data_8S85
# 
_entry.id   8S85 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8S85         pdb_00008s85 10.2210/pdb8s85/pdb 
WWPDB D_1292127965 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        8S85 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              caroline.joannesse@glpg.com 
_pdbx_contact_author.name_first         Caroline 
_pdbx_contact_author.name_last          Joannesse 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9548-5439 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Flower, T.F.'    1 0000-0002-7890-6473 
'Lopez-Ramos, M.' 2 0000-0002-8598-7347 
'Geney, R.'       3 0000-0003-2666-8589 
'Jestel, A.'      4 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            114 
_citation.language                  ? 
_citation.page_first                117932 
_citation.page_last                 117932 
_citation.title                     'Design of a potent and selective dual JAK1/TYK2 inhibitor.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2024.117932 
_citation.pdbx_database_id_PubMed   39447537 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mammoliti, O.'    1  ? 
primary 'Menet, C.'        2  ? 
primary 'Cottereaux, C.'   3  ? 
primary 'Blanc, J.'        4  ? 
primary 'De Blieck, A.'    5  ? 
primary 'Coti, G.'         6  ? 
primary 'Geney, R.'        7  ? 
primary 'Oste, L.'         8  ? 
primary 'Ostyn, K.'        9  ? 
primary 'Palisse, A.'      10 ? 
primary 'Quinton, E.'      11 ? 
primary 'Schmitt, B.'      12 ? 
primary 'Borgonovi, M.'    13 ? 
primary 'Parent, I.'       14 ? 
primary 'Jagerschmidt, C.' 15 ? 
primary 'De Vos, S.'       16 ? 
primary 'Vayssiere, B.'    17 ? 
primary 'Lopez-Ramos, M.'  18 ? 
primary 'Shoji, K.'        19 ? 
primary 'Brys, R.'         20 ? 
primary 'Amantini, D.'     21 ? 
primary 'Galien, R.'       22 ? 
primary 'Joannesse, C.'    23 ? 
# 
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 'Tyrosine-protein kinase JAK1'                                       34746.594 2   2.7.10.2 ? ? ? 
2 non-polymer syn '~{N}-(2-ethylphenyl)-~{N},1-dimethyl-imidazo[4,5-c]pyridin-6-amine' 266.341   2   ?        ? ? ? 
3 non-polymer syn 'SODIUM ION'                                                         22.990    3   ?        ? ? ? 
4 water       nat water                                                                18.015    438 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Janus kinase 1,JAK-1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL
YHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE
SEHQVKIGDFGLTKAIETDKE(PTR)(PTR)TVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSP
MALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL
YHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE
SEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMI
GPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK
;
_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 '~{N}-(2-ethylphenyl)-~{N},1-dimethyl-imidazo[4,5-c]pyridin-6-amine' A1H5R 
3 'SODIUM ION'                                                         NA    
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   ASP n 
1 3   ILE n 
1 4   VAL n 
1 5   SER n 
1 6   GLU n 
1 7   LYS n 
1 8   LYS n 
1 9   PRO n 
1 10  ALA n 
1 11  THR n 
1 12  GLU n 
1 13  VAL n 
1 14  ASP n 
1 15  PRO n 
1 16  THR n 
1 17  HIS n 
1 18  PHE n 
1 19  GLU n 
1 20  LYS n 
1 21  ARG n 
1 22  PHE n 
1 23  LEU n 
1 24  LYS n 
1 25  ARG n 
1 26  ILE n 
1 27  ARG n 
1 28  ASP n 
1 29  LEU n 
1 30  GLY n 
1 31  GLU n 
1 32  GLY n 
1 33  HIS n 
1 34  PHE n 
1 35  GLY n 
1 36  LYS n 
1 37  VAL n 
1 38  GLU n 
1 39  LEU n 
1 40  CYS n 
1 41  ARG n 
1 42  TYR n 
1 43  ASP n 
1 44  PRO n 
1 45  GLU n 
1 46  GLY n 
1 47  ASP n 
1 48  ASN n 
1 49  THR n 
1 50  GLY n 
1 51  GLU n 
1 52  GLN n 
1 53  VAL n 
1 54  ALA n 
1 55  VAL n 
1 56  LYS n 
1 57  SER n 
1 58  LEU n 
1 59  LYS n 
1 60  PRO n 
1 61  GLU n 
1 62  SER n 
1 63  GLY n 
1 64  GLY n 
1 65  ASN n 
1 66  HIS n 
1 67  ILE n 
1 68  ALA n 
1 69  ASP n 
1 70  LEU n 
1 71  LYS n 
1 72  LYS n 
1 73  GLU n 
1 74  ILE n 
1 75  GLU n 
1 76  ILE n 
1 77  LEU n 
1 78  ARG n 
1 79  ASN n 
1 80  LEU n 
1 81  TYR n 
1 82  HIS n 
1 83  GLU n 
1 84  ASN n 
1 85  ILE n 
1 86  VAL n 
1 87  LYS n 
1 88  TYR n 
1 89  LYS n 
1 90  GLY n 
1 91  ILE n 
1 92  CYS n 
1 93  THR n 
1 94  GLU n 
1 95  ASP n 
1 96  GLY n 
1 97  GLY n 
1 98  ASN n 
1 99  GLY n 
1 100 ILE n 
1 101 LYS n 
1 102 LEU n 
1 103 ILE n 
1 104 MET n 
1 105 GLU n 
1 106 PHE n 
1 107 LEU n 
1 108 PRO n 
1 109 SER n 
1 110 GLY n 
1 111 SER n 
1 112 LEU n 
1 113 LYS n 
1 114 GLU n 
1 115 TYR n 
1 116 LEU n 
1 117 PRO n 
1 118 LYS n 
1 119 ASN n 
1 120 LYS n 
1 121 ASN n 
1 122 LYS n 
1 123 ILE n 
1 124 ASN n 
1 125 LEU n 
1 126 LYS n 
1 127 GLN n 
1 128 GLN n 
1 129 LEU n 
1 130 LYS n 
1 131 TYR n 
1 132 ALA n 
1 133 VAL n 
1 134 GLN n 
1 135 ILE n 
1 136 CYS n 
1 137 LYS n 
1 138 GLY n 
1 139 MET n 
1 140 ASP n 
1 141 TYR n 
1 142 LEU n 
1 143 GLY n 
1 144 SER n 
1 145 ARG n 
1 146 GLN n 
1 147 TYR n 
1 148 VAL n 
1 149 HIS n 
1 150 ARG n 
1 151 ASP n 
1 152 LEU n 
1 153 ALA n 
1 154 ALA n 
1 155 ARG n 
1 156 ASN n 
1 157 VAL n 
1 158 LEU n 
1 159 VAL n 
1 160 GLU n 
1 161 SER n 
1 162 GLU n 
1 163 HIS n 
1 164 GLN n 
1 165 VAL n 
1 166 LYS n 
1 167 ILE n 
1 168 GLY n 
1 169 ASP n 
1 170 PHE n 
1 171 GLY n 
1 172 LEU n 
1 173 THR n 
1 174 LYS n 
1 175 ALA n 
1 176 ILE n 
1 177 GLU n 
1 178 THR n 
1 179 ASP n 
1 180 LYS n 
1 181 GLU n 
1 182 PTR n 
1 183 PTR n 
1 184 THR n 
1 185 VAL n 
1 186 LYS n 
1 187 ASP n 
1 188 ASP n 
1 189 ARG n 
1 190 ASP n 
1 191 SER n 
1 192 PRO n 
1 193 VAL n 
1 194 PHE n 
1 195 TRP n 
1 196 TYR n 
1 197 ALA n 
1 198 PRO n 
1 199 GLU n 
1 200 CYS n 
1 201 LEU n 
1 202 MET n 
1 203 GLN n 
1 204 SER n 
1 205 LYS n 
1 206 PHE n 
1 207 TYR n 
1 208 ILE n 
1 209 ALA n 
1 210 SER n 
1 211 ASP n 
1 212 VAL n 
1 213 TRP n 
1 214 SER n 
1 215 PHE n 
1 216 GLY n 
1 217 VAL n 
1 218 THR n 
1 219 LEU n 
1 220 HIS n 
1 221 GLU n 
1 222 LEU n 
1 223 LEU n 
1 224 THR n 
1 225 TYR n 
1 226 CYS n 
1 227 ASP n 
1 228 SER n 
1 229 ASP n 
1 230 SER n 
1 231 SER n 
1 232 PRO n 
1 233 MET n 
1 234 ALA n 
1 235 LEU n 
1 236 PHE n 
1 237 LEU n 
1 238 LYS n 
1 239 MET n 
1 240 ILE n 
1 241 GLY n 
1 242 PRO n 
1 243 THR n 
1 244 HIS n 
1 245 GLY n 
1 246 GLN n 
1 247 MET n 
1 248 THR n 
1 249 VAL n 
1 250 THR n 
1 251 ARG n 
1 252 LEU n 
1 253 VAL n 
1 254 ASN n 
1 255 THR n 
1 256 LEU n 
1 257 LYS n 
1 258 GLU n 
1 259 GLY n 
1 260 LYS n 
1 261 ARG n 
1 262 LEU n 
1 263 PRO n 
1 264 CYS n 
1 265 PRO n 
1 266 PRO n 
1 267 ASN n 
1 268 CYS n 
1 269 PRO n 
1 270 ASP n 
1 271 GLU n 
1 272 VAL n 
1 273 TYR n 
1 274 GLN n 
1 275 LEU n 
1 276 MET n 
1 277 ARG n 
1 278 LYS n 
1 279 CYS n 
1 280 TRP n 
1 281 GLU n 
1 282 PHE n 
1 283 GLN n 
1 284 PRO n 
1 285 SER n 
1 286 ASN n 
1 287 ARG n 
1 288 THR n 
1 289 SER n 
1 290 PHE n 
1 291 GLN n 
1 292 ASN n 
1 293 LEU n 
1 294 ILE n 
1 295 GLU n 
1 296 GLY n 
1 297 PHE n 
1 298 GLU n 
1 299 ALA n 
1 300 LEU n 
1 301 LEU n 
1 302 LYS 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                   302 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'JAK1, JAK1A, JAK1B' 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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 
A1H5R non-polymer         . '~{N}-(2-ethylphenyl)-~{N},1-dimethyl-imidazo[4,5-c]pyridin-6-amine' ?                 'C16 H18 N4' 
266.341 
ALA   'L-peptide linking' y ALANINE                                                              ?                 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                             ?                 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                           ?                 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                      ?                 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                             ?                 'C3 H7 N O2 S' 
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                            ?                 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                      ?                 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                              ?                 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                            ?                 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                ?                 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                           ?                 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                              ?                 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                               ?                 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                           ?                 'C5 H11 N O2 S' 
149.211 
NA    non-polymer         . 'SODIUM ION'                                                         ?                 'Na 1' 22.990  
PHE   'L-peptide linking' y PHENYLALANINE                                                        ?                 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                              ?                 'C5 H9 N O2' 
115.130 
PTR   'L-peptide linking' n O-PHOSPHOTYROSINE                                                    PHOSPHONOTYROSINE 'C9 H12 N O6 P' 
261.168 
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   853  853  GLY GLY A . n 
A 1 2   ASP 2   854  854  ASP ASP A . n 
A 1 3   ILE 3   855  855  ILE ILE A . n 
A 1 4   VAL 4   856  856  VAL VAL A . n 
A 1 5   SER 5   857  857  SER SER A . n 
A 1 6   GLU 6   858  858  GLU GLU A . n 
A 1 7   LYS 7   859  859  LYS LYS A . n 
A 1 8   LYS 8   860  860  LYS LYS A . n 
A 1 9   PRO 9   861  861  PRO PRO A . n 
A 1 10  ALA 10  862  862  ALA ALA A . n 
A 1 11  THR 11  863  863  THR THR A . n 
A 1 12  GLU 12  864  864  GLU GLU A . n 
A 1 13  VAL 13  865  865  VAL VAL A . n 
A 1 14  ASP 14  866  866  ASP ASP A . n 
A 1 15  PRO 15  867  867  PRO PRO A . n 
A 1 16  THR 16  868  868  THR THR A . n 
A 1 17  HIS 17  869  869  HIS HIS A . n 
A 1 18  PHE 18  870  870  PHE PHE A . n 
A 1 19  GLU 19  871  871  GLU GLU A . n 
A 1 20  LYS 20  872  872  LYS LYS A . n 
A 1 21  ARG 21  873  873  ARG ARG A . n 
A 1 22  PHE 22  874  874  PHE PHE A . n 
A 1 23  LEU 23  875  875  LEU LEU A . n 
A 1 24  LYS 24  876  876  LYS LYS A . n 
A 1 25  ARG 25  877  877  ARG ARG A . n 
A 1 26  ILE 26  878  878  ILE ILE A . n 
A 1 27  ARG 27  879  879  ARG ARG A . n 
A 1 28  ASP 28  880  880  ASP ASP A . n 
A 1 29  LEU 29  881  881  LEU LEU A . n 
A 1 30  GLY 30  882  882  GLY GLY A . n 
A 1 31  GLU 31  883  883  GLU GLU A . n 
A 1 32  GLY 32  884  884  GLY GLY A . n 
A 1 33  HIS 33  885  885  HIS HIS A . n 
A 1 34  PHE 34  886  886  PHE PHE A . n 
A 1 35  GLY 35  887  887  GLY GLY A . n 
A 1 36  LYS 36  888  888  LYS LYS A . n 
A 1 37  VAL 37  889  889  VAL VAL A . n 
A 1 38  GLU 38  890  890  GLU GLU A . n 
A 1 39  LEU 39  891  891  LEU LEU A . n 
A 1 40  CYS 40  892  892  CYS CYS A . n 
A 1 41  ARG 41  893  893  ARG ARG A . n 
A 1 42  TYR 42  894  894  TYR TYR A . n 
A 1 43  ASP 43  895  895  ASP ASP A . n 
A 1 44  PRO 44  896  896  PRO PRO A . n 
A 1 45  GLU 45  897  897  GLU GLU A . n 
A 1 46  GLY 46  898  898  GLY GLY A . n 
A 1 47  ASP 47  899  899  ASP ASP A . n 
A 1 48  ASN 48  900  900  ASN ASN A . n 
A 1 49  THR 49  901  901  THR THR A . n 
A 1 50  GLY 50  902  902  GLY GLY A . n 
A 1 51  GLU 51  903  903  GLU GLU A . n 
A 1 52  GLN 52  904  904  GLN GLN A . n 
A 1 53  VAL 53  905  905  VAL VAL A . n 
A 1 54  ALA 54  906  906  ALA ALA A . n 
A 1 55  VAL 55  907  907  VAL VAL A . n 
A 1 56  LYS 56  908  908  LYS LYS A . n 
A 1 57  SER 57  909  909  SER SER A . n 
A 1 58  LEU 58  910  910  LEU LEU A . n 
A 1 59  LYS 59  911  911  LYS LYS A . n 
A 1 60  PRO 60  912  ?    ?   ?   A . n 
A 1 61  GLU 61  913  ?    ?   ?   A . n 
A 1 62  SER 62  914  ?    ?   ?   A . n 
A 1 63  GLY 63  915  ?    ?   ?   A . n 
A 1 64  GLY 64  916  ?    ?   ?   A . n 
A 1 65  ASN 65  917  917  ASN ASN A . n 
A 1 66  HIS 66  918  918  HIS HIS A . n 
A 1 67  ILE 67  919  919  ILE ILE A . n 
A 1 68  ALA 68  920  920  ALA ALA A . n 
A 1 69  ASP 69  921  921  ASP ASP A . n 
A 1 70  LEU 70  922  922  LEU LEU A . n 
A 1 71  LYS 71  923  923  LYS LYS A . n 
A 1 72  LYS 72  924  924  LYS LYS A . n 
A 1 73  GLU 73  925  925  GLU GLU A . n 
A 1 74  ILE 74  926  926  ILE ILE A . n 
A 1 75  GLU 75  927  927  GLU GLU A . n 
A 1 76  ILE 76  928  928  ILE ILE A . n 
A 1 77  LEU 77  929  929  LEU LEU A . n 
A 1 78  ARG 78  930  930  ARG ARG A . n 
A 1 79  ASN 79  931  931  ASN ASN A . n 
A 1 80  LEU 80  932  932  LEU LEU A . n 
A 1 81  TYR 81  933  933  TYR TYR A . n 
A 1 82  HIS 82  934  934  HIS HIS A . n 
A 1 83  GLU 83  935  935  GLU GLU A . n 
A 1 84  ASN 84  936  936  ASN ASN A . n 
A 1 85  ILE 85  937  937  ILE ILE A . n 
A 1 86  VAL 86  938  938  VAL VAL A . n 
A 1 87  LYS 87  939  939  LYS LYS A . n 
A 1 88  TYR 88  940  940  TYR TYR A . n 
A 1 89  LYS 89  941  941  LYS LYS A . n 
A 1 90  GLY 90  942  942  GLY GLY A . n 
A 1 91  ILE 91  943  943  ILE ILE A . n 
A 1 92  CYS 92  944  944  CYS CYS A . n 
A 1 93  THR 93  945  945  THR THR A . n 
A 1 94  GLU 94  946  ?    ?   ?   A . n 
A 1 95  ASP 95  947  ?    ?   ?   A . n 
A 1 96  GLY 96  948  ?    ?   ?   A . n 
A 1 97  GLY 97  949  ?    ?   ?   A . n 
A 1 98  ASN 98  950  950  ASN ASN A . n 
A 1 99  GLY 99  951  951  GLY GLY A . n 
A 1 100 ILE 100 952  952  ILE ILE A . n 
A 1 101 LYS 101 953  953  LYS LYS A . n 
A 1 102 LEU 102 954  954  LEU LEU A . n 
A 1 103 ILE 103 955  955  ILE ILE A . n 
A 1 104 MET 104 956  956  MET MET A . n 
A 1 105 GLU 105 957  957  GLU GLU A . n 
A 1 106 PHE 106 958  958  PHE PHE A . n 
A 1 107 LEU 107 959  959  LEU LEU A . n 
A 1 108 PRO 108 960  960  PRO PRO A . n 
A 1 109 SER 109 961  961  SER SER A . n 
A 1 110 GLY 110 962  962  GLY GLY A . n 
A 1 111 SER 111 963  963  SER SER A . n 
A 1 112 LEU 112 964  964  LEU LEU A . n 
A 1 113 LYS 113 965  965  LYS LYS A . n 
A 1 114 GLU 114 966  966  GLU GLU A . n 
A 1 115 TYR 115 967  967  TYR TYR A . n 
A 1 116 LEU 116 968  968  LEU LEU A . n 
A 1 117 PRO 117 969  969  PRO PRO A . n 
A 1 118 LYS 118 970  970  LYS LYS A . n 
A 1 119 ASN 119 971  971  ASN ASN A . n 
A 1 120 LYS 120 972  972  LYS LYS A . n 
A 1 121 ASN 121 973  973  ASN ASN A . n 
A 1 122 LYS 122 974  974  LYS LYS A . n 
A 1 123 ILE 123 975  975  ILE ILE A . n 
A 1 124 ASN 124 976  976  ASN ASN A . n 
A 1 125 LEU 125 977  977  LEU LEU A . n 
A 1 126 LYS 126 978  978  LYS LYS A . n 
A 1 127 GLN 127 979  979  GLN GLN A . n 
A 1 128 GLN 128 980  980  GLN GLN A . n 
A 1 129 LEU 129 981  981  LEU LEU A . n 
A 1 130 LYS 130 982  982  LYS LYS A . n 
A 1 131 TYR 131 983  983  TYR TYR A . n 
A 1 132 ALA 132 984  984  ALA ALA A . n 
A 1 133 VAL 133 985  985  VAL VAL A . n 
A 1 134 GLN 134 986  986  GLN GLN A . n 
A 1 135 ILE 135 987  987  ILE ILE A . n 
A 1 136 CYS 136 988  988  CYS CYS A . n 
A 1 137 LYS 137 989  989  LYS LYS A . n 
A 1 138 GLY 138 990  990  GLY GLY A . n 
A 1 139 MET 139 991  991  MET MET A . n 
A 1 140 ASP 140 992  992  ASP ASP A . n 
A 1 141 TYR 141 993  993  TYR TYR A . n 
A 1 142 LEU 142 994  994  LEU LEU A . n 
A 1 143 GLY 143 995  995  GLY GLY A . n 
A 1 144 SER 144 996  996  SER SER A . n 
A 1 145 ARG 145 997  997  ARG ARG A . n 
A 1 146 GLN 146 998  998  GLN GLN A . n 
A 1 147 TYR 147 999  999  TYR TYR A . n 
A 1 148 VAL 148 1000 1000 VAL VAL A . n 
A 1 149 HIS 149 1001 1001 HIS HIS A . n 
A 1 150 ARG 150 1002 1002 ARG ARG A . n 
A 1 151 ASP 151 1003 1003 ASP ASP A . n 
A 1 152 LEU 152 1004 1004 LEU LEU A . n 
A 1 153 ALA 153 1005 1005 ALA ALA A . n 
A 1 154 ALA 154 1006 1006 ALA ALA A . n 
A 1 155 ARG 155 1007 1007 ARG ARG A . n 
A 1 156 ASN 156 1008 1008 ASN ASN A . n 
A 1 157 VAL 157 1009 1009 VAL VAL A . n 
A 1 158 LEU 158 1010 1010 LEU LEU A . n 
A 1 159 VAL 159 1011 1011 VAL VAL A . n 
A 1 160 GLU 160 1012 1012 GLU GLU A . n 
A 1 161 SER 161 1013 1013 SER SER A . n 
A 1 162 GLU 162 1014 1014 GLU GLU A . n 
A 1 163 HIS 163 1015 1015 HIS HIS A . n 
A 1 164 GLN 164 1016 1016 GLN GLN A . n 
A 1 165 VAL 165 1017 1017 VAL VAL A . n 
A 1 166 LYS 166 1018 1018 LYS LYS A . n 
A 1 167 ILE 167 1019 1019 ILE ILE A . n 
A 1 168 GLY 168 1020 1020 GLY GLY A . n 
A 1 169 ASP 169 1021 1021 ASP ASP A . n 
A 1 170 PHE 170 1022 1022 PHE PHE A . n 
A 1 171 GLY 171 1023 1023 GLY GLY A . n 
A 1 172 LEU 172 1024 1024 LEU LEU A . n 
A 1 173 THR 173 1025 1025 THR THR A . n 
A 1 174 LYS 174 1026 1026 LYS LYS A . n 
A 1 175 ALA 175 1027 1027 ALA ALA A . n 
A 1 176 ILE 176 1028 1028 ILE ILE A . n 
A 1 177 GLU 177 1029 1029 GLU GLU A . n 
A 1 178 THR 178 1030 1030 THR THR A . n 
A 1 179 ASP 179 1031 1031 ASP ASP A . n 
A 1 180 LYS 180 1032 1032 LYS LYS A . n 
A 1 181 GLU 181 1033 1033 GLU GLU A . n 
A 1 182 PTR 182 1034 1034 PTR PTR A . n 
A 1 183 PTR 183 1035 1035 PTR PTR A . n 
A 1 184 THR 184 1036 1036 THR THR A . n 
A 1 185 VAL 185 1037 1037 VAL VAL A . n 
A 1 186 LYS 186 1038 1038 LYS LYS A . n 
A 1 187 ASP 187 1039 1039 ASP ASP A . n 
A 1 188 ASP 188 1040 1040 ASP ASP A . n 
A 1 189 ARG 189 1041 1041 ARG ARG A . n 
A 1 190 ASP 190 1042 1042 ASP ASP A . n 
A 1 191 SER 191 1043 1043 SER SER A . n 
A 1 192 PRO 192 1044 1044 PRO PRO A . n 
A 1 193 VAL 193 1045 1045 VAL VAL A . n 
A 1 194 PHE 194 1046 1046 PHE PHE A . n 
A 1 195 TRP 195 1047 1047 TRP TRP A . n 
A 1 196 TYR 196 1048 1048 TYR TYR A . n 
A 1 197 ALA 197 1049 1049 ALA ALA A . n 
A 1 198 PRO 198 1050 1050 PRO PRO A . n 
A 1 199 GLU 199 1051 1051 GLU GLU A . n 
A 1 200 CYS 200 1052 1052 CYS CYS A . n 
A 1 201 LEU 201 1053 1053 LEU LEU A . n 
A 1 202 MET 202 1054 1054 MET MET A . n 
A 1 203 GLN 203 1055 1055 GLN GLN A . n 
A 1 204 SER 204 1056 1056 SER SER A . n 
A 1 205 LYS 205 1057 1057 LYS LYS A . n 
A 1 206 PHE 206 1058 1058 PHE PHE A . n 
A 1 207 TYR 207 1059 1059 TYR TYR A . n 
A 1 208 ILE 208 1060 1060 ILE ILE A . n 
A 1 209 ALA 209 1061 1061 ALA ALA A . n 
A 1 210 SER 210 1062 1062 SER SER A . n 
A 1 211 ASP 211 1063 1063 ASP ASP A . n 
A 1 212 VAL 212 1064 1064 VAL VAL A . n 
A 1 213 TRP 213 1065 1065 TRP TRP A . n 
A 1 214 SER 214 1066 1066 SER SER A . n 
A 1 215 PHE 215 1067 1067 PHE PHE A . n 
A 1 216 GLY 216 1068 1068 GLY GLY A . n 
A 1 217 VAL 217 1069 1069 VAL VAL A . n 
A 1 218 THR 218 1070 1070 THR THR A . n 
A 1 219 LEU 219 1071 1071 LEU LEU A . n 
A 1 220 HIS 220 1072 1072 HIS HIS A . n 
A 1 221 GLU 221 1073 1073 GLU GLU A . n 
A 1 222 LEU 222 1074 1074 LEU LEU A . n 
A 1 223 LEU 223 1075 1075 LEU LEU A . n 
A 1 224 THR 224 1076 1076 THR THR A . n 
A 1 225 TYR 225 1077 1077 TYR TYR A . n 
A 1 226 CYS 226 1078 1078 CYS CYS A . n 
A 1 227 ASP 227 1079 1079 ASP ASP A . n 
A 1 228 SER 228 1080 1080 SER SER A . n 
A 1 229 ASP 229 1081 1081 ASP ASP A . n 
A 1 230 SER 230 1082 1082 SER SER A . n 
A 1 231 SER 231 1083 1083 SER SER A . n 
A 1 232 PRO 232 1084 1084 PRO PRO A . n 
A 1 233 MET 233 1085 1085 MET MET A . n 
A 1 234 ALA 234 1086 1086 ALA ALA A . n 
A 1 235 LEU 235 1087 1087 LEU LEU A . n 
A 1 236 PHE 236 1088 1088 PHE PHE A . n 
A 1 237 LEU 237 1089 1089 LEU LEU A . n 
A 1 238 LYS 238 1090 1090 LYS LYS A . n 
A 1 239 MET 239 1091 1091 MET MET A . n 
A 1 240 ILE 240 1092 1092 ILE ILE A . n 
A 1 241 GLY 241 1093 1093 GLY GLY A . n 
A 1 242 PRO 242 1094 1094 PRO PRO A . n 
A 1 243 THR 243 1095 1095 THR THR A . n 
A 1 244 HIS 244 1096 1096 HIS HIS A . n 
A 1 245 GLY 245 1097 1097 GLY GLY A . n 
A 1 246 GLN 246 1098 1098 GLN GLN A . n 
A 1 247 MET 247 1099 1099 MET MET A . n 
A 1 248 THR 248 1100 1100 THR THR A . n 
A 1 249 VAL 249 1101 1101 VAL VAL A . n 
A 1 250 THR 250 1102 1102 THR THR A . n 
A 1 251 ARG 251 1103 1103 ARG ARG A . n 
A 1 252 LEU 252 1104 1104 LEU LEU A . n 
A 1 253 VAL 253 1105 1105 VAL VAL A . n 
A 1 254 ASN 254 1106 1106 ASN ASN A . n 
A 1 255 THR 255 1107 1107 THR THR A . n 
A 1 256 LEU 256 1108 1108 LEU LEU A . n 
A 1 257 LYS 257 1109 1109 LYS LYS A . n 
A 1 258 GLU 258 1110 1110 GLU GLU A . n 
A 1 259 GLY 259 1111 1111 GLY GLY A . n 
A 1 260 LYS 260 1112 1112 LYS LYS A . n 
A 1 261 ARG 261 1113 1113 ARG ARG A . n 
A 1 262 LEU 262 1114 1114 LEU LEU A . n 
A 1 263 PRO 263 1115 1115 PRO PRO A . n 
A 1 264 CYS 264 1116 1116 CYS CYS A . n 
A 1 265 PRO 265 1117 1117 PRO PRO A . n 
A 1 266 PRO 266 1118 1118 PRO PRO A . n 
A 1 267 ASN 267 1119 1119 ASN ASN A . n 
A 1 268 CYS 268 1120 1120 CYS CYS A . n 
A 1 269 PRO 269 1121 1121 PRO PRO A . n 
A 1 270 ASP 270 1122 1122 ASP ASP A . n 
A 1 271 GLU 271 1123 1123 GLU GLU A . n 
A 1 272 VAL 272 1124 1124 VAL VAL A . n 
A 1 273 TYR 273 1125 1125 TYR TYR A . n 
A 1 274 GLN 274 1126 1126 GLN GLN A . n 
A 1 275 LEU 275 1127 1127 LEU LEU A . n 
A 1 276 MET 276 1128 1128 MET MET A . n 
A 1 277 ARG 277 1129 1129 ARG ARG A . n 
A 1 278 LYS 278 1130 1130 LYS LYS A . n 
A 1 279 CYS 279 1131 1131 CYS CYS A . n 
A 1 280 TRP 280 1132 1132 TRP TRP A . n 
A 1 281 GLU 281 1133 1133 GLU GLU A . n 
A 1 282 PHE 282 1134 1134 PHE PHE A . n 
A 1 283 GLN 283 1135 1135 GLN GLN A . n 
A 1 284 PRO 284 1136 1136 PRO PRO A . n 
A 1 285 SER 285 1137 1137 SER SER A . n 
A 1 286 ASN 286 1138 1138 ASN ASN A . n 
A 1 287 ARG 287 1139 1139 ARG ARG A . n 
A 1 288 THR 288 1140 1140 THR THR A . n 
A 1 289 SER 289 1141 1141 SER SER A . n 
A 1 290 PHE 290 1142 1142 PHE PHE A . n 
A 1 291 GLN 291 1143 1143 GLN GLN A . n 
A 1 292 ASN 292 1144 1144 ASN ASN A . n 
A 1 293 LEU 293 1145 1145 LEU LEU A . n 
A 1 294 ILE 294 1146 1146 ILE ILE A . n 
A 1 295 GLU 295 1147 1147 GLU GLU A . n 
A 1 296 GLY 296 1148 1148 GLY GLY A . n 
A 1 297 PHE 297 1149 1149 PHE PHE A . n 
A 1 298 GLU 298 1150 1150 GLU GLU A . n 
A 1 299 ALA 299 1151 1151 ALA ALA A . n 
A 1 300 LEU 300 1152 1152 LEU LEU A . n 
A 1 301 LEU 301 1153 1153 LEU LEU A . n 
A 1 302 LYS 302 1154 1154 LYS LYS A . n 
B 1 1   GLY 1   853  ?    ?   ?   B . n 
B 1 2   ASP 2   854  ?    ?   ?   B . n 
B 1 3   ILE 3   855  ?    ?   ?   B . n 
B 1 4   VAL 4   856  ?    ?   ?   B . n 
B 1 5   SER 5   857  ?    ?   ?   B . n 
B 1 6   GLU 6   858  ?    ?   ?   B . n 
B 1 7   LYS 7   859  ?    ?   ?   B . n 
B 1 8   LYS 8   860  ?    ?   ?   B . n 
B 1 9   PRO 9   861  ?    ?   ?   B . n 
B 1 10  ALA 10  862  ?    ?   ?   B . n 
B 1 11  THR 11  863  ?    ?   ?   B . n 
B 1 12  GLU 12  864  ?    ?   ?   B . n 
B 1 13  VAL 13  865  865  VAL VAL B . n 
B 1 14  ASP 14  866  866  ASP ASP B . n 
B 1 15  PRO 15  867  867  PRO PRO B . n 
B 1 16  THR 16  868  868  THR THR B . n 
B 1 17  HIS 17  869  869  HIS HIS B . n 
B 1 18  PHE 18  870  870  PHE PHE B . n 
B 1 19  GLU 19  871  871  GLU GLU B . n 
B 1 20  LYS 20  872  872  LYS LYS B . n 
B 1 21  ARG 21  873  873  ARG ARG B . n 
B 1 22  PHE 22  874  874  PHE PHE B . n 
B 1 23  LEU 23  875  875  LEU LEU B . n 
B 1 24  LYS 24  876  876  LYS LYS B . n 
B 1 25  ARG 25  877  877  ARG ARG B . n 
B 1 26  ILE 26  878  878  ILE ILE B . n 
B 1 27  ARG 27  879  879  ARG ARG B . n 
B 1 28  ASP 28  880  880  ASP ASP B . n 
B 1 29  LEU 29  881  881  LEU LEU B . n 
B 1 30  GLY 30  882  882  GLY GLY B . n 
B 1 31  GLU 31  883  883  GLU GLU B . n 
B 1 32  GLY 32  884  884  GLY GLY B . n 
B 1 33  HIS 33  885  885  HIS HIS B . n 
B 1 34  PHE 34  886  886  PHE PHE B . n 
B 1 35  GLY 35  887  887  GLY GLY B . n 
B 1 36  LYS 36  888  888  LYS LYS B . n 
B 1 37  VAL 37  889  889  VAL VAL B . n 
B 1 38  GLU 38  890  890  GLU GLU B . n 
B 1 39  LEU 39  891  891  LEU LEU B . n 
B 1 40  CYS 40  892  892  CYS CYS B . n 
B 1 41  ARG 41  893  893  ARG ARG B . n 
B 1 42  TYR 42  894  894  TYR TYR B . n 
B 1 43  ASP 43  895  895  ASP ASP B . n 
B 1 44  PRO 44  896  896  PRO PRO B . n 
B 1 45  GLU 45  897  897  GLU GLU B . n 
B 1 46  GLY 46  898  898  GLY GLY B . n 
B 1 47  ASP 47  899  899  ASP ASP B . n 
B 1 48  ASN 48  900  900  ASN ASN B . n 
B 1 49  THR 49  901  901  THR THR B . n 
B 1 50  GLY 50  902  902  GLY GLY B . n 
B 1 51  GLU 51  903  903  GLU GLU B . n 
B 1 52  GLN 52  904  904  GLN GLN B . n 
B 1 53  VAL 53  905  905  VAL VAL B . n 
B 1 54  ALA 54  906  906  ALA ALA B . n 
B 1 55  VAL 55  907  907  VAL VAL B . n 
B 1 56  LYS 56  908  908  LYS LYS B . n 
B 1 57  SER 57  909  909  SER SER B . n 
B 1 58  LEU 58  910  910  LEU LEU B . n 
B 1 59  LYS 59  911  911  LYS LYS B . n 
B 1 60  PRO 60  912  912  PRO PRO B . n 
B 1 61  GLU 61  913  ?    ?   ?   B . n 
B 1 62  SER 62  914  ?    ?   ?   B . n 
B 1 63  GLY 63  915  ?    ?   ?   B . n 
B 1 64  GLY 64  916  916  GLY GLY B . n 
B 1 65  ASN 65  917  917  ASN ASN B . n 
B 1 66  HIS 66  918  918  HIS HIS B . n 
B 1 67  ILE 67  919  919  ILE ILE B . n 
B 1 68  ALA 68  920  920  ALA ALA B . n 
B 1 69  ASP 69  921  921  ASP ASP B . n 
B 1 70  LEU 70  922  922  LEU LEU B . n 
B 1 71  LYS 71  923  923  LYS LYS B . n 
B 1 72  LYS 72  924  924  LYS LYS B . n 
B 1 73  GLU 73  925  925  GLU GLU B . n 
B 1 74  ILE 74  926  926  ILE ILE B . n 
B 1 75  GLU 75  927  927  GLU GLU B . n 
B 1 76  ILE 76  928  928  ILE ILE B . n 
B 1 77  LEU 77  929  929  LEU LEU B . n 
B 1 78  ARG 78  930  930  ARG ARG B . n 
B 1 79  ASN 79  931  931  ASN ASN B . n 
B 1 80  LEU 80  932  932  LEU LEU B . n 
B 1 81  TYR 81  933  933  TYR TYR B . n 
B 1 82  HIS 82  934  934  HIS HIS B . n 
B 1 83  GLU 83  935  935  GLU GLU B . n 
B 1 84  ASN 84  936  936  ASN ASN B . n 
B 1 85  ILE 85  937  937  ILE ILE B . n 
B 1 86  VAL 86  938  938  VAL VAL B . n 
B 1 87  LYS 87  939  939  LYS LYS B . n 
B 1 88  TYR 88  940  940  TYR TYR B . n 
B 1 89  LYS 89  941  941  LYS LYS B . n 
B 1 90  GLY 90  942  942  GLY GLY B . n 
B 1 91  ILE 91  943  943  ILE ILE B . n 
B 1 92  CYS 92  944  944  CYS CYS B . n 
B 1 93  THR 93  945  945  THR THR B . n 
B 1 94  GLU 94  946  ?    ?   ?   B . n 
B 1 95  ASP 95  947  ?    ?   ?   B . n 
B 1 96  GLY 96  948  ?    ?   ?   B . n 
B 1 97  GLY 97  949  ?    ?   ?   B . n 
B 1 98  ASN 98  950  950  ASN ASN B . n 
B 1 99  GLY 99  951  951  GLY GLY B . n 
B 1 100 ILE 100 952  952  ILE ILE B . n 
B 1 101 LYS 101 953  953  LYS LYS B . n 
B 1 102 LEU 102 954  954  LEU LEU B . n 
B 1 103 ILE 103 955  955  ILE ILE B . n 
B 1 104 MET 104 956  956  MET MET B . n 
B 1 105 GLU 105 957  957  GLU GLU B . n 
B 1 106 PHE 106 958  958  PHE PHE B . n 
B 1 107 LEU 107 959  959  LEU LEU B . n 
B 1 108 PRO 108 960  960  PRO PRO B . n 
B 1 109 SER 109 961  961  SER SER B . n 
B 1 110 GLY 110 962  962  GLY GLY B . n 
B 1 111 SER 111 963  963  SER SER B . n 
B 1 112 LEU 112 964  964  LEU LEU B . n 
B 1 113 LYS 113 965  965  LYS LYS B . n 
B 1 114 GLU 114 966  966  GLU GLU B . n 
B 1 115 TYR 115 967  967  TYR TYR B . n 
B 1 116 LEU 116 968  968  LEU LEU B . n 
B 1 117 PRO 117 969  969  PRO PRO B . n 
B 1 118 LYS 118 970  970  LYS LYS B . n 
B 1 119 ASN 119 971  971  ASN ASN B . n 
B 1 120 LYS 120 972  972  LYS LYS B . n 
B 1 121 ASN 121 973  973  ASN ASN B . n 
B 1 122 LYS 122 974  974  LYS LYS B . n 
B 1 123 ILE 123 975  975  ILE ILE B . n 
B 1 124 ASN 124 976  976  ASN ASN B . n 
B 1 125 LEU 125 977  977  LEU LEU B . n 
B 1 126 LYS 126 978  978  LYS LYS B . n 
B 1 127 GLN 127 979  979  GLN GLN B . n 
B 1 128 GLN 128 980  980  GLN GLN B . n 
B 1 129 LEU 129 981  981  LEU LEU B . n 
B 1 130 LYS 130 982  982  LYS LYS B . n 
B 1 131 TYR 131 983  983  TYR TYR B . n 
B 1 132 ALA 132 984  984  ALA ALA B . n 
B 1 133 VAL 133 985  985  VAL VAL B . n 
B 1 134 GLN 134 986  986  GLN GLN B . n 
B 1 135 ILE 135 987  987  ILE ILE B . n 
B 1 136 CYS 136 988  988  CYS CYS B . n 
B 1 137 LYS 137 989  989  LYS LYS B . n 
B 1 138 GLY 138 990  990  GLY GLY B . n 
B 1 139 MET 139 991  991  MET MET B . n 
B 1 140 ASP 140 992  992  ASP ASP B . n 
B 1 141 TYR 141 993  993  TYR TYR B . n 
B 1 142 LEU 142 994  994  LEU LEU B . n 
B 1 143 GLY 143 995  995  GLY GLY B . n 
B 1 144 SER 144 996  996  SER SER B . n 
B 1 145 ARG 145 997  997  ARG ARG B . n 
B 1 146 GLN 146 998  998  GLN GLN B . n 
B 1 147 TYR 147 999  999  TYR TYR B . n 
B 1 148 VAL 148 1000 1000 VAL VAL B . n 
B 1 149 HIS 149 1001 1001 HIS HIS B . n 
B 1 150 ARG 150 1002 1002 ARG ARG B . n 
B 1 151 ASP 151 1003 1003 ASP ASP B . n 
B 1 152 LEU 152 1004 1004 LEU LEU B . n 
B 1 153 ALA 153 1005 1005 ALA ALA B . n 
B 1 154 ALA 154 1006 1006 ALA ALA B . n 
B 1 155 ARG 155 1007 1007 ARG ARG B . n 
B 1 156 ASN 156 1008 1008 ASN ASN B . n 
B 1 157 VAL 157 1009 1009 VAL VAL B . n 
B 1 158 LEU 158 1010 1010 LEU LEU B . n 
B 1 159 VAL 159 1011 1011 VAL VAL B . n 
B 1 160 GLU 160 1012 1012 GLU GLU B . n 
B 1 161 SER 161 1013 1013 SER SER B . n 
B 1 162 GLU 162 1014 1014 GLU GLU B . n 
B 1 163 HIS 163 1015 1015 HIS HIS B . n 
B 1 164 GLN 164 1016 1016 GLN GLN B . n 
B 1 165 VAL 165 1017 1017 VAL VAL B . n 
B 1 166 LYS 166 1018 1018 LYS LYS B . n 
B 1 167 ILE 167 1019 1019 ILE ILE B . n 
B 1 168 GLY 168 1020 1020 GLY GLY B . n 
B 1 169 ASP 169 1021 1021 ASP ASP B . n 
B 1 170 PHE 170 1022 1022 PHE PHE B . n 
B 1 171 GLY 171 1023 1023 GLY GLY B . n 
B 1 172 LEU 172 1024 1024 LEU LEU B . n 
B 1 173 THR 173 1025 1025 THR THR B . n 
B 1 174 LYS 174 1026 1026 LYS LYS B . n 
B 1 175 ALA 175 1027 1027 ALA ALA B . n 
B 1 176 ILE 176 1028 1028 ILE ILE B . n 
B 1 177 GLU 177 1029 1029 GLU GLU B . n 
B 1 178 THR 178 1030 1030 THR THR B . n 
B 1 179 ASP 179 1031 1031 ASP ASP B . n 
B 1 180 LYS 180 1032 1032 LYS LYS B . n 
B 1 181 GLU 181 1033 1033 GLU GLU B . n 
B 1 182 PTR 182 1034 1034 PTR PTR B . n 
B 1 183 PTR 183 1035 1035 PTR PTR B . n 
B 1 184 THR 184 1036 1036 THR THR B . n 
B 1 185 VAL 185 1037 1037 VAL VAL B . n 
B 1 186 LYS 186 1038 1038 LYS LYS B . n 
B 1 187 ASP 187 1039 1039 ASP ASP B . n 
B 1 188 ASP 188 1040 1040 ASP ASP B . n 
B 1 189 ARG 189 1041 1041 ARG ARG B . n 
B 1 190 ASP 190 1042 1042 ASP ASP B . n 
B 1 191 SER 191 1043 1043 SER SER B . n 
B 1 192 PRO 192 1044 1044 PRO PRO B . n 
B 1 193 VAL 193 1045 1045 VAL VAL B . n 
B 1 194 PHE 194 1046 1046 PHE PHE B . n 
B 1 195 TRP 195 1047 1047 TRP TRP B . n 
B 1 196 TYR 196 1048 1048 TYR TYR B . n 
B 1 197 ALA 197 1049 1049 ALA ALA B . n 
B 1 198 PRO 198 1050 1050 PRO PRO B . n 
B 1 199 GLU 199 1051 1051 GLU GLU B . n 
B 1 200 CYS 200 1052 1052 CYS CYS B . n 
B 1 201 LEU 201 1053 1053 LEU LEU B . n 
B 1 202 MET 202 1054 1054 MET MET B . n 
B 1 203 GLN 203 1055 1055 GLN GLN B . n 
B 1 204 SER 204 1056 1056 SER SER B . n 
B 1 205 LYS 205 1057 1057 LYS LYS B . n 
B 1 206 PHE 206 1058 1058 PHE PHE B . n 
B 1 207 TYR 207 1059 1059 TYR TYR B . n 
B 1 208 ILE 208 1060 1060 ILE ILE B . n 
B 1 209 ALA 209 1061 1061 ALA ALA B . n 
B 1 210 SER 210 1062 1062 SER SER B . n 
B 1 211 ASP 211 1063 1063 ASP ASP B . n 
B 1 212 VAL 212 1064 1064 VAL VAL B . n 
B 1 213 TRP 213 1065 1065 TRP TRP B . n 
B 1 214 SER 214 1066 1066 SER SER B . n 
B 1 215 PHE 215 1067 1067 PHE PHE B . n 
B 1 216 GLY 216 1068 1068 GLY GLY B . n 
B 1 217 VAL 217 1069 1069 VAL VAL B . n 
B 1 218 THR 218 1070 1070 THR THR B . n 
B 1 219 LEU 219 1071 1071 LEU LEU B . n 
B 1 220 HIS 220 1072 1072 HIS HIS B . n 
B 1 221 GLU 221 1073 1073 GLU GLU B . n 
B 1 222 LEU 222 1074 1074 LEU LEU B . n 
B 1 223 LEU 223 1075 1075 LEU LEU B . n 
B 1 224 THR 224 1076 1076 THR THR B . n 
B 1 225 TYR 225 1077 1077 TYR TYR B . n 
B 1 226 CYS 226 1078 1078 CYS CYS B . n 
B 1 227 ASP 227 1079 1079 ASP ASP B . n 
B 1 228 SER 228 1080 1080 SER SER B . n 
B 1 229 ASP 229 1081 1081 ASP ASP B . n 
B 1 230 SER 230 1082 1082 SER SER B . n 
B 1 231 SER 231 1083 1083 SER SER B . n 
B 1 232 PRO 232 1084 1084 PRO PRO B . n 
B 1 233 MET 233 1085 1085 MET MET B . n 
B 1 234 ALA 234 1086 1086 ALA ALA B . n 
B 1 235 LEU 235 1087 1087 LEU LEU B . n 
B 1 236 PHE 236 1088 1088 PHE PHE B . n 
B 1 237 LEU 237 1089 1089 LEU LEU B . n 
B 1 238 LYS 238 1090 1090 LYS LYS B . n 
B 1 239 MET 239 1091 1091 MET MET B . n 
B 1 240 ILE 240 1092 1092 ILE ILE B . n 
B 1 241 GLY 241 1093 1093 GLY GLY B . n 
B 1 242 PRO 242 1094 1094 PRO PRO B . n 
B 1 243 THR 243 1095 1095 THR THR B . n 
B 1 244 HIS 244 1096 1096 HIS HIS B . n 
B 1 245 GLY 245 1097 1097 GLY GLY B . n 
B 1 246 GLN 246 1098 1098 GLN GLN B . n 
B 1 247 MET 247 1099 1099 MET MET B . n 
B 1 248 THR 248 1100 1100 THR THR B . n 
B 1 249 VAL 249 1101 1101 VAL VAL B . n 
B 1 250 THR 250 1102 1102 THR THR B . n 
B 1 251 ARG 251 1103 1103 ARG ARG B . n 
B 1 252 LEU 252 1104 1104 LEU LEU B . n 
B 1 253 VAL 253 1105 1105 VAL VAL B . n 
B 1 254 ASN 254 1106 1106 ASN ASN B . n 
B 1 255 THR 255 1107 1107 THR THR B . n 
B 1 256 LEU 256 1108 1108 LEU LEU B . n 
B 1 257 LYS 257 1109 1109 LYS LYS B . n 
B 1 258 GLU 258 1110 1110 GLU GLU B . n 
B 1 259 GLY 259 1111 1111 GLY GLY B . n 
B 1 260 LYS 260 1112 1112 LYS LYS B . n 
B 1 261 ARG 261 1113 1113 ARG ARG B . n 
B 1 262 LEU 262 1114 1114 LEU LEU B . n 
B 1 263 PRO 263 1115 1115 PRO PRO B . n 
B 1 264 CYS 264 1116 1116 CYS CYS B . n 
B 1 265 PRO 265 1117 1117 PRO PRO B . n 
B 1 266 PRO 266 1118 1118 PRO PRO B . n 
B 1 267 ASN 267 1119 1119 ASN ASN B . n 
B 1 268 CYS 268 1120 1120 CYS CYS B . n 
B 1 269 PRO 269 1121 1121 PRO PRO B . n 
B 1 270 ASP 270 1122 1122 ASP ASP B . n 
B 1 271 GLU 271 1123 1123 GLU GLU B . n 
B 1 272 VAL 272 1124 1124 VAL VAL B . n 
B 1 273 TYR 273 1125 1125 TYR TYR B . n 
B 1 274 GLN 274 1126 1126 GLN GLN B . n 
B 1 275 LEU 275 1127 1127 LEU LEU B . n 
B 1 276 MET 276 1128 1128 MET MET B . n 
B 1 277 ARG 277 1129 1129 ARG ARG B . n 
B 1 278 LYS 278 1130 1130 LYS LYS B . n 
B 1 279 CYS 279 1131 1131 CYS CYS B . n 
B 1 280 TRP 280 1132 1132 TRP TRP B . n 
B 1 281 GLU 281 1133 1133 GLU GLU B . n 
B 1 282 PHE 282 1134 1134 PHE PHE B . n 
B 1 283 GLN 283 1135 1135 GLN GLN B . n 
B 1 284 PRO 284 1136 1136 PRO PRO B . n 
B 1 285 SER 285 1137 1137 SER SER B . n 
B 1 286 ASN 286 1138 1138 ASN ASN B . n 
B 1 287 ARG 287 1139 1139 ARG ARG B . n 
B 1 288 THR 288 1140 1140 THR THR B . n 
B 1 289 SER 289 1141 1141 SER SER B . n 
B 1 290 PHE 290 1142 1142 PHE PHE B . n 
B 1 291 GLN 291 1143 1143 GLN GLN B . n 
B 1 292 ASN 292 1144 1144 ASN ASN B . n 
B 1 293 LEU 293 1145 1145 LEU LEU B . n 
B 1 294 ILE 294 1146 1146 ILE ILE B . n 
B 1 295 GLU 295 1147 1147 GLU GLU B . n 
B 1 296 GLY 296 1148 1148 GLY GLY B . n 
B 1 297 PHE 297 1149 1149 PHE PHE B . n 
B 1 298 GLU 298 1150 1150 GLU GLU B . n 
B 1 299 ALA 299 1151 1151 ALA ALA B . n 
B 1 300 LEU 300 1152 1152 LEU LEU B . n 
B 1 301 LEU 301 1153 1153 LEU LEU B . n 
B 1 302 LYS 302 1154 1154 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H5R 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H5R 
_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 A1H5R 1   1201 1   A1H5R INX A . 
D 3 NA    1   1202 2   NA    NA  A . 
E 3 NA    1   1203 3   NA    NA  A . 
F 3 NA    1   1204 4   NA    NA  A . 
G 2 A1H5R 1   1201 2   A1H5R INX B . 
H 4 HOH   1   1301 429 HOH   HOH A . 
H 4 HOH   2   1302 88  HOH   HOH A . 
H 4 HOH   3   1303 348 HOH   HOH A . 
H 4 HOH   4   1304 435 HOH   HOH A . 
H 4 HOH   5   1305 273 HOH   HOH A . 
H 4 HOH   6   1306 102 HOH   HOH A . 
H 4 HOH   7   1307 295 HOH   HOH A . 
H 4 HOH   8   1308 159 HOH   HOH A . 
H 4 HOH   9   1309 59  HOH   HOH A . 
H 4 HOH   10  1310 198 HOH   HOH A . 
H 4 HOH   11  1311 55  HOH   HOH A . 
H 4 HOH   12  1312 96  HOH   HOH A . 
H 4 HOH   13  1313 334 HOH   HOH A . 
H 4 HOH   14  1314 123 HOH   HOH A . 
H 4 HOH   15  1315 145 HOH   HOH A . 
H 4 HOH   16  1316 152 HOH   HOH A . 
H 4 HOH   17  1317 292 HOH   HOH A . 
H 4 HOH   18  1318 107 HOH   HOH A . 
H 4 HOH   19  1319 138 HOH   HOH A . 
H 4 HOH   20  1320 247 HOH   HOH A . 
H 4 HOH   21  1321 414 HOH   HOH A . 
H 4 HOH   22  1322 81  HOH   HOH A . 
H 4 HOH   23  1323 84  HOH   HOH A . 
H 4 HOH   24  1324 75  HOH   HOH A . 
H 4 HOH   25  1325 233 HOH   HOH A . 
H 4 HOH   26  1326 252 HOH   HOH A . 
H 4 HOH   27  1327 67  HOH   HOH A . 
H 4 HOH   28  1328 276 HOH   HOH A . 
H 4 HOH   29  1329 115 HOH   HOH A . 
H 4 HOH   30  1330 34  HOH   HOH A . 
H 4 HOH   31  1331 45  HOH   HOH A . 
H 4 HOH   32  1332 170 HOH   HOH A . 
H 4 HOH   33  1333 366 HOH   HOH A . 
H 4 HOH   34  1334 279 HOH   HOH A . 
H 4 HOH   35  1335 28  HOH   HOH A . 
H 4 HOH   36  1336 224 HOH   HOH A . 
H 4 HOH   37  1337 165 HOH   HOH A . 
H 4 HOH   38  1338 417 HOH   HOH A . 
H 4 HOH   39  1339 297 HOH   HOH A . 
H 4 HOH   40  1340 322 HOH   HOH A . 
H 4 HOH   41  1341 27  HOH   HOH A . 
H 4 HOH   42  1342 41  HOH   HOH A . 
H 4 HOH   43  1343 260 HOH   HOH A . 
H 4 HOH   44  1344 400 HOH   HOH A . 
H 4 HOH   45  1345 271 HOH   HOH A . 
H 4 HOH   46  1346 319 HOH   HOH A . 
H 4 HOH   47  1347 422 HOH   HOH A . 
H 4 HOH   48  1348 227 HOH   HOH A . 
H 4 HOH   49  1349 21  HOH   HOH A . 
H 4 HOH   50  1350 150 HOH   HOH A . 
H 4 HOH   51  1351 156 HOH   HOH A . 
H 4 HOH   52  1352 313 HOH   HOH A . 
H 4 HOH   53  1353 253 HOH   HOH A . 
H 4 HOH   54  1354 267 HOH   HOH A . 
H 4 HOH   55  1355 244 HOH   HOH A . 
H 4 HOH   56  1356 401 HOH   HOH A . 
H 4 HOH   57  1357 26  HOH   HOH A . 
H 4 HOH   58  1358 125 HOH   HOH A . 
H 4 HOH   59  1359 50  HOH   HOH A . 
H 4 HOH   60  1360 139 HOH   HOH A . 
H 4 HOH   61  1361 69  HOH   HOH A . 
H 4 HOH   62  1362 410 HOH   HOH A . 
H 4 HOH   63  1363 91  HOH   HOH A . 
H 4 HOH   64  1364 430 HOH   HOH A . 
H 4 HOH   65  1365 44  HOH   HOH A . 
H 4 HOH   66  1366 220 HOH   HOH A . 
H 4 HOH   67  1367 217 HOH   HOH A . 
H 4 HOH   68  1368 6   HOH   HOH A . 
H 4 HOH   69  1369 54  HOH   HOH A . 
H 4 HOH   70  1370 274 HOH   HOH A . 
H 4 HOH   71  1371 18  HOH   HOH A . 
H 4 HOH   72  1372 182 HOH   HOH A . 
H 4 HOH   73  1373 3   HOH   HOH A . 
H 4 HOH   74  1374 231 HOH   HOH A . 
H 4 HOH   75  1375 375 HOH   HOH A . 
H 4 HOH   76  1376 337 HOH   HOH A . 
H 4 HOH   77  1377 36  HOH   HOH A . 
H 4 HOH   78  1378 121 HOH   HOH A . 
H 4 HOH   79  1379 288 HOH   HOH A . 
H 4 HOH   80  1380 13  HOH   HOH A . 
H 4 HOH   81  1381 235 HOH   HOH A . 
H 4 HOH   82  1382 136 HOH   HOH A . 
H 4 HOH   83  1383 423 HOH   HOH A . 
H 4 HOH   84  1384 49  HOH   HOH A . 
H 4 HOH   85  1385 255 HOH   HOH A . 
H 4 HOH   86  1386 222 HOH   HOH A . 
H 4 HOH   87  1387 193 HOH   HOH A . 
H 4 HOH   88  1388 1   HOH   HOH A . 
H 4 HOH   89  1389 364 HOH   HOH A . 
H 4 HOH   90  1390 214 HOH   HOH A . 
H 4 HOH   91  1391 362 HOH   HOH A . 
H 4 HOH   92  1392 269 HOH   HOH A . 
H 4 HOH   93  1393 134 HOH   HOH A . 
H 4 HOH   94  1394 174 HOH   HOH A . 
H 4 HOH   95  1395 15  HOH   HOH A . 
H 4 HOH   96  1396 5   HOH   HOH A . 
H 4 HOH   97  1397 85  HOH   HOH A . 
H 4 HOH   98  1398 40  HOH   HOH A . 
H 4 HOH   99  1399 175 HOH   HOH A . 
H 4 HOH   100 1400 111 HOH   HOH A . 
H 4 HOH   101 1401 184 HOH   HOH A . 
H 4 HOH   102 1402 168 HOH   HOH A . 
H 4 HOH   103 1403 392 HOH   HOH A . 
H 4 HOH   104 1404 194 HOH   HOH A . 
H 4 HOH   105 1405 318 HOH   HOH A . 
H 4 HOH   106 1406 248 HOH   HOH A . 
H 4 HOH   107 1407 37  HOH   HOH A . 
H 4 HOH   108 1408 180 HOH   HOH A . 
H 4 HOH   109 1409 327 HOH   HOH A . 
H 4 HOH   110 1410 219 HOH   HOH A . 
H 4 HOH   111 1411 374 HOH   HOH A . 
H 4 HOH   112 1412 306 HOH   HOH A . 
H 4 HOH   113 1413 189 HOH   HOH A . 
H 4 HOH   114 1414 360 HOH   HOH A . 
H 4 HOH   115 1415 191 HOH   HOH A . 
H 4 HOH   116 1416 72  HOH   HOH A . 
H 4 HOH   117 1417 177 HOH   HOH A . 
H 4 HOH   118 1418 367 HOH   HOH A . 
H 4 HOH   119 1419 162 HOH   HOH A . 
H 4 HOH   120 1420 236 HOH   HOH A . 
H 4 HOH   121 1421 207 HOH   HOH A . 
H 4 HOH   122 1422 408 HOH   HOH A . 
H 4 HOH   123 1423 52  HOH   HOH A . 
H 4 HOH   124 1424 433 HOH   HOH A . 
H 4 HOH   125 1425 64  HOH   HOH A . 
H 4 HOH   126 1426 106 HOH   HOH A . 
H 4 HOH   127 1427 287 HOH   HOH A . 
H 4 HOH   128 1428 389 HOH   HOH A . 
H 4 HOH   129 1429 263 HOH   HOH A . 
H 4 HOH   130 1430 60  HOH   HOH A . 
H 4 HOH   131 1431 315 HOH   HOH A . 
H 4 HOH   132 1432 70  HOH   HOH A . 
H 4 HOH   133 1433 92  HOH   HOH A . 
H 4 HOH   134 1434 298 HOH   HOH A . 
H 4 HOH   135 1435 109 HOH   HOH A . 
H 4 HOH   136 1436 192 HOH   HOH A . 
H 4 HOH   137 1437 436 HOH   HOH A . 
H 4 HOH   138 1438 346 HOH   HOH A . 
H 4 HOH   139 1439 285 HOH   HOH A . 
H 4 HOH   140 1440 141 HOH   HOH A . 
H 4 HOH   141 1441 161 HOH   HOH A . 
H 4 HOH   142 1442 71  HOH   HOH A . 
H 4 HOH   143 1443 30  HOH   HOH A . 
H 4 HOH   144 1444 399 HOH   HOH A . 
H 4 HOH   145 1445 323 HOH   HOH A . 
H 4 HOH   146 1446 347 HOH   HOH A . 
H 4 HOH   147 1447 286 HOH   HOH A . 
H 4 HOH   148 1448 169 HOH   HOH A . 
H 4 HOH   149 1449 262 HOH   HOH A . 
H 4 HOH   150 1450 390 HOH   HOH A . 
H 4 HOH   151 1451 246 HOH   HOH A . 
H 4 HOH   152 1452 261 HOH   HOH A . 
H 4 HOH   153 1453 43  HOH   HOH A . 
H 4 HOH   154 1454 343 HOH   HOH A . 
H 4 HOH   155 1455 397 HOH   HOH A . 
H 4 HOH   156 1456 342 HOH   HOH A . 
H 4 HOH   157 1457 308 HOH   HOH A . 
H 4 HOH   158 1458 293 HOH   HOH A . 
H 4 HOH   159 1459 90  HOH   HOH A . 
H 4 HOH   160 1460 56  HOH   HOH A . 
H 4 HOH   161 1461 407 HOH   HOH A . 
H 4 HOH   162 1462 266 HOH   HOH A . 
H 4 HOH   163 1463 142 HOH   HOH A . 
H 4 HOH   164 1464 82  HOH   HOH A . 
H 4 HOH   165 1465 210 HOH   HOH A . 
H 4 HOH   166 1466 22  HOH   HOH A . 
H 4 HOH   167 1467 291 HOH   HOH A . 
H 4 HOH   168 1468 251 HOH   HOH A . 
H 4 HOH   169 1469 242 HOH   HOH A . 
H 4 HOH   170 1470 320 HOH   HOH A . 
H 4 HOH   171 1471 283 HOH   HOH A . 
H 4 HOH   172 1472 118 HOH   HOH A . 
H 4 HOH   173 1473 112 HOH   HOH A . 
H 4 HOH   174 1474 356 HOH   HOH A . 
H 4 HOH   175 1475 341 HOH   HOH A . 
H 4 HOH   176 1476 421 HOH   HOH A . 
H 4 HOH   177 1477 166 HOH   HOH A . 
H 4 HOH   178 1478 282 HOH   HOH A . 
H 4 HOH   179 1479 47  HOH   HOH A . 
H 4 HOH   180 1480 73  HOH   HOH A . 
H 4 HOH   181 1481 147 HOH   HOH A . 
H 4 HOH   182 1482 312 HOH   HOH A . 
H 4 HOH   183 1483 171 HOH   HOH A . 
H 4 HOH   184 1484 33  HOH   HOH A . 
H 4 HOH   185 1485 199 HOH   HOH A . 
H 4 HOH   186 1486 412 HOH   HOH A . 
H 4 HOH   187 1487 137 HOH   HOH A . 
H 4 HOH   188 1488 79  HOH   HOH A . 
H 4 HOH   189 1489 370 HOH   HOH A . 
H 4 HOH   190 1490 120 HOH   HOH A . 
H 4 HOH   191 1491 345 HOH   HOH A . 
H 4 HOH   192 1492 105 HOH   HOH A . 
H 4 HOH   193 1493 110 HOH   HOH A . 
H 4 HOH   194 1494 63  HOH   HOH A . 
H 4 HOH   195 1495 357 HOH   HOH A . 
H 4 HOH   196 1496 124 HOH   HOH A . 
H 4 HOH   197 1497 183 HOH   HOH A . 
H 4 HOH   198 1498 146 HOH   HOH A . 
H 4 HOH   199 1499 419 HOH   HOH A . 
H 4 HOH   200 1500 195 HOH   HOH A . 
H 4 HOH   201 1501 377 HOH   HOH A . 
H 4 HOH   202 1502 229 HOH   HOH A . 
H 4 HOH   203 1503 201 HOH   HOH A . 
H 4 HOH   204 1504 339 HOH   HOH A . 
H 4 HOH   205 1505 243 HOH   HOH A . 
H 4 HOH   206 1506 324 HOH   HOH A . 
H 4 HOH   207 1507 181 HOH   HOH A . 
H 4 HOH   208 1508 434 HOH   HOH A . 
H 4 HOH   209 1509 379 HOH   HOH A . 
H 4 HOH   210 1510 213 HOH   HOH A . 
H 4 HOH   211 1511 284 HOH   HOH A . 
H 4 HOH   212 1512 80  HOH   HOH A . 
H 4 HOH   213 1513 333 HOH   HOH A . 
H 4 HOH   214 1514 205 HOH   HOH A . 
H 4 HOH   215 1515 431 HOH   HOH A . 
H 4 HOH   216 1516 211 HOH   HOH A . 
H 4 HOH   217 1517 382 HOH   HOH A . 
I 4 HOH   1   1301 406 HOH   HOH B . 
I 4 HOH   2   1302 108 HOH   HOH B . 
I 4 HOH   3   1303 223 HOH   HOH B . 
I 4 HOH   4   1304 127 HOH   HOH B . 
I 4 HOH   5   1305 411 HOH   HOH B . 
I 4 HOH   6   1306 188 HOH   HOH B . 
I 4 HOH   7   1307 93  HOH   HOH B . 
I 4 HOH   8   1308 35  HOH   HOH B . 
I 4 HOH   9   1309 14  HOH   HOH B . 
I 4 HOH   10  1310 426 HOH   HOH B . 
I 4 HOH   11  1311 372 HOH   HOH B . 
I 4 HOH   12  1312 427 HOH   HOH B . 
I 4 HOH   13  1313 302 HOH   HOH B . 
I 4 HOH   14  1314 78  HOH   HOH B . 
I 4 HOH   15  1315 330 HOH   HOH B . 
I 4 HOH   16  1316 155 HOH   HOH B . 
I 4 HOH   17  1317 328 HOH   HOH B . 
I 4 HOH   18  1318 95  HOH   HOH B . 
I 4 HOH   19  1319 173 HOH   HOH B . 
I 4 HOH   20  1320 314 HOH   HOH B . 
I 4 HOH   21  1321 264 HOH   HOH B . 
I 4 HOH   22  1322 23  HOH   HOH B . 
I 4 HOH   23  1323 172 HOH   HOH B . 
I 4 HOH   24  1324 32  HOH   HOH B . 
I 4 HOH   25  1325 307 HOH   HOH B . 
I 4 HOH   26  1326 209 HOH   HOH B . 
I 4 HOH   27  1327 206 HOH   HOH B . 
I 4 HOH   28  1328 24  HOH   HOH B . 
I 4 HOH   29  1329 132 HOH   HOH B . 
I 4 HOH   30  1330 369 HOH   HOH B . 
I 4 HOH   31  1331 325 HOH   HOH B . 
I 4 HOH   32  1332 140 HOH   HOH B . 
I 4 HOH   33  1333 87  HOH   HOH B . 
I 4 HOH   34  1334 185 HOH   HOH B . 
I 4 HOH   35  1335 278 HOH   HOH B . 
I 4 HOH   36  1336 151 HOH   HOH B . 
I 4 HOH   37  1337 46  HOH   HOH B . 
I 4 HOH   38  1338 396 HOH   HOH B . 
I 4 HOH   39  1339 228 HOH   HOH B . 
I 4 HOH   40  1340 258 HOH   HOH B . 
I 4 HOH   41  1341 316 HOH   HOH B . 
I 4 HOH   42  1342 212 HOH   HOH B . 
I 4 HOH   43  1343 129 HOH   HOH B . 
I 4 HOH   44  1344 2   HOH   HOH B . 
I 4 HOH   45  1345 239 HOH   HOH B . 
I 4 HOH   46  1346 332 HOH   HOH B . 
I 4 HOH   47  1347 257 HOH   HOH B . 
I 4 HOH   48  1348 329 HOH   HOH B . 
I 4 HOH   49  1349 359 HOH   HOH B . 
I 4 HOH   50  1350 143 HOH   HOH B . 
I 4 HOH   51  1351 272 HOH   HOH B . 
I 4 HOH   52  1352 19  HOH   HOH B . 
I 4 HOH   53  1353 311 HOH   HOH B . 
I 4 HOH   54  1354 48  HOH   HOH B . 
I 4 HOH   55  1355 200 HOH   HOH B . 
I 4 HOH   56  1356 351 HOH   HOH B . 
I 4 HOH   57  1357 42  HOH   HOH B . 
I 4 HOH   58  1358 340 HOH   HOH B . 
I 4 HOH   59  1359 119 HOH   HOH B . 
I 4 HOH   60  1360 418 HOH   HOH B . 
I 4 HOH   61  1361 373 HOH   HOH B . 
I 4 HOH   62  1362 355 HOH   HOH B . 
I 4 HOH   63  1363 398 HOH   HOH B . 
I 4 HOH   64  1364 415 HOH   HOH B . 
I 4 HOH   65  1365 86  HOH   HOH B . 
I 4 HOH   66  1366 8   HOH   HOH B . 
I 4 HOH   67  1367 101 HOH   HOH B . 
I 4 HOH   68  1368 122 HOH   HOH B . 
I 4 HOH   69  1369 391 HOH   HOH B . 
I 4 HOH   70  1370 365 HOH   HOH B . 
I 4 HOH   71  1371 97  HOH   HOH B . 
I 4 HOH   72  1372 113 HOH   HOH B . 
I 4 HOH   73  1373 51  HOH   HOH B . 
I 4 HOH   74  1374 386 HOH   HOH B . 
I 4 HOH   75  1375 20  HOH   HOH B . 
I 4 HOH   76  1376 167 HOH   HOH B . 
I 4 HOH   77  1377 53  HOH   HOH B . 
I 4 HOH   78  1378 385 HOH   HOH B . 
I 4 HOH   79  1379 4   HOH   HOH B . 
I 4 HOH   80  1380 383 HOH   HOH B . 
I 4 HOH   81  1381 117 HOH   HOH B . 
I 4 HOH   82  1382 432 HOH   HOH B . 
I 4 HOH   83  1383 153 HOH   HOH B . 
I 4 HOH   84  1384 133 HOH   HOH B . 
I 4 HOH   85  1385 100 HOH   HOH B . 
I 4 HOH   86  1386 395 HOH   HOH B . 
I 4 HOH   87  1387 259 HOH   HOH B . 
I 4 HOH   88  1388 7   HOH   HOH B . 
I 4 HOH   89  1389 230 HOH   HOH B . 
I 4 HOH   90  1390 275 HOH   HOH B . 
I 4 HOH   91  1391 135 HOH   HOH B . 
I 4 HOH   92  1392 16  HOH   HOH B . 
I 4 HOH   93  1393 202 HOH   HOH B . 
I 4 HOH   94  1394 25  HOH   HOH B . 
I 4 HOH   95  1395 240 HOH   HOH B . 
I 4 HOH   96  1396 9   HOH   HOH B . 
I 4 HOH   97  1397 310 HOH   HOH B . 
I 4 HOH   98  1398 300 HOH   HOH B . 
I 4 HOH   99  1399 393 HOH   HOH B . 
I 4 HOH   100 1400 238 HOH   HOH B . 
I 4 HOH   101 1401 413 HOH   HOH B . 
I 4 HOH   102 1402 11  HOH   HOH B . 
I 4 HOH   103 1403 66  HOH   HOH B . 
I 4 HOH   104 1404 402 HOH   HOH B . 
I 4 HOH   105 1405 178 HOH   HOH B . 
I 4 HOH   106 1406 62  HOH   HOH B . 
I 4 HOH   107 1407 425 HOH   HOH B . 
I 4 HOH   108 1408 77  HOH   HOH B . 
I 4 HOH   109 1409 309 HOH   HOH B . 
I 4 HOH   110 1410 420 HOH   HOH B . 
I 4 HOH   111 1411 289 HOH   HOH B . 
I 4 HOH   112 1412 186 HOH   HOH B . 
I 4 HOH   113 1413 154 HOH   HOH B . 
I 4 HOH   114 1414 176 HOH   HOH B . 
I 4 HOH   115 1415 12  HOH   HOH B . 
I 4 HOH   116 1416 368 HOH   HOH B . 
I 4 HOH   117 1417 294 HOH   HOH B . 
I 4 HOH   118 1418 250 HOH   HOH B . 
I 4 HOH   119 1419 31  HOH   HOH B . 
I 4 HOH   120 1420 190 HOH   HOH B . 
I 4 HOH   121 1421 254 HOH   HOH B . 
I 4 HOH   122 1422 130 HOH   HOH B . 
I 4 HOH   123 1423 144 HOH   HOH B . 
I 4 HOH   124 1424 221 HOH   HOH B . 
I 4 HOH   125 1425 335 HOH   HOH B . 
I 4 HOH   126 1426 164 HOH   HOH B . 
I 4 HOH   127 1427 245 HOH   HOH B . 
I 4 HOH   128 1428 321 HOH   HOH B . 
I 4 HOH   129 1429 39  HOH   HOH B . 
I 4 HOH   130 1430 218 HOH   HOH B . 
I 4 HOH   131 1431 10  HOH   HOH B . 
I 4 HOH   132 1432 104 HOH   HOH B . 
I 4 HOH   133 1433 131 HOH   HOH B . 
I 4 HOH   134 1434 83  HOH   HOH B . 
I 4 HOH   135 1435 148 HOH   HOH B . 
I 4 HOH   136 1436 277 HOH   HOH B . 
I 4 HOH   137 1437 249 HOH   HOH B . 
I 4 HOH   138 1438 99  HOH   HOH B . 
I 4 HOH   139 1439 114 HOH   HOH B . 
I 4 HOH   140 1440 265 HOH   HOH B . 
I 4 HOH   141 1441 353 HOH   HOH B . 
I 4 HOH   142 1442 358 HOH   HOH B . 
I 4 HOH   143 1443 437 HOH   HOH B . 
I 4 HOH   144 1444 58  HOH   HOH B . 
I 4 HOH   145 1445 299 HOH   HOH B . 
I 4 HOH   146 1446 296 HOH   HOH B . 
I 4 HOH   147 1447 208 HOH   HOH B . 
I 4 HOH   148 1448 187 HOH   HOH B . 
I 4 HOH   149 1449 256 HOH   HOH B . 
I 4 HOH   150 1450 304 HOH   HOH B . 
I 4 HOH   151 1451 163 HOH   HOH B . 
I 4 HOH   152 1452 204 HOH   HOH B . 
I 4 HOH   153 1453 196 HOH   HOH B . 
I 4 HOH   154 1454 317 HOH   HOH B . 
I 4 HOH   155 1455 89  HOH   HOH B . 
I 4 HOH   156 1456 387 HOH   HOH B . 
I 4 HOH   157 1457 438 HOH   HOH B . 
I 4 HOH   158 1458 290 HOH   HOH B . 
I 4 HOH   159 1459 128 HOH   HOH B . 
I 4 HOH   160 1460 149 HOH   HOH B . 
I 4 HOH   161 1461 349 HOH   HOH B . 
I 4 HOH   162 1462 384 HOH   HOH B . 
I 4 HOH   163 1463 371 HOH   HOH B . 
I 4 HOH   164 1464 280 HOH   HOH B . 
I 4 HOH   165 1465 68  HOH   HOH B . 
I 4 HOH   166 1466 29  HOH   HOH B . 
I 4 HOH   167 1467 158 HOH   HOH B . 
I 4 HOH   168 1468 38  HOH   HOH B . 
I 4 HOH   169 1469 197 HOH   HOH B . 
I 4 HOH   170 1470 394 HOH   HOH B . 
I 4 HOH   171 1471 352 HOH   HOH B . 
I 4 HOH   172 1472 281 HOH   HOH B . 
I 4 HOH   173 1473 234 HOH   HOH B . 
I 4 HOH   174 1474 232 HOH   HOH B . 
I 4 HOH   175 1475 354 HOH   HOH B . 
I 4 HOH   176 1476 103 HOH   HOH B . 
I 4 HOH   177 1477 116 HOH   HOH B . 
I 4 HOH   178 1478 226 HOH   HOH B . 
I 4 HOH   179 1479 237 HOH   HOH B . 
I 4 HOH   180 1480 361 HOH   HOH B . 
I 4 HOH   181 1481 270 HOH   HOH B . 
I 4 HOH   182 1482 76  HOH   HOH B . 
I 4 HOH   183 1483 409 HOH   HOH B . 
I 4 HOH   184 1484 424 HOH   HOH B . 
I 4 HOH   185 1485 65  HOH   HOH B . 
I 4 HOH   186 1486 157 HOH   HOH B . 
I 4 HOH   187 1487 74  HOH   HOH B . 
I 4 HOH   188 1488 338 HOH   HOH B . 
I 4 HOH   189 1489 416 HOH   HOH B . 
I 4 HOH   190 1490 350 HOH   HOH B . 
I 4 HOH   191 1491 57  HOH   HOH B . 
I 4 HOH   192 1492 241 HOH   HOH B . 
I 4 HOH   193 1493 305 HOH   HOH B . 
I 4 HOH   194 1494 126 HOH   HOH B . 
I 4 HOH   195 1495 98  HOH   HOH B . 
I 4 HOH   196 1496 179 HOH   HOH B . 
I 4 HOH   197 1497 403 HOH   HOH B . 
I 4 HOH   198 1498 301 HOH   HOH B . 
I 4 HOH   199 1499 17  HOH   HOH B . 
I 4 HOH   200 1500 363 HOH   HOH B . 
I 4 HOH   201 1501 225 HOH   HOH B . 
I 4 HOH   202 1502 378 HOH   HOH B . 
I 4 HOH   203 1503 388 HOH   HOH B . 
I 4 HOH   204 1504 61  HOH   HOH B . 
I 4 HOH   205 1505 380 HOH   HOH B . 
I 4 HOH   206 1506 344 HOH   HOH B . 
I 4 HOH   207 1507 376 HOH   HOH B . 
I 4 HOH   208 1508 203 HOH   HOH B . 
I 4 HOH   209 1509 404 HOH   HOH B . 
I 4 HOH   210 1510 331 HOH   HOH B . 
I 4 HOH   211 1511 268 HOH   HOH B . 
I 4 HOH   212 1512 336 HOH   HOH B . 
I 4 HOH   213 1513 216 HOH   HOH B . 
I 4 HOH   214 1514 326 HOH   HOH B . 
I 4 HOH   215 1515 405 HOH   HOH B . 
I 4 HOH   216 1516 381 HOH   HOH B . 
I 4 HOH   217 1517 160 HOH   HOH B . 
I 4 HOH   218 1518 215 HOH   HOH B . 
I 4 HOH   219 1519 94  HOH   HOH B . 
I 4 HOH   220 1520 428 HOH   HOH B . 
I 4 HOH   221 1521 303 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 0 A LYS 860  ? CD  ? A LYS 8   CD  
2   1 Y 0 A LYS 860  ? CE  ? A LYS 8   CE  
3   1 Y 0 A LYS 860  ? NZ  ? A LYS 8   NZ  
4   1 Y 0 A GLU 864  ? CG  ? A GLU 12  CG  
5   1 Y 0 A GLU 864  ? CD  ? A GLU 12  CD  
6   1 Y 0 A GLU 864  ? OE1 ? A GLU 12  OE1 
7   1 Y 0 A GLU 864  ? OE2 ? A GLU 12  OE2 
8   1 Y 0 A LYS 872  ? NZ  ? A LYS 20  NZ  
9   1 Y 0 A GLU 883  ? CD  ? A GLU 31  CD  
10  1 Y 0 A GLU 883  ? OE1 ? A GLU 31  OE1 
11  1 Y 0 A GLU 883  ? OE2 ? A GLU 31  OE2 
12  1 Y 0 A HIS 885  ? CG  ? A HIS 33  CG  
13  1 Y 0 A HIS 885  ? ND1 ? A HIS 33  ND1 
14  1 Y 0 A HIS 885  ? CD2 ? A HIS 33  CD2 
15  1 Y 0 A HIS 885  ? CE1 ? A HIS 33  CE1 
16  1 Y 0 A HIS 885  ? NE2 ? A HIS 33  NE2 
17  1 Y 0 A PHE 886  ? CG  ? A PHE 34  CG  
18  1 Y 0 A PHE 886  ? CD1 ? A PHE 34  CD1 
19  1 Y 0 A PHE 886  ? CD2 ? A PHE 34  CD2 
20  1 Y 0 A PHE 886  ? CE1 ? A PHE 34  CE1 
21  1 Y 0 A PHE 886  ? CE2 ? A PHE 34  CE2 
22  1 Y 0 A PHE 886  ? CZ  ? A PHE 34  CZ  
23  1 Y 0 A LYS 888  ? CD  ? A LYS 36  CD  
24  1 Y 0 A LYS 888  ? CE  ? A LYS 36  CE  
25  1 Y 0 A LYS 888  ? NZ  ? A LYS 36  NZ  
26  1 Y 0 A LYS 911  ? CG  ? A LYS 59  CG  
27  1 Y 0 A LYS 911  ? CD  ? A LYS 59  CD  
28  1 Y 0 A LYS 911  ? CE  ? A LYS 59  CE  
29  1 Y 0 A LYS 911  ? NZ  ? A LYS 59  NZ  
30  1 Y 0 A ASN 917  ? CG  ? A ASN 65  CG  
31  1 Y 0 A ASN 917  ? OD1 ? A ASN 65  OD1 
32  1 Y 0 A ASN 917  ? ND2 ? A ASN 65  ND2 
33  1 Y 0 A HIS 918  ? CG  ? A HIS 66  CG  
34  1 Y 0 A HIS 918  ? ND1 ? A HIS 66  ND1 
35  1 Y 0 A HIS 918  ? CD2 ? A HIS 66  CD2 
36  1 Y 0 A HIS 918  ? CE1 ? A HIS 66  CE1 
37  1 Y 0 A HIS 918  ? NE2 ? A HIS 66  NE2 
38  1 Y 0 A ILE 919  ? CD1 ? A ILE 67  CD1 
39  1 Y 0 A LYS 923  ? NZ  ? A LYS 71  NZ  
40  1 Y 0 A LYS 924  ? NZ  ? A LYS 72  NZ  
41  1 Y 0 A ASN 950  ? CG  ? A ASN 98  CG  
42  1 Y 0 A ASN 950  ? OD1 ? A ASN 98  OD1 
43  1 Y 0 A ASN 950  ? ND2 ? A ASN 98  ND2 
44  1 Y 0 A GLU 966  ? CD  B A GLU 114 CD  
45  1 Y 0 A GLU 966  ? OE1 B A GLU 114 OE1 
46  1 Y 0 A GLU 966  ? OE2 B A GLU 114 OE2 
47  1 Y 0 A ARG 997  ? CZ  ? A ARG 145 CZ  
48  1 Y 0 A ARG 997  ? NH1 ? A ARG 145 NH1 
49  1 Y 0 A ARG 997  ? NH2 ? A ARG 145 NH2 
50  1 Y 0 A LYS 1032 ? CE  ? A LYS 180 CE  
51  1 Y 0 A LYS 1032 ? NZ  ? A LYS 180 NZ  
52  1 Y 0 A GLU 1033 ? CD  ? A GLU 181 CD  
53  1 Y 0 A GLU 1033 ? OE1 ? A GLU 181 OE1 
54  1 Y 0 A GLU 1033 ? OE2 ? A GLU 181 OE2 
55  1 Y 0 A VAL 1037 ? CG1 ? A VAL 185 CG1 
56  1 Y 0 A VAL 1037 ? CG2 ? A VAL 185 CG2 
57  1 Y 0 A LYS 1038 ? CG  ? A LYS 186 CG  
58  1 Y 0 A LYS 1038 ? CD  ? A LYS 186 CD  
59  1 Y 0 A LYS 1038 ? CE  ? A LYS 186 CE  
60  1 Y 0 A LYS 1038 ? NZ  ? A LYS 186 NZ  
61  1 Y 0 A ARG 1041 ? CG  ? A ARG 189 CG  
62  1 Y 0 A ARG 1041 ? CD  ? A ARG 189 CD  
63  1 Y 0 A ARG 1041 ? NE  ? A ARG 189 NE  
64  1 Y 0 A ARG 1041 ? CZ  ? A ARG 189 CZ  
65  1 Y 0 A ARG 1041 ? NH1 ? A ARG 189 NH1 
66  1 Y 0 A ARG 1041 ? NH2 ? A ARG 189 NH2 
67  1 Y 0 A GLN 1055 ? OE1 ? A GLN 203 OE1 
68  1 Y 0 A GLN 1055 ? NE2 ? A GLN 203 NE2 
69  1 Y 0 A LYS 1090 ? CD  ? A LYS 238 CD  
70  1 Y 0 A LYS 1090 ? CE  ? A LYS 238 CE  
71  1 Y 0 A LYS 1090 ? NZ  ? A LYS 238 NZ  
72  1 Y 0 A ILE 1092 ? CD1 ? A ILE 240 CD1 
73  1 Y 0 A GLN 1098 ? CG  ? A GLN 246 CG  
74  1 Y 0 A GLN 1098 ? CD  ? A GLN 246 CD  
75  1 Y 0 A GLN 1098 ? OE1 ? A GLN 246 OE1 
76  1 Y 0 A GLN 1098 ? NE2 ? A GLN 246 NE2 
77  1 Y 0 A LYS 1109 ? CD  ? A LYS 257 CD  
78  1 Y 0 A LYS 1109 ? CE  ? A LYS 257 CE  
79  1 Y 0 A LYS 1109 ? NZ  ? A LYS 257 NZ  
80  1 Y 0 A LYS 1112 ? CE  ? A LYS 260 CE  
81  1 Y 0 A LYS 1112 ? NZ  ? A LYS 260 NZ  
82  1 Y 0 A GLN 1135 ? CG  ? A GLN 283 CG  
83  1 Y 0 A GLN 1135 ? CD  ? A GLN 283 CD  
84  1 Y 0 A GLN 1135 ? OE1 ? A GLN 283 OE1 
85  1 Y 0 A GLN 1135 ? NE2 ? A GLN 283 NE2 
86  1 Y 0 A GLU 1147 ? CD  ? A GLU 295 CD  
87  1 Y 0 A GLU 1147 ? OE1 ? A GLU 295 OE1 
88  1 Y 0 A GLU 1147 ? OE2 ? A GLU 295 OE2 
89  1 Y 0 B VAL 865  ? CG1 ? B VAL 13  CG1 
90  1 Y 0 B VAL 865  ? CG2 ? B VAL 13  CG2 
91  1 Y 0 B HIS 885  ? CG  ? B HIS 33  CG  
92  1 Y 0 B HIS 885  ? ND1 ? B HIS 33  ND1 
93  1 Y 0 B HIS 885  ? CD2 ? B HIS 33  CD2 
94  1 Y 0 B HIS 885  ? CE1 ? B HIS 33  CE1 
95  1 Y 0 B HIS 885  ? NE2 ? B HIS 33  NE2 
96  1 Y 0 B PHE 886  ? CG  ? B PHE 34  CG  
97  1 Y 0 B PHE 886  ? CD1 ? B PHE 34  CD1 
98  1 Y 0 B PHE 886  ? CD2 ? B PHE 34  CD2 
99  1 Y 0 B PHE 886  ? CE1 ? B PHE 34  CE1 
100 1 Y 0 B PHE 886  ? CE2 ? B PHE 34  CE2 
101 1 Y 0 B PHE 886  ? CZ  ? B PHE 34  CZ  
102 1 Y 0 B LYS 939  ? NZ  ? B LYS 87  NZ  
103 1 Y 0 B ASN 950  ? CG  ? B ASN 98  CG  
104 1 Y 0 B ASN 950  ? OD1 ? B ASN 98  OD1 
105 1 Y 0 B ASN 950  ? ND2 ? B ASN 98  ND2 
106 1 Y 0 B LYS 965  ? NZ  B B LYS 113 NZ  
107 1 Y 0 B THR 1030 ? OG1 ? B THR 178 OG1 
108 1 Y 0 B THR 1030 ? CG2 ? B THR 178 CG2 
109 1 Y 0 B ASP 1031 ? CG  ? B ASP 179 CG  
110 1 Y 0 B ASP 1031 ? OD1 ? B ASP 179 OD1 
111 1 Y 0 B ASP 1031 ? OD2 ? B ASP 179 OD2 
112 1 Y 0 B LYS 1032 ? CE  ? B LYS 180 CE  
113 1 Y 0 B LYS 1032 ? NZ  ? B LYS 180 NZ  
114 1 Y 0 B GLU 1033 ? CD  ? B GLU 181 CD  
115 1 Y 0 B GLU 1033 ? OE1 ? B GLU 181 OE1 
116 1 Y 0 B GLU 1033 ? OE2 ? B GLU 181 OE2 
117 1 Y 0 B ASP 1039 ? OD1 ? B ASP 187 OD1 
118 1 Y 0 B ASP 1039 ? OD2 ? B ASP 187 OD2 
119 1 Y 0 B ARG 1041 ? CD  ? B ARG 189 CD  
120 1 Y 0 B ARG 1041 ? NE  ? B ARG 189 NE  
121 1 Y 0 B ARG 1041 ? CZ  ? B ARG 189 CZ  
122 1 Y 0 B ARG 1041 ? NH1 ? B ARG 189 NH1 
123 1 Y 0 B ARG 1041 ? NH2 ? B ARG 189 NH2 
124 1 Y 0 B LYS 1057 ? CD  ? B LYS 205 CD  
125 1 Y 0 B LYS 1057 ? CE  ? B LYS 205 CE  
126 1 Y 0 B LYS 1057 ? NZ  ? B LYS 205 NZ  
127 1 Y 0 B LYS 1090 ? CG  ? B LYS 238 CG  
128 1 Y 0 B LYS 1090 ? CD  ? B LYS 238 CD  
129 1 Y 0 B LYS 1090 ? CE  ? B LYS 238 CE  
130 1 Y 0 B LYS 1090 ? NZ  ? B LYS 238 NZ  
131 1 Y 0 B THR 1095 ? OG1 ? B THR 243 OG1 
132 1 Y 0 B THR 1095 ? CG2 ? B THR 243 CG2 
133 1 Y 0 B GLN 1098 ? CG  ? B GLN 246 CG  
134 1 Y 0 B GLN 1098 ? CD  ? B GLN 246 CD  
135 1 Y 0 B GLN 1098 ? OE1 ? B GLN 246 OE1 
136 1 Y 0 B GLN 1098 ? NE2 ? B GLN 246 NE2 
137 1 Y 0 B ARG 1103 ? CZ  ? B ARG 251 CZ  
138 1 Y 0 B ARG 1103 ? NH1 ? B ARG 251 NH1 
139 1 Y 0 B ARG 1103 ? NH2 ? B ARG 251 NH2 
140 1 Y 0 B LEU 1108 ? CD1 ? B LEU 256 CD1 
141 1 Y 0 B LEU 1108 ? CD2 ? B LEU 256 CD2 
142 1 Y 0 B LYS 1109 ? CG  ? B LYS 257 CG  
143 1 Y 0 B LYS 1109 ? CD  ? B LYS 257 CD  
144 1 Y 0 B LYS 1109 ? CE  ? B LYS 257 CE  
145 1 Y 0 B LYS 1109 ? NZ  ? B LYS 257 NZ  
146 1 Y 0 B LYS 1112 ? CE  ? B LYS 260 CE  
147 1 Y 0 B LYS 1112 ? NZ  ? B LYS 260 NZ  
148 1 Y 0 B LYS 1130 ? NZ  ? B LYS 278 NZ  
149 1 Y 0 B GLN 1135 ? CG  ? B GLN 283 CG  
150 1 Y 0 B GLN 1135 ? CD  ? B GLN 283 CD  
151 1 Y 0 B GLN 1135 ? OE1 ? B GLN 283 OE1 
152 1 Y 0 B GLN 1135 ? NE2 ? B GLN 283 NE2 
153 1 Y 0 B LYS 1154 ? CD  ? B LYS 302 CD  
154 1 Y 0 B LYS 1154 ? CE  ? B LYS 302 CE  
155 1 Y 0 B LYS 1154 ? NZ  ? B LYS 302 NZ  
# 
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 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? . 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? . 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? . 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S85 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.038 
_cell.length_a_esd                 ? 
_cell.length_b                     174.030 
_cell.length_b_esd                 ? 
_cell.length_c                     44.893 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8S85 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8S85 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.00 
_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              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MES pH 5-6 and 25-35% PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2011-01-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979500 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979500 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S85 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               87.01 
_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                                     60553 
_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                           96.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.059 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.05 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.82 
_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                             6840 
_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                               0.657 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_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                               0.547 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.93 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.31 
_refine.aniso_B[2][2]                            -0.56 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.54 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.589 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_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                                 8S85 
_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                            1.75 
_refine.ls_d_res_low                             87.01 
_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                     60553 
_refine.ls_number_reflns_R_free                  2941 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.35 
_refine.ls_percent_reflns_R_free                 4.6 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20988 
_refine.ls_R_factor_R_free                       0.24960 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20791 
_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                    'BABINET MODEL WITH 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                       0.133 
_refine.pdbx_overall_ESU_R_Free                  0.130 
_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                             6.095 
_refine.overall_SU_ML                            0.109 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        87.01 
_refine_hist.number_atoms_solvent             438 
_refine_hist.number_atoms_total               5163 
_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        4682 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_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' ? 0.011  0.022  4764 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  4292 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.330  1.988  6461 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.285  3.000  9983 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.083  5.000  590  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 38.925 24.307 202  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.290 15.000 831  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.534 15.000 23   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  701  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  5288 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  945  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? 0.186  0.200  913  ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.167  0.200  4109 ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? 0.165  0.200  2302 ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? 0.069  0.200  2470 ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? 0.122  0.200  301  ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? 0.017  0.200  1    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? 0.245  0.200  8    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? 0.207  0.200  65   ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? 0.133  0.200  31   ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? 0.036  0.200  2    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.929  2.000  2927 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.484  2.000  1184 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.847  3.000  4726 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.035  4.000  1898 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.581  6.000  1735 ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? 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                       1.751 
_refine_ls_shell.d_res_low                        1.796 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             191 
_refine_ls_shell.number_reflns_R_work             4327 
_refine_ls_shell.percent_reflns_obs               92.07 
_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                  0.296 
_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   20 
_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                  0.365 
# 
_struct.entry_id                     8S85 
_struct.title                        'Crystal structure of JAK1 JH1 domain in complex with an inhibitor' 
_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        8S85 
_struct_keywords.text            'Kinase, JAK1, Inhibitor, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 2 ? 
H N N 4 ? 
I N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    JAK1_HUMAN 
_struct_ref.pdbx_db_accession          P23458 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLY
HENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES
EHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIG
PTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK
;
_struct_ref.pdbx_align_begin           854 
# 
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 8S85 A 2 ? 302 ? P23458 854 ? 1154 ? 854 1154 
2 1 8S85 B 2 ? 302 ? P23458 854 ? 1154 ? 854 1154 
# 
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 8S85 GLY A 1 ? UNP P23458 ? ? 'expression tag' 853 1 
2 8S85 GLY B 1 ? UNP P23458 ? ? 'expression tag' 853 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,F,H 
2 1 B,G,I       
# 
_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_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 19  ? ARG A 21  ? GLU A 871  ARG A 873  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 66  ? ASN A 79  ? HIS A 918  ASN A 931  1 ? 14 
HELX_P HELX_P3  AA3 SER A 111 ? ASN A 119 ? SER A 963  ASN A 971  1 ? 9  
HELX_P HELX_P4  AA4 LYS A 120 ? ILE A 123 ? LYS A 972  ILE A 975  5 ? 4  
HELX_P HELX_P5  AA5 ASN A 124 ? ARG A 145 ? ASN A 976  ARG A 997  1 ? 22 
HELX_P HELX_P6  AA6 ALA A 153 ? ARG A 155 ? ALA A 1005 ARG A 1007 5 ? 3  
HELX_P HELX_P7  AA7 PRO A 192 ? TYR A 196 ? PRO A 1044 TYR A 1048 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 197 ? SER A 204 ? ALA A 1049 SER A 1056 1 ? 8  
HELX_P HELX_P9  AA9 TYR A 207 ? THR A 224 ? TYR A 1059 THR A 1076 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 227 ? SER A 230 ? ASP A 1079 SER A 1082 5 ? 4  
HELX_P HELX_P11 AB2 SER A 231 ? GLY A 241 ? SER A 1083 GLY A 1093 1 ? 11 
HELX_P HELX_P12 AB3 HIS A 244 ? GLN A 246 ? HIS A 1096 GLN A 1098 5 ? 3  
HELX_P HELX_P13 AB4 MET A 247 ? GLU A 258 ? MET A 1099 GLU A 1110 1 ? 12 
HELX_P HELX_P14 AB5 PRO A 269 ? CYS A 279 ? PRO A 1121 CYS A 1131 1 ? 11 
HELX_P HELX_P15 AB6 GLN A 283 ? ARG A 287 ? GLN A 1135 ARG A 1139 5 ? 5  
HELX_P HELX_P16 AB7 SER A 289 ? LYS A 302 ? SER A 1141 LYS A 1154 1 ? 14 
HELX_P HELX_P17 AB8 GLU B 19  ? ARG B 21  ? GLU B 871  ARG B 873  5 ? 3  
HELX_P HELX_P18 AB9 HIS B 66  ? ASN B 79  ? HIS B 918  ASN B 931  1 ? 14 
HELX_P HELX_P19 AC1 SER B 111 ? LYS B 120 ? SER B 963  LYS B 972  1 ? 10 
HELX_P HELX_P20 AC2 ASN B 124 ? ARG B 145 ? ASN B 976  ARG B 997  1 ? 22 
HELX_P HELX_P21 AC3 ALA B 153 ? ARG B 155 ? ALA B 1005 ARG B 1007 5 ? 3  
HELX_P HELX_P22 AC4 PRO B 192 ? TYR B 196 ? PRO B 1044 TYR B 1048 5 ? 5  
HELX_P HELX_P23 AC5 ALA B 197 ? SER B 204 ? ALA B 1049 SER B 1056 1 ? 8  
HELX_P HELX_P24 AC6 ILE B 208 ? THR B 224 ? ILE B 1060 THR B 1076 1 ? 17 
HELX_P HELX_P25 AC7 ASP B 227 ? SER B 230 ? ASP B 1079 SER B 1082 5 ? 4  
HELX_P HELX_P26 AC8 SER B 231 ? GLY B 241 ? SER B 1083 GLY B 1093 1 ? 11 
HELX_P HELX_P27 AC9 HIS B 244 ? GLN B 246 ? HIS B 1096 GLN B 1098 5 ? 3  
HELX_P HELX_P28 AD1 MET B 247 ? GLU B 258 ? MET B 1099 GLU B 1110 1 ? 12 
HELX_P HELX_P29 AD2 PRO B 269 ? CYS B 279 ? PRO B 1121 CYS B 1131 1 ? 11 
HELX_P HELX_P30 AD3 GLN B 283 ? ARG B 287 ? GLN B 1135 ARG B 1139 5 ? 5  
HELX_P HELX_P31 AD4 SER B 289 ? LEU B 301 ? SER B 1141 LEU B 1153 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? A GLU 181 C   ? ? ? 1_555 A PTR 182 N  ? ? A GLU 1033 A PTR 1034 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale2  covale both ? A PTR 182 C   ? ? ? 1_555 A PTR 183 N  ? ? A PTR 1034 A PTR 1035 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale3  covale both ? A PTR 183 C   ? ? ? 1_555 A THR 184 N  ? ? A PTR 1035 A THR 1036 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale4  covale both ? B GLU 181 C   ? ? ? 1_555 B PTR 182 N  ? ? B GLU 1033 B PTR 1034 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale5  covale both ? B PTR 182 C   ? ? ? 1_555 B PTR 183 N  ? ? B PTR 1034 B PTR 1035 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale6  covale both ? B PTR 183 C   ? ? ? 1_555 B THR 184 N  ? ? B PTR 1035 B THR 1036 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
metalc1  metalc ?    ? A GLU 6   OE2 ? ? ? 1_555 F NA  .   NA ? ? A GLU 858  A NA  1204 1_455 ? ? ? ? ? ? ? 2.403 ? ? 
metalc2  metalc ?    ? A GLU 75  OE2 ? ? ? 1_555 D NA  .   NA ? ? A GLU 927  A NA  1202 1_555 ? ? ? ? ? ? ? 2.424 ? ? 
metalc3  metalc ?    ? A LEU 80  O   ? ? ? 1_555 E NA  .   NA ? ? A LEU 932  A NA  1203 1_555 ? ? ? ? ? ? ? 2.393 ? ? 
metalc4  metalc ?    ? A ASN 267 OD1 ? ? ? 1_555 D NA  .   NA ? ? A ASN 1119 A NA  1202 1_655 ? ? ? ? ? ? ? 3.029 ? ? 
metalc5  metalc ?    ? D NA  .   NA  ? ? ? 1_555 H HOH .   O  ? ? A NA  1202 A HOH 1404 1_455 ? ? ? ? ? ? ? 2.624 ? ? 
metalc6  metalc ?    ? D NA  .   NA  ? ? ? 1_555 H HOH .   O  ? ? A NA  1202 A HOH 1496 1_455 ? ? ? ? ? ? ? 2.734 ? ? 
metalc7  metalc ?    ? E NA  .   NA  ? ? ? 1_555 H HOH .   O  ? ? A NA  1203 A HOH 1357 1_555 ? ? ? ? ? ? ? 3.143 ? ? 
metalc8  metalc ?    ? E NA  .   NA  ? ? ? 1_555 H HOH .   O  ? ? A NA  1203 A HOH 1459 1_555 ? ? ? ? ? ? ? 2.760 ? ? 
metalc9  metalc ?    ? F NA  .   NA  ? ? ? 1_555 H HOH .   O  ? ? A NA  1204 A HOH 1310 1_655 ? ? ? ? ? ? ? 2.697 ? ? 
metalc10 metalc ?    ? F NA  .   NA  ? ? ? 1_555 H HOH .   O  ? ? A NA  1204 A HOH 1469 1_655 ? ? ? ? ? ? ? 2.360 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 6   ? A GLU 858  ? 1_555 NA ? F NA . ? A NA 1204 ? 1_455 O   ? H HOH .   ? A HOH 1310 ? 1_655 113.5 ? 
2  OE2 ? A GLU 6   ? A GLU 858  ? 1_555 NA ? F NA . ? A NA 1204 ? 1_455 O   ? H HOH .   ? A HOH 1469 ? 1_655 110.4 ? 
3  O   ? H HOH .   ? A HOH 1310 ? 1_655 NA ? F NA . ? A NA 1204 ? 1_455 O   ? H HOH .   ? A HOH 1469 ? 1_655 5.4   ? 
4  OE2 ? A GLU 75  ? A GLU 927  ? 1_555 NA ? D NA . ? A NA 1202 ? 1_555 OD1 ? A ASN 267 ? A ASN 1119 ? 1_555 76.6  ? 
5  OE2 ? A GLU 75  ? A GLU 927  ? 1_555 NA ? D NA . ? A NA 1202 ? 1_555 O   ? H HOH .   ? A HOH 1404 ? 1_455 116.9 ? 
6  OD1 ? A ASN 267 ? A ASN 1119 ? 1_555 NA ? D NA . ? A NA 1202 ? 1_555 O   ? H HOH .   ? A HOH 1404 ? 1_455 124.3 ? 
7  OE2 ? A GLU 75  ? A GLU 927  ? 1_555 NA ? D NA . ? A NA 1202 ? 1_555 O   ? H HOH .   ? A HOH 1496 ? 1_455 104.9 ? 
8  OD1 ? A ASN 267 ? A ASN 1119 ? 1_555 NA ? D NA . ? A NA 1202 ? 1_555 O   ? H HOH .   ? A HOH 1496 ? 1_455 100.5 ? 
9  O   ? H HOH .   ? A HOH 1404 ? 1_455 NA ? D NA . ? A NA 1202 ? 1_555 O   ? H HOH .   ? A HOH 1496 ? 1_455 123.4 ? 
10 O   ? A LEU 80  ? A LEU 932  ? 1_555 NA ? E NA . ? A NA 1203 ? 1_555 O   ? H HOH .   ? A HOH 1357 ? 1_555 58.0  ? 
11 O   ? A LEU 80  ? A LEU 932  ? 1_555 NA ? E NA . ? A NA 1203 ? 1_555 O   ? H HOH .   ? A HOH 1459 ? 1_555 133.7 ? 
12 O   ? H HOH .   ? A HOH 1357 ? 1_555 NA ? E NA . ? A NA 1203 ? 1_555 O   ? H HOH .   ? A HOH 1459 ? 1_555 93.2  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 PTR A 182 ? . . . . PTR A 1034 ? 1_555 . . . . . . . TYR 1 PTR Phosphorylation 'Named protein modification' 
2 PTR A 183 ? . . . . PTR A 1035 ? 1_555 . . . . . . . TYR 1 PTR Phosphorylation 'Named protein modification' 
3 PTR B 182 ? . . . . PTR B 1034 ? 1_555 . . . . . . . TYR 1 PTR Phosphorylation 'Named protein modification' 
4 PTR B 183 ? . . . . PTR B 1035 ? 1_555 . . . . . . . TYR 1 PTR Phosphorylation 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 23  ? GLY A 32  ? LEU A 875  GLY A 884  
AA1 2 GLY A 35  ? TYR A 42  ? GLY A 887  TYR A 894  
AA1 3 GLU A 51  ? LEU A 58  ? GLU A 903  LEU A 910  
AA1 4 LYS A 101 ? GLU A 105 ? LYS A 953  GLU A 957  
AA1 5 TYR A 88  ? CYS A 92  ? TYR A 940  CYS A 944  
AA2 1 TYR A 147 ? VAL A 148 ? TYR A 999  VAL A 1000 
AA2 2 LYS A 174 ? ALA A 175 ? LYS A 1026 ALA A 1027 
AA3 1 VAL A 157 ? SER A 161 ? VAL A 1009 SER A 1013 
AA3 2 GLN A 164 ? ILE A 167 ? GLN A 1016 ILE A 1019 
AA4 1 PTR A 183 ? THR A 184 ? PTR A 1035 THR A 1036 
AA4 2 LYS A 205 ? PHE A 206 ? LYS A 1057 PHE A 1058 
AA5 1 LEU B 23  ? GLY B 32  ? LEU B 875  GLY B 884  
AA5 2 GLY B 35  ? TYR B 42  ? GLY B 887  TYR B 894  
AA5 3 GLU B 51  ? LEU B 58  ? GLU B 903  LEU B 910  
AA5 4 LYS B 101 ? GLU B 105 ? LYS B 953  GLU B 957  
AA5 5 TYR B 88  ? CYS B 92  ? TYR B 940  CYS B 944  
AA6 1 TYR B 147 ? VAL B 148 ? TYR B 999  VAL B 1000 
AA6 2 LYS B 174 ? ALA B 175 ? LYS B 1026 ALA B 1027 
AA7 1 VAL B 157 ? SER B 161 ? VAL B 1009 SER B 1013 
AA7 2 GLN B 164 ? ILE B 167 ? GLN B 1016 ILE B 1019 
AA8 1 PTR B 182 ? THR B 184 ? PTR B 1034 THR B 1036 
AA8 2 LYS B 205 ? TYR B 207 ? LYS B 1057 TYR B 1059 
# 
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 GLY A 30  ? N GLY A 882  O VAL A 37  ? O VAL A 889  
AA1 2 3 N GLU A 38  ? N GLU A 890  O VAL A 55  ? O VAL A 907  
AA1 3 4 N ALA A 54  ? N ALA A 906  O MET A 104 ? O MET A 956  
AA1 4 5 O ILE A 103 ? O ILE A 955  N GLY A 90  ? N GLY A 942  
AA2 1 2 N VAL A 148 ? N VAL A 1000 O LYS A 174 ? O LYS A 1026 
AA3 1 2 N LEU A 158 ? N LEU A 1010 O LYS A 166 ? O LYS A 1018 
AA4 1 2 N PTR A 183 ? N PTR A 1035 O PHE A 206 ? O PHE A 1058 
AA5 1 2 N ARG B 27  ? N ARG B 879  O LEU B 39  ? O LEU B 891  
AA5 2 3 N TYR B 42  ? N TYR B 894  O GLU B 51  ? O GLU B 903  
AA5 3 4 N ALA B 54  ? N ALA B 906  O MET B 104 ? O MET B 956  
AA5 4 5 O ILE B 103 ? O ILE B 955  N GLY B 90  ? N GLY B 942  
AA6 1 2 N VAL B 148 ? N VAL B 1000 O LYS B 174 ? O LYS B 1026 
AA7 1 2 N LEU B 158 ? N LEU B 1010 O LYS B 166 ? O LYS B 1018 
AA8 1 2 N PTR B 183 ? N PTR B 1035 O PHE B 206 ? O PHE B 1058 
# 
_pdbx_entry_details.entry_id                   8S85 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_1              1037 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_2              1037 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_3              1037 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                121.72 
_pdbx_validate_rmsd_angle.angle_target_value         110.90 
_pdbx_validate_rmsd_angle.angle_deviation            10.82 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 885  ? ? 59.91   75.12  
2 1 PHE A 886  ? ? 69.99   -19.96 
3 1 ASP A 1003 ? ? -149.95 35.44  
4 1 ILE B 878  ? ? -101.12 -62.14 
5 1 ASP B 1003 ? ? -152.06 35.58  
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A PTR 182 A PTR 1034 ? TYR 'modified residue' 
2 A PTR 183 A PTR 1035 ? TYR 'modified residue' 
3 B PTR 182 B PTR 1034 ? TYR 'modified residue' 
4 B PTR 183 B PTR 1035 ? TYR 'modified residue' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 0.0 -3.190 59.390 -2.509 0.0997 ? -0.0166 ? -0.0077 ? 0.0815 ? -0.0475 ? 0.1415 ? 2.8108 ? -0.5511 
? 1.4843  ? 0.7998 ? -1.3104 ? 5.0425 ? 0.1169  ? 0.1604  ? -0.4708 ? -0.2125 ? 0.0665  ? 0.1539  ? 0.2698  ? -0.0462 ? -0.1833 
2 'X-RAY DIFFRACTION' ? refined 0.0 12.778 51.395 16.365 0.1031 ? -0.0056 ? 0.0003  ? 0.0614 ? 0.0428  ? 0.1842 ? 5.0861 ? -0.0280 
? 1.0750  ? 1.7646 ? -0.3351 ? 1.9580 ? 0.1034  ? -0.2643 ? -0.9130 ? 0.1545  ? 0.0711  ? 0.0318  ? 0.1421  ? -0.0603 ? -0.1746 
3 'X-RAY DIFFRACTION' ? refined 0.0 24.743 2.945  -2.749 0.1152 ? -0.0219 ? 0.0317  ? 0.0654 ? -0.0016 ? 0.0460 ? 4.3848 ? 0.4968  
? -0.7105 ? 1.7570 ? 0.3897  ? 5.3949 ? -0.0902 ? 0.2276  ? 0.1437  ? -0.3544 ? 0.0935  ? -0.2291 ? -0.1692 ? 0.1074  ? -0.0034 
4 'X-RAY DIFFRACTION' ? refined 0.0 8.575  10.139 16.123 0.1310 ? -0.0454 ? 0.0723  ? 0.1436 ? -0.1123 ? 0.2290 ? 5.8091 ? 1.6121  
? -1.2123 ? 3.0574 ? 0.0626  ? 1.7817 ? 0.3396  ? -0.6459 ? 1.0908  ? 0.3049  ? -0.1479 ? 0.5443  ? -0.1971 ? 0.1120  ? -0.1916 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 867 ? ? ? A 959  ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 961 ? ? ? A 2000 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? B 867 ? ? ? B 959  ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? B 961 ? ? ? B 2000 ? ? ? 
# 
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 PRO 912 ? A PRO 60 
2  1 Y 1 A GLU 913 ? A GLU 61 
3  1 Y 1 A SER 914 ? A SER 62 
4  1 Y 1 A GLY 915 ? A GLY 63 
5  1 Y 1 A GLY 916 ? A GLY 64 
6  1 Y 1 A GLU 946 ? A GLU 94 
7  1 Y 1 A ASP 947 ? A ASP 95 
8  1 Y 1 A GLY 948 ? A GLY 96 
9  1 Y 1 A GLY 949 ? A GLY 97 
10 1 Y 1 B GLY 853 ? B GLY 1  
11 1 Y 1 B ASP 854 ? B ASP 2  
12 1 Y 1 B ILE 855 ? B ILE 3  
13 1 Y 1 B VAL 856 ? B VAL 4  
14 1 Y 1 B SER 857 ? B SER 5  
15 1 Y 1 B GLU 858 ? B GLU 6  
16 1 Y 1 B LYS 859 ? B LYS 7  
17 1 Y 1 B LYS 860 ? B LYS 8  
18 1 Y 1 B PRO 861 ? B PRO 9  
19 1 Y 1 B ALA 862 ? B ALA 10 
20 1 Y 1 B THR 863 ? B THR 11 
21 1 Y 1 B GLU 864 ? B GLU 12 
22 1 Y 1 B GLU 913 ? B GLU 61 
23 1 Y 1 B SER 914 ? B SER 62 
24 1 Y 1 B GLY 915 ? B GLY 63 
25 1 Y 1 B GLU 946 ? B GLU 94 
26 1 Y 1 B ASP 947 ? B ASP 95 
27 1 Y 1 B GLY 948 ? B GLY 96 
28 1 Y 1 B GLY 949 ? B GLY 97 
# 
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 
A1H5R C1   C  N N 1   
A1H5R C2   C  N N 2   
A1H5R C3   C  Y N 3   
A1H5R C4   C  Y N 4   
A1H5R C5   C  Y N 5   
A1H5R C6   C  Y N 6   
A1H5R C7   C  Y N 7   
A1H5R C8   C  Y N 8   
A1H5R C11  C  Y N 9   
A1H5R C12  C  Y N 10  
A1H5R C15  C  Y N 11  
A1H5R C18  C  Y N 12  
A1H5R N9   N  N N 13  
A1H5R C10  C  N N 14  
A1H5R C13  C  Y N 15  
A1H5R C14  C  Y N 16  
A1H5R N16  N  Y N 17  
A1H5R N17  N  Y N 18  
A1H5R N19  N  Y N 19  
A1H5R C20  C  N N 20  
A1H5R H1   H  N N 21  
A1H5R H2   H  N N 22  
A1H5R H3   H  N N 23  
A1H5R H4   H  N N 24  
A1H5R H5   H  N N 25  
A1H5R H6   H  N N 26  
A1H5R H7   H  N N 27  
A1H5R H8   H  N N 28  
A1H5R H9   H  N N 29  
A1H5R H10  H  N N 30  
A1H5R H11  H  N N 31  
A1H5R H12  H  N N 32  
A1H5R H13  H  N N 33  
A1H5R H14  H  N N 34  
A1H5R H15  H  N N 35  
A1H5R H16  H  N N 36  
A1H5R H17  H  N N 37  
A1H5R H18  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
NA    NA   NA N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
PTR   N    N  N N 329 
PTR   CA   C  N S 330 
PTR   C    C  N N 331 
PTR   O    O  N N 332 
PTR   OXT  O  N N 333 
PTR   CB   C  N N 334 
PTR   CG   C  Y N 335 
PTR   CD1  C  Y N 336 
PTR   CD2  C  Y N 337 
PTR   CE1  C  Y N 338 
PTR   CE2  C  Y N 339 
PTR   CZ   C  Y N 340 
PTR   OH   O  N N 341 
PTR   P    P  N N 342 
PTR   O1P  O  N N 343 
PTR   O2P  O  N N 344 
PTR   O3P  O  N N 345 
PTR   H    H  N N 346 
PTR   H2   H  N N 347 
PTR   HA   H  N N 348 
PTR   HXT  H  N N 349 
PTR   HB2  H  N N 350 
PTR   HB3  H  N N 351 
PTR   HD1  H  N N 352 
PTR   HD2  H  N N 353 
PTR   HE1  H  N N 354 
PTR   HE2  H  N N 355 
PTR   HO2P H  N N 356 
PTR   HO3P H  N N 357 
SER   N    N  N N 358 
SER   CA   C  N S 359 
SER   C    C  N N 360 
SER   O    O  N N 361 
SER   CB   C  N N 362 
SER   OG   O  N N 363 
SER   OXT  O  N N 364 
SER   H    H  N N 365 
SER   H2   H  N N 366 
SER   HA   H  N N 367 
SER   HB2  H  N N 368 
SER   HB3  H  N N 369 
SER   HG   H  N N 370 
SER   HXT  H  N N 371 
THR   N    N  N N 372 
THR   CA   C  N S 373 
THR   C    C  N N 374 
THR   O    O  N N 375 
THR   CB   C  N R 376 
THR   OG1  O  N N 377 
THR   CG2  C  N N 378 
THR   OXT  O  N N 379 
THR   H    H  N N 380 
THR   H2   H  N N 381 
THR   HA   H  N N 382 
THR   HB   H  N N 383 
THR   HG1  H  N N 384 
THR   HG21 H  N N 385 
THR   HG22 H  N N 386 
THR   HG23 H  N N 387 
THR   HXT  H  N N 388 
TRP   N    N  N N 389 
TRP   CA   C  N S 390 
TRP   C    C  N N 391 
TRP   O    O  N N 392 
TRP   CB   C  N N 393 
TRP   CG   C  Y N 394 
TRP   CD1  C  Y N 395 
TRP   CD2  C  Y N 396 
TRP   NE1  N  Y N 397 
TRP   CE2  C  Y N 398 
TRP   CE3  C  Y N 399 
TRP   CZ2  C  Y N 400 
TRP   CZ3  C  Y N 401 
TRP   CH2  C  Y N 402 
TRP   OXT  O  N N 403 
TRP   H    H  N N 404 
TRP   H2   H  N N 405 
TRP   HA   H  N N 406 
TRP   HB2  H  N N 407 
TRP   HB3  H  N N 408 
TRP   HD1  H  N N 409 
TRP   HE1  H  N N 410 
TRP   HE3  H  N N 411 
TRP   HZ2  H  N N 412 
TRP   HZ3  H  N N 413 
TRP   HH2  H  N N 414 
TRP   HXT  H  N N 415 
TYR   N    N  N N 416 
TYR   CA   C  N S 417 
TYR   C    C  N N 418 
TYR   O    O  N N 419 
TYR   CB   C  N N 420 
TYR   CG   C  Y N 421 
TYR   CD1  C  Y N 422 
TYR   CD2  C  Y N 423 
TYR   CE1  C  Y N 424 
TYR   CE2  C  Y N 425 
TYR   CZ   C  Y N 426 
TYR   OH   O  N N 427 
TYR   OXT  O  N N 428 
TYR   H    H  N N 429 
TYR   H2   H  N N 430 
TYR   HA   H  N N 431 
TYR   HB2  H  N N 432 
TYR   HB3  H  N N 433 
TYR   HD1  H  N N 434 
TYR   HD2  H  N N 435 
TYR   HE1  H  N N 436 
TYR   HE2  H  N N 437 
TYR   HH   H  N N 438 
TYR   HXT  H  N N 439 
VAL   N    N  N N 440 
VAL   CA   C  N S 441 
VAL   C    C  N N 442 
VAL   O    O  N N 443 
VAL   CB   C  N N 444 
VAL   CG1  C  N N 445 
VAL   CG2  C  N N 446 
VAL   OXT  O  N N 447 
VAL   H    H  N N 448 
VAL   H2   H  N N 449 
VAL   HA   H  N N 450 
VAL   HB   H  N N 451 
VAL   HG11 H  N N 452 
VAL   HG12 H  N N 453 
VAL   HG13 H  N N 454 
VAL   HG21 H  N N 455 
VAL   HG22 H  N N 456 
VAL   HG23 H  N N 457 
VAL   HXT  H  N N 458 
# 
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 
A1H5R C15 N16  doub Y N 1   
A1H5R C15 C14  sing Y N 2   
A1H5R N16 C11  sing Y N 3   
A1H5R C7  C6   doub Y N 4   
A1H5R C7  C8   sing Y N 5   
A1H5R C10 N9   sing N N 6   
A1H5R C11 N9   sing N N 7   
A1H5R C11 C12  doub Y N 8   
A1H5R N9  C8   sing N N 9   
A1H5R C14 N17  sing Y N 10  
A1H5R C14 C13  doub Y N 11  
A1H5R C6  C5   sing Y N 12  
A1H5R N17 C18  doub Y N 13  
A1H5R C8  C3   doub Y N 14  
A1H5R C12 C13  sing Y N 15  
A1H5R C13 N19  sing Y N 16  
A1H5R C18 N19  sing Y N 17  
A1H5R N19 C20  sing N N 18  
A1H5R C5  C4   doub Y N 19  
A1H5R C3  C4   sing Y N 20  
A1H5R C3  C2   sing N N 21  
A1H5R C2  C1   sing N N 22  
A1H5R C1  H1   sing N N 23  
A1H5R C1  H2   sing N N 24  
A1H5R C1  H3   sing N N 25  
A1H5R C2  H4   sing N N 26  
A1H5R C2  H5   sing N N 27  
A1H5R C4  H6   sing N N 28  
A1H5R C5  H7   sing N N 29  
A1H5R C6  H8   sing N N 30  
A1H5R C7  H9   sing N N 31  
A1H5R C12 H10  sing N N 32  
A1H5R C15 H11  sing N N 33  
A1H5R C18 H12  sing N N 34  
A1H5R C10 H13  sing N N 35  
A1H5R C10 H14  sing N N 36  
A1H5R C10 H15  sing N N 37  
A1H5R C20 H16  sing N N 38  
A1H5R C20 H17  sing N N 39  
A1H5R C20 H18  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
PTR   N   CA   sing N N 317 
PTR   N   H    sing N N 318 
PTR   N   H2   sing N N 319 
PTR   CA  C    sing N N 320 
PTR   CA  CB   sing N N 321 
PTR   CA  HA   sing N N 322 
PTR   C   O    doub N N 323 
PTR   C   OXT  sing N N 324 
PTR   OXT HXT  sing N N 325 
PTR   CB  CG   sing N N 326 
PTR   CB  HB2  sing N N 327 
PTR   CB  HB3  sing N N 328 
PTR   CG  CD1  doub Y N 329 
PTR   CG  CD2  sing Y N 330 
PTR   CD1 CE1  sing Y N 331 
PTR   CD1 HD1  sing N N 332 
PTR   CD2 CE2  doub Y N 333 
PTR   CD2 HD2  sing N N 334 
PTR   CE1 CZ   doub Y N 335 
PTR   CE1 HE1  sing N N 336 
PTR   CE2 CZ   sing Y N 337 
PTR   CE2 HE2  sing N N 338 
PTR   CZ  OH   sing N N 339 
PTR   OH  P    sing N N 340 
PTR   P   O1P  doub N N 341 
PTR   P   O2P  sing N N 342 
PTR   P   O3P  sing N N 343 
PTR   O2P HO2P sing N N 344 
PTR   O3P HO3P sing N N 345 
SER   N   CA   sing N N 346 
SER   N   H    sing N N 347 
SER   N   H2   sing N N 348 
SER   CA  C    sing N N 349 
SER   CA  CB   sing N N 350 
SER   CA  HA   sing N N 351 
SER   C   O    doub N N 352 
SER   C   OXT  sing N N 353 
SER   CB  OG   sing N N 354 
SER   CB  HB2  sing N N 355 
SER   CB  HB3  sing N N 356 
SER   OG  HG   sing N N 357 
SER   OXT HXT  sing N N 358 
THR   N   CA   sing N N 359 
THR   N   H    sing N N 360 
THR   N   H2   sing N N 361 
THR   CA  C    sing N N 362 
THR   CA  CB   sing N N 363 
THR   CA  HA   sing N N 364 
THR   C   O    doub N N 365 
THR   C   OXT  sing N N 366 
THR   CB  OG1  sing N N 367 
THR   CB  CG2  sing N N 368 
THR   CB  HB   sing N N 369 
THR   OG1 HG1  sing N N 370 
THR   CG2 HG21 sing N N 371 
THR   CG2 HG22 sing N N 372 
THR   CG2 HG23 sing N N 373 
THR   OXT HXT  sing N N 374 
TRP   N   CA   sing N N 375 
TRP   N   H    sing N N 376 
TRP   N   H2   sing N N 377 
TRP   CA  C    sing N N 378 
TRP   CA  CB   sing N N 379 
TRP   CA  HA   sing N N 380 
TRP   C   O    doub N N 381 
TRP   C   OXT  sing N N 382 
TRP   CB  CG   sing N N 383 
TRP   CB  HB2  sing N N 384 
TRP   CB  HB3  sing N N 385 
TRP   CG  CD1  doub Y N 386 
TRP   CG  CD2  sing Y N 387 
TRP   CD1 NE1  sing Y N 388 
TRP   CD1 HD1  sing N N 389 
TRP   CD2 CE2  doub Y N 390 
TRP   CD2 CE3  sing Y N 391 
TRP   NE1 CE2  sing Y N 392 
TRP   NE1 HE1  sing N N 393 
TRP   CE2 CZ2  sing Y N 394 
TRP   CE3 CZ3  doub Y N 395 
TRP   CE3 HE3  sing N N 396 
TRP   CZ2 CH2  doub Y N 397 
TRP   CZ2 HZ2  sing N N 398 
TRP   CZ3 CH2  sing Y N 399 
TRP   CZ3 HZ3  sing N N 400 
TRP   CH2 HH2  sing N N 401 
TRP   OXT HXT  sing N N 402 
TYR   N   CA   sing N N 403 
TYR   N   H    sing N N 404 
TYR   N   H2   sing N N 405 
TYR   CA  C    sing N N 406 
TYR   CA  CB   sing N N 407 
TYR   CA  HA   sing N N 408 
TYR   C   O    doub N N 409 
TYR   C   OXT  sing N N 410 
TYR   CB  CG   sing N N 411 
TYR   CB  HB2  sing N N 412 
TYR   CB  HB3  sing N N 413 
TYR   CG  CD1  doub Y N 414 
TYR   CG  CD2  sing Y N 415 
TYR   CD1 CE1  sing Y N 416 
TYR   CD1 HD1  sing N N 417 
TYR   CD2 CE2  doub Y N 418 
TYR   CD2 HD2  sing N N 419 
TYR   CE1 CZ   doub Y N 420 
TYR   CE1 HE1  sing N N 421 
TYR   CE2 CZ   sing Y N 422 
TYR   CE2 HE2  sing N N 423 
TYR   CZ  OH   sing N N 424 
TYR   OH  HH   sing N N 425 
TYR   OXT HXT  sing N N 426 
VAL   N   CA   sing N N 427 
VAL   N   H    sing N N 428 
VAL   N   H2   sing N N 429 
VAL   CA  C    sing N N 430 
VAL   CA  CB   sing N N 431 
VAL   CA  HA   sing N N 432 
VAL   C   O    doub N N 433 
VAL   C   OXT  sing N N 434 
VAL   CB  CG1  sing N N 435 
VAL   CB  CG2  sing N N 436 
VAL   CB  HB   sing N N 437 
VAL   CG1 HG11 sing N N 438 
VAL   CG1 HG12 sing N N 439 
VAL   CG1 HG13 sing N N 440 
VAL   CG2 HG21 sing N N 441 
VAL   CG2 HG22 sing N N 442 
VAL   CG2 HG23 sing N N 443 
VAL   OXT HXT  sing N N 444 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S85 
_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]   0.023235 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001828 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005746 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.022344 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
P  
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   . GLY   A 1 1   ? -48.006 65.877  -20.913 1.00 121.10 ? 853  GLY   A N   1 
ATOM   2    C  CA  . GLY   A 1 1   ? -47.185 67.124  -21.048 1.00 116.98 ? 853  GLY   A CA  1 
ATOM   3    C  C   . GLY   A 1 1   ? -45.710 66.858  -21.319 1.00 111.31 ? 853  GLY   A C   1 
ATOM   4    O  O   . GLY   A 1 1   ? -45.338 65.756  -21.723 1.00 111.23 ? 853  GLY   A O   1 
ATOM   5    N  N   . ASP   A 1 2   ? -44.875 67.869  -21.080 1.00 106.61 ? 854  ASP   A N   1 
ATOM   6    C  CA  . ASP   A 1 2   ? -43.417 67.781  -21.286 1.00 100.95 ? 854  ASP   A CA  1 
ATOM   7    C  C   . ASP   A 1 2   ? -42.772 66.673  -20.460 1.00 97.64  ? 854  ASP   A C   1 
ATOM   8    O  O   . ASP   A 1 2   ? -43.349 66.203  -19.483 1.00 99.69  ? 854  ASP   A O   1 
ATOM   9    C  CB  . ASP   A 1 2   ? -42.717 69.099  -20.920 1.00 98.51  ? 854  ASP   A CB  1 
ATOM   10   C  CG  . ASP   A 1 2   ? -43.164 70.277  -21.775 1.00 100.42 ? 854  ASP   A CG  1 
ATOM   11   O  OD1 . ASP   A 1 2   ? -43.985 70.091  -22.700 1.00 103.03 ? 854  ASP   A OD1 1 
ATOM   12   O  OD2 . ASP   A 1 2   ? -42.685 71.400  -21.504 1.00 99.74  ? 854  ASP   A OD2 1 
ATOM   13   N  N   . ILE   A 1 3   ? -41.561 66.285  -20.863 1.00 92.30  ? 855  ILE   A N   1 
ATOM   14   C  CA  . ILE   A 1 3   ? -40.770 65.267  -20.163 1.00 89.75  ? 855  ILE   A CA  1 
ATOM   15   C  C   . ILE   A 1 3   ? -40.402 65.801  -18.778 1.00 87.00  ? 855  ILE   A C   1 
ATOM   16   O  O   . ILE   A 1 3   ? -39.886 66.914  -18.665 1.00 83.98  ? 855  ILE   A O   1 
ATOM   17   C  CB  . ILE   A 1 3   ? -39.445 64.938  -20.915 1.00 86.05  ? 855  ILE   A CB  1 
ATOM   18   C  CG1 . ILE   A 1 3   ? -39.721 64.382  -22.321 1.00 88.19  ? 855  ILE   A CG1 1 
ATOM   19   C  CG2 . ILE   A 1 3   ? -38.594 63.917  -20.139 1.00 84.19  ? 855  ILE   A CG2 1 
ATOM   20   C  CD1 . ILE   A 1 3   ? -38.514 64.462  -23.251 1.00 84.83  ? 855  ILE   A CD1 1 
ATOM   21   N  N   . VAL   A 1 4   ? -40.673 65.013  -17.739 1.00 87.78  ? 856  VAL   A N   1 
ATOM   22   C  CA  . VAL   A 1 4   ? -40.279 65.394  -16.384 1.00 85.52  ? 856  VAL   A CA  1 
ATOM   23   C  C   . VAL   A 1 4   ? -38.853 64.912  -16.133 1.00 81.58  ? 856  VAL   A C   1 
ATOM   24   O  O   . VAL   A 1 4   ? -38.446 63.845  -16.610 1.00 81.44  ? 856  VAL   A O   1 
ATOM   25   C  CB  . VAL   A 1 4   ? -41.243 64.900  -15.270 1.00 88.86  ? 856  VAL   A CB  1 
ATOM   26   C  CG1 . VAL   A 1 4   ? -42.656 65.427  -15.525 1.00 93.03  ? 856  VAL   A CG1 1 
ATOM   27   C  CG2 . VAL   A 1 4   ? -41.235 63.388  -15.125 1.00 89.81  ? 856  VAL   A CG2 1 
ATOM   28   N  N   . SER   A 1 5   ? -38.109 65.707  -15.377 1.00 78.26  ? 857  SER   A N   1 
ATOM   29   C  CA  . SER   A 1 5   ? -36.723 65.391  -15.051 1.00 74.56  ? 857  SER   A CA  1 
ATOM   30   C  C   . SER   A 1 5   ? -36.453 65.853  -13.629 1.00 73.37  ? 857  SER   A C   1 
ATOM   31   O  O   . SER   A 1 5   ? -37.246 66.576  -13.048 1.00 75.35  ? 857  SER   A O   1 
ATOM   32   C  CB  . SER   A 1 5   ? -35.771 66.080  -16.034 1.00 71.56  ? 857  SER   A CB  1 
ATOM   33   O  OG  . SER   A 1 5   ? -35.847 67.488  -15.929 1.00 71.39  ? 857  SER   A OG  1 
ATOM   34   N  N   . GLU   A 1 6   ? -35.323 65.436  -13.087 1.00 71.07  ? 858  GLU   A N   1 
ATOM   35   C  CA  . GLU   A 1 6   ? -34.984 65.744  -11.719 1.00 70.45  ? 858  GLU   A CA  1 
ATOM   36   C  C   . GLU   A 1 6   ? -34.377 67.137  -11.608 1.00 69.88  ? 858  GLU   A C   1 
ATOM   37   O  O   . GLU   A 1 6   ? -33.535 67.517  -12.422 1.00 65.69  ? 858  GLU   A O   1 
ATOM   38   C  CB  . GLU   A 1 6   ? -34.014 64.696  -11.213 1.00 68.03  ? 858  GLU   A CB  1 
ATOM   39   C  CG  . GLU   A 1 6   ? -33.741 64.774  -9.742  1.00 66.64  ? 858  GLU   A CG  1 
ATOM   40   C  CD  . GLU   A 1 6   ? -33.071 63.535  -9.196  1.00 64.92  ? 858  GLU   A CD  1 
ATOM   41   O  OE1 . GLU   A 1 6   ? -32.953 62.513  -9.911  1.00 64.73  ? 858  GLU   A OE1 1 
ATOM   42   O  OE2 . GLU   A 1 6   ? -32.654 63.605  -8.021  1.00 63.26  ? 858  GLU   A OE2 1 
ATOM   43   N  N   . LYS   A 1 7   ? -34.802 67.890  -10.595 1.00 73.90  ? 859  LYS   A N   1 
ATOM   44   C  CA  . LYS   A 1 7   ? -34.189 69.183  -10.286 1.00 75.55  ? 859  LYS   A CA  1 
ATOM   45   C  C   . LYS   A 1 7   ? -32.734 68.913  -9.917  1.00 72.93  ? 859  LYS   A C   1 
ATOM   46   O  O   . LYS   A 1 7   ? -32.464 68.063  -9.064  1.00 72.88  ? 859  LYS   A O   1 
ATOM   47   C  CB  . LYS   A 1 7   ? -34.903 69.888  -9.120  1.00 79.38  ? 859  LYS   A CB  1 
ATOM   48   C  CG  . LYS   A 1 7   ? -36.389 70.199  -9.361  1.00 84.06  ? 859  LYS   A CG  1 
ATOM   49   C  CD  . LYS   A 1 7   ? -37.050 70.828  -8.145  1.00 87.45  ? 859  LYS   A CD  1 
ATOM   50   C  CE  . LYS   A 1 7   ? -38.473 71.289  -8.452  1.00 92.50  ? 859  LYS   A CE  1 
ATOM   51   N  NZ  . LYS   A 1 7   ? -39.051 72.122  -7.338  1.00 95.30  ? 859  LYS   A NZ  1 
ATOM   52   N  N   . LYS   A 1 8   ? -31.804 69.594  -10.591 1.00 72.81  ? 860  LYS   A N   1 
ATOM   53   C  CA  . LYS   A 1 8   ? -30.371 69.445  -10.301 1.00 72.22  ? 860  LYS   A CA  1 
ATOM   54   C  C   . LYS   A 1 8   ? -30.065 70.154  -8.973  1.00 72.93  ? 860  LYS   A C   1 
ATOM   55   O  O   . LYS   A 1 8   ? -30.302 71.356  -8.841  1.00 73.28  ? 860  LYS   A O   1 
ATOM   56   C  CB  . LYS   A 1 8   ? -29.473 69.955  -11.454 1.00 71.75  ? 860  LYS   A CB  1 
ATOM   57   C  CG  . LYS   A 1 8   ? -29.604 71.427  -11.844 1.00 73.41  ? 860  LYS   A CG  1 
ATOM   58   C  CD  . LYS   A 1 8   ? -28.600 71.773  -12.958 0.00 71.35  ? 860  LYS   A CD  1 
ATOM   59   C  CE  . LYS   A 1 8   ? -28.557 73.270  -13.236 0.00 72.25  ? 860  LYS   A CE  1 
ATOM   60   N  NZ  . LYS   A 1 8   ? -27.965 74.044  -12.110 0.00 71.55  ? 860  LYS   A NZ  1 
ATOM   61   N  N   . PRO   A 1 9   ? -29.574 69.405  -7.967  1.00 73.89  ? 861  PRO   A N   1 
ATOM   62   C  CA  . PRO   A 1 9   ? -29.322 70.037  -6.668  1.00 75.88  ? 861  PRO   A CA  1 
ATOM   63   C  C   . PRO   A 1 9   ? -28.060 70.903  -6.689  1.00 74.19  ? 861  PRO   A C   1 
ATOM   64   O  O   . PRO   A 1 9   ? -27.211 70.745  -7.576  1.00 68.54  ? 861  PRO   A O   1 
ATOM   65   C  CB  . PRO   A 1 9   ? -29.149 68.840  -5.725  1.00 75.86  ? 861  PRO   A CB  1 
ATOM   66   C  CG  . PRO   A 1 9   ? -28.598 67.766  -6.595  1.00 74.22  ? 861  PRO   A CG  1 
ATOM   67   C  CD  . PRO   A 1 9   ? -29.203 67.976  -7.967  1.00 73.05  ? 861  PRO   A CD  1 
ATOM   68   N  N   . ALA   A 1 10  ? -27.962 71.817  -5.726  1.00 77.51  ? 862  ALA   A N   1 
ATOM   69   C  CA  . ALA   A 1 10  ? -26.748 72.615  -5.537  1.00 77.69  ? 862  ALA   A CA  1 
ATOM   70   C  C   . ALA   A 1 10  ? -25.610 71.691  -5.093  1.00 75.78  ? 862  ALA   A C   1 
ATOM   71   O  O   . ALA   A 1 10  ? -25.757 70.944  -4.117  1.00 74.57  ? 862  ALA   A O   1 
ATOM   72   C  CB  . ALA   A 1 10  ? -26.970 73.718  -4.511  1.00 78.99  ? 862  ALA   A CB  1 
ATOM   73   N  N   . THR   A 1 11  ? -24.502 71.735  -5.835  1.00 75.74  ? 863  THR   A N   1 
ATOM   74   C  CA  . THR   A 1 11  ? -23.323 70.910  -5.554  1.00 72.61  ? 863  THR   A CA  1 
ATOM   75   C  C   . THR   A 1 11  ? -22.175 71.772  -5.022  1.00 69.89  ? 863  THR   A C   1 
ATOM   76   O  O   . THR   A 1 11  ? -21.872 72.835  -5.575  1.00 69.82  ? 863  THR   A O   1 
ATOM   77   C  CB  . THR   A 1 11  ? -22.860 70.083  -6.788  1.00 72.80  ? 863  THR   A CB  1 
ATOM   78   O  OG1 . THR   A 1 11  ? -21.729 69.281  -6.421  1.00 72.80  ? 863  THR   A OG1 1 
ATOM   79   C  CG2 . THR   A 1 11  ? -22.492 70.962  -8.004  1.00 72.45  ? 863  THR   A CG2 1 
ATOM   80   N  N   . GLU   A 1 12  ? -21.572 71.314  -3.928  1.00 65.84  ? 864  GLU   A N   1 
ATOM   81   C  CA  . GLU   A 1 12  ? -20.359 71.907  -3.376  1.00 61.38  ? 864  GLU   A CA  1 
ATOM   82   C  C   . GLU   A 1 12  ? -19.238 70.900  -3.601  1.00 55.59  ? 864  GLU   A C   1 
ATOM   83   O  O   . GLU   A 1 12  ? -19.381 69.728  -3.251  1.00 57.05  ? 864  GLU   A O   1 
ATOM   84   C  CB  . GLU   A 1 12  ? -20.530 72.196  -1.883  1.00 63.03  ? 864  GLU   A CB  1 
ATOM   85   C  CG  . GLU   A 1 12  ? -19.431 73.096  -1.303  0.00 62.27  ? 864  GLU   A CG  1 
ATOM   86   C  CD  . GLU   A 1 12  ? -19.720 73.541  0.123   0.00 63.81  ? 864  GLU   A CD  1 
ATOM   87   O  OE1 . GLU   A 1 12  ? -20.251 72.732  0.914   0.00 64.35  ? 864  GLU   A OE1 1 
ATOM   88   O  OE2 . GLU   A 1 12  ? -19.406 74.704  0.455   0.00 64.71  ? 864  GLU   A OE2 1 
ATOM   89   N  N   . VAL   A 1 13  ? -18.135 71.352  -4.191  1.00 49.64  ? 865  VAL   A N   1 
ATOM   90   C  CA  . VAL   A 1 13  ? -17.010 70.466  -4.498  1.00 45.94  ? 865  VAL   A CA  1 
ATOM   91   C  C   . VAL   A 1 13  ? -16.293 70.114  -3.190  1.00 41.48  ? 865  VAL   A C   1 
ATOM   92   O  O   . VAL   A 1 13  ? -16.106 70.962  -2.327  1.00 41.07  ? 865  VAL   A O   1 
ATOM   93   C  CB  . VAL   A 1 13  ? -16.018 71.103  -5.500  1.00 47.47  ? 865  VAL   A CB  1 
ATOM   94   C  CG1 . VAL   A 1 13  ? -14.826 70.171  -5.778  1.00 47.10  ? 865  VAL   A CG1 1 
ATOM   95   C  CG2 . VAL   A 1 13  ? -16.728 71.434  -6.811  1.00 50.08  ? 865  VAL   A CG2 1 
ATOM   96   N  N   . ASP   A 1 14  ? -15.906 68.848  -3.067  1.00 35.52  ? 866  ASP   A N   1 
ATOM   97   C  CA  . ASP   A 1 14  ? -15.216 68.353  -1.885  1.00 32.41  ? 866  ASP   A CA  1 
ATOM   98   C  C   . ASP   A 1 14  ? -13.724 68.427  -2.197  1.00 28.34  ? 866  ASP   A C   1 
ATOM   99   O  O   . ASP   A 1 14  ? -13.266 67.717  -3.079  1.00 26.50  ? 866  ASP   A O   1 
ATOM   100  C  CB  . ASP   A 1 14  ? -15.641 66.911  -1.609  1.00 32.14  ? 866  ASP   A CB  1 
ATOM   101  C  CG  . ASP   A 1 14  ? -15.038 66.344  -0.340  1.00 31.22  ? 866  ASP   A CG  1 
ATOM   102  O  OD1 . ASP   A 1 14  ? -14.025 66.868  0.151   1.00 29.87  ? 866  ASP   A OD1 1 
ATOM   103  O  OD2 . ASP   A 1 14  ? -15.574 65.350  0.167   1.00 35.16  ? 866  ASP   A OD2 1 
ATOM   104  N  N   . PRO   A 1 15  ? -12.957 69.243  -1.447  1.00 28.88  ? 867  PRO   A N   1 
ATOM   105  C  CA  . PRO   A 1 15  ? -11.523 69.365  -1.742  1.00 28.33  ? 867  PRO   A CA  1 
ATOM   106  C  C   . PRO   A 1 15  ? -10.706 68.113  -1.406  1.00 24.28  ? 867  PRO   A C   1 
ATOM   107  O  O   . PRO   A 1 15  ? -9.530  68.049  -1.734  1.00 23.82  ? 867  PRO   A O   1 
ATOM   108  C  CB  . PRO   A 1 15  ? -11.079 70.521  -0.838  1.00 29.84  ? 867  PRO   A CB  1 
ATOM   109  C  CG  . PRO   A 1 15  ? -12.013 70.491  0.280   1.00 30.19  ? 867  PRO   A CG  1 
ATOM   110  C  CD  . PRO   A 1 15  ? -13.329 70.049  -0.272  1.00 29.47  ? 867  PRO   A CD  1 
ATOM   111  N  N   . THR   A 1 16  ? -11.323 67.147  -0.735  1.00 21.53  ? 868  THR   A N   1 
ATOM   112  C  CA  . THR   A 1 16  ? -10.693 65.865  -0.473  1.00 20.99  ? 868  THR   A CA  1 
ATOM   113  C  C   . THR   A 1 16  ? -11.107 64.757  -1.424  1.00 17.17  ? 868  THR   A C   1 
ATOM   114  O  O   . THR   A 1 16  ? -10.728 63.635  -1.194  1.00 18.41  ? 868  THR   A O   1 
ATOM   115  C  CB  . THR   A 1 16  ? -10.980 65.399  0.977   1.00 20.37  ? 868  THR   A CB  1 
ATOM   116  O  OG1 . THR   A 1 16  ? -12.359 65.071  1.115   1.00 18.45  ? 868  THR   A OG1 1 
ATOM   117  C  CG2 . THR   A 1 16  ? -10.587 66.486  1.992   1.00 20.72  ? 868  THR   A CG2 1 
ATOM   118  N  N   A HIS   A 1 17  ? -11.868 65.076  -2.478  0.50 21.19  ? 869  HIS   A N   1 
ATOM   119  N  N   B HIS   A 1 17  ? -11.951 65.055  -2.413  0.50 20.73  ? 869  HIS   A N   1 
ATOM   120  C  CA  A HIS   A 1 17  ? -12.305 64.101  -3.483  0.50 21.49  ? 869  HIS   A CA  1 
ATOM   121  C  CA  B HIS   A 1 17  ? -12.270 64.109  -3.471  0.50 20.30  ? 869  HIS   A CA  1 
ATOM   122  C  C   A HIS   A 1 17  ? -11.573 64.333  -4.806  0.50 21.60  ? 869  HIS   A C   1 
ATOM   123  C  C   B HIS   A 1 17  ? -11.370 64.456  -4.642  0.50 20.62  ? 869  HIS   A C   1 
ATOM   124  O  O   A HIS   A 1 17  ? -11.925 65.248  -5.558  0.50 21.30  ? 869  HIS   A O   1 
ATOM   125  O  O   B HIS   A 1 17  ? -11.327 65.616  -5.064  0.50 19.00  ? 869  HIS   A O   1 
ATOM   126  C  CB  A HIS   A 1 17  ? -13.819 64.205  -3.719  0.50 22.10  ? 869  HIS   A CB  1 
ATOM   127  C  CB  B HIS   A 1 17  ? -13.748 64.189  -3.886  0.50 20.21  ? 869  HIS   A CB  1 
ATOM   128  C  CG  A HIS   A 1 17  ? -14.330 63.282  -4.783  0.50 26.31  ? 869  HIS   A CG  1 
ATOM   129  C  CG  B HIS   A 1 17  ? -14.693 63.569  -2.899  0.50 24.24  ? 869  HIS   A CG  1 
ATOM   130  N  ND1 A HIS   A 1 17  ? -14.537 63.684  -6.084  0.50 30.57  ? 869  HIS   A ND1 1 
ATOM   131  N  ND1 B HIS   A 1 17  ? -14.279 62.709  -1.905  0.50 25.80  ? 869  HIS   A ND1 1 
ATOM   132  C  CD2 A HIS   A 1 17  ? -14.650 61.967  -4.741  0.50 30.73  ? 869  HIS   A CD2 1 
ATOM   133  C  CD2 B HIS   A 1 17  ? -16.039 63.668  -2.772  0.50 22.78  ? 869  HIS   A CD2 1 
ATOM   134  C  CE1 A HIS   A 1 17  ? -14.987 62.665  -6.792  0.50 30.61  ? 869  HIS   A CE1 1 
ATOM   135  C  CE1 B HIS   A 1 17  ? -15.326 62.315  -1.200  0.50 24.44  ? 869  HIS   A CE1 1 
ATOM   136  N  NE2 A HIS   A 1 17  ? -15.058 61.609  -6.001  0.50 33.42  ? 869  HIS   A NE2 1 
ATOM   137  N  NE2 B HIS   A 1 17  ? -16.405 62.884  -1.706  0.50 26.54  ? 869  HIS   A NE2 1 
ATOM   138  N  N   . PHE   A 1 18  ? -10.607 63.464  -5.103  1.00 19.33  ? 870  PHE   A N   1 
ATOM   139  C  CA  . PHE   A 1 18  ? -9.753  63.581  -6.279  1.00 21.31  ? 870  PHE   A CA  1 
ATOM   140  C  C   . PHE   A 1 18  ? -10.371 62.729  -7.391  1.00 23.53  ? 870  PHE   A C   1 
ATOM   141  O  O   . PHE   A 1 18  ? -10.648 61.538  -7.197  1.00 25.25  ? 870  PHE   A O   1 
ATOM   142  C  CB  . PHE   A 1 18  ? -8.325  63.128  -5.921  1.00 16.59  ? 870  PHE   A CB  1 
ATOM   143  C  CG  . PHE   A 1 18  ? -7.630  64.067  -4.973  1.00 20.73  ? 870  PHE   A CG  1 
ATOM   144  C  CD1 . PHE   A 1 18  ? -7.926  64.057  -3.617  1.00 20.67  ? 870  PHE   A CD1 1 
ATOM   145  C  CD2 . PHE   A 1 18  ? -6.690  64.977  -5.440  1.00 22.71  ? 870  PHE   A CD2 1 
ATOM   146  C  CE1 . PHE   A 1 18  ? -7.308  64.967  -2.737  1.00 21.98  ? 870  PHE   A CE1 1 
ATOM   147  C  CE2 . PHE   A 1 18  ? -6.070  65.891  -4.578  1.00 23.43  ? 870  PHE   A CE2 1 
ATOM   148  C  CZ  . PHE   A 1 18  ? -6.374  65.880  -3.235  1.00 20.22  ? 870  PHE   A CZ  1 
ATOM   149  N  N   . GLU   A 1 19  ? -10.613 63.354  -8.540  1.00 22.71  ? 871  GLU   A N   1 
ATOM   150  C  CA  . GLU   A 1 19  ? -11.177 62.674  -9.699  1.00 24.09  ? 871  GLU   A CA  1 
ATOM   151  C  C   . GLU   A 1 19  ? -10.116 61.800  -10.361 1.00 23.43  ? 871  GLU   A C   1 
ATOM   152  O  O   . GLU   A 1 19  ? -8.996  62.247  -10.604 1.00 22.40  ? 871  GLU   A O   1 
ATOM   153  C  CB  . GLU   A 1 19  ? -11.719 63.690  -10.715 1.00 24.06  ? 871  GLU   A CB  1 
ATOM   154  C  CG  . GLU   A 1 19  ? -12.823 64.605  -10.172 1.00 31.65  ? 871  GLU   A CG  1 
ATOM   155  C  CD  . GLU   A 1 19  ? -13.455 65.486  -11.246 1.00 41.33  ? 871  GLU   A CD  1 
ATOM   156  O  OE1 . GLU   A 1 19  ? -13.648 65.010  -12.382 1.00 48.72  ? 871  GLU   A OE1 1 
ATOM   157  O  OE2 . GLU   A 1 19  ? -13.772 66.655  -10.953 1.00 49.18  ? 871  GLU   A OE2 1 
ATOM   158  N  N   . LYS   A 1 20  ? -10.459 60.543  -10.630 1.00 23.32  ? 872  LYS   A N   1 
ATOM   159  C  CA  . LYS   A 1 20  ? -9.562  59.627  -11.337 1.00 25.26  ? 872  LYS   A CA  1 
ATOM   160  C  C   . LYS   A 1 20  ? -8.973  60.236  -12.622 1.00 24.06  ? 872  LYS   A C   1 
ATOM   161  O  O   . LYS   A 1 20  ? -7.767  60.136  -12.875 1.00 23.94  ? 872  LYS   A O   1 
ATOM   162  C  CB  . LYS   A 1 20  ? -10.322 58.339  -11.680 1.00 26.87  ? 872  LYS   A CB  1 
ATOM   163  C  CG  . LYS   A 1 20  ? -9.481  57.225  -12.319 1.00 35.03  ? 872  LYS   A CG  1 
ATOM   164  C  CD  . LYS   A 1 20  ? -10.363 56.011  -12.598 1.00 41.16  ? 872  LYS   A CD  1 
ATOM   165  C  CE  . LYS   A 1 20  ? -9.664  54.976  -13.463 1.00 46.29  ? 872  LYS   A CE  1 
ATOM   166  N  NZ  . LYS   A 1 20  ? -10.527 53.780  -13.706 0.00 48.33  ? 872  LYS   A NZ  1 
ATOM   167  N  N   . ARG   A 1 21  ? -9.825  60.875  -13.419 1.00 27.35  ? 873  ARG   A N   1 
ATOM   168  C  CA  . ARG   A 1 21  ? -9.410  61.388  -14.743 1.00 26.29  ? 873  ARG   A CA  1 
ATOM   169  C  C   . ARG   A 1 21  ? -8.269  62.415  -14.697 1.00 23.92  ? 873  ARG   A C   1 
ATOM   170  O  O   . ARG   A 1 21  ? -7.534  62.565  -15.657 1.00 24.52  ? 873  ARG   A O   1 
ATOM   171  C  CB  . ARG   A 1 21  ? -10.605 61.948  -15.504 1.00 28.38  ? 873  ARG   A CB  1 
ATOM   172  C  CG  . ARG   A 1 21  ? -11.249 63.193  -14.948 1.00 28.44  ? 873  ARG   A CG  1 
ATOM   173  C  CD  . ARG   A 1 21  ? -12.425 63.583  -15.844 1.00 34.43  ? 873  ARG   A CD  1 
ATOM   174  N  NE  . ARG   A 1 21  ? -13.126 64.773  -15.352 1.00 36.33  ? 873  ARG   A NE  1 
ATOM   175  C  CZ  . ARG   A 1 21  ? -13.715 65.701  -16.113 1.00 39.59  ? 873  ARG   A CZ  1 
ATOM   176  N  NH1 . ARG   A 1 21  ? -13.712 65.637  -17.446 1.00 37.56  ? 873  ARG   A NH1 1 
ATOM   177  N  NH2 . ARG   A 1 21  ? -14.311 66.731  -15.526 1.00 42.92  ? 873  ARG   A NH2 1 
ATOM   178  N  N   . PHE   A 1 22  ? -8.120  63.111  -13.573 1.00 21.81  ? 874  PHE   A N   1 
ATOM   179  C  CA  . PHE   A 1 22  ? -7.064  64.107  -13.421 1.00 21.74  ? 874  PHE   A CA  1 
ATOM   180  C  C   . PHE   A 1 22  ? -5.860  63.628  -12.647 1.00 20.78  ? 874  PHE   A C   1 
ATOM   181  O  O   . PHE   A 1 22  ? -4.899  64.397  -12.465 1.00 20.72  ? 874  PHE   A O   1 
ATOM   182  C  CB  . PHE   A 1 22  ? -7.653  65.360  -12.754 1.00 21.80  ? 874  PHE   A CB  1 
ATOM   183  C  CG  . PHE   A 1 22  ? -8.782  65.998  -13.523 1.00 21.00  ? 874  PHE   A CG  1 
ATOM   184  C  CD1 . PHE   A 1 22  ? -8.708  66.167  -14.915 1.00 24.15  ? 874  PHE   A CD1 1 
ATOM   185  C  CD2 . PHE   A 1 22  ? -9.912  66.459  -12.854 1.00 24.81  ? 874  PHE   A CD2 1 
ATOM   186  C  CE1 . PHE   A 1 22  ? -9.730  66.773  -15.603 1.00 21.12  ? 874  PHE   A CE1 1 
ATOM   187  C  CE2 . PHE   A 1 22  ? -10.948 67.062  -13.544 1.00 28.93  ? 874  PHE   A CE2 1 
ATOM   188  C  CZ  . PHE   A 1 22  ? -10.858 67.220  -14.925 1.00 27.36  ? 874  PHE   A CZ  1 
ATOM   189  N  N   . LEU   A 1 23  ? -5.885  62.376  -12.177 1.00 18.48  ? 875  LEU   A N   1 
ATOM   190  C  CA  . LEU   A 1 23  ? -4.817  61.898  -11.268 1.00 21.71  ? 875  LEU   A CA  1 
ATOM   191  C  C   . LEU   A 1 23  ? -3.814  61.130  -12.119 1.00 23.61  ? 875  LEU   A C   1 
ATOM   192  O  O   . LEU   A 1 23  ? -4.051  59.964  -12.493 1.00 25.78  ? 875  LEU   A O   1 
ATOM   193  C  CB  . LEU   A 1 23  ? -5.400  61.075  -10.109 1.00 22.12  ? 875  LEU   A CB  1 
ATOM   194  C  CG  . LEU   A 1 23  ? -4.506  60.742  -8.914  1.00 26.93  ? 875  LEU   A CG  1 
ATOM   195  C  CD1 . LEU   A 1 23  ? -4.151  61.986  -8.135  1.00 25.16  ? 875  LEU   A CD1 1 
ATOM   196  C  CD2 . LEU   A 1 23  ? -5.180  59.728  -7.991  1.00 28.62  ? 875  LEU   A CD2 1 
ATOM   197  N  N   . LYS   A 1 24  ? -2.729  61.812  -12.486 1.00 23.39  ? 876  LYS   A N   1 
ATOM   198  C  CA  . LYS   A 1 24  ? -1.807  61.322  -13.515 1.00 29.15  ? 876  LYS   A CA  1 
ATOM   199  C  C   . LYS   A 1 24  ? -0.497  60.806  -12.917 1.00 29.73  ? 876  LYS   A C   1 
ATOM   200  O  O   . LYS   A 1 24  ? 0.236   61.545  -12.278 1.00 24.50  ? 876  LYS   A O   1 
ATOM   201  C  CB  . LYS   A 1 24  ? -1.518  62.432  -14.534 1.00 30.15  ? 876  LYS   A CB  1 
ATOM   202  C  CG  . LYS   A 1 24  ? -2.751  62.998  -15.252 1.00 36.40  ? 876  LYS   A CG  1 
ATOM   203  C  CD  . LYS   A 1 24  ? -3.543  61.928  -15.978 1.00 42.50  ? 876  LYS   A CD  1 
ATOM   204  C  CE  . LYS   A 1 24  ? -4.607  62.526  -16.860 1.00 46.70  ? 876  LYS   A CE  1 
ATOM   205  N  NZ  . LYS   A 1 24  ? -5.560  61.475  -17.333 1.00 50.28  ? 876  LYS   A NZ  1 
ATOM   206  N  N   . ARG   A 1 25  ? -0.223  59.529  -13.153 1.00 29.06  ? 877  ARG   A N   1 
ATOM   207  C  CA  . ARG   A 1 25  ? 0.968   58.852  -12.655 1.00 31.11  ? 877  ARG   A CA  1 
ATOM   208  C  C   . ARG   A 1 25  ? 2.240   59.439  -13.263 1.00 31.21  ? 877  ARG   A C   1 
ATOM   209  O  O   . ARG   A 1 25  ? 2.318   59.619  -14.492 1.00 34.24  ? 877  ARG   A O   1 
ATOM   210  C  CB  . ARG   A 1 25  ? 0.892   57.352  -13.013 1.00 33.08  ? 877  ARG   A CB  1 
ATOM   211  C  CG  . ARG   A 1 25  ? 1.993   56.474  -12.383 1.00 36.41  ? 877  ARG   A CG  1 
ATOM   212  C  CD  . ARG   A 1 25  ? 1.900   55.038  -12.869 1.00 43.80  ? 877  ARG   A CD  1 
ATOM   213  N  NE  . ARG   A 1 25  ? 3.063   54.233  -12.477 1.00 47.04  ? 877  ARG   A NE  1 
ATOM   214  C  CZ  . ARG   A 1 25  ? 4.264   54.293  -13.051 1.00 45.51  ? 877  ARG   A CZ  1 
ATOM   215  N  NH1 . ARG   A 1 25  ? 4.513   55.148  -14.039 1.00 46.29  ? 877  ARG   A NH1 1 
ATOM   216  N  NH2 . ARG   A 1 25  ? 5.242   53.498  -12.624 1.00 49.51  ? 877  ARG   A NH2 1 
ATOM   217  N  N   . ILE   A 1 26  ? 3.236   59.678  -12.411 1.00 28.39  ? 878  ILE   A N   1 
ATOM   218  C  CA  . ILE   A 1 26  ? 4.612   60.010  -12.841 1.00 28.88  ? 878  ILE   A CA  1 
ATOM   219  C  C   . ILE   A 1 26  ? 5.533   58.785  -12.688 1.00 32.98  ? 878  ILE   A C   1 
ATOM   220  O  O   . ILE   A 1 26  ? 6.188   58.369  -13.655 1.00 33.58  ? 878  ILE   A O   1 
ATOM   221  C  CB  . ILE   A 1 26  ? 5.160   61.243  -12.073 1.00 27.91  ? 878  ILE   A CB  1 
ATOM   222  C  CG1 . ILE   A 1 26  ? 4.313   62.485  -12.393 1.00 26.15  ? 878  ILE   A CG1 1 
ATOM   223  C  CG2 . ILE   A 1 26  ? 6.669   61.500  -12.379 1.00 26.17  ? 878  ILE   A CG2 1 
ATOM   224  C  CD1 . ILE   A 1 26  ? 4.621   63.711  -11.544 1.00 27.32  ? 878  ILE   A CD1 1 
ATOM   225  N  N   . ARG   A 1 27  ? 5.579   58.218  -11.486 1.00 28.21  ? 879  ARG   A N   1 
ATOM   226  C  CA  . ARG   A 1 27  ? 6.442   57.068  -11.181 1.00 31.76  ? 879  ARG   A CA  1 
ATOM   227  C  C   . ARG   A 1 27  ? 6.088   56.410  -9.855  1.00 28.15  ? 879  ARG   A C   1 
ATOM   228  O  O   . ARG   A 1 27  ? 5.386   56.998  -9.026  1.00 29.38  ? 879  ARG   A O   1 
ATOM   229  C  CB  . ARG   A 1 27  ? 7.919   57.495  -11.115 1.00 33.83  ? 879  ARG   A CB  1 
ATOM   230  C  CG  . ARG   A 1 27  ? 8.250   58.503  -10.027 1.00 28.77  ? 879  ARG   A CG  1 
ATOM   231  C  CD  . ARG   A 1 27  ? 9.702   58.927  -10.099 1.00 33.74  ? 879  ARG   A CD  1 
ATOM   232  N  NE  . ARG   A 1 27  ? 10.006  59.899  -9.060  1.00 25.40  ? 879  ARG   A NE  1 
ATOM   233  C  CZ  . ARG   A 1 27  ? 10.514  59.625  -7.859  1.00 29.94  ? 879  ARG   A CZ  1 
ATOM   234  N  NH1 . ARG   A 1 27  ? 10.769  58.376  -7.460  1.00 28.66  ? 879  ARG   A NH1 1 
ATOM   235  N  NH2 . ARG   A 1 27  ? 10.735  60.632  -7.014  1.00 31.41  ? 879  ARG   A NH2 1 
ATOM   236  N  N   . ASP   A 1 28  ? 6.617   55.205  -9.651  1.00 30.02  ? 880  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 28  ? 6.495   54.508  -8.375  1.00 28.49  ? 880  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 28  ? 7.411   55.107  -7.302  1.00 29.54  ? 880  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 28  ? 8.573   55.454  -7.559  1.00 28.50  ? 880  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 28  ? 6.831   53.013  -8.531  1.00 31.81  ? 880  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 28  ? 5.734   52.222  -9.234  1.00 35.45  ? 880  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 28  ? 4.590   52.709  -9.358  1.00 44.23  ? 880  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 28  ? 6.017   51.089  -9.669  1.00 45.75  ? 880  ASP   A OD2 1 
ATOM   244  N  N   . LEU   A 1 29  ? 6.890   55.172  -6.087  1.00 27.33  ? 881  LEU   A N   1 
ATOM   245  C  CA  . LEU   A 1 29  ? 7.672   55.586  -4.918  1.00 26.30  ? 881  LEU   A CA  1 
ATOM   246  C  C   . LEU   A 1 29  ? 8.151   54.398  -4.099  1.00 29.83  ? 881  LEU   A C   1 
ATOM   247  O  O   . LEU   A 1 29  ? 9.281   54.396  -3.622  1.00 32.78  ? 881  LEU   A O   1 
ATOM   248  C  CB  . LEU   A 1 29  ? 6.861   56.551  -4.050  1.00 22.75  ? 881  LEU   A CB  1 
ATOM   249  C  CG  . LEU   A 1 29  ? 6.650   57.936  -4.658  1.00 21.47  ? 881  LEU   A CG  1 
ATOM   250  C  CD1 . LEU   A 1 29  ? 5.746   58.795  -3.776  1.00 22.47  ? 881  LEU   A CD1 1 
ATOM   251  C  CD2 . LEU   A 1 29  ? 7.964   58.672  -4.961  1.00 22.26  ? 881  LEU   A CD2 1 
ATOM   252  N  N   . GLY   A 1 30  ? 7.298   53.392  -3.947  1.00 32.03  ? 882  GLY   A N   1 
ATOM   253  C  CA  . GLY   A 1 30  ? 7.612   52.229  -3.137  1.00 37.62  ? 882  GLY   A CA  1 
ATOM   254  C  C   . GLY   A 1 30  ? 6.434   51.289  -2.980  1.00 42.50  ? 882  GLY   A C   1 
ATOM   255  O  O   . GLY   A 1 30  ? 5.301   51.637  -3.318  1.00 38.62  ? 882  GLY   A O   1 
ATOM   256  N  N   . GLU   A 1 31  ? 6.732   50.085  -2.496  1.00 49.58  ? 883  GLU   A N   1 
ATOM   257  C  CA  . GLU   A 1 31  ? 5.740   49.048  -2.210  1.00 55.44  ? 883  GLU   A CA  1 
ATOM   258  C  C   . GLU   A 1 31  ? 5.770   48.755  -0.711  1.00 58.46  ? 883  GLU   A C   1 
ATOM   259  O  O   . GLU   A 1 31  ? 6.792   48.971  -0.050  1.00 58.45  ? 883  GLU   A O   1 
ATOM   260  C  CB  . GLU   A 1 31  ? 6.054   47.768  -2.996  1.00 59.24  ? 883  GLU   A CB  1 
ATOM   261  C  CG  . GLU   A 1 31  ? 6.108   47.945  -4.515  1.00 61.81  ? 883  GLU   A CG  1 
ATOM   262  C  CD  . GLU   A 1 31  ? 6.231   46.646  -5.290  0.00 65.56  ? 883  GLU   A CD  1 
ATOM   263  O  OE1 . GLU   A 1 31  ? 6.710   45.644  -4.713  0.00 67.72  ? 883  GLU   A OE1 1 
ATOM   264  O  OE2 . GLU   A 1 31  ? 5.855   46.621  -6.481  0.00 66.70  ? 883  GLU   A OE2 1 
ATOM   265  N  N   . GLY   A 1 32  ? 4.656   48.254  -0.178  1.00 61.34  ? 884  GLY   A N   1 
ATOM   266  C  CA  . GLY   A 1 32  ? 4.575   47.933  1.247   1.00 62.20  ? 884  GLY   A CA  1 
ATOM   267  C  C   . GLY   A 1 32  ? 3.305   47.240  1.705   1.00 63.69  ? 884  GLY   A C   1 
ATOM   268  O  O   . GLY   A 1 32  ? 2.290   47.899  1.943   1.00 63.60  ? 884  GLY   A O   1 
ATOM   269  N  N   . HIS   A 1 33  ? 3.378   45.912  1.833   1.00 66.29  ? 885  HIS   A N   1 
ATOM   270  C  CA  . HIS   A 1 33  ? 2.320   45.086  2.438   1.00 67.65  ? 885  HIS   A CA  1 
ATOM   271  C  C   . HIS   A 1 33  ? 0.982   45.200  1.698   1.00 67.84  ? 885  HIS   A C   1 
ATOM   272  O  O   . HIS   A 1 33  ? 0.062   45.885  2.154   1.00 65.48  ? 885  HIS   A O   1 
ATOM   273  C  CB  . HIS   A 1 33  ? 2.166   45.416  3.934   1.00 66.39  ? 885  HIS   A CB  1 
ATOM   274  C  CG  . HIS   A 1 33  ? 1.154   44.602  4.656   0.00 68.71  ? 885  HIS   A CG  1 
ATOM   275  N  ND1 . HIS   A 1 33  ? 1.296   43.250  4.885   0.00 72.03  ? 885  HIS   A ND1 1 
ATOM   276  C  CD2 . HIS   A 1 33  ? -0.034  44.953  5.202   0.00 68.01  ? 885  HIS   A CD2 1 
ATOM   277  C  CE1 . HIS   A 1 33  ? 0.238   42.804  5.538   0.00 73.10  ? 885  HIS   A CE1 1 
ATOM   278  N  NE2 . HIS   A 1 33  ? -0.583  43.818  5.744   0.00 70.69  ? 885  HIS   A NE2 1 
ATOM   279  N  N   . PHE   A 1 34  ? 0.912   44.549  0.533   1.00 70.86  ? 886  PHE   A N   1 
ATOM   280  C  CA  . PHE   A 1 34  ? -0.276  44.529  -0.362  1.00 71.36  ? 886  PHE   A CA  1 
ATOM   281  C  C   . PHE   A 1 34  ? -0.616  45.852  -1.090  1.00 67.07  ? 886  PHE   A C   1 
ATOM   282  O  O   . PHE   A 1 34  ? -1.324  45.824  -2.103  1.00 68.98  ? 886  PHE   A O   1 
ATOM   283  C  CB  . PHE   A 1 34  ? -1.521  43.971  0.354   1.00 73.52  ? 886  PHE   A CB  1 
ATOM   284  C  CG  . PHE   A 1 34  ? -1.408  42.544  0.778   0.00 77.25  ? 886  PHE   A CG  1 
ATOM   285  C  CD1 . PHE   A 1 34  ? -1.686  41.512  -0.115  0.00 80.90  ? 886  PHE   A CD1 1 
ATOM   286  C  CD2 . PHE   A 1 34  ? -1.023  42.220  2.078   0.00 77.54  ? 886  PHE   A CD2 1 
ATOM   287  C  CE1 . PHE   A 1 34  ? -1.577  40.176  0.275   0.00 84.60  ? 886  PHE   A CE1 1 
ATOM   288  C  CE2 . PHE   A 1 34  ? -0.910  40.886  2.481   0.00 81.09  ? 886  PHE   A CE2 1 
ATOM   289  C  CZ  . PHE   A 1 34  ? -1.188  39.862  1.576   0.00 84.71  ? 886  PHE   A CZ  1 
ATOM   290  N  N   . GLY   A 1 35  ? -0.118  46.985  -0.588  1.00 60.83  ? 887  GLY   A N   1 
ATOM   291  C  CA  . GLY   A 1 35  ? -0.283  48.289  -1.235  1.00 56.31  ? 887  GLY   A CA  1 
ATOM   292  C  C   . GLY   A 1 35  ? 0.970   48.730  -1.974  1.00 52.99  ? 887  GLY   A C   1 
ATOM   293  O  O   . GLY   A 1 35  ? 2.051   48.167  -1.772  1.00 53.67  ? 887  GLY   A O   1 
ATOM   294  N  N   . LYS   A 1 36  ? 0.805   49.721  -2.852  1.00 45.35  ? 888  LYS   A N   1 
ATOM   295  C  CA  . LYS   A 1 36  ? 1.925   50.409  -3.501  1.00 40.85  ? 888  LYS   A CA  1 
ATOM   296  C  C   . LYS   A 1 36  ? 1.653   51.906  -3.470  1.00 35.03  ? 888  LYS   A C   1 
ATOM   297  O  O   . LYS   A 1 36  ? 0.492   52.319  -3.508  1.00 29.57  ? 888  LYS   A O   1 
ATOM   298  C  CB  . LYS   A 1 36  ? 2.109   49.942  -4.948  1.00 45.09  ? 888  LYS   A CB  1 
ATOM   299  C  CG  . LYS   A 1 36  ? 0.936   50.234  -5.882  1.00 45.03  ? 888  LYS   A CG  1 
ATOM   300  C  CD  . LYS   A 1 36  ? 1.144   49.633  -7.267  0.00 48.37  ? 888  LYS   A CD  1 
ATOM   301  C  CE  . LYS   A 1 36  ? 2.152   50.425  -8.090  0.00 47.96  ? 888  LYS   A CE  1 
ATOM   302  N  NZ  . LYS   A 1 36  ? 2.281   49.894  -9.475  0.00 50.42  ? 888  LYS   A NZ  1 
ATOM   303  N  N   . VAL   A 1 37  ? 2.726   52.698  -3.418  1.00 29.63  ? 889  VAL   A N   1 
ATOM   304  C  CA  . VAL   A 1 37  ? 2.629   54.147  -3.406  1.00 25.80  ? 889  VAL   A CA  1 
ATOM   305  C  C   . VAL   A 1 37  ? 3.281   54.708  -4.672  1.00 28.50  ? 889  VAL   A C   1 
ATOM   306  O  O   . VAL   A 1 37  ? 4.420   54.330  -5.020  1.00 28.89  ? 889  VAL   A O   1 
ATOM   307  C  CB  . VAL   A 1 37  ? 3.270   54.759  -2.149  1.00 22.43  ? 889  VAL   A CB  1 
ATOM   308  C  CG1 . VAL   A 1 37  ? 3.115   56.265  -2.152  1.00 18.56  ? 889  VAL   A CG1 1 
ATOM   309  C  CG2 . VAL   A 1 37  ? 2.672   54.169  -0.891  1.00 25.61  ? 889  VAL   A CG2 1 
ATOM   310  N  N   . GLU   A 1 38  ? 2.549   55.601  -5.344  1.00 26.89  ? 890  GLU   A N   1 
ATOM   311  C  CA  . GLU   A 1 38  ? 2.985   56.252  -6.568  1.00 25.59  ? 890  GLU   A CA  1 
ATOM   312  C  C   . GLU   A 1 38  ? 3.024   57.765  -6.426  1.00 23.69  ? 890  GLU   A C   1 
ATOM   313  O  O   . GLU   A 1 38  ? 2.133   58.360  -5.779  1.00 23.79  ? 890  GLU   A O   1 
ATOM   314  C  CB  . GLU   A 1 38  ? 2.017   55.955  -7.716  1.00 26.38  ? 890  GLU   A CB  1 
ATOM   315  C  CG  . GLU   A 1 38  ? 1.848   54.513  -8.079  1.00 31.52  ? 890  GLU   A CG  1 
ATOM   316  C  CD  . GLU   A 1 38  ? 0.696   54.317  -9.047  1.00 39.32  ? 890  GLU   A CD  1 
ATOM   317  O  OE1 . GLU   A 1 38  ? -0.421  54.787  -8.754  1.00 39.55  ? 890  GLU   A OE1 1 
ATOM   318  O  OE2 . GLU   A 1 38  ? 0.910   53.685  -10.094 1.00 53.74  ? 890  GLU   A OE2 1 
ATOM   319  N  N   . LEU   A 1 39  ? 4.025   58.380  -7.068  1.00 22.24  ? 891  LEU   A N   1 
ATOM   320  C  CA  . LEU   A 1 39  ? 4.020   59.821  -7.340  1.00 21.94  ? 891  LEU   A CA  1 
ATOM   321  C  C   . LEU   A 1 39  ? 3.095   60.107  -8.523  1.00 22.73  ? 891  LEU   A C   1 
ATOM   322  O  O   . LEU   A 1 39  ? 3.278   59.578  -9.622  1.00 22.35  ? 891  LEU   A O   1 
ATOM   323  C  CB  . LEU   A 1 39  ? 5.420   60.366  -7.661  1.00 21.62  ? 891  LEU   A CB  1 
ATOM   324  C  CG  . LEU   A 1 39  ? 5.522   61.858  -8.031  1.00 17.22  ? 891  LEU   A CG  1 
ATOM   325  C  CD1 . LEU   A 1 39  ? 5.114   62.770  -6.861  1.00 21.45  ? 891  LEU   A CD1 1 
ATOM   326  C  CD2 . LEU   A 1 39  ? 6.931   62.203  -8.447  1.00 21.11  ? 891  LEU   A CD2 1 
ATOM   327  N  N   . CYS   A 1 40  ? 2.102   60.946  -8.268  1.00 23.98  ? 892  CYS   A N   1 
ATOM   328  C  CA  . CYS   A 1 40  ? 1.218   61.477  -9.284  1.00 23.72  ? 892  CYS   A CA  1 
ATOM   329  C  C   . CYS   A 1 40  ? 1.209   62.987  -9.263  1.00 24.89  ? 892  CYS   A C   1 
ATOM   330  O  O   . CYS   A 1 40  ? 1.629   63.604  -8.292  1.00 21.16  ? 892  CYS   A O   1 
ATOM   331  C  CB  . CYS   A 1 40  ? -0.213  60.993  -9.046  1.00 25.16  ? 892  CYS   A CB  1 
ATOM   332  S  SG  . CYS   A 1 40  ? -0.389  59.205  -9.138  1.00 26.69  ? 892  CYS   A SG  1 
ATOM   333  N  N   . ARG   A 1 41  ? 0.731   63.574  -10.355 1.00 22.71  ? 893  ARG   A N   1 
ATOM   334  C  CA  . ARG   A 1 41  ? 0.283   64.956  -10.321 1.00 24.65  ? 893  ARG   A CA  1 
ATOM   335  C  C   . ARG   A 1 41  ? -1.239  64.964  -10.472 1.00 23.22  ? 893  ARG   A C   1 
ATOM   336  O  O   . ARG   A 1 41  ? -1.768  64.332  -11.396 1.00 25.46  ? 893  ARG   A O   1 
ATOM   337  C  CB  . ARG   A 1 41  ? 0.939   65.742  -11.440 1.00 27.01  ? 893  ARG   A CB  1 
ATOM   338  C  CG  . ARG   A 1 41  ? 0.977   67.229  -11.217 1.00 31.31  ? 893  ARG   A CG  1 
ATOM   339  C  CD  . ARG   A 1 41  ? 1.579   67.946  -12.409 1.00 31.90  ? 893  ARG   A CD  1 
ATOM   340  N  NE  . ARG   A 1 41  ? 3.043   68.004  -12.384 1.00 34.27  ? 893  ARG   A NE  1 
ATOM   341  C  CZ  . ARG   A 1 41  ? 3.778   69.049  -11.993 1.00 39.73  ? 893  ARG   A CZ  1 
ATOM   342  N  NH1 . ARG   A 1 41  ? 3.221   70.170  -11.532 1.00 45.85  ? 893  ARG   A NH1 1 
ATOM   343  N  NH2 . ARG   A 1 41  ? 5.098   68.989  -12.056 1.00 46.45  ? 893  ARG   A NH2 1 
ATOM   344  N  N   . TYR   A 1 42  ? -1.937  65.662  -9.576  1.00 20.50  ? 894  TYR   A N   1 
ATOM   345  C  CA  . TYR   A 1 42  ? -3.359  65.928  -9.770  1.00 21.22  ? 894  TYR   A CA  1 
ATOM   346  C  C   . TYR   A 1 42  ? -3.467  67.191  -10.611 1.00 22.03  ? 894  TYR   A C   1 
ATOM   347  O  O   . TYR   A 1 42  ? -3.231  68.311  -10.093 1.00 20.67  ? 894  TYR   A O   1 
ATOM   348  C  CB  . TYR   A 1 42  ? -4.093  66.132  -8.445  1.00 19.31  ? 894  TYR   A CB  1 
ATOM   349  C  CG  . TYR   A 1 42  ? -5.588  66.134  -8.598  1.00 19.15  ? 894  TYR   A CG  1 
ATOM   350  C  CD1 . TYR   A 1 42  ? -6.246  65.017  -9.095  1.00 16.55  ? 894  TYR   A CD1 1 
ATOM   351  C  CD2 . TYR   A 1 42  ? -6.354  67.257  -8.291  1.00 17.80  ? 894  TYR   A CD2 1 
ATOM   352  C  CE1 . TYR   A 1 42  ? -7.609  64.990  -9.231  1.00 19.56  ? 894  TYR   A CE1 1 
ATOM   353  C  CE2 . TYR   A 1 42  ? -7.725  67.246  -8.432  1.00 20.29  ? 894  TYR   A CE2 1 
ATOM   354  C  CZ  . TYR   A 1 42  ? -8.357  66.108  -8.922  1.00 21.74  ? 894  TYR   A CZ  1 
ATOM   355  O  OH  . TYR   A 1 42  ? -9.713  66.061  -9.079  1.00 25.58  ? 894  TYR   A OH  1 
ATOM   356  N  N   . ASP   A 1 43  ? -3.858  67.019  -11.873 1.00 19.81  ? 895  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 43  ? -3.721  68.039  -12.900 1.00 23.17  ? 895  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 43  ? -5.048  68.361  -13.626 1.00 20.24  ? 895  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 43  ? -5.160  68.181  -14.838 1.00 20.43  ? 895  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 43  ? -2.627  67.577  -13.896 1.00 23.97  ? 895  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 43  ? -1.985  68.728  -14.672 1.00 27.38  ? 895  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 43  ? -1.788  69.825  -14.119 1.00 22.37  ? 895  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 43  ? -1.638  68.523  -15.851 1.00 25.89  ? 895  ASP   A OD2 1 
ATOM   364  N  N   . PRO   A 1 44  ? -6.056  68.899  -12.893 1.00 21.60  ? 896  PRO   A N   1 
ATOM   365  C  CA  . PRO   A 1 44  ? -7.354  69.251  -13.495 1.00 21.37  ? 896  PRO   A CA  1 
ATOM   366  C  C   . PRO   A 1 44  ? -7.316  70.264  -14.642 1.00 22.72  ? 896  PRO   A C   1 
ATOM   367  O  O   . PRO   A 1 44  ? -8.214  70.253  -15.479 1.00 24.64  ? 896  PRO   A O   1 
ATOM   368  C  CB  . PRO   A 1 44  ? -8.171  69.810  -12.310 1.00 22.29  ? 896  PRO   A CB  1 
ATOM   369  C  CG  . PRO   A 1 44  ? -7.239  70.028  -11.231 1.00 23.68  ? 896  PRO   A CG  1 
ATOM   370  C  CD  . PRO   A 1 44  ? -6.011  69.233  -11.459 1.00 21.72  ? 896  PRO   A CD  1 
ATOM   371  N  N   . GLU   A 1 45  ? -6.307  71.129  -14.681 1.00 22.26  ? 897  GLU   A N   1 
ATOM   372  C  CA  . GLU   A 1 45  ? -6.161  72.087  -15.775 1.00 28.37  ? 897  GLU   A CA  1 
ATOM   373  C  C   . GLU   A 1 45  ? -5.360  71.528  -16.956 1.00 25.85  ? 897  GLU   A C   1 
ATOM   374  O  O   . GLU   A 1 45  ? -5.142  72.244  -17.917 1.00 31.94  ? 897  GLU   A O   1 
ATOM   375  C  CB  . GLU   A 1 45  ? -5.508  73.379  -15.283 1.00 29.22  ? 897  GLU   A CB  1 
ATOM   376  C  CG  . GLU   A 1 45  ? -6.141  73.931  -14.027 1.00 31.21  ? 897  GLU   A CG  1 
ATOM   377  C  CD  . GLU   A 1 45  ? -5.890  75.409  -13.876 1.00 34.57  ? 897  GLU   A CD  1 
ATOM   378  O  OE1 . GLU   A 1 45  ? -5.066  75.774  -13.039 1.00 36.61  ? 897  GLU   A OE1 1 
ATOM   379  O  OE2 . GLU   A 1 45  ? -6.512  76.201  -14.619 1.00 52.24  ? 897  GLU   A OE2 1 
ATOM   380  N  N   . GLY   A 1 46  ? -4.905  70.276  -16.857 1.00 25.46  ? 898  GLY   A N   1 
ATOM   381  C  CA  . GLY   A 1 46  ? -4.251  69.560  -17.957 1.00 26.61  ? 898  GLY   A CA  1 
ATOM   382  C  C   . GLY   A 1 46  ? -3.010  70.186  -18.572 1.00 29.28  ? 898  GLY   A C   1 
ATOM   383  O  O   . GLY   A 1 46  ? -2.727  69.946  -19.752 1.00 31.38  ? 898  GLY   A O   1 
ATOM   384  N  N   . ASP   A 1 47  ? -2.274  70.975  -17.788 1.00 29.24  ? 899  ASP   A N   1 
ATOM   385  C  CA  . ASP   A 1 47  ? -1.087  71.711  -18.265 1.00 30.06  ? 899  ASP   A CA  1 
ATOM   386  C  C   . ASP   A 1 47  ? 0.221   71.475  -17.475 1.00 32.53  ? 899  ASP   A C   1 
ATOM   387  O  O   . ASP   A 1 47  ? 1.169   72.268  -17.584 1.00 32.96  ? 899  ASP   A O   1 
ATOM   388  C  CB  . ASP   A 1 47  ? -1.418  73.210  -18.320 1.00 33.23  ? 899  ASP   A CB  1 
ATOM   389  C  CG  . ASP   A 1 47  ? -1.713  73.826  -16.948 1.00 31.09  ? 899  ASP   A CG  1 
ATOM   390  O  OD1 . ASP   A 1 47  ? -1.833  73.101  -15.925 1.00 28.94  ? 899  ASP   A OD1 1 
ATOM   391  O  OD2 . ASP   A 1 47  ? -1.822  75.073  -16.900 1.00 36.02  ? 899  ASP   A OD2 1 
ATOM   392  N  N   . ASN   A 1 48  ? 0.275   70.382  -16.715 1.00 27.75  ? 900  ASN   A N   1 
ATOM   393  C  CA  . ASN   A 1 48  ? 1.421   70.049  -15.861 1.00 27.99  ? 900  ASN   A CA  1 
ATOM   394  C  C   . ASN   A 1 48  ? 1.732   71.089  -14.769 1.00 29.19  ? 900  ASN   A C   1 
ATOM   395  O  O   . ASN   A 1 48  ? 2.897   71.306  -14.427 1.00 32.09  ? 900  ASN   A O   1 
ATOM   396  C  CB  . ASN   A 1 48  ? 2.679   69.770  -16.717 1.00 30.61  ? 900  ASN   A CB  1 
ATOM   397  C  CG  . ASN   A 1 48  ? 3.749   68.968  -15.974 1.00 30.82  ? 900  ASN   A CG  1 
ATOM   398  O  OD1 . ASN   A 1 48  ? 3.458   68.224  -15.031 1.00 29.96  ? 900  ASN   A OD1 1 
ATOM   399  N  ND2 . ASN   A 1 48  ? 5.001   69.124  -16.398 1.00 33.68  ? 900  ASN   A ND2 1 
ATOM   400  N  N   . THR   A 1 49  ? 0.698   71.725  -14.216 1.00 25.59  ? 901  THR   A N   1 
ATOM   401  C  CA  . THR   A 1 49  ? 0.891   72.699  -13.134 1.00 26.04  ? 901  THR   A CA  1 
ATOM   402  C  C   . THR   A 1 49  ? 0.290   72.288  -11.795 1.00 25.94  ? 901  THR   A C   1 
ATOM   403  O  O   . THR   A 1 49  ? 0.517   72.950  -10.791 1.00 26.27  ? 901  THR   A O   1 
ATOM   404  C  CB  . THR   A 1 49  ? 0.356   74.095  -13.507 1.00 28.10  ? 901  THR   A CB  1 
ATOM   405  O  OG1 . THR   A 1 49  ? -1.070  74.078  -13.562 1.00 30.38  ? 901  THR   A OG1 1 
ATOM   406  C  CG2 . THR   A 1 49  ? 0.928   74.582  -14.837 1.00 26.69  ? 901  THR   A CG2 1 
ATOM   407  N  N   . GLY   A 1 50  ? -0.451  71.188  -11.773 1.00 23.59  ? 902  GLY   A N   1 
ATOM   408  C  CA  . GLY   A 1 50  ? -1.124  70.725  -10.572 1.00 22.80  ? 902  GLY   A CA  1 
ATOM   409  C  C   . GLY   A 1 50  ? -0.186  70.232  -9.501  1.00 21.80  ? 902  GLY   A C   1 
ATOM   410  O  O   . GLY   A 1 50  ? 1.000   70.030  -9.747  1.00 22.80  ? 902  GLY   A O   1 
ATOM   411  N  N   . GLU   A 1 51  ? -0.715  70.044  -8.291  1.00 23.88  ? 903  GLU   A N   1 
ATOM   412  C  CA  . GLU   A 1 51  ? 0.098   69.611  -7.171  1.00 22.71  ? 903  GLU   A CA  1 
ATOM   413  C  C   . GLU   A 1 51  ? 0.550   68.136  -7.341  1.00 22.35  ? 903  GLU   A C   1 
ATOM   414  O  O   . GLU   A 1 51  ? -0.198  67.287  -7.853  1.00 21.06  ? 903  GLU   A O   1 
ATOM   415  C  CB  . GLU   A 1 51  ? -0.639  69.816  -5.843  1.00 28.22  ? 903  GLU   A CB  1 
ATOM   416  C  CG  . GLU   A 1 51  ? -1.747  68.831  -5.596  1.00 31.14  ? 903  GLU   A CG  1 
ATOM   417  C  CD  . GLU   A 1 51  ? -2.743  69.251  -4.533  1.00 39.95  ? 903  GLU   A CD  1 
ATOM   418  O  OE1 . GLU   A 1 51  ? -2.339  69.907  -3.538  1.00 31.62  ? 903  GLU   A OE1 1 
ATOM   419  O  OE2 . GLU   A 1 51  ? -3.940  68.893  -4.713  1.00 38.32  ? 903  GLU   A OE2 1 
ATOM   420  N  N   . GLN   A 1 52  ? 1.786   67.870  -6.917  1.00 21.78  ? 904  GLN   A N   1 
ATOM   421  C  CA  . GLN   A 1 52  ? 2.293   66.522  -6.794  1.00 18.69  ? 904  GLN   A CA  1 
ATOM   422  C  C   . GLN   A 1 52  ? 1.696   65.933  -5.516  1.00 20.68  ? 904  GLN   A C   1 
ATOM   423  O  O   . GLN   A 1 52  ? 1.586   66.619  -4.504  1.00 21.39  ? 904  GLN   A O   1 
ATOM   424  C  CB  . GLN   A 1 52  ? 3.812   66.521  -6.693  1.00 24.10  ? 904  GLN   A CB  1 
ATOM   425  C  CG  . GLN   A 1 52  ? 4.493   67.108  -7.901  1.00 27.40  ? 904  GLN   A CG  1 
ATOM   426  C  CD  . GLN   A 1 52  ? 6.015   66.999  -7.853  1.00 25.23  ? 904  GLN   A CD  1 
ATOM   427  O  OE1 . GLN   A 1 52  ? 6.624   66.547  -8.807  1.00 23.33  ? 904  GLN   A OE1 1 
ATOM   428  N  NE2 . GLN   A 1 52  ? 6.618   67.413  -6.757  1.00 28.16  ? 904  GLN   A NE2 1 
ATOM   429  N  N   . VAL   A 1 53  ? 1.308   64.675  -5.578  1.00 19.17  ? 905  VAL   A N   1 
ATOM   430  C  CA  . VAL   A 1 53  ? 0.749   63.945  -4.442  1.00 19.47  ? 905  VAL   A CA  1 
ATOM   431  C  C   . VAL   A 1 53  ? 1.246   62.506  -4.454  1.00 20.48  ? 905  VAL   A C   1 
ATOM   432  O  O   . VAL   A 1 53  ? 1.598   61.997  -5.506  1.00 21.56  ? 905  VAL   A O   1 
ATOM   433  C  CB  . VAL   A 1 53  ? -0.797  63.920  -4.498  1.00 18.04  ? 905  VAL   A CB  1 
ATOM   434  C  CG1 . VAL   A 1 53  ? -1.345  65.312  -4.347  1.00 18.29  ? 905  VAL   A CG1 1 
ATOM   435  C  CG2 . VAL   A 1 53  ? -1.313  63.309  -5.802  1.00 17.17  ? 905  VAL   A CG2 1 
ATOM   436  N  N   . ALA   A 1 54  ? 1.290   61.889  -3.277  1.00 17.97  ? 906  ALA   A N   1 
ATOM   437  C  CA  . ALA   A 1 54  ? 1.605   60.477  -3.120  1.00 21.21  ? 906  ALA   A CA  1 
ATOM   438  C  C   . ALA   A 1 54  ? 0.274   59.739  -3.060  1.00 21.72  ? 906  ALA   A C   1 
ATOM   439  O  O   . ALA   A 1 54  ? -0.607  60.103  -2.270  1.00 20.03  ? 906  ALA   A O   1 
ATOM   440  C  CB  . ALA   A 1 54  ? 2.407   60.232  -1.828  1.00 16.62  ? 906  ALA   A CB  1 
ATOM   441  N  N   . VAL   A 1 55  ? 0.134   58.725  -3.911  1.00 20.33  ? 907  VAL   A N   1 
ATOM   442  C  CA  . VAL   A 1 55  ? -1.101  57.943  -4.039  1.00 19.94  ? 907  VAL   A CA  1 
ATOM   443  C  C   . VAL   A 1 55  ? -0.832  56.496  -3.646  1.00 23.46  ? 907  VAL   A C   1 
ATOM   444  O  O   . VAL   A 1 55  ? -0.031  55.820  -4.301  1.00 21.78  ? 907  VAL   A O   1 
ATOM   445  C  CB  . VAL   A 1 55  ? -1.637  57.987  -5.497  1.00 23.15  ? 907  VAL   A CB  1 
ATOM   446  C  CG1 . VAL   A 1 55  ? -2.969  57.221  -5.626  1.00 23.38  ? 907  VAL   A CG1 1 
ATOM   447  C  CG2 . VAL   A 1 55  ? -1.791  59.443  -5.962  1.00 22.82  ? 907  VAL   A CG2 1 
ATOM   448  N  N   . LYS   A 1 56  ? -1.538  56.023  -2.611  1.00 21.63  ? 908  LYS   A N   1 
ATOM   449  C  CA  . LYS   A 1 56  ? -1.477  54.640  -2.172  1.00 23.00  ? 908  LYS   A CA  1 
ATOM   450  C  C   . LYS   A 1 56  ? -2.686  53.870  -2.666  1.00 28.19  ? 908  LYS   A C   1 
ATOM   451  O  O   . LYS   A 1 56  ? -3.832  54.266  -2.453  1.00 25.74  ? 908  LYS   A O   1 
ATOM   452  C  CB  . LYS   A 1 56  ? -1.389  54.522  -0.656  1.00 23.16  ? 908  LYS   A CB  1 
ATOM   453  C  CG  . LYS   A 1 56  ? -1.041  53.104  -0.154  1.00 28.43  ? 908  LYS   A CG  1 
ATOM   454  C  CD  . LYS   A 1 56  ? -0.557  53.183  1.287   1.00 25.68  ? 908  LYS   A CD  1 
ATOM   455  C  CE  . LYS   A 1 56  ? -0.006  51.883  1.754   1.00 34.33  ? 908  LYS   A CE  1 
ATOM   456  N  NZ  . LYS   A 1 56  ? 0.216   51.907  3.203   1.00 25.20  ? 908  LYS   A NZ  1 
ATOM   457  N  N   . SER   A 1 57  ? -2.412  52.742  -3.299  1.00 29.77  ? 909  SER   A N   1 
ATOM   458  C  CA  . SER   A 1 57  ? -3.453  51.921  -3.877  1.00 30.16  ? 909  SER   A CA  1 
ATOM   459  C  C   . SER   A 1 57  ? -3.053  50.462  -3.757  1.00 35.40  ? 909  SER   A C   1 
ATOM   460  O  O   . SER   A 1 57  ? -1.896  50.147  -3.482  1.00 33.74  ? 909  SER   A O   1 
ATOM   461  C  CB  . SER   A 1 57  ? -3.635  52.304  -5.339  1.00 32.07  ? 909  SER   A CB  1 
ATOM   462  O  OG  . SER   A 1 57  ? -2.536  51.858  -6.116  1.00 39.93  ? 909  SER   A OG  1 
ATOM   463  N  N   . LEU   A 1 58  ? -4.016  49.581  -3.987  1.00 38.84  ? 910  LEU   A N   1 
ATOM   464  C  CA  . LEU   A 1 58  ? -3.759  48.142  -3.941  1.00 43.87  ? 910  LEU   A CA  1 
ATOM   465  C  C   . LEU   A 1 58  ? -3.478  47.554  -5.314  1.00 49.32  ? 910  LEU   A C   1 
ATOM   466  O  O   . LEU   A 1 58  ? -4.076  47.977  -6.317  1.00 51.68  ? 910  LEU   A O   1 
ATOM   467  C  CB  . LEU   A 1 58  ? -4.951  47.429  -3.322  1.00 45.74  ? 910  LEU   A CB  1 
ATOM   468  C  CG  . LEU   A 1 58  ? -5.172  47.711  -1.844  1.00 47.32  ? 910  LEU   A CG  1 
ATOM   469  C  CD1 . LEU   A 1 58  ? -6.491  47.149  -1.439  1.00 51.65  ? 910  LEU   A CD1 1 
ATOM   470  C  CD2 . LEU   A 1 58  ? -4.066  47.125  -0.965  1.00 53.73  ? 910  LEU   A CD2 1 
ATOM   471  N  N   . LYS   A 1 59  ? -2.577  46.564  -5.340  1.00 53.92  ? 911  LYS   A N   1 
ATOM   472  C  CA  . LYS   A 1 59  ? -2.343  45.721  -6.518  1.00 56.89  ? 911  LYS   A CA  1 
ATOM   473  C  C   . LYS   A 1 59  ? -3.329  44.558  -6.524  1.00 59.52  ? 911  LYS   A C   1 
ATOM   474  O  O   . LYS   A 1 59  ? -4.544  44.763  -6.558  1.00 59.15  ? 911  LYS   A O   1 
ATOM   475  C  CB  . LYS   A 1 59  ? -0.915  45.171  -6.514  1.00 59.12  ? 911  LYS   A CB  1 
ATOM   476  C  CG  . LYS   A 1 59  ? 0.158   46.221  -6.650  0.00 56.97  ? 911  LYS   A CG  1 
ATOM   477  C  CD  . LYS   A 1 59  ? 1.553   45.611  -6.721  0.00 59.01  ? 911  LYS   A CD  1 
ATOM   478  C  CE  . LYS   A 1 59  ? 1.857   45.036  -8.100  0.00 61.99  ? 911  LYS   A CE  1 
ATOM   479  N  NZ  . LYS   A 1 59  ? 3.257   44.540  -8.199  0.00 63.93  ? 911  LYS   A NZ  1 
ATOM   480  N  N   . ASN   A 1 65  ? -9.264  40.425  0.417   1.00 82.70  ? 917  ASN   A N   1 
ATOM   481  C  CA  . ASN   A 1 65  ? -10.057 41.556  0.906   1.00 78.61  ? 917  ASN   A CA  1 
ATOM   482  C  C   . ASN   A 1 65  ? -9.215  42.590  1.665   1.00 72.89  ? 917  ASN   A C   1 
ATOM   483  O  O   . ASN   A 1 65  ? -9.620  43.096  2.715   1.00 73.81  ? 917  ASN   A O   1 
ATOM   484  C  CB  . ASN   A 1 65  ? -11.225 41.049  1.771   1.00 81.71  ? 917  ASN   A CB  1 
ATOM   485  C  CG  . ASN   A 1 65  ? -10.785 40.196  2.981   0.00 83.94  ? 917  ASN   A CG  1 
ATOM   486  O  OD1 . ASN   A 1 65  ? -9.662  39.691  3.023   0.00 84.26  ? 917  ASN   A OD1 1 
ATOM   487  N  ND2 . ASN   A 1 65  ? -11.674 40.041  3.956   0.00 85.39  ? 917  ASN   A ND2 1 
ATOM   488  N  N   . HIS   A 1 66  ? -8.048  42.912  1.104   1.00 68.01  ? 918  HIS   A N   1 
ATOM   489  C  CA  . HIS   A 1 66  ? -7.146  43.926  1.663   1.00 60.80  ? 918  HIS   A CA  1 
ATOM   490  C  C   . HIS   A 1 66  ? -7.629  45.361  1.375   1.00 55.19  ? 918  HIS   A C   1 
ATOM   491  O  O   . HIS   A 1 66  ? -7.064  46.322  1.912   1.00 49.48  ? 918  HIS   A O   1 
ATOM   492  C  CB  . HIS   A 1 66  ? -5.724  43.735  1.122   1.00 60.14  ? 918  HIS   A CB  1 
ATOM   493  C  CG  . HIS   A 1 66  ? -5.143  42.376  1.362   0.00 64.00  ? 918  HIS   A CG  1 
ATOM   494  N  ND1 . HIS   A 1 66  ? -4.702  41.972  2.603   0.00 64.27  ? 918  HIS   A ND1 1 
ATOM   495  C  CD2 . HIS   A 1 66  ? -4.932  41.329  0.529   0.00 67.17  ? 918  HIS   A CD2 1 
ATOM   496  C  CE1 . HIS   A 1 66  ? -4.248  40.734  2.526   0.00 67.57  ? 918  HIS   A CE1 1 
ATOM   497  N  NE2 . HIS   A 1 66  ? -4.375  40.321  1.277   0.00 69.46  ? 918  HIS   A NE2 1 
ATOM   498  N  N   . ILE   A 1 67  ? -8.647  45.495  0.513   1.00 52.81  ? 919  ILE   A N   1 
ATOM   499  C  CA  . ILE   A 1 67  ? -9.411  46.744  0.342   1.00 48.39  ? 919  ILE   A CA  1 
ATOM   500  C  C   . ILE   A 1 67  ? -9.931  47.219  1.699   1.00 43.57  ? 919  ILE   A C   1 
ATOM   501  O  O   . ILE   A 1 67  ? -9.885  48.413  2.002   1.00 37.85  ? 919  ILE   A O   1 
ATOM   502  C  CB  . ILE   A 1 67  ? -10.609 46.583  -0.669  1.00 51.57  ? 919  ILE   A CB  1 
ATOM   503  C  CG1 . ILE   A 1 67  ? -10.106 46.154  -2.057  1.00 56.45  ? 919  ILE   A CG1 1 
ATOM   504  C  CG2 . ILE   A 1 67  ? -11.425 47.890  -0.805  1.00 52.03  ? 919  ILE   A CG2 1 
ATOM   505  C  CD1 . ILE   A 1 67  ? -10.243 44.704  -2.419  0.00 59.71  ? 919  ILE   A CD1 1 
ATOM   506  N  N   . ALA   A 1 68  ? -10.421 46.282  2.507   1.00 42.22  ? 920  ALA   A N   1 
ATOM   507  C  CA  . ALA   A 1 68  ? -10.878 46.586  3.867   1.00 42.47  ? 920  ALA   A CA  1 
ATOM   508  C  C   . ALA   A 1 68  ? -9.775  47.202  4.746   1.00 40.90  ? 920  ALA   A C   1 
ATOM   509  O  O   . ALA   A 1 68  ? -10.018 48.185  5.443   1.00 39.55  ? 920  ALA   A O   1 
ATOM   510  C  CB  . ALA   A 1 68  ? -11.440 45.342  4.529   1.00 46.71  ? 920  ALA   A CB  1 
ATOM   511  N  N   . ASP   A 1 69  ? -8.574  46.625  4.707   1.00 39.34  ? 921  ASP   A N   1 
ATOM   512  C  CA  . ASP   A 1 69  ? -7.435  47.180  5.451   1.00 37.78  ? 921  ASP   A CA  1 
ATOM   513  C  C   . ASP   A 1 69  ? -7.056  48.581  4.960   1.00 32.98  ? 921  ASP   A C   1 
ATOM   514  O  O   . ASP   A 1 69  ? -6.778  49.470  5.773   1.00 31.84  ? 921  ASP   A O   1 
ATOM   515  C  CB  . ASP   A 1 69  ? -6.208  46.263  5.370   1.00 39.29  ? 921  ASP   A CB  1 
ATOM   516  C  CG  . ASP   A 1 69  ? -6.419  44.921  6.066   1.00 47.15  ? 921  ASP   A CG  1 
ATOM   517  O  OD1 . ASP   A 1 69  ? -7.213  44.844  7.032   1.00 48.83  ? 921  ASP   A OD1 1 
ATOM   518  O  OD2 . ASP   A 1 69  ? -5.769  43.939  5.644   1.00 44.76  ? 921  ASP   A OD2 1 
ATOM   519  N  N   . LEU   A 1 70  ? -7.033  48.779  3.643   1.00 31.16  ? 922  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 70  ? -6.723  50.101  3.107   1.00 30.25  ? 922  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 70  ? -7.761  51.136  3.561   1.00 28.46  ? 922  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 70  ? -7.421  52.290  3.824   1.00 29.40  ? 922  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 70  ? -6.636  50.084  1.580   1.00 31.35  ? 922  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 70  ? -6.338  51.423  0.907   1.00 29.97  ? 922  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 70  ? -4.995  51.986  1.381   1.00 27.51  ? 922  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 70  ? -6.372  51.253  -0.603  1.00 35.83  ? 922  LEU   A CD2 1 
ATOM   527  N  N   . LYS   A 1 71  ? -9.024  50.715  3.628   1.00 29.37  ? 923  LYS   A N   1 
ATOM   528  C  CA  . LYS   A 1 71  ? -10.104 51.596  4.064   1.00 28.59  ? 923  LYS   A CA  1 
ATOM   529  C  C   . LYS   A 1 71  ? -9.919  52.031  5.511   1.00 26.69  ? 923  LYS   A C   1 
ATOM   530  O  O   . LYS   A 1 71  ? -10.097 53.199  5.819   1.00 24.64  ? 923  LYS   A O   1 
ATOM   531  C  CB  . LYS   A 1 71  ? -11.477 50.940  3.851   1.00 33.61  ? 923  LYS   A CB  1 
ATOM   532  C  CG  . LYS   A 1 71  ? -11.945 51.009  2.411   1.00 39.20  ? 923  LYS   A CG  1 
ATOM   533  C  CD  . LYS   A 1 71  ? -13.212 50.186  2.204   1.00 46.75  ? 923  LYS   A CD  1 
ATOM   534  C  CE  . LYS   A 1 71  ? -13.926 50.589  0.927   1.00 51.97  ? 923  LYS   A CE  1 
ATOM   535  N  NZ  . LYS   A 1 71  ? -13.059 50.580  -0.275  0.00 49.64  ? 923  LYS   A NZ  1 
ATOM   536  N  N   . LYS   A 1 72  ? -9.505  51.109  6.384   1.00 31.47  ? 924  LYS   A N   1 
ATOM   537  C  CA  . LYS   A 1 72  ? -9.238  51.435  7.785   1.00 30.35  ? 924  LYS   A CA  1 
ATOM   538  C  C   . LYS   A 1 72  ? -8.020  52.363  7.932   1.00 27.74  ? 924  LYS   A C   1 
ATOM   539  O  O   . LYS   A 1 72  ? -8.052  53.306  8.724   1.00 28.56  ? 924  LYS   A O   1 
ATOM   540  C  CB  . LYS   A 1 72  ? -9.066  50.170  8.640   1.00 34.38  ? 924  LYS   A CB  1 
ATOM   541  C  CG  . LYS   A 1 72  ? -10.322 49.332  8.728   1.00 41.59  ? 924  LYS   A CG  1 
ATOM   542  C  CD  . LYS   A 1 72  ? -10.219 48.180  9.755   1.00 51.50  ? 924  LYS   A CD  1 
ATOM   543  C  CE  . LYS   A 1 72  ? -10.874 48.529  11.093  1.00 58.15  ? 924  LYS   A CE  1 
ATOM   544  N  NZ  . LYS   A 1 72  ? -10.262 49.720  11.739  0.00 53.36  ? 924  LYS   A NZ  1 
ATOM   545  N  N   . GLU   A 1 73  ? -6.959  52.088  7.167   1.00 27.16  ? 925  GLU   A N   1 
ATOM   546  C  CA  . GLU   A 1 73  ? -5.782  52.943  7.097   1.00 24.01  ? 925  GLU   A CA  1 
ATOM   547  C  C   . GLU   A 1 73  ? -6.115  54.369  6.686   1.00 20.81  ? 925  GLU   A C   1 
ATOM   548  O  O   . GLU   A 1 73  ? -5.634  55.320  7.324   1.00 23.46  ? 925  GLU   A O   1 
ATOM   549  C  CB  . GLU   A 1 73  ? -4.779  52.370  6.092   1.00 25.75  ? 925  GLU   A CB  1 
ATOM   550  C  CG  . GLU   A 1 73  ? -3.459  53.128  6.023   1.00 22.08  ? 925  GLU   A CG  1 
ATOM   551  C  CD  . GLU   A 1 73  ? -2.472  52.520  5.032   1.00 27.56  ? 925  GLU   A CD  1 
ATOM   552  O  OE1 . GLU   A 1 73  ? -2.734  51.429  4.472   1.00 25.47  ? 925  GLU   A OE1 1 
ATOM   553  O  OE2 . GLU   A 1 73  ? -1.420  53.158  4.820   1.00 28.96  ? 925  GLU   A OE2 1 
ATOM   554  N  N   . ILE   A 1 74  ? -6.905  54.510  5.609   1.00 22.18  ? 926  ILE   A N   1 
ATOM   555  C  CA  . ILE   A 1 74  ? -7.359  55.822  5.127   1.00 20.59  ? 926  ILE   A CA  1 
ATOM   556  C  C   . ILE   A 1 74  ? -8.050  56.578  6.263   1.00 20.68  ? 926  ILE   A C   1 
ATOM   557  O  O   . ILE   A 1 74  ? -7.819  57.755  6.492   1.00 20.22  ? 926  ILE   A O   1 
ATOM   558  C  CB  . ILE   A 1 74  ? -8.322  55.707  3.886   1.00 20.89  ? 926  ILE   A CB  1 
ATOM   559  C  CG1 . ILE   A 1 74  ? -7.526  55.367  2.636   1.00 24.54  ? 926  ILE   A CG1 1 
ATOM   560  C  CG2 . ILE   A 1 74  ? -9.078  57.033  3.622   1.00 18.51  ? 926  ILE   A CG2 1 
ATOM   561  C  CD1 . ILE   A 1 74  ? -8.332  54.865  1.486   1.00 24.18  ? 926  ILE   A CD1 1 
ATOM   562  N  N   . GLU   A 1 75  ? -8.912  55.884  6.980   1.00 22.87  ? 927  GLU   A N   1 
ATOM   563  C  CA  . GLU   A 1 75  ? -9.715  56.522  8.000   1.00 22.39  ? 927  GLU   A CA  1 
ATOM   564  C  C   . GLU   A 1 75  ? -8.863  56.888  9.243   1.00 23.70  ? 927  GLU   A C   1 
ATOM   565  O  O   . GLU   A 1 75  ? -9.115  57.901  9.899   1.00 22.85  ? 927  GLU   A O   1 
ATOM   566  C  CB  . GLU   A 1 75  ? -10.891 55.609  8.335   1.00 26.42  ? 927  GLU   A CB  1 
ATOM   567  C  CG  . GLU   A 1 75  ? -11.906 56.207  9.238   1.00 30.88  ? 927  GLU   A CG  1 
ATOM   568  C  CD  . GLU   A 1 75  ? -12.520 57.500  8.718   1.00 22.65  ? 927  GLU   A CD  1 
ATOM   569  O  OE1 . GLU   A 1 75  ? -12.408 57.822  7.519   1.00 25.84  ? 927  GLU   A OE1 1 
ATOM   570  O  OE2 . GLU   A 1 75  ? -13.117 58.221  9.542   1.00 31.75  ? 927  GLU   A OE2 1 
ATOM   571  N  N   . ILE   A 1 76  ? -7.858  56.068  9.557   1.00 24.36  ? 928  ILE   A N   1 
ATOM   572  C  CA  . ILE   A 1 76  ? -6.876  56.409  10.590  1.00 22.32  ? 928  ILE   A CA  1 
ATOM   573  C  C   . ILE   A 1 76  ? -6.157  57.712  10.208  1.00 22.94  ? 928  ILE   A C   1 
ATOM   574  O  O   . ILE   A 1 76  ? -6.154  58.672  10.988  1.00 21.98  ? 928  ILE   A O   1 
ATOM   575  C  CB  . ILE   A 1 76  ? -5.820  55.283  10.812  1.00 22.52  ? 928  ILE   A CB  1 
ATOM   576  C  CG1 . ILE   A 1 76  ? -6.459  54.096  11.536  1.00 28.02  ? 928  ILE   A CG1 1 
ATOM   577  C  CG2 . ILE   A 1 76  ? -4.657  55.781  11.669  1.00 23.65  ? 928  ILE   A CG2 1 
ATOM   578  C  CD1 . ILE   A 1 76  ? -5.657  52.786  11.475  1.00 29.20  ? 928  ILE   A CD1 1 
ATOM   579  N  N   . LEU   A 1 77  ? -5.573  57.736  9.008   1.00 19.87  ? 929  LEU   A N   1 
ATOM   580  C  CA  . LEU   A 1 77  ? -4.763  58.883  8.583   1.00 19.34  ? 929  LEU   A CA  1 
ATOM   581  C  C   . LEU   A 1 77  ? -5.565  60.177  8.428   1.00 20.07  ? 929  LEU   A C   1 
ATOM   582  O  O   . LEU   A 1 77  ? -5.058  61.237  8.770   1.00 21.76  ? 929  LEU   A O   1 
ATOM   583  C  CB  . LEU   A 1 77  ? -3.979  58.584  7.304   1.00 18.36  ? 929  LEU   A CB  1 
ATOM   584  C  CG  . LEU   A 1 77  ? -2.898  59.612  6.939   1.00 14.15  ? 929  LEU   A CG  1 
ATOM   585  C  CD1 . LEU   A 1 77  ? -1.887  59.853  8.087   1.00 19.22  ? 929  LEU   A CD1 1 
ATOM   586  C  CD2 . LEU   A 1 77  ? -2.172  59.188  5.660   1.00 20.67  ? 929  LEU   A CD2 1 
ATOM   587  N  N   . ARG   A 1 78  ? -6.810  60.059  7.953   1.00 23.74  ? 930  ARG   A N   1 
ATOM   588  C  CA  . ARG   A 1 78  ? -7.763  61.177  7.829   1.00 22.40  ? 930  ARG   A CA  1 
ATOM   589  C  C   . ARG   A 1 78  ? -7.892  62.002  9.113   1.00 23.95  ? 930  ARG   A C   1 
ATOM   590  O  O   . ARG   A 1 78  ? -8.038  63.238  9.064   1.00 25.79  ? 930  ARG   A O   1 
ATOM   591  C  CB  . ARG   A 1 78  ? -9.132  60.652  7.407   1.00 26.33  ? 930  ARG   A CB  1 
ATOM   592  C  CG  . ARG   A 1 78  ? -10.092 61.730  6.963   1.00 27.45  ? 930  ARG   A CG  1 
ATOM   593  C  CD  . ARG   A 1 78  ? -11.324 61.134  6.322   1.00 28.98  ? 930  ARG   A CD  1 
ATOM   594  N  NE  . ARG   A 1 78  ? -12.297 60.756  7.343   1.00 24.43  ? 930  ARG   A NE  1 
ATOM   595  C  CZ  . ARG   A 1 78  ? -13.078 61.613  7.993   1.00 28.67  ? 930  ARG   A CZ  1 
ATOM   596  N  NH1 . ARG   A 1 78  ? -13.945 61.171  8.890   1.00 34.89  ? 930  ARG   A NH1 1 
ATOM   597  N  NH2 . ARG   A 1 78  ? -13.006 62.917  7.734   1.00 28.04  ? 930  ARG   A NH2 1 
ATOM   598  N  N   . ASN   A 1 79  ? -7.830  61.321  10.253  1.00 24.99  ? 931  ASN   A N   1 
ATOM   599  C  CA  . ASN   A 1 79  ? -8.022  61.948  11.562  1.00 25.21  ? 931  ASN   A CA  1 
ATOM   600  C  C   . ASN   A 1 79  ? -6.768  62.186  12.371  1.00 25.14  ? 931  ASN   A C   1 
ATOM   601  O  O   . ASN   A 1 79  ? -6.873  62.607  13.525  1.00 25.39  ? 931  ASN   A O   1 
ATOM   602  C  CB  . ASN   A 1 79  ? -9.003  61.092  12.360  1.00 30.03  ? 931  ASN   A CB  1 
ATOM   603  C  CG  . ASN   A 1 79  ? -10.375 61.081  11.734  1.00 32.48  ? 931  ASN   A CG  1 
ATOM   604  O  OD1 . ASN   A 1 79  ? -11.023 62.131  11.614  1.00 39.12  ? 931  ASN   A OD1 1 
ATOM   605  N  ND2 . ASN   A 1 79  ? -10.805 59.912  11.272  1.00 28.92  ? 931  ASN   A ND2 1 
ATOM   606  N  N   . LEU   A 1 80  ? -5.592  61.919  11.789  1.00 24.46  ? 932  LEU   A N   1 
ATOM   607  C  CA  . LEU   A 1 80  ? -4.319  62.258  12.415  1.00 23.76  ? 932  LEU   A CA  1 
ATOM   608  C  C   . LEU   A 1 80  ? -3.870  63.621  11.899  1.00 24.77  ? 932  LEU   A C   1 
ATOM   609  O  O   . LEU   A 1 80  ? -3.825  63.834  10.678  1.00 22.61  ? 932  LEU   A O   1 
ATOM   610  C  CB  . LEU   A 1 80  ? -3.238  61.200  12.140  1.00 21.01  ? 932  LEU   A CB  1 
ATOM   611  C  CG  . LEU   A 1 80  ? -3.490  59.781  12.676  1.00 23.43  ? 932  LEU   A CG  1 
ATOM   612  C  CD1 . LEU   A 1 80  ? -2.429  58.829  12.174  1.00 23.72  ? 932  LEU   A CD1 1 
ATOM   613  C  CD2 . LEU   A 1 80  ? -3.561  59.730  14.202  1.00 27.31  ? 932  LEU   A CD2 1 
ATOM   614  N  N   . TYR   A 1 81  ? -3.594  64.532  12.838  1.00 24.96  ? 933  TYR   A N   1 
ATOM   615  C  CA  . TYR   A 1 81  ? -3.134  65.896  12.554  1.00 26.68  ? 933  TYR   A CA  1 
ATOM   616  C  C   . TYR   A 1 81  ? -1.921  66.194  13.412  1.00 21.85  ? 933  TYR   A C   1 
ATOM   617  O  O   . TYR   A 1 81  ? -2.065  66.514  14.578  1.00 22.67  ? 933  TYR   A O   1 
ATOM   618  C  CB  . TYR   A 1 81  ? -4.218  66.925  12.904  1.00 31.92  ? 933  TYR   A CB  1 
ATOM   619  C  CG  . TYR   A 1 81  ? -5.480  66.826  12.115  1.00 37.89  ? 933  TYR   A CG  1 
ATOM   620  C  CD1 . TYR   A 1 81  ? -5.657  67.583  10.947  1.00 47.34  ? 933  TYR   A CD1 1 
ATOM   621  C  CD2 . TYR   A 1 81  ? -6.530  66.007  12.545  1.00 45.65  ? 933  TYR   A CD2 1 
ATOM   622  C  CE1 . TYR   A 1 81  ? -6.847  67.507  10.210  1.00 45.42  ? 933  TYR   A CE1 1 
ATOM   623  C  CE2 . TYR   A 1 81  ? -7.716  65.918  11.817  1.00 43.89  ? 933  TYR   A CE2 1 
ATOM   624  C  CZ  . TYR   A 1 81  ? -7.863  66.665  10.651  1.00 47.52  ? 933  TYR   A CZ  1 
ATOM   625  O  OH  . TYR   A 1 81  ? -9.028  66.581  9.939   1.00 52.90  ? 933  TYR   A OH  1 
ATOM   626  N  N   . HIS   A 1 82  ? -0.732  66.108  12.831  1.00 21.44  ? 934  HIS   A N   1 
ATOM   627  C  CA  . HIS   A 1 82  ? 0.519   66.366  13.563  1.00 17.28  ? 934  HIS   A CA  1 
ATOM   628  C  C   . HIS   A 1 82  ? 1.660   66.739  12.588  1.00 14.96  ? 934  HIS   A C   1 
ATOM   629  O  O   . HIS   A 1 82  ? 1.724   66.236  11.446  1.00 17.71  ? 934  HIS   A O   1 
ATOM   630  C  CB  . HIS   A 1 82  ? 0.886   65.133  14.391  1.00 19.20  ? 934  HIS   A CB  1 
ATOM   631  C  CG  . HIS   A 1 82  ? 1.938   65.379  15.431  1.00 15.65  ? 934  HIS   A CG  1 
ATOM   632  N  ND1 . HIS   A 1 82  ? 3.289   65.358  15.149  1.00 16.62  ? 934  HIS   A ND1 1 
ATOM   633  C  CD2 . HIS   A 1 82  ? 1.836   65.671  16.750  1.00 22.39  ? 934  HIS   A CD2 1 
ATOM   634  C  CE1 . HIS   A 1 82  ? 3.970   65.608  16.253  1.00 21.37  ? 934  HIS   A CE1 1 
ATOM   635  N  NE2 . HIS   A 1 82  ? 3.109   65.810  17.237  1.00 21.69  ? 934  HIS   A NE2 1 
ATOM   636  N  N   . GLU   A 1 83  ? 2.513   67.661  13.033  1.00 19.38  ? 935  GLU   A N   1 
ATOM   637  C  CA  . GLU   A 1 83  ? 3.643   68.193  12.264  1.00 21.62  ? 935  GLU   A CA  1 
ATOM   638  C  C   . GLU   A 1 83  ? 4.590   67.093  11.759  1.00 18.67  ? 935  GLU   A C   1 
ATOM   639  O  O   . GLU   A 1 83  ? 5.221   67.214  10.712  1.00 19.32  ? 935  GLU   A O   1 
ATOM   640  C  CB  . GLU   A 1 83  ? 4.427   69.160  13.165  1.00 24.78  ? 935  GLU   A CB  1 
ATOM   641  C  CG  . GLU   A 1 83  ? 5.607   69.838  12.512  1.00 38.80  ? 935  GLU   A CG  1 
ATOM   642  C  CD  . GLU   A 1 83  ? 6.184   70.974  13.348  1.00 45.66  ? 935  GLU   A CD  1 
ATOM   643  O  OE1 . GLU   A 1 83  ? 6.101   70.907  14.593  1.00 50.72  ? 935  GLU   A OE1 1 
ATOM   644  O  OE2 . GLU   A 1 83  ? 6.729   71.931  12.752  1.00 57.08  ? 935  GLU   A OE2 1 
ATOM   645  N  N   . ASN   A 1 84  ? 4.718   66.047  12.566  1.00 17.15  ? 936  ASN   A N   1 
ATOM   646  C  CA  . ASN   A 1 84  ? 5.555   64.901  12.241  1.00 14.85  ? 936  ASN   A CA  1 
ATOM   647  C  C   . ASN   A 1 84  ? 4.814   63.659  11.748  1.00 15.68  ? 936  ASN   A C   1 
ATOM   648  O  O   . ASN   A 1 84  ? 5.347   62.568  11.854  1.00 13.11  ? 936  ASN   A O   1 
ATOM   649  C  CB  . ASN   A 1 84  ? 6.404   64.573  13.467  1.00 16.60  ? 936  ASN   A CB  1 
ATOM   650  C  CG  . ASN   A 1 84  ? 7.201   65.782  13.947  1.00 19.18  ? 936  ASN   A CG  1 
ATOM   651  O  OD1 . ASN   A 1 84  ? 7.081   66.192  15.109  1.00 20.53  ? 936  ASN   A OD1 1 
ATOM   652  N  ND2 . ASN   A 1 84  ? 8.021   66.342  13.072  1.00 14.69  ? 936  ASN   A ND2 1 
ATOM   653  N  N   A ILE   A 1 85  ? 3.599   63.845  11.231  0.50 15.05  ? 937  ILE   A N   1 
ATOM   654  N  N   B ILE   A 1 85  ? 3.611   63.853  11.206  0.50 14.89  ? 937  ILE   A N   1 
ATOM   655  C  CA  A ILE   A 1 85  ? 2.850   62.798  10.547  0.50 16.19  ? 937  ILE   A CA  1 
ATOM   656  C  CA  B ILE   A 1 85  ? 2.837   62.802  10.559  0.50 15.96  ? 937  ILE   A CA  1 
ATOM   657  C  C   A ILE   A 1 85  ? 2.466   63.318  9.171   0.50 14.68  ? 937  ILE   A C   1 
ATOM   658  C  C   B ILE   A 1 85  ? 2.447   63.309  9.176   0.50 14.39  ? 937  ILE   A C   1 
ATOM   659  O  O   A ILE   A 1 85  ? 1.958   64.432  9.034   0.50 13.83  ? 937  ILE   A O   1 
ATOM   660  O  O   B ILE   A 1 85  ? 1.912   64.411  9.040   0.50 13.34  ? 937  ILE   A O   1 
ATOM   661  C  CB  A ILE   A 1 85  ? 1.588   62.389  11.337  0.50 17.18  ? 937  ILE   A CB  1 
ATOM   662  C  CB  B ILE   A 1 85  ? 1.555   62.471  11.359  0.50 16.88  ? 937  ILE   A CB  1 
ATOM   663  C  CG1 A ILE   A 1 85  ? 2.028   61.664  12.617  0.50 20.22  ? 937  ILE   A CG1 1 
ATOM   664  C  CG1 B ILE   A 1 85  ? 1.904   61.996  12.784  0.50 19.14  ? 937  ILE   A CG1 1 
ATOM   665  C  CG2 A ILE   A 1 85  ? 0.608   61.542  10.451  0.50 17.08  ? 937  ILE   A CG2 1 
ATOM   666  C  CG2 B ILE   A 1 85  ? 0.673   61.450  10.611  0.50 17.46  ? 937  ILE   A CG2 1 
ATOM   667  C  CD1 A ILE   A 1 85  ? 0.927   61.009  13.390  0.50 21.68  ? 937  ILE   A CD1 1 
ATOM   668  C  CD1 B ILE   A 1 85  ? 2.702   60.733  12.884  0.50 21.26  ? 937  ILE   A CD1 1 
ATOM   669  N  N   . VAL   A 1 86  ? 2.703   62.498  8.153   1.00 15.89  ? 938  VAL   A N   1 
ATOM   670  C  CA  . VAL   A 1 86  ? 2.419   62.884  6.778   1.00 15.74  ? 938  VAL   A CA  1 
ATOM   671  C  C   . VAL   A 1 86  ? 0.943   63.287  6.581   1.00 16.96  ? 938  VAL   A C   1 
ATOM   672  O  O   . VAL   A 1 86  ? 0.044   62.704  7.198   1.00 16.18  ? 938  VAL   A O   1 
ATOM   673  C  CB  . VAL   A 1 86  ? 2.817   61.764  5.782   1.00 15.83  ? 938  VAL   A CB  1 
ATOM   674  C  CG1 . VAL   A 1 86  ? 1.898   60.567  5.912   1.00 15.47  ? 938  VAL   A CG1 1 
ATOM   675  C  CG2 . VAL   A 1 86  ? 2.835   62.292  4.340   1.00 13.83  ? 938  VAL   A CG2 1 
ATOM   676  N  N   . LYS   A 1 87  ? 0.708   64.308  5.760   1.00 17.56  ? 939  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 87  ? -0.629  64.880  5.627   1.00 19.34  ? 939  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 87  ? -1.546  64.122  4.680   1.00 17.13  ? 939  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 87  ? -1.252  63.968  3.511   1.00 16.50  ? 939  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 87  ? -0.578  66.347  5.189   1.00 17.81  ? 939  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 87  ? -0.066  67.283  6.280   1.00 21.40  ? 939  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 87  ? -0.014  68.709  5.777   1.00 34.40  ? 939  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 87  ? 0.305   69.682  6.894   1.00 36.52  ? 939  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 87  ? 0.416   71.066  6.363   1.00 38.77  ? 939  LYS   A NZ  1 
ATOM   685  N  N   . TYR   A 1 88  ? -2.678  63.679  5.208   1.00 17.17  ? 940  TYR   A N   1 
ATOM   686  C  CA  . TYR   A 1 88  ? -3.819  63.287  4.403   1.00 16.64  ? 940  TYR   A CA  1 
ATOM   687  C  C   . TYR   A 1 88  ? -4.310  64.457  3.543   1.00 16.38  ? 940  TYR   A C   1 
ATOM   688  O  O   . TYR   A 1 88  ? -4.470  65.577  4.028   1.00 16.60  ? 940  TYR   A O   1 
ATOM   689  C  CB  . TYR   A 1 88  ? -4.957  62.837  5.327   1.00 19.04  ? 940  TYR   A CB  1 
ATOM   690  C  CG  . TYR   A 1 88  ? -6.267  62.521  4.664   1.00 16.89  ? 940  TYR   A CG  1 
ATOM   691  C  CD1 . TYR   A 1 88  ? -6.536  61.230  4.195   1.00 18.44  ? 940  TYR   A CD1 1 
ATOM   692  C  CD2 . TYR   A 1 88  ? -7.274  63.489  4.544   1.00 20.06  ? 940  TYR   A CD2 1 
ATOM   693  C  CE1 . TYR   A 1 88  ? -7.707  60.923  3.594   1.00 20.92  ? 940  TYR   A CE1 1 
ATOM   694  C  CE2 . TYR   A 1 88  ? -8.485  63.185  3.945   1.00 18.09  ? 940  TYR   A CE2 1 
ATOM   695  C  CZ  . TYR   A 1 88  ? -8.705  61.875  3.482   1.00 22.91  ? 940  TYR   A CZ  1 
ATOM   696  O  OH  . TYR   A 1 88  ? -9.886  61.508  2.881   1.00 18.09  ? 940  TYR   A OH  1 
ATOM   697  N  N   . LYS   A 1 89  ? -4.551  64.182  2.266   1.00 16.64  ? 941  LYS   A N   1 
ATOM   698  C  CA  . LYS   A 1 89  ? -5.198  65.149  1.350   1.00 17.26  ? 941  LYS   A CA  1 
ATOM   699  C  C   . LYS   A 1 89  ? -6.592  64.675  0.938   1.00 19.19  ? 941  LYS   A C   1 
ATOM   700  O  O   . LYS   A 1 89  ? -7.520  65.491  0.818   1.00 18.12  ? 941  LYS   A O   1 
ATOM   701  C  CB  . LYS   A 1 89  ? -4.325  65.392  0.117   1.00 18.84  ? 941  LYS   A CB  1 
ATOM   702  C  CG  . LYS   A 1 89  ? -3.066  66.171  0.478   1.00 20.11  ? 941  LYS   A CG  1 
ATOM   703  C  CD  . LYS   A 1 89  ? -2.138  66.396  -0.705  1.00 24.58  ? 941  LYS   A CD  1 
ATOM   704  C  CE  . LYS   A 1 89  ? -2.529  67.594  -1.551  1.00 28.06  ? 941  LYS   A CE  1 
ATOM   705  N  NZ  . LYS   A 1 89  ? -2.463  68.918  -0.833  1.00 25.16  ? 941  LYS   A NZ  1 
ATOM   706  N  N   . GLY   A 1 90  ? -6.760  63.372  0.713   1.00 18.33  ? 942  GLY   A N   1 
ATOM   707  C  CA  . GLY   A 1 90  ? -8.069  62.848  0.363   1.00 16.40  ? 942  GLY   A CA  1 
ATOM   708  C  C   . GLY   A 1 90  ? -8.094  61.447  -0.196  1.00 17.34  ? 942  GLY   A C   1 
ATOM   709  O  O   . GLY   A 1 90  ? -7.186  60.637  0.078   1.00 19.11  ? 942  GLY   A O   1 
ATOM   710  N  N   . ILE   A 1 91  ? -9.129  61.192  -0.994  1.00 20.73  ? 943  ILE   A N   1 
ATOM   711  C  CA  . ILE   A 1 91  ? -9.346  59.887  -1.635  1.00 19.30  ? 943  ILE   A CA  1 
ATOM   712  C  C   . ILE   A 1 91  ? -9.728  60.029  -3.083  1.00 20.27  ? 943  ILE   A C   1 
ATOM   713  O  O   . ILE   A 1 91  ? -10.288 61.043  -3.489  1.00 19.46  ? 943  ILE   A O   1 
ATOM   714  C  CB  . ILE   A 1 91  ? -10.420 59.032  -0.915  1.00 19.74  ? 943  ILE   A CB  1 
ATOM   715  C  CG1 . ILE   A 1 91  ? -11.732 59.816  -0.728  1.00 22.00  ? 943  ILE   A CG1 1 
ATOM   716  C  CG2 . ILE   A 1 91  ? -9.875  58.552  0.432   1.00 19.87  ? 943  ILE   A CG2 1 
ATOM   717  C  CD1 . ILE   A 1 91  ? -12.883 58.985  -0.219  1.00 27.52  ? 943  ILE   A CD1 1 
ATOM   718  N  N   . CYS   A 1 92  ? -9.446  58.977  -3.841  1.00 24.07  ? 944  CYS   A N   1 
ATOM   719  C  CA  . CYS   A 1 92  ? -9.982  58.813  -5.187  1.00 25.19  ? 944  CYS   A CA  1 
ATOM   720  C  C   . CYS   A 1 92  ? -10.765 57.502  -5.174  1.00 26.97  ? 944  CYS   A C   1 
ATOM   721  O  O   . CYS   A 1 92  ? -10.182 56.462  -4.943  1.00 28.21  ? 944  CYS   A O   1 
ATOM   722  C  CB  . CYS   A 1 92  ? -8.855  58.756  -6.205  1.00 25.75  ? 944  CYS   A CB  1 
ATOM   723  S  SG  . CYS   A 1 92  ? -9.439  58.346  -7.835  1.00 29.33  ? 944  CYS   A SG  1 
ATOM   724  N  N   . THR   A 1 93  ? -12.075 57.578  -5.376  1.00 32.16  ? 945  THR   A N   1 
ATOM   725  C  CA  . THR   A 1 93  ? -12.957 56.393  -5.364  1.00 37.44  ? 945  THR   A CA  1 
ATOM   726  C  C   . THR   A 1 93  ? -13.331 55.964  -6.778  1.00 41.30  ? 945  THR   A C   1 
ATOM   727  O  O   . THR   A 1 93  ? -13.824 56.767  -7.564  1.00 45.68  ? 945  THR   A O   1 
ATOM   728  C  CB  . THR   A 1 93  ? -14.245 56.644  -4.546  1.00 38.82  ? 945  THR   A CB  1 
ATOM   729  O  OG1 . THR   A 1 93  ? -14.773 57.944  -4.853  1.00 41.63  ? 945  THR   A OG1 1 
ATOM   730  C  CG2 . THR   A 1 93  ? -13.960 56.563  -3.079  1.00 36.45  ? 945  THR   A CG2 1 
ATOM   731  N  N   . ASN   A 1 98  ? -16.454 50.332  -5.148  1.00 58.86  ? 950  ASN   A N   1 
ATOM   732  C  CA  . ASN   A 1 98  ? -15.766 49.433  -4.213  1.00 58.62  ? 950  ASN   A CA  1 
ATOM   733  C  C   . ASN   A 1 98  ? -14.298 49.811  -3.947  1.00 55.58  ? 950  ASN   A C   1 
ATOM   734  O  O   . ASN   A 1 98  ? -13.850 49.815  -2.791  1.00 55.26  ? 950  ASN   A O   1 
ATOM   735  C  CB  . ASN   A 1 98  ? -15.848 47.988  -4.713  1.00 63.53  ? 950  ASN   A CB  1 
ATOM   736  C  CG  . ASN   A 1 98  ? -15.429 47.785  -6.152  0.00 63.77  ? 950  ASN   A CG  1 
ATOM   737  O  OD1 . ASN   A 1 98  ? -15.122 48.741  -6.867  0.00 61.77  ? 950  ASN   A OD1 1 
ATOM   738  N  ND2 . ASN   A 1 98  ? -15.402 46.531  -6.589  0.00 67.12  ? 950  ASN   A ND2 1 
ATOM   739  N  N   . GLY   A 1 99  ? -13.566 50.126  -5.019  1.00 50.28  ? 951  GLY   A N   1 
ATOM   740  C  CA  . GLY   A 1 99  ? -12.147 50.452  -4.937  1.00 44.88  ? 951  GLY   A CA  1 
ATOM   741  C  C   . GLY   A 1 99  ? -11.894 51.863  -4.414  1.00 40.15  ? 951  GLY   A C   1 
ATOM   742  O  O   . GLY   A 1 99  ? -12.810 52.697  -4.363  1.00 40.27  ? 951  GLY   A O   1 
ATOM   743  N  N   . ILE   A 1 100 ? -10.645 52.131  -4.037  1.00 33.38  ? 952  ILE   A N   1 
ATOM   744  C  CA  . ILE   A 1 100 ? -10.281 53.415  -3.434  1.00 29.99  ? 952  ILE   A CA  1 
ATOM   745  C  C   . ILE   A 1 100 ? -8.763  53.629  -3.408  1.00 29.67  ? 952  ILE   A C   1 
ATOM   746  O  O   . ILE   A 1 100 ? -8.002  52.663  -3.281  1.00 29.06  ? 952  ILE   A O   1 
ATOM   747  C  CB  . ILE   A 1 100 ? -10.844 53.522  -1.981  1.00 30.45  ? 952  ILE   A CB  1 
ATOM   748  C  CG1 . ILE   A 1 100 ? -10.794 54.959  -1.478  1.00 29.13  ? 952  ILE   A CG1 1 
ATOM   749  C  CG2 . ILE   A 1 100 ? -10.113 52.578  -1.006  1.00 32.35  ? 952  ILE   A CG2 1 
ATOM   750  C  CD1 . ILE   A 1 100 ? -11.674 55.203  -0.252  1.00 35.31  ? 952  ILE   A CD1 1 
ATOM   751  N  N   . LYS   A 1 101 ? -8.344  54.894  -3.506  1.00 26.25  ? 953  LYS   A N   1 
ATOM   752  C  CA  . LYS   A 1 101 ? -6.935  55.281  -3.381  1.00 26.15  ? 953  LYS   A CA  1 
ATOM   753  C  C   . LYS   A 1 101 ? -6.770  56.338  -2.298  1.00 22.90  ? 953  LYS   A C   1 
ATOM   754  O  O   . LYS   A 1 101 ? -7.606  57.227  -2.186  1.00 22.24  ? 953  LYS   A O   1 
ATOM   755  C  CB  . LYS   A 1 101 ? -6.404  55.815  -4.701  1.00 23.63  ? 953  LYS   A CB  1 
ATOM   756  C  CG  . LYS   A 1 101 ? -6.478  54.778  -5.790  1.00 30.56  ? 953  LYS   A CG  1 
ATOM   757  C  CD  . LYS   A 1 101 ? -5.803  55.178  -7.068  1.00 30.55  ? 953  LYS   A CD  1 
ATOM   758  C  CE  . LYS   A 1 101 ? -5.750  53.957  -7.985  1.00 37.17  ? 953  LYS   A CE  1 
ATOM   759  N  NZ  . LYS   A 1 101 ? -5.306  54.254  -9.364  1.00 40.22  ? 953  LYS   A NZ  1 
ATOM   760  N  N   . LEU   A 1 102 ? -5.707  56.222  -1.499  1.00 23.56  ? 954  LEU   A N   1 
ATOM   761  C  CA  . LEU   A 1 102 ? -5.361  57.233  -0.501  1.00 19.79  ? 954  LEU   A CA  1 
ATOM   762  C  C   . LEU   A 1 102 ? -4.466  58.293  -1.142  1.00 20.45  ? 954  LEU   A C   1 
ATOM   763  O  O   . LEU   A 1 102 ? -3.398  57.954  -1.653  1.00 19.14  ? 954  LEU   A O   1 
ATOM   764  C  CB  . LEU   A 1 102 ? -4.614  56.590  0.676   1.00 20.59  ? 954  LEU   A CB  1 
ATOM   765  C  CG  . LEU   A 1 102 ? -3.965  57.473  1.746   1.00 20.33  ? 954  LEU   A CG  1 
ATOM   766  C  CD1 . LEU   A 1 102 ? -4.949  58.479  2.334   1.00 20.87  ? 954  LEU   A CD1 1 
ATOM   767  C  CD2 . LEU   A 1 102 ? -3.400  56.578  2.843   1.00 24.67  ? 954  LEU   A CD2 1 
ATOM   768  N  N   . ILE   A 1 103 ? -4.855  59.566  -1.042  1.00 19.02  ? 955  ILE   A N   1 
ATOM   769  C  CA  . ILE   A 1 103 ? -4.044  60.698  -1.552  1.00 19.17  ? 955  ILE   A CA  1 
ATOM   770  C  C   . ILE   A 1 103 ? -3.373  61.431  -0.373  1.00 18.95  ? 955  ILE   A C   1 
ATOM   771  O  O   . ILE   A 1 103 ? -4.058  61.876  0.535   1.00 18.89  ? 955  ILE   A O   1 
ATOM   772  C  CB  . ILE   A 1 103 ? -4.898  61.728  -2.346  1.00 18.96  ? 955  ILE   A CB  1 
ATOM   773  C  CG1 . ILE   A 1 103 ? -5.858  61.042  -3.344  1.00 21.22  ? 955  ILE   A CG1 1 
ATOM   774  C  CG2 . ILE   A 1 103 ? -4.002  62.781  -3.056  1.00 19.25  ? 955  ILE   A CG2 1 
ATOM   775  C  CD1 . ILE   A 1 103 ? -5.214  60.080  -4.300  1.00 21.82  ? 955  ILE   A CD1 1 
ATOM   776  N  N   . MET   A 1 104 ? -2.052  61.581  -0.435  1.00 17.26  ? 956  MET   A N   1 
ATOM   777  C  CA  . MET   A 1 104 ? -1.277  62.245  0.599   1.00 16.26  ? 956  MET   A CA  1 
ATOM   778  C  C   . MET   A 1 104 ? -0.391  63.324  -0.013  1.00 15.02  ? 956  MET   A C   1 
ATOM   779  O  O   . MET   A 1 104 ? -0.154  63.338  -1.225  1.00 15.29  ? 956  MET   A O   1 
ATOM   780  C  CB  . MET   A 1 104 ? -0.390  61.239  1.359   1.00 19.10  ? 956  MET   A CB  1 
ATOM   781  C  CG  . MET   A 1 104 ? -1.160  60.156  2.084   1.00 16.86  ? 956  MET   A CG  1 
ATOM   782  S  SD  . MET   A 1 104 ? -0.128  58.776  2.544   1.00 18.58  ? 956  MET   A SD  1 
ATOM   783  C  CE  . MET   A 1 104 ? -0.021  57.955  0.943   1.00 17.91  ? 956  MET   A CE  1 
ATOM   784  N  N   . GLU   A 1 105 ? 0.113   64.211  0.840   1.00 13.62  ? 957  GLU   A N   1 
ATOM   785  C  CA  . GLU   A 1 105 ? 1.166   65.130  0.410   1.00 13.69  ? 957  GLU   A CA  1 
ATOM   786  C  C   . GLU   A 1 105 ? 2.372   64.335  -0.049  1.00 16.44  ? 957  GLU   A C   1 
ATOM   787  O  O   . GLU   A 1 105 ? 2.599   63.215  0.428   1.00 16.94  ? 957  GLU   A O   1 
ATOM   788  C  CB  . GLU   A 1 105 ? 1.557   66.116  1.496   1.00 14.81  ? 957  GLU   A CB  1 
ATOM   789  C  CG  . GLU   A 1 105 ? 2.223   65.499  2.722   1.00 14.73  ? 957  GLU   A CG  1 
ATOM   790  C  CD  . GLU   A 1 105 ? 2.643   66.504  3.769   1.00 18.68  ? 957  GLU   A CD  1 
ATOM   791  O  OE1 . GLU   A 1 105 ? 2.713   67.720  3.440   1.00 18.73  ? 957  GLU   A OE1 1 
ATOM   792  O  OE2 . GLU   A 1 105 ? 2.918   66.071  4.920   1.00 17.25  ? 957  GLU   A OE2 1 
ATOM   793  N  N   . PHE   A 1 106 ? 3.116   64.908  -0.993  1.00 14.71  ? 958  PHE   A N   1 
ATOM   794  C  CA  . PHE   A 1 106 ? 4.382   64.312  -1.459  1.00 15.47  ? 958  PHE   A CA  1 
ATOM   795  C  C   . PHE   A 1 106 ? 5.591   65.024  -0.866  1.00 17.32  ? 958  PHE   A C   1 
ATOM   796  O  O   . PHE   A 1 106 ? 5.633   66.259  -0.892  1.00 20.17  ? 958  PHE   A O   1 
ATOM   797  C  CB  . PHE   A 1 106 ? 4.401   64.330  -2.981  1.00 16.05  ? 958  PHE   A CB  1 
ATOM   798  C  CG  . PHE   A 1 106 ? 5.700   63.886  -3.570  1.00 15.95  ? 958  PHE   A CG  1 
ATOM   799  C  CD1 . PHE   A 1 106 ? 6.168   62.589  -3.364  1.00 19.06  ? 958  PHE   A CD1 1 
ATOM   800  C  CD2 . PHE   A 1 106 ? 6.454   64.760  -4.345  1.00 19.97  ? 958  PHE   A CD2 1 
ATOM   801  C  CE1 . PHE   A 1 106 ? 7.383   62.174  -3.901  1.00 22.73  ? 958  PHE   A CE1 1 
ATOM   802  C  CE2 . PHE   A 1 106 ? 7.690   64.352  -4.889  1.00 19.47  ? 958  PHE   A CE2 1 
ATOM   803  C  CZ  . PHE   A 1 106 ? 8.132   63.046  -4.692  1.00 23.65  ? 958  PHE   A CZ  1 
ATOM   804  N  N   . LEU   A 1 107 ? 6.547   64.251  -0.305  1.00 17.63  ? 959  LEU   A N   1 
ATOM   805  C  CA  . LEU   A 1 107 ? 7.779   64.760  0.288   1.00 15.68  ? 959  LEU   A CA  1 
ATOM   806  C  C   . LEU   A 1 107 ? 8.947   64.330  -0.612  1.00 22.70  ? 959  LEU   A C   1 
ATOM   807  O  O   . LEU   A 1 107 ? 9.365   63.182  -0.550  1.00 17.49  ? 959  LEU   A O   1 
ATOM   808  C  CB  . LEU   A 1 107 ? 7.963   64.254  1.735   1.00 17.82  ? 959  LEU   A CB  1 
ATOM   809  C  CG  . LEU   A 1 107 ? 7.229   65.043  2.824   1.00 19.06  ? 959  LEU   A CG  1 
ATOM   810  C  CD1 . LEU   A 1 107 ? 5.761   65.106  2.589   1.00 17.34  ? 959  LEU   A CD1 1 
ATOM   811  C  CD2 . LEU   A 1 107 ? 7.499   64.485  4.267   1.00 17.54  ? 959  LEU   A CD2 1 
ATOM   812  N  N   . PRO   A 1 108 ? 9.400   65.230  -1.523  1.00 17.06  ? 960  PRO   A N   1 
ATOM   813  C  CA  . PRO   A 1 108 ? 10.442  64.959  -2.520  1.00 22.42  ? 960  PRO   A CA  1 
ATOM   814  C  C   . PRO   A 1 108 ? 11.735  64.288  -2.029  1.00 19.86  ? 960  PRO   A C   1 
ATOM   815  O  O   . PRO   A 1 108 ? 12.303  63.447  -2.731  1.00 23.35  ? 960  PRO   A O   1 
ATOM   816  C  CB  . PRO   A 1 108 ? 10.769  66.371  -3.031  1.00 22.48  ? 960  PRO   A CB  1 
ATOM   817  C  CG  . PRO   A 1 108 ? 9.574   67.110  -2.917  1.00 24.81  ? 960  PRO   A CG  1 
ATOM   818  C  CD  . PRO   A 1 108 ? 8.830   66.574  -1.727  1.00 22.94  ? 960  PRO   A CD  1 
ATOM   819  N  N   . SER   A 1 109 ? 12.215  64.681  -0.855  1.00 25.59  ? 961  SER   A N   1 
ATOM   820  C  CA  . SER   A 1 109 ? 13.421  64.068  -0.263  1.00 23.36  ? 961  SER   A CA  1 
ATOM   821  C  C   . SER   A 1 109 ? 13.314  62.579  0.106   1.00 21.61  ? 961  SER   A C   1 
ATOM   822  O  O   . SER   A 1 109 ? 14.327  61.917  0.284   1.00 23.82  ? 961  SER   A O   1 
ATOM   823  C  CB  . SER   A 1 109 ? 13.873  64.862  0.965   1.00 23.08  ? 961  SER   A CB  1 
ATOM   824  O  OG  . SER   A 1 109 ? 14.320  66.134  0.544   1.00 26.06  ? 961  SER   A OG  1 
ATOM   825  N  N   . GLY   A 1 110 ? 12.090  62.056  0.193   1.00 18.67  ? 962  GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 110 ? 11.870  60.631  0.375   1.00 21.84  ? 962  GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 110 ? 12.125  60.151  1.786   1.00 18.14  ? 962  GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 110 ? 12.127  60.943  2.738   1.00 19.24  ? 962  GLY   A O   1 
ATOM   829  N  N   . SER   A 1 111 ? 12.369  58.849  1.915   1.00 20.57  ? 963  SER   A N   1 
ATOM   830  C  CA  . SER   A 1 111 ? 12.626  58.241  3.217   1.00 19.16  ? 963  SER   A CA  1 
ATOM   831  C  C   . SER   A 1 111 ? 14.022  58.532  3.747   1.00 20.41  ? 963  SER   A C   1 
ATOM   832  O  O   . SER   A 1 111 ? 14.953  58.836  2.983   1.00 18.75  ? 963  SER   A O   1 
ATOM   833  C  CB  . SER   A 1 111 ? 12.398  56.716  3.190   1.00 19.60  ? 963  SER   A CB  1 
ATOM   834  O  OG  . SER   A 1 111 ? 13.489  56.034  2.578   1.00 24.27  ? 963  SER   A OG  1 
ATOM   835  N  N   . LEU   A 1 112 ? 14.164  58.405  5.069   1.00 19.87  ? 964  LEU   A N   1 
ATOM   836  C  CA  . LEU   A 1 112 ? 15.493  58.396  5.696   1.00 18.66  ? 964  LEU   A CA  1 
ATOM   837  C  C   . LEU   A 1 112 ? 16.427  57.330  5.115   1.00 19.05  ? 964  LEU   A C   1 
ATOM   838  O  O   . LEU   A 1 112 ? 17.622  57.557  5.052   1.00 18.74  ? 964  LEU   A O   1 
ATOM   839  C  CB  . LEU   A 1 112 ? 15.404  58.196  7.218   1.00 18.06  ? 964  LEU   A CB  1 
ATOM   840  C  CG  . LEU   A 1 112 ? 14.854  59.283  8.118   1.00 18.39  ? 964  LEU   A CG  1 
ATOM   841  C  CD1 . LEU   A 1 112 ? 14.828  58.758  9.550   1.00 23.19  ? 964  LEU   A CD1 1 
ATOM   842  C  CD2 . LEU   A 1 112 ? 15.665  60.596  8.001   1.00 17.93  ? 964  LEU   A CD2 1 
ATOM   843  N  N   . LYS   A 1 113 ? 15.888  56.182  4.697   1.00 21.36  ? 965  LYS   A N   1 
ATOM   844  C  CA  . LYS   A 1 113 ? 16.688  55.129  4.051   1.00 25.82  ? 965  LYS   A CA  1 
ATOM   845  C  C   . LYS   A 1 113 ? 17.384  55.638  2.782   1.00 25.73  ? 965  LYS   A C   1 
ATOM   846  O  O   . LYS   A 1 113 ? 18.538  55.306  2.546   1.00 25.23  ? 965  LYS   A O   1 
ATOM   847  C  CB  . LYS   A 1 113 ? 15.822  53.900  3.735   1.00 26.15  ? 965  LYS   A CB  1 
ATOM   848  C  CG  . LYS   A 1 113 ? 16.594  52.649  3.308   1.00 36.40  ? 965  LYS   A CG  1 
ATOM   849  C  CD  . LYS   A 1 113 ? 17.284  51.956  4.489   1.00 41.77  ? 965  LYS   A CD  1 
ATOM   850  C  CE  . LYS   A 1 113 ? 18.066  50.709  4.040   1.00 45.69  ? 965  LYS   A CE  1 
ATOM   851  N  NZ  . LYS   A 1 113 ? 19.417  50.603  4.688   1.00 41.59  ? 965  LYS   A NZ  1 
ATOM   852  N  N   A GLU   A 1 114 ? 16.673  56.429  1.976   0.50 25.57  ? 966  GLU   A N   1 
ATOM   853  N  N   B GLU   A 1 114 ? 16.667  56.459  2.017   0.50 25.16  ? 966  GLU   A N   1 
ATOM   854  C  CA  A GLU   A 1 114 ? 17.235  57.050  0.765   0.50 29.06  ? 966  GLU   A CA  1 
ATOM   855  C  CA  B GLU   A 1 114 ? 17.154  57.057  0.774   0.50 28.28  ? 966  GLU   A CA  1 
ATOM   856  C  C   A GLU   A 1 114 ? 18.048  58.308  1.069   0.50 28.80  ? 966  GLU   A C   1 
ATOM   857  C  C   B GLU   A 1 114 ? 17.995  58.313  1.031   0.50 28.37  ? 966  GLU   A C   1 
ATOM   858  O  O   A GLU   A 1 114 ? 19.141  58.502  0.511   0.50 31.18  ? 966  GLU   A O   1 
ATOM   859  O  O   B GLU   A 1 114 ? 19.061  58.500  0.424   0.50 31.13  ? 966  GLU   A O   1 
ATOM   860  C  CB  A GLU   A 1 114 ? 16.119  57.423  -0.212  0.50 30.61  ? 966  GLU   A CB  1 
ATOM   861  C  CB  B GLU   A 1 114 ? 15.966  57.438  -0.116  0.50 29.18  ? 966  GLU   A CB  1 
ATOM   862  C  CG  A GLU   A 1 114 ? 16.613  57.892  -1.599  0.50 34.26  ? 966  GLU   A CG  1 
ATOM   863  C  CG  B GLU   A 1 114 ? 14.970  56.303  -0.412  0.50 30.32  ? 966  GLU   A CG  1 
ATOM   864  C  CD  A GLU   A 1 114 ? 15.730  58.968  -2.204  0.50 38.29  ? 966  GLU   A CD  1 
ATOM   865  C  CD  B GLU   A 1 114 ? 15.365  55.339  -1.495  0.00 32.80  ? 966  GLU   A CD  1 
ATOM   866  O  OE1 A GLU   A 1 114 ? 14.490  58.786  -2.229  0.50 39.82  ? 966  GLU   A OE1 1 
ATOM   867  O  OE1 B GLU   A 1 114 ? 16.523  55.393  -1.966  0.00 33.99  ? 966  GLU   A OE1 1 
ATOM   868  O  OE2 A GLU   A 1 114 ? 16.281  59.993  -2.663  0.50 39.45  ? 966  GLU   A OE2 1 
ATOM   869  O  OE2 B GLU   A 1 114 ? 14.519  54.509  -1.891  0.00 33.74  ? 966  GLU   A OE2 1 
ATOM   870  N  N   . TYR   A 1 115 ? 17.506  59.162  1.933   1.00 25.95  ? 967  TYR   A N   1 
ATOM   871  C  CA  . TYR   A 1 115 ? 18.099  60.483  2.203   1.00 23.76  ? 967  TYR   A CA  1 
ATOM   872  C  C   . TYR   A 1 115 ? 19.420  60.477  2.952   1.00 18.71  ? 967  TYR   A C   1 
ATOM   873  O  O   . TYR   A 1 115 ? 20.346  61.170  2.551   1.00 21.35  ? 967  TYR   A O   1 
ATOM   874  C  CB  . TYR   A 1 115 ? 17.090  61.341  2.950   1.00 20.31  ? 967  TYR   A CB  1 
ATOM   875  C  CG  . TYR   A 1 115 ? 17.491  62.772  3.219   1.00 18.89  ? 967  TYR   A CG  1 
ATOM   876  C  CD1 . TYR   A 1 115 ? 17.271  63.778  2.273   1.00 19.87  ? 967  TYR   A CD1 1 
ATOM   877  C  CD2 . TYR   A 1 115 ? 18.066  63.128  4.422   1.00 17.17  ? 967  TYR   A CD2 1 
ATOM   878  C  CE1 . TYR   A 1 115 ? 17.617  65.106  2.531   1.00 24.26  ? 967  TYR   A CE1 1 
ATOM   879  C  CE2 . TYR   A 1 115 ? 18.382  64.461  4.718   1.00 20.10  ? 967  TYR   A CE2 1 
ATOM   880  C  CZ  . TYR   A 1 115 ? 18.186  65.437  3.752   1.00 18.86  ? 967  TYR   A CZ  1 
ATOM   881  O  OH  . TYR   A 1 115 ? 18.522  66.742  4.023   1.00 24.86  ? 967  TYR   A OH  1 
ATOM   882  N  N   . LEU   A 1 116 ? 19.490  59.758  4.078   1.00 19.34  ? 968  LEU   A N   1 
ATOM   883  C  CA  . LEU   A 1 116 ? 20.675  59.824  4.934   1.00 18.37  ? 968  LEU   A CA  1 
ATOM   884  C  C   . LEU   A 1 116 ? 21.961  59.414  4.244   1.00 19.43  ? 968  LEU   A C   1 
ATOM   885  O  O   . LEU   A 1 116 ? 22.974  60.106  4.398   1.00 23.54  ? 968  LEU   A O   1 
ATOM   886  C  CB  . LEU   A 1 116 ? 20.481  59.040  6.238   1.00 17.08  ? 968  LEU   A CB  1 
ATOM   887  C  CG  . LEU   A 1 116 ? 19.385  59.535  7.175   1.00 19.84  ? 968  LEU   A CG  1 
ATOM   888  C  CD1 . LEU   A 1 116 ? 19.212  58.588  8.354   1.00 19.80  ? 968  LEU   A CD1 1 
ATOM   889  C  CD2 . LEU   A 1 116 ? 19.690  60.936  7.709   1.00 20.97  ? 968  LEU   A CD2 1 
ATOM   890  N  N   . PRO   A 1 117 ? 21.948  58.303  3.465   1.00 18.61  ? 969  PRO   A N   1 
ATOM   891  C  CA  . PRO   A 1 117 ? 23.222  57.973  2.818   1.00 19.49  ? 969  PRO   A CA  1 
ATOM   892  C  C   . PRO   A 1 117 ? 23.751  59.038  1.846   1.00 24.29  ? 969  PRO   A C   1 
ATOM   893  O  O   . PRO   A 1 117 ? 24.967  59.126  1.622   1.00 27.22  ? 969  PRO   A O   1 
ATOM   894  C  CB  . PRO   A 1 117 ? 22.920  56.654  2.105   1.00 24.04  ? 969  PRO   A CB  1 
ATOM   895  C  CG  . PRO   A 1 117 ? 21.729  56.079  2.830   1.00 21.00  ? 969  PRO   A CG  1 
ATOM   896  C  CD  . PRO   A 1 117 ? 20.920  57.265  3.239   1.00 20.35  ? 969  PRO   A CD  1 
ATOM   897  N  N   . LYS   A 1 118 ? 22.845  59.816  1.264   1.00 24.15  ? 970  LYS   A N   1 
ATOM   898  C  CA  . LYS   A 1 118 ? 23.189  60.853  0.287   1.00 27.37  ? 970  LYS   A CA  1 
ATOM   899  C  C   . LYS   A 1 118 ? 23.518  62.196  0.944   1.00 27.21  ? 970  LYS   A C   1 
ATOM   900  O  O   . LYS   A 1 118 ? 24.014  63.097  0.286   1.00 31.00  ? 970  LYS   A O   1 
ATOM   901  C  CB  . LYS   A 1 118 ? 22.030  61.022  -0.712  1.00 31.18  ? 970  LYS   A CB  1 
ATOM   902  C  CG  . LYS   A 1 118 ? 21.796  59.826  -1.666  1.00 39.50  ? 970  LYS   A CG  1 
ATOM   903  C  CD  . LYS   A 1 118 ? 20.428  59.959  -2.402  1.00 35.44  ? 970  LYS   A CD  1 
ATOM   904  C  CE  . LYS   A 1 118 ? 20.275  59.005  -3.587  1.00 49.07  ? 970  LYS   A CE  1 
ATOM   905  N  NZ  . LYS   A 1 118 ? 18.866  59.019  -4.116  1.00 44.50  ? 970  LYS   A NZ  1 
ATOM   906  N  N   . ASN   A 1 119 ? 23.251  62.326  2.248   1.00 24.24  ? 971  ASN   A N   1 
ATOM   907  C  CA  . ASN   A 1 119 ? 23.359  63.629  2.948   1.00 27.09  ? 971  ASN   A CA  1 
ATOM   908  C  C   . ASN   A 1 119 ? 24.148  63.603  4.250   1.00 24.06  ? 971  ASN   A C   1 
ATOM   909  O  O   . ASN   A 1 119 ? 23.964  64.482  5.099   1.00 24.35  ? 971  ASN   A O   1 
ATOM   910  C  CB  . ASN   A 1 119 ? 21.947  64.216  3.171   1.00 24.97  ? 971  ASN   A CB  1 
ATOM   911  C  CG  . ASN   A 1 119 ? 21.282  64.620  1.868   1.00 26.79  ? 971  ASN   A CG  1 
ATOM   912  O  OD1 . ASN   A 1 119 ? 21.502  65.717  1.363   1.00 32.72  ? 971  ASN   A OD1 1 
ATOM   913  N  ND2 . ASN   A 1 119 ? 20.503  63.723  1.300   1.00 26.52  ? 971  ASN   A ND2 1 
ATOM   914  N  N   . LYS   A 1 120 ? 25.059  62.635  4.406   1.00 24.92  ? 972  LYS   A N   1 
ATOM   915  C  CA  . LYS   A 1 120 ? 25.878  62.529  5.624   1.00 26.66  ? 972  LYS   A CA  1 
ATOM   916  C  C   . LYS   A 1 120 ? 26.568  63.837  5.989   1.00 23.95  ? 972  LYS   A C   1 
ATOM   917  O  O   . LYS   A 1 120 ? 26.550  64.244  7.149   1.00 23.96  ? 972  LYS   A O   1 
ATOM   918  C  CB  . LYS   A 1 120 ? 27.005  61.496  5.486   1.00 27.01  ? 972  LYS   A CB  1 
ATOM   919  C  CG  . LYS   A 1 120 ? 26.608  60.072  5.673   1.00 31.78  ? 972  LYS   A CG  1 
ATOM   920  C  CD  . LYS   A 1 120 ? 27.710  59.203  5.096   1.00 35.49  ? 972  LYS   A CD  1 
ATOM   921  C  CE  . LYS   A 1 120 ? 27.740  57.858  5.711   1.00 41.55  ? 972  LYS   A CE  1 
ATOM   922  N  NZ  . LYS   A 1 120 ? 28.959  57.140  5.228   1.00 46.27  ? 972  LYS   A NZ  1 
ATOM   923  N  N   . ASN   A 1 121 ? 27.181  64.481  5.010   1.00 22.88  ? 973  ASN   A N   1 
ATOM   924  C  CA  . ASN   A 1 121 ? 27.945  65.708  5.260   1.00 28.76  ? 973  ASN   A CA  1 
ATOM   925  C  C   . ASN   A 1 121 ? 27.131  66.858  5.882   1.00 29.96  ? 973  ASN   A C   1 
ATOM   926  O  O   . ASN   A 1 121 ? 27.699  67.667  6.615   1.00 33.97  ? 973  ASN   A O   1 
ATOM   927  C  CB  . ASN   A 1 121 ? 28.659  66.192  3.997   1.00 33.86  ? 973  ASN   A CB  1 
ATOM   928  C  CG  . ASN   A 1 121 ? 29.668  67.318  4.271   1.00 33.76  ? 973  ASN   A CG  1 
ATOM   929  O  OD1 . ASN   A 1 121 ? 30.585  67.180  5.098   1.00 34.76  ? 973  ASN   A OD1 1 
ATOM   930  N  ND2 . ASN   A 1 121 ? 29.509  68.430  3.555   1.00 31.09  ? 973  ASN   A ND2 1 
ATOM   931  N  N   . LYS   A 1 122 ? 25.825  66.924  5.624   1.00 29.49  ? 974  LYS   A N   1 
ATOM   932  C  CA  . LYS   A 1 122 ? 25.019  68.045  6.160   1.00 33.78  ? 974  LYS   A CA  1 
ATOM   933  C  C   . LYS   A 1 122 ? 24.228  67.708  7.421   1.00 31.26  ? 974  LYS   A C   1 
ATOM   934  O  O   . LYS   A 1 122 ? 23.696  68.615  8.054   1.00 31.85  ? 974  LYS   A O   1 
ATOM   935  C  CB  . LYS   A 1 122 ? 24.104  68.658  5.094   1.00 37.09  ? 974  LYS   A CB  1 
ATOM   936  C  CG  . LYS   A 1 122 ? 23.068  67.732  4.520   1.00 37.07  ? 974  LYS   A CG  1 
ATOM   937  C  CD  . LYS   A 1 122 ? 21.849  68.486  3.987   1.00 45.62  ? 974  LYS   A CD  1 
ATOM   938  C  CE  . LYS   A 1 122 ? 22.087  69.047  2.608   1.00 47.06  ? 974  LYS   A CE  1 
ATOM   939  N  NZ  . LYS   A 1 122 ? 20.888  69.806  2.149   1.00 54.38  ? 974  LYS   A NZ  1 
ATOM   940  N  N   . ILE   A 1 123 ? 24.166  66.417  7.764   1.00 25.49  ? 975  ILE   A N   1 
ATOM   941  C  CA  . ILE   A 1 123 ? 23.391  65.898  8.893   1.00 25.56  ? 975  ILE   A CA  1 
ATOM   942  C  C   . ILE   A 1 123 ? 24.386  65.395  9.944   1.00 25.26  ? 975  ILE   A C   1 
ATOM   943  O  O   . ILE   A 1 123 ? 24.969  64.316  9.792   1.00 27.98  ? 975  ILE   A O   1 
ATOM   944  C  CB  . ILE   A 1 123 ? 22.462  64.733  8.470   1.00 25.43  ? 975  ILE   A CB  1 
ATOM   945  C  CG1 . ILE   A 1 123 ? 21.493  65.146  7.348   1.00 27.80  ? 975  ILE   A CG1 1 
ATOM   946  C  CG2 . ILE   A 1 123 ? 21.660  64.205  9.666   1.00 23.27  ? 975  ILE   A CG2 1 
ATOM   947  C  CD1 . ILE   A 1 123 ? 20.660  66.441  7.578   1.00 30.86  ? 975  ILE   A CD1 1 
ATOM   948  N  N   . ASN   A 1 124 ? 24.567  66.198  10.988  1.00 20.98  ? 976  ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 124 ? 25.479  65.896  12.098  1.00 23.52  ? 976  ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 124 ? 24.700  65.319  13.271  1.00 23.16  ? 976  ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 124 ? 23.492  65.165  13.189  1.00 22.87  ? 976  ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 124 ? 26.298  67.138  12.497  1.00 26.91  ? 976  ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 124 ? 25.457  68.268  13.049  1.00 28.74  ? 976  ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 124 ? 24.230  68.178  13.148  1.00 28.40  ? 976  ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 124 ? 26.117  69.375  13.361  1.00 35.11  ? 976  ASN   A ND2 1 
ATOM   956  N  N   . LEU   A 1 125 ? 25.387  65.004  14.362  1.00 21.03  ? 977  LEU   A N   1 
ATOM   957  C  CA  . LEU   A 1 125 ? 24.730  64.348  15.514  1.00 22.03  ? 977  LEU   A CA  1 
ATOM   958  C  C   . LEU   A 1 125 ? 23.561  65.160  16.090  1.00 19.88  ? 977  LEU   A C   1 
ATOM   959  O  O   . LEU   A 1 125 ? 22.488  64.625  16.355  1.00 20.53  ? 977  LEU   A O   1 
ATOM   960  C  CB  . LEU   A 1 125 ? 25.756  64.031  16.594  1.00 23.51  ? 977  LEU   A CB  1 
ATOM   961  C  CG  . LEU   A 1 125 ? 25.252  63.430  17.911  1.00 21.53  ? 977  LEU   A CG  1 
ATOM   962  C  CD1 . LEU   A 1 125 ? 24.565  62.099  17.686  1.00 27.06  ? 977  LEU   A CD1 1 
ATOM   963  C  CD2 . LEU   A 1 125 ? 26.412  63.306  18.888  1.00 28.01  ? 977  LEU   A CD2 1 
ATOM   964  N  N   . LYS   A 1 126 ? 23.786  66.448  16.268  1.00 21.26  ? 978  LYS   A N   1 
ATOM   965  C  CA  . LYS   A 1 126 ? 22.723  67.385  16.654  1.00 19.24  ? 978  LYS   A CA  1 
ATOM   966  C  C   . LYS   A 1 126 ? 21.448  67.229  15.793  1.00 22.48  ? 978  LYS   A C   1 
ATOM   967  O  O   . LYS   A 1 126 ? 20.320  67.133  16.323  1.00 20.01  ? 978  LYS   A O   1 
ATOM   968  C  CB  . LYS   A 1 126 ? 23.268  68.814  16.577  1.00 23.55  ? 978  LYS   A CB  1 
ATOM   969  C  CG  . LYS   A 1 126 ? 22.360  69.839  17.216  1.00 28.38  ? 978  LYS   A CG  1 
ATOM   970  C  CD  . LYS   A 1 126 ? 23.085  71.159  17.464  1.00 39.33  ? 978  LYS   A CD  1 
ATOM   971  C  CE  . LYS   A 1 126 ? 22.439  71.928  18.587  1.00 49.04  ? 978  LYS   A CE  1 
ATOM   972  N  NZ  . LYS   A 1 126 ? 22.666  71.246  19.893  1.00 50.83  ? 978  LYS   A NZ  1 
ATOM   973  N  N   . GLN   A 1 127 ? 21.613  67.171  14.470  1.00 20.19  ? 979  GLN   A N   1 
ATOM   974  C  CA  . GLN   A 1 127 ? 20.455  67.042  13.590  1.00 20.48  ? 979  GLN   A CA  1 
ATOM   975  C  C   . GLN   A 1 127 ? 19.806  65.659  13.721  1.00 17.64  ? 979  GLN   A C   1 
ATOM   976  O  O   . GLN   A 1 127 ? 18.577  65.541  13.683  1.00 17.71  ? 979  GLN   A O   1 
ATOM   977  C  CB  . GLN   A 1 127 ? 20.779  67.321  12.105  1.00 20.41  ? 979  GLN   A CB  1 
ATOM   978  C  CG  . GLN   A 1 127 ? 19.543  67.427  11.245  1.00 19.45  ? 979  GLN   A CG  1 
ATOM   979  C  CD  . GLN   A 1 127 ? 18.609  68.511  11.737  1.00 19.04  ? 979  GLN   A CD  1 
ATOM   980  O  OE1 . GLN   A 1 127 ? 18.944  69.696  11.678  1.00 20.97  ? 979  GLN   A OE1 1 
ATOM   981  N  NE2 . GLN   A 1 127 ? 17.446  68.112  12.247  1.00 19.87  ? 979  GLN   A NE2 1 
ATOM   982  N  N   . GLN   A 1 128 ? 20.639  64.630  13.847  1.00 17.76  ? 980  GLN   A N   1 
ATOM   983  C  CA  . GLN   A 1 128 ? 20.142  63.270  14.076  1.00 16.56  ? 980  GLN   A CA  1 
ATOM   984  C  C   . GLN   A 1 128 ? 19.277  63.199  15.329  1.00 15.68  ? 980  GLN   A C   1 
ATOM   985  O  O   . GLN   A 1 128 ? 18.207  62.557  15.320  1.00 16.68  ? 980  GLN   A O   1 
ATOM   986  C  CB  . GLN   A 1 128 ? 21.315  62.269  14.190  1.00 20.02  ? 980  GLN   A CB  1 
ATOM   987  C  CG  . GLN   A 1 128 ? 22.020  62.001  12.867  1.00 19.21  ? 980  GLN   A CG  1 
ATOM   988  C  CD  . GLN   A 1 128 ? 23.297  61.183  13.027  1.00 21.98  ? 980  GLN   A CD  1 
ATOM   989  O  OE1 . GLN   A 1 128 ? 24.164  61.511  13.834  1.00 26.64  ? 980  GLN   A OE1 1 
ATOM   990  N  NE2 . GLN   A 1 128 ? 23.417  60.117  12.258  1.00 17.85  ? 980  GLN   A NE2 1 
ATOM   991  N  N   . LEU   A 1 129 ? 19.720  63.851  16.392  1.00 17.17  ? 981  LEU   A N   1 
ATOM   992  C  CA  . LEU   A 1 129 ? 18.975  63.863  17.651  1.00 17.41  ? 981  LEU   A CA  1 
ATOM   993  C  C   . LEU   A 1 129 ? 17.685  64.670  17.538  1.00 18.13  ? 981  LEU   A C   1 
ATOM   994  O  O   . LEU   A 1 129 ? 16.674  64.290  18.114  1.00 14.91  ? 981  LEU   A O   1 
ATOM   995  C  CB  . LEU   A 1 129 ? 19.864  64.330  18.781  1.00 19.22  ? 981  LEU   A CB  1 
ATOM   996  C  CG  . LEU   A 1 129 ? 21.088  63.463  19.070  1.00 19.57  ? 981  LEU   A CG  1 
ATOM   997  C  CD1 . LEU   A 1 129 ? 21.769  64.005  20.325  1.00 24.08  ? 981  LEU   A CD1 1 
ATOM   998  C  CD2 . LEU   A 1 129 ? 20.737  61.970  19.205  1.00 20.68  ? 981  LEU   A CD2 1 
ATOM   999  N  N   . LYS   A 1 130 ? 17.694  65.741  16.734  1.00 17.78  ? 982  LYS   A N   1 
ATOM   1000 C  CA  . LYS   A 1 130 ? 16.470  66.482  16.429  1.00 19.03  ? 982  LYS   A CA  1 
ATOM   1001 C  C   . LYS   A 1 130 ? 15.460  65.639  15.678  1.00 16.56  ? 982  LYS   A C   1 
ATOM   1002 O  O   . LYS   A 1 130 ? 14.275  65.629  16.027  1.00 16.10  ? 982  LYS   A O   1 
ATOM   1003 C  CB  . LYS   A 1 130 ? 16.800  67.765  15.644  1.00 19.99  ? 982  LYS   A CB  1 
ATOM   1004 C  CG  . LYS   A 1 130 ? 17.425  68.829  16.533  1.00 21.28  ? 982  LYS   A CG  1 
ATOM   1005 C  CD  . LYS   A 1 130 ? 17.713  70.080  15.739  1.00 23.49  ? 982  LYS   A CD  1 
ATOM   1006 C  CE  . LYS   A 1 130 ? 18.443  71.124  16.505  1.00 32.05  ? 982  LYS   A CE  1 
ATOM   1007 N  NZ  . LYS   A 1 130 ? 18.834  72.229  15.574  1.00 32.96  ? 982  LYS   A NZ  1 
ATOM   1008 N  N   . TYR   A 1 131 ? 15.915  64.902  14.657  1.00 16.00  ? 983  TYR   A N   1 
ATOM   1009 C  CA  . TYR   A 1 131 ? 15.028  63.954  13.976  1.00 15.13  ? 983  TYR   A CA  1 
ATOM   1010 C  C   . TYR   A 1 131 ? 14.461  62.921  14.949  1.00 15.08  ? 983  TYR   A C   1 
ATOM   1011 O  O   . TYR   A 1 131 ? 13.261  62.598  14.890  1.00 16.70  ? 983  TYR   A O   1 
ATOM   1012 C  CB  . TYR   A 1 131 ? 15.752  63.195  12.863  1.00 13.53  ? 983  TYR   A CB  1 
ATOM   1013 C  CG  . TYR   A 1 131 ? 16.138  63.973  11.631  1.00 15.43  ? 983  TYR   A CG  1 
ATOM   1014 C  CD1 . TYR   A 1 131 ? 15.514  65.171  11.288  1.00 13.80  ? 983  TYR   A CD1 1 
ATOM   1015 C  CD2 . TYR   A 1 131 ? 17.099  63.450  10.762  1.00 19.74  ? 983  TYR   A CD2 1 
ATOM   1016 C  CE1 . TYR   A 1 131 ? 15.852  65.843  10.090  1.00 16.74  ? 983  TYR   A CE1 1 
ATOM   1017 C  CE2 . TYR   A 1 131 ? 17.471  64.120  9.594   1.00 20.21  ? 983  TYR   A CE2 1 
ATOM   1018 C  CZ  . TYR   A 1 131 ? 16.849  65.305  9.264   1.00 24.65  ? 983  TYR   A CZ  1 
ATOM   1019 O  OH  . TYR   A 1 131 ? 17.230  65.931  8.109   1.00 27.27  ? 983  TYR   A OH  1 
ATOM   1020 N  N   . ALA   A 1 132 ? 15.307  62.426  15.845  1.00 16.79  ? 984  ALA   A N   1 
ATOM   1021 C  CA  . ALA   A 1 132 ? 14.866  61.449  16.850  1.00 15.89  ? 984  ALA   A CA  1 
ATOM   1022 C  C   . ALA   A 1 132 ? 13.702  61.985  17.722  1.00 16.29  ? 984  ALA   A C   1 
ATOM   1023 O  O   . ALA   A 1 132 ? 12.684  61.307  17.925  1.00 15.87  ? 984  ALA   A O   1 
ATOM   1024 C  CB  . ALA   A 1 132 ? 16.057  61.005  17.723  1.00 15.35  ? 984  ALA   A CB  1 
ATOM   1025 N  N   . VAL   A 1 133 ? 13.842  63.211  18.221  1.00 15.41  ? 985  VAL   A N   1 
ATOM   1026 C  CA  . VAL   A 1 133 ? 12.753  63.868  18.955  1.00 14.89  ? 985  VAL   A CA  1 
ATOM   1027 C  C   . VAL   A 1 133 ? 11.456  63.970  18.135  1.00 17.45  ? 985  VAL   A C   1 
ATOM   1028 O  O   . VAL   A 1 133 ? 10.346  63.753  18.645  1.00 15.76  ? 985  VAL   A O   1 
ATOM   1029 C  CB  . VAL   A 1 133 ? 13.199  65.306  19.398  1.00 19.55  ? 985  VAL   A CB  1 
ATOM   1030 C  CG1 . VAL   A 1 133 ? 12.035  66.145  19.884  1.00 18.57  ? 985  VAL   A CG1 1 
ATOM   1031 C  CG2 . VAL   A 1 133 ? 14.282  65.217  20.489  1.00 19.20  ? 985  VAL   A CG2 1 
ATOM   1032 N  N   . GLN   A 1 134 ? 11.595  64.364  16.879  1.00 17.06  ? 986  GLN   A N   1 
ATOM   1033 C  CA  . GLN   A 1 134 ? 10.438  64.531  16.016  1.00 16.58  ? 986  GLN   A CA  1 
ATOM   1034 C  C   . GLN   A 1 134 ? 9.696   63.210  15.774  1.00 13.62  ? 986  GLN   A C   1 
ATOM   1035 O  O   . GLN   A 1 134 ? 8.471   63.165  15.762  1.00 17.69  ? 986  GLN   A O   1 
ATOM   1036 C  CB  . GLN   A 1 134 ? 10.875  65.138  14.698  1.00 16.80  ? 986  GLN   A CB  1 
ATOM   1037 C  CG  . GLN   A 1 134 ? 11.279  66.582  14.849  1.00 18.51  ? 986  GLN   A CG  1 
ATOM   1038 C  CD  . GLN   A 1 134 ? 11.922  67.106  13.598  1.00 21.49  ? 986  GLN   A CD  1 
ATOM   1039 O  OE1 . GLN   A 1 134 ? 11.899  66.443  12.586  1.00 21.73  ? 986  GLN   A OE1 1 
ATOM   1040 N  NE2 . GLN   A 1 134 ? 12.564  68.272  13.685  1.00 20.37  ? 986  GLN   A NE2 1 
ATOM   1041 N  N   . ILE   A 1 135 ? 10.448  62.153  15.549  1.00 12.84  ? 987  ILE   A N   1 
ATOM   1042 C  CA  . ILE   A 1 135 ? 9.860   60.802  15.458  1.00 12.48  ? 987  ILE   A CA  1 
ATOM   1043 C  C   . ILE   A 1 135 ? 9.157   60.446  16.764  1.00 15.65  ? 987  ILE   A C   1 
ATOM   1044 O  O   . ILE   A 1 135 ? 8.017   59.971  16.739  1.00 17.55  ? 987  ILE   A O   1 
ATOM   1045 C  CB  . ILE   A 1 135 ? 10.910  59.726  15.094  1.00 12.97  ? 987  ILE   A CB  1 
ATOM   1046 C  CG1 . ILE   A 1 135 ? 11.487  59.951  13.682  1.00 15.07  ? 987  ILE   A CG1 1 
ATOM   1047 C  CG2 . ILE   A 1 135 ? 10.286  58.320  15.153  1.00 14.93  ? 987  ILE   A CG2 1 
ATOM   1048 C  CD1 . ILE   A 1 135 ? 12.811  59.240  13.446  1.00 12.41  ? 987  ILE   A CD1 1 
ATOM   1049 N  N   . CYS   A 1 136 ? 9.804   60.700  17.896  1.00 14.18  ? 988  CYS   A N   1 
ATOM   1050 C  CA  . CYS   A 1 136 ? 9.150   60.476  19.202  1.00 17.55  ? 988  CYS   A CA  1 
ATOM   1051 C  C   . CYS   A 1 136 ? 7.859   61.284  19.422  1.00 16.97  ? 988  CYS   A C   1 
ATOM   1052 O  O   . CYS   A 1 136 ? 6.897   60.759  19.959  1.00 18.80  ? 988  CYS   A O   1 
ATOM   1053 C  CB  . CYS   A 1 136 ? 10.114  60.667  20.368  1.00 21.13  ? 988  CYS   A CB  1 
ATOM   1054 S  SG  . CYS   A 1 136 ? 11.442  59.474  20.440  1.00 18.79  ? 988  CYS   A SG  1 
ATOM   1055 N  N   . LYS   A 1 137 ? 7.834   62.552  19.015  1.00 17.56  ? 989  LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 137 ? 6.618   63.359  19.145  1.00 16.30  ? 989  LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 137 ? 5.473   62.794  18.266  1.00 19.15  ? 989  LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 137 ? 4.324   62.714  18.715  1.00 19.87  ? 989  LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 137 ? 6.910   64.827  18.824  1.00 21.72  ? 989  LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 137 ? 7.796   65.513  19.875  1.00 19.53  ? 989  LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 137 ? 8.121   66.940  19.490  1.00 25.40  ? 989  LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 137 ? 8.814   67.681  20.621  1.00 25.65  ? 989  LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 137 ? 9.236   69.054  20.222  1.00 34.16  ? 989  LYS   A NZ  1 
ATOM   1064 N  N   . GLY   A 1 138 ? 5.804   62.393  17.042  1.00 18.25  ? 990  GLY   A N   1 
ATOM   1065 C  CA  . GLY   A 1 138 ? 4.845   61.766  16.122  1.00 18.78  ? 990  GLY   A CA  1 
ATOM   1066 C  C   . GLY   A 1 138 ? 4.244   60.492  16.712  1.00 21.47  ? 990  GLY   A C   1 
ATOM   1067 O  O   . GLY   A 1 138 ? 3.003   60.293  16.713  1.00 19.66  ? 990  GLY   A O   1 
ATOM   1068 N  N   . MET   A 1 139 ? 5.124   59.661  17.259  1.00 19.25  ? 991  MET   A N   1 
ATOM   1069 C  CA  . MET   A 1 139 ? 4.716   58.407  17.924  1.00 18.32  ? 991  MET   A CA  1 
ATOM   1070 C  C   . MET   A 1 139 ? 3.936   58.619  19.206  1.00 22.09  ? 991  MET   A C   1 
ATOM   1071 O  O   . MET   A 1 139 ? 2.985   57.880  19.488  1.00 22.53  ? 991  MET   A O   1 
ATOM   1072 C  CB  . MET   A 1 139 ? 5.938   57.536  18.205  1.00 19.14  ? 991  MET   A CB  1 
ATOM   1073 C  CG  . MET   A 1 139 ? 6.622   57.010  16.969  1.00 22.21  ? 991  MET   A CG  1 
ATOM   1074 S  SD  . MET   A 1 139 ? 5.564   56.023  15.881  1.00 23.24  ? 991  MET   A SD  1 
ATOM   1075 C  CE  . MET   A 1 139 ? 4.924   54.772  17.007  1.00 32.97  ? 991  MET   A CE  1 
ATOM   1076 N  N   . ASP   A 1 140 ? 4.342   59.597  20.006  1.00 19.06  ? 992  ASP   A N   1 
ATOM   1077 C  CA  . ASP   A 1 140 ? 3.607   59.863  21.250  1.00 20.19  ? 992  ASP   A CA  1 
ATOM   1078 C  C   . ASP   A 1 140 ? 2.198   60.396  20.909  1.00 23.05  ? 992  ASP   A C   1 
ATOM   1079 O  O   . ASP   A 1 140 ? 1.229   60.064  21.578  1.00 24.05  ? 992  ASP   A O   1 
ATOM   1080 C  CB  . ASP   A 1 140 ? 4.391   60.824  22.136  1.00 22.69  ? 992  ASP   A CB  1 
ATOM   1081 C  CG  . ASP   A 1 140 ? 3.859   60.867  23.573  1.00 33.77  ? 992  ASP   A CG  1 
ATOM   1082 O  OD1 . ASP   A 1 140 ? 3.681   59.792  24.184  1.00 32.53  ? 992  ASP   A OD1 1 
ATOM   1083 O  OD2 . ASP   A 1 140 ? 3.626   61.984  24.076  1.00 40.86  ? 992  ASP   A OD2 1 
ATOM   1084 N  N   . TYR   A 1 141 ? 2.078   61.169  19.827  1.00 23.05  ? 993  TYR   A N   1 
ATOM   1085 C  CA  . TYR   A 1 141 ? 0.757   61.580  19.335  1.00 25.48  ? 993  TYR   A CA  1 
ATOM   1086 C  C   . TYR   A 1 141 ? -0.096  60.372  18.918  1.00 25.71  ? 993  TYR   A C   1 
ATOM   1087 O  O   . TYR   A 1 141 ? -1.250  60.250  19.333  1.00 25.18  ? 993  TYR   A O   1 
ATOM   1088 C  CB  . TYR   A 1 141 ? 0.899   62.546  18.160  1.00 22.84  ? 993  TYR   A CB  1 
ATOM   1089 C  CG  . TYR   A 1 141 ? -0.409  62.927  17.525  1.00 22.24  ? 993  TYR   A CG  1 
ATOM   1090 C  CD1 . TYR   A 1 141 ? -1.236  63.884  18.116  1.00 26.01  ? 993  TYR   A CD1 1 
ATOM   1091 C  CD2 . TYR   A 1 141 ? -0.824  62.349  16.311  1.00 23.15  ? 993  TYR   A CD2 1 
ATOM   1092 C  CE1 . TYR   A 1 141 ? -2.437  64.247  17.529  1.00 29.48  ? 993  TYR   A CE1 1 
ATOM   1093 C  CE2 . TYR   A 1 141 ? -2.033  62.702  15.723  1.00 25.37  ? 993  TYR   A CE2 1 
ATOM   1094 C  CZ  . TYR   A 1 141 ? -2.827  63.660  16.326  1.00 27.09  ? 993  TYR   A CZ  1 
ATOM   1095 O  OH  . TYR   A 1 141 ? -4.016  64.014  15.755  1.00 26.54  ? 993  TYR   A OH  1 
ATOM   1096 N  N   . LEU   A 1 142 ? 0.502   59.469  18.136  1.00 25.35  ? 994  LEU   A N   1 
ATOM   1097 C  CA  . LEU   A 1 142 ? -0.179  58.256  17.650  1.00 25.56  ? 994  LEU   A CA  1 
ATOM   1098 C  C   . LEU   A 1 142 ? -0.649  57.380  18.804  1.00 28.38  ? 994  LEU   A C   1 
ATOM   1099 O  O   . LEU   A 1 142 ? -1.772  56.877  18.781  1.00 29.33  ? 994  LEU   A O   1 
ATOM   1100 C  CB  . LEU   A 1 142 ? 0.751   57.463  16.733  1.00 27.31  ? 994  LEU   A CB  1 
ATOM   1101 C  CG  . LEU   A 1 142 ? 0.193   56.238  16.021  1.00 27.48  ? 994  LEU   A CG  1 
ATOM   1102 C  CD1 . LEU   A 1 142 ? -0.835  56.616  14.973  1.00 28.23  ? 994  LEU   A CD1 1 
ATOM   1103 C  CD2 . LEU   A 1 142 ? 1.340   55.458  15.403  1.00 27.95  ? 994  LEU   A CD2 1 
ATOM   1104 N  N   . GLY   A 1 143 ? 0.205   57.232  19.820  1.00 26.09  ? 995  GLY   A N   1 
ATOM   1105 C  CA  . GLY   A 1 143 ? -0.151  56.495  21.036  1.00 27.99  ? 995  GLY   A CA  1 
ATOM   1106 C  C   . GLY   A 1 143 ? -1.212  57.165  21.894  1.00 31.15  ? 995  GLY   A C   1 
ATOM   1107 O  O   . GLY   A 1 143 ? -1.980  56.474  22.568  1.00 35.44  ? 995  GLY   A O   1 
ATOM   1108 N  N   . SER   A 1 144 ? -1.256  58.500  21.888  1.00 30.29  ? 996  SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 144 ? -2.333  59.251  22.559  1.00 33.00  ? 996  SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 144 ? -3.700  59.099  21.864  1.00 35.49  ? 996  SER   A C   1 
ATOM   1111 O  O   . SER   A 1 144 ? -4.750  59.283  22.496  1.00 36.73  ? 996  SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 144 ? -1.976  60.731  22.671  1.00 29.27  ? 996  SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 144 ? -2.195  61.403  21.447  1.00 33.75  ? 996  SER   A OG  1 
ATOM   1114 N  N   . ARG   A 1 145 ? -3.685  58.793  20.568  1.00 33.44  ? 997  ARG   A N   1 
ATOM   1115 C  CA  . ARG   A 1 145 ? -4.903  58.418  19.831  1.00 35.67  ? 997  ARG   A CA  1 
ATOM   1116 C  C   . ARG   A 1 145 ? -5.240  56.920  19.953  1.00 33.84  ? 997  ARG   A C   1 
ATOM   1117 O  O   . ARG   A 1 145 ? -6.193  56.455  19.330  1.00 34.23  ? 997  ARG   A O   1 
ATOM   1118 C  CB  . ARG   A 1 145 ? -4.781  58.767  18.343  1.00 32.46  ? 997  ARG   A CB  1 
ATOM   1119 C  CG  . ARG   A 1 145 ? -4.499  60.234  17.985  1.00 41.37  ? 997  ARG   A CG  1 
ATOM   1120 C  CD  . ARG   A 1 145 ? -5.501  61.234  18.562  1.00 47.90  ? 997  ARG   A CD  1 
ATOM   1121 N  NE  . ARG   A 1 145 ? -4.958  61.943  19.715  1.00 54.49  ? 997  ARG   A NE  1 
ATOM   1122 C  CZ  . ARG   A 1 145 ? -5.388  63.066  20.270  0.00 55.70  ? 997  ARG   A CZ  1 
ATOM   1123 N  NH1 . ARG   A 1 145 ? -4.751  63.585  21.313  0.00 56.69  ? 997  ARG   A NH1 1 
ATOM   1124 N  NH2 . ARG   A 1 145 ? -6.474  63.680  19.796  0.00 57.07  ? 997  ARG   A NH2 1 
ATOM   1125 N  N   . GLN   A 1 146 ? -4.465  56.183  20.748  1.00 33.32  ? 998  GLN   A N   1 
ATOM   1126 C  CA  . GLN   A 1 146 ? -4.652  54.736  21.017  1.00 33.96  ? 998  GLN   A CA  1 
ATOM   1127 C  C   . GLN   A 1 146 ? -4.344  53.817  19.828  1.00 33.49  ? 998  GLN   A C   1 
ATOM   1128 O  O   . GLN   A 1 146 ? -4.998  52.792  19.634  1.00 36.58  ? 998  GLN   A O   1 
ATOM   1129 C  CB  . GLN   A 1 146 ? -6.042  54.432  21.620  1.00 38.37  ? 998  GLN   A CB  1 
ATOM   1130 C  CG  . GLN   A 1 146 ? -6.297  55.116  22.941  1.00 36.15  ? 998  GLN   A CG  1 
ATOM   1131 C  CD  . GLN   A 1 146 ? -7.774  55.057  23.325  1.00 50.80  ? 998  GLN   A CD  1 
ATOM   1132 O  OE1 . GLN   A 1 146 ? -8.420  56.090  23.503  1.00 57.22  ? 998  GLN   A OE1 1 
ATOM   1133 N  NE2 . GLN   A 1 146 ? -8.315  53.844  23.430  1.00 47.90  ? 998  GLN   A NE2 1 
ATOM   1134 N  N   . TYR   A 1 147 ? -3.294  54.153  19.074  1.00 29.41  ? 999  TYR   A N   1 
ATOM   1135 C  CA  . TYR   A 1 147 ? -2.828  53.309  17.973  1.00 28.89  ? 999  TYR   A CA  1 
ATOM   1136 C  C   . TYR   A 1 147 ? -1.429  52.793  18.246  1.00 28.09  ? 999  TYR   A C   1 
ATOM   1137 O  O   . TYR   A 1 147 ? -0.616  53.483  18.882  1.00 28.74  ? 999  TYR   A O   1 
ATOM   1138 C  CB  . TYR   A 1 147 ? -2.760  54.087  16.661  1.00 26.77  ? 999  TYR   A CB  1 
ATOM   1139 C  CG  . TYR   A 1 147 ? -4.071  54.579  16.145  1.00 25.58  ? 999  TYR   A CG  1 
ATOM   1140 C  CD1 . TYR   A 1 147 ? -5.020  53.703  15.643  1.00 25.76  ? 999  TYR   A CD1 1 
ATOM   1141 C  CD2 . TYR   A 1 147 ? -4.367  55.945  16.152  1.00 31.59  ? 999  TYR   A CD2 1 
ATOM   1142 C  CE1 . TYR   A 1 147 ? -6.238  54.168  15.170  1.00 26.45  ? 999  TYR   A CE1 1 
ATOM   1143 C  CE2 . TYR   A 1 147 ? -5.573  56.416  15.683  1.00 28.60  ? 999  TYR   A CE2 1 
ATOM   1144 C  CZ  . TYR   A 1 147 ? -6.502  55.536  15.197  1.00 29.52  ? 999  TYR   A CZ  1 
ATOM   1145 O  OH  . TYR   A 1 147 ? -7.687  56.029  14.726  1.00 34.74  ? 999  TYR   A OH  1 
ATOM   1146 N  N   . VAL   A 1 148 ? -1.168  51.590  17.732  1.00 29.16  ? 1000 VAL   A N   1 
ATOM   1147 C  CA  . VAL   A 1 148 ? 0.183   51.036  17.624  1.00 28.86  ? 1000 VAL   A CA  1 
ATOM   1148 C  C   . VAL   A 1 148 ? 0.546   50.984  16.151  1.00 23.38  ? 1000 VAL   A C   1 
ATOM   1149 O  O   . VAL   A 1 148 ? -0.232  50.518  15.326  1.00 23.56  ? 1000 VAL   A O   1 
ATOM   1150 C  CB  . VAL   A 1 148 ? 0.353   49.613  18.252  1.00 31.87  ? 1000 VAL   A CB  1 
ATOM   1151 C  CG1 . VAL   A 1 148 ? 0.521   49.728  19.732  1.00 37.58  ? 1000 VAL   A CG1 1 
ATOM   1152 C  CG2 . VAL   A 1 148 ? -0.795  48.662  17.883  1.00 36.14  ? 1000 VAL   A CG2 1 
ATOM   1153 N  N   . HIS   A 1 149 ? 1.740   51.475  15.833  1.00 20.34  ? 1001 HIS   A N   1 
ATOM   1154 C  CA  . HIS   A 1 149 ? 2.182   51.611  14.471  1.00 20.72  ? 1001 HIS   A CA  1 
ATOM   1155 C  C   . HIS   A 1 149 ? 2.590   50.276  13.879  1.00 22.24  ? 1001 HIS   A C   1 
ATOM   1156 O  O   . HIS   A 1 149 ? 2.182   49.937  12.771  1.00 20.03  ? 1001 HIS   A O   1 
ATOM   1157 C  CB  . HIS   A 1 149 ? 3.357   52.593  14.381  1.00 19.97  ? 1001 HIS   A CB  1 
ATOM   1158 C  CG  . HIS   A 1 149 ? 3.726   52.937  12.971  1.00 18.83  ? 1001 HIS   A CG  1 
ATOM   1159 N  ND1 . HIS   A 1 149 ? 4.664   52.225  12.256  1.00 19.51  ? 1001 HIS   A ND1 1 
ATOM   1160 C  CD2 . HIS   A 1 149 ? 3.279   53.912  12.142  1.00 20.05  ? 1001 HIS   A CD2 1 
ATOM   1161 C  CE1 . HIS   A 1 149 ? 4.765   52.733  11.039  1.00 22.40  ? 1001 HIS   A CE1 1 
ATOM   1162 N  NE2 . HIS   A 1 149 ? 3.936   53.759  10.945  1.00 16.83  ? 1001 HIS   A NE2 1 
ATOM   1163 N  N   . ARG   A 1 150 ? 3.416   49.535  14.618  1.00 22.51  ? 1002 ARG   A N   1 
ATOM   1164 C  CA  . ARG   A 1 150 ? 3.828   48.164  14.230  1.00 22.80  ? 1002 ARG   A CA  1 
ATOM   1165 C  C   . ARG   A 1 150 ? 4.780   48.058  13.043  1.00 24.89  ? 1002 ARG   A C   1 
ATOM   1166 O  O   . ARG   A 1 150 ? 5.112   46.959  12.621  1.00 27.26  ? 1002 ARG   A O   1 
ATOM   1167 C  CB  . ARG   A 1 150 ? 2.630   47.225  13.995  1.00 26.07  ? 1002 ARG   A CB  1 
ATOM   1168 C  CG  . ARG   A 1 150 ? 1.566   47.274  15.039  1.00 25.28  ? 1002 ARG   A CG  1 
ATOM   1169 C  CD  . ARG   A 1 150 ? 0.729   45.988  15.004  1.00 30.67  ? 1002 ARG   A CD  1 
ATOM   1170 N  NE  . ARG   A 1 150 ? 0.058   45.785  13.714  1.00 39.23  ? 1002 ARG   A NE  1 
ATOM   1171 C  CZ  . ARG   A 1 150 ? 0.245   44.779  12.848  1.00 47.68  ? 1002 ARG   A CZ  1 
ATOM   1172 N  NH1 . ARG   A 1 150 ? -0.472  44.750  11.723  1.00 48.41  ? 1002 ARG   A NH1 1 
ATOM   1173 N  NH2 . ARG   A 1 150 ? 1.124   43.801  13.066  1.00 53.55  ? 1002 ARG   A NH2 1 
ATOM   1174 N  N   . ASP   A 1 151 ? 5.252   49.186  12.519  1.00 22.41  ? 1003 ASP   A N   1 
ATOM   1175 C  CA  . ASP   A 1 151 ? 6.145   49.169  11.365  1.00 24.18  ? 1003 ASP   A CA  1 
ATOM   1176 C  C   . ASP   A 1 151 ? 7.116   50.368  11.375  1.00 21.82  ? 1003 ASP   A C   1 
ATOM   1177 O  O   . ASP   A 1 151 ? 7.445   50.915  10.320  1.00 22.54  ? 1003 ASP   A O   1 
ATOM   1178 C  CB  . ASP   A 1 151 ? 5.282   49.166  10.102  1.00 25.02  ? 1003 ASP   A CB  1 
ATOM   1179 C  CG  . ASP   A 1 151 ? 5.999   48.649  8.880   1.00 28.79  ? 1003 ASP   A CG  1 
ATOM   1180 O  OD1 . ASP   A 1 151 ? 6.989   47.910  9.007   1.00 33.91  ? 1003 ASP   A OD1 1 
ATOM   1181 O  OD2 . ASP   A 1 151 ? 5.554   48.969  7.774   1.00 29.60  ? 1003 ASP   A OD2 1 
ATOM   1182 N  N   . LEU   A 1 152 ? 7.551   50.769  12.573  1.00 20.24  ? 1004 LEU   A N   1 
ATOM   1183 C  CA  . LEU   A 1 152 ? 8.412   51.926  12.753  1.00 18.00  ? 1004 LEU   A CA  1 
ATOM   1184 C  C   . LEU   A 1 152 ? 9.843   51.530  12.409  1.00 19.69  ? 1004 LEU   A C   1 
ATOM   1185 O  O   . LEU   A 1 152 ? 10.474  50.776  13.140  1.00 20.54  ? 1004 LEU   A O   1 
ATOM   1186 C  CB  . LEU   A 1 152 ? 8.354   52.479  14.179  1.00 16.73  ? 1004 LEU   A CB  1 
ATOM   1187 C  CG  . LEU   A 1 152 ? 9.195   53.737  14.455  1.00 21.40  ? 1004 LEU   A CG  1 
ATOM   1188 C  CD1 . LEU   A 1 152 ? 8.836   54.886  13.527  1.00 26.27  ? 1004 LEU   A CD1 1 
ATOM   1189 C  CD2 . LEU   A 1 152 ? 9.047   54.153  15.943  1.00 19.34  ? 1004 LEU   A CD2 1 
ATOM   1190 N  N   . ALA   A 1 153 ? 10.283  51.996  11.248  1.00 16.56  ? 1005 ALA   A N   1 
ATOM   1191 C  CA  . ALA   A 1 153 ? 11.637  51.789  10.749  1.00 18.56  ? 1005 ALA   A CA  1 
ATOM   1192 C  C   . ALA   A 1 153 ? 11.974  53.023  9.939   1.00 17.92  ? 1005 ALA   A C   1 
ATOM   1193 O  O   . ALA   A 1 153 ? 11.077  53.774  9.528   1.00 16.37  ? 1005 ALA   A O   1 
ATOM   1194 C  CB  . ALA   A 1 153 ? 11.723  50.551  9.896   1.00 21.29  ? 1005 ALA   A CB  1 
ATOM   1195 N  N   . ALA   A 1 154 ? 13.268  53.243  9.710   1.00 18.15  ? 1006 ALA   A N   1 
ATOM   1196 C  CA  . ALA   A 1 154 ? 13.720  54.405  8.941   1.00 17.30  ? 1006 ALA   A CA  1 
ATOM   1197 C  C   . ALA   A 1 154 ? 13.091  54.507  7.566   1.00 18.67  ? 1006 ALA   A C   1 
ATOM   1198 O  O   . ALA   A 1 154 ? 12.885  55.617  7.083   1.00 21.50  ? 1006 ALA   A O   1 
ATOM   1199 C  CB  . ALA   A 1 154 ? 15.230  54.412  8.781   1.00 15.95  ? 1006 ALA   A CB  1 
ATOM   1200 N  N   . ARG   A 1 155 ? 12.817  53.362  6.931   1.00 19.39  ? 1007 ARG   A N   1 
ATOM   1201 C  CA  . ARG   A 1 155 ? 12.218  53.318  5.606   1.00 22.19  ? 1007 ARG   A CA  1 
ATOM   1202 C  C   . ARG   A 1 155 ? 10.812  53.941  5.604   1.00 19.68  ? 1007 ARG   A C   1 
ATOM   1203 O  O   . ARG   A 1 155 ? 10.340  54.331  4.554   1.00 23.22  ? 1007 ARG   A O   1 
ATOM   1204 C  CB  . ARG   A 1 155 ? 12.166  51.886  5.061   1.00 24.53  ? 1007 ARG   A CB  1 
ATOM   1205 C  CG  . ARG   A 1 155 ? 11.198  50.955  5.787   1.00 27.73  ? 1007 ARG   A CG  1 
ATOM   1206 C  CD  . ARG   A 1 155 ? 11.287  49.511  5.273   1.00 39.64  ? 1007 ARG   A CD  1 
ATOM   1207 N  NE  . ARG   A 1 155 ? 10.914  48.583  6.338   1.00 40.90  ? 1007 ARG   A NE  1 
ATOM   1208 C  CZ  . ARG   A 1 155 ? 9.667   48.334  6.741   1.00 44.53  ? 1007 ARG   A CZ  1 
ATOM   1209 N  NH1 . ARG   A 1 155 ? 9.459   47.487  7.742   1.00 48.06  ? 1007 ARG   A NH1 1 
ATOM   1210 N  NH2 . ARG   A 1 155 ? 8.616   48.905  6.147   1.00 48.09  ? 1007 ARG   A NH2 1 
ATOM   1211 N  N   . ASN   A 1 156 ? 10.168  54.013  6.773   1.00 18.21  ? 1008 ASN   A N   1 
ATOM   1212 C  CA  . ASN   A 1 156 ? 8.839   54.632  6.912   1.00 17.51  ? 1008 ASN   A CA  1 
ATOM   1213 C  C   . ASN   A 1 156 ? 8.841   56.059  7.469   1.00 15.82  ? 1008 ASN   A C   1 
ATOM   1214 O  O   . ASN   A 1 156 ? 7.761   56.611  7.731   1.00 16.55  ? 1008 ASN   A O   1 
ATOM   1215 C  CB  . ASN   A 1 156 ? 7.900   53.696  7.703   1.00 16.18  ? 1008 ASN   A CB  1 
ATOM   1216 C  CG  . ASN   A 1 156 ? 7.509   52.452  6.906   1.00 21.89  ? 1008 ASN   A CG  1 
ATOM   1217 O  OD1 . ASN   A 1 156 ? 7.357   52.514  5.694   1.00 24.19  ? 1008 ASN   A OD1 1 
ATOM   1218 N  ND2 . ASN   A 1 156 ? 7.333   51.329  7.590   1.00 20.79  ? 1008 ASN   A ND2 1 
ATOM   1219 N  N   . VAL   A 1 157 ? 10.033  56.669  7.587   1.00 14.04  ? 1009 VAL   A N   1 
ATOM   1220 C  CA  . VAL   A 1 157 ? 10.182  58.042  8.020   1.00 15.36  ? 1009 VAL   A CA  1 
ATOM   1221 C  C   . VAL   A 1 157 ? 10.611  58.901  6.839   1.00 19.62  ? 1009 VAL   A C   1 
ATOM   1222 O  O   . VAL   A 1 157 ? 11.684  58.667  6.255   1.00 21.25  ? 1009 VAL   A O   1 
ATOM   1223 C  CB  . VAL   A 1 157 ? 11.190  58.168  9.193   1.00 16.42  ? 1009 VAL   A CB  1 
ATOM   1224 C  CG1 . VAL   A 1 157 ? 11.303  59.614  9.674   1.00 17.34  ? 1009 VAL   A CG1 1 
ATOM   1225 C  CG2 . VAL   A 1 157 ? 10.787  57.289  10.321  1.00 17.81  ? 1009 VAL   A CG2 1 
ATOM   1226 N  N   . LEU   A 1 158 ? 9.767   59.888  6.512   1.00 17.43  ? 1010 LEU   A N   1 
ATOM   1227 C  CA  . LEU   A 1 158 ? 9.952   60.799  5.384   1.00 18.14  ? 1010 LEU   A CA  1 
ATOM   1228 C  C   . LEU   A 1 158 ? 10.693  62.053  5.801   1.00 18.58  ? 1010 LEU   A C   1 
ATOM   1229 O  O   . LEU   A 1 158 ? 10.558  62.514  6.951   1.00 15.04  ? 1010 LEU   A O   1 
ATOM   1230 C  CB  . LEU   A 1 158 ? 8.599   61.213  4.776   1.00 19.97  ? 1010 LEU   A CB  1 
ATOM   1231 C  CG  . LEU   A 1 158 ? 7.736   60.115  4.102   1.00 14.35  ? 1010 LEU   A CG  1 
ATOM   1232 C  CD1 . LEU   A 1 158 ? 6.373   60.622  3.636   1.00 19.47  ? 1010 LEU   A CD1 1 
ATOM   1233 C  CD2 . LEU   A 1 158 ? 8.464   59.463  2.959   1.00 17.38  ? 1010 LEU   A CD2 1 
ATOM   1234 N  N   . VAL   A 1 159 ? 11.450  62.610  4.848   1.00 16.21  ? 1011 VAL   A N   1 
ATOM   1235 C  CA  . VAL   A 1 159 ? 12.185  63.842  5.058   1.00 19.49  ? 1011 VAL   A CA  1 
ATOM   1236 C  C   . VAL   A 1 159 ? 11.410  64.978  4.429   1.00 17.75  ? 1011 VAL   A C   1 
ATOM   1237 O  O   . VAL   A 1 159 ? 11.323  65.074  3.210   1.00 22.07  ? 1011 VAL   A O   1 
ATOM   1238 C  CB  . VAL   A 1 159 ? 13.617  63.733  4.495   1.00 17.42  ? 1011 VAL   A CB  1 
ATOM   1239 C  CG1 . VAL   A 1 159 ? 14.356  65.045  4.618   1.00 20.44  ? 1011 VAL   A CG1 1 
ATOM   1240 C  CG2 . VAL   A 1 159 ? 14.364  62.611  5.224   1.00 18.85  ? 1011 VAL   A CG2 1 
ATOM   1241 N  N   . GLU   A 1 160 ? 10.839  65.835  5.275   1.00 19.34  ? 1012 GLU   A N   1 
ATOM   1242 C  CA  . GLU   A 1 160 ? 10.138  67.056  4.853   1.00 23.12  ? 1012 GLU   A CA  1 
ATOM   1243 C  C   . GLU   A 1 160 ? 11.172  68.107  4.437   1.00 25.26  ? 1012 GLU   A C   1 
ATOM   1244 O  O   . GLU   A 1 160 ? 11.051  68.751  3.403   1.00 27.28  ? 1012 GLU   A O   1 
ATOM   1245 C  CB  . GLU   A 1 160 ? 9.274   67.600  6.004   1.00 23.53  ? 1012 GLU   A CB  1 
ATOM   1246 C  CG  . GLU   A 1 160 ? 8.657   69.003  5.824   1.00 26.18  ? 1012 GLU   A CG  1 
ATOM   1247 C  CD  . GLU   A 1 160 ? 7.719   69.128  4.646   1.00 32.34  ? 1012 GLU   A CD  1 
ATOM   1248 O  OE1 . GLU   A 1 160 ? 7.081   68.125  4.251   1.00 29.99  ? 1012 GLU   A OE1 1 
ATOM   1249 O  OE2 . GLU   A 1 160 ? 7.601   70.257  4.117   1.00 42.80  ? 1012 GLU   A OE2 1 
ATOM   1250 N  N   . SER   A 1 161 ? 12.178  68.276  5.278   1.00 26.12  ? 1013 SER   A N   1 
ATOM   1251 C  CA  . SER   A 1 161 ? 13.321  69.149  4.974   1.00 26.95  ? 1013 SER   A CA  1 
ATOM   1252 C  C   . SER   A 1 161 ? 14.534  68.658  5.754   1.00 24.70  ? 1013 SER   A C   1 
ATOM   1253 O  O   . SER   A 1 161 ? 14.442  67.751  6.591   1.00 22.06  ? 1013 SER   A O   1 
ATOM   1254 C  CB  . SER   A 1 161 ? 12.991  70.597  5.364   1.00 29.04  ? 1013 SER   A CB  1 
ATOM   1255 O  OG  . SER   A 1 161 ? 12.979  70.745  6.795   1.00 26.80  ? 1013 SER   A OG  1 
ATOM   1256 N  N   . GLU   A 1 162 ? 15.670  69.309  5.534   1.00 27.05  ? 1014 GLU   A N   1 
ATOM   1257 C  CA  . GLU   A 1 162 ? 16.853  69.098  6.373   1.00 24.65  ? 1014 GLU   A CA  1 
ATOM   1258 C  C   . GLU   A 1 162 ? 16.550  69.198  7.881   1.00 19.60  ? 1014 GLU   A C   1 
ATOM   1259 O  O   . GLU   A 1 162 ? 17.271  68.638  8.694   1.00 21.15  ? 1014 GLU   A O   1 
ATOM   1260 C  CB  . GLU   A 1 162 ? 17.909  70.143  6.005   1.00 26.42  ? 1014 GLU   A CB  1 
ATOM   1261 C  CG  . GLU   A 1 162 ? 19.286  69.871  6.528   1.00 34.73  ? 1014 GLU   A CG  1 
ATOM   1262 C  CD  . GLU   A 1 162 ? 20.183  71.075  6.369   1.00 35.48  ? 1014 GLU   A CD  1 
ATOM   1263 O  OE1 . GLU   A 1 162 ? 20.128  71.704  5.276   1.00 32.58  ? 1014 GLU   A OE1 1 
ATOM   1264 O  OE2 . GLU   A 1 162 ? 20.920  71.387  7.337   1.00 34.41  ? 1014 GLU   A OE2 1 
ATOM   1265 N  N   . HIS   A 1 163 ? 15.516  69.965  8.241   1.00 21.52  ? 1015 HIS   A N   1 
ATOM   1266 C  CA  . HIS   A 1 163 ? 15.166  70.235  9.635   1.00 23.74  ? 1015 HIS   A CA  1 
ATOM   1267 C  C   . HIS   A 1 163 ? 13.923  69.491  10.140  1.00 22.19  ? 1015 HIS   A C   1 
ATOM   1268 O  O   . HIS   A 1 163 ? 13.544  69.662  11.293  1.00 18.21  ? 1015 HIS   A O   1 
ATOM   1269 C  CB  . HIS   A 1 163 ? 14.965  71.744  9.833   1.00 23.67  ? 1015 HIS   A CB  1 
ATOM   1270 C  CG  . HIS   A 1 163 ? 16.098  72.575  9.307   1.00 33.55  ? 1015 HIS   A CG  1 
ATOM   1271 N  ND1 . HIS   A 1 163 ? 17.346  72.595  9.898   1.00 35.39  ? 1015 HIS   A ND1 1 
ATOM   1272 C  CD2 . HIS   A 1 163 ? 16.180  73.388  8.228   1.00 38.23  ? 1015 HIS   A CD2 1 
ATOM   1273 C  CE1 . HIS   A 1 163 ? 18.146  73.386  9.206   1.00 31.60  ? 1015 HIS   A CE1 1 
ATOM   1274 N  NE2 . HIS   A 1 163 ? 17.463  73.882  8.189   1.00 39.12  ? 1015 HIS   A NE2 1 
ATOM   1275 N  N   . GLN   A 1 164 ? 13.280  68.666  9.303   1.00 18.71  ? 1016 GLN   A N   1 
ATOM   1276 C  CA  . GLN   A 1 164 ? 12.022  68.054  9.724   1.00 17.85  ? 1016 GLN   A CA  1 
ATOM   1277 C  C   . GLN   A 1 164 ? 11.753  66.703  9.068   1.00 17.85  ? 1016 GLN   A C   1 
ATOM   1278 O  O   . GLN   A 1 164 ? 11.891  66.558  7.860   1.00 17.20  ? 1016 GLN   A O   1 
ATOM   1279 C  CB  . GLN   A 1 164 ? 10.873  69.009  9.428   1.00 19.47  ? 1016 GLN   A CB  1 
ATOM   1280 C  CG  . GLN   A 1 164 ? 9.517   68.589  9.998   1.00 24.95  ? 1016 GLN   A CG  1 
ATOM   1281 C  CD  . GLN   A 1 164 ? 8.389   69.498  9.541   1.00 27.85  ? 1016 GLN   A CD  1 
ATOM   1282 O  OE1 . GLN   A 1 164 ? 8.618   70.495  8.878   1.00 37.35  ? 1016 GLN   A OE1 1 
ATOM   1283 N  NE2 . GLN   A 1 164 ? 7.164   69.151  9.895   1.00 26.36  ? 1016 GLN   A NE2 1 
ATOM   1284 N  N   . VAL   A 1 165 ? 11.326  65.737  9.886   1.00 17.26  ? 1017 VAL   A N   1 
ATOM   1285 C  CA  . VAL   A 1 165 ? 10.882  64.447  9.372   1.00 15.36  ? 1017 VAL   A CA  1 
ATOM   1286 C  C   . VAL   A 1 165 ? 9.399   64.227  9.711   1.00 16.33  ? 1017 VAL   A C   1 
ATOM   1287 O  O   . VAL   A 1 165 ? 8.837   64.891  10.578  1.00 15.24  ? 1017 VAL   A O   1 
ATOM   1288 C  CB  . VAL   A 1 165 ? 11.736  63.262  9.857   1.00 15.70  ? 1017 VAL   A CB  1 
ATOM   1289 C  CG1 . VAL   A 1 165 ? 13.146  63.317  9.268   1.00 18.64  ? 1017 VAL   A CG1 1 
ATOM   1290 C  CG2 . VAL   A 1 165 ? 11.775  63.141  11.404  1.00 16.15  ? 1017 VAL   A CG2 1 
ATOM   1291 N  N   . LYS   A 1 166 ? 8.792   63.276  9.014   1.00 15.10  ? 1018 LYS   A N   1 
ATOM   1292 C  CA  . LYS   A 1 166 ? 7.405   62.888  9.295   1.00 15.87  ? 1018 LYS   A CA  1 
ATOM   1293 C  C   . LYS   A 1 166 ? 7.268   61.378  9.148   1.00 17.95  ? 1018 LYS   A C   1 
ATOM   1294 O  O   . LYS   A 1 166 ? 7.821   60.789  8.206   1.00 17.64  ? 1018 LYS   A O   1 
ATOM   1295 C  CB  . LYS   A 1 166 ? 6.407   63.527  8.340   1.00 16.71  ? 1018 LYS   A CB  1 
ATOM   1296 C  CG  . LYS   A 1 166 ? 6.458   65.076  8.194   1.00 15.30  ? 1018 LYS   A CG  1 
ATOM   1297 C  CD  . LYS   A 1 166 ? 5.226   65.591  7.509   1.00 14.16  ? 1018 LYS   A CD  1 
ATOM   1298 C  CE  . LYS   A 1 166 ? 5.288   67.096  7.209   1.00 20.74  ? 1018 LYS   A CE  1 
ATOM   1299 N  NZ  . LYS   A 1 166 ? 4.031   67.644  6.598   1.00 21.73  ? 1018 LYS   A NZ  1 
ATOM   1300 N  N   . ILE   A 1 167 ? 6.483   60.780  10.034  1.00 15.78  ? 1019 ILE   A N   1 
ATOM   1301 C  CA  . ILE   A 1 167 ? 6.124   59.360  9.860   1.00 14.52  ? 1019 ILE   A CA  1 
ATOM   1302 C  C   . ILE   A 1 167 ? 5.225   59.294  8.619   1.00 16.23  ? 1019 ILE   A C   1 
ATOM   1303 O  O   . ILE   A 1 167 ? 4.227   60.028  8.493   1.00 15.32  ? 1019 ILE   A O   1 
ATOM   1304 C  CB  . ILE   A 1 167 ? 5.436   58.745  11.091  1.00 17.63  ? 1019 ILE   A CB  1 
ATOM   1305 C  CG1 . ILE   A 1 167 ? 6.316   58.891  12.340  1.00 16.72  ? 1019 ILE   A CG1 1 
ATOM   1306 C  CG2 . ILE   A 1 167 ? 5.143   57.270  10.863  1.00 17.70  ? 1019 ILE   A CG2 1 
ATOM   1307 C  CD1 . ILE   A 1 167 ? 5.563   58.781  13.613  1.00 24.42  ? 1019 ILE   A CD1 1 
ATOM   1308 N  N   . GLY   A 1 168 ? 5.614   58.421  7.688   1.00 13.34  ? 1020 GLY   A N   1 
ATOM   1309 C  CA  . GLY   A 1 168 ? 5.136   58.460  6.330   1.00 15.23  ? 1020 GLY   A CA  1 
ATOM   1310 C  C   . GLY   A 1 168 ? 4.248   57.354  5.817   1.00 16.59  ? 1020 GLY   A C   1 
ATOM   1311 O  O   . GLY   A 1 168 ? 3.772   57.435  4.702   1.00 14.02  ? 1020 GLY   A O   1 
ATOM   1312 N  N   . ASP   A 1 169 ? 4.055   56.302  6.600   1.00 18.41  ? 1021 ASP   A N   1 
ATOM   1313 C  CA  . ASP   A 1 169 ? 3.168   55.221  6.179   1.00 20.08  ? 1021 ASP   A CA  1 
ATOM   1314 C  C   . ASP   A 1 169 ? 2.536   54.610  7.412   1.00 16.63  ? 1021 ASP   A C   1 
ATOM   1315 O  O   . ASP   A 1 169 ? 3.193   54.523  8.435   1.00 17.66  ? 1021 ASP   A O   1 
ATOM   1316 C  CB  . ASP   A 1 169 ? 3.984   54.177  5.419   1.00 18.11  ? 1021 ASP   A CB  1 
ATOM   1317 C  CG  . ASP   A 1 169 ? 3.138   53.078  4.870   1.00 24.98  ? 1021 ASP   A CG  1 
ATOM   1318 O  OD1 . ASP   A 1 169 ? 2.587   53.242  3.755   1.00 20.36  ? 1021 ASP   A OD1 1 
ATOM   1319 O  OD2 . ASP   A 1 169 ? 3.015   52.059  5.583   1.00 23.28  ? 1021 ASP   A OD2 1 
ATOM   1320 N  N   . PHE   A 1 170 ? 1.290   54.152  7.270   1.00 20.45  ? 1022 PHE   A N   1 
ATOM   1321 C  CA  . PHE   A 1 170 ? 0.506   53.577  8.366   1.00 19.41  ? 1022 PHE   A CA  1 
ATOM   1322 C  C   . PHE   A 1 170 ? -0.147  52.262  7.962   1.00 20.26  ? 1022 PHE   A C   1 
ATOM   1323 O  O   . PHE   A 1 170 ? -1.201  51.906  8.469   1.00 21.87  ? 1022 PHE   A O   1 
ATOM   1324 C  CB  . PHE   A 1 170 ? -0.517  54.610  8.854   1.00 19.77  ? 1022 PHE   A CB  1 
ATOM   1325 C  CG  . PHE   A 1 170 ? 0.148   55.827  9.395   1.00 15.24  ? 1022 PHE   A CG  1 
ATOM   1326 C  CD1 . PHE   A 1 170 ? 0.546   56.847  8.539   1.00 16.28  ? 1022 PHE   A CD1 1 
ATOM   1327 C  CD2 . PHE   A 1 170 ? 0.507   55.898  10.736  1.00 17.15  ? 1022 PHE   A CD2 1 
ATOM   1328 C  CE1 . PHE   A 1 170 ? 1.224   57.944  9.026   1.00 13.28  ? 1022 PHE   A CE1 1 
ATOM   1329 C  CE2 . PHE   A 1 170 ? 1.190   57.004  11.241  1.00 21.73  ? 1022 PHE   A CE2 1 
ATOM   1330 C  CZ  . PHE   A 1 170 ? 1.562   58.022  10.375  1.00 14.91  ? 1022 PHE   A CZ  1 
ATOM   1331 N  N   . GLY   A 1 171 ? 0.522   51.545  7.058   1.00 19.14  ? 1023 GLY   A N   1 
ATOM   1332 C  CA  . GLY   A 1 171 ? 0.034   50.287  6.505   1.00 25.15  ? 1023 GLY   A CA  1 
ATOM   1333 C  C   . GLY   A 1 171 ? -0.335  49.196  7.498   1.00 25.09  ? 1023 GLY   A C   1 
ATOM   1334 O  O   . GLY   A 1 171 ? -1.242  48.397  7.221   1.00 27.12  ? 1023 GLY   A O   1 
ATOM   1335 N  N   . LEU   A 1 172 ? 0.364   49.155  8.635   1.00 24.51  ? 1024 LEU   A N   1 
ATOM   1336 C  CA  . LEU   A 1 172 ? 0.148   48.130  9.664   1.00 27.90  ? 1024 LEU   A CA  1 
ATOM   1337 C  C   . LEU   A 1 172 ? -0.483  48.683  10.942  1.00 28.41  ? 1024 LEU   A C   1 
ATOM   1338 O  O   . LEU   A 1 172 ? -0.618  47.964  11.917  1.00 28.28  ? 1024 LEU   A O   1 
ATOM   1339 C  CB  . LEU   A 1 172 ? 1.483   47.431  10.001  1.00 26.52  ? 1024 LEU   A CB  1 
ATOM   1340 C  CG  . LEU   A 1 172 ? 2.178   46.642  8.881   1.00 30.83  ? 1024 LEU   A CG  1 
ATOM   1341 C  CD1 . LEU   A 1 172 ? 3.409   45.918  9.429   1.00 37.71  ? 1024 LEU   A CD1 1 
ATOM   1342 C  CD2 . LEU   A 1 172 ? 1.259   45.630  8.241   1.00 36.11  ? 1024 LEU   A CD2 1 
ATOM   1343 N  N   . THR   A 1 173 ? -0.900  49.948  10.939  1.00 25.65  ? 1025 THR   A N   1 
ATOM   1344 C  CA  . THR   A 1 173 ? -1.308  50.617  12.170  1.00 24.37  ? 1025 THR   A CA  1 
ATOM   1345 C  C   . THR   A 1 173 ? -2.649  50.074  12.686  1.00 25.72  ? 1025 THR   A C   1 
ATOM   1346 O  O   . THR   A 1 173 ? -3.589  49.904  11.902  1.00 25.17  ? 1025 THR   A O   1 
ATOM   1347 C  CB  . THR   A 1 173 ? -1.391  52.160  11.956  1.00 22.45  ? 1025 THR   A CB  1 
ATOM   1348 O  OG1 . THR   A 1 173 ? -0.069  52.675  11.762  1.00 23.52  ? 1025 THR   A OG1 1 
ATOM   1349 C  CG2 . THR   A 1 173 ? -2.038  52.881  13.144  1.00 26.13  ? 1025 THR   A CG2 1 
ATOM   1350 N  N   . LYS   A 1 174 ? -2.727  49.819  13.993  1.00 27.41  ? 1026 LYS   A N   1 
ATOM   1351 C  CA  . LYS   A 1 174 ? -3.920  49.210  14.622  1.00 30.85  ? 1026 LYS   A CA  1 
ATOM   1352 C  C   . LYS   A 1 174 ? -4.357  49.966  15.862  1.00 30.50  ? 1026 LYS   A C   1 
ATOM   1353 O  O   . LYS   A 1 174 ? -3.519  50.490  16.586  1.00 28.33  ? 1026 LYS   A O   1 
ATOM   1354 C  CB  . LYS   A 1 174 ? -3.630  47.756  15.042  1.00 33.72  ? 1026 LYS   A CB  1 
ATOM   1355 C  CG  . LYS   A 1 174 ? -3.310  46.820  13.897  1.00 35.64  ? 1026 LYS   A CG  1 
ATOM   1356 C  CD  . LYS   A 1 174 ? -4.506  46.499  13.017  1.00 42.09  ? 1026 LYS   A CD  1 
ATOM   1357 C  CE  . LYS   A 1 174 ? -4.099  45.563  11.879  1.00 41.31  ? 1026 LYS   A CE  1 
ATOM   1358 N  NZ  . LYS   A 1 174 ? -5.274  44.975  11.206  1.00 36.49  ? 1026 LYS   A NZ  1 
ATOM   1359 N  N   . ALA   A 1 175 ? -5.671  49.997  16.115  1.00 32.79  ? 1027 ALA   A N   1 
ATOM   1360 C  CA  . ALA   A 1 175 ? -6.213  50.529  17.373  1.00 32.65  ? 1027 ALA   A CA  1 
ATOM   1361 C  C   . ALA   A 1 175 ? -6.009  49.545  18.535  1.00 36.56  ? 1027 ALA   A C   1 
ATOM   1362 O  O   . ALA   A 1 175 ? -6.207  48.346  18.369  1.00 41.24  ? 1027 ALA   A O   1 
ATOM   1363 C  CB  . ALA   A 1 175 ? -7.695  50.845  17.229  1.00 31.89  ? 1027 ALA   A CB  1 
ATOM   1364 N  N   . ILE   A 1 176 ? -5.599  50.064  19.695  1.00 36.05  ? 1028 ILE   A N   1 
ATOM   1365 C  CA  . ILE   A 1 176 ? -5.645  49.312  20.950  1.00 37.77  ? 1028 ILE   A CA  1 
ATOM   1366 C  C   . ILE   A 1 176 ? -6.999  49.582  21.617  1.00 41.22  ? 1028 ILE   A C   1 
ATOM   1367 O  O   . ILE   A 1 176 ? -7.415  50.730  21.782  1.00 39.20  ? 1028 ILE   A O   1 
ATOM   1368 C  CB  . ILE   A 1 176 ? -4.527  49.712  21.924  1.00 37.77  ? 1028 ILE   A CB  1 
ATOM   1369 C  CG1 . ILE   A 1 176 ? -3.150  49.493  21.271  1.00 39.67  ? 1028 ILE   A CG1 1 
ATOM   1370 C  CG2 . ILE   A 1 176 ? -4.628  48.911  23.227  1.00 37.41  ? 1028 ILE   A CG2 1 
ATOM   1371 C  CD1 . ILE   A 1 176 ? -1.960  49.551  22.247  1.00 46.06  ? 1028 ILE   A CD1 1 
ATOM   1372 N  N   . GLU   A 1 177 ? -7.656  48.516  22.045  1.00 45.93  ? 1029 GLU   A N   1 
ATOM   1373 C  CA  . GLU   A 1 177 ? -8.949  48.629  22.713  1.00 51.59  ? 1029 GLU   A CA  1 
ATOM   1374 C  C   . GLU   A 1 177 ? -8.844  49.452  24.010  1.00 52.44  ? 1029 GLU   A C   1 
ATOM   1375 O  O   . GLU   A 1 177 ? -7.846  49.375  24.730  1.00 51.97  ? 1029 GLU   A O   1 
ATOM   1376 C  CB  . GLU   A 1 177 ? -9.498  47.235  23.014  1.00 54.77  ? 1029 GLU   A CB  1 
ATOM   1377 C  CG  . GLU   A 1 177 ? -10.943 47.193  23.478  1.00 64.45  ? 1029 GLU   A CG  1 
ATOM   1378 C  CD  . GLU   A 1 177 ? -11.317 45.840  24.036  1.00 70.40  ? 1029 GLU   A CD  1 
ATOM   1379 O  OE1 . GLU   A 1 177 ? -10.774 44.825  23.553  1.00 75.38  ? 1029 GLU   A OE1 1 
ATOM   1380 O  OE2 . GLU   A 1 177 ? -12.149 45.791  24.965  1.00 82.96  ? 1029 GLU   A OE2 1 
ATOM   1381 N  N   . THR   A 1 178 ? -9.880  50.241  24.288  1.00 53.74  ? 1030 THR   A N   1 
ATOM   1382 C  CA  . THR   A 1 178 ? -9.947  51.051  25.506  1.00 55.65  ? 1030 THR   A CA  1 
ATOM   1383 C  C   . THR   A 1 178 ? -9.910  50.123  26.724  1.00 57.50  ? 1030 THR   A C   1 
ATOM   1384 O  O   . THR   A 1 178 ? -10.547 49.072  26.714  1.00 60.48  ? 1030 THR   A O   1 
ATOM   1385 C  CB  . THR   A 1 178 ? -11.217 51.926  25.522  1.00 57.82  ? 1030 THR   A CB  1 
ATOM   1386 O  OG1 . THR   A 1 178 ? -11.291 52.679  24.296  1.00 57.59  ? 1030 THR   A OG1 1 
ATOM   1387 C  CG2 . THR   A 1 178 ? -11.235 52.883  26.725  1.00 58.09  ? 1030 THR   A CG2 1 
ATOM   1388 N  N   . ASP   A 1 179 ? -9.122  50.512  27.732  1.00 58.61  ? 1031 ASP   A N   1 
ATOM   1389 C  CA  . ASP   A 1 179 ? -8.844  49.706  28.940  1.00 61.74  ? 1031 ASP   A CA  1 
ATOM   1390 C  C   . ASP   A 1 179 ? -8.038  48.406  28.692  1.00 61.36  ? 1031 ASP   A C   1 
ATOM   1391 O  O   . ASP   A 1 179 ? -8.001  47.528  29.560  1.00 62.34  ? 1031 ASP   A O   1 
ATOM   1392 C  CB  . ASP   A 1 179 ? -10.137 49.408  29.733  1.00 67.25  ? 1031 ASP   A CB  1 
ATOM   1393 C  CG  . ASP   A 1 179 ? -10.939 50.666  30.056  1.00 68.82  ? 1031 ASP   A CG  1 
ATOM   1394 O  OD1 . ASP   A 1 179 ? -10.331 51.693  30.434  1.00 76.20  ? 1031 ASP   A OD1 1 
ATOM   1395 O  OD2 . ASP   A 1 179 ? -12.180 50.625  29.931  1.00 73.93  ? 1031 ASP   A OD2 1 
ATOM   1396 N  N   . LYS   A 1 180 ? -7.389  48.291  27.530  1.00 54.70  ? 1032 LYS   A N   1 
ATOM   1397 C  CA  . LYS   A 1 180 ? -6.484  47.172  27.225  1.00 55.05  ? 1032 LYS   A CA  1 
ATOM   1398 C  C   . LYS   A 1 180 ? -5.111  47.716  26.857  1.00 50.43  ? 1032 LYS   A C   1 
ATOM   1399 O  O   . LYS   A 1 180 ? -5.007  48.811  26.299  1.00 50.24  ? 1032 LYS   A O   1 
ATOM   1400 C  CB  . LYS   A 1 180 ? -6.997  46.325  26.059  1.00 55.85  ? 1032 LYS   A CB  1 
ATOM   1401 C  CG  . LYS   A 1 180 ? -8.345  45.696  26.266  1.00 59.45  ? 1032 LYS   A CG  1 
ATOM   1402 C  CD  . LYS   A 1 180 ? -8.357  44.701  27.421  1.00 69.13  ? 1032 LYS   A CD  1 
ATOM   1403 C  CE  . LYS   A 1 180 ? -9.668  43.936  27.478  0.00 71.71  ? 1032 LYS   A CE  1 
ATOM   1404 N  NZ  . LYS   A 1 180 ? -9.700  42.958  28.600  0.00 76.24  ? 1032 LYS   A NZ  1 
ATOM   1405 N  N   . GLU   A 1 181 ? -4.073  46.931  27.139  1.00 48.57  ? 1033 GLU   A N   1 
ATOM   1406 C  CA  . GLU   A 1 181 ? -2.671  47.351  26.942  1.00 48.48  ? 1033 GLU   A CA  1 
ATOM   1407 C  C   . GLU   A 1 181 ? -2.051  46.940  25.604  1.00 44.87  ? 1033 GLU   A C   1 
ATOM   1408 O  O   . GLU   A 1 181 ? -0.970  47.418  25.274  1.00 41.97  ? 1033 GLU   A O   1 
ATOM   1409 C  CB  . GLU   A 1 181 ? -1.785  46.818  28.079  1.00 50.55  ? 1033 GLU   A CB  1 
ATOM   1410 C  CG  . GLU   A 1 181 ? -2.105  47.414  29.435  1.00 59.74  ? 1033 GLU   A CG  1 
ATOM   1411 C  CD  . GLU   A 1 181 ? -1.243  46.823  30.556  0.00 60.52  ? 1033 GLU   A CD  1 
ATOM   1412 O  OE1 . GLU   A 1 181 ? -0.016  46.683  30.364  0.00 59.51  ? 1033 GLU   A OE1 1 
ATOM   1413 O  OE2 . GLU   A 1 181 ? -1.795  46.516  31.634  0.00 64.53  ? 1033 GLU   A OE2 1 
HETATM 1414 N  N   . PTR   A 1 182 ? -2.705  46.063  24.843  1.00 45.06  ? 1034 PTR   A N   1 
HETATM 1415 C  CA  . PTR   A 1 182 ? -2.143  45.585  23.578  1.00 42.36  ? 1034 PTR   A CA  1 
HETATM 1416 C  C   . PTR   A 1 182 ? -3.141  45.086  22.548  1.00 43.91  ? 1034 PTR   A C   1 
HETATM 1417 O  O   . PTR   A 1 182 ? -4.297  44.845  22.863  1.00 44.75  ? 1034 PTR   A O   1 
HETATM 1418 C  CB  . PTR   A 1 182 ? -1.130  44.463  23.843  1.00 47.30  ? 1034 PTR   A CB  1 
HETATM 1419 C  CG  . PTR   A 1 182 ? -1.711  43.173  24.392  1.00 48.37  ? 1034 PTR   A CG  1 
HETATM 1420 C  CD1 . PTR   A 1 182 ? -1.601  42.869  25.746  1.00 55.57  ? 1034 PTR   A CD1 1 
HETATM 1421 C  CD2 . PTR   A 1 182 ? -2.316  42.227  23.554  1.00 45.63  ? 1034 PTR   A CD2 1 
HETATM 1422 C  CE1 . PTR   A 1 182 ? -2.106  41.685  26.266  1.00 57.73  ? 1034 PTR   A CE1 1 
HETATM 1423 C  CE2 . PTR   A 1 182 ? -2.831  41.035  24.068  1.00 54.56  ? 1034 PTR   A CE2 1 
HETATM 1424 C  CZ  . PTR   A 1 182 ? -2.730  40.769  25.424  1.00 57.87  ? 1034 PTR   A CZ  1 
HETATM 1425 O  OH  . PTR   A 1 182 ? -3.174  39.687  25.842  1.00 67.98  ? 1034 PTR   A OH  1 
HETATM 1426 P  P   . PTR   A 1 182 ? -4.143  39.499  27.114  1.00 74.99  ? 1034 PTR   A P   1 
HETATM 1427 O  O1P . PTR   A 1 182 ? -5.285  40.533  27.069  1.00 79.24  ? 1034 PTR   A O1P 1 
HETATM 1428 O  O2P . PTR   A 1 182 ? -3.339  39.680  28.341  1.00 75.40  ? 1034 PTR   A O2P 1 
HETATM 1429 O  O3P . PTR   A 1 182 ? -4.743  38.084  27.078  1.00 70.44  ? 1034 PTR   A O3P 1 
HETATM 1430 N  N   . PTR   A 1 183 ? -2.645  44.912  21.324  1.00 44.01  ? 1035 PTR   A N   1 
HETATM 1431 C  CA  . PTR   A 1 183 ? -3.398  44.372  20.200  1.00 45.15  ? 1035 PTR   A CA  1 
HETATM 1432 C  C   . PTR   A 1 183 ? -2.778  43.053  19.799  1.00 46.11  ? 1035 PTR   A C   1 
HETATM 1433 O  O   . PTR   A 1 183 ? -1.564  42.979  19.587  1.00 41.45  ? 1035 PTR   A O   1 
HETATM 1434 C  CB  . PTR   A 1 183 ? -3.284  45.285  18.979  1.00 44.64  ? 1035 PTR   A CB  1 
HETATM 1435 C  CG  . PTR   A 1 183 ? -3.938  44.732  17.729  1.00 46.26  ? 1035 PTR   A CG  1 
HETATM 1436 C  CD1 . PTR   A 1 183 ? -3.171  44.211  16.685  1.00 46.47  ? 1035 PTR   A CD1 1 
HETATM 1437 C  CD2 . PTR   A 1 183 ? -5.315  44.759  17.576  1.00 50.00  ? 1035 PTR   A CD2 1 
HETATM 1438 C  CE1 . PTR   A 1 183 ? -3.763  43.709  15.533  1.00 51.16  ? 1035 PTR   A CE1 1 
HETATM 1439 C  CE2 . PTR   A 1 183 ? -5.926  44.264  16.429  1.00 56.82  ? 1035 PTR   A CE2 1 
HETATM 1440 C  CZ  . PTR   A 1 183 ? -5.145  43.736  15.393  1.00 53.23  ? 1035 PTR   A CZ  1 
HETATM 1441 O  OH  . PTR   A 1 183 ? -5.597  43.269  14.325  1.00 55.80  ? 1035 PTR   A OH  1 
HETATM 1442 P  P   . PTR   A 1 183 ? -7.142  43.185  13.827  1.00 65.38  ? 1035 PTR   A P   1 
HETATM 1443 O  O1P . PTR   A 1 183 ? -7.244  42.330  12.549  1.00 58.76  ? 1035 PTR   A O1P 1 
HETATM 1444 O  O2P . PTR   A 1 183 ? -8.007  42.539  14.916  1.00 64.03  ? 1035 PTR   A O2P 1 
HETATM 1445 O  O3P . PTR   A 1 183 ? -7.637  44.555  13.548  1.00 60.12  ? 1035 PTR   A O3P 1 
ATOM   1446 N  N   . THR   A 1 184 ? -3.609  42.016  19.683  1.00 48.59  ? 1036 THR   A N   1 
ATOM   1447 C  CA  . THR   A 1 184 ? -3.135  40.704  19.268  1.00 51.72  ? 1036 THR   A CA  1 
ATOM   1448 C  C   . THR   A 1 184 ? -3.202  40.596  17.752  1.00 51.87  ? 1036 THR   A C   1 
ATOM   1449 O  O   . THR   A 1 184 ? -4.274  40.752  17.175  1.00 51.48  ? 1036 THR   A O   1 
ATOM   1450 C  CB  . THR   A 1 184 ? -3.971  39.574  19.894  1.00 56.28  ? 1036 THR   A CB  1 
ATOM   1451 O  OG1 . THR   A 1 184 ? -4.425  39.970  21.197  1.00 57.09  ? 1036 THR   A OG1 1 
ATOM   1452 C  CG2 . THR   A 1 184 ? -3.140  38.316  19.992  1.00 62.92  ? 1036 THR   A CG2 1 
ATOM   1453 N  N   . VAL   A 1 185 ? -2.058  40.346  17.109  1.00 53.14  ? 1037 VAL   A N   1 
ATOM   1454 C  CA  . VAL   A 1 185 ? -2.009  40.200  15.648  1.00 55.62  ? 1037 VAL   A CA  1 
ATOM   1455 C  C   . VAL   A 1 185 ? -2.306  38.761  15.230  1.00 61.17  ? 1037 VAL   A C   1 
ATOM   1456 O  O   . VAL   A 1 185 ? -1.654  37.826  15.694  1.00 62.88  ? 1037 VAL   A O   1 
ATOM   1457 C  CB  . VAL   A 1 185 ? -0.648  40.646  15.049  1.00 56.07  ? 1037 VAL   A CB  1 
ATOM   1458 C  CG1 . VAL   A 1 185 ? -0.494  42.168  15.291  0.00 52.59  ? 1037 VAL   A CG1 1 
ATOM   1459 C  CG2 . VAL   A 1 185 ? 0.561   40.000  15.390  0.00 55.28  ? 1037 VAL   A CG2 1 
ATOM   1460 N  N   . LYS   A 1 186 ? -3.316  38.594  14.378  1.00 64.38  ? 1038 LYS   A N   1 
ATOM   1461 C  CA  . LYS   A 1 186 ? -3.625  37.300  13.768  1.00 69.49  ? 1038 LYS   A CA  1 
ATOM   1462 C  C   . LYS   A 1 186 ? -2.642  37.079  12.624  1.00 69.46  ? 1038 LYS   A C   1 
ATOM   1463 O  O   . LYS   A 1 186 ? -1.906  36.086  12.605  1.00 72.05  ? 1038 LYS   A O   1 
ATOM   1464 C  CB  . LYS   A 1 186 ? -5.072  37.259  13.256  1.00 69.86  ? 1038 LYS   A CB  1 
ATOM   1465 C  CG  . LYS   A 1 186 ? -6.146  37.445  14.313  0.00 72.04  ? 1038 LYS   A CG  1 
ATOM   1466 C  CD  . LYS   A 1 186 ? -7.539  37.470  13.698  0.00 73.43  ? 1038 LYS   A CD  1 
ATOM   1467 C  CE  . LYS   A 1 186 ? -8.614  37.692  14.750  0.00 74.78  ? 1038 LYS   A CE  1 
ATOM   1468 N  NZ  . LYS   A 1 186 ? -9.979  37.722  14.156  0.00 76.29  ? 1038 LYS   A NZ  1 
ATOM   1469 N  N   . ASP   A 1 187 ? -2.634  38.024  11.687  1.00 67.05  ? 1039 ASP   A N   1 
ATOM   1470 C  CA  . ASP   A 1 187 ? -1.719  38.006  10.553  1.00 67.09  ? 1039 ASP   A CA  1 
ATOM   1471 C  C   . ASP   A 1 187 ? -0.348  38.539  10.984  1.00 63.80  ? 1039 ASP   A C   1 
ATOM   1472 O  O   . ASP   A 1 187 ? -0.229  39.702  11.390  1.00 60.96  ? 1039 ASP   A O   1 
ATOM   1473 C  CB  . ASP   A 1 187 ? -2.275  38.863  9.417   1.00 66.23  ? 1039 ASP   A CB  1 
ATOM   1474 C  CG  . ASP   A 1 187 ? -1.351  38.915  8.217   1.00 70.57  ? 1039 ASP   A CG  1 
ATOM   1475 O  OD1 . ASP   A 1 187 ? -1.431  37.993  7.378   1.00 81.77  ? 1039 ASP   A OD1 1 
ATOM   1476 O  OD2 . ASP   A 1 187 ? -0.551  39.876  8.117   1.00 62.87  ? 1039 ASP   A OD2 1 
ATOM   1477 N  N   . ASP   A 1 188 ? 0.674   37.684  10.887  1.00 64.33  ? 1040 ASP   A N   1 
ATOM   1478 C  CA  . ASP   A 1 188 ? 2.068   38.055  11.202  1.00 60.88  ? 1040 ASP   A CA  1 
ATOM   1479 C  C   . ASP   A 1 188 ? 3.089   37.649  10.117  1.00 62.02  ? 1040 ASP   A C   1 
ATOM   1480 O  O   . ASP   A 1 188 ? 4.292   37.685  10.360  1.00 61.69  ? 1040 ASP   A O   1 
ATOM   1481 C  CB  . ASP   A 1 188 ? 2.471   37.500  12.584  1.00 61.38  ? 1040 ASP   A CB  1 
ATOM   1482 C  CG  . ASP   A 1 188 ? 2.275   35.992  12.706  1.00 65.64  ? 1040 ASP   A CG  1 
ATOM   1483 O  OD1 . ASP   A 1 188 ? 1.976   35.332  11.692  1.00 59.40  ? 1040 ASP   A OD1 1 
ATOM   1484 O  OD2 . ASP   A 1 188 ? 2.413   35.464  13.829  1.00 71.66  ? 1040 ASP   A OD2 1 
ATOM   1485 N  N   . ARG   A 1 189 ? 2.618   37.293  8.923   1.00 65.33  ? 1041 ARG   A N   1 
ATOM   1486 C  CA  . ARG   A 1 189 ? 3.506   37.003  7.793   1.00 67.03  ? 1041 ARG   A CA  1 
ATOM   1487 C  C   . ARG   A 1 189 ? 3.917   38.323  7.146   1.00 64.76  ? 1041 ARG   A C   1 
ATOM   1488 O  O   . ARG   A 1 189 ? 3.159   39.309  7.180   1.00 66.32  ? 1041 ARG   A O   1 
ATOM   1489 C  CB  . ARG   A 1 189 ? 2.829   36.080  6.772   1.00 70.49  ? 1041 ARG   A CB  1 
ATOM   1490 C  CG  . ARG   A 1 189 ? 3.810   35.442  5.793   0.00 73.11  ? 1041 ARG   A CG  1 
ATOM   1491 C  CD  . ARG   A 1 189 ? 3.103   34.484  4.847   0.00 76.98  ? 1041 ARG   A CD  1 
ATOM   1492 N  NE  . ARG   A 1 189 ? 2.163   35.177  3.964   0.00 76.17  ? 1041 ARG   A NE  1 
ATOM   1493 C  CZ  . ARG   A 1 189 ? 2.497   35.933  2.914   0.00 74.84  ? 1041 ARG   A CZ  1 
ATOM   1494 N  NH1 . ARG   A 1 189 ? 3.773   36.131  2.572   0.00 74.10  ? 1041 ARG   A NH1 1 
ATOM   1495 N  NH2 . ARG   A 1 189 ? 1.538   36.508  2.191   0.00 74.39  ? 1041 ARG   A NH2 1 
ATOM   1496 N  N   . ASP   A 1 190 ? 5.115   38.326  6.558   1.00 63.58  ? 1042 ASP   A N   1 
ATOM   1497 C  CA  . ASP   A 1 190 ? 5.790   39.549  6.085   1.00 59.82  ? 1042 ASP   A CA  1 
ATOM   1498 C  C   . ASP   A 1 190 ? 6.017   40.572  7.214   1.00 54.49  ? 1042 ASP   A C   1 
ATOM   1499 O  O   . ASP   A 1 190 ? 6.049   41.777  6.963   1.00 54.59  ? 1042 ASP   A O   1 
ATOM   1500 C  CB  . ASP   A 1 190 ? 5.039   40.195  4.903   1.00 60.15  ? 1042 ASP   A CB  1 
ATOM   1501 C  CG  . ASP   A 1 190 ? 4.745   39.211  3.776   1.00 65.49  ? 1042 ASP   A CG  1 
ATOM   1502 O  OD1 . ASP   A 1 190 ? 5.589   38.328  3.504   1.00 67.63  ? 1042 ASP   A OD1 1 
ATOM   1503 O  OD2 . ASP   A 1 190 ? 3.668   39.334  3.154   1.00 70.13  ? 1042 ASP   A OD2 1 
ATOM   1504 N  N   . SER   A 1 191 ? 6.206   40.084  8.443   1.00 51.41  ? 1043 SER   A N   1 
ATOM   1505 C  CA  . SER   A 1 191 ? 6.521   40.941  9.603   1.00 47.07  ? 1043 SER   A CA  1 
ATOM   1506 C  C   . SER   A 1 191 ? 7.986   41.388  9.579   1.00 41.71  ? 1043 SER   A C   1 
ATOM   1507 O  O   . SER   A 1 191 ? 8.860   40.571  9.287   1.00 40.06  ? 1043 SER   A O   1 
ATOM   1508 C  CB  . SER   A 1 191 ? 6.264   40.190  10.915  1.00 49.90  ? 1043 SER   A CB  1 
ATOM   1509 O  OG  . SER   A 1 191 ? 4.877   40.054  11.162  1.00 56.16  ? 1043 SER   A OG  1 
ATOM   1510 N  N   . PRO   A 1 192 ? 8.266   42.675  9.889   1.00 36.81  ? 1044 PRO   A N   1 
ATOM   1511 C  CA  . PRO   A 1 192 ? 9.661   43.128  10.011  1.00 33.54  ? 1044 PRO   A CA  1 
ATOM   1512 C  C   . PRO   A 1 192 ? 10.300  42.660  11.325  1.00 31.59  ? 1044 PRO   A C   1 
ATOM   1513 O  O   . PRO   A 1 192 ? 10.481  43.441  12.250  1.00 29.52  ? 1044 PRO   A O   1 
ATOM   1514 C  CB  . PRO   A 1 192 ? 9.541   44.657  9.929   1.00 30.28  ? 1044 PRO   A CB  1 
ATOM   1515 C  CG  . PRO   A 1 192 ? 8.228   44.960  10.495  1.00 29.87  ? 1044 PRO   A CG  1 
ATOM   1516 C  CD  . PRO   A 1 192 ? 7.323   43.794  10.105  1.00 35.20  ? 1044 PRO   A CD  1 
ATOM   1517 N  N   . VAL   A 1 193 ? 10.651  41.374  11.370  1.00 35.48  ? 1045 VAL   A N   1 
ATOM   1518 C  CA  . VAL   A 1 193 ? 11.089  40.710  12.611  1.00 34.63  ? 1045 VAL   A CA  1 
ATOM   1519 C  C   . VAL   A 1 193 ? 12.320  41.340  13.307  1.00 35.65  ? 1045 VAL   A C   1 
ATOM   1520 O  O   . VAL   A 1 193 ? 12.410  41.340  14.534  1.00 36.87  ? 1045 VAL   A O   1 
ATOM   1521 C  CB  . VAL   A 1 193 ? 11.331  39.203  12.387  1.00 39.35  ? 1045 VAL   A CB  1 
ATOM   1522 C  CG1 . VAL   A 1 193 ? 10.025  38.510  12.016  1.00 39.56  ? 1045 VAL   A CG1 1 
ATOM   1523 C  CG2 . VAL   A 1 193 ? 12.413  38.955  11.333  1.00 40.37  ? 1045 VAL   A CG2 1 
ATOM   1524 N  N   . PHE   A 1 194 ? 13.243  41.902  12.530  1.00 34.23  ? 1046 PHE   A N   1 
ATOM   1525 C  CA  . PHE   A 1 194 ? 14.451  42.527  13.100  1.00 32.71  ? 1046 PHE   A CA  1 
ATOM   1526 C  C   . PHE   A 1 194 ? 14.188  43.904  13.733  1.00 29.35  ? 1046 PHE   A C   1 
ATOM   1527 O  O   . PHE   A 1 194 ? 15.066  44.450  14.393  1.00 29.39  ? 1046 PHE   A O   1 
ATOM   1528 C  CB  . PHE   A 1 194 ? 15.575  42.584  12.053  1.00 31.06  ? 1046 PHE   A CB  1 
ATOM   1529 C  CG  . PHE   A 1 194 ? 15.946  41.229  11.513  1.00 33.72  ? 1046 PHE   A CG  1 
ATOM   1530 C  CD1 . PHE   A 1 194 ? 16.487  40.261  12.356  1.00 38.94  ? 1046 PHE   A CD1 1 
ATOM   1531 C  CD2 . PHE   A 1 194 ? 15.726  40.905  10.174  1.00 33.81  ? 1046 PHE   A CD2 1 
ATOM   1532 C  CE1 . PHE   A 1 194 ? 16.824  38.987  11.876  1.00 38.80  ? 1046 PHE   A CE1 1 
ATOM   1533 C  CE2 . PHE   A 1 194 ? 16.070  39.634  9.677   1.00 35.96  ? 1046 PHE   A CE2 1 
ATOM   1534 C  CZ  . PHE   A 1 194 ? 16.612  38.676  10.534  1.00 37.42  ? 1046 PHE   A CZ  1 
ATOM   1535 N  N   . TRP   A 1 195 ? 12.971  44.422  13.561  1.00 27.55  ? 1047 TRP   A N   1 
ATOM   1536 C  CA  . TRP   A 1 195 ? 12.513  45.641  14.245  1.00 24.63  ? 1047 TRP   A CA  1 
ATOM   1537 C  C   . TRP   A 1 195 ? 11.576  45.342  15.430  1.00 26.24  ? 1047 TRP   A C   1 
ATOM   1538 O  O   . TRP   A 1 195 ? 11.159  46.266  16.128  1.00 27.08  ? 1047 TRP   A O   1 
ATOM   1539 C  CB  . TRP   A 1 195 ? 11.831  46.569  13.220  1.00 24.33  ? 1047 TRP   A CB  1 
ATOM   1540 C  CG  . TRP   A 1 195 ? 12.793  47.369  12.409  1.00 21.38  ? 1047 TRP   A CG  1 
ATOM   1541 C  CD1 . TRP   A 1 195 ? 13.069  48.696  12.551  1.00 20.59  ? 1047 TRP   A CD1 1 
ATOM   1542 C  CD2 . TRP   A 1 195 ? 13.634  46.901  11.344  1.00 24.52  ? 1047 TRP   A CD2 1 
ATOM   1543 N  NE1 . TRP   A 1 195 ? 14.004  49.089  11.649  1.00 20.98  ? 1047 TRP   A NE1 1 
ATOM   1544 C  CE2 . TRP   A 1 195 ? 14.388  48.010  10.896  1.00 26.09  ? 1047 TRP   A CE2 1 
ATOM   1545 C  CE3 . TRP   A 1 195 ? 13.834  45.654  10.730  1.00 27.93  ? 1047 TRP   A CE3 1 
ATOM   1546 C  CZ2 . TRP   A 1 195 ? 15.316  47.920  9.843   1.00 29.24  ? 1047 TRP   A CZ2 1 
ATOM   1547 C  CZ3 . TRP   A 1 195 ? 14.772  45.559  9.684   1.00 28.16  ? 1047 TRP   A CZ3 1 
ATOM   1548 C  CH2 . TRP   A 1 195 ? 15.493  46.695  9.251   1.00 25.62  ? 1047 TRP   A CH2 1 
ATOM   1549 N  N   . TYR   A 1 196 ? 11.267  44.059  15.670  1.00 28.38  ? 1048 TYR   A N   1 
ATOM   1550 C  CA  . TYR   A 1 196 ? 10.214  43.666  16.602  1.00 30.62  ? 1048 TYR   A CA  1 
ATOM   1551 C  C   . TYR   A 1 196 ? 10.701  43.265  17.996  1.00 34.12  ? 1048 TYR   A C   1 
ATOM   1552 O  O   . TYR   A 1 196 ? 11.709  42.565  18.162  1.00 35.02  ? 1048 TYR   A O   1 
ATOM   1553 C  CB  . TYR   A 1 196 ? 9.350   42.541  15.982  1.00 31.74  ? 1048 TYR   A CB  1 
ATOM   1554 C  CG  . TYR   A 1 196 ? 8.185   43.015  15.113  1.00 32.50  ? 1048 TYR   A CG  1 
ATOM   1555 C  CD1 . TYR   A 1 196 ? 8.089   44.343  14.655  1.00 28.58  ? 1048 TYR   A CD1 1 
ATOM   1556 C  CD2 . TYR   A 1 196 ? 7.177   42.122  14.722  1.00 39.66  ? 1048 TYR   A CD2 1 
ATOM   1557 C  CE1 . TYR   A 1 196 ? 7.018   44.760  13.876  1.00 33.14  ? 1048 TYR   A CE1 1 
ATOM   1558 C  CE2 . TYR   A 1 196 ? 6.113   42.536  13.919  1.00 36.23  ? 1048 TYR   A CE2 1 
ATOM   1559 C  CZ  . TYR   A 1 196 ? 6.038   43.866  13.507  1.00 36.47  ? 1048 TYR   A CZ  1 
ATOM   1560 O  OH  . TYR   A 1 196 ? 5.006   44.316  12.720  1.00 42.25  ? 1048 TYR   A OH  1 
ATOM   1561 N  N   . ALA   A 1 197 ? 9.941   43.718  18.993  1.00 32.74  ? 1049 ALA   A N   1 
ATOM   1562 C  CA  . ALA   A 1 197 ? 10.136  43.342  20.378  1.00 31.15  ? 1049 ALA   A CA  1 
ATOM   1563 C  C   . ALA   A 1 197 ? 9.884   41.841  20.627  1.00 36.15  ? 1049 ALA   A C   1 
ATOM   1564 O  O   . ALA   A 1 197 ? 9.200   41.183  19.827  1.00 39.15  ? 1049 ALA   A O   1 
ATOM   1565 C  CB  . ALA   A 1 197 ? 9.250   44.163  21.241  1.00 28.21  ? 1049 ALA   A CB  1 
ATOM   1566 N  N   . PRO   A 1 198 ? 10.463  41.285  21.713  1.00 40.02  ? 1050 PRO   A N   1 
ATOM   1567 C  CA  . PRO   A 1 198 ? 10.251  39.857  22.009  1.00 43.06  ? 1050 PRO   A CA  1 
ATOM   1568 C  C   . PRO   A 1 198 ? 8.783   39.438  22.138  1.00 45.60  ? 1050 PRO   A C   1 
ATOM   1569 O  O   . PRO   A 1 198 ? 8.416   38.414  21.585  1.00 48.68  ? 1050 PRO   A O   1 
ATOM   1570 C  CB  . PRO   A 1 198 ? 11.006  39.649  23.331  1.00 44.71  ? 1050 PRO   A CB  1 
ATOM   1571 C  CG  . PRO   A 1 198 ? 12.021  40.727  23.358  1.00 43.81  ? 1050 PRO   A CG  1 
ATOM   1572 C  CD  . PRO   A 1 198 ? 11.378  41.902  22.695  1.00 39.63  ? 1050 PRO   A CD  1 
ATOM   1573 N  N   . GLU   A 1 199 ? 7.963   40.218  22.843  1.00 46.25  ? 1051 GLU   A N   1 
ATOM   1574 C  CA  . GLU   A 1 199 ? 6.510   39.924  22.968  1.00 48.08  ? 1051 GLU   A CA  1 
ATOM   1575 C  C   . GLU   A 1 199 ? 5.758   39.859  21.620  1.00 45.49  ? 1051 GLU   A C   1 
ATOM   1576 O  O   . GLU   A 1 199 ? 4.780   39.111  21.487  1.00 49.16  ? 1051 GLU   A O   1 
ATOM   1577 C  CB  . GLU   A 1 199 ? 5.798   40.896  23.932  1.00 46.44  ? 1051 GLU   A CB  1 
ATOM   1578 C  CG  . GLU   A 1 199 ? 5.630   42.355  23.451  1.00 40.44  ? 1051 GLU   A CG  1 
ATOM   1579 C  CD  . GLU   A 1 199 ? 6.901   43.190  23.555  1.00 39.79  ? 1051 GLU   A CD  1 
ATOM   1580 O  OE1 . GLU   A 1 199 ? 7.936   42.654  24.031  1.00 39.93  ? 1051 GLU   A OE1 1 
ATOM   1581 O  OE2 . GLU   A 1 199 ? 6.850   44.387  23.170  1.00 34.29  ? 1051 GLU   A OE2 1 
ATOM   1582 N  N   . CYS   A 1 200 ? 6.219   40.636  20.636  1.00 44.28  ? 1052 CYS   A N   1 
ATOM   1583 C  CA  . CYS   A 1 200 ? 5.678   40.576  19.267  1.00 42.52  ? 1052 CYS   A CA  1 
ATOM   1584 C  C   . CYS   A 1 200 ? 6.092   39.282  18.569  1.00 47.85  ? 1052 CYS   A C   1 
ATOM   1585 O  O   . CYS   A 1 200 ? 5.254   38.596  17.973  1.00 51.12  ? 1052 CYS   A O   1 
ATOM   1586 C  CB  . CYS   A 1 200 ? 6.121   41.790  18.445  1.00 37.88  ? 1052 CYS   A CB  1 
ATOM   1587 S  SG  . CYS   A 1 200 ? 5.955   43.330  19.352  1.00 37.67  ? 1052 CYS   A SG  1 
ATOM   1588 N  N   . LEU   A 1 201 ? 7.377   38.945  18.660  1.00 46.85  ? 1053 LEU   A N   1 
ATOM   1589 C  CA  . LEU   A 1 201 ? 7.892   37.697  18.090  1.00 47.26  ? 1053 LEU   A CA  1 
ATOM   1590 C  C   . LEU   A 1 201 ? 7.351   36.459  18.821  1.00 50.73  ? 1053 LEU   A C   1 
ATOM   1591 O  O   . LEU   A 1 201 ? 7.006   35.479  18.165  1.00 52.61  ? 1053 LEU   A O   1 
ATOM   1592 C  CB  . LEU   A 1 201 ? 9.432   37.687  18.082  1.00 46.37  ? 1053 LEU   A CB  1 
ATOM   1593 C  CG  . LEU   A 1 201 ? 10.126  38.781  17.247  1.00 40.43  ? 1053 LEU   A CG  1 
ATOM   1594 C  CD1 . LEU   A 1 201 ? 11.614  38.830  17.535  1.00 37.12  ? 1053 LEU   A CD1 1 
ATOM   1595 C  CD2 . LEU   A 1 201 ? 9.902   38.604  15.756  1.00 39.18  ? 1053 LEU   A CD2 1 
ATOM   1596 N  N   . MET   A 1 202 ? 7.244   36.525  20.151  1.00 50.54  ? 1054 MET   A N   1 
ATOM   1597 C  CA  . MET   A 1 202 ? 6.846   35.366  20.969  1.00 58.08  ? 1054 MET   A CA  1 
ATOM   1598 C  C   . MET   A 1 202 ? 5.349   35.099  20.837  1.00 58.47  ? 1054 MET   A C   1 
ATOM   1599 O  O   . MET   A 1 202 ? 4.940   34.001  20.452  1.00 62.34  ? 1054 MET   A O   1 
ATOM   1600 C  CB  . MET   A 1 202 ? 7.162   35.577  22.463  1.00 60.22  ? 1054 MET   A CB  1 
ATOM   1601 C  CG  . MET   A 1 202 ? 8.611   35.871  22.814  1.00 62.10  ? 1054 MET   A CG  1 
ATOM   1602 S  SD  . MET   A 1 202 ? 9.606   34.497  23.282  1.00 83.00  ? 1054 MET   A SD  1 
ATOM   1603 C  CE  . MET   A 1 202 ? 8.965   34.089  24.904  1.00 84.90  ? 1054 MET   A CE  1 
ATOM   1604 N  N   . GLN   A 1 203 ? 4.551   36.118  21.163  1.00 56.39  ? 1055 GLN   A N   1 
ATOM   1605 C  CA  . GLN   A 1 203 ? 3.105   35.963  21.369  1.00 61.05  ? 1055 GLN   A CA  1 
ATOM   1606 C  C   . GLN   A 1 203 ? 2.219   36.756  20.405  1.00 60.09  ? 1055 GLN   A C   1 
ATOM   1607 O  O   . GLN   A 1 203 ? 0.990   36.738  20.548  1.00 63.32  ? 1055 GLN   A O   1 
ATOM   1608 C  CB  . GLN   A 1 203 ? 2.760   36.332  22.815  1.00 62.50  ? 1055 GLN   A CB  1 
ATOM   1609 C  CG  . GLN   A 1 203 ? 3.494   35.493  23.851  1.00 62.53  ? 1055 GLN   A CG  1 
ATOM   1610 C  CD  . GLN   A 1 203 ? 3.036   35.782  25.266  1.00 72.52  ? 1055 GLN   A CD  1 
ATOM   1611 O  OE1 . GLN   A 1 203 ? 2.543   36.839  25.585  0.00 67.51  ? 1055 GLN   A OE1 1 
ATOM   1612 N  NE2 . GLN   A 1 203 ? 3.240   34.780  26.147  0.00 73.29  ? 1055 GLN   A NE2 1 
ATOM   1613 N  N   . SER   A 1 204 ? 2.816   37.423  19.416  1.00 57.87  ? 1056 SER   A N   1 
ATOM   1614 C  CA  . SER   A 1 204 ? 2.053   38.214  18.439  1.00 57.11  ? 1056 SER   A CA  1 
ATOM   1615 C  C   . SER   A 1 204 ? 1.257   39.350  19.124  1.00 55.33  ? 1056 SER   A C   1 
ATOM   1616 O  O   . SER   A 1 204 ? 0.183   39.737  18.652  1.00 55.73  ? 1056 SER   A O   1 
ATOM   1617 C  CB  . SER   A 1 204 ? 1.116   37.296  17.617  1.00 60.81  ? 1056 SER   A CB  1 
ATOM   1618 O  OG  . SER   A 1 204 ? 1.659   35.993  17.425  1.00 64.67  ? 1056 SER   A OG  1 
ATOM   1619 N  N   . LYS   A 1 205 ? 1.795   39.867  20.234  1.00 53.46  ? 1057 LYS   A N   1 
ATOM   1620 C  CA  . LYS   A 1 205 ? 1.165   40.935  21.024  1.00 50.65  ? 1057 LYS   A CA  1 
ATOM   1621 C  C   . LYS   A 1 205 ? 1.903   42.228  20.736  1.00 46.37  ? 1057 LYS   A C   1 
ATOM   1622 O  O   . LYS   A 1 205 ? 3.130   42.213  20.590  1.00 46.19  ? 1057 LYS   A O   1 
ATOM   1623 C  CB  . LYS   A 1 205 ? 1.233   40.630  22.523  1.00 51.56  ? 1057 LYS   A CB  1 
ATOM   1624 C  CG  . LYS   A 1 205 ? 0.361   39.463  22.979  1.00 61.22  ? 1057 LYS   A CG  1 
ATOM   1625 C  CD  . LYS   A 1 205 ? 0.448   39.271  24.495  1.00 64.36  ? 1057 LYS   A CD  1 
ATOM   1626 C  CE  . LYS   A 1 205 ? -0.360  38.073  24.963  1.00 70.09  ? 1057 LYS   A CE  1 
ATOM   1627 N  NZ  . LYS   A 1 205 ? -0.381  37.965  26.449  1.00 74.30  ? 1057 LYS   A NZ  1 
ATOM   1628 N  N   A PHE   A 1 206 ? 1.166   43.334  20.652  0.50 42.78  ? 1058 PHE   A N   1 
ATOM   1629 N  N   B PHE   A 1 206 ? 1.158   43.337  20.670  0.50 42.63  ? 1058 PHE   A N   1 
ATOM   1630 C  CA  A PHE   A 1 206 ? 1.765   44.624  20.313  0.50 37.39  ? 1058 PHE   A CA  1 
ATOM   1631 C  CA  B PHE   A 1 206 ? 1.684   44.662  20.286  0.50 36.97  ? 1058 PHE   A CA  1 
ATOM   1632 C  C   A PHE   A 1 206 ? 1.266   45.739  21.234  0.50 36.15  ? 1058 PHE   A C   1 
ATOM   1633 C  C   B PHE   A 1 206 ? 1.240   45.740  21.265  0.50 36.09  ? 1058 PHE   A C   1 
ATOM   1634 O  O   A PHE   A 1 206 ? 0.085   46.092  21.217  0.50 37.93  ? 1058 PHE   A O   1 
ATOM   1635 O  O   B PHE   A 1 206 ? 0.060   46.093  21.303  0.50 37.63  ? 1058 PHE   A O   1 
ATOM   1636 C  CB  A PHE   A 1 206 ? 1.545   44.953  18.837  0.50 34.44  ? 1058 PHE   A CB  1 
ATOM   1637 C  CB  B PHE   A 1 206 ? 1.196   45.033  18.890  0.50 34.61  ? 1058 PHE   A CB  1 
ATOM   1638 C  CG  A PHE   A 1 206 ? 2.718   45.640  18.219  0.50 32.25  ? 1058 PHE   A CG  1 
ATOM   1639 C  CG  B PHE   A 1 206 ? 1.936   44.345  17.799  0.50 33.53  ? 1058 PHE   A CG  1 
ATOM   1640 C  CD1 A PHE   A 1 206 ? 2.967   46.974  18.503  0.50 27.69  ? 1058 PHE   A CD1 1 
ATOM   1641 C  CD1 B PHE   A 1 206 ? 3.162   44.836  17.364  0.50 34.14  ? 1058 PHE   A CD1 1 
ATOM   1642 C  CD2 A PHE   A 1 206 ? 3.613   44.942  17.411  0.50 32.43  ? 1058 PHE   A CD2 1 
ATOM   1643 C  CD2 B PHE   A 1 206 ? 1.418   43.203  17.201  0.50 36.68  ? 1058 PHE   A CD2 1 
ATOM   1644 C  CE1 A PHE   A 1 206 ? 4.067   47.630  17.949  0.50 19.60  ? 1058 PHE   A CE1 1 
ATOM   1645 C  CE1 B PHE   A 1 206 ? 3.864   44.195  16.346  0.50 30.36  ? 1058 PHE   A CE1 1 
ATOM   1646 C  CE2 A PHE   A 1 206 ? 4.720   45.584  16.860  0.50 24.63  ? 1058 PHE   A CE2 1 
ATOM   1647 C  CE2 B PHE   A 1 206 ? 2.114   42.561  16.186  0.50 38.86  ? 1058 PHE   A CE2 1 
ATOM   1648 C  CZ  A PHE   A 1 206 ? 4.954   46.931  17.150  0.50 24.16  ? 1058 PHE   A CZ  1 
ATOM   1649 C  CZ  B PHE   A 1 206 ? 3.334   43.059  15.760  0.50 31.29  ? 1058 PHE   A CZ  1 
ATOM   1650 N  N   . TYR   A 1 207 ? 2.188   46.248  22.055  1.00 35.12  ? 1059 TYR   A N   1 
ATOM   1651 C  CA  . TYR   A 1 207 ? 1.942   47.345  23.000  1.00 36.12  ? 1059 TYR   A CA  1 
ATOM   1652 C  C   . TYR   A 1 207 ? 2.510   48.634  22.417  1.00 33.15  ? 1059 TYR   A C   1 
ATOM   1653 O  O   . TYR   A 1 207 ? 3.295   48.596  21.451  1.00 30.73  ? 1059 TYR   A O   1 
ATOM   1654 C  CB  . TYR   A 1 207 ? 2.684   47.085  24.319  1.00 36.73  ? 1059 TYR   A CB  1 
ATOM   1655 C  CG  . TYR   A 1 207 ? 2.299   45.845  25.073  1.00 36.09  ? 1059 TYR   A CG  1 
ATOM   1656 C  CD1 . TYR   A 1 207 ? 2.702   44.579  24.637  1.00 36.40  ? 1059 TYR   A CD1 1 
ATOM   1657 C  CD2 . TYR   A 1 207 ? 1.572   45.929  26.264  1.00 38.36  ? 1059 TYR   A CD2 1 
ATOM   1658 C  CE1 . TYR   A 1 207 ? 2.354   43.423  25.344  1.00 38.79  ? 1059 TYR   A CE1 1 
ATOM   1659 C  CE2 . TYR   A 1 207 ? 1.233   44.787  26.981  1.00 45.49  ? 1059 TYR   A CE2 1 
ATOM   1660 C  CZ  . TYR   A 1 207 ? 1.631   43.535  26.514  1.00 44.57  ? 1059 TYR   A CZ  1 
ATOM   1661 O  OH  . TYR   A 1 207 ? 1.300   42.398  27.216  1.00 48.71  ? 1059 TYR   A OH  1 
ATOM   1662 N  N   . ILE   A 1 208 ? 2.175   49.767  23.037  1.00 34.03  ? 1060 ILE   A N   1 
ATOM   1663 C  CA  . ILE   A 1 208 ? 2.897   51.034  22.762  1.00 30.39  ? 1060 ILE   A CA  1 
ATOM   1664 C  C   . ILE   A 1 208 ? 4.396   50.851  23.034  1.00 30.58  ? 1060 ILE   A C   1 
ATOM   1665 O  O   . ILE   A 1 208 ? 5.238   51.336  22.286  1.00 25.81  ? 1060 ILE   A O   1 
ATOM   1666 C  CB  . ILE   A 1 208 ? 2.330   52.238  23.588  1.00 31.65  ? 1060 ILE   A CB  1 
ATOM   1667 C  CG1 . ILE   A 1 208 ? 1.016   52.728  22.970  1.00 36.77  ? 1060 ILE   A CG1 1 
ATOM   1668 C  CG2 . ILE   A 1 208 ? 3.310   53.416  23.627  1.00 31.59  ? 1060 ILE   A CG2 1 
ATOM   1669 C  CD1 . ILE   A 1 208 ? 0.216   53.667  23.861  1.00 37.78  ? 1060 ILE   A CD1 1 
ATOM   1670 N  N   . ALA   A 1 209 ? 4.728   50.144  24.114  1.00 30.06  ? 1061 ALA   A N   1 
ATOM   1671 C  CA  . ALA   A 1 209 ? 6.127   49.794  24.392  1.00 30.18  ? 1061 ALA   A CA  1 
ATOM   1672 C  C   . ALA   A 1 209 ? 6.798   48.974  23.288  1.00 28.39  ? 1061 ALA   A C   1 
ATOM   1673 O  O   . ALA   A 1 209 ? 8.007   49.031  23.138  1.00 27.95  ? 1061 ALA   A O   1 
ATOM   1674 C  CB  . ALA   A 1 209 ? 6.235   49.071  25.713  1.00 33.43  ? 1061 ALA   A CB  1 
ATOM   1675 N  N   . SER   A 1 210 ? 6.031   48.203  22.524  1.00 28.82  ? 1062 SER   A N   1 
ATOM   1676 C  CA  . SER   A 1 210 ? 6.578   47.490  21.362  1.00 28.60  ? 1062 SER   A CA  1 
ATOM   1677 C  C   . SER   A 1 210 ? 7.011   48.476  20.264  1.00 26.78  ? 1062 SER   A C   1 
ATOM   1678 O  O   . SER   A 1 210 ? 8.009   48.251  19.592  1.00 26.52  ? 1062 SER   A O   1 
ATOM   1679 C  CB  . SER   A 1 210 ? 5.568   46.486  20.812  1.00 31.34  ? 1062 SER   A CB  1 
ATOM   1680 O  OG  . SER   A 1 210 ? 4.963   45.752  21.855  1.00 31.49  ? 1062 SER   A OG  1 
ATOM   1681 N  N   . ASP   A 1 211 ? 6.249   49.556  20.081  1.00 26.16  ? 1063 ASP   A N   1 
ATOM   1682 C  CA  . ASP   A 1 211 ? 6.675   50.685  19.227  1.00 24.01  ? 1063 ASP   A CA  1 
ATOM   1683 C  C   . ASP   A 1 211 ? 7.935   51.388  19.766  1.00 20.16  ? 1063 ASP   A C   1 
ATOM   1684 O  O   . ASP   A 1 211 ? 8.791   51.807  18.979  1.00 19.62  ? 1063 ASP   A O   1 
ATOM   1685 C  CB  . ASP   A 1 211 ? 5.552   51.734  19.071  1.00 23.20  ? 1063 ASP   A CB  1 
ATOM   1686 C  CG  . ASP   A 1 211 ? 4.573   51.420  17.952  1.00 24.55  ? 1063 ASP   A CG  1 
ATOM   1687 O  OD1 . ASP   A 1 211 ? 4.860   50.593  17.055  1.00 23.39  ? 1063 ASP   A OD1 1 
ATOM   1688 O  OD2 . ASP   A 1 211 ? 3.471   52.026  17.968  1.00 25.96  ? 1063 ASP   A OD2 1 
ATOM   1689 N  N   . VAL   A 1 212 ? 8.049   51.523  21.092  1.00 23.09  ? 1064 VAL   A N   1 
ATOM   1690 C  CA  . VAL   A 1 212 ? 9.278   52.071  21.715  1.00 21.62  ? 1064 VAL   A CA  1 
ATOM   1691 C  C   . VAL   A 1 212 ? 10.500  51.221  21.351  1.00 22.68  ? 1064 VAL   A C   1 
ATOM   1692 O  O   . VAL   A 1 212 ? 11.534  51.763  20.991  1.00 20.40  ? 1064 VAL   A O   1 
ATOM   1693 C  CB  . VAL   A 1 212 ? 9.125   52.267  23.240  1.00 23.00  ? 1064 VAL   A CB  1 
ATOM   1694 C  CG1 . VAL   A 1 212 ? 10.452  52.604  23.881  1.00 22.18  ? 1064 VAL   A CG1 1 
ATOM   1695 C  CG2 . VAL   A 1 212 ? 8.109   53.370  23.521  1.00 23.70  ? 1064 VAL   A CG2 1 
ATOM   1696 N  N   . TRP   A 1 213 ? 10.359  49.895  21.407  1.00 25.03  ? 1065 TRP   A N   1 
ATOM   1697 C  CA  . TRP   A 1 213 ? 11.450  48.990  20.985  1.00 25.59  ? 1065 TRP   A CA  1 
ATOM   1698 C  C   . TRP   A 1 213 ? 11.850  49.244  19.541  1.00 20.15  ? 1065 TRP   A C   1 
ATOM   1699 O  O   . TRP   A 1 213 ? 13.025  49.421  19.242  1.00 19.18  ? 1065 TRP   A O   1 
ATOM   1700 C  CB  . TRP   A 1 213 ? 11.029  47.539  21.137  1.00 24.73  ? 1065 TRP   A CB  1 
ATOM   1701 C  CG  . TRP   A 1 213 ? 12.022  46.534  20.643  1.00 25.19  ? 1065 TRP   A CG  1 
ATOM   1702 C  CD1 . TRP   A 1 213 ? 12.328  46.258  19.346  1.00 27.11  ? 1065 TRP   A CD1 1 
ATOM   1703 C  CD2 . TRP   A 1 213 ? 12.810  45.637  21.439  1.00 32.16  ? 1065 TRP   A CD2 1 
ATOM   1704 N  NE1 . TRP   A 1 213 ? 13.268  45.275  19.278  1.00 29.24  ? 1065 TRP   A NE1 1 
ATOM   1705 C  CE2 . TRP   A 1 213 ? 13.589  44.870  20.546  1.00 31.76  ? 1065 TRP   A CE2 1 
ATOM   1706 C  CE3 . TRP   A 1 213 ? 12.940  45.412  22.819  1.00 31.32  ? 1065 TRP   A CE3 1 
ATOM   1707 C  CZ2 . TRP   A 1 213 ? 14.486  43.891  20.978  1.00 28.24  ? 1065 TRP   A CZ2 1 
ATOM   1708 C  CZ3 . TRP   A 1 213 ? 13.841  44.440  23.260  1.00 33.14  ? 1065 TRP   A CZ3 1 
ATOM   1709 C  CH2 . TRP   A 1 213 ? 14.596  43.682  22.340  1.00 35.51  ? 1065 TRP   A CH2 1 
ATOM   1710 N  N   A SER   A 1 214 ? 10.856  49.246  18.659  0.50 23.62  ? 1066 SER   A N   1 
ATOM   1711 N  N   B SER   A 1 214 ? 10.865  49.235  18.646  0.50 21.87  ? 1066 SER   A N   1 
ATOM   1712 C  CA  A SER   A 1 214 ? 11.052  49.551  17.229  0.50 22.84  ? 1066 SER   A CA  1 
ATOM   1713 C  CA  B SER   A 1 214 ? 11.086  49.541  17.216  0.50 19.11  ? 1066 SER   A CA  1 
ATOM   1714 C  C   A SER   A 1 214 ? 11.730  50.905  16.982  0.50 20.67  ? 1066 SER   A C   1 
ATOM   1715 C  C   B SER   A 1 214 ? 11.739  50.910  16.978  0.50 18.74  ? 1066 SER   A C   1 
ATOM   1716 O  O   A SER   A 1 214 ? 12.575  51.025  16.093  0.50 19.34  ? 1066 SER   A O   1 
ATOM   1717 O  O   B SER   A 1 214 ? 12.581  51.045  16.089  0.50 17.14  ? 1066 SER   A O   1 
ATOM   1718 C  CB  A SER   A 1 214 ? 9.709   49.527  16.497  0.50 23.89  ? 1066 SER   A CB  1 
ATOM   1719 C  CB  B SER   A 1 214 ? 9.771   49.475  16.431  0.50 19.27  ? 1066 SER   A CB  1 
ATOM   1720 O  OG  A SER   A 1 214 ? 9.894   49.434  15.103  0.50 28.78  ? 1066 SER   A OG  1 
ATOM   1721 O  OG  B SER   A 1 214 ? 9.176   48.187  16.504  0.50 15.63  ? 1066 SER   A OG  1 
ATOM   1722 N  N   . PHE   A 1 215 ? 11.345  51.914  17.763  1.00 18.77  ? 1067 PHE   A N   1 
ATOM   1723 C  CA  . PHE   A 1 215 ? 12.015  53.221  17.727  1.00 19.62  ? 1067 PHE   A CA  1 
ATOM   1724 C  C   . PHE   A 1 215 ? 13.506  53.107  18.054  1.00 18.78  ? 1067 PHE   A C   1 
ATOM   1725 O  O   . PHE   A 1 215 ? 14.339  53.778  17.432  1.00 18.51  ? 1067 PHE   A O   1 
ATOM   1726 C  CB  . PHE   A 1 215 ? 11.403  54.246  18.689  1.00 17.20  ? 1067 PHE   A CB  1 
ATOM   1727 C  CG  . PHE   A 1 215 ? 12.219  55.491  18.768  1.00 17.21  ? 1067 PHE   A CG  1 
ATOM   1728 C  CD1 . PHE   A 1 215 ? 12.217  56.383  17.676  1.00 18.15  ? 1067 PHE   A CD1 1 
ATOM   1729 C  CD2 . PHE   A 1 215 ? 13.117  55.702  19.813  1.00 22.90  ? 1067 PHE   A CD2 1 
ATOM   1730 C  CE1 . PHE   A 1 215 ? 13.043  57.512  17.684  1.00 13.02  ? 1067 PHE   A CE1 1 
ATOM   1731 C  CE2 . PHE   A 1 215 ? 13.944  56.825  19.831  1.00 21.91  ? 1067 PHE   A CE2 1 
ATOM   1732 C  CZ  . PHE   A 1 215 ? 13.919  57.716  18.777  1.00 14.43  ? 1067 PHE   A CZ  1 
ATOM   1733 N  N   . GLY   A 1 216 ? 13.858  52.294  19.040  1.00 18.81  ? 1068 GLY   A N   1 
ATOM   1734 C  CA  . GLY   A 1 216 ? 15.279  52.071  19.349  1.00 18.39  ? 1068 GLY   A CA  1 
ATOM   1735 C  C   . GLY   A 1 216 ? 16.070  51.611  18.132  1.00 20.45  ? 1068 GLY   A C   1 
ATOM   1736 O  O   . GLY   A 1 216 ? 17.200  52.070  17.880  1.00 17.52  ? 1068 GLY   A O   1 
ATOM   1737 N  N   . VAL   A 1 217 ? 15.478  50.686  17.376  1.00 19.16  ? 1069 VAL   A N   1 
ATOM   1738 C  CA  . VAL   A 1 217 ? 16.107  50.123  16.176  1.00 17.27  ? 1069 VAL   A CA  1 
ATOM   1739 C  C   . VAL   A 1 217 ? 16.177  51.196  15.096  1.00 19.41  ? 1069 VAL   A C   1 
ATOM   1740 O  O   . VAL   A 1 217 ? 17.208  51.366  14.446  1.00 19.29  ? 1069 VAL   A O   1 
ATOM   1741 C  CB  . VAL   A 1 217 ? 15.327  48.859  15.673  1.00 22.02  ? 1069 VAL   A CB  1 
ATOM   1742 C  CG1 . VAL   A 1 217 ? 15.945  48.299  14.397  1.00 20.54  ? 1069 VAL   A CG1 1 
ATOM   1743 C  CG2 . VAL   A 1 217 ? 15.303  47.800  16.765  1.00 19.77  ? 1069 VAL   A CG2 1 
ATOM   1744 N  N   . THR   A 1 218 ? 15.091  51.955  14.936  1.00 18.93  ? 1070 THR   A N   1 
ATOM   1745 C  CA  . THR   A 1 218 ? 15.060  53.097  14.030  1.00 16.16  ? 1070 THR   A CA  1 
ATOM   1746 C  C   . THR   A 1 218 ? 16.118  54.146  14.383  1.00 14.75  ? 1070 THR   A C   1 
ATOM   1747 O  O   . THR   A 1 218 ? 16.744  54.687  13.498  1.00 15.03  ? 1070 THR   A O   1 
ATOM   1748 C  CB  . THR   A 1 218 ? 13.660  53.799  13.989  1.00 17.66  ? 1070 THR   A CB  1 
ATOM   1749 O  OG1 . THR   A 1 218 ? 12.663  52.901  13.508  1.00 18.22  ? 1070 THR   A OG1 1 
ATOM   1750 C  CG2 . THR   A 1 218 ? 13.652  55.015  13.022  1.00 16.96  ? 1070 THR   A CG2 1 
ATOM   1751 N  N   . LEU   A 1 219 ? 16.251  54.472  15.664  1.00 13.65  ? 1071 LEU   A N   1 
ATOM   1752 C  CA  . LEU   A 1 219 ? 17.335  55.354  16.146  1.00 14.70  ? 1071 LEU   A CA  1 
ATOM   1753 C  C   . LEU   A 1 219 ? 18.718  54.818  15.755  1.00 14.24  ? 1071 LEU   A C   1 
ATOM   1754 O  O   . LEU   A 1 219 ? 19.566  55.588  15.350  1.00 13.82  ? 1071 LEU   A O   1 
ATOM   1755 C  CB  . LEU   A 1 219 ? 17.298  55.491  17.675  1.00 16.11  ? 1071 LEU   A CB  1 
ATOM   1756 C  CG  . LEU   A 1 219 ? 18.338  56.421  18.352  1.00 22.67  ? 1071 LEU   A CG  1 
ATOM   1757 C  CD1 . LEU   A 1 219 ? 18.236  57.880  17.865  1.00 23.39  ? 1071 LEU   A CD1 1 
ATOM   1758 C  CD2 . LEU   A 1 219 ? 18.179  56.362  19.822  1.00 17.56  ? 1071 LEU   A CD2 1 
ATOM   1759 N  N   . HIS   A 1 220 ? 18.926  53.508  15.901  1.00 15.54  ? 1072 HIS   A N   1 
ATOM   1760 C  CA  . HIS   A 1 220 ? 20.170  52.866  15.454  1.00 16.84  ? 1072 HIS   A CA  1 
ATOM   1761 C  C   . HIS   A 1 220 ? 20.399  53.128  13.969  1.00 18.25  ? 1072 HIS   A C   1 
ATOM   1762 O  O   . HIS   A 1 220 ? 21.485  53.543  13.574  1.00 18.04  ? 1072 HIS   A O   1 
ATOM   1763 C  CB  . HIS   A 1 220 ? 20.173  51.358  15.743  1.00 20.63  ? 1072 HIS   A CB  1 
ATOM   1764 C  CG  . HIS   A 1 220 ? 21.525  50.721  15.621  1.00 18.54  ? 1072 HIS   A CG  1 
ATOM   1765 N  ND1 . HIS   A 1 220 ? 22.104  50.453  14.398  1.00 19.62  ? 1072 HIS   A ND1 1 
ATOM   1766 C  CD2 . HIS   A 1 220 ? 22.384  50.249  16.554  1.00 20.53  ? 1072 HIS   A CD2 1 
ATOM   1767 C  CE1 . HIS   A 1 220 ? 23.275  49.874  14.588  1.00 21.06  ? 1072 HIS   A CE1 1 
ATOM   1768 N  NE2 . HIS   A 1 220 ? 23.464  49.729  15.887  1.00 19.49  ? 1072 HIS   A NE2 1 
ATOM   1769 N  N   . GLU   A 1 221 ? 19.369  52.909  13.155  1.00 16.83  ? 1073 GLU   A N   1 
ATOM   1770 C  CA  . GLU   A 1 221 ? 19.431  53.179  11.717  1.00 17.29  ? 1073 GLU   A CA  1 
ATOM   1771 C  C   . GLU   A 1 221 ? 19.823  54.623  11.418  1.00 18.11  ? 1073 GLU   A C   1 
ATOM   1772 O  O   . GLU   A 1 221 ? 20.687  54.892  10.605  1.00 18.43  ? 1073 GLU   A O   1 
ATOM   1773 C  CB  . GLU   A 1 221 ? 18.069  52.924  11.065  1.00 17.14  ? 1073 GLU   A CB  1 
ATOM   1774 C  CG  . GLU   A 1 221 ? 17.644  51.493  10.991  1.00 19.41  ? 1073 GLU   A CG  1 
ATOM   1775 C  CD  . GLU   A 1 221 ? 16.389  51.337  10.152  1.00 20.76  ? 1073 GLU   A CD  1 
ATOM   1776 O  OE1 . GLU   A 1 221 ? 16.516  51.049  8.943   1.00 20.51  ? 1073 GLU   A OE1 1 
ATOM   1777 O  OE2 . GLU   A 1 221 ? 15.272  51.513  10.692  1.00 20.71  ? 1073 GLU   A OE2 1 
ATOM   1778 N  N   . LEU   A 1 222 ? 19.136  55.550  12.068  1.00 18.06  ? 1074 LEU   A N   1 
ATOM   1779 C  CA  . LEU   A 1 222 ? 19.439  56.975  11.928  1.00 17.26  ? 1074 LEU   A CA  1 
ATOM   1780 C  C   . LEU   A 1 222 ? 20.912  57.284  12.233  1.00 17.63  ? 1074 LEU   A C   1 
ATOM   1781 O  O   . LEU   A 1 222 ? 21.600  57.994  11.470  1.00 18.77  ? 1074 LEU   A O   1 
ATOM   1782 C  CB  . LEU   A 1 222 ? 18.499  57.752  12.875  1.00 20.68  ? 1074 LEU   A CB  1 
ATOM   1783 C  CG  . LEU   A 1 222 ? 18.700  59.232  13.083  1.00 24.10  ? 1074 LEU   A CG  1 
ATOM   1784 C  CD1 . LEU   A 1 222 ? 18.644  59.950  11.754  1.00 23.39  ? 1074 LEU   A CD1 1 
ATOM   1785 C  CD2 . LEU   A 1 222 ? 17.608  59.738  14.013  1.00 29.97  ? 1074 LEU   A CD2 1 
ATOM   1786 N  N   . LEU   A 1 223 ? 21.416  56.716  13.327  1.00 18.55  ? 1075 LEU   A N   1 
ATOM   1787 C  CA  . LEU   A 1 223 ? 22.790  56.944  13.738  1.00 18.35  ? 1075 LEU   A CA  1 
ATOM   1788 C  C   . LEU   A 1 223 ? 23.830  56.319  12.822  1.00 19.49  ? 1075 LEU   A C   1 
ATOM   1789 O  O   . LEU   A 1 223 ? 24.964  56.779  12.797  1.00 22.57  ? 1075 LEU   A O   1 
ATOM   1790 C  CB  . LEU   A 1 223 ? 23.011  56.518  15.195  1.00 17.67  ? 1075 LEU   A CB  1 
ATOM   1791 C  CG  . LEU   A 1 223 ? 22.271  57.446  16.157  1.00 23.19  ? 1075 LEU   A CG  1 
ATOM   1792 C  CD1 . LEU   A 1 223 ? 22.168  56.795  17.491  1.00 19.42  ? 1075 LEU   A CD1 1 
ATOM   1793 C  CD2 . LEU   A 1 223 ? 22.943  58.810  16.291  1.00 23.51  ? 1075 LEU   A CD2 1 
ATOM   1794 N  N   . THR   A 1 224 ? 23.448  55.276  12.078  1.00 19.37  ? 1076 THR   A N   1 
ATOM   1795 C  CA  . THR   A 1 224 ? 24.324  54.666  11.075  1.00 18.67  ? 1076 THR   A CA  1 
ATOM   1796 C  C   . THR   A 1 224 ? 24.093  55.237  9.670   1.00 20.93  ? 1076 THR   A C   1 
ATOM   1797 O  O   . THR   A 1 224 ? 24.675  54.736  8.706   1.00 20.84  ? 1076 THR   A O   1 
ATOM   1798 C  CB  . THR   A 1 224 ? 24.204  53.104  11.050  1.00 22.55  ? 1076 THR   A CB  1 
ATOM   1799 O  OG1 . THR   A 1 224 ? 22.940  52.711  10.541  1.00 26.42  ? 1076 THR   A OG1 1 
ATOM   1800 C  CG2 . THR   A 1 224 ? 24.357  52.523  12.431  1.00 21.63  ? 1076 THR   A CG2 1 
ATOM   1801 N  N   . TYR   A 1 225 ? 23.251  56.273  9.553   1.00 15.79  ? 1077 TYR   A N   1 
ATOM   1802 C  CA  . TYR   A 1 225 ? 22.880  56.879  8.255   1.00 17.41  ? 1077 TYR   A CA  1 
ATOM   1803 C  C   . TYR   A 1 225 ? 22.313  55.855  7.280   1.00 19.52  ? 1077 TYR   A C   1 
ATOM   1804 O  O   . TYR   A 1 225 ? 22.532  55.920  6.044   1.00 22.40  ? 1077 TYR   A O   1 
ATOM   1805 C  CB  . TYR   A 1 225 ? 24.034  57.647  7.623   1.00 19.16  ? 1077 TYR   A CB  1 
ATOM   1806 C  CG  . TYR   A 1 225 ? 24.581  58.777  8.458   1.00 21.21  ? 1077 TYR   A CG  1 
ATOM   1807 C  CD1 . TYR   A 1 225 ? 24.056  60.066  8.347   1.00 22.79  ? 1077 TYR   A CD1 1 
ATOM   1808 C  CD2 . TYR   A 1 225 ? 25.655  58.579  9.316   1.00 21.52  ? 1077 TYR   A CD2 1 
ATOM   1809 C  CE1 . TYR   A 1 225 ? 24.557  61.108  9.087   1.00 20.38  ? 1077 TYR   A CE1 1 
ATOM   1810 C  CE2 . TYR   A 1 225 ? 26.172  59.629  10.088  1.00 23.62  ? 1077 TYR   A CE2 1 
ATOM   1811 C  CZ  . TYR   A 1 225 ? 25.634  60.900  9.957   1.00 21.91  ? 1077 TYR   A CZ  1 
ATOM   1812 O  OH  . TYR   A 1 225 ? 26.125  61.955  10.698  1.00 24.13  ? 1077 TYR   A OH  1 
ATOM   1813 N  N   . CYS   A 1 226 ? 21.554  54.913  7.847   1.00 21.40  ? 1078 CYS   A N   1 
ATOM   1814 C  CA  . CYS   A 1 226 ? 20.892  53.886  7.073   1.00 25.70  ? 1078 CYS   A CA  1 
ATOM   1815 C  C   . CYS   A 1 226 ? 21.874  53.157  6.144   1.00 27.50  ? 1078 CYS   A C   1 
ATOM   1816 O  O   . CYS   A 1 226 ? 21.543  52.864  4.988   1.00 28.45  ? 1078 CYS   A O   1 
ATOM   1817 C  CB  . CYS   A 1 226 ? 19.720  54.482  6.283   1.00 25.05  ? 1078 CYS   A CB  1 
ATOM   1818 S  SG  . CYS   A 1 226 ? 18.305  54.968  7.342   1.00 23.53  ? 1078 CYS   A SG  1 
ATOM   1819 N  N   . ASP   A 1 227 ? 23.080  52.881  6.649   1.00 27.79  ? 1079 ASP   A N   1 
ATOM   1820 C  CA  . ASP   A 1 227 ? 24.073  52.148  5.859   1.00 32.52  ? 1079 ASP   A CA  1 
ATOM   1821 C  C   . ASP   A 1 227 ? 23.559  50.722  5.713   1.00 30.84  ? 1079 ASP   A C   1 
ATOM   1822 O  O   . ASP   A 1 227 ? 23.233  50.081  6.713   1.00 29.78  ? 1079 ASP   A O   1 
ATOM   1823 C  CB  . ASP   A 1 227 ? 25.461  52.179  6.528   1.00 34.66  ? 1079 ASP   A CB  1 
ATOM   1824 C  CG  . ASP   A 1 227 ? 26.501  51.317  5.805   1.00 40.83  ? 1079 ASP   A CG  1 
ATOM   1825 O  OD1 . ASP   A 1 227 ? 26.455  51.211  4.557   1.00 37.22  ? 1079 ASP   A OD1 1 
ATOM   1826 O  OD2 . ASP   A 1 227 ? 27.380  50.764  6.510   1.00 40.18  ? 1079 ASP   A OD2 1 
ATOM   1827 N  N   . SER   A 1 228 ? 23.477  50.248  4.474   1.00 34.46  ? 1080 SER   A N   1 
ATOM   1828 C  CA  . SER   A 1 228 ? 22.918  48.923  4.195   1.00 36.66  ? 1080 SER   A CA  1 
ATOM   1829 C  C   . SER   A 1 228 ? 23.716  47.818  4.900   1.00 38.78  ? 1080 SER   A C   1 
ATOM   1830 O  O   . SER   A 1 228 ? 23.125  46.890  5.451   1.00 37.00  ? 1080 SER   A O   1 
ATOM   1831 C  CB  . SER   A 1 228 ? 22.814  48.673  2.687   1.00 41.48  ? 1080 SER   A CB  1 
ATOM   1832 O  OG  . SER   A 1 228 ? 24.041  48.920  2.021   1.00 48.37  ? 1080 SER   A OG  1 
ATOM   1833 N  N   . ASP   A 1 229 ? 25.049  47.945  4.929   1.00 39.45  ? 1081 ASP   A N   1 
ATOM   1834 C  CA  . ASP   A 1 229 ? 25.904  46.943  5.570   1.00 40.74  ? 1081 ASP   A CA  1 
ATOM   1835 C  C   . ASP   A 1 229 ? 25.837  46.975  7.103   1.00 39.19  ? 1081 ASP   A C   1 
ATOM   1836 O  O   . ASP   A 1 229 ? 26.314  46.049  7.748   1.00 44.54  ? 1081 ASP   A O   1 
ATOM   1837 C  CB  . ASP   A 1 229 ? 27.362  47.077  5.109   1.00 42.10  ? 1081 ASP   A CB  1 
ATOM   1838 C  CG  . ASP   A 1 229 ? 27.561  46.735  3.627   1.00 46.98  ? 1081 ASP   A CG  1 
ATOM   1839 O  OD1 . ASP   A 1 229 ? 26.845  45.870  3.066   1.00 50.77  ? 1081 ASP   A OD1 1 
ATOM   1840 O  OD2 . ASP   A 1 229 ? 28.462  47.338  3.014   1.00 52.30  ? 1081 ASP   A OD2 1 
ATOM   1841 N  N   . SER   A 1 230 ? 25.255  48.027  7.675   1.00 36.02  ? 1082 SER   A N   1 
ATOM   1842 C  CA  . SER   A 1 230 ? 25.048  48.142  9.129   1.00 35.76  ? 1082 SER   A CA  1 
ATOM   1843 C  C   . SER   A 1 230 ? 23.561  48.040  9.514   1.00 34.48  ? 1082 SER   A C   1 
ATOM   1844 O  O   . SER   A 1 230 ? 23.181  48.464  10.613  1.00 31.66  ? 1082 SER   A O   1 
ATOM   1845 C  CB  . SER   A 1 230 ? 25.603  49.484  9.638   1.00 33.87  ? 1082 SER   A CB  1 
ATOM   1846 O  OG  . SER   A 1 230 ? 26.773  49.876  8.934   1.00 39.94  ? 1082 SER   A OG  1 
ATOM   1847 N  N   . SER   A 1 231 ? 22.731  47.480  8.634   1.00 31.56  ? 1083 SER   A N   1 
ATOM   1848 C  CA  . SER   A 1 231 ? 21.281  47.463  8.873   1.00 31.40  ? 1083 SER   A CA  1 
ATOM   1849 C  C   . SER   A 1 231 ? 20.960  46.540  10.051  1.00 29.26  ? 1083 SER   A C   1 
ATOM   1850 O  O   . SER   A 1 231 ? 21.733  45.623  10.349  1.00 30.25  ? 1083 SER   A O   1 
ATOM   1851 C  CB  . SER   A 1 231 ? 20.503  47.043  7.618   1.00 35.29  ? 1083 SER   A CB  1 
ATOM   1852 O  OG  . SER   A 1 231 ? 20.579  45.646  7.408   1.00 39.78  ? 1083 SER   A OG  1 
ATOM   1853 N  N   . PRO   A 1 232 ? 19.855  46.819  10.772  1.00 27.42  ? 1084 PRO   A N   1 
ATOM   1854 C  CA  . PRO   A 1 232 ? 19.404  45.886  11.796  1.00 27.64  ? 1084 PRO   A CA  1 
ATOM   1855 C  C   . PRO   A 1 232 ? 19.319  44.441  11.310  1.00 31.44  ? 1084 PRO   A C   1 
ATOM   1856 O  O   . PRO   A 1 232 ? 19.703  43.545  12.051  1.00 33.30  ? 1084 PRO   A O   1 
ATOM   1857 C  CB  . PRO   A 1 232 ? 18.027  46.429  12.180  1.00 26.64  ? 1084 PRO   A CB  1 
ATOM   1858 C  CG  . PRO   A 1 232 ? 18.157  47.910  11.967  1.00 25.86  ? 1084 PRO   A CG  1 
ATOM   1859 C  CD  . PRO   A 1 232 ? 19.011  48.034  10.731  1.00 28.03  ? 1084 PRO   A CD  1 
ATOM   1860 N  N   . MET   A 1 233 ? 18.845  44.224  10.082  1.00 31.73  ? 1085 MET   A N   1 
ATOM   1861 C  CA  . MET   A 1 233 ? 18.811  42.870  9.476   1.00 35.70  ? 1085 MET   A CA  1 
ATOM   1862 C  C   . MET   A 1 233 ? 20.231  42.311  9.329   1.00 36.08  ? 1085 MET   A C   1 
ATOM   1863 O  O   . MET   A 1 233 ? 20.539  41.243  9.850   1.00 37.64  ? 1085 MET   A O   1 
ATOM   1864 C  CB  . MET   A 1 233 ? 18.105  42.909  8.112   1.00 37.12  ? 1085 MET   A CB  1 
ATOM   1865 C  CG  . MET   A 1 233 ? 18.176  41.615  7.297   1.00 47.00  ? 1085 MET   A CG  1 
ATOM   1866 S  SD  . MET   A 1 233 ? 16.948  41.545  5.979   1.00 52.91  ? 1085 MET   A SD  1 
ATOM   1867 C  CE  . MET   A 1 233 ? 17.096  43.174  5.212   1.00 53.81  ? 1085 MET   A CE  1 
ATOM   1868 N  N   . ALA   A 1 234 ? 21.085  43.067  8.643   1.00 36.78  ? 1086 ALA   A N   1 
ATOM   1869 C  CA  . ALA   A 1 234 ? 22.490  42.680  8.407   1.00 36.50  ? 1086 ALA   A CA  1 
ATOM   1870 C  C   . ALA   A 1 234 ? 23.242  42.361  9.692   1.00 35.74  ? 1086 ALA   A C   1 
ATOM   1871 O  O   . ALA   A 1 234 ? 23.921  41.350  9.775   1.00 39.83  ? 1086 ALA   A O   1 
ATOM   1872 C  CB  . ALA   A 1 234 ? 23.230  43.766  7.627   1.00 37.31  ? 1086 ALA   A CB  1 
ATOM   1873 N  N   . LEU   A 1 235 ? 23.097  43.210  10.698  1.00 33.06  ? 1087 LEU   A N   1 
ATOM   1874 C  CA  . LEU   A 1 235 ? 23.809  43.034  11.958  1.00 34.88  ? 1087 LEU   A CA  1 
ATOM   1875 C  C   . LEU   A 1 235 ? 23.269  41.859  12.770  1.00 38.24  ? 1087 LEU   A C   1 
ATOM   1876 O  O   . LEU   A 1 235 ? 24.059  41.072  13.290  1.00 38.18  ? 1087 LEU   A O   1 
ATOM   1877 C  CB  . LEU   A 1 235 ? 23.808  44.325  12.781  1.00 35.38  ? 1087 LEU   A CB  1 
ATOM   1878 C  CG  . LEU   A 1 235 ? 24.622  45.510  12.211  1.00 33.49  ? 1087 LEU   A CG  1 
ATOM   1879 C  CD1 . LEU   A 1 235 ? 24.539  46.725  13.138  1.00 34.67  ? 1087 LEU   A CD1 1 
ATOM   1880 C  CD2 . LEU   A 1 235 ? 26.097  45.137  11.959  1.00 37.04  ? 1087 LEU   A CD2 1 
ATOM   1881 N  N   . PHE   A 1 236 ? 21.947  41.718  12.866  1.00 35.34  ? 1088 PHE   A N   1 
ATOM   1882 C  CA  . PHE   A 1 236 ? 21.366  40.546  13.553  1.00 39.57  ? 1088 PHE   A CA  1 
ATOM   1883 C  C   . PHE   A 1 236 ? 21.723  39.207  12.878  1.00 42.73  ? 1088 PHE   A C   1 
ATOM   1884 O  O   . PHE   A 1 236 ? 21.986  38.236  13.567  1.00 49.60  ? 1088 PHE   A O   1 
ATOM   1885 C  CB  . PHE   A 1 236 ? 19.839  40.667  13.729  1.00 37.78  ? 1088 PHE   A CB  1 
ATOM   1886 C  CG  . PHE   A 1 236 ? 19.418  41.422  14.976  1.00 35.25  ? 1088 PHE   A CG  1 
ATOM   1887 C  CD1 . PHE   A 1 236 ? 19.836  41.003  16.240  1.00 36.24  ? 1088 PHE   A CD1 1 
ATOM   1888 C  CD2 . PHE   A 1 236 ? 18.577  42.533  14.891  1.00 34.73  ? 1088 PHE   A CD2 1 
ATOM   1889 C  CE1 . PHE   A 1 236 ? 19.444  41.689  17.391  1.00 34.82  ? 1088 PHE   A CE1 1 
ATOM   1890 C  CE2 . PHE   A 1 236 ? 18.166  43.224  16.041  1.00 28.66  ? 1088 PHE   A CE2 1 
ATOM   1891 C  CZ  . PHE   A 1 236 ? 18.597  42.796  17.292  1.00 26.27  ? 1088 PHE   A CZ  1 
ATOM   1892 N  N   . LEU   A 1 237 ? 21.727  39.169  11.544  1.00 44.66  ? 1089 LEU   A N   1 
ATOM   1893 C  CA  . LEU   A 1 237 ? 22.066  37.955  10.784  1.00 46.40  ? 1089 LEU   A CA  1 
ATOM   1894 C  C   . LEU   A 1 237 ? 23.540  37.580  10.914  1.00 48.30  ? 1089 LEU   A C   1 
ATOM   1895 O  O   . LEU   A 1 237 ? 23.884  36.399  10.862  1.00 47.67  ? 1089 LEU   A O   1 
ATOM   1896 C  CB  . LEU   A 1 237 ? 21.664  38.083  9.307   1.00 48.40  ? 1089 LEU   A CB  1 
ATOM   1897 C  CG  . LEU   A 1 237 ? 20.158  37.994  9.012   1.00 47.05  ? 1089 LEU   A CG  1 
ATOM   1898 C  CD1 . LEU   A 1 237 ? 19.878  38.343  7.557   1.00 46.36  ? 1089 LEU   A CD1 1 
ATOM   1899 C  CD2 . LEU   A 1 237 ? 19.572  36.622  9.337   1.00 54.80  ? 1089 LEU   A CD2 1 
ATOM   1900 N  N   . LYS   A 1 238 ? 24.399  38.585  11.091  1.00 45.09  ? 1090 LYS   A N   1 
ATOM   1901 C  CA  . LYS   A 1 238 ? 25.788  38.366  11.499  1.00 49.36  ? 1090 LYS   A CA  1 
ATOM   1902 C  C   . LYS   A 1 238 ? 25.806  37.705  12.880  1.00 49.94  ? 1090 LYS   A C   1 
ATOM   1903 O  O   . LYS   A 1 238 ? 26.504  36.711  13.075  1.00 55.18  ? 1090 LYS   A O   1 
ATOM   1904 C  CB  . LYS   A 1 238 ? 26.578  39.688  11.511  1.00 48.54  ? 1090 LYS   A CB  1 
ATOM   1905 C  CG  . LYS   A 1 238 ? 28.083  39.525  11.416  1.00 55.22  ? 1090 LYS   A CG  1 
ATOM   1906 C  CD  . LYS   A 1 238 ? 28.837  40.834  11.323  0.00 52.55  ? 1090 LYS   A CD  1 
ATOM   1907 C  CE  . LYS   A 1 238 ? 28.923  41.522  12.677  0.00 50.85  ? 1090 LYS   A CE  1 
ATOM   1908 N  NZ  . LYS   A 1 238 ? 29.722  42.777  12.614  0.00 48.97  ? 1090 LYS   A NZ  1 
ATOM   1909 N  N   . MET   A 1 239 ? 25.013  38.238  13.815  1.00 48.26  ? 1091 MET   A N   1 
ATOM   1910 C  CA  . MET   A 1 239 ? 24.951  37.725  15.199  1.00 49.35  ? 1091 MET   A CA  1 
ATOM   1911 C  C   . MET   A 1 239 ? 24.452  36.271  15.282  1.00 53.02  ? 1091 MET   A C   1 
ATOM   1912 O  O   . MET   A 1 239 ? 25.063  35.447  15.966  1.00 53.66  ? 1091 MET   A O   1 
ATOM   1913 C  CB  . MET   A 1 239 ? 24.091  38.638  16.098  1.00 48.63  ? 1091 MET   A CB  1 
ATOM   1914 C  CG  . MET   A 1 239 ? 24.754  39.975  16.471  1.00 50.18  ? 1091 MET   A CG  1 
ATOM   1915 S  SD  . MET   A 1 239 ? 23.661  41.214  17.235  1.00 55.43  ? 1091 MET   A SD  1 
ATOM   1916 C  CE  . MET   A 1 239 ? 23.065  40.327  18.669  1.00 55.86  ? 1091 MET   A CE  1 
ATOM   1917 N  N   . ILE   A 1 240 ? 23.369  35.970  14.562  1.00 50.80  ? 1092 ILE   A N   1 
ATOM   1918 C  CA  . ILE   A 1 240 ? 22.677  34.668  14.665  1.00 55.32  ? 1092 ILE   A CA  1 
ATOM   1919 C  C   . ILE   A 1 240 ? 23.026  33.616  13.599  1.00 59.30  ? 1092 ILE   A C   1 
ATOM   1920 O  O   . ILE   A 1 240 ? 22.709  32.438  13.772  1.00 63.64  ? 1092 ILE   A O   1 
ATOM   1921 C  CB  . ILE   A 1 240 ? 21.126  34.849  14.695  1.00 52.21  ? 1092 ILE   A CB  1 
ATOM   1922 C  CG1 . ILE   A 1 240 ? 20.572  35.332  13.342  1.00 53.45  ? 1092 ILE   A CG1 1 
ATOM   1923 C  CG2 . ILE   A 1 240 ? 20.745  35.767  15.818  1.00 49.67  ? 1092 ILE   A CG2 1 
ATOM   1924 C  CD1 . ILE   A 1 240 ? 19.168  35.926  13.368  0.00 50.51  ? 1092 ILE   A CD1 1 
ATOM   1925 N  N   . GLY   A 1 241 ? 23.648  34.049  12.502  1.00 59.47  ? 1093 GLY   A N   1 
ATOM   1926 C  CA  . GLY   A 1 241 ? 23.895  33.201  11.335  1.00 63.92  ? 1093 GLY   A CA  1 
ATOM   1927 C  C   . GLY   A 1 241 ? 22.938  33.604  10.225  1.00 63.32  ? 1093 GLY   A C   1 
ATOM   1928 O  O   . GLY   A 1 241 ? 21.751  33.825  10.496  1.00 63.54  ? 1093 GLY   A O   1 
ATOM   1929 N  N   . PRO   A 1 242 ? 23.443  33.768  8.986   1.00 63.96  ? 1094 PRO   A N   1 
ATOM   1930 C  CA  . PRO   A 1 242 ? 22.551  34.169  7.888   1.00 65.47  ? 1094 PRO   A CA  1 
ATOM   1931 C  C   . PRO   A 1 242 ? 21.568  33.090  7.438   1.00 69.96  ? 1094 PRO   A C   1 
ATOM   1932 O  O   . PRO   A 1 242 ? 20.354  33.320  7.456   1.00 71.43  ? 1094 PRO   A O   1 
ATOM   1933 C  CB  . PRO   A 1 242 ? 23.517  34.527  6.750   1.00 66.74  ? 1094 PRO   A CB  1 
ATOM   1934 C  CG  . PRO   A 1 242 ? 24.786  33.833  7.066   1.00 68.32  ? 1094 PRO   A CG  1 
ATOM   1935 C  CD  . PRO   A 1 242 ? 24.852  33.677  8.553   1.00 66.18  ? 1094 PRO   A CD  1 
ATOM   1936 N  N   . THR   A 1 243 ? 22.106  31.926  7.090   1.00 72.70  ? 1095 THR   A N   1 
ATOM   1937 C  CA  . THR   A 1 243 ? 21.397  30.901  6.327   1.00 77.09  ? 1095 THR   A CA  1 
ATOM   1938 C  C   . THR   A 1 243 ? 20.671  29.870  7.212   1.00 79.35  ? 1095 THR   A C   1 
ATOM   1939 O  O   . THR   A 1 243 ? 21.038  28.689  7.241   1.00 85.25  ? 1095 THR   A O   1 
ATOM   1940 C  CB  . THR   A 1 243 ? 22.388  30.193  5.362   1.00 82.58  ? 1095 THR   A CB  1 
ATOM   1941 O  OG1 . THR   A 1 243 ? 23.493  29.645  6.103   1.00 78.99  ? 1095 THR   A OG1 1 
ATOM   1942 C  CG2 . THR   A 1 243 ? 22.915  31.179  4.319   1.00 80.06  ? 1095 THR   A CG2 1 
ATOM   1943 N  N   . HIS   A 1 244 ? 19.638  30.323  7.927   1.00 75.11  ? 1096 HIS   A N   1 
ATOM   1944 C  CA  . HIS   A 1 244 ? 18.818  29.438  8.782   1.00 76.57  ? 1096 HIS   A CA  1 
ATOM   1945 C  C   . HIS   A 1 244 ? 17.335  29.326  8.385   1.00 76.40  ? 1096 HIS   A C   1 
ATOM   1946 O  O   . HIS   A 1 244 ? 16.614  28.509  8.962   1.00 76.38  ? 1096 HIS   A O   1 
ATOM   1947 C  CB  . HIS   A 1 244 ? 18.950  29.862  10.245  1.00 73.77  ? 1096 HIS   A CB  1 
ATOM   1948 C  CG  . HIS   A 1 244 ? 20.336  29.705  10.788  1.00 74.60  ? 1096 HIS   A CG  1 
ATOM   1949 N  ND1 . HIS   A 1 244 ? 20.762  28.565  11.436  1.00 76.24  ? 1096 HIS   A ND1 1 
ATOM   1950 C  CD2 . HIS   A 1 244 ? 21.401  30.539  10.758  1.00 72.98  ? 1096 HIS   A CD2 1 
ATOM   1951 C  CE1 . HIS   A 1 244 ? 22.025  28.712  11.797  1.00 76.96  ? 1096 HIS   A CE1 1 
ATOM   1952 N  NE2 . HIS   A 1 244 ? 22.438  29.900  11.393  1.00 69.53  ? 1096 HIS   A NE2 1 
ATOM   1953 N  N   . GLY   A 1 245 ? 16.891  30.135  7.417   1.00 72.91  ? 1097 GLY   A N   1 
ATOM   1954 C  CA  . GLY   A 1 245 ? 15.554  30.017  6.820   1.00 73.67  ? 1097 GLY   A CA  1 
ATOM   1955 C  C   . GLY   A 1 245 ? 14.391  30.175  7.791   1.00 71.96  ? 1097 GLY   A C   1 
ATOM   1956 O  O   . GLY   A 1 245 ? 14.238  31.224  8.413   1.00 66.78  ? 1097 GLY   A O   1 
ATOM   1957 N  N   . GLN   A 1 246 ? 13.588  29.113  7.923   1.00 75.83  ? 1098 GLN   A N   1 
ATOM   1958 C  CA  . GLN   A 1 246 ? 12.429  29.080  8.838   1.00 74.67  ? 1098 GLN   A CA  1 
ATOM   1959 C  C   . GLN   A 1 246 ? 12.797  29.058  10.337  1.00 73.09  ? 1098 GLN   A C   1 
ATOM   1960 O  O   . GLN   A 1 246 ? 11.928  29.296  11.179  1.00 73.61  ? 1098 GLN   A O   1 
ATOM   1961 C  CB  . GLN   A 1 246 ? 11.531  27.871  8.515   1.00 80.99  ? 1098 GLN   A CB  1 
ATOM   1962 C  CG  . GLN   A 1 246 ? 10.733  28.037  7.210   0.00 79.55  ? 1098 GLN   A CG  1 
ATOM   1963 C  CD  . GLN   A 1 246 ? 9.792   26.869  6.948   0.00 84.48  ? 1098 GLN   A CD  1 
ATOM   1964 O  OE1 . GLN   A 1 246 ? 9.992   25.761  7.452   0.00 88.22  ? 1098 GLN   A OE1 1 
ATOM   1965 N  NE2 . GLN   A 1 246 ? 8.761   27.113  6.148   0.00 84.19  ? 1098 GLN   A NE2 1 
ATOM   1966 N  N   . MET   A 1 247 ? 14.063  28.759  10.661  1.00 69.70  ? 1099 MET   A N   1 
ATOM   1967 C  CA  . MET   A 1 247 ? 14.569  28.779  12.050  1.00 66.96  ? 1099 MET   A CA  1 
ATOM   1968 C  C   . MET   A 1 247 ? 15.101  30.155  12.486  1.00 60.00  ? 1099 MET   A C   1 
ATOM   1969 O  O   . MET   A 1 247 ? 15.476  30.326  13.652  1.00 56.76  ? 1099 MET   A O   1 
ATOM   1970 C  CB  . MET   A 1 247 ? 15.695  27.743  12.217  1.00 71.88  ? 1099 MET   A CB  1 
ATOM   1971 C  CG  . MET   A 1 247 ? 15.502  26.726  13.358  1.00 78.82  ? 1099 MET   A CG  1 
ATOM   1972 S  SD  . MET   A 1 247 ? 13.912  25.855  13.410  1.00 72.51  ? 1099 MET   A SD  1 
ATOM   1973 C  CE  . MET   A 1 247 ? 13.527  25.640  11.669  1.00 73.66  ? 1099 MET   A CE  1 
ATOM   1974 N  N   . THR   A 1 248 ? 15.148  31.115  11.565  1.00 56.94  ? 1100 THR   A N   1 
ATOM   1975 C  CA  . THR   A 1 248 ? 15.753  32.434  11.828  1.00 53.66  ? 1100 THR   A CA  1 
ATOM   1976 C  C   . THR   A 1 248 ? 15.134  33.148  13.035  1.00 48.31  ? 1100 THR   A C   1 
ATOM   1977 O  O   . THR   A 1 248 ? 15.857  33.573  13.937  1.00 49.78  ? 1100 THR   A O   1 
ATOM   1978 C  CB  . THR   A 1 248 ? 15.665  33.342  10.573  1.00 51.30  ? 1100 THR   A CB  1 
ATOM   1979 O  OG1 . THR   A 1 248 ? 16.330  32.694  9.481   1.00 57.03  ? 1100 THR   A OG1 1 
ATOM   1980 C  CG2 . THR   A 1 248 ? 16.314  34.719  10.816  1.00 50.33  ? 1100 THR   A CG2 1 
ATOM   1981 N  N   . VAL   A 1 249 ? 13.803  33.266  13.048  1.00 49.35  ? 1101 VAL   A N   1 
ATOM   1982 C  CA  . VAL   A 1 249 ? 13.084  34.026  14.095  1.00 46.61  ? 1101 VAL   A CA  1 
ATOM   1983 C  C   . VAL   A 1 249 ? 13.274  33.401  15.479  1.00 48.42  ? 1101 VAL   A C   1 
ATOM   1984 O  O   . VAL   A 1 249 ? 13.328  34.101  16.479  1.00 46.69  ? 1101 VAL   A O   1 
ATOM   1985 C  CB  . VAL   A 1 249 ? 11.568  34.177  13.761  1.00 47.49  ? 1101 VAL   A CB  1 
ATOM   1986 C  CG1 . VAL   A 1 249 ? 10.762  34.745  14.938  1.00 50.44  ? 1101 VAL   A CG1 1 
ATOM   1987 C  CG2 . VAL   A 1 249 ? 11.380  35.045  12.531  1.00 48.62  ? 1101 VAL   A CG2 1 
ATOM   1988 N  N   . THR   A 1 250 ? 13.382  32.080  15.533  1.00 54.22  ? 1102 THR   A N   1 
ATOM   1989 C  CA  . THR   A 1 250 ? 13.622  31.388  16.799  1.00 56.67  ? 1102 THR   A CA  1 
ATOM   1990 C  C   . THR   A 1 250 ? 15.022  31.690  17.350  1.00 54.90  ? 1102 THR   A C   1 
ATOM   1991 O  O   . THR   A 1 250 ? 15.178  31.948  18.545  1.00 52.12  ? 1102 THR   A O   1 
ATOM   1992 C  CB  . THR   A 1 250 ? 13.419  29.879  16.645  1.00 63.24  ? 1102 THR   A CB  1 
ATOM   1993 O  OG1 . THR   A 1 250 ? 12.246  29.648  15.855  1.00 66.30  ? 1102 THR   A OG1 1 
ATOM   1994 C  CG2 . THR   A 1 250 ? 13.247  29.247  17.989  1.00 63.49  ? 1102 THR   A CG2 1 
ATOM   1995 N  N   . ARG   A 1 251 ? 16.022  31.673  16.470  1.00 56.74  ? 1103 ARG   A N   1 
ATOM   1996 C  CA  . ARG   A 1 251 ? 17.398  32.039  16.840  1.00 57.01  ? 1103 ARG   A CA  1 
ATOM   1997 C  C   . ARG   A 1 251 ? 17.505  33.503  17.270  1.00 52.43  ? 1103 ARG   A C   1 
ATOM   1998 O  O   . ARG   A 1 251 ? 18.273  33.840  18.169  1.00 50.04  ? 1103 ARG   A O   1 
ATOM   1999 C  CB  . ARG   A 1 251 ? 18.372  31.736  15.691  1.00 58.93  ? 1103 ARG   A CB  1 
ATOM   2000 C  CG  . ARG   A 1 251 ? 18.570  30.246  15.430  1.00 64.75  ? 1103 ARG   A CG  1 
ATOM   2001 C  CD  . ARG   A 1 251 ? 19.734  29.976  14.479  1.00 65.95  ? 1103 ARG   A CD  1 
ATOM   2002 N  NE  . ARG   A 1 251 ? 20.079  28.558  14.368  1.00 71.86  ? 1103 ARG   A NE  1 
ATOM   2003 C  CZ  . ARG   A 1 251 ? 20.902  27.878  15.174  1.00 76.59  ? 1103 ARG   A CZ  1 
ATOM   2004 N  NH1 . ARG   A 1 251 ? 21.133  26.587  14.944  1.00 83.89  ? 1103 ARG   A NH1 1 
ATOM   2005 N  NH2 . ARG   A 1 251 ? 21.503  28.461  16.211  1.00 77.41  ? 1103 ARG   A NH2 1 
ATOM   2006 N  N   . LEU   A 1 252 ? 16.721  34.367  16.630  1.00 49.52  ? 1104 LEU   A N   1 
ATOM   2007 C  CA  . LEU   A 1 252 ? 16.644  35.778  17.013  1.00 47.04  ? 1104 LEU   A CA  1 
ATOM   2008 C  C   . LEU   A 1 252 ? 16.072  35.939  18.430  1.00 47.88  ? 1104 LEU   A C   1 
ATOM   2009 O  O   . LEU   A 1 252 ? 16.656  36.635  19.254  1.00 43.06  ? 1104 LEU   A O   1 
ATOM   2010 C  CB  . LEU   A 1 252 ? 15.807  36.543  15.988  1.00 43.32  ? 1104 LEU   A CB  1 
ATOM   2011 C  CG  . LEU   A 1 252 ? 15.539  38.024  16.220  1.00 39.83  ? 1104 LEU   A CG  1 
ATOM   2012 C  CD1 . LEU   A 1 252 ? 16.860  38.788  16.373  1.00 37.79  ? 1104 LEU   A CD1 1 
ATOM   2013 C  CD2 . LEU   A 1 252 ? 14.703  38.554  15.065  1.00 40.99  ? 1104 LEU   A CD2 1 
ATOM   2014 N  N   . VAL   A 1 253 ? 14.958  35.252  18.711  1.00 51.26  ? 1105 VAL   A N   1 
ATOM   2015 C  CA  . VAL   A 1 253 ? 14.323  35.274  20.043  1.00 50.34  ? 1105 VAL   A CA  1 
ATOM   2016 C  C   . VAL   A 1 253 ? 15.284  34.844  21.158  1.00 51.98  ? 1105 VAL   A C   1 
ATOM   2017 O  O   . VAL   A 1 253 ? 15.350  35.478  22.211  1.00 53.16  ? 1105 VAL   A O   1 
ATOM   2018 C  CB  . VAL   A 1 253 ? 13.063  34.374  20.084  1.00 53.54  ? 1105 VAL   A CB  1 
ATOM   2019 C  CG1 . VAL   A 1 253 ? 12.584  34.146  21.514  1.00 57.41  ? 1105 VAL   A CG1 1 
ATOM   2020 C  CG2 . VAL   A 1 253 ? 11.949  34.974  19.272  1.00 51.42  ? 1105 VAL   A CG2 1 
ATOM   2021 N  N   . ASN   A 1 254 ? 15.998  33.749  20.937  1.00 56.22  ? 1106 ASN   A N   1 
ATOM   2022 C  CA  . ASN   A 1 254 ? 16.974  33.271  21.922  1.00 58.92  ? 1106 ASN   A CA  1 
ATOM   2023 C  C   . ASN   A 1 254 ? 18.107  34.268  22.162  1.00 56.99  ? 1106 ASN   A C   1 
ATOM   2024 O  O   . ASN   A 1 254 ? 18.556  34.437  23.298  1.00 58.81  ? 1106 ASN   A O   1 
ATOM   2025 C  CB  . ASN   A 1 254 ? 17.539  31.900  21.532  1.00 64.01  ? 1106 ASN   A CB  1 
ATOM   2026 C  CG  . ASN   A 1 254 ? 16.951  30.775  22.357  1.00 64.58  ? 1106 ASN   A CG  1 
ATOM   2027 O  OD1 . ASN   A 1 254 ? 15.764  30.783  22.698  1.00 64.74  ? 1106 ASN   A OD1 1 
ATOM   2028 N  ND2 . ASN   A 1 254 ? 17.782  29.812  22.696  1.00 77.06  ? 1106 ASN   A ND2 1 
ATOM   2029 N  N   . THR   A 1 255 ? 18.550  34.927  21.096  1.00 51.93  ? 1107 THR   A N   1 
ATOM   2030 C  CA  . THR   A 1 255 ? 19.590  35.961  21.199  1.00 52.52  ? 1107 THR   A CA  1 
ATOM   2031 C  C   . THR   A 1 255 ? 19.139  37.085  22.136  1.00 48.46  ? 1107 THR   A C   1 
ATOM   2032 O  O   . THR   A 1 255 ? 19.881  37.492  23.035  1.00 45.35  ? 1107 THR   A O   1 
ATOM   2033 C  CB  . THR   A 1 255 ? 19.943  36.532  19.809  1.00 50.32  ? 1107 THR   A CB  1 
ATOM   2034 O  OG1 . THR   A 1 255 ? 20.133  35.458  18.885  1.00 59.40  ? 1107 THR   A OG1 1 
ATOM   2035 C  CG2 . THR   A 1 255 ? 21.209  37.328  19.853  1.00 56.59  ? 1107 THR   A CG2 1 
ATOM   2036 N  N   . LEU   A 1 256 ? 17.908  37.555  21.942  1.00 48.39  ? 1108 LEU   A N   1 
ATOM   2037 C  CA  . LEU   A 1 256 ? 17.368  38.643  22.757  1.00 47.61  ? 1108 LEU   A CA  1 
ATOM   2038 C  C   . LEU   A 1 256 ? 17.132  38.219  24.214  1.00 50.03  ? 1108 LEU   A C   1 
ATOM   2039 O  O   . LEU   A 1 256 ? 17.370  39.003  25.131  1.00 49.15  ? 1108 LEU   A O   1 
ATOM   2040 C  CB  . LEU   A 1 256 ? 16.084  39.193  22.136  1.00 46.17  ? 1108 LEU   A CB  1 
ATOM   2041 C  CG  . LEU   A 1 256 ? 16.226  39.782  20.723  1.00 42.02  ? 1108 LEU   A CG  1 
ATOM   2042 C  CD1 . LEU   A 1 256 ? 14.866  39.951  20.086  1.00 40.04  ? 1108 LEU   A CD1 1 
ATOM   2043 C  CD2 . LEU   A 1 256 ? 17.000  41.142  20.703  1.00 36.14  ? 1108 LEU   A CD2 1 
ATOM   2044 N  N   . LYS   A 1 257 ? 16.670  36.987  24.426  1.00 54.78  ? 1109 LYS   A N   1 
ATOM   2045 C  CA  . LYS   A 1 257 ? 16.548  36.420  25.784  1.00 59.63  ? 1109 LYS   A CA  1 
ATOM   2046 C  C   . LYS   A 1 257 ? 17.870  36.407  26.568  1.00 60.76  ? 1109 LYS   A C   1 
ATOM   2047 O  O   . LYS   A 1 257 ? 17.875  36.628  27.780  1.00 60.46  ? 1109 LYS   A O   1 
ATOM   2048 C  CB  . LYS   A 1 257 ? 15.988  34.991  25.736  1.00 63.91  ? 1109 LYS   A CB  1 
ATOM   2049 C  CG  . LYS   A 1 257 ? 14.501  34.920  25.495  1.00 67.85  ? 1109 LYS   A CG  1 
ATOM   2050 C  CD  . LYS   A 1 257 ? 14.024  33.477  25.554  0.00 71.67  ? 1109 LYS   A CD  1 
ATOM   2051 C  CE  . LYS   A 1 257 ? 12.518  33.393  25.387  0.00 72.14  ? 1109 LYS   A CE  1 
ATOM   2052 N  NZ  . LYS   A 1 257 ? 12.026  31.988  25.436  0.00 76.39  ? 1109 LYS   A NZ  1 
ATOM   2053 N  N   . GLU   A 1 258 ? 18.977  36.152  25.869  1.00 60.28  ? 1110 GLU   A N   1 
ATOM   2054 C  CA  . GLU   A 1 258 ? 20.316  36.139  26.479  1.00 61.41  ? 1110 GLU   A CA  1 
ATOM   2055 C  C   . GLU   A 1 258 ? 20.814  37.519  26.932  1.00 59.54  ? 1110 GLU   A C   1 
ATOM   2056 O  O   . GLU   A 1 258 ? 21.789  37.602  27.683  1.00 61.25  ? 1110 GLU   A O   1 
ATOM   2057 C  CB  . GLU   A 1 258 ? 21.331  35.532  25.505  1.00 62.62  ? 1110 GLU   A CB  1 
ATOM   2058 C  CG  . GLU   A 1 258 ? 21.133  34.032  25.267  1.00 68.04  ? 1110 GLU   A CG  1 
ATOM   2059 C  CD  . GLU   A 1 258 ? 21.714  33.531  23.946  1.00 71.79  ? 1110 GLU   A CD  1 
ATOM   2060 O  OE1 . GLU   A 1 258 ? 22.322  34.323  23.191  1.00 71.17  ? 1110 GLU   A OE1 1 
ATOM   2061 O  OE2 . GLU   A 1 258 ? 21.559  32.326  23.662  1.00 82.13  ? 1110 GLU   A OE2 1 
ATOM   2062 N  N   . GLY   A 1 259 ? 20.151  38.583  26.473  1.00 53.46  ? 1111 GLY   A N   1 
ATOM   2063 C  CA  . GLY   A 1 259 ? 20.517  39.961  26.808  1.00 50.74  ? 1111 GLY   A CA  1 
ATOM   2064 C  C   . GLY   A 1 259 ? 21.286  40.661  25.705  1.00 46.55  ? 1111 GLY   A C   1 
ATOM   2065 O  O   . GLY   A 1 259 ? 21.644  41.831  25.868  1.00 46.48  ? 1111 GLY   A O   1 
ATOM   2066 N  N   . LYS   A 1 260 ? 21.519  39.972  24.582  1.00 46.69  ? 1112 LYS   A N   1 
ATOM   2067 C  CA  . LYS   A 1 260 ? 22.237  40.550  23.430  1.00 43.73  ? 1112 LYS   A CA  1 
ATOM   2068 C  C   . LYS   A 1 260 ? 21.415  41.566  22.637  1.00 42.28  ? 1112 LYS   A C   1 
ATOM   2069 O  O   . LYS   A 1 260 ? 20.231  41.373  22.367  1.00 38.69  ? 1112 LYS   A O   1 
ATOM   2070 C  CB  . LYS   A 1 260 ? 22.691  39.466  22.458  1.00 46.31  ? 1112 LYS   A CB  1 
ATOM   2071 C  CG  . LYS   A 1 260 ? 23.761  38.532  23.004  1.00 50.56  ? 1112 LYS   A CG  1 
ATOM   2072 C  CD  . LYS   A 1 260 ? 24.113  37.471  21.984  1.00 57.54  ? 1112 LYS   A CD  1 
ATOM   2073 C  CE  . LYS   A 1 260 ? 25.226  36.558  22.486  0.00 59.63  ? 1112 LYS   A CE  1 
ATOM   2074 N  NZ  . LYS   A 1 260 ? 25.607  35.531  21.477  0.00 62.12  ? 1112 LYS   A NZ  1 
ATOM   2075 N  N   . ARG   A 1 261 ? 22.073  42.630  22.210  1.00 38.71  ? 1113 ARG   A N   1 
ATOM   2076 C  CA  . ARG   A 1 261 ? 21.398  43.720  21.526  1.00 35.43  ? 1113 ARG   A CA  1 
ATOM   2077 C  C   . ARG   A 1 261 ? 22.310  44.246  20.439  1.00 34.01  ? 1113 ARG   A C   1 
ATOM   2078 O  O   . ARG   A 1 261 ? 23.506  43.962  20.455  1.00 31.61  ? 1113 ARG   A O   1 
ATOM   2079 C  CB  . ARG   A 1 261 ? 21.061  44.828  22.520  1.00 34.99  ? 1113 ARG   A CB  1 
ATOM   2080 C  CG  . ARG   A 1 261 ? 20.105  44.438  23.644  1.00 35.88  ? 1113 ARG   A CG  1 
ATOM   2081 C  CD  . ARG   A 1 261 ? 18.716  44.178  23.103  1.00 34.85  ? 1113 ARG   A CD  1 
ATOM   2082 N  NE  . ARG   A 1 261 ? 17.759  43.878  24.163  1.00 35.93  ? 1113 ARG   A NE  1 
ATOM   2083 C  CZ  . ARG   A 1 261 ? 17.617  42.709  24.787  1.00 42.06  ? 1113 ARG   A CZ  1 
ATOM   2084 N  NH1 . ARG   A 1 261 ? 18.387  41.683  24.496  1.00 46.15  ? 1113 ARG   A NH1 1 
ATOM   2085 N  NH2 . ARG   A 1 261 ? 16.695  42.568  25.733  1.00 44.16  ? 1113 ARG   A NH2 1 
ATOM   2086 N  N   . LEU   A 1 262 ? 21.730  44.961  19.477  1.00 32.87  ? 1114 LEU   A N   1 
ATOM   2087 C  CA  . LEU   A 1 262 ? 22.505  45.647  18.442  1.00 32.47  ? 1114 LEU   A CA  1 
ATOM   2088 C  C   . LEU   A 1 262 ? 23.586  46.525  19.109  1.00 33.42  ? 1114 LEU   A C   1 
ATOM   2089 O  O   . LEU   A 1 262 ? 23.329  47.175  20.140  1.00 31.35  ? 1114 LEU   A O   1 
ATOM   2090 C  CB  . LEU   A 1 262 ? 21.608  46.522  17.558  1.00 32.19  ? 1114 LEU   A CB  1 
ATOM   2091 C  CG  . LEU   A 1 262 ? 20.626  45.846  16.590  1.00 32.53  ? 1114 LEU   A CG  1 
ATOM   2092 C  CD1 . LEU   A 1 262 ? 19.678  46.872  15.989  1.00 28.84  ? 1114 LEU   A CD1 1 
ATOM   2093 C  CD2 . LEU   A 1 262 ? 21.343  45.094  15.480  1.00 33.37  ? 1114 LEU   A CD2 1 
ATOM   2094 N  N   . PRO   A 1 263 ? 24.798  46.529  18.534  1.00 32.42  ? 1115 PRO   A N   1 
ATOM   2095 C  CA  . PRO   A 1 263 ? 25.894  47.280  19.147  1.00 30.86  ? 1115 PRO   A CA  1 
ATOM   2096 C  C   . PRO   A 1 263 ? 25.797  48.793  18.945  1.00 27.88  ? 1115 PRO   A C   1 
ATOM   2097 O  O   . PRO   A 1 263 ? 24.999  49.272  18.147  1.00 26.55  ? 1115 PRO   A O   1 
ATOM   2098 C  CB  . PRO   A 1 263 ? 27.122  46.730  18.425  1.00 33.52  ? 1115 PRO   A CB  1 
ATOM   2099 C  CG  . PRO   A 1 263 ? 26.622  46.382  17.080  1.00 35.78  ? 1115 PRO   A CG  1 
ATOM   2100 C  CD  . PRO   A 1 263 ? 25.239  45.833  17.309  1.00 33.92  ? 1115 PRO   A CD  1 
ATOM   2101 N  N   . CYS   A 1 264 ? 26.647  49.520  19.659  1.00 24.87  ? 1116 CYS   A N   1 
ATOM   2102 C  CA  . CYS   A 1 264 ? 26.717  50.974  19.546  1.00 26.05  ? 1116 CYS   A CA  1 
ATOM   2103 C  C   . CYS   A 1 264 ? 27.166  51.392  18.138  1.00 24.60  ? 1116 CYS   A C   1 
ATOM   2104 O  O   . CYS   A 1 264 ? 28.211  50.920  17.673  1.00 26.36  ? 1116 CYS   A O   1 
ATOM   2105 C  CB  . CYS   A 1 264 ? 27.725  51.538  20.554  1.00 24.65  ? 1116 CYS   A CB  1 
ATOM   2106 S  SG  . CYS   A 1 264 ? 27.607  53.323  20.658  1.00 24.91  ? 1116 CYS   A SG  1 
ATOM   2107 N  N   . PRO   A 1 265 ? 26.378  52.246  17.451  1.00 25.79  ? 1117 PRO   A N   1 
ATOM   2108 C  CA  . PRO   A 1 265 ? 26.815  52.751  16.144  1.00 23.89  ? 1117 PRO   A CA  1 
ATOM   2109 C  C   . PRO   A 1 265 ? 28.193  53.426  16.182  1.00 28.63  ? 1117 PRO   A C   1 
ATOM   2110 O  O   . PRO   A 1 265 ? 28.572  53.970  17.234  1.00 24.90  ? 1117 PRO   A O   1 
ATOM   2111 C  CB  . PRO   A 1 265 ? 25.736  53.771  15.769  1.00 19.48  ? 1117 PRO   A CB  1 
ATOM   2112 C  CG  . PRO   A 1 265 ? 24.578  53.416  16.518  1.00 23.41  ? 1117 PRO   A CG  1 
ATOM   2113 C  CD  . PRO   A 1 265 ? 25.019  52.705  17.780  1.00 23.81  ? 1117 PRO   A CD  1 
ATOM   2114 N  N   . PRO   A 1 266 ? 28.940  53.391  15.052  1.00 32.52  ? 1118 PRO   A N   1 
ATOM   2115 C  CA  . PRO   A 1 266 ? 30.178  54.145  14.950  1.00 31.65  ? 1118 PRO   A CA  1 
ATOM   2116 C  C   . PRO   A 1 266 ? 29.993  55.616  15.282  1.00 29.26  ? 1118 PRO   A C   1 
ATOM   2117 O  O   . PRO   A 1 266 ? 29.039  56.242  14.814  1.00 27.79  ? 1118 PRO   A O   1 
ATOM   2118 C  CB  . PRO   A 1 266 ? 30.561  53.980  13.477  1.00 34.90  ? 1118 PRO   A CB  1 
ATOM   2119 C  CG  . PRO   A 1 266 ? 30.017  52.669  13.120  1.00 38.34  ? 1118 PRO   A CG  1 
ATOM   2120 C  CD  . PRO   A 1 266 ? 28.697  52.616  13.819  1.00 34.59  ? 1118 PRO   A CD  1 
ATOM   2121 N  N   . ASN   A 1 267 ? 30.876  56.140  16.127  1.00 27.69  ? 1119 ASN   A N   1 
ATOM   2122 C  CA  . ASN   A 1 267 ? 30.861  57.552  16.507  1.00 29.18  ? 1119 ASN   A CA  1 
ATOM   2123 C  C   . ASN   A 1 267 ? 29.636  57.991  17.306  1.00 24.97  ? 1119 ASN   A C   1 
ATOM   2124 O  O   . ASN   A 1 267 ? 29.410  59.190  17.463  1.00 28.19  ? 1119 ASN   A O   1 
ATOM   2125 C  CB  . ASN   A 1 267 ? 31.004  58.462  15.273  1.00 26.57  ? 1119 ASN   A CB  1 
ATOM   2126 C  CG  . ASN   A 1 267 ? 32.133  58.049  14.383  1.00 37.23  ? 1119 ASN   A CG  1 
ATOM   2127 O  OD1 . ASN   A 1 267 ? 31.925  57.507  13.292  1.00 39.64  ? 1119 ASN   A OD1 1 
ATOM   2128 N  ND2 . ASN   A 1 267 ? 33.343  58.285  14.846  1.00 34.01  ? 1119 ASN   A ND2 1 
ATOM   2129 N  N   . CYS   A 1 268 ? 28.852  57.039  17.814  1.00 22.38  ? 1120 CYS   A N   1 
ATOM   2130 C  CA  . CYS   A 1 268 ? 27.650  57.371  18.582  1.00 23.21  ? 1120 CYS   A CA  1 
ATOM   2131 C  C   . CYS   A 1 268 ? 28.097  57.442  20.025  1.00 23.41  ? 1120 CYS   A C   1 
ATOM   2132 O  O   . CYS   A 1 268 ? 28.601  56.451  20.544  1.00 24.86  ? 1120 CYS   A O   1 
ATOM   2133 C  CB  . CYS   A 1 268 ? 26.567  56.301  18.448  1.00 24.39  ? 1120 CYS   A CB  1 
ATOM   2134 S  SG  . CYS   A 1 268 ? 25.144  56.594  19.535  1.00 23.50  ? 1120 CYS   A SG  1 
ATOM   2135 N  N   . PRO   A 1 269 ? 27.940  58.616  20.677  1.00 22.39  ? 1121 PRO   A N   1 
ATOM   2136 C  CA  . PRO   A 1 269 ? 28.362  58.709  22.066  1.00 23.47  ? 1121 PRO   A CA  1 
ATOM   2137 C  C   . PRO   A 1 269 ? 27.589  57.719  22.952  1.00 21.77  ? 1121 PRO   A C   1 
ATOM   2138 O  O   . PRO   A 1 269 ? 26.376  57.467  22.722  1.00 21.91  ? 1121 PRO   A O   1 
ATOM   2139 C  CB  . PRO   A 1 269 ? 28.031  60.167  22.451  1.00 22.22  ? 1121 PRO   A CB  1 
ATOM   2140 C  CG  . PRO   A 1 269 ? 27.730  60.880  21.204  1.00 25.52  ? 1121 PRO   A CG  1 
ATOM   2141 C  CD  . PRO   A 1 269 ? 27.304  59.863  20.197  1.00 18.34  ? 1121 PRO   A CD  1 
ATOM   2142 N  N   . ASP   A 1 270 ? 28.262  57.212  23.977  1.00 25.24  ? 1122 ASP   A N   1 
ATOM   2143 C  CA  . ASP   A 1 270 ? 27.652  56.246  24.905  1.00 26.86  ? 1122 ASP   A CA  1 
ATOM   2144 C  C   . ASP   A 1 270 ? 26.328  56.747  25.507  1.00 25.85  ? 1122 ASP   A C   1 
ATOM   2145 O  O   . ASP   A 1 270 ? 25.408  55.969  25.724  1.00 22.44  ? 1122 ASP   A O   1 
ATOM   2146 C  CB  . ASP   A 1 270 ? 28.588  55.890  26.049  1.00 27.00  ? 1122 ASP   A CB  1 
ATOM   2147 C  CG  . ASP   A 1 270 ? 28.017  54.792  26.909  1.00 33.80  ? 1122 ASP   A CG  1 
ATOM   2148 O  OD1 . ASP   A 1 270 ? 27.909  53.656  26.401  1.00 29.78  ? 1122 ASP   A OD1 1 
ATOM   2149 O  OD2 . ASP   A 1 270 ? 27.594  55.076  28.050  1.00 34.47  ? 1122 ASP   A OD2 1 
ATOM   2150 N  N   . GLU   A 1 271 ? 26.255  58.044  25.781  1.00 25.88  ? 1123 GLU   A N   1 
ATOM   2151 C  CA  . GLU   A 1 271 ? 25.063  58.640  26.380  1.00 27.92  ? 1123 GLU   A CA  1 
ATOM   2152 C  C   . GLU   A 1 271 ? 23.837  58.538  25.482  1.00 24.08  ? 1123 GLU   A C   1 
ATOM   2153 O  O   . GLU   A 1 271 ? 22.724  58.369  25.965  1.00 25.78  ? 1123 GLU   A O   1 
ATOM   2154 C  CB  . GLU   A 1 271 ? 25.318  60.096  26.854  1.00 31.32  ? 1123 GLU   A CB  1 
ATOM   2155 C  CG  . GLU   A 1 271 ? 25.770  61.096  25.793  1.00 32.97  ? 1123 GLU   A CG  1 
ATOM   2156 C  CD  . GLU   A 1 271 ? 27.282  61.245  25.654  1.00 33.75  ? 1123 GLU   A CD  1 
ATOM   2157 O  OE1 . GLU   A 1 271 ? 28.022  60.304  25.997  1.00 29.69  ? 1123 GLU   A OE1 1 
ATOM   2158 O  OE2 . GLU   A 1 271 ? 27.727  62.310  25.157  1.00 33.77  ? 1123 GLU   A OE2 1 
ATOM   2159 N  N   . VAL   A 1 272 ? 24.048  58.616  24.167  1.00 17.94  ? 1124 VAL   A N   1 
ATOM   2160 C  CA  . VAL   A 1 272 ? 22.981  58.404  23.201  1.00 21.97  ? 1124 VAL   A CA  1 
ATOM   2161 C  C   . VAL   A 1 272 ? 22.616  56.912  23.146  1.00 21.99  ? 1124 VAL   A C   1 
ATOM   2162 O  O   . VAL   A 1 272 ? 21.426  56.543  23.098  1.00 24.72  ? 1124 VAL   A O   1 
ATOM   2163 C  CB  . VAL   A 1 272 ? 23.409  58.917  21.814  1.00 17.76  ? 1124 VAL   A CB  1 
ATOM   2164 C  CG1 . VAL   A 1 272 ? 22.342  58.623  20.768  1.00 18.34  ? 1124 VAL   A CG1 1 
ATOM   2165 C  CG2 . VAL   A 1 272 ? 23.726  60.439  21.870  1.00 16.67  ? 1124 VAL   A CG2 1 
ATOM   2166 N  N   . TYR   A 1 273 ? 23.642  56.063  23.114  1.00 22.50  ? 1125 TYR   A N   1 
ATOM   2167 C  CA  . TYR   A 1 273 ? 23.451  54.603  23.118  1.00 21.82  ? 1125 TYR   A CA  1 
ATOM   2168 C  C   . TYR   A 1 273 ? 22.691  54.109  24.349  1.00 25.64  ? 1125 TYR   A C   1 
ATOM   2169 O  O   . TYR   A 1 273 ? 21.867  53.203  24.238  1.00 25.84  ? 1125 TYR   A O   1 
ATOM   2170 C  CB  . TYR   A 1 273 ? 24.795  53.881  22.999  1.00 24.10  ? 1125 TYR   A CB  1 
ATOM   2171 C  CG  . TYR   A 1 273 ? 24.695  52.360  22.819  1.00 24.84  ? 1125 TYR   A CG  1 
ATOM   2172 C  CD1 . TYR   A 1 273 ? 23.949  51.803  21.769  1.00 23.46  ? 1125 TYR   A CD1 1 
ATOM   2173 C  CD2 . TYR   A 1 273 ? 25.369  51.497  23.666  1.00 30.56  ? 1125 TYR   A CD2 1 
ATOM   2174 C  CE1 . TYR   A 1 273 ? 23.874  50.387  21.598  1.00 26.08  ? 1125 TYR   A CE1 1 
ATOM   2175 C  CE2 . TYR   A 1 273 ? 25.296  50.102  23.513  1.00 31.08  ? 1125 TYR   A CE2 1 
ATOM   2176 C  CZ  . TYR   A 1 273 ? 24.547  49.560  22.477  1.00 30.74  ? 1125 TYR   A CZ  1 
ATOM   2177 O  OH  . TYR   A 1 273 ? 24.504  48.180  22.336  1.00 32.97  ? 1125 TYR   A OH  1 
ATOM   2178 N  N   . GLN   A 1 274 ? 22.946  54.711  25.511  1.00 25.62  ? 1126 GLN   A N   1 
ATOM   2179 C  CA  . GLN   A 1 274 ? 22.189  54.363  26.717  1.00 28.32  ? 1126 GLN   A CA  1 
ATOM   2180 C  C   . GLN   A 1 274 ? 20.683  54.621  26.561  1.00 27.62  ? 1126 GLN   A C   1 
ATOM   2181 O  O   . GLN   A 1 274 ? 19.865  53.795  26.965  1.00 26.79  ? 1126 GLN   A O   1 
ATOM   2182 C  CB  . GLN   A 1 274 ? 22.749  55.067  27.960  1.00 30.48  ? 1126 GLN   A CB  1 
ATOM   2183 C  CG  . GLN   A 1 274 ? 24.100  54.531  28.483  1.00 37.39  ? 1126 GLN   A CG  1 
ATOM   2184 C  CD  . GLN   A 1 274 ? 24.228  53.016  28.408  1.00 41.94  ? 1126 GLN   A CD  1 
ATOM   2185 O  OE1 . GLN   A 1 274 ? 23.409  52.278  28.966  1.00 39.41  ? 1126 GLN   A OE1 1 
ATOM   2186 N  NE2 . GLN   A 1 274 ? 25.244  52.548  27.693  1.00 38.82  ? 1126 GLN   A NE2 1 
ATOM   2187 N  N   . LEU   A 1 275 ? 20.312  55.735  25.929  1.00 27.19  ? 1127 LEU   A N   1 
ATOM   2188 C  CA  . LEU   A 1 275 ? 18.893  56.010  25.647  1.00 26.30  ? 1127 LEU   A CA  1 
ATOM   2189 C  C   . LEU   A 1 275 ? 18.280  54.949  24.727  1.00 25.68  ? 1127 LEU   A C   1 
ATOM   2190 O  O   . LEU   A 1 275 ? 17.139  54.525  24.917  1.00 25.14  ? 1127 LEU   A O   1 
ATOM   2191 C  CB  . LEU   A 1 275 ? 18.723  57.395  25.006  1.00 27.05  ? 1127 LEU   A CB  1 
ATOM   2192 C  CG  . LEU   A 1 275 ? 18.675  58.636  25.895  1.00 32.11  ? 1127 LEU   A CG  1 
ATOM   2193 C  CD1 . LEU   A 1 275 ? 19.600  58.596  27.060  1.00 47.67  ? 1127 LEU   A CD1 1 
ATOM   2194 C  CD2 . LEU   A 1 275 ? 18.966  59.861  25.033  1.00 35.22  ? 1127 LEU   A CD2 1 
ATOM   2195 N  N   . MET   A 1 276 ? 19.042  54.543  23.717  1.00 24.37  ? 1128 MET   A N   1 
ATOM   2196 C  CA  . MET   A 1 276 ? 18.660  53.460  22.815  1.00 22.19  ? 1128 MET   A CA  1 
ATOM   2197 C  C   . MET   A 1 276 ? 18.437  52.124  23.542  1.00 23.97  ? 1128 MET   A C   1 
ATOM   2198 O  O   . MET   A 1 276 ? 17.482  51.405  23.237  1.00 27.24  ? 1128 MET   A O   1 
ATOM   2199 C  CB  . MET   A 1 276 ? 19.745  53.301  21.740  1.00 21.93  ? 1128 MET   A CB  1 
ATOM   2200 C  CG  . MET   A 1 276 ? 19.415  52.379  20.586  1.00 24.09  ? 1128 MET   A CG  1 
ATOM   2201 S  SD  . MET   A 1 276 ? 20.873  52.062  19.564  1.00 29.83  ? 1128 MET   A SD  1 
ATOM   2202 C  CE  . MET   A 1 276 ? 21.255  53.699  18.971  1.00 25.40  ? 1128 MET   A CE  1 
ATOM   2203 N  N   . ARG   A 1 277 ? 19.333  51.791  24.475  1.00 26.55  ? 1129 ARG   A N   1 
ATOM   2204 C  CA  . ARG   A 1 277 ? 19.243  50.544  25.253  1.00 31.38  ? 1129 ARG   A CA  1 
ATOM   2205 C  C   . ARG   A 1 277 ? 17.990  50.474  26.154  1.00 32.57  ? 1129 ARG   A C   1 
ATOM   2206 O  O   . ARG   A 1 277 ? 17.441  49.388  26.377  1.00 30.39  ? 1129 ARG   A O   1 
ATOM   2207 C  CB  . ARG   A 1 277 ? 20.501  50.344  26.105  1.00 33.38  ? 1129 ARG   A CB  1 
ATOM   2208 C  CG  . ARG   A 1 277 ? 21.736  49.914  25.323  1.00 37.33  ? 1129 ARG   A CG  1 
ATOM   2209 C  CD  . ARG   A 1 277 ? 22.857  49.462  26.259  1.00 47.35  ? 1129 ARG   A CD  1 
ATOM   2210 N  NE  . ARG   A 1 277 ? 22.533  48.213  26.965  1.00 51.26  ? 1129 ARG   A NE  1 
ATOM   2211 C  CZ  . ARG   A 1 277 ? 22.524  46.988  26.427  1.00 52.71  ? 1129 ARG   A CZ  1 
ATOM   2212 N  NH1 . ARG   A 1 277 ? 22.823  46.783  25.144  1.00 51.11  ? 1129 ARG   A NH1 1 
ATOM   2213 N  NH2 . ARG   A 1 277 ? 22.213  45.939  27.188  1.00 59.61  ? 1129 ARG   A NH2 1 
ATOM   2214 N  N   . LYS   A 1 278 ? 17.558  51.626  26.666  1.00 30.02  ? 1130 LYS   A N   1 
ATOM   2215 C  CA  . LYS   A 1 278 ? 16.290  51.745  27.412  1.00 31.14  ? 1130 LYS   A CA  1 
ATOM   2216 C  C   . LYS   A 1 278 ? 15.042  51.396  26.596  1.00 32.85  ? 1130 LYS   A C   1 
ATOM   2217 O  O   . LYS   A 1 278 ? 13.996  51.044  27.166  1.00 34.27  ? 1130 LYS   A O   1 
ATOM   2218 C  CB  . LYS   A 1 278 ? 16.139  53.155  27.983  1.00 29.68  ? 1130 LYS   A CB  1 
ATOM   2219 C  CG  . LYS   A 1 278 ? 17.081  53.447  29.154  1.00 32.15  ? 1130 LYS   A CG  1 
ATOM   2220 C  CD  . LYS   A 1 278 ? 17.047  54.926  29.523  1.00 41.75  ? 1130 LYS   A CD  1 
ATOM   2221 C  CE  . LYS   A 1 278 ? 18.066  55.262  30.588  1.00 47.98  ? 1130 LYS   A CE  1 
ATOM   2222 N  NZ  . LYS   A 1 278 ? 17.818  54.542  31.861  1.00 58.31  ? 1130 LYS   A NZ  1 
ATOM   2223 N  N   . CYS   A 1 279 ? 15.156  51.506  25.272  1.00 26.67  ? 1131 CYS   A N   1 
ATOM   2224 C  CA  . CYS   A 1 279 ? 14.124  51.053  24.355  1.00 28.21  ? 1131 CYS   A CA  1 
ATOM   2225 C  C   . CYS   A 1 279 ? 14.020  49.540  24.263  1.00 28.84  ? 1131 CYS   A C   1 
ATOM   2226 O  O   . CYS   A 1 279 ? 13.005  49.036  23.796  1.00 28.54  ? 1131 CYS   A O   1 
ATOM   2227 C  CB  . CYS   A 1 279 ? 14.378  51.596  22.959  1.00 25.79  ? 1131 CYS   A CB  1 
ATOM   2228 S  SG  . CYS   A 1 279 ? 14.363  53.363  22.879  1.00 23.19  ? 1131 CYS   A SG  1 
ATOM   2229 N  N   . TRP   A 1 280 ? 15.071  48.845  24.705  1.00 30.90  ? 1132 TRP   A N   1 
ATOM   2230 C  CA  . TRP   A 1 280 ? 15.255  47.429  24.483  1.00 28.87  ? 1132 TRP   A CA  1 
ATOM   2231 C  C   . TRP   A 1 280 ? 15.332  46.623  25.784  1.00 33.95  ? 1132 TRP   A C   1 
ATOM   2232 O  O   . TRP   A 1 280 ? 15.976  45.592  25.819  1.00 35.63  ? 1132 TRP   A O   1 
ATOM   2233 C  CB  . TRP   A 1 280 ? 16.527  47.207  23.658  1.00 30.94  ? 1132 TRP   A CB  1 
ATOM   2234 C  CG  . TRP   A 1 280 ? 16.551  47.836  22.296  1.00 25.78  ? 1132 TRP   A CG  1 
ATOM   2235 C  CD1 . TRP   A 1 280 ? 15.482  48.119  21.508  1.00 24.36  ? 1132 TRP   A CD1 1 
ATOM   2236 C  CD2 . TRP   A 1 280 ? 17.716  48.179  21.532  1.00 28.28  ? 1132 TRP   A CD2 1 
ATOM   2237 N  NE1 . TRP   A 1 280 ? 15.895  48.643  20.311  1.00 28.43  ? 1132 TRP   A NE1 1 
ATOM   2238 C  CE2 . TRP   A 1 280 ? 17.261  48.708  20.301  1.00 27.66  ? 1132 TRP   A CE2 1 
ATOM   2239 C  CE3 . TRP   A 1 280 ? 19.092  48.130  21.779  1.00 25.43  ? 1132 TRP   A CE3 1 
ATOM   2240 C  CZ2 . TRP   A 1 280 ? 18.132  49.156  19.306  1.00 24.61  ? 1132 TRP   A CZ2 1 
ATOM   2241 C  CZ3 . TRP   A 1 280 ? 19.970  48.578  20.782  1.00 27.54  ? 1132 TRP   A CZ3 1 
ATOM   2242 C  CH2 . TRP   A 1 280 ? 19.482  49.087  19.563  1.00 22.88  ? 1132 TRP   A CH2 1 
ATOM   2243 N  N   . GLU   A 1 281 ? 14.676  47.077  26.849  1.00 33.63  ? 1133 GLU   A N   1 
ATOM   2244 C  CA  . GLU   A 1 281 ? 14.462  46.222  28.013  1.00 36.97  ? 1133 GLU   A CA  1 
ATOM   2245 C  C   . GLU   A 1 281 ? 13.554  45.077  27.579  1.00 36.93  ? 1133 GLU   A C   1 
ATOM   2246 O  O   . GLU   A 1 281 ? 12.641  45.284  26.798  1.00 37.44  ? 1133 GLU   A O   1 
ATOM   2247 C  CB  . GLU   A 1 281 ? 13.834  47.005  29.167  1.00 39.57  ? 1133 GLU   A CB  1 
ATOM   2248 C  CG  . GLU   A 1 281 ? 14.758  48.024  29.818  1.00 42.65  ? 1133 GLU   A CG  1 
ATOM   2249 C  CD  . GLU   A 1 281 ? 15.856  47.388  30.666  1.00 53.02  ? 1133 GLU   A CD  1 
ATOM   2250 O  OE1 . GLU   A 1 281 ? 16.755  46.728  30.109  1.00 59.67  ? 1133 GLU   A OE1 1 
ATOM   2251 O  OE2 . GLU   A 1 281 ? 15.834  47.556  31.900  1.00 60.62  ? 1133 GLU   A OE2 1 
ATOM   2252 N  N   . PHE   A 1 282 ? 13.817  43.866  28.059  1.00 39.24  ? 1134 PHE   A N   1 
ATOM   2253 C  CA  . PHE   A 1 282 ? 13.080  42.692  27.588  1.00 41.05  ? 1134 PHE   A CA  1 
ATOM   2254 C  C   . PHE   A 1 282 ? 11.587  42.795  27.921  1.00 43.89  ? 1134 PHE   A C   1 
ATOM   2255 O  O   . PHE   A 1 282 ? 10.740  42.543  27.061  1.00 43.72  ? 1134 PHE   A O   1 
ATOM   2256 C  CB  . PHE   A 1 282 ? 13.679  41.403  28.165  1.00 45.06  ? 1134 PHE   A CB  1 
ATOM   2257 C  CG  . PHE   A 1 282 ? 13.297  40.170  27.400  1.00 47.82  ? 1134 PHE   A CG  1 
ATOM   2258 C  CD1 . PHE   A 1 282 ? 14.026  39.780  26.282  1.00 50.39  ? 1134 PHE   A CD1 1 
ATOM   2259 C  CD2 . PHE   A 1 282 ? 12.199  39.411  27.782  1.00 50.99  ? 1134 PHE   A CD2 1 
ATOM   2260 C  CE1 . PHE   A 1 282 ? 13.674  38.637  25.565  1.00 51.49  ? 1134 PHE   A CE1 1 
ATOM   2261 C  CE2 . PHE   A 1 282 ? 11.836  38.279  27.064  1.00 53.73  ? 1134 PHE   A CE2 1 
ATOM   2262 C  CZ  . PHE   A 1 282 ? 12.575  37.897  25.948  1.00 52.36  ? 1134 PHE   A CZ  1 
ATOM   2263 N  N   . GLN   A 1 283 ? 11.281  43.182  29.161  1.00 48.36  ? 1135 GLN   A N   1 
ATOM   2264 C  CA  . GLN   A 1 283 ? 9.899   43.410  29.605  1.00 47.89  ? 1135 GLN   A CA  1 
ATOM   2265 C  C   . GLN   A 1 283 ? 9.386   44.792  29.146  1.00 44.46  ? 1135 GLN   A C   1 
ATOM   2266 O  O   . GLN   A 1 283 ? 10.012  45.809  29.470  1.00 43.19  ? 1135 GLN   A O   1 
ATOM   2267 C  CB  . GLN   A 1 283 ? 9.809   43.307  31.131  1.00 54.86  ? 1135 GLN   A CB  1 
ATOM   2268 C  CG  . GLN   A 1 283 ? 10.195  41.938  31.715  0.00 56.74  ? 1135 GLN   A CG  1 
ATOM   2269 C  CD  . GLN   A 1 283 ? 9.253   40.805  31.322  0.00 59.05  ? 1135 GLN   A CD  1 
ATOM   2270 O  OE1 . GLN   A 1 283 ? 8.090   41.027  30.983  0.00 58.07  ? 1135 GLN   A OE1 1 
ATOM   2271 N  NE2 . GLN   A 1 283 ? 9.759   39.578  31.373  0.00 61.40  ? 1135 GLN   A NE2 1 
ATOM   2272 N  N   . PRO   A 1 284 ? 8.251   44.837  28.405  1.00 43.74  ? 1136 PRO   A N   1 
ATOM   2273 C  CA  . PRO   A 1 284 ? 7.626   46.091  27.957  1.00 41.78  ? 1136 PRO   A CA  1 
ATOM   2274 C  C   . PRO   A 1 284 ? 7.490   47.169  29.036  1.00 42.68  ? 1136 PRO   A C   1 
ATOM   2275 O  O   . PRO   A 1 284 ? 7.716   48.348  28.760  1.00 42.57  ? 1136 PRO   A O   1 
ATOM   2276 C  CB  . PRO   A 1 284 ? 6.232   45.644  27.505  1.00 45.91  ? 1136 PRO   A CB  1 
ATOM   2277 C  CG  . PRO   A 1 284 ? 6.362   44.227  27.155  1.00 45.86  ? 1136 PRO   A CG  1 
ATOM   2278 C  CD  . PRO   A 1 284 ? 7.500   43.660  27.921  1.00 45.41  ? 1136 PRO   A CD  1 
ATOM   2279 N  N   . SER   A 1 285 ? 7.116   46.748  30.245  1.00 48.04  ? 1137 SER   A N   1 
ATOM   2280 C  CA  . SER   A 1 285 ? 6.897   47.659  31.381  1.00 49.67  ? 1137 SER   A CA  1 
ATOM   2281 C  C   . SER   A 1 285 ? 8.171   48.337  31.914  1.00 49.60  ? 1137 SER   A C   1 
ATOM   2282 O  O   . SER   A 1 285 ? 8.091   49.398  32.548  1.00 50.55  ? 1137 SER   A O   1 
ATOM   2283 C  CB  . SER   A 1 285 ? 6.188   46.913  32.526  1.00 53.77  ? 1137 SER   A CB  1 
ATOM   2284 O  OG  . SER   A 1 285 ? 6.730   45.609  32.703  1.00 52.23  ? 1137 SER   A OG  1 
ATOM   2285 N  N   . ASN   A 1 286 ? 9.326   47.720  31.669  1.00 47.74  ? 1138 ASN   A N   1 
ATOM   2286 C  CA  . ASN   A 1 286 ? 10.627  48.317  32.009  1.00 47.01  ? 1138 ASN   A CA  1 
ATOM   2287 C  C   . ASN   A 1 286 ? 11.169  49.339  30.996  1.00 44.44  ? 1138 ASN   A C   1 
ATOM   2288 O  O   . ASN   A 1 286 ? 12.096  50.089  31.321  1.00 45.21  ? 1138 ASN   A O   1 
ATOM   2289 C  CB  . ASN   A 1 286 ? 11.674  47.218  32.204  1.00 46.10  ? 1138 ASN   A CB  1 
ATOM   2290 C  CG  . ASN   A 1 286 ? 11.372  46.318  33.398  1.00 54.11  ? 1138 ASN   A CG  1 
ATOM   2291 O  OD1 . ASN   A 1 286 ? 11.781  45.160  33.423  1.00 59.23  ? 1138 ASN   A OD1 1 
ATOM   2292 N  ND2 . ASN   A 1 286 ? 10.660  46.847  34.388  1.00 51.56  ? 1138 ASN   A ND2 1 
ATOM   2293 N  N   . ARG   A 1 287 ? 10.615  49.376  29.787  1.00 41.24  ? 1139 ARG   A N   1 
ATOM   2294 C  CA  . ARG   A 1 287 ? 11.126  50.289  28.758  1.00 39.06  ? 1139 ARG   A CA  1 
ATOM   2295 C  C   . ARG   A 1 287 ? 10.796  51.752  29.045  1.00 38.45  ? 1139 ARG   A C   1 
ATOM   2296 O  O   . ARG   A 1 287 ? 9.846   52.077  29.768  1.00 42.21  ? 1139 ARG   A O   1 
ATOM   2297 C  CB  . ARG   A 1 287 ? 10.592  49.920  27.382  1.00 37.94  ? 1139 ARG   A CB  1 
ATOM   2298 C  CG  . ARG   A 1 287 ? 11.133  48.614  26.874  1.00 39.46  ? 1139 ARG   A CG  1 
ATOM   2299 C  CD  . ARG   A 1 287 ? 10.375  48.137  25.657  1.00 33.58  ? 1139 ARG   A CD  1 
ATOM   2300 N  NE  . ARG   A 1 287 ? 10.570  46.711  25.502  1.00 34.70  ? 1139 ARG   A NE  1 
ATOM   2301 C  CZ  . ARG   A 1 287 ? 9.772   45.879  24.837  1.00 38.44  ? 1139 ARG   A CZ  1 
ATOM   2302 N  NH1 . ARG   A 1 287 ? 8.716   46.324  24.180  1.00 30.27  ? 1139 ARG   A NH1 1 
ATOM   2303 N  NH2 . ARG   A 1 287 ? 10.056  44.582  24.822  1.00 38.02  ? 1139 ARG   A NH2 1 
ATOM   2304 N  N   . THR   A 1 288 ? 11.605  52.631  28.472  1.00 36.91  ? 1140 THR   A N   1 
ATOM   2305 C  CA  . THR   A 1 288 ? 11.355  54.063  28.527  1.00 34.84  ? 1140 THR   A CA  1 
ATOM   2306 C  C   . THR   A 1 288 ? 10.087  54.404  27.744  1.00 33.51  ? 1140 THR   A C   1 
ATOM   2307 O  O   . THR   A 1 288 ? 9.666   53.644  26.873  1.00 33.84  ? 1140 THR   A O   1 
ATOM   2308 C  CB  . THR   A 1 288 ? 12.583  54.856  27.977  1.00 32.57  ? 1140 THR   A CB  1 
ATOM   2309 O  OG1 . THR   A 1 288 ? 12.426  56.250  28.251  1.00 33.92  ? 1140 THR   A OG1 1 
ATOM   2310 C  CG2 . THR   A 1 288 ? 12.783  54.627  26.489  1.00 33.98  ? 1140 THR   A CG2 1 
ATOM   2311 N  N   . SER   A 1 289 ? 9.486   55.545  28.059  1.00 33.45  ? 1141 SER   A N   1 
ATOM   2312 C  CA  . SER   A 1 289 ? 8.365   56.084  27.278  1.00 33.39  ? 1141 SER   A CA  1 
ATOM   2313 C  C   . SER   A 1 289 ? 8.876   56.959  26.122  1.00 26.88  ? 1141 SER   A C   1 
ATOM   2314 O  O   . SER   A 1 289 ? 10.038  57.375  26.115  1.00 30.06  ? 1141 SER   A O   1 
ATOM   2315 C  CB  . SER   A 1 289 ? 7.484   56.934  28.181  1.00 34.34  ? 1141 SER   A CB  1 
ATOM   2316 O  OG  . SER   A 1 289 ? 8.202   58.067  28.645  1.00 30.08  ? 1141 SER   A OG  1 
ATOM   2317 N  N   . PHE   A 1 290 ? 7.993   57.295  25.193  1.00 27.18  ? 1142 PHE   A N   1 
ATOM   2318 C  CA  . PHE   A 1 290 ? 8.338   58.302  24.168  1.00 20.79  ? 1142 PHE   A CA  1 
ATOM   2319 C  C   . PHE   A 1 290 ? 8.620   59.678  24.801  1.00 25.86  ? 1142 PHE   A C   1 
ATOM   2320 O  O   . PHE   A 1 290 ? 9.591   60.345  24.428  1.00 22.52  ? 1142 PHE   A O   1 
ATOM   2321 C  CB  . PHE   A 1 290 ? 7.288   58.380  23.063  1.00 24.97  ? 1142 PHE   A CB  1 
ATOM   2322 C  CG  . PHE   A 1 290 ? 7.419   57.290  22.038  1.00 20.78  ? 1142 PHE   A CG  1 
ATOM   2323 C  CD1 . PHE   A 1 290 ? 8.577   57.202  21.256  1.00 22.71  ? 1142 PHE   A CD1 1 
ATOM   2324 C  CD2 . PHE   A 1 290 ? 6.419   56.337  21.862  1.00 22.26  ? 1142 PHE   A CD2 1 
ATOM   2325 C  CE1 . PHE   A 1 290 ? 8.729   56.214  20.305  1.00 18.14  ? 1142 PHE   A CE1 1 
ATOM   2326 C  CE2 . PHE   A 1 290 ? 6.566   55.314  20.912  1.00 24.02  ? 1142 PHE   A CE2 1 
ATOM   2327 C  CZ  . PHE   A 1 290 ? 7.725   55.259  20.128  1.00 23.46  ? 1142 PHE   A CZ  1 
ATOM   2328 N  N   . GLN   A 1 291 ? 7.829   60.075  25.797  1.00 27.30  ? 1143 GLN   A N   1 
ATOM   2329 C  CA  . GLN   A 1 291 ? 8.057   61.371  26.457  1.00 27.02  ? 1143 GLN   A CA  1 
ATOM   2330 C  C   . GLN   A 1 291 ? 9.401   61.447  27.203  1.00 27.52  ? 1143 GLN   A C   1 
ATOM   2331 O  O   . GLN   A 1 291 ? 10.082  62.464  27.119  1.00 26.19  ? 1143 GLN   A O   1 
ATOM   2332 C  CB  . GLN   A 1 291 ? 6.873   61.778  27.329  1.00 31.66  ? 1143 GLN   A CB  1 
ATOM   2333 C  CG  . GLN   A 1 291 ? 5.711   62.305  26.490  1.00 31.07  ? 1143 GLN   A CG  1 
ATOM   2334 C  CD  . GLN   A 1 291 ? 4.426   62.478  27.268  1.00 38.26  ? 1143 GLN   A CD  1 
ATOM   2335 O  OE1 . GLN   A 1 291 ? 4.380   62.268  28.487  1.00 41.08  ? 1143 GLN   A OE1 1 
ATOM   2336 N  NE2 . GLN   A 1 291 ? 3.369   62.880  26.567  1.00 34.81  ? 1143 GLN   A NE2 1 
ATOM   2337 N  N   . ASN   A 1 292 ? 9.805   60.365  27.872  1.00 29.67  ? 1144 ASN   A N   1 
ATOM   2338 C  CA  . ASN   A 1 292 ? 11.108  60.339  28.564  1.00 32.67  ? 1144 ASN   A CA  1 
ATOM   2339 C  C   . ASN   A 1 292 ? 12.288  60.351  27.577  1.00 27.99  ? 1144 ASN   A C   1 
ATOM   2340 O  O   . ASN   A 1 292 ? 13.317  61.000  27.828  1.00 25.65  ? 1144 ASN   A O   1 
ATOM   2341 C  CB  . ASN   A 1 292 ? 11.203  59.164  29.558  1.00 35.20  ? 1144 ASN   A CB  1 
ATOM   2342 C  CG  . ASN   A 1 292 ? 10.226  59.291  30.730  1.00 47.89  ? 1144 ASN   A CG  1 
ATOM   2343 O  OD1 . ASN   A 1 292 ? 9.718   60.382  31.047  1.00 52.35  ? 1144 ASN   A OD1 1 
ATOM   2344 N  ND2 . ASN   A 1 292 ? 9.964   58.162  31.388  1.00 53.63  ? 1144 ASN   A ND2 1 
ATOM   2345 N  N   . LEU   A 1 293 ? 12.119  59.689  26.431  1.00 27.66  ? 1145 LEU   A N   1 
ATOM   2346 C  CA  . LEU   A 1 293 ? 13.084  59.816  25.331  1.00 26.07  ? 1145 LEU   A CA  1 
ATOM   2347 C  C   . LEU   A 1 293 ? 13.212  61.260  24.866  1.00 23.76  ? 1145 LEU   A C   1 
ATOM   2348 O  O   . LEU   A 1 293 ? 14.326  61.751  24.666  1.00 21.62  ? 1145 LEU   A O   1 
ATOM   2349 C  CB  . LEU   A 1 293 ? 12.695  58.920  24.154  1.00 26.79  ? 1145 LEU   A CB  1 
ATOM   2350 C  CG  . LEU   A 1 293 ? 12.918  57.426  24.381  1.00 25.24  ? 1145 LEU   A CG  1 
ATOM   2351 C  CD1 . LEU   A 1 293 ? 12.088  56.631  23.375  1.00 21.44  ? 1145 LEU   A CD1 1 
ATOM   2352 C  CD2 . LEU   A 1 293 ? 14.418  57.085  24.268  1.00 23.18  ? 1145 LEU   A CD2 1 
ATOM   2353 N  N   . ILE   A 1 294 ? 12.081  61.947  24.722  1.00 23.40  ? 1146 ILE   A N   1 
ATOM   2354 C  CA  . ILE   A 1 294 ? 12.098  63.341  24.258  1.00 25.14  ? 1146 ILE   A CA  1 
ATOM   2355 C  C   . ILE   A 1 294 ? 12.907  64.177  25.268  1.00 28.66  ? 1146 ILE   A C   1 
ATOM   2356 O  O   . ILE   A 1 294 ? 13.807  64.921  24.873  1.00 28.77  ? 1146 ILE   A O   1 
ATOM   2357 C  CB  . ILE   A 1 294 ? 10.647  63.898  24.035  1.00 24.51  ? 1146 ILE   A CB  1 
ATOM   2358 C  CG1 . ILE   A 1 294 ? 9.989   63.202  22.838  1.00 19.58  ? 1146 ILE   A CG1 1 
ATOM   2359 C  CG2 . ILE   A 1 294 ? 10.664  65.410  23.789  1.00 28.11  ? 1146 ILE   A CG2 1 
ATOM   2360 C  CD1 . ILE   A 1 294 ? 8.479   63.267  22.813  1.00 19.87  ? 1146 ILE   A CD1 1 
ATOM   2361 N  N   . GLU   A 1 295 ? 12.603  64.016  26.559  1.00 30.78  ? 1147 GLU   A N   1 
ATOM   2362 C  CA  . GLU   A 1 295 ? 13.352  64.683  27.640  1.00 30.16  ? 1147 GLU   A CA  1 
ATOM   2363 C  C   . GLU   A 1 295 ? 14.849  64.353  27.592  1.00 26.09  ? 1147 GLU   A C   1 
ATOM   2364 O  O   . GLU   A 1 295 ? 15.683  65.247  27.712  1.00 24.30  ? 1147 GLU   A O   1 
ATOM   2365 C  CB  . GLU   A 1 295 ? 12.782  64.320  29.022  1.00 33.54  ? 1147 GLU   A CB  1 
ATOM   2366 C  CG  . GLU   A 1 295 ? 11.424  64.944  29.300  1.00 35.64  ? 1147 GLU   A CG  1 
ATOM   2367 C  CD  . GLU   A 1 295 ? 11.047  64.953  30.772  0.00 37.98  ? 1147 GLU   A CD  1 
ATOM   2368 O  OE1 . GLU   A 1 295 ? 11.427  64.009  31.498  0.00 38.34  ? 1147 GLU   A OE1 1 
ATOM   2369 O  OE2 . GLU   A 1 295 ? 10.364  65.905  31.204  0.00 39.41  ? 1147 GLU   A OE2 1 
ATOM   2370 N  N   . GLY   A 1 296 ? 15.159  63.076  27.357  1.00 25.95  ? 1148 GLY   A N   1 
ATOM   2371 C  CA  . GLY   A 1 296 ? 16.534  62.593  27.233  1.00 25.68  ? 1148 GLY   A CA  1 
ATOM   2372 C  C   . GLY   A 1 296 ? 17.304  63.218  26.079  1.00 21.28  ? 1148 GLY   A C   1 
ATOM   2373 O  O   . GLY   A 1 296 ? 18.428  63.697  26.274  1.00 21.68  ? 1148 GLY   A O   1 
ATOM   2374 N  N   . PHE   A 1 297 ? 16.701  63.242  24.894  1.00 23.37  ? 1149 PHE   A N   1 
ATOM   2375 C  CA  . PHE   A 1 297 ? 17.354  63.884  23.735  1.00 22.14  ? 1149 PHE   A CA  1 
ATOM   2376 C  C   . PHE   A 1 297 ? 17.499  65.380  23.941  1.00 22.31  ? 1149 PHE   A C   1 
ATOM   2377 O  O   . PHE   A 1 297 ? 18.570  65.940  23.703  1.00 24.62  ? 1149 PHE   A O   1 
ATOM   2378 C  CB  . PHE   A 1 297 ? 16.617  63.629  22.435  1.00 21.32  ? 1149 PHE   A CB  1 
ATOM   2379 C  CG  . PHE   A 1 297 ? 16.549  62.192  22.054  1.00 18.99  ? 1149 PHE   A CG  1 
ATOM   2380 C  CD1 . PHE   A 1 297 ? 17.710  61.431  21.932  1.00 22.00  ? 1149 PHE   A CD1 1 
ATOM   2381 C  CD2 . PHE   A 1 297 ? 15.320  61.587  21.775  1.00 20.49  ? 1149 PHE   A CD2 1 
ATOM   2382 C  CE1 . PHE   A 1 297 ? 17.640  60.079  21.562  1.00 22.00  ? 1149 PHE   A CE1 1 
ATOM   2383 C  CE2 . PHE   A 1 297 ? 15.246  60.233  21.426  1.00 19.42  ? 1149 PHE   A CE2 1 
ATOM   2384 C  CZ  . PHE   A 1 297 ? 16.417  59.490  21.308  1.00 21.96  ? 1149 PHE   A CZ  1 
ATOM   2385 N  N   . GLU   A 1 298 ? 16.433  66.017  24.421  1.00 25.66  ? 1150 GLU   A N   1 
ATOM   2386 C  CA  . GLU   A 1 298 ? 16.460  67.448  24.702  1.00 30.07  ? 1150 GLU   A CA  1 
ATOM   2387 C  C   . GLU   A 1 298 ? 17.608  67.812  25.637  1.00 32.30  ? 1150 GLU   A C   1 
ATOM   2388 O  O   . GLU   A 1 298 ? 18.320  68.797  25.389  1.00 31.25  ? 1150 GLU   A O   1 
ATOM   2389 C  CB  . GLU   A 1 298 ? 15.121  67.907  25.269  1.00 33.15  ? 1150 GLU   A CB  1 
ATOM   2390 C  CG  . GLU   A 1 298 ? 14.065  68.035  24.196  1.00 32.11  ? 1150 GLU   A CG  1 
ATOM   2391 C  CD  . GLU   A 1 298 ? 12.683  68.421  24.734  1.00 42.00  ? 1150 GLU   A CD  1 
ATOM   2392 O  OE1 . GLU   A 1 298 ? 12.478  68.436  25.968  1.00 45.25  ? 1150 GLU   A OE1 1 
ATOM   2393 O  OE2 . GLU   A 1 298 ? 11.790  68.707  23.905  1.00 46.96  ? 1150 GLU   A OE2 1 
ATOM   2394 N  N   . ALA   A 1 299 ? 17.805  67.012  26.690  1.00 32.42  ? 1151 ALA   A N   1 
ATOM   2395 C  CA  . ALA   A 1 299 ? 18.907  67.229  27.623  1.00 33.17  ? 1151 ALA   A CA  1 
ATOM   2396 C  C   . ALA   A 1 299 ? 20.276  67.174  26.928  1.00 32.46  ? 1151 ALA   A C   1 
ATOM   2397 O  O   . ALA   A 1 299 ? 21.167  67.978  27.228  1.00 30.32  ? 1151 ALA   A O   1 
ATOM   2398 C  CB  . ALA   A 1 299 ? 18.846  66.224  28.803  1.00 32.68  ? 1151 ALA   A CB  1 
ATOM   2399 N  N   . LEU   A 1 300 ? 20.438  66.243  25.992  1.00 29.88  ? 1152 LEU   A N   1 
ATOM   2400 C  CA  . LEU   A 1 300 ? 21.704  66.119  25.254  1.00 31.34  ? 1152 LEU   A CA  1 
ATOM   2401 C  C   . LEU   A 1 300 ? 21.883  67.217  24.194  1.00 31.71  ? 1152 LEU   A C   1 
ATOM   2402 O  O   . LEU   A 1 300 ? 23.013  67.547  23.835  1.00 34.18  ? 1152 LEU   A O   1 
ATOM   2403 C  CB  . LEU   A 1 300 ? 21.818  64.739  24.606  1.00 31.06  ? 1152 LEU   A CB  1 
ATOM   2404 C  CG  . LEU   A 1 300 ? 21.870  63.555  25.576  1.00 34.43  ? 1152 LEU   A CG  1 
ATOM   2405 C  CD1 . LEU   A 1 300 ? 21.869  62.270  24.771  1.00 33.76  ? 1152 LEU   A CD1 1 
ATOM   2406 C  CD2 . LEU   A 1 300 ? 23.067  63.606  26.523  1.00 35.46  ? 1152 LEU   A CD2 1 
ATOM   2407 N  N   . LEU   A 1 301 ? 20.774  67.777  23.722  1.00 27.69  ? 1153 LEU   A N   1 
ATOM   2408 C  CA  . LEU   A 1 301 ? 20.799  68.907  22.786  1.00 30.53  ? 1153 LEU   A CA  1 
ATOM   2409 C  C   . LEU   A 1 301 ? 21.096  70.271  23.414  1.00 36.18  ? 1153 LEU   A C   1 
ATOM   2410 O  O   . LEU   A 1 301 ? 21.744  71.093  22.774  1.00 36.24  ? 1153 LEU   A O   1 
ATOM   2411 C  CB  . LEU   A 1 301 ? 19.466  68.991  22.044  1.00 27.81  ? 1153 LEU   A CB  1 
ATOM   2412 C  CG  . LEU   A 1 301 ? 19.220  67.936  20.959  1.00 25.36  ? 1153 LEU   A CG  1 
ATOM   2413 C  CD1 . LEU   A 1 301 ? 17.778  68.012  20.509  1.00 26.11  ? 1153 LEU   A CD1 1 
ATOM   2414 C  CD2 . LEU   A 1 301 ? 20.151  68.126  19.781  1.00 27.30  ? 1153 LEU   A CD2 1 
ATOM   2415 N  N   . LYS   A 1 302 ? 20.568  70.516  24.620  1.00 42.56  ? 1154 LYS   A N   1 
ATOM   2416 C  CA  . LYS   A 1 302 ? 20.614  71.833  25.292  1.00 50.79  ? 1154 LYS   A CA  1 
ATOM   2417 C  C   . LYS   A 1 302 ? 20.875  71.685  26.784  1.00 53.46  ? 1154 LYS   A C   1 
ATOM   2418 O  O   . LYS   A 1 302 ? 20.424  70.729  27.418  1.00 53.52  ? 1154 LYS   A O   1 
ATOM   2419 C  CB  . LYS   A 1 302 ? 19.284  72.605  25.147  1.00 53.49  ? 1154 LYS   A CB  1 
ATOM   2420 C  CG  . LYS   A 1 302 ? 18.594  72.557  23.775  1.00 54.32  ? 1154 LYS   A CG  1 
ATOM   2421 C  CD  . LYS   A 1 302 ? 17.469  71.516  23.723  1.00 50.19  ? 1154 LYS   A CD  1 
ATOM   2422 C  CE  . LYS   A 1 302 ? 16.732  71.574  22.382  1.00 53.52  ? 1154 LYS   A CE  1 
ATOM   2423 N  NZ  . LYS   A 1 302 ? 15.406  70.886  22.393  1.00 48.40  ? 1154 LYS   A NZ  1 
ATOM   2424 O  OXT . LYS   A 1 302 ? 21.495  72.553  27.396  1.00 58.93  ? 1154 LYS   A OXT 1 
ATOM   2425 N  N   . VAL   B 1 13  ? 39.732  -9.314  -4.417  1.00 57.68  ? 865  VAL   B N   1 
ATOM   2426 C  CA  . VAL   B 1 13  ? 38.243  -9.187  -4.586  1.00 54.81  ? 865  VAL   B CA  1 
ATOM   2427 C  C   . VAL   B 1 13  ? 37.567  -8.737  -3.283  1.00 51.26  ? 865  VAL   B C   1 
ATOM   2428 O  O   . VAL   B 1 13  ? 37.428  -9.525  -2.347  1.00 53.59  ? 865  VAL   B O   1 
ATOM   2429 C  CB  . VAL   B 1 13  ? 37.591  -10.514 -5.071  1.00 57.13  ? 865  VAL   B CB  1 
ATOM   2430 C  CG1 . VAL   B 1 13  ? 37.835  -10.672 -6.602  0.00 58.71  ? 865  VAL   B CG1 1 
ATOM   2431 C  CG2 . VAL   B 1 13  ? 38.111  -11.777 -4.359  0.00 60.17  ? 865  VAL   B CG2 1 
ATOM   2432 N  N   . ASP   B 1 14  ? 37.173  -7.464  -3.230  1.00 45.29  ? 866  ASP   B N   1 
ATOM   2433 C  CA  . ASP   B 1 14  ? 36.474  -6.905  -2.068  1.00 41.41  ? 866  ASP   B CA  1 
ATOM   2434 C  C   . ASP   B 1 14  ? 34.983  -6.891  -2.400  1.00 37.83  ? 866  ASP   B C   1 
ATOM   2435 O  O   . ASP   B 1 14  ? 34.582  -6.124  -3.286  1.00 34.36  ? 866  ASP   B O   1 
ATOM   2436 C  CB  . ASP   B 1 14  ? 36.966  -5.479  -1.769  1.00 40.28  ? 866  ASP   B CB  1 
ATOM   2437 C  CG  . ASP   B 1 14  ? 36.340  -4.874  -0.497  1.00 39.32  ? 866  ASP   B CG  1 
ATOM   2438 O  OD1 . ASP   B 1 14  ? 35.359  -5.424  0.059   1.00 35.90  ? 866  ASP   B OD1 1 
ATOM   2439 O  OD2 . ASP   B 1 14  ? 36.837  -3.824  -0.053  1.00 41.75  ? 866  ASP   B OD2 1 
ATOM   2440 N  N   . PRO   B 1 15  ? 34.163  -7.675  -1.660  1.00 39.39  ? 867  PRO   B N   1 
ATOM   2441 C  CA  . PRO   B 1 15  ? 32.731  -7.756  -1.963  1.00 37.20  ? 867  PRO   B CA  1 
ATOM   2442 C  C   . PRO   B 1 15  ? 31.945  -6.489  -1.622  1.00 33.49  ? 867  PRO   B C   1 
ATOM   2443 O  O   . PRO   B 1 15  ? 30.764  -6.369  -2.003  1.00 31.63  ? 867  PRO   B O   1 
ATOM   2444 C  CB  . PRO   B 1 15  ? 32.256  -8.934  -1.101  1.00 39.96  ? 867  PRO   B CB  1 
ATOM   2445 C  CG  . PRO   B 1 15  ? 33.208  -8.987  0.029   1.00 39.02  ? 867  PRO   B CG  1 
ATOM   2446 C  CD  . PRO   B 1 15  ? 34.514  -8.490  -0.478  1.00 41.36  ? 867  PRO   B CD  1 
ATOM   2447 N  N   . THR   B 1 16  ? 32.585  -5.573  -0.885  1.00 28.76  ? 868  THR   B N   1 
ATOM   2448 C  CA  . THR   B 1 16  ? 32.039  -4.263  -0.595  1.00 24.50  ? 868  THR   B CA  1 
ATOM   2449 C  C   . THR   B 1 16  ? 32.507  -3.164  -1.553  1.00 22.40  ? 868  THR   B C   1 
ATOM   2450 O  O   . THR   B 1 16  ? 32.167  -2.011  -1.349  1.00 18.23  ? 868  THR   B O   1 
ATOM   2451 C  CB  . THR   B 1 16  ? 32.358  -3.829  0.864   1.00 25.93  ? 868  THR   B CB  1 
ATOM   2452 O  OG1 . THR   B 1 16  ? 33.743  -3.483  0.987   1.00 23.27  ? 868  THR   B OG1 1 
ATOM   2453 C  CG2 . THR   B 1 16  ? 31.996  -4.932  1.863   1.00 27.52  ? 868  THR   B CG2 1 
ATOM   2454 N  N   . HIS   B 1 17  ? 33.268  -3.519  -2.587  1.00 23.99  ? 869  HIS   B N   1 
ATOM   2455 C  CA  . HIS   B 1 17  ? 33.737  -2.576  -3.593  1.00 24.23  ? 869  HIS   B CA  1 
ATOM   2456 C  C   . HIS   B 1 17  ? 32.918  -2.818  -4.863  1.00 25.88  ? 869  HIS   B C   1 
ATOM   2457 O  O   . HIS   B 1 17  ? 33.011  -3.896  -5.461  1.00 27.58  ? 869  HIS   B O   1 
ATOM   2458 C  CB  . HIS   B 1 17  ? 35.232  -2.780  -3.876  1.00 29.10  ? 869  HIS   B CB  1 
ATOM   2459 C  CG  . HIS   B 1 17  ? 35.756  -1.948  -5.010  1.00 37.58  ? 869  HIS   B CG  1 
ATOM   2460 N  ND1 . HIS   B 1 17  ? 36.100  -2.484  -6.233  1.00 52.36  ? 869  HIS   B ND1 1 
ATOM   2461 C  CD2 . HIS   B 1 17  ? 35.981  -0.616  -5.108  1.00 45.38  ? 869  HIS   B CD2 1 
ATOM   2462 C  CE1 . HIS   B 1 17  ? 36.522  -1.520  -7.033  1.00 53.36  ? 869  HIS   B CE1 1 
ATOM   2463 N  NE2 . HIS   B 1 17  ? 36.457  -0.376  -6.375  1.00 53.91  ? 869  HIS   B NE2 1 
ATOM   2464 N  N   . PHE   B 1 18  ? 32.124  -1.813  -5.237  1.00 21.41  ? 870  PHE   B N   1 
ATOM   2465 C  CA  . PHE   B 1 18  ? 31.252  -1.844  -6.404  1.00 23.13  ? 870  PHE   B CA  1 
ATOM   2466 C  C   . PHE   B 1 18  ? 31.872  -0.985  -7.495  1.00 25.06  ? 870  PHE   B C   1 
ATOM   2467 O  O   . PHE   B 1 18  ? 32.103  0.204   -7.307  1.00 23.89  ? 870  PHE   B O   1 
ATOM   2468 C  CB  . PHE   B 1 18  ? 29.848  -1.346  -6.013  1.00 20.87  ? 870  PHE   B CB  1 
ATOM   2469 C  CG  . PHE   B 1 18  ? 29.078  -2.336  -5.179  1.00 20.81  ? 870  PHE   B CG  1 
ATOM   2470 C  CD1 . PHE   B 1 18  ? 29.277  -2.416  -3.816  1.00 16.62  ? 870  PHE   B CD1 1 
ATOM   2471 C  CD2 . PHE   B 1 18  ? 28.139  -3.185  -5.766  1.00 24.07  ? 870  PHE   B CD2 1 
ATOM   2472 C  CE1 . PHE   B 1 18  ? 28.594  -3.362  -3.047  1.00 23.18  ? 870  PHE   B CE1 1 
ATOM   2473 C  CE2 . PHE   B 1 18  ? 27.433  -4.115  -5.007  1.00 22.59  ? 870  PHE   B CE2 1 
ATOM   2474 C  CZ  . PHE   B 1 18  ? 27.682  -4.205  -3.639  1.00 18.47  ? 870  PHE   B CZ  1 
ATOM   2475 N  N   . GLU   B 1 19  ? 32.164  -1.596  -8.636  1.00 26.49  ? 871  GLU   B N   1 
ATOM   2476 C  CA  . GLU   B 1 19  ? 32.800  -0.887  -9.742  1.00 30.12  ? 871  GLU   B CA  1 
ATOM   2477 C  C   . GLU   B 1 19  ? 31.746  -0.059  -10.481 1.00 29.63  ? 871  GLU   B C   1 
ATOM   2478 O  O   . GLU   B 1 19  ? 30.650  -0.551  -10.778 1.00 27.91  ? 871  GLU   B O   1 
ATOM   2479 C  CB  . GLU   B 1 19  ? 33.492  -1.885  -10.665 1.00 33.74  ? 871  GLU   B CB  1 
ATOM   2480 C  CG  . GLU   B 1 19  ? 34.656  -2.560  -9.954  1.00 37.96  ? 871  GLU   B CG  1 
ATOM   2481 C  CD  . GLU   B 1 19  ? 35.340  -3.634  -10.764 1.00 49.96  ? 871  GLU   B CD  1 
ATOM   2482 O  OE1 . GLU   B 1 19  ? 35.067  -3.754  -11.978 1.00 54.64  ? 871  GLU   B OE1 1 
ATOM   2483 O  OE2 . GLU   B 1 19  ? 36.158  -4.367  -10.164 1.00 50.40  ? 871  GLU   B OE2 1 
ATOM   2484 N  N   . LYS   B 1 20  ? 32.069  1.207   -10.760 1.00 27.44  ? 872  LYS   B N   1 
ATOM   2485 C  CA  . LYS   B 1 20  ? 31.136  2.109   -11.439 1.00 27.10  ? 872  LYS   B CA  1 
ATOM   2486 C  C   . LYS   B 1 20  ? 30.660  1.550   -12.774 1.00 27.14  ? 872  LYS   B C   1 
ATOM   2487 O  O   . LYS   B 1 20  ? 29.493  1.714   -13.131 1.00 23.19  ? 872  LYS   B O   1 
ATOM   2488 C  CB  . LYS   B 1 20  ? 31.773  3.491   -11.664 1.00 29.16  ? 872  LYS   B CB  1 
ATOM   2489 C  CG  . LYS   B 1 20  ? 30.795  4.558   -12.152 1.00 36.77  ? 872  LYS   B CG  1 
ATOM   2490 C  CD  . LYS   B 1 20  ? 31.496  5.885   -12.410 1.00 45.82  ? 872  LYS   B CD  1 
ATOM   2491 C  CE  . LYS   B 1 20  ? 30.525  6.937   -12.956 1.00 50.38  ? 872  LYS   B CE  1 
ATOM   2492 N  NZ  . LYS   B 1 20  ? 31.247  8.122   -13.513 1.00 58.59  ? 872  LYS   B NZ  1 
ATOM   2493 N  N   . ARG   B 1 21  ? 31.567  0.898   -13.499 1.00 29.43  ? 873  ARG   B N   1 
ATOM   2494 C  CA  . ARG   B 1 21  ? 31.255  0.380   -14.841 1.00 32.65  ? 873  ARG   B CA  1 
ATOM   2495 C  C   . ARG   B 1 21  ? 30.129  -0.652  -14.871 1.00 30.81  ? 873  ARG   B C   1 
ATOM   2496 O  O   . ARG   B 1 21  ? 29.531  -0.858  -15.924 1.00 33.01  ? 873  ARG   B O   1 
ATOM   2497 C  CB  . ARG   B 1 21  ? 32.498  -0.192  -15.521 1.00 35.75  ? 873  ARG   B CB  1 
ATOM   2498 C  CG  . ARG   B 1 21  ? 33.100  -1.428  -14.880 1.00 36.83  ? 873  ARG   B CG  1 
ATOM   2499 C  CD  . ARG   B 1 21  ? 34.288  -1.948  -15.685 1.00 41.61  ? 873  ARG   B CD  1 
ATOM   2500 N  NE  . ARG   B 1 21  ? 35.126  -2.818  -14.860 1.00 47.40  ? 873  ARG   B NE  1 
ATOM   2501 C  CZ  . ARG   B 1 21  ? 35.853  -3.852  -15.293 1.00 56.98  ? 873  ARG   B CZ  1 
ATOM   2502 N  NH1 . ARG   B 1 21  ? 35.891  -4.204  -16.584 1.00 63.56  ? 873  ARG   B NH1 1 
ATOM   2503 N  NH2 . ARG   B 1 21  ? 36.567  -4.557  -14.413 1.00 61.43  ? 873  ARG   B NH2 1 
ATOM   2504 N  N   . PHE   B 1 22  ? 29.870  -1.320  -13.745 1.00 26.43  ? 874  PHE   B N   1 
ATOM   2505 C  CA  . PHE   B 1 22  ? 28.804  -2.327  -13.653 1.00 26.05  ? 874  PHE   B CA  1 
ATOM   2506 C  C   . PHE   B 1 22  ? 27.583  -1.855  -12.878 1.00 27.30  ? 874  PHE   B C   1 
ATOM   2507 O  O   . PHE   B 1 22  ? 26.615  -2.606  -12.736 1.00 25.66  ? 874  PHE   B O   1 
ATOM   2508 C  CB  . PHE   B 1 22  ? 29.342  -3.615  -13.021 1.00 27.67  ? 874  PHE   B CB  1 
ATOM   2509 C  CG  . PHE   B 1 22  ? 30.549  -4.202  -13.708 1.00 29.68  ? 874  PHE   B CG  1 
ATOM   2510 C  CD1 . PHE   B 1 22  ? 30.597  -4.348  -15.096 1.00 32.94  ? 874  PHE   B CD1 1 
ATOM   2511 C  CD2 . PHE   B 1 22  ? 31.626  -4.677  -12.950 1.00 35.01  ? 874  PHE   B CD2 1 
ATOM   2512 C  CE1 . PHE   B 1 22  ? 31.703  -4.922  -15.710 1.00 39.72  ? 874  PHE   B CE1 1 
ATOM   2513 C  CE2 . PHE   B 1 22  ? 32.735  -5.246  -13.560 1.00 38.10  ? 874  PHE   B CE2 1 
ATOM   2514 C  CZ  . PHE   B 1 22  ? 32.782  -5.364  -14.938 1.00 43.50  ? 874  PHE   B CZ  1 
ATOM   2515 N  N   . LEU   B 1 23  ? 27.616  -0.613  -12.379 1.00 26.81  ? 875  LEU   B N   1 
ATOM   2516 C  CA  . LEU   B 1 23  ? 26.541  -0.079  -11.531 1.00 26.71  ? 875  LEU   B CA  1 
ATOM   2517 C  C   . LEU   B 1 23  ? 25.610  0.721   -12.438 1.00 28.58  ? 875  LEU   B C   1 
ATOM   2518 O  O   . LEU   B 1 23  ? 25.932  1.844   -12.863 1.00 27.55  ? 875  LEU   B O   1 
ATOM   2519 C  CB  . LEU   B 1 23  ? 27.112  0.770   -10.380 1.00 26.61  ? 875  LEU   B CB  1 
ATOM   2520 C  CG  . LEU   B 1 23  ? 26.177  1.206   -9.235  1.00 25.16  ? 875  LEU   B CG  1 
ATOM   2521 C  CD1 . LEU   B 1 23  ? 25.584  0.015   -8.507  1.00 19.88  ? 875  LEU   B CD1 1 
ATOM   2522 C  CD2 . LEU   B 1 23  ? 26.913  2.103   -8.225  1.00 29.05  ? 875  LEU   B CD2 1 
ATOM   2523 N  N   . LYS   B 1 24  ? 24.480  0.108   -12.770 1.00 24.27  ? 876  LYS   B N   1 
ATOM   2524 C  CA  . LYS   B 1 24  ? 23.597  0.606   -13.790 1.00 29.97  ? 876  LYS   B CA  1 
ATOM   2525 C  C   . LYS   B 1 24  ? 22.373  1.195   -13.130 1.00 26.86  ? 876  LYS   B C   1 
ATOM   2526 O  O   . LYS   B 1 24  ? 21.641  0.488   -12.446 1.00 21.82  ? 876  LYS   B O   1 
ATOM   2527 C  CB  . LYS   B 1 24  ? 23.203  -0.534  -14.739 1.00 31.37  ? 876  LYS   B CB  1 
ATOM   2528 C  CG  . LYS   B 1 24  ? 24.399  -1.265  -15.360 1.00 42.11  ? 876  LYS   B CG  1 
ATOM   2529 C  CD  . LYS   B 1 24  ? 25.326  -0.318  -16.134 1.00 46.56  ? 876  LYS   B CD  1 
ATOM   2530 C  CE  . LYS   B 1 24  ? 26.432  -1.052  -16.857 1.00 49.36  ? 876  LYS   B CE  1 
ATOM   2531 N  NZ  . LYS   B 1 24  ? 27.327  -0.078  -17.530 1.00 54.30  ? 876  LYS   B NZ  1 
ATOM   2532 N  N   . ARG   B 1 25  ? 22.169  2.490   -13.362 1.00 25.27  ? 877  ARG   B N   1 
ATOM   2533 C  CA  . ARG   B 1 25  ? 21.040  3.241   -12.821 1.00 25.90  ? 877  ARG   B CA  1 
ATOM   2534 C  C   . ARG   B 1 25  ? 19.707  2.847   -13.449 1.00 24.16  ? 877  ARG   B C   1 
ATOM   2535 O  O   . ARG   B 1 25  ? 19.572  2.892   -14.692 1.00 24.40  ? 877  ARG   B O   1 
ATOM   2536 C  CB  . ARG   B 1 25  ? 21.255  4.737   -13.077 1.00 25.30  ? 877  ARG   B CB  1 
ATOM   2537 C  CG  . ARG   B 1 25  ? 20.082  5.572   -12.600 1.00 29.59  ? 877  ARG   B CG  1 
ATOM   2538 C  CD  . ARG   B 1 25  ? 20.260  7.056   -12.780 1.00 31.61  ? 877  ARG   B CD  1 
ATOM   2539 N  NE  . ARG   B 1 25  ? 19.020  7.731   -12.374 1.00 35.21  ? 877  ARG   B NE  1 
ATOM   2540 C  CZ  . ARG   B 1 25  ? 17.901  7.800   -13.096 1.00 38.97  ? 877  ARG   B CZ  1 
ATOM   2541 N  NH1 . ARG   B 1 25  ? 17.810  7.248   -14.297 1.00 39.23  ? 877  ARG   B NH1 1 
ATOM   2542 N  NH2 . ARG   B 1 25  ? 16.846  8.434   -12.609 1.00 43.36  ? 877  ARG   B NH2 1 
ATOM   2543 N  N   . ILE   B 1 26  ? 18.712  2.532   -12.612 1.00 21.03  ? 878  ILE   B N   1 
ATOM   2544 C  CA  . ILE   B 1 26  ? 17.347  2.227   -13.093 1.00 23.92  ? 878  ILE   B CA  1 
ATOM   2545 C  C   . ILE   B 1 26  ? 16.398  3.408   -12.919 1.00 25.29  ? 878  ILE   B C   1 
ATOM   2546 O  O   . ILE   B 1 26  ? 15.857  3.902   -13.902 1.00 30.90  ? 878  ILE   B O   1 
ATOM   2547 C  CB  . ILE   B 1 26  ? 16.728  0.963   -12.450 1.00 24.61  ? 878  ILE   B CB  1 
ATOM   2548 C  CG1 . ILE   B 1 26  ? 17.643  -0.249  -12.674 1.00 27.76  ? 878  ILE   B CG1 1 
ATOM   2549 C  CG2 . ILE   B 1 26  ? 15.310  0.685   -13.055 1.00 26.65  ? 878  ILE   B CG2 1 
ATOM   2550 C  CD1 . ILE   B 1 26  ? 17.220  -1.521  -11.960 1.00 35.00  ? 878  ILE   B CD1 1 
ATOM   2551 N  N   . ARG   B 1 27  ? 16.170  3.833   -11.670 1.00 20.52  ? 879  ARG   B N   1 
ATOM   2552 C  CA  . ARG   B 1 27  ? 15.276  4.970   -11.401 1.00 24.33  ? 879  ARG   B CA  1 
ATOM   2553 C  C   . ARG   B 1 27  ? 15.530  5.599   -10.039 1.00 20.60  ? 879  ARG   B C   1 
ATOM   2554 O  O   . ARG   B 1 27  ? 16.216  5.017   -9.214  1.00 18.19  ? 879  ARG   B O   1 
ATOM   2555 C  CB  . ARG   B 1 27  ? 13.817  4.532   -11.485 1.00 29.40  ? 879  ARG   B CB  1 
ATOM   2556 C  CG  . ARG   B 1 27  ? 13.438  3.402   -10.538 1.00 29.37  ? 879  ARG   B CG  1 
ATOM   2557 C  CD  . ARG   B 1 27  ? 11.979  2.957   -10.704 1.00 36.91  ? 879  ARG   B CD  1 
ATOM   2558 N  NE  . ARG   B 1 27  ? 11.700  1.860   -9.778  1.00 31.59  ? 879  ARG   B NE  1 
ATOM   2559 C  CZ  . ARG   B 1 27  ? 11.193  1.973   -8.542  1.00 37.32  ? 879  ARG   B CZ  1 
ATOM   2560 N  NH1 . ARG   B 1 27  ? 10.830  3.153   -8.021  1.00 30.62  ? 879  ARG   B NH1 1 
ATOM   2561 N  NH2 . ARG   B 1 27  ? 11.024  0.873   -7.812  1.00 45.99  ? 879  ARG   B NH2 1 
ATOM   2562 N  N   . ASP   B 1 28  ? 14.962  6.781   -9.832  1.00 23.56  ? 880  ASP   B N   1 
ATOM   2563 C  CA  . ASP   B 1 28  ? 15.044  7.465   -8.550  1.00 23.97  ? 880  ASP   B CA  1 
ATOM   2564 C  C   . ASP   B 1 28  ? 14.135  6.801   -7.537  1.00 24.24  ? 880  ASP   B C   1 
ATOM   2565 O  O   . ASP   B 1 28  ? 13.031  6.363   -7.860  1.00 26.49  ? 880  ASP   B O   1 
ATOM   2566 C  CB  . ASP   B 1 28  ? 14.604  8.922   -8.659  1.00 28.63  ? 880  ASP   B CB  1 
ATOM   2567 C  CG  . ASP   B 1 28  ? 15.518  9.757   -9.539  1.00 30.61  ? 880  ASP   B CG  1 
ATOM   2568 O  OD1 . ASP   B 1 28  ? 16.633  9.297   -9.864  1.00 28.95  ? 880  ASP   B OD1 1 
ATOM   2569 O  OD2 . ASP   B 1 28  ? 15.120  10.885  -9.876  1.00 37.33  ? 880  ASP   B OD2 1 
ATOM   2570 N  N   . LEU   B 1 29  ? 14.589  6.786   -6.295  1.00 21.10  ? 881  LEU   B N   1 
ATOM   2571 C  CA  . LEU   B 1 29  ? 13.748  6.337   -5.176  1.00 23.04  ? 881  LEU   B CA  1 
ATOM   2572 C  C   . LEU   B 1 29  ? 13.322  7.507   -4.293  1.00 22.28  ? 881  LEU   B C   1 
ATOM   2573 O  O   . LEU   B 1 29  ? 12.208  7.548   -3.776  1.00 23.77  ? 881  LEU   B O   1 
ATOM   2574 C  CB  . LEU   B 1 29  ? 14.500  5.284   -4.384  1.00 18.85  ? 881  LEU   B CB  1 
ATOM   2575 C  CG  . LEU   B 1 29  ? 14.694  3.966   -5.145  1.00 19.59  ? 881  LEU   B CG  1 
ATOM   2576 C  CD1 . LEU   B 1 29  ? 15.608  3.040   -4.361  1.00 21.35  ? 881  LEU   B CD1 1 
ATOM   2577 C  CD2 . LEU   B 1 29  ? 13.394  3.283   -5.432  1.00 17.64  ? 881  LEU   B CD2 1 
ATOM   2578 N  N   . GLY   B 1 30  ? 14.205  8.476   -4.139  1.00 26.26  ? 882  GLY   B N   1 
ATOM   2579 C  CA  . GLY   B 1 30  ? 13.857  9.702   -3.444  1.00 27.88  ? 882  GLY   B CA  1 
ATOM   2580 C  C   . GLY   B 1 30  ? 15.087  10.521  -3.145  1.00 31.13  ? 882  GLY   B C   1 
ATOM   2581 O  O   . GLY   B 1 30  ? 16.202  10.142  -3.517  1.00 27.97  ? 882  GLY   B O   1 
ATOM   2582 N  N   . GLU   B 1 31  ? 14.861  11.648  -2.472  1.00 39.07  ? 883  GLU   B N   1 
ATOM   2583 C  CA  . GLU   B 1 31  ? 15.909  12.619  -2.158  1.00 45.86  ? 883  GLU   B CA  1 
ATOM   2584 C  C   . GLU   B 1 31  ? 15.764  13.162  -0.735  1.00 48.81  ? 883  GLU   B C   1 
ATOM   2585 O  O   . GLU   B 1 31  ? 14.660  13.218  -0.186  1.00 47.42  ? 883  GLU   B O   1 
ATOM   2586 C  CB  . GLU   B 1 31  ? 15.847  13.794  -3.132  1.00 49.16  ? 883  GLU   B CB  1 
ATOM   2587 C  CG  . GLU   B 1 31  ? 15.739  13.404  -4.618  1.00 55.07  ? 883  GLU   B CG  1 
ATOM   2588 C  CD  . GLU   B 1 31  ? 15.663  14.601  -5.547  1.00 58.85  ? 883  GLU   B CD  1 
ATOM   2589 O  OE1 . GLU   B 1 31  ? 15.557  15.740  -5.047  1.00 65.87  ? 883  GLU   B OE1 1 
ATOM   2590 O  OE2 . GLU   B 1 31  ? 15.699  14.401  -6.783  1.00 62.14  ? 883  GLU   B OE2 1 
ATOM   2591 N  N   . GLY   B 1 32  ? 16.893  13.577  -0.160  1.00 51.34  ? 884  GLY   B N   1 
ATOM   2592 C  CA  . GLY   B 1 32  ? 16.912  14.252  1.139   1.00 52.98  ? 884  GLY   B CA  1 
ATOM   2593 C  C   . GLY   B 1 32  ? 18.286  14.810  1.474   1.00 53.60  ? 884  GLY   B C   1 
ATOM   2594 O  O   . GLY   B 1 32  ? 19.302  14.171  1.183   1.00 48.85  ? 884  GLY   B O   1 
ATOM   2595 N  N   . HIS   B 1 33  ? 18.309  16.016  2.049   1.00 57.43  ? 885  HIS   B N   1 
ATOM   2596 C  CA  . HIS   B 1 33  ? 19.516  16.620  2.655   1.00 57.95  ? 885  HIS   B CA  1 
ATOM   2597 C  C   . HIS   B 1 33  ? 20.778  16.543  1.780   1.00 56.14  ? 885  HIS   B C   1 
ATOM   2598 O  O   . HIS   B 1 33  ? 21.795  15.976  2.183   1.00 55.65  ? 885  HIS   B O   1 
ATOM   2599 C  CB  . HIS   B 1 33  ? 19.769  15.995  4.034   1.00 57.28  ? 885  HIS   B CB  1 
ATOM   2600 C  CG  . HIS   B 1 33  ? 18.582  16.167  4.946   0.00 58.12  ? 885  HIS   B CG  1 
ATOM   2601 N  ND1 . HIS   B 1 33  ? 18.216  17.383  5.483   0.00 61.40  ? 885  HIS   B ND1 1 
ATOM   2602 C  CD2 . HIS   B 1 33  ? 17.679  15.267  5.401   0.00 56.59  ? 885  HIS   B CD2 1 
ATOM   2603 C  CE1 . HIS   B 1 33  ? 17.144  17.223  6.237   0.00 61.63  ? 885  HIS   B CE1 1 
ATOM   2604 N  NE2 . HIS   B 1 33  ? 16.799  15.948  6.205   0.00 58.74  ? 885  HIS   B NE2 1 
ATOM   2605 N  N   . PHE   B 1 34  ? 20.672  17.095  0.571   1.00 56.26  ? 886  PHE   B N   1 
ATOM   2606 C  CA  . PHE   B 1 34  ? 21.757  17.103  -0.434  1.00 54.63  ? 886  PHE   B CA  1 
ATOM   2607 C  C   . PHE   B 1 34  ? 22.142  15.712  -0.990  1.00 48.72  ? 886  PHE   B C   1 
ATOM   2608 O  O   . PHE   B 1 34  ? 23.117  15.588  -1.738  1.00 48.33  ? 886  PHE   B O   1 
ATOM   2609 C  CB  . PHE   B 1 34  ? 22.997  17.841  0.105   1.00 57.34  ? 886  PHE   B CB  1 
ATOM   2610 C  CG  . PHE   B 1 34  ? 22.684  19.215  0.645   0.00 61.04  ? 886  PHE   B CG  1 
ATOM   2611 C  CD1 . PHE   B 1 34  ? 22.552  20.311  -0.205  0.00 64.73  ? 886  PHE   B CD1 1 
ATOM   2612 C  CD2 . PHE   B 1 34  ? 22.514  19.405  2.016   0.00 61.39  ? 886  PHE   B CD2 1 
ATOM   2613 C  CE1 . PHE   B 1 34  ? 22.258  21.579  0.303   0.00 68.50  ? 886  PHE   B CE1 1 
ATOM   2614 C  CE2 . PHE   B 1 34  ? 22.219  20.669  2.534   0.00 65.06  ? 886  PHE   B CE2 1 
ATOM   2615 C  CZ  . PHE   B 1 34  ? 22.092  21.758  1.675   0.00 68.69  ? 886  PHE   B CZ  1 
ATOM   2616 N  N   . GLY   B 1 35  ? 21.360  14.691  -0.638  1.00 43.56  ? 887  GLY   B N   1 
ATOM   2617 C  CA  . GLY   B 1 35  ? 21.543  13.327  -1.120  1.00 37.97  ? 887  GLY   B CA  1 
ATOM   2618 C  C   . GLY   B 1 35  ? 20.404  12.953  -2.055  1.00 36.10  ? 887  GLY   B C   1 
ATOM   2619 O  O   . GLY   B 1 35  ? 19.311  13.553  -2.007  1.00 33.34  ? 887  GLY   B O   1 
ATOM   2620 N  N   . LYS   B 1 36  ? 20.670  11.991  -2.939  1.00 28.48  ? 888  LYS   B N   1 
ATOM   2621 C  CA  . LYS   B 1 36  ? 19.595  11.305  -3.659  1.00 28.10  ? 888  LYS   B CA  1 
ATOM   2622 C  C   . LYS   B 1 36  ? 19.843  9.803   -3.624  1.00 21.30  ? 888  LYS   B C   1 
ATOM   2623 O  O   . LYS   B 1 36  ? 20.984  9.377   -3.652  1.00 20.37  ? 888  LYS   B O   1 
ATOM   2624 C  CB  . LYS   B 1 36  ? 19.431  11.845  -5.097  1.00 31.61  ? 888  LYS   B CB  1 
ATOM   2625 C  CG  . LYS   B 1 36  ? 20.515  11.470  -6.116  1.00 37.79  ? 888  LYS   B CG  1 
ATOM   2626 C  CD  . LYS   B 1 36  ? 20.130  11.908  -7.545  1.00 42.63  ? 888  LYS   B CD  1 
ATOM   2627 C  CE  . LYS   B 1 36  ? 18.923  11.123  -8.092  1.00 44.90  ? 888  LYS   B CE  1 
ATOM   2628 N  NZ  . LYS   B 1 36  ? 18.741  11.269  -9.571  1.00 44.92  ? 888  LYS   B NZ  1 
ATOM   2629 N  N   . VAL   B 1 37  ? 18.772  9.020   -3.564  1.00 17.91  ? 889  VAL   B N   1 
ATOM   2630 C  CA  . VAL   B 1 37  ? 18.870  7.571   -3.542  1.00 15.56  ? 889  VAL   B CA  1 
ATOM   2631 C  C   . VAL   B 1 37  ? 18.225  7.021   -4.829  1.00 17.20  ? 889  VAL   B C   1 
ATOM   2632 O  O   . VAL   B 1 37  ? 17.128  7.434   -5.205  1.00 19.49  ? 889  VAL   B O   1 
ATOM   2633 C  CB  . VAL   B 1 37  ? 18.208  6.968   -2.310  1.00 15.32  ? 889  VAL   B CB  1 
ATOM   2634 C  CG1 . VAL   B 1 37  ? 18.320  5.451   -2.334  1.00 19.09  ? 889  VAL   B CG1 1 
ATOM   2635 C  CG2 . VAL   B 1 37  ? 18.856  7.531   -1.050  1.00 17.00  ? 889  VAL   B CG2 1 
ATOM   2636 N  N   . GLU   B 1 38  ? 18.930  6.109   -5.481  1.00 15.51  ? 890  GLU   B N   1 
ATOM   2637 C  CA  . GLU   B 1 38  ? 18.537  5.590   -6.797  1.00 16.13  ? 890  GLU   B CA  1 
ATOM   2638 C  C   . GLU   B 1 38  ? 18.521  4.065   -6.734  1.00 20.05  ? 890  GLU   B C   1 
ATOM   2639 O  O   . GLU   B 1 38  ? 19.388  3.454   -6.059  1.00 18.66  ? 890  GLU   B O   1 
ATOM   2640 C  CB  . GLU   B 1 38  ? 19.554  6.014   -7.837  1.00 16.79  ? 890  GLU   B CB  1 
ATOM   2641 C  CG  . GLU   B 1 38  ? 19.541  7.472   -8.142  1.00 19.99  ? 890  GLU   B CG  1 
ATOM   2642 C  CD  . GLU   B 1 38  ? 20.656  7.878   -9.074  1.00 27.42  ? 890  GLU   B CD  1 
ATOM   2643 O  OE1 . GLU   B 1 38  ? 21.827  7.509   -8.840  1.00 30.07  ? 890  GLU   B OE1 1 
ATOM   2644 O  OE2 . GLU   B 1 38  ? 20.371  8.603   -10.032 1.00 29.08  ? 890  GLU   B OE2 1 
ATOM   2645 N  N   . LEU   B 1 39  ? 17.568  3.468   -7.467  1.00 17.76  ? 891  LEU   B N   1 
ATOM   2646 C  CA  . LEU   B 1 39  ? 17.568  2.044   -7.722  1.00 18.17  ? 891  LEU   B CA  1 
ATOM   2647 C  C   . LEU   B 1 39  ? 18.556  1.786   -8.848  1.00 18.30  ? 891  LEU   B C   1 
ATOM   2648 O  O   . LEU   B 1 39  ? 18.499  2.413   -9.908  1.00 18.61  ? 891  LEU   B O   1 
ATOM   2649 C  CB  . LEU   B 1 39  ? 16.169  1.520   -8.087  1.00 22.46  ? 891  LEU   B CB  1 
ATOM   2650 C  CG  . LEU   B 1 39  ? 16.052  0.026   -8.389  1.00 20.05  ? 891  LEU   B CG  1 
ATOM   2651 C  CD1 . LEU   B 1 39  ? 16.538  -0.855  -7.217  1.00 23.04  ? 891  LEU   B CD1 1 
ATOM   2652 C  CD2 . LEU   B 1 39  ? 14.628  -0.304  -8.770  1.00 25.39  ? 891  LEU   B CD2 1 
ATOM   2653 N  N   . CYS   B 1 40  ? 19.462  0.864   -8.598  1.00 18.34  ? 892  CYS   B N   1 
ATOM   2654 C  CA  . CYS   B 1 40  ? 20.436  0.443   -9.577  1.00 19.18  ? 892  CYS   B CA  1 
ATOM   2655 C  C   . CYS   B 1 40  ? 20.453  -1.063  -9.635  1.00 20.73  ? 892  CYS   B C   1 
ATOM   2656 O  O   . CYS   B 1 40  ? 19.948  -1.727  -8.734  1.00 21.68  ? 892  CYS   B O   1 
ATOM   2657 C  CB  . CYS   B 1 40  ? 21.812  0.950   -9.169  1.00 18.38  ? 892  CYS   B CB  1 
ATOM   2658 S  SG  . CYS   B 1 40  ? 21.900  2.786   -9.225  1.00 22.50  ? 892  CYS   B SG  1 
ATOM   2659 N  N   A ARG   B 1 41  ? 21.036  -1.594  -10.705 0.50 21.99  ? 893  ARG   B N   1 
ATOM   2660 N  N   B ARG   B 1 41  ? 21.000  -1.603  -10.719 0.50 21.57  ? 893  ARG   B N   1 
ATOM   2661 C  CA  A ARG   B 1 41  ? 21.385  -3.005  -10.791 0.50 22.82  ? 893  ARG   B CA  1 
ATOM   2662 C  CA  B ARG   B 1 41  ? 21.387  -3.004  -10.762 0.50 21.79  ? 893  ARG   B CA  1 
ATOM   2663 C  C   A ARG   B 1 41  ? 22.895  -3.082  -10.874 0.50 23.20  ? 893  ARG   B C   1 
ATOM   2664 C  C   B ARG   B 1 41  ? 22.898  -3.051  -10.841 0.50 22.59  ? 893  ARG   B C   1 
ATOM   2665 O  O   A ARG   B 1 41  ? 23.502  -2.408  -11.719 0.50 24.93  ? 893  ARG   B O   1 
ATOM   2666 O  O   B ARG   B 1 41  ? 23.505  -2.328  -11.644 0.50 24.43  ? 893  ARG   B O   1 
ATOM   2667 C  CB  A ARG   B 1 41  ? 20.772  -3.658  -12.032 0.50 25.59  ? 893  ARG   B CB  1 
ATOM   2668 C  CB  B ARG   B 1 41  ? 20.788  -3.753  -11.957 0.50 24.26  ? 893  ARG   B CB  1 
ATOM   2669 C  CG  A ARG   B 1 41  ? 20.927  -5.188  -12.051 0.50 32.77  ? 893  ARG   B CG  1 
ATOM   2670 C  CG  B ARG   B 1 41  ? 21.097  -5.257  -11.886 0.50 29.07  ? 893  ARG   B CG  1 
ATOM   2671 C  CD  A ARG   B 1 41  ? 20.190  -5.834  -13.226 0.50 33.55  ? 893  ARG   B CD  1 
ATOM   2672 C  CD  B ARG   B 1 41  ? 20.342  -6.086  -12.911 0.50 27.74  ? 893  ARG   B CD  1 
ATOM   2673 N  NE  A ARG   B 1 41  ? 18.774  -5.464  -13.231 0.50 35.58  ? 893  ARG   B NE  1 
ATOM   2674 N  NE  B ARG   B 1 41  ? 18.907  -6.130  -12.618 0.50 29.26  ? 893  ARG   B NE  1 
ATOM   2675 C  CZ  A ARG   B 1 41  ? 17.830  -5.979  -12.439 0.50 39.22  ? 893  ARG   B CZ  1 
ATOM   2676 C  CZ  B ARG   B 1 41  ? 17.936  -5.540  -13.325 0.50 35.74  ? 893  ARG   B CZ  1 
ATOM   2677 N  NH1 A ARG   B 1 41  ? 18.105  -6.933  -11.552 0.50 35.66  ? 893  ARG   B NH1 1 
ATOM   2678 N  NH1 B ARG   B 1 41  ? 18.194  -4.825  -14.421 0.50 35.97  ? 893  ARG   B NH1 1 
ATOM   2679 N  NH2 A ARG   B 1 41  ? 16.580  -5.533  -12.539 0.50 42.47  ? 893  ARG   B NH2 1 
ATOM   2680 N  NH2 B ARG   B 1 41  ? 16.673  -5.672  -12.923 0.50 41.02  ? 893  ARG   B NH2 1 
ATOM   2681 N  N   . TYR   B 1 42  ? 23.503  -3.897  -10.011 1.00 21.90  ? 894  TYR   B N   1 
ATOM   2682 C  CA  . TYR   B 1 42  ? 24.922  -4.150  -10.087 1.00 22.00  ? 894  TYR   B CA  1 
ATOM   2683 C  C   . TYR   B 1 42  ? 25.084  -5.401  -10.943 1.00 24.27  ? 894  TYR   B C   1 
ATOM   2684 O  O   . TYR   B 1 42  ? 24.808  -6.519  -10.494 1.00 21.90  ? 894  TYR   B O   1 
ATOM   2685 C  CB  . TYR   B 1 42  ? 25.555  -4.335  -8.731  1.00 21.44  ? 894  TYR   B CB  1 
ATOM   2686 C  CG  . TYR   B 1 42  ? 27.059  -4.370  -8.840  1.00 22.86  ? 894  TYR   B CG  1 
ATOM   2687 C  CD1 . TYR   B 1 42  ? 27.761  -3.258  -9.323  1.00 24.51  ? 894  TYR   B CD1 1 
ATOM   2688 C  CD2 . TYR   B 1 42  ? 27.795  -5.497  -8.473  1.00 23.88  ? 894  TYR   B CD2 1 
ATOM   2689 C  CE1 . TYR   B 1 42  ? 29.124  -3.264  -9.425  1.00 20.84  ? 894  TYR   B CE1 1 
ATOM   2690 C  CE2 . TYR   B 1 42  ? 29.185  -5.505  -8.588  1.00 22.98  ? 894  TYR   B CE2 1 
ATOM   2691 C  CZ  . TYR   B 1 42  ? 29.839  -4.375  -9.078  1.00 21.64  ? 894  TYR   B CZ  1 
ATOM   2692 O  OH  . TYR   B 1 42  ? 31.201  -4.318  -9.202  1.00 25.05  ? 894  TYR   B OH  1 
ATOM   2693 N  N   . ASP   B 1 43  ? 25.540  -5.207  -12.173 1.00 23.83  ? 895  ASP   B N   1 
ATOM   2694 C  CA  . ASP   B 1 43  ? 25.480  -6.241  -13.180 1.00 22.60  ? 895  ASP   B CA  1 
ATOM   2695 C  C   . ASP   B 1 43  ? 26.850  -6.546  -13.817 1.00 27.34  ? 895  ASP   B C   1 
ATOM   2696 O  O   . ASP   B 1 43  ? 27.035  -6.347  -15.026 1.00 26.19  ? 895  ASP   B O   1 
ATOM   2697 C  CB  . ASP   B 1 43  ? 24.446  -5.809  -14.238 1.00 27.36  ? 895  ASP   B CB  1 
ATOM   2698 C  CG  . ASP   B 1 43  ? 23.996  -6.959  -15.150 1.00 28.50  ? 895  ASP   B CG  1 
ATOM   2699 O  OD1 . ASP   B 1 43  ? 23.700  -8.068  -14.654 1.00 32.30  ? 895  ASP   B OD1 1 
ATOM   2700 O  OD2 . ASP   B 1 43  ? 23.892  -6.743  -16.378 1.00 34.40  ? 895  ASP   B OD2 1 
ATOM   2701 N  N   . PRO   B 1 44  ? 27.805  -7.090  -13.022 1.00 26.14  ? 896  PRO   B N   1 
ATOM   2702 C  CA  . PRO   B 1 44  ? 29.122  -7.459  -13.553 1.00 31.43  ? 896  PRO   B CA  1 
ATOM   2703 C  C   . PRO   B 1 44  ? 29.091  -8.387  -14.775 1.00 32.95  ? 896  PRO   B C   1 
ATOM   2704 O  O   . PRO   B 1 44  ? 29.959  -8.265  -15.629 1.00 37.41  ? 896  PRO   B O   1 
ATOM   2705 C  CB  . PRO   B 1 44  ? 29.831  -8.138  -12.369 1.00 31.17  ? 896  PRO   B CB  1 
ATOM   2706 C  CG  . PRO   B 1 44  ? 28.824  -8.287  -11.313 1.00 25.49  ? 896  PRO   B CG  1 
ATOM   2707 C  CD  . PRO   B 1 44  ? 27.684  -7.403  -11.592 1.00 22.74  ? 896  PRO   B CD  1 
ATOM   2708 N  N   . GLU   B 1 45  ? 28.101  -9.284  -14.858 1.00 34.29  ? 897  GLU   B N   1 
ATOM   2709 C  CA  . GLU   B 1 45  ? 28.006  -10.239 -15.978 1.00 39.46  ? 897  GLU   B CA  1 
ATOM   2710 C  C   . GLU   B 1 45  ? 27.324  -9.662  -17.233 1.00 39.36  ? 897  GLU   B C   1 
ATOM   2711 O  O   . GLU   B 1 45  ? 27.320  -10.306 -18.272 1.00 39.71  ? 897  GLU   B O   1 
ATOM   2712 C  CB  . GLU   B 1 45  ? 27.297  -11.524 -15.537 1.00 40.78  ? 897  GLU   B CB  1 
ATOM   2713 C  CG  . GLU   B 1 45  ? 27.927  -12.177 -14.304 1.00 42.32  ? 897  GLU   B CG  1 
ATOM   2714 C  CD  . GLU   B 1 45  ? 27.355  -13.548 -13.999 1.00 39.10  ? 897  GLU   B CD  1 
ATOM   2715 O  OE1 . GLU   B 1 45  ? 26.297  -13.634 -13.361 1.00 50.53  ? 897  GLU   B OE1 1 
ATOM   2716 O  OE2 . GLU   B 1 45  ? 27.966  -14.543 -14.380 1.00 46.61  ? 897  GLU   B OE2 1 
ATOM   2717 N  N   . GLY   B 1 46  ? 26.739  -8.466  -17.130 1.00 38.73  ? 898  GLY   B N   1 
ATOM   2718 C  CA  . GLY   B 1 46  ? 26.217  -7.754  -18.309 1.00 39.26  ? 898  GLY   B CA  1 
ATOM   2719 C  C   . GLY   B 1 46  ? 24.950  -8.307  -18.956 1.00 42.69  ? 898  GLY   B C   1 
ATOM   2720 O  O   . GLY   B 1 46  ? 24.635  -7.951  -20.089 1.00 44.97  ? 898  GLY   B O   1 
ATOM   2721 N  N   . ASP   B 1 47  ? 24.205  -9.145  -18.239 1.00 41.95  ? 899  ASP   B N   1 
ATOM   2722 C  CA  . ASP   B 1 47  ? 23.021  -9.823  -18.789 1.00 41.02  ? 899  ASP   B CA  1 
ATOM   2723 C  C   . ASP   B 1 47  ? 21.722  -9.560  -18.012 1.00 41.06  ? 899  ASP   B C   1 
ATOM   2724 O  O   . ASP   B 1 47  ? 20.759  -10.331 -18.119 1.00 43.85  ? 899  ASP   B O   1 
ATOM   2725 C  CB  . ASP   B 1 47  ? 23.299  -11.329 -18.887 1.00 44.15  ? 899  ASP   B CB  1 
ATOM   2726 C  CG  . ASP   B 1 47  ? 23.508  -11.991 -17.535 1.00 41.83  ? 899  ASP   B CG  1 
ATOM   2727 O  OD1 . ASP   B 1 47  ? 23.703  -11.290 -16.532 1.00 40.00  ? 899  ASP   B OD1 1 
ATOM   2728 O  OD2 . ASP   B 1 47  ? 23.462  -13.233 -17.482 1.00 50.55  ? 899  ASP   B OD2 1 
ATOM   2729 N  N   . ASN   B 1 48  ? 21.707  -8.477  -17.232 1.00 40.42  ? 900  ASN   B N   1 
ATOM   2730 C  CA  . ASN   B 1 48  ? 20.556  -8.063  -16.426 1.00 39.04  ? 900  ASN   B CA  1 
ATOM   2731 C  C   . ASN   B 1 48  ? 20.103  -9.066  -15.346 1.00 40.59  ? 900  ASN   B C   1 
ATOM   2732 O  O   . ASN   B 1 48  ? 18.944  -9.027  -14.902 1.00 41.08  ? 900  ASN   B O   1 
ATOM   2733 C  CB  . ASN   B 1 48  ? 19.394  -7.636  -17.339 1.00 44.54  ? 900  ASN   B CB  1 
ATOM   2734 C  CG  . ASN   B 1 48  ? 19.769  -6.476  -18.239 1.00 46.42  ? 900  ASN   B CG  1 
ATOM   2735 O  OD1 . ASN   B 1 48  ? 19.769  -6.596  -19.463 1.00 64.29  ? 900  ASN   B OD1 1 
ATOM   2736 N  ND2 . ASN   B 1 48  ? 20.104  -5.345  -17.631 1.00 55.89  ? 900  ASN   B ND2 1 
ATOM   2737 N  N   . THR   B 1 49  ? 21.031  -9.925  -14.903 1.00 38.81  ? 901  THR   B N   1 
ATOM   2738 C  CA  . THR   B 1 49  ? 20.771  -10.922 -13.842 1.00 36.79  ? 901  THR   B CA  1 
ATOM   2739 C  C   . THR   B 1 49  ? 21.345  -10.519 -12.489 1.00 35.23  ? 901  THR   B C   1 
ATOM   2740 O  O   . THR   B 1 49  ? 21.060  -11.167 -11.475 1.00 35.65  ? 901  THR   B O   1 
ATOM   2741 C  CB  . THR   B 1 49  ? 21.346  -12.321 -14.209 1.00 37.01  ? 901  THR   B CB  1 
ATOM   2742 O  OG1 . THR   B 1 49  ? 22.778  -12.268 -14.211 1.00 35.15  ? 901  THR   B OG1 1 
ATOM   2743 C  CG2 . THR   B 1 49  ? 20.839  -12.787 -15.567 1.00 43.72  ? 901  THR   B CG2 1 
ATOM   2744 N  N   . GLY   B 1 50  ? 22.131  -9.446  -12.453 1.00 31.92  ? 902  GLY   B N   1 
ATOM   2745 C  CA  . GLY   B 1 50  ? 22.716  -8.964  -11.202 1.00 28.93  ? 902  GLY   B CA  1 
ATOM   2746 C  C   . GLY   B 1 50  ? 21.717  -8.445  -10.193 1.00 28.39  ? 902  GLY   B C   1 
ATOM   2747 O  O   . GLY   B 1 50  ? 20.547  -8.275  -10.495 1.00 30.16  ? 902  GLY   B O   1 
ATOM   2748 N  N   . GLU   B 1 51  ? 22.199  -8.169  -8.985  1.00 27.53  ? 903  GLU   B N   1 
ATOM   2749 C  CA  . GLU   B 1 51  ? 21.335  -7.772  -7.894  1.00 27.86  ? 903  GLU   B CA  1 
ATOM   2750 C  C   . GLU   B 1 51  ? 20.943  -6.299  -7.998  1.00 27.70  ? 903  GLU   B C   1 
ATOM   2751 O  O   . GLU   B 1 51  ? 21.749  -5.452  -8.433  1.00 25.04  ? 903  GLU   B O   1 
ATOM   2752 C  CB  . GLU   B 1 51  ? 22.014  -8.051  -6.555  1.00 30.37  ? 903  GLU   B CB  1 
ATOM   2753 C  CG  . GLU   B 1 51  ? 22.983  -6.984  -6.104  1.00 37.22  ? 903  GLU   B CG  1 
ATOM   2754 C  CD  . GLU   B 1 51  ? 23.915  -7.456  -5.023  1.00 45.15  ? 903  GLU   B CD  1 
ATOM   2755 O  OE1 . GLU   B 1 51  ? 23.407  -8.130  -4.093  1.00 28.19  ? 903  GLU   B OE1 1 
ATOM   2756 O  OE2 . GLU   B 1 51  ? 25.135  -7.140  -5.115  1.00 44.95  ? 903  GLU   B OE2 1 
ATOM   2757 N  N   . GLN   B 1 52  ? 19.707  -6.012  -7.586  1.00 25.82  ? 904  GLN   B N   1 
ATOM   2758 C  CA  . GLN   B 1 52  ? 19.221  -4.650  -7.464  1.00 23.38  ? 904  GLN   B CA  1 
ATOM   2759 C  C   . GLN   B 1 52  ? 19.749  -4.118  -6.132  1.00 21.94  ? 904  GLN   B C   1 
ATOM   2760 O  O   . GLN   B 1 52  ? 19.771  -4.844  -5.134  1.00 20.92  ? 904  GLN   B O   1 
ATOM   2761 C  CB  . GLN   B 1 52  ? 17.693  -4.597  -7.481  1.00 24.56  ? 904  GLN   B CB  1 
ATOM   2762 C  CG  . GLN   B 1 52  ? 17.065  -4.891  -8.843  1.00 28.63  ? 904  GLN   B CG  1 
ATOM   2763 C  CD  . GLN   B 1 52  ? 15.560  -4.691  -8.829  1.00 33.25  ? 904  GLN   B CD  1 
ATOM   2764 O  OE1 . GLN   B 1 52  ? 14.855  -5.190  -7.944  1.00 41.95  ? 904  GLN   B OE1 1 
ATOM   2765 N  NE2 . GLN   B 1 52  ? 15.061  -3.950  -9.806  1.00 33.05  ? 904  GLN   B NE2 1 
ATOM   2766 N  N   . VAL   B 1 53  ? 20.201  -2.866  -6.131  1.00 19.06  ? 905  VAL   B N   1 
ATOM   2767 C  CA  . VAL   B 1 53  ? 20.728  -2.220  -4.924  1.00 17.27  ? 905  VAL   B CA  1 
ATOM   2768 C  C   . VAL   B 1 53  ? 20.232  -0.764  -4.842  1.00 13.34  ? 905  VAL   B C   1 
ATOM   2769 O  O   . VAL   B 1 53  ? 19.838  -0.188  -5.836  1.00 18.50  ? 905  VAL   B O   1 
ATOM   2770 C  CB  . VAL   B 1 53  ? 22.282  -2.232  -4.881  1.00 16.21  ? 905  VAL   B CB  1 
ATOM   2771 C  CG1 . VAL   B 1 53  ? 22.798  -3.608  -4.761  1.00 19.01  ? 905  VAL   B CG1 1 
ATOM   2772 C  CG2 . VAL   B 1 53  ? 22.897  -1.596  -6.145  1.00 18.93  ? 905  VAL   B CG2 1 
ATOM   2773 N  N   . ALA   B 1 54  ? 20.252  -0.193  -3.641  1.00 13.02  ? 906  ALA   B N   1 
ATOM   2774 C  CA  . ALA   B 1 54  ? 19.893  1.204   -3.428  1.00 12.81  ? 906  ALA   B CA  1 
ATOM   2775 C  C   . ALA   B 1 54  ? 21.199  1.971   -3.280  1.00 15.67  ? 906  ALA   B C   1 
ATOM   2776 O  O   . ALA   B 1 54  ? 22.052  1.590   -2.455  1.00 15.87  ? 906  ALA   B O   1 
ATOM   2777 C  CB  . ALA   B 1 54  ? 19.055  1.355   -2.161  1.00 13.06  ? 906  ALA   B CB  1 
ATOM   2778 N  N   . VAL   B 1 55  ? 21.313  3.061   -4.031  1.00 13.12  ? 907  VAL   B N   1 
ATOM   2779 C  CA  . VAL   B 1 55  ? 22.550  3.840   -4.151  1.00 12.89  ? 907  VAL   B CA  1 
ATOM   2780 C  C   . VAL   B 1 55  ? 22.291  5.277   -3.758  1.00 13.80  ? 907  VAL   B C   1 
ATOM   2781 O  O   . VAL   B 1 55  ? 21.453  5.939   -4.369  1.00 13.87  ? 907  VAL   B O   1 
ATOM   2782 C  CB  . VAL   B 1 55  ? 23.119  3.769   -5.593  1.00 15.26  ? 907  VAL   B CB  1 
ATOM   2783 C  CG1 . VAL   B 1 55  ? 24.502  4.451   -5.687  1.00 15.32  ? 907  VAL   B CG1 1 
ATOM   2784 C  CG2 . VAL   B 1 55  ? 23.218  2.333   -6.008  1.00 14.87  ? 907  VAL   B CG2 1 
ATOM   2785 N  N   . LYS   B 1 56  ? 23.018  5.750   -2.742  1.00 16.30  ? 908  LYS   B N   1 
ATOM   2786 C  CA  . LYS   B 1 56  ? 22.940  7.134   -2.304  1.00 14.14  ? 908  LYS   B CA  1 
ATOM   2787 C  C   . LYS   B 1 56  ? 24.151  7.886   -2.799  1.00 15.08  ? 908  LYS   B C   1 
ATOM   2788 O  O   . LYS   B 1 56  ? 25.278  7.439   -2.616  1.00 17.41  ? 908  LYS   B O   1 
ATOM   2789 C  CB  . LYS   B 1 56  ? 22.835  7.258   -0.772  1.00 15.35  ? 908  LYS   B CB  1 
ATOM   2790 C  CG  . LYS   B 1 56  ? 22.459  8.642   -0.324  1.00 19.91  ? 908  LYS   B CG  1 
ATOM   2791 C  CD  . LYS   B 1 56  ? 22.096  8.640   1.164   1.00 19.67  ? 908  LYS   B CD  1 
ATOM   2792 C  CE  . LYS   B 1 56  ? 21.707  9.963   1.636   1.00 27.36  ? 908  LYS   B CE  1 
ATOM   2793 N  NZ  . LYS   B 1 56  ? 21.221  9.886   3.050   1.00 18.21  ? 908  LYS   B NZ  1 
ATOM   2794 N  N   A SER   B 1 57  ? 23.911  9.038   -3.417  0.50 20.57  ? 909  SER   B N   1 
ATOM   2795 N  N   B SER   B 1 57  ? 23.903  9.014   -3.465  0.50 20.71  ? 909  SER   B N   1 
ATOM   2796 C  CA  A SER   B 1 57  ? 24.976  9.865   -3.967  0.50 18.96  ? 909  SER   B CA  1 
ATOM   2797 C  CA  B SER   B 1 57  ? 24.953  9.877   -4.004  0.50 19.25  ? 909  SER   B CA  1 
ATOM   2798 C  C   A SER   B 1 57  ? 24.679  11.323  -3.691  0.50 25.33  ? 909  SER   B C   1 
ATOM   2799 C  C   B SER   B 1 57  ? 24.710  11.303  -3.554  0.50 25.36  ? 909  SER   B C   1 
ATOM   2800 O  O   A SER   B 1 57  ? 23.524  11.697  -3.459  0.50 24.65  ? 909  SER   B O   1 
ATOM   2801 O  O   B SER   B 1 57  ? 23.634  11.628  -3.045  0.50 24.26  ? 909  SER   B O   1 
ATOM   2802 C  CB  A SER   B 1 57  ? 25.073  9.628   -5.477  0.50 22.30  ? 909  SER   B CB  1 
ATOM   2803 C  CB  B SER   B 1 57  ? 24.936  9.840   -5.538  0.50 23.03  ? 909  SER   B CB  1 
ATOM   2804 O  OG  A SER   B 1 57  ? 23.874  10.010  -6.132  0.50 23.20  ? 909  SER   B OG  1 
ATOM   2805 O  OG  B SER   B 1 57  ? 25.031  8.523   -6.040  0.50 20.30  ? 909  SER   B OG  1 
ATOM   2806 N  N   . LEU   B 1 58  ? 25.720  12.150  -3.730  1.00 26.54  ? 910  LEU   B N   1 
ATOM   2807 C  CA  . LEU   B 1 58  ? 25.549  13.587  -3.572  1.00 31.20  ? 910  LEU   B CA  1 
ATOM   2808 C  C   . LEU   B 1 58  ? 24.822  14.173  -4.779  1.00 37.24  ? 910  LEU   B C   1 
ATOM   2809 O  O   . LEU   B 1 58  ? 25.046  13.751  -5.918  1.00 37.87  ? 910  LEU   B O   1 
ATOM   2810 C  CB  . LEU   B 1 58  ? 26.900  14.286  -3.449  1.00 33.47  ? 910  LEU   B CB  1 
ATOM   2811 C  CG  . LEU   B 1 58  ? 27.742  14.069  -2.195  1.00 35.35  ? 910  LEU   B CG  1 
ATOM   2812 C  CD1 . LEU   B 1 58  ? 28.960  14.972  -2.318  1.00 37.79  ? 910  LEU   B CD1 1 
ATOM   2813 C  CD2 . LEU   B 1 58  ? 26.977  14.384  -0.914  1.00 38.11  ? 910  LEU   B CD2 1 
ATOM   2814 N  N   . LYS   B 1 59  ? 23.951  15.141  -4.521  1.00 43.00  ? 911  LYS   B N   1 
ATOM   2815 C  CA  . LYS   B 1 59  ? 23.420  15.989  -5.576  1.00 50.12  ? 911  LYS   B CA  1 
ATOM   2816 C  C   . LYS   B 1 59  ? 24.464  17.073  -5.843  1.00 54.01  ? 911  LYS   B C   1 
ATOM   2817 O  O   . LYS   B 1 59  ? 24.822  17.802  -4.911  1.00 54.59  ? 911  LYS   B O   1 
ATOM   2818 C  CB  . LYS   B 1 59  ? 22.112  16.637  -5.142  1.00 52.04  ? 911  LYS   B CB  1 
ATOM   2819 C  CG  . LYS   B 1 59  ? 21.024  15.632  -4.822  1.00 53.18  ? 911  LYS   B CG  1 
ATOM   2820 C  CD  . LYS   B 1 59  ? 19.695  16.312  -4.542  1.00 58.38  ? 911  LYS   B CD  1 
ATOM   2821 C  CE  . LYS   B 1 59  ? 19.023  16.779  -5.823  1.00 58.53  ? 911  LYS   B CE  1 
ATOM   2822 N  NZ  . LYS   B 1 59  ? 17.669  17.310  -5.567  1.00 61.49  ? 911  LYS   B NZ  1 
ATOM   2823 N  N   . PRO   B 1 60  ? 24.989  17.157  -7.087  1.00 59.07  ? 912  PRO   B N   1 
ATOM   2824 C  CA  . PRO   B 1 60  ? 25.865  18.287  -7.433  1.00 63.66  ? 912  PRO   B CA  1 
ATOM   2825 C  C   . PRO   B 1 60  ? 25.100  19.604  -7.560  1.00 68.06  ? 912  PRO   B C   1 
ATOM   2826 O  O   . PRO   B 1 60  ? 24.765  20.224  -6.549  1.00 69.05  ? 912  PRO   B O   1 
ATOM   2827 C  CB  . PRO   B 1 60  ? 26.463  17.872  -8.783  1.00 64.98  ? 912  PRO   B CB  1 
ATOM   2828 C  CG  . PRO   B 1 60  ? 25.475  16.935  -9.365  1.00 61.78  ? 912  PRO   B CG  1 
ATOM   2829 C  CD  . PRO   B 1 60  ? 24.829  16.224  -8.220  1.00 57.72  ? 912  PRO   B CD  1 
ATOM   2830 N  N   . GLY   B 1 64  ? 29.381  22.556  -3.030  1.00 84.63  ? 916  GLY   B N   1 
ATOM   2831 C  CA  . GLY   B 1 64  ? 29.039  22.280  -1.639  1.00 81.90  ? 916  GLY   B CA  1 
ATOM   2832 C  C   . GLY   B 1 64  ? 29.980  21.287  -0.980  1.00 78.54  ? 916  GLY   B C   1 
ATOM   2833 O  O   . GLY   B 1 64  ? 30.496  20.377  -1.635  1.00 77.31  ? 916  GLY   B O   1 
ATOM   2834 N  N   . ASN   B 1 65  ? 30.165  21.442  0.331   1.00 77.77  ? 917  ASN   B N   1 
ATOM   2835 C  CA  . ASN   B 1 65  ? 31.129  20.639  1.107   1.00 74.24  ? 917  ASN   B CA  1 
ATOM   2836 C  C   . ASN   B 1 65  ? 30.613  19.268  1.580   1.00 66.05  ? 917  ASN   B C   1 
ATOM   2837 O  O   . ASN   B 1 65  ? 31.262  18.615  2.407   1.00 65.25  ? 917  ASN   B O   1 
ATOM   2838 C  CB  . ASN   B 1 65  ? 31.628  21.457  2.321   1.00 77.91  ? 917  ASN   B CB  1 
ATOM   2839 C  CG  . ASN   B 1 65  ? 30.601  21.531  3.462   1.00 79.41  ? 917  ASN   B CG  1 
ATOM   2840 O  OD1 . ASN   B 1 65  ? 29.397  21.660  3.230   1.00 81.27  ? 917  ASN   B OD1 1 
ATOM   2841 N  ND2 . ASN   B 1 65  ? 31.085  21.446  4.697   1.00 82.41  ? 917  ASN   B ND2 1 
ATOM   2842 N  N   . HIS   B 1 66  ? 29.484  18.816  1.028   1.00 59.76  ? 918  HIS   B N   1 
ATOM   2843 C  CA  . HIS   B 1 66  ? 28.690  17.729  1.624   1.00 50.89  ? 918  HIS   B CA  1 
ATOM   2844 C  C   . HIS   B 1 66  ? 29.265  16.311  1.463   1.00 43.47  ? 918  HIS   B C   1 
ATOM   2845 O  O   . HIS   B 1 66  ? 28.731  15.366  2.048   1.00 38.65  ? 918  HIS   B O   1 
ATOM   2846 C  CB  . HIS   B 1 66  ? 27.248  17.779  1.094   1.00 49.97  ? 918  HIS   B CB  1 
ATOM   2847 C  CG  . HIS   B 1 66  ? 26.556  19.080  1.366   1.00 57.02  ? 918  HIS   B CG  1 
ATOM   2848 N  ND1 . HIS   B 1 66  ? 26.088  19.427  2.615   1.00 62.65  ? 918  HIS   B ND1 1 
ATOM   2849 C  CD2 . HIS   B 1 66  ? 26.277  20.129  0.556   1.00 63.51  ? 918  HIS   B CD2 1 
ATOM   2850 C  CE1 . HIS   B 1 66  ? 25.545  20.631  2.562   1.00 65.23  ? 918  HIS   B CE1 1 
ATOM   2851 N  NE2 . HIS   B 1 66  ? 25.646  21.078  1.323   1.00 66.07  ? 918  HIS   B NE2 1 
ATOM   2852 N  N   . ILE   B 1 67  ? 30.335  16.164  0.678   1.00 40.58  ? 919  ILE   B N   1 
ATOM   2853 C  CA  . ILE   B 1 67  ? 31.068  14.885  0.558   1.00 36.32  ? 919  ILE   B CA  1 
ATOM   2854 C  C   . ILE   B 1 67  ? 31.527  14.344  1.909   1.00 30.58  ? 919  ILE   B C   1 
ATOM   2855 O  O   . ILE   B 1 67  ? 31.440  13.144  2.158   1.00 26.52  ? 919  ILE   B O   1 
ATOM   2856 C  CB  . ILE   B 1 67  ? 32.289  15.032  -0.414  1.00 37.67  ? 919  ILE   B CB  1 
ATOM   2857 C  CG1 . ILE   B 1 67  ? 32.861  13.666  -0.778  1.00 41.06  ? 919  ILE   B CG1 1 
ATOM   2858 C  CG2 . ILE   B 1 67  ? 33.381  15.934  0.170   1.00 42.50  ? 919  ILE   B CG2 1 
ATOM   2859 C  CD1 . ILE   B 1 67  ? 33.694  13.702  -2.019  1.00 48.46  ? 919  ILE   B CD1 1 
ATOM   2860 N  N   . ALA   B 1 68  ? 31.994  15.240  2.777   1.00 33.32  ? 920  ALA   B N   1 
ATOM   2861 C  CA  . ALA   B 1 68  ? 32.434  14.873  4.125   1.00 33.53  ? 920  ALA   B CA  1 
ATOM   2862 C  C   . ALA   B 1 68  ? 31.279  14.280  4.912   1.00 31.12  ? 920  ALA   B C   1 
ATOM   2863 O  O   . ALA   B 1 68  ? 31.437  13.244  5.575   1.00 30.90  ? 920  ALA   B O   1 
ATOM   2864 C  CB  . ALA   B 1 68  ? 32.988  16.071  4.844   1.00 37.29  ? 920  ALA   B CB  1 
ATOM   2865 N  N   . ASP   B 1 69  ? 30.116  14.923  4.823   1.00 30.54  ? 921  ASP   B N   1 
ATOM   2866 C  CA  . ASP   B 1 69  ? 28.915  14.407  5.492   1.00 29.46  ? 921  ASP   B CA  1 
ATOM   2867 C  C   . ASP   B 1 69  ? 28.518  13.034  4.972   1.00 24.48  ? 921  ASP   B C   1 
ATOM   2868 O  O   . ASP   B 1 69  ? 28.184  12.142  5.758   1.00 22.90  ? 921  ASP   B O   1 
ATOM   2869 C  CB  . ASP   B 1 69  ? 27.726  15.361  5.333   1.00 31.30  ? 921  ASP   B CB  1 
ATOM   2870 C  CG  . ASP   B 1 69  ? 27.916  16.682  6.058   1.00 39.34  ? 921  ASP   B CG  1 
ATOM   2871 O  OD1 . ASP   B 1 69  ? 28.601  16.740  7.106   1.00 39.99  ? 921  ASP   B OD1 1 
ATOM   2872 O  OD2 . ASP   B 1 69  ? 27.345  17.673  5.572   1.00 45.05  ? 921  ASP   B OD2 1 
ATOM   2873 N  N   . LEU   B 1 70  ? 28.532  12.854  3.654   1.00 22.52  ? 922  LEU   B N   1 
ATOM   2874 C  CA  . LEU   B 1 70  ? 28.192  11.564  3.078   1.00 20.94  ? 922  LEU   B CA  1 
ATOM   2875 C  C   . LEU   B 1 70  ? 29.194  10.486  3.545   1.00 19.21  ? 922  LEU   B C   1 
ATOM   2876 O  O   . LEU   B 1 70  ? 28.787  9.364   3.879   1.00 16.47  ? 922  LEU   B O   1 
ATOM   2877 C  CB  . LEU   B 1 70  ? 28.108  11.635  1.548   1.00 22.14  ? 922  LEU   B CB  1 
ATOM   2878 C  CG  . LEU   B 1 70  ? 27.791  10.333  0.822   1.00 19.13  ? 922  LEU   B CG  1 
ATOM   2879 C  CD1 . LEU   B 1 70  ? 26.480  9.701   1.289   1.00 19.15  ? 922  LEU   B CD1 1 
ATOM   2880 C  CD2 . LEU   B 1 70  ? 27.771  10.538  -0.708  1.00 23.61  ? 922  LEU   B CD2 1 
ATOM   2881 N  N   . LYS   B 1 71  ? 30.488  10.834  3.554   1.00 19.70  ? 923  LYS   B N   1 
ATOM   2882 C  CA  . LYS   B 1 71  ? 31.524  9.911   4.002   1.00 19.56  ? 923  LYS   B CA  1 
ATOM   2883 C  C   . LYS   B 1 71  ? 31.328  9.525   5.479   1.00 20.89  ? 923  LYS   B C   1 
ATOM   2884 O  O   . LYS   B 1 71  ? 31.492  8.346   5.851   1.00 17.71  ? 923  LYS   B O   1 
ATOM   2885 C  CB  . LYS   B 1 71  ? 32.914  10.501  3.775   1.00 24.23  ? 923  LYS   B CB  1 
ATOM   2886 C  CG  . LYS   B 1 71  ? 33.377  10.457  2.355   1.00 27.43  ? 923  LYS   B CG  1 
ATOM   2887 C  CD  . LYS   B 1 71  ? 34.739  11.090  2.240   1.00 28.16  ? 923  LYS   B CD  1 
ATOM   2888 C  CE  . LYS   B 1 71  ? 35.385  10.769  0.924   1.00 37.37  ? 923  LYS   B CE  1 
ATOM   2889 N  NZ  . LYS   B 1 71  ? 36.799  11.214  0.923   1.00 37.08  ? 923  LYS   B NZ  1 
ATOM   2890 N  N   . LYS   B 1 72  ? 30.905  10.496  6.303   1.00 22.38  ? 924  LYS   B N   1 
ATOM   2891 C  CA  . LYS   B 1 72  ? 30.529  10.221  7.708   1.00 22.63  ? 924  LYS   B CA  1 
ATOM   2892 C  C   . LYS   B 1 72  ? 29.332  9.275   7.817   1.00 20.73  ? 924  LYS   B C   1 
ATOM   2893 O  O   . LYS   B 1 72  ? 29.364  8.302   8.574   1.00 20.39  ? 924  LYS   B O   1 
ATOM   2894 C  CB  . LYS   B 1 72  ? 30.279  11.518  8.500   1.00 26.55  ? 924  LYS   B CB  1 
ATOM   2895 C  CG  . LYS   B 1 72  ? 31.546  12.256  8.935   1.00 36.95  ? 924  LYS   B CG  1 
ATOM   2896 C  CD  . LYS   B 1 72  ? 31.221  13.448  9.867   1.00 41.02  ? 924  LYS   B CD  1 
ATOM   2897 C  CE  . LYS   B 1 72  ? 32.466  14.071  10.480  1.00 49.46  ? 924  LYS   B CE  1 
ATOM   2898 N  NZ  . LYS   B 1 72  ? 32.116  15.261  11.318  1.00 54.31  ? 924  LYS   B NZ  1 
ATOM   2899 N  N   . GLU   B 1 73  ? 28.283  9.537   7.041   1.00 19.70  ? 925  GLU   B N   1 
ATOM   2900 C  CA  . GLU   B 1 73  ? 27.131  8.658   6.971   1.00 17.38  ? 925  GLU   B CA  1 
ATOM   2901 C  C   . GLU   B 1 73  ? 27.455  7.210   6.599   1.00 16.31  ? 925  GLU   B C   1 
ATOM   2902 O  O   . GLU   B 1 73  ? 26.899  6.266   7.172   1.00 16.68  ? 925  GLU   B O   1 
ATOM   2903 C  CB  . GLU   B 1 73  ? 26.157  9.217   5.944   1.00 18.49  ? 925  GLU   B CB  1 
ATOM   2904 C  CG  . GLU   B 1 73  ? 24.823  8.555   5.930   1.00 15.55  ? 925  GLU   B CG  1 
ATOM   2905 C  CD  . GLU   B 1 73  ? 23.897  9.194   4.916   1.00 22.43  ? 925  GLU   B CD  1 
ATOM   2906 O  OE1 . GLU   B 1 73  ? 24.229  10.289  4.393   1.00 19.88  ? 925  GLU   B OE1 1 
ATOM   2907 O  OE2 . GLU   B 1 73  ? 22.818  8.614   4.682   1.00 25.17  ? 925  GLU   B OE2 1 
ATOM   2908 N  N   . ILE   B 1 74  ? 28.309  7.048   5.586   1.00 17.16  ? 926  ILE   B N   1 
ATOM   2909 C  CA  . ILE   B 1 74  ? 28.752  5.757   5.101   1.00 15.85  ? 926  ILE   B CA  1 
ATOM   2910 C  C   . ILE   B 1 74  ? 29.452  4.987   6.226   1.00 17.23  ? 926  ILE   B C   1 
ATOM   2911 O  O   . ILE   B 1 74  ? 29.190  3.795   6.466   1.00 16.21  ? 926  ILE   B O   1 
ATOM   2912 C  CB  . ILE   B 1 74  ? 29.721  5.924   3.890   1.00 19.59  ? 926  ILE   B CB  1 
ATOM   2913 C  CG1 . ILE   B 1 74  ? 28.930  6.288   2.629   1.00 17.23  ? 926  ILE   B CG1 1 
ATOM   2914 C  CG2 . ILE   B 1 74  ? 30.525  4.628   3.626   1.00 20.54  ? 926  ILE   B CG2 1 
ATOM   2915 C  CD1 . ILE   B 1 74  ? 29.754  6.905   1.510   1.00 19.95  ? 926  ILE   B CD1 1 
ATOM   2916 N  N   . GLU   B 1 75  ? 30.338  5.675   6.934   1.00 17.13  ? 927  GLU   B N   1 
ATOM   2917 C  CA  . GLU   B 1 75  ? 31.132  5.029   7.965   1.00 21.77  ? 927  GLU   B CA  1 
ATOM   2918 C  C   . GLU   B 1 75  ? 30.255  4.661   9.174   1.00 22.80  ? 927  GLU   B C   1 
ATOM   2919 O  O   . GLU   B 1 75  ? 30.480  3.636   9.805   1.00 23.10  ? 927  GLU   B O   1 
ATOM   2920 C  CB  . GLU   B 1 75  ? 32.286  5.934   8.405   1.00 26.66  ? 927  GLU   B CB  1 
ATOM   2921 C  CG  . GLU   B 1 75  ? 33.255  5.272   9.360   1.00 28.95  ? 927  GLU   B CG  1 
ATOM   2922 C  CD  . GLU   B 1 75  ? 33.899  4.009   8.806   1.00 31.82  ? 927  GLU   B CD  1 
ATOM   2923 O  OE1 . GLU   B 1 75  ? 33.942  3.818   7.570   1.00 22.60  ? 927  GLU   B OE1 1 
ATOM   2924 O  OE2 . GLU   B 1 75  ? 34.379  3.209   9.628   1.00 28.22  ? 927  GLU   B OE2 1 
ATOM   2925 N  N   . ILE   B 1 76  ? 29.256  5.492   9.470   1.00 20.39  ? 928  ILE   B N   1 
ATOM   2926 C  CA  . ILE   B 1 76  ? 28.210  5.149   10.429  1.00 19.19  ? 928  ILE   B CA  1 
ATOM   2927 C  C   . ILE   B 1 76  ? 27.449  3.886   9.992   1.00 16.67  ? 928  ILE   B C   1 
ATOM   2928 O  O   . ILE   B 1 76  ? 27.332  2.940   10.747  1.00 18.99  ? 928  ILE   B O   1 
ATOM   2929 C  CB  . ILE   B 1 76  ? 27.200  6.301   10.639  1.00 17.28  ? 928  ILE   B CB  1 
ATOM   2930 C  CG1 . ILE   B 1 76  ? 27.871  7.492   11.343  1.00 23.23  ? 928  ILE   B CG1 1 
ATOM   2931 C  CG2 . ILE   B 1 76  ? 25.979  5.814   11.460  1.00 21.63  ? 928  ILE   B CG2 1 
ATOM   2932 C  CD1 . ILE   B 1 76  ? 27.029  8.783   11.324  1.00 23.21  ? 928  ILE   B CD1 1 
ATOM   2933 N  N   . LEU   B 1 77  ? 26.968  3.854   8.768   1.00 15.01  ? 929  LEU   B N   1 
ATOM   2934 C  CA  . LEU   B 1 77  ? 26.108  2.743   8.379   1.00 13.68  ? 929  LEU   B CA  1 
ATOM   2935 C  C   . LEU   B 1 77  ? 26.856  1.421   8.254   1.00 12.37  ? 929  LEU   B C   1 
ATOM   2936 O  O   . LEU   B 1 77  ? 26.290  0.371   8.613   1.00 15.29  ? 929  LEU   B O   1 
ATOM   2937 C  CB  . LEU   B 1 77  ? 25.340  3.055   7.080   1.00 13.50  ? 929  LEU   B CB  1 
ATOM   2938 C  CG  . LEU   B 1 77  ? 24.225  2.068   6.747   1.00 14.48  ? 929  LEU   B CG  1 
ATOM   2939 C  CD1 . LEU   B 1 77  ? 23.089  1.969   7.796   1.00 14.31  ? 929  LEU   B CD1 1 
ATOM   2940 C  CD2 . LEU   B 1 77  ? 23.620  2.431   5.418   1.00 11.30  ? 929  LEU   B CD2 1 
ATOM   2941 N  N   . ARG   B 1 78  ? 28.103  1.482   7.785   1.00 16.16  ? 930  ARG   B N   1 
ATOM   2942 C  CA  . ARG   B 1 78  ? 28.998  0.332   7.642   1.00 19.69  ? 930  ARG   B CA  1 
ATOM   2943 C  C   . ARG   B 1 78  ? 29.134  -0.497  8.921   1.00 20.32  ? 930  ARG   B C   1 
ATOM   2944 O  O   . ARG   B 1 78  ? 29.257  -1.727  8.865   1.00 21.97  ? 930  ARG   B O   1 
ATOM   2945 C  CB  . ARG   B 1 78  ? 30.396  0.816   7.233   1.00 17.46  ? 930  ARG   B CB  1 
ATOM   2946 C  CG  . ARG   B 1 78  ? 31.324  -0.271  6.764   1.00 20.67  ? 930  ARG   B CG  1 
ATOM   2947 C  CD  . ARG   B 1 78  ? 32.580  0.329   6.167   1.00 24.74  ? 930  ARG   B CD  1 
ATOM   2948 N  NE  . ARG   B 1 78  ? 33.524  0.808   7.176   1.00 21.44  ? 930  ARG   B NE  1 
ATOM   2949 C  CZ  . ARG   B 1 78  ? 34.386  0.042   7.847   1.00 28.55  ? 930  ARG   B CZ  1 
ATOM   2950 N  NH1 . ARG   B 1 78  ? 34.407  -1.275  7.657   1.00 27.62  ? 930  ARG   B NH1 1 
ATOM   2951 N  NH2 . ARG   B 1 78  ? 35.243  0.585   8.713   1.00 28.88  ? 930  ARG   B NH2 1 
ATOM   2952 N  N   . ASN   B 1 79  ? 29.132  0.202   10.053  1.00 22.94  ? 931  ASN   B N   1 
ATOM   2953 C  CA  . ASN   B 1 79  ? 29.323  -0.405  11.369  1.00 21.83  ? 931  ASN   B CA  1 
ATOM   2954 C  C   . ASN   B 1 79  ? 28.035  -0.628  12.138  1.00 25.85  ? 931  ASN   B C   1 
ATOM   2955 O  O   . ASN   B 1 79  ? 28.090  -1.017  13.300  1.00 26.56  ? 931  ASN   B O   1 
ATOM   2956 C  CB  . ASN   B 1 79  ? 30.260  0.472   12.192  1.00 27.81  ? 931  ASN   B CB  1 
ATOM   2957 C  CG  . ASN   B 1 79  ? 31.634  0.528   11.591  1.00 30.80  ? 931  ASN   B CG  1 
ATOM   2958 O  OD1 . ASN   B 1 79  ? 32.328  -0.493  11.523  1.00 39.24  ? 931  ASN   B OD1 1 
ATOM   2959 N  ND2 . ASN   B 1 79  ? 32.009  1.704   11.064  1.00 31.30  ? 931  ASN   B ND2 1 
ATOM   2960 N  N   . LEU   B 1 80  ? 26.890  -0.424  11.490  1.00 21.28  ? 932  LEU   B N   1 
ATOM   2961 C  CA  . LEU   B 1 80  ? 25.599  -0.746  12.095  1.00 21.49  ? 932  LEU   B CA  1 
ATOM   2962 C  C   . LEU   B 1 80  ? 25.119  -2.099  11.567  1.00 20.62  ? 932  LEU   B C   1 
ATOM   2963 O  O   . LEU   B 1 80  ? 24.996  -2.298  10.348  1.00 19.82  ? 932  LEU   B O   1 
ATOM   2964 C  CB  . LEU   B 1 80  ? 24.571  0.355   11.833  1.00 19.68  ? 932  LEU   B CB  1 
ATOM   2965 C  CG  . LEU   B 1 80  ? 24.758  1.762   12.432  1.00 23.96  ? 932  LEU   B CG  1 
ATOM   2966 C  CD1 . LEU   B 1 80  ? 23.574  2.647   12.063  1.00 24.34  ? 932  LEU   B CD1 1 
ATOM   2967 C  CD2 . LEU   B 1 80  ? 24.974  1.803   13.959  1.00 26.30  ? 932  LEU   B CD2 1 
ATOM   2968 N  N   . TYR   B 1 81  ? 24.861  -3.029  12.489  1.00 23.27  ? 933  TYR   B N   1 
ATOM   2969 C  CA  . TYR   B 1 81  ? 24.352  -4.374  12.150  1.00 26.94  ? 933  TYR   B CA  1 
ATOM   2970 C  C   . TYR   B 1 81  ? 23.152  -4.699  13.040  1.00 23.76  ? 933  TYR   B C   1 
ATOM   2971 O  O   . TYR   B 1 81  ? 23.312  -5.091  14.197  1.00 23.08  ? 933  TYR   B O   1 
ATOM   2972 C  CB  . TYR   B 1 81  ? 25.411  -5.465  12.345  1.00 32.93  ? 933  TYR   B CB  1 
ATOM   2973 C  CG  . TYR   B 1 81  ? 26.734  -5.229  11.683  1.00 40.99  ? 933  TYR   B CG  1 
ATOM   2974 C  CD1 . TYR   B 1 81  ? 26.958  -5.632  10.360  1.00 50.29  ? 933  TYR   B CD1 1 
ATOM   2975 C  CD2 . TYR   B 1 81  ? 27.796  -4.648  12.388  1.00 48.90  ? 933  TYR   B CD2 1 
ATOM   2976 C  CE1 . TYR   B 1 81  ? 28.202  -5.433  9.742   1.00 49.79  ? 933  TYR   B CE1 1 
ATOM   2977 C  CE2 . TYR   B 1 81  ? 29.041  -4.446  11.782  1.00 49.24  ? 933  TYR   B CE2 1 
ATOM   2978 C  CZ  . TYR   B 1 81  ? 29.235  -4.841  10.460  1.00 52.10  ? 933  TYR   B CZ  1 
ATOM   2979 O  OH  . TYR   B 1 81  ? 30.462  -4.649  9.859   1.00 55.35  ? 933  TYR   B OH  1 
ATOM   2980 N  N   . HIS   B 1 82  ? 21.960  -4.538  12.482  1.00 18.50  ? 934  HIS   B N   1 
ATOM   2981 C  CA  . HIS   B 1 82  ? 20.710  -4.806  13.211  1.00 17.65  ? 934  HIS   B CA  1 
ATOM   2982 C  C   . HIS   B 1 82  ? 19.587  -5.157  12.258  1.00 18.56  ? 934  HIS   B C   1 
ATOM   2983 O  O   . HIS   B 1 82  ? 19.496  -4.609  11.175  1.00 18.28  ? 934  HIS   B O   1 
ATOM   2984 C  CB  . HIS   B 1 82  ? 20.305  -3.596  14.051  1.00 16.20  ? 934  HIS   B CB  1 
ATOM   2985 C  CG  . HIS   B 1 82  ? 19.192  -3.873  15.012  1.00 18.10  ? 934  HIS   B CG  1 
ATOM   2986 N  ND1 . HIS   B 1 82  ? 17.864  -3.721  14.691  1.00 23.43  ? 934  HIS   B ND1 1 
ATOM   2987 C  CD2 . HIS   B 1 82  ? 19.220  -4.309  16.296  1.00 26.37  ? 934  HIS   B CD2 1 
ATOM   2988 C  CE1 . HIS   B 1 82  ? 17.119  -4.046  15.734  1.00 20.02  ? 934  HIS   B CE1 1 
ATOM   2989 N  NE2 . HIS   B 1 82  ? 17.918  -4.403  16.724  1.00 22.04  ? 934  HIS   B NE2 1 
ATOM   2990 N  N   . GLU   B 1 83  ? 18.722  -6.071  12.699  1.00 21.72  ? 935  GLU   B N   1 
ATOM   2991 C  CA  . GLU   B 1 83  ? 17.612  -6.573  11.899  1.00 22.59  ? 935  GLU   B CA  1 
ATOM   2992 C  C   . GLU   B 1 83  ? 16.657  -5.472  11.364  1.00 19.49  ? 935  GLU   B C   1 
ATOM   2993 O  O   . GLU   B 1 83  ? 16.071  -5.613  10.291  1.00 18.35  ? 935  GLU   B O   1 
ATOM   2994 C  CB  . GLU   B 1 83  ? 16.830  -7.588  12.758  1.00 26.71  ? 935  GLU   B CB  1 
ATOM   2995 C  CG  . GLU   B 1 83  ? 15.739  -8.314  12.051  1.00 39.99  ? 935  GLU   B CG  1 
ATOM   2996 C  CD  . GLU   B 1 83  ? 15.173  -9.468  12.859  1.00 45.42  ? 935  GLU   B CD  1 
ATOM   2997 O  OE1 . GLU   B 1 83  ? 14.885  -9.284  14.068  1.00 52.33  ? 935  GLU   B OE1 1 
ATOM   2998 O  OE2 . GLU   B 1 83  ? 15.004  -10.560 12.273  1.00 57.65  ? 935  GLU   B OE2 1 
ATOM   2999 N  N   . ASN   B 1 84  ? 16.509  -4.407  12.150  1.00 16.78  ? 936  ASN   B N   1 
ATOM   3000 C  CA  . ASN   B 1 84  ? 15.679  -3.250  11.850  1.00 14.29  ? 936  ASN   B CA  1 
ATOM   3001 C  C   . ASN   B 1 84  ? 16.434  -1.997  11.360  1.00 11.69  ? 936  ASN   B C   1 
ATOM   3002 O  O   . ASN   B 1 84  ? 15.941  -0.876  11.528  1.00 11.76  ? 936  ASN   B O   1 
ATOM   3003 C  CB  . ASN   B 1 84  ? 14.839  -2.958  13.098  1.00 16.20  ? 936  ASN   B CB  1 
ATOM   3004 C  CG  . ASN   B 1 84  ? 14.005  -4.149  13.485  1.00 19.27  ? 936  ASN   B CG  1 
ATOM   3005 O  OD1 . ASN   B 1 84  ? 14.105  -4.639  14.603  1.00 19.55  ? 936  ASN   B OD1 1 
ATOM   3006 N  ND2 . ASN   B 1 84  ? 13.214  -4.671  12.518  1.00 15.90  ? 936  ASN   B ND2 1 
ATOM   3007 N  N   A ILE   B 1 85  ? 17.615  -2.214  10.777  0.50 10.62  ? 937  ILE   B N   1 
ATOM   3008 N  N   B ILE   B 1 85  ? 17.610  -2.215  10.766  0.50 11.28  ? 937  ILE   B N   1 
ATOM   3009 C  CA  A ILE   B 1 85  ? 18.431  -1.166  10.165  0.50 12.38  ? 937  ILE   B CA  1 
ATOM   3010 C  CA  B ILE   B 1 85  ? 18.439  -1.168  10.170  0.50 13.62  ? 937  ILE   B CA  1 
ATOM   3011 C  C   A ILE   B 1 85  ? 18.828  -1.652  8.781   0.50 12.79  ? 937  ILE   B C   1 
ATOM   3012 C  C   B ILE   B 1 85  ? 18.842  -1.645  8.784   0.50 13.35  ? 937  ILE   B C   1 
ATOM   3013 O  O   A ILE   B 1 85  ? 19.345  -2.765  8.631   0.50 11.65  ? 937  ILE   B O   1 
ATOM   3014 O  O   B ILE   B 1 85  ? 19.380  -2.749  8.637   0.50 12.15  ? 937  ILE   B O   1 
ATOM   3015 C  CB  A ILE   B 1 85  ? 19.668  -0.845  11.003  0.50 13.64  ? 937  ILE   B CB  1 
ATOM   3016 C  CB  B ILE   B 1 85  ? 19.695  -0.887  11.007  0.50 15.53  ? 937  ILE   B CB  1 
ATOM   3017 C  CG1 A ILE   B 1 85  ? 19.232  -0.063  12.251  0.50 11.69  ? 937  ILE   B CG1 1 
ATOM   3018 C  CG1 B ILE   B 1 85  ? 19.315  -0.354  12.401  0.50 16.49  ? 937  ILE   B CG1 1 
ATOM   3019 C  CG2 A ILE   B 1 85  ? 20.708  -0.052  10.151  0.50 13.84  ? 937  ILE   B CG2 1 
ATOM   3020 C  CG2 B ILE   B 1 85  ? 20.636  0.088   10.265  0.50 17.57  ? 937  ILE   B CG2 1 
ATOM   3021 C  CD1 A ILE   B 1 85  ? 20.336  0.297   13.181  0.50 10.85  ? 937  ILE   B CD1 1 
ATOM   3022 C  CD1 B ILE   B 1 85  ? 18.560  0.967   12.428  0.50 15.48  ? 937  ILE   B CD1 1 
ATOM   3023 N  N   . VAL   B 1 86  ? 18.580  -0.821  7.769   1.00 12.90  ? 938  VAL   B N   1 
ATOM   3024 C  CA  . VAL   B 1 86  ? 18.843  -1.223  6.369   1.00 14.91  ? 938  VAL   B CA  1 
ATOM   3025 C  C   . VAL   B 1 86  ? 20.334  -1.604  6.199   1.00 13.66  ? 938  VAL   B C   1 
ATOM   3026 O  O   . VAL   B 1 86  ? 21.239  -0.991  6.808   1.00 12.48  ? 938  VAL   B O   1 
ATOM   3027 C  CB  . VAL   B 1 86  ? 18.467  -0.114  5.353   1.00 13.05  ? 938  VAL   B CB  1 
ATOM   3028 C  CG1 . VAL   B 1 86  ? 19.452  1.047   5.442   1.00 12.66  ? 938  VAL   B CG1 1 
ATOM   3029 C  CG2 . VAL   B 1 86  ? 18.405  -0.672  3.952   1.00 13.00  ? 938  VAL   B CG2 1 
ATOM   3030 N  N   . LYS   B 1 87  ? 20.561  -2.647  5.398   1.00 16.06  ? 939  LYS   B N   1 
ATOM   3031 C  CA  . LYS   B 1 87  ? 21.877  -3.258  5.261   1.00 16.11  ? 939  LYS   B CA  1 
ATOM   3032 C  C   . LYS   B 1 87  ? 22.792  -2.474  4.335   1.00 16.24  ? 939  LYS   B C   1 
ATOM   3033 O  O   . LYS   B 1 87  ? 22.495  -2.324  3.141   1.00 18.52  ? 939  LYS   B O   1 
ATOM   3034 C  CB  . LYS   B 1 87  ? 21.783  -4.702  4.766   1.00 18.53  ? 939  LYS   B CB  1 
ATOM   3035 C  CG  . LYS   B 1 87  ? 21.245  -5.661  5.785   1.00 19.60  ? 939  LYS   B CG  1 
ATOM   3036 C  CD  . LYS   B 1 87  ? 21.283  -7.107  5.310   1.00 32.55  ? 939  LYS   B CD  1 
ATOM   3037 C  CE  . LYS   B 1 87  ? 21.078  -8.075  6.481   1.00 37.78  ? 939  LYS   B CE  1 
ATOM   3038 N  NZ  . LYS   B 1 87  ? 21.180  -9.489  6.069   0.00 39.73  ? 939  LYS   B NZ  1 
ATOM   3039 N  N   . TYR   B 1 88  ? 23.904  -2.020  4.896   1.00 18.84  ? 940  TYR   B N   1 
ATOM   3040 C  CA  . TYR   B 1 88  ? 25.075  -1.592  4.126   1.00 17.77  ? 940  TYR   B CA  1 
ATOM   3041 C  C   . TYR   B 1 88  ? 25.601  -2.757  3.273   1.00 15.85  ? 940  TYR   B C   1 
ATOM   3042 O  O   . TYR   B 1 88  ? 25.764  -3.878  3.785   1.00 19.07  ? 940  TYR   B O   1 
ATOM   3043 C  CB  . TYR   B 1 88  ? 26.180  -1.125  5.076   1.00 17.36  ? 940  TYR   B CB  1 
ATOM   3044 C  CG  . TYR   B 1 88  ? 27.545  -0.837  4.450   1.00 16.29  ? 940  TYR   B CG  1 
ATOM   3045 C  CD1 . TYR   B 1 88  ? 27.864  0.454   3.983   1.00 19.42  ? 940  TYR   B CD1 1 
ATOM   3046 C  CD2 . TYR   B 1 88  ? 28.527  -1.818  4.359   1.00 22.61  ? 940  TYR   B CD2 1 
ATOM   3047 C  CE1 . TYR   B 1 88  ? 29.095  0.748   3.436   1.00 17.13  ? 940  TYR   B CE1 1 
ATOM   3048 C  CE2 . TYR   B 1 88  ? 29.796  -1.537  3.805   1.00 20.12  ? 940  TYR   B CE2 1 
ATOM   3049 C  CZ  . TYR   B 1 88  ? 30.069  -0.237  3.350   1.00 19.28  ? 940  TYR   B CZ  1 
ATOM   3050 O  OH  . TYR   B 1 88  ? 31.279  0.073   2.783   1.00 19.70  ? 940  TYR   B OH  1 
ATOM   3051 N  N   . LYS   B 1 89  ? 25.892  -2.485  1.994   1.00 16.51  ? 941  LYS   B N   1 
ATOM   3052 C  CA  . LYS   B 1 89  ? 26.545  -3.483  1.128   1.00 13.90  ? 941  LYS   B CA  1 
ATOM   3053 C  C   . LYS   B 1 89  ? 27.934  -3.055  0.699   1.00 15.08  ? 941  LYS   B C   1 
ATOM   3054 O  O   . LYS   B 1 89  ? 28.831  -3.893  0.555   1.00 15.25  ? 941  LYS   B O   1 
ATOM   3055 C  CB  . LYS   B 1 89  ? 25.678  -3.774  -0.108  1.00 18.10  ? 941  LYS   B CB  1 
ATOM   3056 C  CG  . LYS   B 1 89  ? 24.424  -4.565  0.221   1.00 18.26  ? 941  LYS   B CG  1 
ATOM   3057 C  CD  . LYS   B 1 89  ? 23.524  -4.731  -0.992  1.00 27.08  ? 941  LYS   B CD  1 
ATOM   3058 C  CE  . LYS   B 1 89  ? 23.934  -5.882  -1.893  1.00 34.34  ? 941  LYS   B CE  1 
ATOM   3059 N  NZ  . LYS   B 1 89  ? 23.887  -7.233  -1.216  1.00 33.01  ? 941  LYS   B NZ  1 
ATOM   3060 N  N   . GLY   B 1 90  ? 28.130  -1.760  0.435   1.00 16.45  ? 942  GLY   B N   1 
ATOM   3061 C  CA  . GLY   B 1 90  ? 29.449  -1.280  0.079   1.00 16.42  ? 942  GLY   B CA  1 
ATOM   3062 C  C   . GLY   B 1 90  ? 29.524  0.167   -0.342  1.00 12.84  ? 942  GLY   B C   1 
ATOM   3063 O  O   . GLY   B 1 90  ? 28.623  0.976   -0.049  1.00 14.94  ? 942  GLY   B O   1 
ATOM   3064 N  N   . ILE   B 1 91  ? 30.590  0.461   -1.079  1.00 17.18  ? 943  ILE   B N   1 
ATOM   3065 C  CA  . ILE   B 1 91  ? 30.796  1.767   -1.712  1.00 19.09  ? 943  ILE   B CA  1 
ATOM   3066 C  C   . ILE   B 1 91  ? 31.188  1.624   -3.188  1.00 19.47  ? 943  ILE   B C   1 
ATOM   3067 O  O   . ILE   B 1 91  ? 31.670  0.582   -3.624  1.00 19.21  ? 943  ILE   B O   1 
ATOM   3068 C  CB  . ILE   B 1 91  ? 31.887  2.622   -0.996  1.00 21.66  ? 943  ILE   B CB  1 
ATOM   3069 C  CG1 . ILE   B 1 91  ? 33.217  1.864   -0.906  1.00 24.44  ? 943  ILE   B CG1 1 
ATOM   3070 C  CG2 . ILE   B 1 91  ? 31.396  3.051   0.408   1.00 18.93  ? 943  ILE   B CG2 1 
ATOM   3071 C  CD1 . ILE   B 1 91  ? 34.385  2.695   -0.335  1.00 26.99  ? 943  ILE   B CD1 1 
ATOM   3072 N  N   . CYS   B 1 92  ? 30.954  2.696   -3.928  1.00 19.04  ? 944  CYS   B N   1 
ATOM   3073 C  CA  . CYS   B 1 92  ? 31.494  2.886   -5.266  1.00 20.64  ? 944  CYS   B CA  1 
ATOM   3074 C  C   . CYS   B 1 92  ? 32.276  4.184   -5.228  1.00 23.14  ? 944  CYS   B C   1 
ATOM   3075 O  O   . CYS   B 1 92  ? 31.719  5.226   -4.870  1.00 24.37  ? 944  CYS   B O   1 
ATOM   3076 C  CB  . CYS   B 1 92  ? 30.372  2.959   -6.280  1.00 20.60  ? 944  CYS   B CB  1 
ATOM   3077 S  SG  . CYS   B 1 92  ? 30.939  3.330   -7.943  1.00 24.22  ? 944  CYS   B SG  1 
ATOM   3078 N  N   . THR   B 1 93  ? 33.571  4.110   -5.545  1.00 27.23  ? 945  THR   B N   1 
ATOM   3079 C  CA  . THR   B 1 93  ? 34.459  5.278   -5.460  1.00 30.82  ? 945  THR   B CA  1 
ATOM   3080 C  C   . THR   B 1 93  ? 34.874  5.704   -6.857  1.00 36.15  ? 945  THR   B C   1 
ATOM   3081 O  O   . THR   B 1 93  ? 35.468  4.912   -7.577  1.00 38.25  ? 945  THR   B O   1 
ATOM   3082 C  CB  . THR   B 1 93  ? 35.713  4.972   -4.617  1.00 35.34  ? 945  THR   B CB  1 
ATOM   3083 O  OG1 . THR   B 1 93  ? 36.367  3.799   -5.121  1.00 37.59  ? 945  THR   B OG1 1 
ATOM   3084 C  CG2 . THR   B 1 93  ? 35.326  4.738   -3.166  1.00 35.00  ? 945  THR   B CG2 1 
ATOM   3085 N  N   . ASN   B 1 98  ? 38.114  11.164  -5.095  1.00 51.64  ? 950  ASN   B N   1 
ATOM   3086 C  CA  . ASN   B 1 98  ? 37.381  11.955  -4.108  1.00 51.28  ? 950  ASN   B CA  1 
ATOM   3087 C  C   . ASN   B 1 98  ? 35.918  11.529  -3.948  1.00 48.22  ? 950  ASN   B C   1 
ATOM   3088 O  O   . ASN   B 1 98  ? 35.465  11.312  -2.825  1.00 49.69  ? 950  ASN   B O   1 
ATOM   3089 C  CB  . ASN   B 1 98  ? 37.467  13.450  -4.451  1.00 54.97  ? 950  ASN   B CB  1 
ATOM   3090 C  CG  . ASN   B 1 98  ? 38.892  13.980  -4.402  0.00 58.39  ? 950  ASN   B CG  1 
ATOM   3091 O  OD1 . ASN   B 1 98  ? 39.858  13.214  -4.400  0.00 58.85  ? 950  ASN   B OD1 1 
ATOM   3092 N  ND2 . ASN   B 1 98  ? 39.028  15.301  -4.369  0.00 61.43  ? 950  ASN   B ND2 1 
ATOM   3093 N  N   . GLY   B 1 99  ? 35.204  11.377  -5.068  1.00 45.31  ? 951  GLY   B N   1 
ATOM   3094 C  CA  . GLY   B 1 99  ? 33.763  11.079  -5.057  1.00 39.95  ? 951  GLY   B CA  1 
ATOM   3095 C  C   . GLY   B 1 99  ? 33.411  9.658   -4.624  1.00 36.56  ? 951  GLY   B C   1 
ATOM   3096 O  O   . GLY   B 1 99  ? 34.176  8.712   -4.880  1.00 35.30  ? 951  GLY   B O   1 
ATOM   3097 N  N   . ILE   B 1 100 ? 32.238  9.511   -3.998  1.00 28.38  ? 952  ILE   B N   1 
ATOM   3098 C  CA  . ILE   B 1 100 ? 31.820  8.246   -3.398  1.00 23.73  ? 952  ILE   B CA  1 
ATOM   3099 C  C   . ILE   B 1 100 ? 30.294  8.036   -3.450  1.00 21.30  ? 952  ILE   B C   1 
ATOM   3100 O  O   . ILE   B 1 100 ? 29.527  9.002   -3.434  1.00 21.29  ? 952  ILE   B O   1 
ATOM   3101 C  CB  . ILE   B 1 100 ? 32.339  8.156   -1.938  1.00 26.59  ? 952  ILE   B CB  1 
ATOM   3102 C  CG1 . ILE   B 1 100 ? 32.261  6.729   -1.397  1.00 25.09  ? 952  ILE   B CG1 1 
ATOM   3103 C  CG2 . ILE   B 1 100 ? 31.591  9.152   -0.995  1.00 27.28  ? 952  ILE   B CG2 1 
ATOM   3104 C  CD1 . ILE   B 1 100 ? 33.085  6.557   -0.123  1.00 27.79  ? 952  ILE   B CD1 1 
ATOM   3105 N  N   . LYS   B 1 101 ? 29.871  6.772   -3.494  1.00 18.53  ? 953  LYS   B N   1 
ATOM   3106 C  CA  . LYS   B 1 101 ? 28.452  6.389   -3.455  1.00 16.35  ? 953  LYS   B CA  1 
ATOM   3107 C  C   . LYS   B 1 101 ? 28.267  5.306   -2.419  1.00 16.34  ? 953  LYS   B C   1 
ATOM   3108 O  O   . LYS   B 1 101 ? 29.097  4.413   -2.303  1.00 17.67  ? 953  LYS   B O   1 
ATOM   3109 C  CB  . LYS   B 1 101 ? 27.922  5.911   -4.824  1.00 16.79  ? 953  LYS   B CB  1 
ATOM   3110 C  CG  . LYS   B 1 101 ? 28.104  6.916   -5.973  1.00 25.32  ? 953  LYS   B CG  1 
ATOM   3111 C  CD  . LYS   B 1 101 ? 27.676  6.296   -7.308  1.00 24.64  ? 953  LYS   B CD  1 
ATOM   3112 C  CE  . LYS   B 1 101 ? 28.023  7.180   -8.480  1.00 28.67  ? 953  LYS   B CE  1 
ATOM   3113 N  NZ  . LYS   B 1 101 ? 27.065  8.290   -8.705  1.00 24.72  ? 953  LYS   B NZ  1 
ATOM   3114 N  N   . LEU   B 1 102 ? 27.179  5.394   -1.665  1.00 15.88  ? 954  LEU   B N   1 
ATOM   3115 C  CA  . LEU   B 1 102 ? 26.836  4.396   -0.641  1.00 15.13  ? 954  LEU   B CA  1 
ATOM   3116 C  C   . LEU   B 1 102 ? 25.915  3.344   -1.267  1.00 15.53  ? 954  LEU   B C   1 
ATOM   3117 O  O   . LEU   B 1 102 ? 24.880  3.705   -1.845  1.00 16.26  ? 954  LEU   B O   1 
ATOM   3118 C  CB  . LEU   B 1 102 ? 26.104  5.090   0.506   1.00 14.00  ? 954  LEU   B CB  1 
ATOM   3119 C  CG  . LEU   B 1 102 ? 25.339  4.223   1.505   1.00 12.37  ? 954  LEU   B CG  1 
ATOM   3120 C  CD1 . LEU   B 1 102 ? 26.275  3.194   2.184   1.00 14.69  ? 954  LEU   B CD1 1 
ATOM   3121 C  CD2 . LEU   B 1 102 ? 24.675  5.136   2.499   1.00 13.86  ? 954  LEU   B CD2 1 
ATOM   3122 N  N   . ILE   B 1 103 ? 26.276  2.067   -1.159  1.00 14.66  ? 955  ILE   B N   1 
ATOM   3123 C  CA  . ILE   B 1 103 ? 25.482  0.975   -1.746  1.00 14.44  ? 955  ILE   B CA  1 
ATOM   3124 C  C   . ILE   B 1 103 ? 24.787  0.213   -0.585  1.00 15.16  ? 955  ILE   B C   1 
ATOM   3125 O  O   . ILE   B 1 103 ? 25.452  -0.223  0.350   1.00 13.65  ? 955  ILE   B O   1 
ATOM   3126 C  CB  . ILE   B 1 103 ? 26.347  -0.030  -2.545  1.00 14.42  ? 955  ILE   B CB  1 
ATOM   3127 C  CG1 . ILE   B 1 103 ? 27.377  0.675   -3.461  1.00 15.99  ? 955  ILE   B CG1 1 
ATOM   3128 C  CG2 . ILE   B 1 103 ? 25.432  -0.991  -3.383  1.00 14.34  ? 955  ILE   B CG2 1 
ATOM   3129 C  CD1 . ILE   B 1 103 ? 26.804  1.649   -4.451  1.00 16.97  ? 955  ILE   B CD1 1 
ATOM   3130 N  N   . MET   B 1 104 ? 23.468  0.082   -0.664  1.00 12.49  ? 956  MET   B N   1 
ATOM   3131 C  CA  . MET   B 1 104 ? 22.639  -0.575  0.327   1.00 13.15  ? 956  MET   B CA  1 
ATOM   3132 C  C   . MET   B 1 104 ? 21.779  -1.642  -0.292  1.00 15.09  ? 956  MET   B C   1 
ATOM   3133 O  O   . MET   B 1 104 ? 21.568  -1.635  -1.514  1.00 13.38  ? 956  MET   B O   1 
ATOM   3134 C  CB  . MET   B 1 104 ? 21.722  0.455   1.023   1.00 14.60  ? 956  MET   B CB  1 
ATOM   3135 C  CG  . MET   B 1 104 ? 22.469  1.478   1.888   1.00 13.08  ? 956  MET   B CG  1 
ATOM   3136 S  SD  . MET   B 1 104 ? 21.490  2.939   2.313   1.00 14.34  ? 956  MET   B SD  1 
ATOM   3137 C  CE  . MET   B 1 104 ? 21.459  3.788   0.705   1.00 14.77  ? 956  MET   B CE  1 
ATOM   3138 N  N   . GLU   B 1 105 ? 21.252  -2.554  0.527   1.00 15.56  ? 957  GLU   B N   1 
ATOM   3139 C  CA  . GLU   B 1 105 ? 20.222  -3.452  0.019   1.00 16.42  ? 957  GLU   B CA  1 
ATOM   3140 C  C   . GLU   B 1 105 ? 19.040  -2.617  -0.490  1.00 17.82  ? 957  GLU   B C   1 
ATOM   3141 O  O   . GLU   B 1 105 ? 18.815  -1.495  -0.007  1.00 12.53  ? 957  GLU   B O   1 
ATOM   3142 C  CB  . GLU   B 1 105 ? 19.749  -4.446  1.057   1.00 17.45  ? 957  GLU   B CB  1 
ATOM   3143 C  CG  . GLU   B 1 105 ? 19.129  -3.801  2.285   1.00 15.64  ? 957  GLU   B CG  1 
ATOM   3144 C  CD  . GLU   B 1 105 ? 18.650  -4.792  3.311   1.00 14.55  ? 957  GLU   B CD  1 
ATOM   3145 O  OE1 . GLU   B 1 105 ? 18.553  -5.990  3.006   1.00 17.97  ? 957  GLU   B OE1 1 
ATOM   3146 O  OE2 . GLU   B 1 105 ? 18.405  -4.357  4.466   1.00 16.11  ? 957  GLU   B OE2 1 
ATOM   3147 N  N   . PHE   B 1 106 ? 18.314  -3.176  -1.451  1.00 16.45  ? 958  PHE   B N   1 
ATOM   3148 C  CA  . PHE   B 1 106 ? 17.068  -2.584  -1.962  1.00 12.79  ? 958  PHE   B CA  1 
ATOM   3149 C  C   . PHE   B 1 106 ? 15.836  -3.260  -1.405  1.00 13.98  ? 958  PHE   B C   1 
ATOM   3150 O  O   . PHE   B 1 106 ? 15.707  -4.516  -1.472  1.00 14.22  ? 958  PHE   B O   1 
ATOM   3151 C  CB  . PHE   B 1 106 ? 17.059  -2.606  -3.491  1.00 16.67  ? 958  PHE   B CB  1 
ATOM   3152 C  CG  . PHE   B 1 106 ? 15.755  -2.139  -4.095  1.00 12.37  ? 958  PHE   B CG  1 
ATOM   3153 C  CD1 . PHE   B 1 106 ? 15.266  -0.870  -3.802  1.00 17.97  ? 958  PHE   B CD1 1 
ATOM   3154 C  CD2 . PHE   B 1 106 ? 15.040  -2.955  -4.991  1.00 13.30  ? 958  PHE   B CD2 1 
ATOM   3155 C  CE1 . PHE   B 1 106 ? 14.032  -0.431  -4.320  1.00 17.14  ? 958  PHE   B CE1 1 
ATOM   3156 C  CE2 . PHE   B 1 106 ? 13.814  -2.525  -5.509  1.00 17.33  ? 958  PHE   B CE2 1 
ATOM   3157 C  CZ  . PHE   B 1 106 ? 13.324  -1.245  -5.192  1.00 19.31  ? 958  PHE   B CZ  1 
ATOM   3158 N  N   . LEU   B 1 107 ? 14.918  -2.447  -0.858  1.00 14.58  ? 959  LEU   B N   1 
ATOM   3159 C  CA  . LEU   B 1 107 ? 13.653  -2.955  -0.292  1.00 17.12  ? 959  LEU   B CA  1 
ATOM   3160 C  C   . LEU   B 1 107 ? 12.479  -2.494  -1.200  1.00 18.96  ? 959  LEU   B C   1 
ATOM   3161 O  O   . LEU   B 1 107 ? 11.998  -1.378  -1.036  1.00 13.70  ? 959  LEU   B O   1 
ATOM   3162 C  CB  . LEU   B 1 107 ? 13.444  -2.502  1.159   1.00 16.27  ? 959  LEU   B CB  1 
ATOM   3163 C  CG  . LEU   B 1 107 ? 14.097  -3.328  2.284   1.00 15.98  ? 959  LEU   B CG  1 
ATOM   3164 C  CD1 . LEU   B 1 107 ? 15.597  -3.439  2.177   1.00 16.14  ? 959  LEU   B CD1 1 
ATOM   3165 C  CD2 . LEU   B 1 107 ? 13.738  -2.744  3.657   1.00 15.48  ? 959  LEU   B CD2 1 
ATOM   3166 N  N   . PRO   B 1 108 ? 12.025  -3.367  -2.136  1.00 17.90  ? 960  PRO   B N   1 
ATOM   3167 C  CA  . PRO   B 1 108 ? 10.992  -3.017  -3.164  1.00 19.09  ? 960  PRO   B CA  1 
ATOM   3168 C  C   . PRO   B 1 108 ? 9.669   -2.473  -2.645  1.00 17.41  ? 960  PRO   B C   1 
ATOM   3169 O  O   . PRO   B 1 108 ? 9.009   -1.686  -3.344  1.00 20.35  ? 960  PRO   B O   1 
ATOM   3170 C  CB  . PRO   B 1 108 ? 10.772  -4.327  -3.931  1.00 20.48  ? 960  PRO   B CB  1 
ATOM   3171 C  CG  . PRO   B 1 108 ? 11.567  -5.350  -3.283  1.00 25.23  ? 960  PRO   B CG  1 
ATOM   3172 C  CD  . PRO   B 1 108 ? 12.469  -4.765  -2.257  1.00 19.61  ? 960  PRO   B CD  1 
ATOM   3173 N  N   . SER   B 1 109 ? 9.281   -2.851  -1.420  1.00 21.37  ? 961  SER   B N   1 
ATOM   3174 C  CA  . SER   B 1 109 ? 8.069   -2.292  -0.798  1.00 21.19  ? 961  SER   B CA  1 
ATOM   3175 C  C   . SER   B 1 109 ? 8.149   -0.815  -0.422  1.00 20.59  ? 961  SER   B C   1 
ATOM   3176 O  O   . SER   B 1 109 ? 7.126   -0.196  -0.194  1.00 20.12  ? 961  SER   B O   1 
ATOM   3177 C  CB  . SER   B 1 109 ? 7.657   -3.105  0.443   1.00 19.22  ? 961  SER   B CB  1 
ATOM   3178 O  OG  . SER   B 1 109 ? 7.220   -4.390  0.069   1.00 22.32  ? 961  SER   B OG  1 
ATOM   3179 N  N   . GLY   B 1 110 ? 9.361   -0.258  -0.321  1.00 17.11  ? 962  GLY   B N   1 
ATOM   3180 C  CA  . GLY   B 1 110 ? 9.545   1.164   -0.117  1.00 19.97  ? 962  GLY   B CA  1 
ATOM   3181 C  C   . GLY   B 1 110 ? 9.246   1.601   1.301   1.00 16.68  ? 962  GLY   B C   1 
ATOM   3182 O  O   . GLY   B 1 110 ? 9.244   0.785   2.212   1.00 17.27  ? 962  GLY   B O   1 
ATOM   3183 N  N   . SER   B 1 111 ? 8.947   2.894   1.450   1.00 18.77  ? 963  SER   B N   1 
ATOM   3184 C  CA  . SER   B 1 111 ? 8.696   3.487   2.751   1.00 14.15  ? 963  SER   B CA  1 
ATOM   3185 C  C   . SER   B 1 111 ? 7.307   3.174   3.262   1.00 17.98  ? 963  SER   B C   1 
ATOM   3186 O  O   . SER   B 1 111 ? 6.402   2.838   2.496   1.00 17.63  ? 963  SER   B O   1 
ATOM   3187 C  CB  . SER   B 1 111 ? 8.915   5.011   2.759   1.00 16.86  ? 963  SER   B CB  1 
ATOM   3188 O  OG  . SER   B 1 111 ? 7.790   5.746   2.327   1.00 23.46  ? 963  SER   B OG  1 
ATOM   3189 N  N   . LEU   B 1 112 ? 7.157   3.309   4.582   1.00 16.77  ? 964  LEU   B N   1 
ATOM   3190 C  CA  . LEU   B 1 112 ? 5.825   3.247   5.215   1.00 18.05  ? 964  LEU   B CA  1 
ATOM   3191 C  C   . LEU   B 1 112 ? 4.891   4.322   4.712   1.00 20.99  ? 964  LEU   B C   1 
ATOM   3192 O  O   . LEU   B 1 112 ? 3.683   4.103   4.663   1.00 18.10  ? 964  LEU   B O   1 
ATOM   3193 C  CB  . LEU   B 1 112 ? 5.929   3.406   6.735   1.00 19.25  ? 964  LEU   B CB  1 
ATOM   3194 C  CG  . LEU   B 1 112 ? 6.404   2.271   7.621   1.00 19.55  ? 964  LEU   B CG  1 
ATOM   3195 C  CD1 . LEU   B 1 112 ? 6.456   2.785   9.040   1.00 22.03  ? 964  LEU   B CD1 1 
ATOM   3196 C  CD2 . LEU   B 1 112 ? 5.474   1.057   7.506   1.00 19.42  ? 964  LEU   B CD2 1 
ATOM   3197 N  N   A LYS   B 1 113 ? 5.436   5.489   4.352   0.50 23.17  ? 965  LYS   B N   1 
ATOM   3198 N  N   B LYS   B 1 113 ? 5.440   5.480   4.346   0.50 22.95  ? 965  LYS   B N   1 
ATOM   3199 C  CA  A LYS   B 1 113 ? 4.636   6.554   3.719   0.50 26.22  ? 965  LYS   B CA  1 
ATOM   3200 C  CA  B LYS   B 1 113 ? 4.638   6.547   3.733   0.50 25.76  ? 965  LYS   B CA  1 
ATOM   3201 C  C   A LYS   B 1 113 ? 3.939   6.054   2.450   0.50 26.75  ? 965  LYS   B C   1 
ATOM   3202 C  C   B LYS   B 1 113 ? 3.947   6.067   2.447   0.50 26.53  ? 965  LYS   B C   1 
ATOM   3203 O  O   A LYS   B 1 113 ? 2.783   6.400   2.206   0.50 28.50  ? 965  LYS   B O   1 
ATOM   3204 O  O   B LYS   B 1 113 ? 2.802   6.438   2.189   0.50 28.21  ? 965  LYS   B O   1 
ATOM   3205 C  CB  A LYS   B 1 113 ? 5.501   7.796   3.417   0.50 27.77  ? 965  LYS   B CB  1 
ATOM   3206 C  CB  B LYS   B 1 113 ? 5.494   7.795   3.469   0.50 27.14  ? 965  LYS   B CB  1 
ATOM   3207 C  CG  A LYS   B 1 113 ? 4.768   9.005   2.834   0.50 32.31  ? 965  LYS   B CG  1 
ATOM   3208 C  CG  B LYS   B 1 113 ? 4.726   9.093   3.527   0.50 29.70  ? 965  LYS   B CG  1 
ATOM   3209 C  CD  A LYS   B 1 113 ? 3.644   9.474   3.735   0.50 29.32  ? 965  LYS   B CD  1 
ATOM   3210 C  CD  B LYS   B 1 113 ? 5.654   10.294  3.365   0.50 26.34  ? 965  LYS   B CD  1 
ATOM   3211 C  CE  A LYS   B 1 113 ? 3.087   10.821  3.342   0.50 28.75  ? 965  LYS   B CE  1 
ATOM   3212 C  CE  B LYS   B 1 113 ? 4.913   11.511  2.838   0.50 33.72  ? 965  LYS   B CE  1 
ATOM   3213 N  NZ  A LYS   B 1 113 ? 1.729   10.995  3.950   0.50 24.48  ? 965  LYS   B NZ  1 
ATOM   3214 N  NZ  B LYS   B 1 113 ? 5.822   12.666  2.622   0.00 33.71  ? 965  LYS   B NZ  1 
ATOM   3215 N  N   . GLU   B 1 114 ? 4.640   5.239   1.661   1.00 25.94  ? 966  GLU   B N   1 
ATOM   3216 C  CA  . GLU   B 1 114 ? 4.077   4.636   0.431   1.00 29.77  ? 966  GLU   B CA  1 
ATOM   3217 C  C   . GLU   B 1 114 ? 3.237   3.377   0.701   1.00 28.74  ? 966  GLU   B C   1 
ATOM   3218 O  O   . GLU   B 1 114 ? 2.190   3.197   0.112   1.00 27.96  ? 966  GLU   B O   1 
ATOM   3219 C  CB  . GLU   B 1 114 ? 5.178   4.251   -0.565  1.00 33.55  ? 966  GLU   B CB  1 
ATOM   3220 C  CG  . GLU   B 1 114 ? 4.615   3.614   -1.875  1.00 42.82  ? 966  GLU   B CG  1 
ATOM   3221 C  CD  . GLU   B 1 114 ? 5.669   3.268   -2.923  1.00 57.19  ? 966  GLU   B CD  1 
ATOM   3222 O  OE1 . GLU   B 1 114 ? 6.833   3.698   -2.798  1.00 58.96  ? 966  GLU   B OE1 1 
ATOM   3223 O  OE2 . GLU   B 1 114 ? 5.316   2.559   -3.893  1.00 63.19  ? 966  GLU   B OE2 1 
ATOM   3224 N  N   . TYR   B 1 115 ? 3.729   2.516   1.578   1.00 23.21  ? 967  TYR   B N   1 
ATOM   3225 C  CA  . TYR   B 1 115 ? 3.198   1.164   1.760   1.00 24.30  ? 967  TYR   B CA  1 
ATOM   3226 C  C   . TYR   B 1 115 ? 1.900   1.118   2.556   1.00 21.39  ? 967  TYR   B C   1 
ATOM   3227 O  O   . TYR   B 1 115 ? 0.998   0.349   2.215   1.00 24.30  ? 967  TYR   B O   1 
ATOM   3228 C  CB  . TYR   B 1 115 ? 4.269   0.290   2.443   1.00 19.79  ? 967  TYR   B CB  1 
ATOM   3229 C  CG  . TYR   B 1 115 ? 3.867   -1.136  2.744   1.00 22.34  ? 967  TYR   B CG  1 
ATOM   3230 C  CD1 . TYR   B 1 115 ? 4.040   -2.152  1.800   1.00 22.58  ? 967  TYR   B CD1 1 
ATOM   3231 C  CD2 . TYR   B 1 115 ? 3.331   -1.474  3.980   1.00 19.02  ? 967  TYR   B CD2 1 
ATOM   3232 C  CE1 . TYR   B 1 115 ? 3.678   -3.475  2.081   1.00 22.59  ? 967  TYR   B CE1 1 
ATOM   3233 C  CE2 . TYR   B 1 115 ? 2.962   -2.785  4.274   1.00 19.48  ? 967  TYR   B CE2 1 
ATOM   3234 C  CZ  . TYR   B 1 115 ? 3.128   -3.777  3.325   1.00 19.91  ? 967  TYR   B CZ  1 
ATOM   3235 O  OH  . TYR   B 1 115 ? 2.795   -5.074  3.641   1.00 25.76  ? 967  TYR   B OH  1 
ATOM   3236 N  N   . LEU   B 1 116 ? 1.806   1.915   3.619   1.00 21.65  ? 968  LEU   B N   1 
ATOM   3237 C  CA  . LEU   B 1 116 ? 0.639   1.851   4.514   1.00 21.78  ? 968  LEU   B CA  1 
ATOM   3238 C  C   . LEU   B 1 116 ? -0.703  2.210   3.845   1.00 24.08  ? 968  LEU   B C   1 
ATOM   3239 O  O   . LEU   B 1 116 ? -1.690  1.480   4.004   1.00 25.98  ? 968  LEU   B O   1 
ATOM   3240 C  CB  . LEU   B 1 116 ? 0.878   2.670   5.798   1.00 17.93  ? 968  LEU   B CB  1 
ATOM   3241 C  CG  . LEU   B 1 116 ? 1.902   2.120   6.800   1.00 21.50  ? 968  LEU   B CG  1 
ATOM   3242 C  CD1 . LEU   B 1 116 ? 2.054   3.069   7.954   1.00 22.96  ? 968  LEU   B CD1 1 
ATOM   3243 C  CD2 . LEU   B 1 116 ? 1.540   0.741   7.329   1.00 19.92  ? 968  LEU   B CD2 1 
ATOM   3244 N  N   . PRO   B 1 117 ? -0.754  3.314   3.064   1.00 24.63  ? 969  PRO   B N   1 
ATOM   3245 C  CA  . PRO   B 1 117 ? -2.034  3.641   2.401   1.00 29.65  ? 969  PRO   B CA  1 
ATOM   3246 C  C   . PRO   B 1 117 ? -2.548  2.553   1.445   1.00 26.18  ? 969  PRO   B C   1 
ATOM   3247 O  O   . PRO   B 1 117 ? -3.757  2.399   1.273   1.00 30.09  ? 969  PRO   B O   1 
ATOM   3248 C  CB  . PRO   B 1 117 ? -1.721  4.944   1.651   1.00 31.21  ? 969  PRO   B CB  1 
ATOM   3249 C  CG  . PRO   B 1 117 ? -0.500  5.501   2.333   1.00 28.75  ? 969  PRO   B CG  1 
ATOM   3250 C  CD  . PRO   B 1 117 ? 0.284   4.336   2.811   1.00 28.37  ? 969  PRO   B CD  1 
ATOM   3251 N  N   . LYS   B 1 118 ? -1.615  1.802   0.853   1.00 28.07  ? 970  LYS   B N   1 
ATOM   3252 C  CA  . LYS   B 1 118 ? -1.923  0.709   -0.065  1.00 32.22  ? 970  LYS   B CA  1 
ATOM   3253 C  C   . LYS   B 1 118 ? -2.168  -0.642  0.599   1.00 29.89  ? 970  LYS   B C   1 
ATOM   3254 O  O   . LYS   B 1 118 ? -2.559  -1.576  -0.089  1.00 32.18  ? 970  LYS   B O   1 
ATOM   3255 C  CB  . LYS   B 1 118 ? -0.798  0.565   -1.086  1.00 35.96  ? 970  LYS   B CB  1 
ATOM   3256 C  CG  . LYS   B 1 118 ? -0.602  1.825   -1.916  1.00 41.64  ? 970  LYS   B CG  1 
ATOM   3257 C  CD  . LYS   B 1 118 ? 0.170   1.570   -3.205  1.00 50.69  ? 970  LYS   B CD  1 
ATOM   3258 C  CE  . LYS   B 1 118 ? 1.677   1.565   -3.011  1.00 49.36  ? 970  LYS   B CE  1 
ATOM   3259 N  NZ  . LYS   B 1 118 ? 2.353   1.840   -4.317  1.00 50.63  ? 970  LYS   B NZ  1 
ATOM   3260 N  N   . ASN   B 1 119 ? -1.967  -0.747  1.916   1.00 26.98  ? 971  ASN   B N   1 
ATOM   3261 C  CA  . ASN   B 1 119 ? -2.017  -2.046  2.631   1.00 25.14  ? 971  ASN   B CA  1 
ATOM   3262 C  C   . ASN   B 1 119 ? -2.801  -2.014  3.970   1.00 26.06  ? 971  ASN   B C   1 
ATOM   3263 O  O   . ASN   B 1 119 ? -2.685  -2.930  4.782   1.00 26.52  ? 971  ASN   B O   1 
ATOM   3264 C  CB  . ASN   B 1 119 ? -0.567  -2.600  2.798   1.00 23.29  ? 971  ASN   B CB  1 
ATOM   3265 C  CG  . ASN   B 1 119 ? 0.076   -3.033  1.445   1.00 29.36  ? 971  ASN   B CG  1 
ATOM   3266 O  OD1 . ASN   B 1 119 ? -0.229  -4.109  0.930   1.00 24.26  ? 971  ASN   B OD1 1 
ATOM   3267 N  ND2 . ASN   B 1 119 ? 0.943   -2.191  0.876   1.00 21.06  ? 971  ASN   B ND2 1 
ATOM   3268 N  N   . LYS   B 1 120 ? -3.653  -1.005  4.178   1.00 26.50  ? 972  LYS   B N   1 
ATOM   3269 C  CA  . LYS   B 1 120 ? -4.451  -0.882  5.423   1.00 28.75  ? 972  LYS   B CA  1 
ATOM   3270 C  C   . LYS   B 1 120 ? -5.173  -2.187  5.792   1.00 26.32  ? 972  LYS   B C   1 
ATOM   3271 O  O   . LYS   B 1 120 ? -5.210  -2.564  6.966   1.00 30.04  ? 972  LYS   B O   1 
ATOM   3272 C  CB  . LYS   B 1 120 ? -5.534  0.221   5.322   1.00 29.45  ? 972  LYS   B CB  1 
ATOM   3273 C  CG  . LYS   B 1 120 ? -5.005  1.629   5.151   1.00 33.03  ? 972  LYS   B CG  1 
ATOM   3274 C  CD  . LYS   B 1 120 ? -5.953  2.720   5.721   1.00 27.57  ? 972  LYS   B CD  1 
ATOM   3275 C  CE  . LYS   B 1 120 ? -7.223  2.844   4.953   1.00 36.57  ? 972  LYS   B CE  1 
ATOM   3276 N  NZ  . LYS   B 1 120 ? -7.890  4.186   5.213   1.00 48.06  ? 972  LYS   B NZ  1 
ATOM   3277 N  N   . ASN   B 1 121 ? -5.760  -2.859  4.808   1.00 26.55  ? 973  ASN   B N   1 
ATOM   3278 C  CA  . ASN   B 1 121 ? -6.503  -4.106  5.074   1.00 31.41  ? 973  ASN   B CA  1 
ATOM   3279 C  C   . ASN   B 1 121 ? -5.622  -5.253  5.613   1.00 32.21  ? 973  ASN   B C   1 
ATOM   3280 O  O   . ASN   B 1 121 ? -6.088  -6.048  6.427   1.00 32.21  ? 973  ASN   B O   1 
ATOM   3281 C  CB  . ASN   B 1 121 ? -7.245  -4.588  3.839   1.00 32.30  ? 973  ASN   B CB  1 
ATOM   3282 C  CG  . ASN   B 1 121 ? -8.300  -5.664  4.158   1.00 38.24  ? 973  ASN   B CG  1 
ATOM   3283 O  OD1 . ASN   B 1 121 ? -9.161  -5.473  5.016   1.00 30.03  ? 973  ASN   B OD1 1 
ATOM   3284 N  ND2 . ASN   B 1 121 ? -8.233  -6.788  3.455   1.00 30.94  ? 973  ASN   B ND2 1 
ATOM   3285 N  N   . LYS   B 1 122 ? -4.386  -5.335  5.118   1.00 30.75  ? 974  LYS   B N   1 
ATOM   3286 C  CA  . LYS   B 1 122 ? -3.341  -6.266  5.620   1.00 33.77  ? 974  LYS   B CA  1 
ATOM   3287 C  C   . LYS   B 1 122 ? -2.839  -5.937  7.010   1.00 31.34  ? 974  LYS   B C   1 
ATOM   3288 O  O   . LYS   B 1 122 ? -2.535  -6.842  7.786   1.00 32.98  ? 974  LYS   B O   1 
ATOM   3289 C  CB  . LYS   B 1 122 ? -2.076  -6.227  4.733   1.00 33.77  ? 974  LYS   B CB  1 
ATOM   3290 C  CG  . LYS   B 1 122 ? -2.077  -7.122  3.530   1.00 40.56  ? 974  LYS   B CG  1 
ATOM   3291 C  CD  . LYS   B 1 122 ? -0.740  -6.996  2.806   1.00 39.67  ? 974  LYS   B CD  1 
ATOM   3292 C  CE  . LYS   B 1 122 ? -0.782  -7.561  1.404   1.00 44.53  ? 974  LYS   B CE  1 
ATOM   3293 N  NZ  . LYS   B 1 122 ? -1.685  -6.774  0.491   1.00 56.54  ? 974  LYS   B NZ  1 
ATOM   3294 N  N   . ILE   B 1 123 ? -2.671  -4.640  7.279   1.00 28.76  ? 975  ILE   B N   1 
ATOM   3295 C  CA  . ILE   B 1 123 ? -1.938  -4.144  8.438   1.00 26.38  ? 975  ILE   B CA  1 
ATOM   3296 C  C   . ILE   B 1 123 ? -2.948  -3.676  9.480   1.00 27.30  ? 975  ILE   B C   1 
ATOM   3297 O  O   . ILE   B 1 123 ? -3.464  -2.565  9.387   1.00 29.88  ? 975  ILE   B O   1 
ATOM   3298 C  CB  . ILE   B 1 123 ? -0.939  -2.993  8.048   1.00 26.69  ? 975  ILE   B CB  1 
ATOM   3299 C  CG1 . ILE   B 1 123 ? -0.022  -3.403  6.879   1.00 24.78  ? 975  ILE   B CG1 1 
ATOM   3300 C  CG2 . ILE   B 1 123 ? -0.108  -2.555  9.230   1.00 29.30  ? 975  ILE   B CG2 1 
ATOM   3301 C  CD1 . ILE   B 1 123 ? 0.691   -4.744  7.022   1.00 30.05  ? 975  ILE   B CD1 1 
ATOM   3302 N  N   . ASN   B 1 124 ? -3.232  -4.552  10.452  1.00 22.56  ? 976  ASN   B N   1 
ATOM   3303 C  CA  . ASN   B 1 124 ? -4.109  -4.246  11.595  1.00 23.34  ? 976  ASN   B CA  1 
ATOM   3304 C  C   . ASN   B 1 124 ? -3.327  -3.681  12.779  1.00 22.86  ? 976  ASN   B C   1 
ATOM   3305 O  O   . ASN   B 1 124 ? -2.107  -3.539  12.702  1.00 20.32  ? 976  ASN   B O   1 
ATOM   3306 C  CB  . ASN   B 1 124 ? -4.934  -5.479  11.990  1.00 24.82  ? 976  ASN   B CB  1 
ATOM   3307 C  CG  . ASN   B 1 124 ? -4.088  -6.642  12.501  1.00 25.43  ? 976  ASN   B CG  1 
ATOM   3308 O  OD1 . ASN   B 1 124 ? -2.920  -6.485  12.847  1.00 21.24  ? 976  ASN   B OD1 1 
ATOM   3309 N  ND2 . ASN   B 1 124 ? -4.679  -7.832  12.511  1.00 27.00  ? 976  ASN   B ND2 1 
ATOM   3310 N  N   . LEU   B 1 125 ? -4.030  -3.355  13.866  1.00 23.21  ? 977  LEU   B N   1 
ATOM   3311 C  CA  . LEU   B 1 125 ? -3.400  -2.767  15.067  1.00 22.05  ? 977  LEU   B CA  1 
ATOM   3312 C  C   . LEU   B 1 125 ? -2.217  -3.604  15.602  1.00 21.15  ? 977  LEU   B C   1 
ATOM   3313 O  O   . LEU   B 1 125 ? -1.141  -3.079  15.879  1.00 19.06  ? 977  LEU   B O   1 
ATOM   3314 C  CB  . LEU   B 1 125 ? -4.456  -2.509  16.150  1.00 21.91  ? 977  LEU   B CB  1 
ATOM   3315 C  CG  . LEU   B 1 125 ? -3.948  -2.005  17.517  1.00 25.31  ? 977  LEU   B CG  1 
ATOM   3316 C  CD1 . LEU   B 1 125 ? -3.142  -0.701  17.385  1.00 25.97  ? 977  LEU   B CD1 1 
ATOM   3317 C  CD2 . LEU   B 1 125 ? -5.115  -1.855  18.465  1.00 32.16  ? 977  LEU   B CD2 1 
ATOM   3318 N  N   . LYS   B 1 126 ? -2.430  -4.906  15.711  1.00 21.77  ? 978  LYS   B N   1 
ATOM   3319 C  CA  . LYS   B 1 126 ? -1.372  -5.847  16.102  1.00 21.26  ? 978  LYS   B CA  1 
ATOM   3320 C  C   . LYS   B 1 126 ? -0.086  -5.674  15.251  1.00 19.82  ? 978  LYS   B C   1 
ATOM   3321 O  O   . LYS   B 1 126 ? 1.025   -5.545  15.785  1.00 15.75  ? 978  LYS   B O   1 
ATOM   3322 C  CB  . LYS   B 1 126 ? -1.916  -7.287  16.067  1.00 26.62  ? 978  LYS   B CB  1 
ATOM   3323 C  CG  . LYS   B 1 126 ? -1.026  -8.284  16.763  1.00 29.79  ? 978  LYS   B CG  1 
ATOM   3324 C  CD  . LYS   B 1 126 ? -1.786  -9.538  17.207  1.00 36.83  ? 978  LYS   B CD  1 
ATOM   3325 C  CE  . LYS   B 1 126 ? -1.083  -10.243 18.374  1.00 40.56  ? 978  LYS   B CE  1 
ATOM   3326 N  NZ  . LYS   B 1 126 ? -2.066  -10.980 19.220  1.00 47.55  ? 978  LYS   B NZ  1 
ATOM   3327 N  N   . GLN   B 1 127 ? -0.246  -5.621  13.929  1.00 18.59  ? 979  GLN   B N   1 
ATOM   3328 C  CA  . GLN   B 1 127 ? 0.883   -5.416  13.039  1.00 17.80  ? 979  GLN   B CA  1 
ATOM   3329 C  C   . GLN   B 1 127 ? 1.508   -4.025  13.162  1.00 16.20  ? 979  GLN   B C   1 
ATOM   3330 O  O   . GLN   B 1 127 ? 2.720   -3.898  13.052  1.00 16.38  ? 979  GLN   B O   1 
ATOM   3331 C  CB  . GLN   B 1 127 ? 0.532   -5.716  11.563  1.00 16.97  ? 979  GLN   B CB  1 
ATOM   3332 C  CG  . GLN   B 1 127 ? 1.778   -5.830  10.684  1.00 18.50  ? 979  GLN   B CG  1 
ATOM   3333 C  CD  . GLN   B 1 127 ? 2.734   -6.907  11.160  1.00 15.53  ? 979  GLN   B CD  1 
ATOM   3334 O  OE1 . GLN   B 1 127 ? 2.408   -8.089  11.095  1.00 19.00  ? 979  GLN   B OE1 1 
ATOM   3335 N  NE2 . GLN   B 1 127 ? 3.904   -6.503  11.661  1.00 16.71  ? 979  GLN   B NE2 1 
ATOM   3336 N  N   . GLN   B 1 128 ? 0.688   -2.989  13.389  1.00 14.50  ? 980  GLN   B N   1 
ATOM   3337 C  CA  . GLN   B 1 128 ? 1.215   -1.648  13.637  1.00 15.57  ? 980  GLN   B CA  1 
ATOM   3338 C  C   . GLN   B 1 128 ? 2.085   -1.609  14.922  1.00 16.16  ? 980  GLN   B C   1 
ATOM   3339 O  O   . GLN   B 1 128 ? 3.159   -1.012  14.949  1.00 14.61  ? 980  GLN   B O   1 
ATOM   3340 C  CB  . GLN   B 1 128 ? 0.057   -0.632  13.734  1.00 19.21  ? 980  GLN   B CB  1 
ATOM   3341 C  CG  . GLN   B 1 128 ? -0.697  -0.408  12.418  1.00 17.79  ? 980  GLN   B CG  1 
ATOM   3342 C  CD  . GLN   B 1 128 ? -1.973  0.412   12.614  1.00 19.79  ? 980  GLN   B CD  1 
ATOM   3343 O  OE1 . GLN   B 1 128 ? -2.827  0.067   13.429  1.00 25.92  ? 980  GLN   B OE1 1 
ATOM   3344 N  NE2 . GLN   B 1 128 ? -2.122  1.469   11.844  1.00 23.91  ? 980  GLN   B NE2 1 
ATOM   3345 N  N   . LEU   B 1 129 ? 1.613   -2.264  15.972  1.00 16.94  ? 981  LEU   B N   1 
ATOM   3346 C  CA  . LEU   B 1 129 ? 2.356   -2.309  17.251  1.00 18.06  ? 981  LEU   B CA  1 
ATOM   3347 C  C   . LEU   B 1 129 ? 3.676   -3.096  17.103  1.00 17.24  ? 981  LEU   B C   1 
ATOM   3348 O  O   . LEU   B 1 129 ? 4.714   -2.696  17.643  1.00 15.23  ? 981  LEU   B O   1 
ATOM   3349 C  CB  . LEU   B 1 129 ? 1.465   -2.875  18.342  1.00 19.25  ? 981  LEU   B CB  1 
ATOM   3350 C  CG  . LEU   B 1 129 ? 0.266   -2.003  18.736  1.00 20.64  ? 981  LEU   B CG  1 
ATOM   3351 C  CD1 . LEU   B 1 129 ? -0.435  -2.685  19.889  1.00 27.60  ? 981  LEU   B CD1 1 
ATOM   3352 C  CD2 . LEU   B 1 129 ? 0.630   -0.573  19.127  1.00 29.40  ? 981  LEU   B CD2 1 
ATOM   3353 N  N   . LYS   B 1 130 ? 3.672   -4.164  16.304  1.00 15.23  ? 982  LYS   B N   1 
ATOM   3354 C  CA  . LYS   B 1 130 ? 4.917   -4.857  15.994  1.00 14.93  ? 982  LYS   B CA  1 
ATOM   3355 C  C   . LYS   B 1 130 ? 5.885   -4.012  15.165  1.00 15.30  ? 982  LYS   B C   1 
ATOM   3356 O  O   . LYS   B 1 130 ? 7.080   -4.031  15.439  1.00 15.01  ? 982  LYS   B O   1 
ATOM   3357 C  CB  . LYS   B 1 130 ? 4.656   -6.225  15.339  1.00 18.94  ? 982  LYS   B CB  1 
ATOM   3358 C  CG  . LYS   B 1 130 ? 4.032   -7.219  16.284  1.00 18.15  ? 982  LYS   B CG  1 
ATOM   3359 C  CD  . LYS   B 1 130 ? 4.033   -8.647  15.752  1.00 28.49  ? 982  LYS   B CD  1 
ATOM   3360 C  CE  . LYS   B 1 130 ? 2.891   -8.930  14.810  1.00 30.37  ? 982  LYS   B CE  1 
ATOM   3361 N  NZ  . LYS   B 1 130 ? 2.566   -10.394 14.718  1.00 30.48  ? 982  LYS   B NZ  1 
ATOM   3362 N  N   . TYR   B 1 131 ? 5.397   -3.290  14.146  1.00 14.08  ? 983  TYR   B N   1 
ATOM   3363 C  CA  . TYR   B 1 131 ? 6.246   -2.290  13.468  1.00 12.62  ? 983  TYR   B CA  1 
ATOM   3364 C  C   . TYR   B 1 131 ? 6.828   -1.276  14.453  1.00 16.25  ? 983  TYR   B C   1 
ATOM   3365 O  O   . TYR   B 1 131 ? 8.009   -0.965  14.384  1.00 14.20  ? 983  TYR   B O   1 
ATOM   3366 C  CB  . TYR   B 1 131 ? 5.497   -1.534  12.377  1.00 15.26  ? 983  TYR   B CB  1 
ATOM   3367 C  CG  . TYR   B 1 131 ? 5.121   -2.312  11.113  1.00 14.09  ? 983  TYR   B CG  1 
ATOM   3368 C  CD1 . TYR   B 1 131 ? 5.708   -3.550  10.776  1.00 17.00  ? 983  TYR   B CD1 1 
ATOM   3369 C  CD2 . TYR   B 1 131 ? 4.214   -1.756  10.205  1.00 19.47  ? 983  TYR   B CD2 1 
ATOM   3370 C  CE1 . TYR   B 1 131 ? 5.369   -4.207  9.580   1.00 16.26  ? 983  TYR   B CE1 1 
ATOM   3371 C  CE2 . TYR   B 1 131 ? 3.864   -2.402  9.011   1.00 18.79  ? 983  TYR   B CE2 1 
ATOM   3372 C  CZ  . TYR   B 1 131 ? 4.445   -3.618  8.697   1.00 21.84  ? 983  TYR   B CZ  1 
ATOM   3373 O  OH  . TYR   B 1 131 ? 4.074   -4.227  7.514   1.00 25.23  ? 983  TYR   B OH  1 
ATOM   3374 N  N   . ALA   B 1 132 ? 5.979   -0.776  15.343  1.00 15.39  ? 984  ALA   B N   1 
ATOM   3375 C  CA  . ALA   B 1 132 ? 6.393   0.158   16.412  1.00 16.23  ? 984  ALA   B CA  1 
ATOM   3376 C  C   . ALA   B 1 132 ? 7.559   -0.417  17.216  1.00 14.13  ? 984  ALA   B C   1 
ATOM   3377 O  O   . ALA   B 1 132 ? 8.582   0.246   17.399  1.00 16.55  ? 984  ALA   B O   1 
ATOM   3378 C  CB  . ALA   B 1 132 ? 5.197   0.472   17.321  1.00 14.52  ? 984  ALA   B CB  1 
ATOM   3379 N  N   . VAL   B 1 133 ? 7.398   -1.655  17.705  1.00 14.92  ? 985  VAL   B N   1 
ATOM   3380 C  CA  . VAL   B 1 133 ? 8.478   -2.350  18.433  1.00 18.15  ? 985  VAL   B CA  1 
ATOM   3381 C  C   . VAL   B 1 133 ? 9.771   -2.415  17.631  1.00 15.76  ? 985  VAL   B C   1 
ATOM   3382 O  O   . VAL   B 1 133 ? 10.852  -2.148  18.139  1.00 16.99  ? 985  VAL   B O   1 
ATOM   3383 C  CB  . VAL   B 1 133 ? 8.046   -3.790  18.862  1.00 16.90  ? 985  VAL   B CB  1 
ATOM   3384 C  CG1 . VAL   B 1 133 ? 9.206   -4.570  19.466  1.00 22.40  ? 985  VAL   B CG1 1 
ATOM   3385 C  CG2 . VAL   B 1 133 ? 6.840   -3.731  19.810  1.00 17.26  ? 985  VAL   B CG2 1 
ATOM   3386 N  N   . GLN   B 1 134 ? 9.662   -2.749  16.356  1.00 18.32  ? 986  GLN   B N   1 
ATOM   3387 C  CA  . GLN   B 1 134 ? 10.839  -2.890  15.525  1.00 14.50  ? 986  GLN   B CA  1 
ATOM   3388 C  C   . GLN   B 1 134 ? 11.557  -1.566  15.325  1.00 13.68  ? 986  GLN   B C   1 
ATOM   3389 O  O   . GLN   B 1 134 ? 12.793  -1.519  15.336  1.00 15.66  ? 986  GLN   B O   1 
ATOM   3390 C  CB  . GLN   B 1 134 ? 10.430  -3.484  14.175  1.00 13.26  ? 986  GLN   B CB  1 
ATOM   3391 C  CG  . GLN   B 1 134 ? 10.075  -4.982  14.292  1.00 13.08  ? 986  GLN   B CG  1 
ATOM   3392 C  CD  . GLN   B 1 134 ? 9.382   -5.518  13.067  1.00 24.61  ? 986  GLN   B CD  1 
ATOM   3393 O  OE1 . GLN   B 1 134 ? 9.401   -4.876  12.042  1.00 21.82  ? 986  GLN   B OE1 1 
ATOM   3394 N  NE2 . GLN   B 1 134 ? 8.739   -6.688  13.182  1.00 21.30  ? 986  GLN   B NE2 1 
ATOM   3395 N  N   . ILE   B 1 135 ? 10.789  -0.505  15.082  1.00 12.49  ? 987  ILE   B N   1 
ATOM   3396 C  CA  . ILE   B 1 135 ? 11.356  0.842   14.957  1.00 13.06  ? 987  ILE   B CA  1 
ATOM   3397 C  C   . ILE   B 1 135 ? 12.113  1.195   16.255  1.00 14.35  ? 987  ILE   B C   1 
ATOM   3398 O  O   . ILE   B 1 135 ? 13.241  1.665   16.194  1.00 14.48  ? 987  ILE   B O   1 
ATOM   3399 C  CB  . ILE   B 1 135 ? 10.288  1.919   14.620  1.00 13.15  ? 987  ILE   B CB  1 
ATOM   3400 C  CG1 . ILE   B 1 135 ? 9.706   1.700   13.210  1.00 12.63  ? 987  ILE   B CG1 1 
ATOM   3401 C  CG2 . ILE   B 1 135 ? 10.883  3.325   14.745  1.00 12.47  ? 987  ILE   B CG2 1 
ATOM   3402 C  CD1 . ILE   B 1 135 ? 8.445   2.450   12.920  1.00 12.58  ? 987  ILE   B CD1 1 
ATOM   3403 N  N   . CYS   B 1 136 ? 11.487  0.939   17.399  1.00 15.29  ? 988  CYS   B N   1 
ATOM   3404 C  CA  . CYS   B 1 136 ? 12.114  1.153   18.717  1.00 16.31  ? 988  CYS   B CA  1 
ATOM   3405 C  C   . CYS   B 1 136 ? 13.406  0.316   18.907  1.00 17.14  ? 988  CYS   B C   1 
ATOM   3406 O  O   . CYS   B 1 136 ? 14.372  0.816   19.481  1.00 23.63  ? 988  CYS   B O   1 
ATOM   3407 C  CB  . CYS   B 1 136 ? 11.118  0.875   19.849  1.00 17.73  ? 988  CYS   B CB  1 
ATOM   3408 S  SG  . CYS   B 1 136 ? 9.794   2.090   19.980  1.00 20.33  ? 988  CYS   B SG  1 
ATOM   3409 N  N   . LYS   B 1 137 ? 13.411  -0.930  18.431  1.00 17.97  ? 989  LYS   B N   1 
ATOM   3410 C  CA  . LYS   B 1 137 ? 14.598  -1.789  18.525  1.00 16.26  ? 989  LYS   B CA  1 
ATOM   3411 C  C   . LYS   B 1 137 ? 15.746  -1.272  17.677  1.00 20.39  ? 989  LYS   B C   1 
ATOM   3412 O  O   . LYS   B 1 137 ? 16.876  -1.225  18.151  1.00 19.57  ? 989  LYS   B O   1 
ATOM   3413 C  CB  . LYS   B 1 137 ? 14.290  -3.257  18.250  1.00 20.62  ? 989  LYS   B CB  1 
ATOM   3414 C  CG  . LYS   B 1 137 ? 13.415  -3.917  19.340  1.00 17.89  ? 989  LYS   B CG  1 
ATOM   3415 C  CD  . LYS   B 1 137 ? 13.115  -5.366  19.017  1.00 23.24  ? 989  LYS   B CD  1 
ATOM   3416 C  CE  . LYS   B 1 137 ? 12.425  -6.086  20.156  1.00 31.99  ? 989  LYS   B CE  1 
ATOM   3417 N  NZ  . LYS   B 1 137 ? 11.870  -7.385  19.669  1.00 34.26  ? 989  LYS   B NZ  1 
ATOM   3418 N  N   . GLY   B 1 138 ? 15.467  -0.864  16.436  1.00 18.29  ? 990  GLY   B N   1 
ATOM   3419 C  CA  . GLY   B 1 138 ? 16.497  -0.201  15.625  1.00 19.38  ? 990  GLY   B CA  1 
ATOM   3420 C  C   . GLY   B 1 138 ? 17.037  1.093   16.250  1.00 17.36  ? 990  GLY   B C   1 
ATOM   3421 O  O   . GLY   B 1 138 ? 18.275  1.301   16.372  1.00 17.56  ? 990  GLY   B O   1 
ATOM   3422 N  N   . MET   B 1 139 ? 16.121  1.966   16.668  1.00 17.09  ? 991  MET   B N   1 
ATOM   3423 C  CA  . MET   B 1 139 ? 16.501  3.229   17.336  1.00 17.64  ? 991  MET   B CA  1 
ATOM   3424 C  C   . MET   B 1 139 ? 17.286  3.058   18.658  1.00 23.21  ? 991  MET   B C   1 
ATOM   3425 O  O   . MET   B 1 139 ? 18.268  3.795   18.924  1.00 23.07  ? 991  MET   B O   1 
ATOM   3426 C  CB  . MET   B 1 139 ? 15.264  4.094   17.595  1.00 18.52  ? 991  MET   B CB  1 
ATOM   3427 C  CG  . MET   B 1 139 ? 14.568  4.645   16.357  1.00 19.13  ? 991  MET   B CG  1 
ATOM   3428 S  SD  . MET   B 1 139 ? 15.645  5.660   15.348  1.00 20.81  ? 991  MET   B SD  1 
ATOM   3429 C  CE  . MET   B 1 139 ? 15.935  7.080   16.382  1.00 24.71  ? 991  MET   B CE  1 
ATOM   3430 N  N   . ASP   B 1 140 ? 16.866  2.098   19.476  1.00 22.57  ? 992  ASP   B N   1 
ATOM   3431 C  CA  . ASP   B 1 140 ? 17.570  1.833   20.729  1.00 25.38  ? 992  ASP   B CA  1 
ATOM   3432 C  C   . ASP   B 1 140 ? 18.995  1.285   20.457  1.00 24.94  ? 992  ASP   B C   1 
ATOM   3433 O  O   . ASP   B 1 140 ? 19.940  1.651   21.132  1.00 28.94  ? 992  ASP   B O   1 
ATOM   3434 C  CB  . ASP   B 1 140 ? 16.763  0.887   21.597  1.00 24.30  ? 992  ASP   B CB  1 
ATOM   3435 C  CG  . ASP   B 1 140 ? 17.236  0.862   23.033  1.00 31.22  ? 992  ASP   B CG  1 
ATOM   3436 O  OD1 . ASP   B 1 140 ? 17.454  1.949   23.605  1.00 30.18  ? 992  ASP   B OD1 1 
ATOM   3437 O  OD2 . ASP   B 1 140 ? 17.374  -0.250  23.573  1.00 36.22  ? 992  ASP   B OD2 1 
ATOM   3438 N  N   . TYR   B 1 141 ? 19.131  0.450   19.423  1.00 25.25  ? 993  TYR   B N   1 
ATOM   3439 C  CA  . TYR   B 1 141 ? 20.444  0.018   18.928  1.00 21.35  ? 993  TYR   B CA  1 
ATOM   3440 C  C   . TYR   B 1 141 ? 21.297  1.225   18.518  1.00 23.44  ? 993  TYR   B C   1 
ATOM   3441 O  O   . TYR   B 1 141 ? 22.456  1.302   18.871  1.00 22.12  ? 993  TYR   B O   1 
ATOM   3442 C  CB  . TYR   B 1 141 ? 20.299  -0.931  17.728  1.00 22.02  ? 993  TYR   B CB  1 
ATOM   3443 C  CG  . TYR   B 1 141 ? 21.624  -1.390  17.141  1.00 20.05  ? 993  TYR   B CG  1 
ATOM   3444 C  CD1 . TYR   B 1 141 ? 22.394  -2.384  17.759  1.00 22.18  ? 993  TYR   B CD1 1 
ATOM   3445 C  CD2 . TYR   B 1 141 ? 22.104  -0.829  15.954  1.00 24.59  ? 993  TYR   B CD2 1 
ATOM   3446 C  CE1 . TYR   B 1 141 ? 23.621  -2.799  17.188  1.00 21.50  ? 993  TYR   B CE1 1 
ATOM   3447 C  CE2 . TYR   B 1 141 ? 23.311  -1.217  15.393  1.00 22.11  ? 993  TYR   B CE2 1 
ATOM   3448 C  CZ  . TYR   B 1 141 ? 24.057  -2.194  15.984  1.00 17.84  ? 993  TYR   B CZ  1 
ATOM   3449 O  OH  . TYR   B 1 141 ? 25.231  -2.536  15.393  1.00 23.36  ? 993  TYR   B OH  1 
ATOM   3450 N  N   . LEU   B 1 142 ? 20.719  2.132   17.724  1.00 19.61  ? 994  LEU   B N   1 
ATOM   3451 C  CA  . LEU   B 1 142 ? 21.427  3.350   17.284  1.00 20.96  ? 994  LEU   B CA  1 
ATOM   3452 C  C   . LEU   B 1 142 ? 21.920  4.187   18.494  1.00 23.16  ? 994  LEU   B C   1 
ATOM   3453 O  O   . LEU   B 1 142 ? 23.063  4.618   18.543  1.00 20.93  ? 994  LEU   B O   1 
ATOM   3454 C  CB  . LEU   B 1 142 ? 20.520  4.176   16.372  1.00 20.75  ? 994  LEU   B CB  1 
ATOM   3455 C  CG  . LEU   B 1 142 ? 21.101  5.434   15.732  1.00 25.48  ? 994  LEU   B CG  1 
ATOM   3456 C  CD1 . LEU   B 1 142 ? 22.193  5.071   14.732  1.00 24.14  ? 994  LEU   B CD1 1 
ATOM   3457 C  CD2 . LEU   B 1 142 ? 20.025  6.239   15.068  1.00 24.16  ? 994  LEU   B CD2 1 
ATOM   3458 N  N   . GLY   B 1 143 ? 21.030  4.411   19.458  1.00 24.84  ? 995  GLY   B N   1 
ATOM   3459 C  CA  . GLY   B 1 143 ? 21.356  5.174   20.666  1.00 26.28  ? 995  GLY   B CA  1 
ATOM   3460 C  C   . GLY   B 1 143 ? 22.334  4.488   21.613  1.00 30.65  ? 995  GLY   B C   1 
ATOM   3461 O  O   . GLY   B 1 143 ? 23.073  5.165   22.334  1.00 29.70  ? 995  GLY   B O   1 
ATOM   3462 N  N   . SER   B 1 144 ? 22.355  3.154   21.599  1.00 32.41  ? 996  SER   B N   1 
ATOM   3463 C  CA  . SER   B 1 144 ? 23.376  2.388   22.312  1.00 32.62  ? 996  SER   B CA  1 
ATOM   3464 C  C   . SER   B 1 144 ? 24.773  2.590   21.727  1.00 33.15  ? 996  SER   B C   1 
ATOM   3465 O  O   . SER   B 1 144 ? 25.754  2.435   22.438  1.00 34.54  ? 996  SER   B O   1 
ATOM   3466 C  CB  . SER   B 1 144 ? 23.057  0.892   22.353  1.00 34.13  ? 996  SER   B CB  1 
ATOM   3467 O  OG  . SER   B 1 144 ? 23.412  0.217   21.151  1.00 35.30  ? 996  SER   B OG  1 
ATOM   3468 N  N   . ARG   B 1 145 ? 24.843  2.945   20.440  1.00 33.29  ? 997  ARG   B N   1 
ATOM   3469 C  CA  . ARG   B 1 145 ? 26.111  3.256   19.760  1.00 32.49  ? 997  ARG   B CA  1 
ATOM   3470 C  C   . ARG   B 1 145 ? 26.449  4.747   19.803  1.00 30.98  ? 997  ARG   B C   1 
ATOM   3471 O  O   . ARG   B 1 145 ? 27.409  5.191   19.159  1.00 35.22  ? 997  ARG   B O   1 
ATOM   3472 C  CB  . ARG   B 1 145 ? 26.079  2.741   18.330  1.00 31.98  ? 997  ARG   B CB  1 
ATOM   3473 C  CG  . ARG   B 1 145 ? 25.626  1.310   18.288  1.00 39.04  ? 997  ARG   B CG  1 
ATOM   3474 C  CD  . ARG   B 1 145 ? 26.128  0.497   17.157  1.00 47.56  ? 997  ARG   B CD  1 
ATOM   3475 N  NE  . ARG   B 1 145 ? 26.539  -0.801  17.687  1.00 56.73  ? 997  ARG   B NE  1 
ATOM   3476 C  CZ  . ARG   B 1 145 ? 27.796  -1.196  17.886  1.00 65.65  ? 997  ARG   B CZ  1 
ATOM   3477 N  NH1 . ARG   B 1 145 ? 28.835  -0.417  17.571  1.00 72.05  ? 997  ARG   B NH1 1 
ATOM   3478 N  NH2 . ARG   B 1 145 ? 28.024  -2.407  18.393  1.00 71.17  ? 997  ARG   B NH2 1 
ATOM   3479 N  N   . GLN   B 1 146 ? 25.675  5.492   20.588  1.00 26.87  ? 998  GLN   B N   1 
ATOM   3480 C  CA  . GLN   B 1 146 ? 25.876  6.907   20.907  1.00 32.06  ? 998  GLN   B CA  1 
ATOM   3481 C  C   . GLN   B 1 146 ? 25.646  7.816   19.691  1.00 32.96  ? 998  GLN   B C   1 
ATOM   3482 O  O   . GLN   B 1 146 ? 26.386  8.785   19.499  1.00 31.81  ? 998  GLN   B O   1 
ATOM   3483 C  CB  . GLN   B 1 146 ? 27.248  7.150   21.590  1.00 37.31  ? 998  GLN   B CB  1 
ATOM   3484 C  CG  . GLN   B 1 146 ? 27.416  6.416   22.942  1.00 40.34  ? 998  GLN   B CG  1 
ATOM   3485 C  CD  . GLN   B 1 146 ? 28.716  5.627   23.024  1.00 50.15  ? 998  GLN   B CD  1 
ATOM   3486 O  OE1 . GLN   B 1 146 ? 29.800  6.202   23.081  1.00 56.26  ? 998  GLN   B OE1 1 
ATOM   3487 N  NE2 . GLN   B 1 146 ? 28.608  4.299   23.014  1.00 54.25  ? 998  GLN   B NE2 1 
ATOM   3488 N  N   . TYR   B 1 147 ? 24.614  7.483   18.897  1.00 30.31  ? 999  TYR   B N   1 
ATOM   3489 C  CA  . TYR   B 1 147 ? 24.120  8.319   17.793  1.00 27.88  ? 999  TYR   B CA  1 
ATOM   3490 C  C   . TYR   B 1 147 ? 22.713  8.825   18.027  1.00 26.48  ? 999  TYR   B C   1 
ATOM   3491 O  O   . TYR   B 1 147 ? 21.867  8.111   18.601  1.00 27.11  ? 999  TYR   B O   1 
ATOM   3492 C  CB  . TYR   B 1 147 ? 24.091  7.555   16.461  1.00 26.18  ? 999  TYR   B CB  1 
ATOM   3493 C  CG  . TYR   B 1 147 ? 25.440  7.104   15.977  1.00 18.76  ? 999  TYR   B CG  1 
ATOM   3494 C  CD1 . TYR   B 1 147 ? 26.338  7.990   15.439  1.00 24.45  ? 999  TYR   B CD1 1 
ATOM   3495 C  CD2 . TYR   B 1 147 ? 25.797  5.755   16.040  1.00 32.98  ? 999  TYR   B CD2 1 
ATOM   3496 C  CE1 . TYR   B 1 147 ? 27.616  7.556   15.001  1.00 21.90  ? 999  TYR   B CE1 1 
ATOM   3497 C  CE2 . TYR   B 1 147 ? 27.036  5.313   15.616  1.00 27.91  ? 999  TYR   B CE2 1 
ATOM   3498 C  CZ  . TYR   B 1 147 ? 27.942  6.209   15.095  1.00 26.64  ? 999  TYR   B CZ  1 
ATOM   3499 O  OH  . TYR   B 1 147 ? 29.159  5.747   14.655  1.00 31.53  ? 999  TYR   B OH  1 
ATOM   3500 N  N   . VAL   B 1 148 ? 22.471  10.036  17.517  1.00 23.23  ? 1000 VAL   B N   1 
ATOM   3501 C  CA  . VAL   B 1 148 ? 21.132  10.610  17.348  1.00 24.50  ? 1000 VAL   B CA  1 
ATOM   3502 C  C   . VAL   B 1 148 ? 20.795  10.630  15.852  1.00 22.26  ? 1000 VAL   B C   1 
ATOM   3503 O  O   . VAL   B 1 148 ? 21.626  11.013  15.052  1.00 21.28  ? 1000 VAL   B O   1 
ATOM   3504 C  CB  . VAL   B 1 148 ? 20.993  12.055  17.983  1.00 29.90  ? 1000 VAL   B CB  1 
ATOM   3505 C  CG1 . VAL   B 1 148 ? 21.041  11.956  19.460  1.00 38.40  ? 1000 VAL   B CG1 1 
ATOM   3506 C  CG2 . VAL   B 1 148 ? 22.075  13.057  17.492  1.00 29.06  ? 1000 VAL   B CG2 1 
ATOM   3507 N  N   . HIS   B 1 149 ? 19.587  10.174  15.504  1.00 19.04  ? 1001 HIS   B N   1 
ATOM   3508 C  CA  . HIS   B 1 149 ? 19.140  10.078  14.106  1.00 18.80  ? 1001 HIS   B CA  1 
ATOM   3509 C  C   . HIS   B 1 149 ? 18.715  11.423  13.482  1.00 18.95  ? 1001 HIS   B C   1 
ATOM   3510 O  O   . HIS   B 1 149 ? 19.051  11.740  12.337  1.00 19.10  ? 1001 HIS   B O   1 
ATOM   3511 C  CB  . HIS   B 1 149 ? 17.954  9.117   14.018  1.00 17.75  ? 1001 HIS   B CB  1 
ATOM   3512 C  CG  . HIS   B 1 149 ? 17.558  8.804   12.619  1.00 16.66  ? 1001 HIS   B CG  1 
ATOM   3513 N  ND1 . HIS   B 1 149 ? 16.649  9.558   11.907  1.00 16.81  ? 1001 HIS   B ND1 1 
ATOM   3514 C  CD2 . HIS   B 1 149 ? 17.966  7.816   11.789  1.00 15.79  ? 1001 HIS   B CD2 1 
ATOM   3515 C  CE1 . HIS   B 1 149 ? 16.530  9.056   10.690  1.00 14.18  ? 1001 HIS   B CE1 1 
ATOM   3516 N  NE2 . HIS   B 1 149 ? 17.301  7.984   10.602  1.00 13.66  ? 1001 HIS   B NE2 1 
ATOM   3517 N  N   . ARG   B 1 150 ? 17.888  12.157  14.212  1.00 19.76  ? 1002 ARG   B N   1 
ATOM   3518 C  CA  . ARG   B 1 150 ? 17.485  13.527  13.861  1.00 21.62  ? 1002 ARG   B CA  1 
ATOM   3519 C  C   . ARG   B 1 150 ? 16.514  13.645  12.677  1.00 22.89  ? 1002 ARG   B C   1 
ATOM   3520 O  O   . ARG   B 1 150 ? 16.238  14.753  12.213  1.00 26.04  ? 1002 ARG   B O   1 
ATOM   3521 C  CB  . ARG   B 1 150 ? 18.704  14.471  13.649  1.00 22.43  ? 1002 ARG   B CB  1 
ATOM   3522 C  CG  . ARG   B 1 150 ? 19.772  14.410  14.714  1.00 25.12  ? 1002 ARG   B CG  1 
ATOM   3523 C  CD  . ARG   B 1 150 ? 20.974  15.306  14.356  1.00 33.19  ? 1002 ARG   B CD  1 
ATOM   3524 N  NE  . ARG   B 1 150 ? 20.576  16.601  13.800  1.00 40.00  ? 1002 ARG   B NE  1 
ATOM   3525 C  CZ  . ARG   B 1 150 ? 21.099  17.211  12.727  1.00 47.20  ? 1002 ARG   B CZ  1 
ATOM   3526 N  NH1 . ARG   B 1 150 ? 22.090  16.681  11.998  1.00 38.08  ? 1002 ARG   B NH1 1 
ATOM   3527 N  NH2 . ARG   B 1 150 ? 20.624  18.409  12.382  1.00 49.09  ? 1002 ARG   B NH2 1 
ATOM   3528 N  N   . ASP   B 1 151 ? 15.991  12.519  12.183  1.00 20.79  ? 1003 ASP   B N   1 
ATOM   3529 C  CA  . ASP   B 1 151 ? 15.091  12.539  11.042  1.00 20.42  ? 1003 ASP   B CA  1 
ATOM   3530 C  C   . ASP   B 1 151 ? 14.114  11.362  11.056  1.00 19.10  ? 1003 ASP   B C   1 
ATOM   3531 O  O   . ASP   B 1 151 ? 13.752  10.828  9.993   1.00 18.17  ? 1003 ASP   B O   1 
ATOM   3532 C  CB  . ASP   B 1 151 ? 15.932  12.526  9.750   1.00 21.51  ? 1003 ASP   B CB  1 
ATOM   3533 C  CG  . ASP   B 1 151 ? 15.190  13.079  8.548   1.00 26.61  ? 1003 ASP   B CG  1 
ATOM   3534 O  OD1 . ASP   B 1 151 ? 14.219  13.834  8.741   1.00 27.04  ? 1003 ASP   B OD1 1 
ATOM   3535 O  OD2 . ASP   B 1 151 ? 15.597  12.776  7.401   1.00 24.67  ? 1003 ASP   B OD2 1 
ATOM   3536 N  N   . LEU   B 1 152 ? 13.681  10.970  12.255  1.00 18.97  ? 1004 LEU   B N   1 
ATOM   3537 C  CA  . LEU   B 1 152 ? 12.846  9.792   12.412  1.00 19.55  ? 1004 LEU   B CA  1 
ATOM   3538 C  C   . LEU   B 1 152 ? 11.396  10.155  12.064  1.00 21.53  ? 1004 LEU   B C   1 
ATOM   3539 O  O   . LEU   B 1 152 ? 10.738  10.958  12.736  1.00 19.79  ? 1004 LEU   B O   1 
ATOM   3540 C  CB  . LEU   B 1 152 ? 12.968  9.169   13.809  1.00 18.98  ? 1004 LEU   B CB  1 
ATOM   3541 C  CG  . LEU   B 1 152 ? 12.070  7.943   14.003  1.00 18.81  ? 1004 LEU   B CG  1 
ATOM   3542 C  CD1 . LEU   B 1 152 ? 12.376  6.801   12.998  1.00 19.55  ? 1004 LEU   B CD1 1 
ATOM   3543 C  CD2 . LEU   B 1 152 ? 12.162  7.430   15.446  1.00 19.07  ? 1004 LEU   B CD2 1 
ATOM   3544 N  N   . ALA   B 1 153 ? 10.924  9.538   10.988  1.00 18.98  ? 1005 ALA   B N   1 
ATOM   3545 C  CA  . ALA   B 1 153 ? 9.637   9.825   10.371  1.00 18.72  ? 1005 ALA   B CA  1 
ATOM   3546 C  C   . ALA   B 1 153 ? 9.270   8.622   9.502   1.00 16.36  ? 1005 ALA   B C   1 
ATOM   3547 O  O   . ALA   B 1 153 ? 10.170  7.869   9.096   1.00 13.38  ? 1005 ALA   B O   1 
ATOM   3548 C  CB  . ALA   B 1 153 ? 9.735   11.067  9.510   1.00 19.79  ? 1005 ALA   B CB  1 
ATOM   3549 N  N   . ALA   B 1 154 ? 7.971   8.412   9.266   1.00 16.61  ? 1006 ALA   B N   1 
ATOM   3550 C  CA  . ALA   B 1 154 ? 7.497   7.254   8.497   1.00 16.94  ? 1006 ALA   B CA  1 
ATOM   3551 C  C   . ALA   B 1 154 ? 8.105   7.171   7.082   1.00 17.52  ? 1006 ALA   B C   1 
ATOM   3552 O  O   . ALA   B 1 154 ? 8.371   6.063   6.584   1.00 16.25  ? 1006 ALA   B O   1 
ATOM   3553 C  CB  . ALA   B 1 154 ? 6.002   7.253   8.405   1.00 18.69  ? 1006 ALA   B CB  1 
ATOM   3554 N  N   . ARG   B 1 155 ? 8.369   8.333   6.490   1.00 20.01  ? 1007 ARG   B N   1 
ATOM   3555 C  CA  . ARG   B 1 155 ? 9.035   8.401   5.200   1.00 19.39  ? 1007 ARG   B CA  1 
ATOM   3556 C  C   . ARG   B 1 155 ? 10.434  7.777   5.198   1.00 18.14  ? 1007 ARG   B C   1 
ATOM   3557 O  O   . ARG   B 1 155 ? 10.882  7.376   4.132   1.00 17.96  ? 1007 ARG   B O   1 
ATOM   3558 C  CB  . ARG   B 1 155 ? 9.093   9.841   4.685   1.00 21.22  ? 1007 ARG   B CB  1 
ATOM   3559 C  CG  . ARG   B 1 155 ? 10.006  10.760  5.458   1.00 23.28  ? 1007 ARG   B CG  1 
ATOM   3560 C  CD  . ARG   B 1 155 ? 9.887   12.212  4.983   1.00 30.17  ? 1007 ARG   B CD  1 
ATOM   3561 N  NE  . ARG   B 1 155 ? 10.303  13.064  6.081   1.00 32.79  ? 1007 ARG   B NE  1 
ATOM   3562 C  CZ  . ARG   B 1 155 ? 11.559  13.339  6.415   1.00 32.88  ? 1007 ARG   B CZ  1 
ATOM   3563 N  NH1 . ARG   B 1 155 ? 12.600  12.912  5.689   1.00 39.92  ? 1007 ARG   B NH1 1 
ATOM   3564 N  NH2 . ARG   B 1 155 ? 11.779  14.097  7.479   1.00 45.53  ? 1007 ARG   B NH2 1 
ATOM   3565 N  N   . ASN   B 1 156 ? 11.111  7.718   6.361   1.00 13.51  ? 1008 ASN   B N   1 
ATOM   3566 C  CA  . ASN   B 1 156 ? 12.427  7.059   6.502   1.00 16.98  ? 1008 ASN   B CA  1 
ATOM   3567 C  C   . ASN   B 1 156 ? 12.460  5.638   7.042   1.00 14.98  ? 1008 ASN   B C   1 
ATOM   3568 O  O   . ASN   B 1 156 ? 13.529  5.132   7.367   1.00 13.08  ? 1008 ASN   B O   1 
ATOM   3569 C  CB  . ASN   B 1 156 ? 13.364  7.944   7.318   1.00 14.90  ? 1008 ASN   B CB  1 
ATOM   3570 C  CG  . ASN   B 1 156 ? 13.776  9.164   6.556   1.00 16.92  ? 1008 ASN   B CG  1 
ATOM   3571 O  OD1 . ASN   B 1 156 ? 13.932  9.099   5.336   1.00 17.86  ? 1008 ASN   B OD1 1 
ATOM   3572 N  ND2 . ASN   B 1 156 ? 13.950  10.279  7.243   1.00 17.51  ? 1008 ASN   B ND2 1 
ATOM   3573 N  N   . VAL   B 1 157 ? 11.292  5.001   7.140   1.00 13.64  ? 1009 VAL   B N   1 
ATOM   3574 C  CA  . VAL   B 1 157 ? 11.214  3.636   7.604   1.00 11.47  ? 1009 VAL   B CA  1 
ATOM   3575 C  C   . VAL   B 1 157 ? 10.789  2.798   6.406   1.00 13.60  ? 1009 VAL   B C   1 
ATOM   3576 O  O   . VAL   B 1 157 ? 9.711   3.024   5.859   1.00 14.72  ? 1009 VAL   B O   1 
ATOM   3577 C  CB  . VAL   B 1 157 ? 10.152  3.442   8.692   1.00 13.86  ? 1009 VAL   B CB  1 
ATOM   3578 C  CG1 . VAL   B 1 157 ? 10.033  1.973   9.042   1.00 12.16  ? 1009 VAL   B CG1 1 
ATOM   3579 C  CG2 . VAL   B 1 157 ? 10.484  4.253   9.919   1.00 15.56  ? 1009 VAL   B CG2 1 
ATOM   3580 N  N   . LEU   B 1 158 ? 11.594  1.810   6.063   1.00 14.38  ? 1010 LEU   B N   1 
ATOM   3581 C  CA  . LEU   B 1 158 ? 11.331  0.921   4.932   1.00 13.53  ? 1010 LEU   B CA  1 
ATOM   3582 C  C   . LEU   B 1 158 ? 10.580  -0.342  5.377   1.00 12.84  ? 1010 LEU   B C   1 
ATOM   3583 O  O   . LEU   B 1 158 ? 10.719  -0.793  6.535   1.00 13.00  ? 1010 LEU   B O   1 
ATOM   3584 C  CB  . LEU   B 1 158 ? 12.642  0.473   4.279   1.00 12.66  ? 1010 LEU   B CB  1 
ATOM   3585 C  CG  . LEU   B 1 158 ? 13.474  1.576   3.655   1.00 12.96  ? 1010 LEU   B CG  1 
ATOM   3586 C  CD1 . LEU   B 1 158 ? 14.878  1.033   3.329   1.00 16.99  ? 1010 LEU   B CD1 1 
ATOM   3587 C  CD2 . LEU   B 1 158 ? 12.778  2.188   2.423   1.00 19.30  ? 1010 LEU   B CD2 1 
ATOM   3588 N  N   . VAL   B 1 159 ? 9.822   -0.906  4.441   1.00 12.13  ? 1011 VAL   B N   1 
ATOM   3589 C  CA  . VAL   B 1 159 ? 9.092   -2.150  4.628   1.00 16.57  ? 1011 VAL   B CA  1 
ATOM   3590 C  C   . VAL   B 1 159 ? 9.882   -3.268  3.950   1.00 18.51  ? 1011 VAL   B C   1 
ATOM   3591 O  O   . VAL   B 1 159 ? 9.979   -3.324  2.706   1.00 14.17  ? 1011 VAL   B O   1 
ATOM   3592 C  CB  . VAL   B 1 159 ? 7.646   -2.058  4.057   1.00 17.02  ? 1011 VAL   B CB  1 
ATOM   3593 C  CG1 . VAL   B 1 159 ? 6.904   -3.358  4.205   1.00 17.88  ? 1011 VAL   B CG1 1 
ATOM   3594 C  CG2 . VAL   B 1 159 ? 6.899   -0.966  4.750   1.00 18.91  ? 1011 VAL   B CG2 1 
ATOM   3595 N  N   . GLU   B 1 160 ? 10.448  -4.148  4.770   1.00 14.73  ? 1012 GLU   B N   1 
ATOM   3596 C  CA  . GLU   B 1 160 ? 11.131  -5.377  4.327   1.00 20.40  ? 1012 GLU   B CA  1 
ATOM   3597 C  C   . GLU   B 1 160 ? 10.126  -6.452  3.857   1.00 21.09  ? 1012 GLU   B C   1 
ATOM   3598 O  O   . GLU   B 1 160 ? 10.351  -7.143  2.857   1.00 19.87  ? 1012 GLU   B O   1 
ATOM   3599 C  CB  . GLU   B 1 160 ? 11.997  -5.929  5.462   1.00 16.39  ? 1012 GLU   B CB  1 
ATOM   3600 C  CG  . GLU   B 1 160 ? 12.632  -7.319  5.267   1.00 24.78  ? 1012 GLU   B CG  1 
ATOM   3601 C  CD  . GLU   B 1 160 ? 13.488  -7.444  4.022   1.00 31.94  ? 1012 GLU   B CD  1 
ATOM   3602 O  OE1 . GLU   B 1 160 ? 14.181  -6.479  3.676   1.00 23.99  ? 1012 GLU   B OE1 1 
ATOM   3603 O  OE2 . GLU   B 1 160 ? 13.498  -8.529  3.389   1.00 30.56  ? 1012 GLU   B OE2 1 
ATOM   3604 N  N   . SER   B 1 161 ? 9.036   -6.569  4.614   1.00 19.49  ? 1013 SER   B N   1 
ATOM   3605 C  CA  . SER   B 1 161 ? 7.907   -7.474  4.353   1.00 19.39  ? 1013 SER   B CA  1 
ATOM   3606 C  C   . SER   B 1 161 ? 6.719   -6.987  5.159   1.00 18.93  ? 1013 SER   B C   1 
ATOM   3607 O  O   . SER   B 1 161 ? 6.859   -6.089  5.998   1.00 18.29  ? 1013 SER   B O   1 
ATOM   3608 C  CB  . SER   B 1 161 ? 8.240   -8.888  4.811   1.00 23.31  ? 1013 SER   B CB  1 
ATOM   3609 O  OG  . SER   B 1 161 ? 8.383   -8.942  6.227   1.00 22.67  ? 1013 SER   B OG  1 
ATOM   3610 N  N   . GLU   B 1 162 ? 5.561   -7.624  5.002   1.00 20.65  ? 1014 GLU   B N   1 
ATOM   3611 C  CA  . GLU   B 1 162 ? 4.424   -7.244  5.829   1.00 20.63  ? 1014 GLU   B CA  1 
ATOM   3612 C  C   . GLU   B 1 162 ? 4.724   -7.442  7.341   1.00 17.42  ? 1014 GLU   B C   1 
ATOM   3613 O  O   . GLU   B 1 162 ? 4.054   -6.851  8.171   1.00 23.36  ? 1014 GLU   B O   1 
ATOM   3614 C  CB  . GLU   B 1 162 ? 3.148   -7.966  5.411   1.00 26.38  ? 1014 GLU   B CB  1 
ATOM   3615 C  CG  . GLU   B 1 162 ? 2.866   -9.273  6.050   1.00 31.97  ? 1014 GLU   B CG  1 
ATOM   3616 C  CD  . GLU   B 1 162 ? 1.480   -9.734  5.685   1.00 35.58  ? 1014 GLU   B CD  1 
ATOM   3617 O  OE1 . GLU   B 1 162 ? 1.301   -10.062 4.493   1.00 31.60  ? 1014 GLU   B OE1 1 
ATOM   3618 O  OE2 . GLU   B 1 162 ? 0.588   -9.729  6.576   1.00 36.28  ? 1014 GLU   B OE2 1 
ATOM   3619 N  N   . HIS   B 1 163 ? 5.730   -8.263  7.661   1.00 16.26  ? 1015 HIS   B N   1 
ATOM   3620 C  CA  . HIS   B 1 163 ? 6.109   -8.555  9.046   1.00 15.59  ? 1015 HIS   B CA  1 
ATOM   3621 C  C   . HIS   B 1 163 ? 7.354   -7.830  9.572   1.00 15.47  ? 1015 HIS   B C   1 
ATOM   3622 O  O   . HIS   B 1 163 ? 7.710   -8.017  10.731  1.00 15.51  ? 1015 HIS   B O   1 
ATOM   3623 C  CB  . HIS   B 1 163 ? 6.295   -10.050 9.217   1.00 22.82  ? 1015 HIS   B CB  1 
ATOM   3624 C  CG  . HIS   B 1 163 ? 5.116   -10.840 8.753   1.00 26.53  ? 1015 HIS   B CG  1 
ATOM   3625 N  ND1 . HIS   B 1 163 ? 3.892   -10.768 9.378   1.00 29.91  ? 1015 HIS   B ND1 1 
ATOM   3626 C  CD2 . HIS   B 1 163 ? 4.959   -11.674 7.700   1.00 31.40  ? 1015 HIS   B CD2 1 
ATOM   3627 C  CE1 . HIS   B 1 163 ? 3.033   -11.542 8.741   1.00 30.91  ? 1015 HIS   B CE1 1 
ATOM   3628 N  NE2 . HIS   B 1 163 ? 3.655   -12.102 7.717   1.00 36.30  ? 1015 HIS   B NE2 1 
ATOM   3629 N  N   . GLN   B 1 164 ? 8.026   -7.013  8.756   1.00 15.40  ? 1016 GLN   B N   1 
ATOM   3630 C  CA  . GLN   B 1 164 ? 9.298   -6.392  9.171   1.00 16.32  ? 1016 GLN   B CA  1 
ATOM   3631 C  C   . GLN   B 1 164 ? 9.558   -5.041  8.513   1.00 12.25  ? 1016 GLN   B C   1 
ATOM   3632 O  O   . GLN   B 1 164 ? 9.375   -4.864  7.281   1.00 12.54  ? 1016 GLN   B O   1 
ATOM   3633 C  CB  . GLN   B 1 164 ? 10.475  -7.313  8.854   1.00 14.30  ? 1016 GLN   B CB  1 
ATOM   3634 C  CG  . GLN   B 1 164 ? 11.846  -6.862  9.415   1.00 16.90  ? 1016 GLN   B CG  1 
ATOM   3635 C  CD  . GLN   B 1 164 ? 12.964  -7.817  9.026   1.00 22.03  ? 1016 GLN   B CD  1 
ATOM   3636 O  OE1 . GLN   B 1 164 ? 12.734  -8.800  8.351   1.00 26.69  ? 1016 GLN   B OE1 1 
ATOM   3637 N  NE2 . GLN   B 1 164 ? 14.185  -7.518  9.446   1.00 27.97  ? 1016 GLN   B NE2 1 
ATOM   3638 N  N   . VAL   B 1 165 ? 10.008  -4.099  9.340   1.00 12.40  ? 1017 VAL   B N   1 
ATOM   3639 C  CA  . VAL   B 1 165 ? 10.407  -2.781  8.854   1.00 11.95  ? 1017 VAL   B CA  1 
ATOM   3640 C  C   . VAL   B 1 165 ? 11.877  -2.553  9.251   1.00 13.96  ? 1017 VAL   B C   1 
ATOM   3641 O  O   . VAL   B 1 165 ? 12.440  -3.226  10.157  1.00 12.11  ? 1017 VAL   B O   1 
ATOM   3642 C  CB  . VAL   B 1 165 ? 9.498   -1.626  9.389   1.00 14.23  ? 1017 VAL   B CB  1 
ATOM   3643 C  CG1 . VAL   B 1 165 ? 8.084   -1.728  8.884   1.00 14.00  ? 1017 VAL   B CG1 1 
ATOM   3644 C  CG2 . VAL   B 1 165 ? 9.482   -1.576  10.944  1.00 16.92  ? 1017 VAL   B CG2 1 
ATOM   3645 N  N   . LYS   B 1 166 ? 12.487  -1.579  8.590   1.00 13.19  ? 1018 LYS   B N   1 
ATOM   3646 C  CA  . LYS   B 1 166 ? 13.854  -1.196  8.860   1.00 14.70  ? 1018 LYS   B CA  1 
ATOM   3647 C  C   . LYS   B 1 166 ? 14.000  0.311   8.703   1.00 14.33  ? 1018 LYS   B C   1 
ATOM   3648 O  O   . LYS   B 1 166 ? 13.463  0.900   7.746   1.00 12.66  ? 1018 LYS   B O   1 
ATOM   3649 C  CB  . LYS   B 1 166 ? 14.833  -1.838  7.873   1.00 13.54  ? 1018 LYS   B CB  1 
ATOM   3650 C  CG  . LYS   B 1 166 ? 14.703  -3.342  7.671   1.00 9.06   ? 1018 LYS   B CG  1 
ATOM   3651 C  CD  . LYS   B 1 166 ? 16.015  -3.912  7.057   1.00 12.57  ? 1018 LYS   B CD  1 
ATOM   3652 C  CE  . LYS   B 1 166 ? 15.915  -5.416  6.777   1.00 18.02  ? 1018 LYS   B CE  1 
ATOM   3653 N  NZ  . LYS   B 1 166 ? 17.144  -6.026  6.180   1.00 18.25  ? 1018 LYS   B NZ  1 
ATOM   3654 N  N   A ILE   B 1 167 ? 14.757  0.917   9.617   0.50 13.24  ? 1019 ILE   B N   1 
ATOM   3655 N  N   B ILE   B 1 167 ? 14.759  0.914   9.622   0.50 14.05  ? 1019 ILE   B N   1 
ATOM   3656 C  CA  A ILE   B 1 167 ? 15.160  2.323   9.477   0.50 12.45  ? 1019 ILE   B CA  1 
ATOM   3657 C  CA  B ILE   B 1 167 ? 15.209  2.309   9.481   0.50 13.86  ? 1019 ILE   B CA  1 
ATOM   3658 C  C   A ILE   B 1 167 ? 16.090  2.412   8.241   0.50 12.42  ? 1019 ILE   B C   1 
ATOM   3659 C  C   B ILE   B 1 167 ? 16.088  2.388   8.219   0.50 13.26  ? 1019 ILE   B C   1 
ATOM   3660 O  O   A ILE   B 1 167 ? 17.110  1.703   8.162   0.50 10.81  ? 1019 ILE   B O   1 
ATOM   3661 O  O   B ILE   B 1 167 ? 17.084  1.653   8.103   0.50 11.69  ? 1019 ILE   B O   1 
ATOM   3662 C  CB  A ILE   B 1 167 ? 15.825  2.895   10.748  0.50 13.17  ? 1019 ILE   B CB  1 
ATOM   3663 C  CB  B ILE   B 1 167 ? 16.009  2.833   10.703  0.50 15.61  ? 1019 ILE   B CB  1 
ATOM   3664 C  CG1 A ILE   B 1 167 ? 14.925  2.725   11.992  0.50 15.28  ? 1019 ILE   B CG1 1 
ATOM   3665 C  CG1 B ILE   B 1 167 ? 15.296  2.573   12.047  0.50 18.86  ? 1019 ILE   B CG1 1 
ATOM   3666 C  CG2 A ILE   B 1 167 ? 16.123  4.382   10.535  0.50 9.47   ? 1019 ILE   B CG2 1 
ATOM   3667 C  CG2 B ILE   B 1 167 ? 16.283  4.332   10.527  0.50 14.52  ? 1019 ILE   B CG2 1 
ATOM   3668 C  CD1 A ILE   B 1 167 ? 15.679  2.727   13.291  0.50 12.03  ? 1019 ILE   B CD1 1 
ATOM   3669 C  CD1 B ILE   B 1 167 ? 13.917  3.171   12.166  0.50 20.53  ? 1019 ILE   B CD1 1 
ATOM   3670 N  N   . GLY   B 1 168 ? 15.719  3.271   7.287   1.00 9.92   ? 1020 GLY   B N   1 
ATOM   3671 C  CA  . GLY   B 1 168 ? 16.247  3.216   5.929   1.00 10.96  ? 1020 GLY   B CA  1 
ATOM   3672 C  C   . GLY   B 1 168 ? 17.100  4.331   5.404   1.00 12.34  ? 1020 GLY   B C   1 
ATOM   3673 O  O   . GLY   B 1 168 ? 17.567  4.236   4.277   1.00 10.64  ? 1020 GLY   B O   1 
ATOM   3674 N  N   . ASP   B 1 169 ? 17.312  5.371   6.212   1.00 13.86  ? 1021 ASP   B N   1 
ATOM   3675 C  CA  . ASP   B 1 169 ? 18.155  6.490   5.825   1.00 16.73  ? 1021 ASP   B CA  1 
ATOM   3676 C  C   . ASP   B 1 169 ? 18.731  7.122   7.070   1.00 12.61  ? 1021 ASP   B C   1 
ATOM   3677 O  O   . ASP   B 1 169 ? 18.038  7.190   8.096   1.00 15.72  ? 1021 ASP   B O   1 
ATOM   3678 C  CB  . ASP   B 1 169 ? 17.357  7.510   5.020   1.00 14.95  ? 1021 ASP   B CB  1 
ATOM   3679 C  CG  . ASP   B 1 169 ? 18.213  8.603   4.440   1.00 20.01  ? 1021 ASP   B CG  1 
ATOM   3680 O  OD1 . ASP   B 1 169 ? 18.697  8.421   3.294   1.00 17.69  ? 1021 ASP   B OD1 1 
ATOM   3681 O  OD2 . ASP   B 1 169 ? 18.376  9.671   5.108   1.00 17.12  ? 1021 ASP   B OD2 1 
ATOM   3682 N  N   . PHE   B 1 170 ? 19.990  7.550   6.970   1.00 13.05  ? 1022 PHE   B N   1 
ATOM   3683 C  CA  . PHE   B 1 170 ? 20.749  8.109   8.088   1.00 16.08  ? 1022 PHE   B CA  1 
ATOM   3684 C  C   . PHE   B 1 170 ? 21.420  9.430   7.716   1.00 16.14  ? 1022 PHE   B C   1 
ATOM   3685 O  O   . PHE   B 1 170 ? 22.448  9.788   8.285   1.00 16.07  ? 1022 PHE   B O   1 
ATOM   3686 C  CB  . PHE   B 1 170 ? 21.760  7.057   8.574   1.00 14.68  ? 1022 PHE   B CB  1 
ATOM   3687 C  CG  . PHE   B 1 170 ? 21.089  5.857   9.148   1.00 13.94  ? 1022 PHE   B CG  1 
ATOM   3688 C  CD1 . PHE   B 1 170 ? 20.667  4.810   8.331   1.00 13.22  ? 1022 PHE   B CD1 1 
ATOM   3689 C  CD2 . PHE   B 1 170 ? 20.802  5.795   10.507  1.00 13.11  ? 1022 PHE   B CD2 1 
ATOM   3690 C  CE1 . PHE   B 1 170 ? 19.996  3.729   8.839   1.00 16.65  ? 1022 PHE   B CE1 1 
ATOM   3691 C  CE2 . PHE   B 1 170 ? 20.138  4.684   11.031  1.00 17.18  ? 1022 PHE   B CE2 1 
ATOM   3692 C  CZ  . PHE   B 1 170 ? 19.727  3.667   10.187  1.00 14.93  ? 1022 PHE   B CZ  1 
ATOM   3693 N  N   . GLY   B 1 171 ? 20.779  10.180  6.833   1.00 14.11  ? 1023 GLY   B N   1 
ATOM   3694 C  CA  . GLY   B 1 171 ? 21.336  11.403  6.280   1.00 16.58  ? 1023 GLY   B CA  1 
ATOM   3695 C  C   . GLY   B 1 171 ? 21.702  12.489  7.297   1.00 16.48  ? 1023 GLY   B C   1 
ATOM   3696 O  O   . GLY   B 1 171 ? 22.633  13.274  7.088   1.00 18.70  ? 1023 GLY   B O   1 
ATOM   3697 N  N   . LEU   B 1 172 ? 20.939  12.543  8.383   1.00 18.20  ? 1024 LEU   B N   1 
ATOM   3698 C  CA  . LEU   B 1 172 ? 21.162  13.544  9.453   1.00 18.98  ? 1024 LEU   B CA  1 
ATOM   3699 C  C   . LEU   B 1 172 ? 21.749  12.955  10.735  1.00 23.07  ? 1024 LEU   B C   1 
ATOM   3700 O  O   . LEU   B 1 172 ? 21.956  13.676  11.703  1.00 21.57  ? 1024 LEU   B O   1 
ATOM   3701 C  CB  . LEU   B 1 172 ? 19.835  14.222  9.784   1.00 21.79  ? 1024 LEU   B CB  1 
ATOM   3702 C  CG  . LEU   B 1 172 ? 19.131  15.037  8.705   1.00 27.36  ? 1024 LEU   B CG  1 
ATOM   3703 C  CD1 . LEU   B 1 172 ? 17.982  15.834  9.363   1.00 29.40  ? 1024 LEU   B CD1 1 
ATOM   3704 C  CD2 . LEU   B 1 172 ? 20.072  15.983  7.973   1.00 31.58  ? 1024 LEU   B CD2 1 
ATOM   3705 N  N   . THR   B 1 173 ? 22.060  11.665  10.735  1.00 20.38  ? 1025 THR   B N   1 
ATOM   3706 C  CA  . THR   B 1 173 ? 22.606  10.993  11.908  1.00 21.92  ? 1025 THR   B CA  1 
ATOM   3707 C  C   . THR   B 1 173 ? 23.981  11.534  12.365  1.00 24.26  ? 1025 THR   B C   1 
ATOM   3708 O  O   . THR   B 1 173 ? 24.908  11.749  11.562  1.00 21.33  ? 1025 THR   B O   1 
ATOM   3709 C  CB  . THR   B 1 173 ? 22.585  9.436   11.706  1.00 17.37  ? 1025 THR   B CB  1 
ATOM   3710 O  OG1 . THR   B 1 173 ? 21.251  8.986   11.440  1.00 18.35  ? 1025 THR   B OG1 1 
ATOM   3711 C  CG2 . THR   B 1 173 ? 23.128  8.698   12.931  1.00 21.70  ? 1025 THR   B CG2 1 
ATOM   3712 N  N   . LYS   B 1 174 ? 24.078  11.826  13.671  1.00 24.51  ? 1026 LYS   B N   1 
ATOM   3713 C  CA  . LYS   B 1 174 ? 25.247  12.462  14.283  1.00 28.18  ? 1026 LYS   B CA  1 
ATOM   3714 C  C   . LYS   B 1 174 ? 25.653  11.724  15.551  1.00 28.32  ? 1026 LYS   B C   1 
ATOM   3715 O  O   . LYS   B 1 174 ? 24.797  11.215  16.270  1.00 25.96  ? 1026 LYS   B O   1 
ATOM   3716 C  CB  . LYS   B 1 174 ? 24.932  13.914  14.658  1.00 28.55  ? 1026 LYS   B CB  1 
ATOM   3717 C  CG  . LYS   B 1 174 ? 24.723  14.855  13.490  1.00 27.92  ? 1026 LYS   B CG  1 
ATOM   3718 C  CD  . LYS   B 1 174 ? 26.010  15.167  12.775  1.00 30.03  ? 1026 LYS   B CD  1 
ATOM   3719 C  CE  . LYS   B 1 174 ? 25.789  16.082  11.578  1.00 29.30  ? 1026 LYS   B CE  1 
ATOM   3720 N  NZ  . LYS   B 1 174 ? 27.102  16.441  10.952  1.00 27.81  ? 1026 LYS   B NZ  1 
ATOM   3721 N  N   . ALA   B 1 175 ? 26.960  11.657  15.804  1.00 30.71  ? 1027 ALA   B N   1 
ATOM   3722 C  CA  . ALA   B 1 175 ? 27.479  11.083  17.044  1.00 31.05  ? 1027 ALA   B CA  1 
ATOM   3723 C  C   . ALA   B 1 175 ? 27.212  12.042  18.220  1.00 33.06  ? 1027 ALA   B C   1 
ATOM   3724 O  O   . ALA   B 1 175 ? 27.291  13.253  18.052  1.00 34.30  ? 1027 ALA   B O   1 
ATOM   3725 C  CB  . ALA   B 1 175 ? 28.949  10.783  16.915  1.00 34.26  ? 1027 ALA   B CB  1 
ATOM   3726 N  N   . ILE   B 1 176 ? 26.832  11.483  19.370  1.00 34.37  ? 1028 ILE   B N   1 
ATOM   3727 C  CA  . ILE   B 1 176 ? 26.844  12.215  20.644  1.00 41.19  ? 1028 ILE   B CA  1 
ATOM   3728 C  C   . ILE   B 1 176 ? 28.235  12.026  21.231  1.00 48.61  ? 1028 ILE   B C   1 
ATOM   3729 O  O   . ILE   B 1 176 ? 28.718  10.899  21.307  1.00 52.11  ? 1028 ILE   B O   1 
ATOM   3730 C  CB  . ILE   B 1 176 ? 25.817  11.671  21.667  1.00 43.35  ? 1028 ILE   B CB  1 
ATOM   3731 C  CG1 . ILE   B 1 176 ? 24.379  11.945  21.204  1.00 40.76  ? 1028 ILE   B CG1 1 
ATOM   3732 C  CG2 . ILE   B 1 176 ? 26.038  12.311  23.044  1.00 46.74  ? 1028 ILE   B CG2 1 
ATOM   3733 C  CD1 . ILE   B 1 176 ? 23.295  11.525  22.230  1.00 43.49  ? 1028 ILE   B CD1 1 
ATOM   3734 N  N   . GLU   B 1 177 ? 28.855  13.108  21.692  1.00 54.80  ? 1029 GLU   B N   1 
ATOM   3735 C  CA  . GLU   B 1 177 ? 30.159  13.007  22.369  1.00 61.11  ? 1029 GLU   B CA  1 
ATOM   3736 C  C   . GLU   B 1 177 ? 30.067  12.213  23.678  1.00 64.24  ? 1029 GLU   B C   1 
ATOM   3737 O  O   . GLU   B 1 177 ? 29.087  12.337  24.419  1.00 65.54  ? 1029 GLU   B O   1 
ATOM   3738 C  CB  . GLU   B 1 177 ? 30.737  14.396  22.638  1.00 64.62  ? 1029 GLU   B CB  1 
ATOM   3739 C  CG  . GLU   B 1 177 ? 31.232  15.078  21.379  1.00 68.68  ? 1029 GLU   B CG  1 
ATOM   3740 C  CD  . GLU   B 1 177 ? 31.624  16.522  21.591  1.00 77.35  ? 1029 GLU   B CD  1 
ATOM   3741 O  OE1 . GLU   B 1 177 ? 31.977  16.906  22.735  1.00 81.47  ? 1029 GLU   B OE1 1 
ATOM   3742 O  OE2 . GLU   B 1 177 ? 31.585  17.272  20.593  1.00 81.65  ? 1029 GLU   B OE2 1 
ATOM   3743 N  N   . THR   B 1 178 ? 31.084  11.390  23.949  1.00 66.79  ? 1030 THR   B N   1 
ATOM   3744 C  CA  . THR   B 1 178 ? 31.156  10.632  25.205  1.00 70.37  ? 1030 THR   B CA  1 
ATOM   3745 C  C   . THR   B 1 178 ? 31.257  11.614  26.372  1.00 73.50  ? 1030 THR   B C   1 
ATOM   3746 O  O   . THR   B 1 178 ? 31.932  12.642  26.261  1.00 74.76  ? 1030 THR   B O   1 
ATOM   3747 C  CB  . THR   B 1 178 ? 32.355  9.660   25.236  1.00 72.99  ? 1030 THR   B CB  1 
ATOM   3748 O  OG1 . THR   B 1 178 ? 32.268  8.768   24.107  0.00 69.40  ? 1030 THR   B OG1 1 
ATOM   3749 C  CG2 . THR   B 1 178 ? 32.304  8.773   26.515  0.00 75.98  ? 1030 THR   B CG2 1 
ATOM   3750 N  N   . ASP   B 1 179 ? 30.554  11.294  27.463  1.00 76.74  ? 1031 ASP   B N   1 
ATOM   3751 C  CA  . ASP   B 1 179 ? 30.371  12.190  28.631  1.00 80.44  ? 1031 ASP   B CA  1 
ATOM   3752 C  C   . ASP   B 1 179 ? 29.528  13.456  28.339  1.00 79.26  ? 1031 ASP   B C   1 
ATOM   3753 O  O   . ASP   B 1 179 ? 29.580  14.420  29.104  1.00 84.36  ? 1031 ASP   B O   1 
ATOM   3754 C  CB  . ASP   B 1 179 ? 31.723  12.564  29.267  1.00 84.04  ? 1031 ASP   B CB  1 
ATOM   3755 C  CG  . ASP   B 1 179 ? 32.601  11.356  29.555  0.00 86.41  ? 1031 ASP   B CG  1 
ATOM   3756 O  OD1 . ASP   B 1 179 ? 32.068  10.280  29.904  0.00 85.85  ? 1031 ASP   B OD1 1 
ATOM   3757 O  OD2 . ASP   B 1 179 ? 33.836  11.486  29.424  0.00 88.06  ? 1031 ASP   B OD2 1 
ATOM   3758 N  N   . LYS   B 1 180 ? 28.752  13.437  27.248  1.00 74.13  ? 1032 LYS   B N   1 
ATOM   3759 C  CA  . LYS   B 1 180 ? 27.824  14.523  26.891  1.00 70.95  ? 1032 LYS   B CA  1 
ATOM   3760 C  C   . LYS   B 1 180 ? 26.493  13.907  26.479  1.00 65.99  ? 1032 LYS   B C   1 
ATOM   3761 O  O   . LYS   B 1 180 ? 26.449  12.755  26.031  1.00 65.05  ? 1032 LYS   B O   1 
ATOM   3762 C  CB  . LYS   B 1 180 ? 28.376  15.400  25.759  1.00 69.04  ? 1032 LYS   B CB  1 
ATOM   3763 C  CG  . LYS   B 1 180 ? 29.733  16.047  26.025  1.00 72.70  ? 1032 LYS   B CG  1 
ATOM   3764 C  CD  . LYS   B 1 180 ? 29.675  17.123  27.108  1.00 80.64  ? 1032 LYS   B CD  1 
ATOM   3765 C  CE  . LYS   B 1 180 ? 28.991  18.408  26.642  0.00 80.46  ? 1032 LYS   B CE  1 
ATOM   3766 N  NZ  . LYS   B 1 180 ? 29.092  19.502  27.647  0.00 85.46  ? 1032 LYS   B NZ  1 
ATOM   3767 N  N   . GLU   B 1 181 ? 25.417  14.675  26.631  1.00 64.35  ? 1033 GLU   B N   1 
ATOM   3768 C  CA  . GLU   B 1 181 ? 24.045  14.169  26.446  1.00 61.83  ? 1033 GLU   B CA  1 
ATOM   3769 C  C   . GLU   B 1 181 ? 23.351  14.621  25.154  1.00 56.76  ? 1033 GLU   B C   1 
ATOM   3770 O  O   . GLU   B 1 181 ? 22.302  14.068  24.805  1.00 55.32  ? 1033 GLU   B O   1 
ATOM   3771 C  CB  . GLU   B 1 181 ? 23.179  14.536  27.663  1.00 63.82  ? 1033 GLU   B CB  1 
ATOM   3772 C  CG  . GLU   B 1 181 ? 23.598  13.830  28.952  1.00 71.77  ? 1033 GLU   B CG  1 
ATOM   3773 C  CD  . GLU   B 1 181 ? 22.617  14.037  30.094  0.00 74.15  ? 1033 GLU   B CD  1 
ATOM   3774 O  OE1 . GLU   B 1 181 ? 22.057  15.148  30.217  0.00 75.87  ? 1033 GLU   B OE1 1 
ATOM   3775 O  OE2 . GLU   B 1 181 ? 22.410  13.087  30.878  0.00 75.70  ? 1033 GLU   B OE2 1 
HETATM 3776 N  N   . PTR   B 1 182 ? 23.915  15.610  24.454  1.00 55.11  ? 1034 PTR   B N   1 
HETATM 3777 C  CA  . PTR   B 1 182 ? 23.350  16.069  23.174  1.00 49.81  ? 1034 PTR   B CA  1 
HETATM 3778 C  C   . PTR   B 1 182 ? 24.378  16.457  22.107  1.00 47.90  ? 1034 PTR   B C   1 
HETATM 3779 O  O   . PTR   B 1 182 ? 25.559  16.601  22.395  1.00 50.78  ? 1034 PTR   B O   1 
HETATM 3780 C  CB  . PTR   B 1 182 ? 22.363  17.221  23.407  1.00 52.81  ? 1034 PTR   B CB  1 
HETATM 3781 C  CG  . PTR   B 1 182 ? 22.932  18.491  24.031  1.00 56.49  ? 1034 PTR   B CG  1 
HETATM 3782 C  CD1 . PTR   B 1 182 ? 22.847  18.714  25.403  1.00 62.37  ? 1034 PTR   B CD1 1 
HETATM 3783 C  CD2 . PTR   B 1 182 ? 23.478  19.499  23.240  1.00 55.19  ? 1034 PTR   B CD2 1 
HETATM 3784 C  CE1 . PTR   B 1 182 ? 23.335  19.884  25.981  1.00 67.49  ? 1034 PTR   B CE1 1 
HETATM 3785 C  CE2 . PTR   B 1 182 ? 23.975  20.670  23.802  1.00 64.09  ? 1034 PTR   B CE2 1 
HETATM 3786 C  CZ  . PTR   B 1 182 ? 23.911  20.860  25.173  1.00 68.79  ? 1034 PTR   B CZ  1 
HETATM 3787 O  OH  . PTR   B 1 182 ? 24.340  21.925  25.628  1.00 74.77  ? 1034 PTR   B OH  1 
HETATM 3788 P  P   . PTR   B 1 182 ? 25.490  22.055  26.751  1.00 81.28  ? 1034 PTR   B P   1 
HETATM 3789 O  O1P . PTR   B 1 182 ? 26.720  21.232  26.327  1.00 82.47  ? 1034 PTR   B O1P 1 
HETATM 3790 O  O2P . PTR   B 1 182 ? 25.868  23.481  26.838  1.00 80.13  ? 1034 PTR   B O2P 1 
HETATM 3791 O  O3P . PTR   B 1 182 ? 24.933  21.564  28.100  1.00 73.26  ? 1034 PTR   B O3P 1 
HETATM 3792 N  N   . PTR   B 1 183 ? 23.893  16.598  20.873  1.00 43.22  ? 1035 PTR   B N   1 
HETATM 3793 C  CA  . PTR   B 1 183 ? 24.640  17.151  19.751  1.00 41.73  ? 1035 PTR   B CA  1 
HETATM 3794 C  C   . PTR   B 1 183 ? 24.020  18.509  19.446  1.00 44.11  ? 1035 PTR   B C   1 
HETATM 3795 O  O   . PTR   B 1 183 ? 22.788  18.630  19.420  1.00 42.20  ? 1035 PTR   B O   1 
HETATM 3796 C  CB  . PTR   B 1 183 ? 24.523  16.258  18.501  1.00 38.56  ? 1035 PTR   B CB  1 
HETATM 3797 C  CG  . PTR   B 1 183 ? 25.150  16.857  17.255  1.00 36.99  ? 1035 PTR   B CG  1 
HETATM 3798 C  CD1 . PTR   B 1 183 ? 24.364  17.500  16.290  1.00 31.53  ? 1035 PTR   B CD1 1 
HETATM 3799 C  CD2 . PTR   B 1 183 ? 26.523  16.781  17.037  1.00 43.56  ? 1035 PTR   B CD2 1 
HETATM 3800 C  CE1 . PTR   B 1 183 ? 24.939  18.066  15.154  1.00 41.31  ? 1035 PTR   B CE1 1 
HETATM 3801 C  CE2 . PTR   B 1 183 ? 27.111  17.341  15.904  1.00 44.83  ? 1035 PTR   B CE2 1 
HETATM 3802 C  CZ  . PTR   B 1 183 ? 26.314  17.985  14.950  1.00 44.05  ? 1035 PTR   B CZ  1 
HETATM 3803 O  OH  . PTR   B 1 183 ? 26.745  18.516  13.901  1.00 43.44  ? 1035 PTR   B OH  1 
HETATM 3804 P  P   . PTR   B 1 183 ? 28.271  18.739  13.395  1.00 51.91  ? 1035 PTR   B P   1 
HETATM 3805 O  O1P . PTR   B 1 183 ? 28.273  19.753  12.236  1.00 46.31  ? 1035 PTR   B O1P 1 
HETATM 3806 O  O2P . PTR   B 1 183 ? 29.174  19.266  14.507  1.00 45.69  ? 1035 PTR   B O2P 1 
HETATM 3807 O  O3P . PTR   B 1 183 ? 28.794  17.431  12.929  1.00 48.14  ? 1035 PTR   B O3P 1 
ATOM   3808 N  N   . THR   B 1 184 ? 24.865  19.519  19.206  1.00 46.76  ? 1036 THR   B N   1 
ATOM   3809 C  CA  . THR   B 1 184 ? 24.407  20.880  18.898  1.00 49.74  ? 1036 THR   B CA  1 
ATOM   3810 C  C   . THR   B 1 184 ? 24.323  21.135  17.389  1.00 48.06  ? 1036 THR   B C   1 
ATOM   3811 O  O   . THR   B 1 184 ? 25.341  21.128  16.707  1.00 45.62  ? 1036 THR   B O   1 
ATOM   3812 C  CB  . THR   B 1 184 ? 25.330  21.931  19.536  1.00 54.34  ? 1036 THR   B CB  1 
ATOM   3813 O  OG1 . THR   B 1 184 ? 25.405  21.694  20.946  1.00 60.35  ? 1036 THR   B OG1 1 
ATOM   3814 C  CG2 . THR   B 1 184 ? 24.820  23.348  19.281  1.00 59.28  ? 1036 THR   B CG2 1 
ATOM   3815 N  N   . VAL   B 1 185 ? 23.117  21.435  16.903  1.00 49.10  ? 1037 VAL   B N   1 
ATOM   3816 C  CA  . VAL   B 1 185 ? 22.848  21.640  15.468  1.00 49.92  ? 1037 VAL   B CA  1 
ATOM   3817 C  C   . VAL   B 1 185 ? 23.326  23.017  14.975  1.00 53.40  ? 1037 VAL   B C   1 
ATOM   3818 O  O   . VAL   B 1 185 ? 23.114  24.025  15.652  1.00 56.85  ? 1037 VAL   B O   1 
ATOM   3819 C  CB  . VAL   B 1 185 ? 21.323  21.538  15.158  1.00 50.14  ? 1037 VAL   B CB  1 
ATOM   3820 C  CG1 . VAL   B 1 185 ? 21.030  21.756  13.662  1.00 50.42  ? 1037 VAL   B CG1 1 
ATOM   3821 C  CG2 . VAL   B 1 185 ? 20.758  20.185  15.603  1.00 50.08  ? 1037 VAL   B CG2 1 
ATOM   3822 N  N   . LYS   B 1 186 ? 23.923  23.042  13.779  1.00 52.02  ? 1038 LYS   B N   1 
ATOM   3823 C  CA  . LYS   B 1 186 ? 24.324  24.281  13.096  1.00 56.24  ? 1038 LYS   B CA  1 
ATOM   3824 C  C   . LYS   B 1 186 ? 23.477  24.534  11.835  1.00 55.85  ? 1038 LYS   B C   1 
ATOM   3825 O  O   . LYS   B 1 186 ? 22.832  25.574  11.733  1.00 60.33  ? 1038 LYS   B O   1 
ATOM   3826 C  CB  . LYS   B 1 186 ? 25.814  24.247  12.746  1.00 56.28  ? 1038 LYS   B CB  1 
ATOM   3827 C  CG  . LYS   B 1 186 ? 26.742  24.156  13.966  1.00 59.66  ? 1038 LYS   B CG  1 
ATOM   3828 C  CD  . LYS   B 1 186 ? 27.078  22.712  14.336  1.00 58.15  ? 1038 LYS   B CD  1 
ATOM   3829 C  CE  . LYS   B 1 186 ? 27.832  22.616  15.656  1.00 58.34  ? 1038 LYS   B CE  1 
ATOM   3830 N  NZ  . LYS   B 1 186 ? 27.901  21.194  16.126  1.00 50.11  ? 1038 LYS   B NZ  1 
ATOM   3831 N  N   . ASP   B 1 187 ? 23.487  23.601  10.882  1.00 51.34  ? 1039 ASP   B N   1 
ATOM   3832 C  CA  . ASP   B 1 187 ? 22.654  23.714  9.673   1.00 50.84  ? 1039 ASP   B CA  1 
ATOM   3833 C  C   . ASP   B 1 187 ? 21.254  23.160  9.965   1.00 49.61  ? 1039 ASP   B C   1 
ATOM   3834 O  O   . ASP   B 1 187 ? 21.104  21.979  10.296  1.00 44.63  ? 1039 ASP   B O   1 
ATOM   3835 C  CB  . ASP   B 1 187 ? 23.290  22.980  8.488   1.00 51.86  ? 1039 ASP   B CB  1 
ATOM   3836 C  CG  . ASP   B 1 187 ? 22.427  23.034  7.225   1.00 54.38  ? 1039 ASP   B CG  1 
ATOM   3837 O  OD1 . ASP   B 1 187 ? 21.854  24.100  6.921   0.00 56.27  ? 1039 ASP   B OD1 1 
ATOM   3838 O  OD2 . ASP   B 1 187 ? 22.367  22.011  6.499   0.00 51.36  ? 1039 ASP   B OD2 1 
ATOM   3839 N  N   . ASP   B 1 188 ? 20.236  24.017  9.835   1.00 50.53  ? 1040 ASP   B N   1 
ATOM   3840 C  CA  . ASP   B 1 188 ? 18.844  23.674  10.221  1.00 47.57  ? 1040 ASP   B CA  1 
ATOM   3841 C  C   . ASP   B 1 188 ? 17.732  24.164  9.266   1.00 48.40  ? 1040 ASP   B C   1 
ATOM   3842 O  O   . ASP   B 1 188 ? 16.540  24.068  9.603   1.00 48.03  ? 1040 ASP   B O   1 
ATOM   3843 C  CB  . ASP   B 1 188 ? 18.585  24.177  11.649  1.00 47.48  ? 1040 ASP   B CB  1 
ATOM   3844 C  CG  . ASP   B 1 188 ? 18.874  25.672  11.825  1.00 54.45  ? 1040 ASP   B CG  1 
ATOM   3845 O  OD1 . ASP   B 1 188 ? 19.272  26.361  10.860  1.00 46.86  ? 1040 ASP   B OD1 1 
ATOM   3846 O  OD2 . ASP   B 1 188 ? 18.722  26.154  12.959  1.00 56.34  ? 1040 ASP   B OD2 1 
ATOM   3847 N  N   . ARG   B 1 189 ? 18.119  24.625  8.072   1.00 51.09  ? 1041 ARG   B N   1 
ATOM   3848 C  CA  . ARG   B 1 189 ? 17.204  25.260  7.102   1.00 55.09  ? 1041 ARG   B CA  1 
ATOM   3849 C  C   . ARG   B 1 189 ? 16.055  24.334  6.678   1.00 54.37  ? 1041 ARG   B C   1 
ATOM   3850 O  O   . ARG   B 1 189 ? 14.904  24.769  6.586   1.00 54.33  ? 1041 ARG   B O   1 
ATOM   3851 C  CB  . ARG   B 1 189 ? 17.963  25.721  5.841   1.00 55.94  ? 1041 ARG   B CB  1 
ATOM   3852 C  CG  . ARG   B 1 189 ? 19.054  26.724  6.074   1.00 61.05  ? 1041 ARG   B CG  1 
ATOM   3853 C  CD  . ARG   B 1 189 ? 19.515  27.323  4.721   0.00 63.81  ? 1041 ARG   B CD  1 
ATOM   3854 N  NE  . ARG   B 1 189 ? 20.306  26.359  3.951   0.00 61.62  ? 1041 ARG   B NE  1 
ATOM   3855 C  CZ  . ARG   B 1 189 ? 21.593  26.061  4.161   0.00 60.60  ? 1041 ARG   B CZ  1 
ATOM   3856 N  NH1 . ARG   B 1 189 ? 22.294  26.639  5.136   0.00 61.67  ? 1041 ARG   B NH1 1 
ATOM   3857 N  NH2 . ARG   B 1 189 ? 22.193  25.164  3.383   0.00 58.73  ? 1041 ARG   B NH2 1 
ATOM   3858 N  N   . ASP   B 1 190 ? 16.379  23.063  6.433   1.00 50.43  ? 1042 ASP   B N   1 
ATOM   3859 C  CA  . ASP   B 1 190 ? 15.399  22.070  5.989   1.00 48.09  ? 1042 ASP   B CA  1 
ATOM   3860 C  C   . ASP   B 1 190 ? 15.034  21.102  7.121   1.00 45.54  ? 1042 ASP   B C   1 
ATOM   3861 O  O   . ASP   B 1 190 ? 14.819  19.920  6.870   1.00 45.38  ? 1042 ASP   B O   1 
ATOM   3862 C  CB  . ASP   B 1 190 ? 15.939  21.295  4.772   1.00 48.17  ? 1042 ASP   B CB  1 
ATOM   3863 C  CG  . ASP   B 1 190 ? 16.512  22.213  3.682   1.00 54.97  ? 1042 ASP   B CG  1 
ATOM   3864 O  OD1 . ASP   B 1 190 ? 15.906  23.263  3.390   1.00 55.87  ? 1042 ASP   B OD1 1 
ATOM   3865 O  OD2 . ASP   B 1 190 ? 17.581  21.881  3.119   1.00 61.30  ? 1042 ASP   B OD2 1 
ATOM   3866 N  N   . SER   B 1 191 ? 14.947  21.598  8.360   1.00 43.96  ? 1043 SER   B N   1 
ATOM   3867 C  CA  . SER   B 1 191 ? 14.563  20.762  9.515   1.00 42.40  ? 1043 SER   B CA  1 
ATOM   3868 C  C   . SER   B 1 191 ? 13.103  20.308  9.389   1.00 39.85  ? 1043 SER   B C   1 
ATOM   3869 O  O   . SER   B 1 191 ? 12.258  21.129  9.015   1.00 42.66  ? 1043 SER   B O   1 
ATOM   3870 C  CB  . SER   B 1 191 ? 14.696  21.546  10.824  1.00 44.08  ? 1043 SER   B CB  1 
ATOM   3871 O  OG  . SER   B 1 191 ? 16.017  21.974  11.052  1.00 46.19  ? 1043 SER   B OG  1 
ATOM   3872 N  N   . PRO   B 1 192 ? 12.802  19.018  9.690   1.00 36.70  ? 1044 PRO   B N   1 
ATOM   3873 C  CA  . PRO   B 1 192 ? 11.427  18.517  9.745   1.00 34.79  ? 1044 PRO   B CA  1 
ATOM   3874 C  C   . PRO   B 1 192 ? 10.786  18.909  11.083  1.00 33.12  ? 1044 PRO   B C   1 
ATOM   3875 O  O   . PRO   B 1 192 ? 10.595  18.082  11.986  1.00 29.89  ? 1044 PRO   B O   1 
ATOM   3876 C  CB  . PRO   B 1 192 ? 11.610  17.001  9.601   1.00 32.20  ? 1044 PRO   B CB  1 
ATOM   3877 C  CG  . PRO   B 1 192 ? 12.883  16.735  10.293  1.00 32.94  ? 1044 PRO   B CG  1 
ATOM   3878 C  CD  . PRO   B 1 192 ? 13.764  17.935  9.988   1.00 36.35  ? 1044 PRO   B CD  1 
ATOM   3879 N  N   . VAL   B 1 193 ? 10.456  20.194  11.183  1.00 35.94  ? 1045 VAL   B N   1 
ATOM   3880 C  CA  . VAL   B 1 193 ? 10.056  20.819  12.447  1.00 38.59  ? 1045 VAL   B CA  1 
ATOM   3881 C  C   . VAL   B 1 193 ? 8.839   20.188  13.130  1.00 36.96  ? 1045 VAL   B C   1 
ATOM   3882 O  O   . VAL   B 1 193 ? 8.765   20.139  14.354  1.00 38.53  ? 1045 VAL   B O   1 
ATOM   3883 C  CB  . VAL   B 1 193 ? 9.804   22.349  12.273  1.00 42.54  ? 1045 VAL   B CB  1 
ATOM   3884 C  CG1 . VAL   B 1 193 ? 11.084  23.056  11.903  1.00 45.54  ? 1045 VAL   B CG1 1 
ATOM   3885 C  CG2 . VAL   B 1 193 ? 8.706   22.648  11.233  1.00 45.30  ? 1045 VAL   B CG2 1 
ATOM   3886 N  N   . PHE   B 1 194 ? 7.905   19.686  12.341  1.00 37.63  ? 1046 PHE   B N   1 
ATOM   3887 C  CA  . PHE   B 1 194 ? 6.699   19.045  12.894  1.00 37.25  ? 1046 PHE   B CA  1 
ATOM   3888 C  C   . PHE   B 1 194 ? 6.955   17.659  13.515  1.00 33.03  ? 1046 PHE   B C   1 
ATOM   3889 O  O   . PHE   B 1 194 ? 6.074   17.109  14.140  1.00 30.52  ? 1046 PHE   B O   1 
ATOM   3890 C  CB  . PHE   B 1 194 ? 5.590   19.037  11.836  1.00 38.23  ? 1046 PHE   B CB  1 
ATOM   3891 C  CG  . PHE   B 1 194 ? 5.188   20.427  11.403  1.00 45.10  ? 1046 PHE   B CG  1 
ATOM   3892 C  CD1 . PHE   B 1 194 ? 4.589   21.296  12.312  1.00 45.14  ? 1046 PHE   B CD1 1 
ATOM   3893 C  CD2 . PHE   B 1 194 ? 5.438   20.881  10.108  1.00 42.41  ? 1046 PHE   B CD2 1 
ATOM   3894 C  CE1 . PHE   B 1 194 ? 4.231   22.598  11.940  1.00 51.64  ? 1046 PHE   B CE1 1 
ATOM   3895 C  CE2 . PHE   B 1 194 ? 5.087   22.181  9.725   1.00 51.51  ? 1046 PHE   B CE2 1 
ATOM   3896 C  CZ  . PHE   B 1 194 ? 4.475   23.039  10.640  1.00 53.33  ? 1046 PHE   B CZ  1 
ATOM   3897 N  N   . TRP   B 1 195 ? 8.176   17.146  13.375  1.00 30.68  ? 1047 TRP   B N   1 
ATOM   3898 C  CA  . TRP   B 1 195 ? 8.637   15.935  14.058  1.00 26.92  ? 1047 TRP   B CA  1 
ATOM   3899 C  C   . TRP   B 1 195 ? 9.565   16.226  15.240  1.00 26.09  ? 1047 TRP   B C   1 
ATOM   3900 O  O   . TRP   B 1 195 ? 9.980   15.312  15.942  1.00 24.73  ? 1047 TRP   B O   1 
ATOM   3901 C  CB  . TRP   B 1 195 ? 9.338   15.018  13.037  1.00 26.65  ? 1047 TRP   B CB  1 
ATOM   3902 C  CG  . TRP   B 1 195 ? 8.383   14.221  12.204  1.00 26.36  ? 1047 TRP   B CG  1 
ATOM   3903 C  CD1 . TRP   B 1 195 ? 8.107   12.896  12.338  1.00 23.66  ? 1047 TRP   B CD1 1 
ATOM   3904 C  CD2 . TRP   B 1 195 ? 7.580   14.690  11.112  1.00 25.10  ? 1047 TRP   B CD2 1 
ATOM   3905 N  NE1 . TRP   B 1 195 ? 7.193   12.508  11.408  1.00 26.65  ? 1047 TRP   B NE1 1 
ATOM   3906 C  CE2 . TRP   B 1 195 ? 6.846   13.582  10.634  1.00 30.43  ? 1047 TRP   B CE2 1 
ATOM   3907 C  CE3 . TRP   B 1 195 ? 7.403   15.937  10.492  1.00 34.52  ? 1047 TRP   B CE3 1 
ATOM   3908 C  CZ2 . TRP   B 1 195 ? 5.936   13.683  9.566   1.00 23.66  ? 1047 TRP   B CZ2 1 
ATOM   3909 C  CZ3 . TRP   B 1 195 ? 6.502   16.037  9.425   1.00 29.79  ? 1047 TRP   B CZ3 1 
ATOM   3910 C  CH2 . TRP   B 1 195 ? 5.795   14.906  8.966   1.00 28.88  ? 1047 TRP   B CH2 1 
ATOM   3911 N  N   . TYR   B 1 196 ? 9.869   17.504  15.479  1.00 30.75  ? 1048 TYR   B N   1 
ATOM   3912 C  CA  . TYR   B 1 196 ? 10.972  17.903  16.353  1.00 31.59  ? 1048 TYR   B CA  1 
ATOM   3913 C  C   . TYR   B 1 196 ? 10.559  18.314  17.771  1.00 35.83  ? 1048 TYR   B C   1 
ATOM   3914 O  O   . TYR   B 1 196 ? 9.577   19.040  17.969  1.00 37.68  ? 1048 TYR   B O   1 
ATOM   3915 C  CB  . TYR   B 1 196 ? 11.780  19.041  15.676  1.00 34.17  ? 1048 TYR   B CB  1 
ATOM   3916 C  CG  . TYR   B 1 196 ? 12.984  18.600  14.848  1.00 30.20  ? 1048 TYR   B CG  1 
ATOM   3917 C  CD1 . TYR   B 1 196 ? 13.090  17.305  14.325  1.00 23.53  ? 1048 TYR   B CD1 1 
ATOM   3918 C  CD2 . TYR   B 1 196 ? 14.008  19.502  14.555  1.00 33.67  ? 1048 TYR   B CD2 1 
ATOM   3919 C  CE1 . TYR   B 1 196 ? 14.177  16.919  13.597  1.00 22.79  ? 1048 TYR   B CE1 1 
ATOM   3920 C  CE2 . TYR   B 1 196 ? 15.124  19.109  13.788  1.00 30.04  ? 1048 TYR   B CE2 1 
ATOM   3921 C  CZ  . TYR   B 1 196 ? 15.181  17.805  13.316  1.00 29.95  ? 1048 TYR   B CZ  1 
ATOM   3922 O  OH  . TYR   B 1 196 ? 16.237  17.364  12.563  1.00 36.50  ? 1048 TYR   B OH  1 
ATOM   3923 N  N   . ALA   B 1 197 ? 11.332  17.849  18.752  1.00 35.92  ? 1049 ALA   B N   1 
ATOM   3924 C  CA  . ALA   B 1 197 ? 11.091  18.181  20.156  1.00 38.43  ? 1049 ALA   B CA  1 
ATOM   3925 C  C   . ALA   B 1 197 ? 11.352  19.665  20.437  1.00 42.72  ? 1049 ALA   B C   1 
ATOM   3926 O  O   . ALA   B 1 197 ? 12.071  20.326  19.675  1.00 40.55  ? 1049 ALA   B O   1 
ATOM   3927 C  CB  . ALA   B 1 197 ? 11.958  17.313  21.053  1.00 38.82  ? 1049 ALA   B CB  1 
ATOM   3928 N  N   . PRO   B 1 198 ? 10.749  20.209  21.520  1.00 46.22  ? 1050 PRO   B N   1 
ATOM   3929 C  CA  . PRO   B 1 198 ? 10.953  21.608  21.901  1.00 49.42  ? 1050 PRO   B CA  1 
ATOM   3930 C  C   . PRO   B 1 198 ? 12.418  22.060  22.021  1.00 47.29  ? 1050 PRO   B C   1 
ATOM   3931 O  O   . PRO   B 1 198 ? 12.767  23.100  21.479  1.00 48.44  ? 1050 PRO   B O   1 
ATOM   3932 C  CB  . PRO   B 1 198 ? 10.229  21.707  23.251  1.00 56.16  ? 1050 PRO   B CB  1 
ATOM   3933 C  CG  . PRO   B 1 198 ? 9.185   20.654  23.188  1.00 49.52  ? 1050 PRO   B CG  1 
ATOM   3934 C  CD  . PRO   B 1 198 ? 9.781   19.539  22.417  1.00 49.01  ? 1050 PRO   B CD  1 
ATOM   3935 N  N   . GLU   B 1 199 ? 13.250  21.287  22.716  1.00 46.14  ? 1051 GLU   B N   1 
ATOM   3936 C  CA  . GLU   B 1 199 ? 14.676  21.620  22.870  1.00 50.49  ? 1051 GLU   B CA  1 
ATOM   3937 C  C   . GLU   B 1 199 ? 15.417  21.766  21.525  1.00 47.65  ? 1051 GLU   B C   1 
ATOM   3938 O  O   . GLU   B 1 199 ? 16.288  22.635  21.393  1.00 51.68  ? 1051 GLU   B O   1 
ATOM   3939 C  CB  . GLU   B 1 199 ? 15.408  20.643  23.819  1.00 51.20  ? 1051 GLU   B CB  1 
ATOM   3940 C  CG  . GLU   B 1 199 ? 15.629  19.198  23.328  1.00 40.05  ? 1051 GLU   B CG  1 
ATOM   3941 C  CD  . GLU   B 1 199 ? 14.394  18.306  23.432  1.00 42.00  ? 1051 GLU   B CD  1 
ATOM   3942 O  OE1 . GLU   B 1 199 ? 13.327  18.795  23.863  1.00 50.91  ? 1051 GLU   B OE1 1 
ATOM   3943 O  OE2 . GLU   B 1 199 ? 14.494  17.119  23.059  1.00 43.34  ? 1051 GLU   B OE2 1 
ATOM   3944 N  N   . CYS   B 1 200 ? 15.046  20.941  20.540  1.00 43.12  ? 1052 CYS   B N   1 
ATOM   3945 C  CA  . CYS   B 1 200 ? 15.579  21.043  19.162  1.00 40.50  ? 1052 CYS   B CA  1 
ATOM   3946 C  C   . CYS   B 1 200 ? 15.157  22.350  18.502  1.00 43.78  ? 1052 CYS   B C   1 
ATOM   3947 O  O   . CYS   B 1 200 ? 15.992  23.064  17.956  1.00 45.30  ? 1052 CYS   B O   1 
ATOM   3948 C  CB  . CYS   B 1 200 ? 15.103  19.883  18.281  1.00 36.37  ? 1052 CYS   B CB  1 
ATOM   3949 S  SG  . CYS   B 1 200 ? 15.180  18.275  19.037  1.00 37.73  ? 1052 CYS   B SG  1 
ATOM   3950 N  N   . LEU   B 1 201 ? 13.864  22.666  18.578  1.00 43.98  ? 1053 LEU   B N   1 
ATOM   3951 C  CA  . LEU   B 1 201 ? 13.318  23.878  17.963  1.00 46.77  ? 1053 LEU   B CA  1 
ATOM   3952 C  C   . LEU   B 1 201 ? 13.774  25.136  18.702  1.00 53.44  ? 1053 LEU   B C   1 
ATOM   3953 O  O   . LEU   B 1 201 ? 14.027  26.165  18.067  1.00 55.50  ? 1053 LEU   B O   1 
ATOM   3954 C  CB  . LEU   B 1 201 ? 11.780  23.837  17.922  1.00 47.96  ? 1053 LEU   B CB  1 
ATOM   3955 C  CG  . LEU   B 1 201 ? 11.069  22.757  17.087  1.00 45.37  ? 1053 LEU   B CG  1 
ATOM   3956 C  CD1 . LEU   B 1 201 ? 9.581   22.758  17.388  1.00 45.10  ? 1053 LEU   B CD1 1 
ATOM   3957 C  CD2 . LEU   B 1 201 ? 11.287  22.927  15.591  1.00 43.62  ? 1053 LEU   B CD2 1 
ATOM   3958 N  N   . MET   B 1 202 ? 13.893  25.054  20.030  1.00 57.42  ? 1054 MET   B N   1 
ATOM   3959 C  CA  . MET   B 1 202 ? 14.217  26.232  20.858  1.00 62.97  ? 1054 MET   B CA  1 
ATOM   3960 C  C   . MET   B 1 202 ? 15.721  26.504  21.017  1.00 65.31  ? 1054 MET   B C   1 
ATOM   3961 O  O   . MET   B 1 202 ? 16.151  27.654  20.896  1.00 70.28  ? 1054 MET   B O   1 
ATOM   3962 C  CB  . MET   B 1 202 ? 13.570  26.109  22.246  1.00 66.15  ? 1054 MET   B CB  1 
ATOM   3963 C  CG  . MET   B 1 202 ? 12.049  26.168  22.215  1.00 65.60  ? 1054 MET   B CG  1 
ATOM   3964 S  SD  . MET   B 1 202 ? 11.261  26.154  23.835  1.00 73.62  ? 1054 MET   B SD  1 
ATOM   3965 C  CE  . MET   B 1 202 ? 11.908  24.674  24.606  1.00 56.12  ? 1054 MET   B CE  1 
ATOM   3966 N  N   . GLN   B 1 203 ? 16.493  25.459  21.320  1.00 62.67  ? 1055 GLN   B N   1 
ATOM   3967 C  CA  . GLN   B 1 203 ? 17.933  25.572  21.628  1.00 67.43  ? 1055 GLN   B CA  1 
ATOM   3968 C  C   . GLN   B 1 203 ? 18.873  24.908  20.599  1.00 64.43  ? 1055 GLN   B C   1 
ATOM   3969 O  O   . GLN   B 1 203 ? 20.093  24.995  20.751  1.00 68.14  ? 1055 GLN   B O   1 
ATOM   3970 C  CB  . GLN   B 1 203 ? 18.213  24.961  23.007  1.00 69.31  ? 1055 GLN   B CB  1 
ATOM   3971 C  CG  . GLN   B 1 203 ? 17.573  25.694  24.186  1.00 75.84  ? 1055 GLN   B CG  1 
ATOM   3972 C  CD  . GLN   B 1 203 ? 17.329  24.768  25.373  1.00 79.95  ? 1055 GLN   B CD  1 
ATOM   3973 O  OE1 . GLN   B 1 203 ? 16.317  24.054  25.429  1.00 78.14  ? 1055 GLN   B OE1 1 
ATOM   3974 N  NE2 . GLN   B 1 203 ? 18.265  24.766  26.321  1.00 79.47  ? 1055 GLN   B NE2 1 
ATOM   3975 N  N   . SER   B 1 204 ? 18.328  24.259  19.567  1.00 60.81  ? 1056 SER   B N   1 
ATOM   3976 C  CA  . SER   B 1 204 ? 19.138  23.509  18.582  1.00 56.79  ? 1056 SER   B CA  1 
ATOM   3977 C  C   . SER   B 1 204 ? 19.970  22.381  19.228  1.00 56.19  ? 1056 SER   B C   1 
ATOM   3978 O  O   . SER   B 1 204 ? 21.048  22.037  18.736  1.00 56.39  ? 1056 SER   B O   1 
ATOM   3979 C  CB  . SER   B 1 204 ? 20.065  24.450  17.783  1.00 59.30  ? 1056 SER   B CB  1 
ATOM   3980 O  OG  . SER   B 1 204 ? 19.495  25.735  17.591  1.00 61.78  ? 1056 SER   B OG  1 
ATOM   3981 N  N   . LYS   B 1 205 ? 19.459  21.813  20.322  1.00 56.13  ? 1057 LYS   B N   1 
ATOM   3982 C  CA  . LYS   B 1 205 ? 20.101  20.698  21.023  1.00 53.02  ? 1057 LYS   B CA  1 
ATOM   3983 C  C   . LYS   B 1 205 ? 19.346  19.438  20.673  1.00 48.85  ? 1057 LYS   B C   1 
ATOM   3984 O  O   . LYS   B 1 205 ? 18.112  19.447  20.716  1.00 48.15  ? 1057 LYS   B O   1 
ATOM   3985 C  CB  . LYS   B 1 205 ? 20.053  20.918  22.533  1.00 56.06  ? 1057 LYS   B CB  1 
ATOM   3986 C  CG  . LYS   B 1 205 ? 20.790  22.153  22.987  1.00 59.90  ? 1057 LYS   B CG  1 
ATOM   3987 C  CD  . LYS   B 1 205 ? 20.686  22.303  24.511  0.00 63.84  ? 1057 LYS   B CD  1 
ATOM   3988 C  CE  . LYS   B 1 205 ? 21.425  23.543  24.988  0.00 68.31  ? 1057 LYS   B CE  1 
ATOM   3989 N  NZ  . LYS   B 1 205 ? 21.414  23.665  26.473  0.00 72.14  ? 1057 LYS   B NZ  1 
ATOM   3990 N  N   . PHE   B 1 206 ? 20.078  18.371  20.320  1.00 44.90  ? 1058 PHE   B N   1 
ATOM   3991 C  CA  . PHE   B 1 206 ? 19.484  17.075  19.965  1.00 40.15  ? 1058 PHE   B CA  1 
ATOM   3992 C  C   . PHE   B 1 206 ? 19.980  15.917  20.866  1.00 40.22  ? 1058 PHE   B C   1 
ATOM   3993 O  O   . PHE   B 1 206 ? 21.163  15.547  20.847  1.00 38.72  ? 1058 PHE   B O   1 
ATOM   3994 C  CB  . PHE   B 1 206 ? 19.682  16.765  18.469  1.00 34.81  ? 1058 PHE   B CB  1 
ATOM   3995 C  CG  . PHE   B 1 206 ? 18.498  16.076  17.859  1.00 34.16  ? 1058 PHE   B CG  1 
ATOM   3996 C  CD1 . PHE   B 1 206 ? 18.250  14.730  18.135  1.00 32.84  ? 1058 PHE   B CD1 1 
ATOM   3997 C  CD2 . PHE   B 1 206 ? 17.588  16.777  17.064  1.00 37.28  ? 1058 PHE   B CD2 1 
ATOM   3998 C  CE1 . PHE   B 1 206 ? 17.118  14.051  17.585  1.00 25.74  ? 1058 PHE   B CE1 1 
ATOM   3999 C  CE2 . PHE   B 1 206 ? 16.456  16.117  16.517  1.00 33.66  ? 1058 PHE   B CE2 1 
ATOM   4000 C  CZ  . PHE   B 1 206 ? 16.216  14.759  16.803  1.00 28.37  ? 1058 PHE   B CZ  1 
ATOM   4001 N  N   . TYR   B 1 207 ? 19.049  15.377  21.665  1.00 39.83  ? 1059 TYR   B N   1 
ATOM   4002 C  CA  . TYR   B 1 207 ? 19.288  14.266  22.607  1.00 40.02  ? 1059 TYR   B CA  1 
ATOM   4003 C  C   . TYR   B 1 207 ? 18.748  12.937  22.082  1.00 35.79  ? 1059 TYR   B C   1 
ATOM   4004 O  O   . TYR   B 1 207 ? 17.887  12.917  21.194  1.00 34.00  ? 1059 TYR   B O   1 
ATOM   4005 C  CB  . TYR   B 1 207 ? 18.544  14.527  23.935  1.00 42.22  ? 1059 TYR   B CB  1 
ATOM   4006 C  CG  . TYR   B 1 207 ? 18.951  15.741  24.730  1.00 47.04  ? 1059 TYR   B CG  1 
ATOM   4007 C  CD1 . TYR   B 1 207 ? 18.508  17.018  24.375  1.00 43.47  ? 1059 TYR   B CD1 1 
ATOM   4008 C  CD2 . TYR   B 1 207 ? 19.731  15.611  25.884  1.00 49.83  ? 1059 TYR   B CD2 1 
ATOM   4009 C  CE1 . TYR   B 1 207 ? 18.860  18.144  25.141  1.00 45.47  ? 1059 TYR   B CE1 1 
ATOM   4010 C  CE2 . TYR   B 1 207 ? 20.085  16.721  26.647  1.00 52.61  ? 1059 TYR   B CE2 1 
ATOM   4011 C  CZ  . TYR   B 1 207 ? 19.650  17.980  26.259  1.00 51.54  ? 1059 TYR   B CZ  1 
ATOM   4012 O  OH  . TYR   B 1 207 ? 20.005  19.075  26.992  1.00 49.71  ? 1059 TYR   B OH  1 
ATOM   4013 N  N   . ILE   B 1 208 ? 19.194  11.822  22.668  1.00 33.14  ? 1060 ILE   B N   1 
ATOM   4014 C  CA  . ILE   B 1 208 ? 18.493  10.527  22.472  1.00 30.30  ? 1060 ILE   B CA  1 
ATOM   4015 C  C   . ILE   B 1 208 ? 16.981  10.684  22.738  1.00 29.48  ? 1060 ILE   B C   1 
ATOM   4016 O  O   . ILE   B 1 208 ? 16.163  10.203  21.954  1.00 29.30  ? 1060 ILE   B O   1 
ATOM   4017 C  CB  . ILE   B 1 208 ? 19.140  9.330   23.269  1.00 30.28  ? 1060 ILE   B CB  1 
ATOM   4018 C  CG1 . ILE   B 1 208 ? 20.456  8.917   22.610  1.00 32.86  ? 1060 ILE   B CG1 1 
ATOM   4019 C  CG2 . ILE   B 1 208 ? 18.219  8.095   23.303  1.00 32.69  ? 1060 ILE   B CG2 1 
ATOM   4020 C  CD1 . ILE   B 1 208 ? 21.377  8.086   23.468  1.00 40.25  ? 1060 ILE   B CD1 1 
ATOM   4021 N  N   . ALA   B 1 209 ? 16.624  11.426  23.801  1.00 30.71  ? 1061 ALA   B N   1 
ATOM   4022 C  CA  . ALA   B 1 209 ? 15.224  11.756  24.103  1.00 33.53  ? 1061 ALA   B CA  1 
ATOM   4023 C  C   . ALA   B 1 209 ? 14.504  12.560  23.001  1.00 31.48  ? 1061 ALA   B C   1 
ATOM   4024 O  O   . ALA   B 1 209 ? 13.284  12.481  22.851  1.00 29.79  ? 1061 ALA   B O   1 
ATOM   4025 C  CB  . ALA   B 1 209 ? 15.146  12.494  25.443  1.00 37.09  ? 1061 ALA   B CB  1 
ATOM   4026 N  N   . SER   B 1 210 ? 15.262  13.331  22.227  1.00 32.86  ? 1062 SER   B N   1 
ATOM   4027 C  CA  . SER   B 1 210 ? 14.709  14.049  21.070  1.00 31.97  ? 1062 SER   B CA  1 
ATOM   4028 C  C   . SER   B 1 210 ? 14.249  13.088  19.962  1.00 29.86  ? 1062 SER   B C   1 
ATOM   4029 O  O   . SER   B 1 210 ? 13.250  13.344  19.292  1.00 31.31  ? 1062 SER   B O   1 
ATOM   4030 C  CB  . SER   B 1 210 ? 15.746  15.028  20.515  1.00 31.24  ? 1062 SER   B CB  1 
ATOM   4031 O  OG  . SER   B 1 210 ? 16.304  15.801  21.553  1.00 33.74  ? 1062 SER   B OG  1 
ATOM   4032 N  N   . ASP   B 1 211 ? 14.983  11.990  19.786  1.00 28.52  ? 1063 ASP   B N   1 
ATOM   4033 C  CA  . ASP   B 1 211 ? 14.562  10.889  18.900  1.00 24.54  ? 1063 ASP   B CA  1 
ATOM   4034 C  C   . ASP   B 1 211 ? 13.332  10.153  19.441  1.00 22.56  ? 1063 ASP   B C   1 
ATOM   4035 O  O   . ASP   B 1 211 ? 12.510  9.695   18.657  1.00 23.75  ? 1063 ASP   B O   1 
ATOM   4036 C  CB  . ASP   B 1 211 ? 15.689  9.868   18.675  1.00 23.36  ? 1063 ASP   B CB  1 
ATOM   4037 C  CG  . ASP   B 1 211 ? 16.674  10.273  17.582  1.00 26.50  ? 1063 ASP   B CG  1 
ATOM   4038 O  OD1 . ASP   B 1 211 ? 16.347  11.060  16.661  1.00 25.20  ? 1063 ASP   B OD1 1 
ATOM   4039 O  OD2 . ASP   B 1 211 ? 17.796  9.752   17.642  1.00 27.03  ? 1063 ASP   B OD2 1 
ATOM   4040 N  N   . VAL   B 1 212 ? 13.202  10.049  20.764  1.00 24.47  ? 1064 VAL   B N   1 
ATOM   4041 C  CA  . VAL   B 1 212 ? 11.991  9.481   21.369  1.00 21.67  ? 1064 VAL   B CA  1 
ATOM   4042 C  C   . VAL   B 1 212 ? 10.774  10.331  21.012  1.00 25.04  ? 1064 VAL   B C   1 
ATOM   4043 O  O   . VAL   B 1 212 ? 9.754   9.775   20.585  1.00 23.70  ? 1064 VAL   B O   1 
ATOM   4044 C  CB  . VAL   B 1 212 ? 12.111  9.251   22.900  1.00 23.07  ? 1064 VAL   B CB  1 
ATOM   4045 C  CG1 . VAL   B 1 212 ? 10.758  8.855   23.471  1.00 25.00  ? 1064 VAL   B CG1 1 
ATOM   4046 C  CG2 . VAL   B 1 212 ? 13.124  8.145   23.168  1.00 28.02  ? 1064 VAL   B CG2 1 
ATOM   4047 N  N   . TRP   B 1 213 ? 10.896  11.658  21.154  1.00 25.91  ? 1065 TRP   B N   1 
ATOM   4048 C  CA  . TRP   B 1 213 ? 9.871   12.604  20.692  1.00 27.98  ? 1065 TRP   B CA  1 
ATOM   4049 C  C   . TRP   B 1 213 ? 9.451   12.314  19.234  1.00 25.79  ? 1065 TRP   B C   1 
ATOM   4050 O  O   . TRP   B 1 213 ? 8.275   12.078  18.947  1.00 25.06  ? 1065 TRP   B O   1 
ATOM   4051 C  CB  . TRP   B 1 213 ? 10.344  14.052  20.827  1.00 31.15  ? 1065 TRP   B CB  1 
ATOM   4052 C  CG  . TRP   B 1 213 ? 9.302   15.061  20.428  1.00 31.10  ? 1065 TRP   B CG  1 
ATOM   4053 C  CD1 . TRP   B 1 213 ? 8.926   15.385  19.166  1.00 30.29  ? 1065 TRP   B CD1 1 
ATOM   4054 C  CD2 . TRP   B 1 213 ? 8.500   15.867  21.298  1.00 37.38  ? 1065 TRP   B CD2 1 
ATOM   4055 N  NE1 . TRP   B 1 213 ? 7.939   16.313  19.182  1.00 36.31  ? 1065 TRP   B NE1 1 
ATOM   4056 C  CE2 . TRP   B 1 213 ? 7.660   16.646  20.479  1.00 36.53  ? 1065 TRP   B CE2 1 
ATOM   4057 C  CE3 . TRP   B 1 213 ? 8.427   16.028  22.689  1.00 42.55  ? 1065 TRP   B CE3 1 
ATOM   4058 C  CZ2 . TRP   B 1 213 ? 6.737   17.558  20.999  1.00 40.79  ? 1065 TRP   B CZ2 1 
ATOM   4059 C  CZ3 . TRP   B 1 213 ? 7.507   16.930  23.206  1.00 44.20  ? 1065 TRP   B CZ3 1 
ATOM   4060 C  CH2 . TRP   B 1 213 ? 6.682   17.691  22.359  1.00 43.71  ? 1065 TRP   B CH2 1 
ATOM   4061 N  N   . SER   B 1 214 ? 10.427  12.335  18.330  1.00 22.34  ? 1066 SER   B N   1 
ATOM   4062 C  CA  . SER   B 1 214 ? 10.187  12.031  16.903  1.00 21.74  ? 1066 SER   B CA  1 
ATOM   4063 C  C   . SER   B 1 214 ? 9.533   10.683  16.671  1.00 18.28  ? 1066 SER   B C   1 
ATOM   4064 O  O   . SER   B 1 214 ? 8.738   10.524  15.722  1.00 21.57  ? 1066 SER   B O   1 
ATOM   4065 C  CB  . SER   B 1 214 ? 11.499  12.078  16.123  1.00 19.89  ? 1066 SER   B CB  1 
ATOM   4066 O  OG  . SER   B 1 214 ? 12.034  13.381  16.172  1.00 25.16  ? 1066 SER   B OG  1 
ATOM   4067 N  N   . PHE   B 1 215 ? 9.897   9.702   17.495  1.00 21.76  ? 1067 PHE   B N   1 
ATOM   4068 C  CA  . PHE   B 1 215 ? 9.262   8.397   17.397  1.00 20.66  ? 1067 PHE   B CA  1 
ATOM   4069 C  C   . PHE   B 1 215 ? 7.751   8.457   17.657  1.00 20.11  ? 1067 PHE   B C   1 
ATOM   4070 O  O   . PHE   B 1 215 ? 6.975   7.807   16.975  1.00 20.84  ? 1067 PHE   B O   1 
ATOM   4071 C  CB  . PHE   B 1 215 ? 9.888   7.366   18.319  1.00 21.46  ? 1067 PHE   B CB  1 
ATOM   4072 C  CG  . PHE   B 1 215 ? 9.077   6.131   18.407  1.00 22.02  ? 1067 PHE   B CG  1 
ATOM   4073 C  CD1 . PHE   B 1 215 ? 9.024   5.252   17.328  1.00 18.31  ? 1067 PHE   B CD1 1 
ATOM   4074 C  CD2 . PHE   B 1 215 ? 8.241   5.905   19.498  1.00 23.71  ? 1067 PHE   B CD2 1 
ATOM   4075 C  CE1 . PHE   B 1 215 ? 8.223   4.116   17.394  1.00 17.12  ? 1067 PHE   B CE1 1 
ATOM   4076 C  CE2 . PHE   B 1 215 ? 7.425   4.781   19.542  1.00 21.50  ? 1067 PHE   B CE2 1 
ATOM   4077 C  CZ  . PHE   B 1 215 ? 7.410   3.915   18.514  1.00 15.74  ? 1067 PHE   B CZ  1 
ATOM   4078 N  N   . GLY   B 1 216 ? 7.332   9.181   18.690  1.00 23.75  ? 1068 GLY   B N   1 
ATOM   4079 C  CA  . GLY   B 1 216 ? 5.910   9.352   18.947  1.00 23.20  ? 1068 GLY   B CA  1 
ATOM   4080 C  C   . GLY   B 1 216 ? 5.151   9.914   17.754  1.00 22.58  ? 1068 GLY   B C   1 
ATOM   4081 O  O   . GLY   B 1 216 ? 4.039   9.492   17.474  1.00 21.33  ? 1068 GLY   B O   1 
ATOM   4082 N  N   . VAL   B 1 217 ? 5.770   10.844  17.025  1.00 19.84  ? 1069 VAL   B N   1 
ATOM   4083 C  CA  . VAL   B 1 217 ? 5.145   11.445  15.848  1.00 20.15  ? 1069 VAL   B CA  1 
ATOM   4084 C  C   . VAL   B 1 217 ? 5.043   10.386  14.757  1.00 20.53  ? 1069 VAL   B C   1 
ATOM   4085 O  O   . VAL   B 1 217 ? 4.005   10.268  14.101  1.00 21.54  ? 1069 VAL   B O   1 
ATOM   4086 C  CB  . VAL   B 1 217 ? 5.923   12.681  15.326  1.00 25.09  ? 1069 VAL   B CB  1 
ATOM   4087 C  CG1 . VAL   B 1 217 ? 5.227   13.255  14.105  1.00 26.59  ? 1069 VAL   B CG1 1 
ATOM   4088 C  CG2 . VAL   B 1 217 ? 6.018   13.757  16.430  1.00 28.92  ? 1069 VAL   B CG2 1 
ATOM   4089 N  N   . THR   B 1 218 ? 6.113   9.617   14.585  1.00 19.23  ? 1070 THR   B N   1 
ATOM   4090 C  CA  . THR   B 1 218 ? 6.135   8.502   13.662  1.00 17.06  ? 1070 THR   B CA  1 
ATOM   4091 C  C   . THR   B 1 218 ? 5.077   7.449   14.031  1.00 17.95  ? 1070 THR   B C   1 
ATOM   4092 O  O   . THR   B 1 218 ? 4.406   6.924   13.149  1.00 16.76  ? 1070 THR   B O   1 
ATOM   4093 C  CB  . THR   B 1 218 ? 7.533   7.811   13.637  1.00 18.88  ? 1070 THR   B CB  1 
ATOM   4094 O  OG1 . THR   B 1 218 ? 8.586   8.751   13.346  1.00 20.65  ? 1070 THR   B OG1 1 
ATOM   4095 C  CG2 . THR   B 1 218 ? 7.567   6.701   12.597  1.00 17.59  ? 1070 THR   B CG2 1 
ATOM   4096 N  N   . LEU   B 1 219 ? 4.943   7.132   15.316  1.00 18.84  ? 1071 LEU   B N   1 
ATOM   4097 C  CA  . LEU   B 1 219 ? 3.887   6.211   15.794  1.00 18.17  ? 1071 LEU   B CA  1 
ATOM   4098 C  C   . LEU   B 1 219 ? 2.498   6.724   15.400  1.00 20.92  ? 1071 LEU   B C   1 
ATOM   4099 O  O   . LEU   B 1 219 ? 1.645   5.974   14.946  1.00 19.37  ? 1071 LEU   B O   1 
ATOM   4100 C  CB  . LEU   B 1 219 ? 3.967   6.026   17.319  1.00 23.53  ? 1071 LEU   B CB  1 
ATOM   4101 C  CG  . LEU   B 1 219 ? 2.948   5.076   17.987  1.00 19.62  ? 1071 LEU   B CG  1 
ATOM   4102 C  CD1 . LEU   B 1 219 ? 3.093   3.655   17.478  1.00 22.48  ? 1071 LEU   B CD1 1 
ATOM   4103 C  CD2 . LEU   B 1 219 ? 3.140   5.099   19.475  1.00 22.07  ? 1071 LEU   B CD2 1 
ATOM   4104 N  N   . HIS   B 1 220 ? 2.278   8.026   15.588  1.00 19.40  ? 1072 HIS   B N   1 
ATOM   4105 C  CA  . HIS   B 1 220 ? 1.061   8.668   15.129  1.00 21.89  ? 1072 HIS   B CA  1 
ATOM   4106 C  C   . HIS   B 1 220 ? 0.833   8.466   13.619  1.00 20.69  ? 1072 HIS   B C   1 
ATOM   4107 O  O   . HIS   B 1 220 ? -0.275  8.139   13.205  1.00 21.21  ? 1072 HIS   B O   1 
ATOM   4108 C  CB  . HIS   B 1 220 ? 1.068   10.160  15.485  1.00 24.98  ? 1072 HIS   B CB  1 
ATOM   4109 C  CG  . HIS   B 1 220 ? -0.278  10.807  15.423  1.00 25.75  ? 1072 HIS   B CG  1 
ATOM   4110 N  ND1 . HIS   B 1 220 ? -0.853  11.209  14.237  1.00 29.99  ? 1072 HIS   B ND1 1 
ATOM   4111 C  CD2 . HIS   B 1 220 ? -1.149  11.157  16.404  1.00 27.71  ? 1072 HIS   B CD2 1 
ATOM   4112 C  CE1 . HIS   B 1 220 ? -2.024  11.766  14.488  1.00 34.64  ? 1072 HIS   B CE1 1 
ATOM   4113 N  NE2 . HIS   B 1 220 ? -2.226  11.744  15.794  1.00 27.07  ? 1072 HIS   B NE2 1 
ATOM   4114 N  N   . GLU   B 1 221 ? 1.883   8.652   12.817  1.00 19.72  ? 1073 GLU   B N   1 
ATOM   4115 C  CA  . GLU   B 1 221 ? 1.806   8.431   11.358  1.00 19.58  ? 1073 GLU   B CA  1 
ATOM   4116 C  C   . GLU   B 1 221 ? 1.422   6.992   11.057  1.00 20.77  ? 1073 GLU   B C   1 
ATOM   4117 O  O   . GLU   B 1 221 ? 0.537   6.727   10.261  1.00 21.33  ? 1073 GLU   B O   1 
ATOM   4118 C  CB  . GLU   B 1 221 ? 3.139   8.704   10.685  1.00 17.95  ? 1073 GLU   B CB  1 
ATOM   4119 C  CG  . GLU   B 1 221 ? 3.591   10.127  10.714  1.00 21.23  ? 1073 GLU   B CG  1 
ATOM   4120 C  CD  . GLU   B 1 221 ? 4.837   10.288  9.868   1.00 17.55  ? 1073 GLU   B CD  1 
ATOM   4121 O  OE1 . GLU   B 1 221 ? 5.947   10.119  10.407  1.00 20.71  ? 1073 GLU   B OE1 1 
ATOM   4122 O  OE2 . GLU   B 1 221 ? 4.673   10.520  8.657   1.00 23.10  ? 1073 GLU   B OE2 1 
ATOM   4123 N  N   . LEU   B 1 222 ? 2.096   6.074   11.724  1.00 21.16  ? 1074 LEU   B N   1 
ATOM   4124 C  CA  . LEU   B 1 222 ? 1.836   4.637   11.537  1.00 20.18  ? 1074 LEU   B CA  1 
ATOM   4125 C  C   . LEU   B 1 222 ? 0.364   4.338   11.793  1.00 21.65  ? 1074 LEU   B C   1 
ATOM   4126 O  O   . LEU   B 1 222 ? -0.328  3.744   10.940  1.00 19.70  ? 1074 LEU   B O   1 
ATOM   4127 C  CB  . LEU   B 1 222 ? 2.749   3.868   12.485  1.00 22.89  ? 1074 LEU   B CB  1 
ATOM   4128 C  CG  . LEU   B 1 222 ? 2.619   2.394   12.765  1.00 25.47  ? 1074 LEU   B CG  1 
ATOM   4129 C  CD1 . LEU   B 1 222 ? 2.652   1.632   11.458  1.00 28.81  ? 1074 LEU   B CD1 1 
ATOM   4130 C  CD2 . LEU   B 1 222 ? 3.767   2.004   13.640  1.00 27.95  ? 1074 LEU   B CD2 1 
ATOM   4131 N  N   . LEU   B 1 223 ? -0.119  4.807   12.941  1.00 21.99  ? 1075 LEU   B N   1 
ATOM   4132 C  CA  . LEU   B 1 223 ? -1.505  4.599   13.365  1.00 23.59  ? 1075 LEU   B CA  1 
ATOM   4133 C  C   . LEU   B 1 223 ? -2.560  5.261   12.445  1.00 25.85  ? 1075 LEU   B C   1 
ATOM   4134 O  O   . LEU   B 1 223 ? -3.717  4.800   12.402  1.00 27.69  ? 1075 LEU   B O   1 
ATOM   4135 C  CB  . LEU   B 1 223 ? -1.666  5.029   14.826  1.00 26.72  ? 1075 LEU   B CB  1 
ATOM   4136 C  CG  . LEU   B 1 223 ? -0.898  4.156   15.832  1.00 27.16  ? 1075 LEU   B CG  1 
ATOM   4137 C  CD1 . LEU   B 1 223 ? -0.675  4.886   17.132  1.00 29.56  ? 1075 LEU   B CD1 1 
ATOM   4138 C  CD2 . LEU   B 1 223 ? -1.634  2.837   16.086  1.00 30.69  ? 1075 LEU   B CD2 1 
ATOM   4139 N  N   . THR   B 1 224 ? -2.178  6.334   11.731  1.00 23.00  ? 1076 THR   B N   1 
ATOM   4140 C  CA  . THR   B 1 224 ? -3.031  6.982   10.718  1.00 25.39  ? 1076 THR   B CA  1 
ATOM   4141 C  C   . THR   B 1 224 ? -2.790  6.458   9.287   1.00 23.46  ? 1076 THR   B C   1 
ATOM   4142 O  O   . THR   B 1 224 ? -3.313  7.025   8.312   1.00 25.11  ? 1076 THR   B O   1 
ATOM   4143 C  CB  . THR   B 1 224 ? -2.906  8.538   10.718  1.00 25.43  ? 1076 THR   B CB  1 
ATOM   4144 O  OG1 . THR   B 1 224 ? -1.574  8.921   10.362  1.00 31.31  ? 1076 THR   B OG1 1 
ATOM   4145 C  CG2 . THR   B 1 224 ? -3.238  9.122   12.066  1.00 30.27  ? 1076 THR   B CG2 1 
ATOM   4146 N  N   . TYR   B 1 225 ? -2.037  5.361   9.164   1.00 23.19  ? 1077 TYR   B N   1 
ATOM   4147 C  CA  . TYR   B 1 225 ? -1.692  4.767   7.872   1.00 20.85  ? 1077 TYR   B CA  1 
ATOM   4148 C  C   . TYR   B 1 225 ? -1.051  5.784   6.896   1.00 23.97  ? 1077 TYR   B C   1 
ATOM   4149 O  O   . TYR   B 1 225 ? -1.233  5.703   5.681   1.00 18.44  ? 1077 TYR   B O   1 
ATOM   4150 C  CB  . TYR   B 1 225 ? -2.891  4.072   7.254   1.00 26.49  ? 1077 TYR   B CB  1 
ATOM   4151 C  CG  . TYR   B 1 225 ? -3.391  2.890   8.049   1.00 26.61  ? 1077 TYR   B CG  1 
ATOM   4152 C  CD1 . TYR   B 1 225 ? -2.773  1.652   7.935   1.00 18.41  ? 1077 TYR   B CD1 1 
ATOM   4153 C  CD2 . TYR   B 1 225 ? -4.483  3.003   8.891   1.00 27.61  ? 1077 TYR   B CD2 1 
ATOM   4154 C  CE1 . TYR   B 1 225 ? -3.230  0.549   8.634   1.00 18.68  ? 1077 TYR   B CE1 1 
ATOM   4155 C  CE2 . TYR   B 1 225 ? -4.944  1.902   9.629   1.00 27.19  ? 1077 TYR   B CE2 1 
ATOM   4156 C  CZ  . TYR   B 1 225 ? -4.319  0.679   9.485   1.00 26.06  ? 1077 TYR   B CZ  1 
ATOM   4157 O  OH  . TYR   B 1 225 ? -4.771  -0.423  10.168  1.00 25.92  ? 1077 TYR   B OH  1 
ATOM   4158 N  N   . CYS   B 1 226 ? -0.278  6.724   7.451   1.00 24.84  ? 1078 CYS   B N   1 
ATOM   4159 C  CA  . CYS   B 1 226 ? 0.396   7.760   6.680   1.00 24.56  ? 1078 CYS   B CA  1 
ATOM   4160 C  C   . CYS   B 1 226 ? -0.530  8.524   5.708   1.00 28.88  ? 1078 CYS   B C   1 
ATOM   4161 O  O   . CYS   B 1 226 ? -0.101  8.941   4.628   1.00 30.18  ? 1078 CYS   B O   1 
ATOM   4162 C  CB  . CYS   B 1 226 ? 1.587   7.135   5.941   1.00 26.20  ? 1078 CYS   B CB  1 
ATOM   4163 S  SG  . CYS   B 1 226 ? 2.965   6.730   7.010   1.00 25.98  ? 1078 CYS   B SG  1 
ATOM   4164 N  N   . ASP   B 1 227 ? -1.792  8.718   6.097   1.00 28.82  ? 1079 ASP   B N   1 
ATOM   4165 C  CA  . ASP   B 1 227 ? -2.732  9.500   5.282   1.00 33.98  ? 1079 ASP   B CA  1 
ATOM   4166 C  C   . ASP   B 1 227 ? -2.276  10.963  5.294   1.00 34.24  ? 1079 ASP   B C   1 
ATOM   4167 O  O   . ASP   B 1 227 ? -1.966  11.505  6.359   1.00 34.10  ? 1079 ASP   B O   1 
ATOM   4168 C  CB  . ASP   B 1 227 ? -4.168  9.392   5.816   1.00 35.37  ? 1079 ASP   B CB  1 
ATOM   4169 C  CG  . ASP   B 1 227 ? -5.122  10.389  5.156   1.00 39.79  ? 1079 ASP   B CG  1 
ATOM   4170 O  OD1 . ASP   B 1 227 ? -5.068  10.536  3.922   1.00 38.98  ? 1079 ASP   B OD1 1 
ATOM   4171 O  OD2 . ASP   B 1 227 ? -5.931  11.026  5.872   1.00 50.62  ? 1079 ASP   B OD2 1 
ATOM   4172 N  N   . SER   B 1 228 ? -2.243  11.583  4.115   1.00 37.18  ? 1080 SER   B N   1 
ATOM   4173 C  CA  . SER   B 1 228 ? -1.670  12.932  3.971   1.00 40.06  ? 1080 SER   B CA  1 
ATOM   4174 C  C   . SER   B 1 228 ? -2.508  13.996  4.691   1.00 43.13  ? 1080 SER   B C   1 
ATOM   4175 O  O   . SER   B 1 228 ? -1.961  14.950  5.238   1.00 42.56  ? 1080 SER   B O   1 
ATOM   4176 C  CB  . SER   B 1 228 ? -1.493  13.294  2.491   1.00 43.82  ? 1080 SER   B CB  1 
ATOM   4177 O  OG  . SER   B 1 228 ? -2.741  13.334  1.809   1.00 50.07  ? 1080 SER   B OG  1 
ATOM   4178 N  N   . ASP   B 1 229 ? -3.834  13.817  4.710   1.00 44.11  ? 1081 ASP   B N   1 
ATOM   4179 C  CA  . ASP   B 1 229 ? -4.724  14.719  5.448   1.00 47.05  ? 1081 ASP   B CA  1 
ATOM   4180 C  C   . ASP   B 1 229 ? -4.666  14.542  6.962   1.00 45.51  ? 1081 ASP   B C   1 
ATOM   4181 O  O   . ASP   B 1 229 ? -5.121  15.416  7.695   1.00 49.99  ? 1081 ASP   B O   1 
ATOM   4182 C  CB  . ASP   B 1 229 ? -6.164  14.605  4.935   1.00 49.03  ? 1081 ASP   B CB  1 
ATOM   4183 C  CG  . ASP   B 1 229 ? -6.315  15.162  3.539   1.00 55.83  ? 1081 ASP   B CG  1 
ATOM   4184 O  OD1 . ASP   B 1 229 ? -6.111  16.380  3.378   1.00 67.88  ? 1081 ASP   B OD1 1 
ATOM   4185 O  OD2 . ASP   B 1 229 ? -6.628  14.395  2.603   1.00 60.34  ? 1081 ASP   B OD2 1 
ATOM   4186 N  N   . SER   B 1 230 ? -4.105  13.421  7.414   1.00 44.37  ? 1082 SER   B N   1 
ATOM   4187 C  CA  . SER   B 1 230 ? -3.825  13.159  8.833   1.00 43.77  ? 1082 SER   B CA  1 
ATOM   4188 C  C   . SER   B 1 230 ? -2.347  13.399  9.211   1.00 41.52  ? 1082 SER   B C   1 
ATOM   4189 O  O   . SER   B 1 230 ? -1.950  13.129  10.346  1.00 41.31  ? 1082 SER   B O   1 
ATOM   4190 C  CB  . SER   B 1 230 ? -4.207  11.711  9.170   1.00 40.88  ? 1082 SER   B CB  1 
ATOM   4191 O  OG  . SER   B 1 230 ? -5.479  11.384  8.623   1.00 50.58  ? 1082 SER   B OG  1 
ATOM   4192 N  N   . SER   B 1 231 ? -1.549  13.915  8.275   1.00 41.57  ? 1083 SER   B N   1 
ATOM   4193 C  CA  . SER   B 1 231 ? -0.111  14.064  8.477   1.00 38.82  ? 1083 SER   B CA  1 
ATOM   4194 C  C   . SER   B 1 231 ? 0.201   15.018  9.638   1.00 39.41  ? 1083 SER   B C   1 
ATOM   4195 O  O   . SER   B 1 231 ? -0.528  16.008  9.837   1.00 41.12  ? 1083 SER   B O   1 
ATOM   4196 C  CB  . SER   B 1 231 ? 0.579   14.536  7.188   1.00 43.01  ? 1083 SER   B CB  1 
ATOM   4197 O  OG  . SER   B 1 231 ? 0.277   15.887  6.871   1.00 49.53  ? 1083 SER   B OG  1 
ATOM   4198 N  N   . PRO   B 1 232 ? 1.262   14.719  10.426  1.00 37.50  ? 1084 PRO   B N   1 
ATOM   4199 C  CA  . PRO   B 1 232 ? 1.722   15.641  11.476  1.00 36.83  ? 1084 PRO   B CA  1 
ATOM   4200 C  C   . PRO   B 1 232 ? 1.826   17.104  11.043  1.00 39.29  ? 1084 PRO   B C   1 
ATOM   4201 O  O   . PRO   B 1 232 ? 1.446   17.980  11.815  1.00 43.17  ? 1084 PRO   B O   1 
ATOM   4202 C  CB  . PRO   B 1 232 ? 3.089   15.076  11.848  1.00 33.11  ? 1084 PRO   B CB  1 
ATOM   4203 C  CG  . PRO   B 1 232 ? 2.927   13.624  11.650  1.00 30.98  ? 1084 PRO   B CG  1 
ATOM   4204 C  CD  . PRO   B 1 232 ? 2.077   13.487  10.420  1.00 32.14  ? 1084 PRO   B CD  1 
ATOM   4205 N  N   . MET   B 1 233 ? 2.283   17.360  9.816   1.00 41.80  ? 1085 MET   B N   1 
ATOM   4206 C  CA  . MET   B 1 233 ? 2.315   18.729  9.266   1.00 47.47  ? 1085 MET   B CA  1 
ATOM   4207 C  C   . MET   B 1 233 ? 0.903   19.289  9.097   1.00 48.90  ? 1085 MET   B C   1 
ATOM   4208 O  O   . MET   B 1 233 ? 0.628   20.398  9.555   1.00 54.46  ? 1085 MET   B O   1 
ATOM   4209 C  CB  . MET   B 1 233 ? 3.052   18.778  7.920   1.00 47.60  ? 1085 MET   B CB  1 
ATOM   4210 C  CG  . MET   B 1 233 ? 3.148   20.182  7.310   1.00 55.83  ? 1085 MET   B CG  1 
ATOM   4211 S  SD  . MET   B 1 233 ? 4.334   20.277  5.967   1.00 62.35  ? 1085 MET   B SD  1 
ATOM   4212 C  CE  . MET   B 1 233 ? 3.304   19.898  4.553   1.00 62.94  ? 1085 MET   B CE  1 
ATOM   4213 N  N   . ALA   B 1 234 ? 0.026   18.521  8.444   1.00 47.51  ? 1086 ALA   B N   1 
ATOM   4214 C  CA  . ALA   B 1 234 ? -1.379  18.910  8.227   1.00 48.17  ? 1086 ALA   B CA  1 
ATOM   4215 C  C   . ALA   B 1 234 ? -2.113  19.231  9.524   1.00 51.01  ? 1086 ALA   B C   1 
ATOM   4216 O  O   . ALA   B 1 234 ? -2.738  20.287  9.641   1.00 52.99  ? 1086 ALA   B O   1 
ATOM   4217 C  CB  . ALA   B 1 234 ? -2.133  17.837  7.459   1.00 46.22  ? 1086 ALA   B CB  1 
ATOM   4218 N  N   . LEU   B 1 235 ? -2.030  18.329  10.492  1.00 46.50  ? 1087 LEU   B N   1 
ATOM   4219 C  CA  . LEU   B 1 235 ? -2.663  18.534  11.799  1.00 49.84  ? 1087 LEU   B CA  1 
ATOM   4220 C  C   . LEU   B 1 235 ? -2.111  19.772  12.495  1.00 51.49  ? 1087 LEU   B C   1 
ATOM   4221 O  O   . LEU   B 1 235 ? -2.883  20.594  12.972  1.00 51.32  ? 1087 LEU   B O   1 
ATOM   4222 C  CB  . LEU   B 1 235 ? -2.556  17.282  12.692  1.00 48.92  ? 1087 LEU   B CB  1 
ATOM   4223 C  CG  . LEU   B 1 235 ? -3.657  16.214  12.509  1.00 55.25  ? 1087 LEU   B CG  1 
ATOM   4224 C  CD1 . LEU   B 1 235 ? -4.094  16.014  11.051  1.00 58.76  ? 1087 LEU   B CD1 1 
ATOM   4225 C  CD2 . LEU   B 1 235 ? -3.232  14.872  13.109  1.00 50.40  ? 1087 LEU   B CD2 1 
ATOM   4226 N  N   . PHE   B 1 236 ? -0.788  19.928  12.517  1.00 49.33  ? 1088 PHE   B N   1 
ATOM   4227 C  CA  . PHE   B 1 236 ? -0.192  21.135  13.103  1.00 51.45  ? 1088 PHE   B CA  1 
ATOM   4228 C  C   . PHE   B 1 236 ? -0.560  22.428  12.352  1.00 56.29  ? 1088 PHE   B C   1 
ATOM   4229 O  O   . PHE   B 1 236 ? -0.846  23.427  12.997  1.00 61.26  ? 1088 PHE   B O   1 
ATOM   4230 C  CB  . PHE   B 1 236 ? 1.335   20.999  13.287  1.00 48.09  ? 1088 PHE   B CB  1 
ATOM   4231 C  CG  . PHE   B 1 236 ? 1.740   20.229  14.539  1.00 44.79  ? 1088 PHE   B CG  1 
ATOM   4232 C  CD1 . PHE   B 1 236 ? 1.321   20.648  15.803  1.00 48.24  ? 1088 PHE   B CD1 1 
ATOM   4233 C  CD2 . PHE   B 1 236 ? 2.554   19.110  14.460  1.00 39.93  ? 1088 PHE   B CD2 1 
ATOM   4234 C  CE1 . PHE   B 1 236 ? 1.689   19.948  16.957  1.00 44.23  ? 1088 PHE   B CE1 1 
ATOM   4235 C  CE2 . PHE   B 1 236 ? 2.938   18.407  15.617  1.00 35.01  ? 1088 PHE   B CE2 1 
ATOM   4236 C  CZ  . PHE   B 1 236 ? 2.502   18.837  16.865  1.00 40.35  ? 1088 PHE   B CZ  1 
ATOM   4237 N  N   . LEU   B 1 237 ? -0.596  22.401  11.016  1.00 58.79  ? 1089 LEU   B N   1 
ATOM   4238 C  CA  . LEU   B 1 237 ? -0.907  23.611  10.223  1.00 64.68  ? 1089 LEU   B CA  1 
ATOM   4239 C  C   . LEU   B 1 237 ? -2.362  24.077  10.368  1.00 68.63  ? 1089 LEU   B C   1 
ATOM   4240 O  O   . LEU   B 1 237 ? -2.628  25.279  10.349  1.00 71.72  ? 1089 LEU   B O   1 
ATOM   4241 C  CB  . LEU   B 1 237 ? -0.565  23.423  8.736   1.00 66.18  ? 1089 LEU   B CB  1 
ATOM   4242 C  CG  . LEU   B 1 237 ? 0.912   23.340  8.331   1.00 65.20  ? 1089 LEU   B CG  1 
ATOM   4243 C  CD1 . LEU   B 1 237 ? 1.027   22.935  6.863   1.00 68.34  ? 1089 LEU   B CD1 1 
ATOM   4244 C  CD2 . LEU   B 1 237 ? 1.654   24.645  8.576   1.00 70.16  ? 1089 LEU   B CD2 1 
ATOM   4245 N  N   . LYS   B 1 238 ? -3.296  23.137  10.500  1.00 66.79  ? 1090 LYS   B N   1 
ATOM   4246 C  CA  . LYS   B 1 238 ? -4.683  23.487  10.851  1.00 70.66  ? 1090 LYS   B CA  1 
ATOM   4247 C  C   . LYS   B 1 238 ? -4.777  23.996  12.300  1.00 71.30  ? 1090 LYS   B C   1 
ATOM   4248 O  O   . LYS   B 1 238 ? -5.586  24.868  12.601  1.00 76.21  ? 1090 LYS   B O   1 
ATOM   4249 C  CB  . LYS   B 1 238 ? -5.616  22.283  10.653  1.00 68.74  ? 1090 LYS   B CB  1 
ATOM   4250 C  CG  . LYS   B 1 238 ? -5.765  21.891  9.162   0.00 68.60  ? 1090 LYS   B CG  1 
ATOM   4251 C  CD  . LYS   B 1 238 ? -6.633  20.657  8.988   0.00 66.91  ? 1090 LYS   B CD  1 
ATOM   4252 C  CE  . LYS   B 1 238 ? -6.712  20.237  7.528   0.00 66.72  ? 1090 LYS   B CE  1 
ATOM   4253 N  NZ  . LYS   B 1 238 ? -7.574  19.037  7.336   0.00 65.42  ? 1090 LYS   B NZ  1 
ATOM   4254 N  N   . MET   B 1 239 ? -3.930  23.455  13.177  1.00 67.26  ? 1091 MET   B N   1 
ATOM   4255 C  CA  . MET   B 1 239 ? -3.980  23.718  14.622  1.00 68.63  ? 1091 MET   B CA  1 
ATOM   4256 C  C   . MET   B 1 239 ? -3.453  25.105  15.023  1.00 72.21  ? 1091 MET   B C   1 
ATOM   4257 O  O   . MET   B 1 239 ? -4.174  25.889  15.648  1.00 75.59  ? 1091 MET   B O   1 
ATOM   4258 C  CB  . MET   B 1 239 ? -3.221  22.606  15.348  1.00 66.18  ? 1091 MET   B CB  1 
ATOM   4259 C  CG  . MET   B 1 239 ? -3.052  22.730  16.851  1.00 71.21  ? 1091 MET   B CG  1 
ATOM   4260 S  SD  . MET   B 1 239 ? -2.778  21.134  17.700  1.00 78.94  ? 1091 MET   B SD  1 
ATOM   4261 C  CE  . MET   B 1 239 ? -2.117  20.045  16.450  1.00 64.97  ? 1091 MET   B CE  1 
ATOM   4262 N  N   . ILE   B 1 240 ? -2.206  25.398  14.669  1.00 68.38  ? 1092 ILE   B N   1 
ATOM   4263 C  CA  . ILE   B 1 240 ? -1.566  26.677  15.039  1.00 73.70  ? 1092 ILE   B CA  1 
ATOM   4264 C  C   . ILE   B 1 240 ? -1.851  27.822  14.059  1.00 78.56  ? 1092 ILE   B C   1 
ATOM   4265 O  O   . ILE   B 1 240 ? -1.815  28.986  14.456  1.00 86.94  ? 1092 ILE   B O   1 
ATOM   4266 C  CB  . ILE   B 1 240 ? -0.026  26.525  15.247  1.00 68.74  ? 1092 ILE   B CB  1 
ATOM   4267 C  CG1 . ILE   B 1 240 ? 0.708   26.299  13.911  1.00 64.48  ? 1092 ILE   B CG1 1 
ATOM   4268 C  CG2 . ILE   B 1 240 ? 0.249   25.416  16.268  1.00 68.94  ? 1092 ILE   B CG2 1 
ATOM   4269 C  CD1 . ILE   B 1 240 ? 2.189   25.989  14.047  1.00 62.25  ? 1092 ILE   B CD1 1 
ATOM   4270 N  N   . GLY   B 1 241 ? -2.102  27.485  12.792  1.00 79.00  ? 1093 GLY   B N   1 
ATOM   4271 C  CA  . GLY   B 1 241 ? -2.299  28.465  11.718  1.00 84.40  ? 1093 GLY   B CA  1 
ATOM   4272 C  C   . GLY   B 1 241 ? -1.415  28.132  10.524  1.00 83.93  ? 1093 GLY   B C   1 
ATOM   4273 O  O   . GLY   B 1 241 ? -0.212  27.918  10.706  1.00 83.02  ? 1093 GLY   B O   1 
ATOM   4274 N  N   . PRO   B 1 242 ? -1.988  28.071  9.299   1.00 85.98  ? 1094 PRO   B N   1 
ATOM   4275 C  CA  . PRO   B 1 242 ? -1.186  27.724  8.111   1.00 84.24  ? 1094 PRO   B CA  1 
ATOM   4276 C  C   . PRO   B 1 242 ? -0.300  28.832  7.526   1.00 86.43  ? 1094 PRO   B C   1 
ATOM   4277 O  O   . PRO   B 1 242 ? 0.923   28.668  7.474   1.00 84.28  ? 1094 PRO   B O   1 
ATOM   4278 C  CB  . PRO   B 1 242 ? -2.243  27.285  7.088   1.00 85.66  ? 1094 PRO   B CB  1 
ATOM   4279 C  CG  . PRO   B 1 242 ? -3.483  27.968  7.488   1.00 91.63  ? 1094 PRO   B CG  1 
ATOM   4280 C  CD  . PRO   B 1 242 ? -3.411  28.261  8.960   1.00 91.39  ? 1094 PRO   B CD  1 
ATOM   4281 N  N   . THR   B 1 243 ? -0.908  29.945  7.114   1.00 91.07  ? 1095 THR   B N   1 
ATOM   4282 C  CA  . THR   B 1 243 ? -0.269  30.922  6.217   1.00 94.08  ? 1095 THR   B CA  1 
ATOM   4283 C  C   . THR   B 1 243 ? 0.545   32.002  6.954   1.00 96.80  ? 1095 THR   B C   1 
ATOM   4284 O  O   . THR   B 1 243 ? 0.303   33.209  6.788   1.00 99.92  ? 1095 THR   B O   1 
ATOM   4285 C  CB  . THR   B 1 243 ? -1.329  31.592  5.307   1.00 100.65 ? 1095 THR   B CB  1 
ATOM   4286 O  OG1 . THR   B 1 243 ? -2.300  32.252  6.045   0.00 103.69 ? 1095 THR   B OG1 1 
ATOM   4287 C  CG2 . THR   B 1 243 ? -1.981  30.523  4.387   0.00 97.79  ? 1095 THR   B CG2 1 
ATOM   4288 N  N   . HIS   B 1 244 ? 1.525   31.559  7.747   1.00 92.83  ? 1096 HIS   B N   1 
ATOM   4289 C  CA  . HIS   B 1 244 ? 2.353   32.458  8.577   1.00 93.82  ? 1096 HIS   B CA  1 
ATOM   4290 C  C   . HIS   B 1 244 ? 3.816   32.602  8.130   1.00 91.31  ? 1096 HIS   B C   1 
ATOM   4291 O  O   . HIS   B 1 244 ? 4.515   33.488  8.622   1.00 93.75  ? 1096 HIS   B O   1 
ATOM   4292 C  CB  . HIS   B 1 244 ? 2.287   32.002  10.036  1.00 91.35  ? 1096 HIS   B CB  1 
ATOM   4293 C  CG  . HIS   B 1 244 ? 0.916   32.098  10.625  1.00 94.45  ? 1096 HIS   B CG  1 
ATOM   4294 N  ND1 . HIS   B 1 244 ? 0.505   33.163  11.398  1.00 91.81  ? 1096 HIS   B ND1 1 
ATOM   4295 C  CD2 . HIS   B 1 244 ? -0.152  31.271  10.527  1.00 91.97  ? 1096 HIS   B CD2 1 
ATOM   4296 C  CE1 . HIS   B 1 244 ? -0.753  32.982  11.761  1.00 95.84  ? 1096 HIS   B CE1 1 
ATOM   4297 N  NE2 . HIS   B 1 244 ? -1.176  31.840  11.245  1.00 89.14  ? 1096 HIS   B NE2 1 
ATOM   4298 N  N   . GLY   B 1 245 ? 4.270   31.745  7.212   1.00 86.43  ? 1097 GLY   B N   1 
ATOM   4299 C  CA  . GLY   B 1 245 ? 5.622   31.829  6.641   1.00 84.63  ? 1097 GLY   B CA  1 
ATOM   4300 C  C   . GLY   B 1 245 ? 6.730   31.618  7.662   1.00 80.92  ? 1097 GLY   B C   1 
ATOM   4301 O  O   . GLY   B 1 245 ? 6.780   30.577  8.321   1.00 77.16  ? 1097 GLY   B O   1 
ATOM   4302 N  N   . GLN   B 1 246 ? 7.593   32.630  7.812   1.00 83.41  ? 1098 GLN   B N   1 
ATOM   4303 C  CA  . GLN   B 1 246 ? 8.730   32.595  8.752   1.00 80.54  ? 1098 GLN   B CA  1 
ATOM   4304 C  C   . GLN   B 1 246 ? 8.355   32.647  10.250  1.00 79.45  ? 1098 GLN   B C   1 
ATOM   4305 O  O   . GLN   B 1 246 ? 9.222   32.474  11.110  1.00 78.39  ? 1098 GLN   B O   1 
ATOM   4306 C  CB  . GLN   B 1 246 ? 9.714   33.728  8.435   1.00 85.43  ? 1098 GLN   B CB  1 
ATOM   4307 C  CG  . GLN   B 1 246 ? 10.460  33.555  7.111   0.00 79.12  ? 1098 GLN   B CG  1 
ATOM   4308 C  CD  . GLN   B 1 246 ? 11.454  34.677  6.842   0.00 83.13  ? 1098 GLN   B CD  1 
ATOM   4309 O  OE1 . GLN   B 1 246 ? 11.302  35.798  7.334   0.00 87.80  ? 1098 GLN   B OE1 1 
ATOM   4310 N  NE2 . GLN   B 1 246 ? 12.477  34.379  6.049   0.00 81.30  ? 1098 GLN   B NE2 1 
ATOM   4311 N  N   . MET   B 1 247 ? 7.079   32.886  10.554  1.00 78.48  ? 1099 MET   B N   1 
ATOM   4312 C  CA  . MET   B 1 247 ? 6.570   32.854  11.933  1.00 77.63  ? 1099 MET   B CA  1 
ATOM   4313 C  C   . MET   B 1 247 ? 6.078   31.470  12.417  1.00 71.92  ? 1099 MET   B C   1 
ATOM   4314 O  O   . MET   B 1 247 ? 5.700   31.316  13.584  1.00 71.48  ? 1099 MET   B O   1 
ATOM   4315 C  CB  . MET   B 1 247 ? 5.416   33.845  12.069  1.00 86.30  ? 1099 MET   B CB  1 
ATOM   4316 C  CG  . MET   B 1 247 ? 5.701   35.225  11.511  1.00 91.80  ? 1099 MET   B CG  1 
ATOM   4317 S  SD  . MET   B 1 247 ? 7.292   35.929  12.001  1.00 85.71  ? 1099 MET   B SD  1 
ATOM   4318 C  CE  . MET   B 1 247 ? 7.141   35.880  13.786  1.00 86.64  ? 1099 MET   B CE  1 
ATOM   4319 N  N   . THR   B 1 248 ? 6.080   30.474  11.545  1.00 65.91  ? 1100 THR   B N   1 
ATOM   4320 C  CA  . THR   B 1 248 ? 5.447   29.183  11.874  1.00 61.29  ? 1100 THR   B CA  1 
ATOM   4321 C  C   . THR   B 1 248 ? 6.036   28.467  13.111  1.00 58.06  ? 1100 THR   B C   1 
ATOM   4322 O  O   . THR   B 1 248 ? 5.278   27.887  13.889  1.00 57.25  ? 1100 THR   B O   1 
ATOM   4323 C  CB  . THR   B 1 248 ? 5.430   28.248  10.639  1.00 58.95  ? 1100 THR   B CB  1 
ATOM   4324 O  OG1 . THR   B 1 248 ? 4.762   28.916  9.560   1.00 64.87  ? 1100 THR   B OG1 1 
ATOM   4325 C  CG2 . THR   B 1 248 ? 4.699   26.936  10.934  1.00 58.35  ? 1100 THR   B CG2 1 
ATOM   4326 N  N   . VAL   B 1 249 ? 7.357   28.526  13.308  1.00 56.93  ? 1101 VAL   B N   1 
ATOM   4327 C  CA  . VAL   B 1 249 ? 8.022   27.733  14.363  1.00 54.13  ? 1101 VAL   B CA  1 
ATOM   4328 C  C   . VAL   B 1 249 ? 7.836   28.228  15.811  1.00 56.98  ? 1101 VAL   B C   1 
ATOM   4329 O  O   . VAL   B 1 249 ? 7.710   27.404  16.714  1.00 55.10  ? 1101 VAL   B O   1 
ATOM   4330 C  CB  . VAL   B 1 249 ? 9.534   27.509  14.058  1.00 51.89  ? 1101 VAL   B CB  1 
ATOM   4331 C  CG1 . VAL   B 1 249 ? 10.234  26.717  15.183  1.00 49.56  ? 1101 VAL   B CG1 1 
ATOM   4332 C  CG2 . VAL   B 1 249 ? 9.701   26.753  12.742  1.00 48.67  ? 1101 VAL   B CG2 1 
ATOM   4333 N  N   . THR   B 1 250 ? 7.857   29.542  16.055  1.00 61.73  ? 1102 THR   B N   1 
ATOM   4334 C  CA  . THR   B 1 250 ? 7.609   30.049  17.427  1.00 65.06  ? 1102 THR   B CA  1 
ATOM   4335 C  C   . THR   B 1 250 ? 6.173   29.737  17.840  1.00 65.81  ? 1102 THR   B C   1 
ATOM   4336 O  O   . THR   B 1 250 ? 5.932   29.349  18.991  1.00 65.96  ? 1102 THR   B O   1 
ATOM   4337 C  CB  . THR   B 1 250 ? 7.878   31.576  17.597  1.00 70.66  ? 1102 THR   B CB  1 
ATOM   4338 O  OG1 . THR   B 1 250 ? 9.162   31.908  17.052  1.00 70.16  ? 1102 THR   B OG1 1 
ATOM   4339 C  CG2 . THR   B 1 250 ? 7.826   31.983  19.071  1.00 73.97  ? 1102 THR   B CG2 1 
ATOM   4340 N  N   . ARG   B 1 251 ? 5.243   29.905  16.895  1.00 66.53  ? 1103 ARG   B N   1 
ATOM   4341 C  CA  . ARG   B 1 251 ? 3.828   29.487  17.058  1.00 66.84  ? 1103 ARG   B CA  1 
ATOM   4342 C  C   . ARG   B 1 251 ? 3.675   28.004  17.413  1.00 62.05  ? 1103 ARG   B C   1 
ATOM   4343 O  O   . ARG   B 1 251 ? 2.795   27.627  18.193  1.00 62.61  ? 1103 ARG   B O   1 
ATOM   4344 C  CB  . ARG   B 1 251 ? 3.023   29.788  15.783  1.00 68.42  ? 1103 ARG   B CB  1 
ATOM   4345 C  CG  . ARG   B 1 251 ? 2.858   31.274  15.491  1.00 77.12  ? 1103 ARG   B CG  1 
ATOM   4346 C  CD  . ARG   B 1 251 ? 2.090   31.529  14.199  1.00 81.35  ? 1103 ARG   B CD  1 
ATOM   4347 N  NE  . ARG   B 1 251 ? 0.649   31.327  14.356  1.00 83.04  ? 1103 ARG   B NE  1 
ATOM   4348 C  CZ  . ARG   B 1 251 ? -0.195  32.253  14.925  0.00 84.05  ? 1103 ARG   B CZ  1 
ATOM   4349 N  NH1 . ARG   B 1 251 ? 0.253   33.401  15.437  0.00 88.54  ? 1103 ARG   B NH1 1 
ATOM   4350 N  NH2 . ARG   B 1 251 ? -1.498  31.991  14.989  0.00 85.60  ? 1103 ARG   B NH2 1 
ATOM   4351 N  N   . LEU   B 1 252 ? 4.535   27.172  16.833  1.00 57.67  ? 1104 LEU   B N   1 
ATOM   4352 C  CA  . LEU   B 1 252 ? 4.585   25.745  17.161  1.00 53.24  ? 1104 LEU   B CA  1 
ATOM   4353 C  C   . LEU   B 1 252 ? 5.150   25.509  18.571  1.00 53.36  ? 1104 LEU   B C   1 
ATOM   4354 O  O   . LEU   B 1 252 ? 4.568   24.758  19.352  1.00 52.55  ? 1104 LEU   B O   1 
ATOM   4355 C  CB  . LEU   B 1 252 ? 5.412   25.002  16.106  1.00 49.13  ? 1104 LEU   B CB  1 
ATOM   4356 C  CG  . LEU   B 1 252 ? 5.623   23.498  16.209  1.00 49.73  ? 1104 LEU   B CG  1 
ATOM   4357 C  CD1 . LEU   B 1 252 ? 4.301   22.735  16.180  1.00 50.24  ? 1104 LEU   B CD1 1 
ATOM   4358 C  CD2 . LEU   B 1 252 ? 6.521   23.071  15.054  1.00 45.77  ? 1104 LEU   B CD2 1 
ATOM   4359 N  N   . VAL   B 1 253 ? 6.269   26.167  18.894  1.00 56.35  ? 1105 VAL   B N   1 
ATOM   4360 C  CA  . VAL   B 1 253 ? 6.870   26.092  20.242  1.00 57.79  ? 1105 VAL   B CA  1 
ATOM   4361 C  C   . VAL   B 1 253 ? 5.899   26.525  21.352  1.00 62.34  ? 1105 VAL   B C   1 
ATOM   4362 O  O   . VAL   B 1 253 ? 5.816   25.892  22.412  1.00 63.79  ? 1105 VAL   B O   1 
ATOM   4363 C  CB  . VAL   B 1 253 ? 8.173   26.931  20.321  1.00 61.21  ? 1105 VAL   B CB  1 
ATOM   4364 C  CG1 . VAL   B 1 253 ? 8.588   27.211  21.768  1.00 63.33  ? 1105 VAL   B CG1 1 
ATOM   4365 C  CG2 . VAL   B 1 253 ? 9.281   26.217  19.591  1.00 59.55  ? 1105 VAL   B CG2 1 
ATOM   4366 N  N   . ASN   B 1 254 ? 5.176   27.602  21.099  1.00 65.44  ? 1106 ASN   B N   1 
ATOM   4367 C  CA  . ASN   B 1 254 ? 4.219   28.129  22.080  1.00 72.60  ? 1106 ASN   B CA  1 
ATOM   4368 C  C   . ASN   B 1 254 ? 3.078   27.166  22.392  1.00 73.26  ? 1106 ASN   B C   1 
ATOM   4369 O  O   . ASN   B 1 254 ? 2.654   27.061  23.543  1.00 77.39  ? 1106 ASN   B O   1 
ATOM   4370 C  CB  . ASN   B 1 254 ? 3.656   29.476  21.615  1.00 78.37  ? 1106 ASN   B CB  1 
ATOM   4371 C  CG  . ASN   B 1 254 ? 4.509   30.652  22.049  1.00 82.05  ? 1106 ASN   B CG  1 
ATOM   4372 O  OD1 . ASN   B 1 254 ? 5.673   30.499  22.445  1.00 84.30  ? 1106 ASN   B OD1 1 
ATOM   4373 N  ND2 . ASN   B 1 254 ? 3.931   31.840  21.968  1.00 89.47  ? 1106 ASN   B ND2 1 
ATOM   4374 N  N   . THR   B 1 255 ? 2.601   26.467  21.368  1.00 72.28  ? 1107 THR   B N   1 
ATOM   4375 C  CA  . THR   B 1 255 ? 1.548   25.458  21.524  1.00 71.80  ? 1107 THR   B CA  1 
ATOM   4376 C  C   . THR   B 1 255 ? 2.066   24.263  22.342  1.00 67.93  ? 1107 THR   B C   1 
ATOM   4377 O  O   . THR   B 1 255 ? 1.396   23.807  23.265  1.00 69.35  ? 1107 THR   B O   1 
ATOM   4378 C  CB  . THR   B 1 255 ? 1.015   24.993  20.143  1.00 70.88  ? 1107 THR   B CB  1 
ATOM   4379 O  OG1 . THR   B 1 255 ? 0.985   26.102  19.238  1.00 75.29  ? 1107 THR   B OG1 1 
ATOM   4380 C  CG2 . THR   B 1 255 ? -0.382  24.439  20.252  1.00 75.15  ? 1107 THR   B CG2 1 
ATOM   4381 N  N   . LEU   B 1 256 ? 3.272   23.788  22.020  1.00 62.31  ? 1108 LEU   B N   1 
ATOM   4382 C  CA  . LEU   B 1 256 ? 3.925   22.725  22.799  1.00 60.29  ? 1108 LEU   B CA  1 
ATOM   4383 C  C   . LEU   B 1 256 ? 4.197   23.132  24.262  1.00 62.40  ? 1108 LEU   B C   1 
ATOM   4384 O  O   . LEU   B 1 256 ? 4.011   22.325  25.174  1.00 60.93  ? 1108 LEU   B O   1 
ATOM   4385 C  CB  . LEU   B 1 256 ? 5.213   22.249  22.109  1.00 54.45  ? 1108 LEU   B CB  1 
ATOM   4386 C  CG  . LEU   B 1 256 ? 5.044   21.609  20.727  1.00 55.38  ? 1108 LEU   B CG  1 
ATOM   4387 C  CD1 . LEU   B 1 256 ? 6.405   21.456  20.048  0.00 50.63  ? 1108 LEU   B CD1 1 
ATOM   4388 C  CD2 . LEU   B 1 256 ? 4.347   20.260  20.818  0.00 50.28  ? 1108 LEU   B CD2 1 
ATOM   4389 N  N   . LYS   B 1 257 ? 4.600   24.387  24.493  1.00 67.78  ? 1109 LYS   B N   1 
ATOM   4390 C  CA  . LYS   B 1 257 ? 4.808   24.881  25.861  1.00 71.70  ? 1109 LYS   B CA  1 
ATOM   4391 C  C   . LYS   B 1 257 ? 3.524   24.819  26.714  1.00 74.98  ? 1109 LYS   B C   1 
ATOM   4392 O  O   . LYS   B 1 257 ? 3.581   24.475  27.895  1.00 76.21  ? 1109 LYS   B O   1 
ATOM   4393 C  CB  . LYS   B 1 257 ? 5.382   26.305  25.847  1.00 74.87  ? 1109 LYS   B CB  1 
ATOM   4394 C  CG  . LYS   B 1 257 ? 6.847   26.438  25.657  0.00 73.54  ? 1109 LYS   B CG  1 
ATOM   4395 C  CD  . LYS   B 1 257 ? 7.289   27.886  25.800  0.00 78.03  ? 1109 LYS   B CD  1 
ATOM   4396 C  CE  . LYS   B 1 257 ? 8.762   28.059  25.489  0.00 76.80  ? 1109 LYS   B CE  1 
ATOM   4397 N  NZ  . LYS   B 1 257 ? 9.242   29.433  25.802  0.00 81.86  ? 1109 LYS   B NZ  1 
ATOM   4398 N  N   . GLU   B 1 258 ? 2.380   25.126  26.098  1.00 75.98  ? 1110 GLU   B N   1 
ATOM   4399 C  CA  . GLU   B 1 258 ? 1.062   25.063  26.761  1.00 79.44  ? 1110 GLU   B CA  1 
ATOM   4400 C  C   . GLU   B 1 258 ? 0.574   23.649  27.137  1.00 76.11  ? 1110 GLU   B C   1 
ATOM   4401 O  O   . GLU   B 1 258 ? -0.374  23.514  27.912  1.00 79.17  ? 1110 GLU   B O   1 
ATOM   4402 C  CB  . GLU   B 1 258 ? -0.001  25.731  25.878  1.00 82.66  ? 1110 GLU   B CB  1 
ATOM   4403 C  CG  . GLU   B 1 258 ? 0.171   27.254  25.736  1.00 91.28  ? 1110 GLU   B CG  1 
ATOM   4404 C  CD  . GLU   B 1 258 ? -0.647  27.867  24.601  1.00 95.20  ? 1110 GLU   B CD  1 
ATOM   4405 O  OE1 . GLU   B 1 258 ? -1.010  27.150  23.637  1.00 96.06  ? 1110 GLU   B OE1 1 
ATOM   4406 O  OE2 . GLU   B 1 258 ? -0.927  29.086  24.679  1.00 108.23 ? 1110 GLU   B OE2 1 
ATOM   4407 N  N   . GLY   B 1 259 ? 1.204   22.615  26.587  1.00 66.94  ? 1111 GLY   B N   1 
ATOM   4408 C  CA  . GLY   B 1 259 ? 0.830   21.215  26.853  1.00 65.90  ? 1111 GLY   B CA  1 
ATOM   4409 C  C   . GLY   B 1 259 ? 0.039   20.543  25.742  1.00 62.94  ? 1111 GLY   B C   1 
ATOM   4410 O  O   . GLY   B 1 259 ? -0.332  19.362  25.866  1.00 60.39  ? 1111 GLY   B O   1 
ATOM   4411 N  N   . LYS   B 1 260 ? -0.198  21.270  24.647  1.00 63.42  ? 1112 LYS   B N   1 
ATOM   4412 C  CA  . LYS   B 1 260 ? -0.956  20.747  23.500  1.00 59.55  ? 1112 LYS   B CA  1 
ATOM   4413 C  C   . LYS   B 1 260 ? -0.150  19.774  22.633  1.00 54.78  ? 1112 LYS   B C   1 
ATOM   4414 O  O   . LYS   B 1 260 ? 0.975   20.061  22.247  1.00 51.64  ? 1112 LYS   B O   1 
ATOM   4415 C  CB  . LYS   B 1 260 ? -1.456  21.891  22.627  1.00 61.46  ? 1112 LYS   B CB  1 
ATOM   4416 C  CG  . LYS   B 1 260 ? -2.576  22.694  23.265  1.00 67.78  ? 1112 LYS   B CG  1 
ATOM   4417 C  CD  . LYS   B 1 260 ? -2.921  23.900  22.423  1.00 67.71  ? 1112 LYS   B CD  1 
ATOM   4418 C  CE  . LYS   B 1 260 ? -4.197  24.569  22.947  0.00 73.24  ? 1112 LYS   B CE  1 
ATOM   4419 N  NZ  . LYS   B 1 260 ? -4.559  25.770  22.145  0.00 76.36  ? 1112 LYS   B NZ  1 
ATOM   4420 N  N   . ARG   B 1 261 ? -0.770  18.644  22.303  1.00 52.08  ? 1113 ARG   B N   1 
ATOM   4421 C  CA  . ARG   B 1 261 ? -0.142  17.582  21.522  1.00 47.64  ? 1113 ARG   B CA  1 
ATOM   4422 C  C   . ARG   B 1 261 ? -1.086  17.124  20.413  1.00 46.07  ? 1113 ARG   B C   1 
ATOM   4423 O  O   . ARG   B 1 261 ? -2.274  17.476  20.411  1.00 46.79  ? 1113 ARG   B O   1 
ATOM   4424 C  CB  . ARG   B 1 261 ? 0.194   16.399  22.428  1.00 48.66  ? 1113 ARG   B CB  1 
ATOM   4425 C  CG  . ARG   B 1 261 ? 1.114   16.713  23.604  1.00 48.19  ? 1113 ARG   B CG  1 
ATOM   4426 C  CD  . ARG   B 1 261 ? 2.534   17.063  23.168  1.00 49.72  ? 1113 ARG   B CD  1 
ATOM   4427 N  NE  . ARG   B 1 261 ? 3.410   17.315  24.323  1.00 47.96  ? 1113 ARG   B NE  1 
ATOM   4428 C  CZ  . ARG   B 1 261 ? 3.712   18.512  24.844  1.00 52.13  ? 1113 ARG   B CZ  1 
ATOM   4429 N  NH1 . ARG   B 1 261 ? 3.225   19.637  24.339  1.00 48.38  ? 1113 ARG   B NH1 1 
ATOM   4430 N  NH2 . ARG   B 1 261 ? 4.524   18.592  25.895  1.00 52.11  ? 1113 ARG   B NH2 1 
ATOM   4431 N  N   . LEU   B 1 262 ? -0.555  16.340  19.473  1.00 43.45  ? 1114 LEU   B N   1 
ATOM   4432 C  CA  . LEU   B 1 262 ? -1.358  15.761  18.383  1.00 41.52  ? 1114 LEU   B CA  1 
ATOM   4433 C  C   . LEU   B 1 262 ? -2.453  14.886  18.974  1.00 42.17  ? 1114 LEU   B C   1 
ATOM   4434 O  O   . LEU   B 1 262 ? -2.217  14.234  19.997  1.00 40.68  ? 1114 LEU   B O   1 
ATOM   4435 C  CB  . LEU   B 1 262 ? -0.497  14.894  17.454  1.00 39.79  ? 1114 LEU   B CB  1 
ATOM   4436 C  CG  . LEU   B 1 262 ? 0.533   15.662  16.621  1.00 42.66  ? 1114 LEU   B CG  1 
ATOM   4437 C  CD1 . LEU   B 1 262 ? 1.649   14.747  16.170  1.00 39.56  ? 1114 LEU   B CD1 1 
ATOM   4438 C  CD2 . LEU   B 1 262 ? -0.124  16.376  15.429  1.00 44.17  ? 1114 LEU   B CD2 1 
ATOM   4439 N  N   . PRO   B 1 263 ? -3.638  14.855  18.329  1.00 43.62  ? 1115 PRO   B N   1 
ATOM   4440 C  CA  . PRO   B 1 263 ? -4.783  14.139  18.883  1.00 44.09  ? 1115 PRO   B CA  1 
ATOM   4441 C  C   . PRO   B 1 263 ? -4.638  12.628  18.759  1.00 38.63  ? 1115 PRO   B C   1 
ATOM   4442 O  O   . PRO   B 1 263 ? -3.839  12.144  17.953  1.00 37.49  ? 1115 PRO   B O   1 
ATOM   4443 C  CB  . PRO   B 1 263 ? -5.941  14.624  18.011  1.00 46.14  ? 1115 PRO   B CB  1 
ATOM   4444 C  CG  . PRO   B 1 263 ? -5.319  14.881  16.705  1.00 45.08  ? 1115 PRO   B CG  1 
ATOM   4445 C  CD  . PRO   B 1 263 ? -3.973  15.459  17.026  1.00 45.34  ? 1115 PRO   B CD  1 
ATOM   4446 N  N   . CYS   B 1 264 ? -5.404  11.894  19.557  1.00 37.63  ? 1116 CYS   B N   1 
ATOM   4447 C  CA  . CYS   B 1 264 ? -5.429  10.430  19.449  1.00 37.65  ? 1116 CYS   B CA  1 
ATOM   4448 C  C   . CYS   B 1 264 ? -5.920  10.008  18.060  1.00 37.55  ? 1116 CYS   B C   1 
ATOM   4449 O  O   . CYS   B 1 264 ? -7.024  10.417  17.657  1.00 41.97  ? 1116 CYS   B O   1 
ATOM   4450 C  CB  . CYS   B 1 264 ? -6.348  9.825   20.508  1.00 36.85  ? 1116 CYS   B CB  1 
ATOM   4451 S  SG  . CYS   B 1 264 ? -6.288  8.028   20.541  1.00 40.59  ? 1116 CYS   B SG  1 
ATOM   4452 N  N   . PRO   B 1 265 ? -5.125  9.199   17.324  1.00 35.00  ? 1117 PRO   B N   1 
ATOM   4453 C  CA  . PRO   B 1 265 ? -5.602  8.748   16.016  1.00 35.53  ? 1117 PRO   B CA  1 
ATOM   4454 C  C   . PRO   B 1 265 ? -6.922  7.973   16.094  1.00 38.07  ? 1117 PRO   B C   1 
ATOM   4455 O  O   . PRO   B 1 265 ? -7.186  7.337   17.117  1.00 33.83  ? 1117 PRO   B O   1 
ATOM   4456 C  CB  . PRO   B 1 265 ? -4.477  7.829   15.511  1.00 29.63  ? 1117 PRO   B CB  1 
ATOM   4457 C  CG  . PRO   B 1 265 ? -3.289  8.201   16.264  1.00 33.78  ? 1117 PRO   B CG  1 
ATOM   4458 C  CD  . PRO   B 1 265 ? -3.783  8.674   17.615  1.00 36.43  ? 1117 PRO   B CD  1 
ATOM   4459 N  N   . PRO   B 1 266 ? -7.759  8.052   15.039  1.00 40.09  ? 1118 PRO   B N   1 
ATOM   4460 C  CA  . PRO   B 1 266 ? -8.941  7.228   14.981  1.00 41.73  ? 1118 PRO   B CA  1 
ATOM   4461 C  C   . PRO   B 1 266 ? -8.625  5.763   15.239  1.00 37.57  ? 1118 PRO   B C   1 
ATOM   4462 O  O   . PRO   B 1 266 ? -7.593  5.259   14.789  1.00 29.93  ? 1118 PRO   B O   1 
ATOM   4463 C  CB  . PRO   B 1 266 ? -9.451  7.446   13.552  1.00 45.98  ? 1118 PRO   B CB  1 
ATOM   4464 C  CG  . PRO   B 1 266 ? -9.002  8.814   13.214  1.00 45.18  ? 1118 PRO   B CG  1 
ATOM   4465 C  CD  . PRO   B 1 266 ? -7.653  8.921   13.852  1.00 44.02  ? 1118 PRO   B CD  1 
ATOM   4466 N  N   . ASN   B 1 267 ? -9.475  5.141   16.050  1.00 37.27  ? 1119 ASN   B N   1 
ATOM   4467 C  CA  . ASN   B 1 267 ? -9.405  3.714   16.376  1.00 37.77  ? 1119 ASN   B CA  1 
ATOM   4468 C  C   . ASN   B 1 267 ? -8.171  3.282   17.181  1.00 35.95  ? 1119 ASN   B C   1 
ATOM   4469 O  O   . ASN   B 1 267 ? -7.932  2.084   17.338  1.00 37.81  ? 1119 ASN   B O   1 
ATOM   4470 C  CB  . ASN   B 1 267 ? -9.560  2.864   15.099  1.00 35.91  ? 1119 ASN   B CB  1 
ATOM   4471 C  CG  . ASN   B 1 267 ? -10.810 3.222   14.300  1.00 41.87  ? 1119 ASN   B CG  1 
ATOM   4472 O  OD1 . ASN   B 1 267 ? -10.732 3.566   13.119  1.00 45.19  ? 1119 ASN   B OD1 1 
ATOM   4473 N  ND2 . ASN   B 1 267 ? -11.962 3.154   14.946  1.00 34.29  ? 1119 ASN   B ND2 1 
ATOM   4474 N  N   . CYS   B 1 268 ? -7.418  4.243   17.723  1.00 35.50  ? 1120 CYS   B N   1 
ATOM   4475 C  CA  . CYS   B 1 268 ? -6.230  3.937   18.520  1.00 32.95  ? 1120 CYS   B CA  1 
ATOM   4476 C  C   . CYS   B 1 268 ? -6.691  3.755   19.970  1.00 35.70  ? 1120 CYS   B C   1 
ATOM   4477 O  O   . CYS   B 1 268 ? -7.317  4.661   20.534  1.00 35.08  ? 1120 CYS   B O   1 
ATOM   4478 C  CB  . CYS   B 1 268 ? -5.192  5.053   18.397  1.00 34.51  ? 1120 CYS   B CB  1 
ATOM   4479 S  SG  . CYS   B 1 268 ? -3.737  4.844   19.434  1.00 29.72  ? 1120 CYS   B SG  1 
ATOM   4480 N  N   . PRO   B 1 269 ? -6.399  2.588   20.590  1.00 34.04  ? 1121 PRO   B N   1 
ATOM   4481 C  CA  . PRO   B 1 269 ? -6.817  2.448   21.987  1.00 36.76  ? 1121 PRO   B CA  1 
ATOM   4482 C  C   . PRO   B 1 269 ? -6.064  3.419   22.901  1.00 35.97  ? 1121 PRO   B C   1 
ATOM   4483 O  O   . PRO   B 1 269 ? -4.905  3.755   22.629  1.00 32.41  ? 1121 PRO   B O   1 
ATOM   4484 C  CB  . PRO   B 1 269 ? -6.465  0.993   22.334  1.00 36.38  ? 1121 PRO   B CB  1 
ATOM   4485 C  CG  . PRO   B 1 269 ? -6.159  0.328   21.057  1.00 38.07  ? 1121 PRO   B CG  1 
ATOM   4486 C  CD  . PRO   B 1 269 ? -5.694  1.389   20.113  1.00 31.33  ? 1121 PRO   B CD  1 
ATOM   4487 N  N   . ASP   B 1 270 ? -6.728  3.870   23.962  1.00 39.57  ? 1122 ASP   B N   1 
ATOM   4488 C  CA  . ASP   B 1 270 ? -6.137  4.853   24.875  1.00 42.60  ? 1122 ASP   B CA  1 
ATOM   4489 C  C   . ASP   B 1 270 ? -4.755  4.443   25.395  1.00 40.25  ? 1122 ASP   B C   1 
ATOM   4490 O  O   . ASP   B 1 270 ? -3.856  5.271   25.451  1.00 38.06  ? 1122 ASP   B O   1 
ATOM   4491 C  CB  . ASP   B 1 270 ? -7.075  5.129   26.059  1.00 45.83  ? 1122 ASP   B CB  1 
ATOM   4492 C  CG  . ASP   B 1 270 ? -6.441  6.040   27.102  1.00 53.91  ? 1122 ASP   B CG  1 
ATOM   4493 O  OD1 . ASP   B 1 270 ? -5.992  7.155   26.736  1.00 50.89  ? 1122 ASP   B OD1 1 
ATOM   4494 O  OD2 . ASP   B 1 270 ? -6.363  5.623   28.276  1.00 55.07  ? 1122 ASP   B OD2 1 
ATOM   4495 N  N   . GLU   B 1 271 ? -4.598  3.171   25.759  1.00 40.04  ? 1123 GLU   B N   1 
ATOM   4496 C  CA  . GLU   B 1 271 ? -3.326  2.679   26.319  1.00 42.33  ? 1123 GLU   B CA  1 
ATOM   4497 C  C   . GLU   B 1 271 ? -2.179  2.732   25.304  1.00 37.17  ? 1123 GLU   B C   1 
ATOM   4498 O  O   . GLU   B 1 271 ? -1.020  2.889   25.698  1.00 39.19  ? 1123 GLU   B O   1 
ATOM   4499 C  CB  . GLU   B 1 271 ? -3.429  1.291   26.988  1.00 45.54  ? 1123 GLU   B CB  1 
ATOM   4500 C  CG  . GLU   B 1 271 ? -4.315  0.247   26.307  1.00 48.57  ? 1123 GLU   B CG  1 
ATOM   4501 C  CD  . GLU   B 1 271 ? -5.783  0.380   26.691  1.00 56.16  ? 1123 GLU   B CD  1 
ATOM   4502 O  OE1 . GLU   B 1 271 ? -6.175  -0.108  27.781  1.00 63.42  ? 1123 GLU   B OE1 1 
ATOM   4503 O  OE2 . GLU   B 1 271 ? -6.539  0.991   25.899  1.00 48.78  ? 1123 GLU   B OE2 1 
ATOM   4504 N  N   . VAL   B 1 272 ? -2.498  2.646   24.011  1.00 34.31  ? 1124 VAL   B N   1 
ATOM   4505 C  CA  . VAL   B 1 272 ? -1.508  2.912   22.952  1.00 32.52  ? 1124 VAL   B CA  1 
ATOM   4506 C  C   . VAL   B 1 272 ? -1.157  4.413   22.955  1.00 32.10  ? 1124 VAL   B C   1 
ATOM   4507 O  O   . VAL   B 1 272 ? 0.013   4.778   23.035  1.00 31.42  ? 1124 VAL   B O   1 
ATOM   4508 C  CB  . VAL   B 1 272 ? -2.012  2.458   21.543  1.00 29.70  ? 1124 VAL   B CB  1 
ATOM   4509 C  CG1 . VAL   B 1 272 ? -1.025  2.847   20.442  1.00 30.04  ? 1124 VAL   B CG1 1 
ATOM   4510 C  CG2 . VAL   B 1 272 ? -2.249  0.955   21.517  1.00 32.01  ? 1124 VAL   B CG2 1 
ATOM   4511 N  N   . TYR   B 1 273 ? -2.185  5.261   22.891  1.00 30.31  ? 1125 TYR   B N   1 
ATOM   4512 C  CA  . TYR   B 1 273 ? -2.033  6.724   22.930  1.00 33.55  ? 1125 TYR   B CA  1 
ATOM   4513 C  C   . TYR   B 1 273 ? -1.272  7.223   24.158  1.00 36.50  ? 1125 TYR   B C   1 
ATOM   4514 O  O   . TYR   B 1 273 ? -0.499  8.176   24.045  1.00 35.25  ? 1125 TYR   B O   1 
ATOM   4515 C  CB  . TYR   B 1 273 ? -3.398  7.426   22.872  1.00 37.35  ? 1125 TYR   B CB  1 
ATOM   4516 C  CG  . TYR   B 1 273 ? -3.332  8.948   22.770  1.00 37.27  ? 1125 TYR   B CG  1 
ATOM   4517 C  CD1 . TYR   B 1 273 ? -2.583  9.572   21.767  1.00 38.78  ? 1125 TYR   B CD1 1 
ATOM   4518 C  CD2 . TYR   B 1 273 ? -4.035  9.758   23.655  1.00 44.05  ? 1125 TYR   B CD2 1 
ATOM   4519 C  CE1 . TYR   B 1 273 ? -2.528  10.967  21.658  1.00 38.12  ? 1125 TYR   B CE1 1 
ATOM   4520 C  CE2 . TYR   B 1 273 ? -3.985  11.155  23.554  1.00 48.87  ? 1125 TYR   B CE2 1 
ATOM   4521 C  CZ  . TYR   B 1 273 ? -3.231  11.748  22.552  1.00 44.25  ? 1125 TYR   B CZ  1 
ATOM   4522 O  OH  . TYR   B 1 273 ? -3.186  13.126  22.451  1.00 47.39  ? 1125 TYR   B OH  1 
ATOM   4523 N  N   . GLN   B 1 274 ? -1.478  6.592   25.312  1.00 35.19  ? 1126 GLN   B N   1 
ATOM   4524 C  CA  . GLN   B 1 274 ? -0.734  6.994   26.519  1.00 40.20  ? 1126 GLN   B CA  1 
ATOM   4525 C  C   . GLN   B 1 274 ? 0.768   6.742   26.395  1.00 40.25  ? 1126 GLN   B C   1 
ATOM   4526 O  O   . GLN   B 1 274 ? 1.566   7.582   26.829  1.00 41.78  ? 1126 GLN   B O   1 
ATOM   4527 C  CB  . GLN   B 1 274 ? -1.288  6.336   27.788  1.00 41.30  ? 1126 GLN   B CB  1 
ATOM   4528 C  CG  . GLN   B 1 274 ? -2.705  6.777   28.169  1.00 45.89  ? 1126 GLN   B CG  1 
ATOM   4529 C  CD  . GLN   B 1 274 ? -2.866  8.286   28.220  1.00 51.23  ? 1126 GLN   B CD  1 
ATOM   4530 O  OE1 . GLN   B 1 274 ? -2.017  8.995   28.761  1.00 53.54  ? 1126 GLN   B OE1 1 
ATOM   4531 N  NE2 . GLN   B 1 274 ? -3.954  8.784   27.645  1.00 50.84  ? 1126 GLN   B NE2 1 
ATOM   4532 N  N   . LEU   B 1 275 ? 1.152   5.614   25.786  1.00 37.86  ? 1127 LEU   B N   1 
ATOM   4533 C  CA  . LEU   B 1 275 ? 2.564   5.349   25.495  1.00 37.29  ? 1127 LEU   B CA  1 
ATOM   4534 C  C   . LEU   B 1 275 ? 3.132   6.420   24.550  1.00 35.06  ? 1127 LEU   B C   1 
ATOM   4535 O  O   . LEU   B 1 275 ? 4.258   6.875   24.732  1.00 34.67  ? 1127 LEU   B O   1 
ATOM   4536 C  CB  . LEU   B 1 275 ? 2.766   3.947   24.910  1.00 34.46  ? 1127 LEU   B CB  1 
ATOM   4537 C  CG  . LEU   B 1 275 ? 2.620   2.782   25.888  1.00 37.26  ? 1127 LEU   B CG  1 
ATOM   4538 C  CD1 . LEU   B 1 275 ? 2.407   1.472   25.142  1.00 35.20  ? 1127 LEU   B CD1 1 
ATOM   4539 C  CD2 . LEU   B 1 275 ? 3.842   2.685   26.802  1.00 40.17  ? 1127 LEU   B CD2 1 
ATOM   4540 N  N   . MET   B 1 276 ? 2.330   6.825   23.565  1.00 35.10  ? 1128 MET   B N   1 
ATOM   4541 C  CA  . MET   B 1 276 ? 2.659   7.920   22.645  1.00 33.49  ? 1128 MET   B CA  1 
ATOM   4542 C  C   . MET   B 1 276 ? 2.859   9.265   23.368  1.00 35.18  ? 1128 MET   B C   1 
ATOM   4543 O  O   . MET   B 1 276 ? 3.780   10.016  23.046  1.00 36.05  ? 1128 MET   B O   1 
ATOM   4544 C  CB  . MET   B 1 276 ? 1.560   8.041   21.567  1.00 32.71  ? 1128 MET   B CB  1 
ATOM   4545 C  CG  . MET   B 1 276 ? 1.820   9.057   20.461  1.00 34.55  ? 1128 MET   B CG  1 
ATOM   4546 S  SD  . MET   B 1 276 ? 0.403   9.369   19.405  1.00 38.93  ? 1128 MET   B SD  1 
ATOM   4547 C  CE  . MET   B 1 276 ? 0.184   7.802   18.623  1.00 31.88  ? 1128 MET   B CE  1 
ATOM   4548 N  N   . ARG   B 1 277 ? 1.999   9.563   24.336  1.00 36.84  ? 1129 ARG   B N   1 
ATOM   4549 C  CA  . ARG   B 1 277 ? 2.129   10.784  25.149  1.00 39.92  ? 1129 ARG   B CA  1 
ATOM   4550 C  C   . ARG   B 1 277 ? 3.410   10.791  26.006  1.00 38.67  ? 1129 ARG   B C   1 
ATOM   4551 O  O   . ARG   B 1 277 ? 3.999   11.843  26.221  1.00 41.39  ? 1129 ARG   B O   1 
ATOM   4552 C  CB  . ARG   B 1 277 ? 0.882   10.973  26.029  1.00 43.70  ? 1129 ARG   B CB  1 
ATOM   4553 C  CG  . ARG   B 1 277 ? -0.380  11.381  25.267  1.00 44.24  ? 1129 ARG   B CG  1 
ATOM   4554 C  CD  . ARG   B 1 277 ? -1.526  11.744  26.233  1.00 56.79  ? 1129 ARG   B CD  1 
ATOM   4555 N  NE  . ARG   B 1 277 ? -1.290  13.026  26.911  1.00 67.50  ? 1129 ARG   B NE  1 
ATOM   4556 C  CZ  . ARG   B 1 277 ? -1.487  14.240  26.383  1.00 70.89  ? 1129 ARG   B CZ  1 
ATOM   4557 N  NH1 . ARG   B 1 277 ? -1.945  14.398  25.140  1.00 68.11  ? 1129 ARG   B NH1 1 
ATOM   4558 N  NH2 . ARG   B 1 277 ? -1.221  15.323  27.114  1.00 76.11  ? 1129 ARG   B NH2 1 
ATOM   4559 N  N   . LYS   B 1 278 ? 3.863   9.617   26.452  1.00 36.01  ? 1130 LYS   B N   1 
ATOM   4560 C  CA  . LYS   B 1 278 ? 5.101   9.513   27.223  1.00 38.19  ? 1130 LYS   B CA  1 
ATOM   4561 C  C   . LYS   B 1 278 ? 6.354   9.818   26.407  1.00 36.08  ? 1130 LYS   B C   1 
ATOM   4562 O  O   . LYS   B 1 278 ? 7.408   10.104  26.983  1.00 41.04  ? 1130 LYS   B O   1 
ATOM   4563 C  CB  . LYS   B 1 278 ? 5.225   8.154   27.907  1.00 39.01  ? 1130 LYS   B CB  1 
ATOM   4564 C  CG  . LYS   B 1 278 ? 4.266   7.985   29.075  1.00 41.90  ? 1130 LYS   B CG  1 
ATOM   4565 C  CD  . LYS   B 1 278 ? 4.457   6.639   29.754  1.00 48.37  ? 1130 LYS   B CD  1 
ATOM   4566 C  CE  . LYS   B 1 278 ? 3.458   6.430   30.891  1.00 49.24  ? 1130 LYS   B CE  1 
ATOM   4567 N  NZ  . LYS   B 1 278 ? 3.644   7.403   31.998  0.00 53.75  ? 1130 LYS   B NZ  1 
ATOM   4568 N  N   . CYS   B 1 279 ? 6.238   9.749   25.076  1.00 36.93  ? 1131 CYS   B N   1 
ATOM   4569 C  CA  . CYS   B 1 279 ? 7.260   10.257  24.144  1.00 34.14  ? 1131 CYS   B CA  1 
ATOM   4570 C  C   . CYS   B 1 279 ? 7.348   11.783  24.087  1.00 36.71  ? 1131 CYS   B C   1 
ATOM   4571 O  O   . CYS   B 1 279 ? 8.391   12.334  23.721  1.00 32.99  ? 1131 CYS   B O   1 
ATOM   4572 C  CB  . CYS   B 1 279 ? 6.981   9.748   22.725  1.00 32.80  ? 1131 CYS   B CB  1 
ATOM   4573 S  SG  . CYS   B 1 279 ? 7.012   7.980   22.591  1.00 29.93  ? 1131 CYS   B SG  1 
ATOM   4574 N  N   . TRP   B 1 280 ? 6.256   12.455  24.452  1.00 40.57  ? 1132 TRP   B N   1 
ATOM   4575 C  CA  . TRP   B 1 280 ? 6.130   13.892  24.304  1.00 39.99  ? 1132 TRP   B CA  1 
ATOM   4576 C  C   . TRP   B 1 280 ? 6.086   14.683  25.621  1.00 43.33  ? 1132 TRP   B C   1 
ATOM   4577 O  O   . TRP   B 1 280 ? 5.507   15.741  25.642  1.00 40.96  ? 1132 TRP   B O   1 
ATOM   4578 C  CB  . TRP   B 1 280 ? 4.875   14.221  23.481  1.00 41.78  ? 1132 TRP   B CB  1 
ATOM   4579 C  CG  . TRP   B 1 280 ? 4.831   13.649  22.111  1.00 38.59  ? 1132 TRP   B CG  1 
ATOM   4580 C  CD1 . TRP   B 1 280 ? 5.895   13.395  21.286  1.00 37.15  ? 1132 TRP   B CD1 1 
ATOM   4581 C  CD2 . TRP   B 1 280 ? 3.655   13.299  21.367  1.00 39.28  ? 1132 TRP   B CD2 1 
ATOM   4582 N  NE1 . TRP   B 1 280 ? 5.452   12.883  20.089  1.00 33.65  ? 1132 TRP   B NE1 1 
ATOM   4583 C  CE2 . TRP   B 1 280 ? 4.087   12.807  20.109  1.00 38.53  ? 1132 TRP   B CE2 1 
ATOM   4584 C  CE3 . TRP   B 1 280 ? 2.282   13.320  21.649  1.00 38.19  ? 1132 TRP   B CE3 1 
ATOM   4585 C  CZ2 . TRP   B 1 280 ? 3.192   12.363  19.125  1.00 31.44  ? 1132 TRP   B CZ2 1 
ATOM   4586 C  CZ3 . TRP   B 1 280 ? 1.388   12.878  20.662  1.00 40.54  ? 1132 TRP   B CZ3 1 
ATOM   4587 C  CH2 . TRP   B 1 280 ? 1.851   12.403  19.418  1.00 36.64  ? 1132 TRP   B CH2 1 
ATOM   4588 N  N   . GLU   B 1 281 ? 6.728   14.200  26.689  1.00 43.46  ? 1133 GLU   B N   1 
ATOM   4589 C  CA  . GLU   B 1 281 ? 6.916   15.011  27.914  1.00 46.43  ? 1133 GLU   B CA  1 
ATOM   4590 C  C   . GLU   B 1 281 ? 7.774   16.208  27.493  1.00 48.04  ? 1133 GLU   B C   1 
ATOM   4591 O  O   . GLU   B 1 281 ? 8.652   16.048  26.647  1.00 43.73  ? 1133 GLU   B O   1 
ATOM   4592 C  CB  . GLU   B 1 281 ? 7.643   14.226  29.023  1.00 48.21  ? 1133 GLU   B CB  1 
ATOM   4593 C  CG  . GLU   B 1 281 ? 7.053   12.839  29.404  1.00 54.39  ? 1133 GLU   B CG  1 
ATOM   4594 C  CD  . GLU   B 1 281 ? 5.678   12.899  30.083  1.00 57.78  ? 1133 GLU   B CD  1 
ATOM   4595 O  OE1 . GLU   B 1 281 ? 5.333   13.945  30.673  1.00 57.14  ? 1133 GLU   B OE1 1 
ATOM   4596 O  OE2 . GLU   B 1 281 ? 4.941   11.881  30.041  1.00 53.64  ? 1133 GLU   B OE2 1 
ATOM   4597 N  N   . PHE   B 1 282 ? 7.543   17.397  28.041  1.00 51.36  ? 1134 PHE   B N   1 
ATOM   4598 C  CA  . PHE   B 1 282 ? 8.309   18.586  27.598  1.00 55.14  ? 1134 PHE   B CA  1 
ATOM   4599 C  C   . PHE   B 1 282 ? 9.824   18.433  27.824  1.00 57.49  ? 1134 PHE   B C   1 
ATOM   4600 O  O   . PHE   B 1 282 ? 10.617  18.699  26.923  1.00 55.35  ? 1134 PHE   B O   1 
ATOM   4601 C  CB  . PHE   B 1 282 ? 7.807   19.879  28.266  1.00 60.84  ? 1134 PHE   B CB  1 
ATOM   4602 C  CG  . PHE   B 1 282 ? 8.109   21.133  27.471  1.00 60.68  ? 1134 PHE   B CG  1 
ATOM   4603 C  CD1 . PHE   B 1 282 ? 7.313   21.488  26.383  1.00 60.33  ? 1134 PHE   B CD1 1 
ATOM   4604 C  CD2 . PHE   B 1 282 ? 9.184   21.955  27.804  1.00 65.35  ? 1134 PHE   B CD2 1 
ATOM   4605 C  CE1 . PHE   B 1 282 ? 7.579   22.639  25.638  1.00 58.49  ? 1134 PHE   B CE1 1 
ATOM   4606 C  CE2 . PHE   B 1 282 ? 9.459   23.111  27.061  1.00 65.42  ? 1134 PHE   B CE2 1 
ATOM   4607 C  CZ  . PHE   B 1 282 ? 8.654   23.448  25.972  1.00 59.08  ? 1134 PHE   B CZ  1 
ATOM   4608 N  N   . GLN   B 1 283 ? 10.212  18.009  29.023  1.00 61.68  ? 1135 GLN   B N   1 
ATOM   4609 C  CA  . GLN   B 1 283 ? 11.628  17.846  29.372  1.00 62.08  ? 1135 GLN   B CA  1 
ATOM   4610 C  C   . GLN   B 1 283 ? 12.119  16.459  28.935  1.00 56.39  ? 1135 GLN   B C   1 
ATOM   4611 O  O   . GLN   B 1 283 ? 11.494  15.466  29.294  1.00 55.23  ? 1135 GLN   B O   1 
ATOM   4612 C  CB  . GLN   B 1 283 ? 11.848  18.029  30.877  1.00 68.06  ? 1135 GLN   B CB  1 
ATOM   4613 C  CG  . GLN   B 1 283 ? 11.447  19.402  31.441  0.00 71.50  ? 1135 GLN   B CG  1 
ATOM   4614 C  CD  . GLN   B 1 283 ? 12.304  20.553  30.927  0.00 72.33  ? 1135 GLN   B CD  1 
ATOM   4615 O  OE1 . GLN   B 1 283 ? 13.504  20.401  30.694  0.00 70.81  ? 1135 GLN   B OE1 1 
ATOM   4616 N  NE2 . GLN   B 1 283 ? 11.685  21.715  30.756  0.00 74.52  ? 1135 GLN   B NE2 1 
ATOM   4617 N  N   . PRO   B 1 284 ? 13.219  16.382  28.156  1.00 51.88  ? 1136 PRO   B N   1 
ATOM   4618 C  CA  . PRO   B 1 284 ? 13.753  15.099  27.674  1.00 49.11  ? 1136 PRO   B CA  1 
ATOM   4619 C  C   . PRO   B 1 284 ? 14.122  14.055  28.741  1.00 50.84  ? 1136 PRO   B C   1 
ATOM   4620 O  O   . PRO   B 1 284 ? 13.971  12.847  28.494  1.00 50.27  ? 1136 PRO   B O   1 
ATOM   4621 C  CB  . PRO   B 1 284 ? 15.005  15.518  26.886  1.00 46.86  ? 1136 PRO   B CB  1 
ATOM   4622 C  CG  . PRO   B 1 284 ? 15.297  16.872  27.291  1.00 50.88  ? 1136 PRO   B CG  1 
ATOM   4623 C  CD  . PRO   B 1 284 ? 14.015  17.502  27.628  1.00 54.20  ? 1136 PRO   B CD  1 
ATOM   4624 N  N   . SER   B 1 285 ? 14.605  14.516  29.894  1.00 56.74  ? 1137 SER   B N   1 
ATOM   4625 C  CA  . SER   B 1 285 ? 14.946  13.635  31.026  1.00 59.45  ? 1137 SER   B CA  1 
ATOM   4626 C  C   . SER   B 1 285 ? 13.748  12.880  31.641  1.00 59.78  ? 1137 SER   B C   1 
ATOM   4627 O  O   . SER   B 1 285 ? 13.943  11.856  32.303  1.00 60.00  ? 1137 SER   B O   1 
ATOM   4628 C  CB  . SER   B 1 285 ? 15.666  14.425  32.121  1.00 64.98  ? 1137 SER   B CB  1 
ATOM   4629 O  OG  . SER   B 1 285 ? 14.842  15.463  32.619  1.00 65.53  ? 1137 SER   B OG  1 
ATOM   4630 N  N   . ASN   B 1 286 ? 12.536  13.406  31.443  1.00 58.19  ? 1138 ASN   B N   1 
ATOM   4631 C  CA  . ASN   B 1 286 ? 11.294  12.749  31.864  1.00 58.98  ? 1138 ASN   B CA  1 
ATOM   4632 C  C   . ASN   B 1 286 ? 10.758  11.680  30.899  1.00 54.28  ? 1138 ASN   B C   1 
ATOM   4633 O  O   . ASN   B 1 286 ? 10.031  10.777  31.324  1.00 54.44  ? 1138 ASN   B O   1 
ATOM   4634 C  CB  . ASN   B 1 286 ? 10.185  13.792  32.068  1.00 60.75  ? 1138 ASN   B CB  1 
ATOM   4635 C  CG  . ASN   B 1 286 ? 10.467  14.761  33.216  1.00 66.25  ? 1138 ASN   B CG  1 
ATOM   4636 O  OD1 . ASN   B 1 286 ? 11.286  14.501  34.104  1.00 61.50  ? 1138 ASN   B OD1 1 
ATOM   4637 N  ND2 . ASN   B 1 286 ? 9.762   15.887  33.202  1.00 63.92  ? 1138 ASN   B ND2 1 
ATOM   4638 N  N   . ARG   B 1 287 ? 11.079  11.804  29.609  1.00 50.87  ? 1139 ARG   B N   1 
ATOM   4639 C  CA  . ARG   B 1 287 ? 10.478  10.958  28.562  1.00 44.73  ? 1139 ARG   B CA  1 
ATOM   4640 C  C   . ARG   B 1 287 ? 10.751  9.467   28.735  1.00 44.94  ? 1139 ARG   B C   1 
ATOM   4641 O  O   . ARG   B 1 287 ? 11.766  9.082   29.316  1.00 43.76  ? 1139 ARG   B O   1 
ATOM   4642 C  CB  . ARG   B 1 287 ? 10.978  11.386  27.170  1.00 43.99  ? 1139 ARG   B CB  1 
ATOM   4643 C  CG  . ARG   B 1 287 ? 10.325  12.648  26.651  1.00 46.77  ? 1139 ARG   B CG  1 
ATOM   4644 C  CD  . ARG   B 1 287 ? 11.070  13.238  25.468  1.00 41.94  ? 1139 ARG   B CD  1 
ATOM   4645 N  NE  . ARG   B 1 287 ? 10.782  14.664  25.336  1.00 42.20  ? 1139 ARG   B NE  1 
ATOM   4646 C  CZ  . ARG   B 1 287 ? 11.488  15.552  24.633  1.00 42.41  ? 1139 ARG   B CZ  1 
ATOM   4647 N  NH1 . ARG   B 1 287 ? 12.541  15.178  23.931  1.00 35.37  ? 1139 ARG   B NH1 1 
ATOM   4648 N  NH2 . ARG   B 1 287 ? 11.121  16.828  24.622  1.00 43.77  ? 1139 ARG   B NH2 1 
ATOM   4649 N  N   . THR   B 1 288 ? 9.864   8.636   28.174  1.00 44.52  ? 1140 THR   B N   1 
ATOM   4650 C  CA  . THR   B 1 288 ? 10.068  7.181   28.153  1.00 43.24  ? 1140 THR   B CA  1 
ATOM   4651 C  C   . THR   B 1 288 ? 11.365  6.809   27.426  1.00 39.70  ? 1140 THR   B C   1 
ATOM   4652 O  O   . THR   B 1 288 ? 11.835  7.556   26.586  1.00 35.44  ? 1140 THR   B O   1 
ATOM   4653 C  CB  . THR   B 1 288 ? 8.859   6.421   27.511  1.00 41.04  ? 1140 THR   B CB  1 
ATOM   4654 O  OG1 . THR   B 1 288 ? 9.040   5.008   27.664  1.00 41.50  ? 1140 THR   B OG1 1 
ATOM   4655 C  CG2 . THR   B 1 288 ? 8.697   6.742   26.035  1.00 38.23  ? 1140 THR   B CG2 1 
ATOM   4656 N  N   . SER   B 1 289 ? 11.957  5.674   27.796  1.00 39.91  ? 1141 SER   B N   1 
ATOM   4657 C  CA  . SER   B 1 289 ? 13.038  5.088   27.016  1.00 37.07  ? 1141 SER   B CA  1 
ATOM   4658 C  C   . SER   B 1 289 ? 12.418  4.295   25.858  1.00 31.68  ? 1141 SER   B C   1 
ATOM   4659 O  O   . SER   B 1 289 ? 11.214  3.966   25.882  1.00 26.90  ? 1141 SER   B O   1 
ATOM   4660 C  CB  . SER   B 1 289 ? 13.910  4.182   27.897  1.00 37.62  ? 1141 SER   B CB  1 
ATOM   4661 O  OG  . SER   B 1 289 ? 13.213  3.018   28.313  1.00 38.85  ? 1141 SER   B OG  1 
ATOM   4662 N  N   . PHE   B 1 290 ? 13.231  4.011   24.844  1.00 28.51  ? 1142 PHE   B N   1 
ATOM   4663 C  CA  . PHE   B 1 290 ? 12.855  3.047   23.810  1.00 27.56  ? 1142 PHE   B CA  1 
ATOM   4664 C  C   . PHE   B 1 290 ? 12.626  1.662   24.457  1.00 27.46  ? 1142 PHE   B C   1 
ATOM   4665 O  O   . PHE   B 1 290 ? 11.675  0.991   24.103  1.00 21.45  ? 1142 PHE   B O   1 
ATOM   4666 C  CB  . PHE   B 1 290 ? 13.865  3.009   22.635  1.00 25.84  ? 1142 PHE   B CB  1 
ATOM   4667 C  CG  . PHE   B 1 290 ? 13.732  4.182   21.647  1.00 22.96  ? 1142 PHE   B CG  1 
ATOM   4668 C  CD1 . PHE   B 1 290 ? 12.531  4.403   20.942  1.00 21.02  ? 1142 PHE   B CD1 1 
ATOM   4669 C  CD2 . PHE   B 1 290 ? 14.814  5.045   21.402  1.00 26.99  ? 1142 PHE   B CD2 1 
ATOM   4670 C  CE1 . PHE   B 1 290 ? 12.394  5.473   20.038  1.00 23.58  ? 1142 PHE   B CE1 1 
ATOM   4671 C  CE2 . PHE   B 1 290 ? 14.696  6.120   20.508  1.00 22.33  ? 1142 PHE   B CE2 1 
ATOM   4672 C  CZ  . PHE   B 1 290 ? 13.482  6.332   19.804  1.00 22.77  ? 1142 PHE   B CZ  1 
ATOM   4673 N  N   . GLN   B 1 291 ? 13.401  1.268   25.480  1.00 28.56  ? 1143 GLN   B N   1 
ATOM   4674 C  CA  . GLN   B 1 291 ? 13.194  -0.065  26.093  1.00 30.65  ? 1143 GLN   B CA  1 
ATOM   4675 C  C   . GLN   B 1 291 ? 11.815  -0.150  26.782  1.00 32.56  ? 1143 GLN   B C   1 
ATOM   4676 O  O   . GLN   B 1 291 ? 11.128  -1.169  26.684  1.00 35.13  ? 1143 GLN   B O   1 
ATOM   4677 C  CB  . GLN   B 1 291 ? 14.344  -0.427  27.070  1.00 37.83  ? 1143 GLN   B CB  1 
ATOM   4678 C  CG  . GLN   B 1 291 ? 14.296  -1.858  27.682  1.00 38.66  ? 1143 GLN   B CG  1 
ATOM   4679 C  CD  . GLN   B 1 291 ? 14.073  -2.995  26.651  1.00 52.45  ? 1143 GLN   B CD  1 
ATOM   4680 O  OE1 . GLN   B 1 291 ? 14.549  -2.940  25.512  1.00 50.62  ? 1143 GLN   B OE1 1 
ATOM   4681 N  NE2 . GLN   B 1 291 ? 13.347  -4.031  27.071  1.00 53.62  ? 1143 GLN   B NE2 1 
ATOM   4682 N  N   . ASN   B 1 292 ? 11.413  0.932   27.451  1.00 31.29  ? 1144 ASN   B N   1 
ATOM   4683 C  CA  . ASN   B 1 292 ? 10.101  1.023   28.086  1.00 34.51  ? 1144 ASN   B CA  1 
ATOM   4684 C  C   . ASN   B 1 292 ? 8.940   1.015   27.089  1.00 31.41  ? 1144 ASN   B C   1 
ATOM   4685 O  O   . ASN   B 1 292 ? 7.867   0.488   27.401  1.00 32.09  ? 1144 ASN   B O   1 
ATOM   4686 C  CB  . ASN   B 1 292 ? 10.034  2.275   28.962  1.00 37.38  ? 1144 ASN   B CB  1 
ATOM   4687 C  CG  . ASN   B 1 292 ? 8.751   2.367   29.792  1.00 43.40  ? 1144 ASN   B CG  1 
ATOM   4688 O  OD1 . ASN   B 1 292 ? 8.410   1.450   30.539  1.00 48.88  ? 1144 ASN   B OD1 1 
ATOM   4689 N  ND2 . ASN   B 1 292 ? 8.054   3.491   29.677  1.00 41.66  ? 1144 ASN   B ND2 1 
ATOM   4690 N  N   . LEU   B 1 293 ? 9.141   1.628   25.926  1.00 26.76  ? 1145 LEU   B N   1 
ATOM   4691 C  CA  . LEU   B 1 293 ? 8.152   1.555   24.826  1.00 27.45  ? 1145 LEU   B CA  1 
ATOM   4692 C  C   . LEU   B 1 293 ? 8.033   0.119   24.324  1.00 25.78  ? 1145 LEU   B C   1 
ATOM   4693 O  O   . LEU   B 1 293 ? 6.931   -0.425  24.194  1.00 23.91  ? 1145 LEU   B O   1 
ATOM   4694 C  CB  . LEU   B 1 293 ? 8.520   2.499   23.688  1.00 24.96  ? 1145 LEU   B CB  1 
ATOM   4695 C  CG  . LEU   B 1 293 ? 8.262   3.998   23.884  1.00 23.52  ? 1145 LEU   B CG  1 
ATOM   4696 C  CD1 . LEU   B 1 293 ? 9.132   4.859   22.986  1.00 26.33  ? 1145 LEU   B CD1 1 
ATOM   4697 C  CD2 . LEU   B 1 293 ? 6.778   4.324   23.689  1.00 22.85  ? 1145 LEU   B CD2 1 
ATOM   4698 N  N   . ILE   B 1 294 ? 9.179   -0.504  24.094  1.00 23.81  ? 1146 ILE   B N   1 
ATOM   4699 C  CA  . ILE   B 1 294 ? 9.228   -1.912  23.697  1.00 27.00  ? 1146 ILE   B CA  1 
ATOM   4700 C  C   . ILE   B 1 294 ? 8.451   -2.768  24.690  1.00 27.26  ? 1146 ILE   B C   1 
ATOM   4701 O  O   . ILE   B 1 294 ? 7.560   -3.524  24.291  1.00 27.11  ? 1146 ILE   B O   1 
ATOM   4702 C  CB  . ILE   B 1 294 ? 10.688  -2.428  23.533  1.00 25.44  ? 1146 ILE   B CB  1 
ATOM   4703 C  CG1 . ILE   B 1 294 ? 11.329  -1.765  22.321  1.00 25.18  ? 1146 ILE   B CG1 1 
ATOM   4704 C  CG2 . ILE   B 1 294 ? 10.726  -3.959  23.358  1.00 25.37  ? 1146 ILE   B CG2 1 
ATOM   4705 C  CD1 . ILE   B 1 294 ? 12.830  -1.937  22.227  1.00 29.33  ? 1146 ILE   B CD1 1 
ATOM   4706 N  N   . GLU   B 1 295 ? 8.764   -2.631  25.979  1.00 30.23  ? 1147 GLU   B N   1 
ATOM   4707 C  CA  . GLU   B 1 295 ? 8.052   -3.361  27.025  1.00 33.48  ? 1147 GLU   B CA  1 
ATOM   4708 C  C   . GLU   B 1 295 ? 6.553   -3.066  27.045  1.00 34.01  ? 1147 GLU   B C   1 
ATOM   4709 O  O   . GLU   B 1 295 ? 5.749   -3.987  27.234  1.00 36.47  ? 1147 GLU   B O   1 
ATOM   4710 C  CB  . GLU   B 1 295 ? 8.664   -3.057  28.390  1.00 36.43  ? 1147 GLU   B CB  1 
ATOM   4711 C  CG  . GLU   B 1 295 ? 10.041  -3.671  28.558  1.00 40.32  ? 1147 GLU   B CG  1 
ATOM   4712 C  CD  . GLU   B 1 295 ? 10.689  -3.332  29.896  1.00 50.44  ? 1147 GLU   B CD  1 
ATOM   4713 O  OE1 . GLU   B 1 295 ? 9.965   -3.195  30.910  1.00 57.16  ? 1147 GLU   B OE1 1 
ATOM   4714 O  OE2 . GLU   B 1 295 ? 11.928  -3.203  29.930  1.00 51.67  ? 1147 GLU   B OE2 1 
ATOM   4715 N  N   . GLY   B 1 296 ? 6.180   -1.804  26.829  1.00 30.18  ? 1148 GLY   B N   1 
ATOM   4716 C  CA  . GLY   B 1 296 ? 4.770   -1.401  26.847  1.00 31.91  ? 1148 GLY   B CA  1 
ATOM   4717 C  C   . GLY   B 1 296 ? 3.958   -1.993  25.702  1.00 29.69  ? 1148 GLY   B C   1 
ATOM   4718 O  O   . GLY   B 1 296 ? 2.842   -2.486  25.911  1.00 30.15  ? 1148 GLY   B O   1 
ATOM   4719 N  N   . PHE   B 1 297 ? 4.527   -1.946  24.498  1.00 27.89  ? 1149 PHE   B N   1 
ATOM   4720 C  CA  . PHE   B 1 297 ? 3.895   -2.534  23.302  1.00 25.36  ? 1149 PHE   B CA  1 
ATOM   4721 C  C   . PHE   B 1 297 ? 3.786   -4.053  23.396  1.00 28.82  ? 1149 PHE   B C   1 
ATOM   4722 O  O   . PHE   B 1 297 ? 2.745   -4.629  23.057  1.00 29.53  ? 1149 PHE   B O   1 
ATOM   4723 C  CB  . PHE   B 1 297 ? 4.667   -2.157  22.037  1.00 22.80  ? 1149 PHE   B CB  1 
ATOM   4724 C  CG  . PHE   B 1 297 ? 4.660   -0.683  21.724  1.00 20.25  ? 1149 PHE   B CG  1 
ATOM   4725 C  CD1 . PHE   B 1 297 ? 3.464   0.038   21.656  1.00 28.69  ? 1149 PHE   B CD1 1 
ATOM   4726 C  CD2 . PHE   B 1 297 ? 5.852   -0.018  21.454  1.00 19.96  ? 1149 PHE   B CD2 1 
ATOM   4727 C  CE1 . PHE   B 1 297 ? 3.466   1.402   21.352  1.00 27.07  ? 1149 PHE   B CE1 1 
ATOM   4728 C  CE2 . PHE   B 1 297 ? 5.857   1.341   21.159  1.00 20.85  ? 1149 PHE   B CE2 1 
ATOM   4729 C  CZ  . PHE   B 1 297 ? 4.663   2.046   21.101  1.00 29.01  ? 1149 PHE   B CZ  1 
ATOM   4730 N  N   . GLU   B 1 298 ? 4.859   -4.692  23.865  1.00 31.75  ? 1150 GLU   B N   1 
ATOM   4731 C  CA  . GLU   B 1 298 ? 4.909   -6.153  24.023  1.00 35.44  ? 1150 GLU   B CA  1 
ATOM   4732 C  C   . GLU   B 1 298 ? 3.843   -6.692  24.994  1.00 37.28  ? 1150 GLU   B C   1 
ATOM   4733 O  O   . GLU   B 1 298 ? 3.311   -7.795  24.780  1.00 37.69  ? 1150 GLU   B O   1 
ATOM   4734 C  CB  . GLU   B 1 298 ? 6.313   -6.608  24.446  1.00 37.15  ? 1150 GLU   B CB  1 
ATOM   4735 C  CG  . GLU   B 1 298 ? 7.311   -6.657  23.292  1.00 34.33  ? 1150 GLU   B CG  1 
ATOM   4736 C  CD  . GLU   B 1 298 ? 8.727   -7.000  23.726  1.00 43.32  ? 1150 GLU   B CD  1 
ATOM   4737 O  OE1 . GLU   B 1 298 ? 8.951   -7.315  24.924  1.00 53.01  ? 1150 GLU   B OE1 1 
ATOM   4738 O  OE2 . GLU   B 1 298 ? 9.626   -6.939  22.856  1.00 50.93  ? 1150 GLU   B OE2 1 
ATOM   4739 N  N   . ALA   B 1 299 ? 3.530   -5.916  26.035  1.00 37.90  ? 1151 ALA   B N   1 
ATOM   4740 C  CA  . ALA   B 1 299 ? 2.447   -6.260  26.963  1.00 41.88  ? 1151 ALA   B CA  1 
ATOM   4741 C  C   . ALA   B 1 299 ? 1.074   -6.178  26.287  1.00 40.71  ? 1151 ALA   B C   1 
ATOM   4742 O  O   . ALA   B 1 299 ? 0.209   -7.032  26.522  1.00 41.67  ? 1151 ALA   B O   1 
ATOM   4743 C  CB  . ALA   B 1 299 ? 2.486   -5.352  28.199  1.00 45.36  ? 1151 ALA   B CB  1 
ATOM   4744 N  N   . LEU   B 1 300 ? 0.875   -5.149  25.464  1.00 36.64  ? 1152 LEU   B N   1 
ATOM   4745 C  CA  . LEU   B 1 300 ? -0.371  -4.984  24.706  1.00 37.23  ? 1152 LEU   B CA  1 
ATOM   4746 C  C   . LEU   B 1 300 ? -0.545  -6.100  23.673  1.00 35.65  ? 1152 LEU   B C   1 
ATOM   4747 O  O   . LEU   B 1 300 ? -1.665  -6.538  23.415  1.00 36.47  ? 1152 LEU   B O   1 
ATOM   4748 C  CB  . LEU   B 1 300 ? -0.423  -3.611  24.025  1.00 35.07  ? 1152 LEU   B CB  1 
ATOM   4749 C  CG  . LEU   B 1 300 ? -0.501  -2.399  24.955  1.00 37.79  ? 1152 LEU   B CG  1 
ATOM   4750 C  CD1 . LEU   B 1 300 ? -0.187  -1.104  24.229  1.00 35.83  ? 1152 LEU   B CD1 1 
ATOM   4751 C  CD2 . LEU   B 1 300 ? -1.873  -2.300  25.603  1.00 42.33  ? 1152 LEU   B CD2 1 
ATOM   4752 N  N   . LEU   B 1 301 ? 0.568   -6.585  23.134  1.00 33.87  ? 1153 LEU   B N   1 
ATOM   4753 C  CA  . LEU   B 1 301 ? 0.566   -7.678  22.155  1.00 35.44  ? 1153 LEU   B CA  1 
ATOM   4754 C  C   . LEU   B 1 301 ? 0.343   -9.072  22.777  1.00 40.60  ? 1153 LEU   B C   1 
ATOM   4755 O  O   . LEU   B 1 301 ? 0.220   -10.057 22.037  1.00 41.59  ? 1153 LEU   B O   1 
ATOM   4756 C  CB  . LEU   B 1 301 ? 1.877   -7.666  21.365  1.00 29.14  ? 1153 LEU   B CB  1 
ATOM   4757 C  CG  . LEU   B 1 301 ? 2.105   -6.476  20.424  1.00 30.05  ? 1153 LEU   B CG  1 
ATOM   4758 C  CD1 . LEU   B 1 301 ? 3.591   -6.265  20.146  1.00 30.03  ? 1153 LEU   B CD1 1 
ATOM   4759 C  CD2 . LEU   B 1 301 ? 1.318   -6.699  19.144  1.00 27.04  ? 1153 LEU   B CD2 1 
ATOM   4760 N  N   . LYS   B 1 302 ? 0.314   -9.130  24.118  1.00 44.59  ? 1154 LYS   B N   1 
ATOM   4761 C  CA  . LYS   B 1 302 ? 0.032   -10.316 24.937  1.00 52.19  ? 1154 LYS   B CA  1 
ATOM   4762 C  C   . LYS   B 1 302 ? 1.244   -11.235 25.012  1.00 56.39  ? 1154 LYS   B C   1 
ATOM   4763 O  O   . LYS   B 1 302 ? 1.993   -11.201 25.999  1.00 59.43  ? 1154 LYS   B O   1 
ATOM   4764 C  CB  . LYS   B 1 302 ? -1.231  -11.066 24.486  1.00 52.30  ? 1154 LYS   B CB  1 
ATOM   4765 C  CG  . LYS   B 1 302 ? -2.463  -10.179 24.412  1.00 52.32  ? 1154 LYS   B CG  1 
ATOM   4766 C  CD  . LYS   B 1 302 ? -3.716  -10.937 24.011  0.00 53.78  ? 1154 LYS   B CD  1 
ATOM   4767 C  CE  . LYS   B 1 302 ? -3.750  -11.229 22.517  0.00 51.61  ? 1154 LYS   B CE  1 
ATOM   4768 N  NZ  . LYS   B 1 302 ? -5.013  -11.902 22.109  0.00 52.61  ? 1154 LYS   B NZ  1 
HETATM 4769 C  C1  . A1H5R C 2 .   ? 7.113   56.426  3.778   1.00 21.00  ? 1201 A1H5R A C1  1 
HETATM 4770 C  C2  . A1H5R C 2 .   ? 8.044   55.787  2.735   1.00 20.84  ? 1201 A1H5R A C2  1 
HETATM 4771 C  C3  . A1H5R C 2 .   ? 7.276   54.925  1.746   1.00 19.90  ? 1201 A1H5R A C3  1 
HETATM 4772 C  C4  . A1H5R C 2 .   ? 6.587   53.820  2.206   1.00 21.29  ? 1201 A1H5R A C4  1 
HETATM 4773 C  C5  . A1H5R C 2 .   ? 5.885   52.988  1.346   1.00 21.02  ? 1201 A1H5R A C5  1 
HETATM 4774 C  C6  . A1H5R C 2 .   ? 5.865   53.259  -0.016  1.00 18.25  ? 1201 A1H5R A C6  1 
HETATM 4775 C  C7  . A1H5R C 2 .   ? 6.547   54.346  -0.512  1.00 20.92  ? 1201 A1H5R A C7  1 
HETATM 4776 C  C8  . A1H5R C 2 .   ? 7.260   55.185  0.359   1.00 19.60  ? 1201 A1H5R A C8  1 
HETATM 4777 C  C11 . A1H5R C 2 .   ? 7.416   57.549  -0.153  1.00 20.23  ? 1201 A1H5R A C11 1 
HETATM 4778 C  C12 . A1H5R C 2 .   ? 6.153   57.791  0.419   1.00 14.25  ? 1201 A1H5R A C12 1 
HETATM 4779 C  C15 . A1H5R C 2 .   ? 7.719   59.796  -0.664  1.00 25.13  ? 1201 A1H5R A C15 1 
HETATM 4780 C  C18 . A1H5R C 2 .   ? 4.646   61.001  0.605   1.00 17.04  ? 1201 A1H5R A C18 1 
HETATM 4781 N  N9  . A1H5R C 2 .   ? 7.969   56.278  -0.144  1.00 19.56  ? 1201 A1H5R A N9  1 
HETATM 4782 C  C10 . A1H5R C 2 .   ? 9.379   56.007  -0.478  1.00 21.92  ? 1201 A1H5R A C10 1 
HETATM 4783 C  C13 . A1H5R C 2 .   ? 5.690   59.094  0.428   1.00 17.17  ? 1201 A1H5R A C13 1 
HETATM 4784 C  C14 . A1H5R C 2 .   ? 6.472   60.125  -0.122  1.00 17.22  ? 1201 A1H5R A C14 1 
HETATM 4785 N  N16 . A1H5R C 2 .   ? 8.129   58.549  -0.660  1.00 20.14  ? 1201 A1H5R A N16 1 
HETATM 4786 N  N17 . A1H5R C 2 .   ? 5.775   61.271  0.021   1.00 15.71  ? 1201 A1H5R A N17 1 
HETATM 4787 N  N19 . A1H5R C 2 .   ? 4.545   59.678  0.890   1.00 20.62  ? 1201 A1H5R A N19 1 
HETATM 4788 C  C20 . A1H5R C 2 .   ? 3.430   58.971  1.529   1.00 20.74  ? 1201 A1H5R A C20 1 
HETATM 4789 NA NA  . NA    D 3 .   ? -13.755 57.849  11.851  1.00 32.92  1 1202 NA    A NA  1 
HETATM 4790 NA NA  . NA    E 3 .   ? -5.102  64.652  8.827   1.00 42.15  1 1203 NA    A NA  1 
HETATM 4791 NA NA  . NA    F 3 .   ? 11.268  65.294  -6.558  1.00 62.05  1 1204 NA    A NA  1 
HETATM 4792 C  C1  . A1H5R G 2 .   ? 14.220  5.269   3.462   1.00 18.95  ? 1201 A1H5R B C1  1 
HETATM 4793 C  C2  . A1H5R G 2 .   ? 13.309  5.962   2.450   1.00 18.44  ? 1201 A1H5R B C2  1 
HETATM 4794 C  C3  . A1H5R G 2 .   ? 14.126  6.851   1.523   1.00 13.98  ? 1201 A1H5R B C3  1 
HETATM 4795 C  C4  . A1H5R G 2 .   ? 14.820  7.931   2.048   1.00 18.00  ? 1201 A1H5R B C4  1 
HETATM 4796 C  C5  . A1H5R G 2 .   ? 15.589  8.787   1.233   1.00 16.12  ? 1201 A1H5R B C5  1 
HETATM 4797 C  C6  . A1H5R G 2 .   ? 15.626  8.564   -0.134  1.00 17.65  ? 1201 A1H5R B C6  1 
HETATM 4798 C  C7  . A1H5R G 2 .   ? 14.918  7.499   -0.676  1.00 17.24  ? 1201 A1H5R B C7  1 
HETATM 4799 C  C8  . A1H5R G 2 .   ? 14.163  6.637   0.125   1.00 15.38  ? 1201 A1H5R B C8  1 
HETATM 4800 C  C11 . A1H5R G 2 .   ? 13.987  4.267   -0.462  1.00 12.38  ? 1201 A1H5R B C11 1 
HETATM 4801 C  C12 . A1H5R G 2 .   ? 15.243  3.957   0.086   1.00 11.19  ? 1201 A1H5R B C12 1 
HETATM 4802 C  C15 . A1H5R G 2 .   ? 13.675  2.038   -1.108  1.00 14.61  ? 1201 A1H5R B C15 1 
HETATM 4803 C  C18 . A1H5R G 2 .   ? 16.651  0.682   0.134   1.00 12.44  ? 1201 A1H5R B C18 1 
HETATM 4804 N  N9  . A1H5R G 2 .   ? 13.447  5.558   -0.410  1.00 15.80  ? 1201 A1H5R B N9  1 
HETATM 4805 C  C10 . A1H5R G 2 .   ? 12.038  5.855   -0.730  1.00 17.64  ? 1201 A1H5R B C10 1 
HETATM 4806 C  C13 . A1H5R G 2 .   ? 15.687  2.642   0.039   1.00 12.54  ? 1201 A1H5R B C13 1 
HETATM 4807 C  C14 . A1H5R G 2 .   ? 14.888  1.642   -0.579  1.00 13.20  ? 1201 A1H5R B C14 1 
HETATM 4808 N  N16 . A1H5R G 2 .   ? 13.281  3.280   -1.009  1.00 15.52  ? 1201 A1H5R B N16 1 
HETATM 4809 N  N17 . A1H5R G 2 .   ? 15.540  0.469   -0.474  1.00 11.84  ? 1201 A1H5R B N17 1 
HETATM 4810 N  N19 . A1H5R G 2 .   ? 16.799  1.989   0.477   1.00 11.39  ? 1201 A1H5R B N19 1 
HETATM 4811 C  C20 . A1H5R G 2 .   ? 17.923  2.629   1.179   1.00 14.07  ? 1201 A1H5R B C20 1 
HETATM 4812 O  O   . HOH   H 4 .   ? -17.237 63.938  -1.446  0.50 18.90  ? 1301 HOH   A O   1 
HETATM 4813 O  O   . HOH   H 4 .   ? -13.344 62.907  -0.426  0.50 12.90  ? 1302 HOH   A O   1 
HETATM 4814 O  O   . HOH   H 4 .   ? 12.663  54.691  -1.211  0.50 22.81  ? 1303 HOH   A O   1 
HETATM 4815 O  O   . HOH   H 4 .   ? -11.023 66.469  8.528   1.00 38.17  ? 1304 HOH   A O   1 
HETATM 4816 O  O   . HOH   H 4 .   ? 18.057  68.563  2.402   1.00 31.62  ? 1305 HOH   A O   1 
HETATM 4817 O  O   . HOH   H 4 .   ? -16.171 63.912  2.107   1.00 25.50  ? 1306 HOH   A O   1 
HETATM 4818 O  O   . HOH   H 4 .   ? -17.279 70.553  -0.116  1.00 43.52  ? 1307 HOH   A O   1 
HETATM 4819 O  O   . HOH   H 4 .   ? 16.631  61.956  -0.789  1.00 30.49  ? 1308 HOH   A O   1 
HETATM 4820 O  O   . HOH   H 4 .   ? 23.617  69.105  10.559  1.00 28.95  ? 1309 HOH   A O   1 
HETATM 4821 O  O   . HOH   H 4 .   ? -33.440 67.398  -6.799  1.00 22.71  ? 1310 HOH   A O   1 
HETATM 4822 O  O   . HOH   H 4 .   ? 7.471   68.455  16.257  1.00 25.06  ? 1311 HOH   A O   1 
HETATM 4823 O  O   . HOH   H 4 .   ? 13.900  41.740  16.588  1.00 27.25  ? 1312 HOH   A O   1 
HETATM 4824 O  O   . HOH   H 4 .   ? -12.872 60.304  -6.827  1.00 39.40  ? 1313 HOH   A O   1 
HETATM 4825 O  O   . HOH   H 4 .   ? -5.225  66.149  -16.440 1.00 34.58  ? 1314 HOH   A O   1 
HETATM 4826 O  O   . HOH   H 4 .   ? -5.569  65.945  16.527  1.00 32.63  ? 1315 HOH   A O   1 
HETATM 4827 O  O   . HOH   H 4 .   ? -8.860  52.444  20.471  1.00 27.78  ? 1316 HOH   A O   1 
HETATM 4828 O  O   . HOH   H 4 .   ? 21.002  70.458  9.765   1.00 37.88  ? 1317 HOH   A O   1 
HETATM 4829 O  O   . HOH   H 4 .   ? -10.990 65.271  11.062  1.00 40.29  ? 1318 HOH   A O   1 
HETATM 4830 O  O   . HOH   H 4 .   ? 16.032  44.223  30.315  1.00 33.09  ? 1319 HOH   A O   1 
HETATM 4831 O  O   . HOH   H 4 .   ? 0.323   49.690  25.355  1.00 39.16  ? 1320 HOH   A O   1 
HETATM 4832 O  O   . HOH   H 4 .   ? 12.688  69.516  21.577  1.00 46.93  ? 1321 HOH   A O   1 
HETATM 4833 O  O   . HOH   H 4 .   ? 8.809   64.758  27.174  1.00 33.68  ? 1322 HOH   A O   1 
HETATM 4834 O  O   . HOH   H 4 .   ? -45.314 66.660  -17.802 1.00 30.47  ? 1323 HOH   A O   1 
HETATM 4835 O  O   . HOH   H 4 .   ? 2.169   53.524  19.690  1.00 23.02  ? 1324 HOH   A O   1 
HETATM 4836 O  O   . HOH   H 4 .   ? 33.240  55.018  16.409  1.00 48.11  ? 1325 HOH   A O   1 
HETATM 4837 O  O   . HOH   H 4 .   ? 6.800   50.418  4.198   1.00 37.76  ? 1326 HOH   A O   1 
HETATM 4838 O  O   . HOH   H 4 .   ? -3.022  73.804  -11.809 1.00 30.66  ? 1327 HOH   A O   1 
HETATM 4839 O  O   . HOH   H 4 .   ? 30.582  59.708  26.271  1.00 40.85  ? 1328 HOH   A O   1 
HETATM 4840 O  O   . HOH   H 4 .   ? 35.735  58.775  13.834  1.00 26.79  ? 1329 HOH   A O   1 
HETATM 4841 O  O   . HOH   H 4 .   ? 5.069   68.870  2.706   1.00 27.24  ? 1330 HOH   A O   1 
HETATM 4842 O  O   . HOH   H 4 .   ? 12.701  57.529  -0.739  0.50 11.59  ? 1331 HOH   A O   1 
HETATM 4843 O  O   . HOH   H 4 .   ? 10.554  53.225  2.159   1.00 28.54  ? 1332 HOH   A O   1 
HETATM 4844 O  O   . HOH   H 4 .   ? 7.388   52.297  26.817  1.00 39.78  ? 1333 HOH   A O   1 
HETATM 4845 O  O   . HOH   H 4 .   ? 13.068  53.655  1.489   1.00 32.10  ? 1334 HOH   A O   1 
HETATM 4846 O  O   . HOH   H 4 .   ? 2.078   67.397  -2.015  1.00 17.39  ? 1335 HOH   A O   1 
HETATM 4847 O  O   . HOH   H 4 .   ? 5.597   68.869  -4.785  1.00 22.93  ? 1336 HOH   A O   1 
HETATM 4848 O  O   . HOH   H 4 .   ? -0.784  53.902  -6.276  1.00 34.66  ? 1337 HOH   A O   1 
HETATM 4849 O  O   . HOH   H 4 .   ? 15.057  67.374  29.182  1.00 33.73  ? 1338 HOH   A O   1 
HETATM 4850 O  O   . HOH   H 4 .   ? 25.413  66.515  24.343  1.00 37.45  ? 1339 HOH   A O   1 
HETATM 4851 O  O   . HOH   H 4 .   ? 26.636  61.169  1.981   1.00 22.36  ? 1340 HOH   A O   1 
HETATM 4852 O  O   . HOH   H 4 .   ? -0.196  55.519  4.993   1.00 19.35  ? 1341 HOH   A O   1 
HETATM 4853 O  O   . HOH   H 4 .   ? -1.996  76.764  -18.954 1.00 34.84  ? 1342 HOH   A O   1 
HETATM 4854 O  O   . HOH   H 4 .   ? -8.305  57.428  18.017  1.00 37.70  ? 1343 HOH   A O   1 
HETATM 4855 O  O   . HOH   H 4 .   ? 15.535  67.917  2.120   1.00 40.67  ? 1344 HOH   A O   1 
HETATM 4856 O  O   . HOH   H 4 .   ? -11.917 54.671  4.527   1.00 24.29  ? 1345 HOH   A O   1 
HETATM 4857 O  O   . HOH   H 4 .   ? 28.324  61.436  16.495  1.00 32.86  ? 1346 HOH   A O   1 
HETATM 4858 O  O   . HOH   H 4 .   ? 3.672   49.956  4.064   1.00 36.41  ? 1347 HOH   A O   1 
HETATM 4859 O  O   A HOH   H 4 .   ? 27.338  54.909  8.462   0.50 17.25  ? 1348 HOH   A O   1 
HETATM 4860 O  O   B HOH   H 4 .   ? 27.621  54.993  6.279   0.50 18.76  ? 1348 HOH   A O   1 
HETATM 4861 O  O   . HOH   H 4 .   ? 1.171   69.456  2.099   1.00 25.08  ? 1349 HOH   A O   1 
HETATM 4862 O  O   . HOH   H 4 .   ? 4.578   68.440  -2.042  1.00 27.97  ? 1350 HOH   A O   1 
HETATM 4863 O  O   . HOH   H 4 .   ? 5.816   63.669  30.279  1.00 39.84  ? 1351 HOH   A O   1 
HETATM 4864 O  O   . HOH   H 4 .   ? -32.652 61.972  -12.529 1.00 37.46  ? 1352 HOH   A O   1 
HETATM 4865 O  O   . HOH   H 4 .   ? 23.242  49.694  29.699  1.00 46.76  ? 1353 HOH   A O   1 
HETATM 4866 O  O   . HOH   H 4 .   ? -12.649 48.173  6.029   1.00 36.31  ? 1354 HOH   A O   1 
HETATM 4867 O  O   . HOH   H 4 .   ? 14.963  44.161  17.071  1.00 24.77  ? 1355 HOH   A O   1 
HETATM 4868 O  O   . HOH   H 4 .   ? -16.194 57.997  -7.951  1.00 38.90  ? 1356 HOH   A O   1 
HETATM 4869 O  O   . HOH   H 4 .   ? -2.244  63.399  8.454   1.00 21.67  ? 1357 HOH   A O   1 
HETATM 4870 O  O   . HOH   H 4 .   ? 8.865   40.799  26.198  1.00 27.93  ? 1358 HOH   A O   1 
HETATM 4871 O  O   . HOH   H 4 .   ? 3.194   55.820  21.226  1.00 19.80  ? 1359 HOH   A O   1 
HETATM 4872 O  O   . HOH   H 4 .   ? -41.508 73.089  -7.927  1.00 40.29  ? 1360 HOH   A O   1 
HETATM 4873 O  O   . HOH   H 4 .   ? 18.904  50.737  7.699   1.00 28.11  ? 1361 HOH   A O   1 
HETATM 4874 O  O   . HOH   H 4 .   ? 16.792  43.080  28.396  1.00 42.64  ? 1362 HOH   A O   1 
HETATM 4875 O  O   . HOH   H 4 .   ? -2.941  55.619  -9.327  1.00 28.57  ? 1363 HOH   A O   1 
HETATM 4876 O  O   . HOH   H 4 .   ? 0.306   48.977  3.451   1.00 34.05  ? 1364 HOH   A O   1 
HETATM 4877 O  O   . HOH   H 4 .   ? 5.255   58.754  26.147  1.00 27.85  ? 1365 HOH   A O   1 
HETATM 4878 O  O   . HOH   H 4 .   ? -13.980 52.936  23.943  1.00 26.65  ? 1366 HOH   A O   1 
HETATM 4879 O  O   A HOH   H 4 .   ? -0.189  71.346  -2.682  0.50 26.33  ? 1367 HOH   A O   1 
HETATM 4880 O  O   B HOH   H 4 .   ? 2.000   71.632  -3.834  0.50 24.88  ? 1367 HOH   A O   1 
HETATM 4881 O  O   . HOH   H 4 .   ? 10.753  66.390  0.892   1.00 18.39  ? 1368 HOH   A O   1 
HETATM 4882 O  O   . HOH   H 4 .   ? 3.701   51.155  8.066   1.00 18.16  ? 1369 HOH   A O   1 
HETATM 4883 O  O   . HOH   H 4 .   ? -7.915  63.556  -18.174 1.00 46.99  ? 1370 HOH   A O   1 
HETATM 4884 O  O   . HOH   H 4 .   ? 19.069  45.555  19.663  1.00 24.97  ? 1371 HOH   A O   1 
HETATM 4885 O  O   . HOH   H 4 .   ? -3.783  70.456  -8.491  1.00 28.20  ? 1372 HOH   A O   1 
HETATM 4886 O  O   . HOH   H 4 .   ? 14.311  50.870  7.332   1.00 17.85  ? 1373 HOH   A O   1 
HETATM 4887 O  O   . HOH   H 4 .   ? -2.243  71.110  5.698   1.00 52.52  ? 1374 HOH   A O   1 
HETATM 4888 O  O   . HOH   H 4 .   ? -29.706 72.075  -3.625  1.00 51.59  ? 1375 HOH   A O   1 
HETATM 4889 O  O   . HOH   H 4 .   ? -6.383  59.280  -15.093 1.00 36.23  ? 1376 HOH   A O   1 
HETATM 4890 O  O   . HOH   H 4 .   ? -3.868  71.250  -13.014 1.00 18.19  ? 1377 HOH   A O   1 
HETATM 4891 O  O   . HOH   H 4 .   ? 12.038  47.293  8.688   1.00 32.78  ? 1378 HOH   A O   1 
HETATM 4892 O  O   . HOH   H 4 .   ? 20.671  52.071  29.177  1.00 32.20  ? 1379 HOH   A O   1 
HETATM 4893 O  O   . HOH   H 4 .   ? 21.541  50.427  11.636  1.00 19.73  ? 1380 HOH   A O   1 
HETATM 4894 O  O   . HOH   H 4 .   ? -6.595  50.716  -4.633  1.00 26.23  ? 1381 HOH   A O   1 
HETATM 4895 O  O   . HOH   H 4 .   ? 27.889  51.017  11.183  1.00 29.55  ? 1382 HOH   A O   1 
HETATM 4896 O  O   . HOH   H 4 .   ? -9.834  53.052  10.816  1.00 27.04  ? 1383 HOH   A O   1 
HETATM 4897 O  O   . HOH   H 4 .   ? 2.146   67.310  8.939   1.00 21.71  ? 1384 HOH   A O   1 
HETATM 4898 O  O   . HOH   H 4 .   ? -3.616  67.542  16.617  1.00 48.04  ? 1385 HOH   A O   1 
HETATM 4899 O  O   . HOH   H 4 .   ? 19.817  62.429  28.306  1.00 30.44  ? 1386 HOH   A O   1 
HETATM 4900 O  O   . HOH   H 4 .   ? 6.761   50.891  29.323  1.00 43.66  ? 1387 HOH   A O   1 
HETATM 4901 O  O   . HOH   H 4 .   ? 31.436  64.608  5.712   1.00 16.78  ? 1388 HOH   A O   1 
HETATM 4902 O  O   . HOH   H 4 .   ? 30.284  55.205  22.375  1.00 34.13  ? 1389 HOH   A O   1 
HETATM 4903 O  O   . HOH   H 4 .   ? -3.600  50.705  9.236   1.00 22.68  ? 1390 HOH   A O   1 
HETATM 4904 O  O   . HOH   H 4 .   ? -2.527  35.302  16.481  1.00 32.65  ? 1391 HOH   A O   1 
HETATM 4905 O  O   . HOH   H 4 .   ? 8.210   53.735  -11.402 1.00 26.77  ? 1392 HOH   A O   1 
HETATM 4906 O  O   . HOH   H 4 .   ? -39.716 70.097  -5.542  1.00 31.22  ? 1393 HOH   A O   1 
HETATM 4907 O  O   . HOH   H 4 .   ? 6.499   68.464  0.585   1.00 23.79  ? 1394 HOH   A O   1 
HETATM 4908 O  O   . HOH   H 4 .   ? 10.468  58.613  -2.184  1.00 20.33  ? 1395 HOH   A O   1 
HETATM 4909 O  O   . HOH   H 4 .   ? 1.878   51.119  10.256  1.00 14.55  ? 1396 HOH   A O   1 
HETATM 4910 O  O   . HOH   H 4 .   ? 28.090  64.199  9.484   1.00 25.46  ? 1397 HOH   A O   1 
HETATM 4911 O  O   . HOH   H 4 .   ? 6.767   49.487  15.324  1.00 19.38  ? 1398 HOH   A O   1 
HETATM 4912 O  O   . HOH   H 4 .   ? -7.020  68.250  0.765   1.00 31.78  ? 1399 HOH   A O   1 
HETATM 4913 O  O   . HOH   H 4 .   ? 4.865   70.321  6.513   1.00 45.21  ? 1400 HOH   A O   1 
HETATM 4914 O  O   . HOH   H 4 .   ? 20.548  71.041  13.549  1.00 25.44  ? 1401 HOH   A O   1 
HETATM 4915 O  O   . HOH   H 4 .   ? 27.998  48.074  21.654  1.00 27.66  ? 1402 HOH   A O   1 
HETATM 4916 O  O   . HOH   H 4 .   ? 17.200  40.245  27.647  1.00 38.40  ? 1403 HOH   A O   1 
HETATM 4917 O  O   . HOH   H 4 .   ? 27.773  55.760  12.343  1.00 27.31  ? 1404 HOH   A O   1 
HETATM 4918 O  O   . HOH   H 4 .   ? 19.072  70.653  29.890  1.00 41.88  ? 1405 HOH   A O   1 
HETATM 4919 O  O   . HOH   H 4 .   ? -5.282  48.712  8.039   1.00 30.10  ? 1406 HOH   A O   1 
HETATM 4920 O  O   . HOH   H 4 .   ? 5.395   56.217  25.420  1.00 23.45  ? 1407 HOH   A O   1 
HETATM 4921 O  O   . HOH   H 4 .   ? 24.991  55.445  4.741   1.00 23.26  ? 1408 HOH   A O   1 
HETATM 4922 O  O   . HOH   H 4 .   ? 27.934  57.734  28.947  1.00 36.61  ? 1409 HOH   A O   1 
HETATM 4923 O  O   . HOH   H 4 .   ? -12.045 63.283  3.319   1.00 21.41  ? 1410 HOH   A O   1 
HETATM 4924 O  O   . HOH   H 4 .   ? -11.467 68.257  -8.741  1.00 39.28  ? 1411 HOH   A O   1 
HETATM 4925 O  O   . HOH   H 4 .   ? 9.004   68.532  24.420  1.00 39.88  ? 1412 HOH   A O   1 
HETATM 4926 O  O   . HOH   H 4 .   ? 13.334  43.778  31.032  1.00 34.57  ? 1413 HOH   A O   1 
HETATM 4927 O  O   . HOH   H 4 .   ? 16.698  65.492  -0.877  1.00 28.12  ? 1414 HOH   A O   1 
HETATM 4928 O  O   . HOH   H 4 .   ? 18.654  46.539  26.009  1.00 39.54  ? 1415 HOH   A O   1 
HETATM 4929 O  O   . HOH   H 4 .   ? 10.309  68.746  17.601  1.00 30.35  ? 1416 HOH   A O   1 
HETATM 4930 O  O   . HOH   H 4 .   ? -3.882  61.301  -19.636 1.00 39.48  ? 1417 HOH   A O   1 
HETATM 4931 O  O   . HOH   H 4 .   ? -10.826 70.838  -14.470 1.00 41.36  ? 1418 HOH   A O   1 
HETATM 4932 O  O   . HOH   H 4 .   ? -9.117  49.697  -3.871  1.00 35.13  ? 1419 HOH   A O   1 
HETATM 4933 O  O   . HOH   H 4 .   ? 3.987   66.919  19.749  1.00 28.41  ? 1420 HOH   A O   1 
HETATM 4934 O  O   . HOH   H 4 .   ? -8.027  54.355  18.591  1.00 33.95  ? 1421 HOH   A O   1 
HETATM 4935 O  O   . HOH   H 4 .   ? 8.104   45.780  18.105  1.00 30.41  ? 1422 HOH   A O   1 
HETATM 4936 O  O   . HOH   H 4 .   ? -0.643  65.320  10.026  1.00 16.68  ? 1423 HOH   A O   1 
HETATM 4937 O  O   . HOH   H 4 .   ? -9.175  65.073  7.134   1.00 28.04  ? 1424 HOH   A O   1 
HETATM 4938 O  O   . HOH   H 4 .   ? -6.374  49.196  11.528  1.00 34.68  ? 1425 HOH   A O   1 
HETATM 4939 O  O   . HOH   H 4 .   ? 31.017  58.026  24.393  1.00 19.66  ? 1426 HOH   A O   1 
HETATM 4940 O  O   . HOH   H 4 .   ? 4.453   69.881  9.155   1.00 43.18  ? 1427 HOH   A O   1 
HETATM 4941 O  O   . HOH   H 4 .   ? 7.929   65.243  29.767  1.00 34.18  ? 1428 HOH   A O   1 
HETATM 4942 O  O   . HOH   H 4 .   ? -12.988 59.493  -9.662  1.00 25.55  ? 1429 HOH   A O   1 
HETATM 4943 O  O   . HOH   H 4 .   ? 26.512  57.609  15.254  1.00 22.84  ? 1430 HOH   A O   1 
HETATM 4944 O  O   . HOH   H 4 .   ? -11.873 50.541  22.188  1.00 29.33  ? 1431 HOH   A O   1 
HETATM 4945 O  O   . HOH   H 4 .   ? 21.294  51.003  8.679   1.00 21.80  ? 1432 HOH   A O   1 
HETATM 4946 O  O   . HOH   H 4 .   ? 22.958  70.795  13.244  1.00 28.97  ? 1433 HOH   A O   1 
HETATM 4947 O  O   . HOH   H 4 .   ? 20.461  56.171  -0.636  1.00 35.18  ? 1434 HOH   A O   1 
HETATM 4948 O  O   . HOH   H 4 .   ? -1.721  68.973  1.988   1.00 30.10  ? 1435 HOH   A O   1 
HETATM 4949 O  O   . HOH   H 4 .   ? 26.627  60.290  14.834  1.00 27.55  ? 1436 HOH   A O   1 
HETATM 4950 O  O   . HOH   H 4 .   ? 28.730  62.740  11.774  1.00 34.23  ? 1437 HOH   A O   1 
HETATM 4951 O  O   . HOH   H 4 .   ? -17.447 66.423  2.159   1.00 30.51  ? 1438 HOH   A O   1 
HETATM 4952 O  O   . HOH   H 4 .   ? -42.422 74.297  -21.095 1.00 37.62  ? 1439 HOH   A O   1 
HETATM 4953 O  O   . HOH   H 4 .   ? 18.089  31.950  5.435   1.00 42.12  ? 1440 HOH   A O   1 
HETATM 4954 O  O   . HOH   H 4 .   ? 1.893   55.967  2.886   1.00 22.50  ? 1441 HOH   A O   1 
HETATM 4955 O  O   . HOH   H 4 .   ? 9.076   68.559  1.224   1.00 32.80  ? 1442 HOH   A O   1 
HETATM 4956 O  O   . HOH   H 4 .   ? -12.735 60.686  -12.989 1.00 18.86  ? 1443 HOH   A O   1 
HETATM 4957 O  O   . HOH   H 4 .   ? 25.196  71.906  14.570  1.00 40.05  ? 1444 HOH   A O   1 
HETATM 4958 O  O   . HOH   H 4 .   ? 16.069  71.506  3.587   1.00 32.00  ? 1445 HOH   A O   1 
HETATM 4959 O  O   . HOH   H 4 .   ? -16.512 66.891  -5.227  1.00 34.98  ? 1446 HOH   A O   1 
HETATM 4960 O  O   . HOH   H 4 .   ? 26.075  63.811  23.179  1.00 34.51  ? 1447 HOH   A O   1 
HETATM 4961 O  O   . HOH   H 4 .   ? 0.512   69.063  -1.029  1.00 33.43  ? 1448 HOH   A O   1 
HETATM 4962 O  O   . HOH   H 4 .   ? 0.606   60.302  -16.843 1.00 38.82  ? 1449 HOH   A O   1 
HETATM 4963 O  O   . HOH   H 4 .   ? -6.500  47.187  9.608   1.00 36.09  ? 1450 HOH   A O   1 
HETATM 4964 O  O   . HOH   H 4 .   ? 18.730  64.002  -1.094  1.00 30.63  ? 1451 HOH   A O   1 
HETATM 4965 O  O   . HOH   H 4 .   ? 1.789   69.115  15.553  1.00 29.06  ? 1452 HOH   A O   1 
HETATM 4966 O  O   . HOH   H 4 .   ? -11.911 59.340  3.340   1.00 16.71  ? 1453 HOH   A O   1 
HETATM 4967 O  O   . HOH   H 4 .   ? 1.149   58.165  24.388  1.00 39.46  ? 1454 HOH   A O   1 
HETATM 4968 O  O   . HOH   H 4 .   ? -9.834  54.179  -6.908  1.00 38.87  ? 1455 HOH   A O   1 
HETATM 4969 O  O   . HOH   H 4 .   ? -2.089  57.551  -14.503 1.00 32.34  ? 1456 HOH   A O   1 
HETATM 4970 O  O   . HOH   H 4 .   ? 9.680   72.389  3.522   1.00 39.31  ? 1457 HOH   A O   1 
HETATM 4971 O  O   . HOH   H 4 .   ? 24.242  66.135  0.113   1.00 36.64  ? 1458 HOH   A O   1 
HETATM 4972 O  O   . HOH   H 4 .   ? -4.666  66.604  6.925   1.00 29.04  ? 1459 HOH   A O   1 
HETATM 4973 O  O   . HOH   H 4 .   ? 13.462  68.452  16.956  1.00 27.39  ? 1460 HOH   A O   1 
HETATM 4974 O  O   . HOH   H 4 .   ? 13.009  42.391  9.495   1.00 30.37  ? 1461 HOH   A O   1 
HETATM 4975 O  O   . HOH   H 4 .   ? 11.772  71.553  2.304   1.00 43.52  ? 1462 HOH   A O   1 
HETATM 4976 O  O   . HOH   H 4 .   ? 26.586  67.771  16.280  1.00 27.76  ? 1463 HOH   A O   1 
HETATM 4977 O  O   . HOH   H 4 .   ? 3.008   50.088  26.690  1.00 22.67  ? 1464 HOH   A O   1 
HETATM 4978 O  O   . HOH   H 4 .   ? 11.130  60.846  -3.947  1.00 34.87  ? 1465 HOH   A O   1 
HETATM 4979 O  O   . HOH   H 4 .   ? 8.914   69.288  13.455  1.00 19.73  ? 1466 HOH   A O   1 
HETATM 4980 O  O   . HOH   H 4 .   ? 20.497  47.697  29.253  1.00 47.24  ? 1467 HOH   A O   1 
HETATM 4981 O  O   . HOH   H 4 .   ? 26.848  56.952  2.809   1.00 32.94  ? 1468 HOH   A O   1 
HETATM 4982 O  O   . HOH   H 4 .   ? -30.416 63.496  -5.849  1.00 40.16  ? 1469 HOH   A O   1 
HETATM 4983 O  O   . HOH   H 4 .   ? -5.474  69.422  -2.033  1.00 46.45  ? 1470 HOH   A O   1 
HETATM 4984 O  O   . HOH   H 4 .   ? -50.031 66.082  -18.524 1.00 47.21  ? 1471 HOH   A O   1 
HETATM 4985 O  O   . HOH   H 4 .   ? 18.659  45.176  28.154  1.00 46.82  ? 1472 HOH   A O   1 
HETATM 4986 O  O   . HOH   H 4 .   ? 30.510  56.505  2.573   1.00 26.13  ? 1473 HOH   A O   1 
HETATM 4987 O  O   . HOH   H 4 .   ? 7.733   55.788  -14.569 1.00 30.64  ? 1474 HOH   A O   1 
HETATM 4988 O  O   . HOH   H 4 .   ? -11.342 68.740  -5.471  1.00 35.23  ? 1475 HOH   A O   1 
HETATM 4989 O  O   . HOH   H 4 .   ? 11.294  57.227  -4.560  1.00 24.27  ? 1476 HOH   A O   1 
HETATM 4990 O  O   . HOH   H 4 .   ? 25.715  37.079  8.364   1.00 34.40  ? 1477 HOH   A O   1 
HETATM 4991 O  O   . HOH   H 4 .   ? 28.835  53.288  4.099   1.00 33.25  ? 1478 HOH   A O   1 
HETATM 4992 O  O   . HOH   H 4 .   ? 3.091   56.703  23.558  1.00 19.03  ? 1479 HOH   A O   1 
HETATM 4993 O  O   . HOH   H 4 .   ? -8.863  68.403  -4.861  1.00 34.88  ? 1480 HOH   A O   1 
HETATM 4994 O  O   . HOH   H 4 .   ? -17.249 64.358  -4.458  0.50 20.30  ? 1481 HOH   A O   1 
HETATM 4995 O  O   . HOH   H 4 .   ? 24.875  42.876  23.822  1.00 43.39  ? 1482 HOH   A O   1 
HETATM 4996 O  O   . HOH   H 4 .   ? 7.453   56.235  32.215  1.00 33.48  ? 1483 HOH   A O   1 
HETATM 4997 O  O   . HOH   H 4 .   ? 16.542  45.434  18.967  1.00 22.98  ? 1484 HOH   A O   1 
HETATM 4998 O  O   . HOH   H 4 .   ? 24.016  70.285  25.389  1.00 37.87  ? 1485 HOH   A O   1 
HETATM 4999 O  O   . HOH   H 4 .   ? 7.635   46.510  1.989   1.00 40.54  ? 1486 HOH   A O   1 
HETATM 5000 O  O   . HOH   H 4 .   ? 31.791  56.288  19.521  1.00 41.39  ? 1487 HOH   A O   1 
HETATM 5001 O  O   A HOH   H 4 .   ? 23.979  39.837  6.743   0.50 15.97  ? 1488 HOH   A O   1 
HETATM 5002 O  O   B HOH   H 4 .   ? 25.142  40.139  7.812   0.50 18.32  ? 1488 HOH   A O   1 
HETATM 5003 O  O   . HOH   H 4 .   ? 32.201  60.994  18.163  1.00 51.30  ? 1489 HOH   A O   1 
HETATM 5004 O  O   . HOH   H 4 .   ? 31.260  59.620  20.302  1.00 44.09  ? 1490 HOH   A O   1 
HETATM 5005 O  O   . HOH   H 4 .   ? 26.891  70.501  16.589  1.00 38.84  ? 1491 HOH   A O   1 
HETATM 5006 O  O   . HOH   H 4 .   ? -1.182  67.809  9.759   1.00 32.83  ? 1492 HOH   A O   1 
HETATM 5007 O  O   . HOH   H 4 .   ? 14.331  68.995  19.428  1.00 31.73  ? 1493 HOH   A O   1 
HETATM 5008 O  O   . HOH   H 4 .   ? 4.441   40.413  26.990  1.00 38.61  ? 1494 HOH   A O   1 
HETATM 5009 O  O   . HOH   H 4 .   ? 17.280  48.203  6.621   1.00 34.22  ? 1495 HOH   A O   1 
HETATM 5010 O  O   . HOH   H 4 .   ? 28.773  60.342  12.850  1.00 27.46  ? 1496 HOH   A O   1 
HETATM 5011 O  O   . HOH   H 4 .   ? 9.565   51.160  1.350   1.00 42.37  ? 1497 HOH   A O   1 
HETATM 5012 O  O   . HOH   H 4 .   ? 14.697  48.550  5.697   1.00 32.33  ? 1498 HOH   A O   1 
HETATM 5013 O  O   . HOH   H 4 .   ? 12.390  40.382  7.742   1.00 33.63  ? 1499 HOH   A O   1 
HETATM 5014 O  O   . HOH   H 4 .   ? -14.063 49.998  23.983  1.00 30.07  ? 1500 HOH   A O   1 
HETATM 5015 O  O   . HOH   H 4 .   ? -10.451 62.545  15.487  1.00 32.56  ? 1501 HOH   A O   1 
HETATM 5016 O  O   . HOH   H 4 .   ? 20.362  57.131  29.615  1.00 41.43  ? 1502 HOH   A O   1 
HETATM 5017 O  O   . HOH   H 4 .   ? -13.824 61.161  2.570   1.00 21.85  ? 1503 HOH   A O   1 
HETATM 5018 O  O   . HOH   H 4 .   ? -8.914  58.189  -16.208 1.00 33.91  ? 1504 HOH   A O   1 
HETATM 5019 O  O   . HOH   H 4 .   ? 21.675  55.525  31.532  1.00 38.01  ? 1505 HOH   A O   1 
HETATM 5020 O  O   . HOH   H 4 .   ? -9.784  52.515  15.121  1.00 44.60  ? 1506 HOH   A O   1 
HETATM 5021 O  O   . HOH   H 4 .   ? 28.170  53.645  10.582  1.00 37.19  ? 1507 HOH   A O   1 
HETATM 5022 O  O   . HOH   H 4 .   ? -7.874  67.166  5.745   1.00 41.08  ? 1508 HOH   A O   1 
HETATM 5023 O  O   . HOH   H 4 .   ? -12.088 70.152  -16.930 1.00 48.39  ? 1509 HOH   A O   1 
HETATM 5024 O  O   . HOH   H 4 .   ? 13.859  41.124  31.728  1.00 35.04  ? 1510 HOH   A O   1 
HETATM 5025 O  O   . HOH   H 4 .   ? -32.806 69.833  -5.130  1.00 31.50  ? 1511 HOH   A O   1 
HETATM 5026 O  O   . HOH   H 4 .   ? 5.254   53.611  26.864  1.00 29.80  ? 1512 HOH   A O   1 
HETATM 5027 O  O   . HOH   H 4 .   ? 25.766  58.861  30.148  1.00 23.76  ? 1513 HOH   A O   1 
HETATM 5028 O  O   . HOH   H 4 .   ? -9.783  47.432  -5.292  1.00 39.97  ? 1514 HOH   A O   1 
HETATM 5029 O  O   . HOH   H 4 .   ? 14.495  49.225  2.908   1.00 34.63  ? 1515 HOH   A O   1 
HETATM 5030 O  O   . HOH   H 4 .   ? 24.973  37.488  5.967   1.00 41.14  ? 1516 HOH   A O   1 
HETATM 5031 O  O   . HOH   H 4 .   ? -11.584 72.573  -18.561 1.00 39.13  ? 1517 HOH   A O   1 
HETATM 5032 O  O   . HOH   I 4 .   ? 29.854  9.047   20.150  1.00 33.74  ? 1301 HOH   B O   1 
HETATM 5033 O  O   . HOH   I 4 .   ? -2.225  -7.546  10.130  1.00 25.74  ? 1302 HOH   B O   1 
HETATM 5034 O  O   . HOH   I 4 .   ? 35.034  3.613   11.996  1.00 26.04  ? 1303 HOH   B O   1 
HETATM 5035 O  O   . HOH   I 4 .   ? 8.733   4.241   -1.272  1.00 19.24  ? 1304 HOH   B O   1 
HETATM 5036 O  O   . HOH   I 4 .   ? 13.490  -2.758  -11.347 1.00 36.22  ? 1305 HOH   B O   1 
HETATM 5037 O  O   . HOH   I 4 .   ? 28.420  -6.350  0.239   1.00 28.72  ? 1306 HOH   B O   1 
HETATM 5038 O  O   . HOH   I 4 .   ? 24.629  -12.093 -12.279 1.00 28.91  ? 1307 HOH   B O   1 
HETATM 5039 O  O   . HOH   I 4 .   ? 26.778  -4.233  16.451  1.00 34.25  ? 1308 HOH   B O   1 
HETATM 5040 O  O   . HOH   I 4 .   ? 22.621  7.589   -6.431  1.00 19.37  ? 1309 HOH   B O   1 
HETATM 5041 O  O   . HOH   I 4 .   ? 18.204  11.891  3.879   1.00 33.38  ? 1310 HOH   B O   1 
HETATM 5042 O  O   . HOH   I 4 .   ? -6.931  0.091   16.090  1.00 40.16  ? 1311 HOH   B O   1 
HETATM 5043 O  O   . HOH   I 4 .   ? 8.797   -8.095  20.718  1.00 42.00  ? 1312 HOH   B O   1 
HETATM 5044 O  O   . HOH   I 4 .   ? 10.393  8.654   -2.314  1.00 34.43  ? 1313 HOH   B O   1 
HETATM 5045 O  O   . HOH   I 4 .   ? 16.020  2.193   25.742  1.00 15.16  ? 1314 HOH   B O   1 
HETATM 5046 O  O   . HOH   I 4 .   ? 12.699  20.149  26.419  1.00 23.36  ? 1315 HOH   B O   1 
HETATM 5047 O  O   . HOH   I 4 .   ? 2.308   11.031  7.741   1.00 28.87  ? 1316 HOH   B O   1 
HETATM 5048 O  O   . HOH   I 4 .   ? 17.717  -2.350  20.331  1.00 31.25  ? 1317 HOH   B O   1 
HETATM 5049 O  O   . HOH   I 4 .   ? 37.262  -2.293  1.997   1.00 19.73  ? 1318 HOH   B O   1 
HETATM 5050 O  O   . HOH   I 4 .   ? 24.400  5.710   24.511  1.00 44.77  ? 1319 HOH   B O   1 
HETATM 5051 O  O   . HOH   I 4 .   ? 33.117  10.249  22.131  1.00 41.12  ? 1320 HOH   B O   1 
HETATM 5052 O  O   . HOH   I 4 .   ? 29.705  4.190   18.416  1.00 36.07  ? 1321 HOH   B O   1 
HETATM 5053 O  O   . HOH   I 4 .   ? 28.132  10.905  -4.565  1.00 23.97  ? 1322 HOH   B O   1 
HETATM 5054 O  O   . HOH   I 4 .   ? 26.501  -3.010  8.326   1.00 23.09  ? 1323 HOH   B O   1 
HETATM 5055 O  O   . HOH   I 4 .   ? 18.137  5.736   20.680  1.00 23.97  ? 1324 HOH   B O   1 
HETATM 5056 O  O   . HOH   I 4 .   ? 21.829  -13.657 -11.190 1.00 34.55  ? 1325 HOH   B O   1 
HETATM 5057 O  O   . HOH   I 4 .   ? 7.394   19.889  16.769  1.00 25.78  ? 1326 HOH   B O   1 
HETATM 5058 O  O   . HOH   I 4 .   ? 24.992  -8.141  -8.429  1.00 36.73  ? 1327 HOH   B O   1 
HETATM 5059 O  O   . HOH   I 4 .   ? 19.140  -5.476  -2.652  1.00 18.57  ? 1328 HOH   B O   1 
HETATM 5060 O  O   . HOH   I 4 .   ? 27.522  -16.866 -13.210 1.00 16.62  ? 1329 HOH   B O   1 
HETATM 5061 O  O   . HOH   I 4 .   ? 2.187   -9.254  2.142   1.00 39.55  ? 1330 HOH   B O   1 
HETATM 5062 O  O   . HOH   I 4 .   ? 9.124   -1.722  -5.992  1.00 40.97  ? 1331 HOH   B O   1 
HETATM 5063 O  O   . HOH   I 4 .   ? 13.146  -6.965  15.439  1.00 23.30  ? 1332 HOH   B O   1 
HETATM 5064 O  O   . HOH   I 4 .   ? 6.230   17.272  16.785  1.00 28.11  ? 1333 HOH   B O   1 
HETATM 5065 O  O   . HOH   I 4 .   ? 32.427  -9.030  -15.015 1.00 33.33  ? 1334 HOH   B O   1 
HETATM 5066 O  O   . HOH   I 4 .   ? 27.567  3.878   -12.370 1.00 44.93  ? 1335 HOH   B O   1 
HETATM 5067 O  O   . HOH   I 4 .   ? -7.128  8.319   24.636  1.00 38.85  ? 1336 HOH   B O   1 
HETATM 5068 O  O   . HOH   I 4 .   ? 21.627  6.246   4.870   1.00 15.19  ? 1337 HOH   B O   1 
HETATM 5069 O  O   . HOH   I 4 .   ? 28.316  2.224   -15.460 1.00 43.57  ? 1338 HOH   B O   1 
HETATM 5070 O  O   . HOH   I 4 .   ? 16.336  -7.186  2.145   1.00 31.36  ? 1339 HOH   B O   1 
HETATM 5071 O  O   . HOH   I 4 .   ? 1.058   5.135   -1.322  1.00 29.58  ? 1340 HOH   B O   1 
HETATM 5072 O  O   . HOH   I 4 .   ? 32.796  -6.376  -8.630  1.00 39.09  ? 1341 HOH   B O   1 
HETATM 5073 O  O   . HOH   I 4 .   ? 32.347  -3.121  10.964  1.00 42.09  ? 1342 HOH   B O   1 
HETATM 5074 O  O   . HOH   I 4 .   ? 33.243  -1.691  3.207   1.00 20.44  ? 1343 HOH   B O   1 
HETATM 5075 O  O   . HOH   I 4 .   ? -10.095 -3.007  5.458   1.00 17.71  ? 1344 HOH   B O   1 
HETATM 5076 O  O   . HOH   I 4 .   ? 29.891  -7.986  -3.946  1.00 43.03  ? 1345 HOH   B O   1 
HETATM 5077 O  O   A HOH   I 4 .   ? 8.376   8.078   1.156   0.50 21.23  ? 1346 HOH   B O   1 
HETATM 5078 O  O   B HOH   I 4 .   ? 8.529   7.141   -1.107  0.50 29.33  ? 1346 HOH   B O   1 
HETATM 5079 O  O   . HOH   I 4 .   ? -4.851  16.900  20.844  1.00 38.84  ? 1347 HOH   B O   1 
HETATM 5080 O  O   . HOH   I 4 .   ? 21.940  -6.614  15.921  1.00 37.17  ? 1348 HOH   B O   1 
HETATM 5081 O  O   . HOH   I 4 .   ? 7.439   32.816  14.971  1.00 30.12  ? 1349 HOH   B O   1 
HETATM 5082 O  O   . HOH   I 4 .   ? 15.003  -6.641  0.013   1.00 33.26  ? 1350 HOH   B O   1 
HETATM 5083 O  O   . HOH   I 4 .   ? 21.137  3.599   -16.758 1.00 30.45  ? 1351 HOH   B O   1 
HETATM 5084 O  O   . HOH   I 4 .   ? 10.639  -4.580  0.421   1.00 14.92  ? 1352 HOH   B O   1 
HETATM 5085 O  O   . HOH   I 4 .   ? 27.285  -4.173  -16.591 1.00 30.74  ? 1353 HOH   B O   1 
HETATM 5086 O  O   . HOH   I 4 .   ? 33.974  13.233  6.478   1.00 28.23  ? 1354 HOH   B O   1 
HETATM 5087 O  O   . HOH   I 4 .   ? 19.780  -7.815  1.447   1.00 23.97  ? 1355 HOH   B O   1 
HETATM 5088 O  O   . HOH   I 4 .   ? 1.540   -1.785  28.167  1.00 28.51  ? 1356 HOH   B O   1 
HETATM 5089 O  O   . HOH   I 4 .   ? 25.079  10.821  9.033   1.00 19.91  ? 1357 HOH   B O   1 
HETATM 5090 O  O   . HOH   I 4 .   ? 29.188  14.954  17.149  1.00 31.92  ? 1358 HOH   B O   1 
HETATM 5091 O  O   . HOH   I 4 .   ? 10.635  -10.209 7.022   1.00 28.82  ? 1359 HOH   B O   1 
HETATM 5092 O  O   . HOH   I 4 .   ? -3.035  -4.473  0.033   1.00 42.50  ? 1360 HOH   B O   1 
HETATM 5093 O  O   . HOH   I 4 .   ? 16.715  -8.079  8.657   1.00 41.07  ? 1361 HOH   B O   1 
HETATM 5094 O  O   . HOH   I 4 .   ? 1.762   13.703  3.818   1.00 41.06  ? 1362 HOH   B O   1 
HETATM 5095 O  O   . HOH   I 4 .   ? -6.319  5.572   12.322  1.00 28.63  ? 1363 HOH   B O   1 
HETATM 5096 O  O   . HOH   I 4 .   ? 25.138  -6.315  15.792  1.00 43.57  ? 1364 HOH   B O   1 
HETATM 5097 O  O   . HOH   I 4 .   ? 3.423   -6.919  1.742   1.00 25.25  ? 1365 HOH   B O   1 
HETATM 5098 O  O   . HOH   I 4 .   ? 19.323  10.609  9.873   1.00 13.25  ? 1366 HOH   B O   1 
HETATM 5099 O  O   . HOH   I 4 .   ? 10.944  -7.373  17.103  1.00 26.76  ? 1367 HOH   B O   1 
HETATM 5100 O  O   . HOH   I 4 .   ? 27.912  14.269  9.513   1.00 30.27  ? 1368 HOH   B O   1 
HETATM 5101 O  O   . HOH   I 4 .   ? 15.228  -9.617  1.579   1.00 49.87  ? 1369 HOH   B O   1 
HETATM 5102 O  O   . HOH   I 4 .   ? 16.377  -6.657  -3.035  1.00 36.46  ? 1370 HOH   B O   1 
HETATM 5103 O  O   . HOH   I 4 .   ? 33.351  6.957   4.404   1.00 21.02  ? 1371 HOH   B O   1 
HETATM 5104 O  O   . HOH   I 4 .   ? 12.103  -6.952  0.755   1.00 29.34  ? 1372 HOH   B O   1 
HETATM 5105 O  O   . HOH   I 4 .   ? 2.169   16.016  19.504  1.00 26.41  ? 1373 HOH   B O   1 
HETATM 5106 O  O   . HOH   I 4 .   ? 35.128  12.314  -7.646  1.00 39.54  ? 1374 HOH   B O   1 
HETATM 5107 O  O   . HOH   I 4 .   ? 33.171  2.014   3.223   1.00 20.15  ? 1375 HOH   B O   1 
HETATM 5108 O  O   . HOH   I 4 .   ? -0.035  -8.598  9.002   1.00 40.52  ? 1376 HOH   B O   1 
HETATM 5109 O  O   . HOH   I 4 .   ? 25.672  -9.515  -13.395 1.00 20.22  ? 1377 HOH   B O   1 
HETATM 5110 O  O   . HOH   I 4 .   ? 9.387   31.290  13.589  1.00 25.98  ? 1378 HOH   B O   1 
HETATM 5111 O  O   . HOH   I 4 .   ? -0.332  11.097  11.513  1.00 24.29  ? 1379 HOH   B O   1 
HETATM 5112 O  O   . HOH   I 4 .   ? 6.203   12.965  5.338   1.00 32.53  ? 1380 HOH   B O   1 
HETATM 5113 O  O   . HOH   I 4 .   ? 19.072  7.987   19.336  1.00 22.12  ? 1381 HOH   B O   1 
HETATM 5114 O  O   . HOH   I 4 .   ? 8.868   29.471  9.748   1.00 35.59  ? 1382 HOH   B O   1 
HETATM 5115 O  O   . HOH   I 4 .   ? 21.239  11.552  25.221  1.00 26.72  ? 1383 HOH   B O   1 
HETATM 5116 O  O   . HOH   I 4 .   ? 23.834  -14.925 -19.635 1.00 32.73  ? 1384 HOH   B O   1 
HETATM 5117 O  O   . HOH   I 4 .   ? 10.734  8.503   1.613   1.00 26.96  ? 1385 HOH   B O   1 
HETATM 5118 O  O   . HOH   I 4 .   ? 23.322  8.750   -10.808 1.00 35.23  ? 1386 HOH   B O   1 
HETATM 5119 O  O   . HOH   I 4 .   ? -5.413  0.243   1.805   1.00 27.46  ? 1387 HOH   B O   1 
HETATM 5120 O  O   . HOH   I 4 .   ? 6.969   10.655  7.069   1.00 16.86  ? 1388 HOH   B O   1 
HETATM 5121 O  O   . HOH   I 4 .   ? 34.368  1.593   -6.396  1.00 28.26  ? 1389 HOH   B O   1 
HETATM 5122 O  O   . HOH   I 4 .   ? 14.118  15.948  6.927   1.00 38.84  ? 1390 HOH   B O   1 
HETATM 5123 O  O   . HOH   I 4 .   ? 25.892  -7.790  0.623   1.00 39.10  ? 1391 HOH   B O   1 
HETATM 5124 O  O   . HOH   I 4 .   ? 23.687  -1.710  7.916   1.00 16.19  ? 1392 HOH   B O   1 
HETATM 5125 O  O   . HOH   I 4 .   ? 26.818  12.701  8.116   1.00 25.68  ? 1393 HOH   B O   1 
HETATM 5126 O  O   . HOH   I 4 .   ? 19.383  5.812   2.590   1.00 17.14  ? 1394 HOH   B O   1 
HETATM 5127 O  O   . HOH   I 4 .   ? 24.894  12.872  5.211   1.00 33.01  ? 1395 HOH   B O   1 
HETATM 5128 O  O   . HOH   I 4 .   ? 5.748   -8.534  12.649  1.00 16.72  ? 1396 HOH   B O   1 
HETATM 5129 O  O   . HOH   I 4 .   ? 35.285  -5.086  -6.837  1.00 39.00  ? 1397 HOH   B O   1 
HETATM 5130 O  O   . HOH   I 4 .   ? 29.603  2.606   21.026  1.00 45.01  ? 1398 HOH   B O   1 
HETATM 5131 O  O   . HOH   I 4 .   ? 28.723  12.391  13.754  1.00 31.01  ? 1399 HOH   B O   1 
HETATM 5132 O  O   . HOH   I 4 .   ? -3.677  5.968   4.329   1.00 28.30  ? 1400 HOH   B O   1 
HETATM 5133 O  O   . HOH   I 4 .   ? 33.149  -6.690  -5.715  1.00 40.07  ? 1401 HOH   B O   1 
HETATM 5134 O  O   . HOH   I 4 .   ? 17.500  10.560  7.629   1.00 16.42  ? 1402 HOH   B O   1 
HETATM 5135 O  O   . HOH   I 4 .   ? 13.135  15.774  17.879  1.00 26.17  ? 1403 HOH   B O   1 
HETATM 5136 O  O   . HOH   I 4 .   ? 23.946  -9.790  6.491   1.00 46.00  ? 1404 HOH   B O   1 
HETATM 5137 O  O   . HOH   I 4 .   ? 19.221  -7.498  15.074  1.00 23.39  ? 1405 HOH   B O   1 
HETATM 5138 O  O   . HOH   I 4 .   ? -6.833  -2.848  9.253   1.00 22.44  ? 1406 HOH   B O   1 
HETATM 5139 O  O   . HOH   I 4 .   ? 21.248  12.705  3.086   1.00 38.75  ? 1407 HOH   B O   1 
HETATM 5140 O  O   . HOH   I 4 .   ? 0.686   -9.610  12.730  1.00 28.10  ? 1408 HOH   B O   1 
HETATM 5141 O  O   . HOH   I 4 .   ? 12.172  12.501  -2.307  1.00 35.16  ? 1409 HOH   B O   1 
HETATM 5142 O  O   . HOH   I 4 .   ? -5.157  3.838   15.033  1.00 27.22  ? 1410 HOH   B O   1 
HETATM 5143 O  O   . HOH   I 4 .   ? 12.075  -10.782 4.367   1.00 40.92  ? 1411 HOH   B O   1 
HETATM 5144 O  O   . HOH   I 4 .   ? 34.693  -1.138  -0.383  1.00 27.34  ? 1412 HOH   B O   1 
HETATM 5145 O  O   . HOH   I 4 .   ? 24.470  -4.214  -17.541 1.00 43.34  ? 1413 HOH   B O   1 
HETATM 5146 O  O   . HOH   I 4 .   ? -9.084  4.908   2.734   1.00 23.41  ? 1414 HOH   B O   1 
HETATM 5147 O  O   . HOH   I 4 .   ? 21.916  -3.698  9.520   1.00 18.19  ? 1415 HOH   B O   1 
HETATM 5148 O  O   . HOH   I 4 .   ? -5.076  1.316   14.653  1.00 25.38  ? 1416 HOH   B O   1 
HETATM 5149 O  O   . HOH   I 4 .   ? 14.541  11.216  3.528   1.00 34.31  ? 1417 HOH   B O   1 
HETATM 5150 O  O   . HOH   I 4 .   ? 17.521  -4.923  19.499  1.00 33.71  ? 1418 HOH   B O   1 
HETATM 5151 O  O   . HOH   I 4 .   ? 14.300  12.442  14.701  1.00 20.41  ? 1419 HOH   B O   1 
HETATM 5152 O  O   . HOH   I 4 .   ? -9.380  2.868   24.366  1.00 31.48  ? 1420 HOH   B O   1 
HETATM 5153 O  O   . HOH   I 4 .   ? 4.857   -4.434  -1.550  1.00 36.45  ? 1421 HOH   B O   1 
HETATM 5154 O  O   . HOH   I 4 .   ? -0.056  10.646  8.648   1.00 28.26  ? 1422 HOH   B O   1 
HETATM 5155 O  O   . HOH   I 4 .   ? 31.245  8.603   10.725  1.00 24.33  ? 1423 HOH   B O   1 
HETATM 5156 O  O   . HOH   I 4 .   ? 18.087  4.726   23.220  1.00 23.88  ? 1424 HOH   B O   1 
HETATM 5157 O  O   . HOH   I 4 .   ? 2.770   4.580   -5.079  1.00 38.10  ? 1425 HOH   B O   1 
HETATM 5158 O  O   . HOH   I 4 .   ? 28.322  19.068  8.770   1.00 47.63  ? 1426 HOH   B O   1 
HETATM 5159 O  O   . HOH   I 4 .   ? 28.121  15.880  21.307  1.00 44.77  ? 1427 HOH   B O   1 
HETATM 5160 O  O   . HOH   I 4 .   ? -3.793  -10.280 13.737  1.00 32.63  ? 1428 HOH   B O   1 
HETATM 5161 O  O   . HOH   I 4 .   ? 19.203  -5.646  8.466   1.00 19.16  ? 1429 HOH   B O   1 
HETATM 5162 O  O   . HOH   I 4 .   ? 18.033  -8.203  -6.714  1.00 24.89  ? 1430 HOH   B O   1 
HETATM 5163 O  O   . HOH   I 4 .   ? 10.926  3.099   -2.684  1.00 15.99  ? 1431 HOH   B O   1 
HETATM 5164 O  O   . HOH   I 4 .   ? -1.718  -9.117  12.695  1.00 28.70  ? 1432 HOH   B O   1 
HETATM 5165 O  O   . HOH   I 4 .   ? 22.106  18.302  28.836  1.00 35.52  ? 1433 HOH   B O   1 
HETATM 5166 O  O   . HOH   I 4 .   ? 27.782  12.130  11.419  1.00 31.59  ? 1434 HOH   B O   1 
HETATM 5167 O  O   . HOH   I 4 .   ? 24.083  3.912   -15.022 1.00 28.90  ? 1435 HOH   B O   1 
HETATM 5168 O  O   . HOH   I 4 .   ? 16.530  -8.871  6.000   1.00 36.11  ? 1436 HOH   B O   1 
HETATM 5169 O  O   . HOH   I 4 .   ? -5.790  -7.280  1.926   1.00 27.20  ? 1437 HOH   B O   1 
HETATM 5170 O  O   . HOH   I 4 .   ? 8.965   14.203  8.422   1.00 41.21  ? 1438 HOH   B O   1 
HETATM 5171 O  O   . HOH   I 4 .   ? 5.308   -9.636  2.891   1.00 41.02  ? 1439 HOH   B O   1 
HETATM 5172 O  O   . HOH   I 4 .   ? -7.197  -1.261  11.577  1.00 29.03  ? 1440 HOH   B O   1 
HETATM 5173 O  O   . HOH   I 4 .   ? 26.736  -7.481  -1.865  1.00 43.76  ? 1441 HOH   B O   1 
HETATM 5174 O  O   . HOH   I 4 .   ? 28.556  3.016   13.411  1.00 30.27  ? 1442 HOH   B O   1 
HETATM 5175 O  O   . HOH   I 4 .   ? 26.108  -4.907  6.511   1.00 29.53  ? 1443 HOH   B O   1 
HETATM 5176 O  O   . HOH   I 4 .   ? 16.018  4.891   25.107  1.00 18.92  ? 1444 HOH   B O   1 
HETATM 5177 O  O   . HOH   I 4 .   ? -4.104  -4.869  2.233   1.00 31.43  ? 1445 HOH   B O   1 
HETATM 5178 O  O   . HOH   I 4 .   ? 1.174   -13.661 7.511   1.00 36.25  ? 1446 HOH   B O   1 
HETATM 5179 O  O   . HOH   I 4 .   ? 13.711  8.019   -12.189 1.00 27.95  ? 1447 HOH   B O   1 
HETATM 5180 O  O   . HOH   I 4 .   ? 37.605  -5.510  -5.389  1.00 35.86  ? 1448 HOH   B O   1 
HETATM 5181 O  O   . HOH   I 4 .   ? 4.476   0.106   -1.441  1.00 36.53  ? 1449 HOH   B O   1 
HETATM 5182 O  O   . HOH   I 4 .   ? 11.766  13.692  10.397  1.00 37.85  ? 1450 HOH   B O   1 
HETATM 5183 O  O   . HOH   I 4 .   ? 5.269   17.138  29.909  1.00 26.62  ? 1451 HOH   B O   1 
HETATM 5184 O  O   . HOH   I 4 .   ? -6.751  13.019  21.934  1.00 29.00  ? 1452 HOH   B O   1 
HETATM 5185 O  O   . HOH   I 4 .   ? 30.374  -3.605  6.858   1.00 24.15  ? 1453 HOH   B O   1 
HETATM 5186 O  O   . HOH   I 4 .   ? -6.205  6.957   9.019   1.00 33.04  ? 1454 HOH   B O   1 
HETATM 5187 O  O   . HOH   I 4 .   ? 2.867   -2.543  -1.391  1.00 26.00  ? 1455 HOH   B O   1 
HETATM 5188 O  O   . HOH   I 4 .   ? 29.479  7.209   18.369  1.00 40.17  ? 1456 HOH   B O   1 
HETATM 5189 O  O   . HOH   I 4 .   ? 20.214  -11.529 -8.619  1.00 39.92  ? 1457 HOH   B O   1 
HETATM 5190 O  O   . HOH   I 4 .   ? 14.647  9.922   29.094  1.00 26.77  ? 1458 HOH   B O   1 
HETATM 5191 O  O   . HOH   I 4 .   ? 15.530  -7.029  -5.653  1.00 24.20  ? 1459 HOH   B O   1 
HETATM 5192 O  O   . HOH   I 4 .   ? -7.026  -2.974  13.557  1.00 28.30  ? 1460 HOH   B O   1 
HETATM 5193 O  O   . HOH   I 4 .   ? 23.110  -7.372  1.718   1.00 41.10  ? 1461 HOH   B O   1 
HETATM 5194 O  O   . HOH   I 4 .   ? 31.548  7.376   -7.015  1.00 40.43  ? 1462 HOH   B O   1 
HETATM 5195 O  O   . HOH   I 4 .   ? -2.432  -10.050 6.795   1.00 44.08  ? 1463 HOH   B O   1 
HETATM 5196 O  O   . HOH   I 4 .   ? 10.365  5.250   -4.550  1.00 30.26  ? 1464 HOH   B O   1 
HETATM 5197 O  O   . HOH   I 4 .   ? 24.555  6.225   -9.322  1.00 37.00  ? 1465 HOH   B O   1 
HETATM 5198 O  O   . HOH   I 4 .   ? -5.250  -6.079  15.647  1.00 23.77  ? 1466 HOH   B O   1 
HETATM 5199 O  O   . HOH   I 4 .   ? 6.510   -6.771  28.252  1.00 27.39  ? 1467 HOH   B O   1 
HETATM 5200 O  O   . HOH   I 4 .   ? 12.286  -7.583  12.967  1.00 20.82  ? 1468 HOH   B O   1 
HETATM 5201 O  O   . HOH   I 4 .   ? 22.092  -9.423  3.118   1.00 46.44  ? 1469 HOH   B O   1 
HETATM 5202 O  O   . HOH   I 4 .   ? 38.932  0.320   -8.107  1.00 39.67  ? 1470 HOH   B O   1 
HETATM 5203 O  O   . HOH   I 4 .   ? -5.687  -7.451  9.164   1.00 38.89  ? 1471 HOH   B O   1 
HETATM 5204 O  O   . HOH   I 4 .   ? 17.633  14.152  -9.245  1.00 32.40  ? 1472 HOH   B O   1 
HETATM 5205 O  O   . HOH   I 4 .   ? -3.838  18.928  22.739  1.00 35.94  ? 1473 HOH   B O   1 
HETATM 5206 O  O   . HOH   I 4 .   ? 14.535  -4.862  23.048  1.00 29.80  ? 1474 HOH   B O   1 
HETATM 5207 O  O   . HOH   I 4 .   ? 30.965  6.297   11.966  1.00 41.64  ? 1475 HOH   B O   1 
HETATM 5208 O  O   . HOH   I 4 .   ? 34.583  2.531   -9.439  1.00 24.80  ? 1476 HOH   B O   1 
HETATM 5209 O  O   . HOH   I 4 .   ? 10.141  -9.331  12.228  1.00 24.72  ? 1477 HOH   B O   1 
HETATM 5210 O  O   . HOH   I 4 .   ? 20.041  5.979   -16.107 1.00 24.95  ? 1478 HOH   B O   1 
HETATM 5211 O  O   . HOH   I 4 .   ? 14.780  -8.604  19.636  1.00 37.36  ? 1479 HOH   B O   1 
HETATM 5212 O  O   . HOH   I 4 .   ? 30.659  -5.984  -5.178  1.00 44.48  ? 1480 HOH   B O   1 
HETATM 5213 O  O   . HOH   I 4 .   ? -10.382 5.150   19.085  1.00 33.81  ? 1481 HOH   B O   1 
HETATM 5214 O  O   . HOH   I 4 .   ? 11.145  0.664   -3.352  1.00 29.31  ? 1482 HOH   B O   1 
HETATM 5215 O  O   . HOH   I 4 .   ? 18.507  11.471  26.378  1.00 25.76  ? 1483 HOH   B O   1 
HETATM 5216 O  O   . HOH   I 4 .   ? 18.570  11.072  0.928   1.00 34.58  ? 1484 HOH   B O   1 
HETATM 5217 O  O   . HOH   I 4 .   ? 4.796   15.912  18.762  1.00 19.52  ? 1485 HOH   B O   1 
HETATM 5218 O  O   . HOH   I 4 .   ? -6.025  6.362   6.641   1.00 30.88  ? 1486 HOH   B O   1 
HETATM 5219 O  O   . HOH   I 4 .   ? 34.691  0.806   -12.795 1.00 24.72  ? 1487 HOH   B O   1 
HETATM 5220 O  O   . HOH   I 4 .   ? 20.666  -7.414  -1.114  1.00 34.79  ? 1488 HOH   B O   1 
HETATM 5221 O  O   . HOH   I 4 .   ? 4.469   -14.315 9.935   1.00 40.53  ? 1489 HOH   B O   1 
HETATM 5222 O  O   . HOH   I 4 .   ? 30.634  12.342  -4.013  1.00 38.12  ? 1490 HOH   B O   1 
HETATM 5223 O  O   . HOH   I 4 .   ? -6.516  10.779  11.648  1.00 42.45  ? 1491 HOH   B O   1 
HETATM 5224 O  O   . HOH   I 4 .   ? 42.588  -10.247 -5.793  1.00 40.33  ? 1492 HOH   B O   1 
HETATM 5225 O  O   . HOH   I 4 .   ? 33.716  12.749  22.466  1.00 39.87  ? 1493 HOH   B O   1 
HETATM 5226 O  O   . HOH   I 4 .   ? 34.028  9.828   7.406   1.00 24.74  ? 1494 HOH   B O   1 
HETATM 5227 O  O   . HOH   I 4 .   ? 7.878   -7.165  16.383  1.00 29.08  ? 1495 HOH   B O   1 
HETATM 5228 O  O   . HOH   I 4 .   ? 25.329  4.682   -11.158 1.00 43.86  ? 1496 HOH   B O   1 
HETATM 5229 O  O   . HOH   I 4 .   ? 37.279  -0.522  -0.749  1.00 42.19  ? 1497 HOH   B O   1 
HETATM 5230 O  O   . HOH   I 4 .   ? 31.240  -14.799 -15.326 1.00 39.56  ? 1498 HOH   B O   1 
HETATM 5231 O  O   . HOH   I 4 .   ? 8.074   19.095  8.969   1.00 24.74  ? 1499 HOH   B O   1 
HETATM 5232 O  O   . HOH   I 4 .   ? 10.758  30.545  19.779  1.00 40.72  ? 1500 HOH   B O   1 
HETATM 5233 O  O   . HOH   I 4 .   ? -5.539  -2.323  25.186  1.00 43.23  ? 1501 HOH   B O   1 
HETATM 5234 O  O   . HOH   I 4 .   ? 3.930   13.175  6.542   1.00 38.11  ? 1502 HOH   B O   1 
HETATM 5235 O  O   . HOH   I 4 .   ? 16.654  10.696  30.435  1.00 39.92  ? 1503 HOH   B O   1 
HETATM 5236 O  O   . HOH   I 4 .   ? 22.499  -6.339  9.499   1.00 30.04  ? 1504 HOH   B O   1 
HETATM 5237 O  O   . HOH   I 4 .   ? 8.098   6.917   30.904  1.00 21.33  ? 1505 HOH   B O   1 
HETATM 5238 O  O   . HOH   I 4 .   ? -5.366  18.430  18.633  1.00 33.69  ? 1506 HOH   B O   1 
HETATM 5239 O  O   . HOH   I 4 .   ? 19.253  -8.891  9.203   1.00 34.10  ? 1507 HOH   B O   1 
HETATM 5240 O  O   . HOH   I 4 .   ? 20.431  -5.136  19.470  1.00 31.96  ? 1508 HOH   B O   1 
HETATM 5241 O  O   . HOH   I 4 .   ? 12.095  10.818  1.381   1.00 35.54  ? 1509 HOH   B O   1 
HETATM 5242 O  O   . HOH   I 4 .   ? -7.077  1.278   12.748  1.00 34.51  ? 1510 HOH   B O   1 
HETATM 5243 O  O   . HOH   I 4 .   ? 19.694  4.693   25.135  1.00 36.63  ? 1511 HOH   B O   1 
HETATM 5244 O  O   . HOH   I 4 .   ? 35.150  0.339   2.596   1.00 28.39  ? 1512 HOH   B O   1 
HETATM 5245 O  O   . HOH   I 4 .   ? 29.019  -5.578  5.224   1.00 39.68  ? 1513 HOH   B O   1 
HETATM 5246 O  O   . HOH   I 4 .   ? 32.237  -1.617  15.427  1.00 39.19  ? 1514 HOH   B O   1 
HETATM 5247 O  O   . HOH   I 4 .   ? 31.608  12.174  13.945  1.00 33.07  ? 1515 HOH   B O   1 
HETATM 5248 O  O   . HOH   I 4 .   ? -4.897  -9.716  4.953   1.00 51.80  ? 1516 HOH   B O   1 
HETATM 5249 O  O   . HOH   I 4 .   ? 8.310   21.278  7.433   1.00 35.56  ? 1517 HOH   B O   1 
HETATM 5250 O  O   . HOH   I 4 .   ? -8.212  -2.112  15.860  1.00 27.67  ? 1518 HOH   B O   1 
HETATM 5251 O  O   . HOH   I 4 .   ? 18.343  8.832   27.029  1.00 28.34  ? 1519 HOH   B O   1 
HETATM 5252 O  O   . HOH   I 4 .   ? 6.973   -7.471  18.907  1.00 29.52  ? 1520 HOH   B O   1 
HETATM 5253 O  O   . HOH   I 4 .   ? 43.824  -9.159  -7.904  1.00 56.18  ? 1521 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   . GLY A 1   ? 0.4886 3.1477 0.9651 -0.0860 -0.2732 0.6489  853  GLY A N   
2    C CA  . GLY A 1   ? 0.4835 3.0440 0.9173 -0.0113 -0.2460 0.6182  853  GLY A CA  
3    C C   . GLY A 1   ? 0.4818 2.8653 0.8820 -0.0299 -0.2465 0.5683  853  GLY A C   
4    O O   . GLY A 1   ? 0.4966 2.8293 0.9005 -0.0975 -0.2703 0.5528  853  GLY A O   
5    N N   . ASP A 2   ? 0.4647 2.7554 0.8307 0.0309  -0.2214 0.5441  854  ASP A N   
6    C CA  . ASP A 2   ? 0.4583 2.5861 0.7910 0.0222  -0.2180 0.4985  854  ASP A CA  
7    C C   . ASP A 2   ? 0.4330 2.4989 0.7779 -0.0272 -0.2246 0.4857  854  ASP A C   
8    O O   . ASP A 2   ? 0.4247 2.5628 0.8001 -0.0410 -0.2250 0.5118  854  ASP A O   
9    C CB  . ASP A 2   ? 0.4649 2.5158 0.7622 0.0964  -0.1896 0.4818  854  ASP A CB  
10   C CG  . ASP A 2   ? 0.4847 2.5693 0.7616 0.1494  -0.1830 0.4903  854  ASP A CG  
11   O OD1 . ASP A 2   ? 0.4850 2.6544 0.7753 0.1302  -0.1991 0.5081  854  ASP A OD1 
12   O OD2 . ASP A 2   ? 0.5069 2.5301 0.7526 0.2104  -0.1626 0.4798  854  ASP A OD2 
13   N N   . ILE A 3   ? 0.4176 2.3519 0.7375 -0.0510 -0.2294 0.4465  855  ILE A N   
14   C CA  . ILE A 3   ? 0.4099 2.2656 0.7348 -0.0935 -0.2354 0.4291  855  ILE A CA  
15   C C   . ILE A 3   ? 0.3823 2.2167 0.7065 -0.0503 -0.2092 0.4316  855  ILE A C   
16   O O   . ILE A 3   ? 0.3699 2.1546 0.6665 0.0072  -0.1872 0.4180  855  ILE A O   
17   C CB  . ILE A 3   ? 0.4205 2.1369 0.7124 -0.1134 -0.2416 0.3840  855  ILE A CB  
18   C CG1 . ILE A 3   ? 0.4455 2.1737 0.7318 -0.1548 -0.2684 0.3764  855  ILE A CG1 
19   C CG2 . ILE A 3   ? 0.4236 2.0566 0.7187 -0.1510 -0.2466 0.3661  855  ILE A CG2 
20   C CD1 . ILE A 3   ? 0.4548 2.0658 0.7025 -0.1532 -0.2688 0.3344  855  ILE A CD1 
21   N N   . VAL A 4   ? 0.3704 2.2417 0.7231 -0.0791 -0.2130 0.4495  856  VAL A N   
22   C CA  . VAL A 4   ? 0.3494 2.1990 0.7009 -0.0429 -0.1899 0.4503  856  VAL A CA  
23   C C   . VAL A 4   ? 0.3535 2.0612 0.6849 -0.0624 -0.1886 0.4130  856  VAL A C   
24   O O   . VAL A 4   ? 0.3682 2.0243 0.7018 -0.1188 -0.2098 0.3983  856  VAL A O   
25   C CB  . VAL A 4   ? 0.3397 2.3059 0.7308 -0.0563 -0.1908 0.4909  856  VAL A CB  
26   C CG1 . VAL A 4   ? 0.3355 2.4526 0.7466 -0.0323 -0.1907 0.5296  856  VAL A CG1 
27   C CG2 . VAL A 4   ? 0.3451 2.3054 0.7619 -0.1355 -0.2167 0.4975  856  VAL A CG2 
28   N N   . SER A 5   ? 0.3392 1.9851 0.6493 -0.0141 -0.1645 0.3978  857  SER A N   
29   C CA  . SER A 5   ? 0.3416 1.8592 0.6321 -0.0250 -0.1601 0.3641  857  SER A CA  
30   C C   . SER A 5   ? 0.3296 1.8397 0.6185 0.0126  -0.1382 0.3681  857  SER A C   
31   O O   . SER A 5   ? 0.3256 1.9169 0.6204 0.0551  -0.1251 0.3914  857  SER A O   
32   C CB  . SER A 5   ? 0.3488 1.7692 0.6011 -0.0040 -0.1552 0.3308  857  SER A CB  
33   O OG  . SER A 5   ? 0.3526 1.7771 0.5828 0.0603  -0.1351 0.3329  857  SER A OG  
34   N N   . GLU A 6   ? 0.3361 1.7495 0.6149 -0.0011 -0.1347 0.3446  858  GLU A N   
35   C CA  . GLU A 6   ? 0.3331 1.7338 0.6099 0.0281  -0.1162 0.3463  858  GLU A CA  
36   C C   . GLU A 6   ? 0.3587 1.6994 0.5973 0.0907  -0.0952 0.3271  858  GLU A C   
37   O O   . GLU A 6   ? 0.3433 1.5980 0.5546 0.0946  -0.0955 0.3006  858  GLU A O   
38   C CB  . GLU A 6   ? 0.3269 1.6494 0.6084 -0.0138 -0.1227 0.3300  858  GLU A CB  
39   C CG  . GLU A 6   ? 0.3085 1.6296 0.5939 0.0059  -0.1070 0.3358  858  GLU A CG  
40   C CD  . GLU A 6   ? 0.2989 1.5697 0.5981 -0.0426 -0.1171 0.3300  858  GLU A CD  
41   O OE1 . GLU A 6   ? 0.3024 1.5466 0.6103 -0.0941 -0.1387 0.3246  858  GLU A OE1 
42   O OE2 . GLU A 6   ? 0.2832 1.5387 0.5817 -0.0266 -0.1038 0.3305  858  GLU A OE2 
43   N N   . LYS A 7   ? 0.3956 1.7815 0.6307 0.1391  -0.0783 0.3410  859  LYS A N   
44   C CA  . LYS A 7   ? 0.4524 1.7708 0.6474 0.1980  -0.0604 0.3222  859  LYS A CA  
45   C C   . LYS A 7   ? 0.4645 1.6636 0.6428 0.1806  -0.0575 0.2920  859  LYS A C   
46   O O   . LYS A 7   ? 0.4582 1.6559 0.6551 0.1532  -0.0583 0.2943  859  LYS A O   
47   C CB  . LYS A 7   ? 0.4785 1.8664 0.6710 0.2520  -0.0444 0.3410  859  LYS A CB  
48   C CG  . LYS A 7   ? 0.4879 2.0083 0.6977 0.2766  -0.0452 0.3741  859  LYS A CG  
49   C CD  . LYS A 7   ? 0.5083 2.1006 0.7140 0.3330  -0.0287 0.3915  859  LYS A CD  
50   C CE  . LYS A 7   ? 0.5246 2.2477 0.7423 0.3672  -0.0278 0.4233  859  LYS A CE  
51   N NZ  . LYS A 7   ? 0.5448 2.3287 0.7473 0.4374  -0.0099 0.4353  859  LYS A NZ  
52   N N   . LYS A 8   ? 0.5060 1.6098 0.6506 0.1938  -0.0551 0.2660  860  LYS A N   
53   C CA  . LYS A 8   ? 0.5412 1.5351 0.6679 0.1804  -0.0518 0.2380  860  LYS A CA  
54   C C   . LYS A 8   ? 0.5642 1.5344 0.6723 0.2218  -0.0359 0.2346  860  LYS A C   
55   O O   . LYS A 8   ? 0.5795 1.5451 0.6595 0.2732  -0.0269 0.2350  860  LYS A O   
56   C CB  . LYS A 8   ? 0.5731 1.4821 0.6708 0.1794  -0.0549 0.2148  860  LYS A CB  
57   C CG  . LYS A 8   ? 0.6120 1.5021 0.6752 0.2307  -0.0475 0.2142  860  LYS A CG  
58   C CD  . LYS A 8   ? 0.6220 1.4288 0.6601 0.2201  -0.0518 0.1938  860  LYS A CD  
59   C CE  . LYS A 8   ? 0.6587 1.4284 0.6582 0.2688  -0.0457 0.1933  860  LYS A CE  
60   N NZ  . LYS A 8   ? 0.6791 1.3880 0.6515 0.3016  -0.0351 0.1840  860  LYS A NZ  
61   N N   . PRO A 9   ? 0.5767 1.5323 0.6985 0.2007  -0.0335 0.2317  861  PRO A N   
62   C CA  . PRO A 9   ? 0.6134 1.5525 0.7170 0.2395  -0.0192 0.2285  861  PRO A CA  
63   C C   . PRO A 9   ? 0.6441 1.4684 0.7063 0.2587  -0.0137 0.2000  861  PRO A C   
64   O O   . PRO A 9   ? 0.5972 1.3553 0.6518 0.2326  -0.0203 0.1832  861  PRO A O   
65   C CB  . PRO A 9   ? 0.5962 1.5560 0.7301 0.2031  -0.0208 0.2358  861  PRO A CB  
66   C CG  . PRO A 9   ? 0.5826 1.5043 0.7332 0.1469  -0.0353 0.2265  861  PRO A CG  
67   C CD  . PRO A 9   ? 0.5590 1.5071 0.7097 0.1428  -0.0448 0.2305  861  PRO A CD  
68   N N   . ALA A 10  ? 0.7021 1.5066 0.7365 0.3043  -0.0028 0.1955  862  ALA A N   
69   C CA  . ALA A 10  ? 0.7539 1.4496 0.7484 0.3193  0.0007  0.1703  862  ALA A CA  
70   C C   . ALA A 10  ? 0.7420 1.3878 0.7495 0.2773  -0.0004 0.1569  862  ALA A C   
71   O O   . ALA A 10  ? 0.7061 1.3910 0.7361 0.2659  0.0028  0.1652  862  ALA A O   
72   C CB  . ALA A 10  ? 0.7848 1.4718 0.7447 0.3768  0.0102  0.1681  862  ALA A CB  
73   N N   . THR A 11  ? 0.7728 1.3382 0.7666 0.2550  -0.0053 0.1382  863  THR A N   
74   C CA  . THR A 11  ? 0.7473 1.2615 0.7502 0.2180  -0.0067 0.1242  863  THR A CA  
75   C C   . THR A 11  ? 0.7537 1.1819 0.7199 0.2352  -0.0019 0.1055  863  THR A C   
76   O O   . THR A 11  ? 0.7804 1.1587 0.7139 0.2549  -0.0033 0.0978  863  THR A O   
77   C CB  . THR A 11  ? 0.7502 1.2469 0.7689 0.1750  -0.0167 0.1174  863  THR A CB  
78   O OG1 . THR A 11  ? 0.7634 1.2135 0.7892 0.1453  -0.0174 0.1041  863  THR A OG1 
79   C CG2 . THR A 11  ? 0.7698 1.2216 0.7615 0.1837  -0.0200 0.1083  863  THR A CG2 
80   N N   . GLU A 12  ? 0.7057 1.1187 0.6772 0.2267  0.0025  0.1002  864  GLU A N   
81   C CA  . GLU A 12  ? 0.6857 1.0193 0.6272 0.2328  0.0050  0.0826  864  GLU A CA  
82   C C   . GLU A 12  ? 0.6172 0.9183 0.5767 0.1893  0.0018  0.0728  864  GLU A C   
83   O O   . GLU A 12  ? 0.6126 0.9506 0.6043 0.1651  0.0013  0.0794  864  GLU A O   
84   C CB  . GLU A 12  ? 0.7064 1.0515 0.6369 0.2606  0.0126  0.0837  864  GLU A CB  
85   C CG  . GLU A 12  ? 0.7382 0.9995 0.6283 0.2744  0.0130  0.0654  864  GLU A CG  
86   C CD  . GLU A 12  ? 0.7602 1.0327 0.6315 0.3093  0.0194  0.0645  864  GLU A CD  
87   O OE1 . GLU A 12  ? 0.7357 1.0741 0.6351 0.3064  0.0251  0.0763  864  GLU A OE1 
88   O OE2 . GLU A 12  ? 0.8062 1.0200 0.6325 0.3394  0.0175  0.0523  864  GLU A OE2 
89   N N   . VAL A 13  ? 0.5714 0.8052 0.5095 0.1801  -0.0011 0.0587  865  VAL A N   
90   C CA  . VAL A 13  ? 0.5296 0.7345 0.4816 0.1439  -0.0036 0.0487  865  VAL A CA  
91   C C   . VAL A 13  ? 0.4780 0.6658 0.4321 0.1400  0.0012  0.0438  865  VAL A C   
92   O O   . VAL A 13  ? 0.4894 0.6524 0.4185 0.1632  0.0049  0.0403  865  VAL A O   
93   C CB  . VAL A 13  ? 0.5757 0.7239 0.5042 0.1362  -0.0075 0.0379  865  VAL A CB  
94   C CG1 . VAL A 13  ? 0.5740 0.6999 0.5158 0.1035  -0.0090 0.0277  865  VAL A CG1 
95   C CG2 . VAL A 13  ? 0.6028 0.7708 0.5291 0.1400  -0.0124 0.0439  865  VAL A CG2 
96   N N   . ASP A 14  ? 0.3894 0.5888 0.3714 0.1112  -0.0001 0.0433  866  ASP A N   
97   C CA  . ASP A 14  ? 0.3518 0.5398 0.3398 0.1046  0.0039  0.0406  866  ASP A CA  
98   C C   . ASP A 14  ? 0.3240 0.4543 0.2986 0.0896  0.0028  0.0257  866  ASP A C   
99   O O   . ASP A 14  ? 0.2989 0.4226 0.2853 0.0677  -0.0014 0.0207  866  ASP A O   
100  C CB  . ASP A 14  ? 0.3219 0.5527 0.3468 0.0816  0.0013  0.0509  866  ASP A CB  
101  C CG  . ASP A 14  ? 0.3091 0.5349 0.3423 0.0757  0.0054  0.0516  866  ASP A CG  
102  O OD1 . ASP A 14  ? 0.3128 0.4963 0.3258 0.0822  0.0092  0.0406  866  ASP A OD1 
103  O OD2 . ASP A 14  ? 0.3367 0.6021 0.3970 0.0626  0.0036  0.0649  866  ASP A OD2 
104  N N   . PRO A 15  ? 0.3522 0.4436 0.3015 0.1013  0.0058  0.0187  867  PRO A N   
105  C CA  . PRO A 15  ? 0.3648 0.4093 0.3022 0.0853  0.0042  0.0077  867  PRO A CA  
106  C C   . PRO A 15  ? 0.3043 0.3528 0.2655 0.0626  0.0053  0.0048  867  PRO A C   
107  O O   . PRO A 15  ? 0.3094 0.3304 0.2651 0.0493  0.0043  -0.0029 867  PRO A O   
108  C CB  . PRO A 15  ? 0.4077 0.4141 0.3121 0.1028  0.0050  0.0032  867  PRO A CB  
109  C CG  . PRO A 15  ? 0.4004 0.4386 0.3080 0.1239  0.0094  0.0094  867  PRO A CG  
110  C CD  . PRO A 15  ? 0.3666 0.4571 0.2959 0.1290  0.0098  0.0205  867  PRO A CD  
111  N N   . THR A 16  ? 0.2490 0.3334 0.2355 0.0592  0.0067  0.0128  868  THR A N   
112  C CA  . THR A 16  ? 0.2339 0.3204 0.2431 0.0389  0.0058  0.0119  868  THR A CA  
113  C C   . THR A 16  ? 0.1727 0.2757 0.2039 0.0210  -0.0010 0.0132  868  THR A C   
114  O O   . THR A 16  ? 0.1832 0.2847 0.2314 0.0061  -0.0038 0.0132  868  THR A O   
115  C CB  . THR A 16  ? 0.2139 0.3242 0.2360 0.0427  0.0097  0.0216  868  THR A CB  
116  O OG1 . THR A 16  ? 0.1679 0.3258 0.2074 0.0464  0.0086  0.0361  868  THR A OG1 
117  C CG2 . THR A 16  ? 0.2329 0.3254 0.2291 0.0621  0.0151  0.0180  868  THR A CG2 
118  N N   A HIS A 17  ? 0.2203 0.3359 0.2488 0.0231  -0.0049 0.0142  869  HIS A N   
119  N N   B HIS A 17  ? 0.2132 0.3315 0.2428 0.0234  -0.0048 0.0152  869  HIS A N   
120  C CA  A HIS A 17  ? 0.2143 0.3431 0.2590 0.0056  -0.0137 0.0136  869  HIS A CA  
121  C CA  B HIS A 17  ? 0.1997 0.3276 0.2440 0.0057  -0.0136 0.0134  869  HIS A CA  
122  C C   A HIS A 17  ? 0.2294 0.3324 0.2589 0.0016  -0.0164 -0.0002 869  HIS A C   
123  C C   B HIS A 17  ? 0.2197 0.3175 0.2465 0.0034  -0.0147 -0.0009 869  HIS A C   
124  O O   A HIS A 17  ? 0.2294 0.3353 0.2445 0.0111  -0.0162 0.0001  869  HIS A O   
125  O O   B HIS A 17  ? 0.2088 0.2977 0.2155 0.0158  -0.0118 -0.0019 869  HIS A O   
126  C CB  A HIS A 17  ? 0.2036 0.3775 0.2586 0.0094  -0.0174 0.0272  869  HIS A CB  
127  C CB  B HIS A 17  ? 0.1811 0.3518 0.2351 0.0081  -0.0180 0.0255  869  HIS A CB  
128  C CG  A HIS A 17  ? 0.2480 0.4349 0.3166 -0.0106 -0.0290 0.0265  869  HIS A CG  
129  C CG  B HIS A 17  ? 0.2105 0.4233 0.2874 0.0043  -0.0190 0.0429  869  HIS A CG  
130  N ND1 A HIS A 17  ? 0.3056 0.4925 0.3633 -0.0096 -0.0331 0.0203  869  HIS A ND1 
131  N ND1 B HIS A 17  ? 0.2268 0.4355 0.3178 -0.0065 -0.0188 0.0470  869  HIS A ND1 
132  C CD2 A HIS A 17  ? 0.2939 0.4904 0.3835 -0.0331 -0.0392 0.0310  869  HIS A CD2 
133  C CD2 B HIS A 17  ? 0.1703 0.4360 0.2593 0.0092  -0.0206 0.0598  869  HIS A CD2 
134  C CE1 A HIS A 17  ? 0.2981 0.4960 0.3689 -0.0298 -0.0452 0.0195  869  HIS A CE1 
135  C CE1 B HIS A 17  ? 0.1870 0.4437 0.2978 -0.0097 -0.0203 0.0665  869  HIS A CE1 
136  N NE2 A HIS A 17  ? 0.3266 0.5271 0.4161 -0.0452 -0.0500 0.0258  869  HIS A NE2 
137  N NE2 B HIS A 17  ? 0.2010 0.4958 0.3116 -0.0002 -0.0212 0.0747  869  HIS A NE2 
138  N N   . PHE A 18  ? 0.2068 0.2884 0.2394 -0.0109 -0.0192 -0.0110 870  PHE A N   
139  C CA  . PHE A 18  ? 0.2428 0.3059 0.2610 -0.0132 -0.0205 -0.0240 870  PHE A CA  
140  C C   . PHE A 18  ? 0.2651 0.3390 0.2900 -0.0240 -0.0312 -0.0291 870  PHE A C   
141  O O   . PHE A 18  ? 0.2819 0.3557 0.3216 -0.0361 -0.0392 -0.0298 870  PHE A O   
142  C CB  . PHE A 18  ? 0.1917 0.2313 0.2074 -0.0161 -0.0171 -0.0329 870  PHE A CB  
143  C CG  . PHE A 18  ? 0.2514 0.2796 0.2567 -0.0082 -0.0086 -0.0288 870  PHE A CG  
144  C CD1 . PHE A 18  ? 0.2465 0.2790 0.2598 -0.0044 -0.0052 -0.0204 870  PHE A CD1 
145  C CD2 . PHE A 18  ? 0.2874 0.3021 0.2732 -0.0060 -0.0053 -0.0323 870  PHE A CD2 
146  C CE1 . PHE A 18  ? 0.2722 0.2912 0.2716 0.0030  0.0007  -0.0185 870  PHE A CE1 
147  C CE2 . PHE A 18  ? 0.3059 0.3056 0.2789 -0.0021 -0.0007 -0.0284 870  PHE A CE2 
148  C CZ  . PHE A 18  ? 0.2633 0.2629 0.2419 0.0031  0.0020  -0.0231 870  PHE A CZ  
149  N N   . GLU A 19  ? 0.2564 0.3379 0.2686 -0.0204 -0.0329 -0.0320 871  GLU A N   
150  C CA  . GLU A 19  ? 0.2696 0.3621 0.2836 -0.0299 -0.0439 -0.0384 871  GLU A CA  
151  C C   . GLU A 19  ? 0.2715 0.3413 0.2776 -0.0346 -0.0479 -0.0564 871  GLU A C   
152  O O   . GLU A 19  ? 0.2666 0.3253 0.2591 -0.0273 -0.0406 -0.0628 871  GLU A O   
153  C CB  . GLU A 19  ? 0.2674 0.3780 0.2686 -0.0223 -0.0437 -0.0348 871  GLU A CB  
154  C CG  . GLU A 19  ? 0.3544 0.4888 0.3594 -0.0115 -0.0402 -0.0177 871  GLU A CG  
155  C CD  . GLU A 19  ? 0.4750 0.6278 0.4677 -0.0033 -0.0420 -0.0132 871  GLU A CD  
156  O OE1 . GLU A 19  ? 0.5654 0.7292 0.5567 -0.0123 -0.0502 -0.0200 871  GLU A OE1 
157  O OE2 . GLU A 19  ? 0.5772 0.7319 0.5594 0.0135  -0.0362 -0.0029 871  GLU A OE2 
158  N N   . LYS A 20  ? 0.2699 0.3331 0.2830 -0.0466 -0.0605 -0.0639 872  LYS A N   
159  C CA  . LYS A 20  ? 0.3066 0.3457 0.3075 -0.0466 -0.0666 -0.0837 872  LYS A CA  
160  C C   . LYS A 20  ? 0.2956 0.3432 0.2755 -0.0368 -0.0631 -0.0944 872  LYS A C   
161  O O   . LYS A 20  ? 0.3014 0.3391 0.2692 -0.0276 -0.0578 -0.1052 872  LYS A O   
162  C CB  . LYS A 20  ? 0.3292 0.3571 0.3347 -0.0621 -0.0853 -0.0902 872  LYS A CB  
163  C CG  . LYS A 20  ? 0.4496 0.4431 0.4382 -0.0591 -0.0949 -0.1133 872  LYS A CG  
164  C CD  . LYS A 20  ? 0.5331 0.5075 0.5232 -0.0778 -0.1173 -0.1184 872  LYS A CD  
165  C CE  . LYS A 20  ? 0.6193 0.5553 0.5843 -0.0712 -0.1299 -0.1453 872  LYS A CE  
166  N NZ  . LYS A 20  ? 0.6555 0.5627 0.6179 -0.0924 -0.1556 -0.1507 872  LYS A NZ  
167  N N   . ARG A 21  ? 0.3306 0.4019 0.3066 -0.0382 -0.0658 -0.0892 873  ARG A N   
168  C CA  . ARG A 21  ? 0.3196 0.4037 0.2756 -0.0307 -0.0644 -0.0973 873  ARG A CA  
169  C C   . ARG A 21  ? 0.2924 0.3787 0.2380 -0.0202 -0.0503 -0.0925 873  ARG A C   
170  O O   . ARG A 21  ? 0.3020 0.3979 0.2317 -0.0144 -0.0485 -0.1003 873  ARG A O   
171  C CB  . ARG A 21  ? 0.3372 0.4487 0.2925 -0.0340 -0.0700 -0.0891 873  ARG A CB  
172  C CG  . ARG A 21  ? 0.3304 0.4578 0.2923 -0.0289 -0.0619 -0.0682 873  ARG A CG  
173  C CD  . ARG A 21  ? 0.3966 0.5547 0.3568 -0.0301 -0.0689 -0.0613 873  ARG A CD  
174  N NE  . ARG A 21  ? 0.4145 0.5877 0.3781 -0.0201 -0.0621 -0.0416 873  ARG A NE  
175  C CZ  . ARG A 21  ? 0.4517 0.6466 0.4059 -0.0120 -0.0622 -0.0321 873  ARG A CZ  
176  N NH1 . ARG A 21  ? 0.4251 0.6347 0.3674 -0.0145 -0.0681 -0.0389 873  ARG A NH1 
177  N NH2 . ARG A 21  ? 0.4915 0.6931 0.4461 0.0013  -0.0565 -0.0155 873  ARG A NH2 
178  N N   . PHE A 22  ? 0.2653 0.3445 0.2188 -0.0187 -0.0415 -0.0790 874  PHE A N   
179  C CA  . PHE A 22  ? 0.2685 0.3458 0.2116 -0.0135 -0.0311 -0.0724 874  PHE A CA  
180  C C   . PHE A 22  ? 0.2598 0.3236 0.2060 -0.0124 -0.0256 -0.0773 874  PHE A C   
181  O O   . PHE A 22  ? 0.2613 0.3261 0.1998 -0.0114 -0.0182 -0.0707 874  PHE A O   
182  C CB  . PHE A 22  ? 0.2704 0.3446 0.2132 -0.0111 -0.0268 -0.0549 874  PHE A CB  
183  C CG  . PHE A 22  ? 0.2565 0.3472 0.1943 -0.0083 -0.0312 -0.0474 874  PHE A CG  
184  C CD1 . PHE A 22  ? 0.2950 0.4027 0.2201 -0.0083 -0.0344 -0.0507 874  PHE A CD1 
185  C CD2 . PHE A 22  ? 0.3012 0.3953 0.2462 -0.0033 -0.0317 -0.0359 874  PHE A CD2 
186  C CE1 . PHE A 22  ? 0.2524 0.3772 0.1729 -0.0049 -0.0385 -0.0423 874  PHE A CE1 
187  C CE2 . PHE A 22  ? 0.3485 0.4618 0.2889 0.0022  -0.0354 -0.0276 874  PHE A CE2 
188  C CZ  . PHE A 22  ? 0.3278 0.4553 0.2563 0.0007  -0.0391 -0.0306 874  PHE A CZ  
189  N N   . LEU A 23  ? 0.2314 0.2823 0.1883 -0.0138 -0.0303 -0.0872 875  LEU A N   
190  C CA  . LEU A 23  ? 0.2750 0.3131 0.2368 -0.0110 -0.0251 -0.0897 875  LEU A CA  
191  C C   . LEU A 23  ? 0.3016 0.3438 0.2518 -0.0025 -0.0263 -0.1059 875  LEU A C   
192  O O   . LEU A 23  ? 0.3341 0.3630 0.2825 0.0001  -0.0358 -0.1206 875  LEU A O   
193  C CB  . LEU A 23  ? 0.2800 0.3010 0.2596 -0.0160 -0.0292 -0.0872 875  LEU A CB  
194  C CG  . LEU A 23  ? 0.3422 0.3515 0.3296 -0.0137 -0.0234 -0.0847 875  LEU A CG  
195  C CD1 . LEU A 23  ? 0.3184 0.3332 0.3042 -0.0137 -0.0137 -0.0714 875  LEU A CD1 
196  C CD2 . LEU A 23  ? 0.3629 0.3571 0.3672 -0.0200 -0.0302 -0.0819 875  LEU A CD2 
197  N N   . LYS A 24  ? 0.2958 0.3573 0.2356 0.0022  -0.0180 -0.1027 876  LYS A N   
198  C CA  . LYS A 24  ? 0.3675 0.4474 0.2929 0.0138  -0.0175 -0.1158 876  LYS A CA  
199  C C   . LYS A 24  ? 0.3730 0.4564 0.3003 0.0232  -0.0114 -0.1189 876  LYS A C   
200  O O   . LYS A 24  ? 0.3013 0.3966 0.2329 0.0184  -0.0033 -0.1050 876  LYS A O   
201  C CB  . LYS A 24  ? 0.3738 0.4857 0.2861 0.0123  -0.0130 -0.1070 876  LYS A CB  
202  C CG  . LYS A 24  ? 0.4538 0.5672 0.3622 0.0059  -0.0188 -0.1029 876  LYS A CG  
203  C CD  . LYS A 24  ? 0.5347 0.6409 0.4391 0.0101  -0.0299 -0.1214 876  LYS A CD  
204  C CE  . LYS A 24  ? 0.5854 0.7046 0.4844 0.0048  -0.0351 -0.1166 876  LYS A CE  
205  N NZ  . LYS A 24  ? 0.6349 0.7427 0.5327 0.0034  -0.0487 -0.1326 876  LYS A NZ  
206  N N   . ARG A 25  ? 0.3702 0.4418 0.2920 0.0372  -0.0168 -0.1372 877  ARG A N   
207  C CA  . ARG A 25  ? 0.3952 0.4697 0.3170 0.0515  -0.0122 -0.1422 877  ARG A CA  
208  C C   . ARG A 25  ? 0.3834 0.5067 0.2955 0.0605  -0.0020 -0.1373 877  ARG A C   
209  O O   . ARG A 25  ? 0.4181 0.5678 0.3148 0.0673  -0.0022 -0.1432 877  ARG A O   
210  C CB  . ARG A 25  ? 0.4336 0.4790 0.3443 0.0683  -0.0232 -0.1656 877  ARG A CB  
211  C CG  . ARG A 25  ? 0.4780 0.5173 0.3882 0.0872  -0.0205 -0.1716 877  ARG A CG  
212  C CD  . ARG A 25  ? 0.5901 0.5920 0.4821 0.1065  -0.0339 -0.1964 877  ARG A CD  
213  N NE  . ARG A 25  ? 0.6337 0.6341 0.5195 0.1318  -0.0309 -0.2036 877  ARG A NE  
214  C CZ  . ARG A 25  ? 0.6042 0.6484 0.4766 0.1563  -0.0215 -0.2087 877  ARG A CZ  
215  N NH1 . ARG A 25  ? 0.5998 0.6945 0.4643 0.1565  -0.0140 -0.2058 877  ARG A NH1 
216  N NH2 . ARG A 25  ? 0.6571 0.6995 0.5244 0.1817  -0.0196 -0.2147 877  ARG A NH2 
217  N N   . ILE A 26  ? 0.3395 0.4788 0.2603 0.0603  0.0062  -0.1256 878  ILE A N   
218  C CA  . ILE A 26  ? 0.3302 0.5227 0.2444 0.0695  0.0153  -0.1192 878  ILE A CA  
219  C C   . ILE A 26  ? 0.3815 0.5802 0.2915 0.0967  0.0167  -0.1332 878  ILE A C   
220  O O   . ILE A 26  ? 0.3833 0.6151 0.2773 0.1190  0.0187  -0.1443 878  ILE A O   
221  C CB  . ILE A 26  ? 0.3077 0.5203 0.2324 0.0481  0.0220  -0.0939 878  ILE A CB  
222  C CG1 . ILE A 26  ? 0.2892 0.4931 0.2113 0.0264  0.0194  -0.0812 878  ILE A CG1 
223  C CG2 . ILE A 26  ? 0.2662 0.5407 0.1875 0.0540  0.0303  -0.0833 878  ILE A CG2 
224  C CD1 . ILE A 26  ? 0.3024 0.5059 0.2297 0.0040  0.0215  -0.0588 878  ILE A CD1 
225  N N   . ARG A 27  ? 0.3269 0.4954 0.2495 0.0971  0.0155  -0.1325 879  ARG A N   
226  C CA  . ARG A 27  ? 0.3731 0.5415 0.2921 0.1239  0.0160  -0.1436 879  ARG A CA  
227  C C   . ARG A 27  ? 0.3384 0.4596 0.2718 0.1198  0.0113  -0.1421 879  ARG A C   
228  O O   . ARG A 27  ? 0.3553 0.4572 0.3038 0.0956  0.0107  -0.1290 879  ARG A O   
229  C CB  . ARG A 27  ? 0.3770 0.6103 0.2981 0.1321  0.0278  -0.1301 879  ARG A CB  
230  C CG  . ARG A 27  ? 0.3018 0.5500 0.2414 0.1056  0.0334  -0.1053 879  ARG A CG  
231  C CD  . ARG A 27  ? 0.3408 0.6596 0.2818 0.1099  0.0428  -0.0903 879  ARG A CD  
232  N NE  . ARG A 27  ? 0.2273 0.5549 0.1828 0.0816  0.0451  -0.0675 879  ARG A NE  
233  C CZ  . ARG A 27  ? 0.2815 0.6069 0.2492 0.0814  0.0467  -0.0607 879  ARG A CZ  
234  N NH1 . ARG A 27  ? 0.2692 0.5812 0.2385 0.1084  0.0466  -0.0732 879  ARG A NH1 
235  N NH2 . ARG A 27  ? 0.2950 0.6269 0.2714 0.0533  0.0470  -0.0412 879  ARG A NH2 
236  N N   . ASP A 28  ? 0.3695 0.4747 0.2965 0.1456  0.0081  -0.1547 880  ASP A N   
237  C CA  . ASP A 28  ? 0.3586 0.4252 0.2987 0.1443  0.0040  -0.1505 880  ASP A CA  
238  C C   . ASP A 28  ? 0.3539 0.4576 0.3110 0.1372  0.0151  -0.1298 880  ASP A C   
239  O O   . ASP A 28  ? 0.3232 0.4820 0.2775 0.1482  0.0244  -0.1240 880  ASP A O   
240  C CB  . ASP A 28  ? 0.4173 0.4499 0.3412 0.1764  -0.0047 -0.1701 880  ASP A CB  
241  C CG  . ASP A 28  ? 0.4883 0.4628 0.3960 0.1772  -0.0214 -0.1901 880  ASP A CG  
242  O OD1 . ASP A 28  ? 0.6022 0.5609 0.5173 0.1503  -0.0264 -0.1860 880  ASP A OD1 
243  O OD2 . ASP A 28  ? 0.6363 0.5800 0.5219 0.2055  -0.0308 -0.2103 880  ASP A OD2 
244  N N   . LEU A 29  ? 0.3293 0.4057 0.3032 0.1193  0.0132  -0.1182 881  LEU A N   
245  C CA  . LEU A 29  ? 0.3025 0.4055 0.2911 0.1126  0.0210  -0.1003 881  LEU A CA  
246  C C   . LEU A 29  ? 0.3522 0.4366 0.3447 0.1323  0.0183  -0.1020 881  LEU A C   
247  O O   . LEU A 29  ? 0.3755 0.4976 0.3723 0.1430  0.0254  -0.0935 881  LEU A O   
248  C CB  . LEU A 29  ? 0.2573 0.3481 0.2591 0.0822  0.0213  -0.0857 881  LEU A CB  
249  C CG  . LEU A 29  ? 0.2352 0.3485 0.2322 0.0631  0.0248  -0.0791 881  LEU A CG  
250  C CD1 . LEU A 29  ? 0.2521 0.3443 0.2571 0.0394  0.0235  -0.0678 881  LEU A CD1 
251  C CD2 . LEU A 29  ? 0.2276 0.3975 0.2207 0.0625  0.0327  -0.0692 881  LEU A CD2 
252  N N   . GLY A 30  ? 0.3996 0.4271 0.3903 0.1361  0.0070  -0.1112 882  GLY A N   
253  C CA  . GLY A 30  ? 0.4791 0.4781 0.4723 0.1527  0.0017  -0.1109 882  GLY A CA  
254  C C   . GLY A 30  ? 0.5637 0.4955 0.5558 0.1459  -0.0138 -0.1168 882  GLY A C   
255  O O   . GLY A 30  ? 0.5199 0.4335 0.5139 0.1246  -0.0193 -0.1181 882  GLY A O   
256  N N   . GLU A 31  ? 0.6664 0.5628 0.6545 0.1643  -0.0219 -0.1191 883  GLU A N   
257  C CA  . GLU A 31  ? 0.7637 0.5925 0.7504 0.1563  -0.0396 -0.1207 883  GLU A CA  
258  C C   . GLU A 31  ? 0.7973 0.6200 0.8041 0.1473  -0.0392 -0.0989 883  GLU A C   
259  O O   . GLU A 31  ? 0.7822 0.6425 0.7962 0.1592  -0.0279 -0.0894 883  GLU A O   
260  C CB  . GLU A 31  ? 0.8374 0.6175 0.7959 0.1874  -0.0537 -0.1429 883  GLU A CB  
261  C CG  . GLU A 31  ? 0.8754 0.6634 0.8096 0.2017  -0.0546 -0.1667 883  GLU A CG  
262  C CD  . GLU A 31  ? 0.9539 0.6824 0.8546 0.2321  -0.0721 -0.1919 883  GLU A CD  
263  O OE1 . GLU A 31  ? 0.9963 0.6875 0.8894 0.2531  -0.0798 -0.1919 883  GLU A OE1 
264  O OE2 . GLU A 31  ? 0.9795 0.6961 0.8588 0.2365  -0.0791 -0.2123 883  GLU A OE2 
265  N N   . GLY A 32  ? 0.8450 0.6251 0.8608 0.1254  -0.0520 -0.0895 884  GLY A N   
266  C CA  . GLY A 32  ? 0.8508 0.6267 0.8857 0.1153  -0.0526 -0.0668 884  GLY A CA  
267  C C   . GLY A 32  ? 0.8823 0.6119 0.9257 0.0906  -0.0693 -0.0548 884  GLY A C   
268  O O   . GLY A 32  ? 0.8703 0.6174 0.9288 0.0632  -0.0675 -0.0438 884  GLY A O   
269  N N   . HIS A 33  ? 0.9381 0.6099 0.9708 0.1009  -0.0862 -0.0557 885  HIS A N   
270  C CA  . HIS A 33  ? 0.9674 0.5938 1.0091 0.0758  -0.1047 -0.0384 885  HIS A CA  
271  C C   . HIS A 33  ? 0.9758 0.5850 1.0168 0.0478  -0.1169 -0.0425 885  HIS A C   
272  O O   . HIS A 33  ? 0.9272 0.5711 0.9897 0.0203  -0.1119 -0.0254 885  HIS A O   
273  C CB  . HIS A 33  ? 0.9298 0.5933 0.9996 0.0591  -0.0955 -0.0081 885  HIS A CB  
274  C CG  . HIS A 33  ? 0.9664 0.5959 1.0482 0.0326  -0.1129 0.0150  885  HIS A CG  
275  N ND1 . HIS A 33  ? 1.0333 0.5989 1.1045 0.0382  -0.1327 0.0204  885  HIS A ND1 
276  C CD2 . HIS A 33  ? 0.9426 0.5958 1.0458 -0.0002 -0.1142 0.0363  885  HIS A CD2 
277  C CE1 . HIS A 33  ? 1.0464 0.5979 1.1334 0.0059  -0.1463 0.0459  885  HIS A CE1 
278  N NE2 . HIS A 33  ? 0.9899 0.5986 1.0973 -0.0170 -0.1346 0.0561  885  HIS A NE2 
279  N N   . PHE A 34  ? 1.0398 0.5987 1.0540 0.0577  -0.1328 -0.0662 886  PHE A N   
280  C CA  . PHE A 34  ? 1.0552 0.5927 1.0633 0.0336  -0.1477 -0.0741 886  PHE A CA  
281  C C   . PHE A 34  ? 0.9801 0.5747 0.9937 0.0271  -0.1319 -0.0822 886  PHE A C   
282  O O   . PHE A 34  ? 1.0137 0.5919 1.0153 0.0170  -0.1431 -0.0957 886  PHE A O   
283  C CB  . PHE A 34  ? 1.0845 0.5987 1.1104 -0.0047 -0.1656 -0.0479 886  PHE A CB  
284  C CG  . PHE A 34  ? 1.1601 0.6009 1.1743 -0.0041 -0.1890 -0.0413 886  PHE A CG  
285  C CD1 . PHE A 34  ? 1.2426 0.6049 1.2265 -0.0046 -0.2168 -0.0596 886  PHE A CD1 
286  C CD2 . PHE A 34  ? 1.1564 0.6025 1.1871 -0.0032 -0.1849 -0.0165 886  PHE A CD2 
287  C CE1 . PHE A 34  ? 1.3207 0.6044 1.2894 -0.0040 -0.2416 -0.0534 886  PHE A CE1 
288  C CE2 . PHE A 34  ? 1.2297 0.6034 1.2481 -0.0025 -0.2080 -0.0081 886  PHE A CE2 
289  C CZ  . PHE A 34  ? 1.3143 0.6033 1.3009 -0.0030 -0.2370 -0.0265 886  PHE A CZ  
290  N N   . GLY A 35  ? 0.8747 0.5323 0.9043 0.0322  -0.1079 -0.0739 887  GLY A N   
291  C CA  . GLY A 35  ? 0.8000 0.5075 0.8319 0.0290  -0.0930 -0.0805 887  GLY A CA  
292  C C   . GLY A 35  ? 0.7560 0.4864 0.7708 0.0586  -0.0800 -0.0997 887  GLY A C   
293  O O   . GLY A 35  ? 0.7708 0.4920 0.7765 0.0835  -0.0781 -0.1049 887  GLY A O   
294  N N   . LYS A 36  ? 0.6499 0.4131 0.6602 0.0561  -0.0715 -0.1085 888  LYS A N   
295  C CA  . LYS A 36  ? 0.5839 0.3855 0.5827 0.0779  -0.0568 -0.1202 888  LYS A CA  
296  C C   . LYS A 36  ? 0.4898 0.3406 0.5005 0.0620  -0.0425 -0.1099 888  LYS A C   
297  O O   . LYS A 36  ? 0.4182 0.2680 0.4372 0.0407  -0.0463 -0.1033 888  LYS A O   
298  C CB  . LYS A 36  ? 0.6531 0.4359 0.6242 0.0964  -0.0652 -0.1461 888  LYS A CB  
299  C CG  . LYS A 36  ? 0.6567 0.4317 0.6226 0.0779  -0.0740 -0.1532 888  LYS A CG  
300  C CD  . LYS A 36  ? 0.7169 0.4692 0.6516 0.0981  -0.0845 -0.1807 888  LYS A CD  
301  C CE  . LYS A 36  ? 0.6979 0.5030 0.6213 0.1195  -0.0682 -0.1898 888  LYS A CE  
302  N NZ  . LYS A 36  ? 0.7449 0.5346 0.6361 0.1407  -0.0777 -0.2170 888  LYS A NZ  
303  N N   . VAL A 37  ? 0.4076 0.3006 0.4175 0.0725  -0.0274 -0.1077 889  VAL A N   
304  C CA  . VAL A 37  ? 0.3439 0.2765 0.3599 0.0586  -0.0158 -0.0983 889  VAL A CA  
305  C C   . VAL A 37  ? 0.3738 0.3353 0.3736 0.0695  -0.0101 -0.1099 889  VAL A C   
306  O O   . VAL A 37  ? 0.3766 0.3545 0.3665 0.0909  -0.0064 -0.1174 889  VAL A O   
307  C CB  . VAL A 37  ? 0.2880 0.2469 0.3171 0.0541  -0.0051 -0.0815 889  VAL A CB  
308  C CG1 . VAL A 37  ? 0.2292 0.2170 0.2589 0.0391  0.0034  -0.0733 889  VAL A CG1 
309  C CG2 . VAL A 37  ? 0.3306 0.2674 0.3752 0.0452  -0.0100 -0.0689 889  VAL A CG2 
310  N N   . GLU A 38  ? 0.3511 0.3224 0.3481 0.0560  -0.0095 -0.1096 890  GLU A N   
311  C CA  . GLU A 38  ? 0.3296 0.3306 0.3121 0.0618  -0.0049 -0.1168 890  GLU A CA  
312  C C   . GLU A 38  ? 0.2944 0.3253 0.2805 0.0455  0.0040  -0.1018 890  GLU A C   
313  O O   . GLU A 38  ? 0.2965 0.3156 0.2917 0.0292  0.0032  -0.0916 890  GLU A O   
314  C CB  . GLU A 38  ? 0.3498 0.3317 0.3208 0.0607  -0.0150 -0.1306 890  GLU A CB  
315  C CG  . GLU A 38  ? 0.4316 0.3743 0.3917 0.0745  -0.0282 -0.1484 890  GLU A CG  
316  C CD  . GLU A 38  ? 0.5404 0.4626 0.4911 0.0660  -0.0406 -0.1594 890  GLU A CD  
317  O OE1 . GLU A 38  ? 0.5402 0.4587 0.5039 0.0442  -0.0434 -0.1482 890  GLU A OE1 
318  O OE2 . GLU A 38  ? 0.7335 0.6459 0.6626 0.0823  -0.0478 -0.1794 890  GLU A OE2 
319  N N   . LEU A 39  ? 0.2661 0.3356 0.2432 0.0505  0.0112  -0.1002 891  LEU A N   
320  C CA  . LEU A 39  ? 0.2559 0.3483 0.2296 0.0341  0.0158  -0.0876 891  LEU A CA  
321  C C   . LEU A 39  ? 0.2709 0.3580 0.2347 0.0312  0.0111  -0.0945 891  LEU A C   
322  O O   . LEU A 39  ? 0.2662 0.3643 0.2185 0.0447  0.0091  -0.1075 891  LEU A O   
323  C CB  . LEU A 39  ? 0.2375 0.3780 0.2058 0.0362  0.0234  -0.0795 891  LEU A CB  
324  C CG  . LEU A 39  ? 0.1771 0.3384 0.1389 0.0164  0.0254  -0.0642 891  LEU A CG  
325  C CD1 . LEU A 39  ? 0.2372 0.3739 0.2040 -0.0031 0.0240  -0.0511 891  LEU A CD1 
326  C CD2 . LEU A 39  ? 0.2096 0.4253 0.1672 0.0172  0.0311  -0.0544 891  LEU A CD2 
327  N N   . CYS A 40  ? 0.2909 0.3626 0.2576 0.0157  0.0092  -0.0858 892  CYS A N   
328  C CA  . CYS A 40  ? 0.2905 0.3621 0.2487 0.0109  0.0054  -0.0875 892  CYS A CA  
329  C C   . CYS A 40  ? 0.3043 0.3847 0.2567 -0.0028 0.0085  -0.0714 892  CYS A C   
330  O O   . CYS A 40  ? 0.2573 0.3340 0.2125 -0.0109 0.0115  -0.0602 892  CYS A O   
331  C CB  . CYS A 40  ? 0.3160 0.3580 0.2821 0.0073  -0.0024 -0.0918 892  CYS A CB  
332  S SG  . CYS A 40  ? 0.3423 0.3605 0.3112 0.0184  -0.0116 -0.1097 892  CYS A SG  
333  N N   . ARG A 41  ? 0.2773 0.3664 0.2190 -0.0053 0.0062  -0.0705 893  ARG A N   
334  C CA  . ARG A 41  ? 0.3067 0.3887 0.2411 -0.0172 0.0055  -0.0559 893  ARG A CA  
335  C C   . ARG A 41  ? 0.2942 0.3573 0.2308 -0.0158 0.0002  -0.0588 893  ARG A C   
336  O O   . ARG A 41  ? 0.3205 0.3908 0.2561 -0.0105 -0.0038 -0.0692 893  ARG A O   
337  C CB  . ARG A 41  ? 0.3318 0.4423 0.2520 -0.0220 0.0067  -0.0477 893  ARG A CB  
338  C CG  . ARG A 41  ? 0.3938 0.4929 0.3030 -0.0368 0.0049  -0.0290 893  ARG A CG  
339  C CD  . ARG A 41  ? 0.3956 0.5251 0.2915 -0.0442 0.0046  -0.0177 893  ARG A CD  
340  N NE  . ARG A 41  ? 0.4141 0.5780 0.3099 -0.0516 0.0083  -0.0088 893  ARG A NE  
341  C CZ  . ARG A 41  ? 0.4859 0.6494 0.3744 -0.0710 0.0057  0.0106  893  ARG A CZ  
342  N NH1 . ARG A 41  ? 0.5814 0.7025 0.4583 -0.0832 -0.0014 0.0212  893  ARG A NH1 
343  N NH2 . ARG A 41  ? 0.5560 0.7620 0.4468 -0.0782 0.0089  0.0199  893  ARG A NH2 
344  N N   . TYR A 42  ? 0.2663 0.3083 0.2044 -0.0196 -0.0005 -0.0499 894  TYR A N   
345  C CA  . TYR A 42  ? 0.2779 0.3118 0.2165 -0.0171 -0.0048 -0.0482 894  TYR A CA  
346  C C   . TYR A 42  ? 0.2933 0.3295 0.2141 -0.0196 -0.0062 -0.0382 894  TYR A C   
347  O O   . TYR A 42  ? 0.2859 0.3047 0.1948 -0.0234 -0.0060 -0.0270 894  TYR A O   
348  C CB  . TYR A 42  ? 0.2573 0.2733 0.2032 -0.0152 -0.0044 -0.0425 894  TYR A CB  
349  C CG  . TYR A 42  ? 0.2525 0.2718 0.2035 -0.0104 -0.0084 -0.0405 894  TYR A CG  
350  C CD1 . TYR A 42  ? 0.2112 0.2426 0.1751 -0.0118 -0.0134 -0.0482 894  TYR A CD1 
351  C CD2 . TYR A 42  ? 0.2414 0.2524 0.1823 -0.0041 -0.0086 -0.0306 894  TYR A CD2 
352  C CE1 . TYR A 42  ? 0.2435 0.2856 0.2140 -0.0103 -0.0180 -0.0439 894  TYR A CE1 
353  C CE2 . TYR A 42  ? 0.2669 0.2904 0.2137 0.0024  -0.0117 -0.0270 894  TYR A CE2 
354  C CZ  . TYR A 42  ? 0.2732 0.3163 0.2366 -0.0024 -0.0163 -0.0326 894  TYR A CZ  
355  O OH  . TYR A 42  ? 0.3126 0.3755 0.2839 0.0010  -0.0204 -0.0267 894  TYR A OH  
356  N N   . ASP A 43  ? 0.2606 0.3147 0.1775 -0.0176 -0.0092 -0.0422 895  ASP A N   
357  C CA  . ASP A 43  ? 0.3056 0.3693 0.2056 -0.0206 -0.0105 -0.0323 895  ASP A CA  
358  C C   . ASP A 43  ? 0.2684 0.3358 0.1648 -0.0153 -0.0155 -0.0299 895  ASP A C   
359  O O   . ASP A 43  ? 0.2648 0.3551 0.1562 -0.0145 -0.0178 -0.0332 895  ASP A O   
360  C CB  . ASP A 43  ? 0.3069 0.4013 0.2026 -0.0222 -0.0082 -0.0375 895  ASP A CB  
361  C CG  . ASP A 43  ? 0.3509 0.4594 0.2299 -0.0306 -0.0083 -0.0212 895  ASP A CG  
362  O OD1 . ASP A 43  ? 0.2978 0.3843 0.1680 -0.0395 -0.0098 -0.0059 895  ASP A OD1 
363  O OD2 . ASP A 43  ? 0.3230 0.4647 0.1960 -0.0289 -0.0078 -0.0232 895  ASP A OD2 
364  N N   . PRO A 44  ? 0.2915 0.3403 0.1889 -0.0099 -0.0171 -0.0232 896  PRO A N   
365  C CA  . PRO A 44  ? 0.2865 0.3442 0.1814 -0.0025 -0.0215 -0.0186 896  PRO A CA  
366  C C   . PRO A 44  ? 0.3080 0.3716 0.1838 -0.0026 -0.0242 -0.0077 896  PRO A C   
367  O O   . PRO A 44  ? 0.3260 0.4087 0.2014 0.0023  -0.0280 -0.0067 896  PRO A O   
368  C CB  . PRO A 44  ? 0.3045 0.3422 0.2002 0.0072  -0.0210 -0.0115 896  PRO A CB  
369  C CG  . PRO A 44  ? 0.3316 0.3443 0.2239 0.0035  -0.0174 -0.0112 896  PRO A CG  
370  C CD  . PRO A 44  ? 0.3012 0.3240 0.2003 -0.0079 -0.0147 -0.0194 896  PRO A CD  
371  N N   . GLU A 45  ? 0.3122 0.3612 0.1724 -0.0098 -0.0234 0.0022  897  GLU A N   
372  C CA  . GLU A 45  ? 0.3939 0.4485 0.2356 -0.0131 -0.0270 0.0161  897  GLU A CA  
373  C C   . GLU A 45  ? 0.3486 0.4424 0.1911 -0.0206 -0.0253 0.0121  897  GLU A C   
374  O O   . GLU A 45  ? 0.4263 0.5327 0.2546 -0.0250 -0.0277 0.0251  897  GLU A O   
375  C CB  . GLU A 45  ? 0.4236 0.4412 0.2453 -0.0204 -0.0301 0.0323  897  GLU A CB  
376  C CG  . GLU A 45  ? 0.4650 0.4404 0.2805 -0.0098 -0.0320 0.0332  897  GLU A CG  
377  C CD  . GLU A 45  ? 0.5324 0.4626 0.3187 -0.0129 -0.0400 0.0498  897  GLU A CD  
378  O OE1 . GLU A 45  ? 0.5708 0.4717 0.3484 -0.0230 -0.0421 0.0519  897  GLU A OE1 
379  O OE2 . GLU A 45  ? 0.7641 0.6863 0.5345 -0.0057 -0.0456 0.0612  897  GLU A OE2 
380  N N   . GLY A 46  ? 0.3329 0.4450 0.1896 -0.0205 -0.0215 -0.0051 898  GLY A N   
381  C CA  . GLY A 46  ? 0.3350 0.4858 0.1902 -0.0207 -0.0199 -0.0140 898  GLY A CA  
382  C C   . GLY A 46  ? 0.3651 0.5392 0.2081 -0.0298 -0.0173 -0.0002 898  GLY A C   
383  O O   . GLY A 46  ? 0.3811 0.5941 0.2173 -0.0274 -0.0168 -0.0022 898  GLY A O   
384  N N   . ASP A 47  ? 0.3727 0.5264 0.2119 -0.0411 -0.0164 0.0144  899  ASP A N   
385  C CA  . ASP A 47  ? 0.3792 0.5556 0.2074 -0.0556 -0.0160 0.0336  899  ASP A CA  
386  C C   . ASP A 47  ? 0.4057 0.5899 0.2406 -0.0647 -0.0116 0.0352  899  ASP A C   
387  O O   . ASP A 47  ? 0.4096 0.6063 0.2362 -0.0821 -0.0133 0.0559  899  ASP A O   
388  C CB  . ASP A 47  ? 0.4357 0.5805 0.2465 -0.0665 -0.0238 0.0577  899  ASP A CB  
389  C CG  . ASP A 47  ? 0.4295 0.5152 0.2366 -0.0688 -0.0279 0.0604  899  ASP A CG  
390  O OD1 . ASP A 47  ? 0.4023 0.4742 0.2229 -0.0616 -0.0240 0.0444  899  ASP A OD1 
391  O OD2 . ASP A 47  ? 0.5098 0.5609 0.2977 -0.0772 -0.0362 0.0792  899  ASP A OD2 
392  N N   . ASN A 48  ? 0.3417 0.5213 0.1915 -0.0545 -0.0070 0.0154  900  ASN A N   
393  C CA  . ASN A 48  ? 0.3395 0.5266 0.1973 -0.0599 -0.0027 0.0154  900  ASN A CA  
394  C C   . ASN A 48  ? 0.3690 0.5188 0.2214 -0.0772 -0.0072 0.0317  900  ASN A C   
395  O O   . ASN A 48  ? 0.3997 0.5671 0.2525 -0.0907 -0.0063 0.0427  900  ASN A O   
396  C CB  . ASN A 48  ? 0.3528 0.6013 0.2090 -0.0612 0.0023  0.0208  900  ASN A CB  
397  C CG  . ASN A 48  ? 0.3451 0.6130 0.2130 -0.0570 0.0085  0.0138  900  ASN A CG  
398  O OD1 . ASN A 48  ? 0.3401 0.5793 0.2189 -0.0478 0.0097  -0.0018 900  ASN A OD1 
399  N ND2 . ASN A 48  ? 0.3640 0.6855 0.2301 -0.0638 0.0121  0.0276  900  ASN A ND2 
400  N N   . THR A 49  ? 0.3421 0.4424 0.1879 -0.0758 -0.0127 0.0329  901  THR A N   
401  C CA  . THR A 49  ? 0.3661 0.4221 0.2011 -0.0884 -0.0188 0.0442  901  THR A CA  
402  C C   . THR A 49  ? 0.3736 0.3951 0.2168 -0.0774 -0.0173 0.0302  901  THR A C   
403  O O   . THR A 49  ? 0.3927 0.3793 0.2262 -0.0851 -0.0220 0.0358  901  THR A O   
404  C CB  . THR A 49  ? 0.4121 0.4323 0.2233 -0.0957 -0.0290 0.0615  901  THR A CB  
405  O OG1 . THR A 49  ? 0.4488 0.4466 0.2589 -0.0764 -0.0296 0.0524  901  THR A OG1 
406  C CG2 . THR A 49  ? 0.3853 0.4412 0.1877 -0.1091 -0.0315 0.0797  901  THR A CG2 
407  N N   . GLY A 50  ? 0.3347 0.3668 0.1947 -0.0606 -0.0119 0.0129  902  GLY A N   
408  C CA  . GLY A 50  ? 0.3295 0.3371 0.1996 -0.0504 -0.0103 0.0023  902  GLY A CA  
409  C C   . GLY A 50  ? 0.3133 0.3224 0.1928 -0.0553 -0.0068 -0.0009 902  GLY A C   
410  O O   . GLY A 50  ? 0.3160 0.3522 0.1980 -0.0643 -0.0045 0.0027  902  GLY A O   
411  N N   . GLU A 51  ? 0.3457 0.3309 0.2307 -0.0483 -0.0062 -0.0065 903  GLU A N   
412  C CA  . GLU A 51  ? 0.3279 0.3135 0.2213 -0.0522 -0.0034 -0.0086 903  GLU A CA  
413  C C   . GLU A 51  ? 0.3055 0.3232 0.2204 -0.0459 0.0029  -0.0194 903  GLU A C   
414  O O   . GLU A 51  ? 0.2832 0.3085 0.2084 -0.0356 0.0038  -0.0293 903  GLU A O   
415  C CB  . GLU A 51  ? 0.4084 0.3635 0.3003 -0.0446 -0.0044 -0.0110 903  GLU A CB  
416  C CG  . GLU A 51  ? 0.4369 0.3991 0.3472 -0.0302 -0.0009 -0.0200 903  GLU A CG  
417  C CD  . GLU A 51  ? 0.5573 0.4977 0.4628 -0.0195 -0.0020 -0.0192 903  GLU A CD  
418  O OE1 . GLU A 51  ? 0.4635 0.3824 0.3557 -0.0213 -0.0038 -0.0165 903  GLU A OE1 
419  O OE2 . GLU A 51  ? 0.5308 0.4797 0.4455 -0.0089 -0.0015 -0.0211 903  GLU A OE2 
420  N N   . GLN A 52  ? 0.2911 0.3259 0.2104 -0.0522 0.0056  -0.0170 904  GLN A N   
421  C CA  . GLN A 52  ? 0.2388 0.2961 0.1751 -0.0427 0.0107  -0.0269 904  GLN A CA  
422  C C   . GLN A 52  ? 0.2673 0.3028 0.2156 -0.0363 0.0114  -0.0319 904  GLN A C   
423  O O   . GLN A 52  ? 0.2847 0.3006 0.2275 -0.0416 0.0099  -0.0258 904  GLN A O   
424  C CB  . GLN A 52  ? 0.2969 0.3852 0.2337 -0.0498 0.0136  -0.0198 904  GLN A CB  
425  C CG  . GLN A 52  ? 0.3316 0.4515 0.2579 -0.0579 0.0132  -0.0107 904  GLN A CG  
426  C CD  . GLN A 52  ? 0.2882 0.4527 0.2178 -0.0640 0.0166  -0.0017 904  GLN A CD  
427  O OE1 . GLN A 52  ? 0.2494 0.4568 0.1801 -0.0560 0.0207  -0.0028 904  GLN A OE1 
428  N NE2 . GLN A 52  ? 0.3270 0.4857 0.2572 -0.0768 0.0147  0.0074  904  GLN A NE2 
429  N N   . VAL A 53  ? 0.2426 0.2807 0.2050 -0.0252 0.0124  -0.0425 905  VAL A N   
430  C CA  . VAL A 53  ? 0.2468 0.2698 0.2230 -0.0206 0.0124  -0.0447 905  VAL A CA  
431  C C   . VAL A 53  ? 0.2530 0.2837 0.2414 -0.0114 0.0131  -0.0534 905  VAL A C   
432  O O   . VAL A 53  ? 0.2639 0.3065 0.2486 -0.0048 0.0124  -0.0618 905  VAL A O   
433  C CB  . VAL A 53  ? 0.2325 0.2407 0.2122 -0.0181 0.0086  -0.0459 905  VAL A CB  
434  C CG1 . VAL A 53  ? 0.2444 0.2408 0.2096 -0.0213 0.0077  -0.0379 905  VAL A CG1 
435  C CG2 . VAL A 53  ? 0.2193 0.2333 0.1996 -0.0146 0.0047  -0.0550 905  VAL A CG2 
436  N N   . ALA A 54  ? 0.2199 0.2428 0.2202 -0.0094 0.0138  -0.0511 906  ALA A N   
437  C CA  . ALA A 54  ? 0.2582 0.2783 0.2691 0.0003  0.0123  -0.0578 906  ALA A CA  
438  C C   . ALA A 54  ? 0.2688 0.2676 0.2888 -0.0007 0.0055  -0.0603 906  ALA A C   
439  O O   . ALA A 54  ? 0.2470 0.2406 0.2735 -0.0071 0.0051  -0.0516 906  ALA A O   
440  C CB  . ALA A 54  ? 0.1957 0.2210 0.2147 0.0014  0.0161  -0.0504 906  ALA A CB  
441  N N   . VAL A 55  ? 0.2550 0.2436 0.2737 0.0058  -0.0010 -0.0720 907  VAL A N   
442  C CA  . VAL A 55  ? 0.2546 0.2227 0.2803 0.0007  -0.0110 -0.0742 907  VAL A CA  
443  C C   . VAL A 55  ? 0.3050 0.2499 0.3364 0.0064  -0.0181 -0.0785 907  VAL A C   
444  O O   . VAL A 55  ? 0.2897 0.2273 0.3104 0.0200  -0.0205 -0.0916 907  VAL A O   
445  C CB  . VAL A 55  ? 0.2993 0.2669 0.3134 0.0008  -0.0169 -0.0856 907  VAL A CB  
446  C CG1 . VAL A 55  ? 0.3058 0.2552 0.3274 -0.0089 -0.0295 -0.0860 907  VAL A CG1 
447  C CG2 . VAL A 55  ? 0.2908 0.2794 0.2969 -0.0032 -0.0103 -0.0800 907  VAL A CG2 
448  N N   . LYS A 56  ? 0.2804 0.2143 0.3270 -0.0027 -0.0224 -0.0667 908  LYS A N   
449  C CA  . LYS A 56  ? 0.3053 0.2109 0.3576 -0.0011 -0.0322 -0.0667 908  LYS A CA  
450  C C   . LYS A 56  ? 0.3783 0.2600 0.4327 -0.0138 -0.0480 -0.0683 908  LYS A C   
451  O O   . LYS A 56  ? 0.3392 0.2345 0.4044 -0.0290 -0.0499 -0.0567 908  LYS A O   
452  C CB  . LYS A 56  ? 0.3001 0.2114 0.3683 -0.0050 -0.0281 -0.0493 908  LYS A CB  
453  C CG  . LYS A 56  ? 0.3759 0.2564 0.4480 -0.0007 -0.0376 -0.0476 908  LYS A CG  
454  C CD  . LYS A 56  ? 0.3317 0.2278 0.4164 0.0003  -0.0296 -0.0313 908  LYS A CD  
455  C CE  . LYS A 56  ? 0.4503 0.3174 0.5365 0.0085  -0.0376 -0.0290 908  LYS A CE  
456  N NZ  . LYS A 56  ? 0.3240 0.2086 0.4248 0.0059  -0.0316 -0.0099 908  LYS A NZ  
457  N N   . SER A 57  ? 0.4142 0.2605 0.4566 -0.0069 -0.0604 -0.0825 909  SER A N   
458  C CA  . SER A 57  ? 0.4299 0.2464 0.4695 -0.0209 -0.0793 -0.0864 909  SER A CA  
459  C C   . SER A 57  ? 0.5165 0.2815 0.5471 -0.0148 -0.0947 -0.0934 909  SER A C   
460  O O   . SER A 57  ? 0.5005 0.2573 0.5239 0.0060  -0.0890 -0.0992 909  SER A O   
461  C CB  . SER A 57  ? 0.4583 0.2799 0.4802 -0.0169 -0.0817 -0.1045 909  SER A CB  
462  O OG  . SER A 57  ? 0.5708 0.3760 0.5702 0.0066  -0.0821 -0.1260 909  SER A OG  
463  N N   . LEU A 58  ? 0.5720 0.3020 0.6015 -0.0331 -0.1156 -0.0922 910  LEU A N   
464  C CA  . LEU A 58  ? 0.6609 0.3289 0.6769 -0.0296 -0.1353 -0.0992 910  LEU A CA  
465  C C   . LEU A 58  ? 0.7542 0.3824 0.7373 -0.0143 -0.1488 -0.1294 910  LEU A C   
466  O O   . LEU A 58  ? 0.7824 0.4235 0.7576 -0.0214 -0.1521 -0.1398 910  LEU A O   
467  C CB  . LEU A 58  ? 0.6864 0.3333 0.7182 -0.0622 -0.1542 -0.0778 910  LEU A CB  
468  C CG  . LEU A 58  ? 0.6854 0.3658 0.7468 -0.0744 -0.1437 -0.0472 910  LEU A CG  
469  C CD1 . LEU A 58  ? 0.7366 0.4113 0.8145 -0.1093 -0.1620 -0.0242 910  LEU A CD1 
470  C CD2 . LEU A 58  ? 0.7743 0.4327 0.8344 -0.0561 -0.1399 -0.0437 910  LEU A CD2 
471  N N   . LYS A 59  ? 0.8354 0.4157 0.7976 0.0090  -0.1571 -0.1435 911  LYS A N   
472  C CA  . LYS A 59  ? 0.9030 0.4307 0.8280 0.0265  -0.1752 -0.1737 911  LYS A CA  
473  C C   . LYS A 59  ? 0.9620 0.4210 0.8785 0.0006  -0.2071 -0.1715 911  LYS A C   
474  O O   . LYS A 59  ? 0.9482 0.4190 0.8802 -0.0343 -0.2162 -0.1578 911  LYS A O   
475  C CB  . LYS A 59  ? 0.9453 0.4523 0.8485 0.0679  -0.1704 -0.1899 911  LYS A CB  
476  C CG  . LYS A 59  ? 0.8939 0.4691 0.8017 0.0930  -0.1420 -0.1928 911  LYS A CG  
477  C CD  . LYS A 59  ? 0.9314 0.4937 0.8170 0.1359  -0.1383 -0.2083 911  LYS A CD  
478  C CE  . LYS A 59  ? 0.9932 0.5247 0.8372 0.1646  -0.1500 -0.2422 911  LYS A CE  
479  N NZ  . LYS A 59  ? 1.0251 0.5570 0.8470 0.2121  -0.1436 -0.2568 911  LYS A NZ  
480  N N   . ASN A 65  ? 1.2265 0.6146 1.3010 -0.2566 -0.3167 0.0672  917  ASN A N   
481  C CA  . ASN A 65  ? 1.1279 0.6199 1.2392 -0.2707 -0.2942 0.0909  917  ASN A CA  
482  C C   . ASN A 65  ? 1.0304 0.5829 1.1561 -0.2364 -0.2570 0.0906  917  ASN A C   
483  O O   . ASN A 65  ? 1.0100 0.6290 1.1655 -0.2460 -0.2423 0.1202  917  ASN A O   
484  C CB  . ASN A 65  ? 1.1491 0.6663 1.2892 -0.3180 -0.3115 0.1367  917  ASN A CB  
485  C CG  . ASN A 65  ? 1.1853 0.6716 1.3326 -0.3225 -0.3186 0.1632  917  ASN A CG  
486  O OD1 . ASN A 65  ? 1.2179 0.6411 1.3425 -0.2935 -0.3194 0.1447  917  ASN A OD1 
487  N ND2 . ASN A 65  ? 1.1767 0.7123 1.3556 -0.3576 -0.3236 0.2077  917  ASN A ND2 
488  N N   . HIS A 66  ? 0.9833 0.5149 1.0860 -0.1966 -0.2428 0.0568  918  HIS A N   
489  C CA  . HIS A 66  ? 0.8716 0.4555 0.9831 -0.1650 -0.2099 0.0527  918  HIS A CA  
490  C C   . HIS A 66  ? 0.7707 0.4309 0.8954 -0.1631 -0.1877 0.0501  918  HIS A C   
491  O O   . HIS A 66  ? 0.6799 0.3873 0.8130 -0.1430 -0.1622 0.0504  918  HIS A O   
492  C CB  . HIS A 66  ? 0.8875 0.4277 0.9701 -0.1251 -0.2042 0.0203  918  HIS A CB  
493  C CG  . HIS A 66  ? 0.9685 0.4301 1.0331 -0.1182 -0.2249 0.0194  918  HIS A CG  
494  N ND1 . HIS A 66  ? 0.9677 0.4288 1.0456 -0.1155 -0.2217 0.0427  918  HIS A ND1 
495  C CD2 . HIS A 66  ? 1.0476 0.4255 1.0791 -0.1115 -0.2502 -0.0022 918  HIS A CD2 
496  C CE1 . HIS A 66  ? 1.0444 0.4238 1.0992 -0.1075 -0.2440 0.0370  918  HIS A CE1 
497  N NE2 . HIS A 66  ? 1.0964 0.4215 1.1213 -0.1040 -0.2621 0.0087  918  HIS A NE2 
498  N N   . ILE A 67  ? 0.7381 0.4066 0.8619 -0.1835 -0.1991 0.0471  919  ILE A N   
499  C CA  . ILE A 67  ? 0.6527 0.3942 0.7917 -0.1873 -0.1827 0.0525  919  ILE A CA  
500  C C   . ILE A 67  ? 0.5604 0.3657 0.7295 -0.1967 -0.1694 0.0862  919  ILE A C   
501  O O   . ILE A 67  ? 0.4670 0.3275 0.6435 -0.1807 -0.1461 0.0866  919  ILE A O   
502  C CB  . ILE A 67  ? 0.6934 0.4357 0.8304 -0.2141 -0.2022 0.0515  919  ILE A CB  
503  C CG1 . ILE A 67  ? 0.7868 0.4680 0.8900 -0.2023 -0.2155 0.0154  919  ILE A CG1 
504  C CG2 . ILE A 67  ? 0.6678 0.4888 0.8205 -0.2144 -0.1848 0.0592  919  ILE A CG2 
505  C CD1 . ILE A 67  ? 0.8608 0.4626 0.9455 -0.2212 -0.2491 0.0108  919  ILE A CD1 
506  N N   . ALA A 68  ? 0.5413 0.3375 0.7252 -0.2222 -0.1854 0.1147  920  ALA A N   
507  C CA  . ALA A 68  ? 0.5146 0.3731 0.7261 -0.2305 -0.1739 0.1488  920  ALA A CA  
508  C C   . ALA A 68  ? 0.4893 0.3646 0.7001 -0.1992 -0.1492 0.1440  920  ALA A C   
509  O O   . ALA A 68  ? 0.4466 0.3861 0.6701 -0.1903 -0.1295 0.1549  920  ALA A O   
510  C CB  . ALA A 68  ? 0.5703 0.4091 0.7954 -0.2642 -0.1977 0.1809  920  ALA A CB  
511  N N   . ASP A 69  ? 0.4941 0.3123 0.6882 -0.1816 -0.1513 0.1276  921  ASP A N   
512  C CA  . ASP A 69  ? 0.4699 0.3037 0.6618 -0.1529 -0.1296 0.1218  921  ASP A CA  
513  C C   . ASP A 69  ? 0.4007 0.2688 0.5836 -0.1299 -0.1075 0.0993  921  ASP A C   
514  O O   . ASP A 69  ? 0.3695 0.2818 0.5587 -0.1172 -0.0884 0.1050  921  ASP A O   
515  C CB  . ASP A 69  ? 0.5165 0.2853 0.6909 -0.1360 -0.1371 0.1077  921  ASP A CB  
516  C CG  . ASP A 69  ? 0.6267 0.3566 0.8080 -0.1555 -0.1582 0.1327  921  ASP A CG  
517  O OD1 . ASP A 69  ? 0.6270 0.3968 0.8316 -0.1777 -0.1596 0.1659  921  ASP A OD1 
518  O OD2 . ASP A 69  ? 0.6266 0.2857 0.7883 -0.1470 -0.1739 0.1195  921  ASP A OD2 
519  N N   . LEU A 70  ? 0.3907 0.2364 0.5569 -0.1250 -0.1115 0.0743  922  LEU A N   
520  C CA  . LEU A 70  ? 0.3721 0.2479 0.5291 -0.1064 -0.0929 0.0559  922  LEU A CA  
521  C C   . LEU A 70  ? 0.3239 0.2615 0.4957 -0.1135 -0.0823 0.0722  922  LEU A C   
522  O O   . LEU A 70  ? 0.3272 0.2952 0.4948 -0.0969 -0.0643 0.0668  922  LEU A O   
523  C CB  . LEU A 70  ? 0.4028 0.2485 0.5398 -0.1020 -0.1004 0.0293  922  LEU A CB  
524  C CG  . LEU A 70  ? 0.3792 0.2536 0.5057 -0.0854 -0.0835 0.0124  922  LEU A CG  
525  C CD1 . LEU A 70  ? 0.3481 0.2296 0.4677 -0.0627 -0.0663 0.0048  922  LEU A CD1 
526  C CD2 . LEU A 70  ? 0.4686 0.3163 0.5764 -0.0836 -0.0932 -0.0107 922  LEU A CD2 
527  N N   . LYS A 71  ? 0.3245 0.2798 0.5115 -0.1377 -0.0949 0.0921  923  LYS A N   
528  C CA  . LYS A 71  ? 0.2883 0.3084 0.4895 -0.1418 -0.0858 0.1098  923  LYS A CA  
529  C C   . LYS A 71  ? 0.2478 0.3074 0.4591 -0.1317 -0.0709 0.1272  923  LYS A C   
530  O O   . LYS A 71  ? 0.2094 0.3092 0.4177 -0.1158 -0.0551 0.1259  923  LYS A O   
531  C CB  . LYS A 71  ? 0.3404 0.3788 0.5580 -0.1721 -0.1040 0.1312  923  LYS A CB  
532  C CG  . LYS A 71  ? 0.4201 0.4426 0.6268 -0.1790 -0.1145 0.1139  923  LYS A CG  
533  C CD  . LYS A 71  ? 0.5064 0.5413 0.7286 -0.2141 -0.1368 0.1360  923  LYS A CD  
534  C CE  . LYS A 71  ? 0.5714 0.6167 0.7866 -0.2194 -0.1431 0.1237  923  LYS A CE  
535  N NZ  . LYS A 71  ? 0.5701 0.5580 0.7580 -0.2050 -0.1456 0.0880  923  LYS A NZ  
536  N N   . LYS A 72  ? 0.3105 0.3546 0.5305 -0.1388 -0.0765 0.1420  924  LYS A N   
537  C CA  . LYS A 72  ? 0.2814 0.3623 0.5095 -0.1288 -0.0631 0.1581  924  LYS A CA  
538  C C   . LYS A 72  ? 0.2569 0.3302 0.4669 -0.1011 -0.0457 0.1356  924  LYS A C   
539  O O   . LYS A 72  ? 0.2545 0.3680 0.4628 -0.0876 -0.0312 0.1395  924  LYS A O   
540  C CB  . LYS A 72  ? 0.3335 0.3981 0.5748 -0.1442 -0.0747 0.1812  924  LYS A CB  
541  C CG  . LYS A 72  ? 0.4124 0.4942 0.6736 -0.1763 -0.0925 0.2107  924  LYS A CG  
542  C CD  . LYS A 72  ? 0.5363 0.6089 0.8116 -0.1931 -0.1038 0.2401  924  LYS A CD  
543  C CE  . LYS A 72  ? 0.5875 0.7394 0.8827 -0.1957 -0.0930 0.2727  924  LYS A CE  
544  N NZ  . LYS A 72  ? 0.5184 0.7051 0.8038 -0.1633 -0.0682 0.2591  924  LYS A NZ  
545  N N   . GLU A 73  ? 0.2711 0.2945 0.4662 -0.0927 -0.0483 0.1127  925  GLU A N   
546  C CA  . GLU A 73  ? 0.2388 0.2565 0.4169 -0.0707 -0.0343 0.0921  925  GLU A CA  
547  C C   . GLU A 73  ? 0.1934 0.2368 0.3605 -0.0610 -0.0231 0.0809  925  GLU A C   
548  O O   . GLU A 73  ? 0.2237 0.2857 0.3821 -0.0476 -0.0106 0.0777  925  GLU A O   
549  C CB  . GLU A 73  ? 0.2820 0.2500 0.4465 -0.0639 -0.0405 0.0705  925  GLU A CB  
550  C CG  . GLU A 73  ? 0.2405 0.2085 0.3898 -0.0440 -0.0275 0.0532  925  GLU A CG  
551  C CD  . GLU A 73  ? 0.3273 0.2566 0.4633 -0.0339 -0.0328 0.0335  925  GLU A CD  
552  O OE1 . GLU A 73  ? 0.3131 0.2062 0.4484 -0.0397 -0.0476 0.0311  925  GLU A OE1 
553  O OE2 . GLU A 73  ? 0.3465 0.2829 0.4709 -0.0196 -0.0228 0.0208  925  GLU A OE2 
554  N N   . ILE A 74  ? 0.2125 0.2529 0.3775 -0.0678 -0.0292 0.0744  926  ILE A N   
555  C CA  . ILE A 74  ? 0.1887 0.2509 0.3427 -0.0585 -0.0207 0.0658  926  ILE A CA  
556  C C   . ILE A 74  ? 0.1729 0.2815 0.3315 -0.0517 -0.0114 0.0818  926  ILE A C   
557  O O   . ILE A 74  ? 0.1691 0.2872 0.3120 -0.0357 -0.0009 0.0736  926  ILE A O   
558  C CB  . ILE A 74  ? 0.1928 0.2530 0.3478 -0.0691 -0.0306 0.0618  926  ILE A CB  
559  C CG1 . ILE A 74  ? 0.2581 0.2753 0.3991 -0.0676 -0.0364 0.0393  926  ILE A CG1 
560  C CG2 . ILE A 74  ? 0.1546 0.2468 0.3018 -0.0588 -0.0222 0.0605  926  ILE A CG2 
561  C CD1 . ILE A 74  ? 0.2568 0.2635 0.3985 -0.0810 -0.0503 0.0351  926  ILE A CD1 
562  N N   . GLU A 75  ? 0.1844 0.3219 0.3629 -0.0638 -0.0166 0.1053  927  GLU A N   
563  C CA  . GLU A 75  ? 0.1588 0.3498 0.3420 -0.0553 -0.0081 0.1220  927  GLU A CA  
564  C C   . GLU A 75  ? 0.1761 0.3730 0.3513 -0.0410 0.0024  0.1224  927  GLU A C   
565  O O   . GLU A 75  ? 0.1597 0.3856 0.3230 -0.0233 0.0123  0.1223  927  GLU A O   
566  C CB  . GLU A 75  ? 0.1891 0.4169 0.3979 -0.0756 -0.0178 0.1506  927  GLU A CB  
567  C CG  . GLU A 75  ? 0.2209 0.5163 0.4362 -0.0660 -0.0096 0.1702  927  GLU A CG  
568  C CD  . GLU A 75  ? 0.1149 0.4315 0.3143 -0.0456 -0.0016 0.1586  927  GLU A CD  
569  O OE1 . GLU A 75  ? 0.1695 0.4542 0.3582 -0.0456 -0.0049 0.1401  927  GLU A OE1 
570  O OE2 . GLU A 75  ? 0.2149 0.5812 0.4104 -0.0270 0.0080  0.1683  927  GLU A OE2 
571  N N   . ILE A 76  ? 0.1926 0.3612 0.3718 -0.0469 -0.0007 0.1222  928  ILE A N   
572  C CA  . ILE A 76  ? 0.1691 0.3398 0.3391 -0.0343 0.0081  0.1198  928  ILE A CA  
573  C C   . ILE A 76  ? 0.1916 0.3449 0.3350 -0.0182 0.0162  0.0956  928  ILE A C   
574  O O   . ILE A 76  ? 0.1779 0.3505 0.3066 -0.0041 0.0241  0.0938  928  ILE A O   
575  C CB  . ILE A 76  ? 0.1791 0.3195 0.3570 -0.0416 0.0026  0.1223  928  ILE A CB  
576  C CG1 . ILE A 76  ? 0.2352 0.3930 0.4365 -0.0574 -0.0057 0.1508  928  ILE A CG1 
577  C CG2 . ILE A 76  ? 0.1970 0.3390 0.3625 -0.0281 0.0117  0.1158  928  ILE A CG2 
578  C CD1 . ILE A 76  ? 0.2616 0.3777 0.4701 -0.0660 -0.0162 0.1543  928  ILE A CD1 
579  N N   . LEU A 77  ? 0.1676 0.2844 0.3029 -0.0207 0.0128  0.0779  929  LEU A N   
580  C CA  . LEU A 77  ? 0.1750 0.2738 0.2863 -0.0103 0.0184  0.0582  929  LEU A CA  
581  C C   . LEU A 77  ? 0.1858 0.2963 0.2803 0.0004  0.0223  0.0533  929  LEU A C   
582  O O   . LEU A 77  ? 0.2170 0.3202 0.2893 0.0107  0.0268  0.0440  929  LEU A O   
583  C CB  . LEU A 77  ? 0.1749 0.2405 0.2821 -0.0149 0.0142  0.0429  929  LEU A CB  
584  C CG  . LEU A 77  ? 0.1337 0.1849 0.2191 -0.0086 0.0189  0.0273  929  LEU A CG  
585  C CD1 . LEU A 77  ? 0.1977 0.2556 0.2770 -0.0048 0.0235  0.0296  929  LEU A CD1 
586  C CD2 . LEU A 77  ? 0.2242 0.2535 0.3078 -0.0117 0.0153  0.0150  929  LEU A CD2 
587  N N   . ARG A 78  ? 0.2233 0.3514 0.3272 -0.0019 0.0193  0.0606  930  ARG A N   
588  C CA  . ARG A 78  ? 0.2053 0.3507 0.2952 0.0119  0.0227  0.0592  930  ARG A CA  
589  C C   . ARG A 78  ? 0.2231 0.3896 0.2975 0.0302  0.0298  0.0623  930  ARG A C   
590  O O   . ARG A 78  ? 0.2581 0.4156 0.3060 0.0472  0.0325  0.0517  930  ARG A O   
591  C CB  . ARG A 78  ? 0.2381 0.4147 0.3476 0.0049  0.0180  0.0733  930  ARG A CB  
592  C CG  . ARG A 78  ? 0.2513 0.4446 0.3469 0.0204  0.0206  0.0707  930  ARG A CG  
593  C CD  . ARG A 78  ? 0.2532 0.4780 0.3700 0.0093  0.0142  0.0843  930  ARG A CD  
594  N NE  . ARG A 78  ? 0.1707 0.4523 0.3053 0.0103  0.0159  0.1080  930  ARG A NE  
595  C CZ  . ARG A 78  ? 0.2138 0.5370 0.3386 0.0337  0.0234  0.1147  930  ARG A CZ  
596  N NH1 . ARG A 78  ? 0.2662 0.6499 0.4095 0.0335  0.0250  0.1388  930  ARG A NH1 
597  N NH2 . ARG A 78  ? 0.2220 0.5267 0.3167 0.0583  0.0285  0.0981  930  ARG A NH2 
598  N N   . ASN A 79  ? 0.2232 0.4148 0.3114 0.0278  0.0317  0.0764  931  ASN A N   
599  C CA  . ASN A 79  ? 0.2215 0.4406 0.2958 0.0460  0.0381  0.0807  931  ASN A CA  
600  C C   . ASN A 79  ? 0.2324 0.4316 0.2914 0.0483  0.0401  0.0721  931  ASN A C   
601  O O   . ASN A 79  ? 0.2322 0.4540 0.2786 0.0628  0.0443  0.0751  931  ASN A O   
602  C CB  . ASN A 79  ? 0.2552 0.5303 0.3554 0.0426  0.0390  0.1066  931  ASN A CB  
603  C CG  . ASN A 79  ? 0.2714 0.5791 0.3835 0.0429  0.0372  0.1173  931  ASN A CG  
604  O OD1 . ASN A 79  ? 0.3579 0.6779 0.4505 0.0644  0.0412  0.1106  931  ASN A OD1 
605  N ND2 . ASN A 79  ? 0.2129 0.5311 0.3548 0.0190  0.0296  0.1332  931  ASN A ND2 
606  N N   . LEU A 80  ? 0.2360 0.3980 0.2954 0.0353  0.0369  0.0619  932  LEU A N   
607  C CA  . LEU A 80  ? 0.2382 0.3828 0.2819 0.0357  0.0377  0.0533  932  LEU A CA  
608  C C   . LEU A 80  ? 0.2737 0.3833 0.2841 0.0417  0.0359  0.0340  932  LEU A C   
609  O O   . LEU A 80  ? 0.2548 0.3411 0.2632 0.0358  0.0330  0.0262  932  LEU A O   
610  C CB  . LEU A 80  ? 0.2015 0.3330 0.2639 0.0202  0.0352  0.0555  932  LEU A CB  
611  C CG  . LEU A 80  ? 0.2146 0.3687 0.3069 0.0123  0.0341  0.0753  932  LEU A CG  
612  C CD1 . LEU A 80  ? 0.2220 0.3529 0.3264 0.0023  0.0303  0.0735  932  LEU A CD1 
613  C CD2 . LEU A 80  ? 0.2522 0.4404 0.3449 0.0193  0.0381  0.0886  932  LEU A CD2 
614  N N   . TYR A 81  ? 0.2868 0.3921 0.2695 0.0530  0.0361  0.0274  933  TYR A N   
615  C CA  . TYR A 81  ? 0.3343 0.3997 0.2797 0.0572  0.0311  0.0104  933  TYR A CA  
616  C C   . TYR A 81  ? 0.2821 0.3368 0.2111 0.0511  0.0279  0.0052  933  TYR A C   
617  O O   . TYR A 81  ? 0.2941 0.3605 0.2068 0.0635  0.0284  0.0046  933  TYR A O   
618  C CB  . TYR A 81  ? 0.4106 0.4746 0.3278 0.0817  0.0312  0.0049  933  TYR A CB  
619  C CG  . TYR A 81  ? 0.4769 0.5566 0.4063 0.0903  0.0337  0.0104  933  TYR A CG  
620  C CD1 . TYR A 81  ? 0.6126 0.6592 0.5270 0.0911  0.0295  0.0012  933  TYR A CD1 
621  C CD2 . TYR A 81  ? 0.5491 0.6806 0.5049 0.0969  0.0396  0.0269  933  TYR A CD2 
622  C CE1 . TYR A 81  ? 0.5783 0.6436 0.5038 0.0995  0.0315  0.0070  933  TYR A CE1 
623  C CE2 . TYR A 81  ? 0.5157 0.6680 0.4837 0.1028  0.0408  0.0339  933  TYR A CE2 
624  C CZ  . TYR A 81  ? 0.5778 0.6971 0.5306 0.1048  0.0370  0.0231  933  TYR A CZ  
625  O OH  . TYR A 81  ? 0.6338 0.7774 0.5986 0.1107  0.0378  0.0305  933  TYR A OH  
626  N N   . HIS A 82  ? 0.2819 0.3186 0.2139 0.0326  0.0243  0.0020  934  HIS A N   
627  C CA  . HIS A 82  ? 0.2353 0.2673 0.1540 0.0229  0.0201  -0.0009 934  HIS A CA  
628  C C   . HIS A 82  ? 0.2156 0.2243 0.1287 0.0033  0.0142  -0.0058 934  HIS A C   
629  O O   . HIS A 82  ? 0.2436 0.2534 0.1760 -0.0034 0.0165  -0.0036 934  HIS A O   
630  C CB  . HIS A 82  ? 0.2373 0.3074 0.1847 0.0207  0.0256  0.0122  934  HIS A CB  
631  C CG  . HIS A 82  ? 0.1950 0.2710 0.1284 0.0153  0.0220  0.0113  934  HIS A CG  
632  N ND1 . HIS A 82  ? 0.2079 0.2807 0.1429 -0.0019 0.0179  0.0109  934  HIS A ND1 
633  C CD2 . HIS A 82  ? 0.2816 0.3708 0.1982 0.0250  0.0213  0.0110  934  HIS A CD2 
634  C CE1 . HIS A 82  ? 0.2692 0.3525 0.1903 -0.0045 0.0143  0.0110  934  HIS A CE1 
635  N NE2 . HIS A 82  ? 0.2750 0.3658 0.1834 0.0119  0.0160  0.0100  934  HIS A NE2 
636  N N   . GLU A 83  ? 0.2878 0.2767 0.1720 -0.0059 0.0056  -0.0121 935  GLU A N   
637  C CA  . GLU A 83  ? 0.3250 0.2968 0.1998 -0.0276 -0.0020 -0.0137 935  GLU A CA  
638  C C   . GLU A 83  ? 0.2648 0.2710 0.1738 -0.0388 0.0036  -0.0041 935  GLU A C   
639  O O   . GLU A 83  ? 0.2724 0.2769 0.1847 -0.0517 0.0016  -0.0029 935  GLU A O   
640  C CB  . GLU A 83  ? 0.3826 0.3355 0.2234 -0.0381 -0.0138 -0.0189 935  GLU A CB  
641  C CG  . GLU A 83  ? 0.5694 0.5074 0.3973 -0.0651 -0.0246 -0.0173 935  GLU A CG  
642  C CD  . GLU A 83  ? 0.6806 0.5871 0.4672 -0.0779 -0.0407 -0.0237 935  GLU A CD  
643  O OE1 . GLU A 83  ? 0.7459 0.6593 0.5221 -0.0682 -0.0414 -0.0277 935  GLU A OE1 
644  O OE2 . GLU A 83  ? 0.8438 0.7180 0.6069 -0.0991 -0.0540 -0.0240 935  GLU A OE2 
645  N N   . ASN A 84  ? 0.2271 0.2656 0.1589 -0.0322 0.0101  0.0034  936  ASN A N   
646  C CA  . ASN A 84  ? 0.1778 0.2468 0.1396 -0.0362 0.0152  0.0121  936  ASN A CA  
647  C C   . ASN A 84  ? 0.1755 0.2536 0.1667 -0.0244 0.0227  0.0165  936  ASN A C   
648  O O   . ASN A 84  ? 0.1284 0.2280 0.1419 -0.0218 0.0263  0.0239  936  ASN A O   
649  C CB  . ASN A 84  ? 0.1900 0.2859 0.1549 -0.0386 0.0147  0.0191  936  ASN A CB  
650  C CG  . ASN A 84  ? 0.2364 0.3220 0.1705 -0.0542 0.0042  0.0147  936  ASN A CG  
651  O OD1 . ASN A 84  ? 0.2603 0.3434 0.1763 -0.0515 0.0003  0.0122  936  ASN A OD1 
652  N ND2 . ASN A 84  ? 0.1836 0.2642 0.1103 -0.0716 -0.0015 0.0145  936  ASN A ND2 
653  N N   A ILE A 85  ? 0.1741 0.2347 0.1632 -0.0174 0.0237  0.0123  937  ILE A N   
654  N N   B ILE A 85  ? 0.1722 0.2324 0.1611 -0.0176 0.0236  0.0122  937  ILE A N   
655  C CA  A ILE A 85  ? 0.1794 0.2431 0.1925 -0.0113 0.0275  0.0155  937  ILE A CA  
656  C CA  B ILE A 85  ? 0.1765 0.2402 0.1896 -0.0112 0.0275  0.0156  937  ILE A CA  
657  C C   A ILE A 85  ? 0.1696 0.2131 0.1750 -0.0139 0.0256  0.0073  937  ILE A C   
658  C C   B ILE A 85  ? 0.1659 0.2095 0.1715 -0.0138 0.0256  0.0073  937  ILE A C   
659  O O   A ILE A 85  ? 0.1723 0.1974 0.1557 -0.0134 0.0227  0.0015  937  ILE A O   
660  O O   B ILE A 85  ? 0.1660 0.1912 0.1498 -0.0129 0.0228  0.0016  937  ILE A O   
661  C CB  A ILE A 85  ? 0.1858 0.2590 0.2080 -0.0013 0.0301  0.0228  937  ILE A CB  
662  C CB  B ILE A 85  ? 0.1828 0.2554 0.2033 -0.0011 0.0300  0.0224  937  ILE A CB  
663  C CG1 A ILE A 85  ? 0.2123 0.3098 0.2462 0.0007  0.0321  0.0339  937  ILE A CG1 
664  C CG1 B ILE A 85  ? 0.2013 0.2976 0.2282 0.0018  0.0319  0.0324  937  ILE A CG1 
665  C CG2 A ILE A 85  ? 0.1786 0.2493 0.2210 0.0002  0.0304  0.0258  937  ILE A CG2 
666  C CG2 B ILE A 85  ? 0.1821 0.2553 0.2259 0.0004  0.0307  0.0271  937  ILE A CG2 
667  C CD1 A ILE A 85  ? 0.2195 0.3359 0.2682 0.0078  0.0346  0.0465  937  ILE A CD1 
668  C CD1 B ILE A 85  ? 0.2157 0.3258 0.2662 -0.0005 0.0330  0.0416  937  ILE A CD1 
669  N N   . VAL A 86  ? 0.1789 0.2247 0.2002 -0.0149 0.0265  0.0063  938  VAL A N   
670  C CA  . VAL A 86  ? 0.1836 0.2156 0.1987 -0.0173 0.0249  -0.0010 938  VAL A CA  
671  C C   . VAL A 86  ? 0.2047 0.2244 0.2152 -0.0118 0.0241  -0.0025 938  VAL A C   
672  O O   . VAL A 86  ? 0.1878 0.2161 0.2110 -0.0059 0.0254  0.0036  938  VAL A O   
673  C CB  . VAL A 86  ? 0.1774 0.2151 0.2091 -0.0150 0.0256  -0.0033 938  VAL A CB  
674  C CG1 . VAL A 86  ? 0.1675 0.2019 0.2183 -0.0090 0.0248  0.0002  938  VAL A CG1 
675  C CG2 . VAL A 86  ? 0.1579 0.1882 0.1795 -0.0184 0.0241  -0.0109 938  VAL A CG2 
676  N N   . LYS A 87  ? 0.2238 0.2272 0.2161 -0.0140 0.0215  -0.0083 939  LYS A N   
677  C CA  . LYS A 87  ? 0.2523 0.2463 0.2362 -0.0059 0.0206  -0.0092 939  LYS A CA  
678  C C   . LYS A 87  ? 0.2164 0.2168 0.2178 -0.0040 0.0207  -0.0089 939  LYS A C   
679  O O   . LYS A 87  ? 0.2095 0.2054 0.2122 -0.0088 0.0192  -0.0137 939  LYS A O   
680  C CB  . LYS A 87  ? 0.2515 0.2201 0.2052 -0.0072 0.0161  -0.0144 939  LYS A CB  
681  C CG  . LYS A 87  ? 0.3102 0.2637 0.2391 -0.0078 0.0125  -0.0158 939  LYS A CG  
682  C CD  . LYS A 87  ? 0.4976 0.4158 0.3934 -0.0109 0.0047  -0.0203 939  LYS A CD  
683  C CE  . LYS A 87  ? 0.5431 0.4365 0.4079 -0.0099 -0.0021 -0.0239 939  LYS A CE  
684  N NZ  . LYS A 87  ? 0.5983 0.4476 0.4274 -0.0154 -0.0130 -0.0275 939  LYS A NZ  
685  N N   . TYR A 88  ? 0.2083 0.2223 0.2219 0.0025  0.0217  -0.0022 940  TYR A N   
686  C CA  . TYR A 88  ? 0.1955 0.2165 0.2204 0.0032  0.0196  -0.0003 940  TYR A CA  
687  C C   . TYR A 88  ? 0.2029 0.2118 0.2076 0.0083  0.0181  -0.0059 940  TYR A C   
688  O O   . TYR A 88  ? 0.2163 0.2155 0.1991 0.0176  0.0186  -0.0070 940  TYR A O   
689  C CB  . TYR A 88  ? 0.2126 0.2591 0.2519 0.0084  0.0208  0.0119  940  TYR A CB  
690  C CG  . TYR A 88  ? 0.1760 0.2383 0.2275 0.0075  0.0176  0.0175  940  TYR A CG  
691  C CD1 . TYR A 88  ? 0.1866 0.2532 0.2607 -0.0052 0.0119  0.0222  940  TYR A CD1 
692  C CD2 . TYR A 88  ? 0.2167 0.2898 0.2558 0.0199  0.0188  0.0189  940  TYR A CD2 
693  C CE1 . TYR A 88  ? 0.2091 0.2917 0.2942 -0.0099 0.0068  0.0283  940  TYR A CE1 
694  C CE2 . TYR A 88  ? 0.1799 0.2755 0.2320 0.0184  0.0156  0.0261  940  TYR A CE2 
695  C CZ  . TYR A 88  ? 0.2307 0.3329 0.3071 0.0012  0.0092  0.0315  940  TYR A CZ  
696  O OH  . TYR A 88  ? 0.1573 0.2830 0.2471 -0.0049 0.0036  0.0397  940  TYR A OH  
697  N N   . LYS A 89  ? 0.2052 0.2121 0.2149 0.0034  0.0151  -0.0096 941  LYS A N   
698  C CA  . LYS A 89  ? 0.2206 0.2205 0.2146 0.0086  0.0132  -0.0123 941  LYS A CA  
699  C C   . LYS A 89  ? 0.2329 0.2544 0.2418 0.0111  0.0110  -0.0067 941  LYS A C   
700  O O   . LYS A 89  ? 0.2208 0.2483 0.2192 0.0224  0.0110  -0.0036 941  LYS A O   
701  C CB  . LYS A 89  ? 0.2484 0.2344 0.2330 0.0005  0.0111  -0.0197 941  LYS A CB  
702  C CG  . LYS A 89  ? 0.2762 0.2454 0.2426 -0.0040 0.0117  -0.0215 941  LYS A CG  
703  C CD  . LYS A 89  ? 0.3364 0.3022 0.2952 -0.0134 0.0100  -0.0250 941  LYS A CD  
704  C CE  . LYS A 89  ? 0.3927 0.3434 0.3302 -0.0126 0.0062  -0.0238 941  LYS A CE  
705  N NZ  . LYS A 89  ? 0.3742 0.2969 0.2850 -0.0104 0.0026  -0.0208 941  LYS A NZ  
706  N N   . GLY A 90  ? 0.2107 0.2433 0.2424 0.0009  0.0077  -0.0047 942  GLY A N   
707  C CA  . GLY A 90  ? 0.1736 0.2290 0.2207 -0.0019 0.0031  0.0028  942  GLY A CA  
708  C C   . GLY A 90  ? 0.1800 0.2335 0.2454 -0.0170 -0.0048 0.0015  942  GLY A C   
709  O O   . GLY A 90  ? 0.2059 0.2436 0.2766 -0.0223 -0.0058 -0.0022 942  GLY A O   
710  N N   . ILE A 91  ? 0.2159 0.2835 0.2882 -0.0228 -0.0117 0.0043  943  ILE A N   
711  C CA  . ILE A 91  ? 0.1957 0.2565 0.2811 -0.0388 -0.0232 0.0022  943  ILE A CA  
712  C C   . ILE A 91  ? 0.2112 0.2707 0.2883 -0.0416 -0.0295 -0.0071 943  ILE A C   
713  O O   . ILE A 91  ? 0.1983 0.2741 0.2669 -0.0332 -0.0260 -0.0050 943  ILE A O   
714  C CB  . ILE A 91  ? 0.1855 0.2710 0.2938 -0.0515 -0.0303 0.0206  943  ILE A CB  
715  C CG1 . ILE A 91  ? 0.1977 0.3275 0.3107 -0.0455 -0.0274 0.0350  943  ILE A CG1 
716  C CG2 . ILE A 91  ? 0.1849 0.2675 0.3025 -0.0518 -0.0263 0.0292  943  ILE A CG2 
717  C CD1 . ILE A 91  ? 0.2475 0.4134 0.3848 -0.0613 -0.0357 0.0562  943  ILE A CD1 
718  N N   . CYS A 92  ? 0.2661 0.3046 0.3439 -0.0520 -0.0399 -0.0174 944  CYS A N   
719  C CA  . CYS A 92  ? 0.2819 0.3214 0.3537 -0.0581 -0.0495 -0.0257 944  CYS A CA  
720  C C   . CYS A 92  ? 0.3007 0.3368 0.3873 -0.0780 -0.0659 -0.0200 944  CYS A C   
721  O O   . CYS A 92  ? 0.3262 0.3318 0.4139 -0.0838 -0.0729 -0.0254 944  CYS A O   
722  C CB  . CYS A 92  ? 0.3037 0.3182 0.3565 -0.0511 -0.0491 -0.0460 944  CYS A CB  
723  S SG  . CYS A 92  ? 0.3527 0.3662 0.3955 -0.0582 -0.0628 -0.0588 944  CYS A SG  
724  N N   . THR A 93  ? 0.3522 0.4202 0.4495 -0.0885 -0.0728 -0.0073 945  THR A N   
725  C CA  . THR A 93  ? 0.4135 0.4833 0.5258 -0.1134 -0.0913 0.0025  945  THR A CA  
726  C C   . THR A 93  ? 0.4698 0.5282 0.5711 -0.1243 -0.1069 -0.0110 945  THR A C   
727  O O   . THR A 93  ? 0.5186 0.6032 0.6138 -0.1184 -0.1040 -0.0126 945  THR A O   
728  C CB  . THR A 93  ? 0.4055 0.5294 0.5402 -0.1215 -0.0905 0.0302  945  THR A CB  
729  O OG1 . THR A 93  ? 0.4301 0.5917 0.5598 -0.1044 -0.0793 0.0334  945  THR A OG1 
730  C CG2 . THR A 93  ? 0.3691 0.4999 0.5161 -0.1175 -0.0815 0.0445  945  THR A CG2 
731  N N   . ASN A 98  ? 0.6873 0.6981 0.8509 -0.2706 -0.2090 0.0615  950  ASN A N   
732  C CA  . ASN A 98  ? 0.6990 0.6637 0.8645 -0.2751 -0.2140 0.0671  950  ASN A CA  
733  C C   . ASN A 98  ? 0.6769 0.6082 0.8268 -0.2386 -0.1931 0.0452  950  ASN A C   
734  O O   . ASN A 98  ? 0.6669 0.6041 0.8285 -0.2310 -0.1815 0.0585  950  ASN A O   
735  C CB  . ASN A 98  ? 0.7892 0.6842 0.9406 -0.3041 -0.2477 0.0607  950  ASN A CB  
736  C CG  . ASN A 98  ? 0.8208 0.6637 0.9384 -0.2950 -0.2592 0.0238  950  ASN A CG  
737  O OD1 . ASN A 98  ? 0.7918 0.6567 0.8987 -0.2693 -0.2419 0.0047  950  ASN A OD1 
738  N ND2 . ASN A 98  ? 0.8936 0.6649 0.9917 -0.3155 -0.2897 0.0135  950  ASN A ND2 
739  N N   . GLY A 99  ? 0.6281 0.5302 0.7521 -0.2172 -0.1889 0.0133  951  GLY A N   
740  C CA  . GLY A 99  ? 0.5741 0.4489 0.6821 -0.1847 -0.1713 -0.0074 951  GLY A CA  
741  C C   . GLY A 99  ? 0.4941 0.4207 0.6109 -0.1621 -0.1428 -0.0015 951  GLY A C   
742  O O   . GLY A 99  ? 0.4734 0.4537 0.6030 -0.1655 -0.1358 0.0129  951  GLY A O   
743  N N   . ILE A 100 ? 0.4171 0.3264 0.5250 -0.1385 -0.1276 -0.0126 952  ILE A N   
744  C CA  . ILE A 100 ? 0.3597 0.3076 0.4722 -0.1191 -0.1034 -0.0075 952  ILE A CA  
745  C C   . ILE A 100 ? 0.3689 0.2924 0.4659 -0.0955 -0.0909 -0.0251 952  ILE A C   
746  O O   . ILE A 100 ? 0.3766 0.2603 0.4672 -0.0928 -0.0980 -0.0329 952  ILE A O   
747  C CB  . ILE A 100 ? 0.3458 0.3290 0.4821 -0.1266 -0.0974 0.0208  952  ILE A CB  
748  C CG1 . ILE A 100 ? 0.3152 0.3394 0.4520 -0.1074 -0.0760 0.0253  952  ILE A CG1 
749  C CG2 . ILE A 100 ? 0.3782 0.3311 0.5197 -0.1285 -0.1006 0.0269  952  ILE A CG2 
750  C CD1 . ILE A 100 ? 0.3709 0.4426 0.5282 -0.1122 -0.0709 0.0524  952  ILE A CD1 
751  N N   . LYS A 101 ? 0.3197 0.2678 0.4100 -0.0791 -0.0734 -0.0294 953  LYS A N   
752  C CA  . LYS A 101 ? 0.3258 0.2636 0.4042 -0.0600 -0.0606 -0.0409 953  LYS A CA  
753  C C   . LYS A 101 ? 0.2732 0.2390 0.3581 -0.0529 -0.0447 -0.0280 953  LYS A C   
754  O O   . LYS A 101 ? 0.2543 0.2481 0.3427 -0.0538 -0.0400 -0.0187 953  LYS A O   
755  C CB  . LYS A 101 ? 0.3013 0.2372 0.3595 -0.0488 -0.0576 -0.0601 953  LYS A CB  
756  C CG  . LYS A 101 ? 0.4029 0.3093 0.4490 -0.0519 -0.0737 -0.0766 953  LYS A CG  
757  C CD  . LYS A 101 ? 0.4094 0.3173 0.4339 -0.0378 -0.0702 -0.0961 953  LYS A CD  
758  C CE  . LYS A 101 ? 0.5109 0.3824 0.5191 -0.0367 -0.0877 -0.1155 953  LYS A CE  
759  N NZ  . LYS A 101 ? 0.5547 0.4330 0.5403 -0.0234 -0.0866 -0.1349 953  LYS A NZ  
760  N N   . LEU A 102 ? 0.2842 0.2419 0.3690 -0.0444 -0.0375 -0.0278 954  LEU A N   
761  C CA  . LEU A 102 ? 0.2292 0.2078 0.3147 -0.0371 -0.0238 -0.0191 954  LEU A CA  
762  C C   . LEU A 102 ? 0.2431 0.2237 0.3104 -0.0265 -0.0149 -0.0309 954  LEU A C   
763  O O   . LEU A 102 ? 0.2332 0.2019 0.2921 -0.0203 -0.0145 -0.0423 954  LEU A O   
764  C CB  . LEU A 102 ? 0.2388 0.2108 0.3326 -0.0350 -0.0216 -0.0119 954  LEU A CB  
765  C CG  . LEU A 102 ? 0.2308 0.2194 0.3220 -0.0272 -0.0093 -0.0061 954  LEU A CG  
766  C CD1 . LEU A 102 ? 0.2289 0.2429 0.3210 -0.0270 -0.0042 0.0046  954  LEU A CD1 
767  C CD2 . LEU A 102 ? 0.2837 0.2676 0.3859 -0.0270 -0.0098 0.0029  954  LEU A CD2 
768  N N   . ILE A 103 ? 0.2221 0.2184 0.2823 -0.0237 -0.0084 -0.0265 955  ILE A N   
769  C CA  . ILE A 103 ? 0.2302 0.2262 0.2719 -0.0176 -0.0018 -0.0334 955  ILE A CA  
770  C C   . ILE A 103 ? 0.2282 0.2268 0.2650 -0.0142 0.0057  -0.0273 955  ILE A C   
771  O O   . ILE A 103 ? 0.2245 0.2303 0.2631 -0.0120 0.0077  -0.0185 955  ILE A O   
772  C CB  . ILE A 103 ? 0.2288 0.2317 0.2599 -0.0165 -0.0022 -0.0331 955  ILE A CB  
773  C CG1 . ILE A 103 ? 0.2541 0.2605 0.2917 -0.0217 -0.0110 -0.0364 955  ILE A CG1 
774  C CG2 . ILE A 103 ? 0.2406 0.2392 0.2517 -0.0139 0.0017  -0.0384 955  ILE A CG2 
775  C CD1 . ILE A 103 ? 0.2668 0.2604 0.3018 -0.0233 -0.0167 -0.0500 955  ILE A CD1 
776  N N   . MET A 104 ? 0.2104 0.2062 0.2393 -0.0133 0.0091  -0.0319 956  MET A N   
777  C CA  . MET A 104 ? 0.1993 0.1971 0.2215 -0.0132 0.0139  -0.0270 956  MET A CA  
778  C C   . MET A 104 ? 0.1901 0.1869 0.1935 -0.0167 0.0153  -0.0297 956  MET A C   
779  O O   . MET A 104 ? 0.1941 0.1942 0.1926 -0.0176 0.0141  -0.0350 956  MET A O   
780  C CB  . MET A 104 ? 0.2297 0.2319 0.2641 -0.0119 0.0153  -0.0252 956  MET A CB  
781  C CG  . MET A 104 ? 0.1956 0.1968 0.2483 -0.0114 0.0124  -0.0187 956  MET A CG  
782  S SD  . MET A 104 ? 0.2143 0.2125 0.2791 -0.0075 0.0113  -0.0181 956  MET A SD  
783  C CE  . MET A 104 ? 0.2122 0.1953 0.2732 -0.0035 0.0049  -0.0326 956  MET A CE  
784  N N   . GLU A 105 ? 0.1777 0.1707 0.1693 -0.0198 0.0165  -0.0250 957  GLU A N   
785  C CA  . GLU A 105 ? 0.1840 0.1771 0.1590 -0.0285 0.0156  -0.0240 957  GLU A CA  
786  C C   . GLU A 105 ? 0.2083 0.2237 0.1927 -0.0298 0.0180  -0.0256 957  GLU A C   
787  O O   . GLU A 105 ? 0.2065 0.2303 0.2068 -0.0231 0.0202  -0.0270 957  GLU A O   
788  C CB  . GLU A 105 ? 0.2076 0.1886 0.1664 -0.0341 0.0136  -0.0193 957  GLU A CB  
789  C CG  . GLU A 105 ? 0.1990 0.1924 0.1684 -0.0338 0.0161  -0.0165 957  GLU A CG  
790  C CD  . GLU A 105 ? 0.2598 0.2406 0.2095 -0.0405 0.0122  -0.0135 957  GLU A CD  
791  O OE1 . GLU A 105 ? 0.2758 0.2346 0.2012 -0.0485 0.0059  -0.0132 957  GLU A OE1 
792  O OE2 . GLU A 105 ? 0.2362 0.2264 0.1928 -0.0381 0.0141  -0.0112 957  GLU A OE2 
793  N N   . PHE A 106 ? 0.1861 0.2129 0.1600 -0.0369 0.0173  -0.0242 958  PHE A N   
794  C CA  . PHE A 106 ? 0.1833 0.2414 0.1633 -0.0358 0.0204  -0.0241 958  PHE A CA  
795  C C   . PHE A 106 ? 0.2035 0.2781 0.1765 -0.0493 0.0196  -0.0137 958  PHE A C   
796  O O   . PHE A 106 ? 0.2494 0.3115 0.2053 -0.0643 0.0145  -0.0069 958  PHE A O   
797  C CB  . PHE A 106 ? 0.1878 0.2593 0.1626 -0.0336 0.0203  -0.0281 958  PHE A CB  
798  C CG  . PHE A 106 ? 0.1725 0.2838 0.1496 -0.0298 0.0240  -0.0271 958  PHE A CG  
799  C CD1 . PHE A 106 ? 0.2037 0.3277 0.1929 -0.0131 0.0273  -0.0342 958  PHE A CD1 
800  C CD2 . PHE A 106 ? 0.2182 0.3562 0.1843 -0.0416 0.0235  -0.0176 958  PHE A CD2 
801  C CE1 . PHE A 106 ? 0.2361 0.4019 0.2257 -0.0041 0.0313  -0.0335 958  PHE A CE1 
802  C CE2 . PHE A 106 ? 0.1945 0.3815 0.1637 -0.0363 0.0279  -0.0145 958  PHE A CE2 
803  C CZ  . PHE A 106 ? 0.2388 0.4408 0.2191 -0.0149 0.0324  -0.0237 958  PHE A CZ  
804  N N   . LEU A 107 ? 0.1949 0.2952 0.1799 -0.0444 0.0232  -0.0118 959  LEU A N   
805  C CA  . LEU A 107 ? 0.1629 0.2883 0.1445 -0.0577 0.0221  -0.0007 959  LEU A CA  
806  C C   . LEU A 107 ? 0.2335 0.4084 0.2206 -0.0536 0.0261  0.0030  959  LEU A C   
807  O O   . LEU A 107 ? 0.1566 0.3516 0.1566 -0.0351 0.0312  -0.0016 959  LEU A O   
808  C CB  . LEU A 107 ? 0.1875 0.3113 0.1783 -0.0538 0.0232  0.0009  959  LEU A CB  
809  C CG  . LEU A 107 ? 0.2187 0.3074 0.1979 -0.0619 0.0183  0.0015  959  LEU A CG  
810  C CD1 . LEU A 107 ? 0.2093 0.2640 0.1856 -0.0536 0.0179  -0.0061 959  LEU A CD1 
811  C CD2 . LEU A 107 ? 0.1941 0.2896 0.1827 -0.0574 0.0199  0.0044  959  LEU A CD2 
819  N N   . SER A 109 ? 0.3016 0.4963 0.1742 -0.0522 -0.0036 0.0615  961  SER A N   
820  C CA  . SER A 109 ? 0.2735 0.4638 0.1504 -0.0517 0.0049  0.0459  961  SER A CA  
821  C C   . SER A 109 ? 0.2511 0.4373 0.1328 -0.0433 0.0088  0.0136  961  SER A C   
822  O O   . SER A 109 ? 0.2754 0.4689 0.1610 -0.0420 0.0152  -0.0007 961  SER A O   
823  C CB  . SER A 109 ? 0.2794 0.4291 0.1685 -0.0530 0.0041  0.0570  961  SER A CB  
824  O OG  . SER A 109 ? 0.3147 0.4709 0.2045 -0.0626 0.0005  0.0853  961  SER A OG  
825  N N   . GLY A 110 ? 0.2161 0.3918 0.1013 -0.0380 0.0039  0.0035  962  GLY A N   
826  C CA  . GLY A 110 ? 0.2540 0.4277 0.1481 -0.0318 0.0051  -0.0247 962  GLY A CA  
827  C C   . GLY A 110 ? 0.2143 0.3509 0.1241 -0.0273 0.0079  -0.0312 962  GLY A C   
828  O O   . GLY A 110 ? 0.2365 0.3458 0.1486 -0.0277 0.0079  -0.0161 962  GLY A O   
829  N N   . SER A 111 ? 0.2409 0.3780 0.1625 -0.0229 0.0094  -0.0542 963  SER A N   
830  C CA  . SER A 111 ? 0.2279 0.3341 0.1660 -0.0189 0.0111  -0.0585 963  SER A CA  
831  C C   . SER A 111 ? 0.2448 0.3478 0.1828 -0.0197 0.0162  -0.0538 963  SER A C   
832  O O   . SER A 111 ? 0.2175 0.3472 0.1477 -0.0226 0.0198  -0.0538 963  SER A O   
833  C CB  . SER A 111 ? 0.2274 0.3323 0.1848 -0.0143 0.0087  -0.0821 963  SER A CB  
834  O OG  . SER A 111 ? 0.2782 0.4044 0.2397 -0.0115 0.0117  -0.1010 963  SER A OG  
835  N N   . LEU A 112 ? 0.2444 0.3186 0.1919 -0.0175 0.0163  -0.0493 964  LEU A N   
836  C CA  . LEU A 112 ? 0.2286 0.2996 0.1809 -0.0174 0.0192  -0.0482 964  LEU A CA  
837  C C   . LEU A 112 ? 0.2223 0.3147 0.1870 -0.0135 0.0219  -0.0672 964  LEU A C   
838  O O   . LEU A 112 ? 0.2134 0.3196 0.1790 -0.0147 0.0254  -0.0660 964  LEU A O   
839  C CB  . LEU A 112 ? 0.2283 0.2694 0.1886 -0.0146 0.0176  -0.0425 964  LEU A CB  
840  C CG  . LEU A 112 ? 0.2430 0.2632 0.1926 -0.0162 0.0161  -0.0272 964  LEU A CG  
841  C CD1 . LEU A 112 ? 0.3078 0.3087 0.2647 -0.0125 0.0154  -0.0253 964  LEU A CD1 
842  C CD2 . LEU A 112 ? 0.2399 0.2625 0.1790 -0.0220 0.0157  -0.0163 964  LEU A CD2 
843  N N   . LYS A 113 ? 0.2461 0.3419 0.2234 -0.0086 0.0196  -0.0858 965  LYS A N   
844  C CA  . LYS A 113 ? 0.2907 0.4073 0.2831 -0.0026 0.0213  -0.1094 965  LYS A CA  
845  C C   . LYS A 113 ? 0.2807 0.4396 0.2573 -0.0046 0.0272  -0.1146 965  LYS A C   
846  O O   . LYS A 113 ? 0.2646 0.4442 0.2497 -0.0008 0.0320  -0.1250 965  LYS A O   
847  C CB  . LYS A 113 ? 0.2909 0.4016 0.3011 0.0021  0.0153  -0.1303 965  LYS A CB  
848  C CG  . LYS A 113 ? 0.4085 0.5312 0.4432 0.0109  0.0148  -0.1586 965  LYS A CG  
849  C CD  . LYS A 113 ? 0.4760 0.5732 0.5379 0.0158  0.0127  -0.1547 965  LYS A CD  
850  C CE  . LYS A 113 ? 0.5121 0.6197 0.6043 0.0266  0.0110  -0.1840 965  LYS A CE  
851  N NZ  . LYS A 113 ? 0.4550 0.5634 0.5620 0.0319  0.0140  -0.1790 965  LYS A NZ  
852  N N   A GLU A 114 ? 0.2806 0.4554 0.2356 -0.0105 0.0267  -0.1057 966  GLU A N   
853  N N   B GLU A 114 ? 0.2757 0.4494 0.2307 -0.0106 0.0266  -0.1048 966  GLU A N   
854  C CA  A GLU A 114 ? 0.3158 0.5355 0.2527 -0.0145 0.0321  -0.1034 966  GLU A CA  
855  C CA  B GLU A 114 ? 0.3065 0.5248 0.2431 -0.0146 0.0317  -0.1031 966  GLU A CA  
856  C C   A GLU A 114 ? 0.3145 0.5366 0.2432 -0.0228 0.0360  -0.0761 966  GLU A C   
857  C C   B GLU A 114 ? 0.3092 0.5317 0.2372 -0.0228 0.0358  -0.0762 966  GLU A C   
858  O O   A GLU A 114 ? 0.3337 0.5905 0.2605 -0.0248 0.0429  -0.0755 966  GLU A O   
859  O O   B GLU A 114 ? 0.3329 0.5914 0.2584 -0.0249 0.0427  -0.0760 966  GLU A O   
860  C CB  A GLU A 114 ? 0.3358 0.5731 0.2540 -0.0184 0.0280  -0.1005 966  GLU A CB  
861  C CB  B GLU A 114 ? 0.3193 0.5515 0.2380 -0.0185 0.0270  -0.0993 966  GLU A CB  
862  C CG  A GLU A 114 ? 0.3704 0.6631 0.2683 -0.0224 0.0332  -0.0988 966  GLU A CG  
863  C CG  B GLU A 114 ? 0.3319 0.5598 0.2602 -0.0128 0.0204  -0.1247 966  GLU A CG  
864  C CD  A GLU A 114 ? 0.4249 0.7278 0.3021 -0.0307 0.0284  -0.0741 966  GLU A CD  
865  C CD  B GLU A 114 ? 0.3501 0.6162 0.2801 -0.0067 0.0218  -0.1575 966  GLU A CD  
866  O OE1 A GLU A 114 ? 0.4495 0.7374 0.3261 -0.0294 0.0203  -0.0773 966  GLU A OE1 
867  O OE1 B GLU A 114 ? 0.3557 0.6544 0.2812 -0.0048 0.0302  -0.1633 966  GLU A OE1 
868  O OE2 A GLU A 114 ? 0.4356 0.7628 0.3004 -0.0388 0.0320  -0.0499 966  GLU A OE2 
869  O OE2 B GLU A 114 ? 0.3596 0.6254 0.2968 -0.0035 0.0144  -0.1795 966  GLU A OE2 
870  N N   . TYR A 115 ? 0.2910 0.4782 0.2167 -0.0274 0.0314  -0.0547 967  TYR A N   
871  C CA  . TYR A 115 ? 0.2662 0.4503 0.1864 -0.0364 0.0318  -0.0288 967  TYR A CA  
872  C C   . TYR A 115 ? 0.1991 0.3794 0.1322 -0.0372 0.0348  -0.0276 967  TYR A C   
873  O O   . TYR A 115 ? 0.2250 0.4292 0.1572 -0.0448 0.0382  -0.0147 967  TYR A O   
874  C CB  . TYR A 115 ? 0.2362 0.3826 0.1527 -0.0387 0.0249  -0.0122 967  TYR A CB  
875  C CG  . TYR A 115 ? 0.2222 0.3587 0.1367 -0.0477 0.0222  0.0127  967  TYR A CG  
876  C CD1 . TYR A 115 ? 0.2315 0.3863 0.1372 -0.0557 0.0201  0.0330  967  TYR A CD1 
877  C CD2 . TYR A 115 ? 0.2069 0.3154 0.1300 -0.0486 0.0201  0.0165  967  TYR A CD2 
878  C CE1 . TYR A 115 ? 0.2901 0.4313 0.2002 -0.0646 0.0154  0.0569  967  TYR A CE1 
879  C CE2 . TYR A 115 ? 0.2480 0.3426 0.1730 -0.0571 0.0151  0.0364  967  TYR A CE2 
880  C CZ  . TYR A 115 ? 0.2286 0.3385 0.1494 -0.0653 0.0127  0.0567  967  TYR A CZ  
881  O OH  . TYR A 115 ? 0.3075 0.4009 0.2362 -0.0743 0.0060  0.0770  967  TYR A OH  
882  N N   . LEU A 116 ? 0.2122 0.3637 0.1588 -0.0306 0.0325  -0.0375 968  LEU A N   
883  C CA  . LEU A 116 ? 0.1978 0.3433 0.1568 -0.0316 0.0328  -0.0339 968  LEU A CA  
884  C C   . LEU A 116 ? 0.1945 0.3801 0.1637 -0.0307 0.0398  -0.0425 968  LEU A C   
885  O O   . LEU A 116 ? 0.2412 0.4382 0.2151 -0.0378 0.0410  -0.0296 968  LEU A O   
886  C CB  . LEU A 116 ? 0.1886 0.3010 0.1593 -0.0244 0.0284  -0.0409 968  LEU A CB  
887  C CG  . LEU A 116 ? 0.2386 0.3151 0.2003 -0.0251 0.0230  -0.0310 968  LEU A CG  
888  C CD1 . LEU A 116 ? 0.2417 0.2957 0.2149 -0.0182 0.0199  -0.0365 968  LEU A CD1 
889  C CD2 . LEU A 116 ? 0.2598 0.3238 0.2133 -0.0332 0.0195  -0.0138 968  LEU A CD2 
890  N N   . PRO A 117 ? 0.1741 0.3836 0.1492 -0.0218 0.0442  -0.0655 969  PRO A N   
891  C CA  . PRO A 117 ? 0.1673 0.4201 0.1534 -0.0193 0.0522  -0.0753 969  PRO A CA  
892  C C   . PRO A 117 ? 0.2185 0.5132 0.1912 -0.0305 0.0586  -0.0578 969  PRO A C   
893  O O   . PRO A 117 ? 0.2407 0.5691 0.2246 -0.0323 0.0651  -0.0559 969  PRO A O   
894  C CB  . PRO A 117 ? 0.2169 0.4859 0.2106 -0.0067 0.0544  -0.1068 969  PRO A CB  
895  C CG  . PRO A 117 ? 0.1925 0.4157 0.1898 -0.0027 0.0456  -0.1117 969  PRO A CG  
896  C CD  . PRO A 117 ? 0.1989 0.3979 0.1762 -0.0132 0.0415  -0.0857 969  PRO A CD  
897  N N   . LYS A 118 ? 0.2235 0.5189 0.1752 -0.0380 0.0566  -0.0434 970  LYS A N   
898  C CA  . LYS A 118 ? 0.2552 0.5904 0.1943 -0.0500 0.0611  -0.0213 970  LYS A CA  
899  C C   . LYS A 118 ? 0.2595 0.5719 0.2025 -0.0637 0.0556  0.0104  970  LYS A C   
900  O O   . LYS A 118 ? 0.2981 0.6411 0.2386 -0.0757 0.0583  0.0334  970  LYS A O   
901  C CB  . LYS A 118 ? 0.3064 0.6554 0.2229 -0.0512 0.0595  -0.0194 970  LYS A CB  
902  C CG  . LYS A 118 ? 0.4019 0.7866 0.3124 -0.0400 0.0645  -0.0520 970  LYS A CG  
903  C CD  . LYS A 118 ? 0.3567 0.7438 0.2461 -0.0411 0.0586  -0.0509 970  LYS A CD  
904  C CE  . LYS A 118 ? 0.5170 0.9515 0.3960 -0.0328 0.0628  -0.0815 970  LYS A CE  
905  N NZ  . LYS A 118 ? 0.4662 0.8964 0.3283 -0.0334 0.0541  -0.0829 970  LYS A NZ  
906  N N   . ASN A 119 ? 0.2367 0.4972 0.1873 -0.0622 0.0472  0.0115  971  ASN A N   
907  C CA  . ASN A 119 ? 0.2811 0.5126 0.2354 -0.0739 0.0392  0.0365  971  ASN A CA  
908  C C   . ASN A 119 ? 0.2460 0.4516 0.2165 -0.0736 0.0345  0.0336  971  ASN A C   
909  O O   . ASN A 119 ? 0.2611 0.4311 0.2332 -0.0794 0.0254  0.0452  971  ASN A O   
910  C CB  . ASN A 119 ? 0.2710 0.4650 0.2128 -0.0736 0.0311  0.0443  971  ASN A CB  
911  C CG  . ASN A 119 ? 0.2896 0.5113 0.2172 -0.0779 0.0326  0.0566  971  ASN A CG  
912  O OD1 . ASN A 119 ? 0.3603 0.5942 0.2886 -0.0900 0.0302  0.0830  971  ASN A OD1 
913  N ND2 . ASN A 119 ? 0.2856 0.5198 0.2021 -0.0688 0.0356  0.0388  971  ASN A ND2 
914  N N   . LYS A 120 ? 0.2459 0.4712 0.2298 -0.0667 0.0397  0.0178  972  LYS A N   
915  C CA  . LYS A 120 ? 0.2688 0.4753 0.2689 -0.0661 0.0342  0.0159  972  LYS A CA  
916  C C   . LYS A 120 ? 0.2335 0.4348 0.2416 -0.0815 0.0275  0.0378  972  LYS A C   
917  O O   . LYS A 120 ? 0.2448 0.4104 0.2553 -0.0834 0.0175  0.0395  972  LYS A O   
918  C CB  . LYS A 120 ? 0.2556 0.4957 0.2750 -0.0584 0.0410  0.0011  972  LYS A CB  
919  C CG  . LYS A 120 ? 0.3172 0.5490 0.3412 -0.0420 0.0425  -0.0231 972  LYS A CG  
920  C CD  . LYS A 120 ? 0.3427 0.6184 0.3875 -0.0341 0.0510  -0.0381 972  LYS A CD  
921  C CE  . LYS A 120 ? 0.4187 0.6786 0.4815 -0.0187 0.0481  -0.0584 972  LYS A CE  
922  N NZ  . LYS A 120 ? 0.4554 0.7585 0.5441 -0.0101 0.0555  -0.0727 972  LYS A NZ  
923  N N   . ASN A 121 ? 0.2058 0.4447 0.2190 -0.0930 0.0325  0.0542  973  ASN A N   
924  C CA  . ASN A 121 ? 0.2759 0.5133 0.3036 -0.1099 0.0253  0.0770  973  ASN A CA  
925  C C   . ASN A 121 ? 0.3096 0.4973 0.3315 -0.1170 0.0121  0.0890  973  ASN A C   
926  O O   . ASN A 121 ? 0.3617 0.5307 0.3984 -0.1271 0.0017  0.0977  973  ASN A O   
927  C CB  . ASN A 121 ? 0.3199 0.6114 0.3553 -0.1224 0.0339  0.0973  973  ASN A CB  
928  C CG  . ASN A 121 ? 0.3094 0.6048 0.3687 -0.1415 0.0263  0.1215  973  ASN A CG  
929  O OD1 . ASN A 121 ? 0.3167 0.6093 0.3948 -0.1428 0.0217  0.1158  973  ASN A OD1 
930  N ND2 . ASN A 121 ? 0.2721 0.5754 0.3335 -0.1571 0.0237  0.1502  973  ASN A ND2 
931  N N   . LYS A 122 ? 0.3167 0.4837 0.3202 -0.1110 0.0116  0.0874  974  LYS A N   
932  C CA  . LYS A 122 ? 0.3867 0.5086 0.3881 -0.1155 -0.0006 0.0972  974  LYS A CA  
933  C C   . LYS A 122 ? 0.3727 0.4508 0.3644 -0.1030 -0.0063 0.0774  974  LYS A C   
934  O O   . LYS A 122 ? 0.3921 0.4337 0.3844 -0.1049 -0.0165 0.0804  974  LYS A O   
935  C CB  . LYS A 122 ? 0.4297 0.5572 0.4222 -0.1192 0.0000  0.1147  974  LYS A CB  
936  C CG  . LYS A 122 ? 0.4329 0.5705 0.4051 -0.1062 0.0079  0.1013  974  LYS A CG  
937  C CD  . LYS A 122 ? 0.5487 0.6719 0.5126 -0.1071 0.0026  0.1157  974  LYS A CD  
938  C CE  . LYS A 122 ? 0.5532 0.7175 0.5173 -0.1190 0.0053  0.1422  974  LYS A CE  
939  N NZ  . LYS A 122 ? 0.6529 0.8014 0.6119 -0.1194 -0.0022 0.1587  974  LYS A NZ  
940  N N   . ILE A 123 ? 0.2999 0.3839 0.2848 -0.0904 0.0001  0.0579  975  ILE A N   
941  C CA  . ILE A 123 ? 0.3148 0.3664 0.2899 -0.0785 -0.0031 0.0418  975  ILE A CA  
942  C C   . ILE A 123 ? 0.3082 0.3592 0.2925 -0.0769 -0.0066 0.0330  975  ILE A C   
943  O O   . ILE A 123 ? 0.3327 0.4068 0.3238 -0.0713 -0.0005 0.0252  975  ILE A O   
944  C CB  . ILE A 123 ? 0.3146 0.3729 0.2787 -0.0663 0.0051  0.0296  975  ILE A CB  
945  C CG1 . ILE A 123 ? 0.3455 0.4107 0.3002 -0.0678 0.0077  0.0381  975  ILE A CG1 
946  C CG2 . ILE A 123 ? 0.2997 0.3282 0.2564 -0.0558 0.0022  0.0176  975  ILE A CG2 
947  C CD1 . ILE A 123 ? 0.3953 0.4305 0.3468 -0.0716 -0.0007 0.0502  975  ILE A CD1 
948  N N   . ASN A 124 ? 0.2619 0.2874 0.2477 -0.0812 -0.0175 0.0335  976  ASN A N   
949  C CA  . ASN A 124 ? 0.2921 0.3166 0.2850 -0.0809 -0.0240 0.0266  976  ASN A CA  
950  C C   . ASN A 124 ? 0.3001 0.3023 0.2775 -0.0689 -0.0262 0.0141  976  ASN A C   
951  O O   . ASN A 124 ? 0.3053 0.2940 0.2695 -0.0615 -0.0220 0.0108  976  ASN A O   
952  C CB  . ASN A 124 ? 0.3335 0.3496 0.3393 -0.0947 -0.0362 0.0337  976  ASN A CB  
953  C CG  . ASN A 124 ? 0.3719 0.3506 0.3696 -0.0961 -0.0459 0.0313  976  ASN A CG  
954  O OD1 . ASN A 124 ? 0.3788 0.3398 0.3606 -0.0862 -0.0425 0.0253  976  ASN A OD1 
955  N ND2 . ASN A 124 ? 0.4512 0.4188 0.4638 -0.1085 -0.0584 0.0355  976  ASN A ND2 
956  N N   . LEU A 125 ? 0.2723 0.2744 0.2523 -0.0675 -0.0331 0.0089  977  LEU A N   
957  C CA  . LEU A 125 ? 0.2943 0.2832 0.2594 -0.0567 -0.0347 0.0007  977  LEU A CA  
958  C C   . LEU A 125 ? 0.2823 0.2442 0.2288 -0.0537 -0.0377 -0.0050 977  LEU A C   
959  O O   . LEU A 125 ? 0.2968 0.2522 0.2309 -0.0442 -0.0321 -0.0081 977  LEU A O   
960  C CB  . LEU A 125 ? 0.3086 0.3059 0.2789 -0.0574 -0.0439 -0.0011 977  LEU A CB  
961  C CG  . LEU A 125 ? 0.2913 0.2813 0.2455 -0.0483 -0.0474 -0.0055 977  LEU A CG  
962  C CD1 . LEU A 125 ? 0.3594 0.3543 0.3145 -0.0380 -0.0377 -0.0026 977  LEU A CD1 
963  C CD2 . LEU A 125 ? 0.3672 0.3696 0.3274 -0.0511 -0.0591 -0.0051 977  LEU A CD2 
964  N N   . LYS A 126 ? 0.3039 0.2514 0.2524 -0.0616 -0.0469 -0.0065 978  LYS A N   
965  C CA  . LYS A 126 ? 0.2909 0.2125 0.2277 -0.0579 -0.0503 -0.0140 978  LYS A CA  
966  C C   . LYS A 126 ? 0.3351 0.2522 0.2669 -0.0514 -0.0399 -0.0098 978  LYS A C   
967  O O   . LYS A 126 ? 0.3117 0.2186 0.2299 -0.0413 -0.0367 -0.0171 978  LYS A O   
968  C CB  . LYS A 126 ? 0.3463 0.2522 0.2964 -0.0694 -0.0626 -0.0138 978  LYS A CB  
969  C CG  . LYS A 126 ? 0.4196 0.2966 0.3621 -0.0640 -0.0695 -0.0270 978  LYS A CG  
970  C CD  . LYS A 126 ? 0.5587 0.4173 0.5183 -0.0754 -0.0860 -0.0313 978  LYS A CD  
971  C CE  . LYS A 126 ? 0.6933 0.5275 0.6425 -0.0668 -0.0951 -0.0543 978  LYS A CE  
972  N NZ  . LYS A 126 ? 0.7185 0.5667 0.6459 -0.0598 -0.0965 -0.0695 978  LYS A NZ  
973  N N   . GLN A 127 ? 0.2983 0.2278 0.2410 -0.0572 -0.0345 0.0020  979  GLN A N   
974  C CA  . GLN A 127 ? 0.3037 0.2325 0.2419 -0.0522 -0.0266 0.0063  979  GLN A CA  
975  C C   . GLN A 127 ? 0.2671 0.2063 0.1969 -0.0419 -0.0175 0.0012  979  GLN A C   
976  O O   . GLN A 127 ? 0.2729 0.2048 0.1954 -0.0345 -0.0134 -0.0009 979  GLN A O   
977  C CB  . GLN A 127 ? 0.2936 0.2391 0.2426 -0.0612 -0.0235 0.0208  979  GLN A CB  
978  C CG  . GLN A 127 ? 0.2838 0.2277 0.2276 -0.0569 -0.0189 0.0259  979  GLN A CG  
979  C CD  . GLN A 127 ? 0.2888 0.2031 0.2316 -0.0530 -0.0259 0.0242  979  GLN A CD  
980  O OE1 . GLN A 127 ? 0.3142 0.2139 0.2685 -0.0607 -0.0351 0.0312  979  GLN A OE1 
981  N NE2 . GLN A 127 ? 0.3056 0.2113 0.2382 -0.0411 -0.0220 0.0146  979  GLN A NE2 
982  N N   . GLN A 128 ? 0.2611 0.2174 0.1962 -0.0416 -0.0151 0.0001  980  GLN A N   
983  C CA  . GLN A 128 ? 0.2442 0.2072 0.1776 -0.0328 -0.0090 -0.0036 980  GLN A CA  
984  C C   . GLN A 128 ? 0.2420 0.1913 0.1625 -0.0255 -0.0103 -0.0076 980  GLN A C   
985  O O   . GLN A 128 ? 0.2558 0.2045 0.1736 -0.0192 -0.0046 -0.0076 980  GLN A O   
986  C CB  . GLN A 128 ? 0.2778 0.2584 0.2242 -0.0329 -0.0092 -0.0040 980  GLN A CB  
987  C CG  . GLN A 128 ? 0.2557 0.2587 0.2157 -0.0368 -0.0042 -0.0029 980  GLN A CG  
988  C CD  . GLN A 128 ? 0.2787 0.3004 0.2559 -0.0358 -0.0052 -0.0047 980  GLN A CD  
989  O OE1 . GLN A 128 ? 0.3365 0.3582 0.3173 -0.0394 -0.0123 -0.0022 980  GLN A OE1 
990  N NE2 . GLN A 128 ? 0.2165 0.2551 0.2064 -0.0302 0.0011  -0.0107 980  GLN A NE2 
991  N N   . LEU A 129 ? 0.2659 0.2075 0.1791 -0.0268 -0.0177 -0.0113 981  LEU A N   
992  C CA  . LEU A 129 ? 0.2762 0.2116 0.1739 -0.0195 -0.0184 -0.0165 981  LEU A CA  
993  C C   . LEU A 129 ? 0.2922 0.2142 0.1823 -0.0144 -0.0155 -0.0212 981  LEU A C   
994  O O   . LEU A 129 ? 0.2534 0.1781 0.1350 -0.0066 -0.0101 -0.0225 981  LEU A O   
995  C CB  . LEU A 129 ? 0.3015 0.2368 0.1921 -0.0219 -0.0283 -0.0222 981  LEU A CB  
996  C CG  . LEU A 129 ? 0.2975 0.2489 0.1971 -0.0252 -0.0323 -0.0163 981  LEU A CG  
997  C CD1 . LEU A 129 ? 0.3578 0.3106 0.2465 -0.0270 -0.0438 -0.0231 981  LEU A CD1 
998  C CD2 . LEU A 129 ? 0.3063 0.2695 0.2102 -0.0189 -0.0259 -0.0076 981  LEU A CD2 
999  N N   . LYS A 130 ? 0.2896 0.1996 0.1863 -0.0190 -0.0188 -0.0212 982  LYS A N   
1000 C CA  . LYS A 130 ? 0.3100 0.2076 0.2056 -0.0135 -0.0168 -0.0235 982  LYS A CA  
1001 C C   . LYS A 130 ? 0.2745 0.1822 0.1727 -0.0094 -0.0075 -0.0169 982  LYS A C   
1002 O O   . LYS A 130 ? 0.2705 0.1769 0.1643 -0.0009 -0.0031 -0.0200 982  LYS A O   
1003 C CB  . LYS A 130 ? 0.3231 0.2061 0.2304 -0.0208 -0.0243 -0.0199 982  LYS A CB  
1004 C CG  . LYS A 130 ? 0.3448 0.2110 0.2527 -0.0233 -0.0358 -0.0307 982  LYS A CG  
1005 C CD  . LYS A 130 ? 0.3726 0.2218 0.2983 -0.0319 -0.0447 -0.0237 982  LYS A CD  
1006 C CE  . LYS A 130 ? 0.4848 0.3155 0.4174 -0.0367 -0.0585 -0.0347 982  LYS A CE  
1007 N NZ  . LYS A 130 ? 0.4933 0.3092 0.4498 -0.0484 -0.0677 -0.0212 982  LYS A NZ  
1008 N N   . TYR A 131 ? 0.2604 0.1807 0.1667 -0.0149 -0.0046 -0.0095 983  TYR A N   
1009 C CA  . TYR A 131 ? 0.2446 0.1756 0.1547 -0.0115 0.0025  -0.0065 983  TYR A CA  
1010 C C   . TYR A 131 ? 0.2432 0.1791 0.1506 -0.0052 0.0068  -0.0082 983  TYR A C   
1011 O O   . TYR A 131 ? 0.2623 0.2008 0.1714 -0.0003 0.0114  -0.0071 983  TYR A O   
1012 C CB  . TYR A 131 ? 0.2161 0.1631 0.1351 -0.0171 0.0044  -0.0037 983  TYR A CB  
1013 C CG  . TYR A 131 ? 0.2370 0.1901 0.1591 -0.0243 0.0026  0.0023  983  TYR A CG  
1014 C CD1 . TYR A 131 ? 0.2205 0.1626 0.1411 -0.0252 -0.0010 0.0082  983  TYR A CD1 
1015 C CD2 . TYR A 131 ? 0.2827 0.2561 0.2111 -0.0295 0.0047  0.0032  983  TYR A CD2 
1016 C CE1 . TYR A 131 ? 0.2532 0.2047 0.1780 -0.0331 -0.0031 0.0191  983  TYR A CE1 
1017 C CE2 . TYR A 131 ? 0.2836 0.2706 0.2137 -0.0369 0.0043  0.0116  983  TYR A CE2 
1018 C CZ  . TYR A 131 ? 0.3442 0.3203 0.2721 -0.0396 0.0001  0.0215  983  TYR A CZ  
1019 O OH  . TYR A 131 ? 0.3710 0.3637 0.3015 -0.0482 -0.0008 0.0346  983  TYR A OH  
1020 N N   . ALA A 132 ? 0.2646 0.2038 0.1697 -0.0058 0.0048  -0.0085 984  ALA A N   
1021 C CA  . ALA A 132 ? 0.2513 0.1978 0.1548 -0.0011 0.0079  -0.0050 984  ALA A CA  
1022 C C   . ALA A 132 ? 0.2605 0.2064 0.1519 0.0058  0.0114  -0.0074 984  ALA A C   
1023 O O   . ALA A 132 ? 0.2510 0.2055 0.1463 0.0094  0.0174  -0.0019 984  ALA A O   
1024 C CB  . ALA A 132 ? 0.2431 0.1950 0.1453 -0.0031 0.0029  -0.0028 984  ALA A CB  
1025 N N   . VAL A 133 ? 0.2563 0.1932 0.1358 0.0079  0.0075  -0.0165 985  VAL A N   
1026 C CA  . VAL A 133 ? 0.2529 0.1905 0.1225 0.0168  0.0112  -0.0235 985  VAL A CA  
1027 C C   . VAL A 133 ? 0.2820 0.2192 0.1618 0.0208  0.0168  -0.0211 985  VAL A C   
1028 O O   . VAL A 133 ? 0.2571 0.2061 0.1357 0.0279  0.0239  -0.0203 985  VAL A O   
1029 C CB  . VAL A 133 ? 0.3198 0.2423 0.1807 0.0186  0.0033  -0.0383 985  VAL A CB  
1030 C CG1 . VAL A 133 ? 0.3095 0.2303 0.1657 0.0300  0.0067  -0.0499 985  VAL A CG1 
1031 C CG2 . VAL A 133 ? 0.3177 0.2461 0.1657 0.0161  -0.0029 -0.0430 985  VAL A CG2 
1032 N N   . GLN A 134 ? 0.2771 0.2040 0.1670 0.0162  0.0135  -0.0190 986  GLN A N   
1033 C CA  . GLN A 134 ? 0.2674 0.1953 0.1672 0.0194  0.0164  -0.0157 986  GLN A CA  
1034 C C   . GLN A 134 ? 0.2216 0.1657 0.1301 0.0188  0.0227  -0.0081 986  GLN A C   
1035 O O   . GLN A 134 ? 0.2685 0.2205 0.1833 0.0241  0.0272  -0.0064 986  GLN A O   
1036 C CB  . GLN A 134 ? 0.2708 0.1898 0.1778 0.0129  0.0105  -0.0117 986  GLN A CB  
1037 C CG  . GLN A 134 ? 0.2988 0.1991 0.2052 0.0133  0.0030  -0.0166 986  GLN A CG  
1038 C CD  . GLN A 134 ? 0.3355 0.2312 0.2498 0.0040  -0.0031 -0.0071 986  GLN A CD  
1039 O OE1 . GLN A 134 ? 0.3329 0.2424 0.2503 -0.0008 -0.0005 0.0008  986  GLN A OE1 
1040 N NE2 . GLN A 134 ? 0.3257 0.2042 0.2441 0.0005  -0.0115 -0.0079 986  GLN A NE2 
1041 N N   . ILE A 135 ? 0.2087 0.1575 0.1215 0.0123  0.0220  -0.0039 987  ILE A N   
1042 C CA  . ILE A 135 ? 0.1959 0.1566 0.1217 0.0109  0.0258  0.0025  987  ILE A CA  
1043 C C   . ILE A 135 ? 0.2333 0.2049 0.1564 0.0156  0.0315  0.0080  987  ILE A C   
1044 O O   . ILE A 135 ? 0.2499 0.2325 0.1843 0.0170  0.0360  0.0136  987  ILE A O   
1045 C CB  . ILE A 135 ? 0.1988 0.1604 0.1336 0.0048  0.0227  0.0038  987  ILE A CB  
1046 C CG1 . ILE A 135 ? 0.2248 0.1850 0.1629 0.0005  0.0193  -0.0018 987  ILE A CG1 
1047 C CG2 . ILE A 135 ? 0.2146 0.1842 0.1684 0.0034  0.0245  0.0102  987  ILE A CG2 
1048 C CD1 . ILE A 135 ? 0.1882 0.1508 0.1326 -0.0032 0.0167  -0.0045 987  ILE A CD1 
1049 N N   . CYS A 136 ? 0.2193 0.1920 0.1277 0.0176  0.0311  0.0068  988  CYS A N   
1050 C CA  . CYS A 136 ? 0.2585 0.2487 0.1595 0.0226  0.0374  0.0124  988  CYS A CA  
1051 C C   . CYS A 136 ? 0.2494 0.2480 0.1475 0.0314  0.0440  0.0068  988  CYS A C   
1052 O O   . CYS A 136 ? 0.2637 0.2830 0.1674 0.0338  0.0516  0.0156  988  CYS A O   
1053 C CB  . CYS A 136 ? 0.3090 0.3029 0.1911 0.0234  0.0345  0.0105  988  CYS A CB  
1054 S SG  . CYS A 136 ? 0.2770 0.2696 0.1675 0.0152  0.0277  0.0219  988  CYS A SG  
1055 N N   . LYS A 137 ? 0.2633 0.2474 0.1563 0.0364  0.0409  -0.0065 989  LYS A N   
1056 C CA  . LYS A 137 ? 0.2444 0.2351 0.1399 0.0468  0.0461  -0.0133 989  LYS A CA  
1057 C C   . LYS A 137 ? 0.2701 0.2703 0.1870 0.0454  0.0496  -0.0034 989  LYS A C   
1058 O O   . LYS A 137 ? 0.2702 0.2908 0.1939 0.0519  0.0576  -0.0008 989  LYS A O   
1059 C CB  . LYS A 137 ? 0.3216 0.2901 0.2136 0.0519  0.0391  -0.0282 989  LYS A CB  
1060 C CG  . LYS A 137 ? 0.3024 0.2644 0.1755 0.0550  0.0351  -0.0422 989  LYS A CG  
1061 C CD  . LYS A 137 ? 0.3843 0.3198 0.2609 0.0581  0.0257  -0.0558 989  LYS A CD  
1062 C CE  . LYS A 137 ? 0.3947 0.3248 0.2552 0.0624  0.0206  -0.0743 989  LYS A CE  
1063 N NZ  . LYS A 137 ? 0.5094 0.4091 0.3794 0.0632  0.0087  -0.0866 989  LYS A NZ  
1064 N N   . GLY A 138 ? 0.2590 0.2480 0.1865 0.0370  0.0435  0.0011  990  GLY A N   
1065 C CA  . GLY A 138 ? 0.2560 0.2542 0.2035 0.0338  0.0440  0.0085  990  GLY A CA  
1066 C C   . GLY A 138 ? 0.2792 0.2975 0.2391 0.0303  0.0500  0.0201  990  GLY A C   
1067 O O   . GLY A 138 ? 0.2453 0.2811 0.2205 0.0326  0.0548  0.0257  990  GLY A O   
1068 N N   . MET A 139 ? 0.2529 0.2697 0.2088 0.0245  0.0492  0.0256  991  MET A N   
1069 C CA  . MET A 139 ? 0.2307 0.2646 0.2009 0.0195  0.0533  0.0412  991  MET A CA  
1070 C C   . MET A 139 ? 0.2722 0.3318 0.2355 0.0259  0.0635  0.0481  991  MET A C   
1071 O O   . MET A 139 ? 0.2645 0.3454 0.2462 0.0229  0.0689  0.0625  991  MET A O   
1072 C CB  . MET A 139 ? 0.2442 0.2692 0.2140 0.0129  0.0482  0.0467  991  MET A CB  
1073 C CG  . MET A 139 ? 0.2846 0.2920 0.2671 0.0068  0.0397  0.0402  991  MET A CG  
1074 S SD  . MET A 139 ? 0.2855 0.2968 0.3009 0.0005  0.0365  0.0425  991  MET A SD  
1075 C CE  . MET A 139 ? 0.3957 0.4230 0.4341 -0.0048 0.0399  0.0654  991  MET A CE  
1076 N N   . ASP A 140 ? 0.2419 0.3024 0.1800 0.0344  0.0662  0.0378  992  ASP A N   
1077 C CA  . ASP A 140 ? 0.2495 0.3403 0.1775 0.0425  0.0770  0.0404  992  ASP A CA  
1078 C C   . ASP A 140 ? 0.2761 0.3812 0.2185 0.0503  0.0837  0.0363  992  ASP A C   
1079 O O   . ASP A 140 ? 0.2752 0.4132 0.2255 0.0528  0.0940  0.0467  992  ASP A O   
1080 C CB  . ASP A 140 ? 0.2921 0.3801 0.1898 0.0505  0.0764  0.0246  992  ASP A CB  
1081 C CG  . ASP A 140 ? 0.4248 0.5512 0.3070 0.0579  0.0875  0.0274  992  ASP A CG  
1082 O OD1 . ASP A 140 ? 0.3991 0.5505 0.2863 0.0511  0.0923  0.0500  992  ASP A OD1 
1083 O OD2 . ASP A 140 ? 0.5180 0.6504 0.3843 0.0707  0.0910  0.0070  992  ASP A OD2 
1084 N N   . TYR A 141 ? 0.2813 0.3646 0.2300 0.0535  0.0775  0.0241  993  TYR A N   
1085 C CA  . TYR A 141 ? 0.3015 0.3974 0.2693 0.0603  0.0812  0.0228  993  TYR A CA  
1086 C C   . TYR A 141 ? 0.2891 0.4030 0.2848 0.0503  0.0829  0.0411  993  TYR A C   
1087 O O   . TYR A 141 ? 0.2672 0.4117 0.2778 0.0543  0.0919  0.0485  993  TYR A O   
1088 C CB  . TYR A 141 ? 0.2761 0.3448 0.2469 0.0634  0.0715  0.0111  993  TYR A CB  
1089 C CG  . TYR A 141 ? 0.2570 0.3378 0.2503 0.0698  0.0725  0.0120  993  TYR A CG  
1090 C CD1 . TYR A 141 ? 0.2989 0.3942 0.2952 0.0859  0.0795  0.0022  993  TYR A CD1 
1091 C CD2 . TYR A 141 ? 0.2623 0.3418 0.2754 0.0608  0.0656  0.0207  993  TYR A CD2 
1092 C CE1 . TYR A 141 ? 0.3306 0.4386 0.3511 0.0929  0.0796  0.0039  993  TYR A CE1 
1093 C CE2 . TYR A 141 ? 0.2785 0.3719 0.3134 0.0665  0.0649  0.0226  993  TYR A CE2 
1094 C CZ  . TYR A 141 ? 0.2942 0.4012 0.3338 0.0826  0.0718  0.0154  993  TYR A CZ  
1095 O OH  . TYR A 141 ? 0.2738 0.3962 0.3384 0.0892  0.0705  0.0181  993  TYR A OH  
1096 N N   . LEU A 142 ? 0.2873 0.3838 0.2921 0.0375  0.0739  0.0474  994  LEU A N   
1097 C CA  . LEU A 142 ? 0.2763 0.3837 0.3112 0.0264  0.0718  0.0617  994  LEU A CA  
1098 C C   . LEU A 142 ? 0.2989 0.4351 0.3442 0.0221  0.0809  0.0814  994  LEU A C   
1099 O O   . LEU A 142 ? 0.2942 0.4541 0.3661 0.0183  0.0846  0.0937  994  LEU A O   
1100 C CB  . LEU A 142 ? 0.3052 0.3872 0.3454 0.0155  0.0601  0.0597  994  LEU A CB  
1101 C CG  . LEU A 142 ? 0.2951 0.3807 0.3684 0.0038  0.0538  0.0677  994  LEU A CG  
1102 C CD1 . LEU A 142 ? 0.2973 0.3901 0.3853 0.0050  0.0498  0.0617  994  LEU A CD1 
1103 C CD2 . LEU A 142 ? 0.3084 0.3700 0.3837 -0.0038 0.0438  0.0619  994  LEU A CD2 
1104 N N   . GLY A 143 ? 0.2764 0.4137 0.3014 0.0223  0.0840  0.0861  995  GLY A N   
1105 C CA  . GLY A 143 ? 0.2880 0.4576 0.3179 0.0185  0.0930  0.1082  995  GLY A CA  
1106 C C   . GLY A 143 ? 0.3167 0.5262 0.3408 0.0294  0.1077  0.1091  995  GLY A C   
1107 O O   . GLY A 143 ? 0.3536 0.5989 0.3942 0.0243  0.1163  0.1312  995  GLY A O   
1108 N N   . SER A 144 ? 0.3140 0.5192 0.3176 0.0445  0.1107  0.0855  996  SER A N   
1109 C CA  . SER A 144 ? 0.3365 0.5789 0.3386 0.0583  0.1244  0.0799  996  SER A CA  
1110 C C   . SER A 144 ? 0.3501 0.6103 0.3880 0.0576  0.1270  0.0868  996  SER A C   
1111 O O   . SER A 144 ? 0.3486 0.6511 0.3959 0.0654  0.1403  0.0914  996  SER A O   
1112 C CB  . SER A 144 ? 0.3030 0.5298 0.2795 0.0753  0.1239  0.0502  996  SER A CB  
1113 O OG  . SER A 144 ? 0.3646 0.5631 0.3547 0.0790  0.1150  0.0375  996  SER A OG  
1114 N N   . ARG A 145 ? 0.3272 0.5588 0.3847 0.0490  0.1144  0.0864  997  ARG A N   
1115 C CA  . ARG A 145 ? 0.3375 0.5855 0.4321 0.0444  0.1132  0.0955  997  ARG A CA  
1116 C C   . ARG A 145 ? 0.2993 0.5634 0.4233 0.0261  0.1124  0.1221  997  ARG A C   
1117 O O   . ARG A 145 ? 0.2884 0.5652 0.4468 0.0190  0.1092  0.1306  997  ARG A O   
1118 C CB  . ARG A 145 ? 0.3057 0.5203 0.4075 0.0431  0.0985  0.0824  997  ARG A CB  
1119 C CG  . ARG A 145 ? 0.4320 0.6262 0.5137 0.0586  0.0956  0.0604  997  ARG A CG  
1120 C CD  . ARG A 145 ? 0.5038 0.7261 0.5903 0.0767  0.1066  0.0529  997  ARG A CD  
1121 N NE  . ARG A 145 ? 0.5959 0.8210 0.6535 0.0889  0.1155  0.0402  997  ARG A NE  
1122 C CZ  . ARG A 145 ? 0.6088 0.8464 0.6610 0.1082  0.1229  0.0233  997  ARG A CZ  
1123 N NH1 . ARG A 145 ? 0.6306 0.8692 0.6541 0.1172  0.1287  0.0093  997  ARG A NH1 
1124 N NH2 . ARG A 145 ? 0.6135 0.8640 0.6909 0.1194  0.1236  0.0190  997  ARG A NH2 
1125 N N   . GLN A 146 ? 0.2964 0.5599 0.4098 0.0182  0.1138  0.1359  998  GLN A N   
1126 C CA  . GLN A 146 ? 0.2904 0.5661 0.4340 0.0003  0.1118  0.1648  998  GLN A CA  
1127 C C   . GLN A 146 ? 0.2872 0.5274 0.4578 -0.0138 0.0943  0.1641  998  GLN A C   
1128 O O   . GLN A 146 ? 0.3097 0.5601 0.5199 -0.0277 0.0899  0.1822  998  GLN A O   
1129 C CB  . GLN A 146 ? 0.3192 0.6475 0.4912 -0.0024 0.1245  0.1868  998  GLN A CB  
1130 C CG  . GLN A 146 ? 0.2853 0.6571 0.4313 0.0108  0.1434  0.1893  998  GLN A CG  
1131 C CD  . GLN A 146 ? 0.4424 0.8702 0.6175 0.0116  0.1573  0.2051  998  GLN A CD  
1132 O OE1 . GLN A 146 ? 0.5185 0.9708 0.6849 0.0290  0.1682  0.1884  998  GLN A OE1 
1133 N NE2 . GLN A 146 ? 0.3859 0.8342 0.6000 -0.0072 0.1562  0.2375  998  GLN A NE2 
1134 N N   . TYR A 147 ? 0.2558 0.4559 0.4057 -0.0107 0.0839  0.1428  999  TYR A N   
1135 C CA  . TYR A 147 ? 0.2531 0.4214 0.4233 -0.0218 0.0679  0.1370  999  TYR A CA  
1136 C C   . TYR A 147 ? 0.2562 0.3983 0.4129 -0.0250 0.0622  0.1375  999  TYR A C   
1137 O O   . TYR A 147 ? 0.2773 0.4156 0.3991 -0.0161 0.0674  0.1320  999  TYR A O   
1138 C CB  . TYR A 147 ? 0.2363 0.3844 0.3964 -0.0158 0.0598  0.1115  999  TYR A CB  
1139 C CG  . TYR A 147 ? 0.2084 0.3782 0.3852 -0.0125 0.0612  0.1093  999  TYR A CG  
1140 C CD1 . TYR A 147 ? 0.1930 0.3756 0.4103 -0.0243 0.0546  0.1183  999  TYR A CD1 
1141 C CD2 . TYR A 147 ? 0.2893 0.4662 0.4447 0.0026  0.0677  0.0979  999  TYR A CD2 
1142 C CE1 . TYR A 147 ? 0.1881 0.3940 0.4229 -0.0211 0.0550  0.1171  999  TYR A CE1 
1143 C CE2 . TYR A 147 ? 0.2382 0.4362 0.4121 0.0071  0.0682  0.0969  999  TYR A CE2 
1144 C CZ  . TYR A 147 ? 0.2318 0.4458 0.4442 -0.0047 0.0622  0.1069  999  TYR A CZ  
1145 O OH  . TYR A 147 ? 0.2836 0.5210 0.5156 0.0001  0.0617  0.1062  999  TYR A OH  
1146 N N   . VAL A 148 ? 0.2655 0.3896 0.4529 -0.0371 0.0501  0.1422  1000 VAL A N   
1147 C CA  . VAL A 148 ? 0.2731 0.3676 0.4558 -0.0391 0.0412  0.1370  1000 VAL A CA  
1148 C C   . VAL A 148 ? 0.2108 0.2794 0.3983 -0.0395 0.0292  0.1105  1000 VAL A C   
1149 O O   . VAL A 148 ? 0.2031 0.2730 0.4190 -0.0461 0.0219  0.1056  1000 VAL A O   
1150 C CB  . VAL A 148 ? 0.3001 0.3928 0.5180 -0.0512 0.0355  0.1628  1000 VAL A CB  
1151 C CG1 . VAL A 148 ? 0.3704 0.4868 0.5706 -0.0494 0.0464  0.1878  1000 VAL A CG1 
1152 C CG2 . VAL A 148 ? 0.3346 0.4358 0.6025 -0.0644 0.0294  0.1754  1000 VAL A CG2 
1153 N N   . HIS A 149 ? 0.1881 0.2371 0.3475 -0.0327 0.0271  0.0935  1001 HIS A N   
1154 C CA  . HIS A 149 ? 0.1998 0.2317 0.3556 -0.0314 0.0183  0.0682  1001 HIS A CA  
1155 C C   . HIS A 149 ? 0.2136 0.2285 0.4028 -0.0391 0.0058  0.0618  1001 HIS A C   
1156 O O   . HIS A 149 ? 0.1809 0.1933 0.3870 -0.0427 -0.0030 0.0458  1001 HIS A O   
1157 C CB  . HIS A 149 ? 0.2069 0.2276 0.3241 -0.0225 0.0211  0.0549  1001 HIS A CB  
1158 C CG  . HIS A 149 ? 0.1982 0.2102 0.3071 -0.0209 0.0145  0.0321  1001 HIS A CG  
1159 N ND1 . HIS A 149 ? 0.2085 0.2070 0.3259 -0.0229 0.0065  0.0178  1001 HIS A ND1 
1160 C CD2 . HIS A 149 ? 0.2166 0.2352 0.3100 -0.0173 0.0147  0.0221  1001 HIS A CD2 
1161 C CE1 . HIS A 149 ? 0.2484 0.2492 0.3533 -0.0211 0.0031  -0.0002 1001 HIS A CE1 
1162 N NE2 . HIS A 149 ? 0.1790 0.1911 0.2693 -0.0184 0.0073  0.0040  1001 HIS A NE2 
1163 N N   . ARG A 150 ? 0.2173 0.2213 0.4167 -0.0408 0.0038  0.0732  1002 ARG A N   
1164 C CA  . ARG A 150 ? 0.2140 0.1991 0.4531 -0.0469 -0.0091 0.0689  1002 ARG A CA  
1165 C C   . ARG A 150 ? 0.2473 0.2161 0.4822 -0.0420 -0.0169 0.0374  1002 ARG A C   
1166 O O   . ARG A 150 ? 0.2711 0.2245 0.5402 -0.0448 -0.0281 0.0276  1002 ARG A O   
1167 C CB  . ARG A 150 ? 0.2389 0.2277 0.5238 -0.0582 -0.0169 0.0766  1002 ARG A CB  
1168 C CG  . ARG A 150 ? 0.2181 0.2303 0.5122 -0.0643 -0.0085 0.1081  1002 ARG A CG  
1169 C CD  . ARG A 150 ? 0.2676 0.2781 0.6195 -0.0785 -0.0193 0.1223  1002 ARG A CD  
1170 N NE  . ARG A 150 ? 0.3707 0.3775 0.7425 -0.0826 -0.0299 0.0975  1002 ARG A NE  
1171 C CZ  . ARG A 150 ? 0.4729 0.4577 0.8810 -0.0879 -0.0466 0.0778  1002 ARG A CZ  
1172 N NH1 . ARG A 150 ? 0.4768 0.4658 0.8965 -0.0913 -0.0556 0.0547  1002 ARG A NH1 
1173 N NH2 . ARG A 150 ? 0.5468 0.5066 0.9815 -0.0890 -0.0557 0.0789  1002 ARG A NH2 
1174 N N   . ASP A 151 ? 0.2275 0.2011 0.4228 -0.0344 -0.0112 0.0218  1003 ASP A N   
1175 C CA  . ASP A 151 ? 0.2547 0.2213 0.4429 -0.0299 -0.0164 -0.0064 1003 ASP A CA  
1176 C C   . ASP A 151 ? 0.2377 0.2078 0.3835 -0.0224 -0.0084 -0.0107 1003 ASP A C   
1177 O O   . ASP A 151 ? 0.2508 0.2269 0.3787 -0.0195 -0.0087 -0.0295 1003 ASP A O   
1178 C CB  . ASP A 151 ? 0.2601 0.2358 0.4546 -0.0329 -0.0225 -0.0254 1003 ASP A CB  
1179 C CG  . ASP A 151 ? 0.3069 0.2793 0.5077 -0.0302 -0.0307 -0.0562 1003 ASP A CG  
1180 O OD1 . ASP A 151 ? 0.3708 0.3302 0.5874 -0.0270 -0.0342 -0.0636 1003 ASP A OD1 
1181 O OD2 . ASP A 151 ? 0.3160 0.3019 0.5067 -0.0306 -0.0340 -0.0737 1003 ASP A OD2 
1182 N N   . LEU A 152 ? 0.2230 0.1918 0.3541 -0.0202 -0.0019 0.0077  1004 LEU A N   
1183 C CA  . LEU A 152 ? 0.2061 0.1768 0.3011 -0.0146 0.0043  0.0055  1004 LEU A CA  
1184 C C   . LEU A 152 ? 0.2287 0.1922 0.3271 -0.0115 0.0005  -0.0068 1004 LEU A C   
1185 O O   . LEU A 152 ? 0.2365 0.1924 0.3514 -0.0110 -0.0026 0.0020  1004 LEU A O   
1186 C CB  . LEU A 152 ? 0.1943 0.1689 0.2725 -0.0131 0.0112  0.0260  1004 LEU A CB  
1187 C CG  . LEU A 152 ? 0.2651 0.2397 0.3084 -0.0081 0.0157  0.0224  1004 LEU A CG  
1188 C CD1 . LEU A 152 ? 0.3320 0.3098 0.3562 -0.0062 0.0178  0.0107  1004 LEU A CD1 
1189 C CD2 . LEU A 152 ? 0.2419 0.2232 0.2699 -0.0061 0.0212  0.0392  1004 LEU A CD2 
1190 N N   . ALA A 153 ? 0.1916 0.1607 0.2771 -0.0095 0.0003  -0.0260 1005 ALA A N   
1191 C CA  . ALA A 153 ? 0.2163 0.1862 0.3026 -0.0057 -0.0013 -0.0403 1005 ALA A CA  
1192 C C   . ALA A 153 ? 0.2141 0.1969 0.2697 -0.0051 0.0034  -0.0479 1005 ALA A C   
1193 O O   . ALA A 153 ? 0.1974 0.1862 0.2383 -0.0072 0.0051  -0.0458 1005 ALA A O   
1194 C CB  . ALA A 153 ? 0.2409 0.2095 0.3585 -0.0045 -0.0086 -0.0600 1005 ALA A CB  
1195 N N   . ALA A 154 ? 0.2174 0.2059 0.2662 -0.0025 0.0049  -0.0545 1006 ALA A N   
1196 C CA  . ALA A 154 ? 0.2104 0.2133 0.2336 -0.0037 0.0089  -0.0577 1006 ALA A CA  
1197 C C   . ALA A 154 ? 0.2241 0.2435 0.2419 -0.0052 0.0081  -0.0703 1006 ALA A C   
1198 O O   . ALA A 154 ? 0.2641 0.2927 0.2602 -0.0079 0.0103  -0.0642 1006 ALA A O   
1199 C CB  . ALA A 154 ? 0.1900 0.2022 0.2139 -0.0016 0.0106  -0.0638 1006 ALA A CB  
1200 N N   . ARG A 155 ? 0.2248 0.2484 0.2635 -0.0034 0.0036  -0.0880 1007 ARG A N   
1201 C CA  . ARG A 155 ? 0.2554 0.2986 0.2891 -0.0047 0.0010  -0.1034 1007 ARG A CA  
1202 C C   . ARG A 155 ? 0.2275 0.2686 0.2518 -0.0089 -0.0008 -0.0910 1007 ARG A C   
1203 O O   . ARG A 155 ? 0.2700 0.3305 0.2819 -0.0107 -0.0027 -0.0968 1007 ARG A O   
1204 C CB  . ARG A 155 ? 0.2750 0.3196 0.3374 -0.0015 -0.0057 -0.1285 1007 ARG A CB  
1205 C CG  . ARG A 155 ? 0.3132 0.3348 0.4054 -0.0037 -0.0126 -0.1238 1007 ARG A CG  
1206 C CD  . ARG A 155 ? 0.4535 0.4717 0.5810 -0.0005 -0.0215 -0.1502 1007 ARG A CD  
1207 N NE  . ARG A 155 ? 0.4668 0.4577 0.6294 -0.0025 -0.0273 -0.1378 1007 ARG A NE  
1208 C CZ  . ARG A 155 ? 0.5111 0.4922 0.6885 -0.0094 -0.0319 -0.1249 1007 ARG A CZ  
1209 N NH1 . ARG A 155 ? 0.5519 0.5118 0.7622 -0.0121 -0.0365 -0.1094 1007 ARG A NH1 
1210 N NH2 . ARG A 155 ? 0.5569 0.5516 0.7188 -0.0141 -0.0324 -0.1253 1007 ARG A NH2 
1211 N N   . ASN A 156 ? 0.2131 0.2349 0.2441 -0.0098 -0.0001 -0.0738 1008 ASN A N   
1212 C CA  . ASN A 156 ? 0.2059 0.2276 0.2316 -0.0121 -0.0005 -0.0614 1008 ASN A CA  
1213 C C   . ASN A 156 ? 0.1937 0.2112 0.1963 -0.0110 0.0049  -0.0440 1008 ASN A C   
1214 O O   . ASN A 156 ? 0.2037 0.2203 0.2047 -0.0106 0.0052  -0.0339 1008 ASN A O   
1215 C CB  . ASN A 156 ? 0.1839 0.1941 0.2366 -0.0139 -0.0033 -0.0557 1008 ASN A CB  
1216 C CG  . ASN A 156 ? 0.2461 0.2603 0.3254 -0.0165 -0.0121 -0.0741 1008 ASN A CG  
1217 O OD1 . ASN A 156 ? 0.2719 0.3028 0.3446 -0.0171 -0.0164 -0.0901 1008 ASN A OD1 
1218 N ND2 . ASN A 156 ? 0.2264 0.2264 0.3371 -0.0185 -0.0159 -0.0715 1008 ASN A ND2 
1219 N N   . VAL A 157 ? 0.1764 0.1926 0.1643 -0.0102 0.0082  -0.0421 1009 VAL A N   
1220 C CA  . VAL A 157 ? 0.2013 0.2113 0.1708 -0.0098 0.0110  -0.0289 1009 VAL A CA  
1221 C C   . VAL A 157 ? 0.2550 0.2807 0.2097 -0.0128 0.0100  -0.0286 1009 VAL A C   
1222 O O   . VAL A 157 ? 0.2723 0.3106 0.2244 -0.0145 0.0111  -0.0358 1009 VAL A O   
1223 C CB  . VAL A 157 ? 0.2203 0.2167 0.1867 -0.0086 0.0138  -0.0240 1009 VAL A CB  
1224 C CG1 . VAL A 157 ? 0.2403 0.2279 0.1905 -0.0082 0.0147  -0.0140 1009 VAL A CG1 
1225 C CG2 . VAL A 157 ? 0.2367 0.2233 0.2167 -0.0065 0.0146  -0.0205 1009 VAL A CG2 
1226 N N   . LEU A 158 ? 0.2293 0.2566 0.1764 -0.0129 0.0079  -0.0185 1010 LEU A N   
1227 C CA  . LEU A 158 ? 0.2370 0.2805 0.1717 -0.0166 0.0054  -0.0116 1010 LEU A CA  
1228 C C   . LEU A 158 ? 0.2492 0.2806 0.1760 -0.0185 0.0060  0.0017  1010 LEU A C   
1229 O O   . LEU A 158 ? 0.2113 0.2199 0.1402 -0.0150 0.0067  0.0054  1010 LEU A O   
1230 C CB  . LEU A 158 ? 0.2572 0.3089 0.1928 -0.0157 0.0003  -0.0050 1010 LEU A CB  
1231 C CG  . LEU A 158 ? 0.1774 0.2458 0.1219 -0.0158 -0.0033 -0.0179 1010 LEU A CG  
1232 C CD1 . LEU A 158 ? 0.2383 0.3153 0.1860 -0.0148 -0.0094 -0.0090 1010 LEU A CD1 
1233 C CD2 . LEU A 158 ? 0.2094 0.3037 0.1474 -0.0193 -0.0043 -0.0320 1010 LEU A CD2 
1234 N N   . VAL A 159 ? 0.2161 0.2653 0.1346 -0.0244 0.0051  0.0085  1011 VAL A N   
1235 C CA  . VAL A 159 ? 0.2618 0.3013 0.1773 -0.0289 0.0036  0.0234  1011 VAL A CA  
1236 C C   . VAL A 159 ? 0.2399 0.2803 0.1544 -0.0304 -0.0026 0.0410  1011 VAL A C   
1237 O O   . VAL A 159 ? 0.2875 0.3552 0.1958 -0.0349 -0.0047 0.0486  1011 VAL A O   
1238 C CB  . VAL A 159 ? 0.2296 0.2905 0.1416 -0.0358 0.0070  0.0236  1011 VAL A CB  
1239 C CG1 . VAL A 159 ? 0.2703 0.3228 0.1835 -0.0430 0.0039  0.0418  1011 VAL A CG1 
1240 C CG2 . VAL A 159 ? 0.2471 0.3041 0.1650 -0.0322 0.0118  0.0066  1011 VAL A CG2 
1241 N N   . GLU A 160 ? 0.2670 0.2794 0.1883 -0.0258 -0.0062 0.0469  1012 GLU A N   
1242 C CA  . GLU A 160 ? 0.3150 0.3213 0.2420 -0.0255 -0.0139 0.0647  1012 GLU A CA  
1243 C C   . GLU A 160 ? 0.3416 0.3476 0.2704 -0.0353 -0.0182 0.0827  1012 GLU A C   
1244 O O   . GLU A 160 ? 0.3618 0.3835 0.2914 -0.0410 -0.0237 0.1024  1012 GLU A O   
1245 C CB  . GLU A 160 ? 0.3269 0.3030 0.2641 -0.0153 -0.0157 0.0605  1012 GLU A CB  
1246 C CG  . GLU A 160 ? 0.3612 0.3222 0.3114 -0.0123 -0.0249 0.0764  1012 GLU A CG  
1247 C CD  . GLU A 160 ? 0.4312 0.4134 0.3844 -0.0123 -0.0304 0.0907  1012 GLU A CD  
1248 O OE1 . GLU A 160 ? 0.3959 0.3999 0.3435 -0.0106 -0.0272 0.0825  1012 GLU A OE1 
1249 O OE2 . GLU A 160 ? 0.5619 0.5389 0.5255 -0.0143 -0.0397 0.1110  1012 GLU A OE2 
1250 N N   . SER A 161 ? 0.3574 0.3467 0.2884 -0.0379 -0.0166 0.0775  1013 SER A N   
1251 C CA  . SER A 161 ? 0.3657 0.3561 0.3021 -0.0494 -0.0205 0.0936  1013 SER A CA  
1252 C C   . SER A 161 ? 0.3388 0.3260 0.2737 -0.0523 -0.0157 0.0808  1013 SER A C   
1253 O O   . SER A 161 ? 0.3093 0.2898 0.2392 -0.0449 -0.0105 0.0615  1013 SER A O   
1254 C CB  . SER A 161 ? 0.3974 0.3556 0.3504 -0.0490 -0.0313 0.1067  1013 SER A CB  
1255 O OG  . SER A 161 ? 0.3785 0.3041 0.3357 -0.0413 -0.0321 0.0884  1013 SER A OG  
1256 N N   . GLU A 162 ? 0.3646 0.3565 0.3066 -0.0637 -0.0185 0.0939  1014 GLU A N   
1257 C CA  . GLU A 162 ? 0.3351 0.3211 0.2804 -0.0672 -0.0169 0.0842  1014 GLU A CA  
1258 C C   . GLU A 162 ? 0.2827 0.2329 0.2293 -0.0584 -0.0204 0.0670  1014 GLU A C   
1259 O O   . GLU A 162 ? 0.3034 0.2522 0.2478 -0.0575 -0.0180 0.0544  1014 GLU A O   
1260 C CB  . GLU A 162 ? 0.3515 0.3414 0.3110 -0.0819 -0.0230 0.1048  1014 GLU A CB  
1261 C CG  . GLU A 162 ? 0.4525 0.4497 0.4174 -0.0883 -0.0212 0.0987  1014 GLU A CG  
1262 C CD  . GLU A 162 ? 0.4566 0.4501 0.4413 -0.1038 -0.0300 0.1197  1014 GLU A CD  
1263 O OE1 . GLU A 162 ? 0.4121 0.4231 0.4028 -0.1132 -0.0317 0.1449  1014 GLU A OE1 
1264 O OE2 . GLU A 162 ? 0.4460 0.4204 0.4411 -0.1073 -0.0361 0.1121  1014 GLU A OE2 
1265 N N   . HIS A 163 ? 0.3141 0.2385 0.2650 -0.0516 -0.0264 0.0673  1015 HIS A N   
1266 C CA  . HIS A 163 ? 0.3520 0.2468 0.3033 -0.0424 -0.0296 0.0503  1015 HIS A CA  
1267 C C   . HIS A 163 ? 0.3358 0.2299 0.2775 -0.0284 -0.0230 0.0367  1015 HIS A C   
1268 O O   . HIS A 163 ? 0.2919 0.1686 0.2316 -0.0197 -0.0238 0.0226  1015 HIS A O   
1269 C CB  . HIS A 163 ? 0.3552 0.2204 0.3237 -0.0433 -0.0418 0.0566  1015 HIS A CB  
1270 C CG  . HIS A 163 ? 0.4755 0.3401 0.4593 -0.0592 -0.0500 0.0743  1015 HIS A CG  
1271 N ND1 . HIS A 163 ? 0.4982 0.3613 0.4852 -0.0676 -0.0528 0.0689  1015 HIS A ND1 
1272 C CD2 . HIS A 163 ? 0.5282 0.3973 0.5269 -0.0693 -0.0563 0.1003  1015 HIS A CD2 
1273 C CE1 . HIS A 163 ? 0.4430 0.3096 0.4479 -0.0827 -0.0599 0.0901  1015 HIS A CE1 
1274 N NE2 . HIS A 163 ? 0.5347 0.4051 0.5466 -0.0843 -0.0619 0.1106  1015 HIS A NE2 
1275 N N   . GLN A 164 ? 0.2862 0.2020 0.2227 -0.0265 -0.0168 0.0403  1016 GLN A N   
1276 C CA  . GLN A 164 ? 0.2766 0.1924 0.2094 -0.0151 -0.0119 0.0307  1016 GLN A CA  
1277 C C   . GLN A 164 ? 0.2699 0.2110 0.1974 -0.0154 -0.0049 0.0283  1016 GLN A C   
1278 O O   . GLN A 164 ? 0.2554 0.2161 0.1821 -0.0214 -0.0053 0.0365  1016 GLN A O   
1279 C CB  . GLN A 164 ? 0.2973 0.2025 0.2400 -0.0088 -0.0172 0.0378  1016 GLN A CB  
1280 C CG  . GLN A 164 ? 0.3662 0.2720 0.3096 0.0038  -0.0123 0.0282  1016 GLN A CG  
1281 C CD  . GLN A 164 ? 0.4004 0.3003 0.3575 0.0107  -0.0181 0.0365  1016 GLN A CD  
1282 O OE1 . GLN A 164 ? 0.5204 0.4117 0.4871 0.0063  -0.0268 0.0503  1016 GLN A OE1 
1283 N NE2 . GLN A 164 ? 0.3781 0.2843 0.3391 0.0213  -0.0136 0.0301  1016 GLN A NE2 
1284 N N   . VAL A 165 ? 0.2631 0.2046 0.1880 -0.0091 0.0007  0.0169  1017 VAL A N   
1285 C CA  . VAL A 165 ? 0.2325 0.1927 0.1584 -0.0087 0.0053  0.0129  1017 VAL A CA  
1286 C C   . VAL A 165 ? 0.2432 0.2028 0.1745 -0.0007 0.0071  0.0111  1017 VAL A C   
1287 O O   . VAL A 165 ? 0.2333 0.1802 0.1658 0.0062  0.0074  0.0102  1017 VAL A O   
1288 C CB  . VAL A 165 ? 0.2353 0.2005 0.1609 -0.0103 0.0092  0.0045  1017 VAL A CB  
1289 C CG1 . VAL A 165 ? 0.2699 0.2446 0.1938 -0.0178 0.0083  0.0057  1017 VAL A CG1 
1290 C CG2 . VAL A 165 ? 0.2462 0.1977 0.1696 -0.0053 0.0111  0.0003  1017 VAL A CG2 
1291 N N   . LYS A 166 ? 0.2204 0.1964 0.1569 -0.0017 0.0082  0.0091  1018 LYS A N   
1292 C CA  . LYS A 166 ? 0.2256 0.2058 0.1715 0.0039  0.0100  0.0085  1018 LYS A CA  
1293 C C   . LYS A 166 ? 0.2452 0.2370 0.1998 0.0009  0.0118  0.0017  1018 LYS A C   
1294 O O   . LYS A 166 ? 0.2378 0.2404 0.1919 -0.0043 0.0095  -0.0036 1018 LYS A O   
1295 C CB  . LYS A 166 ? 0.2316 0.2207 0.1826 0.0054  0.0049  0.0155  1018 LYS A CB  
1296 C CG  . LYS A 166 ? 0.2183 0.1952 0.1676 0.0080  -0.0001 0.0251  1018 LYS A CG  
1297 C CD  . LYS A 166 ? 0.1976 0.1833 0.1572 0.0122  -0.0053 0.0335  1018 LYS A CD  
1298 C CE  . LYS A 166 ? 0.2840 0.2565 0.2476 0.0143  -0.0128 0.0460  1018 LYS A CE  
1299 N NZ  . LYS A 166 ? 0.2890 0.2700 0.2667 0.0202  -0.0192 0.0561  1018 LYS A NZ  
1300 N N   . ILE A 167 ? 0.2146 0.2061 0.1790 0.0043  0.0156  0.0020  1019 ILE A N   
1301 C CA  . ILE A 167 ? 0.1902 0.1907 0.1706 0.0005  0.0151  -0.0020 1019 ILE A CA  
1302 C C   . ILE A 167 ? 0.2044 0.2198 0.1924 -0.0016 0.0094  -0.0041 1019 ILE A C   
1303 O O   . ILE A 167 ? 0.1904 0.2110 0.1807 0.0021  0.0084  0.0022  1019 ILE A O   
1304 C CB  . ILE A 167 ? 0.2256 0.2263 0.2180 0.0027  0.0202  0.0039  1019 ILE A CB  
1305 C CG1 . ILE A 167 ? 0.2212 0.2118 0.2021 0.0050  0.0247  0.0067  1019 ILE A CG1 
1306 C CG2 . ILE A 167 ? 0.2170 0.2234 0.2320 -0.0031 0.0173  0.0018  1019 ILE A CG2 
1307 C CD1 . ILE A 167 ? 0.3156 0.3125 0.2999 0.0090  0.0311  0.0150  1019 ILE A CD1 
1308 N N   . GLY A 168 ? 0.1634 0.1875 0.1559 -0.0067 0.0050  -0.0145 1020 GLY A N   
1309 C CA  . GLY A 168 ? 0.1815 0.2237 0.1735 -0.0094 -0.0018 -0.0195 1020 GLY A CA  
1310 C C   . GLY A 168 ? 0.1880 0.2421 0.2002 -0.0130 -0.0079 -0.0288 1020 GLY A C   
1311 O O   . GLY A 168 ? 0.1500 0.2224 0.1602 -0.0152 -0.0148 -0.0336 1020 GLY A O   
1312 N N   . ASP A 169 ? 0.2072 0.2523 0.2402 -0.0146 -0.0067 -0.0308 1021 ASP A N   
1313 C CA  . ASP A 169 ? 0.2168 0.2705 0.2757 -0.0196 -0.0142 -0.0390 1021 ASP A CA  
1314 C C   . ASP A 169 ? 0.1681 0.2129 0.2508 -0.0210 -0.0105 -0.0270 1021 ASP A C   
1315 O O   . ASP A 169 ? 0.1865 0.2180 0.2663 -0.0191 -0.0039 -0.0195 1021 ASP A O   
1316 C CB  . ASP A 169 ? 0.1893 0.2439 0.2547 -0.0225 -0.0201 -0.0605 1021 ASP A CB  
1317 C CG  . ASP A 169 ? 0.2645 0.3262 0.3583 -0.0281 -0.0306 -0.0736 1021 ASP A CG  
1318 O OD1 . ASP A 169 ? 0.2010 0.2830 0.2898 -0.0300 -0.0383 -0.0835 1021 ASP A OD1 
1319 O OD2 . ASP A 169 ? 0.2381 0.2856 0.3608 -0.0313 -0.0321 -0.0724 1021 ASP A OD2 
1320 N N   . PHE A 170 ? 0.2047 0.2606 0.3117 -0.0253 -0.0156 -0.0245 1022 PHE A N   
1321 C CA  . PHE A 170 ? 0.1830 0.2383 0.3163 -0.0284 -0.0119 -0.0093 1022 PHE A CA  
1322 C C   . PHE A 170 ? 0.1799 0.2385 0.3512 -0.0382 -0.0227 -0.0159 1022 PHE A C   
1323 O O   . PHE A 170 ? 0.1883 0.2564 0.3863 -0.0431 -0.0226 -0.0025 1022 PHE A O   
1324 C CB  . PHE A 170 ? 0.1845 0.2538 0.3131 -0.0231 -0.0049 0.0059  1022 PHE A CB  
1325 C CG  . PHE A 170 ? 0.1401 0.2015 0.2373 -0.0136 0.0042  0.0105  1022 PHE A CG  
1326 C CD1 . PHE A 170 ? 0.1614 0.2220 0.2350 -0.0092 0.0014  0.0041  1022 PHE A CD1 
1327 C CD2 . PHE A 170 ? 0.1686 0.2232 0.2600 -0.0102 0.0142  0.0209  1022 PHE A CD2 
1328 C CE1 . PHE A 170 ? 0.1352 0.1849 0.1846 -0.0020 0.0077  0.0078  1022 PHE A CE1 
1329 C CE2 . PHE A 170 ? 0.2388 0.2845 0.3023 -0.0020 0.0206  0.0214  1022 PHE A CE2 
1330 C CZ  . PHE A 170 ? 0.1603 0.2013 0.2048 0.0017  0.0168  0.0143  1022 PHE A CZ  
1331 N N   . GLY A 171 ? 0.1666 0.2186 0.3419 -0.0409 -0.0322 -0.0377 1023 GLY A N   
1332 C CA  . GLY A 171 ? 0.2305 0.2823 0.4429 -0.0497 -0.0457 -0.0514 1023 GLY A CA  
1333 C C   . GLY A 171 ? 0.2198 0.2599 0.4737 -0.0574 -0.0471 -0.0363 1023 GLY A C   
1334 O O   . GLY A 171 ? 0.2316 0.2764 0.5226 -0.0668 -0.0579 -0.0387 1023 GLY A O   
1335 N N   . LEU A 172 ? 0.2184 0.2451 0.4677 -0.0546 -0.0376 -0.0196 1024 LEU A N   
1336 C CA  . LEU A 172 ? 0.2519 0.2692 0.5390 -0.0623 -0.0386 0.0004  1024 LEU A CA  
1337 C C   . LEU A 172 ? 0.2553 0.2874 0.5366 -0.0620 -0.0250 0.0321  1024 LEU A C   
1338 O O   . LEU A 172 ? 0.2457 0.2760 0.5527 -0.0683 -0.0234 0.0544  1024 LEU A O   
1339 C CB  . LEU A 172 ? 0.2407 0.2342 0.5328 -0.0596 -0.0406 -0.0039 1024 LEU A CB  
1340 C CG  . LEU A 172 ? 0.2952 0.2746 0.6018 -0.0587 -0.0538 -0.0369 1024 LEU A CG  
1341 C CD1 . LEU A 172 ? 0.3855 0.3426 0.7048 -0.0551 -0.0552 -0.0359 1024 LEU A CD1 
1342 C CD2 . LEU A 172 ? 0.3474 0.3255 0.6993 -0.0689 -0.0695 -0.0487 1024 LEU A CD2 
1343 N N   . THR A 173 ? 0.2252 0.2742 0.4752 -0.0545 -0.0155 0.0344  1025 THR A N   
1344 C CA  . THR A 173 ? 0.2079 0.2724 0.4455 -0.0503 -0.0009 0.0582  1025 THR A CA  
1345 C C   . THR A 173 ? 0.2051 0.2917 0.4804 -0.0594 0.0002  0.0794  1025 THR A C   
1346 O O   . THR A 173 ? 0.1870 0.2846 0.4849 -0.0649 -0.0078 0.0731  1025 THR A O   
1347 C CB  . THR A 173 ? 0.1935 0.2674 0.3921 -0.0383 0.0071  0.0514  1025 THR A CB  
1348 O OG1 . THR A 173 ? 0.2242 0.2796 0.3897 -0.0315 0.0080  0.0387  1025 THR A OG1 
1349 C CG2 . THR A 173 ? 0.2361 0.3305 0.4262 -0.0322 0.0216  0.0704  1025 THR A CG2 
1350 N N   . LYS A 174 ? 0.2209 0.3177 0.5027 -0.0614 0.0100  0.1052  1026 LYS A N   
1351 C CA  . LYS A 174 ? 0.2430 0.3657 0.5635 -0.0718 0.0128  0.1310  1026 LYS A CA  
1352 C C   . LYS A 174 ? 0.2346 0.3883 0.5358 -0.0646 0.0315  0.1517  1026 LYS A C   
1353 O O   . LYS A 174 ? 0.2203 0.3697 0.4865 -0.0556 0.0401  0.1527  1026 LYS A O   
1354 C CB  . LYS A 174 ? 0.2705 0.3795 0.6313 -0.0856 0.0040  0.1483  1026 LYS A CB  
1355 C CG  . LYS A 174 ? 0.2948 0.3746 0.6849 -0.0931 -0.0157 0.1263  1026 LYS A CG  
1356 C CD  . LYS A 174 ? 0.3607 0.4523 0.7863 -0.1026 -0.0264 0.1185  1026 LYS A CD  
1357 C CE  . LYS A 174 ? 0.3516 0.4143 0.8036 -0.1088 -0.0471 0.0907  1026 LYS A CE  
1358 N NZ  . LYS A 174 ? 0.2720 0.3456 0.7690 -0.1218 -0.0607 0.0867  1026 LYS A NZ  
1359 N N   . ALA A 175 ? 0.2441 0.4321 0.5698 -0.0684 0.0374  0.1670  1027 ALA A N   
1360 C CA  . ALA A 175 ? 0.2332 0.4595 0.5477 -0.0623 0.0562  0.1880  1027 ALA A CA  
1361 C C   . ALA A 175 ? 0.2731 0.5109 0.6050 -0.0732 0.0605  0.2205  1027 ALA A C   
1362 O O   . ALA A 175 ? 0.3201 0.5506 0.6962 -0.0896 0.0494  0.2357  1027 ALA A O   
1363 C CB  . ALA A 175 ? 0.2027 0.4669 0.5421 -0.0625 0.0616  0.1943  1027 ALA A CB  
1364 N N   . ILE A 176 ? 0.2721 0.5278 0.5700 -0.0642 0.0751  0.2307  1028 ILE A N   
1365 C CA  . ILE A 176 ? 0.2805 0.5633 0.5913 -0.0733 0.0826  0.2672  1028 ILE A CA  
1366 C C   . ILE A 176 ? 0.3004 0.6407 0.6250 -0.0732 0.0989  0.2870  1028 ILE A C   
1367 O O   . ILE A 176 ? 0.2764 0.6397 0.5734 -0.0572 0.1118  0.2713  1028 ILE A O   
1368 C CB  . ILE A 176 ? 0.2964 0.5772 0.5615 -0.0638 0.0898  0.2688  1028 ILE A CB  
1369 C CG1 . ILE A 176 ? 0.3423 0.5701 0.5951 -0.0628 0.0746  0.2490  1028 ILE A CG1 
1370 C CG2 . ILE A 176 ? 0.2761 0.5914 0.5540 -0.0740 0.0969  0.3108  1028 ILE A CG2 
1371 C CD1 . ILE A 176 ? 0.4354 0.6597 0.6549 -0.0580 0.0772  0.2569  1028 ILE A CD1 
1372 N N   . GLU A 177 ? 0.3368 0.7017 0.7068 -0.0908 0.0984  0.3224  1029 GLU A N   
1373 C CA  . GLU A 177 ? 0.3815 0.8079 0.7709 -0.0931 0.1146  0.3461  1029 GLU A CA  
1374 C C   . GLU A 177 ? 0.3928 0.8633 0.7362 -0.0781 0.1369  0.3522  1029 GLU A C   
1375 O O   . GLU A 177 ? 0.4000 0.8623 0.7123 -0.0758 0.1380  0.3586  1029 GLU A O   
1376 C CB  . GLU A 177 ? 0.3965 0.8396 0.8451 -0.1178 0.1086  0.3886  1029 GLU A CB  
1377 C CG  . GLU A 177 ? 0.4864 0.9939 0.9684 -0.1244 0.1228  0.4151  1029 GLU A CG  
1378 C CD  . GLU A 177 ? 0.5367 1.0647 1.0735 -0.1499 0.1185  0.4647  1029 GLU A CD  
1379 O OE1 . GLU A 177 ? 0.6047 1.0855 1.1738 -0.1650 0.0974  0.4705  1029 GLU A OE1 
1380 O OE2 . GLU A 177 ? 0.6698 1.2627 1.2194 -0.1548 0.1362  0.4983  1029 GLU A OE2 
1381 N N   . THR A 178 ? 0.3942 0.9132 0.7346 -0.0672 0.1537  0.3482  1030 THR A N   
1382 C CA  . THR A 178 ? 0.4153 0.9839 0.7151 -0.0513 0.1758  0.3494  1030 THR A CA  
1383 C C   . THR A 178 ? 0.4218 1.0325 0.7302 -0.0657 0.1840  0.3954  1030 THR A C   
1384 O O   . THR A 178 ? 0.4367 1.0649 0.7962 -0.0864 0.1803  0.4310  1030 THR A O   
1385 C CB  . THR A 178 ? 0.4239 1.0415 0.7315 -0.0374 0.1919  0.3381  1030 THR A CB  
1386 O OG1 . THR A 178 ? 0.4347 1.0116 0.7418 -0.0266 0.1810  0.3013  1030 THR A OG1 
1387 C CG2 . THR A 178 ? 0.4259 1.0928 0.6883 -0.0168 0.2145  0.3294  1030 THR A CG2 
1388 N N   . ASP A 179 ? 0.4475 1.0725 0.7069 -0.0556 0.1930  0.3949  1031 ASP A N   
1389 C CA  . ASP A 179 ? 0.4753 1.1385 0.7320 -0.0677 0.1991  0.4386  1031 ASP A CA  
1390 C C   . ASP A 179 ? 0.4760 1.0930 0.7625 -0.0890 0.1777  0.4662  1031 ASP A C   
1391 O O   . ASP A 179 ? 0.4730 1.1212 0.7746 -0.1038 0.1796  0.5118  1031 ASP A O   
1392 C CB  . ASP A 179 ? 0.5085 1.2541 0.7926 -0.0751 0.2188  0.4755  1031 ASP A CB  
1393 C CG  . ASP A 179 ? 0.5202 1.3168 0.7779 -0.0517 0.2410  0.4473  1031 ASP A CG  
1394 O OD1 . ASP A 179 ? 0.6332 1.4264 0.8358 -0.0302 0.2473  0.4132  1031 ASP A OD1 
1395 O OD2 . ASP A 179 ? 0.5578 1.3980 0.8531 -0.0547 0.2513  0.4585  1031 ASP A OD2 
1396 N N   . LYS A 180 ? 0.4123 0.9580 0.7081 -0.0898 0.1576  0.4391  1032 LYS A N   
1397 C CA  . LYS A 180 ? 0.4249 0.9207 0.7462 -0.1051 0.1365  0.4553  1032 LYS A CA  
1398 C C   . LYS A 180 ? 0.3984 0.8413 0.6765 -0.0915 0.1266  0.4193  1032 LYS A C   
1399 O O   . LYS A 180 ? 0.4121 0.8386 0.6583 -0.0750 0.1295  0.3779  1032 LYS A O   
1400 C CB  . LYS A 180 ? 0.4262 0.8867 0.8093 -0.1210 0.1192  0.4560  1032 LYS A CB  
1401 C CG  . LYS A 180 ? 0.4386 0.9454 0.8748 -0.1377 0.1251  0.4916  1032 LYS A CG  
1402 C CD  . LYS A 180 ? 0.5411 1.0846 1.0008 -0.1550 0.1281  0.5491  1032 LYS A CD  
1403 C CE  . LYS A 180 ? 0.5390 1.1227 1.0630 -0.1759 0.1303  0.5874  1032 LYS A CE  
1404 N NZ  . LYS A 180 ? 0.5747 1.1969 1.1251 -0.1947 0.1328  0.6490  1032 LYS A NZ  
1405 N N   . GLU A 181 ? 0.3822 0.7988 0.6643 -0.0993 0.1139  0.4370  1033 GLU A N   
1406 C CA  . GLU A 181 ? 0.4085 0.7814 0.6521 -0.0878 0.1047  0.4087  1033 GLU A CA  
1407 C C   . GLU A 181 ? 0.3766 0.6832 0.6450 -0.0904 0.0846  0.3832  1033 GLU A C   
1408 O O   . GLU A 181 ? 0.3615 0.6342 0.5990 -0.0799 0.0784  0.3552  1033 GLU A O   
1409 C CB  . GLU A 181 ? 0.4349 0.8215 0.6644 -0.0919 0.1024  0.4410  1033 GLU A CB  
1410 C CG  . GLU A 181 ? 0.5427 0.9962 0.7310 -0.0851 0.1221  0.4575  1033 GLU A CG  
1411 C CD  . GLU A 181 ? 0.5511 1.0227 0.7259 -0.0906 0.1179  0.4934  1033 GLU A CD  
1412 O OE1 . GLU A 181 ? 0.5557 0.9846 0.7206 -0.0878 0.1031  0.4826  1033 GLU A OE1 
1413 O OE2 . GLU A 181 ? 0.5817 1.1143 0.7558 -0.0976 0.1296  0.5334  1033 GLU A OE2 
1414 N N   . PTR A 182 ? 0.3658 0.6566 0.6898 -0.1044 0.0741  0.3915  1034 PTR A N   
1415 C CA  . PTR A 182 ? 0.3426 0.5755 0.6916 -0.1068 0.0547  0.3655  1034 PTR A CA  
1416 C C   . PTR A 182 ? 0.3491 0.5718 0.7476 -0.1175 0.0460  0.3587  1034 PTR A C   
1417 O O   . PTR A 182 ? 0.3381 0.5972 0.7649 -0.1275 0.0527  0.3831  1034 PTR A O   
1418 C CB  . PTR A 182 ? 0.4062 0.6100 0.7809 -0.1150 0.0391  0.3861  1034 PTR A CB  
1419 C CG  . PTR A 182 ? 0.3953 0.6138 0.8286 -0.1350 0.0327  0.4345  1034 PTR A CG  
1420 C CD1 . PTR A 182 ? 0.4760 0.7319 0.9034 -0.1403 0.0398  0.4796  1034 PTR A CD1 
1421 C CD2 . PTR A 182 ? 0.3476 0.5423 0.8439 -0.1493 0.0177  0.4360  1034 PTR A CD2 
1422 C CE1 . PTR A 182 ? 0.4796 0.7503 0.9635 -0.1601 0.0332  0.5293  1034 PTR A CE1 
1423 C CE2 . PTR A 182 ? 0.4371 0.6428 0.9932 -0.1694 0.0101  0.4828  1034 PTR A CE2 
1424 C CZ  . PTR A 182 ? 0.4682 0.7120 1.0188 -0.1751 0.0181  0.5315  1034 PTR A CZ  
1425 O OH  . PTR A 182 ? 0.5742 0.8269 1.1820 -0.1944 0.0100  0.5766  1034 PTR A OH  
1426 P P   . PTR A 182 ? 0.6355 0.9601 1.2537 -0.2085 0.0261  0.6363  1034 PTR A P   
1427 O O1P . PTR A 182 ? 0.6826 1.0566 1.2716 -0.2022 0.0485  0.6203  1034 PTR A O1P 
1428 O O2P . PTR A 182 ? 0.6456 0.9989 1.2204 -0.2023 0.0343  0.6641  1034 PTR A O2P 
1429 O O3P . PTR A 182 ? 0.5515 0.8673 1.2577 -0.2348 0.0092  0.6803  1034 PTR A O3P 
1430 N N   . PTR A 183 ? 0.3624 0.5384 0.7713 -0.1156 0.0306  0.3253  1035 PTR A N   
1431 C CA  . PTR A 183 ? 0.3670 0.5269 0.8215 -0.1254 0.0178  0.3118  1035 PTR A CA  
1432 C C   . PTR A 183 ? 0.3770 0.4954 0.8794 -0.1361 -0.0034 0.3147  1035 PTR A C   
1433 O O   . PTR A 183 ? 0.3343 0.4202 0.8205 -0.1279 -0.0105 0.2974  1035 PTR A O   
1434 C CB  . PTR A 183 ? 0.3768 0.5179 0.8015 -0.1128 0.0159  0.2651  1035 PTR A CB  
1435 C CG  . PTR A 183 ? 0.3887 0.5133 0.8556 -0.1219 0.0002  0.2462  1035 PTR A CG  
1436 C CD1 . PTR A 183 ? 0.4016 0.4839 0.8803 -0.1215 -0.0172 0.2165  1035 PTR A CD1 
1437 C CD2 . PTR A 183 ? 0.4171 0.5717 0.9111 -0.1301 0.0027  0.2557  1035 PTR A CD2 
1438 C CE1 . PTR A 183 ? 0.4530 0.5232 0.9677 -0.1294 -0.0326 0.1955  1035 PTR A CE1 
1439 C CE2 . PTR A 183 ? 0.4949 0.6367 1.0272 -0.1391 -0.0134 0.2370  1035 PTR A CE2 
1440 C CZ  . PTR A 183 ? 0.4607 0.5597 1.0020 -0.1388 -0.0317 0.2056  1035 PTR A CZ  
1441 O OH  . PTR A 183 ? 0.4868 0.5739 1.0593 -0.1460 -0.0479 0.1839  1035 PTR A OH  
1442 P P   . PTR A 183 ? 0.5861 0.7015 1.1965 -0.1580 -0.0533 0.1870  1035 PTR A P   
1443 O O1P . PTR A 183 ? 0.4980 0.5866 1.1478 -0.1672 -0.0786 0.1558  1035 PTR A O1P 
1444 O O2P . PTR A 183 ? 0.5444 0.6876 1.2010 -0.1743 -0.0482 0.2339  1035 PTR A O2P 
1445 O O3P . PTR A 183 ? 0.5250 0.6686 1.0908 -0.1446 -0.0401 0.1749  1035 PTR A O3P 
1446 N N   . THR A 184 ? 0.3871 0.5069 0.9521 -0.1542 -0.0142 0.3356  1036 THR A N   
1447 C CA  . THR A 184 ? 0.4223 0.5002 1.0428 -0.1648 -0.0368 0.3367  1036 THR A CA  
1448 C C   . THR A 184 ? 0.4299 0.4758 1.0652 -0.1629 -0.0520 0.2892  1036 THR A C   
1449 O O   . THR A 184 ? 0.4145 0.4763 1.0653 -0.1692 -0.0530 0.2805  1036 THR A O   
1450 C CB  . THR A 184 ? 0.4528 0.5450 1.1407 -0.1872 -0.0438 0.3840  1036 THR A CB  
1451 O OG1 . THR A 184 ? 0.4525 0.5969 1.1196 -0.1896 -0.0237 0.4271  1036 THR A OG1 
1452 C CG2 . THR A 184 ? 0.5344 0.5852 1.2709 -0.1946 -0.0641 0.3972  1036 THR A CG2 
1453 N N   . VAL A 185 ? 0.4613 0.4668 1.0910 -0.1538 -0.0636 0.2582  1037 VAL A N   
1454 C CA  . VAL A 185 ? 0.4980 0.4768 1.1385 -0.1508 -0.0782 0.2104  1037 VAL A CA  
1455 C C   . VAL A 185 ? 0.5518 0.5025 1.2698 -0.1664 -0.1020 0.2109  1037 VAL A C   
1456 O O   . VAL A 185 ? 0.5697 0.4952 1.3243 -0.1701 -0.1126 0.2278  1037 VAL A O   
1457 C CB  . VAL A 185 ? 0.5261 0.4802 1.1241 -0.1327 -0.0786 0.1726  1037 VAL A CB  
1458 C CG1 . VAL A 185 ? 0.4975 0.4780 1.0227 -0.1189 -0.0574 0.1678  1037 VAL A CG1 
1459 C CG2 . VAL A 185 ? 0.5213 0.4476 1.1314 -0.1279 -0.0858 0.1757  1037 VAL A CG2 
1460 N N   . LYS A 186 ? 0.5816 0.5373 1.3273 -0.1756 -0.1116 0.1934  1038 LYS A N   
1461 C CA  . LYS A 186 ? 0.6314 0.5578 1.4508 -0.1899 -0.1372 0.1829  1038 LYS A CA  
1462 C C   . LYS A 186 ? 0.6456 0.5360 1.4576 -0.1767 -0.1508 0.1284  1038 LYS A C   
1463 O O   . LYS A 186 ? 0.6767 0.5308 1.5300 -0.1768 -0.1663 0.1224  1038 LYS A O   
1464 C CB  . LYS A 186 ? 0.6185 0.5676 1.4684 -0.2047 -0.1433 0.1816  1038 LYS A CB  
1465 C CG  . LYS A 186 ? 0.6276 0.6192 1.4905 -0.2181 -0.1293 0.2339  1038 LYS A CG  
1466 C CD  . LYS A 186 ? 0.6269 0.6434 1.5198 -0.2312 -0.1358 0.2284  1038 LYS A CD  
1467 C CE  . LYS A 186 ? 0.6231 0.6887 1.5294 -0.2433 -0.1196 0.2801  1038 LYS A CE  
1468 N NZ  . LYS A 186 ? 0.6221 0.7153 1.5614 -0.2560 -0.1262 0.2758  1038 LYS A NZ  
1469 N N   . ASP A 187 ? 0.6278 0.5315 1.3881 -0.1649 -0.1445 0.0902  1039 ASP A N   
1470 C CA  . ASP A 187 ? 0.6419 0.5235 1.3837 -0.1510 -0.1533 0.0378  1039 ASP A CA  
1471 C C   . ASP A 187 ? 0.6185 0.4931 1.3124 -0.1336 -0.1396 0.0377  1039 ASP A C   
1472 O O   . ASP A 187 ? 0.5940 0.4927 1.2296 -0.1254 -0.1197 0.0496  1039 ASP A O   
1473 C CB  . ASP A 187 ? 0.6359 0.5411 1.3393 -0.1465 -0.1514 0.0036  1039 ASP A CB  
1474 C CG  . ASP A 187 ? 0.7034 0.5955 1.3823 -0.1322 -0.1584 -0.0493 1039 ASP A CG  
1475 O OD1 . ASP A 187 ? 0.8373 0.7114 1.5582 -0.1364 -0.1793 -0.0824 1039 ASP A OD1 
1476 O OD2 . ASP A 187 ? 0.6227 0.5246 1.2416 -0.1172 -0.1433 -0.0581 1039 ASP A OD2 
1477 N N   . ASP A 188 ? 0.6267 0.4684 1.3490 -0.1279 -0.1514 0.0230  1040 ASP A N   
1478 C CA  . ASP A 188 ? 0.5980 0.4319 1.2831 -0.1114 -0.1416 0.0193  1040 ASP A CA  
1479 C C   . ASP A 188 ? 0.6182 0.4304 1.3079 -0.0977 -0.1525 -0.0322 1040 ASP A C   
1480 O O   . ASP A 188 ? 0.6220 0.4243 1.2975 -0.0850 -0.1482 -0.0358 1040 ASP A O   
1481 C CB  . ASP A 188 ? 0.5990 0.4220 1.3110 -0.1157 -0.1407 0.0669  1040 ASP A CB  
1482 C CG  . ASP A 188 ? 0.6355 0.4266 1.4319 -0.1276 -0.1635 0.0772  1040 ASP A CG  
1483 O OD1 . ASP A 188 ? 0.5497 0.3225 1.3847 -0.1305 -0.1811 0.0408  1040 ASP A OD1 
1484 O OD2 . ASP A 188 ? 0.7040 0.4891 1.5297 -0.1345 -0.1649 0.1225  1040 ASP A OD2 
1485 N N   . ARG A 189 ? 0.6549 0.4642 1.3632 -0.0998 -0.1661 -0.0730 1041 ARG A N   
1486 C CA  . ARG A 189 ? 0.6807 0.4791 1.3868 -0.0856 -0.1745 -0.1270 1041 ARG A CA  
1487 C C   . ARG A 189 ? 0.6673 0.4969 1.2965 -0.0734 -0.1571 -0.1473 1041 ARG A C   
1488 O O   . ARG A 189 ? 0.6914 0.5477 1.2808 -0.0783 -0.1456 -0.1318 1041 ARG A O   
1489 C CB  . ARG A 189 ? 0.7121 0.4983 1.4679 -0.0927 -0.1974 -0.1652 1041 ARG A CB  
1490 C CG  . ARG A 189 ? 0.7455 0.5158 1.5165 -0.0775 -0.2091 -0.2207 1041 ARG A CG  
1491 C CD  . ARG A 189 ? 0.7813 0.5386 1.6048 -0.0849 -0.2340 -0.2608 1041 ARG A CD  
1492 N NE  . ARG A 189 ? 0.7720 0.5634 1.5586 -0.0909 -0.2328 -0.2793 1041 ARG A NE  
1493 C CZ  . ARG A 189 ? 0.7642 0.5864 1.4929 -0.0791 -0.2251 -0.3167 1041 ARG A CZ  
1494 N NH1 . ARG A 189 ? 0.7634 0.5896 1.4623 -0.0603 -0.2160 -0.3419 1041 ARG A NH1 
1495 N NH2 . ARG A 189 ? 0.7574 0.6102 1.4589 -0.0864 -0.2266 -0.3268 1041 ARG A NH2 
1496 N N   . ASP A 190 ? 0.6588 0.4859 1.2711 -0.0574 -0.1555 -0.1808 1042 ASP A N   
1497 C CA  . ASP A 190 ? 0.6249 0.4802 1.1677 -0.0455 -0.1381 -0.1936 1042 ASP A CA  
1498 C C   . ASP A 190 ? 0.5679 0.4331 1.0693 -0.0454 -0.1190 -0.1494 1042 ASP A C   
1499 O O   . ASP A 190 ? 0.5794 0.4695 1.0251 -0.0418 -0.1051 -0.1486 1042 ASP A O   
1500 C CB  . ASP A 190 ? 0.6305 0.5151 1.1397 -0.0477 -0.1382 -0.2201 1042 ASP A CB  
1501 C CG  . ASP A 190 ? 0.6874 0.5666 1.2344 -0.0484 -0.1584 -0.2670 1042 ASP A CG  
1502 O OD1 . ASP A 190 ? 0.7100 0.5708 1.2890 -0.0390 -0.1675 -0.2962 1042 ASP A OD1 
1503 O OD2 . ASP A 190 ? 0.7412 0.6362 1.2870 -0.0576 -0.1659 -0.2765 1042 ASP A OD2 
1504 N N   . SER A 191 ? 0.5257 0.3720 1.0556 -0.0491 -0.1195 -0.1136 1043 SER A N   
1505 C CA  . SER A 191 ? 0.4798 0.3358 0.9729 -0.0481 -0.1031 -0.0744 1043 SER A CA  
1506 C C   . SER A 191 ? 0.4214 0.2796 0.8837 -0.0335 -0.0948 -0.0861 1043 SER A C   
1507 O O   . SER A 191 ? 0.3957 0.2376 0.8886 -0.0253 -0.1038 -0.1067 1043 SER A O   
1508 C CB  . SER A 191 ? 0.5071 0.3474 1.0416 -0.0574 -0.1077 -0.0311 1043 SER A CB  
1509 O OG  . SER A 191 ? 0.5773 0.4250 1.1315 -0.0723 -0.1102 -0.0100 1043 SER A OG  
1510 N N   . PRO A 192 ? 0.3716 0.2499 0.7773 -0.0299 -0.0785 -0.0736 1044 PRO A N   
1511 C CA  . PRO A 192 ? 0.3377 0.2194 0.7173 -0.0183 -0.0710 -0.0791 1044 PRO A CA  
1512 C C   . PRO A 192 ? 0.3110 0.1786 0.7108 -0.0176 -0.0725 -0.0472 1044 PRO A C   
1513 O O   . PRO A 192 ? 0.2922 0.1698 0.6597 -0.0183 -0.0623 -0.0205 1044 PRO A O   
1514 C CB  . PRO A 192 ? 0.3087 0.2143 0.6276 -0.0177 -0.0559 -0.0739 1044 PRO A CB  
1515 C CG  . PRO A 192 ? 0.3027 0.2135 0.6186 -0.0279 -0.0531 -0.0486 1044 PRO A CG  
1516 C CD  . PRO A 192 ? 0.3573 0.2563 0.7237 -0.0359 -0.0673 -0.0559 1044 PRO A CD  
1517 N N   . VAL A 193 ? 0.3495 0.1943 0.8044 -0.0158 -0.0866 -0.0516 1045 VAL A N   
1518 C CA  . VAL A 193 ? 0.3334 0.1634 0.8191 -0.0171 -0.0921 -0.0165 1045 VAL A CA  
1519 C C   . VAL A 193 ? 0.3536 0.1934 0.8075 -0.0083 -0.0835 -0.0037 1045 VAL A C   
1520 O O   . VAL A 193 ? 0.3689 0.2101 0.8218 -0.0123 -0.0825 0.0343  1045 VAL A O   
1521 C CB  . VAL A 193 ? 0.3793 0.1798 0.9362 -0.0149 -0.1111 -0.0273 1045 VAL A CB  
1522 C CG1 . VAL A 193 ? 0.3729 0.1617 0.9685 -0.0274 -0.1221 -0.0298 1045 VAL A CG1 
1523 C CG2 . VAL A 193 ? 0.3906 0.1881 0.9552 0.0011  -0.1145 -0.0739 1045 VAL A CG2 
1524 N N   . PHE A 194 ? 0.3409 0.1915 0.7682 0.0026  -0.0776 -0.0343 1046 PHE A N   
1525 C CA  . PHE A 194 ? 0.3271 0.1886 0.7271 0.0100  -0.0706 -0.0249 1046 PHE A CA  
1526 C C   . PHE A 194 ? 0.2974 0.1786 0.6393 0.0047  -0.0568 -0.0044 1046 PHE A C   
1527 O O   . PHE A 194 ? 0.3023 0.1922 0.6220 0.0083  -0.0525 0.0078  1046 PHE A O   
1528 C CB  . PHE A 194 ? 0.3041 0.1736 0.7025 0.0230  -0.0691 -0.0633 1046 PHE A CB  
1529 C CG  . PHE A 194 ? 0.3242 0.1750 0.7821 0.0314  -0.0830 -0.0870 1046 PHE A CG  
1530 C CD1 . PHE A 194 ? 0.3810 0.2121 0.8863 0.0350  -0.0947 -0.0668 1046 PHE A CD1 
1531 C CD2 . PHE A 194 ? 0.3209 0.1743 0.7895 0.0361  -0.0856 -0.1298 1046 PHE A CD2 
1532 C CE1 . PHE A 194 ? 0.3657 0.1755 0.9328 0.0441  -0.1093 -0.0898 1046 PHE A CE1 
1533 C CE2 . PHE A 194 ? 0.3349 0.1698 0.8617 0.0454  -0.0995 -0.1569 1046 PHE A CE2 
1534 C CZ  . PHE A 194 ? 0.3442 0.1552 0.9225 0.0498  -0.1116 -0.1371 1046 PHE A CZ  
1535 N N   . TRP A 195 ? 0.2791 0.1670 0.6008 -0.0036 -0.0513 -0.0013 1047 TRP A N   
1536 C CA  . TRP A 195 ? 0.2524 0.1566 0.5268 -0.0081 -0.0395 0.0183  1047 TRP A CA  
1537 C C   . TRP A 195 ? 0.2691 0.1743 0.5536 -0.0170 -0.0397 0.0547  1047 TRP A C   
1538 O O   . TRP A 195 ? 0.2865 0.2073 0.5350 -0.0195 -0.0300 0.0707  1047 TRP A O   
1539 C CB  . TRP A 195 ? 0.2551 0.1710 0.4984 -0.0092 -0.0321 -0.0029 1047 TRP A CB  
1540 C CG  . TRP A 195 ? 0.2239 0.1500 0.4384 -0.0022 -0.0269 -0.0264 1047 TRP A CG  
1541 C CD1 . TRP A 195 ? 0.2242 0.1629 0.3952 -0.0015 -0.0175 -0.0230 1047 TRP A CD1 
1542 C CD2 . TRP A 195 ? 0.2583 0.1854 0.4879 0.0050  -0.0307 -0.0563 1047 TRP A CD2 
1543 N NE1 . TRP A 195 ? 0.2301 0.1781 0.3889 0.0037  -0.0152 -0.0445 1047 TRP A NE1 
1544 C CE2 . TRP A 195 ? 0.2850 0.2291 0.4773 0.0084  -0.0221 -0.0658 1047 TRP A CE2 
1545 C CE3 . TRP A 195 ? 0.2905 0.2070 0.5636 0.0092  -0.0408 -0.0770 1047 TRP A CE3 
1546 C CZ2 . TRP A 195 ? 0.3200 0.2766 0.5143 0.0154  -0.0214 -0.0932 1047 TRP A CZ2 
1547 C CZ3 . TRP A 195 ? 0.2894 0.2169 0.5638 0.0184  -0.0402 -0.1090 1047 TRP A CZ3 
1548 C CH2 . TRP A 195 ? 0.2632 0.2134 0.4969 0.0212  -0.0296 -0.1156 1047 TRP A CH2 
1549 N N   . TYR A 196 ? 0.2841 0.1746 0.6195 -0.0217 -0.0510 0.0680  1048 TYR A N   
1550 C CA  . TYR A 196 ? 0.3054 0.2008 0.6572 -0.0326 -0.0514 0.1032  1048 TYR A CA  
1551 C C   . TYR A 196 ? 0.3456 0.2450 0.7059 -0.0343 -0.0541 0.1417  1048 TYR A C   
1552 O O   . TYR A 196 ? 0.3527 0.2383 0.7395 -0.0292 -0.0640 0.1446  1048 TYR A O   
1553 C CB  . TYR A 196 ? 0.3070 0.1860 0.7130 -0.0403 -0.0631 0.0981  1048 TYR A CB  
1554 C CG  . TYR A 196 ? 0.3175 0.2055 0.7119 -0.0452 -0.0588 0.0797  1048 TYR A CG  
1555 C CD1 . TYR A 196 ? 0.2798 0.1852 0.6209 -0.0403 -0.0463 0.0625  1048 TYR A CD1 
1556 C CD2 . TYR A 196 ? 0.3958 0.2746 0.8366 -0.0552 -0.0690 0.0799  1048 TYR A CD2 
1557 C CE1 . TYR A 196 ? 0.3370 0.2520 0.6702 -0.0443 -0.0439 0.0486  1048 TYR A CE1 
1558 C CE2 . TYR A 196 ? 0.3516 0.2412 0.7837 -0.0598 -0.0667 0.0634  1048 TYR A CE2 
1559 C CZ  . TYR A 196 ? 0.3666 0.2753 0.7437 -0.0537 -0.0539 0.0486  1048 TYR A CZ  
1560 O OH  . TYR A 196 ? 0.4385 0.3598 0.8071 -0.0574 -0.0526 0.0347  1048 TYR A OH  
1561 N N   . ALA A 197 ? 0.3280 0.2499 0.6659 -0.0410 -0.0452 0.1715  1049 ALA A N   
1562 C CA  . ALA A 197 ? 0.3021 0.2367 0.6450 -0.0449 -0.0469 0.2131  1049 ALA A CA  
1563 C C   . ALA A 197 ? 0.3487 0.2673 0.7576 -0.0536 -0.0616 0.2403  1049 ALA A C   
1564 O O   . ALA A 197 ? 0.3791 0.2805 0.8280 -0.0592 -0.0686 0.2286  1049 ALA A O   
1565 C CB  . ALA A 197 ? 0.2666 0.2339 0.5713 -0.0495 -0.0328 0.2334  1049 ALA A CB  
1566 N N   . PRO A 198 ? 0.3911 0.3150 0.8144 -0.0552 -0.0683 0.2767  1050 PRO A N   
1567 C CA  . PRO A 198 ? 0.4127 0.3200 0.9036 -0.0642 -0.0841 0.3080  1050 PRO A CA  
1568 C C   . PRO A 198 ? 0.4326 0.3493 0.9506 -0.0798 -0.0824 0.3315  1050 PRO A C   
1569 O O   . PRO A 198 ? 0.4605 0.3507 1.0385 -0.0864 -0.0962 0.3302  1050 PRO A O   
1570 C CB  . PRO A 198 ? 0.4297 0.3536 0.9154 -0.0638 -0.0880 0.3496  1050 PRO A CB  
1571 C CG  . PRO A 198 ? 0.4336 0.3681 0.8628 -0.0509 -0.0801 0.3250  1050 PRO A CG  
1572 C CD  . PRO A 198 ? 0.3931 0.3376 0.7750 -0.0490 -0.0641 0.2912  1050 PRO A CD  
1573 N N   . GLU A 199 ? 0.4418 0.3966 0.9187 -0.0852 -0.0664 0.3507  1051 GLU A N   
1574 C CA  . GLU A 199 ? 0.4515 0.4231 0.9524 -0.1000 -0.0623 0.3731  1051 GLU A CA  
1575 C C   . GLU A 199 ? 0.4183 0.3688 0.9415 -0.1023 -0.0653 0.3356  1051 GLU A C   
1576 O O   . GLU A 199 ? 0.4493 0.3975 1.0208 -0.1160 -0.0718 0.3519  1051 GLU A O   
1577 C CB  . GLU A 199 ? 0.4313 0.4533 0.8798 -0.1021 -0.0421 0.3943  1051 GLU A CB  
1578 C CG  . GLU A 199 ? 0.3718 0.4062 0.7584 -0.0908 -0.0259 0.3541  1051 GLU A CG  
1579 C CD  . GLU A 199 ? 0.3815 0.4115 0.7189 -0.0762 -0.0234 0.3315  1051 GLU A CD  
1580 O OE1 . GLU A 199 ? 0.3827 0.4031 0.7313 -0.0740 -0.0336 0.3464  1051 GLU A OE1 
1581 O OE2 . GLU A 199 ? 0.3251 0.3619 0.6159 -0.0674 -0.0122 0.3004  1051 GLU A OE2 
1582 N N   . CYS A 200 ? 0.4184 0.3563 0.9075 -0.0897 -0.0615 0.2875  1052 CYS A N   
1583 C CA  . CYS A 200 ? 0.3966 0.3160 0.9029 -0.0902 -0.0663 0.2485  1052 CYS A CA  
1584 C C   . CYS A 200 ? 0.4558 0.3357 1.0264 -0.0917 -0.0874 0.2350  1052 CYS A C   
1585 O O   . CYS A 200 ? 0.4862 0.3538 1.1024 -0.1016 -0.0974 0.2290  1052 CYS A O   
1586 C CB  . CYS A 200 ? 0.3558 0.2774 0.8061 -0.0766 -0.0563 0.2053  1052 CYS A CB  
1587 S SG  . CYS A 200 ? 0.3644 0.3248 0.7421 -0.0712 -0.0345 0.2171  1052 CYS A SG  
1588 N N   . LEU A 201 ? 0.4473 0.3082 1.0246 -0.0815 -0.0950 0.2293  1053 LEU A N   
1589 C CA  . LEU A 201 ? 0.4437 0.2666 1.0855 -0.0799 -0.1156 0.2155  1053 LEU A CA  
1590 C C   . LEU A 201 ? 0.4686 0.2804 1.1784 -0.0951 -0.1300 0.2606  1053 LEU A C   
1591 O O   . LEU A 201 ? 0.4816 0.2647 1.2527 -0.1008 -0.1469 0.2476  1053 LEU A O   
1592 C CB  . LEU A 201 ? 0.4394 0.2495 1.0729 -0.0637 -0.1192 0.2004  1053 LEU A CB  
1593 C CG  . LEU A 201 ? 0.3804 0.1990 0.9569 -0.0493 -0.1074 0.1553  1053 LEU A CG  
1594 C CD1 . LEU A 201 ? 0.3425 0.1574 0.9104 -0.0358 -0.1092 0.1521  1053 LEU A CD1 
1595 C CD2 . LEU A 201 ? 0.3647 0.1683 0.9557 -0.0454 -0.1127 0.1052  1053 LEU A CD2 
1596 N N   . MET A 202 ? 0.4614 0.2982 1.1607 -0.1024 -0.1239 0.3129  1054 MET A N   
1597 C CA  . MET A 202 ? 0.5375 0.3686 1.3007 -0.1177 -0.1375 0.3648  1054 MET A CA  
1598 C C   . MET A 202 ? 0.5291 0.3708 1.3218 -0.1362 -0.1371 0.3796  1054 MET A C   
1599 O O   . MET A 202 ? 0.5637 0.3764 1.4286 -0.1468 -0.1559 0.3831  1054 MET A O   
1600 C CB  . MET A 202 ? 0.5623 0.4267 1.2990 -0.1204 -0.1297 0.4191  1054 MET A CB  
1601 C CG  . MET A 202 ? 0.5970 0.4585 1.3038 -0.1042 -0.1304 0.4133  1054 MET A CG  
1602 S SD  . MET A 202 ? 0.8484 0.6784 1.6270 -0.1027 -0.1555 0.4444  1054 MET A SD  
1603 C CE  . MET A 202 ? 0.8557 0.7242 1.6459 -0.1219 -0.1547 0.5274  1054 MET A CE  
1604 N N   . GLN A 203 ? 0.5066 0.3902 1.2456 -0.1395 -0.1164 0.3870  1055 GLN A N   
1605 C CA  . GLN A 203 ? 0.5499 0.4578 1.3121 -0.1578 -0.1123 0.4137  1055 GLN A CA  
1606 C C   . GLN A 203 ? 0.5432 0.4618 1.2782 -0.1565 -0.1025 0.3740  1055 GLN A C   
1607 O O   . GLN A 203 ? 0.5702 0.5139 1.3217 -0.1706 -0.0977 0.3938  1055 GLN A O   
1608 C CB  . GLN A 203 ? 0.5612 0.5194 1.2942 -0.1648 -0.0963 0.4688  1055 GLN A CB  
1609 C CG  . GLN A 203 ? 0.5528 0.5075 1.3157 -0.1690 -0.1072 0.5174  1055 GLN A CG  
1610 C CD  . GLN A 203 ? 0.6692 0.6812 1.4049 -0.1779 -0.0918 0.5740  1055 GLN A CD  
1611 O OE1 . GLN A 203 ? 0.6113 0.6656 1.2882 -0.1739 -0.0703 0.5690  1055 GLN A OE1 
1612 N NE2 . GLN A 203 ? 0.6627 0.6769 1.4451 -0.1897 -0.1042 0.6300  1055 GLN A NE2 
1613 N N   . SER A 204 ? 0.5331 0.4356 1.2302 -0.1405 -0.1004 0.3206  1056 SER A N   
1614 C CA  . SER A 204 ? 0.5291 0.4421 1.1987 -0.1382 -0.0927 0.2832  1056 SER A CA  
1615 C C   . SER A 204 ? 0.5078 0.4691 1.1256 -0.1387 -0.0698 0.3025  1056 SER A C   
1616 O O   . SER A 204 ? 0.5074 0.4863 1.1238 -0.1437 -0.0648 0.2929  1056 SER A O   
1617 C CB  . SER A 204 ? 0.5603 0.4553 1.2951 -0.1524 -0.1098 0.2730  1056 SER A CB  
1618 O OG  . SER A 204 ? 0.6010 0.4548 1.4013 -0.1563 -0.1325 0.2725  1056 SER A OG  
1619 N N   . LYS A 205 ? 0.4900 0.4738 1.0673 -0.1328 -0.0571 0.3280  1057 LYS A N   
1620 C CA  . LYS A 205 ? 0.4553 0.4865 0.9827 -0.1307 -0.0353 0.3446  1057 LYS A CA  
1621 C C   . LYS A 205 ? 0.4236 0.4551 0.8831 -0.1122 -0.0242 0.3086  1057 LYS A C   
1622 O O   . LYS A 205 ? 0.4339 0.4411 0.8802 -0.1028 -0.0303 0.2928  1057 LYS A O   
1623 C CB  . LYS A 205 ? 0.4565 0.5182 0.9843 -0.1373 -0.0292 0.3977  1057 LYS A CB  
1624 C CG  . LYS A 205 ? 0.5535 0.6253 1.1474 -0.1581 -0.0374 0.4437  1057 LYS A CG  
1625 C CD  . LYS A 205 ? 0.5828 0.6938 1.1690 -0.1642 -0.0294 0.4992  1057 LYS A CD  
1626 C CE  . LYS A 205 ? 0.6282 0.7503 1.2845 -0.1868 -0.0384 0.5510  1057 LYS A CE  
1627 N NZ  . LYS A 205 ? 0.6694 0.8405 1.3130 -0.1934 -0.0284 0.6084  1057 LYS A NZ  
1628 N N   A PHE A 206 ? 0.3818 0.4409 0.8028 -0.1072 -0.0089 0.2965  1058 PHE A N   
1629 N N   B PHE A 206 ? 0.3798 0.4395 0.8005 -0.1073 -0.0087 0.2970  1058 PHE A N   
1630 C CA  A PHE A 206 ? 0.3338 0.3915 0.6952 -0.0909 0.0003  0.2628  1058 PHE A CA  
1631 C CA  B PHE A 206 ? 0.3281 0.3872 0.6893 -0.0910 0.0009  0.2622  1058 PHE A CA  
1632 C C   A PHE A 206 ? 0.3195 0.4189 0.6350 -0.0848 0.0198  0.2738  1058 PHE A C   
1633 C C   B PHE A 206 ? 0.3184 0.4190 0.6340 -0.0849 0.0202  0.2748  1058 PHE A C   
1634 O O   A PHE A 206 ? 0.3321 0.4581 0.6510 -0.0875 0.0287  0.2779  1058 PHE A O   
1635 O O   B PHE A 206 ? 0.3276 0.4562 0.6460 -0.0877 0.0295  0.2802  1058 PHE A O   
1636 C CB  A PHE A 206 ? 0.3030 0.3406 0.6651 -0.0871 -0.0052 0.2216  1058 PHE A CB  
1637 C CB  B PHE A 206 ? 0.3020 0.3476 0.6653 -0.0886 -0.0029 0.2250  1058 PHE A CB  
1638 C CG  A PHE A 206 ? 0.2948 0.3113 0.6192 -0.0737 -0.0061 0.1880  1058 PHE A CG  
1639 C CG  B PHE A 206 ? 0.2932 0.2996 0.6811 -0.0880 -0.0195 0.1975  1058 PHE A CG  
1640 C CD1 A PHE A 206 ? 0.2503 0.2816 0.5203 -0.0626 0.0070  0.1782  1058 PHE A CD1 
1641 C CD1 B PHE A 206 ? 0.3179 0.3058 0.6733 -0.0757 -0.0203 0.1705  1058 PHE A CD1 
1642 C CD2 A PHE A 206 ? 0.3009 0.2846 0.6469 -0.0722 -0.0202 0.1670  1058 PHE A CD2 
1643 C CD2 B PHE A 206 ? 0.3193 0.3094 0.7649 -0.0996 -0.0347 0.1970  1058 PHE A CD2 
1644 C CE1 A PHE A 206 ? 0.1642 0.1779 0.4025 -0.0521 0.0059  0.1506  1058 PHE A CE1 
1645 C CE1 B PHE A 206 ? 0.2726 0.2302 0.6506 -0.0735 -0.0342 0.1429  1058 PHE A CE1 
1646 C CE2 A PHE A 206 ? 0.2177 0.1881 0.5298 -0.0604 -0.0196 0.1385  1058 PHE A CE2 
1647 C CE2 B PHE A 206 ? 0.3508 0.3068 0.8192 -0.0971 -0.0501 0.1664  1058 PHE A CE2 
1648 C CZ  A PHE A 206 ? 0.2246 0.2102 0.4831 -0.0515 -0.0066 0.1326  1058 PHE A CZ  
1649 C CZ  B PHE A 206 ? 0.2712 0.2131 0.7047 -0.0833 -0.0489 0.1391  1058 PHE A CZ  
1650 N N   . TYR A 207 ? 0.3175 0.4237 0.5932 -0.0762 0.0254  0.2778  1059 TYR A N   
1651 C CA  . TYR A 207 ? 0.3336 0.4774 0.5612 -0.0677 0.0426  0.2823  1059 TYR A CA  
1652 C C   . TYR A 207 ? 0.3162 0.4451 0.4985 -0.0531 0.0461  0.2425  1059 TYR A C   
1653 O O   . TYR A 207 ? 0.2965 0.3900 0.4813 -0.0503 0.0359  0.2178  1059 TYR A O   
1654 C CB  . TYR A 207 ? 0.3407 0.5027 0.5523 -0.0681 0.0439  0.3112  1059 TYR A CB  
1655 C CG  . TYR A 207 ? 0.3126 0.4923 0.5662 -0.0829 0.0399  0.3580  1059 TYR A CG  
1656 C CD1 . TYR A 207 ? 0.3105 0.4561 0.6163 -0.0928 0.0220  0.3702  1059 TYR A CD1 
1657 C CD2 . TYR A 207 ? 0.3274 0.5600 0.5700 -0.0868 0.0535  0.3915  1059 TYR A CD2 
1658 C CE1 . TYR A 207 ? 0.3213 0.4808 0.6717 -0.1077 0.0163  0.4174  1059 TYR A CE1 
1659 C CE2 . TYR A 207 ? 0.3977 0.6502 0.6804 -0.1022 0.0497  0.4403  1059 TYR A CE2 
1660 C CZ  . TYR A 207 ? 0.3805 0.5941 0.7189 -0.1132 0.0302  0.4545  1059 TYR A CZ  
1661 O OH  . TYR A 207 ? 0.4123 0.6426 0.7960 -0.1295 0.0244  0.5060  1059 TYR A OH  
1662 N N   . ILE A 208 ? 0.3312 0.4883 0.4734 -0.0436 0.0602  0.2367  1060 ILE A N   
1663 C CA  . ILE A 208 ? 0.3044 0.4476 0.4028 -0.0302 0.0623  0.2040  1060 ILE A CA  
1664 C C   . ILE A 208 ? 0.3184 0.4412 0.4024 -0.0285 0.0535  0.2023  1060 ILE A C   
1665 O O   . ILE A 208 ? 0.2715 0.3668 0.3424 -0.0232 0.0476  0.1766  1060 ILE A O   
1666 C CB  . ILE A 208 ? 0.3212 0.4990 0.3822 -0.0193 0.0778  0.1983  1060 ILE A CB  
1667 C CG1 . ILE A 208 ? 0.3780 0.5677 0.4512 -0.0166 0.0849  0.1883  1060 ILE A CG1 
1668 C CG2 . ILE A 208 ? 0.3398 0.5023 0.3583 -0.0074 0.0771  0.1705  1060 ILE A CG2 
1669 C CD1 . ILE A 208 ? 0.3852 0.6160 0.4343 -0.0059 0.1011  0.1868  1060 ILE A CD1 
1670 N N   . ALA A 209 ? 0.3047 0.4447 0.3928 -0.0336 0.0523  0.2320  1061 ALA A N   
1671 C CA  . ALA A 209 ? 0.3138 0.4365 0.3964 -0.0329 0.0418  0.2350  1061 ALA A CA  
1672 C C   . ALA A 209 ? 0.2928 0.3750 0.4110 -0.0364 0.0275  0.2246  1061 ALA A C   
1673 O O   . ALA A 209 ? 0.2961 0.3598 0.4060 -0.0320 0.0200  0.2132  1061 ALA A O   
1674 C CB  . ALA A 209 ? 0.3440 0.4956 0.4304 -0.0387 0.0416  0.2741  1061 ALA A CB  
1675 N N   . SER A 210 ? 0.2882 0.3592 0.4476 -0.0439 0.0234  0.2271  1062 SER A N   
1676 C CA  . SER A 210 ? 0.2866 0.3211 0.4789 -0.0454 0.0102  0.2094  1062 SER A CA  
1677 C C   . SER A 210 ? 0.2780 0.2961 0.4434 -0.0365 0.0115  0.1699  1062 SER A C   
1678 O O   . SER A 210 ? 0.2800 0.2755 0.4520 -0.0332 0.0033  0.1523  1062 SER A O   
1679 C CB  . SER A 210 ? 0.3066 0.3349 0.5492 -0.0560 0.0043  0.2182  1062 SER A CB  
1680 O OG  . SER A 210 ? 0.2934 0.3436 0.5595 -0.0658 0.0054  0.2589  1062 SER A OG  
1681 N N   . ASP A 211 ? 0.2747 0.3065 0.4128 -0.0326 0.0218  0.1576  1063 ASP A N   
1682 C CA  . ASP A 211 ? 0.2611 0.2818 0.3692 -0.0245 0.0237  0.1264  1063 ASP A CA  
1683 C C   . ASP A 211 ? 0.2245 0.2424 0.2992 -0.0178 0.0241  0.1204  1063 ASP A C   
1684 O O   . ASP A 211 ? 0.2262 0.2278 0.2913 -0.0141 0.0202  0.0992  1063 ASP A O   
1685 C CB  . ASP A 211 ? 0.2518 0.2885 0.3412 -0.0209 0.0336  0.1186  1063 ASP A CB  
1686 C CG  . ASP A 211 ? 0.2613 0.2943 0.3771 -0.0253 0.0304  0.1100  1063 ASP A CG  
1687 O OD1 . ASP A 211 ? 0.2439 0.2587 0.3860 -0.0299 0.0202  0.1008  1063 ASP A OD1 
1688 O OD2 . ASP A 211 ? 0.2748 0.3256 0.3859 -0.0235 0.0378  0.1108  1063 ASP A OD2 
1689 N N   . VAL A 212 ? 0.2608 0.2983 0.3181 -0.0168 0.0284  0.1392  1064 VAL A N   
1690 C CA  . VAL A 212 ? 0.2519 0.2889 0.2807 -0.0118 0.0261  0.1350  1064 VAL A CA  
1691 C C   . VAL A 212 ? 0.2645 0.2817 0.3156 -0.0134 0.0144  0.1349  1064 VAL A C   
1692 O O   . VAL A 212 ? 0.2440 0.2504 0.2808 -0.0093 0.0111  0.1176  1064 VAL A O   
1693 C CB  . VAL A 212 ? 0.2669 0.3341 0.2727 -0.0108 0.0317  0.1552  1064 VAL A CB  
1694 C CG1 . VAL A 212 ? 0.2643 0.3314 0.2470 -0.0074 0.0257  0.1527  1064 VAL A CG1 
1695 C CG2 . VAL A 212 ? 0.2781 0.3649 0.2575 -0.0052 0.0439  0.1453  1064 VAL A CG2 
1696 N N   . TRP A 213 ? 0.2827 0.2953 0.3728 -0.0192 0.0079  0.1540  1065 TRP A N   
1697 C CA  . TRP A 213 ? 0.2867 0.2791 0.4064 -0.0188 -0.0041 0.1517  1065 TRP A CA  
1698 C C   . TRP A 213 ? 0.2229 0.1960 0.3467 -0.0150 -0.0059 0.1187  1065 TRP A C   
1699 O O   . TRP A 213 ? 0.2147 0.1805 0.3336 -0.0103 -0.0099 0.1053  1065 TRP A O   
1700 C CB  . TRP A 213 ? 0.2616 0.2479 0.4301 -0.0257 -0.0120 0.1752  1065 TRP A CB  
1701 C CG  . TRP A 213 ? 0.2623 0.2256 0.4693 -0.0235 -0.0251 0.1701  1065 TRP A CG  
1702 C CD1 . TRP A 213 ? 0.2867 0.2292 0.5141 -0.0200 -0.0298 0.1404  1065 TRP A CD1 
1703 C CD2 . TRP A 213 ? 0.3428 0.3041 0.5752 -0.0237 -0.0356 0.1953  1065 TRP A CD2 
1704 N NE1 . TRP A 213 ? 0.3064 0.2336 0.5708 -0.0166 -0.0417 0.1420  1065 TRP A NE1 
1705 C CE2 . TRP A 213 ? 0.3334 0.2697 0.6036 -0.0188 -0.0462 0.1766  1065 TRP A CE2 
1706 C CE3 . TRP A 213 ? 0.3274 0.3085 0.5541 -0.0270 -0.0374 0.2320  1065 TRP A CE3 
1707 C CZ2 . TRP A 213 ? 0.2798 0.2065 0.5867 -0.0162 -0.0592 0.1933  1065 TRP A CZ2 
1708 C CZ3 . TRP A 213 ? 0.3419 0.3148 0.6026 -0.0258 -0.0511 0.2521  1065 TRP A CZ3 
1709 C CH2 . TRP A 213 ? 0.3674 0.3114 0.6703 -0.0201 -0.0622 0.2328  1065 TRP A CH2 
1710 N N   A SER A 214 ? 0.2650 0.2341 0.3983 -0.0175 -0.0032 0.1069  1066 SER A N   
1711 N N   B SER A 214 ? 0.2428 0.2117 0.3765 -0.0175 -0.0033 0.1067  1066 SER A N   
1712 C CA  A SER A 214 ? 0.2591 0.2170 0.3919 -0.0146 -0.0041 0.0763  1066 SER A CA  
1713 C CA  B SER A 214 ? 0.2118 0.1694 0.3449 -0.0145 -0.0043 0.0759  1066 SER A CA  
1714 C C   A SER A 214 ? 0.2435 0.2053 0.3363 -0.0094 0.0013  0.0601  1066 SER A C   
1715 C C   B SER A 214 ? 0.2192 0.1809 0.3118 -0.0094 0.0013  0.0600  1066 SER A C   
1716 O O   A SER A 214 ? 0.2287 0.1846 0.3216 -0.0064 -0.0012 0.0409  1066 SER A O   
1717 O O   B SER A 214 ? 0.2010 0.1569 0.2933 -0.0063 -0.0011 0.0407  1066 SER A O   
1718 C CB  A SER A 214 ? 0.2684 0.2282 0.4110 -0.0187 -0.0019 0.0699  1066 SER A CB  
1719 C CB  B SER A 214 ? 0.2098 0.1685 0.3540 -0.0186 -0.0026 0.0686  1066 SER A CB  
1720 O OG  A SER A 214 ? 0.3306 0.2818 0.4813 -0.0170 -0.0060 0.0429  1066 SER A OG  
1721 O OG  B SER A 214 ? 0.1511 0.1037 0.3389 -0.0250 -0.0098 0.0811  1066 SER A OG  
1722 N N   . PHE A 215 ? 0.2261 0.1995 0.2874 -0.0085 0.0085  0.0677  1067 PHE A N   
1723 C CA  . PHE A 215 ? 0.2479 0.2225 0.2753 -0.0046 0.0116  0.0551  1067 PHE A CA  
1724 C C   . PHE A 215 ? 0.2385 0.2103 0.2646 -0.0028 0.0058  0.0547  1067 PHE A C   
1725 O O   . PHE A 215 ? 0.2399 0.2084 0.2550 -0.0014 0.0051  0.0396  1067 PHE A O   
1726 C CB  . PHE A 215 ? 0.2229 0.2097 0.2207 -0.0024 0.0185  0.0612  1067 PHE A CB  
1727 C CG  . PHE A 215 ? 0.2335 0.2174 0.2030 0.0007  0.0184  0.0486  1067 PHE A CG  
1728 C CD1 . PHE A 215 ? 0.2507 0.2262 0.2127 0.0014  0.0192  0.0321  1067 PHE A CD1 
1729 C CD2 . PHE A 215 ? 0.3088 0.2982 0.2633 0.0018  0.0152  0.0539  1067 PHE A CD2 
1730 C CE1 . PHE A 215 ? 0.1939 0.1647 0.1362 0.0024  0.0173  0.0225  1067 PHE A CE1 
1731 C CE2 . PHE A 215 ? 0.3046 0.2896 0.2382 0.0031  0.0128  0.0410  1067 PHE A CE2 
1732 C CZ  . PHE A 215 ? 0.2149 0.1893 0.1443 0.0030  0.0138  0.0260  1067 PHE A CZ  
1733 N N   . GLY A 216 ? 0.2335 0.2093 0.2719 -0.0035 0.0013  0.0733  1068 GLY A N   
1734 C CA  . GLY A 216 ? 0.2271 0.2021 0.2697 -0.0014 -0.0059 0.0745  1068 GLY A CA  
1735 C C   . GLY A 216 ? 0.2486 0.2135 0.3148 0.0009  -0.0098 0.0565  1068 GLY A C   
1736 O O   . GLY A 216 ? 0.2130 0.1802 0.2724 0.0031  -0.0116 0.0462  1068 GLY A O   
1737 N N   . VAL A 217 ? 0.2252 0.1817 0.3209 0.0004  -0.0113 0.0518  1069 VAL A N   
1738 C CA  . VAL A 217 ? 0.1953 0.1456 0.3153 0.0041  -0.0147 0.0308  1069 VAL A CA  
1739 C C   . VAL A 217 ? 0.2286 0.1852 0.3235 0.0043  -0.0082 0.0095  1069 VAL A C   
1740 O O   . VAL A 217 ? 0.2248 0.1873 0.3207 0.0074  -0.0083 -0.0047 1069 VAL A O   
1741 C CB  . VAL A 217 ? 0.2462 0.1852 0.4054 0.0031  -0.0198 0.0284  1069 VAL A CB  
1742 C CG1 . VAL A 217 ? 0.2207 0.1565 0.4033 0.0086  -0.0232 0.0006  1069 VAL A CG1 
1743 C CG2 . VAL A 217 ? 0.2100 0.1426 0.3987 0.0015  -0.0276 0.0548  1069 VAL A CG2 
1744 N N   . THR A 218 ? 0.2293 0.1874 0.3027 0.0009  -0.0025 0.0098  1070 THR A N   
1745 C CA  . THR A 218 ? 0.2003 0.1645 0.2491 0.0001  0.0027  -0.0040 1070 THR A CA  
1746 C C   . THR A 218 ? 0.1884 0.1573 0.2148 0.0001  0.0037  -0.0031 1070 THR A C   
1747 O O   . THR A 218 ? 0.1917 0.1676 0.2118 -0.0003 0.0053  -0.0145 1070 THR A O   
1748 C CB  . THR A 218 ? 0.2248 0.1893 0.2571 -0.0024 0.0073  -0.0003 1070 THR A CB  
1749 O OG1 . THR A 218 ? 0.2249 0.1875 0.2797 -0.0040 0.0055  -0.0026 1070 THR A OG1 
1750 C CG2 . THR A 218 ? 0.2215 0.1914 0.2316 -0.0032 0.0107  -0.0110 1070 THR A CG2 
1751 N N   . LEU A 219 ? 0.1789 0.1466 0.1930 -0.0002 0.0026  0.0106  1071 LEU A N   
1752 C CA  . LEU A 219 ? 0.1966 0.1680 0.1938 -0.0010 0.0007  0.0109  1071 LEU A CA  
1753 C C   . LEU A 219 ? 0.1823 0.1600 0.1987 0.0006  -0.0034 0.0053  1071 LEU A C   
1754 O O   . LEU A 219 ? 0.1774 0.1618 0.1860 -0.0014 -0.0031 -0.0011 1071 LEU A O   
1755 C CB  . LEU A 219 ? 0.2183 0.1913 0.2023 -0.0007 -0.0019 0.0252  1071 LEU A CB  
1756 C CG  . LEU A 219 ? 0.3061 0.2833 0.2720 -0.0021 -0.0064 0.0242  1071 LEU A CG  
1757 C CD1 . LEU A 219 ? 0.3235 0.2958 0.2694 -0.0048 -0.0040 0.0129  1071 LEU A CD1 
1758 C CD2 . LEU A 219 ? 0.2436 0.2274 0.1961 -0.0011 -0.0092 0.0368  1071 LEU A CD2 
1759 N N   . HIS A 220 ? 0.1898 0.1661 0.2346 0.0044  -0.0075 0.0090  1072 HIS A N   
1760 C CA  . HIS A 220 ? 0.1956 0.1789 0.2652 0.0086  -0.0112 0.0011  1072 HIS A CA  
1761 C C   . HIS A 220 ? 0.2097 0.2029 0.2807 0.0092  -0.0057 -0.0192 1072 HIS A C   
1762 O O   . HIS A 220 ? 0.2023 0.2097 0.2735 0.0093  -0.0046 -0.0256 1072 HIS A O   
1763 C CB  . HIS A 220 ? 0.2338 0.2099 0.3402 0.0137  -0.0177 0.0068  1072 HIS A CB  
1764 C CG  . HIS A 220 ? 0.1953 0.1791 0.3299 0.0202  -0.0230 0.0017  1072 HIS A CG  
1765 N ND1 . HIS A 220 ? 0.2001 0.1934 0.3518 0.0254  -0.0201 -0.0209 1072 HIS A ND1 
1766 C CD2 . HIS A 220 ? 0.2143 0.2006 0.3652 0.0232  -0.0313 0.0160  1072 HIS A CD2 
1767 C CE1 . HIS A 220 ? 0.2068 0.2078 0.3856 0.0322  -0.0255 -0.0215 1072 HIS A CE1 
1768 N NE2 . HIS A 220 ? 0.1882 0.1838 0.3683 0.0308  -0.0332 0.0017  1072 HIS A NE2 
1769 N N   . GLU A 221 ? 0.1929 0.1823 0.2644 0.0089  -0.0023 -0.0282 1073 GLU A N   
1770 C CA  . GLU A 221 ? 0.1951 0.1988 0.2630 0.0089  0.0029  -0.0465 1073 GLU A CA  
1771 C C   . GLU A 221 ? 0.2110 0.2258 0.2512 0.0030  0.0074  -0.0436 1073 GLU A C   
1772 O O   . GLU A 221 ? 0.2082 0.2426 0.2495 0.0028  0.0106  -0.0520 1073 GLU A O   
1773 C CB  . GLU A 221 ? 0.1955 0.1937 0.2621 0.0077  0.0041  -0.0531 1073 GLU A CB  
1774 C CG  . GLU A 221 ? 0.2166 0.2051 0.3160 0.0121  -0.0013 -0.0605 1073 GLU A CG  
1775 C CD  . GLU A 221 ? 0.2341 0.2221 0.3324 0.0097  -0.0011 -0.0705 1073 GLU A CD  
1776 O OE1 . GLU A 221 ? 0.2246 0.2265 0.3283 0.0124  -0.0006 -0.0926 1073 GLU A OE1 
1777 O OE2 . GLU A 221 ? 0.2392 0.2167 0.3311 0.0052  -0.0014 -0.0569 1073 GLU A OE2 
1778 N N   . LEU A 222 ? 0.2218 0.2249 0.2396 -0.0017 0.0074  -0.0314 1074 LEU A N   
1779 C CA  . LEU A 222 ? 0.2176 0.2247 0.2137 -0.0078 0.0091  -0.0269 1074 LEU A CA  
1780 C C   . LEU A 222 ? 0.2171 0.2347 0.2182 -0.0099 0.0067  -0.0247 1074 LEU A C   
1781 O O   . LEU A 222 ? 0.2272 0.2605 0.2254 -0.0147 0.0091  -0.0261 1074 LEU A O   
1782 C CB  . LEU A 222 ? 0.2729 0.2627 0.2501 -0.0096 0.0078  -0.0169 1074 LEU A CB  
1783 C CG  . LEU A 222 ? 0.3238 0.3091 0.2828 -0.0148 0.0064  -0.0123 1074 LEU A CG  
1784 C CD1 . LEU A 222 ? 0.3130 0.3078 0.2679 -0.0194 0.0092  -0.0140 1074 LEU A CD1 
1785 C CD2 . LEU A 222 ? 0.4080 0.3780 0.3525 -0.0128 0.0058  -0.0078 1074 LEU A CD2 
1786 N N   . LEU A 223 ? 0.2272 0.2395 0.2381 -0.0068 0.0014  -0.0193 1075 LEU A N   
1787 C CA  . LEU A 223 ? 0.2186 0.2418 0.2368 -0.0086 -0.0027 -0.0164 1075 LEU A CA  
1788 C C   . LEU A 223 ? 0.2174 0.2636 0.2594 -0.0051 0.0001  -0.0261 1075 LEU A C   
1789 O O   . LEU A 223 ? 0.2492 0.3115 0.2968 -0.0086 -0.0011 -0.0244 1075 LEU A O   
1790 C CB  . LEU A 223 ? 0.2118 0.2267 0.2327 -0.0062 -0.0105 -0.0061 1075 LEU A CB  
1791 C CG  . LEU A 223 ? 0.2956 0.2966 0.2890 -0.0100 -0.0128 0.0008  1075 LEU A CG  
1792 C CD1 . LEU A 223 ? 0.2489 0.2468 0.2423 -0.0066 -0.0187 0.0117  1075 LEU A CD1 
1793 C CD2 . LEU A 223 ? 0.3035 0.3064 0.2835 -0.0176 -0.0165 -0.0001 1075 LEU A CD2 
1794 N N   . THR A 224 ? 0.2096 0.2591 0.2673 0.0020  0.0035  -0.0378 1076 THR A N   
1795 C CA  . THR A 224 ? 0.1849 0.2598 0.2647 0.0077  0.0077  -0.0528 1076 THR A CA  
1796 C C   . THR A 224 ? 0.2112 0.3069 0.2773 0.0040  0.0164  -0.0623 1076 THR A C   
1797 O O   . THR A 224 ? 0.1964 0.3188 0.2767 0.0095  0.0217  -0.0778 1076 THR A O   
1798 C CB  . THR A 224 ? 0.2257 0.2944 0.3367 0.0194  0.0046  -0.0645 1076 THR A CB  
1799 O OG1 . THR A 224 ? 0.2803 0.3366 0.3868 0.0201  0.0060  -0.0724 1076 THR A OG1 
1800 C CG2 . THR A 224 ? 0.2155 0.2656 0.3407 0.0221  -0.0049 -0.0495 1076 THR A CG2 
1801 N N   . TYR A 225 ? 0.1582 0.2443 0.1975 -0.0043 0.0176  -0.0531 1077 TYR A N   
1802 C CA  . TYR A 225 ? 0.1773 0.2827 0.2015 -0.0089 0.0241  -0.0569 1077 TYR A CA  
1803 C C   . TYR A 225 ? 0.1977 0.3141 0.2297 -0.0012 0.0272  -0.0767 1077 TYR A C   
1804 O O   . TYR A 225 ? 0.2249 0.3733 0.2527 -0.0013 0.0335  -0.0870 1077 TYR A O   
1805 C CB  . TYR A 225 ? 0.1889 0.3262 0.2130 -0.0154 0.0288  -0.0521 1077 TYR A CB  
1806 C CG  . TYR A 225 ? 0.2203 0.3469 0.2389 -0.0251 0.0238  -0.0339 1077 TYR A CG  
1807 C CD1 . TYR A 225 ? 0.2499 0.3662 0.2497 -0.0353 0.0221  -0.0198 1077 TYR A CD1 
1808 C CD2 . TYR A 225 ? 0.2182 0.3462 0.2532 -0.0242 0.0194  -0.0314 1077 TYR A CD2 
1809 C CE1 . TYR A 225 ? 0.2239 0.3283 0.2222 -0.0442 0.0157  -0.0066 1077 TYR A CE1 
1810 C CE2 . TYR A 225 ? 0.2492 0.3681 0.2800 -0.0340 0.0128  -0.0174 1077 TYR A CE2 
1811 C CZ  . TYR A 225 ? 0.2377 0.3441 0.2506 -0.0442 0.0109  -0.0063 1077 TYR A CZ  
1812 O OH  . TYR A 225 ? 0.2699 0.3648 0.2820 -0.0539 0.0027  0.0042  1077 TYR A OH  
1813 N N   . CYS A 226 ? 0.2260 0.3177 0.2695 0.0047  0.0222  -0.0818 1078 CYS A N   
1814 C CA  . CYS A 226 ? 0.2755 0.3705 0.3306 0.0112  0.0220  -0.1017 1078 CYS A CA  
1815 C C   . CYS A 226 ? 0.2815 0.4080 0.3555 0.0195  0.0261  -0.1248 1078 CYS A C   
1816 O O   . CYS A 226 ? 0.2876 0.4353 0.3582 0.0222  0.0292  -0.1441 1078 CYS A O   
1817 C CB  . CYS A 226 ? 0.2738 0.3723 0.3056 0.0056  0.0235  -0.1011 1078 CYS A CB  
1818 S SG  . CYS A 226 ? 0.2710 0.3330 0.2902 0.0004  0.0186  -0.0812 1078 CYS A SG  
1819 N N   . ASP A 227 ? 0.2765 0.4092 0.3702 0.0242  0.0260  -0.1240 1079 ASP A N   
1820 C CA  . ASP A 227 ? 0.3181 0.4828 0.4346 0.0345  0.0305  -0.1474 1079 ASP A CA  
1821 C C   . ASP A 227 ? 0.2926 0.4416 0.4376 0.0458  0.0243  -0.1707 1079 ASP A C   
1822 O O   . ASP A 227 ? 0.2841 0.3988 0.4485 0.0478  0.0153  -0.1619 1079 ASP A O   
1823 C CB  . ASP A 227 ? 0.3356 0.5101 0.4713 0.0373  0.0304  -0.1393 1079 ASP A CB  
1824 C CG  . ASP A 227 ? 0.3922 0.6007 0.5583 0.0510  0.0351  -0.1651 1079 ASP A CG  
1825 O OD1 . ASP A 227 ? 0.3378 0.5791 0.4975 0.0547  0.0430  -0.1869 1079 ASP A OD1 
1826 O OD2 . ASP A 227 ? 0.3752 0.5800 0.5715 0.0586  0.0305  -0.1636 1079 ASP A OD2 
1827 N N   . SER A 228 ? 0.3285 0.5041 0.4765 0.0524  0.0284  -0.1997 1080 SER A N   
1828 C CA  . SER A 228 ? 0.3519 0.5122 0.5288 0.0625  0.0208  -0.2265 1080 SER A CA  
1829 C C   . SER A 228 ? 0.3685 0.5125 0.5923 0.0749  0.0139  -0.2334 1080 SER A C   
1830 O O   . SER A 228 ? 0.3486 0.4571 0.6003 0.0779  0.0029  -0.2343 1080 SER A O   
1831 C CB  . SER A 228 ? 0.4026 0.6011 0.5722 0.0682  0.0263  -0.2608 1080 SER A CB  
1832 O OG  . SER A 228 ? 0.4745 0.7206 0.6428 0.0743  0.0373  -0.2725 1080 SER A OG  
1833 N N   . ASP A 229 ? 0.3645 0.5349 0.5997 0.0813  0.0196  -0.2346 1081 ASP A N   
1834 C CA  . ASP A 229 ? 0.3688 0.5279 0.6514 0.0944  0.0125  -0.2398 1081 ASP A CA  
1835 C C   . ASP A 229 ? 0.3592 0.4803 0.6495 0.0883  0.0027  -0.2043 1081 ASP A C   
1836 O O   . ASP A 229 ? 0.4188 0.5234 0.7503 0.0980  -0.0066 -0.2033 1081 ASP A O   
1837 C CB  . ASP A 229 ? 0.3667 0.5713 0.6616 0.1037  0.0219  -0.2520 1081 ASP A CB  
1838 C CG  . ASP A 229 ? 0.4135 0.6615 0.7099 0.1145  0.0314  -0.2927 1081 ASP A CG  
1839 O OD1 . ASP A 229 ? 0.4609 0.6975 0.7708 0.1220  0.0260  -0.3214 1081 ASP A OD1 
1840 O OD2 . ASP A 229 ? 0.4683 0.7657 0.7531 0.1151  0.0441  -0.2963 1081 ASP A OD2 
1841 N N   . SER A 230 ? 0.3358 0.4453 0.5877 0.0731  0.0041  -0.1759 1082 SER A N   
1842 C CA  . SER A 230 ? 0.3430 0.4214 0.5944 0.0665  -0.0045 -0.1435 1082 SER A CA  
1843 C C   . SER A 230 ? 0.3414 0.3880 0.5805 0.0585  -0.0093 -0.1321 1082 SER A C   
1844 O O   . SER A 230 ? 0.3167 0.3452 0.5408 0.0505  -0.0128 -0.1045 1082 SER A O   
1845 C CB  . SER A 230 ? 0.3254 0.4171 0.5445 0.0560  0.0003  -0.1210 1082 SER A CB  
1846 O OG  . SER A 230 ? 0.3886 0.5186 0.6103 0.0592  0.0083  -0.1322 1082 SER A OG  
1847 N N   . SER A 231 ? 0.3034 0.3464 0.5494 0.0608  -0.0098 -0.1539 1083 SER A N   
1848 C CA  . SER A 231 ? 0.3133 0.3319 0.5480 0.0521  -0.0135 -0.1436 1083 SER A CA  
1849 C C   . SER A 231 ? 0.2861 0.2727 0.5529 0.0525  -0.0250 -0.1237 1083 SER A C   
1850 O O   . SER A 231 ? 0.2875 0.2681 0.5939 0.0619  -0.0322 -0.1269 1083 SER A O   
1851 C CB  . SER A 231 ? 0.3595 0.3846 0.5969 0.0540  -0.0133 -0.1730 1083 SER A CB  
1852 O OG  . SER A 231 ? 0.4048 0.4168 0.6900 0.0642  -0.0227 -0.1945 1083 SER A OG  
1853 N N   . PRO A 232 ? 0.2740 0.2430 0.5249 0.0423  -0.0266 -0.1004 1084 PRO A N   
1854 C CA  . PRO A 232 ? 0.2749 0.2183 0.5570 0.0409  -0.0370 -0.0792 1084 PRO A CA  
1855 C C   . PRO A 232 ? 0.3104 0.2381 0.6460 0.0484  -0.0476 -0.0984 1084 PRO A C   
1856 O O   . PRO A 232 ? 0.3263 0.2379 0.7009 0.0525  -0.0577 -0.0845 1084 PRO A O   
1857 C CB  . PRO A 232 ? 0.2735 0.2096 0.5292 0.0293  -0.0341 -0.0612 1084 PRO A CB  
1858 C CG  . PRO A 232 ? 0.2740 0.2288 0.4799 0.0253  -0.0230 -0.0610 1084 PRO A CG  
1859 C CD  . PRO A 232 ? 0.2950 0.2696 0.5004 0.0320  -0.0188 -0.0901 1084 PRO A CD  
1860 N N   . MET A 233 ? 0.3113 0.2441 0.6501 0.0504  -0.0466 -0.1302 1085 MET A N   
1861 C CA  . MET A 233 ? 0.3488 0.2673 0.7402 0.0588  -0.0579 -0.1573 1085 MET A CA  
1862 C C   . MET A 233 ? 0.3407 0.2666 0.7636 0.0744  -0.0602 -0.1745 1085 MET A C   
1863 O O   . MET A 233 ? 0.3509 0.2545 0.8246 0.0808  -0.0726 -0.1692 1085 MET A O   
1864 C CB  . MET A 233 ? 0.3664 0.2972 0.7467 0.0583  -0.0558 -0.1924 1085 MET A CB  
1865 C CG  . MET A 233 ? 0.4779 0.3990 0.9087 0.0688  -0.0671 -0.2310 1085 MET A CG  
1866 S SD  . MET A 233 ? 0.5535 0.4835 0.9733 0.0636  -0.0697 -0.2649 1085 MET A SD  
1867 C CE  . MET A 233 ? 0.5745 0.5497 0.9204 0.0599  -0.0508 -0.2669 1085 MET A CE  
1868 N N   . ALA A 234 ? 0.3480 0.3069 0.7425 0.0800  -0.0485 -0.1922 1086 ALA A N   
1869 C CA  . ALA A 234 ? 0.3300 0.3056 0.7512 0.0954  -0.0479 -0.2103 1086 ALA A CA  
1870 C C   . ALA A 234 ? 0.3165 0.2775 0.7639 0.0982  -0.0555 -0.1793 1086 ALA A C   
1871 O O   . ALA A 234 ? 0.3541 0.3063 0.8528 0.1115  -0.0649 -0.1896 1086 ALA A O   
1872 C CB  . ALA A 234 ? 0.3396 0.3585 0.7197 0.0966  -0.0321 -0.2235 1086 ALA A CB  
1873 N N   . LEU A 235 ? 0.2946 0.2537 0.7079 0.0864  -0.0527 -0.1422 1087 LEU A N   
1874 C CA  . LEU A 235 ? 0.3146 0.2662 0.7447 0.0876  -0.0601 -0.1106 1087 LEU A CA  
1875 C C   . LEU A 235 ? 0.3533 0.2707 0.8289 0.0873  -0.0758 -0.0898 1087 LEU A C   
1876 O O   . LEU A 235 ? 0.3405 0.2502 0.8599 0.0967  -0.0865 -0.0810 1087 LEU A O   
1877 C CB  . LEU A 235 ? 0.3345 0.2972 0.7125 0.0753  -0.0531 -0.0810 1087 LEU A CB  
1878 C CG  . LEU A 235 ? 0.3116 0.3076 0.6533 0.0747  -0.0405 -0.0930 1087 LEU A CG  
1879 C CD1 . LEU A 235 ? 0.3403 0.3401 0.6369 0.0621  -0.0371 -0.0644 1087 LEU A CD1 
1880 C CD2 . LEU A 235 ? 0.3388 0.3560 0.7124 0.0882  -0.0414 -0.1071 1087 LEU A CD2 
1881 N N   . PHE A 236 ? 0.3249 0.2233 0.7945 0.0763  -0.0780 -0.0803 1088 PHE A N   
1882 C CA  . PHE A 236 ? 0.3726 0.2396 0.8910 0.0740  -0.0934 -0.0588 1088 PHE A CA  
1883 C C   . PHE A 236 ? 0.3965 0.2453 0.9819 0.0880  -0.1060 -0.0880 1088 PHE A C   
1884 O O   . PHE A 236 ? 0.4735 0.3010 1.1103 0.0920  -0.1207 -0.0684 1088 PHE A O   
1885 C CB  . PHE A 236 ? 0.3597 0.2144 0.8615 0.0585  -0.0924 -0.0434 1088 PHE A CB  
1886 C CG  . PHE A 236 ? 0.3382 0.1999 0.8013 0.0461  -0.0877 -0.0004 1088 PHE A CG  
1887 C CD1 . PHE A 236 ? 0.3461 0.2031 0.8278 0.0453  -0.0966 0.0375  1088 PHE A CD1 
1888 C CD2 . PHE A 236 ? 0.3452 0.2200 0.7545 0.0361  -0.0751 0.0018  1088 PHE A CD2 
1889 C CE1 . PHE A 236 ? 0.3369 0.2059 0.7803 0.0348  -0.0920 0.0741  1088 PHE A CE1 
1890 C CE2 . PHE A 236 ? 0.2770 0.1604 0.6517 0.0267  -0.0705 0.0367  1088 PHE A CE2 
1891 C CZ  . PHE A 236 ? 0.2421 0.1241 0.6321 0.0260  -0.0785 0.0717  1088 PHE A CZ  
1892 N N   . LEU A 237 ? 0.4176 0.2763 1.0028 0.0956  -0.1009 -0.1346 1089 LEU A N   
1893 C CA  . LEU A 237 ? 0.4238 0.2684 1.0707 0.1110  -0.1122 -0.1718 1089 LEU A CA  
1894 C C   . LEU A 237 ? 0.4333 0.2879 1.1139 0.1292  -0.1152 -0.1795 1089 LEU A C   
1895 O O   . LEU A 237 ? 0.4107 0.2434 1.1573 0.1421  -0.1300 -0.1926 1089 LEU A O   
1896 C CB  . LEU A 237 ? 0.4493 0.3095 1.0801 0.1146  -0.1052 -0.2221 1089 LEU A CB  
1897 C CG  . LEU A 237 ? 0.4405 0.2841 1.0632 0.1000  -0.1091 -0.2232 1089 LEU A CG  
1898 C CD1 . LEU A 237 ? 0.4325 0.3018 1.0271 0.1032  -0.1008 -0.2706 1089 LEU A CD1 
1899 C CD2 . LEU A 237 ? 0.5295 0.3307 1.2218 0.0988  -0.1300 -0.2188 1089 LEU A CD2 
1900 N N   . LYS A 238 ? 0.3956 0.2829 1.0347 0.1301  -0.1023 -0.1711 1090 LYS A N   
1901 C CA  . LYS A 238 ? 0.4360 0.3358 1.1036 0.1442  -0.1055 -0.1663 1090 LYS A CA  
1902 C C   . LYS A 238 ? 0.4406 0.3120 1.1449 0.1410  -0.1224 -0.1201 1090 LYS A C   
1903 O O   . LYS A 238 ? 0.4906 0.3489 1.2569 0.1556  -0.1360 -0.1220 1090 LYS A O   
1904 C CB  . LYS A 238 ? 0.4302 0.3707 1.0431 0.1410  -0.0893 -0.1607 1090 LYS A CB  
1905 C CG  . LYS A 238 ? 0.4965 0.4628 1.1386 0.1582  -0.0887 -0.1729 1090 LYS A CG  
1906 C CD  . LYS A 238 ? 0.4656 0.4735 1.0577 0.1530  -0.0732 -0.1687 1090 LYS A CD  
1907 C CE  . LYS A 238 ? 0.4547 0.4586 1.0190 0.1393  -0.0771 -0.1212 1090 LYS A CE  
1908 N NZ  . LYS A 238 ? 0.4321 0.4738 0.9549 0.1338  -0.0648 -0.1179 1090 LYS A NZ  
1909 N N   . MET A 239 ? 0.4341 0.2978 1.1018 0.1226  -0.1217 -0.0788 1091 MET A N   
1910 C CA  . MET A 239 ? 0.4458 0.2906 1.1385 0.1168  -0.1362 -0.0289 1091 MET A CA  
1911 C C   . MET A 239 ? 0.4813 0.2868 1.2464 0.1200  -0.1554 -0.0239 1091 MET A C   
1912 O O   . MET A 239 ? 0.4764 0.2686 1.2939 0.1277  -0.1711 -0.0012 1091 MET A O   
1913 C CB  . MET A 239 ? 0.4544 0.3052 1.0883 0.0967  -0.1292 0.0094  1091 MET A CB  
1914 C CG  . MET A 239 ? 0.4829 0.3670 1.0567 0.0931  -0.1168 0.0175  1091 MET A CG  
1915 S SD  . MET A 239 ? 0.5708 0.4642 1.0710 0.0724  -0.1056 0.0464  1091 MET A SD  
1916 C CE  . MET A 239 ? 0.5726 0.4483 1.1017 0.0641  -0.1209 0.0993  1091 MET A CE  
1917 N N   . ILE A 240 ? 0.4571 0.2448 1.2281 0.1140  -0.1553 -0.0452 1092 ILE A N   
1918 C CA  . ILE A 240 ? 0.5053 0.2530 1.3438 0.1121  -0.1744 -0.0377 1092 ILE A CA  
1919 C C   . ILE A 240 ? 0.5404 0.2687 1.4439 0.1304  -0.1852 -0.0881 1092 ILE A C   
1920 O O   . ILE A 240 ? 0.5845 0.2761 1.5573 0.1316  -0.2049 -0.0812 1092 ILE A O   
1921 C CB  . ILE A 240 ? 0.4773 0.2141 1.2922 0.0915  -0.1717 -0.0241 1092 ILE A CB  
1922 C CG1 . ILE A 240 ? 0.5002 0.2480 1.2828 0.0916  -0.1598 -0.0745 1092 ILE A CG1 
1923 C CG2 . ILE A 240 ? 0.4577 0.2132 1.2163 0.0755  -0.1623 0.0245  1092 ILE A CG2 
1924 C CD1 . ILE A 240 ? 0.4761 0.2265 1.2165 0.0718  -0.1520 -0.0609 1092 ILE A CD1 
1925 N N   . GLY A 241 ? 0.5411 0.2956 1.4230 0.1441  -0.1726 -0.1385 1093 GLY A N   
1926 C CA  . GLY A 241 ? 0.5840 0.3292 1.5156 0.1622  -0.1792 -0.1960 1093 GLY A CA  
1927 C C   . GLY A 241 ? 0.5860 0.3406 1.4791 0.1546  -0.1694 -0.2339 1093 GLY A C   
1928 O O   . GLY A 241 ? 0.6005 0.3425 1.4713 0.1349  -0.1700 -0.2109 1093 GLY A O   
1929 N N   . PRO A 242 ? 0.5886 0.3713 1.4701 0.1697  -0.1594 -0.2900 1094 PRO A N   
1930 C CA  . PRO A 242 ? 0.6161 0.4130 1.4584 0.1626  -0.1510 -0.3256 1094 PRO A CA  
1931 C C   . PRO A 242 ? 0.6681 0.4278 1.5621 0.1601  -0.1697 -0.3500 1094 PRO A C   
1932 O O   . PRO A 242 ? 0.6977 0.4472 1.5691 0.1412  -0.1709 -0.3362 1094 PRO A O   
1933 C CB  . PRO A 242 ? 0.6238 0.4661 1.4459 0.1812  -0.1364 -0.3766 1094 PRO A CB  
1934 C CG  . PRO A 242 ? 0.6259 0.4655 1.5043 0.2023  -0.1433 -0.3823 1094 PRO A CG  
1935 C CD  . PRO A 242 ? 0.6017 0.4117 1.5011 0.1932  -0.1540 -0.3205 1094 PRO A CD  
1936 N N   . THR A 243 ? 0.6855 0.4247 1.6520 0.1793  -0.1851 -0.3848 1095 THR A N   
1937 C CA  . THR A 243 ? 0.7335 0.4439 1.7516 0.1823  -0.2027 -0.4278 1095 THR A CA  
1938 C C   . THR A 243 ? 0.7582 0.4107 1.8459 0.1704  -0.2277 -0.3915 1095 THR A C   
1939 O O   . THR A 243 ? 0.8172 0.4350 1.9870 0.1842  -0.2481 -0.4081 1095 THR A O   
1940 C CB  . THR A 243 ? 0.7846 0.5064 1.8467 0.2119  -0.2061 -0.4938 1095 THR A CB  
1941 O OG1 . THR A 243 ? 0.7258 0.4336 1.8419 0.2281  -0.2137 -0.4758 1095 THR A OG1 
1942 C CG2 . THR A 243 ? 0.7548 0.5400 1.7471 0.2207  -0.1812 -0.5322 1095 THR A CG2 
1943 N N   . HIS A 244 ? 0.7175 0.3613 1.7749 0.1450  -0.2262 -0.3414 1096 HIS A N   
1944 C CA  . HIS A 244 ? 0.7318 0.3278 1.8498 0.1293  -0.2479 -0.2999 1096 HIS A CA  
1945 C C   . HIS A 244 ? 0.7346 0.3175 1.8509 0.1089  -0.2547 -0.3055 1096 HIS A C   
1946 O O   . HIS A 244 ? 0.7279 0.2721 1.9020 0.0952  -0.2739 -0.2755 1096 HIS A O   
1947 C CB  . HIS A 244 ? 0.7021 0.2991 1.8018 0.1171  -0.2433 -0.2253 1096 HIS A CB  
1948 C CG  . HIS A 244 ? 0.7040 0.3053 1.8252 0.1354  -0.2441 -0.2133 1096 HIS A CG  
1949 N ND1 . HIS A 244 ? 0.7093 0.2732 1.9142 0.1427  -0.2666 -0.1919 1096 HIS A ND1 
1950 C CD2 . HIS A 244 ? 0.6865 0.3262 1.7601 0.1478  -0.2263 -0.2194 1096 HIS A CD2 
1951 C CE1 . HIS A 244 ? 0.7125 0.2930 1.9186 0.1596  -0.2625 -0.1851 1096 HIS A CE1 
1952 N NE2 . HIS A 244 ? 0.6291 0.2561 1.7565 0.1625  -0.2380 -0.2023 1096 HIS A NE2 
1953 N N   . GLY A 245 ? 0.7001 0.3168 1.7534 0.1062  -0.2398 -0.3407 1097 GLY A N   
1954 C CA  . GLY A 245 ? 0.7122 0.3220 1.7650 0.0899  -0.2473 -0.3572 1097 GLY A CA  
1955 C C   . GLY A 245 ? 0.6961 0.2921 1.7458 0.0629  -0.2498 -0.2956 1097 GLY A C   
1956 O O   . GLY A 245 ? 0.6428 0.2649 1.6296 0.0531  -0.2313 -0.2550 1097 GLY A O   
1957 N N   . GLN A 246 ? 0.7345 0.2906 1.8562 0.0514  -0.2734 -0.2896 1098 GLN A N   
1958 C CA  . GLN A 246 ? 0.7202 0.2641 1.8527 0.0249  -0.2779 -0.2304 1098 GLN A CA  
1959 C C   . GLN A 246 ? 0.6993 0.2354 1.8423 0.0190  -0.2759 -0.1590 1098 GLN A C   
1960 O O   . GLN A 246 ? 0.7078 0.2485 1.8407 -0.0019 -0.2727 -0.1056 1098 GLN A O   
1961 C CB  . GLN A 246 ? 0.7862 0.2894 2.0018 0.0135  -0.3059 -0.2448 1098 GLN A CB  
1962 C CG  . GLN A 246 ? 0.7698 0.2874 1.9653 0.0102  -0.3080 -0.3020 1098 GLN A CG  
1963 C CD  . GLN A 246 ? 0.8175 0.2951 2.0971 -0.0037 -0.3374 -0.3145 1098 GLN A CD  
1964 O OE1 . GLN A 246 ? 0.8515 0.2846 2.2158 -0.0041 -0.3593 -0.2990 1098 GLN A OE1 
1965 N NE2 . GLN A 246 ? 0.8153 0.3085 2.0748 -0.0156 -0.3396 -0.3419 1098 GLN A NE2 
1966 N N   . MET A 247 ? 0.6519 0.1801 1.8162 0.0376  -0.2781 -0.1585 1099 MET A N   
1967 C CA  . MET A 247 ? 0.6160 0.1427 1.7855 0.0345  -0.2767 -0.0934 1099 MET A CA  
1968 C C   . MET A 247 ? 0.5433 0.1150 1.6214 0.0375  -0.2497 -0.0742 1099 MET A C   
1969 O O   . MET A 247 ? 0.5029 0.0807 1.5729 0.0339  -0.2468 -0.0212 1099 MET A O   
1970 C CB  . MET A 247 ? 0.6638 0.1595 1.9077 0.0537  -0.2951 -0.1003 1099 MET A CB  
1971 C CG  . MET A 247 ? 0.7381 0.1976 2.0590 0.0422  -0.3171 -0.0391 1099 MET A CG  
1972 S SD  . MET A 247 ? 0.6483 0.0736 2.0330 0.0144  -0.3378 -0.0176 1099 MET A SD  
1973 C CE  . MET A 247 ? 0.6630 0.0786 2.0572 0.0235  -0.3437 -0.1100 1099 MET A CE  
1974 N N   . THR A 248 ? 0.5160 0.1193 1.5280 0.0435  -0.2316 -0.1162 1100 THR A N   
1975 C CA  . THR A 248 ? 0.4883 0.1319 1.4186 0.0477  -0.2077 -0.1055 1100 THR A CA  
1976 C C   . THR A 248 ? 0.4295 0.0882 1.3181 0.0294  -0.1974 -0.0438 1100 THR A C   
1977 O O   . THR A 248 ? 0.4513 0.1236 1.3165 0.0324  -0.1906 -0.0109 1100 THR A O   
1978 C CB  . THR A 248 ? 0.4683 0.1429 1.3379 0.0531  -0.1916 -0.1567 1100 THR A CB  
1979 O OG1 . THR A 248 ? 0.5313 0.1996 1.4360 0.0721  -0.1995 -0.2156 1100 THR A OG1 
1980 C CG2 . THR A 248 ? 0.4692 0.1827 1.2603 0.0565  -0.1685 -0.1451 1100 THR A CG2 
1981 N N   . VAL A 249 ? 0.4450 0.1041 1.3259 0.0109  -0.1967 -0.0299 1101 VAL A N   
1982 C CA  . VAL A 249 ? 0.4178 0.0983 1.2548 -0.0056 -0.1843 0.0226  1101 VAL A CA  
1983 C C   . VAL A 249 ? 0.4320 0.1015 1.3064 -0.0122 -0.1939 0.0820  1101 VAL A C   
1984 O O   . VAL A 249 ? 0.4165 0.1105 1.2471 -0.0175 -0.1820 0.1220  1101 VAL A O   
1985 C CB  . VAL A 249 ? 0.4296 0.1147 1.2602 -0.0233 -0.1827 0.0234  1101 VAL A CB  
1986 C CG1 . VAL A 249 ? 0.4699 0.1767 1.2699 -0.0398 -0.1718 0.0801  1101 VAL A CG1 
1987 C CG2 . VAL A 249 ? 0.4542 0.1600 1.2330 -0.0176 -0.1707 -0.0264 1101 VAL A CG2 
1988 N N   . THR A 250 ? 0.4900 0.1235 1.4465 -0.0117 -0.2163 0.0874  1102 THR A N   
1989 C CA  . THR A 250 ? 0.5105 0.1329 1.5099 -0.0176 -0.2283 0.1464  1102 THR A CA  
1990 C C   . THR A 250 ? 0.4908 0.1253 1.4697 -0.0015 -0.2245 0.1559  1102 THR A C   
1991 O O   . THR A 250 ? 0.4561 0.1092 1.4149 -0.0079 -0.2208 0.2079  1102 THR A O   
1992 C CB  . THR A 250 ? 0.5753 0.1519 1.6755 -0.0206 -0.2559 0.1486  1102 THR A CB  
1993 O OG1 . THR A 250 ? 0.6118 0.1773 1.7300 -0.0328 -0.2604 0.1239  1102 THR A OG1 
1994 C CG2 . THR A 250 ? 0.5669 0.1376 1.7080 -0.0343 -0.2672 0.2212  1102 THR A CG2 
1995 N N   . ARG A 251 ? 0.5146 0.1432 1.4979 0.0191  -0.2251 0.1049  1103 ARG A N   
1996 C CA  . ARG A 251 ? 0.5196 0.1640 1.4826 0.0353  -0.2205 0.1070  1103 ARG A CA  
1997 C C   . ARG A 251 ? 0.4781 0.1649 1.3490 0.0315  -0.1971 0.1191  1103 ARG A C   
1998 O O   . ARG A 251 ? 0.4489 0.1529 1.2995 0.0347  -0.1948 0.1494  1103 ARG A O   
1999 C CB  . ARG A 251 ? 0.5389 0.1737 1.5266 0.0583  -0.2240 0.0454  1103 ARG A CB  
2000 C CG  . ARG A 251 ? 0.5942 0.1854 1.6806 0.0671  -0.2497 0.0333  1103 ARG A CG  
2001 C CD  . ARG A 251 ? 0.6020 0.1914 1.7124 0.0936  -0.2517 -0.0246 1103 ARG A CD  
2002 N NE  . ARG A 251 ? 0.6579 0.2049 1.8675 0.1055  -0.2776 -0.0347 1103 ARG A NE  
2003 C CZ  . ARG A 251 ? 0.7048 0.2364 1.9689 0.1146  -0.2930 -0.0017 1103 ARG A CZ  
2004 N NH1 . ARG A 251 ? 0.7796 0.2690 2.1388 0.1262  -0.3177 -0.0165 1103 ARG A NH1 
2005 N NH2 . ARG A 251 ? 0.7188 0.2763 1.9461 0.1126  -0.2857 0.0455  1103 ARG A NH2 
2006 N N   . LEU A 252 ? 0.4535 0.1567 1.2714 0.0246  -0.1814 0.0952  1104 LEU A N   
2007 C CA  . LEU A 252 ? 0.4376 0.1771 1.1724 0.0196  -0.1605 0.1060  1104 LEU A CA  
2008 C C   . LEU A 252 ? 0.4491 0.2021 1.1681 0.0044  -0.1588 0.1667  1104 LEU A C   
2009 O O   . LEU A 252 ? 0.3940 0.1708 1.0713 0.0060  -0.1513 0.1891  1104 LEU A O   
2010 C CB  . LEU A 252 ? 0.4010 0.1515 1.0936 0.0153  -0.1472 0.0699  1104 LEU A CB  
2011 C CG  . LEU A 252 ? 0.3727 0.1561 0.9847 0.0100  -0.1267 0.0760  1104 LEU A CG  
2012 C CD1 . LEU A 252 ? 0.3528 0.1551 0.9281 0.0219  -0.1187 0.0686  1104 LEU A CD1 
2013 C CD2 . LEU A 252 ? 0.3940 0.1834 0.9799 0.0069  -0.1182 0.0395  1104 LEU A CD2 
2014 N N   . VAL A 253 ? 0.4840 0.2240 1.2395 -0.0104 -0.1668 0.1929  1105 VAL A N   
2015 C CA  . VAL A 253 ? 0.4695 0.2271 1.2162 -0.0258 -0.1652 0.2531  1105 VAL A CA  
2016 C C   . VAL A 253 ? 0.4828 0.2440 1.2482 -0.0218 -0.1754 0.2946  1105 VAL A C   
2017 O O   . VAL A 253 ? 0.5024 0.2953 1.2223 -0.0266 -0.1667 0.3297  1105 VAL A O   
2018 C CB  . VAL A 253 ? 0.4976 0.2386 1.2979 -0.0427 -0.1754 0.2758  1105 VAL A CB  
2019 C CG1 . VAL A 253 ? 0.5383 0.2994 1.3435 -0.0579 -0.1765 0.3440  1105 VAL A CG1 
2020 C CG2 . VAL A 253 ? 0.4778 0.2270 1.2488 -0.0500 -0.1635 0.2469  1105 VAL A CG2 
2021 N N   . ASN A 254 ? 0.5239 0.2539 1.3582 -0.0126 -0.1949 0.2906  1106 ASN A N   
2022 C CA  . ASN A 254 ? 0.5492 0.2812 1.4085 -0.0071 -0.2073 0.3297  1106 ASN A CA  
2023 C C   . ASN A 254 ? 0.5349 0.2953 1.3352 0.0054  -0.1965 0.3179  1106 ASN A C   
2024 O O   . ASN A 254 ? 0.5564 0.3398 1.3385 0.0032  -0.1984 0.3599  1106 ASN A O   
2025 C CB  . ASN A 254 ? 0.5969 0.2866 1.5485 0.0029  -0.2316 0.3224  1106 ASN A CB  
2026 C CG  . ASN A 254 ? 0.5878 0.2600 1.6058 -0.0117 -0.2505 0.3803  1106 ASN A CG  
2027 O OD1 . ASN A 254 ? 0.5890 0.2698 1.6010 -0.0311 -0.2461 0.4088  1106 ASN A OD1 
2028 N ND2 . ASN A 254 ? 0.7313 0.3811 1.8154 -0.0027 -0.2718 0.4004  1106 ASN A ND2 
2029 N N   . THR A 255 ? 0.4803 0.2416 1.2512 0.0173  -0.1857 0.2621  1107 THR A N   
2030 C CA  . THR A 255 ? 0.4970 0.2858 1.2126 0.0274  -0.1746 0.2474  1107 THR A CA  
2031 C C   . THR A 255 ? 0.4582 0.2828 1.1005 0.0156  -0.1599 0.2754  1107 THR A C   
2032 O O   . THR A 255 ? 0.4197 0.2674 1.0357 0.0177  -0.1605 0.2988  1107 THR A O   
2033 C CB  . THR A 255 ? 0.4765 0.2643 1.1713 0.0389  -0.1635 0.1850  1107 THR A CB  
2034 O OG1 . THR A 255 ? 0.5794 0.3361 1.3415 0.0494  -0.1763 0.1541  1107 THR A OG1 
2035 C CG2 . THR A 255 ? 0.5597 0.3712 1.2193 0.0503  -0.1568 0.1713  1107 THR A CG2 
2036 N N   . LEU A 256 ? 0.4653 0.2955 1.0776 0.0038  -0.1478 0.2723  1108 LEU A N   
2037 C CA  . LEU A 256 ? 0.4666 0.3309 1.0113 -0.0057 -0.1328 0.2928  1108 LEU A CA  
2038 C C   . LEU A 256 ? 0.4891 0.3718 1.0402 -0.0157 -0.1395 0.3531  1108 LEU A C   
2039 O O   . LEU A 256 ? 0.4842 0.3995 0.9839 -0.0173 -0.1325 0.3714  1108 LEU A O   
2040 C CB  . LEU A 256 ? 0.4567 0.3229 0.9749 -0.0142 -0.1189 0.2737  1108 LEU A CB  
2041 C CG  . LEU A 256 ? 0.4132 0.2697 0.9138 -0.0058 -0.1106 0.2174  1108 LEU A CG  
2042 C CD1 . LEU A 256 ? 0.3910 0.2445 0.8857 -0.0149 -0.1031 0.2045  1108 LEU A CD1 
2043 C CD2 . LEU A 256 ? 0.3523 0.2315 0.7892 0.0012  -0.0979 0.1975  1108 LEU A CD2 
2044 N N   . LYS A 257 ? 0.5343 0.3980 1.1491 -0.0229 -0.1538 0.3839  1109 LYS A N   
2045 C CA  . LYS A 257 ? 0.5844 0.4666 1.2149 -0.0327 -0.1629 0.4470  1109 LYS A CA  
2046 C C   . LYS A 257 ? 0.5955 0.4918 1.2212 -0.0235 -0.1729 0.4668  1109 LYS A C   
2047 O O   . LYS A 257 ? 0.5898 0.5214 1.1859 -0.0301 -0.1723 0.5096  1109 LYS A O   
2048 C CB  . LYS A 257 ? 0.6208 0.4731 1.3345 -0.0414 -0.1803 0.4757  1109 LYS A CB  
2049 C CG  . LYS A 257 ? 0.6688 0.5214 1.3877 -0.0570 -0.1724 0.4808  1109 LYS A CG  
2050 C CD  . LYS A 257 ? 0.6977 0.5207 1.5046 -0.0676 -0.1925 0.5144  1109 LYS A CD  
2051 C CE  . LYS A 257 ? 0.6993 0.5272 1.5147 -0.0853 -0.1853 0.5239  1109 LYS A CE  
2052 N NZ  . LYS A 257 ? 0.7327 0.5305 1.6391 -0.0980 -0.2065 0.5577  1109 LYS A NZ  
2053 N N   . GLU A 258 ? 0.5876 0.4604 1.2422 -0.0080 -0.1820 0.4349  1110 GLU A N   
2054 C CA  . GLU A 258 ? 0.5974 0.4830 1.2530 0.0025  -0.1926 0.4486  1110 GLU A CA  
2055 C C   . GLU A 258 ? 0.5878 0.5118 1.1625 0.0045  -0.1789 0.4373  1110 GLU A C   
2056 O O   . GLU A 258 ? 0.6054 0.5493 1.1725 0.0095  -0.1877 0.4567  1110 GLU A O   
2057 C CB  . GLU A 258 ? 0.6052 0.4583 1.3158 0.0199  -0.2040 0.4119  1110 GLU A CB  
2058 C CG  . GLU A 258 ? 0.6564 0.4700 1.4588 0.0208  -0.2241 0.4274  1110 GLU A CG  
2059 C CD  . GLU A 258 ? 0.6990 0.4776 1.5510 0.0379  -0.2297 0.3728  1110 GLU A CD  
2060 O OE1 . GLU A 258 ? 0.7000 0.4884 1.5157 0.0490  -0.2173 0.3253  1110 GLU A OE1 
2061 O OE2 . GLU A 258 ? 0.8160 0.5586 1.7460 0.0402  -0.2471 0.3775  1110 GLU A OE2 
2062 N N   . GLY A 259 ? 0.5264 0.4599 1.0451 0.0007  -0.1592 0.4060  1111 GLY A N   
2063 C CA  . GLY A 259 ? 0.5060 0.4709 0.9509 0.0020  -0.1465 0.3902  1111 GLY A CA  
2064 C C   . GLY A 259 ? 0.4613 0.4154 0.8922 0.0132  -0.1398 0.3368  1111 GLY A C   
2065 O O   . GLY A 259 ? 0.4716 0.4473 0.8470 0.0139  -0.1305 0.3207  1111 GLY A O   
2066 N N   . LYS A 260 ? 0.4567 0.3796 0.9378 0.0215  -0.1445 0.3089  1112 LYS A N   
2067 C CA  . LYS A 260 ? 0.4243 0.3415 0.8958 0.0322  -0.1372 0.2585  1112 LYS A CA  
2068 C C   . LYS A 260 ? 0.4209 0.3401 0.8453 0.0272  -0.1188 0.2259  1112 LYS A C   
2069 O O   . LYS A 260 ? 0.3781 0.2866 0.8054 0.0195  -0.1139 0.2267  1112 LYS A O   
2070 C CB  . LYS A 260 ? 0.4439 0.3321 0.9835 0.0439  -0.1473 0.2358  1112 LYS A CB  
2071 C CG  . LYS A 260 ? 0.4812 0.3655 1.0742 0.0536  -0.1663 0.2586  1112 LYS A CG  
2072 C CD  . LYS A 260 ? 0.5563 0.4104 1.2193 0.0670  -0.1757 0.2301  1112 LYS A CD  
2073 C CE  . LYS A 260 ? 0.5647 0.4144 1.2866 0.0792  -0.1953 0.2508  1112 LYS A CE  
2074 N NZ  . LYS A 260 ? 0.5821 0.4024 1.3756 0.0950  -0.2046 0.2177  1112 LYS A NZ  
2075 N N   . ARG A 261 ? 0.3842 0.3170 0.7697 0.0315  -0.1097 0.1976  1113 ARG A N   
2076 C CA  . ARG A 261 ? 0.3568 0.2937 0.6957 0.0270  -0.0934 0.1704  1113 ARG A CA  
2077 C C   . ARG A 261 ? 0.3395 0.2789 0.6738 0.0355  -0.0882 0.1316  1113 ARG A C   
2078 O O   . ARG A 261 ? 0.2996 0.2442 0.6571 0.0441  -0.0957 0.1286  1113 ARG A O   
2079 C CB  . ARG A 261 ? 0.3630 0.3233 0.6433 0.0189  -0.0861 0.1870  1113 ARG A CB  
2080 C CG  . ARG A 261 ? 0.3727 0.3411 0.6496 0.0100  -0.0881 0.2263  1113 ARG A CG  
2081 C CD  . ARG A 261 ? 0.3610 0.3164 0.6467 0.0037  -0.0808 0.2226  1113 ARG A CD  
2082 N NE  . ARG A 261 ? 0.3714 0.3409 0.6530 -0.0059 -0.0803 0.2611  1113 ARG A NE  
2083 C CZ  . ARG A 261 ? 0.4357 0.4020 0.7603 -0.0099 -0.0919 0.2979  1113 ARG A CZ  
2084 N NH1 . ARG A 261 ? 0.4765 0.4216 0.8553 -0.0040 -0.1066 0.3004  1113 ARG A NH1 
2085 N NH2 . ARG A 261 ? 0.4587 0.4452 0.7741 -0.0199 -0.0889 0.3340  1113 ARG A NH2 
2086 N N   . LEU A 262 ? 0.3343 0.2725 0.6422 0.0331  -0.0758 0.1038  1114 LEU A N   
2087 C CA  . LEU A 262 ? 0.3303 0.2779 0.6256 0.0387  -0.0685 0.0704  1114 LEU A CA  
2088 C C   . LEU A 262 ? 0.3443 0.3127 0.6129 0.0386  -0.0692 0.0778  1114 LEU A C   
2089 O O   . LEU A 262 ? 0.3266 0.3036 0.5608 0.0314  -0.0691 0.0983  1114 LEU A O   
2090 C CB  . LEU A 262 ? 0.3382 0.2864 0.5984 0.0332  -0.0555 0.0492  1114 LEU A CB  
2091 C CG  . LEU A 262 ? 0.3403 0.2730 0.6228 0.0333  -0.0542 0.0323  1114 LEU A CG  
2092 C CD1 . LEU A 262 ? 0.3056 0.2432 0.5469 0.0264  -0.0426 0.0201  1114 LEU A CD1 
2093 C CD2 . LEU A 262 ? 0.3390 0.2693 0.6597 0.0443  -0.0573 0.0023  1114 LEU A CD2 
2094 N N   . PRO A 263 ? 0.3223 0.3013 0.6081 0.0467  -0.0702 0.0600  1115 PRO A N   
2095 C CA  . PRO A 263 ? 0.3015 0.3013 0.5697 0.0458  -0.0730 0.0672  1115 PRO A CA  
2096 C C   . PRO A 263 ? 0.2769 0.2879 0.4944 0.0371  -0.0628 0.0564  1115 PRO A C   
2097 O O   . PRO A 263 ? 0.2685 0.2735 0.4667 0.0335  -0.0525 0.0410  1115 PRO A O   
2098 C CB  . PRO A 263 ? 0.3182 0.3277 0.6277 0.0577  -0.0760 0.0494  1115 PRO A CB  
2099 C CG  . PRO A 263 ? 0.3451 0.3462 0.6681 0.0623  -0.0674 0.0203  1115 PRO A CG  
2100 C CD  . PRO A 263 ? 0.3293 0.3058 0.6535 0.0573  -0.0691 0.0313  1115 PRO A CD  
2101 N N   . CYS A 264 ? 0.2392 0.2665 0.4393 0.0339  -0.0674 0.0648  1116 CYS A N   
2102 C CA  . CYS A 264 ? 0.2648 0.3011 0.4239 0.0254  -0.0608 0.0553  1116 CYS A CA  
2103 C C   . CYS A 264 ? 0.2415 0.2863 0.4068 0.0265  -0.0512 0.0303  1116 CYS A C   
2104 O O   . CYS A 264 ? 0.2484 0.3075 0.4455 0.0336  -0.0531 0.0224  1116 CYS A O   
2105 C CB  . CYS A 264 ? 0.2449 0.2983 0.3935 0.0219  -0.0709 0.0668  1116 CYS A CB  
2106 S SG  . CYS A 264 ? 0.2630 0.3203 0.3632 0.0101  -0.0664 0.0572  1116 CYS A SG  
2107 N N   . PRO A 265 ? 0.2680 0.3073 0.4047 0.0203  -0.0410 0.0190  1117 PRO A N   
2108 C CA  . PRO A 265 ? 0.2387 0.2919 0.3770 0.0196  -0.0320 -0.0003 1117 PRO A CA  
2109 C C   . PRO A 265 ? 0.2896 0.3661 0.4322 0.0164  -0.0345 -0.0005 1117 PRO A C   
2110 O O   . PRO A 265 ? 0.2464 0.3237 0.3762 0.0109  -0.0430 0.0122  1117 PRO A O   
2111 C CB  . PRO A 265 ? 0.1983 0.2413 0.3005 0.0113  -0.0243 -0.0037 1117 PRO A CB  
2112 C CG  . PRO A 265 ? 0.2580 0.2815 0.3499 0.0114  -0.0264 0.0068  1117 PRO A CG  
2113 C CD  . PRO A 265 ? 0.2587 0.2818 0.3643 0.0146  -0.0371 0.0243  1117 PRO A CD  
2114 N N   . PRO A 266 ? 0.3253 0.4241 0.4862 0.0194  -0.0275 -0.0152 1118 PRO A N   
2115 C CA  . PRO A 266 ? 0.3040 0.4289 0.4699 0.0140  -0.0282 -0.0142 1118 PRO A CA  
2116 C C   . PRO A 266 ? 0.2868 0.4061 0.4188 -0.0008 -0.0294 -0.0065 1118 PRO A C   
2117 O O   . PRO A 266 ? 0.2808 0.3871 0.3879 -0.0062 -0.0230 -0.0093 1118 PRO A O   
2118 C CB  . PRO A 266 ? 0.3312 0.4820 0.5127 0.0183  -0.0159 -0.0321 1118 PRO A CB  
2119 C CG  . PRO A 266 ? 0.3714 0.5117 0.5735 0.0317  -0.0145 -0.0443 1118 PRO A CG  
2120 C CD  . PRO A 266 ? 0.3433 0.4484 0.5227 0.0282  -0.0188 -0.0343 1118 PRO A CD  
2121 N N   . ASN A 267 ? 0.2635 0.3914 0.3973 -0.0067 -0.0394 0.0029  1119 ASN A N   
2122 C CA  . ASN A 267 ? 0.2928 0.4147 0.4010 -0.0207 -0.0437 0.0076  1119 ASN A CA  
2123 C C   . ASN A 267 ? 0.2608 0.3528 0.3350 -0.0233 -0.0468 0.0107  1119 ASN A C   
2124 O O   . ASN A 267 ? 0.3118 0.3942 0.3651 -0.0331 -0.0491 0.0103  1119 ASN A O   
2125 C CB  . ASN A 267 ? 0.2563 0.3913 0.3622 -0.0297 -0.0339 0.0029  1119 ASN A CB  
2126 C CG  . ASN A 267 ? 0.3684 0.5402 0.5060 -0.0267 -0.0276 -0.0013 1119 ASN A CG  
2127 O OD1 . ASN A 267 ? 0.3919 0.5768 0.5373 -0.0198 -0.0158 -0.0111 1119 ASN A OD1 
2128 N ND2 . ASN A 267 ? 0.3143 0.5066 0.4713 -0.0312 -0.0357 0.0047  1119 ASN A ND2 
2129 N N   . CYS A 268 ? 0.2335 0.3118 0.3051 -0.0144 -0.0471 0.0141  1120 CYS A N   
2130 C CA  . CYS A 268 ? 0.2615 0.3179 0.3024 -0.0157 -0.0482 0.0177  1120 CYS A CA  
2131 C C   . CYS A 268 ? 0.2654 0.3260 0.2979 -0.0169 -0.0614 0.0271  1120 CYS A C   
2132 O O   . CYS A 268 ? 0.2743 0.3445 0.3258 -0.0108 -0.0678 0.0367  1120 CYS A O   
2133 C CB  . CYS A 268 ? 0.2794 0.3235 0.3238 -0.0073 -0.0422 0.0197  1120 CYS A CB  
2134 S SG  . CYS A 268 ? 0.2852 0.3116 0.2959 -0.0081 -0.0427 0.0271  1120 CYS A SG  
2135 N N   . PRO A 269 ? 0.2636 0.3180 0.2691 -0.0244 -0.0668 0.0237  1121 PRO A N   
2136 C CA  . PRO A 269 ? 0.2784 0.3412 0.2722 -0.0256 -0.0803 0.0298  1121 PRO A CA  
2137 C C   . PRO A 269 ? 0.2601 0.3223 0.2448 -0.0177 -0.0808 0.0428  1121 PRO A C   
2138 O O   . PRO A 269 ? 0.2697 0.3185 0.2443 -0.0142 -0.0707 0.0431  1121 PRO A O   
2139 C CB  . PRO A 269 ? 0.2758 0.3274 0.2409 -0.0335 -0.0841 0.0180  1121 PRO A CB  
2140 C CG  . PRO A 269 ? 0.3204 0.3594 0.2899 -0.0380 -0.0745 0.0096  1121 PRO A CG  
2141 C CD  . PRO A 269 ? 0.2239 0.2632 0.2097 -0.0311 -0.0619 0.0136  1121 PRO A CD  
2142 N N   . ASP A 270 ? 0.2971 0.3761 0.2859 -0.0161 -0.0930 0.0552  1122 ASP A N   
2143 C CA  . ASP A 270 ? 0.3179 0.4017 0.3008 -0.0102 -0.0952 0.0737  1122 ASP A CA  
2144 C C   . ASP A 270 ? 0.3199 0.3972 0.2650 -0.0107 -0.0890 0.0713  1122 ASP A C   
2145 O O   . ASP A 270 ? 0.2776 0.3530 0.2219 -0.0065 -0.0830 0.0845  1122 ASP A O   
2146 C CB  . ASP A 270 ? 0.3109 0.4181 0.2968 -0.0101 -0.1117 0.0886  1122 ASP A CB  
2147 C CG  . ASP A 270 ? 0.3945 0.5096 0.3801 -0.0048 -0.1142 0.1136  1122 ASP A CG  
2148 O OD1 . ASP A 270 ? 0.3350 0.4424 0.3541 0.0010  -0.1109 0.1255  1122 ASP A OD1 
2149 O OD2 . ASP A 270 ? 0.4095 0.5385 0.3617 -0.0065 -0.1187 0.1206  1122 ASP A OD2 
2150 N N   . GLU A 271 ? 0.3304 0.4052 0.2477 -0.0156 -0.0909 0.0542  1123 GLU A N   
2151 C CA  . GLU A 271 ? 0.3690 0.4406 0.2514 -0.0142 -0.0851 0.0474  1123 GLU A CA  
2152 C C   . GLU A 271 ? 0.3257 0.3784 0.2109 -0.0112 -0.0693 0.0443  1123 GLU A C   
2153 O O   . GLU A 271 ? 0.3518 0.4076 0.2199 -0.0074 -0.0623 0.0492  1123 GLU A O   
2154 C CB  . GLU A 271 ? 0.4208 0.4912 0.2780 -0.0189 -0.0929 0.0253  1123 GLU A CB  
2155 C CG  . GLU A 271 ? 0.4437 0.4945 0.3146 -0.0255 -0.0927 0.0083  1123 GLU A CG  
2156 C CD  . GLU A 271 ? 0.4431 0.5033 0.3358 -0.0328 -0.1054 0.0085  1123 GLU A CD  
2157 O OE1 . GLU A 271 ? 0.3805 0.4592 0.2884 -0.0309 -0.1117 0.0238  1123 GLU A OE1 
2158 O OE2 . GLU A 271 ? 0.4450 0.4945 0.3437 -0.0406 -0.1093 -0.0051 1123 GLU A OE2 
2159 N N   . VAL A 272 ? 0.2456 0.2831 0.1529 -0.0130 -0.0638 0.0371  1124 VAL A N   
2160 C CA  . VAL A 272 ? 0.2996 0.3220 0.2130 -0.0105 -0.0507 0.0349  1124 VAL A CA  
2161 C C   . VAL A 272 ? 0.2917 0.3175 0.2265 -0.0058 -0.0474 0.0523  1124 VAL A C   
2162 O O   . VAL A 272 ? 0.3289 0.3498 0.2604 -0.0033 -0.0391 0.0573  1124 VAL A O   
2163 C CB  . VAL A 272 ? 0.2447 0.2562 0.1739 -0.0143 -0.0470 0.0231  1124 VAL A CB  
2164 C CG1 . VAL A 272 ? 0.2538 0.2536 0.1893 -0.0117 -0.0350 0.0209  1124 VAL A CG1 
2165 C CG2 . VAL A 272 ? 0.2383 0.2432 0.1518 -0.0207 -0.0520 0.0089  1124 VAL A CG2 
2166 N N   . TYR A 273 ? 0.2868 0.3203 0.2480 -0.0046 -0.0546 0.0614  1125 TYR A N   
2167 C CA  . TYR A 273 ? 0.2686 0.3026 0.2578 0.0001  -0.0550 0.0785  1125 TYR A CA  
2168 C C   . TYR A 273 ? 0.3183 0.3622 0.2939 0.0009  -0.0567 0.0996  1125 TYR A C   
2169 O O   . TYR A 273 ? 0.3172 0.3558 0.3087 0.0025  -0.0524 0.1121  1125 TYR A O   
2170 C CB  . TYR A 273 ? 0.2838 0.3259 0.3059 0.0029  -0.0644 0.0838  1125 TYR A CB  
2171 C CG  . TYR A 273 ? 0.2818 0.3192 0.3427 0.0090  -0.0664 0.0980  1125 TYR A CG  
2172 C CD1 . TYR A 273 ? 0.2634 0.2848 0.3431 0.0116  -0.0578 0.0894  1125 TYR A CD1 
2173 C CD2 . TYR A 273 ? 0.3438 0.3922 0.4252 0.0122  -0.0787 0.1193  1125 TYR A CD2 
2174 C CE1 . TYR A 273 ? 0.2855 0.2990 0.4065 0.0172  -0.0620 0.0998  1125 TYR A CE1 
2175 C CE2 . TYR A 273 ? 0.3390 0.3794 0.4625 0.0180  -0.0827 0.1332  1125 TYR A CE2 
2176 C CZ  . TYR A 273 ? 0.3342 0.3556 0.4781 0.0204  -0.0744 0.1220  1125 TYR A CZ  
2177 O OH  . TYR A 273 ? 0.3506 0.3611 0.5409 0.0261  -0.0806 0.1333  1125 TYR A OH  
2178 N N   . GLN A 274 ? 0.3219 0.3829 0.2686 -0.0010 -0.0632 0.1035  1126 GLN A N   
2179 C CA  . GLN A 274 ? 0.3566 0.4354 0.2841 -0.0006 -0.0633 0.1235  1126 GLN A CA  
2180 C C   . GLN A 274 ? 0.3546 0.4281 0.2665 -0.0001 -0.0493 0.1196  1126 GLN A C   
2181 O O   . GLN A 274 ? 0.3392 0.4210 0.2579 0.0000  -0.0455 0.1409  1126 GLN A O   
2182 C CB  . GLN A 274 ? 0.3869 0.4897 0.2815 -0.0021 -0.0730 0.1231  1126 GLN A CB  
2183 C CG  . GLN A 274 ? 0.4639 0.5820 0.3749 -0.0025 -0.0892 0.1375  1126 GLN A CG  
2184 C CD  . GLN A 274 ? 0.5083 0.6258 0.4595 0.0002  -0.0931 0.1662  1126 GLN A CD  
2185 O OE1 . GLN A 274 ? 0.4732 0.5994 0.4249 0.0003  -0.0904 0.1902  1126 GLN A OE1 
2186 N NE2 . GLN A 274 ? 0.4595 0.5673 0.4481 0.0025  -0.0994 0.1637  1126 GLN A NE2 
2187 N N   . LEU A 275 ? 0.3591 0.4192 0.2548 -0.0002 -0.0422 0.0945  1127 LEU A N   
2188 C CA  . LEU A 275 ? 0.3529 0.4077 0.2388 0.0013  -0.0294 0.0894  1127 LEU A CA  
2189 C C   . LEU A 275 ? 0.3383 0.3798 0.2575 0.0010  -0.0238 0.0991  1127 LEU A C   
2190 O O   . LEU A 275 ? 0.3291 0.3761 0.2500 0.0011  -0.0164 0.1106  1127 LEU A O   
2191 C CB  . LEU A 275 ? 0.3729 0.4125 0.2425 0.0017  -0.0253 0.0618  1127 LEU A CB  
2192 C CG  . LEU A 275 ? 0.4455 0.4943 0.2803 0.0034  -0.0275 0.0461  1127 LEU A CG  
2193 C CD1 . LEU A 275 ? 0.6405 0.7102 0.4606 0.0023  -0.0391 0.0516  1127 LEU A CD1 
2194 C CD2 . LEU A 275 ? 0.4926 0.5191 0.3267 0.0017  -0.0288 0.0222  1127 LEU A CD2 
2195 N N   . MET A 276 ? 0.3177 0.3439 0.2645 0.0007  -0.0274 0.0928  1128 MET A N   
2196 C CA  . MET A 276 ? 0.2826 0.2961 0.2646 0.0011  -0.0251 0.0974  1128 MET A CA  
2197 C C   . MET A 276 ? 0.2948 0.3155 0.3003 0.0007  -0.0299 0.1257  1128 MET A C   
2198 O O   . MET A 276 ? 0.3318 0.3464 0.3568 -0.0007 -0.0259 0.1340  1128 MET A O   
2199 C CB  . MET A 276 ? 0.2750 0.2781 0.2803 0.0025  -0.0290 0.0829  1128 MET A CB  
2200 C CG  . MET A 276 ? 0.2955 0.2854 0.3343 0.0043  -0.0266 0.0770  1128 MET A CG  
2201 S SD  . MET A 276 ? 0.3593 0.3479 0.4260 0.0083  -0.0312 0.0609  1128 MET A SD  
2202 C CE  . MET A 276 ? 0.3125 0.3052 0.3473 0.0045  -0.0256 0.0416  1128 MET A CE  
2203 N N   . ARG A 277 ? 0.3226 0.3567 0.3293 0.0011  -0.0399 0.1419  1129 ARG A N   
2204 C CA  . ARG A 277 ? 0.3728 0.4157 0.4038 0.0001  -0.0468 0.1743  1129 ARG A CA  
2205 C C   . ARG A 277 ? 0.3877 0.4490 0.4007 -0.0036 -0.0399 0.1954  1129 ARG A C   
2206 O O   . ARG A 277 ? 0.3502 0.4126 0.3917 -0.0067 -0.0417 0.2215  1129 ARG A O   
2207 C CB  . ARG A 277 ? 0.3927 0.4505 0.4250 0.0016  -0.0601 0.1884  1129 ARG A CB  
2208 C CG  . ARG A 277 ? 0.4356 0.4799 0.5028 0.0061  -0.0685 0.1777  1129 ARG A CG  
2209 C CD  . ARG A 277 ? 0.5534 0.6148 0.6311 0.0078  -0.0834 0.1989  1129 ARG A CD  
2210 N NE  . ARG A 277 ? 0.5920 0.6582 0.6975 0.0071  -0.0910 0.2355  1129 ARG A NE  
2211 C CZ  . ARG A 277 ? 0.5993 0.6461 0.7574 0.0102  -0.0961 0.2452  1129 ARG A CZ  
2212 N NH1 . ARG A 277 ? 0.5770 0.6009 0.7642 0.0155  -0.0936 0.2180  1129 ARG A NH1 
2213 N NH2 . ARG A 277 ? 0.6765 0.7284 0.8600 0.0079  -0.1045 0.2828  1129 ARG A NH2 
2214 N N   . LYS A 278 ? 0.3649 0.4420 0.3337 -0.0033 -0.0324 0.1840  1130 LYS A N   
2215 C CA  . LYS A 278 ? 0.3784 0.4779 0.3270 -0.0051 -0.0224 0.1975  1130 LYS A CA  
2216 C C   . LYS A 278 ? 0.3973 0.4838 0.3672 -0.0072 -0.0126 0.1964  1130 LYS A C   
2217 O O   . LYS A 278 ? 0.4086 0.5150 0.3785 -0.0104 -0.0057 0.2171  1130 LYS A O   
2218 C CB  . LYS A 278 ? 0.3706 0.4868 0.2704 -0.0016 -0.0166 0.1765  1130 LYS A CB  
2219 C CG  . LYS A 278 ? 0.4026 0.5436 0.2755 -0.0009 -0.0263 0.1823  1130 LYS A CG  
2220 C CD  . LYS A 278 ? 0.5357 0.6853 0.3654 0.0033  -0.0230 0.1522  1130 LYS A CD  
2221 C CE  . LYS A 278 ? 0.6154 0.7882 0.4195 0.0034  -0.0352 0.1526  1130 LYS A CE  
2222 N NZ  . LYS A 278 ? 0.7367 0.9505 0.5283 0.0021  -0.0367 0.1852  1130 LYS A NZ  
2223 N N   . CYS A 279 ? 0.3228 0.3803 0.3104 -0.0059 -0.0121 0.1730  1131 CYS A N   
2224 C CA  . CYS A 279 ? 0.3384 0.3819 0.3514 -0.0083 -0.0063 0.1701  1131 CYS A CA  
2225 C C   . CYS A 279 ? 0.3333 0.3686 0.3938 -0.0128 -0.0137 0.1939  1131 CYS A C   
2226 O O   . CYS A 279 ? 0.3237 0.3534 0.4072 -0.0168 -0.0102 0.1981  1131 CYS A O   
2227 C CB  . CYS A 279 ? 0.3147 0.3342 0.3308 -0.0056 -0.0051 0.1383  1131 CYS A CB  
2228 S SG  . CYS A 279 ? 0.2959 0.3183 0.2668 -0.0016 0.0019  0.1121  1131 CYS A SG  
2229 N N   . TRP A 280 ? 0.3539 0.3882 0.4320 -0.0121 -0.0253 0.2090  1132 TRP A N   
2230 C CA  . TRP A 280 ? 0.3159 0.3347 0.4464 -0.0144 -0.0358 0.2270  1132 TRP A CA  
2231 C C   . TRP A 280 ? 0.3696 0.4085 0.5120 -0.0187 -0.0433 0.2701  1132 TRP A C   
2232 O O   . TRP A 280 ? 0.3813 0.4081 0.5644 -0.0183 -0.0561 0.2862  1132 TRP A O   
2233 C CB  . TRP A 280 ? 0.3420 0.3397 0.4940 -0.0078 -0.0447 0.2056  1132 TRP A CB  
2234 C CG  . TRP A 280 ? 0.2841 0.2657 0.4297 -0.0042 -0.0385 0.1671  1132 TRP A CG  
2235 C CD1 . TRP A 280 ? 0.2695 0.2446 0.4113 -0.0067 -0.0300 0.1521  1132 TRP A CD1 
2236 C CD2 . TRP A 280 ? 0.3182 0.2920 0.4642 0.0020  -0.0411 0.1416  1132 TRP A CD2 
2237 N NE1 . TRP A 280 ? 0.3264 0.2908 0.4629 -0.0026 -0.0274 0.1199  1132 TRP A NE1 
2238 C CE2 . TRP A 280 ? 0.3159 0.2805 0.4545 0.0025  -0.0332 0.1130  1132 TRP A CE2 
2239 C CE3 . TRP A 280 ? 0.2788 0.2567 0.4307 0.0068  -0.0492 0.1415  1132 TRP A CE3 
2240 C CZ2 . TRP A 280 ? 0.2792 0.2403 0.4154 0.0071  -0.0322 0.0861  1132 TRP A CZ2 
2241 C CZ3 . TRP A 280 ? 0.3068 0.2805 0.4590 0.0117  -0.0478 0.1130  1132 TRP A CZ3 
2242 C CH2 . TRP A 280 ? 0.2531 0.2195 0.3966 0.0115  -0.0388 0.0864  1132 TRP A CH2 
2243 N N   . GLU A 281 ? 0.3660 0.4375 0.4744 -0.0224 -0.0355 0.2893  1133 GLU A N   
2244 C CA  . GLU A 281 ? 0.3956 0.4918 0.5174 -0.0288 -0.0408 0.3357  1133 GLU A CA  
2245 C C   . GLU A 281 ? 0.3824 0.4633 0.5573 -0.0367 -0.0429 0.3555  1133 GLU A C   
2246 O O   . GLU A 281 ? 0.3909 0.4610 0.5705 -0.0386 -0.0342 0.3369  1133 GLU A O   
2247 C CB  . GLU A 281 ? 0.4303 0.5713 0.5016 -0.0304 -0.0294 0.3481  1133 GLU A CB  
2248 C CG  . GLU A 281 ? 0.4797 0.6392 0.5015 -0.0239 -0.0309 0.3325  1133 GLU A CG  
2249 C CD  . GLU A 281 ? 0.6039 0.7765 0.6342 -0.0244 -0.0467 0.3613  1133 GLU A CD  
2250 O OE1 . GLU A 281 ? 0.6848 0.8291 0.7534 -0.0223 -0.0595 0.3607  1133 GLU A OE1 
2251 O OE2 . GLU A 281 ? 0.6968 0.9112 0.6953 -0.0261 -0.0466 0.3841  1133 GLU A OE2 
2252 N N   . PHE A 282 ? 0.3978 0.4766 0.6163 -0.0418 -0.0561 0.3933  1134 PHE A N   
2253 C CA  . PHE A 282 ? 0.4078 0.4653 0.6866 -0.0500 -0.0620 0.4109  1134 PHE A CA  
2254 C C   . PHE A 282 ? 0.4376 0.5211 0.7090 -0.0602 -0.0488 0.4293  1134 PHE A C   
2255 O O   . PHE A 282 ? 0.4325 0.4973 0.7315 -0.0646 -0.0462 0.4160  1134 PHE A O   
2256 C CB  . PHE A 282 ? 0.4436 0.4946 0.7736 -0.0537 -0.0805 0.4528  1134 PHE A CB  
2257 C CG  . PHE A 282 ? 0.4668 0.4804 0.8699 -0.0590 -0.0921 0.4582  1134 PHE A CG  
2258 C CD1 . PHE A 282 ? 0.5016 0.4730 0.9402 -0.0498 -0.1023 0.4228  1134 PHE A CD1 
2259 C CD2 . PHE A 282 ? 0.4924 0.5149 0.9300 -0.0732 -0.0930 0.4968  1134 PHE A CD2 
2260 C CE1 . PHE A 282 ? 0.5043 0.4403 1.0119 -0.0537 -0.1145 0.4225  1134 PHE A CE1 
2261 C CE2 . PHE A 282 ? 0.5157 0.5010 1.0249 -0.0791 -0.1058 0.4995  1134 PHE A CE2 
2262 C CZ  . PHE A 282 ? 0.5018 0.4423 1.0454 -0.0687 -0.1171 0.4600  1134 PHE A CZ  
2263 N N   . GLN A 283 ? 0.4910 0.6215 0.7249 -0.0636 -0.0406 0.4582  1135 GLN A N   
2264 C CA  . GLN A 283 ? 0.4775 0.6439 0.6982 -0.0716 -0.0252 0.4755  1135 GLN A CA  
2265 C C   . GLN A 283 ? 0.4483 0.6217 0.6194 -0.0633 -0.0080 0.4311  1135 GLN A C   
2266 O O   . GLN A 283 ? 0.4451 0.6302 0.5657 -0.0537 -0.0038 0.4088  1135 GLN A O   
2267 C CB  . GLN A 283 ? 0.5554 0.7764 0.7525 -0.0769 -0.0220 0.5223  1135 GLN A CB  
2268 C CG  . GLN A 283 ? 0.5626 0.7829 0.8105 -0.0867 -0.0393 0.5760  1135 GLN A CG  
2269 C CD  . GLN A 283 ? 0.5746 0.7789 0.8902 -0.1008 -0.0441 0.6044  1135 GLN A CD  
2270 O OE1 . GLN A 283 ? 0.5583 0.7721 0.8759 -0.1062 -0.0313 0.5972  1135 GLN A OE1 
2271 N NE2 . GLN A 283 ? 0.5928 0.7723 0.9680 -0.1068 -0.0641 0.6372  1135 GLN A NE2 
2272 N N   . PRO A 284 ? 0.4357 0.6022 0.6241 -0.0673 0.0002  0.4189  1136 PRO A N   
2273 C CA  . PRO A 284 ? 0.4215 0.5954 0.5704 -0.0597 0.0155  0.3815  1136 PRO A CA  
2274 C C   . PRO A 284 ? 0.4372 0.6576 0.5267 -0.0530 0.0294  0.3806  1136 PRO A C   
2275 O O   . PRO A 284 ? 0.4508 0.6661 0.5006 -0.0422 0.0355  0.3428  1136 PRO A O   
2276 C CB  . PRO A 284 ? 0.4605 0.6390 0.6451 -0.0691 0.0213  0.3915  1136 PRO A CB  
2277 C CG  . PRO A 284 ? 0.4480 0.5985 0.6960 -0.0798 0.0052  0.4150  1136 PRO A CG  
2278 C CD  . PRO A 284 ? 0.4413 0.5909 0.6932 -0.0796 -0.0068 0.4405  1136 PRO A CD  
2279 N N   . SER A 285 ? 0.4912 0.7574 0.5767 -0.0595 0.0338  0.4222  1137 SER A N   
2280 C CA  . SER A 285 ? 0.5127 0.8321 0.5424 -0.0531 0.0475  0.4229  1137 SER A CA  
2281 C C   . SER A 285 ? 0.5263 0.8470 0.5112 -0.0436 0.0409  0.4055  1137 SER A C   
2282 O O   . SER A 285 ? 0.5447 0.8969 0.4790 -0.0346 0.0510  0.3860  1137 SER A O   
2283 C CB  . SER A 285 ? 0.5431 0.9177 0.5823 -0.0640 0.0536  0.4765  1137 SER A CB  
2284 O OG  . SER A 285 ? 0.5134 0.8743 0.5968 -0.0754 0.0370  0.5183  1137 SER A OG  
2285 N N   . ASN A 286 ? 0.5064 0.7945 0.5128 -0.0452 0.0234  0.4114  1138 ASN A N   
2286 C CA  . ASN A 286 ? 0.5101 0.7942 0.4819 -0.0372 0.0146  0.3930  1138 ASN A CA  
2287 C C   . ASN A 286 ? 0.4960 0.7408 0.4519 -0.0276 0.0140  0.3405  1138 ASN A C   
2288 O O   . ASN A 286 ? 0.5163 0.7632 0.4383 -0.0211 0.0091  0.3208  1138 ASN A O   
2289 C CB  . ASN A 286 ? 0.4922 0.7619 0.4975 -0.0422 -0.0044 0.4235  1138 ASN A CB  
2290 C CG  . ASN A 286 ? 0.5757 0.8897 0.5906 -0.0517 -0.0066 0.4804  1138 ASN A CG  
2291 O OD1 . ASN A 286 ? 0.6300 0.9295 0.6910 -0.0586 -0.0211 0.5147  1138 ASN A OD1 
2292 N ND2 . ASN A 286 ? 0.5387 0.9087 0.5118 -0.0517 0.0074  0.4910  1138 ASN A ND2 
2293 N N   . ARG A 287 ? 0.4583 0.6698 0.4389 -0.0276 0.0178  0.3194  1139 ARG A N   
2294 C CA  . ARG A 287 ? 0.4464 0.6227 0.4152 -0.0200 0.0168  0.2748  1139 ARG A CA  
2295 C C   . ARG A 287 ? 0.4491 0.6425 0.3693 -0.0114 0.0279  0.2451  1139 ARG A C   
2296 O O   . ARG A 287 ? 0.4912 0.7209 0.3915 -0.0100 0.0401  0.2522  1139 ARG A O   
2297 C CB  . ARG A 287 ? 0.4313 0.5725 0.4378 -0.0225 0.0172  0.2615  1139 ARG A CB  
2298 C CG  . ARG A 287 ? 0.4428 0.5571 0.4994 -0.0281 0.0036  0.2773  1139 ARG A CG  
2299 C CD  . ARG A 287 ? 0.3645 0.4526 0.4589 -0.0318 0.0041  0.2664  1139 ARG A CD  
2300 N NE  . ARG A 287 ? 0.3666 0.4375 0.5144 -0.0386 -0.0084 0.2898  1139 ARG A NE  
2301 C CZ  . ARG A 287 ? 0.4042 0.4600 0.5965 -0.0456 -0.0112 0.2951  1139 ARG A CZ  
2302 N NH1 . ARG A 287 ? 0.3014 0.3582 0.4903 -0.0469 -0.0021 0.2782  1139 ARG A NH1 
2303 N NH2 . ARG A 287 ? 0.3875 0.4260 0.6312 -0.0513 -0.0250 0.3170  1139 ARG A NH2 
2304 N N   . THR A 288 ? 0.4435 0.6112 0.3477 -0.0056 0.0233  0.2117  1140 THR A N   
2305 C CA  . THR A 288 ? 0.4281 0.6006 0.2951 0.0027  0.0309  0.1792  1140 THR A CA  
2306 C C   . THR A 288 ? 0.4101 0.5756 0.2877 0.0047  0.0425  0.1671  1140 THR A C   
2307 O O   . THR A 288 ? 0.4084 0.5558 0.3215 -0.0007 0.0419  0.1756  1140 THR A O   
2308 C CB  . THR A 288 ? 0.4128 0.5558 0.2691 0.0060  0.0211  0.1502  1140 THR A CB  
2309 O OG1 . THR A 288 ? 0.4396 0.5882 0.2611 0.0135  0.0256  0.1214  1140 THR A OG1 
2310 C CG2 . THR A 288 ? 0.4332 0.5371 0.3209 0.0037  0.0179  0.1385  1140 THR A CG2 
2311 N N   . SER A 289 ? 0.4139 0.5944 0.2625 0.0131  0.0518  0.1459  1141 SER A N   
2312 C CA  . SER A 289 ? 0.4128 0.5856 0.2704 0.0173  0.0614  0.1303  1141 SER A CA  
2313 C C   . SER A 289 ? 0.3436 0.4759 0.2017 0.0205  0.0553  0.1000  1141 SER A C   
2314 O O   . SER A 289 ? 0.3935 0.5095 0.2390 0.0208  0.0459  0.0876  1141 SER A O   
2315 C CB  . SER A 289 ? 0.4219 0.6313 0.2514 0.0269  0.0740  0.1206  1141 SER A CB  
2316 O OG  . SER A 289 ? 0.3801 0.5868 0.1759 0.0352  0.0699  0.0930  1141 SER A OG  
2317 N N   . PHE A 290 ? 0.3467 0.4670 0.2192 0.0226  0.0605  0.0895  1142 PHE A N   
2318 C CA  . PHE A 290 ? 0.2772 0.3656 0.1471 0.0263  0.0558  0.0631  1142 PHE A CA  
2319 C C   . PHE A 290 ? 0.3510 0.4416 0.1899 0.0357  0.0557  0.0394  1142 PHE A C   
2320 O O   . PHE A 290 ? 0.3191 0.3855 0.1510 0.0352  0.0467  0.0238  1142 PHE A O   
2321 C CB  . PHE A 290 ? 0.3260 0.4050 0.2175 0.0267  0.0600  0.0592  1142 PHE A CB  
2322 C CG  . PHE A 290 ? 0.2684 0.3310 0.1901 0.0173  0.0544  0.0700  1142 PHE A CG  
2323 C CD1 . PHE A 290 ? 0.3000 0.3370 0.2257 0.0135  0.0448  0.0619  1142 PHE A CD1 
2324 C CD2 . PHE A 290 ? 0.2743 0.3490 0.2225 0.0122  0.0582  0.0869  1142 PHE A CD2 
2325 C CE1 . PHE A 290 ? 0.2373 0.2614 0.1904 0.0068  0.0396  0.0667  1142 PHE A CE1 
2326 C CE2 . PHE A 290 ? 0.2922 0.3501 0.2704 0.0040  0.0511  0.0924  1142 PHE A CE2 
2327 C CZ  . PHE A 290 ? 0.2930 0.3257 0.2725 0.0023  0.0420  0.0805  1142 PHE A CZ  
2328 N N   . GLN A 291 ? 0.3646 0.4861 0.1865 0.0439  0.0651  0.0363  1143 GLN A N   
2329 C CA  . GLN A 291 ? 0.3695 0.4935 0.1637 0.0543  0.0640  0.0091  1143 GLN A CA  
2330 C C   . GLN A 291 ? 0.3831 0.5070 0.1555 0.0512  0.0533  0.0052  1143 GLN A C   
2331 O O   . GLN A 291 ? 0.3767 0.4797 0.1386 0.0540  0.0447  -0.0185 1143 GLN A O   
2332 C CB  . GLN A 291 ? 0.4199 0.5815 0.2016 0.0660  0.0775  0.0026  1143 GLN A CB  
2333 C CG  . GLN A 291 ? 0.4085 0.5615 0.2106 0.0730  0.0843  -0.0066 1143 GLN A CG  
2334 C CD  . GLN A 291 ? 0.4866 0.6828 0.2843 0.0843  0.0998  -0.0084 1143 GLN A CD  
2335 O OE1 . GLN A 291 ? 0.5163 0.7526 0.2918 0.0874  0.1066  -0.0042 1143 GLN A OE1 
2336 N NE2 . GLN A 291 ? 0.4370 0.6296 0.2560 0.0909  0.1055  -0.0143 1143 GLN A NE2 
2337 N N   . ASN A 292 ? 0.4040 0.5498 0.1737 0.0443  0.0521  0.0301  1144 ASN A N   
2338 C CA  . ASN A 292 ? 0.4470 0.5955 0.1987 0.0408  0.0403  0.0296  1144 ASN A CA  
2339 C C   . ASN A 292 ? 0.3951 0.5045 0.1637 0.0334  0.0276  0.0253  1144 ASN A C   
2340 O O   . ASN A 292 ? 0.3731 0.4734 0.1283 0.0328  0.0168  0.0099  1144 ASN A O   
2341 C CB  . ASN A 292 ? 0.4686 0.6536 0.2154 0.0357  0.0413  0.0616  1144 ASN A CB  
2342 C CG  . ASN A 292 ? 0.6209 0.8552 0.3434 0.0429  0.0538  0.0649  1144 ASN A CG  
2343 O OD1 . ASN A 292 ? 0.6810 0.9246 0.3832 0.0540  0.0597  0.0363  1144 ASN A OD1 
2344 N ND2 . ASN A 292 ? 0.6810 0.9491 0.4076 0.0370  0.0579  0.1005  1144 ASN A ND2 
2345 N N   . LEU A 293 ? 0.3880 0.4764 0.1865 0.0280  0.0288  0.0367  1145 LEU A N   
2346 C CA  . LEU A 293 ? 0.3734 0.4290 0.1882 0.0226  0.0197  0.0294  1145 LEU A CA  
2347 C C   . LEU A 293 ? 0.3540 0.3885 0.1602 0.0262  0.0167  0.0024  1145 LEU A C   
2348 O O   . LEU A 293 ? 0.3323 0.3518 0.1374 0.0223  0.0066  -0.0071 1145 LEU A O   
2349 C CB  . LEU A 293 ? 0.3767 0.4185 0.2228 0.0179  0.0227  0.0416  1145 LEU A CB  
2350 C CG  . LEU A 293 ? 0.3473 0.3987 0.2130 0.0123  0.0206  0.0675  1145 LEU A CG  
2351 C CD1 . LEU A 293 ? 0.2924 0.3343 0.1879 0.0093  0.0251  0.0753  1145 LEU A CD1 
2352 C CD2 . LEU A 293 ? 0.3220 0.3632 0.1953 0.0084  0.0090  0.0690  1145 LEU A CD2 
2353 N N   . ILE A 294 ? 0.3504 0.3849 0.1539 0.0335  0.0247  -0.0087 1146 ILE A N   
2354 C CA  . ILE A 294 ? 0.3808 0.3925 0.1820 0.0376  0.0207  -0.0323 1146 ILE A CA  
2355 C C   . ILE A 294 ? 0.4319 0.4462 0.2107 0.0400  0.0117  -0.0506 1146 ILE A C   
2356 O O   . ILE A 294 ? 0.4396 0.4310 0.2224 0.0355  0.0009  -0.0621 1146 ILE A O   
2357 C CB  . ILE A 294 ? 0.3705 0.3848 0.1759 0.0474  0.0305  -0.0402 1146 ILE A CB  
2358 C CG1 . ILE A 294 ? 0.3022 0.3098 0.1321 0.0431  0.0355  -0.0248 1146 ILE A CG1 
2359 C CG2 . ILE A 294 ? 0.4241 0.4152 0.2286 0.0535  0.0244  -0.0648 1146 ILE A CG2 
2360 C CD1 . ILE A 294 ? 0.2984 0.3209 0.1354 0.0513  0.0464  -0.0240 1146 ILE A CD1 
2361 N N   . GLU A 295 ? 0.4559 0.5013 0.2122 0.0460  0.0156  -0.0523 1147 GLU A N   
2362 C CA  . GLU A 295 ? 0.4531 0.5080 0.1848 0.0484  0.0061  -0.0709 1147 GLU A CA  
2363 C C   . GLU A 295 ? 0.4034 0.4496 0.1382 0.0372  -0.0076 -0.0633 1147 GLU A C   
2364 O O   . GLU A 295 ? 0.3871 0.4186 0.1178 0.0350  -0.0200 -0.0825 1147 GLU A O   
2365 C CB  . GLU A 295 ? 0.4899 0.5898 0.1946 0.0558  0.0139  -0.0686 1147 GLU A CB  
2366 C CG  . GLU A 295 ? 0.5139 0.6284 0.2120 0.0696  0.0265  -0.0850 1147 GLU A CG  
2367 C CD  . GLU A 295 ? 0.5383 0.7013 0.2037 0.0785  0.0327  -0.0925 1147 GLU A CD  
2368 O OE1 . GLU A 295 ? 0.5369 0.7309 0.1887 0.0725  0.0325  -0.0694 1147 GLU A OE1 
2369 O OE2 . GLU A 295 ? 0.5570 0.7294 0.2111 0.0923  0.0375  -0.1215 1147 GLU A OE2 
2370 N N   . GLY A 296 ? 0.3949 0.4491 0.1421 0.0302  -0.0060 -0.0356 1148 GLY A N   
2371 C CA  . GLY A 296 ? 0.3900 0.4391 0.1464 0.0210  -0.0178 -0.0255 1148 GLY A CA  
2372 C C   . GLY A 296 ? 0.3385 0.3552 0.1150 0.0146  -0.0250 -0.0351 1148 GLY A C   
2373 O O   . GLY A 296 ? 0.3455 0.3575 0.1208 0.0094  -0.0375 -0.0436 1148 GLY A O   
2374 N N   . PHE A 297 ? 0.3650 0.3630 0.1600 0.0144  -0.0176 -0.0328 1149 PHE A N   
2375 C CA  . PHE A 297 ? 0.3519 0.3243 0.1649 0.0078  -0.0232 -0.0390 1149 PHE A CA  
2376 C C   . PHE A 297 ? 0.3619 0.3183 0.1675 0.0087  -0.0313 -0.0618 1149 PHE A C   
2377 O O   . PHE A 297 ? 0.3921 0.3371 0.2061 0.0008  -0.0423 -0.0669 1149 PHE A O   
2378 C CB  . PHE A 297 ? 0.3395 0.3000 0.1707 0.0076  -0.0143 -0.0317 1149 PHE A CB  
2379 C CG  . PHE A 297 ? 0.3018 0.2726 0.1470 0.0058  -0.0087 -0.0131 1149 PHE A CG  
2380 C CD1 . PHE A 297 ? 0.3344 0.3098 0.1917 0.0003  -0.0145 -0.0040 1149 PHE A CD1 
2381 C CD2 . PHE A 297 ? 0.3175 0.2929 0.1682 0.0098  0.0014  -0.0053 1149 PHE A CD2 
2382 C CE1 . PHE A 297 ? 0.3262 0.3080 0.2018 -0.0001 -0.0108 0.0108  1149 PHE A CE1 
2383 C CE2 . PHE A 297 ? 0.2959 0.2779 0.1643 0.0076  0.0044  0.0105  1149 PHE A CE2 
2384 C CZ  . PHE A 297 ? 0.3233 0.3066 0.2046 0.0031  -0.0020 0.0175  1149 PHE A CZ  
2385 N N   . GLU A 298 ? 0.4084 0.3652 0.2014 0.0186  -0.0264 -0.0758 1150 GLU A N   
2386 C CA  . GLU A 298 ? 0.4714 0.4108 0.2606 0.0218  -0.0352 -0.1011 1150 GLU A CA  
2387 C C   . GLU A 298 ? 0.5017 0.4466 0.2791 0.0171  -0.0496 -0.1138 1150 GLU A C   
2388 O O   . GLU A 298 ? 0.4919 0.4147 0.2808 0.0109  -0.0624 -0.1265 1150 GLU A O   
2389 C CB  . GLU A 298 ? 0.5120 0.4586 0.2890 0.0362  -0.0267 -0.1163 1150 GLU A CB  
2390 C CG  . GLU A 298 ? 0.4974 0.4302 0.2926 0.0401  -0.0175 -0.1095 1150 GLU A CG  
2391 C CD  . GLU A 298 ? 0.6213 0.5657 0.4087 0.0557  -0.0077 -0.1233 1150 GLU A CD  
2392 O OE1 . GLU A 298 ? 0.6619 0.6308 0.4267 0.0639  -0.0053 -0.1367 1150 GLU A OE1 
2393 O OE2 . GLU A 298 ? 0.6824 0.6152 0.4867 0.0601  -0.0024 -0.1203 1150 GLU A OE2 
2394 N N   . ALA A 299 ? 0.4999 0.4752 0.2566 0.0191  -0.0489 -0.1082 1151 ALA A N   
2395 C CA  . ALA A 299 ? 0.5099 0.4965 0.2537 0.0144  -0.0638 -0.1183 1151 ALA A CA  
2396 C C   . ALA A 299 ? 0.4978 0.4711 0.2645 0.0005  -0.0751 -0.1082 1151 ALA A C   
2397 O O   . ALA A 299 ? 0.4726 0.4380 0.2416 -0.0057 -0.0906 -0.1237 1151 ALA A O   
2398 C CB  . ALA A 299 ? 0.4988 0.5258 0.2171 0.0184  -0.0605 -0.1066 1151 ALA A CB  
2399 N N   . LEU A 300 ? 0.4590 0.4316 0.2447 -0.0042 -0.0676 -0.0840 1152 LEU A N   
2400 C CA  . LEU A 300 ? 0.4717 0.4378 0.2812 -0.0159 -0.0756 -0.0740 1152 LEU A CA  
2401 C C   . LEU A 300 ? 0.4789 0.4167 0.3093 -0.0229 -0.0792 -0.0814 1152 LEU A C   
2402 O O   . LEU A 300 ? 0.5055 0.4397 0.3534 -0.0338 -0.0892 -0.0793 1152 LEU A O   
2403 C CB  . LEU A 300 ? 0.4597 0.4367 0.2839 -0.0167 -0.0664 -0.0494 1152 LEU A CB  
2404 C CG  . LEU A 300 ? 0.4971 0.5011 0.3100 -0.0125 -0.0658 -0.0351 1152 LEU A CG  
2405 C CD1 . LEU A 300 ? 0.4802 0.4870 0.3154 -0.0126 -0.0575 -0.0139 1152 LEU A CD1 
2406 C CD2 . LEU A 300 ? 0.5065 0.5275 0.3132 -0.0171 -0.0814 -0.0369 1152 LEU A CD2 
2407 N N   . LEU A 301 ? 0.4337 0.3543 0.2641 -0.0169 -0.0716 -0.0876 1153 LEU A N   
2408 C CA  . LEU A 301 ? 0.4720 0.3654 0.3224 -0.0228 -0.0762 -0.0921 1153 LEU A CA  
2409 C C   . LEU A 301 ? 0.5494 0.4243 0.4009 -0.0247 -0.0920 -0.1158 1153 LEU A C   
2410 O O   . LEU A 301 ? 0.5486 0.4050 0.4232 -0.0358 -0.1018 -0.1144 1153 LEU A O   
2411 C CB  . LEU A 301 ? 0.4403 0.3230 0.2932 -0.0148 -0.0639 -0.0886 1153 LEU A CB  
2412 C CG  . LEU A 301 ? 0.4031 0.2955 0.2651 -0.0163 -0.0513 -0.0668 1153 LEU A CG  
2413 C CD1 . LEU A 301 ? 0.4152 0.3012 0.2759 -0.0070 -0.0409 -0.0664 1153 LEU A CD1 
2414 C CD2 . LEU A 301 ? 0.4216 0.3096 0.3060 -0.0290 -0.0548 -0.0544 1153 LEU A CD2 
2415 N N   . LYS A 302 ? 0.6359 0.5171 0.4640 -0.0139 -0.0942 -0.1374 1154 LYS A N   
2416 C CA  . LYS A 302 ? 0.7465 0.6090 0.5745 -0.0119 -0.1090 -0.1674 1154 LYS A CA  
2417 C C   . LYS A 302 ? 0.7819 0.6687 0.5806 -0.0065 -0.1160 -0.1872 1154 LYS A C   
2418 O O   . LYS A 302 ? 0.7810 0.6981 0.5546 0.0017  -0.1051 -0.1805 1154 LYS A O   
2419 C CB  . LYS A 302 ? 0.7864 0.6294 0.6165 0.0014  -0.1032 -0.1826 1154 LYS A CB  
2420 C CG  . LYS A 302 ? 0.7952 0.6230 0.6459 0.0009  -0.0923 -0.1612 1154 LYS A CG  
2421 C CD  . LYS A 302 ? 0.7408 0.5909 0.5755 0.0122  -0.0727 -0.1494 1154 LYS A CD  
2422 C CE  . LYS A 302 ? 0.7809 0.6168 0.6357 0.0121  -0.0644 -0.1320 1154 LYS A CE  
2423 N NZ  . LYS A 302 ? 0.7141 0.5666 0.5583 0.0246  -0.0480 -0.1270 1154 LYS A NZ  
2424 O OXT . LYS A 302 ? 0.8536 0.7316 0.6537 -0.0103 -0.1335 -0.2107 1154 LYS A OXT 
2425 N N   . VAL B 13  ? 0.6092 0.7991 0.7832 0.2456  0.1768  -0.0895 865  VAL B N   
2426 C CA  . VAL B 13  ? 0.6104 0.7296 0.7426 0.2160  0.1700  -0.0877 865  VAL B CA  
2427 C C   . VAL B 13  ? 0.5693 0.6790 0.6992 0.2044  0.1472  -0.0648 865  VAL B C   
2428 O O   . VAL B 13  ? 0.6066 0.6898 0.7398 0.2269  0.1388  -0.0510 865  VAL B O   
2429 C CB  . VAL B 13  ? 0.6749 0.7148 0.7811 0.2310  0.1802  -0.0994 865  VAL B CB  
2430 C CG1 . VAL B 13  ? 0.6985 0.7406 0.7916 0.2260  0.2026  -0.1276 865  VAL B CG1 
2431 C CG2 . VAL B 13  ? 0.7155 0.7315 0.8391 0.2764  0.1818  -0.0922 865  VAL B CG2 
2432 N N   . ASP B 14  ? 0.4890 0.6197 0.6121 0.1702  0.1383  -0.0607 866  ASP B N   
2433 C CA  . ASP B 14  ? 0.4434 0.5677 0.5622 0.1563  0.1185  -0.0434 866  ASP B CA  
2434 C C   . ASP B 14  ? 0.4311 0.4935 0.5129 0.1341  0.1151  -0.0444 866  ASP B C   
2435 O O   . ASP B 14  ? 0.3929 0.4542 0.4584 0.1092  0.1192  -0.0524 866  ASP B O   
2436 C CB  . ASP B 14  ? 0.4042 0.5872 0.5392 0.1332  0.1116  -0.0408 866  ASP B CB  
2437 C CG  . ASP B 14  ? 0.3935 0.5750 0.5256 0.1209  0.0921  -0.0268 866  ASP B CG  
2438 O OD1 . ASP B 14  ? 0.3716 0.5072 0.4854 0.1249  0.0839  -0.0181 866  ASP B OD1 
2439 O OD2 . ASP B 14  ? 0.4035 0.6316 0.5512 0.1050  0.0860  -0.0260 866  ASP B OD2 
2440 N N   . PRO B 15  ? 0.4705 0.4867 0.5393 0.1416  0.1070  -0.0343 867  PRO B N   
2441 C CA  . PRO B 15  ? 0.4708 0.4355 0.5072 0.1200  0.1042  -0.0365 867  PRO B CA  
2442 C C   . PRO B 15  ? 0.4217 0.4006 0.4502 0.0929  0.0913  -0.0301 867  PRO B C   
2443 O O   . PRO B 15  ? 0.4162 0.3651 0.4204 0.0743  0.0887  -0.0329 867  PRO B O   
2444 C CB  . PRO B 15  ? 0.5230 0.4426 0.5526 0.1354  0.0999  -0.0250 867  PRO B CB  
2445 C CG  . PRO B 15  ? 0.4896 0.4466 0.5462 0.1592  0.0922  -0.0091 867  PRO B CG  
2446 C CD  . PRO B 15  ? 0.4915 0.5055 0.5745 0.1691  0.0996  -0.0184 867  PRO B CD  
2447 N N   . THR B 16  ? 0.3393 0.3646 0.3887 0.0913  0.0832  -0.0228 868  THR B N   
2448 C CA  . THR B 16  ? 0.2827 0.3213 0.3271 0.0679  0.0734  -0.0198 868  THR B CA  
2449 C C   . THR B 16  ? 0.2478 0.3097 0.2936 0.0509  0.0806  -0.0277 868  THR B C   
2450 O O   . THR B 16  ? 0.1941 0.2623 0.2364 0.0329  0.0739  -0.0251 868  THR B O   
2451 C CB  . THR B 16  ? 0.2840 0.3552 0.3461 0.0713  0.0600  -0.0093 868  THR B CB  
2452 O OG1 . THR B 16  ? 0.2235 0.3472 0.3132 0.0777  0.0626  -0.0117 868  THR B OG1 
2453 C CG2 . THR B 16  ? 0.3115 0.3632 0.3708 0.0887  0.0533  0.0030  868  THR B CG2 
2454 N N   . HIS B 17  ? 0.2634 0.3356 0.3126 0.0565  0.0952  -0.0372 869  HIS B N   
2455 C CA  . HIS B 17  ? 0.2599 0.3540 0.3068 0.0388  0.1045  -0.0429 869  HIS B CA  
2456 C C   . HIS B 17  ? 0.3027 0.3625 0.3182 0.0300  0.1121  -0.0496 869  HIS B C   
2457 O O   . HIS B 17  ? 0.3311 0.3767 0.3403 0.0430  0.1223  -0.0600 869  HIS B O   
2458 C CB  . HIS B 17  ? 0.2964 0.4391 0.3701 0.0499  0.1170  -0.0497 869  HIS B CB  
2459 C CG  . HIS B 17  ? 0.3975 0.5638 0.4665 0.0299  0.1301  -0.0553 869  HIS B CG  
2460 N ND1 . HIS B 17  ? 0.5865 0.7566 0.6465 0.0343  0.1472  -0.0669 869  HIS B ND1 
2461 C CD2 . HIS B 17  ? 0.4900 0.6746 0.5595 0.0040  0.1295  -0.0504 869  HIS B CD2 
2462 C CE1 . HIS B 17  ? 0.5928 0.7872 0.6475 0.0115  0.1564  -0.0668 869  HIS B CE1 
2463 N NE2 . HIS B 17  ? 0.5960 0.7961 0.6562 -0.0076 0.1460  -0.0559 869  HIS B NE2 
2464 N N   . PHE B 18  ? 0.2569 0.3040 0.2525 0.0093  0.1069  -0.0442 870  PHE B N   
2465 C CA  . PHE B 18  ? 0.2972 0.3204 0.2611 -0.0013 0.1105  -0.0477 870  PHE B CA  
2466 C C   . PHE B 18  ? 0.3171 0.3622 0.2730 -0.0162 0.1217  -0.0474 870  PHE B C   
2467 O O   . PHE B 18  ? 0.2972 0.3528 0.2576 -0.0298 0.1187  -0.0373 870  PHE B O   
2468 C CB  . PHE B 18  ? 0.2827 0.2801 0.2303 -0.0100 0.0953  -0.0387 870  PHE B CB  
2469 C CG  . PHE B 18  ? 0.2891 0.2642 0.2375 0.0001  0.0871  -0.0398 870  PHE B CG  
2470 C CD1 . PHE B 18  ? 0.2272 0.2081 0.1961 0.0093  0.0789  -0.0334 870  PHE B CD1 
2471 C CD2 . PHE B 18  ? 0.3460 0.2962 0.2725 -0.0025 0.0880  -0.0472 870  PHE B CD2 
2472 C CE1 . PHE B 18  ? 0.3181 0.2777 0.2851 0.0170  0.0729  -0.0316 870  PHE B CE1 
2473 C CE2 . PHE B 18  ? 0.3350 0.2622 0.2610 0.0024  0.0823  -0.0475 870  PHE B CE2 
2474 C CZ  . PHE B 18  ? 0.2751 0.2058 0.2211 0.0127  0.0752  -0.0381 870  PHE B CZ  
2475 N N   . GLU B 19  ? 0.3377 0.3883 0.2802 -0.0150 0.1359  -0.0590 871  GLU B N   
2476 C CA  . GLU B 19  ? 0.3789 0.4547 0.3108 -0.0301 0.1490  -0.0583 871  GLU B CA  
2477 C C   . GLU B 19  ? 0.3910 0.4466 0.2881 -0.0477 0.1424  -0.0465 871  GLU B C   
2478 O O   . GLU B 19  ? 0.3843 0.4167 0.2594 -0.0461 0.1355  -0.0497 871  GLU B O   
2479 C CB  . GLU B 19  ? 0.4198 0.5130 0.3490 -0.0206 0.1677  -0.0772 871  GLU B CB  
2480 C CG  . GLU B 19  ? 0.4517 0.5715 0.4190 0.0008  0.1745  -0.0858 871  GLU B CG  
2481 C CD  . GLU B 19  ? 0.5987 0.7326 0.5669 0.0168  0.1938  -0.1071 871  GLU B CD  
2482 O OE1 . GLU B 19  ? 0.6690 0.7996 0.6074 0.0067  0.2045  -0.1172 871  GLU B OE1 
2483 O OE2 . GLU B 19  ? 0.5887 0.7386 0.5876 0.0414  0.1982  -0.1140 871  GLU B OE2 
2484 N N   . LYS B 20  ? 0.3618 0.4267 0.2542 -0.0647 0.1443  -0.0319 872  LYS B N   
2485 C CA  . LYS B 20  ? 0.3750 0.4198 0.2348 -0.0779 0.1376  -0.0157 872  LYS B CA  
2486 C C   . LYS B 20  ? 0.3857 0.4344 0.2112 -0.0806 0.1438  -0.0220 872  LYS B C   
2487 O O   . LYS B 20  ? 0.3497 0.3816 0.1499 -0.0822 0.1324  -0.0144 872  LYS B O   
2488 C CB  . LYS B 20  ? 0.4001 0.4500 0.2578 -0.0970 0.1433  0.0014  872  LYS B CB  
2489 C CG  . LYS B 20  ? 0.5169 0.5371 0.3432 -0.1058 0.1342  0.0233  872  LYS B CG  
2490 C CD  . LYS B 20  ? 0.6344 0.6503 0.4561 -0.1267 0.1425  0.0412  872  LYS B CD  
2491 C CE  . LYS B 20  ? 0.7155 0.6955 0.5033 -0.1311 0.1338  0.0666  872  LYS B CE  
2492 N NZ  . LYS B 20  ? 0.8271 0.7981 0.6011 -0.1544 0.1460  0.0865  872  LYS B NZ  
2493 N N   . ARG B 21  ? 0.4056 0.4815 0.2311 -0.0807 0.1618  -0.0373 873  ARG B N   
2494 C CA  . ARG B 21  ? 0.4550 0.5404 0.2454 -0.0858 0.1705  -0.0472 873  ARG B CA  
2495 C C   . ARG B 21  ? 0.4434 0.5075 0.2196 -0.0775 0.1610  -0.0620 873  ARG B C   
2496 O O   . ARG B 21  ? 0.4809 0.5507 0.2228 -0.0858 0.1621  -0.0670 873  ARG B O   
2497 C CB  . ARG B 21  ? 0.4802 0.6014 0.2766 -0.0850 0.1938  -0.0655 873  ARG B CB  
2498 C CG  . ARG B 21  ? 0.4827 0.6062 0.3105 -0.0630 0.2006  -0.0893 873  ARG B CG  
2499 C CD  . ARG B 21  ? 0.5283 0.6918 0.3607 -0.0593 0.2252  -0.1087 873  ARG B CD  
2500 N NE  . ARG B 21  ? 0.5855 0.7572 0.4583 -0.0345 0.2310  -0.1238 873  ARG B NE  
2501 C CZ  . ARG B 21  ? 0.6982 0.8874 0.5794 -0.0169 0.2494  -0.1492 873  ARG B CZ  
2502 N NH1 . ARG B 21  ? 0.7869 0.9901 0.6380 -0.0235 0.2659  -0.1671 873  ARG B NH1 
2503 N NH2 . ARG B 21  ? 0.7398 0.9343 0.6599 0.0097  0.2515  -0.1573 873  ARG B NH2 
2504 N N   . PHE B 22  ? 0.3868 0.4295 0.1878 -0.0635 0.1525  -0.0692 874  PHE B N   
2505 C CA  . PHE B 22  ? 0.3935 0.4129 0.1834 -0.0595 0.1443  -0.0829 874  PHE B CA  
2506 C C   . PHE B 22  ? 0.4152 0.4162 0.2057 -0.0608 0.1232  -0.0674 874  PHE B C   
2507 O O   . PHE B 22  ? 0.4022 0.3880 0.1847 -0.0613 0.1155  -0.0768 874  PHE B O   
2508 C CB  . PHE B 22  ? 0.4111 0.4159 0.2242 -0.0427 0.1524  -0.1028 874  PHE B CB  
2509 C CG  . PHE B 22  ? 0.4287 0.4531 0.2460 -0.0353 0.1743  -0.1216 874  PHE B CG  
2510 C CD1 . PHE B 22  ? 0.4747 0.5163 0.2607 -0.0461 0.1871  -0.1355 874  PHE B CD1 
2511 C CD2 . PHE B 22  ? 0.4827 0.5123 0.3353 -0.0153 0.1823  -0.1267 874  PHE B CD2 
2512 C CE1 . PHE B 22  ? 0.5518 0.6147 0.3426 -0.0375 0.2091  -0.1559 874  PHE B CE1 
2513 C CE2 . PHE B 22  ? 0.5117 0.5643 0.3718 -0.0043 0.2032  -0.1453 874  PHE B CE2 
2514 C CZ  . PHE B 22  ? 0.5847 0.6535 0.4145 -0.0154 0.2175  -0.1610 874  PHE B CZ  
2515 N N   . LEU B 23  ? 0.4054 0.4080 0.2054 -0.0625 0.1149  -0.0452 875  LEU B N   
2516 C CA  . LEU B 23  ? 0.4076 0.3950 0.2124 -0.0601 0.0963  -0.0317 875  LEU B CA  
2517 C C   . LEU B 23  ? 0.4394 0.4329 0.2136 -0.0681 0.0878  -0.0173 875  LEU B C   
2518 O O   . LEU B 23  ? 0.4286 0.4247 0.1935 -0.0729 0.0894  0.0008  875  LEU B O   
2519 C CB  . LEU B 23  ? 0.3986 0.3809 0.2317 -0.0554 0.0928  -0.0196 875  LEU B CB  
2520 C CG  . LEU B 23  ? 0.3811 0.3490 0.2257 -0.0495 0.0762  -0.0108 875  LEU B CG  
2521 C CD1 . LEU B 23  ? 0.3136 0.2743 0.1673 -0.0425 0.0711  -0.0230 875  LEU B CD1 
2522 C CD2 . LEU B 23  ? 0.4231 0.3887 0.2921 -0.0482 0.0753  -0.0030 875  LEU B CD2 
2523 N N   . LYS B 24  ? 0.3893 0.3861 0.1469 -0.0702 0.0792  -0.0250 876  LYS B N   
2524 C CA  . LYS B 24  ? 0.4664 0.4796 0.1926 -0.0765 0.0709  -0.0146 876  LYS B CA  
2525 C C   . LYS B 24  ? 0.4257 0.4368 0.1581 -0.0690 0.0519  -0.0006 876  LYS B C   
2526 O O   . LYS B 24  ? 0.3582 0.3682 0.1027 -0.0676 0.0447  -0.0119 876  LYS B O   
2527 C CB  . LYS B 24  ? 0.4870 0.5158 0.1891 -0.0867 0.0751  -0.0371 876  LYS B CB  
2528 C CG  . LYS B 24  ? 0.6240 0.6548 0.3214 -0.0908 0.0961  -0.0567 876  LYS B CG  
2529 C CD  . LYS B 24  ? 0.6795 0.7254 0.3643 -0.0948 0.1066  -0.0411 876  LYS B CD  
2530 C CE  . LYS B 24  ? 0.7127 0.7712 0.3915 -0.0987 0.1286  -0.0628 876  LYS B CE  
2531 N NZ  . LYS B 24  ? 0.7726 0.8499 0.4407 -0.1057 0.1396  -0.0455 876  LYS B NZ  
2532 N N   . ARG B 25  ? 0.4089 0.4189 0.1322 -0.0642 0.0452  0.0242  877  ARG B N   
2533 C CA  . ARG B 25  ? 0.4154 0.4244 0.1443 -0.0523 0.0281  0.0393  877  ARG B CA  
2534 C C   . ARG B 25  ? 0.3886 0.4300 0.0992 -0.0531 0.0149  0.0370  877  ARG B C   
2535 O O   . ARG B 25  ? 0.3947 0.4579 0.0745 -0.0597 0.0146  0.0422  877  ARG B O   
2536 C CB  . ARG B 25  ? 0.4166 0.4087 0.1360 -0.0457 0.0266  0.0674  877  ARG B CB  
2537 C CG  . ARG B 25  ? 0.4702 0.4596 0.1946 -0.0282 0.0098  0.0830  877  ARG B CG  
2538 C CD  . ARG B 25  ? 0.5087 0.4689 0.2234 -0.0192 0.0090  0.1110  877  ARG B CD  
2539 N NE  . ARG B 25  ? 0.5522 0.5133 0.2722 0.0027  -0.0072 0.1231  877  ARG B NE  
2540 C CZ  . ARG B 25  ? 0.5951 0.5878 0.2975 0.0137  -0.0209 0.1347  877  ARG B CZ  
2541 N NH1 . ARG B 25  ? 0.5967 0.6225 0.2712 0.0026  -0.0214 0.1354  877  ARG B NH1 
2542 N NH2 . ARG B 25  ? 0.6460 0.6422 0.3592 0.0370  -0.0345 0.1443  877  ARG B NH2 
2543 N N   . ILE B 26  ? 0.3400 0.3904 0.0685 -0.0476 0.0036  0.0304  878  ILE B N   
2544 C CA  . ILE B 26  ? 0.3673 0.4578 0.0837 -0.0493 -0.0107 0.0280  878  ILE B CA  
2545 C C   . ILE B 26  ? 0.3792 0.4829 0.0990 -0.0289 -0.0265 0.0516  878  ILE B C   
2546 O O   . ILE B 26  ? 0.4493 0.5793 0.1456 -0.0240 -0.0356 0.0669  878  ILE B O   
2547 C CB  . ILE B 26  ? 0.3675 0.4690 0.0985 -0.0609 -0.0121 0.0034  878  ILE B CB  
2548 C CG1 . ILE B 26  ? 0.4158 0.4973 0.1417 -0.0774 0.0043  -0.0200 878  ILE B CG1 
2549 C CG2 . ILE B 26  ? 0.3805 0.5335 0.0987 -0.0675 -0.0269 -0.0004 878  ILE B CG2 
2550 C CD1 . ILE B 26  ? 0.5051 0.5806 0.2441 -0.0896 0.0062  -0.0420 878  ILE B CD1 
2551 N N   . ARG B 27  ? 0.3147 0.4024 0.0627 -0.0156 -0.0299 0.0539  879  ARG B N   
2552 C CA  . ARG B 27  ? 0.3579 0.4541 0.1124 0.0082  -0.0432 0.0735  879  ARG B CA  
2553 C C   . ARG B 27  ? 0.3127 0.3753 0.0949 0.0213  -0.0404 0.0740  879  ARG B C   
2554 O O   . ARG B 27  ? 0.2830 0.3269 0.0811 0.0108  -0.0310 0.0587  879  ARG B O   
2555 C CB  . ARG B 27  ? 0.4021 0.5545 0.1603 0.0107  -0.0581 0.0676  879  ARG B CB  
2556 C CG  . ARG B 27  ? 0.3899 0.5561 0.1701 -0.0038 -0.0560 0.0429  879  ARG B CG  
2557 C CD  . ARG B 27  ? 0.4631 0.6925 0.2468 -0.0070 -0.0698 0.0362  879  ARG B CD  
2558 N NE  . ARG B 27  ? 0.3876 0.6229 0.1899 -0.0254 -0.0652 0.0142  879  ARG B NE  
2559 C CZ  . ARG B 27  ? 0.4491 0.6909 0.2781 -0.0173 -0.0669 0.0117  879  ARG B CZ  
2560 N NH1 . ARG B 27  ? 0.3582 0.6035 0.2017 0.0114  -0.0734 0.0262  879  ARG B NH1 
2561 N NH2 . ARG B 27  ? 0.5546 0.7985 0.3945 -0.0384 -0.0611 -0.0059 879  ARG B NH2 
2562 N N   . ASP B 28  ? 0.3508 0.4071 0.1371 0.0453  -0.0487 0.0915  880  ASP B N   
2563 C CA  . ASP B 28  ? 0.3576 0.3851 0.1681 0.0590  -0.0468 0.0892  880  ASP B CA  
2564 C C   . ASP B 28  ? 0.3411 0.4040 0.1758 0.0606  -0.0522 0.0715  880  ASP B C   
2565 O O   . ASP B 28  ? 0.3531 0.4655 0.1878 0.0626  -0.0624 0.0694  880  ASP B O   
2566 C CB  . ASP B 28  ? 0.4249 0.4314 0.2315 0.0870  -0.0533 0.1113  880  ASP B CB  
2567 C CG  . ASP B 28  ? 0.4732 0.4351 0.2548 0.0845  -0.0465 0.1328  880  ASP B CG  
2568 O OD1 . ASP B 28  ? 0.4600 0.4073 0.2328 0.0610  -0.0347 0.1276  880  ASP B OD1 
2569 O OD2 . ASP B 28  ? 0.5686 0.5098 0.3399 0.1071  -0.0520 0.1556  880  ASP B OD2 
2570 N N   . LEU B 29  ? 0.3018 0.3432 0.1566 0.0589  -0.0455 0.0596  881  LEU B N   
2571 C CA  . LEU B 29  ? 0.3087 0.3810 0.1859 0.0618  -0.0492 0.0453  881  LEU B CA  
2572 C C   . LEU B 29  ? 0.2974 0.3591 0.1900 0.0872  -0.0519 0.0476  881  LEU B C   
2573 O O   . LEU B 29  ? 0.2986 0.3988 0.2057 0.1004  -0.0586 0.0426  881  LEU B O   
2574 C CB  . LEU B 29  ? 0.2558 0.3185 0.1418 0.0405  -0.0399 0.0295  881  LEU B CB  
2575 C CG  . LEU B 29  ? 0.2655 0.3401 0.1386 0.0176  -0.0367 0.0226  881  LEU B CG  
2576 C CD1 . LEU B 29  ? 0.2920 0.3458 0.1733 0.0025  -0.0265 0.0110  881  LEU B CD1 
2577 C CD2 . LEU B 29  ? 0.2246 0.3485 0.0971 0.0114  -0.0451 0.0170  881  LEU B CD2 
2578 N N   . GLY B 30  ? 0.3661 0.3763 0.2553 0.0933  -0.0456 0.0536  882  GLY B N   
2579 C CA  . GLY B 30  ? 0.3904 0.3791 0.2898 0.1181  -0.0467 0.0547  882  GLY B CA  
2580 C C   . GLY B 30  ? 0.4532 0.3807 0.3488 0.1124  -0.0367 0.0552  882  GLY B C   
2581 O O   . GLY B 30  ? 0.4224 0.3314 0.3091 0.0903  -0.0294 0.0564  882  GLY B O   
2582 N N   . GLU B 31  ? 0.5611 0.4595 0.4640 0.1323  -0.0357 0.0524  883  GLU B N   
2583 C CA  . GLU B 31  ? 0.6691 0.5055 0.5680 0.1265  -0.0262 0.0511  883  GLU B CA  
2584 C C   . GLU B 31  ? 0.7040 0.5303 0.6203 0.1355  -0.0229 0.0292  883  GLU B C   
2585 O O   . GLU B 31  ? 0.6720 0.5291 0.6008 0.1573  -0.0281 0.0211  883  GLU B O   
2586 C CB  . GLU B 31  ? 0.7334 0.5217 0.6129 0.1427  -0.0267 0.0751  883  GLU B CB  
2587 C CG  . GLU B 31  ? 0.8096 0.6149 0.6677 0.1396  -0.0318 0.0993  883  GLU B CG  
2588 C CD  . GLU B 31  ? 0.8812 0.6379 0.7168 0.1569  -0.0326 0.1276  883  GLU B CD  
2589 O OE1 . GLU B 31  ? 0.9862 0.6922 0.8242 0.1751  -0.0296 0.1284  883  GLU B OE1 
2590 O OE2 . GLU B 31  ? 0.9267 0.6941 0.7402 0.1525  -0.0359 0.1493  883  GLU B OE2 
2591 N N   . GLY B 32  ? 0.7485 0.5365 0.6655 0.1174  -0.0137 0.0183  884  GLY B N   
2592 C CA  . GLY B 32  ? 0.7710 0.5423 0.6998 0.1226  -0.0093 -0.0046 884  GLY B CA  
2593 C C   . GLY B 32  ? 0.7951 0.5212 0.7204 0.0976  0.0005  -0.0136 884  GLY B C   
2594 O O   . GLY B 32  ? 0.7322 0.4682 0.6559 0.0717  0.0035  -0.0102 884  GLY B O   
2595 N N   . HIS B 33  ? 0.8600 0.5373 0.7847 0.1055  0.0059  -0.0260 885  HIS B N   
2596 C CA  . HIS B 33  ? 0.8792 0.5192 0.8035 0.0789  0.0153  -0.0427 885  HIS B CA  
2597 C C   . HIS B 33  ? 0.8661 0.4864 0.7806 0.0489  0.0210  -0.0274 885  HIS B C   
2598 O O   . HIS B 33  ? 0.8480 0.4956 0.7709 0.0220  0.0237  -0.0380 885  HIS B O   
2599 C CB  . HIS B 33  ? 0.8492 0.5377 0.7894 0.0666  0.0146  -0.0706 885  HIS B CB  
2600 C CG  . HIS B 33  ? 0.8501 0.5593 0.7987 0.0934  0.0117  -0.0879 885  HIS B CG  
2601 N ND1 . HIS B 33  ? 0.9076 0.5711 0.8543 0.1092  0.0172  -0.1054 885  HIS B ND1 
2602 C CD2 . HIS B 33  ? 0.8066 0.5782 0.7654 0.1064  0.0053  -0.0911 885  HIS B CD2 
2603 C CE1 . HIS B 33  ? 0.8941 0.5967 0.8509 0.1328  0.0143  -0.1196 885  HIS B CE1 
2604 N NE2 . HIS B 33  ? 0.8325 0.6026 0.7967 0.1299  0.0071  -0.1104 885  HIS B NE2 
2605 N N   . PHE B 34  ? 0.8875 0.4659 0.7842 0.0555  0.0226  -0.0011 886  PHE B N   
2606 C CA  . PHE B 34  ? 0.8773 0.4372 0.7611 0.0286  0.0295  0.0172  886  PHE B CA  
2607 C C   . PHE B 34  ? 0.7806 0.4025 0.6682 0.0162  0.0264  0.0248  886  PHE B C   
2608 O O   . PHE B 34  ? 0.7793 0.3980 0.6593 -0.0069 0.0334  0.0357  886  PHE B O   
2609 C CB  . PHE B 34  ? 0.9232 0.4463 0.8091 -0.0038 0.0410  0.0011  886  PHE B CB  
2610 C CG  . PHE B 34  ? 0.9956 0.4482 0.8753 0.0051  0.0462  -0.0101 886  PHE B CG  
2611 C CD1 . PHE B 34  ? 1.0752 0.4514 0.9328 0.0115  0.0521  0.0125  886  PHE B CD1 
2612 C CD2 . PHE B 34  ? 0.9925 0.4533 0.8866 0.0077  0.0458  -0.0434 886  PHE B CD2 
2613 C CE1 . PHE B 34  ? 1.1501 0.4516 1.0012 0.0218  0.0582  0.0011  886  PHE B CE1 
2614 C CE2 . PHE B 34  ? 1.0640 0.4564 0.9517 0.0167  0.0521  -0.0583 886  PHE B CE2 
2615 C CZ  . PHE B 34  ? 1.1447 0.4537 1.0115 0.0244  0.0587  -0.0365 886  PHE B CZ  
2616 N N   . GLY B 35  ? 0.6935 0.3694 0.5921 0.0313  0.0173  0.0185  887  GLY B N   
2617 C CA  . GLY B 35  ? 0.6046 0.3323 0.5057 0.0232  0.0144  0.0236  887  GLY B CA  
2618 C C   . GLY B 35  ? 0.5791 0.3240 0.4686 0.0438  0.0061  0.0412  887  GLY B C   
2619 O O   . GLY B 35  ? 0.5483 0.2829 0.4356 0.0691  -0.0001 0.0457  887  GLY B O   
2620 N N   . LYS B 36  ? 0.4755 0.2489 0.3577 0.0336  0.0062  0.0501  888  LYS B N   
2621 C CA  . LYS B 36  ? 0.4620 0.2691 0.3364 0.0475  -0.0028 0.0596  888  LYS B CA  
2622 C C   . LYS B 36  ? 0.3591 0.2098 0.2405 0.0338  -0.0025 0.0492  888  LYS B C   
2623 O O   . LYS B 36  ? 0.3465 0.1966 0.2307 0.0155  0.0057  0.0444  888  LYS B O   
2624 C CB  . LYS B 36  ? 0.5215 0.3098 0.3699 0.0524  -0.0036 0.0853  888  LYS B CB  
2625 C CG  . LYS B 36  ? 0.6051 0.3926 0.4381 0.0292  0.0056  0.0940  888  LYS B CG  
2626 C CD  . LYS B 36  ? 0.6790 0.4585 0.4823 0.0359  0.0029  0.1210  888  LYS B CD  
2627 C CE  . LYS B 36  ? 0.6936 0.5217 0.4908 0.0499  -0.0098 0.1235  888  LYS B CE  
2628 N NZ  . LYS B 36  ? 0.7019 0.5371 0.4676 0.0506  -0.0122 0.1473  888  LYS B NZ  
2629 N N   . VAL B 37  ? 0.3026 0.1904 0.1874 0.0429  -0.0109 0.0456  889  VAL B N   
2630 C CA  . VAL B 37  ? 0.2606 0.1812 0.1494 0.0301  -0.0101 0.0361  889  VAL B CA  
2631 C C   . VAL B 37  ? 0.2802 0.2225 0.1509 0.0295  -0.0146 0.0449  889  VAL B C   
2632 O O   . VAL B 37  ? 0.3063 0.2631 0.1712 0.0442  -0.0238 0.0533  889  VAL B O   
2633 C CB  . VAL B 37  ? 0.2429 0.1897 0.1494 0.0337  -0.0144 0.0222  889  VAL B CB  
2634 C CG1 . VAL B 37  ? 0.2827 0.2526 0.1902 0.0196  -0.0125 0.0150  889  VAL B CG1 
2635 C CG2 . VAL B 37  ? 0.2647 0.1955 0.1859 0.0334  -0.0106 0.0121  889  VAL B CG2 
2636 N N   . GLU B 38  ? 0.2598 0.2073 0.1221 0.0134  -0.0079 0.0416  890  GLU B N   
2637 C CA  . GLU B 38  ? 0.2684 0.2351 0.1093 0.0083  -0.0100 0.0466  890  GLU B CA  
2638 C C   . GLU B 38  ? 0.3105 0.2971 0.1542 -0.0054 -0.0070 0.0300  890  GLU B C   
2639 O O   . GLU B 38  ? 0.2925 0.2677 0.1489 -0.0124 0.0010  0.0199  890  GLU B O   
2640 C CB  . GLU B 38  ? 0.2895 0.2368 0.1119 0.0001  -0.0010 0.0572  890  GLU B CB  
2641 C CG  . GLU B 38  ? 0.3422 0.2627 0.1546 0.0106  -0.0028 0.0774  890  GLU B CG  
2642 C CD  . GLU B 38  ? 0.4488 0.3498 0.2430 -0.0025 0.0086  0.0887  890  GLU B CD  
2643 O OE1 . GLU B 38  ? 0.4810 0.3768 0.2847 -0.0170 0.0203  0.0784  890  GLU B OE1 
2644 O OE2 . GLU B 38  ? 0.4803 0.3738 0.2507 0.0024  0.0059  0.1095  890  GLU B OE2 
2645 N N   . LEU B 39  ? 0.2762 0.2916 0.1069 -0.0095 -0.0135 0.0276  891  LEU B N   
2646 C CA  . LEU B 39  ? 0.2794 0.3056 0.1053 -0.0261 -0.0089 0.0113  891  LEU B CA  
2647 C C   . LEU B 39  ? 0.2911 0.3065 0.0977 -0.0355 0.0016  0.0097  891  LEU B C   
2648 O O   . LEU B 39  ? 0.2993 0.3224 0.0853 -0.0341 -0.0004 0.0211  891  LEU B O   
2649 C CB  . LEU B 39  ? 0.3232 0.3880 0.1423 -0.0316 -0.0193 0.0060  891  LEU B CB  
2650 C CG  . LEU B 39  ? 0.2934 0.3640 0.1045 -0.0531 -0.0140 -0.0134 891  LEU B CG  
2651 C CD1 . LEU B 39  ? 0.3339 0.3788 0.1627 -0.0585 -0.0057 -0.0235 891  LEU B CD1 
2652 C CD2 . LEU B 39  ? 0.3480 0.4636 0.1531 -0.0617 -0.0253 -0.0185 891  LEU B CD2 
2653 N N   . CYS B 40  ? 0.2949 0.2941 0.1079 -0.0434 0.0131  -0.0035 892  CYS B N   
2654 C CA  . CYS B 40  ? 0.3126 0.3055 0.1105 -0.0514 0.0256  -0.0100 892  CYS B CA  
2655 C C   . CYS B 40  ? 0.3345 0.3230 0.1303 -0.0617 0.0327  -0.0313 892  CYS B C   
2656 O O   . CYS B 40  ? 0.3439 0.3269 0.1528 -0.0631 0.0293  -0.0376 892  CYS B O   
2657 C CB  . CYS B 40  ? 0.3039 0.2782 0.1162 -0.0465 0.0357  -0.0050 892  CYS B CB  
2658 S SG  . CYS B 40  ? 0.3594 0.3262 0.1694 -0.0391 0.0306  0.0192  892  CYS B SG  
2659 N N   A ARG B 41  ? 0.3565 0.3452 0.1339 -0.0695 0.0436  -0.0425 893  ARG B N   
2660 N N   B ARG B 41  ? 0.3512 0.3403 0.1281 -0.0698 0.0433  -0.0426 893  ARG B N   
2661 C CA  A ARG B 41  ? 0.3731 0.3454 0.1487 -0.0764 0.0549  -0.0649 893  ARG B CA  
2662 C CA  B ARG B 41  ? 0.3599 0.3319 0.1361 -0.0762 0.0548  -0.0647 893  ARG B CA  
2663 C C   A ARG B 41  ? 0.3790 0.3388 0.1635 -0.0683 0.0704  -0.0680 893  ARG B C   
2664 C C   B ARG B 41  ? 0.3712 0.3310 0.1563 -0.0680 0.0702  -0.0673 893  ARG B C   
2665 O O   A ARG B 41  ? 0.4002 0.3737 0.1732 -0.0691 0.0763  -0.0623 893  ARG B O   
2666 O O   B ARG B 41  ? 0.3933 0.3667 0.1680 -0.0684 0.0756  -0.0607 893  ARG B O   
2667 C CB  A ARG B 41  ? 0.4132 0.4002 0.1588 -0.0926 0.0564  -0.0817 893  ARG B CB  
2668 C CB  B ARG B 41  ? 0.3967 0.3812 0.1438 -0.0926 0.0569  -0.0829 893  ARG B CB  
2669 C CG  A ARG B 41  ? 0.5141 0.4747 0.2562 -0.1015 0.0681  -0.1082 893  ARG B CG  
2670 C CG  B ARG B 41  ? 0.4677 0.4226 0.2141 -0.0991 0.0697  -0.1082 893  ARG B CG  
2671 C CD  A ARG B 41  ? 0.5292 0.5055 0.2401 -0.1221 0.0685  -0.1292 893  ARG B CD  
2672 C CD  B ARG B 41  ? 0.4575 0.4212 0.1752 -0.1201 0.0711  -0.1313 893  ARG B CD  
2673 N NE  A ARG B 41  ? 0.5457 0.5551 0.2508 -0.1329 0.0505  -0.1220 893  ARG B NE  
2674 N NE  B ARG B 41  ? 0.4708 0.4539 0.1870 -0.1336 0.0557  -0.1294 893  ARG B NE  
2675 C CZ  A ARG B 41  ? 0.5892 0.5956 0.3054 -0.1422 0.0430  -0.1254 893  ARG B CZ  
2676 C CZ  B ARG B 41  ? 0.5435 0.5713 0.2432 -0.1425 0.0422  -0.1242 893  ARG B CZ  
2677 N NH1 A ARG B 41  ? 0.5533 0.5180 0.2837 -0.1434 0.0516  -0.1343 893  ARG B NH1 
2678 N NH1 B ARG B 41  ? 0.5444 0.5992 0.2229 -0.1402 0.0416  -0.1178 893  ARG B NH1 
2679 N NH2 A ARG B 41  ? 0.6174 0.6661 0.3303 -0.1500 0.0268  -0.1186 893  ARG B NH2 
2680 N NH2 B ARG B 41  ? 0.6013 0.6514 0.3058 -0.1537 0.0292  -0.1241 893  ARG B NH2 
2681 N N   . TYR B 42  ? 0.3634 0.3007 0.1679 -0.0603 0.0773  -0.0755 894  TYR B N   
2682 C CA  . TYR B 42  ? 0.3624 0.2949 0.1786 -0.0501 0.0922  -0.0812 894  TYR B CA  
2683 C C   . TYR B 42  ? 0.4012 0.3202 0.2006 -0.0542 0.1058  -0.1059 894  TYR B C   
2684 O O   . TYR B 42  ? 0.3801 0.2702 0.1819 -0.0532 0.1081  -0.1177 894  TYR B O   
2685 C CB  . TYR B 42  ? 0.3490 0.2696 0.1958 -0.0355 0.0916  -0.0746 894  TYR B CB  
2686 C CG  . TYR B 42  ? 0.3585 0.2887 0.2213 -0.0236 0.1053  -0.0779 894  TYR B CG  
2687 C CD1 . TYR B 42  ? 0.3702 0.3267 0.2346 -0.0272 0.1089  -0.0694 894  TYR B CD1 
2688 C CD2 . TYR B 42  ? 0.3721 0.2865 0.2488 -0.0086 0.1153  -0.0887 894  TYR B CD2 
2689 C CE1 . TYR B 42  ? 0.3118 0.2866 0.1932 -0.0191 0.1219  -0.0731 894  TYR B CE1 
2690 C CE2 . TYR B 42  ? 0.3482 0.2819 0.2432 0.0049  0.1277  -0.0921 894  TYR B CE2 
2691 C CZ  . TYR B 42  ? 0.3187 0.2869 0.2167 -0.0021 0.1311  -0.0852 894  TYR B CZ  
2692 O OH  . TYR B 42  ? 0.3455 0.3425 0.2637 0.0076  0.1437  -0.0889 894  TYR B OH  
2693 N N   . ASP B 43  ? 0.3959 0.3334 0.1763 -0.0595 0.1159  -0.1141 895  ASP B N   
2694 C CA  . ASP B 43  ? 0.3907 0.3205 0.1475 -0.0673 0.1280  -0.1409 895  ASP B CA  
2695 C C   . ASP B 43  ? 0.4474 0.3847 0.2067 -0.0570 0.1489  -0.1551 895  ASP B C   
2696 O O   . ASP B 43  ? 0.4330 0.3946 0.1676 -0.0665 0.1575  -0.1642 895  ASP B O   
2697 C CB  . ASP B 43  ? 0.4538 0.4090 0.1768 -0.0871 0.1194  -0.1415 895  ASP B CB  
2698 C CG  . ASP B 43  ? 0.4803 0.4273 0.1753 -0.1018 0.1274  -0.1729 895  ASP B CG  
2699 O OD1 . ASP B 43  ? 0.5387 0.4498 0.2388 -0.1036 0.1303  -0.1896 895  ASP B OD1 
2700 O OD2 . ASP B 43  ? 0.5554 0.5313 0.2204 -0.1138 0.1307  -0.1809 895  ASP B OD2 
2701 N N   . PRO B 44  ? 0.4280 0.3487 0.2165 -0.0366 0.1575  -0.1578 896  PRO B N   
2702 C CA  . PRO B 44  ? 0.4881 0.4216 0.2845 -0.0227 0.1781  -0.1730 896  PRO B CA  
2703 C C   . PRO B 44  ? 0.5196 0.4453 0.2870 -0.0287 0.1944  -0.2053 896  PRO B C   
2704 O O   . PRO B 44  ? 0.5680 0.5232 0.3303 -0.0258 0.2105  -0.2162 896  PRO B O   
2705 C CB  . PRO B 44  ? 0.4807 0.3917 0.3120 0.0028  0.1807  -0.1708 896  PRO B CB  
2706 C CG  . PRO B 44  ? 0.4177 0.2981 0.2527 -0.0011 0.1633  -0.1575 896  PRO B CG  
2707 C CD  . PRO B 44  ? 0.3849 0.2794 0.1998 -0.0243 0.1483  -0.1461 896  PRO B CD  
2708 N N   . GLU B 45  ? 0.5553 0.4444 0.3032 -0.0393 0.1911  -0.2219 897  GLU B N   
2709 C CA  . GLU B 45  ? 0.6350 0.5114 0.3530 -0.0479 0.2068  -0.2578 897  GLU B CA  
2710 C C   . GLU B 45  ? 0.6338 0.5488 0.3128 -0.0746 0.2029  -0.2630 897  GLU B C   
2711 O O   . GLU B 45  ? 0.6472 0.5634 0.2981 -0.0841 0.2163  -0.2939 897  GLU B O   
2712 C CB  . GLU B 45  ? 0.6736 0.4896 0.3862 -0.0513 0.2070  -0.2762 897  GLU B CB  
2713 C CG  . GLU B 45  ? 0.6959 0.4695 0.4424 -0.0233 0.2104  -0.2678 897  GLU B CG  
2714 C CD  . GLU B 45  ? 0.6815 0.3859 0.4180 -0.0268 0.2154  -0.2871 897  GLU B CD  
2715 O OE1 . GLU B 45  ? 0.8343 0.5183 0.5670 -0.0442 0.2007  -0.2757 897  GLU B OE1 
2716 O OE2 . GLU B 45  ? 0.7898 0.4587 0.5224 -0.0122 0.2350  -0.3137 897  GLU B OE2 
2717 N N   . GLY B 46  ? 0.6164 0.5625 0.2927 -0.0853 0.1845  -0.2333 898  GLY B N   
2718 C CA  . GLY B 46  ? 0.6208 0.6097 0.2611 -0.1056 0.1796  -0.2302 898  GLY B CA  
2719 C C   . GLY B 46  ? 0.6753 0.6651 0.2817 -0.1292 0.1713  -0.2496 898  GLY B C   
2720 O O   . GLY B 46  ? 0.7026 0.7312 0.2747 -0.1449 0.1703  -0.2535 898  GLY B O   
2721 N N   . ASP B 47  ? 0.6759 0.6273 0.2907 -0.1339 0.1649  -0.2602 899  ASP B N   
2722 C CA  . ASP B 47  ? 0.6737 0.6254 0.2594 -0.1604 0.1586  -0.2837 899  ASP B CA  
2723 C C   . ASP B 47  ? 0.6701 0.6251 0.2650 -0.1716 0.1355  -0.2651 899  ASP B C   
2724 O O   . ASP B 47  ? 0.7130 0.6591 0.2939 -0.1941 0.1312  -0.2857 899  ASP B O   
2725 C CB  . ASP B 47  ? 0.7328 0.6323 0.3126 -0.1630 0.1779  -0.3242 899  ASP B CB  
2726 C CG  . ASP B 47  ? 0.7121 0.5517 0.3255 -0.1467 0.1799  -0.3181 899  ASP B CG  
2727 O OD1 . ASP B 47  ? 0.6779 0.5209 0.3212 -0.1302 0.1696  -0.2850 899  ASP B OD1 
2728 O OD2 . ASP B 47  ? 0.8422 0.6290 0.4494 -0.1513 0.1923  -0.3469 899  ASP B OD2 
2729 N N   . ASN B 48  ? 0.6493 0.6184 0.2681 -0.1573 0.1220  -0.2284 900  ASN B N   
2730 C CA  . ASN B 48  ? 0.6242 0.6032 0.2559 -0.1626 0.1010  -0.2084 900  ASN B CA  
2731 C C   . ASN B 48  ? 0.6526 0.5871 0.3024 -0.1675 0.1010  -0.2177 900  ASN B C   
2732 O O   . ASN B 48  ? 0.6531 0.6015 0.3062 -0.1809 0.0861  -0.2116 900  ASN B O   
2733 C CB  . ASN B 48  ? 0.6857 0.7176 0.2891 -0.1824 0.0855  -0.2080 900  ASN B CB  
2734 C CG  . ASN B 48  ? 0.7014 0.7749 0.2872 -0.1750 0.0828  -0.1881 900  ASN B CG  
2735 O OD1 . ASN B 48  ? 0.9295 1.0319 0.4815 -0.1878 0.0872  -0.2028 900  ASN B OD1 
2736 N ND2 . ASN B 48  ? 0.8141 0.8889 0.4206 -0.1556 0.0762  -0.1546 900  ASN B ND2 
2737 N N   . THR B 49  ? 0.6429 0.5267 0.3051 -0.1551 0.1179  -0.2300 901  THR B N   
2738 C CA  . THR B 49  ? 0.6295 0.4616 0.3069 -0.1569 0.1203  -0.2347 901  THR B CA  
2739 C C   . THR B 49  ? 0.6034 0.4197 0.3154 -0.1319 0.1168  -0.2063 901  THR B C   
2740 O O   . THR B 49  ? 0.6165 0.3967 0.3412 -0.1323 0.1159  -0.2020 901  THR B O   
2741 C CB  . THR B 49  ? 0.6548 0.4312 0.3203 -0.1583 0.1419  -0.2681 901  THR B CB  
2742 O OG1 . THR B 49  ? 0.6305 0.3947 0.3102 -0.1284 0.1564  -0.2664 901  THR B OG1 
2743 C CG2 . THR B 49  ? 0.7472 0.5383 0.3756 -0.1855 0.1472  -0.3022 901  THR B CG2 
2744 N N   . GLY B 50  ? 0.5476 0.3920 0.2732 -0.1125 0.1148  -0.1867 902  GLY B N   
2745 C CA  . GLY B 50  ? 0.5013 0.3391 0.2589 -0.0909 0.1106  -0.1619 902  GLY B CA  
2746 C C   . GLY B 50  ? 0.4866 0.3359 0.2563 -0.0962 0.0929  -0.1414 902  GLY B C   
2747 O O   . GLY B 50  ? 0.5061 0.3773 0.2625 -0.1147 0.0823  -0.1431 902  GLY B O   
2748 N N   . GLU B 51  ? 0.4698 0.3106 0.2656 -0.0790 0.0898  -0.1229 903  GLU B N   
2749 C CA  . GLU B 51  ? 0.4667 0.3169 0.2749 -0.0821 0.0756  -0.1058 903  GLU B CA  
2750 C C   . GLU B 51  ? 0.4494 0.3422 0.2607 -0.0802 0.0625  -0.0898 903  GLU B C   
2751 O O   . GLU B 51  ? 0.4104 0.3172 0.2239 -0.0701 0.0650  -0.0833 903  GLU B O   
2752 C CB  . GLU B 51  ? 0.4983 0.3259 0.3298 -0.0648 0.0772  -0.0928 903  GLU B CB  
2753 C CG  . GLU B 51  ? 0.5708 0.4207 0.4227 -0.0458 0.0746  -0.0774 903  GLU B CG  
2754 C CD  . GLU B 51  ? 0.6702 0.5026 0.5429 -0.0271 0.0784  -0.0691 903  GLU B CD  
2755 O OE1 . GLU B 51  ? 0.4616 0.2734 0.3363 -0.0291 0.0752  -0.0630 903  GLU B OE1 
2756 O OE2 . GLU B 51  ? 0.6594 0.5030 0.5456 -0.0114 0.0845  -0.0676 903  GLU B OE2 
2757 N N   . GLN B 52  ? 0.4191 0.3313 0.2308 -0.0899 0.0497  -0.0835 904  GLN B N   
2758 C CA  . GLN B 52  ? 0.3748 0.3212 0.1923 -0.0834 0.0369  -0.0672 904  GLN B CA  
2759 C C   . GLN B 52  ? 0.3506 0.2900 0.1928 -0.0676 0.0346  -0.0527 904  GLN B C   
2760 O O   . GLN B 52  ? 0.3400 0.2621 0.1927 -0.0674 0.0365  -0.0525 904  GLN B O   
2761 C CB  . GLN B 52  ? 0.3816 0.3580 0.1937 -0.0966 0.0246  -0.0678 904  GLN B CB  
2762 C CG  . GLN B 52  ? 0.4344 0.4324 0.2213 -0.1134 0.0231  -0.0812 904  GLN B CG  
2763 C CD  . GLN B 52  ? 0.4785 0.5200 0.2647 -0.1242 0.0089  -0.0799 904  GLN B CD  
2764 O OE1 . GLN B 52  ? 0.5840 0.6280 0.3819 -0.1334 0.0064  -0.0819 904  GLN B OE1 
2765 N NE2 . GLN B 52  ? 0.4677 0.5480 0.2401 -0.1227 -0.0005 -0.0751 904  GLN B NE2 
2766 N N   . VAL B 53  ? 0.3080 0.2594 0.1570 -0.0560 0.0311  -0.0406 905  VAL B N   
2767 C CA  . VAL B 53  ? 0.2789 0.2278 0.1496 -0.0435 0.0286  -0.0300 905  VAL B CA  
2768 C C   . VAL B 53  ? 0.2225 0.1887 0.0957 -0.0371 0.0189  -0.0184 905  VAL B C   
2769 O O   . VAL B 53  ? 0.2892 0.2657 0.1478 -0.0384 0.0158  -0.0148 905  VAL B O   
2770 C CB  . VAL B 53  ? 0.2662 0.2027 0.1469 -0.0352 0.0390  -0.0301 905  VAL B CB  
2771 C CG1 . VAL B 53  ? 0.3079 0.2243 0.1900 -0.0343 0.0483  -0.0395 905  VAL B CG1 
2772 C CG2 . VAL B 53  ? 0.3028 0.2452 0.1713 -0.0369 0.0452  -0.0299 905  VAL B CG2 
2773 N N   . ALA B 54  ? 0.2122 0.1801 0.1026 -0.0290 0.0143  -0.0128 906  ALA B N   
2774 C CA  . ALA B 54  ? 0.2058 0.1808 0.1001 -0.0203 0.0071  -0.0043 906  ALA B CA  
2775 C C   . ALA B 54  ? 0.2443 0.2048 0.1464 -0.0169 0.0131  -0.0008 906  ALA B C   
2776 O O   . ALA B 54  ? 0.2430 0.2009 0.1592 -0.0165 0.0171  -0.0044 906  ALA B O   
2777 C CB  . ALA B 54  ? 0.2001 0.1886 0.1075 -0.0153 -0.0002 -0.0048 906  ALA B CB  
2778 N N   . VAL B 55  ? 0.2174 0.1709 0.1103 -0.0151 0.0130  0.0074  907  VAL B N   
2779 C CA  . VAL B 55  ? 0.2178 0.1574 0.1144 -0.0180 0.0205  0.0112  907  VAL B CA  
2780 C C   . VAL B 55  ? 0.2334 0.1585 0.1322 -0.0122 0.0159  0.0184  907  VAL B C   
2781 O O   . VAL B 55  ? 0.2408 0.1601 0.1260 -0.0055 0.0105  0.0281  907  VAL B O   
2782 C CB  . VAL B 55  ? 0.2545 0.1923 0.1331 -0.0257 0.0289  0.0154  907  VAL B CB  
2783 C CG1 . VAL B 55  ? 0.2557 0.1856 0.1407 -0.0331 0.0391  0.0182  907  VAL B CG1 
2784 C CG2 . VAL B 55  ? 0.2475 0.1955 0.1220 -0.0297 0.0341  0.0043  907  VAL B CG2 
2785 N N   . LYS B 56  ? 0.2616 0.1808 0.1769 -0.0141 0.0179  0.0131  908  LYS B N   
2786 C CA  . LYS B 56  ? 0.2410 0.1384 0.1581 -0.0111 0.0160  0.0156  908  LYS B CA  
2787 C C   . LYS B 56  ? 0.2598 0.1388 0.1743 -0.0247 0.0256  0.0201  908  LYS B C   
2788 O O   . LYS B 56  ? 0.2806 0.1743 0.2066 -0.0356 0.0324  0.0137  908  LYS B O   
2789 C CB  . LYS B 56  ? 0.2477 0.1529 0.1825 -0.0074 0.0118  0.0032  908  LYS B CB  
2790 C CG  . LYS B 56  ? 0.3142 0.1937 0.2485 -0.0012 0.0098  0.0017  908  LYS B CG  
2791 C CD  . LYS B 56  ? 0.3013 0.1965 0.2497 0.0042  0.0052  -0.0132 908  LYS B CD  
2792 C CE  . LYS B 56  ? 0.4080 0.2759 0.3557 0.0118  0.0047  -0.0192 908  LYS B CE  
2793 N NZ  . LYS B 56  ? 0.2809 0.1714 0.2398 0.0180  0.0008  -0.0357 908  LYS B NZ  
2794 N N   A SER B 57  ? 0.3446 0.1925 0.2444 -0.0238 0.0265  0.0322  909  SER B N   
2795 N N   B SER B 57  ? 0.3465 0.1948 0.2456 -0.0238 0.0266  0.0326  909  SER B N   
2796 C CA  A SER B 57  ? 0.3339 0.1592 0.2274 -0.0405 0.0370  0.0394  909  SER B CA  
2797 C CA  B SER B 57  ? 0.3380 0.1627 0.2307 -0.0403 0.0369  0.0400  909  SER B CA  
2798 C C   A SER B 57  ? 0.4317 0.2115 0.3191 -0.0380 0.0363  0.0448  909  SER B C   
2799 C C   B SER B 57  ? 0.4308 0.2121 0.3206 -0.0382 0.0361  0.0427  909  SER B C   
2800 O O   A SER B 57  ? 0.4289 0.1956 0.3121 -0.0181 0.0276  0.0476  909  SER B O   
2801 O O   B SER B 57  ? 0.4201 0.1913 0.3103 -0.0194 0.0275  0.0409  909  SER B O   
2802 C CB  A SER B 57  ? 0.3827 0.2106 0.2538 -0.0451 0.0422  0.0550  909  SER B CB  
2803 C CB  B SER B 57  ? 0.3953 0.2165 0.2633 -0.0436 0.0414  0.0578  909  SER B CB  
2804 O OG  A SER B 57  ? 0.4055 0.2197 0.2563 -0.0295 0.0340  0.0700  909  SER B OG  
2805 O OG  B SER B 57  ? 0.3492 0.2059 0.2164 -0.0442 0.0428  0.0523  909  SER B OG  
2806 N N   . LEU B 58  ? 0.4551 0.2108 0.3424 -0.0583 0.0463  0.0456  910  LEU B N   
2807 C CA  . LEU B 58  ? 0.5359 0.2357 0.4139 -0.0592 0.0484  0.0510  910  LEU B CA  
2808 C C   . LEU B 58  ? 0.6332 0.2990 0.4828 -0.0469 0.0473  0.0782  910  LEU B C   
2809 O O   . LEU B 58  ? 0.6412 0.3224 0.4752 -0.0528 0.0509  0.0936  910  LEU B O   
2810 C CB  . LEU B 58  ? 0.5689 0.2512 0.4515 -0.0905 0.0610  0.0461  910  LEU B CB  
2811 C CG  . LEU B 58  ? 0.5738 0.2859 0.4835 -0.1058 0.0620  0.0199  910  LEU B CG  
2812 C CD1 . LEU B 58  ? 0.6118 0.3023 0.5217 -0.1398 0.0750  0.0182  910  LEU B CD1 
2813 C CD2 . LEU B 58  ? 0.6090 0.3108 0.5280 -0.0906 0.0532  0.0019  910  LEU B CD2 
2814 N N   . LYS B 59  ? 0.7232 0.3451 0.5656 -0.0279 0.0424  0.0837  911  LYS B N   
2815 C CA  . LYS B 59  ? 0.8372 0.4155 0.6517 -0.0159 0.0423  0.1129  911  LYS B CA  
2816 C C   . LYS B 59  ? 0.9095 0.4313 0.7115 -0.0429 0.0566  0.1221  911  LYS B C   
2817 O O   . LYS B 59  ? 0.9249 0.4114 0.7380 -0.0526 0.0615  0.1053  911  LYS B O   
2818 C CB  . LYS B 59  ? 0.8705 0.4222 0.6845 0.0187  0.0322  0.1149  911  LYS B CB  
2819 C CG  . LYS B 59  ? 0.8607 0.4716 0.6884 0.0422  0.0189  0.1052  911  LYS B CG  
2820 C CD  . LYS B 59  ? 0.9323 0.5257 0.7603 0.0789  0.0096  0.1095  911  LYS B CD  
2821 C CE  . LYS B 59  ? 0.9480 0.5258 0.7501 0.0991  0.0038  0.1434  911  LYS B CE  
2822 N NZ  . LYS B 59  ? 0.9849 0.5598 0.7917 0.1400  -0.0067 0.1476  911  LYS B NZ  
2823 N N   . PRO B 60  ? 0.9832 0.4993 0.7618 -0.0586 0.0644  0.1467  912  PRO B N   
2824 C CA  . PRO B 60  ? 1.0667 0.5232 0.8291 -0.0857 0.0791  0.1605  912  PRO B CA  
2825 C C   . PRO B 60  ? 1.1568 0.5315 0.8975 -0.0657 0.0775  0.1815  912  PRO B C   
2826 O O   . PRO B 60  ? 1.1778 0.5145 0.9311 -0.0551 0.0756  0.1641  912  PRO B O   
2827 C CB  . PRO B 60  ? 1.0813 0.5651 0.8223 -0.1037 0.0870  0.1827  912  PRO B CB  
2828 C CG  . PRO B 60  ? 1.0274 0.5587 0.7614 -0.0755 0.0736  0.1899  912  PRO B CG  
2829 C CD  . PRO B 60  ? 0.9548 0.5194 0.7189 -0.0553 0.0615  0.1614  912  PRO B CD  
2830 N N   . GLY B 64  ? 1.3841 0.6361 1.1954 -0.2217 0.1257  0.0541  916  GLY B N   
2831 C CA  . GLY B 64  ? 1.3316 0.6127 1.1674 -0.2080 0.1160  0.0170  916  GLY B CA  
2832 C C   . GLY B 64  ? 1.2474 0.6231 1.1137 -0.2303 0.1134  -0.0080 916  GLY B C   
2833 O O   . GLY B 64  ? 1.2092 0.6463 1.0821 -0.2364 0.1136  0.0045  916  GLY B O   
2834 N N   . ASN B 65  ? 1.2271 0.6164 1.1115 -0.2393 0.1105  -0.0438 917  ASN B N   
2835 C CA  . ASN B 65  ? 1.1432 0.6212 1.0566 -0.2613 0.1073  -0.0685 917  ASN B CA  
2836 C C   . ASN B 65  ? 1.0074 0.5639 0.9383 -0.2285 0.0921  -0.0729 917  ASN B C   
2837 O O   . ASN B 65  ? 0.9663 0.5925 0.9203 -0.2394 0.0872  -0.0933 917  ASN B O   
2838 C CB  . ASN B 65  ? 1.1922 0.6540 1.1141 -0.2902 0.1108  -0.1057 917  ASN B CB  
2839 C CG  . ASN B 65  ? 1.2136 0.6663 1.1375 -0.2596 0.1006  -0.1296 917  ASN B CG  
2840 O OD1 . ASN B 65  ? 1.2557 0.6665 1.1659 -0.2210 0.0964  -0.1168 917  ASN B OD1 
2841 N ND2 . ASN B 65  ? 1.2305 0.7293 1.1714 -0.2769 0.0967  -0.1645 917  ASN B ND2 
2842 N N   . HIS B 66  ? 0.9346 0.4819 0.8542 -0.1902 0.0848  -0.0524 918  HIS B N   
2843 C CA  . HIS B 66  ? 0.8000 0.4016 0.7318 -0.1580 0.0710  -0.0587 918  HIS B CA  
2844 C C   . HIS B 66  ? 0.6734 0.3561 0.6221 -0.1587 0.0667  -0.0545 918  HIS B C   
2845 O O   . HIS B 66  ? 0.5943 0.3208 0.5532 -0.1371 0.0564  -0.0603 918  HIS B O   
2846 C CB  . HIS B 66  ? 0.8053 0.3725 0.7206 -0.1193 0.0649  -0.0400 918  HIS B CB  
2847 C CG  . HIS B 66  ? 0.9251 0.4151 0.8264 -0.1084 0.0679  -0.0452 918  HIS B CG  
2848 N ND1 . HIS B 66  ? 0.9952 0.4806 0.9047 -0.0986 0.0645  -0.0739 918  HIS B ND1 
2849 C CD2 . HIS B 66  ? 1.0407 0.4528 0.9195 -0.1047 0.0749  -0.0253 918  HIS B CD2 
2850 C CE1 . HIS B 66  ? 1.0594 0.4654 0.9535 -0.0878 0.0699  -0.0740 918  HIS B CE1 
2851 N NE2 . HIS B 66  ? 1.0924 0.4503 0.9677 -0.0905 0.0758  -0.0430 918  HIS B NE2 
2852 N N   . ILE B 67  ? 0.6299 0.3308 0.5811 -0.1830 0.0758  -0.0445 919  ILE B N   
2853 C CA  . ILE B 67  ? 0.5445 0.3212 0.5144 -0.1842 0.0741  -0.0438 919  ILE B CA  
2854 C C   . ILE B 67  ? 0.4442 0.2789 0.4390 -0.1865 0.0662  -0.0678 919  ILE B C   
2855 O O   . ILE B 67  ? 0.3722 0.2571 0.3785 -0.1679 0.0587  -0.0667 919  ILE B O   
2856 C CB  . ILE B 67  ? 0.5569 0.3465 0.5279 -0.2141 0.0880  -0.0337 919  ILE B CB  
2857 C CG1 . ILE B 67  ? 0.5708 0.4314 0.5579 -0.2059 0.0876  -0.0301 919  ILE B CG1 
2858 C CG2 . ILE B 67  ? 0.6137 0.4045 0.5966 -0.2533 0.0959  -0.0519 919  ILE B CG2 
2859 C CD1 . ILE B 67  ? 0.6633 0.5333 0.6448 -0.2254 0.1020  -0.0157 919  ILE B CD1 
2860 N N   . ALA B 68  ? 0.4801 0.3052 0.4807 -0.2097 0.0680  -0.0891 920  ALA B N   
2861 C CA  . ALA B 68  ? 0.4568 0.3393 0.4778 -0.2143 0.0595  -0.1129 920  ALA B CA  
2862 C C   . ALA B 68  ? 0.4248 0.3148 0.4427 -0.1814 0.0473  -0.1164 920  ALA B C   
2863 O O   . ALA B 68  ? 0.3972 0.3478 0.4291 -0.1700 0.0385  -0.1192 920  ALA B O   
2864 C CB  . ALA B 68  ? 0.5106 0.3733 0.5330 -0.2472 0.0642  -0.1376 920  ALA B CB  
2865 N N   . ASP B 69  ? 0.4437 0.2735 0.4432 -0.1652 0.0472  -0.1144 921  ASP B N   
2866 C CA  . ASP B 69  ? 0.4279 0.2669 0.4243 -0.1345 0.0372  -0.1172 921  ASP B CA  
2867 C C   . ASP B 69  ? 0.3524 0.2263 0.3513 -0.1122 0.0316  -0.0968 921  ASP B C   
2868 O O   . ASP B 69  ? 0.3160 0.2321 0.3220 -0.0984 0.0233  -0.1005 921  ASP B O   
2869 C CB  . ASP B 69  ? 0.4797 0.2513 0.4582 -0.1177 0.0391  -0.1170 921  ASP B CB  
2870 C CG  . ASP B 69  ? 0.5971 0.3264 0.5713 -0.1350 0.0447  -0.1425 921  ASP B CG  
2871 O OD1 . ASP B 69  ? 0.5898 0.3548 0.5747 -0.1546 0.0430  -0.1672 921  ASP B OD1 
2872 O OD2 . ASP B 69  ? 0.6982 0.3566 0.6570 -0.1279 0.0507  -0.1379 921  ASP B OD2 
2873 N N   . LEU B 70  ? 0.3367 0.1916 0.3274 -0.1099 0.0368  -0.0756 922  LEU B N   
2874 C CA  . LEU B 70  ? 0.3071 0.1904 0.2981 -0.0920 0.0331  -0.0597 922  LEU B CA  
2875 C C   . LEU B 70  ? 0.2583 0.2028 0.2689 -0.0971 0.0311  -0.0637 922  LEU B C   
2876 O O   . LEU B 70  ? 0.2129 0.1857 0.2271 -0.0800 0.0246  -0.0599 922  LEU B O   
2877 C CB  . LEU B 70  ? 0.3368 0.1917 0.3129 -0.0916 0.0399  -0.0389 922  LEU B CB  
2878 C CG  . LEU B 70  ? 0.2909 0.1715 0.2645 -0.0767 0.0377  -0.0259 922  LEU B CG  
2879 C CD1 . LEU B 70  ? 0.2901 0.1773 0.2605 -0.0536 0.0277  -0.0261 922  LEU B CD1 
2880 C CD2 . LEU B 70  ? 0.3621 0.2178 0.3173 -0.0796 0.0450  -0.0075 922  LEU B CD2 
2881 N N   . LYS B 71  ? 0.2537 0.2180 0.2767 -0.1204 0.0371  -0.0704 923  LYS B N   
2882 C CA  . LYS B 71  ? 0.2237 0.2513 0.2682 -0.1226 0.0348  -0.0739 923  LYS B CA  
2883 C C   . LYS B 71  ? 0.2260 0.2890 0.2787 -0.1140 0.0233  -0.0859 923  LYS B C   
2884 O O   . LYS B 71  ? 0.1689 0.2728 0.2310 -0.0986 0.0175  -0.0797 923  LYS B O   
2885 C CB  . LYS B 71  ? 0.2708 0.3206 0.3293 -0.1515 0.0433  -0.0808 923  LYS B CB  
2886 C CG  . LYS B 71  ? 0.3161 0.3557 0.3705 -0.1587 0.0554  -0.0666 923  LYS B CG  
2887 C CD  . LYS B 71  ? 0.3107 0.3787 0.3806 -0.1911 0.0647  -0.0749 923  LYS B CD  
2888 C CE  . LYS B 71  ? 0.4230 0.5032 0.4936 -0.1967 0.0775  -0.0617 923  LYS B CE  
2889 N NZ  . LYS B 71  ? 0.3969 0.5234 0.4888 -0.2284 0.0866  -0.0710 923  LYS B NZ  
2890 N N   . LYS B 72  ? 0.2535 0.2969 0.2999 -0.1223 0.0205  -0.1022 924  LYS B N   
2891 C CA  . LYS B 72  ? 0.2454 0.3204 0.2938 -0.1141 0.0102  -0.1143 924  LYS B CA  
2892 C C   . LYS B 72  ? 0.2257 0.2975 0.2646 -0.0868 0.0045  -0.1015 924  LYS B C   
2893 O O   . LYS B 72  ? 0.2057 0.3193 0.2496 -0.0763 -0.0028 -0.0975 924  LYS B O   
2894 C CB  . LYS B 72  ? 0.3056 0.3565 0.3468 -0.1289 0.0108  -0.1384 924  LYS B CB  
2895 C CG  . LYS B 72  ? 0.4251 0.5006 0.4782 -0.1608 0.0132  -0.1579 924  LYS B CG  
2896 C CD  . LYS B 72  ? 0.4883 0.5385 0.5319 -0.1751 0.0137  -0.1868 924  LYS B CD  
2897 C CE  . LYS B 72  ? 0.5793 0.6652 0.6347 -0.2106 0.0143  -0.2105 924  LYS B CE  
2898 N NZ  . LYS B 72  ? 0.6562 0.7081 0.6992 -0.2260 0.0167  -0.2422 924  LYS B NZ  
2899 N N   . GLU B 73  ? 0.2332 0.2573 0.2579 -0.0760 0.0079  -0.0934 925  GLU B N   
2900 C CA  . GLU B 73  ? 0.2070 0.2300 0.2235 -0.0545 0.0036  -0.0816 925  GLU B CA  
2901 C C   . GLU B 73  ? 0.1829 0.2320 0.2047 -0.0458 0.0024  -0.0655 925  GLU B C   
2902 O O   . GLU B 73  ? 0.1820 0.2499 0.2018 -0.0339 -0.0029 -0.0598 925  GLU B O   
2903 C CB  . GLU B 73  ? 0.2418 0.2162 0.2447 -0.0463 0.0074  -0.0740 925  GLU B CB  
2904 C CG  . GLU B 73  ? 0.2064 0.1827 0.2017 -0.0274 0.0029  -0.0662 925  GLU B CG  
2905 C CD  . GLU B 73  ? 0.3107 0.2474 0.2939 -0.0179 0.0049  -0.0585 925  GLU B CD  
2906 O OE1 . GLU B 73  ? 0.2924 0.1924 0.2707 -0.0246 0.0100  -0.0593 925  GLU B OE1 
2907 O OE2 . GLU B 73  ? 0.3448 0.2885 0.3229 -0.0043 0.0012  -0.0510 925  GLU B OE2 
2908 N N   . ILE B 74  ? 0.1930 0.2390 0.2199 -0.0518 0.0089  -0.0581 926  ILE B N   
2909 C CA  . ILE B 74  ? 0.1683 0.2332 0.2008 -0.0427 0.0104  -0.0460 926  ILE B CA  
2910 C C   . ILE B 74  ? 0.1653 0.2776 0.2119 -0.0378 0.0040  -0.0468 926  ILE B C   
2911 O O   . ILE B 74  ? 0.1497 0.2712 0.1949 -0.0230 0.0009  -0.0363 926  ILE B O   
2912 C CB  . ILE B 74  ? 0.2154 0.2764 0.2526 -0.0523 0.0204  -0.0424 926  ILE B CB  
2913 C CG1 . ILE B 74  ? 0.2063 0.2238 0.2246 -0.0519 0.0258  -0.0346 926  ILE B CG1 
2914 C CG2 . ILE B 74  ? 0.2133 0.3047 0.2625 -0.0418 0.0231  -0.0355 926  ILE B CG2 
2915 C CD1 . ILE B 74  ? 0.2444 0.2521 0.2613 -0.0669 0.0365  -0.0316 926  ILE B CD1 
2916 N N   . GLU B 75  ? 0.1500 0.2919 0.2088 -0.0511 0.0019  -0.0586 927  GLU B N   
2917 C CA  . GLU B 75  ? 0.1860 0.3821 0.2590 -0.0463 -0.0055 -0.0582 927  GLU B CA  
2918 C C   . GLU B 75  ? 0.1996 0.4052 0.2617 -0.0369 -0.0148 -0.0570 927  GLU B C   
2919 O O   . GLU B 75  ? 0.1922 0.4281 0.2575 -0.0236 -0.0207 -0.0455 927  GLU B O   
2920 C CB  . GLU B 75  ? 0.2305 0.4634 0.3191 -0.0671 -0.0061 -0.0739 927  GLU B CB  
2921 C CG  . GLU B 75  ? 0.2311 0.5319 0.3370 -0.0612 -0.0150 -0.0720 927  GLU B CG  
2922 C CD  . GLU B 75  ? 0.2564 0.5773 0.3754 -0.0402 -0.0128 -0.0543 927  GLU B CD  
2923 O OE1 . GLU B 75  ? 0.1494 0.4408 0.2684 -0.0376 -0.0023 -0.0490 927  GLU B OE1 
2924 O OE2 . GLU B 75  ? 0.1923 0.5593 0.3207 -0.0251 -0.0216 -0.0458 927  GLU B OE2 
2925 N N   . ILE B 76  ? 0.1821 0.3618 0.2308 -0.0425 -0.0151 -0.0679 928  ILE B N   
2926 C CA  . ILE B 76  ? 0.1690 0.3550 0.2052 -0.0337 -0.0210 -0.0667 928  ILE B CA  
2927 C C   . ILE B 76  ? 0.1453 0.3147 0.1733 -0.0181 -0.0201 -0.0466 928  ILE B C   
2928 O O   . ILE B 76  ? 0.1684 0.3600 0.1930 -0.0096 -0.0250 -0.0353 928  ILE B O   
2929 C CB  . ILE B 76  ? 0.1576 0.3163 0.1827 -0.0390 -0.0191 -0.0835 928  ILE B CB  
2930 C CG1 . ILE B 76  ? 0.2268 0.3996 0.2564 -0.0565 -0.0199 -0.1073 928  ILE B CG1 
2931 C CG2 . ILE B 76  ? 0.2135 0.3822 0.2263 -0.0285 -0.0228 -0.0807 928  ILE B CG2 
2932 C CD1 . ILE B 76  ? 0.2437 0.3748 0.2635 -0.0603 -0.0151 -0.1259 928  ILE B CD1 
2933 N N   . LEU B 77  ? 0.1386 0.2693 0.1622 -0.0159 -0.0137 -0.0418 929  LEU B N   
2934 C CA  . LEU B 77  ? 0.1307 0.2447 0.1446 -0.0059 -0.0125 -0.0275 929  LEU B CA  
2935 C C   . LEU B 77  ? 0.1095 0.2319 0.1286 0.0034  -0.0118 -0.0127 929  LEU B C   
2936 O O   . LEU B 77  ? 0.1506 0.2691 0.1610 0.0102  -0.0131 -0.0006 929  LEU B O   
2937 C CB  . LEU B 77  ? 0.1438 0.2197 0.1495 -0.0066 -0.0070 -0.0274 929  LEU B CB  
2938 C CG  . LEU B 77  ? 0.1644 0.2271 0.1588 -0.0015 -0.0066 -0.0178 929  LEU B CG  
2939 C CD1 . LEU B 77  ? 0.1593 0.2377 0.1469 -0.0007 -0.0110 -0.0187 929  LEU B CD1 
2940 C CD2 . LEU B 77  ? 0.1357 0.1709 0.1227 -0.0027 -0.0027 -0.0183 929  LEU B CD2 
2941 N N   . ARG B 78  ? 0.1491 0.2827 0.1822 0.0035  -0.0088 -0.0138 930  ARG B N   
2942 C CA  . ARG B 78  ? 0.1869 0.3321 0.2293 0.0168  -0.0072 -0.0020 930  ARG B CA  
2943 C C   . ARG B 78  ? 0.1858 0.3583 0.2279 0.0280  -0.0153 0.0104  930  ARG B C   
2944 O O   . ARG B 78  ? 0.2110 0.3726 0.2513 0.0430  -0.0138 0.0256  930  ARG B O   
2945 C CB  . ARG B 78  ? 0.1429 0.3152 0.2052 0.0134  -0.0039 -0.0089 930  ARG B CB  
2946 C CG  . ARG B 78  ? 0.1761 0.3585 0.2508 0.0303  0.0008  0.0004  930  ARG B CG  
2947 C CD  . ARG B 78  ? 0.2108 0.4233 0.3058 0.0235  0.0066  -0.0087 930  ARG B CD  
2948 N NE  . ARG B 78  ? 0.1436 0.4140 0.2571 0.0189  -0.0015 -0.0134 930  ARG B NE  
2949 C CZ  . ARG B 78  ? 0.2129 0.5290 0.3427 0.0368  -0.0075 -0.0044 930  ARG B CZ  
2950 N NH1 . ARG B 78  ? 0.2064 0.5078 0.3354 0.0629  -0.0052 0.0108  930  ARG B NH1 
2951 N NH2 . ARG B 78  ? 0.1911 0.5682 0.3379 0.0292  -0.0159 -0.0109 930  ARG B NH2 
2952 N N   . ASN B 79  ? 0.2077 0.4137 0.2500 0.0206  -0.0234 0.0037  931  ASN B N   
2953 C CA  . ASN B 79  ? 0.1826 0.4246 0.2222 0.0291  -0.0325 0.0157  931  ASN B CA  
2954 C C   . ASN B 79  ? 0.2438 0.4761 0.2624 0.0259  -0.0350 0.0210  931  ASN B C   
2955 O O   . ASN B 79  ? 0.2444 0.5085 0.2562 0.0301  -0.0423 0.0313  931  ASN B O   
2956 C CB  . ASN B 79  ? 0.2357 0.5329 0.2879 0.0208  -0.0402 0.0029  931  ASN B CB  
2957 C CG  . ASN B 79  ? 0.2577 0.5791 0.3336 0.0237  -0.0382 0.0004  931  ASN B CG  
2958 O OD1 . ASN B 79  ? 0.3567 0.6922 0.4421 0.0434  -0.0391 0.0169  931  ASN B OD1 
2959 N ND2 . ASN B 79  ? 0.2606 0.5829 0.3459 0.0048  -0.0338 -0.0197 931  ASN B ND2 
2960 N N   . LEU B 80  ? 0.2020 0.3962 0.2103 0.0189  -0.0289 0.0154  932  LEU B N   
2961 C CA  . LEU B 80  ? 0.2124 0.4010 0.2032 0.0153  -0.0293 0.0208  932  LEU B CA  
2962 C C   . LEU B 80  ? 0.2165 0.3690 0.1979 0.0207  -0.0241 0.0395  932  LEU B C   
2963 O O   . LEU B 80  ? 0.2175 0.3349 0.2009 0.0206  -0.0175 0.0368  932  LEU B O   
2964 C CB  . LEU B 80  ? 0.1940 0.3726 0.1812 0.0052  -0.0266 0.0018  932  LEU B CB  
2965 C CG  . LEU B 80  ? 0.2388 0.4412 0.2305 -0.0020 -0.0297 -0.0204 932  LEU B CG  
2966 C CD1 . LEU B 80  ? 0.2518 0.4342 0.2389 -0.0053 -0.0256 -0.0349 932  LEU B CD1 
2967 C CD2 . LEU B 80  ? 0.2543 0.5046 0.2404 -0.0041 -0.0367 -0.0223 932  LEU B CD2 
2968 N N   . TYR B 81  ? 0.2519 0.4116 0.2208 0.0237  -0.0265 0.0583  933  TYR B N   
2969 C CA  . TYR B 81  ? 0.3159 0.4353 0.2725 0.0254  -0.0207 0.0768  933  TYR B CA  
2970 C C   . TYR B 81  ? 0.2791 0.4065 0.2169 0.0132  -0.0204 0.0856  933  TYR B C   
2971 O O   . TYR B 81  ? 0.2659 0.4175 0.1938 0.0160  -0.0250 0.1019  933  TYR B O   
2972 C CB  . TYR B 81  ? 0.3942 0.5045 0.3527 0.0437  -0.0217 0.0982  933  TYR B CB  
2973 C CG  . TYR B 81  ? 0.4867 0.6044 0.4663 0.0580  -0.0220 0.0913  933  TYR B CG  
2974 C CD1 . TYR B 81  ? 0.6159 0.6936 0.6013 0.0627  -0.0129 0.0858  933  TYR B CD1 
2975 C CD2 . TYR B 81  ? 0.5647 0.7349 0.5583 0.0656  -0.0308 0.0895  933  TYR B CD2 
2976 C CE1 . TYR B 81  ? 0.5983 0.6893 0.6040 0.0754  -0.0114 0.0791  933  TYR B CE1 
2977 C CE2 . TYR B 81  ? 0.5566 0.7421 0.5723 0.0768  -0.0302 0.0829  933  TYR B CE2 
2978 C CZ  . TYR B 81  ? 0.6039 0.7498 0.6259 0.0822  -0.0199 0.0783  933  TYR B CZ  
2979 O OH  . TYR B 81  ? 0.6305 0.7975 0.6749 0.0925  -0.0176 0.0713  933  TYR B OH  
2980 N N   . HIS B 82  ? 0.2192 0.3315 0.1522 -0.0005 -0.0150 0.0756  934  HIS B N   
2981 C CA  . HIS B 82  ? 0.2089 0.3350 0.1268 -0.0151 -0.0129 0.0812  934  HIS B CA  
2982 C C   . HIS B 82  ? 0.2307 0.3295 0.1451 -0.0290 -0.0057 0.0758  934  HIS B C   
2983 O O   . HIS B 82  ? 0.2279 0.3147 0.1521 -0.0280 -0.0047 0.0599  934  HIS B O   
2984 C CB  . HIS B 82  ? 0.1729 0.3491 0.0933 -0.0182 -0.0170 0.0647  934  HIS B CB  
2985 C CG  . HIS B 82  ? 0.1929 0.3965 0.0982 -0.0312 -0.0143 0.0711  934  HIS B CG  
2986 N ND1 . HIS B 82  ? 0.2586 0.4683 0.1635 -0.0436 -0.0088 0.0614  934  HIS B ND1 
2987 C CD2 . HIS B 82  ? 0.2933 0.5256 0.1830 -0.0342 -0.0161 0.0875  934  HIS B CD2 
2988 C CE1 . HIS B 82  ? 0.2093 0.4510 0.1004 -0.0551 -0.0060 0.0700  934  HIS B CE1 
2989 N NE2 . HIS B 82  ? 0.2344 0.4885 0.1143 -0.0501 -0.0101 0.0865  934  HIS B NE2 
2990 N N   . GLU B 83  ? 0.2778 0.3708 0.1768 -0.0439 -0.0009 0.0899  935  GLU B N   
2991 C CA  . GLU B 83  ? 0.2971 0.3697 0.1914 -0.0623 0.0059  0.0856  935  GLU B CA  
2992 C C   . GLU B 83  ? 0.2432 0.3481 0.1492 -0.0668 0.0045  0.0621  935  GLU B C   
2993 O O   . GLU B 83  ? 0.2330 0.3229 0.1412 -0.0754 0.0072  0.0533  935  GLU B O   
2994 C CB  . GLU B 83  ? 0.3556 0.4281 0.2310 -0.0816 0.0116  0.1052  935  GLU B CB  
2995 C CG  . GLU B 83  ? 0.5330 0.5845 0.4019 -0.1063 0.0195  0.1026  935  GLU B CG  
2996 C CD  . GLU B 83  ? 0.6133 0.6516 0.4609 -0.1282 0.0270  0.1257  935  GLU B CD  
2997 O OE1 . GLU B 83  ? 0.6895 0.7691 0.5297 -0.1320 0.0263  0.1363  935  GLU B OE1 
2998 O OE2 . GLU B 83  ? 0.7895 0.7748 0.6262 -0.1434 0.0345  0.1327  935  GLU B OE2 
2999 N N   . ASN B 84  ? 0.1918 0.3416 0.1041 -0.0600 0.0003  0.0523  936  ASN B N   
3000 C CA  . ASN B 84  ? 0.1459 0.3271 0.0699 -0.0574 -0.0012 0.0314  936  ASN B CA  
3001 C C   . ASN B 84  ? 0.1103 0.2863 0.0475 -0.0393 -0.0063 0.0157  936  ASN B C   
3002 O O   . ASN B 84  ? 0.0998 0.3019 0.0450 -0.0322 -0.0079 -0.0003 936  ASN B O   
3003 C CB  . ASN B 84  ? 0.1542 0.3870 0.0745 -0.0632 0.0003  0.0289  936  ASN B CB  
3004 C CG  . ASN B 84  ? 0.1955 0.4341 0.1024 -0.0857 0.0069  0.0449  936  ASN B CG  
3005 O OD1 . ASN B 84  ? 0.1988 0.4520 0.0920 -0.0922 0.0089  0.0597  936  ASN B OD1 
3006 N ND2 . ASN B 84  ? 0.1566 0.3821 0.0652 -0.0999 0.0105  0.0432  936  ASN B ND2 
3007 N N   A ILE B 85  ? 0.1075 0.2493 0.0466 -0.0323 -0.0075 0.0207  937  ILE B N   
3008 N N   B ILE B 85  ? 0.1160 0.2575 0.0551 -0.0323 -0.0075 0.0206  937  ILE B N   
3009 C CA  A ILE B 85  ? 0.1297 0.2610 0.0798 -0.0202 -0.0104 0.0086  937  ILE B CA  
3010 C CA  B ILE B 85  ? 0.1453 0.2766 0.0954 -0.0202 -0.0104 0.0086  937  ILE B CA  
3011 C C   A ILE B 85  ? 0.1473 0.2406 0.0978 -0.0203 -0.0077 0.0117  937  ILE B C   
3012 C C   B ILE B 85  ? 0.1545 0.2478 0.1050 -0.0202 -0.0078 0.0116  937  ILE B C   
3013 O O   A ILE B 85  ? 0.1426 0.2126 0.0876 -0.0222 -0.0048 0.0237  937  ILE B O   
3014 O O   B ILE B 85  ? 0.1488 0.2189 0.0940 -0.0219 -0.0049 0.0236  937  ILE B O   
3015 C CB  A ILE B 85  ? 0.1408 0.2828 0.0945 -0.0130 -0.0141 0.0093  937  ILE B CB  
3016 C CB  B ILE B 85  ? 0.1651 0.3065 0.1185 -0.0130 -0.0141 0.0099  937  ILE B CB  
3017 C CG1 A ILE B 85  ? 0.1032 0.2856 0.0555 -0.0132 -0.0165 -0.0013 937  ILE B CG1 
3018 C CG1 B ILE B 85  ? 0.1645 0.3477 0.1145 -0.0142 -0.0165 0.0034  937  ILE B CG1 
3019 C CG2 A ILE B 85  ? 0.1459 0.2693 0.1107 -0.0059 -0.0149 0.0002  937  ILE B CG2 
3020 C CG2 B ILE B 85  ? 0.1918 0.3190 0.1568 -0.0059 -0.0153 -0.0016 937  ILE B CG2 
3021 C CD1 A ILE B 85  ? 0.0852 0.2881 0.0390 -0.0096 -0.0212 -0.0037 937  ILE B CD1 
3022 C CD1 B ILE B 85  ? 0.1444 0.3433 0.1004 -0.0109 -0.0163 -0.0184 937  ILE B CD1 
3023 N N   . VAL B 86  ? 0.1496 0.2357 0.1049 -0.0169 -0.0082 0.0010  938  VAL B N   
3024 C CA  . VAL B 86  ? 0.1860 0.2420 0.1384 -0.0186 -0.0052 0.0021  938  VAL B CA  
3025 C C   . VAL B 86  ? 0.1760 0.2114 0.1317 -0.0126 -0.0026 0.0071  938  VAL B C   
3026 O O   . VAL B 86  ? 0.1543 0.2013 0.1186 -0.0059 -0.0050 0.0055  938  VAL B O   
3027 C CB  . VAL B 86  ? 0.1621 0.2167 0.1170 -0.0138 -0.0071 -0.0069 938  VAL B CB  
3028 C CG1 . VAL B 86  ? 0.1563 0.2055 0.1191 -0.0049 -0.0081 -0.0120 938  VAL B CG1 
3029 C CG2 . VAL B 86  ? 0.1710 0.2048 0.1180 -0.0192 -0.0042 -0.0058 938  VAL B CG2 
3030 N N   . LYS B 87  ? 0.2174 0.2259 0.1669 -0.0156 0.0026  0.0114  939  LYS B N   
3031 C CA  . LYS B 87  ? 0.2223 0.2138 0.1759 -0.0070 0.0065  0.0166  939  LYS B CA  
3032 C C   . LYS B 87  ? 0.2220 0.2113 0.1835 -0.0016 0.0087  0.0088  939  LYS B C   
3033 O O   . LYS B 87  ? 0.2574 0.2337 0.2124 -0.0061 0.0120  0.0028  939  LYS B O   
3034 C CB  . LYS B 87  ? 0.2678 0.2255 0.2106 -0.0107 0.0135  0.0216  939  LYS B CB  
3035 C CG  . LYS B 87  ? 0.2861 0.2381 0.2204 -0.0162 0.0134  0.0343  939  LYS B CG  
3036 C CD  . LYS B 87  ? 0.4693 0.3758 0.3918 -0.0198 0.0220  0.0391  939  LYS B CD  
3037 C CE  . LYS B 87  ? 0.5426 0.4370 0.4560 -0.0221 0.0226  0.0581  939  LYS B CE  
3038 N NZ  . LYS B 87  ? 0.5900 0.4287 0.4907 -0.0244 0.0322  0.0635  939  LYS B NZ  
3039 N N   . TYR B 88  ? 0.2452 0.2511 0.2196 0.0062  0.0070  0.0097  940  TYR B N   
3040 C CA  . TYR B 88  ? 0.2282 0.2346 0.2122 0.0100  0.0115  0.0049  940  TYR B CA  
3041 C C   . TYR B 88  ? 0.2120 0.1966 0.1936 0.0162  0.0201  0.0068  940  TYR B C   
3042 O O   . TYR B 88  ? 0.2562 0.2312 0.2370 0.0243  0.0212  0.0151  940  TYR B O   
3043 C CB  . TYR B 88  ? 0.2076 0.2443 0.2077 0.0151  0.0075  0.0054  940  TYR B CB  
3044 C CG  . TYR B 88  ? 0.1855 0.2336 0.1999 0.0179  0.0129  0.0014  940  TYR B CG  
3045 C CD1 . TYR B 88  ? 0.2218 0.2754 0.2405 0.0072  0.0145  -0.0076 940  TYR B CD1 
3046 C CD2 . TYR B 88  ? 0.2602 0.3145 0.2845 0.0311  0.0172  0.0067  940  TYR B CD2 
3047 C CE1 . TYR B 88  ? 0.1832 0.2523 0.2152 0.0053  0.0207  -0.0112 940  TYR B CE1 
3048 C CE2 . TYR B 88  ? 0.2161 0.2915 0.2568 0.0336  0.0230  0.0017  940  TYR B CE2 
3049 C CZ  . TYR B 88  ? 0.2010 0.2862 0.2454 0.0182  0.0249  -0.0074 940  TYR B CZ  
3050 O OH  . TYR B 88  ? 0.1932 0.3024 0.2531 0.0159  0.0322  -0.0123 940  TYR B OH  
3051 N N   . LYS B 89  ? 0.2243 0.1998 0.2032 0.0132  0.0269  -0.0006 941  LYS B N   
3052 C CA  . LYS B 89  ? 0.1974 0.1560 0.1749 0.0202  0.0371  -0.0034 941  LYS B CA  
3053 C C   . LYS B 89  ? 0.2000 0.1798 0.1932 0.0264  0.0432  -0.0072 941  LYS B C   
3054 O O   . LYS B 89  ? 0.1990 0.1794 0.2013 0.0402  0.0503  -0.0077 941  LYS B O   
3055 C CB  . LYS B 89  ? 0.2652 0.1999 0.2226 0.0098  0.0421  -0.0112 941  LYS B CB  
3056 C CG  . LYS B 89  ? 0.2783 0.1936 0.2219 0.0021  0.0389  -0.0092 941  LYS B CG  
3057 C CD  . LYS B 89  ? 0.4006 0.3033 0.3252 -0.0115 0.0417  -0.0189 941  LYS B CD  
3058 C CE  . LYS B 89  ? 0.5052 0.3798 0.4200 -0.0105 0.0536  -0.0291 941  LYS B CE  
3059 N NZ  . LYS B 89  ? 0.4996 0.3420 0.4125 -0.0068 0.0575  -0.0258 941  LYS B NZ  
3060 N N   . GLY B 90  ? 0.2107 0.2071 0.2073 0.0163  0.0419  -0.0103 942  GLY B N   
3061 C CA  . GLY B 90  ? 0.1966 0.2183 0.2090 0.0168  0.0485  -0.0138 942  GLY B CA  
3062 C C   . GLY B 90  ? 0.1497 0.1778 0.1602 0.0007  0.0488  -0.0159 942  GLY B C   
3063 O O   . GLY B 90  ? 0.1837 0.1995 0.1847 -0.0072 0.0414  -0.0142 942  GLY B O   
3064 N N   . ILE B 91  ? 0.1961 0.2418 0.2148 -0.0037 0.0587  -0.0194 943  ILE B N   
3065 C CA  . ILE B 91  ? 0.2220 0.2677 0.2356 -0.0217 0.0627  -0.0193 943  ILE B CA  
3066 C C   . ILE B 91  ? 0.2309 0.2756 0.2333 -0.0264 0.0763  -0.0209 943  ILE B C   
3067 O O   . ILE B 91  ? 0.2230 0.2774 0.2295 -0.0151 0.0844  -0.0263 943  ILE B O   
3068 C CB  . ILE B 91  ? 0.2363 0.3144 0.2724 -0.0318 0.0623  -0.0223 943  ILE B CB  
3069 C CG1 . ILE B 91  ? 0.2487 0.3703 0.3096 -0.0222 0.0689  -0.0264 943  ILE B CG1 
3070 C CG2 . ILE B 91  ? 0.2000 0.2783 0.2411 -0.0319 0.0490  -0.0230 943  ILE B CG2 
3071 C CD1 . ILE B 91  ? 0.2582 0.4240 0.3434 -0.0362 0.0692  -0.0311 943  ILE B CD1 
3072 N N   . CYS B 92  ? 0.2352 0.2663 0.2218 -0.0422 0.0790  -0.0159 944  CYS B N   
3073 C CA  . CYS B 92  ? 0.2574 0.2947 0.2322 -0.0521 0.0927  -0.0150 944  CYS B CA  
3074 C C   . CYS B 92  ? 0.2833 0.3303 0.2657 -0.0722 0.0973  -0.0107 944  CYS B C   
3075 O O   . CYS B 92  ? 0.3103 0.3312 0.2847 -0.0811 0.0901  -0.0040 944  CYS B O   
3076 C CB  . CYS B 92  ? 0.2771 0.2861 0.2195 -0.0542 0.0913  -0.0089 944  CYS B CB  
3077 S SG  . CYS B 92  ? 0.3271 0.3453 0.2477 -0.0690 0.1074  -0.0048 944  CYS B SG  
3078 N N   . THR B 93  ? 0.3170 0.4017 0.3160 -0.0794 0.1100  -0.0158 945  THR B N   
3079 C CA  . THR B 93  ? 0.3538 0.4538 0.3633 -0.1038 0.1161  -0.0136 945  THR B CA  
3080 C C   . THR B 93  ? 0.4267 0.5293 0.4176 -0.1211 0.1321  -0.0069 945  THR B C   
3081 O O   . THR B 93  ? 0.4417 0.5758 0.4360 -0.1150 0.1440  -0.0132 945  THR B O   
3082 C CB  . THR B 93  ? 0.3802 0.5353 0.4274 -0.1028 0.1179  -0.0246 945  THR B CB  
3083 O OG1 . THR B 93  ? 0.3926 0.5838 0.4519 -0.0854 0.1276  -0.0316 945  THR B OG1 
3084 C CG2 . THR B 93  ? 0.3713 0.5256 0.4329 -0.0894 0.1013  -0.0284 945  THR B CG2 
3085 N N   . ASN B 98  ? 0.6054 0.7158 0.6409 -0.2653 0.1529  -0.0097 950  ASN B N   
3086 C CA  . ASN B 98  ? 0.6202 0.6787 0.6493 -0.2673 0.1401  -0.0136 950  ASN B CA  
3087 C C   . ASN B 98  ? 0.6032 0.6163 0.6128 -0.2321 0.1256  -0.0073 950  ASN B C   
3088 O O   . ASN B 98  ? 0.6177 0.6317 0.6385 -0.2169 0.1118  -0.0186 950  ASN B O   
3089 C CB  . ASN B 98  ? 0.6927 0.6944 0.7013 -0.3034 0.1499  -0.0047 950  ASN B CB  
3090 C CG  . ASN B 98  ? 0.7136 0.7610 0.7439 -0.3455 0.1638  -0.0143 950  ASN B CG  
3091 O OD1 . ASN B 98  ? 0.6827 0.8111 0.7422 -0.3459 0.1683  -0.0241 950  ASN B OD1 
3092 N ND2 . ASN B 98  ? 0.7740 0.7694 0.7907 -0.3813 0.1712  -0.0118 950  ASN B ND2 
3093 N N   . GLY B 99  ? 0.5864 0.5679 0.5672 -0.2205 0.1288  0.0104  951  GLY B N   
3094 C CA  . GLY B 99  ? 0.5385 0.4800 0.4993 -0.1910 0.1157  0.0176  951  GLY B CA  
3095 C C   . GLY B 99  ? 0.4791 0.4561 0.4539 -0.1615 0.1061  0.0079  951  GLY B C   
3096 O O   . GLY B 99  ? 0.4418 0.4675 0.4321 -0.1572 0.1124  0.0017  951  GLY B O   
3097 N N   . ILE B 100 ? 0.3863 0.3370 0.3549 -0.1408 0.0920  0.0072  952  ILE B N   
3098 C CA  . ILE B 100 ? 0.3150 0.2912 0.2954 -0.1163 0.0825  -0.0010 952  ILE B CA  
3099 C C   . ILE B 100 ? 0.3016 0.2454 0.2625 -0.0963 0.0716  0.0054  952  ILE B C   
3100 O O   . ILE B 100 ? 0.3194 0.2240 0.2655 -0.0968 0.0674  0.0121  952  ILE B O   
3101 C CB  . ILE B 100 ? 0.3322 0.3380 0.3403 -0.1168 0.0755  -0.0159 952  ILE B CB  
3102 C CG1 . ILE B 100 ? 0.2977 0.3362 0.3195 -0.0938 0.0689  -0.0208 952  ILE B CG1 
3103 C CG2 . ILE B 100 ? 0.3541 0.3251 0.3572 -0.1194 0.0662  -0.0204 952  ILE B CG2 
3104 C CD1 . ILE B 100 ? 0.3082 0.3901 0.3576 -0.0949 0.0634  -0.0321 952  ILE B CD1 
3105 N N   . LYS B 101 ? 0.2605 0.2212 0.2223 -0.0788 0.0677  0.0027  953  LYS B N   
3106 C CA  . LYS B 101 ? 0.2438 0.1862 0.1914 -0.0624 0.0574  0.0060  953  LYS B CA  
3107 C C   . LYS B 101 ? 0.2315 0.1944 0.1950 -0.0494 0.0503  -0.0031 953  LYS B C   
3108 O O   . LYS B 101 ? 0.2351 0.2237 0.2125 -0.0465 0.0549  -0.0085 953  LYS B O   
3109 C CB  . LYS B 101 ? 0.2591 0.1958 0.1831 -0.0591 0.0608  0.0140  953  LYS B CB  
3110 C CG  . LYS B 101 ? 0.3804 0.2987 0.2832 -0.0716 0.0682  0.0278  953  LYS B CG  
3111 C CD  . LYS B 101 ? 0.3780 0.3021 0.2563 -0.0690 0.0714  0.0334  953  LYS B CD  
3112 C CE  . LYS B 101 ? 0.4405 0.3532 0.2955 -0.0827 0.0804  0.0493  953  LYS B CE  
3113 N NZ  . LYS B 101 ? 0.4089 0.2867 0.2437 -0.0784 0.0720  0.0677  953  LYS B NZ  
3114 N N   . LEU B 102 ? 0.2300 0.1822 0.1910 -0.0405 0.0397  -0.0039 954  LEU B N   
3115 C CA  . LEU B 102 ? 0.2116 0.1803 0.1830 -0.0298 0.0329  -0.0093 954  LEU B CA  
3116 C C   . LEU B 102 ? 0.2230 0.1864 0.1807 -0.0224 0.0317  -0.0065 954  LEU B C   
3117 O O   . LEU B 102 ? 0.2420 0.1921 0.1839 -0.0213 0.0280  -0.0020 954  LEU B O   
3118 C CB  . LEU B 102 ? 0.1976 0.1622 0.1723 -0.0269 0.0239  -0.0131 954  LEU B CB  
3119 C CG  . LEU B 102 ? 0.1711 0.1496 0.1492 -0.0173 0.0164  -0.0153 954  LEU B CG  
3120 C CD1 . LEU B 102 ? 0.1877 0.1908 0.1799 -0.0148 0.0173  -0.0164 954  LEU B CD1 
3121 C CD2 . LEU B 102 ? 0.1900 0.1670 0.1698 -0.0154 0.0099  -0.0213 954  LEU B CD2 
3122 N N   . ILE B 103 ? 0.2068 0.1803 0.1700 -0.0173 0.0346  -0.0094 955  ILE B N   
3123 C CA  . ILE B 103 ? 0.2116 0.1759 0.1610 -0.0144 0.0352  -0.0102 955  ILE B CA  
3124 C C   . ILE B 103 ? 0.2185 0.1847 0.1727 -0.0092 0.0281  -0.0100 955  ILE B C   
3125 O O   . ILE B 103 ? 0.1915 0.1675 0.1596 -0.0035 0.0277  -0.0093 955  ILE B O   
3126 C CB  . ILE B 103 ? 0.2116 0.1760 0.1604 -0.0124 0.0464  -0.0151 955  ILE B CB  
3127 C CG1 . ILE B 103 ? 0.2284 0.2016 0.1775 -0.0185 0.0559  -0.0153 955  ILE B CG1 
3128 C CG2 . ILE B 103 ? 0.2223 0.1715 0.1509 -0.0148 0.0481  -0.0197 955  ILE B CG2 
3129 C CD1 . ILE B 103 ? 0.2508 0.2144 0.1797 -0.0280 0.0555  -0.0094 955  ILE B CD1 
3130 N N   . MET B 104 ? 0.1901 0.1518 0.1326 -0.0118 0.0225  -0.0095 956  MET B N   
3131 C CA  . MET B 104 ? 0.1967 0.1625 0.1405 -0.0113 0.0171  -0.0084 956  MET B CA  
3132 C C   . MET B 104 ? 0.2292 0.1851 0.1589 -0.0184 0.0189  -0.0110 956  MET B C   
3133 O O   . MET B 104 ? 0.2134 0.1644 0.1305 -0.0233 0.0216  -0.0149 956  MET B O   
3134 C CB  . MET B 104 ? 0.2096 0.1889 0.1560 -0.0101 0.0086  -0.0077 956  MET B CB  
3135 C CG  . MET B 104 ? 0.1836 0.1705 0.1429 -0.0061 0.0068  -0.0091 956  MET B CG  
3136 S SD  . MET B 104 ? 0.1981 0.1893 0.1575 -0.0019 0.0002  -0.0125 956  MET B SD  
3137 C CE  . MET B 104 ? 0.2146 0.1847 0.1618 -0.0019 0.0026  -0.0076 956  MET B CE  
3138 N N   . GLU B 105 ? 0.2359 0.1897 0.1656 -0.0214 0.0176  -0.0090 957  GLU B N   
3139 C CA  . GLU B 105 ? 0.2540 0.2001 0.1699 -0.0340 0.0187  -0.0132 957  GLU B CA  
3140 C C   . GLU B 105 ? 0.2656 0.2354 0.1763 -0.0391 0.0113  -0.0156 957  GLU B C   
3141 O O   . GLU B 105 ? 0.1897 0.1775 0.1089 -0.0310 0.0050  -0.0122 957  GLU B O   
3142 C CB  . GLU B 105 ? 0.2693 0.2091 0.1847 -0.0401 0.0189  -0.0083 957  GLU B CB  
3143 C CG  . GLU B 105 ? 0.2340 0.2023 0.1580 -0.0386 0.0114  -0.0024 957  GLU B CG  
3144 C CD  . GLU B 105 ? 0.2226 0.1874 0.1429 -0.0472 0.0127  0.0052  957  GLU B CD  
3145 O OE1 . GLU B 105 ? 0.2790 0.2149 0.1887 -0.0574 0.0191  0.0057  957  GLU B OE1 
3146 O OE2 . GLU B 105 ? 0.2321 0.2214 0.1587 -0.0443 0.0082  0.0107  957  GLU B OE2 
3147 N N   . PHE B 106 ? 0.2527 0.2229 0.1495 -0.0515 0.0121  -0.0224 958  PHE B N   
3148 C CA  . PHE B 106 ? 0.1976 0.1986 0.0896 -0.0560 0.0037  -0.0238 958  PHE B CA  
3149 C C   . PHE B 106 ? 0.2059 0.2267 0.0986 -0.0704 0.0007  -0.0266 958  PHE B C   
3150 O O   . PHE B 106 ? 0.2178 0.2206 0.1018 -0.0875 0.0068  -0.0325 958  PHE B O   
3151 C CB  . PHE B 106 ? 0.2524 0.2535 0.1274 -0.0616 0.0049  -0.0297 958  PHE B CB  
3152 C CG  . PHE B 106 ? 0.1873 0.2265 0.0562 -0.0656 -0.0052 -0.0300 958  PHE B CG  
3153 C CD1 . PHE B 106 ? 0.2473 0.3097 0.1257 -0.0494 -0.0142 -0.0204 958  PHE B CD1 
3154 C CD2 . PHE B 106 ? 0.1997 0.2525 0.0532 -0.0845 -0.0057 -0.0409 958  PHE B CD2 
3155 C CE1 . PHE B 106 ? 0.2240 0.3274 0.0996 -0.0479 -0.0246 -0.0189 958  PHE B CE1 
3156 C CE2 . PHE B 106 ? 0.2364 0.3355 0.0866 -0.0873 -0.0169 -0.0406 958  PHE B CE2 
3157 C CZ  . PHE B 106 ? 0.2484 0.3745 0.1106 -0.0666 -0.0267 -0.0281 958  PHE B CZ  
3158 N N   . LEU B 107 ? 0.1981 0.2549 0.1008 -0.0643 -0.0075 -0.0233 959  LEU B N   
3159 C CA  . LEU B 107 ? 0.2185 0.3073 0.1248 -0.0788 -0.0101 -0.0260 959  LEU B CA  
3160 C C   . LEU B 107 ? 0.2274 0.3609 0.1320 -0.0809 -0.0189 -0.0303 959  LEU B C   
3161 O O   . LEU B 107 ? 0.1475 0.3104 0.0626 -0.0626 -0.0263 -0.0261 959  LEU B O   
3162 C CB  . LEU B 107 ? 0.1970 0.3034 0.1180 -0.0699 -0.0114 -0.0207 959  LEU B CB  
3163 C CG  . LEU B 107 ? 0.2019 0.2827 0.1227 -0.0757 -0.0044 -0.0150 959  LEU B CG  
3164 C CD1 . LEU B 107 ? 0.2189 0.2572 0.1372 -0.0653 0.0002  -0.0112 959  LEU B CD1 
3165 C CD2 . LEU B 107 ? 0.1818 0.2922 0.1142 -0.0678 -0.0067 -0.0116 959  LEU B CD2 
3173 N N   . SER B 109 ? 0.3151 0.3772 0.1197 -0.1037 -0.0330 -0.0384 961  SER B N   
3174 C CA  . SER B 109 ? 0.3049 0.3703 0.1298 -0.0969 -0.0485 -0.0200 961  SER B CA  
3175 C C   . SER B 109 ? 0.2938 0.3597 0.1290 -0.0855 -0.0573 0.0075  961  SER B C   
3176 O O   . SER B 109 ? 0.2790 0.3530 0.1325 -0.0821 -0.0703 0.0236  961  SER B O   
3177 C CB  . SER B 109 ? 0.2783 0.3217 0.1304 -0.0867 -0.0410 -0.0287 961  SER B CB  
3178 O OG  . SER B 109 ? 0.3176 0.3612 0.1692 -0.0987 -0.0351 -0.0512 961  SER B OG  
3179 N N   . GLY B 110 ? 0.2546 0.3113 0.0842 -0.0796 -0.0487 0.0115  962  GLY B N   
3180 C CA  . GLY B 110 ? 0.2872 0.3438 0.1278 -0.0719 -0.0545 0.0349  962  GLY B CA  
3181 C C   . GLY B 110 ? 0.2405 0.2803 0.1128 -0.0566 -0.0530 0.0389  962  GLY B C   
3182 O O   . GLY B 110 ? 0.2496 0.2767 0.1298 -0.0509 -0.0454 0.0249  962  GLY B O   
3183 N N   . SER B 111 ? 0.2600 0.3013 0.1518 -0.0513 -0.0596 0.0586  963  SER B N   
3184 C CA  . SER B 111 ? 0.1958 0.2235 0.1183 -0.0393 -0.0555 0.0593  963  SER B CA  
3185 C C   . SER B 111 ? 0.2363 0.2674 0.1797 -0.0368 -0.0608 0.0582  963  SER B C   
3186 O O   . SER B 111 ? 0.2270 0.2741 0.1686 -0.0437 -0.0720 0.0636  963  SER B O   
3187 C CB  . SER B 111 ? 0.2238 0.2487 0.1680 -0.0350 -0.0564 0.0768  963  SER B CB  
3188 O OG  . SER B 111 ? 0.2958 0.3310 0.2644 -0.0342 -0.0684 0.0973  963  SER B OG  
3189 N N   . LEU B 112 ? 0.2182 0.2374 0.1815 -0.0284 -0.0522 0.0504  964  LEU B N   
3190 C CA  . LEU B 112 ? 0.2244 0.2470 0.2145 -0.0256 -0.0537 0.0497  964  LEU B CA  
3191 C C   . LEU B 112 ? 0.2470 0.2811 0.2693 -0.0236 -0.0641 0.0683  964  LEU B C   
3192 O O   . LEU B 112 ? 0.1997 0.2456 0.2426 -0.0243 -0.0707 0.0714  964  LEU B O   
3193 C CB  . LEU B 112 ? 0.2392 0.2499 0.2424 -0.0191 -0.0402 0.0380  964  LEU B CB  
3194 C CG  . LEU B 112 ? 0.2523 0.2551 0.2354 -0.0193 -0.0310 0.0242  964  LEU B CG  
3195 C CD1 . LEU B 112 ? 0.2811 0.2799 0.2758 -0.0155 -0.0200 0.0164  964  LEU B CD1 
3196 C CD2 . LEU B 112 ? 0.2501 0.2559 0.2317 -0.0238 -0.0327 0.0206  964  LEU B CD2 
3197 N N   A LYS B 113 ? 0.2723 0.3036 0.3045 -0.0208 -0.0652 0.0823  965  LYS B N   
3198 N N   B LYS B 113 ? 0.2695 0.3009 0.3014 -0.0209 -0.0652 0.0823  965  LYS B N   
3199 C CA  A LYS B 113 ? 0.2954 0.3378 0.3632 -0.0180 -0.0765 0.1071  965  LYS B CA  
3200 C CA  B LYS B 113 ? 0.2896 0.3319 0.3573 -0.0180 -0.0763 0.1068  965  LYS B CA  
3201 C C   A LYS B 113 ? 0.2981 0.3662 0.3522 -0.0266 -0.0959 0.1225  965  LYS B C   
3202 C C   B LYS B 113 ? 0.2953 0.3633 0.3495 -0.0266 -0.0959 0.1227  965  LYS B C   
3203 O O   A LYS B 113 ? 0.3034 0.3879 0.3916 -0.0243 -0.1077 0.1381  965  LYS B O   
3204 O O   B LYS B 113 ? 0.2997 0.3841 0.3882 -0.0242 -0.1078 0.1388  965  LYS B O   
3205 C CB  A LYS B 113 ? 0.3149 0.3478 0.3926 -0.0156 -0.0734 0.1220  965  LYS B CB  
3206 C CB  B LYS B 113 ? 0.3067 0.3391 0.3853 -0.0153 -0.0728 0.1212  965  LYS B CB  
3207 C CG  A LYS B 113 ? 0.3546 0.3950 0.4779 -0.0107 -0.0834 0.1527  965  LYS B CG  
3208 C CG  B LYS B 113 ? 0.3201 0.3517 0.4566 -0.0070 -0.0748 0.1410  965  LYS B CG  
3209 C CD  A LYS B 113 ? 0.2988 0.3362 0.4789 -0.0008 -0.0779 0.1485  965  LYS B CD  
3210 C CD  B LYS B 113 ? 0.2778 0.2945 0.4287 -0.0053 -0.0676 0.1529  965  LYS B CD  
3211 C CE  A LYS B 113 ? 0.2714 0.3102 0.5108 0.0073  -0.0831 0.1782  965  LYS B CE  
3212 C CE  B LYS B 113 ? 0.3516 0.3717 0.5580 0.0013  -0.0754 0.1857  965  LYS B CE  
3213 N NZ  A LYS B 113 ? 0.1962 0.2416 0.4924 0.0159  -0.0815 0.1757  965  LYS B NZ  
3214 N NZ  B LYS B 113 ? 0.3513 0.3547 0.5748 0.0016  -0.0670 0.1994  965  LYS B NZ  
3215 N N   . GLU B 114 ? 0.3016 0.3758 0.3083 -0.0375 -0.0985 0.1164  966  GLU B N   
3216 C CA  . GLU B 114 ? 0.3481 0.4505 0.3325 -0.0506 -0.1155 0.1242  966  GLU B CA  
3217 C C   . GLU B 114 ? 0.3334 0.4429 0.3157 -0.0559 -0.1164 0.1036  966  GLU B C   
3218 O O   . GLU B 114 ? 0.3115 0.4470 0.3038 -0.0627 -0.1322 0.1120  966  GLU B O   
3219 C CB  . GLU B 114 ? 0.4109 0.5185 0.3453 -0.0630 -0.1141 0.1207  966  GLU B CB  
3220 C CG  . GLU B 114 ? 0.5266 0.6684 0.4320 -0.0810 -0.1306 0.1243  966  GLU B CG  
3221 C CD  . GLU B 114 ? 0.7224 0.8731 0.5773 -0.0962 -0.1263 0.1180  966  GLU B CD  
3222 O OE1 . GLU B 114 ? 0.7538 0.8869 0.5993 -0.0921 -0.1132 0.1182  966  GLU B OE1 
3223 O OE2 . GLU B 114 ? 0.7992 0.9773 0.6245 -0.1140 -0.1353 0.1109  966  GLU B OE2 
3224 N N   . TYR B 115 ? 0.2744 0.3622 0.2455 -0.0536 -0.0998 0.0786  967  TYR B N   
3225 C CA  . TYR B 115 ? 0.2899 0.3791 0.2541 -0.0608 -0.0967 0.0579  967  TYR B CA  
3226 C C   . TYR B 115 ? 0.2388 0.3317 0.2420 -0.0559 -0.0977 0.0576  967  TYR B C   
3227 O O   . TYR B 115 ? 0.2687 0.3778 0.2766 -0.0654 -0.1047 0.0509  967  TYR B O   
3228 C CB  . TYR B 115 ? 0.2482 0.3119 0.1919 -0.0585 -0.0781 0.0369  967  TYR B CB  
3229 C CG  . TYR B 115 ? 0.2831 0.3409 0.2247 -0.0645 -0.0709 0.0171  967  TYR B CG  
3230 C CD1 . TYR B 115 ? 0.2915 0.3563 0.2101 -0.0787 -0.0708 0.0018  967  TYR B CD1 
3231 C CD2 . TYR B 115 ? 0.2378 0.2830 0.2017 -0.0577 -0.0619 0.0125  967  TYR B CD2 
3232 C CE1 . TYR B 115 ? 0.2930 0.3488 0.2167 -0.0848 -0.0617 -0.0174 967  TYR B CE1 
3233 C CE2 . TYR B 115 ? 0.2457 0.2833 0.2113 -0.0636 -0.0539 -0.0025 967  TYR B CE2 
3234 C CZ  . TYR B 115 ? 0.2555 0.2968 0.2041 -0.0766 -0.0538 -0.0171 967  TYR B CZ  
3235 O OH  . TYR B 115 ? 0.3307 0.3605 0.2876 -0.0826 -0.0434 -0.0325 967  TYR B OH  
3236 N N   . LEU B 116 ? 0.2369 0.3164 0.2693 -0.0430 -0.0890 0.0618  968  LEU B N   
3237 C CA  . LEU B 116 ? 0.2251 0.3070 0.2953 -0.0388 -0.0845 0.0577  968  LEU B CA  
3238 C C   . LEU B 116 ? 0.2325 0.3440 0.3384 -0.0413 -0.1021 0.0728  968  LEU B C   
3239 O O   . LEU B 116 ? 0.2473 0.3705 0.3692 -0.0468 -0.1034 0.0644  968  LEU B O   
3240 C CB  . LEU B 116 ? 0.1751 0.2390 0.2671 -0.0270 -0.0685 0.0545  968  LEU B CB  
3241 C CG  . LEU B 116 ? 0.2373 0.2789 0.3008 -0.0256 -0.0516 0.0383  968  LEU B CG  
3242 C CD1 . LEU B 116 ? 0.2522 0.2841 0.3362 -0.0177 -0.0381 0.0340  968  LEU B CD1 
3243 C CD2 . LEU B 116 ? 0.2222 0.2598 0.2749 -0.0312 -0.0441 0.0252  968  LEU B CD2 
3244 N N   . PRO B 117 ? 0.2295 0.3554 0.3511 -0.0377 -0.1167 0.0973  969  PRO B N   
3245 C CA  . PRO B 117 ? 0.2691 0.4285 0.4290 -0.0395 -0.1367 0.1164  969  PRO B CA  
3246 C C   . PRO B 117 ? 0.2238 0.4117 0.3593 -0.0570 -0.1528 0.1108  969  PRO B C   
3247 O O   . PRO B 117 ? 0.2529 0.4683 0.4222 -0.0605 -0.1651 0.1155  969  PRO B O   
3248 C CB  . PRO B 117 ? 0.2819 0.4491 0.4546 -0.0335 -0.1494 0.1480  969  PRO B CB  
3249 C CG  . PRO B 117 ? 0.2668 0.3990 0.4264 -0.0252 -0.1298 0.1406  969  PRO B CG  
3250 C CD  . PRO B 117 ? 0.2840 0.3977 0.3962 -0.0318 -0.1153 0.1113  969  PRO B CD  
3251 N N   . LYS B 118 ? 0.2680 0.4503 0.3483 -0.0688 -0.1509 0.0980  970  LYS B N   
3252 C CA  . LYS B 118 ? 0.3221 0.5283 0.3739 -0.0887 -0.1616 0.0849  970  LYS B CA  
3253 C C   . LYS B 118 ? 0.2984 0.4895 0.3477 -0.0951 -0.1460 0.0537  970  LYS B C   
3254 O O   . LYS B 118 ? 0.3259 0.5363 0.3607 -0.1128 -0.1527 0.0389  970  LYS B O   
3255 C CB  . LYS B 118 ? 0.3868 0.5954 0.3840 -0.0999 -0.1638 0.0832  970  LYS B CB  
3256 C CG  . LYS B 118 ? 0.4526 0.6808 0.4486 -0.0975 -0.1809 0.1180  970  LYS B CG  
3257 C CD  . LYS B 118 ? 0.5800 0.8266 0.5196 -0.1159 -0.1875 0.1174  970  LYS B CD  
3258 C CE  . LYS B 118 ? 0.5851 0.7985 0.4920 -0.1121 -0.1663 0.1057  970  LYS B CE  
3259 N NZ  . LYS B 118 ? 0.6085 0.8448 0.4705 -0.1273 -0.1744 0.1176  970  LYS B NZ  
3260 N N   . ASN B 119 ? 0.2674 0.4263 0.3314 -0.0826 -0.1251 0.0443  971  ASN B N   
3261 C CA  . ASN B 119 ? 0.2523 0.3914 0.3116 -0.0878 -0.1075 0.0195  971  ASN B CA  
3262 C C   . ASN B 119 ? 0.2544 0.3831 0.3527 -0.0786 -0.0943 0.0178  971  ASN B C   
3263 O O   . ASN B 119 ? 0.2688 0.3762 0.3627 -0.0800 -0.0769 0.0032  971  ASN B O   
3264 C CB  . ASN B 119 ? 0.2522 0.3607 0.2720 -0.0864 -0.0917 0.0068  971  ASN B CB  
3265 C CG  . ASN B 119 ? 0.3378 0.4582 0.3194 -0.1011 -0.0991 -0.0015 971  ASN B CG  
3266 O OD1 . ASN B 119 ? 0.2734 0.4012 0.2472 -0.1168 -0.0982 -0.0209 971  ASN B OD1 
3267 N ND2 . ASN B 119 ? 0.2391 0.3623 0.1987 -0.0978 -0.1044 0.0114  971  ASN B ND2 
3268 N N   . LYS B 120 ? 0.2404 0.3860 0.3802 -0.0703 -0.1016 0.0331  972  LYS B N   
3269 C CA  . LYS B 120 ? 0.2578 0.3975 0.4373 -0.0630 -0.0865 0.0291  972  LYS B CA  
3270 C C   . LYS B 120 ? 0.2247 0.3647 0.4108 -0.0748 -0.0774 0.0120  972  LYS B C   
3271 O O   . LYS B 120 ? 0.2768 0.3975 0.4672 -0.0720 -0.0566 0.0036  972  LYS B O   
3272 C CB  . LYS B 120 ? 0.2390 0.4052 0.4747 -0.0555 -0.0975 0.0457  972  LYS B CB  
3273 C CG  . LYS B 120 ? 0.2821 0.4449 0.5280 -0.0422 -0.1025 0.0646  972  LYS B CG  
3274 C CD  . LYS B 120 ? 0.1870 0.3600 0.5007 -0.0297 -0.0985 0.0743  972  LYS B CD  
3275 C CE  . LYS B 120 ? 0.2720 0.4846 0.6329 -0.0323 -0.1199 0.0898  972  LYS B CE  
3276 N NZ  . LYS B 120 ? 0.3904 0.6126 0.8230 -0.0165 -0.1194 0.1070  972  LYS B NZ  
3277 N N   . ASN B 121 ? 0.2192 0.3830 0.4065 -0.0896 -0.0923 0.0073  973  ASN B N   
3278 C CA  . ASN B 121 ? 0.2763 0.4411 0.4761 -0.1031 -0.0833 -0.0102 973  ASN B CA  
3279 C C   . ASN B 121 ? 0.3099 0.4376 0.4764 -0.1068 -0.0626 -0.0254 973  ASN B C   
3280 O O   . ASN B 121 ? 0.3088 0.4243 0.4906 -0.1111 -0.0459 -0.0337 973  ASN B O   
3281 C CB  . ASN B 121 ? 0.2733 0.4742 0.4799 -0.1213 -0.1044 -0.0159 973  ASN B CB  
3282 C CG  . ASN B 121 ? 0.3361 0.5443 0.5726 -0.1357 -0.0960 -0.0328 973  ASN B CG  
3283 O OD1 . ASN B 121 ? 0.2169 0.4293 0.4948 -0.1305 -0.0866 -0.0297 973  ASN B OD1 
3284 N ND2 . ASN B 121 ? 0.2491 0.4594 0.4671 -0.1551 -0.0973 -0.0528 973  ASN B ND2 
3285 N N   . LYS B 122 ? 0.3102 0.4222 0.4358 -0.1054 -0.0637 -0.0270 974  LYS B N   
3286 C CA  . LYS B 122 ? 0.3693 0.4457 0.4680 -0.1045 -0.0450 -0.0367 974  LYS B CA  
3287 C C   . LYS B 122 ? 0.3472 0.3998 0.4439 -0.0897 -0.0286 -0.0273 974  LYS B C   
3288 O O   . LYS B 122 ? 0.3772 0.4065 0.4694 -0.0901 -0.0119 -0.0307 974  LYS B O   
3289 C CB  . LYS B 122 ? 0.3844 0.4540 0.4447 -0.1047 -0.0502 -0.0397 974  LYS B CB  
3290 C CG  . LYS B 122 ? 0.4714 0.5514 0.5185 -0.1232 -0.0553 -0.0587 974  LYS B CG  
3291 C CD  . LYS B 122 ? 0.4751 0.5473 0.4850 -0.1222 -0.0555 -0.0620 974  LYS B CD  
3292 C CE  . LYS B 122 ? 0.5356 0.6290 0.5273 -0.1432 -0.0633 -0.0816 974  LYS B CE  
3293 N NZ  . LYS B 122 ? 0.6725 0.8106 0.6653 -0.1528 -0.0890 -0.0714 974  LYS B NZ  
3294 N N   . ILE B 123 ? 0.3114 0.3706 0.4108 -0.0776 -0.0335 -0.0150 975  ILE B N   
3295 C CA  . ILE B 123 ? 0.2908 0.3317 0.3797 -0.0654 -0.0203 -0.0091 975  ILE B CA  
3296 C C   . ILE B 123 ? 0.2892 0.3382 0.4097 -0.0627 -0.0103 -0.0074 975  ILE B C   
3297 O O   . ILE B 123 ? 0.3081 0.3731 0.4540 -0.0572 -0.0164 -0.0025 975  ILE B O   
3298 C CB  . ILE B 123 ? 0.3007 0.3413 0.3722 -0.0558 -0.0289 -0.0011 975  ILE B CB  
3299 C CG1 . ILE B 123 ? 0.2873 0.3251 0.3292 -0.0606 -0.0379 -0.0040 975  ILE B CG1 
3300 C CG2 . ILE B 123 ? 0.3431 0.3679 0.4022 -0.0464 -0.0158 0.0011  975  ILE B CG2 
3301 C CD1 . ILE B 123 ? 0.3674 0.3843 0.3901 -0.0648 -0.0265 -0.0142 975  ILE B CD1 
3302 N N   . ASN B 124 ? 0.2324 0.2705 0.3543 -0.0672 0.0066  -0.0110 976  ASN B N   
3303 C CA  . ASN B 124 ? 0.2318 0.2770 0.3781 -0.0672 0.0218  -0.0118 976  ASN B CA  
3304 C C   . ASN B 124 ? 0.2362 0.2714 0.3609 -0.0601 0.0350  -0.0094 976  ASN B C   
3305 O O   . ASN B 124 ? 0.2183 0.2415 0.3121 -0.0544 0.0307  -0.0058 976  ASN B O   
3306 C CB  . ASN B 124 ? 0.2467 0.2894 0.4067 -0.0789 0.0339  -0.0154 976  ASN B CB  
3307 C CG  . ASN B 124 ? 0.2732 0.2900 0.4031 -0.0816 0.0449  -0.0111 976  ASN B CG  
3308 O OD1 . ASN B 124 ? 0.2348 0.2384 0.3339 -0.0739 0.0456  -0.0047 976  ASN B OD1 
3309 N ND2 . ASN B 124 ? 0.2905 0.3008 0.4344 -0.0927 0.0530  -0.0135 976  ASN B ND2 
3310 N N   . LEU B 125 ? 0.2324 0.2756 0.3737 -0.0620 0.0518  -0.0134 977  LEU B N   
3311 C CA  . LEU B 125 ? 0.2260 0.2662 0.3457 -0.0592 0.0657  -0.0153 977  LEU B CA  
3312 C C   . LEU B 125 ? 0.2351 0.2592 0.3095 -0.0601 0.0682  -0.0061 977  LEU B C   
3313 O O   . LEU B 125 ? 0.2181 0.2391 0.2671 -0.0549 0.0655  -0.0050 977  LEU B O   
3314 C CB  . LEU B 125 ? 0.2118 0.2658 0.3550 -0.0654 0.0870  -0.0240 977  LEU B CB  
3315 C CG  . LEU B 125 ? 0.2624 0.3194 0.3799 -0.0680 0.1049  -0.0302 977  LEU B CG  
3316 C CD1 . LEU B 125 ? 0.2718 0.3288 0.3861 -0.0596 0.0990  -0.0378 977  LEU B CD1 
3317 C CD2 . LEU B 125 ? 0.3355 0.4084 0.4781 -0.0768 0.1285  -0.0415 977  LEU B CD2 
3318 N N   . LYS B 126 ? 0.2474 0.2622 0.3175 -0.0668 0.0730  0.0013  978  LYS B N   
3319 C CA  . LYS B 126 ? 0.2570 0.2556 0.2950 -0.0662 0.0742  0.0148  978  LYS B CA  
3320 C C   . LYS B 126 ? 0.2479 0.2368 0.2683 -0.0569 0.0582  0.0165  978  LYS B C   
3321 O O   . LYS B 126 ? 0.2058 0.1924 0.2003 -0.0521 0.0572  0.0238  978  LYS B O   
3322 C CB  . LYS B 126 ? 0.3251 0.3113 0.3749 -0.0743 0.0816  0.0222  978  LYS B CB  
3323 C CG  . LYS B 126 ? 0.3782 0.3488 0.4048 -0.0738 0.0873  0.0413  978  LYS B CG  
3324 C CD  . LYS B 126 ? 0.4655 0.4259 0.5079 -0.0841 0.1022  0.0517  978  LYS B CD  
3325 C CE  . LYS B 126 ? 0.5230 0.4765 0.5414 -0.0843 0.1110  0.0780  978  LYS B CE  
3326 N NZ  . LYS B 126 ? 0.6080 0.5618 0.6369 -0.0970 0.1301  0.0893  978  LYS B NZ  
3327 N N   . GLN B 127 ? 0.2280 0.2155 0.2628 -0.0558 0.0456  0.0094  979  GLN B N   
3328 C CA  . GLN B 127 ? 0.2254 0.2063 0.2445 -0.0492 0.0328  0.0091  979  GLN B CA  
3329 C C   . GLN B 127 ? 0.2054 0.1952 0.2151 -0.0419 0.0276  0.0073  979  GLN B C   
3330 O O   . GLN B 127 ? 0.2161 0.2004 0.2060 -0.0365 0.0229  0.0104  979  GLN B O   
3331 C CB  . GLN B 127 ? 0.2104 0.1923 0.2419 -0.0534 0.0214  0.0011  979  GLN B CB  
3332 C CG  . GLN B 127 ? 0.2392 0.2125 0.2511 -0.0493 0.0132  -0.0001 979  GLN B CG  
3333 C CD  . GLN B 127 ? 0.2118 0.1658 0.2125 -0.0466 0.0219  0.0059  979  GLN B CD  
3334 O OE1 . GLN B 127 ? 0.2558 0.1978 0.2684 -0.0525 0.0293  0.0044  979  GLN B OE1 
3335 N NE2 . GLN B 127 ? 0.2332 0.1854 0.2163 -0.0378 0.0213  0.0135  979  GLN B NE2 
3336 N N   . GLN B 128 ? 0.1726 0.1760 0.2021 -0.0421 0.0297  0.0014  980  GLN B N   
3337 C CA  . GLN B 128 ? 0.1849 0.1941 0.2126 -0.0365 0.0289  -0.0024 980  GLN B CA  
3338 C C   . GLN B 128 ? 0.2015 0.2107 0.2020 -0.0370 0.0386  -0.0021 980  GLN B C   
3339 O O   . GLN B 128 ? 0.1869 0.1959 0.1722 -0.0332 0.0342  -0.0030 980  GLN B O   
3340 C CB  . GLN B 128 ? 0.2143 0.2364 0.2790 -0.0364 0.0333  -0.0097 980  GLN B CB  
3341 C CG  . GLN B 128 ? 0.1843 0.2137 0.2780 -0.0350 0.0188  -0.0058 980  GLN B CG  
3342 C CD  . GLN B 128 ? 0.1888 0.2333 0.3299 -0.0339 0.0241  -0.0100 980  GLN B CD  
3343 O OE1 . GLN B 128 ? 0.2593 0.3099 0.4155 -0.0389 0.0384  -0.0166 980  GLN B OE1 
3344 N NE2 . GLN B 128 ? 0.2295 0.2809 0.3979 -0.0274 0.0133  -0.0045 980  GLN B NE2 
3345 N N   . LEU B 129 ? 0.2124 0.2250 0.2064 -0.0435 0.0513  0.0001  981  LEU B N   
3346 C CA  . LEU B 129 ? 0.2341 0.2537 0.1983 -0.0469 0.0590  0.0034  981  LEU B CA  
3347 C C   . LEU B 129 ? 0.2347 0.2456 0.1747 -0.0420 0.0490  0.0182  981  LEU B C   
3348 O O   . LEU B 129 ? 0.2134 0.2328 0.1326 -0.0409 0.0460  0.0195  981  LEU B O   
3349 C CB  . LEU B 129 ? 0.2473 0.2749 0.2091 -0.0567 0.0754  0.0058  981  LEU B CB  
3350 C CG  . LEU B 129 ? 0.2519 0.2926 0.2397 -0.0621 0.0898  -0.0119 981  LEU B CG  
3351 C CD1 . LEU B 129 ? 0.3402 0.3904 0.3180 -0.0739 0.1079  -0.0080 981  LEU B CD1 
3352 C CD2 . LEU B 129 ? 0.3588 0.4104 0.3479 -0.0619 0.0942  -0.0301 981  LEU B CD2 
3353 N N   . LYS B 130 ? 0.2120 0.2073 0.1594 -0.0393 0.0439  0.0270  982  LYS B N   
3354 C CA  . LYS B 130 ? 0.2153 0.2009 0.1509 -0.0329 0.0361  0.0383  982  LYS B CA  
3355 C C   . LYS B 130 ? 0.2207 0.2072 0.1533 -0.0264 0.0253  0.0306  982  LYS B C   
3356 O O   . LYS B 130 ? 0.2204 0.2102 0.1396 -0.0220 0.0207  0.0371  982  LYS B O   
3357 C CB  . LYS B 130 ? 0.2676 0.2344 0.2176 -0.0330 0.0375  0.0449  982  LYS B CB  
3358 C CG  . LYS B 130 ? 0.2580 0.2212 0.2104 -0.0390 0.0492  0.0588  982  LYS B CG  
3359 C CD  . LYS B 130 ? 0.3903 0.3313 0.3610 -0.0388 0.0526  0.0666  982  LYS B CD  
3360 C CE  . LYS B 130 ? 0.4085 0.3426 0.4027 -0.0462 0.0550  0.0507  982  LYS B CE  
3361 N NZ  . LYS B 130 ? 0.4098 0.3232 0.4253 -0.0511 0.0649  0.0573  982  LYS B NZ  
3362 N N   . TYR B 131 ? 0.2009 0.1865 0.1475 -0.0262 0.0205  0.0193  983  TYR B N   
3363 C CA  . TYR B 131 ? 0.1825 0.1707 0.1261 -0.0217 0.0123  0.0140  983  TYR B CA  
3364 C C   . TYR B 131 ? 0.2276 0.2282 0.1617 -0.0220 0.0150  0.0098  983  TYR B C   
3365 O O   . TYR B 131 ? 0.2040 0.2073 0.1282 -0.0190 0.0101  0.0104  983  TYR B O   
3366 C CB  . TYR B 131 ? 0.2097 0.1991 0.1712 -0.0224 0.0066  0.0078  983  TYR B CB  
3367 C CG  . TYR B 131 ? 0.1951 0.1787 0.1616 -0.0249 0.0002  0.0081  983  TYR B CG  
3368 C CD1 . TYR B 131 ? 0.2386 0.2113 0.1961 -0.0254 0.0015  0.0094  983  TYR B CD1 
3369 C CD2 . TYR B 131 ? 0.2550 0.2466 0.2382 -0.0276 -0.0072 0.0064  983  TYR B CD2 
3370 C CE1 . TYR B 131 ? 0.2288 0.1985 0.1904 -0.0309 -0.0024 0.0035  983  TYR B CE1 
3371 C CE2 . TYR B 131 ? 0.2456 0.2387 0.2295 -0.0334 -0.0147 0.0045  983  TYR B CE2 
3372 C CZ  . TYR B 131 ? 0.2923 0.2743 0.2634 -0.0362 -0.0112 0.0003  983  TYR B CZ  
3373 O OH  . TYR B 131 ? 0.3338 0.3196 0.3050 -0.0450 -0.0166 -0.0071 983  TYR B OH  
3374 N N   . ALA B 132 ? 0.2119 0.2215 0.1514 -0.0273 0.0243  0.0029  984  ALA B N   
3375 C CA  . ALA B 132 ? 0.2209 0.2450 0.1509 -0.0317 0.0305  -0.0070 984  ALA B CA  
3376 C C   . ALA B 132 ? 0.2003 0.2344 0.1022 -0.0327 0.0269  0.0026  984  ALA B C   
3377 O O   . ALA B 132 ? 0.2304 0.2741 0.1242 -0.0330 0.0226  -0.0027 984  ALA B O   
3378 C CB  . ALA B 132 ? 0.1931 0.2265 0.1323 -0.0393 0.0452  -0.0173 984  ALA B CB  
3379 N N   . VAL B 133 ? 0.2143 0.2475 0.1051 -0.0337 0.0285  0.0184  985  VAL B N   
3380 C CA  . VAL B 133 ? 0.2585 0.3027 0.1283 -0.0329 0.0226  0.0351  985  VAL B CA  
3381 C C   . VAL B 133 ? 0.2285 0.2678 0.1026 -0.0237 0.0108  0.0395  985  VAL B C   
3382 O O   . VAL B 133 ? 0.2420 0.2987 0.1047 -0.0239 0.0042  0.0424  985  VAL B O   
3383 C CB  . VAL B 133 ? 0.2458 0.2834 0.1128 -0.0333 0.0264  0.0571  985  VAL B CB  
3384 C CG1 . VAL B 133 ? 0.3163 0.3642 0.1705 -0.0295 0.0179  0.0809  985  VAL B CG1 
3385 C CG2 . VAL B 133 ? 0.2497 0.2968 0.1093 -0.0447 0.0403  0.0536  985  VAL B CG2 
3386 N N   . GLN B 134 ? 0.2619 0.2808 0.1532 -0.0172 0.0086  0.0383  986  GLN B N   
3387 C CA  . GLN B 134 ? 0.2133 0.2275 0.1101 -0.0097 0.0010  0.0406  986  GLN B CA  
3388 C C   . GLN B 134 ? 0.1999 0.2248 0.0950 -0.0109 -0.0029 0.0276  986  GLN B C   
3389 O O   . GLN B 134 ? 0.2223 0.2565 0.1162 -0.0075 -0.0089 0.0308  986  GLN B O   
3390 C CB  . GLN B 134 ? 0.1997 0.1928 0.1114 -0.0066 0.0021  0.0375  986  GLN B CB  
3391 C CG  . GLN B 134 ? 0.1991 0.1788 0.1192 -0.0050 0.0069  0.0499  986  GLN B CG  
3392 C CD  . GLN B 134 ? 0.3464 0.3086 0.2800 -0.0070 0.0099  0.0405  986  GLN B CD  
3393 O OE1 . GLN B 134 ? 0.3110 0.2734 0.2446 -0.0083 0.0062  0.0285  986  GLN B OE1 
3394 N NE2 . GLN B 134 ? 0.3050 0.2541 0.2502 -0.0091 0.0167  0.0465  986  GLN B NE2 
3395 N N   . ILE B 135 ? 0.1835 0.2064 0.0846 -0.0152 0.0009  0.0137  987  ILE B N   
3396 C CA  . ILE B 135 ? 0.1870 0.2170 0.0923 -0.0176 0.0000  0.0012  987  ILE B CA  
3397 C C   . ILE B 135 ? 0.2002 0.2534 0.0914 -0.0236 -0.0003 -0.0029 987  ILE B C   
3398 O O   . ILE B 135 ? 0.1986 0.2616 0.0900 -0.0238 -0.0053 -0.0063 987  ILE B O   
3399 C CB  . ILE B 135 ? 0.1845 0.2079 0.1074 -0.0205 0.0058  -0.0103 987  ILE B CB  
3400 C CG1 . ILE B 135 ? 0.1789 0.1869 0.1141 -0.0161 0.0016  -0.0042 987  ILE B CG1 
3401 C CG2 . ILE B 135 ? 0.1708 0.2002 0.1030 -0.0242 0.0082  -0.0235 987  ILE B CG2 
3402 C CD1 . ILE B 135 ? 0.1718 0.1765 0.1295 -0.0173 0.0048  -0.0083 987  ILE B CD1 
3403 N N   . CYS B 136 ? 0.2126 0.2774 0.0908 -0.0301 0.0052  -0.0028 988  CYS B N   
3404 C CA  . CYS B 136 ? 0.2229 0.3165 0.0805 -0.0393 0.0040  -0.0058 988  CYS B CA  
3405 C C   . CYS B 136 ? 0.2316 0.3395 0.0802 -0.0342 -0.0093 0.0138  988  CYS B C   
3406 O O   . CYS B 136 ? 0.3080 0.4411 0.1486 -0.0400 -0.0155 0.0087  988  CYS B O   
3407 C CB  . CYS B 136 ? 0.2425 0.3473 0.0837 -0.0488 0.0137  -0.0064 988  CYS B CB  
3408 S SG  . CYS B 136 ? 0.2717 0.3708 0.1299 -0.0571 0.0319  -0.0351 988  CYS B SG  
3409 N N   . LYS B 137 ? 0.2449 0.3380 0.0999 -0.0240 -0.0128 0.0349  989  LYS B N   
3410 C CA  . LYS B 137 ? 0.2186 0.3223 0.0769 -0.0162 -0.0239 0.0555  989  LYS B CA  
3411 C C   . LYS B 137 ? 0.2654 0.3698 0.1397 -0.0110 -0.0295 0.0474  989  LYS B C   
3412 O O   . LYS B 137 ? 0.2463 0.3760 0.1211 -0.0110 -0.0391 0.0534  989  LYS B O   
3413 C CB  . LYS B 137 ? 0.2765 0.3609 0.1459 -0.0069 -0.0226 0.0779  989  LYS B CB  
3414 C CG  . LYS B 137 ? 0.2454 0.3358 0.0983 -0.0131 -0.0183 0.0936  989  LYS B CG  
3415 C CD  . LYS B 137 ? 0.3149 0.3821 0.1859 -0.0044 -0.0150 0.1154  989  LYS B CD  
3416 C CE  . LYS B 137 ? 0.4281 0.5032 0.2844 -0.0109 -0.0109 0.1371  989  LYS B CE  
3417 N NZ  . LYS B 137 ? 0.4590 0.5033 0.3395 -0.0043 -0.0031 0.1520  989  LYS B NZ  
3418 N N   . GLY B 138 ? 0.2423 0.3229 0.1298 -0.0078 -0.0239 0.0348  990  GLY B N   
3419 C CA  . GLY B 138 ? 0.2513 0.3336 0.1516 -0.0058 -0.0263 0.0257  990  GLY B CA  
3420 C C   . GLY B 138 ? 0.2197 0.3244 0.1156 -0.0159 -0.0282 0.0103  990  GLY B C   
3421 O O   . GLY B 138 ? 0.2132 0.3379 0.1160 -0.0163 -0.0350 0.0101  990  GLY B O   
3422 N N   . MET B 139 ? 0.2192 0.3218 0.1082 -0.0250 -0.0210 -0.0047 991  MET B N   
3423 C CA  . MET B 139 ? 0.2201 0.3419 0.1082 -0.0372 -0.0189 -0.0250 991  MET B CA  
3424 C C   . MET B 139 ? 0.2836 0.4441 0.1543 -0.0457 -0.0277 -0.0234 991  MET B C   
3425 O O   . MET B 139 ? 0.2729 0.4555 0.1483 -0.0536 -0.0318 -0.0358 991  MET B O   
3426 C CB  . MET B 139 ? 0.2340 0.3451 0.1246 -0.0448 -0.0062 -0.0426 991  MET B CB  
3427 C CG  . MET B 139 ? 0.2444 0.3252 0.1574 -0.0389 0.0003  -0.0450 991  MET B CG  
3428 S SD  . MET B 139 ? 0.2607 0.3353 0.1947 -0.0389 -0.0006 -0.0505 991  MET B SD  
3429 C CE  . MET B 139 ? 0.3013 0.3925 0.2452 -0.0544 0.0081  -0.0787 991  MET B CE  
3430 N N   . ASP B 140 ? 0.2783 0.4497 0.1295 -0.0456 -0.0310 -0.0071 992  ASP B N   
3431 C CA  . ASP B 140 ? 0.3067 0.5198 0.1378 -0.0542 -0.0421 0.0009  992  ASP B CA  
3432 C C   . ASP B 140 ? 0.2903 0.5202 0.1369 -0.0449 -0.0578 0.0191  992  ASP B C   
3433 O O   . ASP B 140 ? 0.3300 0.5975 0.1724 -0.0537 -0.0684 0.0157  992  ASP B O   
3434 C CB  . ASP B 140 ? 0.2987 0.5183 0.1062 -0.0561 -0.0415 0.0199  992  ASP B CB  
3435 C CG  . ASP B 140 ? 0.3800 0.6483 0.1579 -0.0709 -0.0511 0.0252  992  ASP B CG  
3436 O OD1 . ASP B 140 ? 0.3623 0.6551 0.1292 -0.0877 -0.0484 -0.0028 992  ASP B OD1 
3437 O OD2 . ASP B 140 ? 0.4421 0.7247 0.2092 -0.0666 -0.0610 0.0577  992  ASP B OD2 
3438 N N   . TYR B 141 ? 0.2962 0.4991 0.1642 -0.0282 -0.0578 0.0354  993  TYR B N   
3439 C CA  . TYR B 141 ? 0.2350 0.4480 0.1284 -0.0179 -0.0675 0.0476  993  TYR B CA  
3440 C C   . TYR B 141 ? 0.2537 0.4771 0.1599 -0.0249 -0.0670 0.0244  993  TYR B C   
3441 O O   . TYR B 141 ? 0.2224 0.4785 0.1395 -0.0267 -0.0783 0.0277  993  TYR B O   
3442 C CB  . TYR B 141 ? 0.2480 0.4252 0.1636 -0.0017 -0.0609 0.0590  993  TYR B CB  
3443 C CG  . TYR B 141 ? 0.2095 0.3951 0.1571 0.0093  -0.0663 0.0679  993  TYR B CG  
3444 C CD1 . TYR B 141 ? 0.2232 0.4322 0.1875 0.0182  -0.0783 0.0948  993  TYR B CD1 
3445 C CD2 . TYR B 141 ? 0.2662 0.4376 0.2306 0.0107  -0.0584 0.0511  993  TYR B CD2 
3446 C CE1 . TYR B 141 ? 0.1988 0.4162 0.2018 0.0296  -0.0812 0.1016  993  TYR B CE1 
3447 C CE2 . TYR B 141 ? 0.2212 0.4015 0.2173 0.0196  -0.0598 0.0561  993  TYR B CE2 
3448 C CZ  . TYR B 141 ? 0.1525 0.3549 0.1705 0.0296  -0.0704 0.0794  993  TYR B CZ  
3449 O OH  . TYR B 141 ? 0.2066 0.4180 0.2631 0.0390  -0.0696 0.0821  993  TYR B OH  
3450 N N   . LEU B 142 ? 0.2135 0.4089 0.1225 -0.0285 -0.0539 0.0035  994  LEU B N   
3451 C CA  . LEU B 142 ? 0.2242 0.4240 0.1483 -0.0363 -0.0504 -0.0173 994  LEU B CA  
3452 C C   . LEU B 142 ? 0.2420 0.4809 0.1571 -0.0537 -0.0562 -0.0341 994  LEU B C   
3453 O O   . LEU B 142 ? 0.2004 0.4641 0.1306 -0.0589 -0.0625 -0.0408 994  LEU B O   
3454 C CB  . LEU B 142 ? 0.2320 0.3956 0.1607 -0.0377 -0.0359 -0.0313 994  LEU B CB  
3455 C CG  . LEU B 142 ? 0.2869 0.4459 0.2354 -0.0448 -0.0292 -0.0483 994  LEU B CG  
3456 C CD1 . LEU B 142 ? 0.2640 0.4227 0.2304 -0.0370 -0.0311 -0.0389 994  LEU B CD1 
3457 C CD2 . LEU B 142 ? 0.2791 0.4058 0.2329 -0.0462 -0.0168 -0.0562 994  LEU B CD2 
3458 N N   . GLY B 143 ? 0.2690 0.5150 0.1598 -0.0643 -0.0527 -0.0431 995  GLY B N   
3459 C CA  . GLY B 143 ? 0.2788 0.5642 0.1554 -0.0846 -0.0558 -0.0638 995  GLY B CA  
3460 C C   . GLY B 143 ? 0.3214 0.6573 0.1858 -0.0881 -0.0764 -0.0465 995  GLY B C   
3461 O O   . GLY B 143 ? 0.2973 0.6730 0.1584 -0.1051 -0.0832 -0.0640 995  GLY B O   
3462 N N   . SER B 144 ? 0.3446 0.6803 0.2065 -0.0727 -0.0866 -0.0117 996  SER B N   
3463 C CA  . SER B 144 ? 0.3319 0.7136 0.1940 -0.0709 -0.1084 0.0140  996  SER B CA  
3464 C C   . SER B 144 ? 0.3211 0.7189 0.2197 -0.0658 -0.1173 0.0133  996  SER B C   
3465 O O   . SER B 144 ? 0.3206 0.7682 0.2234 -0.0709 -0.1361 0.0238  996  SER B O   
3466 C CB  . SER B 144 ? 0.3546 0.7260 0.2161 -0.0535 -0.1146 0.0540  996  SER B CB  
3467 O OG  . SER B 144 ? 0.3680 0.7072 0.2660 -0.0325 -0.1113 0.0676  996  SER B OG  
3468 N N   . ARG B 145 ? 0.3269 0.6859 0.2519 -0.0569 -0.1037 0.0018  997  ARG B N   
3469 C CA  . ARG B 145 ? 0.3010 0.6713 0.2622 -0.0537 -0.1068 -0.0030 997  ARG B CA  
3470 C C   . ARG B 145 ? 0.2771 0.6573 0.2426 -0.0734 -0.1000 -0.0383 997  ARG B C   
3471 O O   . ARG B 145 ? 0.3190 0.7041 0.3153 -0.0737 -0.0983 -0.0464 997  ARG B O   
3472 C CB  . ARG B 145 ? 0.3008 0.6276 0.2865 -0.0353 -0.0947 0.0056  997  ARG B CB  
3473 C CG  . ARG B 145 ? 0.3956 0.7074 0.3804 -0.0181 -0.0976 0.0350  997  ARG B CG  
3474 C CD  . ARG B 145 ? 0.4993 0.7899 0.5179 -0.0004 -0.0914 0.0465  997  ARG B CD  
3475 N NE  . ARG B 145 ? 0.6034 0.9125 0.6397 0.0132  -0.1040 0.0780  997  ARG B NE  
3476 C CZ  . ARG B 145 ? 0.6926 1.0369 0.7650 0.0204  -0.1164 0.0927  997  ARG B CZ  
3477 N NH1 . ARG B 145 ? 0.7587 1.1255 0.8535 0.0145  -0.1174 0.0763  997  ARG B NH1 
3478 N NH2 . ARG B 145 ? 0.7515 1.1092 0.8436 0.0342  -0.1276 0.1261  997  ARG B NH2 
3479 N N   . GLN B 146 ? 0.2330 0.6168 0.1711 -0.0907 -0.0942 -0.0600 998  GLN B N   
3480 C CA  . GLN B 146 ? 0.2934 0.6893 0.2355 -0.1129 -0.0862 -0.0972 998  GLN B CA  
3481 C C   . GLN B 146 ? 0.3120 0.6603 0.2800 -0.1104 -0.0657 -0.1134 998  GLN B C   
3482 O O   . GLN B 146 ? 0.2867 0.6434 0.2787 -0.1224 -0.0610 -0.1344 998  GLN B O   
3483 C CB  . GLN B 146 ? 0.3361 0.7915 0.2899 -0.1267 -0.1037 -0.1039 998  GLN B CB  
3484 C CG  . GLN B 146 ? 0.3660 0.8771 0.2896 -0.1339 -0.1260 -0.0874 998  GLN B CG  
3485 C CD  . GLN B 146 ? 0.4676 1.0226 0.4152 -0.1245 -0.1501 -0.0590 998  GLN B CD  
3486 O OE1 . GLN B 146 ? 0.5251 1.1153 0.4975 -0.1354 -0.1579 -0.0733 998  GLN B OE1 
3487 N NE2 . GLN B 146 ? 0.5206 1.0733 0.4672 -0.1039 -0.1610 -0.0184 998  GLN B NE2 
3488 N N   . TYR B 147 ? 0.2956 0.5970 0.2591 -0.0961 -0.0546 -0.1017 999  TYR B N   
3489 C CA  . TYR B 147 ? 0.2735 0.5300 0.2558 -0.0939 -0.0364 -0.1115 999  TYR B CA  
3490 C C   . TYR B 147 ? 0.2683 0.4983 0.2395 -0.0979 -0.0230 -0.1238 999  TYR B C   
3491 O O   . TYR B 147 ? 0.2844 0.5154 0.2304 -0.0941 -0.0258 -0.1151 999  TYR B O   
3492 C CB  . TYR B 147 ? 0.2594 0.4854 0.2500 -0.0745 -0.0346 -0.0871 999  TYR B CB  
3493 C CG  . TYR B 147 ? 0.1522 0.3975 0.1631 -0.0687 -0.0420 -0.0767 999  TYR B CG  
3494 C CD1 . TYR B 147 ? 0.2143 0.4632 0.2517 -0.0768 -0.0356 -0.0891 999  TYR B CD1 
3495 C CD2 . TYR B 147 ? 0.3285 0.5871 0.3374 -0.0546 -0.0536 -0.0536 999  TYR B CD2 
3496 C CE1 . TYR B 147 ? 0.1671 0.4371 0.2278 -0.0717 -0.0408 -0.0807 999  TYR B CE1 
3497 C CE2 . TYR B 147 ? 0.2491 0.5267 0.2845 -0.0480 -0.0587 -0.0448 999  TYR B CE2 
3498 C CZ  . TYR B 147 ? 0.2223 0.5069 0.2829 -0.0567 -0.0522 -0.0592 999  TYR B CZ  
3499 O OH  . TYR B 147 ? 0.2674 0.5724 0.3582 -0.0501 -0.0552 -0.0515 999  TYR B OH  
3500 N N   . VAL B 148 ? 0.2274 0.4323 0.2227 -0.1046 -0.0075 -0.1417 1000 VAL B N   
3501 C CA  . VAL B 148 ? 0.2529 0.4240 0.2539 -0.1038 0.0076  -0.1492 1000 VAL B CA  
3502 C C   . VAL B 148 ? 0.2320 0.3643 0.2494 -0.0894 0.0125  -0.1285 1000 VAL B C   
3503 O O   . VAL B 148 ? 0.2150 0.3425 0.2510 -0.0896 0.0138  -0.1244 1000 VAL B O   
3504 C CB  . VAL B 148 ? 0.3134 0.4853 0.3371 -0.1232 0.0237  -0.1855 1000 VAL B CB  
3505 C CG1 . VAL B 148 ? 0.4163 0.6277 0.4150 -0.1394 0.0204  -0.2075 1000 VAL B CG1 
3506 C CG2 . VAL B 148 ? 0.2917 0.4629 0.3495 -0.1326 0.0292  -0.1976 1000 VAL B CG2 
3507 N N   . HIS B 149 ? 0.2019 0.3110 0.2105 -0.0786 0.0145  -0.1151 1001 HIS B N   
3508 C CA  . HIS B 149 ? 0.2060 0.2846 0.2236 -0.0666 0.0162  -0.0938 1001 HIS B CA  
3509 C C   . HIS B 149 ? 0.2051 0.2579 0.2570 -0.0701 0.0293  -0.0981 1001 HIS B C   
3510 O O   . HIS B 149 ? 0.2076 0.2458 0.2721 -0.0670 0.0307  -0.0833 1001 HIS B O   
3511 C CB  . HIS B 149 ? 0.2027 0.2703 0.2016 -0.0559 0.0126  -0.0795 1001 HIS B CB  
3512 C CG  . HIS B 149 ? 0.1957 0.2409 0.1965 -0.0457 0.0109  -0.0582 1001 HIS B CG  
3513 N ND1 . HIS B 149 ? 0.1983 0.2214 0.2189 -0.0439 0.0168  -0.0522 1001 HIS B ND1 
3514 C CD2 . HIS B 149 ? 0.1896 0.2343 0.1759 -0.0382 0.0040  -0.0422 1001 HIS B CD2 
3515 C CE1 . HIS B 149 ? 0.1710 0.1842 0.1835 -0.0372 0.0117  -0.0324 1001 HIS B CE1 
3516 N NE2 . HIS B 149 ? 0.1677 0.1927 0.1585 -0.0343 0.0055  -0.0288 1001 HIS B NE2 
3517 N N   . ARG B 150 ? 0.2119 0.2589 0.2800 -0.0760 0.0398  -0.1163 1002 ARG B N   
3518 C CA  . ARG B 150 ? 0.2288 0.2520 0.3406 -0.0799 0.0546  -0.1232 1002 ARG B CA  
3519 C C   . ARG B 150 ? 0.2487 0.2440 0.3769 -0.0672 0.0544  -0.0958 1002 ARG B C   
3520 O O   . ARG B 150 ? 0.2819 0.2564 0.4510 -0.0681 0.0647  -0.0927 1002 ARG B O   
3521 C CB  . ARG B 150 ? 0.2304 0.2551 0.3668 -0.0910 0.0609  -0.1333 1002 ARG B CB  
3522 C CG  . ARG B 150 ? 0.2575 0.3157 0.3811 -0.1053 0.0583  -0.1593 1002 ARG B CG  
3523 C CD  . ARG B 150 ? 0.3498 0.4093 0.5019 -0.1165 0.0644  -0.1676 1002 ARG B CD  
3524 N NE  . ARG B 150 ? 0.4312 0.4574 0.6311 -0.1193 0.0818  -0.1686 1002 ARG B NE  
3525 C CZ  . ARG B 150 ? 0.5200 0.5278 0.7456 -0.1191 0.0869  -0.1510 1002 ARG B CZ  
3526 N NH1 . ARG B 150 ? 0.4065 0.4258 0.6146 -0.1170 0.0780  -0.1336 1002 ARG B NH1 
3527 N NH2 . ARG B 150 ? 0.5381 0.5153 0.8120 -0.1216 0.1033  -0.1505 1002 ARG B NH2 
3528 N N   . ASP B 151 ? 0.2315 0.2277 0.3308 -0.0563 0.0425  -0.0751 1003 ASP B N   
3529 C CA  . ASP B 151 ? 0.2294 0.2071 0.3392 -0.0466 0.0389  -0.0489 1003 ASP B CA  
3530 C C   . ASP B 151 ? 0.2197 0.2017 0.3042 -0.0383 0.0298  -0.0397 1003 ASP B C   
3531 O O   . ASP B 151 ? 0.2133 0.1906 0.2866 -0.0318 0.0206  -0.0173 1003 ASP B O   
3532 C CB  . ASP B 151 ? 0.2470 0.2212 0.3492 -0.0459 0.0334  -0.0271 1003 ASP B CB  
3533 C CG  . ASP B 151 ? 0.3103 0.2677 0.4329 -0.0409 0.0317  0.0005  1003 ASP B CG  
3534 O OD1 . ASP B 151 ? 0.3078 0.2529 0.4665 -0.0380 0.0372  0.0018  1003 ASP B OD1 
3535 O OD2 . ASP B 151 ? 0.2915 0.2503 0.3957 -0.0406 0.0252  0.0215  1003 ASP B OD2 
3536 N N   . LEU B 152 ? 0.2178 0.2102 0.2927 -0.0405 0.0332  -0.0580 1004 LEU B N   
3537 C CA  . LEU B 152 ? 0.2314 0.2286 0.2827 -0.0346 0.0265  -0.0509 1004 LEU B CA  
3538 C C   . LEU B 152 ? 0.2511 0.2359 0.3312 -0.0289 0.0295  -0.0430 1004 LEU B C   
3539 O O   . LEU B 152 ? 0.2198 0.2012 0.3309 -0.0313 0.0419  -0.0581 1004 LEU B O   
3540 C CB  . LEU B 152 ? 0.2259 0.2419 0.2532 -0.0403 0.0288  -0.0684 1004 LEU B CB  
3541 C CG  . LEU B 152 ? 0.2299 0.2485 0.2364 -0.0350 0.0240  -0.0591 1004 LEU B CG  
3542 C CD1 . LEU B 152 ? 0.2475 0.2623 0.2333 -0.0273 0.0115  -0.0380 1004 LEU B CD1 
3543 C CD2 . LEU B 152 ? 0.2344 0.2732 0.2171 -0.0424 0.0274  -0.0727 1004 LEU B CD2 
3544 N N   . ALA B 153 ? 0.2229 0.2038 0.2947 -0.0222 0.0183  -0.0205 1005 ALA B N   
3545 C CA  . ALA B 153 ? 0.2123 0.1866 0.3123 -0.0163 0.0157  -0.0062 1005 ALA B CA  
3546 C C   . ALA B 153 ? 0.1901 0.1698 0.2619 -0.0132 0.0017  0.0107  1005 ALA B C   
3547 O O   . ALA B 153 ? 0.1622 0.1453 0.2008 -0.0150 -0.0039 0.0134  1005 ALA B O   
3548 C CB  . ALA B 153 ? 0.2177 0.1808 0.3533 -0.0149 0.0164  0.0089  1005 ALA B CB  
3549 N N   . ALA B 154 ? 0.1870 0.1690 0.2752 -0.0096 -0.0026 0.0189  1006 ALA B N   
3550 C CA  . ALA B 154 ? 0.1966 0.1859 0.2612 -0.0094 -0.0149 0.0302  1006 ALA B CA  
3551 C C   . ALA B 154 ? 0.2096 0.2012 0.2547 -0.0118 -0.0261 0.0477  1006 ALA B C   
3552 O O   . ALA B 154 ? 0.2028 0.1993 0.2153 -0.0150 -0.0316 0.0473  1006 ALA B O   
3553 C CB  . ALA B 154 ? 0.2072 0.2022 0.3007 -0.0064 -0.0184 0.0366  1006 ALA B CB  
3554 N N   . ARG B 155 ? 0.2356 0.2233 0.3016 -0.0114 -0.0270 0.0617  1007 ARG B N   
3555 C CA  . ARG B 155 ? 0.2331 0.2250 0.2787 -0.0159 -0.0349 0.0791  1007 ARG B CA  
3556 C C   . ARG B 155 ? 0.2296 0.2205 0.2391 -0.0204 -0.0297 0.0668  1007 ARG B C   
3557 O O   . ARG B 155 ? 0.2336 0.2316 0.2172 -0.0258 -0.0348 0.0754  1007 ARG B O   
3558 C CB  . ARG B 155 ? 0.2469 0.2329 0.3263 -0.0148 -0.0347 0.0995  1007 ARG B CB  
3559 C CG  . ARG B 155 ? 0.2713 0.2430 0.3703 -0.0150 -0.0198 0.0865  1007 ARG B CG  
3560 C CD  . ARG B 155 ? 0.3469 0.3087 0.4909 -0.0133 -0.0174 0.1081  1007 ARG B CD  
3561 N NE  . ARG B 155 ? 0.3741 0.3213 0.5506 -0.0134 -0.0002 0.0861  1007 ARG B NE  
3562 C CZ  . ARG B 155 ? 0.3800 0.3224 0.5470 -0.0199 0.0096  0.0712  1007 ARG B CZ  
3563 N NH1 . ARG B 155 ? 0.4793 0.4281 0.6094 -0.0255 0.0054  0.0782  1007 ARG B NH1 
3564 N NH2 . ARG B 155 ? 0.5329 0.4659 0.7310 -0.0221 0.0248  0.0473  1007 ARG B NH2 
3565 N N   . ASN B 156 ? 0.1727 0.1584 0.1822 -0.0190 -0.0197 0.0471  1008 ASN B N   
3566 C CA  . ASN B 156 ? 0.2244 0.2130 0.2076 -0.0214 -0.0158 0.0361  1008 ASN B CA  
3567 C C   . ASN B 156 ? 0.2051 0.1976 0.1664 -0.0195 -0.0163 0.0249  1008 ASN B C   
3568 O O   . ASN B 156 ? 0.1840 0.1798 0.1331 -0.0194 -0.0130 0.0169  1008 ASN B O   
3569 C CB  . ASN B 156 ? 0.1939 0.1799 0.1923 -0.0230 -0.0068 0.0250  1008 ASN B CB  
3570 C CG  . ASN B 156 ? 0.2151 0.1954 0.2322 -0.0266 -0.0041 0.0373  1008 ASN B CG  
3571 O OD1 . ASN B 156 ? 0.2307 0.2132 0.2348 -0.0294 -0.0087 0.0540  1008 ASN B OD1 
3572 N ND2 . ASN B 156 ? 0.2148 0.1882 0.2623 -0.0282 0.0045  0.0290  1008 ASN B ND2 
3573 N N   . VAL B 157 ? 0.1881 0.1808 0.1494 -0.0178 -0.0203 0.0259  1009 VAL B N   
3574 C CA  . VAL B 157 ? 0.1657 0.1591 0.1111 -0.0165 -0.0195 0.0183  1009 VAL B CA  
3575 C C   . VAL B 157 ? 0.1965 0.1920 0.1283 -0.0203 -0.0252 0.0229  1009 VAL B C   
3576 O O   . VAL B 157 ? 0.2067 0.2062 0.1463 -0.0226 -0.0320 0.0305  1009 VAL B O   
3577 C CB  . VAL B 157 ? 0.1924 0.1854 0.1488 -0.0145 -0.0171 0.0135  1009 VAL B CB  
3578 C CG1 . VAL B 157 ? 0.1761 0.1679 0.1180 -0.0139 -0.0160 0.0104  1009 VAL B CG1 
3579 C CG2 . VAL B 157 ? 0.2100 0.2048 0.1766 -0.0142 -0.0098 0.0044  1009 VAL B CG2 
3580 N N   . LEU B 158 ? 0.2121 0.2070 0.1272 -0.0215 -0.0220 0.0167  1010 LEU B N   
3581 C CA  . LEU B 158 ? 0.2052 0.2029 0.1059 -0.0280 -0.0239 0.0141  1010 LEU B CA  
3582 C C   . LEU B 158 ? 0.1974 0.1898 0.1007 -0.0277 -0.0221 0.0067  1010 LEU B C   
3583 O O   . LEU B 158 ? 0.1993 0.1848 0.1098 -0.0213 -0.0172 0.0048  1010 LEU B O   
3584 C CB  . LEU B 158 ? 0.1983 0.1969 0.0859 -0.0305 -0.0166 0.0070  1010 LEU B CB  
3585 C CG  . LEU B 158 ? 0.2015 0.2062 0.0847 -0.0336 -0.0160 0.0140  1010 LEU B CG  
3586 C CD1 . LEU B 158 ? 0.2540 0.2602 0.1314 -0.0342 -0.0054 0.0038  1010 LEU B CD1 
3587 C CD2 . LEU B 158 ? 0.2821 0.2970 0.1542 -0.0431 -0.0241 0.0259  1010 LEU B CD2 
3588 N N   . VAL B 159 ? 0.1890 0.1866 0.0855 -0.0362 -0.0260 0.0032  1011 VAL B N   
3589 C CA  . VAL B 159 ? 0.2453 0.2376 0.1466 -0.0391 -0.0230 -0.0059 1011 VAL B CA  
3590 C C   . VAL B 159 ? 0.2747 0.2618 0.1667 -0.0439 -0.0136 -0.0206 1011 VAL B C   
3591 O O   . VAL B 159 ? 0.2216 0.2192 0.0977 -0.0550 -0.0146 -0.0281 1011 VAL B O   
3592 C CB  . VAL B 159 ? 0.2453 0.2502 0.1510 -0.0475 -0.0335 -0.0035 1011 VAL B CB  
3593 C CG1 . VAL B 159 ? 0.2555 0.2551 0.1688 -0.0529 -0.0290 -0.0152 1011 VAL B CG1 
3594 C CG2 . VAL B 159 ? 0.2617 0.2706 0.1861 -0.0411 -0.0396 0.0096  1011 VAL B CG2 
3595 N N   . GLU B 160 ? 0.2278 0.2005 0.1315 -0.0364 -0.0037 -0.0242 1012 GLU B N   
3596 C CA  . GLU B 160 ? 0.3010 0.2642 0.2098 -0.0385 0.0089  -0.0389 1012 GLU B CA  
3597 C C   . GLU B 160 ? 0.3095 0.2681 0.2239 -0.0494 0.0125  -0.0529 1012 GLU B C   
3598 O O   . GLU B 160 ? 0.2951 0.2541 0.2057 -0.0597 0.0208  -0.0723 1012 GLU B O   
3599 C CB  . GLU B 160 ? 0.2481 0.1988 0.1757 -0.0250 0.0162  -0.0318 1012 GLU B CB  
3600 C CG  . GLU B 160 ? 0.3524 0.2887 0.3005 -0.0231 0.0310  -0.0431 1012 GLU B CG  
3601 C CD  . GLU B 160 ? 0.4431 0.3841 0.3864 -0.0297 0.0406  -0.0617 1012 GLU B CD  
3602 O OE1 . GLU B 160 ? 0.3428 0.2969 0.2716 -0.0295 0.0369  -0.0588 1012 GLU B OE1 
3603 O OE2 . GLU B 160 ? 0.4246 0.3560 0.3806 -0.0362 0.0541  -0.0811 1012 GLU B OE2 
3604 N N   . SER B 161 ? 0.2869 0.2423 0.2116 -0.0484 0.0079  -0.0452 1013 SER B N   
3605 C CA  . SER B 161 ? 0.2831 0.2359 0.2179 -0.0593 0.0100  -0.0565 1013 SER B CA  
3606 C C   . SER B 161 ? 0.2728 0.2311 0.2155 -0.0575 0.0014  -0.0432 1013 SER B C   
3607 O O   . SER B 161 ? 0.2643 0.2250 0.2057 -0.0474 -0.0029 -0.0279 1013 SER B O   
3608 C CB  . SER B 161 ? 0.3327 0.2621 0.2909 -0.0565 0.0262  -0.0636 1013 SER B CB  
3609 O OG  . SER B 161 ? 0.3241 0.2425 0.2949 -0.0430 0.0279  -0.0432 1013 SER B OG  
3610 N N   . GLU B 162 ? 0.2898 0.2501 0.2446 -0.0678 0.0013  -0.0511 1014 GLU B N   
3611 C CA  . GLU B 162 ? 0.2832 0.2492 0.2514 -0.0660 -0.0035 -0.0398 1014 GLU B CA  
3612 C C   . GLU B 162 ? 0.2451 0.1949 0.2219 -0.0541 0.0061  -0.0259 1014 GLU B C   
3613 O O   . GLU B 162 ? 0.3163 0.2726 0.2988 -0.0509 0.0042  -0.0161 1014 GLU B O   
3614 C CB  . GLU B 162 ? 0.3485 0.3215 0.3324 -0.0804 -0.0044 -0.0516 1014 GLU B CB  
3615 C CG  . GLU B 162 ? 0.4193 0.3714 0.4241 -0.0832 0.0108  -0.0567 1014 GLU B CG  
3616 C CD  . GLU B 162 ? 0.4548 0.4190 0.4781 -0.0986 0.0081  -0.0679 1014 GLU B CD  
3617 O OE1 . GLU B 162 ? 0.4019 0.3787 0.4203 -0.1133 0.0033  -0.0871 1014 GLU B OE1 
3618 O OE2 . GLU B 162 ? 0.4573 0.4220 0.4990 -0.0973 0.0108  -0.0585 1014 GLU B OE2 
3619 N N   . HIS B 163 ? 0.2357 0.1675 0.2146 -0.0483 0.0165  -0.0248 1015 HIS B N   
3620 C CA  . HIS B 163 ? 0.2290 0.1499 0.2135 -0.0383 0.0235  -0.0076 1015 HIS B CA  
3621 C C   . HIS B 163 ? 0.2306 0.1560 0.2014 -0.0266 0.0200  0.0034  1015 HIS B C   
3622 O O   . HIS B 163 ? 0.2315 0.1545 0.2033 -0.0199 0.0231  0.0189  1015 HIS B O   
3623 C CB  . HIS B 163 ? 0.3209 0.2198 0.3265 -0.0389 0.0369  -0.0076 1015 HIS B CB  
3624 C CG  . HIS B 163 ? 0.3639 0.2575 0.3867 -0.0525 0.0423  -0.0210 1015 HIS B CG  
3625 N ND1 . HIS B 163 ? 0.4024 0.3017 0.4324 -0.0580 0.0424  -0.0152 1015 HIS B ND1 
3626 C CD2 . HIS B 163 ? 0.4239 0.3100 0.4591 -0.0636 0.0484  -0.0428 1015 HIS B CD2 
3627 C CE1 . HIS B 163 ? 0.4102 0.3060 0.4584 -0.0714 0.0470  -0.0312 1015 HIS B CE1 
3628 N NE2 . HIS B 163 ? 0.4804 0.3683 0.5307 -0.0758 0.0505  -0.0492 1015 HIS B NE2 
3629 N N   . GLN B 164 ? 0.2309 0.1655 0.1889 -0.0256 0.0133  -0.0034 1016 GLN B N   
3630 C CA  . GLN B 164 ? 0.2437 0.1832 0.1931 -0.0162 0.0110  0.0044  1016 GLN B CA  
3631 C C   . GLN B 164 ? 0.1922 0.1454 0.1277 -0.0175 0.0025  0.0004  1016 GLN B C   
3632 O O   . GLN B 164 ? 0.1965 0.1538 0.1262 -0.0246 -0.0004 -0.0092 1016 GLN B O   
3633 C CB  . GLN B 164 ? 0.2181 0.1473 0.1781 -0.0110 0.0183  0.0023  1016 GLN B CB  
3634 C CG  . GLN B 164 ? 0.2488 0.1861 0.2073 -0.0008 0.0157  0.0123  1016 GLN B CG  
3635 C CD  . GLN B 164 ? 0.3099 0.2383 0.2888 0.0054  0.0242  0.0098  1016 GLN B CD  
3636 O OE1 . GLN B 164 ? 0.3689 0.2826 0.3626 0.0016  0.0341  -0.0016 1016 GLN B OE1 
3637 N NE2 . GLN B 164 ? 0.3801 0.3187 0.3638 0.0142  0.0213  0.0185  1016 GLN B NE2 
3638 N N   . VAL B 165 ? 0.1931 0.1547 0.1234 -0.0122 -0.0008 0.0081  1017 VAL B N   
3639 C CA  . VAL B 165 ? 0.1866 0.1580 0.1096 -0.0126 -0.0066 0.0063  1017 VAL B CA  
3640 C C   . VAL B 165 ? 0.2113 0.1870 0.1321 -0.0066 -0.0056 0.0089  1017 VAL B C   
3641 O O   . VAL B 165 ? 0.1866 0.1622 0.1114 -0.0011 -0.0032 0.0154  1017 VAL B O   
3642 C CB  . VAL B 165 ? 0.2115 0.1903 0.1387 -0.0140 -0.0101 0.0086  1017 VAL B CB  
3643 C CG1 . VAL B 165 ? 0.2055 0.1852 0.1414 -0.0195 -0.0129 0.0072  1017 VAL B CG1 
3644 C CG2 . VAL B 165 ? 0.2444 0.2268 0.1717 -0.0115 -0.0057 0.0119  1017 VAL B CG2 
3645 N N   . LYS B 166 ? 0.2010 0.1828 0.1175 -0.0080 -0.0081 0.0062  1018 LYS B N   
3646 C CA  . LYS B 166 ? 0.2172 0.2064 0.1350 -0.0042 -0.0074 0.0068  1018 LYS B CA  
3647 C C   . LYS B 166 ? 0.2105 0.2063 0.1275 -0.0075 -0.0102 0.0059  1018 LYS B C   
3648 O O   . LYS B 166 ? 0.1907 0.1845 0.1057 -0.0122 -0.0121 0.0068  1018 LYS B O   
3649 C CB  . LYS B 166 ? 0.2025 0.1899 0.1222 -0.0035 -0.0023 0.0017  1018 LYS B CB  
3650 C CG  . LYS B 166 ? 0.1466 0.1230 0.0745 -0.0015 0.0041  -0.0014 1018 LYS B CG  
3651 C CD  . LYS B 166 ? 0.1870 0.1642 0.1265 0.0017  0.0126  -0.0080 1018 LYS B CD  
3652 C CE  . LYS B 166 ? 0.2551 0.2182 0.2112 0.0034  0.0227  -0.0144 1018 LYS B CE  
3653 N NZ  . LYS B 166 ? 0.2515 0.2146 0.2273 0.0070  0.0345  -0.0238 1018 LYS B NZ  
3654 N N   A ILE B 167 ? 0.1923 0.1977 0.1132 -0.0061 -0.0107 0.0052  1019 ILE B N   
3655 N N   B ILE B 167 ? 0.2026 0.2080 0.1234 -0.0060 -0.0107 0.0052  1019 ILE B N   
3656 C CA  A ILE B 167 ? 0.1789 0.1889 0.1054 -0.0100 -0.0105 0.0021  1019 ILE B CA  
3657 C CA  B ILE B 167 ? 0.1966 0.2070 0.1231 -0.0099 -0.0105 0.0020  1019 ILE B CA  
3658 C C   A ILE B 167 ? 0.1788 0.1890 0.1042 -0.0117 -0.0082 0.0026  1019 ILE B C   
3659 C C   B ILE B 167 ? 0.1895 0.1996 0.1147 -0.0117 -0.0082 0.0027  1019 ILE B C   
3660 O O   A ILE B 167 ? 0.1561 0.1718 0.0829 -0.0087 -0.0058 0.0008  1019 ILE B O   
3661 O O   B ILE B 167 ? 0.1676 0.1827 0.0940 -0.0087 -0.0057 0.0009  1019 ILE B O   
3662 C CB  A ILE B 167 ? 0.1818 0.2056 0.1128 -0.0113 -0.0107 -0.0035 1019 ILE B CB  
3663 C CB  B ILE B 167 ? 0.2125 0.2373 0.1435 -0.0109 -0.0108 -0.0033 1019 ILE B CB  
3664 C CG1 A ILE B 167 ? 0.2089 0.2363 0.1354 -0.0122 -0.0106 -0.0054 1019 ILE B CG1 
3665 C CG1 B ILE B 167 ? 0.2534 0.2842 0.1790 -0.0115 -0.0115 -0.0046 1019 ILE B CG1 
3666 C CG2 A ILE B 167 ? 0.1308 0.1552 0.0738 -0.0170 -0.0078 -0.0095 1019 ILE B CG2 
3667 C CG2 B ILE B 167 ? 0.1945 0.2201 0.1372 -0.0169 -0.0080 -0.0095 1019 ILE B CG2 
3668 C CD1 A ILE B 167 ? 0.1626 0.2105 0.0840 -0.0147 -0.0128 -0.0088 1019 ILE B CD1 
3669 C CD1 B ILE B 167 ? 0.2759 0.2979 0.2063 -0.0146 -0.0079 -0.0085 1019 ILE B CD1 
3670 N N   . GLY B 168 ? 0.1487 0.1545 0.0739 -0.0167 -0.0083 0.0067  1020 GLY B N   
3671 C CA  . GLY B 168 ? 0.1644 0.1712 0.0808 -0.0213 -0.0054 0.0092  1020 GLY B CA  
3672 C C   . GLY B 168 ? 0.1788 0.1894 0.1008 -0.0265 -0.0016 0.0126  1020 GLY B C   
3673 O O   . GLY B 168 ? 0.1598 0.1737 0.0710 -0.0320 0.0026  0.0149  1020 GLY B O   
3674 N N   . ASP B 169 ? 0.1923 0.2031 0.1312 -0.0265 -0.0011 0.0113  1021 ASP B N   
3675 C CA  . ASP B 169 ? 0.2242 0.2368 0.1748 -0.0325 0.0042  0.0138  1021 ASP B CA  
3676 C C   . ASP B 169 ? 0.1639 0.1821 0.1332 -0.0329 0.0061  0.0022  1021 ASP B C   
3677 O O   . ASP B 169 ? 0.2021 0.2191 0.1761 -0.0306 0.0034  -0.0040 1021 ASP B O   
3678 C CB  . ASP B 169 ? 0.2026 0.2060 0.1592 -0.0366 0.0030  0.0295  1021 ASP B CB  
3679 C CG  . ASP B 169 ? 0.2629 0.2657 0.2317 -0.0439 0.0101  0.0367  1021 ASP B CG  
3680 O OD1 . ASP B 169 ? 0.2372 0.2454 0.1896 -0.0497 0.0132  0.0453  1021 ASP B OD1 
3681 O OD2 . ASP B 169 ? 0.2191 0.2163 0.2149 -0.0455 0.0142  0.0329  1021 ASP B OD2 
3682 N N   . PHE B 170 ? 0.1631 0.1903 0.1424 -0.0376 0.0115  -0.0024 1022 PHE B N   
3683 C CA  . PHE B 170 ? 0.1917 0.2309 0.1884 -0.0411 0.0125  -0.0163 1022 PHE B CA  
3684 C C   . PHE B 170 ? 0.1859 0.2225 0.2048 -0.0507 0.0210  -0.0174 1022 PHE B C   
3685 O O   . PHE B 170 ? 0.1750 0.2267 0.2090 -0.0564 0.0233  -0.0298 1022 PHE B O   
3686 C CB  . PHE B 170 ? 0.1684 0.2282 0.1613 -0.0369 0.0087  -0.0223 1022 PHE B CB  
3687 C CG  . PHE B 170 ? 0.1639 0.2243 0.1416 -0.0282 0.0015  -0.0197 1022 PHE B CG  
3688 C CD1 . PHE B 170 ? 0.1625 0.2131 0.1267 -0.0223 0.0019  -0.0118 1022 PHE B CD1 
3689 C CD2 . PHE B 170 ? 0.1503 0.2213 0.1264 -0.0282 -0.0045 -0.0259 1022 PHE B CD2 
3690 C CE1 . PHE B 170 ? 0.2100 0.2580 0.1647 -0.0153 -0.0029 -0.0090 1022 PHE B CE1 
3691 C CE2 . PHE B 170 ? 0.2067 0.2771 0.1689 -0.0211 -0.0099 -0.0200 1022 PHE B CE2 
3692 C CZ  . PHE B 170 ? 0.1854 0.2424 0.1396 -0.0142 -0.0088 -0.0110 1022 PHE B CZ  
3693 N N   . GLY B 171 ? 0.1643 0.1832 0.1885 -0.0531 0.0249  -0.0032 1023 GLY B N   
3694 C CA  . GLY B 171 ? 0.1903 0.2025 0.2372 -0.0622 0.0344  0.0024  1023 GLY B CA  
3695 C C   . GLY B 171 ? 0.1782 0.1904 0.2577 -0.0696 0.0407  -0.0156 1023 GLY B C   
3696 O O   . GLY B 171 ? 0.1986 0.2125 0.2992 -0.0790 0.0496  -0.0186 1023 GLY B O   
3697 N N   . LEU B 172 ? 0.1988 0.2097 0.2830 -0.0673 0.0380  -0.0294 1024 LEU B N   
3698 C CA  . LEU B 172 ? 0.1981 0.2112 0.3116 -0.0769 0.0457  -0.0532 1024 LEU B CA  
3699 C C   . LEU B 172 ? 0.2449 0.2867 0.3451 -0.0805 0.0394  -0.0765 1024 LEU B C   
3700 O O   . LEU B 172 ? 0.2171 0.2675 0.3351 -0.0914 0.0448  -0.1005 1024 LEU B O   
3701 C CB  . LEU B 172 ? 0.2337 0.2265 0.3676 -0.0747 0.0508  -0.0549 1024 LEU B CB  
3702 C CG  . LEU B 172 ? 0.3048 0.2710 0.4638 -0.0713 0.0560  -0.0297 1024 LEU B CG  
3703 C CD1 . LEU B 172 ? 0.3243 0.2743 0.5187 -0.0699 0.0641  -0.0396 1024 LEU B CD1 
3704 C CD2 . LEU B 172 ? 0.3526 0.3108 0.5366 -0.0803 0.0656  -0.0209 1024 LEU B CD2 
3705 N N   . THR B 173 ? 0.2149 0.2733 0.2862 -0.0727 0.0284  -0.0694 1025 THR B N   
3706 C CA  . THR B 173 ? 0.2284 0.3173 0.2871 -0.0745 0.0193  -0.0832 1025 THR B CA  
3707 C C   . THR B 173 ? 0.2429 0.3581 0.3207 -0.0869 0.0200  -0.0998 1025 THR B C   
3708 O O   . THR B 173 ? 0.2005 0.3171 0.2931 -0.0891 0.0242  -0.0945 1025 THR B O   
3709 C CB  . THR B 173 ? 0.1771 0.2738 0.2091 -0.0612 0.0084  -0.0670 1025 THR B CB  
3710 O OG1 . THR B 173 ? 0.2017 0.2773 0.2181 -0.0529 0.0078  -0.0562 1025 THR B OG1 
3711 C CG2 . THR B 173 ? 0.2245 0.3541 0.2461 -0.0617 -0.0029 -0.0736 1025 THR B CG2 
3712 N N   . LYS B 174 ? 0.2383 0.3764 0.3164 -0.0975 0.0171  -0.1220 1026 LYS B N   
3713 C CA  . LYS B 174 ? 0.2685 0.4364 0.3660 -0.1133 0.0168  -0.1433 1026 LYS B CA  
3714 C C   . LYS B 174 ? 0.2625 0.4741 0.3394 -0.1171 0.0008  -0.1511 1026 LYS B C   
3715 O O   . LYS B 174 ? 0.2403 0.4546 0.2914 -0.1141 -0.0040 -0.1502 1026 LYS B O   
3716 C CB  . LYS B 174 ? 0.2686 0.4231 0.3930 -0.1296 0.0324  -0.1693 1026 LYS B CB  
3717 C CG  . LYS B 174 ? 0.2636 0.3789 0.4183 -0.1287 0.0482  -0.1597 1026 LYS B CG  
3718 C CD  . LYS B 174 ? 0.2805 0.4037 0.4567 -0.1347 0.0514  -0.1556 1026 LYS B CD  
3719 C CE  . LYS B 174 ? 0.2749 0.3600 0.4782 -0.1347 0.0672  -0.1400 1026 LYS B CE  
3720 N NZ  . LYS B 174 ? 0.2454 0.3407 0.4706 -0.1437 0.0731  -0.1381 1026 LYS B NZ  
3721 N N   . ALA B 175 ? 0.2763 0.5245 0.3659 -0.1240 -0.0079 -0.1561 1027 ALA B N   
3722 C CA  . ALA B 175 ? 0.2692 0.5673 0.3433 -0.1302 -0.0259 -0.1613 1027 ALA B CA  
3723 C C   . ALA B 175 ? 0.2899 0.6064 0.3600 -0.1532 -0.0217 -0.1955 1027 ALA B C   
3724 O O   . ALA B 175 ? 0.3015 0.6037 0.3982 -0.1673 -0.0061 -0.2195 1027 ALA B O   
3725 C CB  . ALA B 175 ? 0.2903 0.6251 0.3865 -0.1308 -0.0370 -0.1559 1027 ALA B CB  
3726 N N   . ILE B 176 ? 0.3075 0.6536 0.3449 -0.1574 -0.0335 -0.1972 1028 ILE B N   
3727 C CA  . ILE B 176 ? 0.3855 0.7664 0.4133 -0.1833 -0.0327 -0.2321 1028 ILE B CA  
3728 C C   . ILE B 176 ? 0.4575 0.8990 0.4904 -0.1948 -0.0531 -0.2346 1028 ILE B C   
3729 O O   . ILE B 176 ? 0.4966 0.9641 0.5191 -0.1813 -0.0734 -0.2040 1028 ILE B O   
3730 C CB  . ILE B 176 ? 0.4234 0.8156 0.4081 -0.1856 -0.0361 -0.2318 1028 ILE B CB  
3731 C CG1 . ILE B 176 ? 0.4088 0.7463 0.3936 -0.1766 -0.0153 -0.2336 1028 ILE B CG1 
3732 C CG2 . ILE B 176 ? 0.4553 0.8965 0.4241 -0.2160 -0.0375 -0.2689 1028 ILE B CG2 
3733 C CD1 . ILE B 176 ? 0.4527 0.8006 0.3990 -0.1815 -0.0136 -0.2379 1028 ILE B CD1 
3734 N N   . GLU B 177 ? 0.5211 0.9873 0.5736 -0.2202 -0.0479 -0.2711 1029 GLU B N   
3735 C CA  . GLU B 177 ? 0.5769 1.1098 0.6353 -0.2352 -0.0692 -0.2772 1029 GLU B CA  
3736 C C   . GLU B 177 ? 0.6129 1.2019 0.6260 -0.2426 -0.0922 -0.2692 1029 GLU B C   
3737 O O   . GLU B 177 ? 0.6418 1.2280 0.6204 -0.2526 -0.0846 -0.2840 1029 GLU B O   
3738 C CB  . GLU B 177 ? 0.6062 1.1537 0.6951 -0.2649 -0.0566 -0.3236 1029 GLU B CB  
3739 C CG  . GLU B 177 ? 0.6544 1.1617 0.7935 -0.2593 -0.0396 -0.3239 1029 GLU B CG  
3740 C CD  . GLU B 177 ? 0.7515 1.2611 0.9262 -0.2887 -0.0216 -0.3703 1029 GLU B CD  
3741 O OE1 . GLU B 177 ? 0.7895 1.3508 0.9553 -0.3164 -0.0289 -0.4044 1029 GLU B OE1 
3742 O OE2 . GLU B 177 ? 0.8098 1.2701 1.0225 -0.2852 0.0002  -0.3720 1029 GLU B OE2 
3743 N N   . THR B 178 ? 0.6271 1.2682 0.6426 -0.2375 -0.1197 -0.2434 1030 THR B N   
3744 C CA  . THR B 178 ? 0.6651 1.3681 0.6404 -0.2456 -0.1455 -0.2290 1030 THR B CA  
3745 C C   . THR B 178 ? 0.6952 1.4467 0.6509 -0.2844 -0.1450 -0.2761 1030 THR B C   
3746 O O   . THR B 178 ? 0.6969 1.4589 0.6849 -0.3040 -0.1371 -0.3120 1030 THR B O   
3747 C CB  . THR B 178 ? 0.6749 1.4286 0.6698 -0.2327 -0.1762 -0.1910 1030 THR B CB  
3748 O OG1 . THR B 178 ? 0.6378 1.3439 0.6551 -0.1982 -0.1721 -0.1534 1030 THR B OG1 
3749 C CG2 . THR B 178 ? 0.7068 1.5220 0.6582 -0.2383 -0.2045 -0.1654 1030 THR B CG2 
3750 N N   . ASP B 179 ? 0.7444 1.5238 0.6475 -0.2968 -0.1509 -0.2773 1031 ASP B N   
3751 C CA  . ASP B 179 ? 0.7870 1.6086 0.6607 -0.3362 -0.1448 -0.3273 1031 ASP B CA  
3752 C C   . ASP B 179 ? 0.7854 1.5505 0.6755 -0.3490 -0.1055 -0.3783 1031 ASP B C   
3753 O O   . ASP B 179 ? 0.8422 1.6362 0.7268 -0.3834 -0.0946 -0.4298 1031 ASP B O   
3754 C CB  . ASP B 179 ? 0.8022 1.7034 0.6876 -0.3629 -0.1680 -0.3455 1031 ASP B CB  
3755 C CG  . ASP B 179 ? 0.8142 1.7749 0.6940 -0.3491 -0.2081 -0.2923 1031 ASP B CG  
3756 O OD1 . ASP B 179 ? 0.8177 1.7831 0.6610 -0.3334 -0.2210 -0.2504 1031 ASP B OD1 
3757 O OD2 . ASP B 179 ? 0.8085 1.8114 0.7260 -0.3537 -0.2261 -0.2914 1031 ASP B OD2 
3758 N N   . LYS B 180 ? 0.7390 1.4262 0.6514 -0.3221 -0.0846 -0.3637 1032 LYS B N   
3759 C CA  . LYS B 180 ? 0.7110 1.3397 0.6451 -0.3280 -0.0483 -0.4014 1032 LYS B CA  
3760 C C   . LYS B 180 ? 0.6719 1.2469 0.5885 -0.3027 -0.0369 -0.3746 1032 LYS B C   
3761 O O   . LYS B 180 ? 0.6671 1.2333 0.5713 -0.2761 -0.0532 -0.3263 1032 LYS B O   
3762 C CB  . LYS B 180 ? 0.6802 1.2672 0.6759 -0.3230 -0.0334 -0.4121 1032 LYS B CB  
3763 C CG  . LYS B 180 ? 0.7012 1.3369 0.7240 -0.3476 -0.0426 -0.4389 1032 LYS B CG  
3764 C CD  . LYS B 180 ? 0.7925 1.4607 0.8108 -0.3883 -0.0282 -0.5011 1032 LYS B CD  
3765 C CE  . LYS B 180 ? 0.7966 1.4012 0.8593 -0.3953 0.0114  -0.5401 1032 LYS B CE  
3766 N NZ  . LYS B 180 ? 0.8472 1.4837 0.9162 -0.4371 0.0282  -0.6067 1032 LYS B NZ  
3767 N N   . GLU B 181 ? 0.6613 1.2015 0.5824 -0.3115 -0.0078 -0.4074 1033 GLU B N   
3768 C CA  . GLU B 181 ? 0.6491 1.1473 0.5530 -0.2928 0.0043  -0.3888 1033 GLU B CA  
3769 C C   . GLU B 181 ? 0.5947 1.0178 0.5442 -0.2702 0.0253  -0.3807 1033 GLU B C   
3770 O O   . GLU B 181 ? 0.5910 0.9800 0.5309 -0.2508 0.0306  -0.3577 1033 GLU B O   
3771 C CB  . GLU B 181 ? 0.6776 1.1977 0.5496 -0.3182 0.0213  -0.4275 1033 GLU B CB  
3772 C CG  . GLU B 181 ? 0.7730 1.3688 0.5851 -0.3382 -0.0017 -0.4235 1033 GLU B CG  
3773 C CD  . GLU B 181 ? 0.8093 1.4257 0.5823 -0.3621 0.0171  -0.4569 1033 GLU B CD  
3774 O OE1 . GLU B 181 ? 0.8300 1.4232 0.6296 -0.3781 0.0491  -0.5074 1033 GLU B OE1 
3775 O OE2 . GLU B 181 ? 0.8341 1.4902 0.5519 -0.3655 0.0014  -0.4324 1033 GLU B OE2 
3776 N N   . PTR B 182 ? 0.5649 0.9648 0.5640 -0.2738 0.0365  -0.3977 1034 PTR B N   
3777 C CA  . PTR B 182 ? 0.5056 0.8387 0.5485 -0.2532 0.0538  -0.3840 1034 PTR B CA  
3778 C C   . PTR B 182 ? 0.4733 0.7907 0.5561 -0.2470 0.0508  -0.3716 1034 PTR B C   
3779 O O   . PTR B 182 ? 0.4954 0.8517 0.5825 -0.2616 0.0396  -0.3829 1034 PTR B O   
3780 C CB  . PTR B 182 ? 0.5436 0.8446 0.6182 -0.2648 0.0860  -0.4230 1034 PTR B CB  
3781 C CG  . PTR B 182 ? 0.5742 0.8924 0.6798 -0.2964 0.1032  -0.4773 1034 PTR B CG  
3782 C CD1 . PTR B 182 ? 0.6427 1.0062 0.7208 -0.3258 0.1092  -0.5214 1034 PTR B CD1 
3783 C CD2 . PTR B 182 ? 0.5486 0.8361 0.7124 -0.2987 0.1163  -0.4862 1034 PTR B CD2 
3784 C CE1 . PTR B 182 ? 0.6921 1.0720 0.8001 -0.3576 0.1272  -0.5769 1034 PTR B CE1 
3785 C CE2 . PTR B 182 ? 0.6457 0.9458 0.8437 -0.3289 0.1346  -0.5384 1034 PTR B CE2 
3786 C CZ  . PTR B 182 ? 0.6987 1.0454 0.8695 -0.3588 0.1400  -0.5859 1034 PTR B CZ  
3787 O OH  . PTR B 182 ? 0.7599 1.1164 0.9644 -0.3873 0.1583  -0.6362 1034 PTR B OH  
3788 P P   . PTR B 182 ? 0.8256 1.2594 1.0032 -0.4255 0.1448  -0.6776 1034 PTR B P   
3789 O O1P . PTR B 182 ? 0.8356 1.3045 0.9935 -0.4150 0.1080  -0.6354 1034 PTR B O1P 
3790 O O2P . PTR B 182 ? 0.7947 1.2149 1.0351 -0.4530 0.1735  -0.7328 1034 PTR B O2P 
3791 O O3P . PTR B 182 ? 0.7283 1.2134 0.8419 -0.4446 0.1415  -0.7016 1034 PTR B O3P 
3792 N N   . PTR B 183 ? 0.4229 0.6860 0.5335 -0.2259 0.0604  -0.3468 1035 PTR B N   
3793 C CA  . PTR B 183 ? 0.3983 0.6371 0.5500 -0.2211 0.0648  -0.3356 1035 PTR B CA  
3794 C C   . PTR B 183 ? 0.4263 0.6210 0.6286 -0.2280 0.0935  -0.3580 1035 PTR B C   
3795 O O   . PTR B 183 ? 0.4107 0.5750 0.6175 -0.2192 0.1057  -0.3566 1035 PTR B O   
3796 C CB  . PTR B 183 ? 0.3700 0.5822 0.5128 -0.1928 0.0543  -0.2867 1035 PTR B CB  
3797 C CG  . PTR B 183 ? 0.3465 0.5310 0.5281 -0.1887 0.0622  -0.2728 1035 PTR B CG  
3798 C CD1 . PTR B 183 ? 0.2846 0.4182 0.4950 -0.1790 0.0785  -0.2591 1035 PTR B CD1 
3799 C CD2 . PTR B 183 ? 0.4174 0.6292 0.6083 -0.1949 0.0533  -0.2711 1035 PTR B CD2 
3800 C CE1 . PTR B 183 ? 0.4055 0.5161 0.6481 -0.1773 0.0862  -0.2429 1035 PTR B CE1 
3801 C CE2 . PTR B 183 ? 0.4300 0.6182 0.6552 -0.1934 0.0631  -0.2585 1035 PTR B CE2 
3802 C CZ  . PTR B 183 ? 0.4294 0.5662 0.6779 -0.1850 0.0797  -0.2433 1035 PTR B CZ  
3803 O OH  . PTR B 183 ? 0.4199 0.5341 0.6964 -0.1843 0.0894  -0.2277 1035 PTR B OH  
3804 P P   . PTR B 183 ? 0.5131 0.6471 0.8120 -0.1947 0.0904  -0.2272 1035 PTR B P   
3805 O O1P . PTR B 183 ? 0.4430 0.5353 0.7813 -0.1967 0.1104  -0.2105 1035 PTR B O1P 
3806 O O2P . PTR B 183 ? 0.4148 0.5880 0.7331 -0.2189 0.0901  -0.2679 1035 PTR B O2P 
3807 O O3P . PTR B 183 ? 0.4689 0.6253 0.7350 -0.1797 0.0731  -0.2019 1035 PTR B O3P 
3808 N N   . THR B 184 ? 0.4467 0.6376 0.6923 -0.2433 0.1047  -0.3772 1036 THR B N   
3809 C CA  . THR B 184 ? 0.4794 0.6265 0.7840 -0.2507 0.1336  -0.3970 1036 THR B CA  
3810 C C   . THR B 184 ? 0.4634 0.5625 0.8000 -0.2314 0.1387  -0.3559 1036 THR B C   
3811 O O   . THR B 184 ? 0.4280 0.5323 0.7730 -0.2319 0.1326  -0.3400 1036 THR B O   
3812 C CB  . THR B 184 ? 0.5189 0.6869 0.8588 -0.2819 0.1465  -0.4444 1036 THR B CB  
3813 O OG1 . THR B 184 ? 0.5898 0.8089 0.8942 -0.3029 0.1405  -0.4832 1036 THR B OG1 
3814 C CG2 . THR B 184 ? 0.5747 0.6939 0.9839 -0.2898 0.1795  -0.4666 1036 THR B CG2 
3815 N N   . VAL B 185 ? 0.4841 0.5398 0.8418 -0.2166 0.1511  -0.3403 1037 VAL B N   
3816 C CA  . VAL B 185 ? 0.5002 0.5136 0.8829 -0.1981 0.1537  -0.2961 1037 VAL B CA  
3817 C C   . VAL B 185 ? 0.5318 0.5160 0.9813 -0.2102 0.1757  -0.3033 1037 VAL B C   
3818 O O   . VAL B 185 ? 0.5641 0.5374 1.0588 -0.2259 0.1974  -0.3413 1037 VAL B O   
3819 C CB  . VAL B 185 ? 0.5117 0.4932 0.9002 -0.1788 0.1578  -0.2755 1037 VAL B CB  
3820 C CG1 . VAL B 185 ? 0.5200 0.4644 0.9312 -0.1615 0.1574  -0.2268 1037 VAL B CG1 
3821 C CG2 . VAL B 185 ? 0.5232 0.5293 0.8501 -0.1673 0.1386  -0.2668 1037 VAL B CG2 
3822 N N   . LYS B 186 ? 0.5165 0.4868 0.9732 -0.2032 0.1719  -0.2666 1038 LYS B N   
3823 C CA  . LYS B 186 ? 0.5599 0.4976 1.0795 -0.2119 0.1923  -0.2607 1038 LYS B CA  
3824 C C   . LYS B 186 ? 0.5623 0.4570 1.1027 -0.1922 0.1955  -0.2099 1038 LYS B C   
3825 O O   . LYS B 186 ? 0.6112 0.4695 1.2115 -0.1923 0.2150  -0.2096 1038 LYS B O   
3826 C CB  . LYS B 186 ? 0.5539 0.5146 1.0700 -0.2247 0.1882  -0.2600 1038 LYS B CB  
3827 C CG  . LYS B 186 ? 0.5843 0.5921 1.0902 -0.2470 0.1841  -0.3092 1038 LYS B CG  
3828 C CD  . LYS B 186 ? 0.5722 0.6268 1.0104 -0.2386 0.1560  -0.3030 1038 LYS B CD  
3829 C CE  . LYS B 186 ? 0.5612 0.6678 0.9875 -0.2606 0.1486  -0.3487 1038 LYS B CE  
3830 N NZ  . LYS B 186 ? 0.4639 0.6125 0.8275 -0.2495 0.1211  -0.3378 1038 LYS B NZ  
3831 N N   . ASP B 187 ? 0.5185 0.4194 1.0129 -0.1763 0.1769  -0.1676 1039 ASP B N   
3832 C CA  . ASP B 187 ? 0.5195 0.3890 1.0230 -0.1590 0.1752  -0.1173 1039 ASP B CA  
3833 C C   . ASP B 187 ? 0.5111 0.3767 0.9972 -0.1422 0.1661  -0.1120 1039 ASP B C   
3834 O O   . ASP B 187 ? 0.4581 0.3499 0.8877 -0.1352 0.1488  -0.1159 1039 ASP B O   
3835 C CB  . ASP B 187 ? 0.5430 0.4240 1.0036 -0.1533 0.1615  -0.0785 1039 ASP B CB  
3836 C CG  . ASP B 187 ? 0.5828 0.4397 1.0437 -0.1384 0.1569  -0.0259 1039 ASP B CG  
3837 O OD1 . ASP B 187 ? 0.5989 0.4236 1.1156 -0.1372 0.1699  -0.0091 1039 ASP B OD1 
3838 O OD2 . ASP B 187 ? 0.5573 0.4295 0.9646 -0.1289 0.1402  -0.0005 1039 ASP B OD2 
3839 N N   . ASP B 188 ? 0.5156 0.3484 1.0558 -0.1356 0.1788  -0.1019 1040 ASP B N   
3840 C CA  . ASP B 188 ? 0.4800 0.3086 1.0189 -0.1212 0.1746  -0.1021 1040 ASP B CA  
3841 C C   . ASP B 188 ? 0.4868 0.2852 1.0671 -0.1044 0.1748  -0.0565 1040 ASP B C   
3842 O O   . ASP B 188 ? 0.4787 0.2719 1.0744 -0.0931 0.1746  -0.0582 1040 ASP B O   
3843 C CB  . ASP B 188 ? 0.4680 0.2987 1.0374 -0.1330 0.1930  -0.1577 1040 ASP B CB  
3844 C CG  . ASP B 188 ? 0.5389 0.3406 1.1894 -0.1467 0.2213  -0.1781 1040 ASP B CG  
3845 O OD1 . ASP B 188 ? 0.4386 0.2165 1.1254 -0.1465 0.2268  -0.1460 1040 ASP B OD1 
3846 O OD2 . ASP B 188 ? 0.5529 0.3567 1.2311 -0.1597 0.2396  -0.2284 1040 ASP B OD2 
3847 N N   . ARG B 189 ? 0.5208 0.3038 1.1167 -0.1033 0.1738  -0.0138 1041 ARG B N   
3848 C CA  . ARG B 189 ? 0.5646 0.3214 1.2071 -0.0898 0.1733  0.0359  1041 ARG B CA  
3849 C C   . ARG B 189 ? 0.5632 0.3334 1.1692 -0.0718 0.1508  0.0641  1041 ARG B C   
3850 O O   . ARG B 189 ? 0.5515 0.3066 1.2061 -0.0592 0.1522  0.0818  1041 ARG B O   
3851 C CB  . ARG B 189 ? 0.5773 0.3242 1.2241 -0.0947 0.1728  0.0810  1041 ARG B CB  
3852 C CG  . ARG B 189 ? 0.6324 0.3631 1.3243 -0.1127 0.1960  0.0610  1041 ARG B CG  
3853 C CD  . ARG B 189 ? 0.6670 0.3824 1.3751 -0.1155 0.1977  0.1165  1041 ARG B CD  
3854 N NE  . ARG B 189 ? 0.6557 0.4007 1.2849 -0.1197 0.1814  0.1340  1041 ARG B NE  
3855 C CZ  . ARG B 189 ? 0.6466 0.4102 1.2460 -0.1349 0.1861  0.1068  1041 ARG B CZ  
3856 N NH1 . ARG B 189 ? 0.6491 0.4084 1.2858 -0.1494 0.2041  0.0600  1041 ARG B NH1 
3857 N NH2 . ARG B 189 ? 0.6360 0.4255 1.1698 -0.1366 0.1730  0.1249  1041 ARG B NH2 
3858 N N   . ASP B 190 ? 0.5302 0.3295 1.0566 -0.0711 0.1311  0.0666  1042 ASP B N   
3859 C CA  . ASP B 190 ? 0.5087 0.3237 0.9949 -0.0573 0.1095  0.0900  1042 ASP B CA  
3860 C C   . ASP B 190 ? 0.4819 0.3158 0.9325 -0.0553 0.1055  0.0497  1042 ASP B C   
3861 O O   . ASP B 190 ? 0.4922 0.3466 0.8856 -0.0501 0.0877  0.0573  1042 ASP B O   
3862 C CB  . ASP B 190 ? 0.5243 0.3571 0.9489 -0.0587 0.0919  0.1241  1042 ASP B CB  
3863 C CG  . ASP B 190 ? 0.6068 0.4254 1.0566 -0.0649 0.0977  0.1631  1042 ASP B CG  
3864 O OD1 . ASP B 190 ? 0.6046 0.4003 1.1178 -0.0598 0.1043  0.1899  1042 ASP B OD1 
3865 O OD2 . ASP B 190 ? 0.6964 0.5273 1.1055 -0.0750 0.0967  0.1681  1042 ASP B OD2 
3866 N N   . SER B 191 ? 0.4527 0.2803 0.9374 -0.0610 0.1232  0.0068  1043 SER B N   
3867 C CA  . SER B 191 ? 0.4373 0.2845 0.8893 -0.0613 0.1214  -0.0302 1043 SER B CA  
3868 C C   . SER B 191 ? 0.4031 0.2512 0.8599 -0.0461 0.1123  -0.0134 1043 SER B C   
3869 O O   . SER B 191 ? 0.4249 0.2535 0.9424 -0.0375 0.1185  0.0065  1043 SER B O   
3870 C CB  . SER B 191 ? 0.4472 0.2892 0.9387 -0.0736 0.1451  -0.0801 1043 SER B CB  
3871 O OG  . SER B 191 ? 0.4731 0.3184 0.9636 -0.0900 0.1533  -0.1008 1043 SER B OG  
3872 N N   . PRO B 192 ? 0.3749 0.2457 0.7739 -0.0427 0.0981  -0.0196 1044 PRO B N   
3873 C CA  . PRO B 192 ? 0.3478 0.2230 0.7512 -0.0309 0.0913  -0.0109 1044 PRO B CA  
3874 C C   . PRO B 192 ? 0.3159 0.1891 0.7536 -0.0342 0.1114  -0.0514 1044 PRO B C   
3875 O O   . PRO B 192 ? 0.2815 0.1730 0.6811 -0.0378 0.1111  -0.0766 1044 PRO B O   
3876 C CB  . PRO B 192 ? 0.3322 0.2306 0.6606 -0.0298 0.0721  -0.0062 1044 PRO B CB  
3877 C CG  . PRO B 192 ? 0.3495 0.2591 0.6431 -0.0419 0.0763  -0.0341 1044 PRO B CG  
3878 C CD  . PRO B 192 ? 0.3854 0.2795 0.7163 -0.0497 0.0881  -0.0338 1044 PRO B CD  
3879 N N   . VAL B 193 ? 0.3341 0.1848 0.8468 -0.0336 0.1305  -0.0568 1045 VAL B N   
3880 C CA  . VAL B 193 ? 0.3552 0.2015 0.9097 -0.0409 0.1567  -0.1029 1045 VAL B CA  
3881 C C   . VAL B 193 ? 0.3314 0.1912 0.8816 -0.0352 0.1589  -0.1170 1045 VAL B C   
3882 O O   . VAL B 193 ? 0.3502 0.2211 0.8926 -0.0466 0.1758  -0.1611 1045 VAL B O   
3883 C CB  . VAL B 193 ? 0.3838 0.1984 1.0343 -0.0389 0.1790  -0.1023 1045 VAL B CB  
3884 C CG1 . VAL B 193 ? 0.4236 0.2248 1.0819 -0.0498 0.1839  -0.1003 1045 VAL B CG1 
3885 C CG2 . VAL B 193 ? 0.4055 0.2067 1.1091 -0.0188 0.1695  -0.0530 1045 VAL B CG2 
3886 N N   . PHE B 194 ? 0.3383 0.2008 0.8909 -0.0197 0.1419  -0.0799 1046 PHE B N   
3887 C CA  . PHE B 194 ? 0.3289 0.2055 0.8809 -0.0142 0.1434  -0.0898 1046 PHE B CA  
3888 C C   . PHE B 194 ? 0.2950 0.1973 0.7628 -0.0217 0.1329  -0.1050 1046 PHE B C   
3889 O O   . PHE B 194 ? 0.2608 0.1756 0.7233 -0.0208 0.1376  -0.1180 1046 PHE B O   
3890 C CB  . PHE B 194 ? 0.3292 0.2032 0.9201 0.0037  0.1280  -0.0453 1046 PHE B CB  
3891 C CG  . PHE B 194 ? 0.3927 0.2425 1.0784 0.0125  0.1406  -0.0294 1046 PHE B CG  
3892 C CD1 . PHE B 194 ? 0.3730 0.2107 1.1314 0.0119  0.1708  -0.0637 1046 PHE B CD1 
3893 C CD2 . PHE B 194 ? 0.3559 0.1953 1.0603 0.0203  0.1241  0.0194  1046 PHE B CD2 
3894 C CE1 . PHE B 194 ? 0.4311 0.2433 1.2878 0.0212  0.1850  -0.0490 1046 PHE B CE1 
3895 C CE2 . PHE B 194 ? 0.4480 0.2637 1.2455 0.0291  0.1359  0.0390  1046 PHE B CE2 
3896 C CZ  . PHE B 194 ? 0.4493 0.2498 1.3271 0.0306  0.1664  0.0052  1046 PHE B CZ  
3897 N N   . TRP B 195 ? 0.2823 0.1922 0.6911 -0.0294 0.1209  -0.1030 1047 TRP B N   
3898 C CA  . TRP B 195 ? 0.2512 0.1844 0.5873 -0.0372 0.1127  -0.1174 1047 TRP B CA  
3899 C C   . TRP B 195 ? 0.2430 0.1873 0.5610 -0.0549 0.1270  -0.1580 1047 TRP B C   
3900 O O   . TRP B 195 ? 0.2370 0.2037 0.4991 -0.0624 0.1209  -0.1694 1047 TRP B O   
3901 C CB  . TRP B 195 ? 0.2630 0.2014 0.5482 -0.0325 0.0878  -0.0850 1047 TRP B CB  
3902 C CG  . TRP B 195 ? 0.2611 0.2021 0.5382 -0.0206 0.0715  -0.0546 1047 TRP B CG  
3903 C CD1 . TRP B 195 ? 0.2377 0.1934 0.4680 -0.0194 0.0604  -0.0512 1047 TRP B CD1 
3904 C CD2 . TRP B 195 ? 0.2347 0.1656 0.5534 -0.0096 0.0639  -0.0230 1047 TRP B CD2 
3905 N NE1 . TRP B 195 ? 0.2725 0.2283 0.5116 -0.0101 0.0473  -0.0240 1047 TRP B NE1 
3906 C CE2 . TRP B 195 ? 0.3071 0.2507 0.5982 -0.0039 0.0474  -0.0051 1047 TRP B CE2 
3907 C CE3 . TRP B 195 ? 0.3394 0.2533 0.7189 -0.0045 0.0689  -0.0061 1047 TRP B CE3 
3908 C CZ2 . TRP B 195 ? 0.2119 0.1566 0.5305 0.0054  0.0338  0.0275  1047 TRP B CZ2 
3909 C CZ3 . TRP B 195 ? 0.2700 0.1840 0.6781 0.0066  0.0547  0.0315  1047 TRP B CZ3 
3910 C CH2 . TRP B 195 ? 0.2636 0.1955 0.6384 0.0108  0.0362  0.0472  1047 TRP B CH2 
3911 N N   . TYR B 196 ? 0.2899 0.2203 0.6581 -0.0624 0.1462  -0.1796 1048 TYR B N   
3912 C CA  . TYR B 196 ? 0.3016 0.2438 0.6549 -0.0816 0.1567  -0.2159 1048 TYR B CA  
3913 C C   . TYR B 196 ? 0.3471 0.3019 0.7126 -0.0973 0.1817  -0.2656 1048 TYR B C   
3914 O O   . TYR B 196 ? 0.3561 0.2957 0.7799 -0.0945 0.2028  -0.2800 1048 TYR B O   
3915 C CB  . TYR B 196 ? 0.3267 0.2468 0.7247 -0.0842 0.1627  -0.2110 1048 TYR B CB  
3916 C CG  . TYR B 196 ? 0.2879 0.2128 0.6470 -0.0834 0.1423  -0.1846 1048 TYR B CG  
3917 C CD1 . TYR B 196 ? 0.2179 0.1568 0.5195 -0.0742 0.1184  -0.1558 1048 TYR B CD1 
3918 C CD2 . TYR B 196 ? 0.3264 0.2408 0.7122 -0.0926 0.1494  -0.1897 1048 TYR B CD2 
3919 C CE1 . TYR B 196 ? 0.2168 0.1609 0.4884 -0.0741 0.1038  -0.1362 1048 TYR B CE1 
3920 C CE2 . TYR B 196 ? 0.2891 0.2099 0.6424 -0.0927 0.1332  -0.1669 1048 TYR B CE2 
3921 C CZ  . TYR B 196 ? 0.3018 0.2380 0.5982 -0.0830 0.1109  -0.1409 1048 TYR B CZ  
3922 O OH  . TYR B 196 ? 0.3920 0.3355 0.6593 -0.0829 0.0978  -0.1213 1048 TYR B OH  
3923 N N   . ALA B 197 ? 0.3560 0.3414 0.6676 -0.1146 0.1796  -0.2917 1049 ALA B N   
3924 C CA  . ALA B 197 ? 0.3816 0.3874 0.6912 -0.1348 0.2025  -0.3417 1049 ALA B CA  
3925 C C   . ALA B 197 ? 0.4199 0.4102 0.7932 -0.1487 0.2299  -0.3807 1049 ALA B C   
3926 O O   . ALA B 197 ? 0.3887 0.3586 0.7936 -0.1462 0.2271  -0.3687 1049 ALA B O   
3927 C CB  . ALA B 197 ? 0.3979 0.4454 0.6317 -0.1509 0.1889  -0.3532 1049 ALA B CB  
3928 N N   . PRO B 198 ? 0.4540 0.4527 0.8496 -0.1645 0.2590  -0.4288 1050 PRO B N   
3929 C CA  . PRO B 198 ? 0.4777 0.4619 0.9381 -0.1806 0.2897  -0.4741 1050 PRO B CA  
3930 C C   . PRO B 198 ? 0.4514 0.4467 0.8989 -0.1996 0.2852  -0.4924 1050 PRO B C   
3931 O O   . PRO B 198 ? 0.4549 0.4201 0.9656 -0.1995 0.2973  -0.4958 1050 PRO B O   
3932 C CB  . PRO B 198 ? 0.5570 0.5646 1.0123 -0.1999 0.3178  -0.5269 1050 PRO B CB  
3933 C CG  . PRO B 198 ? 0.4805 0.4953 0.9058 -0.1835 0.3071  -0.4975 1050 PRO B CG  
3934 C CD  . PRO B 198 ? 0.4918 0.5133 0.8571 -0.1688 0.2677  -0.4442 1050 PRO B CD  
3935 N N   . GLU B 199 ? 0.4477 0.4868 0.8185 -0.2156 0.2677  -0.5016 1051 GLU B N   
3936 C CA  . GLU B 199 ? 0.5013 0.5593 0.8579 -0.2344 0.2601  -0.5183 1051 GLU B CA  
3937 C C   . GLU B 199 ? 0.4669 0.4968 0.8467 -0.2176 0.2429  -0.4747 1051 GLU B C   
3938 O O   . GLU B 199 ? 0.5088 0.5317 0.9230 -0.2307 0.2512  -0.4927 1051 GLU B O   
3939 C CB  . GLU B 199 ? 0.5199 0.6355 0.7901 -0.2518 0.2393  -0.5271 1051 GLU B CB  
3940 C CG  . GLU B 199 ? 0.3946 0.5242 0.6029 -0.2320 0.2034  -0.4721 1051 GLU B CG  
3941 C CD  . GLU B 199 ? 0.4284 0.5553 0.6121 -0.2168 0.2017  -0.4509 1051 GLU B CD  
3942 O OE1 . GLU B 199 ? 0.5348 0.6501 0.7495 -0.2203 0.2279  -0.4770 1051 GLU B OE1 
3943 O OE2 . GLU B 199 ? 0.4576 0.5930 0.5960 -0.2016 0.1757  -0.4090 1051 GLU B OE2 
3944 N N   . CYS B 200 ? 0.4204 0.4352 0.7826 -0.1910 0.2212  -0.4201 1052 CYS B N   
3945 C CA  . CYS B 200 ? 0.3896 0.3776 0.7716 -0.1745 0.2068  -0.3757 1052 CYS B CA  
3946 C C   . CYS B 200 ? 0.4174 0.3600 0.8861 -0.1690 0.2294  -0.3745 1052 CYS B C   
3947 O O   . CYS B 200 ? 0.4311 0.3586 0.9317 -0.1739 0.2326  -0.3703 1052 CYS B O   
3948 C CB  . CYS B 200 ? 0.3511 0.3345 0.6962 -0.1496 0.1819  -0.3228 1052 CYS B CB  
3949 S SG  . CYS B 200 ? 0.3830 0.4101 0.6404 -0.1505 0.1595  -0.3177 1052 CYS B SG  
3950 N N   . LEU B 201 ? 0.4126 0.3347 0.9238 -0.1590 0.2458  -0.3773 1053 LEU B N   
3951 C CA  . LEU B 201 ? 0.4318 0.3103 1.0351 -0.1504 0.2672  -0.3708 1053 LEU B CA  
3952 C C   . LEU B 201 ? 0.5004 0.3704 1.1598 -0.1742 0.2992  -0.4256 1053 LEU B C   
3953 O O   . LEU B 201 ? 0.5149 0.3506 1.2432 -0.1726 0.3123  -0.4169 1053 LEU B O   
3954 C CB  . LEU B 201 ? 0.4395 0.3034 1.0793 -0.1329 0.2762  -0.3606 1053 LEU B CB  
3955 C CG  . LEU B 201 ? 0.4177 0.2847 1.0215 -0.1088 0.2483  -0.3069 1053 LEU B CG  
3956 C CD1 . LEU B 201 ? 0.4033 0.2651 1.0454 -0.0978 0.2617  -0.3117 1053 LEU B CD1 
3957 C CD2 . LEU B 201 ? 0.3968 0.2399 1.0208 -0.0917 0.2304  -0.2500 1053 LEU B CD2 
3958 N N   . MET B 202 ? 0.5498 0.4520 1.1798 -0.1978 0.3123  -0.4816 1054 MET B N   
3959 C CA  . MET B 202 ? 0.6038 0.5022 1.2864 -0.2245 0.3464  -0.5440 1054 MET B CA  
3960 C C   . MET B 202 ? 0.6338 0.5513 1.2965 -0.2478 0.3404  -0.5641 1054 MET B C   
3961 O O   . MET B 202 ? 0.6824 0.5746 1.4135 -0.2597 0.3629  -0.5867 1054 MET B O   
3962 C CB  . MET B 202 ? 0.6409 0.5689 1.3037 -0.2431 0.3672  -0.6007 1054 MET B CB  
3963 C CG  . MET B 202 ? 0.6261 0.5321 1.3342 -0.2246 0.3845  -0.5948 1054 MET B CG  
3964 S SD  . MET B 202 ? 0.7216 0.6609 1.4146 -0.2493 0.4166  -0.6661 1054 MET B SD  
3965 C CE  . MET B 202 ? 0.5236 0.5275 1.0811 -0.2641 0.3831  -0.6626 1054 MET B CE  
3966 N N   . GLN B 203 ? 0.6143 0.5771 1.1896 -0.2545 0.3113  -0.5567 1055 GLN B N   
3967 C CA  . GLN B 203 ? 0.6728 0.6663 1.2228 -0.2783 0.3023  -0.5783 1055 GLN B CA  
3968 C C   . GLN B 203 ? 0.6449 0.6420 1.1612 -0.2637 0.2699  -0.5244 1055 GLN B C   
3969 O O   . GLN B 203 ? 0.6881 0.7107 1.1904 -0.2812 0.2616  -0.5379 1055 GLN B O   
3970 C CB  . GLN B 203 ? 0.7000 0.7541 1.1795 -0.3033 0.2960  -0.6203 1055 GLN B CB  
3971 C CG  . GLN B 203 ? 0.7713 0.8335 1.2768 -0.3282 0.3313  -0.6876 1055 GLN B CG  
3972 C CD  . GLN B 203 ? 0.8321 0.9505 1.2553 -0.3428 0.3217  -0.7084 1055 GLN B CD  
3973 O OE1 . GLN B 203 ? 0.8184 0.9345 1.2162 -0.3259 0.3186  -0.6869 1055 GLN B OE1 
3974 N NE2 . GLN B 203 ? 0.8222 0.9941 1.2034 -0.3753 0.3162  -0.7483 1055 GLN B NE2 
3975 N N   . SER B 204 ? 0.6102 0.5848 1.1154 -0.2337 0.2529  -0.4667 1056 SER B N   
3976 C CA  . SER B 204 ? 0.5698 0.5500 1.0381 -0.2201 0.2241  -0.4176 1056 SER B CA  
3977 C C   . SER B 204 ? 0.5699 0.6046 0.9605 -0.2288 0.1984  -0.4220 1056 SER B C   
3978 O O   . SER B 204 ? 0.5738 0.6230 0.9458 -0.2286 0.1811  -0.4025 1056 SER B O   
3979 C CB  . SER B 204 ? 0.5923 0.5490 1.1119 -0.2260 0.2323  -0.4099 1056 SER B CB  
3980 O OG  . SER B 204 ? 0.6107 0.5234 1.2132 -0.2276 0.2621  -0.4222 1056 SER B OG  
3981 N N   . LYS B 205 ? 0.5728 0.6383 0.9216 -0.2362 0.1968  -0.4456 1057 LYS B N   
3982 C CA  . LYS B 205 ? 0.5396 0.6583 0.8164 -0.2433 0.1717  -0.4447 1057 LYS B CA  
3983 C C   . LYS B 205 ? 0.5023 0.6184 0.7354 -0.2186 0.1534  -0.4020 1057 LYS B C   
3984 O O   . LYS B 205 ? 0.4969 0.5914 0.7410 -0.2090 0.1654  -0.4006 1057 LYS B O   
3985 C CB  . LYS B 205 ? 0.5715 0.7310 0.8276 -0.2719 0.1827  -0.4989 1057 LYS B CB  
3986 C CG  . LYS B 205 ? 0.6035 0.7701 0.9023 -0.3009 0.2024  -0.5495 1057 LYS B CG  
3987 C CD  . LYS B 205 ? 0.6475 0.8608 0.9174 -0.3325 0.2133  -0.6062 1057 LYS B CD  
3988 C CE  . LYS B 205 ? 0.6863 0.9090 1.0003 -0.3650 0.2343  -0.6631 1057 LYS B CE  
3989 N NZ  . LYS B 205 ? 0.7286 1.0049 1.0074 -0.4001 0.2436  -0.7214 1057 LYS B NZ  
3990 N N   . PHE B 206 ? 0.4595 0.5971 0.6493 -0.2087 0.1261  -0.3687 1058 PHE B N   
3991 C CA  . PHE B 206 ? 0.4135 0.5496 0.5625 -0.1865 0.1083  -0.3287 1058 PHE B CA  
3992 C C   . PHE B 206 ? 0.4178 0.6040 0.5064 -0.1922 0.0869  -0.3252 1058 PHE B C   
3993 O O   . PHE B 206 ? 0.3942 0.6088 0.4683 -0.1957 0.0696  -0.3170 1058 PHE B O   
3994 C CB  . PHE B 206 ? 0.3520 0.4579 0.5127 -0.1644 0.0979  -0.2844 1058 PHE B CB  
3995 C CG  . PHE B 206 ? 0.3552 0.4364 0.5061 -0.1428 0.0942  -0.2533 1058 PHE B CG  
3996 C CD1 . PHE B 206 ? 0.3486 0.4488 0.4505 -0.1339 0.0775  -0.2347 1058 PHE B CD1 
3997 C CD2 . PHE B 206 ? 0.3938 0.4346 0.5880 -0.1324 0.1074  -0.2425 1058 PHE B CD2 
3998 C CE1 . PHE B 206 ? 0.2683 0.3473 0.3626 -0.1159 0.0745  -0.2085 1058 PHE B CE1 
3999 C CE2 . PHE B 206 ? 0.3564 0.3802 0.5423 -0.1140 0.1019  -0.2144 1058 PHE B CE2 
4000 C CZ  . PHE B 206 ? 0.2998 0.3431 0.4351 -0.1069 0.0862  -0.2003 1058 PHE B CZ  
4001 N N   . TYR B 207 ? 0.4193 0.6171 0.4771 -0.1933 0.0891  -0.3301 1059 TYR B N   
4002 C CA  . TYR B 207 ? 0.4255 0.6694 0.4259 -0.1987 0.0707  -0.3222 1059 TYR B CA  
4003 C C   . TYR B 207 ? 0.3849 0.6160 0.3590 -0.1745 0.0559  -0.2773 1059 TYR B C   
4004 O O   . TYR B 207 ? 0.3688 0.5589 0.3640 -0.1570 0.0630  -0.2602 1059 TYR B O   
4005 C CB  . TYR B 207 ? 0.4522 0.7200 0.4322 -0.2196 0.0864  -0.3586 1059 TYR B CB  
4006 C CG  . TYR B 207 ? 0.5001 0.7885 0.4986 -0.2493 0.1040  -0.4122 1059 TYR B CG  
4007 C CD1 . TYR B 207 ? 0.4481 0.6981 0.5057 -0.2532 0.1319  -0.4418 1059 TYR B CD1 
4008 C CD2 . TYR B 207 ? 0.5287 0.8771 0.4876 -0.2751 0.0934  -0.4343 1059 TYR B CD2 
4009 C CE1 . TYR B 207 ? 0.4602 0.7274 0.5399 -0.2827 0.1518  -0.4967 1059 TYR B CE1 
4010 C CE2 . TYR B 207 ? 0.5512 0.9222 0.5255 -0.3062 0.1107  -0.4892 1059 TYR B CE2 
4011 C CZ  . TYR B 207 ? 0.5314 0.8593 0.5675 -0.3099 0.1412  -0.5220 1059 TYR B CZ  
4012 O OH  . TYR B 207 ? 0.4949 0.8422 0.5519 -0.3416 0.1610  -0.5797 1059 TYR B OH  
4013 N N   . ILE B 208 ? 0.3536 0.6213 0.2841 -0.1744 0.0356  -0.2581 1060 ILE B N   
4014 C CA  . ILE B 208 ? 0.3296 0.5876 0.2342 -0.1559 0.0261  -0.2218 1060 ILE B CA  
4015 C C   . ILE B 208 ? 0.3258 0.5624 0.2318 -0.1559 0.0456  -0.2329 1060 ILE B C   
4016 O O   . ILE B 208 ? 0.3314 0.5351 0.2467 -0.1375 0.0469  -0.2100 1060 ILE B O   
4017 C CB  . ILE B 208 ? 0.3287 0.6318 0.1900 -0.1578 0.0034  -0.1990 1060 ILE B CB  
4018 C CG1 . ILE B 208 ? 0.3543 0.6667 0.2274 -0.1475 -0.0160 -0.1765 1060 ILE B CG1 
4019 C CG2 . ILE B 208 ? 0.3711 0.6629 0.2082 -0.1435 -0.0003 -0.1678 1060 ILE B CG2 
4020 C CD1 . ILE B 208 ? 0.4397 0.8046 0.2850 -0.1528 -0.0390 -0.1593 1060 ILE B CD1 
4021 N N   . ALA B 209 ? 0.3364 0.5927 0.2376 -0.1780 0.0624  -0.2713 1061 ALA B N   
4022 C CA  . ALA B 209 ? 0.3746 0.6126 0.2867 -0.1802 0.0858  -0.2891 1061 ALA B CA  
4023 C C   . ALA B 209 ? 0.3462 0.5335 0.3163 -0.1654 0.1012  -0.2905 1061 ALA B C   
4024 O O   . ALA B 209 ? 0.3270 0.4929 0.3119 -0.1569 0.1133  -0.2872 1061 ALA B O   
4025 C CB  . ALA B 209 ? 0.4126 0.6849 0.3117 -0.2099 0.1038  -0.3366 1061 ALA B CB  
4026 N N   . SER B 210 ? 0.3578 0.5281 0.3626 -0.1629 0.1000  -0.2928 1062 SER B N   
4027 C CA  . SER B 210 ? 0.3437 0.4681 0.4027 -0.1478 0.1102  -0.2841 1062 SER B CA  
4028 C C   . SER B 210 ? 0.3268 0.4286 0.3791 -0.1234 0.0947  -0.2391 1062 SER B C   
4029 O O   . SER B 210 ? 0.3441 0.4166 0.4288 -0.1112 0.1025  -0.2290 1062 SER B O   
4030 C CB  . SER B 210 ? 0.3265 0.4409 0.4196 -0.1528 0.1119  -0.2930 1062 SER B CB  
4031 O OG  . SER B 210 ? 0.3486 0.4890 0.4443 -0.1780 0.1239  -0.3365 1062 SER B OG  
4032 N N   . ASP B 211 ? 0.3174 0.4352 0.3310 -0.1173 0.0731  -0.2134 1063 ASP B N   
4033 C CA  . ASP B 211 ? 0.2766 0.3785 0.2772 -0.0978 0.0596  -0.1761 1063 ASP B CA  
4034 C C   . ASP B 211 ? 0.2566 0.3603 0.2401 -0.0952 0.0640  -0.1720 1063 ASP B C   
4035 O O   . ASP B 211 ? 0.2758 0.3580 0.2686 -0.0812 0.0615  -0.1513 1063 ASP B O   
4036 C CB  . ASP B 211 ? 0.2662 0.3851 0.2364 -0.0926 0.0389  -0.1534 1063 ASP B CB  
4037 C CG  . ASP B 211 ? 0.3031 0.4099 0.2939 -0.0874 0.0334  -0.1440 1063 ASP B CG  
4038 O OD1 . ASP B 211 ? 0.2851 0.3638 0.3085 -0.0826 0.0414  -0.1415 1063 ASP B OD1 
4039 O OD2 . ASP B 211 ? 0.3080 0.4357 0.2833 -0.0880 0.0207  -0.1363 1063 ASP B OD2 
4040 N N   . VAL B 212 ? 0.2799 0.4120 0.2381 -0.1104 0.0707  -0.1921 1064 VAL B N   
4041 C CA  . VAL B 212 ? 0.2478 0.3830 0.1924 -0.1112 0.0796  -0.1918 1064 VAL B CA  
4042 C C   . VAL B 212 ? 0.2836 0.3923 0.2757 -0.1070 0.0993  -0.2058 1064 VAL B C   
4043 O O   . VAL B 212 ? 0.2688 0.3628 0.2688 -0.0956 0.0994  -0.1885 1064 VAL B O   
4044 C CB  . VAL B 212 ? 0.2658 0.4413 0.1695 -0.1317 0.0846  -0.2107 1064 VAL B CB  
4045 C CG1 . VAL B 212 ? 0.2924 0.4683 0.1893 -0.1341 0.0996  -0.2139 1064 VAL B CG1 
4046 C CG2 . VAL B 212 ? 0.3340 0.5358 0.1947 -0.1307 0.0611  -0.1839 1064 VAL B CG2 
4047 N N   . TRP B 213 ? 0.2842 0.3872 0.3131 -0.1161 0.1156  -0.2362 1065 TRP B N   
4048 C CA  . TRP B 213 ? 0.2998 0.3748 0.3883 -0.1096 0.1340  -0.2463 1065 TRP B CA  
4049 C C   . TRP B 213 ? 0.2739 0.3202 0.3858 -0.0874 0.1199  -0.2081 1065 TRP B C   
4050 O O   . TRP B 213 ? 0.2613 0.2973 0.3935 -0.0778 0.1236  -0.1976 1065 TRP B O   
4051 C CB  . TRP B 213 ? 0.3283 0.3956 0.4597 -0.1204 0.1509  -0.2784 1065 TRP B CB  
4052 C CG  . TRP B 213 ? 0.3136 0.3522 0.5158 -0.1130 0.1715  -0.2876 1065 TRP B CG  
4053 C CD1 . TRP B 213 ? 0.2987 0.3071 0.5453 -0.0942 0.1650  -0.2580 1065 TRP B CD1 
4054 C CD2 . TRP B 213 ? 0.3801 0.4201 0.6200 -0.1242 0.2020  -0.3278 1065 TRP B CD2 
4055 N NE1 . TRP B 213 ? 0.3586 0.3493 0.6717 -0.0908 0.1871  -0.2726 1065 TRP B NE1 
4056 C CE2 . TRP B 213 ? 0.3554 0.3630 0.6694 -0.1087 0.2120  -0.3178 1065 TRP B CE2 
4057 C CE3 . TRP B 213 ? 0.4432 0.5109 0.6625 -0.1473 0.2227  -0.3722 1065 TRP B CE3 
4058 C CZ2 . TRP B 213 ? 0.3917 0.3908 0.7675 -0.1129 0.2434  -0.3508 1065 TRP B CZ2 
4059 C CZ3 . TRP B 213 ? 0.4483 0.5082 0.7229 -0.1539 0.2558  -0.4091 1065 TRP B CZ3 
4060 C CH2 . TRP B 213 ? 0.4268 0.4509 0.7829 -0.1357 0.2665  -0.3986 1065 TRP B CH2 
4061 N N   . SER B 214 ? 0.2342 0.2717 0.3428 -0.0812 0.1042  -0.1886 1066 SER B N   
4062 C CA  . SER B 214 ? 0.2295 0.2456 0.3509 -0.0638 0.0896  -0.1529 1066 SER B CA  
4063 C C   . SER B 214 ? 0.1943 0.2144 0.2857 -0.0550 0.0772  -0.1301 1066 SER B C   
4064 O O   . SER B 214 ? 0.2342 0.2401 0.3454 -0.0434 0.0712  -0.1089 1066 SER B O   
4065 C CB  . SER B 214 ? 0.2108 0.2241 0.3208 -0.0623 0.0762  -0.1386 1066 SER B CB  
4066 O OG  . SER B 214 ? 0.2682 0.2735 0.4141 -0.0702 0.0884  -0.1570 1066 SER B OG  
4067 N N   . PHE B 215 ? 0.2469 0.2878 0.2922 -0.0611 0.0723  -0.1324 1067 PHE B N   
4068 C CA  . PHE B 215 ? 0.2404 0.2834 0.2612 -0.0545 0.0638  -0.1127 1067 PHE B CA  
4069 C C   . PHE B 215 ? 0.2266 0.2656 0.2719 -0.0533 0.0766  -0.1185 1067 PHE B C   
4070 O O   . PHE B 215 ? 0.2366 0.2671 0.2879 -0.0443 0.0697  -0.0996 1067 PHE B O   
4071 C CB  . PHE B 215 ? 0.2589 0.3246 0.2320 -0.0613 0.0576  -0.1103 1067 PHE B CB  
4072 C CG  . PHE B 215 ? 0.2717 0.3373 0.2276 -0.0568 0.0545  -0.0935 1067 PHE B CG  
4073 C CD1 . PHE B 215 ? 0.2302 0.2811 0.1845 -0.0450 0.0414  -0.0690 1067 PHE B CD1 
4074 C CD2 . PHE B 215 ? 0.2919 0.3710 0.2378 -0.0658 0.0676  -0.1044 1067 PHE B CD2 
4075 C CE1 . PHE B 215 ? 0.2192 0.2681 0.1632 -0.0424 0.0405  -0.0558 1067 PHE B CE1 
4076 C CE2 . PHE B 215 ? 0.2683 0.3453 0.2034 -0.0625 0.0666  -0.0879 1067 PHE B CE2 
4077 C CZ  . PHE B 215 ? 0.2002 0.2614 0.1365 -0.0509 0.0532  -0.0645 1067 PHE B CZ  
4078 N N   . GLY B 216 ? 0.2648 0.3131 0.3244 -0.0641 0.0965  -0.1471 1068 GLY B N   
4079 C CA  . GLY B 216 ? 0.2480 0.2937 0.3398 -0.0631 0.1122  -0.1558 1068 GLY B CA  
4080 C C   . GLY B 216 ? 0.2290 0.2536 0.3754 -0.0488 0.1090  -0.1408 1068 GLY B C   
4081 O O   . GLY B 216 ? 0.2075 0.2308 0.3722 -0.0423 0.1088  -0.1302 1068 GLY B O   
4082 N N   . VAL B 217 ? 0.1903 0.2006 0.3631 -0.0444 0.1051  -0.1371 1069 VAL B N   
4083 C CA  . VAL B 217 ? 0.1828 0.1759 0.4070 -0.0313 0.0995  -0.1166 1069 VAL B CA  
4084 C C   . VAL B 217 ? 0.1964 0.1891 0.3946 -0.0223 0.0758  -0.0833 1069 VAL B C   
4085 O O   . VAL B 217 ? 0.2002 0.1915 0.4268 -0.0141 0.0699  -0.0670 1069 VAL B O   
4086 C CB  . VAL B 217 ? 0.2397 0.2173 0.4963 -0.0303 0.1017  -0.1168 1069 VAL B CB  
4087 C CG1 . VAL B 217 ? 0.2461 0.2092 0.5550 -0.0167 0.0938  -0.0884 1069 VAL B CG1 
4088 C CG2 . VAL B 217 ? 0.2780 0.2554 0.5654 -0.0417 0.1283  -0.1560 1069 VAL B CG2 
4089 N N   . THR B 218 ? 0.1957 0.1919 0.3431 -0.0249 0.0629  -0.0754 1070 THR B N   
4090 C CA  . THR B 218 ? 0.1776 0.1741 0.2965 -0.0194 0.0442  -0.0509 1070 THR B CA  
4091 C C   . THR B 218 ? 0.1892 0.1937 0.2992 -0.0195 0.0449  -0.0496 1070 THR B C   
4092 O O   . THR B 218 ? 0.1721 0.1759 0.2885 -0.0144 0.0336  -0.0324 1070 THR B O   
4093 C CB  . THR B 218 ? 0.2153 0.2152 0.2867 -0.0226 0.0351  -0.0478 1070 THR B CB  
4094 O OG1 . THR B 218 ? 0.2369 0.2316 0.3163 -0.0243 0.0356  -0.0506 1070 THR B OG1 
4095 C CG2 . THR B 218 ? 0.2073 0.2053 0.2556 -0.0176 0.0194  -0.0267 1070 THR B CG2 
4096 N N   . LEU B 219 ? 0.2025 0.2171 0.2964 -0.0272 0.0581  -0.0674 1071 LEU B N   
4097 C CA  . LEU B 219 ? 0.1930 0.2152 0.2823 -0.0293 0.0630  -0.0669 1071 LEU B CA  
4098 C C   . LEU B 219 ? 0.2104 0.2316 0.3529 -0.0240 0.0679  -0.0660 1071 LEU B C   
4099 O O   . LEU B 219 ? 0.1876 0.2118 0.3364 -0.0214 0.0611  -0.0539 1071 LEU B O   
4100 C CB  . LEU B 219 ? 0.2642 0.3006 0.3291 -0.0410 0.0794  -0.0866 1071 LEU B CB  
4101 C CG  . LEU B 219 ? 0.2144 0.2601 0.2709 -0.0459 0.0882  -0.0860 1071 LEU B CG  
4102 C CD1 . LEU B 219 ? 0.2617 0.3028 0.2898 -0.0425 0.0730  -0.0626 1071 LEU B CD1 
4103 C CD2 . LEU B 219 ? 0.2487 0.3122 0.2777 -0.0599 0.1049  -0.1049 1071 LEU B CD2 
4104 N N   . HIS B 220 ? 0.1775 0.1955 0.3640 -0.0228 0.0805  -0.0795 1072 HIS B N   
4105 C CA  . HIS B 220 ? 0.1885 0.2058 0.4374 -0.0151 0.0840  -0.0751 1072 HIS B CA  
4106 C C   . HIS B 220 ? 0.1703 0.1851 0.4307 -0.0055 0.0595  -0.0437 1072 HIS B C   
4107 O O   . HIS B 220 ? 0.1648 0.1886 0.4524 -0.0017 0.0538  -0.0331 1072 HIS B O   
4108 C CB  . HIS B 220 ? 0.2129 0.2229 0.5132 -0.0142 0.1019  -0.0933 1072 HIS B CB  
4109 C CG  . HIS B 220 ? 0.1975 0.2098 0.5709 -0.0070 0.1130  -0.0952 1072 HIS B CG  
4110 N ND1 . HIS B 220 ? 0.2362 0.2457 0.6574 0.0058  0.0972  -0.0669 1072 HIS B ND1 
4111 C CD2 . HIS B 220 ? 0.2075 0.2272 0.6180 -0.0112 0.1390  -0.1217 1072 HIS B CD2 
4112 C CE1 . HIS B 220 ? 0.2704 0.2854 0.7602 0.0112  0.1115  -0.0740 1072 HIS B CE1 
4113 N NE2 . HIS B 220 ? 0.1744 0.1944 0.6599 0.0010  0.1386  -0.1090 1072 HIS B NE2 
4114 N N   . GLU B 221 ? 0.1682 0.1743 0.4068 -0.0035 0.0455  -0.0299 1073 GLU B N   
4115 C CA  . GLU B 221 ? 0.1661 0.1737 0.4042 0.0020  0.0225  -0.0009 1073 GLU B CA  
4116 C C   . GLU B 221 ? 0.1893 0.2066 0.3934 -0.0016 0.0112  0.0054  1073 GLU B C   
4117 O O   . GLU B 221 ? 0.1865 0.2145 0.4095 0.0006  -0.0015 0.0203  1073 GLU B O   
4118 C CB  . GLU B 221 ? 0.1581 0.1564 0.3676 0.0013  0.0135  0.0088  1073 GLU B CB  
4119 C CG  . GLU B 221 ? 0.1914 0.1781 0.4371 0.0039  0.0223  0.0072  1073 GLU B CG  
4120 C CD  . GLU B 221 ? 0.1564 0.1365 0.3738 0.0023  0.0119  0.0210  1073 GLU B CD  
4121 O OE1 . GLU B 221 ? 0.2087 0.1854 0.3928 -0.0035 0.0179  0.0058  1073 GLU B OE1 
4122 O OE2 . GLU B 221 ? 0.2228 0.2050 0.4501 0.0058  -0.0028 0.0481  1073 GLU B OE2 
4123 N N   . LEU B 222 ? 0.2107 0.2253 0.3680 -0.0076 0.0161  -0.0060 1074 LEU B N   
4124 C CA  . LEU B 222 ? 0.2067 0.2258 0.3343 -0.0116 0.0091  -0.0019 1074 LEU B CA  
4125 C C   . LEU B 222 ? 0.2109 0.2410 0.3708 -0.0126 0.0136  -0.0041 1074 LEU B C   
4126 O O   . LEU B 222 ? 0.1809 0.2197 0.3480 -0.0136 0.0006  0.0067  1074 LEU B O   
4127 C CB  . LEU B 222 ? 0.2570 0.2713 0.3413 -0.0165 0.0173  -0.0120 1074 LEU B CB  
4128 C CG  . LEU B 222 ? 0.2987 0.3133 0.3558 -0.0210 0.0175  -0.0104 1074 LEU B CG  
4129 C CD1 . LEU B 222 ? 0.3448 0.3572 0.3928 -0.0209 0.0021  0.0010  1074 LEU B CD1 
4130 C CD2 . LEU B 222 ? 0.3430 0.3547 0.3644 -0.0233 0.0229  -0.0144 1074 LEU B CD2 
4131 N N   . LEU B 223 ? 0.2071 0.2397 0.3888 -0.0139 0.0329  -0.0200 1075 LEU B N   
4132 C CA  . LEU B 223 ? 0.2116 0.2560 0.4285 -0.0156 0.0424  -0.0256 1075 LEU B CA  
4133 C C   . LEU B 223 ? 0.2169 0.2724 0.4928 -0.0082 0.0319  -0.0129 1075 LEU B C   
4134 O O   . LEU B 223 ? 0.2263 0.2959 0.5300 -0.0099 0.0318  -0.0117 1075 LEU B O   
4135 C CB  . LEU B 223 ? 0.2482 0.2947 0.4722 -0.0206 0.0686  -0.0487 1075 LEU B CB  
4136 C CG  . LEU B 223 ? 0.2736 0.3183 0.4399 -0.0300 0.0771  -0.0565 1075 LEU B CG  
4137 C CD1 . LEU B 223 ? 0.3032 0.3530 0.4670 -0.0370 0.0996  -0.0800 1075 LEU B CD1 
4138 C CD2 . LEU B 223 ? 0.3206 0.3710 0.4744 -0.0362 0.0795  -0.0513 1075 LEU B CD2 
4139 N N   . THR B 224 ? 0.1748 0.2259 0.4731 -0.0006 0.0229  -0.0013 1076 THR B N   
4140 C CA  . THR B 224 ? 0.1828 0.2465 0.5354 0.0073  0.0078  0.0196  1076 THR B CA  
4141 C C   . THR B 224 ? 0.1647 0.2370 0.4898 0.0056  -0.0205 0.0437  1076 THR B C   
4142 O O   . THR B 224 ? 0.1688 0.2554 0.5299 0.0108  -0.0378 0.0668  1076 THR B O   
4143 C CB  . THR B 224 ? 0.1687 0.2239 0.5734 0.0169  0.0150  0.0233  1076 THR B CB  
4144 O OG1 . THR B 224 ? 0.2604 0.2995 0.6296 0.0164  0.0101  0.0286  1076 THR B OG1 
4145 C CG2 . THR B 224 ? 0.2208 0.2705 0.6590 0.0165  0.0452  -0.0055 1076 THR B CG2 
4146 N N   . TYR B 225 ? 0.1836 0.2499 0.4475 -0.0025 -0.0247 0.0387  1077 TYR B N   
4147 C CA  . TYR B 225 ? 0.1624 0.2365 0.3934 -0.0075 -0.0467 0.0540  1077 TYR B CA  
4148 C C   . TYR B 225 ? 0.2011 0.2747 0.4349 -0.0030 -0.0597 0.0751  1077 TYR B C   
4149 O O   . TYR B 225 ? 0.1272 0.2180 0.3555 -0.0065 -0.0804 0.0944  1077 TYR B O   
4150 C CB  . TYR B 225 ? 0.2197 0.3181 0.4687 -0.0129 -0.0606 0.0602  1077 TYR B CB  
4151 C CG  . TYR B 225 ? 0.2249 0.3219 0.4642 -0.0202 -0.0481 0.0414  1077 TYR B CG  
4152 C CD1 . TYR B 225 ? 0.1407 0.2281 0.3306 -0.0292 -0.0478 0.0326  1077 TYR B CD1 
4153 C CD2 . TYR B 225 ? 0.2201 0.3252 0.5036 -0.0185 -0.0351 0.0332  1077 TYR B CD2 
4154 C CE1 . TYR B 225 ? 0.1470 0.2311 0.3318 -0.0361 -0.0359 0.0193  1077 TYR B CE1 
4155 C CE2 . TYR B 225 ? 0.2185 0.3222 0.4923 -0.0268 -0.0221 0.0184  1077 TYR B CE2 
4156 C CZ  . TYR B 225 ? 0.2243 0.3168 0.4490 -0.0355 -0.0234 0.0132  1077 TYR B CZ  
4157 O OH  . TYR B 225 ? 0.2256 0.3147 0.4447 -0.0438 -0.0104 0.0026  1077 TYR B OH  
4158 N N   . CYS B 226 ? 0.2160 0.2713 0.4566 0.0027  -0.0467 0.0707  1078 CYS B N   
4159 C CA  . CYS B 226 ? 0.2117 0.2622 0.4594 0.0066  -0.0544 0.0902  1078 CYS B CA  
4160 C C   . CYS B 226 ? 0.2437 0.3130 0.5407 0.0120  -0.0720 0.1209  1078 CYS B C   
4161 O O   . CYS B 226 ? 0.2615 0.3366 0.5485 0.0109  -0.0872 0.1460  1078 CYS B O   
4162 C CB  . CYS B 226 ? 0.2542 0.3012 0.4402 -0.0011 -0.0626 0.0929  1078 CYS B CB  
4163 S SG  . CYS B 226 ? 0.2727 0.2977 0.4166 -0.0036 -0.0437 0.0664  1078 CYS B SG  
4164 N N   . ASP B 227 ? 0.2204 0.3017 0.5728 0.0177  -0.0697 0.1208  1079 ASP B N   
4165 C CA  . ASP B 227 ? 0.2591 0.3613 0.6706 0.0251  -0.0869 0.1527  1079 ASP B CA  
4166 C C   . ASP B 227 ? 0.2541 0.3380 0.7089 0.0353  -0.0789 0.1674  1079 ASP B C   
4167 O O   . ASP B 227 ? 0.2532 0.3137 0.7286 0.0392  -0.0537 0.1436  1079 ASP B O   
4168 C CB  . ASP B 227 ? 0.2514 0.3708 0.7218 0.0299  -0.0829 0.1463  1079 ASP B CB  
4169 C CG  . ASP B 227 ? 0.2743 0.4145 0.8231 0.0412  -0.0980 0.1804  1079 ASP B CG  
4170 O OD1 . ASP B 227 ? 0.2606 0.4203 0.8001 0.0394  -0.1248 0.2147  1079 ASP B OD1 
4171 O OD2 . ASP B 227 ? 0.3875 0.5267 1.0093 0.0516  -0.0826 0.1738  1079 ASP B OD2 
4172 N N   . SER B 228 ? 0.2828 0.3788 0.7512 0.0377  -0.0998 0.2063  1080 SER B N   
4173 C CA  . SER B 228 ? 0.3135 0.3894 0.8192 0.0457  -0.0930 0.2251  1080 SER B CA  
4174 C C   . SER B 228 ? 0.3234 0.3901 0.9252 0.0602  -0.0765 0.2240  1080 SER B C   
4175 O O   . SER B 228 ? 0.3151 0.3536 0.9485 0.0649  -0.0554 0.2143  1080 SER B O   
4176 C CB  . SER B 228 ? 0.3582 0.4526 0.8541 0.0435  -0.1202 0.2726  1080 SER B CB  
4177 O OG  . SER B 228 ? 0.4110 0.5406 0.9508 0.0481  -0.1441 0.3042  1080 SER B OG  
4178 N N   . ASP B 229 ? 0.3109 0.4022 0.9628 0.0662  -0.0844 0.2307  1081 ASP B N   
4179 C CA  . ASP B 229 ? 0.3177 0.4029 1.0672 0.0801  -0.0655 0.2248  1081 ASP B CA  
4180 C C   . ASP B 229 ? 0.3052 0.3698 1.0543 0.0771  -0.0302 0.1717  1081 ASP B C   
4181 O O   . ASP B 229 ? 0.3409 0.3931 1.1655 0.0861  -0.0064 0.1576  1081 ASP B O   
4182 C CB  . ASP B 229 ? 0.3101 0.4331 1.1195 0.0876  -0.0861 0.2512  1081 ASP B CB  
4183 C CG  . ASP B 229 ? 0.3811 0.5265 1.2137 0.0928  -0.1191 0.3093  1081 ASP B CG  
4184 O OD1 . ASP B 229 ? 0.5199 0.6477 1.4116 0.1043  -0.1135 0.3336  1081 ASP B OD1 
4185 O OD2 . ASP B 229 ? 0.4397 0.6211 1.2318 0.0841  -0.1500 0.3310  1081 ASP B OD2 
4186 N N   . SER B 230 ? 0.3192 0.3814 0.9853 0.0639  -0.0262 0.1433  1082 SER B N   
4187 C CA  . SER B 230 ? 0.3238 0.3693 0.9700 0.0575  0.0047  0.0961  1082 SER B CA  
4188 C C   . SER B 230 ? 0.3213 0.3405 0.9159 0.0502  0.0169  0.0787  1082 SER B C   
4189 O O   . SER B 230 ? 0.3313 0.3410 0.8974 0.0423  0.0387  0.0419  1082 SER B O   
4190 C CB  . SER B 230 ? 0.2993 0.3614 0.8926 0.0476  0.0012  0.0794  1082 SER B CB  
4191 O OG  . SER B 230 ? 0.3991 0.4899 1.0330 0.0517  -0.0151 0.0981  1082 SER B OG  
4192 N N   . SER B 231 ? 0.3284 0.3391 0.9121 0.0518  0.0026  0.1059  1083 SER B N   
4193 C CA  . SER B 231 ? 0.3170 0.3071 0.8509 0.0440  0.0107  0.0925  1083 SER B CA  
4194 C C   . SER B 231 ? 0.3188 0.2872 0.8914 0.0433  0.0424  0.0590  1083 SER B C   
4195 O O   . SER B 231 ? 0.3153 0.2773 0.9699 0.0522  0.0557  0.0597  1083 SER B O   
4196 C CB  . SER B 231 ? 0.3743 0.3614 0.8984 0.0453  -0.0086 0.1307  1083 SER B CB  
4197 O OG  . SER B 231 ? 0.4342 0.4105 1.0374 0.0556  -0.0045 0.1535  1083 SER B OG  
4198 N N   . PRO B 232 ? 0.3160 0.2753 0.8336 0.0319  0.0551  0.0281  1084 PRO B N   
4199 C CA  . PRO B 232 ? 0.3036 0.2459 0.8497 0.0269  0.0839  -0.0067 1084 PRO B CA  
4200 C C   . PRO B 232 ? 0.3169 0.2387 0.9372 0.0340  0.0922  0.0070  1084 PRO B C   
4201 O O   . PRO B 232 ? 0.3488 0.2595 1.0318 0.0347  0.1185  -0.0187 1084 PRO B O   
4202 C CB  . PRO B 232 ? 0.2827 0.2240 0.7512 0.0142  0.0829  -0.0241 1084 PRO B CB  
4203 C CG  . PRO B 232 ? 0.2706 0.2295 0.6770 0.0124  0.0651  -0.0155 1084 PRO B CG  
4204 C CD  . PRO B 232 ? 0.2747 0.2417 0.7047 0.0225  0.0436  0.0227  1084 PRO B CD  
4205 N N   . MET B 233 ? 0.3514 0.2687 0.9680 0.0385  0.0719  0.0473  1085 MET B N   
4206 C CA  . MET B 233 ? 0.4048 0.3023 1.0965 0.0464  0.0774  0.0706  1085 MET B CA  
4207 C C   . MET B 233 ? 0.3916 0.2929 1.1737 0.0615  0.0790  0.0892  1085 MET B C   
4208 O O   . MET B 233 ? 0.4410 0.3231 1.3052 0.0667  0.1029  0.0769  1085 MET B O   
4209 C CB  . MET B 233 ? 0.4167 0.3139 1.0779 0.0464  0.0535  0.1154  1085 MET B CB  
4210 C CG  . MET B 233 ? 0.5028 0.3785 1.2400 0.0537  0.0588  0.1461  1085 MET B CG  
4211 S SD  . MET B 233 ? 0.6024 0.4761 1.2904 0.0473  0.0388  0.1889  1085 MET B SD  
4212 C CE  . MET B 233 ? 0.5993 0.5027 1.2893 0.0571  0.0029  0.2502  1085 MET B CE  
4213 N N   . ALA B 234 ? 0.3690 0.2961 1.1399 0.0679  0.0544  0.1171  1086 ALA B N   
4214 C CA  . ALA B 234 ? 0.3449 0.2839 1.2014 0.0827  0.0511  0.1382  1086 ALA B CA  
4215 C C   . ALA B 234 ? 0.3633 0.2964 1.2786 0.0846  0.0843  0.0935  1086 ALA B C   
4216 O O   . ALA B 234 ? 0.3588 0.2806 1.3740 0.0962  0.1003  0.0977  1086 ALA B O   
4217 C CB  . ALA B 234 ? 0.3202 0.2938 1.1420 0.0844  0.0195  0.1659  1086 ALA B CB  
4218 N N   . LEU B 235 ? 0.3232 0.2645 1.1791 0.0727  0.0960  0.0515  1087 LEU B N   
4219 C CA  . LEU B 235 ? 0.3521 0.2921 1.2495 0.0700  0.1300  0.0045  1087 LEU B CA  
4220 C C   . LEU B 235 ? 0.3657 0.2770 1.3136 0.0664  0.1630  -0.0270 1087 LEU B C   
4221 O O   . LEU B 235 ? 0.3356 0.2396 1.3745 0.0734  0.1885  -0.0437 1087 LEU B O   
4222 C CB  . LEU B 235 ? 0.3633 0.3191 1.1763 0.0553  0.1349  -0.0299 1087 LEU B CB  
4223 C CG  . LEU B 235 ? 0.4375 0.4214 1.2405 0.0584  0.1196  -0.0175 1087 LEU B CG  
4224 C CD1 . LEU B 235 ? 0.4727 0.4712 1.2885 0.0698  0.0829  0.0364  1087 LEU B CD1 
4225 C CD2 . LEU B 235 ? 0.4049 0.3998 1.1102 0.0434  0.1174  -0.0386 1087 LEU B CD2 
4226 N N   . PHE B 236 ? 0.3611 0.2569 1.2565 0.0554  0.1635  -0.0356 1088 PHE B N   
4227 C CA  . PHE B 236 ? 0.3805 0.2492 1.3251 0.0496  0.1941  -0.0662 1088 PHE B CA  
4228 C C   . PHE B 236 ? 0.4130 0.2593 1.4663 0.0658  0.1978  -0.0333 1088 PHE B C   
4229 O O   . PHE B 236 ? 0.4545 0.2823 1.5908 0.0667  0.2309  -0.0629 1088 PHE B O   
4230 C CB  . PHE B 236 ? 0.3665 0.2275 1.2331 0.0329  0.1924  -0.0826 1088 PHE B CB  
4231 C CG  . PHE B 236 ? 0.3440 0.2212 1.1367 0.0142  0.2055  -0.1325 1088 PHE B CG  
4232 C CD1 . PHE B 236 ? 0.3761 0.2545 1.2023 0.0043  0.2408  -0.1849 1088 PHE B CD1 
4233 C CD2 . PHE B 236 ? 0.3108 0.2034 1.0031 0.0056  0.1838  -0.1266 1088 PHE B CD2 
4234 C CE1 . PHE B 236 ? 0.3427 0.2410 1.0969 -0.0148 0.2514  -0.2268 1088 PHE B CE1 
4235 C CE2 . PHE B 236 ? 0.2643 0.1743 0.8916 -0.0111 0.1938  -0.1662 1088 PHE B CE2 
4236 C CZ  . PHE B 236 ? 0.3211 0.2353 0.9767 -0.0219 0.2266  -0.2147 1088 PHE B CZ  
4237 N N   . LEU B 237 ? 0.4428 0.2925 1.4985 0.0779  0.1653  0.0274  1089 LEU B N   
4238 C CA  . LEU B 237 ? 0.4899 0.3203 1.6475 0.0937  0.1651  0.0690  1089 LEU B CA  
4239 C C   . LEU B 237 ? 0.5014 0.3375 1.7688 0.1112  0.1759  0.0753  1089 LEU B C   
4240 O O   . LEU B 237 ? 0.5127 0.3247 1.8876 0.1219  0.1957  0.0822  1089 LEU B O   
4241 C CB  . LEU B 237 ? 0.5173 0.3562 1.6409 0.0996  0.1257  0.1356  1089 LEU B CB  
4242 C CG  . LEU B 237 ? 0.5347 0.3621 1.5804 0.0857  0.1177  0.1407  1089 LEU B CG  
4243 C CD1 . LEU B 237 ? 0.5824 0.4282 1.5859 0.0897  0.0785  0.2041  1089 LEU B CD1 
4244 C CD2 . LEU B 237 ? 0.5898 0.3796 1.6963 0.0822  0.1453  0.1287  1089 LEU B CD2 
4245 N N   . LYS B 238 ? 0.4745 0.3421 1.7212 0.1144  0.1640  0.0737  1090 LYS B N   
4246 C CA  . LYS B 238 ? 0.4859 0.3630 1.8358 0.1287  0.1793  0.0686  1090 LYS B CA  
4247 C C   . LYS B 238 ? 0.4856 0.3456 1.8779 0.1197  0.2293  -0.0018 1090 LYS B C   
4248 O O   . LYS B 238 ? 0.5123 0.3626 2.0206 0.1317  0.2550  -0.0110 1090 LYS B O   
4249 C CB  . LYS B 238 ? 0.4607 0.3783 1.7727 0.1311  0.1547  0.0812  1090 LYS B CB  
4250 C CG  . LYS B 238 ? 0.4588 0.3995 1.7482 0.1400  0.1061  0.1508  1090 LYS B CG  
4251 C CD  . LYS B 238 ? 0.4373 0.4186 1.6863 0.1387  0.0829  0.1573  1090 LYS B CD  
4252 C CE  . LYS B 238 ? 0.4366 0.4448 1.6537 0.1426  0.0353  0.2198  1090 LYS B CE  
4253 N NZ  . LYS B 238 ? 0.4182 0.4670 1.6004 0.1392  0.0132  0.2231  1090 LYS B NZ  
4254 N N   . MET B 239 ? 0.4658 0.3244 1.7653 0.0980  0.2430  -0.0508 1091 MET B N   
4255 C CA  . MET B 239 ? 0.4804 0.3331 1.7941 0.0833  0.2880  -0.1220 1091 MET B CA  
4256 C C   . MET B 239 ? 0.5125 0.3291 1.9022 0.0795  0.3235  -0.1516 1091 MET B C   
4257 O O   . MET B 239 ? 0.5255 0.3322 2.0145 0.0835  0.3601  -0.1838 1091 MET B O   
4258 C CB  . MET B 239 ? 0.4873 0.3569 1.6704 0.0607  0.2846  -0.1558 1091 MET B CB  
4259 C CG  . MET B 239 ? 0.5555 0.4265 1.7235 0.0394  0.3260  -0.2281 1091 MET B CG  
4260 S SD  . MET B 239 ? 0.6883 0.5935 1.7175 0.0185  0.3171  -0.2534 1091 MET B SD  
4261 C CE  . MET B 239 ? 0.5393 0.4523 1.4769 0.0254  0.2632  -0.1926 1091 MET B CE  
4262 N N   . ILE B 240 ? 0.4846 0.2820 1.8316 0.0710  0.3147  -0.1429 1092 ILE B N   
4263 C CA  . ILE B 240 ? 0.5419 0.3040 1.9543 0.0637  0.3481  -0.1733 1092 ILE B CA  
4264 C C   . ILE B 240 ? 0.5740 0.3069 2.1042 0.0853  0.3461  -0.1232 1092 ILE B C   
4265 O O   . ILE B 240 ? 0.6584 0.3605 2.2843 0.0845  0.3824  -0.1507 1092 ILE B O   
4266 C CB  . ILE B 240 ? 0.5129 0.2688 1.8302 0.0412  0.3441  -0.1940 1092 ILE B CB  
4267 C CG1 . ILE B 240 ? 0.4753 0.2271 1.7474 0.0490  0.3032  -0.1288 1092 ILE B CG1 
4268 C CG2 . ILE B 240 ? 0.5418 0.3287 1.7489 0.0203  0.3456  -0.2398 1092 ILE B CG2 
4269 C CD1 . ILE B 240 ? 0.4790 0.2308 1.6552 0.0285  0.2958  -0.1452 1092 ILE B CD1 
4270 N N   . GLY B 241 ? 0.5786 0.3224 2.1006 0.1028  0.3044  -0.0504 1093 GLY B N   
4271 C CA  . GLY B 241 ? 0.6216 0.3436 2.2415 0.1230  0.2942  0.0110  1093 GLY B CA  
4272 C C   . GLY B 241 ? 0.6404 0.3657 2.1827 0.1219  0.2537  0.0693  1093 GLY B C   
4273 O O   . GLY B 241 ? 0.6590 0.3769 2.1184 0.1030  0.2546  0.0471  1093 GLY B O   
4274 N N   . PRO B 242 ? 0.6532 0.3935 2.2203 0.1404  0.2178  0.1433  1094 PRO B N   
4275 C CA  . PRO B 242 ? 0.6545 0.4027 2.1434 0.1371  0.1801  0.1987  1094 PRO B CA  
4276 C C   . PRO B 242 ? 0.6802 0.3924 2.2115 0.1363  0.1871  0.2290  1094 PRO B C   
4277 O O   . PRO B 242 ? 0.6821 0.3853 2.1348 0.1190  0.1864  0.2166  1094 PRO B O   
4278 C CB  . PRO B 242 ? 0.6556 0.4390 2.1601 0.1548  0.1409  0.2631  1094 PRO B CB  
4279 C CG  . PRO B 242 ? 0.6884 0.4683 2.3248 0.1736  0.1604  0.2605  1094 PRO B CG  
4280 C CD  . PRO B 242 ? 0.6836 0.4406 2.3482 0.1636  0.2095  0.1783  1094 PRO B CD  
4281 N N   . THR B 243 ? 0.7030 0.3953 2.3620 0.1548  0.1949  0.2685  1095 THR B N   
4282 C CA  . THR B 243 ? 0.7355 0.3998 2.4394 0.1580  0.1913  0.3225  1095 THR B CA  
4283 C C   . THR B 243 ? 0.7668 0.3812 2.5299 0.1469  0.2368  0.2764  1095 THR B C   
4284 O O   . THR B 243 ? 0.7757 0.3562 2.6646 0.1592  0.2568  0.2998  1095 THR B O   
4285 C CB  . THR B 243 ? 0.7792 0.4485 2.5966 0.1844  0.1733  0.3991  1095 THR B CB  
4286 O OG1 . THR B 243 ? 0.7802 0.4345 2.7250 0.1996  0.2039  0.3733  1095 THR B OG1 
4287 C CG2 . THR B 243 ? 0.7482 0.4724 2.4951 0.1908  0.1224  0.4509  1095 THR B CG2 
4288 N N   . HIS B 244 ? 0.7470 0.3585 2.4216 0.1231  0.2523  0.2124  1096 HIS B N   
4289 C CA  . HIS B 244 ? 0.7587 0.3303 2.4756 0.1071  0.2955  0.1561  1096 HIS B CA  
4290 C C   . HIS B 244 ? 0.7530 0.3105 2.4060 0.0887  0.2907  0.1657  1096 HIS B C   
4291 O O   . HIS B 244 ? 0.7792 0.3020 2.4807 0.0758  0.3243  0.1300  1096 HIS B O   
4292 C CB  . HIS B 244 ? 0.7355 0.3169 2.4185 0.0916  0.3235  0.0662  1096 HIS B CB  
4293 C CG  . HIS B 244 ? 0.7450 0.3331 2.5107 0.1066  0.3408  0.0460  1096 HIS B CG  
4294 N ND1 . HIS B 244 ? 0.6811 0.2378 2.5695 0.1083  0.3871  0.0029  1096 HIS B ND1 
4295 C CD2 . HIS B 244 ? 0.7074 0.3307 2.4563 0.1202  0.3193  0.0626  1096 HIS B CD2 
4296 C CE1 . HIS B 244 ? 0.7083 0.2816 2.6515 0.1230  0.3941  -0.0063 1096 HIS B CE1 
4297 N NE2 . HIS B 244 ? 0.6376 0.2518 2.4977 0.1304  0.3526  0.0304  1096 HIS B NE2 
4298 N N   . GLY B 245 ? 0.7167 0.3020 2.2653 0.0863  0.2512  0.2106  1097 GLY B N   
4299 C CA  . GLY B 245 ? 0.7170 0.2935 2.2052 0.0701  0.2445  0.2271  1097 GLY B CA  
4300 C C   . GLY B 245 ? 0.6913 0.2643 2.1189 0.0447  0.2667  0.1519  1097 GLY B C   
4301 O O   . GLY B 245 ? 0.6626 0.2650 2.0040 0.0364  0.2594  0.1097  1097 GLY B O   
4302 N N   . GLN B 246 ? 0.7177 0.2556 2.1961 0.0320  0.2941  0.1360  1098 GLN B N   
4303 C CA  . GLN B 246 ? 0.6974 0.2330 2.1297 0.0054  0.3157  0.0658  1098 GLN B CA  
4304 C C   . GLN B 246 ? 0.6753 0.2122 2.1314 -0.0041 0.3472  -0.0177 1098 GLN B C   
4305 O O   . GLN B 246 ? 0.6755 0.2212 2.0819 -0.0275 0.3608  -0.0779 1098 GLN B O   
4306 C CB  . GLN B 246 ? 0.7527 0.2509 2.2423 -0.0068 0.3370  0.0739  1098 GLN B CB  
4307 C CG  . GLN B 246 ? 0.6884 0.1918 2.1259 -0.0072 0.3093  0.1426  1098 GLN B CG  
4308 C CD  . GLN B 246 ? 0.7322 0.1983 2.2279 -0.0214 0.3331  0.1492  1098 GLN B CD  
4309 O OE1 . GLN B 246 ? 0.7678 0.1950 2.3733 -0.0232 0.3682  0.1250  1098 GLN B OE1 
4310 N NE2 . GLN B 246 ? 0.7288 0.2060 2.1544 -0.0322 0.3160  0.1808  1098 GLN B NE2 
4311 N N   . MET B 247 ? 0.6394 0.1711 2.1713 0.0128  0.3587  -0.0208 1099 MET B N   
4312 C CA  . MET B 247 ? 0.6202 0.1583 2.1710 0.0041  0.3889  -0.0978 1099 MET B CA  
4313 C C   . MET B 247 ? 0.5660 0.1498 2.0169 0.0046  0.3677  -0.1163 1099 MET B C   
4314 O O   . MET B 247 ? 0.5569 0.1521 2.0068 -0.0054 0.3911  -0.1794 1099 MET B O   
4315 C CB  . MET B 247 ? 0.6921 0.2010 2.3861 0.0219  0.4174  -0.0961 1099 MET B CB  
4316 C CG  . MET B 247 ? 0.7391 0.1991 2.5497 0.0264  0.4382  -0.0674 1099 MET B CG  
4317 S SD  . MET B 247 ? 0.6735 0.1086 2.4745 -0.0074 0.4669  -0.1207 1099 MET B SD  
4318 C CE  . MET B 247 ? 0.6823 0.1306 2.4791 -0.0313 0.5077  -0.2352 1099 MET B CE  
4319 N N   . THR B 248 ? 0.5087 0.1185 1.8771 0.0142  0.3260  -0.0635 1100 THR B N   
4320 C CA  . THR B 248 ? 0.4634 0.1125 1.7528 0.0179  0.3058  -0.0722 1100 THR B CA  
4321 C C   . THR B 248 ? 0.4432 0.1163 1.6466 -0.0055 0.3161  -0.1411 1100 THR B C   
4322 O O   . THR B 248 ? 0.4318 0.1258 1.6177 -0.0057 0.3220  -0.1721 1100 THR B O   
4323 C CB  . THR B 248 ? 0.4503 0.1223 1.6670 0.0298  0.2600  -0.0046 1100 THR B CB  
4324 O OG1 . THR B 248 ? 0.5034 0.1602 1.8010 0.0505  0.2493  0.0604  1100 THR B OG1 
4325 C CG2 . THR B 248 ? 0.4538 0.1630 1.6003 0.0339  0.2408  -0.0120 1100 THR B CG2 
4326 N N   . VAL B 249 ? 0.4457 0.1181 1.5992 -0.0258 0.3183  -0.1635 1101 VAL B N   
4327 C CA  . VAL B 249 ? 0.4307 0.1335 1.4924 -0.0477 0.3197  -0.2178 1101 VAL B CA  
4328 C C   . VAL B 249 ? 0.4554 0.1596 1.5498 -0.0663 0.3586  -0.2947 1101 VAL B C   
4329 O O   . VAL B 249 ? 0.4431 0.1795 1.4710 -0.0770 0.3579  -0.3303 1101 VAL B O   
4330 C CB  . VAL B 249 ? 0.4230 0.1327 1.4159 -0.0630 0.3046  -0.2132 1101 VAL B CB  
4331 C CG1 . VAL B 249 ? 0.4110 0.1561 1.3159 -0.0852 0.3041  -0.2660 1101 VAL B CG1 
4332 C CG2 . VAL B 249 ? 0.3972 0.1152 1.3368 -0.0481 0.2665  -0.1455 1101 VAL B CG2 
4333 N N   . THR B 250 ? 0.4935 0.1649 1.6871 -0.0722 0.3934  -0.3217 1102 THR B N   
4334 C CA  . THR B 250 ? 0.5229 0.1971 1.7520 -0.0921 0.4344  -0.4003 1102 THR B CA  
4335 C C   . THR B 250 ? 0.5194 0.2036 1.7774 -0.0785 0.4444  -0.4084 1102 THR B C   
4336 O O   . THR B 250 ? 0.5249 0.2360 1.7454 -0.0952 0.4611  -0.4640 1102 THR B O   
4337 C CB  . THR B 250 ? 0.5697 0.2028 1.9121 -0.1021 0.4747  -0.4324 1102 THR B CB  
4338 O OG1 . THR B 250 ? 0.5732 0.1943 1.8984 -0.1127 0.4645  -0.4161 1102 THR B OG1 
4339 C CG2 . THR B 250 ? 0.6026 0.2465 1.9612 -0.1298 0.5164  -0.5231 1102 THR B CG2 
4340 N N   . ARG B 251 ? 0.5126 0.1785 1.8366 -0.0494 0.4335  -0.3514 1103 ARG B N   
4341 C CA  . ARG B 251 ? 0.5027 0.1820 1.8548 -0.0322 0.4353  -0.3453 1103 ARG B CA  
4342 C C   . ARG B 251 ? 0.4669 0.1902 1.7008 -0.0364 0.4097  -0.3465 1103 ARG B C   
4343 O O   . ARG B 251 ? 0.4673 0.2099 1.7016 -0.0382 0.4248  -0.3777 1103 ARG B O   
4344 C CB  . ARG B 251 ? 0.5035 0.1636 1.9327 -0.0002 0.4162  -0.2707 1103 ARG B CB  
4345 C CG  . ARG B 251 ? 0.5820 0.1971 2.1509 0.0087  0.4454  -0.2648 1103 ARG B CG  
4346 C CD  . ARG B 251 ? 0.6159 0.2183 2.2566 0.0404  0.4213  -0.1825 1103 ARG B CD  
4347 N NE  . ARG B 251 ? 0.6134 0.2301 2.3116 0.0592  0.4253  -0.1775 1103 ARG B NE  
4348 C CZ  . ARG B 251 ? 0.5901 0.1863 2.4170 0.0663  0.4667  -0.2099 1103 ARG B CZ  
4349 N NH1 . ARG B 251 ? 0.6326 0.1923 2.5391 0.0544  0.5087  -0.2539 1103 ARG B NH1 
4350 N NH2 . ARG B 251 ? 0.5871 0.2009 2.4646 0.0844  0.4671  -0.2006 1103 ARG B NH2 
4351 N N   . LEU B 252 ? 0.4385 0.1768 1.5758 -0.0383 0.3729  -0.3125 1104 LEU B N   
4352 C CA  . LEU B 252 ? 0.4073 0.1842 1.4313 -0.0438 0.3486  -0.3130 1104 LEU B CA  
4353 C C   . LEU B 252 ? 0.4205 0.2215 1.3853 -0.0729 0.3688  -0.3810 1104 LEU B C   
4354 O O   . LEU B 252 ? 0.4152 0.2437 1.3378 -0.0787 0.3729  -0.4041 1104 LEU B O   
4355 C CB  . LEU B 252 ? 0.3783 0.1617 1.3268 -0.0378 0.3073  -0.2595 1104 LEU B CB  
4356 C CG  . LEU B 252 ? 0.4120 0.2299 1.2477 -0.0411 0.2786  -0.2500 1104 LEU B CG  
4357 C CD1 . LEU B 252 ? 0.4130 0.2466 1.2491 -0.0269 0.2705  -0.2340 1104 LEU B CD1 
4358 C CD2 . LEU B 252 ? 0.3791 0.1955 1.1645 -0.0355 0.2454  -0.2009 1104 LEU B CD2 
4359 N N   . VAL B 253 ? 0.4615 0.2547 1.4248 -0.0926 0.3814  -0.4122 1105 VAL B N   
4360 C CA  . VAL B 253 ? 0.4877 0.3079 1.4003 -0.1237 0.4007  -0.4790 1105 VAL B CA  
4361 C C   . VAL B 253 ? 0.5272 0.3529 1.4885 -0.1343 0.4416  -0.5370 1105 VAL B C   
4362 O O   . VAL B 253 ? 0.5552 0.4171 1.4513 -0.1530 0.4484  -0.5754 1105 VAL B O   
4363 C CB  . VAL B 253 ? 0.5310 0.3398 1.4548 -0.1436 0.4102  -0.5043 1105 VAL B CB  
4364 C CG1 . VAL B 253 ? 0.5567 0.3913 1.4583 -0.1782 0.4390  -0.5828 1105 VAL B CG1 
4365 C CG2 . VAL B 253 ? 0.5320 0.3520 1.3786 -0.1414 0.3713  -0.4618 1105 VAL B CG2 
4366 N N   . ASN B 254 ? 0.5393 0.3300 1.6171 -0.1225 0.4695  -0.5417 1106 ASN B N   
4367 C CA  . ASN B 254 ? 0.6084 0.4004 1.7497 -0.1312 0.5137  -0.5990 1106 ASN B CA  
4368 C C   . ASN B 254 ? 0.6181 0.4373 1.7282 -0.1217 0.5088  -0.5912 1106 ASN B C   
4369 O O   . ASN B 254 ? 0.6672 0.5107 1.7625 -0.1411 0.5376  -0.6472 1106 ASN B O   
4370 C CB  . ASN B 254 ? 0.6485 0.3938 1.9354 -0.1159 0.5435  -0.5976 1106 ASN B CB  
4371 C CG  . ASN B 254 ? 0.6856 0.4086 2.0232 -0.1393 0.5763  -0.6497 1106 ASN B CG  
4372 O OD1 . ASN B 254 ? 0.7329 0.4738 1.9961 -0.1644 0.5688  -0.6751 1106 ASN B OD1 
4373 N ND2 . ASN B 254 ? 0.7481 0.4323 2.2189 -0.1310 0.6133  -0.6657 1106 ASN B ND2 
4374 N N   . THR B 255 ? 0.6101 0.4273 1.7089 -0.0942 0.4731  -0.5233 1107 THR B N   
4375 C CA  . THR B 255 ? 0.6059 0.4489 1.6734 -0.0843 0.4636  -0.5087 1107 THR B CA  
4376 C C   . THR B 255 ? 0.5861 0.4707 1.5241 -0.1058 0.4497  -0.5271 1107 THR B C   
4377 O O   . THR B 255 ? 0.6033 0.5140 1.5178 -0.1170 0.4679  -0.5595 1107 THR B O   
4378 C CB  . THR B 255 ? 0.5920 0.4254 1.6757 -0.0523 0.4254  -0.4307 1107 THR B CB  
4379 O OG1 . THR B 255 ? 0.6266 0.4223 1.8118 -0.0348 0.4285  -0.4017 1107 THR B OG1 
4380 C CG2 . THR B 255 ? 0.6324 0.4825 1.7405 -0.0390 0.4283  -0.4222 1107 THR B CG2 
4381 N N   . LEU B 256 ? 0.5393 0.4307 1.3976 -0.1121 0.4191  -0.5060 1108 LEU B N   
4382 C CA  . LEU B 256 ? 0.5394 0.4701 1.2810 -0.1326 0.4047  -0.5205 1108 LEU B CA  
4383 C C   . LEU B 256 ? 0.5643 0.5193 1.2874 -0.1664 0.4398  -0.5944 1108 LEU B C   
4384 O O   . LEU B 256 ? 0.5569 0.5487 1.2096 -0.1821 0.4420  -0.6138 1108 LEU B O   
4385 C CB  . LEU B 256 ? 0.4870 0.4189 1.1628 -0.1311 0.3671  -0.4836 1108 LEU B CB  
4386 C CG  . LEU B 256 ? 0.5059 0.4237 1.1748 -0.1031 0.3301  -0.4133 1108 LEU B CG  
4387 C CD1 . LEU B 256 ? 0.4620 0.3763 1.0855 -0.1043 0.3026  -0.3868 1108 LEU B CD1 
4388 C CD2 . LEU B 256 ? 0.4528 0.3949 1.0626 -0.0961 0.3121  -0.3909 1108 LEU B CD2 
4389 N N   . LYS B 257 ? 0.6173 0.5530 1.4049 -0.1791 0.4685  -0.6360 1109 LYS B N   
4390 C CA  . LYS B 257 ? 0.6624 0.6224 1.4397 -0.2143 0.5054  -0.7128 1109 LYS B CA  
4391 C C   . LYS B 257 ? 0.6907 0.6659 1.4923 -0.2201 0.5402  -0.7501 1109 LYS B C   
4392 O O   . LYS B 257 ? 0.7140 0.7297 1.4518 -0.2490 0.5558  -0.7958 1109 LYS B O   
4393 C CB  . LYS B 257 ? 0.6853 0.6159 1.5435 -0.2258 0.5332  -0.7518 1109 LYS B CB  
4394 C CG  . LYS B 257 ? 0.6814 0.6160 1.4968 -0.2395 0.5124  -0.7490 1109 LYS B CG  
4395 C CD  . LYS B 257 ? 0.7185 0.6250 1.6213 -0.2553 0.5474  -0.7972 1109 LYS B CD  
4396 C CE  . LYS B 257 ? 0.7135 0.6220 1.5827 -0.2676 0.5259  -0.7901 1109 LYS B CE  
4397 N NZ  . LYS B 257 ? 0.7585 0.6448 1.7070 -0.2896 0.5630  -0.8466 1109 LYS B NZ  
4398 N N   . GLU B 258 ? 0.6826 0.6290 1.5752 -0.1931 0.5511  -0.7278 1110 GLU B N   
4399 C CA  . GLU B 258 ? 0.7100 0.6688 1.6397 -0.1941 0.5842  -0.7572 1110 GLU B CA  
4400 C C   . GLU B 258 ? 0.6860 0.6834 1.5226 -0.1955 0.5652  -0.7361 1110 GLU B C   
4401 O O   . GLU B 258 ? 0.7144 0.7313 1.5624 -0.2046 0.5954  -0.7688 1110 GLU B O   
4402 C CB  . GLU B 258 ? 0.7208 0.6404 1.7795 -0.1613 0.5950  -0.7295 1110 GLU B CB  
4403 C CG  . GLU B 258 ? 0.8041 0.6840 1.9800 -0.1614 0.6285  -0.7609 1110 GLU B CG  
4404 C CD  . GLU B 258 ? 0.8259 0.6652 2.1260 -0.1240 0.6258  -0.7121 1110 GLU B CD  
4405 O OE1 . GLU B 258 ? 0.8422 0.6815 2.1260 -0.0974 0.5860  -0.6429 1110 GLU B OE1 
4406 O OE2 . GLU B 258 ? 0.9620 0.7706 2.3798 -0.1222 0.6643  -0.7436 1110 GLU B OE2 
4407 N N   . GLY B 259 ? 0.5952 0.6025 1.3459 -0.1870 0.5183  -0.6825 1111 GLY B N   
4408 C CA  . GLY B 259 ? 0.6000 0.6395 1.2644 -0.1872 0.4976  -0.6561 1111 GLY B CA  
4409 C C   . GLY B 259 ? 0.5599 0.5836 1.2478 -0.1540 0.4695  -0.5922 1111 GLY B C   
4410 O O   . GLY B 259 ? 0.5411 0.5872 1.1663 -0.1526 0.4526  -0.5678 1111 GLY B O   
4411 N N   . LYS B 260 ? 0.5487 0.5357 1.3254 -0.1287 0.4633  -0.5634 1112 LYS B N   
4412 C CA  . LYS B 260 ? 0.4940 0.4690 1.2997 -0.0982 0.4350  -0.5025 1112 LYS B CA  
4413 C C   . LYS B 260 ? 0.4598 0.4364 1.1851 -0.0890 0.3863  -0.4475 1112 LYS B C   
4414 O O   . LYS B 260 ? 0.4315 0.3964 1.1343 -0.0916 0.3710  -0.4386 1112 LYS B O   
4415 C CB  . LYS B 260 ? 0.4890 0.4288 1.4174 -0.0755 0.4435  -0.4866 1112 LYS B CB  
4416 C CG  . LYS B 260 ? 0.5368 0.4737 1.5649 -0.0760 0.4896  -0.5298 1112 LYS B CG  
4417 C CD  . LYS B 260 ? 0.5057 0.4057 1.6614 -0.0534 0.4978  -0.5117 1112 LYS B CD  
4418 C CE  . LYS B 260 ? 0.5391 0.4377 1.8061 -0.0486 0.5418  -0.5472 1112 LYS B CE  
4419 N NZ  . LYS B 260 ? 0.5455 0.4074 1.9484 -0.0247 0.5505  -0.5260 1112 LYS B NZ  
4420 N N   . ARG B 261 ? 0.4329 0.4235 1.1225 -0.0786 0.3644  -0.4124 1113 ARG B N   
4421 C CA  . ARG B 261 ? 0.4003 0.3943 1.0155 -0.0707 0.3218  -0.3641 1113 ARG B CA  
4422 C C   . ARG B 261 ? 0.3705 0.3585 1.0214 -0.0466 0.2993  -0.3156 1113 ARG B C   
4423 O O   . ARG B 261 ? 0.3550 0.3426 1.0803 -0.0372 0.3159  -0.3197 1113 ARG B O   
4424 C CB  . ARG B 261 ? 0.4365 0.4610 0.9514 -0.0891 0.3169  -0.3743 1113 ARG B CB  
4425 C CG  . ARG B 261 ? 0.4405 0.4821 0.9085 -0.1163 0.3352  -0.4205 1113 ARG B CG  
4426 C CD  . ARG B 261 ? 0.4716 0.5026 0.9149 -0.1186 0.3161  -0.4123 1113 ARG B CD  
4427 N NE  . ARG B 261 ? 0.4570 0.5115 0.8538 -0.1469 0.3309  -0.4571 1113 ARG B NE  
4428 C CZ  . ARG B 261 ? 0.4973 0.5471 0.9361 -0.1623 0.3591  -0.5045 1113 ARG B CZ  
4429 N NH1 . ARG B 261 ? 0.4282 0.4460 0.9641 -0.1507 0.3785  -0.5132 1113 ARG B NH1 
4430 N NH2 . ARG B 261 ? 0.5051 0.5841 0.8906 -0.1907 0.3682  -0.5438 1113 ARG B NH2 
4431 N N   . LEU B 262 ? 0.3550 0.3411 0.9550 -0.0377 0.2620  -0.2715 1114 LEU B N   
4432 C CA  . LEU B 262 ? 0.3240 0.3105 0.9432 -0.0188 0.2365  -0.2259 1114 LEU B CA  
4433 C C   . LEU B 262 ? 0.3277 0.3363 0.9382 -0.0222 0.2453  -0.2341 1114 LEU B C   
4434 O O   . LEU B 262 ? 0.3241 0.3488 0.8727 -0.0393 0.2566  -0.2585 1114 LEU B O   
4435 C CB  . LEU B 262 ? 0.3256 0.3110 0.8754 -0.0148 0.1992  -0.1871 1114 LEU B CB  
4436 C CG  . LEU B 262 ? 0.3656 0.3306 0.9246 -0.0099 0.1865  -0.1696 1114 LEU B CG  
4437 C CD1 . LEU B 262 ? 0.3532 0.3218 0.8281 -0.0137 0.1600  -0.1495 1114 LEU B CD1 
4438 C CD2 . LEU B 262 ? 0.3634 0.3155 0.9995 0.0092  0.1754  -0.1335 1114 LEU B CD2 
4439 N N   . PRO B 263 ? 0.3243 0.3365 0.9967 -0.0069 0.2393  -0.2114 1115 PRO B N   
4440 C CA  . PRO B 263 ? 0.3210 0.3545 0.9999 -0.0103 0.2513  -0.2211 1115 PRO B CA  
4441 C C   . PRO B 263 ? 0.2753 0.3222 0.8702 -0.0159 0.2281  -0.2004 1115 PRO B C   
4442 O O   . PRO B 263 ? 0.2794 0.3190 0.8262 -0.0121 0.1983  -0.1717 1115 PRO B O   
4443 C CB  . PRO B 263 ? 0.3145 0.3485 1.0900 0.0096  0.2449  -0.1962 1115 PRO B CB  
4444 C CG  . PRO B 263 ? 0.3058 0.3254 1.0814 0.0226  0.2117  -0.1544 1115 PRO B CG  
4445 C CD  . PRO B 263 ? 0.3278 0.3281 1.0669 0.0135  0.2191  -0.1723 1115 PRO B CD  
4446 N N   . CYS B 264 ? 0.2611 0.3269 0.8420 -0.0256 0.2439  -0.2157 1116 CYS B N   
4447 C CA  . CYS B 264 ? 0.2799 0.3566 0.7941 -0.0306 0.2249  -0.1950 1116 CYS B CA  
4448 C C   . CYS B 264 ? 0.2705 0.3468 0.8095 -0.0151 0.1927  -0.1547 1116 CYS B C   
4449 O O   . CYS B 264 ? 0.2982 0.3825 0.9138 -0.0047 0.1949  -0.1483 1116 CYS B O   
4450 C CB  . CYS B 264 ? 0.2643 0.3615 0.7744 -0.0435 0.2509  -0.2165 1116 CYS B CB  
4451 S SG  . CYS B 264 ? 0.3354 0.4420 0.7648 -0.0522 0.2326  -0.1928 1116 CYS B SG  
4452 N N   . PRO B 265 ? 0.2605 0.3307 0.7386 -0.0142 0.1632  -0.1285 1117 PRO B N   
4453 C CA  . PRO B 265 ? 0.2600 0.3347 0.7553 -0.0037 0.1336  -0.0944 1117 PRO B CA  
4454 C C   . PRO B 265 ? 0.2768 0.3715 0.7984 -0.0058 0.1364  -0.0924 1117 PRO B C   
4455 O O   . PRO B 265 ? 0.2292 0.3310 0.7252 -0.0179 0.1566  -0.1114 1117 PRO B O   
4456 C CB  . PRO B 265 ? 0.2146 0.2806 0.6304 -0.0077 0.1103  -0.0776 1117 PRO B CB  
4457 C CG  . PRO B 265 ? 0.2849 0.3392 0.6594 -0.0144 0.1221  -0.0956 1117 PRO B CG  
4458 C CD  . PRO B 265 ? 0.3087 0.3707 0.7048 -0.0232 0.1559  -0.1295 1117 PRO B CD  
4459 N N   . PRO B 266 ? 0.2807 0.3875 0.8548 0.0045  0.1165  -0.0687 1118 PRO B N   
4460 C CA  . PRO B 266 ? 0.2866 0.4151 0.8837 0.0011  0.1148  -0.0651 1118 PRO B CA  
4461 C C   . PRO B 266 ? 0.2594 0.3865 0.7816 -0.0125 0.1111  -0.0658 1118 PRO B C   
4462 O O   . PRO B 266 ? 0.1875 0.3012 0.6484 -0.0146 0.0938  -0.0546 1118 PRO B O   
4463 C CB  . PRO B 266 ? 0.3209 0.4634 0.9627 0.0125  0.0827  -0.0329 1118 PRO B CB  
4464 C CG  . PRO B 266 ? 0.3019 0.4320 0.9827 0.0252  0.0813  -0.0248 1118 PRO B CG  
4465 C CD  . PRO B 266 ? 0.3176 0.4219 0.9331 0.0185  0.0938  -0.0421 1118 PRO B CD  
4466 N N   . ASN B 267 ? 0.2483 0.3881 0.7796 -0.0220 0.1312  -0.0803 1119 ASN B N   
4467 C CA  . ASN B 267 ? 0.2737 0.4130 0.7484 -0.0354 0.1317  -0.0792 1119 ASN B CA  
4468 C C   . ASN B 267 ? 0.2830 0.4042 0.6788 -0.0439 0.1404  -0.0860 1119 ASN B C   
4469 O O   . ASN B 267 ? 0.3238 0.4405 0.6723 -0.0529 0.1374  -0.0789 1119 ASN B O   
4470 C CB  . ASN B 267 ? 0.2509 0.3952 0.7184 -0.0346 0.1001  -0.0560 1119 ASN B CB  
4471 C CG  . ASN B 267 ? 0.2922 0.4622 0.8365 -0.0281 0.0875  -0.0465 1119 ASN B CG  
4472 O OD1 . ASN B 267 ? 0.3269 0.5035 0.8866 -0.0201 0.0596  -0.0267 1119 ASN B OD1 
4473 N ND2 . ASN B 267 ? 0.1737 0.3619 0.7674 -0.0322 0.1079  -0.0592 1119 ASN B ND2 
4474 N N   . CYS B 268 ? 0.2833 0.3959 0.6697 -0.0419 0.1518  -0.0997 1120 CYS B N   
4475 C CA  . CYS B 268 ? 0.2782 0.3802 0.5937 -0.0506 0.1581  -0.1059 1120 CYS B CA  
4476 C C   . CYS B 268 ? 0.3123 0.4274 0.6168 -0.0653 0.1904  -0.1277 1120 CYS B C   
4477 O O   . CYS B 268 ? 0.2860 0.4111 0.6356 -0.0668 0.2141  -0.1510 1120 CYS B O   
4478 C CB  . CYS B 268 ? 0.3033 0.3937 0.6142 -0.0443 0.1544  -0.1121 1120 CYS B CB  
4479 S SG  . CYS B 268 ? 0.2704 0.3562 0.5026 -0.0559 0.1611  -0.1222 1120 CYS B SG  
4480 N N   . PRO B 269 ? 0.3100 0.4260 0.5573 -0.0771 0.1934  -0.1200 1121 PRO B N   
4481 C CA  . PRO B 269 ? 0.3444 0.4765 0.5757 -0.0935 0.2246  -0.1382 1121 PRO B CA  
4482 C C   . PRO B 269 ? 0.3403 0.4779 0.5485 -0.1006 0.2409  -0.1630 1121 PRO B C   
4483 O O   . PRO B 269 ? 0.3084 0.4352 0.4878 -0.0957 0.2246  -0.1587 1121 PRO B O   
4484 C CB  . PRO B 269 ? 0.3602 0.4894 0.5326 -0.1030 0.2192  -0.1164 1121 PRO B CB  
4485 C CG  . PRO B 269 ? 0.3872 0.4989 0.5603 -0.0914 0.1889  -0.0920 1121 PRO B CG  
4486 C CD  . PRO B 269 ? 0.2962 0.3997 0.4947 -0.0769 0.1715  -0.0949 1121 PRO B CD  
4487 N N   . ASP B 270 ? 0.3750 0.5310 0.5977 -0.1136 0.2740  -0.1910 1122 ASP B N   
4488 C CA  . ASP B 270 ? 0.4159 0.5811 0.6217 -0.1241 0.2937  -0.2223 1122 ASP B CA  
4489 C C   . ASP B 270 ? 0.4127 0.5803 0.5362 -0.1336 0.2811  -0.2131 1122 ASP B C   
4490 O O   . ASP B 270 ? 0.3891 0.5541 0.5029 -0.1335 0.2775  -0.2274 1122 ASP B O   
4491 C CB  . ASP B 270 ? 0.4435 0.6330 0.6648 -0.1419 0.3347  -0.2549 1122 ASP B CB  
4492 C CG  . ASP B 270 ? 0.5499 0.7535 0.7447 -0.1583 0.3573  -0.2920 1122 ASP B CG  
4493 O OD1 . ASP B 270 ? 0.5045 0.6963 0.7329 -0.1499 0.3555  -0.3096 1122 ASP B OD1 
4494 O OD2 . ASP B 270 ? 0.5754 0.8030 0.7139 -0.1809 0.3763  -0.3026 1122 ASP B OD2 
4495 N N   . GLU B 271 ? 0.4260 0.5991 0.4964 -0.1415 0.2743  -0.1879 1123 GLU B N   
4496 C CA  . GLU B 271 ? 0.4774 0.6575 0.4736 -0.1501 0.2612  -0.1737 1123 GLU B CA  
4497 C C   . GLU B 271 ? 0.4214 0.5803 0.4106 -0.1334 0.2284  -0.1552 1123 GLU B C   
4498 O O   . GLU B 271 ? 0.4588 0.6255 0.4049 -0.1386 0.2193  -0.1553 1123 GLU B O   
4499 C CB  . GLU B 271 ? 0.5310 0.7215 0.4777 -0.1619 0.2626  -0.1462 1123 GLU B CB  
4500 C CG  . GLU B 271 ? 0.5653 0.7400 0.5403 -0.1538 0.2573  -0.1213 1123 GLU B CG  
4501 C CD  . GLU B 271 ? 0.6431 0.8303 0.6603 -0.1625 0.2871  -0.1402 1123 GLU B CD  
4502 O OE1 . GLU B 271 ? 0.7386 0.9462 0.7250 -0.1818 0.3097  -0.1405 1123 GLU B OE1 
4503 O OE2 . GLU B 271 ? 0.5306 0.7095 0.6135 -0.1505 0.2880  -0.1535 1123 GLU B OE2 
4504 N N   . VAL B 272 ? 0.3784 0.5147 0.4105 -0.1152 0.2113  -0.1408 1124 VAL B N   
4505 C CA  . VAL B 272 ? 0.3616 0.4790 0.3949 -0.1002 0.1844  -0.1285 1124 VAL B CA  
4506 C C   . VAL B 272 ? 0.3473 0.4647 0.4076 -0.0988 0.1918  -0.1562 1124 VAL B C   
4507 O O   . VAL B 272 ? 0.3480 0.4654 0.3804 -0.1001 0.1822  -0.1588 1124 VAL B O   
4508 C CB  . VAL B 272 ? 0.3202 0.4182 0.3900 -0.0844 0.1653  -0.1075 1124 VAL B CB  
4509 C CG1 . VAL B 272 ? 0.3296 0.4113 0.4003 -0.0712 0.1409  -0.0972 1124 VAL B CG1 
4510 C CG2 . VAL B 272 ? 0.3586 0.4534 0.4043 -0.0872 0.1591  -0.0832 1124 VAL B CG2 
4511 N N   . TYR B 273 ? 0.3047 0.4226 0.4245 -0.0966 0.2100  -0.1769 1125 TYR B N   
4512 C CA  . TYR B 273 ? 0.3332 0.4482 0.4932 -0.0954 0.2226  -0.2052 1125 TYR B CA  
4513 C C   . TYR B 273 ? 0.3780 0.5106 0.4981 -0.1143 0.2399  -0.2347 1125 TYR B C   
4514 O O   . TYR B 273 ? 0.3611 0.4875 0.4908 -0.1139 0.2387  -0.2500 1125 TYR B O   
4515 C CB  . TYR B 273 ? 0.3554 0.4718 0.5919 -0.0911 0.2446  -0.2231 1125 TYR B CB  
4516 C CG  . TYR B 273 ? 0.3379 0.4457 0.6326 -0.0866 0.2584  -0.2491 1125 TYR B CG  
4517 C CD1 . TYR B 273 ? 0.3578 0.4454 0.6704 -0.0730 0.2374  -0.2348 1125 TYR B CD1 
4518 C CD2 . TYR B 273 ? 0.4062 0.5253 0.7423 -0.0966 0.2946  -0.2882 1125 TYR B CD2 
4519 C CE1 . TYR B 273 ? 0.3333 0.4096 0.7055 -0.0688 0.2512  -0.2558 1125 TYR B CE1 
4520 C CE2 . TYR B 273 ? 0.4501 0.5578 0.8490 -0.0922 0.3099  -0.3131 1125 TYR B CE2 
4521 C CZ  . TYR B 273 ? 0.3929 0.4780 0.8105 -0.0779 0.2875  -0.2951 1125 TYR B CZ  
4522 O OH  . TYR B 273 ? 0.4148 0.4858 0.8998 -0.0736 0.3039  -0.3171 1125 TYR B OH  
4523 N N   . GLN B 274 ? 0.3685 0.5249 0.4437 -0.1326 0.2556  -0.2424 1126 GLN B N   
4524 C CA  . GLN B 274 ? 0.4394 0.6205 0.4677 -0.1544 0.2697  -0.2698 1126 GLN B CA  
4525 C C   . GLN B 274 ? 0.4568 0.6392 0.4331 -0.1542 0.2423  -0.2522 1126 GLN B C   
4526 O O   . GLN B 274 ? 0.4762 0.6692 0.4421 -0.1647 0.2468  -0.2779 1126 GLN B O   
4527 C CB  . GLN B 274 ? 0.4573 0.6687 0.4430 -0.1763 0.2918  -0.2777 1126 GLN B CB  
4528 C CG  . GLN B 274 ? 0.4960 0.7137 0.5337 -0.1820 0.3272  -0.3066 1126 GLN B CG  
4529 C CD  . GLN B 274 ? 0.5453 0.7587 0.6423 -0.1831 0.3505  -0.3516 1126 GLN B CD  
4530 O OE1 . GLN B 274 ? 0.5788 0.8029 0.6527 -0.1965 0.3564  -0.3787 1126 GLN B OE1 
4531 N NE2 . GLN B 274 ? 0.5182 0.7166 0.6969 -0.1691 0.3636  -0.3594 1126 GLN B NE2 
4532 N N   . LEU B 275 ? 0.4389 0.6110 0.3887 -0.1425 0.2152  -0.2109 1127 LEU B N   
4533 C CA  . LEU B 275 ? 0.4442 0.6153 0.3573 -0.1384 0.1884  -0.1917 1127 LEU B CA  
4534 C C   . LEU B 275 ? 0.4096 0.5599 0.3627 -0.1263 0.1797  -0.2018 1127 LEU B C   
4535 O O   . LEU B 275 ? 0.4085 0.5671 0.3416 -0.1318 0.1718  -0.2102 1127 LEU B O   
4536 C CB  . LEU B 275 ? 0.4197 0.5792 0.3105 -0.1264 0.1649  -0.1481 1127 LEU B CB  
4537 C CG  . LEU B 275 ? 0.4643 0.6446 0.3069 -0.1388 0.1682  -0.1290 1127 LEU B CG  
4538 C CD1 . LEU B 275 ? 0.4443 0.6038 0.2895 -0.1251 0.1526  -0.0911 1127 LEU B CD1 
4539 C CD2 . LEU B 275 ? 0.5100 0.7197 0.2968 -0.1521 0.1590  -0.1254 1127 LEU B CD2 
4540 N N   . MET B 276 ? 0.3989 0.5248 0.4099 -0.1110 0.1811  -0.1994 1128 MET B N   
4541 C CA  . MET B 276 ? 0.3700 0.4753 0.4273 -0.0996 0.1761  -0.2058 1128 MET B CA  
4542 C C   . MET B 276 ? 0.3813 0.4943 0.4609 -0.1126 0.1993  -0.2476 1128 MET B C   
4543 O O   . MET B 276 ? 0.3923 0.4975 0.4800 -0.1117 0.1930  -0.2545 1128 MET B O   
4544 C CB  . MET B 276 ? 0.3470 0.4320 0.4637 -0.0825 0.1738  -0.1919 1128 MET B CB  
4545 C CG  . MET B 276 ? 0.3613 0.4247 0.5268 -0.0690 0.1650  -0.1872 1128 MET B CG  
4546 S SD  . MET B 276 ? 0.3960 0.4461 0.6369 -0.0520 0.1639  -0.1722 1128 MET B SD  
4547 C CE  . MET B 276 ? 0.3187 0.3691 0.5236 -0.0452 0.1381  -0.1357 1128 MET B CE  
4548 N N   . ARG B 277 ? 0.3933 0.5216 0.4848 -0.1260 0.2281  -0.2775 1129 ARG B N   
4549 C CA  . ARG B 277 ? 0.4221 0.5604 0.5343 -0.1423 0.2554  -0.3246 1129 ARG B CA  
4550 C C   . ARG B 277 ? 0.4186 0.5829 0.4679 -0.1625 0.2505  -0.3396 1129 ARG B C   
4551 O O   . ARG B 277 ? 0.4469 0.6119 0.5139 -0.1720 0.2608  -0.3709 1129 ARG B O   
4552 C CB  . ARG B 277 ? 0.4572 0.6100 0.5932 -0.1541 0.2902  -0.3552 1129 ARG B CB  
4553 C CG  . ARG B 277 ? 0.4436 0.5742 0.6632 -0.1356 0.3005  -0.3513 1129 ARG B CG  
4554 C CD  . ARG B 277 ? 0.5863 0.7335 0.8382 -0.1491 0.3407  -0.3900 1129 ARG B CD  
4555 N NE  . ARG B 277 ? 0.7105 0.8615 0.9928 -0.1641 0.3710  -0.4414 1129 ARG B NE  
4556 C CZ  . ARG B 277 ? 0.7333 0.8599 1.1002 -0.1529 0.3836  -0.4580 1129 ARG B CZ  
4557 N NH1 . ARG B 277 ? 0.6863 0.7855 1.1161 -0.1259 0.3665  -0.4241 1129 ARG B NH1 
4558 N NH2 . ARG B 277 ? 0.7900 0.9209 1.1808 -0.1702 0.4141  -0.5093 1129 ARG B NH2 
4559 N N   . LYS B 278 ? 0.4006 0.5865 0.3810 -0.1687 0.2335  -0.3152 1130 LYS B N   
4560 C CA  . LYS B 278 ? 0.4379 0.6543 0.3589 -0.1865 0.2231  -0.3216 1130 LYS B CA  
4561 C C   . LYS B 278 ? 0.4139 0.6167 0.3401 -0.1762 0.1985  -0.3085 1130 LYS B C   
4562 O O   . LYS B 278 ? 0.4789 0.7067 0.3738 -0.1918 0.1930  -0.3234 1130 LYS B O   
4563 C CB  . LYS B 278 ? 0.4619 0.7056 0.3147 -0.1942 0.2105  -0.2924 1130 LYS B CB  
4564 C CG  . LYS B 278 ? 0.4967 0.7673 0.3281 -0.2147 0.2385  -0.3131 1130 LYS B CG  
4565 C CD  . LYS B 278 ? 0.5921 0.8899 0.3559 -0.2229 0.2249  -0.2780 1130 LYS B CD  
4566 C CE  . LYS B 278 ? 0.6019 0.9274 0.3416 -0.2448 0.2544  -0.2954 1130 LYS B CE  
4567 N NZ  . LYS B 278 ? 0.6535 1.0155 0.3731 -0.2747 0.2786  -0.3470 1130 LYS B NZ  
4568 N N   . CYS B 279 ? 0.4239 0.5911 0.3884 -0.1517 0.1840  -0.2811 1131 CYS B N   
4569 C CA  . CYS B 279 ? 0.3883 0.5375 0.3715 -0.1414 0.1669  -0.2722 1131 CYS B CA  
4570 C C   . CYS B 279 ? 0.4073 0.5444 0.4433 -0.1472 0.1862  -0.3088 1131 CYS B C   
4571 O O   . CYS B 279 ? 0.3595 0.4921 0.4018 -0.1480 0.1771  -0.3116 1131 CYS B O   
4572 C CB  . CYS B 279 ? 0.3739 0.4915 0.3809 -0.1163 0.1485  -0.2332 1131 CYS B CB  
4573 S SG  . CYS B 279 ? 0.3521 0.4763 0.3088 -0.1082 0.1264  -0.1915 1131 CYS B SG  
4574 N N   . TRP B 280 ? 0.4438 0.5752 0.5225 -0.1515 0.2146  -0.3369 1132 TRP B N   
4575 C CA  . TRP B 280 ? 0.4205 0.5332 0.5656 -0.1535 0.2366  -0.3694 1132 TRP B CA  
4576 C C   . TRP B 280 ? 0.4547 0.5913 0.6005 -0.1811 0.2685  -0.4264 1132 TRP B C   
4577 O O   . TRP B 280 ? 0.4082 0.5281 0.6198 -0.1822 0.2956  -0.4569 1132 TRP B O   
4578 C CB  . TRP B 280 ? 0.4296 0.5120 0.6457 -0.1333 0.2457  -0.3568 1132 TRP B CB  
4579 C CG  . TRP B 280 ? 0.3942 0.4545 0.6176 -0.1090 0.2172  -0.3066 1132 TRP B CG  
4580 C CD1 . TRP B 280 ? 0.3866 0.4387 0.5862 -0.1013 0.1907  -0.2787 1132 TRP B CD1 
4581 C CD2 . TRP B 280 ? 0.3956 0.4420 0.6550 -0.0909 0.2132  -0.2807 1132 TRP B CD2 
4582 N NE1 . TRP B 280 ? 0.3436 0.3780 0.5569 -0.0811 0.1715  -0.2387 1132 TRP B NE1 
4583 C CE2 . TRP B 280 ? 0.3944 0.4262 0.6434 -0.0747 0.1831  -0.2384 1132 TRP B CE2 
4584 C CE3 . TRP B 280 ? 0.3678 0.4163 0.6670 -0.0883 0.2322  -0.2901 1132 TRP B CE3 
4585 C CZ2 . TRP B 280 ? 0.2998 0.3207 0.5741 -0.0575 0.1700  -0.2063 1132 TRP B CZ2 
4586 C CZ3 . TRP B 280 ? 0.3912 0.4285 0.7208 -0.0693 0.2179  -0.2558 1132 TRP B CZ3 
4587 C CH2 . TRP B 280 ? 0.3509 0.3757 0.6658 -0.0550 0.1863  -0.2147 1132 TRP B CH2 
4588 N N   . GLU B 281 ? 0.4661 0.6431 0.5419 -0.2039 0.2653  -0.4406 1133 GLU B N   
4589 C CA  . GLU B 281 ? 0.4967 0.7025 0.5650 -0.2350 0.2933  -0.4988 1133 GLU B CA  
4590 C C   . GLU B 281 ? 0.5078 0.6954 0.6221 -0.2378 0.2967  -0.5214 1133 GLU B C   
4591 O O   . GLU B 281 ? 0.4589 0.6332 0.5693 -0.2243 0.2693  -0.4891 1133 GLU B O   
4592 C CB  . GLU B 281 ? 0.5318 0.7902 0.5098 -0.2593 0.2809  -0.5011 1133 GLU B CB  
4593 C CG  . GLU B 281 ? 0.6223 0.9001 0.5443 -0.2565 0.2706  -0.4663 1133 GLU B CG  
4594 C CD  . GLU B 281 ? 0.6587 0.9425 0.5942 -0.2660 0.3052  -0.4922 1133 GLU B CD  
4595 O OE1 . GLU B 281 ? 0.6378 0.9273 0.6059 -0.2841 0.3393  -0.5465 1133 GLU B OE1 
4596 O OE2 . GLU B 281 ? 0.6128 0.8964 0.5288 -0.2563 0.3000  -0.4598 1133 GLU B OE2 
4597 N N   . PHE B 282 ? 0.5349 0.7206 0.6961 -0.2553 0.3315  -0.5766 1134 PHE B N   
4598 C CA  . PHE B 282 ? 0.5723 0.7354 0.7876 -0.2579 0.3378  -0.5980 1134 PHE B CA  
4599 C C   . PHE B 282 ? 0.6105 0.8030 0.7709 -0.2739 0.3134  -0.5979 1134 PHE B C   
4600 O O   . PHE B 282 ? 0.5833 0.7537 0.7661 -0.2615 0.2956  -0.5753 1134 PHE B O   
4601 C CB  . PHE B 282 ? 0.6253 0.7825 0.9040 -0.2773 0.3837  -0.6638 1134 PHE B CB  
4602 C CG  . PHE B 282 ? 0.6082 0.7218 0.9756 -0.2685 0.3952  -0.6734 1134 PHE B CG  
4603 C CD1 . PHE B 282 ? 0.5932 0.6590 1.0400 -0.2377 0.3982  -0.6418 1134 PHE B CD1 
4604 C CD2 . PHE B 282 ? 0.6625 0.7845 1.0360 -0.2917 0.4024  -0.7118 1134 PHE B CD2 
4605 C CE1 . PHE B 282 ? 0.5556 0.5807 1.0862 -0.2292 0.4086  -0.6441 1134 PHE B CE1 
4606 C CE2 . PHE B 282 ? 0.6491 0.7281 1.1085 -0.2841 0.4148  -0.7180 1134 PHE B CE2 
4607 C CZ  . PHE B 282 ? 0.5593 0.5886 1.0971 -0.2521 0.4179  -0.6819 1134 PHE B CZ  
4608 N N   . GLN B 283 ? 0.6695 0.9147 0.7594 -0.3020 0.3124  -0.6219 1135 GLN B N   
4609 C CA  . GLN B 283 ? 0.6792 0.9622 0.7175 -0.3196 0.2882  -0.6234 1135 GLN B CA  
4610 C C   . GLN B 283 ? 0.6225 0.9173 0.6029 -0.3008 0.2464  -0.5597 1135 GLN B C   
4611 O O   . GLN B 283 ? 0.6171 0.9270 0.5543 -0.2967 0.2407  -0.5365 1135 GLN B O   
4612 C CB  . GLN B 283 ? 0.7523 1.0937 0.7400 -0.3606 0.3039  -0.6766 1135 GLN B CB  
4613 C CG  . GLN B 283 ? 0.7796 1.1145 0.8226 -0.3849 0.3493  -0.7500 1135 GLN B CG  
4614 C CD  . GLN B 283 ? 0.7778 1.0886 0.8819 -0.3891 0.3547  -0.7747 1135 GLN B CD  
4615 O OE1 . GLN B 283 ? 0.7611 1.0886 0.8407 -0.3920 0.3260  -0.7576 1135 GLN B OE1 
4616 N NE2 . GLN B 283 ? 0.7903 1.0616 0.9796 -0.3896 0.3931  -0.8146 1135 GLN B NE2 
4617 N N   . PRO B 284 ? 0.5667 0.8538 0.5506 -0.2895 0.2196  -0.5319 1136 PRO B N   
4618 C CA  . PRO B 284 ? 0.5437 0.8393 0.4829 -0.2707 0.1825  -0.4741 1136 PRO B CA  
4619 C C   . PRO B 284 ? 0.5728 0.9258 0.4331 -0.2864 0.1641  -0.4626 1136 PRO B C   
4620 O O   . PRO B 284 ? 0.5761 0.9291 0.4049 -0.2687 0.1435  -0.4149 1136 PRO B O   
4621 C CB  . PRO B 284 ? 0.5103 0.7963 0.4738 -0.2653 0.1655  -0.4648 1136 PRO B CB  
4622 C CG  . PRO B 284 ? 0.5478 0.8361 0.5492 -0.2889 0.1897  -0.5197 1136 PRO B CG  
4623 C CD  . PRO B 284 ? 0.5852 0.8524 0.6217 -0.2932 0.2250  -0.5530 1136 PRO B CD  
4624 N N   . SER B 285 ? 0.6411 1.0430 0.4716 -0.3200 0.1715  -0.5047 1137 SER B N   
4625 C CA  . SER B 285 ? 0.6803 1.1448 0.4338 -0.3395 0.1545  -0.4949 1137 SER B CA  
4626 C C   . SER B 285 ? 0.6940 1.1659 0.4116 -0.3407 0.1668  -0.4842 1137 SER B C   
4627 O O   . SER B 285 ? 0.7035 1.2166 0.3595 -0.3471 0.1474  -0.4542 1137 SER B O   
4628 C CB  . SER B 285 ? 0.7396 1.2591 0.4701 -0.3796 0.1617  -0.5484 1137 SER B CB  
4629 O OG  . SER B 285 ? 0.7405 1.2511 0.4985 -0.3999 0.2030  -0.6089 1137 SER B OG  
4630 N N   . ASN B 286 ? 0.6722 1.1064 0.4322 -0.3354 0.1993  -0.5077 1138 ASN B N   
4631 C CA  . ASN B 286 ? 0.6893 1.1232 0.4286 -0.3337 0.2145  -0.4979 1138 ASN B CA  
4632 C C   . ASN B 286 ? 0.6394 1.0348 0.3883 -0.2985 0.1974  -0.4384 1138 ASN B C   
4633 O O   . ASN B 286 ? 0.6490 1.0552 0.3642 -0.2981 0.1992  -0.4167 1138 ASN B O   
4634 C CB  . ASN B 286 ? 0.7020 1.1140 0.4921 -0.3428 0.2588  -0.5510 1138 ASN B CB  
4635 C CG  . ASN B 286 ? 0.7624 1.2163 0.5386 -0.3832 0.2842  -0.6185 1138 ASN B CG  
4636 O OD1 . ASN B 286 ? 0.7048 1.2157 0.4164 -0.4095 0.2695  -0.6252 1138 ASN B OD1 
4637 N ND2 . ASN B 286 ? 0.7205 1.1475 0.5607 -0.3888 0.3232  -0.6695 1138 ASN B ND2 
4638 N N   . ARG B 287 ? 0.5952 0.9468 0.3907 -0.2712 0.1832  -0.4145 1139 ARG B N   
4639 C CA  . ARG B 287 ? 0.5247 0.8363 0.3386 -0.2395 0.1712  -0.3668 1139 ARG B CA  
4640 C C   . ARG B 287 ? 0.5389 0.8703 0.2983 -0.2325 0.1447  -0.3176 1139 ARG B C   
4641 O O   . ARG B 287 ? 0.5254 0.8962 0.2409 -0.2443 0.1251  -0.3076 1139 ARG B O   
4642 C CB  . ARG B 287 ? 0.5123 0.7820 0.3772 -0.2162 0.1587  -0.3511 1139 ARG B CB  
4643 C CG  . ARG B 287 ? 0.5363 0.7696 0.4713 -0.2121 0.1845  -0.3817 1139 ARG B CG  
4644 C CD  . ARG B 287 ? 0.4713 0.6733 0.4489 -0.1969 0.1727  -0.3698 1139 ARG B CD  
4645 N NE  . ARG B 287 ? 0.4610 0.6400 0.5025 -0.2023 0.1993  -0.4080 1139 ARG B NE  
4646 C CZ  . ARG B 287 ? 0.4568 0.6143 0.5404 -0.1991 0.1985  -0.4129 1139 ARG B CZ  
4647 N NH1 . ARG B 287 ? 0.3732 0.5298 0.4408 -0.1901 0.1723  -0.3829 1139 ARG B NH1 
4648 N NH2 . ARG B 287 ? 0.4602 0.5958 0.6072 -0.2048 0.2261  -0.4478 1139 ARG B NH2 
4649 N N   . THR B 288 ? 0.5397 0.8433 0.3084 -0.2127 0.1434  -0.2854 1140 THR B N   
4650 C CA  . THR B 288 ? 0.5336 0.8452 0.2639 -0.2023 0.1202  -0.2357 1140 THR B CA  
4651 C C   . THR B 288 ? 0.4900 0.7981 0.2203 -0.1879 0.0900  -0.2067 1140 THR B C   
4652 O O   . THR B 288 ? 0.4311 0.7169 0.1986 -0.1791 0.0877  -0.2174 1140 THR B O   
4653 C CB  . THR B 288 ? 0.5104 0.7873 0.2615 -0.1834 0.1258  -0.2105 1140 THR B CB  
4654 O OG1 . THR B 288 ? 0.5253 0.8116 0.2401 -0.1773 0.1075  -0.1662 1140 THR B OG1 
4655 C CG2 . THR B 288 ? 0.4721 0.7023 0.2781 -0.1591 0.1209  -0.2025 1140 THR B CG2 
4656 N N   . SER B 289 ? 0.4976 0.8299 0.1889 -0.1863 0.0685  -0.1698 1141 SER B N   
4657 C CA  . SER B 289 ? 0.4616 0.7863 0.1607 -0.1684 0.0419  -0.1370 1141 SER B CA  
4658 C C   . SER B 289 ? 0.3998 0.6778 0.1261 -0.1427 0.0396  -0.1076 1141 SER B C   
4659 O O   . SER B 289 ? 0.3437 0.6049 0.0734 -0.1406 0.0539  -0.1054 1141 SER B O   
4660 C CB  . SER B 289 ? 0.4679 0.8386 0.1229 -0.1760 0.0201  -0.1072 1141 SER B CB  
4661 O OG  . SER B 289 ? 0.4910 0.8630 0.1220 -0.1731 0.0202  -0.0745 1141 SER B OG  
4662 N N   . PHE B 290 ? 0.3588 0.6186 0.1057 -0.1250 0.0228  -0.0882 1142 PHE B N   
4663 C CA  . PHE B 290 ? 0.3527 0.5767 0.1178 -0.1034 0.0174  -0.0585 1142 PHE B CA  
4664 C C   . PHE B 290 ? 0.3564 0.5927 0.0941 -0.1024 0.0111  -0.0245 1142 PHE B C   
4665 O O   . PHE B 290 ? 0.2858 0.4971 0.0320 -0.0945 0.0183  -0.0118 1142 PHE B O   
4666 C CB  . PHE B 290 ? 0.3284 0.5351 0.1184 -0.0876 0.0031  -0.0475 1142 PHE B CB  
4667 C CG  . PHE B 290 ? 0.2894 0.4695 0.1136 -0.0841 0.0119  -0.0712 1142 PHE B CG  
4668 C CD1 . PHE B 290 ? 0.2678 0.4159 0.1150 -0.0773 0.0242  -0.0760 1142 PHE B CD1 
4669 C CD2 . PHE B 290 ? 0.3334 0.5220 0.1701 -0.0877 0.0071  -0.0854 1142 PHE B CD2 
4670 C CE1 . PHE B 290 ? 0.2964 0.4219 0.1774 -0.0736 0.0307  -0.0912 1142 PHE B CE1 
4671 C CE2 . PHE B 290 ? 0.2717 0.4349 0.1417 -0.0850 0.0160  -0.1024 1142 PHE B CE2 
4672 C CZ  . PHE B 290 ? 0.2806 0.4118 0.1729 -0.0772 0.0272  -0.1031 1142 PHE B CZ  
4673 N N   . GLN B 291 ? 0.3674 0.6448 0.0729 -0.1125 -0.0013 -0.0097 1143 GLN B N   
4674 C CA  . GLN B 291 ? 0.3978 0.6858 0.0810 -0.1110 -0.0075 0.0290  1143 GLN B CA  
4675 C C   . GLN B 291 ? 0.4284 0.7161 0.0928 -0.1237 0.0134  0.0214  1143 GLN B C   
4676 O O   . GLN B 291 ? 0.4662 0.7352 0.1334 -0.1164 0.0171  0.0473  1143 GLN B O   
4677 C CB  . GLN B 291 ? 0.4816 0.8199 0.1357 -0.1196 -0.0279 0.0516  1143 GLN B CB  
4678 C CG  . GLN B 291 ? 0.4939 0.8442 0.1307 -0.1159 -0.0374 0.1011  1143 GLN B CG  
4679 C CD  . GLN B 291 ? 0.6719 0.9749 0.3459 -0.0913 -0.0382 0.1303  1143 GLN B CD  
4680 O OE1 . GLN B 291 ? 0.6463 0.9212 0.3559 -0.0747 -0.0424 0.1249  1143 GLN B OE1 
4681 N NE2 . GLN B 291 ? 0.6922 0.9877 0.3573 -0.0911 -0.0324 0.1601  1143 GLN B NE2 
4682 N N   . ASN B 292 ? 0.4104 0.7180 0.0604 -0.1433 0.0291  -0.0165 1144 ASN B N   
4683 C CA  . ASN B 292 ? 0.4548 0.7639 0.0924 -0.1567 0.0532  -0.0314 1144 ASN B CA  
4684 C C   . ASN B 292 ? 0.4172 0.6794 0.0967 -0.1423 0.0678  -0.0383 1144 ASN B C   
4685 O O   . ASN B 292 ? 0.4290 0.6857 0.1047 -0.1462 0.0822  -0.0315 1144 ASN B O   
4686 C CB  . ASN B 292 ? 0.4864 0.8274 0.1065 -0.1814 0.0692  -0.0771 1144 ASN B CB  
4687 C CG  . ASN B 292 ? 0.5646 0.9156 0.1687 -0.1988 0.0970  -0.0954 1144 ASN B CG  
4688 O OD1 . ASN B 292 ? 0.6392 1.0093 0.2088 -0.2071 0.0982  -0.0687 1144 ASN B OD1 
4689 N ND2 . ASN B 292 ? 0.5370 0.8761 0.1697 -0.2049 0.1209  -0.1403 1144 ASN B ND2 
4690 N N   . LEU B 293 ? 0.3553 0.5876 0.0739 -0.1278 0.0640  -0.0513 1145 LEU B N   
4691 C CA  . LEU B 293 ? 0.3641 0.5557 0.1233 -0.1129 0.0717  -0.0519 1145 LEU B CA  
4692 C C   . LEU B 293 ? 0.3486 0.5213 0.1094 -0.0994 0.0612  -0.0138 1145 LEU B C   
4693 O O   . LEU B 293 ? 0.3263 0.4837 0.0986 -0.0979 0.0718  -0.0077 1145 LEU B O   
4694 C CB  . LEU B 293 ? 0.3280 0.4967 0.1238 -0.1016 0.0672  -0.0682 1145 LEU B CB  
4695 C CG  . LEU B 293 ? 0.3017 0.4741 0.1180 -0.1114 0.0836  -0.1082 1145 LEU B CG  
4696 C CD1 . LEU B 293 ? 0.3333 0.4921 0.1751 -0.1035 0.0745  -0.1168 1145 LEU B CD1 
4697 C CD2 . LEU B 293 ? 0.2878 0.4431 0.1372 -0.1100 0.1036  -0.1222 1145 LEU B CD2 
4698 N N   . ILE B 294 ? 0.3255 0.5009 0.0784 -0.0908 0.0417  0.0103  1146 ILE B N   
4699 C CA  . ILE B 294 ? 0.3698 0.5277 0.1282 -0.0786 0.0331  0.0457  1146 ILE B CA  
4700 C C   . ILE B 294 ? 0.3767 0.5457 0.1134 -0.0887 0.0429  0.0648  1146 ILE B C   
4701 O O   . ILE B 294 ? 0.3771 0.5218 0.1312 -0.0839 0.0507  0.0753  1146 ILE B O   
4702 C CB  . ILE B 294 ? 0.3480 0.5143 0.1043 -0.0690 0.0124  0.0689  1146 ILE B CB  
4703 C CG1 . ILE B 294 ? 0.3419 0.4901 0.1248 -0.0578 0.0057  0.0527  1146 ILE B CG1 
4704 C CG2 . ILE B 294 ? 0.3494 0.4997 0.1150 -0.0581 0.0071  0.1065  1146 ILE B CG2 
4705 C CD1 . ILE B 294 ? 0.3890 0.5523 0.1732 -0.0511 -0.0118 0.0662  1146 ILE B CD1 
4706 N N   . GLU B 295 ? 0.4141 0.6222 0.1125 -0.1048 0.0432  0.0684  1147 GLU B N   
4707 C CA  . GLU B 295 ? 0.4588 0.6830 0.1301 -0.1179 0.0540  0.0878  1147 GLU B CA  
4708 C C   . GLU B 295 ? 0.4659 0.6772 0.1490 -0.1258 0.0790  0.0646  1147 GLU B C   
4709 O O   . GLU B 295 ? 0.4999 0.7012 0.1847 -0.1275 0.0885  0.0850  1147 GLU B O   
4710 C CB  . GLU B 295 ? 0.4952 0.7712 0.1177 -0.1377 0.0498  0.0903  1147 GLU B CB  
4711 C CG  . GLU B 295 ? 0.5413 0.8369 0.1536 -0.1304 0.0233  0.1258  1147 GLU B CG  
4712 C CD  . GLU B 295 ? 0.6665 1.0213 0.2285 -0.1522 0.0152  0.1288  1147 GLU B CD  
4713 O OE1 . GLU B 295 ? 0.7551 1.1363 0.2803 -0.1740 0.0311  0.1212  1147 GLU B OE1 
4714 O OE2 . GLU B 295 ? 0.6752 1.0535 0.2345 -0.1488 -0.0068 0.1377  1147 GLU B OE2 
4715 N N   . GLY B 296 ? 0.4127 0.6235 0.1103 -0.1300 0.0903  0.0233  1148 GLY B N   
4716 C CA  . GLY B 296 ? 0.4308 0.6327 0.1488 -0.1364 0.1147  -0.0010 1148 GLY B CA  
4717 C C   . GLY B 296 ? 0.4012 0.5647 0.1620 -0.1207 0.1149  0.0085  1148 GLY B C   
4718 O O   . GLY B 296 ? 0.4055 0.5645 0.1755 -0.1260 0.1306  0.0118  1148 GLY B O   
4719 N N   . PHE B 297 ? 0.3781 0.5173 0.1641 -0.1034 0.0981  0.0117  1149 PHE B N   
4720 C CA  . PHE B 297 ? 0.3447 0.4513 0.1676 -0.0902 0.0950  0.0196  1149 PHE B CA  
4721 C C   . PHE B 297 ? 0.3940 0.4899 0.2113 -0.0885 0.0927  0.0529  1149 PHE B C   
4722 O O   . PHE B 297 ? 0.4004 0.4810 0.2407 -0.0888 0.1018  0.0555  1149 PHE B O   
4723 C CB  . PHE B 297 ? 0.3117 0.3998 0.1546 -0.0751 0.0778  0.0160  1149 PHE B CB  
4724 C CG  . PHE B 297 ? 0.2728 0.3638 0.1328 -0.0749 0.0807  -0.0134 1149 PHE B CG  
4725 C CD1 . PHE B 297 ? 0.3704 0.4598 0.2597 -0.0781 0.0960  -0.0344 1149 PHE B CD1 
4726 C CD2 . PHE B 297 ? 0.2700 0.3644 0.1239 -0.0708 0.0688  -0.0189 1149 PHE B CD2 
4727 C CE1 . PHE B 297 ? 0.3418 0.4310 0.2556 -0.0765 0.0996  -0.0587 1149 PHE B CE1 
4728 C CE2 . PHE B 297 ? 0.2746 0.3685 0.1492 -0.0710 0.0731  -0.0442 1149 PHE B CE2 
4729 C CZ  . PHE B 297 ? 0.3688 0.4587 0.2746 -0.0733 0.0885  -0.0631 1149 PHE B CZ  
4730 N N   . GLU B 298 ? 0.4365 0.5415 0.2284 -0.0870 0.0808  0.0788  1150 GLU B N   
4731 C CA  . GLU B 298 ? 0.4870 0.5807 0.2788 -0.0842 0.0787  0.1150  1150 GLU B CA  
4732 C C   . GLU B 298 ? 0.5112 0.6143 0.2908 -0.0992 0.0976  0.1259  1150 GLU B C   
4733 O O   . GLU B 298 ? 0.5172 0.5994 0.3156 -0.0975 0.1031  0.1460  1150 GLU B O   
4734 C CB  . GLU B 298 ? 0.5108 0.6183 0.2826 -0.0792 0.0615  0.1431  1150 GLU B CB  
4735 C CG  . GLU B 298 ? 0.4735 0.5616 0.2695 -0.0617 0.0453  0.1423  1150 GLU B CG  
4736 C CD  . GLU B 298 ? 0.5853 0.6918 0.3690 -0.0559 0.0282  0.1682  1150 GLU B CD  
4737 O OE1 . GLU B 298 ? 0.7080 0.8432 0.4630 -0.0651 0.0259  0.1925  1150 GLU B OE1 
4738 O OE2 . GLU B 298 ? 0.6788 0.7743 0.4822 -0.0428 0.0166  0.1648  1150 GLU B OE2 
4739 N N   . ALA B 299 ? 0.5184 0.6530 0.2687 -0.1154 0.1096  0.1105  1151 ALA B N   
4740 C CA  . ALA B 299 ? 0.5687 0.7163 0.3062 -0.1324 0.1316  0.1150  1151 ALA B CA  
4741 C C   . ALA B 299 ? 0.5468 0.6733 0.3264 -0.1315 0.1477  0.0936  1151 ALA B C   
4742 O O   . ALA B 299 ? 0.5584 0.6777 0.3473 -0.1383 0.1614  0.1085  1151 ALA B O   
4743 C CB  . ALA B 299 ? 0.6128 0.8026 0.3081 -0.1520 0.1428  0.0965  1151 ALA B CB  
4744 N N   . LEU B 300 ? 0.4886 0.6074 0.2962 -0.1239 0.1457  0.0609  1152 LEU B N   
4745 C CA  . LEU B 300 ? 0.4860 0.5892 0.3395 -0.1212 0.1560  0.0421  1152 LEU B CA  
4746 C C   . LEU B 300 ? 0.4666 0.5394 0.3486 -0.1109 0.1461  0.0608  1152 LEU B C   
4747 O O   . LEU B 300 ? 0.4697 0.5346 0.3814 -0.1149 0.1572  0.0581  1152 LEU B O   
4748 C CB  . LEU B 300 ? 0.4499 0.5530 0.3294 -0.1138 0.1528  0.0092  1152 LEU B CB  
4749 C CG  . LEU B 300 ? 0.4799 0.6097 0.3461 -0.1255 0.1688  -0.0192 1152 LEU B CG  
4750 C CD1 . LEU B 300 ? 0.4481 0.5725 0.3407 -0.1157 0.1616  -0.0446 1152 LEU B CD1 
4751 C CD2 . LEU B 300 ? 0.5273 0.6705 0.4106 -0.1388 0.1966  -0.0346 1152 LEU B CD2 
4752 N N   . LEU B 301 ? 0.4513 0.5094 0.3262 -0.0994 0.1270  0.0781  1153 LEU B N   
4753 C CA  . LEU B 301 ? 0.4721 0.5010 0.3733 -0.0909 0.1192  0.0924  1153 LEU B CA  
4754 C C   . LEU B 301 ? 0.5412 0.5613 0.4400 -0.0976 0.1288  0.1235  1153 LEU B C   
4755 O O   . LEU B 301 ? 0.5532 0.5473 0.4796 -0.0931 0.1269  0.1326  1153 LEU B O   
4756 C CB  . LEU B 301 ? 0.3972 0.4144 0.2957 -0.0766 0.0989  0.0967  1153 LEU B CB  
4757 C CG  . LEU B 301 ? 0.4050 0.4229 0.3140 -0.0688 0.0884  0.0703  1153 LEU B CG  
4758 C CD1 . LEU B 301 ? 0.4100 0.4275 0.3035 -0.0588 0.0722  0.0761  1153 LEU B CD1 
4759 C CD2 . LEU B 301 ? 0.3608 0.3611 0.3057 -0.0657 0.0860  0.0587  1153 LEU B CD2 
4760 N N   . LYS B 302 ? 0.5953 0.6377 0.4613 -0.1095 0.1396  0.1391  1154 LYS B N   
4761 C CA  . LYS B 302 ? 0.6947 0.7347 0.5535 -0.1189 0.1513  0.1731  1154 LYS B CA  
4762 C C   . LYS B 302 ? 0.7540 0.7829 0.6057 -0.1090 0.1367  0.2103  1154 LYS B C   
4763 O O   . LYS B 302 ? 0.7968 0.8501 0.6112 -0.1126 0.1312  0.2336  1154 LYS B O   
4764 C CB  . LYS B 302 ? 0.6897 0.7089 0.5886 -0.1246 0.1666  0.1699  1154 LYS B CB  
4765 C CG  . LYS B 302 ? 0.6798 0.7133 0.5947 -0.1332 0.1806  0.1353  1154 LYS B CG  
4766 C CD  . LYS B 302 ? 0.6893 0.7078 0.6463 -0.1406 0.1949  0.1325  1154 LYS B CD  
4767 C CE  . LYS B 302 ? 0.6568 0.6499 0.6541 -0.1297 0.1805  0.1192  1154 LYS B CE  
4768 N NZ  . LYS B 302 ? 0.6582 0.6421 0.6985 -0.1395 0.1932  0.1120  1154 LYS B NZ  
# 
