ILE   A N   
966  C CA  . ILE   A 133 ? 0.1774 0.2797 0.2203 0.0014  0.0473  0.0682  155 ILE   A CA  
967  C C   . ILE   A 133 ? 0.1788 0.2822 0.2284 0.0076  0.0426  0.0714  155 ILE   A C   
968  O O   . ILE   A 133 ? 0.1771 0.2879 0.2556 0.0142  0.0382  0.0637  155 ILE   A O   
969  C CB  . ILE   A 133 ? 0.1724 0.2965 0.2445 0.0057  0.0524  0.0652  155 ILE   A CB  
970  C CG1 . ILE   A 133 ? 0.1618 0.2834 0.2706 -0.0126 0.0513  0.0650  155 ILE   A CG1 
971  C CG2 . ILE   A 133 ? 0.1727 0.3085 0.2341 -0.0024 0.0877  0.0637  155 ILE   A CG2 
972  C CD1 . ILE   A 133 ? 0.1710 0.3010 0.3096 -0.0250 0.0378  0.0569  155 ILE   A CD1 
973  N N   . TRP   A 134 ? 0.1765 0.2684 0.1941 0.0076  0.0396  0.0540  156 TRP   A N   
974  C CA  . TRP   A 134 ? 0.1925 0.2760 0.2049 0.0072  0.0391  0.0525  156 TRP   A CA  
975  C C   . TRP   A 134 ? 0.2112 0.2754 0.2085 0.0086  0.0453  0.0407  156 TRP   A C   
976  O O   . TRP   A 134 ? 0.1893 0.2774 0.1908 0.0128  0.0644  0.0429  156 TRP   A O   
977  C CB  . TRP   A 134 ? 0.1937 0.2720 0.2186 0.0127  0.0307  0.0497  156 TRP   A CB  
978  C CG  . TRP   A 134 ? 0.2006 0.2608 0.2217 0.0221  0.0314  0.0456  156 TRP   A CG  
979  C CD1 . TRP   A 134 ? 0.2062 0.2503 0.2139 0.0090  0.0300  0.0424  156 TRP   A CD1 
980  C CD2 . TRP   A 134 ? 0.2026 0.2553 0.2012 0.0120  0.0323  0.0486  156 TRP   A CD2 
981  N NE1 . TRP   A 134 ? 0.1908 0.2402 0.2005 0.0203  0.0310  0.0441  156 TRP   A NE1 
982  C CE2 . TRP   A 134 ? 0.2056 0.2539 0.2066 0.0165  0.0339  0.0437  156 TRP   A CE2 
983  C CE3 . TRP   A 134 ? 0.2191 0.2602 0.2066 0.0297  0.0337  0.0464  156 TRP   A CE3 
984  C CZ2 . TRP   A 134 ? 0.2251 0.2581 0.1996 0.0202  0.0267  0.0518  156 TRP   A CZ2 
985  C CZ3 . TRP   A 134 ? 0.2090 0.2592 0.1975 0.0186  0.0313  0.0389  156 TRP   A CZ3 
986  C CH2 . TRP   A 134 ? 0.1983 0.2638 0.2004 0.0200  0.0331  0.0440  156 TRP   A CH2 
987  N N   . ASP   A 135 ? 0.2345 0.2697 0.2316 0.0125  0.0442  0.0344  157 ASP   A N   
988  C CA  . ASP   A 135 ? 0.2717 0.2925 0.2352 0.0064  0.0493  0.0251  157 ASP   A CA  
989  C C   . ASP   A 135 ? 0.2628 0.2697 0.2345 0.0135  0.0465  0.0318  157 ASP   A C   
990  O O   . ASP   A 135 ? 0.2828 0.2408 0.2366 0.0118  0.0285  0.0123  157 ASP   A O   
991  C CB  . ASP   A 135 ? 0.2909 0.3297 0.2588 0.0147  0.0605  0.0183  157 ASP   A CB  
992  C CG  . ASP   A 135 ? 0.3560 0.3747 0.2612 -0.0149 0.0760  0.0128  157 ASP   A CG  
993  O OD1 . ASP   A 135 ? 0.3913 0.4356 0.3371 -0.0307 0.0942  -0.0048 157 ASP   A OD1 
994  O OD2 . ASP   A 135 ? 0.4325 0.4172 0.2684 -0.0595 0.0781  0.0072  157 ASP   A OD2 
995  N N   . VAL   A 136 ? 0.2663 0.2682 0.2056 0.0163  0.0483  0.0393  158 VAL   A N   
996  C CA  . VAL   A 136 ? 0.2504 0.2618 0.2256 0.0174  0.0601  0.0309  158 VAL   A CA  
997  C C   . VAL   A 136 ? 0.2782 0.2729 0.2497 0.0241  0.0577  0.0123  158 VAL   A C   
998  O O   . VAL   A 136 ? 0.2780 0.2585 0.2683 0.0205  0.0465  -0.0170 158 VAL   A O   
999  C CB  . VAL   A 136 ? 0.2183 0.2641 0.2280 0.0215  0.0518  0.0317  158 VAL   A CB  
1000 C CG1 . VAL   A 136 ? 0.2071 0.2626 0.2451 0.0194  0.0586  0.0346  158 VAL   A CG1 
1001 C CG2 . VAL   A 136 ? 0.1968 0.2519 0.2299 0.0218  0.0672  0.0348  158 VAL   A CG2 
1002 N N   . LYS   A 137 ? 0.3007 0.2960 0.2600 0.0312  0.0584  0.0000  159 LYS   A N   
1003 C CA  . LYS   A 137 ? 0.3589 0.3097 0.2784 0.0273  0.0739  -0.0162 159 LYS   A CA  
1004 C C   . LYS   A 137 ? 0.3807 0.3186 0.2888 0.0236  0.0695  -0.0180 159 LYS   A C   
1005 O O   . LYS   A 137 ? 0.3856 0.3115 0.3002 0.0035  0.0566  -0.0422 159 LYS   A O   
1006 C CB  . LYS   A 137 ? 0.3775 0.3667 0.3072 0.0145  0.0918  -0.0205 159 LYS   A CB  
1007 C CG  . LYS   A 137 ? 0.4370 0.4268 0.3749 -0.0010 0.0758  -0.0644 159 LYS   A CG  
1008 N N   . THR   A 138 ? 0.3915 0.3295 0.2677 0.0462  0.0590  -0.0123 160 THR   A N   
1009 C CA  . THR   A 138 ? 0.4227 0.2926 0.2817 0.0378  0.0648  -0.0143 160 THR   A CA  
1010 C C   . THR   A 138 ? 0.4137 0.2653 0.2972 0.0309  0.0456  0.0123  160 THR   A C   
1011 O O   . THR   A 138 ? 0.4770 0.2590 0.3505 -0.0075 0.0241  0.0154  160 THR   A O   
1012 C CB  . THR   A 138 ? 0.4308 0.2961 0.3142 0.0512  0.0615  -0.0028 160 THR   A CB  
1013 O OG1 . THR   A 138 ? 0.4521 0.2883 0.3435 0.0488  0.0602  -0.0007 160 THR   A OG1 
1014 C CG2 . THR   A 138 ? 0.4414 0.3205 0.3571 0.0581  0.0661  -0.0052 160 THR   A CG2 
1015 N N   . GLY   A 139 ? 0.3933 0.2340 0.2627 0.0399  0.0354  0.0157  161 GLY   A N   
1016 C CA  . GLY   A 139 ? 0.3855 0.2742 0.2972 0.0397  0.0344  0.0195  161 GLY   A CA  
1017 C C   . GLY   A 139 ? 0.3888 0.2844 0.3144 0.0587  0.0347  0.0355  161 GLY   A C   
1018 O O   . GLY   A 139 ? 0.4066 0.3413 0.3262 0.0570  0.0667  0.0622  161 GLY   A O   
1019 N N   . LYS   A 140 ? 0.3597 0.2880 0.3195 0.0633  0.0080  0.0281  162 LYS   A N   
1020 C CA  . LYS   A 140 ? 0.3709 0.3040 0.3204 0.0522  -0.0098 0.0296  162 LYS   A CA  
1021 C C   . LYS   A 140 ? 0.2988 0.3218 0.2968 0.0385  -0.0075 0.0384  162 LYS   A C   
1022 O O   . LYS   A 140 ? 0.2644 0.3196 0.2899 0.0627  -0.0208 0.0234  162 LYS   A O   
1023 C CB  . LYS   A 140 ? 0.3766 0.3074 0.3608 0.0606  -0.0320 0.0303  162 LYS   A CB  
1024 C CG  . LYS   A 140 ? 0.4346 0.3176 0.3939 0.0323  -0.0476 0.0369  162 LYS   A CG  
1025 N N   . CYS   A 141 ? 0.2653 0.3029 0.2773 0.0282  0.0241  0.0486  163 CYS   A N   
1026 C CA  . CYS   A 141 ? 0.2276 0.2999 0.2706 0.0294  0.0280  0.0463  163 CYS   A CA  
1027 C C   . CYS   A 141 ? 0.2300 0.2965 0.2967 0.0470  0.0410  0.0497  163 CYS   A C   
1028 O O   . CYS   A 141 ? 0.2607 0.2725 0.3542 0.0493  0.0607  0.0573  163 CYS   A O   
1029 C CB  . CYS   A 141 ? 0.2127 0.3034 0.2732 0.0242  0.0263  0.0450  163 CYS   A CB  
1030 S SG  . CYS   A 141 ? 0.2724 0.3467 0.2687 0.0281  0.0302  0.0254  163 CYS   A SG  
1031 N N   . LEU   A 142 ? 0.2244 0.3052 0.2895 0.0385  0.0330  0.0465  164 LEU   A N   
1032 C CA  . LEU   A 142 ? 0.2266 0.3246 0.2919 0.0413  0.0392  0.0468  164 LEU   A CA  
1033 C C   . LEU   A 142 ? 0.2043 0.3235 0.3060 0.0348  0.0402  0.0515  164 LEU   A C   
1034 O O   . LEU   A 142 ? 0.2307 0.3251 0.3808 0.0724  0.0479  0.0414  164 LEU   A O   
1035 C CB  . LEU   A 142 ? 0.2205 0.3513 0.2873 0.0422  0.0347  0.0548  164 LEU   A CB  
1036 C CG  . LEU   A 142 ? 0.2479 0.3934 0.3022 0.0464  0.0267  0.0465  164 LEU   A CG  
1037 C CD1 . LEU   A 142 ? 0.2657 0.4072 0.3023 0.0445  0.0183  0.0621  164 LEU   A CD1 
1038 C CD2 . LEU   A 142 ? 0.2811 0.4279 0.3407 0.0541  0.0140  0.0145  164 LEU   A CD2 
1039 N N   . LYS   A 143 ? 0.2048 0.3253 0.2949 0.0271  0.0330  0.0539  165 LYS   A N   
1040 C CA  . LYS   A 143 ? 0.2193 0.3526 0.2782 0.0144  0.0463  0.0430  165 LYS   A CA  
1041 C C   . LYS   A 143 ? 0.2008 0.3478 0.2733 0.0051  0.0488  0.0612  165 LYS   A C   
1042 O O   . LYS   A 143 ? 0.2168 0.3250 0.2611 -0.0010 0.0231  0.0496  165 LYS   A O   
1043 C CB  . LYS   A 143 ? 0.2157 0.3639 0.2875 -0.0033 0.0570  0.0329  165 LYS   A CB  
1044 C CG  . LYS   A 143 ? 0.2498 0.3916 0.3172 -0.0319 0.0808  0.0211  165 LYS   A CG  
1045 C CD  . LYS   A 143 ? 0.2918 0.4097 0.3634 -0.0663 0.0884  0.0045  165 LYS   A CD  
1046 C CE  . LYS   A 143 ? 0.3270 0.4252 0.3766 -0.0672 0.1080  0.0016  165 LYS   A CE  
1047 N NZ  . LYS   A 143 ? 0.3583 0.4314 0.3925 -0.0820 0.1010  -0.0066 165 LYS   A NZ  
1048 N N   . THR   A 144 ? 0.1989 0.3676 0.2768 0.0173  0.0352  0.0569  166 THR   A N   
1049 C CA  . THR   A 144 ? 0.2150 0.3667 0.2718 0.0101  0.0340  0.0675  166 THR   A CA  
1050 C C   . THR   A 144 ? 0.1746 0.3649 0.2809 0.0129  0.0251  0.0701  166 THR   A C   
1051 O O   . THR   A 144 ? 0.1698 0.3484 0.2887 0.0252  0.0157  0.0706  166 THR   A O   
1052 C CB  . THR   A 144 ? 0.2328 0.3781 0.2909 0.0090  0.0251  0.0712  166 THR   A CB  
1053 O OG1 . THR   A 144 ? 0.2608 0.3922 0.3085 0.0048  0.0311  0.0565  166 THR   A OG1 
1054 C CG2 . THR   A 144 ? 0.2156 0.3714 0.2788 0.0180  0.0195  0.0638  166 THR   A CG2 
1055 N N   . LEU   A 145 ? 0.1546 0.3539 0.2651 0.0107  0.0293  0.0564  167 LEU   A N   
1056 C CA  . LEU   A 145 ? 0.1712 0.3693 0.2680 -0.0055 0.0199  0.0623  167 LEU   A CA  
1057 C C   . LEU   A 145 ? 0.1970 0.3495 0.2512 0.0016  0.0144  0.0806  167 LEU   A C   
1058 O O   . LEU   A 145 ? 0.2010 0.3542 0.2402 0.0441  -0.0110 0.1023  167 LEU   A O   
1059 C CB  . LEU   A 145 ? 0.1773 0.3715 0.2726 0.0070  0.0116  0.0536  167 LEU   A CB  
1060 C CG  . LEU   A 145 ? 0.2012 0.4050 0.2970 -0.0214 0.0177  0.0578  167 LEU   A CG  
1061 C CD1 . LEU   A 145 ? 0.1818 0.4100 0.2961 -0.0421 0.0097  0.0537  167 LEU   A CD1 
1062 C CD2 . LEU   A 145 ? 0.2253 0.4319 0.3161 -0.0113 0.0318  0.0589  167 LEU   A CD2 
1063 N N   . PRO   A 146 ? 0.2178 0.3811 0.2642 -0.0011 0.0011  0.0730  168 PRO   A N   
1064 C CA  . PRO   A 146 ? 0.2387 0.3764 0.2751 -0.0004 -0.0059 0.0711  168 PRO   A CA  
1065 C C   . PRO   A 146 ? 0.2124 0.3872 0.2600 -0.0167 -0.0246 0.0586  168 PRO   A C   
1066 O O   . PRO   A 146 ? 0.2429 0.3989 0.2478 -0.0077 -0.0496 0.0617  168 PRO   A O   
1067 C CB  . PRO   A 146 ? 0.2502 0.4143 0.3023 -0.0016 -0.0093 0.0636  168 PRO   A CB  
1068 C CG  . PRO   A 146 ? 0.2655 0.4217 0.3018 0.0126  0.0007  0.0569  168 PRO   A CG  
1069 C CD  . PRO   A 146 ? 0.2420 0.4119 0.2785 0.0062  0.0044  0.0599  168 PRO   A CD  
1070 N N   . ALA   A 147 ? 0.1915 0.3562 0.2466 -0.0253 -0.0102 0.0620  169 ALA   A N   
1071 C CA  . ALA   A 147 ? 0.1894 0.3557 0.2089 -0.0099 -0.0087 0.0532  169 ALA   A CA  
1072 C C   . ALA   A 147 ? 0.2020 0.3303 0.1988 -0.0135 -0.0204 0.0630  169 ALA   A C   
1073 O O   . ALA   A 147 ? 0.2096 0.3527 0.1947 -0.0423 -0.0340 0.0699  169 ALA   A O   
1074 C CB  . ALA   A 147 ? 0.2176 0.3713 0.1827 -0.0033 -0.0142 0.0380  169 ALA   A CB  
1075 N N   . HIS   A 148 ? 0.1988 0.3027 0.2119 -0.0100 -0.0103 0.0573  170 HIS   A N   
1076 C CA  . HIS   A 148 ? 0.2079 0.3085 0.2008 -0.0071 -0.0182 0.0587  170 HIS   A CA  
1077 C C   . HIS   A 148 ? 0.2259 0.3112 0.1970 -0.0110 -0.0139 0.0571  170 HIS   A C   
1078 O O   . HIS   A 148 ? 0.2310 0.3087 0.1924 -0.0338 0.0019  0.0355  170 HIS   A O   
1079 C CB  . HIS   A 148 ? 0.1974 0.2955 0.2131 -0.0080 -0.0165 0.0603  170 HIS   A CB  
1080 C CG  . HIS   A 148 ? 0.1927 0.2906 0.2253 -0.0051 -0.0109 0.0645  170 HIS   A CG  
1081 N ND1 . HIS   A 148 ? 0.2105 0.2817 0.2399 0.0000  -0.0069 0.0719  170 HIS   A ND1 
1082 C CD2 . HIS   A 148 ? 0.1947 0.2954 0.2339 -0.0140 -0.0021 0.0706  170 HIS   A CD2 
1083 C CE1 . HIS   A 148 ? 0.2182 0.3028 0.2230 -0.0080 -0.0063 0.0718  170 HIS   A CE1 
1084 N NE2 . HIS   A 148 ? 0.2047 0.3033 0.2302 -0.0126 -0.0013 0.0628  170 HIS   A NE2 
1085 N N   . SER   A 149 ? 0.2341 0.3287 0.1977 -0.0071 -0.0108 0.0506  171 SER   A N   
1086 C CA  . SER   A 149 ? 0.2460 0.3460 0.1988 0.0035  -0.0216 0.0620  171 SER   A CA  
1087 C C   . SER   A 149 ? 0.2387 0.3300 0.1924 0.0093  -0.0124 0.0601  171 SER   A C   
1088 O O   . SER   A 149 ? 0.2492 0.3524 0.1962 0.0236  -0.0121 0.0378  171 SER   A O   
1089 C CB  . SER   A 149 ? 0.2590 0.3609 0.2093 0.0011  -0.0165 0.0489  171 SER   A CB  
1090 O OG  . SER   A 149 ? 0.2418 0.3652 0.2052 0.0307  -0.0134 0.0601  171 SER   A OG  
1091 N N   . ASP   A 150 ? 0.2409 0.3505 0.1773 0.0140  -0.0041 0.0627  172 ASP   A N   
1092 C CA  . ASP   A 150 ? 0.2428 0.3548 0.1758 0.0226  0.0015  0.0584  172 ASP   A CA  
1093 C C   . ASP   A 150 ? 0.2218 0.3448 0.1857 0.0175  0.0035  0.0541  172 ASP   A C   
1094 O O   . ASP   A 150 ? 0.1868 0.3342 0.1694 0.0183  -0.0142 0.0367  172 ASP   A O   
1095 C CB  . ASP   A 150 ? 0.2683 0.3605 0.2261 0.0302  0.0034  0.0616  172 ASP   A CB  
1096 C CG  . ASP   A 150 ? 0.2930 0.3962 0.2436 0.0406  0.0135  0.0680  172 ASP   A CG  
1097 O OD1 . ASP   A 150 ? 0.3111 0.4109 0.2732 0.0639  0.0514  0.0967  172 ASP   A OD1 
1098 O OD2 . ASP   A 150 ? 0.3403 0.4275 0.2439 0.0517  0.0095  0.0247  172 ASP   A OD2 
1099 N N   . PRO   A 151 ? 0.2167 0.3313 0.1838 0.0178  0.0171  0.0592  173 PRO   A N   
1100 C CA  . PRO   A 151 ? 0.2168 0.3083 0.1872 0.0127  0.0161  0.0714  173 PRO   A CA  
1101 C C   . PRO   A 151 ? 0.2221 0.2997 0.1847 0.0148  0.0023  0.0637  173 PRO   A C   
1102 O O   . PRO   A 151 ? 0.2465 0.3073 0.1779 0.0223  0.0024  0.0658  173 PRO   A O   
1103 C CB  . PRO   A 151 ? 0.2146 0.3141 0.1938 0.0192  0.0132  0.0710  173 PRO   A CB  
1104 C CG  . PRO   A 151 ? 0.2164 0.3188 0.2009 0.0092  0.0198  0.0791  173 PRO   A CG  
1105 C CD  . PRO   A 151 ? 0.2286 0.3261 0.1957 0.0106  0.0232  0.0675  173 PRO   A CD  
1106 N N   . VAL   A 152 ? 0.2006 0.2821 0.1724 0.0137  -0.0022 0.0571  174 VAL   A N   
1107 C CA  . VAL   A 152 ? 0.1934 0.2837 0.1800 0.0084  -0.0061 0.0587  174 VAL   A CA  
1108 C C   . VAL   A 152 ? 0.1850 0.2839 0.1806 0.0065  -0.0060 0.0467  174 VAL   A C   
1109 O O   . VAL   A 152 ? 0.1935 0.2980 0.2077 -0.0179 -0.0131 0.0516  174 VAL   A O   
1110 C CB  . VAL   A 152 ? 0.1862 0.2785 0.1854 0.0128  -0.0203 0.0615  174 VAL   A CB  
1111 C CG1 . VAL   A 152 ? 0.1832 0.2656 0.1917 -0.0018 -0.0265 0.0622  174 VAL   A CG1 
1112 C CG2 . VAL   A 152 ? 0.1889 0.2840 0.2086 0.0141  -0.0257 0.0637  174 VAL   A CG2 
1113 N N   . SER   A 153 ? 0.1786 0.2834 0.1842 0.0080  0.0097  0.0497  175 SER   A N   
1114 C CA  . SER   A 153 ? 0.1818 0.2761 0.1842 0.0131  -0.0006 0.0476  175 SER   A CA  
1115 C C   . SER   A 153 ? 0.1649 0.2696 0.1744 0.0193  0.0125  0.0393  175 SER   A C   
1116 O O   . SER   A 153 ? 0.1569 0.2746 0.1874 0.0152  0.0077  0.0429  175 SER   A O   
1117 C CB  . SER   A 153 ? 0.1926 0.2755 0.1927 0.0104  0.0018  0.0459  175 SER   A CB  
1118 O OG  . SER   A 153 ? 0.2011 0.2834 0.2244 0.0025  0.0036  0.0345  175 SER   A OG  
1119 N N   . ALA   A 154 ? 0.1639 0.2728 0.1786 0.0236  0.0105  0.0316  176 ALA   A N   
1120 C CA  . ALA   A 154 ? 0.1641 0.2544 0.1770 0.0243  0.0357  0.0401  176 ALA   A CA  
1121 C C   . ALA   A 154 ? 0.1475 0.2690 0.1711 0.0149  0.0252  0.0361  176 ALA   A C   
1122 O O   . ALA   A 154 ? 0.1668 0.2641 0.1477 0.0099  0.0101  0.0400  176 ALA   A O   
1123 C CB  . ALA   A 154 ? 0.1592 0.2503 0.1764 0.0276  0.0395  0.0355  176 ALA   A CB  
1124 N N   . VAL   A 155 ? 0.1512 0.2776 0.1736 0.0094  0.0170  0.0375  177 VAL   A N   
1125 C CA  . VAL   A 155 ? 0.1522 0.2824 0.1697 -0.0040 0.0211  0.0328  177 VAL   A CA  
1126 C C   . VAL   A 155 ? 0.1579 0.2793 0.1744 -0.0097 0.0218  0.0493  177 VAL   A C   
1127 O O   . VAL   A 155 ? 0.1935 0.2861 0.1597 -0.0258 0.0177  0.0577  177 VAL   A O   
1128 C CB  . VAL   A 155 ? 0.1732 0.2892 0.1814 -0.0043 0.0181  0.0265  177 VAL   A CB  
1129 C CG1 . VAL   A 155 ? 0.1915 0.3060 0.1676 -0.0004 0.0227  0.0148  177 VAL   A CG1 
1130 C CG2 . VAL   A 155 ? 0.1938 0.2895 0.1537 -0.0042 0.0129  0.0162  177 VAL   A CG2 
1131 N N   . HIS   A 156 ? 0.1565 0.2869 0.1828 -0.0140 0.0139  0.0504  178 HIS   A N   
1132 C CA  . HIS   A 156 ? 0.1578 0.2764 0.1957 -0.0248 0.0152  0.0579  178 HIS   A CA  
1133 C C   . HIS   A 156 ? 0.1577 0.2927 0.2018 -0.0274 0.0132  0.0585  178 HIS   A C   
1134 O O   . HIS   A 156 ? 0.1442 0.3308 0.2228 -0.0118 0.0048  0.0594  178 HIS   A O   
1135 C CB  . HIS   A 156 ? 0.1637 0.2734 0.2057 -0.0293 0.0136  0.0566  178 HIS   A CB  
1136 C CG  . HIS   A 156 ? 0.1915 0.2624 0.2159 -0.0392 0.0098  0.0664  178 HIS   A CG  
1137 N ND1 . HIS   A 156 ? 0.2233 0.2797 0.2328 -0.0416 0.0184  0.0729  178 HIS   A ND1 
1138 C CD2 . HIS   A 156 ? 0.1883 0.2716 0.2325 -0.0406 0.0094  0.0775  178 HIS   A CD2 
1139 C CE1 . HIS   A 156 ? 0.2433 0.2546 0.2625 -0.0477 -0.0054 0.0752  178 HIS   A CE1 
1140 N NE2 . HIS   A 156 ? 0.2077 0.2560 0.2677 -0.0528 -0.0004 0.0839  178 HIS   A NE2 
1141 N N   . PHE   A 157 ? 0.1664 0.2933 0.1992 -0.0336 0.0192  0.0476  179 PHE   A N   
1142 C CA  . PHE   A 157 ? 0.1830 0.2931 0.1988 -0.0395 0.0214  0.0571  179 PHE   A CA  
1143 C C   . PHE   A 157 ? 0.1912 0.3031 0.2192 -0.0399 0.0323  0.0647  179 PHE   A C   
1144 O O   . PHE   A 157 ? 0.1898 0.3254 0.2435 -0.0331 0.0317  0.0806  179 PHE   A O   
1145 C CB  . PHE   A 157 ? 0.1972 0.2839 0.2014 -0.0371 0.0312  0.0526  179 PHE   A CB  
1146 C CG  . PHE   A 157 ? 0.2013 0.2623 0.1931 -0.0505 0.0300  0.0508  179 PHE   A CG  
1147 C CD1 . PHE   A 157 ? 0.2030 0.2523 0.1983 -0.0526 0.0279  0.0403  179 PHE   A CD1 
1148 C CD2 . PHE   A 157 ? 0.2067 0.2691 0.1712 -0.0541 0.0319  0.0472  179 PHE   A CD2 
1149 C CE1 . PHE   A 157 ? 0.2108 0.2568 0.1771 -0.0505 0.0324  0.0623  179 PHE   A CE1 
1150 C CE2 . PHE   A 157 ? 0.1993 0.2603 0.1584 -0.0565 0.0330  0.0576  179 PHE   A CE2 
1151 C CZ  . PHE   A 157 ? 0.2033 0.2640 0.1749 -0.0536 0.0257  0.0548  179 PHE   A CZ  
1152 N N   . ASN   A 158 ? 0.1973 0.2898 0.2023 -0.0430 0.0402  0.0640  180 ASN   A N   
1153 C CA  . ASN   A 158 ? 0.1999 0.2977 0.2163 -0.0435 0.0464  0.0674  180 ASN   A CA  
1154 C C   . ASN   A 158 ? 0.2184 0.3091 0.2252 -0.0278 0.0463  0.0694  180 ASN   A C   
1155 O O   . ASN   A 158 ? 0.2036 0.3057 0.2023 -0.0275 0.0588  0.0748  180 ASN   A O   
1156 C CB  . ASN   A 158 ? 0.2097 0.3096 0.2335 -0.0464 0.0398  0.0642  180 ASN   A CB  
1157 C CG  . ASN   A 158 ? 0.2040 0.3087 0.2403 -0.0453 0.0423  0.0596  180 ASN   A CG  
1158 O OD1 . ASN   A 158 ? 0.2030 0.2833 0.2334 -0.0360 0.0471  0.0842  180 ASN   A OD1 
1159 N ND2 . ASN   A 158 ? 0.2230 0.3203 0.2713 -0.0439 0.0284  0.0509  180 ASN   A ND2 
1160 N N   . ARG   A 159 ? 0.2417 0.3162 0.2422 -0.0150 0.0642  0.0825  181 ARG   A N   
1161 C CA  . ARG   A 159 ? 0.2921 0.3351 0.2559 -0.0127 0.0597  0.0783  181 ARG   A CA  
1162 C C   . ARG   A 159 ? 0.2774 0.3399 0.2647 -0.0089 0.0620  0.0874  181 ARG   A C   
1163 O O   . ARG   A 159 ? 0.3210 0.3362 0.2200 0.0042  0.0581  0.0782  181 ARG   A O   
1164 C CB  . ARG   A 159 ? 0.3843 0.3476 0.3152 0.0092  0.0590  0.1060  181 ARG   A CB  
1165 C CG  . ARG   A 159 ? 0.4805 0.3759 0.3486 -0.0016 0.0551  0.0965  181 ARG   A CG  
1166 C CD  . ARG   A 159 ? 0.5454 0.3523 0.3932 0.0171  0.0662  0.1150  181 ARG   A CD  
1167 N NE  . ARG   A 159 ? 0.6439 0.3713 0.4261 -0.0143 0.0655  0.1240  181 ARG   A NE  
1168 C CZ  . ARG   A 159 ? 0.7180 0.4346 0.4595 -0.0544 0.0788  0.1016  181 ARG   A CZ  
1169 N NH1 . ARG   A 159 ? 0.7201 0.5153 0.4655 -0.0805 0.0569  0.0739  181 ARG   A NH1 
1170 N NH2 . ARG   A 159 ? 0.7912 0.4047 0.4062 -0.0417 0.0901  0.1349  181 ARG   A NH2 
1171 N N   . ASP   A 160 ? 0.2535 0.3353 0.2420 0.0015  0.0664  0.0961  182 ASP   A N   
1172 C CA  . ASP   A 160 ? 0.2380 0.3382 0.2453 -0.0157 0.0840  0.0975  182 ASP   A CA  
1173 C C   . ASP   A 160 ? 0.2287 0.3278 0.2389 -0.0013 0.0656  0.0877  182 ASP   A C   
1174 O O   . ASP   A 160 ? 0.2785 0.3531 0.2492 0.0077  0.0699  0.0776  182 ASP   A O   
1175 C CB  . ASP   A 160 ? 0.2379 0.3572 0.2636 -0.0284 0.0895  0.1021  182 ASP   A CB  
1176 C CG  . ASP   A 160 ? 0.2323 0.3719 0.2582 -0.0500 0.1030  0.1020  182 ASP   A CG  
1177 O OD1 . ASP   A 160 ? 0.2550 0.3519 0.2564 -0.0730 0.0972  0.0804  182 ASP   A OD1 
1178 O OD2 . ASP   A 160 ? 0.2330 0.4048 0.3095 -0.0640 0.1317  0.0926  182 ASP   A OD2 
1179 N N   . GLY   A 161 ? 0.1987 0.3061 0.2367 -0.0067 0.0602  0.0878  183 GLY   A N   
1180 C CA  . GLY   A 161 ? 0.1974 0.2902 0.2548 0.0031  0.0455  0.0833  183 GLY   A CA  
1181 C C   . GLY   A 161 ? 0.2002 0.2972 0.2610 -0.0103 0.0428  0.0864  183 GLY   A C   
1182 O O   . GLY   A 161 ? 0.1995 0.2910 0.2435 -0.0100 0.0164  0.1021  183 GLY   A O   
1183 N N   . SER   A 162 ? 0.1898 0.3247 0.2739 -0.0183 0.0462  0.0865  184 SER   A N   
1184 C CA  . SER   A 162 ? 0.1835 0.3055 0.2604 -0.0205 0.0449  0.0892  184 SER   A CA  
1185 C C   . SER   A 162 ? 0.1788 0.3035 0.2607 -0.0284 0.0486  0.1010  184 SER   A C   
1186 O O   . SER   A 162 ? 0.1873 0.3250 0.2558 -0.0257 0.0552  0.1197  184 SER   A O   
1187 C CB  . SER   A 162 ? 0.2078 0.3045 0.2663 -0.0211 0.0578  0.0955  184 SER   A CB  
1188 O OG  . SER   A 162 ? 0.2235 0.2856 0.2874 -0.0551 0.0497  0.0843  184 SER   A OG  
1189 N N   . LEU   A 163 ? 0.1793 0.3218 0.2425 -0.0258 0.0359  0.0934  185 LEU   A N   
1190 C CA  . LEU   A 163 ? 0.1849 0.3150 0.2421 -0.0454 0.0275  0.0898  185 LEU   A CA  
1191 C C   . LEU   A 163 ? 0.1738 0.3138 0.2318 -0.0469 0.0192  0.0709  185 LEU   A C   
1192 O O   . LEU   A 163 ? 0.1953 0.3291 0.2335 -0.0622 0.0180  0.0747  185 LEU   A O   
1193 C CB  . LEU   A 163 ? 0.1978 0.3267 0.2621 -0.0611 0.0247  0.0929  185 LEU   A CB  
1194 C CG  . LEU   A 163 ? 0.2024 0.3457 0.2888 -0.0637 0.0438  0.0963  185 LEU   A CG  
1195 C CD1 . LEU   A 163 ? 0.2161 0.3434 0.2799 -0.0921 0.0525  0.0958  185 LEU   A CD1 
1196 C CD2 . LEU   A 163 ? 0.1993 0.3715 0.3024 -0.0663 0.0344  0.0964  185 LEU   A CD2 
1197 N N   . ILE   A 164 ? 0.1608 0.3147 0.2369 -0.0537 0.0043  0.0659  186 ILE   A N   
1198 C CA  . ILE   A 164 ? 0.1731 0.3162 0.2217 -0.0394 0.0116  0.0552  186 ILE   A CA  
1199 C C   . ILE   A 164 ? 0.1864 0.2934 0.2295 -0.0405 0.0155  0.0507  186 ILE   A C   
1200 O O   . ILE   A 164 ? 0.2126 0.2934 0.2231 -0.0344 -0.0025 0.0531  186 ILE   A O   
1201 C CB  . ILE   A 164 ? 0.1555 0.3048 0.2241 -0.0455 0.0068  0.0501  186 ILE   A CB  
1202 C CG1 . ILE   A 164 ? 0.1560 0.3181 0.2113 -0.0388 0.0228  0.0577  186 ILE   A CG1 
1203 C CG2 . ILE   A 164 ? 0.1573 0.2962 0.2136 -0.0374 0.0069  0.0373  186 ILE   A CG2 
1204 C CD1 . ILE   A 164 ? 0.1569 0.3251 0.2089 -0.0335 0.0156  0.0665  186 ILE   A CD1 
1205 N N   . VAL   A 165 ? 0.1827 0.2999 0.2129 -0.0302 0.0160  0.0525  187 VAL   A N   
1206 C CA  . VAL   A 165 ? 0.1841 0.2883 0.2166 -0.0312 0.0168  0.0441  187 VAL   A CA  
1207 C C   . VAL   A 165 ? 0.1908 0.2866 0.2047 -0.0342 0.0123  0.0477  187 VAL   A C   
1208 O O   . VAL   A 165 ? 0.1984 0.2999 0.1633 -0.0256 0.0038  0.0578  187 VAL   A O   
1209 C CB  . VAL   A 165 ? 0.2096 0.3028 0.2332 -0.0276 0.0142  0.0349  187 VAL   A CB  
1210 C CG1 . VAL   A 165 ? 0.2247 0.3097 0.2495 -0.0170 0.0090  0.0323  187 VAL   A CG1 
1211 C CG2 . VAL   A 165 ? 0.2110 0.3007 0.2398 -0.0245 -0.0074 0.0304  187 VAL   A CG2 
1212 N N   . SER   A 166 ? 0.1761 0.2933 0.2018 -0.0464 0.0075  0.0381  188 SER   A N   
1213 C CA  . SER   A 166 ? 0.1975 0.2882 0.2017 -0.0427 -0.0009 0.0491  188 SER   A CA  
1214 C C   . SER   A 166 ? 0.2027 0.2867 0.2096 -0.0348 0.0006  0.0445  188 SER   A C   
1215 O O   . SER   A 166 ? 0.2147 0.3246 0.2073 -0.0566 -0.0159 0.0305  188 SER   A O   
1216 C CB  . SER   A 166 ? 0.2154 0.2980 0.2087 -0.0429 -0.0021 0.0490  188 SER   A CB  
1217 O OG  . SER   A 166 ? 0.2074 0.2816 0.2331 -0.0236 -0.0044 0.0645  188 SER   A OG  
1218 N N   . SER   A 167 ? 0.1978 0.2583 0.1889 -0.0061 0.0016  0.0430  189 SER   A N   
1219 C CA  . SER   A 167 ? 0.2125 0.2552 0.2029 0.0119  -0.0074 0.0264  189 SER   A CA  
1220 C C   . SER   A 167 ? 0.2160 0.2357 0.1873 0.0132  -0.0044 0.0241  189 SER   A C   
1221 O O   . SER   A 167 ? 0.2165 0.2631 0.1699 0.0042  0.0006  0.0131  189 SER   A O   
1222 C CB  . SER   A 167 ? 0.2230 0.2423 0.2141 0.0216  0.0049  0.0238  189 SER   A CB  
1223 O OG  . SER   A 167 ? 0.2046 0.2336 0.2245 0.0359  0.0097  0.0277  189 SER   A OG  
1224 N N   . SER   A 168 ? 0.2143 0.2389 0.1917 0.0214  -0.0229 0.0321  190 SER   A N   
1225 C CA  . SER   A 168 ? 0.2189 0.2467 0.1817 0.0257  -0.0307 0.0372  190 SER   A CA  
1226 C C   . SER   A 168 ? 0.2240 0.2528 0.1963 0.0282  -0.0254 0.0334  190 SER   A C   
1227 O O   . SER   A 168 ? 0.2472 0.2581 0.1954 0.0261  -0.0326 0.0066  190 SER   A O   
1228 C CB  . SER   A 168 ? 0.2180 0.2549 0.1836 0.0291  -0.0235 0.0472  190 SER   A CB  
1229 O OG  . SER   A 168 ? 0.2349 0.2814 0.1855 0.0448  -0.0134 0.0564  190 SER   A OG  
1230 N N   . TYR   A 169 ? 0.2323 0.2778 0.1812 0.0099  -0.0210 0.0273  191 TYR   A N   
1231 C CA  . TYR   A 169 ? 0.2692 0.3183 0.1916 0.0270  -0.0057 0.0254  191 TYR   A CA  
1232 C C   . TYR   A 169 ? 0.2844 0.3335 0.1835 0.0193  -0.0127 0.0212  191 TYR   A C   
1233 O O   . TYR   A 169 ? 0.3174 0.3644 0.1923 0.0386  -0.0126 0.0219  191 TYR   A O   
1234 C CB  . TYR   A 169 ? 0.3001 0.3519 0.1885 0.0080  0.0037  0.0331  191 TYR   A CB  
1235 C CG  . TYR   A 169 ? 0.3588 0.4269 0.2023 -0.0084 0.0260  0.0431  191 TYR   A CG  
1236 C CD1 . TYR   A 169 ? 0.4219 0.5277 0.2207 0.0050  0.0301  0.0528  191 TYR   A CD1 
1237 C CD2 . TYR   A 169 ? 0.3872 0.4564 0.2467 -0.0060 0.0491  0.0616  191 TYR   A CD2 
1238 C CE1 . TYR   A 169 ? 0.4399 0.5574 0.2158 -0.0031 0.0530  0.0641  191 TYR   A CE1 
1239 C CE2 . TYR   A 169 ? 0.4278 0.5206 0.2412 -0.0215 0.0598  0.0654  191 TYR   A CE2 
1240 C CZ  . TYR   A 169 ? 0.4513 0.5974 0.2278 -0.0202 0.0629  0.0553  191 TYR   A CZ  
1241 O OH  . TYR   A 169 ? 0.4970 0.6979 0.2708 -0.0445 0.1261  0.0337  191 TYR   A OH  
1242 N N   . ASP   A 170 ? 0.2921 0.3308 0.1936 0.0005  -0.0151 0.0109  192 ASP   A N   
1243 C CA  . ASP   A 170 ? 0.2826 0.3344 0.2094 -0.0021 -0.0210 0.0178  192 ASP   A CA  
1244 C C   . ASP   A 170 ? 0.2857 0.3435 0.2243 -0.0083 -0.0426 0.0146  192 ASP   A C   
1245 O O   . ASP   A 170 ? 0.3043 0.3621 0.2667 -0.0006 -0.0822 0.0132  192 ASP   A O   
1246 C CB  . ASP   A 170 ? 0.2845 0.3257 0.2054 -0.0077 -0.0209 0.0132  192 ASP   A CB  
1247 C CG  . ASP   A 170 ? 0.2697 0.3125 0.2276 -0.0048 0.0015  0.0098  192 ASP   A CG  
1248 O OD1 . ASP   A 170 ? 0.2616 0.2836 0.2272 -0.0067 -0.0029 0.0059  192 ASP   A OD1 
1249 O OD2 . ASP   A 170 ? 0.2528 0.3179 0.2219 -0.0011 0.0169  0.0234  192 ASP   A OD2 
1250 N N   . GLY   A 171 ? 0.2832 0.3313 0.2187 -0.0178 -0.0368 0.0231  193 GLY   A N   
1251 C CA  . GLY   A 171 ? 0.3076 0.3487 0.2325 -0.0079 -0.0295 0.0184  193 GLY   A CA  
1252 C C   . GLY   A 171 ? 0.2940 0.3647 0.2434 -0.0260 -0.0398 0.0234  193 GLY   A C   
1253 O O   . GLY   A 171 ? 0.3065 0.3844 0.2480 -0.0192 -0.0655 0.0305  193 GLY   A O   
1254 N N   . LEU   A 172 ? 0.2792 0.3750 0.2388 -0.0376 -0.0397 0.0247  194 LEU   A N   
1255 C CA  . LEU   A 172 ? 0.2726 0.3819 0.2450 -0.0281 -0.0441 0.0165  194 LEU   A CA  
1256 C C   . LEU   A 172 ? 0.2604 0.3517 0.2482 -0.0258 -0.0359 0.0430  194 LEU   A C   
1257 O O   . LEU   A 172 ? 0.2436 0.3310 0.2532 -0.0173 -0.0097 0.0451  194 LEU   A O   
1258 C CB  . LEU   A 172 ? 0.2942 0.3918 0.2644 -0.0123 -0.0679 0.0310  194 LEU   A CB  
1259 C CG  . LEU   A 172 ? 0.3050 0.4210 0.2627 -0.0094 -0.0581 0.0444  194 LEU   A CG  
1260 C CD1 . LEU   A 172 ? 0.3045 0.4234 0.2773 0.0081  -0.0569 0.0597  194 LEU   A CD1 
1261 C CD2 . LEU   A 172 ? 0.3036 0.4345 0.3097 -0.0156 -0.0635 0.0520  194 LEU   A CD2 
1262 N N   A CYS   A 173 ? 0.2790 0.3374 0.2736 -0.0369 -0.0375 0.0454  195 CYS   A N   
1263 N N   B CYS   A 173 ? 0.2492 0.3254 0.2377 -0.0323 -0.0408 0.0456  195 CYS   A N   
1264 C CA  A CYS   A 173 ? 0.2840 0.3422 0.2793 -0.0285 -0.0377 0.0436  195 CYS   A CA  
1265 C CA  B CYS   A 173 ? 0.2319 0.3076 0.2294 -0.0288 -0.0363 0.0576  195 CYS   A CA  
1266 C C   A CYS   A 173 ? 0.2651 0.3262 0.2661 -0.0370 -0.0485 0.0470  195 CYS   A C   
1267 C C   B CYS   A 173 ? 0.2322 0.3109 0.2383 -0.0384 -0.0410 0.0566  195 CYS   A C   
1268 O O   A CYS   A 173 ? 0.2533 0.3375 0.2633 -0.0228 -0.0650 0.0413  195 CYS   A O   
1269 O O   B CYS   A 173 ? 0.2383 0.3059 0.2375 -0.0461 -0.0418 0.0534  195 CYS   A O   
1270 C CB  A CYS   A 173 ? 0.3267 0.3557 0.3196 -0.0292 -0.0290 0.0483  195 CYS   A CB  
1271 C CB  B CYS   A 173 ? 0.2170 0.3093 0.2181 -0.0295 -0.0239 0.0616  195 CYS   A CB  
1272 S SG  A CYS   A 173 ? 0.3844 0.4050 0.4007 0.0068  -0.0263 0.0409  195 CYS   A SG  
1273 S SG  B CYS   A 173 ? 0.2076 0.2897 0.2126 -0.0208 -0.0268 0.0752  195 CYS   A SG  
1274 N N   . ARG   A 174 ? 0.2364 0.3214 0.2368 -0.0389 -0.0502 0.0527  196 ARG   A N   
1275 C CA  . ARG   A 174 ? 0.2304 0.3215 0.2558 -0.0489 -0.0615 0.0545  196 ARG   A CA  
1276 C C   . ARG   A 174 ? 0.2418 0.3092 0.2412 -0.0602 -0.0430 0.0569  196 ARG   A C   
1277 O O   . ARG   A 174 ? 0.2315 0.3545 0.2309 -0.0910 -0.0182 0.0572  196 ARG   A O   
1278 C CB  . ARG   A 174 ? 0.2566 0.3130 0.2869 -0.0569 -0.0588 0.0642  196 ARG   A CB  
1279 C CG  . ARG   A 174 ? 0.2399 0.3247 0.3082 -0.0656 -0.0742 0.0731  196 ARG   A CG  
1280 C CD  . ARG   A 174 ? 0.2668 0.3168 0.3323 -0.0696 -0.0716 0.0917  196 ARG   A CD  
1281 N NE  . ARG   A 174 ? 0.2665 0.3500 0.3679 -0.0799 -0.0705 0.0932  196 ARG   A NE  
1282 C CZ  . ARG   A 174 ? 0.3156 0.4040 0.3735 -0.0709 -0.0945 0.1067  196 ARG   A CZ  
1283 N NH1 . ARG   A 174 ? 0.3260 0.4507 0.3954 -0.0782 -0.1108 0.1155  196 ARG   A NH1 
1284 N NH2 . ARG   A 174 ? 0.3276 0.3793 0.3790 -0.0609 -0.1048 0.1236  196 ARG   A NH2 
1285 N N   . ILE   A 175 ? 0.2324 0.2815 0.2460 -0.0558 -0.0545 0.0375  197 ILE   A N   
1286 C CA  . ILE   A 175 ? 0.2610 0.2924 0.2420 -0.0514 -0.0316 0.0583  197 ILE   A CA  
1287 C C   . ILE   A 175 ? 0.2300 0.3101 0.2284 -0.0438 -0.0312 0.0720  197 ILE   A C   
1288 O O   . ILE   A 175 ? 0.2392 0.3607 0.2563 -0.0530 -0.0290 0.0786  197 ILE   A O   
1289 C CB  . ILE   A 175 ? 0.3112 0.3022 0.2790 -0.0401 -0.0260 0.0651  197 ILE   A CB  
1290 C CG1 . ILE   A 175 ? 0.3175 0.2869 0.2911 -0.0488 -0.0142 0.0563  197 ILE   A CG1 
1291 C CG2 . ILE   A 175 ? 0.3350 0.3141 0.2962 -0.0319 -0.0031 0.0692  197 ILE   A CG2 
1292 C CD1 . ILE   A 175 ? 0.3425 0.3082 0.3148 -0.0565 -0.0452 0.0621  197 ILE   A CD1 
1293 N N   . TRP   A 176 ? 0.2201 0.2872 0.2407 -0.0344 -0.0266 0.0642  198 TRP   A N   
1294 C CA  . TRP   A 176 ? 0.1962 0.2959 0.2266 -0.0240 -0.0169 0.0779  198 TRP   A CA  
1295 C C   . TRP   A 176 ? 0.1988 0.2921 0.2428 -0.0309 -0.0032 0.0833  198 TRP   A C   
1296 O O   . TRP   A 176 ? 0.2337 0.3150 0.2476 -0.0210 -0.0121 0.0772  198 TRP   A O   
1297 C CB  . TRP   A 176 ? 0.1616 0.2989 0.2245 -0.0238 -0.0083 0.0685  198 TRP   A CB  
1298 C CG  . TRP   A 176 ? 0.1675 0.2919 0.2267 -0.0192 -0.0096 0.0761  198 TRP   A CG  
1299 C CD1 . TRP   A 176 ? 0.1893 0.3047 0.2319 -0.0160 0.0041  0.0810  198 TRP   A CD1 
1300 C CD2 . TRP   A 176 ? 0.1758 0.3085 0.2522 -0.0148 -0.0115 0.0776  198 TRP   A CD2 
1301 N NE1 . TRP   A 176 ? 0.1917 0.3108 0.2365 -0.0104 -0.0019 0.0693  198 TRP   A NE1 
1302 C CE2 . TRP   A 176 ? 0.1840 0.3144 0.2499 -0.0253 -0.0126 0.0846  198 TRP   A CE2 
1303 C CE3 . TRP   A 176 ? 0.1848 0.3226 0.2667 -0.0219 -0.0302 0.0735  198 TRP   A CE3 
1304 C CZ2 . TRP   A 176 ? 0.1712 0.3308 0.2495 -0.0301 -0.0194 0.0847  198 TRP   A CZ2 
1305 C CZ3 . TRP   A 176 ? 0.1776 0.3288 0.2679 -0.0221 -0.0352 0.0727  198 TRP   A CZ3 
1306 C CH2 . TRP   A 176 ? 0.1785 0.3493 0.2772 -0.0302 -0.0219 0.0809  198 TRP   A CH2 
1307 N N   . ASP   A 177 ? 0.2017 0.3222 0.2689 -0.0265 -0.0077 0.0854  199 ASP   A N   
1308 C CA  . ASP   A 177 ? 0.1897 0.3281 0.2619 -0.0215 0.0098  0.0941  199 ASP   A CA  
1309 C C   . ASP   A 177 ? 0.1748 0.3370 0.2507 -0.0205 0.0271  0.0813  199 ASP   A C   
1310 O O   . ASP   A 177 ? 0.1682 0.3237 0.2808 -0.0045 0.0276  0.0784  199 ASP   A O   
1311 C CB  . ASP   A 177 ? 0.2031 0.3467 0.2950 -0.0389 0.0147  0.1026  199 ASP   A CB  
1312 C CG  . ASP   A 177 ? 0.2131 0.3530 0.2990 -0.0297 0.0213  0.1143  199 ASP   A CG  
1313 O OD1 . ASP   A 177 ? 0.2367 0.3602 0.3389 -0.0150 0.0441  0.1439  199 ASP   A OD1 
1314 O OD2 . ASP   A 177 ? 0.2090 0.3790 0.3209 -0.0249 0.0178  0.0919  199 ASP   A OD2 
1315 N N   . THR   A 178 ? 0.1763 0.3434 0.2296 -0.0287 0.0386  0.0756  200 THR   A N   
1316 C CA  . THR   A 178 ? 0.1696 0.3530 0.2278 -0.0388 0.0401  0.0848  200 THR   A CA  
1317 C C   . THR   A 178 ? 0.1756 0.3664 0.2438 -0.0326 0.0495  0.0828  200 THR   A C   
1318 O O   . THR   A 178 ? 0.1802 0.3798 0.2699 -0.0117 0.0689  0.0827  200 THR   A O   
1319 C CB  . THR   A 178 ? 0.1639 0.3360 0.2185 -0.0377 0.0323  0.0821  200 THR   A CB  
1320 O OG1 . THR   A 178 ? 0.1621 0.3622 0.2257 -0.0355 0.0239  0.0721  200 THR   A OG1 
1321 C CG2 . THR   A 178 ? 0.1595 0.3475 0.2297 -0.0319 0.0215  0.0894  200 THR   A CG2 
1322 N N   . ALA   A 179 ? 0.1812 0.3966 0.2705 -0.0303 0.0574  0.0858  201 ALA   A N   
1323 C CA  . ALA   A 179 ? 0.2080 0.3991 0.3090 -0.0336 0.0626  0.0820  201 ALA   A CA  
1324 C C   . ALA   A 179 ? 0.2130 0.3997 0.3234 -0.0350 0.0504  0.0822  201 ALA   A C   
1325 O O   . ALA   A 179 ? 0.2292 0.4194 0.3475 -0.0309 0.0444  0.0782  201 ALA   A O   
1326 C CB  . ALA   A 179 ? 0.2327 0.4092 0.3358 -0.0557 0.0646  0.0887  201 ALA   A CB  
1327 N N   . SER   A 180 ? 0.2091 0.3980 0.3100 -0.0199 0.0407  0.0736  202 SER   A N   
1328 C CA  . SER   A 180 ? 0.2080 0.3903 0.3463 -0.0165 0.0286  0.0733  202 SER   A CA  
1329 C C   . SER   A 180 ? 0.2190 0.3700 0.3140 -0.0050 0.0031  0.0872  202 SER   A C   
1330 O O   . SER   A 180 ? 0.1879 0.3316 0.2822 -0.0019 0.0056  0.0967  202 SER   A O   
1331 C CB  . SER   A 180 ? 0.2075 0.3954 0.3400 -0.0141 0.0114  0.0575  202 SER   A CB  
1332 O OG  . SER   A 180 ? 0.1612 0.4089 0.3128 -0.0271 0.0477  0.0468  202 SER   A OG  
1333 N N   . GLY   A 181 ? 0.1947 0.3837 0.3176 -0.0148 0.0163  0.0990  203 GLY   A N   
1334 C CA  . GLY   A 181 ? 0.1996 0.3930 0.3349 -0.0268 0.0338  0.1148  203 GLY   A CA  
1335 C C   . GLY   A 181 ? 0.2058 0.3966 0.3219 -0.0368 0.0342  0.1449  203 GLY   A C   
1336 O O   . GLY   A 181 ? 0.2109 0.3849 0.3282 0.0023  0.0654  0.1362  203 GLY   A O   
1337 N N   . GLN   A 182 ? 0.1931 0.4433 0.3282 -0.0484 0.0300  0.1576  204 GLN   A N   
1338 C CA  . GLN   A 182 ? 0.2364 0.4463 0.3293 -0.0537 0.0158  0.1745  204 GLN   A CA  
1339 C C   . GLN   A 182 ? 0.1839 0.4472 0.3176 -0.0634 0.0087  0.1495  204 GLN   A C   
1340 O O   . GLN   A 182 ? 0.1943 0.4413 0.3688 -0.0524 -0.0209 0.1403  204 GLN   A O   
1341 C CB  . GLN   A 182 ? 0.2311 0.5300 0.3928 -0.0241 0.0312  0.1631  204 GLN   A CB  
1342 C CG  . GLN   A 182 ? 0.3616 0.5128 0.4667 -0.0375 0.0483  0.1829  204 GLN   A CG  
1343 C CD  . GLN   A 182 ? 0.4118 0.5414 0.5233 -0.0297 0.0439  0.1866  204 GLN   A CD  
1344 O OE1 . GLN   A 182 ? 0.4892 0.7109 0.6308 -0.0011 0.0457  0.0589  204 GLN   A OE1 
1345 N NE2 . GLN   A 182 ? 0.3902 0.4929 0.5207 -0.0657 0.1192  0.2654  204 GLN   A NE2 
1346 N N   . CYS   A 183 ? 0.2069 0.4298 0.3304 -0.0620 -0.0466 0.1394  205 CYS   A N   
1347 C CA  . CYS   A 183 ? 0.2099 0.4159 0.3396 -0.0719 -0.0475 0.1137  205 CYS   A CA  
1348 C C   . CYS   A 183 ? 0.2243 0.4155 0.3892 -0.0720 -0.0483 0.1133  205 CYS   A C   
1349 O O   . CYS   A 183 ? 0.2250 0.4236 0.4474 -0.0960 -0.0606 0.1215  205 CYS   A O   
1350 C CB  . CYS   A 183 ? 0.2496 0.4254 0.3567 -0.0681 -0.0280 0.1165  205 CYS   A CB  
1351 S SG  . CYS   A 183 ? 0.2889 0.4649 0.3493 -0.0657 -0.0426 0.0778  205 CYS   A SG  
1352 N N   . LEU   A 184 ? 0.2172 0.3959 0.3878 -0.0728 -0.0462 0.1101  206 LEU   A N   
1353 C CA  . LEU   A 184 ? 0.2204 0.3956 0.4021 -0.0854 -0.0461 0.0860  206 LEU   A CA  
1354 C C   . LEU   A 184 ? 0.2222 0.3871 0.4002 -0.1031 -0.0555 0.0773  206 LEU   A C   
1355 O O   . LEU   A 184 ? 0.3099 0.4076 0.4259 -0.1625 -0.0571 0.0253  206 LEU   A O   
1356 C CB  . LEU   A 184 ? 0.2402 0.4116 0.3866 -0.0871 -0.0365 0.0838  206 LEU   A CB  
1357 C CG  . LEU   A 184 ? 0.2641 0.4082 0.4192 -0.0694 -0.0139 0.0805  206 LEU   A CG  
1358 C CD1 . LEU   A 184 ? 0.2567 0.4346 0.3860 -0.0851 0.0076  0.0987  206 LEU   A CD1 
1359 C CD2 . LEU   A 184 ? 0.2688 0.4316 0.4714 -0.0898 -0.0136 0.0524  206 LEU   A CD2 
1360 N N   . LYS   A 185 ? 0.2446 0.3915 0.4101 -0.0973 -0.0408 0.0757  207 LYS   A N   
1361 C CA  . LYS   A 185 ? 0.2531 0.4058 0.3994 -0.0961 -0.0466 0.0668  207 LYS   A CA  
1362 C C   . LYS   A 185 ? 0.2772 0.3907 0.3705 -0.1060 -0.0612 0.0630  207 LYS   A C   
1363 O O   . LYS   A 185 ? 0.2679 0.3853 0.3542 -0.0969 -0.0834 0.0642  207 LYS   A O   
1364 C CB  . LYS   A 185 ? 0.2834 0.4141 0.4163 -0.0625 -0.0325 0.0710  207 LYS   A CB  
1365 C CG  . LYS   A 185 ? 0.3391 0.4409 0.4363 -0.0586 -0.0240 0.0746  207 LYS   A CG  
1366 C CD  . LYS   A 185 ? 0.4318 0.4080 0.4737 -0.0226 -0.0559 0.1031  207 LYS   A CD  
1367 N N   . THR   A 186 ? 0.2967 0.4128 0.3634 -0.1158 -0.0712 0.0333  208 THR   A N   
1368 C CA  . THR   A 186 ? 0.3330 0.4214 0.3598 -0.1284 -0.0698 0.0446  208 THR   A CA  
1369 C C   . THR   A 186 ? 0.3647 0.4313 0.4059 -0.1380 -0.0671 0.0084  208 THR   A C   
1370 O O   . THR   A 186 ? 0.3297 0.4449 0.4333 -0.1236 -0.0759 -0.0167 208 THR   A O   
1371 C CB  . THR   A 186 ? 0.3417 0.4441 0.3538 -0.0932 -0.0709 0.0438  208 THR   A CB  
1372 O OG1 . THR   A 186 ? 0.2921 0.4059 0.3389 -0.1016 -0.0675 0.0455  208 THR   A OG1 
1373 C CG2 . THR   A 186 ? 0.3731 0.4641 0.3390 -0.1045 -0.0584 0.0427  208 THR   A CG2 
1374 N N   . LEU   A 187 ? 0.4214 0.4520 0.4518 -0.1137 -0.0613 -0.0084 209 LEU   A N   
1375 C CA  . LEU   A 187 ? 0.5229 0.4697 0.5576 -0.0861 -0.0581 -0.0064 209 LEU   A CA  
1376 C C   . LEU   A 187 ? 0.6449 0.5255 0.5271 -0.1025 -0.0935 -0.0456 209 LEU   A C   
1377 O O   . LEU   A 187 ? 0.6524 0.5068 0.5681 -0.1016 -0.0887 -0.0949 209 LEU   A O   
1378 C CB  . LEU   A 187 ? 0.5410 0.4497 0.5518 -0.0567 -0.0546 0.0281  209 LEU   A CB  
1379 C CG  . LEU   A 187 ? 0.5157 0.3926 0.5615 -0.0562 -0.0357 0.0344  209 LEU   A CG  
1380 C CD1 . LEU   A 187 ? 0.5203 0.3246 0.5491 -0.0602 -0.0340 0.0351  209 LEU   A CD1 
1381 C CD2 . LEU   A 187 ? 0.5319 0.4242 0.5790 -0.0299 -0.0061 0.0350  209 LEU   A CD2 
1382 N N   . ILE   A 188 ? 0.6330 0.5401 0.6850 -0.1896 -0.1688 -0.1092 210 ILE   A N   
1383 C CA  . ILE   A 188 ? 0.7546 0.6066 0.6999 -0.2185 -0.1618 -0.1295 210 ILE   A CA  
1384 C C   . ILE   A 188 ? 0.8704 0.7633 0.6753 -0.1981 -0.2038 -0.2287 210 ILE   A C   
1385 O O   . ILE   A 188 ? 1.0885 0.8107 0.7176 -0.2365 -0.3446 -0.3007 210 ILE   A O   
1386 C CB  . ILE   A 188 ? 0.7741 0.5973 0.6283 -0.2471 -0.1932 -0.1431 210 ILE   A CB  
1387 N N   . ASP   A 191 ? 0.9044 0.6403 0.8137 0.1045  0.0427  -0.2728 213 ASP   A N   
1388 C CA  . ASP   A 191 ? 0.8853 0.6482 0.7824 0.1147  0.0339  -0.2311 213 ASP   A CA  
1389 C C   . ASP   A 191 ? 0.8607 0.6455 0.7101 0.0648  -0.0420 -0.1585 213 ASP   A C   
1390 O O   . ASP   A 191 ? 0.9158 0.6962 0.6870 0.0523  -0.0315 -0.2138 213 ASP   A O   
1391 C CB  . ASP   A 191 ? 0.9149 0.6748 0.8267 0.1470  0.0667  -0.1882 213 ASP   A CB  
1392 C CG  . ASP   A 191 ? 0.8952 0.6996 0.8868 0.2167  0.0969  -0.1781 213 ASP   A CG  
1393 O OD1 . ASP   A 191 ? 0.9166 0.7890 0.8053 0.1927  0.1031  -0.1121 213 ASP   A OD1 
1394 O OD2 . ASP   A 191 ? 0.9484 0.6644 0.9286 0.2868  0.1425  -0.2046 213 ASP   A OD2 
1395 N N   . ASN   A 192 ? 0.7240 0.5812 0.5790 0.0754  -0.1199 -0.1215 214 ASN   A N   
1396 C CA  . ASN   A 192 ? 0.6406 0.5296 0.5152 0.0879  -0.1558 -0.0586 214 ASN   A CA  
1397 C C   . ASN   A 192 ? 0.5567 0.4489 0.4015 0.0855  -0.1546 -0.0259 214 ASN   A C   
1398 O O   . ASN   A 192 ? 0.5532 0.4386 0.3631 0.0472  -0.1843 -0.0095 214 ASN   A O   
1399 C CB  . ASN   A 192 ? 0.6868 0.5760 0.5637 0.1277  -0.1786 -0.0683 214 ASN   A CB  
1400 C CG  . ASN   A 192 ? 0.7403 0.5838 0.6273 0.1564  -0.1834 -0.0359 214 ASN   A CG  
1401 O OD1 . ASN   A 192 ? 0.8164 0.6451 0.6316 0.1353  -0.1846 -0.0685 214 ASN   A OD1 
1402 N ND2 . ASN   A 192 ? 0.7408 0.6274 0.6796 0.1708  -0.2009 -0.0229 214 ASN   A ND2 
1403 N N   . PRO   A 193 ? 0.4771 0.4078 0.3303 0.0536  -0.1188 -0.0299 215 PRO   A N   
1404 C CA  . PRO   A 193 ? 0.4525 0.3913 0.3027 0.0566  -0.0884 -0.0189 215 PRO   A CA  
1405 C C   . PRO   A 193 ? 0.3826 0.3499 0.2869 0.0325  -0.0825 -0.0086 215 PRO   A C   
1406 O O   . PRO   A 193 ? 0.3468 0.3360 0.2858 0.0215  -0.0765 0.0018  215 PRO   A O   
1407 C CB  . PRO   A 193 ? 0.4713 0.3943 0.3334 0.0572  -0.0839 -0.0288 215 PRO   A CB  
1408 C CG  . PRO   A 193 ? 0.4581 0.4058 0.2982 0.0593  -0.1005 -0.0316 215 PRO   A CG  
1409 C CD  . PRO   A 193 ? 0.4751 0.4175 0.3161 0.0672  -0.1263 -0.0231 215 PRO   A CD  
1410 N N   . PRO   A 194 ? 0.3691 0.3558 0.2567 0.0376  -0.0472 -0.0065 216 PRO   A N   
1411 C CA  . PRO   A 194 ? 0.3315 0.3180 0.2359 0.0334  -0.0404 -0.0086 216 PRO   A CA  
1412 C C   . PRO   A 194 ? 0.3207 0.3203 0.2374 0.0323  -0.0307 -0.0075 216 PRO   A C   
1413 O O   . PRO   A 194 ? 0.3032 0.3201 0.2021 0.0323  -0.0043 -0.0084 216 PRO   A O   
1414 C CB  . PRO   A 194 ? 0.3407 0.3398 0.2445 0.0477  -0.0301 -0.0124 216 PRO   A CB  
1415 C CG  . PRO   A 194 ? 0.3385 0.3589 0.2428 0.0292  -0.0507 -0.0154 216 PRO   A CG  
1416 C CD  . PRO   A 194 ? 0.3815 0.3657 0.2710 0.0390  -0.0452 -0.0182 216 PRO   A CD  
1417 N N   . VAL   A 195 ? 0.3011 0.3100 0.1987 0.0169  -0.0386 0.0097  217 VAL   A N   
1418 C CA  . VAL   A 195 ? 0.2937 0.2895 0.2208 0.0258  -0.0474 0.0260  217 VAL   A CA  
1419 C C   . VAL   A 195 ? 0.2758 0.2986 0.2009 0.0246  -0.0434 0.0291  217 VAL   A C   
1420 O O   . VAL   A 195 ? 0.2681 0.3054 0.2220 0.0439  -0.0494 0.0194  217 VAL   A O   
1421 C CB  . VAL   A 195 ? 0.2979 0.2685 0.2175 0.0288  -0.0479 0.0236  217 VAL   A CB  
1422 C CG1 . VAL   A 195 ? 0.2898 0.2568 0.2173 0.0339  -0.0524 0.0201  217 VAL   A CG1 
1423 C CG2 . VAL   A 195 ? 0.3025 0.2636 0.2396 0.0367  -0.0671 0.0434  217 VAL   A CG2 
1424 N N   . SER   A 196 ? 0.2536 0.3051 0.2287 0.0305  -0.0178 0.0127  218 SER   A N   
1425 C CA  . SER   A 196 ? 0.2447 0.3042 0.2017 0.0255  -0.0149 0.0103  218 SER   A CA  
1426 C C   . SER   A 196 ? 0.2266 0.2962 0.1954 0.0102  -0.0038 0.0142  218 SER   A C   
1427 O O   . SER   A 196 ? 0.2283 0.3102 0.1781 0.0054  0.0008  0.0221  218 SER   A O   
1428 C CB  . SER   A 196 ? 0.2502 0.3020 0.1861 0.0351  -0.0168 0.0119  218 SER   A CB  
1429 O OG  . SER   A 196 ? 0.2555 0.3038 0.2239 0.0342  -0.0117 -0.0299 218 SER   A OG  
1430 N N   . PHE   A 197 ? 0.2270 0.2891 0.1974 0.0111  -0.0074 0.0160  219 PHE   A N   
1431 C CA  . PHE   A 197 ? 0.2184 0.2870 0.2017 0.0046  0.0122  0.0058  219 PHE   A CA  
1432 C C   . PHE   A 197 ? 0.2022 0.2661 0.1977 0.0075  0.0105  0.0123  219 PHE   A C   
1433 O O   . PHE   A 197 ? 0.2088 0.2946 0.2267 0.0040  0.0194  0.0101  219 PHE   A O   
1434 C CB  . PHE   A 197 ? 0.2267 0.3109 0.2074 0.0109  0.0059  0.0167  219 PHE   A CB  
1435 C CG  . PHE   A 197 ? 0.2527 0.3476 0.2256 0.0203  0.0152  0.0076  219 PHE   A CG  
1436 C CD1 . PHE   A 197 ? 0.2540 0.3664 0.2277 0.0230  0.0079  -0.0029 219 PHE   A CD1 
1437 C CD2 . PHE   A 197 ? 0.2755 0.3676 0.2342 0.0298  0.0112  0.0168  219 PHE   A CD2 
1438 C CE1 . PHE   A 197 ? 0.2635 0.3716 0.2189 0.0332  0.0154  0.0073  219 PHE   A CE1 
1439 C CE2 . PHE   A 197 ? 0.2619 0.3736 0.2339 0.0304  0.0114  0.0204  219 PHE   A CE2 
1440 C CZ  . PHE   A 197 ? 0.2729 0.3738 0.2185 0.0319  0.0140  0.0111  219 PHE   A CZ  
1441 N N   . VAL   A 198 ? 0.1915 0.2673 0.2159 0.0054  0.0132  0.0042  220 VAL   A N   
1442 C CA  . VAL   A 198 ? 0.2173 0.2787 0.2196 -0.0089 0.0106  0.0042  220 VAL   A CA  
1443 C C   . VAL   A 198 ? 0.2342 0.2724 0.2114 -0.0243 0.0193  0.0180  220 VAL   A C   
1444 O O   . VAL   A 198 ? 0.2191 0.2783 0.1950 -0.0199 0.0219  0.0032  220 VAL   A O   
1445 C CB  . VAL   A 198 ? 0.2229 0.3078 0.2686 0.0031  0.0111  0.0001  220 VAL   A CB  
1446 C CG1 . VAL   A 198 ? 0.2724 0.3470 0.3044 0.0069  0.0037  -0.0078 220 VAL   A CG1 
1447 C CG2 . VAL   A 198 ? 0.2082 0.2962 0.2588 -0.0075 0.0192  0.0106  220 VAL   A CG2 
1448 N N   A LYS   A 199 ? 0.2359 0.2807 0.2090 -0.0436 0.0215  0.0198  221 LYS   A N   
1449 N N   B LYS   A 199 ? 0.2261 0.2732 0.2087 -0.0422 0.0181  0.0136  221 LYS   A N   
1450 C CA  A LYS   A 199 ? 0.2552 0.2804 0.2071 -0.0437 0.0247  0.0243  221 LYS   A CA  
1451 C CA  B LYS   A 199 ? 0.2334 0.2681 0.2068 -0.0413 0.0186  0.0149  221 LYS   A CA  
1452 C C   A LYS   A 199 ? 0.2540 0.2816 0.2129 -0.0452 0.0242  0.0254  221 LYS   A C   
1453 C C   B LYS   A 199 ? 0.2420 0.2748 0.2141 -0.0453 0.0200  0.0198  221 LYS   A C   
1454 O O   A LYS   A 199 ? 0.2492 0.2863 0.2028 -0.0579 0.0187  0.0175  221 LYS   A O   
1455 O O   B LYS   A 199 ? 0.2377 0.2853 0.2101 -0.0579 0.0142  0.0098  221 LYS   A O   
1456 C CB  A LYS   A 199 ? 0.2629 0.2799 0.2051 -0.0448 0.0231  0.0332  221 LYS   A CB  
1457 C CB  B LYS   A 199 ? 0.2338 0.2532 0.2029 -0.0422 0.0128  0.0182  221 LYS   A CB  
1458 C CG  A LYS   A 199 ? 0.2880 0.2813 0.2162 -0.0437 0.0129  0.0369  221 LYS   A CG  
1459 C CG  B LYS   A 199 ? 0.2374 0.2596 0.2039 -0.0381 0.0107  0.0156  221 LYS   A CG  
1460 C CD  A LYS   A 199 ? 0.3049 0.2766 0.2059 -0.0390 -0.0083 0.0404  221 LYS   A CD  
1461 C CD  B LYS   A 199 ? 0.2513 0.2598 0.2091 -0.0270 -0.0006 0.0184  221 LYS   A CD  
1462 C CE  A LYS   A 199 ? 0.3254 0.2839 0.2262 -0.0315 -0.0156 0.0337  221 LYS   A CE  
1463 C CE  B LYS   A 199 ? 0.2565 0.2672 0.2111 -0.0226 -0.0082 0.0142  221 LYS   A CE  
1464 N NZ  A LYS   A 199 ? 0.3330 0.2857 0.2136 -0.0304 -0.0348 0.0253  221 LYS   A NZ  
1465 N NZ  B LYS   A 199 ? 0.2690 0.2679 0.2280 -0.0241 -0.0134 0.0217  221 LYS   A NZ  
1466 N N   . PHE   A 200 ? 0.2495 0.2850 0.2129 -0.0317 0.0232  0.0249  222 PHE   A N   
1467 C CA  . PHE   A 200 ? 0.2448 0.2786 0.2358 -0.0353 0.0113  0.0426  222 PHE   A CA  
1468 C C   . PHE   A 200 ? 0.2652 0.2931 0.2414 -0.0337 0.0102  0.0525  222 PHE   A C   
1469 O O   . PHE   A 200 ? 0.2608 0.3112 0.2360 -0.0258 0.0346  0.0614  222 PHE   A O   
1470 C CB  . PHE   A 200 ? 0.2506 0.2947 0.2352 -0.0369 0.0096  0.0560  222 PHE   A CB  
1471 C CG  . PHE   A 200 ? 0.2411 0.3041 0.2380 -0.0405 0.0014  0.0702  222 PHE   A CG  
1472 C CD1 . PHE   A 200 ? 0.2582 0.3057 0.2716 -0.0418 -0.0088 0.0802  222 PHE   A CD1 
1473 C CD2 . PHE   A 200 ? 0.2476 0.3124 0.2163 -0.0348 0.0113  0.0752  222 PHE   A CD2 
1474 C CE1 . PHE   A 200 ? 0.2450 0.3134 0.2379 -0.0443 0.0016  0.0802  222 PHE   A CE1 
1475 C CE2 . PHE   A 200 ? 0.2496 0.3331 0.2375 -0.0378 0.0056  0.0749  222 PHE   A CE2 
1476 C CZ  . PHE   A 200 ? 0.2496 0.3104 0.2422 -0.0373 0.0038  0.0751  222 PHE   A CZ  
1477 N N   . SER   A 201 ? 0.2815 0.2938 0.2729 -0.0281 0.0086  0.0661  223 SER   A N   
1478 C CA  . SER   A 201 ? 0.2865 0.2859 0.2597 -0.0268 0.0218  0.0606  223 SER   A CA  
1479 C C   . SER   A 201 ? 0.2761 0.3046 0.2725 -0.0167 0.0249  0.0567  223 SER   A C   
1480 O O   . SER   A 201 ? 0.2586 0.2940 0.2678 -0.0211 0.0259  0.0517  223 SER   A O   
1481 C CB  . SER   A 201 ? 0.2867 0.2924 0.2637 -0.0263 0.0355  0.0601  223 SER   A CB  
1482 O OG  . SER   A 201 ? 0.2729 0.2716 0.2767 -0.0234 0.0389  0.0316  223 SER   A OG  
1483 N N   . PRO   A 202 ? 0.2954 0.3097 0.2761 0.0131  0.0348  0.0849  224 PRO   A N   
1484 C CA  . PRO   A 202 ? 0.3130 0.3362 0.3003 0.0261  0.0525  0.0788  224 PRO   A CA  
1485 C C   . PRO   A 202 ? 0.3320 0.3446 0.2858 0.0197  0.0706  0.0936  224 PRO   A C   
1486 O O   . PRO   A 202 ? 0.3674 0.3796 0.2754 0.0392  0.0435  0.0814  224 PRO   A O   
1487 C CB  . PRO   A 202 ? 0.3094 0.3629 0.3032 0.0215  0.0506  0.0834  224 PRO   A CB  
1488 C CG  . PRO   A 202 ? 0.3132 0.3654 0.2982 0.0227  0.0471  0.0844  224 PRO   A CG  
1489 C CD  . PRO   A 202 ? 0.3041 0.3339 0.2951 0.0164  0.0391  0.0759  224 PRO   A CD  
1490 N N   . ASN   A 203 ? 0.3544 0.3709 0.2955 0.0160  0.0721  0.0837  225 ASN   A N   
1491 C CA  . ASN   A 203 ? 0.3667 0.3779 0.3118 0.0099  0.0877  0.0675  225 ASN   A CA  
1492 C C   . ASN   A 203 ? 0.3396 0.3904 0.3136 0.0054  0.0851  0.0588  225 ASN   A C   
1493 O O   . ASN   A 203 ? 0.3460 0.4295 0.3422 0.0069  0.0966  0.0080  225 ASN   A O   
1494 C CB  . ASN   A 203 ? 0.4391 0.3757 0.3674 0.0043  0.0926  0.0828  225 ASN   A CB  
1495 C CG  . ASN   A 203 ? 0.4980 0.3543 0.3757 -0.0281 0.0612  0.0991  225 ASN   A CG  
1496 O OD1 . ASN   A 203 ? 0.4327 0.3225 0.3900 -0.0182 0.0600  0.1186  225 ASN   A OD1 
1497 N ND2 . ASN   A 203 ? 0.5575 0.3679 0.4147 -0.0439 0.0652  0.1277  225 ASN   A ND2 
1498 N N   . GLY   A 204 ? 0.2960 0.3575 0.3198 0.0081  0.0735  0.0679  226 GLY   A N   
1499 C CA  . GLY   A 204 ? 0.3179 0.3293 0.3331 -0.0018 0.0629  0.0660  226 GLY   A CA  
1500 C C   . GLY   A 204 ? 0.3217 0.3249 0.3480 -0.0169 0.0613  0.0609  226 GLY   A C   
1501 O O   . GLY   A 204 ? 0.3054 0.3500 0.3246 -0.0141 0.0596  0.0388  226 GLY   A O   
1502 N N   . LYS   A 205 ? 0.3282 0.3114 0.3600 -0.0294 0.0534  0.0815  227 LYS   A N   
1503 C CA  . LYS   A 205 ? 0.3320 0.3424 0.3604 -0.0495 0.0403  0.0668  227 LYS   A CA  
1504 C C   . LYS   A 205 ? 0.3365 0.3349 0.3572 -0.0688 0.0144  0.0483  227 LYS   A C   
1505 O O   . LYS   A 205 ? 0.3287 0.3845 0.3758 -0.0713 -0.0001 0.0530  227 LYS   A O   
1506 C CB  . LYS   A 205 ? 0.3478 0.3673 0.3666 -0.0601 0.0599  0.0867  227 LYS   A CB  
1507 C CG  . LYS   A 205 ? 0.3898 0.4557 0.3491 -0.0253 0.0529  0.0581  227 LYS   A CG  
1508 N N   . TYR   A 206 ? 0.3353 0.2837 0.3154 -0.0836 0.0048  0.0356  228 TYR   A N   
1509 C CA  . TYR   A 206 ? 0.3564 0.2722 0.3278 -0.1070 0.0121  0.0325  228 TYR   A CA  
1510 C C   . TYR   A 206 ? 0.3472 0.2662 0.2899 -0.0843 0.0135  0.0364  228 TYR   A C   
1511 O O   . TYR   A 206 ? 0.3497 0.2724 0.2509 -0.0681 0.0377  0.0264  228 TYR   A O   
1512 C CB  . TYR   A 206 ? 0.3783 0.2778 0.3446 -0.1108 0.0139  0.0417  228 TYR   A CB  
1513 C CG  . TYR   A 206 ? 0.4331 0.2974 0.3828 -0.1271 0.0152  0.0648  228 TYR   A CG  
1514 C CD1 . TYR   A 206 ? 0.4677 0.3466 0.4100 -0.1356 0.0043  0.0565  228 TYR   A CD1 
1515 C CD2 . TYR   A 206 ? 0.4704 0.3267 0.4540 -0.1269 -0.0181 0.0697  228 TYR   A CD2 
1516 C CE1 . TYR   A 206 ? 0.5041 0.3279 0.4724 -0.1239 0.0060  0.0636  228 TYR   A CE1 
1517 C CE2 . TYR   A 206 ? 0.5014 0.3163 0.4770 -0.1167 0.0048  0.0704  228 TYR   A CE2 
1518 C CZ  . TYR   A 206 ? 0.5085 0.3012 0.4843 -0.1326 0.0093  0.0719  228 TYR   A CZ  
1519 O OH  . TYR   A 206 ? 0.5684 0.3004 0.5555 -0.1822 0.0564  0.0492  228 TYR   A OH  
1520 N N   . ILE   A 207 ? 0.3167 0.2771 0.2837 -0.0615 -0.0059 0.0302  229 ILE   A N   
1521 C CA  . ILE   A 207 ? 0.3006 0.2759 0.2596 -0.0405 0.0027  0.0307  229 ILE   A CA  
1522 C C   . ILE   A 207 ? 0.3022 0.2745 0.2374 -0.0366 -0.0078 0.0226  229 ILE   A C   
1523 O O   . ILE   A 207 ? 0.2982 0.2543 0.2907 -0.0501 -0.0112 0.0111  229 ILE   A O   
1524 C CB  . ILE   A 207 ? 0.3111 0.2737 0.2593 -0.0302 0.0016  0.0396  229 ILE   A CB  
1525 C CG1 . ILE   A 207 ? 0.3252 0.2830 0.2719 -0.0192 -0.0159 0.0368  229 ILE   A CG1 
1526 C CG2 . ILE   A 207 ? 0.3236 0.2763 0.2787 -0.0263 0.0109  0.0445  229 ILE   A CG2 
1527 C CD1 . ILE   A 207 ? 0.3380 0.2880 0.2932 -0.0131 -0.0140 0.0349  229 ILE   A CD1 
1528 N N   . LEU   A 208 ? 0.2823 0.2877 0.2018 -0.0286 -0.0088 0.0203  230 LEU   A N   
1529 C CA  . LEU   A 208 ? 0.2867 0.2802 0.2141 -0.0128 0.0059  0.0207  230 LEU   A CA  
1530 C C   . LEU   A 208 ? 0.2995 0.2768 0.2151 -0.0021 -0.0013 0.0300  230 LEU   A C   
1531 O O   . LEU   A 208 ? 0.3171 0.2979 0.2038 -0.0035 -0.0084 0.0215  230 LEU   A O   
1532 C CB  . LEU   A 208 ? 0.2772 0.2967 0.2256 0.0023  0.0097  0.0385  230 LEU   A CB  
1533 C CG  . LEU   A 208 ? 0.2638 0.3163 0.2338 -0.0058 0.0136  0.0327  230 LEU   A CG  
1534 C CD1 . LEU   A 208 ? 0.2612 0.3197 0.2464 -0.0051 0.0205  0.0329  230 LEU   A CD1 
1535 C CD2 . LEU   A 208 ? 0.2571 0.3215 0.2734 -0.0146 0.0082  0.0267  230 LEU   A CD2 
1536 N N   . ALA   A 209 ? 0.2926 0.2788 0.2220 -0.0116 -0.0118 0.0214  231 ALA   A N   
1537 C CA  . ALA   A 209 ? 0.2776 0.2671 0.2324 0.0080  -0.0190 0.0321  231 ALA   A CA  
1538 C C   . ALA   A 209 ? 0.2755 0.2763 0.2276 0.0048  -0.0097 0.0373  231 ALA   A C   
1539 O O   . ALA   A 209 ? 0.3227 0.2985 0.2457 -0.0166 0.0033  0.0294  231 ALA   A O   
1540 C CB  . ALA   A 209 ? 0.2740 0.2730 0.2250 0.0097  -0.0298 0.0163  231 ALA   A CB  
1541 N N   . ALA   A 210 ? 0.2537 0.2796 0.2226 0.0032  -0.0173 0.0347  232 ALA   A N   
1542 C CA  . ALA   A 210 ? 0.2542 0.3007 0.2231 0.0096  -0.0260 0.0318  232 ALA   A CA  
1543 C C   . ALA   A 210 ? 0.2540 0.3152 0.2227 0.0210  -0.0324 0.0258  232 ALA   A C   
1544 O O   . ALA   A 210 ? 0.2864 0.3430 0.2261 0.0275  -0.0175 0.0185  232 ALA   A O   
1545 C CB  . ALA   A 210 ? 0.2407 0.3049 0.2263 0.0074  -0.0180 0.0467  232 ALA   A CB  
1546 N N   . THR   A 211 ? 0.2877 0.3186 0.2415 0.0394  -0.0488 0.0120  233 THR   A N   
1547 C CA  . THR   A 211 ? 0.2996 0.3124 0.2384 0.0396  -0.0445 0.0106  233 THR   A CA  
1548 C C   . THR   A 211 ? 0.3088 0.3294 0.2239 0.0376  -0.0505 -0.0053 233 THR   A C   
1549 O O   . THR   A 211 ? 0.2885 0.3541 0.2299 0.0340  -0.0402 -0.0159 233 THR   A O   
1550 C CB  . THR   A 211 ? 0.3136 0.3249 0.2774 0.0466  -0.0437 0.0069  233 THR   A CB  
1551 O OG1 . THR   A 211 ? 0.3175 0.3242 0.2734 0.0467  -0.0477 -0.0138 233 THR   A OG1 
1552 C CG2 . THR   A 211 ? 0.3288 0.3342 0.3026 0.0406  -0.0288 -0.0015 233 THR   A CG2 
1553 N N   . LEU   A 212 ? 0.3116 0.3441 0.2134 0.0338  -0.0433 -0.0037 234 LEU   A N   
1554 C CA  . LEU   A 212 ? 0.3270 0.3544 0.2220 0.0216  -0.0486 0.0176  234 LEU   A CA  
1555 C C   . LEU   A 212 ? 0.3359 0.3562 0.2038 0.0041  -0.0455 0.0143  234 LEU   A C   
1556 O O   . LEU   A 212 ? 0.4269 0.3802 0.2082 -0.0313 -0.0255 0.0138  234 LEU   A O   
1557 C CB  . LEU   A 212 ? 0.3380 0.3566 0.2476 0.0283  -0.0597 0.0259  234 LEU   A CB  
1558 C CG  . LEU   A 212 ? 0.3749 0.3455 0.2802 0.0312  -0.0279 0.0243  234 LEU   A CG  
1559 C CD1 . LEU   A 212 ? 0.3772 0.3606 0.2999 0.0243  -0.0150 0.0440  234 LEU   A CD1 
1560 C CD2 . LEU   A 212 ? 0.3678 0.3529 0.2949 0.0288  -0.0267 0.0244  234 LEU   A CD2 
1561 N N   . ASP   A 213 ? 0.3561 0.3760 0.2406 -0.0042 -0.0243 0.0050  235 ASP   A N   
1562 C CA  . ASP   A 213 ? 0.3643 0.3730 0.2753 0.0023  -0.0335 -0.0037 235 ASP   A CA  
1563 C C   . ASP   A 213 ? 0.3550 0.3667 0.2642 0.0207  -0.0244 -0.0234 235 ASP   A C   
1564 O O   . ASP   A 213 ? 0.3966 0.3733 0.2257 0.0205  -0.0229 -0.0465 235 ASP   A O   
1565 C CB  . ASP   A 213 ? 0.3863 0.3788 0.3101 0.0066  -0.0712 -0.0237 235 ASP   A CB  
1566 C CG  . ASP   A 213 ? 0.3904 0.3970 0.3152 0.0130  -0.0804 -0.0224 235 ASP   A CG  
1567 O OD1 . ASP   A 213 ? 0.4201 0.4322 0.3063 0.0369  -0.0771 -0.0376 235 ASP   A OD1 
1568 O OD2 . ASP   A 213 ? 0.3933 0.4133 0.3998 0.0092  -0.0957 -0.0146 235 ASP   A OD2 
1569 N N   . ASN   A 214 ? 0.3560 0.3678 0.2777 0.0168  -0.0169 -0.0367 236 ASN   A N   
1570 C CA  . ASN   A 214 ? 0.3572 0.3798 0.2556 0.0104  -0.0205 -0.0355 236 ASN   A CA  
1571 C C   . ASN   A 214 ? 0.3605 0.3431 0.2718 0.0127  -0.0144 -0.0412 236 ASN   A C   
1572 O O   . ASN   A 214 ? 0.3808 0.3555 0.2228 0.0268  0.0076  -0.0501 236 ASN   A O   
1573 C CB  . ASN   A 214 ? 0.3543 0.4171 0.2530 0.0049  -0.0269 -0.0380 236 ASN   A CB  
1574 C CG  . ASN   A 214 ? 0.3672 0.4287 0.2425 -0.0009 -0.0315 -0.0328 236 ASN   A CG  
1575 O OD1 . ASN   A 214 ? 0.3452 0.4253 0.2002 0.0237  -0.0425 -0.0500 236 ASN   A OD1 
1576 N ND2 . ASN   A 214 ? 0.3715 0.4714 0.2627 -0.0274 -0.0344 -0.0489 236 ASN   A ND2 
1577 N N   . THR   A 215 ? 0.3754 0.3179 0.2804 0.0195  -0.0037 -0.0273 237 THR   A N   
1578 C CA  . THR   A 215 ? 0.3692 0.3008 0.2832 0.0219  -0.0229 -0.0304 237 THR   A CA  
1579 C C   . THR   A 215 ? 0.3592 0.2967 0.2592 0.0219  -0.0376 -0.0164 237 THR   A C   
1580 O O   . THR   A 215 ? 0.3602 0.2862 0.2396 0.0256  -0.0239 -0.0033 237 THR   A O   
1581 C CB  . THR   A 215 ? 0.3833 0.3055 0.2742 0.0169  -0.0176 -0.0460 237 THR   A CB  
1582 O OG1 . THR   A 215 ? 0.3858 0.3259 0.3140 0.0278  -0.0036 -0.0657 237 THR   A OG1 
1583 C CG2 . THR   A 215 ? 0.3944 0.3101 0.3009 0.0088  -0.0286 -0.0502 237 THR   A CG2 
1584 N N   . LEU   A 216 ? 0.3528 0.2731 0.2616 0.0157  -0.0516 -0.0117 238 LEU   A N   
1585 C CA  . LEU   A 216 ? 0.3420 0.2873 0.2729 0.0159  -0.0586 -0.0269 238 LEU   A CA  
1586 C C   . LEU   A 216 ? 0.3483 0.3053 0.2764 0.0089  -0.0444 -0.0240 238 LEU   A C   
1587 O O   . LEU   A 216 ? 0.3850 0.3208 0.3071 0.0385  -0.0383 -0.0108 238 LEU   A O   
1588 C CB  . LEU   A 216 ? 0.3600 0.3048 0.2806 0.0162  -0.0573 -0.0174 238 LEU   A CB  
1589 C CG  . LEU   A 216 ? 0.3386 0.3128 0.3055 0.0260  -0.0445 -0.0383 238 LEU   A CG  
1590 C CD1 . LEU   A 216 ? 0.3399 0.3096 0.3303 0.0408  -0.0364 -0.0320 238 LEU   A CD1 
1591 C CD2 . LEU   A 216 ? 0.3360 0.3037 0.3203 0.0357  -0.0377 -0.0299 238 LEU   A CD2 
1592 N N   . LYS   A 217 ? 0.3443 0.2977 0.2561 -0.0097 -0.0348 -0.0288 239 LYS   A N   
1593 C CA  . LYS   A 217 ? 0.3597 0.2890 0.2592 -0.0181 -0.0291 -0.0272 239 LYS   A CA  
1594 C C   . LYS   A 217 ? 0.3566 0.2779 0.2576 -0.0247 -0.0304 -0.0111 239 LYS   A C   
1595 O O   . LYS   A 217 ? 0.4145 0.2892 0.2328 -0.0585 -0.0096 -0.0119 239 LYS   A O   
1596 C CB  . LYS   A 217 ? 0.3591 0.3045 0.2872 -0.0174 -0.0390 -0.0256 239 LYS   A CB  
1597 C CG  . LYS   A 217 ? 0.3932 0.3274 0.3038 -0.0018 -0.0416 -0.0498 239 LYS   A CG  
1598 C CD  . LYS   A 217 ? 0.4112 0.3457 0.3334 -0.0031 -0.0626 -0.0476 239 LYS   A CD  
1599 C CE  . LYS   A 217 ? 0.4604 0.4496 0.3461 0.0037  -0.0557 -0.0459 239 LYS   A CE  
1600 N NZ  . LYS   A 217 ? 0.5141 0.4744 0.3932 0.0114  -0.0628 -0.0498 239 LYS   A NZ  
1601 N N   . LEU   A 218 ? 0.3467 0.2672 0.2710 -0.0356 -0.0397 -0.0076 240 LEU   A N   
1602 C CA  . LEU   A 218 ? 0.3476 0.2875 0.2800 -0.0609 -0.0447 -0.0028 240 LEU   A CA  
1603 C C   . LEU   A 218 ? 0.3374 0.2938 0.2997 -0.0674 -0.0391 0.0049  240 LEU   A C   
1604 O O   . LEU   A 218 ? 0.3369 0.3128 0.3247 -0.0620 -0.0400 -0.0155 240 LEU   A O   
1605 C CB  . LEU   A 218 ? 0.3648 0.2986 0.2907 -0.0899 -0.0435 0.0115  240 LEU   A CB  
1606 C CG  . LEU   A 218 ? 0.3839 0.3256 0.2773 -0.0848 -0.0452 0.0163  240 LEU   A CG  
1607 C CD1 . LEU   A 218 ? 0.3801 0.3376 0.2715 -0.0902 -0.0447 0.0220  240 LEU   A CD1 
1608 C CD2 . LEU   A 218 ? 0.4098 0.3499 0.3083 -0.0810 -0.0407 0.0206  240 LEU   A CD2 
1609 N N   . TRP   A 219 ? 0.3306 0.3068 0.2937 -0.0695 -0.0317 -0.0168 241 TRP   A N   
1610 C CA  . TRP   A 219 ? 0.3326 0.3241 0.3393 -0.0968 -0.0408 -0.0069 241 TRP   A CA  
1611 C C   . TRP   A 219 ? 0.3599 0.3167 0.3505 -0.0936 -0.0322 0.0116  241 TRP   A C   
1612 O O   . TRP   A 219 ? 0.3646 0.3165 0.3418 -0.0888 -0.0267 0.0160  241 TRP   A O   
1613 C CB  . TRP   A 219 ? 0.3232 0.3692 0.3453 -0.0889 -0.0550 0.0171  241 TRP   A CB  
1614 C CG  . TRP   A 219 ? 0.3375 0.4016 0.3655 -0.0818 -0.0364 0.0394  241 TRP   A CG  
1615 C CD1 . TRP   A 219 ? 0.3537 0.4316 0.3714 -0.0941 -0.0377 0.0599  241 TRP   A CD1 
1616 C CD2 . TRP   A 219 ? 0.3502 0.4215 0.3658 -0.0957 -0.0338 0.0464  241 TRP   A CD2 
1617 N NE1 . TRP   A 219 ? 0.3470 0.4425 0.3711 -0.1062 -0.0379 0.0505  241 TRP   A NE1 
1618 C CE2 . TRP   A 219 ? 0.3417 0.4659 0.3724 -0.1084 -0.0330 0.0605  241 TRP   A CE2 
1619 C CE3 . TRP   A 219 ? 0.3570 0.4523 0.3729 -0.1060 -0.0160 0.0684  241 TRP   A CE3 
1620 C CZ2 . TRP   A 219 ? 0.3677 0.5101 0.3874 -0.0968 -0.0406 0.0711  241 TRP   A CZ2 
1621 C CZ3 . TRP   A 219 ? 0.3923 0.5237 0.3823 -0.1130 -0.0054 0.0720  241 TRP   A CZ3 
1622 C CH2 . TRP   A 219 ? 0.3663 0.5342 0.3890 -0.1345 -0.0112 0.0728  241 TRP   A CH2 
1623 N N   . ASP   A 220 ? 0.3682 0.3396 0.3820 -0.0993 -0.0157 0.0164  242 ASP   A N   
1624 C CA  . ASP   A 220 ? 0.3663 0.3710 0.4078 -0.0867 0.0027  0.0376  242 ASP   A CA  
1625 C C   . ASP   A 220 ? 0.3765 0.3990 0.4299 -0.0879 0.0120  0.0304  242 ASP   A C   
1626 O O   . ASP   A 220 ? 0.3795 0.4328 0.4523 -0.0713 -0.0132 0.0012  242 ASP   A O   
1627 C CB  . ASP   A 220 ? 0.3957 0.4086 0.4358 -0.0896 -0.0094 0.0498  242 ASP   A CB  
1628 C CG  . ASP   A 220 ? 0.3820 0.4362 0.4823 -0.0799 0.0075  0.0663  242 ASP   A CG  
1629 O OD1 . ASP   A 220 ? 0.3812 0.4180 0.4777 -0.0798 -0.0270 0.0803  242 ASP   A OD1 
1630 O OD2 . ASP   A 220 ? 0.4152 0.4850 0.5409 -0.0188 0.0287  0.1017  242 ASP   A OD2 
1631 N N   . TYR   A 221 ? 0.3977 0.3498 0.4530 -0.0816 0.0028  0.0416  243 TYR   A N   
1632 C CA  . TYR   A 221 ? 0.3841 0.3524 0.4700 -0.0776 -0.0078 0.0566  243 TYR   A CA  
1633 C C   . TYR   A 221 ? 0.3794 0.3955 0.4740 -0.0881 -0.0189 0.0614  243 TYR   A C   
1634 O O   . TYR   A 221 ? 0.3267 0.3551 0.4894 -0.0818 -0.0621 0.0515  243 TYR   A O   
1635 C CB  . TYR   A 221 ? 0.3919 0.3086 0.4760 -0.0616 -0.0008 0.0585  243 TYR   A CB  
1636 C CG  . TYR   A 221 ? 0.3926 0.2934 0.4944 -0.0540 0.0340  0.0447  243 TYR   A CG  
1637 C CD1 . TYR   A 221 ? 0.3809 0.3045 0.4783 -0.0490 0.0417  0.0485  243 TYR   A CD1 
1638 C CD2 . TYR   A 221 ? 0.4521 0.3016 0.5191 -0.0132 0.0542  0.0504  243 TYR   A CD2 
1639 C CE1 . TYR   A 221 ? 0.4392 0.3177 0.5112 -0.0318 0.0291  0.0485  243 TYR   A CE1 
1640 C CE2 . TYR   A 221 ? 0.4651 0.3015 0.5287 -0.0108 0.0547  0.0586  243 TYR   A CE2 
1641 C CZ  . TYR   A 221 ? 0.4561 0.3230 0.5286 -0.0106 0.0355  0.0467  243 TYR   A CZ  
1642 O OH  . TYR   A 221 ? 0.5228 0.3046 0.6085 0.0003  -0.0127 0.0614  243 TYR   A OH  
1643 N N   . SER   A 222 ? 0.3889 0.4381 0.4561 -0.0988 -0.0080 0.0535  244 SER   A N   
1644 C CA  . SER   A 222 ? 0.3776 0.5179 0.4801 -0.0959 0.0056  0.0393  244 SER   A CA  
1645 C C   . SER   A 222 ? 0.3875 0.5747 0.5387 -0.0953 -0.0215 0.0222  244 SER   A C   
1646 O O   . SER   A 222 ? 0.3898 0.5972 0.6329 -0.0652 0.0115  -0.0063 244 SER   A O   
1647 C CB  . SER   A 222 ? 0.3770 0.5929 0.4583 -0.0960 0.0052  0.0556  244 SER   A CB  
1648 N N   . LYS   A 223 ? 0.3973 0.5387 0.5605 -0.1335 -0.0397 0.0093  245 LYS   A N   
1649 C CA  . LYS   A 223 ? 0.4149 0.5704 0.5540 -0.1625 -0.0692 0.0432  245 LYS   A CA  
1650 C C   . LYS   A 223 ? 0.4193 0.6049 0.5320 -0.1655 -0.0912 0.0471  245 LYS   A C   
1651 O O   . LYS   A 223 ? 0.4136 0.6323 0.5736 -0.1854 -0.1129 0.0146  245 LYS   A O   
1652 C CB  . LYS   A 223 ? 0.4334 0.5588 0.5814 -0.1498 -0.0689 0.0432  245 LYS   A CB  
1653 C CG  . LYS   A 223 ? 0.4716 0.5551 0.5569 -0.1381 -0.0544 0.0575  245 LYS   A CG  
1654 C CD  . LYS   A 223 ? 0.5121 0.5563 0.5754 -0.1172 -0.0622 0.0578  245 LYS   A CD  
1655 N N   . GLY   A 224 ? 0.4386 0.5728 0.4713 -0.1727 -0.0836 0.0605  246 GLY   A N   
1656 C CA  . GLY   A 224 ? 0.4581 0.5419 0.4840 -0.1313 -0.0825 0.0733  246 GLY   A CA  
1657 C C   . GLY   A 224 ? 0.4770 0.5229 0.4583 -0.1128 -0.0747 0.0778  246 GLY   A C   
1658 O O   . GLY   A 224 ? 0.5253 0.5367 0.4834 -0.0736 -0.1457 0.1150  246 GLY   A O   
1659 N N   . LYS   A 225 ? 0.4173 0.4751 0.4812 -0.0858 -0.0275 0.0606  247 LYS   A N   
1660 C CA  . LYS   A 225 ? 0.4006 0.4486 0.4439 -0.1229 -0.0528 0.0244  247 LYS   A CA  
1661 C C   . LYS   A 225 ? 0.4087 0.4250 0.4256 -0.0916 -0.0532 -0.0125 247 LYS   A C   
1662 O O   . LYS   A 225 ? 0.4340 0.3402 0.4058 -0.0841 -0.0423 -0.0594 247 LYS   A O   
1663 C CB  . LYS   A 225 ? 0.3890 0.4465 0.4347 -0.1353 -0.0511 0.0459  247 LYS   A CB  
1664 N N   . CYS   A 226 ? 0.4200 0.4211 0.4129 -0.1042 -0.0637 -0.0220 248 CYS   A N   
1665 C CA  . CYS   A 226 ? 0.4060 0.3747 0.4187 -0.1237 -0.0891 -0.0269 248 CYS   A CA  
1666 C C   . CYS   A 226 ? 0.4201 0.3333 0.4299 -0.1326 -0.1097 -0.0624 248 CYS   A C   
1667 O O   . CYS   A 226 ? 0.4927 0.3441 0.4348 -0.1363 -0.1384 -0.1044 248 CYS   A O   
1668 C CB  . CYS   A 226 ? 0.4111 0.4116 0.4277 -0.1066 -0.0688 -0.0084 248 CYS   A CB  
1669 S SG  . CYS   A 226 ? 0.4289 0.5073 0.4109 -0.1146 -0.0746 0.0258  248 CYS   A SG  
1670 N N   . LEU   A 227 ? 0.4135 0.3313 0.4233 -0.1104 -0.0965 -0.0599 249 LEU   A N   
1671 C CA  . LEU   A 227 ? 0.4231 0.3291 0.4320 -0.0774 -0.0960 -0.0533 249 LEU   A CA  
1672 C C   . LEU   A 227 ? 0.4453 0.3156 0.4098 -0.0713 -0.0989 -0.0570 249 LEU   A C   
1673 O O   . LEU   A 227 ? 0.4810 0.3096 0.4752 -0.0907 -0.0919 -0.0298 249 LEU   A O   
1674 C CB  . LEU   A 227 ? 0.4410 0.3732 0.4522 -0.0468 -0.0912 -0.0265 249 LEU   A CB  
1675 C CG  . LEU   A 227 ? 0.4602 0.3619 0.4857 -0.0327 -0.0892 -0.0278 249 LEU   A CG  
1676 C CD1 . LEU   A 227 ? 0.4673 0.3723 0.4856 -0.0509 -0.0942 -0.0407 249 LEU   A CD1 
1677 C CD2 . LEU   A 227 ? 0.4534 0.3555 0.5056 -0.0502 -0.0895 -0.0377 249 LEU   A CD2 
1678 N N   . LYS   A 228 ? 0.4367 0.2947 0.3957 -0.0542 -0.0849 -0.0420 250 LYS   A N   
1679 C CA  . LYS   A 228 ? 0.4197 0.2901 0.3803 -0.0528 -0.0734 -0.0352 250 LYS   A CA  
1680 C C   . LYS   A 228 ? 0.4040 0.3099 0.3433 -0.0244 -0.0779 -0.0360 250 LYS   A C   
1681 O O   . LYS   A 228 ? 0.3626 0.3193 0.3468 -0.0077 -0.0567 -0.0546 250 LYS   A O   
1682 C CB  . LYS   A 228 ? 0.4265 0.2780 0.3711 -0.0499 -0.0727 -0.0247 250 LYS   A CB  
1683 C CG  . LYS   A 228 ? 0.4330 0.3136 0.3895 -0.0565 -0.0666 -0.0260 250 LYS   A CG  
1684 C CD  . LYS   A 228 ? 0.4613 0.3249 0.4053 -0.0658 -0.0687 -0.0134 250 LYS   A CD  
1685 C CE  . LYS   A 228 ? 0.4750 0.3237 0.4328 -0.0810 -0.0600 -0.0087 250 LYS   A CE  
1686 N NZ  . LYS   A 228 ? 0.4839 0.3282 0.4551 -0.0672 -0.0540 0.0033  250 LYS   A NZ  
1687 N N   . THR   A 229 ? 0.4192 0.3262 0.3209 -0.0289 -0.0767 -0.0598 251 THR   A N   
1688 C CA  . THR   A 229 ? 0.4262 0.3528 0.3412 -0.0254 -0.0592 -0.0520 251 THR   A CA  
1689 C C   . THR   A 229 ? 0.4424 0.3299 0.3219 -0.0228 -0.0494 -0.0443 251 THR   A C   
1690 O O   . THR   A 229 ? 0.4693 0.3312 0.3592 0.0022  -0.0041 -0.0732 251 THR   A O   
1691 C CB  . THR   A 229 ? 0.4250 0.4546 0.3597 -0.0367 -0.0868 -0.0459 251 THR   A CB  
1692 O OG1 . THR   A 229 ? 0.4250 0.4870 0.3882 -0.0467 -0.1183 -0.0979 251 THR   A OG1 
1693 C CG2 . THR   A 229 ? 0.4562 0.4944 0.3800 -0.0351 -0.0856 -0.0416 251 THR   A CG2 
1694 N N   . TYR   A 230 ? 0.4489 0.2901 0.2765 -0.0156 -0.0559 -0.0684 252 TYR   A N   
1695 C CA  . TYR   A 230 ? 0.4477 0.2860 0.2547 -0.0033 -0.0563 -0.0366 252 TYR   A CA  
1696 C C   . TYR   A 230 ? 0.4506 0.3199 0.2338 -0.0018 -0.0596 -0.0486 252 TYR   A C   
1697 O O   . TYR   A 230 ? 0.4181 0.3312 0.2201 0.0142  -0.0687 -0.0104 252 TYR   A O   
1698 C CB  . TYR   A 230 ? 0.4305 0.2702 0.2504 0.0088  -0.0565 -0.0386 252 TYR   A CB  
1699 C CG  . TYR   A 230 ? 0.4127 0.2527 0.2666 -0.0015 -0.0558 -0.0245 252 TYR   A CG  
1700 C CD1 . TYR   A 230 ? 0.4117 0.2589 0.2725 -0.0132 -0.0696 -0.0240 252 TYR   A CD1 
1701 C CD2 . TYR   A 230 ? 0.4069 0.2787 0.2910 0.0014  -0.0518 -0.0212 252 TYR   A CD2 
1702 C CE1 . TYR   A 230 ? 0.3897 0.2377 0.2800 -0.0167 -0.0581 -0.0084 252 TYR   A CE1 
1703 C CE2 . TYR   A 230 ? 0.3839 0.2384 0.2922 -0.0034 -0.0538 -0.0028 252 TYR   A CE2 
1704 C CZ  . TYR   A 230 ? 0.3872 0.2467 0.2690 -0.0121 -0.0606 -0.0066 252 TYR   A CZ  
1705 O OH  . TYR   A 230 ? 0.3632 0.2397 0.2708 -0.0206 -0.0512 0.0178  252 TYR   A OH  
1706 N N   . THR   A 231 ? 0.4209 0.3469 0.2741 0.0104  -0.0607 -0.0432 253 THR   A N   
1707 C CA  . THR   A 231 ? 0.4489 0.3395 0.2489 0.0155  -0.0671 -0.0539 253 THR   A CA  
1708 C C   . THR   A 231 ? 0.4561 0.3388 0.2464 0.0446  -0.0681 -0.0689 253 THR   A C   
1709 O O   . THR   A 231 ? 0.5007 0.3472 0.2296 0.0550  -0.0930 -0.0969 253 THR   A O   
1710 C CB  . THR   A 231 ? 0.4637 0.3233 0.2709 -0.0054 -0.0630 -0.0598 253 THR   A CB  
1711 O OG1 . THR   A 231 ? 0.4871 0.3082 0.2573 -0.0448 -0.0492 -0.0957 253 THR   A OG1 
1712 C CG2 . THR   A 231 ? 0.4550 0.3268 0.2862 -0.0081 -0.0693 -0.0625 253 THR   A CG2 
1713 N N   . GLY   A 232 ? 0.4356 0.3833 0.2744 0.0642  -0.0649 -0.0413 254 GLY   A N   
1714 C CA  . GLY   A 232 ? 0.4321 0.4103 0.2778 0.0624  -0.0532 -0.0417 254 GLY   A CA  
1715 C C   . GLY   A 232 ? 0.4128 0.4030 0.2923 0.0688  -0.0408 -0.0356 254 GLY   A C   
1716 O O   . GLY   A 232 ? 0.3761 0.4618 0.3190 0.0973  -0.0633 -0.0361 254 GLY   A O   
1717 N N   . HIS   A 233 ? 0.3981 0.3873 0.2698 0.0643  -0.0349 -0.0234 255 HIS   A N   
1718 C CA  . HIS   A 233 ? 0.3803 0.3729 0.2530 0.0606  -0.0502 -0.0146 255 HIS   A CA  
1719 C C   . HIS   A 233 ? 0.3887 0.3754 0.2449 0.0392  -0.0406 -0.0207 255 HIS   A C   
1720 O O   . HIS   A 233 ? 0.4167 0.3455 0.2457 0.0397  -0.0631 -0.0325 255 HIS   A O   
1721 C CB  . HIS   A 233 ? 0.3839 0.3839 0.2398 0.0492  -0.0363 -0.0080 255 HIS   A CB  
1722 C CG  . HIS   A 233 ? 0.3829 0.4239 0.2670 0.0439  -0.0248 -0.0114 255 HIS   A CG  
1723 N ND1 . HIS   A 233 ? 0.3850 0.4461 0.2622 0.0429  -0.0306 -0.0091 255 HIS   A ND1 
1724 C CD2 . HIS   A 233 ? 0.3953 0.4348 0.3101 0.0410  -0.0176 -0.0067 255 HIS   A CD2 
1725 C CE1 . HIS   A 233 ? 0.3956 0.4629 0.2984 0.0526  -0.0116 -0.0099 255 HIS   A CE1 
1726 N NE2 . HIS   A 233 ? 0.3813 0.4302 0.3127 0.0675  -0.0099 0.0079  255 HIS   A NE2 
1727 N N   . LYS   A 234 ? 0.3624 0.3460 0.2495 0.0525  -0.0317 -0.0379 256 LYS   A N   
1728 C CA  . LYS   A 234 ? 0.3429 0.3724 0.2424 0.0495  -0.0209 -0.0296 256 LYS   A CA  
1729 C C   . LYS   A 234 ? 0.3006 0.3741 0.2159 0.0436  -0.0135 -0.0302 256 LYS   A C   
1730 O O   . LYS   A 234 ? 0.2797 0.3773 0.2143 0.0220  -0.0152 -0.0215 256 LYS   A O   
1731 C CB  . LYS   A 234 ? 0.3394 0.4200 0.2843 0.0613  -0.0229 -0.0104 256 LYS   A CB  
1732 C CG  . LYS   A 234 ? 0.4207 0.4755 0.3535 0.0450  0.0142  0.0231  256 LYS   A CG  
1733 C CD  . LYS   A 234 ? 0.4714 0.5601 0.4042 0.0518  0.0432  0.0478  256 LYS   A CD  
1734 C CE  . LYS   A 234 ? 0.5292 0.5866 0.4677 0.0443  0.0581  0.0904  256 LYS   A CE  
1735 N NZ  . LYS   A 234 ? 0.5527 0.6366 0.5320 0.0398  0.0526  0.0883  256 LYS   A NZ  
1736 N N   . ASN   A 235 ? 0.2919 0.3781 0.2209 0.0251  -0.0244 -0.0259 257 ASN   A N   
1737 C CA  . ASN   A 235 ? 0.2950 0.3719 0.2205 0.0414  -0.0193 -0.0209 257 ASN   A CA  
1738 C C   . ASN   A 235 ? 0.3230 0.3866 0.1999 0.0397  -0.0104 -0.0115 257 ASN   A C   
1739 O O   . ASN   A 235 ? 0.3300 0.4049 0.2008 0.0601  -0.0192 -0.0243 257 ASN   A O   
1740 C CB  . ASN   A 235 ? 0.2929 0.3678 0.2534 0.0545  -0.0108 -0.0160 257 ASN   A CB  
1741 C CG  . ASN   A 235 ? 0.2920 0.3506 0.2529 0.0599  0.0073  -0.0097 257 ASN   A CG  
1742 O OD1 . ASN   A 235 ? 0.3089 0.3511 0.2959 0.0520  0.0335  0.0411  257 ASN   A OD1 
1743 N ND2 . ASN   A 235 ? 0.2722 0.3463 0.2478 0.0703  0.0123  -0.0022 257 ASN   A ND2 
1744 N N   A GLU   A 236 ? 0.3301 0.3963 0.2226 0.0365  -0.0108 0.0040  258 GLU   A N   
1745 N N   B GLU   A 236 ? 0.3259 0.4039 0.2049 0.0277  -0.0135 -0.0038 258 GLU   A N   
1746 C CA  A GLU   A 236 ? 0.3410 0.4066 0.2124 0.0386  0.0006  0.0144  258 GLU   A CA  
1747 C CA  B GLU   A 236 ? 0.3341 0.4182 0.1787 0.0227  -0.0008 -0.0011 258 GLU   A CA  
1748 C C   A GLU   A 236 ? 0.3221 0.4087 0.1839 0.0418  -0.0211 0.0247  258 GLU   A C   
1749 C C   B GLU   A 236 ? 0.3177 0.4183 0.1732 0.0347  -0.0186 0.0208  258 GLU   A C   
1750 O O   A GLU   A 236 ? 0.3034 0.4096 0.1771 0.0359  -0.0344 0.0273  258 GLU   A O   
1751 O O   B GLU   A 236 ? 0.3032 0.4155 0.1713 0.0276  -0.0313 0.0297  258 GLU   A O   
1752 C CB  A GLU   A 236 ? 0.3781 0.4145 0.2508 0.0533  0.0175  0.0036  258 GLU   A CB  
1753 C CB  B GLU   A 236 ? 0.3669 0.4409 0.1947 0.0203  0.0078  -0.0220 258 GLU   A CB  
1754 C CG  A GLU   A 236 ? 0.3860 0.4101 0.2743 0.0671  0.0379  0.0077  258 GLU   A CG  
1755 C CG  B GLU   A 236 ? 0.3706 0.4409 0.1735 0.0147  0.0204  -0.0353 258 GLU   A CG  
1756 C CD  A GLU   A 236 ? 0.4221 0.4070 0.3073 0.0725  0.0624  -0.0010 258 GLU   A CD  
1757 C CD  B GLU   A 236 ? 0.3966 0.4477 0.1968 0.0131  0.0457  -0.0519 258 GLU   A CD  
1758 O OE1 A GLU   A 236 ? 0.4358 0.4292 0.2931 0.0761  0.1085  -0.0113 258 GLU   A OE1 
1759 O OE1 B GLU   A 236 ? 0.4236 0.4752 0.1335 0.0065  0.0159  -0.0677 258 GLU   A OE1 
1760 O OE2 A GLU   A 236 ? 0.4458 0.3944 0.3660 0.0999  0.0637  -0.0231 258 GLU   A OE2 
1761 O OE2 B GLU   A 236 ? 0.4238 0.4553 0.2313 0.0046  0.1013  -0.0765 258 GLU   A OE2 
1762 N N   . LYS   A 237 ? 0.3217 0.4146 0.1688 0.0355  -0.0028 0.0141  259 LYS   A N   
1763 C CA  . LYS   A 237 ? 0.3271 0.4188 0.1755 0.0450  -0.0076 0.0437  259 LYS   A CA  
1764 C C   . LYS   A 237 ? 0.3167 0.4069 0.1949 0.0422  -0.0188 0.0366  259 LYS   A C   
1765 O O   . LYS   A 237 ? 0.3485 0.3936 0.2075 0.0496  -0.0452 0.0371  259 LYS   A O   
1766 C CB  . LYS   A 237 ? 0.3537 0.4520 0.2151 0.0255  0.0017  0.0471  259 LYS   A CB  
1767 C CG  . LYS   A 237 ? 0.4103 0.5064 0.2689 0.0146  0.0223  0.0319  259 LYS   A CG  
1768 C CD  . LYS   A 237 ? 0.4178 0.5466 0.3337 0.0056  0.0330  0.0302  259 LYS   A CD  
1769 C CE  . LYS   A 237 ? 0.4658 0.5878 0.4067 0.0070  0.0547  0.0206  259 LYS   A CE  
1770 N NZ  . LYS   A 237 ? 0.4935 0.6384 0.4845 -0.0016 0.0753  0.0197  259 LYS   A NZ  
1771 N N   . TYR   A 238 ? 0.2982 0.3888 0.1994 0.0470  -0.0168 0.0396  260 TYR   A N   
1772 C CA  . TYR   A 238 ? 0.2869 0.3644 0.2062 0.0471  0.0082  0.0326  260 TYR   A CA  
1773 C C   . TYR   A 238 ? 0.2815 0.3403 0.1901 0.0611  0.0169  0.0344  260 TYR   A C   
1774 O O   . TYR   A 238 ? 0.2839 0.3552 0.1798 0.0589  0.0247  0.0273  260 TYR   A O   
1775 C CB  . TYR   A 238 ? 0.2788 0.3628 0.2086 0.0481  0.0034  0.0323  260 TYR   A CB  
1776 C CG  . TYR   A 238 ? 0.2832 0.3601 0.1975 0.0584  0.0074  0.0349  260 TYR   A CG  
1777 C CD1 . TYR   A 238 ? 0.2910 0.3641 0.2106 0.0593  0.0187  0.0205  260 TYR   A CD1 
1778 C CD2 . TYR   A 238 ? 0.2900 0.3702 0.2047 0.0641  -0.0002 0.0286  260 TYR   A CD2 
1779 C CE1 . TYR   A 238 ? 0.3061 0.3434 0.2421 0.0550  0.0066  0.0339  260 TYR   A CE1 
1780 C CE2 . TYR   A 238 ? 0.2884 0.3732 0.2645 0.0610  -0.0023 0.0367  260 TYR   A CE2 
1781 C CZ  . TYR   A 238 ? 0.2835 0.3747 0.2699 0.0596  -0.0026 0.0376  260 TYR   A CZ  
1782 O OH  . TYR   A 238 ? 0.3078 0.4407 0.3445 0.0471  0.0010  0.0634  260 TYR   A OH  
1783 N N   . CYS   A 239 ? 0.2945 0.3413 0.1672 0.0370  0.0195  0.0323  261 CYS   A N   
1784 C CA  . CYS   A 239 ? 0.2627 0.3125 0.1574 0.0411  0.0049  0.0390  261 CYS   A CA  
1785 C C   . CYS   A 239 ? 0.2291 0.3027 0.1694 0.0283  -0.0105 0.0170  261 CYS   A C   
1786 O O   . CYS   A 239 ? 0.2773 0.2799 0.1986 0.0300  -0.0309 0.0085  261 CYS   A O   
1787 C CB  . CYS   A 239 ? 0.2520 0.3242 0.1461 0.0381  0.0066  0.0383  261 CYS   A CB  
1788 S SG  . CYS   A 239 ? 0.2435 0.3675 0.1805 0.0357  -0.0114 0.0494  261 CYS   A SG  
1789 N N   . ILE   A 240 ? 0.2245 0.3001 0.1790 0.0208  -0.0165 0.0171  262 ILE   A N   
1790 C CA  . ILE   A 240 ? 0.2430 0.3132 0.1746 0.0316  -0.0134 0.0271  262 ILE   A CA  
1791 C C   . ILE   A 240 ? 0.2474 0.3149 0.1909 0.0228  -0.0033 0.0320  262 ILE   A C   
1792 O O   . ILE   A 240 ? 0.2569 0.3221 0.2017 0.0234  -0.0129 0.0104  262 ILE   A O   
1793 C CB  . ILE   A 240 ? 0.2665 0.3262 0.1920 0.0381  -0.0171 0.0294  262 ILE   A CB  
1794 C CG1 . ILE   A 240 ? 0.2996 0.3544 0.1729 0.0484  -0.0267 0.0281  262 ILE   A CG1 
1795 C CG2 . ILE   A 240 ? 0.2682 0.3366 0.1897 0.0464  -0.0157 0.0300  262 ILE   A CG2 
1796 C CD1 . ILE   A 240 ? 0.3162 0.3639 0.1777 0.0533  -0.0207 0.0340  262 ILE   A CD1 
1797 N N   . PHE   A 241 ? 0.2456 0.3054 0.1986 0.0176  0.0154  0.0249  263 PHE   A N   
1798 C CA  . PHE   A 241 ? 0.2684 0.2894 0.2076 0.0063  0.0186  0.0509  263 PHE   A CA  
1799 C C   . PHE   A 241 ? 0.2828 0.2994 0.2504 0.0124  0.0228  0.0445  263 PHE   A C   
1800 O O   . PHE   A 241 ? 0.3239 0.3206 0.3355 0.0412  0.0681  0.0757  263 PHE   A O   
1801 C CB  . PHE   A 241 ? 0.2573 0.2746 0.2112 -0.0003 0.0285  0.0459  263 PHE   A CB  
1802 C CG  . PHE   A 241 ? 0.2500 0.2719 0.1998 -0.0008 0.0227  0.0497  263 PHE   A CG  
1803 C CD1 . PHE   A 241 ? 0.2370 0.2717 0.1769 -0.0004 0.0137  0.0498  263 PHE   A CD1 
1804 C CD2 . PHE   A 241 ? 0.2345 0.2617 0.2060 -0.0030 0.0152  0.0468  263 PHE   A CD2 
1805 C CE1 . PHE   A 241 ? 0.2488 0.2715 0.1845 -0.0032 0.0239  0.0422  263 PHE   A CE1 
1806 C CE2 . PHE   A 241 ? 0.2437 0.2713 0.2104 -0.0039 0.0147  0.0426  263 PHE   A CE2 
1807 C CZ  . PHE   A 241 ? 0.2473 0.2667 0.2155 0.0015  0.0268  0.0489  263 PHE   A CZ  
1808 N N   . ALA   A 242 ? 0.2710 0.2886 0.2066 -0.0114 -0.0055 0.0346  264 ALA   A N   
1809 C CA  . ALA   A 242 ? 0.2719 0.2787 0.2090 -0.0130 -0.0086 0.0122  264 ALA   A CA  
1810 C C   . ALA   A 242 ? 0.2568 0.2568 0.2050 -0.0109 -0.0146 0.0149  264 ALA   A C   
1811 O O   . ALA   A 242 ? 0.2587 0.2766 0.1885 0.0004  -0.0166 0.0170  264 ALA   A O   
1812 C CB  . ALA   A 242 ? 0.2695 0.2747 0.2416 -0.0254 -0.0062 0.0097  264 ALA   A CB  
1813 N N   . ASN   A 243 ? 0.2528 0.2497 0.2296 -0.0075 -0.0251 0.0106  265 ASN   A N   
1814 C CA  . ASN   A 243 ? 0.2597 0.2521 0.2332 -0.0232 -0.0265 0.0100  265 ASN   A CA  
1815 C C   . ASN   A 243 ? 0.2619 0.2455 0.2465 -0.0151 -0.0342 0.0036  265 ASN   A C   
1816 O O   . ASN   A 243 ? 0.2451 0.2755 0.2446 -0.0095 -0.0292 -0.0096 265 ASN   A O   
1817 C CB  . ASN   A 243 ? 0.2583 0.2725 0.2569 -0.0373 -0.0322 0.0319  265 ASN   A CB  
1818 C CG  . ASN   A 243 ? 0.2603 0.2860 0.2716 -0.0428 -0.0339 0.0409  265 ASN   A CG  
1819 O OD1 . ASN   A 243 ? 0.2648 0.3901 0.3036 -0.0484 -0.0185 0.0532  265 ASN   A OD1 
1820 N ND2 . ASN   A 243 ? 0.2818 0.2510 0.2861 -0.0537 -0.0293 0.0385  265 ASN   A ND2 
1821 N N   . PHE   A 244 ? 0.2633 0.2405 0.2534 -0.0143 -0.0304 0.0049  266 PHE   A N   
1822 C CA  . PHE   A 244 ? 0.2780 0.2331 0.2673 -0.0194 -0.0387 0.0000  266 PHE   A CA  
1823 C C   . PHE   A 244 ? 0.3075 0.2391 0.2501 -0.0031 -0.0424 -0.0160 266 PHE   A C   
1824 O O   . PHE   A 244 ? 0.3284 0.2541 0.2554 0.0103  -0.0563 -0.0478 266 PHE   A O   
1825 C CB  . PHE   A 244 ? 0.2671 0.2265 0.2634 -0.0373 -0.0311 0.0253  266 PHE   A CB  
1826 C CG  . PHE   A 244 ? 0.2775 0.2229 0.2683 -0.0492 -0.0347 0.0401  266 PHE   A CG  
1827 C CD1 . PHE   A 244 ? 0.2691 0.2320 0.2628 -0.0491 -0.0180 0.0482  266 PHE   A CD1 
1828 C CD2 . PHE   A 244 ? 0.2874 0.2586 0.2933 -0.0602 -0.0534 0.0348  266 PHE   A CD2 
1829 C CE1 . PHE   A 244 ? 0.2747 0.2314 0.2770 -0.0601 -0.0222 0.0344  266 PHE   A CE1 
1830 C CE2 . PHE   A 244 ? 0.2703 0.2514 0.3004 -0.0739 -0.0408 0.0421  266 PHE   A CE2 
1831 C CZ  . PHE   A 244 ? 0.2606 0.2357 0.2735 -0.0676 -0.0171 0.0443  266 PHE   A CZ  
1832 N N   . SER   A 245 ? 0.3120 0.2219 0.2290 -0.0003 -0.0386 -0.0132 267 SER   A N   
1833 C CA  . SER   A 245 ? 0.3080 0.2490 0.2268 -0.0210 -0.0475 -0.0061 267 SER   A CA  
1834 C C   . SER   A 245 ? 0.3189 0.2360 0.2339 -0.0244 -0.0468 0.0139  267 SER   A C   
1835 O O   . SER   A 245 ? 0.3318 0.2316 0.2502 -0.0279 -0.0291 0.0146  267 SER   A O   
1836 C CB  . SER   A 245 ? 0.2975 0.2783 0.2366 -0.0202 -0.0601 0.0034  267 SER   A CB  
1837 O OG  . SER   A 245 ? 0.3268 0.2945 0.2517 -0.0088 -0.0688 0.0413  267 SER   A OG  
1838 N N   . VAL   A 246 ? 0.3128 0.2488 0.2237 -0.0245 -0.0446 0.0386  268 VAL   A N   
1839 C CA  . VAL   A 246 ? 0.3161 0.2851 0.2612 -0.0266 -0.0457 0.0572  268 VAL   A CA  
1840 C C   . VAL   A 246 ? 0.3278 0.2846 0.2418 -0.0383 -0.0456 0.0656  268 VAL   A C   
1841 O O   . VAL   A 246 ? 0.3363 0.2888 0.2642 -0.0547 -0.0422 0.0793  268 VAL   A O   
1842 C CB  . VAL   A 246 ? 0.3122 0.3176 0.3062 -0.0172 -0.0459 0.0662  268 VAL   A CB  
1843 C CG1 . VAL   A 246 ? 0.3199 0.3285 0.3007 -0.0095 -0.0388 0.0874  268 VAL   A CG1 
1844 C CG2 . VAL   A 246 ? 0.3376 0.3388 0.3311 -0.0148 -0.0539 0.0431  268 VAL   A CG2 
1845 N N   . THR   A 247 ? 0.3404 0.2726 0.2094 -0.0411 -0.0676 0.0484  269 THR   A N   
1846 C CA  . THR   A 247 ? 0.3306 0.2579 0.2335 -0.0385 -0.0746 0.0423  269 THR   A CA  
1847 C C   . THR   A 247 ? 0.3388 0.2605 0.2606 -0.0430 -0.0694 0.0475  269 THR   A C   
1848 O O   . THR   A 247 ? 0.3691 0.2564 0.2890 -0.0081 -0.0796 0.0560  269 THR   A O   
1849 C CB  . THR   A 247 ? 0.3361 0.2374 0.2336 -0.0490 -0.0662 0.0355  269 THR   A CB  
1850 O OG1 . THR   A 247 ? 0.3527 0.2253 0.2427 -0.0705 -0.0667 0.0302  269 THR   A OG1 
1851 C CG2 . THR   A 247 ? 0.3415 0.2536 0.2366 -0.0463 -0.0525 0.0293  269 THR   A CG2 
1852 N N   . GLY   A 248 ? 0.3347 0.2668 0.2720 -0.0494 -0.0881 0.0390  270 GLY   A N   
1853 C CA  . GLY   A 248 ? 0.3664 0.2833 0.2965 -0.0273 -0.0757 0.0242  270 GLY   A CA  
1854 C C   . GLY   A 248 ? 0.3821 0.2754 0.3136 -0.0347 -0.0623 0.0108  270 GLY   A C   
1855 O O   . GLY   A 248 ? 0.3798 0.2897 0.3244 -0.0462 -0.0388 0.0194  270 GLY   A O   
1856 N N   . GLY   A 249 ? 0.3972 0.2907 0.3265 -0.0233 -0.0499 -0.0073 271 GLY   A N   
1857 C CA  . GLY   A 249 ? 0.3936 0.3046 0.3230 -0.0359 -0.0596 0.0109  271 GLY   A CA  
1858 C C   . GLY   A 249 ? 0.4157 0.2776 0.3208 -0.0531 -0.0747 0.0246  271 GLY   A C   
1859 O O   . GLY   A 249 ? 0.4514 0.2804 0.3230 -0.0583 -0.0851 0.0082  271 GLY   A O   
1860 N N   . LYS   A 250 ? 0.4205 0.2471 0.3302 -0.0591 -0.0678 0.0200  272 LYS   A N   
1861 C CA  . LYS   A 250 ? 0.4117 0.2745 0.2995 -0.0436 -0.0714 0.0157  272 LYS   A CA  
1862 C C   . LYS   A 250 ? 0.4183 0.2678 0.3041 -0.0587 -0.0673 0.0056  272 LYS   A C   
1863 O O   . LYS   A 250 ? 0.4362 0.2472 0.3034 -0.0668 -0.0704 0.0075  272 LYS   A O   
1864 C CB  . LYS   A 250 ? 0.4046 0.2653 0.3133 -0.0346 -0.0566 0.0240  272 LYS   A CB  
1865 C CG  . LYS   A 250 ? 0.4217 0.3336 0.3328 -0.0201 -0.0350 0.0268  272 LYS   A CG  
1866 C CD  . LYS   A 250 ? 0.4393 0.3635 0.3435 -0.0253 -0.0243 0.0146  272 LYS   A CD  
1867 C CE  . LYS   A 250 ? 0.4716 0.4241 0.3770 -0.0153 0.0265  0.0231  272 LYS   A CE  
1868 N NZ  . LYS   A 250 ? 0.5029 0.4587 0.4074 0.0104  0.0313  0.0448  272 LYS   A NZ  
1869 N N   . TRP   A 251 ? 0.3872 0.2477 0.2696 -0.0477 -0.0746 0.0030  273 TRP   A N   
1870 C CA  . TRP   A 251 ? 0.3623 0.2584 0.2723 -0.0345 -0.0715 -0.0055 273 TRP   A CA  
1871 C C   . TRP   A 251 ? 0.3316 0.2488 0.2513 -0.0279 -0.0653 -0.0025 273 TRP   A C   
1872 O O   . TRP   A 251 ? 0.3144 0.2476 0.2443 -0.0214 -0.0513 0.0141  273 TRP   A O   
1873 C CB  . TRP   A 251 ? 0.3689 0.2761 0.2778 -0.0482 -0.0748 -0.0003 273 TRP   A CB  
1874 C CG  . TRP   A 251 ? 0.3845 0.3164 0.2850 -0.0331 -0.0737 0.0040  273 TRP   A CG  
1875 C CD1 . TRP   A 251 ? 0.3902 0.3260 0.2921 -0.0296 -0.0924 0.0169  273 TRP   A CD1 
1876 C CD2 . TRP   A 251 ? 0.4049 0.3277 0.2976 -0.0222 -0.0809 0.0097  273 TRP   A CD2 
1877 N NE1 . TRP   A 251 ? 0.4062 0.3629 0.3069 -0.0054 -0.1017 0.0052  273 TRP   A NE1 
1878 C CE2 . TRP   A 251 ? 0.4122 0.3496 0.3130 -0.0275 -0.0948 0.0136  273 TRP   A CE2 
1879 C CE3 . TRP   A 251 ? 0.4117 0.3343 0.3212 -0.0381 -0.1075 0.0221  273 TRP   A CE3 
1880 C CZ2 . TRP   A 251 ? 0.4399 0.3556 0.3270 -0.0100 -0.0934 0.0092  273 TRP   A CZ2 
1881 C CZ3 . TRP   A 251 ? 0.4302 0.3479 0.3421 -0.0286 -0.1116 0.0102  273 TRP   A CZ3 
1882 C CH2 . TRP   A 251 ? 0.4388 0.3492 0.3422 -0.0273 -0.1032 0.0300  273 TRP   A CH2 
1883 N N   . ILE   A 252 ? 0.3233 0.2487 0.2572 -0.0099 -0.0690 -0.0129 274 ILE   A N   
1884 C CA  . ILE   A 252 ? 0.3186 0.2542 0.2320 -0.0058 -0.0580 -0.0012 274 ILE   A CA  
1885 C C   . ILE   A 252 ? 0.3187 0.2654 0.2389 0.0117  -0.0596 0.0015  274 ILE   A C   
1886 O O   . ILE   A 252 ? 0.3105 0.2886 0.2525 0.0059  -0.0238 0.0163  274 ILE   A O   
1887 C CB  . ILE   A 252 ? 0.3277 0.2603 0.2495 -0.0081 -0.0635 -0.0047 274 ILE   A CB  
1888 C CG1 . ILE   A 252 ? 0.3345 0.2591 0.2584 -0.0077 -0.0562 -0.0126 274 ILE   A CG1 
1889 C CG2 . ILE   A 252 ? 0.3277 0.2788 0.2319 0.0017  -0.0765 0.0033  274 ILE   A CG2 
1890 C CD1 . ILE   A 252 ? 0.3349 0.2855 0.2668 -0.0014 -0.0571 -0.0151 274 ILE   A CD1 
1891 N N   . VAL   A 253 ? 0.2749 0.2594 0.2427 0.0156  -0.0626 -0.0099 275 VAL   A N   
1892 C CA  . VAL   A 253 ? 0.2826 0.2663 0.2512 0.0142  -0.0548 -0.0069 275 VAL   A CA  
1893 C C   . VAL   A 253 ? 0.2556 0.2820 0.2369 0.0212  -0.0405 0.0040  275 VAL   A C   
1894 O O   . VAL   A 253 ? 0.2392 0.3001 0.2565 0.0268  0.0056  0.0108  275 VAL   A O   
1895 C CB  . VAL   A 253 ? 0.2740 0.2675 0.2645 0.0089  -0.0585 -0.0084 275 VAL   A CB  
1896 C CG1 . VAL   A 253 ? 0.2952 0.2632 0.2930 0.0011  -0.0592 -0.0092 275 VAL   A CG1 
1897 C CG2 . VAL   A 253 ? 0.2759 0.2567 0.2683 0.0171  -0.0539 -0.0161 275 VAL   A CG2 
1898 N N   . SER   A 254 ? 0.2611 0.2943 0.2244 0.0409  -0.0412 -0.0041 276 SER   A N   
1899 C CA  . SER   A 254 ? 0.2857 0.3054 0.2205 0.0272  -0.0218 0.0053  276 SER   A CA  
1900 C C   . SER   A 254 ? 0.2933 0.2999 0.2340 0.0421  -0.0236 0.0046  276 SER   A C   
1901 O O   . SER   A 254 ? 0.3019 0.3181 0.2481 0.0690  -0.0027 -0.0149 276 SER   A O   
1902 C CB  . SER   A 254 ? 0.3016 0.3150 0.2280 0.0202  -0.0247 0.0030  276 SER   A CB  
1903 O OG  . SER   A 254 ? 0.3181 0.3422 0.2022 0.0128  -0.0582 0.0017  276 SER   A OG  
1904 N N   . GLY   A 255 ? 0.2994 0.2711 0.2271 0.0368  -0.0231 -0.0034 277 GLY   A N   
1905 C CA  . GLY   A 255 ? 0.2945 0.2783 0.2244 0.0372  -0.0321 0.0049  277 GLY   A CA  
1906 C C   . GLY   A 255 ? 0.3037 0.3023 0.2349 0.0318  -0.0349 -0.0085 277 GLY   A C   
1907 O O   . GLY   A 255 ? 0.3032 0.2945 0.2276 0.0352  -0.0294 -0.0304 277 GLY   A O   
1908 N N   . SER   A 256 ? 0.2972 0.3313 0.2028 0.0363  -0.0438 -0.0196 278 SER   A N   
1909 C CA  . SER   A 256 ? 0.3143 0.3215 0.2073 0.0556  -0.0339 -0.0183 278 SER   A CA  
1910 C C   . SER   A 256 ? 0.3136 0.3350 0.2076 0.0500  -0.0270 -0.0190 278 SER   A C   
1911 O O   . SER   A 256 ? 0.3080 0.3464 0.1989 0.0444  -0.0088 -0.0064 278 SER   A O   
1912 C CB  . SER   A 256 ? 0.3315 0.3250 0.2218 0.0673  -0.0543 -0.0263 278 SER   A CB  
1913 O OG  . SER   A 256 ? 0.3477 0.3268 0.2359 0.0775  -0.0375 -0.0324 278 SER   A OG  
1914 N N   . GLU   A 257 ? 0.2909 0.3261 0.1943 0.0532  -0.0144 -0.0141 279 GLU   A N   
1915 C CA  . GLU   A 257 ? 0.2915 0.3510 0.2022 0.0602  -0.0149 -0.0050 279 GLU   A CA  
1916 C C   . GLU   A 257 ? 0.2992 0.3753 0.2141 0.0639  0.0009  -0.0109 279 GLU   A C   
1917 O O   . GLU   A 257 ? 0.2979 0.3787 0.2158 0.0623  0.0199  0.0110  279 GLU   A O   
1918 C CB  . GLU   A 257 ? 0.2922 0.3598 0.1855 0.0581  -0.0151 -0.0168 279 GLU   A CB  
1919 C CG  . GLU   A 257 ? 0.2940 0.3562 0.1783 0.0643  -0.0157 -0.0145 279 GLU   A CG  
1920 C CD  . GLU   A 257 ? 0.3049 0.3687 0.1687 0.0625  -0.0147 -0.0220 279 GLU   A CD  
1921 O OE1 . GLU   A 257 ? 0.3197 0.3395 0.1582 0.0628  -0.0051 -0.0209 279 GLU   A OE1 
1922 O OE2 . GLU   A 257 ? 0.2806 0.4069 0.1936 0.0738  -0.0228 -0.0136 279 GLU   A OE2 
1923 N N   . ASP   A 258 ? 0.3046 0.3966 0.2228 0.0738  -0.0166 -0.0087 280 ASP   A N   
1924 C CA  . ASP   A 258 ? 0.3150 0.4090 0.2420 0.0893  -0.0098 -0.0400 280 ASP   A CA  
1925 C C   . ASP   A 258 ? 0.3063 0.4395 0.2400 0.0985  -0.0113 -0.0429 280 ASP   A C   
1926 O O   . ASP   A 258 ? 0.2941 0.4532 0.2464 0.1126  -0.0146 -0.0772 280 ASP   A O   
1927 C CB  . ASP   A 258 ? 0.3302 0.4026 0.2462 0.0922  -0.0180 -0.0636 280 ASP   A CB  
1928 C CG  . ASP   A 258 ? 0.3581 0.3972 0.2401 0.1015  -0.0090 -0.0790 280 ASP   A CG  
1929 O OD1 . ASP   A 258 ? 0.3294 0.4176 0.2086 0.1300  -0.0092 -0.0628 280 ASP   A OD1 
1930 O OD2 . ASP   A 258 ? 0.4114 0.3681 0.2707 0.1095  -0.0204 -0.1012 280 ASP   A OD2 
1931 N N   . ASN   A 259 ? 0.2964 0.4551 0.2362 0.1056  0.0090  -0.0335 281 ASN   A N   
1932 C CA  . ASN   A 259 ? 0.2703 0.4717 0.2340 0.0844  0.0087  -0.0061 281 ASN   A CA  
1933 C C   . ASN   A 259 ? 0.2761 0.4524 0.2626 0.0919  -0.0061 -0.0053 281 ASN   A C   
1934 O O   . ASN   A 259 ? 0.2477 0.4470 0.2738 0.0658  -0.0074 -0.0054 281 ASN   A O   
1935 C CB  . ASN   A 259 ? 0.2788 0.5020 0.2378 0.0818  0.0137  -0.0002 281 ASN   A CB  
1936 C CG  . ASN   A 259 ? 0.2665 0.5352 0.2214 0.0736  0.0273  -0.0076 281 ASN   A CG  
1937 O OD1 . ASN   A 259 ? 0.2907 0.5435 0.2215 0.1070  0.0360  -0.0190 281 ASN   A OD1 
1938 N ND2 . ASN   A 259 ? 0.2654 0.5546 0.2297 0.0548  0.0316  -0.0195 281 ASN   A ND2 
1939 N N   . LEU   A 260 ? 0.2849 0.4091 0.2579 0.0900  -0.0168 -0.0122 282 LEU   A N   
1940 C CA  . LEU   A 260 ? 0.2926 0.3836 0.2626 0.1060  -0.0299 -0.0229 282 LEU   A CA  
1941 C C   . LEU   A 260 ? 0.2929 0.3553 0.2436 0.0877  -0.0321 -0.0348 282 LEU   A C   
1942 O O   . LEU   A 260 ? 0.2677 0.3696 0.2246 0.1002  -0.0210 -0.0500 282 LEU   A O   
1943 C CB  . LEU   A 260 ? 0.3277 0.3895 0.2707 0.1147  -0.0449 -0.0244 282 LEU   A CB  
1944 C CG  . LEU   A 260 ? 0.3434 0.4048 0.2737 0.1052  -0.0297 -0.0099 282 LEU   A CG  
1945 C CD1 . LEU   A 260 ? 0.3643 0.3870 0.2672 0.1044  -0.0430 0.0130  282 LEU   A CD1 
1946 C CD2 . LEU   A 260 ? 0.3420 0.4032 0.2750 0.0984  -0.0304 -0.0300 282 LEU   A CD2 
1947 N N   . VAL   A 261 ? 0.2762 0.3248 0.2496 0.0832  -0.0341 -0.0248 283 VAL   A N   
1948 C CA  . VAL   A 261 ? 0.3032 0.3198 0.2487 0.0731  -0.0309 -0.0387 283 VAL   A CA  
1949 C C   . VAL   A 261 ? 0.3079 0.3148 0.2473 0.0590  -0.0289 -0.0458 283 VAL   A C   
1950 O O   . VAL   A 261 ? 0.3191 0.3211 0.2493 0.0698  -0.0215 -0.0659 283 VAL   A O   
1951 C CB  . VAL   A 261 ? 0.2924 0.3220 0.2457 0.0617  -0.0396 -0.0466 283 VAL   A CB  
1952 C CG1 . VAL   A 261 ? 0.3002 0.3287 0.2223 0.0440  -0.0356 -0.0477 283 VAL   A CG1 
1953 C CG2 . VAL   A 261 ? 0.2907 0.3308 0.2606 0.0495  -0.0457 -0.0416 283 VAL   A CG2 
1954 N N   . TYR   A 262 ? 0.3048 0.3027 0.2121 0.0630  -0.0237 -0.0394 284 TYR   A N   
1955 C CA  . TYR   A 262 ? 0.3248 0.2726 0.2233 0.0616  -0.0271 -0.0446 284 TYR   A CA  
1956 C C   . TYR   A 262 ? 0.3460 0.2532 0.2543 0.0431  -0.0353 -0.0280 284 TYR   A C   
1957 O O   . TYR   A 262 ? 0.3302 0.2558 0.2191 0.0385  -0.0409 -0.0323 284 TYR   A O   
1958 C CB  . TYR   A 262 ? 0.3169 0.2818 0.2501 0.0696  -0.0318 -0.0381 284 TYR   A CB  
1959 C CG  . TYR   A 262 ? 0.3307 0.2937 0.2362 0.0681  -0.0280 -0.0258 284 TYR   A CG  
1960 C CD1 . TYR   A 262 ? 0.3292 0.3117 0.2545 0.0687  -0.0200 -0.0473 284 TYR   A CD1 
1961 C CD2 . TYR   A 262 ? 0.3563 0.3079 0.2592 0.0690  -0.0202 -0.0292 284 TYR   A CD2 
1962 C CE1 . TYR   A 262 ? 0.3510 0.3233 0.2355 0.0658  -0.0093 -0.0382 284 TYR   A CE1 
1963 C CE2 . TYR   A 262 ? 0.3641 0.3129 0.2548 0.0746  -0.0267 -0.0304 284 TYR   A CE2 
1964 C CZ  . TYR   A 262 ? 0.3514 0.3293 0.2487 0.0677  -0.0160 -0.0440 284 TYR   A CZ  
1965 O OH  . TYR   A 262 ? 0.3870 0.3364 0.2508 0.1042  -0.0275 -0.1089 284 TYR   A OH  
1966 N N   . ILE   A 263 ? 0.3687 0.2539 0.2465 0.0510  -0.0570 -0.0071 285 ILE   A N   
1967 C CA  . ILE   A 263 ? 0.3609 0.2503 0.2689 0.0355  -0.0619 -0.0262 285 ILE   A CA  
1968 C C   . ILE   A 263 ? 0.3835 0.2542 0.2801 0.0314  -0.0750 -0.0327 285 ILE   A C   
1969 O O   . ILE   A 263 ? 0.4055 0.2435 0.3088 0.0446  -0.0810 -0.0366 285 ILE   A O   
1970 C CB  . ILE   A 263 ? 0.3554 0.2588 0.2631 0.0331  -0.0687 -0.0239 285 ILE   A CB  
1971 C CG1 . ILE   A 263 ? 0.3420 0.2872 0.2720 0.0263  -0.0645 -0.0054 285 ILE   A CG1 
1972 C CG2 . ILE   A 263 ? 0.3725 0.2488 0.2834 0.0310  -0.0782 -0.0178 285 ILE   A CG2 
1973 C CD1 . ILE   A 263 ? 0.3444 0.3188 0.2595 0.0163  -0.0601 -0.0100 285 ILE   A CD1 
1974 N N   . TRP   A 264 ? 0.3656 0.2438 0.2412 0.0168  -0.0734 -0.0227 286 TRP   A N   
1975 C CA  . TRP   A 264 ? 0.3882 0.2242 0.2594 0.0137  -0.0587 -0.0244 286 TRP   A CA  
1976 C C   . TRP   A 264 ? 0.3994 0.2282 0.2734 -0.0104 -0.0557 -0.0287 286 TRP   A C   
1977 O O   . TRP   A 264 ? 0.3973 0.2254 0.2640 -0.0211 -0.0666 -0.0348 286 TRP   A O   
1978 C CB  . TRP   A 264 ? 0.3962 0.2316 0.2435 0.0119  -0.0644 -0.0351 286 TRP   A CB  
1979 C CG  . TRP   A 264 ? 0.3823 0.2628 0.2577 0.0080  -0.0381 -0.0447 286 TRP   A CG  
1980 C CD1 . TRP   A 264 ? 0.3973 0.2573 0.2588 -0.0093 -0.0445 -0.0409 286 TRP   A CD1 
1981 C CD2 . TRP   A 264 ? 0.3735 0.2562 0.2351 0.0191  -0.0455 -0.0400 286 TRP   A CD2 
1982 N NE1 . TRP   A 264 ? 0.4148 0.2880 0.2463 0.0029  -0.0517 -0.0373 286 TRP   A NE1 
1983 C CE2 . TRP   A 264 ? 0.3911 0.2652 0.2330 0.0127  -0.0472 -0.0440 286 TRP   A CE2 
1984 C CE3 . TRP   A 264 ? 0.3537 0.2626 0.2249 0.0235  -0.0545 -0.0420 286 TRP   A CE3 
1985 C CZ2 . TRP   A 264 ? 0.3727 0.2697 0.2124 0.0283  -0.0622 -0.0464 286 TRP   A CZ2 
1986 C CZ3 . TRP   A 264 ? 0.3508 0.2721 0.2207 0.0325  -0.0581 -0.0368 286 TRP   A CZ3 
1987 C CH2 . TRP   A 264 ? 0.3649 0.2714 0.2135 0.0306  -0.0623 -0.0423 286 TRP   A CH2 
1988 N N   . ASN   A 265 ? 0.4161 0.2145 0.2902 -0.0241 -0.0756 -0.0322 287 ASN   A N   
1989 C CA  . ASN   A 265 ? 0.4436 0.2567 0.3100 -0.0329 -0.0810 -0.0090 287 ASN   A CA  
1990 C C   . ASN   A 265 ? 0.4344 0.2535 0.2956 -0.0524 -0.0980 -0.0032 287 ASN   A C   
1991 O O   . ASN   A 265 ? 0.4589 0.2621 0.2971 -0.0401 -0.1102 -0.0212 287 ASN   A O   
1992 C CB  . ASN   A 265 ? 0.4744 0.2693 0.3492 -0.0390 -0.0950 -0.0119 287 ASN   A CB  
1993 C CG  . ASN   A 265 ? 0.4959 0.3121 0.3544 -0.0391 -0.0972 0.0105  287 ASN   A CG  
1994 O OD1 . ASN   A 265 ? 0.4955 0.3422 0.2937 -0.0547 -0.1468 -0.0321 287 ASN   A OD1 
1995 N ND2 . ASN   A 265 ? 0.5268 0.3039 0.4293 -0.0343 -0.1099 0.0262  287 ASN   A ND2 
1996 N N   . LEU   A 266 ? 0.4327 0.2491 0.2783 -0.0654 -0.0961 0.0147  288 LEU   A N   
1997 C CA  . LEU   A 266 ? 0.4280 0.2777 0.3002 -0.0819 -0.1017 -0.0072 288 LEU   A CA  
1998 C C   . LEU   A 266 ? 0.4683 0.2719 0.3233 -0.0925 -0.1169 -0.0068 288 LEU   A C   
1999 O O   . LEU   A 266 ? 0.4806 0.3046 0.3208 -0.0964 -0.1232 -0.0056 288 LEU   A O   
2000 C CB  . LEU   A 266 ? 0.4443 0.2939 0.2861 -0.0749 -0.0937 -0.0022 288 LEU   A CB  
2001 C CG  . LEU   A 266 ? 0.4381 0.2928 0.2760 -0.0858 -0.0998 0.0039  288 LEU   A CG  
2002 C CD1 . LEU   A 266 ? 0.4530 0.2877 0.2574 -0.0857 -0.0892 0.0202  288 LEU   A CD1 
2003 C CD2 . LEU   A 266 ? 0.4266 0.3156 0.2787 -0.0898 -0.1112 -0.0010 288 LEU   A CD2 
2004 N N   . GLN   A 267 ? 0.4869 0.2602 0.3550 -0.0823 -0.1176 -0.0078 289 GLN   A N   
2005 C CA  . GLN   A 267 ? 0.4927 0.2750 0.3935 -0.0982 -0.1245 0.0043  289 GLN   A CA  
2006 C C   . GLN   A 267 ? 0.4953 0.2746 0.3969 -0.0885 -0.1582 -0.0097 289 GLN   A C   
2007 O O   . GLN   A 267 ? 0.4967 0.2714 0.4155 -0.0764 -0.1878 -0.0088 289 GLN   A O   
2008 C CB  . GLN   A 267 ? 0.5564 0.3214 0.3895 -0.0787 -0.1160 0.0137  289 GLN   A CB  
2009 C CG  . GLN   A 267 ? 0.5740 0.3541 0.4299 -0.0963 -0.1140 -0.0113 289 GLN   A CG  
2010 C CD  . GLN   A 267 ? 0.5552 0.3864 0.4212 -0.1257 -0.1247 -0.0234 289 GLN   A CD  
2011 O OE1 . GLN   A 267 ? 0.5418 0.3941 0.4596 -0.1373 -0.1527 0.0085  289 GLN   A OE1 
2012 N NE2 . GLN   A 267 ? 0.5357 0.3833 0.4289 -0.1595 -0.1136 -0.0309 289 GLN   A NE2 
2013 N N   . THR   A 268 ? 0.5196 0.2399 0.4109 -0.0630 -0.1639 -0.0242 290 THR   A N   
2014 C CA  . THR   A 268 ? 0.5701 0.2964 0.4346 -0.0422 -0.1348 -0.0308 290 THR   A CA  
2015 C C   . THR   A 268 ? 0.5562 0.2736 0.3928 -0.0289 -0.1478 -0.0495 290 THR   A C   
2016 O O   . THR   A 268 ? 0.5879 0.2531 0.3969 -0.0213 -0.1472 -0.0784 290 THR   A O   
2017 C CB  . THR   A 268 ? 0.5736 0.2990 0.4471 -0.0193 -0.1294 -0.0184 290 THR   A CB  
2018 O OG1 . THR   A 268 ? 0.6128 0.2581 0.4384 -0.0210 -0.1230 -0.0306 290 THR   A OG1 
2019 C CG2 . THR   A 268 ? 0.5897 0.3028 0.4531 -0.0346 -0.1153 -0.0260 290 THR   A CG2 
2020 N N   . LYS   A 269 ? 0.5461 0.2780 0.3838 -0.0345 -0.1465 -0.0719 291 LYS   A N   
2021 C CA  . LYS   A 269 ? 0.5539 0.2952 0.4145 -0.0068 -0.1513 -0.0600 291 LYS   A CA  
2022 C C   . LYS   A 269 ? 0.5632 0.2950 0.3944 0.0143  -0.1502 -0.0538 291 LYS   A C   
2023 O O   . LYS   A 269 ? 0.5000 0.3314 0.4064 0.0132  -0.1575 -0.0621 291 LYS   A O   
2024 C CB  . LYS   A 269 ? 0.5669 0.3116 0.4527 -0.0206 -0.1603 -0.0681 291 LYS   A CB  
2025 C CG  . LYS   A 269 ? 0.5842 0.3779 0.4826 -0.0181 -0.1578 -0.0787 291 LYS   A CG  
2026 C CD  . LYS   A 269 ? 0.5955 0.4007 0.5085 -0.0288 -0.1665 -0.0884 291 LYS   A CD  
2027 C CE  . LYS   A 269 ? 0.6267 0.4125 0.5339 -0.0304 -0.1528 -0.0865 291 LYS   A CE  
2028 N NZ  . LYS   A 269 ? 0.6577 0.4140 0.5573 -0.0379 -0.1593 -0.1011 291 LYS   A NZ  
2029 N N   . GLU   A 270 ? 0.5519 0.2964 0.3647 0.0331  -0.1478 -0.0437 292 GLU   A N   
2030 C CA  . GLU   A 270 ? 0.5809 0.3262 0.3524 0.0296  -0.1164 -0.0412 292 GLU   A CA  
2031 C C   . GLU   A 270 ? 0.5343 0.2943 0.3078 0.0584  -0.1227 -0.0400 292 GLU   A C   
2032 O O   . GLU   A 270 ? 0.5035 0.2415 0.3111 0.0132  -0.1577 -0.0854 292 GLU   A O   
2033 C CB  . GLU   A 270 ? 0.6588 0.3295 0.4446 0.0477  -0.0674 -0.0150 292 GLU   A CB  
2034 C CG  . GLU   A 270 ? 0.7151 0.4040 0.5357 0.0440  -0.0280 0.0322  292 GLU   A CG  
2035 C CD  . GLU   A 270 ? 0.7913 0.4492 0.6401 0.1058  -0.0121 0.0909  292 GLU   A CD  
2036 O OE1 . GLU   A 270 ? 0.8526 0.4490 0.6951 0.1949  0.0033  0.1081  292 GLU   A OE1 
2037 O OE2 . GLU   A 270 ? 0.8244 0.5167 0.6982 0.1090  0.0523  0.1410  292 GLU   A OE2 
2038 N N   . ILE   A 271 ? 0.4909 0.3030 0.2912 0.0751  -0.1247 -0.0542 293 ILE   A N   
2039 C CA  . ILE   A 271 ? 0.4763 0.3174 0.3166 0.0761  -0.1088 -0.0500 293 ILE   A CA  
2040 C C   . ILE   A 271 ? 0.4914 0.2895 0.3161 0.0988  -0.1021 -0.0549 293 ILE   A C   
2041 O O   . ILE   A 271 ? 0.5067 0.3101 0.3405 0.1252  -0.0629 -0.1013 293 ILE   A O   
2042 C CB  . ILE   A 271 ? 0.4788 0.3549 0.3013 0.0493  -0.1066 -0.0373 293 ILE   A CB  
2043 C CG1 . ILE   A 271 ? 0.4752 0.3872 0.3486 0.0450  -0.1008 -0.0201 293 ILE   A CG1 
2044 C CG2 . ILE   A 271 ? 0.4738 0.3720 0.2985 0.0421  -0.0970 -0.0123 293 ILE   A CG2 
2045 C CD1 . ILE   A 271 ? 0.4764 0.4299 0.3705 0.0310  -0.0955 -0.0208 293 ILE   A CD1 
2046 N N   . VAL   A 272 ? 0.4779 0.2864 0.3239 0.0970  -0.1070 -0.0534 294 VAL   A N   
2047 C CA  . VAL   A 272 ? 0.4626 0.2969 0.3190 0.0900  -0.1183 -0.0441 294 VAL   A CA  
2048 C C   . VAL   A 272 ? 0.4297 0.3291 0.3207 0.0999  -0.0986 -0.0244 294 VAL   A C   
2049 O O   . VAL   A 272 ? 0.4067 0.3528 0.3439 0.0816  -0.1064 -0.0256 294 VAL   A O   
2050 C CB  . VAL   A 272 ? 0.4815 0.2954 0.3441 0.0678  -0.1175 -0.0126 294 VAL   A CB  
2051 C CG1 . VAL   A 272 ? 0.5038 0.3064 0.3514 0.0488  -0.1437 -0.0307 294 VAL   A CG1 
2052 C CG2 . VAL   A 272 ? 0.5090 0.2903 0.3023 0.0566  -0.1158 -0.0149 294 VAL   A CG2 
2053 N N   . GLN   A 273 ? 0.3851 0.3174 0.3085 0.1112  -0.1130 -0.0484 295 GLN   A N   
2054 C CA  . GLN   A 273 ? 0.4029 0.3447 0.3128 0.1049  -0.0922 -0.0531 295 GLN   A CA  
2055 C C   . GLN   A 273 ? 0.3889 0.3225 0.3063 0.1042  -0.0977 -0.0550 295 GLN   A C   
2056 O O   . GLN   A 273 ? 0.3871 0.2823 0.3378 0.1060  -0.0870 -0.0445 295 GLN   A O   
2057 C CB  . GLN   A 273 ? 0.3929 0.3816 0.3072 0.0858  -0.0894 -0.0609 295 GLN   A CB  
2058 C CG  . GLN   A 273 ? 0.4014 0.3904 0.3229 0.0910  -0.0911 -0.0648 295 GLN   A CG  
2059 C CD  . GLN   A 273 ? 0.3751 0.3557 0.2910 0.0996  -0.0824 -0.0622 295 GLN   A CD  
2060 O OE1 . GLN   A 273 ? 0.3383 0.3123 0.2734 0.0929  -0.0947 -0.0722 295 GLN   A OE1 
2061 N NE2 . GLN   A 273 ? 0.3909 0.3417 0.2941 0.1260  -0.0667 -0.0685 295 GLN   A NE2 
2062 N N   . LYS   A 274 ? 0.4015 0.3265 0.3186 0.0890  -0.0905 -0.0550 296 LYS   A N   
2063 C CA  . LYS   A 274 ? 0.3898 0.3284 0.3495 0.0744  -0.0991 -0.0610 296 LYS   A CA  
2064 C C   . LYS   A 274 ? 0.3663 0.3654 0.3502 0.0763  -0.1020 -0.0473 296 LYS   A C   
2065 O O   . LYS   A 274 ? 0.4340 0.3528 0.4533 0.1126  -0.1044 -0.0354 296 LYS   A O   
2066 C CB  . LYS   A 274 ? 0.4309 0.3300 0.3393 0.0748  -0.0847 -0.0441 296 LYS   A CB  
2067 C CG  . LYS   A 274 ? 0.4489 0.3467 0.3554 0.0553  -0.0775 -0.0624 296 LYS   A CG  
2068 C CD  . LYS   A 274 ? 0.5092 0.4020 0.3575 0.0577  -0.0376 -0.0661 296 LYS   A CD  
2069 C CE  . LYS   A 274 ? 0.5627 0.4369 0.3827 0.0461  -0.0238 -0.0501 296 LYS   A CE  
2070 N NZ  . LYS   A 274 ? 0.5691 0.4555 0.4190 0.0439  -0.0243 -0.0577 296 LYS   A NZ  
2071 N N   . LEU   A 275 ? 0.3209 0.3540 0.2981 0.0873  -0.0765 -0.0412 297 LEU   A N   
2072 C CA  . LEU   A 275 ? 0.3304 0.3686 0.2946 0.0708  -0.0417 -0.0248 297 LEU   A CA  
2073 C C   . LEU   A 275 ? 0.3234 0.3984 0.2704 0.0908  -0.0150 -0.0291 297 LEU   A C   
2074 O O   . LEU   A 275 ? 0.2903 0.3997 0.2306 0.0944  0.0159  -0.0359 297 LEU   A O   
2075 C CB  . LEU   A 275 ? 0.3236 0.3517 0.2818 0.0875  -0.0397 -0.0128 297 LEU   A CB  
2076 C CG  . LEU   A 275 ? 0.3487 0.3697 0.2943 0.0725  -0.0245 -0.0058 297 LEU   A CG  
2077 C CD1 . LEU   A 275 ? 0.3529 0.3817 0.2798 0.0665  -0.0347 -0.0122 297 LEU   A CD1 
2078 C CD2 . LEU   A 275 ? 0.3696 0.3793 0.2961 0.0513  -0.0064 0.0017  297 LEU   A CD2 
2079 N N   . GLN   A 276 ? 0.3121 0.3963 0.2969 0.1108  -0.0292 -0.0208 298 GLN   A N   
2080 C CA  . GLN   A 276 ? 0.3448 0.4264 0.3236 0.1009  -0.0258 -0.0225 298 GLN   A CA  
2081 C C   . GLN   A 276 ? 0.3345 0.4058 0.2947 0.1055  -0.0196 -0.0073 298 GLN   A C   
2082 O O   . GLN   A 276 ? 0.3255 0.3772 0.2815 0.0853  -0.0327 -0.0031 298 GLN   A O   
2083 C CB  . GLN   A 276 ? 0.4170 0.4324 0.3937 0.1102  -0.0299 -0.0393 298 GLN   A CB  
2084 C CG  . GLN   A 276 ? 0.4753 0.5003 0.4814 0.1330  -0.0207 -0.0439 298 GLN   A CG  
2085 C CD  . GLN   A 276 ? 0.5847 0.5839 0.5979 0.1191  -0.0203 -0.0249 298 GLN   A CD  
2086 O OE1 . GLN   A 276 ? 0.7472 0.6235 0.6254 0.1930  0.0469  -0.0371 298 GLN   A OE1 
2087 N NE2 . GLN   A 276 ? 0.6475 0.6448 0.6736 0.1607  -0.0586 0.0112  298 GLN   A NE2 
2088 N N   . GLY   A 277 ? 0.3054 0.4248 0.2701 0.0902  -0.0048 -0.0064 299 GLY   A N   
2089 C CA  . GLY   A 277 ? 0.2921 0.4202 0.2855 0.0971  -0.0035 0.0055  299 GLY   A CA  
2090 C C   . GLY   A 277 ? 0.2631 0.4308 0.2877 0.0808  0.0073  0.0030  299 GLY   A C   
2091 O O   . GLY   A 277 ? 0.2135 0.4640 0.3096 0.0744  0.0294  -0.0076 299 GLY   A O   
2092 N N   . HIS   A 278 ? 0.2647 0.4388 0.2707 0.0858  0.0164  -0.0022 300 HIS   A N   
2093 C CA  . HIS   A 278 ? 0.2616 0.4105 0.2343 0.0792  0.0153  -0.0092 300 HIS   A CA  
2094 C C   . HIS   A 278 ? 0.2499 0.4189 0.2419 0.0746  0.0225  -0.0040 300 HIS   A C   
2095 O O   . HIS   A 278 ? 0.2219 0.4286 0.2611 0.0665  0.0077  -0.0165 300 HIS   A O   
2096 C CB  . HIS   A 278 ? 0.2562 0.3827 0.2262 0.0729  -0.0042 -0.0149 300 HIS   A CB  
2097 C CG  . HIS   A 278 ? 0.2565 0.3749 0.2110 0.0625  -0.0136 -0.0044 300 HIS   A CG  
2098 N ND1 . HIS   A 278 ? 0.2576 0.3606 0.1805 0.0816  -0.0260 -0.0081 300 HIS   A ND1 
2099 C CD2 . HIS   A 278 ? 0.2688 0.3497 0.1891 0.0629  -0.0309 0.0084  300 HIS   A CD2 
2100 C CE1 . HIS   A 278 ? 0.2797 0.3591 0.1897 0.0654  -0.0261 0.0074  300 HIS   A CE1 
2101 N NE2 . HIS   A 278 ? 0.2686 0.3484 0.2003 0.0669  -0.0387 0.0164  300 HIS   A NE2 
2102 N N   . THR   A 279 ? 0.2366 0.4115 0.2336 0.0661  0.0052  0.0066  301 THR   A N   
2103 C CA  . THR   A 279 ? 0.2437 0.4067 0.2292 0.0591  -0.0009 0.0312  301 THR   A CA  
2104 C C   . THR   A 279 ? 0.2475 0.4036 0.2076 0.0492  0.0076  0.0425  301 THR   A C   
2105 O O   . THR   A 279 ? 0.2793 0.4123 0.2001 0.0301  0.0021  0.0546  301 THR   A O   
2106 C CB  . THR   A 279 ? 0.2388 0.4144 0.2783 0.0566  -0.0180 0.0216  301 THR   A CB  
2107 O OG1 . THR   A 279 ? 0.2307 0.4252 0.2811 0.0447  -0.0087 0.0039  301 THR   A OG1 
2108 C CG2 . THR   A 279 ? 0.2623 0.4100 0.2992 0.0538  -0.0110 0.0416  301 THR   A CG2 
2109 N N   . ASP   A 280 ? 0.2573 0.4132 0.1758 0.0632  0.0144  0.0297  302 ASP   A N   
2110 C CA  . ASP   A 280 ? 0.2432 0.3963 0.1718 0.0592  0.0160  0.0215  302 ASP   A CA  
2111 C C   . ASP   A 280 ? 0.2431 0.4023 0.1975 0.0550  0.0097  0.0290  302 ASP   A C   
2112 O O   . ASP   A 280 ? 0.2592 0.4126 0.1943 0.0739  0.0086  0.0255  302 ASP   A O   
2113 C CB  . ASP   A 280 ? 0.2537 0.4129 0.1974 0.0507  0.0254  0.0270  302 ASP   A CB  
2114 C CG  . ASP   A 280 ? 0.2328 0.3977 0.1902 0.0508  0.0118  0.0133  302 ASP   A CG  
2115 O OD1 . ASP   A 280 ? 0.2234 0.4048 0.1698 0.0421  0.0239  0.0116  302 ASP   A OD1 
2116 O OD2 . ASP   A 280 ? 0.2358 0.4029 0.2321 0.0478  0.0223  0.0134  302 ASP   A OD2 
2117 N N   . VAL   A 281 ? 0.2473 0.4094 0.1990 0.0455  0.0041  0.0238  303 VAL   A N   
2118 C CA  . VAL   A 281 ? 0.2372 0.3933 0.2038 0.0378  0.0148  0.0120  303 VAL   A CA  
2119 C C   . VAL   A 281 ? 0.2241 0.3774 0.1961 0.0406  -0.0125 0.0153  303 VAL   A C   
2120 O O   . VAL   A 281 ? 0.2249 0.4019 0.1726 0.0238  -0.0019 0.0275  303 VAL   A O   
2121 C CB  . VAL   A 281 ? 0.2491 0.3836 0.2221 0.0413  0.0126  0.0061  303 VAL   A CB  
2122 C CG1 . VAL   A 281 ? 0.2614 0.3824 0.2262 0.0485  0.0290  0.0120  303 VAL   A CG1 
2123 C CG2 . VAL   A 281 ? 0.2503 0.3986 0.2363 0.0384  0.0153  0.0039  303 VAL   A CG2 
2124 N N   . VAL   A 282 ? 0.2299 0.3501 0.2043 0.0480  -0.0141 0.0087  304 VAL   A N   
2125 C CA  . VAL   A 282 ? 0.2304 0.3210 0.1959 0.0431  -0.0186 -0.0093 304 VAL   A CA  
2126 C C   . VAL   A 282 ? 0.2324 0.3245 0.2080 0.0411  -0.0126 0.0045  304 VAL   A C   
2127 O O   . VAL   A 282 ? 0.2466 0.3315 0.2223 0.0352  -0.0205 0.0280  304 VAL   A O   
2128 C CB  . VAL   A 282 ? 0.2495 0.3112 0.1951 0.0553  -0.0164 -0.0173 304 VAL   A CB  
2129 C CG1 . VAL   A 282 ? 0.2738 0.3038 0.1995 0.0603  -0.0032 -0.0211 304 VAL   A CG1 
2130 C CG2 . VAL   A 282 ? 0.2605 0.2920 0.1832 0.0702  -0.0041 -0.0231 304 VAL   A CG2 
2131 N N   . ILE   A 283 ? 0.2112 0.3125 0.1870 0.0257  -0.0003 0.0122  305 ILE   A N   
2132 C CA  . ILE   A 283 ? 0.2127 0.3138 0.1962 0.0336  0.0107  0.0143  305 ILE   A CA  
2133 C C   . ILE   A 283 ? 0.2088 0.2968 0.1921 0.0316  0.0087  0.0242  305 ILE   A C   
2134 O O   . ILE   A 283 ? 0.2112 0.2946 0.2219 0.0403  -0.0016 0.0314  305 ILE   A O   
2135 C CB  . ILE   A 283 ? 0.2120 0.3218 0.1996 0.0267  0.0225  0.0276  305 ILE   A CB  
2136 C CG1 . ILE   A 283 ? 0.2323 0.3201 0.2134 0.0321  0.0140  0.0282  305 ILE   A CG1 
2137 C CG2 . ILE   A 283 ? 0.1993 0.3321 0.1812 0.0252  0.0181  0.0336  305 ILE   A CG2 
2138 C CD1 . ILE   A 283 ? 0.2524 0.3197 0.2302 0.0378  0.0041  0.0070  305 ILE   A CD1 
2139 N N   . SER   A 284 ? 0.2060 0.2876 0.1853 0.0444  0.0109  0.0226  306 SER   A N   
2140 C CA  . SER   A 284 ? 0.2280 0.2657 0.1688 0.0304  -0.0009 0.0248  306 SER   A CA  
2141 C C   . SER   A 284 ? 0.2215 0.2789 0.1649 0.0136  -0.0087 0.0397  306 SER   A C   
2142 O O   . SER   A 284 ? 0.2176 0.2800 0.1693 0.0170  0.0100  0.0810  306 SER   A O   
2143 C CB  . SER   A 284 ? 0.2405 0.2589 0.1773 0.0310  0.0137  0.0202  306 SER   A CB  
2144 O OG  . SER   A 284 ? 0.2599 0.2435 0.1491 0.0290  0.0082  0.0070  306 SER   A OG  
2145 N N   . THR   A 285 ? 0.2277 0.2690 0.1525 0.0044  -0.0169 0.0411  307 THR   A N   
2146 C CA  . THR   A 285 ? 0.2348 0.2619 0.1699 0.0121  -0.0072 0.0434  307 THR   A CA  
2147 C C   . THR   A 285 ? 0.2236 0.2536 0.1825 0.0031  -0.0022 0.0476  307 THR   A C   
2148 O O   . THR   A 285 ? 0.2261 0.2623 0.1882 0.0060  0.0142  0.0444  307 THR   A O   
2149 C CB  . THR   A 285 ? 0.2641 0.2787 0.1975 0.0120  0.0084  0.0354  307 THR   A CB  
2150 O OG1 . THR   A 285 ? 0.2788 0.2855 0.2075 0.0354  -0.0148 0.0409  307 THR   A OG1 
2151 C CG2 . THR   A 285 ? 0.2827 0.2812 0.2150 0.0279  0.0127  0.0180  307 THR   A CG2 
2152 N N   . ALA   A 286 ? 0.2211 0.2329 0.1783 0.0017  -0.0012 0.0554  308 ALA   A N   
2153 C CA  . ALA   A 286 ? 0.2217 0.2386 0.1967 0.0000  -0.0016 0.0558  308 ALA   A CA  
2154 C C   . ALA   A 286 ? 0.2242 0.2247 0.2040 0.0015  -0.0209 0.0483  308 ALA   A C   
2155 O O   . ALA   A 286 ? 0.2132 0.2146 0.2422 -0.0197 -0.0222 0.0488  308 ALA   A O   
2156 C CB  . ALA   A 286 ? 0.2233 0.2350 0.1866 0.0050  0.0015  0.0561  308 ALA   A CB  
2157 N N   . CYS   A 287 ? 0.2065 0.2446 0.2097 -0.0105 -0.0321 0.0478  309 CYS   A N   
2158 C CA  . CYS   A 287 ? 0.2437 0.2463 0.2034 -0.0131 -0.0256 0.0361  309 CYS   A CA  
2159 C C   . CYS   A 287 ? 0.2342 0.2460 0.1945 -0.0154 -0.0177 0.0466  309 CYS   A C   
2160 O O   . CYS   A 287 ? 0.2433 0.2641 0.1928 -0.0055 -0.0183 0.0522  309 CYS   A O   
2161 C CB  . CYS   A 287 ? 0.2595 0.2576 0.2095 -0.0128 -0.0218 0.0228  309 CYS   A CB  
2162 S SG  . CYS   A 287 ? 0.3071 0.2642 0.2164 -0.0152 -0.0420 0.0133  309 CYS   A SG  
2163 N N   . HIS   A 288 ? 0.2371 0.2344 0.1970 -0.0089 -0.0197 0.0364  310 HIS   A N   
2164 C CA  . HIS   A 288 ? 0.2290 0.2435 0.1907 -0.0129 -0.0121 0.0357  310 HIS   A CA  
2165 C C   . HIS   A 288 ? 0.2156 0.2509 0.2203 -0.0264 -0.0179 0.0373  310 HIS   A C   
2166 O O   . HIS   A 288 ? 0.2504 0.2696 0.2316 -0.0407 -0.0267 0.0371  310 HIS   A O   
2167 C CB  . HIS   A 288 ? 0.2119 0.2474 0.1878 -0.0110 -0.0068 0.0157  310 HIS   A CB  
2168 C CG  . HIS   A 288 ? 0.2149 0.2642 0.1709 -0.0111 -0.0035 0.0280  310 HIS   A CG  
2169 N ND1 . HIS   A 288 ? 0.2040 0.2674 0.1720 -0.0177 0.0020  0.0324  310 HIS   A ND1 
2170 C CD2 . HIS   A 288 ? 0.2077 0.2502 0.1669 -0.0166 0.0061  0.0331  310 HIS   A CD2 
2171 C CE1 . HIS   A 288 ? 0.2126 0.2652 0.1518 -0.0203 -0.0053 0.0421  310 HIS   A CE1 
2172 N NE2 . HIS   A 288 ? 0.2048 0.2724 0.1497 -0.0146 -0.0045 0.0461  310 HIS   A NE2 
2173 N N   . PRO   A 289 ? 0.2182 0.2498 0.2250 -0.0507 -0.0018 0.0463  311 PRO   A N   
2174 C CA  . PRO   A 289 ? 0.2134 0.2546 0.2303 -0.0493 0.0014  0.0487  311 PRO   A CA  
2175 C C   . PRO   A 289 ? 0.2287 0.2641 0.2350 -0.0433 0.0029  0.0606  311 PRO   A C   
2176 O O   . PRO   A 289 ? 0.2090 0.3219 0.2944 -0.0419 0.0086  0.0555  311 PRO   A O   
2177 C CB  . PRO   A 289 ? 0.2191 0.2426 0.2323 -0.0584 -0.0063 0.0582  311 PRO   A CB  
2178 C CG  . PRO   A 289 ? 0.2080 0.2469 0.2272 -0.0576 0.0028  0.0520  311 PRO   A CG  
2179 C CD  . PRO   A 289 ? 0.2112 0.2442 0.2216 -0.0543 -0.0057 0.0434  311 PRO   A CD  
2180 N N   . THR   A 290 ? 0.2441 0.2560 0.2152 -0.0322 0.0003  0.0599  312 THR   A N   
2181 C CA  . THR   A 290 ? 0.2664 0.2473 0.2147 -0.0290 0.0025  0.0504  312 THR   A CA  
2182 C C   . THR   A 290 ? 0.2867 0.2321 0.2064 -0.0245 -0.0125 0.0657  312 THR   A C   
2183 O O   . THR   A 290 ? 0.3139 0.2255 0.2310 -0.0387 -0.0006 0.0678  312 THR   A O   
2184 C CB  . THR   A 290 ? 0.2515 0.2596 0.2096 -0.0204 0.0069  0.0466  312 THR   A CB  
2185 O OG1 . THR   A 290 ? 0.2376 0.2759 0.1863 -0.0322 0.0141  0.0257  312 THR   A OG1 
2186 C CG2 . THR   A 290 ? 0.2535 0.2629 0.2341 -0.0157 0.0105  0.0438  312 THR   A CG2 
2187 N N   . GLU   A 291 ? 0.3021 0.2378 0.2480 -0.0355 -0.0123 0.0496  313 GLU   A N   
2188 C CA  . GLU   A 291 ? 0.3143 0.2644 0.2346 -0.0255 -0.0214 0.0489  313 GLU   A CA  
2189 C C   . GLU   A 291 ? 0.3148 0.2714 0.2212 -0.0121 -0.0169 0.0505  313 GLU   A C   
2190 O O   . GLU   A 291 ? 0.2693 0.2728 0.2052 -0.0094 -0.0096 0.0521  313 GLU   A O   
2191 C CB  . GLU   A 291 ? 0.3357 0.2853 0.2551 -0.0373 -0.0313 0.0415  313 GLU   A CB  
2192 C CG  . GLU   A 291 ? 0.3591 0.3006 0.2641 -0.0287 -0.0539 0.0523  313 GLU   A CG  
2193 C CD  . GLU   A 291 ? 0.3931 0.3029 0.3120 -0.0150 -0.0562 0.0471  313 GLU   A CD  
2194 O OE1 . GLU   A 291 ? 0.4722 0.2819 0.3638 0.0219  -0.0901 0.0242  313 GLU   A OE1 
2195 O OE2 . GLU   A 291 ? 0.3802 0.3258 0.2739 0.0006  -0.0405 0.0494  313 GLU   A OE2 
2196 N N   . ASN   A 292 ? 0.3286 0.2745 0.2141 0.0020  -0.0190 0.0452  314 ASN   A N   
2197 C CA  . ASN   A 292 ? 0.3289 0.2722 0.2211 -0.0046 -0.0306 0.0460  314 ASN   A CA  
2198 C C   . ASN   A 292 ? 0.2976 0.2835 0.2170 0.0083  -0.0312 0.0397  314 ASN   A C   
2199 O O   . ASN   A 292 ? 0.3092 0.2937 0.2019 0.0244  -0.0333 0.0262  314 ASN   A O   
2200 C CB  . ASN   A 292 ? 0.3447 0.2794 0.2439 -0.0022 -0.0383 0.0406  314 ASN   A CB  
2201 C CG  . ASN   A 292 ? 0.3350 0.2761 0.2617 -0.0156 -0.0461 0.0436  314 ASN   A CG  
2202 O OD1 . ASN   A 292 ? 0.3435 0.3069 0.2884 -0.0122 -0.0153 0.0381  314 ASN   A OD1 
2203 N ND2 . ASN   A 292 ? 0.3212 0.2805 0.2853 -0.0232 -0.0605 0.0478  314 ASN   A ND2 
2204 N N   . ILE   A 293 ? 0.2468 0.2780 0.2014 0.0061  -0.0378 0.0586  315 ILE   A N   
2205 C CA  . ILE   A 293 ? 0.2428 0.2946 0.2167 0.0131  -0.0159 0.0457  315 ILE   A CA  
2206 C C   . ILE   A 293 ? 0.2395 0.2831 0.2055 0.0218  -0.0142 0.0362  315 ILE   A C   
2207 O O   . ILE   A 293 ? 0.2378 0.2784 0.2042 0.0359  -0.0275 0.0376  315 ILE   A O   
2208 C CB  . ILE   A 293 ? 0.2310 0.2844 0.2264 0.0017  -0.0126 0.0515  315 ILE   A CB  
2209 C CG1 . ILE   A 293 ? 0.2355 0.2762 0.2350 -0.0021 -0.0138 0.0549  315 ILE   A CG1 
2210 C CG2 . ILE   A 293 ? 0.2495 0.2720 0.2426 0.0132  -0.0245 0.0669  315 ILE   A CG2 
2211 C CD1 . ILE   A 293 ? 0.2372 0.2689 0.2269 -0.0182 -0.0118 0.0532  315 ILE   A CD1 
2212 N N   . ILE   A 294 ? 0.2439 0.2635 0.2167 0.0125  -0.0135 0.0310  316 ILE   A N   
2213 C CA  . ILE   A 294 ? 0.2339 0.2428 0.1975 0.0203  -0.0144 0.0237  316 ILE   A CA  
2214 C C   . ILE   A 294 ? 0.2376 0.2589 0.1944 0.0221  -0.0142 0.0195  316 ILE   A C   
2215 O O   . ILE   A 294 ? 0.2544 0.2735 0.2117 0.0441  0.0051  0.0324  316 ILE   A O   
2216 C CB  . ILE   A 294 ? 0.2469 0.2210 0.2255 0.0205  -0.0218 0.0131  316 ILE   A CB  
2217 C CG1 . ILE   A 294 ? 0.2611 0.2287 0.2419 0.0134  -0.0243 0.0161  316 ILE   A CG1 
2218 C CG2 . ILE   A 294 ? 0.2485 0.2298 0.2091 0.0102  -0.0062 -0.0010 316 ILE   A CG2 
2219 C CD1 . ILE   A 294 ? 0.2848 0.2369 0.2496 0.0255  -0.0349 0.0141  316 ILE   A CD1 
2220 N N   . ALA   A 295 ? 0.2319 0.2621 0.1990 0.0226  -0.0055 0.0299  317 ALA   A N   
2221 C CA  . ALA   A 295 ? 0.2291 0.2875 0.1821 0.0204  -0.0091 0.0232  317 ALA   A CA  
2222 C C   . ALA   A 295 ? 0.2250 0.2946 0.1728 0.0201  -0.0150 0.0143  317 ALA   A C   
2223 O O   . ALA   A 295 ? 0.2289 0.3043 0.1508 0.0199  -0.0235 0.0318  317 ALA   A O   
2224 C CB  . ALA   A 295 ? 0.2288 0.2820 0.1728 0.0106  -0.0193 0.0161  317 ALA   A CB  
2225 N N   . SER   A 296 ? 0.2178 0.3114 0.1643 0.0277  -0.0179 0.0059  318 SER   A N   
2226 C CA  . SER   A 296 ? 0.2187 0.2969 0.1696 0.0377  -0.0196 0.0221  318 SER   A CA  
2227 C C   . SER   A 296 ? 0.1974 0.3168 0.1740 0.0234  -0.0162 0.0186  318 SER   A C   
2228 O O   . SER   A 296 ? 0.1836 0.3376 0.1904 0.0190  -0.0312 0.0415  318 SER   A O   
2229 C CB  . SER   A 296 ? 0.2148 0.3243 0.1661 0.0407  -0.0165 0.0037  318 SER   A CB  
2230 O OG  . SER   A 296 ? 0.2136 0.3090 0.1849 0.0638  -0.0216 -0.0108 318 SER   A OG  
2231 N N   . ALA   A 297 ? 0.2030 0.2950 0.1753 0.0189  -0.0074 0.0311  319 ALA   A N   
2232 C CA  . ALA   A 297 ? 0.2115 0.3028 0.1777 0.0257  0.0028  0.0318  319 ALA   A CA  
2233 C C   . ALA   A 297 ? 0.2168 0.3178 0.1826 0.0308  -0.0008 0.0269  319 ALA   A C   
2234 O O   . ALA   A 297 ? 0.2016 0.2886 0.2301 0.0356  0.0106  0.0000  319 ALA   A O   
2235 C CB  . ALA   A 297 ? 0.2296 0.2932 0.1977 0.0229  0.0031  0.0384  319 ALA   A CB  
2236 N N   . ALA   A 298 ? 0.2154 0.3504 0.1838 0.0225  0.0049  0.0300  320 ALA   A N   
2237 C CA  . ALA   A 298 ? 0.2298 0.3753 0.1772 0.0220  0.0008  0.0282  320 ALA   A CA  
2238 C C   . ALA   A 298 ? 0.2265 0.3801 0.1881 0.0102  0.0180  0.0307  320 ALA   A C   
2239 O O   . ALA   A 298 ? 0.2005 0.3669 0.1802 -0.0059 0.0248  0.0428  320 ALA   A O   
2240 C CB  . ALA   A 298 ? 0.2432 0.3914 0.1900 0.0222  0.0145  0.0258  320 ALA   A CB  
2241 N N   . LEU   A 299 ? 0.2428 0.3834 0.1852 0.0137  0.0183  0.0443  321 LEU   A N   
2242 C CA  . LEU   A 299 ? 0.2198 0.4232 0.1792 -0.0020 0.0174  0.0621  321 LEU   A CA  
2243 C C   . LEU   A 299 ? 0.2147 0.4551 0.1866 -0.0030 0.0160  0.0600  321 LEU   A C   
2244 O O   . LEU   A 299 ? 0.1884 0.4586 0.1932 -0.0080 0.0181  0.0560  321 LEU   A O   
2245 C CB  . LEU   A 299 ? 0.2227 0.4222 0.1941 0.0038  0.0092  0.0496  321 LEU   A CB  
2246 C CG  . LEU   A 299 ? 0.2124 0.4356 0.1859 0.0294  0.0138  0.0401  321 LEU   A CG  
2247 C CD1 . LEU   A 299 ? 0.2032 0.4362 0.2065 0.0355  0.0097  0.0292  321 LEU   A CD1 
2248 C CD2 . LEU   A 299 ? 0.2110 0.4368 0.1670 0.0120  0.0112  0.0318  321 LEU   A CD2 
2249 N N   . GLU   A 300 ? 0.2146 0.4839 0.2191 -0.0216 0.0021  0.0816  322 GLU   A N   
2250 C CA  . GLU   A 300 ? 0.2068 0.5268 0.2359 -0.0243 0.0097  0.1016  322 GLU   A CA  
2251 C C   . GLU   A 300 ? 0.2186 0.5192 0.2424 -0.0119 0.0173  0.0973  322 GLU   A C   
2252 O O   . GLU   A 300 ? 0.2105 0.5287 0.3025 -0.0082 0.0152  0.0806  322 GLU   A O   
2253 C CB  . GLU   A 300 ? 0.2365 0.5658 0.3124 -0.0144 -0.0105 0.1257  322 GLU   A CB  
2254 C CG  . GLU   A 300 ? 0.3260 0.6231 0.3226 -0.0335 -0.0137 0.1250  322 GLU   A CG  
2255 C CD  . GLU   A 300 ? 0.3430 0.6973 0.3542 -0.0271 -0.0092 0.1628  322 GLU   A CD  
2256 O OE1 . GLU   A 300 ? 0.3774 0.6346 0.3166 -0.0755 -0.0118 0.1792  322 GLU   A OE1 
2257 O OE2 . GLU   A 300 ? 0.4536 0.7126 0.3402 -0.0572 -0.0413 0.1592  322 GLU   A OE2 
2258 N N   . ASN   A 301 ? 0.2338 0.5416 0.2449 -0.0084 0.0249  0.0778  323 ASN   A N   
2259 C CA  . ASN   A 301 ? 0.2910 0.5685 0.2641 0.0297  0.0255  0.0618  323 ASN   A CA  
2260 C C   . ASN   A 301 ? 0.2650 0.5429 0.2476 0.0391  0.0506  0.0702  323 ASN   A C   
2261 O O   . ASN   A 301 ? 0.3049 0.6215 0.3059 0.1080  0.0669  0.0664  323 ASN   A O   
2262 C CB  . ASN   A 301 ? 0.3286 0.6121 0.3433 0.0194  0.0368  0.0291  323 ASN   A CB  
2263 C CG  . ASN   A 301 ? 0.3492 0.6395 0.4223 0.0144  0.0584  0.0406  323 ASN   A CG  
2264 O OD1 . ASN   A 301 ? 0.3763 0.6708 0.4396 -0.0025 0.0687  0.0596  323 ASN   A OD1 
2265 N ND2 . ASN   A 301 ? 0.3719 0.6633 0.4502 0.0005  0.0879  0.0188  323 ASN   A ND2 
2266 N N   . ASP   A 302 ? 0.2418 0.4481 0.2023 0.0166  0.0378  0.0855  324 ASP   A N   
2267 C CA  . ASP   A 302 ? 0.2232 0.4073 0.2014 0.0092  0.0190  0.0652  324 ASP   A CA  
2268 C C   . ASP   A 302 ? 0.2045 0.3932 0.2019 0.0036  0.0139  0.0641  324 ASP   A C   
2269 O O   . ASP   A 302 ? 0.1616 0.4096 0.2200 0.0038  0.0413  0.0377  324 ASP   A O   
2270 C CB  . ASP   A 302 ? 0.2684 0.3829 0.2082 0.0011  0.0136  0.0616  324 ASP   A CB  
2271 C CG  . ASP   A 302 ? 0.2594 0.3524 0.2107 0.0027  0.0172  0.0546  324 ASP   A CG  
2272 O OD1 . ASP   A 302 ? 0.2634 0.3361 0.2625 -0.0236 -0.0401 0.0370  324 ASP   A OD1 
2273 O OD2 . ASP   A 302 ? 0.2442 0.3695 0.2562 -0.0263 0.0287  0.0005  324 ASP   A OD2 
2274 N N   . LYS   A 303 ? 0.2116 0.3928 0.2073 0.0055  0.0373  0.0669  325 LYS   A N   
2275 C CA  . LYS   A 303 ? 0.2224 0.3906 0.2143 0.0153  0.0292  0.0735  325 LYS   A CA  
2276 C C   . LYS   A 303 ? 0.1964 0.3784 0.2042 0.0194  0.0132  0.0585  325 LYS   A C   
2277 O O   . LYS   A 303 ? 0.1742 0.3679 0.2050 0.0253  -0.0073 0.0688  325 LYS   A O   
2278 C CB  . LYS   A 303 ? 0.2766 0.4024 0.2595 0.0326  0.0514  0.0771  325 LYS   A CB  
2279 C CG  . LYS   A 303 ? 0.3232 0.4356 0.2905 0.0331  0.0682  0.0932  325 LYS   A CG  
2280 C CD  . LYS   A 303 ? 0.3799 0.4708 0.3375 0.0155  0.0949  0.1050  325 LYS   A CD  
2281 C CE  . LYS   A 303 ? 0.4505 0.5717 0.4097 -0.0247 0.1276  0.0926  325 LYS   A CE  
2282 N NZ  . LYS   A 303 ? 0.4963 0.6211 0.3997 -0.0582 0.1738  0.1032  325 LYS   A NZ  
2283 N N   . THR   A 304 ? 0.1963 0.3783 0.1762 -0.0006 0.0102  0.0649  326 THR   A N   
2284 C CA  . THR   A 304 ? 0.2206 0.3809 0.1983 0.0135  0.0084  0.0617  326 THR   A CA  
2285 C C   . THR   A 304 ? 0.2147 0.3640 0.1915 0.0122  0.0082  0.0571  326 THR   A C   
2286 O O   . THR   A 304 ? 0.2357 0.3654 0.1673 -0.0059 0.0196  0.0487  326 THR   A O   
2287 C CB  . THR   A 304 ? 0.2348 0.3846 0.2146 0.0241  0.0038  0.0533  326 THR   A CB  
2288 O OG1 . THR   A 304 ? 0.2687 0.3872 0.2213 0.0576  0.0132  0.0227  326 THR   A OG1 
2289 C CG2 . THR   A 304 ? 0.2261 0.3906 0.2120 0.0163  -0.0023 0.0475  326 THR   A CG2 
2290 N N   . ILE   A 305 ? 0.2080 0.3537 0.1836 0.0192  0.0022  0.0491  327 ILE   A N   
2291 C CA  . ILE   A 305 ? 0.2090 0.3422 0.2064 0.0176  0.0015  0.0434  327 ILE   A CA  
2292 C C   . ILE   A 305 ? 0.2024 0.3479 0.2036 0.0337  0.0009  0.0358  327 ILE   A C   
2293 O O   . ILE   A 305 ? 0.1912 0.3487 0.2256 0.0155  0.0042  0.0165  327 ILE   A O   
2294 C CB  . ILE   A 305 ? 0.2183 0.3368 0.2119 0.0099  0.0037  0.0342  327 ILE   A CB  
2295 C CG1 . ILE   A 305 ? 0.2455 0.3343 0.2221 0.0010  0.0151  0.0415  327 ILE   A CG1 
2296 C CG2 . ILE   A 305 ? 0.2225 0.3332 0.1888 0.0146  0.0110  0.0342  327 ILE   A CG2 
2297 C CD1 . ILE   A 305 ? 0.2566 0.3489 0.2278 -0.0032 0.0284  0.0309  327 ILE   A CD1 
2298 N N   . LYS   A 306 ? 0.1717 0.3496 0.1929 0.0331  0.0154  0.0455  328 LYS   A N   
2299 C CA  . LYS   A 306 ? 0.2059 0.3569 0.2045 0.0400  0.0206  0.0427  328 LYS   A CA  
2300 C C   . LYS   A 306 ? 0.2009 0.3328 0.2090 0.0339  0.0185  0.0439  328 LYS   A C   
2301 O O   . LYS   A 306 ? 0.2005 0.3267 0.1999 0.0530  0.0221  0.0470  328 LYS   A O   
2302 C CB  . LYS   A 306 ? 0.2263 0.3755 0.2249 0.0563  0.0157  0.0429  328 LYS   A CB  
2303 C CG  . LYS   A 306 ? 0.2375 0.3937 0.2222 0.0679  0.0195  0.0407  328 LYS   A CG  
2304 C CD  . LYS   A 306 ? 0.2593 0.3962 0.2177 0.0716  0.0047  0.0374  328 LYS   A CD  
2305 C CE  . LYS   A 306 ? 0.2682 0.4063 0.2336 0.0706  0.0061  0.0277  328 LYS   A CE  
2306 N NZ  . LYS   A 306 ? 0.2458 0.3936 0.2426 0.0724  0.0252  0.0210  328 LYS   A NZ  
2307 N N   . LEU   A 307 ? 0.1968 0.3180 0.2019 0.0438  0.0048  0.0239  329 LEU   A N   
2308 C CA  . LEU   A 307 ? 0.2040 0.3070 0.2155 0.0257  -0.0021 0.0239  329 LEU   A CA  
2309 C C   . LEU   A 307 ? 0.2235 0.3047 0.2274 0.0308  -0.0059 0.0206  329 LEU   A C   
2310 O O   . LEU   A 307 ? 0.2255 0.3010 0.2175 0.0216  -0.0176 0.0277  329 LEU   A O   
2311 C CB  . LEU   A 307 ? 0.2067 0.3244 0.2346 0.0168  -0.0161 0.0210  329 LEU   A CB  
2312 C CG  . LEU   A 307 ? 0.2252 0.3235 0.2368 0.0230  -0.0159 0.0164  329 LEU   A CG  
2313 C CD1 . LEU   A 307 ? 0.2259 0.3433 0.2390 0.0172  -0.0336 0.0320  329 LEU   A CD1 
2314 C CD2 . LEU   A 307 ? 0.2341 0.3327 0.2695 0.0315  -0.0395 0.0110  329 LEU   A CD2 
2315 N N   . TRP   A 308 ? 0.2337 0.2939 0.2419 0.0338  -0.0054 0.0198  330 TRP   A N   
2316 C CA  . TRP   A 308 ? 0.2639 0.3018 0.2165 0.0382  -0.0017 0.0199  330 TRP   A CA  
2317 C C   . TRP   A 308 ? 0.2724 0.2987 0.2359 0.0337  0.0039  0.0354  330 TRP   A C   
2318 O O   . TRP   A 308 ? 0.2820 0.2711 0.2479 0.0632  0.0116  0.0309  330 TRP   A O   
2319 C CB  . TRP   A 308 ? 0.2716 0.3020 0.2204 0.0447  -0.0184 0.0243  330 TRP   A CB  
2320 C CG  . TRP   A 308 ? 0.2917 0.3016 0.2055 0.0372  -0.0122 0.0113  330 TRP   A CG  
2321 C CD1 . TRP   A 308 ? 0.3055 0.2991 0.1863 0.0358  -0.0143 0.0147  330 TRP   A CD1 
2322 C CD2 . TRP   A 308 ? 0.3048 0.2945 0.2157 0.0387  -0.0005 0.0058  330 TRP   A CD2 
2323 N NE1 . TRP   A 308 ? 0.3074 0.3052 0.1956 0.0307  -0.0082 0.0144  330 TRP   A NE1 
2324 C CE2 . TRP   A 308 ? 0.3046 0.3155 0.2078 0.0318  -0.0019 0.0078  330 TRP   A CE2 
2325 C CE3 . TRP   A 308 ? 0.2988 0.2985 0.2142 0.0318  0.0056  0.0007  330 TRP   A CE3 
2326 C CZ2 . TRP   A 308 ? 0.3071 0.3233 0.1972 0.0315  0.0016  0.0041  330 TRP   A CZ2 
2327 C CZ3 . TRP   A 308 ? 0.3051 0.2992 0.2034 0.0321  0.0018  -0.0006 330 TRP   A CZ3 
2328 C CH2 . TRP   A 308 ? 0.3197 0.3124 0.2147 0.0296  0.0041  0.0000  330 TRP   A CH2 
2329 N N   . LYS   A 309 ? 0.2773 0.3058 0.2460 0.0438  0.0018  0.0316  331 LYS   A N   
2330 C CA  . LYS   A 309 ? 0.3212 0.3167 0.2356 0.0341  -0.0048 0.0335  331 LYS   A CA  
2331 C C   . LYS   A 309 ? 0.3212 0.3103 0.2207 0.0282  -0.0263 0.0087  331 LYS   A C   
2332 O O   . LYS   A 309 ? 0.2999 0.3118 0.2335 0.0271  -0.0268 -0.0043 331 LYS   A O   
2333 C CB  . LYS   A 309 ? 0.3729 0.3393 0.2447 0.0180  0.0012  0.0240  331 LYS   A CB  
2334 C CG  . LYS   A 309 ? 0.4395 0.3759 0.2736 0.0085  0.0205  0.0429  331 LYS   A CG  
2335 C CD  . LYS   A 309 ? 0.5100 0.4116 0.3353 -0.0057 0.0236  0.0230  331 LYS   A CD  
2336 C CE  . LYS   A 309 ? 0.5667 0.4373 0.4006 -0.0032 0.0836  0.0238  331 LYS   A CE  
2337 N NZ  . LYS   A 309 ? 0.6267 0.4744 0.4524 0.0001  0.0812  0.0454  331 LYS   A NZ  
2338 N N   . SER   A 310 ? 0.3424 0.3003 0.2317 0.0344  -0.0141 -0.0001 332 SER   A N   
2339 C CA  . SER   A 310 ? 0.3981 0.2906 0.2533 0.0319  -0.0150 0.0039  332 SER   A CA  
2340 C C   . SER   A 310 ? 0.4454 0.3031 0.2497 0.0205  -0.0181 0.0059  332 SER   A C   
2341 O O   . SER   A 310 ? 0.4388 0.3073 0.2429 0.0329  0.0006  0.0220  332 SER   A O   
2342 C CB  . SER   A 310 ? 0.3915 0.2792 0.2674 0.0316  -0.0125 0.0012  332 SER   A CB  
2343 O OG  . SER   A 310 ? 0.4073 0.2823 0.2991 0.0062  -0.0140 0.0127  332 SER   A OG  
2344 N N   . ASP   A 311 ? 0.4972 0.3006 0.2705 0.0368  -0.0295 0.0095  333 ASP   A N   
2345 C CA  . ASP   A 311 ? 0.5422 0.3393 0.3091 0.0337  -0.0281 0.0214  333 ASP   A CA  
2346 C C   . ASP   A 311 ? 0.5695 0.3755 0.3662 0.0045  -0.0116 0.0118  333 ASP   A C   
2347 O O   . ASP   A 311 ? 0.6045 0.3958 0.3770 -0.0355 0.0029  0.0039  333 ASP   A O   
2348 C CB  . ASP   A 311 ? 0.5574 0.3668 0.3307 0.0691  -0.0451 0.0409  333 ASP   A CB  
2349 C CG  . ASP   A 311 ? 0.5675 0.4042 0.3762 0.0679  -0.0472 0.0342  333 ASP   A CG  
2350 O OD1 . ASP   A 311 ? 0.6084 0.4202 0.4242 0.0963  -0.0948 0.0379  333 ASP   A OD1 
2351 O OD2 . ASP   A 311 ? 0.5329 0.4505 0.4493 0.1120  -0.0584 0.0572  333 ASP   A OD2 
2352 N N   . CYS   A 312 ? 0.5545 0.3512 0.3687 -0.0285 -0.0334 -0.0074 334 CYS   A N   
2353 C CA  . CYS   A 312 ? 0.5905 0.3755 0.4311 -0.0345 -0.0171 -0.0166 334 CYS   A CA  
2354 C C   . CYS   A 312 ? 0.5348 0.3681 0.4415 -0.0463 -0.0380 -0.0331 334 CYS   A C   
2355 O O   . CYS   A 312 ? 0.4971 0.2508 0.4078 -0.0141 -0.0475 -0.0327 334 CYS   A O   
2356 C CB  . CYS   A 312 ? 0.6437 0.4137 0.4543 -0.0582 -0.0166 -0.0474 334 CYS   A CB  
2357 S SG  . CYS   A 312 ? 0.7240 0.3635 0.4345 -0.0271 -0.0009 -0.0334 334 CYS   A SG  
2358 O OXT . CYS   A 312 ? 0.5287 0.3454 0.4793 -0.0657 -0.0213 -0.0707 334 CYS   A OXT 
2359 N N   . VAL   B 9   ? 0.8320 0.5597 0.8944 -0.0174 -0.0139 0.0694  31  VAL   B N   
2360 C CA  . VAL   B 9   ? 0.8178 0.5190 0.8418 -0.0526 -0.0449 0.0522  31  VAL   B CA  
2361 C C   . VAL   B 9   ? 0.7676 0.4907 0.7783 -0.0982 -0.0442 0.0195  31  VAL   B C   
2362 O O   . VAL   B 9   ? 0.8075 0.4920 0.8146 -0.0663 -0.0233 0.0141  31  VAL   B O   
2363 C CB  . VAL   B 9   ? 0.8047 0.5317 0.7926 -0.0450 -0.0618 0.0359  31  VAL   B CB  
2364 N N   . LYS   B 10  ? 0.7273 0.3911 0.6445 -0.1692 -0.0732 -0.0262 32  LYS   B N   
2365 C CA  . LYS   B 10  ? 0.6946 0.3197 0.5840 -0.2111 -0.0428 -0.0390 32  LYS   B CA  
2366 C C   . LYS   B 10  ? 0.6630 0.3159 0.5134 -0.2145 -0.0224 0.0117  32  LYS   B C   
2367 O O   . LYS   B 10  ? 0.6188 0.4274 0.4987 -0.2269 -0.0461 0.0215  32  LYS   B O   
2368 C CB  . LYS   B 10  ? 0.7278 0.4091 0.5681 -0.1640 -0.0490 -0.0656 32  LYS   B CB  
2369 C CG  . LYS   B 10  ? 0.7300 0.3980 0.5757 -0.1577 -0.0333 -0.0773 32  LYS   B CG  
2370 N N   . PRO   B 11  ? 0.6554 0.3160 0.4289 -0.2055 -0.0122 0.0437  33  PRO   B N   
2371 C CA  . PRO   B 11  ? 0.6610 0.3022 0.3739 -0.2139 -0.0117 0.0506  33  PRO   B CA  
2372 C C   . PRO   B 11  ? 0.6509 0.3413 0.3581 -0.2151 -0.0178 0.0778  33  PRO   B C   
2373 O O   . PRO   B 11  ? 0.6814 0.3645 0.3986 -0.2448 -0.0638 0.0602  33  PRO   B O   
2374 C CB  . PRO   B 11  ? 0.6429 0.3135 0.4347 -0.2121 0.0005  0.0436  33  PRO   B CB  
2375 C CG  . PRO   B 11  ? 0.6529 0.2881 0.4078 -0.2191 0.0033  0.0474  33  PRO   B CG  
2376 C CD  . PRO   B 11  ? 0.6453 0.3103 0.4377 -0.2197 -0.0075 0.0311  33  PRO   B CD  
2377 N N   . ASN   B 12  ? 0.6208 0.4219 0.3908 -0.2255 -0.0247 0.0964  34  ASN   B N   
2378 C CA  . ASN   B 12  ? 0.6123 0.4678 0.3986 -0.2279 -0.0437 0.1095  34  ASN   B CA  
2379 C C   . ASN   B 12  ? 0.5483 0.4568 0.3749 -0.2254 -0.0347 0.1255  34  ASN   B C   
2380 O O   . ASN   B 12  ? 0.5264 0.4765 0.3928 -0.2621 0.0193  0.1388  34  ASN   B O   
2381 C CB  . ASN   B 12  ? 0.6390 0.4977 0.4545 -0.2531 -0.0302 0.1312  34  ASN   B CB  
2382 C CG  . ASN   B 12  ? 0.6441 0.5233 0.4614 -0.2962 -0.0481 0.1399  34  ASN   B CG  
2383 O OD1 . ASN   B 12  ? 0.7082 0.4737 0.4321 -0.2873 -0.1044 0.1526  34  ASN   B OD1 
2384 N ND2 . ASN   B 12  ? 0.6360 0.5755 0.5345 -0.3375 -0.0361 0.1313  34  ASN   B ND2 
2385 N N   . TYR   B 13  ? 0.5017 0.4538 0.3434 -0.2001 -0.0533 0.1340  35  TYR   B N   
2386 C CA  . TYR   B 13  ? 0.4682 0.4619 0.3543 -0.1919 -0.0601 0.1056  35  TYR   B CA  
2387 C C   . TYR   B 13  ? 0.4402 0.4675 0.3463 -0.1969 -0.0493 0.0860  35  TYR   B C   
2388 O O   . TYR   B 13  ? 0.4301 0.4559 0.3392 -0.1983 -0.0597 0.0830  35  TYR   B O   
2389 C CB  . TYR   B 13  ? 0.4656 0.4418 0.2774 -0.1673 -0.0708 0.1229  35  TYR   B CB  
2390 C CG  . TYR   B 13  ? 0.4485 0.4177 0.2681 -0.1408 -0.0805 0.1387  35  TYR   B CG  
2391 C CD1 . TYR   B 13  ? 0.4327 0.4246 0.2628 -0.1422 -0.0801 0.1401  35  TYR   B CD1 
2392 C CD2 . TYR   B 13  ? 0.4430 0.4234 0.2832 -0.1417 -0.0883 0.1324  35  TYR   B CD2 
2393 C CE1 . TYR   B 13  ? 0.4245 0.3948 0.2454 -0.1371 -0.0864 0.1404  35  TYR   B CE1 
2394 C CE2 . TYR   B 13  ? 0.4469 0.4068 0.2756 -0.1411 -0.1012 0.1304  35  TYR   B CE2 
2395 C CZ  . TYR   B 13  ? 0.4448 0.4039 0.2559 -0.1287 -0.0915 0.1282  35  TYR   B CZ  
2396 O OH  . TYR   B 13  ? 0.4353 0.3934 0.2610 -0.1369 -0.0878 0.0957  35  TYR   B OH  
2397 N N   . ALA   B 14  ? 0.4070 0.5067 0.3682 -0.2067 -0.0125 0.1008  36  ALA   B N   
2398 C CA  . ALA   B 14  ? 0.4136 0.5242 0.4005 -0.2013 -0.0243 0.1049  36  ALA   B CA  
2399 C C   . ALA   B 14  ? 0.3665 0.5154 0.3645 -0.2199 -0.0428 0.1252  36  ALA   B C   
2400 O O   . ALA   B 14  ? 0.3400 0.5398 0.2962 -0.2069 -0.0454 0.1266  36  ALA   B O   
2401 C CB  . ALA   B 14  ? 0.4397 0.5327 0.4302 -0.1953 -0.0001 0.1207  36  ALA   B CB  
2402 N N   . LEU   B 15  ? 0.3348 0.5750 0.3612 -0.2081 -0.0394 0.1322  37  LEU   B N   
2403 C CA  . LEU   B 15  ? 0.2858 0.5850 0.3626 -0.1985 -0.0181 0.1400  37  LEU   B CA  
2404 C C   . LEU   B 15  ? 0.2592 0.6017 0.3659 -0.2087 0.0000  0.1447  37  LEU   B C   
2405 O O   . LEU   B 15  ? 0.2535 0.6114 0.4019 -0.2151 0.0126  0.1215  37  LEU   B O   
2406 C CB  . LEU   B 15  ? 0.2946 0.6271 0.3814 -0.1779 -0.0165 0.1666  37  LEU   B CB  
2407 C CG  . LEU   B 15  ? 0.2955 0.6117 0.3732 -0.1655 -0.0288 0.1780  37  LEU   B CG  
2408 C CD1 . LEU   B 15  ? 0.2771 0.6406 0.3529 -0.1638 -0.0420 0.1850  37  LEU   B CD1 
2409 C CD2 . LEU   B 15  ? 0.3313 0.6722 0.4026 -0.1508 -0.0429 0.1623  37  LEU   B CD2 
2410 N N   . LYS   B 16  ? 0.2693 0.6328 0.3977 -0.1937 0.0213  0.1312  38  LYS   B N   
2411 C CA  . LYS   B 16  ? 0.2883 0.6367 0.4250 -0.1908 0.0347  0.1459  38  LYS   B CA  
2412 C C   . LYS   B 16  ? 0.2836 0.6296 0.4284 -0.1740 0.0239  0.1663  38  LYS   B C   
2413 O O   . LYS   B 16  ? 0.2467 0.6135 0.5276 -0.1770 0.0103  0.1686  38  LYS   B O   
2414 C CB  . LYS   B 16  ? 0.3191 0.6695 0.4211 -0.1767 0.0273  0.1535  38  LYS   B CB  
2415 C CG  . LYS   B 16  ? 0.3764 0.7017 0.4952 -0.1811 0.0384  0.1308  38  LYS   B CG  
2416 C CD  . LYS   B 16  ? 0.4102 0.7453 0.5244 -0.2113 0.0405  0.1361  38  LYS   B CD  
2417 C CE  . LYS   B 16  ? 0.4605 0.7811 0.5750 -0.2178 0.0464  0.1406  38  LYS   B CE  
2418 N NZ  . LYS   B 16  ? 0.5012 0.7567 0.6148 -0.2085 0.0245  0.1564  38  LYS   B NZ  
2419 N N   . PHE   B 17  ? 0.2462 0.6274 0.3904 -0.1603 0.0161  0.1575  39  PHE   B N   
2420 C CA  . PHE   B 17  ? 0.2921 0.6313 0.3543 -0.1266 0.0164  0.1893  39  PHE   B CA  
2421 C C   . PHE   B 17  ? 0.2790 0.6197 0.3543 -0.1118 0.0092  0.1911  39  PHE   B C   
2422 O O   . PHE   B 17  ? 0.2664 0.6172 0.3802 -0.0977 0.0059  0.2015  39  PHE   B O   
2423 C CB  . PHE   B 17  ? 0.3067 0.6249 0.2971 -0.1325 0.0042  0.1973  39  PHE   B CB  
2424 C CG  . PHE   B 17  ? 0.3440 0.6317 0.3003 -0.1264 0.0036  0.2052  39  PHE   B CG  
2425 C CD1 . PHE   B 17  ? 0.3511 0.6411 0.3000 -0.1189 -0.0014 0.1884  39  PHE   B CD1 
2426 C CD2 . PHE   B 17  ? 0.3165 0.6710 0.3041 -0.1408 -0.0191 0.1689  39  PHE   B CD2 
2427 C CE1 . PHE   B 17  ? 0.3319 0.6591 0.3140 -0.1381 -0.0062 0.1965  39  PHE   B CE1 
2428 C CE2 . PHE   B 17  ? 0.3321 0.6665 0.3227 -0.1346 -0.0196 0.1894  39  PHE   B CE2 
2429 C CZ  . PHE   B 17  ? 0.3335 0.6591 0.3311 -0.1421 -0.0014 0.1863  39  PHE   B CZ  
2430 N N   . THR   B 18  ? 0.2633 0.6358 0.3671 -0.1176 -0.0095 0.1742  40  THR   B N   
2431 C CA  . THR   B 18  ? 0.2740 0.6147 0.3485 -0.1236 -0.0019 0.1580  40  THR   B CA  
2432 C C   . THR   B 18  ? 0.2655 0.6448 0.3480 -0.1020 0.0074  0.1451  40  THR   B C   
2433 O O   . THR   B 18  ? 0.2623 0.6596 0.3693 -0.1253 0.0300  0.1317  40  THR   B O   
2434 C CB  . THR   B 18  ? 0.2729 0.6100 0.3416 -0.1128 -0.0083 0.1509  40  THR   B CB  
2435 O OG1 . THR   B 18  ? 0.3007 0.6212 0.3152 -0.1339 -0.0202 0.1177  40  THR   B OG1 
2436 C CG2 . THR   B 18  ? 0.2646 0.5934 0.3504 -0.0853 -0.0036 0.1503  40  THR   B CG2 
2437 N N   . LEU   B 19  ? 0.2479 0.6334 0.3347 -0.0861 -0.0006 0.1600  41  LEU   B N   
2438 C CA  . LEU   B 19  ? 0.2501 0.6536 0.3017 -0.0486 0.0155  0.1426  41  LEU   B CA  
2439 C C   . LEU   B 19  ? 0.2045 0.6420 0.2939 -0.0490 0.0389  0.1454  41  LEU   B C   
2440 O O   . LEU   B 19  ? 0.2338 0.6934 0.3105 -0.0467 0.0665  0.1332  41  LEU   B O   
2441 C CB  . LEU   B 19  ? 0.2752 0.6534 0.2935 -0.0394 -0.0184 0.1551  41  LEU   B CB  
2442 C CG  . LEU   B 19  ? 0.3150 0.6690 0.3050 -0.0448 -0.0400 0.1641  41  LEU   B CG  
2443 C CD1 . LEU   B 19  ? 0.3334 0.6606 0.2476 -0.0570 -0.0496 0.1671  41  LEU   B CD1 
2444 C CD2 . LEU   B 19  ? 0.2828 0.6705 0.3101 -0.0424 -0.0434 0.1554  41  LEU   B CD2 
2445 N N   . ALA   B 20  ? 0.2175 0.6548 0.2845 -0.0441 0.0416  0.1366  42  ALA   B N   
2446 C CA  . ALA   B 20  ? 0.2010 0.6292 0.3101 -0.0305 0.0211  0.1202  42  ALA   B CA  
2447 C C   . ALA   B 20  ? 0.1987 0.6330 0.2862 -0.0171 0.0216  0.1049  42  ALA   B C   
2448 O O   . ALA   B 20  ? 0.1776 0.6451 0.2431 0.0103  0.0383  0.1068  42  ALA   B O   
2449 C CB  . ALA   B 20  ? 0.2220 0.6523 0.3474 -0.0382 0.0008  0.1107  42  ALA   B CB  
2450 N N   . GLY   B 21  ? 0.1898 0.5891 0.2964 -0.0017 -0.0001 0.1126  43  GLY   B N   
2451 C CA  . GLY   B 21  ? 0.1897 0.6057 0.3179 -0.0077 0.0114  0.0979  43  GLY   B CA  
2452 C C   . GLY   B 21  ? 0.2009 0.5849 0.2960 0.0105  0.0196  0.1009  43  GLY   B C   
2453 O O   . GLY   B 21  ? 0.1935 0.6090 0.3009 0.0386  0.0325  0.0978  43  GLY   B O   
2454 N N   . HIS   B 22  ? 0.2383 0.5569 0.2617 0.0018  0.0381  0.0884  44  HIS   B N   
2455 C CA  . HIS   B 22  ? 0.2071 0.5358 0.2455 0.0104  0.0261  0.0899  44  HIS   B CA  
2456 C C   . HIS   B 22  ? 0.2017 0.5377 0.2607 0.0024  0.0193  0.1111  44  HIS   B C   
2457 O O   . HIS   B 22  ? 0.2313 0.5684 0.2354 -0.0075 0.0143  0.1121  44  HIS   B O   
2458 C CB  . HIS   B 22  ? 0.1937 0.5111 0.2216 -0.0013 0.0257  0.0764  44  HIS   B CB  
2459 C CG  . HIS   B 22  ? 0.1874 0.4704 0.2013 0.0045  0.0292  0.0794  44  HIS   B CG  
2460 N ND1 . HIS   B 22  ? 0.1895 0.4517 0.1919 0.0074  0.0028  0.0691  44  HIS   B ND1 
2461 C CD2 . HIS   B 22  ? 0.1755 0.4503 0.2048 0.0103  0.0326  0.0684  44  HIS   B CD2 
2462 C CE1 . HIS   B 22  ? 0.1812 0.4466 0.2084 0.0282  0.0087  0.0583  44  HIS   B CE1 
2463 N NE2 . HIS   B 22  ? 0.1940 0.4565 0.2088 0.0068  0.0338  0.0685  44  HIS   B NE2 
2464 N N   . THR   B 23  ? 0.1674 0.5241 0.2968 -0.0018 0.0194  0.1248  45  THR   B N   
2465 C CA  . THR   B 23  ? 0.1968 0.5061 0.2669 0.0164  0.0255  0.1345  45  THR   B CA  
2466 C C   . THR   B 23  ? 0.1901 0.4974 0.2595 0.0257  0.0087  0.1423  45  THR   B C   
2467 O O   . THR   B 23  ? 0.1305 0.5509 0.2903 0.0502  -0.0120 0.1421  45  THR   B O   
2468 C CB  . THR   B 23  ? 0.2306 0.5185 0.2814 0.0214  0.0177  0.1229  45  THR   B CB  
2469 O OG1 . THR   B 23  ? 0.2289 0.5127 0.3011 0.0177  -0.0085 0.1116  45  THR   B OG1 
2470 C CG2 . THR   B 23  ? 0.2473 0.5331 0.2884 0.0343  0.0169  0.1155  45  THR   B CG2 
2471 N N   . LYS   B 24  ? 0.1727 0.4873 0.2411 -0.0033 0.0142  0.1449  46  LYS   B N   
2472 C CA  . LYS   B 24  ? 0.1950 0.4621 0.2572 -0.0018 -0.0102 0.1120  46  LYS   B CA  
2473 C C   . LYS   B 24  ? 0.2014 0.4300 0.2662 -0.0243 0.0053  0.1084  46  LYS   B C   
2474 O O   . LYS   B 24  ? 0.1664 0.4239 0.2745 -0.0207 0.0006  0.1118  46  LYS   B O   
2475 C CB  . LYS   B 24  ? 0.1963 0.4591 0.2545 -0.0033 -0.0189 0.1116  46  LYS   B CB  
2476 C CG  . LYS   B 24  ? 0.2331 0.4474 0.2527 -0.0088 -0.0082 0.1037  46  LYS   B CG  
2477 C CD  . LYS   B 24  ? 0.2403 0.4278 0.2496 0.0069  -0.0110 0.1045  46  LYS   B CD  
2478 C CE  . LYS   B 24  ? 0.2323 0.4214 0.2175 0.0171  -0.0142 0.0933  46  LYS   B CE  
2479 N NZ  . LYS   B 24  ? 0.2239 0.3753 0.2058 0.0088  -0.0316 0.0959  46  LYS   B NZ  
2480 N N   . ALA   B 25  ? 0.1921 0.4233 0.2679 -0.0263 0.0098  0.1079  47  ALA   B N   
2481 C CA  . ALA   B 25  ? 0.1864 0.4422 0.2481 -0.0328 0.0078  0.1003  47  ALA   B CA  
2482 C C   . ALA   B 25  ? 0.1976 0.4206 0.2190 -0.0444 0.0146  0.1045  47  ALA   B C   
2483 O O   . ALA   B 25  ? 0.1633 0.4303 0.2395 -0.0565 0.0121  0.1125  47  ALA   B O   
2484 C CB  . ALA   B 25  ? 0.1994 0.4478 0.2296 -0.0314 0.0192  0.1075  47  ALA   B CB  
2485 N N   . VAL   B 26  ? 0.1880 0.3996 0.2167 -0.0608 0.0012  0.1026  48  VAL   B N   
2486 C CA  . VAL   B 26  ? 0.1898 0.4098 0.1952 -0.0463 0.0026  0.0903  48  VAL   B CA  
2487 C C   . VAL   B 26  ? 0.1858 0.3846 0.1905 -0.0330 -0.0118 0.0760  48  VAL   B C   
2488 O O   . VAL   B 26  ? 0.1991 0.4167 0.2187 -0.0332 -0.0171 0.0393  48  VAL   B O   
2489 C CB  . VAL   B 26  ? 0.1960 0.4014 0.2304 -0.0564 0.0103  0.1051  48  VAL   B CB  
2490 C CG1 . VAL   B 26  ? 0.2020 0.3799 0.2015 -0.0666 0.0269  0.1001  48  VAL   B CG1 
2491 C CG2 . VAL   B 26  ? 0.2224 0.4401 0.2411 -0.0584 0.0187  0.0988  48  VAL   B CG2 
2492 N N   . SER   B 27  ? 0.1775 0.3640 0.1821 -0.0276 -0.0072 0.0698  49  SER   B N   
2493 C CA  . SER   B 27  ? 0.1777 0.3403 0.1764 -0.0218 0.0021  0.0799  49  SER   B CA  
2494 C C   . SER   B 27  ? 0.1750 0.3264 0.1799 -0.0243 0.0087  0.0779  49  SER   B C   
2495 O O   . SER   B 27  ? 0.1970 0.3010 0.1572 -0.0333 0.0108  0.0749  49  SER   B O   
2496 C CB  . SER   B 27  ? 0.1772 0.3264 0.1740 -0.0196 -0.0047 0.0763  49  SER   B CB  
2497 O OG  . SER   B 27  ? 0.1843 0.3224 0.1710 -0.0065 -0.0019 0.0737  49  SER   B OG  
2498 N N   . SER   B 28  ? 0.1835 0.3247 0.1931 -0.0295 0.0218  0.0812  50  SER   B N   
2499 C CA  . SER   B 28  ? 0.1865 0.3068 0.2092 -0.0332 0.0270  0.0814  50  SER   B CA  
2500 C C   . SER   B 28  ? 0.1747 0.3123 0.2091 -0.0291 0.0326  0.0751  50  SER   B C   
2501 O O   . SER   B 28  ? 0.1979 0.3571 0.2126 -0.0127 0.0539  0.0628  50  SER   B O   
2502 C CB  . SER   B 28  ? 0.2003 0.3117 0.2601 -0.0500 0.0357  0.1061  50  SER   B CB  
2503 O OG  . SER   B 28  ? 0.2450 0.3643 0.2677 -0.0599 0.0384  0.0921  50  SER   B OG  
2504 N N   . VAL   B 29  ? 0.1638 0.3163 0.1905 -0.0218 0.0328  0.0733  51  VAL   B N   
2505 C CA  . VAL   B 29  ? 0.1649 0.3129 0.1876 -0.0246 0.0333  0.0571  51  VAL   B CA  
2506 C C   . VAL   B 29  ? 0.1557 0.2862 0.1710 -0.0280 0.0422  0.0632  51  VAL   B C   
2507 O O   . VAL   B 29  ? 0.1584 0.2856 0.1685 -0.0287 0.0516  0.0601  51  VAL   B O   
2508 C CB  . VAL   B 29  ? 0.1688 0.3208 0.1954 -0.0334 0.0260  0.0665  51  VAL   B CB  
2509 C CG1 . VAL   B 29  ? 0.1609 0.3437 0.2417 -0.0420 0.0152  0.0541  51  VAL   B CG1 
2510 C CG2 . VAL   B 29  ? 0.1693 0.3229 0.2077 -0.0390 0.0151  0.0747  51  VAL   B CG2 
2511 N N   . LYS   B 30  ? 0.1626 0.2968 0.1810 -0.0307 0.0433  0.0546  52  LYS   B N   
2512 C CA  . LYS   B 30  ? 0.1898 0.2848 0.1661 -0.0224 0.0375  0.0766  52  LYS   B CA  
2513 C C   . LYS   B 30  ? 0.1815 0.3063 0.1793 -0.0202 0.0483  0.0615  52  LYS   B C   
2514 O O   . LYS   B 30  ? 0.1809 0.2984 0.1879 -0.0162 0.0308  0.0495  52  LYS   B O   
2515 C CB  . LYS   B 30  ? 0.1994 0.3135 0.1753 -0.0233 0.0529  0.0714  52  LYS   B CB  
2516 C CG  . LYS   B 30  ? 0.2023 0.3022 0.1691 -0.0275 0.0475  0.0694  52  LYS   B CG  
2517 C CD  . LYS   B 30  ? 0.2201 0.3061 0.1910 -0.0321 0.0491  0.0660  52  LYS   B CD  
2518 C CE  . LYS   B 30  ? 0.2509 0.3131 0.2022 -0.0407 0.0559  0.0673  52  LYS   B CE  
2519 N NZ  . LYS   B 30  ? 0.2414 0.3281 0.2181 -0.0445 0.0559  0.0777  52  LYS   B NZ  
2520 N N   . PHE   B 31  ? 0.1801 0.3299 0.1790 -0.0169 0.0374  0.0765  53  PHE   B N   
2521 C CA  . PHE   B 31  ? 0.2129 0.3412 0.1827 -0.0262 0.0324  0.0819  53  PHE   B CA  
2522 C C   . PHE   B 31  ? 0.2206 0.3532 0.1808 -0.0186 0.0364  0.0767  53  PHE   B C   
2523 O O   . PHE   B 31  ? 0.2329 0.3676 0.1563 -0.0116 0.0519  0.0572  53  PHE   B O   
2524 C CB  . PHE   B 31  ? 0.2298 0.3493 0.1811 -0.0439 0.0175  0.0842  53  PHE   B CB  
2525 C CG  . PHE   B 31  ? 0.2378 0.3411 0.1860 -0.0524 0.0217  0.0940  53  PHE   B CG  
2526 C CD1 . PHE   B 31  ? 0.2546 0.3780 0.1834 -0.0634 0.0282  0.0839  53  PHE   B CD1 
2527 C CD2 . PHE   B 31  ? 0.2423 0.3339 0.1953 -0.0596 0.0212  0.1032  53  PHE   B CD2 
2528 C CE1 . PHE   B 31  ? 0.2565 0.3864 0.1894 -0.0599 0.0145  0.0778  53  PHE   B CE1 
2529 C CE2 . PHE   B 31  ? 0.2466 0.3403 0.2083 -0.0416 0.0020  0.0832  53  PHE   B CE2 
2530 C CZ  . PHE   B 31  ? 0.2621 0.3611 0.2074 -0.0551 0.0167  0.0761  53  PHE   B CZ  
2531 N N   . SER   B 32  ? 0.2000 0.3507 0.1870 -0.0085 0.0396  0.0782  54  SER   B N   
2532 C CA  . SER   B 32  ? 0.1873 0.3473 0.2107 -0.0156 0.0308  0.0839  54  SER   B CA  
2533 C C   . SER   B 32  ? 0.1832 0.3397 0.1990 -0.0201 0.0280  0.0785  54  SER   B C   
2534 O O   . SER   B 32  ? 0.1892 0.3265 0.1536 -0.0134 0.0270  0.0832  54  SER   B O   
2535 C CB  . SER   B 32  ? 0.1790 0.3685 0.2314 -0.0084 0.0242  0.0892  54  SER   B CB  
2536 O OG  . SER   B 32  ? 0.1375 0.3623 0.2258 -0.0081 0.0136  0.0903  54  SER   B OG  
2537 N N   . PRO   B 33  ? 0.1833 0.3192 0.1746 -0.0280 0.0292  0.0683  55  PRO   B N   
2538 C CA  . PRO   B 33  ? 0.1792 0.3126 0.1755 -0.0302 0.0220  0.0744  55  PRO   B CA  
2539 C C   . PRO   B 33  ? 0.2010 0.3385 0.1667 -0.0202 0.0175  0.0777  55  PRO   B C   
2540 O O   . PRO   B 33  ? 0.2106 0.3284 0.2012 -0.0267 0.0107  0.0716  55  PRO   B O   
2541 C CB  . PRO   B 33  ? 0.1854 0.3201 0.1843 -0.0273 0.0329  0.0701  55  PRO   B CB  
2542 C CG  . PRO   B 33  ? 0.1777 0.3071 0.1860 -0.0288 0.0272  0.0687  55  PRO   B CG  
2543 C CD  . PRO   B 33  ? 0.1777 0.3087 0.1730 -0.0286 0.0248  0.0700  55  PRO   B CD  
2544 N N   . ASN   B 34  ? 0.2047 0.3595 0.1737 -0.0124 0.0194  0.0757  56  ASN   B N   
2545 C CA  . ASN   B 34  ? 0.2193 0.3721 0.1857 -0.0179 0.0265  0.0699  56  ASN   B CA  
2546 C C   . ASN   B 34  ? 0.2294 0.3858 0.1912 -0.0219 0.0373  0.0825  56  ASN   B C   
2547 O O   . ASN   B 34  ? 0.2345 0.3776 0.1927 -0.0047 0.0470  0.0970  56  ASN   B O   
2548 C CB  . ASN   B 34  ? 0.2385 0.3743 0.1926 -0.0203 0.0220  0.0616  56  ASN   B CB  
2549 C CG  . ASN   B 34  ? 0.2481 0.3788 0.2070 -0.0205 0.0136  0.0500  56  ASN   B CG  
2550 O OD1 . ASN   B 34  ? 0.2354 0.4115 0.1837 -0.0510 0.0227  0.0680  56  ASN   B OD1 
2551 N ND2 . ASN   B 34  ? 0.2731 0.3758 0.2112 0.0068  0.0023  0.0312  56  ASN   B ND2 
2552 N N   . GLY   B 35  ? 0.2395 0.4007 0.1815 -0.0316 0.0255  0.0934  57  GLY   B N   
2553 C CA  . GLY   B 35  ? 0.2544 0.3989 0.1899 -0.0311 0.0189  0.0823  57  GLY   B CA  
2554 C C   . GLY   B 35  ? 0.2470 0.4005 0.2062 -0.0392 0.0206  0.0847  57  GLY   B C   
2555 O O   . GLY   B 35  ? 0.2267 0.4417 0.1903 -0.0435 -0.0293 0.0998  57  GLY   B O   
2556 N N   . GLU   B 36  ? 0.2561 0.3897 0.2057 -0.0294 0.0464  0.0896  58  GLU   B N   
2557 C CA  . GLU   B 36  ? 0.2578 0.3883 0.2277 -0.0215 0.0432  0.0920  58  GLU   B CA  
2558 C C   . GLU   B 36  ? 0.2192 0.3970 0.2120 -0.0265 0.0539  0.0842  58  GLU   B C   
2559 O O   . GLU   B 36  ? 0.2186 0.4081 0.2119 -0.0107 0.0578  0.0963  58  GLU   B O   
2560 C CB  . GLU   B 36  ? 0.2848 0.3839 0.2733 -0.0229 0.0441  0.0657  58  GLU   B CB  
2561 C CG  . GLU   B 36  ? 0.3280 0.3915 0.3054 -0.0305 0.0545  0.0473  58  GLU   B CG  
2562 C CD  . GLU   B 36  ? 0.3947 0.4377 0.3950 -0.0034 0.0674  -0.0055 58  GLU   B CD  
2563 O OE1 . GLU   B 36  ? 0.3775 0.4788 0.4420 -0.0738 0.1275  -0.0404 58  GLU   B OE1 
2564 O OE2 . GLU   B 36  ? 0.5890 0.3664 0.4626 0.1369  0.0373  -0.0141 58  GLU   B OE2 
2565 N N   . TRP   B 37  ? 0.1827 0.4063 0.2081 -0.0134 0.0469  0.1018  59  TRP   B N   
2566 C CA  . TRP   B 37  ? 0.1925 0.4259 0.2227 -0.0076 0.0384  0.1060  59  TRP   B CA  
2567 C C   . TRP   B 37  ? 0.1934 0.4255 0.2105 -0.0056 0.0338  0.1064  59  TRP   B C   
2568 O O   . TRP   B 37  ? 0.2031 0.4295 0.2149 0.0069  0.0443  0.1152  59  TRP   B O   
2569 C CB  . TRP   B 37  ? 0.2286 0.4228 0.2302 0.0036  0.0221  0.1044  59  TRP   B CB  
2570 C CG  . TRP   B 37  ? 0.2446 0.4298 0.2298 0.0088  0.0554  0.1041  59  TRP   B CG  
2571 C CD1 . TRP   B 37  ? 0.2778 0.4340 0.1936 0.0224  0.0532  0.1094  59  TRP   B CD1 
2572 C CD2 . TRP   B 37  ? 0.2712 0.4338 0.2361 0.0321  0.0557  0.0893  59  TRP   B CD2 
2573 N NE1 . TRP   B 37  ? 0.3006 0.4302 0.2432 0.0330  0.0315  0.0827  59  TRP   B NE1 
2574 C CE2 . TRP   B 37  ? 0.2775 0.4487 0.2282 0.0324  0.0571  0.0995  59  TRP   B CE2 
2575 C CE3 . TRP   B 37  ? 0.2791 0.4570 0.2346 0.0328  0.0607  0.0782  59  TRP   B CE3 
2576 C CZ2 . TRP   B 37  ? 0.3188 0.4714 0.2245 0.0576  0.0551  0.0693  59  TRP   B CZ2 
2577 C CZ3 . TRP   B 37  ? 0.3037 0.4613 0.2498 0.0472  0.0644  0.0706  59  TRP   B CZ3 
2578 C CH2 . TRP   B 37  ? 0.3115 0.4695 0.2269 0.0578  0.0741  0.0709  59  TRP   B CH2 
2579 N N   . LEU   B 38  ? 0.1896 0.4290 0.1889 -0.0121 0.0385  0.0978  60  LEU   B N   
2580 C CA  . LEU   B 38  ? 0.2104 0.4221 0.2012 -0.0060 0.0482  0.0834  60  LEU   B CA  
2581 C C   . LEU   B 38  ? 0.1871 0.4078 0.1843 0.0089  0.0504  0.0703  60  LEU   B C   
2582 O O   . LEU   B 38  ? 0.2024 0.4286 0.1833 0.0176  0.0519  0.0736  60  LEU   B O   
2583 C CB  . LEU   B 38  ? 0.2189 0.4379 0.2189 -0.0044 0.0316  0.0716  60  LEU   B CB  
2584 C CG  . LEU   B 38  ? 0.2548 0.4380 0.2447 0.0003  0.0264  0.0392  60  LEU   B CG  
2585 C CD1 . LEU   B 38  ? 0.2524 0.4298 0.2265 -0.0021 0.0325  0.0406  60  LEU   B CD1 
2586 C CD2 . LEU   B 38  ? 0.2612 0.4391 0.2800 -0.0048 0.0159  0.0315  60  LEU   B CD2 
2587 N N   . ALA   B 39  ? 0.1503 0.3776 0.1843 0.0066  0.0367  0.0716  61  ALA   B N   
2588 C CA  . ALA   B 39  ? 0.1631 0.3825 0.1739 0.0113  0.0414  0.0625  61  ALA   B CA  
2589 C C   . ALA   B 39  ? 0.1773 0.3834 0.1721 0.0097  0.0387  0.0716  61  ALA   B C   
2590 O O   . ALA   B 39  ? 0.1981 0.3651 0.1926 0.0024  0.0197  0.0762  61  ALA   B O   
2591 C CB  . ALA   B 39  ? 0.1624 0.3809 0.1638 0.0178  0.0476  0.0602  61  ALA   B CB  
2592 N N   . SER   B 40  ? 0.1806 0.3949 0.1810 0.0169  0.0357  0.0639  62  SER   B N   
2593 C CA  . SER   B 40  ? 0.1956 0.4020 0.1787 0.0125  0.0219  0.0722  62  SER   B CA  
2594 C C   . SER   B 40  ? 0.1830 0.3887 0.1785 0.0183  0.0338  0.0617  62  SER   B C   
2595 O O   . SER   B 40  ? 0.2046 0.3981 0.1813 0.0340  0.0306  0.0678  62  SER   B O   
2596 C CB  . SER   B 40  ? 0.1977 0.4112 0.1896 0.0203  0.0196  0.0748  62  SER   B CB  
2597 O OG  . SER   B 40  ? 0.2075 0.4299 0.2077 0.0197  0.0089  0.0697  62  SER   B OG  
2598 N N   . SER   B 41  ? 0.1810 0.3916 0.1890 0.0130  0.0444  0.0707  63  SER   B N   
2599 C CA  . SER   B 41  ? 0.1562 0.3761 0.1959 0.0108  0.0385  0.0690  63  SER   B CA  
2600 C C   . SER   B 41  ? 0.1219 0.3788 0.2111 0.0020  0.0333  0.0640  63  SER   B C   
2601 O O   . SER   B 41  ? 0.1179 0.3842 0.1988 0.0085  0.0489  0.0672  63  SER   B O   
2602 C CB  . SER   B 41  ? 0.1603 0.3666 0.1927 0.0060  0.0319  0.0742  63  SER   B CB  
2603 O OG  . SER   B 41  ? 0.1716 0.3499 0.1741 0.0065  0.0276  0.0855  63  SER   B OG  
2604 N N   . SER   B 42  ? 0.1199 0.3894 0.2068 -0.0113 0.0260  0.0699  64  SER   B N   
2605 C CA  . SER   B 42  ? 0.1472 0.3892 0.1899 -0.0152 0.0162  0.0579  64  SER   B CA  
2606 C C   . SER   B 42  ? 0.1463 0.3715 0.2013 -0.0193 0.0071  0.0616  64  SER   B C   
2607 O O   . SER   B 42  ? 0.1508 0.3856 0.1723 -0.0232 0.0042  0.0437  64  SER   B O   
2608 C CB  . SER   B 42  ? 0.1420 0.4049 0.1904 -0.0263 0.0012  0.0641  64  SER   B CB  
2609 O OG  . SER   B 42  ? 0.1592 0.4118 0.2038 -0.0418 -0.0097 0.0731  64  SER   B OG  
2610 N N   . ALA   B 43  ? 0.1610 0.3647 0.2003 -0.0156 -0.0034 0.0737  65  ALA   B N   
2611 C CA  . ALA   B 43  ? 0.1748 0.3639 0.2271 0.0047  -0.0144 0.0831  65  ALA   B CA  
2612 C C   . ALA   B 43  ? 0.1710 0.3791 0.2195 0.0178  -0.0136 0.0834  65  ALA   B C   
2613 O O   . ALA   B 43  ? 0.1907 0.3921 0.2302 0.0329  -0.0008 0.0888  65  ALA   B O   
2614 C CB  . ALA   B 43  ? 0.1697 0.3614 0.2460 0.0147  -0.0293 0.0760  65  ALA   B CB  
2615 N N   . ASP   B 44  ? 0.1675 0.3845 0.2277 0.0282  -0.0117 0.0881  66  ASP   B N   
2616 C CA  . ASP   B 44  ? 0.1930 0.3798 0.2415 0.0291  -0.0129 0.0869  66  ASP   B CA  
2617 C C   . ASP   B 44  ? 0.2147 0.3763 0.2351 0.0492  -0.0057 0.0705  66  ASP   B C   
2618 O O   . ASP   B 44  ? 0.2242 0.3254 0.2340 0.0591  -0.0086 0.0777  66  ASP   B O   
2619 C CB  . ASP   B 44  ? 0.1897 0.4021 0.2380 0.0265  -0.0171 0.0891  66  ASP   B CB  
2620 C CG  . ASP   B 44  ? 0.1861 0.3963 0.2581 0.0151  -0.0155 0.1113  66  ASP   B CG  
2621 O OD1 . ASP   B 44  ? 0.1821 0.3707 0.2552 0.0266  -0.0233 0.0944  66  ASP   B OD1 
2622 O OD2 . ASP   B 44  ? 0.2043 0.4100 0.2697 0.0218  0.0049  0.1228  66  ASP   B OD2 
2623 N N   . LYS   B 45  ? 0.2156 0.3814 0.2121 0.0511  -0.0002 0.0720  67  LYS   B N   
2624 C CA  . LYS   B 45  ? 0.2295 0.3911 0.2251 0.0474  -0.0006 0.0651  67  LYS   B CA  
2625 C C   . LYS   B 45  ? 0.2239 0.3971 0.2171 0.0426  -0.0030 0.0585  67  LYS   B C   
2626 O O   . LYS   B 45  ? 0.2316 0.4040 0.2353 0.0301  -0.0130 0.0711  67  LYS   B O   
2627 C CB  . LYS   B 45  ? 0.2739 0.4082 0.2630 0.0656  0.0018  0.0557  67  LYS   B CB  
2628 C CG  . LYS   B 45  ? 0.3006 0.4086 0.2659 0.0626  -0.0016 0.0587  67  LYS   B CG  
2629 C CD  . LYS   B 45  ? 0.3740 0.4269 0.3423 0.0734  0.0021  0.0628  67  LYS   B CD  
2630 C CE  . LYS   B 45  ? 0.4545 0.4481 0.3922 0.0923  -0.0201 0.0680  67  LYS   B CE  
2631 N NZ  . LYS   B 45  ? 0.5369 0.4654 0.4839 0.1120  -0.0199 0.0307  67  LYS   B NZ  
2632 N N   . LEU   B 46  ? 0.2257 0.4004 0.2026 0.0467  -0.0084 0.0604  68  LEU   B N   
2633 C CA  . LEU   B 46  ? 0.2192 0.4314 0.2149 0.0615  0.0090  0.0707  68  LEU   B CA  
2634 C C   . LEU   B 46  ? 0.2187 0.4178 0.2056 0.0569  0.0147  0.0619  68  LEU   B C   
2635 O O   . LEU   B 46  ? 0.1695 0.3931 0.1949 0.0589  0.0392  0.0793  68  LEU   B O   
2636 C CB  . LEU   B 46  ? 0.2181 0.4595 0.2348 0.0461  0.0050  0.0838  68  LEU   B CB  
2637 C CG  . LEU   B 46  ? 0.2392 0.4792 0.2839 0.0587  0.0053  0.0851  68  LEU   B CG  
2638 C CD1 . LEU   B 46  ? 0.2318 0.4883 0.3013 0.0609  -0.0116 0.1038  68  LEU   B CD1 
2639 C CD2 . LEU   B 46  ? 0.2416 0.4987 0.2813 0.0553  0.0019  0.0846  68  LEU   B CD2 
2640 N N   . ILE   B 47  ? 0.2290 0.4201 0.1997 0.0522  0.0212  0.0682  69  ILE   B N   
2641 C CA  . ILE   B 47  ? 0.2058 0.4223 0.2016 0.0559  0.0302  0.0555  69  ILE   B CA  
2642 C C   . ILE   B 47  ? 0.2018 0.4389 0.2011 0.0675  0.0357  0.0525  69  ILE   B C   
2643 O O   . ILE   B 47  ? 0.2296 0.4693 0.2421 0.0793  0.0528  0.0394  69  ILE   B O   
2644 C CB  . ILE   B 47  ? 0.2038 0.4419 0.2284 0.0445  0.0340  0.0418  69  ILE   B CB  
2645 C CG1 . ILE   B 47  ? 0.1842 0.4512 0.2535 0.0356  0.0322  0.0286  69  ILE   B CG1 
2646 C CG2 . ILE   B 47  ? 0.1848 0.4488 0.2197 0.0494  0.0278  0.0375  69  ILE   B CG2 
2647 C CD1 . ILE   B 47  ? 0.2195 0.4621 0.2770 0.0408  0.0244  0.0126  69  ILE   B CD1 
2648 N N   . LYS   B 48  ? 0.2018 0.4618 0.2096 0.0610  0.0488  0.0422  70  LYS   B N   
2649 C CA  . LYS   B 48  ? 0.2219 0.4811 0.2094 0.0557  0.0539  0.0589  70  LYS   B CA  
2650 C C   . LYS   B 48  ? 0.2457 0.4752 0.2217 0.0558  0.0501  0.0580  70  LYS   B C   
2651 O O   . LYS   B 48  ? 0.2284 0.4761 0.1769 0.0377  0.0761  0.0800  70  LYS   B O   
2652 C CB  . LYS   B 48  ? 0.2181 0.4989 0.2248 0.0568  0.0502  0.0491  70  LYS   B CB  
2653 C CG  . LYS   B 48  ? 0.2133 0.5170 0.2389 0.0539  0.0467  0.0541  70  LYS   B CG  
2654 C CD  . LYS   B 48  ? 0.2018 0.5313 0.2545 0.0620  0.0313  0.0509  70  LYS   B CD  
2655 C CE  . LYS   B 48  ? 0.2237 0.5387 0.2611 0.0635  0.0303  0.0484  70  LYS   B CE  
2656 N NZ  . LYS   B 48  ? 0.1938 0.5558 0.2813 0.0665  0.0292  0.0695  70  LYS   B NZ  
2657 N N   . ILE   B 49  ? 0.2451 0.4709 0.2134 0.0619  0.0519  0.0799  71  ILE   B N   
2658 C CA  . ILE   B 49  ? 0.2428 0.4700 0.2040 0.0468  0.0503  0.0706  71  ILE   B CA  
2659 C C   . ILE   B 49  ? 0.2281 0.4839 0.2336 0.0393  0.0472  0.0712  71  ILE   B C   
2660 O O   . ILE   B 49  ? 0.2235 0.4991 0.2767 0.0481  0.0431  0.0670  71  ILE   B O   
2661 C CB  . ILE   B 49  ? 0.2610 0.4531 0.2029 0.0524  0.0427  0.0689  71  ILE   B CB  
2662 C CG1 . ILE   B 49  ? 0.2371 0.4445 0.2078 0.0581  0.0591  0.0588  71  ILE   B CG1 
2663 C CG2 . ILE   B 49  ? 0.2949 0.4636 0.1928 0.0453  0.0267  0.0668  71  ILE   B CG2 
2664 C CD1 . ILE   B 49  ? 0.2447 0.4341 0.2125 0.0605  0.0607  0.0528  71  ILE   B CD1 
2665 N N   . TRP   B 50  ? 0.1923 0.4999 0.2398 0.0250  0.0397  0.0788  72  TRP   B N   
2666 C CA  . TRP   B 50  ? 0.1844 0.5066 0.2274 0.0070  0.0601  0.0933  72  TRP   B CA  
2667 C C   . TRP   B 50  ? 0.1617 0.4968 0.2239 -0.0080 0.0539  0.1084  72  TRP   B C   
2668 O O   . TRP   B 50  ? 0.1553 0.5274 0.2205 -0.0229 0.0756  0.1207  72  TRP   B O   
2669 C CB  . TRP   B 50  ? 0.1835 0.5092 0.2321 0.0128  0.0391  0.1063  72  TRP   B CB  
2670 C CG  . TRP   B 50  ? 0.1921 0.5279 0.2358 0.0240  0.0182  0.1024  72  TRP   B CG  
2671 C CD1 . TRP   B 50  ? 0.1511 0.5187 0.2469 0.0133  0.0021  0.0933  72  TRP   B CD1 
2672 C CD2 . TRP   B 50  ? 0.1867 0.5231 0.2577 0.0256  0.0116  0.1026  72  TRP   B CD2 
2673 N NE1 . TRP   B 50  ? 0.1906 0.5199 0.2609 0.0295  0.0065  0.1065  72  TRP   B NE1 
2674 C CE2 . TRP   B 50  ? 0.1793 0.5254 0.2569 0.0330  0.0007  0.1097  72  TRP   B CE2 
2675 C CE3 . TRP   B 50  ? 0.1942 0.5467 0.2837 0.0362  0.0005  0.1149  72  TRP   B CE3 
2676 C CZ2 . TRP   B 50  ? 0.1863 0.5326 0.2631 0.0376  0.0024  0.1177  72  TRP   B CZ2 
2677 C CZ3 . TRP   B 50  ? 0.2133 0.5666 0.2892 0.0315  0.0037  0.1290  72  TRP   B CZ3 
2678 C CH2 . TRP   B 50  ? 0.1938 0.5646 0.2800 0.0297  0.0009  0.1263  72  TRP   B CH2 
2679 N N   . GLY   B 51  ? 0.1636 0.5285 0.2124 -0.0074 0.0480  0.1153  73  GLY   B N   
2680 C CA  . GLY   B 51  ? 0.1678 0.5098 0.2475 -0.0245 0.0302  0.1248  73  GLY   B CA  
2681 C C   . GLY   B 51  ? 0.1979 0.5063 0.2176 -0.0504 0.0273  0.1233  73  GLY   B C   
2682 O O   . GLY   B 51  ? 0.2222 0.5231 0.2250 -0.0711 0.0107  0.1491  73  GLY   B O   
2683 N N   . ALA   B 52  ? 0.2173 0.4647 0.2140 -0.0616 0.0160  0.1274  74  ALA   B N   
2684 C CA  . ALA   B 52  ? 0.2317 0.4840 0.2234 -0.0767 0.0075  0.1184  74  ALA   B CA  
2685 C C   . ALA   B 52  ? 0.2774 0.4736 0.2138 -0.0872 0.0012  0.1099  74  ALA   B C   
2686 O O   . ALA   B 52  ? 0.3022 0.4671 0.2183 -0.0740 0.0058  0.1021  74  ALA   B O   
2687 C CB  . ALA   B 52  ? 0.2369 0.4845 0.2633 -0.0740 -0.0024 0.1239  74  ALA   B CB  
2688 N N   . TYR   B 53  ? 0.2443 0.4728 0.2266 -0.0866 0.0111  0.1165  75  TYR   B N   
2689 C CA  . TYR   B 53  ? 0.2721 0.4821 0.2482 -0.0854 -0.0025 0.1272  75  TYR   B CA  
2690 C C   . TYR   B 53  ? 0.2778 0.4779 0.2949 -0.0912 -0.0156 0.1113  75  TYR   B C   
2691 O O   . TYR   B 53  ? 0.3358 0.4400 0.3289 -0.0970 -0.0172 0.1332  75  TYR   B O   
2692 C CB  . TYR   B 53  ? 0.2786 0.4884 0.2328 -0.0779 0.0042  0.1417  75  TYR   B CB  
2693 C CG  . TYR   B 53  ? 0.2668 0.4862 0.2222 -0.0784 0.0184  0.1386  75  TYR   B CG  
2694 C CD1 . TYR   B 53  ? 0.2920 0.4937 0.2345 -0.0732 0.0215  0.1214  75  TYR   B CD1 
2695 C CD2 . TYR   B 53  ? 0.2810 0.4957 0.2065 -0.0662 0.0196  0.1256  75  TYR   B CD2 
2696 C CE1 . TYR   B 53  ? 0.2954 0.4769 0.2292 -0.0747 0.0194  0.1338  75  TYR   B CE1 
2697 C CE2 . TYR   B 53  ? 0.2748 0.4983 0.1985 -0.0692 0.0212  0.1151  75  TYR   B CE2 
2698 C CZ  . TYR   B 53  ? 0.2768 0.4832 0.2214 -0.0712 0.0227  0.1318  75  TYR   B CZ  
2699 O OH  . TYR   B 53  ? 0.2551 0.4688 0.2537 -0.0400 0.0538  0.1382  75  TYR   B OH  
2700 N N   . ASP   B 54  ? 0.2881 0.4532 0.3048 -0.0885 0.0111  0.0996  76  ASP   B N   
2701 C CA  . ASP   B 54  ? 0.2940 0.5281 0.3333 -0.0741 0.0289  0.0772  76  ASP   B CA  
2702 C C   . ASP   B 54  ? 0.2485 0.5625 0.3283 -0.0647 0.0440  0.1007  76  ASP   B C   
2703 O O   . ASP   B 54  ? 0.2248 0.5668 0.3241 -0.0481 0.0478  0.1012  76  ASP   B O   
2704 C CB  . ASP   B 54  ? 0.3349 0.5272 0.3419 -0.0907 0.0413  0.0440  76  ASP   B CB  
2705 C CG  . ASP   B 54  ? 0.3676 0.5343 0.3486 -0.0980 0.0652  0.0165  76  ASP   B CG  
2706 O OD1 . ASP   B 54  ? 0.3455 0.5314 0.3463 -0.0865 0.0647  0.0112  76  ASP   B OD1 
2707 O OD2 . ASP   B 54  ? 0.4249 0.5547 0.4047 -0.0839 0.1398  -0.0114 76  ASP   B OD2 
2708 N N   . GLY   B 55  ? 0.2379 0.5817 0.3478 -0.0602 0.0456  0.0971  77  GLY   B N   
2709 C CA  . GLY   B 55  ? 0.2202 0.5943 0.3490 -0.0504 0.0634  0.1013  77  GLY   B CA  
2710 C C   . GLY   B 55  ? 0.2425 0.6114 0.3333 -0.0057 0.0625  0.0874  77  GLY   B C   
2711 O O   . GLY   B 55  ? 0.2821 0.6128 0.3799 -0.0170 0.0110  0.1013  77  GLY   B O   
2712 N N   . LYS   B 56  ? 0.2032 0.6194 0.3332 -0.0006 0.0898  0.0823  78  LYS   B N   
2713 C CA  . LYS   B 56  ? 0.2455 0.6194 0.2865 0.0167  0.0917  0.0861  78  LYS   B CA  
2714 C C   . LYS   B 56  ? 0.2166 0.6040 0.3088 0.0365  0.0643  0.0937  78  LYS   B C   
2715 O O   . LYS   B 56  ? 0.1952 0.5969 0.3159 0.0595  0.1021  0.1257  78  LYS   B O   
2716 C CB  . LYS   B 56  ? 0.2979 0.6310 0.2643 0.0079  0.1096  0.0908  78  LYS   B CB  
2717 N N   . PHE   B 57  ? 0.1983 0.6344 0.3155 0.0414  0.0532  0.0890  79  PHE   B N   
2718 C CA  . PHE   B 57  ? 0.1887 0.6262 0.3198 0.0684  0.1002  0.0858  79  PHE   B CA  
2719 C C   . PHE   B 57  ? 0.2018 0.6402 0.2863 0.0974  0.1440  0.0717  79  PHE   B C   
2720 O O   . PHE   B 57  ? 0.1616 0.6637 0.3295 0.0850  0.1670  0.0994  79  PHE   B O   
2721 C CB  . PHE   B 57  ? 0.2287 0.6207 0.3422 0.0677  0.1045  0.0925  79  PHE   B CB  
2722 C CG  . PHE   B 57  ? 0.2508 0.6077 0.3362 0.0547  0.0947  0.1140  79  PHE   B CG  
2723 C CD1 . PHE   B 57  ? 0.2512 0.6040 0.3480 0.0508  0.0929  0.1257  79  PHE   B CD1 
2724 C CD2 . PHE   B 57  ? 0.2496 0.6044 0.3685 0.0597  0.0950  0.1286  79  PHE   B CD2 
2725 C CE1 . PHE   B 57  ? 0.2852 0.6125 0.3228 0.0524  0.0876  0.1314  79  PHE   B CE1 
2726 C CE2 . PHE   B 57  ? 0.2545 0.6041 0.3534 0.0465  0.0880  0.1336  79  PHE   B CE2 
2727 C CZ  . PHE   B 57  ? 0.2767 0.6114 0.3419 0.0597  0.0907  0.1345  79  PHE   B CZ  
2728 N N   . GLU   B 58  ? 0.2422 0.6348 0.2859 0.0924  0.0772  0.0782  80  GLU   B N   
2729 C CA  . GLU   B 58  ? 0.3020 0.6172 0.2826 0.1184  0.0774  0.0674  80  GLU   B CA  
2730 C C   . GLU   B 58  ? 0.3004 0.5975 0.2996 0.1446  0.0896  0.0624  80  GLU   B C   
2731 O O   . GLU   B 58  ? 0.3761 0.5828 0.3208 0.1585  0.1084  0.0581  80  GLU   B O   
2732 C CB  . GLU   B 58  ? 0.3068 0.6099 0.2861 0.1342  0.0730  0.0672  80  GLU   B CB  
2733 C CG  . GLU   B 58  ? 0.3871 0.6488 0.2801 0.1050  0.0530  0.0815  80  GLU   B CG  
2734 C CD  . GLU   B 58  ? 0.4208 0.6718 0.3515 0.0913  0.1040  0.0575  80  GLU   B CD  
2735 O OE1 . GLU   B 58  ? 0.4088 0.6991 0.3287 0.0753  0.1590  0.1149  80  GLU   B OE1 
2736 O OE2 . GLU   B 58  ? 0.5295 0.6769 0.3588 0.1060  0.0500  0.0235  80  GLU   B OE2 
2737 N N   . LYS   B 59  ? 0.2779 0.5898 0.2904 0.1466  0.0686  0.0720  81  LYS   B N   
2738 C CA  . LYS   B 59  ? 0.2760 0.5841 0.2589 0.1448  0.0651  0.0633  81  LYS   B CA  
2739 C C   . LYS   B 59  ? 0.2837 0.5677 0.2403 0.1325  0.0540  0.0553  81  LYS   B C   
2740 O O   . LYS   B 59  ? 0.2950 0.5387 0.2212 0.1409  0.0383  0.0932  81  LYS   B O   
2741 C CB  . LYS   B 59  ? 0.2688 0.5962 0.2713 0.1444  0.0592  0.0450  81  LYS   B CB  
2742 C CG  . LYS   B 59  ? 0.2781 0.6412 0.3499 0.1526  0.0366  0.0242  81  LYS   B CG  
2743 C CD  . LYS   B 59  ? 0.3212 0.6786 0.3644 0.1608  0.0254  0.0073  81  LYS   B CD  
2744 C CE  . LYS   B 59  ? 0.3463 0.7185 0.3745 0.1636  0.0481  -0.0212 81  LYS   B CE  
2745 N NZ  . LYS   B 59  ? 0.3619 0.7377 0.3923 0.1550  0.0587  -0.0282 81  LYS   B NZ  
2746 N N   . THR   B 60  ? 0.3245 0.5488 0.2201 0.1246  0.0634  0.0419  82  THR   B N   
2747 C CA  . THR   B 60  ? 0.3244 0.5539 0.1954 0.1018  0.0272  0.0290  82  THR   B CA  
2748 C C   . THR   B 60  ? 0.3414 0.5124 0.2073 0.1143  0.0254  0.0301  82  THR   B C   
2749 O O   . THR   B 60  ? 0.3436 0.4880 0.2332 0.1390  0.0139  0.0301  82  THR   B O   
2750 C CB  . THR   B 60  ? 0.3264 0.5611 0.2091 0.1077  0.0198  0.0330  82  THR   B CB  
2751 O OG1 . THR   B 60  ? 0.2827 0.5952 0.2037 0.1133  -0.0083 0.0324  82  THR   B OG1 
2752 C CG2 . THR   B 60  ? 0.3368 0.5852 0.2149 0.0994  0.0374  0.0123  82  THR   B CG2 
2753 N N   . ILE   B 61  ? 0.3196 0.4620 0.2127 0.1070  0.0129  0.0505  83  ILE   B N   
2754 C CA  . ILE   B 61  ? 0.3351 0.4490 0.2201 0.1100  -0.0056 0.0384  83  ILE   B CA  
2755 C C   . ILE   B 61  ? 0.3496 0.4205 0.2313 0.1051  0.0151  0.0374  83  ILE   B C   
2756 O O   . ILE   B 61  ? 0.3331 0.4107 0.2055 0.0909  0.0162  0.0427  83  ILE   B O   
2757 C CB  . ILE   B 61  ? 0.3300 0.4506 0.2172 0.1021  -0.0213 0.0354  83  ILE   B CB  
2758 C CG1 . ILE   B 61  ? 0.3461 0.4538 0.2329 0.1083  -0.0384 0.0564  83  ILE   B CG1 
2759 C CG2 . ILE   B 61  ? 0.3304 0.4572 0.2376 0.0993  -0.0184 0.0330  83  ILE   B CG2 
2760 C CD1 . ILE   B 61  ? 0.3639 0.4416 0.2398 0.1077  -0.0412 0.0631  83  ILE   B CD1 
2761 N N   . SER   B 62  ? 0.3488 0.4050 0.2564 0.1335  0.0193  0.0210  84  SER   B N   
2762 C CA  . SER   B 62  ? 0.3710 0.3940 0.2662 0.1244  0.0242  0.0258  84  SER   B CA  
2763 C C   . SER   B 62  ? 0.3340 0.3649 0.2682 0.1236  0.0032  0.0287  84  SER   B C   
2764 O O   . SER   B 62  ? 0.3262 0.3477 0.2750 0.1187  0.0149  0.0325  84  SER   B O   
2765 C CB  . SER   B 62  ? 0.4077 0.4430 0.3077 0.1270  0.0081  0.0220  84  SER   B CB  
2766 O OG  . SER   B 62  ? 0.4737 0.4458 0.3745 0.1582  0.0285  0.0498  84  SER   B OG  
2767 N N   . GLY   B 63  ? 0.3138 0.3570 0.2778 0.1152  0.0124  0.0204  85  GLY   B N   
2768 C CA  . GLY   B 63  ? 0.3102 0.3520 0.2886 0.1070  -0.0050 0.0361  85  GLY   B CA  
2769 C C   . GLY   B 63  ? 0.3458 0.3468 0.2613 0.0947  -0.0303 0.0498  85  GLY   B C   
2770 O O   . GLY   B 63  ? 0.4020 0.3594 0.3331 0.0686  -0.0330 0.0724  85  GLY   B O   
2771 N N   . HIS   B 64  ? 0.3448 0.3410 0.2320 0.0863  -0.0262 0.0330  86  HIS   B N   
2772 C CA  . HIS   B 64  ? 0.3414 0.3350 0.2437 0.0801  -0.0218 0.0364  86  HIS   B CA  
2773 C C   . HIS   B 64  ? 0.3608 0.3466 0.2326 0.0819  -0.0188 0.0413  86  HIS   B C   
2774 O O   . HIS   B 64  ? 0.3718 0.3810 0.2307 0.0917  -0.0110 0.0160  86  HIS   B O   
2775 C CB  . HIS   B 64  ? 0.3002 0.3074 0.2237 0.0616  -0.0238 0.0328  86  HIS   B CB  
2776 C CG  . HIS   B 64  ? 0.2591 0.2914 0.2093 0.0356  -0.0164 0.0358  86  HIS   B CG  
2777 N ND1 . HIS   B 64  ? 0.2334 0.2732 0.1941 0.0214  -0.0223 0.0361  86  HIS   B ND1 
2778 C CD2 . HIS   B 64  ? 0.2426 0.2900 0.2029 0.0231  -0.0257 0.0382  86  HIS   B CD2 
2779 C CE1 . HIS   B 64  ? 0.2357 0.2740 0.1966 0.0306  -0.0072 0.0343  86  HIS   B CE1 
2780 N NE2 . HIS   B 64  ? 0.2426 0.2796 0.1901 0.0292  -0.0117 0.0390  86  HIS   B NE2 
2781 N N   . LYS   B 65  ? 0.3718 0.3452 0.2546 0.0729  -0.0208 0.0717  87  LYS   B N   
2782 C CA  . LYS   B 65  ? 0.3672 0.3636 0.2868 0.0793  -0.0548 0.0611  87  LYS   B CA  
2783 C C   . LYS   B 65  ? 0.3152 0.3601 0.2667 0.0796  -0.0624 0.0689  87  LYS   B C   
2784 O O   . LYS   B 65  ? 0.3423 0.3545 0.2539 0.0816  -0.0853 0.0466  87  LYS   B O   
2785 C CB  . LYS   B 65  ? 0.4356 0.4086 0.3462 0.0548  -0.0578 0.0714  87  LYS   B CB  
2786 C CG  . LYS   B 65  ? 0.5072 0.4345 0.3826 0.0464  -0.0562 0.0599  87  LYS   B CG  
2787 C CD  . LYS   B 65  ? 0.5608 0.4699 0.4341 0.0119  -0.0405 0.0788  87  LYS   B CD  
2788 N N   . LEU   B 66  ? 0.2861 0.3481 0.2514 0.0638  -0.0492 0.0516  88  LEU   B N   
2789 C CA  . LEU   B 66  ? 0.2411 0.3695 0.2165 0.0581  -0.0180 0.0625  88  LEU   B CA  
2790 C C   . LEU   B 66  ? 0.2283 0.3598 0.1950 0.0403  -0.0100 0.0657  88  LEU   B C   
2791 O O   . LEU   B 66  ? 0.2278 0.3787 0.1896 0.0511  -0.0087 0.0817  88  LEU   B O   
2792 C CB  . LEU   B 66  ? 0.2596 0.3614 0.2124 0.0577  -0.0095 0.0749  88  LEU   B CB  
2793 C CG  . LEU   B 66  ? 0.2566 0.3552 0.2182 0.0673  -0.0136 0.0848  88  LEU   B CG  
2794 C CD1 . LEU   B 66  ? 0.2419 0.3553 0.2344 0.0775  -0.0228 0.0995  88  LEU   B CD1 
2795 C CD2 . LEU   B 66  ? 0.2475 0.3174 0.2171 0.0602  -0.0044 0.0867  88  LEU   B CD2 
2796 N N   . GLY   B 67  ? 0.1931 0.3498 0.2107 0.0340  -0.0007 0.0708  89  GLY   B N   
2797 C CA  . GLY   B 67  ? 0.1772 0.3391 0.2123 0.0299  -0.0056 0.0677  89  GLY   B CA  
2798 C C   . GLY   B 67  ? 0.1740 0.3351 0.2111 0.0231  -0.0009 0.0686  89  GLY   B C   
2799 O O   . GLY   B 67  ? 0.1810 0.3219 0.2183 0.0030  -0.0046 0.0724  89  GLY   B O   
2800 N N   . ILE   B 68  ? 0.1631 0.3373 0.1961 0.0158  0.0205  0.0594  90  ILE   B N   
2801 C CA  . ILE   B 68  ? 0.1738 0.3305 0.1768 0.0075  0.0044  0.0590  90  ILE   B CA  
2802 C C   . ILE   B 68  ? 0.1541 0.3449 0.1614 0.0050  0.0128  0.0639  90  ILE   B C   
2803 O O   . ILE   B 68  ? 0.1671 0.3520 0.1822 -0.0014 0.0179  0.0727  90  ILE   B O   
2804 C CB  . ILE   B 68  ? 0.1968 0.3497 0.1907 0.0113  -0.0020 0.0469  90  ILE   B CB  
2805 C CG1 . ILE   B 68  ? 0.2050 0.3677 0.2152 0.0208  -0.0017 0.0347  90  ILE   B CG1 
2806 C CG2 . ILE   B 68  ? 0.1830 0.3610 0.2129 0.0110  -0.0046 0.0458  90  ILE   B CG2 
2807 C CD1 . ILE   B 68  ? 0.2283 0.3751 0.2376 0.0087  0.0173  0.0353  90  ILE   B CD1 
2808 N N   . SER   B 69  ? 0.1359 0.3227 0.1609 -0.0056 0.0234  0.0609  91  SER   B N   
2809 C CA  . SER   B 69  ? 0.1388 0.3108 0.1829 -0.0105 0.0255  0.0597  91  SER   B CA  
2810 C C   . SER   B 69  ? 0.1528 0.2928 0.1928 -0.0102 0.0129  0.0528  91  SER   B C   
2811 O O   . SER   B 69  ? 0.1640 0.3026 0.2014 -0.0272 -0.0180 0.0388  91  SER   B O   
2812 C CB  . SER   B 69  ? 0.1545 0.3139 0.1952 0.0028  0.0385  0.0588  91  SER   B CB  
2813 O OG  . SER   B 69  ? 0.1479 0.3190 0.1994 0.0105  0.0463  0.0589  91  SER   B OG  
2814 N N   . ASP   B 70  ? 0.1591 0.2879 0.1871 0.0002  0.0234  0.0510  92  ASP   B N   
2815 C CA  . ASP   B 70  ? 0.1628 0.2858 0.1869 0.0037  0.0298  0.0504  92  ASP   B CA  
2816 C C   . ASP   B 70  ? 0.1821 0.2716 0.1826 0.0000  0.0423  0.0526  92  ASP   B C   
2817 O O   . ASP   B 70  ? 0.2027 0.2638 0.1480 -0.0254 0.0320  0.0478  92  ASP   B O   
2818 C CB  . ASP   B 70  ? 0.1594 0.2860 0.1986 0.0084  0.0357  0.0621  92  ASP   B CB  
2819 C CG  . ASP   B 70  ? 0.1542 0.2769 0.2049 0.0032  0.0375  0.0587  92  ASP   B CG  
2820 O OD1 . ASP   B 70  ? 0.1757 0.2820 0.1945 0.0024  0.0324  0.0618  92  ASP   B OD1 
2821 O OD2 . ASP   B 70  ? 0.1345 0.2391 0.1845 -0.0165 0.0414  0.0774  92  ASP   B OD2 
2822 N N   . VAL   B 71  ? 0.1857 0.2686 0.1671 -0.0012 0.0283  0.0489  93  VAL   B N   
2823 C CA  . VAL   B 71  ? 0.2000 0.2697 0.1772 -0.0027 0.0327  0.0419  93  VAL   B CA  
2824 C C   . VAL   B 71  ? 0.2024 0.2674 0.1710 0.0000  0.0257  0.0341  93  VAL   B C   
2825 O O   . VAL   B 71  ? 0.2261 0.2795 0.1543 0.0077  0.0052  0.0287  93  VAL   B O   
2826 C CB  . VAL   B 71  ? 0.2190 0.2989 0.2042 -0.0061 0.0484  0.0356  93  VAL   B CB  
2827 C CG1 . VAL   B 71  ? 0.2325 0.3107 0.2172 0.0011  0.0537  0.0326  93  VAL   B CG1 
2828 C CG2 . VAL   B 71  ? 0.2440 0.3292 0.2248 -0.0091 0.0472  0.0304  93  VAL   B CG2 
2829 N N   . ALA   B 72  ? 0.1786 0.2668 0.1746 -0.0064 0.0188  0.0478  94  ALA   B N   
2830 C CA  . ALA   B 72  ? 0.1886 0.2584 0.1719 0.0005  0.0310  0.0546  94  ALA   B CA  
2831 C C   . ALA   B 72  ? 0.1717 0.2564 0.1791 0.0043  0.0226  0.0394  94  ALA   B C   
2832 O O   . ALA   B 72  ? 0.1726 0.2678 0.2018 0.0195  0.0323  0.0368  94  ALA   B O   
2833 C CB  . ALA   B 72  ? 0.1931 0.2720 0.1700 -0.0097 0.0270  0.0635  94  ALA   B CB  
2834 N N   . TRP   B 73  ? 0.1926 0.2593 0.1782 0.0181  0.0243  0.0376  95  TRP   B N   
2835 C CA  . TRP   B 73  ? 0.1863 0.2827 0.1734 0.0241  0.0341  0.0328  95  TRP   B CA  
2836 C C   . TRP   B 73  ? 0.1712 0.2809 0.1644 0.0179  0.0389  0.0280  95  TRP   B C   
2837 O O   . TRP   B 73  ? 0.1555 0.2785 0.1606 0.0110  0.0414  0.0060  95  TRP   B O   
2838 C CB  . TRP   B 73  ? 0.1847 0.2914 0.1811 0.0288  0.0302  0.0490  95  TRP   B CB  
2839 C CG  . TRP   B 73  ? 0.1871 0.3214 0.1874 0.0354  0.0264  0.0544  95  TRP   B CG  
2840 C CD1 . TRP   B 73  ? 0.2009 0.3354 0.1863 0.0422  0.0300  0.0473  95  TRP   B CD1 
2841 C CD2 . TRP   B 73  ? 0.1919 0.3288 0.1863 0.0389  0.0329  0.0576  95  TRP   B CD2 
2842 N NE1 . TRP   B 73  ? 0.1894 0.3303 0.1695 0.0446  0.0398  0.0616  95  TRP   B NE1 
2843 C CE2 . TRP   B 73  ? 0.1951 0.3392 0.1868 0.0476  0.0277  0.0568  95  TRP   B CE2 
2844 C CE3 . TRP   B 73  ? 0.1936 0.3352 0.1587 0.0362  0.0332  0.0713  95  TRP   B CE3 
2845 C CZ2 . TRP   B 73  ? 0.2005 0.3397 0.1960 0.0600  0.0333  0.0574  95  TRP   B CZ2 
2846 C CZ3 . TRP   B 73  ? 0.1944 0.3458 0.1797 0.0513  0.0217  0.0560  95  TRP   B CZ3 
2847 C CH2 . TRP   B 73  ? 0.2058 0.3567 0.1901 0.0478  0.0281  0.0504  95  TRP   B CH2 
2848 N N   . SER   B 74  ? 0.1755 0.3036 0.1466 0.0230  0.0436  0.0273  96  SER   B N   
2849 C CA  . SER   B 74  ? 0.1930 0.3145 0.1540 0.0242  0.0360  0.0393  96  SER   B CA  
2850 C C   . SER   B 74  ? 0.2056 0.2999 0.1667 0.0221  0.0146  0.0403  96  SER   B C   
2851 O O   . SER   B 74  ? 0.2144 0.2847 0.1672 0.0243  0.0014  0.0340  96  SER   B O   
2852 C CB  . SER   B 74  ? 0.2029 0.3390 0.1440 0.0237  0.0319  0.0414  96  SER   B CB  
2853 O OG  . SER   B 74  ? 0.2138 0.3632 0.1843 0.0384  0.0340  0.0368  96  SER   B OG  
2854 N N   . SER   B 75  ? 0.1985 0.2856 0.1756 0.0172  0.0185  0.0369  97  SER   B N   
2855 C CA  . SER   B 75  ? 0.2161 0.2793 0.1952 0.0189  0.0095  0.0373  97  SER   B CA  
2856 C C   . SER   B 75  ? 0.2184 0.2895 0.1980 0.0229  0.0110  0.0491  97  SER   B C   
2857 O O   . SER   B 75  ? 0.2326 0.2963 0.2011 0.0100  0.0147  0.0554  97  SER   B O   
2858 C CB  . SER   B 75  ? 0.2203 0.2887 0.2033 0.0032  -0.0010 0.0316  97  SER   B CB  
2859 O OG  . SER   B 75  ? 0.2558 0.2790 0.2162 0.0009  0.0202  0.0220  97  SER   B OG  
2860 N N   . ASP   B 76  ? 0.2097 0.2972 0.1861 0.0331  0.0177  0.0383  98  ASP   B N   
2861 C CA  . ASP   B 76  ? 0.2378 0.3136 0.1696 0.0304  0.0130  0.0411  98  ASP   B CA  
2862 C C   . ASP   B 76  ? 0.2363 0.3113 0.1744 0.0357  0.0262  0.0293  98  ASP   B C   
2863 O O   . ASP   B 76  ? 0.2564 0.3254 0.1891 0.0477  0.0311  0.0298  98  ASP   B O   
2864 C CB  . ASP   B 76  ? 0.2476 0.3306 0.2004 0.0263  0.0031  0.0321  98  ASP   B CB  
2865 C CG  . ASP   B 76  ? 0.2574 0.3474 0.2106 0.0167  -0.0050 0.0425  98  ASP   B CG  
2866 O OD1 . ASP   B 76  ? 0.2429 0.3666 0.2180 0.0168  -0.0082 0.0605  98  ASP   B OD1 
2867 O OD2 . ASP   B 76  ? 0.2806 0.3824 0.2277 0.0164  -0.0311 0.0380  98  ASP   B OD2 
2868 N N   . SER   B 77  ? 0.2374 0.3196 0.1767 0.0355  0.0223  0.0158  99  SER   B N   
2869 C CA  . SER   B 77  ? 0.2438 0.3379 0.1711 0.0285  0.0196  0.0040  99  SER   B CA  
2870 C C   . SER   B 77  ? 0.2629 0.3533 0.1959 0.0352  0.0186  0.0133  99  SER   B C   
2871 O O   . SER   B 77  ? 0.2679 0.3504 0.2356 0.0444  -0.0205 0.0141  99  SER   B O   
2872 C CB  . SER   B 77  ? 0.2548 0.3349 0.1658 0.0216  0.0334  0.0094  99  SER   B CB  
2873 O OG  . SER   B 77  ? 0.2565 0.3408 0.1892 0.0165  0.0450  0.0111  99  SER   B OG  
2874 N N   . ASN   B 78  ? 0.2689 0.3808 0.1764 0.0421  0.0183  -0.0049 100 ASN   B N   
2875 C CA  . ASN   B 78  ? 0.2872 0.3888 0.2044 0.0650  0.0241  0.0178  100 ASN   B CA  
2876 C C   . ASN   B 78  ? 0.2903 0.3808 0.2153 0.0599  0.0219  0.0282  100 ASN   B C   
2877 O O   . ASN   B 78  ? 0.3230 0.3956 0.2416 0.0775  0.0281  0.0422  100 ASN   B O   
2878 C CB  . ASN   B 78  ? 0.3056 0.4180 0.2242 0.0806  0.0233  0.0021  100 ASN   B CB  
2879 C CG  . ASN   B 78  ? 0.3304 0.4456 0.2458 0.0548  0.0119  0.0242  100 ASN   B CG  
2880 O OD1 . ASN   B 78  ? 0.3407 0.4374 0.2360 0.0289  0.0223  0.0253  100 ASN   B OD1 
2881 N ND2 . ASN   B 78  ? 0.3275 0.4391 0.2509 0.0614  -0.0106 0.0361  100 ASN   B ND2 
2882 N N   . LEU   B 79  ? 0.2713 0.3441 0.1699 0.0474  0.0173  0.0458  101 LEU   B N   
2883 C CA  . LEU   B 79  ? 0.2681 0.3243 0.1937 0.0372  0.0185  0.0454  101 LEU   B CA  
2884 C C   . LEU   B 79  ? 0.2465 0.3217 0.1794 0.0351  0.0236  0.0449  101 LEU   B C   
2885 O O   . LEU   B 79  ? 0.2285 0.3225 0.1446 0.0679  0.0234  0.0222  101 LEU   B O   
2886 C CB  . LEU   B 79  ? 0.2917 0.3201 0.2145 0.0295  0.0265  0.0497  101 LEU   B CB  
2887 C CG  . LEU   B 79  ? 0.3047 0.3203 0.2283 0.0321  0.0115  0.0349  101 LEU   B CG  
2888 C CD1 . LEU   B 79  ? 0.3322 0.3282 0.2543 0.0233  0.0224  0.0294  101 LEU   B CD1 
2889 C CD2 . LEU   B 79  ? 0.3306 0.3212 0.2583 0.0226  0.0186  0.0328  101 LEU   B CD2 
2890 N N   . LEU   B 80  ? 0.2335 0.3188 0.2140 0.0420  0.0003  0.0360  102 LEU   B N   
2891 C CA  . LEU   B 80  ? 0.2491 0.3095 0.2097 0.0257  0.0133  0.0333  102 LEU   B CA  
2892 C C   . LEU   B 80  ? 0.2501 0.3024 0.1963 0.0256  0.0071  0.0253  102 LEU   B C   
2893 O O   . LEU   B 80  ? 0.2869 0.3026 0.1759 0.0544  -0.0065 0.0156  102 LEU   B O   
2894 C CB  . LEU   B 80  ? 0.2423 0.3219 0.2621 0.0349  0.0151  0.0373  102 LEU   B CB  
2895 C CG  . LEU   B 80  ? 0.2586 0.3616 0.3097 0.0301  0.0199  0.0372  102 LEU   B CG  
2896 C CD1 . LEU   B 80  ? 0.2680 0.3935 0.3441 0.0305  0.0011  0.0419  102 LEU   B CD1 
2897 C CD2 . LEU   B 80  ? 0.2690 0.3407 0.3422 0.0236  0.0030  0.0552  102 LEU   B CD2 
2898 N N   . VAL   B 81  ? 0.2405 0.2863 0.1743 0.0250  0.0068  0.0268  103 VAL   B N   
2899 C CA  . VAL   B 81  ? 0.2228 0.2837 0.1729 0.0187  0.0072  0.0241  103 VAL   B CA  
2900 C C   . VAL   B 81  ? 0.2289 0.2772 0.1725 0.0116  0.0066  0.0274  103 VAL   B C   
2901 O O   . VAL   B 81  ? 0.2466 0.2878 0.1839 0.0017  -0.0068 0.0396  103 VAL   B O   
2902 C CB  . VAL   B 81  ? 0.2276 0.2862 0.1826 0.0198  -0.0031 0.0188  103 VAL   B CB  
2903 C CG1 . VAL   B 81  ? 0.2068 0.2880 0.1662 0.0254  -0.0023 0.0028  103 VAL   B CG1 
2904 C CG2 . VAL   B 81  ? 0.2307 0.2849 0.1865 0.0147  -0.0009 0.0182  103 VAL   B CG2 
2905 N N   . SER   B 82  ? 0.2165 0.2836 0.1771 0.0118  -0.0079 0.0256  104 SER   B N   
2906 C CA  . SER   B 82  ? 0.2057 0.2651 0.1918 0.0057  -0.0134 0.0393  104 SER   B CA  
2907 C C   . SER   B 82  ? 0.1997 0.2685 0.1915 -0.0016 -0.0124 0.0321  104 SER   B C   
2908 O O   . SER   B 82  ? 0.2151 0.2704 0.1889 -0.0051 -0.0118 0.0436  104 SER   B O   
2909 C CB  . SER   B 82  ? 0.2073 0.2816 0.2033 0.0114  -0.0114 0.0292  104 SER   B CB  
2910 O OG  . SER   B 82  ? 0.2214 0.2824 0.2059 0.0358  -0.0309 0.0341  104 SER   B OG  
2911 N N   . ALA   B 83  ? 0.1932 0.2582 0.1974 -0.0114 -0.0037 0.0290  105 ALA   B N   
2912 C CA  . ALA   B 83  ? 0.2044 0.2468 0.2045 0.0000  -0.0065 0.0340  105 ALA   B CA  
2913 C C   . ALA   B 83  ? 0.1973 0.2297 0.1987 0.0020  -0.0059 0.0451  105 ALA   B C   
2914 O O   . ALA   B 83  ? 0.1798 0.2428 0.1836 -0.0037 -0.0156 0.0673  105 ALA   B O   
2915 C CB  . ALA   B 83  ? 0.2092 0.2444 0.2054 0.0065  -0.0030 0.0333  105 ALA   B CB  
2916 N N   . SER   B 84  ? 0.1964 0.2224 0.2032 0.0070  -0.0064 0.0449  106 SER   B N   
2917 C CA  . SER   B 84  ? 0.2215 0.2404 0.2016 0.0134  -0.0122 0.0482  106 SER   B CA  
2918 C C   . SER   B 84  ? 0.2380 0.2632 0.2131 0.0146  -0.0142 0.0565  106 SER   B C   
2919 O O   . SER   B 84  ? 0.2249 0.2763 0.2015 0.0301  -0.0062 0.0678  106 SER   B O   
2920 C CB  . SER   B 84  ? 0.2341 0.2455 0.2109 0.0290  -0.0229 0.0509  106 SER   B CB  
2921 O OG  . SER   B 84  ? 0.2585 0.2357 0.2257 0.0416  -0.0175 0.0611  106 SER   B OG  
2922 N N   . ASP   B 85  ? 0.2524 0.3013 0.2153 0.0007  -0.0187 0.0570  107 ASP   B N   
2923 C CA  . ASP   B 85  ? 0.2641 0.2939 0.2103 -0.0025 -0.0231 0.0525  107 ASP   B CA  
2924 C C   . ASP   B 85  ? 0.2708 0.2935 0.2134 0.0020  -0.0291 0.0495  107 ASP   B C   
2925 O O   . ASP   B 85  ? 0.2796 0.2816 0.2052 0.0105  -0.0237 0.0396  107 ASP   B O   
2926 C CB  . ASP   B 85  ? 0.2554 0.2973 0.2163 -0.0081 -0.0184 0.0535  107 ASP   B CB  
2927 C CG  . ASP   B 85  ? 0.2277 0.3049 0.2171 -0.0157 -0.0212 0.0471  107 ASP   B CG  
2928 O OD1 . ASP   B 85  ? 0.2170 0.3226 0.2176 -0.0196 -0.0308 0.0481  107 ASP   B OD1 
2929 O OD2 . ASP   B 85  ? 0.2071 0.3368 0.2532 0.0016  -0.0279 0.0116  107 ASP   B OD2 
2930 N N   . ASP   B 86  ? 0.2600 0.2727 0.2178 0.0116  -0.0236 0.0497  108 ASP   B N   
2931 C CA  . ASP   B 86  ? 0.2835 0.2799 0.2309 0.0210  -0.0227 0.0441  108 ASP   B CA  
2932 C C   . ASP   B 86  ? 0.2857 0.2486 0.2415 0.0128  -0.0279 0.0517  108 ASP   B C   
2933 O O   . ASP   B 86  ? 0.2631 0.2227 0.2520 0.0265  -0.0222 0.0222  108 ASP   B O   
2934 C CB  . ASP   B 86  ? 0.2974 0.2970 0.2345 0.0422  -0.0131 0.0513  108 ASP   B CB  
2935 C CG  . ASP   B 86  ? 0.3035 0.3070 0.2204 0.0570  -0.0011 0.0424  108 ASP   B CG  
2936 O OD1 . ASP   B 86  ? 0.3062 0.3024 0.2120 0.0705  -0.0135 0.0766  108 ASP   B OD1 
2937 O OD2 . ASP   B 86  ? 0.2897 0.3146 0.2335 0.0657  0.0359  0.0506  108 ASP   B OD2 
2938 N N   . LYS   B 87  ? 0.2966 0.2327 0.2346 0.0065  -0.0315 0.0659  109 LYS   B N   
2939 C CA  . LYS   B 87  ? 0.3084 0.2536 0.2377 -0.0097 -0.0350 0.0818  109 LYS   B CA  
2940 C C   . LYS   B 87  ? 0.2962 0.2453 0.2443 -0.0052 -0.0341 0.0660  109 LYS   B C   
2941 O O   . LYS   B 87  ? 0.2955 0.2594 0.2419 -0.0070 -0.0401 0.0686  109 LYS   B O   
2942 C CB  . LYS   B 87  ? 0.3395 0.2710 0.2745 -0.0098 -0.0323 0.1020  109 LYS   B CB  
2943 C CG  . LYS   B 87  ? 0.3437 0.3015 0.2849 -0.0049 -0.0469 0.1498  109 LYS   B CG  
2944 C CD  . LYS   B 87  ? 0.3817 0.3703 0.3362 -0.0368 -0.0243 0.1717  109 LYS   B CD  
2945 C CE  . LYS   B 87  ? 0.4218 0.4594 0.3698 -0.0441 -0.0137 0.1643  109 LYS   B CE  
2946 N NZ  . LYS   B 87  ? 0.4568 0.5088 0.4450 -0.0492 0.0227  0.1688  109 LYS   B NZ  
2947 N N   . THR   B 88  ? 0.2868 0.2191 0.2398 -0.0036 -0.0331 0.0587  110 THR   B N   
2948 C CA  . THR   B 88  ? 0.2803 0.2359 0.2500 -0.0052 -0.0489 0.0454  110 THR   B CA  
2949 C C   . THR   B 88  ? 0.2575 0.2396 0.2371 0.0023  -0.0412 0.0406  110 THR   B C   
2950 O O   . THR   B 88  ? 0.2385 0.2563 0.2474 -0.0116 -0.0143 0.0511  110 THR   B O   
2951 C CB  . THR   B 88  ? 0.3072 0.2560 0.2631 0.0003  -0.0636 0.0317  110 THR   B CB  
2952 O OG1 . THR   B 88  ? 0.2896 0.2512 0.2596 0.0117  -0.0578 0.0452  110 THR   B OG1 
2953 C CG2 . THR   B 88  ? 0.3319 0.2484 0.2865 0.0056  -0.0695 0.0285  110 THR   B CG2 
2954 N N   . LEU   B 89  ? 0.2384 0.2279 0.2308 0.0183  -0.0394 0.0541  111 LEU   B N   
2955 C CA  . LEU   B 89  ? 0.2353 0.2373 0.2256 0.0184  -0.0331 0.0468  111 LEU   B CA  
2956 C C   . LEU   B 89  ? 0.2620 0.2552 0.2410 0.0244  -0.0403 0.0422  111 LEU   B C   
2957 O O   . LEU   B 89  ? 0.2804 0.2417 0.2752 0.0294  -0.0525 0.0679  111 LEU   B O   
2958 C CB  . LEU   B 89  ? 0.2239 0.2507 0.2199 0.0181  -0.0227 0.0455  111 LEU   B CB  
2959 C CG  . LEU   B 89  ? 0.2123 0.2542 0.2264 0.0208  -0.0116 0.0479  111 LEU   B CG  
2960 C CD1 . LEU   B 89  ? 0.2152 0.2838 0.2297 0.0100  -0.0202 0.0495  111 LEU   B CD1 
2961 C CD2 . LEU   B 89  ? 0.2112 0.2558 0.2165 0.0169  -0.0013 0.0561  111 LEU   B CD2 
2962 N N   . LYS   B 90  ? 0.2806 0.2433 0.2055 0.0242  -0.0383 0.0362  112 LYS   B N   
2963 C CA  . LYS   B 90  ? 0.3100 0.2513 0.2129 0.0493  -0.0203 0.0295  112 LYS   B CA  
2964 C C   . LYS   B 90  ? 0.3129 0.2427 0.2127 0.0600  -0.0238 0.0213  112 LYS   B C   
2965 O O   . LYS   B 90  ? 0.2980 0.2470 0.1974 0.0476  -0.0016 0.0177  112 LYS   B O   
2966 C CB  . LYS   B 90  ? 0.3182 0.2742 0.2187 0.0602  -0.0138 0.0194  112 LYS   B CB  
2967 C CG  . LYS   B 90  ? 0.3308 0.2757 0.2245 0.0657  -0.0134 0.0241  112 LYS   B CG  
2968 C CD  . LYS   B 90  ? 0.3439 0.2857 0.2582 0.0701  -0.0110 0.0231  112 LYS   B CD  
2969 C CE  . LYS   B 90  ? 0.3788 0.2805 0.2873 0.0732  -0.0077 0.0210  112 LYS   B CE  
2970 N NZ  . LYS   B 90  ? 0.3873 0.2942 0.3400 0.0772  0.0002  0.0141  112 LYS   B NZ  
2971 N N   . ILE   B 91  ? 0.3272 0.2418 0.2047 0.0681  -0.0268 0.0120  113 ILE   B N   
2972 C CA  . ILE   B 91  ? 0.3374 0.2549 0.2184 0.0607  -0.0411 0.0193  113 ILE   B CA  
2973 C C   . ILE   B 91  ? 0.3457 0.2710 0.2264 0.0750  -0.0316 -0.0009 113 ILE   B C   
2974 O O   . ILE   B 91  ? 0.3629 0.2785 0.2544 0.0881  -0.0454 0.0091  113 ILE   B O   
2975 C CB  . ILE   B 91  ? 0.3612 0.2540 0.2366 0.0457  -0.0520 0.0230  113 ILE   B CB  
2976 C CG1 . ILE   B 91  ? 0.3628 0.2487 0.2663 0.0374  -0.0546 0.0331  113 ILE   B CG1 
2977 C CG2 . ILE   B 91  ? 0.3516 0.2544 0.2162 0.0572  -0.0781 0.0135  113 ILE   B CG2 
2978 C CD1 . ILE   B 91  ? 0.3640 0.2331 0.2596 0.0335  -0.0685 0.0567  113 ILE   B CD1 
2979 N N   . TRP   B 92  ? 0.3463 0.2860 0.2162 0.0878  -0.0120 0.0086  114 TRP   B N   
2980 C CA  . TRP   B 92  ? 0.3291 0.3165 0.2202 0.0794  -0.0177 0.0080  114 TRP   B CA  
2981 C C   . TRP   B 92  ? 0.3368 0.3356 0.2294 0.0859  -0.0188 0.0037  114 TRP   B C   
2982 O O   . TRP   B 92  ? 0.3120 0.3045 0.2381 0.0790  -0.0106 -0.0233 114 TRP   B O   
2983 C CB  . TRP   B 92  ? 0.3432 0.3148 0.2061 0.0690  -0.0145 0.0038  114 TRP   B CB  
2984 C CG  . TRP   B 92  ? 0.3464 0.3203 0.2132 0.0616  -0.0206 0.0189  114 TRP   B CG  
2985 C CD1 . TRP   B 92  ? 0.3244 0.3119 0.2190 0.0692  -0.0225 0.0199  114 TRP   B CD1 
2986 C CD2 . TRP   B 92  ? 0.3403 0.3315 0.2235 0.0821  -0.0217 0.0067  114 TRP   B CD2 
2987 N NE1 . TRP   B 92  ? 0.3166 0.3028 0.1947 0.0462  -0.0166 0.0177  114 TRP   B NE1 
2988 C CE2 . TRP   B 92  ? 0.3455 0.3169 0.2233 0.0689  -0.0206 0.0223  114 TRP   B CE2 
2989 C CE3 . TRP   B 92  ? 0.3691 0.3352 0.2479 0.0888  -0.0310 0.0142  114 TRP   B CE3 
2990 C CZ2 . TRP   B 92  ? 0.3562 0.3446 0.2198 0.0968  -0.0350 0.0087  114 TRP   B CZ2 
2991 C CZ3 . TRP   B 92  ? 0.3678 0.3497 0.2389 0.1054  -0.0256 0.0135  114 TRP   B CZ3 
2992 C CH2 . TRP   B 92  ? 0.3777 0.3647 0.2409 0.1069  -0.0301 0.0050  114 TRP   B CH2 
2993 N N   . ASP   B 93  ? 0.3194 0.3824 0.2312 0.1049  -0.0079 0.0084  115 ASP   B N   
2994 C CA  . ASP   B 93  ? 0.3396 0.4524 0.2474 0.0982  0.0177  0.0004  115 ASP   B CA  
2995 C C   . ASP   B 93  ? 0.2978 0.4733 0.2377 0.1170  0.0275  0.0177  115 ASP   B C   
2996 O O   . ASP   B 93  ? 0.3453 0.4807 0.2417 0.1502  0.0062  0.0581  115 ASP   B O   
2997 C CB  . ASP   B 93  ? 0.3718 0.4859 0.2701 0.1007  0.0299  -0.0107 115 ASP   B CB  
2998 C CG  . ASP   B 93  ? 0.4161 0.5698 0.2706 0.0853  0.0440  -0.0142 115 ASP   B CG  
2999 O OD1 . ASP   B 93  ? 0.4035 0.5856 0.2935 0.0869  0.0439  -0.0111 115 ASP   B OD1 
3000 O OD2 . ASP   B 93  ? 0.4859 0.6543 0.3148 0.0668  0.0345  -0.0234 115 ASP   B OD2 
3001 N N   . VAL   B 94  ? 0.2850 0.4625 0.2179 0.1266  0.0200  -0.0013 116 VAL   B N   
3002 C CA  . VAL   B 94  ? 0.3019 0.4930 0.2658 0.1140  0.0408  0.0010  116 VAL   B CA  
3003 C C   . VAL   B 94  ? 0.3148 0.5140 0.2590 0.1318  0.0308  -0.0063 116 VAL   B C   
3004 O O   . VAL   B 94  ? 0.3320 0.5572 0.2530 0.1138  0.0272  0.0201  116 VAL   B O   
3005 C CB  . VAL   B 94  ? 0.2986 0.5003 0.3512 0.0998  0.0576  -0.0066 116 VAL   B CB  
3006 C CG1 . VAL   B 94  ? 0.3476 0.5240 0.4192 0.0980  0.0573  0.0035  116 VAL   B CG1 
3007 C CG2 . VAL   B 94  ? 0.2836 0.4923 0.3441 0.0939  0.0545  -0.0044 116 VAL   B CG2 
3008 N N   . SER   B 95  ? 0.3452 0.5323 0.2675 0.1700  0.0224  -0.0326 117 SER   B N   
3009 C CA  . SER   B 95  ? 0.3588 0.5555 0.2843 0.1562  0.0377  -0.0214 117 SER   B CA  
3010 C C   . SER   B 95  ? 0.3584 0.5578 0.2880 0.1719  0.0524  -0.0370 117 SER   B C   
3011 O O   . SER   B 95  ? 0.3364 0.6209 0.3566 0.1788  0.0761  -0.0483 117 SER   B O   
3012 C CB  . SER   B 95  ? 0.4202 0.6065 0.3404 0.1287  -0.0033 -0.0349 117 SER   B CB  
3013 O OG  . SER   B 95  ? 0.4794 0.6764 0.4194 0.1013  -0.0320 -0.0288 117 SER   B OG  
3014 N N   . SER   B 96  ? 0.4026 0.4704 0.3084 0.1967  0.0259  -0.0282 118 SER   B N   
3015 C CA  . SER   B 96  ? 0.4207 0.4683 0.3197 0.2189  0.0227  -0.0268 118 SER   B CA  
3016 C C   . SER   B 96  ? 0.4052 0.4479 0.3326 0.2529  0.0110  0.0008  118 SER   B C   
3017 O O   . SER   B 96  ? 0.3951 0.4484 0.3394 0.2657  0.0204  0.0169  118 SER   B O   
3018 C CB  . SER   B 96  ? 0.4314 0.4399 0.3120 0.2102  0.0398  -0.0272 118 SER   B CB  
3019 O OG  . SER   B 96  ? 0.4533 0.4336 0.3129 0.2033  0.0637  -0.0292 118 SER   B OG  
3020 N N   . GLY   B 97  ? 0.4285 0.4844 0.3006 0.2618  0.0039  -0.0032 119 GLY   B N   
3021 C CA  . GLY   B 97  ? 0.4168 0.4723 0.3037 0.2653  0.0019  0.0297  119 GLY   B CA  
3022 C C   . GLY   B 97  ? 0.4448 0.4722 0.2977 0.2420  -0.0098 0.0315  119 GLY   B C   
3023 O O   . GLY   B 97  ? 0.5129 0.5335 0.2764 0.2267  0.0478  0.0199  119 GLY   B O   
3024 N N   . LYS   B 98  ? 0.4468 0.4561 0.3006 0.2097  -0.0165 0.0275  120 LYS   B N   
3025 C CA  . LYS   B 98  ? 0.4663 0.4233 0.3066 0.1907  -0.0416 0.0215  120 LYS   B CA  
3026 C C   . LYS   B 98  ? 0.4611 0.3914 0.2772 0.1622  -0.0337 0.0051  120 LYS   B C   
3027 O O   . LYS   B 98  ? 0.4190 0.4186 0.2831 0.1536  -0.0374 -0.0158 120 LYS   B O   
3028 C CB  . LYS   B 98  ? 0.4799 0.4644 0.3104 0.1806  -0.0860 0.0205  120 LYS   B CB  
3029 N N   . CYS   B 99  ? 0.4715 0.3945 0.2808 0.1414  -0.0420 -0.0122 121 CYS   B N   
3030 C CA  . CYS   B 99  ? 0.4912 0.3721 0.2723 0.1238  -0.0423 0.0019  121 CYS   B CA  
3031 C C   . CYS   B 99  ? 0.4823 0.3428 0.2709 0.1219  -0.0572 -0.0006 121 CYS   B C   
3032 O O   . CYS   B 99  ? 0.4998 0.3528 0.2814 0.1220  -0.0619 -0.0099 121 CYS   B O   
3033 C CB  . CYS   B 99  ? 0.4952 0.3713 0.2810 0.1303  -0.0385 0.0210  121 CYS   B CB  
3034 S SG  . CYS   B 99  ? 0.5354 0.3862 0.2577 0.1347  -0.0122 0.0110  121 CYS   B SG  
3035 N N   . LEU   B 100 ? 0.4718 0.3376 0.3118 0.1108  -0.0615 -0.0173 122 LEU   B N   
3036 C CA  . LEU   B 100 ? 0.4925 0.3260 0.3152 0.1061  -0.0606 -0.0059 122 LEU   B CA  
3037 C C   . LEU   B 100 ? 0.4882 0.3117 0.3334 0.0742  -0.0584 -0.0219 122 LEU   B C   
3038 O O   . LEU   B 100 ? 0.5480 0.2819 0.3248 0.0804  -0.0704 -0.0337 122 LEU   B O   
3039 C CB  . LEU   B 100 ? 0.4716 0.3501 0.3007 0.1025  -0.0648 0.0104  122 LEU   B CB  
3040 C CG  . LEU   B 100 ? 0.4812 0.3847 0.3131 0.1096  -0.0511 0.0198  122 LEU   B CG  
3041 C CD1 . LEU   B 100 ? 0.4647 0.3845 0.3302 0.1116  -0.0473 0.0238  122 LEU   B CD1 
3042 C CD2 . LEU   B 100 ? 0.5004 0.4189 0.3190 0.1080  -0.0528 0.0109  122 LEU   B CD2 
3043 N N   . LYS   B 101 ? 0.4796 0.3245 0.3154 0.0641  -0.0666 -0.0185 123 LYS   B N   
3044 C CA  . LYS   B 101 ? 0.5148 0.3251 0.3216 0.0494  -0.0653 -0.0150 123 LYS   B CA  
3045 C C   . LYS   B 101 ? 0.4555 0.2990 0.3046 0.0604  -0.0657 0.0046  123 LYS   B C   
3046 O O   . LYS   B 101 ? 0.4240 0.2778 0.2639 0.0880  -0.0615 -0.0259 123 LYS   B O   
3047 C CB  . LYS   B 101 ? 0.5257 0.3444 0.3326 0.0359  -0.0596 -0.0260 123 LYS   B CB  
3048 C CG  . LYS   B 101 ? 0.5560 0.3995 0.3733 0.0135  -0.0762 -0.0203 123 LYS   B CG  
3049 C CD  . LYS   B 101 ? 0.6020 0.4343 0.3744 -0.0117 -0.0648 -0.0357 123 LYS   B CD  
3050 C CE  . LYS   B 101 ? 0.6182 0.4697 0.3672 -0.0029 -0.0578 -0.0416 123 LYS   B CE  
3051 N NZ  . LYS   B 101 ? 0.6401 0.4946 0.3881 -0.0205 -0.0588 -0.0589 123 LYS   B NZ  
3052 N N   . THR   B 102 ? 0.4277 0.2913 0.3182 0.0450  -0.0679 0.0127  124 THR   B N   
3053 C CA  . THR   B 102 ? 0.4035 0.2466 0.2976 0.0413  -0.0514 0.0273  124 THR   B CA  
3054 C C   . THR   B 102 ? 0.3991 0.2320 0.3040 -0.0010 -0.0647 0.0427  124 THR   B C   
3055 O O   . THR   B 102 ? 0.4449 0.2046 0.3729 -0.0046 -0.0807 0.0560  124 THR   B O   
3056 C CB  . THR   B 102 ? 0.3914 0.2821 0.2901 0.0472  -0.0361 0.0383  124 THR   B CB  
3057 O OG1 . THR   B 102 ? 0.3629 0.2475 0.3116 0.0684  -0.0273 0.0381  124 THR   B OG1 
3058 C CG2 . THR   B 102 ? 0.3916 0.2904 0.2849 0.0410  -0.0460 0.0430  124 THR   B CG2 
3059 N N   . LEU   B 103 ? 0.3660 0.2317 0.2611 -0.0038 -0.0779 0.0521  125 LEU   B N   
3060 C CA  . LEU   B 103 ? 0.3558 0.2565 0.2625 -0.0169 -0.0825 0.0431  125 LEU   B CA  
3061 C C   . LEU   B 103 ? 0.3674 0.2454 0.2762 -0.0238 -0.0813 0.0577  125 LEU   B C   
3062 O O   . LEU   B 103 ? 0.3440 0.2721 0.2794 -0.0386 -0.0916 0.0669  125 LEU   B O   
3063 C CB  . LEU   B 103 ? 0.3596 0.2756 0.2800 -0.0108 -0.0812 0.0491  125 LEU   B CB  
3064 C CG  . LEU   B 103 ? 0.3753 0.3172 0.2916 -0.0066 -0.0903 0.0589  125 LEU   B CG  
3065 C CD1 . LEU   B 103 ? 0.3498 0.3433 0.2601 0.0119  -0.0979 0.0608  125 LEU   B CD1 
3066 C CD2 . LEU   B 103 ? 0.3945 0.3541 0.3167 -0.0159 -0.0966 0.0550  125 LEU   B CD2 
3067 N N   . LYS   B 104 ? 0.3822 0.2668 0.3013 -0.0413 -0.0679 0.0524  126 LYS   B N   
3068 C CA  . LYS   B 104 ? 0.3922 0.2756 0.3229 -0.0433 -0.0804 0.0753  126 LYS   B CA  
3069 C C   . LYS   B 104 ? 0.3780 0.2749 0.3195 -0.0787 -0.0653 0.0959  126 LYS   B C   
3070 O O   . LYS   B 104 ? 0.3667 0.2747 0.3552 -0.0970 -0.0526 0.1180  126 LYS   B O   
3071 C CB  . LYS   B 104 ? 0.4549 0.3027 0.3829 -0.0225 -0.0766 0.0688  126 LYS   B CB  
3072 C CG  . LYS   B 104 ? 0.5100 0.3514 0.4443 -0.0106 -0.0404 0.0626  126 LYS   B CG  
3073 C CD  . LYS   B 104 ? 0.5873 0.3666 0.5309 0.0011  -0.0339 0.0682  126 LYS   B CD  
3074 C CE  . LYS   B 104 ? 0.6180 0.4448 0.5672 -0.0132 -0.0247 0.0430  126 LYS   B CE  
3075 N NZ  . LYS   B 104 ? 0.6477 0.4955 0.6162 -0.0279 -0.0375 0.0323  126 LYS   B NZ  
3076 N N   . GLY   B 105 ? 0.3315 0.2856 0.3266 -0.0760 -0.0761 0.0902  127 GLY   B N   
3077 C CA  . GLY   B 105 ? 0.3099 0.2913 0.3336 -0.0722 -0.0762 0.0880  127 GLY   B CA  
3078 C C   . GLY   B 105 ? 0.2904 0.2851 0.3069 -0.0833 -0.0643 0.1028  127 GLY   B C   
3079 O O   . GLY   B 105 ? 0.3034 0.3039 0.3407 -0.1061 -0.0579 0.1205  127 GLY   B O   
3080 N N   . HIS   B 106 ? 0.2908 0.2571 0.2840 -0.0635 -0.0603 0.0994  128 HIS   B N   
3081 C CA  . HIS   B 106 ? 0.2805 0.2431 0.2763 -0.0596 -0.0422 0.0949  128 HIS   B CA  
3082 C C   . HIS   B 106 ? 0.2957 0.2583 0.2846 -0.0548 -0.0447 0.1043  128 HIS   B C   
3083 O O   . HIS   B 106 ? 0.3158 0.2168 0.3330 -0.0721 -0.0532 0.1188  128 HIS   B O   
3084 C CB  . HIS   B 106 ? 0.2670 0.2519 0.2532 -0.0540 -0.0248 0.0888  128 HIS   B CB  
3085 C CG  . HIS   B 106 ? 0.2452 0.2579 0.2389 -0.0368 -0.0216 0.0851  128 HIS   B CG  
3086 N ND1 . HIS   B 106 ? 0.2223 0.2808 0.2232 -0.0211 -0.0209 0.1015  128 HIS   B ND1 
3087 C CD2 . HIS   B 106 ? 0.2326 0.2731 0.2495 -0.0278 -0.0191 0.0951  128 HIS   B CD2 
3088 C CE1 . HIS   B 106 ? 0.2311 0.2687 0.2577 -0.0209 -0.0044 0.1003  128 HIS   B CE1 
3089 N NE2 . HIS   B 106 ? 0.2433 0.2544 0.2419 -0.0367 -0.0189 0.0979  128 HIS   B NE2 
3090 N N   . SER   B 107 ? 0.2980 0.2688 0.2944 -0.0568 -0.0254 0.1196  129 SER   B N   
3091 C CA  . SER   B 107 ? 0.2896 0.2976 0.2885 -0.0515 -0.0240 0.1271  129 SER   B CA  
3092 C C   . SER   B 107 ? 0.2811 0.2890 0.2814 -0.0630 -0.0152 0.1311  129 SER   B C   
3093 O O   . SER   B 107 ? 0.2813 0.3234 0.2809 -0.0571 -0.0494 0.1194  129 SER   B O   
3094 C CB  . SER   B 107 ? 0.2966 0.2974 0.3107 -0.0513 -0.0014 0.1331  129 SER   B CB  
3095 O OG  . SER   B 107 ? 0.2566 0.3158 0.2891 -0.0275 0.0089  0.1379  129 SER   B OG  
3096 N N   . ASN   B 108 ? 0.2805 0.2606 0.2692 -0.0392 -0.0193 0.1142  130 ASN   B N   
3097 C CA  . ASN   B 108 ? 0.2570 0.2748 0.2435 -0.0494 -0.0032 0.1088  130 ASN   B CA  
3098 C C   . ASN   B 108 ? 0.2214 0.2679 0.2269 -0.0348 -0.0015 0.0900  130 ASN   B C   
3099 O O   . ASN   B 108 ? 0.2331 0.2709 0.2365 -0.0360 -0.0092 0.0857  130 ASN   B O   
3100 C CB  . ASN   B 108 ? 0.2532 0.3077 0.2290 -0.0622 -0.0047 0.1004  130 ASN   B CB  
3101 C CG  . ASN   B 108 ? 0.2704 0.3994 0.2338 -0.0481 -0.0151 0.0987  130 ASN   B CG  
3102 O OD1 . ASN   B 108 ? 0.2599 0.4096 0.2563 -0.0428 -0.0467 0.1078  130 ASN   B OD1 
3103 N ND2 . ASN   B 108 ? 0.2771 0.4646 0.2446 -0.0583 -0.0294 0.0726  130 ASN   B ND2 
3104 N N   . TYR   B 109 ? 0.2126 0.2611 0.1993 -0.0233 0.0013  0.0673  131 TYR   B N   
3105 C CA  . TYR   B 109 ? 0.2019 0.2664 0.1983 -0.0286 -0.0010 0.0648  131 TYR   B CA  
3106 C C   . TYR   B 109 ? 0.1653 0.2522 0.2051 -0.0374 0.0010  0.0550  131 TYR   B C   
3107 O O   . TYR   B 109 ? 0.1590 0.2448 0.2266 -0.0330 0.0083  0.0495  131 TYR   B O   
3108 C CB  . TYR   B 109 ? 0.2033 0.3099 0.1836 -0.0353 -0.0085 0.0548  131 TYR   B CB  
3109 C CG  . TYR   B 109 ? 0.2191 0.3439 0.2143 -0.0169 -0.0245 0.0547  131 TYR   B CG  
3110 C CD1 . TYR   B 109 ? 0.2034 0.3565 0.1854 -0.0160 -0.0067 0.0593  131 TYR   B CD1 
3111 C CD2 . TYR   B 109 ? 0.2834 0.3814 0.2604 -0.0161 -0.0501 0.0534  131 TYR   B CD2 
3112 C CE1 . TYR   B 109 ? 0.2336 0.4016 0.2120 0.0124  -0.0115 0.0616  131 TYR   B CE1 
3113 C CE2 . TYR   B 109 ? 0.2807 0.4264 0.2912 -0.0063 -0.0634 0.0542  131 TYR   B CE2 
3114 C CZ  . TYR   B 109 ? 0.2534 0.4145 0.2626 0.0011  -0.0385 0.0531  131 TYR   B CZ  
3115 O OH  . TYR   B 109 ? 0.3171 0.5372 0.2578 0.0345  -0.0524 0.0381  131 TYR   B OH  
3116 N N   . VAL   B 110 ? 0.1706 0.2491 0.1963 -0.0284 -0.0027 0.0534  132 VAL   B N   
3117 C CA  . VAL   B 110 ? 0.1738 0.2450 0.1937 -0.0299 -0.0012 0.0606  132 VAL   B CA  
3118 C C   . VAL   B 110 ? 0.1732 0.2435 0.1803 -0.0217 -0.0002 0.0565  132 VAL   B C   
3119 O O   . VAL   B 110 ? 0.1818 0.2335 0.1993 -0.0090 0.0067  0.0352  132 VAL   B O   
3120 C CB  . VAL   B 110 ? 0.1800 0.2539 0.1835 -0.0395 -0.0072 0.0768  132 VAL   B CB  
3121 C CG1 . VAL   B 110 ? 0.1908 0.2529 0.1925 -0.0408 -0.0106 0.0768  132 VAL   B CG1 
3122 C CG2 . VAL   B 110 ? 0.1932 0.2622 0.1848 -0.0433 -0.0071 0.0835  132 VAL   B CG2 
3123 N N   . PHE   B 111 ? 0.1755 0.2596 0.1883 -0.0218 -0.0009 0.0448  133 PHE   B N   
3124 C CA  . PHE   B 111 ? 0.1616 0.2575 0.1843 -0.0245 0.0045  0.0457  133 PHE   B CA  
3125 C C   . PHE   B 111 ? 0.1589 0.2579 0.1750 -0.0326 0.0090  0.0409  133 PHE   B C   
3126 O O   . PHE   B 111 ? 0.1745 0.2823 0.1824 -0.0552 0.0050  0.0463  133 PHE   B O   
3127 C CB  . PHE   B 111 ? 0.1792 0.2927 0.1849 -0.0173 0.0067  0.0485  133 PHE   B CB  
3128 C CG  . PHE   B 111 ? 0.1887 0.3189 0.1988 -0.0086 0.0064  0.0278  133 PHE   B CG  
3129 C CD1 . PHE   B 111 ? 0.1955 0.3374 0.2207 0.0043  -0.0027 0.0308  133 PHE   B CD1 
3130 C CD2 . PHE   B 111 ? 0.1893 0.3393 0.2478 0.0034  0.0071  0.0110  133 PHE   B CD2 
3131 C CE1 . PHE   B 111 ? 0.2045 0.3254 0.2380 0.0000  0.0077  0.0365  133 PHE   B CE1 
3132 C CE2 . PHE   B 111 ? 0.1898 0.3425 0.2727 0.0008  0.0131  0.0109  133 PHE   B CE2 
3133 C CZ  . PHE   B 111 ? 0.2048 0.3429 0.2620 0.0071  0.0128  0.0184  133 PHE   B CZ  
3134 N N   . CYS   B 112 ? 0.1572 0.2305 0.1752 -0.0445 0.0144  0.0515  134 CYS   B N   
3135 C CA  . CYS   B 112 ? 0.1512 0.2404 0.1649 -0.0268 0.0099  0.0477  134 CYS   B CA  
3136 C C   . CYS   B 112 ? 0.1600 0.2328 0.1725 -0.0323 0.0166  0.0458  134 CYS   B C   
3137 O O   . CYS   B 112 ? 0.1398 0.2354 0.1764 -0.0257 0.0180  0.0610  134 CYS   B O   
3138 C CB  . CYS   B 112 ? 0.1610 0.2263 0.1529 -0.0274 0.0129  0.0567  134 CYS   B CB  
3139 S SG  . CYS   B 112 ? 0.1686 0.2471 0.1788 -0.0013 0.0335  0.0409  134 CYS   B SG  
3140 N N   . CYS   B 113 ? 0.1520 0.2167 0.1714 -0.0332 0.0318  0.0443  135 CYS   B N   
3141 C CA  . CYS   B 113 ? 0.1532 0.2066 0.1686 -0.0295 0.0294  0.0405  135 CYS   B CA  
3142 C C   . CYS   B 113 ? 0.1486 0.2232 0.1633 -0.0231 0.0308  0.0390  135 CYS   B C   
3143 O O   . CYS   B 113 ? 0.1646 0.2218 0.1686 -0.0253 0.0241  0.0490  135 CYS   B O   
3144 C CB  . CYS   B 113 ? 0.1811 0.2178 0.1621 -0.0204 0.0384  0.0322  135 CYS   B CB  
3145 S SG  . CYS   B 113 ? 0.1984 0.2312 0.1964 -0.0038 0.0254  0.0394  135 CYS   B SG  
3146 N N   . ASN   B 114 ? 0.1451 0.2287 0.1686 -0.0167 0.0237  0.0537  136 ASN   B N   
3147 C CA  . ASN   B 114 ? 0.1480 0.2353 0.1686 -0.0175 0.0230  0.0529  136 ASN   B CA  
3148 C C   . ASN   B 114 ? 0.1505 0.2344 0.1725 -0.0162 0.0208  0.0519  136 ASN   B C   
3149 O O   . ASN   B 114 ? 0.1773 0.2430 0.1671 -0.0333 0.0337  0.0619  136 ASN   B O   
3150 C CB  . ASN   B 114 ? 0.1583 0.2444 0.1806 -0.0198 0.0211  0.0500  136 ASN   B CB  
3151 C CG  . ASN   B 114 ? 0.1571 0.2567 0.2003 -0.0237 0.0349  0.0562  136 ASN   B CG  
3152 O OD1 . ASN   B 114 ? 0.1710 0.2549 0.2179 -0.0300 0.0548  0.0669  136 ASN   B OD1 
3153 N ND2 . ASN   B 114 ? 0.1443 0.2444 0.1917 -0.0265 0.0346  0.0502  136 ASN   B ND2 
3154 N N   . PHE   B 115 ? 0.1501 0.2383 0.1670 -0.0108 0.0222  0.0406  137 PHE   B N   
3155 C CA  . PHE   B 115 ? 0.1698 0.2199 0.1655 -0.0026 0.0157  0.0333  137 PHE   B CA  
3156 C C   . PHE   B 115 ? 0.1768 0.2142 0.1773 -0.0050 0.0128  0.0277  137 PHE   B C   
3157 O O   . PHE   B 115 ? 0.1907 0.2100 0.1620 -0.0058 0.0327  0.0184  137 PHE   B O   
3158 C CB  . PHE   B 115 ? 0.1752 0.2170 0.1601 -0.0055 0.0182  0.0332  137 PHE   B CB  
3159 C CG  . PHE   B 115 ? 0.1856 0.2270 0.1720 -0.0011 0.0083  0.0254  137 PHE   B CG  
3160 C CD1 . PHE   B 115 ? 0.1911 0.2320 0.1720 0.0028  0.0075  0.0170  137 PHE   B CD1 
3161 C CD2 . PHE   B 115 ? 0.1920 0.2332 0.2030 0.0007  0.0075  0.0186  137 PHE   B CD2 
3162 C CE1 . PHE   B 115 ? 0.2039 0.2347 0.1938 0.0053  -0.0004 0.0209  137 PHE   B CE1 
3163 C CE2 . PHE   B 115 ? 0.1855 0.2432 0.2139 0.0025  -0.0020 0.0122  137 PHE   B CE2 
3164 C CZ  . PHE   B 115 ? 0.2021 0.2393 0.1996 0.0089  -0.0002 0.0184  137 PHE   B CZ  
3165 N N   . ASN   B 116 ? 0.1798 0.2112 0.1918 -0.0117 0.0108  0.0371  138 ASN   B N   
3166 C CA  . ASN   B 116 ? 0.1799 0.2264 0.1812 -0.0121 0.0064  0.0404  138 ASN   B CA  
3167 C C   . ASN   B 116 ? 0.1903 0.2306 0.1804 -0.0097 0.0135  0.0353  138 ASN   B C   
3168 O O   . ASN   B 116 ? 0.1806 0.2275 0.1853 -0.0182 0.0262  0.0512  138 ASN   B O   
3169 C CB  . ASN   B 116 ? 0.1877 0.2349 0.1893 -0.0215 0.0060  0.0407  138 ASN   B CB  
3170 C CG  . ASN   B 116 ? 0.1848 0.2318 0.2098 -0.0324 -0.0063 0.0446  138 ASN   B CG  
3171 O OD1 . ASN   B 116 ? 0.1935 0.2356 0.1862 -0.0389 -0.0217 0.0472  138 ASN   B OD1 
3172 N ND2 . ASN   B 116 ? 0.1853 0.2471 0.2275 -0.0322 -0.0007 0.0436  138 ASN   B ND2 
3173 N N   . PRO   B 117 ? 0.2190 0.2461 0.1753 0.0066  0.0214  0.0311  139 PRO   B N   
3174 C CA  . PRO   B 117 ? 0.2134 0.2507 0.1839 -0.0004 0.0250  0.0324  139 PRO   B CA  
3175 C C   . PRO   B 117 ? 0.2116 0.2548 0.1982 -0.0085 0.0251  0.0264  139 PRO   B C   
3176 O O   . PRO   B 117 ? 0.1964 0.2718 0.1933 -0.0164 0.0254  0.0338  139 PRO   B O   
3177 C CB  . PRO   B 117 ? 0.2238 0.2467 0.1795 0.0003  0.0211  0.0261  139 PRO   B CB  
3178 C CG  . PRO   B 117 ? 0.2184 0.2444 0.1857 0.0051  0.0202  0.0263  139 PRO   B CG  
3179 C CD  . PRO   B 117 ? 0.2087 0.2472 0.1898 0.0063  0.0108  0.0283  139 PRO   B CD  
3180 N N   . GLN   B 118 ? 0.2153 0.2507 0.2059 -0.0052 0.0252  0.0264  140 GLN   B N   
3181 C CA  . GLN   B 118 ? 0.2181 0.2411 0.1957 0.0016  0.0194  0.0245  140 GLN   B CA  
3182 C C   . GLN   B 118 ? 0.2215 0.2488 0.1915 0.0100  0.0132  0.0175  140 GLN   B C   
3183 O O   . GLN   B 118 ? 0.2428 0.2279 0.2005 0.0234  -0.0113 0.0242  140 GLN   B O   
3184 C CB  . GLN   B 118 ? 0.2203 0.2523 0.2172 0.0025  0.0240  0.0201  140 GLN   B CB  
3185 C CG  . GLN   B 118 ? 0.2109 0.2690 0.2298 0.0024  0.0224  0.0363  140 GLN   B CG  
3186 C CD  . GLN   B 118 ? 0.2050 0.2867 0.2566 -0.0242 0.0216  0.0157  140 GLN   B CD  
3187 O OE1 . GLN   B 118 ? 0.1539 0.2827 0.2561 -0.0399 0.0079  0.0618  140 GLN   B OE1 
3188 N NE2 . GLN   B 118 ? 0.2080 0.3359 0.2891 -0.0469 0.0130  -0.0080 140 GLN   B NE2 
3189 N N   . SER   B 119 ? 0.2158 0.2434 0.1807 0.0139  0.0209  0.0180  141 SER   B N   
3190 C CA  . SER   B 119 ? 0.2182 0.2484 0.2003 0.0189  0.0253  0.0125  141 SER   B CA  
3191 C C   . SER   B 119 ? 0.2326 0.2516 0.2297 0.0105  0.0076  0.0137  141 SER   B C   
3192 O O   . SER   B 119 ? 0.2673 0.2370 0.2712 0.0135  0.0064  0.0111  141 SER   B O   
3193 C CB  . SER   B 119 ? 0.2111 0.2510 0.2062 0.0258  0.0290  0.0025  141 SER   B CB  
3194 O OG  . SER   B 119 ? 0.1937 0.2456 0.2050 0.0439  0.0354  -0.0003 141 SER   B OG  
3195 N N   . ASN   B 120 ? 0.2373 0.2472 0.2211 -0.0074 -0.0246 0.0355  142 ASN   B N   
3196 C CA  . ASN   B 120 ? 0.2560 0.2616 0.2268 -0.0189 -0.0306 0.0545  142 ASN   B CA  
3197 C C   . ASN   B 120 ? 0.2401 0.2627 0.2294 -0.0331 -0.0266 0.0617  142 ASN   B C   
3198 O O   . ASN   B 120 ? 0.2409 0.2656 0.2577 -0.0488 -0.0515 0.0723  142 ASN   B O   
3199 C CB  . ASN   B 120 ? 0.2661 0.2788 0.2313 -0.0349 -0.0295 0.0440  142 ASN   B CB  
3200 C CG  . ASN   B 120 ? 0.2623 0.2821 0.2035 -0.0386 -0.0256 0.0529  142 ASN   B CG  
3201 O OD1 . ASN   B 120 ? 0.2659 0.2838 0.1686 -0.0363 -0.0303 0.0489  142 ASN   B OD1 
3202 N ND2 . ASN   B 120 ? 0.2705 0.3142 0.2432 -0.0513 -0.0308 0.0489  142 ASN   B ND2 
3203 N N   . LEU   B 121 ? 0.2177 0.2435 0.2046 -0.0293 -0.0226 0.0682  143 LEU   B N   
3204 C CA  . LEU   B 121 ? 0.2042 0.2479 0.1968 -0.0335 -0.0195 0.0669  143 LEU   B CA  
3205 C C   . LEU   B 121 ? 0.2089 0.2294 0.1858 -0.0273 -0.0117 0.0492  143 LEU   B C   
3206 O O   . LEU   B 121 ? 0.1965 0.2385 0.1694 -0.0402 -0.0142 0.0518  143 LEU   B O   
3207 C CB  . LEU   B 121 ? 0.2263 0.2563 0.1988 -0.0303 -0.0228 0.0670  143 LEU   B CB  
3208 C CG  . LEU   B 121 ? 0.2315 0.2688 0.2254 -0.0471 -0.0242 0.0694  143 LEU   B CG  
3209 C CD1 . LEU   B 121 ? 0.2305 0.2760 0.2087 -0.0592 -0.0241 0.0736  143 LEU   B CD1 
3210 C CD2 . LEU   B 121 ? 0.2410 0.2765 0.2283 -0.0480 -0.0362 0.0668  143 LEU   B CD2 
3211 N N   . ILE   B 122 ? 0.1903 0.2166 0.2025 -0.0184 -0.0273 0.0529  144 ILE   B N   
3212 C CA  . ILE   B 122 ? 0.1820 0.2340 0.2026 -0.0143 -0.0222 0.0467  144 ILE   B CA  
3213 C C   . ILE   B 122 ? 0.1689 0.2337 0.2068 -0.0258 -0.0198 0.0500  144 ILE   B C   
3214 O O   . ILE   B 122 ? 0.1890 0.2288 0.2220 -0.0298 -0.0136 0.0596  144 ILE   B O   
3215 C CB  . ILE   B 122 ? 0.2024 0.2395 0.2208 -0.0003 -0.0311 0.0351  144 ILE   B CB  
3216 C CG1 . ILE   B 122 ? 0.1998 0.2477 0.2241 0.0079  -0.0253 0.0202  144 ILE   B CG1 
3217 C CG2 . ILE   B 122 ? 0.2118 0.2446 0.2287 0.0132  -0.0463 0.0309  144 ILE   B CG2 
3218 C CD1 . ILE   B 122 ? 0.2150 0.2593 0.2422 0.0206  -0.0247 0.0212  144 ILE   B CD1 
3219 N N   . VAL   B 123 ? 0.1597 0.2367 0.1856 -0.0208 -0.0052 0.0510  145 VAL   B N   
3220 C CA  . VAL   B 123 ? 0.1460 0.2493 0.1975 -0.0341 -0.0003 0.0442  145 VAL   B CA  
3221 C C   . VAL   B 123 ? 0.1492 0.2391 0.1918 -0.0253 0.0030  0.0567  145 VAL   B C   
3222 O O   . VAL   B 123 ? 0.1464 0.2183 0.1731 -0.0188 0.0213  0.0423  145 VAL   B O   
3223 C CB  . VAL   B 123 ? 0.1478 0.2508 0.1748 -0.0250 0.0031  0.0372  145 VAL   B CB  
3224 C CG1 . VAL   B 123 ? 0.1646 0.2408 0.1632 -0.0201 0.0001  0.0307  145 VAL   B CG1 
3225 C CG2 . VAL   B 123 ? 0.1697 0.2817 0.1869 -0.0228 0.0108  0.0457  145 VAL   B CG2 
3226 N N   . SER   B 124 ? 0.1495 0.2251 0.1986 -0.0276 0.0122  0.0516  146 SER   B N   
3227 C CA  . SER   B 124 ? 0.1625 0.2395 0.2026 -0.0272 0.0047  0.0591  146 SER   B CA  
3228 C C   . SER   B 124 ? 0.1634 0.2621 0.2081 -0.0229 0.0053  0.0556  146 SER   B C   
3229 O O   . SER   B 124 ? 0.1624 0.2682 0.2159 -0.0580 -0.0103 0.0929  146 SER   B O   
3230 C CB  . SER   B 124 ? 0.1702 0.2317 0.2051 -0.0214 0.0115  0.0588  146 SER   B CB  
3231 O OG  . SER   B 124 ? 0.1823 0.2360 0.2024 -0.0291 -0.0045 0.0623  146 SER   B OG  
3232 N N   . GLY   B 125 ? 0.1711 0.2618 0.2054 -0.0324 0.0090  0.0498  147 GLY   B N   
3233 C CA  . GLY   B 125 ? 0.1819 0.2545 0.1948 -0.0131 0.0037  0.0485  147 GLY   B CA  
3234 C C   . GLY   B 125 ? 0.1741 0.2567 0.1884 -0.0148 0.0081  0.0533  147 GLY   B C   
3235 O O   . GLY   B 125 ? 0.1740 0.2419 0.1769 -0.0361 0.0106  0.0638  147 GLY   B O   
3236 N N   . SER   B 126 ? 0.1591 0.2697 0.1958 -0.0070 0.0148  0.0647  148 SER   B N   
3237 C CA  . SER   B 126 ? 0.1811 0.2704 0.1985 -0.0096 0.0112  0.0731  148 SER   B CA  
3238 C C   . SER   B 126 ? 0.1815 0.2872 0.2154 -0.0035 0.0076  0.0692  148 SER   B C   
3239 O O   . SER   B 126 ? 0.1659 0.2817 0.1987 -0.0020 0.0112  0.0809  148 SER   B O   
3240 C CB  . SER   B 126 ? 0.1924 0.2721 0.2117 -0.0100 -0.0055 0.0662  148 SER   B CB  
3241 O OG  . SER   B 126 ? 0.2087 0.2694 0.2091 -0.0091 0.0062  0.0834  148 SER   B OG  
3242 N N   . PHE   B 127 ? 0.1760 0.2957 0.1918 -0.0142 0.0049  0.0707  149 PHE   B N   
3243 C CA  . PHE   B 127 ? 0.1990 0.3263 0.2027 -0.0289 0.0065  0.0714  149 PHE   B CA  
3244 C C   . PHE   B 127 ? 0.1939 0.3364 0.1831 -0.0280 0.0105  0.0718  149 PHE   B C   
3245 O O   . PHE   B 127 ? 0.1985 0.3506 0.1743 -0.0420 0.0042  0.0772  149 PHE   B O   
3246 C CB  . PHE   B 127 ? 0.1904 0.3296 0.1980 -0.0314 0.0086  0.0776  149 PHE   B CB  
3247 C CG  . PHE   B 127 ? 0.2172 0.3473 0.2150 -0.0485 0.0244  0.0680  149 PHE   B CG  
3248 C CD1 . PHE   B 127 ? 0.2565 0.3685 0.2163 -0.0616 0.0234  0.0786  149 PHE   B CD1 
3249 C CD2 . PHE   B 127 ? 0.2303 0.3628 0.2350 -0.0721 0.0537  0.0393  149 PHE   B CD2 
3250 C CE1 . PHE   B 127 ? 0.2906 0.3716 0.2269 -0.0696 0.0138  0.0782  149 PHE   B CE1 
3251 C CE2 . PHE   B 127 ? 0.2572 0.3420 0.2560 -0.0668 0.0504  0.0420  149 PHE   B CE2 
3252 C CZ  . PHE   B 127 ? 0.2824 0.3508 0.2523 -0.0602 0.0336  0.0502  149 PHE   B CZ  
3253 N N   . ASP   B 128 ? 0.1980 0.3239 0.1950 -0.0426 0.0191  0.0731  150 ASP   B N   
3254 C CA  . ASP   B 128 ? 0.2161 0.3241 0.1903 -0.0447 0.0299  0.0910  150 ASP   B CA  
3255 C C   . ASP   B 128 ? 0.1898 0.3399 0.1908 -0.0571 0.0489  0.0997  150 ASP   B C   
3256 O O   . ASP   B 128 ? 0.1954 0.3366 0.2435 -0.0547 0.0703  0.1144  150 ASP   B O   
3257 C CB  . ASP   B 128 ? 0.2168 0.3213 0.2030 -0.0434 0.0228  0.0800  150 ASP   B CB  
3258 C CG  . ASP   B 128 ? 0.2182 0.3039 0.2023 -0.0393 0.0208  0.0865  150 ASP   B CG  
3259 O OD1 . ASP   B 128 ? 0.2217 0.3038 0.2302 -0.0384 0.0054  0.0945  150 ASP   B OD1 
3260 O OD2 . ASP   B 128 ? 0.2245 0.2820 0.2077 -0.0525 0.0001  0.0835  150 ASP   B OD2 
3261 N N   . GLU   B 129 ? 0.2042 0.3487 0.2082 -0.0491 0.0492  0.0826  151 GLU   B N   
3262 C CA  . GLU   B 129 ? 0.1796 0.3953 0.2047 -0.0482 0.0217  0.0924  151 GLU   B CA  
3263 C C   . GLU   B 129 ? 0.1950 0.3993 0.1952 -0.0365 0.0256  0.0954  151 GLU   B C   
3264 O O   . GLU   B 129 ? 0.1852 0.4449 0.2015 -0.0315 0.0374  0.0742  151 GLU   B O   
3265 C CB  . GLU   B 129 ? 0.1976 0.4344 0.1837 -0.0256 0.0027  0.0932  151 GLU   B CB  
3266 C CG  . GLU   B 129 ? 0.1852 0.4511 0.2179 -0.0203 -0.0223 0.0980  151 GLU   B CG  
3267 C CD  . GLU   B 129 ? 0.1846 0.4487 0.2180 -0.0143 -0.0166 0.0993  151 GLU   B CD  
3268 O OE1 . GLU   B 129 ? 0.1950 0.4633 0.2221 -0.0149 0.0158  0.1179  151 GLU   B OE1 
3269 O OE2 . GLU   B 129 ? 0.2502 0.4471 0.2244 0.0088  -0.0457 0.1085  151 GLU   B OE2 
3270 N N   . SER   B 130 ? 0.1920 0.3674 0.2026 -0.0623 0.0241  0.1053  152 SER   B N   
3271 C CA  . SER   B 130 ? 0.1840 0.3494 0.2170 -0.0605 0.0132  0.1064  152 SER   B CA  
3272 C C   . SER   B 130 ? 0.1684 0.3211 0.2077 -0.0606 -0.0005 0.1004  152 SER   B C   
3273 O O   . SER   B 130 ? 0.1630 0.2838 0.2121 -0.0532 0.0003  0.0656  152 SER   B O   
3274 C CB  . SER   B 130 ? 0.2088 0.3579 0.2455 -0.0545 0.0114  0.1034  152 SER   B CB  
3275 O OG  . SER   B 130 ? 0.2406 0.3495 0.2515 -0.0368 0.0139  0.1109  152 SER   B OG  
3276 N N   . VAL   B 131 ? 0.1654 0.3189 0.2093 -0.0471 -0.0037 0.1034  153 VAL   B N   
3277 C CA  . VAL   B 131 ? 0.1673 0.3281 0.2079 -0.0573 0.0006  0.1011  153 VAL   B CA  
3278 C C   . VAL   B 131 ? 0.1940 0.3306 0.2101 -0.0610 -0.0121 0.1110  153 VAL   B C   
3279 O O   . VAL   B 131 ? 0.2001 0.3716 0.2482 -0.0752 -0.0090 0.1037  153 VAL   B O   
3280 C CB  . VAL   B 131 ? 0.1720 0.3386 0.1887 -0.0535 0.0025  0.0974  153 VAL   B CB  
3281 C CG1 . VAL   B 131 ? 0.1887 0.3589 0.1828 -0.0328 0.0011  0.0830  153 VAL   B CG1 
3282 C CG2 . VAL   B 131 ? 0.1799 0.3425 0.1610 -0.0415 0.0075  0.0922  153 VAL   B CG2 
3283 N N   A ARG   B 132 ? 0.2048 0.3328 0.2273 -0.0685 -0.0107 0.1100  154 ARG   B N   
3284 N N   B ARG   B 132 ? 0.2060 0.3233 0.2307 -0.0683 -0.0109 0.1111  154 ARG   B N   
3285 C CA  A ARG   B 132 ? 0.2268 0.3257 0.2250 -0.0761 -0.0094 0.1084  154 ARG   B CA  
3286 C CA  B ARG   B 132 ? 0.2287 0.3086 0.2320 -0.0752 -0.0103 0.1112  154 ARG   B CA  
3287 C C   A ARG   B 132 ? 0.2381 0.2997 0.2317 -0.0816 -0.0149 0.1090  154 ARG   B C   
3288 C C   B ARG   B 132 ? 0.2392 0.2922 0.2355 -0.0818 -0.0154 0.1095  154 ARG   B C   
3289 O O   A ARG   B 132 ? 0.2402 0.2668 0.2203 -0.0783 -0.0183 0.0960  154 ARG   B O   
3290 O O   B ARG   B 132 ? 0.2404 0.2618 0.2232 -0.0799 -0.0181 0.0941  154 ARG   B O   
3291 C CB  A ARG   B 132 ? 0.2368 0.3407 0.2371 -0.0771 -0.0081 0.1089  154 ARG   B CB  
3292 C CB  B ARG   B 132 ? 0.2411 0.3114 0.2498 -0.0774 -0.0094 0.1140  154 ARG   B CB  
3293 C CG  A ARG   B 132 ? 0.2434 0.3591 0.2450 -0.0798 -0.0019 0.1140  154 ARG   B CG  
3294 C CG  B ARG   B 132 ? 0.2486 0.3131 0.2651 -0.0779 -0.0058 0.1213  154 ARG   B CG  
3295 C CD  A ARG   B 132 ? 0.2684 0.3844 0.2678 -0.0726 -0.0065 0.1113  154 ARG   B CD  
3296 C CD  B ARG   B 132 ? 0.2787 0.3266 0.2891 -0.0699 -0.0111 0.1220  154 ARG   B CD  
3297 N NE  A ARG   B 132 ? 0.2987 0.4160 0.2839 -0.0701 -0.0044 0.1212  154 ARG   B NE  
3298 N NE  B ARG   B 132 ? 0.3098 0.3248 0.3235 -0.0700 -0.0151 0.1283  154 ARG   B NE  
3299 C CZ  A ARG   B 132 ? 0.3316 0.4357 0.2955 -0.0856 -0.0196 0.1118  154 ARG   B CZ  
3300 C CZ  B ARG   B 132 ? 0.3392 0.3368 0.3328 -0.0792 -0.0180 0.1288  154 ARG   B CZ  
3301 N NH1 A ARG   B 132 ? 0.3438 0.4669 0.2936 -0.0659 -0.0553 0.1190  154 ARG   B NH1 
3302 N NH1 B ARG   B 132 ? 0.3352 0.3292 0.3501 -0.0762 -0.0284 0.1164  154 ARG   B NH1 
3303 N NH2 A ARG   B 132 ? 0.3429 0.4543 0.3078 -0.1025 -0.0107 0.1137  154 ARG   B NH2 
3304 N NH2 B ARG   B 132 ? 0.3484 0.3656 0.3567 -0.1017 -0.0196 0.1255  154 ARG   B NH2 
3305 N N   . ILE   B 133 ? 0.2388 0.2827 0.2467 -0.0864 -0.0194 0.1072  155 ILE   B N   
3306 C CA  . ILE   B 133 ? 0.2569 0.2792 0.2508 -0.0700 -0.0240 0.1080  155 ILE   B CA  
3307 C C   . ILE   B 133 ? 0.2669 0.2634 0.2771 -0.0779 -0.0357 0.0951  155 ILE   B C   
3308 O O   . ILE   B 133 ? 0.2571 0.2994 0.2872 -0.0976 -0.0612 0.1055  155 ILE   B O   
3309 C CB  . ILE   B 133 ? 0.2633 0.3033 0.2811 -0.0630 -0.0134 0.1166  155 ILE   B CB  
3310 C CG1 . ILE   B 133 ? 0.2436 0.2862 0.2711 -0.0503 -0.0084 0.1284  155 ILE   B CG1 
3311 C CG2 . ILE   B 133 ? 0.2817 0.2896 0.2781 -0.0624 -0.0152 0.1317  155 ILE   B CG2 
3312 C CD1 . ILE   B 133 ? 0.2434 0.2794 0.3049 -0.0528 -0.0075 0.1446  155 ILE   B CD1 
3313 N N   . TRP   B 134 ? 0.2683 0.2109 0.2653 -0.0655 -0.0413 0.0679  156 TRP   B N   
3314 C CA  . TRP   B 134 ? 0.2783 0.2375 0.2737 -0.0488 -0.0538 0.0668  156 TRP   B CA  
3315 C C   . TRP   B 134 ? 0.2725 0.2375 0.2777 -0.0483 -0.0595 0.0506  156 TRP   B C   
3316 O O   . TRP   B 134 ? 0.2177 0.2264 0.2785 -0.0390 -0.0578 0.0452  156 TRP   B O   
3317 C CB  . TRP   B 134 ? 0.2781 0.2355 0.2641 -0.0369 -0.0626 0.0590  156 TRP   B CB  
3318 C CG  . TRP   B 134 ? 0.2737 0.2280 0.2418 -0.0217 -0.0574 0.0500  156 TRP   B CG  
3319 C CD1 . TRP   B 134 ? 0.2764 0.2326 0.2449 -0.0134 -0.0598 0.0552  156 TRP   B CD1 
3320 C CD2 . TRP   B 134 ? 0.2723 0.2381 0.2447 -0.0178 -0.0709 0.0403  156 TRP   B CD2 
3321 N NE1 . TRP   B 134 ? 0.2696 0.2288 0.2363 -0.0074 -0.0579 0.0353  156 TRP   B NE1 
3322 C CE2 . TRP   B 134 ? 0.2830 0.2368 0.2358 -0.0099 -0.0558 0.0462  156 TRP   B CE2 
3323 C CE3 . TRP   B 134 ? 0.3021 0.2410 0.2298 -0.0187 -0.0728 0.0497  156 TRP   B CE3 
3324 C CZ2 . TRP   B 134 ? 0.2994 0.2426 0.2374 -0.0164 -0.0569 0.0503  156 TRP   B CZ2 
3325 C CZ3 . TRP   B 134 ? 0.2947 0.2517 0.2482 -0.0175 -0.0803 0.0575  156 TRP   B CZ3 
3326 C CH2 . TRP   B 134 ? 0.3056 0.2506 0.2357 -0.0046 -0.0678 0.0444  156 TRP   B CH2 
3327 N N   . ASP   B 135 ? 0.2996 0.2322 0.3033 -0.0492 -0.0560 0.0387  157 ASP   B N   
3328 C CA  . ASP   B 135 ? 0.3286 0.2600 0.3131 -0.0360 -0.0871 0.0370  157 ASP   B CA  
3329 C C   . ASP   B 135 ? 0.3428 0.2396 0.3214 -0.0238 -0.0750 0.0431  157 ASP   B C   
3330 O O   . ASP   B 135 ? 0.3917 0.2125 0.3507 -0.0215 -0.0864 0.0459  157 ASP   B O   
3331 C CB  . ASP   B 135 ? 0.3539 0.2602 0.3344 -0.0333 -0.0933 0.0360  157 ASP   B CB  
3332 C CG  . ASP   B 135 ? 0.3994 0.3312 0.3309 -0.0066 -0.1262 0.0135  157 ASP   B CG  
3333 O OD1 . ASP   B 135 ? 0.4675 0.4395 0.3913 0.0379  -0.1361 0.0327  157 ASP   B OD1 
3334 O OD2 . ASP   B 135 ? 0.4845 0.4343 0.3500 0.0121  -0.1230 0.0304  157 ASP   B OD2 
3335 N N   . VAL   B 136 ? 0.3155 0.2478 0.2943 -0.0154 -0.0835 0.0319  158 VAL   B N   
3336 C CA  . VAL   B 136 ? 0.3216 0.2471 0.2877 -0.0065 -0.0691 0.0377  158 VAL   B CA  
3337 C C   . VAL   B 136 ? 0.3582 0.2465 0.3031 0.0025  -0.0737 0.0301  158 VAL   B C   
3338 O O   . VAL   B 136 ? 0.4011 0.2389 0.3458 0.0063  -0.0697 0.0202  158 VAL   B O   
3339 C CB  . VAL   B 136 ? 0.2801 0.2561 0.2670 0.0076  -0.0574 0.0472  158 VAL   B CB  
3340 C CG1 . VAL   B 136 ? 0.2923 0.2670 0.2699 0.0123  -0.0532 0.0509  158 VAL   B CG1 
3341 C CG2 . VAL   B 136 ? 0.2505 0.2481 0.2551 0.0035  -0.0463 0.0573  158 VAL   B CG2 
3342 N N   . LYS   B 137 ? 0.4050 0.2674 0.3192 0.0041  -0.0870 0.0118  159 LYS   B N   
3343 C CA  . LYS   B 137 ? 0.4680 0.2933 0.3771 0.0214  -0.0973 0.0013  159 LYS   B CA  
3344 C C   . LYS   B 137 ? 0.4829 0.2872 0.3699 0.0061  -0.1083 0.0019  159 LYS   B C   
3345 O O   . LYS   B 137 ? 0.5070 0.3667 0.3879 0.0399  -0.0917 -0.0297 159 LYS   B O   
3346 C CB  . LYS   B 137 ? 0.4974 0.3448 0.4019 0.0273  -0.1065 0.0327  159 LYS   B CB  
3347 C CG  . LYS   B 137 ? 0.5341 0.3668 0.4824 0.0458  -0.0804 0.0620  159 LYS   B CG  
3348 N N   . THR   B 138 ? 0.5168 0.2857 0.3989 -0.0206 -0.1194 -0.0024 160 THR   B N   
3349 C CA  . THR   B 138 ? 0.5360 0.2735 0.4169 -0.0161 -0.1404 0.0173  160 THR   B CA  
3350 C C   . THR   B 138 ? 0.5559 0.2530 0.4187 -0.0106 -0.1339 0.0335  160 THR   B C   
3351 O O   . THR   B 138 ? 0.6183 0.2148 0.4645 -0.0098 -0.1395 0.0202  160 THR   B O   
3352 C CB  . THR   B 138 ? 0.5322 0.2621 0.4165 -0.0336 -0.1414 0.0176  160 THR   B CB  
3353 O OG1 . THR   B 138 ? 0.5147 0.2717 0.4152 -0.0062 -0.1590 0.0209  160 THR   B OG1 
3354 C CG2 . THR   B 138 ? 0.5215 0.2683 0.4515 -0.0688 -0.1485 -0.0034 160 THR   B CG2 
3355 N N   . GLY   B 139 ? 0.5328 0.2520 0.3804 -0.0404 -0.1229 0.0433  161 GLY   B N   
3356 C CA  . GLY   B 139 ? 0.5457 0.2861 0.3807 -0.0439 -0.1131 0.0536  161 GLY   B CA  
3357 C C   . GLY   B 139 ? 0.5472 0.2402 0.3699 -0.0688 -0.1192 0.0965  161 GLY   B C   
3358 O O   . GLY   B 139 ? 0.5979 0.3254 0.3830 -0.0728 -0.1333 0.0565  161 GLY   B O   
3359 N N   . LYS   B 140 ? 0.5350 0.2663 0.3543 -0.0747 -0.0926 0.1285  162 LYS   B N   
3360 C CA  . LYS   B 140 ? 0.4877 0.3445 0.3790 -0.0887 -0.0899 0.1122  162 LYS   B CA  
3361 C C   . LYS   B 140 ? 0.4060 0.3329 0.3680 -0.1073 -0.0999 0.1258  162 LYS   B C   
3362 O O   . LYS   B 140 ? 0.3447 0.3546 0.3634 -0.1182 -0.1109 0.1335  162 LYS   B O   
3363 C CB  . LYS   B 140 ? 0.4558 0.3759 0.3970 -0.0982 -0.0827 0.1147  162 LYS   B CB  
3364 N N   . CYS   B 141 ? 0.3564 0.3164 0.3643 -0.1081 -0.1114 0.1427  163 CYS   B N   
3365 C CA  . CYS   B 141 ? 0.3557 0.3146 0.3745 -0.1155 -0.1040 0.1447  163 CYS   B CA  
3366 C C   . CYS   B 141 ? 0.3382 0.3051 0.4103 -0.1677 -0.0938 0.1383  163 CYS   B C   
3367 O O   . CYS   B 141 ? 0.3436 0.3261 0.4710 -0.1837 -0.0984 0.1519  163 CYS   B O   
3368 C CB  . CYS   B 141 ? 0.3697 0.3264 0.3731 -0.1024 -0.0991 0.1346  163 CYS   B CB  
3369 S SG  . CYS   B 141 ? 0.4056 0.3403 0.3705 -0.1369 -0.0866 0.1169  163 CYS   B SG  
3370 N N   . LEU   B 142 ? 0.3224 0.3254 0.3971 -0.1742 -0.0951 0.1504  164 LEU   B N   
3371 C CA  . LEU   B 142 ? 0.3207 0.3518 0.3911 -0.1639 -0.0655 0.1336  164 LEU   B CA  
3372 C C   . LEU   B 142 ? 0.3090 0.3703 0.3568 -0.1794 -0.0479 0.1547  164 LEU   B C   
3373 O O   . LEU   B 142 ? 0.2844 0.4327 0.3739 -0.1578 -0.0196 0.1323  164 LEU   B O   
3374 C CB  . LEU   B 142 ? 0.3031 0.3328 0.3933 -0.1784 -0.0638 0.1317  164 LEU   B CB  
3375 C CG  . LEU   B 142 ? 0.3470 0.3644 0.4129 -0.1565 -0.0513 0.1213  164 LEU   B CG  
3376 C CD1 . LEU   B 142 ? 0.3759 0.3530 0.4373 -0.1502 -0.0358 0.1318  164 LEU   B CD1 
3377 C CD2 . LEU   B 142 ? 0.3819 0.3883 0.4243 -0.1609 -0.0557 0.1016  164 LEU   B CD2 
3378 N N   . LYS   B 143 ? 0.3138 0.3881 0.3529 -0.1787 -0.0490 0.1632  165 LYS   B N   
3379 C CA  . LYS   B 143 ? 0.3161 0.4185 0.3527 -0.1656 -0.0555 0.1374  165 LYS   B CA  
3380 C C   . LYS   B 143 ? 0.3127 0.4057 0.3252 -0.1573 -0.0394 0.1386  165 LYS   B C   
3381 O O   . LYS   B 143 ? 0.3053 0.3812 0.2805 -0.1562 -0.0300 0.1362  165 LYS   B O   
3382 C CB  . LYS   B 143 ? 0.3044 0.4563 0.3540 -0.1534 -0.0590 0.1299  165 LYS   B CB  
3383 C CG  . LYS   B 143 ? 0.3101 0.5157 0.3786 -0.1363 -0.0677 0.1106  165 LYS   B CG  
3384 C CD  . LYS   B 143 ? 0.3299 0.5587 0.4416 -0.1073 -0.0753 0.0801  165 LYS   B CD  
3385 C CE  . LYS   B 143 ? 0.2918 0.6017 0.5055 -0.0982 -0.0684 0.0720  165 LYS   B CE  
3386 N NZ  . LYS   B 143 ? 0.2748 0.6241 0.5254 -0.1109 -0.0922 0.0627  165 LYS   B NZ  
3387 N N   . THR   B 144 ? 0.2858 0.4075 0.3210 -0.1625 -0.0258 0.1488  166 THR   B N   
3388 C CA  . THR   B 144 ? 0.2507 0.4153 0.3248 -0.1347 -0.0245 0.1465  166 THR   B CA  
3389 C C   . THR   B 144 ? 0.2203 0.4507 0.3310 -0.1295 -0.0077 0.1377  166 THR   B C   
3390 O O   . THR   B 144 ? 0.2239 0.4754 0.3857 -0.1293 0.0192  0.1140  166 THR   B O   
3391 C CB  . THR   B 144 ? 0.2744 0.4236 0.3397 -0.1090 -0.0264 0.1466  166 THR   B CB  
3392 O OG1 . THR   B 144 ? 0.2922 0.4056 0.3937 -0.1079 -0.0462 0.1411  166 THR   B OG1 
3393 C CG2 . THR   B 144 ? 0.2758 0.4189 0.3445 -0.0998 -0.0361 0.1516  166 THR   B CG2 
3394 N N   . LEU   B 145 ? 0.1817 0.4797 0.3201 -0.1163 -0.0025 0.1114  167 LEU   B N   
3395 C CA  . LEU   B 145 ? 0.1570 0.5005 0.3013 -0.0982 -0.0034 0.1042  167 LEU   B CA  
3396 C C   . LEU   B 145 ? 0.1571 0.5323 0.2929 -0.0942 0.0181  0.0719  167 LEU   B C   
3397 O O   . LEU   B 145 ? 0.1415 0.5225 0.2843 -0.0417 0.0164  0.0749  167 LEU   B O   
3398 C CB  . LEU   B 145 ? 0.1986 0.4911 0.3101 -0.0689 -0.0280 0.1066  167 LEU   B CB  
3399 C CG  . LEU   B 145 ? 0.2326 0.4928 0.3170 -0.0531 -0.0249 0.1217  167 LEU   B CG  
3400 C CD1 . LEU   B 145 ? 0.2417 0.5008 0.3090 -0.0350 -0.0363 0.1460  167 LEU   B CD1 
3401 C CD2 . LEU   B 145 ? 0.2608 0.5124 0.3459 -0.0487 -0.0489 0.1243  167 LEU   B CD2 
3402 N N   . PRO   B 146 ? 0.2055 0.5489 0.3001 -0.1037 0.0517  0.0623  168 PRO   B N   
3403 C CA  . PRO   B 146 ? 0.1981 0.5581 0.2994 -0.0808 0.0473  0.0741  168 PRO   B CA  
3404 C C   . PRO   B 146 ? 0.1799 0.5364 0.2581 -0.0575 0.0506  0.0947  168 PRO   B C   
3405 O O   . PRO   B 146 ? 0.1839 0.5522 0.2521 -0.0657 0.0595  0.1102  168 PRO   B O   
3406 C CB  . PRO   B 146 ? 0.2427 0.5746 0.3099 -0.0999 0.0637  0.0707  168 PRO   B CB  
3407 C CG  . PRO   B 146 ? 0.1979 0.5799 0.3340 -0.1076 0.0735  0.0697  168 PRO   B CG  
3408 C CD  . PRO   B 146 ? 0.2250 0.5854 0.3264 -0.0911 0.0453  0.0468  168 PRO   B CD  
3409 N N   . ALA   B 147 ? 0.1657 0.4875 0.2251 -0.0225 0.0504  0.1068  169 ALA   B N   
3410 C CA  . ALA   B 147 ? 0.1811 0.4722 0.2163 -0.0175 0.0485  0.0889  169 ALA   B CA  
3411 C C   . ALA   B 147 ? 0.1936 0.4374 0.2068 -0.0091 0.0518  0.1012  169 ALA   B C   
3412 O O   . ALA   B 147 ? 0.2288 0.4307 0.1958 -0.0032 0.0460  0.0868  169 ALA   B O   
3413 C CB  . ALA   B 147 ? 0.1659 0.4737 0.2215 -0.0210 0.0494  0.0862  169 ALA   B CB  
3414 N N   . HIS   B 148 ? 0.1977 0.4144 0.1967 -0.0119 0.0411  0.0962  170 HIS   B N   
3415 C CA  . HIS   B 148 ? 0.2053 0.3866 0.1977 -0.0059 0.0539  0.0922  170 HIS   B CA  
3416 C C   . HIS   B 148 ? 0.2225 0.3957 0.1887 -0.0191 0.0466  0.0924  170 HIS   B C   
3417 O O   . HIS   B 148 ? 0.2087 0.3921 0.2152 -0.0214 0.0358  0.1060  170 HIS   B O   
3418 C CB  . HIS   B 148 ? 0.1979 0.3561 0.1988 0.0032  0.0593  0.0865  170 HIS   B CB  
3419 C CG  . HIS   B 148 ? 0.1975 0.3497 0.1791 0.0105  0.0668  0.0814  170 HIS   B CG  
3420 N ND1 . HIS   B 148 ? 0.2016 0.3147 0.1961 0.0167  0.0567  0.0988  170 HIS   B ND1 
3421 C CD2 . HIS   B 148 ? 0.2260 0.3346 0.1749 0.0192  0.0592  0.1055  170 HIS   B CD2 
3422 C CE1 . HIS   B 148 ? 0.2487 0.3345 0.1818 0.0310  0.0580  0.0853  170 HIS   B CE1 
3423 N NE2 . HIS   B 148 ? 0.2320 0.3317 0.1909 0.0409  0.0786  0.0817  170 HIS   B NE2 
3424 N N   . SER   B 149 ? 0.2036 0.4101 0.1898 -0.0212 0.0577  0.0902  171 SER   B N   
3425 C CA  . SER   B 149 ? 0.2133 0.4213 0.1871 -0.0294 0.0522  0.1007  171 SER   B CA  
3426 C C   . SER   B 149 ? 0.2011 0.4202 0.2032 -0.0303 0.0547  0.1069  171 SER   B C   
3427 O O   . SER   B 149 ? 0.1839 0.4249 0.2127 -0.0390 0.0597  0.1081  171 SER   B O   
3428 C CB  . SER   B 149 ? 0.1956 0.4161 0.1868 -0.0291 0.0619  0.1023  171 SER   B CB  
3429 O OG  . SER   B 149 ? 0.2430 0.4202 0.1766 0.0019  0.0560  0.1077  171 SER   B OG  
3430 N N   . ASP   B 150 ? 0.2180 0.4255 0.2109 -0.0315 0.0502  0.1104  172 ASP   B N   
3431 C CA  . ASP   B 150 ? 0.2081 0.4069 0.1929 -0.0303 0.0506  0.1075  172 ASP   B CA  
3432 C C   . ASP   B 150 ? 0.2072 0.3887 0.1748 -0.0257 0.0362  0.1211  172 ASP   B C   
3433 O O   . ASP   B 150 ? 0.1779 0.4023 0.1766 -0.0427 0.0414  0.1147  172 ASP   B O   
3434 C CB  . ASP   B 150 ? 0.2318 0.4171 0.2120 -0.0380 0.0449  0.1026  172 ASP   B CB  
3435 C CG  . ASP   B 150 ? 0.2446 0.4363 0.2252 -0.0536 0.0319  0.1145  172 ASP   B CG  
3436 O OD1 . ASP   B 150 ? 0.2684 0.4871 0.2000 -0.0655 0.0002  0.1422  172 ASP   B OD1 
3437 O OD2 . ASP   B 150 ? 0.2889 0.4275 0.2380 -0.0543 0.0423  0.1030  172 ASP   B OD2 
3438 N N   . PRO   B 151 ? 0.2049 0.3568 0.1872 -0.0215 0.0300  0.1160  173 PRO   B N   
3439 C CA  . PRO   B 151 ? 0.2082 0.3281 0.2018 -0.0159 0.0259  0.1158  173 PRO   B CA  
3440 C C   . PRO   B 151 ? 0.2134 0.2988 0.1875 -0.0095 0.0286  0.1010  173 PRO   B C   
3441 O O   . PRO   B 151 ? 0.2237 0.3111 0.1807 0.0021  0.0475  0.1070  173 PRO   B O   
3442 C CB  . PRO   B 151 ? 0.2103 0.3329 0.2180 -0.0223 0.0236  0.1221  173 PRO   B CB  
3443 C CG  . PRO   B 151 ? 0.2092 0.3656 0.2041 -0.0160 0.0380  0.1134  173 PRO   B CG  
3444 C CD  . PRO   B 151 ? 0.2093 0.3654 0.2066 -0.0062 0.0286  0.1150  173 PRO   B CD  
3445 N N   . VAL   B 152 ? 0.1890 0.2629 0.1906 -0.0086 0.0280  0.0886  174 VAL   B N   
3446 C CA  . VAL   B 152 ? 0.1828 0.2779 0.1865 -0.0094 0.0286  0.0832  174 VAL   B CA  
3447 C C   . VAL   B 152 ? 0.1759 0.2679 0.1950 -0.0110 0.0329  0.0781  174 VAL   B C   
3448 O O   . VAL   B 152 ? 0.1677 0.2662 0.2165 -0.0069 0.0335  0.0764  174 VAL   B O   
3449 C CB  . VAL   B 152 ? 0.1774 0.2935 0.1842 -0.0111 0.0116  0.0858  174 VAL   B CB  
3450 C CG1 . VAL   B 152 ? 0.1902 0.2959 0.1825 -0.0085 0.0221  0.0841  174 VAL   B CG1 
3451 C CG2 . VAL   B 152 ? 0.1796 0.3173 0.1856 -0.0149 0.0017  0.0823  174 VAL   B CG2 
3452 N N   . SER   B 153 ? 0.1785 0.2783 0.1792 -0.0086 0.0326  0.0667  175 SER   B N   
3453 C CA  . SER   B 153 ? 0.1822 0.2814 0.1824 -0.0152 0.0316  0.0642  175 SER   B CA  
3454 C C   . SER   B 153 ? 0.1754 0.2823 0.1744 -0.0089 0.0366  0.0601  175 SER   B C   
3455 O O   . SER   B 153 ? 0.1890 0.2922 0.1576 0.0086  0.0448  0.0635  175 SER   B O   
3456 C CB  . SER   B 153 ? 0.2041 0.2851 0.1877 -0.0156 0.0348  0.0666  175 SER   B CB  
3457 O OG  . SER   B 153 ? 0.2163 0.2857 0.1909 -0.0237 0.0383  0.0698  175 SER   B OG  
3458 N N   . ALA   B 154 ? 0.1640 0.2718 0.1563 -0.0214 0.0441  0.0513  176 ALA   B N   
3459 C CA  . ALA   B 154 ? 0.1543 0.2659 0.1551 -0.0182 0.0398  0.0500  176 ALA   B CA  
3460 C C   . ALA   B 154 ? 0.1495 0.2709 0.1565 -0.0131 0.0397  0.0469  176 ALA   B C   
3461 O O   . ALA   B 154 ? 0.1579 0.2793 0.1410 -0.0130 0.0481  0.0544  176 ALA   B O   
3462 C CB  . ALA   B 154 ? 0.1537 0.2668 0.1441 -0.0081 0.0459  0.0569  176 ALA   B CB  
3463 N N   . VAL   B 155 ? 0.1496 0.2612 0.1571 -0.0154 0.0388  0.0384  177 VAL   B N   
3464 C CA  . VAL   B 155 ? 0.1819 0.2532 0.1369 -0.0113 0.0313  0.0341  177 VAL   B CA  
3465 C C   . VAL   B 155 ? 0.1906 0.2490 0.1341 -0.0056 0.0320  0.0318  177 VAL   B C   
3466 O O   . VAL   B 155 ? 0.2057 0.2599 0.1238 0.0009  0.0430  0.0363  177 VAL   B O   
3467 C CB  . VAL   B 155 ? 0.1922 0.2516 0.1401 -0.0099 0.0311  0.0353  177 VAL   B CB  
3468 C CG1 . VAL   B 155 ? 0.2066 0.2675 0.1347 -0.0079 0.0408  0.0227  177 VAL   B CG1 
3469 C CG2 . VAL   B 155 ? 0.2110 0.2419 0.1447 -0.0016 0.0238  0.0402  177 VAL   B CG2 
3470 N N   . HIS   B 156 ? 0.2027 0.2554 0.1408 0.0005  0.0315  0.0446  178 HIS   B N   
3471 C CA  . HIS   B 156 ? 0.1959 0.2583 0.1337 0.0033  0.0260  0.0456  178 HIS   B CA  
3472 C C   . HIS   B 156 ? 0.1929 0.2734 0.1556 0.0060  0.0251  0.0467  178 HIS   B C   
3473 O O   . HIS   B 156 ? 0.1955 0.3068 0.1641 0.0110  0.0295  0.0487  178 HIS   B O   
3474 C CB  . HIS   B 156 ? 0.1980 0.2599 0.1522 0.0007  0.0244  0.0422  178 HIS   B CB  
3475 C CG  . HIS   B 156 ? 0.2217 0.2590 0.1656 -0.0032 0.0199  0.0476  178 HIS   B CG  
3476 N ND1 . HIS   B 156 ? 0.2377 0.2674 0.1866 -0.0169 0.0156  0.0521  178 HIS   B ND1 
3477 C CD2 . HIS   B 156 ? 0.2278 0.2587 0.1751 -0.0040 0.0216  0.0475  178 HIS   B CD2 
3478 C CE1 . HIS   B 156 ? 0.2421 0.2571 0.1739 -0.0083 0.0152  0.0487  178 HIS   B CE1 
3479 N NE2 . HIS   B 156 ? 0.2310 0.2286 0.1724 0.0032  0.0015  0.0427  178 HIS   B NE2 
3480 N N   . PHE   B 157 ? 0.1926 0.2862 0.1554 0.0121  0.0120  0.0337  179 PHE   B N   
3481 C CA  . PHE   B 157 ? 0.2058 0.2736 0.1679 -0.0016 0.0009  0.0384  179 PHE   B CA  
3482 C C   . PHE   B 157 ? 0.2328 0.2756 0.1714 0.0158  -0.0035 0.0274  179 PHE   B C   
3483 O O   . PHE   B 157 ? 0.2305 0.2818 0.1570 0.0087  -0.0052 0.0035  179 PHE   B O   
3484 C CB  . PHE   B 157 ? 0.2020 0.2577 0.1656 -0.0123 0.0101  0.0493  179 PHE   B CB  
3485 C CG  . PHE   B 157 ? 0.1790 0.2523 0.1716 -0.0265 0.0095  0.0482  179 PHE   B CG  
3486 C CD1 . PHE   B 157 ? 0.1877 0.2601 0.2003 -0.0267 0.0171  0.0579  179 PHE   B CD1 
3487 C CD2 . PHE   B 157 ? 0.1786 0.2500 0.1454 -0.0272 0.0221  0.0479  179 PHE   B CD2 
3488 C CE1 . PHE   B 157 ? 0.1751 0.2542 0.1886 -0.0336 0.0165  0.0643  179 PHE   B CE1 
3489 C CE2 . PHE   B 157 ? 0.1762 0.2650 0.1629 -0.0337 0.0187  0.0531  179 PHE   B CE2 
3490 C CZ  . PHE   B 157 ? 0.1758 0.2572 0.1849 -0.0357 0.0174  0.0636  179 PHE   B CZ  
3491 N N   . ASN   B 158 ? 0.2519 0.2714 0.1686 0.0294  -0.0032 0.0264  180 ASN   B N   
3492 C CA  . ASN   B 158 ? 0.2559 0.2721 0.1703 0.0418  0.0021  0.0378  180 ASN   B CA  
3493 C C   . ASN   B 158 ? 0.2710 0.2783 0.1718 0.0300  0.0139  0.0510  180 ASN   B C   
3494 O O   . ASN   B 158 ? 0.2414 0.2903 0.1276 0.0249  0.0414  0.0660  180 ASN   B O   
3495 C CB  . ASN   B 158 ? 0.2664 0.2623 0.1796 0.0550  0.0085  0.0350  180 ASN   B CB  
3496 C CG  . ASN   B 158 ? 0.2764 0.2756 0.2114 0.0572  0.0023  0.0306  180 ASN   B CG  
3497 O OD1 . ASN   B 158 ? 0.2866 0.2697 0.1960 0.0481  -0.0171 0.0376  180 ASN   B OD1 
3498 N ND2 . ASN   B 158 ? 0.3034 0.3186 0.2777 0.0599  -0.0126 0.0143  180 ASN   B ND2 
3499 N N   . ARG   B 159 ? 0.3133 0.2880 0.1883 0.0440  0.0040  0.0598  181 ARG   B N   
3500 C CA  . ARG   B 159 ? 0.3327 0.3132 0.2017 0.0426  0.0058  0.0517  181 ARG   B CA  
3501 C C   . ARG   B 159 ? 0.3044 0.3031 0.1865 0.0315  0.0261  0.0568  181 ARG   B C   
3502 O O   . ARG   B 159 ? 0.2975 0.2973 0.1965 0.0171  0.0240  0.0277  181 ARG   B O   
3503 C CB  . ARG   B 159 ? 0.3847 0.3488 0.2793 0.0505  0.0001  0.0534  181 ARG   B CB  
3504 C CG  . ARG   B 159 ? 0.3839 0.3962 0.3333 0.0520  0.0045  0.0316  181 ARG   B CG  
3505 C CD  . ARG   B 159 ? 0.4007 0.4285 0.4131 0.0664  -0.0136 -0.0044 181 ARG   B CD  
3506 N NE  . ARG   B 159 ? 0.3987 0.4799 0.4609 0.0586  -0.0437 -0.0269 181 ARG   B NE  
3507 C CZ  . ARG   B 159 ? 0.4210 0.5390 0.5291 0.0569  -0.0465 -0.0434 181 ARG   B CZ  
3508 N NH1 . ARG   B 159 ? 0.4179 0.5841 0.5657 0.0416  -0.0404 -0.0694 181 ARG   B NH1 
3509 N NH2 . ARG   B 159 ? 0.4586 0.5686 0.5640 0.0570  -0.0463 -0.0584 181 ARG   B NH2 
3510 N N   . ASP   B 160 ? 0.2800 0.3175 0.1539 0.0408  0.0264  0.0493  182 ASP   B N   
3511 C CA  . ASP   B 160 ? 0.2559 0.3425 0.1596 0.0427  0.0223  0.0511  182 ASP   B CA  
3512 C C   . ASP   B 160 ? 0.2311 0.3271 0.1507 0.0422  0.0190  0.0492  182 ASP   B C   
3513 O O   . ASP   B 160 ? 0.2503 0.3028 0.1661 0.0428  0.0180  0.0547  182 ASP   B O   
3514 C CB  . ASP   B 160 ? 0.2737 0.3754 0.1658 0.0554  0.0073  0.0514  182 ASP   B CB  
3515 C CG  . ASP   B 160 ? 0.2695 0.4153 0.1740 0.0790  -0.0063 0.0426  182 ASP   B CG  
3516 O OD1 . ASP   B 160 ? 0.2823 0.4350 0.1516 0.0885  -0.0102 0.0178  182 ASP   B OD1 
3517 O OD2 . ASP   B 160 ? 0.2990 0.5211 0.2451 0.1251  -0.0159 0.0477  182 ASP   B OD2 
3518 N N   . GLY   B 161 ? 0.2211 0.3303 0.1670 0.0344  0.0047  0.0648  183 GLY   B N   
3519 C CA  . GLY   B 161 ? 0.2199 0.3377 0.1905 0.0249  0.0048  0.0733  183 GLY   B CA  
3520 C C   . GLY   B 161 ? 0.2275 0.3503 0.1902 0.0363  0.0100  0.0815  183 GLY   B C   
3521 O O   . GLY   B 161 ? 0.2249 0.3613 0.1915 -0.0107 -0.0123 0.0867  183 GLY   B O   
3522 N N   . SER   B 162 ? 0.2094 0.3705 0.1904 0.0492  0.0265  0.0733  184 SER   B N   
3523 C CA  . SER   B 162 ? 0.2148 0.3875 0.2054 0.0520  0.0282  0.0845  184 SER   B CA  
3524 C C   . SER   B 162 ? 0.1996 0.4028 0.1980 0.0490  0.0204  0.0816  184 SER   B C   
3525 O O   . SER   B 162 ? 0.2044 0.4470 0.1950 0.0289  0.0232  0.0804  184 SER   B O   
3526 C CB  . SER   B 162 ? 0.2245 0.4050 0.2134 0.0558  0.0169  0.0846  184 SER   B CB  
3527 O OG  . SER   B 162 ? 0.2685 0.3959 0.2439 0.0711  -0.0055 0.0680  184 SER   B OG  
3528 N N   . LEU   B 163 ? 0.2088 0.3967 0.2175 0.0568  0.0291  0.0810  185 LEU   B N   
3529 C CA  . LEU   B 163 ? 0.2036 0.3750 0.2008 0.0608  0.0132  0.0821  185 LEU   B CA  
3530 C C   . LEU   B 163 ? 0.1950 0.3674 0.1985 0.0449  0.0220  0.0824  185 LEU   B C   
3531 O O   . LEU   B 163 ? 0.1840 0.3320 0.1997 0.0460  0.0241  0.0845  185 LEU   B O   
3532 C CB  . LEU   B 163 ? 0.2359 0.3996 0.2123 0.0669  0.0154  0.0778  185 LEU   B CB  
3533 C CG  . LEU   B 163 ? 0.2480 0.4165 0.2423 0.0834  0.0219  0.0621  185 LEU   B CG  
3534 C CD1 . LEU   B 163 ? 0.2871 0.4450 0.2445 0.0977  0.0152  0.0468  185 LEU   B CD1 
3535 C CD2 . LEU   B 163 ? 0.2444 0.4319 0.2539 0.0903  0.0344  0.0730  185 LEU   B CD2 
3536 N N   . ILE   B 164 ? 0.1955 0.3432 0.1827 0.0300  0.0295  0.0753  186 ILE   B N   
3537 C CA  . ILE   B 164 ? 0.1782 0.3210 0.1997 0.0187  0.0225  0.0541  186 ILE   B CA  
3538 C C   . ILE   B 164 ? 0.1778 0.3222 0.1835 0.0304  0.0360  0.0512  186 ILE   B C   
3539 O O   . ILE   B 164 ? 0.1712 0.3348 0.2281 0.0103  0.0489  0.0501  186 ILE   B O   
3540 C CB  . ILE   B 164 ? 0.1765 0.3258 0.2002 0.0117  0.0241  0.0650  186 ILE   B CB  
3541 C CG1 . ILE   B 164 ? 0.1842 0.3126 0.2014 0.0021  0.0071  0.0589  186 ILE   B CG1 
3542 C CG2 . ILE   B 164 ? 0.1824 0.3303 0.2044 0.0191  0.0267  0.0699  186 ILE   B CG2 
3543 C CD1 . ILE   B 164 ? 0.1991 0.3150 0.2155 0.0017  -0.0049 0.0550  186 ILE   B CD1 
3544 N N   . VAL   B 165 ? 0.1724 0.3000 0.1575 0.0320  0.0408  0.0491  187 VAL   B N   
3545 C CA  . VAL   B 165 ? 0.1955 0.3074 0.1617 0.0444  0.0333  0.0515  187 VAL   B CA  
3546 C C   . VAL   B 165 ? 0.1862 0.3242 0.1574 0.0415  0.0398  0.0558  187 VAL   B C   
3547 O O   . VAL   B 165 ? 0.1551 0.3291 0.1690 0.0371  0.0277  0.0708  187 VAL   B O   
3548 C CB  . VAL   B 165 ? 0.2151 0.2989 0.1776 0.0529  0.0209  0.0394  187 VAL   B CB  
3549 C CG1 . VAL   B 165 ? 0.2219 0.2872 0.1665 0.0566  0.0200  0.0420  187 VAL   B CG1 
3550 C CG2 . VAL   B 165 ? 0.2222 0.3073 0.1857 0.0596  0.0216  0.0358  187 VAL   B CG2 
3551 N N   . SER   B 166 ? 0.1816 0.3273 0.1600 0.0393  0.0475  0.0717  188 SER   B N   
3552 C CA  . SER   B 166 ? 0.1758 0.3450 0.1795 0.0340  0.0423  0.0661  188 SER   B CA  
3553 C C   . SER   B 166 ? 0.2062 0.3355 0.1774 0.0274  0.0444  0.0650  188 SER   B C   
3554 O O   . SER   B 166 ? 0.2504 0.3606 0.1663 0.0419  0.0327  0.0388  188 SER   B O   
3555 C CB  . SER   B 166 ? 0.1705 0.3567 0.1851 0.0358  0.0521  0.0665  188 SER   B CB  
3556 O OG  . SER   B 166 ? 0.1475 0.4035 0.2100 0.0390  0.0451  0.0718  188 SER   B OG  
3557 N N   . SER   B 167 ? 0.2008 0.3190 0.1885 0.0155  0.0456  0.0524  189 SER   B N   
3558 C CA  . SER   B 167 ? 0.2115 0.3093 0.1585 0.0136  0.0405  0.0644  189 SER   B CA  
3559 C C   . SER   B 167 ? 0.2146 0.2963 0.1577 0.0085  0.0323  0.0624  189 SER   B C   
3560 O O   . SER   B 167 ? 0.2334 0.2889 0.1239 0.0016  0.0225  0.0549  189 SER   B O   
3561 C CB  . SER   B 167 ? 0.2131 0.2941 0.1584 0.0111  0.0368  0.0602  189 SER   B CB  
3562 O OG  . SER   B 167 ? 0.1989 0.2716 0.1728 -0.0051 0.0485  0.0562  189 SER   B OG  
3563 N N   . SER   B 168 ? 0.2209 0.2979 0.1501 0.0078  0.0480  0.0760  190 SER   B N   
3564 C CA  . SER   B 168 ? 0.2198 0.3064 0.1628 0.0094  0.0329  0.0749  190 SER   B CA  
3565 C C   . SER   B 168 ? 0.2360 0.3087 0.1589 0.0089  0.0296  0.0738  190 SER   B C   
3566 O O   . SER   B 168 ? 0.2542 0.3123 0.1667 0.0236  0.0286  0.0692  190 SER   B O   
3567 C CB  . SER   B 168 ? 0.2216 0.2928 0.1806 0.0088  0.0211  0.0797  190 SER   B CB  
3568 O OG  . SER   B 168 ? 0.2282 0.3084 0.1953 0.0022  0.0085  0.0913  190 SER   B OG  
3569 N N   . TYR   B 169 ? 0.2346 0.3051 0.1673 0.0086  0.0171  0.0692  191 TYR   B N   
3570 C CA  . TYR   B 169 ? 0.2457 0.3440 0.1644 0.0097  0.0204  0.0702  191 TYR   B CA  
3571 C C   . TYR   B 169 ? 0.2641 0.3736 0.1694 0.0269  0.0223  0.0654  191 TYR   B C   
3572 O O   . TYR   B 169 ? 0.2743 0.4268 0.1924 0.0331  0.0332  0.0460  191 TYR   B O   
3573 C CB  . TYR   B 169 ? 0.2691 0.3693 0.1843 0.0175  0.0149  0.0768  191 TYR   B CB  
3574 C CG  . TYR   B 169 ? 0.3134 0.4118 0.1829 0.0209  -0.0043 0.0735  191 TYR   B CG  
3575 C CD1 . TYR   B 169 ? 0.3635 0.4521 0.2106 0.0073  -0.0122 0.0689  191 TYR   B CD1 
3576 C CD2 . TYR   B 169 ? 0.3454 0.4386 0.2015 0.0212  -0.0016 0.0728  191 TYR   B CD2 
3577 C CE1 . TYR   B 169 ? 0.4129 0.5004 0.2452 -0.0055 -0.0410 0.0496  191 TYR   B CE1 
3578 C CE2 . TYR   B 169 ? 0.4016 0.4722 0.2420 0.0088  -0.0422 0.0886  191 TYR   B CE2 
3579 C CZ  . TYR   B 169 ? 0.4187 0.5146 0.2492 0.0133  -0.0471 0.0774  191 TYR   B CZ  
3580 O OH  . TYR   B 169 ? 0.5123 0.6054 0.2788 0.0399  -0.0932 0.0513  191 TYR   B OH  
3581 N N   . ASP   B 170 ? 0.2663 0.3825 0.1632 0.0361  0.0315  0.0626  192 ASP   B N   
3582 C CA  . ASP   B 170 ? 0.2520 0.4032 0.1944 0.0524  0.0425  0.0507  192 ASP   B CA  
3583 C C   . ASP   B 170 ? 0.2619 0.4240 0.1900 0.0783  0.0647  0.0283  192 ASP   B C   
3584 O O   . ASP   B 170 ? 0.2473 0.4752 0.2005 0.1038  0.0504  0.0027  192 ASP   B O   
3585 C CB  . ASP   B 170 ? 0.2471 0.4079 0.1966 0.0500  0.0501  0.0437  192 ASP   B CB  
3586 C CG  . ASP   B 170 ? 0.2367 0.4059 0.2004 0.0482  0.0538  0.0569  192 ASP   B CG  
3587 O OD1 . ASP   B 170 ? 0.2125 0.4355 0.1851 0.0458  0.0538  0.0744  192 ASP   B OD1 
3588 O OD2 . ASP   B 170 ? 0.2594 0.4380 0.1793 0.0462  0.0362  0.0601  192 ASP   B OD2 
3589 N N   . GLY   B 171 ? 0.2805 0.4161 0.2039 0.0847  0.0674  0.0308  193 GLY   B N   
3590 C CA  . GLY   B 171 ? 0.3036 0.4115 0.2090 0.0835  0.0736  0.0224  193 GLY   B CA  
3591 C C   . GLY   B 171 ? 0.3243 0.4241 0.2217 0.0898  0.0714  0.0256  193 GLY   B C   
3592 O O   . GLY   B 171 ? 0.3335 0.4143 0.2834 0.0861  0.0761  0.0538  193 GLY   B O   
3593 N N   . LEU   B 172 ? 0.3338 0.4586 0.2347 0.0842  0.0475  0.0312  194 LEU   B N   
3594 C CA  . LEU   B 172 ? 0.3220 0.4695 0.2098 0.1067  0.0593  0.0367  194 LEU   B CA  
3595 C C   . LEU   B 172 ? 0.3047 0.4475 0.1991 0.1007  0.0429  0.0599  194 LEU   B C   
3596 O O   . LEU   B 172 ? 0.3061 0.4272 0.1599 0.0891  0.0480  0.0526  194 LEU   B O   
3597 C CB  . LEU   B 172 ? 0.3030 0.5093 0.2228 0.1135  0.0608  0.0307  194 LEU   B CB  
3598 C CG  . LEU   B 172 ? 0.3320 0.5552 0.2611 0.1144  0.0828  0.0551  194 LEU   B CG  
3599 C CD1 . LEU   B 172 ? 0.3047 0.5929 0.2728 0.1027  0.0714  0.0615  194 LEU   B CD1 
3600 C CD2 . LEU   B 172 ? 0.3545 0.5550 0.2674 0.1295  0.0794  0.0507  194 LEU   B CD2 
3601 N N   A CYS   B 173 ? 0.2900 0.4471 0.1740 0.0950  0.0420  0.0662  195 CYS   B N   
3602 N N   B CYS   B 173 ? 0.3108 0.4483 0.2193 0.1160  0.0437  0.0666  195 CYS   B N   
3603 C CA  A CYS   B 173 ? 0.2808 0.4437 0.1715 0.0922  0.0368  0.0849  195 CYS   B CA  
3604 C CA  B CYS   B 173 ? 0.3134 0.4609 0.2335 0.1166  0.0502  0.0686  195 CYS   B CA  
3605 C C   A CYS   B 173 ? 0.2798 0.4562 0.1761 0.1072  0.0293  0.0839  195 CYS   B C   
3606 C C   B CYS   B 173 ? 0.2998 0.4643 0.2227 0.1290  0.0464  0.0664  195 CYS   B C   
3607 O O   A CYS   B 173 ? 0.2846 0.4562 0.1627 0.1112  0.0208  0.0906  195 CYS   B O   
3608 O O   B CYS   B 173 ? 0.3074 0.4770 0.2353 0.1386  0.0499  0.0584  195 CYS   B O   
3609 C CB  A CYS   B 173 ? 0.2810 0.4446 0.1559 0.0853  0.0255  0.0958  195 CYS   B CB  
3610 C CB  B CYS   B 173 ? 0.3491 0.4667 0.2764 0.1163  0.0515  0.0839  195 CYS   B CB  
3611 S SG  A CYS   B 173 ? 0.2909 0.4221 0.1414 0.0531  0.0188  0.1205  195 CYS   B SG  
3612 S SG  B CYS   B 173 ? 0.3994 0.4761 0.3010 0.0947  0.0414  0.0956  195 CYS   B SG  
3613 N N   . ARG   B 174 ? 0.2739 0.4618 0.2181 0.1272  0.0422  0.0786  196 ARG   B N   
3614 C CA  . ARG   B 174 ? 0.2602 0.4784 0.1948 0.1215  0.0404  0.0765  196 ARG   B CA  
3615 C C   . ARG   B 174 ? 0.2473 0.4827 0.1997 0.1183  0.0518  0.0815  196 ARG   B C   
3616 O O   . ARG   B 174 ? 0.2014 0.4639 0.1891 0.1209  0.0316  0.1003  196 ARG   B O   
3617 C CB  . ARG   B 174 ? 0.2691 0.5007 0.2207 0.1058  0.0477  0.0915  196 ARG   B CB  
3618 C CG  . ARG   B 174 ? 0.3010 0.5305 0.2423 0.1081  0.0515  0.1070  196 ARG   B CG  
3619 C CD  . ARG   B 174 ? 0.2968 0.5379 0.2748 0.1203  0.0771  0.1372  196 ARG   B CD  
3620 N NE  . ARG   B 174 ? 0.3183 0.5947 0.3301 0.1276  0.1043  0.1313  196 ARG   B NE  
3621 C CZ  . ARG   B 174 ? 0.3141 0.6085 0.3611 0.1150  0.1601  0.1489  196 ARG   B CZ  
3622 N NH1 . ARG   B 174 ? 0.3527 0.6371 0.3805 0.1245  0.1667  0.1261  196 ARG   B NH1 
3623 N NH2 . ARG   B 174 ? 0.3327 0.6408 0.3814 0.1363  0.1930  0.1426  196 ARG   B NH2 
3624 N N   . ILE   B 175 ? 0.2465 0.4790 0.1941 0.1129  0.0465  0.0906  197 ILE   B N   
3625 C CA  . ILE   B 175 ? 0.2595 0.4846 0.2030 0.0836  0.0527  0.0833  197 ILE   B CA  
3626 C C   . ILE   B 175 ? 0.2050 0.4940 0.2085 0.0614  0.0627  0.1008  197 ILE   B C   
3627 O O   . ILE   B 175 ? 0.1851 0.5085 0.2792 0.0691  0.0787  0.0946  197 ILE   B O   
3628 C CB  . ILE   B 175 ? 0.3160 0.4989 0.2354 0.1005  0.0397  0.0795  197 ILE   B CB  
3629 C CG1 . ILE   B 175 ? 0.3356 0.4921 0.2923 0.1022  0.0269  0.0779  197 ILE   B CG1 
3630 C CG2 . ILE   B 175 ? 0.3565 0.5330 0.2540 0.1120  0.0313  0.0693  197 ILE   B CG2 
3631 C CD1 . ILE   B 175 ? 0.3157 0.4702 0.2891 0.1213  0.0108  0.0590  197 ILE   B CD1 
3632 N N   . TRP   B 176 ? 0.1732 0.4938 0.2382 0.0355  0.0676  0.0912  198 TRP   B N   
3633 C CA  . TRP   B 176 ? 0.1722 0.5084 0.2249 0.0123  0.0609  0.0922  198 TRP   B CA  
3634 C C   . TRP   B 176 ? 0.1516 0.5112 0.2392 0.0006  0.0410  0.1044  198 TRP   B C   
3635 O O   . TRP   B 176 ? 0.1556 0.5230 0.2312 -0.0009 0.0373  0.1033  198 TRP   B O   
3636 C CB  . TRP   B 176 ? 0.1647 0.5024 0.1950 0.0116  0.0412  0.1071  198 TRP   B CB  
3637 C CG  . TRP   B 176 ? 0.1796 0.5109 0.1935 -0.0046 0.0622  0.1266  198 TRP   B CG  
3638 C CD1 . TRP   B 176 ? 0.1906 0.5040 0.1908 -0.0070 0.0475  0.1338  198 TRP   B CD1 
3639 C CD2 . TRP   B 176 ? 0.1965 0.5108 0.1983 -0.0190 0.0420  0.1450  198 TRP   B CD2 
3640 N NE1 . TRP   B 176 ? 0.2046 0.4952 0.2023 -0.0041 0.0432  0.1326  198 TRP   B NE1 
3641 C CE2 . TRP   B 176 ? 0.1837 0.5115 0.2167 -0.0083 0.0291  0.1465  198 TRP   B CE2 
3642 C CE3 . TRP   B 176 ? 0.1951 0.5437 0.2363 -0.0273 0.0177  0.1655  198 TRP   B CE3 
3643 C CZ2 . TRP   B 176 ? 0.1944 0.5181 0.2392 -0.0242 0.0349  0.1670  198 TRP   B CZ2 
3644 C CZ3 . TRP   B 176 ? 0.1791 0.5374 0.2505 -0.0324 0.0357  0.1725  198 TRP   B CZ3 
3645 C CH2 . TRP   B 176 ? 0.2075 0.5224 0.2588 -0.0297 0.0246  0.1740  198 TRP   B CH2 
3646 N N   . ASP   B 177 ? 0.1518 0.5558 0.2699 -0.0291 0.0485  0.0918  199 ASP   B N   
3647 C CA  . ASP   B 177 ? 0.1656 0.5603 0.2938 -0.0449 0.0161  0.1053  199 ASP   B CA  
3648 C C   . ASP   B 177 ? 0.1739 0.5335 0.2935 -0.0571 0.0081  0.0983  199 ASP   B C   
3649 O O   . ASP   B 177 ? 0.1991 0.5760 0.2567 -0.0815 -0.0052 0.1431  199 ASP   B O   
3650 C CB  . ASP   B 177 ? 0.1602 0.5868 0.2895 -0.0302 0.0219  0.1033  199 ASP   B CB  
3651 C CG  . ASP   B 177 ? 0.1699 0.5872 0.2881 -0.0368 0.0132  0.1031  199 ASP   B CG  
3652 O OD1 . ASP   B 177 ? 0.2352 0.6049 0.2807 -0.0525 -0.0145 0.1079  199 ASP   B OD1 
3653 O OD2 . ASP   B 177 ? 0.1825 0.6006 0.2566 -0.0429 -0.0125 0.0893  199 ASP   B OD2 
3654 N N   . THR   B 178 ? 0.1807 0.4917 0.2704 -0.0615 -0.0024 0.1183  200 THR   B N   
3655 C CA  . THR   B 178 ? 0.1596 0.4651 0.2961 -0.0569 -0.0082 0.1121  200 THR   B CA  
3656 C C   . THR   B 178 ? 0.1513 0.4934 0.3094 -0.0670 -0.0193 0.1052  200 THR   B C   
3657 O O   . THR   B 178 ? 0.1471 0.4708 0.2919 -0.0636 -0.0021 0.1098  200 THR   B O   
3658 C CB  . THR   B 178 ? 0.1287 0.4333 0.2909 -0.0454 -0.0030 0.0960  200 THR   B CB  
3659 O OG1 . THR   B 178 ? 0.1375 0.4069 0.2846 -0.0353 0.0059  0.0786  200 THR   B OG1 
3660 C CG2 . THR   B 178 ? 0.1457 0.4022 0.3112 -0.0407 -0.0246 0.1195  200 THR   B CG2 
3661 N N   . ALA   B 179 ? 0.1322 0.5262 0.3019 -0.0777 -0.0113 0.0977  201 ALA   B N   
3662 C CA  . ALA   B 179 ? 0.1672 0.5320 0.3489 -0.1123 -0.0244 0.1101  201 ALA   B CA  
3663 C C   . ALA   B 179 ? 0.1792 0.5370 0.3330 -0.1076 -0.0382 0.1207  201 ALA   B C   
3664 O O   . ALA   B 179 ? 0.2652 0.5525 0.3740 -0.0921 -0.0162 0.0907  201 ALA   B O   
3665 C CB  . ALA   B 179 ? 0.1659 0.5441 0.3727 -0.1224 -0.0361 0.1199  201 ALA   B CB  
3666 N N   . SER   B 180 ? 0.1522 0.5560 0.3463 -0.1029 -0.0270 0.1201  202 SER   B N   
3667 C CA  . SER   B 180 ? 0.2046 0.5735 0.3503 -0.0889 -0.0204 0.1554  202 SER   B CA  
3668 C C   . SER   B 180 ? 0.2201 0.6010 0.3588 -0.0845 -0.0269 0.1704  202 SER   B C   
3669 O O   . SER   B 180 ? 0.1745 0.6308 0.3420 -0.0781 -0.0166 0.1779  202 SER   B O   
3670 C CB  . SER   B 180 ? 0.2230 0.5698 0.3417 -0.0807 -0.0075 0.1458  202 SER   B CB  
3671 O OG  . SER   B 180 ? 0.2479 0.6121 0.3373 -0.0732 -0.0262 0.1404  202 SER   B OG  
3672 N N   . GLY   B 181 ? 0.2454 0.6307 0.3523 -0.0967 -0.0267 0.1679  203 GLY   B N   
3673 C CA  . GLY   B 181 ? 0.2329 0.6122 0.3493 -0.0768 -0.0083 0.1817  203 GLY   B CA  
3674 C C   . GLY   B 181 ? 0.2453 0.6338 0.3176 -0.0468 0.0019  0.1866  203 GLY   B C   
3675 O O   . GLY   B 181 ? 0.2289 0.6161 0.3320 -0.0351 -0.0006 0.1982  203 GLY   B O   
3676 N N   . GLN   B 182 ? 0.2452 0.6660 0.3044 -0.0348 0.0105  0.1936  204 GLN   B N   
3677 C CA  . GLN   B 182 ? 0.2407 0.7148 0.3456 -0.0139 0.0180  0.1760  204 GLN   B CA  
3678 C C   . GLN   B 182 ? 0.2174 0.7338 0.3015 0.0102  0.0350  0.1470  204 GLN   B C   
3679 O O   . GLN   B 182 ? 0.2111 0.7107 0.2846 -0.0069 0.0504  0.1344  204 GLN   B O   
3680 C CB  . GLN   B 182 ? 0.2347 0.7492 0.3872 -0.0367 0.0112  0.1850  204 GLN   B CB  
3681 C CG  . GLN   B 182 ? 0.3141 0.7633 0.4544 -0.0309 -0.0045 0.1836  204 GLN   B CG  
3682 C CD  . GLN   B 182 ? 0.3055 0.7541 0.4959 -0.0553 0.0010  0.1818  204 GLN   B CD  
3683 O OE1 . GLN   B 182 ? 0.3990 0.7169 0.5827 -0.0253 -0.0384 0.2092  204 GLN   B OE1 
3684 N NE2 . GLN   B 182 ? 0.2516 0.7841 0.4801 -0.0874 0.0131  0.1652  204 GLN   B NE2 
3685 N N   . CYS   B 183 ? 0.1975 0.7962 0.2777 0.0435  0.0364  0.1499  205 CYS   B N   
3686 C CA  . CYS   B 183 ? 0.2015 0.8038 0.2880 0.0544  0.0776  0.1306  205 CYS   B CA  
3687 C C   . CYS   B 183 ? 0.2156 0.8420 0.3348 0.0911  0.0971  0.1213  205 CYS   B C   
3688 O O   . CYS   B 183 ? 0.2534 0.9251 0.3483 0.1094  0.1405  0.1539  205 CYS   B O   
3689 C CB  . CYS   B 183 ? 0.2196 0.8272 0.2839 0.0485  0.0986  0.1160  205 CYS   B CB  
3690 S SG  . CYS   B 183 ? 0.2914 0.8813 0.3436 0.0417  0.0630  0.0935  205 CYS   B SG  
3691 N N   . LEU   B 184 ? 0.2061 0.8359 0.3060 0.1327  0.1207  0.0967  206 LEU   B N   
3692 C CA  . LEU   B 184 ? 0.1913 0.8581 0.3333 0.1688  0.0586  0.0619  206 LEU   B CA  
3693 C C   . LEU   B 184 ? 0.2635 0.8636 0.3137 0.2369  0.0792  0.0435  206 LEU   B C   
3694 O O   . LEU   B 184 ? 0.3918 0.8642 0.3375 0.3061  0.0156  0.0324  206 LEU   B O   
3695 C CB  . LEU   B 184 ? 0.2489 0.8728 0.3521 0.1477  0.0565  0.0563  206 LEU   B CB  
3696 C CG  . LEU   B 184 ? 0.2628 0.9012 0.3563 0.1358  0.0447  0.0366  206 LEU   B CG  
3697 C CD1 . LEU   B 184 ? 0.2815 0.9088 0.3740 0.1312  0.0357  0.0628  206 LEU   B CD1 
3698 C CD2 . LEU   B 184 ? 0.2835 0.9284 0.3986 0.1295  0.0329  0.0179  206 LEU   B CD2 
3699 N N   . LYS   B 185 ? 0.2791 0.8337 0.2601 0.2409  0.0871  0.0411  207 LYS   B N   
3700 C CA  . LYS   B 185 ? 0.3817 0.8379 0.2859 0.2517  0.0713  0.0315  207 LYS   B CA  
3701 C C   . LYS   B 185 ? 0.4010 0.8222 0.2550 0.2588  0.0814  0.0432  207 LYS   B C   
3702 O O   . LYS   B 185 ? 0.3755 0.7737 0.2530 0.2370  0.0751  0.0583  207 LYS   B O   
3703 C CB  . LYS   B 185 ? 0.4566 0.8467 0.3198 0.2382  0.0897  0.0151  207 LYS   B CB  
3704 C CG  . LYS   B 185 ? 0.5394 0.8137 0.4307 0.2310  0.0496  0.0142  207 LYS   B CG  
3705 N N   . THR   B 186 ? 0.4236 0.8273 0.2725 0.2759  0.0749  0.0276  208 THR   B N   
3706 C CA  . THR   B 186 ? 0.4267 0.8352 0.2863 0.3027  0.0582  0.0565  208 THR   B CA  
3707 C C   . THR   B 186 ? 0.4761 0.8316 0.3453 0.3470  0.0432  0.0280  208 THR   B C   
3708 O O   . THR   B 186 ? 0.4543 0.9432 0.3906 0.3827  0.0619  0.0452  208 THR   B O   
3709 C CB  . THR   B 186 ? 0.3980 0.8428 0.2864 0.2658  0.0748  0.0436  208 THR   B CB  
3710 O OG1 . THR   B 186 ? 0.3249 0.8493 0.3110 0.2349  0.0612  0.0754  208 THR   B OG1 
3711 C CG2 . THR   B 186 ? 0.4114 0.8454 0.3035 0.2645  0.0612  0.0649  208 THR   B CG2 
3712 N N   . LEU   B 187 ? 0.4887 0.8040 0.3810 0.3764  0.0336  0.0117  209 LEU   B N   
3713 C CA  . LEU   B 187 ? 0.5787 0.7963 0.5022 0.3626  0.0007  0.0391  209 LEU   B CA  
3714 C C   . LEU   B 187 ? 0.6567 0.7711 0.4509 0.3634  0.0107  0.0138  209 LEU   B C   
3715 O O   . LEU   B 187 ? 0.5812 0.7822 0.3767 0.3277  0.0100  0.0270  209 LEU   B O   
3716 C CB  . LEU   B 187 ? 0.6115 0.8155 0.4763 0.3462  0.0285  0.0741  209 LEU   B CB  
3717 C CG  . LEU   B 187 ? 0.6448 0.8594 0.5785 0.3214  -0.0003 0.1229  209 LEU   B CG  
3718 C CD1 . LEU   B 187 ? 0.6925 0.8708 0.5674 0.3015  0.0134  0.1521  209 LEU   B CD1 
3719 C CD2 . LEU   B 187 ? 0.6492 0.8924 0.6341 0.3203  0.0330  0.0887  209 LEU   B CD2 
3720 N N   . ILE   B 188 ? 0.7071 0.7548 0.5843 0.4135  0.0546  -0.0199 210 ILE   B N   
3721 C CA  . ILE   B 188 ? 0.7755 0.7301 0.5695 0.4211  0.0380  -0.0610 210 ILE   B CA  
3722 C C   . ILE   B 188 ? 0.8615 0.6791 0.5954 0.4608  0.0613  -0.0943 210 ILE   B C   
3723 O O   . ILE   B 188 ? 0.9154 0.7099 0.5735 0.4366  -0.0048 -0.0988 210 ILE   B O   
3724 C CB  . ILE   B 188 ? 0.7394 0.7317 0.5322 0.4357  0.1085  -0.0897 210 ILE   B CB  
3725 N N   . ASP   B 191 ? 0.8457 0.7568 0.7599 0.2731  0.0163  -0.1467 213 ASP   B N   
3726 C CA  . ASP   B 191 ? 0.8451 0.7185 0.7542 0.2790  0.0637  -0.1892 213 ASP   B CA  
3727 C C   . ASP   B 191 ? 0.8558 0.7785 0.7152 0.2544  0.1059  -0.1831 213 ASP   B C   
3728 O O   . ASP   B 191 ? 0.8303 0.8109 0.7384 0.3376  0.0878  -0.2538 213 ASP   B O   
3729 C CB  . ASP   B 191 ? 0.9071 0.7692 0.7627 0.2332  0.0432  -0.1900 213 ASP   B CB  
3730 C CG  . ASP   B 191 ? 0.9556 0.8326 0.7262 0.1732  0.0006  -0.1684 213 ASP   B CG  
3731 O OD1 . ASP   B 191 ? 1.0092 0.8591 0.6617 0.1043  -0.0490 -0.1122 213 ASP   B OD1 
3732 O OD2 . ASP   B 191 ? 0.9827 0.8815 0.8230 0.1228  -0.0054 -0.1389 213 ASP   B OD2 
3733 N N   . ASN   B 192 ? 0.7792 0.7378 0.6268 0.2096  0.1524  -0.1262 214 ASN   B N   
3734 C CA  . ASN   B 192 ? 0.7092 0.6654 0.6132 0.1533  0.1231  -0.0798 214 ASN   B CA  
3735 C C   . ASN   B 192 ? 0.6624 0.5951 0.4575 0.1139  0.0835  -0.0246 214 ASN   B C   
3736 O O   . ASN   B 192 ? 0.6423 0.6148 0.3635 0.1300  0.0884  0.0292  214 ASN   B O   
3737 C CB  . ASN   B 192 ? 0.7081 0.6937 0.6669 0.1198  0.1513  -0.0529 214 ASN   B CB  
3738 C CG  . ASN   B 192 ? 0.7677 0.6744 0.7096 0.0888  0.1463  -0.0334 214 ASN   B CG  
3739 O OD1 . ASN   B 192 ? 0.7870 0.6993 0.7684 0.1136  0.1643  -0.0700 214 ASN   B OD1 
3740 N ND2 . ASN   B 192 ? 0.7899 0.6669 0.7785 0.0520  0.1321  -0.0383 214 ASN   B ND2 
3741 N N   . PRO   B 193 ? 0.5770 0.5432 0.3816 0.1070  0.0456  -0.0644 215 PRO   B N   
3742 C CA  . PRO   B 193 ? 0.5554 0.4886 0.3472 0.0849  0.0306  -0.0568 215 PRO   B CA  
3743 C C   . PRO   B 193 ? 0.4686 0.4454 0.2768 0.0663  0.0424  -0.0206 215 PRO   B C   
3744 O O   . PRO   B 193 ? 0.4446 0.4157 0.2645 0.0571  0.0570  -0.0563 215 PRO   B O   
3745 C CB  . PRO   B 193 ? 0.5665 0.5186 0.4077 0.0838  0.0278  -0.0581 215 PRO   B CB  
3746 C CG  . PRO   B 193 ? 0.5862 0.5142 0.3908 0.0845  0.0383  -0.0683 215 PRO   B CG  
3747 C CD  . PRO   B 193 ? 0.5954 0.5174 0.4169 0.0868  0.0535  -0.0731 215 PRO   B CD  
3748 N N   . PRO   B 194 ? 0.4594 0.3877 0.2214 0.0367  0.0285  0.0041  216 PRO   B N   
3749 C CA  . PRO   B 194 ? 0.4184 0.3772 0.1740 0.0335  0.0162  0.0235  216 PRO   B CA  
3750 C C   . PRO   B 194 ? 0.3769 0.3311 0.1781 0.0282  0.0099  0.0252  216 PRO   B C   
3751 O O   . PRO   B 194 ? 0.4041 0.3104 0.2069 0.0329  0.0061  0.0183  216 PRO   B O   
3752 C CB  . PRO   B 194 ? 0.4227 0.3915 0.2032 0.0317  0.0015  0.0276  216 PRO   B CB  
3753 C CG  . PRO   B 194 ? 0.4489 0.4072 0.2258 0.0275  0.0044  0.0015  216 PRO   B CG  
3754 C CD  . PRO   B 194 ? 0.4618 0.4169 0.2453 0.0384  0.0081  -0.0065 216 PRO   B CD  
3755 N N   . VAL   B 195 ? 0.3548 0.2916 0.1645 0.0347  0.0259  0.0124  217 VAL   B N   
3756 C CA  . VAL   B 195 ? 0.3328 0.3082 0.1764 0.0098  0.0147  0.0293  217 VAL   B CA  
3757 C C   . VAL   B 195 ? 0.3054 0.2877 0.1574 -0.0023 0.0150  0.0225  217 VAL   B C   
3758 O O   . VAL   B 195 ? 0.3020 0.2899 0.1615 0.0036  0.0543  0.0536  217 VAL   B O   
3759 C CB  . VAL   B 195 ? 0.3388 0.3402 0.1848 0.0299  0.0098  0.0285  217 VAL   B CB  
3760 C CG1 . VAL   B 195 ? 0.3134 0.3506 0.1746 0.0267  0.0042  0.0225  217 VAL   B CG1 
3761 C CG2 . VAL   B 195 ? 0.3730 0.3688 0.1919 0.0301  0.0187  0.0117  217 VAL   B CG2 
3762 N N   . SER   B 196 ? 0.3098 0.2847 0.1823 -0.0035 0.0051  0.0250  218 SER   B N   
3763 C CA  . SER   B 196 ? 0.3029 0.2598 0.1930 -0.0153 0.0059  0.0101  218 SER   B CA  
3764 C C   . SER   B 196 ? 0.2942 0.2589 0.1971 -0.0175 0.0196  0.0196  218 SER   B C   
3765 O O   . SER   B 196 ? 0.2563 0.2467 0.1797 -0.0359 0.0415  0.0123  218 SER   B O   
3766 C CB  . SER   B 196 ? 0.3282 0.2607 0.2219 -0.0176 -0.0144 0.0057  218 SER   B CB  
3767 O OG  . SER   B 196 ? 0.3383 0.2403 0.2244 -0.0061 -0.0317 0.0100  218 SER   B OG  
3768 N N   . PHE   B 197 ? 0.2917 0.2737 0.1958 -0.0130 0.0203  0.0181  219 PHE   B N   
3769 C CA  . PHE   B 197 ? 0.2960 0.2694 0.1925 -0.0158 0.0301  0.0272  219 PHE   B CA  
3770 C C   . PHE   B 197 ? 0.2908 0.2479 0.1901 -0.0019 0.0380  0.0254  219 PHE   B C   
3771 O O   . PHE   B 197 ? 0.2952 0.2574 0.2142 0.0079  0.0227  0.0237  219 PHE   B O   
3772 C CB  . PHE   B 197 ? 0.3024 0.2890 0.2093 -0.0185 0.0313  0.0404  219 PHE   B CB  
3773 C CG  . PHE   B 197 ? 0.3199 0.3163 0.2088 -0.0269 0.0482  0.0461  219 PHE   B CG  
3774 C CD1 . PHE   B 197 ? 0.3121 0.3339 0.2115 -0.0382 0.0438  0.0469  219 PHE   B CD1 
3775 C CD2 . PHE   B 197 ? 0.3379 0.3592 0.1971 -0.0283 0.0431  0.0512  219 PHE   B CD2 
3776 C CE1 . PHE   B 197 ? 0.3171 0.3494 0.2078 -0.0369 0.0440  0.0512  219 PHE   B CE1 
3777 C CE2 . PHE   B 197 ? 0.3428 0.3498 0.1882 -0.0369 0.0397  0.0552  219 PHE   B CE2 
3778 C CZ  . PHE   B 197 ? 0.3405 0.3586 0.1800 -0.0279 0.0369  0.0601  219 PHE   B CZ  
3779 N N   . VAL   B 198 ? 0.2807 0.2512 0.1900 0.0154  0.0269  0.0320  220 VAL   B N   
3780 C CA  . VAL   B 198 ? 0.2953 0.2448 0.1924 0.0124  0.0316  0.0199  220 VAL   B CA  
3781 C C   . VAL   B 198 ? 0.2906 0.2374 0.1868 0.0152  0.0349  0.0238  220 VAL   B C   
3782 O O   . VAL   B 198 ? 0.3164 0.2465 0.1794 0.0168  0.0406  0.0418  220 VAL   B O   
3783 C CB  . VAL   B 198 ? 0.2891 0.2777 0.2092 -0.0005 0.0203  0.0260  220 VAL   B CB  
3784 C CG1 . VAL   B 198 ? 0.2921 0.2901 0.1906 0.0031  0.0228  0.0191  220 VAL   B CG1 
3785 C CG2 . VAL   B 198 ? 0.3148 0.3065 0.2564 -0.0071 0.0354  0.0137  220 VAL   B CG2 
3786 N N   A LYS   B 199 ? 0.3052 0.2254 0.1793 0.0174  0.0402  0.0127  221 LYS   B N   
3787 N N   B LYS   B 199 ? 0.2934 0.2362 0.1688 0.0173  0.0481  0.0188  221 LYS   B N   
3788 C CA  A LYS   B 199 ? 0.3195 0.2230 0.1901 0.0209  0.0246  0.0035  221 LYS   B CA  
3789 C CA  B LYS   B 199 ? 0.2981 0.2394 0.1716 0.0202  0.0387  0.0167  221 LYS   B CA  
3790 C C   A LYS   B 199 ? 0.3249 0.2208 0.1816 0.0250  0.0209  0.0024  221 LYS   B C   
3791 C C   B LYS   B 199 ? 0.3178 0.2265 0.1695 0.0261  0.0289  0.0149  221 LYS   B C   
3792 O O   A LYS   B 199 ? 0.3108 0.2331 0.1804 0.0375  0.0179  -0.0213 221 LYS   B O   
3793 O O   B LYS   B 199 ? 0.3262 0.2299 0.1745 0.0389  0.0264  0.0102  221 LYS   B O   
3794 C CB  A LYS   B 199 ? 0.3351 0.2324 0.2005 0.0135  0.0313  -0.0010 221 LYS   B CB  
3795 C CB  B LYS   B 199 ? 0.2989 0.2582 0.1638 0.0171  0.0507  0.0185  221 LYS   B CB  
3796 C CG  A LYS   B 199 ? 0.3501 0.2293 0.2278 0.0096  0.0290  0.0027  221 LYS   B CG  
3797 C CG  B LYS   B 199 ? 0.2953 0.2780 0.1660 0.0090  0.0620  0.0227  221 LYS   B CG  
3798 C CD  A LYS   B 199 ? 0.3651 0.2407 0.2555 0.0095  0.0413  0.0032  221 LYS   B CD  
3799 C CD  B LYS   B 199 ? 0.3033 0.2897 0.1688 0.0005  0.0650  0.0185  221 LYS   B CD  
3800 C CE  A LYS   B 199 ? 0.3868 0.2502 0.2774 0.0112  0.0501  0.0023  221 LYS   B CE  
3801 C CE  B LYS   B 199 ? 0.2927 0.2992 0.1730 -0.0054 0.0804  0.0193  221 LYS   B CE  
3802 N NZ  A LYS   B 199 ? 0.3969 0.2510 0.2979 0.0183  0.0588  0.0097  221 LYS   B NZ  
3803 N NZ  B LYS   B 199 ? 0.2951 0.3022 0.1657 -0.0064 0.0807  0.0257  221 LYS   B NZ  
3804 N N   . PHE   B 200 ? 0.3266 0.2153 0.1782 0.0344  0.0109  0.0147  222 PHE   B N   
3805 C CA  . PHE   B 200 ? 0.3380 0.2262 0.1830 0.0551  -0.0009 -0.0016 222 PHE   B CA  
3806 C C   . PHE   B 200 ? 0.3611 0.2244 0.1832 0.0452  -0.0143 0.0064  222 PHE   B C   
3807 O O   . PHE   B 200 ? 0.3676 0.2221 0.1861 0.0338  0.0051  0.0223  222 PHE   B O   
3808 C CB  . PHE   B 200 ? 0.3403 0.2385 0.1954 0.0662  -0.0088 0.0131  222 PHE   B CB  
3809 C CG  . PHE   B 200 ? 0.3248 0.2625 0.1730 0.0702  0.0201  0.0103  222 PHE   B CG  
3810 C CD1 . PHE   B 200 ? 0.3385 0.2764 0.2276 0.0673  0.0223  0.0129  222 PHE   B CD1 
3811 C CD2 . PHE   B 200 ? 0.3155 0.2701 0.1556 0.0690  0.0220  0.0244  222 PHE   B CD2 
3812 C CE1 . PHE   B 200 ? 0.3244 0.2866 0.2215 0.0599  0.0251  -0.0012 222 PHE   B CE1 
3813 C CE2 . PHE   B 200 ? 0.3210 0.2824 0.1738 0.0718  0.0217  0.0191  222 PHE   B CE2 
3814 C CZ  . PHE   B 200 ? 0.3147 0.2826 0.2171 0.0794  0.0222  0.0199  222 PHE   B CZ  
3815 N N   . SER   B 201 ? 0.3866 0.2396 0.2186 0.0492  -0.0272 -0.0071 223 SER   B N   
3816 C CA  . SER   B 201 ? 0.4365 0.2423 0.2532 0.0270  -0.0347 0.0055  223 SER   B CA  
3817 C C   . SER   B 201 ? 0.4654 0.2459 0.2592 0.0096  -0.0383 0.0041  223 SER   B C   
3818 O O   . SER   B 201 ? 0.4391 0.2001 0.2279 0.0126  -0.0479 0.0203  223 SER   B O   
3819 C CB  . SER   B 201 ? 0.4410 0.2438 0.2809 0.0357  -0.0366 0.0166  223 SER   B CB  
3820 O OG  . SER   B 201 ? 0.4333 0.2366 0.3184 0.0328  -0.0302 0.0149  223 SER   B OG  
3821 N N   . PRO   B 202 ? 0.4937 0.2797 0.2684 -0.0329 -0.0424 0.0116  224 PRO   B N   
3822 C CA  . PRO   B 202 ? 0.5091 0.3031 0.2357 -0.0526 -0.0581 0.0343  224 PRO   B CA  
3823 C C   . PRO   B 202 ? 0.5301 0.3048 0.2277 -0.0324 -0.0666 0.0179  224 PRO   B C   
3824 O O   . PRO   B 202 ? 0.5096 0.3500 0.1952 -0.0351 -0.0604 -0.0152 224 PRO   B O   
3825 C CB  . PRO   B 202 ? 0.5233 0.3171 0.2775 -0.0708 -0.0524 0.0195  224 PRO   B CB  
3826 C CG  . PRO   B 202 ? 0.5144 0.3228 0.2776 -0.0605 -0.0525 0.0164  224 PRO   B CG  
3827 C CD  . PRO   B 202 ? 0.5005 0.2881 0.2704 -0.0449 -0.0557 0.0087  224 PRO   B CD  
3828 N N   . ASN   B 203 ? 0.5629 0.3267 0.2237 0.0035  -0.1003 0.0181  225 ASN   B N   
3829 C CA  . ASN   B 203 ? 0.5904 0.3350 0.3202 0.0477  -0.0920 0.0105  225 ASN   B CA  
3830 C C   . ASN   B 203 ? 0.5376 0.3682 0.2736 0.0831  -0.0772 0.0136  225 ASN   B C   
3831 O O   . ASN   B 203 ? 0.5255 0.3433 0.2688 0.1438  -0.0677 0.0080  225 ASN   B O   
3832 C CB  . ASN   B 203 ? 0.6489 0.3321 0.3466 0.0653  -0.1064 0.0039  225 ASN   B CB  
3833 C CG  . ASN   B 203 ? 0.7222 0.2845 0.3555 0.0839  -0.1340 -0.0051 225 ASN   B CG  
3834 O OD1 . ASN   B 203 ? 0.7376 0.2870 0.3355 0.0895  -0.1711 -0.0071 225 ASN   B OD1 
3835 N ND2 . ASN   B 203 ? 0.7384 0.2903 0.3954 0.1122  -0.1476 0.0370  225 ASN   B ND2 
3836 N N   . GLY   B 204 ? 0.4845 0.3617 0.2925 0.0895  -0.0610 0.0287  226 GLY   B N   
3837 C CA  . GLY   B 204 ? 0.4801 0.3761 0.2667 0.1249  -0.0277 0.0229  226 GLY   B CA  
3838 C C   . GLY   B 204 ? 0.4640 0.3876 0.3028 0.1556  -0.0102 0.0206  226 GLY   B C   
3839 O O   . GLY   B 204 ? 0.4384 0.4320 0.3324 0.1581  0.0541  -0.0413 226 GLY   B O   
3840 N N   . LYS   B 205 ? 0.4750 0.4020 0.2808 0.1719  -0.0063 -0.0010 227 LYS   B N   
3841 C CA  . LYS   B 205 ? 0.4838 0.4237 0.2689 0.1932  -0.0226 0.0018  227 LYS   B CA  
3842 C C   . LYS   B 205 ? 0.5073 0.4451 0.2907 0.1827  -0.0303 -0.0176 227 LYS   B C   
3843 O O   . LYS   B 205 ? 0.5038 0.4508 0.2733 0.1986  -0.0622 -0.0359 227 LYS   B O   
3844 C CB  . LYS   B 205 ? 0.5061 0.4443 0.2755 0.2072  -0.0396 0.0158  227 LYS   B CB  
3845 C CG  . LYS   B 205 ? 0.5464 0.5116 0.2538 0.1903  -0.0258 0.0330  227 LYS   B CG  
3846 N N   . TYR   B 206 ? 0.5245 0.3991 0.2618 0.1793  -0.0558 0.0024  228 TYR   B N   
3847 C CA  . TYR   B 206 ? 0.5106 0.3474 0.2813 0.1664  -0.0476 -0.0092 228 TYR   B CA  
3848 C C   . TYR   B 206 ? 0.4802 0.3244 0.2337 0.1392  -0.0399 -0.0097 228 TYR   B C   
3849 O O   . TYR   B 206 ? 0.4791 0.3052 0.2178 0.1220  -0.0528 -0.0173 228 TYR   B O   
3850 C CB  . TYR   B 206 ? 0.5564 0.3560 0.3107 0.1703  -0.0505 -0.0089 228 TYR   B CB  
3851 C CG  . TYR   B 206 ? 0.5952 0.3699 0.3505 0.1699  -0.0701 0.0212  228 TYR   B CG  
3852 C CD1 . TYR   B 206 ? 0.6049 0.3919 0.3700 0.1765  -0.0674 0.0229  228 TYR   B CD1 
3853 C CD2 . TYR   B 206 ? 0.6056 0.3824 0.3719 0.1669  -0.0716 0.0238  228 TYR   B CD2 
3854 C CE1 . TYR   B 206 ? 0.6306 0.3922 0.4006 0.1745  -0.0538 0.0527  228 TYR   B CE1 
3855 C CE2 . TYR   B 206 ? 0.6441 0.3489 0.4185 0.1618  -0.0624 0.0277  228 TYR   B CE2 
3856 C CZ  . TYR   B 206 ? 0.6460 0.3915 0.4385 0.1825  -0.0594 0.0704  228 TYR   B CZ  
3857 O OH  . TYR   B 206 ? 0.6966 0.3701 0.5009 0.1852  -0.0178 0.1182  228 TYR   B OH  
3858 N N   A ILE   B 207 ? 0.4317 0.3183 0.2214 0.1335  -0.0320 -0.0371 229 ILE   B N   
3859 N N   B ILE   B 207 ? 0.4675 0.3381 0.2328 0.1180  -0.0312 -0.0208 229 ILE   B N   
3860 C CA  A ILE   B 207 ? 0.4214 0.3041 0.2068 0.1302  -0.0239 -0.0351 229 ILE   B CA  
3861 C CA  B ILE   B 207 ? 0.4663 0.3296 0.2361 0.1114  -0.0246 -0.0154 229 ILE   B CA  
3862 C C   A ILE   B 207 ? 0.4333 0.3004 0.2076 0.1168  -0.0236 -0.0255 229 ILE   B C   
3863 C C   B ILE   B 207 ? 0.4532 0.3156 0.2234 0.1072  -0.0164 -0.0118 229 ILE   B C   
3864 O O   A ILE   B 207 ? 0.4505 0.3009 0.2205 0.1295  -0.0160 -0.0255 229 ILE   B O   
3865 O O   B ILE   B 207 ? 0.4747 0.3113 0.2323 0.1086  0.0029  -0.0082 229 ILE   B O   
3866 C CB  A ILE   B 207 ? 0.3859 0.3148 0.1884 0.1336  -0.0143 -0.0443 229 ILE   B CB  
3867 C CB  B ILE   B 207 ? 0.4732 0.3670 0.2478 0.0950  -0.0141 -0.0177 229 ILE   B CB  
3868 C CG1 A ILE   B 207 ? 0.3830 0.3218 0.1835 0.1254  -0.0201 -0.0483 229 ILE   B CG1 
3869 C CG1 B ILE   B 207 ? 0.4827 0.3851 0.2448 0.0823  -0.0123 -0.0117 229 ILE   B CG1 
3870 C CG2 A ILE   B 207 ? 0.3782 0.3244 0.1688 0.1286  -0.0083 -0.0351 229 ILE   B CG2 
3871 C CG2 B ILE   B 207 ? 0.4773 0.3759 0.2416 0.0872  -0.0121 -0.0108 229 ILE   B CG2 
3872 C CD1 A ILE   B 207 ? 0.3730 0.3261 0.2004 0.1214  -0.0200 -0.0563 229 ILE   B CD1 
3873 C CD1 B ILE   B 207 ? 0.4782 0.3998 0.2663 0.0811  -0.0240 -0.0082 229 ILE   B CD1 
3874 N N   . LEU   B 208 ? 0.4327 0.2823 0.1938 0.1050  -0.0234 -0.0019 230 LEU   B N   
3875 C CA  . LEU   B 208 ? 0.4206 0.2830 0.2047 0.0752  -0.0203 0.0064  230 LEU   B CA  
3876 C C   . LEU   B 208 ? 0.3849 0.2837 0.1963 0.0606  -0.0261 0.0059  230 LEU   B C   
3877 O O   . LEU   B 208 ? 0.3699 0.3102 0.2137 0.0840  -0.0411 -0.0038 230 LEU   B O   
3878 C CB  . LEU   B 208 ? 0.4492 0.2691 0.2216 0.0735  -0.0047 0.0278  230 LEU   B CB  
3879 C CG  . LEU   B 208 ? 0.4569 0.2778 0.2544 0.0435  -0.0014 0.0291  230 LEU   B CG  
3880 C CD1 . LEU   B 208 ? 0.4877 0.3180 0.2762 0.0521  -0.0120 0.0310  230 LEU   B CD1 
3881 C CD2 . LEU   B 208 ? 0.4564 0.2500 0.2810 0.0106  0.0084  0.0455  230 LEU   B CD2 
3882 N N   . ALA   B 209 ? 0.4143 0.3141 0.2022 0.0557  -0.0219 -0.0097 231 ALA   B N   
3883 C CA  . ALA   B 209 ? 0.4149 0.3031 0.2100 0.0466  -0.0152 -0.0093 231 ALA   B CA  
3884 C C   . ALA   B 209 ? 0.4424 0.3178 0.2096 0.0279  -0.0048 -0.0009 231 ALA   B C   
3885 O O   . ALA   B 209 ? 0.4790 0.3127 0.2212 0.0217  0.0051  0.0247  231 ALA   B O   
3886 C CB  . ALA   B 209 ? 0.4247 0.3232 0.2170 0.0455  -0.0179 -0.0191 231 ALA   B CB  
3887 N N   . ALA   B 210 ? 0.4326 0.3035 0.2069 0.0261  0.0064  0.0058  232 ALA   B N   
3888 C CA  . ALA   B 210 ? 0.4677 0.2949 0.1781 0.0190  0.0145  0.0001  232 ALA   B CA  
3889 C C   . ALA   B 210 ? 0.4920 0.2761 0.1966 0.0132  0.0069  0.0288  232 ALA   B C   
3890 O O   . ALA   B 210 ? 0.4618 0.2540 0.2063 0.0067  -0.0072 0.0177  232 ALA   B O   
3891 C CB  . ALA   B 210 ? 0.4484 0.2737 0.1606 0.0251  0.0230  -0.0114 232 ALA   B CB  
3892 N N   . THR   B 211 ? 0.5243 0.2682 0.2121 0.0079  0.0001  0.0194  233 THR   B N   
3893 C CA  . THR   B 211 ? 0.5444 0.3111 0.2160 0.0247  0.0034  0.0290  233 THR   B CA  
3894 C C   . THR   B 211 ? 0.5615 0.3406 0.2216 -0.0028 -0.0150 0.0347  233 THR   B C   
3895 O O   . THR   B 211 ? 0.6034 0.2965 0.2644 -0.0217 -0.0419 0.0619  233 THR   B O   
3896 C CB  . THR   B 211 ? 0.5581 0.3188 0.2603 0.0470  0.0053  0.0203  233 THR   B CB  
3897 O OG1 . THR   B 211 ? 0.5501 0.3044 0.2062 0.0699  0.0126  -0.0139 233 THR   B OG1 
3898 C CG2 . THR   B 211 ? 0.5421 0.3161 0.2694 0.0688  0.0040  0.0302  233 THR   B CG2 
3899 N N   . LEU   B 212 ? 0.5823 0.3306 0.2127 0.0116  -0.0274 0.0193  234 LEU   B N   
3900 C CA  . LEU   B 212 ? 0.5822 0.3625 0.2087 -0.0017 -0.0268 -0.0010 234 LEU   B CA  
3901 C C   . LEU   B 212 ? 0.6367 0.3952 0.2230 -0.0014 -0.0349 -0.0238 234 LEU   B C   
3902 O O   . LEU   B 212 ? 0.6843 0.4334 0.2263 0.0243  -0.0471 -0.0994 234 LEU   B O   
3903 C CB  . LEU   B 212 ? 0.5589 0.3782 0.2381 -0.0074 -0.0428 0.0067  234 LEU   B CB  
3904 C CG  . LEU   B 212 ? 0.5134 0.3509 0.2537 -0.0288 -0.0604 0.0066  234 LEU   B CG  
3905 C CD1 . LEU   B 212 ? 0.5293 0.3747 0.2751 -0.0231 -0.0783 0.0235  234 LEU   B CD1 
3906 C CD2 . LEU   B 212 ? 0.4969 0.3546 0.2394 -0.0236 -0.0769 0.0104  234 LEU   B CD2 
3907 N N   . ASP   B 213 ? 0.6798 0.3810 0.2522 -0.0061 -0.0363 -0.0475 235 ASP   B N   
3908 C CA  . ASP   B 213 ? 0.7009 0.3675 0.2882 -0.0019 -0.0438 -0.0496 235 ASP   B CA  
3909 C C   . ASP   B 213 ? 0.6879 0.3207 0.2747 -0.0046 -0.0865 -0.0251 235 ASP   B C   
3910 O O   . ASP   B 213 ? 0.7182 0.3020 0.3308 -0.0350 -0.1003 -0.0458 235 ASP   B O   
3911 C CB  . ASP   B 213 ? 0.7365 0.4160 0.2966 0.0056  -0.0098 -0.0652 235 ASP   B CB  
3912 C CG  . ASP   B 213 ? 0.7535 0.4337 0.3025 0.0467  0.0147  -0.0423 235 ASP   B CG  
3913 O OD1 . ASP   B 213 ? 0.7935 0.3429 0.2802 0.0152  0.0094  -0.0145 235 ASP   B OD1 
3914 O OD2 . ASP   B 213 ? 0.7876 0.5371 0.3645 0.0788  0.0546  -0.0352 235 ASP   B OD2 
3915 N N   . ASN   B 214 ? 0.6530 0.3025 0.2337 -0.0233 -0.1016 -0.0075 236 ASN   B N   
3916 C CA  . ASN   B 214 ? 0.6572 0.3324 0.2462 -0.0218 -0.1098 -0.0046 236 ASN   B CA  
3917 C C   . ASN   B 214 ? 0.6812 0.3208 0.2374 -0.0268 -0.1066 -0.0034 236 ASN   B C   
3918 O O   . ASN   B 214 ? 0.7082 0.3133 0.2682 -0.0501 -0.1241 -0.0168 236 ASN   B O   
3919 C CB  . ASN   B 214 ? 0.6588 0.3348 0.2673 -0.0285 -0.1049 -0.0077 236 ASN   B CB  
3920 C CG  . ASN   B 214 ? 0.6664 0.3460 0.2800 -0.0414 -0.1133 -0.0016 236 ASN   B CG  
3921 O OD1 . ASN   B 214 ? 0.6175 0.3458 0.2951 -0.0930 -0.1191 0.0174  236 ASN   B OD1 
3922 N ND2 . ASN   B 214 ? 0.6898 0.3900 0.3072 -0.0238 -0.1183 -0.0099 236 ASN   B ND2 
3923 N N   . THR   B 215 ? 0.6545 0.3284 0.2648 -0.0107 -0.1088 -0.0170 237 THR   B N   
3924 C CA  . THR   B 215 ? 0.6729 0.3514 0.2505 0.0041  -0.0950 -0.0257 237 THR   B CA  
3925 C C   . THR   B 215 ? 0.6292 0.3120 0.2365 0.0003  -0.0678 -0.0078 237 THR   B C   
3926 O O   . THR   B 215 ? 0.6006 0.3049 0.2210 -0.0037 -0.0620 0.0183  237 THR   B O   
3927 C CB  . THR   B 215 ? 0.6992 0.3738 0.2521 0.0376  -0.1038 -0.0771 237 THR   B CB  
3928 O OG1 . THR   B 215 ? 0.7809 0.3816 0.2626 0.0643  -0.1129 -0.1201 237 THR   B OG1 
3929 C CG2 . THR   B 215 ? 0.7106 0.4254 0.2958 0.0612  -0.0797 -0.0656 237 THR   B CG2 
3930 N N   . LEU   B 216 ? 0.6214 0.3059 0.2227 -0.0054 -0.0611 -0.0128 238 LEU   B N   
3931 C CA  . LEU   B 216 ? 0.6000 0.2756 0.2231 0.0032  -0.0550 0.0025  238 LEU   B CA  
3932 C C   . LEU   B 216 ? 0.6147 0.2809 0.2367 0.0395  -0.0532 -0.0176 238 LEU   B C   
3933 O O   . LEU   B 216 ? 0.6360 0.2750 0.2687 0.0347  -0.1142 0.0131  238 LEU   B O   
3934 C CB  . LEU   B 216 ? 0.5773 0.2528 0.2395 -0.0260 -0.0333 -0.0086 238 LEU   B CB  
3935 C CG  . LEU   B 216 ? 0.5479 0.2658 0.2533 -0.0383 -0.0178 -0.0231 238 LEU   B CG  
3936 C CD1 . LEU   B 216 ? 0.5533 0.2937 0.2780 -0.0490 -0.0180 -0.0132 238 LEU   B CD1 
3937 C CD2 . LEU   B 216 ? 0.5483 0.2677 0.2563 -0.0463 -0.0118 -0.0123 238 LEU   B CD2 
3938 N N   . LYS   B 217 ? 0.6060 0.2785 0.2233 0.0633  -0.0443 -0.0132 239 LYS   B N   
3939 C CA  . LYS   B 217 ? 0.6270 0.3027 0.2427 0.0789  -0.0456 -0.0181 239 LYS   B CA  
3940 C C   . LYS   B 217 ? 0.6297 0.2805 0.2377 0.1116  -0.0550 -0.0125 239 LYS   B C   
3941 O O   . LYS   B 217 ? 0.6015 0.2644 0.1816 0.1499  -0.0482 -0.0050 239 LYS   B O   
3942 C CB  . LYS   B 217 ? 0.6352 0.3477 0.2345 0.0586  -0.0226 0.0082  239 LYS   B CB  
3943 C CG  . LYS   B 217 ? 0.6373 0.3775 0.2741 0.0405  -0.0300 -0.0248 239 LYS   B CG  
3944 C CD  . LYS   B 217 ? 0.6567 0.3775 0.3244 0.0396  -0.0048 0.0252  239 LYS   B CD  
3945 N N   . LEU   B 218 ? 0.6349 0.2758 0.2257 0.1233  -0.0679 -0.0212 240 LEU   B N   
3946 C CA  . LEU   B 218 ? 0.6469 0.3061 0.2240 0.1390  -0.0539 -0.0419 240 LEU   B CA  
3947 C C   . LEU   B 218 ? 0.6412 0.3286 0.2516 0.1658  -0.0566 -0.0490 240 LEU   B C   
3948 O O   . LEU   B 218 ? 0.6454 0.3480 0.3019 0.1641  -0.0390 -0.0640 240 LEU   B O   
3949 C CB  . LEU   B 218 ? 0.6672 0.2925 0.2189 0.1617  -0.0524 -0.0248 240 LEU   B CB  
3950 C CG  . LEU   B 218 ? 0.6771 0.3182 0.2118 0.1644  -0.0460 0.0053  240 LEU   B CG  
3951 C CD1 . LEU   B 218 ? 0.6667 0.3226 0.2063 0.1677  -0.0523 0.0089  240 LEU   B CD1 
3952 C CD2 . LEU   B 218 ? 0.7139 0.3339 0.2115 0.1735  -0.0333 0.0229  240 LEU   B CD2 
3953 N N   . TRP   B 219 ? 0.6289 0.2933 0.2524 0.1889  -0.0487 -0.0547 241 TRP   B N   
3954 C CA  . TRP   B 219 ? 0.6417 0.3542 0.2890 0.1972  -0.0247 -0.0514 241 TRP   B CA  
3955 C C   . TRP   B 219 ? 0.6402 0.3688 0.3132 0.2158  -0.0362 -0.0509 241 TRP   B C   
3956 O O   . TRP   B 219 ? 0.6185 0.3408 0.3247 0.2496  -0.0352 -0.0623 241 TRP   B O   
3957 C CB  . TRP   B 219 ? 0.6464 0.3761 0.3177 0.2140  -0.0191 -0.0309 241 TRP   B CB  
3958 C CG  . TRP   B 219 ? 0.6704 0.4014 0.3103 0.2156  0.0068  -0.0165 241 TRP   B CG  
3959 C CD1 . TRP   B 219 ? 0.6817 0.3794 0.3316 0.2158  0.0215  -0.0076 241 TRP   B CD1 
3960 C CD2 . TRP   B 219 ? 0.7035 0.4585 0.3240 0.2391  0.0236  0.0047  241 TRP   B CD2 
3961 N NE1 . TRP   B 219 ? 0.7022 0.4191 0.3315 0.2026  0.0350  0.0063  241 TRP   B NE1 
3962 C CE2 . TRP   B 219 ? 0.7030 0.4587 0.3659 0.2334  0.0247  0.0029  241 TRP   B CE2 
3963 C CE3 . TRP   B 219 ? 0.7309 0.5057 0.3764 0.2528  0.0183  0.0054  241 TRP   B CE3 
3964 C CZ2 . TRP   B 219 ? 0.7462 0.5312 0.3742 0.2365  0.0304  0.0118  241 TRP   B CZ2 
3965 C CZ3 . TRP   B 219 ? 0.7537 0.5575 0.3782 0.2536  0.0243  0.0319  241 TRP   B CZ3 
3966 C CH2 . TRP   B 219 ? 0.7412 0.5578 0.3960 0.2423  0.0077  0.0124  241 TRP   B CH2 
3967 N N   . ASP   B 220 ? 0.6572 0.4140 0.3712 0.2348  -0.0535 -0.0316 242 ASP   B N   
3968 C CA  . ASP   B 220 ? 0.6718 0.5023 0.4479 0.2447  -0.0740 -0.0129 242 ASP   B CA  
3969 C C   . ASP   B 220 ? 0.6699 0.5494 0.4666 0.2313  -0.0665 -0.0040 242 ASP   B C   
3970 O O   . ASP   B 220 ? 0.6588 0.5563 0.4698 0.2101  -0.1207 -0.0393 242 ASP   B O   
3971 C CB  . ASP   B 220 ? 0.6967 0.5297 0.4456 0.2579  -0.0794 -0.0056 242 ASP   B CB  
3972 C CG  . ASP   B 220 ? 0.7234 0.5831 0.4538 0.2503  -0.0971 -0.0025 242 ASP   B CG  
3973 O OD1 . ASP   B 220 ? 0.7508 0.6199 0.5005 0.2524  -0.0712 -0.0318 242 ASP   B OD1 
3974 O OD2 . ASP   B 220 ? 0.7761 0.6649 0.4569 0.2543  -0.1433 0.0196  242 ASP   B OD2 
3975 N N   . TYR   B 221 ? 0.7001 0.6096 0.5267 0.2261  -0.0247 -0.0297 243 TYR   B N   
3976 C CA  . TYR   B 221 ? 0.7230 0.6699 0.5009 0.2452  0.0093  -0.0395 243 TYR   B CA  
3977 C C   . TYR   B 221 ? 0.7415 0.7664 0.6257 0.2420  0.0284  -0.0712 243 TYR   B C   
3978 O O   . TYR   B 221 ? 0.7713 0.8001 0.7032 0.2641  0.0636  -0.0428 243 TYR   B O   
3979 C CB  . TYR   B 221 ? 0.6989 0.6508 0.4498 0.2393  0.0191  -0.0294 243 TYR   B CB  
3980 C CG  . TYR   B 221 ? 0.6858 0.6435 0.4293 0.2287  0.0715  -0.0165 243 TYR   B CG  
3981 C CD1 . TYR   B 221 ? 0.6301 0.6208 0.3934 0.2329  0.0951  -0.0059 243 TYR   B CD1 
3982 C CD2 . TYR   B 221 ? 0.6793 0.6703 0.4527 0.1939  0.0787  -0.0317 243 TYR   B CD2 
3983 C CE1 . TYR   B 221 ? 0.6315 0.6706 0.4294 0.2192  0.0800  -0.0032 243 TYR   B CE1 
3984 C CE2 . TYR   B 221 ? 0.6913 0.7036 0.4463 0.1813  0.0679  0.0020  243 TYR   B CE2 
3985 C CZ  . TYR   B 221 ? 0.6392 0.7217 0.4272 0.1885  0.0616  0.0123  243 TYR   B CZ  
3986 O OH  . TYR   B 221 ? 0.5287 0.7134 0.3686 0.2015  0.0587  0.0630  243 TYR   B OH  
3987 N N   . SER   B 222 ? 0.7599 0.7738 0.6026 0.2548  0.0045  -0.0705 244 SER   B N   
3988 C CA  . SER   B 222 ? 0.7733 0.8514 0.6355 0.2160  0.0337  -0.1267 244 SER   B CA  
3989 C C   . SER   B 222 ? 0.7766 0.8954 0.7196 0.2235  0.0626  -0.1690 244 SER   B C   
3990 O O   . SER   B 222 ? 0.8206 0.9446 0.6548 0.2282  0.1093  -0.2137 244 SER   B O   
3991 C CB  . SER   B 222 ? 0.8260 0.8602 0.5812 0.1770  0.0105  -0.1414 244 SER   B CB  
3992 N N   . LYS   B 223 ? 0.7914 0.8843 0.7628 0.2502  0.0744  -0.1871 245 LYS   B N   
3993 C CA  . LYS   B 223 ? 0.7789 0.9374 0.7368 0.2347  0.0593  -0.2061 245 LYS   B CA  
3994 C C   . LYS   B 223 ? 0.7249 0.9695 0.7792 0.2623  0.0463  -0.1921 245 LYS   B C   
3995 O O   . LYS   B 223 ? 0.7774 1.0395 0.7827 0.2414  -0.0037 -0.2484 245 LYS   B O   
3996 C CB  . LYS   B 223 ? 0.8104 0.8601 0.7142 0.2361  0.0905  -0.2561 245 LYS   B CB  
3997 N N   . GLY   B 224 ? 0.7302 0.9362 0.7228 0.2487  -0.0116 -0.1301 246 GLY   B N   
3998 C CA  . GLY   B 224 ? 0.6615 0.8460 0.6657 0.2630  0.0054  -0.1222 246 GLY   B CA  
3999 C C   . GLY   B 224 ? 0.6829 0.8401 0.5215 0.2719  -0.0059 -0.0982 246 GLY   B C   
4000 O O   . GLY   B 224 ? 0.7321 0.8968 0.5519 0.2558  -0.0117 -0.0681 246 GLY   B O   
4001 N N   . LYS   B 225 ? 0.6700 0.7226 0.4268 0.2778  -0.0658 -0.0786 247 LYS   B N   
4002 C CA  . LYS   B 225 ? 0.6686 0.6477 0.3829 0.3069  -0.0411 -0.0676 247 LYS   B CA  
4003 C C   . LYS   B 225 ? 0.6828 0.5529 0.3721 0.3415  -0.0516 -0.0737 247 LYS   B C   
4004 O O   . LYS   B 225 ? 0.7005 0.5126 0.4042 0.3687  -0.0276 -0.0876 247 LYS   B O   
4005 C CB  . LYS   B 225 ? 0.5771 0.6547 0.4023 0.3344  -0.0552 -0.0780 247 LYS   B CB  
4006 N N   . CYS   B 226 ? 0.7346 0.5605 0.4028 0.2888  -0.0344 -0.0892 248 CYS   B N   
4007 C CA  . CYS   B 226 ? 0.7626 0.5050 0.3919 0.2706  -0.0383 -0.0898 248 CYS   B CA  
4008 C C   . CYS   B 226 ? 0.8388 0.4528 0.3800 0.2638  -0.0287 -0.1039 248 CYS   B C   
4009 O O   . CYS   B 226 ? 0.8626 0.4718 0.3710 0.2744  -0.0230 -0.1157 248 CYS   B O   
4010 C CB  . CYS   B 226 ? 0.7274 0.4693 0.3566 0.2508  -0.0426 -0.0874 248 CYS   B CB  
4011 S SG  . CYS   B 226 ? 0.7332 0.5032 0.3856 0.1995  -0.0407 -0.0966 248 CYS   B SG  
4012 N N   . LEU   B 227 ? 0.8499 0.3816 0.3465 0.2739  -0.0276 -0.1338 249 LEU   B N   
4013 C CA  . LEU   B 227 ? 0.8698 0.3922 0.3766 0.2466  -0.0635 -0.1193 249 LEU   B CA  
4014 C C   . LEU   B 227 ? 0.8940 0.3377 0.4002 0.2408  -0.0689 -0.1154 249 LEU   B C   
4015 O O   . LEU   B 227 ? 0.9294 0.3004 0.4423 0.3142  -0.0810 -0.0741 249 LEU   B O   
4016 C CB  . LEU   B 227 ? 0.8901 0.4101 0.3655 0.2466  -0.0565 -0.1090 249 LEU   B CB  
4017 C CG  . LEU   B 227 ? 0.9079 0.4246 0.4047 0.2413  -0.0584 -0.0946 249 LEU   B CG  
4018 C CD1 . LEU   B 227 ? 0.9407 0.4545 0.4055 0.2316  -0.0744 -0.0704 249 LEU   B CD1 
4019 C CD2 . LEU   B 227 ? 0.9235 0.3951 0.4327 0.2458  -0.0843 -0.1008 249 LEU   B CD2 
4020 N N   . LYS   B 228 ? 0.8448 0.3076 0.3262 0.2086  -0.0931 -0.0990 250 LYS   B N   
4021 C CA  . LYS   B 228 ? 0.8626 0.3221 0.3445 0.1660  -0.0967 -0.0732 250 LYS   B CA  
4022 C C   . LYS   B 228 ? 0.8601 0.3259 0.2986 0.1402  -0.0981 -0.0692 250 LYS   B C   
4023 O O   . LYS   B 228 ? 0.8801 0.3355 0.2798 0.1434  -0.0954 -0.0956 250 LYS   B O   
4024 C CB  . LYS   B 228 ? 0.8445 0.3405 0.3346 0.1582  -0.1028 -0.0654 250 LYS   B CB  
4025 C CG  . LYS   B 228 ? 0.8685 0.3716 0.3750 0.1378  -0.1247 -0.0416 250 LYS   B CG  
4026 C CD  . LYS   B 228 ? 0.8807 0.3675 0.3961 0.1385  -0.1252 -0.0184 250 LYS   B CD  
4027 C CE  . LYS   B 228 ? 0.8917 0.3927 0.3787 0.1378  -0.1274 -0.0390 250 LYS   B CE  
4028 N NZ  . LYS   B 228 ? 0.9172 0.4064 0.3946 0.1230  -0.1324 -0.0320 250 LYS   B NZ  
4029 N N   . THR   B 229 ? 0.8423 0.3285 0.3347 0.1080  -0.0645 -0.0388 251 THR   B N   
4030 C CA  . THR   B 229 ? 0.8130 0.3492 0.2733 0.0650  -0.0672 -0.0276 251 THR   B CA  
4031 C C   . THR   B 229 ? 0.8041 0.2833 0.2925 0.0555  -0.0574 -0.0023 251 THR   B C   
4032 O O   . THR   B 229 ? 0.8224 0.2567 0.2922 0.0359  -0.0774 0.0071  251 THR   B O   
4033 C CB  . THR   B 229 ? 0.8346 0.4374 0.3104 0.0754  -0.0366 -0.0472 251 THR   B CB  
4034 O OG1 . THR   B 229 ? 0.8586 0.4978 0.3147 0.0770  -0.0314 -0.0999 251 THR   B OG1 
4035 C CG2 . THR   B 229 ? 0.8451 0.4705 0.3412 0.0772  -0.0546 -0.0367 251 THR   B CG2 
4036 N N   . TYR   B 230 ? 0.7630 0.2245 0.2506 0.0283  -0.0686 -0.0141 252 TYR   B N   
4037 C CA  . TYR   B 230 ? 0.7551 0.2342 0.2436 0.0120  -0.0616 0.0075  252 TYR   B CA  
4038 C C   . TYR   B 230 ? 0.7246 0.2328 0.2402 0.0156  -0.0547 -0.0018 252 TYR   B C   
4039 O O   . TYR   B 230 ? 0.7059 0.2358 0.2254 0.0004  -0.0354 0.0229  252 TYR   B O   
4040 C CB  . TYR   B 230 ? 0.7255 0.2218 0.2472 -0.0089 -0.0653 0.0011  252 TYR   B CB  
4041 C CG  . TYR   B 230 ? 0.7199 0.2409 0.2522 -0.0043 -0.0857 0.0051  252 TYR   B CG  
4042 C CD1 . TYR   B 230 ? 0.6969 0.2668 0.2487 0.0071  -0.0937 0.0206  252 TYR   B CD1 
4043 C CD2 . TYR   B 230 ? 0.7023 0.2729 0.2550 -0.0117 -0.0940 0.0058  252 TYR   B CD2 
4044 C CE1 . TYR   B 230 ? 0.7015 0.2868 0.2359 0.0008  -0.0950 0.0046  252 TYR   B CE1 
4045 C CE2 . TYR   B 230 ? 0.7126 0.2636 0.2320 0.0166  -0.0949 0.0088  252 TYR   B CE2 
4046 C CZ  . TYR   B 230 ? 0.6988 0.2424 0.2314 0.0201  -0.1098 0.0047  252 TYR   B CZ  
4047 O OH  . TYR   B 230 ? 0.7235 0.2969 0.2761 0.0467  -0.1371 -0.0233 252 TYR   B OH  
4048 N N   . THR   B 231 ? 0.7361 0.2888 0.2814 0.0032  -0.0676 -0.0300 253 THR   B N   
4049 C CA  . THR   B 231 ? 0.7380 0.2973 0.2930 -0.0085 -0.0742 -0.0292 253 THR   B CA  
4050 C C   . THR   B 231 ? 0.7368 0.2887 0.3054 -0.0454 -0.1091 -0.0260 253 THR   B C   
4051 O O   . THR   B 231 ? 0.7089 0.3042 0.3086 -0.0599 -0.1280 -0.0131 253 THR   B O   
4052 C CB  . THR   B 231 ? 0.7805 0.3400 0.2985 -0.0006 -0.0693 -0.0298 253 THR   B CB  
4053 O OG1 . THR   B 231 ? 0.8107 0.3145 0.3298 0.0566  -0.0747 -0.0131 253 THR   B OG1 
4054 C CG2 . THR   B 231 ? 0.7743 0.3863 0.3338 0.0125  -0.0635 -0.0414 253 THR   B CG2 
4055 N N   . GLY   B 232 ? 0.7107 0.2766 0.2980 -0.0889 -0.1209 -0.0134 254 GLY   B N   
4056 C CA  . GLY   B 232 ? 0.7307 0.3257 0.3349 -0.0960 -0.1173 0.0085  254 GLY   B CA  
4057 C C   . GLY   B 232 ? 0.6991 0.2933 0.3470 -0.1049 -0.1403 0.0188  254 GLY   B C   
4058 O O   . GLY   B 232 ? 0.7133 0.3344 0.3637 -0.1009 -0.1466 0.0287  254 GLY   B O   
4059 N N   . HIS   B 233 ? 0.7028 0.3275 0.3583 -0.1283 -0.1348 0.0029  255 HIS   B N   
4060 C CA  . HIS   B 233 ? 0.6767 0.3170 0.3248 -0.1256 -0.1353 0.0352  255 HIS   B CA  
4061 C C   . HIS   B 233 ? 0.6962 0.3586 0.2924 -0.1477 -0.1392 0.0188  255 HIS   B C   
4062 O O   . HIS   B 233 ? 0.7923 0.3502 0.2644 -0.1745 -0.1016 0.0296  255 HIS   B O   
4063 C CB  . HIS   B 233 ? 0.6854 0.3168 0.2821 -0.0964 -0.1371 0.0501  255 HIS   B CB  
4064 C CG  . HIS   B 233 ? 0.6760 0.2558 0.2823 -0.1065 -0.1448 0.0754  255 HIS   B CG  
4065 N ND1 . HIS   B 233 ? 0.7039 0.2567 0.3041 -0.0788 -0.1290 0.0641  255 HIS   B ND1 
4066 C CD2 . HIS   B 233 ? 0.6974 0.1834 0.2721 -0.0986 -0.1454 0.0994  255 HIS   B CD2 
4067 C CE1 . HIS   B 233 ? 0.6512 0.2066 0.2853 -0.1161 -0.1708 0.0563  255 HIS   B CE1 
4068 N NE2 . HIS   B 233 ? 0.6678 0.2726 0.3267 -0.0907 -0.1364 0.0688  255 HIS   B NE2 
4069 N N   . LYS   B 234 ? 0.6581 0.3674 0.2803 -0.1468 -0.1363 0.0335  256 LYS   B N   
4070 C CA  . LYS   B 234 ? 0.6569 0.3690 0.3031 -0.1426 -0.1248 0.0571  256 LYS   B CA  
4071 C C   . LYS   B 234 ? 0.5720 0.3558 0.2789 -0.1215 -0.1285 0.0632  256 LYS   B C   
4072 O O   . LYS   B 234 ? 0.5510 0.3642 0.2571 -0.1676 -0.1308 0.0788  256 LYS   B O   
4073 C CB  . LYS   B 234 ? 0.6854 0.4227 0.3334 -0.1307 -0.1101 0.0608  256 LYS   B CB  
4074 C CG  . LYS   B 234 ? 0.7565 0.4931 0.3378 -0.1154 -0.1096 0.0588  256 LYS   B CG  
4075 C CD  . LYS   B 234 ? 0.8105 0.5822 0.3734 -0.1166 -0.1053 0.0429  256 LYS   B CD  
4076 C CE  . LYS   B 234 ? 0.8609 0.6477 0.3584 -0.1260 -0.1033 0.0370  256 LYS   B CE  
4077 N NZ  . LYS   B 234 ? 0.8383 0.7338 0.3788 -0.1417 -0.1070 0.0639  256 LYS   B NZ  
4078 N N   . ASN   B 235 ? 0.5578 0.3122 0.2514 -0.1072 -0.1114 0.0554  257 ASN   B N   
4079 C CA  . ASN   B 235 ? 0.5328 0.3055 0.2235 -0.0916 -0.0922 0.0269  257 ASN   B CA  
4080 C C   . ASN   B 235 ? 0.5472 0.3423 0.2034 -0.0679 -0.0840 0.0021  257 ASN   B C   
4081 O O   . ASN   B 235 ? 0.5554 0.3759 0.2113 -0.0691 -0.0784 -0.0212 257 ASN   B O   
4082 C CB  . ASN   B 235 ? 0.5159 0.2663 0.1994 -0.0888 -0.0832 0.0109  257 ASN   B CB  
4083 C CG  . ASN   B 235 ? 0.5255 0.2777 0.2262 -0.0930 -0.0765 0.0058  257 ASN   B CG  
4084 O OD1 . ASN   B 235 ? 0.5059 0.2388 0.2352 -0.0875 -0.0670 0.0223  257 ASN   B OD1 
4085 N ND2 . ASN   B 235 ? 0.5006 0.2645 0.2292 -0.0821 -0.0681 -0.0268 257 ASN   B ND2 
4086 N N   . GLU   B 236 ? 0.5455 0.3573 0.2346 -0.0406 -0.0767 0.0118  258 GLU   B N   
4087 C CA  . GLU   B 236 ? 0.5548 0.3758 0.2324 -0.0429 -0.0620 0.0118  258 GLU   B CA  
4088 C C   . GLU   B 236 ? 0.5006 0.3645 0.1946 -0.0352 -0.0426 0.0387  258 GLU   B C   
4089 O O   . GLU   B 236 ? 0.5122 0.3649 0.1854 -0.0467 -0.0207 0.0496  258 GLU   B O   
4090 C CB  . GLU   B 236 ? 0.6235 0.3902 0.2815 -0.0268 -0.0698 -0.0454 258 GLU   B CB  
4091 C CG  . GLU   B 236 ? 0.6851 0.4105 0.3292 -0.0198 -0.0987 -0.0714 258 GLU   B CG  
4092 C CD  . GLU   B 236 ? 0.7526 0.4116 0.3625 0.0113  -0.1425 -0.1091 258 GLU   B CD  
4093 O OE1 . GLU   B 236 ? 0.7944 0.5067 0.4623 -0.0322 -0.2148 -0.1598 258 GLU   B OE1 
4094 O OE2 . GLU   B 236 ? 0.8033 0.3354 0.3292 0.0433  -0.1489 -0.0754 258 GLU   B OE2 
4095 N N   . LYS   B 237 ? 0.4427 0.4007 0.1759 -0.0472 -0.0499 0.0494  259 LYS   B N   
4096 C CA  . LYS   B 237 ? 0.4202 0.4000 0.2464 -0.0581 -0.0275 0.0443  259 LYS   B CA  
4097 C C   . LYS   B 237 ? 0.3908 0.3865 0.2276 -0.0643 0.0059  0.0333  259 LYS   B C   
4098 O O   . LYS   B 237 ? 0.3948 0.3722 0.2026 -0.0547 0.0397  0.0003  259 LYS   B O   
4099 C CB  . LYS   B 237 ? 0.4228 0.4538 0.3286 -0.0424 -0.0348 0.0690  259 LYS   B CB  
4100 C CG  . LYS   B 237 ? 0.4452 0.5225 0.4364 -0.0403 -0.0251 0.0824  259 LYS   B CG  
4101 C CD  . LYS   B 237 ? 0.4396 0.5692 0.4910 -0.0172 -0.0518 0.0989  259 LYS   B CD  
4102 C CE  . LYS   B 237 ? 0.4466 0.5936 0.5759 -0.0153 -0.0714 0.1046  259 LYS   B CE  
4103 N NZ  . LYS   B 237 ? 0.4296 0.5926 0.5969 -0.0286 -0.0906 0.1065  259 LYS   B NZ  
4104 N N   . TYR   B 238 ? 0.3702 0.3575 0.2266 -0.0762 0.0058  0.0314  260 TYR   B N   
4105 C CA  . TYR   B 238 ? 0.3410 0.3678 0.2347 -0.0747 -0.0017 0.0273  260 TYR   B CA  
4106 C C   . TYR   B 238 ? 0.3214 0.3518 0.2221 -0.0786 -0.0024 0.0132  260 TYR   B C   
4107 O O   . TYR   B 238 ? 0.3381 0.3726 0.2269 -0.0729 0.0001  0.0000  260 TYR   B O   
4108 C CB  . TYR   B 238 ? 0.3236 0.3842 0.2481 -0.0851 -0.0136 0.0426  260 TYR   B CB  
4109 C CG  . TYR   B 238 ? 0.3234 0.4190 0.2578 -0.0772 -0.0184 0.0487  260 TYR   B CG  
4110 C CD1 . TYR   B 238 ? 0.3278 0.4384 0.2560 -0.0755 -0.0241 0.0389  260 TYR   B CD1 
4111 C CD2 . TYR   B 238 ? 0.3464 0.4429 0.2796 -0.0684 -0.0405 0.0523  260 TYR   B CD2 
4112 C CE1 . TYR   B 238 ? 0.3406 0.4642 0.3075 -0.0616 -0.0130 0.0435  260 TYR   B CE1 
4113 C CE2 . TYR   B 238 ? 0.3646 0.4669 0.3155 -0.0527 -0.0430 0.0518  260 TYR   B CE2 
4114 C CZ  . TYR   B 238 ? 0.3525 0.4678 0.3216 -0.0552 -0.0334 0.0426  260 TYR   B CZ  
4115 O OH  . TYR   B 238 ? 0.3507 0.4679 0.4020 -0.0438 -0.0335 0.0816  260 TYR   B OH  
4116 N N   . CYS   B 239 ? 0.3010 0.3366 0.2009 -0.0637 -0.0029 0.0225  261 CYS   B N   
4117 C CA  . CYS   B 239 ? 0.2787 0.3020 0.1600 -0.0511 0.0237  0.0324  261 CYS   B CA  
4118 C C   . CYS   B 239 ? 0.2945 0.2865 0.1821 -0.0563 0.0311  0.0384  261 CYS   B C   
4119 O O   . CYS   B 239 ? 0.3085 0.2686 0.2044 -0.0436 0.0409  0.0387  261 CYS   B O   
4120 C CB  . CYS   B 239 ? 0.2571 0.3106 0.1666 -0.0427 0.0278  0.0316  261 CYS   B CB  
4121 S SG  . CYS   B 239 ? 0.2464 0.3229 0.1765 -0.0395 0.0376  0.0213  261 CYS   B SG  
4122 N N   . ILE   B 240 ? 0.3056 0.2780 0.1753 -0.0643 0.0136  0.0576  262 ILE   B N   
4123 C CA  . ILE   B 240 ? 0.3031 0.2884 0.1982 -0.0787 0.0016  0.0626  262 ILE   B CA  
4124 C C   . ILE   B 240 ? 0.2926 0.2807 0.2010 -0.0716 -0.0052 0.0790  262 ILE   B C   
4125 O O   . ILE   B 240 ? 0.3045 0.3036 0.2064 -0.0561 -0.0094 0.0817  262 ILE   B O   
4126 C CB  . ILE   B 240 ? 0.3440 0.2846 0.2128 -0.0784 -0.0116 0.0601  262 ILE   B CB  
4127 C CG1 . ILE   B 240 ? 0.3663 0.2996 0.2113 -0.0832 -0.0231 0.0619  262 ILE   B CG1 
4128 C CG2 . ILE   B 240 ? 0.3322 0.2874 0.2221 -0.0887 -0.0050 0.0676  262 ILE   B CG2 
4129 C CD1 . ILE   B 240 ? 0.3745 0.3175 0.2247 -0.0860 -0.0250 0.0435  262 ILE   B CD1 
4130 N N   . PHE   B 241 ? 0.2893 0.3361 0.2243 -0.0581 -0.0405 0.0611  263 PHE   B N   
4131 C CA  . PHE   B 241 ? 0.3029 0.3122 0.2094 -0.0493 -0.0172 0.0843  263 PHE   B CA  
4132 C C   . PHE   B 241 ? 0.3512 0.3109 0.2560 -0.0608 -0.0360 0.0782  263 PHE   B C   
4133 O O   . PHE   B 241 ? 0.4047 0.3755 0.3360 -0.0784 -0.0833 0.0902  263 PHE   B O   
4134 C CB  . PHE   B 241 ? 0.2696 0.3247 0.2150 -0.0523 -0.0155 0.0770  263 PHE   B CB  
4135 C CG  . PHE   B 241 ? 0.2303 0.3190 0.1800 -0.0469 0.0123  0.0648  263 PHE   B CG  
4136 C CD1 . PHE   B 241 ? 0.2114 0.3235 0.1784 -0.0407 0.0301  0.0651  263 PHE   B CD1 
4137 C CD2 . PHE   B 241 ? 0.2133 0.3241 0.1917 -0.0455 0.0126  0.0552  263 PHE   B CD2 
4138 C CE1 . PHE   B 241 ? 0.2020 0.3163 0.1933 -0.0407 0.0150  0.0418  263 PHE   B CE1 
4139 C CE2 . PHE   B 241 ? 0.2270 0.3327 0.1893 -0.0393 0.0000  0.0408  263 PHE   B CE2 
4140 C CZ  . PHE   B 241 ? 0.2210 0.3319 0.2038 -0.0354 0.0129  0.0362  263 PHE   B CZ  
4141 N N   . ALA   B 242 ? 0.3641 0.2789 0.2369 -0.0546 -0.0252 0.0629  264 ALA   B N   
4142 C CA  . ALA   B 242 ? 0.3793 0.2656 0.2216 -0.0594 -0.0225 0.0641  264 ALA   B CA  
4143 C C   . ALA   B 242 ? 0.3602 0.2408 0.2205 -0.0741 -0.0222 0.0537  264 ALA   B C   
4144 O O   . ALA   B 242 ? 0.3765 0.2365 0.2273 -0.0835 -0.0099 0.0673  264 ALA   B O   
4145 C CB  . ALA   B 242 ? 0.4099 0.2810 0.2335 -0.0580 -0.0260 0.0539  264 ALA   B CB  
4146 N N   . ASN   B 243 ? 0.3564 0.2367 0.2181 -0.0627 -0.0210 0.0536  265 ASN   B N   
4147 C CA  . ASN   B 243 ? 0.3427 0.2536 0.2136 -0.0584 -0.0143 0.0551  265 ASN   B CA  
4148 C C   . ASN   B 243 ? 0.3623 0.2499 0.2171 -0.0571 -0.0180 0.0410  265 ASN   B C   
4149 O O   . ASN   B 243 ? 0.3552 0.2700 0.2016 -0.0641 -0.0320 0.0468  265 ASN   B O   
4150 C CB  . ASN   B 243 ? 0.3590 0.2784 0.2485 -0.0482 0.0107  0.0515  265 ASN   B CB  
4151 C CG  . ASN   B 243 ? 0.3633 0.3104 0.2566 -0.0360 0.0323  0.0621  265 ASN   B CG  
4152 O OD1 . ASN   B 243 ? 0.3966 0.4528 0.3345 0.0074  0.0017  0.0506  265 ASN   B OD1 
4153 N ND2 . ASN   B 243 ? 0.3861 0.2699 0.2706 -0.0395 0.0677  0.0639  265 ASN   B ND2 
4154 N N   . PHE   B 244 ? 0.3772 0.2440 0.2011 -0.0466 -0.0120 0.0421  266 PHE   B N   
4155 C CA  . PHE   B 244 ? 0.3902 0.2325 0.1878 -0.0345 -0.0044 0.0302  266 PHE   B CA  
4156 C C   . PHE   B 244 ? 0.3955 0.2412 0.1919 -0.0527 0.0056  0.0254  266 PHE   B C   
4157 O O   . PHE   B 244 ? 0.3935 0.2633 0.2079 -0.0787 0.0147  -0.0040 266 PHE   B O   
4158 C CB  . PHE   B 244 ? 0.4126 0.2171 0.1927 -0.0263 -0.0160 0.0284  266 PHE   B CB  
4159 C CG  . PHE   B 244 ? 0.4183 0.2048 0.1907 -0.0038 -0.0104 0.0217  266 PHE   B CG  
4160 C CD1 . PHE   B 244 ? 0.4414 0.2293 0.2050 0.0001  0.0104  0.0383  266 PHE   B CD1 
4161 C CD2 . PHE   B 244 ? 0.4465 0.1947 0.2051 0.0000  -0.0015 0.0323  266 PHE   B CD2 
4162 C CE1 . PHE   B 244 ? 0.4583 0.2234 0.2140 0.0211  0.0090  0.0363  266 PHE   B CE1 
4163 C CE2 . PHE   B 244 ? 0.4565 0.1996 0.2275 0.0193  0.0086  0.0167  266 PHE   B CE2 
4164 C CZ  . PHE   B 244 ? 0.4636 0.2373 0.2008 0.0106  0.0130  0.0312  266 PHE   B CZ  
4165 N N   . SER   B 245 ? 0.3825 0.2501 0.1996 -0.0593 -0.0022 0.0309  267 SER   B N   
4166 C CA  . SER   B 245 ? 0.4002 0.2741 0.1847 -0.0552 -0.0048 0.0478  267 SER   B CA  
4167 C C   . SER   B 245 ? 0.4281 0.2594 0.2127 -0.0531 -0.0063 0.0585  267 SER   B C   
4168 O O   . SER   B 245 ? 0.4402 0.2585 0.2327 -0.0462 -0.0104 0.0481  267 SER   B O   
4169 C CB  . SER   B 245 ? 0.4016 0.2624 0.1982 -0.0692 -0.0013 0.0464  267 SER   B CB  
4170 O OG  . SER   B 245 ? 0.4240 0.2633 0.2310 -0.0883 0.0128  0.0583  267 SER   B OG  
4171 N N   . VAL   B 246 ? 0.4180 0.2644 0.2134 -0.0646 -0.0194 0.0594  268 VAL   B N   
4172 C CA  . VAL   B 246 ? 0.4291 0.2762 0.2235 -0.0726 -0.0260 0.0594  268 VAL   B CA  
4173 C C   . VAL   B 246 ? 0.4470 0.2952 0.2138 -0.0729 -0.0264 0.0729  268 VAL   B C   
4174 O O   . VAL   B 246 ? 0.4887 0.2749 0.2362 -0.0411 -0.0342 0.0754  268 VAL   B O   
4175 C CB  . VAL   B 246 ? 0.4070 0.3096 0.2388 -0.0650 -0.0271 0.0531  268 VAL   B CB  
4176 C CG1 . VAL   B 246 ? 0.3938 0.3230 0.2642 -0.0578 -0.0220 0.0485  268 VAL   B CG1 
4177 C CG2 . VAL   B 246 ? 0.3876 0.2902 0.2636 -0.0888 -0.0253 0.0418  268 VAL   B CG2 
4178 N N   . THR   B 247 ? 0.4553 0.3240 0.2039 -0.0808 -0.0134 0.0846  269 THR   B N   
4179 C CA  . THR   B 247 ? 0.4505 0.3732 0.2342 -0.0890 -0.0007 0.1073  269 THR   B CA  
4180 C C   . THR   B 247 ? 0.4818 0.3689 0.2273 -0.0800 -0.0034 0.1069  269 THR   B C   
4181 O O   . THR   B 247 ? 0.4763 0.3775 0.2500 -0.1178 0.0242  0.1266  269 THR   B O   
4182 C CB  . THR   B 247 ? 0.4346 0.3655 0.2442 -0.0843 0.0007  0.0977  269 THR   B CB  
4183 O OG1 . THR   B 247 ? 0.4228 0.3732 0.2439 -0.0652 -0.0250 0.1033  269 THR   B OG1 
4184 C CG2 . THR   B 247 ? 0.4438 0.3825 0.2822 -0.0866 -0.0191 0.0916  269 THR   B CG2 
4185 N N   . GLY   B 248 ? 0.4960 0.3904 0.2324 -0.0817 0.0138  0.1056  270 GLY   B N   
4186 C CA  . GLY   B 248 ? 0.5307 0.3740 0.2632 -0.0608 -0.0069 0.0939  270 GLY   B CA  
4187 C C   . GLY   B 248 ? 0.5513 0.3458 0.2605 -0.0669 -0.0085 0.1045  270 GLY   B C   
4188 O O   . GLY   B 248 ? 0.5518 0.3088 0.3004 -0.0447 0.0099  0.0761  270 GLY   B O   
4189 N N   . GLY   B 249 ? 0.5591 0.3283 0.2980 -0.0964 -0.0161 0.0939  271 GLY   B N   
4190 C CA  . GLY   B 249 ? 0.5861 0.3733 0.2813 -0.0912 -0.0202 0.0980  271 GLY   B CA  
4191 C C   . GLY   B 249 ? 0.6159 0.3241 0.2951 -0.0968 -0.0368 0.0985  271 GLY   B C   
4192 O O   . GLY   B 249 ? 0.6096 0.3298 0.2990 -0.1188 -0.0305 0.1110  271 GLY   B O   
4193 N N   . LYS   B 250 ? 0.6008 0.3088 0.3220 -0.0755 -0.0674 0.0896  272 LYS   B N   
4194 C CA  A LYS   B 250 ? 0.6177 0.3040 0.3142 -0.0670 -0.0718 0.0833  272 LYS   B CA  
4195 C CA  B LYS   B 250 ? 0.6248 0.2898 0.3146 -0.0665 -0.0700 0.0783  272 LYS   B CA  
4196 C C   . LYS   B 250 ? 0.6314 0.2885 0.3130 -0.0543 -0.0821 0.0563  272 LYS   B C   
4197 O O   . LYS   B 250 ? 0.6606 0.2794 0.2885 -0.0537 -0.0843 0.0484  272 LYS   B O   
4198 C CB  A LYS   B 250 ? 0.6186 0.3089 0.3269 -0.0567 -0.0801 0.0959  272 LYS   B CB  
4199 C CB  B LYS   B 250 ? 0.6329 0.2743 0.3331 -0.0551 -0.0740 0.0829  272 LYS   B CB  
4200 C CG  A LYS   B 250 ? 0.6209 0.3382 0.3371 -0.0537 -0.0894 0.1090  272 LYS   B CG  
4201 C CG  B LYS   B 250 ? 0.6448 0.2830 0.3435 -0.0513 -0.0807 0.0868  272 LYS   B CG  
4202 C CD  A LYS   B 250 ? 0.6117 0.3648 0.3411 -0.0407 -0.1022 0.1173  272 LYS   B CD  
4203 C CD  B LYS   B 250 ? 0.6481 0.2936 0.3585 -0.0384 -0.0914 0.0857  272 LYS   B CD  
4204 C CE  A LYS   B 250 ? 0.6107 0.4029 0.3493 -0.0416 -0.1075 0.1361  272 LYS   B CE  
4205 C CE  B LYS   B 250 ? 0.6572 0.3058 0.3665 -0.0379 -0.0937 0.0982  272 LYS   B CE  
4206 N NZ  A LYS   B 250 ? 0.6093 0.4405 0.3364 -0.0353 -0.1340 0.1493  272 LYS   B NZ  
4207 N NZ  B LYS   B 250 ? 0.6674 0.2944 0.3711 -0.0349 -0.0987 0.1034  272 LYS   B NZ  
4208 N N   . TRP   B 251 ? 0.6098 0.2535 0.2917 -0.0732 -0.0864 0.0378  273 TRP   B N   
4209 C CA  . TRP   B 251 ? 0.5865 0.2605 0.2867 -0.0776 -0.0831 0.0496  273 TRP   B CA  
4210 C C   . TRP   B 251 ? 0.5915 0.2219 0.2570 -0.0609 -0.0778 0.0414  273 TRP   B C   
4211 O O   . TRP   B 251 ? 0.5508 0.2210 0.2566 -0.0595 -0.0930 0.0861  273 TRP   B O   
4212 C CB  . TRP   B 251 ? 0.5957 0.3116 0.2990 -0.0864 -0.1042 0.0431  273 TRP   B CB  
4213 C CG  . TRP   B 251 ? 0.5888 0.3131 0.2902 -0.1165 -0.1150 0.0443  273 TRP   B CG  
4214 C CD1 . TRP   B 251 ? 0.5784 0.3258 0.3233 -0.1251 -0.0875 0.0523  273 TRP   B CD1 
4215 C CD2 . TRP   B 251 ? 0.6132 0.3161 0.3204 -0.1120 -0.0957 0.0553  273 TRP   B CD2 
4216 N NE1 . TRP   B 251 ? 0.6139 0.2856 0.3346 -0.1382 -0.0849 0.0511  273 TRP   B NE1 
4217 C CE2 . TRP   B 251 ? 0.6305 0.3152 0.3390 -0.1232 -0.0831 0.0445  273 TRP   B CE2 
4218 C CE3 . TRP   B 251 ? 0.6424 0.3197 0.3236 -0.1441 -0.0907 0.0429  273 TRP   B CE3 
4219 C CZ2 . TRP   B 251 ? 0.6495 0.3128 0.3392 -0.1324 -0.0785 0.0395  273 TRP   B CZ2 
4220 C CZ3 . TRP   B 251 ? 0.6537 0.3241 0.3381 -0.1291 -0.0809 0.0438  273 TRP   B CZ3 
4221 C CH2 . TRP   B 251 ? 0.6591 0.3132 0.3693 -0.1254 -0.0741 0.0514  273 TRP   B CH2 
4222 N N   . ILE   B 252 ? 0.5569 0.1843 0.2507 -0.0734 -0.0692 0.0372  274 ILE   B N   
4223 C CA  . ILE   B 252 ? 0.5313 0.2061 0.2538 -0.0553 -0.0445 0.0422  274 ILE   B CA  
4224 C C   . ILE   B 252 ? 0.5174 0.2403 0.2612 -0.1030 -0.0517 0.0434  274 ILE   B C   
4225 O O   . ILE   B 252 ? 0.5289 0.2437 0.2469 -0.1210 -0.0344 0.0186  274 ILE   B O   
4226 C CB  . ILE   B 252 ? 0.5336 0.2151 0.2493 -0.0337 -0.0434 0.0172  274 ILE   B CB  
4227 C CG1 . ILE   B 252 ? 0.5306 0.2471 0.2522 -0.0230 -0.0309 0.0067  274 ILE   B CG1 
4228 C CG2 . ILE   B 252 ? 0.5255 0.2040 0.2584 -0.0345 -0.0367 -0.0044 274 ILE   B CG2 
4229 C CD1 . ILE   B 252 ? 0.5161 0.2452 0.2342 -0.0030 -0.0399 0.0065  274 ILE   B CD1 
4230 N N   . VAL   B 253 ? 0.4882 0.2385 0.2663 -0.1071 -0.0565 0.0405  275 VAL   B N   
4231 C CA  . VAL   B 253 ? 0.4750 0.2582 0.2878 -0.1314 -0.0395 0.0563  275 VAL   B CA  
4232 C C   . VAL   B 253 ? 0.4683 0.2725 0.2844 -0.1302 -0.0606 0.0628  275 VAL   B C   
4233 O O   . VAL   B 253 ? 0.4686 0.2328 0.2961 -0.1427 -0.0446 0.0865  275 VAL   B O   
4234 C CB  . VAL   B 253 ? 0.4696 0.2569 0.2779 -0.1281 -0.0281 0.0743  275 VAL   B CB  
4235 C CG1 . VAL   B 253 ? 0.4624 0.2690 0.2809 -0.1332 -0.0328 0.0766  275 VAL   B CG1 
4236 C CG2 . VAL   B 253 ? 0.4469 0.2525 0.2770 -0.1389 -0.0124 0.0744  275 VAL   B CG2 
4237 N N   . SER   B 254 ? 0.4737 0.2665 0.2742 -0.1474 -0.0726 0.0508  276 SER   B N   
4238 C CA  . SER   B 254 ? 0.4566 0.2659 0.2663 -0.1379 -0.0668 0.0673  276 SER   B CA  
4239 C C   . SER   B 254 ? 0.4463 0.2950 0.2906 -0.1630 -0.0771 0.0767  276 SER   B C   
4240 O O   . SER   B 254 ? 0.4768 0.3240 0.2915 -0.1834 -0.0949 0.1054  276 SER   B O   
4241 C CB  . SER   B 254 ? 0.4665 0.2384 0.2920 -0.1217 -0.0583 0.0697  276 SER   B CB  
4242 O OG  . SER   B 254 ? 0.4783 0.2497 0.2776 -0.1180 -0.0423 0.0706  276 SER   B OG  
4243 N N   . GLY   B 255 ? 0.4090 0.3025 0.2753 -0.1505 -0.0863 0.0819  277 GLY   B N   
4244 C CA  . GLY   B 255 ? 0.4064 0.3269 0.2594 -0.1493 -0.0855 0.0713  277 GLY   B CA  
4245 C C   . GLY   B 255 ? 0.4243 0.3297 0.2665 -0.1563 -0.0876 0.0696  277 GLY   B C   
4246 O O   . GLY   B 255 ? 0.4300 0.3186 0.2180 -0.1487 -0.0868 0.0460  277 GLY   B O   
4247 N N   . SER   B 256 ? 0.4666 0.3360 0.2544 -0.1757 -0.1003 0.0745  278 SER   B N   
4248 C CA  . SER   B 256 ? 0.5056 0.3409 0.2657 -0.1793 -0.1093 0.0706  278 SER   B CA  
4249 C C   . SER   B 256 ? 0.5096 0.3787 0.2556 -0.1761 -0.1192 0.0714  278 SER   B C   
4250 O O   . SER   B 256 ? 0.4947 0.4277 0.2426 -0.1750 -0.0987 0.0900  278 SER   B O   
4251 C CB  . SER   B 256 ? 0.5335 0.3309 0.2533 -0.1631 -0.1160 0.0810  278 SER   B CB  
4252 O OG  . SER   B 256 ? 0.5572 0.3771 0.2828 -0.1402 -0.1062 0.0590  278 SER   B OG  
4253 N N   . GLU   B 257 ? 0.5240 0.4371 0.2647 -0.1718 -0.1071 0.0660  279 GLU   B N   
4254 C CA  . GLU   B 257 ? 0.4859 0.4366 0.2651 -0.1885 -0.1351 0.0666  279 GLU   B CA  
4255 C C   . GLU   B 257 ? 0.5291 0.4538 0.3078 -0.2256 -0.1496 0.0818  279 GLU   B C   
4256 O O   . GLU   B 257 ? 0.5174 0.5430 0.3156 -0.2121 -0.1228 0.0956  279 GLU   B O   
4257 C CB  . GLU   B 257 ? 0.4688 0.4307 0.2645 -0.1753 -0.1312 0.0525  279 GLU   B CB  
4258 C CG  . GLU   B 257 ? 0.4768 0.3957 0.2735 -0.1688 -0.1120 0.0700  279 GLU   B CG  
4259 C CD  . GLU   B 257 ? 0.4694 0.3802 0.2732 -0.1601 -0.1167 0.0701  279 GLU   B CD  
4260 O OE1 . GLU   B 257 ? 0.4410 0.3603 0.2606 -0.1675 -0.1583 0.0814  279 GLU   B OE1 
4261 O OE2 . GLU   B 257 ? 0.4379 0.3689 0.2938 -0.1469 -0.1057 0.0918  279 GLU   B OE2 
4262 N N   . ASP   B 258 ? 0.5284 0.4485 0.3184 -0.2522 -0.1685 0.0842  280 ASP   B N   
4263 C CA  . ASP   B 258 ? 0.5819 0.4271 0.3775 -0.2822 -0.1480 0.0851  280 ASP   B CA  
4264 C C   . ASP   B 258 ? 0.5214 0.4658 0.3896 -0.3185 -0.1418 0.1021  280 ASP   B C   
4265 O O   . ASP   B 258 ? 0.5413 0.4757 0.3978 -0.3360 -0.1426 0.0945  280 ASP   B O   
4266 C CB  . ASP   B 258 ? 0.6323 0.4291 0.3978 -0.2638 -0.1733 0.0796  280 ASP   B CB  
4267 C CG  . ASP   B 258 ? 0.6719 0.4022 0.4120 -0.2600 -0.2013 0.0713  280 ASP   B CG  
4268 O OD1 . ASP   B 258 ? 0.6533 0.3602 0.3517 -0.2510 -0.1767 0.1222  280 ASP   B OD1 
4269 O OD2 . ASP   B 258 ? 0.7417 0.3715 0.3884 -0.2925 -0.2657 0.0595  280 ASP   B OD2 
4270 N N   . ASN   B 259 ? 0.5257 0.5295 0.3447 -0.2894 -0.1463 0.0989  281 ASN   B N   
4271 C CA  . ASN   B 259 ? 0.5200 0.5256 0.3103 -0.2780 -0.1391 0.1313  281 ASN   B CA  
4272 C C   . ASN   B 259 ? 0.4934 0.5184 0.3138 -0.2711 -0.1177 0.1344  281 ASN   B C   
4273 O O   . ASN   B 259 ? 0.4277 0.5636 0.3327 -0.2782 -0.0982 0.1374  281 ASN   B O   
4274 C CB  . ASN   B 259 ? 0.5437 0.5188 0.2922 -0.2856 -0.1421 0.1507  281 ASN   B CB  
4275 C CG  . ASN   B 259 ? 0.5701 0.5274 0.2763 -0.2693 -0.1757 0.1393  281 ASN   B CG  
4276 O OD1 . ASN   B 259 ? 0.6028 0.5082 0.3166 -0.2804 -0.1657 0.1291  281 ASN   B OD1 
4277 N ND2 . ASN   B 259 ? 0.6018 0.5315 0.2769 -0.2802 -0.1713 0.1286  281 ASN   B ND2 
4278 N N   . LEU   B 260 ? 0.4907 0.4744 0.3259 -0.2749 -0.1120 0.1350  282 LEU   B N   
4279 C CA  . LEU   B 260 ? 0.5207 0.4634 0.2878 -0.2594 -0.1174 0.1197  282 LEU   B CA  
4280 C C   . LEU   B 260 ? 0.5106 0.4541 0.3086 -0.2507 -0.1174 0.1347  282 LEU   B C   
4281 O O   . LEU   B 260 ? 0.5351 0.5292 0.2942 -0.2516 -0.1106 0.1378  282 LEU   B O   
4282 C CB  . LEU   B 260 ? 0.5357 0.4761 0.2939 -0.2409 -0.1037 0.1200  282 LEU   B CB  
4283 C CG  . LEU   B 260 ? 0.5548 0.4796 0.2817 -0.2282 -0.1084 0.1085  282 LEU   B CG  
4284 C CD1 . LEU   B 260 ? 0.5927 0.5022 0.3105 -0.2053 -0.0867 0.1170  282 LEU   B CD1 
4285 C CD2 . LEU   B 260 ? 0.5618 0.4788 0.3354 -0.2283 -0.1130 0.1097  282 LEU   B CD2 
4286 N N   . VAL   B 261 ? 0.4877 0.4539 0.3047 -0.2467 -0.1068 0.1406  283 VAL   B N   
4287 C CA  . VAL   B 261 ? 0.5080 0.4232 0.3160 -0.2315 -0.1186 0.1297  283 VAL   B CA  
4288 C C   . VAL   B 261 ? 0.5351 0.4119 0.3298 -0.2312 -0.1292 0.1004  283 VAL   B C   
4289 O O   . VAL   B 261 ? 0.5485 0.4633 0.3535 -0.2544 -0.1165 0.1312  283 VAL   B O   
4290 C CB  . VAL   B 261 ? 0.4934 0.4027 0.3104 -0.2260 -0.1063 0.1301  283 VAL   B CB  
4291 C CG1 . VAL   B 261 ? 0.4728 0.3974 0.3503 -0.2430 -0.1011 0.1250  283 VAL   B CG1 
4292 C CG2 . VAL   B 261 ? 0.5031 0.4368 0.3308 -0.2199 -0.0925 0.1368  283 VAL   B CG2 
4293 N N   . TYR   B 262 ? 0.5463 0.3595 0.2938 -0.2241 -0.1343 0.0865  284 TYR   B N   
4294 C CA  . TYR   B 262 ? 0.5618 0.3490 0.2751 -0.2027 -0.1377 0.0791  284 TYR   B CA  
4295 C C   . TYR   B 262 ? 0.5300 0.3087 0.2701 -0.2011 -0.1252 0.0688  284 TYR   B C   
4296 O O   . TYR   B 262 ? 0.5009 0.3052 0.2594 -0.1847 -0.1368 0.0770  284 TYR   B O   
4297 C CB  . TYR   B 262 ? 0.6001 0.3510 0.2810 -0.2025 -0.1282 0.0841  284 TYR   B CB  
4298 C CG  . TYR   B 262 ? 0.6571 0.3394 0.2786 -0.2016 -0.1398 0.0433  284 TYR   B CG  
4299 C CD1 . TYR   B 262 ? 0.6778 0.3520 0.2649 -0.2062 -0.1367 0.0334  284 TYR   B CD1 
4300 C CD2 . TYR   B 262 ? 0.7022 0.3544 0.2832 -0.1917 -0.1580 0.0328  284 TYR   B CD2 
4301 C CE1 . TYR   B 262 ? 0.7015 0.3551 0.2946 -0.2107 -0.1572 0.0191  284 TYR   B CE1 
4302 C CE2 . TYR   B 262 ? 0.7011 0.3581 0.3167 -0.1977 -0.1721 0.0318  284 TYR   B CE2 
4303 C CZ  . TYR   B 262 ? 0.7228 0.3486 0.2704 -0.2046 -0.1686 0.0284  284 TYR   B CZ  
4304 O OH  . TYR   B 262 ? 0.7307 0.3274 0.3176 -0.2298 -0.1915 -0.0028 284 TYR   B OH  
4305 N N   . ILE   B 263 ? 0.5139 0.3155 0.2838 -0.2076 -0.1092 0.0807  285 ILE   B N   
4306 C CA  . ILE   B 263 ? 0.5384 0.2874 0.2723 -0.1974 -0.0989 0.0681  285 ILE   B CA  
4307 C C   . ILE   B 263 ? 0.6016 0.2710 0.2969 -0.1884 -0.1139 0.0755  285 ILE   B C   
4308 O O   . ILE   B 263 ? 0.6098 0.2607 0.3790 -0.2021 -0.1217 0.0686  285 ILE   B O   
4309 C CB  . ILE   B 263 ? 0.5099 0.2851 0.3056 -0.2037 -0.0860 0.0822  285 ILE   B CB  
4310 C CG1 . ILE   B 263 ? 0.4879 0.3073 0.3029 -0.1914 -0.0725 0.0935  285 ILE   B CG1 
4311 C CG2 . ILE   B 263 ? 0.4970 0.2647 0.2666 -0.2028 -0.0693 0.0850  285 ILE   B CG2 
4312 C CD1 . ILE   B 263 ? 0.5039 0.3627 0.3009 -0.1780 -0.0877 0.0915  285 ILE   B CD1 
4313 N N   . TRP   B 264 ? 0.6245 0.2784 0.2815 -0.1553 -0.1303 0.0658  286 TRP   B N   
4314 C CA  . TRP   B 264 ? 0.6821 0.2527 0.2941 -0.1312 -0.1271 0.0357  286 TRP   B CA  
4315 C C   . TRP   B 264 ? 0.7262 0.2428 0.3077 -0.0940 -0.1228 0.0357  286 TRP   B C   
4316 O O   . TRP   B 264 ? 0.7146 0.3136 0.2379 -0.0838 -0.1357 0.0479  286 TRP   B O   
4317 C CB  . TRP   B 264 ? 0.6831 0.2906 0.2824 -0.1196 -0.1328 0.0279  286 TRP   B CB  
4318 C CG  . TRP   B 264 ? 0.6952 0.2965 0.2606 -0.1042 -0.1287 0.0169  286 TRP   B CG  
4319 C CD1 . TRP   B 264 ? 0.7251 0.3331 0.2538 -0.0768 -0.1381 0.0096  286 TRP   B CD1 
4320 C CD2 . TRP   B 264 ? 0.7176 0.3079 0.2565 -0.0920 -0.1316 0.0130  286 TRP   B CD2 
4321 N NE1 . TRP   B 264 ? 0.7374 0.3091 0.2626 -0.0756 -0.1436 0.0039  286 TRP   B NE1 
4322 C CE2 . TRP   B 264 ? 0.7294 0.3032 0.2631 -0.0923 -0.1525 0.0217  286 TRP   B CE2 
4323 C CE3 . TRP   B 264 ? 0.7122 0.2740 0.2644 -0.0851 -0.1249 0.0430  286 TRP   B CE3 
4324 C CZ2 . TRP   B 264 ? 0.7383 0.2842 0.2958 -0.0967 -0.1347 0.0227  286 TRP   B CZ2 
4325 C CZ3 . TRP   B 264 ? 0.7260 0.2805 0.2530 -0.0684 -0.1197 0.0300  286 TRP   B CZ3 
4326 C CH2 . TRP   B 264 ? 0.7401 0.2653 0.2563 -0.0846 -0.1329 0.0321  286 TRP   B CH2 
4327 N N   . ASN   B 265 ? 0.7553 0.2326 0.3493 -0.0823 -0.1170 0.0275  287 ASN   B N   
4328 C CA  . ASN   B 265 ? 0.8169 0.2376 0.3395 -0.0473 -0.1247 0.0167  287 ASN   B CA  
4329 C C   . ASN   B 265 ? 0.8250 0.2210 0.3188 -0.0311 -0.1096 0.0153  287 ASN   B C   
4330 O O   . ASN   B 265 ? 0.8748 0.1965 0.3439 0.0027  -0.1181 -0.0097 287 ASN   B O   
4331 C CB  . ASN   B 265 ? 0.8510 0.2424 0.3805 -0.0427 -0.1318 0.0018  287 ASN   B CB  
4332 C CG  . ASN   B 265 ? 0.8730 0.2474 0.3499 -0.0222 -0.1415 -0.0004 287 ASN   B CG  
4333 O OD1 . ASN   B 265 ? 0.8754 0.2510 0.3861 0.0212  -0.1332 0.0100  287 ASN   B OD1 
4334 N ND2 . ASN   B 265 ? 0.8951 0.3072 0.3553 -0.0321 -0.1283 -0.0013 287 ASN   B ND2 
4335 N N   . LEU   B 266 ? 0.8434 0.2607 0.2911 0.0016  -0.1084 0.0173  288 LEU   B N   
4336 C CA  . LEU   B 266 ? 0.8256 0.2433 0.2658 0.0172  -0.0810 0.0109  288 LEU   B CA  
4337 C C   . LEU   B 266 ? 0.8747 0.2653 0.2684 0.0484  -0.0761 -0.0013 288 LEU   B C   
4338 O O   . LEU   B 266 ? 0.8904 0.2408 0.2667 0.0826  -0.0775 0.0188  288 LEU   B O   
4339 C CB  . LEU   B 266 ? 0.8195 0.2632 0.2591 0.0165  -0.0687 0.0237  288 LEU   B CB  
4340 C CG  . LEU   B 266 ? 0.8046 0.2709 0.2728 0.0250  -0.0613 0.0214  288 LEU   B CG  
4341 C CD1 . LEU   B 266 ? 0.7902 0.2645 0.2607 0.0104  -0.0247 0.0206  288 LEU   B CD1 
4342 C CD2 . LEU   B 266 ? 0.8110 0.2598 0.3125 0.0511  -0.0596 -0.0004 288 LEU   B CD2 
4343 N N   . GLN   B 267 ? 0.9124 0.2786 0.2640 0.0985  -0.0869 -0.0148 289 GLN   B N   
4344 C CA  . GLN   B 267 ? 0.9496 0.3187 0.2821 0.1158  -0.1186 0.0042  289 GLN   B CA  
4345 C C   . GLN   B 267 ? 0.9659 0.3371 0.2603 0.0999  -0.0915 -0.0189 289 GLN   B C   
4346 O O   . GLN   B 267 ? 0.9625 0.2809 0.3143 0.1710  -0.0590 0.0077  289 GLN   B O   
4347 C CB  . GLN   B 267 ? 0.9514 0.3704 0.2229 0.1170  -0.1060 0.0067  289 GLN   B CB  
4348 C CG  . GLN   B 267 ? 0.9495 0.3795 0.2945 0.1390  -0.1238 -0.0148 289 GLN   B CG  
4349 C CD  . GLN   B 267 ? 0.9795 0.4114 0.3138 0.1443  -0.1011 -0.0303 289 GLN   B CD  
4350 O OE1 . GLN   B 267 ? 1.0144 0.5043 0.4081 0.1858  -0.0429 -0.0767 289 GLN   B OE1 
4351 N NE2 . GLN   B 267 ? 0.9883 0.4053 0.3702 0.1352  -0.0951 -0.0577 289 GLN   B NE2 
4352 N N   . THR   B 268 ? 0.9888 0.3137 0.2922 0.0568  -0.0828 -0.0155 290 THR   B N   
4353 C CA  . THR   B 268 ? 0.9858 0.3055 0.2771 0.0568  -0.0767 -0.0295 290 THR   B CA  
4354 C C   . THR   B 268 ? 0.9793 0.3187 0.2684 0.0529  -0.0921 -0.0545 290 THR   B C   
4355 O O   . THR   B 268 ? 0.9807 0.2891 0.3015 0.0737  -0.1129 -0.0854 290 THR   B O   
4356 C CB  . THR   B 268 ? 1.0175 0.3696 0.3069 0.0586  -0.0590 -0.0169 290 THR   B CB  
4357 O OG1 . THR   B 268 ? 0.9939 0.3065 0.3073 0.0298  -0.0562 0.0163  290 THR   B OG1 
4358 C CG2 . THR   B 268 ? 1.0259 0.3608 0.3541 0.0616  -0.0403 0.0183  290 THR   B CG2 
4359 N N   . LYS   B 269 ? 0.9536 0.2970 0.3000 0.0343  -0.0947 -0.0324 291 LYS   B N   
4360 C CA  . LYS   B 269 ? 0.9479 0.3153 0.3053 0.0138  -0.1212 -0.0242 291 LYS   B CA  
4361 C C   . LYS   B 269 ? 0.9605 0.3402 0.2809 -0.0507 -0.1616 -0.0073 291 LYS   B C   
4362 O O   . LYS   B 269 ? 0.9947 0.3811 0.3103 -0.0671 -0.1713 0.0374  291 LYS   B O   
4363 C CB  . LYS   B 269 ? 0.9709 0.3096 0.3178 0.0484  -0.1062 -0.0444 291 LYS   B CB  
4364 C CG  . LYS   B 269 ? 0.9867 0.2869 0.3275 0.0568  -0.1152 -0.0786 291 LYS   B CG  
4365 C CD  . LYS   B 269 ? 1.0124 0.3220 0.3694 0.0766  -0.1046 -0.0740 291 LYS   B CD  
4366 C CE  . LYS   B 269 ? 1.0320 0.3384 0.3895 0.1114  -0.1057 -0.0890 291 LYS   B CE  
4367 N NZ  . LYS   B 269 ? 1.0350 0.3267 0.4115 0.1274  -0.1290 -0.0930 291 LYS   B NZ  
4368 N N   . GLU   B 270 ? 0.9283 0.3728 0.2920 -0.0996 -0.1821 -0.0199 292 GLU   B N   
4369 C CA  . GLU   B 270 ? 0.9256 0.3468 0.3561 -0.1278 -0.1644 -0.0041 292 GLU   B CA  
4370 C C   . GLU   B 270 ? 0.8759 0.3204 0.3525 -0.1636 -0.1640 0.0288  292 GLU   B C   
4371 O O   . GLU   B 270 ? 0.8801 0.3104 0.3186 -0.1234 -0.1621 0.0736  292 GLU   B O   
4372 C CB  . GLU   B 270 ? 0.9311 0.3752 0.3223 -0.1322 -0.1541 0.0308  292 GLU   B CB  
4373 N N   . ILE   B 271 ? 0.8407 0.3227 0.3130 -0.2415 -0.1744 0.0120  293 ILE   B N   
4374 C CA  . ILE   B 271 ? 0.8357 0.3003 0.3522 -0.2835 -0.1406 -0.0070 293 ILE   B CA  
4375 C C   . ILE   B 271 ? 0.8275 0.3209 0.3974 -0.2892 -0.1297 0.0090  293 ILE   B C   
4376 O O   . ILE   B 271 ? 0.9291 0.3020 0.4223 -0.3073 -0.0494 0.0042  293 ILE   B O   
4377 C CB  . ILE   B 271 ? 0.8387 0.3327 0.3876 -0.2740 -0.1397 0.0101  293 ILE   B CB  
4378 C CG1 . ILE   B 271 ? 0.8574 0.3578 0.4222 -0.2919 -0.1411 0.0333  293 ILE   B CG1 
4379 C CG2 . ILE   B 271 ? 0.8235 0.3417 0.3496 -0.2802 -0.1290 -0.0137 293 ILE   B CG2 
4380 C CD1 . ILE   B 271 ? 0.8636 0.3594 0.4359 -0.3213 -0.1532 -0.0027 293 ILE   B CD1 
4381 N N   . VAL   B 272 ? 0.7874 0.3428 0.3781 -0.2603 -0.1008 0.0378  294 VAL   B N   
4382 C CA  . VAL   B 272 ? 0.7620 0.3825 0.3576 -0.2282 -0.1214 0.0491  294 VAL   B CA  
4383 C C   . VAL   B 272 ? 0.7318 0.3845 0.3767 -0.2443 -0.0952 0.0615  294 VAL   B C   
4384 O O   . VAL   B 272 ? 0.7272 0.4392 0.4124 -0.2872 -0.0825 0.0742  294 VAL   B O   
4385 C CB  . VAL   B 272 ? 0.7686 0.3848 0.3582 -0.2048 -0.1297 0.0348  294 VAL   B CB  
4386 C CG1 . VAL   B 272 ? 0.7657 0.4057 0.3559 -0.1878 -0.1298 0.0251  294 VAL   B CG1 
4387 C CG2 . VAL   B 272 ? 0.7947 0.3668 0.2834 -0.1864 -0.1352 0.0525  294 VAL   B CG2 
4388 N N   . GLN   B 273 ? 0.6878 0.3685 0.3906 -0.2606 -0.1145 0.0597  295 GLN   B N   
4389 C CA  . GLN   B 273 ? 0.6614 0.3732 0.3648 -0.2555 -0.1294 0.0456  295 GLN   B CA  
4390 C C   . GLN   B 273 ? 0.6577 0.3993 0.3548 -0.2596 -0.1302 0.0428  295 GLN   B C   
4391 O O   . GLN   B 273 ? 0.6541 0.4335 0.3482 -0.2520 -0.1550 0.0635  295 GLN   B O   
4392 C CB  . GLN   B 273 ? 0.6385 0.4148 0.3916 -0.2484 -0.1282 0.0338  295 GLN   B CB  
4393 C CG  . GLN   B 273 ? 0.6341 0.4313 0.4301 -0.2281 -0.1198 0.0294  295 GLN   B CG  
4394 C CD  . GLN   B 273 ? 0.5747 0.4432 0.3810 -0.2216 -0.1229 0.0939  295 GLN   B CD  
4395 O OE1 . GLN   B 273 ? 0.5794 0.3450 0.3764 -0.1914 -0.1295 0.0619  295 GLN   B OE1 
4396 N NE2 . GLN   B 273 ? 0.5296 0.4594 0.3950 -0.2365 -0.1256 0.1200  295 GLN   B NE2 
4397 N N   . LYS   B 274 ? 0.6474 0.4112 0.3332 -0.2421 -0.1067 0.0386  296 LYS   B N   
4398 C CA  . LYS   B 274 ? 0.6303 0.4046 0.3765 -0.2500 -0.0906 0.0261  296 LYS   B CA  
4399 C C   . LYS   B 274 ? 0.5893 0.4379 0.4168 -0.2667 -0.0757 0.0412  296 LYS   B C   
4400 O O   . LYS   B 274 ? 0.6156 0.4723 0.4569 -0.2831 -0.0389 0.0075  296 LYS   B O   
4401 C CB  . LYS   B 274 ? 0.6780 0.4335 0.3759 -0.2300 -0.1164 0.0277  296 LYS   B CB  
4402 C CG  . LYS   B 274 ? 0.7318 0.4435 0.3960 -0.2142 -0.1118 -0.0019 296 LYS   B CG  
4403 C CD  . LYS   B 274 ? 0.8076 0.4956 0.4137 -0.2082 -0.1281 -0.0284 296 LYS   B CD  
4404 C CE  . LYS   B 274 ? 0.8729 0.5344 0.4308 -0.1921 -0.1519 -0.0228 296 LYS   B CE  
4405 N NZ  . LYS   B 274 ? 0.9390 0.5807 0.4694 -0.1998 -0.1844 -0.0407 296 LYS   B NZ  
4406 N N   . LEU   B 275 ? 0.5086 0.4191 0.3531 -0.2708 -0.0668 0.0875  297 LEU   B N   
4407 C CA  . LEU   B 275 ? 0.5131 0.4602 0.3759 -0.2659 -0.0772 0.1091  297 LEU   B CA  
4408 C C   . LEU   B 275 ? 0.5132 0.5012 0.3834 -0.2784 -0.0915 0.1159  297 LEU   B C   
4409 O O   . LEU   B 275 ? 0.5218 0.5149 0.3322 -0.3098 -0.0958 0.0912  297 LEU   B O   
4410 C CB  . LEU   B 275 ? 0.4994 0.4463 0.3331 -0.2408 -0.0751 0.1225  297 LEU   B CB  
4411 C CG  . LEU   B 275 ? 0.4845 0.4417 0.3537 -0.2453 -0.0752 0.1342  297 LEU   B CG  
4412 C CD1 . LEU   B 275 ? 0.4733 0.4561 0.3604 -0.2412 -0.0763 0.1385  297 LEU   B CD1 
4413 C CD2 . LEU   B 275 ? 0.4769 0.4325 0.3719 -0.2325 -0.0852 0.1278  297 LEU   B CD2 
4414 N N   . GLN   B 276 ? 0.5298 0.5278 0.4390 -0.3103 -0.1099 0.1130  298 GLN   B N   
4415 C CA  . GLN   B 276 ? 0.5152 0.5693 0.4587 -0.2975 -0.1285 0.1214  298 GLN   B CA  
4416 C C   . GLN   B 276 ? 0.5312 0.5496 0.4672 -0.2750 -0.1364 0.1449  298 GLN   B C   
4417 O O   . GLN   B 276 ? 0.5836 0.5268 0.4180 -0.2232 -0.1373 0.1616  298 GLN   B O   
4418 C CB  . GLN   B 276 ? 0.5719 0.6106 0.5430 -0.3260 -0.1508 0.1089  298 GLN   B CB  
4419 C CG  . GLN   B 276 ? 0.6532 0.7214 0.5790 -0.3191 -0.1614 0.1267  298 GLN   B CG  
4420 C CD  . GLN   B 276 ? 0.7036 0.8852 0.6567 -0.2878 -0.1625 0.1400  298 GLN   B CD  
4421 O OE1 . GLN   B 276 ? 0.8009 0.9480 0.7221 -0.3415 -0.1071 0.1615  298 GLN   B OE1 
4422 N NE2 . GLN   B 276 ? 0.7966 0.9685 0.6771 -0.2642 -0.1737 0.1581  298 GLN   B NE2 
4423 N N   . GLY   B 277 ? 0.4523 0.5719 0.4999 -0.2559 -0.1402 0.1550  299 GLY   B N   
4424 C CA  . GLY   B 277 ? 0.4226 0.5722 0.5040 -0.2427 -0.1394 0.1639  299 GLY   B CA  
4425 C C   . GLY   B 277 ? 0.3488 0.5980 0.4628 -0.2213 -0.1350 0.1726  299 GLY   B C   
4426 O O   . GLY   B 277 ? 0.2746 0.6525 0.4874 -0.2218 -0.0703 0.1908  299 GLY   B O   
4427 N N   . HIS   B 278 ? 0.3476 0.5623 0.4006 -0.2080 -0.1007 0.1955  300 HIS   B N   
4428 C CA  . HIS   B 278 ? 0.3539 0.5528 0.3746 -0.2022 -0.0999 0.1714  300 HIS   B CA  
4429 C C   . HIS   B 278 ? 0.3604 0.5599 0.3920 -0.2082 -0.1344 0.1588  300 HIS   B C   
4430 O O   . HIS   B 278 ? 0.4024 0.5522 0.4108 -0.2166 -0.1245 0.1756  300 HIS   B O   
4431 C CB  . HIS   B 278 ? 0.3497 0.5406 0.3272 -0.1992 -0.0818 0.1544  300 HIS   B CB  
4432 C CG  . HIS   B 278 ? 0.3246 0.5184 0.2974 -0.1944 -0.0606 0.1464  300 HIS   B CG  
4433 N ND1 . HIS   B 278 ? 0.3438 0.5486 0.2721 -0.1672 -0.0391 0.1438  300 HIS   B ND1 
4434 C CD2 . HIS   B 278 ? 0.3494 0.4889 0.3063 -0.1800 -0.0551 0.1408  300 HIS   B CD2 
4435 C CE1 . HIS   B 278 ? 0.3470 0.5455 0.2485 -0.1580 -0.0285 0.1199  300 HIS   B CE1 
4436 N NE2 . HIS   B 278 ? 0.3239 0.5575 0.2317 -0.1604 -0.0435 0.1152  300 HIS   B NE2 
4437 N N   . THR   B 279 ? 0.3274 0.5706 0.3741 -0.2188 -0.1278 0.1467  301 THR   B N   
4438 C CA  . THR   B 279 ? 0.3241 0.5866 0.3566 -0.1866 -0.1113 0.1513  301 THR   B CA  
4439 C C   . THR   B 279 ? 0.3493 0.5725 0.3175 -0.1682 -0.1204 0.1585  301 THR   B C   
4440 O O   . THR   B 279 ? 0.3830 0.5438 0.3195 -0.1459 -0.1180 0.1779  301 THR   B O   
4441 C CB  . THR   B 279 ? 0.3458 0.5992 0.3749 -0.1603 -0.1131 0.1366  301 THR   B CB  
4442 O OG1 . THR   B 279 ? 0.3298 0.5885 0.4075 -0.1609 -0.0963 0.1195  301 THR   B OG1 
4443 C CG2 . THR   B 279 ? 0.3449 0.6059 0.4050 -0.1572 -0.0963 0.1354  301 THR   B CG2 
4444 N N   . ASP   B 280 ? 0.3298 0.5477 0.2991 -0.1868 -0.0894 0.1370  302 ASP   B N   
4445 C CA  . ASP   B 280 ? 0.3502 0.5300 0.3068 -0.1772 -0.0707 0.1276  302 ASP   B CA  
4446 C C   . ASP   B 280 ? 0.3347 0.5103 0.2799 -0.1728 -0.0754 0.1313  302 ASP   B C   
4447 O O   . ASP   B 280 ? 0.3543 0.5658 0.2976 -0.1752 -0.0953 0.1400  302 ASP   B O   
4448 C CB  . ASP   B 280 ? 0.3801 0.5377 0.3056 -0.1566 -0.0870 0.1269  302 ASP   B CB  
4449 C CG  . ASP   B 280 ? 0.3862 0.5108 0.3114 -0.1740 -0.0929 0.1182  302 ASP   B CG  
4450 O OD1 . ASP   B 280 ? 0.4177 0.5157 0.3044 -0.1807 -0.1051 0.1151  302 ASP   B OD1 
4451 O OD2 . ASP   B 280 ? 0.4237 0.4994 0.2834 -0.1849 -0.1122 0.1352  302 ASP   B OD2 
4452 N N   . VAL   B 281 ? 0.3500 0.4608 0.2408 -0.1576 -0.0554 0.1129  303 VAL   B N   
4453 C CA  . VAL   B 281 ? 0.3470 0.4077 0.2273 -0.1497 -0.0662 0.0897  303 VAL   B CA  
4454 C C   . VAL   B 281 ? 0.3297 0.3781 0.2361 -0.1595 -0.0569 0.0689  303 VAL   B C   
4455 O O   . VAL   B 281 ? 0.2922 0.4366 0.2022 -0.1355 -0.0286 0.0309  303 VAL   B O   
4456 C CB  . VAL   B 281 ? 0.3756 0.4057 0.2525 -0.1588 -0.0554 0.0926  303 VAL   B CB  
4457 C CG1 . VAL   B 281 ? 0.3857 0.3866 0.2424 -0.1412 -0.0380 0.1087  303 VAL   B CG1 
4458 C CG2 . VAL   B 281 ? 0.3941 0.3865 0.2656 -0.1597 -0.0435 0.1043  303 VAL   B CG2 
4459 N N   . VAL   B 282 ? 0.3204 0.3579 0.2498 -0.1711 -0.0755 0.0568  304 VAL   B N   
4460 C CA  . VAL   B 282 ? 0.3256 0.3434 0.2359 -0.1411 -0.0535 0.0684  304 VAL   B CA  
4461 C C   . VAL   B 282 ? 0.3083 0.3283 0.2346 -0.1221 -0.0378 0.0689  304 VAL   B C   
4462 O O   . VAL   B 282 ? 0.3347 0.2944 0.2643 -0.1179 -0.0175 0.0472  304 VAL   B O   
4463 C CB  . VAL   B 282 ? 0.3410 0.3620 0.2446 -0.1472 -0.0464 0.0779  304 VAL   B CB  
4464 C CG1 . VAL   B 282 ? 0.3512 0.3652 0.2531 -0.1434 -0.0642 0.0957  304 VAL   B CG1 
4465 C CG2 . VAL   B 282 ? 0.3494 0.3904 0.2605 -0.1493 -0.0499 0.0784  304 VAL   B CG2 
4466 N N   . ILE   B 283 ? 0.2726 0.3321 0.2390 -0.1113 -0.0386 0.0482  305 ILE   B N   
4467 C CA  . ILE   B 283 ? 0.2897 0.3228 0.2353 -0.1178 -0.0296 0.0543  305 ILE   B CA  
4468 C C   . ILE   B 283 ? 0.2689 0.2894 0.2114 -0.1133 -0.0197 0.0613  305 ILE   B C   
4469 O O   . ILE   B 283 ? 0.2841 0.2848 0.2162 -0.1083 -0.0020 0.0672  305 ILE   B O   
4470 C CB  . ILE   B 283 ? 0.2733 0.3291 0.2269 -0.1032 -0.0459 0.0599  305 ILE   B CB  
4471 C CG1 . ILE   B 283 ? 0.2713 0.3485 0.2485 -0.1083 -0.0381 0.0500  305 ILE   B CG1 
4472 C CG2 . ILE   B 283 ? 0.2662 0.3617 0.2397 -0.1070 -0.0404 0.0582  305 ILE   B CG2 
4473 C CD1 . ILE   B 283 ? 0.2881 0.3478 0.2413 -0.1025 -0.0341 0.0574  305 ILE   B CD1 
4474 N N   . SER   B 284 ? 0.2741 0.3103 0.2059 -0.1181 -0.0252 0.0628  306 SER   B N   
4475 C CA  . SER   B 284 ? 0.2677 0.3088 0.1980 -0.1090 -0.0153 0.0671  306 SER   B CA  
4476 C C   . SER   B 284 ? 0.2736 0.3016 0.2059 -0.1056 -0.0083 0.0647  306 SER   B C   
4477 O O   . SER   B 284 ? 0.2761 0.3192 0.2065 -0.0923 0.0027  0.0404  306 SER   B O   
4478 C CB  . SER   B 284 ? 0.2589 0.3035 0.2000 -0.0996 -0.0183 0.0740  306 SER   B CB  
4479 O OG  . SER   B 284 ? 0.2722 0.2836 0.2057 -0.1035 -0.0245 0.0892  306 SER   B OG  
4480 N N   . THR   B 285 ? 0.2597 0.3122 0.2065 -0.1014 -0.0079 0.0689  307 THR   B N   
4481 C CA  . THR   B 285 ? 0.2701 0.3047 0.2029 -0.0935 -0.0084 0.0694  307 THR   B CA  
4482 C C   . THR   B 285 ? 0.2638 0.3128 0.1994 -0.0922 -0.0014 0.0694  307 THR   B C   
4483 O O   . THR   B 285 ? 0.2617 0.3209 0.2141 -0.0853 0.0011  0.0700  307 THR   B O   
4484 C CB  . THR   B 285 ? 0.3032 0.3060 0.2104 -0.0951 -0.0115 0.0777  307 THR   B CB  
4485 O OG1 . THR   B 285 ? 0.3208 0.3085 0.2046 -0.0950 0.0231  0.0805  307 THR   B OG1 
4486 C CG2 . THR   B 285 ? 0.3282 0.2870 0.2149 -0.1017 -0.0234 0.0866  307 THR   B CG2 
4487 N N   . ALA   B 286 ? 0.2385 0.3147 0.1967 -0.0871 -0.0056 0.0795  308 ALA   B N   
4488 C CA  . ALA   B 286 ? 0.2336 0.3034 0.2046 -0.0958 -0.0022 0.0775  308 ALA   B CA  
4489 C C   . ALA   B 286 ? 0.2342 0.3345 0.2101 -0.0991 -0.0051 0.0885  308 ALA   B C   
4490 O O   . ALA   B 286 ? 0.2375 0.3271 0.2120 -0.1194 0.0104  0.0844  308 ALA   B O   
4491 C CB  . ALA   B 286 ? 0.2337 0.3100 0.2143 -0.0792 -0.0159 0.0797  308 ALA   B CB  
4492 N N   . CYS   B 287 ? 0.2304 0.3455 0.2357 -0.0883 -0.0162 0.0938  309 CYS   B N   
4493 C CA  . CYS   B 287 ? 0.2361 0.3499 0.2097 -0.0905 -0.0028 0.0895  309 CYS   B CA  
4494 C C   . CYS   B 287 ? 0.2159 0.3569 0.1980 -0.0925 0.0000  0.0948  309 CYS   B C   
4495 O O   . CYS   B 287 ? 0.2075 0.3741 0.2040 -0.1046 0.0102  0.0818  309 CYS   B O   
4496 C CB  . CYS   B 287 ? 0.2717 0.3432 0.2263 -0.0790 -0.0195 0.0937  309 CYS   B CB  
4497 S SG  . CYS   B 287 ? 0.3337 0.3189 0.2528 -0.0825 -0.0189 0.0892  309 CYS   B SG  
4498 N N   . HIS   B 288 ? 0.2284 0.3440 0.1773 -0.0909 0.0079  0.0953  310 HIS   B N   
4499 C CA  . HIS   B 288 ? 0.2406 0.3661 0.1854 -0.0810 0.0242  0.0915  310 HIS   B CA  
4500 C C   . HIS   B 288 ? 0.2493 0.3700 0.1755 -0.0678 0.0113  0.0714  310 HIS   B C   
4501 O O   . HIS   B 288 ? 0.2662 0.3806 0.1594 -0.0288 0.0141  0.0727  310 HIS   B O   
4502 C CB  . HIS   B 288 ? 0.2412 0.3588 0.1682 -0.0990 0.0172  0.1048  310 HIS   B CB  
4503 C CG  . HIS   B 288 ? 0.2467 0.3616 0.1711 -0.1003 0.0108  0.0946  310 HIS   B CG  
4504 N ND1 . HIS   B 288 ? 0.2740 0.3511 0.1524 -0.1058 0.0251  0.1120  310 HIS   B ND1 
4505 C CD2 . HIS   B 288 ? 0.2438 0.3530 0.1755 -0.1008 0.0140  0.1080  310 HIS   B CD2 
4506 C CE1 . HIS   B 288 ? 0.2663 0.3747 0.1720 -0.0892 0.0162  0.1018  310 HIS   B CE1 
4507 N NE2 . HIS   B 288 ? 0.2430 0.3798 0.1685 -0.0940 0.0233  0.0961  310 HIS   B NE2 
4508 N N   . PRO   B 289 ? 0.2456 0.3692 0.1978 -0.0495 0.0176  0.0597  311 PRO   B N   
4509 C CA  . PRO   B 289 ? 0.2602 0.3777 0.2011 -0.0405 0.0053  0.0562  311 PRO   B CA  
4510 C C   . PRO   B 289 ? 0.2565 0.3864 0.1818 -0.0366 0.0106  0.0684  311 PRO   B C   
4511 O O   . PRO   B 289 ? 0.2416 0.3908 0.1950 -0.0409 0.0039  0.0520  311 PRO   B O   
4512 C CB  . PRO   B 289 ? 0.2376 0.3760 0.1935 -0.0427 0.0148  0.0649  311 PRO   B CB  
4513 C CG  . PRO   B 289 ? 0.2096 0.3806 0.1762 -0.0530 0.0207  0.0687  311 PRO   B CG  
4514 C CD  . PRO   B 289 ? 0.2178 0.3903 0.1657 -0.0446 0.0278  0.0521  311 PRO   B CD  
4515 N N   . THR   B 290 ? 0.2588 0.3872 0.2158 -0.0604 -0.0052 0.0753  312 THR   B N   
4516 C CA  . THR   B 290 ? 0.2750 0.3822 0.2091 -0.0530 0.0053  0.0847  312 THR   B CA  
4517 C C   . THR   B 290 ? 0.2973 0.3924 0.2488 -0.0735 -0.0052 0.0978  312 THR   B C   
4518 O O   . THR   B 290 ? 0.3216 0.3961 0.2734 -0.0983 0.0091  0.1104  312 THR   B O   
4519 C CB  . THR   B 290 ? 0.2590 0.4005 0.2053 -0.0456 0.0133  0.0817  312 THR   B CB  
4520 O OG1 . THR   B 290 ? 0.2526 0.4001 0.1875 -0.0161 0.0250  0.1038  312 THR   B OG1 
4521 C CG2 . THR   B 290 ? 0.2725 0.4048 0.1873 -0.0495 0.0129  0.0654  312 THR   B CG2 
4522 N N   . GLU   B 291 ? 0.2967 0.3835 0.2474 -0.0771 0.0164  0.1103  313 GLU   B N   
4523 C CA  . GLU   B 291 ? 0.2923 0.3941 0.2692 -0.0841 0.0099  0.0998  313 GLU   B CA  
4524 C C   . GLU   B 291 ? 0.2901 0.3831 0.2557 -0.0996 0.0130  0.1097  313 GLU   B C   
4525 O O   . GLU   B 291 ? 0.2959 0.3889 0.2403 -0.1176 -0.0064 0.0966  313 GLU   B O   
4526 C CB  . GLU   B 291 ? 0.2981 0.4167 0.2852 -0.0716 0.0317  0.0994  313 GLU   B CB  
4527 C CG  . GLU   B 291 ? 0.3110 0.4420 0.2987 -0.0629 0.0245  0.0929  313 GLU   B CG  
4528 C CD  . GLU   B 291 ? 0.2978 0.4377 0.3145 -0.0693 0.0388  0.0939  313 GLU   B CD  
4529 O OE1 . GLU   B 291 ? 0.3001 0.3921 0.3202 -0.0545 0.0538  0.1077  313 GLU   B OE1 
4530 O OE2 . GLU   B 291 ? 0.3055 0.4613 0.3088 -0.0616 0.0600  0.0801  313 GLU   B OE2 
4531 N N   . ASN   B 292 ? 0.3737 0.4322 0.2563 -0.1240 0.0044  0.1067  314 ASN   B N   
4532 C CA  . ASN   B 292 ? 0.4031 0.3972 0.2879 -0.1494 -0.0148 0.1014  314 ASN   B CA  
4533 C C   . ASN   B 292 ? 0.3696 0.4170 0.2913 -0.1700 -0.0124 0.0971  314 ASN   B C   
4534 O O   . ASN   B 292 ? 0.3774 0.4299 0.2980 -0.1929 -0.0090 0.0907  314 ASN   B O   
4535 C CB  . ASN   B 292 ? 0.4519 0.3980 0.2939 -0.1528 0.0021  0.1272  314 ASN   B CB  
4536 C CG  . ASN   B 292 ? 0.5013 0.3834 0.2928 -0.1450 0.0139  0.1321  314 ASN   B CG  
4537 O OD1 . ASN   B 292 ? 0.5209 0.3541 0.3156 -0.1202 -0.0027 0.0952  314 ASN   B OD1 
4538 N ND2 . ASN   B 292 ? 0.5385 0.3595 0.3226 -0.1503 0.0174  0.1355  314 ASN   B ND2 
4539 N N   . ILE   B 293 ? 0.3774 0.4191 0.2658 -0.1477 -0.0170 0.1030  315 ILE   B N   
4540 C CA  . ILE   B 293 ? 0.3295 0.4160 0.2510 -0.1567 0.0135  0.0957  315 ILE   B CA  
4541 C C   . ILE   B 293 ? 0.3199 0.4184 0.2495 -0.1631 0.0078  0.1029  315 ILE   B C   
4542 O O   . ILE   B 293 ? 0.3187 0.4243 0.2453 -0.1635 0.0164  0.1084  315 ILE   B O   
4543 C CB  . ILE   B 293 ? 0.3314 0.4410 0.2432 -0.1496 0.0114  0.0873  315 ILE   B CB  
4544 C CG1 . ILE   B 293 ? 0.3384 0.4802 0.2421 -0.1359 0.0220  0.0766  315 ILE   B CG1 
4545 C CG2 . ILE   B 293 ? 0.3329 0.4087 0.2342 -0.1508 0.0309  0.0926  315 ILE   B CG2 
4546 C CD1 . ILE   B 293 ? 0.3097 0.4924 0.2132 -0.1232 0.0162  0.0636  315 ILE   B CD1 
4547 N N   . ILE   B 294 ? 0.3031 0.4021 0.2394 -0.1657 0.0164  0.0990  316 ILE   B N   
4548 C CA  . ILE   B 294 ? 0.2751 0.3944 0.2465 -0.1599 0.0194  0.1034  316 ILE   B CA  
4549 C C   . ILE   B 294 ? 0.2604 0.4066 0.2177 -0.1422 0.0082  0.1038  316 ILE   B C   
4550 O O   . ILE   B 294 ? 0.2567 0.4282 0.2116 -0.1117 -0.0092 0.0903  316 ILE   B O   
4551 C CB  . ILE   B 294 ? 0.3017 0.3799 0.2645 -0.1657 0.0173  0.0948  316 ILE   B CB  
4552 C CG1 . ILE   B 294 ? 0.3351 0.3838 0.2925 -0.1622 0.0146  0.0821  316 ILE   B CG1 
4553 C CG2 . ILE   B 294 ? 0.3188 0.4047 0.2608 -0.1484 0.0023  0.0805  316 ILE   B CG2 
4554 C CD1 . ILE   B 294 ? 0.3656 0.3850 0.2874 -0.1540 0.0045  0.0749  316 ILE   B CD1 
4555 N N   . ALA   B 295 ? 0.2318 0.3916 0.2374 -0.1369 -0.0089 0.0900  317 ALA   B N   
4556 C CA  . ALA   B 295 ? 0.2304 0.3960 0.2354 -0.1316 0.0062  0.0869  317 ALA   B CA  
4557 C C   . ALA   B 295 ? 0.2410 0.4002 0.2251 -0.1219 0.0093  0.0908  317 ALA   B C   
4558 O O   . ALA   B 295 ? 0.2745 0.3742 0.2292 -0.1204 0.0270  0.0882  317 ALA   B O   
4559 C CB  . ALA   B 295 ? 0.2239 0.3998 0.2368 -0.1396 0.0056  0.0876  317 ALA   B CB  
4560 N N   . SER   B 296 ? 0.2348 0.4285 0.2320 -0.1160 0.0190  0.0683  318 SER   B N   
4561 C CA  . SER   B 296 ? 0.2421 0.4532 0.2403 -0.1163 0.0202  0.0899  318 SER   B CA  
4562 C C   . SER   B 296 ? 0.2326 0.4644 0.2481 -0.0968 0.0040  0.0863  318 SER   B C   
4563 O O   . SER   B 296 ? 0.2765 0.5239 0.2216 -0.1090 0.0335  0.0963  318 SER   B O   
4564 C CB  . SER   B 296 ? 0.2564 0.4623 0.2177 -0.1104 0.0102  0.0729  318 SER   B CB  
4565 O OG  . SER   B 296 ? 0.2701 0.4820 0.2373 -0.1229 0.0255  0.0825  318 SER   B OG  
4566 N N   . ALA   B 297 ? 0.2271 0.4489 0.2573 -0.0876 -0.0114 0.0897  319 ALA   B N   
4567 C CA  . ALA   B 297 ? 0.2173 0.4452 0.2298 -0.0698 -0.0248 0.1001  319 ALA   B CA  
4568 C C   . ALA   B 297 ? 0.2288 0.4238 0.2290 -0.0770 -0.0014 0.0994  319 ALA   B C   
4569 O O   . ALA   B 297 ? 0.2419 0.3792 0.2725 -0.0443 -0.0132 0.0738  319 ALA   B O   
4570 C CB  . ALA   B 297 ? 0.2142 0.4504 0.2344 -0.0558 -0.0281 0.1041  319 ALA   B CB  
4571 N N   . ALA   B 298 ? 0.2281 0.4395 0.2186 -0.0848 -0.0125 0.1082  320 ALA   B N   
4572 C CA  . ALA   B 298 ? 0.2705 0.4417 0.2293 -0.1082 -0.0400 0.1086  320 ALA   B CA  
4573 C C   . ALA   B 298 ? 0.2566 0.4539 0.2626 -0.1030 -0.0449 0.1053  320 ALA   B C   
4574 O O   . ALA   B 298 ? 0.2066 0.4891 0.2910 -0.0986 -0.0458 0.0978  320 ALA   B O   
4575 C CB  . ALA   B 298 ? 0.2768 0.4352 0.2394 -0.1086 -0.0505 0.1186  320 ALA   B CB  
4576 N N   . LEU   B 299 ? 0.2650 0.4554 0.2661 -0.1143 -0.0419 0.1056  321 LEU   B N   
4577 C CA  . LEU   B 299 ? 0.2647 0.4661 0.2390 -0.1126 -0.0203 0.1121  321 LEU   B CA  
4578 C C   . LEU   B 299 ? 0.2795 0.4999 0.2465 -0.1068 -0.0288 0.1172  321 LEU   B C   
4579 O O   . LEU   B 299 ? 0.2459 0.4749 0.2298 -0.1003 -0.0227 0.0994  321 LEU   B O   
4580 C CB  . LEU   B 299 ? 0.2767 0.4392 0.2490 -0.1153 -0.0191 0.0898  321 LEU   B CB  
4581 C CG  . LEU   B 299 ? 0.2708 0.4377 0.2213 -0.1073 -0.0293 0.0750  321 LEU   B CG  
4582 C CD1 . LEU   B 299 ? 0.2757 0.4503 0.2351 -0.1007 -0.0226 0.0724  321 LEU   B CD1 
4583 C CD2 . LEU   B 299 ? 0.2581 0.4371 0.2282 -0.0959 -0.0484 0.0761  321 LEU   B CD2 
4584 N N   . GLU   B 300 ? 0.3014 0.5397 0.2718 -0.0997 -0.0399 0.1403  322 GLU   B N   
4585 C CA  . GLU   B 300 ? 0.2839 0.5976 0.2978 -0.0828 -0.0612 0.1367  322 GLU   B CA  
4586 C C   . GLU   B 300 ? 0.2921 0.5946 0.3091 -0.1014 -0.0714 0.1494  322 GLU   B C   
4587 O O   . GLU   B 300 ? 0.2925 0.6275 0.3339 -0.1179 -0.0353 0.0833  322 GLU   B O   
4588 C CB  . GLU   B 300 ? 0.3267 0.6431 0.3318 -0.0438 -0.0597 0.1659  322 GLU   B CB  
4589 C CG  . GLU   B 300 ? 0.3688 0.6706 0.3198 -0.0219 -0.0952 0.1660  322 GLU   B CG  
4590 C CD  . GLU   B 300 ? 0.4000 0.7144 0.4107 -0.0298 -0.0587 0.2030  322 GLU   B CD  
4591 O OE1 . GLU   B 300 ? 0.3765 0.7346 0.3844 -0.0648 -0.0478 0.2470  322 GLU   B OE1 
4592 O OE2 . GLU   B 300 ? 0.4880 0.7585 0.4430 0.0394  -0.0519 0.1874  322 GLU   B OE2 
4593 N N   . ASN   B 301 ? 0.3148 0.5836 0.3393 -0.1251 -0.1039 0.1956  323 ASN   B N   
4594 C CA  . ASN   B 301 ? 0.3418 0.6378 0.3622 -0.1560 -0.1045 0.1876  323 ASN   B CA  
4595 C C   . ASN   B 301 ? 0.3500 0.6692 0.3578 -0.1661 -0.0999 0.1745  323 ASN   B C   
4596 O O   . ASN   B 301 ? 0.3689 0.7639 0.3305 -0.2182 -0.0687 0.1593  323 ASN   B O   
4597 C CB  . ASN   B 301 ? 0.3738 0.6803 0.3779 -0.1535 -0.1221 0.1904  323 ASN   B CB  
4598 C CG  . ASN   B 301 ? 0.4147 0.7010 0.4562 -0.1773 -0.1152 0.1981  323 ASN   B CG  
4599 O OD1 . ASN   B 301 ? 0.3379 0.7939 0.4954 -0.1851 -0.1087 0.1744  323 ASN   B OD1 
4600 N ND2 . ASN   B 301 ? 0.4783 0.6944 0.4510 -0.1703 -0.1201 0.1887  323 ASN   B ND2 
4601 N N   . ASP   B 302 ? 0.3794 0.6233 0.2972 -0.1433 -0.0839 0.1696  324 ASP   B N   
4602 C CA  . ASP   B 302 ? 0.3165 0.5918 0.2968 -0.1236 -0.0532 0.1637  324 ASP   B CA  
4603 C C   . ASP   B 302 ? 0.2757 0.6128 0.3001 -0.0906 -0.0373 0.1522  324 ASP   B C   
4604 O O   . ASP   B 302 ? 0.2592 0.5995 0.3186 -0.0612 -0.0333 0.1428  324 ASP   B O   
4605 C CB  . ASP   B 302 ? 0.3272 0.5858 0.2927 -0.1196 -0.0696 0.1504  324 ASP   B CB  
4606 C CG  . ASP   B 302 ? 0.3282 0.5434 0.2893 -0.1178 -0.0529 0.1443  324 ASP   B CG  
4607 O OD1 . ASP   B 302 ? 0.3727 0.5175 0.3008 -0.0732 -0.0607 0.1380  324 ASP   B OD1 
4608 O OD2 . ASP   B 302 ? 0.3508 0.5603 0.3220 -0.1331 -0.0582 0.1077  324 ASP   B OD2 
4609 N N   . LYS   B 303 ? 0.2584 0.6215 0.3157 -0.0841 -0.0121 0.1393  325 LYS   B N   
4610 C CA  . LYS   B 303 ? 0.2285 0.6286 0.2716 -0.0624 -0.0106 0.1212  325 LYS   B CA  
4611 C C   . LYS   B 303 ? 0.2031 0.5934 0.2726 -0.0641 -0.0028 0.1099  325 LYS   B C   
4612 O O   . LYS   B 303 ? 0.1963 0.6038 0.2415 -0.0519 0.0022  0.0822  325 LYS   B O   
4613 C CB  . LYS   B 303 ? 0.2530 0.6414 0.2758 -0.0628 -0.0017 0.1279  325 LYS   B CB  
4614 C CG  . LYS   B 303 ? 0.2561 0.6858 0.3081 -0.0733 0.0005  0.1403  325 LYS   B CG  
4615 C CD  . LYS   B 303 ? 0.2691 0.7179 0.3658 -0.0677 -0.0076 0.1530  325 LYS   B CD  
4616 C CE  . LYS   B 303 ? 0.3237 0.7814 0.3812 -0.0698 0.0003  0.1410  325 LYS   B CE  
4617 N NZ  . LYS   B 303 ? 0.3398 0.8275 0.4617 -0.0654 0.0025  0.1486  325 LYS   B NZ  
4618 N N   . THR   B 304 ? 0.2244 0.5946 0.2663 -0.0626 0.0049  0.1145  326 THR   B N   
4619 C CA  . THR   B 304 ? 0.2325 0.5949 0.2816 -0.0774 -0.0040 0.1125  326 THR   B CA  
4620 C C   . THR   B 304 ? 0.2392 0.5731 0.2658 -0.0625 0.0188  0.1273  326 THR   B C   
4621 O O   . THR   B 304 ? 0.2833 0.5356 0.2210 -0.0742 0.0262  0.1339  326 THR   B O   
4622 C CB  . THR   B 304 ? 0.2332 0.5955 0.2926 -0.0786 0.0013  0.1183  326 THR   B CB  
4623 O OG1 . THR   B 304 ? 0.2429 0.5652 0.3237 -0.0770 -0.0122 0.1390  326 THR   B OG1 
4624 C CG2 . THR   B 304 ? 0.2410 0.6222 0.3001 -0.0744 -0.0219 0.1070  326 THR   B CG2 
4625 N N   . ILE   B 305 ? 0.2006 0.5711 0.2485 -0.0645 0.0245  0.1114  327 ILE   B N   
4626 C CA  . ILE   B 305 ? 0.2006 0.5602 0.2867 -0.0577 0.0326  0.1151  327 ILE   B CA  
4627 C C   . ILE   B 305 ? 0.2315 0.5617 0.2902 -0.0830 0.0111  0.1170  327 ILE   B C   
4628 O O   . ILE   B 305 ? 0.2442 0.5928 0.3394 -0.0980 0.0515  0.1265  327 ILE   B O   
4629 C CB  . ILE   B 305 ? 0.1630 0.5463 0.2834 -0.0442 0.0311  0.1144  327 ILE   B CB  
4630 C CG1 . ILE   B 305 ? 0.1980 0.5499 0.2922 -0.0449 0.0517  0.1072  327 ILE   B CG1 
4631 C CG2 . ILE   B 305 ? 0.1448 0.5441 0.3136 -0.0498 0.0174  0.1196  327 ILE   B CG2 
4632 C CD1 . ILE   B 305 ? 0.2225 0.5409 0.2699 -0.0513 0.0732  0.1012  327 ILE   B CD1 
4633 N N   . LYS   B 306 ? 0.2562 0.5169 0.2846 -0.1126 -0.0282 0.1299  328 LYS   B N   
4634 C CA  . LYS   B 306 ? 0.2493 0.5133 0.3043 -0.1354 -0.0204 0.1325  328 LYS   B CA  
4635 C C   . LYS   B 306 ? 0.2660 0.4998 0.2934 -0.1475 -0.0125 0.1333  328 LYS   B C   
4636 O O   . LYS   B 306 ? 0.2799 0.4797 0.2512 -0.1554 -0.0076 0.1329  328 LYS   B O   
4637 C CB  . LYS   B 306 ? 0.2578 0.5131 0.3441 -0.1454 -0.0384 0.1459  328 LYS   B CB  
4638 C CG  . LYS   B 306 ? 0.2614 0.5375 0.3375 -0.1319 -0.0367 0.1544  328 LYS   B CG  
4639 C CD  . LYS   B 306 ? 0.2685 0.5776 0.3450 -0.1272 -0.0278 0.1496  328 LYS   B CD  
4640 C CE  . LYS   B 306 ? 0.2602 0.6175 0.3523 -0.1275 -0.0401 0.1384  328 LYS   B CE  
4641 N NZ  . LYS   B 306 ? 0.2424 0.6309 0.3897 -0.1301 -0.0486 0.1323  328 LYS   B NZ  
4642 N N   . LEU   B 307 ? 0.2413 0.4965 0.3082 -0.1511 -0.0013 0.1313  329 LEU   B N   
4643 C CA  . LEU   B 307 ? 0.2490 0.4887 0.3046 -0.1532 -0.0044 0.1233  329 LEU   B CA  
4644 C C   . LEU   B 307 ? 0.2795 0.4917 0.2750 -0.1698 -0.0221 0.1120  329 LEU   B C   
4645 O O   . LEU   B 307 ? 0.2785 0.4962 0.3248 -0.1670 -0.0093 0.1248  329 LEU   B O   
4646 C CB  . LEU   B 307 ? 0.2373 0.4765 0.3114 -0.1373 0.0251  0.1422  329 LEU   B CB  
4647 C CG  . LEU   B 307 ? 0.2493 0.4849 0.3694 -0.1220 0.0322  0.1209  329 LEU   B CG  
4648 C CD1 . LEU   B 307 ? 0.2446 0.4778 0.3818 -0.1032 0.0392  0.1406  329 LEU   B CD1 
4649 C CD2 . LEU   B 307 ? 0.2646 0.4932 0.3927 -0.1149 0.0209  0.1057  329 LEU   B CD2 
4650 N N   . TRP   B 308 ? 0.2825 0.4837 0.2882 -0.1889 -0.0541 0.0741  330 TRP   B N   
4651 C CA  . TRP   B 308 ? 0.3259 0.4936 0.3060 -0.1780 -0.0463 0.0926  330 TRP   B CA  
4652 C C   . TRP   B 308 ? 0.3205 0.5048 0.2948 -0.1845 -0.0309 0.0943  330 TRP   B C   
4653 O O   . TRP   B 308 ? 0.2932 0.5216 0.3377 -0.1932 -0.0242 0.1141  330 TRP   B O   
4654 C CB  . TRP   B 308 ? 0.3375 0.4871 0.2691 -0.2024 -0.0695 0.0819  330 TRP   B CB  
4655 C CG  . TRP   B 308 ? 0.3603 0.4982 0.2625 -0.2268 -0.0850 0.0826  330 TRP   B CG  
4656 C CD1 . TRP   B 308 ? 0.3777 0.5216 0.2435 -0.2362 -0.0896 0.0927  330 TRP   B CD1 
4657 C CD2 . TRP   B 308 ? 0.3870 0.5160 0.2913 -0.2478 -0.0979 0.0779  330 TRP   B CD2 
4658 N NE1 . TRP   B 308 ? 0.3880 0.5277 0.2524 -0.2430 -0.1013 0.0900  330 TRP   B NE1 
4659 C CE2 . TRP   B 308 ? 0.3891 0.5254 0.2788 -0.2378 -0.0965 0.0751  330 TRP   B CE2 
4660 C CE3 . TRP   B 308 ? 0.4130 0.5262 0.3452 -0.2544 -0.1125 0.0704  330 TRP   B CE3 
4661 C CZ2 . TRP   B 308 ? 0.3887 0.5133 0.2983 -0.2183 -0.1085 0.0833  330 TRP   B CZ2 
4662 C CZ3 . TRP   B 308 ? 0.4069 0.5104 0.3300 -0.2655 -0.0977 0.0825  330 TRP   B CZ3 
4663 C CH2 . TRP   B 308 ? 0.4072 0.5305 0.3392 -0.2260 -0.0976 0.0803  330 TRP   B CH2 
4664 N N   . LYS   B 309 ? 0.3053 0.5339 0.2961 -0.1874 -0.0069 0.1179  331 LYS   B N   
4665 C CA  . LYS   B 309 ? 0.3398 0.5482 0.3132 -0.1915 -0.0153 0.1277  331 LYS   B CA  
4666 C C   . LYS   B 309 ? 0.3970 0.5319 0.2986 -0.1930 -0.0235 0.1256  331 LYS   B C   
4667 O O   . LYS   B 309 ? 0.3715 0.5393 0.2781 -0.1759 -0.0153 0.1285  331 LYS   B O   
4668 C CB  . LYS   B 309 ? 0.3704 0.5916 0.3026 -0.1801 -0.0118 0.1291  331 LYS   B CB  
4669 C CG  . LYS   B 309 ? 0.3692 0.6192 0.3546 -0.1705 -0.0224 0.1493  331 LYS   B CG  
4670 C CD  . LYS   B 309 ? 0.3971 0.6192 0.3806 -0.2105 -0.0153 0.1328  331 LYS   B CD  
4671 C CE  . LYS   B 309 ? 0.3917 0.6501 0.4207 -0.2036 -0.0370 0.1294  331 LYS   B CE  
4672 N NZ  . LYS   B 309 ? 0.4827 0.6556 0.4286 -0.1929 -0.0214 0.1546  331 LYS   B NZ  
4673 N N   . SER   B 310 ? 0.4502 0.4813 0.2948 -0.2131 -0.0650 0.1309  332 SER   B N   
4674 C CA  . SER   B 310 ? 0.5163 0.4808 0.3134 -0.2309 -0.0750 0.1236  332 SER   B CA  
4675 C C   . SER   B 310 ? 0.5844 0.4967 0.3053 -0.2408 -0.0718 0.1394  332 SER   B C   
4676 O O   . SER   B 310 ? 0.6098 0.5195 0.2383 -0.2538 -0.0072 0.1132  332 SER   B O   
4677 C CB  . SER   B 310 ? 0.5146 0.4487 0.3225 -0.2302 -0.0763 0.1463  332 SER   B CB  
4678 O OG  . SER   B 310 ? 0.5364 0.4199 0.3524 -0.2316 -0.0966 0.1592  332 SER   B OG  
4679 N N   . ASP   B 311 ? 0.6763 0.5253 0.3638 -0.2146 -0.1171 0.1291  333 ASP   B N   
4680 C CA  . ASP   B 311 ? 0.7078 0.5568 0.3701 -0.1973 -0.1206 0.1482  333 ASP   B CA  
4681 C C   . ASP   B 311 ? 0.7287 0.5439 0.3806 -0.1756 -0.1791 0.1454  333 ASP   B C   
4682 O O   . ASP   B 311 ? 0.7557 0.5748 0.4115 -0.1617 -0.1994 0.1720  333 ASP   B O   
4683 C CB  . ASP   B 311 ? 0.7094 0.5377 0.4169 -0.2006 -0.1206 0.1087  333 ASP   B CB  
4684 C CG  . ASP   B 311 ? 0.7218 0.5503 0.4150 -0.2183 -0.0995 0.0722  333 ASP   B CG  
4685 O OD1 . ASP   B 311 ? 0.7446 0.6221 0.4866 -0.1738 -0.0644 0.0411  333 ASP   B OD1 
4686 O OD2 . ASP   B 311 ? 0.7379 0.4795 0.4059 -0.2059 -0.0753 0.0497  333 ASP   B OD2 
4687 N N   . CYS   B 312 ? 0.7550 0.5275 0.4197 -0.1354 -0.1649 0.1589  334 CYS   B N   
4688 C CA  . CYS   B 312 ? 0.8091 0.5135 0.4946 -0.1301 -0.1752 0.0968  334 CYS   B CA  
4689 C C   . CYS   B 312 ? 0.7430 0.5182 0.5390 -0.1314 -0.1400 0.0743  334 CYS   B C   
4690 O O   . CYS   B 312 ? 0.6947 0.4470 0.4499 -0.1755 -0.0831 0.0943  334 CYS   B O   
4691 C CB  . CYS   B 312 ? 0.9134 0.5570 0.5249 -0.1078 -0.1982 0.0657  334 CYS   B CB  
4692 S SG  . CYS   B 312 ? 1.0445 0.5227 0.5183 -0.1333 -0.2448 0.0836  334 CYS   B SG  
4693 O OXT . CYS   B 312 ? 0.7476 0.5281 0.6517 -0.1030 -0.1374 0.0267  334 CYS   B OXT 
4694 C C4  . A1A16 C .   ? 0.2804 0.4866 0.2387 0.0181  0.0063  0.0431  401 A1A16 A C4  
4695 C C5  . A1A16 C .   ? 0.2833 0.4497 0.2468 0.0278  0.0035  0.0260  401 A1A16 A C5  
4696 C C7  . A1A16 C .   ? 0.2285 0.4436 0.2741 0.0202  0.0342  0.0323  401 A1A16 A C7  
4697 C C8  . A1A16 C .   ? 0.2776 0.4342 0.2575 0.0326  0.0367  0.0425  401 A1A16 A C8  
4698 C C10 . A1A16 C .   ? 0.2515 0.4228 0.2391 0.0308  0.0105  0.0628  401 A1A16 A C10 
4699 C C13 . A1A16 C .   ? 0.2846 0.4080 0.2423 0.0284  0.0052  0.0793  401 A1A16 A C13 
4700 C C17 . A1A16 C .   ? 0.2873 0.4221 0.2264 0.0324  -0.0006 0.0342  401 A1A16 A C17 
4701 C C20 . A1A16 C .   ? 0.2475 0.3866 0.2403 0.0222  0.0121  0.0379  401 A1A16 A C20 
4702 C C21 . A1A16 C .   ? 0.2740 0.4013 0.3213 0.0034  0.0054  0.0630  401 A1A16 A C21 
4703 C C22 . A1A16 C .   ? 0.2793 0.4218 0.4304 -0.0089 0.0103  0.0466  401 A1A16 A C22 
4704 C C24 . A1A16 C .   ? 0.3367 0.4432 0.5248 -0.0701 0.0370  0.0599  401 A1A16 A C24 
4705 C C28 . A1A16 C .   ? 0.2628 0.5073 0.3531 0.0265  0.0513  0.0521  401 A1A16 A C28 
4706 C C1  . A1A16 C .   ? 0.3495 0.5396 0.3685 0.0038  0.0304  0.0444  401 A1A16 A C1  
4707 C C2  . A1A16 C .   ? 0.3195 0.4973 0.3278 0.0036  0.0167  0.0586  401 A1A16 A C2  
4708 C C3  . A1A16 C .   ? 0.3281 0.4973 0.2997 0.0112  0.0130  0.0662  401 A1A16 A C3  
4709 N N6  . A1A16 C .   ? 0.2368 0.4562 0.2515 0.0277  0.0095  0.0253  401 A1A16 A N6  
4710 C C9  . A1A16 C .   ? 0.2524 0.4492 0.2725 0.0202  0.0262  0.0323  401 A1A16 A C9  
4711 C C11 . A1A16 C .   ? 0.2525 0.4446 0.2388 0.0178  0.0043  0.0580  401 A1A16 A C11 
4712 S S12 . A1A16 C .   ? 0.3133 0.4460 0.2268 0.0179  -0.0036 0.0800  401 A1A16 A S12 
4713 C C14 . A1A16 C .   ? 0.2516 0.4189 0.2445 0.0274  0.0065  0.0792  401 A1A16 A C14 
4714 O O15 . A1A16 C .   ? 0.3183 0.4045 0.2374 0.0405  -0.0068 0.0254  401 A1A16 A O15 
4715 N N16 . A1A16 C .   ? 0.2658 0.4478 0.2398 0.0279  -0.0010 0.0520  401 A1A16 A N16 
4716 C C18 . A1A16 C .   ? 0.2702 0.3758 0.2200 0.0411  0.0060  0.0263  401 A1A16 A C18 
4717 C C19 . A1A16 C .   ? 0.2526 0.3785 0.2389 0.0319  0.0169  0.0231  401 A1A16 A C19 
4718 N N23 . A1A16 C .   ? 0.3060 0.4305 0.4952 -0.0263 0.0227  0.0640  401 A1A16 A N23 
4719 C C25 . A1A16 C .   ? 0.3081 0.4331 0.5024 -0.0785 0.0365  0.0691  401 A1A16 A C25 
4720 N N26 . A1A16 C .   ? 0.2243 0.4626 0.3944 -0.0320 0.0107  0.0598  401 A1A16 A N26 
4721 C C27 . A1A16 C .   ? 0.2487 0.4486 0.3507 0.0131  0.0268  0.0570  401 A1A16 A C27 
4722 F F29 . A1A16 C .   ? 0.3002 0.5051 0.2879 0.0165  0.0336  0.0696  401 A1A16 A F29 
4723 F F30 . A1A16 C .   ? 0.2656 0.5184 0.3531 0.0967  0.0752  0.0383  401 A1A16 A F30 
4724 F F31 . A1A16 C .   ? 0.2953 0.5919 0.3442 0.0121  0.0642  0.0628  401 A1A16 A F31 
4725 C C32 . A1A16 C .   ? 0.2406 0.3386 0.2431 0.0263  0.0125  0.0311  401 A1A16 A C32 
4726 C C33 . A1A16 C .   ? 0.2631 0.3398 0.2378 0.0445  0.0084  0.0250  401 A1A16 A C33 
4727 C C34 . A1A16 C .   ? 0.2484 0.3360 0.2434 0.0437  0.0238  0.0261  401 A1A16 A C34 
4728 N N35 . A1A16 C .   ? 0.2470 0.3163 0.2679 0.0469  0.0190  0.0261  401 A1A16 A N35 
4729 C C36 . A1A16 C .   ? 0.2370 0.2818 0.2469 0.0512  0.0026  0.0355  401 A1A16 A C36 
4730 N N37 . A1A16 C .   ? 0.2454 0.2952 0.2816 0.0469  0.0099  0.0267  401 A1A16 A N37 
4731 C C38 . A1A16 C .   ? 0.2323 0.2863 0.2780 0.0472  0.0126  0.0429  401 A1A16 A C38 
4732 C C39 . A1A16 C .   ? 0.2319 0.2780 0.2646 0.0508  0.0214  0.0440  401 A1A16 A C39 
4733 C C40 . A1A16 C .   ? 0.2676 0.3564 0.2272 0.0369  0.0220  0.0194  401 A1A16 A C40 
4734 O O41 . A1A16 C .   ? 0.2723 0.4177 0.2034 0.0345  -0.0025 0.0424  401 A1A16 A O41 
4735 C C1  . EDO   D .   ? 0.5417 0.4263 0.5316 -0.0921 -0.0497 0.0401  402 EDO   A C1  
4736 O O1  . EDO   D .   ? 0.5653 0.4166 0.5324 -0.0898 -0.0730 0.0058  402 EDO   A O1  
4737 C C2  . EDO   D .   ? 0.5323 0.4266 0.4783 -0.0757 -0.0834 0.0349  402 EDO   A C2  
4738 O O2  . EDO   D .   ? 0.5423 0.4085 0.5309 -0.0568 -0.1009 0.0636  402 EDO   A O2  
4739 C C1  . EDO   E .   ? 0.6440 0.3994 0.6036 0.0030  0.0088  0.0949  403 EDO   A C1  
4740 O O1  . EDO   E .   ? 0.6293 0.3298 0.5309 -0.0185 -0.0151 0.0894  403 EDO   A O1  
4741 C C2  . EDO   E .   ? 0.6648 0.4274 0.6519 -0.0104 0.0023  0.0961  403 EDO   A C2  
4742 O O2  . EDO   E .   ? 0.7448 0.4489 0.7147 0.0047  -0.0113 0.0824  403 EDO   A O2  
4743 C C4  . A1A16 F .   ? 0.2837 0.4293 0.2647 -0.0315 0.0490  0.0799  401 A1A16 B C4  
4744 C C5  . A1A16 F .   ? 0.2799 0.4005 0.2655 -0.0212 0.0499  0.0677  401 A1A16 B C5  
4745 C C7  . A1A16 F .   ? 0.3124 0.3741 0.3039 -0.0065 0.0422  0.0636  401 A1A16 B C7  
4746 C C8  . A1A16 F .   ? 0.3168 0.3556 0.2959 -0.0077 0.0369  0.0597  401 A1A16 B C8  
4747 C C10 . A1A16 F .   ? 0.2745 0.3663 0.2550 0.0071  0.0657  0.0978  401 A1A16 B C10 
4748 C C13 . A1A16 F .   ? 0.2800 0.3895 0.2388 0.0161  0.0534  0.0873  401 A1A16 B C13 
4749 C C17 . A1A16 F .   ? 0.2387 0.3587 0.2505 -0.0520 0.0446  0.0858  401 A1A16 B C17 
4750 C C20 . A1A16 F .   ? 0.2393 0.3448 0.2542 -0.0382 0.0024  0.0621  401 A1A16 B C20 
4751 C C21 . A1A16 F .   ? 0.2568 0.3826 0.3261 -0.0154 -0.0038 0.0575  401 A1A16 B C21 
4752 C C22 . A1A16 F .   ? 0.2640 0.3960 0.4028 -0.0300 -0.0044 0.0383  401 A1A16 B C22 
4753 C C24 . A1A16 F .   ? 0.2929 0.4156 0.4870 0.0089  -0.0271 0.0202  401 A1A16 B C24 
4754 C C28 . A1A16 F .   ? 0.2500 0.4670 0.3413 -0.0227 -0.0104 0.0412  401 A1A16 B C28 
4755 C C1  . A1A16 F .   ? 0.3395 0.4899 0.3352 -0.0686 0.0570  0.0735  401 A1A16 B C1  
4756 C C2  . A1A16 F .   ? 0.3248 0.4804 0.3185 -0.0611 0.0434  0.0846  401 A1A16 B C2  
4757 C C3  . A1A16 F .   ? 0.3170 0.4689 0.2768 -0.0450 0.0301  0.0895  401 A1A16 B C3  
4758 N N6  . A1A16 F .   ? 0.2981 0.3632 0.2497 -0.0041 0.0614  0.0723  401 A1A16 B N6  
4759 C C9  . A1A16 F .   ? 0.2824 0.3691 0.2562 0.0125  0.0625  0.0819  401 A1A16 B C9  
4760 C C11 . A1A16 F .   ? 0.2821 0.3786 0.2861 0.0094  0.0541  0.0702  401 A1A16 B C11 
4761 S S12 . A1A16 F .   ? 0.3328 0.4117 0.2705 0.0208  0.0502  0.1037  401 A1A16 B S12 
4762 C C14 . A1A16 F .   ? 0.2694 0.3710 0.2219 0.0052  0.0626  0.1049  401 A1A16 B C14 
4763 O O15 . A1A16 F .   ? 0.3048 0.3854 0.2569 -0.0125 0.0625  0.0624  401 A1A16 B O15 
4764 N N16 . A1A16 F .   ? 0.2501 0.3907 0.2497 -0.0415 0.0553  0.0958  401 A1A16 B N16 
4765 C C18 . A1A16 F .   ? 0.2424 0.3490 0.2402 -0.0381 0.0254  0.0740  401 A1A16 B C18 
4766 C C19 . A1A16 F .   ? 0.2351 0.3328 0.2566 -0.0325 0.0115  0.0640  401 A1A16 B C19 
4767 N N23 . A1A16 F .   ? 0.2758 0.4004 0.4656 -0.0191 -0.0149 0.0364  401 A1A16 B N23 
4768 C C25 . A1A16 F .   ? 0.2920 0.4258 0.4828 0.0158  0.0032  0.0075  401 A1A16 B C25 
4769 N N26 . A1A16 F .   ? 0.2429 0.4302 0.4052 0.0084  -0.0009 0.0507  401 A1A16 B N26 
4770 C C27 . A1A16 F .   ? 0.2629 0.4186 0.3448 -0.0253 0.0015  0.0464  401 A1A16 B C27 
4771 F F29 . A1A16 F .   ? 0.2799 0.4446 0.2897 -0.0172 0.0198  0.0587  401 A1A16 B F29 
4772 F F30 . A1A16 F .   ? 0.2996 0.4590 0.3375 -0.0831 -0.0230 0.0047  401 A1A16 B F30 
4773 F F31 . A1A16 F .   ? 0.2838 0.5364 0.3210 0.0106  -0.0293 0.0444  401 A1A16 B F31 
4774 C C32 . A1A16 F .   ? 0.2335 0.3300 0.2409 -0.0434 0.0235  0.0599  401 A1A16 B C32 
4775 C C33 . A1A16 F .   ? 0.2308 0.3253 0.2279 -0.0430 0.0117  0.0624  401 A1A16 B C33 
4776 C C34 . A1A16 F .   ? 0.2310 0.3237 0.2184 -0.0477 0.0135  0.0527  401 A1A16 B C34 
4777 N N35 . A1A16 F .   ? 0.2375 0.3043 0.2188 -0.0469 0.0068  0.0475  401 A1A16 B N35 
4778 C C36 . A1A16 F .   ? 0.2355 0.3009 0.2192 -0.0474 0.0004  0.0383  401 A1A16 B C36 
4779 N N37 . A1A16 F .   ? 0.2430 0.3188 0.2719 -0.0457 -0.0046 0.0323  401 A1A16 B N37 
4780 C C38 . A1A16 F .   ? 0.2293 0.3098 0.2618 -0.0462 -0.0034 0.0356  401 A1A16 B C38 
4781 C C39 . A1A16 F .   ? 0.2358 0.3202 0.2446 -0.0385 0.0051  0.0342  401 A1A16 B C39 
4782 C C40 . A1A16 F .   ? 0.2246 0.3351 0.2255 -0.0402 0.0274  0.0743  401 A1A16 B C40 
4783 O O41 . A1A16 F .   ? 0.2887 0.3102 0.2321 -0.0767 0.0352  0.0847  401 A1A16 B O41 
4784 C C1  . EDO   G .   ? 0.4076 0.6818 0.5501 -0.1731 -0.0625 -0.0368 402 EDO   B C1  
4785 O O1  . EDO   G .   ? 0.4788 0.6762 0.6068 -0.1334 -0.0801 -0.0847 402 EDO   B O1  
4786 C C2  . EDO   G .   ? 0.3951 0.6853 0.5186 -0.1340 -0.0762 -0.0009 402 EDO   B C2  
4787 O O2  . EDO   G .   ? 0.4291 0.6879 0.4821 -0.1264 -0.0538 0.0295  402 EDO   B O2  
4788 C C1  . EDO   H .   ? 0.7194 0.4116 0.5268 0.1233  -0.0508 0.1326  403 EDO   B C1  
4789 O O1  . EDO   H .   ? 0.7133 0.4318 0.4909 0.1145  -0.0403 0.1142  403 EDO   B O1  
4790 C C2  . EDO   H .   ? 0.6931 0.3872 0.5376 0.1426  -0.0651 0.1108  403 EDO   B C2  
4791 O O2  . EDO   H .   ? 0.7441 0.4007 0.6044 0.1472  -0.0701 0.0969  403 EDO   B O2  
4792 C C1  . EDO   I .   ? 0.7980 0.5239 0.5375 -0.0410 -0.2786 0.0313  404 EDO   B C1  
4793 O O1  . EDO   I .   ? 0.7341 0.4435 0.5288 -0.0714 -0.2909 0.0654  404 EDO   B O1  
4794 C C2  . EDO   I .   ? 0.8342 0.5374 0.5701 -0.0342 -0.2453 0.0558  404 EDO   B C2  
4795 O O2  . EDO   I .   ? 0.8553 0.6129 0.5676 -0.0112 -0.2451 0.0544  404 EDO   B O2  
4796 O O   . HOH   J .   ? 0.3915 0.3384 0.6439 -0.0442 -0.2478 0.1040  501 HOH   A O   
4797 O O   . HOH   J .   ? 0.4512 0.5882 0.5959 0.0041  0.1243  0.1159  502 HOH   A O   
4798 O O   . HOH   J .   ? 0.2995 0.4376 0.4288 -0.0354 0.0139  0.0112  503 HOH   A O   
4799 O O   . HOH   J .   ? 0.3032 1.0271 0.5580 0.1423  -0.0721 0.0303  504 HOH   A O   
4800 O O   . HOH   J .   ? 0.1773 0.3373 0.2193 0.0090  0.0079  0.0636  505 HOH   A O   
4801 O O   . HOH   J .   ? 0.4933 0.7801 0.3408 0.0987  0.0156  -0.0365 506 HOH   A O   
4802 O O   . HOH   J .   ? 0.2275 0.3224 0.2708 -0.0164 0.0162  0.0297  507 HOH   A O   
4803 O O   . HOH   J .   ? 0.3423 0.7189 0.2837 0.1574  0.0539  0.0448  508 HOH   A O   
4804 O O   . HOH   J .   ? 0.4292 0.4151 0.6959 0.0116  -0.1314 0.2028  509 HOH   A O   
4805 O O   . HOH   J .   ? 0.5082 0.3005 0.7615 -0.0655 -0.2008 0.0298  510 HOH   A O   
4806 O O   . HOH   J .   ? 0.5763 0.4943 0.3708 0.1421  -0.0769 0.1182  511 HOH   A O   
4807 O O   . HOH   J .   ? 0.1798 0.3029 0.2126 0.0268  0.0046  0.1092  512 HOH   A O   
4808 O O   . HOH   J .   ? 0.2345 0.6146 0.6231 -0.1115 -0.0861 0.0469  513 HOH   A O   
4809 O O   . HOH   J .   ? 0.6926 0.6011 0.6711 -0.0158 -0.1442 0.0412  514 HOH   A O   
4810 O O   . HOH   J .   ? 0.4269 1.2010 0.3189 0.1668  0.0602  0.0156  515 HOH   A O   
4811 O O   . HOH   J .   ? 0.4150 0.5284 0.8860 0.2164  0.0113  -0.0934 516 HOH   A O   
4812 O O   . HOH   J .   ? 0.4297 0.6082 0.4100 0.0885  -0.0421 0.1338  517 HOH   A O   
4813 O O   . HOH   J .   ? 0.2665 0.4328 0.3677 0.0328  -0.0031 0.0839  518 HOH   A O   
4814 O O   . HOH   J .   ? 0.2739 0.3784 0.5451 0.0359  0.0369  0.0389  519 HOH   A O   
4815 O O   . HOH   J .   ? 0.3116 0.5544 0.4653 -0.1008 0.1065  0.0152  520 HOH   A O   
4816 O O   . HOH   J .   ? 0.3350 0.2680 0.2615 -0.0028 -0.0983 0.0225  521 HOH   A O   
4817 O O   . HOH   J .   ? 0.3225 0.4946 0.3018 0.0133  -0.0047 0.1226  522 HOH   A O   
4818 O O   . HOH   J .   ? 0.4178 0.5187 0.5265 -0.1590 -0.0049 0.1455  523 HOH   A O   
4819 O O   . HOH   J .   ? 0.3826 0.8687 0.2706 -0.0648 -0.0039 0.1203  524 HOH   A O   
4820 O O   . HOH   J .   ? 0.2433 0.3219 0.1853 0.0389  0.0024  -0.0002 525 HOH   A O   
4821 O O   . HOH   J .   ? 0.6215 0.8780 0.4178 0.0764  -0.0716 0.0034  526 HOH   A O   
4822 O O   . HOH   J .   ? 0.2737 0.5066 0.5921 -0.0511 -0.0226 -0.0569 527 HOH   A O   
4823 O O   . HOH   J .   ? 0.5418 0.2533 0.4771 0.0108  -0.1179 -0.0099 528 HOH   A O   
4824 O O   . HOH   J .   ? 0.3849 0.4758 0.4756 0.1938  -0.0882 -0.0177 529 HOH   A O   
4825 O O   . HOH   J .   ? 0.4866 0.3631 0.4261 -0.1144 0.0986  0.0155  530 HOH   A O   
4826 O O   . HOH   J .   ? 0.1905 0.5096 0.3044 0.0070  0.0024  0.1086  531 HOH   A O   
4827 O O   . HOH   J .   ? 0.3074 0.5195 0.2787 0.1240  -0.0778 0.0602  532 HOH   A O   
4828 O O   . HOH   J .   ? 0.2414 0.3260 0.5267 -0.0868 0.0795  0.0495  533 HOH   A O   
4829 O O   . HOH   J .   ? 0.4127 0.3329 0.2676 -0.0022 -0.0694 -0.0631 534 HOH   A O   
4830 O O   . HOH   J .   ? 0.6443 0.4300 0.5235 -0.2250 0.1918  -0.0825 535 HOH   A O   
4831 O O   . HOH   J .   ? 0.2594 0.3910 0.2662 0.0018  0.0131  0.0225  536 HOH   A O   
4832 O O   . HOH   J .   ? 0.2279 0.4718 0.2767 -0.0425 0.0077  0.1373  537 HOH   A O   
4833 O O   . HOH   J .   ? 0.3333 0.3489 0.3909 0.0570  0.0372  -0.0076 538 HOH   A O   
4834 O O   . HOH   J .   ? 0.7088 0.8586 0.2256 -0.0818 -0.1843 0.0186  539 HOH   A O   
4835 O O   . HOH   J .   ? 0.2893 0.2831 0.2473 -0.0141 -0.0597 0.0572  540 HOH   A O   
4836 O O   . HOH   J .   ? 0.2206 0.3366 0.3042 -0.0529 0.0180  0.0424  541 HOH   A O   
4837 O O   . HOH   J .   ? 0.6564 0.6789 0.3456 0.2150  0.0476  0.1059  542 HOH   A O   
4838 O O   . HOH   J .   ? 0.2646 0.4515 0.4511 -0.0014 0.0163  0.1321  543 HOH   A O   
4839 O O   . HOH   J .   ? 0.4384 0.4522 0.7849 -0.0928 0.0896  -0.0070 544 HOH   A O   
4840 O O   . HOH   J .   ? 0.2781 0.3846 0.2303 -0.0086 0.0098  0.0790  545 HOH   A O   
4841 O O   . HOH   J .   ? 0.2366 0.2526 0.2757 -0.0125 -0.0104 0.0266  546 HOH   A O   
4842 O O   . HOH   J .   ? 0.4704 0.5504 0.3568 -0.1859 0.0030  0.1551  547 HOH   A O   
4843 O O   . HOH   J .   ? 0.4858 0.4585 0.3474 -0.1150 0.0613  -0.0712 548 HOH   A O   
4844 O O   . HOH   J .   ? 0.4465 0.6221 0.3033 0.0637  -0.0064 0.1253  549 HOH   A O   
4845 O O   . HOH   J .   ? 0.3201 0.4046 0.4362 -0.0592 0.1412  0.0022  550 HOH   A O   
4846 O O   . HOH   J .   ? 0.2891 0.5204 0.4126 0.0063  -0.0813 0.0726  551 HOH   A O   
4847 O O   . HOH   J .   ? 0.2732 0.4313 0.2119 -0.0156 -0.0595 -0.0188 552 HOH   A O   
4848 O O   . HOH   J .   ? 0.2701 0.3876 0.3892 0.0773  0.0822  0.1070  553 HOH   A O   
4849 O O   . HOH   J .   ? 0.3176 0.4314 0.3284 0.0665  0.0189  0.1414  554 HOH   A O   
4850 O O   . HOH   J .   ? 0.4339 0.7643 0.2600 0.1240  -0.0812 0.1367  555 HOH   A O   
4851 O O   . HOH   J .   ? 0.9074 0.3408 0.5450 0.1938  0.1189  -0.0274 556 HOH   A O   
4852 O O   . HOH   J .   ? 0.2785 0.2903 0.1907 -0.0029 0.0000  0.0099  557 HOH   A O   
4853 O O   . HOH   J .   ? 0.1861 0.3214 0.3203 0.0449  0.0295  0.0961  558 HOH   A O   
4854 O O   . HOH   J .   ? 0.5556 0.3650 0.2882 -0.1748 -0.0036 0.0028  559 HOH   A O   
4855 O O   . HOH   J .   ? 0.2771 0.5212 0.4287 0.0286  0.0276  0.1436  560 HOH   A O   
4856 O O   . HOH   J .   ? 0.2857 0.5425 0.3111 0.1064  0.0563  0.0785  561 HOH   A O   
4857 O O   . HOH   J .   ? 0.3707 0.3978 0.3522 -0.1116 -0.0554 0.1596  562 HOH   A O   
4858 O O   . HOH   J .   ? 0.4258 0.8227 0.2857 0.1480  0.0306  0.0990  563 HOH   A O   
4859 O O   . HOH   J .   ? 0.2267 0.4535 0.4024 -0.0308 0.0790  0.0413  564 HOH   A O   
4860 O O   . HOH   J .   ? 0.2427 0.4255 0.2675 0.0372  0.0004  0.0718  565 HOH   A O   
4861 O O   . HOH   J .   ? 0.1907 0.3540 0.2438 -0.1046 0.0175  0.0808  566 HOH   A O   
4862 O O   . HOH   J .   ? 0.2282 0.3221 0.1652 0.0032  0.0130  0.1006  567 HOH   A O   
4863 O O   . HOH   J .   ? 0.4499 0.4724 0.2211 0.1774  0.0283  0.0925  568 HOH   A O   
4864 O O   . HOH   J .   ? 0.5374 0.4721 0.5284 -0.0064 -0.0319 -0.0668 569 HOH   A O   
4865 O O   . HOH   J .   ? 0.4987 0.3858 0.5015 -0.0725 0.0533  0.2444  570 HOH   A O   
4866 O O   . HOH   J .   ? 0.5133 0.3240 0.5095 -0.0313 -0.1890 -0.1127 571 HOH   A O   
4867 O O   . HOH   J .   ? 0.3186 0.3263 0.3235 -0.0410 0.0453  -0.0290 572 HOH   A O   
4868 O O   . HOH   J .   ? 0.4583 0.3135 0.3117 0.0322  -0.0970 -0.0724 573 HOH   A O   
4869 O O   . HOH   J .   ? 0.4386 0.7864 0.3856 -0.1250 0.0104  -0.1461 574 HOH   A O   
4870 O O   . HOH   J .   ? 0.2317 0.3467 0.3296 -0.0455 0.0809  0.0179  575 HOH   A O   
4871 O O   . HOH   J .   ? 0.8994 0.9400 0.2837 0.3941  -0.2060 -0.3611 576 HOH   A O   
4872 O O   . HOH   J .   ? 0.3166 0.2633 0.2170 -0.0207 -0.0344 0.0016  577 HOH   A O   
4873 O O   . HOH   J .   ? 0.5645 0.4547 0.5821 -0.1090 -0.2308 0.1465  578 HOH   A O   
4874 O O   . HOH   J .   ? 0.4430 0.4661 0.3063 -0.0809 0.0584  0.0985  579 HOH   A O   
4875 O O   . HOH   J .   ? 0.2955 0.7967 0.7767 0.3350  0.0669  0.0798  580 HOH   A O   
4876 O O   . HOH   J .   ? 0.6393 0.9047 0.3083 0.2690  -0.0584 0.0216  581 HOH   A O   
4877 O O   . HOH   J .   ? 0.5513 0.4979 0.5451 -0.0757 -0.1726 -0.0853 582 HOH   A O   
4878 O O   . HOH   J .   ? 0.2874 0.4427 0.6886 -0.1470 -0.0772 0.2199  583 HOH   A O   
4879 O O   . HOH   J .   ? 0.3132 0.2659 0.3141 -0.0374 0.0220  0.1050  584 HOH   A O   
4880 O O   . HOH   J .   ? 0.7219 0.5093 0.6101 0.1209  -0.1291 -0.1929 585 HOH   A O   
4881 O O   . HOH   J .   ? 0.4359 0.2702 0.2203 -0.0493 -0.0508 0.0532  586 HOH   A O   
4882 O O   . HOH   J .   ? 0.4257 0.4456 0.2028 0.0002  0.0141  -0.0183 587 HOH   A O   
4883 O O   . HOH   J .   ? 0.3240 0.2771 0.2093 0.0331  -0.0447 -0.0045 588 HOH   A O   
4884 O O   . HOH   J .   ? 0.2976 0.6756 0.3514 0.0843  0.0441  0.2669  589 HOH   A O   
4885 O O   . HOH   J .   ? 0.4440 0.4101 0.3778 -0.0131 -0.0634 -0.0090 590 HOH   A O   
4886 O O   . HOH   J .   ? 0.6049 0.3675 0.3467 -0.0673 0.0198  -0.0312 591 HOH   A O   
4887 O O   . HOH   J .   ? 0.4255 0.2826 0.4296 -0.0701 0.0975  0.0734  592 HOH   A O   
4888 O O   . HOH   J .   ? 0.2376 0.4483 0.2047 -0.0612 0.0417  0.1007  593 HOH   A O   
4889 O O   . HOH   J .   ? 0.7967 0.4033 0.7132 -0.1230 -0.0403 -0.0767 594 HOH   A O   
4890 O O   . HOH   J .   ? 0.7618 0.3627 0.6119 0.2735  0.2144  0.1426  595 HOH   A O   
4891 O O   . HOH   J .   ? 0.5365 0.3207 0.6589 -0.0070 0.1911  0.1045  596 HOH   A O   
4892 O O   . HOH   J .   ? 0.2608 0.5041 0.4619 -0.1139 -0.1216 0.1784  597 HOH   A O   
4893 O O   . HOH   J .   ? 0.3166 0.2642 0.2906 0.0276  -0.0635 -0.0252 598 HOH   A O   
4894 O O   . HOH   J .   ? 0.4163 0.4227 0.1995 -0.0283 0.1315  0.0082  599 HOH   A O   
4895 O O   . HOH   J .   ? 0.7027 0.7499 0.3983 0.0404  0.0615  0.3741  600 HOH   A O   
4896 O O   . HOH   J .   ? 0.1960 0.6156 0.2164 -0.0599 0.0983  0.0523  601 HOH   A O   
4897 O O   . HOH   J .   ? 1.0988 0.4101 0.5253 -0.0836 -0.1921 0.0296  602 HOH   A O   
4898 O O   . HOH   J .   ? 0.2866 0.3630 0.4085 0.0653  0.0132  -0.0204 603 HOH   A O   
4899 O O   . HOH   J .   ? 0.3320 0.3112 0.4572 -0.0830 -0.0489 0.0343  604 HOH   A O   
4900 O O   . HOH   J .   ? 0.2936 0.4829 0.4049 0.1587  -0.0269 -0.0567 605 HOH   A O   
4901 O O   . HOH   J .   ? 0.3243 0.4814 0.3439 0.0781  0.0851  0.0641  606 HOH   A O   
4902 O O   . HOH   J .   ? 0.7648 0.3829 0.2731 -0.2276 0.1091  -0.0078 607 HOH   A O   
4903 O O   . HOH   J .   ? 0.3357 0.4189 0.3397 0.1233  -0.0588 0.0895  608 HOH   A O   
4904 O O   . HOH   J .   ? 0.5374 0.3090 0.3382 0.0899  -0.0708 0.0473  609 HOH   A O   
4905 O O   . HOH   J .   ? 0.3137 0.3610 0.1974 -0.0762 -0.0059 0.0835  610 HOH   A O   
4906 O O   . HOH   J .   ? 0.3275 0.4021 0.2450 0.0792  -0.0197 -0.0410 611 HOH   A O   
4907 O O   . HOH   J .   ? 0.3539 0.6731 0.4660 -0.0154 -0.0268 0.2972  612 HOH   A O   
4908 O O   . HOH   J .   ? 0.5806 0.3418 0.3830 -0.1088 0.0687  0.0483  613 HOH   A O   
4909 O O   . HOH   J .   ? 0.2652 0.3801 0.1863 0.0478  -0.0271 0.0516  614 HOH   A O   
4910 O O   . HOH   J .   ? 0.1896 0.3314 0.2363 -0.0311 0.0606  0.0488  615 HOH   A O   
4911 O O   . HOH   J .   ? 0.7190 0.6281 0.2775 0.2727  0.1255  0.1499  616 HOH   A O   
4912 O O   . HOH   J .   ? 0.3876 0.3073 0.2429 0.0356  0.0711  0.1452  617 HOH   A O   
4913 O O   . HOH   J .   ? 0.8623 0.3823 0.5501 0.1439  -0.0565 0.0835  618 HOH   A O   
4914 O O   . HOH   J .   ? 0.4482 0.2732 0.2574 -0.0460 0.0022  -0.0178 619 HOH   A O   
4915 O O   . HOH   J .   ? 0.3992 0.2036 0.2911 -0.0724 -0.0563 -0.0131 620 HOH   A O   
4916 O O   . HOH   J .   ? 0.2872 0.3034 0.3007 0.0692  -0.0260 -0.0808 621 HOH   A O   
4917 O O   . HOH   J .   ? 0.3164 0.5778 0.3347 0.0167  -0.0275 0.1649  622 HOH   A O   
4918 O O   . HOH   J .   ? 0.2512 0.2975 0.4341 -0.0522 0.0829  0.0719  623 HOH   A O   
4919 O O   . HOH   J .   ? 0.6374 0.3686 1.3455 0.0718  -0.2518 -0.1749 624 HOH   A O   
4920 O O   . HOH   J .   ? 0.2717 0.2532 0.2381 -0.0076 -0.0131 0.0395  625 HOH   A O   
4921 O O   . HOH   J .   ? 0.3311 1.0753 0.4374 0.0173  0.0182  0.2633  626 HOH   A O   
4922 O O   . HOH   J .   ? 0.7833 0.2618 0.6600 -0.1478 -0.0061 -0.0545 627 HOH   A O   
4923 O O   . HOH   J .   ? 0.9290 0.3187 0.2535 -0.2263 -0.0581 -0.0052 628 HOH   A O   
4924 O O   . HOH   J .   ? 0.3785 0.6923 0.7769 -0.1089 0.0087  -0.3061 629 HOH   A O   
4925 O O   . HOH   J .   ? 0.3962 0.5835 0.4344 0.1229  -0.0255 -0.1794 630 HOH   A O   
4926 O O   . HOH   J .   ? 0.4146 0.3930 0.4797 0.0535  0.0806  -0.1564 631 HOH   A O   
4927 O O   . HOH   J .   ? 0.3118 0.3567 0.1959 0.0249  -0.0162 0.0803  632 HOH   A O   
4928 O O   . HOH   J .   ? 0.3085 0.8893 0.5741 -0.2661 -0.1051 -0.0512 633 HOH   A O   
4929 O O   . HOH   J .   ? 0.3560 0.3454 0.3260 -0.0862 -0.0103 0.1143  634 HOH   A O   
4930 O O   . HOH   J .   ? 0.2123 0.2351 0.2280 -0.0074 0.0209  0.0850  635 HOH   A O   
4931 O O   . HOH   J .   ? 0.4197 0.5426 1.0399 0.0342  0.2163  0.2011  636 HOH   A O   
4932 O O   . HOH   J .   ? 0.2991 0.4429 0.1858 -0.0074 0.0975  0.1669  637 HOH   A O   
4933 O O   . HOH   J .   ? 0.2232 0.2992 0.2072 -0.0302 0.0449  0.0687  638 HOH   A O   
4934 O O   . HOH   J .   ? 0.2603 0.4154 0.7123 -0.1128 0.0166  0.3506  639 HOH   A O   
4935 O O   . HOH   J .   ? 0.2604 0.2947 0.2363 -0.0453 0.0383  0.0114  640 HOH   A O   
4936 O O   . HOH   J .   ? 0.2530 0.3870 0.5046 0.0016  0.1458  0.1344  641 HOH   A O   
4937 O O   . HOH   J .   ? 0.7662 0.5839 0.5872 0.0171  -0.1392 -0.0183 642 HOH   A O   
4938 O O   . HOH   J .   ? 0.2994 0.3928 0.3200 -0.0466 -0.0990 0.0385  643 HOH   A O   
4939 O O   . HOH   J .   ? 0.4922 0.3831 0.4297 0.1566  -0.0382 -0.0179 644 HOH   A O   
4940 O O   . HOH   J .   ? 0.2841 0.3229 0.3659 -0.0784 -0.0616 0.0794  645 HOH   A O   
4941 O O   . HOH   J .   ? 0.6138 0.5504 0.7670 -0.1606 -0.3393 -0.0020 646 HOH   A O   
4942 O O   . HOH   J .   ? 0.6503 0.4409 0.5849 -0.1808 0.1097  -0.0654 647 HOH   A O   
4943 O O   . HOH   J .   ? 0.4712 0.3847 0.4339 0.0018  -0.0398 0.0067  648 HOH   A O   
4944 O O   . HOH   J .   ? 0.3108 0.7543 0.3770 0.2271  -0.0638 -0.0905 649 HOH   A O   
4945 O O   . HOH   J .   ? 0.5073 0.2572 0.4379 -0.0302 0.2012  0.0260  650 HOH   A O   
4946 O O   . HOH   J .   ? 0.3573 0.2341 0.3031 0.0126  -0.1050 0.0235  651 HOH   A O   
4947 O O   . HOH   J .   ? 0.2208 0.2808 0.1768 0.0268  0.0124  0.0300  652 HOH   A O   
4948 O O   . HOH   J .   ? 0.4329 0.4053 0.2214 0.1042  0.0071  0.0300  653 HOH   A O   
4949 O O   . HOH   J .   ? 0.2845 0.3571 0.1540 -0.0509 0.0182  0.0125  654 HOH   A O   
4950 O O   . HOH   J .   ? 0.5299 0.7237 0.2394 0.1163  0.1322  0.0465  655 HOH   A O   
4951 O O   . HOH   J .   ? 0.4103 0.4191 0.4078 -0.1489 0.0224  -0.0628 656 HOH   A O   
4952 O O   . HOH   J .   ? 0.4066 0.6382 0.4707 0.1631  0.0568  -0.0915 657 HOH   A O   
4953 O O   . HOH   J .   ? 0.4951 0.4919 0.4885 0.0700  0.0578  -0.0313 658 HOH   A O   
4954 O O   . HOH   J .   ? 0.3392 0.8856 0.9652 -0.0480 -0.2222 -0.3081 659 HOH   A O   
4955 O O   . HOH   J .   ? 0.2766 0.6689 0.6619 0.0035  0.0179  0.3885  660 HOH   A O   
4956 O O   . HOH   J .   ? 0.4409 0.3383 0.4172 -0.1746 -0.0154 0.0573  661 HOH   A O   
4957 O O   . HOH   J .   ? 0.2691 0.3784 0.3691 -0.0454 0.0613  0.1176  662 HOH   A O   
4958 O O   . HOH   J .   ? 0.2464 1.0343 0.5161 0.1185  -0.0748 -0.0168 663 HOH   A O   
4959 O O   . HOH   J .   ? 0.5558 0.8485 0.2163 0.3646  -0.0711 -0.0025 664 HOH   A O   
4960 O O   . HOH   J .   ? 0.2333 0.2828 0.2412 -0.0517 -0.0157 0.0461  665 HOH   A O   
4961 O O   . HOH   J .   ? 0.3123 0.5243 0.2490 -0.0764 -0.0568 0.1068  666 HOH   A O   
4962 O O   . HOH   J .   ? 0.1822 0.4627 0.3736 0.0553  -0.0110 0.2393  667 HOH   A O   
4963 O O   . HOH   J .   ? 0.2350 0.2825 0.1931 0.0222  0.0309  0.0981  668 HOH   A O   
4964 O O   . HOH   J .   ? 0.4291 0.4179 0.5386 0.0196  -0.1193 0.0674  669 HOH   A O   
4965 O O   . HOH   J .   ? 0.4212 0.4559 0.4934 0.0100  0.0575  0.2935  670 HOH   A O   
4966 O O   . HOH   J .   ? 0.2690 0.2839 0.2914 -0.0164 0.0041  0.0867  671 HOH   A O   
4967 O O   . HOH   J .   ? 0.4869 0.6575 0.5021 0.2301  -0.0646 -0.0713 672 HOH   A O   
4968 O O   . HOH   J .   ? 0.3589 0.7822 0.5031 0.1635  -0.0039 0.1474  673 HOH   A O   
4969 O O   . HOH   J .   ? 0.7895 0.2537 0.4143 -0.0871 0.0978  0.0672  674 HOH   A O   
4970 O O   . HOH   J .   ? 0.1594 0.3616 0.2396 -0.0160 0.0074  -0.0014 675 HOH   A O   
4971 O O   . HOH   J .   ? 0.8496 0.3519 0.1832 -0.0166 0.0168  0.0450  676 HOH   A O   
4972 O O   . HOH   J .   ? 0.2176 0.2530 0.2622 0.0280  -0.0010 -0.0043 677 HOH   A O   
4973 O O   . HOH   J .   ? 0.4062 0.5788 0.9096 -0.0993 0.2264  0.0061  678 HOH   A O   
4974 O O   . HOH   J .   ? 0.7402 0.4808 0.3429 -0.0217 -0.1632 -0.0417 679 HOH   A O   
4975 O O   . HOH   J .   ? 0.4885 0.4809 0.3598 -0.0706 -0.0910 0.1590  680 HOH   A O   
4976 O O   . HOH   J .   ? 0.5314 0.3228 0.3497 -0.1283 -0.0952 0.0856  681 HOH   A O   
4977 O O   . HOH   J .   ? 0.3018 0.3980 0.3378 0.0715  -0.0272 0.1634  682 HOH   A O   
4978 O O   . HOH   J .   ? 0.6917 0.3685 0.5123 -0.1278 -0.0759 0.0069  683 HOH   A O   
4979 O O   . HOH   J .   ? 0.6028 0.5169 0.3225 0.1027  0.1239  0.1031  684 HOH   A O   
4980 O O   . HOH   J .   ? 0.2336 0.3802 0.2670 -0.0546 -0.0233 0.0785  685 HOH   A O   
4981 O O   . HOH   J .   ? 0.5698 0.4197 0.4091 0.0325  -0.0098 -0.0458 686 HOH   A O   
4982 O O   . HOH   J .   ? 0.4059 0.3646 0.2885 -0.0428 -0.0332 0.0503  687 HOH   A O   
4983 O O   . HOH   J .   ? 0.3767 0.7281 0.5424 -0.2195 0.1129  -0.1692 688 HOH   A O   
4984 O O   . HOH   J .   ? 0.5050 0.5898 0.5115 -0.1909 -0.1711 0.1166  689 HOH   A O   
4985 O O   . HOH   J .   ? 0.5020 0.6754 0.6288 -0.1493 0.1174  -0.2273 690 HOH   A O   
4986 O O   . HOH   J .   ? 0.5094 0.5507 0.4981 0.0010  0.1363  -0.0705 691 HOH   A O   
4987 O O   . HOH   J .   ? 0.4932 0.4517 0.2376 -0.1091 -0.0358 -0.0126 692 HOH   A O   
4988 O O   . HOH   J .   ? 0.4868 0.3184 0.3537 0.1420  -0.0979 -0.0719 693 HOH   A O   
4989 O O   . HOH   J .   ? 0.8526 0.6945 0.4409 -0.2587 -0.0514 0.1939  694 HOH   A O   
4990 O O   . HOH   J .   ? 0.3185 1.0816 0.4125 0.2384  0.0677  0.1799  695 HOH   A O   
4991 O O   . HOH   J .   ? 0.4670 0.4266 1.2322 -0.0469 0.0678  0.2602  696 HOH   A O   
4992 O O   . HOH   J .   ? 0.4457 0.7774 0.4916 -0.2736 -0.2299 0.3330  697 HOH   A O   
4993 O O   . HOH   J .   ? 0.2922 0.3442 0.4326 -0.0861 -0.0659 -0.0233 698 HOH   A O   
4994 O O   . HOH   J .   ? 0.5344 0.5003 0.5978 -0.1140 -0.1831 0.1614  699 HOH   A O   
4995 O O   . HOH   J .   ? 0.3584 0.5621 0.4156 -0.1400 0.0490  -0.0599 700 HOH   A O   
4996 O O   . HOH   J .   ? 0.5183 0.5583 0.3294 -0.0704 -0.0416 0.2834  701 HOH   A O   
4997 O O   . HOH   J .   ? 0.4341 0.3934 0.6359 0.0322  -0.0008 -0.0399 702 HOH   A O   
4998 O O   . HOH   J .   ? 0.8122 0.5412 0.6017 0.1003  0.0318  -0.1337 703 HOH   A O   
4999 O O   . HOH   J .   ? 0.4143 0.5714 0.4047 0.0225  0.1587  0.1849  704 HOH   A O   
5000 O O   . HOH   J .   ? 0.3375 0.3863 0.4334 0.0403  -0.0671 0.0466  705 HOH   A O   
5001 O O   . HOH   J .   ? 0.2854 0.7005 0.4258 -0.1110 -0.0206 0.0811  706 HOH   A O   
5002 O O   . HOH   J .   ? 0.5564 0.5224 0.6702 -0.0297 -0.3007 -0.0282 707 HOH   A O   
5003 O O   . HOH   J .   ? 0.5044 0.4086 0.5642 -0.1293 -0.0006 0.0644  708 HOH   A O   
5004 O O   . HOH   J .   ? 0.3188 0.3063 0.5833 -0.0503 -0.0025 0.0412  709 HOH   A O   
5005 O O   . HOH   J .   ? 0.7829 0.4377 0.4044 0.1448  0.1147  0.1982  710 HOH   A O   
5006 O O   . HOH   J .   ? 0.2073 0.8679 0.6755 0.2028  -0.0593 -0.0733 711 HOH   A O   
5007 O O   . HOH   J .   ? 0.3359 0.5427 0.5565 0.1549  0.2503  0.1867  712 HOH   A O   
5008 O O   . HOH   J .   ? 0.4984 0.6412 0.4413 0.0796  0.0512  0.1369  713 HOH   A O   
5009 O O   . HOH   J .   ? 0.8765 0.5512 0.3322 -0.2173 0.0197  0.0393  714 HOH   A O   
5010 O O   . HOH   J .   ? 0.1858 0.2387 0.2062 -0.0024 0.0240  0.0153  715 HOH   A O   
5011 O O   . HOH   J .   ? 0.9854 0.8334 0.6441 -0.3803 0.1524  0.1784  716 HOH   A O   
5012 O O   . HOH   J .   ? 0.4033 0.4806 0.2764 -0.0544 -0.0812 0.0377  717 HOH   A O   
5013 O O   . HOH   J .   ? 0.5010 0.3717 0.6414 0.0217  0.0317  0.0717  718 HOH   A O   
5014 O O   . HOH   J .   ? 0.5359 0.3446 0.3440 -0.0808 0.1500  0.0729  719 HOH   A O   
5015 O O   . HOH   J .   ? 0.3168 0.2621 0.3203 0.0064  0.0041  -0.0148 720 HOH   A O   
5016 O O   . HOH   J .   ? 0.5842 0.7483 0.4099 0.0101  -0.0381 0.0167  721 HOH   A O   
5017 O O   . HOH   J .   ? 0.3518 0.4540 0.2947 -0.0357 0.0275  0.0440  722 HOH   A O   
5018 O O   . HOH   J .   ? 0.5746 0.7239 0.4818 0.0623  -0.0327 0.2069  723 HOH   A O   
5019 O O   . HOH   J .   ? 0.2542 0.3893 0.2205 -0.0253 0.0329  0.1395  724 HOH   A O   
5020 O O   . HOH   J .   ? 0.4675 0.6756 0.8307 -0.2059 -0.2875 0.2937  725 HOH   A O   
5021 O O   . HOH   J .   ? 0.3028 0.5059 0.4899 -0.0749 0.1242  0.1995  726 HOH   A O   
5022 O O   . HOH   J .   ? 0.5534 0.5265 0.6710 0.0120  0.0938  0.0038  727 HOH   A O   
5023 O O   . HOH   J .   ? 0.4510 0.5534 0.3765 -0.0457 0.0859  0.0645  728 HOH   A O   
5024 O O   . HOH   J .   ? 0.4041 0.4304 0.2719 -0.0267 0.0492  -0.0434 729 HOH   A O   
5025 O O   . HOH   J .   ? 0.4454 0.5752 0.4444 0.0062  -0.1133 0.0411  730 HOH   A O   
5026 O O   . HOH   J .   ? 0.3337 0.5608 1.0442 -0.0306 0.1159  0.0057  731 HOH   A O   
5027 O O   . HOH   J .   ? 0.3509 0.7066 0.2832 0.0065  -0.0202 0.0415  732 HOH   A O   
5028 O O   . HOH   J .   ? 0.4743 0.5289 0.5020 -0.0073 0.1233  -0.0198 733 HOH   A O   
5029 O O   . HOH   J .   ? 0.5527 0.7909 0.3374 -0.1968 0.0099  0.1324  734 HOH   A O   
5030 O O   . HOH   J .   ? 1.1865 0.4287 0.3618 -0.2151 -0.0804 -0.0245 735 HOH   A O   
5031 O O   . HOH   J .   ? 0.5390 0.4054 0.7082 -0.0558 0.1319  -0.1381 736 HOH   A O   
5032 O O   . HOH   J .   ? 0.6305 0.4541 0.6081 0.0485  0.1421  0.1526  737 HOH   A O   
5033 O O   . HOH   J .   ? 0.7282 0.4487 0.7046 0.0896  -0.3372 -0.0651 738 HOH   A O   
5034 O O   . HOH   J .   ? 0.4215 0.3708 0.5776 -0.0987 -0.0187 0.1539  739 HOH   A O   
5035 O O   . HOH   J .   ? 0.4248 0.3742 0.6989 -0.0802 0.2279  0.0231  740 HOH   A O   
5036 O O   . HOH   J .   ? 0.3095 0.7372 0.4749 -0.0553 -0.0462 0.1871  741 HOH   A O   
5037 O O   . HOH   J .   ? 0.3795 1.2610 0.3924 -0.1494 0.0115  0.1324  742 HOH   A O   
5038 O O   . HOH   J .   ? 0.4725 0.6460 0.3950 -0.1316 0.0061  0.1690  743 HOH   A O   
5039 O O   . HOH   J .   ? 0.5440 0.5100 0.2994 0.1280  0.0133  -0.1072 744 HOH   A O   
5040 O O   . HOH   J .   ? 0.4603 0.6062 0.3986 -0.1264 0.0886  0.0233  745 HOH   A O   
5041 O O   . HOH   J .   ? 0.6056 0.6359 0.8043 -0.2032 -0.0923 0.1184  746 HOH   A O   
5042 O O   . HOH   J .   ? 0.3238 0.4124 0.4398 -0.1433 0.0331  0.0820  747 HOH   A O   
5043 O O   . HOH   J .   ? 0.4224 0.4523 0.3937 -0.0292 -0.0551 0.1068  748 HOH   A O   
5044 O O   . HOH   J .   ? 0.3882 0.4213 0.5182 -0.0244 -0.1337 0.0722  749 HOH   A O   
5045 O O   . HOH   J .   ? 0.3073 0.7803 0.4204 -0.1300 -0.0998 0.1326  750 HOH   A O   
5046 O O   . HOH   J .   ? 0.4703 0.4881 0.3060 0.0930  0.0785  -0.0449 751 HOH   A O   
5047 O O   . HOH   J .   ? 0.2229 0.5433 0.2102 -0.0878 0.0351  0.0636  752 HOH   A O   
5048 O O   . HOH   J .   ? 0.4553 0.7350 0.4218 0.0314  0.0310  -0.1597 753 HOH   A O   
5049 O O   . HOH   J .   ? 0.7476 0.3212 0.8515 -0.0781 -0.1602 0.0390  754 HOH   A O   
5050 O O   . HOH   J .   ? 0.4441 0.4723 0.5516 -0.0409 0.0231  0.1173  755 HOH   A O   
5051 O O   . HOH   J .   ? 0.6136 0.5781 0.6725 0.1795  0.2554  0.0001  756 HOH   A O   
5052 O O   . HOH   J .   ? 0.3359 0.5192 0.4012 0.1312  0.1975  0.0906  757 HOH   A O   
5053 O O   . HOH   J .   ? 0.8290 0.6759 0.6786 -0.1733 -0.3504 0.2618  758 HOH   A O   
5054 O O   . HOH   J .   ? 0.4897 0.5968 0.4962 -0.2467 0.1189  0.0494  759 HOH   A O   
5055 O O   . HOH   J .   ? 0.3411 0.6379 0.4740 0.0471  0.0157  -0.0763 760 HOH   A O   
5056 O O   . HOH   J .   ? 0.3991 0.6066 0.6108 -0.0330 -0.0053 0.0161  761 HOH   A O   
5057 O O   . HOH   J .   ? 0.5059 0.4388 0.2634 -0.0679 0.0796  0.0470  762 HOH   A O   
5058 O O   . HOH   J .   ? 0.3531 0.3620 0.5773 0.0244  0.0856  0.1011  763 HOH   A O   
5059 O O   . HOH   J .   ? 0.3870 0.6482 0.2601 0.0464  0.0678  0.0954  764 HOH   A O   
5060 O O   . HOH   J .   ? 0.3834 0.7250 0.4339 -0.1098 -0.0845 0.2494  765 HOH   A O   
5061 O O   . HOH   J .   ? 0.3292 0.3671 0.3523 -0.1158 -0.0302 -0.0283 766 HOH   A O   
5062 O O   . HOH   J .   ? 0.5341 0.3745 0.4049 0.0133  0.1399  0.0340  767 HOH   A O   
5063 O O   . HOH   J .   ? 0.4805 0.5422 0.5513 -0.0789 0.1223  -0.2889 768 HOH   A O   
5064 O O   . HOH   K .   ? 0.9838 0.5008 0.6869 -0.3598 -0.1693 0.0772  501 HOH   B O   
5065 O O   . HOH   K .   ? 0.3356 0.7049 0.5148 0.0958  -0.0577 -0.1157 502 HOH   B O   
5066 O O   . HOH   K .   ? 0.4931 0.7960 0.3633 0.1650  0.0764  0.2574  503 HOH   B O   
5067 O O   . HOH   K .   ? 0.2087 0.2170 0.2077 -0.0370 0.0223  0.0102  504 HOH   B O   
5068 O O   . HOH   K .   ? 0.8503 0.5058 0.7895 0.2144  0.2221  0.0795  505 HOH   B O   
5069 O O   . HOH   K .   ? 0.2971 0.5396 0.4598 0.0114  0.1087  0.1668  506 HOH   B O   
5070 O O   . HOH   K .   ? 0.4195 0.3826 0.3183 0.0233  -0.0196 -0.0099 507 HOH   B O   
5071 O O   . HOH   K .   ? 0.2563 0.7736 0.7081 -0.0135 0.1351  -0.1488 508 HOH   B O   
5072 O O   . HOH   K .   ? 0.3809 0.7020 0.7316 0.1347  0.2161  -0.2125 509 HOH   B O   
5073 O O   . HOH   K .   ? 0.1950 0.2974 0.2277 0.0015  0.0081  0.0803  510 HOH   B O   
5074 O O   . HOH   K .   ? 0.5717 0.7772 0.2710 0.1976  -0.0660 -0.0114 511 HOH   B O   
5075 O O   . HOH   K .   ? 0.3310 0.5711 0.7158 0.1574  -0.0611 0.0718  512 HOH   B O   
5076 O O   . HOH   K .   ? 0.5910 0.2802 0.2572 -0.1659 -0.0477 0.0937  513 HOH   B O   
5077 O O   . HOH   K .   ? 0.4337 0.2844 0.1997 -0.1117 0.0071  0.1205  514 HOH   B O   
5078 O O   . HOH   K .   ? 0.1825 0.3220 0.3553 -0.0067 0.0351  0.0900  515 HOH   B O   
5079 O O   . HOH   K .   ? 0.3284 0.6088 0.3459 -0.1032 -0.0147 0.0089  516 HOH   B O   
5080 O O   . HOH   K .   ? 0.2415 0.7283 0.5124 0.0184  0.0209  0.0841  517 HOH   B O   
5081 O O   . HOH   K .   ? 0.2193 0.5000 0.3786 0.1310  0.0595  0.0746  518 HOH   B O   
5082 O O   . HOH   K .   ? 0.5041 0.5779 0.3318 -0.0502 -0.0244 0.1653  519 HOH   B O   
5083 O O   . HOH   K .   ? 0.2693 0.4082 0.2396 0.0742  -0.0439 0.0359  520 HOH   B O   
5084 O O   . HOH   K .   ? 0.6028 0.4228 0.4502 0.1344  -0.0110 0.1425  521 HOH   B O   
5085 O O   . HOH   K .   ? 0.1968 0.6104 0.2533 -0.0588 0.0553  0.0055  522 HOH   B O   
5086 O O   . HOH   K .   ? 0.5260 0.3291 0.5429 0.0671  -0.2069 0.1127  523 HOH   B O   
5087 O O   . HOH   K .   ? 0.1838 0.5422 0.1620 0.0111  0.0043  0.0714  524 HOH   B O   
5088 O O   . HOH   K .   ? 0.2201 0.4166 0.2177 -0.0108 0.0661  0.0638  525 HOH   B O   
5089 O O   . HOH   K .   ? 0.1971 0.2875 0.2406 -0.0387 0.0081  0.0753  526 HOH   B O   
5090 O O   . HOH   K .   ? 0.2095 0.8040 0.3544 -0.0567 -0.0148 0.2255  527 HOH   B O   
5091 O O   . HOH   K .   ? 0.3820 0.5598 0.3653 -0.2607 -0.1374 0.1538  528 HOH   B O   
5092 O O   . HOH   K .   ? 0.2898 0.5259 0.5310 -0.0211 0.1592  0.0352  529 HOH   B O   
5093 O O   . HOH   K .   ? 0.4346 0.4014 0.3600 0.1089  0.0409  -0.0640 530 HOH   B O   
5094 O O   . HOH   K .   ? 0.2319 0.4667 0.2716 0.0019  0.0439  0.1236  531 HOH   B O   
5095 O O   . HOH   K .   ? 0.8146 0.6214 0.6540 0.1177  0.1199  0.4149  532 HOH   B O   
5096 O O   . HOH   K .   ? 0.7038 0.3612 0.9990 0.0088  -0.2645 0.0730  533 HOH   B O   
5097 O O   . HOH   K .   ? 0.2137 0.3025 0.1995 -0.0098 0.0571  0.0915  534 HOH   B O   
5098 O O   . HOH   K .   ? 0.3821 0.4268 0.3420 -0.0564 -0.0819 0.1819  535 HOH   B O   
5099 O O   . HOH   K .   ? 0.6809 0.8103 0.2957 0.2812  0.1499  0.1371  536 HOH   B O   
5100 O O   . HOH   K .   ? 0.4603 0.4060 0.2652 0.0802  0.0081  0.0123  537 HOH   B O   
5101 O O   . HOH   K .   ? 0.2944 0.7231 0.6498 0.1189  0.0286  0.0489  538 HOH   B O   
5102 O O   . HOH   K .   ? 0.3198 0.2918 0.1639 -0.0136 -0.0072 0.0063  539 HOH   B O   
5103 O O   . HOH   K .   ? 0.3314 0.5304 0.3530 -0.1012 0.0280  0.1276  540 HOH   B O   
5104 O O   . HOH   K .   ? 0.4852 0.3663 0.4195 -0.1240 -0.0908 0.1309  541 HOH   B O   
5105 O O   . HOH   K .   ? 0.3609 0.4087 0.3433 -0.0371 -0.0028 0.0234  542 HOH   B O   
5106 O O   . HOH   K .   ? 0.5455 0.6555 0.4218 -0.1139 0.2358  0.0179  543 HOH   B O   
5107 O O   . HOH   K .   ? 0.3395 0.1818 0.3488 -0.0624 -0.1332 0.1048  544 HOH   B O   
5108 O O   . HOH   K .   ? 0.3117 0.3834 0.2230 0.1463  -0.0007 0.0182  545 HOH   B O   
5109 O O   . HOH   K .   ? 0.5609 0.4824 0.2446 0.0097  -0.0772 0.0423  546 HOH   B O   
5110 O O   . HOH   K .   ? 0.3417 0.8816 0.4054 0.3728  -0.0147 -0.0725 547 HOH   B O   
5111 O O   . HOH   K .   ? 0.4667 0.3033 0.2154 -0.0496 -0.1075 0.0142  548 HOH   B O   
5112 O O   . HOH   K .   ? 0.8748 0.6500 0.4364 0.1338  0.1981  0.0824  549 HOH   B O   
5113 O O   . HOH   K .   ? 0.9376 0.4555 0.2230 -0.0291 -0.0325 -0.1420 550 HOH   B O   
5114 O O   . HOH   K .   ? 0.5850 0.4757 0.3629 -0.1424 0.1924  0.0253  551 HOH   B O   
5115 O O   . HOH   K .   ? 0.3752 0.9237 0.3660 0.1908  0.1215  0.3015  552 HOH   B O   
5116 O O   . HOH   K .   ? 0.2427 0.3993 0.3160 0.0126  -0.0319 0.1425  553 HOH   B O   
5117 O O   . HOH   K .   ? 0.1643 0.3899 0.1796 0.0063  0.0302  0.0438  554 HOH   B O   
5118 O O   . HOH   K .   ? 0.5603 0.4066 0.2951 0.0505  -0.0471 0.1395  555 HOH   B O   
5119 O O   . HOH   K .   ? 0.2716 0.9237 0.3752 0.1004  0.2225  0.2955  556 HOH   B O   
5120 O O   . HOH   K .   ? 0.2345 0.3177 0.2840 0.0003  0.0604  0.0633  557 HOH   B O   
5121 O O   . HOH   K .   ? 0.5516 0.5351 0.2849 0.1107  0.1609  0.2500  558 HOH   B O   
5122 O O   . HOH   K .   ? 0.2766 0.6040 0.9050 -0.0471 -0.1420 0.1775  559 HOH   B O   
5123 O O   . HOH   K .   ? 0.4213 0.8113 0.4557 -0.3580 -0.1105 0.1948  560 HOH   B O   
5124 O O   . HOH   K .   ? 0.4286 0.3956 0.2978 -0.1246 0.1166  0.0637  561 HOH   B O   
5125 O O   . HOH   K .   ? 0.4183 0.5183 0.1827 0.1776  0.0267  0.0045  562 HOH   B O   
5126 O O   . HOH   K .   ? 0.5620 0.2066 0.5225 -0.0381 -0.1601 0.0137  563 HOH   B O   
5127 O O   . HOH   K .   ? 0.2748 0.5561 0.2429 -0.0435 0.0310  0.1113  564 HOH   B O   
5128 O O   . HOH   K .   ? 0.5213 0.3874 0.3323 -0.2153 -0.0990 0.0759  565 HOH   B O   
5129 O O   . HOH   K .   ? 0.4954 0.6365 0.3262 -0.3612 -0.1223 0.0909  566 HOH   B O   
5130 O O   . HOH   K .   ? 0.3058 0.8932 0.3911 -0.1465 -0.0067 0.3074  567 HOH   B O   
5131 O O   . HOH   K .   ? 0.7676 0.4069 0.7335 -0.0994 -0.2171 0.1185  568 HOH   B O   
5132 O O   . HOH   K .   ? 0.9771 0.7101 0.4837 -0.1850 -0.1266 -0.1628 569 HOH   B O   
5133 O O   . HOH   K .   ? 0.5203 0.4808 0.8980 0.0308  -0.0126 0.1523  570 HOH   B O   
5134 O O   . HOH   K .   ? 0.3135 0.7743 0.4440 -0.2543 0.0059  -0.0515 571 HOH   B O   
5135 O O   . HOH   K .   ? 0.4034 0.4512 0.2837 0.0000  -0.0388 0.0345  572 HOH   B O   
5136 O O   . HOH   K .   ? 0.4154 0.4390 0.3953 -0.2276 -0.0360 0.1727  573 HOH   B O   
5137 O O   . HOH   K .   ? 0.3794 0.4675 0.3094 -0.0463 0.0262  0.1234  574 HOH   B O   
5138 O O   . HOH   K .   ? 0.3393 0.5107 0.2567 -0.0406 -0.0205 0.1699  575 HOH   B O   
5139 O O   . HOH   K .   ? 0.2316 0.3180 0.2631 -0.0213 -0.0144 0.0117  576 HOH   B O   
5140 O O   . HOH   K .   ? 0.3512 0.5249 0.5032 0.0020  -0.0789 -0.0542 577 HOH   B O   
5141 O O   . HOH   K .   ? 0.4252 0.8199 0.5271 -0.0823 0.2782  0.0678  578 HOH   B O   
5142 O O   . HOH   K .   ? 0.3251 0.7001 0.5141 0.1435  0.1357  0.0366  579 HOH   B O   
5143 O O   . HOH   K .   ? 0.3454 0.2425 0.2525 -0.0581 -0.0369 0.0541  580 HOH   B O   
5144 O O   . HOH   K .   ? 0.4976 0.3967 0.3091 0.1814  0.0018  0.0446  581 HOH   B O   
5145 O O   . HOH   K .   ? 0.2363 0.4711 0.2464 0.0977  -0.0669 0.0408  582 HOH   B O   
5146 O O   . HOH   K .   ? 0.2868 0.4296 0.2934 -0.0478 0.0215  0.1325  583 HOH   B O   
5147 O O   . HOH   K .   ? 0.4825 0.4635 0.6728 -0.0239 -0.0758 0.0655  584 HOH   B O   
5148 O O   . HOH   K .   ? 0.5186 0.4593 0.4152 0.0072  -0.0760 0.2176  585 HOH   B O   
5149 O O   . HOH   K .   ? 0.3565 0.3167 0.2534 -0.0047 0.0638  0.0516  586 HOH   B O   
5150 O O   . HOH   K .   ? 0.3268 0.9187 0.4399 0.0697  -0.0031 0.2768  587 HOH   B O   
5151 O O   . HOH   K .   ? 0.2525 0.4995 0.2812 -0.0405 -0.0855 0.1455  588 HOH   B O   
5152 O O   . HOH   K .   ? 0.6121 0.3488 0.4379 0.1181  0.1355  0.0608  589 HOH   B O   
5153 O O   . HOH   K .   ? 0.3011 0.2915 0.2651 -0.0423 0.0119  0.0774  590 HOH   B O   
5154 O O   . HOH   K .   ? 0.4586 0.8016 0.2934 0.0073  0.0238  0.0655  591 HOH   B O   
5155 O O   . HOH   K .   ? 0.2830 0.3724 0.2775 -0.1447 0.0617  0.0045  592 HOH   B O   
5156 O O   . HOH   K .   ? 0.2234 0.3774 0.2336 0.0287  0.0015  0.0991  593 HOH   B O   
5157 O O   . HOH   K .   ? 0.5755 0.4763 0.3161 0.1385  -0.1474 0.0203  594 HOH   B O   
5158 O O   . HOH   K .   ? 0.2050 0.2593 0.2149 -0.0224 0.0311  0.0232  595 HOH   B O   
5159 O O   . HOH   K .   ? 0.2473 0.8773 0.3924 -0.0143 0.0781  0.0526  596 HOH   B O   
5160 O O   . HOH   K .   ? 1.0614 0.1946 0.3483 -0.1068 -0.2453 0.0328  597 HOH   B O   
5161 O O   . HOH   K .   ? 0.2284 0.2995 0.2440 -0.0121 0.0446  0.0065  598 HOH   B O   
5162 O O   . HOH   K .   ? 0.2115 0.3114 0.2206 0.0234  0.0090  0.0017  599 HOH   B O   
5163 O O   . HOH   K .   ? 0.1291 0.6257 0.2882 0.0062  0.0463  0.1552  600 HOH   B O   
5164 O O   . HOH   K .   ? 0.3510 0.5449 0.4311 -0.0382 0.1083  0.2818  601 HOH   B O   
5165 O O   . HOH   K .   ? 0.3592 0.4245 0.2453 -0.1963 -0.0403 0.0863  602 HOH   B O   
5166 O O   . HOH   K .   ? 0.2446 0.2525 0.2268 -0.0613 -0.0197 0.0624  603 HOH   B O   
5167 O O   . HOH   K .   ? 0.2675 0.4644 0.2553 0.1490  -0.0439 0.0386  604 HOH   B O   
5168 O O   . HOH   K .   ? 0.5074 0.4588 0.4492 -0.0365 0.0075  -0.0579 605 HOH   B O   
5169 O O   . HOH   K .   ? 0.2451 0.6019 0.3953 0.1136  0.0190  0.2448  606 HOH   B O   
5170 O O   . HOH   K .   ? 0.5797 0.8987 0.5493 -0.1880 0.0057  0.2641  607 HOH   B O   
5171 O O   . HOH   K .   ? 0.3324 0.6554 0.4538 -0.1699 0.0100  0.1987  608 HOH   B O   
5172 O O   . HOH   K .   ? 0.9611 0.8638 0.4422 -0.1686 -0.1997 0.4111  609 HOH   B O   
5173 O O   . HOH   K .   ? 0.5596 0.3478 0.4486 -0.0771 -0.1240 0.1468  610 HOH   B O   
5174 O O   . HOH   K .   ? 0.5293 1.2356 0.4248 -0.0707 0.1297  -0.1313 611 HOH   B O   
5175 O O   . HOH   K .   ? 0.5196 0.5268 0.2312 0.0330  -0.0066 -0.0426 612 HOH   B O   
5176 O O   . HOH   K .   ? 1.2628 0.3967 0.3080 0.3871  0.1134  -0.0134 613 HOH   B O   
5177 O O   . HOH   K .   ? 0.8138 0.5738 0.5612 -0.2989 -0.0533 -0.0307 614 HOH   B O   
5178 O O   . HOH   K .   ? 0.5129 0.3158 0.3269 0.0085  0.1050  0.0397  615 HOH   B O   
5179 O O   . HOH   K .   ? 0.6233 0.2378 0.2182 -0.0347 -0.0966 -0.0125 616 HOH   B O   
5180 O O   . HOH   K .   ? 0.7377 0.3715 0.2616 -0.0589 -0.0482 0.0202  617 HOH   B O   
5181 O O   . HOH   K .   ? 0.2816 0.6081 0.2006 -0.1018 0.0602  0.0416  618 HOH   B O   
5182 O O   . HOH   K .   ? 0.6254 0.3500 0.3565 0.1372  -0.2222 -0.1302 619 HOH   B O   
5183 O O   . HOH   K .   ? 0.3394 0.6178 0.4317 -0.1056 0.0477  0.1136  620 HOH   B O   
5184 O O   . HOH   K .   ? 0.3500 0.6871 0.3881 -0.1118 0.0962  -0.0340 621 HOH   B O   
5185 O O   . HOH   K .   ? 0.6853 0.4377 0.3433 -0.0476 -0.1252 -0.0429 622 HOH   B O   
5186 O O   . HOH   K .   ? 0.3383 0.4943 0.4957 -0.1140 0.0870  0.0947  623 HOH   B O   
5187 O O   . HOH   K .   ? 0.3180 0.3289 0.5489 0.0247  0.0195  0.1598  624 HOH   B O   
5188 O O   . HOH   K .   ? 0.4087 0.7949 0.2530 -0.1032 0.1988  0.1473  625 HOH   B O   
5189 O O   . HOH   K .   ? 0.1755 0.6308 0.3108 -0.0429 0.0163  0.1656  626 HOH   B O   
5190 O O   . HOH   K .   ? 0.8568 0.2704 0.4374 -0.0318 -0.2106 -0.0131 627 HOH   B O   
5191 O O   . HOH   K .   ? 0.3667 0.4207 0.3060 0.1207  -0.0315 0.0275  628 HOH   B O   
5192 O O   . HOH   K .   ? 0.2135 0.6062 0.4381 0.0983  0.0115  0.0551  629 HOH   B O   
5193 O O   . HOH   K .   ? 0.3999 0.1998 0.1654 -0.0833 0.0354  0.0172  630 HOH   B O   
5194 O O   . HOH   K .   ? 0.2427 0.4854 0.3539 -0.0613 0.0369  0.2027  631 HOH   B O   
5195 O O   . HOH   K .   ? 0.4601 0.7422 0.3369 -0.0108 0.0029  0.1207  632 HOH   B O   
5196 O O   . HOH   K .   ? 0.6174 0.9074 0.7444 -0.2874 0.1898  -0.3013 633 HOH   B O   
5197 O O   . HOH   K .   ? 0.4786 0.3945 0.2621 0.0507  -0.0223 0.0228  634 HOH   B O   
5198 O O   . HOH   K .   ? 0.5598 0.2367 0.6269 -0.0026 -0.0320 -0.0326 635 HOH   B O   
5199 O O   . HOH   K .   ? 0.2632 0.7927 0.3526 0.2477  0.1107  0.0834  636 HOH   B O   
5200 O O   . HOH   K .   ? 0.6095 0.3502 0.4013 0.1979  -0.0388 -0.0744 637 HOH   B O   
5201 O O   . HOH   K .   ? 0.8260 0.6039 0.2489 0.2248  0.0102  0.0192  638 HOH   B O   
5202 O O   . HOH   K .   ? 0.2092 0.3273 0.1844 0.0248  0.0042  0.0279  639 HOH   B O   
5203 O O   . HOH   K .   ? 0.4616 0.8709 0.5955 -0.1917 0.0353  0.1386  640 HOH   B O   
5204 O O   . HOH   K .   ? 0.7041 0.4501 0.2823 -0.1611 -0.1169 0.0378  641 HOH   B O   
5205 O O   . HOH   K .   ? 0.4396 0.5739 0.5735 -0.2899 -0.0563 0.1234  642 HOH   B O   
5206 O O   . HOH   K .   ? 0.7011 0.3174 0.8234 -0.1209 0.0641  -0.1013 643 HOH   B O   
5207 O O   . HOH   K .   ? 0.2574 0.7422 0.3842 -0.0149 0.1643  0.1885  644 HOH   B O   
5208 O O   . HOH   K .   ? 0.4622 0.4516 0.4627 -0.0202 -0.0308 0.0509  645 HOH   B O   
5209 O O   . HOH   K .   ? 0.2521 0.4302 0.2334 0.0090  -0.0124 0.0037  646 HOH   B O   
5210 O O   . HOH   K .   ? 0.9037 0.2104 0.3328 -0.0106 -0.1431 0.0816  647 HOH   B O   
5211 O O   . HOH   K .   ? 0.3720 0.5380 0.5184 -0.1336 0.0179  0.0728  648 HOH   B O   
5212 O O   . HOH   K .   ? 0.4200 0.7787 0.2858 0.0212  0.1208  0.1486  649 HOH   B O   
5213 O O   . HOH   K .   ? 0.1832 0.3142 0.2223 -0.0366 -0.0083 0.0805  650 HOH   B O   
5214 O O   A HOH   K .   ? 0.2240 0.7979 0.1456 0.0638  -0.0317 0.1183  651 HOH   B O   
5215 O O   B HOH   K .   ? 0.1277 0.5311 0.2713 0.0011  0.0629  -0.0579 651 HOH   B O   
5216 O O   . HOH   K .   ? 0.3755 0.6305 0.6167 -0.1077 -0.0798 0.2565  652 HOH   B O   
5217 O O   . HOH   K .   ? 0.7107 0.4202 0.2551 0.2187  -0.0518 0.0064  653 HOH   B O   
5218 O O   . HOH   K .   ? 0.3310 0.7581 0.6984 0.0192  -0.1236 0.0746  654 HOH   B O   
5219 O O   . HOH   K .   ? 0.4421 0.4529 0.9492 -0.0883 -0.0346 0.0708  655 HOH   B O   
5220 O O   . HOH   K .   ? 0.5767 0.3621 0.3236 0.0985  -0.0338 0.0028  656 HOH   B O   
5221 O O   . HOH   K .   ? 0.4895 0.2578 0.9475 -0.1369 0.0150  -0.1495 657 HOH   B O   
5222 O O   . HOH   K .   ? 0.4692 0.5941 0.5191 -0.1573 -0.0909 0.2627  658 HOH   B O   
5223 O O   . HOH   K .   ? 0.7233 0.2435 0.4520 -0.0974 -0.0855 0.0037  659 HOH   B O   
5224 O O   . HOH   K .   ? 0.2646 0.5966 0.2134 -0.0284 0.0382  -0.0092 660 HOH   B O   
5225 O O   . HOH   K .   ? 0.4058 1.1541 0.3570 0.1168  0.1630  0.3300  661 HOH   B O   
5226 O O   . HOH   K .   ? 0.2748 0.4057 0.4050 -0.0787 -0.0614 0.0840  662 HOH   B O   
5227 O O   . HOH   K .   ? 0.4169 0.6750 0.2808 0.0866  -0.0422 -0.0330 663 HOH   B O   
5228 O O   . HOH   K .   ? 0.6641 0.5078 0.6060 0.2604  0.2808  0.1515  664 HOH   B O   
5229 O O   . HOH   K .   ? 0.3047 0.7696 0.7036 -0.0824 -0.0100 0.5222  665 HOH   B O   
5230 O O   . HOH   K .   ? 0.3721 0.5778 0.2809 -0.0298 0.0561  0.0547  666 HOH   B O   
5231 O O   . HOH   K .   ? 0.4088 0.5151 0.4915 -0.0700 -0.0788 0.0836  667 HOH   B O   
5232 O O   . HOH   K .   ? 0.4240 0.3889 0.5723 -0.2575 -0.1490 0.1144  668 HOH   B O   
5233 O O   A HOH   K .   ? 0.2457 0.2425 0.4327 0.0505  0.0160  -0.0318 669 HOH   B O   
5234 O O   B HOH   K .   ? 0.3465 0.6173 0.2719 0.0694  -0.0712 -0.2184 669 HOH   B O   
5235 O O   . HOH   K .   ? 0.5234 0.5052 0.3358 0.1117  -0.0383 0.0770  670 HOH   B O   
5236 O O   . HOH   K .   ? 0.3667 1.1051 0.4569 0.1856  0.0607  0.3223  671 HOH   B O   
5237 O O   . HOH   K .   ? 0.4155 0.4854 0.9595 0.0416  -0.0876 -0.0287 672 HOH   B O   
5238 O O   . HOH   K .   ? 0.3965 0.4025 0.5446 -0.0252 -0.0832 -0.0417 673 HOH   B O   
5239 O O   . HOH   K .   ? 0.5046 0.7214 0.6571 -0.0066 -0.0849 0.1535  674 HOH   B O   
5240 O O   . HOH   K .   ? 0.2231 0.2892 0.1645 -0.0110 0.0722  0.0851  675 HOH   B O   
5241 O O   . HOH   K .   ? 0.8680 0.6773 1.6935 -0.1080 -0.1141 0.1255  676 HOH   B O   
5242 O O   . HOH   K .   ? 0.9144 0.3182 0.4485 0.0630  0.0364  0.0670  677 HOH   B O   
5243 O O   . HOH   K .   ? 0.3690 0.4694 0.7648 -0.0938 -0.1063 0.0628  678 HOH   B O   
5244 O O   . HOH   K .   ? 0.4331 0.4891 0.6749 0.0232  0.1134  0.1182  679 HOH   B O   
5245 O O   . HOH   K .   ? 0.3254 0.8026 0.6532 -0.0639 -0.1599 -0.0629 680 HOH   B O   
5246 O O   . HOH   K .   ? 0.8794 0.3484 0.9604 0.1129  0.3212  -0.0286 681 HOH   B O   
5247 O O   . HOH   K .   ? 0.5090 0.4963 0.3302 -0.1387 0.1301  0.0551  682 HOH   B O   
5248 O O   . HOH   K .   ? 0.3631 0.4381 0.3714 -0.0541 -0.0229 0.1081  683 HOH   B O   
5249 O O   . HOH   K .   ? 0.4551 0.3885 0.4582 -0.0603 0.0834  0.1237  684 HOH   B O   
5250 O O   . HOH   K .   ? 0.2862 0.3249 0.2787 -0.0381 -0.0743 0.0811  685 HOH   B O   
5251 O O   . HOH   K .   ? 0.7482 0.7394 0.3950 0.2222  -0.1572 -0.1848 686 HOH   B O   
5252 O O   . HOH   K .   ? 0.9582 0.5700 0.4157 -0.0145 0.1422  0.0787  687 HOH   B O   
5253 O O   . HOH   K .   ? 0.3627 0.4067 0.3213 -0.0138 -0.0211 0.0607  688 HOH   B O   
5254 O O   . HOH   K .   ? 0.4028 0.5567 0.7006 0.0722  -0.1136 -0.2277 689 HOH   B O   
5255 O O   . HOH   K .   ? 0.7127 0.5087 0.4986 0.0177  -0.0779 -0.0005 690 HOH   B O   
5256 O O   . HOH   K .   ? 0.6706 0.8603 0.6777 0.4115  -0.3212 -0.4679 691 HOH   B O   
5257 O O   . HOH   K .   ? 0.5393 0.6207 0.3853 -0.0490 -0.0478 0.0186  692 HOH   B O   
5258 O O   . HOH   K .   ? 0.4023 0.8139 0.5339 0.1155  0.0292  0.0085  693 HOH   B O   
5259 O O   . HOH   K .   ? 0.3532 0.5416 0.3490 -0.0969 -0.0196 0.1672  694 HOH   B O   
5260 O O   . HOH   K .   ? 0.3477 0.6536 0.4070 0.1090  -0.0568 0.0121  695 HOH   B O   
5261 O O   . HOH   K .   ? 0.3522 0.5176 0.5222 -0.1167 0.0187  0.1566  696 HOH   B O   
5262 O O   . HOH   K .   ? 0.2382 0.7081 0.4709 0.2195  -0.0256 -0.1130 697 HOH   B O   
5263 O O   . HOH   K .   ? 0.6838 0.3878 0.3295 0.1574  0.0312  0.0045  698 HOH   B O   
5264 O O   . HOH   K .   ? 0.3310 0.7828 0.5905 -0.0524 0.0718  -0.2660 699 HOH   B O   
5265 O O   . HOH   K .   ? 0.6864 0.3314 0.3249 0.0589  -0.0820 0.0095  700 HOH   B O   
5266 O O   . HOH   K .   ? 0.2987 0.4681 0.5713 0.0353  -0.0911 0.0946  701 HOH   B O   
5267 O O   . HOH   K .   ? 0.4036 0.5202 0.4777 -0.1167 -0.0180 0.0702  702 HOH   B O   
5268 O O   . HOH   K .   ? 0.7283 0.4677 0.5326 -0.1806 -0.1922 0.1007  703 HOH   B O   
5269 O O   . HOH   K .   ? 0.7709 0.5857 0.2919 0.1066  -0.1182 -0.0137 704 HOH   B O   
5270 O O   . HOH   K .   ? 0.4927 0.2832 0.2770 -0.0045 -0.0502 0.0280  705 HOH   B O   
5271 O O   . HOH   K .   ? 0.5690 0.5986 0.3670 0.0126  -0.1399 0.0446  706 HOH   B O   
# 
