data_9EDN
# 
_entry.id   9EDN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EDN         pdb_00009edn 10.2210/pdb9edn/pdb 
WWPDB D_1000289916 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-19 ? 
3 'Structure model' 1 2 2025-04-23 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDN 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              g.hansman@griffith.edu.au 
_pdbx_contact_author.name_first         Grant 
_pdbx_contact_author.name_last          Hansman 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8735-4618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Holroyd, D.L.' 1 0009-0002-2830-6020 
'Kumar, A.'     2 0000-0001-7540-6177 
'Bruning, J.B.' 3 0000-0002-6919-1824 
'Hansman, G.S.' 4 0000-0001-8735-4618 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Virol. 
_citation.journal_id_ASTM           JOVIAM 
_citation.journal_id_CSD            0825 
_citation.journal_id_ISSN           1098-5514 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            99 
_citation.language                  ? 
_citation.page_first                e0197124 
_citation.page_last                 e0197124 
_citation.title                     'Antigenic structural analysis of bat and human norovirus protruding (P) domains.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/jvi.01971-24 
_citation.pdbx_database_id_PubMed   40062838 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Holroyd, D.L.'    1 0009-0002-2830-6020 
primary 'Kumar, A.'        2 0000-0001-7540-6177 
primary 'Vasquez, E.'      3 ?                   
primary 'Masic, V.'        4 ?                   
primary 'von Itzstein, M.' 5 0000-0001-6302-7524 
primary 'Bruning, J.B.'    6 0000-0002-6919-1824 
primary 'Hansman, G.S.'    7 0000-0001-8735-4618 
# 
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 VP1            34424.496 2    ? ? 'protruding domain' ? 
2 non-polymer syn 1,2-ETHANEDIOL 62.068    17   ? ? ?                   ? 
3 non-polymer syn 'CHLORIDE ION' 35.453    3    ? ? ?                   ? 
4 water       nat water          18.015    1345 ? ? ?                   ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SKPFTIPILTIGEMTNSRFPVPIDMLHTSPTENIVVQPQNGRCTIDGELLGTTQLITSNICSFRGSISGHEGNDDQHLWH
FNITNPNGTPFDPTEDVPAPLGTPDFRGQLYGVISQRDREGTPSENNQKANRSHQGVISTISPKFVPKLGSVMIGTWTTD
DIKNQPSKFTPIGLNDDDNFKQWELPNYSGALTLNMGLAPSVFPTYPGEQILFFRSYLPLKGGYGSPFIDCLVPQEWVAH
FYQESAPAQTDVALIRYVNPETGRVLFEAKLHRQGFITVAKSGDSPINVPANGYFRFDSWVNQFYSLAPM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SKPFTIPILTIGEMTNSRFPVPIDMLHTSPTENIVVQPQNGRCTIDGELLGTTQLITSNICSFRGSISGHEGNDDQHLWH
FNITNPNGTPFDPTEDVPAPLGTPDFRGQLYGVISQRDREGTPSENNQKANRSHQGVISTISPKFVPKLGSVMIGTWTTD
DIKNQPSKFTPIGLNDDDNFKQWELPNYSGALTLNMGLAPSVFPTYPGEQILFFRSYLPLKGGYGSPFIDCLVPQEWVAH
FYQESAPAQTDVALIRYVNPETGRVLFEAKLHRQGFITVAKSGDSPINVPANGYFRFDSWVNQFYSLAPM
;
_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 1,2-ETHANEDIOL EDO 
3 'CHLORIDE ION' CL  
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   LYS n 
1 3   PRO n 
1 4   PHE n 
1 5   THR n 
1 6   ILE n 
1 7   PRO n 
1 8   ILE n 
1 9   LEU n 
1 10  THR n 
1 11  ILE n 
1 12  GLY n 
1 13  GLU n 
1 14  MET n 
1 15  THR n 
1 16  ASN n 
1 17  SER n 
1 18  ARG n 
1 19  PHE n 
1 20  PRO n 
1 21  VAL n 
1 22  PRO n 
1 23  ILE n 
1 24  ASP n 
1 25  MET n 
1 26  LEU n 
1 27  HIS n 
1 28  THR n 
1 29  SER n 
1 30  PRO n 
1 31  THR n 
1 32  GLU n 
1 33  ASN n 
1 34  ILE n 
1 35  VAL n 
1 36  VAL n 
1 37  GLN n 
1 38  PRO n 
1 39  GLN n 
1 40  ASN n 
1 41  GLY n 
1 42  ARG n 
1 43  CYS n 
1 44  THR n 
1 45  ILE n 
1 46  ASP n 
1 47  GLY n 
1 48  GLU n 
1 49  LEU n 
1 50  LEU n 
1 51  GLY n 
1 52  THR n 
1 53  THR n 
1 54  GLN n 
1 55  LEU n 
1 56  ILE n 
1 57  THR n 
1 58  SER n 
1 59  ASN n 
1 60  ILE n 
1 61  CYS n 
1 62  SER n 
1 63  PHE n 
1 64  ARG n 
1 65  GLY n 
1 66  SER n 
1 67  ILE n 
1 68  SER n 
1 69  GLY n 
1 70  HIS n 
1 71  GLU n 
1 72  GLY n 
1 73  ASN n 
1 74  ASP n 
1 75  ASP n 
1 76  GLN n 
1 77  HIS n 
1 78  LEU n 
1 79  TRP n 
1 80  HIS n 
1 81  PHE n 
1 82  ASN n 
1 83  ILE n 
1 84  THR n 
1 85  ASN n 
1 86  PRO n 
1 87  ASN n 
1 88  GLY n 
1 89  THR n 
1 90  PRO n 
1 91  PHE n 
1 92  ASP n 
1 93  PRO n 
1 94  THR n 
1 95  GLU n 
1 96  ASP n 
1 97  VAL n 
1 98  PRO n 
1 99  ALA n 
1 100 PRO n 
1 101 LEU n 
1 102 GLY n 
1 103 THR n 
1 104 PRO n 
1 105 ASP n 
1 106 PHE n 
1 107 ARG n 
1 108 GLY n 
1 109 GLN n 
1 110 LEU n 
1 111 TYR n 
1 112 GLY n 
1 113 VAL n 
1 114 ILE n 
1 115 SER n 
1 116 GLN n 
1 117 ARG n 
1 118 ASP n 
1 119 ARG n 
1 120 GLU n 
1 121 GLY n 
1 122 THR n 
1 123 PRO n 
1 124 SER n 
1 125 GLU n 
1 126 ASN n 
1 127 ASN n 
1 128 GLN n 
1 129 LYS n 
1 130 ALA n 
1 131 ASN n 
1 132 ARG n 
1 133 SER n 
1 134 HIS n 
1 135 GLN n 
1 136 GLY n 
1 137 VAL n 
1 138 ILE n 
1 139 SER n 
1 140 THR n 
1 141 ILE n 
1 142 SER n 
1 143 PRO n 
1 144 LYS n 
1 145 PHE n 
1 146 VAL n 
1 147 PRO n 
1 148 LYS n 
1 149 LEU n 
1 150 GLY n 
1 151 SER n 
1 152 VAL n 
1 153 MET n 
1 154 ILE n 
1 155 GLY n 
1 156 THR n 
1 157 TRP n 
1 158 THR n 
1 159 THR n 
1 160 ASP n 
1 161 ASP n 
1 162 ILE n 
1 163 LYS n 
1 164 ASN n 
1 165 GLN n 
1 166 PRO n 
1 167 SER n 
1 168 LYS n 
1 169 PHE n 
1 170 THR n 
1 171 PRO n 
1 172 ILE n 
1 173 GLY n 
1 174 LEU n 
1 175 ASN n 
1 176 ASP n 
1 177 ASP n 
1 178 ASP n 
1 179 ASN n 
1 180 PHE n 
1 181 LYS n 
1 182 GLN n 
1 183 TRP n 
1 184 GLU n 
1 185 LEU n 
1 186 PRO n 
1 187 ASN n 
1 188 TYR n 
1 189 SER n 
1 190 GLY n 
1 191 ALA n 
1 192 LEU n 
1 193 THR n 
1 194 LEU n 
1 195 ASN n 
1 196 MET n 
1 197 GLY n 
1 198 LEU n 
1 199 ALA n 
1 200 PRO n 
1 201 SER n 
1 202 VAL n 
1 203 PHE n 
1 204 PRO n 
1 205 THR n 
1 206 TYR n 
1 207 PRO n 
1 208 GLY n 
1 209 GLU n 
1 210 GLN n 
1 211 ILE n 
1 212 LEU n 
1 213 PHE n 
1 214 PHE n 
1 215 ARG n 
1 216 SER n 
1 217 TYR n 
1 218 LEU n 
1 219 PRO n 
1 220 LEU n 
1 221 LYS n 
1 222 GLY n 
1 223 GLY n 
1 224 TYR n 
1 225 GLY n 
1 226 SER n 
1 227 PRO n 
1 228 PHE n 
1 229 ILE n 
1 230 ASP n 
1 231 CYS n 
1 232 LEU n 
1 233 VAL n 
1 234 PRO n 
1 235 GLN n 
1 236 GLU n 
1 237 TRP n 
1 238 VAL n 
1 239 ALA n 
1 240 HIS n 
1 241 PHE n 
1 242 TYR n 
1 243 GLN n 
1 244 GLU n 
1 245 SER n 
1 246 ALA n 
1 247 PRO n 
1 248 ALA n 
1 249 GLN n 
1 250 THR n 
1 251 ASP n 
1 252 VAL n 
1 253 ALA n 
1 254 LEU n 
1 255 ILE n 
1 256 ARG n 
1 257 TYR n 
1 258 VAL n 
1 259 ASN n 
1 260 PRO n 
1 261 GLU n 
1 262 THR n 
1 263 GLY n 
1 264 ARG n 
1 265 VAL n 
1 266 LEU n 
1 267 PHE n 
1 268 GLU n 
1 269 ALA n 
1 270 LYS n 
1 271 LEU n 
1 272 HIS n 
1 273 ARG n 
1 274 GLN n 
1 275 GLY n 
1 276 PHE n 
1 277 ILE n 
1 278 THR n 
1 279 VAL n 
1 280 ALA n 
1 281 LYS n 
1 282 SER n 
1 283 GLY n 
1 284 ASP n 
1 285 SER n 
1 286 PRO n 
1 287 ILE n 
1 288 ASN n 
1 289 VAL n 
1 290 PRO n 
1 291 ALA n 
1 292 ASN n 
1 293 GLY n 
1 294 TYR n 
1 295 PHE n 
1 296 ARG n 
1 297 PHE n 
1 298 ASP n 
1 299 SER n 
1 300 TRP n 
1 301 VAL n 
1 302 ASN n 
1 303 GLN n 
1 304 PHE n 
1 305 TYR n 
1 306 SER n 
1 307 LEU n 
1 308 ALA n 
1 309 PRO n 
1 310 MET 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                   310 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    GII.23/Loreto1847 
_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      'Norovirus GII' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     122929 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_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 
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 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
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   SER 1   224 224 SER SER A . n 
A 1 2   LYS 2   225 225 LYS LYS A . n 
A 1 3   PRO 3   226 226 PRO PRO A . n 
A 1 4   PHE 4   227 227 PHE PHE A . n 
A 1 5   THR 5   228 228 THR THR A . n 
A 1 6   ILE 6   229 229 ILE ILE A . n 
A 1 7   PRO 7   230 230 PRO PRO A . n 
A 1 8   ILE 8   231 231 ILE ILE A . n 
A 1 9   LEU 9   232 232 LEU LEU A . n 
A 1 10  THR 10  233 233 THR THR A . n 
A 1 11  ILE 11  234 234 ILE ILE A . n 
A 1 12  GLY 12  235 235 GLY GLY A . n 
A 1 13  GLU 13  236 236 GLU GLU A . n 
A 1 14  MET 14  237 237 MET MET A . n 
A 1 15  THR 15  238 238 THR THR A . n 
A 1 16  ASN 16  239 239 ASN ASN A . n 
A 1 17  SER 17  240 240 SER SER A . n 
A 1 18  ARG 18  241 241 ARG ARG A . n 
A 1 19  PHE 19  242 242 PHE PHE A . n 
A 1 20  PRO 20  243 243 PRO PRO A . n 
A 1 21  VAL 21  244 244 VAL VAL A . n 
A 1 22  PRO 22  245 245 PRO PRO A . n 
A 1 23  ILE 23  246 246 ILE ILE A . n 
A 1 24  ASP 24  247 247 ASP ASP A . n 
A 1 25  MET 25  248 248 MET MET A . n 
A 1 26  LEU 26  249 249 LEU LEU A . n 
A 1 27  HIS 27  250 250 HIS HIS A . n 
A 1 28  THR 28  251 251 THR THR A . n 
A 1 29  SER 29  252 252 SER SER A . n 
A 1 30  PRO 30  253 253 PRO PRO A . n 
A 1 31  THR 31  254 254 THR THR A . n 
A 1 32  GLU 32  255 255 GLU GLU A . n 
A 1 33  ASN 33  256 256 ASN ASN A . n 
A 1 34  ILE 34  257 257 ILE ILE A . n 
A 1 35  VAL 35  258 258 VAL VAL A . n 
A 1 36  VAL 36  259 259 VAL VAL A . n 
A 1 37  GLN 37  260 260 GLN GLN A . n 
A 1 38  PRO 38  261 261 PRO PRO A . n 
A 1 39  GLN 39  262 262 GLN GLN A . n 
A 1 40  ASN 40  263 263 ASN ASN A . n 
A 1 41  GLY 41  264 264 GLY GLY A . n 
A 1 42  ARG 42  265 265 ARG ARG A . n 
A 1 43  CYS 43  266 266 CYS CYS A . n 
A 1 44  THR 44  267 267 THR THR A . n 
A 1 45  ILE 45  268 268 ILE ILE A . n 
A 1 46  ASP 46  269 269 ASP ASP A . n 
A 1 47  GLY 47  270 270 GLY GLY A . n 
A 1 48  GLU 48  271 271 GLU GLU A . n 
A 1 49  LEU 49  272 272 LEU LEU A . n 
A 1 50  LEU 50  273 273 LEU LEU A . n 
A 1 51  GLY 51  274 274 GLY GLY A . n 
A 1 52  THR 52  275 275 THR THR A . n 
A 1 53  THR 53  276 276 THR THR A . n 
A 1 54  GLN 54  277 277 GLN GLN A . n 
A 1 55  LEU 55  278 278 LEU LEU A . n 
A 1 56  ILE 56  279 279 ILE ILE A . n 
A 1 57  THR 57  280 280 THR THR A . n 
A 1 58  SER 58  281 281 SER SER A . n 
A 1 59  ASN 59  282 282 ASN ASN A . n 
A 1 60  ILE 60  283 283 ILE ILE A . n 
A 1 61  CYS 61  284 284 CYS CYS A . n 
A 1 62  SER 62  285 285 SER SER A . n 
A 1 63  PHE 63  286 286 PHE PHE A . n 
A 1 64  ARG 64  287 287 ARG ARG A . n 
A 1 65  GLY 65  288 288 GLY GLY A . n 
A 1 66  SER 66  289 289 SER SER A . n 
A 1 67  ILE 67  290 290 ILE ILE A . n 
A 1 68  SER 68  291 291 SER SER A . n 
A 1 69  GLY 69  292 292 GLY GLY A . n 
A 1 70  HIS 70  293 293 HIS HIS A . n 
A 1 71  GLU 71  294 294 GLU GLU A . n 
A 1 72  GLY 72  295 295 GLY GLY A . n 
A 1 73  ASN 73  296 296 ASN ASN A . n 
A 1 74  ASP 74  297 297 ASP ASP A . n 
A 1 75  ASP 75  298 298 ASP ASP A . n 
A 1 76  GLN 76  299 299 GLN GLN A . n 
A 1 77  HIS 77  300 300 HIS HIS A . n 
A 1 78  LEU 78  301 301 LEU LEU A . n 
A 1 79  TRP 79  302 302 TRP TRP A . n 
A 1 80  HIS 80  303 303 HIS HIS A . n 
A 1 81  PHE 81  304 304 PHE PHE A . n 
A 1 82  ASN 82  305 305 ASN ASN A . n 
A 1 83  ILE 83  306 306 ILE ILE A . n 
A 1 84  THR 84  307 307 THR THR A . n 
A 1 85  ASN 85  308 308 ASN ASN A . n 
A 1 86  PRO 86  309 309 PRO PRO A . n 
A 1 87  ASN 87  310 310 ASN ASN A . n 
A 1 88  GLY 88  311 311 GLY GLY A . n 
A 1 89  THR 89  312 312 THR THR A . n 
A 1 90  PRO 90  313 313 PRO PRO A . n 
A 1 91  PHE 91  314 314 PHE PHE A . n 
A 1 92  ASP 92  315 315 ASP ASP A . n 
A 1 93  PRO 93  316 316 PRO PRO A . n 
A 1 94  THR 94  317 317 THR THR A . n 
A 1 95  GLU 95  318 318 GLU GLU A . n 
A 1 96  ASP 96  319 319 ASP ASP A . n 
A 1 97  VAL 97  320 320 VAL VAL A . n 
A 1 98  PRO 98  321 321 PRO PRO A . n 
A 1 99  ALA 99  322 322 ALA ALA A . n 
A 1 100 PRO 100 323 323 PRO PRO A . n 
A 1 101 LEU 101 324 324 LEU LEU A . n 
A 1 102 GLY 102 325 325 GLY GLY A . n 
A 1 103 THR 103 326 326 THR THR A . n 
A 1 104 PRO 104 327 327 PRO PRO A . n 
A 1 105 ASP 105 328 328 ASP ASP A . n 
A 1 106 PHE 106 329 329 PHE PHE A . n 
A 1 107 ARG 107 330 330 ARG ARG A . n 
A 1 108 GLY 108 331 331 GLY GLY A . n 
A 1 109 GLN 109 332 332 GLN GLN A . n 
A 1 110 LEU 110 333 333 LEU LEU A . n 
A 1 111 TYR 111 334 334 TYR TYR A . n 
A 1 112 GLY 112 335 335 GLY GLY A . n 
A 1 113 VAL 113 336 336 VAL VAL A . n 
A 1 114 ILE 114 337 337 ILE ILE A . n 
A 1 115 SER 115 338 338 SER SER A . n 
A 1 116 GLN 116 339 339 GLN GLN A . n 
A 1 117 ARG 117 340 340 ARG ARG A . n 
A 1 118 ASP 118 341 341 ASP ASP A . n 
A 1 119 ARG 119 342 342 ARG ARG A . n 
A 1 120 GLU 120 343 343 GLU GLU A . n 
A 1 121 GLY 121 344 344 GLY GLY A . n 
A 1 122 THR 122 345 345 THR THR A . n 
A 1 123 PRO 123 346 346 PRO PRO A . n 
A 1 124 SER 124 347 347 SER SER A . n 
A 1 125 GLU 125 348 348 GLU GLU A . n 
A 1 126 ASN 126 349 349 ASN ASN A . n 
A 1 127 ASN 127 350 350 ASN ASN A . n 
A 1 128 GLN 128 351 351 GLN GLN A . n 
A 1 129 LYS 129 352 352 LYS LYS A . n 
A 1 130 ALA 130 353 353 ALA ALA A . n 
A 1 131 ASN 131 354 354 ASN ASN A . n 
A 1 132 ARG 132 355 355 ARG ARG A . n 
A 1 133 SER 133 356 356 SER SER A . n 
A 1 134 HIS 134 357 357 HIS HIS A . n 
A 1 135 GLN 135 358 358 GLN GLN A . n 
A 1 136 GLY 136 359 359 GLY GLY A . n 
A 1 137 VAL 137 360 360 VAL VAL A . n 
A 1 138 ILE 138 361 361 ILE ILE A . n 
A 1 139 SER 139 362 362 SER SER A . n 
A 1 140 THR 140 363 363 THR THR A . n 
A 1 141 ILE 141 364 364 ILE ILE A . n 
A 1 142 SER 142 365 365 SER SER A . n 
A 1 143 PRO 143 366 366 PRO PRO A . n 
A 1 144 LYS 144 367 367 LYS LYS A . n 
A 1 145 PHE 145 368 368 PHE PHE A . n 
A 1 146 VAL 146 369 369 VAL VAL A . n 
A 1 147 PRO 147 370 370 PRO PRO A . n 
A 1 148 LYS 148 371 371 LYS LYS A . n 
A 1 149 LEU 149 372 372 LEU LEU A . n 
A 1 150 GLY 150 373 373 GLY GLY A . n 
A 1 151 SER 151 374 374 SER SER A . n 
A 1 152 VAL 152 375 375 VAL VAL A . n 
A 1 153 MET 153 376 376 MET MET A . n 
A 1 154 ILE 154 377 377 ILE ILE A . n 
A 1 155 GLY 155 378 378 GLY GLY A . n 
A 1 156 THR 156 379 379 THR THR A . n 
A 1 157 TRP 157 380 380 TRP TRP A . n 
A 1 158 THR 158 381 381 THR THR A . n 
A 1 159 THR 159 382 382 THR THR A . n 
A 1 160 ASP 160 383 383 ASP ASP A . n 
A 1 161 ASP 161 384 384 ASP ASP A . n 
A 1 162 ILE 162 385 385 ILE ILE A . n 
A 1 163 LYS 163 386 386 LYS LYS A . n 
A 1 164 ASN 164 387 387 ASN ASN A . n 
A 1 165 GLN 165 388 388 GLN GLN A . n 
A 1 166 PRO 166 389 389 PRO PRO A . n 
A 1 167 SER 167 390 390 SER SER A . n 
A 1 168 LYS 168 391 391 LYS LYS A . n 
A 1 169 PHE 169 392 392 PHE PHE A . n 
A 1 170 THR 170 393 393 THR THR A . n 
A 1 171 PRO 171 394 394 PRO PRO A . n 
A 1 172 ILE 172 395 395 ILE ILE A . n 
A 1 173 GLY 173 396 396 GLY GLY A . n 
A 1 174 LEU 174 397 397 LEU LEU A . n 
A 1 175 ASN 175 398 398 ASN ASN A . n 
A 1 176 ASP 176 399 399 ASP ASP A . n 
A 1 177 ASP 177 400 400 ASP ASP A . n 
A 1 178 ASP 178 401 401 ASP ASP A . n 
A 1 179 ASN 179 402 402 ASN ASN A . n 
A 1 180 PHE 180 403 403 PHE PHE A . n 
A 1 181 LYS 181 404 404 LYS LYS A . n 
A 1 182 GLN 182 405 405 GLN GLN A . n 
A 1 183 TRP 183 406 406 TRP TRP A . n 
A 1 184 GLU 184 407 407 GLU GLU A . n 
A 1 185 LEU 185 408 408 LEU LEU A . n 
A 1 186 PRO 186 409 409 PRO PRO A . n 
A 1 187 ASN 187 410 410 ASN ASN A . n 
A 1 188 TYR 188 411 411 TYR TYR A . n 
A 1 189 SER 189 412 412 SER SER A . n 
A 1 190 GLY 190 413 413 GLY GLY A . n 
A 1 191 ALA 191 414 414 ALA ALA A . n 
A 1 192 LEU 192 415 415 LEU LEU A . n 
A 1 193 THR 193 416 416 THR THR A . n 
A 1 194 LEU 194 417 417 LEU LEU A . n 
A 1 195 ASN 195 418 418 ASN ASN A . n 
A 1 196 MET 196 419 419 MET MET A . n 
A 1 197 GLY 197 420 420 GLY GLY A . n 
A 1 198 LEU 198 421 421 LEU LEU A . n 
A 1 199 ALA 199 422 422 ALA ALA A . n 
A 1 200 PRO 200 423 423 PRO PRO A . n 
A 1 201 SER 201 424 424 SER SER A . n 
A 1 202 VAL 202 425 425 VAL VAL A . n 
A 1 203 PHE 203 426 426 PHE PHE A . n 
A 1 204 PRO 204 427 427 PRO PRO A . n 
A 1 205 THR 205 428 428 THR THR A . n 
A 1 206 TYR 206 429 429 TYR TYR A . n 
A 1 207 PRO 207 430 430 PRO PRO A . n 
A 1 208 GLY 208 431 431 GLY GLY A . n 
A 1 209 GLU 209 432 432 GLU GLU A . n 
A 1 210 GLN 210 433 433 GLN GLN A . n 
A 1 211 ILE 211 434 434 ILE ILE A . n 
A 1 212 LEU 212 435 435 LEU LEU A . n 
A 1 213 PHE 213 436 436 PHE PHE A . n 
A 1 214 PHE 214 437 437 PHE PHE A . n 
A 1 215 ARG 215 438 438 ARG ARG A . n 
A 1 216 SER 216 439 439 SER SER A . n 
A 1 217 TYR 217 440 440 TYR TYR A . n 
A 1 218 LEU 218 441 441 LEU LEU A . n 
A 1 219 PRO 219 442 442 PRO PRO A . n 
A 1 220 LEU 220 443 443 LEU LEU A . n 
A 1 221 LYS 221 444 444 LYS LYS A . n 
A 1 222 GLY 222 445 445 GLY GLY A . n 
A 1 223 GLY 223 446 446 GLY GLY A . n 
A 1 224 TYR 224 447 447 TYR TYR A . n 
A 1 225 GLY 225 448 448 GLY GLY A . n 
A 1 226 SER 226 449 449 SER SER A . n 
A 1 227 PRO 227 450 450 PRO PRO A . n 
A 1 228 PHE 228 451 451 PHE PHE A . n 
A 1 229 ILE 229 452 452 ILE ILE A . n 
A 1 230 ASP 230 453 453 ASP ASP A . n 
A 1 231 CYS 231 454 454 CYS CYS A . n 
A 1 232 LEU 232 455 455 LEU LEU A . n 
A 1 233 VAL 233 456 456 VAL VAL A . n 
A 1 234 PRO 234 457 457 PRO PRO A . n 
A 1 235 GLN 235 458 458 GLN GLN A . n 
A 1 236 GLU 236 459 459 GLU GLU A . n 
A 1 237 TRP 237 460 460 TRP TRP A . n 
A 1 238 VAL 238 461 461 VAL VAL A . n 
A 1 239 ALA 239 462 462 ALA ALA A . n 
A 1 240 HIS 240 463 463 HIS HIS A . n 
A 1 241 PHE 241 464 464 PHE PHE A . n 
A 1 242 TYR 242 465 465 TYR TYR A . n 
A 1 243 GLN 243 466 466 GLN GLN A . n 
A 1 244 GLU 244 467 467 GLU GLU A . n 
A 1 245 SER 245 468 468 SER SER A . n 
A 1 246 ALA 246 469 469 ALA ALA A . n 
A 1 247 PRO 247 470 470 PRO PRO A . n 
A 1 248 ALA 248 471 471 ALA ALA A . n 
A 1 249 GLN 249 472 472 GLN GLN A . n 
A 1 250 THR 250 473 473 THR THR A . n 
A 1 251 ASP 251 474 474 ASP ASP A . n 
A 1 252 VAL 252 475 475 VAL VAL A . n 
A 1 253 ALA 253 476 476 ALA ALA A . n 
A 1 254 LEU 254 477 477 LEU LEU A . n 
A 1 255 ILE 255 478 478 ILE ILE A . n 
A 1 256 ARG 256 479 479 ARG ARG A . n 
A 1 257 TYR 257 480 480 TYR TYR A . n 
A 1 258 VAL 258 481 481 VAL VAL A . n 
A 1 259 ASN 259 482 482 ASN ASN A . n 
A 1 260 PRO 260 483 483 PRO PRO A . n 
A 1 261 GLU 261 484 484 GLU GLU A . n 
A 1 262 THR 262 485 485 THR THR A . n 
A 1 263 GLY 263 486 486 GLY GLY A . n 
A 1 264 ARG 264 487 487 ARG ARG A . n 
A 1 265 VAL 265 488 488 VAL VAL A . n 
A 1 266 LEU 266 489 489 LEU LEU A . n 
A 1 267 PHE 267 490 490 PHE PHE A . n 
A 1 268 GLU 268 491 491 GLU GLU A . n 
A 1 269 ALA 269 492 492 ALA ALA A . n 
A 1 270 LYS 270 493 493 LYS LYS A . n 
A 1 271 LEU 271 494 494 LEU LEU A . n 
A 1 272 HIS 272 495 495 HIS HIS A . n 
A 1 273 ARG 273 496 496 ARG ARG A . n 
A 1 274 GLN 274 497 497 GLN GLN A . n 
A 1 275 GLY 275 498 498 GLY GLY A . n 
A 1 276 PHE 276 499 499 PHE PHE A . n 
A 1 277 ILE 277 500 500 ILE ILE A . n 
A 1 278 THR 278 501 501 THR THR A . n 
A 1 279 VAL 279 502 502 VAL VAL A . n 
A 1 280 ALA 280 503 503 ALA ALA A . n 
A 1 281 LYS 281 504 504 LYS LYS A . n 
A 1 282 SER 282 505 505 SER SER A . n 
A 1 283 GLY 283 506 506 GLY GLY A . n 
A 1 284 ASP 284 507 507 ASP ASP A . n 
A 1 285 SER 285 508 508 SER SER A . n 
A 1 286 PRO 286 509 509 PRO PRO A . n 
A 1 287 ILE 287 510 510 ILE ILE A . n 
A 1 288 ASN 288 511 511 ASN ASN A . n 
A 1 289 VAL 289 512 512 VAL VAL A . n 
A 1 290 PRO 290 513 513 PRO PRO A . n 
A 1 291 ALA 291 514 514 ALA ALA A . n 
A 1 292 ASN 292 515 515 ASN ASN A . n 
A 1 293 GLY 293 516 516 GLY GLY A . n 
A 1 294 TYR 294 517 517 TYR TYR A . n 
A 1 295 PHE 295 518 518 PHE PHE A . n 
A 1 296 ARG 296 519 519 ARG ARG A . n 
A 1 297 PHE 297 520 520 PHE PHE A . n 
A 1 298 ASP 298 521 521 ASP ASP A . n 
A 1 299 SER 299 522 522 SER SER A . n 
A 1 300 TRP 300 523 523 TRP TRP A . n 
A 1 301 VAL 301 524 524 VAL VAL A . n 
A 1 302 ASN 302 525 525 ASN ASN A . n 
A 1 303 GLN 303 526 526 GLN GLN A . n 
A 1 304 PHE 304 527 527 PHE PHE A . n 
A 1 305 TYR 305 528 528 TYR TYR A . n 
A 1 306 SER 306 529 529 SER SER A . n 
A 1 307 LEU 307 530 530 LEU LEU A . n 
A 1 308 ALA 308 531 531 ALA ALA A . n 
A 1 309 PRO 309 532 532 PRO PRO A . n 
A 1 310 MET 310 533 533 MET MET A . n 
B 1 1   SER 1   224 ?   ?   ?   B . n 
B 1 2   LYS 2   225 225 LYS LYS B . n 
B 1 3   PRO 3   226 226 PRO PRO B . n 
B 1 4   PHE 4   227 227 PHE PHE B . n 
B 1 5   THR 5   228 228 THR THR B . n 
B 1 6   ILE 6   229 229 ILE ILE B . n 
B 1 7   PRO 7   230 230 PRO PRO B . n 
B 1 8   ILE 8   231 231 ILE ILE B . n 
B 1 9   LEU 9   232 232 LEU LEU B . n 
B 1 10  THR 10  233 233 THR THR B . n 
B 1 11  ILE 11  234 234 ILE ILE B . n 
B 1 12  GLY 12  235 235 GLY GLY B . n 
B 1 13  GLU 13  236 236 GLU GLU B . n 
B 1 14  MET 14  237 237 MET MET B . n 
B 1 15  THR 15  238 238 THR THR B . n 
B 1 16  ASN 16  239 239 ASN ASN B . n 
B 1 17  SER 17  240 240 SER SER B . n 
B 1 18  ARG 18  241 241 ARG ARG B . n 
B 1 19  PHE 19  242 242 PHE PHE B . n 
B 1 20  PRO 20  243 243 PRO PRO B . n 
B 1 21  VAL 21  244 244 VAL VAL B . n 
B 1 22  PRO 22  245 245 PRO PRO B . n 
B 1 23  ILE 23  246 246 ILE ILE B . n 
B 1 24  ASP 24  247 247 ASP ASP B . n 
B 1 25  MET 25  248 248 MET MET B . n 
B 1 26  LEU 26  249 249 LEU LEU B . n 
B 1 27  HIS 27  250 250 HIS HIS B . n 
B 1 28  THR 28  251 251 THR THR B . n 
B 1 29  SER 29  252 252 SER SER B . n 
B 1 30  PRO 30  253 253 PRO PRO B . n 
B 1 31  THR 31  254 254 THR THR B . n 
B 1 32  GLU 32  255 255 GLU GLU B . n 
B 1 33  ASN 33  256 256 ASN ASN B . n 
B 1 34  ILE 34  257 257 ILE ILE B . n 
B 1 35  VAL 35  258 258 VAL VAL B . n 
B 1 36  VAL 36  259 259 VAL VAL B . n 
B 1 37  GLN 37  260 260 GLN GLN B . n 
B 1 38  PRO 38  261 261 PRO PRO B . n 
B 1 39  GLN 39  262 262 GLN GLN B . n 
B 1 40  ASN 40  263 263 ASN ASN B . n 
B 1 41  GLY 41  264 264 GLY GLY B . n 
B 1 42  ARG 42  265 265 ARG ARG B . n 
B 1 43  CYS 43  266 266 CYS CYS B . n 
B 1 44  THR 44  267 267 THR THR B . n 
B 1 45  ILE 45  268 268 ILE ILE B . n 
B 1 46  ASP 46  269 269 ASP ASP B . n 
B 1 47  GLY 47  270 270 GLY GLY B . n 
B 1 48  GLU 48  271 271 GLU GLU B . n 
B 1 49  LEU 49  272 272 LEU LEU B . n 
B 1 50  LEU 50  273 273 LEU LEU B . n 
B 1 51  GLY 51  274 274 GLY GLY B . n 
B 1 52  THR 52  275 275 THR THR B . n 
B 1 53  THR 53  276 276 THR THR B . n 
B 1 54  GLN 54  277 277 GLN GLN B . n 
B 1 55  LEU 55  278 278 LEU LEU B . n 
B 1 56  ILE 56  279 279 ILE ILE B . n 
B 1 57  THR 57  280 280 THR THR B . n 
B 1 58  SER 58  281 281 SER SER B . n 
B 1 59  ASN 59  282 282 ASN ASN B . n 
B 1 60  ILE 60  283 283 ILE ILE B . n 
B 1 61  CYS 61  284 284 CYS CYS B . n 
B 1 62  SER 62  285 285 SER SER B . n 
B 1 63  PHE 63  286 286 PHE PHE B . n 
B 1 64  ARG 64  287 287 ARG ARG B . n 
B 1 65  GLY 65  288 288 GLY GLY B . n 
B 1 66  SER 66  289 289 SER SER B . n 
B 1 67  ILE 67  290 290 ILE ILE B . n 
B 1 68  SER 68  291 291 SER SER B . n 
B 1 69  GLY 69  292 292 GLY GLY B . n 
B 1 70  HIS 70  293 293 HIS HIS B . n 
B 1 71  GLU 71  294 294 GLU GLU B . n 
B 1 72  GLY 72  295 295 GLY GLY B . n 
B 1 73  ASN 73  296 296 ASN ASN B . n 
B 1 74  ASP 74  297 297 ASP ASP B . n 
B 1 75  ASP 75  298 298 ASP ASP B . n 
B 1 76  GLN 76  299 299 GLN GLN B . n 
B 1 77  HIS 77  300 300 HIS HIS B . n 
B 1 78  LEU 78  301 301 LEU LEU B . n 
B 1 79  TRP 79  302 302 TRP TRP B . n 
B 1 80  HIS 80  303 303 HIS HIS B . n 
B 1 81  PHE 81  304 304 PHE PHE B . n 
B 1 82  ASN 82  305 305 ASN ASN B . n 
B 1 83  ILE 83  306 306 ILE ILE B . n 
B 1 84  THR 84  307 307 THR THR B . n 
B 1 85  ASN 85  308 308 ASN ASN B . n 
B 1 86  PRO 86  309 309 PRO PRO B . n 
B 1 87  ASN 87  310 310 ASN ASN B . n 
B 1 88  GLY 88  311 311 GLY GLY B . n 
B 1 89  THR 89  312 312 THR THR B . n 
B 1 90  PRO 90  313 313 PRO PRO B . n 
B 1 91  PHE 91  314 314 PHE PHE B . n 
B 1 92  ASP 92  315 315 ASP ASP B . n 
B 1 93  PRO 93  316 316 PRO PRO B . n 
B 1 94  THR 94  317 317 THR THR B . n 
B 1 95  GLU 95  318 318 GLU GLU B . n 
B 1 96  ASP 96  319 319 ASP ASP B . n 
B 1 97  VAL 97  320 320 VAL VAL B . n 
B 1 98  PRO 98  321 321 PRO PRO B . n 
B 1 99  ALA 99  322 322 ALA ALA B . n 
B 1 100 PRO 100 323 323 PRO PRO B . n 
B 1 101 LEU 101 324 324 LEU LEU B . n 
B 1 102 GLY 102 325 325 GLY GLY B . n 
B 1 103 THR 103 326 326 THR THR B . n 
B 1 104 PRO 104 327 327 PRO PRO B . n 
B 1 105 ASP 105 328 328 ASP ASP B . n 
B 1 106 PHE 106 329 329 PHE PHE B . n 
B 1 107 ARG 107 330 330 ARG ARG B . n 
B 1 108 GLY 108 331 331 GLY GLY B . n 
B 1 109 GLN 109 332 332 GLN GLN B . n 
B 1 110 LEU 110 333 333 LEU LEU B . n 
B 1 111 TYR 111 334 334 TYR TYR B . n 
B 1 112 GLY 112 335 335 GLY GLY B . n 
B 1 113 VAL 113 336 336 VAL VAL B . n 
B 1 114 ILE 114 337 337 ILE ILE B . n 
B 1 115 SER 115 338 338 SER SER B . n 
B 1 116 GLN 116 339 339 GLN GLN B . n 
B 1 117 ARG 117 340 340 ARG ARG B . n 
B 1 118 ASP 118 341 341 ASP ASP B . n 
B 1 119 ARG 119 342 342 ARG ARG B . n 
B 1 120 GLU 120 343 343 GLU GLU B . n 
B 1 121 GLY 121 344 344 GLY GLY B . n 
B 1 122 THR 122 345 345 THR THR B . n 
B 1 123 PRO 123 346 346 PRO PRO B . n 
B 1 124 SER 124 347 347 SER SER B . n 
B 1 125 GLU 125 348 348 GLU GLU B . n 
B 1 126 ASN 126 349 349 ASN ASN B . n 
B 1 127 ASN 127 350 350 ASN ASN B . n 
B 1 128 GLN 128 351 351 GLN GLN B . n 
B 1 129 LYS 129 352 352 LYS LYS B . n 
B 1 130 ALA 130 353 353 ALA ALA B . n 
B 1 131 ASN 131 354 354 ASN ASN B . n 
B 1 132 ARG 132 355 355 ARG ARG B . n 
B 1 133 SER 133 356 356 SER SER B . n 
B 1 134 HIS 134 357 357 HIS HIS B . n 
B 1 135 GLN 135 358 358 GLN GLN B . n 
B 1 136 GLY 136 359 359 GLY GLY B . n 
B 1 137 VAL 137 360 360 VAL VAL B . n 
B 1 138 ILE 138 361 361 ILE ILE B . n 
B 1 139 SER 139 362 362 SER SER B . n 
B 1 140 THR 140 363 363 THR THR B . n 
B 1 141 ILE 141 364 364 ILE ILE B . n 
B 1 142 SER 142 365 365 SER SER B . n 
B 1 143 PRO 143 366 366 PRO PRO B . n 
B 1 144 LYS 144 367 367 LYS LYS B . n 
B 1 145 PHE 145 368 368 PHE PHE B . n 
B 1 146 VAL 146 369 369 VAL VAL B . n 
B 1 147 PRO 147 370 370 PRO PRO B . n 
B 1 148 LYS 148 371 371 LYS LYS B . n 
B 1 149 LEU 149 372 372 LEU LEU B . n 
B 1 150 GLY 150 373 373 GLY GLY B . n 
B 1 151 SER 151 374 374 SER SER B . n 
B 1 152 VAL 152 375 375 VAL VAL B . n 
B 1 153 MET 153 376 376 MET MET B . n 
B 1 154 ILE 154 377 377 ILE ILE B . n 
B 1 155 GLY 155 378 378 GLY GLY B . n 
B 1 156 THR 156 379 379 THR THR B . n 
B 1 157 TRP 157 380 380 TRP TRP B . n 
B 1 158 THR 158 381 381 THR THR B . n 
B 1 159 THR 159 382 382 THR THR B . n 
B 1 160 ASP 160 383 383 ASP ASP B . n 
B 1 161 ASP 161 384 384 ASP ASP B . n 
B 1 162 ILE 162 385 385 ILE ILE B . n 
B 1 163 LYS 163 386 386 LYS LYS B . n 
B 1 164 ASN 164 387 387 ASN ASN B . n 
B 1 165 GLN 165 388 388 GLN GLN B . n 
B 1 166 PRO 166 389 389 PRO PRO B . n 
B 1 167 SER 167 390 390 SER SER B . n 
B 1 168 LYS 168 391 391 LYS LYS B . n 
B 1 169 PHE 169 392 392 PHE PHE B . n 
B 1 170 THR 170 393 393 THR THR B . n 
B 1 171 PRO 171 394 394 PRO PRO B . n 
B 1 172 ILE 172 395 395 ILE ILE B . n 
B 1 173 GLY 173 396 396 GLY GLY B . n 
B 1 174 LEU 174 397 397 LEU LEU B . n 
B 1 175 ASN 175 398 398 ASN ASN B . n 
B 1 176 ASP 176 399 399 ASP ASP B . n 
B 1 177 ASP 177 400 400 ASP ASP B . n 
B 1 178 ASP 178 401 401 ASP ASP B . n 
B 1 179 ASN 179 402 402 ASN ASN B . n 
B 1 180 PHE 180 403 403 PHE PHE B . n 
B 1 181 LYS 181 404 404 LYS LYS B . n 
B 1 182 GLN 182 405 405 GLN GLN B . n 
B 1 183 TRP 183 406 406 TRP TRP B . n 
B 1 184 GLU 184 407 407 GLU GLU B . n 
B 1 185 LEU 185 408 408 LEU LEU B . n 
B 1 186 PRO 186 409 409 PRO PRO B . n 
B 1 187 ASN 187 410 410 ASN ASN B . n 
B 1 188 TYR 188 411 411 TYR TYR B . n 
B 1 189 SER 189 412 412 SER SER B . n 
B 1 190 GLY 190 413 413 GLY GLY B . n 
B 1 191 ALA 191 414 414 ALA ALA B . n 
B 1 192 LEU 192 415 415 LEU LEU B . n 
B 1 193 THR 193 416 416 THR THR B . n 
B 1 194 LEU 194 417 417 LEU LEU B . n 
B 1 195 ASN 195 418 418 ASN ASN B . n 
B 1 196 MET 196 419 419 MET MET B . n 
B 1 197 GLY 197 420 420 GLY GLY B . n 
B 1 198 LEU 198 421 421 LEU LEU B . n 
B 1 199 ALA 199 422 422 ALA ALA B . n 
B 1 200 PRO 200 423 423 PRO PRO B . n 
B 1 201 SER 201 424 424 SER SER B . n 
B 1 202 VAL 202 425 425 VAL VAL B . n 
B 1 203 PHE 203 426 426 PHE PHE B . n 
B 1 204 PRO 204 427 427 PRO PRO B . n 
B 1 205 THR 205 428 428 THR THR B . n 
B 1 206 TYR 206 429 429 TYR TYR B . n 
B 1 207 PRO 207 430 430 PRO PRO B . n 
B 1 208 GLY 208 431 431 GLY GLY B . n 
B 1 209 GLU 209 432 432 GLU GLU B . n 
B 1 210 GLN 210 433 433 GLN GLN B . n 
B 1 211 ILE 211 434 434 ILE ILE B . n 
B 1 212 LEU 212 435 435 LEU LEU B . n 
B 1 213 PHE 213 436 436 PHE PHE B . n 
B 1 214 PHE 214 437 437 PHE PHE B . n 
B 1 215 ARG 215 438 438 ARG ARG B . n 
B 1 216 SER 216 439 439 SER SER B . n 
B 1 217 TYR 217 440 440 TYR TYR B . n 
B 1 218 LEU 218 441 441 LEU LEU B . n 
B 1 219 PRO 219 442 442 PRO PRO B . n 
B 1 220 LEU 220 443 443 LEU LEU B . n 
B 1 221 LYS 221 444 444 LYS LYS B . n 
B 1 222 GLY 222 445 445 GLY GLY B . n 
B 1 223 GLY 223 446 446 GLY GLY B . n 
B 1 224 TYR 224 447 447 TYR TYR B . n 
B 1 225 GLY 225 448 448 GLY GLY B . n 
B 1 226 SER 226 449 449 SER SER B . n 
B 1 227 PRO 227 450 450 PRO PRO B . n 
B 1 228 PHE 228 451 451 PHE PHE B . n 
B 1 229 ILE 229 452 452 ILE ILE B . n 
B 1 230 ASP 230 453 453 ASP ASP B . n 
B 1 231 CYS 231 454 454 CYS CYS B . n 
B 1 232 LEU 232 455 455 LEU LEU B . n 
B 1 233 VAL 233 456 456 VAL VAL B . n 
B 1 234 PRO 234 457 457 PRO PRO B . n 
B 1 235 GLN 235 458 458 GLN GLN B . n 
B 1 236 GLU 236 459 459 GLU GLU B . n 
B 1 237 TRP 237 460 460 TRP TRP B . n 
B 1 238 VAL 238 461 461 VAL VAL B . n 
B 1 239 ALA 239 462 462 ALA ALA B . n 
B 1 240 HIS 240 463 463 HIS HIS B . n 
B 1 241 PHE 241 464 464 PHE PHE B . n 
B 1 242 TYR 242 465 465 TYR TYR B . n 
B 1 243 GLN 243 466 466 GLN GLN B . n 
B 1 244 GLU 244 467 467 GLU GLU B . n 
B 1 245 SER 245 468 468 SER SER B . n 
B 1 246 ALA 246 469 469 ALA ALA B . n 
B 1 247 PRO 247 470 470 PRO PRO B . n 
B 1 248 ALA 248 471 471 ALA ALA B . n 
B 1 249 GLN 249 472 472 GLN GLN B . n 
B 1 250 THR 250 473 473 THR THR B . n 
B 1 251 ASP 251 474 474 ASP ASP B . n 
B 1 252 VAL 252 475 475 VAL VAL B . n 
B 1 253 ALA 253 476 476 ALA ALA B . n 
B 1 254 LEU 254 477 477 LEU LEU B . n 
B 1 255 ILE 255 478 478 ILE ILE B . n 
B 1 256 ARG 256 479 479 ARG ARG B . n 
B 1 257 TYR 257 480 480 TYR TYR B . n 
B 1 258 VAL 258 481 481 VAL VAL B . n 
B 1 259 ASN 259 482 482 ASN ASN B . n 
B 1 260 PRO 260 483 483 PRO PRO B . n 
B 1 261 GLU 261 484 484 GLU GLU B . n 
B 1 262 THR 262 485 485 THR THR B . n 
B 1 263 GLY 263 486 486 GLY GLY B . n 
B 1 264 ARG 264 487 487 ARG ARG B . n 
B 1 265 VAL 265 488 488 VAL VAL B . n 
B 1 266 LEU 266 489 489 LEU LEU B . n 
B 1 267 PHE 267 490 490 PHE PHE B . n 
B 1 268 GLU 268 491 491 GLU GLU B . n 
B 1 269 ALA 269 492 492 ALA ALA B . n 
B 1 270 LYS 270 493 493 LYS LYS B . n 
B 1 271 LEU 271 494 494 LEU LEU B . n 
B 1 272 HIS 272 495 495 HIS HIS B . n 
B 1 273 ARG 273 496 496 ARG ARG B . n 
B 1 274 GLN 274 497 497 GLN GLN B . n 
B 1 275 GLY 275 498 498 GLY GLY B . n 
B 1 276 PHE 276 499 499 PHE PHE B . n 
B 1 277 ILE 277 500 500 ILE ILE B . n 
B 1 278 THR 278 501 501 THR THR B . n 
B 1 279 VAL 279 502 502 VAL VAL B . n 
B 1 280 ALA 280 503 503 ALA ALA B . n 
B 1 281 LYS 281 504 504 LYS LYS B . n 
B 1 282 SER 282 505 505 SER SER B . n 
B 1 283 GLY 283 506 506 GLY GLY B . n 
B 1 284 ASP 284 507 507 ASP ASP B . n 
B 1 285 SER 285 508 508 SER SER B . n 
B 1 286 PRO 286 509 509 PRO PRO B . n 
B 1 287 ILE 287 510 510 ILE ILE B . n 
B 1 288 ASN 288 511 511 ASN ASN B . n 
B 1 289 VAL 289 512 512 VAL VAL B . n 
B 1 290 PRO 290 513 513 PRO PRO B . n 
B 1 291 ALA 291 514 514 ALA ALA B . n 
B 1 292 ASN 292 515 515 ASN ASN B . n 
B 1 293 GLY 293 516 516 GLY GLY B . n 
B 1 294 TYR 294 517 517 TYR TYR B . n 
B 1 295 PHE 295 518 518 PHE PHE B . n 
B 1 296 ARG 296 519 519 ARG ARG B . n 
B 1 297 PHE 297 520 520 PHE PHE B . n 
B 1 298 ASP 298 521 521 ASP ASP B . n 
B 1 299 SER 299 522 522 SER SER B . n 
B 1 300 TRP 300 523 523 TRP TRP B . n 
B 1 301 VAL 301 524 524 VAL VAL B . n 
B 1 302 ASN 302 525 525 ASN ASN B . n 
B 1 303 GLN 303 526 526 GLN GLN B . n 
B 1 304 PHE 304 527 527 PHE PHE B . n 
B 1 305 TYR 305 528 528 TYR TYR B . n 
B 1 306 SER 306 529 529 SER SER B . n 
B 1 307 LEU 307 530 530 LEU LEU B . n 
B 1 308 ALA 308 531 531 ALA ALA B . n 
B 1 309 PRO 309 532 532 PRO PRO B . n 
B 1 310 MET 310 533 533 MET MET B . n 
# 
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 EDO 1   601  3    EDO EDO A . 
D 2 EDO 1   602  5    EDO EDO A . 
E 2 EDO 1   603  6    EDO EDO A . 
F 2 EDO 1   604  7    EDO EDO A . 
G 2 EDO 1   605  8    EDO EDO A . 
H 2 EDO 1   606  9    EDO EDO A . 
I 2 EDO 1   607  11   EDO EDO A . 
J 2 EDO 1   608  15   EDO EDO A . 
K 2 EDO 1   609  16   EDO EDO A . 
L 2 EDO 1   610  18   EDO EDO A . 
M 3 CL  1   611  2    CL  CL  A . 
N 3 CL  1   612  3    CL  CL  A . 
O 2 EDO 1   601  1    EDO EDO B . 
P 2 EDO 1   602  2    EDO EDO B . 
Q 2 EDO 1   603  4    EDO EDO B . 
R 2 EDO 1   604  10   EDO EDO B . 
S 2 EDO 1   605  12   EDO EDO B . 
T 2 EDO 1   606  13   EDO EDO B . 
U 2 EDO 1   607  17   EDO EDO B . 
V 3 CL  1   608  1    CL  CL  B . 
W 4 HOH 1   701  1435 HOH HOH A . 
W 4 HOH 2   702  1502 HOH HOH A . 
W 4 HOH 3   703  1685 HOH HOH A . 
W 4 HOH 4   704  1639 HOH HOH A . 
W 4 HOH 5   705  1205 HOH HOH A . 
W 4 HOH 6   706  1218 HOH HOH A . 
W 4 HOH 7   707  764  HOH HOH A . 
W 4 HOH 8   708  1098 HOH HOH A . 
W 4 HOH 9   709  846  HOH HOH A . 
W 4 HOH 10  710  1421 HOH HOH A . 
W 4 HOH 11  711  1328 HOH HOH A . 
W 4 HOH 12  712  1202 HOH HOH A . 
W 4 HOH 13  713  1476 HOH HOH A . 
W 4 HOH 14  714  1273 HOH HOH A . 
W 4 HOH 15  715  1003 HOH HOH A . 
W 4 HOH 16  716  1303 HOH HOH A . 
W 4 HOH 17  717  1430 HOH HOH A . 
W 4 HOH 18  718  118  HOH HOH A . 
W 4 HOH 19  719  1477 HOH HOH A . 
W 4 HOH 20  720  599  HOH HOH A . 
W 4 HOH 21  721  408  HOH HOH A . 
W 4 HOH 22  722  1067 HOH HOH A . 
W 4 HOH 23  723  1167 HOH HOH A . 
W 4 HOH 24  724  943  HOH HOH A . 
W 4 HOH 25  725  1228 HOH HOH A . 
W 4 HOH 26  726  365  HOH HOH A . 
W 4 HOH 27  727  1716 HOH HOH A . 
W 4 HOH 28  728  1173 HOH HOH A . 
W 4 HOH 29  729  1183 HOH HOH A . 
W 4 HOH 30  730  586  HOH HOH A . 
W 4 HOH 31  731  630  HOH HOH A . 
W 4 HOH 32  732  488  HOH HOH A . 
W 4 HOH 33  733  404  HOH HOH A . 
W 4 HOH 34  734  568  HOH HOH A . 
W 4 HOH 35  735  1668 HOH HOH A . 
W 4 HOH 36  736  1316 HOH HOH A . 
W 4 HOH 37  737  385  HOH HOH A . 
W 4 HOH 38  738  1452 HOH HOH A . 
W 4 HOH 39  739  1404 HOH HOH A . 
W 4 HOH 40  740  540  HOH HOH A . 
W 4 HOH 41  741  129  HOH HOH A . 
W 4 HOH 42  742  1170 HOH HOH A . 
W 4 HOH 43  743  406  HOH HOH A . 
W 4 HOH 44  744  1467 HOH HOH A . 
W 4 HOH 45  745  1266 HOH HOH A . 
W 4 HOH 46  746  1615 HOH HOH A . 
W 4 HOH 47  747  359  HOH HOH A . 
W 4 HOH 48  748  258  HOH HOH A . 
W 4 HOH 49  749  403  HOH HOH A . 
W 4 HOH 50  750  699  HOH HOH A . 
W 4 HOH 51  751  850  HOH HOH A . 
W 4 HOH 52  752  353  HOH HOH A . 
W 4 HOH 53  753  329  HOH HOH A . 
W 4 HOH 54  754  1579 HOH HOH A . 
W 4 HOH 55  755  281  HOH HOH A . 
W 4 HOH 56  756  755  HOH HOH A . 
W 4 HOH 57  757  81   HOH HOH A . 
W 4 HOH 58  758  859  HOH HOH A . 
W 4 HOH 59  759  919  HOH HOH A . 
W 4 HOH 60  760  1121 HOH HOH A . 
W 4 HOH 61  761  398  HOH HOH A . 
W 4 HOH 62  762  562  HOH HOH A . 
W 4 HOH 63  763  751  HOH HOH A . 
W 4 HOH 64  764  153  HOH HOH A . 
W 4 HOH 65  765  816  HOH HOH A . 
W 4 HOH 66  766  1097 HOH HOH A . 
W 4 HOH 67  767  695  HOH HOH A . 
W 4 HOH 68  768  890  HOH HOH A . 
W 4 HOH 69  769  1444 HOH HOH A . 
W 4 HOH 70  770  124  HOH HOH A . 
W 4 HOH 71  771  633  HOH HOH A . 
W 4 HOH 72  772  1647 HOH HOH A . 
W 4 HOH 73  773  564  HOH HOH A . 
W 4 HOH 74  774  492  HOH HOH A . 
W 4 HOH 75  775  1656 HOH HOH A . 
W 4 HOH 76  776  270  HOH HOH A . 
W 4 HOH 77  777  334  HOH HOH A . 
W 4 HOH 78  778  145  HOH HOH A . 
W 4 HOH 79  779  1310 HOH HOH A . 
W 4 HOH 80  780  212  HOH HOH A . 
W 4 HOH 81  781  156  HOH HOH A . 
W 4 HOH 82  782  554  HOH HOH A . 
W 4 HOH 83  783  1710 HOH HOH A . 
W 4 HOH 84  784  1624 HOH HOH A . 
W 4 HOH 85  785  653  HOH HOH A . 
W 4 HOH 86  786  332  HOH HOH A . 
W 4 HOH 87  787  1614 HOH HOH A . 
W 4 HOH 88  788  101  HOH HOH A . 
W 4 HOH 89  789  1621 HOH HOH A . 
W 4 HOH 90  790  526  HOH HOH A . 
W 4 HOH 91  791  1487 HOH HOH A . 
W 4 HOH 92  792  393  HOH HOH A . 
W 4 HOH 93  793  519  HOH HOH A . 
W 4 HOH 94  794  1406 HOH HOH A . 
W 4 HOH 95  795  59   HOH HOH A . 
W 4 HOH 96  796  261  HOH HOH A . 
W 4 HOH 97  797  304  HOH HOH A . 
W 4 HOH 98  798  570  HOH HOH A . 
W 4 HOH 99  799  743  HOH HOH A . 
W 4 HOH 100 800  343  HOH HOH A . 
W 4 HOH 101 801  171  HOH HOH A . 
W 4 HOH 102 802  818  HOH HOH A . 
W 4 HOH 103 803  352  HOH HOH A . 
W 4 HOH 104 804  117  HOH HOH A . 
W 4 HOH 105 805  286  HOH HOH A . 
W 4 HOH 106 806  1554 HOH HOH A . 
W 4 HOH 107 807  138  HOH HOH A . 
W 4 HOH 108 808  93   HOH HOH A . 
W 4 HOH 109 809  831  HOH HOH A . 
W 4 HOH 110 810  468  HOH HOH A . 
W 4 HOH 111 811  131  HOH HOH A . 
W 4 HOH 112 812  1606 HOH HOH A . 
W 4 HOH 113 813  799  HOH HOH A . 
W 4 HOH 114 814  700  HOH HOH A . 
W 4 HOH 115 815  50   HOH HOH A . 
W 4 HOH 116 816  243  HOH HOH A . 
W 4 HOH 117 817  1682 HOH HOH A . 
W 4 HOH 118 818  1568 HOH HOH A . 
W 4 HOH 119 819  111  HOH HOH A . 
W 4 HOH 120 820  8    HOH HOH A . 
W 4 HOH 121 821  517  HOH HOH A . 
W 4 HOH 122 822  115  HOH HOH A . 
W 4 HOH 123 823  262  HOH HOH A . 
W 4 HOH 124 824  48   HOH HOH A . 
W 4 HOH 125 825  784  HOH HOH A . 
W 4 HOH 126 826  185  HOH HOH A . 
W 4 HOH 127 827  474  HOH HOH A . 
W 4 HOH 128 828  363  HOH HOH A . 
W 4 HOH 129 829  110  HOH HOH A . 
W 4 HOH 130 830  828  HOH HOH A . 
W 4 HOH 131 831  339  HOH HOH A . 
W 4 HOH 132 832  46   HOH HOH A . 
W 4 HOH 133 833  1687 HOH HOH A . 
W 4 HOH 134 834  747  HOH HOH A . 
W 4 HOH 135 835  1325 HOH HOH A . 
W 4 HOH 136 836  1431 HOH HOH A . 
W 4 HOH 137 837  413  HOH HOH A . 
W 4 HOH 138 838  246  HOH HOH A . 
W 4 HOH 139 839  849  HOH HOH A . 
W 4 HOH 140 840  219  HOH HOH A . 
W 4 HOH 141 841  65   HOH HOH A . 
W 4 HOH 142 842  252  HOH HOH A . 
W 4 HOH 143 843  370  HOH HOH A . 
W 4 HOH 144 844  136  HOH HOH A . 
W 4 HOH 145 845  83   HOH HOH A . 
W 4 HOH 146 846  1287 HOH HOH A . 
W 4 HOH 147 847  242  HOH HOH A . 
W 4 HOH 148 848  449  HOH HOH A . 
W 4 HOH 149 849  422  HOH HOH A . 
W 4 HOH 150 850  686  HOH HOH A . 
W 4 HOH 151 851  317  HOH HOH A . 
W 4 HOH 152 852  21   HOH HOH A . 
W 4 HOH 153 853  651  HOH HOH A . 
W 4 HOH 154 854  506  HOH HOH A . 
W 4 HOH 155 855  558  HOH HOH A . 
W 4 HOH 156 856  350  HOH HOH A . 
W 4 HOH 157 857  120  HOH HOH A . 
W 4 HOH 158 858  907  HOH HOH A . 
W 4 HOH 159 859  22   HOH HOH A . 
W 4 HOH 160 860  459  HOH HOH A . 
W 4 HOH 161 861  41   HOH HOH A . 
W 4 HOH 162 862  52   HOH HOH A . 
W 4 HOH 163 863  1711 HOH HOH A . 
W 4 HOH 164 864  199  HOH HOH A . 
W 4 HOH 165 865  446  HOH HOH A . 
W 4 HOH 166 866  222  HOH HOH A . 
W 4 HOH 167 867  183  HOH HOH A . 
W 4 HOH 168 868  4    HOH HOH A . 
W 4 HOH 169 869  372  HOH HOH A . 
W 4 HOH 170 870  27   HOH HOH A . 
W 4 HOH 171 871  177  HOH HOH A . 
W 4 HOH 172 872  296  HOH HOH A . 
W 4 HOH 173 873  534  HOH HOH A . 
W 4 HOH 174 874  931  HOH HOH A . 
W 4 HOH 175 875  639  HOH HOH A . 
W 4 HOH 176 876  508  HOH HOH A . 
W 4 HOH 177 877  74   HOH HOH A . 
W 4 HOH 178 878  1051 HOH HOH A . 
W 4 HOH 179 879  439  HOH HOH A . 
W 4 HOH 180 880  119  HOH HOH A . 
W 4 HOH 181 881  289  HOH HOH A . 
W 4 HOH 182 882  114  HOH HOH A . 
W 4 HOH 183 883  229  HOH HOH A . 
W 4 HOH 184 884  390  HOH HOH A . 
W 4 HOH 185 885  70   HOH HOH A . 
W 4 HOH 186 886  264  HOH HOH A . 
W 4 HOH 187 887  522  HOH HOH A . 
W 4 HOH 188 888  467  HOH HOH A . 
W 4 HOH 189 889  141  HOH HOH A . 
W 4 HOH 190 890  5    HOH HOH A . 
W 4 HOH 191 891  435  HOH HOH A . 
W 4 HOH 192 892  1398 HOH HOH A . 
W 4 HOH 193 893  95   HOH HOH A . 
W 4 HOH 194 894  1153 HOH HOH A . 
W 4 HOH 195 895  204  HOH HOH A . 
W 4 HOH 196 896  89   HOH HOH A . 
W 4 HOH 197 897  116  HOH HOH A . 
W 4 HOH 198 898  340  HOH HOH A . 
W 4 HOH 199 899  162  HOH HOH A . 
W 4 HOH 200 900  1690 HOH HOH A . 
W 4 HOH 201 901  706  HOH HOH A . 
W 4 HOH 202 902  752  HOH HOH A . 
W 4 HOH 203 903  791  HOH HOH A . 
W 4 HOH 204 904  1450 HOH HOH A . 
W 4 HOH 205 905  803  HOH HOH A . 
W 4 HOH 206 906  112  HOH HOH A . 
W 4 HOH 207 907  1139 HOH HOH A . 
W 4 HOH 208 908  235  HOH HOH A . 
W 4 HOH 209 909  1609 HOH HOH A . 
W 4 HOH 210 910  900  HOH HOH A . 
W 4 HOH 211 911  496  HOH HOH A . 
W 4 HOH 212 912  1300 HOH HOH A . 
W 4 HOH 213 913  1620 HOH HOH A . 
W 4 HOH 214 914  173  HOH HOH A . 
W 4 HOH 215 915  234  HOH HOH A . 
W 4 HOH 216 916  419  HOH HOH A . 
W 4 HOH 217 917  323  HOH HOH A . 
W 4 HOH 218 918  610  HOH HOH A . 
W 4 HOH 219 919  362  HOH HOH A . 
W 4 HOH 220 920  58   HOH HOH A . 
W 4 HOH 221 921  1424 HOH HOH A . 
W 4 HOH 222 922  973  HOH HOH A . 
W 4 HOH 223 923  42   HOH HOH A . 
W 4 HOH 224 924  201  HOH HOH A . 
W 4 HOH 225 925  157  HOH HOH A . 
W 4 HOH 226 926  676  HOH HOH A . 
W 4 HOH 227 927  316  HOH HOH A . 
W 4 HOH 228 928  1291 HOH HOH A . 
W 4 HOH 229 929  1312 HOH HOH A . 
W 4 HOH 230 930  1348 HOH HOH A . 
W 4 HOH 231 931  792  HOH HOH A . 
W 4 HOH 232 932  1470 HOH HOH A . 
W 4 HOH 233 933  793  HOH HOH A . 
W 4 HOH 234 934  382  HOH HOH A . 
W 4 HOH 235 935  852  HOH HOH A . 
W 4 HOH 236 936  813  HOH HOH A . 
W 4 HOH 237 937  321  HOH HOH A . 
W 4 HOH 238 938  1235 HOH HOH A . 
W 4 HOH 239 939  56   HOH HOH A . 
W 4 HOH 240 940  485  HOH HOH A . 
W 4 HOH 241 941  1434 HOH HOH A . 
W 4 HOH 242 942  63   HOH HOH A . 
W 4 HOH 243 943  727  HOH HOH A . 
W 4 HOH 244 944  581  HOH HOH A . 
W 4 HOH 245 945  948  HOH HOH A . 
W 4 HOH 246 946  265  HOH HOH A . 
W 4 HOH 247 947  457  HOH HOH A . 
W 4 HOH 248 948  655  HOH HOH A . 
W 4 HOH 249 949  1284 HOH HOH A . 
W 4 HOH 250 950  64   HOH HOH A . 
W 4 HOH 251 951  939  HOH HOH A . 
W 4 HOH 252 952  838  HOH HOH A . 
W 4 HOH 253 953  97   HOH HOH A . 
W 4 HOH 254 954  25   HOH HOH A . 
W 4 HOH 255 955  1714 HOH HOH A . 
W 4 HOH 256 956  1171 HOH HOH A . 
W 4 HOH 257 957  607  HOH HOH A . 
W 4 HOH 258 958  1449 HOH HOH A . 
W 4 HOH 259 959  169  HOH HOH A . 
W 4 HOH 260 960  445  HOH HOH A . 
W 4 HOH 261 961  1332 HOH HOH A . 
W 4 HOH 262 962  32   HOH HOH A . 
W 4 HOH 263 963  178  HOH HOH A . 
W 4 HOH 264 964  217  HOH HOH A . 
W 4 HOH 265 965  596  HOH HOH A . 
W 4 HOH 266 966  297  HOH HOH A . 
W 4 HOH 267 967  883  HOH HOH A . 
W 4 HOH 268 968  1165 HOH HOH A . 
W 4 HOH 269 969  226  HOH HOH A . 
W 4 HOH 270 970  1466 HOH HOH A . 
W 4 HOH 271 971  504  HOH HOH A . 
W 4 HOH 272 972  80   HOH HOH A . 
W 4 HOH 273 973  456  HOH HOH A . 
W 4 HOH 274 974  1199 HOH HOH A . 
W 4 HOH 275 975  121  HOH HOH A . 
W 4 HOH 276 976  1336 HOH HOH A . 
W 4 HOH 277 977  1203 HOH HOH A . 
W 4 HOH 278 978  1456 HOH HOH A . 
W 4 HOH 279 979  612  HOH HOH A . 
W 4 HOH 280 980  30   HOH HOH A . 
W 4 HOH 281 981  76   HOH HOH A . 
W 4 HOH 282 982  16   HOH HOH A . 
W 4 HOH 283 983  78   HOH HOH A . 
W 4 HOH 284 984  236  HOH HOH A . 
W 4 HOH 285 985  910  HOH HOH A . 
W 4 HOH 286 986  161  HOH HOH A . 
W 4 HOH 287 987  585  HOH HOH A . 
W 4 HOH 288 988  210  HOH HOH A . 
W 4 HOH 289 989  1700 HOH HOH A . 
W 4 HOH 290 990  469  HOH HOH A . 
W 4 HOH 291 991  163  HOH HOH A . 
W 4 HOH 292 992  694  HOH HOH A . 
W 4 HOH 293 993  993  HOH HOH A . 
W 4 HOH 294 994  1344 HOH HOH A . 
W 4 HOH 295 995  255  HOH HOH A . 
W 4 HOH 296 996  36   HOH HOH A . 
W 4 HOH 297 997  1248 HOH HOH A . 
W 4 HOH 298 998  886  HOH HOH A . 
W 4 HOH 299 999  956  HOH HOH A . 
W 4 HOH 300 1000 866  HOH HOH A . 
W 4 HOH 301 1001 1688 HOH HOH A . 
W 4 HOH 302 1002 318  HOH HOH A . 
W 4 HOH 303 1003 378  HOH HOH A . 
W 4 HOH 304 1004 381  HOH HOH A . 
W 4 HOH 305 1005 500  HOH HOH A . 
W 4 HOH 306 1006 862  HOH HOH A . 
W 4 HOH 307 1007 616  HOH HOH A . 
W 4 HOH 308 1008 175  HOH HOH A . 
W 4 HOH 309 1009 1422 HOH HOH A . 
W 4 HOH 310 1010 208  HOH HOH A . 
W 4 HOH 311 1011 1495 HOH HOH A . 
W 4 HOH 312 1012 452  HOH HOH A . 
W 4 HOH 313 1013 18   HOH HOH A . 
W 4 HOH 314 1014 575  HOH HOH A . 
W 4 HOH 315 1015 360  HOH HOH A . 
W 4 HOH 316 1016 376  HOH HOH A . 
W 4 HOH 317 1017 1174 HOH HOH A . 
W 4 HOH 318 1018 311  HOH HOH A . 
W 4 HOH 319 1019 39   HOH HOH A . 
W 4 HOH 320 1020 762  HOH HOH A . 
W 4 HOH 321 1021 198  HOH HOH A . 
W 4 HOH 322 1022 1049 HOH HOH A . 
W 4 HOH 323 1023 705  HOH HOH A . 
W 4 HOH 324 1024 165  HOH HOH A . 
W 4 HOH 325 1025 1096 HOH HOH A . 
W 4 HOH 326 1026 181  HOH HOH A . 
W 4 HOH 327 1027 941  HOH HOH A . 
W 4 HOH 328 1028 335  HOH HOH A . 
W 4 HOH 329 1029 220  HOH HOH A . 
W 4 HOH 330 1030 207  HOH HOH A . 
W 4 HOH 331 1031 497  HOH HOH A . 
W 4 HOH 332 1032 168  HOH HOH A . 
W 4 HOH 333 1033 631  HOH HOH A . 
W 4 HOH 334 1034 577  HOH HOH A . 
W 4 HOH 335 1035 736  HOH HOH A . 
W 4 HOH 336 1036 328  HOH HOH A . 
W 4 HOH 337 1037 1044 HOH HOH A . 
W 4 HOH 338 1038 1132 HOH HOH A . 
W 4 HOH 339 1039 308  HOH HOH A . 
W 4 HOH 340 1040 1463 HOH HOH A . 
W 4 HOH 341 1041 425  HOH HOH A . 
W 4 HOH 342 1042 410  HOH HOH A . 
W 4 HOH 343 1043 1707 HOH HOH A . 
W 4 HOH 344 1044 155  HOH HOH A . 
W 4 HOH 345 1045 1264 HOH HOH A . 
W 4 HOH 346 1046 463  HOH HOH A . 
W 4 HOH 347 1047 1297 HOH HOH A . 
W 4 HOH 348 1048 407  HOH HOH A . 
W 4 HOH 349 1049 251  HOH HOH A . 
W 4 HOH 350 1050 1642 HOH HOH A . 
W 4 HOH 351 1051 851  HOH HOH A . 
W 4 HOH 352 1052 230  HOH HOH A . 
W 4 HOH 353 1053 441  HOH HOH A . 
W 4 HOH 354 1054 1315 HOH HOH A . 
W 4 HOH 355 1055 1649 HOH HOH A . 
W 4 HOH 356 1056 125  HOH HOH A . 
W 4 HOH 357 1057 1130 HOH HOH A . 
W 4 HOH 358 1058 789  HOH HOH A . 
W 4 HOH 359 1059 911  HOH HOH A . 
W 4 HOH 360 1060 73   HOH HOH A . 
W 4 HOH 361 1061 164  HOH HOH A . 
W 4 HOH 362 1062 214  HOH HOH A . 
W 4 HOH 363 1063 325  HOH HOH A . 
W 4 HOH 364 1064 1627 HOH HOH A . 
W 4 HOH 365 1065 205  HOH HOH A . 
W 4 HOH 366 1066 104  HOH HOH A . 
W 4 HOH 367 1067 436  HOH HOH A . 
W 4 HOH 368 1068 23   HOH HOH A . 
W 4 HOH 369 1069 284  HOH HOH A . 
W 4 HOH 370 1070 85   HOH HOH A . 
W 4 HOH 371 1071 1017 HOH HOH A . 
W 4 HOH 372 1072 609  HOH HOH A . 
W 4 HOH 373 1073 9    HOH HOH A . 
W 4 HOH 374 1074 979  HOH HOH A . 
W 4 HOH 375 1075 54   HOH HOH A . 
W 4 HOH 376 1076 427  HOH HOH A . 
W 4 HOH 377 1077 399  HOH HOH A . 
W 4 HOH 378 1078 836  HOH HOH A . 
W 4 HOH 379 1079 1418 HOH HOH A . 
W 4 HOH 380 1080 665  HOH HOH A . 
W 4 HOH 381 1081 975  HOH HOH A . 
W 4 HOH 382 1082 628  HOH HOH A . 
W 4 HOH 383 1083 108  HOH HOH A . 
W 4 HOH 384 1084 1213 HOH HOH A . 
W 4 HOH 385 1085 1272 HOH HOH A . 
W 4 HOH 386 1086 228  HOH HOH A . 
W 4 HOH 387 1087 1417 HOH HOH A . 
W 4 HOH 388 1088 1633 HOH HOH A . 
W 4 HOH 389 1089 1339 HOH HOH A . 
W 4 HOH 390 1090 1608 HOH HOH A . 
W 4 HOH 391 1091 389  HOH HOH A . 
W 4 HOH 392 1092 717  HOH HOH A . 
W 4 HOH 393 1093 477  HOH HOH A . 
W 4 HOH 394 1094 301  HOH HOH A . 
W 4 HOH 395 1095 344  HOH HOH A . 
W 4 HOH 396 1096 732  HOH HOH A . 
W 4 HOH 397 1097 951  HOH HOH A . 
W 4 HOH 398 1098 1717 HOH HOH A . 
W 4 HOH 399 1099 827  HOH HOH A . 
W 4 HOH 400 1100 837  HOH HOH A . 
W 4 HOH 401 1101 184  HOH HOH A . 
W 4 HOH 402 1102 1555 HOH HOH A . 
W 4 HOH 403 1103 1000 HOH HOH A . 
W 4 HOH 404 1104 1283 HOH HOH A . 
W 4 HOH 405 1105 233  HOH HOH A . 
W 4 HOH 406 1106 734  HOH HOH A . 
W 4 HOH 407 1107 92   HOH HOH A . 
W 4 HOH 408 1108 1408 HOH HOH A . 
W 4 HOH 409 1109 765  HOH HOH A . 
W 4 HOH 410 1110 557  HOH HOH A . 
W 4 HOH 411 1111 1270 HOH HOH A . 
W 4 HOH 412 1112 1646 HOH HOH A . 
W 4 HOH 413 1113 718  HOH HOH A . 
W 4 HOH 414 1114 1561 HOH HOH A . 
W 4 HOH 415 1115 1324 HOH HOH A . 
W 4 HOH 416 1116 1292 HOH HOH A . 
W 4 HOH 417 1117 957  HOH HOH A . 
W 4 HOH 418 1118 580  HOH HOH A . 
W 4 HOH 419 1119 1064 HOH HOH A . 
W 4 HOH 420 1120 1445 HOH HOH A . 
W 4 HOH 421 1121 1317 HOH HOH A . 
W 4 HOH 422 1122 1240 HOH HOH A . 
W 4 HOH 423 1123 917  HOH HOH A . 
W 4 HOH 424 1124 869  HOH HOH A . 
W 4 HOH 425 1125 298  HOH HOH A . 
W 4 HOH 426 1126 511  HOH HOH A . 
W 4 HOH 427 1127 881  HOH HOH A . 
W 4 HOH 428 1128 1706 HOH HOH A . 
W 4 HOH 429 1129 894  HOH HOH A . 
W 4 HOH 430 1130 796  HOH HOH A . 
W 4 HOH 431 1131 1318 HOH HOH A . 
W 4 HOH 432 1132 940  HOH HOH A . 
W 4 HOH 433 1133 1625 HOH HOH A . 
W 4 HOH 434 1134 1486 HOH HOH A . 
W 4 HOH 435 1135 872  HOH HOH A . 
W 4 HOH 436 1136 754  HOH HOH A . 
W 4 HOH 437 1137 1629 HOH HOH A . 
W 4 HOH 438 1138 103  HOH HOH A . 
W 4 HOH 439 1139 1389 HOH HOH A . 
W 4 HOH 440 1140 745  HOH HOH A . 
W 4 HOH 441 1141 884  HOH HOH A . 
W 4 HOH 442 1142 1504 HOH HOH A . 
W 4 HOH 443 1143 1630 HOH HOH A . 
W 4 HOH 444 1144 1295 HOH HOH A . 
W 4 HOH 445 1145 667  HOH HOH A . 
W 4 HOH 446 1146 1242 HOH HOH A . 
W 4 HOH 447 1147 1446 HOH HOH A . 
W 4 HOH 448 1148 1002 HOH HOH A . 
W 4 HOH 449 1149 955  HOH HOH A . 
W 4 HOH 450 1150 986  HOH HOH A . 
W 4 HOH 451 1151 645  HOH HOH A . 
W 4 HOH 452 1152 1473 HOH HOH A . 
W 4 HOH 453 1153 895  HOH HOH A . 
W 4 HOH 454 1154 1152 HOH HOH A . 
W 4 HOH 455 1155 1211 HOH HOH A . 
W 4 HOH 456 1156 1560 HOH HOH A . 
W 4 HOH 457 1157 829  HOH HOH A . 
W 4 HOH 458 1158 1471 HOH HOH A . 
W 4 HOH 459 1159 1013 HOH HOH A . 
W 4 HOH 460 1160 996  HOH HOH A . 
W 4 HOH 461 1161 744  HOH HOH A . 
W 4 HOH 462 1162 1405 HOH HOH A . 
W 4 HOH 463 1163 240  HOH HOH A . 
W 4 HOH 464 1164 1552 HOH HOH A . 
W 4 HOH 465 1165 927  HOH HOH A . 
W 4 HOH 466 1166 929  HOH HOH A . 
W 4 HOH 467 1167 1681 HOH HOH A . 
W 4 HOH 468 1168 1447 HOH HOH A . 
W 4 HOH 469 1169 624  HOH HOH A . 
W 4 HOH 470 1170 1018 HOH HOH A . 
W 4 HOH 471 1171 1198 HOH HOH A . 
W 4 HOH 472 1172 1468 HOH HOH A . 
W 4 HOH 473 1173 746  HOH HOH A . 
W 4 HOH 474 1174 937  HOH HOH A . 
W 4 HOH 475 1175 914  HOH HOH A . 
W 4 HOH 476 1176 1419 HOH HOH A . 
W 4 HOH 477 1177 729  HOH HOH A . 
W 4 HOH 478 1178 1192 HOH HOH A . 
W 4 HOH 479 1179 1453 HOH HOH A . 
W 4 HOH 480 1180 891  HOH HOH A . 
W 4 HOH 481 1181 1154 HOH HOH A . 
W 4 HOH 482 1182 1669 HOH HOH A . 
W 4 HOH 483 1183 375  HOH HOH A . 
W 4 HOH 484 1184 1118 HOH HOH A . 
W 4 HOH 485 1185 1385 HOH HOH A . 
W 4 HOH 486 1186 505  HOH HOH A . 
W 4 HOH 487 1187 926  HOH HOH A . 
W 4 HOH 488 1188 493  HOH HOH A . 
W 4 HOH 489 1189 524  HOH HOH A . 
W 4 HOH 490 1190 1438 HOH HOH A . 
W 4 HOH 491 1191 489  HOH HOH A . 
W 4 HOH 492 1192 588  HOH HOH A . 
W 4 HOH 493 1193 1654 HOH HOH A . 
W 4 HOH 494 1194 1661 HOH HOH A . 
W 4 HOH 495 1195 740  HOH HOH A . 
W 4 HOH 496 1196 1263 HOH HOH A . 
W 4 HOH 497 1197 567  HOH HOH A . 
W 4 HOH 498 1198 1691 HOH HOH A . 
W 4 HOH 499 1199 1718 HOH HOH A . 
W 4 HOH 500 1200 1065 HOH HOH A . 
W 4 HOH 501 1201 1320 HOH HOH A . 
W 4 HOH 502 1202 1370 HOH HOH A . 
W 4 HOH 503 1203 1327 HOH HOH A . 
W 4 HOH 504 1204 863  HOH HOH A . 
W 4 HOH 505 1205 1337 HOH HOH A . 
W 4 HOH 506 1206 1415 HOH HOH A . 
W 4 HOH 507 1207 1015 HOH HOH A . 
W 4 HOH 508 1208 1193 HOH HOH A . 
W 4 HOH 509 1209 1261 HOH HOH A . 
W 4 HOH 510 1210 1191 HOH HOH A . 
W 4 HOH 511 1211 1301 HOH HOH A . 
W 4 HOH 512 1212 565  HOH HOH A . 
W 4 HOH 513 1213 1563 HOH HOH A . 
W 4 HOH 514 1214 1719 HOH HOH A . 
W 4 HOH 515 1215 520  HOH HOH A . 
W 4 HOH 516 1216 1464 HOH HOH A . 
W 4 HOH 517 1217 1558 HOH HOH A . 
W 4 HOH 518 1218 1465 HOH HOH A . 
W 4 HOH 519 1219 541  HOH HOH A . 
W 4 HOH 520 1220 1231 HOH HOH A . 
W 4 HOH 521 1221 873  HOH HOH A . 
W 4 HOH 522 1222 1258 HOH HOH A . 
W 4 HOH 523 1223 915  HOH HOH A . 
W 4 HOH 524 1224 1442 HOH HOH A . 
W 4 HOH 525 1225 659  HOH HOH A . 
W 4 HOH 526 1226 1387 HOH HOH A . 
W 4 HOH 527 1227 960  HOH HOH A . 
W 4 HOH 528 1228 1437 HOH HOH A . 
W 4 HOH 529 1229 1566 HOH HOH A . 
W 4 HOH 530 1230 1048 HOH HOH A . 
W 4 HOH 531 1231 1021 HOH HOH A . 
W 4 HOH 532 1232 977  HOH HOH A . 
W 4 HOH 533 1233 1480 HOH HOH A . 
W 4 HOH 534 1234 1611 HOH HOH A . 
W 4 HOH 535 1235 1683 HOH HOH A . 
W 4 HOH 536 1236 855  HOH HOH A . 
W 4 HOH 537 1237 1215 HOH HOH A . 
W 4 HOH 538 1238 652  HOH HOH A . 
W 4 HOH 539 1239 972  HOH HOH A . 
W 4 HOH 540 1240 802  HOH HOH A . 
W 4 HOH 541 1241 766  HOH HOH A . 
W 4 HOH 542 1242 1499 HOH HOH A . 
W 4 HOH 543 1243 1459 HOH HOH A . 
W 4 HOH 544 1244 553  HOH HOH A . 
W 4 HOH 545 1245 578  HOH HOH A . 
W 4 HOH 546 1246 654  HOH HOH A . 
W 4 HOH 547 1247 1201 HOH HOH A . 
W 4 HOH 548 1248 1479 HOH HOH A . 
W 4 HOH 549 1249 1500 HOH HOH A . 
W 4 HOH 550 1250 391  HOH HOH A . 
W 4 HOH 551 1251 1414 HOH HOH A . 
W 4 HOH 552 1252 885  HOH HOH A . 
W 4 HOH 553 1253 812  HOH HOH A . 
W 4 HOH 554 1254 1675 HOH HOH A . 
W 4 HOH 555 1255 1441 HOH HOH A . 
W 4 HOH 556 1256 1308 HOH HOH A . 
W 4 HOH 557 1257 684  HOH HOH A . 
W 4 HOH 558 1258 741  HOH HOH A . 
W 4 HOH 559 1259 1148 HOH HOH A . 
W 4 HOH 560 1260 1321 HOH HOH A . 
W 4 HOH 561 1261 418  HOH HOH A . 
W 4 HOH 562 1262 292  HOH HOH A . 
W 4 HOH 563 1263 603  HOH HOH A . 
W 4 HOH 564 1264 1286 HOH HOH A . 
W 4 HOH 565 1265 889  HOH HOH A . 
W 4 HOH 566 1266 1715 HOH HOH A . 
W 4 HOH 567 1267 901  HOH HOH A . 
W 4 HOH 568 1268 331  HOH HOH A . 
W 4 HOH 569 1269 172  HOH HOH A . 
W 4 HOH 570 1270 1628 HOH HOH A . 
W 4 HOH 571 1271 383  HOH HOH A . 
W 4 HOH 572 1272 1038 HOH HOH A . 
W 4 HOH 573 1273 753  HOH HOH A . 
W 4 HOH 574 1274 1032 HOH HOH A . 
W 4 HOH 575 1275 448  HOH HOH A . 
W 4 HOH 576 1276 491  HOH HOH A . 
W 4 HOH 577 1277 647  HOH HOH A . 
W 4 HOH 578 1278 1290 HOH HOH A . 
W 4 HOH 579 1279 154  HOH HOH A . 
W 4 HOH 580 1280 336  HOH HOH A . 
W 4 HOH 581 1281 542  HOH HOH A . 
W 4 HOH 582 1282 1131 HOH HOH A . 
W 4 HOH 583 1283 288  HOH HOH A . 
W 4 HOH 584 1284 636  HOH HOH A . 
W 4 HOH 585 1285 1492 HOH HOH A . 
W 4 HOH 586 1286 861  HOH HOH A . 
W 4 HOH 587 1287 1506 HOH HOH A . 
W 4 HOH 588 1288 897  HOH HOH A . 
W 4 HOH 589 1289 1497 HOH HOH A . 
W 4 HOH 590 1290 1271 HOH HOH A . 
W 4 HOH 591 1291 1481 HOH HOH A . 
W 4 HOH 592 1292 716  HOH HOH A . 
W 4 HOH 593 1293 1113 HOH HOH A . 
W 4 HOH 594 1294 1708 HOH HOH A . 
W 4 HOH 595 1295 1443 HOH HOH A . 
W 4 HOH 596 1296 602  HOH HOH A . 
W 4 HOH 597 1297 416  HOH HOH A . 
W 4 HOH 598 1298 1212 HOH HOH A . 
W 4 HOH 599 1299 893  HOH HOH A . 
W 4 HOH 600 1300 1436 HOH HOH A . 
W 4 HOH 601 1301 1005 HOH HOH A . 
W 4 HOH 602 1302 739  HOH HOH A . 
W 4 HOH 603 1303 529  HOH HOH A . 
W 4 HOH 604 1304 899  HOH HOH A . 
W 4 HOH 605 1305 1281 HOH HOH A . 
W 4 HOH 606 1306 587  HOH HOH A . 
W 4 HOH 607 1307 188  HOH HOH A . 
W 4 HOH 608 1308 1288 HOH HOH A . 
W 4 HOH 609 1309 708  HOH HOH A . 
W 4 HOH 610 1310 470  HOH HOH A . 
W 4 HOH 611 1311 643  HOH HOH A . 
W 4 HOH 612 1312 1482 HOH HOH A . 
W 4 HOH 613 1313 3    HOH HOH A . 
W 4 HOH 614 1314 778  HOH HOH A . 
W 4 HOH 615 1315 537  HOH HOH A . 
W 4 HOH 616 1316 981  HOH HOH A . 
W 4 HOH 617 1317 1469 HOH HOH A . 
W 4 HOH 618 1318 1289 HOH HOH A . 
W 4 HOH 619 1319 1475 HOH HOH A . 
W 4 HOH 620 1320 1472 HOH HOH A . 
W 4 HOH 621 1321 916  HOH HOH A . 
W 4 HOH 622 1322 795  HOH HOH A . 
W 4 HOH 623 1323 576  HOH HOH A . 
W 4 HOH 624 1324 379  HOH HOH A . 
W 4 HOH 625 1325 1699 HOH HOH A . 
W 4 HOH 626 1326 394  HOH HOH A . 
W 4 HOH 627 1327 704  HOH HOH A . 
W 4 HOH 628 1328 1478 HOH HOH A . 
W 4 HOH 629 1329 1412 HOH HOH A . 
W 4 HOH 630 1330 661  HOH HOH A . 
W 4 HOH 631 1331 1285 HOH HOH A . 
W 4 HOH 632 1332 1640 HOH HOH A . 
W 4 HOH 633 1333 1119 HOH HOH A . 
W 4 HOH 634 1334 1539 HOH HOH A . 
W 4 HOH 635 1335 1440 HOH HOH A . 
W 4 HOH 636 1336 1701 HOH HOH A . 
W 4 HOH 637 1337 1660 HOH HOH A . 
W 4 HOH 638 1338 1331 HOH HOH A . 
W 4 HOH 639 1339 1713 HOH HOH A . 
W 4 HOH 640 1340 824  HOH HOH A . 
W 4 HOH 641 1341 1313 HOH HOH A . 
W 4 HOH 642 1342 775  HOH HOH A . 
W 4 HOH 643 1343 1501 HOH HOH A . 
W 4 HOH 644 1344 1019 HOH HOH A . 
W 4 HOH 645 1345 263  HOH HOH A . 
W 4 HOH 646 1346 1491 HOH HOH A . 
W 4 HOH 647 1347 1265 HOH HOH A . 
W 4 HOH 648 1348 701  HOH HOH A . 
W 4 HOH 649 1349 1474 HOH HOH A . 
W 4 HOH 650 1350 692  HOH HOH A . 
W 4 HOH 651 1351 896  HOH HOH A . 
W 4 HOH 652 1352 1483 HOH HOH A . 
W 4 HOH 653 1353 748  HOH HOH A . 
W 4 HOH 654 1354 528  HOH HOH A . 
W 4 HOH 655 1355 985  HOH HOH A . 
W 4 HOH 656 1356 826  HOH HOH A . 
W 4 HOH 657 1357 1322 HOH HOH A . 
W 4 HOH 658 1358 512  HOH HOH A . 
W 4 HOH 659 1359 1508 HOH HOH A . 
W 4 HOH 660 1360 1338 HOH HOH A . 
W 4 HOH 661 1361 819  HOH HOH A . 
W 4 HOH 662 1362 1622 HOH HOH A . 
W 4 HOH 663 1363 842  HOH HOH A . 
W 4 HOH 664 1364 687  HOH HOH A . 
W 4 HOH 665 1365 1333 HOH HOH A . 
W 4 HOH 666 1366 1462 HOH HOH A . 
W 4 HOH 667 1367 785  HOH HOH A . 
W 4 HOH 668 1368 988  HOH HOH A . 
W 4 HOH 669 1369 1564 HOH HOH A . 
W 4 HOH 670 1370 1323 HOH HOH A . 
W 4 HOH 671 1371 1553 HOH HOH A . 
W 4 HOH 672 1372 1451 HOH HOH A . 
W 4 HOH 673 1373 879  HOH HOH A . 
W 4 HOH 674 1374 547  HOH HOH A . 
W 4 HOH 675 1375 605  HOH HOH A . 
W 4 HOH 676 1376 935  HOH HOH A . 
W 4 HOH 677 1377 1276 HOH HOH A . 
W 4 HOH 678 1378 938  HOH HOH A . 
W 4 HOH 679 1379 1712 HOH HOH A . 
W 4 HOH 680 1380 936  HOH HOH A . 
W 4 HOH 681 1381 1378 HOH HOH A . 
W 4 HOH 682 1382 1420 HOH HOH A . 
X 4 HOH 1   701  1657 HOH HOH B . 
X 4 HOH 2   702  1695 HOH HOH B . 
X 4 HOH 3   703  1161 HOH HOH B . 
X 4 HOH 4   704  1136 HOH HOH B . 
X 4 HOH 5   705  640  HOH HOH B . 
X 4 HOH 6   706  1293 HOH HOH B . 
X 4 HOH 7   707  1663 HOH HOH B . 
X 4 HOH 8   708  189  HOH HOH B . 
X 4 HOH 9   709  1678 HOH HOH B . 
X 4 HOH 10  710  946  HOH HOH B . 
X 4 HOH 11  711  1543 HOH HOH B . 
X 4 HOH 12  712  1432 HOH HOH B . 
X 4 HOH 13  713  1250 HOH HOH B . 
X 4 HOH 14  714  1595 HOH HOH B . 
X 4 HOH 15  715  835  HOH HOH B . 
X 4 HOH 16  716  1702 HOH HOH B . 
X 4 HOH 17  717  731  HOH HOH B . 
X 4 HOH 18  718  735  HOH HOH B . 
X 4 HOH 19  719  1546 HOH HOH B . 
X 4 HOH 20  720  620  HOH HOH B . 
X 4 HOH 21  721  1677 HOH HOH B . 
X 4 HOH 22  722  1046 HOH HOH B . 
X 4 HOH 23  723  1105 HOH HOH B . 
X 4 HOH 24  724  965  HOH HOH B . 
X 4 HOH 25  725  1025 HOH HOH B . 
X 4 HOH 26  726  361  HOH HOH B . 
X 4 HOH 27  727  1188 HOH HOH B . 
X 4 HOH 28  728  980  HOH HOH B . 
X 4 HOH 29  729  670  HOH HOH B . 
X 4 HOH 30  730  1592 HOH HOH B . 
X 4 HOH 31  731  536  HOH HOH B . 
X 4 HOH 32  732  1596 HOH HOH B . 
X 4 HOH 33  733  681  HOH HOH B . 
X 4 HOH 34  734  1532 HOH HOH B . 
X 4 HOH 35  735  227  HOH HOH B . 
X 4 HOH 36  736  582  HOH HOH B . 
X 4 HOH 37  737  1159 HOH HOH B . 
X 4 HOH 38  738  821  HOH HOH B . 
X 4 HOH 39  739  769  HOH HOH B . 
X 4 HOH 40  740  423  HOH HOH B . 
X 4 HOH 41  741  1490 HOH HOH B . 
X 4 HOH 42  742  1099 HOH HOH B . 
X 4 HOH 43  743  1376 HOH HOH B . 
X 4 HOH 44  744  483  HOH HOH B . 
X 4 HOH 45  745  1143 HOH HOH B . 
X 4 HOH 46  746  437  HOH HOH B . 
X 4 HOH 47  747  913  HOH HOH B . 
X 4 HOH 48  748  1184 HOH HOH B . 
X 4 HOH 49  749  787  HOH HOH B . 
X 4 HOH 50  750  533  HOH HOH B . 
X 4 HOH 51  751  801  HOH HOH B . 
X 4 HOH 52  752  1037 HOH HOH B . 
X 4 HOH 53  753  299  HOH HOH B . 
X 4 HOH 54  754  465  HOH HOH B . 
X 4 HOH 55  755  310  HOH HOH B . 
X 4 HOH 56  756  1616 HOH HOH B . 
X 4 HOH 57  757  306  HOH HOH B . 
X 4 HOH 58  758  396  HOH HOH B . 
X 4 HOH 59  759  1394 HOH HOH B . 
X 4 HOH 60  760  348  HOH HOH B . 
X 4 HOH 61  761  271  HOH HOH B . 
X 4 HOH 62  762  1112 HOH HOH B . 
X 4 HOH 63  763  364  HOH HOH B . 
X 4 HOH 64  764  294  HOH HOH B . 
X 4 HOH 65  765  202  HOH HOH B . 
X 4 HOH 66  766  592  HOH HOH B . 
X 4 HOH 67  767  644  HOH HOH B . 
X 4 HOH 68  768  82   HOH HOH B . 
X 4 HOH 69  769  333  HOH HOH B . 
X 4 HOH 70  770  450  HOH HOH B . 
X 4 HOH 71  771  106  HOH HOH B . 
X 4 HOH 72  772  1651 HOH HOH B . 
X 4 HOH 73  773  738  HOH HOH B . 
X 4 HOH 74  774  623  HOH HOH B . 
X 4 HOH 75  775  1604 HOH HOH B . 
X 4 HOH 76  776  1034 HOH HOH B . 
X 4 HOH 77  777  432  HOH HOH B . 
X 4 HOH 78  778  974  HOH HOH B . 
X 4 HOH 79  779  223  HOH HOH B . 
X 4 HOH 80  780  349  HOH HOH B . 
X 4 HOH 81  781  395  HOH HOH B . 
X 4 HOH 82  782  12   HOH HOH B . 
X 4 HOH 83  783  1545 HOH HOH B . 
X 4 HOH 84  784  1401 HOH HOH B . 
X 4 HOH 85  785  669  HOH HOH B . 
X 4 HOH 86  786  250  HOH HOH B . 
X 4 HOH 87  787  96   HOH HOH B . 
X 4 HOH 88  788  86   HOH HOH B . 
X 4 HOH 89  789  60   HOH HOH B . 
X 4 HOH 90  790  79   HOH HOH B . 
X 4 HOH 91  791  502  HOH HOH B . 
X 4 HOH 92  792  109  HOH HOH B . 
X 4 HOH 93  793  187  HOH HOH B . 
X 4 HOH 94  794  291  HOH HOH B . 
X 4 HOH 95  795  300  HOH HOH B . 
X 4 HOH 96  796  244  HOH HOH B . 
X 4 HOH 97  797  810  HOH HOH B . 
X 4 HOH 98  798  11   HOH HOH B . 
X 4 HOH 99  799  290  HOH HOH B . 
X 4 HOH 100 800  211  HOH HOH B . 
X 4 HOH 101 801  668  HOH HOH B . 
X 4 HOH 102 802  195  HOH HOH B . 
X 4 HOH 103 803  1094 HOH HOH B . 
X 4 HOH 104 804  556  HOH HOH B . 
X 4 HOH 105 805  276  HOH HOH B . 
X 4 HOH 106 806  591  HOH HOH B . 
X 4 HOH 107 807  976  HOH HOH B . 
X 4 HOH 108 808  590  HOH HOH B . 
X 4 HOH 109 809  147  HOH HOH B . 
X 4 HOH 110 810  358  HOH HOH B . 
X 4 HOH 111 811  397  HOH HOH B . 
X 4 HOH 112 812  327  HOH HOH B . 
X 4 HOH 113 813  357  HOH HOH B . 
X 4 HOH 114 814  15   HOH HOH B . 
X 4 HOH 115 815  122  HOH HOH B . 
X 4 HOH 116 816  137  HOH HOH B . 
X 4 HOH 117 817  215  HOH HOH B . 
X 4 HOH 118 818  295  HOH HOH B . 
X 4 HOH 119 819  1582 HOH HOH B . 
X 4 HOH 120 820  1129 HOH HOH B . 
X 4 HOH 121 821  1722 HOH HOH B . 
X 4 HOH 122 822  572  HOH HOH B . 
X 4 HOH 123 823  180  HOH HOH B . 
X 4 HOH 124 824  942  HOH HOH B . 
X 4 HOH 125 825  100  HOH HOH B . 
X 4 HOH 126 826  355  HOH HOH B . 
X 4 HOH 127 827  726  HOH HOH B . 
X 4 HOH 128 828  40   HOH HOH B . 
X 4 HOH 129 829  471  HOH HOH B . 
X 4 HOH 130 830  90   HOH HOH B . 
X 4 HOH 131 831  525  HOH HOH B . 
X 4 HOH 132 832  411  HOH HOH B . 
X 4 HOH 133 833  77   HOH HOH B . 
X 4 HOH 134 834  737  HOH HOH B . 
X 4 HOH 135 835  480  HOH HOH B . 
X 4 HOH 136 836  1126 HOH HOH B . 
X 4 HOH 137 837  1509 HOH HOH B . 
X 4 HOH 138 838  494  HOH HOH B . 
X 4 HOH 139 839  315  HOH HOH B . 
X 4 HOH 140 840  132  HOH HOH B . 
X 4 HOH 141 841  1062 HOH HOH B . 
X 4 HOH 142 842  1047 HOH HOH B . 
X 4 HOH 143 843  473  HOH HOH B . 
X 4 HOH 144 844  374  HOH HOH B . 
X 4 HOH 145 845  903  HOH HOH B . 
X 4 HOH 146 846  140  HOH HOH B . 
X 4 HOH 147 847  130  HOH HOH B . 
X 4 HOH 148 848  320  HOH HOH B . 
X 4 HOH 149 849  876  HOH HOH B . 
X 4 HOH 150 850  26   HOH HOH B . 
X 4 HOH 151 851  1053 HOH HOH B . 
X 4 HOH 152 852  1535 HOH HOH B . 
X 4 HOH 153 853  139  HOH HOH B . 
X 4 HOH 154 854  1100 HOH HOH B . 
X 4 HOH 155 855  402  HOH HOH B . 
X 4 HOH 156 856  7    HOH HOH B . 
X 4 HOH 157 857  712  HOH HOH B . 
X 4 HOH 158 858  330  HOH HOH B . 
X 4 HOH 159 859  10   HOH HOH B . 
X 4 HOH 160 860  532  HOH HOH B . 
X 4 HOH 161 861  495  HOH HOH B . 
X 4 HOH 162 862  371  HOH HOH B . 
X 4 HOH 163 863  6    HOH HOH B . 
X 4 HOH 164 864  107  HOH HOH B . 
X 4 HOH 165 865  68   HOH HOH B . 
X 4 HOH 166 866  31   HOH HOH B . 
X 4 HOH 167 867  99   HOH HOH B . 
X 4 HOH 168 868  206  HOH HOH B . 
X 4 HOH 169 869  1542 HOH HOH B . 
X 4 HOH 170 870  75   HOH HOH B . 
X 4 HOH 171 871  248  HOH HOH B . 
X 4 HOH 172 872  1612 HOH HOH B . 
X 4 HOH 173 873  170  HOH HOH B . 
X 4 HOH 174 874  14   HOH HOH B . 
X 4 HOH 175 875  932  HOH HOH B . 
X 4 HOH 176 876  1115 HOH HOH B . 
X 4 HOH 177 877  843  HOH HOH B . 
X 4 HOH 178 878  69   HOH HOH B . 
X 4 HOH 179 879  703  HOH HOH B . 
X 4 HOH 180 880  19   HOH HOH B . 
X 4 HOH 181 881  254  HOH HOH B . 
X 4 HOH 182 882  742  HOH HOH B . 
X 4 HOH 183 883  135  HOH HOH B . 
X 4 HOH 184 884  324  HOH HOH B . 
X 4 HOH 185 885  1353 HOH HOH B . 
X 4 HOH 186 886  1022 HOH HOH B . 
X 4 HOH 187 887  186  HOH HOH B . 
X 4 HOH 188 888  37   HOH HOH B . 
X 4 HOH 189 889  128  HOH HOH B . 
X 4 HOH 190 890  1514 HOH HOH B . 
X 4 HOH 191 891  113  HOH HOH B . 
X 4 HOH 192 892  193  HOH HOH B . 
X 4 HOH 193 893  151  HOH HOH B . 
X 4 HOH 194 894  571  HOH HOH B . 
X 4 HOH 195 895  1721 HOH HOH B . 
X 4 HOH 196 896  346  HOH HOH B . 
X 4 HOH 197 897  924  HOH HOH B . 
X 4 HOH 198 898  617  HOH HOH B . 
X 4 HOH 199 899  815  HOH HOH B . 
X 4 HOH 200 900  697  HOH HOH B . 
X 4 HOH 201 901  377  HOH HOH B . 
X 4 HOH 202 902  91   HOH HOH B . 
X 4 HOH 203 903  635  HOH HOH B . 
X 4 HOH 204 904  33   HOH HOH B . 
X 4 HOH 205 905  1117 HOH HOH B . 
X 4 HOH 206 906  458  HOH HOH B . 
X 4 HOH 207 907  637  HOH HOH B . 
X 4 HOH 208 908  149  HOH HOH B . 
X 4 HOH 209 909  279  HOH HOH B . 
X 4 HOH 210 910  548  HOH HOH B . 
X 4 HOH 211 911  725  HOH HOH B . 
X 4 HOH 212 912  356  HOH HOH B . 
X 4 HOH 213 913  102  HOH HOH B . 
X 4 HOH 214 914  345  HOH HOH B . 
X 4 HOH 215 915  1307 HOH HOH B . 
X 4 HOH 216 916  613  HOH HOH B . 
X 4 HOH 217 917  216  HOH HOH B . 
X 4 HOH 218 918  1511 HOH HOH B . 
X 4 HOH 219 919  1548 HOH HOH B . 
X 4 HOH 220 920  1593 HOH HOH B . 
X 4 HOH 221 921  510  HOH HOH B . 
X 4 HOH 222 922  62   HOH HOH B . 
X 4 HOH 223 923  94   HOH HOH B . 
X 4 HOH 224 924  811  HOH HOH B . 
X 4 HOH 225 925  1144 HOH HOH B . 
X 4 HOH 226 926  1014 HOH HOH B . 
X 4 HOH 227 927  239  HOH HOH B . 
X 4 HOH 228 928  283  HOH HOH B . 
X 4 HOH 229 929  1720 HOH HOH B . 
X 4 HOH 230 930  1626 HOH HOH B . 
X 4 HOH 231 931  150  HOH HOH B . 
X 4 HOH 232 932  434  HOH HOH B . 
X 4 HOH 233 933  1454 HOH HOH B . 
X 4 HOH 234 934  247  HOH HOH B . 
X 4 HOH 235 935  152  HOH HOH B . 
X 4 HOH 236 936  1234 HOH HOH B . 
X 4 HOH 237 937  1111 HOH HOH B . 
X 4 HOH 238 938  43   HOH HOH B . 
X 4 HOH 239 939  584  HOH HOH B . 
X 4 HOH 240 940  277  HOH HOH B . 
X 4 HOH 241 941  47   HOH HOH B . 
X 4 HOH 242 942  454  HOH HOH B . 
X 4 HOH 243 943  313  HOH HOH B . 
X 4 HOH 244 944  484  HOH HOH B . 
X 4 HOH 245 945  45   HOH HOH B . 
X 4 HOH 246 946  1352 HOH HOH B . 
X 4 HOH 247 947  928  HOH HOH B . 
X 4 HOH 248 948  28   HOH HOH B . 
X 4 HOH 249 949  354  HOH HOH B . 
X 4 HOH 250 950  721  HOH HOH B . 
X 4 HOH 251 951  1520 HOH HOH B . 
X 4 HOH 252 952  1634 HOH HOH B . 
X 4 HOH 253 953  253  HOH HOH B . 
X 4 HOH 254 954  388  HOH HOH B . 
X 4 HOH 255 955  535  HOH HOH B . 
X 4 HOH 256 956  774  HOH HOH B . 
X 4 HOH 257 957  1101 HOH HOH B . 
X 4 HOH 258 958  34   HOH HOH B . 
X 4 HOH 259 959  24   HOH HOH B . 
X 4 HOH 260 960  1342 HOH HOH B . 
X 4 HOH 261 961  351  HOH HOH B . 
X 4 HOH 262 962  1079 HOH HOH B . 
X 4 HOH 263 963  530  HOH HOH B . 
X 4 HOH 264 964  282  HOH HOH B . 
X 4 HOH 265 965  98   HOH HOH B . 
X 4 HOH 266 966  179  HOH HOH B . 
X 4 HOH 267 967  84   HOH HOH B . 
X 4 HOH 268 968  72   HOH HOH B . 
X 4 HOH 269 969  167  HOH HOH B . 
X 4 HOH 270 970  126  HOH HOH B . 
X 4 HOH 271 971  49   HOH HOH B . 
X 4 HOH 272 972  825  HOH HOH B . 
X 4 HOH 273 973  763  HOH HOH B . 
X 4 HOH 274 974  146  HOH HOH B . 
X 4 HOH 275 975  615  HOH HOH B . 
X 4 HOH 276 976  1383 HOH HOH B . 
X 4 HOH 277 977  158  HOH HOH B . 
X 4 HOH 278 978  272  HOH HOH B . 
X 4 HOH 279 979  1637 HOH HOH B . 
X 4 HOH 280 980  57   HOH HOH B . 
X 4 HOH 281 981  1698 HOH HOH B . 
X 4 HOH 282 982  1186 HOH HOH B . 
X 4 HOH 283 983  20   HOH HOH B . 
X 4 HOH 284 984  1572 HOH HOH B . 
X 4 HOH 285 985  67   HOH HOH B . 
X 4 HOH 286 986  794  HOH HOH B . 
X 4 HOH 287 987  273  HOH HOH B . 
X 4 HOH 288 988  1305 HOH HOH B . 
X 4 HOH 289 989  1073 HOH HOH B . 
X 4 HOH 290 990  1355 HOH HOH B . 
X 4 HOH 291 991  44   HOH HOH B . 
X 4 HOH 292 992  194  HOH HOH B . 
X 4 HOH 293 993  144  HOH HOH B . 
X 4 HOH 294 994  691  HOH HOH B . 
X 4 HOH 295 995  1330 HOH HOH B . 
X 4 HOH 296 996  444  HOH HOH B . 
X 4 HOH 297 997  302  HOH HOH B . 
X 4 HOH 298 998  249  HOH HOH B . 
X 4 HOH 299 999  55   HOH HOH B . 
X 4 HOH 300 1000 865  HOH HOH B . 
X 4 HOH 301 1001 689  HOH HOH B . 
X 4 HOH 302 1002 309  HOH HOH B . 
X 4 HOH 303 1003 182  HOH HOH B . 
X 4 HOH 304 1004 1269 HOH HOH B . 
X 4 HOH 305 1005 341  HOH HOH B . 
X 4 HOH 306 1006 545  HOH HOH B . 
X 4 HOH 307 1007 420  HOH HOH B . 
X 4 HOH 308 1008 552  HOH HOH B . 
X 4 HOH 309 1009 133  HOH HOH B . 
X 4 HOH 310 1010 1599 HOH HOH B . 
X 4 HOH 311 1011 268  HOH HOH B . 
X 4 HOH 312 1012 476  HOH HOH B . 
X 4 HOH 313 1013 990  HOH HOH B . 
X 4 HOH 314 1014 702  HOH HOH B . 
X 4 HOH 315 1015 29   HOH HOH B . 
X 4 HOH 316 1016 35   HOH HOH B . 
X 4 HOH 317 1017 690  HOH HOH B . 
X 4 HOH 318 1018 1057 HOH HOH B . 
X 4 HOH 319 1019 1114 HOH HOH B . 
X 4 HOH 320 1020 1106 HOH HOH B . 
X 4 HOH 321 1021 1081 HOH HOH B . 
X 4 HOH 322 1022 275  HOH HOH B . 
X 4 HOH 323 1023 237  HOH HOH B . 
X 4 HOH 324 1024 1010 HOH HOH B . 
X 4 HOH 325 1025 460  HOH HOH B . 
X 4 HOH 326 1026 190  HOH HOH B . 
X 4 HOH 327 1027 782  HOH HOH B . 
X 4 HOH 328 1028 730  HOH HOH B . 
X 4 HOH 329 1029 159  HOH HOH B . 
X 4 HOH 330 1030 1388 HOH HOH B . 
X 4 HOH 331 1031 53   HOH HOH B . 
X 4 HOH 332 1032 123  HOH HOH B . 
X 4 HOH 333 1033 1278 HOH HOH B . 
X 4 HOH 334 1034 166  HOH HOH B . 
X 4 HOH 335 1035 629  HOH HOH B . 
X 4 HOH 336 1036 598  HOH HOH B . 
X 4 HOH 337 1037 999  HOH HOH B . 
X 4 HOH 338 1038 1407 HOH HOH B . 
X 4 HOH 339 1039 142  HOH HOH B . 
X 4 HOH 340 1040 1085 HOH HOH B . 
X 4 HOH 341 1041 1522 HOH HOH B . 
X 4 HOH 342 1042 1343 HOH HOH B . 
X 4 HOH 343 1043 1157 HOH HOH B . 
X 4 HOH 344 1044 809  HOH HOH B . 
X 4 HOH 345 1045 788  HOH HOH B . 
X 4 HOH 346 1046 1054 HOH HOH B . 
X 4 HOH 347 1047 671  HOH HOH B . 
X 4 HOH 348 1048 971  HOH HOH B . 
X 4 HOH 349 1049 546  HOH HOH B . 
X 4 HOH 350 1050 191  HOH HOH B . 
X 4 HOH 351 1051 232  HOH HOH B . 
X 4 HOH 352 1052 806  HOH HOH B . 
X 4 HOH 353 1053 51   HOH HOH B . 
X 4 HOH 354 1054 421  HOH HOH B . 
X 4 HOH 355 1055 442  HOH HOH B . 
X 4 HOH 356 1056 71   HOH HOH B . 
X 4 HOH 357 1057 771  HOH HOH B . 
X 4 HOH 358 1058 231  HOH HOH B . 
X 4 HOH 359 1059 368  HOH HOH B . 
X 4 HOH 360 1060 963  HOH HOH B . 
X 4 HOH 361 1061 1306 HOH HOH B . 
X 4 HOH 362 1062 174  HOH HOH B . 
X 4 HOH 363 1063 1384 HOH HOH B . 
X 4 HOH 364 1064 1536 HOH HOH B . 
X 4 HOH 365 1065 722  HOH HOH B . 
X 4 HOH 366 1066 61   HOH HOH B . 
X 4 HOH 367 1067 521  HOH HOH B . 
X 4 HOH 368 1068 417  HOH HOH B . 
X 4 HOH 369 1069 305  HOH HOH B . 
X 4 HOH 370 1070 1521 HOH HOH B . 
X 4 HOH 371 1071 969  HOH HOH B . 
X 4 HOH 372 1072 259  HOH HOH B . 
X 4 HOH 373 1073 1039 HOH HOH B . 
X 4 HOH 374 1074 1359 HOH HOH B . 
X 4 HOH 375 1075 443  HOH HOH B . 
X 4 HOH 376 1076 13   HOH HOH B . 
X 4 HOH 377 1077 1294 HOH HOH B . 
X 4 HOH 378 1078 322  HOH HOH B . 
X 4 HOH 379 1079 1023 HOH HOH B . 
X 4 HOH 380 1080 531  HOH HOH B . 
X 4 HOH 381 1081 832  HOH HOH B . 
X 4 HOH 382 1082 1666 HOH HOH B . 
X 4 HOH 383 1083 196  HOH HOH B . 
X 4 HOH 384 1084 160  HOH HOH B . 
X 4 HOH 385 1085 17   HOH HOH B . 
X 4 HOH 386 1086 714  HOH HOH B . 
X 4 HOH 387 1087 516  HOH HOH B . 
X 4 HOH 388 1088 1090 HOH HOH B . 
X 4 HOH 389 1089 1350 HOH HOH B . 
X 4 HOH 390 1090 1093 HOH HOH B . 
X 4 HOH 391 1091 649  HOH HOH B . 
X 4 HOH 392 1092 218  HOH HOH B . 
X 4 HOH 393 1093 844  HOH HOH B . 
X 4 HOH 394 1094 880  HOH HOH B . 
X 4 HOH 395 1095 1696 HOH HOH B . 
X 4 HOH 396 1096 367  HOH HOH B . 
X 4 HOH 397 1097 921  HOH HOH B . 
X 4 HOH 398 1098 1358 HOH HOH B . 
X 4 HOH 399 1099 920  HOH HOH B . 
X 4 HOH 400 1100 287  HOH HOH B . 
X 4 HOH 401 1101 197  HOH HOH B . 
X 4 HOH 402 1102 1137 HOH HOH B . 
X 4 HOH 403 1103 1670 HOH HOH B . 
X 4 HOH 404 1104 1362 HOH HOH B . 
X 4 HOH 405 1105 830  HOH HOH B . 
X 4 HOH 406 1106 1533 HOH HOH B . 
X 4 HOH 407 1107 481  HOH HOH B . 
X 4 HOH 408 1108 430  HOH HOH B . 
X 4 HOH 409 1109 1361 HOH HOH B . 
X 4 HOH 410 1110 428  HOH HOH B . 
X 4 HOH 411 1111 1724 HOH HOH B . 
X 4 HOH 412 1112 841  HOH HOH B . 
X 4 HOH 413 1113 1411 HOH HOH B . 
X 4 HOH 414 1114 1703 HOH HOH B . 
X 4 HOH 415 1115 563  HOH HOH B . 
X 4 HOH 416 1116 1507 HOH HOH B . 
X 4 HOH 417 1117 683  HOH HOH B . 
X 4 HOH 418 1118 280  HOH HOH B . 
X 4 HOH 419 1119 1537 HOH HOH B . 
X 4 HOH 420 1120 909  HOH HOH B . 
X 4 HOH 421 1121 1390 HOH HOH B . 
X 4 HOH 422 1122 499  HOH HOH B . 
X 4 HOH 423 1123 498  HOH HOH B . 
X 4 HOH 424 1124 1179 HOH HOH B . 
X 4 HOH 425 1125 875  HOH HOH B . 
X 4 HOH 426 1126 1345 HOH HOH B . 
X 4 HOH 427 1127 887  HOH HOH B . 
X 4 HOH 428 1128 461  HOH HOH B . 
X 4 HOH 429 1129 1366 HOH HOH B . 
X 4 HOH 430 1130 1260 HOH HOH B . 
X 4 HOH 431 1131 1531 HOH HOH B . 
X 4 HOH 432 1132 1056 HOH HOH B . 
X 4 HOH 433 1133 1341 HOH HOH B . 
X 4 HOH 434 1134 858  HOH HOH B . 
X 4 HOH 435 1135 798  HOH HOH B . 
X 4 HOH 436 1136 773  HOH HOH B . 
X 4 HOH 437 1137 1528 HOH HOH B . 
X 4 HOH 438 1138 768  HOH HOH B . 
X 4 HOH 439 1139 260  HOH HOH B . 
X 4 HOH 440 1140 641  HOH HOH B . 
X 4 HOH 441 1141 1588 HOH HOH B . 
X 4 HOH 442 1142 1189 HOH HOH B . 
X 4 HOH 443 1143 1141 HOH HOH B . 
X 4 HOH 444 1144 906  HOH HOH B . 
X 4 HOH 445 1145 987  HOH HOH B . 
X 4 HOH 446 1146 1524 HOH HOH B . 
X 4 HOH 447 1147 650  HOH HOH B . 
X 4 HOH 448 1148 1249 HOH HOH B . 
X 4 HOH 449 1149 1544 HOH HOH B . 
X 4 HOH 450 1150 1151 HOH HOH B . 
X 4 HOH 451 1151 713  HOH HOH B . 
X 4 HOH 452 1152 660  HOH HOH B . 
X 4 HOH 453 1153 1526 HOH HOH B . 
X 4 HOH 454 1154 1351 HOH HOH B . 
X 4 HOH 455 1155 776  HOH HOH B . 
X 4 HOH 456 1156 1256 HOH HOH B . 
X 4 HOH 457 1157 559  HOH HOH B . 
X 4 HOH 458 1158 224  HOH HOH B . 
X 4 HOH 459 1159 614  HOH HOH B . 
X 4 HOH 460 1160 1346 HOH HOH B . 
X 4 HOH 461 1161 878  HOH HOH B . 
X 4 HOH 462 1162 127  HOH HOH B . 
X 4 HOH 463 1163 447  HOH HOH B . 
X 4 HOH 464 1164 1089 HOH HOH B . 
X 4 HOH 465 1165 1309 HOH HOH B . 
X 4 HOH 466 1166 868  HOH HOH B . 
X 4 HOH 467 1167 611  HOH HOH B . 
X 4 HOH 468 1168 1074 HOH HOH B . 
X 4 HOH 469 1169 1692 HOH HOH B . 
X 4 HOH 470 1170 1155 HOH HOH B . 
X 4 HOH 471 1171 1108 HOH HOH B . 
X 4 HOH 472 1172 1164 HOH HOH B . 
X 4 HOH 473 1173 1178 HOH HOH B . 
X 4 HOH 474 1174 922  HOH HOH B . 
X 4 HOH 475 1175 905  HOH HOH B . 
X 4 HOH 476 1176 664  HOH HOH B . 
X 4 HOH 477 1177 949  HOH HOH B . 
X 4 HOH 478 1178 1676 HOH HOH B . 
X 4 HOH 479 1179 426  HOH HOH B . 
X 4 HOH 480 1180 600  HOH HOH B . 
X 4 HOH 481 1181 621  HOH HOH B . 
X 4 HOH 482 1182 892  HOH HOH B . 
X 4 HOH 483 1183 1632 HOH HOH B . 
X 4 HOH 484 1184 1395 HOH HOH B . 
X 4 HOH 485 1185 1723 HOH HOH B . 
X 4 HOH 486 1186 1158 HOH HOH B . 
X 4 HOH 487 1187 1123 HOH HOH B . 
X 4 HOH 488 1188 595  HOH HOH B . 
X 4 HOH 489 1189 1704 HOH HOH B . 
X 4 HOH 490 1190 1363 HOH HOH B . 
X 4 HOH 491 1191 1156 HOH HOH B . 
X 4 HOH 492 1192 820  HOH HOH B . 
X 4 HOH 493 1193 1549 HOH HOH B . 
X 4 HOH 494 1194 148  HOH HOH B . 
X 4 HOH 495 1195 1036 HOH HOH B . 
X 4 HOH 496 1196 1600 HOH HOH B . 
X 4 HOH 497 1197 453  HOH HOH B . 
X 4 HOH 498 1198 405  HOH HOH B . 
X 4 HOH 499 1199 964  HOH HOH B . 
X 4 HOH 500 1200 1227 HOH HOH B . 
X 4 HOH 501 1201 1638 HOH HOH B . 
X 4 HOH 502 1202 1314 HOH HOH B . 
X 4 HOH 503 1203 1601 HOH HOH B . 
X 4 HOH 504 1204 1035 HOH HOH B . 
X 4 HOH 505 1205 1360 HOH HOH B . 
X 4 HOH 506 1206 710  HOH HOH B . 
X 4 HOH 507 1207 1349 HOH HOH B . 
X 4 HOH 508 1208 1665 HOH HOH B . 
X 4 HOH 509 1209 1583 HOH HOH B . 
X 4 HOH 510 1210 1570 HOH HOH B . 
X 4 HOH 511 1211 1518 HOH HOH B . 
X 4 HOH 512 1212 1214 HOH HOH B . 
X 4 HOH 513 1213 1236 HOH HOH B . 
X 4 HOH 514 1214 962  HOH HOH B . 
X 4 HOH 515 1215 1055 HOH HOH B . 
X 4 HOH 516 1216 860  HOH HOH B . 
X 4 HOH 517 1217 817  HOH HOH B . 
X 4 HOH 518 1218 415  HOH HOH B . 
X 4 HOH 519 1219 767  HOH HOH B . 
X 4 HOH 520 1220 833  HOH HOH B . 
X 4 HOH 521 1221 203  HOH HOH B . 
X 4 HOH 522 1222 711  HOH HOH B . 
X 4 HOH 523 1223 632  HOH HOH B . 
X 4 HOH 524 1224 267  HOH HOH B . 
X 4 HOH 525 1225 677  HOH HOH B . 
X 4 HOH 526 1226 307  HOH HOH B . 
X 4 HOH 527 1227 1116 HOH HOH B . 
X 4 HOH 528 1228 1603 HOH HOH B . 
X 4 HOH 529 1229 761  HOH HOH B . 
X 4 HOH 530 1230 1016 HOH HOH B . 
X 4 HOH 531 1231 1375 HOH HOH B . 
X 4 HOH 532 1232 777  HOH HOH B . 
X 4 HOH 533 1233 1110 HOH HOH B . 
X 4 HOH 534 1234 1150 HOH HOH B . 
X 4 HOH 535 1235 1648 HOH HOH B . 
X 4 HOH 536 1236 642  HOH HOH B . 
X 4 HOH 537 1237 1636 HOH HOH B . 
X 4 HOH 538 1238 845  HOH HOH B . 
X 4 HOH 539 1239 1505 HOH HOH B . 
X 4 HOH 540 1240 1176 HOH HOH B . 
X 4 HOH 541 1241 1641 HOH HOH B . 
X 4 HOH 542 1242 1525 HOH HOH B . 
X 4 HOH 543 1243 221  HOH HOH B . 
X 4 HOH 544 1244 1204 HOH HOH B . 
X 4 HOH 545 1245 1027 HOH HOH B . 
X 4 HOH 546 1246 601  HOH HOH B . 
X 4 HOH 547 1247 626  HOH HOH B . 
X 4 HOH 548 1248 269  HOH HOH B . 
X 4 HOH 549 1249 1354 HOH HOH B . 
X 4 HOH 550 1250 619  HOH HOH B . 
X 4 HOH 551 1251 384  HOH HOH B . 
X 4 HOH 552 1252 472  HOH HOH B . 
X 4 HOH 553 1253 1562 HOH HOH B . 
X 4 HOH 554 1254 749  HOH HOH B . 
X 4 HOH 555 1255 672  HOH HOH B . 
X 4 HOH 556 1256 312  HOH HOH B . 
X 4 HOH 557 1257 1275 HOH HOH B . 
X 4 HOH 558 1258 1107 HOH HOH B . 
X 4 HOH 559 1259 369  HOH HOH B . 
X 4 HOH 560 1260 696  HOH HOH B . 
X 4 HOH 561 1261 707  HOH HOH B . 
X 4 HOH 562 1262 1619 HOH HOH B . 
X 4 HOH 563 1263 1684 HOH HOH B . 
X 4 HOH 564 1264 760  HOH HOH B . 
X 4 HOH 565 1265 478  HOH HOH B . 
X 4 HOH 566 1266 646  HOH HOH B . 
X 4 HOH 567 1267 555  HOH HOH B . 
X 4 HOH 568 1268 1591 HOH HOH B . 
X 4 HOH 569 1269 1674 HOH HOH B . 
X 4 HOH 570 1270 1671 HOH HOH B . 
X 4 HOH 571 1271 424  HOH HOH B . 
X 4 HOH 572 1272 1602 HOH HOH B . 
X 4 HOH 573 1273 657  HOH HOH B . 
X 4 HOH 574 1274 807  HOH HOH B . 
X 4 HOH 575 1275 1590 HOH HOH B . 
X 4 HOH 576 1276 1380 HOH HOH B . 
X 4 HOH 577 1277 507  HOH HOH B . 
X 4 HOH 578 1278 1484 HOH HOH B . 
X 4 HOH 579 1279 1644 HOH HOH B . 
X 4 HOH 580 1280 1597 HOH HOH B . 
X 4 HOH 581 1281 573  HOH HOH B . 
X 4 HOH 582 1282 997  HOH HOH B . 
X 4 HOH 583 1283 1329 HOH HOH B . 
X 4 HOH 584 1284 392  HOH HOH B . 
X 4 HOH 585 1285 594  HOH HOH B . 
X 4 HOH 586 1286 1523 HOH HOH B . 
X 4 HOH 587 1287 225  HOH HOH B . 
X 4 HOH 588 1288 544  HOH HOH B . 
X 4 HOH 589 1289 213  HOH HOH B . 
X 4 HOH 590 1290 1133 HOH HOH B . 
X 4 HOH 591 1291 1008 HOH HOH B . 
X 4 HOH 592 1292 1396 HOH HOH B . 
X 4 HOH 593 1293 1372 HOH HOH B . 
X 4 HOH 594 1294 1635 HOH HOH B . 
X 4 HOH 595 1295 908  HOH HOH B . 
X 4 HOH 596 1296 1680 HOH HOH B . 
X 4 HOH 597 1297 1247 HOH HOH B . 
X 4 HOH 598 1298 720  HOH HOH B . 
X 4 HOH 599 1299 1697 HOH HOH B . 
X 4 HOH 600 1300 1232 HOH HOH B . 
X 4 HOH 601 1301 87   HOH HOH B . 
X 4 HOH 602 1302 758  HOH HOH B . 
X 4 HOH 603 1303 1369 HOH HOH B . 
X 4 HOH 604 1304 723  HOH HOH B . 
X 4 HOH 605 1305 1618 HOH HOH B . 
X 4 HOH 606 1306 1357 HOH HOH B . 
X 4 HOH 607 1307 1667 HOH HOH B . 
X 4 HOH 608 1308 515  HOH HOH B . 
X 4 HOH 609 1309 293  HOH HOH B . 
X 4 HOH 610 1310 1367 HOH HOH B . 
X 4 HOH 611 1311 1012 HOH HOH B . 
X 4 HOH 612 1312 625  HOH HOH B . 
X 4 HOH 613 1313 466  HOH HOH B . 
X 4 HOH 614 1314 1575 HOH HOH B . 
X 4 HOH 615 1315 1381 HOH HOH B . 
X 4 HOH 616 1316 675  HOH HOH B . 
X 4 HOH 617 1317 1356 HOH HOH B . 
X 4 HOH 618 1318 1280 HOH HOH B . 
X 4 HOH 619 1319 1279 HOH HOH B . 
X 4 HOH 620 1320 1664 HOH HOH B . 
X 4 HOH 621 1321 678  HOH HOH B . 
X 4 HOH 622 1322 982  HOH HOH B . 
X 4 HOH 623 1323 1578 HOH HOH B . 
X 4 HOH 624 1324 589  HOH HOH B . 
X 4 HOH 625 1325 682  HOH HOH B . 
X 4 HOH 626 1326 898  HOH HOH B . 
X 4 HOH 627 1327 200  HOH HOH B . 
X 4 HOH 628 1328 1587 HOH HOH B . 
X 4 HOH 629 1329 1092 HOH HOH B . 
X 4 HOH 630 1330 854  HOH HOH B . 
X 4 HOH 631 1331 1377 HOH HOH B . 
X 4 HOH 632 1332 1007 HOH HOH B . 
X 4 HOH 633 1333 1709 HOH HOH B . 
X 4 HOH 634 1334 1496 HOH HOH B . 
X 4 HOH 635 1335 1371 HOH HOH B . 
X 4 HOH 636 1336 797  HOH HOH B . 
X 4 HOH 637 1337 1392 HOH HOH B . 
X 4 HOH 638 1338 501  HOH HOH B . 
X 4 HOH 639 1339 680  HOH HOH B . 
X 4 HOH 640 1340 1277 HOH HOH B . 
X 4 HOH 641 1341 1397 HOH HOH B . 
X 4 HOH 642 1342 380  HOH HOH B . 
X 4 HOH 643 1343 1386 HOH HOH B . 
X 4 HOH 644 1344 978  HOH HOH B . 
X 4 HOH 645 1345 1410 HOH HOH B . 
X 4 HOH 646 1346 663  HOH HOH B . 
X 4 HOH 647 1347 1693 HOH HOH B . 
X 4 HOH 648 1348 1175 HOH HOH B . 
X 4 HOH 649 1349 709  HOH HOH B . 
X 4 HOH 650 1350 1028 HOH HOH B . 
X 4 HOH 651 1351 800  HOH HOH B . 
X 4 HOH 652 1352 783  HOH HOH B . 
X 4 HOH 653 1353 853  HOH HOH B . 
X 4 HOH 654 1354 1527 HOH HOH B . 
X 4 HOH 655 1355 1374 HOH HOH B . 
X 4 HOH 656 1356 1584 HOH HOH B . 
X 4 HOH 657 1357 1426 HOH HOH B . 
X 4 HOH 658 1358 1210 HOH HOH B . 
X 4 HOH 659 1359 1551 HOH HOH B . 
X 4 HOH 660 1360 808  HOH HOH B . 
X 4 HOH 661 1361 1326 HOH HOH B . 
X 4 HOH 662 1362 1485 HOH HOH B . 
X 4 HOH 663 1363 1694 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ASN 296 ? CG  ? A ASN 73 CG  
2 1 Y 1 A ASN 296 ? OD1 ? A ASN 73 OD1 
3 1 Y 1 A ASN 296 ? ND2 ? A ASN 73 ND2 
4 1 Y 1 A ASP 297 ? CG  ? A ASP 74 CG  
5 1 Y 1 A ASP 297 ? OD1 ? A ASP 74 OD1 
6 1 Y 1 A ASP 297 ? OD2 ? A ASP 74 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.20.1_4487 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.8       2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .           3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 9.0.002     4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .           5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   113.44 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EDN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.140 
_cell.length_a_esd                 ? 
_cell.length_b                     80.960 
_cell.length_b_esd                 ? 
_cell.length_c                     71.790 
_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                         9EDN 
_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                   9EDN 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.87 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M sodium acetate (pH 4.6), 8% w/v PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-12 
_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   0.95373 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95373 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EDN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.21 
_reflns.d_resolution_low                               45.59 
_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                                     185707 
_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                           97.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.43 
_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                                0.141 
_reflns.pdbx_Rpim_I_all                                0.071 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.121 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.21 
_reflns_shell.d_res_low                                     1.23 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           19626 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5677 
_reflns_shell.percent_possible_obs                          60.5 
_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                               3.5 
_reflns_shell.pdbx_chi_squared                              0.31 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.1 
_reflns_shell.pdbx_Rrim_I_all                               0.803 
_reflns_shell.pdbx_Rpim_I_all                               0.396 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.688 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.695 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EDN 
_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                            1.22 
_refine.ls_d_res_low                             40.48 
_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                     185707 
_refine.ls_number_reflns_R_free                  9286 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.43 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1238 
_refine.ls_R_factor_R_free                       0.1463 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1226 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 13.21 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.09 
_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                       1.22 
_refine_hist.d_res_low                        40.48 
_refine_hist.number_atoms_solvent             1345 
_refine_hist.number_atoms_total               6266 
_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        4850 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         71 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 5391 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.000  ? 7419 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.977 ? 2065 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.086  ? 801  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 997  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.22 1.23  . . 286 5437 93.00  . . . . 0.1585 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 1.23 1.25  . . 307 5853 99.00  . . . . 0.1466 . . . . . . . . . . . 0.1822 
'X-RAY DIFFRACTION' 1.25 1.26  . . 308 5853 99.00  . . . . 0.1483 . . . . . . . . . . . 0.1885 
'X-RAY DIFFRACTION' 1.26 1.28  . . 313 5938 100.00 . . . . 0.1452 . . . . . . . . . . . 0.1679 
'X-RAY DIFFRACTION' 1.28 1.30  . . 307 5837 100.00 . . . . 0.1444 . . . . . . . . . . . 0.1889 
'X-RAY DIFFRACTION' 1.30 1.31  . . 310 5888 100.00 . . . . 0.1442 . . . . . . . . . . . 0.1722 
'X-RAY DIFFRACTION' 1.31 1.33  . . 310 5883 100.00 . . . . 0.1458 . . . . . . . . . . . 0.1819 
'X-RAY DIFFRACTION' 1.33 1.35  . . 311 5899 100.00 . . . . 0.1479 . . . . . . . . . . . 0.1822 
'X-RAY DIFFRACTION' 1.35 1.37  . . 308 5856 100.00 . . . . 0.1503 . . . . . . . . . . . 0.1668 
'X-RAY DIFFRACTION' 1.37 1.40  . . 312 5921 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1720 
'X-RAY DIFFRACTION' 1.40 1.42  . . 309 5868 100.00 . . . . 0.1303 . . . . . . . . . . . 0.1700 
'X-RAY DIFFRACTION' 1.42 1.45  . . 308 5861 100.00 . . . . 0.1299 . . . . . . . . . . . 0.1682 
'X-RAY DIFFRACTION' 1.45 1.47  . . 311 5901 100.00 . . . . 0.1210 . . . . . . . . . . . 0.1506 
'X-RAY DIFFRACTION' 1.47 1.51  . . 312 5926 100.00 . . . . 0.1154 . . . . . . . . . . . 0.1455 
'X-RAY DIFFRACTION' 1.51 1.54  . . 307 5841 100.00 . . . . 0.1144 . . . . . . . . . . . 0.1500 
'X-RAY DIFFRACTION' 1.54 1.57  . . 310 5884 100.00 . . . . 0.1165 . . . . . . . . . . . 0.1526 
'X-RAY DIFFRACTION' 1.57 1.61  . . 312 5916 100.00 . . . . 0.1137 . . . . . . . . . . . 0.1377 
'X-RAY DIFFRACTION' 1.61 1.66  . . 312 5923 100.00 . . . . 0.1202 . . . . . . . . . . . 0.1461 
'X-RAY DIFFRACTION' 1.66 1.71  . . 310 5888 100.00 . . . . 0.1224 . . . . . . . . . . . 0.1576 
'X-RAY DIFFRACTION' 1.71 1.76  . . 309 5884 100.00 . . . . 0.1230 . . . . . . . . . . . 0.1423 
'X-RAY DIFFRACTION' 1.76 1.82  . . 309 5881 100.00 . . . . 0.1258 . . . . . . . . . . . 0.1465 
'X-RAY DIFFRACTION' 1.82 1.90  . . 310 5888 100.00 . . . . 0.1233 . . . . . . . . . . . 0.1418 
'X-RAY DIFFRACTION' 1.90 1.98  . . 311 5906 100.00 . . . . 0.1212 . . . . . . . . . . . 0.1335 
'X-RAY DIFFRACTION' 1.98 2.09  . . 312 5910 100.00 . . . . 0.1144 . . . . . . . . . . . 0.1228 
'X-RAY DIFFRACTION' 2.09 2.22  . . 310 5893 100.00 . . . . 0.1120 . . . . . . . . . . . 0.1286 
'X-RAY DIFFRACTION' 2.22 2.39  . . 312 5930 100.00 . . . . 0.1110 . . . . . . . . . . . 0.1293 
'X-RAY DIFFRACTION' 2.39 2.63  . . 312 5922 100.00 . . . . 0.1194 . . . . . . . . . . . 0.1456 
'X-RAY DIFFRACTION' 2.63 3.01  . . 312 5925 99.00  . . . . 0.1193 . . . . . . . . . . . 0.1307 
'X-RAY DIFFRACTION' 3.01 3.79  . . 310 5907 99.00  . . . . 0.1081 . . . . . . . . . . . 0.1304 
'X-RAY DIFFRACTION' 3.79 40.48 . . 316 6002 99.00  . . . . 0.1260 . . . . . . . . . . . 0.1530 
# 
_struct.entry_id                     9EDN 
_struct.title                        'GII.23: Loreto1847 norovirus protruding domain' 
_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        9EDN 
_struct_keywords.text            'norovirus, P domain, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 2 ? 
T N N 2 ? 
U N N 2 ? 
V N N 3 ? 
W N N 4 ? 
X N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0U2T5K7_9CALI 
_struct_ref.pdbx_db_accession          A0A0U2T5K7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KPFTIPILTIGEMTNSRFPVPIDMLHTSPTENIVVQPQNGRCTIDGELLGTTQLITSNICSFRGSISGHEGNDDQHLWHF
NITNPNGTPFDPTEDVPAPLGTPDFRGQLYGVISQRDREGTPSENNQKANRSHQGVISTISPKFVPKLGSVMIGTWTTDD
IKNQPSKFTPIGLNDDDNFKQWELPNYSGALTLNMGLAPSVFPTYPGEQILFFRSYLPLKGGYGSPFIDCLVPQEWVAHF
YQESAPAQTDVALIRYVNPETGRVLFEAKLHRQGFITVAKSGDSPINVPANGYFRFDSWVNQFYSLAPM
;
_struct_ref.pdbx_align_begin           225 
# 
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 9EDN A 2 ? 310 ? A0A0U2T5K7 225 ? 533 ? 225 533 
2 1 9EDN B 2 ? 310 ? A0A0U2T5K7 225 ? 533 ? 225 533 
# 
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 9EDN SER A 1 ? UNP A0A0U2T5K7 ? ? 'expression tag' 224 1 
2 9EDN SER B 1 ? UNP A0A0U2T5K7 ? ? 'expression tag' 224 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7050  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  25200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X 
# 
_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 THR A 10  ? MET A 14  ? THR A 233 MET A 237 5 ? 5  
HELX_P HELX_P2  AA2 ILE A 56  ? ILE A 60  ? ILE A 279 ILE A 283 5 ? 5  
HELX_P HELX_P3  AA3 THR A 122 ? ASN A 126 ? THR A 345 ASN A 349 5 ? 5  
HELX_P HELX_P4  AA4 VAL A 146 ? LEU A 149 ? VAL A 369 LEU A 372 5 ? 4  
HELX_P HELX_P5  AA5 PRO A 234 ? SER A 245 ? PRO A 457 SER A 468 1 ? 12 
HELX_P HELX_P6  AA6 THR B 10  ? MET B 14  ? THR B 233 MET B 237 5 ? 5  
HELX_P HELX_P7  AA7 ILE B 56  ? ILE B 60  ? ILE B 279 ILE B 283 5 ? 5  
HELX_P HELX_P8  AA8 THR B 122 ? ASN B 126 ? THR B 345 ASN B 349 5 ? 5  
HELX_P HELX_P9  AA9 VAL B 146 ? LEU B 149 ? VAL B 369 LEU B 372 5 ? 4  
HELX_P HELX_P10 AB1 PRO B 234 ? SER B 245 ? PRO B 457 SER B 468 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
AA4 ? 3 ? 
AA5 ? 6 ? 
AA6 ? 8 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA6 7 8 ? 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 MET A 25  ? THR A 28  ? MET A 248 THR A 251 
AA1 2 GLU A 209 ? TYR A 217 ? GLU A 432 TYR A 440 
AA1 3 PHE A 228 ? CYS A 231 ? PHE A 451 CYS A 454 
AA2 1 MET A 25  ? THR A 28  ? MET A 248 THR A 251 
AA2 2 GLU A 209 ? TYR A 217 ? GLU A 432 TYR A 440 
AA2 3 PHE A 276 ? ALA A 280 ? PHE A 499 ALA A 503 
AA2 4 VAL A 265 ? HIS A 272 ? VAL A 488 HIS A 495 
AA2 5 VAL A 252 ? VAL A 258 ? VAL A 475 VAL A 481 
AA2 6 TYR A 294 ? VAL A 301 ? TYR A 517 VAL A 524 
AA3 1 PHE A 63  ? HIS A 70  ? PHE A 286 HIS A 293 
AA3 2 LEU A 78  ? ILE A 83  ? LEU A 301 ILE A 306 
AA3 3 SER A 151 ? GLY A 155 ? SER A 374 GLY A 378 
AA3 4 ASN A 131 ? SER A 139 ? ASN A 354 SER A 362 
AA3 5 GLN A 109 ? ARG A 117 ? GLN A 332 ARG A 340 
AA3 6 PRO A 166 ? LEU A 174 ? PRO A 389 LEU A 397 
AA3 7 PHE A 63  ? HIS A 70  ? PHE A 286 HIS A 293 
AA4 1 MET B 25  ? THR B 28  ? MET B 248 THR B 251 
AA4 2 GLU B 209 ? TYR B 217 ? GLU B 432 TYR B 440 
AA4 3 PHE B 228 ? CYS B 231 ? PHE B 451 CYS B 454 
AA5 1 MET B 25  ? THR B 28  ? MET B 248 THR B 251 
AA5 2 GLU B 209 ? TYR B 217 ? GLU B 432 TYR B 440 
AA5 3 PHE B 276 ? ALA B 280 ? PHE B 499 ALA B 503 
AA5 4 VAL B 265 ? HIS B 272 ? VAL B 488 HIS B 495 
AA5 5 VAL B 252 ? VAL B 258 ? VAL B 475 VAL B 481 
AA5 6 TYR B 294 ? VAL B 301 ? TYR B 517 VAL B 524 
AA6 1 GLU B 71  ? ASN B 73  ? GLU B 294 ASN B 296 
AA6 2 GLN B 76  ? ILE B 83  ? GLN B 299 ILE B 306 
AA6 3 SER B 151 ? GLY B 155 ? SER B 374 GLY B 378 
AA6 4 ASN B 131 ? SER B 139 ? ASN B 354 SER B 362 
AA6 5 GLN B 109 ? ARG B 117 ? GLN B 332 ARG B 340 
AA6 6 PRO B 166 ? LEU B 174 ? PRO B 389 LEU B 397 
AA6 7 PHE B 63  ? ILE B 67  ? PHE B 286 ILE B 290 
AA6 8 GLN B 76  ? ILE B 83  ? GLN B 299 ILE B 306 
# 
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 HIS A 27  ? N HIS A 250 O PHE A 213 ? O PHE A 436 
AA1 2 3 N PHE A 214 ? N PHE A 437 O CYS A 231 ? O CYS A 454 
AA2 1 2 N HIS A 27  ? N HIS A 250 O PHE A 213 ? O PHE A 436 
AA2 2 3 N GLN A 210 ? N GLN A 433 O VAL A 279 ? O VAL A 502 
AA2 3 4 O PHE A 276 ? O PHE A 499 N HIS A 272 ? N HIS A 495 
AA2 4 5 O LEU A 266 ? O LEU A 489 N TYR A 257 ? N TYR A 480 
AA2 5 6 N LEU A 254 ? N LEU A 477 O SER A 299 ? O SER A 522 
AA3 1 2 N SER A 68  ? N SER A 291 O HIS A 80  ? O HIS A 303 
AA3 2 3 N PHE A 81  ? N PHE A 304 O VAL A 152 ? O VAL A 375 
AA3 3 4 O GLY A 155 ? O GLY A 378 N VAL A 137 ? N VAL A 360 
AA3 4 5 O ILE A 138 ? O ILE A 361 N LEU A 110 ? N LEU A 333 
AA3 5 6 N TYR A 111 ? N TYR A 334 O ILE A 172 ? O ILE A 395 
AA3 6 7 O PHE A 169 ? O PHE A 392 N PHE A 63  ? N PHE A 286 
AA4 1 2 N HIS B 27  ? N HIS B 250 O PHE B 213 ? O PHE B 436 
AA4 2 3 N PHE B 214 ? N PHE B 437 O CYS B 231 ? O CYS B 454 
AA5 1 2 N HIS B 27  ? N HIS B 250 O PHE B 213 ? O PHE B 436 
AA5 2 3 N GLN B 210 ? N GLN B 433 O VAL B 279 ? O VAL B 502 
AA5 3 4 O PHE B 276 ? O PHE B 499 N HIS B 272 ? N HIS B 495 
AA5 4 5 O LEU B 266 ? O LEU B 489 N TYR B 257 ? N TYR B 480 
AA5 5 6 N LEU B 254 ? N LEU B 477 O SER B 299 ? O SER B 522 
AA6 1 2 N GLU B 71  ? N GLU B 294 O LEU B 78  ? O LEU B 301 
AA6 2 3 N PHE B 81  ? N PHE B 304 O VAL B 152 ? O VAL B 375 
AA6 3 4 O GLY B 155 ? O GLY B 378 N VAL B 137 ? N VAL B 360 
AA6 4 5 O ARG B 132 ? O ARG B 355 N GLN B 116 ? N GLN B 339 
AA6 5 6 N TYR B 111 ? N TYR B 334 O ILE B 172 ? O ILE B 395 
AA6 6 7 O PHE B 169 ? O PHE B 392 N PHE B 63  ? N PHE B 286 
AA6 7 8 N SER B 66  ? N SER B 289 O ASN B 82  ? O ASN B 305 
# 
_pdbx_entry_details.entry_id                   9EDN 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HZ2 A LYS 391  ? A O A HOH 721  ? ? 1.57 
2 1 O   B HOH 973  ? ? O B HOH 1228 ? ? 2.19 
3 1 O   A HOH 1359 ? ? O B HOH 1246 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 296 ? ? -96.47  -124.84 
2 1 ASP A 298 ? ? 67.24   -52.73  
3 1 TRP A 380 ? ? 55.87   -127.35 
4 1 VAL A 524 ? ? -127.98 -158.79 
5 1 PRO B 226 ? ? -66.60  -167.55 
6 1 ASP B 297 ? ? 60.43   -123.52 
7 1 TRP B 380 ? ? 56.00   -130.10 
8 1 VAL B 524 ? ? -127.68 -158.17 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     342 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.080 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1363 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.57 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      224 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_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   4OOS 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EDN 
_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]   0.016628 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007209 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012352 
_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]   0.015182 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
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    . SER A 1 1   ? -12.932 6.643   36.370  1.00 37.20  ?  224  SER A N    1 
ATOM   2     C  CA   . SER A 1 1   ? -11.541 6.535   35.947  1.00 29.78  ?  224  SER A CA   1 
ATOM   3     C  C    . SER A 1 1   ? -11.411 6.837   34.462  1.00 19.99  ?  224  SER A C    1 
ATOM   4     O  O    . SER A 1 1   ? -12.229 6.390   33.658  1.00 21.46  ?  224  SER A O    1 
ATOM   5     C  CB   . SER A 1 1   ? -11.006 5.131   36.224  1.00 34.08  ?  224  SER A CB   1 
ATOM   6     O  OG   . SER A 1 1   ? -10.883 4.897   37.616  1.00 72.02  ?  224  SER A OG   1 
ATOM   7     H  HA   . SER A 1 1   ? -11.007 7.172   36.446  1.00 35.74  ?  224  SER A HA   1 
ATOM   8     H  HB2  . SER A 1 1   ? -11.621 4.480   35.849  1.00 40.90  ?  224  SER A HB2  1 
ATOM   9     H  HB3  . SER A 1 1   ? -10.133 5.039   35.811  1.00 40.90  ?  224  SER A HB3  1 
ATOM   10    H  HG   . SER A 1 1   ? -11.635 4.961   37.985  1.00 86.42  ?  224  SER A HG   1 
ATOM   11    N  N    . LYS A 1 2   ? -10.375 7.584   34.106  1.00 18.41  ?  225  LYS A N    1 
ATOM   12    C  CA   . LYS A 1 2   ? -10.136 7.892   32.704  1.00 17.14  ?  225  LYS A CA   1 
ATOM   13    C  C    . LYS A 1 2   ? -9.961  6.595   31.919  1.00 14.33  ?  225  LYS A C    1 
ATOM   14    O  O    . LYS A 1 2   ? -9.120  5.765   32.288  1.00 14.10  ?  225  LYS A O    1 
ATOM   15    C  CB   . LYS A 1 2   ? -8.875  8.745   32.560  1.00 18.37  ?  225  LYS A CB   1 
ATOM   16    C  CG   . LYS A 1 2   ? -8.566  9.098   31.117  1.00 19.62  ?  225  LYS A CG   1 
ATOM   17    C  CD   . LYS A 1 2   ? -7.212  9.747   30.946  1.00 20.52  ?  225  LYS A CD   1 
ATOM   18    C  CE   . LYS A 1 2   ? -7.242  11.203  31.265  1.00 21.41  ?  225  LYS A CE   1 
ATOM   19    N  NZ   . LYS A 1 2   ? -5.987  11.856  30.869  1.00 20.61  ?  225  LYS A NZ   1 
ATOM   20    H  H    . LYS A 1 2   ? -9.801  7.922   34.650  1.00 22.09  ?  225  LYS A H    1 
ATOM   21    H  HA   . LYS A 1 2   ? -10.891 8.384   32.346  1.00 20.57  ?  225  LYS A HA   1 
ATOM   22    H  HB2  . LYS A 1 2   ? -8.996  9.572   33.053  1.00 22.04  ?  225  LYS A HB2  1 
ATOM   23    H  HB3  . LYS A 1 2   ? -8.119  8.253   32.918  1.00 22.04  ?  225  LYS A HB3  1 
ATOM   24    H  HG2  . LYS A 1 2   ? -8.578  8.288   30.584  1.00 23.55  ?  225  LYS A HG2  1 
ATOM   25    H  HG3  . LYS A 1 2   ? -9.238  9.718   30.793  1.00 23.55  ?  225  LYS A HG3  1 
ATOM   26    H  HD2  . LYS A 1 2   ? -6.577  9.320   31.541  1.00 24.62  ?  225  LYS A HD2  1 
ATOM   27    H  HD3  . LYS A 1 2   ? -6.925  9.646   30.025  1.00 24.62  ?  225  LYS A HD3  1 
ATOM   28    H  HE2  . LYS A 1 2   ? -7.972  11.624  30.785  1.00 25.69  ?  225  LYS A HE2  1 
ATOM   29    H  HE3  . LYS A 1 2   ? -7.361  11.322  32.220  1.00 25.69  ?  225  LYS A HE3  1 
ATOM   30    H  HZ1  . LYS A 1 2   ? -6.025  12.726  31.052  1.00 24.73  ?  225  LYS A HZ1  1 
ATOM   31    H  HZ2  . LYS A 1 2   ? -5.304  11.497  31.312  1.00 24.73  ?  225  LYS A HZ2  1 
ATOM   32    H  HZ3  . LYS A 1 2   ? -5.852  11.751  29.995  1.00 24.73  ?  225  LYS A HZ3  1 
ATOM   33    N  N    . PRO A 1 3   ? -10.723 6.378   30.845  1.00 13.95  ?  226  PRO A N    1 
ATOM   34    C  CA   . PRO A 1 3   ? -10.549 5.147   30.068  1.00 13.59  ?  226  PRO A CA   1 
ATOM   35    C  C    . PRO A 1 3   ? -9.158  5.040   29.457  1.00 11.92  ?  226  PRO A C    1 
ATOM   36    O  O    . PRO A 1 3   ? -8.612  6.002   28.912  1.00 12.24  ?  226  PRO A O    1 
ATOM   37    C  CB   . PRO A 1 3   ? -11.618 5.255   28.978  1.00 16.16  ?  226  PRO A CB   1 
ATOM   38    C  CG   . PRO A 1 3   ? -12.668 6.148   29.563  1.00 17.08  ?  226  PRO A CG   1 
ATOM   39    C  CD   . PRO A 1 3   ? -11.920 7.134   30.418  1.00 16.18  ?  226  PRO A CD   1 
ATOM   40    H  HA   . PRO A 1 3   ? -10.716 4.376   30.633  1.00 16.31  ?  226  PRO A HA   1 
ATOM   41    H  HB2  . PRO A 1 3   ? -11.235 5.646   28.177  1.00 19.40  ?  226  PRO A HB2  1 
ATOM   42    H  HB3  . PRO A 1 3   ? -11.979 4.377   28.779  1.00 19.40  ?  226  PRO A HB3  1 
ATOM   43    H  HG2  . PRO A 1 3   ? -13.147 6.602   28.852  1.00 20.50  ?  226  PRO A HG2  1 
ATOM   44    H  HG3  . PRO A 1 3   ? -13.284 5.625   30.098  1.00 20.50  ?  226  PRO A HG3  1 
ATOM   45    H  HD2  . PRO A 1 3   ? -11.669 7.917   29.903  1.00 19.42  ?  226  PRO A HD2  1 
ATOM   46    H  HD3  . PRO A 1 3   ? -12.452 7.399   31.185  1.00 19.42  ?  226  PRO A HD3  1 
ATOM   47    N  N    . PHE A 1 4   ? -8.597  3.840   29.534  1.00 10.35  ?  227  PHE A N    1 
ATOM   48    C  CA   . PHE A 1 4   ? -7.334  3.529   28.888  1.00 9.91   ?  227  PHE A CA   1 
ATOM   49    C  C    . PHE A 1 4   ? -7.529  3.366   27.384  1.00 9.68   ?  227  PHE A C    1 
ATOM   50    O  O    . PHE A 1 4   ? -8.493  2.755   26.923  1.00 10.91  ?  227  PHE A O    1 
ATOM   51    C  CB   . PHE A 1 4   ? -6.757  2.252   29.502  1.00 9.79   ?  227  PHE A CB   1 
ATOM   52    C  CG   . PHE A 1 4   ? -5.499  1.798   28.849  1.00 8.92   ?  227  PHE A CG   1 
ATOM   53    C  CD1  . PHE A 1 4   ? -4.333  2.560   28.938  1.00 9.67   ?  227  PHE A CD1  1 
ATOM   54    C  CD2  . PHE A 1 4   ? -5.469  0.629   28.107  1.00 9.84   ?  227  PHE A CD2  1 
ATOM   55    C  CE1  . PHE A 1 4   ? -3.174  2.141   28.320  1.00 8.87   ?  227  PHE A CE1  1 
ATOM   56    C  CE2  . PHE A 1 4   ? -4.310  0.214   27.498  1.00 9.89   ?  227  PHE A CE2  1 
ATOM   57    C  CZ   . PHE A 1 4   ? -3.164  0.980   27.599  1.00 9.40   ?  227  PHE A CZ   1 
ATOM   58    H  H    . PHE A 1 4   ? -8.936  3.177   29.964  1.00 12.43  ?  227  PHE A H    1 
ATOM   59    H  HA   . PHE A 1 4   ? -6.698  4.250   29.020  1.00 11.90  ?  227  PHE A HA   1 
ATOM   60    H  HB2  . PHE A 1 4   ? -6.564  2.415   30.439  1.00 11.75  ?  227  PHE A HB2  1 
ATOM   61    H  HB3  . PHE A 1 4   ? -7.410  1.540   29.417  1.00 11.75  ?  227  PHE A HB3  1 
ATOM   62    H  HD1  . PHE A 1 4   ? -4.337  3.356   29.419  1.00 11.61  ?  227  PHE A HD1  1 
ATOM   63    H  HD2  . PHE A 1 4   ? -6.242  0.120   28.021  1.00 11.81  ?  227  PHE A HD2  1 
ATOM   64    H  HE1  . PHE A 1 4   ? -2.398  2.648   28.393  1.00 10.64  ?  227  PHE A HE1  1 
ATOM   65    H  HE2  . PHE A 1 4   ? -4.297  -0.582  27.017  1.00 11.86  ?  227  PHE A HE2  1 
ATOM   66    H  HZ   . PHE A 1 4   ? -2.384  0.704   27.175  1.00 11.28  ?  227  PHE A HZ   1 
ATOM   67    N  N    . THR A 1 5   ? -6.596  3.918   26.608  1.00 8.84   ?  228  THR A N    1 
ATOM   68    C  CA   . THR A 1 5   ? -6.646  3.856   25.154  1.00 8.22   ?  228  THR A CA   1 
ATOM   69    C  C    . THR A 1 5   ? -5.241  3.680   24.595  1.00 7.20   ?  228  THR A C    1 
ATOM   70    O  O    . THR A 1 5   ? -4.237  4.045   25.224  1.00 7.78   ?  228  THR A O    1 
ATOM   71    C  CB   . THR A 1 5   ? -7.248  5.134   24.542  1.00 9.07   ?  228  THR A CB   1 
ATOM   72    O  OG1  . THR A 1 5   ? -6.410  6.262   24.844  1.00 9.30   ?  228  THR A OG1  1 
ATOM   73    C  CG2  . THR A 1 5   ? -8.696  5.392   25.017  1.00 10.01  ?  228  THR A CG2  1 
ATOM   74    H  H    . THR A 1 5   ? -5.911  4.342   26.910  1.00 10.61  ?  228  THR A H    1 
ATOM   75    H  HA   . THR A 1 5   ? -7.188  3.091   24.906  1.00 9.86   ?  228  THR A HA   1 
ATOM   76    H  HB   . THR A 1 5   ? -7.295  5.020   23.579  1.00 10.88  ?  228  THR A HB   1 
ATOM   77    H  HG1  . THR A 1 5   ? -6.384  6.386   25.675  1.00 11.17  ?  228  THR A HG1  1 
ATOM   78    H  HG21 . THR A 1 5   ? -9.043  6.198   24.602  1.00 12.01  ?  228  THR A HG21 1 
ATOM   79    H  HG22 . THR A 1 5   ? -9.263  4.644   24.774  1.00 12.01  ?  228  THR A HG22 1 
ATOM   80    H  HG23 . THR A 1 5   ? -8.714  5.502   25.980  1.00 12.01  ?  228  THR A HG23 1 
ATOM   81    N  N    . ILE A 1 6   ? -5.191  3.149   23.377  1.00 7.53   ?  229  ILE A N    1 
ATOM   82    C  CA   . ILE A 1 6   ? -3.969  2.929   22.602  1.00 7.39   ?  229  ILE A CA   1 
ATOM   83    C  C    . ILE A 1 6   ? -4.067  3.753   21.325  1.00 6.82   ?  229  ILE A C    1 
ATOM   84    O  O    . ILE A 1 6   ? -5.164  3.875   20.774  1.00 6.81   ?  229  ILE A O    1 
ATOM   85    C  CB   . ILE A 1 6   ? -3.821  1.432   22.295  1.00 8.29   ?  229  ILE A CB   1 
ATOM   86    C  CG1  . ILE A 1 6   ? -3.658  0.651   23.600  1.00 9.37   ?  229  ILE A CG1  1 
ATOM   87    C  CG2  . ILE A 1 6   ? -2.655  1.143   21.363  1.00 9.15   ?  229  ILE A CG2  1 
ATOM   88    C  CD1  . ILE A 1 6   ? -3.710  -0.844  23.418  1.00 10.22  ?  229  ILE A CD1  1 
ATOM   89    H  H    . ILE A 1 6   ? -5.892  2.892   22.951  1.00 9.03   ?  229  ILE A H    1 
ATOM   90    H  HA   . ILE A 1 6   ? -3.188  3.228   23.094  1.00 8.87   ?  229  ILE A HA   1 
ATOM   91    H  HB   . ILE A 1 6   ? -4.630  1.150   21.839  1.00 9.95   ?  229  ILE A HB   1 
ATOM   92    H  HG12 . ILE A 1 6   ? -2.799  0.873   23.992  1.00 11.24  ?  229  ILE A HG12 1 
ATOM   93    H  HG13 . ILE A 1 6   ? -4.374  0.902   24.205  1.00 11.24  ?  229  ILE A HG13 1 
ATOM   94    H  HG21 . ILE A 1 6   ? -2.577  0.184   21.243  1.00 10.99  ?  229  ILE A HG21 1 
ATOM   95    H  HG22 . ILE A 1 6   ? -2.819  1.572   20.509  1.00 10.99  ?  229  ILE A HG22 1 
ATOM   96    H  HG23 . ILE A 1 6   ? -1.841  1.494   21.758  1.00 10.99  ?  229  ILE A HG23 1 
ATOM   97    H  HD11 . ILE A 1 6   ? -3.805  -1.265  24.286  1.00 12.26  ?  229  ILE A HD11 1 
ATOM   98    H  HD12 . ILE A 1 6   ? -4.470  -1.068  22.857  1.00 12.26  ?  229  ILE A HD12 1 
ATOM   99    H  HD13 . ILE A 1 6   ? -2.889  -1.139  22.994  1.00 12.26  ?  229  ILE A HD13 1 
ATOM   100   N  N    . PRO A 1 7   ? -2.972  4.310   20.803  1.00 6.11   ?  230  PRO A N    1 
ATOM   101   C  CA   . PRO A 1 7   ? -3.065  5.033   19.529  1.00 6.12   ?  230  PRO A CA   1 
ATOM   102   C  C    . PRO A 1 7   ? -3.630  4.161   18.423  1.00 6.30   ?  230  PRO A C    1 
ATOM   103   O  O    . PRO A 1 7   ? -3.467  2.942   18.425  1.00 7.03   ?  230  PRO A O    1 
ATOM   104   C  CB   . PRO A 1 7   ? -1.613  5.419   19.234  1.00 6.91   ?  230  PRO A CB   1 
ATOM   105   C  CG   . PRO A 1 7   ? -0.999  5.541   20.614  1.00 6.98   ?  230  PRO A CG   1 
ATOM   106   C  CD   . PRO A 1 7   ? -1.620  4.421   21.388  1.00 6.98   ?  230  PRO A CD   1 
ATOM   107   H  HA   . PRO A 1 7   ? -3.611  5.828   19.629  1.00 7.35   ?  230  PRO A HA   1 
ATOM   108   H  HB2  . PRO A 1 7   ? -1.178  4.725   18.714  1.00 8.29   ?  230  PRO A HB2  1 
ATOM   109   H  HB3  . PRO A 1 7   ? -1.579  6.262   18.756  1.00 8.29   ?  230  PRO A HB3  1 
ATOM   110   H  HG2  . PRO A 1 7   ? -0.036  5.439   20.562  1.00 8.38   ?  230  PRO A HG2  1 
ATOM   111   H  HG3  . PRO A 1 7   ? -1.221  6.401   21.004  1.00 8.38   ?  230  PRO A HG3  1 
ATOM   112   H  HD2  . PRO A 1 7   ? -1.122  3.598   21.264  1.00 8.38   ?  230  PRO A HD2  1 
ATOM   113   H  HD3  . PRO A 1 7   ? -1.669  4.639   22.332  1.00 8.38   ?  230  PRO A HD3  1 
ATOM   114   N  N    . ILE A 1 8   ? -4.300  4.807   17.469  1.00 6.80   ?  231  ILE A N    1 
ATOM   115   C  CA   . ILE A 1 8   ? -4.838  4.095   16.315  1.00 7.64   ?  231  ILE A CA   1 
ATOM   116   C  C    . ILE A 1 8   ? -3.897  4.152   15.118  1.00 8.31   ?  231  ILE A C    1 
ATOM   117   O  O    . ILE A 1 8   ? -4.225  3.665   14.038  1.00 9.37   ?  231  ILE A O    1 
ATOM   118   C  CB   . ILE A 1 8   ? -6.253  4.596   15.953  1.00 9.14   ?  231  ILE A CB   1 
ATOM   119   C  CG1  . ILE A 1 8   ? -6.254  6.049   15.487  1.00 10.17  ?  231  ILE A CG1  1 
ATOM   120   C  CG2  . ILE A 1 8   ? -7.188  4.406   17.141  1.00 10.28  ?  231  ILE A CG2  1 
ATOM   121   C  CD1  . ILE A 1 8   ? -7.607  6.499   14.932  1.00 11.41  ?  231  ILE A CD1  1 
ATOM   122   H  H    . ILE A 1 8   ? -4.454  5.653   17.468  1.00 8.17   ?  231  ILE A H    1 
ATOM   123   H  HA   . ILE A 1 8   ? -4.896  3.159   16.561  1.00 9.17   ?  231  ILE A HA   1 
ATOM   124   H  HB   . ILE A 1 8   ? -6.569  4.064   15.206  1.00 10.97  ?  231  ILE A HB   1 
ATOM   125   H  HG12 . ILE A 1 8   ? -6.034  6.621   16.239  1.00 12.21  ?  231  ILE A HG12 1 
ATOM   126   H  HG13 . ILE A 1 8   ? -5.593  6.155   14.785  1.00 12.21  ?  231  ILE A HG13 1 
ATOM   127   H  HG21 . ILE A 1 8   ? -8.100  4.579   16.857  1.00 12.34  ?  231  ILE A HG21 1 
ATOM   128   H  HG22 . ILE A 1 8   ? -7.110  3.494   17.462  1.00 12.34  ?  231  ILE A HG22 1 
ATOM   129   H  HG23 . ILE A 1 8   ? -6.937  5.027   17.843  1.00 12.34  ?  231  ILE A HG23 1 
ATOM   130   H  HD11 . ILE A 1 8   ? -7.511  7.384   14.546  1.00 13.70  ?  231  ILE A HD11 1 
ATOM   131   H  HD12 . ILE A 1 8   ? -7.893  5.870   14.250  1.00 13.70  ?  231  ILE A HD12 1 
ATOM   132   H  HD13 . ILE A 1 8   ? -8.253  6.521   15.654  1.00 13.70  ?  231  ILE A HD13 1 
ATOM   133   N  N    . LEU A 1 9   ? -2.707  4.703   15.304  1.00 7.59   ?  232  LEU A N    1 
ATOM   134   C  CA   . LEU A 1 9   ? -1.730  4.766   14.226  1.00 7.06   ?  232  LEU A CA   1 
ATOM   135   C  C    . LEU A 1 9   ? -1.335  3.365   13.752  1.00 7.33   ?  232  LEU A C    1 
ATOM   136   O  O    . LEU A 1 9   ? -1.156  2.446   14.550  1.00 7.87   ?  232  LEU A O    1 
ATOM   137   C  CB   . LEU A 1 9   ? -0.483  5.505   14.734  1.00 7.00   ?  232  LEU A CB   1 
ATOM   138   C  CG   . LEU A 1 9   ? -0.674  6.955   15.169  1.00 7.82   ?  232  LEU A CG   1 
ATOM   139   C  CD1  . LEU A 1 9   ? 0.603   7.494   15.792  1.00 9.13   ?  232  LEU A CD1  1 
ATOM   140   C  CD2  . LEU A 1 9   ? -1.089  7.836   14.010  1.00 9.58   ?  232  LEU A CD2  1 
ATOM   141   H  H    . LEU A 1 9   ? -2.439  5.048   16.044  1.00 9.11   ?  232  LEU A H    1 
ATOM   142   H  HA   . LEU A 1 9   ? -2.110  5.238   13.468  1.00 8.47   ?  232  LEU A HA   1 
ATOM   143   H  HB2  . LEU A 1 9   ? -0.140  5.021   15.501  1.00 8.40   ?  232  LEU A HB2  1 
ATOM   144   H  HB3  . LEU A 1 9   ? 0.175   5.507   14.021  1.00 8.40   ?  232  LEU A HB3  1 
ATOM   145   H  HG   . LEU A 1 9   ? -1.384  6.979   15.830  1.00 9.38   ?  232  LEU A HG   1 
ATOM   146   H  HD11 . LEU A 1 9   ? 0.452   8.408   16.080  1.00 10.96  ?  232  LEU A HD11 1 
ATOM   147   H  HD12 . LEU A 1 9   ? 0.840   6.942   16.553  1.00 10.96  ?  232  LEU A HD12 1 
ATOM   148   H  HD13 . LEU A 1 9   ? 1.312   7.468   15.131  1.00 10.96  ?  232  LEU A HD13 1 
ATOM   149   H  HD21 . LEU A 1 9   ? -1.149  8.754   14.317  1.00 11.50  ?  232  LEU A HD21 1 
ATOM   150   H  HD22 . LEU A 1 9   ? -0.424  7.766   13.306  1.00 11.50  ?  232  LEU A HD22 1 
ATOM   151   H  HD23 . LEU A 1 9   ? -1.952  7.539   13.681  1.00 11.50  ?  232  LEU A HD23 1 
ATOM   152   N  N    . THR A 1 10  ? -1.152  3.219   12.441  1.00 7.53   ?  233  THR A N    1 
ATOM   153   C  CA   . THR A 1 10  ? -0.665  1.978   11.871  1.00 9.20   ?  233  THR A CA   1 
ATOM   154   C  C    . THR A 1 10  ? 0.835   1.856   12.110  1.00 9.74   ?  233  THR A C    1 
ATOM   155   O  O    . THR A 1 10  ? 1.511   2.811   12.503  1.00 8.61   ?  233  THR A O    1 
ATOM   156   C  CB   . THR A 1 10  ? -0.909  1.945   10.365  1.00 10.19  ?  233  THR A CB   1 
ATOM   157   O  OG1  . THR A 1 10  ? -0.118  2.963   9.770   1.00 10.72  ?  233  THR A OG1  1 
ATOM   158   C  CG2  . THR A 1 10  ? -2.372  2.161   10.031  1.00 11.06  ?  233  THR A CG2  1 
ATOM   159   H  H    . THR A 1 10  ? -1.307  3.833   11.859  1.00 9.04   ?  233  THR A H    1 
ATOM   160   H  HA   . THR A 1 10  ? -1.135  1.239   12.288  1.00 11.04  ?  233  THR A HA   1 
ATOM   161   H  HB   . THR A 1 10  ? -0.667  1.076   10.008  1.00 12.23  ?  233  THR A HB   1 
ATOM   162   H  HG1  . THR A 1 10  ? -0.211  2.947   8.935   1.00 12.86  ?  233  THR A HG1  1 
ATOM   163   H  HG21 . THR A 1 10  ? -2.511  2.074   9.075   1.00 13.27  ?  233  THR A HG21 1 
ATOM   164   H  HG22 . THR A 1 10  ? -2.918  1.502   10.489  1.00 13.27  ?  233  THR A HG22 1 
ATOM   165   H  HG23 . THR A 1 10  ? -2.649  3.048   10.310  1.00 13.27  ?  233  THR A HG23 1 
ATOM   166   N  N    . ILE A 1 11  ? 1.353   0.651   11.857  1.00 11.11  ?  234  ILE A N    1 
ATOM   167   C  CA   . ILE A 1 11  ? 2.787   0.397   11.910  1.00 14.77  ?  234  ILE A CA   1 
ATOM   168   C  C    . ILE A 1 11  ? 3.529   1.390   11.044  1.00 14.40  ?  234  ILE A C    1 
ATOM   169   O  O    . ILE A 1 11  ? 4.571   1.924   11.443  1.00 14.82  ?  234  ILE A O    1 
ATOM   170   C  CB   . ILE A 1 11  ? 3.053   -1.054  11.451  1.00 18.76  ?  234  ILE A CB   1 
ATOM   171   C  CG1  . ILE A 1 11  ? 2.437   -2.050  12.436  1.00 19.80  ?  234  ILE A CG1  1 
ATOM   172   C  CG2  . ILE A 1 11  ? 4.526   -1.311  11.252  1.00 21.42  ?  234  ILE A CG2  1 
ATOM   173   C  CD1  . ILE A 1 11  ? 2.919   -1.877  13.836  1.00 19.50  ?  234  ILE A CD1  1 
ATOM   174   H  H    . ILE A 1 11  ? 0.888   -0.043  11.651  1.00 13.34  ?  234  ILE A H    1 
ATOM   175   H  HA   . ILE A 1 11  ? 3.101   0.505   12.821  1.00 17.72  ?  234  ILE A HA   1 
ATOM   176   H  HB   . ILE A 1 11  ? 2.624   -1.176  10.590  1.00 22.52  ?  234  ILE A HB   1 
ATOM   177   H  HG12 . ILE A 1 11  ? 1.474   -1.934  12.438  1.00 23.76  ?  234  ILE A HG12 1 
ATOM   178   H  HG13 . ILE A 1 11  ? 2.662   -2.950  12.153  1.00 23.76  ?  234  ILE A HG13 1 
ATOM   179   H  HG21 . ILE A 1 11  ? 4.690   -2.265  11.305  1.00 25.70  ?  234  ILE A HG21 1 
ATOM   180   H  HG22 . ILE A 1 11  ? 4.790   -0.977  10.380  1.00 25.70  ?  234  ILE A HG22 1 
ATOM   181   H  HG23 . ILE A 1 11  ? 5.023   -0.851  11.947  1.00 25.70  ?  234  ILE A HG23 1 
ATOM   182   H  HD11 . ILE A 1 11  ? 2.711   -2.677  14.343  1.00 23.40  ?  234  ILE A HD11 1 
ATOM   183   H  HD12 . ILE A 1 11  ? 3.879   -1.734  13.823  1.00 23.40  ?  234  ILE A HD12 1 
ATOM   184   H  HD13 . ILE A 1 11  ? 2.475   -1.110  14.230  1.00 23.40  ?  234  ILE A HD13 1 
ATOM   185   N  N    . GLY A 1 12  ? 2.997   1.670   9.837   1.00 14.79  ?  235  GLY A N    1 
ATOM   186   C  CA   . GLY A 1 12  ? 3.575   2.612   8.891   1.00 15.52  ?  235  GLY A CA   1 
ATOM   187   C  C    . GLY A 1 12  ? 3.331   4.061   9.234   1.00 14.36  ?  235  GLY A C    1 
ATOM   188   O  O    . GLY A 1 12  ? 3.595   4.974   8.438   1.00 17.00  ?  235  GLY A O    1 
ATOM   189   H  H    . GLY A 1 12  ? 2.275   1.307   9.544   1.00 17.75  ?  235  GLY A H    1 
ATOM   190   H  HA2  . GLY A 1 12  ? 4.534   2.471   8.855   1.00 18.63  ?  235  GLY A HA2  1 
ATOM   191   H  HA3  . GLY A 1 12  ? 3.198   2.446   8.013   1.00 18.63  ?  235  GLY A HA3  1 
ATOM   192   N  N    . GLU A 1 13  ? 2.811   4.311   10.435  1.00 10.85  ?  236  GLU A N    1 
ATOM   193   C  CA   . GLU A 1 13  ? 2.660   5.655   10.963  1.00 9.60   ?  236  GLU A CA   1 
ATOM   194   C  C    . GLU A 1 13  ? 3.395   5.829   12.280  1.00 8.51   ?  236  GLU A C    1 
ATOM   195   O  O    . GLU A 1 13  ? 3.192   6.849   12.941  1.00 9.57   ?  236  GLU A O    1 
ATOM   196   C  CB   . GLU A 1 13  ? 1.179   6.004   11.113  1.00 9.21   ?  236  GLU A CB   1 
ATOM   197   C  CG   . GLU A 1 13  ? 0.453   6.084   9.769   1.00 9.38   ?  236  GLU A CG   1 
ATOM   198   C  CD   . GLU A 1 13  ? -1.079  6.120   9.856   1.00 9.76   ?  236  GLU A CD   1 
ATOM   199   O  OE1  . GLU A 1 13  ? -1.649  5.762   10.916  1.00 10.01  ?  236  GLU A OE1  1 
ATOM   200   O  OE2  . GLU A 1 13  ? -1.724  6.507   8.843   1.00 11.06  -1 236  GLU A OE2  1 
ATOM   201   H  H    . GLU A 1 13  ? 2.532   3.699   10.972  1.00 13.02  ?  236  GLU A H    1 
ATOM   202   H  HA   . GLU A 1 13  ? 3.036   6.290   10.334  1.00 11.52  ?  236  GLU A HA   1 
ATOM   203   H  HB2  . GLU A 1 13  ? 0.746   5.320   11.649  1.00 11.06  ?  236  GLU A HB2  1 
ATOM   204   H  HB3  . GLU A 1 13  ? 1.100   6.866   11.550  1.00 11.06  ?  236  GLU A HB3  1 
ATOM   205   H  HG2  . GLU A 1 13  ? 0.736   6.894   9.316   1.00 11.26  ?  236  GLU A HG2  1 
ATOM   206   H  HG3  . GLU A 1 13  ? 0.695   5.307   9.243   1.00 11.26  ?  236  GLU A HG3  1 
ATOM   207   N  N    . MET A 1 14  ? 4.261   4.889   12.651  1.00 7.61   ?  237  MET A N    1 
ATOM   208   C  CA   . MET A 1 14  ? 4.908   4.898   13.954  1.00 7.19   ?  237  MET A CA   1 
ATOM   209   C  C    . MET A 1 14  ? 6.403   4.641   13.838  1.00 7.81   ?  237  MET A C    1 
ATOM   210   O  O    . MET A 1 14  ? 6.902   4.153   12.813  1.00 8.89   ?  237  MET A O    1 
ATOM   211   C  CB   . MET A 1 14  ? 4.245   3.880   14.904  1.00 6.59   ?  237  MET A CB   1 
ATOM   212   C  CG   . MET A 1 14  ? 2.826   4.271   15.280  1.00 6.83   ?  237  MET A CG   1 
ATOM   213   S  SD   . MET A 1 14  ? 2.112   3.309   16.635  1.00 7.42   ?  237  MET A SD   1 
ATOM   214   C  CE   . MET A 1 14  ? 1.930   1.708   15.846  1.00 7.72   ?  237  MET A CE   1 
ATOM   215   H  H    . MET A 1 14  ? 4.492   4.226   12.155  1.00 9.13   ?  237  MET A H    1 
ATOM   216   H  HA   . MET A 1 14  ? 4.808   5.786   14.331  1.00 8.63   ?  237  MET A HA   1 
ATOM   217   H  HB2  . MET A 1 14  ? 4.214   3.014   14.468  1.00 7.91   ?  237  MET A HB2  1 
ATOM   218   H  HB3  . MET A 1 14  ? 4.767   3.822   15.720  1.00 7.91   ?  237  MET A HB3  1 
ATOM   219   H  HG2  . MET A 1 14  ? 2.824   5.202   15.551  1.00 8.20   ?  237  MET A HG2  1 
ATOM   220   H  HG3  . MET A 1 14  ? 2.257   4.150   14.504  1.00 8.20   ?  237  MET A HG3  1 
ATOM   221   H  HE1  . MET A 1 14  ? 1.512   1.094   16.470  1.00 9.27   ?  237  MET A HE1  1 
ATOM   222   H  HE2  . MET A 1 14  ? 1.375   1.806   15.056  1.00 9.27   ?  237  MET A HE2  1 
ATOM   223   H  HE3  . MET A 1 14  ? 2.807   1.378   15.595  1.00 9.27   ?  237  MET A HE3  1 
ATOM   224   N  N    . THR A 1 15  ? 7.101   4.933   14.946  1.00 6.96   ?  238  THR A N    1 
ATOM   225   C  CA   A THR A 1 15  ? 8.555   4.936   15.048  0.40 6.81   ?  238  THR A CA   1 
ATOM   226   C  CA   B THR A 1 15  ? 8.544   4.823   14.960  0.60 7.11   ?  238  THR A CA   1 
ATOM   227   C  C    . THR A 1 15  ? 9.003   3.894   16.070  1.00 5.98   ?  238  THR A C    1 
ATOM   228   O  O    . THR A 1 15  ? 8.359   3.728   17.117  1.00 6.99   ?  238  THR A O    1 
ATOM   229   C  CB   A THR A 1 15  ? 9.046   6.322   15.548  0.40 7.12   ?  238  THR A CB   1 
ATOM   230   C  CB   B THR A 1 15  ? 9.227   6.181   15.098  0.60 7.45   ?  238  THR A CB   1 
ATOM   231   O  OG1  A THR A 1 15  ? 8.433   7.379   14.800  0.40 7.62   ?  238  THR A OG1  1 
ATOM   232   O  OG1  B THR A 1 15  ? 8.731   6.827   16.269  0.60 8.26   ?  238  THR A OG1  1 
ATOM   233   C  CG2  A THR A 1 15  ? 10.555  6.455   15.430  0.40 7.73   ?  238  THR A CG2  1 
ATOM   234   C  CG2  B THR A 1 15  ? 8.999   7.037   13.855  0.60 7.81   ?  238  THR A CG2  1 
ATOM   235   H  H    A THR A 1 15  ? 6.726   5.145   15.691  0.40 8.35   ?  238  THR A H    1 
ATOM   236   H  H    B THR A 1 15  ? 6.753   5.194   15.688  0.60 8.35   ?  238  THR A H    1 
ATOM   237   H  HA   A THR A 1 15  ? 8.941   4.727   14.184  0.40 8.17   ?  238  THR A HA   1 
ATOM   238   H  HA   B THR A 1 15  ? 8.828   4.438   14.117  0.60 8.53   ?  238  THR A HA   1 
ATOM   239   H  HB   A THR A 1 15  ? 8.801   6.403   16.483  0.40 8.55   ?  238  THR A HB   1 
ATOM   240   H  HB   B THR A 1 15  ? 10.187  6.070   15.183  0.60 8.95   ?  238  THR A HB   1 
ATOM   241   H  HG1  A THR A 1 15  ? 7.599   7.354   14.898  0.40 9.15   ?  238  THR A HG1  1 
ATOM   242   H  HG1  B THR A 1 15  ? 7.899   6.921   16.215  0.60 9.92   ?  238  THR A HG1  1 
ATOM   243   H  HG21 A THR A 1 15  ? 10.831  7.347   15.693  0.40 9.28   ?  238  THR A HG21 1 
ATOM   244   H  HG21 B THR A 1 15  ? 8.049   7.179   13.720  0.60 9.37   ?  238  THR A HG21 1 
ATOM   245   H  HG22 A THR A 1 15  ? 10.991  5.808   16.006  0.40 9.28   ?  238  THR A HG22 1 
ATOM   246   H  HG22 B THR A 1 15  ? 9.434   7.898   13.961  0.60 9.37   ?  238  THR A HG22 1 
ATOM   247   H  HG23 A THR A 1 15  ? 10.832  6.297   14.514  0.40 9.28   ?  238  THR A HG23 1 
ATOM   248   H  HG23 B THR A 1 15  ? 9.365   6.593   13.075  0.60 9.37   ?  238  THR A HG23 1 
ATOM   249   N  N    . ASN A 1 16  ? 10.127  3.255   15.804  1.00 5.37   ?  239  ASN A N    1 
ATOM   250   C  CA   . ASN A 1 16  ? 10.744  2.391   16.802  1.00 5.00   ?  239  ASN A CA   1 
ATOM   251   C  C    . ASN A 1 16  ? 11.174  3.237   17.997  1.00 5.40   ?  239  ASN A C    1 
ATOM   252   O  O    . ASN A 1 16  ? 11.714  4.326   17.839  1.00 7.05   ?  239  ASN A O    1 
ATOM   253   C  CB   . ASN A 1 16  ? 11.942  1.705   16.145  1.00 5.34   ?  239  ASN A CB   1 
ATOM   254   C  CG   . ASN A 1 16  ? 12.383  0.472   16.882  1.00 5.59   ?  239  ASN A CG   1 
ATOM   255   O  OD1  . ASN A 1 16  ? 12.869  0.543   18.000  1.00 6.07   ?  239  ASN A OD1  1 
ATOM   256   N  ND2  . ASN A 1 16  ? 12.230  -0.682  16.241  1.00 6.59   ?  239  ASN A ND2  1 
ATOM   257   H  H    . ASN A 1 16  ? 10.554  3.302   15.059  1.00 6.44   ?  239  ASN A H    1 
ATOM   258   H  HA   . ASN A 1 16  ? 10.135  1.710   17.128  1.00 6.00   ?  239  ASN A HA   1 
ATOM   259   H  HB2  . ASN A 1 16  ? 11.700  1.445   15.243  1.00 6.41   ?  239  ASN A HB2  1 
ATOM   260   H  HB3  . ASN A 1 16  ? 12.688  2.325   16.124  1.00 6.41   ?  239  ASN A HB3  1 
ATOM   261   H  HD21 . ASN A 1 16  ? 12.467  -1.418  16.619  1.00 7.90   ?  239  ASN A HD21 1 
ATOM   262   H  HD22 . ASN A 1 16  ? 11.894  -0.694  15.450  1.00 7.90   ?  239  ASN A HD22 1 
ATOM   263   N  N    . SER A 1 17  ? 10.930  2.738   19.202  1.00 5.49   ?  240  SER A N    1 
ATOM   264   C  CA   . SER A 1 17  ? 11.289  3.459   20.415  1.00 5.27   ?  240  SER A CA   1 
ATOM   265   C  C    . SER A 1 17  ? 12.725  3.209   20.852  1.00 5.27   ?  240  SER A C    1 
ATOM   266   O  O    . SER A 1 17  ? 13.184  3.812   21.827  1.00 6.00   ?  240  SER A O    1 
ATOM   267   C  CB   . SER A 1 17  ? 10.316  3.138   21.546  1.00 5.58   ?  240  SER A CB   1 
ATOM   268   O  OG   . SER A 1 17  ? 10.307  1.750   21.778  1.00 5.68   ?  240  SER A OG   1 
ATOM   269   H  H    . SER A 1 17  ? 10.555  1.978   19.344  1.00 6.59   ?  240  SER A H    1 
ATOM   270   H  HA   . SER A 1 17  ? 11.204  4.409   20.243  1.00 6.33   ?  240  SER A HA   1 
ATOM   271   H  HB2  . SER A 1 17  ? 10.598  3.597   22.353  1.00 6.70   ?  240  SER A HB2  1 
ATOM   272   H  HB3  . SER A 1 17  ? 9.425   3.427   21.295  1.00 6.70   ?  240  SER A HB3  1 
ATOM   273   H  HG   . SER A 1 17  ? 9.755   1.564   22.383  1.00 6.81   ?  240  SER A HG   1 
ATOM   274   N  N    . ARG A 1 18  ? 13.460  2.363   20.135  1.00 4.95   ?  241  ARG A N    1 
ATOM   275   C  CA   . ARG A 1 18  ? 14.863  2.116   20.421  1.00 5.07   ?  241  ARG A CA   1 
ATOM   276   C  C    . ARG A 1 18  ? 15.797  2.654   19.344  1.00 5.40   ?  241  ARG A C    1 
ATOM   277   O  O    . ARG A 1 18  ? 17.016  2.601   19.526  1.00 5.58   ?  241  ARG A O    1 
ATOM   278   C  CB   . ARG A 1 18  ? 15.103  0.621   20.664  1.00 4.98   ?  241  ARG A CB   1 
ATOM   279   C  CG   . ARG A 1 18  ? 14.417  0.127   21.911  1.00 5.39   ?  241  ARG A CG   1 
ATOM   280   C  CD   . ARG A 1 18  ? 14.654  -1.348  22.142  1.00 5.14   ?  241  ARG A CD   1 
ATOM   281   N  NE   . ARG A 1 18  ? 16.060  -1.581  22.423  1.00 5.26   ?  241  ARG A NE   1 
ATOM   282   C  CZ   . ARG A 1 18  ? 16.738  -2.664  22.079  1.00 5.63   ?  241  ARG A CZ   1 
ATOM   283   N  NH1  . ARG A 1 18  ? 16.142  -3.698  21.510  1.00 6.35   ?  241  ARG A NH1  1 
ATOM   284   N  NH2  . ARG A 1 18  ? 18.057  -2.689  22.278  1.00 6.35   ?  241  ARG A NH2  1 
ATOM   285   H  H    . ARG A 1 18  ? 13.160  1.913   19.466  1.00 5.95   ?  241  ARG A H    1 
ATOM   286   H  HA   . ARG A 1 18  ? 15.107  2.566   21.246  1.00 6.09   ?  241  ARG A HA   1 
ATOM   287   H  HB2  . ARG A 1 18  ? 14.758  0.118   19.909  1.00 5.98   ?  241  ARG A HB2  1 
ATOM   288   H  HB3  . ARG A 1 18  ? 16.055  0.464   20.760  1.00 5.98   ?  241  ARG A HB3  1 
ATOM   289   H  HG2  . ARG A 1 18  ? 14.759  0.612   22.678  1.00 6.48   ?  241  ARG A HG2  1 
ATOM   290   H  HG3  . ARG A 1 18  ? 13.461  0.270   21.828  1.00 6.48   ?  241  ARG A HG3  1 
ATOM   291   H  HD2  . ARG A 1 18  ? 14.130  -1.649  22.901  1.00 6.17   ?  241  ARG A HD2  1 
ATOM   292   H  HD3  . ARG A 1 18  ? 14.407  -1.848  21.348  1.00 6.17   ?  241  ARG A HD3  1 
ATOM   293   H  HE   . ARG A 1 18  ? 16.486  -0.966  22.846  1.00 6.31   ?  241  ARG A HE   1 
ATOM   294   H  HH11 . ARG A 1 18  ? 15.296  -3.676  21.355  1.00 7.62   ?  241  ARG A HH11 1 
ATOM   295   H  HH12 . ARG A 1 18  ? 16.600  -4.393  21.294  1.00 7.62   ?  241  ARG A HH12 1 
ATOM   296   H  HH21 . ARG A 1 18  ? 18.452  -2.008  22.624  1.00 7.62   ?  241  ARG A HH21 1 
ATOM   297   H  HH22 . ARG A 1 18  ? 18.511  -3.386  22.060  1.00 7.62   ?  241  ARG A HH22 1 
ATOM   298   N  N    . PHE A 1 19  ? 15.266  3.185   18.234  1.00 5.54   ?  242  PHE A N    1 
ATOM   299   C  CA   . PHE A 1 19  ? 16.110  3.746   17.181  1.00 5.71   ?  242  PHE A CA   1 
ATOM   300   C  C    . PHE A 1 19  ? 15.201  4.583   16.299  1.00 6.07   ?  242  PHE A C    1 
ATOM   301   O  O    . PHE A 1 19  ? 14.078  4.142   16.023  1.00 6.49   ?  242  PHE A O    1 
ATOM   302   C  CB   . PHE A 1 19  ? 16.805  2.659   16.345  1.00 6.12   ?  242  PHE A CB   1 
ATOM   303   C  CG   . PHE A 1 19  ? 17.997  3.172   15.615  1.00 6.41   ?  242  PHE A CG   1 
ATOM   304   C  CD1  . PHE A 1 19  ? 19.216  3.221   16.234  1.00 7.86   ?  242  PHE A CD1  1 
ATOM   305   C  CD2  . PHE A 1 19  ? 17.890  3.650   14.318  1.00 7.88   ?  242  PHE A CD2  1 
ATOM   306   C  CE1  . PHE A 1 19  ? 20.321  3.737   15.583  1.00 9.26   ?  242  PHE A CE1  1 
ATOM   307   C  CE2  . PHE A 1 19  ? 18.986  4.173   13.668  1.00 9.94   ?  242  PHE A CE2  1 
ATOM   308   C  CZ   . PHE A 1 19  ? 20.202  4.218   14.298  1.00 9.79   ?  242  PHE A CZ   1 
ATOM   309   H  H    . PHE A 1 19  ? 14.422  3.231   18.072  1.00 6.65   ?  242  PHE A H    1 
ATOM   310   H  HA   . PHE A 1 19  ? 16.806  4.298   17.570  1.00 6.85   ?  242  PHE A HA   1 
ATOM   311   H  HB2  . PHE A 1 19  ? 17.096  1.946   16.933  1.00 7.35   ?  242  PHE A HB2  1 
ATOM   312   H  HB3  . PHE A 1 19  ? 16.177  2.314   15.691  1.00 7.35   ?  242  PHE A HB3  1 
ATOM   313   H  HD1  . PHE A 1 19  ? 19.302  2.903   17.103  1.00 9.43   ?  242  PHE A HD1  1 
ATOM   314   H  HD2  . PHE A 1 19  ? 17.069  3.616   13.882  1.00 9.46   ?  242  PHE A HD2  1 
ATOM   315   H  HE1  . PHE A 1 19  ? 21.145  3.759   16.014  1.00 11.11  ?  242  PHE A HE1  1 
ATOM   316   H  HE2  . PHE A 1 19  ? 18.900  4.497   12.800  1.00 11.93  ?  242  PHE A HE2  1 
ATOM   317   H  HZ   . PHE A 1 19  ? 20.943  4.571   13.861  1.00 11.75  ?  242  PHE A HZ   1 
ATOM   318   N  N    . PRO A 1 20  ? 15.623  5.776   15.852  1.00 6.57   ?  243  PRO A N    1 
ATOM   319   C  CA   . PRO A 1 20  ? 14.672  6.696   15.193  1.00 7.55   ?  243  PRO A CA   1 
ATOM   320   C  C    . PRO A 1 20  ? 14.400  6.377   13.729  1.00 7.22   ?  243  PRO A C    1 
ATOM   321   O  O    . PRO A 1 20  ? 14.799  7.105   12.808  1.00 8.80   ?  243  PRO A O    1 
ATOM   322   C  CB   . PRO A 1 20  ? 15.355  8.053   15.394  1.00 8.11   ?  243  PRO A CB   1 
ATOM   323   C  CG   . PRO A 1 20  ? 16.802  7.745   15.392  1.00 8.23   ?  243  PRO A CG   1 
ATOM   324   C  CD   . PRO A 1 20  ? 16.894  6.460   16.177  1.00 6.69   ?  243  PRO A CD   1 
ATOM   325   H  HA   . PRO A 1 20  ? 13.826  6.670   15.667  1.00 9.07   ?  243  PRO A HA   1 
ATOM   326   H  HB2  . PRO A 1 20  ? 15.124  8.652   14.666  1.00 9.74   ?  243  PRO A HB2  1 
ATOM   327   H  HB3  . PRO A 1 20  ? 15.082  8.440   16.241  1.00 9.74   ?  243  PRO A HB3  1 
ATOM   328   H  HG2  . PRO A 1 20  ? 17.119  7.625   14.483  1.00 9.88   ?  243  PRO A HG2  1 
ATOM   329   H  HG3  . PRO A 1 20  ? 17.298  8.457   15.825  1.00 9.88   ?  243  PRO A HG3  1 
ATOM   330   H  HD2  . PRO A 1 20  ? 17.654  5.931   15.888  1.00 8.03   ?  243  PRO A HD2  1 
ATOM   331   H  HD3  . PRO A 1 20  ? 16.957  6.639   17.128  1.00 8.03   ?  243  PRO A HD3  1 
ATOM   332   N  N    . VAL A 1 21  ? 13.676  5.286   13.513  1.00 6.73   ?  244  VAL A N    1 
ATOM   333   C  CA   . VAL A 1 21  ? 13.279  4.842   12.177  1.00 6.63   ?  244  VAL A CA   1 
ATOM   334   C  C    . VAL A 1 21  ? 11.863  4.311   12.245  1.00 6.31   ?  244  VAL A C    1 
ATOM   335   O  O    . VAL A 1 21  ? 11.366  3.942   13.319  1.00 6.07   ?  244  VAL A O    1 
ATOM   336   C  CB   . VAL A 1 21  ? 14.217  3.744   11.620  1.00 7.81   ?  244  VAL A CB   1 
ATOM   337   C  CG1  . VAL A 1 21  ? 15.581  4.312   11.322  1.00 9.19   ?  244  VAL A CG1  1 
ATOM   338   C  CG2  . VAL A 1 21  ? 14.334  2.577   12.604  1.00 7.84   ?  244  VAL A CG2  1 
ATOM   339   H  H    . VAL A 1 21  ? 13.393  4.769   14.139  1.00 8.08   ?  244  VAL A H    1 
ATOM   340   H  HA   . VAL A 1 21  ? 13.305  5.599   11.570  1.00 7.96   ?  244  VAL A HA   1 
ATOM   341   H  HB   . VAL A 1 21  ? 13.837  3.406   10.794  1.00 9.37   ?  244  VAL A HB   1 
ATOM   342   H  HG11 . VAL A 1 21  ? 16.141  3.612   10.951  1.00 11.03  ?  244  VAL A HG11 1 
ATOM   343   H  HG12 . VAL A 1 21  ? 15.489  5.036   10.683  1.00 11.03  ?  244  VAL A HG12 1 
ATOM   344   H  HG13 . VAL A 1 21  ? 15.971  4.646   12.146  1.00 11.03  ?  244  VAL A HG13 1 
ATOM   345   H  HG21 . VAL A 1 21  ? 14.951  1.921   12.244  1.00 9.41   ?  244  VAL A HG21 1 
ATOM   346   H  HG22 . VAL A 1 21  ? 14.664  2.912   13.453  1.00 9.41   ?  244  VAL A HG22 1 
ATOM   347   H  HG23 . VAL A 1 21  ? 13.458  2.177   12.724  1.00 9.41   ?  244  VAL A HG23 1 
ATOM   348   N  N    . PRO A 1 22  ? 11.180  4.239   11.102  1.00 6.93   ?  245  PRO A N    1 
ATOM   349   C  CA   . PRO A 1 22  ? 9.847   3.633   11.072  1.00 6.73   ?  245  PRO A CA   1 
ATOM   350   C  C    . PRO A 1 22  ? 9.889   2.184   11.532  1.00 6.55   ?  245  PRO A C    1 
ATOM   351   O  O    . PRO A 1 22  ? 10.902  1.495   11.403  1.00 6.74   ?  245  PRO A O    1 
ATOM   352   C  CB   . PRO A 1 22  ? 9.456   3.718   9.592   1.00 7.83   ?  245  PRO A CB   1 
ATOM   353   C  CG   . PRO A 1 22  ? 10.275  4.820   9.045   1.00 8.38   ?  245  PRO A CG   1 
ATOM   354   C  CD   . PRO A 1 22  ? 11.582  4.732   9.774   1.00 7.73   ?  245  PRO A CD   1 
ATOM   355   H  HA   . PRO A 1 22  ? 9.225   4.140   11.617  1.00 8.08   ?  245  PRO A HA   1 
ATOM   356   H  HB2  . PRO A 1 22  ? 9.660   2.880   9.147   1.00 9.40   ?  245  PRO A HB2  1 
ATOM   357   H  HB3  . PRO A 1 22  ? 8.509   3.914   9.510   1.00 9.40   ?  245  PRO A HB3  1 
ATOM   358   H  HG2  . PRO A 1 22  ? 10.401  4.697   8.091   1.00 10.06  ?  245  PRO A HG2  1 
ATOM   359   H  HG3  . PRO A 1 22  ? 9.840   5.671   9.214   1.00 10.06  ?  245  PRO A HG3  1 
ATOM   360   H  HD2  . PRO A 1 22  ? 12.181  4.105   9.339   1.00 9.28   ?  245  PRO A HD2  1 
ATOM   361   H  HD3  . PRO A 1 22  ? 12.003  5.603   9.840   1.00 9.28   ?  245  PRO A HD3  1 
ATOM   362   N  N    . ILE A 1 23  ? 8.759   1.718   12.059  1.00 7.33   ?  246  ILE A N    1 
ATOM   363   C  CA   . ILE A 1 23  ? 8.604   0.295   12.345  1.00 7.16   ?  246  ILE A CA   1 
ATOM   364   C  C    . ILE A 1 23  ? 8.391   -0.447  11.030  1.00 7.83   ?  246  ILE A C    1 
ATOM   365   O  O    . ILE A 1 23  ? 7.564   -0.048  10.208  1.00 9.47   ?  246  ILE A O    1 
ATOM   366   C  CB   . ILE A 1 23  ? 7.428   0.076   13.315  1.00 7.96   ?  246  ILE A CB   1 
ATOM   367   C  CG1  . ILE A 1 23  ? 7.736   0.766   14.646  1.00 10.99  ?  246  ILE A CG1  1 
ATOM   368   C  CG2  . ILE A 1 23  ? 7.176   -1.426  13.514  1.00 7.65   ?  246  ILE A CG2  1 
ATOM   369   C  CD1  . ILE A 1 23  ? 6.616   0.830   15.614  1.00 11.94  ?  246  ILE A CD1  1 
ATOM   370   H  H    . ILE A 1 23  ? 8.075   2.200   12.257  1.00 8.80   ?  246  ILE A H    1 
ATOM   371   H  HA   . ILE A 1 23  ? 9.408   -0.047  12.764  1.00 8.59   ?  246  ILE A HA   1 
ATOM   372   H  HB   . ILE A 1 23  ? 6.623   0.466   12.940  1.00 9.55   ?  246  ILE A HB   1 
ATOM   373   H  HG12 . ILE A 1 23  ? 8.461   0.286   15.076  1.00 13.19  ?  246  ILE A HG12 1 
ATOM   374   H  HG13 . ILE A 1 23  ? 8.007   1.678   14.459  1.00 13.19  ?  246  ILE A HG13 1 
ATOM   375   H  HG21 . ILE A 1 23  ? 6.480   -1.544  14.180  1.00 9.19   ?  246  ILE A HG21 1 
ATOM   376   H  HG22 . ILE A 1 23  ? 6.895   -1.814  12.671  1.00 9.19   ?  246  ILE A HG22 1 
ATOM   377   H  HG23 . ILE A 1 23  ? 7.996   -1.847  13.815  1.00 9.19   ?  246  ILE A HG23 1 
ATOM   378   H  HD11 . ILE A 1 23  ? 6.896   1.346   16.387  1.00 14.33  ?  246  ILE A HD11 1 
ATOM   379   H  HD12 . ILE A 1 23  ? 5.855   1.257   15.190  1.00 14.33  ?  246  ILE A HD12 1 
ATOM   380   H  HD13 . ILE A 1 23  ? 6.381   -0.071  15.886  1.00 14.33  ?  246  ILE A HD13 1 
ATOM   381   N  N    . ASP A 1 24  ? 9.108   -1.556  10.830  1.00 6.61   ?  247  ASP A N    1 
ATOM   382   C  CA   . ASP A 1 24  ? 8.954   -2.377  9.635   1.00 7.18   ?  247  ASP A CA   1 
ATOM   383   C  C    . ASP A 1 24  ? 7.905   -3.473  9.794   1.00 7.85   ?  247  ASP A C    1 
ATOM   384   O  O    . ASP A 1 24  ? 7.161   -3.736  8.844   1.00 9.51   ?  247  ASP A O    1 
ATOM   385   C  CB   . ASP A 1 24  ? 10.302  -2.970  9.220   1.00 8.52   ?  247  ASP A CB   1 
ATOM   386   C  CG   . ASP A 1 24  ? 11.236  -1.922  8.674   1.00 10.15  ?  247  ASP A CG   1 
ATOM   387   O  OD1  . ASP A 1 24  ? 10.892  -1.280  7.668   1.00 14.85  ?  247  ASP A OD1  1 
ATOM   388   O  OD2  . ASP A 1 24  ? 12.285  -1.683  9.263   1.00 8.93   -1 247  ASP A OD2  1 
ATOM   389   H  H    . ASP A 1 24  ? 9.696   -1.856  11.382  1.00 7.94   ?  247  ASP A H    1 
ATOM   390   H  HA   . ASP A 1 24  ? 8.655   -1.807  8.909   1.00 8.62   ?  247  ASP A HA   1 
ATOM   391   H  HB2  . ASP A 1 24  ? 10.722  -3.378  9.993   1.00 10.23  ?  247  ASP A HB2  1 
ATOM   392   H  HB3  . ASP A 1 24  ? 10.158  -3.637  8.530   1.00 10.23  ?  247  ASP A HB3  1 
ATOM   393   N  N    . MET A 1 25  ? 7.844   -4.151  10.934  1.00 7.24   ?  248  MET A N    1 
ATOM   394   C  CA   . MET A 1 25  ? 6.952   -5.305  11.057  1.00 7.41   ?  248  MET A CA   1 
ATOM   395   C  C    . MET A 1 25  ? 6.798   -5.667  12.527  1.00 7.05   ?  248  MET A C    1 
ATOM   396   O  O    . MET A 1 25  ? 7.624   -5.297  13.356  1.00 7.79   ?  248  MET A O    1 
ATOM   397   C  CB   . MET A 1 25  ? 7.514   -6.514  10.290  1.00 9.29   ?  248  MET A CB   1 
ATOM   398   C  CG   . MET A 1 25  ? 8.889   -6.971  10.818  1.00 13.02  ?  248  MET A CG   1 
ATOM   399   S  SD   . MET A 1 25  ? 9.956   -7.888  9.676   1.00 19.03  ?  248  MET A SD   1 
ATOM   400   C  CE   . MET A 1 25  ? 8.868   -9.211  9.195   1.00 21.09  ?  248  MET A CE   1 
ATOM   401   H  H    . MET A 1 25  ? 8.300   -3.968  11.640  1.00 8.69   ?  248  MET A H    1 
ATOM   402   H  HA   . MET A 1 25  ? 6.084   -5.066  10.698  1.00 8.89   ?  248  MET A HA   1 
ATOM   403   H  HB2  . MET A 1 25  ? 6.897   -7.257  10.377  1.00 11.15  ?  248  MET A HB2  1 
ATOM   404   H  HB3  . MET A 1 25  ? 7.616   -6.274  9.355   1.00 11.15  ?  248  MET A HB3  1 
ATOM   405   H  HG2  . MET A 1 25  ? 9.383   -6.181  11.088  1.00 15.62  ?  248  MET A HG2  1 
ATOM   406   H  HG3  . MET A 1 25  ? 8.738   -7.546  11.584  1.00 15.62  ?  248  MET A HG3  1 
ATOM   407   H  HE1  . MET A 1 25  ? 9.336   -9.797  8.580   1.00 25.31  ?  248  MET A HE1  1 
ATOM   408   H  HE2  . MET A 1 25  ? 8.603   -9.706  9.987   1.00 25.31  ?  248  MET A HE2  1 
ATOM   409   H  HE3  . MET A 1 25  ? 8.085   -8.835  8.763   1.00 25.31  ?  248  MET A HE3  1 
ATOM   410   N  N    . LEU A 1 26  ? 5.747   -6.418  12.825  1.00 7.38   ?  249  LEU A N    1 
ATOM   411   C  CA   . LEU A 1 26  ? 5.641   -7.135  14.084  1.00 7.52   ?  249  LEU A CA   1 
ATOM   412   C  C    . LEU A 1 26  ? 6.551   -8.356  14.051  1.00 7.51   ?  249  LEU A C    1 
ATOM   413   O  O    . LEU A 1 26  ? 6.843   -8.899  12.987  1.00 9.24   ?  249  LEU A O    1 
ATOM   414   C  CB   . LEU A 1 26  ? 4.207   -7.607  14.288  1.00 8.07   ?  249  LEU A CB   1 
ATOM   415   C  CG   . LEU A 1 26  ? 3.138   -6.534  14.394  1.00 9.15   ?  249  LEU A CG   1 
ATOM   416   C  CD1  . LEU A 1 26  ? 1.771   -7.188  14.541  1.00 9.65   ?  249  LEU A CD1  1 
ATOM   417   C  CD2  . LEU A 1 26  ? 3.387   -5.582  15.549  1.00 10.91  ?  249  LEU A CD2  1 
ATOM   418   H  H    . LEU A 1 26  ? 5.070   -6.530  12.306  1.00 8.86   ?  249  LEU A H    1 
ATOM   419   H  HA   . LEU A 1 26  ? 5.895   -6.558  14.820  1.00 9.03   ?  249  LEU A HA   1 
ATOM   420   H  HB2  . LEU A 1 26  ? 3.968   -8.172  13.536  1.00 9.69   ?  249  LEU A HB2  1 
ATOM   421   H  HB3  . LEU A 1 26  ? 4.176   -8.120  15.111  1.00 9.69   ?  249  LEU A HB3  1 
ATOM   422   H  HG   . LEU A 1 26  ? 3.162   -6.003  13.583  1.00 10.98  ?  249  LEU A HG   1 
ATOM   423   H  HD11 . LEU A 1 26  ? 1.098   -6.495  14.638  1.00 11.58  ?  249  LEU A HD11 1 
ATOM   424   H  HD12 . LEU A 1 26  ? 1.587   -7.718  13.750  1.00 11.58  ?  249  LEU A HD12 1 
ATOM   425   H  HD13 . LEU A 1 26  ? 1.775   -7.757  15.327  1.00 11.58  ?  249  LEU A HD13 1 
ATOM   426   H  HD21 . LEU A 1 26  ? 2.641   -4.965  15.616  1.00 13.10  ?  249  LEU A HD21 1 
ATOM   427   H  HD22 . LEU A 1 26  ? 3.466   -6.095  16.369  1.00 13.10  ?  249  LEU A HD22 1 
ATOM   428   H  HD23 . LEU A 1 26  ? 4.208   -5.093  15.384  1.00 13.10  ?  249  LEU A HD23 1 
ATOM   429   N  N    . HIS A 1 27  ? 6.989   -8.798  15.230  1.00 6.83   ?  250  HIS A N    1 
ATOM   430   C  CA   . HIS A 1 27  ? 7.853   -9.964  15.342  1.00 7.71   ?  250  HIS A CA   1 
ATOM   431   C  C    . HIS A 1 27  ? 7.561   -10.672 16.656  1.00 6.96   ?  250  HIS A C    1 
ATOM   432   O  O    . HIS A 1 27  ? 7.467   -10.020 17.691  1.00 7.34   ?  250  HIS A O    1 
ATOM   433   C  CB   . HIS A 1 27  ? 9.340   -9.546  15.395  1.00 9.33   ?  250  HIS A CB   1 
ATOM   434   C  CG   . HIS A 1 27  ? 10.253  -10.683 15.735  1.00 10.85  ?  250  HIS A CG   1 
ATOM   435   N  ND1  . HIS A 1 27  ? 10.672  -11.581 14.786  1.00 10.84  ?  250  HIS A ND1  1 
ATOM   436   C  CD2  . HIS A 1 27  ? 10.756  -11.123 16.916  1.00 10.90  ?  250  HIS A CD2  1 
ATOM   437   C  CE1  . HIS A 1 27  ? 11.409  -12.519 15.357  1.00 10.80  ?  250  HIS A CE1  1 
ATOM   438   N  NE2  . HIS A 1 27  ? 11.474  -12.264 16.653  1.00 11.40  ?  250  HIS A NE2  1 
ATOM   439   H  H    . HIS A 1 27  ? 6.796   -8.434  15.984  1.00 8.20   ?  250  HIS A H    1 
ATOM   440   H  HA   . HIS A 1 27  ? 7.680   -10.551 14.589  1.00 9.25   ?  250  HIS A HA   1 
ATOM   441   H  HB2  . HIS A 1 27  ? 9.602   -9.201  14.527  1.00 11.20  ?  250  HIS A HB2  1 
ATOM   442   H  HB3  . HIS A 1 27  ? 9.451   -8.860  16.072  1.00 11.20  ?  250  HIS A HB3  1 
ATOM   443   H  HD1  . HIS A 1 27  ? 10.484  -11.541 13.948  1.00 13.01  ?  250  HIS A HD1  1 
ATOM   444   H  HD2  . HIS A 1 27  ? 10.638  -10.725 17.749  1.00 13.08  ?  250  HIS A HD2  1 
ATOM   445   H  HE1  . HIS A 1 27  ? 11.813  -13.235 14.921  1.00 12.96  ?  250  HIS A HE1  1 
ATOM   446   N  N    . THR A 1 28  ? 7.511   -12.002 16.638  1.00 7.08   ?  251  THR A N    1 
ATOM   447   C  CA   . THR A 1 28  ? 7.534   -12.758 17.887  1.00 7.41   ?  251  THR A CA   1 
ATOM   448   C  C    . THR A 1 28  ? 8.384   -14.006 17.705  1.00 8.32   ?  251  THR A C    1 
ATOM   449   O  O    . THR A 1 28  ? 8.387   -14.616 16.636  1.00 9.84   ?  251  THR A O    1 
ATOM   450   C  CB   . THR A 1 28  ? 6.126   -13.078 18.420  1.00 7.76   ?  251  THR A CB   1 
ATOM   451   O  OG1  . THR A 1 28  ? 6.234   -13.701 19.703  1.00 8.17   ?  251  THR A OG1  1 
ATOM   452   C  CG2  . THR A 1 28  ? 5.330   -13.983 17.506  1.00 8.32   ?  251  THR A CG2  1 
ATOM   453   H  H    . THR A 1 28  ? 7.465   -12.482 15.925  1.00 8.50   ?  251  THR A H    1 
ATOM   454   H  HA   . THR A 1 28  ? 7.957   -12.226 18.579  1.00 8.89   ?  251  THR A HA   1 
ATOM   455   H  HB   . THR A 1 28  ? 5.638   -12.242 18.478  1.00 9.31   ?  251  THR A HB   1 
ATOM   456   H  HG1  . THR A 1 28  ? 6.573   -13.165 20.254  1.00 9.80   ?  251  THR A HG1  1 
ATOM   457   H  HG21 . THR A 1 28  ? 4.429   -14.092 17.849  1.00 9.99   ?  251  THR A HG21 1 
ATOM   458   H  HG22 . THR A 1 28  ? 5.285   -13.600 16.616  1.00 9.99   ?  251  THR A HG22 1 
ATOM   459   H  HG23 . THR A 1 28  ? 5.753   -14.855 17.452  1.00 9.99   ?  251  THR A HG23 1 
ATOM   460   N  N    . SER A 1 29  ? 9.107   -14.367 18.754  1.00 8.87   ?  252  SER A N    1 
ATOM   461   C  CA   . SER A 1 29  ? 9.943   -15.564 18.736  1.00 10.46  ?  252  SER A CA   1 
ATOM   462   C  C    . SER A 1 29  ? 10.229  -15.959 20.176  1.00 11.20  ?  252  SER A C    1 
ATOM   463   O  O    . SER A 1 29  ? 9.995   -15.173 21.104  1.00 10.94  ?  252  SER A O    1 
ATOM   464   C  CB   . SER A 1 29  ? 11.241  -15.322 17.957  1.00 11.65  ?  252  SER A CB   1 
ATOM   465   O  OG   . SER A 1 29  ? 11.988  -14.278 18.537  1.00 13.02  ?  252  SER A OG   1 
ATOM   466   H  H    . SER A 1 29  ? 9.133   -13.933 19.497  1.00 10.65  ?  252  SER A H    1 
ATOM   467   H  HA   . SER A 1 29  ? 9.464   -16.293 18.311  1.00 12.55  ?  252  SER A HA   1 
ATOM   468   H  HB2  . SER A 1 29  ? 11.772  -16.134 17.969  1.00 13.98  ?  252  SER A HB2  1 
ATOM   469   H  HB3  . SER A 1 29  ? 11.021  -15.083 17.043  1.00 13.98  ?  252  SER A HB3  1 
ATOM   470   H  HG   . SER A 1 29  ? 11.502  -13.600 18.641  1.00 15.63  ?  252  SER A HG   1 
ATOM   471   N  N    . PRO A 1 30  ? 10.722  -17.183 20.402  1.00 12.67  ?  253  PRO A N    1 
ATOM   472   C  CA   . PRO A 1 30  ? 11.081  -17.584 21.769  1.00 13.44  ?  253  PRO A CA   1 
ATOM   473   C  C    . PRO A 1 30  ? 12.236  -16.748 22.309  1.00 13.39  ?  253  PRO A C    1 
ATOM   474   O  O    . PRO A 1 30  ? 13.166  -16.405 21.579  1.00 15.74  ?  253  PRO A O    1 
ATOM   475   C  CB   . PRO A 1 30  ? 11.490  -19.057 21.609  1.00 14.66  ?  253  PRO A CB   1 
ATOM   476   C  CG   . PRO A 1 30  ? 10.960  -19.496 20.302  1.00 14.98  ?  253  PRO A CG   1 
ATOM   477   C  CD   . PRO A 1 30  ? 10.882  -18.283 19.433  1.00 13.88  ?  253  PRO A CD   1 
ATOM   478   H  HA   . PRO A 1 30  ? 10.316  -17.512 22.360  1.00 16.13  ?  253  PRO A HA   1 
ATOM   479   H  HB2  . PRO A 1 30  ? 12.457  -19.129 21.629  1.00 17.59  ?  253  PRO A HB2  1 
ATOM   480   H  HB3  . PRO A 1 30  ? 11.104  -19.581 22.329  1.00 17.59  ?  253  PRO A HB3  1 
ATOM   481   H  HG2  . PRO A 1 30  ? 11.560  -20.152 19.915  1.00 17.98  ?  253  PRO A HG2  1 
ATOM   482   H  HG3  . PRO A 1 30  ? 10.079  -19.883 20.425  1.00 17.98  ?  253  PRO A HG3  1 
ATOM   483   H  HD2  . PRO A 1 30  ? 11.696  -18.174 18.918  1.00 16.65  ?  253  PRO A HD2  1 
ATOM   484   H  HD3  . PRO A 1 30  ? 10.117  -18.333 18.839  1.00 16.65  ?  253  PRO A HD3  1 
ATOM   485   N  N    . THR A 1 31  ? 12.180  -16.428 23.609  1.00 13.89  ?  254  THR A N    1 
ATOM   486   C  CA   . THR A 1 31  ? 13.211  -15.610 24.244  1.00 14.56  ?  254  THR A CA   1 
ATOM   487   C  C    . THR A 1 31  ? 13.722  -16.233 25.540  1.00 16.17  ?  254  THR A C    1 
ATOM   488   O  O    . THR A 1 31  ? 14.317  -15.536 26.373  1.00 16.08  ?  254  THR A O    1 
ATOM   489   C  CB   . THR A 1 31  ? 12.713  -14.180 24.500  1.00 15.15  ?  254  THR A CB   1 
ATOM   490   O  OG1  . THR A 1 31  ? 11.505  -14.207 25.273  1.00 16.20  ?  254  THR A OG1  1 
ATOM   491   C  CG2  . THR A 1 31  ? 12.463  -13.453 23.183  1.00 16.42  ?  254  THR A CG2  1 
ATOM   492   H  H    . THR A 1 31  ? 11.552  -16.675 24.141  1.00 16.67  ?  254  THR A H    1 
ATOM   493   H  HA   . THR A 1 31  ? 13.962  -15.550 23.633  1.00 17.47  ?  254  THR A HA   1 
ATOM   494   H  HB   . THR A 1 31  ? 13.390  -13.692 24.994  1.00 18.18  ?  254  THR A HB   1 
ATOM   495   H  HG1  . THR A 1 31  ? 11.239  -13.424 25.417  1.00 19.44  ?  254  THR A HG1  1 
ATOM   496   H  HG21 . THR A 1 31  ? 12.193  -12.537 23.356  1.00 19.70  ?  254  THR A HG21 1 
ATOM   497   H  HG22 . THR A 1 31  ? 13.272  -13.448 22.648  1.00 19.70  ?  254  THR A HG22 1 
ATOM   498   H  HG23 . THR A 1 31  ? 11.760  -13.900 22.686  1.00 19.70  ?  254  THR A HG23 1 
ATOM   499   N  N    . GLU A 1 32  ? 13.515  -17.538 25.713  0.86 17.17  ?  255  GLU A N    1 
ATOM   500   C  CA   . GLU A 1 32  ? 13.862  -18.179 26.976  0.86 19.57  ?  255  GLU A CA   1 
ATOM   501   C  C    . GLU A 1 32  ? 15.337  -18.016 27.304  0.86 19.93  ?  255  GLU A C    1 
ATOM   502   O  O    . GLU A 1 32  ? 15.705  -17.929 28.482  0.86 21.49  ?  255  GLU A O    1 
ATOM   503   C  CB   . GLU A 1 32  ? 13.506  -19.668 26.933  0.86 21.78  ?  255  GLU A CB   1 
ATOM   504   C  CG   . GLU A 1 32  ? 12.022  -19.977 26.757  0.86 95.30  ?  255  GLU A CG   1 
ATOM   505   C  CD   . GLU A 1 32  ? 11.568  -19.909 25.311  0.86 81.34  ?  255  GLU A CD   1 
ATOM   506   O  OE1  . GLU A 1 32  ? 12.435  -19.888 24.412  0.86 29.67  ?  255  GLU A OE1  1 
ATOM   507   O  OE2  . GLU A 1 32  ? 10.342  -19.874 25.073  0.86 64.84  -1 255  GLU A OE2  1 
ATOM   508   H  H    . GLU A 1 32  ? 13.180  -18.066 25.123  0.86 20.61  ?  255  GLU A H    1 
ATOM   509   H  HA   . GLU A 1 32  ? 13.344  -17.760 27.681  0.86 23.48  ?  255  GLU A HA   1 
ATOM   510   H  HB2  . GLU A 1 32  ? 13.977  -20.074 26.188  0.86 26.14  ?  255  GLU A HB2  1 
ATOM   511   H  HB3  . GLU A 1 32  ? 13.790  -20.075 27.766  0.86 26.14  ?  255  GLU A HB3  1 
ATOM   512   H  HG2  . GLU A 1 32  ? 11.847  -20.874 27.083  0.86 114.36 ?  255  GLU A HG2  1 
ATOM   513   H  HG3  . GLU A 1 32  ? 11.504  -19.333 27.264  0.86 114.36 ?  255  GLU A HG3  1 
ATOM   514   N  N    . ASN A 1 33  ? 16.200  -17.970 26.292  0.72 18.78  ?  256  ASN A N    1 
ATOM   515   C  CA   . ASN A 1 33  ? 17.637  -17.932 26.532  0.72 20.60  ?  256  ASN A CA   1 
ATOM   516   C  C    . ASN A 1 33  ? 18.234  -16.543 26.335  0.72 19.60  ?  256  ASN A C    1 
ATOM   517   O  O    . ASN A 1 33  ? 19.457  -16.403 26.238  0.72 20.93  ?  256  ASN A O    1 
ATOM   518   C  CB   . ASN A 1 33  ? 18.338  -18.985 25.674  0.72 23.44  ?  256  ASN A CB   1 
ATOM   519   C  CG   . ASN A 1 33  ? 17.997  -20.403 26.110  0.72 26.22  ?  256  ASN A CG   1 
ATOM   520   O  OD1  . ASN A 1 33  ? 17.980  -20.706 27.304  0.72 27.48  ?  256  ASN A OD1  1 
ATOM   521   N  ND2  . ASN A 1 33  ? 17.707  -21.271 25.148  0.72 27.74  ?  256  ASN A ND2  1 
ATOM   522   H  H    . ASN A 1 33  ? 15.976  -17.961 25.462  0.72 22.54  ?  256  ASN A H    1 
ATOM   523   H  HA   . ASN A 1 33  ? 17.806  -18.166 27.458  0.72 24.73  ?  256  ASN A HA   1 
ATOM   524   H  HB2  . ASN A 1 33  ? 18.063  -18.878 24.750  0.72 28.13  ?  256  ASN A HB2  1 
ATOM   525   H  HB3  . ASN A 1 33  ? 19.298  -18.869 25.749  0.72 28.13  ?  256  ASN A HB3  1 
ATOM   526   H  HD21 . ASN A 1 33  ? 17.508  -22.084 25.348  0.72 33.30  ?  256  ASN A HD21 1 
ATOM   527   H  HD22 . ASN A 1 33  ? 17.717  -21.020 24.326  0.72 33.30  ?  256  ASN A HD22 1 
ATOM   528   N  N    . ILE A 1 34  ? 17.405  -15.511 26.308  0.82 17.79  ?  257  ILE A N    1 
ATOM   529   C  CA   . ILE A 1 34  ? 17.913  -14.151 26.269  0.82 18.38  ?  257  ILE A CA   1 
ATOM   530   C  C    . ILE A 1 34  ? 17.245  -13.369 27.388  0.82 15.72  ?  257  ILE A C    1 
ATOM   531   O  O    . ILE A 1 34  ? 16.137  -13.690 27.827  0.82 18.70  ?  257  ILE A O    1 
ATOM   532   C  CB   . ILE A 1 34  ? 17.719  -13.473 24.896  0.82 21.71  ?  257  ILE A CB   1 
ATOM   533   C  CG1  . ILE A 1 34  ? 16.248  -13.224 24.604  0.82 21.55  ?  257  ILE A CG1  1 
ATOM   534   C  CG2  . ILE A 1 34  ? 18.287  -14.340 23.785  0.82 23.60  ?  257  ILE A CG2  1 
ATOM   535   C  CD1  . ILE A 1 34  ? 16.036  -12.185 23.527  0.82 21.62  ?  257  ILE A CD1  1 
ATOM   536   H  H    . ILE A 1 34  ? 16.547  -15.574 26.311  0.82 21.35  ?  257  ILE A H    1 
ATOM   537   H  HA   . ILE A 1 34  ? 18.869  -14.159 26.432  0.82 22.06  ?  257  ILE A HA   1 
ATOM   538   H  HB   . ILE A 1 34  ? 18.188  -12.624 24.933  0.82 26.06  ?  257  ILE A HB   1 
ATOM   539   H  HG12 . ILE A 1 34  ? 15.840  -14.052 24.307  0.82 25.86  ?  257  ILE A HG12 1 
ATOM   540   H  HG13 . ILE A 1 34  ? 15.813  -12.911 25.413  0.82 25.86  ?  257  ILE A HG13 1 
ATOM   541   H  HG21 . ILE A 1 34  ? 18.255  -13.847 22.951  0.82 28.32  ?  257  ILE A HG21 1 
ATOM   542   H  HG22 . ILE A 1 34  ? 19.205  -14.567 24.000  0.82 28.32  ?  257  ILE A HG22 1 
ATOM   543   H  HG23 . ILE A 1 34  ? 17.755  -15.148 23.712  0.82 28.32  ?  257  ILE A HG23 1 
ATOM   544   H  HD11 . ILE A 1 34  ? 15.086  -12.110 23.343  0.82 25.95  ?  257  ILE A HD11 1 
ATOM   545   H  HD12 . ILE A 1 34  ? 16.381  -11.333 23.838  0.82 25.95  ?  257  ILE A HD12 1 
ATOM   546   H  HD13 . ILE A 1 34  ? 16.507  -12.460 22.726  0.82 25.95  ?  257  ILE A HD13 1 
ATOM   547   N  N    . VAL A 1 35  ? 17.920  -12.337 27.855  1.00 14.69  ?  258  VAL A N    1 
ATOM   548   C  CA   . VAL A 1 35  ? 17.343  -11.426 28.833  1.00 12.44  ?  258  VAL A CA   1 
ATOM   549   C  C    . VAL A 1 35  ? 16.890  -10.187 28.076  1.00 10.92  ?  258  VAL A C    1 
ATOM   550   O  O    . VAL A 1 35  ? 17.702  -9.476  27.465  1.00 12.46  ?  258  VAL A O    1 
ATOM   551   C  CB   . VAL A 1 35  ? 18.328  -11.096 29.966  1.00 14.25  ?  258  VAL A CB   1 
ATOM   552   C  CG1  . VAL A 1 35  ? 17.709  -10.090 30.938  1.00 14.53  ?  258  VAL A CG1  1 
ATOM   553   C  CG2  . VAL A 1 35  ? 18.743  -12.373 30.700  1.00 17.26  ?  258  VAL A CG2  1 
ATOM   554   H  H    . VAL A 1 35  ? 18.723  -12.139 27.619  1.00 17.63  ?  258  VAL A H    1 
ATOM   555   H  HA   . VAL A 1 35  ? 16.567  -11.831 29.249  1.00 14.93  ?  258  VAL A HA   1 
ATOM   556   H  HB   . VAL A 1 35  ? 19.124  -10.695 29.584  1.00 17.10  ?  258  VAL A HB   1 
ATOM   557   H  HG11 . VAL A 1 35  ? 18.282  -10.010 31.716  1.00 17.44  ?  258  VAL A HG11 1 
ATOM   558   H  HG12 . VAL A 1 35  ? 17.631  -9.230  30.495  1.00 17.44  ?  258  VAL A HG12 1 
ATOM   559   H  HG13 . VAL A 1 35  ? 16.832  -10.406 31.204  1.00 17.44  ?  258  VAL A HG13 1 
ATOM   560   H  HG21 . VAL A 1 35  ? 19.352  -12.141 31.418  1.00 20.71  ?  258  VAL A HG21 1 
ATOM   561   H  HG22 . VAL A 1 35  ? 17.951  -12.801 31.063  1.00 20.71  ?  258  VAL A HG22 1 
ATOM   562   H  HG23 . VAL A 1 35  ? 19.182  -12.969 30.073  1.00 20.71  ?  258  VAL A HG23 1 
ATOM   563   N  N    . VAL A 1 36  ? 15.588  -9.942  28.101  1.00 8.19   ?  259  VAL A N    1 
ATOM   564   C  CA   . VAL A 1 36  ? 14.990  -8.822  27.383  1.00 7.53   ?  259  VAL A CA   1 
ATOM   565   C  C    . VAL A 1 36  ? 14.888  -7.654  28.362  1.00 6.94   ?  259  VAL A C    1 
ATOM   566   O  O    . VAL A 1 36  ? 13.972  -7.592  29.187  1.00 8.30   ?  259  VAL A O    1 
ATOM   567   C  CB   . VAL A 1 36  ? 13.639  -9.211  26.792  1.00 8.48   ?  259  VAL A CB   1 
ATOM   568   C  CG1  . VAL A 1 36  ? 13.016  -8.006  26.087  1.00 9.03   ?  259  VAL A CG1  1 
ATOM   569   C  CG2  . VAL A 1 36  ? 13.800  -10.376 25.830  1.00 10.54  ?  259  VAL A CG2  1 
ATOM   570   H  H    . VAL A 1 36  ? 15.018  -10.418 28.534  1.00 9.83   ?  259  VAL A H    1 
ATOM   571   H  HA   . VAL A 1 36  ? 15.574  -8.544  26.660  1.00 9.04   ?  259  VAL A HA   1 
ATOM   572   H  HB   . VAL A 1 36  ? 13.043  -9.491  27.504  1.00 10.18  ?  259  VAL A HB   1 
ATOM   573   H  HG11 . VAL A 1 36  ? 12.243  -8.301  25.581  1.00 10.84  ?  259  VAL A HG11 1 
ATOM   574   H  HG12 . VAL A 1 36  ? 12.747  -7.354  26.753  1.00 10.84  ?  259  VAL A HG12 1 
ATOM   575   H  HG13 . VAL A 1 36  ? 13.673  -7.615  25.489  1.00 10.84  ?  259  VAL A HG13 1 
ATOM   576   H  HG21 . VAL A 1 36  ? 12.945  -10.559 25.411  1.00 12.65  ?  259  VAL A HG21 1 
ATOM   577   H  HG22 . VAL A 1 36  ? 14.456  -10.140 25.156  1.00 12.65  ?  259  VAL A HG22 1 
ATOM   578   H  HG23 . VAL A 1 36  ? 14.100  -11.154 26.325  1.00 12.65  ?  259  VAL A HG23 1 
ATOM   579   N  N    . GLN A 1 37  ? 15.848  -6.731  28.289  1.00 6.43   ?  260  GLN A N    1 
ATOM   580   C  CA   . GLN A 1 37  ? 15.914  -5.623  29.246  1.00 6.82   ?  260  GLN A CA   1 
ATOM   581   C  C    . GLN A 1 37  ? 16.297  -4.319  28.549  1.00 5.51   ?  260  GLN A C    1 
ATOM   582   O  O    . GLN A 1 37  ? 17.200  -3.600  29.003  1.00 6.23   ?  260  GLN A O    1 
ATOM   583   C  CB   . GLN A 1 37  ? 16.875  -5.975  30.383  1.00 7.67   ?  260  GLN A CB   1 
ATOM   584   C  CG   . GLN A 1 37  ? 16.772  -5.056  31.565  1.00 8.95   ?  260  GLN A CG   1 
ATOM   585   C  CD   . GLN A 1 37  ? 17.542  -5.510  32.787  1.00 10.62  ?  260  GLN A CD   1 
ATOM   586   O  OE1  . GLN A 1 37  ? 18.478  -6.329  32.710  1.00 12.79  ?  260  GLN A OE1  1 
ATOM   587   N  NE2  . GLN A 1 37  ? 17.160  -4.957  33.931  1.00 10.48  ?  260  GLN A NE2  1 
ATOM   588   H  H    . GLN A 1 37  ? 16.472  -6.724  27.697  1.00 7.72   ?  260  GLN A H    1 
ATOM   589   H  HA   . GLN A 1 37  ? 15.037  -5.472  29.633  1.00 8.19   ?  260  GLN A HA   1 
ATOM   590   H  HB2  . GLN A 1 37  ? 16.681  -6.875  30.689  1.00 9.20   ?  260  GLN A HB2  1 
ATOM   591   H  HB3  . GLN A 1 37  ? 17.785  -5.928  30.049  1.00 9.20   ?  260  GLN A HB3  1 
ATOM   592   H  HG2  . GLN A 1 37  ? 17.116  -4.186  31.311  1.00 10.74  ?  260  GLN A HG2  1 
ATOM   593   H  HG3  . GLN A 1 37  ? 15.839  -4.983  31.819  1.00 10.74  ?  260  GLN A HG3  1 
ATOM   594   H  HE21 . GLN A 1 37  ? 16.518  -4.385  33.938  1.00 12.58  ?  260  GLN A HE21 1 
ATOM   595   H  HE22 . GLN A 1 37  ? 17.555  -5.169  34.665  1.00 12.58  ?  260  GLN A HE22 1 
ATOM   596   N  N    . PRO A 1 38  ? 15.601  -3.945  27.476  1.00 5.40   ?  261  PRO A N    1 
ATOM   597   C  CA   . PRO A 1 38  ? 15.910  -2.673  26.822  1.00 5.84   ?  261  PRO A CA   1 
ATOM   598   C  C    . PRO A 1 38  ? 15.602  -1.519  27.766  1.00 5.65   ?  261  PRO A C    1 
ATOM   599   O  O    . PRO A 1 38  ? 14.792  -1.631  28.687  1.00 6.03   ?  261  PRO A O    1 
ATOM   600   C  CB   . PRO A 1 38  ? 14.979  -2.669  25.609  1.00 6.15   ?  261  PRO A CB   1 
ATOM   601   C  CG   . PRO A 1 38  ? 13.817  -3.488  26.042  1.00 6.12   ?  261  PRO A CG   1 
ATOM   602   C  CD   . PRO A 1 38  ? 14.414  -4.589  26.883  1.00 6.14   ?  261  PRO A CD   1 
ATOM   603   H  HA   . PRO A 1 38  ? 16.830  -2.629  26.521  1.00 7.01   ?  261  PRO A HA   1 
ATOM   604   H  HB2  . PRO A 1 38  ? 14.709  -1.762  25.398  1.00 7.38   ?  261  PRO A HB2  1 
ATOM   605   H  HB3  . PRO A 1 38  ? 15.425  -3.069  24.846  1.00 7.38   ?  261  PRO A HB3  1 
ATOM   606   H  HG2  . PRO A 1 38  ? 13.205  -2.946  26.563  1.00 7.34   ?  261  PRO A HG2  1 
ATOM   607   H  HG3  . PRO A 1 38  ? 13.361  -3.851  25.267  1.00 7.34   ?  261  PRO A HG3  1 
ATOM   608   H  HD2  . PRO A 1 38  ? 13.794  -4.874  27.572  1.00 7.37   ?  261  PRO A HD2  1 
ATOM   609   H  HD3  . PRO A 1 38  ? 14.669  -5.346  26.333  1.00 7.37   ?  261  PRO A HD3  1 
ATOM   610   N  N    . GLN A 1 39  ? 16.273  -0.391  27.525  1.00 5.84   ?  262  GLN A N    1 
ATOM   611   C  CA   . GLN A 1 39  ? 16.130  0.783   28.375  1.00 5.76   ?  262  GLN A CA   1 
ATOM   612   C  C    . GLN A 1 39  ? 15.468  1.962   27.680  1.00 5.92   ?  262  GLN A C    1 
ATOM   613   O  O    . GLN A 1 39  ? 14.930  2.841   28.368  1.00 6.26   ?  262  GLN A O    1 
ATOM   614   C  CB   . GLN A 1 39  ? 17.496  1.199   28.939  1.00 6.30   ?  262  GLN A CB   1 
ATOM   615   C  CG   . GLN A 1 39  ? 18.115  0.094   29.777  1.00 6.57   ?  262  GLN A CG   1 
ATOM   616   C  CD   . GLN A 1 39  ? 17.248  -0.244  30.976  1.00 6.49   ?  262  GLN A CD   1 
ATOM   617   O  OE1  . GLN A 1 39  ? 16.856  0.625   31.753  1.00 7.27   ?  262  GLN A OE1  1 
ATOM   618   N  NE2  . GLN A 1 39  ? 16.944  -1.529  31.132  1.00 6.30   ?  262  GLN A NE2  1 
ATOM   619   H  H    . GLN A 1 39  ? 16.820  -0.284  26.870  1.00 7.00   ?  262  GLN A H    1 
ATOM   620   H  HA   . GLN A 1 39  ? 15.571  0.560   29.136  1.00 6.91   ?  262  GLN A HA   1 
ATOM   621   H  HB2  . GLN A 1 39  ? 18.098  1.399   28.206  1.00 7.56   ?  262  GLN A HB2  1 
ATOM   622   H  HB3  . GLN A 1 39  ? 17.385  1.982   29.501  1.00 7.56   ?  262  GLN A HB3  1 
ATOM   623   H  HG2  . GLN A 1 39  ? 18.211  -0.704  29.234  1.00 7.88   ?  262  GLN A HG2  1 
ATOM   624   H  HG3  . GLN A 1 39  ? 18.983  0.383   30.099  1.00 7.88   ?  262  GLN A HG3  1 
ATOM   625   H  HE21 . GLN A 1 39  ? 17.236  -2.111  30.570  1.00 7.56   ?  262  GLN A HE21 1 
ATOM   626   H  HE22 . GLN A 1 39  ? 16.456  -1.778  31.795  1.00 7.56   ?  262  GLN A HE22 1 
ATOM   627   N  N    . ASN A 1 40  ? 15.480  1.999   26.350  1.00 5.74   ?  263  ASN A N    1 
ATOM   628   C  CA   . ASN A 1 40  ? 14.641  2.915   25.592  1.00 6.00   ?  263  ASN A CA   1 
ATOM   629   C  C    . ASN A 1 40  ? 13.341  2.204   25.233  1.00 5.81   ?  263  ASN A C    1 
ATOM   630   O  O    . ASN A 1 40  ? 13.280  0.971   25.183  1.00 6.15   ?  263  ASN A O    1 
ATOM   631   C  CB   . ASN A 1 40  ? 15.370  3.405   24.345  1.00 5.62   ?  263  ASN A CB   1 
ATOM   632   C  CG   . ASN A 1 40  ? 16.495  4.349   24.687  1.00 5.80   ?  263  ASN A CG   1 
ATOM   633   O  OD1  . ASN A 1 40  ? 16.312  5.280   25.477  1.00 6.37   ?  263  ASN A OD1  1 
ATOM   634   N  ND2  . ASN A 1 40  ? 17.652  4.144   24.089  1.00 6.50   ?  263  ASN A ND2  1 
ATOM   635   H  H    . ASN A 1 40  ? 15.973  1.494   25.858  1.00 6.89   ?  263  ASN A H    1 
ATOM   636   H  HA   . ASN A 1 40  ? 14.425  3.704   26.113  1.00 7.20   ?  263  ASN A HA   1 
ATOM   637   H  HB2  . ASN A 1 40  ? 15.744  2.644   23.874  1.00 6.74   ?  263  ASN A HB2  1 
ATOM   638   H  HB3  . ASN A 1 40  ? 14.743  3.875   23.772  1.00 6.74   ?  263  ASN A HB3  1 
ATOM   639   H  HD21 . ASN A 1 40  ? 18.319  4.660   24.256  1.00 7.80   ?  263  ASN A HD21 1 
ATOM   640   H  HD22 . ASN A 1 40  ? 17.738  3.496   23.531  1.00 7.80   ?  263  ASN A HD22 1 
ATOM   641   N  N    . GLY A 1 41  ? 12.289  2.991   25.039  1.00 5.78   ?  264  GLY A N    1 
ATOM   642   C  CA   . GLY A 1 41  ? 10.983  2.432   24.762  1.00 6.59   ?  264  GLY A CA   1 
ATOM   643   C  C    . GLY A 1 41  ? 10.356  1.749   25.953  1.00 6.31   ?  264  GLY A C    1 
ATOM   644   O  O    . GLY A 1 41  ? 9.643   0.750   25.787  1.00 6.46   ?  264  GLY A O    1 
ATOM   645   H  H    . GLY A 1 41  ? 12.310  3.850   25.064  1.00 6.94   ?  264  GLY A H    1 
ATOM   646   H  HA2  . GLY A 1 41  ? 10.389  3.143   24.475  1.00 7.92   ?  264  GLY A HA2  1 
ATOM   647   H  HA3  . GLY A 1 41  ? 11.063  1.780   24.048  1.00 7.92   ?  264  GLY A HA3  1 
ATOM   648   N  N    . ARG A 1 42  ? 10.591  2.288   27.160  1.00 5.98   ?  265  ARG A N    1 
ATOM   649   C  CA   . ARG A 1 42  ? 10.091  1.725   28.412  1.00 5.85   ?  265  ARG A CA   1 
ATOM   650   C  C    . ARG A 1 42  ? 9.150   2.738   29.058  1.00 6.37   ?  265  ARG A C    1 
ATOM   651   O  O    . ARG A 1 42  ? 9.584   3.782   29.567  1.00 7.03   ?  265  ARG A O    1 
ATOM   652   C  CB   . ARG A 1 42  ? 11.240  1.331   29.344  1.00 6.67   ?  265  ARG A CB   1 
ATOM   653   C  CG   . ARG A 1 42  ? 12.202  0.358   28.723  1.00 6.90   ?  265  ARG A CG   1 
ATOM   654   C  CD   . ARG A 1 42  ? 11.583  -0.993  28.431  1.00 7.60   ?  265  ARG A CD   1 
ATOM   655   N  NE   . ARG A 1 42  ? 11.008  -1.635  29.604  1.00 8.04   ?  265  ARG A NE   1 
ATOM   656   C  CZ   . ARG A 1 42  ? 11.557  -2.603  30.325  1.00 10.19  ?  265  ARG A CZ   1 
ATOM   657   N  NH1  . ARG A 1 42  ? 12.762  -3.105  30.029  1.00 10.95  ?  265  ARG A NH1  1 
ATOM   658   N  NH2  . ARG A 1 42  ? 10.882  -3.077  31.369  1.00 11.58  ?  265  ARG A NH2  1 
ATOM   659   H  H    . ARG A 1 42  ? 11.055  3.003   27.276  1.00 7.18   ?  265  ARG A H    1 
ATOM   660   H  HA   . ARG A 1 42  ? 9.577   0.924   28.223  1.00 7.02   ?  265  ARG A HA   1 
ATOM   661   H  HB2  . ARG A 1 42  ? 11.736  2.129   29.584  1.00 8.00   ?  265  ARG A HB2  1 
ATOM   662   H  HB3  . ARG A 1 42  ? 10.870  0.918   30.140  1.00 8.00   ?  265  ARG A HB3  1 
ATOM   663   H  HG2  . ARG A 1 42  ? 12.523  0.725   27.884  1.00 8.28   ?  265  ARG A HG2  1 
ATOM   664   H  HG3  . ARG A 1 42  ? 12.945  0.219   29.330  1.00 8.28   ?  265  ARG A HG3  1 
ATOM   665   H  HD2  . ARG A 1 42  ? 10.875  -0.879  27.778  1.00 9.13   ?  265  ARG A HD2  1 
ATOM   666   H  HD3  . ARG A 1 42  ? 12.268  -1.582  28.077  1.00 9.13   ?  265  ARG A HD3  1 
ATOM   667   H  HE   . ARG A 1 42  ? 10.233  -1.359  29.855  1.00 9.65   ?  265  ARG A HE   1 
ATOM   668   H  HH11 . ARG A 1 42  ? 13.201  -2.800  29.356  1.00 13.14  ?  265  ARG A HH11 1 
ATOM   669   H  HH12 . ARG A 1 42  ? 13.096  -3.733  30.513  1.00 13.14  ?  265  ARG A HH12 1 
ATOM   670   H  HH21 . ARG A 1 42  ? 10.108  -2.755  31.563  1.00 13.90  ?  265  ARG A HH21 1 
ATOM   671   H  HH22 . ARG A 1 42  ? 11.219  -3.705  31.850  1.00 13.90  ?  265  ARG A HH22 1 
ATOM   672   N  N    . CYS A 1 43  ? 7.864   2.418   29.056  1.00 6.81   ?  266  CYS A N    1 
ATOM   673   C  CA   . CYS A 1 43  ? 6.858   3.252   29.694  1.00 7.27   ?  266  CYS A CA   1 
ATOM   674   C  C    . CYS A 1 43  ? 5.737   2.354   30.185  1.00 7.15   ?  266  CYS A C    1 
ATOM   675   O  O    . CYS A 1 43  ? 5.253   1.496   29.437  1.00 7.82   ?  266  CYS A O    1 
ATOM   676   C  CB   . CYS A 1 43  ? 6.302   4.253   28.685  1.00 7.48   ?  266  CYS A CB   1 
ATOM   677   S  SG   . CYS A 1 43  ? 5.184   5.495   29.371  1.00 8.81   ?  266  CYS A SG   1 
ATOM   678   H  H    . CYS A 1 43  ? 7.544   1.710   28.686  1.00 8.17   ?  266  CYS A H    1 
ATOM   679   H  HA   . CYS A 1 43  ? 7.237   3.727   30.450  1.00 8.72   ?  266  CYS A HA   1 
ATOM   680   H  HB2  . CYS A 1 43  ? 7.047   4.725   28.280  1.00 8.98   ?  266  CYS A HB2  1 
ATOM   681   H  HB3  . CYS A 1 43  ? 5.811   3.764   28.006  1.00 8.98   ?  266  CYS A HB3  1 
ATOM   682   H  HG   . CYS A 1 43  ? 4.192   4.950   29.769  1.00 10.58  ?  266  CYS A HG   1 
ATOM   683   N  N    . THR A 1 44  ? 5.342   2.516   31.440  1.00 6.75   ?  267  THR A N    1 
ATOM   684   C  CA   . THR A 1 44  ? 4.191   1.771   31.917  1.00 7.12   ?  267  THR A CA   1 
ATOM   685   C  C    . THR A 1 44  ? 2.922   2.278   31.223  1.00 6.69   ?  267  THR A C    1 
ATOM   686   O  O    . THR A 1 44  ? 2.857   3.409   30.737  1.00 7.25   ?  267  THR A O    1 
ATOM   687   C  CB   . THR A 1 44  ? 4.057   1.875   33.436  1.00 7.42   ?  267  THR A CB   1 
ATOM   688   O  OG1  . THR A 1 44  ? 3.717   3.210   33.800  1.00 7.80   ?  267  THR A OG1  1 
ATOM   689   C  CG2  . THR A 1 44  ? 5.343   1.468   34.116  1.00 8.63   ?  267  THR A CG2  1 
ATOM   690   H  H    . THR A 1 44  ? 5.713   3.035   32.017  1.00 8.11   ?  267  THR A H    1 
ATOM   691   H  HA   . THR A 1 44  ? 4.299   0.830   31.709  1.00 8.55   ?  267  THR A HA   1 
ATOM   692   H  HB   . THR A 1 44  ? 3.357   1.276   33.739  1.00 8.91   ?  267  THR A HB   1 
ATOM   693   H  HG1  . THR A 1 44  ? 2.931   3.382   33.558  1.00 9.36   ?  267  THR A HG1  1 
ATOM   694   H  HG21 . THR A 1 44  ? 5.218   1.448   35.078  1.00 10.35  ?  267  THR A HG21 1 
ATOM   695   H  HG22 . THR A 1 44  ? 5.612   0.586   33.816  1.00 10.35  ?  267  THR A HG22 1 
ATOM   696   H  HG23 . THR A 1 44  ? 6.046   2.101   33.904  1.00 10.35  ?  267  THR A HG23 1 
ATOM   697   N  N    . ILE A 1 45  ? 1.878   1.442   31.222  1.00 7.07   ?  268  ILE A N    1 
ATOM   698   C  CA   . ILE A 1 45  ? 0.680   1.819   30.488  1.00 6.89   ?  268  ILE A CA   1 
ATOM   699   C  C    . ILE A 1 45  ? -0.052  2.953   31.177  1.00 7.22   ?  268  ILE A C    1 
ATOM   700   O  O    . ILE A 1 45  ? -0.888  3.610   30.538  1.00 8.31   ?  268  ILE A O    1 
ATOM   701   C  CB   . ILE A 1 45  ? -0.253  0.631   30.192  1.00 7.90   ?  268  ILE A CB   1 
ATOM   702   C  CG1  . ILE A 1 45  ? -0.894  0.101   31.480  1.00 8.94   ?  268  ILE A CG1  1 
ATOM   703   C  CG2  . ILE A 1 45  ? 0.509   -0.439  29.443  1.00 9.51   ?  268  ILE A CG2  1 
ATOM   704   C  CD1  . ILE A 1 45  ? -1.882  -1.060  31.279  1.00 11.57  ?  268  ILE A CD1  1 
ATOM   705   H  H    . ILE A 1 45  ? 1.845   0.683   31.624  1.00 8.49   ?  268  ILE A H    1 
ATOM   706   H  HA   . ILE A 1 45  ? 0.972   2.128   29.616  1.00 8.27   ?  268  ILE A HA   1 
ATOM   707   H  HB   . ILE A 1 45  ? -0.982  0.931   29.627  1.00 9.48   ?  268  ILE A HB   1 
ATOM   708   H  HG12 . ILE A 1 45  ? -0.189  -0.214  32.067  1.00 10.73  ?  268  ILE A HG12 1 
ATOM   709   H  HG13 . ILE A 1 45  ? -1.378  0.827   31.904  1.00 10.73  ?  268  ILE A HG13 1 
ATOM   710   H  HG21 . ILE A 1 45  ? -0.112  -1.130  29.162  1.00 11.41  ?  268  ILE A HG21 1 
ATOM   711   H  HG22 . ILE A 1 45  ? 0.933   -0.040  28.667  1.00 11.41  ?  268  ILE A HG22 1 
ATOM   712   H  HG23 . ILE A 1 45  ? 1.181   -0.818  30.030  1.00 11.41  ?  268  ILE A HG23 1 
ATOM   713   H  HD11 . ILE A 1 45  ? -2.280  -1.287  32.134  1.00 13.88  ?  268  ILE A HD11 1 
ATOM   714   H  HD12 . ILE A 1 45  ? -2.572  -0.783  30.656  1.00 13.88  ?  268  ILE A HD12 1 
ATOM   715   H  HD13 . ILE A 1 45  ? -1.402  -1.825  30.924  1.00 13.88  ?  268  ILE A HD13 1 
ATOM   716   N  N    . ASP A 1 46  ? 0.235   3.181   32.469  1.00 7.44   ?  269  ASP A N    1 
ATOM   717   C  CA   . ASP A 1 46  ? -0.302  4.318   33.209  1.00 8.22   ?  269  ASP A CA   1 
ATOM   718   C  C    . ASP A 1 46  ? 0.636   5.534   33.185  1.00 8.14   ?  269  ASP A C    1 
ATOM   719   O  O    . ASP A 1 46  ? 0.380   6.506   33.902  1.00 9.72   ?  269  ASP A O    1 
ATOM   720   C  CB   . ASP A 1 46  ? -0.792  3.926   34.616  1.00 10.27  ?  269  ASP A CB   1 
ATOM   721   C  CG   . ASP A 1 46  ? 0.241   3.182   35.452  1.00 12.02  ?  269  ASP A CG   1 
ATOM   722   O  OD1  . ASP A 1 46  ? 1.333   2.870   34.967  1.00 11.72  ?  269  ASP A OD1  1 
ATOM   723   O  OD2  . ASP A 1 46  ? -0.050  2.890   36.630  1.00 15.63  -1 269  ASP A OD2  1 
ATOM   724   H  H    . ASP A 1 46  ? 0.748   2.677   32.941  1.00 8.93   ?  269  ASP A H    1 
ATOM   725   H  HA   . ASP A 1 46  ? -1.119  4.613   32.777  1.00 9.87   ?  269  ASP A HA   1 
ATOM   726   H  HB2  . ASP A 1 46  ? -1.033  4.733   35.097  1.00 12.33  ?  269  ASP A HB2  1 
ATOM   727   H  HB3  . ASP A 1 46  ? -1.567  3.350   34.526  1.00 12.33  ?  269  ASP A HB3  1 
ATOM   728   N  N    . GLY A 1 47  ? 1.680   5.508   32.348  1.00 7.67   ?  270  GLY A N    1 
ATOM   729   C  CA   . GLY A 1 47  ? 2.424   6.699   31.977  1.00 8.68   ?  270  GLY A CA   1 
ATOM   730   C  C    . GLY A 1 47  ? 3.752   6.968   32.662  1.00 8.38   ?  270  GLY A C    1 
ATOM   731   O  O    . GLY A 1 47  ? 4.253   8.093   32.542  1.00 8.79   ?  270  GLY A O    1 
ATOM   732   H  H    . GLY A 1 47  ? 1.978   4.792   31.977  1.00 9.20   ?  270  GLY A H    1 
ATOM   733   H  HA2  . GLY A 1 47  ? 2.604   6.649   31.025  1.00 10.42  ?  270  GLY A HA2  1 
ATOM   734   H  HA3  . GLY A 1 47  ? 1.858   7.467   32.152  1.00 10.42  ?  270  GLY A HA3  1 
ATOM   735   N  N    . GLU A 1 48  ? 4.348   5.991   33.337  1.00 7.71   ?  271  GLU A N    1 
ATOM   736   C  CA   . GLU A 1 48  ? 5.640   6.204   33.989  1.00 8.25   ?  271  GLU A CA   1 
ATOM   737   C  C    . GLU A 1 48  ? 6.785   5.837   33.044  1.00 7.09   ?  271  GLU A C    1 
ATOM   738   O  O    . GLU A 1 48  ? 6.924   4.679   32.651  1.00 7.47   ?  271  GLU A O    1 
ATOM   739   C  CB   . GLU A 1 48  ? 5.732   5.383   35.275  1.00 11.01  ?  271  GLU A CB   1 
ATOM   740   C  CG   . GLU A 1 48  ? 7.005   5.647   36.061  1.00 16.05  ?  271  GLU A CG   1 
ATOM   741   C  CD   . GLU A 1 48  ? 7.213   4.686   37.226  1.00 20.51  ?  271  GLU A CD   1 
ATOM   742   O  OE1  . GLU A 1 48  ? 6.480   3.674   37.327  1.00 22.70  ?  271  GLU A OE1  1 
ATOM   743   O  OE2  . GLU A 1 48  ? 8.121   4.944   38.053  1.00 22.45  -1 271  GLU A OE2  1 
ATOM   744   H  H    . GLU A 1 48  ? 4.028   5.199   33.433  1.00 9.25   ?  271  GLU A H    1 
ATOM   745   H  HA   . GLU A 1 48  ? 5.725   7.146   34.205  1.00 9.91   ?  271  GLU A HA   1 
ATOM   746   H  HB2  . GLU A 1 48  ? 4.978   5.604   35.844  1.00 13.22  ?  271  GLU A HB2  1 
ATOM   747   H  HB3  . GLU A 1 48  ? 5.711   4.440   35.049  1.00 13.22  ?  271  GLU A HB3  1 
ATOM   748   H  HG2  . GLU A 1 48  ? 7.765   5.560   35.464  1.00 19.26  ?  271  GLU A HG2  1 
ATOM   749   H  HG3  . GLU A 1 48  ? 6.968   6.547   36.422  1.00 19.26  ?  271  GLU A HG3  1 
ATOM   750   N  N    . LEU A 1 49  ? 7.623   6.818   32.706  1.00 7.57   ?  272  LEU A N    1 
ATOM   751   C  CA   . LEU A 1 49  ? 8.819   6.549   31.916  1.00 7.44   ?  272  LEU A CA   1 
ATOM   752   C  C    . LEU A 1 49  ? 9.840   5.795   32.757  1.00 7.31   ?  272  LEU A C    1 
ATOM   753   O  O    . LEU A 1 49  ? 10.038  6.106   33.932  1.00 7.83   ?  272  LEU A O    1 
ATOM   754   C  CB   . LEU A 1 49  ? 9.464   7.855   31.434  1.00 7.90   ?  272  LEU A CB   1 
ATOM   755   C  CG   . LEU A 1 49  ? 8.564   8.815   30.655  1.00 7.81   ?  272  LEU A CG   1 
ATOM   756   C  CD1  . LEU A 1 49  ? 9.301   10.110  30.322  1.00 9.18   ?  272  LEU A CD1  1 
ATOM   757   C  CD2  . LEU A 1 49  ? 8.012   8.155   29.397  1.00 8.85   ?  272  LEU A CD2  1 
ATOM   758   H  H    . LEU A 1 49  ? 7.521   7.644   32.922  1.00 9.09   ?  272  LEU A H    1 
ATOM   759   H  HA   . LEU A 1 49  ? 8.568   6.019   31.143  1.00 8.93   ?  272  LEU A HA   1 
ATOM   760   H  HB2  . LEU A 1 49  ? 9.787   8.335   32.212  1.00 9.48   ?  272  LEU A HB2  1 
ATOM   761   H  HB3  . LEU A 1 49  ? 10.207  7.626   30.853  1.00 9.48   ?  272  LEU A HB3  1 
ATOM   762   H  HG   . LEU A 1 49  ? 7.808   9.046   31.216  1.00 9.38   ?  272  LEU A HG   1 
ATOM   763   H  HD11 . LEU A 1 49  ? 8.699   10.702  29.845  1.00 11.01  ?  272  LEU A HD11 1 
ATOM   764   H  HD12 . LEU A 1 49  ? 9.592   10.530  31.147  1.00 11.01  ?  272  LEU A HD12 1 
ATOM   765   H  HD13 . LEU A 1 49  ? 10.070  9.903   29.768  1.00 11.01  ?  272  LEU A HD13 1 
ATOM   766   H  HD21 . LEU A 1 49  ? 7.487   8.804   28.904  1.00 10.62  ?  272  LEU A HD21 1 
ATOM   767   H  HD22 . LEU A 1 49  ? 8.753   7.847   28.851  1.00 10.62  ?  272  LEU A HD22 1 
ATOM   768   H  HD23 . LEU A 1 49  ? 7.455   7.403   29.653  1.00 10.62  ?  272  LEU A HD23 1 
ATOM   769   N  N    . LEU A 1 50  ? 10.520  4.828   32.139  1.00 7.03   ?  273  LEU A N    1 
ATOM   770   C  CA   . LEU A 1 50  ? 11.517  4.009   32.813  1.00 6.79   ?  273  LEU A CA   1 
ATOM   771   C  C    . LEU A 1 50  ? 12.830  4.012   32.038  1.00 7.11   ?  273  LEU A C    1 
ATOM   772   O  O    . LEU A 1 50  ? 12.899  4.384   30.866  1.00 6.64   ?  273  LEU A O    1 
ATOM   773   C  CB   . LEU A 1 50  ? 11.030  2.558   32.949  1.00 7.33   ?  273  LEU A CB   1 
ATOM   774   C  CG   . LEU A 1 50  ? 9.662   2.351   33.586  1.00 9.96   ?  273  LEU A CG   1 
ATOM   775   C  CD1  . LEU A 1 50  ? 9.236   0.899   33.423  1.00 11.47  ?  273  LEU A CD1  1 
ATOM   776   C  CD2  . LEU A 1 50  ? 9.651   2.765   35.039  1.00 13.24  ?  273  LEU A CD2  1 
ATOM   777   H  H    . LEU A 1 50  ? 10.416  4.626   31.310  1.00 8.44   ?  273  LEU A H    1 
ATOM   778   H  HA   . LEU A 1 50  ? 11.686  4.385   33.691  1.00 8.15   ?  273  LEU A HA   1 
ATOM   779   H  HB2  . LEU A 1 50  ? 10.991  2.171   32.061  1.00 8.79   ?  273  LEU A HB2  1 
ATOM   780   H  HB3  . LEU A 1 50  ? 11.672  2.076   33.493  1.00 8.79   ?  273  LEU A HB3  1 
ATOM   781   H  HG   . LEU A 1 50  ? 9.016   2.917   33.136  1.00 11.96  ?  273  LEU A HG   1 
ATOM   782   H  HD11 . LEU A 1 50  ? 8.363   0.779   33.829  1.00 13.76  ?  273  LEU A HD11 1 
ATOM   783   H  HD12 . LEU A 1 50  ? 9.193   0.687   32.478  1.00 13.76  ?  273  LEU A HD12 1 
ATOM   784   H  HD13 . LEU A 1 50  ? 9.886   0.328   33.861  1.00 13.76  ?  273  LEU A HD13 1 
ATOM   785   H  HD21 . LEU A 1 50  ? 8.766   2.609   35.405  1.00 15.89  ?  273  LEU A HD21 1 
ATOM   786   H  HD22 . LEU A 1 50  ? 10.306  2.238   35.522  1.00 15.89  ?  273  LEU A HD22 1 
ATOM   787   H  HD23 . LEU A 1 50  ? 9.873   3.707   35.101  1.00 15.89  ?  273  LEU A HD23 1 
ATOM   788   N  N    . GLY A 1 51  ? 13.888  3.567   32.699  1.00 6.92   ?  274  GLY A N    1 
ATOM   789   C  CA   . GLY A 1 51  ? 15.150  3.408   32.000  1.00 7.33   ?  274  GLY A CA   1 
ATOM   790   C  C    . GLY A 1 51  ? 15.685  4.735   31.515  1.00 7.09   ?  274  GLY A C    1 
ATOM   791   O  O    . GLY A 1 51  ? 15.722  5.731   32.253  1.00 8.11   ?  274  GLY A O    1 
ATOM   792   H  H    . GLY A 1 51  ? 13.901  3.356   33.533  1.00 8.31   ?  274  GLY A H    1 
ATOM   793   H  HA2  . GLY A 1 51  ? 15.803  3.010   32.597  1.00 8.80   ?  274  GLY A HA2  1 
ATOM   794   H  HA3  . GLY A 1 51  ? 15.026  2.826   31.234  1.00 8.80   ?  274  GLY A HA3  1 
ATOM   795   N  N    . THR A 1 52  ? 16.145  4.755   30.266  1.00 6.55   ?  275  THR A N    1 
ATOM   796   C  CA   . THR A 1 52  ? 16.617  5.968   29.610  1.00 6.65   ?  275  THR A CA   1 
ATOM   797   C  C    . THR A 1 52  ? 15.566  6.580   28.694  1.00 6.30   ?  275  THR A C    1 
ATOM   798   O  O    . THR A 1 52  ? 15.899  7.366   27.795  1.00 6.40   ?  275  THR A O    1 
ATOM   799   C  CB   . THR A 1 52  ? 17.909  5.694   28.839  1.00 6.72   ?  275  THR A CB   1 
ATOM   800   O  OG1  . THR A 1 52  ? 17.700  4.631   27.902  1.00 6.63   ?  275  THR A OG1  1 
ATOM   801   C  CG2  . THR A 1 52  ? 19.056  5.290   29.762  1.00 6.87   ?  275  THR A CG2  1 
ATOM   802   H  H    . THR A 1 52  ? 16.194  4.057   29.766  1.00 7.86   ?  275  THR A H    1 
ATOM   803   H  HA   . THR A 1 52  ? 16.823  6.622   30.296  1.00 7.98   ?  275  THR A HA   1 
ATOM   804   H  HB   . THR A 1 52  ? 18.161  6.512   28.382  1.00 8.07   ?  275  THR A HB   1 
ATOM   805   H  HG1  . THR A 1 52  ? 17.087  4.837   27.366  1.00 7.96   ?  275  THR A HG1  1 
ATOM   806   H  HG21 . THR A 1 52  ? 19.864  5.146   29.245  1.00 8.25   ?  275  THR A HG21 1 
ATOM   807   H  HG22 . THR A 1 52  ? 19.220  5.989   30.414  1.00 8.25   ?  275  THR A HG22 1 
ATOM   808   H  HG23 . THR A 1 52  ? 18.833  4.470   30.230  1.00 8.25   ?  275  THR A HG23 1 
ATOM   809   N  N    . THR A 1 53  ? 14.299  6.245   28.888  1.00 5.73   ?  276  THR A N    1 
ATOM   810   C  CA   . THR A 1 53  ? 13.267  6.635   27.934  1.00 6.26   ?  276  THR A CA   1 
ATOM   811   C  C    . THR A 1 53  ? 12.896  8.102   28.044  1.00 6.76   ?  276  THR A C    1 
ATOM   812   O  O    . THR A 1 53  ? 12.593  8.606   29.128  1.00 7.77   ?  276  THR A O    1 
ATOM   813   C  CB   . THR A 1 53  ? 12.052  5.745   28.114  1.00 6.58   ?  276  THR A CB   1 
ATOM   814   O  OG1  . THR A 1 53  ? 12.422  4.401   27.808  1.00 6.82   ?  276  THR A OG1  1 
ATOM   815   C  CG2  . THR A 1 53  ? 10.937  6.126   27.162  1.00 6.66   ?  276  THR A CG2  1 
ATOM   816   H  H    . THR A 1 53  ? 14.010  5.794   29.561  1.00 6.88   ?  276  THR A H    1 
ATOM   817   H  HA   . THR A 1 53  ? 13.616  6.521   27.036  1.00 7.52   ?  276  THR A HA   1 
ATOM   818   H  HB   . THR A 1 53  ? 11.732  5.835   29.025  1.00 7.89   ?  276  THR A HB   1 
ATOM   819   H  HG1  . THR A 1 53  ? 13.006  4.134   28.349  1.00 8.18   ?  276  THR A HG1  1 
ATOM   820   H  HG21 . THR A 1 53  ? 10.245  5.446   27.172  1.00 8.00   ?  276  THR A HG21 1 
ATOM   821   H  HG22 . THR A 1 53  ? 10.549  6.974   27.428  1.00 8.00   ?  276  THR A HG22 1 
ATOM   822   H  HG23 . THR A 1 53  ? 11.284  6.208   26.260  1.00 8.00   ?  276  THR A HG23 1 
ATOM   823   N  N    . GLN A 1 54  ? 12.913  8.781   26.910  1.00 5.99   ?  277  GLN A N    1 
ATOM   824   C  CA   . GLN A 1 54  ? 12.417  10.155  26.796  1.00 6.47   ?  277  GLN A CA   1 
ATOM   825   C  C    . GLN A 1 54  ? 11.383  10.210  25.673  1.00 6.96   ?  277  GLN A C    1 
ATOM   826   O  O    . GLN A 1 54  ? 11.006  9.163   25.131  1.00 7.69   ?  277  GLN A O    1 
ATOM   827   C  CB   . GLN A 1 54  ? 13.573  11.155  26.675  1.00 7.36   ?  277  GLN A CB   1 
ATOM   828   C  CG   . GLN A 1 54  ? 14.593  10.816  25.597  1.00 7.41   ?  277  GLN A CG   1 
ATOM   829   C  CD   . GLN A 1 54  ? 14.080  11.111  24.206  1.00 7.07   ?  277  GLN A CD   1 
ATOM   830   O  OE1  . GLN A 1 54  ? 13.678  12.239  23.911  1.00 7.97   ?  277  GLN A OE1  1 
ATOM   831   N  NE2  . GLN A 1 54  ? 14.058  10.092  23.345  1.00 7.36   ?  277  GLN A NE2  1 
ATOM   832   H  H    . GLN A 1 54  ? 13.214  8.467   26.168  1.00 7.19   ?  277  GLN A H    1 
ATOM   833   H  HA   . GLN A 1 54  ? 11.961  10.443  27.602  1.00 7.77   ?  277  GLN A HA   1 
ATOM   834   H  HB2  . GLN A 1 54  ? 13.206  12.028  26.465  1.00 8.83   ?  277  GLN A HB2  1 
ATOM   835   H  HB3  . GLN A 1 54  ? 14.044  11.188  27.522  1.00 8.83   ?  277  GLN A HB3  1 
ATOM   836   H  HG2  . GLN A 1 54  ? 15.394  11.342  25.741  1.00 8.89   ?  277  GLN A HG2  1 
ATOM   837   H  HG3  . GLN A 1 54  ? 14.804  9.870   25.646  1.00 8.89   ?  277  GLN A HG3  1 
ATOM   838   H  HE21 . GLN A 1 54  ? 14.328  9.314   23.593  1.00 8.84   ?  277  GLN A HE21 1 
ATOM   839   H  HE22 . GLN A 1 54  ? 13.775  10.213  22.542  1.00 8.84   ?  277  GLN A HE22 1 
ATOM   840   N  N    . LEU A 1 55  ? 10.894  11.409  25.335  1.00 7.45   ?  278  LEU A N    1 
ATOM   841   C  CA   . LEU A 1 55  ? 9.677   11.535  24.543  1.00 7.16   ?  278  LEU A CA   1 
ATOM   842   C  C    . LEU A 1 55  ? 9.897   11.745  23.049  1.00 7.90   ?  278  LEU A C    1 
ATOM   843   O  O    . LEU A 1 55  ? 8.968   11.490  22.286  1.00 8.49   ?  278  LEU A O    1 
ATOM   844   C  CB   . LEU A 1 55  ? 8.832   12.713  25.039  1.00 8.32   ?  278  LEU A CB   1 
ATOM   845   C  CG   . LEU A 1 55  ? 7.799   12.391  26.105  1.00 10.85  ?  278  LEU A CG   1 
ATOM   846   C  CD1  . LEU A 1 55  ? 6.716   11.511  25.518  1.00 12.04  ?  278  LEU A CD1  1 
ATOM   847   C  CD2  . LEU A 1 55  ? 8.429   11.737  27.270  1.00 12.43  ?  278  LEU A CD2  1 
ATOM   848   H  H    . LEU A 1 55  ? 11.252  12.160  25.554  1.00 8.94   ?  278  LEU A H    1 
ATOM   849   H  HA   . LEU A 1 55  ? 9.186   10.706  24.660  1.00 8.59   ?  278  LEU A HA   1 
ATOM   850   H  HB2  . LEU A 1 55  ? 9.430   13.379  25.411  1.00 9.99   ?  278  LEU A HB2  1 
ATOM   851   H  HB3  . LEU A 1 55  ? 8.355   13.084  24.280  1.00 9.99   ?  278  LEU A HB3  1 
ATOM   852   H  HG   . LEU A 1 55  ? 7.393   13.214  26.417  1.00 13.02  ?  278  LEU A HG   1 
ATOM   853   H  HD11 . LEU A 1 55  ? 5.973   11.467  26.141  1.00 14.45  ?  278  LEU A HD11 1 
ATOM   854   H  HD12 . LEU A 1 55  ? 6.420   11.891  24.677  1.00 14.45  ?  278  LEU A HD12 1 
ATOM   855   H  HD13 . LEU A 1 55  ? 7.076   10.622  25.372  1.00 14.45  ?  278  LEU A HD13 1 
ATOM   856   H  HD21 . LEU A 1 55  ? 7.782   11.685  27.991  1.00 14.91  ?  278  LEU A HD21 1 
ATOM   857   H  HD22 . LEU A 1 55  ? 8.715   10.846  27.016  1.00 14.91  ?  278  LEU A HD22 1 
ATOM   858   H  HD23 . LEU A 1 55  ? 9.195   12.263  27.550  1.00 14.91  ?  278  LEU A HD23 1 
ATOM   859   N  N    . ILE A 1 56  ? 11.064  12.215  22.613  1.00 8.12   ?  279  ILE A N    1 
ATOM   860   C  CA   . ILE A 1 56  ? 11.271  12.688  21.245  1.00 9.21   ?  279  ILE A CA   1 
ATOM   861   C  C    . ILE A 1 56  ? 11.917  11.567  20.435  1.00 8.65   ?  279  ILE A C    1 
ATOM   862   O  O    . ILE A 1 56  ? 13.008  11.102  20.781  1.00 7.57   ?  279  ILE A O    1 
ATOM   863   C  CB   . ILE A 1 56  ? 12.144  13.960  21.223  1.00 12.24  ?  279  ILE A CB   1 
ATOM   864   C  CG1  . ILE A 1 56  ? 11.473  15.114  21.971  1.00 13.21  ?  279  ILE A CG1  1 
ATOM   865   C  CG2  . ILE A 1 56  ? 12.469  14.352  19.783  1.00 13.76  ?  279  ILE A CG2  1 
ATOM   866   C  CD1  . ILE A 1 56  ? 12.266  16.399  21.953  1.00 13.36  ?  279  ILE A CD1  1 
ATOM   867   H  H    . ILE A 1 56  ? 11.768  12.272  23.104  1.00 9.75   ?  279  ILE A H    1 
ATOM   868   H  HA   . ILE A 1 56  ? 10.412  12.891  20.844  1.00 11.06  ?  279  ILE A HA   1 
ATOM   869   H  HB   . ILE A 1 56  ? 12.974  13.763  21.686  1.00 14.69  ?  279  ILE A HB   1 
ATOM   870   H  HG12 . ILE A 1 56  ? 10.612  15.292  21.561  1.00 15.86  ?  279  ILE A HG12 1 
ATOM   871   H  HG13 . ILE A 1 56  ? 11.351  14.855  22.898  1.00 15.86  ?  279  ILE A HG13 1 
ATOM   872   H  HG21 . ILE A 1 56  ? 12.688  15.296  19.754  1.00 16.52  ?  279  ILE A HG21 1 
ATOM   873   H  HG22 . ILE A 1 56  ? 13.226  13.828  19.476  1.00 16.52  ?  279  ILE A HG22 1 
ATOM   874   H  HG23 . ILE A 1 56  ? 11.696  14.174  19.225  1.00 16.52  ?  279  ILE A HG23 1 
ATOM   875   H  HD11 . ILE A 1 56  ? 11.945  16.978  22.661  1.00 16.04  ?  279  ILE A HD11 1 
ATOM   876   H  HD12 . ILE A 1 56  ? 13.203  16.193  22.093  1.00 16.04  ?  279  ILE A HD12 1 
ATOM   877   H  HD13 . ILE A 1 56  ? 12.147  16.831  21.093  1.00 16.04  ?  279  ILE A HD13 1 
ATOM   878   N  N    . THR A 1 57  ? 11.280  11.167  19.327  1.00 9.15   ?  280  THR A N    1 
ATOM   879   C  CA   A THR A 1 57  ? 11.832  10.146  18.440  0.48 9.65   ?  280  THR A CA   1 
ATOM   880   C  CA   B THR A 1 57  ? 11.867  10.104  18.519  0.52 9.54   ?  280  THR A CA   1 
ATOM   881   C  C    . THR A 1 57  ? 13.265  10.479  18.054  1.00 8.33   ?  280  THR A C    1 
ATOM   882   O  O    . THR A 1 57  ? 14.185  9.654   18.147  1.00 8.96   ?  280  THR A O    1 
ATOM   883   C  CB   A THR A 1 57  ? 10.967  10.103  17.171  0.48 11.43  ?  280  THR A CB   1 
ATOM   884   C  CB   B THR A 1 57  ? 10.989  9.713   17.329  0.52 11.01  ?  280  THR A CB   1 
ATOM   885   O  OG1  A THR A 1 57  ? 10.728  11.447  16.697  0.48 12.02  ?  280  THR A OG1  1 
ATOM   886   O  OG1  B THR A 1 57  ? 9.837   9.008   17.800  0.52 11.91  ?  280  THR A OG1  1 
ATOM   887   C  CG2  A THR A 1 57  ? 9.636   9.428   17.435  0.48 11.99  ?  280  THR A CG2  1 
ATOM   888   C  CG2  B THR A 1 57  ? 11.763  8.800   16.361  0.52 11.19  ?  280  THR A CG2  1 
ATOM   889   H  H    A THR A 1 57  ? 10.521  11.476  19.067  0.48 10.98  ?  280  THR A H    1 
ATOM   890   H  H    B THR A 1 57  ? 10.536  11.486  19.036  0.52 10.98  ?  280  THR A H    1 
ATOM   891   H  HA   A THR A 1 57  ? 11.822  9.285   18.886  0.48 11.58  ?  280  THR A HA   1 
ATOM   892   H  HA   B THR A 1 57  ? 11.920  9.316   19.082  0.52 11.45  ?  280  THR A HA   1 
ATOM   893   H  HB   A THR A 1 57  ? 11.436  9.593   16.492  0.48 13.72  ?  280  THR A HB   1 
ATOM   894   H  HB   B THR A 1 57  ? 10.718  10.514  16.853  0.52 13.21  ?  280  THR A HB   1 
ATOM   895   H  HG1  A THR A 1 57  ? 10.244  11.427  16.011  0.48 14.42  ?  280  THR A HG1  1 
ATOM   896   H  HG1  B THR A 1 57  ? 9.355   8.779   17.151  0.52 14.29  ?  280  THR A HG1  1 
ATOM   897   H  HG21 A THR A 1 57  ? 9.087   9.454   16.636  0.48 14.39  ?  280  THR A HG21 1 
ATOM   898   H  HG21 B THR A 1 57  ? 11.143  8.328   15.783  0.52 13.43  ?  280  THR A HG21 1 
ATOM   899   H  HG22 A THR A 1 57  ? 9.778   8.503   17.689  0.48 14.39  ?  280  THR A HG22 1 
ATOM   900   H  HG22 B THR A 1 57  ? 12.363  9.330   15.813  0.52 13.43  ?  280  THR A HG22 1 
ATOM   901   H  HG23 A THR A 1 57  ? 9.170   9.884   18.153  0.48 14.39  ?  280  THR A HG23 1 
ATOM   902   H  HG23 B THR A 1 57  ? 12.284  8.151   16.860  0.52 13.43  ?  280  THR A HG23 1 
ATOM   903   N  N    . SER A 1 58  ? 13.456  11.711  17.594  1.00 9.22   ?  281  SER A N    1 
ATOM   904   C  CA   A SER A 1 58  ? 14.730  12.128  17.028  0.68 10.31  ?  281  SER A CA   1 
ATOM   905   C  CA   B SER A 1 58  ? 14.737  12.109  17.027  0.32 10.56  ?  281  SER A CA   1 
ATOM   906   C  C    . SER A 1 58  ? 15.856  12.155  18.057  1.00 10.66  ?  281  SER A C    1 
ATOM   907   O  O    . SER A 1 58  ? 17.018  12.207  17.660  1.00 13.99  ?  281  SER A O    1 
ATOM   908   C  CB   A SER A 1 58  ? 14.534  13.486  16.345  0.68 10.94  ?  281  SER A CB   1 
ATOM   909   C  CB   B SER A 1 58  ? 14.619  13.450  16.292  0.32 11.76  ?  281  SER A CB   1 
ATOM   910   O  OG   A SER A 1 58  ? 13.456  13.462  15.399  0.68 11.57  ?  281  SER A OG   1 
ATOM   911   O  OG   B SER A 1 58  ? 14.313  14.529  17.158  0.32 12.76  ?  281  SER A OG   1 
ATOM   912   H  H    A SER A 1 58  ? 12.858  12.329  17.598  0.68 11.06  ?  281  SER A H    1 
ATOM   913   H  H    B SER A 1 58  ? 12.861  12.332  17.599  0.32 11.06  ?  281  SER A H    1 
ATOM   914   H  HA   A SER A 1 58  ? 15.021  11.502  16.347  0.68 12.37  ?  281  SER A HA   1 
ATOM   915   H  HA   B SER A 1 58  ? 14.989  11.451  16.360  0.32 12.67  ?  281  SER A HA   1 
ATOM   916   H  HB2  A SER A 1 58  ? 14.337  14.150  17.025  0.68 13.12  ?  281  SER A HB2  1 
ATOM   917   H  HB2  B SER A 1 58  ? 15.465  13.636  15.855  0.32 14.11  ?  281  SER A HB2  1 
ATOM   918   H  HB3  A SER A 1 58  ? 15.351  13.720  15.879  0.68 13.12  ?  281  SER A HB3  1 
ATOM   919   H  HB3  B SER A 1 58  ? 13.914  13.377  15.630  0.32 14.11  ?  281  SER A HB3  1 
ATOM   920   H  HG   A SER A 1 58  ? 13.612  12.895  14.800  0.68 13.88  ?  281  SER A HG   1 
ATOM   921   H  HG   B SER A 1 58  ? 14.922  14.620  17.729  0.32 15.31  ?  281  SER A HG   1 
ATOM   922   N  N    . ASN A 1 59  ? 15.550  12.103  19.359  1.00 8.44   ?  282  ASN A N    1 
ATOM   923   C  CA   . ASN A 1 59  ? 16.579  12.069  20.393  1.00 7.56   ?  282  ASN A CA   1 
ATOM   924   C  C    . ASN A 1 59  ? 16.980  10.660  20.805  1.00 6.20   ?  282  ASN A C    1 
ATOM   925   O  O    . ASN A 1 59  ? 17.919  10.505  21.586  1.00 7.33   ?  282  ASN A O    1 
ATOM   926   C  CB   . ASN A 1 59  ? 16.165  12.899  21.598  1.00 9.27   ?  282  ASN A CB   1 
ATOM   927   C  CG   . ASN A 1 59  ? 16.411  14.389  21.377  1.00 10.33  ?  282  ASN A CG   1 
ATOM   928   O  OD1  . ASN A 1 59  ? 16.917  14.803  20.337  1.00 12.17  ?  282  ASN A OD1  1 
ATOM   929   N  ND2  . ASN A 1 59  ? 16.062  15.185  22.354  1.00 10.57  ?  282  ASN A ND2  1 
ATOM   930   H  H    . ASN A 1 59  ? 14.747  12.087  19.666  1.00 10.13  ?  282  ASN A H    1 
ATOM   931   H  HA   . ASN A 1 59  ? 17.379  12.488  20.037  1.00 9.07   ?  282  ASN A HA   1 
ATOM   932   H  HB2  . ASN A 1 59  ? 15.218  12.770  21.765  1.00 11.13  ?  282  ASN A HB2  1 
ATOM   933   H  HB3  . ASN A 1 59  ? 16.679  12.618  22.371  1.00 11.13  ?  282  ASN A HB3  1 
ATOM   934   H  HD21 . ASN A 1 59  ? 16.180  16.034  22.280  1.00 12.68  ?  282  ASN A HD21 1 
ATOM   935   H  HD22 . ASN A 1 59  ? 15.716  14.860  23.071  1.00 12.68  ?  282  ASN A HD22 1 
ATOM   936   N  N    . ILE A 1 60  ? 16.321  9.635   20.283  1.00 6.07   ?  283  ILE A N    1 
ATOM   937   C  CA   . ILE A 1 60  ? 16.721  8.270   20.591  1.00 6.27   ?  283  ILE A CA   1 
ATOM   938   C  C    . ILE A 1 60  ? 18.055  7.973   19.922  1.00 5.53   ?  283  ILE A C    1 
ATOM   939   O  O    . ILE A 1 60  ? 18.213  8.163   18.710  1.00 6.02   ?  283  ILE A O    1 
ATOM   940   C  CB   . ILE A 1 60  ? 15.648  7.282   20.118  1.00 6.52   ?  283  ILE A CB   1 
ATOM   941   C  CG1  . ILE A 1 60  ? 14.273  7.597   20.720  1.00 6.93   ?  283  ILE A CG1  1 
ATOM   942   C  CG2  . ILE A 1 60  ? 16.080  5.858   20.440  1.00 7.36   ?  283  ILE A CG2  1 
ATOM   943   C  CD1  . ILE A 1 60  ? 13.130  6.854   20.063  1.00 7.86   ?  283  ILE A CD1  1 
ATOM   944   H  H    . ILE A 1 60  ? 15.646  9.701   19.754  1.00 7.28   ?  283  ILE A H    1 
ATOM   945   H  HA   . ILE A 1 60  ? 16.827  8.180   21.551  1.00 7.53   ?  283  ILE A HA   1 
ATOM   946   H  HB   . ILE A 1 60  ? 15.557  7.374   19.157  1.00 7.83   ?  283  ILE A HB   1 
ATOM   947   H  HG12 . ILE A 1 60  ? 14.282  7.354   21.659  1.00 8.31   ?  283  ILE A HG12 1 
ATOM   948   H  HG13 . ILE A 1 60  ? 14.102  8.547   20.625  1.00 8.31   ?  283  ILE A HG13 1 
ATOM   949   H  HG21 . ILE A 1 60  ? 15.329  5.261   20.303  1.00 8.83   ?  283  ILE A HG21 1 
ATOM   950   H  HG22 . ILE A 1 60  ? 16.812  5.610   19.853  1.00 8.83   ?  283  ILE A HG22 1 
ATOM   951   H  HG23 . ILE A 1 60  ? 16.370  5.818   21.365  1.00 8.83   ?  283  ILE A HG23 1 
ATOM   952   H  HD11 . ILE A 1 60  ? 12.291  7.204   20.401  1.00 9.44   ?  283  ILE A HD11 1 
ATOM   953   H  HD12 . ILE A 1 60  ? 13.179  6.984   19.103  1.00 9.44   ?  283  ILE A HD12 1 
ATOM   954   H  HD13 . ILE A 1 60  ? 13.204  5.910   20.274  1.00 9.44   ?  283  ILE A HD13 1 
ATOM   955   N  N    . CYS A 1 61  ? 19.017  7.489   20.700  1.00 6.02   ?  284  CYS A N    1 
ATOM   956   C  CA   . CYS A 1 61  ? 20.377  7.226   20.226  1.00 6.34   ?  284  CYS A CA   1 
ATOM   957   C  C    . CYS A 1 61  ? 21.095  8.485   19.742  1.00 6.57   ?  284  CYS A C    1 
ATOM   958   O  O    . CYS A 1 61  ? 22.035  8.400   18.959  1.00 7.09   ?  284  CYS A O    1 
ATOM   959   C  CB   . CYS A 1 61  ? 20.447  6.107   19.181  1.00 6.38   ?  284  CYS A CB   1 
ATOM   960   S  SG   . CYS A 1 61  ? 20.171  4.455   19.858  1.00 6.89   ?  284  CYS A SG   1 
ATOM   961   H  H    . CYS A 1 61  ? 18.905  7.298   21.531  1.00 7.22   ?  284  CYS A H    1 
ATOM   962   H  HA   . CYS A 1 61  ? 20.877  6.902   20.992  1.00 7.61   ?  284  CYS A HA   1 
ATOM   963   H  HB2  . CYS A 1 61  ? 19.768  6.268   18.508  1.00 7.66   ?  284  CYS A HB2  1 
ATOM   964   H  HB3  . CYS A 1 61  ? 21.327  6.117   18.774  1.00 7.66   ?  284  CYS A HB3  1 
ATOM   965   H  HG   . CYS A 1 61  ? 20.272  3.649   18.975  1.00 8.27   ?  284  CYS A HG   1 
ATOM   966   N  N    . SER A 1 62  ? 20.676  9.646   20.224  1.00 5.95   ?  285  SER A N    1 
ATOM   967   C  CA   A SER A 1 62  ? 21.368  10.896  19.979  0.75 6.27   ?  285  SER A CA   1 
ATOM   968   C  CA   B SER A 1 62  ? 21.341  10.913  19.991  0.25 6.75   ?  285  SER A CA   1 
ATOM   969   C  C    . SER A 1 62  ? 22.081  11.328  21.252  1.00 6.67   ?  285  SER A C    1 
ATOM   970   O  O    . SER A 1 62  ? 21.674  10.986  22.364  1.00 9.23   ?  285  SER A O    1 
ATOM   971   C  CB   A SER A 1 62  ? 20.374  11.975  19.546  0.75 6.97   ?  285  SER A CB   1 
ATOM   972   C  CB   B SER A 1 62  ? 20.309  12.000  19.710  0.25 7.82   ?  285  SER A CB   1 
ATOM   973   O  OG   A SER A 1 62  ? 20.979  13.235  19.279  0.75 6.82   ?  285  SER A OG   1 
ATOM   974   O  OG   B SER A 1 62  ? 19.720  12.431  20.934  0.25 8.60   ?  285  SER A OG   1 
ATOM   975   H  H    A SER A 1 62  ? 19.973  9.735   20.710  0.75 7.15   ?  285  SER A H    1 
ATOM   976   H  H    B SER A 1 62  ? 19.974  9.727   20.714  0.25 7.15   ?  285  SER A H    1 
ATOM   977   H  HA   A SER A 1 62  ? 22.029  10.791  19.276  0.75 7.53   ?  285  SER A HA   1 
ATOM   978   H  HA   B SER A 1 62  ? 21.954  10.827  19.244  0.25 8.10   ?  285  SER A HA   1 
ATOM   979   H  HB2  A SER A 1 62  ? 19.930  11.673  18.738  0.75 8.36   ?  285  SER A HB2  1 
ATOM   980   H  HB2  B SER A 1 62  ? 20.745  12.753  19.281  0.25 9.39   ?  285  SER A HB2  1 
ATOM   981   H  HB3  A SER A 1 62  ? 19.724  12.093  20.257  0.75 8.36   ?  285  SER A HB3  1 
ATOM   982   H  HB3  B SER A 1 62  ? 19.618  11.643  19.130  0.25 9.39   ?  285  SER A HB3  1 
ATOM   983   H  HG   A SER A 1 62  ? 21.537  13.159  18.655  0.75 8.18   ?  285  SER A HG   1 
ATOM   984   H  HG   B SER A 1 62  ? 19.343  11.785  21.315  0.25 10.32  ?  285  SER A HG   1 
ATOM   985   N  N    . PHE A 1 63  ? 23.161  12.083  21.069  1.00 5.84   ?  286  PHE A N    1 
ATOM   986   C  CA   . PHE A 1 63  ? 23.871  12.728  22.158  1.00 6.65   ?  286  PHE A CA   1 
ATOM   987   C  C    . PHE A 1 63  ? 24.086  14.191  21.808  1.00 6.66   ?  286  PHE A C    1 
ATOM   988   O  O    . PHE A 1 63  ? 24.230  14.547  20.629  1.00 6.89   ?  286  PHE A O    1 
ATOM   989   C  CB   . PHE A 1 63  ? 25.267  12.147  22.362  1.00 6.63   ?  286  PHE A CB   1 
ATOM   990   C  CG   . PHE A 1 63  ? 25.287  10.723  22.849  1.00 7.52   ?  286  PHE A CG   1 
ATOM   991   C  CD1  . PHE A 1 63  ? 24.914  10.415  24.141  1.00 7.54   ?  286  PHE A CD1  1 
ATOM   992   C  CD2  . PHE A 1 63  ? 25.748  9.705   22.035  1.00 8.69   ?  286  PHE A CD2  1 
ATOM   993   C  CE1  . PHE A 1 63  ? 24.978  9.117   24.620  1.00 8.40   ?  286  PHE A CE1  1 
ATOM   994   C  CE2  . PHE A 1 63  ? 25.806  8.397   22.496  1.00 9.68   ?  286  PHE A CE2  1 
ATOM   995   C  CZ   . PHE A 1 63  ? 25.438  8.109   23.793  1.00 8.79   ?  286  PHE A CZ   1 
ATOM   996   H  H    . PHE A 1 63  ? 23.508  12.239  20.298  1.00 7.01   ?  286  PHE A H    1 
ATOM   997   H  HA   . PHE A 1 63  ? 23.343  12.624  22.965  1.00 7.98   ?  286  PHE A HA   1 
ATOM   998   H  HB2  . PHE A 1 63  ? 25.739  12.173  21.516  1.00 7.95   ?  286  PHE A HB2  1 
ATOM   999   H  HB3  . PHE A 1 63  ? 25.733  12.687  23.019  1.00 7.95   ?  286  PHE A HB3  1 
ATOM   1000  H  HD1  . PHE A 1 63  ? 24.614  11.094  24.702  1.00 9.04   ?  286  PHE A HD1  1 
ATOM   1001  H  HD2  . PHE A 1 63  ? 26.023  9.899   21.168  1.00 10.43  ?  286  PHE A HD2  1 
ATOM   1002  H  HE1  . PHE A 1 63  ? 24.714  8.924   25.491  1.00 10.08  ?  286  PHE A HE1  1 
ATOM   1003  H  HE2  . PHE A 1 63  ? 26.092  7.717   21.930  1.00 11.61  ?  286  PHE A HE2  1 
ATOM   1004  H  HZ   . PHE A 1 63  ? 25.500  7.238   24.112  1.00 10.55  ?  286  PHE A HZ   1 
ATOM   1005  N  N    . ARG A 1 64  ? 24.136  15.039  22.820  1.00 6.38   ?  287  ARG A N    1 
ATOM   1006  C  CA   A ARG A 1 64  ? 24.532  16.429  22.641  0.41 6.98   ?  287  ARG A CA   1 
ATOM   1007  C  CA   B ARG A 1 64  ? 24.575  16.413  22.613  0.59 6.85   ?  287  ARG A CA   1 
ATOM   1008  C  C    . ARG A 1 64  ? 25.471  16.823  23.773  1.00 6.59   ?  287  ARG A C    1 
ATOM   1009  O  O    . ARG A 1 64  ? 25.445  16.228  24.848  1.00 7.32   ?  287  ARG A O    1 
ATOM   1010  C  CB   A ARG A 1 64  ? 23.323  17.367  22.587  0.41 9.34   ?  287  ARG A CB   1 
ATOM   1011  C  CB   B ARG A 1 64  ? 23.419  17.392  22.325  0.59 9.28   ?  287  ARG A CB   1 
ATOM   1012  C  CG   A ARG A 1 64  ? 22.501  17.404  23.852  0.41 11.04  ?  287  ARG A CG   1 
ATOM   1013  C  CG   B ARG A 1 64  ? 22.727  18.026  23.523  0.59 10.05  ?  287  ARG A CG   1 
ATOM   1014  C  CD   A ARG A 1 64  ? 21.390  18.428  23.759  0.41 12.38  ?  287  ARG A CD   1 
ATOM   1015  C  CD   B ARG A 1 64  ? 22.101  16.987  24.426  0.59 11.32  ?  287  ARG A CD   1 
ATOM   1016  N  NE   A ARG A 1 64  ? 21.891  19.784  23.581  0.41 13.70  ?  287  ARG A NE   1 
ATOM   1017  N  NE   B ARG A 1 64  ? 21.198  16.106  23.702  0.59 11.67  ?  287  ARG A NE   1 
ATOM   1018  C  CZ   A ARG A 1 64  ? 21.132  20.872  23.545  0.41 14.51  ?  287  ARG A CZ   1 
ATOM   1019  C  CZ   B ARG A 1 64  ? 20.488  15.142  24.263  0.59 12.02  ?  287  ARG A CZ   1 
ATOM   1020  N  NH1  A ARG A 1 64  ? 19.818  20.809  23.707  0.41 14.35  ?  287  ARG A NH1  1 
ATOM   1021  N  NH1  B ARG A 1 64  ? 20.488  14.960  25.577  0.59 12.24  ?  287  ARG A NH1  1 
ATOM   1022  N  NH2  A ARG A 1 64  ? 21.704  22.053  23.343  0.41 15.39  ?  287  ARG A NH2  1 
ATOM   1023  N  NH2  B ARG A 1 64  ? 19.737  14.369  23.496  0.59 12.85  ?  287  ARG A NH2  1 
ATOM   1024  H  H    A ARG A 1 64  ? 23.943  14.833  23.632  0.41 7.66   ?  287  ARG A H    1 
ATOM   1025  H  H    B ARG A 1 64  ? 23.923  14.847  23.631  0.59 7.66   ?  287  ARG A H    1 
ATOM   1026  H  HA   A ARG A 1 64  ? 25.011  16.525  21.803  0.41 8.38   ?  287  ARG A HA   1 
ATOM   1027  H  HA   B ARG A 1 64  ? 25.126  16.468  21.817  0.59 8.22   ?  287  ARG A HA   1 
ATOM   1028  H  HB2  A ARG A 1 64  ? 23.639  18.269  22.418  0.41 11.21  ?  287  ARG A HB2  1 
ATOM   1029  H  HB2  B ARG A 1 64  ? 23.770  18.118  21.786  0.59 11.14  ?  287  ARG A HB2  1 
ATOM   1030  H  HB3  A ARG A 1 64  ? 22.740  17.079  21.867  0.41 11.21  ?  287  ARG A HB3  1 
ATOM   1031  H  HB3  B ARG A 1 64  ? 22.737  16.911  21.830  0.59 11.14  ?  287  ARG A HB3  1 
ATOM   1032  H  HG2  A ARG A 1 64  ? 22.101  16.533  24.001  0.41 13.25  ?  287  ARG A HG2  1 
ATOM   1033  H  HG2  B ARG A 1 64  ? 23.378  18.525  24.041  0.59 12.07  ?  287  ARG A HG2  1 
ATOM   1034  H  HG3  A ARG A 1 64  ? 23.072  17.640  24.600  0.41 13.25  ?  287  ARG A HG3  1 
ATOM   1035  H  HG3  B ARG A 1 64  ? 22.026  18.620  23.211  0.59 12.07  ?  287  ARG A HG3  1 
ATOM   1036  H  HD2  A ARG A 1 64  ? 20.825  18.214  23.000  0.41 14.85  ?  287  ARG A HD2  1 
ATOM   1037  H  HD2  B ARG A 1 64  ? 22.801  16.444  24.821  0.59 13.58  ?  287  ARG A HD2  1 
ATOM   1038  H  HD3  A ARG A 1 64  ? 20.869  18.405  24.577  0.41 14.85  ?  287  ARG A HD3  1 
ATOM   1039  H  HD3  B ARG A 1 64  ? 21.594  17.433  25.122  0.59 13.58  ?  287  ARG A HD3  1 
ATOM   1040  H  HE   A ARG A 1 64  ? 22.741  19.887  23.493  0.41 16.44  ?  287  ARG A HE   1 
ATOM   1041  H  HE   B ARG A 1 64  ? 21.121  16.219  22.853  0.59 14.01  ?  287  ARG A HE   1 
ATOM   1042  H  HH11 A ARG A 1 64  ? 19.437  20.050  23.840  0.41 17.22  ?  287  ARG A HH11 1 
ATOM   1043  H  HH11 B ARG A 1 64  ? 20.956  15.475  26.082  0.59 14.69  ?  287  ARG A HH11 1 
ATOM   1044  H  HH12 A ARG A 1 64  ? 19.347  21.528  23.680  0.41 17.22  ?  287  ARG A HH12 1 
ATOM   1045  H  HH12 B ARG A 1 64  ? 20.020  14.327  25.923  0.59 14.69  ?  287  ARG A HH12 1 
ATOM   1046  H  HH21 A ARG A 1 64  ? 22.556  22.106  23.238  0.41 18.47  ?  287  ARG A HH21 1 
ATOM   1047  H  HH21 B ARG A 1 64  ? 19.270  13.738  23.847  0.59 15.42  ?  287  ARG A HH21 1 
ATOM   1048  H  HH22 A ARG A 1 64  ? 21.223  22.765  23.318  0.41 18.47  ?  287  ARG A HH22 1 
ATOM   1049  H  HH22 B ARG A 1 64  ? 19.715  14.498  22.646  0.59 15.42  ?  287  ARG A HH22 1 
ATOM   1050  N  N    . GLY A 1 65  ? 26.309  17.821  23.511  1.00 6.43   ?  288  GLY A N    1 
ATOM   1051  C  CA   . GLY A 1 65  ? 27.250  18.315  24.493  1.00 6.55   ?  288  GLY A CA   1 
ATOM   1052  C  C    . GLY A 1 65  ? 28.357  19.047  23.776  1.00 7.00   ?  288  GLY A C    1 
ATOM   1053  O  O    . GLY A 1 65  ? 28.079  19.950  22.994  1.00 7.45   ?  288  GLY A O    1 
ATOM   1054  H  H    . GLY A 1 65  ? 26.348  18.233  22.757  1.00 7.72   ?  288  GLY A H    1 
ATOM   1055  H  HA2  . GLY A 1 65  ? 26.807  18.922  25.106  1.00 7.86   ?  288  GLY A HA2  1 
ATOM   1056  H  HA3  . GLY A 1 65  ? 27.627  17.576  24.997  1.00 7.86   ?  288  GLY A HA3  1 
ATOM   1057  N  N    . SER A 1 66  ? 29.604  18.655  24.011  1.00 7.72   ?  289  SER A N    1 
ATOM   1058  C  CA   A SER A 1 66  ? 30.721  19.335  23.376  0.75 8.07   ?  289  SER A CA   1 
ATOM   1059  C  CA   B SER A 1 66  ? 30.740  19.361  23.430  0.25 7.96   ?  289  SER A CA   1 
ATOM   1060  C  C    . SER A 1 66  ? 31.923  18.409  23.341  1.00 7.48   ?  289  SER A C    1 
ATOM   1061  O  O    . SER A 1 66  ? 32.072  17.522  24.176  1.00 8.48   ?  289  SER A O    1 
ATOM   1062  C  CB   A SER A 1 66  ? 31.059  20.635  24.114  0.75 8.91   ?  289  SER A CB   1 
ATOM   1063  C  CB   B SER A 1 66  ? 31.136  20.578  24.282  0.25 8.72   ?  289  SER A CB   1 
ATOM   1064  O  OG   A SER A 1 66  ? 31.311  20.379  25.478  0.75 10.68  ?  289  SER A OG   1 
ATOM   1065  O  OG   B SER A 1 66  ? 30.121  21.567  24.312  0.25 9.69   ?  289  SER A OG   1 
ATOM   1066  H  H    A SER A 1 66  ? 29.825  18.005  24.528  0.75 9.27   ?  289  SER A H    1 
ATOM   1067  H  H    B SER A 1 66  ? 29.819  17.983  24.503  0.25 9.27   ?  289  SER A H    1 
ATOM   1068  H  HA   A SER A 1 66  ? 30.491  19.548  22.458  0.75 9.68   ?  289  SER A HA   1 
ATOM   1069  H  HA   B SER A 1 66  ? 30.505  19.658  22.537  0.25 9.56   ?  289  SER A HA   1 
ATOM   1070  H  HB2  A SER A 1 66  ? 31.850  21.030  23.714  0.75 10.69  ?  289  SER A HB2  1 
ATOM   1071  H  HB2  B SER A 1 66  ? 31.305  20.280  25.190  0.25 10.46  ?  289  SER A HB2  1 
ATOM   1072  H  HB3  A SER A 1 66  ? 30.310  21.246  24.039  0.75 10.69  ?  289  SER A HB3  1 
ATOM   1073  H  HB3  B SER A 1 66  ? 31.940  20.971  23.907  0.25 10.46  ?  289  SER A HB3  1 
ATOM   1074  H  HG   A SER A 1 66  ? 31.967  19.860  25.556  0.75 12.82  ?  289  SER A HG   1 
ATOM   1075  H  HG   B SER A 1 66  ? 30.356  22.207  24.802  0.25 11.64  ?  289  SER A HG   1 
ATOM   1076  N  N    . ILE A 1 67  ? 32.762  18.620  22.336  1.00 7.41   ?  290  ILE A N    1 
ATOM   1077  C  CA   . ILE A 1 67  ? 34.036  17.921  22.245  1.00 7.19   ?  290  ILE A CA   1 
ATOM   1078  C  C    . ILE A 1 67  ? 35.058  18.682  23.078  1.00 8.20   ?  290  ILE A C    1 
ATOM   1079  O  O    . ILE A 1 67  ? 35.150  19.912  23.004  1.00 7.88   ?  290  ILE A O    1 
ATOM   1080  C  CB   . ILE A 1 67  ? 34.494  17.798  20.786  1.00 7.55   ?  290  ILE A CB   1 
ATOM   1081  C  CG1  . ILE A 1 67  ? 33.514  16.945  19.973  1.00 7.56   ?  290  ILE A CG1  1 
ATOM   1082  C  CG2  . ILE A 1 67  ? 35.909  17.258  20.696  1.00 8.29   ?  290  ILE A CG2  1 
ATOM   1083  C  CD1  . ILE A 1 67  ? 33.396  15.491  20.383  1.00 7.51   ?  290  ILE A CD1  1 
ATOM   1084  H  H    . ILE A 1 67  ? 32.615  19.167  21.688  1.00 8.89   ?  290  ILE A H    1 
ATOM   1085  H  HA   . ILE A 1 67  ? 33.937  17.024  22.601  1.00 8.63   ?  290  ILE A HA   1 
ATOM   1086  H  HB   . ILE A 1 67  ? 34.498  18.688  20.402  1.00 9.06   ?  290  ILE A HB   1 
ATOM   1087  H  HG12 . ILE A 1 67  ? 32.631  17.338  20.055  1.00 9.07   ?  290  ILE A HG12 1 
ATOM   1088  H  HG13 . ILE A 1 67  ? 33.798  16.959  19.046  1.00 9.07   ?  290  ILE A HG13 1 
ATOM   1089  H  HG21 . ILE A 1 67  ? 36.084  16.981  19.783  1.00 9.95   ?  290  ILE A HG21 1 
ATOM   1090  H  HG22 . ILE A 1 67  ? 36.530  17.957  20.955  1.00 9.95   ?  290  ILE A HG22 1 
ATOM   1091  H  HG23 . ILE A 1 67  ? 35.996  16.500  21.294  1.00 9.95   ?  290  ILE A HG23 1 
ATOM   1092  H  HD11 . ILE A 1 67  ? 32.814  15.033  19.758  1.00 9.02   ?  290  ILE A HD11 1 
ATOM   1093  H  HD12 . ILE A 1 67  ? 34.278  15.088  20.372  1.00 9.02   ?  290  ILE A HD12 1 
ATOM   1094  H  HD13 . ILE A 1 67  ? 33.023  15.445  21.277  1.00 9.02   ?  290  ILE A HD13 1 
ATOM   1095  N  N    A SER A 1 68  ? 35.771  17.944  23.927  0.33 9.79   ?  291  SER A N    1 
ATOM   1096  N  N    B SER A 1 68  ? 35.870  17.956  23.847  0.67 9.50   ?  291  SER A N    1 
ATOM   1097  C  CA   A SER A 1 68  ? 36.857  18.465  24.746  0.33 11.98  ?  291  SER A CA   1 
ATOM   1098  C  CA   B SER A 1 68  ? 36.842  18.600  24.721  0.67 12.23  ?  291  SER A CA   1 
ATOM   1099  C  C    A SER A 1 68  ? 38.039  17.507  24.621  0.33 13.68  ?  291  SER A C    1 
ATOM   1100  C  C    B SER A 1 68  ? 38.291  18.334  24.350  0.67 14.50  ?  291  SER A C    1 
ATOM   1101  O  O    A SER A 1 68  ? 38.411  16.777  25.537  0.33 14.08  ?  291  SER A O    1 
ATOM   1102  O  O    B SER A 1 68  ? 39.177  18.976  24.913  0.67 16.77  ?  291  SER A O    1 
ATOM   1103  C  CB   A SER A 1 68  ? 36.440  18.666  26.199  0.33 13.29  ?  291  SER A CB   1 
ATOM   1104  C  CB   B SER A 1 68  ? 36.636  18.162  26.178  0.67 14.05  ?  291  SER A CB   1 
ATOM   1105  O  OG   A SER A 1 68  ? 36.004  17.448  26.767  0.33 14.22  ?  291  SER A OG   1 
ATOM   1106  O  OG   B SER A 1 68  ? 36.990  16.805  26.343  0.67 16.35  ?  291  SER A OG   1 
ATOM   1107  H  H    A SER A 1 68  ? 35.636  17.104  24.049  0.33 11.75  ?  291  SER A H    1 
ATOM   1108  H  H    B SER A 1 68  ? 35.875  17.097  23.877  0.67 11.40  ?  291  SER A H    1 
ATOM   1109  H  HA   A SER A 1 68  ? 37.121  19.337  24.411  0.33 14.38  ?  291  SER A HA   1 
ATOM   1110  H  HA   B SER A 1 68  ? 36.690  19.557  24.663  0.67 14.68  ?  291  SER A HA   1 
ATOM   1111  H  HB2  A SER A 1 68  ? 37.200  18.996  26.703  0.33 15.95  ?  291  SER A HB2  1 
ATOM   1112  H  HB2  B SER A 1 68  ? 37.194  18.707  26.755  0.67 16.86  ?  291  SER A HB2  1 
ATOM   1113  H  HB3  A SER A 1 68  ? 35.715  19.309  26.233  0.33 15.95  ?  291  SER A HB3  1 
ATOM   1114  H  HB3  B SER A 1 68  ? 35.703  18.277  26.415  0.67 16.86  ?  291  SER A HB3  1 
ATOM   1115  H  HG   A SER A 1 68  ? 35.335  17.159  26.349  0.33 17.06  ?  291  SER A HG   1 
ATOM   1116  H  HG   B SER A 1 68  ? 36.962  16.597  27.156  0.67 19.62  ?  291  SER A HG   1 
ATOM   1117  N  N    . GLY A 1 69  ? 38.557  17.441  23.411  1.00 14.80  ?  292  GLY A N    1 
ATOM   1118  C  CA   . GLY A 1 69  ? 39.900  16.978  23.176  1.00 16.46  ?  292  GLY A CA   1 
ATOM   1119  C  C    . GLY A 1 69  ? 39.966  15.825  22.209  1.00 15.67  ?  292  GLY A C    1 
ATOM   1120  O  O    . GLY A 1 69  ? 38.994  15.120  21.979  1.00 12.12  ?  292  GLY A O    1 
ATOM   1121  H  H    A GLY A 1 69  ? 38.139  17.665  22.693  0.33 17.76  ?  292  GLY A H    1 
ATOM   1122  H  H    B GLY A 1 69  ? 37.968  17.088  22.894  0.67 17.76  ?  292  GLY A H    1 
ATOM   1123  H  HA2  . GLY A 1 69  ? 40.429  17.707  22.816  1.00 19.75  ?  292  GLY A HA2  1 
ATOM   1124  H  HA3  . GLY A 1 69  ? 40.289  16.691  24.017  1.00 19.75  ?  292  GLY A HA3  1 
ATOM   1125  N  N    . HIS A 1 70  ? 41.140  15.667  21.628  1.00 19.38  ?  293  HIS A N    1 
ATOM   1126  C  CA   . HIS A 1 70  ? 41.486  14.592  20.724  1.00 19.46  ?  293  HIS A CA   1 
ATOM   1127  C  C    . HIS A 1 70  ? 42.193  13.496  21.498  1.00 23.92  ?  293  HIS A C    1 
ATOM   1128  O  O    . HIS A 1 70  ? 43.043  13.768  22.347  1.00 24.52  ?  293  HIS A O    1 
ATOM   1129  C  CB   . HIS A 1 70  ? 42.448  15.183  19.703  1.00 17.61  ?  293  HIS A CB   1 
ATOM   1130  C  CG   . HIS A 1 70  ? 42.923  14.219  18.678  1.00 15.92  ?  293  HIS A CG   1 
ATOM   1131  N  ND1  . HIS A 1 70  ? 44.200  13.708  18.686  1.00 16.20  ?  293  HIS A ND1  1 
ATOM   1132  C  CD2  . HIS A 1 70  ? 42.311  13.702  17.588  1.00 16.52  ?  293  HIS A CD2  1 
ATOM   1133  C  CE1  . HIS A 1 70  ? 44.349  12.900  17.654  1.00 16.58  ?  293  HIS A CE1  1 
ATOM   1134  N  NE2  . HIS A 1 70  ? 43.222  12.888  16.968  1.00 17.04  ?  293  HIS A NE2  1 
ATOM   1135  H  H    . HIS A 1 70  ? 41.798  16.208  21.752  1.00 23.26  ?  293  HIS A H    1 
ATOM   1136  H  HA   . HIS A 1 70  ? 40.708  14.202  20.295  1.00 23.35  ?  293  HIS A HA   1 
ATOM   1137  H  HB2  . HIS A 1 70  ? 42.000  15.908  19.239  1.00 21.14  ?  293  HIS A HB2  1 
ATOM   1138  H  HB3  . HIS A 1 70  ? 43.227  15.521  20.172  1.00 21.14  ?  293  HIS A HB3  1 
ATOM   1139  H  HD1  . HIS A 1 70  ? 44.805  13.887  19.271  1.00 19.44  ?  293  HIS A HD1  1 
ATOM   1140  H  HD2  . HIS A 1 70  ? 41.438  13.867  17.313  1.00 19.83  ?  293  HIS A HD2  1 
ATOM   1141  H  HE1  . HIS A 1 70  ? 45.118  12.419  17.446  1.00 19.90  ?  293  HIS A HE1  1 
ATOM   1142  N  N    . GLU A 1 71  ? 41.834  12.255  21.206  1.00 28.16  ?  294  GLU A N    1 
ATOM   1143  C  CA   . GLU A 1 71  ? 42.512  11.097  21.761  1.00 35.45  ?  294  GLU A CA   1 
ATOM   1144  C  C    . GLU A 1 71  ? 43.051  10.212  20.652  1.00 41.74  ?  294  GLU A C    1 
ATOM   1145  O  O    . GLU A 1 71  ? 43.665  9.177   20.941  1.00 42.61  ?  294  GLU A O    1 
ATOM   1146  C  CB   . GLU A 1 71  ? 41.549  10.273  22.628  1.00 37.12  ?  294  GLU A CB   1 
ATOM   1147  C  CG   . GLU A 1 71  ? 40.504  11.095  23.386  1.00 37.53  ?  294  GLU A CG   1 
ATOM   1148  C  CD   . GLU A 1 71  ? 40.547  10.870  24.889  1.00 37.53  ?  294  GLU A CD   1 
ATOM   1149  O  OE1  . GLU A 1 71  ? 40.953  9.771   25.333  1.00 38.46  ?  294  GLU A OE1  1 
ATOM   1150  O  OE2  . GLU A 1 71  ? 40.179  11.802  25.627  1.00 36.53  -1 294  GLU A OE2  1 
ATOM   1151  H  H    . GLU A 1 71  ? 41.186  12.054  20.678  1.00 33.79  ?  294  GLU A H    1 
ATOM   1152  H  HA   . GLU A 1 71  ? 43.239  11.385  22.335  1.00 42.54  ?  294  GLU A HA   1 
ATOM   1153  H  HB2  . GLU A 1 71  ? 41.072  9.654   22.054  1.00 44.55  ?  294  GLU A HB2  1 
ATOM   1154  H  HB3  . GLU A 1 71  ? 42.068  9.784   23.285  1.00 44.55  ?  294  GLU A HB3  1 
ATOM   1155  H  HG2  . GLU A 1 71  ? 40.663  12.038  23.221  1.00 45.04  ?  294  GLU A HG2  1 
ATOM   1156  H  HG3  . GLU A 1 71  ? 39.620  10.848  23.073  1.00 45.04  ?  294  GLU A HG3  1 
ATOM   1157  N  N    . GLY A 1 72  ? 42.843  10.603  19.397  1.00 47.62  ?  295  GLY A N    1 
ATOM   1158  C  CA   . GLY A 1 72  ? 42.983  9.725   18.260  1.00 15.12  ?  295  GLY A CA   1 
ATOM   1159  C  C    . GLY A 1 72  ? 44.402  9.246   17.996  1.00 46.56  ?  295  GLY A C    1 
ATOM   1160  O  O    . GLY A 1 72  ? 45.249  10.020  17.543  1.00 49.41  ?  295  GLY A O    1 
ATOM   1161  H  H    . GLY A 1 72  ? 42.611  11.401  19.178  1.00 57.14  ?  295  GLY A H    1 
ATOM   1162  H  HA2  . GLY A 1 72  ? 42.429  8.942   18.401  1.00 18.14  ?  295  GLY A HA2  1 
ATOM   1163  H  HA3  . GLY A 1 72  ? 42.676  10.191  17.467  1.00 18.14  ?  295  GLY A HA3  1 
ATOM   1164  N  N    . ASN A 1 73  ? 44.669  7.966   18.256  1.00 60.57  ?  296  ASN A N    1 
ATOM   1165  C  CA   . ASN A 1 73  ? 45.970  7.382   17.947  1.00 72.51  ?  296  ASN A CA   1 
ATOM   1166  C  C    . ASN A 1 73  ? 45.912  6.671   16.599  1.00 68.90  ?  296  ASN A C    1 
ATOM   1167  O  O    . ASN A 1 73  ? 45.544  7.283   15.591  1.00 51.21  ?  296  ASN A O    1 
ATOM   1168  C  CB   . ASN A 1 73  ? 46.404  6.425   19.059  1.00 97.37  ?  296  ASN A CB   1 
ATOM   1169  H  H    . ASN A 1 73  ? 44.112  7.416   18.611  1.00 72.68  ?  296  ASN A H    1 
ATOM   1170  H  HA   . ASN A 1 73  ? 46.641  8.079   17.892  1.00 87.01  ?  296  ASN A HA   1 
ATOM   1171  N  N    . ASP A 1 74  ? 46.274  5.392   16.562  1.00 110.92 ?  297  ASP A N    1 
ATOM   1172  C  CA   . ASP A 1 74  ? 46.259  4.651   15.310  1.00 58.26  ?  297  ASP A CA   1 
ATOM   1173  C  C    . ASP A 1 74  ? 44.817  4.394   14.875  1.00 40.89  ?  297  ASP A C    1 
ATOM   1174  O  O    . ASP A 1 74  ? 43.855  4.715   15.579  1.00 102.36 ?  297  ASP A O    1 
ATOM   1175  C  CB   . ASP A 1 74  ? 47.031  3.343   15.459  1.00 119.84 ?  297  ASP A CB   1 
ATOM   1176  H  H    . ASP A 1 74  ? 46.531  4.936   17.244  1.00 133.10 ?  297  ASP A H    1 
ATOM   1177  H  HA   . ASP A 1 74  ? 46.694  5.180   14.624  1.00 69.91  ?  297  ASP A HA   1 
ATOM   1178  N  N    . ASP A 1 75  ? 44.677  3.809   13.687  1.00 114.37 ?  298  ASP A N    1 
ATOM   1179  C  CA   . ASP A 1 75  ? 43.376  3.518   13.095  1.00 137.74 ?  298  ASP A CA   1 
ATOM   1180  C  C    . ASP A 1 75  ? 42.609  4.781   12.720  1.00 40.80  ?  298  ASP A C    1 
ATOM   1181  O  O    . ASP A 1 75  ? 42.167  4.910   11.574  1.00 49.06  ?  298  ASP A O    1 
ATOM   1182  C  CB   . ASP A 1 75  ? 42.533  2.614   14.001  1.00 82.37  ?  298  ASP A CB   1 
ATOM   1183  C  CG   . ASP A 1 75  ? 42.904  1.150   13.868  1.00 106.80 ?  298  ASP A CG   1 
ATOM   1184  O  OD1  . ASP A 1 75  ? 43.984  0.763   14.362  1.00 91.88  ?  298  ASP A OD1  1 
ATOM   1185  O  OD2  . ASP A 1 75  ? 42.118  0.389   13.263  1.00 121.30 ?  298  ASP A OD2  1 
ATOM   1186  H  H    . ASP A 1 75  ? 45.337  3.565   13.193  1.00 137.25 ?  298  ASP A H    1 
ATOM   1187  H  HA   . ASP A 1 75  ? 43.540  3.033   12.270  1.00 165.29 ?  298  ASP A HA   1 
ATOM   1188  H  HB2  . ASP A 1 75  ? 42.669  2.876   14.925  1.00 98.85  ?  298  ASP A HB2  1 
ATOM   1189  H  HB3  . ASP A 1 75  ? 41.597  2.710   13.763  1.00 98.85  ?  298  ASP A HB3  1 
ATOM   1190  N  N    . GLN A 1 76  ? 42.436  5.721   13.648  1.00 33.43  ?  299  GLN A N    1 
ATOM   1191  C  CA   . GLN A 1 76  ? 41.572  6.850   13.336  1.00 25.68  ?  299  GLN A CA   1 
ATOM   1192  C  C    . GLN A 1 76  ? 41.676  7.941   14.392  1.00 19.88  ?  299  GLN A C    1 
ATOM   1193  O  O    . GLN A 1 76  ? 42.251  7.756   15.468  1.00 21.36  ?  299  GLN A O    1 
ATOM   1194  C  CB   . GLN A 1 76  ? 40.116  6.391   13.223  1.00 25.43  ?  299  GLN A CB   1 
ATOM   1195  C  CG   . GLN A 1 76  ? 39.568  5.755   14.490  1.00 24.91  ?  299  GLN A CG   1 
ATOM   1196  C  CD   . GLN A 1 76  ? 38.065  5.579   14.424  1.00 24.08  ?  299  GLN A CD   1 
ATOM   1197  O  OE1  . GLN A 1 76  ? 37.373  6.336   13.740  1.00 22.98  ?  299  GLN A OE1  1 
ATOM   1198  N  NE2  . GLN A 1 76  ? 37.552  4.569   15.121  1.00 24.09  ?  299  GLN A NE2  1 
ATOM   1199  H  H    . GLN A 1 76  ? 42.793  5.723   14.430  1.00 40.12  ?  299  GLN A H    1 
ATOM   1200  H  HA   . GLN A 1 76  ? 41.888  7.236   12.505  1.00 30.82  ?  299  GLN A HA   1 
ATOM   1201  H  HB2  . GLN A 1 76  ? 39.563  7.160   13.016  1.00 30.52  ?  299  GLN A HB2  1 
ATOM   1202  H  HB3  . GLN A 1 76  ? 40.052  5.735   12.512  1.00 30.52  ?  299  GLN A HB3  1 
ATOM   1203  H  HG2  . GLN A 1 76  ? 39.972  4.881   14.610  1.00 29.90  ?  299  GLN A HG2  1 
ATOM   1204  H  HG3  . GLN A 1 76  ? 39.775  6.322   15.249  1.00 29.90  ?  299  GLN A HG3  1 
ATOM   1205  H  HE21 . GLN A 1 76  ? 38.068  4.056   15.579  1.00 28.91  ?  299  GLN A HE21 1 
ATOM   1206  H  HE22 . GLN A 1 76  ? 36.703  4.430   15.115  1.00 28.91  ?  299  GLN A HE22 1 
ATOM   1207  N  N    . HIS A 1 77  ? 41.069  9.080   14.070  1.00 13.05  ?  300  HIS A N    1 
ATOM   1208  C  CA   . HIS A 1 77  ? 40.919  10.166  15.026  1.00 10.71  ?  300  HIS A CA   1 
ATOM   1209  C  C    . HIS A 1 77  ? 39.774  9.845   15.974  1.00 9.99   ?  300  HIS A C    1 
ATOM   1210  O  O    . HIS A 1 77  ? 38.682  9.456   15.539  1.00 10.36  ?  300  HIS A O    1 
ATOM   1211  C  CB   . HIS A 1 77  ? 40.650  11.476  14.297  1.00 11.26  ?  300  HIS A CB   1 
ATOM   1212  C  CG   . HIS A 1 77  ? 41.825  11.963  13.514  1.00 12.86  ?  300  HIS A CG   1 
ATOM   1213  N  ND1  . HIS A 1 77  ? 42.969  12.436  14.119  1.00 14.46  ?  300  HIS A ND1  1 
ATOM   1214  C  CD2  . HIS A 1 77  ? 42.057  12.009  12.182  1.00 14.83  ?  300  HIS A CD2  1 
ATOM   1215  C  CE1  . HIS A 1 77  ? 43.841  12.785  13.194  1.00 14.95  ?  300  HIS A CE1  1 
ATOM   1216  N  NE2  . HIS A 1 77  ? 43.314  12.534  12.011  1.00 15.87  ?  300  HIS A NE2  1 
ATOM   1217  H  H    . HIS A 1 77  ? 40.733  9.249   13.296  1.00 15.66  ?  300  HIS A H    1 
ATOM   1218  H  HA   . HIS A 1 77  ? 41.733  10.270  15.542  1.00 12.85  ?  300  HIS A HA   1 
ATOM   1219  H  HB2  . HIS A 1 77  ? 39.912  11.347  13.681  1.00 13.51  ?  300  HIS A HB2  1 
ATOM   1220  H  HB3  . HIS A 1 77  ? 40.422  12.157  14.949  1.00 13.51  ?  300  HIS A HB3  1 
ATOM   1221  H  HD1  . HIS A 1 77  ? 43.095  12.494  14.967  1.00 17.36  ?  300  HIS A HD1  1 
ATOM   1222  H  HD2  . HIS A 1 77  ? 41.475  11.736  11.510  1.00 17.80  ?  300  HIS A HD2  1 
ATOM   1223  H  HE1  . HIS A 1 77  ? 44.684  13.146  13.349  1.00 17.94  ?  300  HIS A HE1  1 
ATOM   1224  N  N    A LEU A 1 78  ? 40.036  10.016  17.264  0.99 9.01   ?  301  LEU A N    1 
ATOM   1225  C  CA   A LEU A 1 78  ? 39.087  9.767   18.340  0.99 9.56   ?  301  LEU A CA   1 
ATOM   1226  C  C    A LEU A 1 78  ? 38.968  11.044  19.155  0.99 9.08   ?  301  LEU A C    1 
ATOM   1227  O  O    A LEU A 1 78  ? 39.957  11.755  19.348  0.99 10.47  ?  301  LEU A O    1 
ATOM   1228  C  CB   A LEU A 1 78  ? 39.560  8.637   19.252  0.99 11.46  ?  301  LEU A CB   1 
ATOM   1229  C  CG   A LEU A 1 78  ? 39.851  7.299   18.568  0.99 13.96  ?  301  LEU A CG   1 
ATOM   1230  C  CD1  A LEU A 1 78  ? 40.585  6.410   19.543  0.99 16.12  ?  301  LEU A CD1  1 
ATOM   1231  C  CD2  A LEU A 1 78  ? 38.577  6.639   18.090  0.99 15.99  ?  301  LEU A CD2  1 
ATOM   1232  H  H    A LEU A 1 78  ? 40.797  10.290  17.556  0.99 10.81  ?  301  LEU A H    1 
ATOM   1233  H  HA   A LEU A 1 78  ? 38.224  9.516   17.975  0.99 11.47  ?  301  LEU A HA   1 
ATOM   1234  H  HB2  A LEU A 1 78  ? 40.380  8.922   19.686  0.99 13.75  ?  301  LEU A HB2  1 
ATOM   1235  H  HB3  A LEU A 1 78  ? 38.872  8.476   19.917  0.99 13.75  ?  301  LEU A HB3  1 
ATOM   1236  H  HG   A LEU A 1 78  ? 40.402  7.441   17.782  0.99 16.75  ?  301  LEU A HG   1 
ATOM   1237  H  HD11 A LEU A 1 78  ? 40.748  5.549   19.125  0.99 19.35  ?  301  LEU A HD11 1 
ATOM   1238  H  HD12 A LEU A 1 78  ? 41.428  6.828   19.779  0.99 19.35  ?  301  LEU A HD12 1 
ATOM   1239  H  HD13 A LEU A 1 78  ? 40.040  6.294   20.337  0.99 19.35  ?  301  LEU A HD13 1 
ATOM   1240  H  HD21 A LEU A 1 78  ? 38.797  5.789   17.678  0.99 19.20  ?  301  LEU A HD21 1 
ATOM   1241  H  HD22 A LEU A 1 78  ? 37.991  6.497   18.850  0.99 19.20  ?  301  LEU A HD22 1 
ATOM   1242  H  HD23 A LEU A 1 78  ? 38.145  7.219   17.443  0.99 19.20  ?  301  LEU A HD23 1 
ATOM   1243  N  N    . TRP A 1 79  ? 37.769  11.313  19.656  1.00 8.48   ?  302  TRP A N    1 
ATOM   1244  C  CA   . TRP A 1 79  ? 37.478  12.583  20.300  1.00 8.20   ?  302  TRP A CA   1 
ATOM   1245  C  C    . TRP A 1 79  ? 36.689  12.330  21.573  1.00 7.76   ?  302  TRP A C    1 
ATOM   1246  O  O    . TRP A 1 79  ? 35.811  11.461  21.612  1.00 8.66   ?  302  TRP A O    1 
ATOM   1247  C  CB   . TRP A 1 79  ? 36.678  13.503  19.371  1.00 7.78   ?  302  TRP A CB   1 
ATOM   1248  C  CG   . TRP A 1 79  ? 37.258  13.594  17.987  1.00 7.93   ?  302  TRP A CG   1 
ATOM   1249  C  CD1  . TRP A 1 79  ? 36.990  12.750  16.954  1.00 8.04   ?  302  TRP A CD1  1 
ATOM   1250  C  CD2  . TRP A 1 79  ? 38.214  14.548  17.489  1.00 8.12   ?  302  TRP A CD2  1 
ATOM   1251  N  NE1  . TRP A 1 79  ? 37.704  13.112  15.844  1.00 8.20   ?  302  TRP A NE1  1 
ATOM   1252  C  CE2  . TRP A 1 79  ? 38.474  14.207  16.142  1.00 8.25   ?  302  TRP A CE2  1 
ATOM   1253  C  CE3  . TRP A 1 79  ? 38.880  15.650  18.045  1.00 8.75   ?  302  TRP A CE3  1 
ATOM   1254  C  CZ2  . TRP A 1 79  ? 39.348  14.945  15.340  1.00 9.70   ?  302  TRP A CZ2  1 
ATOM   1255  C  CZ3  . TRP A 1 79  ? 39.749  16.386  17.230  1.00 9.94   ?  302  TRP A CZ3  1 
ATOM   1256  C  CH2  . TRP A 1 79  ? 39.970  16.023  15.902  1.00 10.30  ?  302  TRP A CH2  1 
ATOM   1257  H  H    . TRP A 1 79  ? 37.103  10.770  19.633  1.00 10.17  ?  302  TRP A H    1 
ATOM   1258  H  HA   . TRP A 1 79  ? 38.308  13.027  20.537  1.00 9.85   ?  302  TRP A HA   1 
ATOM   1259  H  HB2  . TRP A 1 79  ? 35.773  13.162  19.294  1.00 9.34   ?  302  TRP A HB2  1 
ATOM   1260  H  HB3  . TRP A 1 79  ? 36.664  14.397  19.748  1.00 9.34   ?  302  TRP A HB3  1 
ATOM   1261  H  HD1  . TRP A 1 79  ? 36.404  12.029  16.997  1.00 9.66   ?  302  TRP A HD1  1 
ATOM   1262  H  HE1  . TRP A 1 79  ? 37.674  12.716  15.081  1.00 9.84   ?  302  TRP A HE1  1 
ATOM   1263  H  HE3  . TRP A 1 79  ? 38.748  15.887  18.934  1.00 10.50  ?  302  TRP A HE3  1 
ATOM   1264  H  HZ2  . TRP A 1 79  ? 39.502  14.710  14.453  1.00 11.64  ?  302  TRP A HZ2  1 
ATOM   1265  H  HZ3  . TRP A 1 79  ? 40.186  17.129  17.580  1.00 11.93  ?  302  TRP A HZ3  1 
ATOM   1266  H  HH2  . TRP A 1 79  ? 40.555  16.528  15.385  1.00 12.36  ?  302  TRP A HH2  1 
ATOM   1267  N  N    . HIS A 1 80  ? 36.986  13.118  22.599  1.00 7.81   ?  303  HIS A N    1 
ATOM   1268  C  CA   . HIS A 1 80  ? 36.292  13.051  23.872  1.00 8.12   ?  303  HIS A CA   1 
ATOM   1269  C  C    . HIS A 1 80  ? 35.047  13.925  23.810  1.00 7.36   ?  303  HIS A C    1 
ATOM   1270  O  O    . HIS A 1 80  ? 35.140  15.143  23.653  1.00 8.43   ?  303  HIS A O    1 
ATOM   1271  C  CB   . HIS A 1 80  ? 37.198  13.542  24.999  1.00 8.85   ?  303  HIS A CB   1 
ATOM   1272  C  CG   . HIS A 1 80  ? 36.559  13.467  26.352  1.00 10.87  ?  303  HIS A CG   1 
ATOM   1273  N  ND1  . HIS A 1 80  ? 36.754  12.415  27.214  1.00 13.63  ?  303  HIS A ND1  1 
ATOM   1274  C  CD2  . HIS A 1 80  ? 35.713  14.316  26.985  1.00 12.54  ?  303  HIS A CD2  1 
ATOM   1275  C  CE1  . HIS A 1 80  ? 36.060  12.617  28.319  1.00 13.41  ?  303  HIS A CE1  1 
ATOM   1276  N  NE2  . HIS A 1 80  ? 35.427  13.770  28.208  1.00 13.27  ?  303  HIS A NE2  1 
ATOM   1277  H  H    . HIS A 1 80  ? 37.604  13.715  22.579  1.00 9.37   ?  303  HIS A H    1 
ATOM   1278  H  HA   . HIS A 1 80  ? 36.031  12.133  24.046  1.00 9.75   ?  303  HIS A HA   1 
ATOM   1279  H  HB2  . HIS A 1 80  ? 37.999  12.995  25.018  1.00 10.62  ?  303  HIS A HB2  1 
ATOM   1280  H  HB3  . HIS A 1 80  ? 37.433  14.468  24.832  1.00 10.62  ?  303  HIS A HB3  1 
ATOM   1281  H  HD1  . HIS A 1 80  ? 37.252  11.731  27.058  1.00 16.36  ?  303  HIS A HD1  1 
ATOM   1282  H  HD2  . HIS A 1 80  ? 35.387  15.120  26.650  1.00 15.05  ?  303  HIS A HD2  1 
ATOM   1283  H  HE1  . HIS A 1 80  ? 36.023  12.044  29.051  1.00 16.10  ?  303  HIS A HE1  1 
ATOM   1284  N  N    . PHE A 1 81  ? 33.888  13.302  23.949  1.00 7.20   ?  304  PHE A N    1 
ATOM   1285  C  CA   . PHE A 1 81  ? 32.574  13.934  23.784  1.00 6.80   ?  304  PHE A CA   1 
ATOM   1286  C  C    . PHE A 1 81  ? 31.899  14.000  25.148  1.00 6.90   ?  304  PHE A C    1 
ATOM   1287  O  O    . PHE A 1 81  ? 31.357  13.009  25.642  1.00 7.54   ?  304  PHE A O    1 
ATOM   1288  C  CB   . PHE A 1 81  ? 31.800  13.101  22.764  1.00 7.36   ?  304  PHE A CB   1 
ATOM   1289  C  CG   . PHE A 1 81  ? 30.511  13.700  22.247  1.00 7.65   ?  304  PHE A CG   1 
ATOM   1290  C  CD1  . PHE A 1 81  ? 29.998  14.918  22.671  1.00 7.79   ?  304  PHE A CD1  1 
ATOM   1291  C  CD2  . PHE A 1 81  ? 29.788  12.985  21.316  1.00 10.03  ?  304  PHE A CD2  1 
ATOM   1292  C  CE1  . PHE A 1 81  ? 28.787  15.399  22.160  1.00 8.10   ?  304  PHE A CE1  1 
ATOM   1293  C  CE2  . PHE A 1 81  ? 28.606  13.468  20.807  1.00 10.74  ?  304  PHE A CE2  1 
ATOM   1294  C  CZ   . PHE A 1 81  ? 28.108  14.672  21.217  1.00 9.64   ?  304  PHE A CZ   1 
ATOM   1295  H  H    . PHE A 1 81  ? 33.827  12.468  24.150  1.00 8.64   ?  304  PHE A H    1 
ATOM   1296  H  HA   . PHE A 1 81  ? 32.640  14.852  23.479  1.00 8.16   ?  304  PHE A HA   1 
ATOM   1297  H  HB2  . PHE A 1 81  ? 32.374  12.955  21.996  1.00 8.84   ?  304  PHE A HB2  1 
ATOM   1298  H  HB3  . PHE A 1 81  ? 31.575  12.252  23.176  1.00 8.84   ?  304  PHE A HB3  1 
ATOM   1299  H  HD1  . PHE A 1 81  ? 30.464  15.419  23.301  1.00 9.35   ?  304  PHE A HD1  1 
ATOM   1300  H  HD2  . PHE A 1 81  ? 30.107  12.161  21.026  1.00 12.03  ?  304  PHE A HD2  1 
ATOM   1301  H  HE1  . PHE A 1 81  ? 28.444  16.210  22.460  1.00 9.72   ?  304  PHE A HE1  1 
ATOM   1302  H  HE2  . PHE A 1 81  ? 28.139  12.969  20.177  1.00 12.89  ?  304  PHE A HE2  1 
ATOM   1303  H  HZ   . PHE A 1 81  ? 27.314  14.996  20.858  1.00 11.57  ?  304  PHE A HZ   1 
ATOM   1304  N  N    . ASN A 1 82  ? 31.950  15.176  25.769  1.00 7.51   ?  305  ASN A N    1 
ATOM   1305  C  CA   . ASN A 1 82  ? 31.190  15.425  26.985  1.00 8.53   ?  305  ASN A CA   1 
ATOM   1306  C  C    . ASN A 1 82  ? 29.723  15.569  26.617  1.00 8.08   ?  305  ASN A C    1 
ATOM   1307  O  O    . ASN A 1 82  ? 29.382  16.337  25.716  1.00 10.21  ?  305  ASN A O    1 
ATOM   1308  C  CB   . ASN A 1 82  ? 31.704  16.708  27.655  1.00 10.55  ?  305  ASN A CB   1 
ATOM   1309  C  CG   . ASN A 1 82  ? 33.086  16.539  28.276  1.00 14.09  ?  305  ASN A CG   1 
ATOM   1310  O  OD1  . ASN A 1 82  ? 33.967  17.395  28.115  1.00 18.42  ?  305  ASN A OD1  1 
ATOM   1311  N  ND2  . ASN A 1 82  ? 33.284  15.451  28.997  1.00 13.74  ?  305  ASN A ND2  1 
ATOM   1312  H  H    . ASN A 1 82  ? 32.419  15.847  25.504  1.00 9.01   ?  305  ASN A H    1 
ATOM   1313  H  HA   . ASN A 1 82  ? 31.289  14.694  27.615  1.00 10.23  ?  305  ASN A HA   1 
ATOM   1314  H  HB2  . ASN A 1 82  ? 31.758  17.411  26.989  1.00 12.67  ?  305  ASN A HB2  1 
ATOM   1315  H  HB3  . ASN A 1 82  ? 31.088  16.964  28.359  1.00 12.67  ?  305  ASN A HB3  1 
ATOM   1316  H  HD21 . ASN A 1 82  ? 32.649  14.880  29.097  1.00 16.49  ?  305  ASN A HD21 1 
ATOM   1317  H  HD22 . ASN A 1 82  ? 34.048  15.314  29.367  1.00 16.49  ?  305  ASN A HD22 1 
ATOM   1318  N  N    . ILE A 1 83  ? 28.855  14.823  27.295  1.00 7.41   ?  306  ILE A N    1 
ATOM   1319  C  CA   . ILE A 1 83  ? 27.436  14.809  26.965  1.00 7.37   ?  306  ILE A CA   1 
ATOM   1320  C  C    . ILE A 1 83  ? 26.625  15.415  28.098  1.00 8.06   ?  306  ILE A C    1 
ATOM   1321  O  O    . ILE A 1 83  ? 26.970  15.308  29.280  1.00 9.85   ?  306  ILE A O    1 
ATOM   1322  C  CB   . ILE A 1 83  ? 26.939  13.401  26.590  1.00 7.09   ?  306  ILE A CB   1 
ATOM   1323  C  CG1  . ILE A 1 83  ? 27.079  12.411  27.751  1.00 7.77   ?  306  ILE A CG1  1 
ATOM   1324  C  CG2  . ILE A 1 83  ? 27.677  12.913  25.360  1.00 8.26   ?  306  ILE A CG2  1 
ATOM   1325  C  CD1  . ILE A 1 83  ? 26.396  11.058  27.470  1.00 7.77   ?  306  ILE A CD1  1 
ATOM   1326  H  H    . ILE A 1 83  ? 29.068  14.313  27.954  1.00 8.89   ?  306  ILE A H    1 
ATOM   1327  H  HA   . ILE A 1 83  ? 27.300  15.383  26.195  1.00 8.84   ?  306  ILE A HA   1 
ATOM   1328  H  HB   . ILE A 1 83  ? 25.992  13.461  26.391  1.00 8.51   ?  306  ILE A HB   1 
ATOM   1329  H  HG12 . ILE A 1 83  ? 28.021  12.244  27.912  1.00 9.33   ?  306  ILE A HG12 1 
ATOM   1330  H  HG13 . ILE A 1 83  ? 26.670  12.794  28.543  1.00 9.33   ?  306  ILE A HG13 1 
ATOM   1331  H  HG21 . ILE A 1 83  ? 27.265  12.091  25.051  1.00 9.91   ?  306  ILE A HG21 1 
ATOM   1332  H  HG22 . ILE A 1 83  ? 27.622  13.591  24.669  1.00 9.91   ?  306  ILE A HG22 1 
ATOM   1333  H  HG23 . ILE A 1 83  ? 28.605  12.751  25.592  1.00 9.91   ?  306  ILE A HG23 1 
ATOM   1334  H  HD11 . ILE A 1 83  ? 26.420  10.519  28.276  1.00 9.32   ?  306  ILE A HD11 1 
ATOM   1335  H  HD12 . ILE A 1 83  ? 25.477  11.217  27.206  1.00 9.32   ?  306  ILE A HD12 1 
ATOM   1336  H  HD13 . ILE A 1 83  ? 26.873  10.606  26.756  1.00 9.32   ?  306  ILE A HD13 1 
ATOM   1337  N  N    . THR A 1 84  ? 25.506  16.018  27.721  1.00 7.99   ?  307  THR A N    1 
ATOM   1338  C  CA   . THR A 1 84  ? 24.613  16.700  28.633  1.00 8.34   ?  307  THR A CA   1 
ATOM   1339  C  C    . THR A 1 84  ? 23.207  16.145  28.502  1.00 9.80   ?  307  THR A C    1 
ATOM   1340  O  O    . THR A 1 84  ? 22.939  15.238  27.700  1.00 12.98  ?  307  THR A O    1 
ATOM   1341  C  CB   . THR A 1 84  ? 24.561  18.205  28.310  1.00 10.01  ?  307  THR A CB   1 
ATOM   1342  O  OG1  . THR A 1 84  ? 23.926  18.397  27.029  1.00 11.45  ?  307  THR A OG1  1 
ATOM   1343  C  CG2  . THR A 1 84  ? 25.949  18.829  28.268  1.00 10.61  ?  307  THR A CG2  1 
ATOM   1344  H  H    . THR A 1 84  ? 25.235  16.044  26.905  1.00 9.59   ?  307  THR A H    1 
ATOM   1345  H  HA   . THR A 1 84  ? 24.934  16.563  29.538  1.00 10.01  ?  307  THR A HA   1 
ATOM   1346  H  HB   . THR A 1 84  ? 24.059  18.652  29.009  1.00 12.02  ?  307  THR A HB   1 
ATOM   1347  H  HG1  . THR A 1 84  ? 23.106  18.223  27.086  1.00 13.75  ?  307  THR A HG1  1 
ATOM   1348  H  HG21 . THR A 1 84  ? 25.878  19.787  28.134  1.00 12.74  ?  307  THR A HG21 1 
ATOM   1349  H  HG22 . THR A 1 84  ? 26.413  18.661  29.103  1.00 12.74  ?  307  THR A HG22 1 
ATOM   1350  H  HG23 . THR A 1 84  ? 26.463  18.446  27.540  1.00 12.74  ?  307  THR A HG23 1 
ATOM   1351  N  N    A ASN A 1 85  ? 22.312  16.578  29.367  0.65 10.42  ?  308  ASN A N    1 
ATOM   1352  N  N    B ASN A 1 85  ? 22.294  16.814  29.220  0.35 9.28   ?  308  ASN A N    1 
ATOM   1353  C  CA   A ASN A 1 85  ? 20.938  16.173  29.178  0.65 11.79  ?  308  ASN A CA   1 
ATOM   1354  C  CA   B ASN A 1 85  ? 20.852  16.779  29.001  0.35 8.39   ?  308  ASN A CA   1 
ATOM   1355  C  C    A ASN A 1 85  ? 20.512  16.586  27.775  0.65 12.12  ?  308  ASN A C    1 
ATOM   1356  C  C    B ASN A 1 85  ? 20.450  17.760  27.895  0.35 8.00   ?  308  ASN A C    1 
ATOM   1357  O  O    A ASN A 1 85  ? 21.123  17.473  27.174  0.65 11.79  ?  308  ASN A O    1 
ATOM   1358  O  O    B ASN A 1 85  ? 21.228  18.634  27.505  0.35 8.07   ?  308  ASN A O    1 
ATOM   1359  C  CB   A ASN A 1 85  ? 20.058  16.836  30.227  0.65 12.41  ?  308  ASN A CB   1 
ATOM   1360  C  CB   B ASN A 1 85  ? 20.134  17.158  30.298  0.35 8.86   ?  308  ASN A CB   1 
ATOM   1361  C  CG   A ASN A 1 85  ? 20.251  16.231  31.589  0.65 11.56  ?  308  ASN A CG   1 
ATOM   1362  C  CG   B ASN A 1 85  ? 20.545  16.294  31.480  0.35 8.83   ?  308  ASN A CG   1 
ATOM   1363  O  OD1  A ASN A 1 85  ? 20.391  15.014  31.719  0.65 12.00  ?  308  ASN A OD1  1 
ATOM   1364  O  OD1  B ASN A 1 85  ? 20.714  15.079  31.355  0.35 9.12   ?  308  ASN A OD1  1 
ATOM   1365  N  ND2  A ASN A 1 85  ? 20.276  17.069  32.614  0.65 12.03  ?  308  ASN A ND2  1 
ATOM   1366  N  ND2  B ASN A 1 85  ? 20.706  16.923  32.641  0.35 9.39   ?  308  ASN A ND2  1 
ATOM   1367  H  H    A ASN A 1 85  ? 22.468  17.086  30.043  0.65 12.51  ?  308  ASN A H    1 
ATOM   1368  H  H    B ASN A 1 85  ? 22.503  17.326  29.879  0.35 11.14  ?  308  ASN A H    1 
ATOM   1369  H  HA   A ASN A 1 85  ? 20.833  15.214  29.273  0.65 14.15  ?  308  ASN A HA   1 
ATOM   1370  H  HA   B ASN A 1 85  ? 20.597  15.881  28.736  0.35 10.07  ?  308  ASN A HA   1 
ATOM   1371  H  HB2  A ASN A 1 85  ? 20.281  17.779  30.281  0.65 14.90  ?  308  ASN A HB2  1 
ATOM   1372  H  HB2  B ASN A 1 85  ? 20.342  18.080  30.516  0.35 10.64  ?  308  ASN A HB2  1 
ATOM   1373  H  HB3  A ASN A 1 85  ? 19.127  16.729  29.977  0.65 14.90  ?  308  ASN A HB3  1 
ATOM   1374  H  HB3  B ASN A 1 85  ? 19.178  17.054  30.171  0.35 10.64  ?  308  ASN A HB3  1 
ATOM   1375  H  HD21 A ASN A 1 85  ? 20.384  16.768  33.412  0.65 14.44  ?  308  ASN A HD21 1 
ATOM   1376  H  HD21 B ASN A 1 85  ? 20.579  17.772  32.691  0.35 11.27  ?  308  ASN A HD21 1 
ATOM   1377  H  HD22 A ASN A 1 85  ? 20.184  17.914  32.481  0.65 14.44  ?  308  ASN A HD22 1 
ATOM   1378  H  HD22 B ASN A 1 85  ? 20.938  16.481  33.341  0.35 11.27  ?  308  ASN A HD22 1 
ATOM   1379  N  N    A PRO A 1 86  ? 19.473  15.952  27.221  0.65 12.90  ?  309  PRO A N    1 
ATOM   1380  N  N    B PRO A 1 86  ? 19.218  17.648  27.372  0.35 7.43   ?  309  PRO A N    1 
ATOM   1381  C  CA   A PRO A 1 86  ? 18.960  16.391  25.920  0.65 13.87  ?  309  PRO A CA   1 
ATOM   1382  C  CA   B PRO A 1 86  ? 18.851  18.449  26.185  0.35 7.92   ?  309  PRO A CA   1 
ATOM   1383  C  C    A PRO A 1 86  ? 18.582  17.866  25.875  0.65 14.77  ?  309  PRO A C    1 
ATOM   1384  C  C    B PRO A 1 86  ? 18.960  19.953  26.369  0.35 8.29   ?  309  PRO A C    1 
ATOM   1385  O  O    A PRO A 1 86  ? 18.570  18.450  24.794  0.65 15.04  ?  309  PRO A O    1 
ATOM   1386  O  O    B PRO A 1 86  ? 19.412  20.652  25.451  0.35 8.99   ?  309  PRO A O    1 
ATOM   1387  C  CB   A PRO A 1 86  ? 17.736  15.493  25.699  0.65 14.46  ?  309  PRO A CB   1 
ATOM   1388  C  CB   B PRO A 1 86  ? 17.403  18.010  25.898  0.35 7.98   ?  309  PRO A CB   1 
ATOM   1389  C  CG   A PRO A 1 86  ? 18.025  14.270  26.477  0.65 13.94  ?  309  PRO A CG   1 
ATOM   1390  C  CG   B PRO A 1 86  ? 17.316  16.635  26.461  0.35 7.86   ?  309  PRO A CG   1 
ATOM   1391  C  CD   A PRO A 1 86  ? 18.793  14.730  27.694  0.65 13.73  ?  309  PRO A CD   1 
ATOM   1392  C  CD   B PRO A 1 86  ? 18.177  16.655  27.699  0.35 7.46   ?  309  PRO A CD   1 
ATOM   1393  H  HA   A PRO A 1 86  ? 19.625  16.218  25.235  0.65 16.64  ?  309  PRO A HA   1 
ATOM   1394  H  HA   B PRO A 1 86  ? 19.426  18.190  25.448  0.35 9.51   ?  309  PRO A HA   1 
ATOM   1395  H  HB2  A PRO A 1 86  ? 16.938  15.934  26.028  0.65 17.35  ?  309  PRO A HB2  1 
ATOM   1396  H  HB2  B PRO A 1 86  ? 16.780  18.609  26.340  0.35 9.57   ?  309  PRO A HB2  1 
ATOM   1397  H  HB3  A PRO A 1 86  ? 17.639  15.291  24.755  0.65 17.35  ?  309  PRO A HB3  1 
ATOM   1398  H  HB3  B PRO A 1 86  ? 17.240  18.008  24.942  0.35 9.57   ?  309  PRO A HB3  1 
ATOM   1399  H  HG2  A PRO A 1 86  ? 17.194  13.842  26.735  0.65 16.73  ?  309  PRO A HG2  1 
ATOM   1400  H  HG2  B PRO A 1 86  ? 16.395  16.429  26.685  0.35 9.43   ?  309  PRO A HG2  1 
ATOM   1401  H  HG3  A PRO A 1 86  ? 18.559  13.661  25.943  0.65 16.73  ?  309  PRO A HG3  1 
ATOM   1402  H  HG3  B PRO A 1 86  ? 17.653  15.994  25.816  0.35 9.43   ?  309  PRO A HG3  1 
ATOM   1403  H  HD2  A PRO A 1 86  ? 18.191  14.931  28.427  0.65 16.48  ?  309  PRO A HD2  1 
ATOM   1404  H  HD2  B PRO A 1 86  ? 17.663  16.935  28.473  0.35 8.95   ?  309  PRO A HD2  1 
ATOM   1405  H  HD3  A PRO A 1 86  ? 19.438  14.060  27.970  0.65 16.48  ?  309  PRO A HD3  1 
ATOM   1406  H  HD3  B PRO A 1 86  ? 18.570  15.783  27.860  0.35 8.95   ?  309  PRO A HD3  1 
ATOM   1407  N  N    A ASN A 1 87  ? 18.270  18.477  27.019  0.65 15.08  ?  310  ASN A N    1 
ATOM   1408  N  N    B ASN A 1 87  ? 18.556  20.482  27.516  0.35 8.61   ?  310  ASN A N    1 
ATOM   1409  C  CA   A ASN A 1 87  ? 17.943  19.898  27.041  0.65 16.27  ?  310  ASN A CA   1 
ATOM   1410  C  CA   B ASN A 1 87  ? 18.553  21.928  27.699  0.35 9.75   ?  310  ASN A CA   1 
ATOM   1411  C  C    A ASN A 1 87  ? 19.157  20.795  27.261  0.65 16.07  ?  310  ASN A C    1 
ATOM   1412  C  C    B ASN A 1 87  ? 19.927  22.492  28.047  0.35 11.33  ?  310  ASN A C    1 
ATOM   1413  O  O    A ASN A 1 87  ? 18.998  22.015  27.305  0.65 16.27  ?  310  ASN A O    1 
ATOM   1414  O  O    B ASN A 1 87  ? 20.010  23.605  28.577  0.35 11.96  ?  310  ASN A O    1 
ATOM   1415  C  CB   A ASN A 1 87  ? 16.859  20.205  28.088  0.65 17.21  ?  310  ASN A CB   1 
ATOM   1416  C  CB   B ASN A 1 87  ? 17.524  22.339  28.757  0.35 9.96   ?  310  ASN A CB   1 
ATOM   1417  C  CG   A ASN A 1 87  ? 17.339  20.005  29.519  0.65 18.37  ?  310  ASN A CG   1 
ATOM   1418  C  CG   B ASN A 1 87  ? 17.859  21.808  30.135  0.35 9.96   ?  310  ASN A CG   1 
ATOM   1419  O  OD1  A ASN A 1 87  ? 18.509  19.701  29.759  0.65 17.20  ?  310  ASN A OD1  1 
ATOM   1420  O  OD1  B ASN A 1 87  ? 18.911  21.205  30.344  0.35 9.76   ?  310  ASN A OD1  1 
ATOM   1421  N  ND2  A ASN A 1 87  ? 16.440  20.208  30.479  0.65 19.81  ?  310  ASN A ND2  1 
ATOM   1422  N  ND2  B ASN A 1 87  ? 16.967  22.040  31.091  0.35 11.10  ?  310  ASN A ND2  1 
ATOM   1423  H  H    A ASN A 1 87  ? 18.241  18.090  27.786  0.65 18.10  ?  310  ASN A H    1 
ATOM   1424  H  H    B ASN A 1 87  ? 18.283  20.030  28.194  0.35 10.34  ?  310  ASN A H    1 
ATOM   1425  H  HA   A ASN A 1 87  ? 17.568  20.126  26.176  0.65 19.52  ?  310  ASN A HA   1 
ATOM   1426  H  HA   B ASN A 1 87  ? 18.277  22.332  26.861  0.35 11.70  ?  310  ASN A HA   1 
ATOM   1427  H  HB2  A ASN A 1 87  ? 16.581  21.129  27.992  0.65 20.65  ?  310  ASN A HB2  1 
ATOM   1428  H  HB2  B ASN A 1 87  ? 17.492  23.307  28.808  0.35 11.95  ?  310  ASN A HB2  1 
ATOM   1429  H  HB3  A ASN A 1 87  ? 16.103  19.615  27.941  0.65 20.65  ?  310  ASN A HB3  1 
ATOM   1430  H  HB3  B ASN A 1 87  ? 16.655  21.990  28.504  0.35 11.95  ?  310  ASN A HB3  1 
ATOM   1431  H  HD21 A ASN A 1 87  ? 15.637  20.440  30.275  0.65 23.77  ?  310  ASN A HD21 1 
ATOM   1432  H  HD21 B ASN A 1 87  ? 16.245  22.471  30.911  0.35 13.32  ?  310  ASN A HD21 1 
ATOM   1433  H  HD22 A ASN A 1 87  ? 16.662  20.108  31.304  0.65 23.77  ?  310  ASN A HD22 1 
ATOM   1434  H  HD22 B ASN A 1 87  ? 17.111  21.759  31.891  0.35 13.32  ?  310  ASN A HD22 1 
ATOM   1435  N  N    A GLY A 1 88  ? 20.355  20.240  27.410  0.65 15.58  ?  311  GLY A N    1 
ATOM   1436  N  N    B GLY A 1 88  ? 21.004  21.773  27.746  0.35 12.19  ?  311  GLY A N    1 
ATOM   1437  C  CA   A GLY A 1 88  ? 21.560  21.041  27.473  0.65 15.42  ?  311  GLY A CA   1 
ATOM   1438  C  CA   B GLY A 1 88  ? 22.318  22.177  28.180  0.35 12.55  ?  311  GLY A CA   1 
ATOM   1439  C  C    A GLY A 1 88  ? 22.139  21.279  28.858  0.65 16.78  ?  311  GLY A C    1 
ATOM   1440  C  C    B GLY A 1 88  ? 22.577  21.915  29.638  0.35 13.47  ?  311  GLY A C    1 
ATOM   1441  O  O    A GLY A 1 88  ? 23.258  21.787  28.946  0.65 17.79  ?  311  GLY A O    1 
ATOM   1442  O  O    B GLY A 1 88  ? 23.718  22.089  30.090  0.35 13.43  ?  311  GLY A O    1 
ATOM   1443  H  H    A GLY A 1 88  ? 20.491  19.394  27.477  0.65 18.69  ?  311  GLY A H    1 
ATOM   1444  H  H    B GLY A 1 88  ? 20.991  21.044  27.289  0.35 14.63  ?  311  GLY A H    1 
ATOM   1445  H  HA2  A GLY A 1 88  ? 22.245  20.602  26.944  0.65 18.51  ?  311  GLY A HA2  1 
ATOM   1446  H  HA2  B GLY A 1 88  ? 22.983  21.694  27.664  0.35 15.06  ?  311  GLY A HA2  1 
ATOM   1447  H  HA3  A GLY A 1 88  ? 21.370  21.909  27.085  0.65 18.51  ?  311  GLY A HA3  1 
ATOM   1448  H  HA3  B GLY A 1 88  ? 22.424  23.128  28.021  0.35 15.06  ?  311  GLY A HA3  1 
ATOM   1449  N  N    A THR A 1 89  ? 21.436  20.922  29.942  0.65 16.85  ?  312  THR A N    1 
ATOM   1450  N  N    B THR A 1 89  ? 21.564  21.499  30.386  0.35 14.78  ?  312  THR A N    1 
ATOM   1451  C  CA   A THR A 1 89  ? 21.979  21.119  31.293  0.65 15.97  ?  312  THR A CA   1 
ATOM   1452  C  CA   B THR A 1 89  ? 21.782  21.163  31.777  0.35 15.78  ?  312  THR A CA   1 
ATOM   1453  C  C    A THR A 1 89  ? 22.900  19.948  31.663  0.65 14.10  ?  312  THR A C    1 
ATOM   1454  C  C    B THR A 1 89  ? 22.736  19.977  31.866  0.35 15.54  ?  312  THR A C    1 
ATOM   1455  O  O    A THR A 1 89  ? 22.858  18.899  31.019  0.65 11.16  ?  312  THR A O    1 
ATOM   1456  O  O    B THR A 1 89  ? 22.555  18.973  31.164  0.35 15.19  ?  312  THR A O    1 
ATOM   1457  C  CB   A THR A 1 89  ? 20.827  21.237  32.293  0.65 16.47  ?  312  THR A CB   1 
ATOM   1458  C  CB   B THR A 1 89  ? 20.489  20.862  32.538  0.35 16.42  ?  312  THR A CB   1 
ATOM   1459  O  OG1  A THR A 1 89  ? 20.099  20.003  32.359  0.65 14.91  ?  312  THR A OG1  1 
ATOM   1460  O  OG1  B THR A 1 89  ? 19.693  19.919  31.811  0.35 16.36  ?  312  THR A OG1  1 
ATOM   1461  C  CG2  A THR A 1 89  ? 19.872  22.362  31.873  0.65 17.28  ?  312  THR A CG2  1 
ATOM   1462  C  CG2  B THR A 1 89  ? 19.711  22.151  32.796  0.35 17.16  ?  312  THR A CG2  1 
ATOM   1463  H  H    A THR A 1 89  ? 20.652  20.568  29.922  0.65 20.22  ?  312  THR A H    1 
ATOM   1464  H  H    B THR A 1 89  ? 20.753  21.406  30.114  0.35 17.74  ?  312  THR A H    1 
ATOM   1465  H  HA   A THR A 1 89  ? 22.499  21.937  31.337  0.65 19.16  ?  312  THR A HA   1 
ATOM   1466  H  HA   B THR A 1 89  ? 22.174  21.936  32.213  0.35 18.94  ?  312  THR A HA   1 
ATOM   1467  H  HB   A THR A 1 89  ? 21.187  21.441  33.171  0.65 19.77  ?  312  THR A HB   1 
ATOM   1468  H  HB   B THR A 1 89  ? 20.701  20.469  33.400  0.35 19.70  ?  312  THR A HB   1 
ATOM   1469  H  HG1  A THR A 1 89  ? 19.455  20.077  32.894  0.65 17.90  ?  312  THR A HG1  1 
ATOM   1470  H  HG1  B THR A 1 89  ? 19.779  20.047  30.986  0.35 19.63  ?  312  THR A HG1  1 
ATOM   1471  H  HG21 A THR A 1 89  ? 19.199  22.499  32.558  0.65 20.74  ?  312  THR A HG21 1 
ATOM   1472  H  HG21 B THR A 1 89  ? 18.791  21.944  33.023  0.35 20.60  ?  312  THR A HG21 1 
ATOM   1473  H  HG22 A THR A 1 89  ? 20.366  23.187  31.747  0.65 20.74  ?  312  THR A HG22 1 
ATOM   1474  H  HG22 B THR A 1 89  ? 20.114  22.641  33.530  0.35 20.60  ?  312  THR A HG22 1 
ATOM   1475  H  HG23 A THR A 1 89  ? 19.431  22.128  31.041  0.65 20.74  ?  312  THR A HG23 1 
ATOM   1476  H  HG23 B THR A 1 89  ? 19.721  22.709  32.002  0.35 20.60  ?  312  THR A HG23 1 
ATOM   1477  N  N    . PRO A 1 90  ? 23.764  20.074  32.684  1.00 15.76  ?  313  PRO A N    1 
ATOM   1478  C  CA   . PRO A 1 90  ? 24.665  18.946  32.942  1.00 15.03  ?  313  PRO A CA   1 
ATOM   1479  C  C    . PRO A 1 90  ? 23.923  17.746  33.507  1.00 14.50  ?  313  PRO A C    1 
ATOM   1480  O  O    . PRO A 1 90  ? 23.011  17.879  34.326  1.00 15.43  ?  313  PRO A O    1 
ATOM   1481  C  CB   . PRO A 1 90  ? 25.676  19.520  33.943  1.00 17.69  ?  313  PRO A CB   1 
ATOM   1482  C  CG   . PRO A 1 90  ? 24.985  20.637  34.572  1.00 18.45  ?  313  PRO A CG   1 
ATOM   1483  C  CD   . PRO A 1 90  ? 24.056  21.222  33.563  1.00 17.90  ?  313  PRO A CD   1 
ATOM   1484  H  HA   . PRO A 1 90  ? 25.123  18.683  32.129  1.00 18.04  ?  313  PRO A HA   1 
ATOM   1485  H  HB2  . PRO A 1 90  ? 25.914  18.844  34.597  1.00 21.24  ?  313  PRO A HB2  1 
ATOM   1486  H  HB3  . PRO A 1 90  ? 26.470  19.822  33.474  1.00 21.24  ?  313  PRO A HB3  1 
ATOM   1487  H  HG2  . PRO A 1 90  ? 24.487  20.313  35.340  1.00 22.14  ?  313  PRO A HG2  1 
ATOM   1488  H  HG3  . PRO A 1 90  ? 25.636  21.298  34.854  1.00 22.14  ?  313  PRO A HG3  1 
ATOM   1489  H  HD2  . PRO A 1 90  ? 23.247  21.551  33.985  1.00 21.48  ?  313  PRO A HD2  1 
ATOM   1490  H  HD3  . PRO A 1 90  ? 24.487  21.937  33.068  1.00 21.48  ?  313  PRO A HD3  1 
ATOM   1491  N  N    . PHE A 1 91  ? 24.306  16.564  33.037  1.00 14.84  ?  314  PHE A N    1 
ATOM   1492  C  CA   . PHE A 1 91  ? 23.719  15.338  33.549  1.00 16.03  ?  314  PHE A CA   1 
ATOM   1493  C  C    . PHE A 1 91  ? 24.190  15.103  34.978  1.00 18.02  ?  314  PHE A C    1 
ATOM   1494  O  O    . PHE A 1 91  ? 25.370  15.270  35.290  1.00 18.73  ?  314  PHE A O    1 
ATOM   1495  C  CB   . PHE A 1 91  ? 24.124  14.170  32.653  1.00 15.72  ?  314  PHE A CB   1 
ATOM   1496  C  CG   . PHE A 1 91  ? 23.643  12.845  33.143  1.00 15.01  ?  314  PHE A CG   1 
ATOM   1497  C  CD1  . PHE A 1 91  ? 22.295  12.522  33.090  1.00 15.33  ?  314  PHE A CD1  1 
ATOM   1498  C  CD2  . PHE A 1 91  ? 24.532  11.919  33.646  1.00 15.81  ?  314  PHE A CD2  1 
ATOM   1499  C  CE1  . PHE A 1 91  ? 21.847  11.302  33.537  1.00 16.22  ?  314  PHE A CE1  1 
ATOM   1500  C  CE2  . PHE A 1 91  ? 24.091  10.701  34.090  1.00 16.46  ?  314  PHE A CE2  1 
ATOM   1501  C  CZ   . PHE A 1 91  ? 22.745  10.386  34.042  1.00 16.23  ?  314  PHE A CZ   1 
ATOM   1502  H  H    . PHE A 1 91  ? 24.900  16.448  32.426  1.00 17.81  ?  314  PHE A H    1 
ATOM   1503  H  HA   . PHE A 1 91  ? 22.751  15.396  33.554  1.00 19.24  ?  314  PHE A HA   1 
ATOM   1504  H  HB2  . PHE A 1 91  ? 23.753  14.312  31.768  1.00 18.87  ?  314  PHE A HB2  1 
ATOM   1505  H  HB3  . PHE A 1 91  ? 25.092  14.135  32.604  1.00 18.87  ?  314  PHE A HB3  1 
ATOM   1506  H  HD1  . PHE A 1 91  ? 21.688  13.138  32.747  1.00 18.40  ?  314  PHE A HD1  1 
ATOM   1507  H  HD2  . PHE A 1 91  ? 25.439  12.122  33.683  1.00 18.97  ?  314  PHE A HD2  1 
ATOM   1508  H  HE1  . PHE A 1 91  ? 20.941  11.095  33.499  1.00 19.47  ?  314  PHE A HE1  1 
ATOM   1509  H  HE2  . PHE A 1 91  ? 24.699  10.083  34.426  1.00 19.76  ?  314  PHE A HE2  1 
ATOM   1510  H  HZ   . PHE A 1 91  ? 22.448  9.560   34.348  1.00 19.48  ?  314  PHE A HZ   1 
ATOM   1511  N  N    . ASP A 1 92  ? 23.250  14.735  35.851  1.00 18.81  ?  315  ASP A N    1 
ATOM   1512  C  CA   . ASP A 1 92  ? 23.534  14.462  37.254  1.00 21.29  ?  315  ASP A CA   1 
ATOM   1513  C  C    . ASP A 1 92  ? 23.579  12.954  37.443  1.00 22.88  ?  315  ASP A C    1 
ATOM   1514  O  O    . ASP A 1 92  ? 22.518  12.310  37.439  1.00 23.61  ?  315  ASP A O    1 
ATOM   1515  C  CB   . ASP A 1 92  ? 22.441  15.072  38.136  1.00 22.35  ?  315  ASP A CB   1 
ATOM   1516  C  CG   . ASP A 1 92  ? 22.705  14.883  39.620  1.00 24.31  ?  315  ASP A CG   1 
ATOM   1517  O  OD1  . ASP A 1 92  ? 23.653  14.149  39.979  1.00 24.32  ?  315  ASP A OD1  1 
ATOM   1518  O  OD2  . ASP A 1 92  ? 21.956  15.471  40.429  1.00 26.29  -1 315  ASP A OD2  1 
ATOM   1519  H  H    . ASP A 1 92  ? 22.420  14.635  35.647  1.00 22.57  ?  315  ASP A H    1 
ATOM   1520  H  HA   . ASP A 1 92  ? 24.389  14.843  37.507  1.00 25.55  ?  315  ASP A HA   1 
ATOM   1521  H  HB2  . ASP A 1 92  ? 22.388  16.025  37.960  1.00 26.82  ?  315  ASP A HB2  1 
ATOM   1522  H  HB3  . ASP A 1 92  ? 21.593  14.649  37.926  1.00 26.82  ?  315  ASP A HB3  1 
ATOM   1523  N  N    . PRO A 1 93  ? 24.758  12.348  37.633  1.00 24.28  ?  316  PRO A N    1 
ATOM   1524  C  CA   A PRO A 1 93  ? 24.822  10.882  37.748  0.50 24.85  ?  316  PRO A CA   1 
ATOM   1525  C  CA   B PRO A 1 93  ? 24.830  10.883  37.753  0.50 24.92  ?  316  PRO A CA   1 
ATOM   1526  C  C    . PRO A 1 93  ? 24.172  10.319  39.004  1.00 25.39  ?  316  PRO A C    1 
ATOM   1527  O  O    . PRO A 1 93  ? 24.015  9.092   39.093  1.00 26.00  ?  316  PRO A O    1 
ATOM   1528  C  CB   A PRO A 1 93  ? 26.328  10.600  37.740  0.50 25.02  ?  316  PRO A CB   1 
ATOM   1529  C  CB   B PRO A 1 93  ? 26.340  10.602  37.748  0.50 25.23  ?  316  PRO A CB   1 
ATOM   1530  C  CG   A PRO A 1 93  ? 26.912  11.801  38.369  0.50 24.68  ?  316  PRO A CG   1 
ATOM   1531  C  CG   B PRO A 1 93  ? 26.960  11.805  37.110  0.50 25.02  ?  316  PRO A CG   1 
ATOM   1532  C  CD   A PRO A 1 93  ? 26.074  12.964  37.882  0.50 24.72  ?  316  PRO A CD   1 
ATOM   1533  C  CD   B PRO A 1 93  ? 26.097  12.955  37.519  0.50 24.61  ?  316  PRO A CD   1 
ATOM   1534  H  HA   A PRO A 1 93  ? 24.408  10.476  36.971  0.50 29.82  ?  316  PRO A HA   1 
ATOM   1535  H  HA   B PRO A 1 93  ? 24.423  10.473  36.974  0.50 29.90  ?  316  PRO A HA   1 
ATOM   1536  H  HB2  A PRO A 1 93  ? 26.522  9.803   38.256  0.50 30.02  ?  316  PRO A HB2  1 
ATOM   1537  H  HB2  B PRO A 1 93  ? 26.658  10.491  38.658  0.50 30.28  ?  316  PRO A HB2  1 
ATOM   1538  H  HB3  A PRO A 1 93  ? 26.644  10.492  36.829  0.50 30.02  ?  316  PRO A HB3  1 
ATOM   1539  H  HB3  B PRO A 1 93  ? 26.525  9.802   37.232  0.50 30.28  ?  316  PRO A HB3  1 
ATOM   1540  H  HG2  A PRO A 1 93  ? 26.864  11.722  39.335  0.50 29.62  ?  316  PRO A HG2  1 
ATOM   1541  H  HG2  B PRO A 1 93  ? 27.867  11.921  37.434  0.50 30.02  ?  316  PRO A HG2  1 
ATOM   1542  H  HG3  A PRO A 1 93  ? 27.836  11.901  38.091  0.50 29.62  ?  316  PRO A HG3  1 
ATOM   1543  H  HG3  B PRO A 1 93  ? 26.963  11.702  36.145  0.50 30.02  ?  316  PRO A HG3  1 
ATOM   1544  H  HD2  A PRO A 1 93  ? 26.010  13.653  38.562  0.50 29.67  ?  316  PRO A HD2  1 
ATOM   1545  H  HD2  B PRO A 1 93  ? 26.386  13.318  38.372  0.50 29.54  ?  316  PRO A HD2  1 
ATOM   1546  H  HD3  A PRO A 1 93  ? 26.441  13.337  37.066  0.50 29.67  ?  316  PRO A HD3  1 
ATOM   1547  H  HD3  B PRO A 1 93  ? 26.104  13.651  36.843  0.50 29.54  ?  316  PRO A HD3  1 
ATOM   1548  N  N    . THR A 1 94  ? 23.802  11.150  39.977  1.00 26.07  ?  317  THR A N    1 
ATOM   1549  C  CA   . THR A 1 94  ? 23.106  10.633  41.149  1.00 26.65  ?  317  THR A CA   1 
ATOM   1550  C  C    . THR A 1 94  ? 21.620  10.434  40.888  1.00 27.05  ?  317  THR A C    1 
ATOM   1551  O  O    . THR A 1 94  ? 20.927  9.862   41.737  1.00 28.11  ?  317  THR A O    1 
ATOM   1552  C  CB   . THR A 1 94  ? 23.310  11.555  42.357  1.00 27.44  ?  317  THR A CB   1 
ATOM   1553  O  OG1  . THR A 1 94  ? 22.552  12.760  42.185  1.00 27.50  ?  317  THR A OG1  1 
ATOM   1554  C  CG2  . THR A 1 94  ? 24.789  11.903  42.519  1.00 28.12  ?  317  THR A CG2  1 
ATOM   1555  H  H    . THR A 1 94  ? 23.940  11.999  39.980  1.00 31.28  ?  317  THR A H    1 
ATOM   1556  H  HA   . THR A 1 94  ? 23.491  9.775   41.389  1.00 31.98  ?  317  THR A HA   1 
ATOM   1557  H  HB   . THR A 1 94  ? 23.011  11.102  43.161  1.00 32.93  ?  317  THR A HB   1 
ATOM   1558  H  HG1  . THR A 1 94  ? 22.815  13.169  41.499  1.00 33.00  ?  317  THR A HG1  1 
ATOM   1559  H  HG21 . THR A 1 94  ? 24.931  12.365  43.360  1.00 33.75  ?  317  THR A HG21 1 
ATOM   1560  H  HG22 . THR A 1 94  ? 25.323  11.093  42.510  1.00 33.75  ?  317  THR A HG22 1 
ATOM   1561  H  HG23 . THR A 1 94  ? 25.076  12.477  41.792  1.00 33.75  ?  317  THR A HG23 1 
ATOM   1562  N  N    A GLU A 1 95  ? 21.121  10.885  39.737  0.79 26.12  ?  318  GLU A N    1 
ATOM   1563  C  CA   A GLU A 1 95  ? 19.751  10.582  39.357  0.79 25.78  ?  318  GLU A CA   1 
ATOM   1564  C  C    A GLU A 1 95  ? 19.596  9.079   39.176  0.79 22.84  ?  318  GLU A C    1 
ATOM   1565  O  O    A GLU A 1 95  ? 20.509  8.397   38.702  0.79 21.97  ?  318  GLU A O    1 
ATOM   1566  C  CB   A GLU A 1 95  ? 19.414  11.289  38.045  0.79 28.54  ?  318  GLU A CB   1 
ATOM   1567  C  CG   A GLU A 1 95  ? 19.241  12.785  38.172  0.79 31.16  ?  318  GLU A CG   1 
ATOM   1568  C  CD   A GLU A 1 95  ? 17.845  13.166  38.597  0.79 33.09  ?  318  GLU A CD   1 
ATOM   1569  O  OE1  A GLU A 1 95  ? 17.495  12.948  39.777  0.79 34.23  ?  318  GLU A OE1  1 
ATOM   1570  O  OE2  A GLU A 1 95  ? 17.092  13.677  37.744  0.79 34.02  -1 318  GLU A OE2  1 
ATOM   1571  H  H    A GLU A 1 95  ? 21.554  11.363  39.168  0.79 31.34  ?  318  GLU A H    1 
ATOM   1572  H  HA   A GLU A 1 95  ? 19.138  10.889  40.042  0.79 30.93  ?  318  GLU A HA   1 
ATOM   1573  H  HB2  A GLU A 1 95  ? 20.133  11.129  37.413  0.79 34.26  ?  318  GLU A HB2  1 
ATOM   1574  H  HB3  A GLU A 1 95  ? 18.583  10.925  37.702  0.79 34.26  ?  318  GLU A HB3  1 
ATOM   1575  H  HG2  A GLU A 1 95  ? 19.862  13.121  38.837  0.79 37.40  ?  318  GLU A HG2  1 
ATOM   1576  H  HG3  A GLU A 1 95  ? 19.419  13.199  37.313  0.79 37.40  ?  318  GLU A HG3  1 
ATOM   1577  N  N    . ASP A 1 96  ? 18.425  8.565   39.552  1.00 21.92  ?  319  ASP A N    1 
ATOM   1578  C  CA   . ASP A 1 96  ? 18.124  7.135   39.468  1.00 21.00  ?  319  ASP A CA   1 
ATOM   1579  C  C    . ASP A 1 96  ? 17.777  6.732   38.032  1.00 18.37  ?  319  ASP A C    1 
ATOM   1580  O  O    . ASP A 1 96  ? 16.715  6.182   37.744  1.00 19.12  ?  319  ASP A O    1 
ATOM   1581  C  CB   . ASP A 1 96  ? 16.988  6.796   40.425  1.00 22.88  ?  319  ASP A CB   1 
ATOM   1582  C  CG   . ASP A 1 96  ? 16.760  5.305   40.557  1.00 24.56  ?  319  ASP A CG   1 
ATOM   1583  O  OD1  . ASP A 1 96  ? 17.732  4.539   40.384  1.00 24.72  -1 319  ASP A OD1  1 
ATOM   1584  O  OD2  . ASP A 1 96  ? 15.605  4.903   40.834  1.00 26.28  ?  319  ASP A OD2  1 
ATOM   1585  H  H    . ASP A 1 96  ? 17.775  9.033   39.865  1.00 26.30  ?  319  ASP A H    1 
ATOM   1586  H  HA   . ASP A 1 96  ? 18.914  6.636   39.731  1.00 25.20  ?  319  ASP A HA   1 
ATOM   1587  H  HB2  . ASP A 1 96  ? 17.199  7.146   41.305  1.00 27.46  ?  319  ASP A HB2  1 
ATOM   1588  H  HB3  . ASP A 1 96  ? 16.168  7.197   40.097  1.00 27.46  ?  319  ASP A HB3  1 
ATOM   1589  N  N    . VAL A 1 97  ? 18.708  7.022   37.133  1.00 15.73  ?  320  VAL A N    1 
ATOM   1590  C  CA   A VAL A 1 97  ? 18.555  6.662   35.722  0.65 14.41  ?  320  VAL A CA   1 
ATOM   1591  C  CA   B VAL A 1 97  ? 18.591  6.760   35.700  0.35 14.17  ?  320  VAL A CA   1 
ATOM   1592  C  C    . VAL A 1 97  ? 19.871  6.059   35.254  1.00 11.75  ?  320  VAL A C    1 
ATOM   1593  O  O    . VAL A 1 97  ? 20.934  6.307   35.832  1.00 12.09  ?  320  VAL A O    1 
ATOM   1594  C  CB   A VAL A 1 97  ? 18.142  7.873   34.849  0.65 16.25  ?  320  VAL A CB   1 
ATOM   1595  C  CB   B VAL A 1 97  ? 18.381  8.080   34.939  0.35 15.24  ?  320  VAL A CB   1 
ATOM   1596  C  CG1  A VAL A 1 97  ? 16.798  8.448   35.289  0.65 16.90  ?  320  VAL A CG1  1 
ATOM   1597  C  CG1  B VAL A 1 97  ? 19.683  8.876   34.872  0.35 15.93  ?  320  VAL A CG1  1 
ATOM   1598  C  CG2  A VAL A 1 97  ? 19.210  8.949   34.865  0.65 16.88  ?  320  VAL A CG2  1 
ATOM   1599  C  CG2  B VAL A 1 97  ? 17.844  7.824   33.553  0.35 14.94  ?  320  VAL A CG2  1 
ATOM   1600  H  H    A VAL A 1 97  ? 19.443  7.430   37.312  0.65 18.88  ?  320  VAL A H    1 
ATOM   1601  H  H    B VAL A 1 97  ? 19.458  7.392   37.336  0.35 18.88  ?  320  VAL A H    1 
ATOM   1602  H  HA   A VAL A 1 97  ? 17.859  5.992   35.632  0.65 17.30  ?  320  VAL A HA   1 
ATOM   1603  H  HA   B VAL A 1 97  ? 17.838  6.176   35.517  0.35 17.00  ?  320  VAL A HA   1 
ATOM   1604  H  HB   A VAL A 1 97  ? 18.046  7.558   33.936  0.65 19.50  ?  320  VAL A HB   1 
ATOM   1605  H  HB   B VAL A 1 97  ? 17.726  8.610   35.419  0.35 18.28  ?  320  VAL A HB   1 
ATOM   1606  H  HG11 A VAL A 1 97  ? 16.567  9.192   34.710  0.65 20.28  ?  320  VAL A HG11 1 
ATOM   1607  H  HG11 B VAL A 1 97  ? 19.478  9.798   34.654  0.35 19.12  ?  320  VAL A HG11 1 
ATOM   1608  H  HG12 A VAL A 1 97  ? 16.121  7.756   35.223  0.65 20.28  ?  320  VAL A HG12 1 
ATOM   1609  H  HG12 B VAL A 1 97  ? 20.126  8.830   35.734  0.35 19.12  ?  320  VAL A HG12 1 
ATOM   1610  H  HG13 A VAL A 1 97  ? 16.870  8.753   36.207  0.65 20.28  ?  320  VAL A HG13 1 
ATOM   1611  H  HG13 B VAL A 1 97  ? 20.253  8.492   34.187  0.35 19.12  ?  320  VAL A HG13 1 
ATOM   1612  H  HG21 A VAL A 1 97  ? 18.863  9.745   34.432  0.65 20.26  ?  320  VAL A HG21 1 
ATOM   1613  H  HG21 B VAL A 1 97  ? 17.554  8.665   33.167  0.35 17.93  ?  320  VAL A HG21 1 
ATOM   1614  H  HG22 A VAL A 1 97  ? 19.443  9.149   35.785  0.65 20.26  ?  320  VAL A HG22 1 
ATOM   1615  H  HG22 B VAL A 1 97  ? 18.547  7.434   33.010  0.35 17.93  ?  320  VAL A HG22 1 
ATOM   1616  H  HG23 A VAL A 1 97  ? 19.991  8.627   34.389  0.65 20.26  ?  320  VAL A HG23 1 
ATOM   1617  H  HG23 B VAL A 1 97  ? 17.094  7.211   33.614  0.35 17.93  ?  320  VAL A HG23 1 
ATOM   1618  N  N    . PRO A 1 98  ? 19.840  5.237   34.201  1.00 9.16   ?  321  PRO A N    1 
ATOM   1619  C  CA   . PRO A 1 98  ? 21.074  4.536   33.805  1.00 8.11   ?  321  PRO A CA   1 
ATOM   1620  C  C    . PRO A 1 98  ? 22.129  5.422   33.194  1.00 8.17   ?  321  PRO A C    1 
ATOM   1621  O  O    . PRO A 1 98  ? 23.315  5.083   33.278  1.00 8.51   ?  321  PRO A O    1 
ATOM   1622  C  CB   . PRO A 1 98  ? 20.584  3.491   32.795  1.00 8.64   ?  321  PRO A CB   1 
ATOM   1623  C  CG   . PRO A 1 98  ? 19.133  3.336   33.085  1.00 9.31   ?  321  PRO A CG   1 
ATOM   1624  C  CD   . PRO A 1 98  ? 18.666  4.692   33.506  1.00 9.22   ?  321  PRO A CD   1 
ATOM   1625  H  HA   . PRO A 1 98  ? 21.445  4.096   34.586  1.00 9.73   ?  321  PRO A HA   1 
ATOM   1626  H  HB2  . PRO A 1 98  ? 20.725  3.813   31.891  1.00 10.37  ?  321  PRO A HB2  1 
ATOM   1627  H  HB3  . PRO A 1 98  ? 21.057  2.655   32.928  1.00 10.37  ?  321  PRO A HB3  1 
ATOM   1628  H  HG2  . PRO A 1 98  ? 18.668  3.043   32.286  1.00 11.17  ?  321  PRO A HG2  1 
ATOM   1629  H  HG3  . PRO A 1 98  ? 19.007  2.690   33.798  1.00 11.17  ?  321  PRO A HG3  1 
ATOM   1630  H  HD2  . PRO A 1 98  ? 18.435  5.235   32.736  1.00 11.06  ?  321  PRO A HD2  1 
ATOM   1631  H  HD3  . PRO A 1 98  ? 17.907  4.627   34.106  1.00 11.06  ?  321  PRO A HD3  1 
ATOM   1632  N  N    . ALA A 1 99  ? 21.718  6.507   32.543  1.00 7.62   ?  322  ALA A N    1 
ATOM   1633  C  CA   . ALA A 1 99  ? 22.548  7.318   31.676  1.00 7.23   ?  322  ALA A CA   1 
ATOM   1634  C  C    . ALA A 1 99  ? 21.659  8.449   31.185  1.00 6.89   ?  322  ALA A C    1 
ATOM   1635  O  O    . ALA A 1 99  ? 20.440  8.403   31.379  1.00 7.31   ?  322  ALA A O    1 
ATOM   1636  C  CB   . ALA A 1 99  ? 23.023  6.471   30.499  1.00 7.29   ?  322  ALA A CB   1 
ATOM   1637  H  H    . ALA A 1 99  ? 20.914  6.808   32.594  1.00 9.14   ?  322  ALA A H    1 
ATOM   1638  H  HA   . ALA A 1 99  ? 23.331  7.670   32.128  1.00 8.67   ?  322  ALA A HA   1 
ATOM   1639  H  HB1  . ALA A 1 99  ? 23.578  7.017   29.921  1.00 8.75   ?  322  ALA A HB1  1 
ATOM   1640  H  HB2  . ALA A 1 99  ? 23.536  5.720   30.837  1.00 8.75   ?  322  ALA A HB2  1 
ATOM   1641  H  HB3  . ALA A 1 99  ? 22.250  6.149   30.009  1.00 8.75   ?  322  ALA A HB3  1 
ATOM   1642  N  N    . PRO A 1 100 ? 22.203  9.447   30.494  1.00 6.78   ?  323  PRO A N    1 
ATOM   1643  C  CA   . PRO A 1 100 ? 21.350  10.482  29.904  1.00 7.00   ?  323  PRO A CA   1 
ATOM   1644  C  C    . PRO A 1 100 ? 20.256  9.873   29.036  1.00 6.52   ?  323  PRO A C    1 
ATOM   1645  O  O    . PRO A 1 100 ? 20.446  8.857   28.354  1.00 7.00   ?  323  PRO A O    1 
ATOM   1646  C  CB   . PRO A 1 100 ? 22.343  11.337  29.104  1.00 7.37   ?  323  PRO A CB   1 
ATOM   1647  C  CG   . PRO A 1 100 ? 23.638  11.206  29.882  1.00 7.30   ?  323  PRO A CG   1 
ATOM   1648  C  CD   . PRO A 1 100 ? 23.636  9.740   30.292  1.00 7.64   ?  323  PRO A CD   1 
ATOM   1649  H  HA   . PRO A 1 100 ? 20.937  11.032  30.588  1.00 8.41   ?  323  PRO A HA   1 
ATOM   1650  H  HB2  . PRO A 1 100 ? 22.436  10.989  28.204  1.00 8.85   ?  323  PRO A HB2  1 
ATOM   1651  H  HB3  . PRO A 1 100 ? 22.042  12.259  29.074  1.00 8.85   ?  323  PRO A HB3  1 
ATOM   1652  H  HG2  . PRO A 1 100 ? 24.397  11.414  29.315  1.00 8.77   ?  323  PRO A HG2  1 
ATOM   1653  H  HG3  . PRO A 1 100 ? 23.631  11.791  30.655  1.00 8.77   ?  323  PRO A HG3  1 
ATOM   1654  H  HD2  . PRO A 1 100 ? 24.006  9.184   29.589  1.00 9.17   ?  323  PRO A HD2  1 
ATOM   1655  H  HD3  . PRO A 1 100 ? 24.134  9.611   31.114  1.00 9.17   ?  323  PRO A HD3  1 
ATOM   1656  N  N    . LEU A 1 101 ? 19.078  10.475  29.080  1.00 6.17   ?  324  LEU A N    1 
ATOM   1657  C  CA   . LEU A 1 101 ? 17.958  9.874   28.379  1.00 6.87   ?  324  LEU A CA   1 
ATOM   1658  C  C    . LEU A 1 101 ? 18.266  9.800   26.887  1.00 6.37   ?  324  LEU A C    1 
ATOM   1659  O  O    . LEU A 1 101 ? 18.897  10.693  26.305  1.00 7.69   ?  324  LEU A O    1 
ATOM   1660  C  CB   . LEU A 1 101 ? 16.677  10.648  28.658  1.00 8.04   ?  324  LEU A CB   1 
ATOM   1661  C  CG   . LEU A 1 101 ? 16.310  10.767  30.133  1.00 8.03   ?  324  LEU A CG   1 
ATOM   1662  C  CD1  . LEU A 1 101 ? 14.931  11.402  30.232  1.00 8.63   ?  324  LEU A CD1  1 
ATOM   1663  C  CD2  . LEU A 1 101 ? 16.356  9.440   30.892  1.00 8.13   ?  324  LEU A CD2  1 
ATOM   1664  H  H    . LEU A 1 101 ? 18.906  11.208  29.495  1.00 7.41   ?  324  LEU A H    1 
ATOM   1665  H  HA   . LEU A 1 101 ? 17.806  8.969   28.695  1.00 8.24   ?  324  LEU A HA   1 
ATOM   1666  H  HB2  . LEU A 1 101 ? 16.780  11.548  28.310  1.00 9.65   ?  324  LEU A HB2  1 
ATOM   1667  H  HB3  . LEU A 1 101 ? 15.943  10.200  28.209  1.00 9.65   ?  324  LEU A HB3  1 
ATOM   1668  H  HG   . LEU A 1 101 ? 16.974  11.322  30.571  1.00 9.64   ?  324  LEU A HG   1 
ATOM   1669  H  HD11 . LEU A 1 101 ? 14.716  11.547  31.166  1.00 10.36  ?  324  LEU A HD11 1 
ATOM   1670  H  HD12 . LEU A 1 101 ? 14.939  12.249  29.759  1.00 10.36  ?  324  LEU A HD12 1 
ATOM   1671  H  HD13 . LEU A 1 101 ? 14.279  10.806  29.831  1.00 10.36  ?  324  LEU A HD13 1 
ATOM   1672  H  HD21 . LEU A 1 101 ? 16.013  9.577   31.789  1.00 9.76   ?  324  LEU A HD21 1 
ATOM   1673  H  HD22 . LEU A 1 101 ? 15.808  8.790   30.424  1.00 9.76   ?  324  LEU A HD22 1 
ATOM   1674  H  HD23 . LEU A 1 101 ? 17.274  9.131   30.932  1.00 9.76   ?  324  LEU A HD23 1 
ATOM   1675  N  N    . GLY A 1 102 ? 17.844  8.697   26.267  1.00 6.50   ?  325  GLY A N    1 
ATOM   1676  C  CA   . GLY A 1 102 ? 18.096  8.431   24.869  1.00 6.17   ?  325  GLY A CA   1 
ATOM   1677  C  C    . GLY A 1 102 ? 19.402  7.727   24.565  1.00 6.36   ?  325  GLY A C    1 
ATOM   1678  O  O    . GLY A 1 102 ? 19.615  7.333   23.412  1.00 6.73   ?  325  GLY A O    1 
ATOM   1679  H  H    . GLY A 1 102 ? 17.397  8.074   26.655  1.00 7.81   ?  325  GLY A H    1 
ATOM   1680  H  HA2  . GLY A 1 102 ? 17.378  7.877   24.527  1.00 7.40   ?  325  GLY A HA2  1 
ATOM   1681  H  HA3  . GLY A 1 102 ? 18.100  9.275   24.391  1.00 7.40   ?  325  GLY A HA3  1 
ATOM   1682  N  N    . THR A 1 103 ? 20.294  7.583   25.539  1.00 5.87   ?  326  THR A N    1 
ATOM   1683  C  CA   . THR A 1 103 ? 21.544  6.866   25.303  1.00 6.19   ?  326  THR A CA   1 
ATOM   1684  C  C    . THR A 1 103 ? 21.231  5.488   24.713  1.00 5.55   ?  326  THR A C    1 
ATOM   1685  O  O    . THR A 1 103 ? 20.247  4.860   25.118  1.00 5.91   ?  326  THR A O    1 
ATOM   1686  C  CB   . THR A 1 103 ? 22.255  6.678   26.654  1.00 6.34   ?  326  THR A CB   1 
ATOM   1687  O  OG1  . THR A 1 103 ? 22.679  7.937   27.180  1.00 7.10   ?  326  THR A OG1  1 
ATOM   1688  C  CG2  . THR A 1 103 ? 23.491  5.800   26.567  1.00 6.41   ?  326  THR A CG2  1 
ATOM   1689  H  H    . THR A 1 103 ? 20.202  7.887   26.338  1.00 7.04   ?  326  THR A H    1 
ATOM   1690  H  HA   . THR A 1 103 ? 22.113  7.356   24.688  1.00 7.43   ?  326  THR A HA   1 
ATOM   1691  H  HB   . THR A 1 103 ? 21.610  6.249   27.238  1.00 7.61   ?  326  THR A HB   1 
ATOM   1692  H  HG1  . THR A 1 103 ? 22.011  8.417   27.350  1.00 8.53   ?  326  THR A HG1  1 
ATOM   1693  H  HG21 . THR A 1 103 ? 23.913  5.732   27.438  1.00 7.69   ?  326  THR A HG21 1 
ATOM   1694  H  HG22 . THR A 1 103 ? 23.246  4.911   26.266  1.00 7.69   ?  326  THR A HG22 1 
ATOM   1695  H  HG23 . THR A 1 103 ? 24.125  6.181   25.939  1.00 7.69   ?  326  THR A HG23 1 
ATOM   1696  N  N    . PRO A 1 104 ? 22.033  4.973   23.769  1.00 5.75   ?  327  PRO A N    1 
ATOM   1697  C  CA   A PRO A 1 104 ? 21.765  3.625   23.247  0.50 6.08   ?  327  PRO A CA   1 
ATOM   1698  C  CA   B PRO A 1 104 ? 21.783  3.622   23.245  0.50 6.17   ?  327  PRO A CA   1 
ATOM   1699  C  C    . PRO A 1 104 ? 21.770  2.570   24.346  1.00 6.32   ?  327  PRO A C    1 
ATOM   1700  O  O    . PRO A 1 104 ? 22.512  2.656   25.323  1.00 6.70   ?  327  PRO A O    1 
ATOM   1701  C  CB   A PRO A 1 104 ? 22.904  3.388   22.245  0.50 6.23   ?  327  PRO A CB   1 
ATOM   1702  C  CB   B PRO A 1 104 ? 22.962  3.396   22.294  0.50 6.48   ?  327  PRO A CB   1 
ATOM   1703  C  CG   A PRO A 1 104 ? 23.944  4.383   22.572  0.50 6.18   ?  327  PRO A CG   1 
ATOM   1704  C  CG   B PRO A 1 104 ? 23.392  4.776   21.921  0.50 6.62   ?  327  PRO A CG   1 
ATOM   1705  C  CD   A PRO A 1 104 ? 23.215  5.572   23.121  0.50 6.08   ?  327  PRO A CD   1 
ATOM   1706  C  CD   B PRO A 1 104 ? 23.213  5.590   23.138  0.50 6.37   ?  327  PRO A CD   1 
ATOM   1707  H  HA   A PRO A 1 104 ? 20.910  3.611   22.788  0.50 7.30   ?  327  PRO A HA   1 
ATOM   1708  H  HA   B PRO A 1 104 ? 20.941  3.599   22.764  0.50 7.41   ?  327  PRO A HA   1 
ATOM   1709  H  HB2  A PRO A 1 104 ? 23.246  2.486   22.347  0.50 7.48   ?  327  PRO A HB2  1 
ATOM   1710  H  HB2  B PRO A 1 104 ? 23.672  2.918   22.750  0.50 7.78   ?  327  PRO A HB2  1 
ATOM   1711  H  HB3  A PRO A 1 104 ? 22.576  3.518   21.341  0.50 7.48   ?  327  PRO A HB3  1 
ATOM   1712  H  HB3  B PRO A 1 104 ? 22.672  2.895   21.515  0.50 7.78   ?  327  PRO A HB3  1 
ATOM   1713  H  HG2  A PRO A 1 104 ? 24.551  4.016   23.234  0.50 7.42   ?  327  PRO A HG2  1 
ATOM   1714  H  HG2  B PRO A 1 104 ? 24.322  4.767   21.646  0.50 7.94   ?  327  PRO A HG2  1 
ATOM   1715  H  HG3  A PRO A 1 104 ? 24.434  4.621   21.769  0.50 7.42   ?  327  PRO A HG3  1 
ATOM   1716  H  HG3  B PRO A 1 104 ? 22.836  5.109   21.199  0.50 7.94   ?  327  PRO A HG3  1 
ATOM   1717  H  HD2  A PRO A 1 104 ? 23.762  6.044   23.769  0.50 7.30   ?  327  PRO A HD2  1 
ATOM   1718  H  HD2  B PRO A 1 104 ? 23.989  5.526   23.716  0.50 7.65   ?  327  PRO A HD2  1 
ATOM   1719  H  HD3  A PRO A 1 104 ? 22.950  6.175   22.409  0.50 7.30   ?  327  PRO A HD3  1 
ATOM   1720  H  HD3  B PRO A 1 104 ? 23.041  6.518   22.914  0.50 7.65   ?  327  PRO A HD3  1 
ATOM   1721  N  N    . ASP A 1 105 ? 20.946  1.532   24.148  1.00 5.91   ?  328  ASP A N    1 
ATOM   1722  C  CA   . ASP A 1 105 ? 20.763  0.453   25.114  1.00 6.03   ?  328  ASP A CA   1 
ATOM   1723  C  C    . ASP A 1 105 ? 21.217  -0.902  24.579  1.00 6.14   ?  328  ASP A C    1 
ATOM   1724  O  O    . ASP A 1 105 ? 20.673  -1.947  24.947  1.00 6.85   ?  328  ASP A O    1 
ATOM   1725  C  CB   . ASP A 1 105 ? 19.313  0.388   25.589  1.00 5.74   ?  328  ASP A CB   1 
ATOM   1726  C  CG   . ASP A 1 105 ? 18.330  0.057   24.484  1.00 6.32   ?  328  ASP A CG   1 
ATOM   1727  O  OD1  . ASP A 1 105 ? 18.761  -0.079  23.309  1.00 5.75   ?  328  ASP A OD1  1 
ATOM   1728  O  OD2  . ASP A 1 105 ? 17.123  -0.079  24.816  1.00 6.60   -1 328  ASP A OD2  1 
ATOM   1729  H  H    . ASP A 1 105 ? 20.470  1.433   23.439  1.00 7.09   ?  328  ASP A H    1 
ATOM   1730  H  HA   . ASP A 1 105 ? 21.323  0.651   25.881  1.00 7.23   ?  328  ASP A HA   1 
ATOM   1731  H  HB2  . ASP A 1 105 ? 19.237  -0.299  26.270  1.00 6.89   ?  328  ASP A HB2  1 
ATOM   1732  H  HB3  . ASP A 1 105 ? 19.066  1.250   25.959  1.00 6.89   ?  328  ASP A HB3  1 
ATOM   1733  N  N    . PHE A 1 106 ? 22.247  -0.902  23.738  1.00 6.04   ?  329  PHE A N    1 
ATOM   1734  C  CA   . PHE A 1 106 ? 22.761  -2.116  23.121  1.00 5.92   ?  329  PHE A CA   1 
ATOM   1735  C  C    . PHE A 1 106 ? 24.268  -1.999  22.986  1.00 6.09   ?  329  PHE A C    1 
ATOM   1736  O  O    . PHE A 1 106 ? 24.824  -0.903  22.992  1.00 6.91   ?  329  PHE A O    1 
ATOM   1737  C  CB   . PHE A 1 106 ? 22.130  -2.369  21.740  1.00 7.03   ?  329  PHE A CB   1 
ATOM   1738  C  CG   . PHE A 1 106 ? 22.225  -1.196  20.809  1.00 6.95   ?  329  PHE A CG   1 
ATOM   1739  C  CD1  . PHE A 1 106 ? 23.366  -0.962  20.070  1.00 8.03   ?  329  PHE A CD1  1 
ATOM   1740  C  CD2  . PHE A 1 106 ? 21.159  -0.315  20.684  1.00 7.55   ?  329  PHE A CD2  1 
ATOM   1741  C  CE1  . PHE A 1 106 ? 23.440  0.134   19.233  1.00 9.03   ?  329  PHE A CE1  1 
ATOM   1742  C  CE2  . PHE A 1 106 ? 21.229  0.761   19.834  1.00 9.02   ?  329  PHE A CE2  1 
ATOM   1743  C  CZ   . PHE A 1 106 ? 22.371  0.991   19.126  1.00 8.98   ?  329  PHE A CZ   1 
ATOM   1744  H  H    . PHE A 1 106 ? 22.675  -0.194  23.505  1.00 7.25   ?  329  PHE A H    1 
ATOM   1745  H  HA   . PHE A 1 106 ? 22.558  -2.875  23.690  1.00 7.10   ?  329  PHE A HA   1 
ATOM   1746  H  HB2  . PHE A 1 106 ? 22.584  -3.117  21.321  1.00 8.44   ?  329  PHE A HB2  1 
ATOM   1747  H  HB3  . PHE A 1 106 ? 21.190  -2.576  21.859  1.00 8.44   ?  329  PHE A HB3  1 
ATOM   1748  H  HD1  . PHE A 1 106 ? 24.088  -1.544  20.135  1.00 9.64   ?  329  PHE A HD1  1 
ATOM   1749  H  HD2  . PHE A 1 106 ? 20.387  -0.457  21.182  1.00 9.07   ?  329  PHE A HD2  1 
ATOM   1750  H  HE1  . PHE A 1 106 ? 24.213  0.292   18.741  1.00 10.83  ?  329  PHE A HE1  1 
ATOM   1751  H  HE2  . PHE A 1 106 ? 20.500  1.331   19.742  1.00 10.83  ?  329  PHE A HE2  1 
ATOM   1752  H  HZ   . PHE A 1 106 ? 22.427  1.733   18.567  1.00 10.78  ?  329  PHE A HZ   1 
ATOM   1753  N  N    . ARG A 1 107 ? 24.912  -3.147  22.792  1.00 6.61   ?  330  ARG A N    1 
ATOM   1754  C  CA   . ARG A 1 107 ? 26.337  -3.228  22.479  1.00 6.24   ?  330  ARG A CA   1 
ATOM   1755  C  C    . ARG A 1 107 ? 26.506  -3.227  20.962  1.00 6.61   ?  330  ARG A C    1 
ATOM   1756  O  O    . ARG A 1 107 ? 25.955  -4.085  20.261  1.00 7.42   ?  330  ARG A O    1 
ATOM   1757  C  CB   . ARG A 1 107 ? 26.952  -4.489  23.082  1.00 7.12   ?  330  ARG A CB   1 
ATOM   1758  C  CG   . ARG A 1 107 ? 27.121  -4.430  24.587  1.00 8.04   ?  330  ARG A CG   1 
ATOM   1759  C  CD   . ARG A 1 107 ? 27.761  -5.686  25.184  1.00 9.69   ?  330  ARG A CD   1 
ATOM   1760  N  NE   . ARG A 1 107 ? 29.107  -5.983  24.674  1.00 12.40  ?  330  ARG A NE   1 
ATOM   1761  C  CZ   . ARG A 1 107 ? 30.252  -5.571  25.217  1.00 13.32  ?  330  ARG A CZ   1 
ATOM   1762  N  NH1  . ARG A 1 107 ? 30.277  -4.823  26.315  1.00 12.84  ?  330  ARG A NH1  1 
ATOM   1763  N  NH2  . ARG A 1 107 ? 31.404  -5.919  24.641  1.00 14.20  ?  330  ARG A NH2  1 
ATOM   1764  H  H    . ARG A 1 107 ? 24.534  -3.918  22.838  1.00 7.94   ?  330  ARG A H    1 
ATOM   1765  H  HA   . ARG A 1 107 ? 26.796  -2.458  22.850  1.00 7.49   ?  330  ARG A HA   1 
ATOM   1766  H  HB2  . ARG A 1 107 ? 26.377  -5.243  22.878  1.00 8.55   ?  330  ARG A HB2  1 
ATOM   1767  H  HB3  . ARG A 1 107 ? 27.829  -4.625  22.691  1.00 8.55   ?  330  ARG A HB3  1 
ATOM   1768  H  HG2  . ARG A 1 107 ? 27.689  -3.675  24.808  1.00 9.65   ?  330  ARG A HG2  1 
ATOM   1769  H  HG3  . ARG A 1 107 ? 26.248  -4.320  24.996  1.00 9.65   ?  330  ARG A HG3  1 
ATOM   1770  H  HD2  . ARG A 1 107 ? 27.831  -5.572  26.145  1.00 11.63  ?  330  ARG A HD2  1 
ATOM   1771  H  HD3  . ARG A 1 107 ? 27.196  -6.448  24.981  1.00 11.63  ?  330  ARG A HD3  1 
ATOM   1772  H  HE   . ARG A 1 107 ? 29.160  -6.464  23.963  1.00 14.88  ?  330  ARG A HE   1 
ATOM   1773  H  HH11 . ARG A 1 107 ? 29.540  -4.593  26.695  1.00 15.41  ?  330  ARG A HH11 1 
ATOM   1774  H  HH12 . ARG A 1 107 ? 31.029  -4.570  26.646  1.00 15.41  ?  330  ARG A HH12 1 
ATOM   1775  H  HH21 . ARG A 1 107 ? 31.400  -6.403  23.930  1.00 17.04  ?  330  ARG A HH21 1 
ATOM   1776  H  HH22 . ARG A 1 107 ? 32.150  -5.660  24.981  1.00 17.04  ?  330  ARG A HH22 1 
ATOM   1777  N  N    . GLY A 1 108 ? 27.263  -2.264  20.455  1.00 6.70   ?  331  GLY A N    1 
ATOM   1778  C  CA   . GLY A 1 108 ? 27.509  -2.189  19.031  1.00 7.62   ?  331  GLY A CA   1 
ATOM   1779  C  C    . GLY A 1 108 ? 28.245  -0.912  18.682  1.00 6.83   ?  331  GLY A C    1 
ATOM   1780  O  O    . GLY A 1 108 ? 28.687  -0.161  19.554  1.00 7.66   ?  331  GLY A O    1 
ATOM   1781  H  H    . GLY A 1 108 ? 27.642  -1.644  20.916  1.00 8.04   ?  331  GLY A H    1 
ATOM   1782  H  HA2  . GLY A 1 108 ? 28.048  -2.946  18.751  1.00 9.15   ?  331  GLY A HA2  1 
ATOM   1783  H  HA3  . GLY A 1 108 ? 26.667  -2.206  18.551  1.00 9.15   ?  331  GLY A HA3  1 
ATOM   1784  N  N    . GLN A 1 109 ? 28.356  -0.692  17.378  1.00 6.36   ?  332  GLN A N    1 
ATOM   1785  C  CA   . GLN A 1 109 ? 29.093  0.435   16.813  1.00 6.61   ?  332  GLN A CA   1 
ATOM   1786  C  C    . GLN A 1 109 ? 28.064  1.367   16.176  1.00 5.88   ?  332  GLN A C    1 
ATOM   1787  O  O    . GLN A 1 109 ? 27.588  1.118   15.064  1.00 6.88   ?  332  GLN A O    1 
ATOM   1788  C  CB   . GLN A 1 109 ? 30.091  -0.065  15.774  1.00 7.73   ?  332  GLN A CB   1 
ATOM   1789  C  CG   . GLN A 1 109 ? 31.111  -1.046  16.307  1.00 8.85   ?  332  GLN A CG   1 
ATOM   1790  C  CD   . GLN A 1 109 ? 31.938  -0.420  17.390  1.00 10.27  ?  332  GLN A CD   1 
ATOM   1791  O  OE1  . GLN A 1 109 ? 32.447  0.672   17.236  1.00 11.72  ?  332  GLN A OE1  1 
ATOM   1792  N  NE2  . GLN A 1 109 ? 32.038  -1.097  18.522  1.00 12.76  ?  332  GLN A NE2  1 
ATOM   1793  H  H    . GLN A 1 109 ? 28.002  -1.198  16.779  1.00 7.64   ?  332  GLN A H    1 
ATOM   1794  H  HA   . GLN A 1 109 ? 29.569  0.912   17.510  1.00 7.93   ?  332  GLN A HA   1 
ATOM   1795  H  HB2  . GLN A 1 109 ? 29.601  -0.507  15.064  1.00 9.28   ?  332  GLN A HB2  1 
ATOM   1796  H  HB3  . GLN A 1 109 ? 30.575  0.697   15.419  1.00 9.28   ?  332  GLN A HB3  1 
ATOM   1797  H  HG2  . GLN A 1 109 ? 30.655  -1.818  16.675  1.00 10.62  ?  332  GLN A HG2  1 
ATOM   1798  H  HG3  . GLN A 1 109 ? 31.701  -1.320  15.588  1.00 10.62  ?  332  GLN A HG3  1 
ATOM   1799  H  HE21 . GLN A 1 109 ? 31.640  -1.855  18.607  1.00 15.31  ?  332  GLN A HE21 1 
ATOM   1800  H  HE22 . GLN A 1 109 ? 32.502  -0.779  19.173  1.00 15.31  ?  332  GLN A HE22 1 
ATOM   1801  N  N    . LEU A 1 110 ? 27.722  2.429   16.890  1.00 5.81   ?  333  LEU A N    1 
ATOM   1802  C  CA   . LEU A 1 110 ? 26.670  3.343   16.457  1.00 6.16   ?  333  LEU A CA   1 
ATOM   1803  C  C    . LEU A 1 110 ? 27.226  4.338   15.442  1.00 6.39   ?  333  LEU A C    1 
ATOM   1804  O  O    . LEU A 1 110 ? 28.139  5.102   15.762  1.00 7.86   ?  333  LEU A O    1 
ATOM   1805  C  CB   . LEU A 1 110 ? 26.117  4.043   17.706  1.00 7.02   ?  333  LEU A CB   1 
ATOM   1806  C  CG   . LEU A 1 110 ? 25.023  5.072   17.486  1.00 7.58   ?  333  LEU A CG   1 
ATOM   1807  C  CD1  . LEU A 1 110 ? 23.770  4.449   16.880  1.00 8.58   ?  333  LEU A CD1  1 
ATOM   1808  C  CD2  . LEU A 1 110 ? 24.685  5.751   18.809  1.00 9.04   ?  333  LEU A CD2  1 
ATOM   1809  H  H    . LEU A 1 110 ? 28.086  2.647   17.638  1.00 6.97   ?  333  LEU A H    1 
ATOM   1810  H  HA   . LEU A 1 110 ? 25.952  2.869   16.009  1.00 7.39   ?  333  LEU A HA   1 
ATOM   1811  H  HB2  . LEU A 1 110 ? 25.752  3.363   18.293  1.00 8.43   ?  333  LEU A HB2  1 
ATOM   1812  H  HB3  . LEU A 1 110 ? 26.852  4.499   18.144  1.00 8.43   ?  333  LEU A HB3  1 
ATOM   1813  H  HG   . LEU A 1 110 ? 25.346  5.735   16.856  1.00 9.10   ?  333  LEU A HG   1 
ATOM   1814  H  HD11 . LEU A 1 110 ? 23.091  5.135   16.785  1.00 10.30  ?  333  LEU A HD11 1 
ATOM   1815  H  HD12 . LEU A 1 110 ? 23.990  4.080   16.010  1.00 10.30  ?  333  LEU A HD12 1 
ATOM   1816  H  HD13 . LEU A 1 110 ? 23.452  3.746   17.467  1.00 10.30  ?  333  LEU A HD13 1 
ATOM   1817  H  HD21 . LEU A 1 110 ? 24.040  6.457   18.645  1.00 10.85  ?  333  LEU A HD21 1 
ATOM   1818  H  HD22 . LEU A 1 110 ? 24.310  5.093   19.414  1.00 10.85  ?  333  LEU A HD22 1 
ATOM   1819  H  HD23 . LEU A 1 110 ? 25.496  6.125   19.188  1.00 10.85  ?  333  LEU A HD23 1 
ATOM   1820  N  N    . TYR A 1 111 ? 26.667  4.333   14.225  1.00 5.73   ?  334  TYR A N    1 
ATOM   1821  C  CA   . TYR A 1 111 ? 27.109  5.169   13.114  1.00 6.26   ?  334  TYR A CA   1 
ATOM   1822  C  C    . TYR A 1 111 ? 26.145  6.331   12.914  1.00 4.88   ?  334  TYR A C    1 
ATOM   1823  O  O    . TYR A 1 111 ? 24.921  6.163   12.947  1.00 5.70   ?  334  TYR A O    1 
ATOM   1824  C  CB   . TYR A 1 111 ? 27.171  4.316   11.845  1.00 6.82   ?  334  TYR A CB   1 
ATOM   1825  C  CG   . TYR A 1 111 ? 27.253  5.081   10.540  1.00 6.07   ?  334  TYR A CG   1 
ATOM   1826  C  CD1  . TYR A 1 111 ? 28.359  5.853   10.226  1.00 6.57   ?  334  TYR A CD1  1 
ATOM   1827  C  CD2  . TYR A 1 111 ? 26.226  5.032   9.628   1.00 6.35   ?  334  TYR A CD2  1 
ATOM   1828  C  CE1  . TYR A 1 111 ? 28.426  6.560   9.026   1.00 6.76   ?  334  TYR A CE1  1 
ATOM   1829  C  CE2  . TYR A 1 111 ? 26.284  5.706   8.442   1.00 7.04   ?  334  TYR A CE2  1 
ATOM   1830  C  CZ   . TYR A 1 111 ? 27.383  6.466   8.131   1.00 6.96   ?  334  TYR A CZ   1 
ATOM   1831  O  OH   . TYR A 1 111 ? 27.410  7.143   6.930   1.00 7.06   ?  334  TYR A OH   1 
ATOM   1832  H  H    . TYR A 1 111 ? 26.002  3.831   14.014  1.00 6.88   ?  334  TYR A H    1 
ATOM   1833  H  HA   . TYR A 1 111 ? 27.985  5.544   13.296  1.00 7.52   ?  334  TYR A HA   1 
ATOM   1834  H  HB2  . TYR A 1 111 ? 27.957  3.751   11.897  1.00 8.18   ?  334  TYR A HB2  1 
ATOM   1835  H  HB3  . TYR A 1 111 ? 26.370  3.769   11.808  1.00 8.18   ?  334  TYR A HB3  1 
ATOM   1836  H  HD1  . TYR A 1 111 ? 29.069  5.900   10.825  1.00 7.89   ?  334  TYR A HD1  1 
ATOM   1837  H  HD2  . TYR A 1 111 ? 25.471  4.525   9.823   1.00 7.62   ?  334  TYR A HD2  1 
ATOM   1838  H  HE1  . TYR A 1 111 ? 29.166  7.088   8.832   1.00 8.11   ?  334  TYR A HE1  1 
ATOM   1839  H  HE2  . TYR A 1 111 ? 25.576  5.649   7.842   1.00 8.45   ?  334  TYR A HE2  1 
ATOM   1840  H  HH   . TYR A 1 111 ? 28.133  7.564   6.853   1.00 8.47   ?  334  TYR A HH   1 
ATOM   1841  N  N    . GLY A 1 112 ? 26.698  7.518   12.712  1.00 5.15   ?  335  GLY A N    1 
ATOM   1842  C  CA   . GLY A 1 112 ? 25.888  8.683   12.443  1.00 5.30   ?  335  GLY A CA   1 
ATOM   1843  C  C    . GLY A 1 112 ? 26.739  9.861   12.041  1.00 5.70   ?  335  GLY A C    1 
ATOM   1844  O  O    . GLY A 1 112 ? 27.838  9.696   11.493  1.00 5.83   ?  335  GLY A O    1 
ATOM   1845  H  H    . GLY A 1 112 ? 27.544  7.672   12.727  1.00 6.18   ?  335  GLY A H    1 
ATOM   1846  H  HA2  . GLY A 1 112 ? 25.268  8.488   11.723  1.00 6.36   ?  335  GLY A HA2  1 
ATOM   1847  H  HA3  . GLY A 1 112 ? 25.385  8.920   13.238  1.00 6.36   ?  335  GLY A HA3  1 
ATOM   1848  N  N    . VAL A 1 113 ? 26.235  11.063  12.304  1.00 5.00   ?  336  VAL A N    1 
ATOM   1849  C  CA   . VAL A 1 113 ? 26.913  12.300  11.932  1.00 5.30   ?  336  VAL A CA   1 
ATOM   1850  C  C    . VAL A 1 113 ? 27.033  13.166  13.169  1.00 5.13   ?  336  VAL A C    1 
ATOM   1851  O  O    . VAL A 1 113 ? 26.044  13.386  13.881  1.00 5.48   ?  336  VAL A O    1 
ATOM   1852  C  CB   . VAL A 1 113 ? 26.177  13.053  10.799  1.00 5.57   ?  336  VAL A CB   1 
ATOM   1853  C  CG1  . VAL A 1 113 ? 26.713  14.452  10.652  1.00 5.66   ?  336  VAL A CG1  1 
ATOM   1854  C  CG2  . VAL A 1 113 ? 26.316  12.272  9.502   1.00 7.81   ?  336  VAL A CG2  1 
ATOM   1855  H  H    . VAL A 1 113 ? 25.485  11.189  12.705  1.00 6.00   ?  336  VAL A H    1 
ATOM   1856  H  HA   . VAL A 1 113 ? 27.807  12.092  11.617  1.00 6.36   ?  336  VAL A HA   1 
ATOM   1857  H  HB   . VAL A 1 113 ? 25.235  13.129  11.017  1.00 6.68   ?  336  VAL A HB   1 
ATOM   1858  H  HG11 . VAL A 1 113 ? 26.436  14.808  9.793   1.00 6.80   ?  336  VAL A HG11 1 
ATOM   1859  H  HG12 . VAL A 1 113 ? 26.360  15.003  11.368  1.00 6.80   ?  336  VAL A HG12 1 
ATOM   1860  H  HG13 . VAL A 1 113 ? 27.682  14.426  10.702  1.00 6.80   ?  336  VAL A HG13 1 
ATOM   1861  H  HG21 . VAL A 1 113 ? 25.834  12.736  8.800   1.00 9.38   ?  336  VAL A HG21 1 
ATOM   1862  H  HG22 . VAL A 1 113 ? 27.256  12.207  9.271   1.00 9.38   ?  336  VAL A HG22 1 
ATOM   1863  H  HG23 . VAL A 1 113 ? 25.944  11.384  9.627   1.00 9.38   ?  336  VAL A HG23 1 
ATOM   1864  N  N    . ILE A 1 114 ? 28.240  13.648  13.430  1.00 4.94   ?  337  ILE A N    1 
ATOM   1865  C  CA   . ILE A 1 114 ? 28.460  14.683  14.433  1.00 5.44   ?  337  ILE A CA   1 
ATOM   1866  C  C    . ILE A 1 114 ? 28.445  16.045  13.748  1.00 4.74   ?  337  ILE A C    1 
ATOM   1867  O  O    . ILE A 1 114 ? 29.175  16.281  12.770  1.00 5.21   ?  337  ILE A O    1 
ATOM   1868  C  CB   . ILE A 1 114 ? 29.766  14.451  15.230  1.00 6.21   ?  337  ILE A CB   1 
ATOM   1869  C  CG1  . ILE A 1 114 ? 30.017  15.608  16.192  1.00 6.70   ?  337  ILE A CG1  1 
ATOM   1870  C  CG2  . ILE A 1 114 ? 30.962  14.200  14.340  1.00 7.41   ?  337  ILE A CG2  1 
ATOM   1871  C  CD1  . ILE A 1 114 ? 31.076  15.315  17.226  1.00 7.70   ?  337  ILE A CD1  1 
ATOM   1872  H  H    . ILE A 1 114 ? 28.958  13.388  13.036  1.00 5.92   ?  337  ILE A H    1 
ATOM   1873  H  HA   . ILE A 1 114 ? 27.729  14.659  15.070  1.00 6.53   ?  337  ILE A HA   1 
ATOM   1874  H  HB   . ILE A 1 114 ? 29.640  13.640  15.748  1.00 7.46   ?  337  ILE A HB   1 
ATOM   1875  H  HG12 . ILE A 1 114 ? 30.306  16.381  15.682  1.00 8.04   ?  337  ILE A HG12 1 
ATOM   1876  H  HG13 . ILE A 1 114 ? 29.192  15.810  16.661  1.00 8.04   ?  337  ILE A HG13 1 
ATOM   1877  H  HG21 . ILE A 1 114 ? 31.755  14.117  14.893  1.00 8.89   ?  337  ILE A HG21 1 
ATOM   1878  H  HG22 . ILE A 1 114 ? 30.819  13.381  13.842  1.00 8.89   ?  337  ILE A HG22 1 
ATOM   1879  H  HG23 . ILE A 1 114 ? 31.063  14.946  13.728  1.00 8.89   ?  337  ILE A HG23 1 
ATOM   1880  H  HD11 . ILE A 1 114 ? 31.070  16.020  17.892  1.00 9.24   ?  337  ILE A HD11 1 
ATOM   1881  H  HD12 . ILE A 1 114 ? 30.882  14.462  17.644  1.00 9.24   ?  337  ILE A HD12 1 
ATOM   1882  H  HD13 . ILE A 1 114 ? 31.942  15.280  16.789  1.00 9.24   ?  337  ILE A HD13 1 
ATOM   1883  N  N    . SER A 1 115 ? 27.599  16.939  14.260  1.00 4.89   ?  338  SER A N    1 
ATOM   1884  C  CA   A SER A 1 115 ? 27.509  18.310  13.792  0.49 5.29   ?  338  SER A CA   1 
ATOM   1885  C  CA   B SER A 1 115 ? 27.490  18.312  13.798  0.51 5.00   ?  338  SER A CA   1 
ATOM   1886  C  C    . SER A 1 115 ? 27.935  19.253  14.905  1.00 5.05   ?  338  SER A C    1 
ATOM   1887  O  O    . SER A 1 115 ? 27.629  19.025  16.081  1.00 6.41   ?  338  SER A O    1 
ATOM   1888  C  CB   A SER A 1 115 ? 26.091  18.649  13.326  0.49 5.63   ?  338  SER A CB   1 
ATOM   1889  C  CB   B SER A 1 115 ? 26.045  18.640  13.431  0.51 4.90   ?  338  SER A CB   1 
ATOM   1890  O  OG   A SER A 1 115 ? 25.115  18.368  14.314  0.49 6.08   ?  338  SER A OG   1 
ATOM   1891  O  OG   B SER A 1 115 ? 25.597  17.851  12.347  0.51 5.33   ?  338  SER A OG   1 
ATOM   1892  H  H    A SER A 1 115 ? 27.052  16.764  14.900  0.49 5.86   ?  338  SER A H    1 
ATOM   1893  H  H    B SER A 1 115 ? 27.058  16.761  14.904  0.51 5.86   ?  338  SER A H    1 
ATOM   1894  H  HA   A SER A 1 115 ? 28.107  18.437  13.039  0.49 6.35   ?  338  SER A HA   1 
ATOM   1895  H  HA   B SER A 1 115 ? 28.055  18.440  13.020  0.51 6.00   ?  338  SER A HA   1 
ATOM   1896  H  HB2  A SER A 1 115 ? 26.053  19.595  13.114  0.49 6.75   ?  338  SER A HB2  1 
ATOM   1897  H  HB2  B SER A 1 115 ? 25.479  18.467  14.200  0.51 5.88   ?  338  SER A HB2  1 
ATOM   1898  H  HB3  A SER A 1 115 ? 25.892  18.124  12.535  0.49 6.75   ?  338  SER A HB3  1 
ATOM   1899  H  HB3  B SER A 1 115 ? 25.989  19.576  13.182  0.51 5.88   ?  338  SER A HB3  1 
ATOM   1900  H  HG   A SER A 1 115 ? 25.271  18.815  15.007  0.49 7.29   ?  338  SER A HG   1 
ATOM   1901  H  HG   B SER A 1 115 ? 26.065  18.004  11.667  0.51 6.40   ?  338  SER A HG   1 
ATOM   1902  N  N    . GLN A 1 116 ? 28.624  20.321  14.528  1.00 5.50   ?  339  GLN A N    1 
ATOM   1903  C  CA   . GLN A 1 116 ? 29.084  21.322  15.468  1.00 5.05   ?  339  GLN A CA   1 
ATOM   1904  C  C    . GLN A 1 116 ? 28.664  22.704  14.994  1.00 5.80   ?  339  GLN A C    1 
ATOM   1905  O  O    . GLN A 1 116 ? 28.667  22.996  13.797  1.00 5.61   ?  339  GLN A O    1 
ATOM   1906  C  CB   . GLN A 1 116 ? 30.602  21.319  15.581  1.00 6.00   ?  339  GLN A CB   1 
ATOM   1907  C  CG   . GLN A 1 116 ? 31.195  19.942  15.836  1.00 6.41   ?  339  GLN A CG   1 
ATOM   1908  C  CD   . GLN A 1 116 ? 32.629  20.022  16.287  1.00 6.87   ?  339  GLN A CD   1 
ATOM   1909  O  OE1  . GLN A 1 116 ? 33.473  20.606  15.603  1.00 7.44   ?  339  GLN A OE1  1 
ATOM   1910  N  NE2  . GLN A 1 116 ? 32.919  19.449  17.441  1.00 6.46   ?  339  GLN A NE2  1 
ATOM   1911  H  H    . GLN A 1 116 ? 28.841  20.488  13.713  1.00 6.60   ?  339  GLN A H    1 
ATOM   1912  H  HA   . GLN A 1 116 ? 28.688  21.141  16.335  1.00 6.06   ?  339  GLN A HA   1 
ATOM   1913  H  HB2  . GLN A 1 116 ? 30.977  21.654  14.751  1.00 7.21   ?  339  GLN A HB2  1 
ATOM   1914  H  HB3  . GLN A 1 116 ? 30.861  21.894  16.318  1.00 7.21   ?  339  GLN A HB3  1 
ATOM   1915  H  HG2  . GLN A 1 116 ? 30.683  19.498  16.530  1.00 7.69   ?  339  GLN A HG2  1 
ATOM   1916  H  HG3  . GLN A 1 116 ? 31.163  19.423  15.017  1.00 7.69   ?  339  GLN A HG3  1 
ATOM   1917  H  HE21 . GLN A 1 116 ? 32.302  19.056  17.893  1.00 7.76   ?  339  GLN A HE21 1 
ATOM   1918  H  HE22 . GLN A 1 116 ? 33.725  19.468  17.740  1.00 7.76   ?  339  GLN A HE22 1 
ATOM   1919  N  N    . ARG A 1 117 ? 28.358  23.570  15.958  1.00 5.67   ?  340  ARG A N    1 
ATOM   1920  C  CA   . ARG A 1 117 ? 28.191  25.002  15.722  1.00 6.14   ?  340  ARG A CA   1 
ATOM   1921  C  C    . ARG A 1 117 ? 28.932  25.683  16.861  1.00 6.15   ?  340  ARG A C    1 
ATOM   1922  O  O    . ARG A 1 117 ? 28.693  25.371  18.030  1.00 6.89   ?  340  ARG A O    1 
ATOM   1923  C  CB   . ARG A 1 117 ? 26.717  25.421  15.682  1.00 6.36   ?  340  ARG A CB   1 
ATOM   1924  C  CG   . ARG A 1 117 ? 26.562  26.941  15.550  1.00 7.55   ?  340  ARG A CG   1 
ATOM   1925  C  CD   . ARG A 1 117 ? 25.125  27.393  15.306  1.00 8.80   ?  340  ARG A CD   1 
ATOM   1926  N  NE   . ARG A 1 117 ? 24.709  27.004  13.977  1.00 8.75   ?  340  ARG A NE   1 
ATOM   1927  C  CZ   . ARG A 1 117 ? 23.772  26.123  13.661  1.00 8.76   ?  340  ARG A CZ   1 
ATOM   1928  N  NH1  . ARG A 1 117 ? 22.877  25.703  14.539  1.00 11.21  ?  340  ARG A NH1  1 
ATOM   1929  N  NH2  . ARG A 1 117 ? 23.722  25.669  12.423  1.00 7.80   ?  340  ARG A NH2  1 
ATOM   1930  H  H    . ARG A 1 117 ? 28.239  23.346  16.780  1.00 6.80   ?  340  ARG A H    1 
ATOM   1931  H  HA   . ARG A 1 117 ? 28.559  25.270  14.866  1.00 7.37   ?  340  ARG A HA   1 
ATOM   1932  H  HB2  . ARG A 1 117 ? 26.287  25.004  14.919  1.00 7.63   ?  340  ARG A HB2  1 
ATOM   1933  H  HB3  . ARG A 1 117 ? 26.282  25.140  16.502  1.00 7.63   ?  340  ARG A HB3  1 
ATOM   1934  H  HG2  . ARG A 1 117 ? 26.867  27.358  16.371  1.00 9.07   ?  340  ARG A HG2  1 
ATOM   1935  H  HG3  . ARG A 1 117 ? 27.099  27.246  14.802  1.00 9.07   ?  340  ARG A HG3  1 
ATOM   1936  H  HD2  . ARG A 1 117 ? 24.535  26.975  15.952  1.00 10.57  ?  340  ARG A HD2  1 
ATOM   1937  H  HD3  . ARG A 1 117 ? 25.068  28.359  15.381  1.00 10.57  ?  340  ARG A HD3  1 
ATOM   1938  H  HE   . ARG A 1 117 ? 25.114  27.386  13.321  1.00 10.50  ?  340  ARG A HE   1 
ATOM   1939  H  HH11 . ARG A 1 117 ? 22.892  26.003  15.345  1.00 13.45  ?  340  ARG A HH11 1 
ATOM   1940  H  HH12 . ARG A 1 117 ? 22.281  25.130  14.305  1.00 13.45  ?  340  ARG A HH12 1 
ATOM   1941  H  HH21 . ARG A 1 117 ? 24.290  25.946  11.840  1.00 9.36   ?  340  ARG A HH21 1 
ATOM   1942  H  HH22 . ARG A 1 117 ? 23.120  25.097  12.199  1.00 9.36   ?  340  ARG A HH22 1 
ATOM   1943  N  N    . ASP A 1 118 ? 29.865  26.564  16.531  1.00 6.68   ?  341  ASP A N    1 
ATOM   1944  C  CA   . ASP A 1 118 ? 30.773  27.095  17.543  1.00 7.11   ?  341  ASP A CA   1 
ATOM   1945  C  C    . ASP A 1 118 ? 30.041  27.995  18.540  1.00 7.69   ?  341  ASP A C    1 
ATOM   1946  O  O    . ASP A 1 118 ? 28.988  28.564  18.261  1.00 8.14   ?  341  ASP A O    1 
ATOM   1947  C  CB   . ASP A 1 118 ? 31.971  27.760  16.850  1.00 10.31  ?  341  ASP A CB   1 
ATOM   1948  C  CG   . ASP A 1 118 ? 32.856  26.706  16.097  1.00 11.72  ?  341  ASP A CG   1 
ATOM   1949  O  OD1  . ASP A 1 118 ? 32.502  25.517  16.135  1.00 14.15  -1 341  ASP A OD1  1 
ATOM   1950  O  OD2  . ASP A 1 118 ? 33.907  27.038  15.517  1.00 15.84  ?  341  ASP A OD2  1 
ATOM   1951  H  H    . ASP A 1 118 ? 29.993  26.870  15.738  1.00 8.02   ?  341  ASP A H    1 
ATOM   1952  H  HA   . ASP A 1 118 ? 31.141  26.385  18.094  1.00 8.53   ?  341  ASP A HA   1 
ATOM   1953  H  HB2  . ASP A 1 118 ? 31.650  28.407  16.203  1.00 12.37  ?  341  ASP A HB2  1 
ATOM   1954  H  HB3  . ASP A 1 118 ? 32.522  28.202  17.515  1.00 12.37  ?  341  ASP A HB3  1 
ATOM   1955  N  N    . ARG A 1 119 ? 30.586  28.056  19.756  1.00 8.71   ?  342  ARG A N    1 
ATOM   1956  C  CA   . ARG A 1 119 ? 29.885  28.745  20.840  1.00 10.46  ?  342  ARG A CA   1 
ATOM   1957  C  C    . ARG A 1 119 ? 29.963  30.257  20.718  1.00 11.87  ?  342  ARG A C    1 
ATOM   1958  O  O    . ARG A 1 119 ? 29.076  30.958  21.215  1.00 13.66  ?  342  ARG A O    1 
ATOM   1959  C  CB   . ARG A 1 119 ? 30.321  28.248  22.228  1.00 12.82  ?  342  ARG A CB   1 
ATOM   1960  C  CG   . ARG A 1 119 ? 31.785  28.276  22.541  1.00 13.59  ?  342  ARG A CG   1 
ATOM   1961  C  CD   . ARG A 1 119 ? 32.042  27.719  23.968  1.00 12.44  ?  342  ARG A CD   1 
ATOM   1962  N  NE   . ARG A 1 119 ? 31.754  26.294  24.150  1.00 12.83  ?  342  ARG A NE   1 
ATOM   1963  C  CZ   . ARG A 1 119 ? 32.591  25.304  23.851  1.00 11.86  ?  342  ARG A CZ   1 
ATOM   1964  N  NH1  . ARG A 1 119 ? 33.787  25.541  23.346  1.00 11.41  ?  342  ARG A NH1  1 
ATOM   1965  N  NH2  . ARG A 1 119 ? 32.201  24.042  24.029  1.00 13.17  ?  342  ARG A NH2  1 
ATOM   1966  H  H    . ARG A 1 119 ? 31.344  27.715  19.975  1.00 10.45  ?  342  ARG A H    1 
ATOM   1967  H  HA   . ARG A 1 119 ? 28.946  28.508  20.779  1.00 12.55  ?  342  ARG A HA   1 
ATOM   1968  H  HB2  . ARG A 1 119 ? 29.881  28.799  22.894  1.00 15.39  ?  342  ARG A HB2  1 
ATOM   1969  H  HB3  . ARG A 1 119 ? 30.032  27.326  22.318  1.00 15.39  ?  342  ARG A HB3  1 
ATOM   1970  H  HG2  . ARG A 1 119 ? 32.265  27.727  21.902  1.00 16.31  ?  342  ARG A HG2  1 
ATOM   1971  H  HG3  . ARG A 1 119 ? 32.109  29.190  22.502  1.00 16.31  ?  342  ARG A HG3  1 
ATOM   1972  H  HD2  . ARG A 1 119 ? 32.977  27.854  24.185  1.00 14.93  ?  342  ARG A HD2  1 
ATOM   1973  H  HD3  . ARG A 1 119 ? 31.482  28.207  24.592  1.00 14.93  ?  342  ARG A HD3  1 
ATOM   1974  H  HE   . ARG A 1 119 ? 30.987  26.081  24.473  1.00 15.39  ?  342  ARG A HE   1 
ATOM   1975  H  HH11 . ARG A 1 119 ? 34.041  26.350  23.203  1.00 13.69  ?  342  ARG A HH11 1 
ATOM   1976  H  HH12 . ARG A 1 119 ? 34.312  24.886  23.161  1.00 13.69  ?  342  ARG A HH12 1 
ATOM   1977  H  HH21 . ARG A 1 119 ? 31.414  23.874  24.334  1.00 15.81  ?  342  ARG A HH21 1 
ATOM   1978  H  HH22 . ARG A 1 119 ? 32.735  23.396  23.839  1.00 15.81  ?  342  ARG A HH22 1 
ATOM   1979  N  N    . GLU A 1 120 ? 30.992  30.780  20.067  1.00 11.54  ?  343  GLU A N    1 
ATOM   1980  C  CA   . GLU A 1 120 ? 31.107  32.214  19.842  1.00 12.72  ?  343  GLU A CA   1 
ATOM   1981  C  C    . GLU A 1 120 ? 31.236  32.486  18.351  1.00 10.53  ?  343  GLU A C    1 
ATOM   1982  O  O    . GLU A 1 120 ? 31.688  31.634  17.586  1.00 10.78  ?  343  GLU A O    1 
ATOM   1983  C  CB   . GLU A 1 120 ? 32.305  32.816  20.580  1.00 15.08  ?  343  GLU A CB   1 
ATOM   1984  C  CG   . GLU A 1 120 ? 32.080  32.938  22.083  1.00 25.80  ?  343  GLU A CG   1 
ATOM   1985  C  CD   . GLU A 1 120 ? 30.865  33.784  22.424  1.00 171.78 ?  343  GLU A CD   1 
ATOM   1986  O  OE1  . GLU A 1 120 ? 30.558  34.721  21.658  1.00 61.62  ?  343  GLU A OE1  1 
ATOM   1987  O  OE2  . GLU A 1 120 ? 30.208  33.504  23.448  1.00 39.22  -1 343  GLU A OE2  1 
ATOM   1988  H  H    . GLU A 1 120 ? 31.642  30.320  19.743  1.00 13.85  ?  343  GLU A H    1 
ATOM   1989  H  HA   . GLU A 1 120 ? 30.308  32.652  20.173  1.00 15.26  ?  343  GLU A HA   1 
ATOM   1990  H  HB2  . GLU A 1 120 ? 33.080  32.249  20.438  1.00 18.10  ?  343  GLU A HB2  1 
ATOM   1991  H  HB3  . GLU A 1 120 ? 32.476  33.705  20.230  1.00 18.10  ?  343  GLU A HB3  1 
ATOM   1992  H  HG2  . GLU A 1 120 ? 31.945  32.053  22.456  1.00 30.96  ?  343  GLU A HG2  1 
ATOM   1993  H  HG3  . GLU A 1 120 ? 32.858  33.353  22.487  1.00 30.96  ?  343  GLU A HG3  1 
ATOM   1994  N  N    . GLY A 1 121 ? 30.797  33.674  17.944  1.00 10.87  ?  344  GLY A N    1 
ATOM   1995  C  CA   . GLY A 1 121 ? 30.927  34.072  16.562  1.00 10.28  ?  344  GLY A CA   1 
ATOM   1996  C  C    . GLY A 1 121 ? 32.369  34.293  16.148  1.00 10.14  ?  344  GLY A C    1 
ATOM   1997  O  O    . GLY A 1 121 ? 33.276  34.460  16.964  1.00 11.61  ?  344  GLY A O    1 
ATOM   1998  H  H    . GLY A 1 121 ? 30.423  34.259  18.450  1.00 13.05  ?  344  GLY A H    1 
ATOM   1999  H  HA2  . GLY A 1 121 ? 30.549  33.383  15.994  1.00 12.34  ?  344  GLY A HA2  1 
ATOM   2000  H  HA3  . GLY A 1 121 ? 30.440  34.899  16.421  1.00 12.34  ?  344  GLY A HA3  1 
ATOM   2001  N  N    . THR A 1 122 ? 32.566  34.314  14.829  1.00 9.10   ?  345  THR A N    1 
ATOM   2002  C  CA   . THR A 1 122 ? 33.876  34.528  14.235  1.00 9.19   ?  345  THR A CA   1 
ATOM   2003  C  C    . THR A 1 122 ? 33.987  35.982  13.810  1.00 8.89   ?  345  THR A C    1 
ATOM   2004  O  O    . THR A 1 122 ? 33.216  36.428  12.939  1.00 9.56   ?  345  THR A O    1 
ATOM   2005  C  CB   . THR A 1 122 ? 34.030  33.591  13.037  1.00 9.16   ?  345  THR A CB   1 
ATOM   2006  O  OG1  . THR A 1 122 ? 34.134  32.252  13.524  1.00 9.63   ?  345  THR A OG1  1 
ATOM   2007  C  CG2  . THR A 1 122 ? 35.270  33.889  12.231  1.00 9.42   ?  345  THR A CG2  1 
ATOM   2008  H  H    . THR A 1 122 ? 31.940  34.204  14.248  1.00 10.93  ?  345  THR A H    1 
ATOM   2009  H  HA   . THR A 1 122 ? 34.587  34.346  14.869  1.00 11.03  ?  345  THR A HA   1 
ATOM   2010  H  HB   . THR A 1 122 ? 33.264  33.706  12.453  1.00 10.99  ?  345  THR A HB   1 
ATOM   2011  H  HG1  . THR A 1 122 ? 33.428  32.036  13.923  1.00 11.56  ?  345  THR A HG1  1 
ATOM   2012  H  HG21 . THR A 1 122 ? 35.439  33.169  11.604  1.00 11.31  ?  345  THR A HG21 1 
ATOM   2013  H  HG22 . THR A 1 122 ? 35.154  34.716  11.737  1.00 11.31  ?  345  THR A HG22 1 
ATOM   2014  H  HG23 . THR A 1 122 ? 36.035  33.979  12.820  1.00 11.31  ?  345  THR A HG23 1 
ATOM   2015  N  N    . PRO A 1 123 ? 34.907  36.774  14.389  1.00 9.99   ?  346  PRO A N    1 
ATOM   2016  C  CA   A PRO A 1 123 ? 34.908  38.216  14.103  0.51 11.03  ?  346  PRO A CA   1 
ATOM   2017  C  CA   B PRO A 1 123 ? 34.892  38.216  14.101  0.49 10.73  ?  346  PRO A CA   1 
ATOM   2018  C  C    . PRO A 1 123 ? 35.191  38.566  12.653  1.00 9.99   ?  346  PRO A C    1 
ATOM   2019  O  O    . PRO A 1 123 ? 34.747  39.622  12.191  1.00 11.42  ?  346  PRO A O    1 
ATOM   2020  C  CB   A PRO A 1 123 ? 35.980  38.755  15.062  0.51 12.30  ?  346  PRO A CB   1 
ATOM   2021  C  CB   B PRO A 1 123 ? 35.933  38.785  15.078  0.49 11.36  ?  346  PRO A CB   1 
ATOM   2022  C  CG   A PRO A 1 123 ? 35.983  37.785  16.198  0.51 12.31  ?  346  PRO A CG   1 
ATOM   2023  C  CG   B PRO A 1 123 ? 36.831  37.657  15.376  0.49 10.66  ?  346  PRO A CG   1 
ATOM   2024  C  CD   A PRO A 1 123 ? 35.731  36.449  15.569  0.51 10.79  ?  346  PRO A CD   1 
ATOM   2025  C  CD   B PRO A 1 123 ? 35.965  36.421  15.352  0.49 10.45  ?  346  PRO A CD   1 
ATOM   2026  H  HA   A PRO A 1 123 ? 34.050  38.598  14.341  0.51 13.24  ?  346  PRO A HA   1 
ATOM   2027  H  HA   B PRO A 1 123 ? 34.024  38.583  14.327  0.49 12.87  ?  346  PRO A HA   1 
ATOM   2028  H  HB2  A PRO A 1 123 ? 36.843  38.777  14.619  0.51 14.76  ?  346  PRO A HB2  1 
ATOM   2029  H  HB2  B PRO A 1 123 ? 36.417  39.513  14.657  0.49 13.63  ?  346  PRO A HB2  1 
ATOM   2030  H  HB3  A PRO A 1 123 ? 35.739  39.645  15.364  0.51 14.76  ?  346  PRO A HB3  1 
ATOM   2031  H  HB3  B PRO A 1 123 ? 35.493  39.101  15.882  0.49 13.63  ?  346  PRO A HB3  1 
ATOM   2032  H  HG2  A PRO A 1 123 ? 36.844  37.801  16.645  0.51 14.78  ?  346  PRO A HG2  1 
ATOM   2033  H  HG2  B PRO A 1 123 ? 37.524  37.603  14.699  0.49 12.80  ?  346  PRO A HG2  1 
ATOM   2034  H  HG3  A PRO A 1 123 ? 35.279  38.010  16.827  0.51 14.78  ?  346  PRO A HG3  1 
ATOM   2035  H  HG3  B PRO A 1 123 ? 37.231  37.780  16.251  0.49 12.80  ?  346  PRO A HG3  1 
ATOM   2036  H  HD2  A PRO A 1 123 ? 36.565  36.032  15.303  0.51 12.95  ?  346  PRO A HD2  1 
ATOM   2037  H  HD2  B PRO A 1 123 ? 36.469  35.651  15.046  0.49 12.54  ?  346  PRO A HD2  1 
ATOM   2038  H  HD3  A PRO A 1 123 ? 35.248  35.868  16.177  0.51 12.95  ?  346  PRO A HD3  1 
ATOM   2039  H  HD3  B PRO A 1 123 ? 35.590  36.245  16.229  0.49 12.54  ?  346  PRO A HD3  1 
ATOM   2040  N  N    . SER A 1 124 ? 35.907  37.718  11.916  1.00 9.65   ?  347  SER A N    1 
ATOM   2041  C  CA   . SER A 1 124 ? 36.189  37.987  10.506  1.00 10.07  ?  347  SER A CA   1 
ATOM   2042  C  C    . SER A 1 124 ? 35.068  37.539  9.578   1.00 9.81   ?  347  SER A C    1 
ATOM   2043  O  O    . SER A 1 124 ? 35.213  37.670  8.351   1.00 10.12  ?  347  SER A O    1 
ATOM   2044  C  CB   . SER A 1 124 ? 37.514  37.341  10.094  1.00 11.54  ?  347  SER A CB   1 
ATOM   2045  O  OG   . SER A 1 124 ? 37.459  35.919  10.221  1.00 11.85  ?  347  SER A OG   1 
ATOM   2046  H  H    . SER A 1 124 ? 36.241  36.982  12.209  1.00 11.59  ?  347  SER A H    1 
ATOM   2047  H  HA   . SER A 1 124 ? 36.292  38.944  10.390  1.00 12.09  ?  347  SER A HA   1 
ATOM   2048  H  HB2  . SER A 1 124 ? 37.699  37.566  9.168   1.00 13.85  ?  347  SER A HB2  1 
ATOM   2049  H  HB3  . SER A 1 124 ? 38.220  37.681  10.665  1.00 13.85  ?  347  SER A HB3  1 
ATOM   2050  H  HG   . SER A 1 124 ? 37.306  35.708  11.019  1.00 14.22  ?  347  SER A HG   1 
ATOM   2051  N  N    . GLU A 1 125 ? 33.979  37.018  10.136  1.00 8.38   ?  348  GLU A N    1 
ATOM   2052  C  CA   . GLU A 1 125 ? 32.782  36.622  9.393   1.00 8.92   ?  348  GLU A CA   1 
ATOM   2053  C  C    . GLU A 1 125 ? 31.555  37.309  9.969   1.00 8.95   ?  348  GLU A C    1 
ATOM   2054  O  O    . GLU A 1 125 ? 30.500  36.697  10.152  1.00 9.94   ?  348  GLU A O    1 
ATOM   2055  C  CB   . GLU A 1 125 ? 32.601  35.108  9.391   1.00 9.31   ?  348  GLU A CB   1 
ATOM   2056  C  CG   . GLU A 1 125 ? 33.659  34.346  8.626   1.00 9.66   ?  348  GLU A CG   1 
ATOM   2057  C  CD   . GLU A 1 125 ? 33.523  34.462  7.111   1.00 9.88   ?  348  GLU A CD   1 
ATOM   2058  O  OE1  . GLU A 1 125 ? 32.496  34.959  6.605   1.00 9.70   ?  348  GLU A OE1  1 
ATOM   2059  O  OE2  . GLU A 1 125 ? 34.450  34.005  6.412   1.00 11.84  -1 348  GLU A OE2  1 
ATOM   2060  H  H    . GLU A 1 125 ? 33.905  36.878  10.981  1.00 10.06  ?  348  GLU A H    1 
ATOM   2061  H  HA   . GLU A 1 125 ? 32.885  36.906  8.472   1.00 10.71  ?  348  GLU A HA   1 
ATOM   2062  H  HB2  . GLU A 1 125 ? 32.621  34.794  10.309  1.00 11.17  ?  348  GLU A HB2  1 
ATOM   2063  H  HB3  . GLU A 1 125 ? 31.743  34.901  8.989   1.00 11.17  ?  348  GLU A HB3  1 
ATOM   2064  H  HG2  . GLU A 1 125 ? 34.531  34.691  8.873   1.00 11.59  ?  348  GLU A HG2  1 
ATOM   2065  H  HG3  . GLU A 1 125 ? 33.596  33.407  8.858   1.00 11.59  ?  348  GLU A HG3  1 
ATOM   2066  N  N    . ASN A 1 126 ? 31.682  38.599  10.281  1.00 10.36  ?  349  ASN A N    1 
ATOM   2067  C  CA   A ASN A 1 126 ? 30.582  39.411  10.811  0.42 11.45  ?  349  ASN A CA   1 
ATOM   2068  C  CA   B ASN A 1 126 ? 30.561  39.386  10.788  0.58 11.30  ?  349  ASN A CA   1 
ATOM   2069  C  C    . ASN A 1 126 ? 29.943  38.764  12.040  1.00 10.46  ?  349  ASN A C    1 
ATOM   2070  O  O    . ASN A 1 126 ? 28.734  38.869  12.270  1.00 12.13  ?  349  ASN A O    1 
ATOM   2071  C  CB   A ASN A 1 126 ? 29.536  39.726  9.731   0.42 13.69  ?  349  ASN A CB   1 
ATOM   2072  C  CB   B ASN A 1 126 ? 29.467  39.572  9.725   0.58 13.29  ?  349  ASN A CB   1 
ATOM   2073  C  CG   A ASN A 1 126 ? 28.514  40.762  10.180  0.42 15.96  ?  349  ASN A CG   1 
ATOM   2074  C  CG   B ASN A 1 126 ? 29.951  40.317  8.503   0.58 15.15  ?  349  ASN A CG   1 
ATOM   2075  O  OD1  A ASN A 1 126 ? 28.837  41.692  10.918  0.42 17.21  ?  349  ASN A OD1  1 
ATOM   2076  O  OD1  B ASN A 1 126 ? 29.946  39.782  7.394   0.58 15.34  ?  349  ASN A OD1  1 
ATOM   2077  N  ND2  A ASN A 1 126 ? 27.269  40.593  9.745   0.42 16.59  ?  349  ASN A ND2  1 
ATOM   2078  N  ND2  B ASN A 1 126 ? 30.343  41.569  8.689   0.58 16.25  ?  349  ASN A ND2  1 
ATOM   2079  H  H    A ASN A 1 126 ? 32.415  39.040  10.194  0.42 12.43  ?  349  ASN A H    1 
ATOM   2080  H  H    B ASN A 1 126 ? 32.414  39.043  10.208  0.58 12.43  ?  349  ASN A H    1 
ATOM   2081  H  HA   A ASN A 1 126 ? 30.951  40.260  11.101  0.42 13.74  ?  349  ASN A HA   1 
ATOM   2082  H  HA   B ASN A 1 126 ? 30.911  40.259  11.024  0.58 13.56  ?  349  ASN A HA   1 
ATOM   2083  H  HB2  A ASN A 1 126 ? 29.988  40.072  8.945   0.42 16.43  ?  349  ASN A HB2  1 
ATOM   2084  H  HB2  B ASN A 1 126 ? 29.153  38.700  9.439   0.58 15.95  ?  349  ASN A HB2  1 
ATOM   2085  H  HB3  A ASN A 1 126 ? 29.058  38.912  9.507   0.42 16.43  ?  349  ASN A HB3  1 
ATOM   2086  H  HB3  B ASN A 1 126 ? 28.734  40.077  10.112  0.58 15.95  ?  349  ASN A HB3  1 
ATOM   2087  H  HD21 A ASN A 1 126 ? 26.655  41.151  9.971   0.42 19.91  ?  349  ASN A HD21 1 
ATOM   2088  H  HD21 B ASN A 1 126 ? 30.627  42.034  8.024   0.58 19.50  ?  349  ASN A HD21 1 
ATOM   2089  H  HD22 A ASN A 1 126 ? 27.078  39.925  9.238   0.42 19.91  ?  349  ASN A HD22 1 
ATOM   2090  H  HD22 B ASN A 1 126 ? 30.313  41.917  9.476   0.58 19.50  ?  349  ASN A HD22 1 
ATOM   2091  N  N    . ASN A 1 127 ? 30.752  38.089  12.850  0.88 8.35   ?  350  ASN A N    1 
ATOM   2092  C  CA   . ASN A 1 127 ? 30.312  37.458  14.093  0.88 8.94   ?  350  ASN A CA   1 
ATOM   2093  C  C    . ASN A 1 127 ? 29.374  36.269  13.875  0.88 7.68   ?  350  ASN A C    1 
ATOM   2094  O  O    . ASN A 1 127 ? 28.706  35.830  14.816  0.88 8.81   ?  350  ASN A O    1 
ATOM   2095  C  CB   . ASN A 1 127 ? 29.680  38.479  15.058  0.88 12.99  ?  350  ASN A CB   1 
ATOM   2096  C  CG   . ASN A 1 127 ? 29.577  37.970  16.491  0.88 17.79  ?  350  ASN A CG   1 
ATOM   2097  O  OD1  . ASN A 1 127 ? 30.486  37.314  16.996  0.88 20.06  ?  350  ASN A OD1  1 
ATOM   2098  N  ND2  . ASN A 1 127 ? 28.464  38.281  17.154  0.88 19.88  ?  350  ASN A ND2  1 
ATOM   2099  H  H    . ASN A 1 127 ? 31.591  37.980  12.695  0.88 10.02  ?  350  ASN A H    1 
ATOM   2100  H  HA   . ASN A 1 127 ? 31.101  37.100  14.529  0.88 10.74  ?  350  ASN A HA   1 
ATOM   2101  H  HB2  . ASN A 1 127 ? 30.224  39.283  15.065  0.88 15.59  ?  350  ASN A HB2  1 
ATOM   2102  H  HB3  . ASN A 1 127 ? 28.784  38.689  14.751  0.88 15.59  ?  350  ASN A HB3  1 
ATOM   2103  H  HD21 . ASN A 1 127 ? 27.850  38.746  16.771  0.88 23.86  ?  350  ASN A HD21 1 
ATOM   2104  H  HD22 . ASN A 1 127 ? 28.359  38.016  17.966  0.88 23.86  ?  350  ASN A HD22 1 
ATOM   2105  N  N    . GLN A 1 128 ? 29.312  35.726  12.667  1.00 8.44   ?  351  GLN A N    1 
ATOM   2106  C  CA   . GLN A 1 128 ? 28.566  34.502  12.453  1.00 7.62   ?  351  GLN A CA   1 
ATOM   2107  C  C    . GLN A 1 128 ? 29.321  33.316  13.042  1.00 7.13   ?  351  GLN A C    1 
ATOM   2108  O  O    . GLN A 1 128 ? 30.549  33.330  13.151  1.00 8.08   ?  351  GLN A O    1 
ATOM   2109  C  CB   . GLN A 1 128 ? 28.397  34.260  10.962  1.00 7.70   ?  351  GLN A CB   1 
ATOM   2110  C  CG   . GLN A 1 128 ? 27.521  35.261  10.265  1.00 9.31   ?  351  GLN A CG   1 
ATOM   2111  C  CD   . GLN A 1 128 ? 27.311  34.886  8.819   1.00 10.13  ?  351  GLN A CD   1 
ATOM   2112  O  OE1  . GLN A 1 128 ? 28.207  35.017  7.990   1.00 11.27  ?  351  GLN A OE1  1 
ATOM   2113  N  NE2  . GLN A 1 128 ? 26.134  34.369  8.516   1.00 10.88  ?  351  GLN A NE2  1 
ATOM   2114  H  H    . GLN A 1 128 ? 29.689  36.045  11.963  1.00 10.13  ?  351  GLN A H    1 
ATOM   2115  H  HA   . GLN A 1 128 ? 27.695  34.575  12.875  1.00 9.15   ?  351  GLN A HA   1 
ATOM   2116  H  HB2  . GLN A 1 128 ? 29.272  34.293  10.543  1.00 9.24   ?  351  GLN A HB2  1 
ATOM   2117  H  HB3  . GLN A 1 128 ? 28.001  33.384  10.834  1.00 9.24   ?  351  GLN A HB3  1 
ATOM   2118  H  HG2  . GLN A 1 128 ? 26.656  35.292  10.703  1.00 11.17  ?  351  GLN A HG2  1 
ATOM   2119  H  HG3  . GLN A 1 128 ? 27.941  36.134  10.298  1.00 11.17  ?  351  GLN A HG3  1 
ATOM   2120  H  HE21 . GLN A 1 128 ? 25.540  34.263  9.129   1.00 13.06  ?  351  GLN A HE21 1 
ATOM   2121  H  HE22 . GLN A 1 128 ? 25.961  34.138  7.706   1.00 13.06  ?  351  GLN A HE22 1 
ATOM   2122  N  N    . LYS A 1 129 ? 28.569  32.280  13.401  1.00 7.31   ?  352  LYS A N    1 
ATOM   2123  C  CA   A LYS A 1 129 ? 29.157  31.084  13.976  0.64 7.26   ?  352  LYS A CA   1 
ATOM   2124  C  CA   B LYS A 1 129 ? 29.123  31.066  13.982  0.36 7.14   ?  352  LYS A CA   1 
ATOM   2125  C  C    . LYS A 1 129 ? 29.602  30.115  12.892  1.00 6.45   ?  352  LYS A C    1 
ATOM   2126  O  O    . LYS A 1 129 ? 28.900  29.894  11.901  1.00 6.72   ?  352  LYS A O    1 
ATOM   2127  C  CB   A LYS A 1 129 ? 28.149  30.406  14.903  0.64 8.36   ?  352  LYS A CB   1 
ATOM   2128  C  CB   B LYS A 1 129 ? 28.042  30.321  14.776  0.36 7.83   ?  352  LYS A CB   1 
ATOM   2129  C  CG   A LYS A 1 129 ? 27.919  31.194  16.190  0.64 9.45   ?  352  LYS A CG   1 
ATOM   2130  C  CG   B LYS A 1 129 ? 27.335  31.118  15.869  0.36 9.01   ?  352  LYS A CG   1 
ATOM   2131  C  CD   A LYS A 1 129 ? 26.705  30.700  16.928  0.64 10.43  ?  352  LYS A CD   1 
ATOM   2132  C  CD   B LYS A 1 129 ? 28.305  31.610  16.920  0.36 9.89   ?  352  LYS A CD   1 
ATOM   2133  C  CE   A LYS A 1 129 ? 26.471  31.485  18.202  0.64 11.88  ?  352  LYS A CE   1 
ATOM   2134  C  CE   B LYS A 1 129 ? 27.616  31.836  18.256  0.36 11.09  ?  352  LYS A CE   1 
ATOM   2135  N  NZ   A LYS A 1 129 ? 25.213  31.060  18.846  0.64 13.65  ?  352  LYS A NZ   1 
ATOM   2136  N  NZ   B LYS A 1 129 ? 27.283  30.545  18.918  0.36 12.54  ?  352  LYS A NZ   1 
ATOM   2137  H  H    A LYS A 1 129 ? 27.713  32.249  13.320  0.64 8.77   ?  352  LYS A H    1 
ATOM   2138  H  H    B LYS A 1 129 ? 27.713  32.256  13.316  0.36 8.77   ?  352  LYS A H    1 
ATOM   2139  H  HA   A LYS A 1 129 ? 29.945  31.328  14.487  0.64 8.72   ?  352  LYS A HA   1 
ATOM   2140  H  HA   B LYS A 1 129 ? 29.864  31.312  14.559  0.36 8.56   ?  352  LYS A HA   1 
ATOM   2141  H  HB2  A LYS A 1 129 ? 27.299  30.326  14.442  0.64 10.04  ?  352  LYS A HB2  1 
ATOM   2142  H  HB2  B LYS A 1 129 ? 27.360  30.026  14.152  0.36 9.39   ?  352  LYS A HB2  1 
ATOM   2143  H  HB3  A LYS A 1 129 ? 28.481  29.527  15.142  0.64 10.04  ?  352  LYS A HB3  1 
ATOM   2144  H  HB3  B LYS A 1 129 ? 28.455  29.555  15.204  0.36 9.39   ?  352  LYS A HB3  1 
ATOM   2145  H  HG2  A LYS A 1 129 ? 28.690  31.094  16.770  0.64 11.35  ?  352  LYS A HG2  1 
ATOM   2146  H  HG2  B LYS A 1 129 ? 26.899  31.889  15.473  0.36 10.81  ?  352  LYS A HG2  1 
ATOM   2147  H  HG3  A LYS A 1 129 ? 27.785  32.130  15.975  0.64 11.35  ?  352  LYS A HG3  1 
ATOM   2148  H  HG3  B LYS A 1 129 ? 26.677  30.553  16.303  0.36 10.81  ?  352  LYS A HG3  1 
ATOM   2149  H  HD2  A LYS A 1 129 ? 25.924  30.797  16.362  0.64 12.52  ?  352  LYS A HD2  1 
ATOM   2150  H  HD2  B LYS A 1 129 ? 29.004  30.949  17.046  0.36 11.87  ?  352  LYS A HD2  1 
ATOM   2151  H  HD3  A LYS A 1 129 ? 26.830  29.767  17.163  0.64 12.52  ?  352  LYS A HD3  1 
ATOM   2152  H  HD3  B LYS A 1 129 ? 28.692  32.451  16.631  0.36 11.87  ?  352  LYS A HD3  1 
ATOM   2153  H  HE2  A LYS A 1 129 ? 27.203  31.329  18.819  0.64 14.26  ?  352  LYS A HE2  1 
ATOM   2154  H  HE2  B LYS A 1 129 ? 28.205  32.336  18.842  0.36 13.31  ?  352  LYS A HE2  1 
ATOM   2155  H  HE3  A LYS A 1 129 ? 26.408  32.430  17.994  0.64 14.26  ?  352  LYS A HE3  1 
ATOM   2156  H  HE3  B LYS A 1 129 ? 26.792  32.328  18.115  0.36 13.31  ?  352  LYS A HE3  1 
ATOM   2157  H  HZ1  A LYS A 1 129 ? 25.247  30.191  19.036  0.64 16.39  ?  352  LYS A HZ1  1 
ATOM   2158  H  HZ1  B LYS A 1 129 ? 26.681  30.102  18.435  0.36 15.05  ?  352  LYS A HZ1  1 
ATOM   2159  H  HZ2  A LYS A 1 129 ? 25.089  31.515  19.601  0.64 16.39  ?  352  LYS A HZ2  1 
ATOM   2160  H  HZ2  B LYS A 1 129 ? 28.016  30.045  18.995  0.36 15.05  ?  352  LYS A HZ2  1 
ATOM   2161  H  HZ3  A LYS A 1 129 ? 24.526  31.210  18.301  0.64 16.39  ?  352  LYS A HZ3  1 
ATOM   2162  H  HZ3  B LYS A 1 129 ? 26.949  30.695  19.729  0.36 15.05  ?  352  LYS A HZ3  1 
ATOM   2163  N  N    . ALA A 1 130 ? 30.770  29.513  13.109  1.00 6.18   ?  353  ALA A N    1 
ATOM   2164  C  CA   . ALA A 1 130 ? 31.285  28.469  12.245  1.00 6.42   ?  353  ALA A CA   1 
ATOM   2165  C  C    . ALA A 1 130 ? 30.610  27.137  12.548  1.00 6.34   ?  353  ALA A C    1 
ATOM   2166  O  O    . ALA A 1 130 ? 30.136  26.886  13.665  1.00 6.61   ?  353  ALA A O    1 
ATOM   2167  C  CB   . ALA A 1 130 ? 32.789  28.308  12.465  1.00 7.01   ?  353  ALA A CB   1 
ATOM   2168  H  H    . ALA A 1 130 ? 31.291  29.699  13.768  1.00 7.42   ?  353  ALA A H    1 
ATOM   2169  H  HA   . ALA A 1 130 ? 31.112  28.708  11.321  1.00 7.71   ?  353  ALA A HA   1 
ATOM   2170  H  HB1  . ALA A 1 130 ? 33.153  27.747  11.762  1.00 8.41   ?  353  ALA A HB1  1 
ATOM   2171  H  HB2  . ALA A 1 130 ? 33.207  29.183  12.441  1.00 8.41   ?  353  ALA A HB2  1 
ATOM   2172  H  HB3  . ALA A 1 130 ? 32.939  27.894  13.330  1.00 8.41   ?  353  ALA A HB3  1 
ATOM   2173  N  N    . ASN A 1 131 ? 30.603  26.261  11.534  1.00 5.77   ?  354  ASN A N    1 
ATOM   2174  C  CA   . ASN A 1 131 ? 29.922  24.975  11.595  1.00 5.41   ?  354  ASN A CA   1 
ATOM   2175  C  C    . ASN A 1 131 ? 30.773  23.912  10.914  1.00 5.30   ?  354  ASN A C    1 
ATOM   2176  O  O    . ASN A 1 131 ? 31.524  24.205  9.983   1.00 5.74   ?  354  ASN A O    1 
ATOM   2177  C  CB   . ASN A 1 131 ? 28.596  24.988  10.804  1.00 5.36   ?  354  ASN A CB   1 
ATOM   2178  C  CG   . ASN A 1 131 ? 27.591  25.994  11.318  1.00 5.69   ?  354  ASN A CG   1 
ATOM   2179  O  OD1  . ASN A 1 131 ? 26.634  25.635  12.013  1.00 5.72   ?  354  ASN A OD1  1 
ATOM   2180  N  ND2  . ASN A 1 131 ? 27.769  27.248  10.942  1.00 6.41   ?  354  ASN A ND2  1 
ATOM   2181  H  H    . ASN A 1 131 ? 30.998  26.400  10.782  1.00 6.92   ?  354  ASN A H    1 
ATOM   2182  H  HA   . ASN A 1 131 ? 29.775  24.768  12.531  1.00 6.50   ?  354  ASN A HA   1 
ATOM   2183  H  HB2  . ASN A 1 131 ? 28.786  25.205  9.878   1.00 6.43   ?  354  ASN A HB2  1 
ATOM   2184  H  HB3  . ASN A 1 131 ? 28.190  24.109  10.861  1.00 6.43   ?  354  ASN A HB3  1 
ATOM   2185  H  HD21 . ASN A 1 131 ? 27.224  27.859  11.208  1.00 7.69   ?  354  ASN A HD21 1 
ATOM   2186  H  HD22 . ASN A 1 131 ? 28.430  27.455  10.432  1.00 7.69   ?  354  ASN A HD22 1 
ATOM   2187  N  N    . ARG A 1 132 ? 30.575  22.663  11.315  1.00 4.71   ?  355  ARG A N    1 
ATOM   2188  C  CA   . ARG A 1 132 ? 31.089  21.535  10.550  1.00 5.37   ?  355  ARG A CA   1 
ATOM   2189  C  C    . ARG A 1 132 ? 30.320  20.287  10.948  1.00 5.35   ?  355  ARG A C    1 
ATOM   2190  O  O    . ARG A 1 132 ? 29.945  20.138  12.112  1.00 5.86   ?  355  ARG A O    1 
ATOM   2191  C  CB   . ARG A 1 132 ? 32.594  21.341  10.774  1.00 6.12   ?  355  ARG A CB   1 
ATOM   2192  C  CG   . ARG A 1 132 ? 32.988  21.005  12.187  1.00 6.71   ?  355  ARG A CG   1 
ATOM   2193  C  CD   . ARG A 1 132 ? 34.379  21.534  12.533  1.00 7.07   ?  355  ARG A CD   1 
ATOM   2194  N  NE   . ARG A 1 132 ? 34.456  22.989  12.507  1.00 8.22   ?  355  ARG A NE   1 
ATOM   2195  C  CZ   . ARG A 1 132 ? 33.991  23.800  13.446  1.00 9.04   ?  355  ARG A CZ   1 
ATOM   2196  N  NH1  . ARG A 1 132 ? 33.411  23.343  14.543  1.00 8.47   ?  355  ARG A NH1  1 
ATOM   2197  N  NH2  . ARG A 1 132 ? 34.094  25.114  13.269  1.00 9.39   ?  355  ARG A NH2  1 
ATOM   2198  H  H    . ARG A 1 132 ? 30.146  22.441  12.027  1.00 5.66   ?  355  ARG A H    1 
ATOM   2199  H  HA   . ARG A 1 132 ? 30.945  21.692  9.603   1.00 6.45   ?  355  ARG A HA   1 
ATOM   2200  H  HB2  . ARG A 1 132 ? 32.898  20.614  10.207  1.00 7.34   ?  355  ARG A HB2  1 
ATOM   2201  H  HB3  . ARG A 1 132 ? 33.050  22.162  10.533  1.00 7.34   ?  355  ARG A HB3  1 
ATOM   2202  H  HG2  . ARG A 1 132 ? 32.350  21.404  12.799  1.00 8.05   ?  355  ARG A HG2  1 
ATOM   2203  H  HG3  . ARG A 1 132 ? 32.994  20.041  12.296  1.00 8.05   ?  355  ARG A HG3  1 
ATOM   2204  H  HD2  . ARG A 1 132 ? 34.616  21.238  13.426  1.00 8.49   ?  355  ARG A HD2  1 
ATOM   2205  H  HD3  . ARG A 1 132 ? 35.017  21.189  11.890  1.00 8.49   ?  355  ARG A HD3  1 
ATOM   2206  H  HE   . ARG A 1 132 ? 34.834  23.351  11.825  1.00 9.87   ?  355  ARG A HE   1 
ATOM   2207  H  HH11 . ARG A 1 132 ? 33.327  22.495  14.664  1.00 10.17  ?  355  ARG A HH11 1 
ATOM   2208  H  HH12 . ARG A 1 132 ? 33.119  23.893  15.136  1.00 10.17  ?  355  ARG A HH12 1 
ATOM   2209  H  HH21 . ARG A 1 132 ? 34.458  25.424  12.554  1.00 11.27  ?  355  ARG A HH21 1 
ATOM   2210  H  HH22 . ARG A 1 132 ? 33.797  25.653  13.869  1.00 11.27  ?  355  ARG A HH22 1 
ATOM   2211  N  N    . SER A 1 133 ? 30.122  19.380  9.985   1.00 5.16   ?  356  SER A N    1 
ATOM   2212  C  CA   . SER A 1 133 ? 29.536  18.072  10.258  1.00 5.39   ?  356  SER A CA   1 
ATOM   2213  C  C    . SER A 1 133 ? 30.315  17.003  9.509   1.00 5.03   ?  356  SER A C    1 
ATOM   2214  O  O    . SER A 1 133 ? 30.729  17.231  8.369   1.00 5.27   ?  356  SER A O    1 
ATOM   2215  C  CB   . SER A 1 133 ? 28.088  18.000  9.784   1.00 5.32   ?  356  SER A CB   1 
ATOM   2216  O  OG   . SER A 1 133 ? 27.241  18.951  10.425  1.00 6.27   ?  356  SER A OG   1 
ATOM   2217  H  H    . SER A 1 133 ? 30.321  19.504  9.157   1.00 6.19   ?  356  SER A H    1 
ATOM   2218  H  HA   . SER A 1 133 ? 29.580  17.904  11.213  1.00 6.47   ?  356  SER A HA   1 
ATOM   2219  H  HB2  . SER A 1 133 ? 28.070  18.169  8.828   1.00 6.38   ?  356  SER A HB2  1 
ATOM   2220  H  HB3  . SER A 1 133 ? 27.748  17.111  9.970   1.00 6.38   ?  356  SER A HB3  1 
ATOM   2221  H  HG   . SER A 1 133 ? 27.516  19.730  10.273  1.00 7.52   ?  356  SER A HG   1 
ATOM   2222  N  N    . HIS A 1 134 ? 30.489  15.839  10.152  1.00 4.73   ?  357  HIS A N    1 
ATOM   2223  C  CA   . HIS A 1 134 ? 31.193  14.711  9.565   1.00 4.69   ?  357  HIS A CA   1 
ATOM   2224  C  C    . HIS A 1 134 ? 30.607  13.424  10.120  1.00 4.90   ?  357  HIS A C    1 
ATOM   2225  O  O    . HIS A 1 134 ? 29.997  13.414  11.191  1.00 5.72   ?  357  HIS A O    1 
ATOM   2226  C  CB   . HIS A 1 134 ? 32.674  14.774  9.918   1.00 6.45   ?  357  HIS A CB   1 
ATOM   2227  C  CG   . HIS A 1 134 ? 33.337  15.998  9.389   1.00 6.33   ?  357  HIS A CG   1 
ATOM   2228  N  ND1  . HIS A 1 134 ? 33.614  16.178  8.051   1.00 6.63   ?  357  HIS A ND1  1 
ATOM   2229  C  CD2  . HIS A 1 134 ? 33.737  17.128  10.026  1.00 7.49   ?  357  HIS A CD2  1 
ATOM   2230  C  CE1  . HIS A 1 134 ? 34.187  17.361  7.895   1.00 7.19   ?  357  HIS A CE1  1 
ATOM   2231  N  NE2  . HIS A 1 134 ? 34.276  17.951  9.076   1.00 7.88   ?  357  HIS A NE2  1 
ATOM   2232  H  H    . HIS A 1 134 ? 30.200  15.683  10.947  1.00 5.67   ?  357  HIS A H    1 
ATOM   2233  H  HA   . HIS A 1 134 ? 31.078  14.718  8.602   1.00 5.63   ?  357  HIS A HA   1 
ATOM   2234  H  HB2  . HIS A 1 134 ? 32.769  14.774  10.884  1.00 7.74   ?  357  HIS A HB2  1 
ATOM   2235  H  HB3  . HIS A 1 134 ? 33.122  14.002  9.541   1.00 7.74   ?  357  HIS A HB3  1 
ATOM   2236  H  HD2  . HIS A 1 134 ? 33.660  17.308  10.935  1.00 8.99   ?  357  HIS A HD2  1 
ATOM   2237  H  HE1  . HIS A 1 134 ? 34.479  17.718  7.087   1.00 8.63   ?  357  HIS A HE1  1 
ATOM   2238  H  HE2  . HIS A 1 134 ? 34.616  18.727  9.222   1.00 9.46   ?  357  HIS A HE2  1 
ATOM   2239  N  N    . GLN A 1 135 ? 30.850  12.322  9.408   1.00 5.47   ?  358  GLN A N    1 
ATOM   2240  C  CA   . GLN A 1 135 ? 30.464  11.015  9.913   1.00 5.50   ?  358  GLN A CA   1 
ATOM   2241  C  C    . GLN A 1 135 ? 31.269  10.655  11.150  1.00 5.47   ?  358  GLN A C    1 
ATOM   2242  O  O    . GLN A 1 135 ? 32.443  11.003  11.275  1.00 6.49   ?  358  GLN A O    1 
ATOM   2243  C  CB   . GLN A 1 135 ? 30.721  9.945   8.862   1.00 5.85   ?  358  GLN A CB   1 
ATOM   2244  C  CG   . GLN A 1 135 ? 29.890  10.094  7.615   1.00 6.90   ?  358  GLN A CG   1 
ATOM   2245  C  CD   . GLN A 1 135 ? 30.392  9.223   6.490   1.00 7.06   ?  358  GLN A CD   1 
ATOM   2246  O  OE1  . GLN A 1 135 ? 29.825  8.163   6.198   1.00 7.25   ?  358  GLN A OE1  1 
ATOM   2247  N  NE2  . GLN A 1 135 ? 31.442  9.667   5.843   1.00 8.27   ?  358  GLN A NE2  1 
ATOM   2248  H  H    . GLN A 1 135 ? 31.234  12.309  8.638   1.00 6.57   ?  358  GLN A H    1 
ATOM   2249  H  HA   . GLN A 1 135 ? 29.520  11.034  10.135  1.00 6.61   ?  358  GLN A HA   1 
ATOM   2250  H  HB2  . GLN A 1 135 ? 31.654  9.985   8.600   1.00 7.02   ?  358  GLN A HB2  1 
ATOM   2251  H  HB3  . GLN A 1 135 ? 30.521  9.077   9.247   1.00 7.02   ?  358  GLN A HB3  1 
ATOM   2252  H  HG2  . GLN A 1 135 ? 28.974  9.839   7.809   1.00 8.28   ?  358  GLN A HG2  1 
ATOM   2253  H  HG3  . GLN A 1 135 ? 29.921  11.018  7.319   1.00 8.28   ?  358  GLN A HG3  1 
ATOM   2254  H  HE21 . GLN A 1 135 ? 31.802  10.415  6.069   1.00 9.92   ?  358  GLN A HE21 1 
ATOM   2255  H  HE22 . GLN A 1 135 ? 31.770  9.211   5.192   1.00 9.92   ?  358  GLN A HE22 1 
ATOM   2256  N  N    . GLY A 1 136 ? 30.634  9.929   12.068  1.00 5.92   ?  359  GLY A N    1 
ATOM   2257  C  CA   . GLY A 1 136 ? 31.333  9.421   13.231  1.00 7.28   ?  359  GLY A CA   1 
ATOM   2258  C  C    . GLY A 1 136 ? 30.721  8.121   13.700  1.00 6.22   ?  359  GLY A C    1 
ATOM   2259  O  O    . GLY A 1 136 ? 29.600  7.756   13.322  1.00 7.12   ?  359  GLY A O    1 
ATOM   2260  H  H    . GLY A 1 136 ? 29.800  9.720   12.035  1.00 7.11   ?  359  GLY A H    1 
ATOM   2261  H  HA2  . GLY A 1 136 ? 32.265  9.266   13.012  1.00 8.74   ?  359  GLY A HA2  1 
ATOM   2262  H  HA3  . GLY A 1 136 ? 31.281  10.068  13.952  1.00 8.74   ?  359  GLY A HA3  1 
ATOM   2263  N  N    . VAL A 1 137 ? 31.490  7.412   14.521  1.00 6.52   ?  360  VAL A N    1 
ATOM   2264  C  CA   A VAL A 1 137 ? 31.065  6.157   15.125  0.83 6.24   ?  360  VAL A CA   1 
ATOM   2265  C  CA   B VAL A 1 137 ? 31.043  6.170   15.129  0.17 6.20   ?  360  VAL A CA   1 
ATOM   2266  C  C    . VAL A 1 137 ? 31.293  6.253   16.623  1.00 6.52   ?  360  VAL A C    1 
ATOM   2267  O  O    . VAL A 1 137 ? 32.382  6.650   17.065  1.00 7.25   ?  360  VAL A O    1 
ATOM   2268  C  CB   A VAL A 1 137 ? 31.827  4.942   14.555  0.83 6.97   ?  360  VAL A CB   1 
ATOM   2269  C  CB   B VAL A 1 137 ? 31.735  4.935   14.524  0.17 5.80   ?  360  VAL A CB   1 
ATOM   2270  C  CG1  A VAL A 1 137 ? 31.425  3.653   15.313  0.83 6.60   ?  360  VAL A CG1  1 
ATOM   2271  C  CG1  B VAL A 1 137 ? 31.081  4.555   13.203  0.17 6.31   ?  360  VAL A CG1  1 
ATOM   2272  C  CG2  A VAL A 1 137 ? 31.580  4.804   13.086  0.83 9.23   ?  360  VAL A CG2  1 
ATOM   2273  C  CG2  B VAL A 1 137 ? 33.207  5.201   14.343  0.17 5.31   ?  360  VAL A CG2  1 
ATOM   2274  H  H    A VAL A 1 137 ? 32.286  7.647   14.749  0.83 7.83   ?  360  VAL A H    1 
ATOM   2275  H  H    B VAL A 1 137 ? 32.290  7.638   14.743  0.17 7.83   ?  360  VAL A H    1 
ATOM   2276  H  HA   A VAL A 1 137 ? 30.119  6.032   14.953  0.83 7.49   ?  360  VAL A HA   1 
ATOM   2277  H  HA   B VAL A 1 137 ? 30.088  6.074   14.982  0.17 7.44   ?  360  VAL A HA   1 
ATOM   2278  H  HB   A VAL A 1 137 ? 32.780  5.078   14.679  0.83 8.36   ?  360  VAL A HB   1 
ATOM   2279  H  HB   B VAL A 1 137 ? 31.638  4.183   15.130  0.17 6.96   ?  360  VAL A HB   1 
ATOM   2280  H  HG11 A VAL A 1 137 ? 31.725  2.882   14.806  0.83 7.92   ?  360  VAL A HG11 1 
ATOM   2281  H  HG11 B VAL A 1 137 ? 31.578  3.825   12.802  0.17 7.58   ?  360  VAL A HG11 1 
ATOM   2282  H  HG12 A VAL A 1 137 ? 31.845  3.658   16.188  0.83 7.92   ?  360  VAL A HG12 1 
ATOM   2283  H  HG12 B VAL A 1 137 ? 30.166  4.279   13.371  0.17 7.58   ?  360  VAL A HG12 1 
ATOM   2284  H  HG13 A VAL A 1 137 ? 30.460  3.631   15.409  0.83 7.92   ?  360  VAL A HG13 1 
ATOM   2285  H  HG13 B VAL A 1 137 ? 31.091  5.325   12.613  0.17 7.58   ?  360  VAL A HG13 1 
ATOM   2286  H  HG21 A VAL A 1 137 ? 32.190  4.143   12.724  0.83 11.08  ?  360  VAL A HG21 1 
ATOM   2287  H  HG21 B VAL A 1 137 ? 33.648  4.375   14.087  0.17 6.37   ?  360  VAL A HG21 1 
ATOM   2288  H  HG22 A VAL A 1 137 ? 30.663  4.521   12.945  0.83 11.08  ?  360  VAL A HG22 1 
ATOM   2289  H  HG22 B VAL A 1 137 ? 33.325  5.867   13.648  0.17 6.37   ?  360  VAL A HG22 1 
ATOM   2290  H  HG23 A VAL A 1 137 ? 31.731  5.662   12.659  0.83 11.08  ?  360  VAL A HG23 1 
ATOM   2291  H  HG23 B VAL A 1 137 ? 33.574  5.526   15.179  0.17 6.37   ?  360  VAL A HG23 1 
ATOM   2292  N  N    . ILE A 1 138 ? 30.278  5.890   17.398  1.00 6.00   ?  361  ILE A N    1 
ATOM   2293  C  CA   . ILE A 1 138 ? 30.375  5.805   18.848  1.00 6.20   ?  361  ILE A CA   1 
ATOM   2294  C  C    . ILE A 1 138 ? 30.283  4.328   19.204  1.00 6.18   ?  361  ILE A C    1 
ATOM   2295  O  O    . ILE A 1 138 ? 29.224  3.701   19.055  1.00 7.61   ?  361  ILE A O    1 
ATOM   2296  C  CB   . ILE A 1 138 ? 29.289  6.641   19.535  1.00 6.70   ?  361  ILE A CB   1 
ATOM   2297  C  CG1  . ILE A 1 138 ? 29.514  8.122   19.220  1.00 7.45   ?  361  ILE A CG1  1 
ATOM   2298  C  CG2  . ILE A 1 138 ? 29.309  6.412   21.032  1.00 7.90   ?  361  ILE A CG2  1 
ATOM   2299  C  CD1  . ILE A 1 138 ? 28.390  9.024   19.667  1.00 8.20   ?  361  ILE A CD1  1 
ATOM   2300  H  H    . ILE A 1 138 ? 29.499  5.683   17.096  1.00 7.20   ?  361  ILE A H    1 
ATOM   2301  H  HA   . ILE A 1 138 ? 31.234  6.136   19.151  1.00 7.44   ?  361  ILE A HA   1 
ATOM   2302  H  HB   . ILE A 1 138 ? 28.421  6.368   19.198  1.00 8.05   ?  361  ILE A HB   1 
ATOM   2303  H  HG12 . ILE A 1 138 ? 30.323  8.415   19.668  1.00 8.95   ?  361  ILE A HG12 1 
ATOM   2304  H  HG13 . ILE A 1 138 ? 29.610  8.224   18.261  1.00 8.95   ?  361  ILE A HG13 1 
ATOM   2305  H  HG21 . ILE A 1 138 ? 28.690  7.028   21.454  1.00 9.48   ?  361  ILE A HG21 1 
ATOM   2306  H  HG22 . ILE A 1 138 ? 29.042  5.497   21.215  1.00 9.48   ?  361  ILE A HG22 1 
ATOM   2307  H  HG23 . ILE A 1 138 ? 30.207  6.566   21.363  1.00 9.48   ?  361  ILE A HG23 1 
ATOM   2308  H  HD11 . ILE A 1 138 ? 28.527  9.908   19.291  1.00 9.84   ?  361  ILE A HD11 1 
ATOM   2309  H  HD12 . ILE A 1 138 ? 27.548  8.659   19.355  1.00 9.84   ?  361  ILE A HD12 1 
ATOM   2310  H  HD13 . ILE A 1 138 ? 28.390  9.073   20.636  1.00 9.84   ?  361  ILE A HD13 1 
ATOM   2311  N  N    . SER A 1 139 ? 31.390  3.773   19.696  1.00 6.44   ?  362  SER A N    1 
ATOM   2312  C  CA   . SER A 1 139 ? 31.406  2.408   20.182  1.00 6.95   ?  362  SER A CA   1 
ATOM   2313  C  C    . SER A 1 139 ? 30.771  2.354   21.563  1.00 6.88   ?  362  SER A C    1 
ATOM   2314  O  O    . SER A 1 139 ? 31.267  2.996   22.496  1.00 8.14   ?  362  SER A O    1 
ATOM   2315  C  CB   . SER A 1 139 ? 32.836  1.901   20.276  1.00 7.64   ?  362  SER A CB   1 
ATOM   2316  O  OG   . SER A 1 139 ? 32.793  0.631   20.896  1.00 9.09   ?  362  SER A OG   1 
ATOM   2317  H  H    . SER A 1 139 ? 32.148  4.175   19.757  1.00 7.73   ?  362  SER A H    1 
ATOM   2318  H  HA   . SER A 1 139 ? 30.902  1.850   19.569  1.00 8.34   ?  362  SER A HA   1 
ATOM   2319  H  HB2  . SER A 1 139 ? 33.217  1.821   19.387  1.00 9.17   ?  362  SER A HB2  1 
ATOM   2320  H  HB3  . SER A 1 139 ? 33.368  2.511   20.810  1.00 9.17   ?  362  SER A HB3  1 
ATOM   2321  H  HG   . SER A 1 139 ? 33.571  0.327   20.982  1.00 10.91  ?  362  SER A HG   1 
ATOM   2322  N  N    . THR A 1 140 ? 29.703  1.575   21.711  1.00 6.13   ?  363  THR A N    1 
ATOM   2323  C  CA   . THR A 1 140 ? 29.085  1.443   23.024  1.00 6.22   ?  363  THR A CA   1 
ATOM   2324  C  C    . THR A 1 140 ? 29.758  0.376   23.870  1.00 6.74   ?  363  THR A C    1 
ATOM   2325  O  O    . THR A 1 140 ? 29.346  0.170   25.016  1.00 8.12   ?  363  THR A O    1 
ATOM   2326  C  CB   . THR A 1 140 ? 27.584  1.173   22.953  1.00 6.63   ?  363  THR A CB   1 
ATOM   2327  O  OG1  . THR A 1 140 ? 27.376  -0.158  22.493  1.00 6.84   ?  363  THR A OG1  1 
ATOM   2328  C  CG2  . THR A 1 140 ? 26.885  2.158   22.026  1.00 7.43   ?  363  THR A CG2  1 
ATOM   2329  H  H    . THR A 1 140 ? 29.329  1.125   21.081  1.00 7.36   ?  363  THR A H    1 
ATOM   2330  H  HA   . THR A 1 140 ? 29.169  2.302   23.467  1.00 7.47   ?  363  THR A HA   1 
ATOM   2331  H  HB   . THR A 1 140 ? 27.191  1.282   23.834  1.00 7.95   ?  363  THR A HB   1 
ATOM   2332  H  HG1  . THR A 1 140 ? 26.555  -0.332  22.475  1.00 8.21   ?  363  THR A HG1  1 
ATOM   2333  H  HG21 . THR A 1 140 ? 25.926  2.018   22.055  1.00 8.91   ?  363  THR A HG21 1 
ATOM   2334  H  HG22 . THR A 1 140 ? 27.079  3.068   22.301  1.00 8.91   ?  363  THR A HG22 1 
ATOM   2335  H  HG23 . THR A 1 140 ? 27.194  2.032   21.115  1.00 8.91   ?  363  THR A HG23 1 
ATOM   2336  N  N    . ILE A 1 141 ? 30.803  -0.267  23.342  1.00 7.47   ?  364  ILE A N    1 
ATOM   2337  C  CA   . ILE A 1 141 ? 31.579  -1.252  24.093  1.00 9.25   ?  364  ILE A CA   1 
ATOM   2338  C  C    . ILE A 1 141 ? 32.944  -0.741  24.524  1.00 9.35   ?  364  ILE A C    1 
ATOM   2339  O  O    . ILE A 1 141 ? 33.640  -1.432  25.270  1.00 10.62  ?  364  ILE A O    1 
ATOM   2340  C  CB   . ILE A 1 141 ? 31.710  -2.586  23.331  1.00 10.36  ?  364  ILE A CB   1 
ATOM   2341  C  CG1  . ILE A 1 141 ? 32.579  -2.438  22.084  1.00 11.12  ?  364  ILE A CG1  1 
ATOM   2342  C  CG2  . ILE A 1 141 ? 30.338  -3.111  22.925  1.00 10.66  ?  364  ILE A CG2  1 
ATOM   2343  C  CD1  . ILE A 1 141 ? 32.979  -3.768  21.508  1.00 11.74  ?  364  ILE A CD1  1 
ATOM   2344  H  H    . ILE A 1 141 ? 31.085  -0.148  22.538  1.00 8.96   ?  364  ILE A H    1 
ATOM   2345  H  HA   . ILE A 1 141 ? 31.090  -1.446  24.908  1.00 11.10  ?  364  ILE A HA   1 
ATOM   2346  H  HB   . ILE A 1 141 ? 32.136  -3.215  23.934  1.00 12.44  ?  364  ILE A HB   1 
ATOM   2347  H  HG12 . ILE A 1 141 ? 32.083  -1.952  21.407  1.00 13.35  ?  364  ILE A HG12 1 
ATOM   2348  H  HG13 . ILE A 1 141 ? 33.386  -1.953  22.316  1.00 13.35  ?  364  ILE A HG13 1 
ATOM   2349  H  HG21 . ILE A 1 141 ? 30.444  -3.978  22.502  1.00 12.79  ?  364  ILE A HG21 1 
ATOM   2350  H  HG22 . ILE A 1 141 ? 29.785  -3.195  23.717  1.00 12.79  ?  364  ILE A HG22 1 
ATOM   2351  H  HG23 . ILE A 1 141 ? 29.932  -2.487  22.303  1.00 12.79  ?  364  ILE A HG23 1 
ATOM   2352  H  HD11 . ILE A 1 141 ? 33.654  -3.626  20.826  1.00 14.09  ?  364  ILE A HD11 1 
ATOM   2353  H  HD12 . ILE A 1 141 ? 33.338  -4.324  22.217  1.00 14.09  ?  364  ILE A HD12 1 
ATOM   2354  H  HD13 . ILE A 1 141 ? 32.198  -4.191  21.118  1.00 14.09  ?  364  ILE A HD13 1 
ATOM   2355  N  N    . SER A 1 142 ? 33.347  0.436   24.093  1.00 9.34   ?  365  SER A N    1 
ATOM   2356  C  CA   . SER A 1 142 ? 34.647  0.962   24.459  1.00 9.52   ?  365  SER A CA   1 
ATOM   2357  C  C    . SER A 1 142 ? 34.704  1.223   25.959  1.00 9.15   ?  365  SER A C    1 
ATOM   2358  O  O    . SER A 1 142 ? 33.710  1.634   26.559  1.00 8.65   ?  365  SER A O    1 
ATOM   2359  C  CB   . SER A 1 142 ? 34.834  2.297   23.743  1.00 10.75  ?  365  SER A CB   1 
ATOM   2360  O  OG   . SER A 1 142 ? 35.919  3.022   24.280  1.00 11.53  ?  365  SER A OG   1 
ATOM   2361  H  H    . SER A 1 142 ? 32.887  0.955   23.585  1.00 11.20  ?  365  SER A H    1 
ATOM   2362  H  HA   . SER A 1 142 ? 35.349  0.336   24.220  1.00 11.43  ?  365  SER A HA   1 
ATOM   2363  H  HB2  . SER A 1 142 ? 35.005  2.127   22.804  1.00 12.90  ?  365  SER A HB2  1 
ATOM   2364  H  HB3  . SER A 1 142 ? 34.025  2.822   23.844  1.00 12.90  ?  365  SER A HB3  1 
ATOM   2365  H  HG   . SER A 1 142 ? 36.640  2.623   24.118  1.00 13.84  ?  365  SER A HG   1 
ATOM   2366  N  N    . PRO A 1 143 ? 35.869  1.053   26.589  1.00 10.25  ?  366  PRO A N    1 
ATOM   2367  C  CA   A PRO A 1 143 ? 36.027  1.502   27.982  0.45 10.74  ?  366  PRO A CA   1 
ATOM   2368  C  CA   B PRO A 1 143 ? 35.994  1.490   27.989  0.55 10.72  ?  366  PRO A CA   1 
ATOM   2369  C  C    . PRO A 1 143 ? 35.780  2.986   28.161  1.00 9.97   ?  366  PRO A C    1 
ATOM   2370  O  O    . PRO A 1 143 ? 35.564  3.436   29.291  1.00 10.49  ?  366  PRO A O    1 
ATOM   2371  C  CB   A PRO A 1 143 ? 37.483  1.138   28.310  0.45 12.18  ?  366  PRO A CB   1 
ATOM   2372  C  CB   B PRO A 1 143 ? 37.413  1.061   28.384  0.55 12.37  ?  366  PRO A CB   1 
ATOM   2373  C  CG   A PRO A 1 143 ? 37.821  0.029   27.369  0.45 12.23  ?  366  PRO A CG   1 
ATOM   2374  C  CG   B PRO A 1 143 ? 38.155  0.966   27.101  0.55 12.04  ?  366  PRO A CG   1 
ATOM   2375  C  CD   A PRO A 1 143 ? 37.027  0.268   26.120  0.45 11.38  ?  366  PRO A CD   1 
ATOM   2376  C  CD   B PRO A 1 143 ? 37.148  0.552   26.052  0.55 11.41  ?  366  PRO A CD   1 
ATOM   2377  H  HA   A PRO A 1 143 ? 35.435  1.001   28.564  0.45 12.89  ?  366  PRO A HA   1 
ATOM   2378  H  HA   B PRO A 1 143 ? 35.370  1.008   28.554  0.55 12.87  ?  366  PRO A HA   1 
ATOM   2379  H  HB2  A PRO A 1 143 ? 38.057  1.905   28.163  0.45 14.62  ?  366  PRO A HB2  1 
ATOM   2380  H  HB2  B PRO A 1 143 ? 37.810  1.727   28.966  0.55 14.85  ?  366  PRO A HB2  1 
ATOM   2381  H  HB3  A PRO A 1 143 ? 37.551  0.844   29.232  0.45 14.62  ?  366  PRO A HB3  1 
ATOM   2382  H  HB3  B PRO A 1 143 ? 37.386  0.202   28.833  0.55 14.85  ?  366  PRO A HB3  1 
ATOM   2383  H  HG2  A PRO A 1 143 ? 38.771  0.046   27.177  0.45 14.68  ?  366  PRO A HG2  1 
ATOM   2384  H  HG2  B PRO A 1 143 ? 38.539  1.830   26.883  0.55 14.45  ?  366  PRO A HG2  1 
ATOM   2385  H  HG3  A PRO A 1 143 ? 37.578  -0.820  27.769  0.45 14.68  ?  366  PRO A HG3  1 
ATOM   2386  H  HG3  B PRO A 1 143 ? 38.858  0.301   27.181  0.55 14.45  ?  366  PRO A HG3  1 
ATOM   2387  H  HD2  A PRO A 1 143 ? 37.546  0.773   25.474  0.45 13.66  ?  366  PRO A HD2  1 
ATOM   2388  H  HD2  B PRO A 1 143 ? 37.349  0.966   25.199  0.55 13.69  ?  366  PRO A HD2  1 
ATOM   2389  H  HD3  A PRO A 1 143 ? 36.738  -0.571  25.730  0.45 13.66  ?  366  PRO A HD3  1 
ATOM   2390  H  HD3  B PRO A 1 143 ? 37.127  -0.413  25.956  0.55 13.69  ?  366  PRO A HD3  1 
ATOM   2391  N  N    . LYS A 1 144 ? 35.815  3.759   27.080  1.00 9.87   ?  367  LYS A N    1 
ATOM   2392  C  CA   . LYS A 1 144 ? 35.559  5.189   27.126  1.00 10.16  ?  367  LYS A CA   1 
ATOM   2393  C  C    . LYS A 1 144 ? 34.091  5.528   26.905  1.00 8.49   ?  367  LYS A C    1 
ATOM   2394  O  O    . LYS A 1 144 ? 33.737  6.707   26.901  1.00 8.62   ?  367  LYS A O    1 
ATOM   2395  C  CB   . LYS A 1 144 ? 36.422  5.895   26.076  1.00 14.40  ?  367  LYS A CB   1 
ATOM   2396  C  CG   . LYS A 1 144 ? 37.920  5.665   26.226  1.00 19.54  ?  367  LYS A CG   1 
ATOM   2397  C  CD   . LYS A 1 144 ? 38.479  6.390   27.433  1.00 22.93  ?  367  LYS A CD   1 
ATOM   2398  C  CE   . LYS A 1 144 ? 40.007  6.308   27.491  1.00 26.65  ?  367  LYS A CE   1 
ATOM   2399  N  NZ   . LYS A 1 144 ? 40.684  6.918   26.316  1.00 29.30  ?  367  LYS A NZ   1 
ATOM   2400  H  H    . LYS A 1 144 ? 35.989  3.468   26.289  1.00 11.85  ?  367  LYS A H    1 
ATOM   2401  H  HA   . LYS A 1 144 ? 35.809  5.533   27.998  1.00 12.19  ?  367  LYS A HA   1 
ATOM   2402  H  HB2  . LYS A 1 144 ? 36.163  5.573   25.198  1.00 17.29  ?  367  LYS A HB2  1 
ATOM   2403  H  HB3  . LYS A 1 144 ? 36.265  6.850   26.139  1.00 17.29  ?  367  LYS A HB3  1 
ATOM   2404  H  HG2  . LYS A 1 144 ? 38.090  4.716   26.335  1.00 23.44  ?  367  LYS A HG2  1 
ATOM   2405  H  HG3  . LYS A 1 144 ? 38.376  5.994   25.435  1.00 23.44  ?  367  LYS A HG3  1 
ATOM   2406  H  HD2  . LYS A 1 144 ? 38.227  7.326   27.389  1.00 27.52  ?  367  LYS A HD2  1 
ATOM   2407  H  HD3  . LYS A 1 144 ? 38.122  5.988   28.241  1.00 27.52  ?  367  LYS A HD3  1 
ATOM   2408  H  HE2  . LYS A 1 144 ? 40.316  6.773   28.284  1.00 31.98  ?  367  LYS A HE2  1 
ATOM   2409  H  HE3  . LYS A 1 144 ? 40.269  5.374   27.531  1.00 31.98  ?  367  LYS A HE3  1 
ATOM   2410  H  HZ1  . LYS A 1 144 ? 41.567  6.875   26.418  1.00 35.16  ?  367  LYS A HZ1  1 
ATOM   2411  H  HZ2  . LYS A 1 144 ? 40.457  6.482   25.574  1.00 35.16  ?  367  LYS A HZ2  1 
ATOM   2412  H  HZ3  . LYS A 1 144 ? 40.443  7.771   26.235  1.00 35.16  ?  367  LYS A HZ3  1 
ATOM   2413  N  N    . PHE A 1 145 ? 33.241  4.528   26.701  1.00 7.81   ?  368  PHE A N    1 
ATOM   2414  C  CA   . PHE A 1 145 ? 31.797  4.746   26.656  1.00 7.39   ?  368  PHE A CA   1 
ATOM   2415  C  C    . PHE A 1 145 ? 31.326  4.771   28.104  1.00 6.84   ?  368  PHE A C    1 
ATOM   2416  O  O    . PHE A 1 145 ? 31.053  3.731   28.707  1.00 7.25   ?  368  PHE A O    1 
ATOM   2417  C  CB   . PHE A 1 145 ? 31.117  3.656   25.844  1.00 7.48   ?  368  PHE A CB   1 
ATOM   2418  C  CG   . PHE A 1 145 ? 29.643  3.862   25.685  1.00 7.17   ?  368  PHE A CG   1 
ATOM   2419  C  CD1  . PHE A 1 145 ? 29.158  4.767   24.761  1.00 7.37   ?  368  PHE A CD1  1 
ATOM   2420  C  CD2  . PHE A 1 145 ? 28.738  3.170   26.467  1.00 7.57   ?  368  PHE A CD2  1 
ATOM   2421  C  CE1  . PHE A 1 145 ? 27.805  4.961   24.582  1.00 7.82   ?  368  PHE A CE1  1 
ATOM   2422  C  CE2  . PHE A 1 145 ? 27.374  3.362   26.311  1.00 7.93   ?  368  PHE A CE2  1 
ATOM   2423  C  CZ   . PHE A 1 145 ? 26.907  4.266   25.363  1.00 7.99   ?  368  PHE A CZ   1 
ATOM   2424  H  H    . PHE A 1 145 ? 33.476  3.709   26.584  1.00 9.37   ?  368  PHE A H    1 
ATOM   2425  H  HA   . PHE A 1 145 ? 31.583  5.593   26.234  1.00 8.87   ?  368  PHE A HA   1 
ATOM   2426  H  HB2  . PHE A 1 145 ? 31.512  3.634   24.958  1.00 8.98   ?  368  PHE A HB2  1 
ATOM   2427  H  HB3  . PHE A 1 145 ? 31.252  2.805   26.289  1.00 8.98   ?  368  PHE A HB3  1 
ATOM   2428  H  HD1  . PHE A 1 145 ? 29.758  5.257   24.248  1.00 8.85   ?  368  PHE A HD1  1 
ATOM   2429  H  HD2  . PHE A 1 145 ? 29.047  2.568   27.105  1.00 9.09   ?  368  PHE A HD2  1 
ATOM   2430  H  HE1  . PHE A 1 145 ? 27.500  5.559   23.937  1.00 9.38   ?  368  PHE A HE1  1 
ATOM   2431  H  HE2  . PHE A 1 145 ? 26.773  2.888   26.839  1.00 9.52   ?  368  PHE A HE2  1 
ATOM   2432  H  HZ   . PHE A 1 145 ? 25.993  4.400   25.256  1.00 9.58   ?  368  PHE A HZ   1 
ATOM   2433  N  N    . VAL A 1 146 ? 31.262  5.973   28.673  1.00 6.77   ?  369  VAL A N    1 
ATOM   2434  C  CA   . VAL A 1 146 ? 30.876  6.155   30.070  1.00 6.69   ?  369  VAL A CA   1 
ATOM   2435  C  C    . VAL A 1 146 ? 29.798  7.229   30.164  1.00 6.42   ?  369  VAL A C    1 
ATOM   2436  O  O    . VAL A 1 146 ? 29.944  8.220   30.895  1.00 6.68   ?  369  VAL A O    1 
ATOM   2437  C  CB   . VAL A 1 146 ? 32.094  6.407   30.977  1.00 7.59   ?  369  VAL A CB   1 
ATOM   2438  C  CG1  . VAL A 1 146 ? 32.950  5.134   31.045  1.00 8.99   ?  369  VAL A CG1  1 
ATOM   2439  C  CG2  . VAL A 1 146 ? 32.917  7.591   30.521  1.00 7.92   ?  369  VAL A CG2  1 
ATOM   2440  H  H    . VAL A 1 146 ? 31.439  6.709   28.264  1.00 8.13   ?  369  VAL A H    1 
ATOM   2441  H  HA   . VAL A 1 146 ? 30.468  5.337   30.397  1.00 8.03   ?  369  VAL A HA   1 
ATOM   2442  H  HB   . VAL A 1 146 ? 31.776  6.627   31.866  1.00 9.11   ?  369  VAL A HB   1 
ATOM   2443  H  HG11 . VAL A 1 146 ? 33.698  5.288   31.642  1.00 10.79  ?  369  VAL A HG11 1 
ATOM   2444  H  HG12 . VAL A 1 146 ? 32.405  4.405   31.378  1.00 10.79  ?  369  VAL A HG12 1 
ATOM   2445  H  HG13 . VAL A 1 146 ? 33.275  4.925   30.155  1.00 10.79  ?  369  VAL A HG13 1 
ATOM   2446  H  HG21 . VAL A 1 146 ? 33.651  7.723   31.141  1.00 9.51   ?  369  VAL A HG21 1 
ATOM   2447  H  HG22 . VAL A 1 146 ? 33.262  7.412   29.632  1.00 9.51   ?  369  VAL A HG22 1 
ATOM   2448  H  HG23 . VAL A 1 146 ? 32.352  8.379   30.504  1.00 9.51   ?  369  VAL A HG23 1 
ATOM   2449  N  N    . PRO A 1 147 ? 28.673  7.053   29.476  1.00 5.93   ?  370  PRO A N    1 
ATOM   2450  C  CA   . PRO A 1 147 ? 27.671  8.133   29.454  1.00 6.55   ?  370  PRO A CA   1 
ATOM   2451  C  C    . PRO A 1 147 ? 27.126  8.491   30.836  1.00 6.58   ?  370  PRO A C    1 
ATOM   2452  O  O    . PRO A 1 147 ? 26.806  9.664   31.070  1.00 7.21   ?  370  PRO A O    1 
ATOM   2453  C  CB   . PRO A 1 147 ? 26.594  7.576   28.507  1.00 7.09   ?  370  PRO A CB   1 
ATOM   2454  C  CG   . PRO A 1 147 ? 26.765  6.048   28.621  1.00 6.53   ?  370  PRO A CG   1 
ATOM   2455  C  CD   . PRO A 1 147 ? 28.241  5.885   28.684  1.00 6.09   ?  370  PRO A CD   1 
ATOM   2456  H  HA   . PRO A 1 147 ? 28.044  8.936   29.060  1.00 7.86   ?  370  PRO A HA   1 
ATOM   2457  H  HB2  . PRO A 1 147 ? 25.713  7.855   28.800  1.00 8.51   ?  370  PRO A HB2  1 
ATOM   2458  H  HB3  . PRO A 1 147 ? 26.754  7.881   27.600  1.00 8.51   ?  370  PRO A HB3  1 
ATOM   2459  H  HG2  . PRO A 1 147 ? 26.337  5.717   29.426  1.00 7.84   ?  370  PRO A HG2  1 
ATOM   2460  H  HG3  . PRO A 1 147 ? 26.392  5.606   27.842  1.00 7.84   ?  370  PRO A HG3  1 
ATOM   2461  H  HD2  . PRO A 1 147 ? 28.479  5.057   29.129  1.00 7.31   ?  370  PRO A HD2  1 
ATOM   2462  H  HD3  . PRO A 1 147 ? 28.629  5.907   27.795  1.00 7.31   ?  370  PRO A HD3  1 
ATOM   2463  N  N    . LYS A 1 148 ? 26.999  7.515   31.743  1.00 7.14   ?  371  LYS A N    1 
ATOM   2464  C  CA   . LYS A 1 148 ? 26.553  7.809   33.106  1.00 8.35   ?  371  LYS A CA   1 
ATOM   2465  C  C    . LYS A 1 148 ? 27.530  8.735   33.816  1.00 9.15   ?  371  LYS A C    1 
ATOM   2466  O  O    . LYS A 1 148 ? 27.130  9.496   34.703  1.00 10.75  ?  371  LYS A O    1 
ATOM   2467  C  CB   . LYS A 1 148 ? 26.371  6.487   33.873  1.00 9.70   ?  371  LYS A CB   1 
ATOM   2468  C  CG   . LYS A 1 148 ? 26.097  6.565   35.353  1.00 13.63  ?  371  LYS A CG   1 
ATOM   2469  C  CD   . LYS A 1 148 ? 24.725  7.025   35.686  1.00 15.52  ?  371  LYS A CD   1 
ATOM   2470  C  CE   . LYS A 1 148 ? 24.350  6.495   37.081  1.00 18.05  ?  371  LYS A CE   1 
ATOM   2471  N  NZ   . LYS A 1 148 ? 23.116  7.102   37.617  1.00 19.15  ?  371  LYS A NZ   1 
ATOM   2472  H  H    . LYS A 1 148 ? 27.162  6.683   31.596  1.00 8.58   ?  371  LYS A H    1 
ATOM   2473  H  HA   . LYS A 1 148 ? 25.695  8.260   33.087  1.00 10.02  ?  371  LYS A HA   1 
ATOM   2474  H  HB2  . LYS A 1 148 ? 25.622  6.015   33.475  1.00 11.65  ?  371  LYS A HB2  1 
ATOM   2475  H  HB3  . LYS A 1 148 ? 27.184  5.968   33.766  1.00 11.65  ?  371  LYS A HB3  1 
ATOM   2476  H  HG2  . LYS A 1 148 ? 26.214  5.683   35.739  1.00 16.36  ?  371  LYS A HG2  1 
ATOM   2477  H  HG3  . LYS A 1 148 ? 26.723  7.188   35.754  1.00 16.36  ?  371  LYS A HG3  1 
ATOM   2478  H  HD2  . LYS A 1 148 ? 24.694  7.994   35.697  1.00 18.63  ?  371  LYS A HD2  1 
ATOM   2479  H  HD3  . LYS A 1 148 ? 24.093  6.680   35.036  1.00 18.63  ?  371  LYS A HD3  1 
ATOM   2480  H  HE2  . LYS A 1 148 ? 24.212  5.536   37.027  1.00 21.66  ?  371  LYS A HE2  1 
ATOM   2481  H  HE3  . LYS A 1 148 ? 25.072  6.693   37.698  1.00 21.66  ?  371  LYS A HE3  1 
ATOM   2482  H  HZ1  . LYS A 1 148 ? 23.203  7.987   37.653  1.00 22.99  ?  371  LYS A HZ1  1 
ATOM   2483  H  HZ2  . LYS A 1 148 ? 22.425  6.901   37.093  1.00 22.99  ?  371  LYS A HZ2  1 
ATOM   2484  H  HZ3  . LYS A 1 148 ? 22.956  6.794   38.436  1.00 22.99  ?  371  LYS A HZ3  1 
ATOM   2485  N  N    . LEU A 1 149 ? 28.809  8.678   33.444  1.00 8.26   ?  372  LEU A N    1 
ATOM   2486  C  CA   . LEU A 1 149 ? 29.837  9.559   33.974  1.00 9.88   ?  372  LEU A CA   1 
ATOM   2487  C  C    . LEU A 1 149 ? 30.037  10.814  33.135  1.00 10.11  ?  372  LEU A C    1 
ATOM   2488  O  O    . LEU A 1 149 ? 30.973  11.575  33.398  1.00 12.55  ?  372  LEU A O    1 
ATOM   2489  C  CB   . LEU A 1 149 ? 31.162  8.803   34.065  1.00 10.55  ?  372  LEU A CB   1 
ATOM   2490  C  CG   . LEU A 1 149 ? 31.114  7.505   34.871  1.00 12.58  ?  372  LEU A CG   1 
ATOM   2491  C  CD1  . LEU A 1 149 ? 32.494  6.870   34.918  1.00 13.50  ?  372  LEU A CD1  1 
ATOM   2492  C  CD2  . LEU A 1 149 ? 30.559  7.728   36.268  1.00 14.36  ?  372  LEU A CD2  1 
ATOM   2493  H  H    . LEU A 1 149 ? 29.111  8.117   32.866  1.00 9.91   ?  372  LEU A H    1 
ATOM   2494  H  HA   . LEU A 1 149 ? 29.573  9.836   34.866  1.00 11.85  ?  372  LEU A HA   1 
ATOM   2495  H  HB2  . LEU A 1 149 ? 31.447  8.578   33.166  1.00 12.66  ?  372  LEU A HB2  1 
ATOM   2496  H  HB3  . LEU A 1 149 ? 31.816  9.383   34.486  1.00 12.66  ?  372  LEU A HB3  1 
ATOM   2497  H  HG   . LEU A 1 149 ? 30.510  6.886   34.432  1.00 15.10  ?  372  LEU A HG   1 
ATOM   2498  H  HD11 . LEU A 1 149 ? 32.446  6.046   35.427  1.00 16.21  ?  372  LEU A HD11 1 
ATOM   2499  H  HD12 . LEU A 1 149 ? 32.786  6.682   34.012  1.00 16.21  ?  372  LEU A HD12 1 
ATOM   2500  H  HD13 . LEU A 1 149 ? 33.111  7.486   35.343  1.00 16.21  ?  372  LEU A HD13 1 
ATOM   2501  H  HD21 . LEU A 1 149 ? 30.667  6.915   36.785  1.00 17.23  ?  372  LEU A HD21 1 
ATOM   2502  H  HD22 . LEU A 1 149 ? 31.045  8.455   36.689  1.00 17.23  ?  372  LEU A HD22 1 
ATOM   2503  H  HD23 . LEU A 1 149 ? 29.618  7.955   36.202  1.00 17.23  ?  372  LEU A HD23 1 
ATOM   2504  N  N    . GLY A 1 150 ? 29.195  11.037  32.135  1.00 9.32   ?  373  GLY A N    1 
ATOM   2505  C  CA   . GLY A 1 150 ? 29.174  12.278  31.400  1.00 8.94   ?  373  GLY A CA   1 
ATOM   2506  C  C    . GLY A 1 150 ? 29.949  12.329  30.102  1.00 8.23   ?  373  GLY A C    1 
ATOM   2507  O  O    . GLY A 1 150 ? 30.074  13.413  29.532  1.00 8.69   ?  373  GLY A O    1 
ATOM   2508  H  H    . GLY A 1 150 ? 28.614  10.465  31.861  1.00 11.19  ?  373  GLY A H    1 
ATOM   2509  H  HA2  . GLY A 1 150 ? 28.250  12.487  31.190  1.00 10.73  ?  373  GLY A HA2  1 
ATOM   2510  H  HA3  . GLY A 1 150 ? 29.532  12.974  31.974  1.00 10.73  ?  373  GLY A HA3  1 
ATOM   2511  N  N    . SER A 1 151 ? 30.435  11.208  29.577  1.00 7.70   ?  374  SER A N    1 
ATOM   2512  C  CA   . SER A 1 151 ? 31.168  11.304  28.321  1.00 7.88   ?  374  SER A CA   1 
ATOM   2513  C  C    . SER A 1 151 ? 31.158  9.991   27.555  1.00 7.29   ?  374  SER A C    1 
ATOM   2514  O  O    . SER A 1 151 ? 30.980  8.907   28.124  1.00 7.41   ?  374  SER A O    1 
ATOM   2515  C  CB   . SER A 1 151 ? 32.615  11.772  28.521  1.00 8.21   ?  374  SER A CB   1 
ATOM   2516  O  OG   . SER A 1 151 ? 33.405  10.815  29.205  1.00 9.61   ?  374  SER A OG   1 
ATOM   2517  H  H    . SER A 1 151 ? 30.356  10.420  29.912  1.00 9.24   ?  374  SER A H    1 
ATOM   2518  H  HA   . SER A 1 151 ? 30.690  11.953  27.781  1.00 9.46   ?  374  SER A HA   1 
ATOM   2519  H  HB2  . SER A 1 151 ? 33.011  11.933  27.650  1.00 9.86   ?  374  SER A HB2  1 
ATOM   2520  H  HB3  . SER A 1 151 ? 32.606  12.592  29.039  1.00 9.86   ?  374  SER A HB3  1 
ATOM   2521  H  HG   . SER A 1 151 ? 33.099  10.688  29.977  1.00 11.53  ?  374  SER A HG   1 
ATOM   2522  N  N    . VAL A 1 152 ? 31.377  10.113  26.242  1.00 6.77   ?  375  VAL A N    1 
ATOM   2523  C  CA   . VAL A 1 152 ? 31.608  8.991   25.341  1.00 7.05   ?  375  VAL A CA   1 
ATOM   2524  C  C    . VAL A 1 152 ? 32.755  9.385   24.422  1.00 7.08   ?  375  VAL A C    1 
ATOM   2525  O  O    . VAL A 1 152 ? 33.161  10.545  24.361  1.00 8.41   ?  375  VAL A O    1 
ATOM   2526  C  CB   . VAL A 1 152 ? 30.350  8.615   24.521  1.00 7.09   ?  375  VAL A CB   1 
ATOM   2527  C  CG1  . VAL A 1 152 ? 29.178  8.297   25.450  1.00 7.35   ?  375  VAL A CG1  1 
ATOM   2528  C  CG2  . VAL A 1 152 ? 29.980  9.709   23.522  1.00 7.36   ?  375  VAL A CG2  1 
ATOM   2529  H  H    . VAL A 1 152 ? 31.397  10.872  25.837  1.00 8.12   ?  375  VAL A H    1 
ATOM   2530  H  HA   . VAL A 1 152 ? 31.863  8.205   25.849  1.00 8.46   ?  375  VAL A HA   1 
ATOM   2531  H  HB   . VAL A 1 152 ? 30.552  7.818   24.006  1.00 8.51   ?  375  VAL A HB   1 
ATOM   2532  H  HG11 . VAL A 1 152 ? 28.421  8.010   24.916  1.00 8.82   ?  375  VAL A HG11 1 
ATOM   2533  H  HG12 . VAL A 1 152 ? 29.441  7.590   26.060  1.00 8.82   ?  375  VAL A HG12 1 
ATOM   2534  H  HG13 . VAL A 1 152 ? 28.946  9.096   25.950  1.00 8.82   ?  375  VAL A HG13 1 
ATOM   2535  H  HG21 . VAL A 1 152 ? 29.094  9.529   23.170  1.00 8.83   ?  375  VAL A HG21 1 
ATOM   2536  H  HG22 . VAL A 1 152 ? 29.987  10.566  23.975  1.00 8.83   ?  375  VAL A HG22 1 
ATOM   2537  H  HG23 . VAL A 1 152 ? 30.628  9.710   22.800  1.00 8.83   ?  375  VAL A HG23 1 
ATOM   2538  N  N    . MET A 1 153 ? 33.262  8.407   23.684  1.00 7.69   ?  376  MET A N    1 
ATOM   2539  C  CA   B MET A 1 153 ? 34.287  8.643   22.677  0.61 7.85   ?  376  MET A CA   1 
ATOM   2540  C  CA   C MET A 1 153 ? 34.284  8.647   22.676  0.39 7.90   ?  376  MET A CA   1 
ATOM   2541  C  C    . MET A 1 153 ? 33.689  8.448   21.287  1.00 7.40   ?  376  MET A C    1 
ATOM   2542  O  O    . MET A 1 153 ? 32.955  7.487   21.044  1.00 8.57   ?  376  MET A O    1 
ATOM   2543  C  CB   B MET A 1 153 ? 35.465  7.690   22.873  0.61 10.25  ?  376  MET A CB   1 
ATOM   2544  C  CB   C MET A 1 153 ? 35.476  7.710   22.873  0.39 9.69   ?  376  MET A CB   1 
ATOM   2545  C  CG   B MET A 1 153 ? 36.675  8.029   22.024  0.61 12.84  ?  376  MET A CG   1 
ATOM   2546  C  CG   C MET A 1 153 ? 36.587  7.912   21.856  0.39 11.47  ?  376  MET A CG   1 
ATOM   2547  S  SD   B MET A 1 153 ? 38.156  7.120   22.504  0.61 15.31  ?  376  MET A SD   1 
ATOM   2548  S  SD   C MET A 1 153 ? 36.326  6.980   20.336  0.39 13.49  ?  376  MET A SD   1 
ATOM   2549  C  CE   B MET A 1 153 ? 37.622  5.433   22.238  0.61 15.85  ?  376  MET A CE   1 
ATOM   2550  C  CE   C MET A 1 153 ? 36.566  5.312   20.958  0.39 14.40  ?  376  MET A CE   1 
ATOM   2551  H  H    B MET A 1 153 ? 33.023  7.583   23.749  0.61 9.23   ?  376  MET A H    1 
ATOM   2552  H  H    C MET A 1 153 ? 33.025  7.583   23.749  0.39 9.23   ?  376  MET A H    1 
ATOM   2553  H  HA   B MET A 1 153 ? 34.619  9.551   22.756  0.61 9.42   ?  376  MET A HA   1 
ATOM   2554  H  HA   C MET A 1 153 ? 34.607  9.558   22.755  0.39 9.48   ?  376  MET A HA   1 
ATOM   2555  H  HB2  B MET A 1 153 ? 35.739  7.720   23.803  0.61 12.30  ?  376  MET A HB2  1 
ATOM   2556  H  HB2  C MET A 1 153 ? 35.850  7.863   23.755  0.39 11.63  ?  376  MET A HB2  1 
ATOM   2557  H  HB3  B MET A 1 153 ? 35.182  6.792   22.640  0.61 12.30  ?  376  MET A HB3  1 
ATOM   2558  H  HB3  C MET A 1 153 ? 35.168  6.794   22.798  0.39 11.63  ?  376  MET A HB3  1 
ATOM   2559  H  HG2  B MET A 1 153 ? 36.480  7.813   21.099  0.61 15.41  ?  376  MET A HG2  1 
ATOM   2560  H  HG2  C MET A 1 153 ? 36.636  8.853   21.625  0.39 13.77  ?  376  MET A HG2  1 
ATOM   2561  H  HG3  B MET A 1 153 ? 36.864  8.976   22.111  0.61 15.41  ?  376  MET A HG3  1 
ATOM   2562  H  HG3  C MET A 1 153 ? 37.427  7.622   22.244  0.39 13.77  ?  376  MET A HG3  1 
ATOM   2563  H  HE1  B MET A 1 153 ? 38.393  4.889   22.015  0.61 19.03  ?  376  MET A HE1  1 
ATOM   2564  H  HE1  C MET A 1 153 ? 36.612  4.698   20.208  0.39 17.29  ?  376  MET A HE1  1 
ATOM   2565  H  HE2  B MET A 1 153 ? 37.207  5.101   23.050  0.61 19.03  ?  376  MET A HE2  1 
ATOM   2566  H  HE2  C MET A 1 153 ? 37.394  5.279   21.463  0.39 17.29  ?  376  MET A HE2  1 
ATOM   2567  H  HE3  B MET A 1 153 ? 36.983  5.415   21.509  0.61 19.03  ?  376  MET A HE3  1 
ATOM   2568  H  HE3  C MET A 1 153 ? 35.820  5.078   21.531  0.39 17.29  ?  376  MET A HE3  1 
ATOM   2569  N  N    . ILE A 1 154 ? 34.004  9.365   20.368  1.00 7.15   ?  377  ILE A N    1 
ATOM   2570  C  CA   . ILE A 1 154 ? 33.531  9.286   18.990  1.00 6.91   ?  377  ILE A CA   1 
ATOM   2571  C  C    . ILE A 1 154 ? 34.742  9.225   18.066  1.00 6.71   ?  377  ILE A C    1 
ATOM   2572  O  O    . ILE A 1 154 ? 35.707  9.981   18.245  1.00 8.15   ?  377  ILE A O    1 
ATOM   2573  C  CB   . ILE A 1 154 ? 32.578  10.448  18.633  1.00 7.77   ?  377  ILE A CB   1 
ATOM   2574  C  CG1  . ILE A 1 154 ? 32.015  10.261  17.217  1.00 7.72   ?  377  ILE A CG1  1 
ATOM   2575  C  CG2  . ILE A 1 154 ? 33.236  11.829  18.801  1.00 8.31   ?  377  ILE A CG2  1 
ATOM   2576  C  CD1  . ILE A 1 154 ? 30.843  11.158  16.919  1.00 9.10   ?  377  ILE A CD1  1 
ATOM   2577  H  H    . ILE A 1 154 ? 34.498  10.051  20.525  1.00 8.58   ?  377  ILE A H    1 
ATOM   2578  H  HA   . ILE A 1 154 ? 33.033  8.463   18.869  1.00 8.29   ?  377  ILE A HA   1 
ATOM   2579  H  HB   . ILE A 1 154 ? 31.843  10.420  19.265  1.00 9.33   ?  377  ILE A HB   1 
ATOM   2580  H  HG12 . ILE A 1 154 ? 32.713  10.459  16.573  1.00 9.26   ?  377  ILE A HG12 1 
ATOM   2581  H  HG13 . ILE A 1 154 ? 31.721  9.342   17.116  1.00 9.26   ?  377  ILE A HG13 1 
ATOM   2582  H  HG21 . ILE A 1 154 ? 32.572  12.517  18.637  1.00 9.97   ?  377  ILE A HG21 1 
ATOM   2583  H  HG22 . ILE A 1 154 ? 33.577  11.908  19.706  1.00 9.97   ?  377  ILE A HG22 1 
ATOM   2584  H  HG23 . ILE A 1 154 ? 33.963  11.912  18.165  1.00 9.97   ?  377  ILE A HG23 1 
ATOM   2585  H  HD11 . ILE A 1 154 ? 30.500  10.946  16.036  1.00 10.92  ?  377  ILE A HD11 1 
ATOM   2586  H  HD12 . ILE A 1 154 ? 30.154  11.010  17.586  1.00 10.92  ?  377  ILE A HD12 1 
ATOM   2587  H  HD13 . ILE A 1 154 ? 31.137  12.082  16.946  1.00 10.92  ?  377  ILE A HD13 1 
ATOM   2588  N  N    . GLY A 1 155 ? 34.693  8.318   17.090  1.00 6.88   ?  378  GLY A N    1 
ATOM   2589  C  CA   . GLY A 1 155 ? 35.719  8.232   16.068  1.00 7.36   ?  378  GLY A CA   1 
ATOM   2590  C  C    . GLY A 1 155 ? 35.242  8.806   14.749  1.00 7.20   ?  378  GLY A C    1 
ATOM   2591  O  O    . GLY A 1 155 ? 34.079  8.663   14.395  1.00 7.94   ?  378  GLY A O    1 
ATOM   2592  H  H    . GLY A 1 155 ? 34.065  7.737   17.002  1.00 8.25   ?  378  GLY A H    1 
ATOM   2593  H  HA2  . GLY A 1 155 ? 36.504  8.725   16.354  1.00 8.84   ?  378  GLY A HA2  1 
ATOM   2594  H  HA3  . GLY A 1 155 ? 35.962  7.303   15.931  1.00 8.84   ?  378  GLY A HA3  1 
ATOM   2595  N  N    . THR A 1 156 ? 36.170  9.420   14.002  1.00 7.64   ?  379  THR A N    1 
ATOM   2596  C  CA   . THR A 1 156 ? 35.839  10.058  12.736  1.00 7.95   ?  379  THR A CA   1 
ATOM   2597  C  C    . THR A 1 156 ? 36.751  9.595   11.602  1.00 8.06   ?  379  THR A C    1 
ATOM   2598  O  O    . THR A 1 156 ? 36.922  10.307  10.612  1.00 9.26   ?  379  THR A O    1 
ATOM   2599  C  CB   . THR A 1 156 ? 35.856  11.583  12.867  1.00 8.11   ?  379  THR A CB   1 
ATOM   2600  O  OG1  . THR A 1 156 ? 37.150  12.001  13.299  1.00 8.59   ?  379  THR A OG1  1 
ATOM   2601  C  CG2  . THR A 1 156 ? 34.830  12.064  13.854  1.00 8.14   ?  379  THR A CG2  1 
ATOM   2602  H  H    . THR A 1 156 ? 37.001  9.476   14.215  1.00 9.17   ?  379  THR A H    1 
ATOM   2603  H  HA   . THR A 1 156 ? 34.938  9.791   12.495  1.00 9.54   ?  379  THR A HA   1 
ATOM   2604  H  HB   . THR A 1 156 ? 35.645  11.976  12.006  1.00 9.73   ?  379  THR A HB   1 
ATOM   2605  H  HG1  . THR A 1 156 ? 37.721  11.820  12.711  1.00 10.31  ?  379  THR A HG1  1 
ATOM   2606  H  HG21 . THR A 1 156 ? 34.841  13.033  13.899  1.00 9.77   ?  379  THR A HG21 1 
ATOM   2607  H  HG22 . THR A 1 156 ? 33.945  11.772  13.583  1.00 9.77   ?  379  THR A HG22 1 
ATOM   2608  H  HG23 . THR A 1 156 ? 35.023  11.706  14.735  1.00 9.77   ?  379  THR A HG23 1 
ATOM   2609  N  N    . TRP A 1 157 ? 37.324  8.398   11.720  0.91 7.86   ?  380  TRP A N    1 
ATOM   2610  C  CA   . TRP A 1 157 ? 38.206  7.830   10.688  0.91 9.25   ?  380  TRP A CA   1 
ATOM   2611  C  C    . TRP A 1 157 ? 39.347  8.811   10.420  0.91 9.60   ?  380  TRP A C    1 
ATOM   2612  O  O    . TRP A 1 157 ? 40.028  9.243   11.359  0.91 9.81   ?  380  TRP A O    1 
ATOM   2613  C  CB   . TRP A 1 157 ? 37.409  7.443   9.455   0.91 10.14  ?  380  TRP A CB   1 
ATOM   2614  C  CG   . TRP A 1 157 ? 36.445  6.348   9.568   0.91 11.51  ?  380  TRP A CG   1 
ATOM   2615  C  CD1  . TRP A 1 157 ? 36.701  5.025   9.423   0.91 14.22  ?  380  TRP A CD1  1 
ATOM   2616  C  CD2  . TRP A 1 157 ? 35.031  6.466   9.749   0.91 11.71  ?  380  TRP A CD2  1 
ATOM   2617  N  NE1  . TRP A 1 157 ? 35.539  4.301   9.544   0.91 15.00  ?  380  TRP A NE1  1 
ATOM   2618  C  CE2  . TRP A 1 157 ? 34.500  5.167   9.745   0.91 13.25  ?  380  TRP A CE2  1 
ATOM   2619  C  CE3  . TRP A 1 157 ? 34.166  7.540   9.937   0.91 12.52  ?  380  TRP A CE3  1 
ATOM   2620  C  CZ2  . TRP A 1 157 ? 33.146  4.909   9.903   0.91 13.73  ?  380  TRP A CZ2  1 
ATOM   2621  C  CZ3  . TRP A 1 157 ? 32.822  7.278   10.115  0.91 13.80  ?  380  TRP A CZ3  1 
ATOM   2622  C  CH2  . TRP A 1 157 ? 32.327  5.970   10.090  0.91 14.69  ?  380  TRP A CH2  1 
ATOM   2623  H  H    . TRP A 1 157 ? 37.218  7.882   12.400  0.91 9.43   ?  380  TRP A H    1 
ATOM   2624  H  HA   . TRP A 1 157 ? 38.594  7.027   11.071  0.91 11.10  ?  380  TRP A HA   1 
ATOM   2625  H  HB2  . TRP A 1 157 ? 36.909  8.224   9.171   0.91 12.16  ?  380  TRP A HB2  1 
ATOM   2626  H  HB3  . TRP A 1 157 ? 38.041  7.185   8.766   0.91 12.16  ?  380  TRP A HB3  1 
ATOM   2627  H  HD1  . TRP A 1 157 ? 37.541  4.659   9.265   0.91 17.06  ?  380  TRP A HD1  1 
ATOM   2628  H  HE1  . TRP A 1 157 ? 35.476  3.444   9.500   0.91 18.00  ?  380  TRP A HE1  1 
ATOM   2629  H  HE3  . TRP A 1 157 ? 34.486  8.413   9.943   0.91 15.03  ?  380  TRP A HE3  1 
ATOM   2630  H  HZ2  . TRP A 1 157 ? 32.815  4.041   9.882   0.91 16.48  ?  380  TRP A HZ2  1 
ATOM   2631  H  HZ3  . TRP A 1 157 ? 32.235  7.985   10.255  0.91 16.56  ?  380  TRP A HZ3  1 
ATOM   2632  H  HH2  . TRP A 1 157 ? 31.415  5.826   10.204  0.91 17.63  ?  380  TRP A HH2  1 
ATOM   2633  N  N    . THR A 1 158 ? 39.595  9.195   9.175   1.00 10.85  ?  381  THR A N    1 
ATOM   2634  C  CA   . THR A 1 158 ? 40.719  10.068  8.849   1.00 13.04  ?  381  THR A CA   1 
ATOM   2635  C  C    . THR A 1 158 ? 40.358  11.548  8.910   1.00 12.02  ?  381  THR A C    1 
ATOM   2636  O  O    . THR A 1 158 ? 41.217  12.390  8.624   1.00 13.35  ?  381  THR A O    1 
ATOM   2637  C  CB   . THR A 1 158 ? 41.281  9.730   7.463   1.00 17.43  ?  381  THR A CB   1 
ATOM   2638  O  OG1  . THR A 1 158 ? 40.285  10.009  6.478   1.00 20.10  ?  381  THR A OG1  1 
ATOM   2639  C  CG2  . THR A 1 158 ? 41.711  8.265   7.377   1.00 19.32  ?  381  THR A CG2  1 
ATOM   2640  H  H    . THR A 1 158 ? 39.124  8.963   8.494   1.00 13.02  ?  381  THR A H    1 
ATOM   2641  H  HA   . THR A 1 158 ? 41.424  9.908   9.495   1.00 15.65  ?  381  THR A HA   1 
ATOM   2642  H  HB   . THR A 1 158 ? 42.069  10.268  7.291   1.00 20.92  ?  381  THR A HB   1 
ATOM   2643  H  HG1  . THR A 1 158 ? 40.580  9.828   5.713   1.00 24.12  ?  381  THR A HG1  1 
ATOM   2644  H  HG21 . THR A 1 158 ? 42.099  8.084   6.506   1.00 23.18  ?  381  THR A HG21 1 
ATOM   2645  H  HG22 . THR A 1 158 ? 42.371  8.073   8.061   1.00 23.18  ?  381  THR A HG22 1 
ATOM   2646  H  HG23 . THR A 1 158 ? 40.945  7.686   7.507   1.00 23.18  ?  381  THR A HG23 1 
ATOM   2647  N  N    . THR A 1 159 ? 39.131  11.892  9.293   1.00 10.33  ?  382  THR A N    1 
ATOM   2648  C  CA   . THR A 1 159 ? 38.714  13.284  9.348   1.00 10.17  ?  382  THR A CA   1 
ATOM   2649  C  C    . THR A 1 159 ? 39.221  13.931  10.636  1.00 10.02  ?  382  THR A C    1 
ATOM   2650  O  O    . THR A 1 159 ? 38.852  13.507  11.737  1.00 10.50  ?  382  THR A O    1 
ATOM   2651  C  CB   . THR A 1 159 ? 37.190  13.342  9.278   1.00 13.51  ?  382  THR A CB   1 
ATOM   2652  O  OG1  . THR A 1 159 ? 36.762  12.811  8.011   1.00 15.99  ?  382  THR A OG1  1 
ATOM   2653  C  CG2  . THR A 1 159 ? 36.716  14.779  9.459   1.00 14.01  ?  382  THR A CG2  1 
ATOM   2654  H  H    . THR A 1 159 ? 38.521  11.333  9.526   1.00 12.40  ?  382  THR A H    1 
ATOM   2655  H  HA   . THR A 1 159 ? 39.092  13.778  8.603   1.00 12.21  ?  382  THR A HA   1 
ATOM   2656  H  HB   . THR A 1 159 ? 36.789  12.813  9.985   1.00 16.21  ?  382  THR A HB   1 
ATOM   2657  H  HG1  . THR A 1 159 ? 35.924  12.837  7.956   1.00 19.19  ?  382  THR A HG1  1 
ATOM   2658  H  HG21 . THR A 1 159 ? 35.825  14.884  9.090   1.00 16.81  ?  382  THR A HG21 1 
ATOM   2659  H  HG22 . THR A 1 159 ? 36.695  15.005  10.402  1.00 16.81  ?  382  THR A HG22 1 
ATOM   2660  H  HG23 . THR A 1 159 ? 37.319  15.387  9.002   1.00 16.81  ?  382  THR A HG23 1 
ATOM   2661  N  N    . ASP A 1 160 ? 40.034  14.979  10.496  1.00 10.53  ?  383  ASP A N    1 
ATOM   2662  C  CA   . ASP A 1 160 ? 40.579  15.715  11.635  1.00 11.60  ?  383  ASP A CA   1 
ATOM   2663  C  C    . ASP A 1 160 ? 39.856  17.030  11.917  1.00 9.57   ?  383  ASP A C    1 
ATOM   2664  O  O    . ASP A 1 160 ? 40.250  17.753  12.834  1.00 10.54  ?  383  ASP A O    1 
ATOM   2665  C  CB   . ASP A 1 160 ? 42.092  15.960  11.459  1.00 15.63  ?  383  ASP A CB   1 
ATOM   2666  C  CG   . ASP A 1 160 ? 42.432  16.810  10.232  1.00 18.00  ?  383  ASP A CG   1 
ATOM   2667  O  OD1  . ASP A 1 160 ? 41.544  17.417  9.616   1.00 21.53  -1 383  ASP A OD1  1 
ATOM   2668  O  OD2  . ASP A 1 160 ? 43.633  16.876  9.871   1.00 22.46  -1 383  ASP A OD2  1 
ATOM   2669  H  H    . ASP A 1 160 ? 40.289  15.288  9.735   1.00 12.64  ?  383  ASP A H    1 
ATOM   2670  H  HA   . ASP A 1 160 ? 40.473  15.159  12.423  1.00 13.92  ?  383  ASP A HA   1 
ATOM   2671  H  HB2  . ASP A 1 160 ? 42.427  16.422  12.243  1.00 18.76  ?  383  ASP A HB2  1 
ATOM   2672  H  HB3  . ASP A 1 160 ? 42.539  15.105  11.361  1.00 18.76  ?  383  ASP A HB3  1 
ATOM   2673  N  N    . ASP A 1 161 ? 38.793  17.331  11.179  1.00 8.79   ?  384  ASP A N    1 
ATOM   2674  C  CA   . ASP A 1 161 ? 38.103  18.620  11.228  1.00 9.03   ?  384  ASP A CA   1 
ATOM   2675  C  C    . ASP A 1 161 ? 36.982  18.595  12.264  1.00 8.00   ?  384  ASP A C    1 
ATOM   2676  O  O    . ASP A 1 161 ? 35.797  18.743  11.953  1.00 7.77   ?  384  ASP A O    1 
ATOM   2677  C  CB   . ASP A 1 161 ? 37.564  18.950  9.840   1.00 9.25   ?  384  ASP A CB   1 
ATOM   2678  C  CG   . ASP A 1 161 ? 36.862  20.286  9.779   1.00 9.35   ?  384  ASP A CG   1 
ATOM   2679  O  OD1  . ASP A 1 161 ? 37.372  21.256  10.372  1.00 10.91  -1 384  ASP A OD1  1 
ATOM   2680  O  OD2  . ASP A 1 161 ? 35.805  20.369  9.110   1.00 9.50   -1 384  ASP A OD2  1 
ATOM   2681  H  H    . ASP A 1 161 ? 38.436  16.784  10.618  1.00 10.55  ?  384  ASP A H    1 
ATOM   2682  H  HA   . ASP A 1 161 ? 38.732  19.308  11.495  1.00 10.84  ?  384  ASP A HA   1 
ATOM   2683  H  HB2  . ASP A 1 161 ? 38.303  18.973  9.212   1.00 11.10  ?  384  ASP A HB2  1 
ATOM   2684  H  HB3  . ASP A 1 161 ? 36.927  18.266  9.578   1.00 11.10  ?  384  ASP A HB3  1 
ATOM   2685  N  N    . ILE A 1 162 ? 37.385  18.406  13.523  1.00 8.20   ?  385  ILE A N    1 
ATOM   2686  C  CA   . ILE A 1 162 ? 36.511  18.433  14.684  1.00 7.28   ?  385  ILE A CA   1 
ATOM   2687  C  C    . ILE A 1 162 ? 37.136  19.399  15.672  1.00 7.57   ?  385  ILE A C    1 
ATOM   2688  O  O    . ILE A 1 162 ? 38.338  19.310  15.941  1.00 8.87   ?  385  ILE A O    1 
ATOM   2689  C  CB   . ILE A 1 162 ? 36.392  17.034  15.321  1.00 6.96   ?  385  ILE A CB   1 
ATOM   2690  C  CG1  . ILE A 1 162 ? 35.825  16.023  14.313  1.00 8.15   ?  385  ILE A CG1  1 
ATOM   2691  C  CG2  . ILE A 1 162 ? 35.575  17.088  16.603  1.00 7.60   ?  385  ILE A CG2  1 
ATOM   2692  C  CD1  . ILE A 1 162 ? 34.365  16.264  13.914  1.00 8.79   ?  385  ILE A CD1  1 
ATOM   2693  H  H    . ILE A 1 162 ? 38.204  18.253  13.735  1.00 9.84   ?  385  ILE A H    1 
ATOM   2694  H  HA   . ILE A 1 162 ? 35.624  18.740  14.441  1.00 8.74   ?  385  ILE A HA   1 
ATOM   2695  H  HB   . ILE A 1 162 ? 37.282  16.731  15.561  1.00 8.35   ?  385  ILE A HB   1 
ATOM   2696  H  HG12 . ILE A 1 162 ? 36.359  16.062  13.505  1.00 9.78   ?  385  ILE A HG12 1 
ATOM   2697  H  HG13 . ILE A 1 162 ? 35.878  15.137  14.704  1.00 9.78   ?  385  ILE A HG13 1 
ATOM   2698  H  HG21 . ILE A 1 162 ? 35.341  16.185  16.868  1.00 9.12   ?  385  ILE A HG21 1 
ATOM   2699  H  HG22 . ILE A 1 162 ? 36.105  17.509  17.298  1.00 9.12   ?  385  ILE A HG22 1 
ATOM   2700  H  HG23 . ILE A 1 162 ? 34.769  17.605  16.443  1.00 9.12   ?  385  ILE A HG23 1 
ATOM   2701  H  HD11 . ILE A 1 162 ? 34.107  15.606  13.249  1.00 10.55  ?  385  ILE A HD11 1 
ATOM   2702  H  HD12 . ILE A 1 162 ? 33.804  16.178  14.700  1.00 10.55  ?  385  ILE A HD12 1 
ATOM   2703  H  HD13 . ILE A 1 162 ? 34.282  17.157  13.544  1.00 10.55  ?  385  ILE A HD13 1 
ATOM   2704  N  N    . LYS A 1 163 ? 36.348  20.340  16.175  1.00 7.12   ?  386  LYS A N    1 
ATOM   2705  C  CA   . LYS A 1 163 ? 36.815  21.359  17.101  1.00 6.85   ?  386  LYS A CA   1 
ATOM   2706  C  C    . LYS A 1 163 ? 36.244  21.134  18.490  1.00 7.25   ?  386  LYS A C    1 
ATOM   2707  O  O    . LYS A 1 163 ? 35.311  20.352  18.695  1.00 7.47   ?  386  LYS A O    1 
ATOM   2708  C  CB   . LYS A 1 163 ? 36.438  22.751  16.585  1.00 7.54   ?  386  LYS A CB   1 
ATOM   2709  C  CG   . LYS A 1 163 ? 36.897  23.047  15.145  1.00 8.14   ?  386  LYS A CG   1 
ATOM   2710  C  CD   . LYS A 1 163 ? 38.397  22.993  14.990  1.00 8.33   ?  386  LYS A CD   1 
ATOM   2711  C  CE   . LYS A 1 163 ? 38.818  23.137  13.540  1.00 10.54  ?  386  LYS A CE   1 
ATOM   2712  N  NZ   . LYS A 1 163 ? 40.275  22.985  13.364  1.00 11.95  ?  386  LYS A NZ   1 
ATOM   2713  H  H    . LYS A 1 163 ? 35.511  20.410  15.988  1.00 8.55   ?  386  LYS A H    1 
ATOM   2714  H  HA   . LYS A 1 163 ? 37.781  21.302  17.174  1.00 8.22   ?  386  LYS A HA   1 
ATOM   2715  H  HB2  . LYS A 1 163 ? 35.472  22.838  16.607  1.00 9.05   ?  386  LYS A HB2  1 
ATOM   2716  H  HB3  . LYS A 1 163 ? 36.844  23.415  17.164  1.00 9.05   ?  386  LYS A HB3  1 
ATOM   2717  H  HG2  . LYS A 1 163 ? 36.510  22.388  14.548  1.00 9.77   ?  386  LYS A HG2  1 
ATOM   2718  H  HG3  . LYS A 1 163 ? 36.602  23.936  14.895  1.00 9.77   ?  386  LYS A HG3  1 
ATOM   2719  H  HD2  . LYS A 1 163 ? 38.798  23.717  15.496  1.00 10.00  ?  386  LYS A HD2  1 
ATOM   2720  H  HD3  . LYS A 1 163 ? 38.723  22.140  15.317  1.00 10.00  ?  386  LYS A HD3  1 
ATOM   2721  H  HE2  . LYS A 1 163 ? 38.377  22.454  13.011  1.00 12.65  ?  386  LYS A HE2  1 
ATOM   2722  H  HE3  . LYS A 1 163 ? 38.566  24.018  13.221  1.00 12.65  ?  386  LYS A HE3  1 
ATOM   2723  H  HZ1  . LYS A 1 163 ? 40.705  23.598  13.845  1.00 14.35  ?  386  LYS A HZ1  1 
ATOM   2724  H  HZ2  . LYS A 1 163 ? 40.531  22.176  13.632  1.00 14.35  ?  386  LYS A HZ2  1 
ATOM   2725  H  HZ3  . LYS A 1 163 ? 40.490  23.087  12.506  1.00 14.35  ?  386  LYS A HZ3  1 
ATOM   2726  N  N    A ASN A 1 164 ? 36.818  21.840  19.461  0.96 7.84   ?  387  ASN A N    1 
ATOM   2727  C  CA   A ASN A 1 164 ? 36.399  21.703  20.854  0.96 7.59   ?  387  ASN A CA   1 
ATOM   2728  C  C    A ASN A 1 164 ? 35.209  22.629  21.093  0.96 7.78   ?  387  ASN A C    1 
ATOM   2729  O  O    A ASN A 1 164 ? 35.315  23.713  21.672  0.96 9.28   ?  387  ASN A O    1 
ATOM   2730  C  CB   A ASN A 1 164 ? 37.561  21.964  21.805  0.96 9.02   ?  387  ASN A CB   1 
ATOM   2731  C  CG   A ASN A 1 164 ? 38.656  20.926  21.668  0.96 10.91  ?  387  ASN A CG   1 
ATOM   2732  O  OD1  A ASN A 1 164 ? 38.389  19.772  21.372  0.96 12.20  ?  387  ASN A OD1  1 
ATOM   2733  N  ND2  A ASN A 1 164 ? 39.894  21.331  21.871  0.96 14.02  ?  387  ASN A ND2  1 
ATOM   2734  H  H    A ASN A 1 164 ? 37.454  22.406  19.338  0.96 9.41   ?  387  ASN A H    1 
ATOM   2735  H  HA   A ASN A 1 164 ? 36.101  20.794  21.011  0.96 9.11   ?  387  ASN A HA   1 
ATOM   2736  H  HB2  A ASN A 1 164 ? 37.944  22.834  21.609  0.96 10.82  ?  387  ASN A HB2  1 
ATOM   2737  H  HB3  A ASN A 1 164 ? 37.236  21.942  22.718  0.96 10.82  ?  387  ASN A HB3  1 
ATOM   2738  H  HD21 A ASN A 1 164 ? 40.545  20.773  21.803  0.96 16.83  ?  387  ASN A HD21 1 
ATOM   2739  H  HD22 A ASN A 1 164 ? 40.050  22.153  22.071  0.96 16.83  ?  387  ASN A HD22 1 
ATOM   2740  N  N    . GLN A 1 165 ? 34.048  22.176  20.615  1.00 7.12   ?  388  GLN A N    1 
ATOM   2741  C  CA   . GLN A 1 165 ? 32.907  23.056  20.403  1.00 6.69   ?  388  GLN A CA   1 
ATOM   2742  C  C    . GLN A 1 165 ? 31.621  22.286  20.639  1.00 6.48   ?  388  GLN A C    1 
ATOM   2743  O  O    . GLN A 1 165 ? 31.623  21.040  20.672  1.00 6.98   ?  388  GLN A O    1 
ATOM   2744  C  CB   . GLN A 1 165 ? 32.917  23.619  18.979  1.00 6.93   ?  388  GLN A CB   1 
ATOM   2745  C  CG   . GLN A 1 165 ? 34.049  24.586  18.713  1.00 7.84   ?  388  GLN A CG   1 
ATOM   2746  C  CD   . GLN A 1 165 ? 33.852  25.915  19.374  1.00 8.55   ?  388  GLN A CD   1 
ATOM   2747  O  OE1  . GLN A 1 165 ? 32.810  26.206  19.935  1.00 8.61   ?  388  GLN A OE1  1 
ATOM   2748  N  NE2  . GLN A 1 165 ? 34.880  26.746  19.307  1.00 11.73  ?  388  GLN A NE2  1 
ATOM   2749  H  H    . GLN A 1 165 ? 33.900  21.355  20.405  1.00 8.54   ?  388  GLN A H    1 
ATOM   2750  H  HA   . GLN A 1 165 ? 32.944  23.780  21.048  1.00 8.02   ?  388  GLN A HA   1 
ATOM   2751  H  HB2  . GLN A 1 165 ? 33.003  22.883  18.354  1.00 8.31   ?  388  GLN A HB2  1 
ATOM   2752  H  HB3  . GLN A 1 165 ? 32.083  24.090  18.825  1.00 8.31   ?  388  GLN A HB3  1 
ATOM   2753  H  HG2  . GLN A 1 165 ? 34.875  24.205  19.049  1.00 9.41   ?  388  GLN A HG2  1 
ATOM   2754  H  HG3  . GLN A 1 165 ? 34.117  24.735  17.757  1.00 9.41   ?  388  GLN A HG3  1 
ATOM   2755  H  HE21 . GLN A 1 165 ? 35.600  26.508  18.903  1.00 14.08  ?  388  GLN A HE21 1 
ATOM   2756  H  HE22 . GLN A 1 165 ? 34.827  27.525  19.669  1.00 14.08  ?  388  GLN A HE22 1 
ATOM   2757  N  N    . PRO A 1 166 ? 30.491  22.998  20.774  1.00 6.69   ?  389  PRO A N    1 
ATOM   2758  C  CA   . PRO A 1 166 ? 29.187  22.334  20.936  1.00 6.87   ?  389  PRO A CA   1 
ATOM   2759  C  C    . PRO A 1 166 ? 28.892  21.401  19.784  1.00 6.85   ?  389  PRO A C    1 
ATOM   2760  O  O    . PRO A 1 166 ? 29.110  21.734  18.618  1.00 7.37   ?  389  PRO A O    1 
ATOM   2761  C  CB   . PRO A 1 166 ? 28.200  23.510  20.993  1.00 7.31   ?  389  PRO A CB   1 
ATOM   2762  C  CG   . PRO A 1 166 ? 29.020  24.642  21.530  1.00 7.65   ?  389  PRO A CG   1 
ATOM   2763  C  CD   . PRO A 1 166 ? 30.364  24.461  20.880  1.00 7.55   ?  389  PRO A CD   1 
ATOM   2764  H  HA   . PRO A 1 166 ? 29.152  21.837  21.768  1.00 8.24   ?  389  PRO A HA   1 
ATOM   2765  H  HB2  . PRO A 1 166 ? 27.865  23.709  20.104  1.00 8.77   ?  389  PRO A HB2  1 
ATOM   2766  H  HB3  . PRO A 1 166 ? 27.462  23.299  21.586  1.00 8.77   ?  389  PRO A HB3  1 
ATOM   2767  H  HG2  . PRO A 1 166 ? 28.622  25.491  21.280  1.00 9.18   ?  389  PRO A HG2  1 
ATOM   2768  H  HG3  . PRO A 1 166 ? 29.086  24.578  22.495  1.00 9.18   ?  389  PRO A HG3  1 
ATOM   2769  H  HD2  . PRO A 1 166 ? 30.383  24.874  20.003  1.00 9.06   ?  389  PRO A HD2  1 
ATOM   2770  H  HD3  . PRO A 1 166 ? 31.069  24.829  21.436  1.00 9.06   ?  389  PRO A HD3  1 
ATOM   2771  N  N    . SER A 1 167 ? 28.382  20.225  20.129  1.00 5.94   ?  390  SER A N    1 
ATOM   2772  C  CA   . SER A 1 167 ? 28.248  19.125  19.195  1.00 6.12   ?  390  SER A CA   1 
ATOM   2773  C  C    . SER A 1 167 ? 26.974  18.340  19.458  1.00 6.21   ?  390  SER A C    1 
ATOM   2774  O  O    . SER A 1 167 ? 26.537  18.193  20.603  1.00 7.20   ?  390  SER A O    1 
ATOM   2775  C  CB   . SER A 1 167 ? 29.420  18.161  19.335  1.00 7.16   ?  390  SER A CB   1 
ATOM   2776  O  OG   . SER A 1 167 ? 30.658  18.811  19.130  1.00 7.88   ?  390  SER A OG   1 
ATOM   2777  H  H    . SER A 1 167 ? 28.100  20.039  20.920  1.00 7.13   ?  390  SER A H    1 
ATOM   2778  H  HA   . SER A 1 167 ? 28.201  19.489  18.297  1.00 7.35   ?  390  SER A HA   1 
ATOM   2779  H  HB2  . SER A 1 167 ? 29.410  17.784  20.229  1.00 8.60   ?  390  SER A HB2  1 
ATOM   2780  H  HB3  . SER A 1 167 ? 29.325  17.455  18.676  1.00 8.60   ?  390  SER A HB3  1 
ATOM   2781  H  HG   . SER A 1 167 ? 30.757  19.424  19.696  1.00 9.46   ?  390  SER A HG   1 
ATOM   2782  N  N    A LYS A 1 168 ? 26.429  17.781  18.388  0.98 5.85   ?  391  LYS A N    1 
ATOM   2783  C  CA   A LYS A 1 168 ? 25.311  16.862  18.447  0.98 6.25   ?  391  LYS A CA   1 
ATOM   2784  C  C    A LYS A 1 168 ? 25.633  15.668  17.563  0.98 6.10   ?  391  LYS A C    1 
ATOM   2785  O  O    A LYS A 1 168 ? 26.173  15.812  16.462  0.98 7.39   ?  391  LYS A O    1 
ATOM   2786  C  CB   A LYS A 1 168 ? 24.018  17.526  17.984  0.98 8.26   ?  391  LYS A CB   1 
ATOM   2787  C  CG   A LYS A 1 168 ? 22.810  16.596  17.957  0.98 10.72  ?  391  LYS A CG   1 
ATOM   2788  C  CD   A LYS A 1 168 ? 21.525  17.348  17.628  0.98 13.67  ?  391  LYS A CD   1 
ATOM   2789  C  CE   A LYS A 1 168 ? 20.355  16.369  17.462  0.98 16.69  ?  391  LYS A CE   1 
ATOM   2790  N  NZ   A LYS A 1 168 ? 19.037  17.010  17.143  0.98 19.43  ?  391  LYS A NZ   1 
ATOM   2791  H  H    A LYS A 1 168 ? 26.703  17.926  17.586  0.98 7.02   ?  391  LYS A H    1 
ATOM   2792  H  HA   A LYS A 1 168 ? 25.173  16.555  19.357  0.98 7.50   ?  391  LYS A HA   1 
ATOM   2793  H  HB2  . LYS A 1 168 ? 23.813  18.257  18.587  1.00 9.92   ?  391  LYS A HB2  1 
ATOM   2794  H  HB3  A LYS A 1 168 ? 24.149  17.864  17.084  0.98 9.92   ?  391  LYS A HB3  1 
ATOM   2795  H  HG2  A LYS A 1 168 ? 22.946  15.915  17.280  0.98 12.87  ?  391  LYS A HG2  1 
ATOM   2796  H  HG3  A LYS A 1 168 ? 22.706  16.182  18.828  0.98 12.87  ?  391  LYS A HG3  1 
ATOM   2797  H  HD2  A LYS A 1 168 ? 21.314  17.962  18.349  0.98 16.40  ?  391  LYS A HD2  1 
ATOM   2798  H  HD3  A LYS A 1 168 ? 21.638  17.837  16.798  0.98 16.40  ?  391  LYS A HD3  1 
ATOM   2799  H  HE2  A LYS A 1 168 ? 20.564  15.759  16.737  0.98 20.03  ?  391  LYS A HE2  1 
ATOM   2800  H  HE3  A LYS A 1 168 ? 20.246  15.876  18.290  0.98 20.03  ?  391  LYS A HE3  1 
ATOM   2801  H  HZ1  A LYS A 1 168 ? 19.115  17.526  16.423  0.98 23.31  ?  391  LYS A HZ1  1 
ATOM   2802  H  HZ2  A LYS A 1 168 ? 18.424  16.384  16.985  0.98 23.31  ?  391  LYS A HZ2  1 
ATOM   2803  H  HZ3  A LYS A 1 168 ? 18.768  17.510  17.829  0.98 23.31  ?  391  LYS A HZ3  1 
ATOM   2804  N  N    . PHE A 1 169 ? 25.312  14.486  18.053  1.00 6.00   ?  392  PHE A N    1 
ATOM   2805  C  CA   . PHE A 1 169 ? 25.405  13.267  17.268  1.00 5.68   ?  392  PHE A CA   1 
ATOM   2806  C  C    . PHE A 1 169 ? 24.009  12.820  16.869  1.00 6.02   ?  392  PHE A C    1 
ATOM   2807  O  O    . PHE A 1 169 ? 23.166  12.590  17.735  1.00 6.51   ?  392  PHE A O    1 
ATOM   2808  C  CB   . PHE A 1 169 ? 26.088  12.161  18.067  1.00 6.06   ?  392  PHE A CB   1 
ATOM   2809  C  CG   . PHE A 1 169 ? 26.161  10.852  17.328  1.00 6.12   ?  392  PHE A CG   1 
ATOM   2810  C  CD1  . PHE A 1 169 ? 27.179  10.608  16.417  1.00 7.41   ?  392  PHE A CD1  1 
ATOM   2811  C  CD2  . PHE A 1 169 ? 25.208  9.865   17.545  1.00 7.04   ?  392  PHE A CD2  1 
ATOM   2812  C  CE1  . PHE A 1 169 ? 27.252  9.405   15.736  1.00 7.63   ?  392  PHE A CE1  1 
ATOM   2813  C  CE2  . PHE A 1 169 ? 25.279  8.660   16.878  1.00 7.55   ?  392  PHE A CE2  1 
ATOM   2814  C  CZ   . PHE A 1 169 ? 26.302  8.438   15.973  1.00 7.45   ?  392  PHE A CZ   1 
ATOM   2815  H  H    . PHE A 1 169 ? 25.032  14.359  18.856  1.00 7.20   ?  392  PHE A H    1 
ATOM   2816  H  HA   . PHE A 1 169 ? 25.918  13.447  16.464  1.00 6.81   ?  392  PHE A HA   1 
ATOM   2817  H  HB2  . PHE A 1 169 ? 26.994  12.437  18.275  1.00 7.28   ?  392  PHE A HB2  1 
ATOM   2818  H  HB3  . PHE A 1 169 ? 25.590  12.013  18.887  1.00 7.28   ?  392  PHE A HB3  1 
ATOM   2819  H  HD1  . PHE A 1 169 ? 27.821  11.263  16.262  1.00 8.89   ?  392  PHE A HD1  1 
ATOM   2820  H  HD2  . PHE A 1 169 ? 24.515  10.018  18.147  1.00 8.45   ?  392  PHE A HD2  1 
ATOM   2821  H  HE1  . PHE A 1 169 ? 27.936  9.253   15.124  1.00 9.16   ?  392  PHE A HE1  1 
ATOM   2822  H  HE2  . PHE A 1 169 ? 24.642  8.001   17.034  1.00 9.06   ?  392  PHE A HE2  1 
ATOM   2823  H  HZ   . PHE A 1 169 ? 26.349  7.627   15.521  1.00 8.94   ?  392  PHE A HZ   1 
ATOM   2824  N  N    . THR A 1 170 ? 23.777  12.710  15.563  1.00 5.55   ?  393  THR A N    1 
ATOM   2825  C  CA   . THR A 1 170 ? 22.535  12.219  14.998  1.00 6.30   ?  393  THR A CA   1 
ATOM   2826  C  C    . THR A 1 170 ? 22.770  10.807  14.486  1.00 5.50   ?  393  THR A C    1 
ATOM   2827  O  O    . THR A 1 170 ? 23.638  10.607  13.616  1.00 5.73   ?  393  THR A O    1 
ATOM   2828  C  CB   . THR A 1 170 ? 22.089  13.097  13.836  1.00 7.70   ?  393  THR A CB   1 
ATOM   2829  O  OG1  . THR A 1 170 ? 21.901  14.437  14.281  1.00 10.25  ?  393  THR A OG1  1 
ATOM   2830  C  CG2  . THR A 1 170 ? 20.785  12.554  13.237  1.00 8.62   ?  393  THR A CG2  1 
ATOM   2831  H  H    . THR A 1 170 ? 24.353  12.925  14.961  1.00 6.66   ?  393  THR A H    1 
ATOM   2832  H  HA   . THR A 1 170 ? 21.845  12.223  15.678  1.00 7.56   ?  393  THR A HA   1 
ATOM   2833  H  HB   . THR A 1 170 ? 22.768  13.094  13.143  1.00 9.24   ?  393  THR A HB   1 
ATOM   2834  H  HG1  . THR A 1 170 ? 21.329  14.458  14.896  1.00 12.31  ?  393  THR A HG1  1 
ATOM   2835  H  HG21 . THR A 1 170 ? 20.391  13.215  12.645  1.00 10.34  ?  393  THR A HG21 1 
ATOM   2836  H  HG22 . THR A 1 170 ? 20.963  11.746  12.731  1.00 10.34  ?  393  THR A HG22 1 
ATOM   2837  H  HG23 . THR A 1 170 ? 20.154  12.350  13.945  1.00 10.34  ?  393  THR A HG23 1 
ATOM   2838  N  N    . PRO A 1 171 ? 22.033  9.816   14.976  1.00 5.80   ?  394  PRO A N    1 
ATOM   2839  C  CA   . PRO A 1 171 ? 22.276  8.439   14.550  1.00 6.18   ?  394  PRO A CA   1 
ATOM   2840  C  C    . PRO A 1 171 ? 21.700  8.162   13.169  1.00 6.13   ?  394  PRO A C    1 
ATOM   2841  O  O    . PRO A 1 171 ? 20.668  8.704   12.778  1.00 6.86   ?  394  PRO A O    1 
ATOM   2842  C  CB   . PRO A 1 171 ? 21.526  7.629   15.611  1.00 7.23   ?  394  PRO A CB   1 
ATOM   2843  C  CG   . PRO A 1 171 ? 20.380  8.508   15.969  1.00 7.14   ?  394  PRO A CG   1 
ATOM   2844  C  CD   . PRO A 1 171 ? 20.961  9.897   15.984  1.00 6.72   ?  394  PRO A CD   1 
ATOM   2845  H  HA   . PRO A 1 171 ? 23.223  8.229   14.561  1.00 7.41   ?  394  PRO A HA   1 
ATOM   2846  H  HB2  . PRO A 1 171 ? 21.222  6.787   15.238  1.00 8.67   ?  394  PRO A HB2  1 
ATOM   2847  H  HB3  . PRO A 1 171 ? 22.098  7.465   16.376  1.00 8.67   ?  394  PRO A HB3  1 
ATOM   2848  H  HG2  . PRO A 1 171 ? 19.680  8.430   15.303  1.00 8.57   ?  394  PRO A HG2  1 
ATOM   2849  H  HG3  . PRO A 1 171 ? 20.035  8.265   16.843  1.00 8.57   ?  394  PRO A HG3  1 
ATOM   2850  H  HD2  . PRO A 1 171 ? 20.295  10.554  15.730  1.00 8.07   ?  394  PRO A HD2  1 
ATOM   2851  H  HD3  . PRO A 1 171 ? 21.323  10.112  16.858  1.00 8.07   ?  394  PRO A HD3  1 
ATOM   2852  N  N    . ILE A 1 172 ? 22.361  7.247   12.459  1.00 5.89   ?  395  ILE A N    1 
ATOM   2853  C  CA   . ILE A 1 172 ? 21.914  6.740   11.170  1.00 6.26   ?  395  ILE A CA   1 
ATOM   2854  C  C    . ILE A 1 172 ? 21.713  5.236   11.210  1.00 6.06   ?  395  ILE A C    1 
ATOM   2855  O  O    . ILE A 1 172 ? 20.724  4.720   10.704  1.00 6.75   ?  395  ILE A O    1 
ATOM   2856  C  CB   . ILE A 1 172 ? 22.894  7.123   10.048  1.00 7.04   ?  395  ILE A CB   1 
ATOM   2857  C  CG1  . ILE A 1 172 ? 22.944  8.643   9.879   1.00 9.27   ?  395  ILE A CG1  1 
ATOM   2858  C  CG2  . ILE A 1 172 ? 22.526  6.444   8.723   1.00 8.72   ?  395  ILE A CG2  1 
ATOM   2859  C  CD1  . ILE A 1 172 ? 21.713  9.227   9.263   1.00 10.73  ?  395  ILE A CD1  1 
ATOM   2860  H  H    . ILE A 1 172 ? 23.101  6.893   12.718  1.00 7.07   ?  395  ILE A H    1 
ATOM   2861  H  HA   . ILE A 1 172 ? 21.057  7.146   10.964  1.00 7.52   ?  395  ILE A HA   1 
ATOM   2862  H  HB   . ILE A 1 172 ? 23.774  6.809   10.306  1.00 8.45   ?  395  ILE A HB   1 
ATOM   2863  H  HG12 . ILE A 1 172 ? 23.058  9.049   10.753  1.00 11.13  ?  395  ILE A HG12 1 
ATOM   2864  H  HG13 . ILE A 1 172 ? 23.695  8.867   9.309   1.00 11.13  ?  395  ILE A HG13 1 
ATOM   2865  H  HG21 . ILE A 1 172 ? 22.993  6.889   7.999   1.00 10.47  ?  395  ILE A HG21 1 
ATOM   2866  H  HG22 . ILE A 1 172 ? 22.790  5.511   8.762   1.00 10.47  ?  395  ILE A HG22 1 
ATOM   2867  H  HG23 . ILE A 1 172 ? 21.568  6.511   8.589   1.00 10.47  ?  395  ILE A HG23 1 
ATOM   2868  H  HD11 . ILE A 1 172 ? 21.793  10.194  9.254   1.00 12.88  ?  395  ILE A HD11 1 
ATOM   2869  H  HD12 . ILE A 1 172 ? 21.626  8.895   8.355   1.00 12.88  ?  395  ILE A HD12 1 
ATOM   2870  H  HD13 . ILE A 1 172 ? 20.941  8.963   9.787   1.00 12.88  ?  395  ILE A HD13 1 
ATOM   2871  N  N    . GLY A 1 173 ? 22.663  4.512   11.782  1.00 5.71   ?  396  GLY A N    1 
ATOM   2872  C  CA   . GLY A 1 173 ? 22.567  3.072   11.847  1.00 5.71   ?  396  GLY A CA   1 
ATOM   2873  C  C    . GLY A 1 173 ? 23.754  2.516   12.580  1.00 6.20   ?  396  GLY A C    1 
ATOM   2874  O  O    . GLY A 1 173 ? 24.163  3.078   13.600  1.00 6.41   ?  396  GLY A O    1 
ATOM   2875  H  H    . GLY A 1 173 ? 23.375  4.837   12.140  1.00 6.85   ?  396  GLY A H    1 
ATOM   2876  H  HA2  . GLY A 1 173 ? 21.757  2.815   12.314  1.00 6.85   ?  396  GLY A HA2  1 
ATOM   2877  H  HA3  . GLY A 1 173 ? 22.545  2.700   10.951  1.00 6.85   ?  396  GLY A HA3  1 
ATOM   2878  N  N    . LEU A 1 174 ? 24.326  1.429   12.066  1.00 5.58   ?  397  LEU A N    1 
ATOM   2879  C  CA   . LEU A 1 174 ? 25.480  0.791   12.681  1.00 5.77   ?  397  LEU A CA   1 
ATOM   2880  C  C    . LEU A 1 174 ? 26.659  0.864   11.725  1.00 6.05   ?  397  LEU A C    1 
ATOM   2881  O  O    . LEU A 1 174 ? 26.484  0.890   10.508  1.00 6.73   ?  397  LEU A O    1 
ATOM   2882  C  CB   . LEU A 1 174 ? 25.173  -0.679  12.993  1.00 6.57   ?  397  LEU A CB   1 
ATOM   2883  C  CG   . LEU A 1 174 ? 24.021  -0.955  13.963  1.00 6.92   ?  397  LEU A CG   1 
ATOM   2884  C  CD1  . LEU A 1 174 ? 23.727  -2.444  14.029  1.00 8.57   ?  397  LEU A CD1  1 
ATOM   2885  C  CD2  . LEU A 1 174 ? 24.352  -0.428  15.327  1.00 8.93   ?  397  LEU A CD2  1 
ATOM   2886  H  H    . LEU A 1 174 ? 24.057  1.039   11.348  1.00 6.69   ?  397  LEU A H    1 
ATOM   2887  H  HA   . LEU A 1 174 ? 25.717  1.244   13.505  1.00 6.93   ?  397  LEU A HA   1 
ATOM   2888  H  HB2  . LEU A 1 174 ? 24.953  -1.122  12.158  1.00 7.88   ?  397  LEU A HB2  1 
ATOM   2889  H  HB3  . LEU A 1 174 ? 25.970  -1.075  13.379  1.00 7.88   ?  397  LEU A HB3  1 
ATOM   2890  H  HG   . LEU A 1 174 ? 23.223  -0.503  13.646  1.00 8.31   ?  397  LEU A HG   1 
ATOM   2891  H  HD11 . LEU A 1 174 ? 22.990  -2.594  14.642  1.00 10.29  ?  397  LEU A HD11 1 
ATOM   2892  H  HD12 . LEU A 1 174 ? 23.488  -2.758  13.143  1.00 10.29  ?  397  LEU A HD12 1 
ATOM   2893  H  HD13 . LEU A 1 174 ? 24.518  -2.909  14.343  1.00 10.29  ?  397  LEU A HD13 1 
ATOM   2894  H  HD21 . LEU A 1 174 ? 23.640  -0.669  15.940  1.00 10.71  ?  397  LEU A HD21 1 
ATOM   2895  H  HD22 . LEU A 1 174 ? 25.189  -0.818  15.622  1.00 10.71  ?  397  LEU A HD22 1 
ATOM   2896  H  HD23 . LEU A 1 174 ? 24.435  0.538   15.280  1.00 10.71  ?  397  LEU A HD23 1 
ATOM   2897  N  N    . ASN A 1 175 ? 27.869  0.917   12.276  1.00 6.26   ?  398  ASN A N    1 
ATOM   2898  C  CA   A ASN A 1 175 ? 29.045  0.896   11.415  0.58 6.83   ?  398  ASN A CA   1 
ATOM   2899  C  CA   B ASN A 1 175 ? 29.045  0.901   11.412  0.42 7.03   ?  398  ASN A CA   1 
ATOM   2900  C  C    . ASN A 1 175 ? 29.181  -0.452  10.737  1.00 7.78   ?  398  ASN A C    1 
ATOM   2901  O  O    . ASN A 1 175 ? 29.480  -0.535  9.543   1.00 9.19   ?  398  ASN A O    1 
ATOM   2902  C  CB   A ASN A 1 175 ? 30.313  1.158   12.212  0.58 8.19   ?  398  ASN A CB   1 
ATOM   2903  C  CB   B ASN A 1 175 ? 30.301  1.213   12.222  0.42 8.20   ?  398  ASN A CB   1 
ATOM   2904  C  CG   A ASN A 1 175 ? 31.545  1.067   11.347  0.58 9.25   ?  398  ASN A CG   1 
ATOM   2905  C  CG   B ASN A 1 175 ? 31.513  1.444   11.341  0.42 9.37   ?  398  ASN A CG   1 
ATOM   2906  O  OD1  A ASN A 1 175 ? 31.838  1.992   10.600  0.58 8.84   ?  398  ASN A OD1  1 
ATOM   2907  O  OD1  B ASN A 1 175 ? 31.387  1.833   10.186  0.42 9.21   ?  398  ASN A OD1  1 
ATOM   2908  N  ND2  A ASN A 1 175 ? 32.249  -0.053  11.416  0.58 10.38  ?  398  ASN A ND2  1 
ATOM   2909  N  ND2  B ASN A 1 175 ? 32.693  1.201   11.883  0.42 9.49   ?  398  ASN A ND2  1 
ATOM   2910  H  H    A ASN A 1 175 ? 28.031  0.963   13.120  0.58 7.52   ?  398  ASN A H    1 
ATOM   2911  H  H    B ASN A 1 175 ? 28.032  0.960   13.120  0.42 7.52   ?  398  ASN A H    1 
ATOM   2912  H  HA   A ASN A 1 175 ? 28.942  1.600   10.756  0.58 8.20   ?  398  ASN A HA   1 
ATOM   2913  H  HA   B ASN A 1 175 ? 28.950  1.588   10.733  0.42 8.44   ?  398  ASN A HA   1 
ATOM   2914  H  HB2  A ASN A 1 175 ? 30.274  2.049   12.592  0.58 9.83   ?  398  ASN A HB2  1 
ATOM   2915  H  HB2  B ASN A 1 175 ? 30.150  2.017   12.744  0.42 9.84   ?  398  ASN A HB2  1 
ATOM   2916  H  HB3  A ASN A 1 175 ? 30.389  0.498   12.919  0.58 9.83   ?  398  ASN A HB3  1 
ATOM   2917  H  HB3  B ASN A 1 175 ? 30.493  0.466   12.810  0.42 9.84   ?  398  ASN A HB3  1 
ATOM   2918  H  HD21 A ASN A 1 175 ? 32.959  -0.144  10.938  0.58 12.45  ?  398  ASN A HD21 1 
ATOM   2919  H  HD21 B ASN A 1 175 ? 33.410  1.317   11.423  0.42 11.39  ?  398  ASN A HD21 1 
ATOM   2920  H  HD22 A ASN A 1 175 ? 31.997  -0.688  11.938  0.58 12.45  ?  398  ASN A HD22 1 
ATOM   2921  H  HD22 B ASN A 1 175 ? 32.745  0.927   12.697  0.42 11.39  ?  398  ASN A HD22 1 
ATOM   2922  N  N    . ASP A 1 176 ? 28.940  -1.506  11.496  1.00 8.01   ?  399  ASP A N    1 
ATOM   2923  C  CA   . ASP A 1 176 ? 29.037  -2.897  11.096  1.00 8.50   ?  399  ASP A CA   1 
ATOM   2924  C  C    . ASP A 1 176 ? 28.118  -3.613  12.073  1.00 8.61   ?  399  ASP A C    1 
ATOM   2925  O  O    . ASP A 1 176 ? 27.723  -3.042  13.082  1.00 10.48  ?  399  ASP A O    1 
ATOM   2926  C  CB   . ASP A 1 176 ? 30.480  -3.406  11.208  1.00 9.82   ?  399  ASP A CB   1 
ATOM   2927  C  CG   . ASP A 1 176 ? 30.987  -3.426  12.636  1.00 10.93  ?  399  ASP A CG   1 
ATOM   2928  O  OD1  . ASP A 1 176 ? 30.626  -4.359  13.374  1.00 10.45  ?  399  ASP A OD1  1 
ATOM   2929  O  OD2  . ASP A 1 176 ? 31.731  -2.505  13.031  1.00 13.86  -1 399  ASP A OD2  1 
ATOM   2930  H  H    . ASP A 1 176 ? 28.698  -1.436  12.319  1.00 9.61   ?  399  ASP A H    1 
ATOM   2931  H  HA   . ASP A 1 176 ? 28.760  -3.044  10.178  1.00 10.20  ?  399  ASP A HA   1 
ATOM   2932  H  HB2  . ASP A 1 176 ? 30.524  -4.311  10.862  1.00 11.78  ?  399  ASP A HB2  1 
ATOM   2933  H  HB3  . ASP A 1 176 ? 31.061  -2.826  10.692  1.00 11.78  ?  399  ASP A HB3  1 
ATOM   2934  N  N    . ASP A 1 177 ? 27.790  -4.866  11.803  1.00 10.33  ?  400  ASP A N    1 
ATOM   2935  C  CA   . ASP A 1 177 ? 27.032  -5.614  12.806  1.00 10.95  ?  400  ASP A CA   1 
ATOM   2936  C  C    . ASP A 1 177 ? 27.808  -6.825  13.309  1.00 11.51  ?  400  ASP A C    1 
ATOM   2937  O  O    . ASP A 1 177 ? 27.205  -7.774  13.826  1.00 13.46  ?  400  ASP A O    1 
ATOM   2938  C  CB   . ASP A 1 177 ? 25.622  -5.965  12.337  1.00 12.34  ?  400  ASP A CB   1 
ATOM   2939  C  CG   . ASP A 1 177 ? 25.611  -7.023  11.275  1.00 14.28  ?  400  ASP A CG   1 
ATOM   2940  O  OD1  . ASP A 1 177 ? 26.658  -7.220  10.623  1.00 16.27  -1 400  ASP A OD1  1 
ATOM   2941  O  OD2  . ASP A 1 177 ? 24.558  -7.673  11.106  1.00 15.56  -1 400  ASP A OD2  1 
ATOM   2942  H  H    . ASP A 1 177 ? 27.984  -5.290  11.081  1.00 12.40  ?  400  ASP A H    1 
ATOM   2943  H  HA   . ASP A 1 177 ? 26.891  -5.034  13.571  1.00 13.14  ?  400  ASP A HA   1 
ATOM   2944  H  HB2  . ASP A 1 177 ? 25.110  -6.293  13.093  1.00 14.81  ?  400  ASP A HB2  1 
ATOM   2945  H  HB3  . ASP A 1 177 ? 25.203  -5.170  11.973  1.00 14.81  ?  400  ASP A HB3  1 
ATOM   2946  N  N    . ASP A 1 178 ? 29.139  -6.770  13.218  1.00 10.39  ?  401  ASP A N    1 
ATOM   2947  C  CA   . ASP A 1 178 ? 29.979  -7.901  13.591  1.00 11.55  ?  401  ASP A CA   1 
ATOM   2948  C  C    . ASP A 1 178 ? 29.647  -8.412  14.985  1.00 12.13  ?  401  ASP A C    1 
ATOM   2949  O  O    . ASP A 1 178 ? 29.589  -9.625  15.216  1.00 13.34  ?  401  ASP A O    1 
ATOM   2950  C  CB   . ASP A 1 178 ? 31.456  -7.489  13.580  1.00 12.92  ?  401  ASP A CB   1 
ATOM   2951  C  CG   . ASP A 1 178 ? 31.975  -7.143  12.192  1.00 14.53  ?  401  ASP A CG   1 
ATOM   2952  O  OD1  . ASP A 1 178 ? 31.234  -7.294  11.201  1.00 15.60  ?  401  ASP A OD1  1 
ATOM   2953  O  OD2  . ASP A 1 178 ? 33.141  -6.702  12.095  1.00 17.52  -1 401  ASP A OD2  1 
ATOM   2954  H  H    . ASP A 1 178 ? 29.580  -6.086  12.941  1.00 12.47  ?  401  ASP A H    1 
ATOM   2955  H  HA   . ASP A 1 178 ? 29.827  -8.605  12.941  1.00 13.86  ?  401  ASP A HA   1 
ATOM   2956  H  HB2  . ASP A 1 178 ? 31.568  -6.707  14.143  1.00 15.50  ?  401  ASP A HB2  1 
ATOM   2957  H  HB3  . ASP A 1 178 ? 31.989  -8.223  13.923  1.00 15.50  ?  401  ASP A HB3  1 
ATOM   2958  N  N    . ASN A 1 179 ? 29.451  -7.498  15.930  1.00 11.61  ?  402  ASN A N    1 
ATOM   2959  C  CA   . ASN A 1 179 ? 29.200  -7.849  17.322  1.00 13.03  ?  402  ASN A CA   1 
ATOM   2960  C  C    . ASN A 1 179 ? 28.019  -7.058  17.869  1.00 11.16  ?  402  ASN A C    1 
ATOM   2961  O  O    . ASN A 1 179 ? 27.978  -6.729  19.056  1.00 12.81  ?  402  ASN A O    1 
ATOM   2962  C  CB   . ASN A 1 179 ? 30.441  -7.612  18.183  1.00 16.62  ?  402  ASN A CB   1 
ATOM   2963  C  CG   . ASN A 1 179 ? 31.632  -8.412  17.718  1.00 20.41  ?  402  ASN A CG   1 
ATOM   2964  O  OD1  . ASN A 1 179 ? 31.630  -9.639  17.786  1.00 22.12  ?  402  ASN A OD1  1 
ATOM   2965  N  ND2  . ASN A 1 179 ? 32.660  -7.719  17.241  1.00 21.48  ?  402  ASN A ND2  1 
ATOM   2966  H  H    . ASN A 1 179 ? 29.459  -6.650  15.786  1.00 13.94  ?  402  ASN A H    1 
ATOM   2967  H  HA   . ASN A 1 179 ? 28.984  -8.793  17.370  1.00 15.64  ?  402  ASN A HA   1 
ATOM   2968  H  HB2  . ASN A 1 179 ? 30.677  -6.672  18.146  1.00 19.95  ?  402  ASN A HB2  1 
ATOM   2969  H  HB3  . ASN A 1 179 ? 30.245  -7.870  19.097  1.00 19.95  ?  402  ASN A HB3  1 
ATOM   2970  H  HD21 . ASN A 1 179 ? 32.622  -6.861  17.210  1.00 25.78  ?  402  ASN A HD21 1 
ATOM   2971  H  HD22 . ASN A 1 179 ? 33.363  -8.129  16.963  1.00 25.78  ?  402  ASN A HD22 1 
ATOM   2972  N  N    . PHE A 1 180 ? 27.062  -6.731  17.009  1.00 9.58   ?  403  PHE A N    1 
ATOM   2973  C  CA   . PHE A 1 180 ? 25.863  -6.021  17.442  1.00 8.32   ?  403  PHE A CA   1 
ATOM   2974  C  C    . PHE A 1 180 ? 24.971  -6.960  18.240  1.00 7.29   ?  403  PHE A C    1 
ATOM   2975  O  O    . PHE A 1 180 ? 24.482  -7.967  17.720  1.00 8.12   ?  403  PHE A O    1 
ATOM   2976  C  CB   . PHE A 1 180 ? 25.134  -5.492  16.209  1.00 8.04   ?  403  PHE A CB   1 
ATOM   2977  C  CG   . PHE A 1 180 ? 23.752  -4.953  16.475  1.00 6.71   ?  403  PHE A CG   1 
ATOM   2978  C  CD1  . PHE A 1 180 ? 23.544  -3.967  17.424  1.00 7.13   ?  403  PHE A CD1  1 
ATOM   2979  C  CD2  . PHE A 1 180 ? 22.674  -5.406  15.750  1.00 7.10   ?  403  PHE A CD2  1 
ATOM   2980  C  CE1  . PHE A 1 180 ? 22.277  -3.457  17.635  1.00 7.60   ?  403  PHE A CE1  1 
ATOM   2981  C  CE2  . PHE A 1 180 ? 21.419  -4.905  15.948  1.00 7.21   ?  403  PHE A CE2  1 
ATOM   2982  C  CZ   . PHE A 1 180 ? 21.211  -3.933  16.900  1.00 7.81   ?  403  PHE A CZ   1 
ATOM   2983  H  H    . PHE A 1 180 ? 27.081  -6.908  16.167  1.00 11.50  ?  403  PHE A H    1 
ATOM   2984  H  HA   . PHE A 1 180 ? 26.099  -5.275  18.015  1.00 9.98   ?  403  PHE A HA   1 
ATOM   2985  H  HB2  . PHE A 1 180 ? 25.659  -4.771  15.826  1.00 9.65   ?  403  PHE A HB2  1 
ATOM   2986  H  HB3  . PHE A 1 180 ? 25.046  -6.215  15.568  1.00 9.65   ?  403  PHE A HB3  1 
ATOM   2987  H  HD1  . PHE A 1 180 ? 24.261  -3.647  17.922  1.00 8.56   ?  403  PHE A HD1  1 
ATOM   2988  H  HD2  . PHE A 1 180 ? 22.803  -6.069  15.111  1.00 8.52   ?  403  PHE A HD2  1 
ATOM   2989  H  HE1  . PHE A 1 180 ? 22.144  -2.793  18.272  1.00 9.13   ?  403  PHE A HE1  1 
ATOM   2990  H  HE2  . PHE A 1 180 ? 20.706  -5.221  15.441  1.00 8.65   ?  403  PHE A HE2  1 
ATOM   2991  H  HZ   . PHE A 1 180 ? 20.356  -3.599  17.047  1.00 9.38   ?  403  PHE A HZ   1 
ATOM   2992  N  N    . LYS A 1 181 ? 24.763  -6.640  19.511  1.00 6.61   ?  404  LYS A N    1 
ATOM   2993  C  CA   . LYS A 1 181 ? 23.985  -7.473  20.443  1.00 6.71   ?  404  LYS A CA   1 
ATOM   2994  C  C    . LYS A 1 181 ? 22.894  -6.585  21.024  1.00 5.85   ?  404  LYS A C    1 
ATOM   2995  O  O    . LYS A 1 181 ? 23.118  -5.886  22.011  1.00 6.36   ?  404  LYS A O    1 
ATOM   2996  C  CB   . LYS A 1 181 ? 24.868  -8.089  21.513  1.00 8.18   ?  404  LYS A CB   1 
ATOM   2997  C  CG   . LYS A 1 181 ? 25.907  -9.048  20.949  1.00 11.08  ?  404  LYS A CG   1 
ATOM   2998  C  CD   . LYS A 1 181 ? 25.250  -10.322 20.406  1.00 15.89  ?  404  LYS A CD   1 
ATOM   2999  C  CE   . LYS A 1 181 ? 26.231  -11.471 20.259  1.00 21.15  ?  404  LYS A CE   1 
ATOM   3000  N  NZ   . LYS A 1 181 ? 25.540  -12.711 19.814  1.00 24.22  ?  404  LYS A NZ   1 
ATOM   3001  H  H    . LYS A 1 181 ? 25.069  -5.924  19.876  1.00 7.94   ?  404  LYS A H    1 
ATOM   3002  H  HA   . LYS A 1 181 ? 23.567  -8.202  19.960  1.00 8.05   ?  404  LYS A HA   1 
ATOM   3003  H  HB2  . LYS A 1 181 ? 25.338  -7.380  21.979  1.00 9.81   ?  404  LYS A HB2  1 
ATOM   3004  H  HB3  . LYS A 1 181 ? 24.311  -8.582  22.134  1.00 9.81   ?  404  LYS A HB3  1 
ATOM   3005  H  HG2  . LYS A 1 181 ? 26.384  -8.617  20.224  1.00 13.30  ?  404  LYS A HG2  1 
ATOM   3006  H  HG3  . LYS A 1 181 ? 26.527  -9.300  21.651  1.00 13.30  ?  404  LYS A HG3  1 
ATOM   3007  H  HD2  . LYS A 1 181 ? 24.550  -10.602 21.015  1.00 19.07  ?  404  LYS A HD2  1 
ATOM   3008  H  HD3  . LYS A 1 181 ? 24.874  -10.136 19.531  1.00 19.07  ?  404  LYS A HD3  1 
ATOM   3009  H  HE2  . LYS A 1 181 ? 26.902  -11.239 19.599  1.00 25.39  ?  404  LYS A HE2  1 
ATOM   3010  H  HE3  . LYS A 1 181 ? 26.653  -11.645 21.115  1.00 25.39  ?  404  LYS A HE3  1 
ATOM   3011  H  HZ1  . LYS A 1 181 ? 26.128  -13.374 19.732  1.00 29.07  ?  404  LYS A HZ1  1 
ATOM   3012  H  HZ2  . LYS A 1 181 ? 24.922  -12.945 20.409  1.00 29.07  ?  404  LYS A HZ2  1 
ATOM   3013  H  HZ3  . LYS A 1 181 ? 25.147  -12.574 19.027  1.00 29.07  ?  404  LYS A HZ3  1 
ATOM   3014  N  N    . GLN A 1 182 ? 21.705  -6.635  20.417  1.00 5.71   ?  405  GLN A N    1 
ATOM   3015  C  CA   . GLN A 1 182 ? 20.642  -5.717  20.804  1.00 5.38   ?  405  GLN A CA   1 
ATOM   3016  C  C    . GLN A 1 182 ? 20.112  -5.985  22.211  1.00 5.96   ?  405  GLN A C    1 
ATOM   3017  O  O    . GLN A 1 182 ? 19.477  -5.103  22.790  1.00 6.74   ?  405  GLN A O    1 
ATOM   3018  C  CB   . GLN A 1 182 ? 19.495  -5.717  19.796  1.00 5.90   ?  405  GLN A CB   1 
ATOM   3019  C  CG   . GLN A 1 182 ? 18.644  -6.966  19.798  1.00 6.23   ?  405  GLN A CG   1 
ATOM   3020  C  CD   . GLN A 1 182 ? 17.280  -6.724  19.203  1.00 6.24   ?  405  GLN A CD   1 
ATOM   3021  O  OE1  . GLN A 1 182 ? 16.673  -5.672  19.415  1.00 6.35   ?  405  GLN A OE1  1 
ATOM   3022  N  NE2  . GLN A 1 182 ? 16.775  -7.707  18.488  1.00 7.23   ?  405  GLN A NE2  1 
ATOM   3023  H  H    . GLN A 1 182 ? 21.495  -7.183  19.789  1.00 6.85   ?  405  GLN A H    1 
ATOM   3024  H  HA   . GLN A 1 182 ? 21.016  -4.822  20.794  1.00 6.45   ?  405  GLN A HA   1 
ATOM   3025  H  HB2  . GLN A 1 182 ? 18.912  -4.968  19.993  1.00 7.08   ?  405  GLN A HB2  1 
ATOM   3026  H  HB3  . GLN A 1 182 ? 19.869  -5.622  18.906  1.00 7.08   ?  405  GLN A HB3  1 
ATOM   3027  H  HG2  . GLN A 1 182 ? 19.085  -7.653  19.274  1.00 7.47   ?  405  GLN A HG2  1 
ATOM   3028  H  HG3  . GLN A 1 182 ? 18.526  -7.270  20.712  1.00 7.47   ?  405  GLN A HG3  1 
ATOM   3029  H  HE21 . GLN A 1 182 ? 17.221  -8.435  18.383  1.00 8.68   ?  405  GLN A HE21 1 
ATOM   3030  H  HE22 . GLN A 1 182 ? 16.000  -7.621  18.126  1.00 8.68   ?  405  GLN A HE22 1 
ATOM   3031  N  N    . TRP A 1 183 ? 20.325  -7.184  22.750  1.00 6.57   ?  406  TRP A N    1 
ATOM   3032  C  CA   . TRP A 1 183 ? 19.812  -7.535  24.065  1.00 7.43   ?  406  TRP A CA   1 
ATOM   3033  C  C    . TRP A 1 183 ? 20.888  -7.525  25.142  1.00 8.54   ?  406  TRP A C    1 
ATOM   3034  O  O    . TRP A 1 183 ? 20.601  -7.902  26.280  1.00 11.77  ?  406  TRP A O    1 
ATOM   3035  C  CB   . TRP A 1 183 ? 19.099  -8.890  24.044  1.00 8.50   ?  406  TRP A CB   1 
ATOM   3036  C  CG   . TRP A 1 183 ? 17.969  -8.942  23.097  1.00 7.41   ?  406  TRP A CG   1 
ATOM   3037  C  CD1  . TRP A 1 183 ? 17.813  -9.817  22.063  1.00 8.16   ?  406  TRP A CD1  1 
ATOM   3038  C  CD2  . TRP A 1 183 ? 16.822  -8.079  23.076  1.00 7.43   ?  406  TRP A CD2  1 
ATOM   3039  N  NE1  . TRP A 1 183 ? 16.629  -9.562  21.405  1.00 8.81   ?  406  TRP A NE1  1 
ATOM   3040  C  CE2  . TRP A 1 183 ? 16.004  -8.498  22.003  1.00 8.18   ?  406  TRP A CE2  1 
ATOM   3041  C  CE3  . TRP A 1 183 ? 16.406  -6.993  23.853  1.00 7.60   ?  406  TRP A CE3  1 
ATOM   3042  C  CZ2  . TRP A 1 183 ? 14.802  -7.877  21.701  1.00 8.39   ?  406  TRP A CZ2  1 
ATOM   3043  C  CZ3  . TRP A 1 183 ? 15.212  -6.370  23.533  1.00 8.20   ?  406  TRP A CZ3  1 
ATOM   3044  C  CH2  . TRP A 1 183 ? 14.433  -6.804  22.457  1.00 8.05   ?  406  TRP A CH2  1 
ATOM   3045  H  H    . TRP A 1 183 ? 20.769  -7.813  22.368  1.00 7.88   ?  406  TRP A H    1 
ATOM   3046  H  HA   . TRP A 1 183 ? 19.145  -6.872  24.304  1.00 8.92   ?  406  TRP A HA   1 
ATOM   3047  H  HB2  . TRP A 1 183 ? 19.735  -9.575  23.786  1.00 10.20  ?  406  TRP A HB2  1 
ATOM   3048  H  HB3  . TRP A 1 183 ? 18.753  -9.076  24.931  1.00 10.20  ?  406  TRP A HB3  1 
ATOM   3049  H  HD1  . TRP A 1 183 ? 18.417  -10.487 21.836  1.00 9.80   ?  406  TRP A HD1  1 
ATOM   3050  H  HE1  . TRP A 1 183 ? 16.330  -10.001 20.728  1.00 10.57  ?  406  TRP A HE1  1 
ATOM   3051  H  HE3  . TRP A 1 183 ? 16.920  -6.696  24.568  1.00 9.12   ?  406  TRP A HE3  1 
ATOM   3052  H  HZ2  . TRP A 1 183 ? 14.265  -8.182  21.006  1.00 10.07  ?  406  TRP A HZ2  1 
ATOM   3053  H  HZ3  . TRP A 1 183 ? 14.922  -5.649  24.044  1.00 9.84   ?  406  TRP A HZ3  1 
ATOM   3054  H  HH2  . TRP A 1 183 ? 13.646  -6.352  22.253  1.00 9.66   ?  406  TRP A HH2  1 
ATOM   3055  N  N    . GLU A 1 184 ? 22.092  -7.068  24.819  1.00 6.85   ?  407  GLU A N    1 
ATOM   3056  C  CA   . GLU A 1 184 ? 23.174  -6.911  25.779  1.00 6.43   ?  407  GLU A CA   1 
ATOM   3057  C  C    . GLU A 1 184 ? 23.350  -5.426  26.051  1.00 6.49   ?  407  GLU A C    1 
ATOM   3058  O  O    . GLU A 1 184 ? 23.672  -4.661  25.145  1.00 7.93   ?  407  GLU A O    1 
ATOM   3059  C  CB   . GLU A 1 184 ? 24.469  -7.537  25.266  1.00 7.41   ?  407  GLU A CB   1 
ATOM   3060  C  CG   . GLU A 1 184 ? 24.327  -9.037  25.097  1.00 8.38   ?  407  GLU A CG   1 
ATOM   3061  C  CD   . GLU A 1 184 ? 25.586  -9.729  24.602  1.00 10.62  ?  407  GLU A CD   1 
ATOM   3062  O  OE1  . GLU A 1 184 ? 26.671  -9.140  24.673  1.00 11.56  ?  407  GLU A OE1  1 
ATOM   3063  O  OE2  . GLU A 1 184 ? 25.479  -10.883 24.139  1.00 13.78  -1 407  GLU A OE2  1 
ATOM   3064  H  H    . GLU A 1 184 ? 22.313  -6.836  24.021  1.00 8.23   ?  407  GLU A H    1 
ATOM   3065  H  HA   . GLU A 1 184 ? 22.946  -7.354  26.611  1.00 7.72   ?  407  GLU A HA   1 
ATOM   3066  H  HB2  . GLU A 1 184 ? 24.694  -7.152  24.404  1.00 8.89   ?  407  GLU A HB2  1 
ATOM   3067  H  HB3  . GLU A 1 184 ? 25.182  -7.367  25.901  1.00 8.89   ?  407  GLU A HB3  1 
ATOM   3068  H  HG2  . GLU A 1 184 ? 24.096  -9.426  25.955  1.00 10.06  ?  407  GLU A HG2  1 
ATOM   3069  H  HG3  . GLU A 1 184 ? 23.623  -9.211  24.453  1.00 10.06  ?  407  GLU A HG3  1 
ATOM   3070  N  N    . LEU A 1 185 ? 23.112  -5.018  27.296  1.00 6.51   ?  408  LEU A N    1 
ATOM   3071  C  CA   . LEU A 1 185 ? 23.276  -3.621  27.647  1.00 6.82   ?  408  LEU A CA   1 
ATOM   3072  C  C    . LEU A 1 185 ? 24.753  -3.234  27.632  1.00 7.20   ?  408  LEU A C    1 
ATOM   3073  O  O    . LEU A 1 185 ? 25.626  -4.032  27.983  1.00 7.62   ?  408  LEU A O    1 
ATOM   3074  C  CB   . LEU A 1 185 ? 22.701  -3.339  29.031  1.00 7.40   ?  408  LEU A CB   1 
ATOM   3075  C  CG   . LEU A 1 185 ? 21.184  -3.508  29.178  1.00 7.07   ?  408  LEU A CG   1 
ATOM   3076  C  CD1  . LEU A 1 185 ? 20.758  -3.279  30.598  1.00 8.48   ?  408  LEU A CD1  1 
ATOM   3077  C  CD2  . LEU A 1 185 ? 20.463  -2.545  28.233  1.00 7.77   ?  408  LEU A CD2  1 
ATOM   3078  H  H    . LEU A 1 185 ? 22.859  -5.525  27.942  1.00 7.81   ?  408  LEU A H    1 
ATOM   3079  H  HA   . LEU A 1 185 ? 22.802  -3.076  26.999  1.00 8.18   ?  408  LEU A HA   1 
ATOM   3080  H  HB2  . LEU A 1 185 ? 23.120  -3.946  29.661  1.00 8.88   ?  408  LEU A HB2  1 
ATOM   3081  H  HB3  . LEU A 1 185 ? 22.912  -2.422  29.264  1.00 8.88   ?  408  LEU A HB3  1 
ATOM   3082  H  HG   . LEU A 1 185 ? 20.935  -4.415  28.942  1.00 8.48   ?  408  LEU A HG   1 
ATOM   3083  H  HD11 . LEU A 1 185 ? 19.799  -3.405  30.664  1.00 10.17  ?  408  LEU A HD11 1 
ATOM   3084  H  HD12 . LEU A 1 185 ? 21.215  -3.915  31.170  1.00 10.17  ?  408  LEU A HD12 1 
ATOM   3085  H  HD13 . LEU A 1 185 ? 20.992  -2.374  30.856  1.00 10.17  ?  408  LEU A HD13 1 
ATOM   3086  H  HD21 . LEU A 1 185 ? 19.515  -2.550  28.439  1.00 9.32   ?  408  LEU A HD21 1 
ATOM   3087  H  HD22 . LEU A 1 185 ? 20.823  -1.653  28.355  1.00 9.32   ?  408  LEU A HD22 1 
ATOM   3088  H  HD23 . LEU A 1 185 ? 20.603  -2.835  27.318  1.00 9.32   ?  408  LEU A HD23 1 
ATOM   3089  N  N    . PRO A 1 186 ? 25.057  -1.996  27.254  1.00 7.12   ?  409  PRO A N    1 
ATOM   3090  C  CA   . PRO A 1 186 ? 26.416  -1.484  27.435  1.00 7.61   ?  409  PRO A CA   1 
ATOM   3091  C  C    . PRO A 1 186 ? 26.684  -1.270  28.914  1.00 7.05   ?  409  PRO A C    1 
ATOM   3092  O  O    . PRO A 1 186 ? 25.774  -1.288  29.745  1.00 7.92   ?  409  PRO A O    1 
ATOM   3093  C  CB   . PRO A 1 186 ? 26.383  -0.163  26.671  1.00 9.34   ?  409  PRO A CB   1 
ATOM   3094  C  CG   . PRO A 1 186 ? 24.990  0.249   26.672  1.00 9.53   ?  409  PRO A CG   1 
ATOM   3095  C  CD   . PRO A 1 186 ? 24.123  -0.958  26.808  1.00 7.86   ?  409  PRO A CD   1 
ATOM   3096  H  HA   . PRO A 1 186 ? 27.090  -2.065  27.049  1.00 9.13   ?  409  PRO A HA   1 
ATOM   3097  H  HB2  . PRO A 1 186 ? 26.937  0.492   27.123  1.00 11.21  ?  409  PRO A HB2  1 
ATOM   3098  H  HB3  . PRO A 1 186 ? 26.703  -0.300  25.765  1.00 11.21  ?  409  PRO A HB3  1 
ATOM   3099  H  HG2  . PRO A 1 186 ? 24.841  0.850   27.418  1.00 11.43  ?  409  PRO A HG2  1 
ATOM   3100  H  HG3  . PRO A 1 186 ? 24.797  0.703   25.836  1.00 11.43  ?  409  PRO A HG3  1 
ATOM   3101  H  HD2  . PRO A 1 186 ? 23.428  -0.811  27.468  1.00 9.44   ?  409  PRO A HD2  1 
ATOM   3102  H  HD3  . PRO A 1 186 ? 23.725  -1.195  25.955  1.00 9.44   ?  409  PRO A HD3  1 
ATOM   3103  N  N    . ASN A 1 187 ? 27.960  -1.048  29.244  1.00 7.47   ?  410  ASN A N    1 
ATOM   3104  C  CA   . ASN A 1 187 ? 28.325  -0.601  30.581  1.00 7.27   ?  410  ASN A CA   1 
ATOM   3105  C  C    . ASN A 1 187 ? 28.218  0.919   30.572  1.00 7.08   ?  410  ASN A C    1 
ATOM   3106  O  O    . ASN A 1 187 ? 29.108  1.608   30.066  1.00 8.84   ?  410  ASN A O    1 
ATOM   3107  C  CB   . ASN A 1 187 ? 29.757  -0.983  30.934  1.00 8.96   ?  410  ASN A CB   1 
ATOM   3108  C  CG   . ASN A 1 187 ? 29.943  -2.458  31.199  1.00 12.13  ?  410  ASN A CG   1 
ATOM   3109  O  OD1  . ASN A 1 187 ? 29.447  -3.309  30.478  1.00 14.45  ?  410  ASN A OD1  1 
ATOM   3110  N  ND2  . ASN A 1 187 ? 30.715  -2.760  32.218  1.00 12.97  ?  410  ASN A ND2  1 
ATOM   3111  H  H    . ASN A 1 187 ? 28.626  -1.149  28.709  1.00 8.96   ?  410  ASN A H    1 
ATOM   3112  H  HA   . ASN A 1 187 ? 27.720  -1.006  31.222  1.00 8.72   ?  410  ASN A HA   1 
ATOM   3113  H  HB2  . ASN A 1 187 ? 30.337  -0.740  30.196  1.00 10.76  ?  410  ASN A HB2  1 
ATOM   3114  H  HB3  . ASN A 1 187 ? 30.020  -0.504  31.735  1.00 10.76  ?  410  ASN A HB3  1 
ATOM   3115  H  HD21 . ASN A 1 187 ? 30.859  -3.584  32.419  1.00 15.57  ?  410  ASN A HD21 1 
ATOM   3116  H  HD22 . ASN A 1 187 ? 31.076  -2.134  32.685  1.00 15.57  ?  410  ASN A HD22 1 
ATOM   3117  N  N    . TYR A 1 188 ? 27.152  1.464   31.147  1.00 6.79   ?  411  TYR A N    1 
ATOM   3118  C  CA   . TYR A 1 188 ? 26.968  2.905   31.125  1.00 6.79   ?  411  TYR A CA   1 
ATOM   3119  C  C    . TYR A 1 188 ? 28.033  3.648   31.926  1.00 7.23   ?  411  TYR A C    1 
ATOM   3120  O  O    . TYR A 1 188 ? 28.250  4.842   31.684  1.00 7.55   ?  411  TYR A O    1 
ATOM   3121  C  CB   . TYR A 1 188 ? 25.580  3.260   31.636  1.00 7.03   ?  411  TYR A CB   1 
ATOM   3122  C  CG   . TYR A 1 188 ? 24.428  2.703   30.824  1.00 7.08   ?  411  TYR A CG   1 
ATOM   3123  C  CD1  . TYR A 1 188 ? 24.185  3.135   29.530  1.00 7.37   ?  411  TYR A CD1  1 
ATOM   3124  C  CD2  . TYR A 1 188 ? 23.561  1.784   31.372  1.00 7.25   ?  411  TYR A CD2  1 
ATOM   3125  C  CE1  . TYR A 1 188 ? 23.105  2.663   28.802  1.00 7.46   ?  411  TYR A CE1  1 
ATOM   3126  C  CE2  . TYR A 1 188 ? 22.481  1.292   30.660  1.00 7.81   ?  411  TYR A CE2  1 
ATOM   3127  C  CZ   . TYR A 1 188 ? 22.258  1.746   29.377  1.00 7.30   ?  411  TYR A CZ   1 
ATOM   3128  O  OH   . TYR A 1 188 ? 21.189  1.242   28.692  1.00 7.63   ?  411  TYR A OH   1 
ATOM   3129  H  H    . TYR A 1 188 ? 26.531  1.026   31.550  1.00 8.15   ?  411  TYR A H    1 
ATOM   3130  H  HA   . TYR A 1 188 ? 27.034  3.211   30.207  1.00 8.15   ?  411  TYR A HA   1 
ATOM   3131  H  HB2  . TYR A 1 188 ? 25.490  2.916   32.539  1.00 8.44   ?  411  TYR A HB2  1 
ATOM   3132  H  HB3  . TYR A 1 188 ? 25.493  4.226   31.638  1.00 8.44   ?  411  TYR A HB3  1 
ATOM   3133  H  HD1  . TYR A 1 188 ? 24.759  3.756   29.142  1.00 8.85   ?  411  TYR A HD1  1 
ATOM   3134  H  HD2  . TYR A 1 188 ? 23.704  1.486   32.241  1.00 8.70   ?  411  TYR A HD2  1 
ATOM   3135  H  HE1  . TYR A 1 188 ? 22.955  2.962   27.934  1.00 8.95   ?  411  TYR A HE1  1 
ATOM   3136  H  HE2  . TYR A 1 188 ? 21.912  0.663   31.042  1.00 9.37   ?  411  TYR A HE2  1 
ATOM   3137  H  HH   . TYR A 1 188 ? 21.130  1.610   27.939  1.00 9.16   ?  411  TYR A HH   1 
ATOM   3138  N  N    . SER A 1 189 ? 28.677  2.978   32.886  1.00 7.56   ?  412  SER A N    1 
ATOM   3139  C  CA   . SER A 1 189 ? 29.790  3.530   33.644  1.00 8.45   ?  412  SER A CA   1 
ATOM   3140  C  C    . SER A 1 189 ? 31.109  2.828   33.347  1.00 8.97   ?  412  SER A C    1 
ATOM   3141  O  O    . SER A 1 189 ? 32.058  2.962   34.117  1.00 11.07  ?  412  SER A O    1 
ATOM   3142  C  CB   . SER A 1 189 ? 29.513  3.448   35.140  1.00 9.72   ?  412  SER A CB   1 
ATOM   3143  O  OG   . SER A 1 189 ? 28.412  4.254   35.461  1.00 10.70  ?  412  SER A OG   1 
ATOM   3144  H  H    . SER A 1 189 ? 28.476  2.175   33.120  1.00 9.08   ?  412  SER A H    1 
ATOM   3145  H  HA   . SER A 1 189 ? 29.877  4.463   33.391  1.00 10.15  ?  412  SER A HA   1 
ATOM   3146  H  HB2  . SER A 1 189 ? 29.318  2.529   35.380  1.00 11.67  ?  412  SER A HB2  1 
ATOM   3147  H  HB3  . SER A 1 189 ? 30.292  3.760   35.628  1.00 11.67  ?  412  SER A HB3  1 
ATOM   3148  H  HG   . SER A 1 189 ? 28.281  4.244   36.290  1.00 12.84  ?  412  SER A HG   1 
ATOM   3149  N  N    . GLY A 1 190 ? 31.205  2.089   32.259  1.00 8.24   ?  413  GLY A N    1 
ATOM   3150  C  CA   . GLY A 1 190 ? 32.473  1.471   31.946  1.00 11.06  ?  413  GLY A CA   1 
ATOM   3151  C  C    . GLY A 1 190 ? 32.825  0.247   32.775  1.00 11.52  ?  413  GLY A C    1 
ATOM   3152  O  O    . GLY A 1 190 ? 32.015  -0.373  33.495  1.00 10.80  ?  413  GLY A O    1 
ATOM   3153  H  H    . GLY A 1 190 ? 30.568  1.935   31.702  1.00 9.90   ?  413  GLY A H    1 
ATOM   3154  H  HA2  . GLY A 1 190 ? 32.464  1.201   31.015  1.00 13.27  ?  413  GLY A HA2  1 
ATOM   3155  H  HA3  . GLY A 1 190 ? 33.177  2.125   32.078  1.00 13.27  ?  413  GLY A HA3  1 
ATOM   3156  N  N    . ALA A 1 191 ? 34.100  -0.104  32.642  1.00 11.97  ?  414  ALA A N    1 
ATOM   3157  C  CA   . ALA A 1 191 ? 34.578  -1.398  33.082  1.00 12.62  ?  414  ALA A CA   1 
ATOM   3158  C  C    . ALA A 1 191 ? 34.435  -1.528  34.588  1.00 11.66  ?  414  ALA A C    1 
ATOM   3159  O  O    . ALA A 1 191 ? 34.635  -0.575  35.351  1.00 13.51  ?  414  ALA A O    1 
ATOM   3160  C  CB   . ALA A 1 191 ? 36.039  -1.599  32.674  1.00 15.12  ?  414  ALA A CB   1 
ATOM   3161  H  H    . ALA A 1 191 ? 34.709  0.395   32.298  1.00 14.36  ?  414  ALA A H    1 
ATOM   3162  H  HA   . ALA A 1 191 ? 34.051  -2.094  32.658  1.00 15.15  ?  414  ALA A HA   1 
ATOM   3163  H  HB1  . ALA A 1 191 ? 36.332  -2.475  32.970  1.00 18.15  ?  414  ALA A HB1  1 
ATOM   3164  H  HB2  . ALA A 1 191 ? 36.109  -1.535  31.709  1.00 18.15  ?  414  ALA A HB2  1 
ATOM   3165  H  HB3  . ALA A 1 191 ? 36.580  -0.910  33.091  1.00 18.15  ?  414  ALA A HB3  1 
ATOM   3166  N  N    . LEU A 1 192 ? 34.032  -2.714  34.994  1.00 9.93   ?  415  LEU A N    1 
ATOM   3167  C  CA   . LEU A 1 192 ? 33.946  -3.190  36.366  1.00 8.43   ?  415  LEU A CA   1 
ATOM   3168  C  C    . LEU A 1 192 ? 32.867  -2.517  37.195  1.00 7.64   ?  415  LEU A C    1 
ATOM   3169  O  O    . LEU A 1 192 ? 32.785  -2.775  38.396  1.00 9.36   ?  415  LEU A O    1 
ATOM   3170  C  CB   . LEU A 1 192 ? 35.292  -3.136  37.089  1.00 10.24  ?  415  LEU A CB   1 
ATOM   3171  C  CG   . LEU A 1 192 ? 36.345  -4.058  36.493  1.00 14.41  ?  415  LEU A CG   1 
ATOM   3172  C  CD1  . LEU A 1 192 ? 37.679  -3.809  37.163  1.00 15.11  ?  415  LEU A CD1  1 
ATOM   3173  C  CD2  . LEU A 1 192 ? 35.904  -5.506  36.673  1.00 17.72  ?  415  LEU A CD2  1 
ATOM   3174  H  H    . LEU A 1 192 ? 33.778  -3.321  34.441  1.00 11.92  ?  415  LEU A H    1 
ATOM   3175  H  HA   . LEU A 1 192 ? 33.687  -4.124  36.318  1.00 10.12  ?  415  LEU A HA   1 
ATOM   3176  H  HB2  . LEU A 1 192 ? 35.633  -2.228  37.043  1.00 12.28  ?  415  LEU A HB2  1 
ATOM   3177  H  HB3  . LEU A 1 192 ? 35.160  -3.395  38.014  1.00 12.28  ?  415  LEU A HB3  1 
ATOM   3178  H  HG   . LEU A 1 192 ? 36.450  -3.886  35.544  1.00 17.30  ?  415  LEU A HG   1 
ATOM   3179  H  HD11 . LEU A 1 192 ? 38.338  -4.414  36.788  1.00 18.14  ?  415  LEU A HD11 1 
ATOM   3180  H  HD12 . LEU A 1 192 ? 37.946  -2.890  37.004  1.00 18.14  ?  415  LEU A HD12 1 
ATOM   3181  H  HD13 . LEU A 1 192 ? 37.588  -3.968  38.116  1.00 18.14  ?  415  LEU A HD13 1 
ATOM   3182  H  HD21 . LEU A 1 192 ? 36.666  -6.088  36.527  1.00 21.27  ?  415  LEU A HD21 1 
ATOM   3183  H  HD22 . LEU A 1 192 ? 35.566  -5.623  37.574  1.00 21.27  ?  415  LEU A HD22 1 
ATOM   3184  H  HD23 . LEU A 1 192 ? 35.206  -5.706  36.029  1.00 21.27  ?  415  LEU A HD23 1 
ATOM   3185  N  N    . THR A 1 193 ? 31.996  -1.717  36.592  1.00 7.83   ?  416  THR A N    1 
ATOM   3186  C  CA   . THR A 1 193 ? 30.944  -1.015  37.317  1.00 8.57   ?  416  THR A CA   1 
ATOM   3187  C  C    . THR A 1 193 ? 29.596  -1.461  36.782  1.00 8.25   ?  416  THR A C    1 
ATOM   3188  O  O    . THR A 1 193 ? 29.411  -1.558  35.567  1.00 8.34   ?  416  THR A O    1 
ATOM   3189  C  CB   . THR A 1 193 ? 31.126  0.501   37.181  1.00 10.73  ?  416  THR A CB   1 
ATOM   3190  O  OG1  . THR A 1 193 ? 32.420  0.839   37.690  1.00 13.30  ?  416  THR A OG1  1 
ATOM   3191  C  CG2  . THR A 1 193 ? 30.079  1.257   37.973  1.00 11.53  ?  416  THR A CG2  1 
ATOM   3192  H  H    . THR A 1 193 ? 31.994  -1.561  35.746  1.00 9.40   ?  416  THR A H    1 
ATOM   3193  H  HA   . THR A 1 193 ? 30.972  -1.237  38.261  1.00 10.28  ?  416  THR A HA   1 
ATOM   3194  H  HB   . THR A 1 193 ? 31.035  0.760   36.250  1.00 12.88  ?  416  THR A HB   1 
ATOM   3195  H  HG1  . THR A 1 193 ? 32.542  1.668   37.638  1.00 15.97  ?  416  THR A HG1  1 
ATOM   3196  H  HG21 . THR A 1 193 ? 30.289  2.204   37.982  1.00 13.83  ?  416  THR A HG21 1 
ATOM   3197  H  HG22 . THR A 1 193 ? 29.205  1.132   37.572  1.00 13.83  ?  416  THR A HG22 1 
ATOM   3198  H  HG23 . THR A 1 193 ? 30.055  0.931   38.887  1.00 13.83  ?  416  THR A HG23 1 
ATOM   3199  N  N    . LEU A 1 194 ? 28.682  -1.786  37.689  1.00 7.91   ?  417  LEU A N    1 
ATOM   3200  C  CA   . LEU A 1 194 ? 27.364  -2.254  37.283  1.00 7.74   ?  417  LEU A CA   1 
ATOM   3201  C  C    . LEU A 1 194 ? 26.475  -1.090  36.839  1.00 7.26   ?  417  LEU A C    1 
ATOM   3202  O  O    . LEU A 1 194 ? 26.672  0.068   37.209  1.00 8.51   ?  417  LEU A O    1 
ATOM   3203  C  CB   . LEU A 1 194 ? 26.696  -2.979  38.451  1.00 7.25   ?  417  LEU A CB   1 
ATOM   3204  C  CG   . LEU A 1 194 ? 27.437  -4.224  38.950  1.00 8.14   ?  417  LEU A CG   1 
ATOM   3205  C  CD1  . LEU A 1 194 ? 26.670  -4.866  40.098  1.00 8.93   ?  417  LEU A CD1  1 
ATOM   3206  C  CD2  . LEU A 1 194 ? 27.666  -5.219  37.818  1.00 9.14   ?  417  LEU A CD2  1 
ATOM   3207  H  H    . LEU A 1 194 ? 28.800  -1.744  38.540  1.00 9.49   ?  417  LEU A H    1 
ATOM   3208  H  HA   . LEU A 1 194 ? 27.458  -2.863  36.533  1.00 9.29   ?  417  LEU A HA   1 
ATOM   3209  H  HB2  . LEU A 1 194 ? 26.630  -2.361  39.196  1.00 8.70   ?  417  LEU A HB2  1 
ATOM   3210  H  HB3  . LEU A 1 194 ? 25.810  -3.258  38.172  1.00 8.70   ?  417  LEU A HB3  1 
ATOM   3211  H  HG   . LEU A 1 194 ? 28.310  -3.962  39.280  1.00 9.77   ?  417  LEU A HG   1 
ATOM   3212  H  HD11 . LEU A 1 194 ? 27.151  -5.653  40.398  1.00 10.72  ?  417  LEU A HD11 1 
ATOM   3213  H  HD12 . LEU A 1 194 ? 26.595  -4.228  40.824  1.00 10.72  ?  417  LEU A HD12 1 
ATOM   3214  H  HD13 . LEU A 1 194 ? 25.787  -5.118  39.786  1.00 10.72  ?  417  LEU A HD13 1 
ATOM   3215  H  HD21 . LEU A 1 194 ? 27.999  -6.050  38.190  1.00 10.97  ?  417  LEU A HD21 1 
ATOM   3216  H  HD22 . LEU A 1 194 ? 26.826  -5.374  37.359  1.00 10.97  ?  417  LEU A HD22 1 
ATOM   3217  H  HD23 . LEU A 1 194 ? 28.316  -4.849  37.200  1.00 10.97  ?  417  LEU A HD23 1 
ATOM   3218  N  N    . ASN A 1 195 ? 25.476  -1.416  36.034  1.00 7.09   ?  418  ASN A N    1 
ATOM   3219  C  CA   . ASN A 1 195 ? 24.475  -0.439  35.646  1.00 6.83   ?  418  ASN A CA   1 
ATOM   3220  C  C    . ASN A 1 195 ? 23.483  -0.212  36.787  1.00 7.22   ?  418  ASN A C    1 
ATOM   3221  O  O    . ASN A 1 195 ? 23.306  -1.062  37.670  1.00 7.93   ?  418  ASN A O    1 
ATOM   3222  C  CB   . ASN A 1 195 ? 23.752  -0.916  34.393  1.00 6.86   ?  418  ASN A CB   1 
ATOM   3223  C  CG   . ASN A 1 195 ? 24.653  -0.931  33.178  1.00 7.10   ?  418  ASN A CG   1 
ATOM   3224  O  OD1  . ASN A 1 195 ? 25.608  -0.147  33.094  1.00 7.71   ?  418  ASN A OD1  1 
ATOM   3225  N  ND2  . ASN A 1 195 ? 24.323  -1.769  32.205  1.00 7.72   ?  418  ASN A ND2  1 
ATOM   3226  H  H    . ASN A 1 195 ? 25.355  -2.198  35.699  1.00 8.51   ?  418  ASN A H    1 
ATOM   3227  H  HA   . ASN A 1 195 ? 24.896  0.412   35.447  1.00 8.20   ?  418  ASN A HA   1 
ATOM   3228  H  HB2  . ASN A 1 195 ? 23.426  -1.818  34.538  1.00 8.23   ?  418  ASN A HB2  1 
ATOM   3229  H  HB3  . ASN A 1 195 ? 23.008  -0.320  34.210  1.00 8.23   ?  418  ASN A HB3  1 
ATOM   3230  H  HD21 . ASN A 1 195 ? 24.805  -1.814  31.494  1.00 9.27   ?  418  ASN A HD21 1 
ATOM   3231  H  HD22 . ASN A 1 195 ? 23.627  -2.268  32.285  1.00 9.27   ?  418  ASN A HD22 1 
ATOM   3232  N  N    . MET A 1 196 ? 22.810  0.940   36.740  1.00 7.99   ?  419  MET A N    1 
ATOM   3233  C  CA   A MET A 1 196 ? 21.866  1.349   37.773  0.75 8.49   ?  419  MET A CA   1 
ATOM   3234  C  CA   B MET A 1 196 ? 21.885  1.383   37.772  0.25 8.71   ?  419  MET A CA   1 
ATOM   3235  C  C    . MET A 1 196 ? 20.648  1.979   37.110  1.00 8.32   ?  419  MET A C    1 
ATOM   3236  O  O    . MET A 1 196 ? 20.651  2.302   35.916  1.00 9.01   ?  419  MET A O    1 
ATOM   3237  C  CB   A MET A 1 196 ? 22.504  2.356   38.752  0.75 10.38  ?  419  MET A CB   1 
ATOM   3238  C  CB   B MET A 1 196 ? 22.531  2.466   38.653  0.25 10.20  ?  419  MET A CB   1 
ATOM   3239  C  CG   A MET A 1 196 ? 23.755  1.855   39.438  0.75 13.14  ?  419  MET A CG   1 
ATOM   3240  C  CG   B MET A 1 196 ? 23.820  2.041   39.315  0.25 11.86  ?  419  MET A CG   1 
ATOM   3241  S  SD   A MET A 1 196 ? 24.509  3.074   40.526  0.75 16.42  ?  419  MET A SD   1 
ATOM   3242  S  SD   B MET A 1 196 ? 23.503  1.070   40.787  0.25 14.11  ?  419  MET A SD   1 
ATOM   3243  C  CE   A MET A 1 196 ? 23.224  3.341   41.742  0.75 17.23  ?  419  MET A CE   1 
ATOM   3244  C  CE   B MET A 1 196 ? 23.174  2.362   41.983  0.25 14.51  ?  419  MET A CE   1 
ATOM   3245  H  H    A MET A 1 196 ? 22.888  1.513   36.104  0.75 9.59   ?  419  MET A H    1 
ATOM   3246  H  H    B MET A 1 196 ? 22.879  1.502   36.092  0.25 9.59   ?  419  MET A H    1 
ATOM   3247  H  HA   A MET A 1 196 ? 21.591  0.563   38.272  0.75 10.20  ?  419  MET A HA   1 
ATOM   3248  H  HA   B MET A 1 196 ? 21.636  0.619   38.315  0.25 10.45  ?  419  MET A HA   1 
ATOM   3249  H  HB2  A MET A 1 196 ? 22.740  3.158   38.260  0.75 12.46  ?  419  MET A HB2  1 
ATOM   3250  H  HB2  B MET A 1 196 ? 22.725  3.239   38.100  0.25 12.24  ?  419  MET A HB2  1 
ATOM   3251  H  HB3  A MET A 1 196 ? 21.857  2.568   39.442  0.75 12.46  ?  419  MET A HB3  1 
ATOM   3252  H  HB3  B MET A 1 196 ? 21.906  2.707   39.354  0.25 12.24  ?  419  MET A HB3  1 
ATOM   3253  H  HG2  A MET A 1 196 ? 23.530  1.077   39.973  0.75 15.77  ?  419  MET A HG2  1 
ATOM   3254  H  HG2  B MET A 1 196 ? 24.337  1.501   38.697  0.25 14.24  ?  419  MET A HG2  1 
ATOM   3255  H  HG3  A MET A 1 196 ? 24.409  1.615   38.762  0.75 15.77  ?  419  MET A HG3  1 
ATOM   3256  H  HG3  B MET A 1 196 ? 24.326  2.829   39.570  0.25 14.24  ?  419  MET A HG3  1 
ATOM   3257  H  HE1  A MET A 1 196 ? 23.565  3.923   42.439  0.75 20.68  ?  419  MET A HE1  1 
ATOM   3258  H  HE1  B MET A 1 196 ? 23.486  2.072   42.854  0.25 17.42  ?  419  MET A HE1  1 
ATOM   3259  H  HE2  A MET A 1 196 ? 22.461  3.755   41.309  0.75 20.68  ?  419  MET A HE2  1 
ATOM   3260  H  HE2  B MET A 1 196 ? 23.642  3.167   41.715  0.25 17.42  ?  419  MET A HE2  1 
ATOM   3261  H  HE3  A MET A 1 196 ? 22.966  2.487   42.121  0.75 20.68  ?  419  MET A HE3  1 
ATOM   3262  H  HE3  B MET A 1 196 ? 22.218  2.528   42.012  0.25 17.42  ?  419  MET A HE3  1 
ATOM   3263  N  N    . GLY A 1 197 ? 19.600  2.156   37.912  1.00 8.03   ?  420  GLY A N    1 
ATOM   3264  C  CA   . GLY A 1 197 ? 18.409  2.847   37.455  1.00 8.55   ?  420  GLY A CA   1 
ATOM   3265  C  C    . GLY A 1 197 ? 17.655  2.150   36.346  1.00 8.02   ?  420  GLY A C    1 
ATOM   3266  O  O    . GLY A 1 197 ? 16.913  2.806   35.608  1.00 9.16   ?  420  GLY A O    1 
ATOM   3267  H  H    . GLY A 1 197 ? 19.557  1.884   38.727  1.00 9.64   ?  420  GLY A H    1 
ATOM   3268  H  HA2  . GLY A 1 197 ? 17.802  2.951   38.204  1.00 10.27  ?  420  GLY A HA2  1 
ATOM   3269  H  HA3  . GLY A 1 197 ? 18.664  3.726   37.131  1.00 10.27  ?  420  GLY A HA3  1 
ATOM   3270  N  N    . LEU A 1 198 ? 17.794  0.838   36.221  1.00 7.46   ?  421  LEU A N    1 
ATOM   3271  C  CA   . LEU A 1 198 ? 17.328  0.126   35.044  1.00 7.75   ?  421  LEU A CA   1 
ATOM   3272  C  C    . LEU A 1 198 ? 15.833  -0.156  35.075  1.00 7.56   ?  421  LEU A C    1 
ATOM   3273  O  O    . LEU A 1 198 ? 15.262  -0.527  36.106  1.00 8.84   ?  421  LEU A O    1 
ATOM   3274  C  CB   . LEU A 1 198 ? 18.033  -1.228  34.948  1.00 7.33   ?  421  LEU A CB   1 
ATOM   3275  C  CG   . LEU A 1 198 ? 19.538  -1.232  34.721  1.00 7.64   ?  421  LEU A CG   1 
ATOM   3276  C  CD1  . LEU A 1 198 ? 20.011  -2.658  34.592  1.00 8.83   ?  421  LEU A CD1  1 
ATOM   3277  C  CD2  . LEU A 1 198 ? 19.904  -0.449  33.486  1.00 7.94   ?  421  LEU A CD2  1 
ATOM   3278  H  H    . LEU A 1 198 ? 18.160  0.331   36.812  1.00 8.96   ?  421  LEU A H    1 
ATOM   3279  H  HA   . LEU A 1 198 ? 17.519  0.687   34.276  1.00 9.30   ?  421  LEU A HA   1 
ATOM   3280  H  HB2  . LEU A 1 198 ? 17.875  -1.702  35.779  1.00 8.80   ?  421  LEU A HB2  1 
ATOM   3281  H  HB3  . LEU A 1 198 ? 17.638  -1.714  34.208  1.00 8.80   ?  421  LEU A HB3  1 
ATOM   3282  H  HG   . LEU A 1 198 ? 19.980  -0.809  35.474  1.00 9.17   ?  421  LEU A HG   1 
ATOM   3283  H  HD11 . LEU A 1 198 ? 20.978  -2.665  34.518  1.00 10.60  ?  421  LEU A HD11 1 
ATOM   3284  H  HD12 . LEU A 1 198 ? 19.736  -3.154  35.380  1.00 10.60  ?  421  LEU A HD12 1 
ATOM   3285  H  HD13 . LEU A 1 198 ? 19.615  -3.052  33.799  1.00 10.60  ?  421  LEU A HD13 1 
ATOM   3286  H  HD21 . LEU A 1 198 ? 20.847  -0.578  33.298  1.00 9.53   ?  421  LEU A HD21 1 
ATOM   3287  H  HD22 . LEU A 1 198 ? 19.372  -0.768  32.741  1.00 9.53   ?  421  LEU A HD22 1 
ATOM   3288  H  HD23 . LEU A 1 198 ? 19.724  0.491   33.643  1.00 9.53   ?  421  LEU A HD23 1 
ATOM   3289  N  N    . ALA A 1 199 ? 15.219  -0.050  33.907  1.00 7.24   ?  422  ALA A N    1 
ATOM   3290  C  CA   . ALA A 1 199 ? 13.938  -0.690  33.694  1.00 8.11   ?  422  ALA A CA   1 
ATOM   3291  C  C    . ALA A 1 199 ? 14.130  -2.199  33.811  1.00 8.66   ?  422  ALA A C    1 
ATOM   3292  O  O    . ALA A 1 199 ? 15.151  -2.733  33.349  1.00 8.62   ?  422  ALA A O    1 
ATOM   3293  C  CB   . ALA A 1 199 ? 13.433  -0.347  32.296  1.00 8.29   ?  422  ALA A CB   1 
ATOM   3294  H  H    . ALA A 1 199 ? 15.522  0.383   33.229  1.00 8.69   ?  422  ALA A H    1 
ATOM   3295  H  HA   . ALA A 1 199 ? 13.285  -0.395  34.347  1.00 9.73   ?  422  ALA A HA   1 
ATOM   3296  H  HB1  . ALA A 1 199 ? 12.580  -0.786  32.151  1.00 9.95   ?  422  ALA A HB1  1 
ATOM   3297  H  HB2  . ALA A 1 199 ? 13.327  0.615   32.225  1.00 9.95   ?  422  ALA A HB2  1 
ATOM   3298  H  HB3  . ALA A 1 199 ? 14.079  -0.657  31.642  1.00 9.95   ?  422  ALA A HB3  1 
ATOM   3299  N  N    . PRO A 1 200 ? 13.189  -2.917  34.418  1.00 10.63  ?  423  PRO A N    1 
ATOM   3300  C  CA   . PRO A 1 200 ? 13.405  -4.343  34.665  1.00 11.02  ?  423  PRO A CA   1 
ATOM   3301  C  C    . PRO A 1 200 ? 13.332  -5.163  33.392  1.00 10.62  ?  423  PRO A C    1 
ATOM   3302  O  O    . PRO A 1 200 ? 12.763  -4.760  32.371  1.00 11.29  ?  423  PRO A O    1 
ATOM   3303  C  CB   . PRO A 1 200 ? 12.255  -4.724  35.608  1.00 13.33  ?  423  PRO A CB   1 
ATOM   3304  C  CG   . PRO A 1 200 ? 11.175  -3.782  35.252  1.00 14.10  ?  423  PRO A CG   1 
ATOM   3305  C  CD   . PRO A 1 200 ? 11.885  -2.467  34.939  1.00 12.94  ?  423  PRO A CD   1 
ATOM   3306  H  HA   . PRO A 1 200 ? 14.262  -4.480  35.099  1.00 13.22  ?  423  PRO A HA   1 
ATOM   3307  H  HB2  . PRO A 1 200 ? 11.985  -5.643  35.451  1.00 16.00  ?  423  PRO A HB2  1 
ATOM   3308  H  HB3  . PRO A 1 200 ? 12.528  -4.612  36.532  1.00 16.00  ?  423  PRO A HB3  1 
ATOM   3309  H  HG2  . PRO A 1 200 ? 10.693  -4.109  34.476  1.00 16.92  ?  423  PRO A HG2  1 
ATOM   3310  H  HG3  . PRO A 1 200 ? 10.566  -3.678  36.000  1.00 16.92  ?  423  PRO A HG3  1 
ATOM   3311  H  HD2  . PRO A 1 200 ? 11.399  -1.962  34.268  1.00 15.53  ?  423  PRO A HD2  1 
ATOM   3312  H  HD3  . PRO A 1 200 ? 11.997  -1.934  35.741  1.00 15.53  ?  423  PRO A HD3  1 
ATOM   3313  N  N    . SER A 1 201 ? 13.893  -6.363  33.473  1.00 10.96  ?  424  SER A N    1 
ATOM   3314  C  CA   A SER A 1 201 ? 13.725  -7.302  32.376  0.82 11.43  ?  424  SER A CA   1 
ATOM   3315  C  CA   B SER A 1 201 ? 13.726  -7.307  32.383  0.18 11.29  ?  424  SER A CA   1 
ATOM   3316  C  C    . SER A 1 201 ? 12.268  -7.752  32.316  1.00 11.63  ?  424  SER A C    1 
ATOM   3317  O  O    . SER A 1 201 ? 11.528  -7.692  33.306  1.00 13.51  ?  424  SER A O    1 
ATOM   3318  C  CB   A SER A 1 201 ? 14.657  -8.500  32.535  0.82 13.06  ?  424  SER A CB   1 
ATOM   3319  C  CB   B SER A 1 201 ? 14.648  -8.507  32.579  0.18 11.59  ?  424  SER A CB   1 
ATOM   3320  O  OG   A SER A 1 201 ? 14.288  -9.295  33.643  0.82 15.35  ?  424  SER A OG   1 
ATOM   3321  O  OG   B SER A 1 201 ? 15.992  -8.080  32.714  0.18 12.10  ?  424  SER A OG   1 
ATOM   3322  H  H    A SER A 1 201 ? 14.363  -6.648  34.135  0.82 13.15  ?  424  SER A H    1 
ATOM   3323  H  H    B SER A 1 201 ? 14.364  -6.646  34.135  0.18 13.15  ?  424  SER A H    1 
ATOM   3324  H  HA   A SER A 1 201 ? 13.956  -6.879  31.534  0.82 13.72  ?  424  SER A HA   1 
ATOM   3325  H  HA   B SER A 1 201 ? 13.961  -6.896  31.536  0.18 13.55  ?  424  SER A HA   1 
ATOM   3326  H  HB2  A SER A 1 201 ? 14.611  -9.041  31.731  0.82 15.67  ?  424  SER A HB2  1 
ATOM   3327  H  HB2  B SER A 1 201 ? 14.383  -8.982  33.382  0.18 13.91  ?  424  SER A HB2  1 
ATOM   3328  H  HB3  A SER A 1 201 ? 15.562  -8.178  32.667  0.82 15.67  ?  424  SER A HB3  1 
ATOM   3329  H  HB3  B SER A 1 201 ? 14.576  -9.092  31.809  0.18 13.91  ?  424  SER A HB3  1 
ATOM   3330  H  HG   A SER A 1 201 ? 14.809  -9.950  33.713  0.82 18.42  ?  424  SER A HG   1 
ATOM   3331  H  HG   B SER A 1 201 ? 16.493  -8.743  32.835  0.18 14.52  ?  424  SER A HG   1 
ATOM   3332  N  N    . VAL A 1 202 ? 11.851  -8.182  31.129  1.00 10.35  ?  425  VAL A N    1 
ATOM   3333  C  CA   . VAL A 1 202 ? 10.474  -8.606  30.894  1.00 10.09  ?  425  VAL A CA   1 
ATOM   3334  C  C    . VAL A 1 202 ? 10.494  -9.997  30.283  1.00 9.67   ?  425  VAL A C    1 
ATOM   3335  O  O    . VAL A 1 202 ? 11.408  -10.350 29.537  1.00 9.75   ?  425  VAL A O    1 
ATOM   3336  C  CB   . VAL A 1 202 ? 9.688   -7.625  29.984  1.00 11.39  ?  425  VAL A CB   1 
ATOM   3337  C  CG1  . VAL A 1 202 ? 9.561   -6.277  30.668  1.00 13.17  ?  425  VAL A CG1  1 
ATOM   3338  C  CG2  . VAL A 1 202 ? 10.341  -7.483  28.611  1.00 11.31  ?  425  VAL A CG2  1 
ATOM   3339  H  H    . VAL A 1 202 ? 12.354  -8.239  30.434  1.00 12.42  ?  425  VAL A H    1 
ATOM   3340  H  HA   . VAL A 1 202 ? 10.014  -8.646  31.747  1.00 12.12  ?  425  VAL A HA   1 
ATOM   3341  H  HB   . VAL A 1 202 ? 8.799   -7.984  29.836  1.00 13.67  ?  425  VAL A HB   1 
ATOM   3342  H  HG11 . VAL A 1 202 ? 9.051   -5.680  30.099  1.00 15.80  ?  425  VAL A HG11 1 
ATOM   3343  H  HG12 . VAL A 1 202 ? 9.105   -6.395  31.516  1.00 15.80  ?  425  VAL A HG12 1 
ATOM   3344  H  HG13 . VAL A 1 202 ? 10.448  -5.914  30.818  1.00 15.80  ?  425  VAL A HG13 1 
ATOM   3345  H  HG21 . VAL A 1 202 ? 9.863   -6.810  28.102  1.00 13.58  ?  425  VAL A HG21 1 
ATOM   3346  H  HG22 . VAL A 1 202 ? 11.266  -7.216  28.727  1.00 13.58  ?  425  VAL A HG22 1 
ATOM   3347  H  HG23 . VAL A 1 202 ? 10.299  -8.337  28.152  1.00 13.58  ?  425  VAL A HG23 1 
ATOM   3348  N  N    . PHE A 1 203 ? 9.484   -10.796 30.611  1.00 10.37  ?  426  PHE A N    1 
ATOM   3349  C  CA   . PHE A 1 203 ? 9.400   -12.128 30.033  1.00 11.20  ?  426  PHE A CA   1 
ATOM   3350  C  C    . PHE A 1 203 ? 7.976   -12.636 30.169  1.00 10.72  ?  426  PHE A C    1 
ATOM   3351  O  O    . PHE A 1 203 ? 7.217   -12.165 31.025  1.00 11.89  ?  426  PHE A O    1 
ATOM   3352  C  CB   . PHE A 1 203 ? 10.398  -13.093 30.694  1.00 14.14  ?  426  PHE A CB   1 
ATOM   3353  C  CG   . PHE A 1 203 ? 10.361  -13.068 32.178  1.00 18.87  ?  426  PHE A CG   1 
ATOM   3354  C  CD1  . PHE A 1 203 ? 11.046  -12.095 32.891  1.00 21.09  ?  426  PHE A CD1  1 
ATOM   3355  C  CD2  . PHE A 1 203 ? 9.642   -14.023 32.872  1.00 21.14  ?  426  PHE A CD2  1 
ATOM   3356  C  CE1  . PHE A 1 203 ? 11.010  -12.078 34.274  1.00 22.89  ?  426  PHE A CE1  1 
ATOM   3357  C  CE2  . PHE A 1 203 ? 9.614   -14.015 34.252  1.00 22.91  ?  426  PHE A CE2  1 
ATOM   3358  C  CZ   . PHE A 1 203 ? 10.296  -13.036 34.950  1.00 23.34  ?  426  PHE A CZ   1 
ATOM   3359  H  H    . PHE A 1 203 ? 8.849   -10.592 31.154  1.00 12.44  ?  426  PHE A H    1 
ATOM   3360  H  HA   . PHE A 1 203 ? 9.608   -12.081 29.087  1.00 13.44  ?  426  PHE A HA   1 
ATOM   3361  H  HB2  . PHE A 1 203 ? 10.193  -13.997 30.407  1.00 16.97  ?  426  PHE A HB2  1 
ATOM   3362  H  HB3  . PHE A 1 203 ? 11.295  -12.852 30.416  1.00 16.97  ?  426  PHE A HB3  1 
ATOM   3363  H  HD1  . PHE A 1 203 ? 11.534  -11.448 32.435  1.00 25.31  ?  426  PHE A HD1  1 
ATOM   3364  H  HD2  . PHE A 1 203 ? 9.172   -14.676 32.406  1.00 25.37  ?  426  PHE A HD2  1 
ATOM   3365  H  HE1  . PHE A 1 203 ? 11.469  -11.419 34.744  1.00 27.47  ?  426  PHE A HE1  1 
ATOM   3366  H  HE2  . PHE A 1 203 ? 9.137   -14.667 34.712  1.00 27.49  ?  426  PHE A HE2  1 
ATOM   3367  H  HZ   . PHE A 1 203 ? 10.271  -13.027 35.880  1.00 28.01  ?  426  PHE A HZ   1 
ATOM   3368  N  N    . PRO A 1 204 ? 7.576   -13.591 29.329  1.00 10.95  ?  427  PRO A N    1 
ATOM   3369  C  CA   . PRO A 1 204 ? 6.244   -14.188 29.485  1.00 12.49  ?  427  PRO A CA   1 
ATOM   3370  C  C    . PRO A 1 204 ? 6.247   -15.110 30.692  1.00 13.70  ?  427  PRO A C    1 
ATOM   3371  O  O    . PRO A 1 204 ? 7.167   -15.910 30.883  1.00 17.38  ?  427  PRO A O    1 
ATOM   3372  C  CB   . PRO A 1 204 ? 6.037   -14.975 28.188  1.00 13.48  ?  427  PRO A CB   1 
ATOM   3373  C  CG   . PRO A 1 204 ? 7.176   -14.644 27.318  1.00 13.74  ?  427  PRO A CG   1 
ATOM   3374  C  CD   . PRO A 1 204 ? 8.295   -14.158 28.179  1.00 11.99  ?  427  PRO A CD   1 
ATOM   3375  H  HA   . PRO A 1 204 ? 5.556   -13.510 29.562  1.00 14.99  ?  427  PRO A HA   1 
ATOM   3376  H  HB2  . PRO A 1 204 ? 6.021   -15.925 28.383  1.00 16.18  ?  427  PRO A HB2  1 
ATOM   3377  H  HB3  . PRO A 1 204 ? 5.202   -14.707 27.775  1.00 16.18  ?  427  PRO A HB3  1 
ATOM   3378  H  HG2  . PRO A 1 204 ? 7.447   -15.439 26.833  1.00 16.49  ?  427  PRO A HG2  1 
ATOM   3379  H  HG3  . PRO A 1 204 ? 6.908   -13.950 26.695  1.00 16.49  ?  427  PRO A HG3  1 
ATOM   3380  H  HD2  . PRO A 1 204 ? 8.870   -14.890 28.452  1.00 14.39  ?  427  PRO A HD2  1 
ATOM   3381  H  HD3  . PRO A 1 204 ? 8.817   -13.479 27.724  1.00 14.39  ?  427  PRO A HD3  1 
ATOM   3382  N  N    . THR A 1 205 ? 5.217   -14.988 31.511  1.00 12.46  ?  428  THR A N    1 
ATOM   3383  C  CA   . THR A 1 205 ? 5.007   -15.920 32.603  1.00 12.93  ?  428  THR A CA   1 
ATOM   3384  C  C    . THR A 1 205 ? 4.008   -17.012 32.267  1.00 12.71  ?  428  THR A C    1 
ATOM   3385  O  O    . THR A 1 205 ? 4.092   -18.103 32.825  1.00 15.03  ?  428  THR A O    1 
ATOM   3386  C  CB   . THR A 1 205 ? 4.547   -15.157 33.848  1.00 15.29  ?  428  THR A CB   1 
ATOM   3387  O  OG1  . THR A 1 205 ? 3.378   -14.390 33.550  1.00 16.19  ?  428  THR A OG1  1 
ATOM   3388  C  CG2  . THR A 1 205 ? 5.631   -14.201 34.314  1.00 17.13  ?  428  THR A CG2  1 
ATOM   3389  H  H    . THR A 1 205 ? 4.622   -14.370 31.454  1.00 14.96  ?  428  THR A H    1 
ATOM   3390  H  HA   . THR A 1 205 ? 5.845   -16.359 32.821  1.00 15.51  ?  428  THR A HA   1 
ATOM   3391  H  HB   . THR A 1 205 ? 4.354   -15.795 34.553  1.00 18.35  ?  428  THR A HB   1 
ATOM   3392  H  HG1  . THR A 1 205 ? 3.125   -13.973 34.234  1.00 19.43  ?  428  THR A HG1  1 
ATOM   3393  H  HG21 . THR A 1 205 ? 5.352   -13.755 35.129  1.00 20.56  ?  428  THR A HG21 1 
ATOM   3394  H  HG22 . THR A 1 205 ? 6.451   -14.688 34.487  1.00 20.56  ?  428  THR A HG22 1 
ATOM   3395  H  HG23 . THR A 1 205 ? 5.799   -13.533 33.631  1.00 20.56  ?  428  THR A HG23 1 
ATOM   3396  N  N    . TYR A 1 206 ? 3.096   -16.768 31.375  1.00 11.44  ?  429  TYR A N    1 
ATOM   3397  C  CA   . TYR A 1 206 ? 2.037   -17.737 31.129  1.00 12.31  ?  429  TYR A CA   1 
ATOM   3398  C  C    . TYR A 1 206 ? 2.523   -18.779 30.127  1.00 12.16  ?  429  TYR A C    1 
ATOM   3399  O  O    . TYR A 1 206 ? 3.090   -18.419 29.096  1.00 11.04  ?  429  TYR A O    1 
ATOM   3400  C  CB   . TYR A 1 206 ? 0.818   -17.010 30.562  1.00 13.94  ?  429  TYR A CB   1 
ATOM   3401  C  CG   . TYR A 1 206 ? -0.444  -17.838 30.580  1.00 16.89  ?  429  TYR A CG   1 
ATOM   3402  C  CD1  . TYR A 1 206 ? -1.233  -17.902 31.718  1.00 20.27  ?  429  TYR A CD1  1 
ATOM   3403  C  CD2  . TYR A 1 206 ? -0.831  -18.572 29.476  1.00 18.32  ?  429  TYR A CD2  1 
ATOM   3404  C  CE1  . TYR A 1 206 ? -2.381  -18.668 31.752  1.00 21.84  ?  429  TYR A CE1  1 
ATOM   3405  C  CE2  . TYR A 1 206 ? -1.981  -19.343 29.504  1.00 20.17  ?  429  TYR A CE2  1 
ATOM   3406  C  CZ   . TYR A 1 206 ? -2.748  -19.380 30.641  1.00 21.53  ?  429  TYR A CZ   1 
ATOM   3407  O  OH   . TYR A 1 206 ? -3.891  -20.137 30.663  1.00 22.45  ?  429  TYR A OH   1 
ATOM   3408  H  H    . TYR A 1 206 ? 3.055   -16.056 30.894  1.00 13.73  ?  429  TYR A H    1 
ATOM   3409  H  HA   . TYR A 1 206 ? 1.789   -18.190 31.950  1.00 14.77  ?  429  TYR A HA   1 
ATOM   3410  H  HB2  . TYR A 1 206 ? 0.657   -16.212 31.090  1.00 16.73  ?  429  TYR A HB2  1 
ATOM   3411  H  HB3  . TYR A 1 206 ? 1.000   -16.767 29.641  1.00 16.73  ?  429  TYR A HB3  1 
ATOM   3412  H  HD1  . TYR A 1 206 ? -0.984  -17.419 32.473  1.00 24.33  ?  429  TYR A HD1  1 
ATOM   3413  H  HD2  . TYR A 1 206 ? -0.313  -18.548 28.704  1.00 21.98  ?  429  TYR A HD2  1 
ATOM   3414  H  HE1  . TYR A 1 206 ? -2.901  -18.701 32.523  1.00 26.22  ?  429  TYR A HE1  1 
ATOM   3415  H  HE2  . TYR A 1 206 ? -2.233  -19.834 28.755  1.00 24.21  ?  429  TYR A HE2  1 
ATOM   3416  H  HH   . TYR A 1 206 ? -3.890  -20.677 30.020  1.00 26.94  ?  429  TYR A HH   1 
ATOM   3417  N  N    . PRO A 1 207 ? 2.315   -20.073 30.390  1.00 12.36  ?  430  PRO A N    1 
ATOM   3418  C  CA   A PRO A 1 207 ? 2.785   -21.092 29.440  0.86 14.21  ?  430  PRO A CA   1 
ATOM   3419  C  CA   B PRO A 1 207 ? 2.793   -21.088 29.439  0.14 13.48  ?  430  PRO A CA   1 
ATOM   3420  C  C    . PRO A 1 207 ? 2.224   -20.866 28.044  1.00 14.33  ?  430  PRO A C    1 
ATOM   3421  O  O    . PRO A 1 207 ? 1.050   -20.538 27.876  1.00 15.73  ?  430  PRO A O    1 
ATOM   3422  C  CB   A PRO A 1 207 ? 2.264   -22.403 30.040  0.86 15.36  ?  430  PRO A CB   1 
ATOM   3423  C  CB   B PRO A 1 207 ? 2.297   -22.406 30.046  0.14 13.66  ?  430  PRO A CB   1 
ATOM   3424  C  CG   A PRO A 1 207 ? 2.126   -22.128 31.515  0.86 14.60  ?  430  PRO A CG   1 
ATOM   3425  C  CG   B PRO A 1 207 ? 1.150   -22.017 30.919  0.14 13.41  ?  430  PRO A CG   1 
ATOM   3426  C  CD   A PRO A 1 207 ? 1.741   -20.669 31.613  0.86 13.38  ?  430  PRO A CD   1 
ATOM   3427  C  CD   B PRO A 1 207 ? 1.512   -20.670 31.471  0.14 12.91  ?  430  PRO A CD   1 
ATOM   3428  H  HA   A PRO A 1 207 ? 3.755   -21.101 29.405  0.86 17.06  ?  430  PRO A HA   1 
ATOM   3429  H  HA   B PRO A 1 207 ? 3.762   -21.086 29.399  0.14 16.18  ?  430  PRO A HA   1 
ATOM   3430  H  HB2  A PRO A 1 207 ? 1.407   -22.628 29.647  0.86 18.44  ?  430  PRO A HB2  1 
ATOM   3431  H  HB2  B PRO A 1 207 ? 2.009   -23.007 29.341  0.14 16.40  ?  430  PRO A HB2  1 
ATOM   3432  H  HB3  A PRO A 1 207 ? 2.901   -23.117 29.878  0.86 18.44  ?  430  PRO A HB3  1 
ATOM   3433  H  HB3  B PRO A 1 207 ? 3.005   -22.819 30.565  0.14 16.40  ?  430  PRO A HB3  1 
ATOM   3434  H  HG2  A PRO A 1 207 ? 1.435   -22.694 31.892  0.86 17.52  ?  430  PRO A HG2  1 
ATOM   3435  H  HG2  B PRO A 1 207 ? 0.337   -21.968 30.392  0.14 16.10  ?  430  PRO A HG2  1 
ATOM   3436  H  HG3  A PRO A 1 207 ? 2.971   -22.294 31.962  0.86 17.52  ?  430  PRO A HG3  1 
ATOM   3437  H  HG3  B PRO A 1 207 ? 1.044   -22.666 31.632  0.14 16.10  ?  430  PRO A HG3  1 
ATOM   3438  H  HD2  A PRO A 1 207 ? 0.777   -20.568 31.625  0.86 16.06  ?  430  PRO A HD2  1 
ATOM   3439  H  HD2  B PRO A 1 207 ? 0.717   -20.142 31.644  0.14 15.49  ?  430  PRO A HD2  1 
ATOM   3440  H  HD3  A PRO A 1 207 ? 2.127   -20.264 32.406  0.86 16.06  ?  430  PRO A HD3  1 
ATOM   3441  H  HD3  B PRO A 1 207 ? 2.035   -20.758 32.283  0.14 15.49  ?  430  PRO A HD3  1 
ATOM   3442  N  N    . GLY A 1 208 ? 3.078   -21.033 27.041  1.00 13.92  ?  431  GLY A N    1 
ATOM   3443  C  CA   . GLY A 1 208 ? 2.663   -20.896 25.657  1.00 13.08  ?  431  GLY A CA   1 
ATOM   3444  C  C    . GLY A 1 208 ? 2.708   -19.487 25.100  1.00 11.85  ?  431  GLY A C    1 
ATOM   3445  O  O    . GLY A 1 208 ? 2.367   -19.286 23.924  1.00 13.22  ?  431  GLY A O    1 
ATOM   3446  H  H    . GLY A 1 208 ? 3.910   -21.227 27.140  1.00 16.71  ?  431  GLY A H    1 
ATOM   3447  H  HA2  . GLY A 1 208 ? 3.240   -21.448 25.106  1.00 15.70  ?  431  GLY A HA2  1 
ATOM   3448  H  HA3  . GLY A 1 208 ? 1.751   -21.215 25.576  1.00 15.70  ?  431  GLY A HA3  1 
ATOM   3449  N  N    . GLU A 1 209 ? 3.145   -18.510 25.881  1.00 9.61   ?  432  GLU A N    1 
ATOM   3450  C  CA   . GLU A 1 209 ? 3.210   -17.138 25.411  1.00 8.35   ?  432  GLU A CA   1 
ATOM   3451  C  C    . GLU A 1 209 ? 4.628   -16.721 25.059  1.00 7.67   ?  432  GLU A C    1 
ATOM   3452  O  O    . GLU A 1 209 ? 5.614   -17.211 25.616  1.00 8.84   ?  432  GLU A O    1 
ATOM   3453  C  CB   . GLU A 1 209 ? 2.617   -16.174 26.440  1.00 7.75   ?  432  GLU A CB   1 
ATOM   3454  C  CG   . GLU A 1 209 ? 1.116   -16.304 26.550  1.00 8.63   ?  432  GLU A CG   1 
ATOM   3455  C  CD   . GLU A 1 209 ? 0.451   -15.288 27.437  1.00 9.30   ?  432  GLU A CD   1 
ATOM   3456  O  OE1  . GLU A 1 209 ? 1.116   -14.320 27.859  1.00 9.64   ?  432  GLU A OE1  1 
ATOM   3457  O  OE2  . GLU A 1 209 ? -0.760  -15.457 27.707  1.00 10.09  -1 432  GLU A OE2  1 
ATOM   3458  H  H    . GLU A 1 209 ? 3.411   -18.619 26.692  1.00 11.53  ?  432  GLU A H    1 
ATOM   3459  H  HA   . GLU A 1 209 ? 2.689   -17.074 24.595  1.00 10.02  ?  432  GLU A HA   1 
ATOM   3460  H  HB2  . GLU A 1 209 ? 3.001   -16.364 27.310  1.00 9.30   ?  432  GLU A HB2  1 
ATOM   3461  H  HB3  . GLU A 1 209 ? 2.823   -15.264 26.177  1.00 9.30   ?  432  GLU A HB3  1 
ATOM   3462  H  HG2  . GLU A 1 209 ? 0.733   -16.209 25.664  1.00 10.36  ?  432  GLU A HG2  1 
ATOM   3463  H  HG3  . GLU A 1 209 ? 0.909   -17.181 26.909  1.00 10.36  ?  432  GLU A HG3  1 
ATOM   3464  N  N    . GLN A 1 210 ? 4.702   -15.778 24.121  1.00 7.30   ?  433  GLN A N    1 
ATOM   3465  C  CA   . GLN A 1 210 ? 5.932   -15.119 23.703  1.00 6.73   ?  433  GLN A CA   1 
ATOM   3466  C  C    . GLN A 1 210 ? 5.709   -13.615 23.744  1.00 7.18   ?  433  GLN A C    1 
ATOM   3467  O  O    . GLN A 1 210 ? 4.573   -13.139 23.695  1.00 7.56   ?  433  GLN A O    1 
ATOM   3468  C  CB   . GLN A 1 210 ? 6.326   -15.521 22.274  1.00 7.79   ?  433  GLN A CB   1 
ATOM   3469  C  CG   . GLN A 1 210 ? 6.768   -16.977 22.185  1.00 9.29   ?  433  GLN A CG   1 
ATOM   3470  C  CD   . GLN A 1 210 ? 7.131   -17.474 20.787  1.00 10.00  ?  433  GLN A CD   1 
ATOM   3471  O  OE1  . GLN A 1 210 ? 7.635   -18.585 20.651  1.00 11.21  ?  433  GLN A OE1  1 
ATOM   3472  N  NE2  . GLN A 1 210 ? 6.846   -16.700 19.759  1.00 9.99   ?  433  GLN A NE2  1 
ATOM   3473  H  H    . GLN A 1 210 ? 4.016   -15.490 23.691  1.00 8.76   ?  433  GLN A H    1 
ATOM   3474  H  HA   . GLN A 1 210 ? 6.653   -15.361 24.305  1.00 8.08   ?  433  GLN A HA   1 
ATOM   3475  H  HB2  . GLN A 1 210 ? 5.562   -15.400 21.688  1.00 9.35   ?  433  GLN A HB2  1 
ATOM   3476  H  HB3  . GLN A 1 210 ? 7.062   -14.962 21.978  1.00 9.35   ?  433  GLN A HB3  1 
ATOM   3477  H  HG2  . GLN A 1 210 ? 7.553   -17.092 22.744  1.00 11.15  ?  433  GLN A HG2  1 
ATOM   3478  H  HG3  . GLN A 1 210 ? 6.045   -17.536 22.510  1.00 11.15  ?  433  GLN A HG3  1 
ATOM   3479  H  HE21 . GLN A 1 210 ? 6.466   -15.939 19.886  1.00 11.99  ?  433  GLN A HE21 1 
ATOM   3480  H  HE22 . GLN A 1 210 ? 7.040   -16.956 18.961  1.00 11.99  ?  433  GLN A HE22 1 
ATOM   3481  N  N    . ILE A 1 211 ? 6.801   -12.860 23.833  1.00 6.51   ?  434  ILE A N    1 
ATOM   3482  C  CA   . ILE A 1 211 ? 6.717   -11.415 23.692  1.00 6.45   ?  434  ILE A CA   1 
ATOM   3483  C  C    . ILE A 1 211 ? 6.485   -11.067 22.229  1.00 6.45   ?  434  ILE A C    1 
ATOM   3484  O  O    . ILE A 1 211 ? 7.070   -11.683 21.331  1.00 7.00   ?  434  ILE A O    1 
ATOM   3485  C  CB   . ILE A 1 211 ? 8.000   -10.747 24.215  1.00 7.23   ?  434  ILE A CB   1 
ATOM   3486  C  CG1  . ILE A 1 211 ? 8.196   -11.037 25.704  1.00 8.63   ?  434  ILE A CG1  1 
ATOM   3487  C  CG2  . ILE A 1 211 ? 7.959   -9.229  23.940  1.00 7.74   ?  434  ILE A CG2  1 
ATOM   3488  C  CD1  . ILE A 1 211 ? 9.619   -10.738 26.150  1.00 10.70  ?  434  ILE A CD1  1 
ATOM   3489  H  H    . ILE A 1 211 ? 7.595   -13.160 23.972  1.00 7.81   ?  434  ILE A H    1 
ATOM   3490  H  HA   . ILE A 1 211 ? 5.969   -11.089 24.217  1.00 7.75   ?  434  ILE A HA   1 
ATOM   3491  H  HB   . ILE A 1 211 ? 8.759   -11.122 23.742  1.00 8.68   ?  434  ILE A HB   1 
ATOM   3492  H  HG12 . ILE A 1 211 ? 7.591   -10.483 26.221  1.00 10.36  ?  434  ILE A HG12 1 
ATOM   3493  H  HG13 . ILE A 1 211 ? 8.014   -11.975 25.873  1.00 10.36  ?  434  ILE A HG13 1 
ATOM   3494  H  HG21 . ILE A 1 211 ? 8.657   -8.795  24.455  1.00 9.29   ?  434  ILE A HG21 1 
ATOM   3495  H  HG22 . ILE A 1 211 ? 8.102   -9.076  22.993  1.00 9.29   ?  434  ILE A HG22 1 
ATOM   3496  H  HG23 . ILE A 1 211 ? 7.091   -8.884  24.203  1.00 9.29   ?  434  ILE A HG23 1 
ATOM   3497  H  HD11 . ILE A 1 211 ? 9.728   -11.024 27.070  1.00 12.84  ?  434  ILE A HD11 1 
ATOM   3498  H  HD12 . ILE A 1 211 ? 10.237  -11.219 25.578  1.00 12.84  ?  434  ILE A HD12 1 
ATOM   3499  H  HD13 . ILE A 1 211 ? 9.777   -9.783  26.079  1.00 12.84  ?  434  ILE A HD13 1 
ATOM   3500  N  N    . LEU A 1 212 ? 5.638   -10.064 21.985  1.00 6.04   ?  435  LEU A N    1 
ATOM   3501  C  CA   . LEU A 1 212 ? 5.444   -9.480  20.662  1.00 6.26   ?  435  LEU A CA   1 
ATOM   3502  C  C    . LEU A 1 212 ? 6.228   -8.176  20.597  1.00 6.13   ?  435  LEU A C    1 
ATOM   3503  O  O    . LEU A 1 212 ? 6.056   -7.305  21.451  1.00 7.50   ?  435  LEU A O    1 
ATOM   3504  C  CB   . LEU A 1 212 ? 3.964   -9.202  20.419  1.00 7.00   ?  435  LEU A CB   1 
ATOM   3505  C  CG   . LEU A 1 212 ? 3.603   -8.659  19.033  1.00 6.93   ?  435  LEU A CG   1 
ATOM   3506  C  CD1  . LEU A 1 212 ? 3.781   -9.705  17.964  1.00 8.36   ?  435  LEU A CD1  1 
ATOM   3507  C  CD2  . LEU A 1 212 ? 2.188   -8.121  19.036  1.00 8.53   ?  435  LEU A CD2  1 
ATOM   3508  H  H    . LEU A 1 212 ? 5.150   -9.697  22.590  1.00 7.25   ?  435  LEU A H    1 
ATOM   3509  H  HA   . LEU A 1 212 ? 5.764   -10.084 19.974  1.00 7.52   ?  435  LEU A HA   1 
ATOM   3510  H  HB2  . LEU A 1 212 ? 3.477   -10.033 20.538  1.00 8.41   ?  435  LEU A HB2  1 
ATOM   3511  H  HB3  . LEU A 1 212 ? 3.668   -8.548  21.071  1.00 8.41   ?  435  LEU A HB3  1 
ATOM   3512  H  HG   . LEU A 1 212 ? 4.207   -7.931  18.819  1.00 8.32   ?  435  LEU A HG   1 
ATOM   3513  H  HD11 . LEU A 1 212 ? 3.491   -9.339  17.113  1.00 10.03  ?  435  LEU A HD11 1 
ATOM   3514  H  HD12 . LEU A 1 212 ? 4.718   -9.952  17.916  1.00 10.03  ?  435  LEU A HD12 1 
ATOM   3515  H  HD13 . LEU A 1 212 ? 3.245   -10.481 18.189  1.00 10.03  ?  435  LEU A HD13 1 
ATOM   3516  H  HD21 . LEU A 1 212 ? 1.974   -7.790  18.150  1.00 10.23  ?  435  LEU A HD21 1 
ATOM   3517  H  HD22 . LEU A 1 212 ? 1.579   -8.837  19.278  1.00 10.23  ?  435  LEU A HD22 1 
ATOM   3518  H  HD23 . LEU A 1 212 ? 2.125   -7.401  19.683  1.00 10.23  ?  435  LEU A HD23 1 
ATOM   3519  N  N    . PHE A 1 213 ? 7.057   -8.045  19.566  1.00 5.50   ?  436  PHE A N    1 
ATOM   3520  C  CA   . PHE A 1 213 ? 7.942   -6.909  19.383  1.00 5.94   ?  436  PHE A CA   1 
ATOM   3521  C  C    . PHE A 1 213 ? 7.549   -6.126  18.135  1.00 5.84   ?  436  PHE A C    1 
ATOM   3522  O  O    . PHE A 1 213 ? 6.915   -6.649  17.219  1.00 6.05   ?  436  PHE A O    1 
ATOM   3523  C  CB   . PHE A 1 213 ? 9.398   -7.367  19.190  1.00 6.97   ?  436  PHE A CB   1 
ATOM   3524  C  CG   . PHE A 1 213 ? 9.982   -8.122  20.357  1.00 7.25   ?  436  PHE A CG   1 
ATOM   3525  C  CD1  . PHE A 1 213 ? 10.610  -7.469  21.402  1.00 7.96   ?  436  PHE A CD1  1 
ATOM   3526  C  CD2  . PHE A 1 213 ? 9.919   -9.508  20.392  1.00 8.31   ?  436  PHE A CD2  1 
ATOM   3527  C  CE1  . PHE A 1 213 ? 11.166  -8.201  22.461  1.00 9.38   ?  436  PHE A CE1  1 
ATOM   3528  C  CE2  . PHE A 1 213 ? 10.469  -10.224 21.432  1.00 9.97   ?  436  PHE A CE2  1 
ATOM   3529  C  CZ   . PHE A 1 213 ? 11.086  -9.566  22.462  1.00 10.23  ?  436  PHE A CZ   1 
ATOM   3530  H  H    . PHE A 1 213 ? 7.125   -8.627  18.936  1.00 6.61   ?  436  PHE A H    1 
ATOM   3531  H  HA   . PHE A 1 213 ? 7.869   -6.339  20.165  1.00 7.12   ?  436  PHE A HA   1 
ATOM   3532  H  HB2  . PHE A 1 213 ? 9.437   -7.951  18.416  1.00 8.36   ?  436  PHE A HB2  1 
ATOM   3533  H  HB3  . PHE A 1 213 ? 9.951   -6.584  19.043  1.00 8.36   ?  436  PHE A HB3  1 
ATOM   3534  H  HD1  . PHE A 1 213 ? 10.665  -6.540  21.402  1.00 9.56   ?  436  PHE A HD1  1 
ATOM   3535  H  HD2  . PHE A 1 213 ? 9.497   -9.963  19.699  1.00 9.98   ?  436  PHE A HD2  1 
ATOM   3536  H  HE1  . PHE A 1 213 ? 11.589  -7.758  23.161  1.00 11.25  ?  436  PHE A HE1  1 
ATOM   3537  H  HE2  . PHE A 1 213 ? 10.422  -11.153 21.435  1.00 11.96  ?  436  PHE A HE2  1 
ATOM   3538  H  HZ   . PHE A 1 213 ? 11.453  -10.050 23.166  1.00 12.28  ?  436  PHE A HZ   1 
ATOM   3539  N  N    . PHE A 1 214 ? 8.015   -4.884  18.094  1.00 5.45   ?  437  PHE A N    1 
ATOM   3540  C  CA   . PHE A 1 214 ? 7.935   -4.016  16.924  1.00 4.99   ?  437  PHE A CA   1 
ATOM   3541  C  C    . PHE A 1 214 ? 9.356   -3.879  16.387  1.00 5.25   ?  437  PHE A C    1 
ATOM   3542  O  O    . PHE A 1 214 ? 10.233  -3.351  17.077  1.00 5.97   ?  437  PHE A O    1 
ATOM   3543  C  CB   . PHE A 1 214 ? 7.333   -2.667  17.330  1.00 6.12   ?  437  PHE A CB   1 
ATOM   3544  C  CG   . PHE A 1 214 ? 5.942   -2.777  17.912  1.00 5.63   ?  437  PHE A CG   1 
ATOM   3545  C  CD1  . PHE A 1 214 ? 5.757   -3.094  19.248  1.00 6.08   ?  437  PHE A CD1  1 
ATOM   3546  C  CD2  . PHE A 1 214 ? 4.818   -2.562  17.129  1.00 6.20   ?  437  PHE A CD2  1 
ATOM   3547  C  CE1  . PHE A 1 214 ? 4.482   -3.204  19.771  1.00 6.43   ?  437  PHE A CE1  1 
ATOM   3548  C  CE2  . PHE A 1 214 ? 3.551   -2.669  17.657  1.00 6.94   ?  437  PHE A CE2  1 
ATOM   3549  C  CZ   . PHE A 1 214 ? 3.384   -2.992  18.978  1.00 6.72   ?  437  PHE A CZ   1 
ATOM   3550  H  H    . PHE A 1 214 ? 8.399   -4.503  18.762  1.00 6.55   ?  437  PHE A H    1 
ATOM   3551  H  HA   . PHE A 1 214 ? 7.377   -4.386  16.221  1.00 5.99   ?  437  PHE A HA   1 
ATOM   3552  H  HB2  . PHE A 1 214 ? 7.904   -2.259  18.000  1.00 7.34   ?  437  PHE A HB2  1 
ATOM   3553  H  HB3  . PHE A 1 214 ? 7.283   -2.098  16.546  1.00 7.34   ?  437  PHE A HB3  1 
ATOM   3554  H  HD1  . PHE A 1 214 ? 6.495   -3.235  19.796  1.00 7.29   ?  437  PHE A HD1  1 
ATOM   3555  H  HD2  . PHE A 1 214 ? 4.922   -2.342  16.231  1.00 7.44   ?  437  PHE A HD2  1 
ATOM   3556  H  HE1  . PHE A 1 214 ? 4.368   -3.423  20.668  1.00 7.72   ?  437  PHE A HE1  1 
ATOM   3557  H  HE2  . PHE A 1 214 ? 2.808   -2.521  17.117  1.00 8.34   ?  437  PHE A HE2  1 
ATOM   3558  H  HZ   . PHE A 1 214 ? 2.529   -3.068  19.335  1.00 8.06   ?  437  PHE A HZ   1 
ATOM   3559  N  N    . ARG A 1 215 ? 9.590   -4.383  15.179  1.00 5.47   ?  438  ARG A N    1 
ATOM   3560  C  CA   . ARG A 1 215 ? 10.922  -4.547  14.622  1.00 5.84   ?  438  ARG A CA   1 
ATOM   3561  C  C    . ARG A 1 215 ? 11.207  -3.539  13.524  1.00 5.64   ?  438  ARG A C    1 
ATOM   3562  O  O    . ARG A 1 215 ? 10.360  -3.282  12.664  1.00 5.94   ?  438  ARG A O    1 
ATOM   3563  C  CB   . ARG A 1 215 ? 11.058  -5.963  14.045  1.00 6.40   ?  438  ARG A CB   1 
ATOM   3564  C  CG   . ARG A 1 215 ? 12.384  -6.201  13.342  1.00 7.40   ?  438  ARG A CG   1 
ATOM   3565  C  CD   . ARG A 1 215 ? 12.624  -7.669  13.045  1.00 7.08   ?  438  ARG A CD   1 
ATOM   3566  N  NE   . ARG A 1 215 ? 12.839  -8.415  14.275  1.00 7.27   ?  438  ARG A NE   1 
ATOM   3567  C  CZ   . ARG A 1 215 ? 13.331  -9.637  14.337  1.00 8.24   ?  438  ARG A CZ   1 
ATOM   3568  N  NH1  . ARG A 1 215 ? 13.581  -10.338 13.241  1.00 9.72   ?  438  ARG A NH1  1 
ATOM   3569  N  NH2  . ARG A 1 215 ? 13.575  -10.177 15.527  1.00 8.38   ?  438  ARG A NH2  1 
ATOM   3570  H  H    . ARG A 1 215 ? 8.969   -4.646  14.646  1.00 6.57   ?  438  ARG A H    1 
ATOM   3571  H  HA   . ARG A 1 215 ? 11.576  -4.395  15.322  1.00 7.01   ?  438  ARG A HA   1 
ATOM   3572  H  HB2  . ARG A 1 215 ? 10.984  -6.605  14.768  1.00 7.68   ?  438  ARG A HB2  1 
ATOM   3573  H  HB3  . ARG A 1 215 ? 10.348  -6.107  13.400  1.00 7.68   ?  438  ARG A HB3  1 
ATOM   3574  H  HG2  . ARG A 1 215 ? 12.390  -5.719  12.501  1.00 8.88   ?  438  ARG A HG2  1 
ATOM   3575  H  HG3  . ARG A 1 215 ? 13.106  -5.887  13.909  1.00 8.88   ?  438  ARG A HG3  1 
ATOM   3576  H  HD2  . ARG A 1 215 ? 11.850  -8.039  12.591  1.00 8.50   ?  438  ARG A HD2  1 
ATOM   3577  H  HD3  . ARG A 1 215 ? 13.412  -7.762  12.487  1.00 8.50   ?  438  ARG A HD3  1 
ATOM   3578  H  HE   . ARG A 1 215 ? 12.629  -8.031  15.016  1.00 8.72   ?  438  ARG A HE   1 
ATOM   3579  H  HH11 . ARG A 1 215 ? 13.422  -9.998  12.468  1.00 11.67  ?  438  ARG A HH11 1 
ATOM   3580  H  HH12 . ARG A 1 215 ? 13.903  -11.133 13.304  1.00 11.67  ?  438  ARG A HH12 1 
ATOM   3581  H  HH21 . ARG A 1 215 ? 13.410  -9.730  16.244  1.00 10.06  ?  438  ARG A HH21 1 
ATOM   3582  H  HH22 . ARG A 1 215 ? 13.896  -10.972 15.581  1.00 10.06  ?  438  ARG A HH22 1 
ATOM   3583  N  N    . SER A 1 216 ? 12.434  -3.001  13.533  1.00 5.51   ?  439  SER A N    1 
ATOM   3584  C  CA   . SER A 1 216 ? 12.944  -2.179  12.449  1.00 5.74   ?  439  SER A CA   1 
ATOM   3585  C  C    . SER A 1 216 ? 14.311  -2.655  12.000  1.00 5.71   ?  439  SER A C    1 
ATOM   3586  O  O    . SER A 1 216 ? 15.157  -3.003  12.827  1.00 6.53   ?  439  SER A O    1 
ATOM   3587  C  CB   . SER A 1 216 ? 13.093  -0.716  12.861  1.00 6.08   ?  439  SER A CB   1 
ATOM   3588  O  OG   . SER A 1 216 ? 11.866  -0.181  13.311  1.00 6.38   ?  439  SER A OG   1 
ATOM   3589  H  H    . SER A 1 216 ? 12.996  -3.107  14.175  1.00 6.62   ?  439  SER A H    1 
ATOM   3590  H  HA   . SER A 1 216 ? 12.317  -2.257  11.713  1.00 6.90   ?  439  SER A HA   1 
ATOM   3591  H  HB2  . SER A 1 216 ? 13.743  -0.657  13.579  1.00 7.30   ?  439  SER A HB2  1 
ATOM   3592  H  HB3  . SER A 1 216 ? 13.397  -0.204  12.096  1.00 7.30   ?  439  SER A HB3  1 
ATOM   3593  H  HG   . SER A 1 216 ? 11.405  0.072   12.656  1.00 7.66   ?  439  SER A HG   1 
ATOM   3594  N  N    . TYR A 1 217 ? 14.547  -2.597  10.694  1.00 6.00   ?  440  TYR A N    1 
ATOM   3595  C  CA   . TYR A 1 217 ? 15.886  -2.804  10.171  1.00 6.25   ?  440  TYR A CA   1 
ATOM   3596  C  C    . TYR A 1 217 ? 16.704  -1.537  10.332  1.00 7.33   ?  440  TYR A C    1 
ATOM   3597  O  O    . TYR A 1 217 ? 16.170  -0.430  10.431  1.00 9.09   ?  440  TYR A O    1 
ATOM   3598  C  CB   . TYR A 1 217 ? 15.829  -3.224  8.706   1.00 8.43   ?  440  TYR A CB   1 
ATOM   3599  C  CG   . TYR A 1 217 ? 15.236  -4.586  8.530   1.00 10.41  ?  440  TYR A CG   1 
ATOM   3600  C  CD1  . TYR A 1 217 ? 15.961  -5.726  8.839   1.00 11.50  ?  440  TYR A CD1  1 
ATOM   3601  C  CD2  . TYR A 1 217 ? 13.943  -4.736  8.074   1.00 12.65  ?  440  TYR A CD2  1 
ATOM   3602  C  CE1  . TYR A 1 217 ? 15.419  -6.977  8.693   1.00 13.29  ?  440  TYR A CE1  1 
ATOM   3603  C  CE2  . TYR A 1 217 ? 13.385  -5.986  7.917   1.00 14.86  ?  440  TYR A CE2  1 
ATOM   3604  C  CZ   . TYR A 1 217 ? 14.124  -7.106  8.228   1.00 15.88  ?  440  TYR A CZ   1 
ATOM   3605  O  OH   . TYR A 1 217 ? 13.553  -8.354  8.078   1.00 18.81  ?  440  TYR A OH   1 
ATOM   3606  H  H    . TYR A 1 217 ? 13.950  -2.440  10.095  1.00 7.21   ?  440  TYR A H    1 
ATOM   3607  H  HA   . TYR A 1 217 ? 16.327  -3.516  10.660  1.00 7.51   ?  440  TYR A HA   1 
ATOM   3608  H  HB2  . TYR A 1 217 ? 15.282  -2.591  8.215   1.00 10.12  ?  440  TYR A HB2  1 
ATOM   3609  H  HB3  . TYR A 1 217 ? 16.728  -3.237  8.344   1.00 10.12  ?  440  TYR A HB3  1 
ATOM   3610  H  HD1  . TYR A 1 217 ? 16.833  -5.640  9.153   1.00 13.80  ?  440  TYR A HD1  1 
ATOM   3611  H  HD2  . TYR A 1 217 ? 13.439  -3.981  7.869   1.00 15.18  ?  440  TYR A HD2  1 
ATOM   3612  H  HE1  . TYR A 1 217 ? 15.919  -7.732  8.905   1.00 15.95  ?  440  TYR A HE1  1 
ATOM   3613  H  HE2  . TYR A 1 217 ? 12.514  -6.073  7.603   1.00 17.83  ?  440  TYR A HE2  1 
ATOM   3614  H  HH   . TYR A 1 217 ? 14.101  -8.950  8.305   1.00 22.58  ?  440  TYR A HH   1 
ATOM   3615  N  N    . LEU A 1 218 ? 18.023  -1.716  10.375  1.00 7.13   ?  441  LEU A N    1 
ATOM   3616  C  CA   . LEU A 1 218 ? 18.967  -0.635  10.560  1.00 7.23   ?  441  LEU A CA   1 
ATOM   3617  C  C    . LEU A 1 218 ? 19.927  -0.526  9.381   1.00 6.37   ?  441  LEU A C    1 
ATOM   3618  O  O    . LEU A 1 218 ? 20.449  -1.541  8.913   1.00 7.24   ?  441  LEU A O    1 
ATOM   3619  C  CB   . LEU A 1 218 ? 19.798  -0.857  11.825  1.00 7.97   ?  441  LEU A CB   1 
ATOM   3620  C  CG   . LEU A 1 218 ? 19.031  -0.910  13.142  1.00 10.17  ?  441  LEU A CG   1 
ATOM   3621  C  CD1  . LEU A 1 218 ? 19.972  -1.289  14.270  1.00 12.56  ?  441  LEU A CD1  1 
ATOM   3622  C  CD2  . LEU A 1 218 ? 18.323  0.408   13.432  1.00 12.24  ?  441  LEU A CD2  1 
ATOM   3623  H  H    . LEU A 1 218 ? 18.402  -2.484  10.297  1.00 8.56   ?  441  LEU A H    1 
ATOM   3624  H  HA   . LEU A 1 218 ? 18.473  0.197   10.633  1.00 8.68   ?  441  LEU A HA   1 
ATOM   3625  H  HB2  . LEU A 1 218 ? 20.265  -1.702  11.733  1.00 9.57   ?  441  LEU A HB2  1 
ATOM   3626  H  HB3  . LEU A 1 218 ? 20.436  -0.130  11.897  1.00 9.57   ?  441  LEU A HB3  1 
ATOM   3627  H  HG   . LEU A 1 218 ? 18.340  -1.588  13.079  1.00 12.21  ?  441  LEU A HG   1 
ATOM   3628  H  HD11 . LEU A 1 218 ? 19.475  -1.312  15.102  1.00 15.08  ?  441  LEU A HD11 1 
ATOM   3629  H  HD12 . LEU A 1 218 ? 20.349  -2.164  14.086  1.00 15.08  ?  441  LEU A HD12 1 
ATOM   3630  H  HD13 . LEU A 1 218 ? 20.681  -0.629  14.325  1.00 15.08  ?  441  LEU A HD13 1 
ATOM   3631  H  HD21 . LEU A 1 218 ? 17.927  0.366   14.317  1.00 14.69  ?  441  LEU A HD21 1 
ATOM   3632  H  HD22 . LEU A 1 218 ? 18.970  1.129   13.394  1.00 14.69  ?  441  LEU A HD22 1 
ATOM   3633  H  HD23 . LEU A 1 218 ? 17.632  0.548   12.766  1.00 14.69  ?  441  LEU A HD23 1 
ATOM   3634  N  N    . PRO A 1 219 ? 20.206  0.694   8.913   1.00 6.31   ?  442  PRO A N    1 
ATOM   3635  C  CA   . PRO A 1 219 ? 21.257  0.883   7.915   1.00 5.81   ?  442  PRO A CA   1 
ATOM   3636  C  C    . PRO A 1 219 ? 22.628  0.509   8.448   1.00 5.56   ?  442  PRO A C    1 
ATOM   3637  O  O    . PRO A 1 219 ? 22.900  0.584   9.648   1.00 5.90   ?  442  PRO A O    1 
ATOM   3638  C  CB   . PRO A 1 219 ? 21.190  2.387   7.618   1.00 7.91   ?  442  PRO A CB   1 
ATOM   3639  C  CG   . PRO A 1 219 ? 19.853  2.822   8.069   1.00 9.05   ?  442  PRO A CG   1 
ATOM   3640  C  CD   . PRO A 1 219 ? 19.506  1.957   9.210   1.00 7.35   ?  442  PRO A CD   1 
ATOM   3641  H  HA   . PRO A 1 219 ? 21.062  0.364   7.118   1.00 6.98   ?  442  PRO A HA   1 
ATOM   3642  H  HB2  . PRO A 1 219 ? 21.887  2.849   8.109   1.00 9.49   ?  442  PRO A HB2  1 
ATOM   3643  H  HB3  . PRO A 1 219 ? 21.299  2.538   6.666   1.00 9.49   ?  442  PRO A HB3  1 
ATOM   3644  H  HG2  . PRO A 1 219 ? 19.887  3.753   8.342   1.00 10.86  ?  442  PRO A HG2  1 
ATOM   3645  H  HG3  . PRO A 1 219 ? 19.213  2.712   7.348   1.00 10.86  ?  442  PRO A HG3  1 
ATOM   3646  H  HD2  . PRO A 1 219 ? 19.825  2.340   10.042  1.00 8.82   ?  442  PRO A HD2  1 
ATOM   3647  H  HD3  . PRO A 1 219 ? 18.547  1.816   9.256   1.00 8.82   ?  442  PRO A HD3  1 
ATOM   3648  N  N    . LEU A 1 220 ? 23.521  0.167   7.511   1.00 5.65   ?  443  LEU A N    1 
ATOM   3649  C  CA   . LEU A 1 220 ? 24.919  -0.119  7.791   1.00 5.58   ?  443  LEU A CA   1 
ATOM   3650  C  C    . LEU A 1 220 ? 25.836  0.810   7.005   1.00 5.19   ?  443  LEU A C    1 
ATOM   3651  O  O    . LEU A 1 220 ? 25.605  1.086   5.823   1.00 5.72   ?  443  LEU A O    1 
ATOM   3652  C  CB   . LEU A 1 220 ? 25.271  -1.573  7.419   1.00 6.00   ?  443  LEU A CB   1 
ATOM   3653  C  CG   . LEU A 1 220 ? 24.847  -2.601  8.451   1.00 6.46   ?  443  LEU A CG   1 
ATOM   3654  C  CD1  . LEU A 1 220 ? 24.894  -4.009  7.863   1.00 7.74   ?  443  LEU A CD1  1 
ATOM   3655  C  CD2  . LEU A 1 220 ? 25.729  -2.523  9.664   1.00 8.30   ?  443  LEU A CD2  1 
ATOM   3656  H  H    . LEU A 1 220 ? 23.326  0.093   6.677   1.00 6.78   ?  443  LEU A H    1 
ATOM   3657  H  HA   . LEU A 1 220 ? 25.073  0.028   8.737   1.00 6.69   ?  443  LEU A HA   1 
ATOM   3658  H  HB2  . LEU A 1 220 ? 24.829  -1.795  6.585   1.00 7.20   ?  443  LEU A HB2  1 
ATOM   3659  H  HB3  . LEU A 1 220 ? 26.232  -1.641  7.314   1.00 7.20   ?  443  LEU A HB3  1 
ATOM   3660  H  HG   . LEU A 1 220 ? 23.934  -2.413  8.720   1.00 7.75   ?  443  LEU A HG   1 
ATOM   3661  H  HD11 . LEU A 1 220 ? 24.683  -4.650  8.560   1.00 9.29   ?  443  LEU A HD11 1 
ATOM   3662  H  HD12 . LEU A 1 220 ? 24.243  -4.074  7.146   1.00 9.29   ?  443  LEU A HD12 1 
ATOM   3663  H  HD13 . LEU A 1 220 ? 25.784  -4.178  7.517   1.00 9.29   ?  443  LEU A HD13 1 
ATOM   3664  H  HD21 . LEU A 1 220 ? 25.474  -3.222  10.286  1.00 9.96   ?  443  LEU A HD21 1 
ATOM   3665  H  HD22 . LEU A 1 220 ? 26.652  -2.643  9.391   1.00 9.96   ?  443  LEU A HD22 1 
ATOM   3666  H  HD23 . LEU A 1 220 ? 25.618  -1.653  10.080  1.00 9.96   ?  443  LEU A HD23 1 
ATOM   3667  N  N    . LYS A 1 221 ? 26.922  1.224   7.658   1.00 5.36   ?  444  LYS A N    1 
ATOM   3668  C  CA   . LYS A 1 221 ? 27.971  1.965   6.961   1.00 5.59   ?  444  LYS A CA   1 
ATOM   3669  C  C    . LYS A 1 221 ? 28.653  1.090   5.914   1.00 5.55   ?  444  LYS A C    1 
ATOM   3670  O  O    . LYS A 1 221 ? 29.041  1.568   4.837   1.00 5.94   ?  444  LYS A O    1 
ATOM   3671  C  CB   . LYS A 1 221 ? 29.002  2.494   7.965   1.00 5.81   ?  444  LYS A CB   1 
ATOM   3672  C  CG   . LYS A 1 221 ? 30.269  3.087   7.359   1.00 5.90   ?  444  LYS A CG   1 
ATOM   3673  C  CD   . LYS A 1 221 ? 30.037  4.316   6.478   1.00 5.89   ?  444  LYS A CD   1 
ATOM   3674  C  CE   . LYS A 1 221 ? 31.327  4.725   5.787   1.00 6.75   ?  444  LYS A CE   1 
ATOM   3675  N  NZ   . LYS A 1 221 ? 31.138  5.911   4.917   1.00 6.23   ?  444  LYS A NZ   1 
ATOM   3676  H  H    . LYS A 1 221 ? 27.074  1.091   8.494   1.00 6.44   ?  444  LYS A H    1 
ATOM   3677  H  HA   . LYS A 1 221 ? 27.570  2.726   6.512   1.00 6.71   ?  444  LYS A HA   1 
ATOM   3678  H  HB2  . LYS A 1 221 ? 28.582  3.190   8.494   1.00 6.98   ?  444  LYS A HB2  1 
ATOM   3679  H  HB3  . LYS A 1 221 ? 29.273  1.759   8.538   1.00 6.98   ?  444  LYS A HB3  1 
ATOM   3680  H  HG2  . LYS A 1 221 ? 30.862  3.353   8.080   1.00 7.08   ?  444  LYS A HG2  1 
ATOM   3681  H  HG3  . LYS A 1 221 ? 30.696  2.411   6.811   1.00 7.08   ?  444  LYS A HG3  1 
ATOM   3682  H  HD2  . LYS A 1 221 ? 29.375  4.109   5.799   1.00 7.07   ?  444  LYS A HD2  1 
ATOM   3683  H  HD3  . LYS A 1 221 ? 29.730  5.056   7.025   1.00 7.07   ?  444  LYS A HD3  1 
ATOM   3684  H  HE2  . LYS A 1 221 ? 31.993  4.945   6.458   1.00 8.10   ?  444  LYS A HE2  1 
ATOM   3685  H  HE3  . LYS A 1 221 ? 31.642  3.992   5.236   1.00 8.10   ?  444  LYS A HE3  1 
ATOM   3686  H  HZ1  . LYS A 1 221 ? 30.513  5.744   4.306   1.00 7.48   ?  444  LYS A HZ1  1 
ATOM   3687  H  HZ2  . LYS A 1 221 ? 30.884  6.610   5.406   1.00 7.48   ?  444  LYS A HZ2  1 
ATOM   3688  H  HZ3  . LYS A 1 221 ? 31.901  6.110   4.503   1.00 7.48   ?  444  LYS A HZ3  1 
ATOM   3689  N  N    . GLY A 1 222 ? 28.832  -0.192  6.228   1.00 6.38   ?  445  GLY A N    1 
ATOM   3690  C  CA   . GLY A 1 222 ? 29.451  -1.132  5.322   1.00 6.52   ?  445  GLY A CA   1 
ATOM   3691  C  C    . GLY A 1 222 ? 29.255  -2.549  5.810   1.00 6.91   ?  445  GLY A C    1 
ATOM   3692  O  O    . GLY A 1 222 ? 28.602  -2.795  6.829   1.00 7.66   ?  445  GLY A O    1 
ATOM   3693  H  H    . GLY A 1 222 ? 28.598  -0.542  6.978   1.00 7.66   ?  445  GLY A H    1 
ATOM   3694  H  HA2  . GLY A 1 222 ? 29.055  -1.048  4.441   1.00 7.83   ?  445  GLY A HA2  1 
ATOM   3695  H  HA3  . GLY A 1 222 ? 30.402  -0.952  5.260   1.00 7.83   ?  445  GLY A HA3  1 
ATOM   3696  N  N    . GLY A 1 223 ? 29.816  -3.471  5.040   1.00 7.66   ?  446  GLY A N    1 
ATOM   3697  C  CA   . GLY A 1 223 ? 29.709  -4.889  5.336   1.00 7.77   ?  446  GLY A CA   1 
ATOM   3698  C  C    . GLY A 1 223 ? 28.378  -5.483  4.899   1.00 6.76   ?  446  GLY A C    1 
ATOM   3699  O  O    . GLY A 1 223 ? 27.624  -4.917  4.097   1.00 7.08   ?  446  GLY A O    1 
ATOM   3700  H  H    . GLY A 1 223 ? 30.270  -3.299  4.330   1.00 9.20   ?  446  GLY A H    1 
ATOM   3701  H  HA2  . GLY A 1 223 ? 30.419  -5.366  4.878   1.00 9.33   ?  446  GLY A HA2  1 
ATOM   3702  H  HA3  . GLY A 1 223 ? 29.803  -5.024  6.292   1.00 9.33   ?  446  GLY A HA3  1 
ATOM   3703  N  N    A TYR A 1 224 ? 28.089  -6.649  5.467   0.98 7.25   ?  447  TYR A N    1 
ATOM   3704  C  CA   A TYR A 1 224 ? 27.015  -7.520  5.008   0.98 7.51   ?  447  TYR A CA   1 
ATOM   3705  C  C    A TYR A 1 224 ? 26.003  -7.734  6.121   0.98 8.24   ?  447  TYR A C    1 
ATOM   3706  O  O    A TYR A 1 224 ? 26.361  -7.794  7.301   0.98 10.88  ?  447  TYR A O    1 
ATOM   3707  C  CB   A TYR A 1 224 ? 27.596  -8.878  4.548   0.98 7.68   ?  447  TYR A CB   1 
ATOM   3708  C  CG   A TYR A 1 224 ? 28.468  -8.678  3.341   0.98 6.40   ?  447  TYR A CG   1 
ATOM   3709  C  CD1  A TYR A 1 224 ? 29.796  -8.278  3.471   0.98 7.69   ?  447  TYR A CD1  1 
ATOM   3710  C  CD2  A TYR A 1 224 ? 27.946  -8.800  2.064   0.98 7.12   ?  447  TYR A CD2  1 
ATOM   3711  C  CE1  A TYR A 1 224 ? 30.566  -8.013  2.377   0.98 7.97   ?  447  TYR A CE1  1 
ATOM   3712  C  CE2  A TYR A 1 224 ? 28.730  -8.555  0.951   0.98 7.72   ?  447  TYR A CE2  1 
ATOM   3713  C  CZ   A TYR A 1 224 ? 30.039  -8.162  1.118   0.98 8.21   ?  447  TYR A CZ   1 
ATOM   3714  O  OH   A TYR A 1 224 ? 30.790  -7.902  0.005   0.98 11.33  ?  447  TYR A OH   1 
ATOM   3715  H  H    A TYR A 1 224 ? 28.516  -6.966  6.142   0.98 8.71   ?  447  TYR A H    1 
ATOM   3716  H  HA   A TYR A 1 224 ? 26.547  -7.108  4.265   0.98 9.01   ?  447  TYR A HA   1 
ATOM   3717  H  HB2  A TYR A 1 224 ? 28.132  -9.263  5.260   0.98 9.22   ?  447  TYR A HB2  1 
ATOM   3718  H  HB3  A TYR A 1 224 ? 26.873  -9.481  4.315   0.98 9.22   ?  447  TYR A HB3  1 
ATOM   3719  H  HD1  A TYR A 1 224 ? 30.165  -8.190  4.320   0.98 9.23   ?  447  TYR A HD1  1 
ATOM   3720  H  HD2  A TYR A 1 224 ? 27.058  -9.051  1.953   0.98 8.54   ?  447  TYR A HD2  1 
ATOM   3721  H  HE1  A TYR A 1 224 ? 31.446  -7.732  2.484   0.98 9.57   ?  447  TYR A HE1  1 
ATOM   3722  H  HE2  A TYR A 1 224 ? 28.375  -8.654  0.097   0.98 9.27   ?  447  TYR A HE2  1 
ATOM   3723  H  HH   A TYR A 1 224 ? 31.543  -7.604  0.229   0.98 13.59  ?  447  TYR A HH   1 
ATOM   3724  N  N    . GLY A 1 225 ? 24.736  -7.835  5.744   1.00 7.49   ?  448  GLY A N    1 
ATOM   3725  C  CA   . GLY A 1 225 ? 23.688  -8.141  6.695   1.00 7.98   ?  448  GLY A CA   1 
ATOM   3726  C  C    . GLY A 1 225 ? 22.508  -7.195  6.602   1.00 7.38   ?  448  GLY A C    1 
ATOM   3727  O  O    . GLY A 1 225 ? 22.513  -6.183  5.895   1.00 7.45   ?  448  GLY A O    1 
ATOM   3728  H  H    . GLY A 1 225 ? 24.461  -7.730  4.937   1.00 8.99   ?  448  GLY A H    1 
ATOM   3729  H  HA2  . GLY A 1 225 ? 23.366  -9.042  6.536   1.00 9.58   ?  448  GLY A HA2  1 
ATOM   3730  H  HA3  . GLY A 1 225 ? 24.048  -8.088  7.594   1.00 9.58   ?  448  GLY A HA3  1 
ATOM   3731  N  N    . SER A 1 226 ? 21.482  -7.570  7.355   1.00 7.34   ?  449  SER A N    1 
ATOM   3732  C  CA   . SER A 1 226 ? 20.250  -6.803  7.523   1.00 7.41   ?  449  SER A CA   1 
ATOM   3733  C  C    . SER A 1 226 ? 19.937  -6.723  9.015   1.00 7.02   ?  449  SER A C    1 
ATOM   3734  O  O    . SER A 1 226 ? 18.971  -7.329  9.498   1.00 7.62   ?  449  SER A O    1 
ATOM   3735  C  CB   . SER A 1 226 ? 19.098  -7.470  6.777   1.00 8.74   ?  449  SER A CB   1 
ATOM   3736  O  OG   . SER A 1 226 ? 19.344  -7.480  5.389   1.00 9.18   ?  449  SER A OG   1 
ATOM   3737  H  H    . SER A 1 226 ? 21.473  -8.304  7.803   1.00 8.81   ?  449  SER A H    1 
ATOM   3738  H  HA   . SER A 1 226 ? 20.374  -5.907  7.174   1.00 8.89   ?  449  SER A HA   1 
ATOM   3739  H  HB2  . SER A 1 226 ? 19.005  -8.384  7.089   1.00 10.49  ?  449  SER A HB2  1 
ATOM   3740  H  HB3  . SER A 1 226 ? 18.281  -6.976  6.950   1.00 10.49  ?  449  SER A HB3  1 
ATOM   3741  H  HG   . SER A 1 226 ? 20.043  -7.916  5.224   1.00 11.01  ?  449  SER A HG   1 
ATOM   3742  N  N    . PRO A 1 227 ? 20.750  -5.997  9.777   1.00 6.92   ?  450  PRO A N    1 
ATOM   3743  C  CA   . PRO A 1 227 ? 20.539  -5.961  11.228  1.00 6.49   ?  450  PRO A CA   1 
ATOM   3744  C  C    . PRO A 1 227 ? 19.205  -5.314  11.566  1.00 6.29   ?  450  PRO A C    1 
ATOM   3745  O  O    . PRO A 1 227 ? 18.677  -4.481  10.821  1.00 6.79   ?  450  PRO A O    1 
ATOM   3746  C  CB   . PRO A 1 227 ? 21.717  -5.125  11.739  1.00 7.44   ?  450  PRO A CB   1 
ATOM   3747  C  CG   . PRO A 1 227 ? 22.127  -4.302  10.548  1.00 7.37   ?  450  PRO A CG   1 
ATOM   3748  C  CD   . PRO A 1 227 ? 21.917  -5.201  9.366   1.00 7.09   ?  450  PRO A CD   1 
ATOM   3749  H  HA   . PRO A 1 227 ? 20.582  -6.850  11.612  1.00 7.79   ?  450  PRO A HA   1 
ATOM   3750  H  HB2  . PRO A 1 227 ? 21.431  -4.560  12.474  1.00 8.93   ?  450  PRO A HB2  1 
ATOM   3751  H  HB3  . PRO A 1 227 ? 22.438  -5.706  12.028  1.00 8.93   ?  450  PRO A HB3  1 
ATOM   3752  H  HG2  . PRO A 1 227 ? 21.570  -3.511  10.484  1.00 8.85   ?  450  PRO A HG2  1 
ATOM   3753  H  HG3  . PRO A 1 227 ? 23.059  -4.047  10.627  1.00 8.85   ?  450  PRO A HG3  1 
ATOM   3754  H  HD2  . PRO A 1 227 ? 21.724  -4.687  8.566   1.00 8.51   ?  450  PRO A HD2  1 
ATOM   3755  H  HD3  . PRO A 1 227 ? 22.690  -5.768  9.217   1.00 8.51   ?  450  PRO A HD3  1 
ATOM   3756  N  N    . PHE A 1 228 ? 18.675  -5.690  12.729  1.00 6.05   ?  451  PHE A N    1 
ATOM   3757  C  CA   . PHE A 1 228 ? 17.376  -5.199  13.168  1.00 6.33   ?  451  PHE A CA   1 
ATOM   3758  C  C    . PHE A 1 228 ? 17.360  -4.960  14.675  1.00 5.69   ?  451  PHE A C    1 
ATOM   3759  O  O    . PHE A 1 228 ? 18.179  -5.486  15.437  1.00 6.27   ?  451  PHE A O    1 
ATOM   3760  C  CB   . PHE A 1 228 ? 16.241  -6.174  12.775  1.00 6.89   ?  451  PHE A CB   1 
ATOM   3761  C  CG   . PHE A 1 228 ? 16.489  -7.576  13.255  1.00 7.64   ?  451  PHE A CG   1 
ATOM   3762  C  CD1  . PHE A 1 228 ? 16.252  -7.922  14.571  1.00 8.38   ?  451  PHE A CD1  1 
ATOM   3763  C  CD2  . PHE A 1 228 ? 16.991  -8.537  12.400  1.00 8.97   ?  451  PHE A CD2  1 
ATOM   3764  C  CE1  . PHE A 1 228 ? 16.530  -9.195  15.029  1.00 8.87   ?  451  PHE A CE1  1 
ATOM   3765  C  CE2  . PHE A 1 228 ? 17.245  -9.822  12.855  1.00 10.29  ?  451  PHE A CE2  1 
ATOM   3766  C  CZ   . PHE A 1 228 ? 17.012  -10.150 14.168  1.00 10.00  ?  451  PHE A CZ   1 
ATOM   3767  H  H    . PHE A 1 228 ? 19.051  -6.231  13.281  1.00 7.26   ?  451  PHE A H    1 
ATOM   3768  H  HA   . PHE A 1 228 ? 17.219  -4.340  12.744  1.00 7.60   ?  451  PHE A HA   1 
ATOM   3769  H  HB2  . PHE A 1 228 ? 15.409  -5.865  13.167  1.00 8.27   ?  451  PHE A HB2  1 
ATOM   3770  H  HB3  . PHE A 1 228 ? 16.164  -6.197  11.809  1.00 8.27   ?  451  PHE A HB3  1 
ATOM   3771  H  HD1  . PHE A 1 228 ? 15.900  -7.290  15.156  1.00 10.05  ?  451  PHE A HD1  1 
ATOM   3772  H  HD2  . PHE A 1 228 ? 17.161  -8.321  11.511  1.00 10.76  ?  451  PHE A HD2  1 
ATOM   3773  H  HE1  . PHE A 1 228 ? 16.390  -9.406  15.924  1.00 10.64  ?  451  PHE A HE1  1 
ATOM   3774  H  HE2  . PHE A 1 228 ? 17.574  -10.464 12.268  1.00 12.35  ?  451  PHE A HE2  1 
ATOM   3775  H  HZ   . PHE A 1 228 ? 17.180  -11.013 14.472  1.00 12.01  ?  451  PHE A HZ   1 
ATOM   3776  N  N    . ILE A 1 229 ? 16.404  -4.145  15.103  1.00 5.85   ?  452  ILE A N    1 
ATOM   3777  C  CA   . ILE A 1 229 ? 16.221  -3.824  16.512  1.00 5.70   ?  452  ILE A CA   1 
ATOM   3778  C  C    . ILE A 1 229 ? 14.744  -3.913  16.853  1.00 5.25   ?  452  ILE A C    1 
ATOM   3779  O  O    . ILE A 1 229 ? 13.887  -3.438  16.098  1.00 5.80   ?  452  ILE A O    1 
ATOM   3780  C  CB   . ILE A 1 229 ? 16.856  -2.453  16.862  1.00 6.24   ?  452  ILE A CB   1 
ATOM   3781  C  CG1  . ILE A 1 229 ? 16.963  -2.246  18.370  1.00 6.75   ?  452  ILE A CG1  1 
ATOM   3782  C  CG2  . ILE A 1 229 ? 16.141  -1.314  16.184  1.00 7.32   ?  452  ILE A CG2  1 
ATOM   3783  C  CD1  . ILE A 1 229 ? 17.899  -1.117  18.751  1.00 7.05   ?  452  ILE A CD1  1 
ATOM   3784  H  H    . ILE A 1 229 ? 15.837  -3.758  14.584  1.00 7.03   ?  452  ILE A H    1 
ATOM   3785  H  HA   . ILE A 1 229 ? 16.661  -4.486  17.068  1.00 6.84   ?  452  ILE A HA   1 
ATOM   3786  H  HB   . ILE A 1 229 ? 17.761  -2.465  16.513  1.00 7.49   ?  452  ILE A HB   1 
ATOM   3787  H  HG12 . ILE A 1 229 ? 16.084  -2.037  18.722  1.00 8.10   ?  452  ILE A HG12 1 
ATOM   3788  H  HG13 . ILE A 1 229 ? 17.298  -3.061  18.776  1.00 8.10   ?  452  ILE A HG13 1 
ATOM   3789  H  HG21 . ILE A 1 229 ? 16.651  -0.499  16.315  1.00 8.79   ?  452  ILE A HG21 1 
ATOM   3790  H  HG22 . ILE A 1 229 ? 16.065  -1.508  15.237  1.00 8.79   ?  452  ILE A HG22 1 
ATOM   3791  H  HG23 . ILE A 1 229 ? 15.259  -1.218  16.574  1.00 8.79   ?  452  ILE A HG23 1 
ATOM   3792  H  HD11 . ILE A 1 229 ? 17.994  -1.097  19.716  1.00 8.46   ?  452  ILE A HD11 1 
ATOM   3793  H  HD12 . ILE A 1 229 ? 18.763  -1.269  18.336  1.00 8.46   ?  452  ILE A HD12 1 
ATOM   3794  H  HD13 . ILE A 1 229 ? 17.525  -0.278  18.438  1.00 8.46   ?  452  ILE A HD13 1 
ATOM   3795  N  N    . ASP A 1 230 ? 14.456  -4.544  17.982  1.00 5.66   ?  453  ASP A N    1 
ATOM   3796  C  CA   . ASP A 1 230 ? 13.101  -4.844  18.433  1.00 5.38   ?  453  ASP A CA   1 
ATOM   3797  C  C    . ASP A 1 230 ? 12.754  -4.001  19.651  1.00 5.84   ?  453  ASP A C    1 
ATOM   3798  O  O    . ASP A 1 230 ? 13.486  -4.018  20.647  1.00 6.32   ?  453  ASP A O    1 
ATOM   3799  C  CB   . ASP A 1 230 ? 13.015  -6.327  18.808  1.00 6.16   ?  453  ASP A CB   1 
ATOM   3800  C  CG   . ASP A 1 230 ? 13.148  -7.236  17.608  1.00 7.25   ?  453  ASP A CG   1 
ATOM   3801  O  OD1  . ASP A 1 230 ? 12.436  -6.991  16.617  1.00 8.59   ?  453  ASP A OD1  1 
ATOM   3802  O  OD2  . ASP A 1 230 ? 13.961  -8.196  17.666  1.00 7.63   -1 453  ASP A OD2  1 
ATOM   3803  H  H    . ASP A 1 230 ? 15.056  -4.823  18.531  1.00 6.79   ?  453  ASP A H    1 
ATOM   3804  H  HA   . ASP A 1 230 ? 12.466  -4.631  17.731  1.00 6.45   ?  453  ASP A HA   1 
ATOM   3805  H  HB2  . ASP A 1 230 ? 13.730  -6.540  19.428  1.00 7.40   ?  453  ASP A HB2  1 
ATOM   3806  H  HB3  . ASP A 1 230 ? 12.154  -6.499  19.222  1.00 7.40   ?  453  ASP A HB3  1 
ATOM   3807  N  N    . CYS A 1 231 ? 11.630  -3.295  19.585  1.00 5.36   ?  454  CYS A N    1 
ATOM   3808  C  CA   . CYS A 1 231 ? 11.177  -2.519  20.726  1.00 5.32   ?  454  CYS A CA   1 
ATOM   3809  C  C    . CYS A 1 231 ? 9.891   -3.111  21.289  1.00 5.52   ?  454  CYS A C    1 
ATOM   3810  O  O    . CYS A 1 231 ? 9.165   -3.863  20.620  1.00 5.56   ?  454  CYS A O    1 
ATOM   3811  C  CB   . CYS A 1 231 ? 11.018  -1.034  20.381  1.00 5.82   ?  454  CYS A CB   1 
ATOM   3812  S  SG   . CYS A 1 231 ? 9.680   -0.586  19.302  1.00 6.02   ?  454  CYS A SG   1 
ATOM   3813  H  H    . CYS A 1 231 ? 11.119  -3.253  18.894  1.00 6.43   ?  454  CYS A H    1 
ATOM   3814  H  HA   . CYS A 1 231 ? 11.844  -2.563  21.429  1.00 6.38   ?  454  CYS A HA   1 
ATOM   3815  H  HB2  . CYS A 1 231 ? 10.885  -0.548  21.210  1.00 6.99   ?  454  CYS A HB2  1 
ATOM   3816  H  HB3  . CYS A 1 231 ? 11.836  -0.738  19.952  1.00 6.99   ?  454  CYS A HB3  1 
ATOM   3817  H  HG   . CYS A 1 231 ? 9.335   0.536   19.552  1.00 7.23   ?  454  CYS A HG   1 
ATOM   3818  N  N    . LEU A 1 232 ? 9.619   -2.766  22.551  1.00 5.16   ?  455  LEU A N    1 
ATOM   3819  C  CA   . LEU A 1 232 ? 8.468   -3.332  23.260  1.00 5.70   ?  455  LEU A CA   1 
ATOM   3820  C  C    . LEU A 1 232 ? 7.153   -2.646  22.883  1.00 5.51   ?  455  LEU A C    1 
ATOM   3821  O  O    . LEU A 1 232 ? 6.115   -3.302  22.804  1.00 5.91   ?  455  LEU A O    1 
ATOM   3822  C  CB   . LEU A 1 232 ? 8.679   -3.288  24.779  1.00 5.97   ?  455  LEU A CB   1 
ATOM   3823  C  CG   . LEU A 1 232 ? 9.903   -4.046  25.275  1.00 7.09   ?  455  LEU A CG   1 
ATOM   3824  C  CD1  . LEU A 1 232 ? 9.998   -3.932  26.781  1.00 8.57   ?  455  LEU A CD1  1 
ATOM   3825  C  CD2  . LEU A 1 232 ? 9.873   -5.515  24.879  1.00 8.57   ?  455  LEU A CD2  1 
ATOM   3826  H  H    . LEU A 1 232 ? 10.081  -2.210  23.016  1.00 6.19   ?  455  LEU A H    1 
ATOM   3827  H  HA   . LEU A 1 232 ? 8.399   -4.265  23.001  1.00 6.84   ?  455  LEU A HA   1 
ATOM   3828  H  HB2  . LEU A 1 232 ? 8.779   -2.362  25.048  1.00 7.17   ?  455  LEU A HB2  1 
ATOM   3829  H  HB3  . LEU A 1 232 ? 7.901   -3.676  25.209  1.00 7.17   ?  455  LEU A HB3  1 
ATOM   3830  H  HG   . LEU A 1 232 ? 10.687  -3.651  24.862  1.00 8.51   ?  455  LEU A HG   1 
ATOM   3831  H  HD11 . LEU A 1 232 ? 10.785  -4.410  27.085  1.00 10.29  ?  455  LEU A HD11 1 
ATOM   3832  H  HD12 . LEU A 1 232 ? 10.065  -2.995  27.023  1.00 10.29  ?  455  LEU A HD12 1 
ATOM   3833  H  HD13 . LEU A 1 232 ? 9.202   -4.320  27.178  1.00 10.29  ?  455  LEU A HD13 1 
ATOM   3834  H  HD21 . LEU A 1 232 ? 10.604  -5.976  25.319  1.00 10.28  ?  455  LEU A HD21 1 
ATOM   3835  H  HD22 . LEU A 1 232 ? 9.026   -5.899  25.155  1.00 10.28  ?  455  LEU A HD22 1 
ATOM   3836  H  HD23 . LEU A 1 232 ? 9.969   -5.585  23.917  1.00 10.28  ?  455  LEU A HD23 1 
ATOM   3837  N  N    . VAL A 1 233 ? 7.180   -1.328  22.700  1.00 5.78   ?  456  VAL A N    1 
ATOM   3838  C  CA   . VAL A 1 233 ? 6.054   -0.547  22.189  1.00 5.57   ?  456  VAL A CA   1 
ATOM   3839  C  C    . VAL A 1 233 ? 6.606   0.555   21.309  1.00 5.32   ?  456  VAL A C    1 
ATOM   3840  O  O    . VAL A 1 233 ? 7.752   1.000   21.494  1.00 6.09   ?  456  VAL A O    1 
ATOM   3841  C  CB   . VAL A 1 233 ? 5.182   0.077   23.316  1.00 6.23   ?  456  VAL A CB   1 
ATOM   3842  C  CG1  . VAL A 1 233 ? 4.582   -0.984  24.252  1.00 6.10   ?  456  VAL A CG1  1 
ATOM   3843  C  CG2  . VAL A 1 233 ? 5.965   1.139   24.103  1.00 7.65   ?  456  VAL A CG2  1 
ATOM   3844  H  H    . VAL A 1 233 ? 7.867   -0.841  22.873  1.00 6.94   ?  456  VAL A H    1 
ATOM   3845  H  HA   . VAL A 1 233 ? 5.475   -1.123  21.666  1.00 6.68   ?  456  VAL A HA   1 
ATOM   3846  H  HB   . VAL A 1 233 ? 4.432   0.518   22.886  1.00 7.48   ?  456  VAL A HB   1 
ATOM   3847  H  HG11 . VAL A 1 233 ? 4.005   -0.546  24.896  1.00 7.33   ?  456  VAL A HG11 1 
ATOM   3848  H  HG12 . VAL A 1 233 ? 4.070   -1.617  23.725  1.00 7.33   ?  456  VAL A HG12 1 
ATOM   3849  H  HG13 . VAL A 1 233 ? 5.303   -1.442  24.712  1.00 7.33   ?  456  VAL A HG13 1 
ATOM   3850  H  HG21 . VAL A 1 233 ? 5.459   1.384   24.893  1.00 9.18   ?  456  VAL A HG21 1 
ATOM   3851  H  HG22 . VAL A 1 233 ? 6.824   0.770   24.362  1.00 9.18   ?  456  VAL A HG22 1 
ATOM   3852  H  HG23 . VAL A 1 233 ? 6.096   1.917   23.539  1.00 9.18   ?  456  VAL A HG23 1 
ATOM   3853  N  N    . PRO A 1 234 ? 5.830   1.029   20.336  1.00 5.50   ?  457  PRO A N    1 
ATOM   3854  C  CA   . PRO A 1 234 ? 6.276   2.161   19.522  1.00 5.98   ?  457  PRO A CA   1 
ATOM   3855  C  C    . PRO A 1 234 ? 6.480   3.420   20.353  1.00 5.33   ?  457  PRO A C    1 
ATOM   3856  O  O    . PRO A 1 234 ? 5.878   3.606   21.410  1.00 5.70   ?  457  PRO A O    1 
ATOM   3857  C  CB   . PRO A 1 234 ? 5.119   2.364   18.536  1.00 7.01   ?  457  PRO A CB   1 
ATOM   3858  C  CG   . PRO A 1 234 ? 4.418   1.020   18.502  1.00 7.56   ?  457  PRO A CG   1 
ATOM   3859  C  CD   . PRO A 1 234 ? 4.524   0.504   19.891  1.00 6.16   ?  457  PRO A CD   1 
ATOM   3860  H  HA   . PRO A 1 234 ? 7.095   1.934   19.055  1.00 7.18   ?  457  PRO A HA   1 
ATOM   3861  H  HB2  . PRO A 1 234 ? 4.525   3.060   18.858  1.00 8.41   ?  457  PRO A HB2  1 
ATOM   3862  H  HB3  . PRO A 1 234 ? 5.464   2.601   17.661  1.00 8.41   ?  457  PRO A HB3  1 
ATOM   3863  H  HG2  . PRO A 1 234 ? 3.491   1.136   18.243  1.00 9.07   ?  457  PRO A HG2  1 
ATOM   3864  H  HG3  . PRO A 1 234 ? 4.866   0.429   17.876  1.00 9.07   ?  457  PRO A HG3  1 
ATOM   3865  H  HD2  . PRO A 1 234 ? 3.806   0.848   20.445  1.00 7.40   ?  457  PRO A HD2  1 
ATOM   3866  H  HD3  . PRO A 1 234 ? 4.517   -0.466  19.903  1.00 7.40   ?  457  PRO A HD3  1 
ATOM   3867  N  N    . GLN A 1 235 ? 7.312   4.321   19.831  1.00 5.62   ?  458  GLN A N    1 
ATOM   3868  C  CA   . GLN A 1 235 ? 7.538   5.575   20.542  1.00 5.84   ?  458  GLN A CA   1 
ATOM   3869  C  C    . GLN A 1 235 ? 6.250   6.371   20.710  1.00 5.58   ?  458  GLN A C    1 
ATOM   3870  O  O    . GLN A 1 235 ? 6.061   7.046   21.726  1.00 6.24   ?  458  GLN A O    1 
ATOM   3871  C  CB   . GLN A 1 235 ? 8.575   6.415   19.804  1.00 5.90   ?  458  GLN A CB   1 
ATOM   3872  C  CG   . GLN A 1 235 ? 8.913   7.711   20.527  1.00 6.24   ?  458  GLN A CG   1 
ATOM   3873  C  CD   . GLN A 1 235 ? 9.569   7.500   21.869  1.00 7.14   ?  458  GLN A CD   1 
ATOM   3874  O  OE1  . GLN A 1 235 ? 10.125  6.439   22.152  1.00 7.57   ?  458  GLN A OE1  1 
ATOM   3875  N  NE2  . GLN A 1 235 ? 9.526   8.531   22.712  1.00 8.27   ?  458  GLN A NE2  1 
ATOM   3876  H  H    . GLN A 1 235 ? 7.744   4.232   19.092  1.00 6.75   ?  458  GLN A H    1 
ATOM   3877  H  HA   . GLN A 1 235 ? 7.882   5.370   21.426  1.00 7.01   ?  458  GLN A HA   1 
ATOM   3878  H  HB2  . GLN A 1 235 ? 9.392   5.900   19.715  1.00 7.08   ?  458  GLN A HB2  1 
ATOM   3879  H  HB3  . GLN A 1 235 ? 8.230   6.643   18.927  1.00 7.08   ?  458  GLN A HB3  1 
ATOM   3880  H  HG2  . GLN A 1 235 ? 9.523   8.227   19.976  1.00 7.48   ?  458  GLN A HG2  1 
ATOM   3881  H  HG3  . GLN A 1 235 ? 8.094   8.210   20.672  1.00 7.48   ?  458  GLN A HG3  1 
ATOM   3882  H  HE21 . GLN A 1 235 ? 9.139   9.263   22.477  1.00 9.93   ?  458  GLN A HE21 1 
ATOM   3883  H  HE22 . GLN A 1 235 ? 9.884   8.465   23.491  1.00 9.93   ?  458  GLN A HE22 1 
ATOM   3884  N  N    . GLU A 1 236 ? 5.344   6.291   19.739  1.00 5.65   ?  459  GLU A N    1 
ATOM   3885  C  CA   . GLU A 1 236 ? 4.094   7.038   19.836  1.00 5.95   ?  459  GLU A CA   1 
ATOM   3886  C  C    . GLU A 1 236 ? 3.201   6.476   20.944  1.00 6.00   ?  459  GLU A C    1 
ATOM   3887  O  O    . GLU A 1 236 ? 2.386   7.208   21.520  1.00 6.68   ?  459  GLU A O    1 
ATOM   3888  C  CB   . GLU A 1 236 ? 3.389   7.059   18.485  1.00 7.23   ?  459  GLU A CB   1 
ATOM   3889  C  CG   . GLU A 1 236 ? 4.128   7.894   17.431  1.00 7.06   ?  459  GLU A CG   1 
ATOM   3890  C  CD   . GLU A 1 236 ? 5.371   7.231   16.858  1.00 7.85   ?  459  GLU A CD   1 
ATOM   3891  O  OE1  . GLU A 1 236 ? 5.536   6.012   17.007  1.00 7.27   ?  459  GLU A OE1  1 
ATOM   3892  O  OE2  . GLU A 1 236 ? 6.189   7.947   16.242  1.00 9.71   -1 459  GLU A OE2  1 
ATOM   3893  H  H    . GLU A 1 236 ? 5.426   5.819   19.024  1.00 6.79   ?  459  GLU A H    1 
ATOM   3894  H  HA   . GLU A 1 236 ? 4.281   7.963   20.063  1.00 7.14   ?  459  GLU A HA   1 
ATOM   3895  H  HB2  . GLU A 1 236 ? 3.321   6.151   18.152  1.00 8.67   ?  459  GLU A HB2  1 
ATOM   3896  H  HB3  . GLU A 1 236 ? 2.504   7.438   18.598  1.00 8.67   ?  459  GLU A HB3  1 
ATOM   3897  H  HG2  . GLU A 1 236 ? 3.522   8.067   16.693  1.00 8.48   ?  459  GLU A HG2  1 
ATOM   3898  H  HG3  . GLU A 1 236 ? 4.404   8.730   17.837  1.00 8.48   ?  459  GLU A HG3  1 
ATOM   3899  N  N    . TRP A 1 237 ? 3.353   5.194   21.291  1.00 5.56   ?  460  TRP A N    1 
ATOM   3900  C  CA   . TRP A 1 237 ? 2.646   4.682   22.454  1.00 5.15   ?  460  TRP A CA   1 
ATOM   3901  C  C    . TRP A 1 237 ? 3.238   5.248   23.741  1.00 5.47   ?  460  TRP A C    1 
ATOM   3902  O  O    . TRP A 1 237 ? 2.500   5.576   24.676  1.00 6.29   ?  460  TRP A O    1 
ATOM   3903  C  CB   . TRP A 1 237 ? 2.675   3.163   22.511  1.00 5.79   ?  460  TRP A CB   1 
ATOM   3904  C  CG   . TRP A 1 237 ? 1.864   2.431   21.484  1.00 5.72   ?  460  TRP A CG   1 
ATOM   3905  C  CD1  . TRP A 1 237 ? 1.488   2.852   20.239  1.00 5.96   ?  460  TRP A CD1  1 
ATOM   3906  C  CD2  . TRP A 1 237 ? 1.370   1.097   21.622  1.00 5.81   ?  460  TRP A CD2  1 
ATOM   3907  N  NE1  . TRP A 1 237 ? 0.785   1.851   19.594  1.00 5.79   ?  460  TRP A NE1  1 
ATOM   3908  C  CE2  . TRP A 1 237 ? 0.704   0.760   20.423  1.00 5.83   ?  460  TRP A CE2  1 
ATOM   3909  C  CE3  . TRP A 1 237 ? 1.429   0.153   22.645  1.00 5.93   ?  460  TRP A CE3  1 
ATOM   3910  C  CZ2  . TRP A 1 237 ? 0.106   -0.483  20.245  1.00 6.27   ?  460  TRP A CZ2  1 
ATOM   3911  C  CZ3  . TRP A 1 237 ? 0.830   -1.067  22.465  1.00 6.50   ?  460  TRP A CZ3  1 
ATOM   3912  C  CH2  . TRP A 1 237 ? 0.182   -1.382  21.275  1.00 6.66   ?  460  TRP A CH2  1 
ATOM   3913  H  H    . TRP A 1 237 ? 3.845   4.622   20.879  1.00 6.67   ?  460  TRP A H    1 
ATOM   3914  H  HA   . TRP A 1 237 ? 1.718   4.952   22.373  1.00 6.18   ?  460  TRP A HA   1 
ATOM   3915  H  HB2  . TRP A 1 237 ? 3.595   2.876   22.402  1.00 6.95   ?  460  TRP A HB2  1 
ATOM   3916  H  HB3  . TRP A 1 237 ? 2.343   2.889   23.380  1.00 6.95   ?  460  TRP A HB3  1 
ATOM   3917  H  HD1  . TRP A 1 237 ? 1.677   3.689   19.879  1.00 7.16   ?  460  TRP A HD1  1 
ATOM   3918  H  HE1  . TRP A 1 237 ? 0.453   1.903   18.803  1.00 6.95   ?  460  TRP A HE1  1 
ATOM   3919  H  HE3  . TRP A 1 237 ? 1.869   0.348   23.441  1.00 7.12   ?  460  TRP A HE3  1 
ATOM   3920  H  HZ2  . TRP A 1 237 ? -0.330  -0.697  19.452  1.00 7.53   ?  460  TRP A HZ2  1 
ATOM   3921  H  HZ3  . TRP A 1 237 ? 0.857   -1.695  23.150  1.00 7.80   ?  460  TRP A HZ3  1 
ATOM   3922  H  HH2  . TRP A 1 237 ? -0.208  -2.220  21.178  1.00 8.00   ?  460  TRP A HH2  1 
ATOM   3923  N  N    . VAL A 1 238 ? 4.575   5.338   23.830  1.00 6.13   ?  461  VAL A N    1 
ATOM   3924  C  CA   . VAL A 1 238 ? 5.198   5.995   24.978  1.00 6.18   ?  461  VAL A CA   1 
ATOM   3925  C  C    . VAL A 1 238 ? 4.578   7.368   25.193  1.00 6.74   ?  461  VAL A C    1 
ATOM   3926  O  O    . VAL A 1 238 ? 4.164   7.724   26.296  1.00 7.34   ?  461  VAL A O    1 
ATOM   3927  C  CB   . VAL A 1 238 ? 6.724   6.095   24.788  1.00 6.69   ?  461  VAL A CB   1 
ATOM   3928  C  CG1  . VAL A 1 238 ? 7.367   6.955   25.892  1.00 7.46   ?  461  VAL A CG1  1 
ATOM   3929  C  CG2  . VAL A 1 238 ? 7.381   4.719   24.749  1.00 6.84   ?  461  VAL A CG2  1 
ATOM   3930  H  H    . VAL A 1 238 ? 5.129   5.032   23.247  1.00 7.36   ?  461  VAL A H    1 
ATOM   3931  H  HA   . VAL A 1 238 ? 5.030   5.457   25.768  1.00 7.42   ?  461  VAL A HA   1 
ATOM   3932  H  HB   . VAL A 1 238 ? 6.879   6.524   23.932  1.00 8.04   ?  461  VAL A HB   1 
ATOM   3933  H  HG11 . VAL A 1 238 ? 8.330   6.844   25.858  1.00 8.95   ?  461  VAL A HG11 1 
ATOM   3934  H  HG12 . VAL A 1 238 ? 7.136   7.885   25.743  1.00 8.95   ?  461  VAL A HG12 1 
ATOM   3935  H  HG13 . VAL A 1 238 ? 7.032   6.665   26.755  1.00 8.95   ?  461  VAL A HG13 1 
ATOM   3936  H  HG21 . VAL A 1 238 ? 8.339   4.830   24.646  1.00 8.21   ?  461  VAL A HG21 1 
ATOM   3937  H  HG22 . VAL A 1 238 ? 7.189   4.253   25.578  1.00 8.21   ?  461  VAL A HG22 1 
ATOM   3938  H  HG23 . VAL A 1 238 ? 7.024   4.219   23.998  1.00 8.21   ?  461  VAL A HG23 1 
ATOM   3939  N  N    . ALA A 1 239 ? 4.517   8.169   24.127  1.00 6.47   ?  462  ALA A N    1 
ATOM   3940  C  CA   . ALA A 1 239 ? 4.055   9.535   24.288  1.00 7.09   ?  462  ALA A CA   1 
ATOM   3941  C  C    . ALA A 1 239 ? 2.574   9.585   24.625  1.00 6.44   ?  462  ALA A C    1 
ATOM   3942  O  O    . ALA A 1 239 ? 2.138   10.477  25.363  1.00 7.26   ?  462  ALA A O    1 
ATOM   3943  C  CB   . ALA A 1 239 ? 4.301   10.325  23.009  1.00 8.56   ?  462  ALA A CB   1 
ATOM   3944  H  H    . ALA A 1 239 ? 4.732   7.947   23.325  1.00 7.76   ?  462  ALA A H    1 
ATOM   3945  H  HA   . ALA A 1 239 ? 4.556   9.944   25.011  1.00 8.51   ?  462  ALA A HA   1 
ATOM   3946  H  HB1  . ALA A 1 239 ? 3.985   11.233  23.133  1.00 10.28  ?  462  ALA A HB1  1 
ATOM   3947  H  HB2  . ALA A 1 239 ? 5.252   10.328  22.817  1.00 10.28  ?  462  ALA A HB2  1 
ATOM   3948  H  HB3  . ALA A 1 239 ? 3.818   9.904   22.280  1.00 10.28  ?  462  ALA A HB3  1 
ATOM   3949  N  N    . HIS A 1 240 ? 1.791   8.633   24.115  1.00 6.26   ?  463  HIS A N    1 
ATOM   3950  C  CA   . HIS A 1 240 ? 0.371   8.550   24.426  1.00 6.52   ?  463  HIS A CA   1 
ATOM   3951  C  C    . HIS A 1 240 ? 0.147   8.208   25.895  1.00 6.59   ?  463  HIS A C    1 
ATOM   3952  O  O    . HIS A 1 240 ? -0.610  8.898   26.594  1.00 7.08   ?  463  HIS A O    1 
ATOM   3953  C  CB   . HIS A 1 240 ? -0.255  7.508   23.514  1.00 6.91   ?  463  HIS A CB   1 
ATOM   3954  C  CG   . HIS A 1 240 ? -1.745  7.470   23.555  1.00 7.09   ?  463  HIS A CG   1 
ATOM   3955  N  ND1  . HIS A 1 240 ? -2.525  8.394   22.904  1.00 9.09   ?  463  HIS A ND1  1 
ATOM   3956  C  CD2  . HIS A 1 240 ? -2.597  6.610   24.159  1.00 7.32   ?  463  HIS A CD2  1 
ATOM   3957  C  CE1  . HIS A 1 240 ? -3.797  8.101   23.104  1.00 9.33   ?  463  HIS A CE1  1 
ATOM   3958  N  NE2  . HIS A 1 240 ? -3.867  7.025   23.861  1.00 8.14   ?  463  HIS A NE2  1 
ATOM   3959  H  H    . HIS A 1 240 ? 2.063   8.017   23.580  1.00 7.52   ?  463  HIS A H    1 
ATOM   3960  H  HA   . HIS A 1 240 ? -0.057  9.406   24.267  1.00 7.83   ?  463  HIS A HA   1 
ATOM   3961  H  HB2  . HIS A 1 240 ? 0.009   7.698   22.600  1.00 8.29   ?  463  HIS A HB2  1 
ATOM   3962  H  HB3  . HIS A 1 240 ? 0.068   6.632   23.777  1.00 8.29   ?  463  HIS A HB3  1 
ATOM   3963  H  HD2  . HIS A 1 240 ? -2.364  5.874   24.678  1.00 8.79   ?  463  HIS A HD2  1 
ATOM   3964  H  HE1  . HIS A 1 240 ? -4.523  8.575   22.766  1.00 11.20  ?  463  HIS A HE1  1 
ATOM   3965  H  HE2  . HIS A 1 240 ? -4.592  6.645   24.125  1.00 9.77   ?  463  HIS A HE2  1 
ATOM   3966  N  N    . PHE A 1 241 ? 0.780   7.137   26.386  1.00 6.23   ?  464  PHE A N    1 
ATOM   3967  C  CA   . PHE A 1 241 ? 0.573   6.743   27.776  1.00 6.54   ?  464  PHE A CA   1 
ATOM   3968  C  C    . PHE A 1 241 ? 1.089   7.819   28.725  1.00 5.95   ?  464  PHE A C    1 
ATOM   3969  O  O    . PHE A 1 241 ? 0.470   8.108   29.753  1.00 6.92   ?  464  PHE A O    1 
ATOM   3970  C  CB   . PHE A 1 241 ? 1.283   5.413   28.050  1.00 6.90   ?  464  PHE A CB   1 
ATOM   3971  C  CG   . PHE A 1 241 ? 0.834   4.257   27.174  1.00 6.57   ?  464  PHE A CG   1 
ATOM   3972  C  CD1  . PHE A 1 241 ? -0.434  4.202   26.627  1.00 7.80   ?  464  PHE A CD1  1 
ATOM   3973  C  CD2  . PHE A 1 241 ? 1.692   3.201   26.933  1.00 6.19   ?  464  PHE A CD2  1 
ATOM   3974  C  CE1  . PHE A 1 241 ? -0.826  3.107   25.843  1.00 8.09   ?  464  PHE A CE1  1 
ATOM   3975  C  CE2  . PHE A 1 241 ? 1.313   2.131   26.151  1.00 7.48   ?  464  PHE A CE2  1 
ATOM   3976  C  CZ   . PHE A 1 241 ? 0.048   2.091   25.597  1.00 7.73   ?  464  PHE A CZ   1 
ATOM   3977  H  H    . PHE A 1 241 ? 1.322   6.636   25.944  1.00 7.48   ?  464  PHE A H    1 
ATOM   3978  H  HA   . PHE A 1 241 ? -0.377  6.621   27.934  1.00 7.86   ?  464  PHE A HA   1 
ATOM   3979  H  HB2  . PHE A 1 241 ? 2.234   5.537   27.904  1.00 8.28   ?  464  PHE A HB2  1 
ATOM   3980  H  HB3  . PHE A 1 241 ? 1.119   5.161   28.972  1.00 8.28   ?  464  PHE A HB3  1 
ATOM   3981  H  HD1  . PHE A 1 241 ? -1.033  4.897   26.780  1.00 9.36   ?  464  PHE A HD1  1 
ATOM   3982  H  HD2  . PHE A 1 241 ? 2.544   3.213   27.306  1.00 7.43   ?  464  PHE A HD2  1 
ATOM   3983  H  HE1  . PHE A 1 241 ? -1.686  3.075   25.490  1.00 9.71   ?  464  PHE A HE1  1 
ATOM   3984  H  HE2  . PHE A 1 241 ? 1.910   1.435   25.996  1.00 8.98   ?  464  PHE A HE2  1 
ATOM   3985  H  HZ   . PHE A 1 241 ? -0.205  1.375   25.060  1.00 9.27   ?  464  PHE A HZ   1 
ATOM   3986  N  N    . TYR A 1 242 ? 2.236   8.414   28.391  1.00 6.28   ?  465  TYR A N    1 
ATOM   3987  C  CA   . TYR A 1 242 ? 2.808   9.476   29.211  1.00 7.21   ?  465  TYR A CA   1 
ATOM   3988  C  C    . TYR A 1 242 ? 1.821   10.618  29.390  1.00 7.33   ?  465  TYR A C    1 
ATOM   3989  O  O    . TYR A 1 242 ? 1.636   11.122  30.500  1.00 8.33   ?  465  TYR A O    1 
ATOM   3990  C  CB   . TYR A 1 242 ? 4.083   9.968   28.539  1.00 7.88   ?  465  TYR A CB   1 
ATOM   3991  C  CG   . TYR A 1 242 ? 4.762   11.150  29.160  1.00 8.74   ?  465  TYR A CG   1 
ATOM   3992  C  CD1  . TYR A 1 242 ? 5.530   11.016  30.305  1.00 9.52   ?  465  TYR A CD1  1 
ATOM   3993  C  CD2  . TYR A 1 242 ? 4.686   12.406  28.564  1.00 10.78  ?  465  TYR A CD2  1 
ATOM   3994  C  CE1  . TYR A 1 242 ? 6.197   12.094  30.846  1.00 10.82  ?  465  TYR A CE1  1 
ATOM   3995  C  CE2  . TYR A 1 242 ? 5.353   13.487  29.097  1.00 12.29  ?  465  TYR A CE2  1 
ATOM   3996  C  CZ   . TYR A 1 242 ? 6.100   13.326  30.247  1.00 12.10  ?  465  TYR A CZ   1 
ATOM   3997  O  OH   . TYR A 1 242 ? 6.793   14.374  30.805  1.00 15.11  ?  465  TYR A OH   1 
ATOM   3998  H  H    . TYR A 1 242 ? 2.702   8.220   27.694  1.00 7.53   ?  465  TYR A H    1 
ATOM   3999  H  HA   . TYR A 1 242 ? 3.025   9.136   30.093  1.00 8.66   ?  465  TYR A HA   1 
ATOM   4000  H  HB2  . TYR A 1 242 ? 4.723   9.240   28.542  1.00 9.46   ?  465  TYR A HB2  1 
ATOM   4001  H  HB3  . TYR A 1 242 ? 3.865   10.214  27.627  1.00 9.46   ?  465  TYR A HB3  1 
ATOM   4002  H  HD1  . TYR A 1 242 ? 5.596   10.184  30.716  1.00 11.43  ?  465  TYR A HD1  1 
ATOM   4003  H  HD2  . TYR A 1 242 ? 4.176   12.517  27.794  1.00 12.93  ?  465  TYR A HD2  1 
ATOM   4004  H  HE1  . TYR A 1 242 ? 6.712   11.988  31.613  1.00 12.98  ?  465  TYR A HE1  1 
ATOM   4005  H  HE2  . TYR A 1 242 ? 5.301   14.320  28.686  1.00 14.76  ?  465  TYR A HE2  1 
ATOM   4006  H  HH   . TYR A 1 242 ? 6.697   15.064  30.336  1.00 18.13  ?  465  TYR A HH   1 
ATOM   4007  N  N    . GLN A 1 243 ? 1.155   11.031  28.311  1.00 7.27   ?  466  GLN A N    1 
ATOM   4008  C  CA   . GLN A 1 243 ? 0.192   12.116  28.407  1.00 7.55   ?  466  GLN A CA   1 
ATOM   4009  C  C    . GLN A 1 243 ? -1.110  11.680  29.055  1.00 7.57   ?  466  GLN A C    1 
ATOM   4010  O  O    . GLN A 1 243 ? -1.682  12.420  29.852  1.00 8.82   ?  466  GLN A O    1 
ATOM   4011  C  CB   . GLN A 1 243 ? -0.142  12.654  27.021  1.00 7.98   ?  466  GLN A CB   1 
ATOM   4012  C  CG   . GLN A 1 243 ? 0.984   13.365  26.330  1.00 7.76   ?  466  GLN A CG   1 
ATOM   4013  C  CD   . GLN A 1 243 ? 0.560   13.847  24.972  1.00 8.29   ?  466  GLN A CD   1 
ATOM   4014  O  OE1  . GLN A 1 243 ? -0.060  14.902  24.845  1.00 8.72   ?  466  GLN A OE1  1 
ATOM   4015  N  NE2  . GLN A 1 243 ? 0.854   13.055  23.947  1.00 9.24   ?  466  GLN A NE2  1 
ATOM   4016  H  H    . GLN A 1 243 ? 1.244   10.700  27.522  1.00 8.73   ?  466  GLN A H    1 
ATOM   4017  H  HA   . GLN A 1 243 ? 0.604   12.809  28.947  1.00 9.06   ?  466  GLN A HA   1 
ATOM   4018  H  HB2  . GLN A 1 243 ? -0.405  11.909  26.458  1.00 9.58   ?  466  GLN A HB2  1 
ATOM   4019  H  HB3  . GLN A 1 243 ? -0.876  13.282  27.104  1.00 9.58   ?  466  GLN A HB3  1 
ATOM   4020  H  HG2  . GLN A 1 243 ? 1.255   14.132  26.858  1.00 9.31   ?  466  GLN A HG2  1 
ATOM   4021  H  HG3  . GLN A 1 243 ? 1.732   12.757  26.221  1.00 9.31   ?  466  GLN A HG3  1 
ATOM   4022  H  HE21 . GLN A 1 243 ? 1.266   12.311  24.082  1.00 11.09  ?  466  GLN A HE21 1 
ATOM   4023  H  HE22 . GLN A 1 243 ? 0.633   13.285  23.148  1.00 11.09  ?  466  GLN A HE22 1 
ATOM   4024  N  N    . GLU A 1 244 ? -1.638  10.524  28.654  1.00 7.24   ?  467  GLU A N    1 
ATOM   4025  C  CA   . GLU A 1 244 ? -2.946  10.092  29.137  1.00 8.34   ?  467  GLU A CA   1 
ATOM   4026  C  C    . GLU A 1 244 ? -2.912  9.744   30.620  1.00 8.23   ?  467  GLU A C    1 
ATOM   4027  O  O    . GLU A 1 244 ? -3.814  10.122  31.380  1.00 8.92   ?  467  GLU A O    1 
ATOM   4028  C  CB   . GLU A 1 244 ? -3.414  8.890   28.325  1.00 8.53   ?  467  GLU A CB   1 
ATOM   4029  C  CG   . GLU A 1 244 ? -3.862  9.246   26.932  1.00 9.91   ?  467  GLU A CG   1 
ATOM   4030  C  CD   . GLU A 1 244 ? -5.135  10.068  26.952  1.00 11.66  ?  467  GLU A CD   1 
ATOM   4031  O  OE1  . GLU A 1 244 ? -6.148  9.580   27.498  1.00 12.13  ?  467  GLU A OE1  1 
ATOM   4032  O  OE2  . GLU A 1 244 ? -5.109  11.209  26.445  1.00 13.72  -1 467  GLU A OE2  1 
ATOM   4033  H  H    . GLU A 1 244 ? -1.263  9.977   28.107  1.00 8.69   ?  467  GLU A H    1 
ATOM   4034  H  HA   . GLU A 1 244 ? -3.576  10.820  29.019  1.00 10.02  ?  467  GLU A HA   1 
ATOM   4035  H  HB2  . GLU A 1 244 ? -2.682  8.258   28.249  1.00 10.23  ?  467  GLU A HB2  1 
ATOM   4036  H  HB3  . GLU A 1 244 ? -4.163  8.476   28.781  1.00 10.23  ?  467  GLU A HB3  1 
ATOM   4037  H  HG2  . GLU A 1 244 ? -3.169  9.767   26.495  1.00 11.89  ?  467  GLU A HG2  1 
ATOM   4038  H  HG3  . GLU A 1 244 ? -4.031  8.433   26.430  1.00 11.89  ?  467  GLU A HG3  1 
ATOM   4039  N  N    . SER A 1 245 ? -1.891  9.001   31.047  1.00 8.71   ?  468  SER A N    1 
ATOM   4040  C  CA   . SER A 1 245 ? -1.788  8.515   32.421  1.00 10.24  ?  468  SER A CA   1 
ATOM   4041  C  C    . SER A 1 245 ? -3.111  7.945   32.922  1.00 9.45   ?  468  SER A C    1 
ATOM   4042  O  O    . SER A 1 245 ? -3.563  8.220   34.037  1.00 11.29  ?  468  SER A O    1 
ATOM   4043  C  CB   . SER A 1 245 ? -1.269  9.610   33.345  1.00 12.35  ?  468  SER A CB   1 
ATOM   4044  O  OG   . SER A 1 245 ? 0.004   10.054  32.928  1.00 14.75  ?  468  SER A OG   1 
ATOM   4045  H  H    . SER A 1 245 ? -1.233  8.761   30.549  1.00 10.45  ?  468  SER A H    1 
ATOM   4046  H  HA   . SER A 1 245 ? -1.149  7.784   32.431  1.00 12.29  ?  468  SER A HA   1 
ATOM   4047  H  HB2  . SER A 1 245 ? -1.886  10.358  33.328  1.00 14.82  ?  468  SER A HB2  1 
ATOM   4048  H  HB3  . SER A 1 245 ? -1.201  9.257   34.246  1.00 14.82  ?  468  SER A HB3  1 
ATOM   4049  H  HG   . SER A 1 245 ? 0.277   10.664  33.438  1.00 17.70  ?  468  SER A HG   1 
ATOM   4050  N  N    . ALA A 1 246 ? -3.718  7.095   32.108  1.00 8.81   ?  469  ALA A N    1 
ATOM   4051  C  CA   . ALA A 1 246 ? -4.967  6.484   32.529  1.00 9.51   ?  469  ALA A CA   1 
ATOM   4052  C  C    . ALA A 1 246 ? -4.687  5.430   33.596  1.00 10.44  ?  469  ALA A C    1 
ATOM   4053  O  O    . ALA A 1 246 ? -3.715  4.687   33.482  1.00 10.19  ?  469  ALA A O    1 
ATOM   4054  C  CB   . ALA A 1 246 ? -5.671  5.819   31.350  1.00 10.18  ?  469  ALA A CB   1 
ATOM   4055  H  H    . ALA A 1 246 ? -3.436  6.862   31.329  1.00 10.57  ?  469  ALA A H    1 
ATOM   4056  H  HA   . ALA A 1 246 ? -5.552  7.167   32.891  1.00 11.41  ?  469  ALA A HA   1 
ATOM   4057  H  HB1  . ALA A 1 246 ? -6.497  5.418   31.662  1.00 12.22  ?  469  ALA A HB1  1 
ATOM   4058  H  HB2  . ALA A 1 246 ? -5.862  6.491   30.677  1.00 12.22  ?  469  ALA A HB2  1 
ATOM   4059  H  HB3  . ALA A 1 246 ? -5.090  5.136   30.980  1.00 12.22  ?  469  ALA A HB3  1 
ATOM   4060  N  N    . PRO A 1 247 ? -5.526  5.328   34.629  1.00 11.50  ?  470  PRO A N    1 
ATOM   4061  C  CA   . PRO A 1 247 ? -5.295  4.306   35.658  1.00 12.13  ?  470  PRO A CA   1 
ATOM   4062  C  C    . PRO A 1 247 ? -5.382  2.900   35.081  1.00 12.02  ?  470  PRO A C    1 
ATOM   4063  O  O    . PRO A 1 247 ? -6.291  2.575   34.312  1.00 13.78  ?  470  PRO A O    1 
ATOM   4064  C  CB   . PRO A 1 247 ? -6.423  4.557   36.669  1.00 14.23  ?  470  PRO A CB   1 
ATOM   4065  C  CG   . PRO A 1 247 ? -6.848  5.939   36.464  1.00 15.23  ?  470  PRO A CG   1 
ATOM   4066  C  CD   . PRO A 1 247 ? -6.619  6.245   35.006  1.00 12.58  ?  470  PRO A CD   1 
ATOM   4067  H  HA   . PRO A 1 247 ? -4.431  4.437   36.077  1.00 14.56  ?  470  PRO A HA   1 
ATOM   4068  H  HB2  . PRO A 1 247 ? -7.156  3.944   36.499  1.00 17.08  ?  470  PRO A HB2  1 
ATOM   4069  H  HB3  . PRO A 1 247 ? -6.088  4.431   37.570  1.00 17.08  ?  470  PRO A HB3  1 
ATOM   4070  H  HG2  . PRO A 1 247 ? -7.787  6.026   36.688  1.00 18.27  ?  470  PRO A HG2  1 
ATOM   4071  H  HG3  . PRO A 1 247 ? -6.317  6.528   37.023  1.00 18.27  ?  470  PRO A HG3  1 
ATOM   4072  H  HD2  . PRO A 1 247 ? -7.417  6.061   34.487  1.00 15.10  ?  470  PRO A HD2  1 
ATOM   4073  H  HD3  . PRO A 1 247 ? -6.351  7.169   34.886  1.00 15.10  ?  470  PRO A HD3  1 
ATOM   4074  N  N    . ALA A 1 248 ? -4.419  2.063   35.467  1.00 10.99  ?  471  ALA A N    1 
ATOM   4075  C  CA   . ALA A 1 248 ? -4.406  0.653   35.089  1.00 11.22  ?  471  ALA A CA   1 
ATOM   4076  C  C    . ALA A 1 248 ? -5.301  -0.082  36.072  1.00 11.17  ?  471  ALA A C    1 
ATOM   4077  O  O    . ALA A 1 248 ? -4.912  -0.352  37.214  1.00 13.12  ?  471  ALA A O    1 
ATOM   4078  C  CB   . ALA A 1 248 ? -2.992  0.099   35.132  1.00 12.41  ?  471  ALA A CB   1 
ATOM   4079  H  H    . ALA A 1 248 ? -3.750  2.294   35.956  1.00 13.19  ?  471  ALA A H    1 
ATOM   4080  H  HA   . ALA A 1 248 ? -4.750  0.547   34.188  1.00 13.46  ?  471  ALA A HA   1 
ATOM   4081  H  HB1  . ALA A 1 248 ? -3.010  -0.833  34.863  1.00 14.89  ?  471  ALA A HB1  1 
ATOM   4082  H  HB2  . ALA A 1 248 ? -2.435  0.608   34.523  1.00 14.89  ?  471  ALA A HB2  1 
ATOM   4083  H  HB3  . ALA A 1 248 ? -2.650  0.175   36.036  1.00 14.89  ?  471  ALA A HB3  1 
ATOM   4084  N  N    . GLN A 1 249 ? -6.510  -0.420  35.631  1.00 10.31  ?  472  GLN A N    1 
ATOM   4085  C  CA   A GLN A 1 249 ? -7.479  -0.982  36.566  0.69 10.81  ?  472  GLN A CA   1 
ATOM   4086  C  CA   B GLN A 1 249 ? -7.498  -0.991  36.545  0.31 10.85  ?  472  GLN A CA   1 
ATOM   4087  C  C    . GLN A 1 249 ? -7.117  -2.399  36.980  1.00 10.24  ?  472  GLN A C    1 
ATOM   4088  O  O    . GLN A 1 249 ? -7.497  -2.835  38.073  1.00 12.08  ?  472  GLN A O    1 
ATOM   4089  C  CB   A GLN A 1 249 ? -8.872  -0.907  35.961  0.69 11.28  ?  472  GLN A CB   1 
ATOM   4090  C  CB   B GLN A 1 249 ? -8.876  -0.987  35.885  0.31 11.76  ?  472  GLN A CB   1 
ATOM   4091  C  CG   A GLN A 1 249 ? -9.289  0.529   35.707  0.69 13.97  ?  472  GLN A CG   1 
ATOM   4092  C  CG   B GLN A 1 249 ? -9.375  0.400   35.502  0.31 13.53  ?  472  GLN A CG   1 
ATOM   4093  C  CD   A GLN A 1 249 ? -10.716 0.668   35.255  0.69 15.84  ?  472  GLN A CD   1 
ATOM   4094  C  CD   B GLN A 1 249 ? -9.533  1.309   36.701  0.31 15.11  ?  472  GLN A CD   1 
ATOM   4095  O  OE1  A GLN A 1 249 ? -11.582 -0.145  35.602  0.69 17.33  ?  472  GLN A OE1  1 
ATOM   4096  O  OE1  B GLN A 1 249 ? -8.970  2.402   36.746  0.31 16.15  ?  472  GLN A OE1  1 
ATOM   4097  N  NE2  A GLN A 1 249 ? -10.977 1.709   34.479  0.69 15.84  ?  472  GLN A NE2  1 
ATOM   4098  N  NE2  B GLN A 1 249 ? -10.299 0.859   37.683  0.31 15.53  ?  472  GLN A NE2  1 
ATOM   4099  H  H    A GLN A 1 249 ? -6.786  -0.336  34.821  0.69 12.37  ?  472  GLN A H    1 
ATOM   4100  H  H    B GLN A 1 249 ? -6.782  -0.330  34.820  0.31 12.37  ?  472  GLN A H    1 
ATOM   4101  H  HA   A GLN A 1 249 ? -7.487  -0.454  37.380  0.69 12.98  ?  472  GLN A HA   1 
ATOM   4102  H  HA   B GLN A 1 249 ? -7.544  -0.440  37.342  0.31 13.03  ?  472  GLN A HA   1 
ATOM   4103  H  HB2  A GLN A 1 249 ? -8.881  -1.382  35.116  0.69 13.54  ?  472  GLN A HB2  1 
ATOM   4104  H  HB2  B GLN A 1 249 ? -8.835  -1.521  35.076  0.31 14.11  ?  472  GLN A HB2  1 
ATOM   4105  H  HB3  A GLN A 1 249 ? -9.510  -1.307  36.573  0.69 13.54  ?  472  GLN A HB3  1 
ATOM   4106  H  HB3  B GLN A 1 249 ? -9.517  -1.372  36.503  0.31 14.11  ?  472  GLN A HB3  1 
ATOM   4107  H  HG2  A GLN A 1 249 ? -9.188  1.035   36.529  0.69 16.76  ?  472  GLN A HG2  1 
ATOM   4108  H  HG2  B GLN A 1 249 ? -8.738  0.810   34.896  0.31 16.23  ?  472  GLN A HG2  1 
ATOM   4109  H  HG3  A GLN A 1 249 ? -8.721  0.903   35.016  0.69 16.76  ?  472  GLN A HG3  1 
ATOM   4110  H  HG3  B GLN A 1 249 ? -10.239 0.318   35.070  0.31 16.23  ?  472  GLN A HG3  1 
ATOM   4111  H  HE21 A GLN A 1 249 ? -10.347 2.254   34.265  0.69 19.01  ?  472  GLN A HE21 1 
ATOM   4112  H  HE21 B GLN A 1 249 ? -10.674 0.088   37.617  0.31 18.64  ?  472  GLN A HE21 1 
ATOM   4113  H  HE22 A GLN A 1 249 ? -11.776 1.840   34.189  0.69 19.01  ?  472  GLN A HE22 1 
ATOM   4114  H  HE22 B GLN A 1 249 ? -10.421 1.337   38.387  0.31 18.64  ?  472  GLN A HE22 1 
ATOM   4115  N  N    . THR A 1 250 ? -6.404  -3.131  36.134  1.00 9.73   ?  473  THR A N    1 
ATOM   4116  C  CA   . THR A 1 250 ? -5.711  -4.355  36.500  1.00 9.30   ?  473  THR A CA   1 
ATOM   4117  C  C    . THR A 1 250 ? -4.323  -4.244  35.881  1.00 8.86   ?  473  THR A C    1 
ATOM   4118  O  O    . THR A 1 250 ? -3.984  -3.238  35.256  1.00 9.45   ?  473  THR A O    1 
ATOM   4119  C  CB   . THR A 1 250 ? -6.393  -5.618  35.968  1.00 9.33   ?  473  THR A CB   1 
ATOM   4120  O  OG1  . THR A 1 250 ? -6.247  -5.625  34.544  1.00 9.61   ?  473  THR A OG1  1 
ATOM   4121  C  CG2  . THR A 1 250 ? -7.860  -5.675  36.382  1.00 10.68  ?  473  THR A CG2  1 
ATOM   4122  H  H    . THR A 1 250 ? -6.302  -2.927  35.304  1.00 11.68  ?  473  THR A H    1 
ATOM   4123  H  HA   . THR A 1 250 ? -5.684  -4.431  37.467  1.00 11.16  ?  473  THR A HA   1 
ATOM   4124  H  HB   . THR A 1 250 ? -5.984  -6.415  36.339  1.00 11.20  ?  473  THR A HB   1 
ATOM   4125  H  HG1  . THR A 1 250 ? -6.605  -6.313  34.222  1.00 11.53  ?  473  THR A HG1  1 
ATOM   4126  H  HG21 . THR A 1 250 ? -8.278  -6.469  36.013  1.00 12.82  ?  473  THR A HG21 1 
ATOM   4127  H  HG22 . THR A 1 250 ? -7.931  -5.703  37.349  1.00 12.82  ?  473  THR A HG22 1 
ATOM   4128  H  HG23 . THR A 1 250 ? -8.329  -4.891  36.055  1.00 12.82  ?  473  THR A HG23 1 
ATOM   4129  N  N    . ASP A 1 251 ? -3.514  -5.274  36.053  1.00 8.76   ?  474  ASP A N    1 
ATOM   4130  C  CA   . ASP A 1 251 ? -2.157  -5.230  35.542  1.00 8.63   ?  474  ASP A CA   1 
ATOM   4131  C  C    . ASP A 1 251 ? -2.038  -5.795  34.132  1.00 8.31   ?  474  ASP A C    1 
ATOM   4132  O  O    . ASP A 1 251 ? -0.924  -5.840  33.593  1.00 8.39   ?  474  ASP A O    1 
ATOM   4133  C  CB   . ASP A 1 251 ? -1.190  -5.921  36.496  1.00 10.59  ?  474  ASP A CB   1 
ATOM   4134  C  CG   . ASP A 1 251 ? -0.984  -5.146  37.800  1.00 12.93  ?  474  ASP A CG   1 
ATOM   4135  O  OD1  . ASP A 1 251 ? -1.418  -3.983  37.902  1.00 13.09  ?  474  ASP A OD1  1 
ATOM   4136  O  OD2  . ASP A 1 251 ? -0.381  -5.704  38.739  1.00 15.29  -1 474  ASP A OD2  1 
ATOM   4137  H  H    . ASP A 1 251 ? -3.726  -6.003  36.457  1.00 10.51  ?  474  ASP A H    1 
ATOM   4138  H  HA   . ASP A 1 251 ? -1.873  -4.303  35.502  1.00 10.36  ?  474  ASP A HA   1 
ATOM   4139  H  HB2  . ASP A 1 251 ? -1.541  -6.797  36.721  1.00 12.71  ?  474  ASP A HB2  1 
ATOM   4140  H  HB3  . ASP A 1 251 ? -0.328  -6.011  36.061  1.00 12.71  ?  474  ASP A HB3  1 
ATOM   4141  N  N    . VAL A 1 252 ? -3.148  -6.188  33.505  1.00 8.11   ?  475  VAL A N    1 
ATOM   4142  C  CA   . VAL A 1 252 ? -3.108  -6.710  32.142  1.00 8.38   ?  475  VAL A CA   1 
ATOM   4143  C  C    . VAL A 1 252 ? -4.304  -6.186  31.364  1.00 7.59   ?  475  VAL A C    1 
ATOM   4144  O  O    . VAL A 1 252 ? -5.450  -6.423  31.746  1.00 8.97   ?  475  VAL A O    1 
ATOM   4145  C  CB   . VAL A 1 252 ? -3.118  -8.245  32.094  1.00 9.27   ?  475  VAL A CB   1 
ATOM   4146  C  CG1  . VAL A 1 252 ? -3.000  -8.714  30.655  1.00 10.16  ?  475  VAL A CG1  1 
ATOM   4147  C  CG2  . VAL A 1 252 ? -1.980  -8.817  32.932  1.00 9.20   ?  475  VAL A CG2  1 
ATOM   4148  H  H    . VAL A 1 252 ? -3.935  -6.162  33.850  1.00 9.74   ?  475  VAL A H    1 
ATOM   4149  H  HA   . VAL A 1 252 ? -2.297  -6.377  31.726  1.00 10.06  ?  475  VAL A HA   1 
ATOM   4150  H  HB   . VAL A 1 252 ? -3.954  -8.569  32.463  1.00 11.13  ?  475  VAL A HB   1 
ATOM   4151  H  HG11 . VAL A 1 252 ? -2.802  -9.663  30.647  1.00 12.20  ?  475  VAL A HG11 1 
ATOM   4152  H  HG12 . VAL A 1 252 ? -3.840  -8.547  30.199  1.00 12.20  ?  475  VAL A HG12 1 
ATOM   4153  H  HG13 . VAL A 1 252 ? -2.285  -8.223  30.221  1.00 12.20  ?  475  VAL A HG13 1 
ATOM   4154  H  HG21 . VAL A 1 252 ? -1.967  -9.782  32.831  1.00 11.04  ?  475  VAL A HG21 1 
ATOM   4155  H  HG22 . VAL A 1 252 ? -1.140  -8.441  32.623  1.00 11.04  ?  475  VAL A HG22 1 
ATOM   4156  H  HG23 . VAL A 1 252 ? -2.124  -8.584  33.862  1.00 11.04  ?  475  VAL A HG23 1 
ATOM   4157  N  N    . ALA A 1 253 ? -4.035  -5.507  30.262  1.00 7.51   ?  476  ALA A N    1 
ATOM   4158  C  CA   . ALA A 1 253 ? -5.053  -5.070  29.322  1.00 8.25   ?  476  ALA A CA   1 
ATOM   4159  C  C    . ALA A 1 253 ? -5.158  -6.075  28.179  1.00 8.20   ?  476  ALA A C    1 
ATOM   4160  O  O    . ALA A 1 253 ? -4.153  -6.412  27.552  1.00 8.98   ?  476  ALA A O    1 
ATOM   4161  C  CB   . ALA A 1 253 ? -4.661  -3.705  28.758  1.00 8.98   ?  476  ALA A CB   1 
ATOM   4162  H  H    . ALA A 1 253 ? -3.240  -5.279  30.026  1.00 9.01   ?  476  ALA A H    1 
ATOM   4163  H  HA   . ALA A 1 253 ? -5.916  -5.012  29.763  1.00 9.91   ?  476  ALA A HA   1 
ATOM   4164  H  HB1  . ALA A 1 253 ? -5.319  -3.436  28.097  1.00 10.78  ?  476  ALA A HB1  1 
ATOM   4165  H  HB2  . ALA A 1 253 ? -4.636  -3.060  29.481  1.00 10.78  ?  476  ALA A HB2  1 
ATOM   4166  H  HB3  . ALA A 1 253 ? -3.786  -3.774  28.345  1.00 10.78  ?  476  ALA A HB3  1 
ATOM   4167  N  N    . LEU A 1 254 ? -6.364  -6.559  27.919  1.00 7.48   ?  477  LEU A N    1 
ATOM   4168  C  CA   . LEU A 1 254 ? -6.611  -7.387  26.744  1.00 7.44   ?  477  LEU A CA   1 
ATOM   4169  C  C    . LEU A 1 254 ? -6.772  -6.456  25.559  1.00 7.45   ?  477  LEU A C    1 
ATOM   4170  O  O    . LEU A 1 254 ? -7.608  -5.544  25.597  1.00 8.05   ?  477  LEU A O    1 
ATOM   4171  C  CB   . LEU A 1 254 ? -7.872  -8.223  26.938  1.00 8.53   ?  477  LEU A CB   1 
ATOM   4172  C  CG   . LEU A 1 254 ? -8.222  -9.157  25.778  1.00 9.64   ?  477  LEU A CG   1 
ATOM   4173  C  CD1  . LEU A 1 254 ? -7.163  -10.224 25.549  1.00 10.36  ?  477  LEU A CD1  1 
ATOM   4174  C  CD2  . LEU A 1 254 ? -9.574  -9.832  26.023  1.00 10.68  ?  477  LEU A CD2  1 
ATOM   4175  H  H    . LEU A 1 254 ? -7.058  -6.424  28.408  1.00 8.98   ?  477  LEU A H    1 
ATOM   4176  H  HA   . LEU A 1 254 ? -5.872  -7.996  26.592  1.00 8.93   ?  477  LEU A HA   1 
ATOM   4177  H  HB2  . LEU A 1 254 ? -7.755  -8.773  27.728  1.00 10.24  ?  477  LEU A HB2  1 
ATOM   4178  H  HB3  . LEU A 1 254 ? -8.622  -7.620  27.061  1.00 10.24  ?  477  LEU A HB3  1 
ATOM   4179  H  HG   . LEU A 1 254 ? -8.268  -8.613  24.976  1.00 11.57  ?  477  LEU A HG   1 
ATOM   4180  H  HD11 . LEU A 1 254 ? -7.473  -10.834 24.861  1.00 12.44  ?  477  LEU A HD11 1 
ATOM   4181  H  HD12 . LEU A 1 254 ? -6.340  -9.796  25.265  1.00 12.44  ?  477  LEU A HD12 1 
ATOM   4182  H  HD13 . LEU A 1 254 ? -7.016  -10.707 26.377  1.00 12.44  ?  477  LEU A HD13 1 
ATOM   4183  H  HD21 . LEU A 1 254 ? -9.768  -10.428 25.283  1.00 12.82  ?  477  LEU A HD21 1 
ATOM   4184  H  HD22 . LEU A 1 254 ? -9.530  -10.335 26.851  1.00 12.82  ?  477  LEU A HD22 1 
ATOM   4185  H  HD23 . LEU A 1 254 ? -10.261 -9.149  26.087  1.00 12.82  ?  477  LEU A HD23 1 
ATOM   4186  N  N    . ILE A 1 255 ? -5.959  -6.674  24.522  1.00 7.28   ?  478  ILE A N    1 
ATOM   4187  C  CA   . ILE A 1 255 ? -5.948  -5.835  23.331  1.00 7.15   ?  478  ILE A CA   1 
ATOM   4188  C  C    . ILE A 1 255 ? -6.183  -6.724  22.120  1.00 7.32   ?  478  ILE A C    1 
ATOM   4189  O  O    . ILE A 1 255 ? -5.788  -7.890  22.094  1.00 7.71   ?  478  ILE A O    1 
ATOM   4190  C  CB   . ILE A 1 255 ? -4.646  -4.999  23.215  1.00 7.40   ?  478  ILE A CB   1 
ATOM   4191  C  CG1  . ILE A 1 255 ? -3.409  -5.869  23.021  1.00 7.56   ?  478  ILE A CG1  1 
ATOM   4192  C  CG2  . ILE A 1 255 ? -4.505  -4.130  24.464  1.00 7.92   ?  478  ILE A CG2  1 
ATOM   4193  C  CD1  . ILE A 1 255 ? -2.121  -5.083  22.753  1.00 7.56   ?  478  ILE A CD1  1 
ATOM   4194  H  H    . ILE A 1 255 ? -5.391  -7.319  24.489  1.00 8.74   ?  478  ILE A H    1 
ATOM   4195  H  HA   . ILE A 1 255 ? -6.680  -5.199  23.367  1.00 8.58   ?  478  ILE A HA   1 
ATOM   4196  H  HB   . ILE A 1 255 ? -4.714  -4.443  22.424  1.00 8.88   ?  478  ILE A HB   1 
ATOM   4197  H  HG12 . ILE A 1 255 ? -3.270  -6.395  23.824  1.00 9.07   ?  478  ILE A HG12 1 
ATOM   4198  H  HG13 . ILE A 1 255 ? -3.558  -6.456  22.263  1.00 9.07   ?  478  ILE A HG13 1 
ATOM   4199  H  HG21 . ILE A 1 255 ? -3.741  -3.543  24.356  1.00 9.51   ?  478  ILE A HG21 1 
ATOM   4200  H  HG22 . ILE A 1 255 ? -5.313  -3.604  24.574  1.00 9.51   ?  478  ILE A HG22 1 
ATOM   4201  H  HG23 . ILE A 1 255 ? -4.376  -4.703  25.235  1.00 9.51   ?  478  ILE A HG23 1 
ATOM   4202  H  HD11 . ILE A 1 255 ? -1.406  -5.707  22.550  1.00 9.08   ?  478  ILE A HD11 1 
ATOM   4203  H  HD12 . ILE A 1 255 ? -2.265  -4.489  22.000  1.00 9.08   ?  478  ILE A HD12 1 
ATOM   4204  H  HD13 . ILE A 1 255 ? -1.896  -4.567  23.543  1.00 9.08   ?  478  ILE A HD13 1 
ATOM   4205  N  N    . ARG A 1 256 ? -6.846  -6.164  21.116  1.00 7.63   ?  479  ARG A N    1 
ATOM   4206  C  CA   . ARG A 1 256 ? -7.123  -6.884  19.889  1.00 8.11   ?  479  ARG A CA   1 
ATOM   4207  C  C    . ARG A 1 256 ? -6.558  -6.097  18.715  1.00 7.61   ?  479  ARG A C    1 
ATOM   4208  O  O    . ARG A 1 256 ? -6.696  -4.875  18.652  1.00 7.98   ?  479  ARG A O    1 
ATOM   4209  C  CB   . ARG A 1 256 ? -8.635  -7.054  19.681  1.00 10.28  ?  479  ARG A CB   1 
ATOM   4210  C  CG   . ARG A 1 256 ? -9.235  -8.337  20.213  1.00 12.86  ?  479  ARG A CG   1 
ATOM   4211  C  CD   . ARG A 1 256 ? -9.208  -8.427  21.712  1.00 14.24  ?  479  ARG A CD   1 
ATOM   4212  N  NE   . ARG A 1 256 ? -9.832  -9.661  22.182  1.00 15.26  ?  479  ARG A NE   1 
ATOM   4213  C  CZ   . ARG A 1 256 ? -11.118 -9.798  22.472  1.00 17.42  ?  479  ARG A CZ   1 
ATOM   4214  N  NH1  . ARG A 1 256 ? -11.966 -8.784  22.364  1.00 19.74  ?  479  ARG A NH1  1 
ATOM   4215  N  NH2  . ARG A 1 256 ? -11.563 -10.979 22.886  1.00 18.17  ?  479  ARG A NH2  1 
ATOM   4216  H  H    . ARG A 1 256 ? -7.148  -5.358  21.126  1.00 9.15   ?  479  ARG A H    1 
ATOM   4217  H  HA   . ARG A 1 256 ? -6.708  -7.760  19.923  1.00 9.73   ?  479  ARG A HA   1 
ATOM   4218  H  HB2  . ARG A 1 256 ? -9.087  -6.320  20.126  1.00 12.33  ?  479  ARG A HB2  1 
ATOM   4219  H  HB3  . ARG A 1 256 ? -8.815  -7.026  18.728  1.00 12.33  ?  479  ARG A HB3  1 
ATOM   4220  H  HG2  . ARG A 1 256 ? -10.161 -8.394  19.928  1.00 15.44  ?  479  ARG A HG2  1 
ATOM   4221  H  HG3  . ARG A 1 256 ? -8.733  -9.089  19.861  1.00 15.44  ?  479  ARG A HG3  1 
ATOM   4222  H  HD2  . ARG A 1 256 ? -8.288  -8.414  22.018  1.00 17.09  ?  479  ARG A HD2  1 
ATOM   4223  H  HD3  . ARG A 1 256 ? -9.693  -7.677  22.088  1.00 17.09  ?  479  ARG A HD3  1 
ATOM   4224  H  HE   . ARG A 1 256 ? -9.327  -10.351 22.278  1.00 18.32  ?  479  ARG A HE   1 
ATOM   4225  H  HH11 . ARG A 1 256 ? -11.685 -8.015  22.099  1.00 23.69  ?  479  ARG A HH11 1 
ATOM   4226  H  HH12 . ARG A 1 256 ? -12.796 -8.895  22.557  1.00 23.69  ?  479  ARG A HH12 1 
ATOM   4227  H  HH21 . ARG A 1 256 ? -11.020 -11.641 22.962  1.00 21.81  ?  479  ARG A HH21 1 
ATOM   4228  H  HH22 . ARG A 1 256 ? -12.395 -11.082 23.078  1.00 21.81  ?  479  ARG A HH22 1 
ATOM   4229  N  N    . TYR A 1 257 ? -5.930  -6.798  17.784  1.00 8.03   ?  480  TYR A N    1 
ATOM   4230  C  CA   . TYR A 1 257 ? -5.454  -6.177  16.552  1.00 7.62   ?  480  TYR A CA   1 
ATOM   4231  C  C    . TYR A 1 257 ? -6.604  -6.197  15.567  1.00 8.40   ?  480  TYR A C    1 
ATOM   4232  O  O    . TYR A 1 257 ? -7.173  -7.263  15.310  1.00 9.06   ?  480  TYR A O    1 
ATOM   4233  C  CB   . TYR A 1 257 ? -4.271  -6.948  15.973  1.00 9.01   ?  480  TYR A CB   1 
ATOM   4234  C  CG   . TYR A 1 257 ? -3.250  -6.142  15.194  1.00 9.44   ?  480  TYR A CG   1 
ATOM   4235  C  CD1  . TYR A 1 257 ? -2.425  -5.233  15.837  1.00 9.74   ?  480  TYR A CD1  1 
ATOM   4236  C  CD2  . TYR A 1 257 ? -3.056  -6.342  13.842  1.00 10.91  ?  480  TYR A CD2  1 
ATOM   4237  C  CE1  . TYR A 1 257 ? -1.459  -4.525  15.159  1.00 10.48  ?  480  TYR A CE1  1 
ATOM   4238  C  CE2  . TYR A 1 257 ? -2.085  -5.622  13.139  1.00 10.85  ?  480  TYR A CE2  1 
ATOM   4239  C  CZ   . TYR A 1 257 ? -1.287  -4.722  13.821  1.00 9.87   ?  480  TYR A CZ   1 
ATOM   4240  O  OH   . TYR A 1 257 ? -0.297  -4.010  13.191  1.00 11.04  ?  480  TYR A OH   1 
ATOM   4241  H  H    . TYR A 1 257 ? -5.765  -7.640  17.840  1.00 9.63   ?  480  TYR A H    1 
ATOM   4242  H  HA   . TYR A 1 257 ? -5.161  -5.267  16.718  1.00 9.15   ?  480  TYR A HA   1 
ATOM   4243  H  HB2  . TYR A 1 257 ? -3.799  -7.369  16.708  1.00 10.81  ?  480  TYR A HB2  1 
ATOM   4244  H  HB3  . TYR A 1 257 ? -4.619  -7.623  15.371  1.00 10.81  ?  480  TYR A HB3  1 
ATOM   4245  H  HD1  . TYR A 1 257 ? -2.527  -5.097  16.751  1.00 11.69  ?  480  TYR A HD1  1 
ATOM   4246  H  HD2  . TYR A 1 257 ? -3.579  -6.965  13.392  1.00 13.09  ?  480  TYR A HD2  1 
ATOM   4247  H  HE1  . TYR A 1 257 ? -0.925  -3.913  15.613  1.00 12.58  ?  480  TYR A HE1  1 
ATOM   4248  H  HE2  . TYR A 1 257 ? -1.978  -5.747  12.224  1.00 13.03  ?  480  TYR A HE2  1 
ATOM   4249  H  HH   . TYR A 1 257 ? 0.116   -3.537  13.749  1.00 13.25  ?  480  TYR A HH   1 
ATOM   4250  N  N    A VAL A 1 258 ? -6.949  -5.030  15.029  0.93 7.63   ?  481  VAL A N    1 
ATOM   4251  C  CA   A VAL A 1 258 ? -8.144  -4.889  14.214  0.93 8.70   ?  481  VAL A CA   1 
ATOM   4252  C  C    A VAL A 1 258 ? -7.790  -4.297  12.867  0.93 8.83   ?  481  VAL A C    1 
ATOM   4253  O  O    A VAL A 1 258 ? -6.868  -3.482  12.736  0.93 9.13   ?  481  VAL A O    1 
ATOM   4254  C  CB   A VAL A 1 258 ? -9.221  -4.025  14.917  0.93 11.36  ?  481  VAL A CB   1 
ATOM   4255  C  CG1  A VAL A 1 258 ? -9.552  -4.583  16.284  0.93 12.21  ?  481  VAL A CG1  1 
ATOM   4256  C  CG2  A VAL A 1 258 ? -8.780  -2.604  15.025  0.93 13.26  ?  481  VAL A CG2  1 
ATOM   4257  H  H    A VAL A 1 258 ? -6.500  -4.302  15.124  0.93 9.16   ?  481  VAL A H    1 
ATOM   4258  H  HA   A VAL A 1 258 ? -8.507  -5.774  14.055  0.93 10.44  ?  481  VAL A HA   1 
ATOM   4259  H  HB   A VAL A 1 258 ? -10.027 -4.049  14.379  0.93 13.64  ?  481  VAL A HB   1 
ATOM   4260  H  HG11 A VAL A 1 258 ? -10.273 -4.062  16.672  0.93 14.65  ?  481  VAL A HG11 1 
ATOM   4261  H  HG12 A VAL A 1 258 ? -9.827  -5.509  16.190  0.93 14.65  ?  481  VAL A HG12 1 
ATOM   4262  H  HG13 A VAL A 1 258 ? -8.764  -4.528  16.847  0.93 14.65  ?  481  VAL A HG13 1 
ATOM   4263  H  HG21 A VAL A 1 258 ? -9.358  -2.140  15.651  0.93 15.91  ?  481  VAL A HG21 1 
ATOM   4264  H  HG22 A VAL A 1 258 ? -7.863  -2.581  15.342  0.93 15.91  ?  481  VAL A HG22 1 
ATOM   4265  H  HG23 A VAL A 1 258 ? -8.838  -2.188  14.151  0.93 15.91  ?  481  VAL A HG23 1 
ATOM   4266  N  N    . ASN A 1 259 ? -8.567  -4.705  11.863  1.00 9.78   ?  482  ASN A N    1 
ATOM   4267  C  CA   . ASN A 1 259 ? -8.562  -4.095  10.544  1.00 10.71  ?  482  ASN A CA   1 
ATOM   4268  C  C    . ASN A 1 259 ? -9.702  -3.090  10.496  1.00 11.16  ?  482  ASN A C    1 
ATOM   4269  O  O    . ASN A 1 259 ? -10.869 -3.499  10.484  1.00 11.62  ?  482  ASN A O    1 
ATOM   4270  C  CB   . ASN A 1 259 ? -8.770  -5.171  9.480   1.00 10.63  ?  482  ASN A CB   1 
ATOM   4271  C  CG   . ASN A 1 259 ? -8.766  -4.611  8.071   1.00 11.99  ?  482  ASN A CG   1 
ATOM   4272  O  OD1  . ASN A 1 259 ? -9.262  -3.506  7.826   1.00 12.42  ?  482  ASN A OD1  1 
ATOM   4273  N  ND2  . ASN A 1 259 ? -8.219  -5.371  7.133   1.00 12.40  ?  482  ASN A ND2  1 
ATOM   4274  H  H    . ASN A 1 259 ? -9.123  -5.357  11.927  1.00 11.74  ?  482  ASN A H    1 
ATOM   4275  H  HA   . ASN A 1 259 ? -7.721  -3.642  10.377  1.00 12.85  ?  482  ASN A HA   1 
ATOM   4276  H  HB2  . ASN A 1 259 ? -8.055  -5.823  9.545   1.00 12.76  ?  482  ASN A HB2  1 
ATOM   4277  H  HB3  . ASN A 1 259 ? -9.627  -5.601  9.629   1.00 12.76  ?  482  ASN A HB3  1 
ATOM   4278  H  HD21 . ASN A 1 259 ? -8.193  -5.096  6.318   1.00 14.88  ?  482  ASN A HD21 1 
ATOM   4279  H  HD22 . ASN A 1 259 ? -7.890  -6.138  7.339   1.00 14.88  ?  482  ASN A HD22 1 
ATOM   4280  N  N    . PRO A 1 260 ? -9.431  -1.785  10.480  1.00 12.15  ?  483  PRO A N    1 
ATOM   4281  C  CA   . PRO A 1 260 ? -10.534 -0.816  10.527  1.00 14.19  ?  483  PRO A CA   1 
ATOM   4282  C  C    . PRO A 1 260 ? -11.366 -0.769  9.258   1.00 15.31  ?  483  PRO A C    1 
ATOM   4283  O  O    . PRO A 1 260 ? -12.504 -0.288  9.308   1.00 17.81  ?  483  PRO A O    1 
ATOM   4284  C  CB   . PRO A 1 260 ? -9.807  0.511   10.764  1.00 14.33  ?  483  PRO A CB   1 
ATOM   4285  C  CG   . PRO A 1 260 ? -8.480  0.306   10.120  1.00 14.34  ?  483  PRO A CG   1 
ATOM   4286  C  CD   . PRO A 1 260 ? -8.119  -1.118  10.438  1.00 12.92  ?  483  PRO A CD   1 
ATOM   4287  H  HA   . PRO A 1 260 ? -11.119 -1.009  11.277  1.00 17.03  ?  483  PRO A HA   1 
ATOM   4288  H  HB2  . PRO A 1 260 ? -10.292 1.240   10.346  1.00 17.20  ?  483  PRO A HB2  1 
ATOM   4289  H  HB3  . PRO A 1 260 ? -9.714  0.677   11.715  1.00 17.20  ?  483  PRO A HB3  1 
ATOM   4290  H  HG2  . PRO A 1 260 ? -8.552  0.441   9.162   1.00 17.21  ?  483  PRO A HG2  1 
ATOM   4291  H  HG3  . PRO A 1 260 ? -7.831  0.922   10.493  1.00 17.21  ?  483  PRO A HG3  1 
ATOM   4292  H  HD2  . PRO A 1 260 ? -7.558  -1.497  9.743   1.00 15.50  ?  483  PRO A HD2  1 
ATOM   4293  H  HD3  . PRO A 1 260 ? -7.670  -1.179  11.296  1.00 15.50  ?  483  PRO A HD3  1 
ATOM   4294  N  N    . GLU A 1 261 ? -10.827 -1.214  8.120   0.87 14.80  ?  484  GLU A N    1 
ATOM   4295  C  CA   . GLU A 1 261 ? -11.591 -1.195  6.876   0.87 15.80  ?  484  GLU A CA   1 
ATOM   4296  C  C    . GLU A 1 261 ? -12.657 -2.287  6.875   0.87 15.81  ?  484  GLU A C    1 
ATOM   4297  O  O    . GLU A 1 261 ? -13.814 -2.043  6.514   0.87 17.63  ?  484  GLU A O    1 
ATOM   4298  C  CB   . GLU A 1 261 ? -10.650 -1.359  5.680   0.87 17.81  ?  484  GLU A CB   1 
ATOM   4299  C  CG   . GLU A 1 261 ? -11.360 -1.198  4.324   0.87 20.89  ?  484  GLU A CG   1 
ATOM   4300  C  CD   . GLU A 1 261 ? -10.477 -1.491  3.117   0.87 24.23  ?  484  GLU A CD   1 
ATOM   4301  O  OE1  . GLU A 1 261 ? -9.254  -1.680  3.281   0.87 25.21  ?  484  GLU A OE1  1 
ATOM   4302  O  OE2  . GLU A 1 261 ? -11.020 -1.522  1.986   0.87 27.12  -1 484  GLU A OE2  1 
ATOM   4303  H  H    . GLU A 1 261 ? -10.030 -1.528  8.044   0.87 17.76  ?  484  GLU A H    1 
ATOM   4304  H  HA   . GLU A 1 261 ? -12.036 -0.337  6.793   0.87 18.97  ?  484  GLU A HA   1 
ATOM   4305  H  HB2  . GLU A 1 261 ? -9.953  -0.686  5.734   0.87 21.37  ?  484  GLU A HB2  1 
ATOM   4306  H  HB3  . GLU A 1 261 ? -10.257 -2.246  5.708   0.87 21.37  ?  484  GLU A HB3  1 
ATOM   4307  H  HG2  . GLU A 1 261 ? -12.112 -1.810  4.293   0.87 25.07  ?  484  GLU A HG2  1 
ATOM   4308  H  HG3  . GLU A 1 261 ? -11.674 -0.284  4.245   0.87 25.07  ?  484  GLU A HG3  1 
ATOM   4309  N  N    . THR A 1 262 ? -12.285 -3.505  7.264   1.00 15.50  ?  485  THR A N    1 
ATOM   4310  C  CA   . THR A 1 262 ? -13.250 -4.594  7.325   1.00 15.08  ?  485  THR A CA   1 
ATOM   4311  C  C    . THR A 1 262 ? -14.000 -4.626  8.647   1.00 15.82  ?  485  THR A C    1 
ATOM   4312  O  O    . THR A 1 262 ? -15.060 -5.257  8.729   1.00 17.00  ?  485  THR A O    1 
ATOM   4313  C  CB   . THR A 1 262 ? -12.547 -5.944  7.166   1.00 14.67  ?  485  THR A CB   1 
ATOM   4314  O  OG1  . THR A 1 262 ? -11.661 -6.129  8.272   1.00 13.03  ?  485  THR A OG1  1 
ATOM   4315  C  CG2  . THR A 1 262 ? -11.761 -6.014  5.860   1.00 14.75  ?  485  THR A CG2  1 
ATOM   4316  H  H    . THR A 1 262 ? -11.486 -3.723  7.496   1.00 18.60  ?  485  THR A H    1 
ATOM   4317  H  HA   . THR A 1 262 ? -13.879 -4.484  6.595   1.00 18.09  ?  485  THR A HA   1 
ATOM   4318  H  HB   . THR A 1 262 ? -13.207 -6.654  7.141   1.00 17.60  ?  485  THR A HB   1 
ATOM   4319  H  HG1  . THR A 1 262 ? -11.252 -6.858  8.193   1.00 15.64  ?  485  THR A HG1  1 
ATOM   4320  H  HG21 . THR A 1 262 ? -11.359 -6.891  5.761   1.00 17.70  ?  485  THR A HG21 1 
ATOM   4321  H  HG22 . THR A 1 262 ? -12.353 -5.853  5.108   1.00 17.70  ?  485  THR A HG22 1 
ATOM   4322  H  HG23 . THR A 1 262 ? -11.060 -5.344  5.858   1.00 17.70  ?  485  THR A HG23 1 
ATOM   4323  N  N    . GLY A 1 263 ? -13.450 -3.993  9.685   1.00 15.01  ?  486  GLY A N    1 
ATOM   4324  C  CA   . GLY A 1 263 ? -13.999 -4.046  11.025  1.00 14.64  ?  486  GLY A CA   1 
ATOM   4325  C  C    . GLY A 1 263 ? -13.690 -5.309  11.794  1.00 15.27  ?  486  GLY A C    1 
ATOM   4326  O  O    . GLY A 1 263 ? -14.183 -5.473  12.918  1.00 19.21  ?  486  GLY A O    1 
ATOM   4327  H  H    . GLY A 1 263 ? -12.737 -3.515  9.630   1.00 18.01  ?  486  GLY A H    1 
ATOM   4328  H  HA2  . GLY A 1 263 ? -13.649 -3.298  11.533  1.00 17.57  ?  486  GLY A HA2  1 
ATOM   4329  H  HA3  . GLY A 1 263 ? -14.964 -3.964  10.968  1.00 17.57  ?  486  GLY A HA3  1 
ATOM   4330  N  N    . ARG A 1 264 ? -12.898 -6.207  11.237  1.00 12.15  ?  487  ARG A N    1 
ATOM   4331  C  CA   . ARG A 1 264 ? -12.698 -7.504  11.859  1.00 11.59  ?  487  ARG A CA   1 
ATOM   4332  C  C    . ARG A 1 264 ? -11.463 -7.532  12.754  1.00 10.86  ?  487  ARG A C    1 
ATOM   4333  O  O    . ARG A 1 264 ? -10.441 -6.879  12.492  1.00 10.68  ?  487  ARG A O    1 
ATOM   4334  C  CB   . ARG A 1 264 ? -12.591 -8.606  10.806  1.00 12.64  ?  487  ARG A CB   1 
ATOM   4335  C  CG   . ARG A 1 264 ? -13.904 -8.856  10.058  1.00 13.49  ?  487  ARG A CG   1 
ATOM   4336  C  CD   . ARG A 1 264 ? -13.869 -10.149 9.259   1.00 14.60  ?  487  ARG A CD   1 
ATOM   4337  N  NE   . ARG A 1 264 ? -13.011 -10.046 8.083   1.00 13.44  ?  487  ARG A NE   1 
ATOM   4338  C  CZ   . ARG A 1 264 ? -13.392 -9.505  6.932   1.00 14.60  ?  487  ARG A CZ   1 
ATOM   4339  N  NH1  . ARG A 1 264 ? -14.598 -8.982  6.783   1.00 15.68  ?  487  ARG A NH1  1 
ATOM   4340  N  NH2  . ARG A 1 264 ? -12.545 -9.489  5.906   1.00 14.19  ?  487  ARG A NH2  1 
ATOM   4341  H  H    . ARG A 1 264 ? -12.466 -6.091  10.503  1.00 14.58  ?  487  ARG A H    1 
ATOM   4342  H  HA   . ARG A 1 264 ? -13.467 -7.684  12.422  1.00 13.91  ?  487  ARG A HA   1 
ATOM   4343  H  HB2  . ARG A 1 264 ? -11.920 -8.353  10.153  1.00 15.17  ?  487  ARG A HB2  1 
ATOM   4344  H  HB3  . ARG A 1 264 ? -12.335 -9.434  11.242  1.00 15.17  ?  487  ARG A HB3  1 
ATOM   4345  H  HG2  . ARG A 1 264 ? -14.630 -8.915  10.698  1.00 16.19  ?  487  ARG A HG2  1 
ATOM   4346  H  HG3  . ARG A 1 264 ? -14.064 -8.124  9.441   1.00 16.19  ?  487  ARG A HG3  1 
ATOM   4347  H  HD2  . ARG A 1 264 ? -13.528 -10.862 9.821   1.00 17.52  ?  487  ARG A HD2  1 
ATOM   4348  H  HD3  . ARG A 1 264 ? -14.767 -10.364 8.960   1.00 17.52  ?  487  ARG A HD3  1 
ATOM   4349  H  HE   . ARG A 1 264 ? -12.210 -10.355 8.139   1.00 16.12  ?  487  ARG A HE   1 
ATOM   4350  H  HH11 . ARG A 1 264 ? -15.154 -8.989  7.440   1.00 18.82  ?  487  ARG A HH11 1 
ATOM   4351  H  HH12 . ARG A 1 264 ? -14.827 -8.636  6.030   1.00 18.82  ?  487  ARG A HH12 1 
ATOM   4352  H  HH21 . ARG A 1 264 ? -11.759 -9.827  5.992   1.00 17.04  ?  487  ARG A HH21 1 
ATOM   4353  H  HH22 . ARG A 1 264 ? -12.784 -9.140  5.157   1.00 17.04  ?  487  ARG A HH22 1 
ATOM   4354  N  N    . VAL A 1 265 ? -11.575 -8.306  13.830  1.00 12.13  ?  488  VAL A N    1 
ATOM   4355  C  CA   A VAL A 1 265 ? -10.481 -8.586  14.734  0.70 12.12  ?  488  VAL A CA   1 
ATOM   4356  C  CA   B VAL A 1 265 ? -10.433 -8.531  14.701  0.30 12.08  ?  488  VAL A CA   1 
ATOM   4357  C  C    . VAL A 1 265 ? -9.595  -9.669  14.139  1.00 11.43  ?  488  VAL A C    1 
ATOM   4358  O  O    . VAL A 1 265 ? -10.114 -10.694 13.682  1.00 14.11  ?  488  VAL A O    1 
ATOM   4359  C  CB   A VAL A 1 265 ? -11.014 -9.046  16.098  0.70 13.24  ?  488  VAL A CB   1 
ATOM   4360  C  CB   B VAL A 1 265 ? -10.882 -8.806  16.147  0.30 12.84  ?  488  VAL A CB   1 
ATOM   4361  C  CG1  A VAL A 1 265 ? -9.850  -9.324  17.033  0.70 13.32  ?  488  VAL A CG1  1 
ATOM   4362  C  CG1  B VAL A 1 265 ? -11.512 -7.553  16.748  0.30 13.05  ?  488  VAL A CG1  1 
ATOM   4363  C  CG2  A VAL A 1 265 ? -11.947 -8.009  16.691  0.70 15.11  ?  488  VAL A CG2  1 
ATOM   4364  C  CG2  B VAL A 1 265 ? -11.828 -9.985  16.201  0.30 13.01  ?  488  VAL A CG2  1 
ATOM   4365  H  H    A VAL A 1 265 ? -12.307 -8.694  14.061  0.70 14.56  ?  488  VAL A H    1 
ATOM   4366  H  H    B VAL A 1 265 ? -12.297 -8.707  14.072  0.30 14.56  ?  488  VAL A H    1 
ATOM   4367  H  HA   A VAL A 1 265 ? -9.957  -7.780  14.863  0.70 14.54  ?  488  VAL A HA   1 
ATOM   4368  H  HA   B VAL A 1 265 ? -9.886  -7.730  14.719  0.30 14.49  ?  488  VAL A HA   1 
ATOM   4369  H  HB   A VAL A 1 265 ? -11.525 -9.863  15.984  0.70 15.89  ?  488  VAL A HB   1 
ATOM   4370  H  HB   B VAL A 1 265 ? -10.108 -9.036  16.685  0.30 15.41  ?  488  VAL A HB   1 
ATOM   4371  H  HG11 A VAL A 1 265 ? -10.194 -9.501  17.922  0.70 15.99  ?  488  VAL A HG11 1 
ATOM   4372  H  HG11 B VAL A 1 265 ? -11.785 -7.743  17.659  0.30 15.66  ?  488  VAL A HG11 1 
ATOM   4373  H  HG12 A VAL A 1 265 ? -9.361  -10.096 16.708  0.70 15.99  ?  488  VAL A HG12 1 
ATOM   4374  H  HG12 B VAL A 1 265 ? -10.858 -6.837  16.741  0.30 15.66  ?  488  VAL A HG12 1 
ATOM   4375  H  HG13 A VAL A 1 265 ? -9.268  -8.548  17.052  0.70 15.99  ?  488  VAL A HG13 1 
ATOM   4376  H  HG13 B VAL A 1 265 ? -12.283 -7.302  16.216  0.30 15.66  ?  488  VAL A HG13 1 
ATOM   4377  H  HG21 A VAL A 1 265 ? -12.212 -8.293  17.580  0.70 18.13  ?  488  VAL A HG21 1 
ATOM   4378  H  HG21 B VAL A 1 265 ? -11.987 -10.220 17.129  0.30 15.61  ?  488  VAL A HG21 1 
ATOM   4379  H  HG22 A VAL A 1 265 ? -11.482 -7.158  16.741  0.70 18.13  ?  488  VAL A HG22 1 
ATOM   4380  H  HG22 B VAL A 1 265 ? -12.663 -9.740  15.774  0.30 15.61  ?  488  VAL A HG22 1 
ATOM   4381  H  HG23 A VAL A 1 265 ? -12.729 -7.926  16.123  0.70 18.13  ?  488  VAL A HG23 1 
ATOM   4382  H  HG23 B VAL A 1 265 ? -11.425 -10.735 15.735  0.30 15.61  ?  488  VAL A HG23 1 
ATOM   4383  N  N    B LEU A 1 266 ? -8.285  -9.500  14.185  1.00 9.06   ?  489  LEU A N    1 
ATOM   4384  C  CA   B LEU A 1 266 ? -7.340  -10.448 13.608  1.00 9.66   ?  489  LEU A CA   1 
ATOM   4385  C  C    B LEU A 1 266 ? -6.731  -11.388 14.642  1.00 8.79   ?  489  LEU A C    1 
ATOM   4386  O  O    B LEU A 1 266 ? -6.639  -12.595 14.395  1.00 9.21   ?  489  LEU A O    1 
ATOM   4387  C  CB   B LEU A 1 266 ? -6.242  -9.657  12.886  1.00 12.53  ?  489  LEU A CB   1 
ATOM   4388  C  CG   B LEU A 1 266 ? -6.814  -8.621  11.891  1.00 15.74  ?  489  LEU A CG   1 
ATOM   4389  C  CD1  B LEU A 1 266 ? -5.764  -7.651  11.433  1.00 19.19  ?  489  LEU A CD1  1 
ATOM   4390  C  CD2  B LEU A 1 266 ? -7.462  -9.360  10.735  1.00 16.76  ?  489  LEU A CD2  1 
ATOM   4391  H  H    B LEU A 1 266 ? -7.904  -8.824  14.557  1.00 10.88  ?  489  LEU A H    1 
ATOM   4392  H  HA   B LEU A 1 266 ? -7.785  -11.013 12.958  1.00 11.60  ?  489  LEU A HA   1 
ATOM   4393  H  HB2  B LEU A 1 266 ? -5.711  -9.181  13.544  1.00 15.04  ?  489  LEU A HB2  1 
ATOM   4394  H  HB3  B LEU A 1 266 ? -5.682  -10.274 12.391  1.00 15.04  ?  489  LEU A HB3  1 
ATOM   4395  H  HG   B LEU A 1 266 ? -7.491  -8.079  12.326  1.00 18.88  ?  489  LEU A HG   1 
ATOM   4396  H  HD11 B LEU A 1 266 ? -6.163  -7.024  10.810  1.00 23.03  ?  489  LEU A HD11 1 
ATOM   4397  H  HD12 B LEU A 1 266 ? -5.415  -7.177  12.203  1.00 23.03  ?  489  LEU A HD12 1 
ATOM   4398  H  HD13 B LEU A 1 266 ? -5.050  -8.142  10.996  1.00 23.03  ?  489  LEU A HD13 1 
ATOM   4399  H  HD21 B LEU A 1 266 ? -7.697  -8.722  10.043  1.00 20.11  ?  489  LEU A HD21 1 
ATOM   4400  H  HD22 B LEU A 1 266 ? -6.834  -10.012 10.385  1.00 20.11  ?  489  LEU A HD22 1 
ATOM   4401  H  HD23 B LEU A 1 266 ? -8.260  -9.809  11.055  1.00 20.11  ?  489  LEU A HD23 1 
ATOM   4402  N  N    . PHE A 1 267 ? -6.310  -10.864 15.787  1.00 7.91   ?  490  PHE A N    1 
ATOM   4403  C  CA   . PHE A 1 267 ? -5.764  -11.683 16.864  1.00 7.87   ?  490  PHE A CA   1 
ATOM   4404  C  C    . PHE A 1 267 ? -5.829  -10.848 18.129  1.00 7.55   ?  490  PHE A C    1 
ATOM   4405  O  O    . PHE A 1 267 ? -6.124  -9.652  18.081  1.00 8.02   ?  490  PHE A O    1 
ATOM   4406  C  CB   . PHE A 1 267 ? -4.334  -12.185 16.552  1.00 8.22   ?  490  PHE A CB   1 
ATOM   4407  C  CG   . PHE A 1 267 ? -3.238  -11.128 16.608  1.00 7.33   ?  490  PHE A CG   1 
ATOM   4408  C  CD1  . PHE A 1 267 ? -2.921  -10.364 15.502  1.00 7.61   ?  490  PHE A CD1  1 
ATOM   4409  C  CD2  . PHE A 1 267 ? -2.500  -10.946 17.751  1.00 8.42   ?  490  PHE A CD2  1 
ATOM   4410  C  CE1  . PHE A 1 267 ? -1.919  -9.419  15.543  1.00 8.43   ?  490  PHE A CE1  1 
ATOM   4411  C  CE2  . PHE A 1 267 ? -1.499  -9.998  17.798  1.00 8.69   ?  490  PHE A CE2  1 
ATOM   4412  C  CZ   . PHE A 1 267 ? -1.201  -9.241  16.688  1.00 8.83   ?  490  PHE A CZ   1 
ATOM   4413  H  H    . PHE A 1 267 ? -6.330  -10.023 15.968  1.00 9.49   ?  490  PHE A H    1 
ATOM   4414  H  HA   . PHE A 1 267 ? -6.305  -12.478 16.990  1.00 9.45   ?  490  PHE A HA   1 
ATOM   4415  H  HB2  . PHE A 1 267 ? -4.105  -12.873 17.197  1.00 9.86   ?  490  PHE A HB2  1 
ATOM   4416  H  HB3  . PHE A 1 267 ? -4.330  -12.556 15.656  1.00 9.86   ?  490  PHE A HB3  1 
ATOM   4417  H  HD1  . PHE A 1 267 ? -3.394  -10.490 14.711  1.00 9.14   ?  490  PHE A HD1  1 
ATOM   4418  H  HD2  . PHE A 1 267 ? -2.676  -11.466 18.501  1.00 10.10  ?  490  PHE A HD2  1 
ATOM   4419  H  HE1  . PHE A 1 267 ? -1.733  -8.905  14.791  1.00 10.11  ?  490  PHE A HE1  1 
ATOM   4420  H  HE2  . PHE A 1 267 ? -1.021  -9.871  18.586  1.00 10.43  ?  490  PHE A HE2  1 
ATOM   4421  H  HZ   . PHE A 1 267 ? -0.517  -8.612  16.719  1.00 10.60  ?  490  PHE A HZ   1 
ATOM   4422  N  N    . GLU A 1 268 ? -5.537  -11.489 19.260  1.00 7.47   ?  491  GLU A N    1 
ATOM   4423  C  CA   . GLU A 1 268 ? -5.558  -10.813 20.549  1.00 7.09   ?  491  GLU A CA   1 
ATOM   4424  C  C    . GLU A 1 268 ? -4.249  -11.040 21.294  1.00 6.85   ?  491  GLU A C    1 
ATOM   4425  O  O    . GLU A 1 268 ? -3.480  -11.954 20.987  1.00 7.35   ?  491  GLU A O    1 
ATOM   4426  C  CB   . GLU A 1 268 ? -6.757  -11.237 21.409  1.00 8.19   ?  491  GLU A CB   1 
ATOM   4427  C  CG   . GLU A 1 268 ? -6.764  -12.700 21.782  1.00 9.46   ?  491  GLU A CG   1 
ATOM   4428  C  CD   . GLU A 1 268 ? -7.957  -13.104 22.635  1.00 10.04  ?  491  GLU A CD   1 
ATOM   4429  O  OE1  . GLU A 1 268 ? -8.898  -12.306 22.810  1.00 11.17  ?  491  GLU A OE1  1 
ATOM   4430  O  OE2  . GLU A 1 268 ? -7.949  -14.243 23.139  1.00 10.22  -1 491  GLU A OE2  1 
ATOM   4431  H  H    . GLU A 1 268 ? -5.324  -12.321 19.303  1.00 8.97   ?  491  GLU A H    1 
ATOM   4432  H  HA   . GLU A 1 268 ? -5.635  -9.859  20.394  1.00 8.51   ?  491  GLU A HA   1 
ATOM   4433  H  HB2  . GLU A 1 268 ? -6.745  -10.723 22.232  1.00 9.83   ?  491  GLU A HB2  1 
ATOM   4434  H  HB3  . GLU A 1 268 ? -7.572  -11.055 20.916  1.00 9.83   ?  491  GLU A HB3  1 
ATOM   4435  H  HG2  . GLU A 1 268 ? -6.787  -13.230 20.970  1.00 11.35  ?  491  GLU A HG2  1 
ATOM   4436  H  HG3  . GLU A 1 268 ? -5.959  -12.898 22.286  1.00 11.35  ?  491  GLU A HG3  1 
ATOM   4437  N  N    . ALA A 1 269 ? -4.006  -10.177 22.278  1.00 6.61   ?  492  ALA A N    1 
ATOM   4438  C  CA   . ALA A 1 269 ? -2.738  -10.121 22.981  1.00 6.17   ?  492  ALA A CA   1 
ATOM   4439  C  C    . ALA A 1 269 ? -2.977  -9.523  24.360  1.00 6.73   ?  492  ALA A C    1 
ATOM   4440  O  O    . ALA A 1 269 ? -4.029  -8.937  24.639  1.00 7.27   ?  492  ALA A O    1 
ATOM   4441  C  CB   . ALA A 1 269 ? -1.716  -9.296  22.189  1.00 6.68   ?  492  ALA A CB   1 
ATOM   4442  H  H    . ALA A 1 269 ? -4.577  -9.601  22.561  1.00 7.94   ?  492  ALA A H    1 
ATOM   4443  H  HA   . ALA A 1 269 ? -2.388  -11.018 23.099  1.00 7.41   ?  492  ALA A HA   1 
ATOM   4444  H  HB1  . ALA A 1 269 ? -0.871  -9.297  22.666  1.00 8.01   ?  492  ALA A HB1  1 
ATOM   4445  H  HB2  . ALA A 1 269 ? -1.600  -9.693  21.311  1.00 8.01   ?  492  ALA A HB2  1 
ATOM   4446  H  HB3  . ALA A 1 269 ? -2.044  -8.387  22.100  1.00 8.01   ?  492  ALA A HB3  1 
ATOM   4447  N  N    . LYS A 1 270 ? -1.989  -9.688  25.235  1.00 6.53   ?  493  LYS A N    1 
ATOM   4448  C  CA   . LYS A 1 270 ? -1.986  -9.075  26.554  1.00 6.62   ?  493  LYS A CA   1 
ATOM   4449  C  C    . LYS A 1 270 ? -0.986  -7.935  26.570  1.00 7.18   ?  493  LYS A C    1 
ATOM   4450  O  O    . LYS A 1 270 ? 0.192   -8.147  26.280  1.00 8.99   ?  493  LYS A O    1 
ATOM   4451  C  CB   . LYS A 1 270 ? -1.551  -10.100 27.595  1.00 8.00   ?  493  LYS A CB   1 
ATOM   4452  C  CG   . LYS A 1 270 ? -2.546  -11.147 27.950  1.00 10.71  ?  493  LYS A CG   1 
ATOM   4453  C  CD   . LYS A 1 270 ? -1.781  -12.180 28.789  1.00 13.38  ?  493  LYS A CD   1 
ATOM   4454  C  CE   . LYS A 1 270 ? -2.672  -13.122 29.471  1.00 13.12  ?  493  LYS A CE   1 
ATOM   4455  N  NZ   . LYS A 1 270 ? -1.965  -14.351 29.892  1.00 9.76   ?  493  LYS A NZ   1 
ATOM   4456  H  H    . LYS A 1 270 ? -1.290  -10.165 25.079  1.00 7.83   ?  493  LYS A H    1 
ATOM   4457  H  HA   . LYS A 1 270 ? -2.872  -8.733  26.752  1.00 7.95   ?  493  LYS A HA   1 
ATOM   4458  H  HB2  . LYS A 1 270 ? -0.765  -10.557 27.257  1.00 9.60   ?  493  LYS A HB2  1 
ATOM   4459  H  HB3  . LYS A 1 270 ? -1.334  -9.626  28.412  1.00 9.60   ?  493  LYS A HB3  1 
ATOM   4460  H  HG2  . LYS A 1 270 ? -3.269  -10.769 28.474  1.00 12.85  ?  493  LYS A HG2  1 
ATOM   4461  H  HG3  . LYS A 1 270 ? -2.900  -11.569 27.152  1.00 12.85  ?  493  LYS A HG3  1 
ATOM   4462  H  HD2  . LYS A 1 270 ? -1.195  -12.689 28.207  1.00 16.05  ?  493  LYS A HD2  1 
ATOM   4463  H  HD3  . LYS A 1 270 ? -1.260  -11.718 29.464  1.00 16.05  ?  493  LYS A HD3  1 
ATOM   4464  H  HE2  . LYS A 1 270 ? -3.039  -12.698 30.262  1.00 15.74  ?  493  LYS A HE2  1 
ATOM   4465  H  HE3  . LYS A 1 270 ? -3.388  -13.377 28.869  1.00 15.74  ?  493  LYS A HE3  1 
ATOM   4466  H  HZ1  . LYS A 1 270 ? -1.647  -14.778 29.180  1.00 11.72  ?  493  LYS A HZ1  1 
ATOM   4467  H  HZ2  . LYS A 1 270 ? -1.288  -14.143 30.432  1.00 11.72  ?  493  LYS A HZ2  1 
ATOM   4468  H  HZ3  . LYS A 1 270 ? -2.525  -14.890 30.326  1.00 11.72  ?  493  LYS A HZ3  1 
ATOM   4469  N  N    . LEU A 1 271 ? -1.449  -6.743  26.933  1.00 6.24   ?  494  LEU A N    1 
ATOM   4470  C  CA   . LEU A 1 271 ? -0.572  -5.608  27.185  1.00 6.18   ?  494  LEU A CA   1 
ATOM   4471  C  C    . LEU A 1 271 ? -0.387  -5.502  28.694  1.00 5.97   ?  494  LEU A C    1 
ATOM   4472  O  O    . LEU A 1 271 ? -1.307  -5.130  29.425  1.00 6.82   ?  494  LEU A O    1 
ATOM   4473  C  CB   . LEU A 1 271 ? -1.136  -4.337  26.560  1.00 6.69   ?  494  LEU A CB   1 
ATOM   4474  C  CG   . LEU A 1 271 ? -0.392  -3.040  26.921  1.00 6.80   ?  494  LEU A CG   1 
ATOM   4475  C  CD1  . LEU A 1 271 ? 1.046   -3.064  26.449  1.00 7.48   ?  494  LEU A CD1  1 
ATOM   4476  C  CD2  . LEU A 1 271 ? -1.094  -1.863  26.314  1.00 8.15   ?  494  LEU A CD2  1 
ATOM   4477  H  H    . LEU A 1 271 ? -2.284  -6.565  27.042  1.00 7.49   ?  494  LEU A H    1 
ATOM   4478  H  HA   . LEU A 1 271 ? 0.300   -5.750  26.785  1.00 7.42   ?  494  LEU A HA   1 
ATOM   4479  H  HB2  . LEU A 1 271 ? -1.104  -4.431  25.595  1.00 8.03   ?  494  LEU A HB2  1 
ATOM   4480  H  HB3  . LEU A 1 271 ? -2.055  -4.234  26.853  1.00 8.03   ?  494  LEU A HB3  1 
ATOM   4481  H  HG   . LEU A 1 271 ? -0.383  -2.957  27.887  1.00 8.16   ?  494  LEU A HG   1 
ATOM   4482  H  HD11 . LEU A 1 271 ? 1.461   -2.213  26.659  1.00 8.98   ?  494  LEU A HD11 1 
ATOM   4483  H  HD12 . LEU A 1 271 ? 1.515   -3.782  26.902  1.00 8.98   ?  494  LEU A HD12 1 
ATOM   4484  H  HD13 . LEU A 1 271 ? 1.061   -3.211  25.490  1.00 8.98   ?  494  LEU A HD13 1 
ATOM   4485  H  HD21 . LEU A 1 271 ? -0.610  -1.054  26.541  1.00 9.78   ?  494  LEU A HD21 1 
ATOM   4486  H  HD22 . LEU A 1 271 ? -1.120  -1.973  25.350  1.00 9.78   ?  494  LEU A HD22 1 
ATOM   4487  H  HD23 . LEU A 1 271 ? -1.997  -1.819  26.666  1.00 9.78   ?  494  LEU A HD23 1 
ATOM   4488  N  N    . HIS A 1 272 ? 0.795   -5.873  29.147  1.00 6.04   ?  495  HIS A N    1 
ATOM   4489  C  CA   . HIS A 1 272 ? 1.119   -5.853  30.562  1.00 6.60   ?  495  HIS A CA   1 
ATOM   4490  C  C    . HIS A 1 272 ? 1.373   -4.430  31.025  1.00 6.79   ?  495  HIS A C    1 
ATOM   4491  O  O    . HIS A 1 272 ? 1.955   -3.620  30.297  1.00 6.54   ?  495  HIS A O    1 
ATOM   4492  C  CB   . HIS A 1 272 ? 2.343   -6.732  30.788  1.00 7.04   ?  495  HIS A CB   1 
ATOM   4493  C  CG   . HIS A 1 272 ? 2.076   -8.147  30.427  1.00 6.75   ?  495  HIS A CG   1 
ATOM   4494  N  ND1  . HIS A 1 272 ? 1.492   -9.036  31.301  1.00 8.49   ?  495  HIS A ND1  1 
ATOM   4495  C  CD2  . HIS A 1 272 ? 2.205   -8.799  29.247  1.00 8.05   ?  495  HIS A CD2  1 
ATOM   4496  C  CE1  . HIS A 1 272 ? 1.313   -10.189 30.684  1.00 7.84   ?  495  HIS A CE1  1 
ATOM   4497  N  NE2  . HIS A 1 272 ? 1.749   -10.078 29.441  1.00 8.12   ?  495  HIS A NE2  1 
ATOM   4498  H  H    . HIS A 1 272 ? 1.440   -6.145  28.648  1.00 7.25   ?  495  HIS A H    1 
ATOM   4499  H  HA   . HIS A 1 272 ? 0.386   -6.196  31.096  1.00 7.92   ?  495  HIS A HA   1 
ATOM   4500  H  HB2  . HIS A 1 272 ? 3.074   -6.409  30.238  1.00 8.45   ?  495  HIS A HB2  1 
ATOM   4501  H  HB3  . HIS A 1 272 ? 2.593   -6.698  31.725  1.00 8.45   ?  495  HIS A HB3  1 
ATOM   4502  H  HD2  . HIS A 1 272 ? 2.540   -8.445  28.454  1.00 9.66   ?  495  HIS A HD2  1 
ATOM   4503  H  HE1  . HIS A 1 272 ? 0.941   -10.953 31.061  1.00 9.42   ?  495  HIS A HE1  1 
ATOM   4504  H  HE2  . HIS A 1 272 ? 1.747   -10.705 28.851  1.00 9.74   ?  495  HIS A HE2  1 
ATOM   4505  N  N    . ARG A 1 273 ? 0.948   -4.137  32.252  1.00 6.94   ?  496  ARG A N    1 
ATOM   4506  C  CA   . ARG A 1 273 ? 1.080   -2.792  32.812  1.00 7.66   ?  496  ARG A CA   1 
ATOM   4507  C  C    . ARG A 1 273 ? 2.514   -2.282  32.731  1.00 7.34   ?  496  ARG A C    1 
ATOM   4508  O  O    . ARG A 1 273 ? 2.741   -1.084  32.508  1.00 7.88   ?  496  ARG A O    1 
ATOM   4509  C  CB   . ARG A 1 273 ? 0.579   -2.803  34.255  1.00 9.02   ?  496  ARG A CB   1 
ATOM   4510  C  CG   . ARG A 1 273 ? 0.708   -1.492  34.994  1.00 11.10  ?  496  ARG A CG   1 
ATOM   4511  C  CD   . ARG A 1 273 ? 0.174   -1.647  36.399  1.00 13.13  ?  496  ARG A CD   1 
ATOM   4512  N  NE   . ARG A 1 273 ? 0.332   -0.419  37.160  1.00 15.36  ?  496  ARG A NE   1 
ATOM   4513  C  CZ   . ARG A 1 273 ? -0.103  -0.257  38.394  1.00 17.85  ?  496  ARG A CZ   1 
ATOM   4514  N  NH1  . ARG A 1 273 ? -0.731  -1.226  39.035  1.00 19.61  ?  496  ARG A NH1  1 
ATOM   4515  N  NH2  . ARG A 1 273 ? 0.077   0.914   38.994  1.00 18.91  ?  496  ARG A NH2  1 
ATOM   4516  H  H    . ARG A 1 273 ? 0.577   -4.700  32.786  1.00 8.33   ?  496  ARG A H    1 
ATOM   4517  H  HA   . ARG A 1 273 ? 0.533   -2.175  32.301  1.00 9.19   ?  496  ARG A HA   1 
ATOM   4518  H  HB2  . ARG A 1 273 ? -0.361  -3.042  34.250  1.00 10.82  ?  496  ARG A HB2  1 
ATOM   4519  H  HB3  . ARG A 1 273 ? 1.087   -3.466  34.749  1.00 10.82  ?  496  ARG A HB3  1 
ATOM   4520  H  HG2  . ARG A 1 273 ? 1.641   -1.232  35.041  1.00 13.33  ?  496  ARG A HG2  1 
ATOM   4521  H  HG3  . ARG A 1 273 ? 0.195   -0.806  34.539  1.00 13.33  ?  496  ARG A HG3  1 
ATOM   4522  H  HD2  . ARG A 1 273 ? -0.770  -1.866  36.363  1.00 15.76  ?  496  ARG A HD2  1 
ATOM   4523  H  HD3  . ARG A 1 273 ? 0.661   -2.353  36.853  1.00 15.76  ?  496  ARG A HD3  1 
ATOM   4524  H  HE   . ARG A 1 273 ? 0.733   0.241   36.782  1.00 18.44  ?  496  ARG A HE   1 
ATOM   4525  H  HH11 . ARG A 1 273 ? -0.863  -1.983  38.647  1.00 23.53  ?  496  ARG A HH11 1 
ATOM   4526  H  HH12 . ARG A 1 273 ? -1.007  -1.102  39.840  1.00 23.53  ?  496  ARG A HH12 1 
ATOM   4527  H  HH21 . ARG A 1 273 ? 0.473   1.554   38.577  1.00 22.70  ?  496  ARG A HH21 1 
ATOM   4528  H  HH22 . ARG A 1 273 ? -0.202  1.033   39.799  1.00 22.70  ?  496  ARG A HH22 1 
ATOM   4529  N  N    . GLN A 1 274 ? 3.492   -3.177  32.898  0.93 7.04   ?  497  GLN A N    1 
ATOM   4530  C  CA   . GLN A 1 274 ? 4.896   -2.795  32.825  0.93 8.35   ?  497  GLN A CA   1 
ATOM   4531  C  C    . GLN A 1 274 ? 5.290   -2.230  31.474  0.93 7.94   ?  497  GLN A C    1 
ATOM   4532  O  O    . GLN A 1 274 ? 6.307   -1.547  31.395  0.93 9.40   ?  497  GLN A O    1 
ATOM   4533  C  CB   . GLN A 1 274 ? 5.789   -4.020  33.103  0.93 12.62  ?  497  GLN A CB   1 
ATOM   4534  C  CG   . GLN A 1 274 ? 5.867   -4.454  34.555  0.93 17.44  ?  497  GLN A CG   1 
ATOM   4535  C  CD   . GLN A 1 274 ? 6.573   -5.797  34.729  0.93 21.11  ?  497  GLN A CD   1 
ATOM   4536  O  OE1  . GLN A 1 274 ? 6.103   -6.833  34.250  0.93 21.83  ?  497  GLN A OE1  1 
ATOM   4537  N  NE2  . GLN A 1 274 ? 7.706   -5.781  35.423  0.93 22.57  ?  497  GLN A NE2  1 
ATOM   4538  H  H    . GLN A 1 274 ? 3.365   -4.013  33.055  0.93 8.45   ?  497  GLN A H    1 
ATOM   4539  H  HA   . GLN A 1 274 ? 5.048   -2.116  33.502  0.93 10.02  ?  497  GLN A HA   1 
ATOM   4540  H  HB2  . GLN A 1 274 ? 5.443   -4.771  32.595  0.93 15.15  ?  497  GLN A HB2  1 
ATOM   4541  H  HB3  . GLN A 1 274 ? 6.691   -3.812  32.814  0.93 15.15  ?  497  GLN A HB3  1 
ATOM   4542  H  HG2  . GLN A 1 274 ? 6.359   -3.788  35.059  0.93 20.94  ?  497  GLN A HG2  1 
ATOM   4543  H  HG3  . GLN A 1 274 ? 4.968   -4.540  34.909  0.93 20.94  ?  497  GLN A HG3  1 
ATOM   4544  H  HE21 . GLN A 1 274 ? 8.003   -5.040  35.745  0.93 27.08  ?  497  GLN A HE21 1 
ATOM   4545  H  HE22 . GLN A 1 274 ? 8.143   -6.510  35.549  0.93 27.08  ?  497  GLN A HE22 1 
ATOM   4546  N  N    . GLY A 1 275 ? 4.519   -2.501  30.419  1.00 7.48   ?  498  GLY A N    1 
ATOM   4547  C  CA   . GLY A 1 275 ? 4.751   -1.905  29.122  1.00 6.61   ?  498  GLY A CA   1 
ATOM   4548  C  C    . GLY A 1 275 ? 5.270   -2.842  28.054  1.00 6.78   ?  498  GLY A C    1 
ATOM   4549  O  O    . GLY A 1 275 ? 6.139   -2.458  27.264  1.00 7.90   ?  498  GLY A O    1 
ATOM   4550  H  H    . GLY A 1 275 ? 3.847   -3.037  30.437  1.00 8.98   ?  498  GLY A H    1 
ATOM   4551  H  HA2  . GLY A 1 275 ? 3.915   -1.532  28.802  1.00 7.94   ?  498  GLY A HA2  1 
ATOM   4552  H  HA3  . GLY A 1 275 ? 5.399   -1.190  29.223  1.00 7.94   ?  498  GLY A HA3  1 
ATOM   4553  N  N    . PHE A 1 276 ? 4.741   -4.059  27.986  1.00 6.46   ?  499  PHE A N    1 
ATOM   4554  C  CA   . PHE A 1 276 ? 5.125   -4.983  26.929  1.00 6.39   ?  499  PHE A CA   1 
ATOM   4555  C  C    . PHE A 1 276 ? 3.946   -5.900  26.640  1.00 5.89   ?  499  PHE A C    1 
ATOM   4556  O  O    . PHE A 1 276 ? 3.010   -6.018  27.437  1.00 6.89   ?  499  PHE A O    1 
ATOM   4557  C  CB   . PHE A 1 276 ? 6.392   -5.785  27.274  1.00 7.57   ?  499  PHE A CB   1 
ATOM   4558  C  CG   . PHE A 1 276 ? 6.211   -6.809  28.369  1.00 7.94   ?  499  PHE A CG   1 
ATOM   4559  C  CD1  . PHE A 1 276 ? 6.172   -6.445  29.716  1.00 8.78   ?  499  PHE A CD1  1 
ATOM   4560  C  CD2  . PHE A 1 276 ? 6.146   -8.160  28.053  1.00 8.85   ?  499  PHE A CD2  1 
ATOM   4561  C  CE1  . PHE A 1 276 ? 6.019   -7.415  30.696  1.00 9.32   ?  499  PHE A CE1  1 
ATOM   4562  C  CE2  . PHE A 1 276 ? 6.003   -9.108  29.040  1.00 9.74   ?  499  PHE A CE2  1 
ATOM   4563  C  CZ   . PHE A 1 276 ? 5.938   -8.737  30.355  1.00 10.31  ?  499  PHE A CZ   1 
ATOM   4564  H  H    . PHE A 1 276 ? 4.160   -4.370  28.539  1.00 7.75   ?  499  PHE A H    1 
ATOM   4565  H  HA   . PHE A 1 276 ? 5.325   -4.482  26.123  1.00 7.67   ?  499  PHE A HA   1 
ATOM   4566  H  HB2  . PHE A 1 276 ? 6.685   -6.256  26.479  1.00 9.08   ?  499  PHE A HB2  1 
ATOM   4567  H  HB3  . PHE A 1 276 ? 7.079   -5.165  27.564  1.00 9.08   ?  499  PHE A HB3  1 
ATOM   4568  H  HD1  . PHE A 1 276 ? 6.247   -5.550  29.957  1.00 10.54  ?  499  PHE A HD1  1 
ATOM   4569  H  HD2  . PHE A 1 276 ? 6.200   -8.427  27.164  1.00 10.62  ?  499  PHE A HD2  1 
ATOM   4570  H  HE1  . PHE A 1 276 ? 5.972   -7.164  31.590  1.00 11.19  ?  499  PHE A HE1  1 
ATOM   4571  H  HE2  . PHE A 1 276 ? 5.949   -10.008 28.811  1.00 11.69  ?  499  PHE A HE2  1 
ATOM   4572  H  HZ   . PHE A 1 276 ? 5.840   -9.383  31.017  1.00 12.37  ?  499  PHE A HZ   1 
ATOM   4573  N  N    . ILE A 1 277 ? 4.007   -6.536  25.468  1.00 6.20   ?  500  ILE A N    1 
ATOM   4574  C  CA   . ILE A 1 277 ? 2.913   -7.335  24.936  1.00 6.01   ?  500  ILE A CA   1 
ATOM   4575  C  C    . ILE A 1 277 ? 3.330   -8.796  24.884  1.00 6.07   ?  500  ILE A C    1 
ATOM   4576  O  O    . ILE A 1 277 ? 4.442   -9.117  24.445  1.00 6.56   ?  500  ILE A O    1 
ATOM   4577  C  CB   . ILE A 1 277 ? 2.540   -6.862  23.515  1.00 6.33   ?  500  ILE A CB   1 
ATOM   4578  C  CG1  . ILE A 1 277 ? 2.157   -5.385  23.525  1.00 6.94   ?  500  ILE A CG1  1 
ATOM   4579  C  CG2  . ILE A 1 277 ? 1.422   -7.703  22.938  1.00 6.50   ?  500  ILE A CG2  1 
ATOM   4580  C  CD1  . ILE A 1 277 ? 2.037   -4.789  22.119  1.00 7.87   ?  500  ILE A CD1  1 
ATOM   4581  H  H    . ILE A 1 277 ? 4.694   -6.515  24.951  1.00 7.44   ?  500  ILE A H    1 
ATOM   4582  H  HA   . ILE A 1 277 ? 2.151   -7.253  25.529  1.00 7.22   ?  500  ILE A HA   1 
ATOM   4583  H  HB   . ILE A 1 277 ? 3.321   -6.972  22.950  1.00 7.59   ?  500  ILE A HB   1 
ATOM   4584  H  HG12 . ILE A 1 277 ? 1.300   -5.285  23.967  1.00 8.33   ?  500  ILE A HG12 1 
ATOM   4585  H  HG13 . ILE A 1 277 ? 2.837   -4.886  24.004  1.00 8.33   ?  500  ILE A HG13 1 
ATOM   4586  H  HG21 . ILE A 1 277 ? 1.136   -7.313  22.097  1.00 7.80   ?  500  ILE A HG21 1 
ATOM   4587  H  HG22 . ILE A 1 277 ? 1.749   -8.604  22.790  1.00 7.80   ?  500  ILE A HG22 1 
ATOM   4588  H  HG23 . ILE A 1 277 ? 0.682   -7.718  23.564  1.00 7.80   ?  500  ILE A HG23 1 
ATOM   4589  H  HD11 . ILE A 1 277 ? 2.010   -3.822  22.188  1.00 9.45   ?  500  ILE A HD11 1 
ATOM   4590  H  HD12 . ILE A 1 277 ? 2.805   -5.062  21.594  1.00 9.45   ?  500  ILE A HD12 1 
ATOM   4591  H  HD13 . ILE A 1 277 ? 1.222   -5.115  21.707  1.00 9.45   ?  500  ILE A HD13 1 
ATOM   4592  N  N    . THR A 1 278 ? 2.413   -9.687  25.259  1.00 6.25   ?  501  THR A N    1 
ATOM   4593  C  CA   . THR A 1 278 ? 2.572   -11.106 24.988  1.00 6.02   ?  501  THR A CA   1 
ATOM   4594  C  C    . THR A 1 278 ? 1.417   -11.646 24.150  1.00 6.44   ?  501  THR A C    1 
ATOM   4595  O  O    . THR A 1 278 ? 0.295   -11.116 24.165  1.00 6.86   ?  501  THR A O    1 
ATOM   4596  C  CB   . THR A 1 278 ? 2.746   -11.929 26.274  1.00 6.58   ?  501  THR A CB   1 
ATOM   4597  O  OG1  . THR A 1 278 ? 1.605   -11.780 27.119  1.00 7.75   ?  501  THR A OG1  1 
ATOM   4598  C  CG2  . THR A 1 278 ? 3.994   -11.498 27.026  1.00 7.32   ?  501  THR A CG2  1 
ATOM   4599  H  H    . THR A 1 278 ? 1.687   -9.488  25.674  1.00 7.50   ?  501  THR A H    1 
ATOM   4600  H  HA   . THR A 1 278 ? 3.378   -11.224 24.461  1.00 7.23   ?  501  THR A HA   1 
ATOM   4601  H  HB   . THR A 1 278 ? 2.840   -12.865 26.035  1.00 7.90   ?  501  THR A HB   1 
ATOM   4602  H  HG1  . THR A 1 278 ? 1.641   -12.333 27.750  1.00 9.30   ?  501  THR A HG1  1 
ATOM   4603  H  HG21 . THR A 1 278 ? 4.104   -12.039 27.824  1.00 8.79   ?  501  THR A HG21 1 
ATOM   4604  H  HG22 . THR A 1 278 ? 4.775   -11.606 26.462  1.00 8.79   ?  501  THR A HG22 1 
ATOM   4605  H  HG23 . THR A 1 278 ? 3.919   -10.566 27.285  1.00 8.79   ?  501  THR A HG23 1 
ATOM   4606  N  N    . VAL A 1 279 ? 1.740   -12.705 23.409  1.00 6.43   ?  502  VAL A N    1 
ATOM   4607  C  CA   . VAL A 1 279 ? 0.823   -13.400 22.522  1.00 6.67   ?  502  VAL A CA   1 
ATOM   4608  C  C    . VAL A 1 279 ? 0.969   -14.896 22.753  1.00 7.10   ?  502  VAL A C    1 
ATOM   4609  O  O    . VAL A 1 279 ? 2.038   -15.390 23.138  1.00 7.74   ?  502  VAL A O    1 
ATOM   4610  C  CB   . VAL A 1 279 ? 1.073   -13.067 21.032  1.00 6.67   ?  502  VAL A CB   1 
ATOM   4611  C  CG1  . VAL A 1 279 ? 0.642   -11.636 20.719  1.00 7.13   ?  502  VAL A CG1  1 
ATOM   4612  C  CG2  . VAL A 1 279 ? 2.550   -13.295 20.665  1.00 7.68   ?  502  VAL A CG2  1 
ATOM   4613  H  H    . VAL A 1 279 ? 2.527   -13.053 23.406  1.00 7.71   ?  502  VAL A H    1 
ATOM   4614  H  HA   . VAL A 1 279 ? -0.083  -13.134 22.742  1.00 8.01   ?  502  VAL A HA   1 
ATOM   4615  H  HB   . VAL A 1 279 ? 0.537   -13.662 20.484  1.00 8.01   ?  502  VAL A HB   1 
ATOM   4616  H  HG11 . VAL A 1 279 ? 0.829   -11.447 19.786  1.00 8.55   ?  502  VAL A HG11 1 
ATOM   4617  H  HG12 . VAL A 1 279 ? -0.309  -11.548 20.891  1.00 8.55   ?  502  VAL A HG12 1 
ATOM   4618  H  HG13 . VAL A 1 279 ? 1.138   -11.026 21.287  1.00 8.55   ?  502  VAL A HG13 1 
ATOM   4619  H  HG21 . VAL A 1 279 ? 2.676   -13.097 19.724  1.00 9.22   ?  502  VAL A HG21 1 
ATOM   4620  H  HG22 . VAL A 1 279 ? 3.103   -12.708 21.204  1.00 9.22   ?  502  VAL A HG22 1 
ATOM   4621  H  HG23 . VAL A 1 279 ? 2.780   -14.221 20.842  1.00 9.22   ?  502  VAL A HG23 1 
ATOM   4622  N  N    . ALA A 1 280 ? -0.092  -15.635 22.442  1.00 7.31   ?  503  ALA A N    1 
ATOM   4623  C  CA   . ALA A 1 280 ? -0.077  -17.098 22.466  1.00 7.75   ?  503  ALA A CA   1 
ATOM   4624  C  C    . ALA A 1 280 ? 0.409   -17.603 21.111  1.00 8.21   ?  503  ALA A C    1 
ATOM   4625  O  O    . ALA A 1 280 ? -0.360  -17.798 20.176  1.00 9.67   ?  503  ALA A O    1 
ATOM   4626  C  CB   . ALA A 1 280 ? -1.460  -17.639 22.801  1.00 8.31   ?  503  ALA A CB   1 
ATOM   4627  H  H    . ALA A 1 280 ? -0.852  -15.306 22.208  1.00 8.77   ?  503  ALA A H    1 
ATOM   4628  H  HA   . ALA A 1 280 ? 0.551   -17.398 23.142  1.00 9.30   ?  503  ALA A HA   1 
ATOM   4629  H  HB1  . ALA A 1 280 ? -1.430  -18.608 22.797  1.00 9.98   ?  503  ALA A HB1  1 
ATOM   4630  H  HB2  . ALA A 1 280 ? -1.719  -17.320 23.680  1.00 9.98   ?  503  ALA A HB2  1 
ATOM   4631  H  HB3  . ALA A 1 280 ? -2.092  -17.325 22.136  1.00 9.98   ?  503  ALA A HB3  1 
ATOM   4632  N  N    . LYS A 1 281 ? 1.712   -17.829 21.010  1.00 9.33   ?  504  LYS A N    1 
ATOM   4633  C  CA   . LYS A 1 281 ? 2.316   -18.371 19.804  1.00 10.14  ?  504  LYS A CA   1 
ATOM   4634  C  C    . LYS A 1 281 ? 3.595   -19.093 20.204  1.00 10.97  ?  504  LYS A C    1 
ATOM   4635  O  O    . LYS A 1 281 ? 4.269   -18.698 21.153  1.00 11.24  ?  504  LYS A O    1 
ATOM   4636  C  CB   . LYS A 1 281 ? 2.646   -17.268 18.777  1.00 10.81  ?  504  LYS A CB   1 
ATOM   4637  C  CG   . LYS A 1 281 ? 3.200   -17.823 17.452  1.00 11.16  ?  504  LYS A CG   1 
ATOM   4638  C  CD   . LYS A 1 281 ? 3.244   -16.816 16.306  1.00 12.36  ?  504  LYS A CD   1 
ATOM   4639  C  CE   . LYS A 1 281 ? 3.871   -17.454 15.073  1.00 12.25  ?  504  LYS A CE   1 
ATOM   4640  N  NZ   . LYS A 1 281 ? 3.945   -16.518 13.925  1.00 12.75  ?  504  LYS A NZ   1 
ATOM   4641  H  H    . LYS A 1 281 ? 2.277   -17.674 21.639  1.00 11.20  ?  504  LYS A H    1 
ATOM   4642  H  HA   . LYS A 1 281 ? 1.704   -18.997 19.387  1.00 12.17  ?  504  LYS A HA   1 
ATOM   4643  H  HB2  . LYS A 1 281 ? 1.837   -16.771 18.577  1.00 12.97  ?  504  LYS A HB2  1 
ATOM   4644  H  HB3  . LYS A 1 281 ? 3.315   -16.676 19.155  1.00 12.97  ?  504  LYS A HB3  1 
ATOM   4645  H  HG2  . LYS A 1 281 ? 4.107   -18.133 17.602  1.00 13.39  ?  504  LYS A HG2  1 
ATOM   4646  H  HG3  . LYS A 1 281 ? 2.640   -18.563 17.169  1.00 13.39  ?  504  LYS A HG3  1 
ATOM   4647  H  HD2  . LYS A 1 281 ? 2.343   -16.533 16.085  1.00 14.83  ?  504  LYS A HD2  1 
ATOM   4648  H  HD3  . LYS A 1 281 ? 3.779   -16.049 16.565  1.00 14.83  ?  504  LYS A HD3  1 
ATOM   4649  H  HE2  . LYS A 1 281 ? 4.773   -17.739 15.287  1.00 14.71  ?  504  LYS A HE2  1 
ATOM   4650  H  HE3  . LYS A 1 281 ? 3.336   -18.217 14.805  1.00 14.71  ?  504  LYS A HE3  1 
ATOM   4651  H  HZ1  . LYS A 1 281 ? 3.129   -16.241 13.704  1.00 15.30  ?  504  LYS A HZ1  1 
ATOM   4652  H  HZ2  . LYS A 1 281 ? 4.442   -15.812 14.139  1.00 15.30  ?  504  LYS A HZ2  1 
ATOM   4653  H  HZ3  . LYS A 1 281 ? 4.311   -16.926 13.223  1.00 15.30  ?  504  LYS A HZ3  1 
ATOM   4654  N  N    . SER A 1 282 ? 3.916   -20.164 19.496  1.00 11.34  ?  505  SER A N    1 
ATOM   4655  C  CA   A SER A 1 282 ? 5.164   -20.891 19.695  0.48 13.06  ?  505  SER A CA   1 
ATOM   4656  C  CA   B SER A 1 282 ? 5.161   -20.901 19.693  0.52 13.47  ?  505  SER A CA   1 
ATOM   4657  C  C    . SER A 1 282 ? 5.946   -20.856 18.388  1.00 13.46  ?  505  SER A C    1 
ATOM   4658  O  O    . SER A 1 282 ? 5.514   -21.428 17.386  1.00 16.29  ?  505  SER A O    1 
ATOM   4659  C  CB   A SER A 1 282 ? 4.897   -22.329 20.136  0.48 14.71  ?  505  SER A CB   1 
ATOM   4660  C  CB   B SER A 1 282 ? 4.887   -22.351 20.097  0.52 15.91  ?  505  SER A CB   1 
ATOM   4661  O  OG   A SER A 1 282 ? 4.510   -22.368 21.497  0.48 16.18  ?  505  SER A OG   1 
ATOM   4662  O  OG   B SER A 1 282 ? 6.084   -23.117 20.097  0.52 18.07  ?  505  SER A OG   1 
ATOM   4663  H  H    A SER A 1 282 ? 3.417   -20.497 18.880  0.48 13.60  ?  505  SER A H    1 
ATOM   4664  H  H    B SER A 1 282 ? 3.418   -20.494 18.877  0.52 13.60  ?  505  SER A H    1 
ATOM   4665  H  HA   A SER A 1 282 ? 5.690   -20.452 20.382  0.48 15.67  ?  505  SER A HA   1 
ATOM   4666  H  HA   B SER A 1 282 ? 5.679   -20.474 20.394  0.52 16.17  ?  505  SER A HA   1 
ATOM   4667  H  HB2  A SER A 1 282 ? 4.184   -22.699 19.593  0.48 17.66  ?  505  SER A HB2  1 
ATOM   4668  H  HB2  B SER A 1 282 ? 4.505   -22.362 20.989  0.52 19.09  ?  505  SER A HB2  1 
ATOM   4669  H  HB3  A SER A 1 282 ? 5.707   -22.850 20.022  0.48 17.66  ?  505  SER A HB3  1 
ATOM   4670  H  HB3  B SER A 1 282 ? 4.264   -22.741 19.465  0.52 19.09  ?  505  SER A HB3  1 
ATOM   4671  H  HG   A SER A 1 282 ? 3.799   -21.936 21.605  0.48 19.42  ?  505  SER A HG   1 
ATOM   4672  H  HG   B SER A 1 282 ? 6.628   -22.801 20.655  0.52 21.68  ?  505  SER A HG   1 
ATOM   4673  N  N    . GLY A 1 283 ? 7.091   -20.195 18.398  1.00 12.31  ?  506  GLY A N    1 
ATOM   4674  C  CA   . GLY A 1 283 ? 7.971   -20.147 17.247  1.00 12.56  ?  506  GLY A CA   1 
ATOM   4675  C  C    . GLY A 1 283 ? 7.979   -18.784 16.576  1.00 12.21  ?  506  GLY A C    1 
ATOM   4676  O  O    . GLY A 1 283 ? 7.350   -17.817 17.016  1.00 13.43  ?  506  GLY A O    1 
ATOM   4677  H  H    . GLY A 1 283 ? 7.386   -19.757 19.076  1.00 14.77  ?  506  GLY A H    1 
ATOM   4678  H  HA2  . GLY A 1 283 ? 8.876   -20.353 17.527  1.00 15.07  ?  506  GLY A HA2  1 
ATOM   4679  H  HA3  . GLY A 1 283 ? 7.684   -20.805 16.596  1.00 15.07  ?  506  GLY A HA3  1 
ATOM   4680  N  N    . ASP A 1 284 ? 8.729   -18.748 15.484  1.00 12.43  ?  507  ASP A N    1 
ATOM   4681  C  CA   . ASP A 1 284 ? 8.972   -17.556 14.683  1.00 13.55  ?  507  ASP A CA   1 
ATOM   4682  C  C    . ASP A 1 284 ? 8.544   -17.918 13.269  1.00 14.14  ?  507  ASP A C    1 
ATOM   4683  O  O    . ASP A 1 284 ? 9.181   -18.754 12.619  1.00 16.33  ?  507  ASP A O    1 
ATOM   4684  C  CB   . ASP A 1 284 ? 10.453  -17.189 14.750  1.00 14.01  ?  507  ASP A CB   1 
ATOM   4685  C  CG   . ASP A 1 284 ? 10.782  -15.934 13.992  1.00 15.40  ?  507  ASP A CG   1 
ATOM   4686  O  OD1  . ASP A 1 284 ? 9.855   -15.309 13.438  1.00 15.45  -1 507  ASP A OD1  1 
ATOM   4687  O  OD2  . ASP A 1 284 ? 11.981  -15.579 13.945  1.00 17.55  ?  507  ASP A OD2  1 
ATOM   4688  H  H    . ASP A 1 284 ? 9.131   -19.440 15.169  1.00 14.91  ?  507  ASP A H    1 
ATOM   4689  H  HA   . ASP A 1 284 ? 8.457   -16.793 14.988  1.00 16.26  ?  507  ASP A HA   1 
ATOM   4690  H  HB2  . ASP A 1 284 ? 10.702  -17.051 15.678  1.00 16.81  ?  507  ASP A HB2  1 
ATOM   4691  H  HB3  . ASP A 1 284 ? 10.975  -17.913 14.371  1.00 16.81  ?  507  ASP A HB3  1 
ATOM   4692  N  N    . SER A 1 285 ? 7.441   -17.339 12.818  1.00 12.36  ?  508  SER A N    1 
ATOM   4693  C  CA   . SER A 1 285 ? 6.950   -17.540 11.463  1.00 11.93  ?  508  SER A CA   1 
ATOM   4694  C  C    . SER A 1 285 ? 6.237   -16.267 11.031  1.00 11.58  ?  508  SER A C    1 
ATOM   4695  O  O    . SER A 1 285 ? 5.900   -15.430 11.870  1.00 11.92  ?  508  SER A O    1 
ATOM   4696  C  CB   . SER A 1 285 ? 6.018   -18.758 11.376  1.00 12.27  ?  508  SER A CB   1 
ATOM   4697  O  OG   . SER A 1 285 ? 4.882   -18.609 12.207  1.00 11.66  ?  508  SER A OG   1 
ATOM   4698  H  H    . SER A 1 285 ? 6.949   -16.813 13.288  1.00 14.84  ?  508  SER A H    1 
ATOM   4699  H  HA   . SER A 1 285 ? 7.691   -17.693 10.856  1.00 14.31  ?  508  SER A HA   1 
ATOM   4700  H  HB2  . SER A 1 285 ? 5.721   -18.859 10.458  1.00 14.72  ?  508  SER A HB2  1 
ATOM   4701  H  HB3  . SER A 1 285 ? 6.508   -19.547 11.655  1.00 14.72  ?  508  SER A HB3  1 
ATOM   4702  H  HG   . SER A 1 285 ? 5.111   -18.648 13.014  1.00 14.00  ?  508  SER A HG   1 
ATOM   4703  N  N    . PRO A 1 286 ? 5.996   -16.097 9.732   1.00 12.10  ?  509  PRO A N    1 
ATOM   4704  C  CA   . PRO A 1 286 ? 5.378   -14.862 9.237   1.00 12.21  ?  509  PRO A CA   1 
ATOM   4705  C  C    . PRO A 1 286 ? 4.092   -14.516 9.978   1.00 11.83  ?  509  PRO A C    1 
ATOM   4706  O  O    . PRO A 1 286 ? 3.232   -15.367 10.215  1.00 11.99  ?  509  PRO A O    1 
ATOM   4707  C  CB   . PRO A 1 286 ? 5.132   -15.172 7.750   1.00 13.03  ?  509  PRO A CB   1 
ATOM   4708  C  CG   . PRO A 1 286 ? 6.237   -16.117 7.405   1.00 14.38  ?  509  PRO A CG   1 
ATOM   4709  C  CD   . PRO A 1 286 ? 6.406   -16.984 8.630   1.00 13.57  ?  509  PRO A CD   1 
ATOM   4710  H  HA   . PRO A 1 286 ? 5.991   -14.115 9.323   1.00 14.65  ?  509  PRO A HA   1 
ATOM   4711  H  HB2  . PRO A 1 286 ? 4.264   -15.587 7.631   1.00 15.64  ?  509  PRO A HB2  1 
ATOM   4712  H  HB3  . PRO A 1 286 ? 5.186   -14.360 7.223   1.00 15.64  ?  509  PRO A HB3  1 
ATOM   4713  H  HG2  . PRO A 1 286 ? 5.987   -16.650 6.634   1.00 17.25  ?  509  PRO A HG2  1 
ATOM   4714  H  HG3  . PRO A 1 286 ? 7.049   -15.621 7.216   1.00 17.25  ?  509  PRO A HG3  1 
ATOM   4715  H  HD2  . PRO A 1 286 ? 5.831   -17.764 8.583   1.00 16.29  ?  509  PRO A HD2  1 
ATOM   4716  H  HD3  . PRO A 1 286 ? 7.330   -17.259 8.734   1.00 16.29  ?  509  PRO A HD3  1 
ATOM   4717  N  N    . ILE A 1 287 ? 3.974   -13.237 10.335  1.00 11.02  ?  510  ILE A N    1 
ATOM   4718  C  CA   . ILE A 1 287 ? 2.795   -12.679 10.992  1.00 10.67  ?  510  ILE A CA   1 
ATOM   4719  C  C    . ILE A 1 287 ? 1.957   -12.003 9.914   1.00 10.46  ?  510  ILE A C    1 
ATOM   4720  O  O    . ILE A 1 287 ? 2.287   -10.930 9.416   1.00 11.45  ?  510  ILE A O    1 
ATOM   4721  C  CB   . ILE A 1 287 ? 3.191   -11.716 12.112  1.00 10.61  ?  510  ILE A CB   1 
ATOM   4722  C  CG1  . ILE A 1 287 ? 3.977   -12.473 13.182  1.00 11.19  ?  510  ILE A CG1  1 
ATOM   4723  C  CG2  . ILE A 1 287 ? 1.959   -11.046 12.722  1.00 10.68  ?  510  ILE A CG2  1 
ATOM   4724  C  CD1  . ILE A 1 287 ? 4.598   -11.572 14.224  1.00 11.72  ?  510  ILE A CD1  1 
ATOM   4725  H  H    . ILE A 1 287 ? 4.589   -12.651 10.201  1.00 13.23  ?  510  ILE A H    1 
ATOM   4726  H  HA   . ILE A 1 287 ? 2.264   -13.394 11.376  1.00 12.80  ?  510  ILE A HA   1 
ATOM   4727  H  HB   . ILE A 1 287 ? 3.750   -11.018 11.737  1.00 12.73  ?  510  ILE A HB   1 
ATOM   4728  H  HG12 . ILE A 1 287 ? 3.377   -13.085 13.637  1.00 13.43  ?  510  ILE A HG12 1 
ATOM   4729  H  HG13 . ILE A 1 287 ? 4.692   -12.969 12.753  1.00 13.43  ?  510  ILE A HG13 1 
ATOM   4730  H  HG21 . ILE A 1 287 ? 2.236   -10.503 13.476  1.00 12.82  ?  510  ILE A HG21 1 
ATOM   4731  H  HG22 . ILE A 1 287 ? 1.537   -10.489 12.049  1.00 12.82  ?  510  ILE A HG22 1 
ATOM   4732  H  HG23 . ILE A 1 287 ? 1.341   -11.733 13.018  1.00 12.82  ?  510  ILE A HG23 1 
ATOM   4733  H  HD11 . ILE A 1 287 ? 5.238   -12.083 14.743  1.00 14.06  ?  510  ILE A HD11 1 
ATOM   4734  H  HD12 . ILE A 1 287 ? 5.047   -10.836 13.778  1.00 14.06  ?  510  ILE A HD12 1 
ATOM   4735  H  HD13 . ILE A 1 287 ? 3.899   -11.230 14.803  1.00 14.06  ?  510  ILE A HD13 1 
ATOM   4736  N  N    . ASN A 1 288 ? 0.869   -12.650 9.513   1.00 10.20  ?  511  ASN A N    1 
ATOM   4737  C  CA   . ASN A 1 288 ? 0.097   -12.223 8.342   1.00 10.35  ?  511  ASN A CA   1 
ATOM   4738  C  C    . ASN A 1 288 ? -1.020  -11.294 8.791   1.00 10.20  ?  511  ASN A C    1 
ATOM   4739  O  O    . ASN A 1 288 ? -2.121  -11.718 9.126   1.00 10.15  ?  511  ASN A O    1 
ATOM   4740  C  CB   . ASN A 1 288 ? -0.395  -13.450 7.591   1.00 10.18  ?  511  ASN A CB   1 
ATOM   4741  C  CG   . ASN A 1 288 ? 0.746   -14.178 6.906   1.00 10.42  ?  511  ASN A CG   1 
ATOM   4742  O  OD1  . ASN A 1 288 ? 1.554   -13.551 6.217   1.00 11.62  ?  511  ASN A OD1  1 
ATOM   4743  N  ND2  . ASN A 1 288 ? 0.842   -15.487 7.103   1.00 9.93   ?  511  ASN A ND2  1 
ATOM   4744  H  H    . ASN A 1 288 ? 0.551   -13.347 9.904   1.00 12.25  ?  511  ASN A H    1 
ATOM   4745  H  HA   . ASN A 1 288 ? 0.653   -11.699 7.744   1.00 12.42  ?  511  ASN A HA   1 
ATOM   4746  H  HB2  . ASN A 1 288 ? -0.815  -14.062 8.216   1.00 12.22  ?  511  ASN A HB2  1 
ATOM   4747  H  HB3  . ASN A 1 288 ? -1.034  -13.178 6.914   1.00 12.22  ?  511  ASN A HB3  1 
ATOM   4748  H  HD21 . ASN A 1 288 ? 1.477   -15.933 6.731   1.00 11.92  ?  511  ASN A HD21 1 
ATOM   4749  H  HD22 . ASN A 1 288 ? 0.271   -15.890 7.604   1.00 11.92  ?  511  ASN A HD22 1 
ATOM   4750  N  N    . VAL A 1 289 ? -0.715  -9.999  8.799   1.00 10.60  ?  512  VAL A N    1 
ATOM   4751  C  CA   . VAL A 1 289 ? -1.662  -8.956  9.192   1.00 11.22  ?  512  VAL A CA   1 
ATOM   4752  C  C    . VAL A 1 289 ? -1.663  -7.866  8.129   1.00 11.55  ?  512  VAL A C    1 
ATOM   4753  O  O    . VAL A 1 289 ? -0.680  -7.698  7.392   1.00 13.40  ?  512  VAL A O    1 
ATOM   4754  C  CB   . VAL A 1 289 ? -1.319  -8.347  10.571  1.00 11.89  ?  512  VAL A CB   1 
ATOM   4755  C  CG1  . VAL A 1 289 ? -1.526  -9.372  11.670  1.00 12.32  ?  512  VAL A CG1  1 
ATOM   4756  C  CG2  . VAL A 1 289 ? 0.108   -7.784  10.606  1.00 13.00  ?  512  VAL A CG2  1 
ATOM   4757  H  H    . VAL A 1 289 ? 0.056   -9.689  8.575   1.00 12.73  ?  512  VAL A H    1 
ATOM   4758  H  HA   . VAL A 1 289 ? -2.547  -9.351  9.237   1.00 13.47  ?  512  VAL A HA   1 
ATOM   4759  H  HB   . VAL A 1 289 ? -1.920  -7.603  10.731  1.00 14.27  ?  512  VAL A HB   1 
ATOM   4760  H  HG11 . VAL A 1 289 ? -1.307  -8.969  12.524  1.00 14.78  ?  512  VAL A HG11 1 
ATOM   4761  H  HG12 . VAL A 1 289 ? -2.454  -9.655  11.666  1.00 14.78  ?  512  VAL A HG12 1 
ATOM   4762  H  HG13 . VAL A 1 289 ? -0.948  -10.133 11.505  1.00 14.78  ?  512  VAL A HG13 1 
ATOM   4763  H  HG21 . VAL A 1 289 ? 0.300   -7.464  11.501  1.00 15.60  ?  512  VAL A HG21 1 
ATOM   4764  H  HG22 . VAL A 1 289 ? 0.731   -8.488  10.366  1.00 15.60  ?  512  VAL A HG22 1 
ATOM   4765  H  HG23 . VAL A 1 289 ? 0.175   -7.053  9.971   1.00 15.60  ?  512  VAL A HG23 1 
ATOM   4766  N  N    A PRO A 1 290 ? -2.748  -7.095  8.040   0.97 11.11  ?  513  PRO A N    1 
ATOM   4767  C  CA   A PRO A 1 290 ? -2.821  -6.007  7.064   0.97 11.58  ?  513  PRO A CA   1 
ATOM   4768  C  C    A PRO A 1 290 ? -2.043  -4.777  7.509   0.97 11.22  ?  513  PRO A C    1 
ATOM   4769  O  O    A PRO A 1 290 ? -1.893  -4.501  8.699   0.97 12.18  ?  513  PRO A O    1 
ATOM   4770  C  CB   A PRO A 1 290 ? -4.319  -5.691  7.022   0.97 12.58  ?  513  PRO A CB   1 
ATOM   4771  C  CG   A PRO A 1 290 ? -4.803  -6.031  8.382   0.97 12.70  ?  513  PRO A CG   1 
ATOM   4772  C  CD   A PRO A 1 290 ? -4.007  -7.239  8.798   0.97 12.21  ?  513  PRO A CD   1 
ATOM   4773  H  HA   A PRO A 1 290 ? -2.503  -6.304  6.197   0.97 13.90  ?  513  PRO A HA   1 
ATOM   4774  H  HB2  A PRO A 1 290 ? -4.455  -4.750  6.827   0.97 15.10  ?  513  PRO A HB2  1 
ATOM   4775  H  HB3  A PRO A 1 290 ? -4.756  -6.236  6.349   0.97 15.10  ?  513  PRO A HB3  1 
ATOM   4776  H  HG2  A PRO A 1 290 ? -4.642  -5.287  8.984   0.97 15.25  ?  513  PRO A HG2  1 
ATOM   4777  H  HG3  A PRO A 1 290 ? -5.751  -6.235  8.352   0.97 15.25  ?  513  PRO A HG3  1 
ATOM   4778  H  HD2  A PRO A 1 290 ? -3.837  -7.229  9.754   0.97 14.65  ?  513  PRO A HD2  1 
ATOM   4779  H  HD3  A PRO A 1 290 ? -4.466  -8.057  8.552   0.97 14.65  ?  513  PRO A HD3  1 
ATOM   4780  N  N    . ALA A 1 291 ? -1.569  -4.025  6.515   1.00 12.01  ?  514  ALA A N    1 
ATOM   4781  C  CA   . ALA A 1 291 ? -0.852  -2.788  6.797   1.00 13.25  ?  514  ALA A CA   1 
ATOM   4782  C  C    . ALA A 1 291 ? -1.688  -1.767  7.558   1.00 11.65  ?  514  ALA A C    1 
ATOM   4783  O  O    . ALA A 1 291 ? -1.122  -0.902  8.226   1.00 12.28  ?  514  ALA A O    1 
ATOM   4784  C  CB   . ALA A 1 291 ? -0.359  -2.164  5.500   1.00 14.65  ?  514  ALA A CB   1 
ATOM   4785  H  H    . ALA A 1 291 ? -1.649  -4.208  5.678   1.00 14.41  ?  514  ALA A H    1 
ATOM   4786  H  HA   . ALA A 1 291 ? -0.093  -3.018  7.355   1.00 15.90  ?  514  ALA A HA   1 
ATOM   4787  H  HB1  . ALA A 1 291 ? 0.129   -1.351  5.707   1.00 17.58  ?  514  ALA A HB1  1 
ATOM   4788  H  HB2  . ALA A 1 291 ? 0.224   -2.794  5.048   1.00 17.58  ?  514  ALA A HB2  1 
ATOM   4789  H  HB3  . ALA A 1 291 ? -1.123  -1.958  4.939   1.00 17.58  ?  514  ALA A HB3  1 
ATOM   4790  N  N    . ASN A 1 292 ? -3.015  -1.812  7.445   1.00 11.49  ?  515  ASN A N    1 
ATOM   4791  C  CA   . ASN A 1 292 ? -3.862  -0.833  8.108   1.00 11.45  ?  515  ASN A CA   1 
ATOM   4792  C  C    . ASN A 1 292 ? -4.210  -1.207  9.550   1.00 10.54  ?  515  ASN A C    1 
ATOM   4793  O  O    . ASN A 1 292 ? -4.983  -0.479  10.189  1.00 11.49  ?  515  ASN A O    1 
ATOM   4794  C  CB   . ASN A 1 292 ? -5.153  -0.590  7.317   1.00 12.66  ?  515  ASN A CB   1 
ATOM   4795  C  CG   . ASN A 1 292 ? -6.091  -1.786  7.330   1.00 13.42  ?  515  ASN A CG   1 
ATOM   4796  O  OD1  . ASN A 1 292 ? -5.817  -2.815  7.950   1.00 13.28  ?  515  ASN A OD1  1 
ATOM   4797  N  ND2  . ASN A 1 292 ? -7.214  -1.650  6.659   1.00 14.62  ?  515  ASN A ND2  1 
ATOM   4798  H  H    . ASN A 1 292 ? -3.445  -2.401  6.989   1.00 13.80  ?  515  ASN A H    1 
ATOM   4799  H  HA   . ASN A 1 292 ? -3.370  0.003   8.128   1.00 13.74  ?  515  ASN A HA   1 
ATOM   4800  H  HB2  . ASN A 1 292 ? -5.624  0.163   7.706   1.00 15.20  ?  515  ASN A HB2  1 
ATOM   4801  H  HB3  . ASN A 1 292 ? -4.925  -0.399  6.394   1.00 15.20  ?  515  ASN A HB3  1 
ATOM   4802  H  HD21 . ASN A 1 292 ? -7.780  -2.297  6.633   1.00 17.55  ?  515  ASN A HD21 1 
ATOM   4803  H  HD22 . ASN A 1 292 ? -7.382  -0.915  6.245   1.00 17.55  ?  515  ASN A HD22 1 
ATOM   4804  N  N    . GLY A 1 293 ? -3.643  -2.291  10.083  1.00 10.35  ?  516  GLY A N    1 
ATOM   4805  C  CA   . GLY A 1 293 ? -4.078  -2.799  11.369  1.00 8.86   ?  516  GLY A CA   1 
ATOM   4806  C  C    . GLY A 1 293 ? -3.525  -2.015  12.545  1.00 7.94   ?  516  GLY A C    1 
ATOM   4807  O  O    . GLY A 1 293 ? -2.476  -1.386  12.483  1.00 8.81   ?  516  GLY A O    1 
ATOM   4808  H  H    . GLY A 1 293 ? -3.010  -2.744  9.718   1.00 12.43  ?  516  GLY A H    1 
ATOM   4809  H  HA2  . GLY A 1 293 ? -5.046  -2.764  11.413  1.00 10.63  ?  516  GLY A HA2  1 
ATOM   4810  H  HA3  . GLY A 1 293 ? -3.790  -3.720  11.460  1.00 10.63  ?  516  GLY A HA3  1 
ATOM   4811  N  N    . TYR A 1 294 ? -4.260  -2.059  13.651  1.00 7.76   ?  517  TYR A N    1 
ATOM   4812  C  CA   . TYR A 1 294 ? -3.778  -1.454  14.883  1.00 7.44   ?  517  TYR A CA   1 
ATOM   4813  C  C    . TYR A 1 294 ? -4.429  -2.131  16.078  1.00 7.42   ?  517  TYR A C    1 
ATOM   4814  O  O    . TYR A 1 294 ? -5.470  -2.775  15.966  1.00 7.78   ?  517  TYR A O    1 
ATOM   4815  C  CB   . TYR A 1 294 ? -4.033  0.065   14.923  1.00 8.13   ?  517  TYR A CB   1 
ATOM   4816  C  CG   . TYR A 1 294 ? -5.484  0.469   14.877  1.00 8.94   ?  517  TYR A CG   1 
ATOM   4817  C  CD1  . TYR A 1 294 ? -6.241  0.532   16.034  1.00 9.98   ?  517  TYR A CD1  1 
ATOM   4818  C  CD2  . TYR A 1 294 ? -6.091  0.813   13.681  1.00 11.58  ?  517  TYR A CD2  1 
ATOM   4819  C  CE1  . TYR A 1 294 ? -7.584  0.888   15.991  1.00 11.97  ?  517  TYR A CE1  1 
ATOM   4820  C  CE2  . TYR A 1 294 ? -7.427  1.186   13.632  1.00 12.95  ?  517  TYR A CE2  1 
ATOM   4821  C  CZ   . TYR A 1 294 ? -8.166  1.215   14.791  1.00 14.01  ?  517  TYR A CZ   1 
ATOM   4822  O  OH   . TYR A 1 294 ? -9.495  1.584   14.751  1.00 16.44  ?  517  TYR A OH   1 
ATOM   4823  H  H    . TYR A 1 294 ? -5.033  -2.430  13.711  1.00 9.32   ?  517  TYR A H    1 
ATOM   4824  H  HA   . TYR A 1 294 ? -2.821  -1.601  14.940  1.00 8.93   ?  517  TYR A HA   1 
ATOM   4825  H  HB2  . TYR A 1 294 ? -3.659  0.418   15.746  1.00 9.76   ?  517  TYR A HB2  1 
ATOM   4826  H  HB3  . TYR A 1 294 ? -3.593  0.471   14.159  1.00 9.76   ?  517  TYR A HB3  1 
ATOM   4827  H  HD1  . TYR A 1 294 ? -5.846  0.332   16.852  1.00 11.97  ?  517  TYR A HD1  1 
ATOM   4828  H  HD2  . TYR A 1 294 ? -5.594  0.795   12.895  1.00 13.90  ?  517  TYR A HD2  1 
ATOM   4829  H  HE1  . TYR A 1 294 ? -8.087  0.905   16.773  1.00 14.37  ?  517  TYR A HE1  1 
ATOM   4830  H  HE2  . TYR A 1 294 ? -7.820  1.414   12.821  1.00 15.54  ?  517  TYR A HE2  1 
ATOM   4831  H  HH   . TYR A 1 294 ? -9.825  1.550   15.523  1.00 19.73  ?  517  TYR A HH   1 
ATOM   4832  N  N    . PHE A 1 295 ? -3.790  -1.972  17.235  1.00 6.53   ?  518  PHE A N    1 
ATOM   4833  C  CA   . PHE A 1 295 ? -4.299  -2.537  18.470  1.00 6.95   ?  518  PHE A CA   1 
ATOM   4834  C  C    . PHE A 1 295 ? -5.335  -1.618  19.104  1.00 6.59   ?  518  PHE A C    1 
ATOM   4835  O  O    . PHE A 1 295 ? -5.165  -0.396  19.152  1.00 7.74   ?  518  PHE A O    1 
ATOM   4836  C  CB   . PHE A 1 295 ? -3.158  -2.748  19.465  1.00 7.01   ?  518  PHE A CB   1 
ATOM   4837  C  CG   . PHE A 1 295 ? -2.395  -4.017  19.258  1.00 7.06   ?  518  PHE A CG   1 
ATOM   4838  C  CD1  . PHE A 1 295 ? -3.003  -5.246  19.460  1.00 7.96   ?  518  PHE A CD1  1 
ATOM   4839  C  CD2  . PHE A 1 295 ? -1.055  -3.982  18.925  1.00 7.55   ?  518  PHE A CD2  1 
ATOM   4840  C  CE1  . PHE A 1 295 ? -2.297  -6.420  19.311  1.00 8.29   ?  518  PHE A CE1  1 
ATOM   4841  C  CE2  . PHE A 1 295 ? -0.348  -5.150  18.765  1.00 7.93   ?  518  PHE A CE2  1 
ATOM   4842  C  CZ   . PHE A 1 295 ? -0.975  -6.376  18.963  1.00 8.60   ?  518  PHE A CZ   1 
ATOM   4843  H  H    . PHE A 1 295 ? -3.054  -1.537  17.327  1.00 7.83   ?  518  PHE A H    1 
ATOM   4844  H  HA   . PHE A 1 295 ? -4.716  -3.390  18.273  1.00 8.34   ?  518  PHE A HA   1 
ATOM   4845  H  HB2  . PHE A 1 295 ? -2.533  -2.012  19.382  1.00 8.41   ?  518  PHE A HB2  1 
ATOM   4846  H  HB3  . PHE A 1 295 ? -3.528  -2.770  20.361  1.00 8.41   ?  518  PHE A HB3  1 
ATOM   4847  H  HD1  . PHE A 1 295 ? -3.901  -5.280  19.699  1.00 9.55   ?  518  PHE A HD1  1 
ATOM   4848  H  HD2  . PHE A 1 295 ? -0.629  -3.163  18.808  1.00 9.07   ?  518  PHE A HD2  1 
ATOM   4849  H  HE1  . PHE A 1 295 ? -2.717  -7.239  19.446  1.00 9.95   ?  518  PHE A HE1  1 
ATOM   4850  H  HE2  . PHE A 1 295 ? 0.550   -5.121  18.525  1.00 9.51   ?  518  PHE A HE2  1 
ATOM   4851  H  HZ   . PHE A 1 295 ? -0.495  -7.165  18.859  1.00 10.32  ?  518  PHE A HZ   1 
ATOM   4852  N  N    . ARG A 1 296 ? -6.379  -2.240  19.645  0.93 6.84   ?  519  ARG A N    1 
ATOM   4853  C  CA   . ARG A 1 296 ? -7.457  -1.579  20.360  0.93 7.61   ?  519  ARG A CA   1 
ATOM   4854  C  C    . ARG A 1 296 ? -7.617  -2.220  21.733  0.93 6.83   ?  519  ARG A C    1 
ATOM   4855  O  O    . ARG A 1 296 ? -7.671  -3.448  21.856  0.93 7.67   ?  519  ARG A O    1 
ATOM   4856  C  CB   . ARG A 1 296 ? -8.728  -1.765  19.540  0.93 10.42  ?  519  ARG A CB   1 
ATOM   4857  C  CG   . ARG A 1 296 ? -9.967  -1.106  20.054  0.93 12.88  ?  519  ARG A CG   1 
ATOM   4858  C  CD   . ARG A 1 296 ? -11.175 -1.608  19.245  0.93 15.57  ?  519  ARG A CD   1 
ATOM   4859  N  NE   . ARG A 1 296 ? -11.430 -3.019  19.527  0.93 18.76  ?  519  ARG A NE   1 
ATOM   4860  C  CZ   . ARG A 1 296 ? -12.201 -3.825  18.810  0.93 20.30  ?  519  ARG A CZ   1 
ATOM   4861  N  NH1  . ARG A 1 296 ? -12.791 -3.416  17.697  0.93 20.27  ?  519  ARG A NH1  1 
ATOM   4862  N  NH2  . ARG A 1 296 ? -12.378 -5.078  19.216  0.93 21.18  ?  519  ARG A NH2  1 
ATOM   4863  H  H    . ARG A 1 296 ? -6.488  -3.092  19.607  0.93 8.21   ?  519  ARG A H    1 
ATOM   4864  H  HA   . ARG A 1 296 ? -7.273  -0.638  20.504  0.93 9.14   ?  519  ARG A HA   1 
ATOM   4865  H  HB2  . ARG A 1 296 ? -8.566  -1.409  18.652  0.93 12.51  ?  519  ARG A HB2  1 
ATOM   4866  H  HB3  . ARG A 1 296 ? -8.914  -2.715  19.488  0.93 12.51  ?  519  ARG A HB3  1 
ATOM   4867  H  HG2  . ARG A 1 296 ? -10.098 -1.332  20.988  0.93 15.45  ?  519  ARG A HG2  1 
ATOM   4868  H  HG3  . ARG A 1 296 ? -9.897  -0.144  19.952  0.93 15.45  ?  519  ARG A HG3  1 
ATOM   4869  H  HD2  . ARG A 1 296 ? -11.963 -1.096  19.486  0.93 18.69  ?  519  ARG A HD2  1 
ATOM   4870  H  HD3  . ARG A 1 296 ? -10.993 -1.510  18.297  0.93 18.69  ?  519  ARG A HD3  1 
ATOM   4871  H  HE   . ARG A 1 296 ? -11.047 -3.356  20.220  0.93 22.51  ?  519  ARG A HE   1 
ATOM   4872  H  HH11 . ARG A 1 296 ? -12.679 -2.608  17.423  0.93 24.32  ?  519  ARG A HH11 1 
ATOM   4873  H  HH12 . ARG A 1 296 ? -13.286 -3.957  17.249  0.93 24.32  ?  519  ARG A HH12 1 
ATOM   4874  H  HH21 . ARG A 1 296 ? -11.996 -5.355  19.935  0.93 25.42  ?  519  ARG A HH21 1 
ATOM   4875  H  HH22 . ARG A 1 296 ? -12.876 -5.611  18.761  0.93 25.42  ?  519  ARG A HH22 1 
ATOM   4876  N  N    . PHE A 1 297 ? -7.706  -1.384  22.765  1.00 7.41   ?  520  PHE A N    1 
ATOM   4877  C  CA   . PHE A 1 297 ? -7.990  -1.873  24.106  1.00 8.32   ?  520  PHE A CA   1 
ATOM   4878  C  C    . PHE A 1 297 ? -9.406  -2.410  24.181  1.00 9.78   ?  520  PHE A C    1 
ATOM   4879  O  O    . PHE A 1 297 ? -10.357 -1.727  23.796  1.00 12.59  ?  520  PHE A O    1 
ATOM   4880  C  CB   . PHE A 1 297 ? -7.832  -0.743  25.114  1.00 9.24   ?  520  PHE A CB   1 
ATOM   4881  C  CG   . PHE A 1 297 ? -8.301  -1.112  26.495  1.00 10.90  ?  520  PHE A CG   1 
ATOM   4882  C  CD1  . PHE A 1 297 ? -7.633  -2.073  27.224  1.00 10.68  ?  520  PHE A CD1  1 
ATOM   4883  C  CD2  . PHE A 1 297 ? -9.419  -0.532  27.047  1.00 13.38  ?  520  PHE A CD2  1 
ATOM   4884  C  CE1  . PHE A 1 297 ? -8.059  -2.425  28.492  1.00 10.78  ?  520  PHE A CE1  1 
ATOM   4885  C  CE2  . PHE A 1 297 ? -9.853  -0.891  28.308  1.00 14.06  ?  520  PHE A CE2  1 
ATOM   4886  C  CZ   . PHE A 1 297 ? -9.167  -1.835  29.030  1.00 12.36  ?  520  PHE A CZ   1 
ATOM   4887  H  H    . PHE A 1 297 ? -7.605  -0.531  22.713  1.00 8.90   ?  520  PHE A H    1 
ATOM   4888  H  HA   . PHE A 1 297 ? -7.369  -2.586  24.323  1.00 9.99   ?  520  PHE A HA   1 
ATOM   4889  H  HB2  . PHE A 1 297 ? -6.894  -0.503  25.172  1.00 11.09  ?  520  PHE A HB2  1 
ATOM   4890  H  HB3  . PHE A 1 297 ? -8.352  0.019   24.816  1.00 11.09  ?  520  PHE A HB3  1 
ATOM   4891  H  HD1  . PHE A 1 297 ? -6.887  -2.490  26.858  1.00 12.82  ?  520  PHE A HD1  1 
ATOM   4892  H  HD2  . PHE A 1 297 ? -9.889  0.110   26.565  1.00 16.06  ?  520  PHE A HD2  1 
ATOM   4893  H  HE1  . PHE A 1 297 ? -7.591  -3.065  28.979  1.00 12.94  ?  520  PHE A HE1  1 
ATOM   4894  H  HE2  . PHE A 1 297 ? -10.611 -0.491  28.670  1.00 16.87  ?  520  PHE A HE2  1 
ATOM   4895  H  HZ   . PHE A 1 297 ? -9.455  -2.072  29.882  1.00 14.84  ?  520  PHE A HZ   1 
ATOM   4896  N  N    . ASP A 1 298 ? -9.557  -3.629  24.691  1.00 9.75   ?  521  ASP A N    1 
ATOM   4897  C  CA   A ASP A 1 298 ? -10.850 -4.291  24.848  0.63 10.90  ?  521  ASP A CA   1 
ATOM   4898  C  CA   B ASP A 1 298 ? -10.893 -4.170  24.851  0.37 10.72  ?  521  ASP A CA   1 
ATOM   4899  C  C    . ASP A 1 298 ? -11.339 -4.325  26.293  1.00 10.63  ?  521  ASP A C    1 
ATOM   4900  O  O    . ASP A 1 298 ? -12.466 -3.931  26.595  1.00 11.98  ?  521  ASP A O    1 
ATOM   4901  C  CB   A ASP A 1 298 ? -10.766 -5.742  24.345  0.63 12.72  ?  521  ASP A CB   1 
ATOM   4902  C  CB   B ASP A 1 298 ? -11.069 -5.450  24.033  0.37 12.02  ?  521  ASP A CB   1 
ATOM   4903  C  CG   A ASP A 1 298 ? -12.083 -6.494  24.500  0.63 14.31  ?  521  ASP A CG   1 
ATOM   4904  C  CG   B ASP A 1 298 ? -11.258 -5.144  22.548  0.37 12.58  ?  521  ASP A CG   1 
ATOM   4905  O  OD1  A ASP A 1 298 ? -12.967 -6.342  23.633  0.63 15.81  -1 521  ASP A OD1  1 
ATOM   4906  O  OD1  B ASP A 1 298 ? -11.330 -3.940  22.198  0.37 13.69  -1 521  ASP A OD1  1 
ATOM   4907  O  OD2  A ASP A 1 298 ? -12.243 -7.223  25.496  0.63 13.93  -1 521  ASP A OD2  1 
ATOM   4908  O  OD2  B ASP A 1 298 ? -11.333 -6.079  21.733  0.37 12.47  -1 521  ASP A OD2  1 
ATOM   4909  H  H    A ASP A 1 298 ? -8.900  -4.112  24.964  0.63 11.70  ?  521  ASP A H    1 
ATOM   4910  H  H    B ASP A 1 298 ? -8.916  -4.143  24.943  0.37 11.70  ?  521  ASP A H    1 
ATOM   4911  H  HA   A ASP A 1 298 ? -11.493 -3.799  24.315  0.63 13.08  ?  521  ASP A HA   1 
ATOM   4912  H  HA   B ASP A 1 298 ? -11.530 -3.547  24.467  0.37 12.87  ?  521  ASP A HA   1 
ATOM   4913  H  HB2  A ASP A 1 298 ? -10.531 -5.738  23.404  0.63 15.26  ?  521  ASP A HB2  1 
ATOM   4914  H  HB2  B ASP A 1 298 ? -10.280 -6.006  24.132  0.37 14.43  ?  521  ASP A HB2  1 
ATOM   4915  H  HB3  A ASP A 1 298 ? -10.089 -6.215  24.854  0.63 15.26  ?  521  ASP A HB3  1 
ATOM   4916  H  HB3  B ASP A 1 298 ? -11.853 -5.928  24.348  0.37 14.43  ?  521  ASP A HB3  1 
ATOM   4917  N  N    . SER A 1 299 ? -10.513 -4.833  27.207  1.00 9.91   ?  522  SER A N    1 
ATOM   4918  C  CA   . SER A 1 299 ? -10.986 -5.021  28.577  1.00 10.20  ?  522  SER A CA   1 
ATOM   4919  C  C    . SER A 1 299 ? -9.811  -5.300  29.501  1.00 9.47   ?  522  SER A C    1 
ATOM   4920  O  O    . SER A 1 299 ? -8.724  -5.668  29.057  1.00 9.57   ?  522  SER A O    1 
ATOM   4921  C  CB   . SER A 1 299 ? -11.990 -6.178  28.662  1.00 12.28  ?  522  SER A CB   1 
ATOM   4922  O  OG   . SER A 1 299 ? -11.434 -7.352  28.123  1.00 13.81  ?  522  SER A OG   1 
ATOM   4923  H  H    . SER A 1 299 ? -9.699  -5.070  27.061  1.00 11.90  ?  522  SER A H    1 
ATOM   4924  H  HA   . SER A 1 299 ? -11.405 -4.197  28.871  1.00 12.24  ?  522  SER A HA   1 
ATOM   4925  H  HB2  . SER A 1 299 ? -12.218 -6.333  29.592  1.00 14.73  ?  522  SER A HB2  1 
ATOM   4926  H  HB3  . SER A 1 299 ? -12.786 -5.945  28.159  1.00 14.73  ?  522  SER A HB3  1 
ATOM   4927  H  HG   . SER A 1 299 ? -11.239 -7.233  27.315  1.00 16.57  ?  522  SER A HG   1 
ATOM   4928  N  N    . TRP A 1 300 ? -10.054 -5.137  30.798  1.00 10.21  ?  523  TRP A N    1 
ATOM   4929  C  CA   . TRP A 1 300 ? -9.060  -5.437  31.816  1.00 10.12  ?  523  TRP A CA   1 
ATOM   4930  C  C    . TRP A 1 300 ? -9.158  -6.896  32.228  1.00 10.64  ?  523  TRP A C    1 
ATOM   4931  O  O    . TRP A 1 300 ? -10.235 -7.368  32.596  1.00 12.25  ?  523  TRP A O    1 
ATOM   4932  C  CB   . TRP A 1 300 ? -9.285  -4.548  33.037  1.00 10.14  ?  523  TRP A CB   1 
ATOM   4933  C  CG   . TRP A 1 300 ? -9.060  -3.111  32.748  1.00 9.81   ?  523  TRP A CG   1 
ATOM   4934  C  CD1  . TRP A 1 300 ? -10.006 -2.141  32.631  1.00 11.02  ?  523  TRP A CD1  1 
ATOM   4935  C  CD2  . TRP A 1 300 ? -7.801  -2.475  32.536  1.00 9.68   ?  523  TRP A CD2  1 
ATOM   4936  N  NE1  . TRP A 1 300 ? -9.421  -0.935  32.366  1.00 11.24  ?  523  TRP A NE1  1 
ATOM   4937  C  CE2  . TRP A 1 300 ? -8.064  -1.111  32.296  1.00 10.91  ?  523  TRP A CE2  1 
ATOM   4938  C  CE3  . TRP A 1 300 ? -6.481  -2.923  32.524  1.00 9.57   ?  523  TRP A CE3  1 
ATOM   4939  C  CZ2  . TRP A 1 300 ? -7.058  -0.194  32.039  1.00 11.78  ?  523  TRP A CZ2  1 
ATOM   4940  C  CZ3  . TRP A 1 300 ? -5.480  -2.010  32.269  1.00 10.71  ?  523  TRP A CZ3  1 
ATOM   4941  C  CH2  . TRP A 1 300 ? -5.773  -0.656  32.035  1.00 10.97  ?  523  TRP A CH2  1 
ATOM   4942  H  H    . TRP A 1 300 ? -10.800 -4.849  31.116  1.00 12.25  ?  523  TRP A H    1 
ATOM   4943  H  HA   . TRP A 1 300 ? -8.173  -5.277  31.457  1.00 12.15  ?  523  TRP A HA   1 
ATOM   4944  H  HB2  . TRP A 1 300 ? -10.200 -4.654  33.341  1.00 12.18  ?  523  TRP A HB2  1 
ATOM   4945  H  HB3  . TRP A 1 300 ? -8.670  -4.814  33.739  1.00 12.18  ?  523  TRP A HB3  1 
ATOM   4946  H  HD1  . TRP A 1 300 ? -10.922 -2.278  32.718  1.00 13.23  ?  523  TRP A HD1  1 
ATOM   4947  H  HE1  . TRP A 1 300 ? -9.835  -0.189  32.261  1.00 13.49  ?  523  TRP A HE1  1 
ATOM   4948  H  HE3  . TRP A 1 300 ? -6.281  -3.816  32.685  1.00 11.48  ?  523  TRP A HE3  1 
ATOM   4949  H  HZ2  . TRP A 1 300 ? -7.250  0.701   31.876  1.00 14.14  ?  523  TRP A HZ2  1 
ATOM   4950  H  HZ3  . TRP A 1 300 ? -4.595  -2.296  32.251  1.00 12.86  ?  523  TRP A HZ3  1 
ATOM   4951  H  HH2  . TRP A 1 300 ? -5.077  -0.061  31.875  1.00 13.17  ?  523  TRP A HH2  1 
ATOM   4952  N  N    . VAL A 1 301 ? -8.032  -7.608  32.164  1.00 10.35  ?  524  VAL A N    1 
ATOM   4953  C  CA   . VAL A 1 301 ? -7.970  -9.022  32.532  1.00 10.53  ?  524  VAL A CA   1 
ATOM   4954  C  C    . VAL A 1 301 ? -6.834  -9.206  33.535  1.00 10.24  ?  524  VAL A C    1 
ATOM   4955  O  O    . VAL A 1 301 ? -6.452  -8.264  34.225  1.00 10.44  ?  524  VAL A O    1 
ATOM   4956  C  CB   . VAL A 1 301 ? -7.858  -9.923  31.287  1.00 10.67  ?  524  VAL A CB   1 
ATOM   4957  C  CG1  . VAL A 1 301 ? -9.061  -9.734  30.357  1.00 12.05  ?  524  VAL A CG1  1 
ATOM   4958  C  CG2  . VAL A 1 301 ? -6.583  -9.676  30.506  1.00 10.20  ?  524  VAL A CG2  1 
ATOM   4959  H  H    . VAL A 1 301 ? -7.276  -7.288  31.906  1.00 12.42  ?  524  VAL A H    1 
ATOM   4960  H  HA   . VAL A 1 301 ? -8.788  -9.294  32.978  1.00 12.63  ?  524  VAL A HA   1 
ATOM   4961  H  HB   . VAL A 1 301 ? -7.841  -10.838 31.610  1.00 12.80  ?  524  VAL A HB   1 
ATOM   4962  H  HG11 . VAL A 1 301 ? -8.979  -10.343 29.607  1.00 14.46  ?  524  VAL A HG11 1 
ATOM   4963  H  HG12 . VAL A 1 301 ? -9.874  -9.923  30.850  1.00 14.46  ?  524  VAL A HG12 1 
ATOM   4964  H  HG13 . VAL A 1 301 ? -9.073  -8.817  30.039  1.00 14.46  ?  524  VAL A HG13 1 
ATOM   4965  H  HG21 . VAL A 1 301 ? -6.577  -10.248 29.722  1.00 12.25  ?  524  VAL A HG21 1 
ATOM   4966  H  HG22 . VAL A 1 301 ? -6.553  -8.745  30.236  1.00 12.25  ?  524  VAL A HG22 1 
ATOM   4967  H  HG23 . VAL A 1 301 ? -5.822  -9.882  31.071  1.00 12.25  ?  524  VAL A HG23 1 
ATOM   4968  N  N    . ASN A 1 302 ? -6.315  -10.416 33.684  1.00 10.84  ?  525  ASN A N    1 
ATOM   4969  C  CA   . ASN A 1 302 ? -5.161  -10.629 34.559  1.00 10.58  ?  525  ASN A CA   1 
ATOM   4970  C  C    . ASN A 1 302 ? -4.163  -11.538 33.851  1.00 10.38  ?  525  ASN A C    1 
ATOM   4971  O  O    . ASN A 1 302 ? -4.372  -11.957 32.710  1.00 10.80  ?  525  ASN A O    1 
ATOM   4972  C  CB   . ASN A 1 302 ? -5.568  -11.119 35.959  1.00 11.99  ?  525  ASN A CB   1 
ATOM   4973  C  CG   . ASN A 1 302 ? -6.196  -12.496 35.951  1.00 14.87  ?  525  ASN A CG   1 
ATOM   4974  O  OD1  . ASN A 1 302 ? -5.873  -13.323 35.114  1.00 14.27  ?  525  ASN A OD1  1 
ATOM   4975  N  ND2  . ASN A 1 302 ? -7.074  -12.752 36.907  1.00 18.63  ?  525  ASN A ND2  1 
ATOM   4976  H  H    . ASN A 1 302 ? -6.608  -11.125 33.294  1.00 13.00  ?  525  ASN A H    1 
ATOM   4977  H  HA   . ASN A 1 302 ? -4.713  -9.781  34.700  1.00 12.70  ?  525  ASN A HA   1 
ATOM   4978  H  HB2  . ASN A 1 302 ? -4.778  -11.155 36.521  1.00 14.39  ?  525  ASN A HB2  1 
ATOM   4979  H  HB3  . ASN A 1 302 ? -6.214  -10.499 36.333  1.00 14.39  ?  525  ASN A HB3  1 
ATOM   4980  H  HD21 . ASN A 1 302 ? -7.262  -12.149 37.491  1.00 22.35  ?  525  ASN A HD21 1 
ATOM   4981  H  HD22 . ASN A 1 302 ? -7.458  -13.521 36.944  1.00 22.35  ?  525  ASN A HD22 1 
ATOM   4982  N  N    . GLN A 1 303 ? -3.063  -11.832 34.544  1.00 10.69  ?  526  GLN A N    1 
ATOM   4983  C  CA   . GLN A 1 303 ? -1.974  -12.578 33.936  1.00 11.74  ?  526  GLN A CA   1 
ATOM   4984  C  C    . GLN A 1 303 ? -2.361  -14.005 33.584  1.00 12.57  ?  526  GLN A C    1 
ATOM   4985  O  O    . GLN A 1 303 ? -1.627  -14.655 32.846  1.00 13.93  ?  526  GLN A O    1 
ATOM   4986  C  CB   . GLN A 1 303 ? -0.770  -12.605 34.870  1.00 11.94  ?  526  GLN A CB   1 
ATOM   4987  C  CG   . GLN A 1 303 ? -1.015  -13.297 36.198  1.00 12.76  ?  526  GLN A CG   1 
ATOM   4988  C  CD   . GLN A 1 303 ? 0.249   -13.443 37.006  1.00 14.52  ?  526  GLN A CD   1 
ATOM   4989  O  OE1  . GLN A 1 303 ? 1.217   -14.043 36.552  1.00 16.00  ?  526  GLN A OE1  1 
ATOM   4990  N  NE2  . GLN A 1 303 ? 0.248   -12.897 38.211  1.00 14.22  ?  526  GLN A NE2  1 
ATOM   4991  H  H    . GLN A 1 303 ? -2.927  -11.610 35.363  1.00 12.83  ?  526  GLN A H    1 
ATOM   4992  H  HA   . GLN A 1 303 ? -1.722  -12.124 33.117  1.00 14.09  ?  526  GLN A HA   1 
ATOM   4993  H  HB2  . GLN A 1 303 ? -0.045  -13.073 34.426  1.00 14.32  ?  526  GLN A HB2  1 
ATOM   4994  H  HB3  . GLN A 1 303 ? -0.507  -11.691 35.061  1.00 14.32  ?  526  GLN A HB3  1 
ATOM   4995  H  HG2  . GLN A 1 303 ? -1.647  -12.775 36.717  1.00 15.31  ?  526  GLN A HG2  1 
ATOM   4996  H  HG3  . GLN A 1 303 ? -1.373  -14.184 36.034  1.00 15.31  ?  526  GLN A HG3  1 
ATOM   4997  H  HE21 . GLN A 1 303 ? -0.451  -12.485 38.496  1.00 17.07  ?  526  GLN A HE21 1 
ATOM   4998  H  HE22 . GLN A 1 303 ? 0.946   -12.954 38.709  1.00 17.07  ?  526  GLN A HE22 1 
ATOM   4999  N  N    . PHE A 1 304 ? -3.470  -14.512 34.111  1.00 12.70  ?  527  PHE A N    1 
ATOM   5000  C  CA   . PHE A 1 304 ? -3.892  -15.885 33.870  1.00 13.71  ?  527  PHE A CA   1 
ATOM   5001  C  C    . PHE A 1 304 ? -4.914  -15.998 32.750  1.00 13.82  ?  527  PHE A C    1 
ATOM   5002  O  O    . PHE A 1 304 ? -5.432  -17.092 32.509  1.00 14.72  ?  527  PHE A O    1 
ATOM   5003  C  CB   . PHE A 1 304 ? -4.408  -16.502 35.168  1.00 15.31  ?  527  PHE A CB   1 
ATOM   5004  C  CG   . PHE A 1 304 ? -3.419  -16.408 36.290  1.00 16.45  ?  527  PHE A CG   1 
ATOM   5005  C  CD1  . PHE A 1 304 ? -2.216  -17.084 36.208  1.00 17.54  ?  527  PHE A CD1  1 
ATOM   5006  C  CD2  . PHE A 1 304 ? -3.667  -15.610 37.395  1.00 17.90  ?  527  PHE A CD2  1 
ATOM   5007  C  CE1  . PHE A 1 304 ? -1.288  -16.994 37.221  1.00 18.08  ?  527  PHE A CE1  1 
ATOM   5008  C  CE2  . PHE A 1 304 ? -2.742  -15.510 38.418  1.00 18.07  ?  527  PHE A CE2  1 
ATOM   5009  C  CZ   . PHE A 1 304 ? -1.550  -16.206 38.334  1.00 18.55  ?  527  PHE A CZ   1 
ATOM   5010  H  H    . PHE A 1 304 ? -4.004  -14.071 34.620  1.00 15.24  ?  527  PHE A H    1 
ATOM   5011  H  HA   . PHE A 1 304 ? -3.126  -16.412 33.594  1.00 16.45  ?  527  PHE A HA   1 
ATOM   5012  H  HB2  . PHE A 1 304 ? -5.215  -16.037 35.439  1.00 18.37  ?  527  PHE A HB2  1 
ATOM   5013  H  HB3  . PHE A 1 304 ? -4.602  -17.440 35.016  1.00 18.37  ?  527  PHE A HB3  1 
ATOM   5014  H  HD1  . PHE A 1 304 ? -2.030  -17.605 35.460  1.00 21.05  ?  527  PHE A HD1  1 
ATOM   5015  H  HD2  . PHE A 1 304 ? -4.465  -15.136 37.449  1.00 21.48  ?  527  PHE A HD2  1 
ATOM   5016  H  HE1  . PHE A 1 304 ? -0.486  -17.461 37.161  1.00 21.69  ?  527  PHE A HE1  1 
ATOM   5017  H  HE2  . PHE A 1 304 ? -2.921  -14.977 39.158  1.00 21.69  ?  527  PHE A HE2  1 
ATOM   5018  H  HZ   . PHE A 1 304 ? -0.926  -16.147 39.021  1.00 22.27  ?  527  PHE A HZ   1 
ATOM   5019  N  N    . TYR A 1 305 ? -5.189  -14.909 32.034  1.00 12.55  ?  528  TYR A N    1 
ATOM   5020  C  CA   . TYR A 1 305 ? -6.125  -14.976 30.924  1.00 12.32  ?  528  TYR A CA   1 
ATOM   5021  C  C    . TYR A 1 305 ? -5.526  -15.842 29.831  1.00 11.53  ?  528  TYR A C    1 
ATOM   5022  O  O    . TYR A 1 305 ? -4.356  -15.689 29.477  1.00 12.17  ?  528  TYR A O    1 
ATOM   5023  C  CB   . TYR A 1 305 ? -6.397  -13.567 30.394  1.00 12.49  ?  528  TYR A CB   1 
ATOM   5024  C  CG   . TYR A 1 305 ? -7.498  -13.507 29.362  1.00 13.37  ?  528  TYR A CG   1 
ATOM   5025  C  CD1  . TYR A 1 305 ? -8.822  -13.365 29.753  1.00 14.76  ?  528  TYR A CD1  1 
ATOM   5026  C  CD2  . TYR A 1 305 ? -7.218  -13.610 28.006  1.00 13.02  ?  528  TYR A CD2  1 
ATOM   5027  C  CE1  . TYR A 1 305 ? -9.839  -13.326 28.833  1.00 15.56  ?  528  TYR A CE1  1 
ATOM   5028  C  CE2  . TYR A 1 305 ? -8.238  -13.563 27.061  1.00 13.96  ?  528  TYR A CE2  1 
ATOM   5029  C  CZ   . TYR A 1 305 ? -9.548  -13.420 27.490  1.00 15.53  ?  528  TYR A CZ   1 
ATOM   5030  O  OH   . TYR A 1 305 ? -10.595 -13.382 26.606  1.00 17.58  ?  528  TYR A OH   1 
ATOM   5031  H  H    . TYR A 1 305 ? -4.849  -14.131 32.171  1.00 15.06  ?  528  TYR A H    1 
ATOM   5032  H  HA   . TYR A 1 305 ? -6.968  -15.360 31.210  1.00 14.79  ?  528  TYR A HA   1 
ATOM   5033  H  HB2  . TYR A 1 305 ? -6.656  -12.999 31.137  1.00 14.99  ?  528  TYR A HB2  1 
ATOM   5034  H  HB3  . TYR A 1 305 ? -5.587  -13.227 29.983  1.00 14.99  ?  528  TYR A HB3  1 
ATOM   5035  H  HD1  . TYR A 1 305 ? -9.024  -13.296 30.658  1.00 17.72  ?  528  TYR A HD1  1 
ATOM   5036  H  HD2  . TYR A 1 305 ? -6.337  -13.712 27.726  1.00 15.62  ?  528  TYR A HD2  1 
ATOM   5037  H  HE1  . TYR A 1 305 ? -10.720 -13.235 29.115  1.00 18.68  ?  528  TYR A HE1  1 
ATOM   5038  H  HE2  . TYR A 1 305 ? -8.044  -13.627 26.154  1.00 16.75  ?  528  TYR A HE2  1 
ATOM   5039  H  HH   . TYR A 1 305 ? -11.320 -13.307 27.022  1.00 21.10  ?  528  TYR A HH   1 
ATOM   5040  N  N    . SER A 1 306 ? -6.334  -16.745 29.291  1.00 11.52  ?  529  SER A N    1 
ATOM   5041  C  CA   A SER A 1 306 ? -5.898  -17.659 28.239  0.51 11.57  ?  529  SER A CA   1 
ATOM   5042  C  CA   B SER A 1 306 ? -5.900  -17.658 28.241  0.49 11.41  ?  529  SER A CA   1 
ATOM   5043  C  C    . SER A 1 306 ? -6.230  -17.048 26.881  1.00 10.79  ?  529  SER A C    1 
ATOM   5044  O  O    . SER A 1 306 ? -7.394  -17.002 26.481  1.00 11.57  ?  529  SER A O    1 
ATOM   5045  C  CB   A SER A 1 306 ? -6.578  -19.016 28.404  0.51 12.85  ?  529  SER A CB   1 
ATOM   5046  C  CB   B SER A 1 306 ? -6.605  -19.000 28.416  0.49 12.35  ?  529  SER A CB   1 
ATOM   5047  O  OG   A SER A 1 306 ? -6.193  -19.613 29.626  0.51 14.32  ?  529  SER A OG   1 
ATOM   5048  O  OG   B SER A 1 306 ? -6.167  -19.917 27.440  0.49 13.55  ?  529  SER A OG   1 
ATOM   5049  H  H    A SER A 1 306 ? -7.157  -16.851 29.520  0.51 13.82  ?  529  SER A H    1 
ATOM   5050  H  H    B SER A 1 306 ? -7.157  -16.851 29.520  0.49 13.82  ?  529  SER A H    1 
ATOM   5051  H  HA   A SER A 1 306 ? -4.936  -17.778 28.295  0.51 13.88  ?  529  SER A HA   1 
ATOM   5052  H  HA   B SER A 1 306 ? -4.939  -17.784 28.291  0.49 13.70  ?  529  SER A HA   1 
ATOM   5053  H  HB2  A SER A 1 306 ? -7.540  -18.892 28.401  0.51 15.42  ?  529  SER A HB2  1 
ATOM   5054  H  HB2  B SER A 1 306 ? -6.402  -19.353 29.296  0.49 14.82  ?  529  SER A HB2  1 
ATOM   5055  H  HB3  A SER A 1 306 ? -6.316  -19.594 27.671  0.51 15.42  ?  529  SER A HB3  1 
ATOM   5056  H  HB3  B SER A 1 306 ? -7.562  -18.870 28.323  0.49 14.82  ?  529  SER A HB3  1 
ATOM   5057  H  HG   A SER A 1 306 ? -5.357  -19.585 29.709  0.51 17.19  ?  529  SER A HG   1 
ATOM   5058  H  HG   B SER A 1 306 ? -6.379  -19.644 26.674  0.49 16.26  ?  529  SER A HG   1 
ATOM   5059  N  N    . LEU A 1 307 ? -5.206  -16.600 26.162  1.00 10.19  ?  530  LEU A N    1 
ATOM   5060  C  CA   . LEU A 1 307 ? -5.413  -15.987 24.860  1.00 10.12  ?  530  LEU A CA   1 
ATOM   5061  C  C    . LEU A 1 307 ? -5.736  -17.035 23.808  1.00 10.58  ?  530  LEU A C    1 
ATOM   5062  O  O    . LEU A 1 307 ? -5.224  -18.152 23.843  1.00 10.95  ?  530  LEU A O    1 
ATOM   5063  C  CB   . LEU A 1 307 ? -4.141  -15.269 24.408  1.00 10.21  ?  530  LEU A CB   1 
ATOM   5064  C  CG   . LEU A 1 307 ? -3.729  -14.053 25.226  1.00 9.02   ?  530  LEU A CG   1 
ATOM   5065  C  CD1  . LEU A 1 307 ? -2.298  -13.657 24.912  1.00 8.76   ?  530  LEU A CD1  1 
ATOM   5066  C  CD2  . LEU A 1 307 ? -4.681  -12.884 24.960  1.00 10.30  ?  530  LEU A CD2  1 
ATOM   5067  H  H    . LEU A 1 307 ? -4.382  -16.641 26.407  1.00 12.23  ?  530  LEU A H    1 
ATOM   5068  H  HA   . LEU A 1 307 ? -6.147  -15.357 24.932  1.00 12.15  ?  530  LEU A HA   1 
ATOM   5069  H  HB2  . LEU A 1 307 ? -3.407  -15.902 24.447  1.00 12.26  ?  530  LEU A HB2  1 
ATOM   5070  H  HB3  . LEU A 1 307 ? -4.273  -14.968 23.495  1.00 12.26  ?  530  LEU A HB3  1 
ATOM   5071  H  HG   . LEU A 1 307 ? -3.778  -14.276 26.169  1.00 10.83  ?  530  LEU A HG   1 
ATOM   5072  H  HD11 . LEU A 1 307 ? -2.064  -12.876 25.437  1.00 10.52  ?  530  LEU A HD11 1 
ATOM   5073  H  HD12 . LEU A 1 307 ? -1.710  -14.395 25.137  1.00 10.52  ?  530  LEU A HD12 1 
ATOM   5074  H  HD13 . LEU A 1 307 ? -2.227  -13.454 23.966  1.00 10.52  ?  530  LEU A HD13 1 
ATOM   5075  H  HD21 . LEU A 1 307 ? -4.442  -12.144 25.540  1.00 12.36  ?  530  LEU A HD21 1 
ATOM   5076  H  HD22 . LEU A 1 307 ? -4.599  -12.615 24.031  1.00 12.36  ?  530  LEU A HD22 1 
ATOM   5077  H  HD23 . LEU A 1 307 ? -5.590  -13.168 25.143  1.00 12.36  ?  530  LEU A HD23 1 
ATOM   5078  N  N    . ALA A 1 308 ? -6.525  -16.635 22.815  1.00 10.21  ?  531  ALA A N    1 
ATOM   5079  C  CA   . ALA A 1 308 ? -6.666  -17.451 21.621  1.00 10.55  ?  531  ALA A CA   1 
ATOM   5080  C  C    . ALA A 1 308 ? -5.341  -17.547 20.876  1.00 10.55  ?  531  ALA A C    1 
ATOM   5081  O  O    . ALA A 1 308 ? -4.584  -16.562 20.804  1.00 9.47   ?  531  ALA A O    1 
ATOM   5082  C  CB   . ALA A 1 308 ? -7.707  -16.842 20.687  1.00 11.76  ?  531  ALA A CB   1 
ATOM   5083  H  H    . ALA A 1 308 ? -6.981  -15.906 22.810  1.00 12.25  ?  531  ALA A H    1 
ATOM   5084  H  HA   . ALA A 1 308 ? -6.945  -18.342 21.884  1.00 12.66  ?  531  ALA A HA   1 
ATOM   5085  H  HB1  . ALA A 1 308 ? -7.801  -17.409 19.905  1.00 14.11  ?  531  ALA A HB1  1 
ATOM   5086  H  HB2  . ALA A 1 308 ? -8.555  -16.781 21.155  1.00 14.11  ?  531  ALA A HB2  1 
ATOM   5087  H  HB3  . ALA A 1 308 ? -7.413  -15.957 20.420  1.00 14.11  ?  531  ALA A HB3  1 
ATOM   5088  N  N    . PRO A 1 309 ? -5.034  -18.713 20.296  1.00 12.86  ?  532  PRO A N    1 
ATOM   5089  C  CA   A PRO A 1 309 ? -3.782  -18.865 19.549  0.33 12.95  ?  532  PRO A CA   1 
ATOM   5090  C  CA   B PRO A 1 309 ? -3.781  -18.865 19.550  0.67 13.10  ?  532  PRO A CA   1 
ATOM   5091  C  C    . PRO A 1 309 ? -3.703  -17.881 18.397  1.00 11.56  ?  532  PRO A C    1 
ATOM   5092  O  O    . PRO A 1 309 ? -4.617  -17.778 17.575  1.00 13.32  ?  532  PRO A O    1 
ATOM   5093  C  CB   A PRO A 1 309 ? -3.843  -20.309 19.031  0.33 14.53  ?  532  PRO A CB   1 
ATOM   5094  C  CB   B PRO A 1 309 ? -3.845  -20.312 19.035  0.67 15.14  ?  532  PRO A CB   1 
ATOM   5095  C  CG   A PRO A 1 309 ? -4.917  -20.989 19.781  0.33 16.01  ?  532  PRO A CG   1 
ATOM   5096  C  CG   B PRO A 1 309 ? -4.963  -20.951 19.744  0.67 17.04  ?  532  PRO A CG   1 
ATOM   5097  C  CD   A PRO A 1 309 ? -5.594  -20.019 20.690  0.33 14.75  ?  532  PRO A CD   1 
ATOM   5098  C  CD   B PRO A 1 309 ? -5.914  -19.884 20.115  0.67 14.43  ?  532  PRO A CD   1 
ATOM   5099  H  HA   . PRO A 1 309 ? -3.022  -18.751 20.140  1.00 15.72  ?  532  PRO A HA   1 
ATOM   5100  H  HB2  A PRO A 1 309 ? -4.042  -20.303 18.082  0.33 17.44  ?  532  PRO A HB2  1 
ATOM   5101  H  HB2  B PRO A 1 309 ? -4.003  -20.310 18.078  0.67 18.17  ?  532  PRO A HB2  1 
ATOM   5102  H  HB3  A PRO A 1 309 ? -2.990  -20.744 19.188  0.33 17.44  ?  532  PRO A HB3  1 
ATOM   5103  H  HB3  B PRO A 1 309 ? -3.011  -20.765 19.232  0.67 18.17  ?  532  PRO A HB3  1 
ATOM   5104  H  HG2  A PRO A 1 309 ? -5.558  -21.349 19.149  0.33 19.21  ?  532  PRO A HG2  1 
ATOM   5105  H  HG2  B PRO A 1 309 ? -5.390  -21.595 19.157  0.67 20.45  ?  532  PRO A HG2  1 
ATOM   5106  H  HG3  A PRO A 1 309 ? -4.525  -21.708 20.302  0.33 19.21  ?  532  PRO A HG3  1 
ATOM   5107  H  HG3  B PRO A 1 309 ? -4.628  -21.397 20.537  0.67 20.45  ?  532  PRO A HG3  1 
ATOM   5108  H  HD2  A PRO A 1 309 ? -6.554  -20.035 20.555  0.33 17.70  ?  532  PRO A HD2  1 
ATOM   5109  H  HD2  B PRO A 1 309 ? -6.557  -19.728 19.405  0.67 17.31  ?  532  PRO A HD2  1 
ATOM   5110  H  HD3  A PRO A 1 309 ? -5.387  -20.215 21.617  0.33 17.70  ?  532  PRO A HD3  1 
ATOM   5111  H  HD3  B PRO A 1 309 ? -6.377  -20.101 20.939  0.67 17.31  ?  532  PRO A HD3  1 
ATOM   5112  N  N    . MET A 1 310 ? -2.595  -17.167 18.333  1.00 9.40   ?  533  MET A N    1 
ATOM   5113  C  CA   . MET A 1 310 ? -2.337  -16.248 17.246  1.00 10.28  ?  533  MET A CA   1 
ATOM   5114  C  C    . MET A 1 310 ? -1.883  -17.055 16.028  1.00 11.64  ?  533  MET A C    1 
ATOM   5115  O  O    . MET A 1 310 ? -2.243  -16.742 14.883  1.00 12.72  ?  533  MET A O    1 
ATOM   5116  C  CB   . MET A 1 310 ? -1.241  -15.288 17.700  1.00 12.28  ?  533  MET A CB   1 
ATOM   5117  C  CG   . MET A 1 310 ? -0.722  -14.336 16.682  1.00 13.86  ?  533  MET A CG   1 
ATOM   5118  S  SD   . MET A 1 310 ? 0.719   -13.540 17.386  1.00 13.90  ?  533  MET A SD   1 
ATOM   5119  C  CE   . MET A 1 310 ? 1.045   -12.416 16.035  1.00 18.05  ?  533  MET A CE   1 
ATOM   5120  O  OXT  . MET A 1 310 ? -1.130  -18.030 16.171  1.00 14.87  ?  533  MET A OXT  1 
ATOM   5121  H  H    . MET A 1 310 ? -1.966  -17.198 18.918  1.00 11.28  ?  533  MET A H    1 
ATOM   5122  H  HA   . MET A 1 310 ? -3.120  -15.727 17.007  1.00 12.34  ?  533  MET A HA   1 
ATOM   5123  H  HB2  . MET A 1 310 ? -1.591  -14.758 18.432  1.00 14.73  ?  533  MET A HB2  1 
ATOM   5124  H  HB3  . MET A 1 310 ? -0.486  -15.817 18.004  1.00 14.73  ?  533  MET A HB3  1 
ATOM   5125  H  HG2  . MET A 1 310 ? -0.468  -14.810 15.875  1.00 16.64  ?  533  MET A HG2  1 
ATOM   5126  H  HG3  . MET A 1 310 ? -1.392  -13.665 16.475  1.00 16.64  ?  533  MET A HG3  1 
ATOM   5127  H  HE1  . MET A 1 310 ? 1.814   -11.869 16.258  1.00 21.66  ?  533  MET A HE1  1 
ATOM   5128  H  HE2  . MET A 1 310 ? 1.226   -12.931 15.233  1.00 21.66  ?  533  MET A HE2  1 
ATOM   5129  H  HE3  . MET A 1 310 ? 0.267   -11.853 15.898  1.00 21.66  ?  533  MET A HE3  1 
ATOM   5130  N  N    A LYS B 1 2   ? -12.980 13.216  24.015  0.63 90.99  ?  225  LYS B N    1 
ATOM   5131  C  CA   A LYS B 1 2   ? -14.277 13.524  23.419  0.63 19.98  ?  225  LYS B CA   1 
ATOM   5132  C  C    A LYS B 1 2   ? -14.298 14.951  22.853  0.63 15.58  ?  225  LYS B C    1 
ATOM   5133  O  O    A LYS B 1 2   ? -14.418 15.126  21.639  0.63 33.89  ?  225  LYS B O    1 
ATOM   5134  C  CB   A LYS B 1 2   ? -15.404 13.293  24.431  0.63 14.48  ?  225  LYS B CB   1 
ATOM   5135  C  CG   A LYS B 1 2   ? -14.933 12.816  25.798  0.63 27.52  ?  225  LYS B CG   1 
ATOM   5136  C  CD   A LYS B 1 2   ? -16.103 12.486  26.711  0.63 44.21  ?  225  LYS B CD   1 
ATOM   5137  C  CE   A LYS B 1 2   ? -16.566 11.048  26.552  0.63 26.54  ?  225  LYS B CE   1 
ATOM   5138  N  NZ   A LYS B 1 2   ? -17.515 10.671  27.636  0.63 62.16  ?  225  LYS B NZ   1 
ATOM   5139  H  HA   A LYS B 1 2   ? -14.443 12.925  22.675  0.63 23.97  ?  225  LYS B HA   1 
ATOM   5140  H  HB2  A LYS B 1 2   ? -15.880 14.129  24.559  0.63 17.38  ?  225  LYS B HB2  1 
ATOM   5141  H  HB3  A LYS B 1 2   ? -16.006 12.620  24.076  0.63 17.38  ?  225  LYS B HB3  1 
ATOM   5142  H  HG2  A LYS B 1 2   ? -14.397 12.015  25.690  0.63 33.03  ?  225  LYS B HG2  1 
ATOM   5143  H  HG3  A LYS B 1 2   ? -14.407 13.514  26.217  0.63 33.03  ?  225  LYS B HG3  1 
ATOM   5144  H  HD2  A LYS B 1 2   ? -15.834 12.617  27.634  0.63 53.06  ?  225  LYS B HD2  1 
ATOM   5145  H  HD3  A LYS B 1 2   ? -16.849 13.069  26.497  0.63 53.06  ?  225  LYS B HD3  1 
ATOM   5146  H  HE2  A LYS B 1 2   ? -17.017 10.946  25.699  0.63 31.86  ?  225  LYS B HE2  1 
ATOM   5147  H  HE3  A LYS B 1 2   ? -15.799 10.455  26.595  0.63 31.86  ?  225  LYS B HE3  1 
ATOM   5148  H  HZ1  A LYS B 1 2   ? -17.785 9.830   27.525  0.63 74.60  ?  225  LYS B HZ1  1 
ATOM   5149  H  HZ2  A LYS B 1 2   ? -17.117 10.745  28.428  0.63 74.60  ?  225  LYS B HZ2  1 
ATOM   5150  H  HZ3  A LYS B 1 2   ? -18.226 11.206  27.618  0.63 74.60  ?  225  LYS B HZ3  1 
ATOM   5151  N  N    . PRO B 1 3   ? -14.165 15.976  23.721  1.00 23.44  ?  226  PRO B N    1 
ATOM   5152  C  CA   . PRO B 1 3   ? -14.061 17.349  23.214  1.00 111.24 ?  226  PRO B CA   1 
ATOM   5153  C  C    . PRO B 1 3   ? -12.780 17.567  22.440  1.00 109.38 ?  226  PRO B C    1 
ATOM   5154  O  O    . PRO B 1 3   ? -12.054 16.618  22.119  1.00 35.02  ?  226  PRO B O    1 
ATOM   5155  C  CB   . PRO B 1 3   ? -14.051 18.202  24.490  1.00 33.70  ?  226  PRO B CB   1 
ATOM   5156  C  CG   . PRO B 1 3   ? -13.497 17.306  25.520  1.00 22.47  ?  226  PRO B CG   1 
ATOM   5157  C  CD   . PRO B 1 3   ? -14.038 15.942  25.188  1.00 24.56  ?  226  PRO B CD   1 
ATOM   5158  H  HA   . PRO B 1 3   ? -14.836 17.566  22.671  1.00 133.49 ?  226  PRO B HA   1 
ATOM   5159  H  HB2  . PRO B 1 3   ? -13.489 18.982  24.365  1.00 40.44  ?  226  PRO B HB2  1 
ATOM   5160  H  HB3  . PRO B 1 3   ? -14.954 18.476  24.714  1.00 40.44  ?  226  PRO B HB3  1 
ATOM   5161  H  HG2  . PRO B 1 3   ? -12.528 17.314  25.477  1.00 26.97  ?  226  PRO B HG2  1 
ATOM   5162  H  HG3  . PRO B 1 3   ? -13.793 17.591  26.399  1.00 26.97  ?  226  PRO B HG3  1 
ATOM   5163  H  HD2  . PRO B 1 3   ? -13.419 15.249  25.465  1.00 29.48  ?  226  PRO B HD2  1 
ATOM   5164  H  HD3  . PRO B 1 3   ? -14.902 15.802  25.606  1.00 29.48  ?  226  PRO B HD3  1 
ATOM   5165  N  N    . PHE B 1 4   ? -12.474 18.827  22.164  1.00 43.86  ?  227  PHE B N    1 
ATOM   5166  C  CA   . PHE B 1 4   ? -11.254 19.124  21.452  1.00 22.25  ?  227  PHE B CA   1 
ATOM   5167  C  C    . PHE B 1 4   ? -10.075 19.189  22.408  1.00 10.91  ?  227  PHE B C    1 
ATOM   5168  O  O    . PHE B 1 4   ? -10.118 19.866  23.434  1.00 14.26  ?  227  PHE B O    1 
ATOM   5169  C  CB   . PHE B 1 4   ? -11.334 20.426  20.672  1.00 17.64  ?  227  PHE B CB   1 
ATOM   5170  C  CG   . PHE B 1 4   ? -10.282 20.502  19.642  1.00 11.16  ?  227  PHE B CG   1 
ATOM   5171  C  CD1  . PHE B 1 4   ? -10.443 19.830  18.458  1.00 24.63  ?  227  PHE B CD1  1 
ATOM   5172  C  CD2  . PHE B 1 4   ? -9.093  21.158  19.878  1.00 19.36  ?  227  PHE B CD2  1 
ATOM   5173  C  CE1  . PHE B 1 4   ? -9.472  19.845  17.506  1.00 20.06  ?  227  PHE B CE1  1 
ATOM   5174  C  CE2  . PHE B 1 4   ? -8.095  21.169  18.905  1.00 18.70  ?  227  PHE B CE2  1 
ATOM   5175  C  CZ   . PHE B 1 4   ? -8.294  20.483  17.729  1.00 13.77  ?  227  PHE B CZ   1 
ATOM   5176  H  H    . PHE B 1 4   ? -12.951 19.511  22.377  1.00 52.64  ?  227  PHE B H    1 
ATOM   5177  H  HA   . PHE B 1 4   ? -11.115 18.405  20.816  1.00 26.70  ?  227  PHE B HA   1 
ATOM   5178  H  HB2  . PHE B 1 4   ? -12.197 20.484  20.232  1.00 21.17  ?  227  PHE B HB2  1 
ATOM   5179  H  HB3  . PHE B 1 4   ? -11.221 21.173  21.281  1.00 21.17  ?  227  PHE B HB3  1 
ATOM   5180  H  HD1  . PHE B 1 4   ? -11.228 19.357  18.304  1.00 29.55  ?  227  PHE B HD1  1 
ATOM   5181  H  HD2  . PHE B 1 4   ? -8.956  21.594  20.688  1.00 23.23  ?  227  PHE B HD2  1 
ATOM   5182  H  HE1  . PHE B 1 4   ? -9.616  19.415  16.694  1.00 24.08  ?  227  PHE B HE1  1 
ATOM   5183  H  HE2  . PHE B 1 4   ? -7.303  21.635  19.049  1.00 22.45  ?  227  PHE B HE2  1 
ATOM   5184  H  HZ   . PHE B 1 4   ? -7.622  20.456  17.086  1.00 16.53  ?  227  PHE B HZ   1 
ATOM   5185  N  N    . THR B 1 5   ? -9.000  18.494  22.039  1.00 10.96  ?  228  THR B N    1 
ATOM   5186  C  CA   . THR B 1 5   ? -7.779  18.520  22.817  1.00 10.13  ?  228  THR B CA   1 
ATOM   5187  C  C    . THR B 1 5   ? -6.560  18.787  21.945  1.00 8.94   ?  228  THR B C    1 
ATOM   5188  O  O    . THR B 1 5   ? -6.496  18.436  20.762  1.00 8.97   ?  228  THR B O    1 
ATOM   5189  C  CB   . THR B 1 5   ? -7.574  17.216  23.588  1.00 10.65  ?  228  THR B CB   1 
ATOM   5190  O  OG1  . THR B 1 5   ? -7.428  16.133  22.658  1.00 10.12  ?  228  THR B OG1  1 
ATOM   5191  C  CG2  . THR B 1 5   ? -8.732  16.953  24.531  1.00 12.09  ?  228  THR B CG2  1 
ATOM   5192  H  H    . THR B 1 5   ? -8.961  18.000  21.336  1.00 13.15  ?  228  THR B H    1 
ATOM   5193  H  HA   . THR B 1 5   ? -7.844  19.254  23.447  1.00 12.16  ?  228  THR B HA   1 
ATOM   5194  H  HB   . THR B 1 5   ? -6.772  17.279  24.131  1.00 12.78  ?  228  THR B HB   1 
ATOM   5195  H  HG1  . THR B 1 5   ? -7.282  15.417  23.072  1.00 12.14  ?  228  THR B HG1  1 
ATOM   5196  H  HG21 . THR B 1 5   ? -8.571  16.140  25.036  1.00 14.51  ?  228  THR B HG21 1 
ATOM   5197  H  HG22 . THR B 1 5   ? -8.830  17.693  25.150  1.00 14.51  ?  228  THR B HG22 1 
ATOM   5198  H  HG23 . THR B 1 5   ? -9.554  16.853  24.027  1.00 14.51  ?  228  THR B HG23 1 
ATOM   5199  N  N    . ILE B 1 6   ? -5.577  19.394  22.591  1.00 7.88   ?  229  ILE B N    1 
ATOM   5200  C  CA   . ILE B 1 6   ? -4.226  19.610  22.089  1.00 7.77   ?  229  ILE B CA   1 
ATOM   5201  C  C    . ILE B 1 6   ? -3.276  18.792  22.951  1.00 7.38   ?  229  ILE B C    1 
ATOM   5202  O  O    . ILE B 1 6   ? -3.492  18.686  24.168  1.00 7.69   ?  229  ILE B O    1 
ATOM   5203  C  CB   . ILE B 1 6   ? -3.915  21.112  22.144  1.00 9.32   ?  229  ILE B CB   1 
ATOM   5204  C  CG1  . ILE B 1 6   ? -4.920  21.857  21.247  1.00 10.63  ?  229  ILE B CG1  1 
ATOM   5205  C  CG2  . ILE B 1 6   ? -2.485  21.433  21.762  1.00 9.59   ?  229  ILE B CG2  1 
ATOM   5206  C  CD1  . ILE B 1 6   ? -4.861  23.337  21.363  1.00 11.48  ?  229  ILE B CD1  1 
ATOM   5207  H  H    . ILE B 1 6   ? -5.672  19.716  23.383  1.00 9.45   ?  229  ILE B H    1 
ATOM   5208  H  HA   . ILE B 1 6   ? -4.126  19.304  21.174  1.00 9.32   ?  229  ILE B HA   1 
ATOM   5209  H  HB   . ILE B 1 6   ? -4.012  21.407  23.063  1.00 11.19  ?  229  ILE B HB   1 
ATOM   5210  H  HG12 . ILE B 1 6   ? -4.739  21.628  20.322  1.00 12.76  ?  229  ILE B HG12 1 
ATOM   5211  H  HG13 . ILE B 1 6   ? -5.817  21.579  21.488  1.00 12.76  ?  229  ILE B HG13 1 
ATOM   5212  H  HG21 . ILE B 1 6   ? -2.354  22.393  21.808  1.00 11.51  ?  229  ILE B HG21 1 
ATOM   5213  H  HG22 . ILE B 1 6   ? -1.886  20.987  22.380  1.00 11.51  ?  229  ILE B HG22 1 
ATOM   5214  H  HG23 . ILE B 1 6   ? -2.322  21.120  20.859  1.00 11.51  ?  229  ILE B HG23 1 
ATOM   5215  H  HD11 . ILE B 1 6   ? -5.619  23.720  20.895  1.00 13.77  ?  229  ILE B HD11 1 
ATOM   5216  H  HD12 . ILE B 1 6   ? -4.893  23.582  22.301  1.00 13.77  ?  229  ILE B HD12 1 
ATOM   5217  H  HD13 . ILE B 1 6   ? -4.034  23.652  20.966  1.00 13.77  ?  229  ILE B HD13 1 
ATOM   5218  N  N    . PRO B 1 7   ? -2.205  18.220  22.397  1.00 6.77   ?  230  PRO B N    1 
ATOM   5219  C  CA   . PRO B 1 7   ? -1.251  17.495  23.248  1.00 6.39   ?  230  PRO B CA   1 
ATOM   5220  C  C    . PRO B 1 7   ? -0.737  18.361  24.388  1.00 6.32   ?  230  PRO B C    1 
ATOM   5221  O  O    . PRO B 1 7   ? -0.616  19.577  24.264  1.00 7.28   ?  230  PRO B O    1 
ATOM   5222  C  CB   . PRO B 1 7   ? -0.123  17.142  22.279  1.00 7.36   ?  230  PRO B CB   1 
ATOM   5223  C  CG   . PRO B 1 7   ? -0.825  17.022  20.950  1.00 7.27   ?  230  PRO B CG   1 
ATOM   5224  C  CD   . PRO B 1 7   ? -1.822  18.147  20.971  1.00 7.43   ?  230  PRO B CD   1 
ATOM   5225  H  HA   . PRO B 1 7   ? -1.659  16.691  23.607  1.00 7.67   ?  230  PRO B HA   1 
ATOM   5226  H  HB2  . PRO B 1 7   ? 0.541   17.849  22.265  1.00 8.84   ?  230  PRO B HB2  1 
ATOM   5227  H  HB3  . PRO B 1 7   ? 0.291   16.303  22.536  1.00 8.84   ?  230  PRO B HB3  1 
ATOM   5228  H  HG2  . PRO B 1 7   ? -0.190  17.128  20.225  1.00 8.73   ?  230  PRO B HG2  1 
ATOM   5229  H  HG3  . PRO B 1 7   ? -1.268  16.161  20.881  1.00 8.73   ?  230  PRO B HG3  1 
ATOM   5230  H  HD2  . PRO B 1 7   ? -1.414  18.977  20.678  1.00 8.91   ?  230  PRO B HD2  1 
ATOM   5231  H  HD3  . PRO B 1 7   ? -2.590  17.941  20.415  1.00 8.91   ?  230  PRO B HD3  1 
ATOM   5232  N  N    . ILE B 1 8   ? -0.420  17.717  25.506  1.00 6.45   ?  231  ILE B N    1 
ATOM   5233  C  CA   . ILE B 1 8   ? 0.156   18.414  26.651  1.00 7.12   ?  231  ILE B CA   1 
ATOM   5234  C  C    . ILE B 1 8   ? 1.680   18.372  26.645  1.00 8.39   ?  231  ILE B C    1 
ATOM   5235  O  O    . ILE B 1 8   ? 2.335   18.852  27.570  1.00 9.55   ?  231  ILE B O    1 
ATOM   5236  C  CB   . ILE B 1 8   ? -0.443  17.915  27.983  1.00 8.10   ?  231  ILE B CB   1 
ATOM   5237  C  CG1  . ILE B 1 8   ? -0.117  16.446  28.242  1.00 9.76   ?  231  ILE B CG1  1 
ATOM   5238  C  CG2  . ILE B 1 8   ? -1.951  18.195  27.999  1.00 8.95   ?  231  ILE B CG2  1 
ATOM   5239  C  CD1  . ILE B 1 8   ? -0.573  15.991  29.631  1.00 10.93  ?  231  ILE B CD1  1 
ATOM   5240  H  H    . ILE B 1 8   ? -0.530  16.873  25.627  1.00 7.74   ?  231  ILE B H    1 
ATOM   5241  H  HA   . ILE B 1 8   ? -0.072  19.352  26.556  1.00 8.55   ?  231  ILE B HA   1 
ATOM   5242  H  HB   . ILE B 1 8   ? -0.032  18.405  28.712  1.00 9.72   ?  231  ILE B HB   1 
ATOM   5243  H  HG12 . ILE B 1 8   ? -0.568  15.898  27.581  1.00 11.71  ?  231  ILE B HG12 1 
ATOM   5244  H  HG13 . ILE B 1 8   ? 0.843   16.317  28.181  1.00 11.71  ?  231  ILE B HG13 1 
ATOM   5245  H  HG21 . ILE B 1 8   ? -2.294  18.025  28.890  1.00 10.75  ?  231  ILE B HG21 1 
ATOM   5246  H  HG22 . ILE B 1 8   ? -2.102  19.123  27.758  1.00 10.75  ?  231  ILE B HG22 1 
ATOM   5247  H  HG23 . ILE B 1 8   ? -2.387  17.612  27.359  1.00 10.75  ?  231  ILE B HG23 1 
ATOM   5248  H  HD11 . ILE B 1 8   ? -0.239  15.095  29.795  1.00 13.11  ?  231  ILE B HD11 1 
ATOM   5249  H  HD12 . ILE B 1 8   ? -0.219  16.602  30.295  1.00 13.11  ?  231  ILE B HD12 1 
ATOM   5250  H  HD13 . ILE B 1 8   ? -1.542  15.994  29.661  1.00 13.11  ?  231  ILE B HD13 1 
ATOM   5251  N  N    . LEU B 1 9   ? 2.272   17.853  25.579  1.00 7.33   ?  232  LEU B N    1 
ATOM   5252  C  CA   . LEU B 1 9   ? 3.724   17.801  25.480  1.00 7.01   ?  232  LEU B CA   1 
ATOM   5253  C  C    . LEU B 1 9   ? 4.327   19.199  25.445  1.00 6.76   ?  232  LEU B C    1 
ATOM   5254  O  O    . LEU B 1 9   ? 3.799   20.115  24.807  1.00 7.34   ?  232  LEU B O    1 
ATOM   5255  C  CB   . LEU B 1 9   ? 4.086   17.062  24.197  1.00 7.36   ?  232  LEU B CB   1 
ATOM   5256  C  CG   . LEU B 1 9   ? 3.592   15.613  24.085  1.00 8.50   ?  232  LEU B CG   1 
ATOM   5257  C  CD1  . LEU B 1 9   ? 3.835   15.084  22.669  1.00 9.91   ?  232  LEU B CD1  1 
ATOM   5258  C  CD2  . LEU B 1 9   ? 4.245   14.689  25.106  1.00 9.65   ?  232  LEU B CD2  1 
ATOM   5259  H  H    . LEU B 1 9   ? 1.858   17.525  24.900  1.00 8.80   ?  232  LEU B H    1 
ATOM   5260  H  HA   . LEU B 1 9   ? 4.091   17.342  26.251  1.00 8.41   ?  232  LEU B HA   1 
ATOM   5261  H  HB2  . LEU B 1 9   ? 3.709   17.551  23.450  1.00 8.83   ?  232  LEU B HB2  1 
ATOM   5262  H  HB3  . LEU B 1 9   ? 5.054   17.040  24.125  1.00 8.83   ?  232  LEU B HB3  1 
ATOM   5263  H  HG   . LEU B 1 9   ? 2.641   15.612  24.275  1.00 10.21  ?  232  LEU B HG   1 
ATOM   5264  H  HD11 . LEU B 1 9   ? 3.496   14.178  22.607  1.00 11.90  ?  232  LEU B HD11 1 
ATOM   5265  H  HD12 . LEU B 1 9   ? 3.373   15.654  22.035  1.00 11.90  ?  232  LEU B HD12 1 
ATOM   5266  H  HD13 . LEU B 1 9   ? 4.788   15.093  22.487  1.00 11.90  ?  232  LEU B HD13 1 
ATOM   5267  H  HD21 . LEU B 1 9   ? 3.906   13.789  24.980  1.00 11.58  ?  232  LEU B HD21 1 
ATOM   5268  H  HD22 . LEU B 1 9   ? 5.206   14.702  24.975  1.00 11.58  ?  232  LEU B HD22 1 
ATOM   5269  H  HD23 . LEU B 1 9   ? 4.029   15.001  25.999  1.00 11.58  ?  232  LEU B HD23 1 
ATOM   5270  N  N    . THR B 1 10  ? 5.470   19.346  26.106  1.00 7.75   ?  233  THR B N    1 
ATOM   5271  C  CA   . THR B 1 10  ? 6.217   20.589  26.060  1.00 9.04   ?  233  THR B CA   1 
ATOM   5272  C  C    . THR B 1 10  ? 6.972   20.704  24.735  1.00 9.64   ?  233  THR B C    1 
ATOM   5273  O  O    . THR B 1 10  ? 7.106   19.735  23.986  1.00 8.57   ?  233  THR B O    1 
ATOM   5274  C  CB   . THR B 1 10  ? 7.244   20.622  27.188  1.00 10.05  ?  233  THR B CB   1 
ATOM   5275  O  OG1  . THR B 1 10  ? 8.200   19.593  26.937  1.00 11.33  ?  233  THR B OG1  1 
ATOM   5276  C  CG2  . THR B 1 10  ? 6.583   20.413  28.541  1.00 11.04  ?  233  THR B CG2  1 
ATOM   5277  H  H    . THR B 1 10  ? 5.834   18.736  26.590  1.00 9.30   ?  233  THR B H    1 
ATOM   5278  H  HA   . THR B 1 10  ? 5.597   21.329  26.152  1.00 10.84  ?  233  THR B HA   1 
ATOM   5279  H  HB   . THR B 1 10  ? 7.683   21.487  27.224  1.00 12.06  ?  233  THR B HB   1 
ATOM   5280  H  HG1  . THR B 1 10  ? 8.786   19.592  27.539  1.00 13.60  ?  233  THR B HG1  1 
ATOM   5281  H  HG21 . THR B 1 10  ? 7.237   20.520  29.250  1.00 13.25  ?  233  THR B HG21 1 
ATOM   5282  H  HG22 . THR B 1 10  ? 5.873   21.062  28.667  1.00 13.25  ?  233  THR B HG22 1 
ATOM   5283  H  HG23 . THR B 1 10  ? 6.207   19.521  28.592  1.00 13.25  ?  233  THR B HG23 1 
ATOM   5284  N  N    . ILE B 1 11  ? 7.509   21.908  24.489  1.00 10.87  ?  234  ILE B N    1 
ATOM   5285  C  CA   . ILE B 1 11  ? 8.384   22.145  23.345  1.00 14.49  ?  234  ILE B CA   1 
ATOM   5286  C  C    . ILE B 1 11  ? 9.509   21.128  23.320  1.00 13.85  ?  234  ILE B C    1 
ATOM   5287  O  O    . ILE B 1 11  ? 9.840   20.577  22.260  1.00 14.36  ?  234  ILE B O    1 
ATOM   5288  C  CB   . ILE B 1 11  ? 8.946   23.584  23.418  1.00 19.51  ?  234  ILE B CB   1 
ATOM   5289  C  CG1  . ILE B 1 11  ? 7.841   24.605  23.144  1.00 22.41  ?  234  ILE B CG1  1 
ATOM   5290  C  CG2  . ILE B 1 11  ? 10.145  23.758  22.508  1.00 21.29  ?  234  ILE B CG2  1 
ATOM   5291  C  CD1  . ILE B 1 11  ? 7.029   24.319  21.913  1.00 23.27  ?  234  ILE B CD1  1 
ATOM   5292  H  H    . ILE B 1 11  ? 7.378   22.606  24.974  1.00 13.05  ?  234  ILE B H    1 
ATOM   5293  H  HA   . ILE B 1 11  ? 7.869   22.046  22.529  1.00 17.39  ?  234  ILE B HA   1 
ATOM   5294  H  HB   . ILE B 1 11  ? 9.265   23.743  24.320  1.00 23.42  ?  234  ILE B HB   1 
ATOM   5295  H  HG12 . ILE B 1 11  ? 7.234   24.616  23.901  1.00 26.89  ?  234  ILE B HG12 1 
ATOM   5296  H  HG13 . ILE B 1 11  ? 8.247   25.479  23.032  1.00 26.89  ?  234  ILE B HG13 1 
ATOM   5297  H  HG21 . ILE B 1 11  ? 10.278  24.704  22.339  1.00 25.55  ?  234  ILE B HG21 1 
ATOM   5298  H  HG22 . ILE B 1 11  ? 10.928  23.387  22.944  1.00 25.55  ?  234  ILE B HG22 1 
ATOM   5299  H  HG23 . ILE B 1 11  ? 9.979   23.292  21.674  1.00 25.55  ?  234  ILE B HG23 1 
ATOM   5300  H  HD11 . ILE B 1 11  ? 6.584   25.134  21.631  1.00 27.93  ?  234  ILE B HD11 1 
ATOM   5301  H  HD12 . ILE B 1 11  ? 7.620   24.005  21.211  1.00 27.93  ?  234  ILE B HD12 1 
ATOM   5302  H  HD13 . ILE B 1 11  ? 6.370   23.638  22.121  1.00 27.93  ?  234  ILE B HD13 1 
ATOM   5303  N  N    . GLY B 1 12  ? 10.095  20.852  24.495  1.00 14.74  ?  235  GLY B N    1 
ATOM   5304  C  CA   . GLY B 1 12  ? 11.168  19.886  24.657  1.00 15.29  ?  235  GLY B CA   1 
ATOM   5305  C  C    . GLY B 1 12  ? 10.734  18.434  24.599  1.00 14.53  ?  235  GLY B C    1 
ATOM   5306  O  O    . GLY B 1 12  ? 11.536  17.526  24.844  1.00 17.70  ?  235  GLY B O    1 
ATOM   5307  H  H    . GLY B 1 12  ? 9.875   21.230  25.236  1.00 17.69  ?  235  GLY B H    1 
ATOM   5308  H  HA2  . GLY B 1 12  ? 11.821  20.027  23.954  1.00 18.35  ?  235  GLY B HA2  1 
ATOM   5309  H  HA3  . GLY B 1 12  ? 11.592  20.034  25.516  1.00 18.35  ?  235  GLY B HA3  1 
ATOM   5310  N  N    . GLU B 1 13  ? 9.465   18.201  24.276  1.00 11.35  ?  236  GLU B N    1 
ATOM   5311  C  CA   . GLU B 1 13  ? 8.949   16.859  24.068  1.00 9.40   ?  236  GLU B CA   1 
ATOM   5312  C  C    . GLU B 1 13  ? 8.379   16.705  22.663  1.00 8.29   ?  236  GLU B C    1 
ATOM   5313  O  O    . GLU B 1 13  ? 7.721   15.701  22.388  1.00 9.39   ?  236  GLU B O    1 
ATOM   5314  C  CB   . GLU B 1 13  ? 7.907   16.534  25.144  1.00 9.25   ?  236  GLU B CB   1 
ATOM   5315  C  CG   . GLU B 1 13  ? 8.518   16.460  26.543  1.00 9.76   ?  236  GLU B CG   1 
ATOM   5316  C  CD   . GLU B 1 13  ? 7.496   16.417  27.659  1.00 10.35  ?  236  GLU B CD   1 
ATOM   5317  O  OE1  . GLU B 1 13  ? 6.321   16.797  27.442  1.00 10.26  ?  236  GLU B OE1  1 
ATOM   5318  O  OE2  . GLU B 1 13  ? 7.887   16.022  28.779  1.00 11.78  -1 236  GLU B OE2  1 
ATOM   5319  H  H    . GLU B 1 13  ? 8.876   18.819  24.170  1.00 13.62  ?  236  GLU B H    1 
ATOM   5320  H  HA   . GLU B 1 13  ? 9.656   16.202  24.163  1.00 11.28  ?  236  GLU B HA   1 
ATOM   5321  H  HB2  . GLU B 1 13  ? 7.229   17.227  25.148  1.00 11.10  ?  236  GLU B HB2  1 
ATOM   5322  H  HB3  . GLU B 1 13  ? 7.503   15.675  24.946  1.00 11.10  ?  236  GLU B HB3  1 
ATOM   5323  H  HG2  . GLU B 1 13  ? 9.057   15.656  26.606  1.00 11.71  ?  236  GLU B HG2  1 
ATOM   5324  H  HG3  . GLU B 1 13  ? 9.073   17.244  26.682  1.00 11.71  ?  236  GLU B HG3  1 
ATOM   5325  N  N    . MET B 1 14  ? 8.636   17.658  21.764  1.00 7.47   ?  237  MET B N    1 
ATOM   5326  C  CA   . MET B 1 14  ? 8.035   17.649  20.443  1.00 6.57   ?  237  MET B CA   1 
ATOM   5327  C  C    . MET B 1 14  ? 9.055   17.928  19.344  1.00 7.09   ?  237  MET B C    1 
ATOM   5328  O  O    . MET B 1 14  ? 10.172  18.394  19.591  1.00 8.36   ?  237  MET B O    1 
ATOM   5329  C  CB   . MET B 1 14  ? 6.885   18.659  20.366  1.00 6.80   ?  237  MET B CB   1 
ATOM   5330  C  CG   . MET B 1 14  ? 5.714   18.277  21.246  1.00 6.89   ?  237  MET B CG   1 
ATOM   5331  S  SD   . MET B 1 14  ? 4.219   19.254  20.953  1.00 7.32   ?  237  MET B SD   1 
ATOM   5332  C  CE   . MET B 1 14  ? 4.695   20.853  21.581  1.00 7.82   ?  237  MET B CE   1 
ATOM   5333  H  H    . MET B 1 14  ? 9.161   18.324  21.904  1.00 8.96   ?  237  MET B H    1 
ATOM   5334  H  HA   . MET B 1 14  ? 7.692   16.757  20.278  1.00 7.89   ?  237  MET B HA   1 
ATOM   5335  H  HB2  . MET B 1 14  ? 7.207   19.527  20.654  1.00 8.17   ?  237  MET B HB2  1 
ATOM   5336  H  HB3  . MET B 1 14  ? 6.569   18.709  19.450  1.00 8.17   ?  237  MET B HB3  1 
ATOM   5337  H  HG2  . MET B 1 14  ? 5.494   17.347  21.084  1.00 8.27   ?  237  MET B HG2  1 
ATOM   5338  H  HG3  . MET B 1 14  ? 5.969   18.402  22.174  1.00 8.27   ?  237  MET B HG3  1 
ATOM   5339  H  HE1  . MET B 1 14  ? 3.947   21.464  21.490  1.00 9.38   ?  237  MET B HE1  1 
ATOM   5340  H  HE2  . MET B 1 14  ? 4.940   20.766  22.515  1.00 9.38   ?  237  MET B HE2  1 
ATOM   5341  H  HE3  . MET B 1 14  ? 5.452   21.180  21.070  1.00 9.38   ?  237  MET B HE3  1 
ATOM   5342  N  N    . THR B 1 15  ? 8.644   17.593  18.117  1.00 7.16   ?  238  THR B N    1 
ATOM   5343  C  CA   A THR B 1 15  ? 9.517   17.717  16.968  0.60 6.69   ?  238  THR B CA   1 
ATOM   5344  C  CA   B THR B 1 15  ? 9.460   17.621  16.917  0.40 6.98   ?  238  THR B CA   1 
ATOM   5345  C  C    . THR B 1 15  ? 8.927   18.647  15.921  1.00 6.21   ?  238  THR B C    1 
ATOM   5346  O  O    . THR B 1 15  ? 7.708   18.803  15.775  1.00 6.57   ?  238  THR B O    1 
ATOM   5347  C  CB   A THR B 1 15  ? 9.854   16.368  16.322  0.60 7.80   ?  238  THR B CB   1 
ATOM   5348  C  CB   B THR B 1 15  ? 9.381   16.257  16.206  0.40 8.76   ?  238  THR B CB   1 
ATOM   5349  O  OG1  A THR B 1 15  ? 8.639   15.695  15.989  0.60 7.23   ?  238  THR B OG1  1 
ATOM   5350  O  OG1  B THR B 1 15  ? 9.591   15.182  17.133  0.40 9.50   ?  238  THR B OG1  1 
ATOM   5351  C  CG2  A THR B 1 15  ? 10.704  15.539  17.256  0.60 8.45   ?  238  THR B CG2  1 
ATOM   5352  C  CG2  B THR B 1 15  ? 10.407  16.205  15.114  0.40 9.03   ?  238  THR B CG2  1 
ATOM   5353  H  H    A THR B 1 15  ? 7.860   17.292  17.934  0.60 8.59   ?  238  THR B H    1 
ATOM   5354  H  H    B THR B 1 15  ? 7.842   17.330  17.952  0.40 8.59   ?  238  THR B H    1 
ATOM   5355  H  HA   A THR B 1 15  ? 10.347  18.109  17.280  0.60 8.03   ?  238  THR B HA   1 
ATOM   5356  H  HA   B THR B 1 15  ? 10.369  17.851  17.165  0.40 8.38   ?  238  THR B HA   1 
ATOM   5357  H  HB   A THR B 1 15  ? 10.367  16.495  15.509  0.60 9.37   ?  238  THR B HB   1 
ATOM   5358  H  HB   B THR B 1 15  ? 8.499   16.142  15.819  0.40 10.51  ?  238  THR B HB   1 
ATOM   5359  H  HG1  A THR B 1 15  ? 8.188   15.556  16.683  0.60 8.67   ?  238  THR B HG1  1 
ATOM   5360  H  HG1  B THR B 1 15  ? 8.989   15.187  17.720  0.40 11.40  ?  238  THR B HG1  1 
ATOM   5361  H  HG21 A THR B 1 15  ? 11.527  16.009  17.462  0.60 10.14  ?  238  THR B HG21 1 
ATOM   5362  H  HG21 B THR B 1 15  ? 10.856  17.062  15.039  0.40 10.84  ?  238  THR B HG21 1 
ATOM   5363  H  HG22 A THR B 1 15  ? 10.223  15.371  18.082  0.60 10.14  ?  238  THR B HG22 1 
ATOM   5364  H  HG22 B THR B 1 15  ? 11.065  15.520  15.309  0.40 10.84  ?  238  THR B HG22 1 
ATOM   5365  H  HG23 A THR B 1 15  ? 10.923  14.690  16.841  0.60 10.14  ?  238  THR B HG23 1 
ATOM   5366  H  HG23 B THR B 1 15  ? 9.979   15.999  14.267  0.40 10.84  ?  238  THR B HG23 1 
ATOM   5367  N  N    . ASN B 1 16  ? 9.830   19.278  15.192  1.00 5.40   ?  239  ASN B N    1 
ATOM   5368  C  CA   . ASN B 1 16  ? 9.442   20.142  14.089  1.00 5.46   ?  239  ASN B CA   1 
ATOM   5369  C  C    . ASN B 1 16  ? 8.791   19.296  12.997  1.00 5.53   ?  239  ASN B C    1 
ATOM   5370  O  O    . ASN B 1 16  ? 9.263   18.203  12.673  1.00 7.23   ?  239  ASN B O    1 
ATOM   5371  C  CB   . ASN B 1 16  ? 10.706  20.825  13.560  1.00 5.38   ?  239  ASN B CB   1 
ATOM   5372  C  CG   . ASN B 1 16  ? 10.409  22.070  12.759  1.00 4.95   ?  239  ASN B CG   1 
ATOM   5373  O  OD1  . ASN B 1 16  ? 9.838   22.013  11.681  1.00 5.79   ?  239  ASN B OD1  1 
ATOM   5374  N  ND2  . ASN B 1 16  ? 10.815  23.210  13.294  1.00 5.68   ?  239  ASN B ND2  1 
ATOM   5375  H  H    . ASN B 1 16  ? 10.680  19.225  15.314  1.00 6.49   ?  239  ASN B H    1 
ATOM   5376  H  HA   . ASN B 1 16  ? 8.807   20.821  14.364  1.00 6.55   ?  239  ASN B HA   1 
ATOM   5377  H  HB2  . ASN B 1 16  ? 11.266  21.078  14.311  1.00 6.45   ?  239  ASN B HB2  1 
ATOM   5378  H  HB3  . ASN B 1 16  ? 11.182  20.205  12.985  1.00 6.45   ?  239  ASN B HB3  1 
ATOM   5379  H  HD21 . ASN B 1 16  ? 10.674  23.952  12.883  1.00 6.82   ?  239  ASN B HD21 1 
ATOM   5380  H  HD22 . ASN B 1 16  ? 11.220  23.210  14.052  1.00 6.82   ?  239  ASN B HD22 1 
ATOM   5381  N  N    . SER B 1 17  ? 7.686   19.791  12.438  1.00 4.98   ?  240  SER B N    1 
ATOM   5382  C  CA   . SER B 1 17  ? 6.982   19.062  11.393  1.00 4.99   ?  240  SER B CA   1 
ATOM   5383  C  C    . SER B 1 17  ? 7.545   19.325  9.999   1.00 4.70   ?  240  SER B C    1 
ATOM   5384  O  O    . SER B 1 17  ? 7.076   18.721  9.031   1.00 5.55   ?  240  SER B O    1 
ATOM   5385  C  CB   . SER B 1 17  ? 5.486   19.366  11.465  1.00 5.38   ?  240  SER B CB   1 
ATOM   5386  O  OG   . SER B 1 17  ? 5.300   20.754  11.292  1.00 5.68   ?  240  SER B OG   1 
ATOM   5387  H  H    . SER B 1 17  ? 7.330   20.544  12.649  1.00 5.98   ?  240  SER B H    1 
ATOM   5388  H  HA   . SER B 1 17  ? 7.076   18.108  11.544  1.00 5.99   ?  240  SER B HA   1 
ATOM   5389  H  HB2  . SER B 1 17  ? 5.023   18.886  10.761  1.00 6.46   ?  240  SER B HB2  1 
ATOM   5390  H  HB3  . SER B 1 17  ? 5.142   19.097  12.332  1.00 6.46   ?  240  SER B HB3  1 
ATOM   5391  H  HG   . SER B 1 17  ? 4.492   20.951  11.404  1.00 6.82   ?  240  SER B HG   1 
ATOM   5392  N  N    . ARG B 1 18  ? 8.565   20.175  9.874   1.00 4.99   ?  241  ARG B N    1 
ATOM   5393  C  CA   . ARG B 1 18  ? 9.210   20.430  8.593   1.00 4.63   ?  241  ARG B CA   1 
ATOM   5394  C  C    . ARG B 1 18  ? 10.642  19.908  8.529   1.00 5.50   ?  241  ARG B C    1 
ATOM   5395  O  O    . ARG B 1 18  ? 11.252  19.954  7.458   1.00 5.79   ?  241  ARG B O    1 
ATOM   5396  C  CB   . ARG B 1 18  ? 9.170   21.923  8.262   1.00 4.85   ?  241  ARG B CB   1 
ATOM   5397  C  CG   . ARG B 1 18  ? 7.751   22.414  8.058   1.00 4.83   ?  241  ARG B CG   1 
ATOM   5398  C  CD   . ARG B 1 18  ? 7.686   23.881  7.713   1.00 5.11   ?  241  ARG B CD   1 
ATOM   5399  N  NE   . ARG B 1 18  ? 8.334   24.125  6.427   1.00 5.67   ?  241  ARG B NE   1 
ATOM   5400  C  CZ   . ARG B 1 18  ? 9.033   25.203  6.115   1.00 5.44   ?  241  ARG B CZ   1 
ATOM   5401  N  NH1  . ARG B 1 18  ? 9.127   26.238  6.942   1.00 6.10   ?  241  ARG B NH1  1 
ATOM   5402  N  NH2  . ARG B 1 18  ? 9.666   25.245  4.942   1.00 5.93   ?  241  ARG B NH2  1 
ATOM   5403  H  H    . ARG B 1 18  ? 8.903   20.620  10.528  1.00 6.00   ?  241  ARG B H    1 
ATOM   5404  H  HA   . ARG B 1 18  ? 8.713   19.978  7.893   1.00 5.56   ?  241  ARG B HA   1 
ATOM   5405  H  HB2  . ARG B 1 18  ? 9.564   22.423  8.994   1.00 5.83   ?  241  ARG B HB2  1 
ATOM   5406  H  HB3  . ARG B 1 18  ? 9.668   22.083  7.445   1.00 5.83   ?  241  ARG B HB3  1 
ATOM   5407  H  HG2  . ARG B 1 18  ? 7.345   21.917  7.331   1.00 5.80   ?  241  ARG B HG2  1 
ATOM   5408  H  HG3  . ARG B 1 18  ? 7.247   22.276  8.876   1.00 5.80   ?  241  ARG B HG3  1 
ATOM   5409  H  HD2  . ARG B 1 18  ? 6.760   24.161  7.653   1.00 6.13   ?  241  ARG B HD2  1 
ATOM   5410  H  HD3  . ARG B 1 18  ? 8.145   24.397  8.395   1.00 6.13   ?  241  ARG B HD3  1 
ATOM   5411  H  HE   . ARG B 1 18  ? 8.254   23.518  5.823   1.00 6.80   ?  241  ARG B HE   1 
ATOM   5412  H  HH11 . ARG B 1 18  ? 8.727   26.218  7.703   1.00 7.32   ?  241  ARG B HH11 1 
ATOM   5413  H  HH12 . ARG B 1 18  ? 9.588   26.928  6.717   1.00 7.32   ?  241  ARG B HH12 1 
ATOM   5414  H  HH21 . ARG B 1 18  ? 9.616   24.577  4.403   1.00 7.12   ?  241  ARG B HH21 1 
ATOM   5415  H  HH22 . ARG B 1 18  ? 10.125  25.939  4.725   1.00 7.12   ?  241  ARG B HH22 1 
ATOM   5416  N  N    . PHE B 1 19  ? 11.193  19.386  9.632   1.00 5.42   ?  242  PHE B N    1 
ATOM   5417  C  CA   . PHE B 1 19  ? 12.532  18.823  9.627   1.00 5.89   ?  242  PHE B CA   1 
ATOM   5418  C  C    . PHE B 1 19  ? 12.652  17.986  10.884  1.00 5.52   ?  242  PHE B C    1 
ATOM   5419  O  O    . PHE B 1 19  ? 12.157  18.417  11.939  1.00 6.47   ?  242  PHE B O    1 
ATOM   5420  C  CB   . PHE B 1 19  ? 13.602  19.920  9.582   1.00 6.15   ?  242  PHE B CB   1 
ATOM   5421  C  CG   . PHE B 1 19  ? 14.931  19.427  9.108   1.00 6.62   ?  242  PHE B CG   1 
ATOM   5422  C  CD1  . PHE B 1 19  ? 15.232  19.392  7.762   1.00 8.16   ?  242  PHE B CD1  1 
ATOM   5423  C  CD2  . PHE B 1 19  ? 15.860  18.917  10.001  1.00 8.58   ?  242  PHE B CD2  1 
ATOM   5424  C  CE1  . PHE B 1 19  ? 16.439  18.895  7.327   1.00 9.30   ?  242  PHE B CE1  1 
ATOM   5425  C  CE2  . PHE B 1 19  ? 17.061  18.417  9.557   1.00 9.15   ?  242  PHE B CE2  1 
ATOM   5426  C  CZ   . PHE B 1 19  ? 17.345  18.401  8.220   1.00 9.99   ?  242  PHE B CZ   1 
ATOM   5427  H  H    . PHE B 1 19  ? 10.803  19.350  10.397  1.00 6.50   ?  242  PHE B H    1 
ATOM   5428  H  HA   . PHE B 1 19  ? 12.672  18.257  8.852   1.00 7.07   ?  242  PHE B HA   1 
ATOM   5429  H  HB2  . PHE B 1 19  ? 13.309  20.619  8.977   1.00 7.38   ?  242  PHE B HB2  1 
ATOM   5430  H  HB3  . PHE B 1 19  ? 13.718  20.281  10.475  1.00 7.38   ?  242  PHE B HB3  1 
ATOM   5431  H  HD1  . PHE B 1 19  ? 14.613  19.706  7.143   1.00 9.79   ?  242  PHE B HD1  1 
ATOM   5432  H  HD2  . PHE B 1 19  ? 15.669  18.914  10.911  1.00 10.30  ?  242  PHE B HD2  1 
ATOM   5433  H  HE1  . PHE B 1 19  ? 16.639  18.896  6.419   1.00 11.17  ?  242  PHE B HE1  1 
ATOM   5434  H  HE2  . PHE B 1 19  ? 17.680  18.088  10.167  1.00 10.99  ?  242  PHE B HE2  1 
ATOM   5435  H  HZ   . PHE B 1 19  ? 18.155  18.055  7.920   1.00 11.99  ?  242  PHE B HZ   1 
ATOM   5436  N  N    . PRO B 1 20  ? 13.268  16.789  10.832  1.00 5.81   ?  243  PRO B N    1 
ATOM   5437  C  CA   . PRO B 1 20  ? 13.200  15.861  11.988  1.00 7.23   ?  243  PRO B CA   1 
ATOM   5438  C  C    . PRO B 1 20  ? 14.169  16.192  13.116  1.00 7.05   ?  243  PRO B C    1 
ATOM   5439  O  O    . PRO B 1 20  ? 15.137  15.461  13.362  1.00 8.50   ?  243  PRO B O    1 
ATOM   5440  C  CB   . PRO B 1 20  ? 13.487  14.504  11.331  1.00 7.91   ?  243  PRO B CB   1 
ATOM   5441  C  CG   . PRO B 1 20  ? 14.396  14.830  10.183  1.00 7.97   ?  243  PRO B CG   1 
ATOM   5442  C  CD   . PRO B 1 20  ? 13.839  16.124  9.637   1.00 6.69   ?  243  PRO B CD   1 
ATOM   5443  H  HA   . PRO B 1 20  ? 12.300  15.874  12.350  1.00 8.67   ?  243  PRO B HA   1 
ATOM   5444  H  HB2  . PRO B 1 20  ? 13.923  13.913  11.965  1.00 9.49   ?  243  PRO B HB2  1 
ATOM   5445  H  HB3  . PRO B 1 20  ? 12.660  14.104  11.019  1.00 9.49   ?  243  PRO B HB3  1 
ATOM   5446  H  HG2  . PRO B 1 20  ? 15.306  14.946  10.499  1.00 9.56   ?  243  PRO B HG2  1 
ATOM   5447  H  HG3  . PRO B 1 20  ? 14.363  14.125  9.518   1.00 9.56   ?  243  PRO B HG3  1 
ATOM   5448  H  HD2  . PRO B 1 20  ? 14.543  16.665  9.246   1.00 8.03   ?  243  PRO B HD2  1 
ATOM   5449  H  HD3  . PRO B 1 20  ? 13.149  15.951  8.977   1.00 8.03   ?  243  PRO B HD3  1 
ATOM   5450  N  N    . VAL B 1 21  ? 13.871  17.276  13.829  1.00 6.81   ?  244  VAL B N    1 
ATOM   5451  C  CA   . VAL B 1 21  ? 14.655  17.718  14.982  1.00 6.71   ?  244  VAL B CA   1 
ATOM   5452  C  C    . VAL B 1 21  ? 13.701  18.231  16.050  1.00 6.44   ?  244  VAL B C    1 
ATOM   5453  O  O    . VAL B 1 21  ? 12.566  18.613  15.756  1.00 6.21   ?  244  VAL B O    1 
ATOM   5454  C  CB   . VAL B 1 21  ? 15.663  18.824  14.608  1.00 7.44   ?  244  VAL B CB   1 
ATOM   5455  C  CG1  . VAL B 1 21  ? 16.729  18.268  13.691  1.00 8.75   ?  244  VAL B CG1  1 
ATOM   5456  C  CG2  . VAL B 1 21  ? 14.936  19.991  13.960  1.00 8.37   ?  244  VAL B CG2  1 
ATOM   5457  H  H    . VAL B 1 21  ? 13.200  17.787  13.661  1.00 8.17   ?  244  VAL B H    1 
ATOM   5458  H  HA   . VAL B 1 21  ? 15.152  16.966  15.342  1.00 8.05   ?  244  VAL B HA   1 
ATOM   5459  H  HB   . VAL B 1 21  ? 16.101  19.152  15.409  1.00 8.93   ?  244  VAL B HB   1 
ATOM   5460  H  HG11 . VAL B 1 21  ? 17.364  18.971  13.482  1.00 10.50  ?  244  VAL B HG11 1 
ATOM   5461  H  HG12 . VAL B 1 21  ? 17.180  17.536  14.139  1.00 10.50  ?  244  VAL B HG12 1 
ATOM   5462  H  HG13 . VAL B 1 21  ? 16.309  17.949  12.876  1.00 10.50  ?  244  VAL B HG13 1 
ATOM   5463  H  HG21 . VAL B 1 21  ? 15.589  20.646  13.667  1.00 10.05  ?  244  VAL B HG21 1 
ATOM   5464  H  HG22 . VAL B 1 21  ? 14.431  19.665  13.199  1.00 10.05  ?  244  VAL B HG22 1 
ATOM   5465  H  HG23 . VAL B 1 21  ? 14.336  20.389  14.609  1.00 10.05  ?  244  VAL B HG23 1 
ATOM   5466  N  N    . PRO B 1 22  ? 14.171  18.302  17.297  1.00 6.63   ?  245  PRO B N    1 
ATOM   5467  C  CA   . PRO B 1 22  ? 13.341  18.903  18.347  1.00 6.45   ?  245  PRO B CA   1 
ATOM   5468  C  C    . PRO B 1 22  ? 13.017  20.355  18.033  1.00 6.45   ?  245  PRO B C    1 
ATOM   5469  O  O    . PRO B 1 22  ? 13.755  21.052  17.334  1.00 7.00   ?  245  PRO B O    1 
ATOM   5470  C  CB   . PRO B 1 22  ? 14.232  18.802  19.593  1.00 8.39   ?  245  PRO B CB   1 
ATOM   5471  C  CG   . PRO B 1 22  ? 15.165  17.687  19.291  1.00 9.18   ?  245  PRO B CG   1 
ATOM   5472  C  CD   . PRO B 1 22  ? 15.447  17.810  17.829  1.00 8.29   ?  245  PRO B CD   1 
ATOM   5473  H  HA   . PRO B 1 22  ? 12.522  18.399  18.473  1.00 7.74   ?  245  PRO B HA   1 
ATOM   5474  H  HB2  . PRO B 1 22  ? 14.713  19.633  19.726  1.00 10.06  ?  245  PRO B HB2  1 
ATOM   5475  H  HB3  . PRO B 1 22  ? 13.691  18.603  20.373  1.00 10.06  ?  245  PRO B HB3  1 
ATOM   5476  H  HG2  . PRO B 1 22  ? 15.978  17.786  19.811  1.00 11.02  ?  245  PRO B HG2  1 
ATOM   5477  H  HG3  . PRO B 1 22  ? 14.743  16.837  19.493  1.00 11.02  ?  245  PRO B HG3  1 
ATOM   5478  H  HD2  . PRO B 1 22  ? 16.160  18.447  17.665  1.00 9.94   ?  245  PRO B HD2  1 
ATOM   5479  H  HD3  . PRO B 1 22  ? 15.676  16.949  17.446  1.00 9.94   ?  245  PRO B HD3  1 
ATOM   5480  N  N    . ILE B 1 23  ? 11.888  20.817  18.565  1.00 7.24   ?  246  ILE B N    1 
ATOM   5481  C  CA   . ILE B 1 23  ? 11.569  22.244  18.522  1.00 6.90   ?  246  ILE B CA   1 
ATOM   5482  C  C    . ILE B 1 23  ? 12.448  22.987  19.520  1.00 7.39   ?  246  ILE B C    1 
ATOM   5483  O  O    . ILE B 1 23  ? 12.588  22.559  20.663  1.00 9.11   ?  246  ILE B O    1 
ATOM   5484  C  CB   . ILE B 1 23  ? 10.085  22.460  18.838  1.00 7.61   ?  246  ILE B CB   1 
ATOM   5485  C  CG1  . ILE B 1 23  ? 9.255   21.796  17.739  1.00 9.77   ?  246  ILE B CG1  1 
ATOM   5486  C  CG2  . ILE B 1 23  ? 9.743   23.948  18.962  1.00 7.10   ?  246  ILE B CG2  1 
ATOM   5487  C  CD1  . ILE B 1 23  ? 7.794   21.719  18.001  1.00 11.30  ?  246  ILE B CD1  1 
ATOM   5488  H  H    . ILE B 1 23  ? 11.294  20.331  18.953  1.00 8.69   ?  246  ILE B H    1 
ATOM   5489  H  HA   . ILE B 1 23  ? 11.754  22.586  17.633  1.00 8.28   ?  246  ILE B HA   1 
ATOM   5490  H  HB   . ILE B 1 23  ? 9.883   22.056  19.696  1.00 9.13   ?  246  ILE B HB   1 
ATOM   5491  H  HG12 . ILE B 1 23  ? 9.375   22.299  16.919  1.00 11.73  ?  246  ILE B HG12 1 
ATOM   5492  H  HG13 . ILE B 1 23  ? 9.575   20.888  17.621  1.00 11.73  ?  246  ILE B HG13 1 
ATOM   5493  H  HG21 . ILE B 1 23  ? 8.786   24.042  19.091  1.00 8.52   ?  246  ILE B HG21 1 
ATOM   5494  H  HG22 . ILE B 1 23  ? 10.218  24.319  19.723  1.00 8.52   ?  246  ILE B HG22 1 
ATOM   5495  H  HG23 . ILE B 1 23  ? 10.014  24.403  18.150  1.00 8.52   ?  246  ILE B HG23 1 
ATOM   5496  H  HD11 . ILE B 1 23  ? 7.369   21.229  17.280  1.00 13.56  ?  246  ILE B HD11 1 
ATOM   5497  H  HD12 . ILE B 1 23  ? 7.647   21.261  18.843  1.00 13.56  ?  246  ILE B HD12 1 
ATOM   5498  H  HD13 . ILE B 1 23  ? 7.433   22.619  18.047  1.00 13.56  ?  246  ILE B HD13 1 
ATOM   5499  N  N    . ASP B 1 24  ? 13.022  24.117  19.107  1.00 6.82   ?  247  ASP B N    1 
ATOM   5500  C  CA   . ASP B 1 24  ? 13.857  24.928  19.981  1.00 7.20   ?  247  ASP B CA   1 
ATOM   5501  C  C    . ASP B 1 24  ? 13.102  26.046  20.689  1.00 7.54   ?  247  ASP B C    1 
ATOM   5502  O  O    . ASP B 1 24  ? 13.373  26.303  21.868  1.00 8.80   ?  247  ASP B O    1 
ATOM   5503  C  CB   . ASP B 1 24  ? 15.037  25.510  19.209  1.00 8.91   ?  247  ASP B CB   1 
ATOM   5504  C  CG   . ASP B 1 24  ? 16.002  24.440  18.774  1.00 10.23  ?  247  ASP B CG   1 
ATOM   5505  O  OD1  . ASP B 1 24  ? 16.292  23.512  19.557  1.00 14.47  ?  247  ASP B OD1  1 
ATOM   5506  O  OD2  . ASP B 1 24  ? 16.444  24.457  17.637  1.00 10.38  -1 247  ASP B OD2  1 
ATOM   5507  H  H    . ASP B 1 24  ? 12.941  24.437  18.313  1.00 8.18   ?  247  ASP B H    1 
ATOM   5508  H  HA   . ASP B 1 24  ? 14.206  24.341  20.670  1.00 8.64   ?  247  ASP B HA   1 
ATOM   5509  H  HB2  . ASP B 1 24  ? 14.708  25.964  18.417  1.00 10.69  ?  247  ASP B HB2  1 
ATOM   5510  H  HB3  . ASP B 1 24  ? 15.513  26.137  19.776  1.00 10.69  ?  247  ASP B HB3  1 
ATOM   5511  N  N    . MET B 1 25  ? 12.152  26.699  20.035  1.00 6.62   ?  248  MET B N    1 
ATOM   5512  C  CA   . MET B 1 25  ? 11.512  27.869  20.625  1.00 6.94   ?  248  MET B CA   1 
ATOM   5513  C  C    . MET B 1 25  ? 10.270  28.228  19.820  1.00 6.79   ?  248  MET B C    1 
ATOM   5514  O  O    . MET B 1 25  ? 10.134  27.846  18.653  1.00 7.41   ?  248  MET B O    1 
ATOM   5515  C  CB   . MET B 1 25  ? 12.468  29.073  20.649  1.00 9.63   ?  248  MET B CB   1 
ATOM   5516  C  CG   . MET B 1 25  ? 12.948  29.496  19.244  1.00 12.77  ?  248  MET B CG   1 
ATOM   5517  S  SD   . MET B 1 25  ? 14.462  30.484  19.201  1.00 17.40  ?  248  MET B SD   1 
ATOM   5518  C  CE   . MET B 1 25  ? 14.035  31.790  20.328  1.00 19.21  ?  248  MET B CE   1 
ATOM   5519  H  H    . MET B 1 25  ? 11.862  26.488  19.253  1.00 7.94   ?  248  MET B H    1 
ATOM   5520  H  HA   . MET B 1 25  ? 11.248  27.647  21.531  1.00 8.32   ?  248  MET B HA   1 
ATOM   5521  H  HB2  . MET B 1 25  ? 12.010  29.830  21.048  1.00 11.55  ?  248  MET B HB2  1 
ATOM   5522  H  HB3  . MET B 1 25  ? 13.250  28.843  21.175  1.00 11.55  ?  248  MET B HB3  1 
ATOM   5523  H  HG2  . MET B 1 25  ? 13.112  28.694  18.724  1.00 15.33  ?  248  MET B HG2  1 
ATOM   5524  H  HG3  . MET B 1 25  ? 12.248  30.023  18.828  1.00 15.33  ?  248  MET B HG3  1 
ATOM   5525  H  HE1  . MET B 1 25  ? 14.769  32.423  20.370  1.00 23.06  ?  248  MET B HE1  1 
ATOM   5526  H  HE2  . MET B 1 25  ? 13.234  32.233  20.009  1.00 23.06  ?  248  MET B HE2  1 
ATOM   5527  H  HE3  . MET B 1 25  ? 13.875  31.410  21.206  1.00 23.06  ?  248  MET B HE3  1 
ATOM   5528  N  N    . LEU B 1 26  ? 9.379   28.988  20.452  1.00 6.66   ?  249  LEU B N    1 
ATOM   5529  C  CA   . LEU B 1 26  ? 8.320   29.688  19.738  1.00 6.92   ?  249  LEU B CA   1 
ATOM   5530  C  C    . LEU B 1 26  ? 8.904   30.913  19.048  1.00 7.71   ?  249  LEU B C    1 
ATOM   5531  O  O    . LEU B 1 26  ? 9.929   31.447  19.473  1.00 9.28   ?  249  LEU B O    1 
ATOM   5532  C  CB   . LEU B 1 26  ? 7.238   30.157  20.717  1.00 7.07   ?  249  LEU B CB   1 
ATOM   5533  C  CG   . LEU B 1 26  ? 6.507   29.077  21.498  1.00 8.05   ?  249  LEU B CG   1 
ATOM   5534  C  CD1  . LEU B 1 26  ? 5.519   29.721  22.448  1.00 8.46   ?  249  LEU B CD1  1 
ATOM   5535  C  CD2  . LEU B 1 26  ? 5.783   28.099  20.610  1.00 9.44   ?  249  LEU B CD2  1 
ATOM   5536  H  H    . LEU B 1 26  ? 9.367   29.115  21.303  1.00 8.00   ?  249  LEU B H    1 
ATOM   5537  H  HA   . LEU B 1 26  ? 7.917   29.097  19.084  1.00 8.30   ?  249  LEU B HA   1 
ATOM   5538  H  HB2  . LEU B 1 26  ? 7.656   30.743  21.366  1.00 8.49   ?  249  LEU B HB2  1 
ATOM   5539  H  HB3  . LEU B 1 26  ? 6.569   30.644  20.211  1.00 8.49   ?  249  LEU B HB3  1 
ATOM   5540  H  HG   . LEU B 1 26  ? 7.171   28.570  21.991  1.00 9.67   ?  249  LEU B HG   1 
ATOM   5541  H  HD11 . LEU B 1 26  ? 5.068   29.027  22.953  1.00 10.16  ?  249  LEU B HD11 1 
ATOM   5542  H  HD12 . LEU B 1 26  ? 5.999   30.310  23.051  1.00 10.16  ?  249  LEU B HD12 1 
ATOM   5543  H  HD13 . LEU B 1 26  ? 4.872   30.229  21.934  1.00 10.16  ?  249  LEU B HD13 1 
ATOM   5544  H  HD21 . LEU B 1 26  ? 5.286   27.477  21.164  1.00 11.33  ?  249  LEU B HD21 1 
ATOM   5545  H  HD22 . LEU B 1 26  ? 5.175   28.587  20.033  1.00 11.33  ?  249  LEU B HD22 1 
ATOM   5546  H  HD23 . LEU B 1 26  ? 6.433   27.619  20.073  1.00 11.33  ?  249  LEU B HD23 1 
ATOM   5547  N  N    . HIS B 1 27  ? 8.268   31.335  17.956  1.00 7.22   ?  250  HIS B N    1 
ATOM   5548  C  CA   . HIS B 1 27  ? 8.706   32.502  17.202  1.00 7.49   ?  250  HIS B CA   1 
ATOM   5549  C  C    . HIS B 1 27  ? 7.493   33.196  16.602  1.00 6.87   ?  250  HIS B C    1 
ATOM   5550  O  O    . HIS B 1 27  ? 6.623   32.532  16.051  1.00 7.21   ?  250  HIS B O    1 
ATOM   5551  C  CB   . HIS B 1 27  ? 9.612   32.101  16.019  1.00 9.19   ?  250  HIS B CB   1 
ATOM   5552  C  CG   . HIS B 1 27  ? 9.902   33.237  15.088  1.00 10.28  ?  250  HIS B CG   1 
ATOM   5553  N  ND1  . HIS B 1 27  ? 10.883  34.157  15.360  1.00 10.17  ?  250  HIS B ND1  1 
ATOM   5554  C  CD2  . HIS B 1 27  ? 9.286   33.668  13.960  1.00 10.45  ?  250  HIS B CD2  1 
ATOM   5555  C  CE1  . HIS B 1 27  ? 10.888  35.090  14.425  1.00 11.07  ?  250  HIS B CE1  1 
ATOM   5556  N  NE2  . HIS B 1 27  ? 9.930   34.813  13.557  1.00 11.53  ?  250  HIS B NE2  1 
ATOM   5557  H  H    . HIS B 1 27  ? 7.570   30.955  17.629  1.00 8.66   ?  250  HIS B H    1 
ATOM   5558  H  HA   . HIS B 1 27  ? 9.174   33.096  17.810  1.00 8.99   ?  250  HIS B HA   1 
ATOM   5559  H  HB2  . HIS B 1 27  ? 10.458  31.777  16.366  1.00 11.03  ?  250  HIS B HB2  1 
ATOM   5560  H  HB3  . HIS B 1 27  ? 9.173   31.402  15.509  1.00 11.03  ?  250  HIS B HB3  1 
ATOM   5561  H  HD1  . HIS B 1 27  ? 11.414  34.131  16.037  1.00 12.21  ?  250  HIS B HD1  1 
ATOM   5562  H  HD2  . HIS B 1 27  ? 8.563   33.264  13.537  1.00 12.54  ?  250  HIS B HD2  1 
ATOM   5563  H  HE1  . HIS B 1 27  ? 11.466  35.817  14.385  1.00 13.28  ?  250  HIS B HE1  1 
ATOM   5564  N  N    . THR B 1 28  ? 7.460   34.528  16.662  1.00 6.72   ?  251  THR B N    1 
ATOM   5565  C  CA   . THR B 1 28  ? 6.496   35.277  15.857  1.00 7.01   ?  251  THR B CA   1 
ATOM   5566  C  C    . THR B 1 28  ? 7.152   36.529  15.298  1.00 8.27   ?  251  THR B C    1 
ATOM   5567  O  O    . THR B 1 28  ? 7.972   37.155  15.960  1.00 8.97   ?  251  THR B O    1 
ATOM   5568  C  CB   . THR B 1 28  ? 5.196   35.586  16.616  1.00 7.53   ?  251  THR B CB   1 
ATOM   5569  O  OG1  . THR B 1 28  ? 4.249   36.208  15.746  1.00 7.67   ?  251  THR B OG1  1 
ATOM   5570  C  CG2  . THR B 1 28  ? 5.404   36.497  17.791  1.00 7.89   ?  251  THR B CG2  1 
ATOM   5571  H  H    . THR B 1 28  ? 7.976   35.010  17.153  1.00 8.07   ?  251  THR B H    1 
ATOM   5572  H  HA   . THR B 1 28  ? 6.232   34.740  15.094  1.00 8.41   ?  251  THR B HA   1 
ATOM   5573  H  HB   . THR B 1 28  ? 4.859   34.739  16.948  1.00 9.04   ?  251  THR B HB   1 
ATOM   5574  H  HG1  . THR B 1 28  ? 4.058   35.691  15.112  1.00 9.21   ?  251  THR B HG1  1 
ATOM   5575  H  HG21 . THR B 1 28  ? 4.572   36.607  18.277  1.00 9.47   ?  251  THR B HG21 1 
ATOM   5576  H  HG22 . THR B 1 28  ? 6.070   36.121  18.388  1.00 9.47   ?  251  THR B HG22 1 
ATOM   5577  H  HG23 . THR B 1 28  ? 5.709   37.366  17.487  1.00 9.47   ?  251  THR B HG23 1 
ATOM   5578  N  N    . SER B 1 29  ? 6.794   36.881  14.071  1.00 8.65   ?  252  SER B N    1 
ATOM   5579  C  CA   . SER B 1 29  ? 7.320   38.076  13.425  1.00 9.29   ?  252  SER B CA   1 
ATOM   5580  C  C    . SER B 1 29  ? 6.370   38.461  12.303  1.00 11.31  ?  252  SER B C    1 
ATOM   5581  O  O    . SER B 1 29  ? 5.485   37.683  11.932  1.00 11.34  ?  252  SER B O    1 
ATOM   5582  C  CB   . SER B 1 29  ? 8.746   37.852  12.901  1.00 10.34  ?  252  SER B CB   1 
ATOM   5583  O  OG   . SER B 1 29  ? 8.809   36.784  11.982  1.00 11.44  ?  252  SER B OG   1 
ATOM   5584  H  H    . SER B 1 29  ? 6.240   36.438  13.584  1.00 10.38  ?  252  SER B H    1 
ATOM   5585  H  HA   . SER B 1 29  ? 7.347   38.806  14.063  1.00 11.15  ?  252  SER B HA   1 
ATOM   5586  H  HB2  . SER B 1 29  ? 9.046   38.662  12.459  1.00 12.41  ?  252  SER B HB2  1 
ATOM   5587  H  HB3  . SER B 1 29  ? 9.326   37.651  13.652  1.00 12.41  ?  252  SER B HB3  1 
ATOM   5588  H  HG   . SER B 1 29  ? 8.415   36.112  12.296  1.00 13.73  ?  252  SER B HG   1 
ATOM   5589  N  N    . PRO B 1 30  ? 6.512   39.668  11.757  1.00 12.17  ?  253  PRO B N    1 
ATOM   5590  C  CA   . PRO B 1 30  ? 5.657   40.074  10.632  1.00 12.09  ?  253  PRO B CA   1 
ATOM   5591  C  C    . PRO B 1 30  ? 5.945   39.240  9.394   1.00 11.21  ?  253  PRO B C    1 
ATOM   5592  O  O    . PRO B 1 30  ? 7.100   38.915  9.107   1.00 13.36  ?  253  PRO B O    1 
ATOM   5593  C  CB   . PRO B 1 30  ? 6.042   41.543  10.413  1.00 13.78  ?  253  PRO B CB   1 
ATOM   5594  C  CG   . PRO B 1 30  ? 6.669   41.987  11.668  1.00 13.77  ?  253  PRO B CG   1 
ATOM   5595  C  CD   . PRO B 1 30  ? 7.311   40.788  12.279  1.00 13.13  ?  253  PRO B CD   1 
ATOM   5596  H  HA   . PRO B 1 30  ? 4.718   40.007  10.866  1.00 14.51  ?  253  PRO B HA   1 
ATOM   5597  H  HB2  . PRO B 1 30  ? 6.666   41.610  9.673   1.00 16.54  ?  253  PRO B HB2  1 
ATOM   5598  H  HB3  . PRO B 1 30  ? 5.246   42.065  10.223  1.00 16.54  ?  253  PRO B HB3  1 
ATOM   5599  H  HG2  . PRO B 1 30  ? 7.334   42.666  11.474  1.00 16.53  ?  253  PRO B HG2  1 
ATOM   5600  H  HG3  . PRO B 1 30  ? 5.990   42.347  12.259  1.00 16.53  ?  253  PRO B HG3  1 
ATOM   5601  H  HD2  . PRO B 1 30  ? 8.236   40.711  11.998  1.00 15.75  ?  253  PRO B HD2  1 
ATOM   5602  H  HD3  . PRO B 1 30  ? 7.260   40.825  13.247  1.00 15.75  ?  253  PRO B HD3  1 
ATOM   5603  N  N    . THR B 1 31  ? 4.883   38.882  8.656   1.00 11.52  ?  254  THR B N    1 
ATOM   5604  C  CA   . THR B 1 31  ? 5.029   38.089  7.437   1.00 12.87  ?  254  THR B CA   1 
ATOM   5605  C  C    . THR B 1 31  ? 4.240   38.666  6.266   1.00 14.98  ?  254  THR B C    1 
ATOM   5606  O  O    . THR B 1 31  ? 3.969   37.949  5.298   1.00 14.87  ?  254  THR B O    1 
ATOM   5607  C  CB   . THR B 1 31  ? 4.625   36.626  7.658   1.00 13.90  ?  254  THR B CB   1 
ATOM   5608  O  OG1  . THR B 1 31  ? 3.291   36.557  8.177   1.00 14.62  ?  254  THR B OG1  1 
ATOM   5609  C  CG2  . THR B 1 31  ? 5.583   35.957  8.622   1.00 14.95  ?  254  THR B CG2  1 
ATOM   5610  H  H    . THR B 1 31  ? 4.070   39.089  8.846   1.00 13.83  ?  254  THR B H    1 
ATOM   5611  H  HA   . THR B 1 31  ? 5.969   38.104  7.198   1.00 15.45  ?  254  THR B HA   1 
ATOM   5612  H  HB   . THR B 1 31  ? 4.657   36.150  6.813   1.00 16.68  ?  254  THR B HB   1 
ATOM   5613  H  HG1  . THR B 1 31  ? 2.759   36.940  7.652   1.00 17.55  ?  254  THR B HG1  1 
ATOM   5614  H  HG21 . THR B 1 31  ? 5.365   35.015  8.706   1.00 17.95  ?  254  THR B HG21 1 
ATOM   5615  H  HG22 . THR B 1 31  ? 6.493   36.041  8.297   1.00 17.95  ?  254  THR B HG22 1 
ATOM   5616  H  HG23 . THR B 1 31  ? 5.520   36.374  9.495   1.00 17.95  ?  254  THR B HG23 1 
ATOM   5617  N  N    . GLU B 1 32  ? 3.880   39.951  6.326   1.00 17.42  ?  255  GLU B N    1 
ATOM   5618  C  CA   . GLU B 1 32  ? 3.067   40.543  5.266   1.00 21.53  ?  255  GLU B CA   1 
ATOM   5619  C  C    . GLU B 1 32  ? 3.763   40.472  3.910   1.00 21.80  ?  255  GLU B C    1 
ATOM   5620  O  O    . GLU B 1 32  ? 3.090   40.451  2.871   1.00 22.86  ?  255  GLU B O    1 
ATOM   5621  C  CB   . GLU B 1 32  ? 2.740   42.005  5.592   1.00 25.10  ?  255  GLU B CB   1 
ATOM   5622  C  CG   . GLU B 1 32  ? 2.136   42.256  6.968   1.00 28.46  ?  255  GLU B CG   1 
ATOM   5623  C  CD   . GLU B 1 32  ? 3.172   42.680  7.998   1.00 31.20  ?  255  GLU B CD   1 
ATOM   5624  O  OE1  . GLU B 1 32  ? 4.343   42.258  7.889   1.00 31.00  ?  255  GLU B OE1  1 
ATOM   5625  O  OE2  . GLU B 1 32  ? 2.813   43.448  8.917   1.00 33.14  -1 255  GLU B OE2  1 
ATOM   5626  H  H    . GLU B 1 32  ? 4.090   40.492  6.960   1.00 20.90  ?  255  GLU B H    1 
ATOM   5627  H  HA   . GLU B 1 32  ? 2.236   40.045  5.215   1.00 25.84  ?  255  GLU B HA   1 
ATOM   5628  H  HB2  . GLU B 1 32  ? 3.560   42.520  5.540   1.00 30.13  ?  255  GLU B HB2  1 
ATOM   5629  H  HB3  . GLU B 1 32  ? 2.103   42.328  4.936   1.00 30.13  ?  255  GLU B HB3  1 
ATOM   5630  H  HG2  . GLU B 1 32  ? 1.475   42.962  6.898   1.00 34.16  ?  255  GLU B HG2  1 
ATOM   5631  H  HG3  . GLU B 1 32  ? 1.717   41.440  7.282   1.00 34.16  ?  255  GLU B HG3  1 
ATOM   5632  N  N    . ASN B 1 33  ? 5.097   40.438  3.893   1.00 21.47  ?  256  ASN B N    1 
ATOM   5633  C  CA   . ASN B 1 33  ? 5.858   40.463  2.652   1.00 23.94  ?  256  ASN B CA   1 
ATOM   5634  C  C    . ASN B 1 33  ? 6.425   39.103  2.253   1.00 22.53  ?  256  ASN B C    1 
ATOM   5635  O  O    . ASN B 1 33  ? 7.250   39.033  1.339   1.00 24.40  ?  256  ASN B O    1 
ATOM   5636  C  CB   . ASN B 1 33  ? 6.990   41.492  2.745   1.00 27.52  ?  256  ASN B CB   1 
ATOM   5637  C  CG   . ASN B 1 33  ? 6.491   42.922  2.641   1.00 30.83  ?  256  ASN B CG   1 
ATOM   5638  O  OD1  . ASN B 1 33  ? 5.312   43.165  2.372   1.00 32.25  ?  256  ASN B OD1  1 
ATOM   5639  N  ND2  . ASN B 1 33  ? 7.391   43.878  2.839   1.00 32.20  ?  256  ASN B ND2  1 
ATOM   5640  H  H    . ASN B 1 33  ? 5.586   40.399  4.599   1.00 25.77  ?  256  ASN B H    1 
ATOM   5641  H  HA   . ASN B 1 33  ? 5.254   40.739  1.945   1.00 28.73  ?  256  ASN B HA   1 
ATOM   5642  H  HB2  . ASN B 1 33  ? 7.440   41.392  3.598   1.00 33.03  ?  256  ASN B HB2  1 
ATOM   5643  H  HB3  . ASN B 1 33  ? 7.617   41.339  2.020   1.00 33.03  ?  256  ASN B HB3  1 
ATOM   5644  H  HD21 . ASN B 1 33  ? 7.158   44.705  2.791   1.00 38.64  ?  256  ASN B HD21 1 
ATOM   5645  H  HD22 . ASN B 1 33  ? 8.207   43.671  3.015   1.00 38.64  ?  256  ASN B HD22 1 
ATOM   5646  N  N    . ILE B 1 34  ? 6.015   38.027  2.912   1.00 19.18  ?  257  ILE B N    1 
ATOM   5647  C  CA   . ILE B 1 34  ? 6.396   36.687  2.492   1.00 19.28  ?  257  ILE B CA   1 
ATOM   5648  C  C    . ILE B 1 34  ? 5.114   35.896  2.298   1.00 17.14  ?  257  ILE B C    1 
ATOM   5649  O  O    . ILE B 1 34  ? 4.067   36.233  2.844   1.00 19.57  ?  257  ILE B O    1 
ATOM   5650  C  CB   . ILE B 1 34  ? 7.336   35.995  3.495   1.00 23.02  ?  257  ILE B CB   1 
ATOM   5651  C  CG1  . ILE B 1 34  ? 6.606   35.638  4.785   1.00 24.65  ?  257  ILE B CG1  1 
ATOM   5652  C  CG2  . ILE B 1 34  ? 8.524   36.896  3.810   1.00 24.41  ?  257  ILE B CG2  1 
ATOM   5653  C  CD1  . ILE B 1 34  ? 7.345   34.617  5.611   1.00 25.41  ?  257  ILE B CD1  1 
ATOM   5654  H  H    . ILE B 1 34  ? 5.513   38.048  3.609   1.00 23.02  ?  257  ILE B H    1 
ATOM   5655  H  HA   . ILE B 1 34  ? 6.871   36.726  1.647   1.00 23.14  ?  257  ILE B HA   1 
ATOM   5656  H  HB   . ILE B 1 34  ? 7.649   35.173  3.085   1.00 27.63  ?  257  ILE B HB   1 
ATOM   5657  H  HG12 . ILE B 1 34  ? 6.503   36.439  5.321   1.00 29.58  ?  257  ILE B HG12 1 
ATOM   5658  H  HG13 . ILE B 1 34  ? 5.736   35.272  4.564   1.00 29.58  ?  257  ILE B HG13 1 
ATOM   5659  H  HG21 . ILE B 1 34  ? 9.167   36.398  4.338   1.00 29.29  ?  257  ILE B HG21 1 
ATOM   5660  H  HG22 . ILE B 1 34  ? 8.930   37.185  2.978   1.00 29.29  ?  257  ILE B HG22 1 
ATOM   5661  H  HG23 . ILE B 1 34  ? 8.211   37.667  4.310   1.00 29.29  ?  257  ILE B HG23 1 
ATOM   5662  H  HD11 . ILE B 1 34  ? 6.889   34.508  6.460   1.00 30.49  ?  257  ILE B HD11 1 
ATOM   5663  H  HD12 . ILE B 1 34  ? 7.359   33.773  5.132   1.00 30.49  ?  257  ILE B HD12 1 
ATOM   5664  H  HD13 . ILE B 1 34  ? 8.252   34.927  5.759   1.00 30.49  ?  257  ILE B HD13 1 
ATOM   5665  N  N    . VAL B 1 35  ? 5.196   34.836  1.519   1.00 14.92  ?  258  VAL B N    1 
ATOM   5666  C  CA   . VAL B 1 35  ? 4.072   33.919  1.362   1.00 13.38  ?  258  VAL B CA   1 
ATOM   5667  C  C    . VAL B 1 35  ? 4.385   32.686  2.192   1.00 11.98  ?  258  VAL B C    1 
ATOM   5668  O  O    . VAL B 1 35  ? 5.362   31.975  1.926   1.00 13.85  ?  258  VAL B O    1 
ATOM   5669  C  CB   . VAL B 1 35  ? 3.818   33.564  -0.108  1.00 15.16  ?  258  VAL B CB   1 
ATOM   5670  C  CG1  . VAL B 1 35  ? 2.733   32.494  -0.227  1.00 15.76  ?  258  VAL B CG1  1 
ATOM   5671  C  CG2  . VAL B 1 35  ? 3.405   34.807  -0.889  1.00 17.03  ?  258  VAL B CG2  1 
ATOM   5672  H  H    . VAL B 1 35  ? 5.895   34.620  1.067   1.00 17.91  ?  258  VAL B H    1 
ATOM   5673  H  HA   . VAL B 1 35  ? 3.261   34.331  1.700   1.00 16.06  ?  258  VAL B HA   1 
ATOM   5674  H  HB   . VAL B 1 35  ? 4.638   33.212  -0.487  1.00 18.20  ?  258  VAL B HB   1 
ATOM   5675  H  HG11 . VAL B 1 35  ? 2.456   32.426  -1.154  1.00 18.91  ?  258  VAL B HG11 1 
ATOM   5676  H  HG12 . VAL B 1 35  ? 3.093   31.645  0.074   1.00 18.91  ?  258  VAL B HG12 1 
ATOM   5677  H  HG13 . VAL B 1 35  ? 1.977   32.747  0.327   1.00 18.91  ?  258  VAL B HG13 1 
ATOM   5678  H  HG21 . VAL B 1 35  ? 3.243   34.561  -1.813  1.00 20.44  ?  258  VAL B HG21 1 
ATOM   5679  H  HG22 . VAL B 1 35  ? 2.596   35.172  -0.497  1.00 20.44  ?  258  VAL B HG22 1 
ATOM   5680  H  HG23 . VAL B 1 35  ? 4.119   35.462  -0.842  1.00 20.44  ?  258  VAL B HG23 1 
ATOM   5681  N  N    . VAL B 1 36  ? 3.574   32.444  3.213   1.00 8.23   ?  259  VAL B N    1 
ATOM   5682  C  CA   . VAL B 1 36  ? 3.779   31.329  4.125   1.00 7.44   ?  259  VAL B CA   1 
ATOM   5683  C  C    . VAL B 1 36  ? 2.948   30.164  3.591   1.00 6.77   ?  259  VAL B C    1 
ATOM   5684  O  O    . VAL B 1 36  ? 1.726   30.097  3.793   1.00 7.31   ?  259  VAL B O    1 
ATOM   5685  C  CB   . VAL B 1 36  ? 3.409   31.721  5.559   1.00 8.06   ?  259  VAL B CB   1 
ATOM   5686  C  CG1  . VAL B 1 36  ? 3.595   30.522  6.492   1.00 8.03   ?  259  VAL B CG1  1 
ATOM   5687  C  CG2  . VAL B 1 36  ? 4.232   32.900  6.048   1.00 10.13  ?  259  VAL B CG2  1 
ATOM   5688  H  H    . VAL B 1 36  ? 2.885   32.922  3.402   1.00 9.88   ?  259  VAL B H    1 
ATOM   5689  H  HA   . VAL B 1 36  ? 4.708   31.053  4.120   1.00 8.93   ?  259  VAL B HA   1 
ATOM   5690  H  HB   . VAL B 1 36  ? 2.477   31.992  5.571   1.00 9.67   ?  259  VAL B HB   1 
ATOM   5691  H  HG11 . VAL B 1 36  ? 3.474   30.814  7.409   1.00 9.63   ?  259  VAL B HG11 1 
ATOM   5692  H  HG12 . VAL B 1 36  ? 2.937   29.844  6.271   1.00 9.63   ?  259  VAL B HG12 1 
ATOM   5693  H  HG13 . VAL B 1 36  ? 4.490   30.166  6.374   1.00 9.63   ?  259  VAL B HG13 1 
ATOM   5694  H  HG21 . VAL B 1 36  ? 3.989   33.095  6.967   1.00 12.15  ?  259  VAL B HG21 1 
ATOM   5695  H  HG22 . VAL B 1 36  ? 5.173   32.671  5.996   1.00 12.15  ?  259  VAL B HG22 1 
ATOM   5696  H  HG23 . VAL B 1 36  ? 4.046   33.669  5.486   1.00 12.15  ?  259  VAL B HG23 1 
ATOM   5697  N  N    . GLN B 1 37  ? 3.607   29.241  2.881   1.00 6.50   ?  260  GLN B N    1 
ATOM   5698  C  CA   . GLN B 1 37  ? 2.910   28.130  2.247   1.00 6.74   ?  260  GLN B CA   1 
ATOM   5699  C  C    . GLN B 1 37  ? 3.691   26.828  2.393   1.00 5.87   ?  260  GLN B C    1 
ATOM   5700  O  O    . GLN B 1 37  ? 3.924   26.109  1.408   1.00 5.55   ?  260  GLN B O    1 
ATOM   5701  C  CB   . GLN B 1 37  ? 2.653   28.453  0.773   1.00 6.95   ?  260  GLN B CB   1 
ATOM   5702  C  CG   . GLN B 1 37  ? 1.646   27.548  0.137   1.00 8.77   ?  260  GLN B CG   1 
ATOM   5703  C  CD   . GLN B 1 37  ? 1.182   28.002  -1.221  1.00 10.50  ?  260  GLN B CD   1 
ATOM   5704  O  OE1  . GLN B 1 37  ? 1.825   28.825  -1.885  1.00 13.49  ?  260  GLN B OE1  1 
ATOM   5705  N  NE2  . GLN B 1 37  ? 0.061   27.443  -1.650  1.00 9.98   ?  260  GLN B NE2  1 
ATOM   5706  H  H    . GLN B 1 37  ? 4.458   29.241  2.755   1.00 7.80   ?  260  GLN B H    1 
ATOM   5707  H  HA   . GLN B 1 37  ? 2.059   27.993  2.691   1.00 8.09   ?  260  GLN B HA   1 
ATOM   5708  H  HB2  . GLN B 1 37  ? 2.322   29.363  0.704   1.00 8.35   ?  260  GLN B HB2  1 
ATOM   5709  H  HB3  . GLN B 1 37  ? 3.485   28.365  0.283   1.00 8.35   ?  260  GLN B HB3  1 
ATOM   5710  H  HG2  . GLN B 1 37  ? 2.040   26.668  0.034   1.00 10.52  ?  260  GLN B HG2  1 
ATOM   5711  H  HG3  . GLN B 1 37  ? 0.867   27.497  0.713   1.00 10.52  ?  260  GLN B HG3  1 
ATOM   5712  H  HE21 . GLN B 1 37  ? -0.346  26.865  -1.160  1.00 11.98  ?  260  GLN B HE21 1 
ATOM   5713  H  HE22 . GLN B 1 37  ? -0.260  27.657  -2.418  1.00 11.98  ?  260  GLN B HE22 1 
ATOM   5714  N  N    . PRO B 1 38  ? 4.111   26.469  3.610   1.00 5.71   ?  261  PRO B N    1 
ATOM   5715  C  CA   . PRO B 1 38  ? 4.807   25.191  3.779   1.00 5.45   ?  261  PRO B CA   1 
ATOM   5716  C  C    . PRO B 1 38  ? 3.886   24.034  3.424   1.00 5.28   ?  261  PRO B C    1 
ATOM   5717  O  O    . PRO B 1 38  ? 2.657   24.137  3.471   1.00 5.71   ?  261  PRO B O    1 
ATOM   5718  C  CB   . PRO B 1 38  ? 5.186   25.187  5.261   1.00 5.66   ?  261  PRO B CB   1 
ATOM   5719  C  CG   . PRO B 1 38  ? 4.099   26.021  5.904   1.00 6.34   ?  261  PRO B CG   1 
ATOM   5720  C  CD   . PRO B 1 38  ? 3.793   27.103  4.907   1.00 5.90   ?  261  PRO B CD   1 
ATOM   5721  H  HA   . PRO B 1 38  ? 5.617   25.145  3.246   1.00 6.54   ?  261  PRO B HA   1 
ATOM   5722  H  HB2  . PRO B 1 38  ? 5.185   24.280  5.606   1.00 6.80   ?  261  PRO B HB2  1 
ATOM   5723  H  HB3  . PRO B 1 38  ? 6.060   25.589  5.386   1.00 6.80   ?  261  PRO B HB3  1 
ATOM   5724  H  HG2  . PRO B 1 38  ? 3.317   25.473  6.071   1.00 7.61   ?  261  PRO B HG2  1 
ATOM   5725  H  HG3  . PRO B 1 38  ? 4.423   26.400  6.737   1.00 7.61   ?  261  PRO B HG3  1 
ATOM   5726  H  HD2  . PRO B 1 38  ? 2.857   27.356  4.947   1.00 7.08   ?  261  PRO B HD2  1 
ATOM   5727  H  HD3  . PRO B 1 38  ? 4.353   27.881  5.057   1.00 7.08   ?  261  PRO B HD3  1 
ATOM   5728  N  N    . GLN B 1 39  ? 4.498   22.915  3.061   1.00 5.52   ?  262  GLN B N    1 
ATOM   5729  C  CA   . GLN B 1 39  ? 3.762   21.730  2.639   1.00 5.21   ?  262  GLN B CA   1 
ATOM   5730  C  C    . GLN B 1 39  ? 3.899   20.556  3.596   1.00 5.41   ?  262  GLN B C    1 
ATOM   5731  O  O    . GLN B 1 39  ? 3.038   19.674  3.575   1.00 6.03   ?  262  GLN B O    1 
ATOM   5732  C  CB   . GLN B 1 39  ? 4.174   21.317  1.219   1.00 5.40   ?  262  GLN B CB   1 
ATOM   5733  C  CG   . GLN B 1 39  ? 3.897   22.401  0.192   1.00 6.23   ?  262  GLN B CG   1 
ATOM   5734  C  CD   . GLN B 1 39  ? 2.429   22.754  0.135   1.00 6.06   ?  262  GLN B CD   1 
ATOM   5735  O  OE1  . GLN B 1 39  ? 1.585   21.883  -0.038  1.00 6.63   ?  262  GLN B OE1  1 
ATOM   5736  N  NE2  . GLN B 1 39  ? 2.122   24.045  0.279   1.00 6.40   ?  262  GLN B NE2  1 
ATOM   5737  H  H    . GLN B 1 39  ? 5.352   22.814  3.050   1.00 6.63   ?  262  GLN B H    1 
ATOM   5738  H  HA   . GLN B 1 39  ? 2.817   21.943  2.596   1.00 6.26   ?  262  GLN B HA   1 
ATOM   5739  H  HB2  . GLN B 1 39  ? 5.126   21.129  1.207   1.00 6.48   ?  262  GLN B HB2  1 
ATOM   5740  H  HB3  . GLN B 1 39  ? 3.676   20.525  0.963   1.00 6.48   ?  262  GLN B HB3  1 
ATOM   5741  H  HG2  . GLN B 1 39  ? 4.393   23.200  0.427   1.00 7.47   ?  262  GLN B HG2  1 
ATOM   5742  H  HG3  . GLN B 1 39  ? 4.168   22.087  -0.685  1.00 7.47   ?  262  GLN B HG3  1 
ATOM   5743  H  HE21 . GLN B 1 39  ? 2.746   24.625  0.396   1.00 7.69   ?  262  GLN B HE21 1 
ATOM   5744  H  HE22 . GLN B 1 39  ? 1.300   24.297  0.254   1.00 7.69   ?  262  GLN B HE22 1 
ATOM   5745  N  N    . ASN B 1 40  ? 4.940   20.531  4.424   1.00 5.43   ?  263  ASN B N    1 
ATOM   5746  C  CA   . ASN B 1 40  ? 5.027   19.616  5.553   1.00 5.49   ?  263  ASN B CA   1 
ATOM   5747  C  C    . ASN B 1 40  ? 4.483   20.314  6.792   1.00 5.00   ?  263  ASN B C    1 
ATOM   5748  O  O    . ASN B 1 40  ? 4.452   21.546  6.871   1.00 5.79   ?  263  ASN B O    1 
ATOM   5749  C  CB   . ASN B 1 40  ? 6.465   19.152  5.743   1.00 5.40   ?  263  ASN B CB   1 
ATOM   5750  C  CG   . ASN B 1 40  ? 6.885   18.172  4.662   1.00 5.88   ?  263  ASN B CG   1 
ATOM   5751  O  OD1  . ASN B 1 40  ? 6.123   17.256  4.306   1.00 5.97   ?  263  ASN B OD1  1 
ATOM   5752  N  ND2  . ASN B 1 40  ? 8.083   18.348  4.131   1.00 5.88   ?  263  ASN B ND2  1 
ATOM   5753  H  H    . ASN B 1 40  ? 5.624   21.047  4.349   1.00 6.51   ?  263  ASN B H    1 
ATOM   5754  H  HA   . ASN B 1 40  ? 4.498   18.816  5.406   1.00 6.58   ?  263  ASN B HA   1 
ATOM   5755  H  HB2  . ASN B 1 40  ? 7.057   19.919  5.705   1.00 6.48   ?  263  ASN B HB2  1 
ATOM   5756  H  HB3  . ASN B 1 40  ? 6.548   18.711  6.603   1.00 6.48   ?  263  ASN B HB3  1 
ATOM   5757  H  HD21 . ASN B 1 40  ? 8.363   17.817  3.515   1.00 7.05   ?  263  ASN B HD21 1 
ATOM   5758  H  HD22 . ASN B 1 40  ? 8.583   18.994  4.401   1.00 7.05   ?  263  ASN B HD22 1 
ATOM   5759  N  N    . GLY B 1 41  ? 3.993   19.519  7.737   1.00 5.77   ?  264  GLY B N    1 
ATOM   5760  C  CA   . GLY B 1 41  ? 3.368   20.073  8.928   1.00 5.18   ?  264  GLY B CA   1 
ATOM   5761  C  C    . GLY B 1 41  ? 2.051   20.760  8.663   1.00 5.58   ?  264  GLY B C    1 
ATOM   5762  O  O    . GLY B 1 41  ? 1.722   21.749  9.338   1.00 6.22   ?  264  GLY B O    1 
ATOM   5763  H  H    . GLY B 1 41  ? 4.011   18.660  7.711   1.00 6.92   ?  264  GLY B H    1 
ATOM   5764  H  HA2  . GLY B 1 41  ? 3.209   19.356  9.562   1.00 6.22   ?  264  GLY B HA2  1 
ATOM   5765  H  HA3  . GLY B 1 41  ? 3.969   20.721  9.327   1.00 6.22   ?  264  GLY B HA3  1 
ATOM   5766  N  N    . ARG B 1 42  ? 1.269   20.232  7.724   1.00 5.48   ?  265  ARG B N    1 
ATOM   5767  C  CA   . ARG B 1 42  ? -0.028  20.776  7.342   1.00 5.65   ?  265  ARG B CA   1 
ATOM   5768  C  C    . ARG B 1 42  ? -1.109  19.755  7.660   1.00 5.68   ?  265  ARG B C    1 
ATOM   5769  O  O    . ARG B 1 42  ? -1.222  18.714  7.007   1.00 6.46   ?  265  ARG B O    1 
ATOM   5770  C  CB   . ARG B 1 42  ? -0.032  21.142  5.862   1.00 6.47   ?  265  ARG B CB   1 
ATOM   5771  C  CG   . ARG B 1 42  ? 1.023   22.174  5.450   1.00 7.18   ?  265  ARG B CG   1 
ATOM   5772  C  CD   . ARG B 1 42  ? 0.890   23.510  6.163   1.00 7.51   ?  265  ARG B CD   1 
ATOM   5773  N  NE   . ARG B 1 42  ? -0.380  24.163  5.873   1.00 7.67   ?  265  ARG B NE   1 
ATOM   5774  C  CZ   . ARG B 1 42  ? -0.612  25.103  4.966   1.00 9.39   ?  265  ARG B CZ   1 
ATOM   5775  N  NH1  . ARG B 1 42  ? 0.358   25.597  4.183   1.00 9.63   ?  265  ARG B NH1  1 
ATOM   5776  N  NH2  . ARG B 1 42  ? -1.857  25.554  4.825   1.00 10.83  ?  265  ARG B NH2  1 
ATOM   5777  H  H    . ARG B 1 42  ? 1.479   19.528  7.277   1.00 6.58   ?  265  ARG B H    1 
ATOM   5778  H  HA   . ARG B 1 42  ? -0.213  21.572  7.865   1.00 6.78   ?  265  ARG B HA   1 
ATOM   5779  H  HB2  . ARG B 1 42  ? 0.131   20.337  5.345   1.00 7.76   ?  265  ARG B HB2  1 
ATOM   5780  H  HB3  . ARG B 1 42  ? -0.902  21.509  5.638   1.00 7.76   ?  265  ARG B HB3  1 
ATOM   5781  H  HG2  . ARG B 1 42  ? 1.902   21.819  5.653   1.00 8.62   ?  265  ARG B HG2  1 
ATOM   5782  H  HG3  . ARG B 1 42  ? 0.943   22.339  4.498   1.00 8.62   ?  265  ARG B HG3  1 
ATOM   5783  H  HD2  . ARG B 1 42  ? 0.945   23.367  7.120   1.00 9.02   ?  265  ARG B HD2  1 
ATOM   5784  H  HD3  . ARG B 1 42  ? 1.605   24.097  5.873   1.00 9.02   ?  265  ARG B HD3  1 
ATOM   5785  H  HE   . ARG B 1 42  ? -1.055  23.911  6.343   1.00 9.21   ?  265  ARG B HE   1 
ATOM   5786  H  HH11 . ARG B 1 42  ? 1.163   25.305  4.259   1.00 11.56  ?  265  ARG B HH11 1 
ATOM   5787  H  HH12 . ARG B 1 42  ? 0.175   26.207  3.604   1.00 11.56  ?  265  ARG B HH12 1 
ATOM   5788  H  HH21 . ARG B 1 42  ? -2.487  25.235  5.316   1.00 12.99  ?  265  ARG B HH21 1 
ATOM   5789  H  HH22 . ARG B 1 42  ? -2.030  26.163  4.244   1.00 12.99  ?  265  ARG B HH22 1 
ATOM   5790  N  N    . CYS B 1 43  ? -1.911  20.058  8.667   1.00 6.46   ?  266  CYS B N    1 
ATOM   5791  C  CA   . CYS B 1 43  ? -3.033  19.220  9.056   1.00 6.53   ?  266  CYS B CA   1 
ATOM   5792  C  C    . CYS B 1 43  ? -4.113  20.120  9.621   1.00 7.32   ?  266  CYS B C    1 
ATOM   5793  O  O    . CYS B 1 43  ? -3.838  20.954  10.490  1.00 8.00   ?  266  CYS B O    1 
ATOM   5794  C  CB   . CYS B 1 43  ? -2.579  18.215  10.115  1.00 7.90   ?  266  CYS B CB   1 
ATOM   5795  S  SG   . CYS B 1 43  ? -3.818  16.966  10.578  1.00 8.77   ?  266  CYS B SG   1 
ATOM   5796  H  H    . CYS B 1 43  ? -1.825  20.761  9.155   1.00 7.75   ?  266  CYS B H    1 
ATOM   5797  H  HA   . CYS B 1 43  ? -3.393  18.741  8.293   1.00 7.83   ?  266  CYS B HA   1 
ATOM   5798  H  HB2  . CYS B 1 43  ? -1.803  17.742  9.775   1.00 9.49   ?  266  CYS B HB2  1 
ATOM   5799  H  HB3  . CYS B 1 43  ? -2.344  18.703  10.919  1.00 9.49   ?  266  CYS B HB3  1 
ATOM   5800  H  HG   . CYS B 1 43  ? -4.729  17.508  11.140  1.00 10.52  ?  266  CYS B HG   1 
ATOM   5801  N  N    . THR B 1 44  ? -5.336  19.958  9.131   1.00 6.47   ?  267  THR B N    1 
ATOM   5802  C  CA   . THR B 1 44  ? -6.433  20.702  9.741   1.00 6.28   ?  267  THR B CA   1 
ATOM   5803  C  C    . THR B 1 44  ? -6.689  20.191  11.163  1.00 6.13   ?  267  THR B C    1 
ATOM   5804  O  O    . THR B 1 44  ? -6.335  19.065  11.520  1.00 6.36   ?  267  THR B O    1 
ATOM   5805  C  CB   . THR B 1 44  ? -7.708  20.592  8.912   1.00 7.04   ?  267  THR B CB   1 
ATOM   5806  O  OG1  . THR B 1 44  ? -8.186  19.250  8.979   1.00 7.35   ?  267  THR B OG1  1 
ATOM   5807  C  CG2  . THR B 1 44  ? -7.465  20.964  7.448   1.00 8.06   ?  267  THR B CG2  1 
ATOM   5808  H  H    . THR B 1 44  ? -5.549  19.445  8.475   1.00 7.77   ?  267  THR B H    1 
ATOM   5809  H  HA   . THR B 1 44  ? -6.195  21.641  9.782   1.00 7.54   ?  267  THR B HA   1 
ATOM   5810  H  HB   . THR B 1 44  ? -8.370  21.208  9.264   1.00 8.45   ?  267  THR B HB   1 
ATOM   5811  H  HG1  . THR B 1 44  ? -8.882  19.169  8.515   1.00 8.82   ?  267  THR B HG1  1 
ATOM   5812  H  HG21 . THR B 1 44  ? -8.305  20.973  6.963   1.00 9.67   ?  267  THR B HG21 1 
ATOM   5813  H  HG22 . THR B 1 44  ? -7.060  21.843  7.392   1.00 9.67   ?  267  THR B HG22 1 
ATOM   5814  H  HG23 . THR B 1 44  ? -6.871  20.317  7.036   1.00 9.67   ?  267  THR B HG23 1 
ATOM   5815  N  N    . ILE B 1 45  ? -7.322  21.029  11.989  1.00 6.57   ?  268  ILE B N    1 
ATOM   5816  C  CA   . ILE B 1 45  ? -7.504  20.644  13.384  1.00 7.10   ?  268  ILE B CA   1 
ATOM   5817  C  C    . ILE B 1 45  ? -8.476  19.487  13.522  1.00 7.30   ?  268  ILE B C    1 
ATOM   5818  O  O    . ILE B 1 45  ? -8.476  18.819  14.564  1.00 8.25   ?  268  ILE B O    1 
ATOM   5819  C  CB   . ILE B 1 45  ? -7.870  21.812  14.314  1.00 8.27   ?  268  ILE B CB   1 
ATOM   5820  C  CG1  . ILE B 1 45  ? -9.286  22.320  14.041  1.00 8.94   ?  268  ILE B CG1  1 
ATOM   5821  C  CG2  . ILE B 1 45  ? -6.828  22.889  14.179  1.00 8.82   ?  268  ILE B CG2  1 
ATOM   5822  C  CD1  . ILE B 1 45  ? -9.697  23.479  14.916  1.00 11.42  ?  268  ILE B CD1  1 
ATOM   5823  H  H    . ILE B 1 45  ? -7.643  21.797  11.772  1.00 7.89   ?  268  ILE B H    1 
ATOM   5824  H  HA   . ILE B 1 45  ? -6.632  20.351  13.694  1.00 8.52   ?  268  ILE B HA   1 
ATOM   5825  H  HB   . ILE B 1 45  ? -7.876  21.504  15.234  1.00 9.93   ?  268  ILE B HB   1 
ATOM   5826  H  HG12 . ILE B 1 45  ? -9.339  22.613  13.118  1.00 10.73  ?  268  ILE B HG12 1 
ATOM   5827  H  HG13 . ILE B 1 45  ? -9.913  21.596  14.196  1.00 10.73  ?  268  ILE B HG13 1 
ATOM   5828  H  HG21 . ILE B 1 45  ? -6.966  23.551  14.874  1.00 10.59  ?  268  ILE B HG21 1 
ATOM   5829  H  HG22 . ILE B 1 45  ? -5.948  22.491  14.272  1.00 10.59  ?  268  ILE B HG22 1 
ATOM   5830  H  HG23 . ILE B 1 45  ? -6.913  23.303  13.306  1.00 10.59  ?  268  ILE B HG23 1 
ATOM   5831  H  HD11 . ILE B 1 45  ? -10.631 23.683  14.752  1.00 13.71  ?  268  ILE B HD11 1 
ATOM   5832  H  HD12 . ILE B 1 45  ? -9.570  23.233  15.846  1.00 13.71  ?  268  ILE B HD12 1 
ATOM   5833  H  HD13 . ILE B 1 45  ? -9.147  24.248  14.700  1.00 13.71  ?  268  ILE B HD13 1 
ATOM   5834  N  N    . ASP B 1 46  ? -9.318  19.247  12.508  1.00 7.24   ?  269  ASP B N    1 
ATOM   5835  C  CA   . ASP B 1 46  ? -10.214 18.103  12.461  1.00 8.32   ?  269  ASP B CA   1 
ATOM   5836  C  C    . ASP B 1 46  ? -9.605  16.912  11.726  1.00 7.65   ?  269  ASP B C    1 
ATOM   5837  O  O    . ASP B 1 46  ? -10.314 15.929  11.479  1.00 9.88   ?  269  ASP B O    1 
ATOM   5838  C  CB   . ASP B 1 46  ? -11.607 18.492  11.936  1.00 10.15  ?  269  ASP B CB   1 
ATOM   5839  C  CG   . ASP B 1 46  ? -11.605 19.200  10.585  1.00 12.61  ?  269  ASP B CG   1 
ATOM   5840  O  OD1  . ASP B 1 46  ? -10.556 19.565  10.046  1.00 13.03  ?  269  ASP B OD1  1 
ATOM   5841  O  OD2  . ASP B 1 46  ? -12.715 19.425  10.053  1.00 15.50  -1 269  ASP B OD2  1 
ATOM   5842  H  H    . ASP B 1 46  ? -9.384  19.754  11.817  1.00 8.69   ?  269  ASP B H    1 
ATOM   5843  H  HA   . ASP B 1 46  ? -10.383 17.801  13.367  1.00 9.98   ?  269  ASP B HA   1 
ATOM   5844  H  HB2  . ASP B 1 46  ? -12.137 17.685  11.841  1.00 12.18  ?  269  ASP B HB2  1 
ATOM   5845  H  HB3  . ASP B 1 46  ? -12.023 19.088  12.577  1.00 12.18  ?  269  ASP B HB3  1 
ATOM   5846  N  N    . GLY B 1 47  ? -8.306  16.957  11.414  1.00 7.16   ?  270  GLY B N    1 
ATOM   5847  C  CA   . GLY B 1 47  ? -7.565  15.760  11.078  1.00 7.38   ?  270  GLY B CA   1 
ATOM   5848  C  C    . GLY B 1 47  ? -7.265  15.485  9.619   1.00 7.59   ?  270  GLY B C    1 
ATOM   5849  O  O    . GLY B 1 47  ? -6.845  14.363  9.305   1.00 8.42   ?  270  GLY B O    1 
ATOM   5850  H  H    . GLY B 1 47  ? -7.838  17.678  11.393  1.00 8.60   ?  270  GLY B H    1 
ATOM   5851  H  HA2  . GLY B 1 47  ? -6.711  15.801  11.536  1.00 8.86   ?  270  GLY B HA2  1 
ATOM   5852  H  HA3  . GLY B 1 47  ? -8.065  14.998  11.410  1.00 8.86   ?  270  GLY B HA3  1 
ATOM   5853  N  N    . GLU B 1 48  ? -7.428  16.459  8.731   1.00 6.84   ?  271  GLU B N    1 
ATOM   5854  C  CA   . GLU B 1 48  ? -7.132  16.259  7.320   1.00 7.38   ?  271  GLU B CA   1 
ATOM   5855  C  C    . GLU B 1 48  ? -5.682  16.643  7.017   1.00 6.30   ?  271  GLU B C    1 
ATOM   5856  O  O    . GLU B 1 48  ? -5.301  17.808  7.165   1.00 6.98   ?  271  GLU B O    1 
ATOM   5857  C  CB   . GLU B 1 48  ? -8.082  17.083  6.451   1.00 9.24   ?  271  GLU B CB   1 
ATOM   5858  C  CG   . GLU B 1 48  ? -7.933  16.812  4.958   1.00 14.72  ?  271  GLU B CG   1 
ATOM   5859  C  CD   . GLU B 1 48  ? -8.722  17.762  4.062   1.00 20.06  ?  271  GLU B CD   1 
ATOM   5860  O  OE1  . GLU B 1 48  ? -9.347  18.715  4.575   1.00 22.02  ?  271  GLU B OE1  1 
ATOM   5861  O  OE2  . GLU B 1 48  ? -8.702  17.550  2.826   1.00 22.13  -1 271  GLU B OE2  1 
ATOM   5862  H  H    . GLU B 1 48  ? -7.711  17.248  8.924   1.00 8.21   ?  271  GLU B H    1 
ATOM   5863  H  HA   . GLU B 1 48  ? -7.244  15.318  7.113   1.00 8.85   ?  271  GLU B HA   1 
ATOM   5864  H  HB2  . GLU B 1 48  ? -8.995  16.874  6.701   1.00 11.09  ?  271  GLU B HB2  1 
ATOM   5865  H  HB3  . GLU B 1 48  ? -7.904  18.025  6.600   1.00 11.09  ?  271  GLU B HB3  1 
ATOM   5866  H  HG2  . GLU B 1 48  ? -6.997  16.895  4.720   1.00 17.66  ?  271  GLU B HG2  1 
ATOM   5867  H  HG3  . GLU B 1 48  ? -8.244  15.911  4.775   1.00 17.66  ?  271  GLU B HG3  1 
ATOM   5868  N  N    . LEU B 1 49  ? -4.895  15.667  6.562   1.00 6.91   ?  272  LEU B N    1 
ATOM   5869  C  CA   . LEU B 1 49  ? -3.526  15.939  6.139   1.00 7.09   ?  272  LEU B CA   1 
ATOM   5870  C  C    . LEU B 1 49  ? -3.533  16.685  4.816   1.00 6.88   ?  272  LEU B C    1 
ATOM   5871  O  O    . LEU B 1 49  ? -4.314  16.363  3.922   1.00 8.16   ?  272  LEU B O    1 
ATOM   5872  C  CB   . LEU B 1 49  ? -2.767  14.633  5.930   1.00 8.10   ?  272  LEU B CB   1 
ATOM   5873  C  CG   . LEU B 1 49  ? -2.674  13.692  7.124   1.00 8.18   ?  272  LEU B CG   1 
ATOM   5874  C  CD1  . LEU B 1 49  ? -1.961  12.393  6.721   1.00 10.21  ?  272  LEU B CD1  1 
ATOM   5875  C  CD2  . LEU B 1 49  ? -1.990  14.347  8.305   1.00 9.27   ?  272  LEU B CD2  1 
ATOM   5876  H  H    . LEU B 1 49  ? -5.130  14.843  6.490   1.00 8.30   ?  272  LEU B H    1 
ATOM   5877  H  HA   . LEU B 1 49  ? -3.083  16.468  6.822   1.00 8.51   ?  272  LEU B HA   1 
ATOM   5878  H  HB2  . LEU B 1 49  ? -3.206  14.143  5.217   1.00 9.73   ?  272  LEU B HB2  1 
ATOM   5879  H  HB3  . LEU B 1 49  ? -1.858  14.853  5.672   1.00 9.73   ?  272  LEU B HB3  1 
ATOM   5880  H  HG   . LEU B 1 49  ? -3.573  13.469  7.413   1.00 9.82   ?  272  LEU B HG   1 
ATOM   5881  H  HD11 . LEU B 1 49  ? -1.921  11.803  7.491   1.00 12.25  ?  272  LEU B HD11 1 
ATOM   5882  H  HD12 . LEU B 1 49  ? -2.459  11.969  6.005   1.00 12.25  ?  272  LEU B HD12 1 
ATOM   5883  H  HD13 . LEU B 1 49  ? -1.064  12.606  6.420   1.00 12.25  ?  272  LEU B HD13 1 
ATOM   5884  H  HD21 . LEU B 1 49  ? -1.920  13.704  9.027   1.00 11.12  ?  272  LEU B HD21 1 
ATOM   5885  H  HD22 . LEU B 1 49  ? -1.105  14.639  8.035   1.00 11.12  ?  272  LEU B HD22 1 
ATOM   5886  H  HD23 . LEU B 1 49  ? -2.516  15.110  8.591   1.00 11.12  ?  272  LEU B HD23 1 
ATOM   5887  N  N    . LEU B 1 50  ? -2.640  17.667  4.681   1.00 6.47   ?  273  LEU B N    1 
ATOM   5888  C  CA   . LEU B 1 50  ? -2.551  18.482  3.477   1.00 6.62   ?  273  LEU B CA   1 
ATOM   5889  C  C    . LEU B 1 50  ? -1.125  18.475  2.926   1.00 7.17   ?  273  LEU B C    1 
ATOM   5890  O  O    . LEU B 1 50  ? -0.166  18.112  3.606   1.00 6.97   ?  273  LEU B O    1 
ATOM   5891  C  CB   . LEU B 1 50  ? -2.967  19.935  3.752   1.00 8.02   ?  273  LEU B CB   1 
ATOM   5892  C  CG   . LEU B 1 50  ? -4.286  20.138  4.483   1.00 10.16  ?  273  LEU B CG   1 
ATOM   5893  C  CD1  . LEU B 1 50  ? -4.455  21.598  4.874   1.00 10.96  ?  273  LEU B CD1  1 
ATOM   5894  C  CD2  . LEU B 1 50  ? -5.450  19.674  3.629   1.00 12.42  ?  273  LEU B CD2  1 
ATOM   5895  H  H    . LEU B 1 50  ? -2.067  17.881  5.286   1.00 7.77   ?  273  LEU B H    1 
ATOM   5896  H  HA   . LEU B 1 50  ? -3.139  18.094  2.810   1.00 7.95   ?  273  LEU B HA   1 
ATOM   5897  H  HB2  . LEU B 1 50  ? -2.276  20.348  4.293   1.00 9.63   ?  273  LEU B HB2  1 
ATOM   5898  H  HB3  . LEU B 1 50  ? -3.040  20.393  2.901   1.00 9.63   ?  273  LEU B HB3  1 
ATOM   5899  H  HG   . LEU B 1 50  ? -4.283  19.605  5.294   1.00 12.20  ?  273  LEU B HG   1 
ATOM   5900  H  HD11 . LEU B 1 50  ? -5.306  21.706  5.328   1.00 13.15  ?  273  LEU B HD11 1 
ATOM   5901  H  HD12 . LEU B 1 50  ? -3.730  21.852  5.466   1.00 13.15  ?  273  LEU B HD12 1 
ATOM   5902  H  HD13 . LEU B 1 50  ? -4.436  22.144  4.073   1.00 13.15  ?  273  LEU B HD13 1 
ATOM   5903  H  HD21 . LEU B 1 50  ? -6.278  19.851  4.102   1.00 14.90  ?  273  LEU B HD21 1 
ATOM   5904  H  HD22 . LEU B 1 50  ? -5.438  20.160  2.789   1.00 14.90  ?  273  LEU B HD22 1 
ATOM   5905  H  HD23 . LEU B 1 50  ? -5.360  18.723  3.463   1.00 14.90  ?  273  LEU B HD23 1 
ATOM   5906  N  N    . GLY B 1 51  ? -0.979  18.926  1.685   1.00 6.61   ?  274  GLY B N    1 
ATOM   5907  C  CA   . GLY B 1 51  ? 0.350   19.069  1.112   1.00 7.11   ?  274  GLY B CA   1 
ATOM   5908  C  C    . GLY B 1 51  ? 1.070   17.748  1.000   1.00 6.45   ?  274  GLY B C    1 
ATOM   5909  O  O    . GLY B 1 51  ? 0.523   16.749  0.513   1.00 7.40   ?  274  GLY B O    1 
ATOM   5910  H  H    . GLY B 1 51  ? -1.623  19.153  1.162   1.00 7.94   ?  274  GLY B H    1 
ATOM   5911  H  HA2  . GLY B 1 51  ? 0.278   19.455  0.225   1.00 8.53   ?  274  GLY B HA2  1 
ATOM   5912  H  HA3  . GLY B 1 51  ? 0.879   19.660  1.671   1.00 8.53   ?  274  GLY B HA3  1 
ATOM   5913  N  N    . THR B 1 52  ? 2.334   17.739  1.419   1.00 5.72   ?  275  THR B N    1 
ATOM   5914  C  CA   . THR B 1 52  ? 3.146   16.528  1.467   1.00 5.77   ?  275  THR B CA   1 
ATOM   5915  C  C    . THR B 1 52  ? 3.201   15.934  2.881   1.00 5.88   ?  275  THR B C    1 
ATOM   5916  O  O    . THR B 1 52  ? 4.103   15.157  3.194   1.00 6.15   ?  275  THR B O    1 
ATOM   5917  C  CB   . THR B 1 52  ? 4.560   16.815  0.956   1.00 6.23   ?  275  THR B CB   1 
ATOM   5918  O  OG1  . THR B 1 52  ? 5.155   17.867  1.727   1.00 5.89   ?  275  THR B OG1  1 
ATOM   5919  C  CG2  . THR B 1 52  ? 4.568   17.211  -0.503  1.00 7.16   ?  275  THR B CG2  1 
ATOM   5920  H  H    . THR B 1 52  ? 2.753   18.440  1.687   1.00 6.87   ?  275  THR B H    1 
ATOM   5921  H  HA   . THR B 1 52  ? 2.750   15.867  0.878   1.00 6.93   ?  275  THR B HA   1 
ATOM   5922  H  HB   . THR B 1 52  ? 5.082   16.002  1.044   1.00 7.47   ?  275  THR B HB   1 
ATOM   5923  H  HG1  . THR B 1 52  ? 5.242   17.624  2.526   1.00 7.07   ?  275  THR B HG1  1 
ATOM   5924  H  HG21 . THR B 1 52  ? 5.479   17.362  -0.800  1.00 8.59   ?  275  THR B HG21 1 
ATOM   5925  H  HG22 . THR B 1 52  ? 4.174   16.507  -1.040  1.00 8.59   ?  275  THR B HG22 1 
ATOM   5926  H  HG23 . THR B 1 52  ? 4.057   18.026  -0.628  1.00 8.59   ?  275  THR B HG23 1 
ATOM   5927  N  N    . THR B 1 53  ? 2.259   16.298  3.746   1.00 5.80   ?  276  THR B N    1 
ATOM   5928  C  CA   . THR B 1 53  ? 2.347   15.899  5.148   1.00 5.89   ?  276  THR B CA   1 
ATOM   5929  C  C    . THR B 1 53  ? 2.024   14.420  5.365   1.00 6.54   ?  276  THR B C    1 
ATOM   5930  O  O    . THR B 1 53  ? 0.999   13.910  4.896   1.00 7.26   ?  276  THR B O    1 
ATOM   5931  C  CB   . THR B 1 53  ? 1.441   16.797  5.989   1.00 6.10   ?  276  THR B CB   1 
ATOM   5932  O  OG1  . THR B 1 53  ? 1.911   18.138  5.883   1.00 5.97   ?  276  THR B OG1  1 
ATOM   5933  C  CG2  . THR B 1 53  ? 1.459   16.406  7.442   1.00 6.43   ?  276  THR B CG2  1 
ATOM   5934  H  H    . THR B 1 53  ? 1.567   16.769  3.550   1.00 6.96   ?  276  THR B H    1 
ATOM   5935  H  HA   . THR B 1 53  ? 3.264   16.009  5.445   1.00 7.07   ?  276  THR B HA   1 
ATOM   5936  H  HB   . THR B 1 53  ? 0.529   16.715  5.669   1.00 7.32   ?  276  THR B HB   1 
ATOM   5937  H  HG1  . THR B 1 53  ? 1.887   18.388  5.081   1.00 7.17   ?  276  THR B HG1  1 
ATOM   5938  H  HG21 . THR B 1 53  ? 0.985   17.068  7.970   1.00 7.72   ?  276  THR B HG21 1 
ATOM   5939  H  HG22 . THR B 1 53  ? 1.029   15.544  7.559   1.00 7.72   ?  276  THR B HG22 1 
ATOM   5940  H  HG23 . THR B 1 53  ? 2.374   16.347  7.758   1.00 7.72   ?  276  THR B HG23 1 
ATOM   5941  N  N    . GLN B 1 54  ? 2.912   13.738  6.074   1.00 6.18   ?  277  GLN B N    1 
ATOM   5942  C  CA   . GLN B 1 54  ? 2.724   12.362  6.534   1.00 6.57   ?  277  GLN B CA   1 
ATOM   5943  C  C    . GLN B 1 54  ? 2.966   12.319  8.041   1.00 6.63   ?  277  GLN B C    1 
ATOM   5944  O  O    . GLN B 1 54  ? 3.192   13.356  8.666   1.00 7.53   ?  277  GLN B O    1 
ATOM   5945  C  CB   . GLN B 1 54  ? 3.546   11.362  5.705   1.00 6.89   ?  277  GLN B CB   1 
ATOM   5946  C  CG   . GLN B 1 54  ? 5.008   11.712  5.565   1.00 7.30   ?  277  GLN B CG   1 
ATOM   5947  C  CD   . GLN B 1 54  ? 5.766   11.424  6.852   1.00 7.36   ?  277  GLN B CD   1 
ATOM   5948  O  OE1  . GLN B 1 54  ? 5.760   10.301  7.348   1.00 8.00   ?  277  GLN B OE1  1 
ATOM   5949  N  NE2  . GLN B 1 54  ? 6.419   12.440  7.402   1.00 7.73   ?  277  GLN B NE2  1 
ATOM   5950  H  H    . GLN B 1 54  ? 3.671   14.064  6.314   1.00 7.41   ?  277  GLN B H    1 
ATOM   5951  H  HA   . GLN B 1 54  ? 1.805   12.080  6.407   1.00 7.88   ?  277  GLN B HA   1 
ATOM   5952  H  HB2  . GLN B 1 54  ? 3.493   10.492  6.131   1.00 8.27   ?  277  GLN B HB2  1 
ATOM   5953  H  HB3  . GLN B 1 54  ? 3.169   11.318  4.813   1.00 8.27   ?  277  GLN B HB3  1 
ATOM   5954  H  HG2  . GLN B 1 54  ? 5.400   11.182  4.853   1.00 8.76   ?  277  GLN B HG2  1 
ATOM   5955  H  HG3  . GLN B 1 54  ? 5.096   12.657  5.363   1.00 8.76   ?  277  GLN B HG3  1 
ATOM   5956  H  HE21 . GLN B 1 54  ? 6.400   13.215  7.030   1.00 9.27   ?  277  GLN B HE21 1 
ATOM   5957  H  HE22 . GLN B 1 54  ? 6.861   12.324  8.130   1.00 9.27   ?  277  GLN B HE22 1 
ATOM   5958  N  N    . LEU B 1 55  ? 2.893   11.120  8.630   1.00 6.50   ?  278  LEU B N    1 
ATOM   5959  C  CA   . LEU B 1 55  ? 2.762   11.001  10.084  1.00 7.30   ?  278  LEU B CA   1 
ATOM   5960  C  C    . LEU B 1 55  ? 4.070   10.806  10.839  1.00 8.51   ?  278  LEU B C    1 
ATOM   5961  O  O    . LEU B 1 55  ? 4.098   11.079  12.041  1.00 9.25   ?  278  LEU B O    1 
ATOM   5962  C  CB   . LEU B 1 55  ? 1.852   9.822   10.448  1.00 8.49   ?  278  LEU B CB   1 
ATOM   5963  C  CG   . LEU B 1 55  ? 0.388   10.139  10.639  1.00 10.43  ?  278  LEU B CG   1 
ATOM   5964  C  CD1  . LEU B 1 55  ? 0.178   11.013  11.838  1.00 12.12  ?  278  LEU B CD1  1 
ATOM   5965  C  CD2  . LEU B 1 55  ? -0.141  10.760  9.433   1.00 10.12  ?  278  LEU B CD2  1 
ATOM   5966  H  H    . LEU B 1 55  ? 2.917   10.369  8.213   1.00 7.80   ?  278  LEU B H    1 
ATOM   5967  H  HA   . LEU B 1 55  ? 2.364   11.832  10.387  1.00 8.76   ?  278  LEU B HA   1 
ATOM   5968  H  HB2  . LEU B 1 55  ? 1.911   9.165   9.736   1.00 10.20  ?  278  LEU B HB2  1 
ATOM   5969  H  HB3  . LEU B 1 55  ? 2.172   9.440   11.280  1.00 10.20  ?  278  LEU B HB3  1 
ATOM   5970  H  HG   . LEU B 1 55  ? -0.101  9.317   10.800  1.00 12.52  ?  278  LEU B HG   1 
ATOM   5971  H  HD11 . LEU B 1 55  ? -0.770  11.055  12.036  1.00 14.54  ?  278  LEU B HD11 1 
ATOM   5972  H  HD12 . LEU B 1 55  ? 0.657   10.636  12.592  1.00 14.54  ?  278  LEU B HD12 1 
ATOM   5973  H  HD13 . LEU B 1 55  ? 0.515   11.902  11.643  1.00 14.54  ?  278  LEU B HD13 1 
ATOM   5974  H  HD21 . LEU B 1 55  ? -1.107  10.817  9.505   1.00 12.15  ?  278  LEU B HD21 1 
ATOM   5975  H  HD22 . LEU B 1 55  ? 0.236   11.649  9.344   1.00 12.15  ?  278  LEU B HD22 1 
ATOM   5976  H  HD23 . LEU B 1 55  ? 0.102   10.219  8.666   1.00 12.15  ?  278  LEU B HD23 1 
ATOM   5977  N  N    A ILE B 1 56  ? 5.123   10.299  10.201  0.96 8.77   ?  279  ILE B N    1 
ATOM   5978  C  CA   A ILE B 1 56  ? 6.328   9.856   10.902  0.96 8.95   ?  279  ILE B CA   1 
ATOM   5979  C  C    A ILE B 1 56  ? 7.366   10.972  10.886  0.96 8.00   ?  279  ILE B C    1 
ATOM   5980  O  O    A ILE B 1 56  ? 7.782   11.419  9.812   0.96 7.52   ?  279  ILE B O    1 
ATOM   5981  C  CB   A ILE B 1 56  ? 6.895   8.575   10.258  0.96 11.35  ?  279  ILE B CB   1 
ATOM   5982  C  CG1  A ILE B 1 56  ? 5.890   7.423   10.334  0.96 13.07  ?  279  ILE B CG1  1 
ATOM   5983  C  CG2  A ILE B 1 56  ? 8.196   8.194   10.934  0.96 13.73  ?  279  ILE B CG2  1 
ATOM   5984  C  CD1  A ILE B 1 56  ? 6.402   6.131   9.742   0.96 13.98  ?  279  ILE B CD1  1 
ATOM   5985  H  H    A ILE B 1 56  ? 5.164   10.200  9.347   0.96 10.53  ?  279  ILE B H    1 
ATOM   5986  H  HA   A ILE B 1 56  ? 6.102   9.682   11.829  0.96 10.74  ?  279  ILE B HA   1 
ATOM   5987  H  HB   A ILE B 1 56  ? 7.064   8.756   9.320   0.96 13.63  ?  279  ILE B HB   1 
ATOM   5988  H  HG12 A ILE B 1 56  ? 5.675   7.257   11.266  0.96 15.68  ?  279  ILE B HG12 1 
ATOM   5989  H  HG13 A ILE B 1 56  ? 5.089   7.674   9.849   0.96 15.68  ?  279  ILE B HG13 1 
ATOM   5990  H  HG21 A ILE B 1 56  ? 8.852   8.890   10.771  0.96 16.48  ?  279  ILE B HG21 1 
ATOM   5991  H  HG22 A ILE B 1 56  ? 8.041   8.101   11.887  0.96 16.48  ?  279  ILE B HG22 1 
ATOM   5992  H  HG23 A ILE B 1 56  ? 8.508   7.353   10.565  0.96 16.48  ?  279  ILE B HG23 1 
ATOM   5993  H  HD11 A ILE B 1 56  ? 7.031   5.727   10.361  0.96 16.78  ?  279  ILE B HD11 1 
ATOM   5994  H  HD12 A ILE B 1 56  ? 5.652   5.532   9.595   0.96 16.78  ?  279  ILE B HD12 1 
ATOM   5995  H  HD13 A ILE B 1 56  ? 6.843   6.322   8.900   0.96 16.78  ?  279  ILE B HD13 1 
ATOM   5996  N  N    . THR B 1 57  ? 7.823   11.394  12.069  1.00 9.04   ?  280  THR B N    1 
ATOM   5997  C  CA   A THR B 1 57  ? 8.862   12.412  12.155  0.39 9.68   ?  280  THR B CA   1 
ATOM   5998  C  CA   B THR B 1 57  ? 8.846   12.431  12.098  0.61 9.60   ?  280  THR B CA   1 
ATOM   5999  C  C    . THR B 1 57  ? 10.051  12.049  11.285  1.00 7.89   ?  280  THR B C    1 
ATOM   6000  O  O    . THR B 1 57  ? 10.556  12.872  10.521  1.00 9.51   ?  280  THR B O    1 
ATOM   6001  C  CB   A THR B 1 57  ? 9.296   12.527  13.621  0.39 16.22  ?  280  THR B CB   1 
ATOM   6002  C  CB   B THR B 1 57  ? 9.321   12.764  13.527  0.61 9.16   ?  280  THR B CB   1 
ATOM   6003  O  OG1  A THR B 1 57  ? 9.477   11.211  14.179  0.39 12.84  ?  280  THR B OG1  1 
ATOM   6004  O  OG1  B THR B 1 57  ? 8.276   13.461  14.210  0.61 11.42  ?  280  THR B OG1  1 
ATOM   6005  C  CG2  A THR B 1 57  ? 8.250   13.282  14.420  0.39 21.37  ?  280  THR B CG2  1 
ATOM   6006  C  CG2  B THR B 1 57  ? 10.576  13.618  13.488  0.61 13.85  ?  280  THR B CG2  1 
ATOM   6007  H  H    . THR B 1 57  ? 7.554   11.114  12.835  1.00 10.85  ?  280  THR B H    1 
ATOM   6008  H  HA   A THR B 1 57  ? 8.516   13.265  11.849  0.39 11.62  ?  280  THR B HA   1 
ATOM   6009  H  HA   B THR B 1 57  ? 8.452   13.231  11.717  0.61 11.52  ?  280  THR B HA   1 
ATOM   6010  H  HB   A THR B 1 57  ? 10.133  13.013  13.677  0.39 19.46  ?  280  THR B HB   1 
ATOM   6011  H  HB   B THR B 1 57  ? 9.536   11.949  14.007  0.61 10.99  ?  280  THR B HB   1 
ATOM   6012  H  HG1  A THR B 1 57  ? 10.185  10.869  13.885  0.39 15.41  ?  280  THR B HG1  1 
ATOM   6013  H  HG1  B THR B 1 57  ? 8.521   13.655  14.990  0.61 13.70  ?  280  THR B HG1  1 
ATOM   6014  H  HG21 A THR B 1 57  ? 8.490   13.286  15.359  0.39 25.64  ?  280  THR B HG21 1 
ATOM   6015  H  HG21 B THR B 1 57  ? 10.854  13.842  14.390  0.61 16.62  ?  280  THR B HG21 1 
ATOM   6016  H  HG22 A THR B 1 57  ? 8.190   14.198  14.106  0.39 25.64  ?  280  THR B HG22 1 
ATOM   6017  H  HG22 B THR B 1 57  ? 11.293  13.135  13.048  0.61 16.62  ?  280  THR B HG22 1 
ATOM   6018  H  HG23 A THR B 1 57  ? 7.384   12.857  14.318  0.39 25.64  ?  280  THR B HG23 1 
ATOM   6019  H  HG23 B THR B 1 57  ? 10.404  14.438  12.999  0.61 16.62  ?  280  THR B HG23 1 
ATOM   6020  N  N    . SER B 1 58  ? 10.526  10.811  11.420  1.00 9.43   ?  281  SER B N    1 
ATOM   6021  C  CA   A SER B 1 58  ? 11.769  10.405  10.784  0.47 16.97  ?  281  SER B CA   1 
ATOM   6022  C  CA   B SER B 1 58  ? 11.773  10.419  10.777  0.53 6.43   ?  281  SER B CA   1 
ATOM   6023  C  C    . SER B 1 58  ? 11.656  10.329  9.266   1.00 11.99  ?  281  SER B C    1 
ATOM   6024  O  O    . SER B 1 58  ? 12.681  10.183  8.595   1.00 16.73  ?  281  SER B O    1 
ATOM   6025  C  CB   A SER B 1 58  ? 12.225  9.061   11.368  0.47 42.06  ?  281  SER B CB   1 
ATOM   6026  C  CB   B SER B 1 58  ? 12.288  9.102   11.354  0.53 4.80   ?  281  SER B CB   1 
ATOM   6027  O  OG   A SER B 1 58  ? 12.223  9.069   12.799  0.47 10.60  ?  281  SER B OG   1 
ATOM   6028  O  OG   B SER B 1 58  ? 11.359  8.057   11.184  0.53 14.46  ?  281  SER B OG   1 
ATOM   6029  H  H    . SER B 1 58  ? 10.148  10.187  11.875  1.00 11.32  ?  281  SER B H    1 
ATOM   6030  H  HA   . SER B 1 58  ? 12.460  11.057  10.979  0.62 7.72   ?  281  SER B HA   1 
ATOM   6031  H  HB2  A SER B 1 58  ? 11.621  8.367   11.060  0.47 50.48  ?  281  SER B HB2  1 
ATOM   6032  H  HB2  B SER B 1 58  ? 13.112  8.864   10.901  0.53 5.76   ?  281  SER B HB2  1 
ATOM   6033  H  HB3  A SER B 1 58  ? 13.126  8.877   11.059  0.47 50.48  ?  281  SER B HB3  1 
ATOM   6034  H  HB3  B SER B 1 58  ? 12.454  9.221   12.302  0.53 5.76   ?  281  SER B HB3  1 
ATOM   6035  H  HG   A SER B 1 58  ? 12.746  9.661   13.084  0.47 12.72  ?  281  SER B HG   1 
ATOM   6036  H  HG   B SER B 1 58  ? 11.663  7.346   11.514  0.53 17.36  ?  281  SER B HG   1 
ATOM   6037  N  N    . ASN B 1 59  ? 10.459  10.423  8.703   1.00 8.69   ?  282  ASN B N    1 
ATOM   6038  C  CA   . ASN B 1 59  ? 10.317  10.453  7.252   1.00 7.70   ?  282  ASN B CA   1 
ATOM   6039  C  C    . ASN B 1 59  ? 10.263  11.870  6.675   1.00 6.78   ?  282  ASN B C    1 
ATOM   6040  O  O    . ASN B 1 59  ? 10.232  12.031  5.452   1.00 7.30   ?  282  ASN B O    1 
ATOM   6041  C  CB   . ASN B 1 59  ? 9.108   9.634   6.814   1.00 9.09   ?  282  ASN B CB   1 
ATOM   6042  C  CG   . ASN B 1 59  ? 9.413   8.154   6.762   1.00 11.04  ?  282  ASN B CG   1 
ATOM   6043  O  OD1  . ASN B 1 59  ? 10.555  7.733   6.986   1.00 12.05  ?  282  ASN B OD1  1 
ATOM   6044  N  ND2  . ASN B 1 59  ? 8.409   7.359   6.468   1.00 11.41  ?  282  ASN B ND2  1 
ATOM   6045  H  H    . ASN B 1 59  ? 9.717   10.471  9.136   1.00 10.42  ?  282  ASN B H    1 
ATOM   6046  H  HA   . ASN B 1 59  ? 11.095  10.027  6.859   1.00 9.24   ?  282  ASN B HA   1 
ATOM   6047  H  HB2  . ASN B 1 59  ? 8.384   9.772   7.445   1.00 10.91  ?  282  ASN B HB2  1 
ATOM   6048  H  HB3  . ASN B 1 59  ? 8.834   9.918   5.928   1.00 10.91  ?  282  ASN B HB3  1 
ATOM   6049  H  HD21 . ASN B 1 59  ? 8.532   6.508   6.427   1.00 13.70  ?  282  ASN B HD21 1 
ATOM   6050  H  HD22 . ASN B 1 59  ? 7.629   7.688   6.318   1.00 13.70  ?  282  ASN B HD22 1 
ATOM   6051  N  N    . ILE B 1 60  ? 10.282  12.897  7.516   1.00 5.91   ?  283  ILE B N    1 
ATOM   6052  C  CA   . ILE B 1 60  ? 10.270  14.263  7.017   1.00 5.42   ?  283  ILE B CA   1 
ATOM   6053  C  C    . ILE B 1 60  ? 11.626  14.566  6.393   1.00 5.53   ?  283  ILE B C    1 
ATOM   6054  O  O    . ILE B 1 60  ? 12.663  14.379  7.026   1.00 6.08   ?  283  ILE B O    1 
ATOM   6055  C  CB   . ILE B 1 60  ? 9.977   15.234  8.163   1.00 5.74   ?  283  ILE B CB   1 
ATOM   6056  C  CG1  . ILE B 1 60  ? 8.629   14.942  8.827   1.00 6.63   ?  283  ILE B CG1  1 
ATOM   6057  C  CG2  . ILE B 1 60  ? 10.031  16.661  7.642   1.00 6.52   ?  283  ILE B CG2  1 
ATOM   6058  C  CD1  . ILE B 1 60  ? 8.451   15.678  10.156  1.00 7.95   ?  283  ILE B CD1  1 
ATOM   6059  H  H    . ILE B 1 60  ? 10.301  12.829  8.373   1.00 7.10   ?  283  ILE B H    1 
ATOM   6060  H  HA   . ILE B 1 60  ? 9.581   14.357  6.341   1.00 6.50   ?  283  ILE B HA   1 
ATOM   6061  H  HB   . ILE B 1 60  ? 10.656  15.113  8.844   1.00 6.89   ?  283  ILE B HB   1 
ATOM   6062  H  HG12 . ILE B 1 60  ? 7.916   15.222  8.232   1.00 7.96   ?  283  ILE B HG12 1 
ATOM   6063  H  HG13 . ILE B 1 60  ? 8.562   13.990  9.000   1.00 7.96   ?  283  ILE B HG13 1 
ATOM   6064  H  HG21 . ILE B 1 60  ? 9.662   17.256  8.313   1.00 7.83   ?  283  ILE B HG21 1 
ATOM   6065  H  HG22 . ILE B 1 60  ? 10.954  16.897  7.462   1.00 7.83   ?  283  ILE B HG22 1 
ATOM   6066  H  HG23 . ILE B 1 60  ? 9.509   16.719  6.825   1.00 7.83   ?  283  ILE B HG23 1 
ATOM   6067  H  HD11 . ILE B 1 60  ? 7.653   15.347  10.596  1.00 9.54   ?  283  ILE B HD11 1 
ATOM   6068  H  HD12 . ILE B 1 60  ? 9.228   15.514  10.714  1.00 9.54   ?  283  ILE B HD12 1 
ATOM   6069  H  HD13 . ILE B 1 60  ? 8.363   16.628  9.982   1.00 9.54   ?  283  ILE B HD13 1 
ATOM   6070  N  N    . CYS B 1 61  ? 11.625  15.033  5.147   1.00 5.41   ?  284  CYS B N    1 
ATOM   6071  C  CA   . CYS B 1 61  ? 12.844  15.323  4.394   1.00 5.79   ?  284  CYS B CA   1 
ATOM   6072  C  C    . CYS B 1 61  ? 13.667  14.065  4.111   1.00 6.02   ?  284  CYS B C    1 
ATOM   6073  O  O    . CYS B 1 61  ? 14.873  14.150  3.862   1.00 7.06   ?  284  CYS B O    1 
ATOM   6074  C  CB   . CYS B 1 61  ? 13.689  16.436  5.013   1.00 6.62   ?  284  CYS B CB   1 
ATOM   6075  S  SG   . CYS B 1 61  ? 12.986  18.083  4.801   1.00 6.96   ?  284  CYS B SG   1 
ATOM   6076  H  H    . CYS B 1 61  ? 10.907  15.195  4.701   1.00 6.50   ?  284  CYS B H    1 
ATOM   6077  H  HA   . CYS B 1 61  ? 12.569  15.672  3.532   1.00 6.94   ?  284  CYS B HA   1 
ATOM   6078  H  HB2  . CYS B 1 61  ? 13.774  16.270  5.965   1.00 7.95   ?  284  CYS B HB2  1 
ATOM   6079  H  HB3  . CYS B 1 61  ? 14.565  16.431  4.596   1.00 7.95   ?  284  CYS B HB3  1 
ATOM   6080  H  HG   . CYS B 1 61  ? 13.725  18.890  5.294   1.00 8.35   ?  284  CYS B HG   1 
ATOM   6081  N  N    . SER B 1 62  ? 13.032  12.904  4.166   1.00 5.97   ?  285  SER B N    1 
ATOM   6082  C  CA   A SER B 1 62  ? 13.647  11.642  3.786   0.73 6.36   ?  285  SER B CA   1 
ATOM   6083  C  CA   B SER B 1 62  ? 13.652  11.649  3.779   0.27 6.84   ?  285  SER B CA   1 
ATOM   6084  C  C    . SER B 1 62  ? 13.133  11.223  2.412   1.00 7.08   ?  285  SER B C    1 
ATOM   6085  O  O    . SER B 1 62  ? 12.029  11.577  2.014   1.00 9.09   ?  285  SER B O    1 
ATOM   6086  C  CB   A SER B 1 62  ? 13.314  10.561  4.822   0.73 7.55   ?  285  SER B CB   1 
ATOM   6087  C  CB   B SER B 1 62  ? 13.302  10.556  4.783   0.27 8.01   ?  285  SER B CB   1 
ATOM   6088  O  OG   A SER B 1 62  ? 13.956  9.324   4.543   0.73 7.35   ?  285  SER B OG   1 
ATOM   6089  O  OG   B SER B 1 62  ? 11.988  10.099  4.536   0.27 8.74   ?  285  SER B OG   1 
ATOM   6090  H  H    A SER B 1 62  ? 12.218  12.818  4.428   0.73 7.17   ?  285  SER B H    1 
ATOM   6091  H  H    B SER B 1 62  ? 12.219  12.815  4.431   0.27 7.17   ?  285  SER B H    1 
ATOM   6092  H  HA   A SER B 1 62  ? 14.612  11.733  3.741   0.73 7.63   ?  285  SER B HA   1 
ATOM   6093  H  HA   B SER B 1 62  ? 14.616  11.758  3.743   0.27 8.21   ?  285  SER B HA   1 
ATOM   6094  H  HB2  A SER B 1 62  ? 13.604  10.869  5.695   0.73 9.07   ?  285  SER B HB2  1 
ATOM   6095  H  HB2  B SER B 1 62  ? 13.923  9.818   4.685   0.27 9.62   ?  285  SER B HB2  1 
ATOM   6096  H  HB3  A SER B 1 62  ? 12.355  10.418  4.822   0.73 9.07   ?  285  SER B HB3  1 
ATOM   6097  H  HB3  B SER B 1 62  ? 13.354  10.916  5.682   0.27 9.62   ?  285  SER B HB3  1 
ATOM   6098  H  HG   A SER B 1 62  ? 14.789  9.429   4.528   0.73 8.82   ?  285  SER B HG   1 
ATOM   6099  H  HG   B SER B 1 62  ? 11.447  10.740  4.585   0.27 10.49  ?  285  SER B HG   1 
ATOM   6100  N  N    . PHE B 1 63  ? 13.955  10.459  1.695   1.00 5.98   ?  286  PHE B N    1 
ATOM   6101  C  CA   . PHE B 1 63  ? 13.567  9.834   0.446   1.00 6.43   ?  286  PHE B CA   1 
ATOM   6102  C  C    . PHE B 1 63  ? 13.990  8.375   0.495   1.00 6.52   ?  286  PHE B C    1 
ATOM   6103  O  O    . PHE B 1 63  ? 14.994  8.034   1.133   1.00 6.75   ?  286  PHE B O    1 
ATOM   6104  C  CB   . PHE B 1 63  ? 14.300  10.438  -0.748  1.00 7.64   ?  286  PHE B CB   1 
ATOM   6105  C  CG   . PHE B 1 63  ? 13.910  11.857  -1.064  1.00 7.67   ?  286  PHE B CG   1 
ATOM   6106  C  CD1  . PHE B 1 63  ? 12.662  12.156  -1.596  1.00 8.42   ?  286  PHE B CD1  1 
ATOM   6107  C  CD2  . PHE B 1 63  ? 14.806  12.886  -0.884  1.00 8.57   ?  286  PHE B CD2  1 
ATOM   6108  C  CE1  . PHE B 1 63  ? 12.319  13.437  -1.931  1.00 9.17   ?  286  PHE B CE1  1 
ATOM   6109  C  CE2  . PHE B 1 63  ? 14.473  14.185  -1.230  1.00 8.69   ?  286  PHE B CE2  1 
ATOM   6110  C  CZ   . PHE B 1 63  ? 13.232  14.452  -1.763  1.00 8.83   ?  286  PHE B CZ   1 
ATOM   6111  H  H    . PHE B 1 63  ? 14.767  10.287  1.923   1.00 7.18   ?  286  PHE B H    1 
ATOM   6112  H  HA   . PHE B 1 63  ? 12.609  9.933   0.332   1.00 7.72   ?  286  PHE B HA   1 
ATOM   6113  H  HB2  . PHE B 1 63  ? 15.252  10.430  -0.562  1.00 9.17   ?  286  PHE B HB2  1 
ATOM   6114  H  HB3  . PHE B 1 63  ? 14.110  9.900   -1.532  1.00 9.17   ?  286  PHE B HB3  1 
ATOM   6115  H  HD1  . PHE B 1 63  ? 12.047  11.471  -1.728  1.00 10.11  ?  286  PHE B HD1  1 
ATOM   6116  H  HD2  . PHE B 1 63  ? 15.645  12.707  -0.525  1.00 10.28  ?  286  PHE B HD2  1 
ATOM   6117  H  HE1  . PHE B 1 63  ? 11.473  13.621  -2.271  1.00 11.00  ?  286  PHE B HE1  1 
ATOM   6118  H  HE2  . PHE B 1 63  ? 15.085  14.874  -1.103  1.00 10.43  ?  286  PHE B HE2  1 
ATOM   6119  H  HZ   . PHE B 1 63  ? 13.011  15.320  -2.010  1.00 10.59  ?  286  PHE B HZ   1 
ATOM   6120  N  N    . ARG B 1 64  ? 13.242  7.522   -0.198  1.00 6.79   ?  287  ARG B N    1 
ATOM   6121  C  CA   C ARG B 1 64  ? 13.691  6.154   -0.422  0.51 7.48   ?  287  ARG B CA   1 
ATOM   6122  C  CA   D ARG B 1 64  ? 13.634  6.133   -0.402  0.49 7.34   ?  287  ARG B CA   1 
ATOM   6123  C  C    . ARG B 1 64  ? 13.354  5.754   -1.848  1.00 6.60   ?  287  ARG B C    1 
ATOM   6124  O  O    . ARG B 1 64  ? 12.487  6.339   -2.497  1.00 7.44   ?  287  ARG B O    1 
ATOM   6125  C  CB   C ARG B 1 64  ? 13.175  5.166   0.640   0.51 10.40  ?  287  ARG B CB   1 
ATOM   6126  C  CB   D ARG B 1 64  ? 12.912  5.191   0.568   0.49 10.43  ?  287  ARG B CB   1 
ATOM   6127  C  CG   C ARG B 1 64  ? 11.814  4.561   0.380   0.51 11.36  ?  287  ARG B CG   1 
ATOM   6128  C  CG   D ARG B 1 64  ? 11.419  5.192   0.440   0.49 12.04  ?  287  ARG B CG   1 
ATOM   6129  C  CD   C ARG B 1 64  ? 10.723  5.608   0.309   0.51 12.20  ?  287  ARG B CD   1 
ATOM   6130  C  CD   D ARG B 1 64  ? 10.790  4.199   1.397   0.49 13.18  ?  287  ARG B CD   1 
ATOM   6131  N  NE   C ARG B 1 64  ? 10.751  6.486   1.466   0.51 12.30  ?  287  ARG B NE   1 
ATOM   6132  N  NE   D ARG B 1 64  ? 11.151  2.828   1.058   0.49 15.16  ?  287  ARG B NE   1 
ATOM   6133  C  CZ   C ARG B 1 64  ? 9.876   7.454   1.685   0.51 13.02  ?  287  ARG B CZ   1 
ATOM   6134  C  CZ   D ARG B 1 64  ? 10.679  1.746   1.663   0.49 16.48  ?  287  ARG B CZ   1 
ATOM   6135  N  NH1  C ARG B 1 64  ? 8.832   7.634   0.894   0.51 13.76  ?  287  ARG B NH1  1 
ATOM   6136  N  NH1  D ARG B 1 64  ? 9.803   1.828   2.652   0.49 16.13  ?  287  ARG B NH1  1 
ATOM   6137  N  NH2  C ARG B 1 64  ? 10.051  8.257   2.718   0.51 12.96  ?  287  ARG B NH2  1 
ATOM   6138  N  NH2  D ARG B 1 64  ? 11.091  0.551   1.258   0.49 17.59  ?  287  ARG B NH2  1 
ATOM   6139  H  H    C ARG B 1 64  ? 12.478  7.711   -0.545  0.51 8.16   ?  287  ARG B H    1 
ATOM   6140  H  H    D ARG B 1 64  ? 12.492  7.727   -0.565  0.49 8.16   ?  287  ARG B H    1 
ATOM   6141  H  HA   C ARG B 1 64  ? 14.657  6.106   -0.346  0.51 8.97   ?  287  ARG B HA   1 
ATOM   6142  H  HA   D ARG B 1 64  ? 14.586  6.030   -0.246  0.49 8.82   ?  287  ARG B HA   1 
ATOM   6143  H  HB2  C ARG B 1 64  ? 13.807  4.433   0.704   0.51 12.49  ?  287  ARG B HB2  1 
ATOM   6144  H  HB2  D ARG B 1 64  ? 13.219  4.285   0.406   0.49 12.51  ?  287  ARG B HB2  1 
ATOM   6145  H  HB3  C ARG B 1 64  ? 13.123  5.634   1.488   0.51 12.49  ?  287  ARG B HB3  1 
ATOM   6146  H  HB3  D ARG B 1 64  ? 13.128  5.457   1.476   0.49 12.51  ?  287  ARG B HB3  1 
ATOM   6147  H  HG2  C ARG B 1 64  ? 11.833  4.087   -0.466  0.51 13.63  ?  287  ARG B HG2  1 
ATOM   6148  H  HG2  D ARG B 1 64  ? 11.078  6.076   0.646   0.49 14.45  ?  287  ARG B HG2  1 
ATOM   6149  H  HG3  C ARG B 1 64  ? 11.597  3.947   1.099   0.51 13.63  ?  287  ARG B HG3  1 
ATOM   6150  H  HG3  D ARG B 1 64  ? 11.173  4.944   -0.465  0.49 14.45  ?  287  ARG B HG3  1 
ATOM   6151  H  HD2  C ARG B 1 64  ? 10.847  6.147   -0.487  0.51 14.64  ?  287  ARG B HD2  1 
ATOM   6152  H  HD2  D ARG B 1 64  ? 11.099  4.382   2.298   0.49 15.82  ?  287  ARG B HD2  1 
ATOM   6153  H  HD3  C ARG B 1 64  ? 9.859   5.169   0.281   0.51 14.64  ?  287  ARG B HD3  1 
ATOM   6154  H  HD3  D ARG B 1 64  ? 9.825   4.280   1.354   0.49 15.82  ?  287  ARG B HD3  1 
ATOM   6155  H  HE   C ARG B 1 64  ? 11.377  6.370   2.045   0.51 14.76  ?  287  ARG B HE   1 
ATOM   6156  H  HE   D ARG B 1 64  ? 11.713  2.712   0.418   0.49 18.19  ?  287  ARG B HE   1 
ATOM   6157  H  HH11 C ARG B 1 64  ? 8.710   7.115   0.219   0.51 16.52  ?  287  ARG B HH11 1 
ATOM   6158  H  HH11 D ARG B 1 64  ? 9.526   2.597   2.918   0.49 19.36  ?  287  ARG B HH11 1 
ATOM   6159  H  HH12 C ARG B 1 64  ? 8.275   8.269   1.054   0.51 16.52  ?  287  ARG B HH12 1 
ATOM   6160  H  HH12 D ARG B 1 64  ? 9.512   1.112   3.028   0.49 19.36  ?  287  ARG B HH12 1 
ATOM   6161  H  HH21 C ARG B 1 64  ? 10.727  8.147   3.238   0.51 15.56  ?  287  ARG B HH21 1 
ATOM   6162  H  HH21 D ARG B 1 64  ? 11.656  0.487   0.613   0.49 21.11  ?  287  ARG B HH21 1 
ATOM   6163  H  HH22 C ARG B 1 64  ? 9.490   8.890   2.871   0.51 15.56  ?  287  ARG B HH22 1 
ATOM   6164  H  HH22 D ARG B 1 64  ? 10.793  -0.159  1.641   0.49 21.11  ?  287  ARG B HH22 1 
ATOM   6165  N  N    . GLY B 1 65  ? 14.083  4.757   -2.337  1.00 5.85   ?  288  GLY B N    1 
ATOM   6166  C  CA   . GLY B 1 65  ? 13.940  4.293   -3.700  1.00 6.47   ?  288  GLY B CA   1 
ATOM   6167  C  C    . GLY B 1 65  ? 15.200  3.564   -4.110  1.00 6.56   ?  288  GLY B C    1 
ATOM   6168  O  O    . GLY B 1 65  ? 15.651  2.665   -3.393  1.00 6.82   ?  288  GLY B O    1 
ATOM   6169  H  H    . GLY B 1 65  ? 14.677  4.328   -1.887  1.00 7.02   ?  288  GLY B H    1 
ATOM   6170  H  HA2  . GLY B 1 65  ? 13.185  3.689   -3.769  1.00 7.76   ?  288  GLY B HA2  1 
ATOM   6171  H  HA3  . GLY B 1 65  ? 13.799  5.046   -4.296  1.00 7.76   ?  288  GLY B HA3  1 
ATOM   6172  N  N    . SER B 1 66  ? 15.783  3.941   -5.247  1.00 7.23   ?  289  SER B N    1 
ATOM   6173  C  CA   A SER B 1 66  ? 16.980  3.282   -5.736  0.53 6.97   ?  289  SER B CA   1 
ATOM   6174  C  CA   B SER B 1 66  ? 16.958  3.260   -5.774  0.47 7.02   ?  289  SER B CA   1 
ATOM   6175  C  C    . SER B 1 66  ? 17.752  4.238   -6.632  1.00 6.67   ?  289  SER B C    1 
ATOM   6176  O  O    . SER B 1 66  ? 17.183  5.109   -7.284  1.00 8.07   ?  289  SER B O    1 
ATOM   6177  C  CB   A SER B 1 66  ? 16.604  2.022   -6.516  0.53 7.74   ?  289  SER B CB   1 
ATOM   6178  C  CB   B SER B 1 66  ? 16.586  2.056   -6.660  0.47 7.89   ?  289  SER B CB   1 
ATOM   6179  O  OG   A SER B 1 66  ? 15.632  2.333   -7.497  0.53 8.94   ?  289  SER B OG   1 
ATOM   6180  O  OG   B SER B 1 66  ? 15.965  1.000   -5.949  0.47 9.30   ?  289  SER B OG   1 
ATOM   6181  H  H    A SER B 1 66  ? 15.500  4.579   -5.751  0.53 8.68   ?  289  SER B H    1 
ATOM   6182  H  H    B SER B 1 66  ? 15.513  4.596   -5.735  0.47 8.68   ?  289  SER B H    1 
ATOM   6183  H  HA   A SER B 1 66  ? 17.558  3.044   -4.994  0.53 8.36   ?  289  SER B HA   1 
ATOM   6184  H  HA   B SER B 1 66  ? 17.493  2.956   -5.025  0.47 8.43   ?  289  SER B HA   1 
ATOM   6185  H  HB2  A SER B 1 66  ? 17.395  1.667   -6.951  0.53 9.29   ?  289  SER B HB2  1 
ATOM   6186  H  HB2  B SER B 1 66  ? 15.975  2.361   -7.349  0.47 9.47   ?  289  SER B HB2  1 
ATOM   6187  H  HB3  A SER B 1 66  ? 16.239  1.364   -5.903  0.53 9.29   ?  289  SER B HB3  1 
ATOM   6188  H  HB3  B SER B 1 66  ? 17.398  1.713   -7.066  0.47 9.47   ?  289  SER B HB3  1 
ATOM   6189  H  HG   A SER B 1 66  ? 15.933  2.913   -8.025  0.53 10.73  ?  289  SER B HG   1 
ATOM   6190  H  HG   B SER B 1 66  ? 15.236  1.263   -5.624  0.47 11.16  ?  289  SER B HG   1 
ATOM   6191  N  N    . ILE B 1 67  ? 19.060  4.058   -6.644  1.00 6.85   ?  290  ILE B N    1 
ATOM   6192  C  CA   . ILE B 1 67  ? 19.925  4.783   -7.568  1.00 6.60   ?  290  ILE B CA   1 
ATOM   6193  C  C    . ILE B 1 67  ? 19.899  4.063   -8.904  1.00 7.40   ?  290  ILE B C    1 
ATOM   6194  O  O    . ILE B 1 67  ? 19.941  2.825   -8.956  1.00 7.31   ?  290  ILE B O    1 
ATOM   6195  C  CB   . ILE B 1 67  ? 21.358  4.887   -7.015  1.00 6.51   ?  290  ILE B CB   1 
ATOM   6196  C  CG1  . ILE B 1 67  ? 21.393  5.683   -5.695  1.00 6.93   ?  290  ILE B CG1  1 
ATOM   6197  C  CG2  . ILE B 1 67  ? 22.304  5.472   -8.065  1.00 7.19   ?  290  ILE B CG2  1 
ATOM   6198  C  CD1  . ILE B 1 67  ? 20.929  7.149   -5.820  1.00 7.37   ?  290  ILE B CD1  1 
ATOM   6199  H  H    . ILE B 1 67  ? 19.480  3.517   -6.123  1.00 8.22   ?  290  ILE B H    1 
ATOM   6200  H  HA   . ILE B 1 67  ? 19.591  5.686   -7.683  1.00 7.92   ?  290  ILE B HA   1 
ATOM   6201  H  HB   . ILE B 1 67  ? 21.667  3.990   -6.812  1.00 7.81   ?  290  ILE B HB   1 
ATOM   6202  H  HG12 . ILE B 1 67  ? 20.811  5.245   -5.054  1.00 8.32   ?  290  ILE B HG12 1 
ATOM   6203  H  HG13 . ILE B 1 67  ? 22.305  5.692   -5.363  1.00 8.32   ?  290  ILE B HG13 1 
ATOM   6204  H  HG21 . ILE B 1 67  ? 23.133  5.733   -7.633  1.00 8.63   ?  290  ILE B HG21 1 
ATOM   6205  H  HG22 . ILE B 1 67  ? 22.482  4.799   -8.740  1.00 8.63   ?  290  ILE B HG22 1 
ATOM   6206  H  HG23 . ILE B 1 67  ? 21.885  6.247   -8.471  1.00 8.63   ?  290  ILE B HG23 1 
ATOM   6207  H  HD11 . ILE B 1 67  ? 21.120  7.613   -4.990  1.00 8.85   ?  290  ILE B HD11 1 
ATOM   6208  H  HD12 . ILE B 1 67  ? 21.407  7.570   -6.552  1.00 8.85   ?  290  ILE B HD12 1 
ATOM   6209  H  HD13 . ILE B 1 67  ? 19.975  7.164   -5.996  1.00 8.85   ?  290  ILE B HD13 1 
ATOM   6210  N  N    A SER B 1 68  ? 19.865  4.816   -10.008 0.70 8.56   ?  291  SER B N    1 
ATOM   6211  N  N    B SER B 1 68  ? 19.763  4.831   -9.980  0.30 8.10   ?  291  SER B N    1 
ATOM   6212  C  CA   A SER B 1 68  ? 19.839  4.169   -11.319 0.70 10.07  ?  291  SER B CA   1 
ATOM   6213  C  CA   B SER B 1 68  ? 19.828  4.284   -11.322 0.30 9.24   ?  291  SER B CA   1 
ATOM   6214  C  C    A SER B 1 68  ? 20.837  4.694   -12.342 0.70 10.36  ?  291  SER B C    1 
ATOM   6215  C  C    B SER B 1 68  ? 20.449  5.359   -12.215 0.30 10.15  ?  291  SER B C    1 
ATOM   6216  O  O    A SER B 1 68  ? 20.823  4.221   -13.481 0.70 11.84  ?  291  SER B O    1 
ATOM   6217  O  O    B SER B 1 68  ? 19.815  5.996   -13.052 0.30 10.03  ?  291  SER B O    1 
ATOM   6218  C  CB   A SER B 1 68  ? 18.433  4.210   -11.932 0.70 13.54  ?  291  SER B CB   1 
ATOM   6219  C  CB   B SER B 1 68  ? 18.473  3.804   -11.840 0.30 10.87  ?  291  SER B CB   1 
ATOM   6220  O  OG   A SER B 1 68  ? 18.045  5.526   -12.193 0.70 15.53  ?  291  SER B OG   1 
ATOM   6221  O  OG   B SER B 1 68  ? 18.630  3.135   -13.077 0.30 11.62  ?  291  SER B OG   1 
ATOM   6222  H  H    A SER B 1 68  ? 19.857  5.676   -10.021 0.70 10.27  ?  291  SER B H    1 
ATOM   6223  H  H    B SER B 1 68  ? 19.632  5.681   -9.953  0.30 9.72   ?  291  SER B H    1 
ATOM   6224  H  HA   A SER B 1 68  ? 20.075  3.241   -11.161 0.70 12.08  ?  291  SER B HA   1 
ATOM   6225  H  HA   B SER B 1 68  ? 20.409  3.507   -11.320 0.30 11.09  ?  291  SER B HA   1 
ATOM   6226  H  HB2  A SER B 1 68  ? 18.437  3.710   -12.764 0.70 16.25  ?  291  SER B HB2  1 
ATOM   6227  H  HB2  B SER B 1 68  ? 18.084  3.192   -11.195 0.30 13.04  ?  291  SER B HB2  1 
ATOM   6228  H  HB3  A SER B 1 68  ? 17.805  3.812   -11.309 0.70 16.25  ?  291  SER B HB3  1 
ATOM   6229  H  HB3  B SER B 1 68  ? 17.890  4.570   -11.965 0.30 13.04  ?  291  SER B HB3  1 
ATOM   6230  H  HG   A SER B 1 68  ? 18.567  5.875   -12.751 0.70 18.64  ?  291  SER B HG   1 
ATOM   6231  H  HG   B SER B 1 68  ? 19.124  2.463   -12.980 0.30 13.94  ?  291  SER B HG   1 
ATOM   6232  N  N    . GLY B 1 69  ? 21.717  5.610   -11.975 1.00 10.20  ?  292  GLY B N    1 
ATOM   6233  C  CA   . GLY B 1 69  ? 22.592  6.242   -12.942 1.00 10.50  ?  292  GLY B CA   1 
ATOM   6234  C  C    . GLY B 1 69  ? 23.545  7.198   -12.267 1.00 9.67   ?  292  GLY B C    1 
ATOM   6235  O  O    . GLY B 1 69  ? 23.336  7.624   -11.125 1.00 8.98   ?  292  GLY B O    1 
ATOM   6236  H  H    A GLY B 1 69  ? 21.827  5.884   -11.168 0.70 12.24  ?  292  GLY B H    1 
ATOM   6237  H  H    B GLY B 1 69  ? 22.110  5.417   -11.235 0.30 12.24  ?  292  GLY B H    1 
ATOM   6238  H  HA2  . GLY B 1 69  ? 23.108  5.566   -13.407 1.00 12.60  ?  292  GLY B HA2  1 
ATOM   6239  H  HA3  . GLY B 1 69  ? 22.063  6.736   -13.588 1.00 12.60  ?  292  GLY B HA3  1 
ATOM   6240  N  N    . HIS B 1 70  ? 24.583  7.572   -13.013 1.00 10.77  ?  293  HIS B N    1 
ATOM   6241  C  CA   . HIS B 1 70  ? 25.697  8.366   -12.531 1.00 12.28  ?  293  HIS B CA   1 
ATOM   6242  C  C    . HIS B 1 70  ? 26.056  9.420   -13.562 1.00 14.49  ?  293  HIS B C    1 
ATOM   6243  O  O    . HIS B 1 70  ? 25.946  9.194   -14.773 1.00 15.58  ?  293  HIS B O    1 
ATOM   6244  C  CB   . HIS B 1 70  ? 26.936  7.484   -12.319 1.00 12.66  ?  293  HIS B CB   1 
ATOM   6245  C  CG   . HIS B 1 70  ? 28.199  8.250   -12.079 1.00 13.27  ?  293  HIS B CG   1 
ATOM   6246  N  ND1  . HIS B 1 70  ? 29.107  8.524   -13.083 1.00 16.12  ?  293  HIS B ND1  1 
ATOM   6247  C  CD2  . HIS B 1 70  ? 28.716  8.785   -10.945 1.00 12.75  ?  293  HIS B CD2  1 
ATOM   6248  C  CE1  . HIS B 1 70  ? 30.117  9.210   -12.578 1.00 16.06  ?  293  HIS B CE1  1 
ATOM   6249  N  NE2  . HIS B 1 70  ? 29.905  9.378   -11.287 1.00 14.38  ?  293  HIS B NE2  1 
ATOM   6250  H  H    . HIS B 1 70  ? 24.665  7.364   -13.843 1.00 12.92  ?  293  HIS B H    1 
ATOM   6251  H  HA   . HIS B 1 70  ? 25.442  8.801   -11.703 1.00 14.74  ?  293  HIS B HA   1 
ATOM   6252  H  HB2  . HIS B 1 70  ? 26.785  6.917   -11.546 1.00 15.19  ?  293  HIS B HB2  1 
ATOM   6253  H  HB3  . HIS B 1 70  ? 27.068  6.939   -13.110 1.00 15.19  ?  293  HIS B HB3  1 
ATOM   6254  H  HD1  . HIS B 1 70  ? 29.027  8.287   -13.905 1.00 19.35  ?  293  HIS B HD1  1 
ATOM   6255  H  HD2  . HIS B 1 70  ? 28.335  8.757   -10.097 1.00 15.30  ?  293  HIS B HD2  1 
ATOM   6256  H  HE1  . HIS B 1 70  ? 30.854  9.521   -13.052 1.00 19.27  ?  293  HIS B HE1  1 
ATOM   6257  N  N    . GLU B 1 71  ? 26.503  10.573  -13.067 1.00 16.66  ?  294  GLU B N    1 
ATOM   6258  C  CA   . GLU B 1 71  ? 27.083  11.621  -13.894 1.00 19.42  ?  294  GLU B CA   1 
ATOM   6259  C  C    . GLU B 1 71  ? 28.304  12.175  -13.180 1.00 20.08  ?  294  GLU B C    1 
ATOM   6260  O  O    . GLU B 1 71  ? 28.244  12.485  -11.986 1.00 18.60  ?  294  GLU B O    1 
ATOM   6261  C  CB   . GLU B 1 71  ? 26.064  12.736  -14.129 1.00 23.39  ?  294  GLU B CB   1 
ATOM   6262  C  CG   . GLU B 1 71  ? 26.568  13.886  -14.968 1.00 28.22  ?  294  GLU B CG   1 
ATOM   6263  C  CD   . GLU B 1 71  ? 25.495  14.928  -15.194 1.00 31.88  ?  294  GLU B CD   1 
ATOM   6264  O  OE1  . GLU B 1 71  ? 24.302  14.587  -15.053 1.00 33.16  ?  294  GLU B OE1  1 
ATOM   6265  O  OE2  . GLU B 1 71  ? 25.845  16.085  -15.503 1.00 33.80  -1 294  GLU B OE2  1 
ATOM   6266  H  H    . GLU B 1 71  ? 26.479  10.774  -12.231 1.00 19.99  ?  294  GLU B H    1 
ATOM   6267  H  HA   . GLU B 1 71  ? 27.360  11.262  -14.751 1.00 23.30  ?  294  GLU B HA   1 
ATOM   6268  H  HB2  . GLU B 1 71  ? 25.294  12.360  -14.582 1.00 28.07  ?  294  GLU B HB2  1 
ATOM   6269  H  HB3  . GLU B 1 71  ? 25.799  13.098  -13.268 1.00 28.07  ?  294  GLU B HB3  1 
ATOM   6270  H  HG2  . GLU B 1 71  ? 27.313  14.310  -14.515 1.00 33.87  ?  294  GLU B HG2  1 
ATOM   6271  H  HG3  . GLU B 1 71  ? 26.852  13.550  -15.832 1.00 33.87  ?  294  GLU B HG3  1 
ATOM   6272  N  N    . GLY B 1 72  ? 29.411  12.284  -13.907 1.00 22.98  ?  295  GLY B N    1 
ATOM   6273  C  CA   . GLY B 1 72  ? 30.580  12.938  -13.368 1.00 25.63  ?  295  GLY B CA   1 
ATOM   6274  C  C    . GLY B 1 72  ? 30.476  14.446  -13.485 1.00 27.60  ?  295  GLY B C    1 
ATOM   6275  O  O    . GLY B 1 72  ? 29.809  14.987  -14.369 1.00 28.74  ?  295  GLY B O    1 
ATOM   6276  H  H    . GLY B 1 72  ? 29.504  11.988  -14.709 1.00 27.58  ?  295  GLY B H    1 
ATOM   6277  H  HA2  . GLY B 1 72  ? 30.678  12.706  -12.431 1.00 30.75  ?  295  GLY B HA2  1 
ATOM   6278  H  HA3  . GLY B 1 72  ? 31.368  12.643  -13.851 1.00 30.75  ?  295  GLY B HA3  1 
ATOM   6279  N  N    . ASN B 1 73  ? 31.154  15.129  -12.570 0.77 28.06  ?  296  ASN B N    1 
ATOM   6280  C  CA   . ASN B 1 73  ? 31.120  16.595  -12.493 0.77 28.80  ?  296  ASN B CA   1 
ATOM   6281  C  C    . ASN B 1 73  ? 32.503  17.004  -11.970 0.77 28.68  ?  296  ASN B C    1 
ATOM   6282  O  O    . ASN B 1 73  ? 32.706  17.172  -10.765 0.77 27.92  ?  296  ASN B O    1 
ATOM   6283  C  CB   . ASN B 1 73  ? 29.978  17.061  -11.605 0.77 29.99  ?  296  ASN B CB   1 
ATOM   6284  C  CG   . ASN B 1 73  ? 30.022  18.548  -11.314 0.77 31.25  ?  296  ASN B CG   1 
ATOM   6285  O  OD1  . ASN B 1 73  ? 29.755  18.976  -10.187 0.77 31.85  ?  296  ASN B OD1  1 
ATOM   6286  N  ND2  . ASN B 1 73  ? 30.355  19.344  -12.323 0.77 31.50  ?  296  ASN B ND2  1 
ATOM   6287  H  H    . ASN B 1 73  ? 31.650  14.765  -11.969 0.77 33.67  ?  296  ASN B H    1 
ATOM   6288  H  HA   . ASN B 1 73  ? 30.987  16.999  -13.365 0.77 34.57  ?  296  ASN B HA   1 
ATOM   6289  H  HB2  . ASN B 1 73  ? 29.136  16.869  -12.048 0.77 35.99  ?  296  ASN B HB2  1 
ATOM   6290  H  HB3  . ASN B 1 73  ? 30.023  16.589  -10.759 0.77 35.99  ?  296  ASN B HB3  1 
ATOM   6291  H  HD21 . ASN B 1 73  ? 30.393  20.195  -12.205 0.77 37.80  ?  296  ASN B HD21 1 
ATOM   6292  H  HD22 . ASN B 1 73  ? 30.532  19.009  -13.095 0.77 37.80  ?  296  ASN B HD22 1 
ATOM   6293  N  N    . ASP B 1 74  ? 33.448  17.131  -12.896 0.59 29.13  ?  297  ASP B N    1 
ATOM   6294  C  CA   . ASP B 1 74  ? 34.868  17.295  -12.564 0.59 30.20  ?  297  ASP B CA   1 
ATOM   6295  C  C    . ASP B 1 74  ? 35.289  16.056  -11.782 0.59 29.42  ?  297  ASP B C    1 
ATOM   6296  O  O    . ASP B 1 74  ? 35.109  14.937  -12.294 0.59 28.84  ?  297  ASP B O    1 
ATOM   6297  C  CB   . ASP B 1 74  ? 35.071  18.650  -11.881 0.59 31.80  ?  297  ASP B CB   1 
ATOM   6298  C  CG   . ASP B 1 74  ? 36.527  18.925  -11.539 0.59 33.72  ?  297  ASP B CG   1 
ATOM   6299  O  OD1  . ASP B 1 74  ? 37.391  18.082  -11.869 0.59 34.62  -1 297  ASP B OD1  1 
ATOM   6300  O  OD2  . ASP B 1 74  ? 36.805  19.980  -10.929 0.59 34.28  -1 297  ASP B OD2  1 
ATOM   6301  H  H    . ASP B 1 74  ? 33.292  17.126  -13.741 0.59 34.96  ?  297  ASP B H    1 
ATOM   6302  H  HA   . ASP B 1 74  ? 35.392  17.308  -13.380 0.59 36.24  ?  297  ASP B HA   1 
ATOM   6303  H  HB2  . ASP B 1 74  ? 34.764  19.352  -12.475 0.59 38.16  ?  297  ASP B HB2  1 
ATOM   6304  H  HB3  . ASP B 1 74  ? 34.561  18.667  -11.056 0.59 38.16  ?  297  ASP B HB3  1 
ATOM   6305  N  N    . ASP B 1 75  ? 35.820  16.185  -10.570 1.00 28.99  ?  298  ASP B N    1 
ATOM   6306  C  CA   . ASP B 1 75  ? 36.179  15.044  -9.741  1.00 28.40  ?  298  ASP B CA   1 
ATOM   6307  C  C    . ASP B 1 75  ? 35.049  14.620  -8.810  1.00 25.02  ?  298  ASP B C    1 
ATOM   6308  O  O    . ASP B 1 75  ? 35.283  13.822  -7.895  1.00 25.62  ?  298  ASP B O    1 
ATOM   6309  C  CB   . ASP B 1 75  ? 37.432  15.374  -8.921  1.00 30.81  ?  298  ASP B CB   1 
ATOM   6310  C  CG   . ASP B 1 75  ? 37.228  16.558  -7.988  1.00 32.94  ?  298  ASP B CG   1 
ATOM   6311  O  OD1  . ASP B 1 75  ? 36.337  17.392  -8.260  1.00 33.96  ?  298  ASP B OD1  1 
ATOM   6312  O  OD2  . ASP B 1 75  ? 37.967  16.658  -6.984  1.00 33.53  -1 298  ASP B OD2  1 
ATOM   6313  H  H    . ASP B 1 75  ? 35.985  16.943  -10.199 1.00 34.79  ?  298  ASP B H    1 
ATOM   6314  H  HA   . ASP B 1 75  ? 36.387  14.292  -10.317 1.00 34.08  ?  298  ASP B HA   1 
ATOM   6315  H  HB2  . ASP B 1 75  ? 37.668  14.603  -8.381  1.00 36.97  ?  298  ASP B HB2  1 
ATOM   6316  H  HB3  . ASP B 1 75  ? 38.158  15.590  -9.526  1.00 36.97  ?  298  ASP B HB3  1 
ATOM   6317  N  N    A GLN B 1 76  ? 33.838  15.122  -9.037  0.76 20.56  ?  299  GLN B N    1 
ATOM   6318  C  CA   A GLN B 1 76  ? 32.695  14.927  -8.157  0.76 18.58  ?  299  GLN B CA   1 
ATOM   6319  C  C    A GLN B 1 76  ? 31.689  13.993  -8.808  0.76 14.33  ?  299  GLN B C    1 
ATOM   6320  O  O    A GLN B 1 76  ? 31.732  13.745  -10.016 0.76 14.75  ?  299  GLN B O    1 
ATOM   6321  C  CB   A GLN B 1 76  ? 32.012  16.268  -7.891  0.76 21.24  ?  299  GLN B CB   1 
ATOM   6322  C  CG   A GLN B 1 76  ? 32.949  17.344  -7.404  0.76 24.25  ?  299  GLN B CG   1 
ATOM   6323  C  CD   A GLN B 1 76  ? 32.887  17.468  -5.915  0.76 25.69  ?  299  GLN B CD   1 
ATOM   6324  O  OE1  A GLN B 1 76  ? 31.970  18.078  -5.379  0.76 25.55  ?  299  GLN B OE1  1 
ATOM   6325  N  NE2  A GLN B 1 76  ? 33.822  16.829  -5.228  0.76 27.01  ?  299  GLN B NE2  1 
ATOM   6326  H  H    A GLN B 1 76  ? 33.648  15.599  -9.726  0.76 24.68  ?  299  GLN B H    1 
ATOM   6327  H  HA   A GLN B 1 76  ? 32.998  14.537  -7.322  0.76 22.30  ?  299  GLN B HA   1 
ATOM   6328  H  HB2  A GLN B 1 76  ? 31.606  16.580  -8.715  0.76 25.49  ?  299  GLN B HB2  1 
ATOM   6329  H  HB3  A GLN B 1 76  ? 31.331  16.141  -7.212  0.76 25.49  ?  299  GLN B HB3  1 
ATOM   6330  H  HG2  A GLN B 1 76  ? 33.858  17.121  -7.658  0.76 29.10  ?  299  GLN B HG2  1 
ATOM   6331  H  HG3  A GLN B 1 76  ? 32.696  18.195  -7.795  0.76 29.10  ?  299  GLN B HG3  1 
ATOM   6332  H  HE21 A GLN B 1 76  ? 34.423  16.373  -5.642  0.76 32.41  ?  299  GLN B HE21 1 
ATOM   6333  H  HE22 A GLN B 1 76  ? 33.828  16.869  -4.369  0.76 32.41  ?  299  GLN B HE22 1 
ATOM   6334  N  N    . HIS B 1 77  ? 30.753  13.492  -7.992  1.00 11.22  ?  300  HIS B N    1 
ATOM   6335  C  CA   . HIS B 1 77  ? 29.834  12.449  -8.426  1.00 9.34   ?  300  HIS B CA   1 
ATOM   6336  C  C    . HIS B 1 77  ? 28.400  12.831  -8.124  1.00 8.66   ?  300  HIS B C    1 
ATOM   6337  O  O    . HIS B 1 77  ? 28.080  13.262  -7.011  1.00 9.08   ?  300  HIS B O    1 
ATOM   6338  C  CB   . HIS B 1 77  ? 30.205  11.112  -7.785  1.00 8.84   ?  300  HIS B CB   1 
ATOM   6339  C  CG   . HIS B 1 77  ? 31.586  10.686  -8.136  1.00 9.57   ?  300  HIS B CG   1 
ATOM   6340  N  ND1  . HIS B 1 77  ? 31.898  10.137  -9.364  1.00 11.58  ?  300  HIS B ND1  1 
ATOM   6341  C  CD2  . HIS B 1 77  ? 32.752  10.799  -7.461  1.00 10.68  ?  300  HIS B CD2  1 
ATOM   6342  C  CE1  . HIS B 1 77  ? 33.199  9.908   -9.415  1.00 11.88  ?  300  HIS B CE1  1 
ATOM   6343  N  NE2  . HIS B 1 77  ? 33.736  10.289  -8.272  1.00 11.59  ?  300  HIS B NE2  1 
ATOM   6344  H  H    . HIS B 1 77  ? 30.634  13.747  -7.179  1.00 13.46  ?  300  HIS B H    1 
ATOM   6345  H  HA   . HIS B 1 77  ? 29.887  12.356  -9.390  1.00 11.21  ?  300  HIS B HA   1 
ATOM   6346  H  HB2  . HIS B 1 77  ? 30.150  11.195  -6.820  1.00 10.61  ?  300  HIS B HB2  1 
ATOM   6347  H  HB3  . HIS B 1 77  ? 29.590  10.429  -8.094  1.00 10.61  ?  300  HIS B HB3  1 
ATOM   6348  H  HD1  . HIS B 1 77  ? 31.337  9.971   -9.994  1.00 13.90  ?  300  HIS B HD1  1 
ATOM   6349  H  HD2  . HIS B 1 77  ? 32.866  11.154  -6.609  1.00 12.82  ?  300  HIS B HD2  1 
ATOM   6350  H  HE1  . HIS B 1 77  ? 33.658  9.541   -10.135 1.00 14.25  ?  300  HIS B HE1  1 
ATOM   6351  N  N    . LEU B 1 78  ? 27.551  12.671  -9.136  1.00 8.39   ?  301  LEU B N    1 
ATOM   6352  C  CA   . LEU B 1 78  ? 26.121  12.927  -9.059  1.00 8.93   ?  301  LEU B CA   1 
ATOM   6353  C  C    . LEU B 1 78  ? 25.399  11.645  -9.455  1.00 8.42   ?  301  LEU B C    1 
ATOM   6354  O  O    . LEU B 1 78  ? 25.859  10.912  -10.334 1.00 9.92   ?  301  LEU B O    1 
ATOM   6355  C  CB   . LEU B 1 78  ? 25.719  14.033  -10.032 1.00 11.09  ?  301  LEU B CB   1 
ATOM   6356  C  CG   . LEU B 1 78  ? 26.479  15.346  -9.873  1.00 14.30  ?  301  LEU B CG   1 
ATOM   6357  C  CD1  . LEU B 1 78  ? 26.251  16.261  -11.074 1.00 15.51  ?  301  LEU B CD1  1 
ATOM   6358  C  CD2  . LEU B 1 78  ? 26.052  16.014  -8.588  1.00 16.35  ?  301  LEU B CD2  1 
ATOM   6359  H  H    . LEU B 1 78  ? 27.795  12.401  -9.915  1.00 10.07  ?  301  LEU B H    1 
ATOM   6360  H  HA   . LEU B 1 78  ? 25.868  13.193  -8.162  1.00 10.72  ?  301  LEU B HA   1 
ATOM   6361  H  HB2  . LEU B 1 78  ? 25.873  13.716  -10.936 1.00 13.31  ?  301  LEU B HB2  1 
ATOM   6362  H  HB3  . LEU B 1 78  ? 24.777  14.226  -9.904  1.00 13.31  ?  301  LEU B HB3  1 
ATOM   6363  H  HG   . LEU B 1 78  ? 27.432  15.170  -9.833  1.00 17.17  ?  301  LEU B HG   1 
ATOM   6364  H  HD11 . LEU B 1 78  ? 26.745  17.084  -10.941 1.00 18.61  ?  301  LEU B HD11 1 
ATOM   6365  H  HD12 . LEU B 1 78  ? 26.562  15.813  -11.876 1.00 18.61  ?  301  LEU B HD12 1 
ATOM   6366  H  HD13 . LEU B 1 78  ? 25.303  16.453  -11.149 1.00 18.61  ?  301  LEU B HD13 1 
ATOM   6367  H  HD21 . LEU B 1 78  ? 26.823  16.441  -8.183  1.00 19.62  ?  301  LEU B HD21 1 
ATOM   6368  H  HD22 . LEU B 1 78  ? 25.372  16.677  -8.786  1.00 19.62  ?  301  LEU B HD22 1 
ATOM   6369  H  HD23 . LEU B 1 78  ? 25.693  15.342  -7.987  1.00 19.62  ?  301  LEU B HD23 1 
ATOM   6370  N  N    . TRP B 1 79  ? 24.267  11.386  -8.810  1.00 7.43   ?  302  TRP B N    1 
ATOM   6371  C  CA   . TRP B 1 79  ? 23.569  10.126  -8.985  1.00 7.49   ?  302  TRP B CA   1 
ATOM   6372  C  C    . TRP B 1 79  ? 22.081  10.373  -9.164  1.00 7.16   ?  302  TRP B C    1 
ATOM   6373  O  O    . TRP B 1 79  ? 21.501  11.227  -8.489  1.00 8.08   ?  302  TRP B O    1 
ATOM   6374  C  CB   . TRP B 1 79  ? 23.790  9.181   -7.777  1.00 7.04   ?  302  TRP B CB   1 
ATOM   6375  C  CG   . TRP B 1 79  ? 25.250  9.105   -7.352  1.00 7.00   ?  302  TRP B CG   1 
ATOM   6376  C  CD1  . TRP B 1 79  ? 25.889  9.952   -6.492  1.00 6.73   ?  302  TRP B CD1  1 
ATOM   6377  C  CD2  . TRP B 1 79  ? 26.235  8.169   -7.793  1.00 7.25   ?  302  TRP B CD2  1 
ATOM   6378  N  NE1  . TRP B 1 79  ? 27.204  9.607   -6.374  1.00 6.78   ?  302  TRP B NE1  1 
ATOM   6379  C  CE2  . TRP B 1 79  ? 27.447  8.509   -7.155  1.00 7.56   ?  302  TRP B CE2  1 
ATOM   6380  C  CE3  . TRP B 1 79  ? 26.209  7.064   -8.651  1.00 8.10   ?  302  TRP B CE3  1 
ATOM   6381  C  CZ2  . TRP B 1 79  ? 28.616  7.785   -7.351  1.00 8.13   ?  302  TRP B CZ2  1 
ATOM   6382  C  CZ3  . TRP B 1 79  ? 27.365  6.348   -8.838  1.00 7.81   ?  302  TRP B CZ3  1 
ATOM   6383  C  CH2  . TRP B 1 79  ? 28.560  6.710   -8.193  1.00 8.39   ?  302  TRP B CH2  1 
ATOM   6384  H  H    . TRP B 1 79  ? 23.884  11.929  -8.264  1.00 8.92   ?  302  TRP B H    1 
ATOM   6385  H  HA   . TRP B 1 79  ? 23.903  9.694   -9.787  1.00 8.99   ?  302  TRP B HA   1 
ATOM   6386  H  HB2  . TRP B 1 79  ? 23.274  9.506   -7.022  1.00 8.45   ?  302  TRP B HB2  1 
ATOM   6387  H  HB3  . TRP B 1 79  ? 23.500  8.287   -8.017  1.00 8.45   ?  302  TRP B HB3  1 
ATOM   6388  H  HD1  . TRP B 1 79  ? 25.485  10.663  -6.050  1.00 8.08   ?  302  TRP B HD1  1 
ATOM   6389  H  HE1  . TRP B 1 79  ? 27.785  10.014  -5.888  1.00 8.13   ?  302  TRP B HE1  1 
ATOM   6390  H  HE3  . TRP B 1 79  ? 25.424  6.819   -9.086  1.00 9.73   ?  302  TRP B HE3  1 
ATOM   6391  H  HZ2  . TRP B 1 79  ? 29.408  8.023   -6.924  1.00 9.76   ?  302  TRP B HZ2  1 
ATOM   6392  H  HZ3  . TRP B 1 79  ? 27.357  5.609   -9.402  1.00 9.37   ?  302  TRP B HZ3  1 
ATOM   6393  H  HH2  . TRP B 1 79  ? 29.328  6.207   -8.343  1.00 10.07  ?  302  TRP B HH2  1 
ATOM   6394  N  N    . HIS B 1 80  ? 21.472  9.591   -10.045 1.00 7.08   ?  303  HIS B N    1 
ATOM   6395  C  CA   . HIS B 1 80  ? 20.042  9.649   -10.304 1.00 7.47   ?  303  HIS B CA   1 
ATOM   6396  C  C    . HIS B 1 80  ? 19.326  8.767   -9.289  1.00 7.14   ?  303  HIS B C    1 
ATOM   6397  O  O    . HIS B 1 80  ? 19.559  7.557   -9.235  1.00 8.11   ?  303  HIS B O    1 
ATOM   6398  C  CB   . HIS B 1 80  ? 19.761  9.170   -11.724 1.00 8.45   ?  303  HIS B CB   1 
ATOM   6399  C  CG   . HIS B 1 80  ? 18.314  9.216   -12.089 1.00 11.03  ?  303  HIS B CG   1 
ATOM   6400  N  ND1  . HIS B 1 80  ? 17.755  10.267  -12.782 1.00 13.66  ?  303  HIS B ND1  1 
ATOM   6401  C  CD2  . HIS B 1 80  ? 17.304  8.356   -11.830 1.00 12.84  ?  303  HIS B CD2  1 
ATOM   6402  C  CE1  . HIS B 1 80  ? 16.464  10.042  -12.946 1.00 12.97  ?  303  HIS B CE1  1 
ATOM   6403  N  NE2  . HIS B 1 80  ? 16.167  8.886   -12.385 1.00 13.39  ?  303  HIS B NE2  1 
ATOM   6404  H  H    . HIS B 1 80  ? 21.879  9.001   -10.520 1.00 8.50   ?  303  HIS B H    1 
ATOM   6405  H  HA   . HIS B 1 80  ? 19.716  10.557  -10.208 1.00 8.96   ?  303  HIS B HA   1 
ATOM   6406  H  HB2  . HIS B 1 80  ? 20.243  9.736   -12.347 1.00 10.14  ?  303  HIS B HB2  1 
ATOM   6407  H  HB3  . HIS B 1 80  ? 20.060  8.252   -11.810 1.00 10.14  ?  303  HIS B HB3  1 
ATOM   6408  H  HD2  . HIS B 1 80  ? 17.368  7.555   -11.363 1.00 15.41  ?  303  HIS B HD2  1 
ATOM   6409  H  HE1  . HIS B 1 80  ? 15.866  10.603  -13.384 1.00 15.57  ?  303  HIS B HE1  1 
ATOM   6410  H  HE2  . HIS B 1 80  ? 15.387  8.524   -12.370 1.00 16.07  ?  303  HIS B HE2  1 
ATOM   6411  N  N    . PHE B 1 81  ? 18.462  9.383   -8.483  1.00 6.87   ?  304  PHE B N    1 
ATOM   6412  C  CA   . PHE B 1 81  ? 17.802  8.726   -7.357  1.00 6.79   ?  304  PHE B CA   1 
ATOM   6413  C  C    . PHE B 1 81  ? 16.309  8.644   -7.664  1.00 6.28   ?  304  PHE B C    1 
ATOM   6414  O  O    . PHE B 1 81  ? 15.573  9.627   -7.528  1.00 6.68   ?  304  PHE B O    1 
ATOM   6415  C  CB   . PHE B 1 81  ? 18.083  9.552   -6.105  1.00 6.65   ?  304  PHE B CB   1 
ATOM   6416  C  CG   . PHE B 1 81  ? 17.657  8.932   -4.790  1.00 7.23   ?  304  PHE B CG   1 
ATOM   6417  C  CD1  . PHE B 1 81  ? 17.062  7.682   -4.671  1.00 7.63   ?  304  PHE B CD1  1 
ATOM   6418  C  CD2  . PHE B 1 81  ? 17.894  9.655   -3.636  1.00 9.06   ?  304  PHE B CD2  1 
ATOM   6419  C  CE1  . PHE B 1 81  ? 16.723  7.186   -3.398  1.00 8.34   ?  304  PHE B CE1  1 
ATOM   6420  C  CE2  . PHE B 1 81  ? 17.547  9.171   -2.410  1.00 9.98   ?  304  PHE B CE2  1 
ATOM   6421  C  CZ   . PHE B 1 81  ? 16.975  7.940   -2.295  1.00 9.07   ?  304  PHE B CZ   1 
ATOM   6422  H  H    . PHE B 1 81  ? 18.236  10.208  -8.572  1.00 8.24   ?  304  PHE B H    1 
ATOM   6423  H  HA   . PHE B 1 81  ? 18.121  7.818   -7.238  1.00 8.15   ?  304  PHE B HA   1 
ATOM   6424  H  HB2  . PHE B 1 81  ? 19.039  9.708   -6.052  1.00 7.98   ?  304  PHE B HB2  1 
ATOM   6425  H  HB3  . PHE B 1 81  ? 17.613  10.397  -6.188  1.00 7.98   ?  304  PHE B HB3  1 
ATOM   6426  H  HD1  . PHE B 1 81  ? 16.889  7.174   -5.431  1.00 9.16   ?  304  PHE B HD1  1 
ATOM   6427  H  HD2  . PHE B 1 81  ? 18.300  10.490  -3.697  1.00 10.88  ?  304  PHE B HD2  1 
ATOM   6428  H  HE1  . PHE B 1 81  ? 16.329  6.348   -3.312  1.00 10.01  ?  304  PHE B HE1  1 
ATOM   6429  H  HE2  . PHE B 1 81  ? 17.700  9.683   -1.649  1.00 11.97  ?  304  PHE B HE2  1 
ATOM   6430  H  HZ   . PHE B 1 81  ? 16.755  7.612   -1.454  1.00 10.88  ?  304  PHE B HZ   1 
ATOM   6431  N  N    . ASN B 1 82  ? 15.868  7.468   -8.117  1.00 7.02   ?  305  ASN B N    1 
ATOM   6432  C  CA   . ASN B 1 82  ? 14.441  7.207   -8.285  1.00 8.01   ?  305  ASN B CA   1 
ATOM   6433  C  C    . ASN B 1 82  ? 13.803  7.053   -6.917  1.00 8.47   ?  305  ASN B C    1 
ATOM   6434  O  O    . ASN B 1 82  ? 14.303  6.308   -6.073  1.00 9.96   ?  305  ASN B O    1 
ATOM   6435  C  CB   . ASN B 1 82  ? 14.245  5.930   -9.103  1.00 10.16  ?  305  ASN B CB   1 
ATOM   6436  C  CG   . ASN B 1 82  ? 14.565  6.125   -10.570 1.00 13.60  ?  305  ASN B CG   1 
ATOM   6437  O  OD1  . ASN B 1 82  ? 14.190  7.131   -11.164 1.00 15.84  ?  305  ASN B OD1  1 
ATOM   6438  N  ND2  . ASN B 1 82  ? 15.270  5.168   -11.158 1.00 17.29  ?  305  ASN B ND2  1 
ATOM   6439  H  H    . ASN B 1 82  ? 16.375  6.808   -8.333  1.00 8.42   ?  305  ASN B H    1 
ATOM   6440  H  HA   . ASN B 1 82  ? 14.014  7.940   -8.755  1.00 9.61   ?  305  ASN B HA   1 
ATOM   6441  H  HB2  . ASN B 1 82  ? 14.832  5.239   -8.757  1.00 12.20  ?  305  ASN B HB2  1 
ATOM   6442  H  HB3  . ASN B 1 82  ? 13.320  5.647   -9.032  1.00 12.20  ?  305  ASN B HB3  1 
ATOM   6443  H  HD21 . ASN B 1 82  ? 15.522  4.481   -10.707 1.00 20.75  ?  305  ASN B HD21 1 
ATOM   6444  H  HD22 . ASN B 1 82  ? 15.476  5.235   -11.991 1.00 20.75  ?  305  ASN B HD22 1 
ATOM   6445  N  N    . ILE B 1 83  ? 12.730  7.776   -6.673  1.00 6.81   ?  306  ILE B N    1 
ATOM   6446  C  CA   . ILE B 1 83  ? 12.104  7.781   -5.355  1.00 7.35   ?  306  ILE B CA   1 
ATOM   6447  C  C    . ILE B 1 83  ? 10.714  7.161   -5.424  1.00 7.92   ?  306  ILE B C    1 
ATOM   6448  O  O    . ILE B 1 83  ? 10.027  7.234   -6.449  1.00 9.37   ?  306  ILE B O    1 
ATOM   6449  C  CB   . ILE B 1 83  ? 12.068  9.183   -4.711  1.00 7.25   ?  306  ILE B CB   1 
ATOM   6450  C  CG1  . ILE B 1 83  ? 11.178  10.154  -5.508  1.00 7.94   ?  306  ILE B CG1  1 
ATOM   6451  C  CG2  . ILE B 1 83  ? 13.494  9.688   -4.546  1.00 8.05   ?  306  ILE B CG2  1 
ATOM   6452  C  CD1  . ILE B 1 83  ? 10.983  11.505  -4.820  1.00 8.12   ?  306  ILE B CD1  1 
ATOM   6453  H  H    . ILE B 1 83  ? 12.340  8.277   -7.254  1.00 8.18   ?  306  ILE B H    1 
ATOM   6454  H  HA   . ILE B 1 83  ? 12.638  7.211   -4.779  1.00 8.82   ?  306  ILE B HA   1 
ATOM   6455  H  HB   . ILE B 1 83  ? 11.660  9.123   -3.832  1.00 8.71   ?  306  ILE B HB   1 
ATOM   6456  H  HG12 . ILE B 1 83  ? 11.587  10.316  -6.372  1.00 9.53   ?  306  ILE B HG12 1 
ATOM   6457  H  HG13 . ILE B 1 83  ? 10.303  9.752   -5.626  1.00 9.53   ?  306  ILE B HG13 1 
ATOM   6458  H  HG21 . ILE B 1 83  ? 13.481  10.511  -4.033  1.00 9.66   ?  306  ILE B HG21 1 
ATOM   6459  H  HG22 . ILE B 1 83  ? 14.016  9.016   -4.081  1.00 9.66   ?  306  ILE B HG22 1 
ATOM   6460  H  HG23 . ILE B 1 83  ? 13.874  9.853   -5.424  1.00 9.66   ?  306  ILE B HG23 1 
ATOM   6461  H  HD11 . ILE B 1 83  ? 10.366  12.040  -5.344  1.00 9.74   ?  306  ILE B HD11 1 
ATOM   6462  H  HD12 . ILE B 1 83  ? 10.623  11.358  -3.932  1.00 9.74   ?  306  ILE B HD12 1 
ATOM   6463  H  HD13 . ILE B 1 83  ? 11.841  11.955  -4.759  1.00 9.74   ?  306  ILE B HD13 1 
ATOM   6464  N  N    . THR B 1 84  ? 10.304  6.550   -4.318  1.00 7.88   ?  307  THR B N    1 
ATOM   6465  C  CA   . THR B 1 84  ? 9.024   5.870   -4.179  1.00 8.24   ?  307  THR B CA   1 
ATOM   6466  C  C    . THR B 1 84  ? 8.238   6.459   -3.011  1.00 10.08  ?  307  THR B C    1 
ATOM   6467  O  O    . THR B 1 84  ? 8.696   7.380   -2.321  1.00 12.52  ?  307  THR B O    1 
ATOM   6468  C  CB   . THR B 1 84  ? 9.221   4.369   -3.918  1.00 8.92   ?  307  THR B CB   1 
ATOM   6469  O  OG1  . THR B 1 84  ? 9.811   4.187   -2.620  1.00 10.26  ?  307  THR B OG1  1 
ATOM   6470  C  CG2  . THR B 1 84  ? 10.097  3.738   -4.981  1.00 10.32  ?  307  THR B CG2  1 
ATOM   6471  H  H    . THR B 1 84  ? 10.774  6.515   -3.599  1.00 9.46   ?  307  THR B H    1 
ATOM   6472  H  HA   . THR B 1 84  ? 8.544   6.010   -5.010  1.00 9.89   ?  307  THR B HA   1 
ATOM   6473  H  HB   . THR B 1 84  ? 8.363   3.918   -3.948  1.00 10.70  ?  307  THR B HB   1 
ATOM   6474  H  HG1  . THR B 1 84  ? 9.252   4.377   -2.022  1.00 12.31  ?  307  THR B HG1  1 
ATOM   6475  H  HG21 . THR B 1 84  ? 10.155  2.780   -4.838  1.00 12.39  ?  307  THR B HG21 1 
ATOM   6476  H  HG22 . THR B 1 84  ? 9.723   3.903   -5.860  1.00 12.39  ?  307  THR B HG22 1 
ATOM   6477  H  HG23 . THR B 1 84  ? 10.990  4.116   -4.943  1.00 12.39  ?  307  THR B HG23 1 
ATOM   6478  N  N    A ASN B 1 85  ? 6.995   6.029   -2.843  0.67 10.55  ?  308  ASN B N    1 
ATOM   6479  N  N    B ASN B 1 85  ? 7.114   5.781   -2.727  0.33 10.78  ?  308  ASN B N    1 
ATOM   6480  C  CA   A ASN B 1 85  ? 6.285   6.422   -1.643  0.67 11.39  ?  308  ASN B CA   1 
ATOM   6481  C  CA   B ASN B 1 85  ? 6.419   5.796   -1.445  0.33 10.36  ?  308  ASN B CA   1 
ATOM   6482  C  C    A ASN B 1 85  ? 7.105   5.986   -0.427  0.67 11.23  ?  308  ASN B C    1 
ATOM   6483  C  C    B ASN B 1 85  ? 7.044   4.796   -0.466  0.33 9.75   ?  308  ASN B C    1 
ATOM   6484  O  O    A ASN B 1 85  ? 7.958   5.099   -0.528  0.67 11.31  ?  308  ASN B O    1 
ATOM   6485  O  O    B ASN B 1 85  ? 7.810   3.901   -0.846  0.33 10.88  ?  308  ASN B O    1 
ATOM   6486  C  CB   A ASN B 1 85  ? 4.903   5.781   -1.613  0.67 11.80  ?  308  ASN B CB   1 
ATOM   6487  C  CB   B ASN B 1 85  ? 4.953   5.408   -1.657  0.33 10.54  ?  308  ASN B CB   1 
ATOM   6488  C  CG   A ASN B 1 85  ? 3.983   6.340   -2.673  0.67 11.78  ?  308  ASN B CG   1 
ATOM   6489  C  CG   B ASN B 1 85  ? 4.240   6.299   -2.658  0.33 10.46  ?  308  ASN B CG   1 
ATOM   6490  O  OD1  A ASN B 1 85  ? 3.966   7.544   -2.922  0.67 11.36  ?  308  ASN B OD1  1 
ATOM   6491  O  OD1  B ASN B 1 85  ? 4.393   7.520   -2.643  0.33 10.15  ?  308  ASN B OD1  1 
ATOM   6492  N  ND2  A ASN B 1 85  ? 3.223   5.466   -3.320  0.67 11.81  ?  308  ASN B ND2  1 
ATOM   6493  N  ND2  B ASN B 1 85  ? 3.443   5.687   -3.531  0.33 10.40  ?  308  ASN B ND2  1 
ATOM   6494  H  H    A ASN B 1 85  ? 6.560   5.529   -3.390  0.67 12.67  ?  308  ASN B H    1 
ATOM   6495  H  H    B ASN B 1 85  ? 6.716   5.278   -3.299  0.33 12.94  ?  308  ASN B H    1 
ATOM   6496  H  HA   A ASN B 1 85  ? 6.160   7.384   -1.616  0.67 13.66  ?  308  ASN B HA   1 
ATOM   6497  H  HA   B ASN B 1 85  ? 6.484   6.690   -1.076  0.33 12.44  ?  308  ASN B HA   1 
ATOM   6498  H  HB2  A ASN B 1 85  ? 4.993   4.827   -1.764  0.67 14.17  ?  308  ASN B HB2  1 
ATOM   6499  H  HB2  B ASN B 1 85  ? 4.913   4.497   -1.986  0.33 12.65  ?  308  ASN B HB2  1 
ATOM   6500  H  HB3  A ASN B 1 85  ? 4.498   5.942   -0.746  0.67 14.17  ?  308  ASN B HB3  1 
ATOM   6501  H  HB3  B ASN B 1 85  ? 4.484   5.476   -0.810  0.33 12.65  ?  308  ASN B HB3  1 
ATOM   6502  H  HD21 A ASN B 1 85  ? 2.683   5.736   -3.933  0.67 14.17  ?  308  ASN B HD21 1 
ATOM   6503  H  HD21 B ASN B 1 85  ? 3.017   6.147   -4.119  0.33 12.48  ?  308  ASN B HD21 1 
ATOM   6504  H  HD22 A ASN B 1 85  ? 3.271   4.629   -3.127  0.67 14.17  ?  308  ASN B HD22 1 
ATOM   6505  H  HD22 B ASN B 1 85  ? 3.356   4.832   -3.507  0.33 12.48  ?  308  ASN B HD22 1 
ATOM   6506  N  N    A PRO B 1 86  ? 6.885   6.617   0.724   0.64 11.55  ?  309  PRO B N    1 
ATOM   6507  N  N    B PRO B 1 86  ? 6.710   4.909   0.827   0.36 9.94   ?  309  PRO B N    1 
ATOM   6508  C  CA   A PRO B 1 86  ? 7.558   6.164   1.950   0.64 12.24  ?  309  PRO B CA   1 
ATOM   6509  C  CA   B PRO B 1 86  ? 7.344   4.047   1.842   0.36 10.23  ?  309  PRO B CA   1 
ATOM   6510  C  C    A PRO B 1 86  ? 7.347   4.696   2.276   0.64 12.73  ?  309  PRO B C    1 
ATOM   6511  C  C    B PRO B 1 86  ? 7.271   2.545   1.589   0.36 11.02  ?  309  PRO B C    1 
ATOM   6512  O  O    A PRO B 1 86  ? 8.202   4.112   2.948   0.64 13.04  ?  309  PRO B O    1 
ATOM   6513  O  O    B PRO B 1 86  ? 8.275   1.848   1.796   0.36 11.82  ?  309  PRO B O    1 
ATOM   6514  C  CB   A PRO B 1 86  ? 6.964   7.076   3.034   0.64 13.17  ?  309  PRO B CB   1 
ATOM   6515  C  CB   B PRO B 1 86  ? 6.608   4.441   3.135   0.36 10.07  ?  309  PRO B CB   1 
ATOM   6516  C  CG   A PRO B 1 86  ? 6.554   8.307   2.294   0.64 12.34  ?  309  PRO B CG   1 
ATOM   6517  C  CG   B PRO B 1 86  ? 6.218   5.868   2.922   0.36 10.56  ?  309  PRO B CG   1 
ATOM   6518  C  CD   A PRO B 1 86  ? 6.087   7.832   0.946   0.64 11.74  ?  309  PRO B CD   1 
ATOM   6519  C  CD   B PRO B 1 86  ? 6.076   6.096   1.434   0.36 10.53  ?  309  PRO B CD   1 
ATOM   6520  H  HA   A PRO B 1 86  ? 8.510   6.332   1.872   0.64 14.69  ?  309  PRO B HA   1 
ATOM   6521  H  HA   B PRO B 1 86  ? 8.281   4.291   1.897   0.36 12.28  ?  309  PRO B HA   1 
ATOM   6522  H  HB2  A PRO B 1 86  ? 6.200   6.647   3.449   0.64 15.81  ?  309  PRO B HB2  1 
ATOM   6523  H  HB2  B PRO B 1 86  ? 5.826   3.880   3.257   0.36 12.09  ?  309  PRO B HB2  1 
ATOM   6524  H  HB3  A PRO B 1 86  ? 7.635   7.278   3.704   0.64 15.81  ?  309  PRO B HB3  1 
ATOM   6525  H  HB3  B PRO B 1 86  ? 7.203   4.352   3.897   0.36 12.09  ?  309  PRO B HB3  1 
ATOM   6526  H  HG2  A PRO B 1 86  ? 5.836   8.753   2.770   0.64 14.81  ?  309  PRO B HG2  1 
ATOM   6527  H  HG2  B PRO B 1 86  ? 5.374   6.038   3.369   0.36 12.68  ?  309  PRO B HG2  1 
ATOM   6528  H  HG3  A PRO B 1 86  ? 7.314   8.905   2.205   0.64 14.81  ?  309  PRO B HG3  1 
ATOM   6529  H  HG3  B PRO B 1 86  ? 6.908   6.445   3.285   0.36 12.68  ?  309  PRO B HG3  1 
ATOM   6530  H  HD2  A PRO B 1 86  ? 5.140   7.625   0.961   0.64 14.09  ?  309  PRO B HD2  1 
ATOM   6531  H  HD2  B PRO B 1 86  ? 5.141   6.149   1.183   0.36 12.64  ?  309  PRO B HD2  1 
ATOM   6532  H  HD3  A PRO B 1 86  ? 6.271   8.496   0.262   0.64 14.09  ?  309  PRO B HD3  1 
ATOM   6533  H  HD3  B PRO B 1 86  ? 6.539   6.905   1.166   0.36 12.64  ?  309  PRO B HD3  1 
ATOM   6534  N  N    A ASN B 1 87  ? 6.233   4.088   1.861   0.65 12.52  ?  310  ASN B N    1 
ATOM   6535  N  N    B ASN B 1 87  ? 6.117   2.014   1.186   0.35 10.97  ?  310  ASN B N    1 
ATOM   6536  C  CA   A ASN B 1 87  ? 5.995   2.674   2.126   0.65 14.08  ?  310  ASN B CA   1 
ATOM   6537  C  CA   B ASN B 1 87  ? 5.969   0.569   1.038   0.35 12.22  ?  310  ASN B CA   1 
ATOM   6538  C  C    A ASN B 1 87  ? 6.592   1.766   1.058   0.65 14.20  ?  310  ASN B C    1 
ATOM   6539  C  C    B ASN B 1 87  ? 6.599   0.020   -0.239  0.35 12.92  ?  310  ASN B C    1 
ATOM   6540  O  O    A ASN B 1 87  ? 6.409   0.548   1.131   0.65 15.30  ?  310  ASN B O    1 
ATOM   6541  O  O    B ASN B 1 87  ? 6.479   -1.182  -0.501  0.35 13.99  ?  310  ASN B O    1 
ATOM   6542  C  CB   A ASN B 1 87  ? 4.493   2.388   2.296   0.65 15.78  ?  310  ASN B CB   1 
ATOM   6543  C  CB   B ASN B 1 87  ? 4.493   0.162   1.101   0.35 12.92  ?  310  ASN B CB   1 
ATOM   6544  C  CG   A ASN B 1 87  ? 3.696   2.595   1.017   0.65 16.13  ?  310  ASN B CG   1 
ATOM   6545  C  CG   B ASN B 1 87  ? 3.686   0.691   -0.069  0.35 13.15  ?  310  ASN B CG   1 
ATOM   6546  O  OD1  A ASN B 1 87  ? 4.257   2.822   -0.058  0.65 15.54  ?  310  ASN B OD1  1 
ATOM   6547  O  OD1  B ASN B 1 87  ? 4.232   1.256   -1.018  0.35 13.15  ?  310  ASN B OD1  1 
ATOM   6548  N  ND2  A ASN B 1 87  ? 2.369   2.487   1.126   0.65 18.85  ?  310  ASN B ND2  1 
ATOM   6549  N  ND2  B ASN B 1 87  ? 2.373   0.492   -0.012  0.35 14.06  ?  310  ASN B ND2  1 
ATOM   6550  H  H    A ASN B 1 87  ? 5.602   4.476   1.423   0.64 15.03  ?  310  ASN B H    1 
ATOM   6551  H  H    B ASN B 1 87  ? 5.412   2.467   0.994   0.36 13.16  ?  310  ASN B H    1 
ATOM   6552  H  HA   A ASN B 1 87  ? 6.415   2.448   2.971   0.65 16.90  ?  310  ASN B HA   1 
ATOM   6553  H  HA   B ASN B 1 87  ? 6.417   0.151   1.789   0.35 14.66  ?  310  ASN B HA   1 
ATOM   6554  H  HB2  A ASN B 1 87  ? 4.377   1.466   2.574   0.65 18.93  ?  310  ASN B HB2  1 
ATOM   6555  H  HB2  B ASN B 1 87  ? 4.432   -0.806  1.093   0.35 15.50  ?  310  ASN B HB2  1 
ATOM   6556  H  HB3  A ASN B 1 87  ? 4.133   2.986   2.971   0.65 18.93  ?  310  ASN B HB3  1 
ATOM   6557  H  HB3  B ASN B 1 87  ? 4.103   0.512   1.917   0.35 15.50  ?  310  ASN B HB3  1 
ATOM   6558  H  HD21 A ASN B 1 87  ? 1.870   2.595   0.433   0.65 22.62  ?  310  ASN B HD21 1 
ATOM   6559  H  HD21 B ASN B 1 87  ? 1.868   0.772   -0.650  0.35 16.87  ?  310  ASN B HD21 1 
ATOM   6560  H  HD22 A ASN B 1 87  ? 2.013   2.311   1.889   0.65 22.62  ?  310  ASN B HD22 1 
ATOM   6561  H  HD22 B ASN B 1 87  ? 2.028   0.083   0.661   0.35 16.87  ?  310  ASN B HD22 1 
ATOM   6562  N  N    A GLY B 1 88  ? 7.295   2.326   0.071   0.71 14.14  ?  311  GLY B N    1 
ATOM   6563  N  N    B GLY B 1 88  ? 7.259   0.853   -1.036  0.29 13.31  ?  311  GLY B N    1 
ATOM   6564  C  CA   A GLY B 1 88  ? 8.018   1.549   -0.911  0.71 14.35  ?  311  GLY B CA   1 
ATOM   6565  C  CA   B GLY B 1 88  ? 7.908   0.384   -2.247  0.29 13.86  ?  311  GLY B CA   1 
ATOM   6566  C  C    A GLY B 1 88  ? 7.300   1.310   -2.224  0.71 14.59  ?  311  GLY B C    1 
ATOM   6567  C  C    B GLY B 1 88  ? 7.261   0.932   -3.504  0.29 14.45  ?  311  GLY B C    1 
ATOM   6568  O  O    A GLY B 1 88  ? 7.934   0.805   -3.162  0.71 15.80  ?  311  GLY B O    1 
ATOM   6569  O  O    B GLY B 1 88  ? 7.386   0.358   -4.583  0.29 14.38  ?  311  GLY B O    1 
ATOM   6570  H  H    A GLY B 1 88  ? 7.363   3.175   -0.046  0.65 16.97  ?  311  GLY B H    1 
ATOM   6571  H  H    B GLY B 1 88  ? 7.343   1.697   -0.894  0.35 15.98  ?  311  GLY B H    1 
ATOM   6572  H  HA2  A GLY B 1 88  ? 8.849   2.008   -1.112  0.71 17.22  ?  311  GLY B HA2  1 
ATOM   6573  H  HA2  B GLY B 1 88  ? 8.838   0.659   -2.238  0.29 16.63  ?  311  GLY B HA2  1 
ATOM   6574  H  HA3  A GLY B 1 88  ? 8.221   0.682   -0.527  0.71 17.22  ?  311  GLY B HA3  1 
ATOM   6575  H  HA3  B GLY B 1 88  ? 7.866   -0.584  -2.278  0.29 16.63  ?  311  GLY B HA3  1 
ATOM   6576  N  N    A THR B 1 89  ? 6.008   1.645   -2.328  0.92 15.84  ?  312  THR B N    1 
ATOM   6577  C  CA   A THR B 1 89  ? 5.274   1.454   -3.578  0.92 15.70  ?  312  THR B CA   1 
ATOM   6578  C  C    A THR B 1 89  ? 5.577   2.606   -4.552  0.92 14.00  ?  312  THR B C    1 
ATOM   6579  O  O    A THR B 1 89  ? 6.010   3.674   -4.141  0.92 12.32  ?  312  THR B O    1 
ATOM   6580  C  CB   A THR B 1 89  ? 3.768   1.394   -3.303  0.92 17.61  ?  312  THR B CB   1 
ATOM   6581  O  OG1  A THR B 1 89  ? 3.328   2.621   -2.717  0.92 15.91  ?  312  THR B OG1  1 
ATOM   6582  C  CG2  A THR B 1 89  ? 3.411   0.246   -2.344  0.92 19.11  ?  312  THR B CG2  1 
ATOM   6583  H  H    A THR B 1 89  ? 5.539   1.984   -1.691  0.71 19.01  ?  312  THR B H    1 
ATOM   6584  H  HA   A THR B 1 89  ? 5.540   0.617   -3.988  0.92 18.84  ?  312  THR B HA   1 
ATOM   6585  H  HB   A THR B 1 89  ? 3.315   1.242   -4.146  0.92 21.14  ?  312  THR B HB   1 
ATOM   6586  H  HG1  A THR B 1 89  ? 3.711   2.741   -1.979  0.92 19.09  ?  312  THR B HG1  1 
ATOM   6587  H  HG21 A THR B 1 89  ? 2.451   0.210   -2.213  0.92 22.93  ?  312  THR B HG21 1 
ATOM   6588  H  HG22 A THR B 1 89  ? 3.711   -0.600  -2.712  0.92 22.93  ?  312  THR B HG22 1 
ATOM   6589  H  HG23 A THR B 1 89  ? 3.841   0.385   -1.485  0.92 22.93  ?  312  THR B HG23 1 
ATOM   6590  N  N    . PRO B 1 90  ? 5.355   2.409   -5.854  1.00 15.27  ?  313  PRO B N    1 
ATOM   6591  C  CA   . PRO B 1 90  ? 5.653   3.482   -6.819  1.00 14.39  ?  313  PRO B CA   1 
ATOM   6592  C  C    . PRO B 1 90  ? 4.761   4.707   -6.629  1.00 13.93  ?  313  PRO B C    1 
ATOM   6593  O  O    . PRO B 1 90  ? 3.556   4.599   -6.419  1.00 14.35  ?  313  PRO B O    1 
ATOM   6594  C  CB   . PRO B 1 90  ? 5.424   2.809   -8.184  1.00 16.41  ?  313  PRO B CB   1 
ATOM   6595  C  CG   . PRO B 1 90  ? 4.591   1.628   -7.893  1.00 17.49  ?  313  PRO B CG   1 
ATOM   6596  C  CD   . PRO B 1 90  ? 4.943   1.163   -6.520  1.00 16.94  ?  313  PRO B CD   1 
ATOM   6597  H  HA   . PRO B 1 90  ? 6.579   3.758   -6.740  1.00 17.27  ?  313  PRO B HA   1 
ATOM   6598  H  HB2  . PRO B 1 90  ? 4.964   3.421   -8.781  1.00 19.69  ?  313  PRO B HB2  1 
ATOM   6599  H  HB3  . PRO B 1 90  ? 6.275   2.548   -8.570  1.00 19.69  ?  313  PRO B HB3  1 
ATOM   6600  H  HG2  . PRO B 1 90  ? 3.654   1.878   -7.935  1.00 20.99  ?  313  PRO B HG2  1 
ATOM   6601  H  HG3  . PRO B 1 90  ? 4.779   0.934   -8.544  1.00 20.99  ?  313  PRO B HG3  1 
ATOM   6602  H  HD2  . PRO B 1 90  ? 4.175   0.769   -6.078  1.00 20.33  ?  313  PRO B HD2  1 
ATOM   6603  H  HD3  . PRO B 1 90  ? 5.674   0.525   -6.546  1.00 20.33  ?  313  PRO B HD3  1 
ATOM   6604  N  N    . PHE B 1 91  ? 5.365   5.892   -6.682  1.00 13.17  ?  314  PHE B N    1 
ATOM   6605  C  CA   . PHE B 1 91  ? 4.592   7.118   -6.541  1.00 13.96  ?  314  PHE B CA   1 
ATOM   6606  C  C    . PHE B 1 91  ? 3.768   7.366   -7.805  1.00 15.64  ?  314  PHE B C    1 
ATOM   6607  O  O    . PHE B 1 91  ? 4.274   7.233   -8.924  1.00 17.13  ?  314  PHE B O    1 
ATOM   6608  C  CB   . PHE B 1 91  ? 5.538   8.290   -6.278  1.00 14.07  ?  314  PHE B CB   1 
ATOM   6609  C  CG   . PHE B 1 91  ? 4.854   9.622   -6.238  1.00 13.94  ?  314  PHE B CG   1 
ATOM   6610  C  CD1  . PHE B 1 91  ? 4.020   9.963   -5.178  1.00 14.33  ?  314  PHE B CD1  1 
ATOM   6611  C  CD2  . PHE B 1 91  ? 5.059   10.547  -7.246  1.00 13.69  ?  314  PHE B CD2  1 
ATOM   6612  C  CE1  . PHE B 1 91  ? 3.395   11.193  -5.133  1.00 14.35  ?  314  PHE B CE1  1 
ATOM   6613  C  CE2  . PHE B 1 91  ? 4.430   11.780  -7.215  1.00 14.68  ?  314  PHE B CE2  1 
ATOM   6614  C  CZ   . PHE B 1 91  ? 3.595   12.103  -6.154  1.00 14.59  ?  314  PHE B CZ   1 
ATOM   6615  H  H    . PHE B 1 91  ? 6.209   6.010   -6.798  1.00 15.80  ?  314  PHE B H    1 
ATOM   6616  H  HA   . PHE B 1 91  ? 3.980   7.042   -5.792  1.00 16.75  ?  314  PHE B HA   1 
ATOM   6617  H  HB2  . PHE B 1 91  ? 5.972   8.154   -5.421  1.00 16.88  ?  314  PHE B HB2  1 
ATOM   6618  H  HB3  . PHE B 1 91  ? 6.202   8.319   -6.984  1.00 16.88  ?  314  PHE B HB3  1 
ATOM   6619  H  HD1  . PHE B 1 91  ? 3.881   9.353   -4.489  1.00 17.20  ?  314  PHE B HD1  1 
ATOM   6620  H  HD2  . PHE B 1 91  ? 5.625   10.338  -7.953  1.00 16.42  ?  314  PHE B HD2  1 
ATOM   6621  H  HE1  . PHE B 1 91  ? 2.841   11.409  -4.418  1.00 17.22  ?  314  PHE B HE1  1 
ATOM   6622  H  HE2  . PHE B 1 91  ? 4.567   12.390  -7.904  1.00 17.62  ?  314  PHE B HE2  1 
ATOM   6623  H  HZ   . PHE B 1 91  ? 3.170   12.930  -6.131  1.00 17.52  ?  314  PHE B HZ   1 
ATOM   6624  N  N    . ASP B 1 92  ? 2.483   7.718   -7.625  1.00 16.93  ?  315  ASP B N    1 
ATOM   6625  C  CA   . ASP B 1 92  ? 1.576   8.027   -8.719  1.00 19.69  ?  315  ASP B CA   1 
ATOM   6626  C  C    . ASP B 1 92  ? 1.453   9.537   -8.837  1.00 21.44  ?  315  ASP B C    1 
ATOM   6627  O  O    . ASP B 1 92  ? 0.791   10.164  -7.994  1.00 22.16  ?  315  ASP B O    1 
ATOM   6628  C  CB   . ASP B 1 92  ? 0.206   7.405   -8.449  1.00 20.67  ?  315  ASP B CB   1 
ATOM   6629  C  CG   . ASP B 1 92  ? -0.792  7.659   -9.566  1.00 23.16  ?  315  ASP B CG   1 
ATOM   6630  O  OD1  . ASP B 1 92  ? -0.464  8.369   -10.537 1.00 22.82  ?  315  ASP B OD1  1 
ATOM   6631  O  OD2  . ASP B 1 92  ? -1.918  7.135   -9.468  1.00 25.58  -1 315  ASP B OD2  1 
ATOM   6632  H  H    . ASP B 1 92  ? 2.112   7.784   -6.852  1.00 20.32  ?  315  ASP B H    1 
ATOM   6633  H  HA   . ASP B 1 92  ? 1.927   7.674   -9.552  1.00 23.63  ?  315  ASP B HA   1 
ATOM   6634  H  HB2  . ASP B 1 92  ? 0.309   6.445   -8.354  1.00 24.81  ?  315  ASP B HB2  1 
ATOM   6635  H  HB3  . ASP B 1 92  ? -0.157  7.783   -7.633  1.00 24.81  ?  315  ASP B HB3  1 
ATOM   6636  N  N    . PRO B 1 93  ? 2.028   10.162  -9.866  1.00 22.48  ?  316  PRO B N    1 
ATOM   6637  C  CA   . PRO B 1 93  ? 1.962   11.625  -9.965  1.00 22.66  ?  316  PRO B CA   1 
ATOM   6638  C  C    . PRO B 1 93  ? 0.571   12.169  -10.247 1.00 23.28  ?  316  PRO B C    1 
ATOM   6639  O  O    . PRO B 1 93  ? 0.376   13.381  -10.121 1.00 24.04  ?  316  PRO B O    1 
ATOM   6640  C  CB   . PRO B 1 93  ? 2.914   11.935  -11.125 1.00 23.44  ?  316  PRO B CB   1 
ATOM   6641  C  CG   . PRO B 1 93  ? 2.810   10.739  -11.994 1.00 24.13  ?  316  PRO B CG   1 
ATOM   6642  C  CD   . PRO B 1 93  ? 2.683   9.567   -11.045 1.00 23.71  ?  316  PRO B CD   1 
ATOM   6643  H  HA   . PRO B 1 93  ? 2.299   12.026  -9.149  1.00 27.20  ?  316  PRO B HA   1 
ATOM   6644  H  HB2  . PRO B 1 93  ? 2.625   12.735  -11.592 1.00 28.13  ?  316  PRO B HB2  1 
ATOM   6645  H  HB3  . PRO B 1 93  ? 3.818   12.052  -10.795 1.00 28.13  ?  316  PRO B HB3  1 
ATOM   6646  H  HG2  . PRO B 1 93  ? 2.027   10.811  -12.561 1.00 28.96  ?  316  PRO B HG2  1 
ATOM   6647  H  HG3  . PRO B 1 93  ? 3.608   10.657  -12.539 1.00 28.96  ?  316  PRO B HG3  1 
ATOM   6648  H  HD2  . PRO B 1 93  ? 2.133   8.867   -11.430 1.00 28.46  ?  316  PRO B HD2  1 
ATOM   6649  H  HD3  . PRO B 1 93  ? 3.556   9.212   -10.813 1.00 28.46  ?  316  PRO B HD3  1 
ATOM   6650  N  N    . THR B 1 94  ? -0.394  11.337  -10.642 1.00 23.59  ?  317  THR B N    1 
ATOM   6651  C  CA   . THR B 1 94  ? -1.746  11.840  -10.858 1.00 25.14  ?  317  THR B CA   1 
ATOM   6652  C  C    . THR B 1 94  ? -2.499  12.056  -9.555  1.00 25.73  ?  317  THR B C    1 
ATOM   6653  O  O    . THR B 1 94  ? -3.603  12.607  -9.582  1.00 26.18  ?  317  THR B O    1 
ATOM   6654  C  CB   . THR B 1 94  ? -2.552  10.900  -11.759 1.00 25.87  ?  317  THR B CB   1 
ATOM   6655  O  OG1  . THR B 1 94  ? -2.902  9.710   -11.040 1.00 25.60  ?  317  THR B OG1  1 
ATOM   6656  C  CG2  . THR B 1 94  ? -1.748  10.529  -12.995 1.00 26.45  ?  317  THR B CG2  1 
ATOM   6657  H  H    . THR B 1 94  ? -0.292  10.496  -10.788 1.00 28.31  ?  317  THR B H    1 
ATOM   6658  H  HA   . THR B 1 94  ? -1.679  12.689  -11.323 1.00 30.17  ?  317  THR B HA   1 
ATOM   6659  H  HB   . THR B 1 94  ? -3.364  11.348  -12.044 1.00 31.04  ?  317  THR B HB   1 
ATOM   6660  H  HG1  . THR B 1 94  ? -2.206  9.301   -10.806 1.00 30.72  ?  317  THR B HG1  1 
ATOM   6661  H  HG21 . THR B 1 94  ? -2.312  10.059  -13.629 1.00 31.75  ?  317  THR B HG21 1 
ATOM   6662  H  HG22 . THR B 1 94  ? -1.400  11.330  -13.418 1.00 31.75  ?  317  THR B HG22 1 
ATOM   6663  H  HG23 . THR B 1 94  ? -1.006  9.955   -12.748 1.00 31.75  ?  317  THR B HG23 1 
ATOM   6664  N  N    . GLU B 1 95  ? -1.939  11.630  -8.425  1.00 25.17  ?  318  GLU B N    1 
ATOM   6665  C  CA   . GLU B 1 95  ? -2.547  11.937  -7.140  1.00 26.28  ?  318  GLU B CA   1 
ATOM   6666  C  C    . GLU B 1 95  ? -2.453  13.432  -6.861  1.00 23.07  ?  318  GLU B C    1 
ATOM   6667  O  O    . GLU B 1 95  ? -1.504  14.110  -7.274  1.00 22.32  ?  318  GLU B O    1 
ATOM   6668  C  CB   . GLU B 1 95  ? -1.850  11.160  -6.026  1.00 30.07  ?  318  GLU B CB   1 
ATOM   6669  C  CG   . GLU B 1 95  ? -2.088  9.662   -6.095  1.00 33.68  ?  318  GLU B CG   1 
ATOM   6670  C  CD   . GLU B 1 95  ? -3.008  9.168   -4.999  1.00 36.34  ?  318  GLU B CD   1 
ATOM   6671  O  OE1  . GLU B 1 95  ? -2.794  9.552   -3.832  1.00 37.90  ?  318  GLU B OE1  1 
ATOM   6672  O  OE2  . GLU B 1 95  ? -3.945  8.398   -5.305  1.00 37.72  -1 318  GLU B OE2  1 
ATOM   6673  H  H    . GLU B 1 95  ? -1.215  11.168  -8.379  1.00 30.20  ?  318  GLU B H    1 
ATOM   6674  H  HA   . GLU B 1 95  ? -3.482  11.679  -7.150  1.00 31.53  ?  318  GLU B HA   1 
ATOM   6675  H  HB2  . GLU B 1 95  ? -0.894  11.313  -6.088  1.00 36.08  ?  318  GLU B HB2  1 
ATOM   6676  H  HB3  . GLU B 1 95  ? -2.181  11.475  -5.170  1.00 36.08  ?  318  GLU B HB3  1 
ATOM   6677  H  HG2  . GLU B 1 95  ? -2.493  9.445   -6.949  1.00 40.42  ?  318  GLU B HG2  1 
ATOM   6678  H  HG3  . GLU B 1 95  ? -1.238  9.202   -6.005  1.00 40.42  ?  318  GLU B HG3  1 
ATOM   6679  N  N    . ASP B 1 96  ? -3.447  13.938  -6.131  1.00 21.99  ?  319  ASP B N    1 
ATOM   6680  C  CA   . ASP B 1 96  ? -3.575  15.368  -5.847  1.00 20.52  ?  319  ASP B CA   1 
ATOM   6681  C  C    . ASP B 1 96  ? -2.685  15.766  -4.666  1.00 17.88  ?  319  ASP B C    1 
ATOM   6682  O  O    . ASP B 1 96  ? -3.122  16.317  -3.657  1.00 18.93  ?  319  ASP B O    1 
ATOM   6683  C  CB   . ASP B 1 96  ? -5.042  15.699  -5.596  1.00 22.07  ?  319  ASP B CB   1 
ATOM   6684  C  CG   . ASP B 1 96  ? -5.297  17.188  -5.487  1.00 23.53  ?  319  ASP B CG   1 
ATOM   6685  O  OD1  . ASP B 1 96  ? -4.576  17.976  -6.133  1.00 23.92  ?  319  ASP B OD1  1 
ATOM   6686  O  OD2  . ASP B 1 96  ? -6.234  17.571  -4.754  1.00 25.38  -1 319  ASP B OD2  1 
ATOM   6687  H  H    . ASP B 1 96  ? -4.073  13.464  -5.782  1.00 26.39  ?  319  ASP B H    1 
ATOM   6688  H  HA   . ASP B 1 96  ? -3.274  15.879  -6.614  1.00 24.63  ?  319  ASP B HA   1 
ATOM   6689  H  HB2  . ASP B 1 96  ? -5.574  15.357  -6.331  1.00 26.49  ?  319  ASP B HB2  1 
ATOM   6690  H  HB3  . ASP B 1 96  ? -5.322  15.286  -4.764  1.00 26.49  ?  319  ASP B HB3  1 
ATOM   6691  N  N    . VAL B 1 97  ? -1.399  15.478  -4.821  1.00 15.51  ?  320  VAL B N    1 
ATOM   6692  C  CA   . VAL B 1 97  ? -0.375  15.822  -3.835  1.00 13.70  ?  320  VAL B CA   1 
ATOM   6693  C  C    . VAL B 1 97  ? 0.788   16.450  -4.587  1.00 10.72  ?  320  VAL B C    1 
ATOM   6694  O  O    . VAL B 1 97  ? 0.968   16.215  -5.792  1.00 11.25  ?  320  VAL B O    1 
ATOM   6695  C  CB   . VAL B 1 97  ? 0.096   14.585  -3.030  1.00 18.17  ?  320  VAL B CB   1 
ATOM   6696  C  CG1  . VAL B 1 97  ? -1.054  13.963  -2.251  1.00 19.31  ?  320  VAL B CG1  1 
ATOM   6697  C  CG2  . VAL B 1 97  ? 0.743   13.564  -3.946  1.00 19.16  ?  320  VAL B CG2  1 
ATOM   6698  H  H    . VAL B 1 97  ? -1.081  15.071  -5.509  1.00 18.62  ?  320  VAL B H    1 
ATOM   6699  H  HA   . VAL B 1 97  ? -0.735  16.466  -3.205  1.00 16.44  ?  320  VAL B HA   1 
ATOM   6700  H  HB   . VAL B 1 97  ? 0.760   14.876  -2.386  1.00 21.81  ?  320  VAL B HB   1 
ATOM   6701  H  HG11 . VAL B 1 97  ? -0.836  13.040  -2.050  1.00 23.17  ?  320  VAL B HG11 1 
ATOM   6702  H  HG12 . VAL B 1 97  ? -1.182  14.460  -1.428  1.00 23.17  ?  320  VAL B HG12 1 
ATOM   6703  H  HG13 . VAL B 1 97  ? -1.859  14.003  -2.791  1.00 23.17  ?  320  VAL B HG13 1 
ATOM   6704  H  HG21 . VAL B 1 97  ? 0.910   12.750  -3.445  1.00 23.00  ?  320  VAL B HG21 1 
ATOM   6705  H  HG22 . VAL B 1 97  ? 0.144   13.379  -4.687  1.00 23.00  ?  320  VAL B HG22 1 
ATOM   6706  H  HG23 . VAL B 1 97  ? 1.580   13.924  -4.279  1.00 23.00  ?  320  VAL B HG23 1 
ATOM   6707  N  N    . PRO B 1 98  ? 1.599   17.262  -3.909  1.00 8.69   ?  321  PRO B N    1 
ATOM   6708  C  CA   . PRO B 1 98  ? 2.662   17.971  -4.643  1.00 8.36   ?  321  PRO B CA   1 
ATOM   6709  C  C    . PRO B 1 98  ? 3.805   17.088  -5.069  1.00 7.91   ?  321  PRO B C    1 
ATOM   6710  O  O    . PRO B 1 98  ? 4.480   17.409  -6.062  1.00 8.17   ?  321  PRO B O    1 
ATOM   6711  C  CB   . PRO B 1 98  ? 3.144   19.016  -3.626  1.00 8.08   ?  321  PRO B CB   1 
ATOM   6712  C  CG   . PRO B 1 98  ? 2.009   19.164  -2.661  1.00 8.66   ?  321  PRO B CG   1 
ATOM   6713  C  CD   . PRO B 1 98  ? 1.408   17.806  -2.556  1.00 9.20   ?  321  PRO B CD   1 
ATOM   6714  H  HA   . PRO B 1 98  ? 2.280   18.404  -5.422  1.00 10.03  ?  321  PRO B HA   1 
ATOM   6715  H  HB2  . PRO B 1 98  ? 3.943   18.696  -3.178  1.00 9.70   ?  321  PRO B HB2  1 
ATOM   6716  H  HB3  . PRO B 1 98  ? 3.330   19.855  -4.077  1.00 9.70   ?  321  PRO B HB3  1 
ATOM   6717  H  HG2  . PRO B 1 98  ? 2.344   19.461  -1.800  1.00 10.40  ?  321  PRO B HG2  1 
ATOM   6718  H  HG3  . PRO B 1 98  ? 1.365   19.802  -3.004  1.00 10.40  ?  321  PRO B HG3  1 
ATOM   6719  H  HD2  . PRO B 1 98  ? 1.875   17.269  -1.897  1.00 11.04  ?  321  PRO B HD2  1 
ATOM   6720  H  HD3  . PRO B 1 98  ? 0.465   17.859  -2.333  1.00 11.04  ?  321  PRO B HD3  1 
ATOM   6721  N  N    . ALA B 1 99  ? 4.051   15.998  -4.341  1.00 7.49   ?  322  ALA B N    1 
ATOM   6722  C  CA   . ALA B 1 99  ? 5.254   15.194  -4.433  1.00 7.44   ?  322  ALA B CA   1 
ATOM   6723  C  C    . ALA B 1 99  ? 5.075   14.049  -3.443  1.00 7.24   ?  322  ALA B C    1 
ATOM   6724  O  O    . ALA B 1 99  ? 4.149   14.085  -2.617  1.00 7.13   ?  322  ALA B O    1 
ATOM   6725  C  CB   . ALA B 1 99  ? 6.469   16.040  -4.054  1.00 7.98   ?  322  ALA B CB   1 
ATOM   6726  H  H    . ALA B 1 99  ? 3.501   15.692  -3.755  1.00 8.99   ?  322  ALA B H    1 
ATOM   6727  H  HA   . ALA B 1 99  ? 5.401   14.851  -5.328  1.00 8.93   ?  322  ALA B HA   1 
ATOM   6728  H  HB1  . ALA B 1 99  ? 7.268   15.494  -4.122  1.00 9.58   ?  322  ALA B HB1  1 
ATOM   6729  H  HB2  . ALA B 1 99  ? 6.531   16.794  -4.662  1.00 9.58   ?  322  ALA B HB2  1 
ATOM   6730  H  HB3  . ALA B 1 99  ? 6.362   16.357  -3.144  1.00 9.58   ?  322  ALA B HB3  1 
ATOM   6731  N  N    . PRO B 1 100 ? 5.958   13.052  -3.447  1.00 6.99   ?  323  PRO B N    1 
ATOM   6732  C  CA   . PRO B 1 100 ? 5.895   12.019  -2.408  1.00 6.91   ?  323  PRO B CA   1 
ATOM   6733  C  C    . PRO B 1 100 ? 5.881   12.637  -1.011  1.00 6.13   ?  323  PRO B C    1 
ATOM   6734  O  O    . PRO B 1 100 ? 6.539   13.646  -0.742  1.00 6.56   ?  323  PRO B O    1 
ATOM   6735  C  CB   . PRO B 1 100 ? 7.147   11.180  -2.671  1.00 7.70   ?  323  PRO B CB   1 
ATOM   6736  C  CG   . PRO B 1 100 ? 7.355   11.323  -4.158  1.00 7.58   ?  323  PRO B CG   1 
ATOM   6737  C  CD   . PRO B 1 100 ? 7.021   12.766  -4.425  1.00 7.54   ?  323  PRO B CD   1 
ATOM   6738  H  HA   . PRO B 1 100 ? 5.109   11.461  -2.515  1.00 8.30   ?  323  PRO B HA   1 
ATOM   6739  H  HB2  . PRO B 1 100 ? 7.900   11.534  -2.173  1.00 9.24   ?  323  PRO B HB2  1 
ATOM   6740  H  HB3  . PRO B 1 100 ? 6.991   10.256  -2.424  1.00 9.24   ?  323  PRO B HB3  1 
ATOM   6741  H  HG2  . PRO B 1 100 ? 8.277   11.127  -4.389  1.00 9.10   ?  323  PRO B HG2  1 
ATOM   6742  H  HG3  . PRO B 1 100 ? 6.759   10.729  -4.640  1.00 9.10   ?  323  PRO B HG3  1 
ATOM   6743  H  HD2  . PRO B 1 100 ? 7.793   13.333  -4.272  1.00 9.05   ?  323  PRO B HD2  1 
ATOM   6744  H  HD3  . PRO B 1 100 ? 6.697   12.883  -5.332  1.00 9.05   ?  323  PRO B HD3  1 
ATOM   6745  N  N    . LEU B 1 101 ? 5.116   12.033  -0.116  1.00 6.24   ?  324  LEU B N    1 
ATOM   6746  C  CA   . LEU B 1 101 ? 4.958   12.620  1.207   1.00 6.13   ?  324  LEU B CA   1 
ATOM   6747  C  C    . LEU B 1 101 ? 6.304   12.701  1.914   1.00 6.65   ?  324  LEU B C    1 
ATOM   6748  O  O    . LEU B 1 101 ? 7.156   11.824  1.782   1.00 7.58   ?  324  LEU B O    1 
ATOM   6749  C  CB   . LEU B 1 101 ? 3.939   11.836  2.023   1.00 7.50   ?  324  LEU B CB   1 
ATOM   6750  C  CG   . LEU B 1 101 ? 2.540   11.711  1.404   1.00 7.52   ?  324  LEU B CG   1 
ATOM   6751  C  CD1  . LEU B 1 101 ? 1.579   11.083  2.412   1.00 8.26   ?  324  LEU B CD1  1 
ATOM   6752  C  CD2  . LEU B 1 101 ? 1.994   13.046  0.892   1.00 8.29   ?  324  LEU B CD2  1 
ATOM   6753  H  H    . LEU B 1 101 ? 4.687   11.299  -0.244  1.00 7.49   ?  324  LEU B H    1 
ATOM   6754  H  HA   . LEU B 1 101 ? 4.616   13.525  1.127   1.00 7.36   ?  324  LEU B HA   1 
ATOM   6755  H  HB2  . LEU B 1 101 ? 4.280   10.937  2.149   1.00 9.01   ?  324  LEU B HB2  1 
ATOM   6756  H  HB3  . LEU B 1 101 ? 3.836   12.275  2.882   1.00 9.01   ?  324  LEU B HB3  1 
ATOM   6757  H  HG   . LEU B 1 101 ? 2.609   11.134  0.628   1.00 9.02   ?  324  LEU B HG   1 
ATOM   6758  H  HD11 . LEU B 1 101 ? 0.750   10.860  1.961   1.00 9.91   ?  324  LEU B HD11 1 
ATOM   6759  H  HD12 . LEU B 1 101 ? 1.984   10.280  2.777   1.00 9.91   ?  324  LEU B HD12 1 
ATOM   6760  H  HD13 . LEU B 1 101 ? 1.408   11.719  3.124   1.00 9.91   ?  324  LEU B HD13 1 
ATOM   6761  H  HD21 . LEU B 1 101 ? 1.071   12.926  0.619   1.00 9.95   ?  324  LEU B HD21 1 
ATOM   6762  H  HD22 . LEU B 1 101 ? 2.046   13.702  1.605   1.00 9.95   ?  324  LEU B HD22 1 
ATOM   6763  H  HD23 . LEU B 1 101 ? 2.528   13.336  0.136   1.00 9.95   ?  324  LEU B HD23 1 
ATOM   6764  N  N    . GLY B 1 102 ? 6.513   13.810  2.629   1.00 5.67   ?  325  GLY B N    1 
ATOM   6765  C  CA   . GLY B 1 102 ? 7.764   14.080  3.302   1.00 5.84   ?  325  GLY B CA   1 
ATOM   6766  C  C    . GLY B 1 102 ? 8.821   14.781  2.470   1.00 5.75   ?  325  GLY B C    1 
ATOM   6767  O  O    . GLY B 1 102 ? 9.833   15.200  3.037   1.00 6.12   ?  325  GLY B O    1 
ATOM   6768  H  H    . GLY B 1 102 ? 5.926   14.429  2.736   1.00 6.81   ?  325  GLY B H    1 
ATOM   6769  H  HA2  . GLY B 1 102 ? 7.584   14.637  4.075   1.00 7.01   ?  325  GLY B HA2  1 
ATOM   6770  H  HA3  . GLY B 1 102 ? 8.140   13.237  3.601   1.00 7.01   ?  325  GLY B HA3  1 
ATOM   6771  N  N    . THR B 1 103 ? 8.620   14.924  1.156   1.00 5.55   ?  326  THR B N    1 
ATOM   6772  C  CA   . THR B 1 103 ? 9.571   15.658  0.324   1.00 6.13   ?  326  THR B CA   1 
ATOM   6773  C  C    . THR B 1 103 ? 9.819   17.032  0.943   1.00 5.53   ?  326  THR B C    1 
ATOM   6774  O  O    . THR B 1 103 ? 8.877   17.649  1.460   1.00 5.67   ?  326  THR B O    1 
ATOM   6775  C  CB   . THR B 1 103 ? 8.971   15.829  -1.082  1.00 6.65   ?  326  THR B CB   1 
ATOM   6776  O  OG1  . THR B 1 103 ? 8.848   14.553  -1.728  1.00 7.34   ?  326  THR B OG1  1 
ATOM   6777  C  CG2  . THR B 1 103 ? 9.805   16.736  -1.972  1.00 6.92   ?  326  THR B CG2  1 
ATOM   6778  H  H    . THR B 1 103 ? 7.946   14.607  0.727   1.00 6.66   ?  326  THR B H    1 
ATOM   6779  H  HA   . THR B 1 103 ? 10.415  15.183  0.260   1.00 7.35   ?  326  THR B HA   1 
ATOM   6780  H  HB   . THR B 1 103 ? 8.100   16.241  -0.972  1.00 7.99   ?  326  THR B HB   1 
ATOM   6781  H  HG1  . THR B 1 103 ? 8.310   14.067  -1.304  1.00 8.81   ?  326  THR B HG1  1 
ATOM   6782  H  HG21 . THR B 1 103 ? 9.372   16.844  -2.833  1.00 8.30   ?  326  THR B HG21 1 
ATOM   6783  H  HG22 . THR B 1 103 ? 9.903   17.608  -1.557  1.00 8.30   ?  326  THR B HG22 1 
ATOM   6784  H  HG23 . THR B 1 103 ? 10.685  16.351  -2.107  1.00 8.30   ?  326  THR B HG23 1 
ATOM   6785  N  N    . PRO B 1 104 ? 11.058  17.536  0.935   1.00 5.85   ?  327  PRO B N    1 
ATOM   6786  C  CA   A PRO B 1 104 ? 11.310  18.895  1.435   0.55 5.76   ?  327  PRO B CA   1 
ATOM   6787  C  CA   B PRO B 1 104 ? 11.290  18.891  1.455   0.45 5.82   ?  327  PRO B CA   1 
ATOM   6788  C  C    . PRO B 1 104 ? 10.418  19.931  0.761   1.00 5.65   ?  327  PRO B C    1 
ATOM   6789  O  O    . PRO B 1 104 ? 10.108  19.830  -0.427  1.00 6.20   ?  327  PRO B O    1 
ATOM   6790  C  CB   A PRO B 1 104 ? 12.782  19.135  1.078   0.55 6.29   ?  327  PRO B CB   1 
ATOM   6791  C  CB   B PRO B 1 104 ? 12.781  19.139  1.180   0.45 6.30   ?  327  PRO B CB   1 
ATOM   6792  C  CG   A PRO B 1 104 ? 13.355  17.784  0.974   0.55 6.31   ?  327  PRO B CG   1 
ATOM   6793  C  CG   B PRO B 1 104 ? 13.160  18.149  0.142   0.45 6.55   ?  327  PRO B CG   1 
ATOM   6794  C  CD   A PRO B 1 104 ? 12.285  16.907  0.420   0.55 6.56   ?  327  PRO B CD   1 
ATOM   6795  C  CD   B PRO B 1 104 ? 12.291  16.948  0.380   0.45 6.56   ?  327  PRO B CD   1 
ATOM   6796  H  HA   A PRO B 1 104 ? 11.179  18.926  2.395   0.55 6.92   ?  327  PRO B HA   1 
ATOM   6797  H  HA   B PRO B 1 104 ? 11.122  18.914  2.410   0.45 6.99   ?  327  PRO B HA   1 
ATOM   6798  H  HB2  A PRO B 1 104 ? 12.847  19.609  0.233   0.55 7.55   ?  327  PRO B HB2  1 
ATOM   6799  H  HB2  B PRO B 1 104 ? 12.909  20.045  0.857   0.45 7.56   ?  327  PRO B HB2  1 
ATOM   6800  H  HB3  A PRO B 1 104 ? 13.216  19.646  1.779   0.55 7.55   ?  327  PRO B HB3  1 
ATOM   6801  H  HB3  B PRO B 1 104 ? 13.292  19.001  1.992   0.45 7.56   ?  327  PRO B HB3  1 
ATOM   6802  H  HG2  A PRO B 1 104 ? 14.122  17.802  0.380   0.55 7.58   ?  327  PRO B HG2  1 
ATOM   6803  H  HG2  B PRO B 1 104 ? 12.997  18.521  -0.739  0.45 7.86   ?  327  PRO B HG2  1 
ATOM   6804  H  HG3  A PRO B 1 104 ? 13.624  17.477  1.854   0.55 7.58   ?  327  PRO B HG3  1 
ATOM   6805  H  HG3  B PRO B 1 104 ? 14.097  17.919  0.236   0.45 7.86   ?  327  PRO B HG3  1 
ATOM   6806  H  HD2  A PRO B 1 104 ? 12.298  16.913  -0.550  0.55 7.87   ?  327  PRO B HD2  1 
ATOM   6807  H  HD2  B PRO B 1 104 ? 12.109  16.482  -0.451  0.45 7.87   ?  327  PRO B HD2  1 
ATOM   6808  H  HD3  A PRO B 1 104 ? 12.375  15.999  0.747   0.55 7.87   ?  327  PRO B HD3  1 
ATOM   6809  H  HD3  B PRO B 1 104 ? 12.703  16.343  1.017   0.45 7.87   ?  327  PRO B HD3  1 
ATOM   6810  N  N    . ASP B 1 105 ? 10.054  20.971  1.527   1.00 5.49   ?  328  ASP B N    1 
ATOM   6811  C  CA   . ASP B 1 105 ? 9.172   22.042  1.077   1.00 5.75   ?  328  ASP B CA   1 
ATOM   6812  C  C    . ASP B 1 105 ? 9.882   23.390  1.025   1.00 5.90   ?  328  ASP B C    1 
ATOM   6813  O  O    . ASP B 1 105 ? 9.258   24.428  1.201   1.00 6.67   ?  328  ASP B O    1 
ATOM   6814  C  CB   . ASP B 1 105 ? 7.904   22.123  1.930   1.00 4.95   ?  328  ASP B CB   1 
ATOM   6815  C  CG   . ASP B 1 105 ? 8.171   22.478  3.378   1.00 5.67   ?  328  ASP B CG   1 
ATOM   6816  O  OD1  . ASP B 1 105 ? 9.350   22.625  3.773   1.00 6.05   ?  328  ASP B OD1  1 
ATOM   6817  O  OD2  . ASP B 1 105 ? 7.164   22.600  4.122   1.00 6.16   -1 328  ASP B OD2  1 
ATOM   6818  H  H    . ASP B 1 105 ? 10.319  21.075  2.339   1.00 6.59   ?  328  ASP B H    1 
ATOM   6819  H  HA   . ASP B 1 105 ? 8.896   21.829  0.172   1.00 6.90   ?  328  ASP B HA   1 
ATOM   6820  H  HB2  . ASP B 1 105 ? 7.322   22.805  1.560   1.00 5.94   ?  328  ASP B HB2  1 
ATOM   6821  H  HB3  . ASP B 1 105 ? 7.459   21.262  1.912   1.00 5.94   ?  328  ASP B HB3  1 
ATOM   6822  N  N    . PHE B 1 106 ? 11.183  23.384  0.742   1.00 5.58   ?  329  PHE B N    1 
ATOM   6823  C  CA   . PHE B 1 106 ? 11.964  24.608  0.717   1.00 5.67   ?  329  PHE B CA   1 
ATOM   6824  C  C    . PHE B 1 106 ? 13.024  24.487  -0.368  1.00 5.86   ?  329  PHE B C    1 
ATOM   6825  O  O    . PHE B 1 106 ? 13.393  23.385  -0.770  1.00 6.58   ?  329  PHE B O    1 
ATOM   6826  C  CB   . PHE B 1 106 ? 12.644  24.872  2.068   1.00 6.24   ?  329  PHE B CB   1 
ATOM   6827  C  CG   . PHE B 1 106 ? 13.427  23.698  2.600   1.00 6.12   ?  329  PHE B CG   1 
ATOM   6828  C  CD1  . PHE B 1 106 ? 14.718  23.426  2.178   1.00 7.57   ?  329  PHE B CD1  1 
ATOM   6829  C  CD2  . PHE B 1 106 ? 12.849  22.850  3.550   1.00 6.02   ?  329  PHE B CD2  1 
ATOM   6830  C  CE1  . PHE B 1 106 ? 15.417  22.341  2.688   1.00 8.90   ?  329  PHE B CE1  1 
ATOM   6831  C  CE2  . PHE B 1 106 ? 13.541  21.770  4.052   1.00 7.06   ?  329  PHE B CE2  1 
ATOM   6832  C  CZ   . PHE B 1 106 ? 14.826  21.510  3.605   1.00 7.91   ?  329  PHE B CZ   1 
ATOM   6833  H  H    . PHE B 1 106 ? 11.636  22.676  0.559   1.00 6.70   ?  329  PHE B H    1 
ATOM   6834  H  HA   . PHE B 1 106 ? 11.379  25.354  0.511   1.00 6.80   ?  329  PHE B HA   1 
ATOM   6835  H  HB2  . PHE B 1 106 ? 13.260  25.615  1.967   1.00 7.49   ?  329  PHE B HB2  1 
ATOM   6836  H  HB3  . PHE B 1 106 ? 11.963  25.092  2.722   1.00 7.49   ?  329  PHE B HB3  1 
ATOM   6837  H  HD1  . PHE B 1 106 ? 15.121  23.977  1.546   1.00 9.09   ?  329  PHE B HD1  1 
ATOM   6838  H  HD2  . PHE B 1 106 ? 11.985  23.019  3.849   1.00 7.23   ?  329  PHE B HD2  1 
ATOM   6839  H  HE1  . PHE B 1 106 ? 16.288  22.176  2.407   1.00 10.68  ?  329  PHE B HE1  1 
ATOM   6840  H  HE2  . PHE B 1 106 ? 13.147  21.217  4.687   1.00 8.48   ?  329  PHE B HE2  1 
ATOM   6841  H  HZ   . PHE B 1 106 ? 15.290  20.772  3.929   1.00 9.50   ?  329  PHE B HZ   1 
ATOM   6842  N  N    . ARG B 1 107 ? 13.531  25.632  -0.811  1.00 6.31   ?  330  ARG B N    1 
ATOM   6843  C  CA   . ARG B 1 107 ? 14.701  25.707  -1.673  1.00 6.19   ?  330  ARG B CA   1 
ATOM   6844  C  C    . ARG B 1 107 ? 15.945  25.692  -0.797  1.00 6.10   ?  330  ARG B C    1 
ATOM   6845  O  O    . ARG B 1 107 ? 16.065  26.482  0.137   1.00 7.76   ?  330  ARG B O    1 
ATOM   6846  C  CB   . ARG B 1 107 ? 14.640  26.989  -2.505  1.00 7.94   ?  330  ARG B CB   1 
ATOM   6847  C  CG   . ARG B 1 107 ? 13.569  26.946  -3.586  1.00 9.17   ?  330  ARG B CG   1 
ATOM   6848  C  CD   . ARG B 1 107 ? 13.509  28.201  -4.478  1.00 12.68  ?  330  ARG B CD   1 
ATOM   6849  N  NE   . ARG B 1 107 ? 14.756  28.499  -5.188  1.00 16.57  ?  330  ARG B NE   1 
ATOM   6850  C  CZ   . ARG B 1 107 ? 15.065  28.102  -6.421  1.00 17.87  ?  330  ARG B CZ   1 
ATOM   6851  N  NH1  . ARG B 1 107 ? 14.246  27.334  -7.133  1.00 17.65  ?  330  ARG B NH1  1 
ATOM   6852  N  NH2  . ARG B 1 107 ? 16.223  28.492  -6.956  1.00 18.33  ?  330  ARG B NH2  1 
ATOM   6853  H  H    . ARG B 1 107 ? 13.203  26.404  -0.619  1.00 7.58   ?  330  ARG B H    1 
ATOM   6854  H  HA   . ARG B 1 107 ? 14.739  24.951  -2.280  1.00 7.42   ?  330  ARG B HA   1 
ATOM   6855  H  HB2  . ARG B 1 107 ? 14.444  27.736  -1.918  1.00 9.53   ?  330  ARG B HB2  1 
ATOM   6856  H  HB3  . ARG B 1 107 ? 15.497  27.124  -2.938  1.00 9.53   ?  330  ARG B HB3  1 
ATOM   6857  H  HG2  . ARG B 1 107 ? 13.742  26.185  -4.163  1.00 11.01  ?  330  ARG B HG2  1 
ATOM   6858  H  HG3  . ARG B 1 107 ? 12.703  26.849  -3.160  1.00 11.01  ?  330  ARG B HG3  1 
ATOM   6859  H  HD2  . ARG B 1 107 ? 12.816  28.075  -5.145  1.00 15.21  ?  330  ARG B HD2  1 
ATOM   6860  H  HD3  . ARG B 1 107 ? 13.298  28.967  -3.922  1.00 15.21  ?  330  ARG B HD3  1 
ATOM   6861  H  HE   . ARG B 1 107 ? 15.341  28.972  -4.771  1.00 19.88  ?  330  ARG B HE   1 
ATOM   6862  H  HH11 . ARG B 1 107 ? 13.496  27.080  -6.799  1.00 21.18  ?  330  ARG B HH11 1 
ATOM   6863  H  HH12 . ARG B 1 107 ? 14.468  27.091  -7.927  1.00 21.18  ?  330  ARG B HH12 1 
ATOM   6864  H  HH21 . ARG B 1 107 ? 16.758  28.991  -6.505  1.00 22.00  ?  330  ARG B HH21 1 
ATOM   6865  H  HH22 . ARG B 1 107 ? 16.435  28.243  -7.751  1.00 22.00  ?  330  ARG B HH22 1 
ATOM   6866  N  N    . GLY B 1 108 ? 16.850  24.761  -1.065  1.00 6.09   ?  331  GLY B N    1 
ATOM   6867  C  CA   . GLY B 1 108 ? 18.060  24.671  -0.273  1.00 6.96   ?  331  GLY B CA   1 
ATOM   6868  C  C    . GLY B 1 108 ? 18.885  23.478  -0.702  1.00 6.04   ?  331  GLY B C    1 
ATOM   6869  O  O    . GLY B 1 108 ? 18.510  22.706  -1.593  1.00 7.05   ?  331  GLY B O    1 
ATOM   6870  H  H    . GLY B 1 108 ? 16.786  24.178  -1.694  1.00 7.31   ?  331  GLY B H    1 
ATOM   6871  H  HA2  . GLY B 1 108 ? 18.589  25.476  -0.388  1.00 8.36   ?  331  GLY B HA2  1 
ATOM   6872  H  HA3  . GLY B 1 108 ? 17.832  24.575  0.665   1.00 8.36   ?  331  GLY B HA3  1 
ATOM   6873  N  N    . GLN B 1 109 ? 19.994  23.311  -0.010  1.00 5.70   ?  332  GLN B N    1 
ATOM   6874  C  CA   . GLN B 1 109 ? 20.934  22.222  -0.244  1.00 6.08   ?  332  GLN B CA   1 
ATOM   6875  C  C    . GLN B 1 109 ? 20.812  21.256  0.932   1.00 5.71   ?  332  GLN B C    1 
ATOM   6876  O  O    . GLN B 1 109 ? 21.386  21.471  1.996   1.00 6.23   ?  332  GLN B O    1 
ATOM   6877  C  CB   . GLN B 1 109 ? 22.338  22.785  -0.399  1.00 7.07   ?  332  GLN B CB   1 
ATOM   6878  C  CG   . GLN B 1 109 ? 22.492  23.765  -1.545  1.00 8.28   ?  332  GLN B CG   1 
ATOM   6879  C  CD   . GLN B 1 109 ? 22.193  23.111  -2.852  1.00 10.45  ?  332  GLN B CD   1 
ATOM   6880  O  OE1  . GLN B 1 109 ? 22.764  22.088  -3.184  1.00 11.93  ?  332  GLN B OE1  1 
ATOM   6881  N  NE2  . GLN B 1 109 ? 21.222  23.640  -3.565  1.00 13.49  ?  332  GLN B NE2  1 
ATOM   6882  H  H    . GLN B 1 109 ? 20.238  23.835  0.628   1.00 6.84   ?  332  GLN B H    1 
ATOM   6883  H  HA   . GLN B 1 109 ? 20.710  21.734  -1.051  1.00 7.29   ?  332  GLN B HA   1 
ATOM   6884  H  HB2  . GLN B 1 109 ? 22.579  23.249  0.419   1.00 8.48   ?  332  GLN B HB2  1 
ATOM   6885  H  HB3  . GLN B 1 109 ? 22.952  22.050  -0.556  1.00 8.48   ?  332  GLN B HB3  1 
ATOM   6886  H  HG2  . GLN B 1 109 ? 21.874  24.504  -1.423  1.00 9.94   ?  332  GLN B HG2  1 
ATOM   6887  H  HG3  . GLN B 1 109 ? 23.403  24.096  -1.568  1.00 9.94   ?  332  GLN B HG3  1 
ATOM   6888  H  HE21 . GLN B 1 109 ? 20.797  24.326  -3.270  1.00 16.18  ?  332  GLN B HE21 1 
ATOM   6889  H  HE22 . GLN B 1 109 ? 21.013  23.298  -4.326  1.00 16.18  ?  332  GLN B HE22 1 
ATOM   6890  N  N    . LEU B 1 110 ? 20.030  20.203  0.752   1.00 5.59   ?  333  LEU B N    1 
ATOM   6891  C  CA   . LEU B 1 110 ? 19.700  19.289  1.835   1.00 4.88   ?  333  LEU B CA   1 
ATOM   6892  C  C    . LEU B 1 110 ? 20.850  18.305  2.042   1.00 5.17   ?  333  LEU B C    1 
ATOM   6893  O  O    . LEU B 1 110 ? 21.179  17.536  1.136   1.00 6.54   ?  333  LEU B O    1 
ATOM   6894  C  CB   . LEU B 1 110 ? 18.399  18.575  1.487   1.00 6.08   ?  333  LEU B CB   1 
ATOM   6895  C  CG   . LEU B 1 110 ? 17.884  17.542  2.489   1.00 6.40   ?  333  LEU B CG   1 
ATOM   6896  C  CD1  . LEU B 1 110 ? 17.593  18.170  3.836   1.00 7.27   ?  333  LEU B CD1  1 
ATOM   6897  C  CD2  . LEU B 1 110 ? 16.644  16.847  1.930   1.00 7.29   ?  333  LEU B CD2  1 
ATOM   6898  H  H    . LEU B 1 110 ? 19.672  19.991  -0.000  1.00 6.71   ?  333  LEU B H    1 
ATOM   6899  H  HA   . LEU B 1 110 ? 19.581  19.768  2.670   1.00 5.86   ?  333  LEU B HA   1 
ATOM   6900  H  HB2  . LEU B 1 110 ? 17.706  19.247  1.393   1.00 7.30   ?  333  LEU B HB2  1 
ATOM   6901  H  HB3  . LEU B 1 110 ? 18.529  18.112  0.645   1.00 7.30   ?  333  LEU B HB3  1 
ATOM   6902  H  HG   . LEU B 1 110 ? 18.574  16.874  2.632   1.00 7.69   ?  333  LEU B HG   1 
ATOM   6903  H  HD11 . LEU B 1 110 ? 17.209  17.499  4.421   1.00 8.73   ?  333  LEU B HD11 1 
ATOM   6904  H  HD12 . LEU B 1 110 ? 18.421  18.505  4.214   1.00 8.73   ?  333  LEU B HD12 1 
ATOM   6905  H  HD13 . LEU B 1 110 ? 16.966  18.900  3.715   1.00 8.73   ?  333  LEU B HD13 1 
ATOM   6906  H  HD21 . LEU B 1 110 ? 16.326  16.199  2.579   1.00 8.75   ?  333  LEU B HD21 1 
ATOM   6907  H  HD22 . LEU B 1 110 ? 15.958  17.512  1.763   1.00 8.75   ?  333  LEU B HD22 1 
ATOM   6908  H  HD23 . LEU B 1 110 ? 16.879  16.399  1.103   1.00 8.75   ?  333  LEU B HD23 1 
ATOM   6909  N  N    . TYR B 1 111 ? 21.445  18.316  3.233   1.00 5.09   ?  334  TYR B N    1 
ATOM   6910  C  CA   . TYR B 1 111 ? 22.599  17.495  3.569   1.00 5.04   ?  334  TYR B CA   1 
ATOM   6911  C  C    . TYR B 1 111 ? 22.171  16.316  4.431   1.00 4.53   ?  334  TYR B C    1 
ATOM   6912  O  O    . TYR B 1 111 ? 21.396  16.471  5.375   1.00 5.05   ?  334  TYR B O    1 
ATOM   6913  C  CB   . TYR B 1 111 ? 23.629  18.366  4.316   1.00 6.04   ?  334  TYR B CB   1 
ATOM   6914  C  CG   . TYR B 1 111 ? 24.680  17.592  5.080   1.00 5.91   ?  334  TYR B CG   1 
ATOM   6915  C  CD1  . TYR B 1 111 ? 25.608  16.804  4.425   1.00 5.61   ?  334  TYR B CD1  1 
ATOM   6916  C  CD2  . TYR B 1 111 ? 24.752  17.659  6.460   1.00 5.97   ?  334  TYR B CD2  1 
ATOM   6917  C  CE1  . TYR B 1 111 ? 26.566  16.096  5.134   1.00 6.27   ?  334  TYR B CE1  1 
ATOM   6918  C  CE2  . TYR B 1 111 ? 25.693  16.959  7.173   1.00 6.14   ?  334  TYR B CE2  1 
ATOM   6919  C  CZ   . TYR B 1 111 ? 26.608  16.196  6.513   1.00 6.04   ?  334  TYR B CZ   1 
ATOM   6920  O  OH   . TYR B 1 111 ? 27.548  15.505  7.243   1.00 6.72   ?  334  TYR B OH   1 
ATOM   6921  H  H    . TYR B 1 111 ? 21.185  18.811  3.887   1.00 6.12   ?  334  TYR B H    1 
ATOM   6922  H  HA   . TYR B 1 111 ? 23.008  17.130  2.769   1.00 6.04   ?  334  TYR B HA   1 
ATOM   6923  H  HB2  . TYR B 1 111 ? 24.089  18.922  3.668   1.00 7.26   ?  334  TYR B HB2  1 
ATOM   6924  H  HB3  . TYR B 1 111 ? 23.156  18.922  4.954   1.00 7.26   ?  334  TYR B HB3  1 
ATOM   6925  H  HD1  . TYR B 1 111 ? 25.590  16.749  3.497   1.00 6.74   ?  334  TYR B HD1  1 
ATOM   6926  H  HD2  . TYR B 1 111 ? 24.145  18.194  6.918   1.00 7.16   ?  334  TYR B HD2  1 
ATOM   6927  H  HE1  . TYR B 1 111 ? 27.177  15.557  4.685   1.00 7.53   ?  334  TYR B HE1  1 
ATOM   6928  H  HE2  . TYR B 1 111 ? 25.705  17.005  8.102   1.00 7.37   ?  334  TYR B HE2  1 
ATOM   6929  H  HH   . TYR B 1 111 ? 28.087  15.120  6.726   1.00 8.07   ?  334  TYR B HH   1 
ATOM   6930  N  N    . GLY B 1 112 ? 22.694  15.136  4.125   1.00 4.70   ?  335  GLY B N    1 
ATOM   6931  C  CA   . GLY B 1 112 ? 22.372  13.966  4.902   1.00 5.51   ?  335  GLY B CA   1 
ATOM   6932  C  C    . GLY B 1 112 ? 23.207  12.791  4.489   1.00 4.94   ?  335  GLY B C    1 
ATOM   6933  O  O    . GLY B 1 112 ? 24.328  12.966  3.978   1.00 5.27   ?  335  GLY B O    1 
ATOM   6934  H  H    . GLY B 1 112 ? 23.235  14.995  3.472   1.00 5.64   ?  335  GLY B H    1 
ATOM   6935  H  HA2  . GLY B 1 112 ? 22.533  14.146  5.842   1.00 6.61   ?  335  GLY B HA2  1 
ATOM   6936  H  HA3  . GLY B 1 112 ? 21.437  13.742  4.780   1.00 6.61   ?  335  GLY B HA3  1 
ATOM   6937  N  N    . VAL B 1 113 ? 22.686  11.594  4.729   1.00 5.25   ?  336  VAL B N    1 
ATOM   6938  C  CA   . VAL B 1 113 ? 23.398  10.350  4.469   1.00 5.13   ?  336  VAL B CA   1 
ATOM   6939  C  C    . VAL B 1 113 ? 22.531  9.450   3.606   1.00 5.04   ?  336  VAL B C    1 
ATOM   6940  O  O    . VAL B 1 113 ? 21.359  9.224   3.927   1.00 5.71   ?  336  VAL B O    1 
ATOM   6941  C  CB   . VAL B 1 113 ? 23.804  9.636   5.774   1.00 6.10   ?  336  VAL B CB   1 
ATOM   6942  C  CG1  . VAL B 1 113 ? 24.308  8.241   5.500   1.00 6.87   ?  336  VAL B CG1  1 
ATOM   6943  C  CG2  . VAL B 1 113 ? 24.863  10.456  6.488   1.00 8.52   ?  336  VAL B CG2  1 
ATOM   6944  H  H    . VAL B 1 113 ? 21.898  11.474  5.052   1.00 6.30   ?  336  VAL B H    1 
ATOM   6945  H  HA   . VAL B 1 113 ? 24.203  10.550  3.966   1.00 6.15   ?  336  VAL B HA   1 
ATOM   6946  H  HB   . VAL B 1 113 ? 23.025  9.552   6.346   1.00 7.33   ?  336  VAL B HB   1 
ATOM   6947  H  HG11 . VAL B 1 113 ? 24.755  7.906   6.293   1.00 8.24   ?  336  VAL B HG11 1 
ATOM   6948  H  HG12 . VAL B 1 113 ? 23.556  7.671   5.279   1.00 8.24   ?  336  VAL B HG12 1 
ATOM   6949  H  HG13 . VAL B 1 113 ? 24.931  8.271   4.757   1.00 8.24   ?  336  VAL B HG13 1 
ATOM   6950  H  HG21 . VAL B 1 113 ? 25.100  10.013  7.317   1.00 10.23  ?  336  VAL B HG21 1 
ATOM   6951  H  HG22 . VAL B 1 113 ? 25.643  10.530  5.917   1.00 10.23  ?  336  VAL B HG22 1 
ATOM   6952  H  HG23 . VAL B 1 113 ? 24.505  11.338  6.675   1.00 10.23  ?  336  VAL B HG23 1 
ATOM   6953  N  N    . ILE B 1 114 ? 23.099  8.942   2.514   1.00 4.82   ?  337  ILE B N    1 
ATOM   6954  C  CA   . ILE B 1 114 ? 22.473  7.910   1.705   1.00 5.11   ?  337  ILE B CA   1 
ATOM   6955  C  C    . ILE B 1 114 ? 23.002  6.557   2.158   1.00 4.87   ?  337  ILE B C    1 
ATOM   6956  O  O    . ILE B 1 114 ? 24.219  6.342   2.237   1.00 5.45   ?  337  ILE B O    1 
ATOM   6957  C  CB   . ILE B 1 114 ? 22.678  8.161   0.194   1.00 6.05   ?  337  ILE B CB   1 
ATOM   6958  C  CG1  . ILE B 1 114 ? 22.064  7.003   -0.603  1.00 7.21   ?  337  ILE B CG1  1 
ATOM   6959  C  CG2  . ILE B 1 114 ? 24.143  8.378   -0.173  1.00 7.31   ?  337  ILE B CG2  1 
ATOM   6960  C  CD1  . ILE B 1 114 ? 21.940  7.278   -2.101  1.00 8.77   ?  337  ILE B CD1  1 
ATOM   6961  H  H    . ILE B 1 114 ? 23.868  9.188   2.218   1.00 5.78   ?  337  ILE B H    1 
ATOM   6962  H  HA   . ILE B 1 114 ? 21.515  7.910   1.857   1.00 6.13   ?  337  ILE B HA   1 
ATOM   6963  H  HB   . ILE B 1 114 ? 22.223  8.986   -0.035  1.00 7.26   ?  337  ILE B HB   1 
ATOM   6964  H  HG12 . ILE B 1 114 ? 22.623  6.218   -0.492  1.00 8.65   ?  337  ILE B HG12 1 
ATOM   6965  H  HG13 . ILE B 1 114 ? 21.174  6.827   -0.260  1.00 8.65   ?  337  ILE B HG13 1 
ATOM   6966  H  HG21 . ILE B 1 114 ? 24.218  8.464   -1.136  1.00 8.77   ?  337  ILE B HG21 1 
ATOM   6967  H  HG22 . ILE B 1 114 ? 24.459  9.188   0.257   1.00 8.77   ?  337  ILE B HG22 1 
ATOM   6968  H  HG23 . ILE B 1 114 ? 24.661  7.617   0.132   1.00 8.77   ?  337  ILE B HG23 1 
ATOM   6969  H  HD11 . ILE B 1 114 ? 21.463  6.543   -2.519  1.00 10.53  ?  337  ILE B HD11 1 
ATOM   6970  H  HD12 . ILE B 1 114 ? 21.450  8.105   -2.231  1.00 10.53  ?  337  ILE B HD12 1 
ATOM   6971  H  HD13 . ILE B 1 114 ? 22.828  7.356   -2.483  1.00 10.53  ?  337  ILE B HD13 1 
ATOM   6972  N  N    . SER B 1 115 ? 22.088  5.658   2.471   1.00 5.08   ?  338  SER B N    1 
ATOM   6973  C  CA   A SER B 1 115 ? 22.420  4.289   2.820   0.36 5.25   ?  338  SER B CA   1 
ATOM   6974  C  CA   B SER B 1 115 ? 22.405  4.288   2.826   0.64 4.95   ?  338  SER B CA   1 
ATOM   6975  C  C    . SER B 1 115 ? 21.821  3.348   1.787   1.00 5.22   ?  338  SER B C    1 
ATOM   6976  O  O    . SER B 1 115 ? 20.700  3.558   1.305   1.00 6.46   ?  338  SER B O    1 
ATOM   6977  C  CB   A SER B 1 115 ? 21.915  3.933   4.224   0.36 6.15   ?  338  SER B CB   1 
ATOM   6978  C  CB   B SER B 1 115 ? 21.774  3.931   4.163   0.64 5.89   ?  338  SER B CB   1 
ATOM   6979  O  OG   A SER B 1 115 ? 20.531  4.203   4.391   0.36 6.43   ?  338  SER B OG   1 
ATOM   6980  O  OG   B SER B 1 115 ? 22.299  4.709   5.218   0.64 5.99   ?  338  SER B OG   1 
ATOM   6981  H  H    A SER B 1 115 ? 21.244  5.821   2.489   0.36 6.09   ?  338  SER B H    1 
ATOM   6982  H  H    B SER B 1 115 ? 21.244  5.823   2.485   0.64 6.09   ?  338  SER B H    1 
ATOM   6983  H  HA   A SER B 1 115 ? 23.383  4.173   2.815   0.36 6.30   ?  338  SER B HA   1 
ATOM   6984  H  HA   B SER B 1 115 ? 23.369  4.180   2.866   0.64 5.94   ?  338  SER B HA   1 
ATOM   6985  H  HB2  A SER B 1 115 ? 22.065  2.987   4.376   0.36 7.39   ?  338  SER B HB2  1 
ATOM   6986  H  HB2  B SER B 1 115 ? 20.818  4.087   4.108   0.64 7.07   ?  338  SER B HB2  1 
ATOM   6987  H  HB3  A SER B 1 115 ? 22.412  4.456   4.873   0.36 7.39   ?  338  SER B HB3  1 
ATOM   6988  H  HB3  B SER B 1 115 ? 21.948  2.996   4.350   0.64 7.07   ?  338  SER B HB3  1 
ATOM   6989  H  HG   A SER B 1 115 ? 20.098  3.898   3.739   0.36 7.72   ?  338  SER B HG   1 
ATOM   6990  H  HG   B SER B 1 115 ? 23.128  4.588   5.280   0.64 7.19   ?  338  SER B HG   1 
ATOM   6991  N  N    . GLN B 1 116 ? 22.572  2.311   1.459   1.00 5.31   ?  339  GLN B N    1 
ATOM   6992  C  CA   . GLN B 1 116 ? 22.160  1.311   0.489   1.00 5.23   ?  339  GLN B CA   1 
ATOM   6993  C  C    . GLN B 1 116 ? 22.241  -0.074  1.114   1.00 5.45   ?  339  GLN B C    1 
ATOM   6994  O  O    . GLN B 1 116 ? 23.137  -0.369  1.916   1.00 5.69   ?  339  GLN B O    1 
ATOM   6995  C  CB   . GLN B 1 116 ? 23.049  1.313   -0.764  1.00 5.61   ?  339  GLN B CB   1 
ATOM   6996  C  CG   . GLN B 1 116 ? 23.289  2.686   -1.361  1.00 6.06   ?  339  GLN B CG   1 
ATOM   6997  C  CD   . GLN B 1 116 ? 23.814  2.612   -2.768  1.00 6.06   ?  339  GLN B CD   1 
ATOM   6998  O  OE1  . GLN B 1 116 ? 24.875  2.032   -3.023  1.00 6.54   ?  339  GLN B OE1  1 
ATOM   6999  N  NE2  . GLN B 1 116 ? 23.065  3.167   -3.691  1.00 6.38   ?  339  GLN B NE2  1 
ATOM   7000  H  H    . GLN B 1 116 ? 23.350  2.160   1.795   1.00 6.37   ?  339  GLN B H    1 
ATOM   7001  H  HA   . GLN B 1 116 ? 21.245  1.501   0.228   1.00 6.28   ?  339  GLN B HA   1 
ATOM   7002  H  HB2  . GLN B 1 116 ? 23.914  0.940   -0.530  1.00 6.74   ?  339  GLN B HB2  1 
ATOM   7003  H  HB3  . GLN B 1 116 ? 22.626  0.767   -1.445  1.00 6.74   ?  339  GLN B HB3  1 
ATOM   7004  H  HG2  . GLN B 1 116 ? 22.453  3.177   -1.376  1.00 7.28   ?  339  GLN B HG2  1 
ATOM   7005  H  HG3  . GLN B 1 116 ? 23.941  3.159   -0.820  1.00 7.28   ?  339  GLN B HG3  1 
ATOM   7006  H  HE21 . GLN B 1 116 ? 22.323  3.543   -3.474  1.00 7.66   ?  339  GLN B HE21 1 
ATOM   7007  H  HE22 . GLN B 1 116 ? 23.317  3.154   -4.513  1.00 7.66   ?  339  GLN B HE22 1 
ATOM   7008  N  N    . ARG B 1 117 ? 21.315  -0.930  0.685   1.00 5.49   ?  340  ARG B N    1 
ATOM   7009  C  CA   . ARG B 1 117 ? 21.348  -2.358  0.978   1.00 5.84   ?  340  ARG B CA   1 
ATOM   7010  C  C    . ARG B 1 117 ? 20.975  -3.054  -0.318  1.00 5.88   ?  340  ARG B C    1 
ATOM   7011  O  O    . ARG B 1 117 ? 19.923  -2.775  -0.893  1.00 6.28   ?  340  ARG B O    1 
ATOM   7012  C  CB   . ARG B 1 117 ? 20.398  -2.743  2.112   1.00 6.85   ?  340  ARG B CB   1 
ATOM   7013  C  CG   . ARG B 1 117 ? 20.372  -4.251  2.347   1.00 7.12   ?  340  ARG B CG   1 
ATOM   7014  C  CD   . ARG B 1 117 ? 19.618  -4.641  3.614   1.00 8.75   ?  340  ARG B CD   1 
ATOM   7015  N  NE   . ARG B 1 117 ? 20.393  -4.255  4.774   1.00 9.51   ?  340  ARG B NE   1 
ATOM   7016  C  CZ   . ARG B 1 117 ? 20.023  -3.399  5.713   1.00 9.31   ?  340  ARG B CZ   1 
ATOM   7017  N  NH1  . ARG B 1 117 ? 18.775  -2.983  5.825   1.00 12.61  ?  340  ARG B NH1  1 
ATOM   7018  N  NH2  . ARG B 1 117 ? 20.931  -2.962  6.566   1.00 8.32   ?  340  ARG B NH2  1 
ATOM   7019  H  H    . ARG B 1 117 ? 20.638  -0.699  0.208   1.00 6.59   ?  340  ARG B H    1 
ATOM   7020  H  HA   . ARG B 1 117 ? 22.234  -2.631  1.265   1.00 7.01   ?  340  ARG B HA   1 
ATOM   7021  H  HB2  . ARG B 1 117 ? 20.689  -2.313  2.932   1.00 8.22   ?  340  ARG B HB2  1 
ATOM   7022  H  HB3  . ARG B 1 117 ? 19.500  -2.455  1.887   1.00 8.22   ?  340  ARG B HB3  1 
ATOM   7023  H  HG2  . ARG B 1 117 ? 19.934  -4.680  1.595   1.00 8.55   ?  340  ARG B HG2  1 
ATOM   7024  H  HG3  . ARG B 1 117 ? 21.283  -4.574  2.430   1.00 8.55   ?  340  ARG B HG3  1 
ATOM   7025  H  HD2  . ARG B 1 117 ? 18.763  -4.183  3.642   1.00 10.50  ?  340  ARG B HD2  1 
ATOM   7026  H  HD3  . ARG B 1 117 ? 19.481  -5.601  3.634   1.00 10.50  ?  340  ARG B HD3  1 
ATOM   7027  H  HE   . ARG B 1 117 ? 21.168  -4.617  4.861   1.00 11.41  ?  340  ARG B HE   1 
ATOM   7028  H  HH11 . ARG B 1 117 ? 18.176  -3.270  5.279   1.00 15.14  ?  340  ARG B HH11 1 
ATOM   7029  H  HH12 . ARG B 1 117 ? 18.562  -2.426  6.444   1.00 15.14  ?  340  ARG B HH12 1 
ATOM   7030  H  HH21 . ARG B 1 117 ? 21.745  -3.234  6.506   1.00 9.99   ?  340  ARG B HH21 1 
ATOM   7031  H  HH22 . ARG B 1 117 ? 20.709  -2.405  7.183   1.00 9.99   ?  340  ARG B HH22 1 
ATOM   7032  N  N    . ASP B 1 118 ? 21.858  -3.912  -0.812  1.00 6.05   ?  341  ASP B N    1 
ATOM   7033  C  CA   . ASP B 1 118 ? 21.723  -4.437  -2.162  1.00 6.63   ?  341  ASP B CA   1 
ATOM   7034  C  C    . ASP B 1 118 ? 20.551  -5.412  -2.262  1.00 6.59   ?  341  ASP B C    1 
ATOM   7035  O  O    . ASP B 1 118 ? 20.119  -6.014  -1.278  1.00 7.05   ?  341  ASP B O    1 
ATOM   7036  C  CB   . ASP B 1 118 ? 23.063  -5.037  -2.614  1.00 7.72   ?  341  ASP B CB   1 
ATOM   7037  C  CG   . ASP B 1 118 ? 24.178  -3.990  -2.725  1.00 7.35   ?  341  ASP B CG   1 
ATOM   7038  O  OD1  . ASP B 1 118 ? 23.883  -2.784  -2.665  1.00 8.69   ?  341  ASP B OD1  1 
ATOM   7039  O  OD2  . ASP B 1 118 ? 25.359  -4.378  -2.866  1.00 8.89   -1 341  ASP B OD2  1 
ATOM   7040  H  H    . ASP B 1 118 ? 22.545  -4.205  -0.385  1.00 7.27   ?  341  ASP B H    1 
ATOM   7041  H  HA   . ASP B 1 118 ? 21.511  -3.729  -2.791  1.00 7.96   ?  341  ASP B HA   1 
ATOM   7042  H  HB2  . ASP B 1 118 ? 23.342  -5.705  -1.969  1.00 9.26   ?  341  ASP B HB2  1 
ATOM   7043  H  HB3  . ASP B 1 118 ? 22.947  -5.445  -3.486  1.00 9.26   ?  341  ASP B HB3  1 
ATOM   7044  N  N    . ARG B 1 119 ? 20.024  -5.542  -3.486  1.00 6.80   ?  342  ARG B N    1 
ATOM   7045  C  CA   . ARG B 1 119 ? 18.785  -6.287  -3.694  1.00 8.90   ?  342  ARG B CA   1 
ATOM   7046  C  C    . ARG B 1 119 ? 18.976  -7.778  -3.520  1.00 10.02  ?  342  ARG B C    1 
ATOM   7047  O  O    . ARG B 1 119 ? 18.037  -8.477  -3.122  1.00 11.73  ?  342  ARG B O    1 
ATOM   7048  C  CB   . ARG B 1 119 ? 18.283  -6.161  -5.132  1.00 12.57  ?  342  ARG B CB   1 
ATOM   7049  C  CG   . ARG B 1 119 ? 17.912  -4.851  -5.531  1.00 13.42  ?  342  ARG B CG   1 
ATOM   7050  C  CD   . ARG B 1 119 ? 17.447  -4.856  -6.973  1.00 13.13  ?  342  ARG B CD   1 
ATOM   7051  N  NE   . ARG B 1 119 ? 17.108  -3.475  -7.246  1.00 11.97  ?  342  ARG B NE   1 
ATOM   7052  C  CZ   . ARG B 1 119 ? 17.955  -2.551  -7.671  1.00 10.63  ?  342  ARG B CZ   1 
ATOM   7053  N  NH1  . ARG B 1 119 ? 19.132  -2.871  -8.188  1.00 11.22  ?  342  ARG B NH1  1 
ATOM   7054  N  NH2  . ARG B 1 119 ? 17.615  -1.273  -7.567  1.00 11.40  ?  342  ARG B NH2  1 
ATOM   7055  H  H    . ARG B 1 119 ? 20.363  -5.211  -4.204  1.00 8.17   ?  342  ARG B H    1 
ATOM   7056  H  HA   . ARG B 1 119 ? 18.157  -5.912  -3.057  1.00 10.68  ?  342  ARG B HA   1 
ATOM   7057  H  HB2  . ARG B 1 119 ? 18.988  -6.458  -5.729  1.00 15.09  ?  342  ARG B HB2  1 
ATOM   7058  H  HB3  . ARG B 1 119 ? 17.502  -6.727  -5.234  1.00 15.09  ?  342  ARG B HB3  1 
ATOM   7059  H  HG2  . ARG B 1 119 ? 17.187  -4.533  -4.971  1.00 16.11  ?  342  ARG B HG2  1 
ATOM   7060  H  HG3  . ARG B 1 119 ? 18.676  -4.258  -5.453  1.00 16.11  ?  342  ARG B HG3  1 
ATOM   7061  H  HD2  . ARG B 1 119 ? 18.155  -5.150  -7.566  1.00 15.76  ?  342  ARG B HD2  1 
ATOM   7062  H  HD3  . ARG B 1 119 ? 16.666  -5.421  -7.084  1.00 15.76  ?  342  ARG B HD3  1 
ATOM   7063  H  HE   . ARG B 1 119 ? 16.291  -3.236  -7.121  1.00 14.36  ?  342  ARG B HE   1 
ATOM   7064  H  HH11 . ARG B 1 119 ? 19.362  -3.697  -8.254  1.00 13.46  ?  342  ARG B HH11 1 
ATOM   7065  H  HH12 . ARG B 1 119 ? 19.665  -2.253  -8.458  1.00 13.46  ?  342  ARG B HH12 1 
ATOM   7066  H  HH21 . ARG B 1 119 ? 16.855  -1.057  -7.228  1.00 13.68  ?  342  ARG B HH21 1 
ATOM   7067  H  HH22 . ARG B 1 119 ? 18.154  -0.661  -7.839  1.00 13.68  ?  342  ARG B HH22 1 
ATOM   7068  N  N    . GLU B 1 120 ? 20.143  -8.288  -3.894  1.00 9.87   ?  343  GLU B N    1 
ATOM   7069  C  CA   . GLU B 1 120 ? 20.407  -9.715  -3.851  1.00 11.02  ?  343  GLU B CA   1 
ATOM   7070  C  C    . GLU B 1 120 ? 21.557  -9.971  -2.893  1.00 9.75   ?  343  GLU B C    1 
ATOM   7071  O  O    . GLU B 1 120 ? 22.466  -9.155  -2.759  1.00 10.84  ?  343  GLU B O    1 
ATOM   7072  C  CB   . GLU B 1 120 ? 20.798  -10.251 -5.238  1.00 13.60  ?  343  GLU B CB   1 
ATOM   7073  C  CG   . GLU B 1 120 ? 19.658  -10.272 -6.244  1.00 21.29  ?  343  GLU B CG   1 
ATOM   7074  C  CD   . GLU B 1 120 ? 18.554  -11.241 -5.857  1.00 149.33 ?  343  GLU B CD   1 
ATOM   7075  O  OE1  . GLU B 1 120 ? 18.852  -12.248 -5.179  1.00 70.19  ?  343  GLU B OE1  1 
ATOM   7076  O  OE2  . GLU B 1 120 ? 17.387  -10.993 -6.226  1.00 76.15  -1 343  GLU B OE2  1 
ATOM   7077  H  H    . GLU B 1 120 ? 20.804  -7.819  -4.179  1.00 11.85  ?  343  GLU B H    1 
ATOM   7078  H  HA   . GLU B 1 120 ? 19.616  -10.187 -3.548  1.00 13.23  ?  343  GLU B HA   1 
ATOM   7079  H  HB2  . GLU B 1 120 ? 21.499  -9.688  -5.601  1.00 16.32  ?  343  GLU B HB2  1 
ATOM   7080  H  HB3  . GLU B 1 120 ? 21.120  -11.160 -5.139  1.00 16.32  ?  343  GLU B HB3  1 
ATOM   7081  H  HG2  . GLU B 1 120 ? 19.271  -9.385  -6.303  1.00 25.55  ?  343  GLU B HG2  1 
ATOM   7082  H  HG3  . GLU B 1 120 ? 20.004  -10.542 -7.109  1.00 25.55  ?  343  GLU B HG3  1 
ATOM   7083  N  N    . GLY B 1 121 ? 21.500  -11.102 -2.218  1.00 9.65   ?  344  GLY B N    1 
ATOM   7084  C  CA   . GLY B 1 121 ? 22.562  -11.493 -1.318  1.00 9.33   ?  344  GLY B CA   1 
ATOM   7085  C  C    . GLY B 1 121 ? 23.838  -11.910 -2.028  1.00 8.58   ?  344  GLY B C    1 
ATOM   7086  O  O    . GLY B 1 121 ? 23.892  -12.135 -3.242  1.00 9.64   ?  344  GLY B O    1 
ATOM   7087  H  H    . GLY B 1 121 ? 20.852  -11.665 -2.265  1.00 11.59  ?  344  GLY B H    1 
ATOM   7088  H  HA2  . GLY B 1 121 ? 22.772  -10.748 -0.733  1.00 11.19  ?  344  GLY B HA2  1 
ATOM   7089  H  HA3  . GLY B 1 121 ? 22.260  -12.241 -0.779  1.00 11.19  ?  344  GLY B HA3  1 
ATOM   7090  N  N    . THR B 1 122 ? 24.897  -12.009 -1.225  1.00 7.64   ?  345  THR B N    1 
ATOM   7091  C  CA   . THR B 1 122 ? 26.224  -12.387 -1.688  1.00 6.98   ?  345  THR B CA   1 
ATOM   7092  C  C    . THR B 1 122 ? 26.545  -13.794 -1.202  1.00 7.09   ?  345  THR B C    1 
ATOM   7093  O  O    . THR B 1 122 ? 26.639  -14.022 0.018   1.00 7.70   ?  345  THR B O    1 
ATOM   7094  C  CB   . THR B 1 122 ? 27.240  -11.368 -1.163  1.00 6.42   ?  345  THR B CB   1 
ATOM   7095  O  OG1  . THR B 1 122 ? 27.033  -10.097 -1.793  1.00 6.85   ?  345  THR B OG1  1 
ATOM   7096  C  CG2  . THR B 1 122 ? 28.659  -11.801 -1.479  1.00 6.98   ?  345  THR B CG2  1 
ATOM   7097  H  H    . THR B 1 122 ? 24.867  -11.857 -0.379  1.00 9.17   ?  345  THR B H    1 
ATOM   7098  H  HA   . THR B 1 122 ? 26.263  -12.399 -2.657  1.00 8.37   ?  345  THR B HA   1 
ATOM   7099  H  HB   . THR B 1 122 ? 27.128  -11.296 -0.202  1.00 7.70   ?  345  THR B HB   1 
ATOM   7100  H  HG1  . THR B 1 122 ? 26.266  -9.808  -1.611  1.00 8.23   ?  345  THR B HG1  1 
ATOM   7101  H  HG21 . THR B 1 122 ? 29.269  -11.058 -1.349  1.00 8.38   ?  345  THR B HG21 1 
ATOM   7102  H  HG22 . THR B 1 122 ? 28.921  -12.529 -0.894  1.00 8.38   ?  345  THR B HG22 1 
ATOM   7103  H  HG23 . THR B 1 122 ? 28.717  -12.099 -2.400  1.00 8.38   ?  345  THR B HG23 1 
ATOM   7104  N  N    . PRO B 1 123 ? 26.696  -14.767 -2.113  1.00 6.81   ?  346  PRO B N    1 
ATOM   7105  C  CA   . PRO B 1 123 ? 26.934  -16.160 -1.679  1.00 7.22   ?  346  PRO B CA   1 
ATOM   7106  C  C    . PRO B 1 123 ? 28.108  -16.327 -0.732  1.00 7.62   ?  346  PRO B C    1 
ATOM   7107  O  O    . PRO B 1 123 ? 28.030  -17.117 0.212   1.00 7.27   ?  346  PRO B O    1 
ATOM   7108  C  CB   . PRO B 1 123 ? 27.141  -16.905 -3.017  1.00 8.51   ?  346  PRO B CB   1 
ATOM   7109  C  CG   . PRO B 1 123 ? 26.311  -16.142 -3.980  1.00 8.47   ?  346  PRO B CG   1 
ATOM   7110  C  CD   . PRO B 1 123 ? 26.473  -14.687 -3.569  1.00 7.50   ?  346  PRO B CD   1 
ATOM   7111  H  HA   . PRO B 1 123 ? 26.139  -16.504 -1.242  1.00 8.67   ?  346  PRO B HA   1 
ATOM   7112  H  HB2  . PRO B 1 123 ? 28.077  -16.887 -3.268  1.00 10.22  ?  346  PRO B HB2  1 
ATOM   7113  H  HB3  . PRO B 1 123 ? 26.836  -17.822 -2.939  1.00 10.22  ?  346  PRO B HB3  1 
ATOM   7114  H  HG2  . PRO B 1 123 ? 26.636  -16.286 -4.883  1.00 10.17  ?  346  PRO B HG2  1 
ATOM   7115  H  HG3  . PRO B 1 123 ? 25.385  -16.421 -3.912  1.00 10.17  ?  346  PRO B HG3  1 
ATOM   7116  H  HD2  . PRO B 1 123 ? 27.235  -14.285 -4.014  1.00 9.00   ?  346  PRO B HD2  1 
ATOM   7117  H  HD3  . PRO B 1 123 ? 25.669  -14.181 -3.767  1.00 9.00   ?  346  PRO B HD3  1 
ATOM   7118  N  N    . SER B 1 124 ? 29.193  -15.579 -0.946  1.00 7.03   ?  347  SER B N    1 
ATOM   7119  C  CA   . SER B 1 124 ? 30.373  -15.735 -0.104  1.00 7.14   ?  347  SER B CA   1 
ATOM   7120  C  C    . SER B 1 124 ? 30.183  -15.178 1.299   1.00 6.99   ?  347  SER B C    1 
ATOM   7121  O  O    . SER B 1 124 ? 31.060  -15.379 2.147   1.00 8.75   ?  347  SER B O    1 
ATOM   7122  C  CB   . SER B 1 124 ? 31.597  -15.064 -0.720  1.00 7.23   ?  347  SER B CB   1 
ATOM   7123  O  OG   . SER B 1 124 ? 31.410  -13.662 -0.857  1.00 7.88   ?  347  SER B OG   1 
ATOM   7124  H  H    . SER B 1 124 ? 29.268  -14.985 -1.563  1.00 8.43   ?  347  SER B H    1 
ATOM   7125  H  HA   . SER B 1 124 ? 30.550  -16.687 -0.048  1.00 8.57   ?  347  SER B HA   1 
ATOM   7126  H  HB2  . SER B 1 124 ? 32.363  -15.223 -0.147  1.00 8.68   ?  347  SER B HB2  1 
ATOM   7127  H  HB3  . SER B 1 124 ? 31.755  -15.445 -1.598  1.00 8.68   ?  347  SER B HB3  1 
ATOM   7128  H  HG   . SER B 1 124 ? 32.103  -13.309 -1.175  1.00 9.46   ?  347  SER B HG   1 
ATOM   7129  N  N    . GLU B 1 125 ? 29.082  -14.478 1.552   1.00 7.16   ?  348  GLU B N    1 
ATOM   7130  C  CA   . GLU B 1 125 ? 28.721  -13.929 2.850   1.00 7.34   ?  348  GLU B CA   1 
ATOM   7131  C  C    . GLU B 1 125 ? 27.413  -14.550 3.326   1.00 8.09   ?  348  GLU B C    1 
ATOM   7132  O  O    . GLU B 1 125 ? 26.540  -13.878 3.878   1.00 8.85   ?  348  GLU B O    1 
ATOM   7133  C  CB   . GLU B 1 125 ? 28.641  -12.403 2.785   1.00 8.22   ?  348  GLU B CB   1 
ATOM   7134  C  CG   . GLU B 1 125 ? 29.973  -11.739 2.467   1.00 8.95   ?  348  GLU B CG   1 
ATOM   7135  C  CD   . GLU B 1 125 ? 30.986  -11.826 3.579   1.00 10.92  ?  348  GLU B CD   1 
ATOM   7136  O  OE1  . GLU B 1 125 ? 30.580  -11.934 4.754   1.00 12.49  ?  348  GLU B OE1  1 
ATOM   7137  O  OE2  . GLU B 1 125 ? 32.201  -11.764 3.277   1.00 12.29  -1 348  GLU B OE2  1 
ATOM   7138  H  H    . GLU B 1 125 ? 28.495  -14.299 0.949   1.00 8.60   ?  348  GLU B H    1 
ATOM   7139  H  HA   . GLU B 1 125 ? 29.403  -14.147 3.504   1.00 8.81   ?  348  GLU B HA   1 
ATOM   7140  H  HB2  . GLU B 1 125 ? 28.011  -12.152 2.091   1.00 9.87   ?  348  GLU B HB2  1 
ATOM   7141  H  HB3  . GLU B 1 125 ? 28.340  -12.068 3.643   1.00 9.87   ?  348  GLU B HB3  1 
ATOM   7142  H  HG2  . GLU B 1 125 ? 30.356  -12.169 1.686   1.00 10.74  ?  348  GLU B HG2  1 
ATOM   7143  H  HG3  . GLU B 1 125 ? 29.816  -10.800 2.284   1.00 10.74  ?  348  GLU B HG3  1 
ATOM   7144  N  N    . ASN B 1 126 ? 27.259  -15.850 3.078   1.00 9.38   ?  349  ASN B N    1 
ATOM   7145  C  CA   . ASN B 1 126 ? 26.080  -16.604 3.490   1.00 10.77  ?  349  ASN B CA   1 
ATOM   7146  C  C    . ASN B 1 126 ? 24.785  -15.980 2.975   1.00 9.65   ?  349  ASN B C    1 
ATOM   7147  O  O    . ASN B 1 126 ? 23.754  -15.980 3.648   1.00 11.13  ?  349  ASN B O    1 
ATOM   7148  C  CB   . ASN B 1 126 ? 26.039  -16.810 5.002   1.00 13.55  ?  349  ASN B CB   1 
ATOM   7149  C  CG   . ASN B 1 126 ? 25.092  -17.933 5.407   1.00 17.56  ?  349  ASN B CG   1 
ATOM   7150  O  OD1  . ASN B 1 126 ? 24.936  -18.926 4.694   1.00 19.03  ?  349  ASN B OD1  1 
ATOM   7151  N  ND2  . ASN B 1 126 ? 24.444  -17.771 6.557   1.00 19.12  ?  349  ASN B ND2  1 
ATOM   7152  H  H    . ASN B 1 126 ? 27.839  -16.329 2.662   1.00 11.25  ?  349  ASN B H    1 
ATOM   7153  H  HA   . ASN B 1 126 ? 26.146  -17.480 3.080   1.00 12.92  ?  349  ASN B HA   1 
ATOM   7154  H  HB2  . ASN B 1 126 ? 26.928  -17.037 5.316   1.00 16.26  ?  349  ASN B HB2  1 
ATOM   7155  H  HB3  . ASN B 1 126 ? 25.736  -15.992 5.426   1.00 16.26  ?  349  ASN B HB3  1 
ATOM   7156  H  HD21 . ASN B 1 126 ? 24.571  -17.062 7.026   1.00 22.95  ?  349  ASN B HD21 1 
ATOM   7157  H  HD22 . ASN B 1 126 ? 23.898  -18.376 6.831   1.00 22.95  ?  349  ASN B HD22 1 
ATOM   7158  N  N    . ASN B 1 127 ? 24.840  -15.452 1.754   0.89 8.58   ?  350  ASN B N    1 
ATOM   7159  C  CA   . ASN B 1 127 ? 23.698  -14.866 1.066   0.89 8.87   ?  350  ASN B CA   1 
ATOM   7160  C  C    . ASN B 1 127 ? 23.188  -13.607 1.751   0.89 8.69   ?  350  ASN B C    1 
ATOM   7161  O  O    . ASN B 1 127 ? 22.060  -13.180 1.519   0.89 10.39  ?  350  ASN B O    1 
ATOM   7162  C  CB   . ASN B 1 127 ? 22.599  -15.895 0.831   0.89 11.84  ?  350  ASN B CB   1 
ATOM   7163  C  CG   . ASN B 1 127 ? 23.110  -17.100 0.061   0.89 16.04  ?  350  ASN B CG   1 
ATOM   7164  O  OD1  . ASN B 1 127 ? 23.681  -16.967 -1.035  0.89 17.58  ?  350  ASN B OD1  1 
ATOM   7165  N  ND2  . ASN B 1 127 ? 22.957  -18.277 0.648   0.89 18.70  ?  350  ASN B ND2  1 
ATOM   7166  H  H    . ASN B 1 127 ? 25.561  -15.423 1.286   0.89 10.29  ?  350  ASN B H    1 
ATOM   7167  H  HA   . ASN B 1 127 ? 23.978  -14.577 0.183   0.89 10.65  ?  350  ASN B HA   1 
ATOM   7168  H  HB2  . ASN B 1 127 ? 22.260  -16.203 1.686   0.89 14.21  ?  350  ASN B HB2  1 
ATOM   7169  H  HB3  . ASN B 1 127 ? 21.883  -15.488 0.318   0.89 14.21  ?  350  ASN B HB3  1 
ATOM   7170  H  HD21 . ASN B 1 127 ? 22.585  -18.326 1.422   0.89 22.44  ?  350  ASN B HD21 1 
ATOM   7171  H  HD22 . ASN B 1 127 ? 23.229  -18.992 0.255   0.89 22.44  ?  350  ASN B HD22 1 
ATOM   7172  N  N    . GLN B 1 128 ? 24.018  -12.975 2.569   1.00 8.19   ?  351  GLN B N    1 
ATOM   7173  C  CA   . GLN B 1 128 ? 23.666  -11.688 3.141   1.00 7.76   ?  351  GLN B CA   1 
ATOM   7174  C  C    . GLN B 1 128 ? 23.891  -10.566 2.130   1.00 6.91   ?  351  GLN B C    1 
ATOM   7175  O  O    . GLN B 1 128 ? 24.730  -10.660 1.229   1.00 7.31   ?  351  GLN B O    1 
ATOM   7176  C  CB   . GLN B 1 128 ? 24.526  -11.422 4.362   1.00 9.07   ?  351  GLN B CB   1 
ATOM   7177  C  CG   . GLN B 1 128 ? 24.280  -12.347 5.517   1.00 11.90  ?  351  GLN B CG   1 
ATOM   7178  C  CD   . GLN B 1 128 ? 25.143  -11.974 6.677   1.00 15.92  ?  351  GLN B CD   1 
ATOM   7179  O  OE1  . GLN B 1 128 ? 26.357  -12.026 6.591   1.00 19.01  ?  351  GLN B OE1  1 
ATOM   7180  N  NE2  . GLN B 1 128 ? 24.524  -11.528 7.748   1.00 18.76  ?  351  GLN B NE2  1 
ATOM   7181  H  H    . GLN B 1 128 ? 24.789  -13.272 2.808   1.00 9.84   ?  351  GLN B H    1 
ATOM   7182  H  HA   . GLN B 1 128 ? 22.730  -11.691 3.396   1.00 9.32   ?  351  GLN B HA   1 
ATOM   7183  H  HB2  . GLN B 1 128 ? 25.458  -11.514 4.108   1.00 10.88  ?  351  GLN B HB2  1 
ATOM   7184  H  HB3  . GLN B 1 128 ? 24.354  -10.519 4.670   1.00 10.88  ?  351  GLN B HB3  1 
ATOM   7185  H  HG2  . GLN B 1 128 ? 23.351  -12.286 5.790   1.00 14.28  ?  351  GLN B HG2  1 
ATOM   7186  H  HG3  . GLN B 1 128 ? 24.490  -13.257 5.256   1.00 14.28  ?  351  GLN B HG3  1 
ATOM   7187  H  HE21 . GLN B 1 128 ? 23.667  -11.464 7.755   1.00 22.51  ?  351  GLN B HE21 1 
ATOM   7188  H  HE22 . GLN B 1 128 ? 24.978  -11.300 8.443   1.00 22.51  ?  351  GLN B HE22 1 
ATOM   7189  N  N    . LYS B 1 129 ? 23.139  -9.494  2.310   1.00 6.73   ?  352  LYS B N    1 
ATOM   7190  C  CA   . LYS B 1 129 ? 23.205  -8.354  1.407   1.00 7.51   ?  352  LYS B CA   1 
ATOM   7191  C  C    . LYS B 1 129 ? 24.332  -7.399  1.784   1.00 6.26   ?  352  LYS B C    1 
ATOM   7192  O  O    . LYS B 1 129 ? 24.573  -7.122  2.963   1.00 6.80   ?  352  LYS B O    1 
ATOM   7193  C  CB   . LYS B 1 129 ? 21.866  -7.616  1.466   1.00 9.03   ?  352  LYS B CB   1 
ATOM   7194  C  CG   . LYS B 1 129 ? 20.715  -8.471  0.899   1.00 10.53  ?  352  LYS B CG   1 
ATOM   7195  C  CD   . LYS B 1 129 ? 19.383  -7.909  1.264   1.00 12.13  ?  352  LYS B CD   1 
ATOM   7196  C  CE   . LYS B 1 129 ? 18.264  -8.691  0.591   1.00 14.83  ?  352  LYS B CE   1 
ATOM   7197  N  NZ   . LYS B 1 129 ? 16.945  -8.300  1.165   1.00 17.56  ?  352  LYS B NZ   1 
ATOM   7198  H  H    . LYS B 1 129 ? 22.577  -9.398  2.953   1.00 8.07   ?  352  LYS B H    1 
ATOM   7199  H  HA   . LYS B 1 129 ? 23.382  -8.659  0.503   1.00 9.02   ?  352  LYS B HA   1 
ATOM   7200  H  HB2  . LYS B 1 129 ? 21.660  -7.402  2.389   1.00 10.84  ?  352  LYS B HB2  1 
ATOM   7201  H  HB3  . LYS B 1 129 ? 21.927  -6.801  0.942   1.00 10.84  ?  352  LYS B HB3  1 
ATOM   7202  H  HG2  . LYS B 1 129 ? 20.781  -8.496  -0.069  1.00 12.64  ?  352  LYS B HG2  1 
ATOM   7203  H  HG3  . LYS B 1 129 ? 20.776  -9.370  1.258   1.00 12.64  ?  352  LYS B HG3  1 
ATOM   7204  H  HD2  . LYS B 1 129 ? 19.261  -7.963  2.225   1.00 14.56  ?  352  LYS B HD2  1 
ATOM   7205  H  HD3  . LYS B 1 129 ? 19.330  -6.985  0.974   1.00 14.56  ?  352  LYS B HD3  1 
ATOM   7206  H  HE2  . LYS B 1 129 ? 18.258  -8.498  -0.359  1.00 17.80  ?  352  LYS B HE2  1 
ATOM   7207  H  HE3  . LYS B 1 129 ? 18.397  -9.640  0.737   1.00 17.80  ?  352  LYS B HE3  1 
ATOM   7208  H  HZ1  . LYS B 1 129 ? 16.298  -8.796  0.807   1.00 21.07  ?  352  LYS B HZ1  1 
ATOM   7209  H  HZ2  . LYS B 1 129 ? 16.948  -8.422  2.046   1.00 21.07  ?  352  LYS B HZ2  1 
ATOM   7210  H  HZ3  . LYS B 1 129 ? 16.780  -7.443  0.993   1.00 21.07  ?  352  LYS B HZ3  1 
ATOM   7211  N  N    . ALA B 1 130 ? 25.022  -6.889  0.760   1.00 5.99   ?  353  ALA B N    1 
ATOM   7212  C  CA   . ALA B 1 130 ? 26.036  -5.866  0.956   1.00 5.62   ?  353  ALA B CA   1 
ATOM   7213  C  C    . ALA B 1 130 ? 25.392  -4.509  1.246   1.00 5.59   ?  353  ALA B C    1 
ATOM   7214  O  O    . ALA B 1 130 ? 24.273  -4.219  0.807   1.00 6.00   ?  353  ALA B O    1 
ATOM   7215  C  CB   . ALA B 1 130 ? 26.887  -5.752  -0.311  1.00 6.57   ?  353  ALA B CB   1 
ATOM   7216  H  H    . ALA B 1 130 ? 24.917  -7.123  -0.061  1.00 7.19   ?  353  ALA B H    1 
ATOM   7217  H  HA   . ALA B 1 130 ? 26.600  -6.103  1.708   1.00 6.74   ?  353  ALA B HA   1 
ATOM   7218  H  HB1  . ALA B 1 130 ? 27.595  -5.107  -0.159  1.00 7.89   ?  353  ALA B HB1  1 
ATOM   7219  H  HB2  . ALA B 1 130 ? 27.269  -6.621  -0.513  1.00 7.89   ?  353  ALA B HB2  1 
ATOM   7220  H  HB3  . ALA B 1 130 ? 26.324  -5.460  -1.044  1.00 7.89   ?  353  ALA B HB3  1 
ATOM   7221  N  N    . ASN B 1 131 ? 26.133  -3.664  1.971   1.00 5.43   ?  354  ASN B N    1 
ATOM   7222  C  CA   . ASN B 1 131 ? 25.645  -2.363  2.414   1.00 5.86   ?  354  ASN B CA   1 
ATOM   7223  C  C    . ASN B 1 131 ? 26.726  -1.303  2.227   1.00 5.92   ?  354  ASN B C    1 
ATOM   7224  O  O    . ASN B 1 131 ? 27.920  -1.603  2.310   1.00 6.31   ?  354  ASN B O    1 
ATOM   7225  C  CB   . ASN B 1 131 ? 25.360  -2.349  3.934   1.00 6.21   ?  354  ASN B CB   1 
ATOM   7226  C  CG   . ASN B 1 131 ? 24.251  -3.295  4.357   1.00 6.28   ?  354  ASN B CG   1 
ATOM   7227  O  OD1  . ASN B 1 131 ? 23.113  -2.877  4.625   1.00 6.65   ?  354  ASN B OD1  1 
ATOM   7228  N  ND2  . ASN B 1 131 ? 24.585  -4.575  4.456   1.00 7.09   ?  354  ASN B ND2  1 
ATOM   7229  H  H    . ASN B 1 131 ? 26.939  -3.829  2.222   1.00 6.51   ?  354  ASN B H    1 
ATOM   7230  H  HA   . ASN B 1 131 ? 24.854  -2.161  1.889   1.00 7.04   ?  354  ASN B HA   1 
ATOM   7231  H  HB2  . ASN B 1 131 ? 26.167  -2.610  4.405   1.00 7.45   ?  354  ASN B HB2  1 
ATOM   7232  H  HB3  . ASN B 1 131 ? 25.099  -1.452  4.194   1.00 7.45   ?  354  ASN B HB3  1 
ATOM   7233  H  HD21 . ASN B 1 131 ? 23.997  -5.156  4.692   1.00 8.51   ?  354  ASN B HD21 1 
ATOM   7234  H  HD22 . ASN B 1 131 ? 25.391  -4.823  4.283   1.00 8.51   ?  354  ASN B HD22 1 
ATOM   7235  N  N    . ARG B 1 132 ? 26.301  -0.048  2.076   1.00 5.24   ?  355  ARG B N    1 
ATOM   7236  C  CA   . ARG B 1 132 ? 27.216  1.080   2.203   1.00 5.76   ?  355  ARG B CA   1 
ATOM   7237  C  C    . ARG B 1 132 ? 26.406  2.328   2.517   1.00 5.86   ?  355  ARG B C    1 
ATOM   7238  O  O    . ARG B 1 132 ? 25.270  2.458   2.075   1.00 6.67   ?  355  ARG B O    1 
ATOM   7239  C  CB   . ARG B 1 132 ? 28.035  1.319   0.926   1.00 6.23   ?  355  ARG B CB   1 
ATOM   7240  C  CG   . ARG B 1 132 ? 27.186  1.653   -0.305  1.00 6.09   ?  355  ARG B CG   1 
ATOM   7241  C  CD   . ARG B 1 132 ? 27.810  1.131   -1.590  1.00 6.78   ?  355  ARG B CD   1 
ATOM   7242  N  NE   . ARG B 1 132 ? 27.921  -0.322  -1.560  1.00 7.50   ?  355  ARG B NE   1 
ATOM   7243  C  CZ   . ARG B 1 132 ? 26.914  -1.152  -1.776  1.00 6.76   ?  355  ARG B CZ   1 
ATOM   7244  N  NH1  . ARG B 1 132 ? 25.733  -0.721  -2.177  1.00 6.75   ?  355  ARG B NH1  1 
ATOM   7245  N  NH2  . ARG B 1 132 ? 27.082  -2.451  -1.556  1.00 7.76   ?  355  ARG B NH2  1 
ATOM   7246  H  H    . ARG B 1 132 ? 25.489  0.173   1.900   1.00 6.29   ?  355  ARG B H    1 
ATOM   7247  H  HA   . ARG B 1 132 ? 27.830  0.897   2.931   1.00 6.91   ?  355  ARG B HA   1 
ATOM   7248  H  HB2  . ARG B 1 132 ? 28.639  2.062   1.078   1.00 7.47   ?  355  ARG B HB2  1 
ATOM   7249  H  HB3  . ARG B 1 132 ? 28.540  0.515   0.726   1.00 7.47   ?  355  ARG B HB3  1 
ATOM   7250  H  HG2  . ARG B 1 132 ? 26.310  1.248   -0.208  1.00 7.31   ?  355  ARG B HG2  1 
ATOM   7251  H  HG3  . ARG B 1 132 ? 27.099  2.616   -0.381  1.00 7.31   ?  355  ARG B HG3  1 
ATOM   7252  H  HD2  . ARG B 1 132 ? 27.255  1.381   -2.345  1.00 8.14   ?  355  ARG B HD2  1 
ATOM   7253  H  HD3  . ARG B 1 132 ? 28.699  1.505   -1.694  1.00 8.14   ?  355  ARG B HD3  1 
ATOM   7254  H  HE   . ARG B 1 132 ? 28.692  -0.663  -1.390  1.00 9.00   ?  355  ARG B HE   1 
ATOM   7255  H  HH11 . ARG B 1 132 ? 25.602  0.119   -2.305  1.00 8.10   ?  355  ARG B HH11 1 
ATOM   7256  H  HH12 . ARG B 1 132 ? 25.093  -1.281  -2.311  1.00 8.10   ?  355  ARG B HH12 1 
ATOM   7257  H  HH21 . ARG B 1 132 ? 27.841  -2.744  -1.276  1.00 9.32   ?  355  ARG B HH21 1 
ATOM   7258  H  HH22 . ARG B 1 132 ? 26.433  -2.998  -1.694  1.00 9.32   ?  355  ARG B HH22 1 
ATOM   7259  N  N    . SER B 1 133 ? 27.015  3.250   3.261   1.00 5.17   ?  356  SER B N    1 
ATOM   7260  C  CA   . SER B 1 133 ? 26.435  4.564   3.503   1.00 5.61   ?  356  SER B CA   1 
ATOM   7261  C  C    . SER B 1 133 ? 27.505  5.636   3.339   1.00 5.56   ?  356  SER B C    1 
ATOM   7262  O  O    . SER B 1 133 ? 28.659  5.438   3.722   1.00 6.10   ?  356  SER B O    1 
ATOM   7263  C  CB   . SER B 1 133 ? 25.877  4.677   4.926   1.00 6.02   ?  356  SER B CB   1 
ATOM   7264  O  OG   . SER B 1 133 ? 24.859  3.725   5.190   1.00 6.08   ?  356  SER B OG   1 
ATOM   7265  H  H    . SER B 1 133 ? 27.777  3.134   3.641   1.00 6.21   ?  356  SER B H    1 
ATOM   7266  H  HA   . SER B 1 133 ? 25.727  4.713   2.857   1.00 6.74   ?  356  SER B HA   1 
ATOM   7267  H  HB2  . SER B 1 133 ? 26.602  4.535   5.554   1.00 7.23   ?  356  SER B HB2  1 
ATOM   7268  H  HB3  . SER B 1 133 ? 25.506  5.566   5.043   1.00 7.23   ?  356  SER B HB3  1 
ATOM   7269  H  HG   . SER B 1 133 ? 25.167  2.947   5.114   1.00 7.29   ?  356  SER B HG   1 
ATOM   7270  N  N    . HIS B 1 134 ? 27.092  6.805   2.820   1.00 5.27   ?  357  HIS B N    1 
ATOM   7271  C  CA   . HIS B 1 134 ? 27.973  7.947   2.609   1.00 5.36   ?  357  HIS B CA   1 
ATOM   7272  C  C    . HIS B 1 134 ? 27.163  9.231   2.723   1.00 5.49   ?  357  HIS B C    1 
ATOM   7273  O  O    . HIS B 1 134 ? 25.940  9.230   2.573   1.00 6.25   ?  357  HIS B O    1 
ATOM   7274  C  CB   . HIS B 1 134 ? 28.644  7.894   1.223   1.00 6.53   ?  357  HIS B CB   1 
ATOM   7275  C  CG   . HIS B 1 134 ? 29.495  6.693   1.034   1.00 6.12   ?  357  HIS B CG   1 
ATOM   7276  N  ND1  . HIS B 1 134 ? 30.693  6.535   1.693   1.00 6.98   ?  357  HIS B ND1  1 
ATOM   7277  C  CD2  . HIS B 1 134 ? 29.300  5.572   0.302   1.00 6.77   ?  357  HIS B CD2  1 
ATOM   7278  C  CE1  . HIS B 1 134 ? 31.208  5.367   1.361   1.00 7.62   ?  357  HIS B CE1  1 
ATOM   7279  N  NE2  . HIS B 1 134 ? 30.389  4.766   0.512   1.00 7.68   ?  357  HIS B NE2  1 
ATOM   7280  H  H    . HIS B 1 134 ? 26.281  6.959   2.579   1.00 6.33   ?  357  HIS B H    1 
ATOM   7281  H  HA   . HIS B 1 134 ? 28.659  7.943   3.295   1.00 6.44   ?  357  HIS B HA   1 
ATOM   7282  H  HB2  . HIS B 1 134 ? 27.955  7.884   0.540   1.00 7.84   ?  357  HIS B HB2  1 
ATOM   7283  H  HB3  . HIS B 1 134 ? 29.206  8.678   1.115   1.00 7.84   ?  357  HIS B HB3  1 
ATOM   7284  H  HD2  . HIS B 1 134 ? 28.568  5.385   -0.239  1.00 8.12   ?  357  HIS B HD2  1 
ATOM   7285  H  HE1  . HIS B 1 134 ? 32.014  5.022   1.671   1.00 9.15   ?  357  HIS B HE1  1 
ATOM   7286  H  HE2  . HIS B 1 134 ? 30.518  3.996   0.152   1.00 9.21   ?  357  HIS B HE2  1 
ATOM   7287  N  N    . GLN B 1 135 ? 27.857  10.336  2.973   1.00 5.37   ?  358  GLN B N    1 
ATOM   7288  C  CA   . GLN B 1 135 ? 27.191  11.626  2.972   1.00 5.15   ?  358  GLN B CA   1 
ATOM   7289  C  C    . GLN B 1 135 ? 26.777  12.022  1.565   1.00 5.41   ?  358  GLN B C    1 
ATOM   7290  O  O    . GLN B 1 135 ? 27.431  11.685  0.579   1.00 6.46   ?  358  GLN B O    1 
ATOM   7291  C  CB   . GLN B 1 135 ? 28.143  12.691  3.482   1.00 5.53   ?  358  GLN B CB   1 
ATOM   7292  C  CG   . GLN B 1 135 ? 28.623  12.480  4.906   1.00 6.86   ?  358  GLN B CG   1 
ATOM   7293  C  CD   . GLN B 1 135 ? 29.782  13.382  5.239   1.00 7.58   ?  358  GLN B CD   1 
ATOM   7294  O  OE1  . GLN B 1 135 ? 29.632  14.435  5.875   1.00 7.85   ?  358  GLN B OE1  1 
ATOM   7295  N  NE2  . GLN B 1 135 ? 30.945  12.997  4.782   1.00 8.89   ?  358  GLN B NE2  1 
ATOM   7296  H  H    . GLN B 1 135 ? 28.699  10.363  3.144   1.00 6.45   ?  358  GLN B H    1 
ATOM   7297  H  HA   . GLN B 1 135 ? 26.405  11.575  3.538   1.00 6.18   ?  358  GLN B HA   1 
ATOM   7298  H  HB2  . GLN B 1 135 ? 28.925  12.705  2.909   1.00 6.64   ?  358  GLN B HB2  1 
ATOM   7299  H  HB3  . GLN B 1 135 ? 27.692  13.549  3.450   1.00 6.64   ?  358  GLN B HB3  1 
ATOM   7300  H  HG2  . GLN B 1 135 ? 27.898  12.675  5.520   1.00 8.23   ?  358  GLN B HG2  1 
ATOM   7301  H  HG3  . GLN B 1 135 ? 28.911  11.560  5.014   1.00 8.23   ?  358  GLN B HG3  1 
ATOM   7302  H  HE21 . GLN B 1 135 ? 31.009  12.271  4.324   1.00 10.67  ?  358  GLN B HE21 1 
ATOM   7303  H  HE22 . GLN B 1 135 ? 31.647  13.469  4.938   1.00 10.67  ?  358  GLN B HE22 1 
ATOM   7304  N  N    . GLY B 1 136 ? 25.693  12.789  1.485   1.00 5.56   ?  359  GLY B N    1 
ATOM   7305  C  CA   . GLY B 1 136 ? 25.269  13.343  0.216   1.00 6.15   ?  359  GLY B CA   1 
ATOM   7306  C  C    . GLY B 1 136 ? 24.504  14.634  0.406   1.00 6.26   ?  359  GLY B C    1 
ATOM   7307  O  O    . GLY B 1 136 ? 24.051  14.968  1.508   1.00 6.25   ?  359  GLY B O    1 
ATOM   7308  H  H    . GLY B 1 136 ? 25.191  12.999  2.152   1.00 6.67   ?  359  GLY B H    1 
ATOM   7309  H  HA2  . GLY B 1 136 ? 26.046  13.522  -0.337  1.00 7.38   ?  359  GLY B HA2  1 
ATOM   7310  H  HA3  . GLY B 1 136 ? 24.695  12.708  -0.242  1.00 7.38   ?  359  GLY B HA3  1 
ATOM   7311  N  N    . VAL B 1 137 ? 24.340  15.348  -0.710  1.00 5.36   ?  360  VAL B N    1 
ATOM   7312  C  CA   . VAL B 1 137 ? 23.532  16.555  -0.760  1.00 5.88   ?  360  VAL B CA   1 
ATOM   7313  C  C    . VAL B 1 137 ? 22.511  16.402  -1.867  1.00 5.79   ?  360  VAL B C    1 
ATOM   7314  O  O    . VAL B 1 137 ? 22.859  16.011  -2.988  1.00 6.48   ?  360  VAL B O    1 
ATOM   7315  C  CB   . VAL B 1 137 ? 24.394  17.805  -1.010  1.00 6.87   ?  360  VAL B CB   1 
ATOM   7316  C  CG1  . VAL B 1 137 ? 23.532  19.062  -1.220  1.00 8.40   ?  360  VAL B CG1  1 
ATOM   7317  C  CG2  . VAL B 1 137 ? 25.323  18.037  0.132   1.00 10.02  ?  360  VAL B CG2  1 
ATOM   7318  H  H    . VAL B 1 137 ? 24.696  15.142  -1.466  1.00 6.43   ?  360  VAL B H    1 
ATOM   7319  H  HA   . VAL B 1 137 ? 23.064  16.661  0.083   1.00 7.06   ?  360  VAL B HA   1 
ATOM   7320  H  HB   . VAL B 1 137 ? 24.906  17.647  -1.819  1.00 8.25   ?  360  VAL B HB   1 
ATOM   7321  H  HG11 . VAL B 1 137 ? 24.095  19.848  -1.137  1.00 10.08  ?  360  VAL B HG11 1 
ATOM   7322  H  HG12 . VAL B 1 137 ? 23.138  19.029  -2.105  1.00 10.08  ?  360  VAL B HG12 1 
ATOM   7323  H  HG13 . VAL B 1 137 ? 22.834  19.082  -0.547  1.00 10.08  ?  360  VAL B HG13 1 
ATOM   7324  H  HG21 . VAL B 1 137 ? 26.018  18.654  -0.146  1.00 12.02  ?  360  VAL B HG21 1 
ATOM   7325  H  HG22 . VAL B 1 137 ? 24.824  18.414  0.874   1.00 12.02  ?  360  VAL B HG22 1 
ATOM   7326  H  HG23 . VAL B 1 137 ? 25.718  17.191  0.396   1.00 12.02  ?  360  VAL B HG23 1 
ATOM   7327  N  N    . ILE B 1 138 ? 21.267  16.734  -1.555  1.00 5.68   ?  361  ILE B N    1 
ATOM   7328  C  CA   . ILE B 1 138 ? 20.187  16.791  -2.529  1.00 5.71   ?  361  ILE B CA   1 
ATOM   7329  C  C    . ILE B 1 138 ? 19.825  18.265  -2.690  1.00 5.61   ?  361  ILE B C    1 
ATOM   7330  O  O    . ILE B 1 138 ? 19.260  18.891  -1.774  1.00 6.31   ?  361  ILE B O    1 
ATOM   7331  C  CB   . ILE B 1 138 ? 18.981  15.936  -2.116  1.00 5.91   ?  361  ILE B CB   1 
ATOM   7332  C  CG1  . ILE B 1 138 ? 19.369  14.462  -2.065  1.00 6.95   ?  361  ILE B CG1  1 
ATOM   7333  C  CG2  . ILE B 1 138 ? 17.809  16.171  -3.061  1.00 6.93   ?  361  ILE B CG2  1 
ATOM   7334  C  CD1  . ILE B 1 138 ? 18.306  13.562  -1.469  1.00 7.32   ?  361  ILE B CD1  1 
ATOM   7335  H  H    . ILE B 1 138 ? 21.015  16.936  -0.758  1.00 6.82   ?  361  ILE B H    1 
ATOM   7336  H  HA   . ILE B 1 138 ? 20.495  16.453  -3.385  1.00 6.85   ?  361  ILE B HA   1 
ATOM   7337  H  HB   . ILE B 1 138 ? 18.702  16.203  -1.227  1.00 7.10   ?  361  ILE B HB   1 
ATOM   7338  H  HG12 . ILE B 1 138 ? 19.542  14.155  -2.969  1.00 8.34   ?  361  ILE B HG12 1 
ATOM   7339  H  HG13 . ILE B 1 138 ? 20.169  14.370  -1.525  1.00 8.34   ?  361  ILE B HG13 1 
ATOM   7340  H  HG21 . ILE B 1 138 ? 17.113  15.524  -2.868  1.00 8.32   ?  361  ILE B HG21 1 
ATOM   7341  H  HG22 . ILE B 1 138 ? 17.471  17.071  -2.928  1.00 8.32   ?  361  ILE B HG22 1 
ATOM   7342  H  HG23 . ILE B 1 138 ? 18.114  16.065  -3.976  1.00 8.32   ?  361  ILE B HG23 1 
ATOM   7343  H  HD11 . ILE B 1 138 ? 18.687  12.684  -1.312  1.00 8.79   ?  361  ILE B HD11 1 
ATOM   7344  H  HD12 . ILE B 1 138 ? 18.001  13.946  -0.631  1.00 8.79   ?  361  ILE B HD12 1 
ATOM   7345  H  HD13 . ILE B 1 138 ? 17.564  13.495  -2.090  1.00 8.79   ?  361  ILE B HD13 1 
ATOM   7346  N  N    . SER B 1 139 ? 20.158  18.832  -3.847  1.00 5.23   ?  362  SER B N    1 
ATOM   7347  C  CA   . SER B 1 139 ? 19.763  20.194  -4.157  1.00 5.65   ?  362  SER B CA   1 
ATOM   7348  C  C    . SER B 1 139 ? 18.290  20.236  -4.518  1.00 5.94   ?  362  SER B C    1 
ATOM   7349  O  O    . SER B 1 139 ? 17.873  19.597  -5.491  1.00 7.81   ?  362  SER B O    1 
ATOM   7350  C  CB   . SER B 1 139 ? 20.575  20.701  -5.337  1.00 7.00   ?  362  SER B CB   1 
ATOM   7351  O  OG   . SER B 1 139 ? 20.068  21.963  -5.723  1.00 8.05   ?  362  SER B OG   1 
ATOM   7352  H  H    . SER B 1 139 ? 20.612  18.445  -4.466  1.00 6.28   ?  362  SER B H    1 
ATOM   7353  H  HA   . SER B 1 139 ? 19.915  20.754  -3.379  1.00 6.79   ?  362  SER B HA   1 
ATOM   7354  H  HB2  . SER B 1 139 ? 21.505  20.790  -5.076  1.00 8.40   ?  362  SER B HB2  1 
ATOM   7355  H  HB3  . SER B 1 139 ? 20.496  20.078  -6.077  1.00 8.40   ?  362  SER B HB3  1 
ATOM   7356  H  HG   . SER B 1 139 ? 20.512  22.265  -6.369  1.00 9.66   ?  362  SER B HG   1 
ATOM   7357  N  N    . THR B 1 140 ? 17.500  21.007  -3.786  1.00 5.66   ?  363  THR B N    1 
ATOM   7358  C  CA   . THR B 1 140 ? 16.089  21.122  -4.132  1.00 5.68   ?  363  THR B CA   1 
ATOM   7359  C  C    . THR B 1 140 ? 15.839  22.197  -5.179  1.00 6.72   ?  363  THR B C    1 
ATOM   7360  O  O    . THR B 1 140 ? 14.681  22.435  -5.534  1.00 8.26   ?  363  THR B O    1 
ATOM   7361  C  CB   . THR B 1 140 ? 15.199  21.355  -2.914  1.00 6.33   ?  363  THR B CB   1 
ATOM   7362  O  OG1  . THR B 1 140 ? 15.419  22.671  -2.437  1.00 6.52   ?  363  THR B OG1  1 
ATOM   7363  C  CG2  . THR B 1 140 ? 15.493  20.369  -1.824  1.00 7.34   ?  363  THR B CG2  1 
ATOM   7364  H  H    . THR B 1 140 ? 17.751  21.463  -3.102  1.00 6.80   ?  363  THR B H    1 
ATOM   7365  H  HA   . THR B 1 140 ? 15.809  20.266  -4.491  1.00 6.82   ?  363  THR B HA   1 
ATOM   7366  H  HB   . THR B 1 140 ? 14.269  21.239  -3.164  1.00 7.59   ?  363  THR B HB   1 
ATOM   7367  H  HG1  . THR B 1 140 ? 14.909  22.831  -1.789  1.00 7.82   ?  363  THR B HG1  1 
ATOM   7368  H  HG21 . THR B 1 140 ? 14.867  20.488  -1.092  1.00 8.81   ?  363  THR B HG21 1 
ATOM   7369  H  HG22 . THR B 1 140 ? 15.411  19.465  -2.164  1.00 8.81   ?  363  THR B HG22 1 
ATOM   7370  H  HG23 . THR B 1 140 ? 16.394  20.501  -1.492  1.00 8.81   ?  363  THR B HG23 1 
ATOM   7371  N  N    . ILE B 1 141 ? 16.898  22.852  -5.650  1.00 6.90   ?  364  ILE B N    1 
ATOM   7372  C  CA   . ILE B 1 141 ? 16.786  23.846  -6.707  1.00 8.96   ?  364  ILE B CA   1 
ATOM   7373  C  C    . ILE B 1 141 ? 17.278  23.350  -8.056  1.00 9.30   ?  364  ILE B C    1 
ATOM   7374  O  O    . ILE B 1 141 ? 17.086  24.043  -9.061  1.00 11.55  ?  364  ILE B O    1 
ATOM   7375  C  CB   . ILE B 1 141 ? 17.465  25.174  -6.327  1.00 10.82  ?  364  ILE B CB   1 
ATOM   7376  C  CG1  . ILE B 1 141 ? 18.979  25.029  -6.289  1.00 11.71  ?  364  ILE B CG1  1 
ATOM   7377  C  CG2  . ILE B 1 141 ? 16.975  25.675  -4.969  1.00 12.19  ?  364  ILE B CG2  1 
ATOM   7378  C  CD1  . ILE B 1 141 ? 19.667  26.365  -6.337  1.00 13.22  ?  364  ILE B CD1  1 
ATOM   7379  H  H    . ILE B 1 141 ? 17.702  22.736  -5.369  1.00 8.28   ?  364  ILE B H    1 
ATOM   7380  H  HA   . ILE B 1 141 ? 15.842  24.042  -6.817  1.00 10.75  ?  364  ILE B HA   1 
ATOM   7381  H  HB   . ILE B 1 141 ? 17.225  25.817  -7.013  1.00 12.99  ?  364  ILE B HB   1 
ATOM   7382  H  HG12 . ILE B 1 141 ? 19.237  24.582  -5.467  1.00 14.05  ?  364  ILE B HG12 1 
ATOM   7383  H  HG13 . ILE B 1 141 ? 19.270  24.509  -7.054  1.00 14.05  ?  364  ILE B HG13 1 
ATOM   7384  H  HG21 . ILE B 1 141 ? 17.317  26.570  -4.821  1.00 14.63  ?  364  ILE B HG21 1 
ATOM   7385  H  HG22 . ILE B 1 141 ? 16.005  25.687  -4.969  1.00 14.63  ?  364  ILE B HG22 1 
ATOM   7386  H  HG23 . ILE B 1 141 ? 17.298  25.077  -4.277  1.00 14.63  ?  364  ILE B HG23 1 
ATOM   7387  H  HD11 . ILE B 1 141 ? 20.625  26.225  -6.391  1.00 15.87  ?  364  ILE B HD11 1 
ATOM   7388  H  HD12 . ILE B 1 141 ? 19.359  26.851  -7.118  1.00 15.87  ?  364  ILE B HD12 1 
ATOM   7389  H  HD13 . ILE B 1 141 ? 19.450  26.861  -5.532  1.00 15.87  ?  364  ILE B HD13 1 
ATOM   7390  N  N    . SER B 1 142 ? 17.907  22.187  -8.111  1.00 9.15   ?  365  SER B N    1 
ATOM   7391  C  CA   . SER B 1 142 ? 18.435  21.668  -9.354  1.00 9.50   ?  365  SER B CA   1 
ATOM   7392  C  C    . SER B 1 142 ? 17.300  21.412  -10.336 1.00 9.19   ?  365  SER B C    1 
ATOM   7393  O  O    . SER B 1 142 ? 16.218  20.983  -9.938  1.00 9.31   ?  365  SER B O    1 
ATOM   7394  C  CB   . SER B 1 142 ? 19.133  20.337  -9.069  1.00 10.83  ?  365  SER B CB   1 
ATOM   7395  O  OG   . SER B 1 142 ? 19.434  19.660  -10.274 1.00 12.08  ?  365  SER B OG   1 
ATOM   7396  H  H    . SER B 1 142 ? 18.041  21.675  -7.433  1.00 10.98  ?  365  SER B H    1 
ATOM   7397  H  HA   . SER B 1 142 ? 19.055  22.302  -9.747  1.00 11.40  ?  365  SER B HA   1 
ATOM   7398  H  HB2  . SER B 1 142 ? 19.958  20.510  -8.589  1.00 12.99  ?  365  SER B HB2  1 
ATOM   7399  H  HB3  . SER B 1 142 ? 18.547  19.781  -8.532  1.00 12.99  ?  365  SER B HB3  1 
ATOM   7400  H  HG   . SER B 1 142 ? 19.947  20.128  -10.746 1.00 14.50  ?  365  SER B HG   1 
ATOM   7401  N  N    . PRO B 1 143 ? 17.545  21.590  -11.638 1.00 10.16  ?  366  PRO B N    1 
ATOM   7402  C  CA   . PRO B 1 143 ? 16.561  21.127  -12.632 1.00 11.21  ?  366  PRO B CA   1 
ATOM   7403  C  C    . PRO B 1 143 ? 16.276  19.639  -12.532 1.00 9.92   ?  366  PRO B C    1 
ATOM   7404  O  O    . PRO B 1 143 ? 15.257  19.177  -13.057 1.00 10.73  ?  366  PRO B O    1 
ATOM   7405  C  CB   . PRO B 1 143 ? 17.209  21.478  -13.983 1.00 13.89  ?  366  PRO B CB   1 
ATOM   7406  C  CG   . PRO B 1 143 ? 18.259  22.449  -13.691 1.00 15.39  ?  366  PRO B CG   1 
ATOM   7407  C  CD   . PRO B 1 143 ? 18.704  22.244  -12.271 1.00 13.02  ?  366  PRO B CD   1 
ATOM   7408  H  HA   . PRO B 1 143 ? 15.736  21.629  -12.541 1.00 13.45  ?  366  PRO B HA   1 
ATOM   7409  H  HB2  . PRO B 1 143 ? 17.584  20.677  -14.381 1.00 16.67  ?  366  PRO B HB2  1 
ATOM   7410  H  HB3  . PRO B 1 143 ? 16.542  21.862  -14.573 1.00 16.67  ?  366  PRO B HB3  1 
ATOM   7411  H  HG2  . PRO B 1 143 ? 19.001  22.307  -14.298 1.00 18.47  ?  366  PRO B HG2  1 
ATOM   7412  H  HG3  . PRO B 1 143 ? 17.904  23.345  -13.804 1.00 18.47  ?  366  PRO B HG3  1 
ATOM   7413  H  HD2  . PRO B 1 143 ? 19.485  21.671  -12.234 1.00 15.63  ?  366  PRO B HD2  1 
ATOM   7414  H  HD3  . PRO B 1 143 ? 18.896  23.094  -11.844 1.00 15.63  ?  366  PRO B HD3  1 
ATOM   7415  N  N    . LYS B 1 144 ? 17.162  18.875  -11.900 1.00 9.75   ?  367  LYS B N    1 
ATOM   7416  C  CA   . LYS B 1 144 ? 16.995  17.444  -11.719 1.00 10.71  ?  367  LYS B CA   1 
ATOM   7417  C  C    . LYS B 1 144 ? 16.227  17.104  -10.458 1.00 8.46   ?  367  LYS B C    1 
ATOM   7418  O  O    . LYS B 1 144 ? 15.997  15.922  -10.198 1.00 8.34   ?  367  LYS B O    1 
ATOM   7419  C  CB   . LYS B 1 144 ? 18.369  16.762  -11.691 1.00 15.13  ?  367  LYS B CB   1 
ATOM   7420  C  CG   . LYS B 1 144 ? 19.183  16.946  -12.968 1.00 20.19  ?  367  LYS B CG   1 
ATOM   7421  C  CD   . LYS B 1 144 ? 18.490  16.292  -14.157 1.00 24.29  ?  367  LYS B CD   1 
ATOM   7422  C  CE   . LYS B 1 144 ? 19.342  16.331  -15.437 1.00 27.28  ?  367  LYS B CE   1 
ATOM   7423  N  NZ   . LYS B 1 144 ? 20.480  15.378  -15.446 1.00 29.81  ?  367  LYS B NZ   1 
ATOM   7424  H  H    . LYS B 1 144 ? 17.891  19.176  -11.557 1.00 11.70  ?  367  LYS B H    1 
ATOM   7425  H  HA   . LYS B 1 144 ? 16.499  17.085  -12.472 1.00 12.85  ?  367  LYS B HA   1 
ATOM   7426  H  HB2  . LYS B 1 144 ? 18.885  17.132  -10.958 1.00 18.16  ?  367  LYS B HB2  1 
ATOM   7427  H  HB3  . LYS B 1 144 ? 18.240  15.809  -11.559 1.00 18.16  ?  367  LYS B HB3  1 
ATOM   7428  H  HG2  . LYS B 1 144 ? 19.283  17.893  -13.153 1.00 24.23  ?  367  LYS B HG2  1 
ATOM   7429  H  HG3  . LYS B 1 144 ? 20.055  16.535  -12.857 1.00 24.23  ?  367  LYS B HG3  1 
ATOM   7430  H  HD2  . LYS B 1 144 ? 18.309  15.363  -13.946 1.00 29.15  ?  367  LYS B HD2  1 
ATOM   7431  H  HD3  . LYS B 1 144 ? 17.660  16.760  -14.336 1.00 29.15  ?  367  LYS B HD3  1 
ATOM   7432  H  HE2  . LYS B 1 144 ? 18.774  16.116  -16.194 1.00 32.74  ?  367  LYS B HE2  1 
ATOM   7433  H  HE3  . LYS B 1 144 ? 19.707  17.224  -15.539 1.00 32.74  ?  367  LYS B HE3  1 
ATOM   7434  H  HZ1  . LYS B 1 144 ? 20.180  14.544  -15.364 1.00 35.78  ?  367  LYS B HZ1  1 
ATOM   7435  H  HZ2  . LYS B 1 144 ? 20.930  15.449  -16.210 1.00 35.78  ?  367  LYS B HZ2  1 
ATOM   7436  H  HZ3  . LYS B 1 144 ? 21.030  15.555  -14.769 1.00 35.78  ?  367  LYS B HZ3  1 
ATOM   7437  N  N    . PHE B 1 145 ? 15.827  18.100  -9.671  1.00 7.69   ?  368  PHE B N    1 
ATOM   7438  C  CA   . PHE B 1 145 ? 14.957  17.862  -8.515  1.00 6.76   ?  368  PHE B CA   1 
ATOM   7439  C  C    . PHE B 1 145 ? 13.532  17.831  -9.040  1.00 6.89   ?  368  PHE B C    1 
ATOM   7440  O  O    . PHE B 1 145 ? 12.892  18.872  -9.220  1.00 7.22   ?  368  PHE B O    1 
ATOM   7441  C  CB   . PHE B 1 145 ? 15.146  18.950  -7.466  1.00 6.51   ?  368  PHE B CB   1 
ATOM   7442  C  CG   . PHE B 1 145 ? 14.354  18.722  -6.212  1.00 6.57   ?  368  PHE B CG   1 
ATOM   7443  C  CD1  . PHE B 1 145 ? 14.807  17.816  -5.258  1.00 6.69   ?  368  PHE B CD1  1 
ATOM   7444  C  CD2  . PHE B 1 145 ? 13.170  19.402  -5.978  1.00 7.39   ?  368  PHE B CD2  1 
ATOM   7445  C  CE1  . PHE B 1 145 ? 14.096  17.603  -4.099  1.00 7.42   ?  368  PHE B CE1  1 
ATOM   7446  C  CE2  . PHE B 1 145 ? 12.447  19.183  -4.810  1.00 7.10   ?  368  PHE B CE2  1 
ATOM   7447  C  CZ   . PHE B 1 145 ? 12.911  18.280  -3.877  1.00 7.76   ?  368  PHE B CZ   1 
ATOM   7448  H  H    . PHE B 1 145 ? 16.045  18.924  -9.785  1.00 9.23   ?  368  PHE B H    1 
ATOM   7449  H  HA   . PHE B 1 145 ? 15.168  17.011  -8.101  1.00 8.11   ?  368  PHE B HA   1 
ATOM   7450  H  HB2  . PHE B 1 145 ? 16.084  18.988  -7.221  1.00 7.82   ?  368  PHE B HB2  1 
ATOM   7451  H  HB3  . PHE B 1 145 ? 14.867  19.799  -7.843  1.00 7.82   ?  368  PHE B HB3  1 
ATOM   7452  H  HD1  . PHE B 1 145 ? 15.599  17.351  -5.405  1.00 8.04   ?  368  PHE B HD1  1 
ATOM   7453  H  HD2  . PHE B 1 145 ? 12.856  20.011  -6.607  1.00 8.87   ?  368  PHE B HD2  1 
ATOM   7454  H  HE1  . PHE B 1 145 ? 14.413  17.002  -3.463  1.00 8.91   ?  368  PHE B HE1  1 
ATOM   7455  H  HE2  . PHE B 1 145 ? 11.653  19.644  -4.659  1.00 8.52   ?  368  PHE B HE2  1 
ATOM   7456  H  HZ   . PHE B 1 145 ? 12.427  18.126  -3.099  1.00 9.32   ?  368  PHE B HZ   1 
ATOM   7457  N  N    . VAL B 1 146 ? 13.060  16.632  -9.351  1.00 6.89   ?  369  VAL B N    1 
ATOM   7458  C  CA   . VAL B 1 146 ? 11.730  16.442  -9.924  1.00 6.67   ?  369  VAL B CA   1 
ATOM   7459  C  C    . VAL B 1 146 ? 10.989  15.352  -9.153  1.00 6.19   ?  369  VAL B C    1 
ATOM   7460  O  O    . VAL B 1 146 ? 10.530  14.355  -9.731  1.00 6.77   ?  369  VAL B O    1 
ATOM   7461  C  CB   . VAL B 1 146 ? 11.799  16.202  -11.441 1.00 7.39   ?  369  VAL B CB   1 
ATOM   7462  C  CG1  . VAL B 1 146 ? 12.252  17.477  -12.147 1.00 8.08   ?  369  VAL B CG1  1 
ATOM   7463  C  CG2  . VAL B 1 146 ? 12.711  15.036  -11.809 1.00 7.95   ?  369  VAL B CG2  1 
ATOM   7464  H  H    . VAL B 1 146 ? 13.496  15.899  -9.239  1.00 8.27   ?  369  VAL B H    1 
ATOM   7465  H  HA   . VAL B 1 146 ? 11.208  17.250  -9.800  1.00 8.00   ?  369  VAL B HA   1 
ATOM   7466  H  HB   . VAL B 1 146 ? 10.909  15.963  -11.743 1.00 8.88   ?  369  VAL B HB   1 
ATOM   7467  H  HG11 . VAL B 1 146 ? 12.264  17.321  -13.104 1.00 9.70   ?  369  VAL B HG11 1 
ATOM   7468  H  HG12 . VAL B 1 146 ? 11.632  18.192  -11.936 1.00 9.70   ?  369  VAL B HG12 1 
ATOM   7469  H  HG13 . VAL B 1 146 ? 13.142  17.709  -11.838 1.00 9.70   ?  369  VAL B HG13 1 
ATOM   7470  H  HG21 . VAL B 1 146 ? 12.699  14.917  -12.772 1.00 9.54   ?  369  VAL B HG21 1 
ATOM   7471  H  HG22 . VAL B 1 146 ? 13.613  15.235  -11.512 1.00 9.54   ?  369  VAL B HG22 1 
ATOM   7472  H  HG23 . VAL B 1 146 ? 12.389  14.232  -11.373 1.00 9.54   ?  369  VAL B HG23 1 
ATOM   7473  N  N    . PRO B 1 147 ? 10.821  15.522  -7.839  1.00 6.29   ?  370  PRO B N    1 
ATOM   7474  C  CA   . PRO B 1 147 ? 10.203  14.442  -7.049  1.00 6.51   ?  370  PRO B CA   1 
ATOM   7475  C  C    . PRO B 1 147 ? 8.798   14.079  -7.498  1.00 6.74   ?  370  PRO B C    1 
ATOM   7476  O  O    . PRO B 1 147 ? 8.418   12.904  -7.417  1.00 7.59   ?  370  PRO B O    1 
ATOM   7477  C  CB   . PRO B 1 147 ? 10.247  14.993  -5.608  1.00 5.99   ?  370  PRO B CB   1 
ATOM   7478  C  CG   . PRO B 1 147 ? 10.284  16.512  -5.806  1.00 5.40   ?  370  PRO B CG   1 
ATOM   7479  C  CD   . PRO B 1 147 ? 11.164  16.687  -7.003  1.00 5.60   ?  370  PRO B CD   1 
ATOM   7480  H  HA   . PRO B 1 147 ? 10.752  13.643  -7.093  1.00 7.81   ?  370  PRO B HA   1 
ATOM   7481  H  HB2  . PRO B 1 147 ? 9.454   14.720  -5.120  1.00 7.19   ?  370  PRO B HB2  1 
ATOM   7482  H  HB3  . PRO B 1 147 ? 11.042  14.677  -5.151  1.00 7.19   ?  370  PRO B HB3  1 
ATOM   7483  H  HG2  . PRO B 1 147 ? 9.390   16.851  -5.974  1.00 6.48   ?  370  PRO B HG2  1 
ATOM   7484  H  HG3  . PRO B 1 147 ? 10.661  16.944  -5.025  1.00 6.48   ?  370  PRO B HG3  1 
ATOM   7485  H  HD2  . PRO B 1 147 ? 10.962  17.516  -7.464  1.00 6.72   ?  370  PRO B HD2  1 
ATOM   7486  H  HD3  . PRO B 1 147 ? 12.101  16.669  -6.750  1.00 6.72   ?  370  PRO B HD3  1 
ATOM   7487  N  N    . LYS B 1 148 ? 8.019   15.046  -7.983  1.00 7.02   ?  371  LYS B N    1 
ATOM   7488  C  CA   A LYS B 1 148 ? 6.680   14.744  -8.496  0.77 7.99   ?  371  LYS B CA   1 
ATOM   7489  C  CA   B LYS B 1 148 ? 6.682   14.743  -8.491  0.23 7.94   ?  371  LYS B CA   1 
ATOM   7490  C  C    . LYS B 1 148 ? 6.747   13.818  -9.697  1.00 8.55   ?  371  LYS B C    1 
ATOM   7491  O  O    . LYS B 1 148 ? 5.795   13.076  -9.961  1.00 10.51  ?  371  LYS B O    1 
ATOM   7492  C  CB   A LYS B 1 148 ? 5.982   16.064  -8.855  0.77 9.27   ?  371  LYS B CB   1 
ATOM   7493  C  CB   B LYS B 1 148 ? 5.968   16.051  -8.843  0.23 8.50   ?  371  LYS B CB   1 
ATOM   7494  C  CG   A LYS B 1 148 ? 4.671   15.986  -9.621  0.77 12.32  ?  371  LYS B CG   1 
ATOM   7495  C  CG   B LYS B 1 148 ? 4.522   15.914  -9.287  0.23 9.65   ?  371  LYS B CG   1 
ATOM   7496  C  CD   A LYS B 1 148 ? 3.516   15.588  -8.747  0.77 12.44  ?  371  LYS B CD   1 
ATOM   7497  C  CD   B LYS B 1 148 ? 3.667   15.208  -8.266  0.23 10.67  ?  371  LYS B CD   1 
ATOM   7498  C  CE   A LYS B 1 148 ? 2.156   16.035  -9.337  0.77 13.32  ?  371  LYS B CE   1 
ATOM   7499  C  CE   B LYS B 1 148 ? 2.187   15.353  -8.591  0.23 11.54  ?  371  LYS B CE   1 
ATOM   7500  N  NZ   A LYS B 1 148 ? 1.024   15.412  -8.598  0.77 13.86  ?  371  LYS B NZ   1 
ATOM   7501  N  NZ   B LYS B 1 148 ? 1.744   16.778  -8.581  0.23 12.37  ?  371  LYS B NZ   1 
ATOM   7502  H  H    . LYS B 1 148 ? 8.235   15.877  -8.028  1.00 8.43   ?  371  LYS B H    1 
ATOM   7503  H  HA   . LYS B 1 148 ? 6.155   14.296  -7.815  1.00 9.53   ?  371  LYS B HA   1 
ATOM   7504  H  HB2  A LYS B 1 148 ? 5.794   16.535  -8.028  0.77 11.13  ?  371  LYS B HB2  1 
ATOM   7505  H  HB2  B LYS B 1 148 ? 5.975   16.622  -8.058  0.23 10.20  ?  371  LYS B HB2  1 
ATOM   7506  H  HB3  A LYS B 1 148 ? 6.593   16.584  -9.401  0.77 11.13  ?  371  LYS B HB3  1 
ATOM   7507  H  HB3  B LYS B 1 148 ? 6.452   16.477  -9.567  0.23 10.20  ?  371  LYS B HB3  1 
ATOM   7508  H  HG2  A LYS B 1 148 ? 4.474   16.856  -10.002 0.77 14.79  ?  371  LYS B HG2  1 
ATOM   7509  H  HG2  B LYS B 1 148 ? 4.149   16.798  -9.431  0.23 11.59  ?  371  LYS B HG2  1 
ATOM   7510  H  HG3  A LYS B 1 148 ? 4.755   15.326  -10.327 0.77 14.79  ?  371  LYS B HG3  1 
ATOM   7511  H  HG3  B LYS B 1 148 ? 4.490   15.403  -10.111 0.23 11.59  ?  371  LYS B HG3  1 
ATOM   7512  H  HD2  A LYS B 1 148 ? 3.503   14.623  -8.656  0.77 14.93  ?  371  LYS B HD2  1 
ATOM   7513  H  HD2  B LYS B 1 148 ? 3.887   14.263  -8.259  0.23 12.81  ?  371  LYS B HD2  1 
ATOM   7514  H  HD3  A LYS B 1 148 ? 3.618   16.002  -7.876  0.77 14.93  ?  371  LYS B HD3  1 
ATOM   7515  H  HD3  B LYS B 1 148 ? 3.827   15.592  -7.390  0.23 12.81  ?  371  LYS B HD3  1 
ATOM   7516  H  HE2  A LYS B 1 148 ? 2.075   16.999  -9.268  0.77 15.98  ?  371  LYS B HE2  1 
ATOM   7517  H  HE2  B LYS B 1 148 ? 2.018   14.991  -9.475  0.23 13.85  ?  371  LYS B HE2  1 
ATOM   7518  H  HE3  A LYS B 1 148 ? 2.102   15.763  -10.267 0.77 15.98  ?  371  LYS B HE3  1 
ATOM   7519  H  HE3  B LYS B 1 148 ? 1.667   14.870  -7.930  0.23 13.85  ?  371  LYS B HE3  1 
ATOM   7520  H  HZ1  A LYS B 1 148 ? 1.086   14.525  -8.636  0.77 16.64  ?  371  LYS B HZ1  1 
ATOM   7521  H  HZ1  B LYS B 1 148 ? 0.858   16.821  -8.657  0.23 14.84  ?  371  LYS B HZ1  1 
ATOM   7522  H  HZ2  A LYS B 1 148 ? 1.041   15.666  -7.745  0.77 16.64  ?  371  LYS B HZ2  1 
ATOM   7523  H  HZ2  B LYS B 1 148 ? 2.114   17.216  -9.261  0.23 14.84  ?  371  LYS B HZ2  1 
ATOM   7524  H  HZ3  A LYS B 1 148 ? 0.250   15.663  -8.958  0.77 16.64  ?  371  LYS B HZ3  1 
ATOM   7525  H  HZ3  B LYS B 1 148 ? 1.988   17.167  -7.818  0.23 14.84  ?  371  LYS B HZ3  1 
ATOM   7526  N  N    . LEU B 1 149 ? 7.846   13.853  -10.431 1.00 8.08   ?  372  LEU B N    1 
ATOM   7527  C  CA   . LEU B 1 149 ? 8.087   12.987  -11.569 1.00 9.23   ?  372  LEU B CA   1 
ATOM   7528  C  C    . LEU B 1 149 ? 8.882   11.751  -11.194 1.00 9.40   ?  372  LEU B C    1 
ATOM   7529  O  O    . LEU B 1 149 ? 9.283   11.005  -12.085 1.00 11.85  ?  372  LEU B O    1 
ATOM   7530  C  CB   . LEU B 1 149 ? 8.829   13.762  -12.653 1.00 9.04   ?  372  LEU B CB   1 
ATOM   7531  C  CG   . LEU B 1 149 ? 8.141   15.051  -13.111 1.00 11.02  ?  372  LEU B CG   1 
ATOM   7532  C  CD1  . LEU B 1 149 ? 8.946   15.712  -14.226 1.00 11.92  ?  372  LEU B CD1  1 
ATOM   7533  C  CD2  . LEU B 1 149 ? 6.701   14.806  -13.553 1.00 12.60  ?  372  LEU B CD2  1 
ATOM   7534  H  H    . LEU B 1 149 ? 8.497   14.395  -10.283 1.00 9.70   ?  372  LEU B H    1 
ATOM   7535  H  HA   . LEU B 1 149 ? 7.235   12.698  -11.930 1.00 11.07  ?  372  LEU B HA   1 
ATOM   7536  H  HB2  . LEU B 1 149 ? 9.704   14.004  -12.312 1.00 10.84  ?  372  LEU B HB2  1 
ATOM   7537  H  HB3  . LEU B 1 149 ? 8.922   13.189  -13.430 1.00 10.84  ?  372  LEU B HB3  1 
ATOM   7538  H  HG   . LEU B 1 149 ? 8.102   15.658  -12.356 1.00 13.22  ?  372  LEU B HG   1 
ATOM   7539  H  HD11 . LEU B 1 149 ? 8.500   16.529  -14.496 1.00 14.30  ?  372  LEU B HD11 1 
ATOM   7540  H  HD12 . LEU B 1 149 ? 9.836   15.914  -13.896 1.00 14.30  ?  372  LEU B HD12 1 
ATOM   7541  H  HD13 . LEU B 1 149 ? 9.004   15.102  -14.978 1.00 14.30  ?  372  LEU B HD13 1 
ATOM   7542  H  HD21 . LEU B 1 149 ? 6.348   15.621  -13.945 1.00 15.13  ?  372  LEU B HD21 1 
ATOM   7543  H  HD22 . LEU B 1 149 ? 6.688   14.091  -14.208 1.00 15.13  ?  372  LEU B HD22 1 
ATOM   7544  H  HD23 . LEU B 1 149 ? 6.171   14.556  -12.779 1.00 15.13  ?  372  LEU B HD23 1 
ATOM   7545  N  N    . GLY B 1 150 ? 9.113   11.522  -9.917  1.00 8.20   ?  373  GLY B N    1 
ATOM   7546  C  CA   . GLY B 1 150 ? 9.703   10.281  -9.467  1.00 7.71   ?  373  GLY B CA   1 
ATOM   7547  C  C    . GLY B 1 150 ? 11.207  10.246  -9.255  1.00 7.37   ?  373  GLY B C    1 
ATOM   7548  O  O    . GLY B 1 150 ? 11.743  9.156   -9.027  1.00 7.85   ?  373  GLY B O    1 
ATOM   7549  H  H    . GLY B 1 150 ? 8.935   12.077  -9.284  1.00 9.84   ?  373  GLY B H    1 
ATOM   7550  H  HA2  . GLY B 1 150 ? 9.293   10.044  -8.621  1.00 9.26   ?  373  GLY B HA2  1 
ATOM   7551  H  HA3  . GLY B 1 150 ? 9.494   9.596   -10.122 1.00 9.26   ?  373  GLY B HA3  1 
ATOM   7552  N  N    . SER B 1 151 ? 11.914  11.377  -9.302  1.00 7.41   ?  374  SER B N    1 
ATOM   7553  C  CA   . SER B 1 151 ? 13.350  11.301  -9.071  1.00 7.05   ?  374  SER B CA   1 
ATOM   7554  C  C    . SER B 1 151 ? 13.922  12.622  -8.590  1.00 6.23   ?  374  SER B C    1 
ATOM   7555  O  O    . SER B 1 151 ? 13.357  13.697  -8.794  1.00 6.80   ?  374  SER B O    1 
ATOM   7556  C  CB   . SER B 1 151 ? 14.095  10.843  -10.333 1.00 7.95   ?  374  SER B CB   1 
ATOM   7557  O  OG   . SER B 1 151 ? 14.065  11.819  -11.355 1.00 9.25   ?  374  SER B OG   1 
ATOM   7558  H  H    . SER B 1 151 ? 11.597  12.161  -9.459  1.00 8.89   ?  374  SER B H    1 
ATOM   7559  H  HA   . SER B 1 151 ? 13.485  10.664  -8.352  1.00 8.47   ?  374  SER B HA   1 
ATOM   7560  H  HB2  . SER B 1 151 ? 15.020  10.667  -10.099 1.00 9.55   ?  374  SER B HB2  1 
ATOM   7561  H  HB3  . SER B 1 151 ? 13.676  10.033  -10.664 1.00 9.55   ?  374  SER B HB3  1 
ATOM   7562  H  HG   . SER B 1 151 ? 13.270  11.995  -11.561 1.00 11.10  ?  374  SER B HG   1 
ATOM   7563  N  N    . VAL B 1 152 ? 15.087  12.516  -7.955  1.00 6.40   ?  375  VAL B N    1 
ATOM   7564  C  CA   . VAL B 1 152 ? 15.923  13.641  -7.560  1.00 6.24   ?  375  VAL B CA   1 
ATOM   7565  C  C    . VAL B 1 152 ? 17.364  13.259  -7.877  1.00 6.30   ?  375  VAL B C    1 
ATOM   7566  O  O    . VAL B 1 152 ? 17.677  12.112  -8.177  1.00 7.95   ?  375  VAL B O    1 
ATOM   7567  C  CB   . VAL B 1 152 ? 15.767  13.996  -6.062  1.00 6.56   ?  375  VAL B CB   1 
ATOM   7568  C  CG1  . VAL B 1 152 ? 14.314  14.260  -5.751  1.00 6.85   ?  375  VAL B CG1  1 
ATOM   7569  C  CG2  . VAL B 1 152 ? 16.326  12.900  -5.168  1.00 7.37   ?  375  VAL B CG2  1 
ATOM   7570  H  H    . VAL B 1 152 ? 15.431  11.760  -7.731  1.00 7.68   ?  375  VAL B H    1 
ATOM   7571  H  HA   . VAL B 1 152 ? 15.684  14.430  -8.070  1.00 7.48   ?  375  VAL B HA   1 
ATOM   7572  H  HB   . VAL B 1 152 ? 16.278  14.800  -5.874  1.00 7.87   ?  375  VAL B HB   1 
ATOM   7573  H  HG11 . VAL B 1 152 ? 14.240  14.582  -4.839  1.00 8.23   ?  375  VAL B HG11 1 
ATOM   7574  H  HG12 . VAL B 1 152 ? 13.977  14.930  -6.367  1.00 8.23   ?  375  VAL B HG12 1 
ATOM   7575  H  HG13 . VAL B 1 152 ? 13.815  13.435  -5.853  1.00 8.23   ?  375  VAL B HG13 1 
ATOM   7576  H  HG21 . VAL B 1 152 ? 16.030  13.054  -4.257  1.00 8.85   ?  375  VAL B HG21 1 
ATOM   7577  H  HG22 . VAL B 1 152 ? 16.002  12.041  -5.481  1.00 8.85   ?  375  VAL B HG22 1 
ATOM   7578  H  HG23 . VAL B 1 152 ? 17.295  12.922  -5.209  1.00 8.85   ?  375  VAL B HG23 1 
ATOM   7579  N  N    . MET B 1 153 ? 18.257  14.237  -7.783  1.00 6.96   ?  376  MET B N    1 
ATOM   7580  C  CA   A MET B 1 153 ? 19.684  14.003  -7.932  0.51 7.07   ?  376  MET B CA   1 
ATOM   7581  C  CA   B MET B 1 153 ? 19.687  14.022  -7.934  0.49 8.06   ?  376  MET B CA   1 
ATOM   7582  C  C    . MET B 1 153 ? 20.379  14.190  -6.589  1.00 6.54   ?  376  MET B C    1 
ATOM   7583  O  O    . MET B 1 153 ? 20.079  15.127  -5.847  1.00 7.91   ?  376  MET B O    1 
ATOM   7584  C  CB   A MET B 1 153 ? 20.267  14.941  -8.988  0.51 8.86   ?  376  MET B CB   1 
ATOM   7585  C  CB   B MET B 1 153 ? 20.276  15.036  -8.908  0.49 11.61  ?  376  MET B CB   1 
ATOM   7586  C  CG   A MET B 1 153 ? 21.734  14.718  -9.272  0.51 11.21  ?  376  MET B CG   1 
ATOM   7587  C  CG   B MET B 1 153 ? 21.696  14.719  -9.312  0.49 15.32  ?  376  MET B CG   1 
ATOM   7588  S  SD   A MET B 1 153 ? 22.794  15.666  -8.169  0.51 13.56  ?  376  MET B SD   1 
ATOM   7589  S  SD   B MET B 1 153 ? 22.294  15.785  -10.625 0.49 19.52  ?  376  MET B SD   1 
ATOM   7590  C  CE   A MET B 1 153 ? 22.541  17.330  -8.789  0.51 14.34  ?  376  MET B CE   1 
ATOM   7591  C  CE   B MET B 1 153 ? 22.095  17.405  -9.887  0.49 20.42  ?  376  MET B CE   1 
ATOM   7592  H  H    A MET B 1 153 ? 18.055  15.059  -7.632  0.51 8.35   ?  376  MET B H    1 
ATOM   7593  H  H    B MET B 1 153 ? 18.051  15.058  -7.629  0.49 8.35   ?  376  MET B H    1 
ATOM   7594  H  HA   A MET B 1 153 ? 19.844  13.093  -8.227  0.51 8.48   ?  376  MET B HA   1 
ATOM   7595  H  HA   B MET B 1 153 ? 19.839  13.125  -8.271  0.49 9.67   ?  376  MET B HA   1 
ATOM   7596  H  HB2  A MET B 1 153 ? 19.783  14.812  -9.819  0.51 10.64  ?  376  MET B HB2  1 
ATOM   7597  H  HB2  B MET B 1 153 ? 19.734  15.051  -9.712  0.49 13.94  ?  376  MET B HB2  1 
ATOM   7598  H  HB3  A MET B 1 153 ? 20.162  15.856  -8.682  0.51 10.64  ?  376  MET B HB3  1 
ATOM   7599  H  HB3  B MET B 1 153 ? 20.274  15.912  -8.490  0.49 13.94  ?  376  MET B HB3  1 
ATOM   7600  H  HG2  A MET B 1 153 ? 21.941  13.777  -9.155  0.51 13.46  ?  376  MET B HG2  1 
ATOM   7601  H  HG2  B MET B 1 153 ? 22.277  14.834  -8.544  0.49 18.38  ?  376  MET B HG2  1 
ATOM   7602  H  HG3  A MET B 1 153 ? 21.927  14.989  -10.183 0.51 13.46  ?  376  MET B HG3  1 
ATOM   7603  H  HG3  B MET B 1 153 ? 21.738  13.802  -9.626  0.49 18.38  ?  376  MET B HG3  1 
ATOM   7604  H  HE1  A MET B 1 153 ? 23.133  17.936  -8.317  0.51 17.21  ?  376  MET B HE1  1 
ATOM   7605  H  HE1  B MET B 1 153 ? 22.495  18.069  -10.471 0.49 24.51  ?  376  MET B HE1  1 
ATOM   7606  H  HE2  A MET B 1 153 ? 22.739  17.347  -9.739  0.51 17.21  ?  376  MET B HE2  1 
ATOM   7607  H  HE2  B MET B 1 153 ? 21.149  17.588  -9.777  0.49 24.51  ?  376  MET B HE2  1 
ATOM   7608  H  HE3  A MET B 1 153 ? 21.618  17.586  -8.640  0.51 17.21  ?  376  MET B HE3  1 
ATOM   7609  H  HE3  B MET B 1 153 ? 22.537  17.415  -9.024  0.49 24.51  ?  376  MET B HE3  1 
ATOM   7610  N  N    . ILE B 1 154 ? 21.314  13.291  -6.286  1.00 6.91   ?  377  ILE B N    1 
ATOM   7611  C  CA   . ILE B 1 154 ? 22.112  13.364  -5.062  1.00 6.20   ?  377  ILE B CA   1 
ATOM   7612  C  C    . ILE B 1 154 ? 23.586  13.426  -5.433  1.00 6.01   ?  377  ILE B C    1 
ATOM   7613  O  O    . ILE B 1 154 ? 24.051  12.661  -6.286  1.00 7.64   ?  377  ILE B O    1 
ATOM   7614  C  CB   . ILE B 1 154 ? 21.797  12.205  -4.090  1.00 6.90   ?  377  ILE B CB   1 
ATOM   7615  C  CG1  . ILE B 1 154 ? 22.575  12.386  -2.785  1.00 6.93   ?  377  ILE B CG1  1 
ATOM   7616  C  CG2  . ILE B 1 154 ? 22.066  10.813  -4.705  1.00 7.38   ?  377  ILE B CG2  1 
ATOM   7617  C  CD1  . ILE B 1 154 ? 22.098  11.470  -1.678  1.00 8.26   ?  377  ILE B CD1  1 
ATOM   7618  H  H    . ILE B 1 154 ? 21.508  12.617  -6.783  1.00 8.29   ?  377  ILE B H    1 
ATOM   7619  H  HA   . ILE B 1 154 ? 21.903  14.190  -4.599  1.00 7.44   ?  377  ILE B HA   1 
ATOM   7620  H  HB   . ILE B 1 154 ? 20.846  12.242  -3.903  1.00 8.29   ?  377  ILE B HB   1 
ATOM   7621  H  HG12 . ILE B 1 154 ? 23.512  12.194  -2.949  1.00 8.31   ?  377  ILE B HG12 1 
ATOM   7622  H  HG13 . ILE B 1 154 ? 22.471  13.301  -2.482  1.00 8.31   ?  377  ILE B HG13 1 
ATOM   7623  H  HG21 . ILE B 1 154 ? 21.740  10.131  -4.097  1.00 8.86   ?  377  ILE B HG21 1 
ATOM   7624  H  HG22 . ILE B 1 154 ? 21.603  10.749  -5.554  1.00 8.86   ?  377  ILE B HG22 1 
ATOM   7625  H  HG23 . ILE B 1 154 ? 23.021  10.707  -4.840  1.00 8.86   ?  377  ILE B HG23 1 
ATOM   7626  H  HD11 . ILE B 1 154 ? 22.564  11.697  -0.858  1.00 9.92   ?  377  ILE B HD11 1 
ATOM   7627  H  HD12 . ILE B 1 154 ? 21.143  11.589  -1.559  1.00 9.92   ?  377  ILE B HD12 1 
ATOM   7628  H  HD13 . ILE B 1 154 ? 22.290  10.551  -1.923  1.00 9.92   ?  377  ILE B HD13 1 
ATOM   7629  N  N    . GLY B 1 155 ? 24.314  14.336  -4.809  1.00 5.79   ?  378  GLY B N    1 
ATOM   7630  C  CA   . GLY B 1 155 ? 25.753  14.461  -5.001  1.00 6.24   ?  378  GLY B CA   1 
ATOM   7631  C  C    . GLY B 1 155 ? 26.496  13.922  -3.790  1.00 6.69   ?  378  GLY B C    1 
ATOM   7632  O  O    . GLY B 1 155 ? 26.063  14.122  -2.663  1.00 7.08   ?  378  GLY B O    1 
ATOM   7633  H  H    . GLY B 1 155 ? 23.992  14.909  -4.255  1.00 6.95   ?  378  GLY B H    1 
ATOM   7634  H  HA2  . GLY B 1 155 ? 26.025  13.959  -5.785  1.00 7.49   ?  378  GLY B HA2  1 
ATOM   7635  H  HA3  . GLY B 1 155 ? 25.989  15.393  -5.125  1.00 7.49   ?  378  GLY B HA3  1 
ATOM   7636  N  N    . THR B 1 156 ? 27.624  13.256  -4.030  1.00 6.15   ?  379  THR B N    1 
ATOM   7637  C  CA   . THR B 1 156 ? 28.408  12.645  -2.959  1.00 6.54   ?  379  THR B CA   1 
ATOM   7638  C  C    . THR B 1 156 ? 29.859  13.139  -2.946  1.00 6.66   ?  379  THR B C    1 
ATOM   7639  O  O    . THR B 1 156 ? 30.749  12.458  -2.434  1.00 7.54   ?  379  THR B O    1 
ATOM   7640  C  CB   . THR B 1 156 ? 28.365  11.117  -3.057  1.00 6.87   ?  379  THR B CB   1 
ATOM   7641  O  OG1  . THR B 1 156 ? 28.857  10.719  -4.336  1.00 7.04   ?  379  THR B OG1  1 
ATOM   7642  C  CG2  . THR B 1 156 ? 26.949  10.581  -2.865  1.00 7.01   ?  379  THR B CG2  1 
ATOM   7643  H  H    . THR B 1 156 ? 27.959  13.143  -4.815  1.00 7.38   ?  379  THR B H    1 
ATOM   7644  H  HA   . THR B 1 156 ? 28.009  12.898  -2.112  1.00 7.86   ?  379  THR B HA   1 
ATOM   7645  H  HB   . THR B 1 156 ? 28.915  10.736  -2.354  1.00 8.24   ?  379  THR B HB   1 
ATOM   7646  H  HG1  . THR B 1 156 ? 29.662  10.942  -4.416  1.00 8.46   ?  379  THR B HG1  1 
ATOM   7647  H  HG21 . THR B 1 156 ? 26.945  9.615   -2.950  1.00 8.42   ?  379  THR B HG21 1 
ATOM   7648  H  HG22 . THR B 1 156 ? 26.620  10.821  -1.984  1.00 8.42   ?  379  THR B HG22 1 
ATOM   7649  H  HG23 . THR B 1 156 ? 26.358  10.959  -3.535  1.00 8.42   ?  379  THR B HG23 1 
ATOM   7650  N  N    . TRP B 1 157 ? 30.104  14.326  -3.484  1.00 7.06   ?  380  TRP B N    1 
ATOM   7651  C  CA   . TRP B 1 157 ? 31.446  14.904  -3.537  1.00 8.45   ?  380  TRP B CA   1 
ATOM   7652  C  C    . TRP B 1 157 ? 32.369  13.916  -4.251  1.00 8.69   ?  380  TRP B C    1 
ATOM   7653  O  O    . TRP B 1 157 ? 32.031  13.453  -5.350  1.00 9.50   ?  380  TRP B O    1 
ATOM   7654  C  CB   . TRP B 1 157 ? 31.917  15.357  -2.176  1.00 8.69   ?  380  TRP B CB   1 
ATOM   7655  C  CG   . TRP B 1 157 ? 31.148  16.451  -1.550  1.00 8.49   ?  380  TRP B CG   1 
ATOM   7656  C  CD1  . TRP B 1 157 ? 31.333  17.787  -1.750  1.00 10.43  ?  380  TRP B CD1  1 
ATOM   7657  C  CD2  . TRP B 1 157 ? 30.135  16.334  -0.546  1.00 9.06   ?  380  TRP B CD2  1 
ATOM   7658  N  NE1  . TRP B 1 157 ? 30.488  18.504  -0.949  1.00 10.12  ?  380  TRP B NE1  1 
ATOM   7659  C  CE2  . TRP B 1 157 ? 29.740  17.636  -0.200  1.00 9.78   ?  380  TRP B CE2  1 
ATOM   7660  C  CE3  . TRP B 1 157 ? 29.514  15.260  0.080   1.00 9.96   ?  380  TRP B CE3  1 
ATOM   7661  C  CZ2  . TRP B 1 157 ? 28.765  17.892  0.752   1.00 10.92  ?  380  TRP B CZ2  1 
ATOM   7662  C  CZ3  . TRP B 1 157 ? 28.538  15.515  1.022   1.00 11.87  ?  380  TRP B CZ3  1 
ATOM   7663  C  CH2  . TRP B 1 157 ? 28.172  16.813  1.350   1.00 12.01  ?  380  TRP B CH2  1 
ATOM   7664  H  H    . TRP B 1 157 ? 29.500  14.828  -3.833  1.00 8.47   ?  380  TRP B H    1 
ATOM   7665  H  HA   . TRP B 1 157 ? 31.376  15.695  -4.094  1.00 10.14  ?  380  TRP B HA   1 
ATOM   7666  H  HB2  . TRP B 1 157 ? 31.876  14.598  -1.573  1.00 10.44  ?  380  TRP B HB2  1 
ATOM   7667  H  HB3  . TRP B 1 157 ? 32.834  15.664  -2.260  1.00 10.44  ?  380  TRP B HB3  1 
ATOM   7668  H  HD1  . TRP B 1 157 ? 31.945  18.157  -2.344  1.00 12.52  ?  380  TRP B HD1  1 
ATOM   7669  H  HE1  . TRP B 1 157 ? 30.435  19.362  -0.921  1.00 12.15  ?  380  TRP B HE1  1 
ATOM   7670  H  HE3  . TRP B 1 157 ? 29.752  14.387  -0.131  1.00 11.96  ?  380  TRP B HE3  1 
ATOM   7671  H  HZ2  . TRP B 1 157 ? 28.523  18.762  0.975   1.00 13.11  ?  380  TRP B HZ2  1 
ATOM   7672  H  HZ3  . TRP B 1 157 ? 28.117  14.802  1.446   1.00 14.25  ?  380  TRP B HZ3  1 
ATOM   7673  H  HH2  . TRP B 1 157 ? 27.510  16.952  1.989   1.00 14.41  ?  380  TRP B HH2  1 
ATOM   7674  N  N    A THR B 1 158 ? 33.530  13.587  -3.689  0.96 8.90   ?  381  THR B N    1 
ATOM   7675  C  CA   A THR B 1 158 ? 34.486  12.723  -4.372  0.96 10.28  ?  381  THR B CA   1 
ATOM   7676  C  C    A THR B 1 158 ? 34.263  11.237  -4.109  0.96 9.57   ?  381  THR B C    1 
ATOM   7677  O  O    A THR B 1 158 ? 35.022  10.413  -4.622  0.96 11.06  ?  381  THR B O    1 
ATOM   7678  C  CB   A THR B 1 158 ? 35.937  13.083  -4.019  0.96 13.03  ?  381  THR B CB   1 
ATOM   7679  O  OG1  A THR B 1 158 ? 36.152  12.862  -2.628  0.96 15.72  ?  381  THR B OG1  1 
ATOM   7680  C  CG2  A THR B 1 158 ? 36.273  14.536  -4.360  0.96 14.25  ?  381  THR B CG2  1 
ATOM   7681  H  H    A THR B 1 158 ? 33.787  13.852  -2.912  0.96 10.69  ?  381  THR B H    1 
ATOM   7682  H  HA   A THR B 1 158 ? 34.374  12.883  -5.322  0.96 12.34  ?  381  THR B HA   1 
ATOM   7683  H  HB   A THR B 1 158 ? 36.529  12.523  -4.545  0.96 15.64  ?  381  THR B HB   1 
ATOM   7684  H  HG1  A THR B 1 158 ? 36.069  12.045  -2.451  0.96 18.87  ?  381  THR B HG1  1 
ATOM   7685  H  HG21 A THR B 1 158 ? 37.202  14.719  -4.149  0.96 17.10  ?  381  THR B HG21 1 
ATOM   7686  H  HG22 A THR B 1 158 ? 36.127  14.697  -5.305  0.96 17.10  ?  381  THR B HG22 1 
ATOM   7687  H  HG23 A THR B 1 158 ? 35.709  15.136  -3.847  0.96 17.10  ?  381  THR B HG23 1 
ATOM   7688  N  N    . THR B 1 159 ? 33.227  10.878  -3.368  1.00 8.64   ?  382  THR B N    1 
ATOM   7689  C  CA   . THR B 1 159 ? 32.951  9.481   -3.061  1.00 8.99   ?  382  THR B CA   1 
ATOM   7690  C  C    . THR B 1 159 ? 32.235  8.828   -4.231  1.00 8.63   ?  382  THR B C    1 
ATOM   7691  O  O    . THR B 1 159 ? 31.161  9.280   -4.637  1.00 9.42   ?  382  THR B O    1 
ATOM   7692  C  CB   . THR B 1 159 ? 32.107  9.407   -1.794  1.00 11.22  ?  382  THR B CB   1 
ATOM   7693  O  OG1  . THR B 1 159 ? 32.854  9.953   -0.692  1.00 13.94  ?  382  THR B OG1  1 
ATOM   7694  C  CG2  . THR B 1 159 ? 31.713  7.957   -1.506  1.00 11.50  ?  382  THR B CG2  1 
ATOM   7695  H  H    . THR B 1 159 ? 32.662  11.428  -3.026  1.00 10.37  ?  382  THR B H    1 
ATOM   7696  H  HA   . THR B 1 159 ? 33.781  8.998   -2.918  1.00 10.78  ?  382  THR B HA   1 
ATOM   7697  H  HB   . THR B 1 159 ? 31.291  9.920   -1.903  1.00 13.46  ?  382  THR B HB   1 
ATOM   7698  H  HG1  . THR B 1 159 ? 33.048  10.755  -0.845  1.00 16.73  ?  382  THR B HG1  1 
ATOM   7699  H  HG21 . THR B 1 159 ? 31.408  7.872   -0.589  1.00 13.80  ?  382  THR B HG21 1 
ATOM   7700  H  HG22 . THR B 1 159 ? 30.999  7.683   -2.102  1.00 13.80  ?  382  THR B HG22 1 
ATOM   7701  H  HG23 . THR B 1 159 ? 32.476  7.373   -1.640  1.00 13.80  ?  382  THR B HG23 1 
ATOM   7702  N  N    . ASP B 1 160 ? 32.832  7.776   -4.788  1.00 8.67   ?  383  ASP B N    1 
ATOM   7703  C  CA   . ASP B 1 160 ? 32.249  7.079   -5.926  1.00 9.79   ?  383  ASP B CA   1 
ATOM   7704  C  C    . ASP B 1 160 ? 31.685  5.713   -5.556  1.00 8.85   ?  383  ASP B C    1 
ATOM   7705  O  O    . ASP B 1 160 ? 31.246  4.974   -6.442  1.00 9.48   ?  383  ASP B O    1 
ATOM   7706  C  CB   . ASP B 1 160 ? 33.238  6.970   -7.087  1.00 13.27  ?  383  ASP B CB   1 
ATOM   7707  C  CG   . ASP B 1 160 ? 34.410  6.079   -6.778  1.00 16.05  ?  383  ASP B CG   1 
ATOM   7708  O  OD1  . ASP B 1 160 ? 34.459  5.485   -5.681  1.00 16.76  ?  383  ASP B OD1  1 
ATOM   7709  O  OD2  . ASP B 1 160 ? 35.281  5.954   -7.660  1.00 20.67  -1 383  ASP B OD2  1 
ATOM   7710  H  H    . ASP B 1 160 ? 33.580  7.446   -4.520  1.00 10.40  ?  383  ASP B H    1 
ATOM   7711  H  HA   . ASP B 1 160 ? 31.510  7.617   -6.251  1.00 11.74  ?  383  ASP B HA   1 
ATOM   7712  H  HB2  . ASP B 1 160 ? 32.779  6.603   -7.859  1.00 15.93  ?  383  ASP B HB2  1 
ATOM   7713  H  HB3  . ASP B 1 160 ? 33.581  7.854   -7.293  1.00 15.93  ?  383  ASP B HB3  1 
ATOM   7714  N  N    . ASP B 1 161 ? 31.631  5.389   -4.261  1.00 8.16   ?  384  ASP B N    1 
ATOM   7715  C  CA   . ASP B 1 161 ? 31.199  4.074   -3.771  1.00 7.97   ?  384  ASP B CA   1 
ATOM   7716  C  C    . ASP B 1 161 ? 29.678  4.052   -3.578  1.00 7.39   ?  384  ASP B C    1 
ATOM   7717  O  O    . ASP B 1 161 ? 29.149  3.938   -2.471  1.00 7.53   ?  384  ASP B O    1 
ATOM   7718  C  CB   . ASP B 1 161 ? 31.933  3.774   -2.471  1.00 8.75   ?  384  ASP B CB   1 
ATOM   7719  C  CG   . ASP B 1 161 ? 31.550  2.440   -1.864  1.00 9.17   ?  384  ASP B CG   1 
ATOM   7720  O  OD1  . ASP B 1 161 ? 31.416  1.471   -2.627  1.00 10.79  ?  384  ASP B OD1  1 
ATOM   7721  O  OD2  . ASP B 1 161 ? 31.406  2.365   -0.624  1.00 10.04  -1 384  ASP B OD2  1 
ATOM   7722  H  H    . ASP B 1 161 ? 31.847  5.929   -3.627  1.00 9.79   ?  384  ASP B H    1 
ATOM   7723  H  HA   . ASP B 1 161 ? 31.413  3.397   -4.432  1.00 9.56   ?  384  ASP B HA   1 
ATOM   7724  H  HB2  . ASP B 1 161 ? 32.887  3.760   -2.644  1.00 10.50  ?  384  ASP B HB2  1 
ATOM   7725  H  HB3  . ASP B 1 161 ? 31.723  4.467   -1.824  1.00 10.50  ?  384  ASP B HB3  1 
ATOM   7726  N  N    . ILE B 1 162 ? 28.970  4.155   -4.706  1.00 7.42   ?  385  ILE B N    1 
ATOM   7727  C  CA   . ILE B 1 162 ? 27.515  4.111   -4.771  1.00 6.47   ?  385  ILE B CA   1 
ATOM   7728  C  C    . ILE B 1 162 ? 27.159  3.146   -5.892  1.00 6.71   ?  385  ILE B C    1 
ATOM   7729  O  O    . ILE B 1 162 ? 27.749  3.221   -6.975  1.00 8.63   ?  385  ILE B O    1 
ATOM   7730  C  CB   . ILE B 1 162 ? 26.917  5.504   -5.076  1.00 7.38   ?  385  ILE B CB   1 
ATOM   7731  C  CG1  . ILE B 1 162 ? 27.266  6.505   -3.972  1.00 8.28   ?  385  ILE B CG1  1 
ATOM   7732  C  CG2  . ILE B 1 162 ? 25.407  5.425   -5.287  1.00 7.36   ?  385  ILE B CG2  1 
ATOM   7733  C  CD1  . ILE B 1 162 ? 26.601  6.275   -2.612  1.00 8.69   ?  385  ILE B CD1  1 
ATOM   7734  H  H    . ILE B 1 162 ? 29.332  4.255   -5.480  1.00 8.90   ?  385  ILE B H    1 
ATOM   7735  H  HA   . ILE B 1 162 ? 27.150  3.796   -3.929  1.00 7.77   ?  385  ILE B HA   1 
ATOM   7736  H  HB   . ILE B 1 162 ? 27.316  5.818   -5.902  1.00 8.86   ?  385  ILE B HB   1 
ATOM   7737  H  HG12 . ILE B 1 162 ? 28.225  6.475   -3.830  1.00 9.94   ?  385  ILE B HG12 1 
ATOM   7738  H  HG13 . ILE B 1 162 ? 27.002  7.389   -4.273  1.00 9.94   ?  385  ILE B HG13 1 
ATOM   7739  H  HG21 . ILE B 1 162 ? 25.037  6.321   -5.266  1.00 8.84   ?  385  ILE B HG21 1 
ATOM   7740  H  HG22 . ILE B 1 162 ? 25.229  5.014   -6.147  1.00 8.84   ?  385  ILE B HG22 1 
ATOM   7741  H  HG23 . ILE B 1 162 ? 25.017  4.890   -4.578  1.00 8.84   ?  385  ILE B HG23 1 
ATOM   7742  H  HD11 . ILE B 1 162 ? 26.926  6.941   -1.986  1.00 10.42  ?  385  ILE B HD11 1 
ATOM   7743  H  HD12 . ILE B 1 162 ? 25.640  6.356   -2.713  1.00 10.42  ?  385  ILE B HD12 1 
ATOM   7744  H  HD13 . ILE B 1 162 ? 26.827  5.386   -2.296  1.00 10.42  ?  385  ILE B HD13 1 
ATOM   7745  N  N    . LYS B 1 163 ? 26.201  2.259   -5.641  1.00 6.67   ?  386  LYS B N    1 
ATOM   7746  C  CA   . LYS B 1 163 ? 25.734  1.312   -6.643  1.00 6.31   ?  386  LYS B CA   1 
ATOM   7747  C  C    . LYS B 1 163 ? 24.302  1.646   -7.060  1.00 5.98   ?  386  LYS B C    1 
ATOM   7748  O  O    . LYS B 1 163 ? 23.600  2.399   -6.377  1.00 6.81   ?  386  LYS B O    1 
ATOM   7749  C  CB   . LYS B 1 163 ? 25.757  -0.125  -6.100  1.00 6.46   ?  386  LYS B CB   1 
ATOM   7750  C  CG   . LYS B 1 163 ? 27.120  -0.669  -5.705  1.00 7.87   ?  386  LYS B CG   1 
ATOM   7751  C  CD   . LYS B 1 163 ? 26.962  -2.142  -5.297  1.00 9.05   ?  386  LYS B CD   1 
ATOM   7752  C  CE   . LYS B 1 163 ? 28.219  -2.776  -4.746  1.00 9.15   ?  386  LYS B CE   1 
ATOM   7753  N  NZ   . LYS B 1 163 ? 27.893  -4.145  -4.253  1.00 9.58   ?  386  LYS B NZ   1 
ATOM   7754  H  H    . LYS B 1 163 ? 25.800  2.187   -4.884  1.00 8.01   ?  386  LYS B H    1 
ATOM   7755  H  HA   . LYS B 1 163 ? 26.321  1.374   -7.412  1.00 7.57   ?  386  LYS B HA   1 
ATOM   7756  H  HB2  . LYS B 1 163 ? 25.195  -0.160  -5.310  1.00 7.76   ?  386  LYS B HB2  1 
ATOM   7757  H  HB3  . LYS B 1 163 ? 25.402  -0.713  -6.785  1.00 7.76   ?  386  LYS B HB3  1 
ATOM   7758  H  HG2  . LYS B 1 163 ? 27.731  -0.613  -6.456  1.00 9.45   ?  386  LYS B HG2  1 
ATOM   7759  H  HG3  . LYS B 1 163 ? 27.473  -0.168  -4.953  1.00 9.45   ?  386  LYS B HG3  1 
ATOM   7760  H  HD2  . LYS B 1 163 ? 26.279  -2.202  -4.610  1.00 10.86  ?  386  LYS B HD2  1 
ATOM   7761  H  HD3  . LYS B 1 163 ? 26.693  -2.653  -6.076  1.00 10.86  ?  386  LYS B HD3  1 
ATOM   7762  H  HE2  . LYS B 1 163 ? 28.889  -2.843  -5.444  1.00 10.98  ?  386  LYS B HE2  1 
ATOM   7763  H  HE3  . LYS B 1 163 ? 28.560  -2.248  -4.008  1.00 10.98  ?  386  LYS B HE3  1 
ATOM   7764  H  HZ1  . LYS B 1 163 ? 27.592  -4.647  -4.923  1.00 11.50  ?  386  LYS B HZ1  1 
ATOM   7765  H  HZ2  . LYS B 1 163 ? 28.621  -4.526  -3.911  1.00 11.50  ?  386  LYS B HZ2  1 
ATOM   7766  H  HZ3  . LYS B 1 163 ? 27.267  -4.100  -3.622  1.00 11.50  ?  386  LYS B HZ3  1 
ATOM   7767  N  N    . ASN B 1 164 ? 23.847  1.054   -8.170  1.00 5.90   ?  387  ASN B N    1 
ATOM   7768  C  CA   . ASN B 1 164 ? 22.469  1.239   -8.632  1.00 6.90   ?  387  ASN B CA   1 
ATOM   7769  C  C    . ASN B 1 164 ? 21.559  0.267   -7.874  1.00 6.52   ?  387  ASN B C    1 
ATOM   7770  O  O    . ASN B 1 164 ? 21.132  -0.770  -8.381  1.00 7.90   ?  387  ASN B O    1 
ATOM   7771  C  CB   . ASN B 1 164 ? 22.358  1.044   -10.140 1.00 7.49   ?  387  ASN B CB   1 
ATOM   7772  C  CG   . ASN B 1 164 ? 23.052  2.120   -10.937 1.00 9.00   ?  387  ASN B CG   1 
ATOM   7773  O  OD1  . ASN B 1 164 ? 23.271  3.226   -10.459 1.00 10.69  ?  387  ASN B OD1  1 
ATOM   7774  N  ND2  . ASN B 1 164 ? 23.371  1.809   -12.190 1.00 11.44  ?  387  ASN B ND2  1 
ATOM   7775  H  H    . ASN B 1 164 ? 24.319  0.539   -8.672  1.00 7.09   ?  387  ASN B H    1 
ATOM   7776  H  HA   . ASN B 1 164 ? 22.196  2.148   -8.433  1.00 8.28   ?  387  ASN B HA   1 
ATOM   7777  H  HB2  . ASN B 1 164 ? 22.761  0.193   -10.377 1.00 9.00   ?  387  ASN B HB2  1 
ATOM   7778  H  HB3  . ASN B 1 164 ? 21.421  1.047   -10.389 1.00 9.00   ?  387  ASN B HB3  1 
ATOM   7779  H  HD21 . ASN B 1 164 ? 23.768  2.386   -12.689 1.00 13.73  ?  387  ASN B HD21 1 
ATOM   7780  H  HD22 . ASN B 1 164 ? 23.181  1.030   -12.501 1.00 13.73  ?  387  ASN B HD22 1 
ATOM   7781  N  N    . GLN B 1 165 ? 21.318  0.603   -6.601  1.00 5.80   ?  388  GLN B N    1 
ATOM   7782  C  CA   . GLN B 1 165 ? 20.746  -0.302  -5.611  1.00 5.49   ?  388  GLN B CA   1 
ATOM   7783  C  C    . GLN B 1 165 ? 19.739  0.426   -4.728  1.00 5.81   ?  388  GLN B C    1 
ATOM   7784  O  O    . GLN B 1 165 ? 19.702  1.670   -4.703  1.00 5.99   ?  388  GLN B O    1 
ATOM   7785  C  CB   . GLN B 1 165 ? 21.866  -0.911  -4.760  1.00 5.92   ?  388  GLN B CB   1 
ATOM   7786  C  CG   . GLN B 1 165 ? 22.789  -1.848  -5.545  1.00 7.19   ?  388  GLN B CG   1 
ATOM   7787  C  CD   . GLN B 1 165 ? 22.173  -3.214  -5.773  1.00 7.45   ?  388  GLN B CD   1 
ATOM   7788  O  OE1  . GLN B 1 165 ? 21.102  -3.552  -5.258  1.00 7.11   ?  388  GLN B OE1  1 
ATOM   7789  N  NE2  . GLN B 1 165 ? 22.868  -4.027  -6.541  1.00 10.51  ?  388  GLN B NE2  1 
ATOM   7790  H  H    . GLN B 1 165 ? 21.485  1.382   -6.278  1.00 6.96   ?  388  GLN B H    1 
ATOM   7791  H  HA   . GLN B 1 165 ? 20.270  -1.015  -6.064  1.00 6.59   ?  388  GLN B HA   1 
ATOM   7792  H  HB2  . GLN B 1 165 ? 22.410  -0.194  -4.398  1.00 7.10   ?  388  GLN B HB2  1 
ATOM   7793  H  HB3  . GLN B 1 165 ? 21.468  -1.422  -4.038  1.00 7.10   ?  388  GLN B HB3  1 
ATOM   7794  H  HG2  . GLN B 1 165 ? 22.978  -1.455  -6.411  1.00 8.63   ?  388  GLN B HG2  1 
ATOM   7795  H  HG3  . GLN B 1 165 ? 23.614  -1.969  -5.049  1.00 8.63   ?  388  GLN B HG3  1 
ATOM   7796  H  HE21 . GLN B 1 165 ? 23.617  -3.767  -6.874  1.00 12.62  ?  388  GLN B HE21 1 
ATOM   7797  H  HE22 . GLN B 1 165 ? 22.573  -4.817  -6.709  1.00 12.62  ?  388  GLN B HE22 1 
ATOM   7798  N  N    . PRO B 1 166 ? 18.914  -0.318  -3.986  1.00 5.83   ?  389  PRO B N    1 
ATOM   7799  C  CA   . PRO B 1 166 ? 17.961  0.308   -3.065  1.00 5.94   ?  389  PRO B CA   1 
ATOM   7800  C  C    . PRO B 1 166 ? 18.665  1.209   -2.071  1.00 5.79   ?  389  PRO B C    1 
ATOM   7801  O  O    . PRO B 1 166 ? 19.687  0.845   -1.491  1.00 6.45   ?  389  PRO B O    1 
ATOM   7802  C  CB   . PRO B 1 166 ? 17.300  -0.900  -2.377  1.00 6.71   ?  389  PRO B CB   1 
ATOM   7803  C  CG   . PRO B 1 166 ? 17.411  -2.002  -3.397  1.00 7.39   ?  389  PRO B CG   1 
ATOM   7804  C  CD   . PRO B 1 166 ? 18.796  -1.790  -3.970  1.00 6.48   ?  389  PRO B CD   1 
ATOM   7805  H  HA   . PRO B 1 166 ? 17.292  0.819   -3.547  1.00 7.13   ?  389  PRO B HA   1 
ATOM   7806  H  HB2  . PRO B 1 166 ? 17.778  -1.125  -1.563  1.00 8.05   ?  389  PRO B HB2  1 
ATOM   7807  H  HB3  . PRO B 1 166 ? 16.372  -0.703  -2.172  1.00 8.05   ?  389  PRO B HB3  1 
ATOM   7808  H  HG2  . PRO B 1 166 ? 17.333  -2.870  -2.970  1.00 8.87   ?  389  PRO B HG2  1 
ATOM   7809  H  HG3  . PRO B 1 166 ? 16.727  -1.905  -4.078  1.00 8.87   ?  389  PRO B HG3  1 
ATOM   7810  H  HD2  . PRO B 1 166 ? 19.473  -2.187  -3.400  1.00 7.77   ?  389  PRO B HD2  1 
ATOM   7811  H  HD3  . PRO B 1 166 ? 18.862  -2.154  -4.867  1.00 7.77   ?  389  PRO B HD3  1 
ATOM   7812  N  N    . SER B 1 167 ? 18.069  2.379   -1.850  1.00 5.66   ?  390  SER B N    1 
ATOM   7813  C  CA   . SER B 1 167 ? 18.704  3.460   -1.126  1.00 5.74   ?  390  SER B CA   1 
ATOM   7814  C  C    . SER B 1 167 ? 17.681  4.242   -0.317  1.00 5.78   ?  390  SER B C    1 
ATOM   7815  O  O    . SER B 1 167 ? 16.522  4.395   -0.717  1.00 6.60   ?  390  SER B O    1 
ATOM   7816  C  CB   . SER B 1 167 ? 19.375  4.439   -2.106  1.00 6.82   ?  390  SER B CB   1 
ATOM   7817  O  OG   . SER B 1 167 ? 20.335  3.783   -2.916  1.00 7.24   ?  390  SER B OG   1 
ATOM   7818  H  H    . SER B 1 167 ? 17.275  2.571   -2.120  1.00 6.79   ?  390  SER B H    1 
ATOM   7819  H  HA   . SER B 1 167 ? 19.350  3.077   -0.512  1.00 6.89   ?  390  SER B HA   1 
ATOM   7820  H  HB2  . SER B 1 167 ? 18.695  4.827   -2.678  1.00 8.19   ?  390  SER B HB2  1 
ATOM   7821  H  HB3  . SER B 1 167 ? 19.819  5.137   -1.598  1.00 8.19   ?  390  SER B HB3  1 
ATOM   7822  H  HG   . SER B 1 167 ? 19.964  3.178   -3.367  1.00 8.69   ?  390  SER B HG   1 
ATOM   7823  N  N    . LYS B 1 168 ? 18.155  4.768   0.803   1.00 5.79   ?  391  LYS B N    1 
ATOM   7824  C  CA   A LYS B 1 168 ? 17.393  5.666   1.659   0.45 6.37   ?  391  LYS B CA   1 
ATOM   7825  C  CA   B LYS B 1 168 ? 17.389  5.672   1.649   0.55 6.51   ?  391  LYS B CA   1 
ATOM   7826  C  C    . LYS B 1 168 ? 18.267  6.871   1.984   1.00 5.72   ?  391  LYS B C    1 
ATOM   7827  O  O    . LYS B 1 168 ? 19.452  6.717   2.278   1.00 7.09   ?  391  LYS B O    1 
ATOM   7828  C  CB   A LYS B 1 168 ? 16.982  4.961   2.968   0.45 8.53   ?  391  LYS B CB   1 
ATOM   7829  C  CB   B LYS B 1 168 ? 16.895  5.004   2.937   0.55 9.02   ?  391  LYS B CB   1 
ATOM   7830  C  CG   A LYS B 1 168 ? 16.306  5.872   4.004   0.45 9.61   ?  391  LYS B CG   1 
ATOM   7831  C  CG   B LYS B 1 168 ? 16.059  5.944   3.814   0.55 9.70   ?  391  LYS B CG   1 
ATOM   7832  C  CD   A LYS B 1 168 ? 15.918  5.141   5.305   0.45 10.11  ?  391  LYS B CD   1 
ATOM   7833  C  CD   B LYS B 1 168 ? 15.299  5.217   4.922   0.55 11.27  ?  391  LYS B CD   1 
ATOM   7834  C  CE   A LYS B 1 168 ? 17.075  5.070   6.329   0.45 9.62   ?  391  LYS B CE   1 
ATOM   7835  C  CE   B LYS B 1 168 ? 14.911  6.169   6.054   0.55 12.67  ?  391  LYS B CE   1 
ATOM   7836  N  NZ   A LYS B 1 168 ? 16.677  4.559   7.718   0.45 8.97   ?  391  LYS B NZ   1 
ATOM   7837  N  NZ   B LYS B 1 168 ? 14.202  5.484   7.174   0.55 13.84  ?  391  LYS B NZ   1 
ATOM   7838  H  H    . LYS B 1 168 ? 18.945  4.608   1.104   1.00 6.95   ?  391  LYS B H    1 
ATOM   7839  H  HA   . LYS B 1 168 ? 16.589  5.966   1.206   1.00 7.82   ?  391  LYS B HA   1 
ATOM   7840  H  HB2  A LYS B 1 168 ? 16.358  4.250   2.753   0.45 10.24  ?  391  LYS B HB2  1 
ATOM   7841  H  HB2  B LYS B 1 168 ? 16.344  4.240   2.704   0.55 10.82  ?  391  LYS B HB2  1 
ATOM   7842  H  HB3  A LYS B 1 168 ? 17.778  4.589   3.381   0.45 10.24  ?  391  LYS B HB3  1 
ATOM   7843  H  HB3  B LYS B 1 168 ? 17.662  4.713   3.455   0.55 10.82  ?  391  LYS B HB3  1 
ATOM   7844  H  HG2  A LYS B 1 168 ? 16.917  6.589   4.238   0.45 11.54  ?  391  LYS B HG2  1 
ATOM   7845  H  HG2  B LYS B 1 168 ? 16.648  6.592   4.232   0.55 11.64  ?  391  LYS B HG2  1 
ATOM   7846  H  HG3  A LYS B 1 168 ? 15.496  6.240   3.618   0.45 11.54  ?  391  LYS B HG3  1 
ATOM   7847  H  HG3  B LYS B 1 168 ? 15.408  6.399   3.256   0.55 11.64  ?  391  LYS B HG3  1 
ATOM   7848  H  HD2  A LYS B 1 168 ? 15.179  5.611   5.722   0.45 12.13  ?  391  LYS B HD2  1 
ATOM   7849  H  HD2  B LYS B 1 168 ? 14.488  4.831   4.556   0.55 13.52  ?  391  LYS B HD2  1 
ATOM   7850  H  HD3  A LYS B 1 168 ? 15.655  4.233   5.090   0.45 12.13  ?  391  LYS B HD3  1 
ATOM   7851  H  HD3  B LYS B 1 168 ? 15.861  4.517   5.291   0.55 13.52  ?  391  LYS B HD3  1 
ATOM   7852  H  HE2  A LYS B 1 168 ? 17.756  4.471   5.984   0.45 11.55  ?  391  LYS B HE2  1 
ATOM   7853  H  HE2  B LYS B 1 168 ? 15.715  6.575   6.414   0.55 15.21  ?  391  LYS B HE2  1 
ATOM   7854  H  HE3  A LYS B 1 168 ? 17.442  5.961   6.441   0.45 11.55  ?  391  LYS B HE3  1 
ATOM   7855  H  HE3  B LYS B 1 168 ? 14.322  6.854   5.702   0.55 15.21  ?  391  LYS B HE3  1 
ATOM   7856  H  HZ1  A LYS B 1 168 ? 16.054  5.088   8.070   0.45 10.77  ?  391  LYS B HZ1  1 
ATOM   7857  H  HZ1  B LYS B 1 168 ? 14.687  4.798   7.468   0.55 16.62  ?  391  LYS B HZ1  1 
ATOM   7858  H  HZ2  A LYS B 1 168 ? 16.353  3.732   7.658   0.45 10.77  ?  391  LYS B HZ2  1 
ATOM   7859  H  HZ2  B LYS B 1 168 ? 14.071  6.054   7.845   0.55 16.62  ?  391  LYS B HZ2  1 
ATOM   7860  H  HZ3  A LYS B 1 168 ? 17.387  4.552   8.255   0.45 10.77  ?  391  LYS B HZ3  1 
ATOM   7861  H  HZ3  B LYS B 1 168 ? 13.413  5.182   6.894   0.55 16.62  ?  391  LYS B HZ3  1 
ATOM   7862  N  N    . PHE B 1 169 ? 17.686  8.060   1.931   1.00 5.81   ?  392  PHE B N    1 
ATOM   7863  C  CA   . PHE B 1 169 ? 18.351  9.288   2.341   1.00 5.60   ?  392  PHE B CA   1 
ATOM   7864  C  C    . PHE B 1 169 ? 17.764  9.749   3.670   1.00 5.90   ?  392  PHE B C    1 
ATOM   7865  O  O    . PHE B 1 169 ? 16.557  9.966   3.776   1.00 6.62   ?  392  PHE B O    1 
ATOM   7866  C  CB   . PHE B 1 169 ? 18.174  10.383  1.300   1.00 6.51   ?  392  PHE B CB   1 
ATOM   7867  C  CG   . PHE B 1 169 ? 18.768  11.703  1.703   1.00 6.38   ?  392  PHE B CG   1 
ATOM   7868  C  CD1  . PHE B 1 169 ? 20.103  11.974  1.476   1.00 7.10   ?  392  PHE B CD1  1 
ATOM   7869  C  CD2  . PHE B 1 169 ? 17.986  12.686  2.295   1.00 7.01   ?  392  PHE B CD2  1 
ATOM   7870  C  CE1  . PHE B 1 169 ? 20.653  13.205  1.841   1.00 7.24   ?  392  PHE B CE1  1 
ATOM   7871  C  CE2  . PHE B 1 169 ? 18.526  13.907  2.649   1.00 6.82   ?  392  PHE B CE2  1 
ATOM   7872  C  CZ   . PHE B 1 169 ? 19.855  14.161  2.411   1.00 7.56   ?  392  PHE B CZ   1 
ATOM   7873  H  H    . PHE B 1 169 ? 16.882  8.185   1.653   1.00 6.97   ?  392  PHE B H    1 
ATOM   7874  H  HA   . PHE B 1 169 ? 19.298  9.111   2.455   1.00 6.72   ?  392  PHE B HA   1 
ATOM   7875  H  HB2  . PHE B 1 169 ? 18.605  10.103  0.477   1.00 7.81   ?  392  PHE B HB2  1 
ATOM   7876  H  HB3  . PHE B 1 169 ? 17.226  10.519  1.149   1.00 7.81   ?  392  PHE B HB3  1 
ATOM   7877  H  HD1  . PHE B 1 169 ? 20.641  11.330  1.075   1.00 8.52   ?  392  PHE B HD1  1 
ATOM   7878  H  HD2  . PHE B 1 169 ? 17.085  12.520  2.455   1.00 8.41   ?  392  PHE B HD2  1 
ATOM   7879  H  HE1  . PHE B 1 169 ? 21.556  13.374  1.699   1.00 8.69   ?  392  PHE B HE1  1 
ATOM   7880  H  HE2  . PHE B 1 169 ? 17.991  14.555  3.048   1.00 8.18   ?  392  PHE B HE2  1 
ATOM   7881  H  HZ   . PHE B 1 169 ? 20.216  14.988  2.638   1.00 9.07   ?  392  PHE B HZ   1 
ATOM   7882  N  N    . THR B 1 170 ? 18.632  9.878   4.673   1.00 6.28   ?  393  THR B N    1 
ATOM   7883  C  CA   . THR B 1 170 ? 18.298  10.377  5.992   1.00 6.28   ?  393  THR B CA   1 
ATOM   7884  C  C    . THR B 1 170 ? 18.835  11.794  6.102   1.00 5.84   ?  393  THR B C    1 
ATOM   7885  O  O    . THR B 1 170 ? 20.053  11.988  5.978   1.00 5.74   ?  393  THR B O    1 
ATOM   7886  C  CB   . THR B 1 170 ? 18.947  9.497   7.066   1.00 9.00   ?  393  THR B CB   1 
ATOM   7887  O  OG1  . THR B 1 170 ? 18.505  8.139   6.952   1.00 12.32  ?  393  THR B OG1  1 
ATOM   7888  C  CG2  . THR B 1 170 ? 18.609  10.026  8.446   1.00 9.41   ?  393  THR B CG2  1 
ATOM   7889  H  H    . THR B 1 170 ? 19.464  9.671   4.604   1.00 7.54   ?  393  THR B H    1 
ATOM   7890  H  HA   . THR B 1 170 ? 17.337  10.375  6.126   1.00 7.54   ?  393  THR B HA   1 
ATOM   7891  H  HB   . THR B 1 170 ? 19.909  9.515   6.947   1.00 10.80  ?  393  THR B HB   1 
ATOM   7892  H  HG1  . THR B 1 170 ? 18.738  7.823   6.209   1.00 14.79  ?  393  THR B HG1  1 
ATOM   7893  H  HG21 . THR B 1 170 ? 18.803  9.352   9.116   1.00 11.30  ?  393  THR B HG21 1 
ATOM   7894  H  HG22 . THR B 1 170 ? 19.134  10.819  8.635   1.00 11.30  ?  393  THR B HG22 1 
ATOM   7895  H  HG23 . THR B 1 170 ? 17.667  10.253  8.492   1.00 11.30  ?  393  THR B HG23 1 
ATOM   7896  N  N    . PRO B 1 171 ? 18.004  12.785  6.383   1.00 5.63   ?  394  PRO B N    1 
ATOM   7897  C  CA   . PRO B 1 171 ? 18.489  14.157  6.443   1.00 5.38   ?  394  PRO B CA   1 
ATOM   7898  C  C    . PRO B 1 171 ? 19.194  14.445  7.751   1.00 5.45   ?  394  PRO B C    1 
ATOM   7899  O  O    . PRO B 1 171 ? 18.850  13.904  8.797   1.00 6.05   ?  394  PRO B O    1 
ATOM   7900  C  CB   . PRO B 1 171 ? 17.194  14.975  6.370   1.00 7.06   ?  394  PRO B CB   1 
ATOM   7901  C  CG   . PRO B 1 171 ? 16.185  14.098  7.037   1.00 7.77   ?  394  PRO B CG   1 
ATOM   7902  C  CD   . PRO B 1 171 ? 16.549  12.712  6.583   1.00 7.28   ?  394  PRO B CD   1 
ATOM   7903  H  HA   . PRO B 1 171 ? 19.071  14.353  5.692   1.00 6.45   ?  394  PRO B HA   1 
ATOM   7904  H  HB2  . PRO B 1 171 ? 17.300  15.814  6.845   1.00 8.48   ?  394  PRO B HB2  1 
ATOM   7905  H  HB3  . PRO B 1 171 ? 16.956  15.144  5.445   1.00 8.48   ?  394  PRO B HB3  1 
ATOM   7906  H  HG2  . PRO B 1 171 ? 16.255  14.181  8.001   1.00 9.32   ?  394  PRO B HG2  1 
ATOM   7907  H  HG3  . PRO B 1 171 ? 15.290  14.338  6.748   1.00 9.32   ?  394  PRO B HG3  1 
ATOM   7908  H  HD2  . PRO B 1 171 ? 16.327  12.058  7.265   1.00 8.73   ?  394  PRO B HD2  1 
ATOM   7909  H  HD3  . PRO B 1 171 ? 16.098  12.492  5.753   1.00 8.73   ?  394  PRO B HD3  1 
ATOM   7910  N  N    . ILE B 1 172 ? 20.191  15.329  7.674   1.00 5.20   ?  395  ILE B N    1 
ATOM   7911  C  CA   . ILE B 1 172 ? 20.897  15.844  8.841   1.00 5.08   ?  395  ILE B CA   1 
ATOM   7912  C  C    . ILE B 1 172 ? 20.733  17.356  8.966   1.00 5.18   ?  395  ILE B C    1 
ATOM   7913  O  O    . ILE B 1 172 ? 20.492  17.883  10.058  1.00 6.31   ?  395  ILE B O    1 
ATOM   7914  C  CB   . ILE B 1 172 ? 22.390  15.462  8.803   1.00 6.05   ?  395  ILE B CB   1 
ATOM   7915  C  CG1  . ILE B 1 172 ? 22.577  13.949  8.817   1.00 8.14   ?  395  ILE B CG1  1 
ATOM   7916  C  CG2  . ILE B 1 172 ? 23.145  16.135  9.948   1.00 8.07   ?  395  ILE B CG2  1 
ATOM   7917  C  CD1  . ILE B 1 172 ? 22.166  13.272  10.100  1.00 8.53   ?  395  ILE B CD1  1 
ATOM   7918  H  H    . ILE B 1 172 ? 20.483  15.652  6.932   1.00 6.25   ?  395  ILE B H    1 
ATOM   7919  H  HA   . ILE B 1 172 ? 20.511  15.442  9.635   1.00 6.09   ?  395  ILE B HA   1 
ATOM   7920  H  HB   . ILE B 1 172 ? 22.762  15.786  7.967   1.00 7.26   ?  395  ILE B HB   1 
ATOM   7921  H  HG12 . ILE B 1 172 ? 22.044  13.566  8.102   1.00 9.77   ?  395  ILE B HG12 1 
ATOM   7922  H  HG13 . ILE B 1 172 ? 23.515  13.753  8.672   1.00 9.77   ?  395  ILE B HG13 1 
ATOM   7923  H  HG21 . ILE B 1 172 ? 24.003  15.697  10.060  1.00 9.68   ?  395  ILE B HG21 1 
ATOM   7924  H  HG22 . ILE B 1 172 ? 23.277  17.071  9.732   1.00 9.68   ?  395  ILE B HG22 1 
ATOM   7925  H  HG23 . ILE B 1 172 ? 22.622  16.053  10.761  1.00 9.68   ?  395  ILE B HG23 1 
ATOM   7926  H  HD11 . ILE B 1 172 ? 22.346  12.322  10.027  1.00 10.24  ?  395  ILE B HD11 1 
ATOM   7927  H  HD12 . ILE B 1 172 ? 22.675  13.651  10.833  1.00 10.24  ?  395  ILE B HD12 1 
ATOM   7928  H  HD13 . ILE B 1 172 ? 21.218  13.419  10.245  1.00 10.24  ?  395  ILE B HD13 1 
ATOM   7929  N  N    . GLY B 1 173 ? 20.896  18.080  7.873   1.00 5.08   ?  396  GLY B N    1 
ATOM   7930  C  CA   . GLY B 1 173 ? 20.788  19.524  7.924   1.00 5.09   ?  396  GLY B CA   1 
ATOM   7931  C  C    . GLY B 1 173 ? 20.959  20.104  6.542   1.00 4.89   ?  396  GLY B C    1 
ATOM   7932  O  O    . GLY B 1 173 ? 20.375  19.591  5.587   1.00 5.24   ?  396  GLY B O    1 
ATOM   7933  H  H    . GLY B 1 173 ? 21.070  17.760  7.094   1.00 6.10   ?  396  GLY B H    1 
ATOM   7934  H  HA2  . GLY B 1 173 ? 19.918  19.778  8.268   1.00 6.11   ?  396  GLY B HA2  1 
ATOM   7935  H  HA3  . GLY B 1 173 ? 21.475  19.886  8.505   1.00 6.11   ?  396  GLY B HA3  1 
ATOM   7936  N  N    . LEU B 1 174 ? 21.770  21.148  6.418   1.00 4.77   ?  397  LEU B N    1 
ATOM   7937  C  CA   . LEU B 1 174 ? 21.926  21.887  5.174   1.00 4.75   ?  397  LEU B CA   1 
ATOM   7938  C  C    . LEU B 1 174 ? 23.400  21.971  4.806   1.00 4.96   ?  397  LEU B C    1 
ATOM   7939  O  O    . LEU B 1 174 ? 24.281  21.924  5.664   1.00 5.64   ?  397  LEU B O    1 
ATOM   7940  C  CB   . LEU B 1 174 ? 21.375  23.300  5.359   1.00 5.28   ?  397  LEU B CB   1 
ATOM   7941  C  CG   . LEU B 1 174 ? 19.866  23.405  5.618   1.00 6.33   ?  397  LEU B CG   1 
ATOM   7942  C  CD1  . LEU B 1 174 ? 19.536  24.801  6.136   1.00 7.93   ?  397  LEU B CD1  1 
ATOM   7943  C  CD2  . LEU B 1 174 ? 19.080  23.072  4.366   1.00 7.47   ?  397  LEU B CD2  1 
ATOM   7944  H  H    . LEU B 1 174 ? 22.255  21.454  7.059   1.00 5.72   ?  397  LEU B H    1 
ATOM   7945  H  HA   . LEU B 1 174 ? 21.464  21.438  4.449   1.00 5.70   ?  397  LEU B HA   1 
ATOM   7946  H  HB2  . LEU B 1 174 ? 21.825  23.703  6.118   1.00 6.33   ?  397  LEU B HB2  1 
ATOM   7947  H  HB3  . LEU B 1 174 ? 21.565  23.806  4.554   1.00 6.33   ?  397  LEU B HB3  1 
ATOM   7948  H  HG   . LEU B 1 174 ? 19.600  22.761  6.293   1.00 7.60   ?  397  LEU B HG   1 
ATOM   7949  H  HD11 . LEU B 1 174 ? 18.580  24.866  6.282   1.00 9.51   ?  397  LEU B HD11 1 
ATOM   7950  H  HD12 . LEU B 1 174 ? 20.009  24.948  6.970   1.00 9.51   ?  397  LEU B HD12 1 
ATOM   7951  H  HD13 . LEU B 1 174 ? 19.815  25.456  5.477   1.00 9.51   ?  397  LEU B HD13 1 
ATOM   7952  H  HD21 . LEU B 1 174 ? 18.134  23.184  4.548   1.00 8.97   ?  397  LEU B HD21 1 
ATOM   7953  H  HD22 . LEU B 1 174 ? 19.353  23.671  3.653   1.00 8.97   ?  397  LEU B HD22 1 
ATOM   7954  H  HD23 . LEU B 1 174 ? 19.263  22.154  4.113   1.00 8.97   ?  397  LEU B HD23 1 
ATOM   7955  N  N    . ASN B 1 175 ? 23.663  22.111  3.503   1.00 5.41   ?  398  ASN B N    1 
ATOM   7956  C  CA   . ASN B 1 175 ? 25.027  22.323  3.038   1.00 6.04   ?  398  ASN B CA   1 
ATOM   7957  C  C    . ASN B 1 175 ? 25.445  23.791  3.109   1.00 5.97   ?  398  ASN B C    1 
ATOM   7958  O  O    . ASN B 1 175 ? 26.642  24.086  3.166   1.00 7.60   ?  398  ASN B O    1 
ATOM   7959  C  CB   . ASN B 1 175 ? 25.206  21.833  1.602   1.00 6.36   ?  398  ASN B CB   1 
ATOM   7960  C  CG   . ASN B 1 175 ? 26.656  21.495  1.280   1.00 6.55   ?  398  ASN B CG   1 
ATOM   7961  O  OD1  . ASN B 1 175 ? 27.385  20.957  2.106   1.00 7.35   ?  398  ASN B OD1  1 
ATOM   7962  N  ND2  . ASN B 1 175 ? 27.081  21.817  0.064   1.00 7.49   ?  398  ASN B ND2  1 
ATOM   7963  H  H    . ASN B 1 175 ? 23.073  22.088  2.878   1.00 6.49   ?  398  ASN B H    1 
ATOM   7964  H  HA   . ASN B 1 175 ? 25.610  21.800  3.612   1.00 7.25   ?  398  ASN B HA   1 
ATOM   7965  H  HB2  . ASN B 1 175 ? 24.674  21.033  1.471   1.00 7.64   ?  398  ASN B HB2  1 
ATOM   7966  H  HB3  . ASN B 1 175 ? 24.916  22.528  0.992   1.00 7.64   ?  398  ASN B HB3  1 
ATOM   7967  H  HD21 . ASN B 1 175 ? 27.891  21.647  -0.167  1.00 9.00   ?  398  ASN B HD21 1 
ATOM   7968  H  HD22 . ASN B 1 175 ? 26.545  22.196  -0.493  1.00 9.00   ?  398  ASN B HD22 1 
ATOM   7969  N  N    . ASP B 1 176 ? 24.494  24.720  3.060   1.00 6.02   ?  399  ASP B N    1 
ATOM   7970  C  CA   . ASP B 1 176 ? 24.818  26.137  3.192   1.00 6.89   ?  399  ASP B CA   1 
ATOM   7971  C  C    . ASP B 1 176 ? 23.634  26.870  3.795   1.00 6.49   ?  399  ASP B C    1 
ATOM   7972  O  O    . ASP B 1 176 ? 22.538  26.321  3.956   1.00 6.89   ?  399  ASP B O    1 
ATOM   7973  C  CB   . ASP B 1 176 ? 25.359  26.761  1.884   1.00 8.83   ?  399  ASP B CB   1 
ATOM   7974  C  CG   . ASP B 1 176 ? 24.288  27.024  0.829   1.00 8.33   ?  399  ASP B CG   1 
ATOM   7975  O  OD1  . ASP B 1 176 ? 23.115  27.309  1.158   1.00 9.28   ?  399  ASP B OD1  1 
ATOM   7976  O  OD2  . ASP B 1 176 ? 24.651  26.992  -0.375  1.00 11.47  -1 399  ASP B OD2  1 
ATOM   7977  H  H    . ASP B 1 176 ? 23.657  24.555  2.952   1.00 7.22   ?  399  ASP B H    1 
ATOM   7978  H  HA   . ASP B 1 176 ? 25.543  26.235  3.830   1.00 8.28   ?  399  ASP B HA   1 
ATOM   7979  H  HB2  . ASP B 1 176 ? 25.779  27.610  2.094   1.00 10.59  ?  399  ASP B HB2  1 
ATOM   7980  H  HB3  . ASP B 1 176 ? 26.011  26.156  1.496   1.00 10.59  ?  399  ASP B HB3  1 
ATOM   7981  N  N    . ASP B 1 177 ? 23.890  28.116  4.166   1.00 6.93   ?  400  ASP B N    1 
ATOM   7982  C  CA   . ASP B 1 177 ? 22.918  29.003  4.781   1.00 7.73   ?  400  ASP B CA   1 
ATOM   7983  C  C    . ASP B 1 177 ? 22.310  29.961  3.763   1.00 7.57   ?  400  ASP B C    1 
ATOM   7984  O  O    . ASP B 1 177 ? 21.090  30.091  3.691   1.00 8.51   ?  400  ASP B O    1 
ATOM   7985  C  CB   . ASP B 1 177 ? 23.640  29.784  5.896   1.00 8.75   ?  400  ASP B CB   1 
ATOM   7986  C  CG   . ASP B 1 177 ? 22.716  30.681  6.702   1.00 10.01  ?  400  ASP B CG   1 
ATOM   7987  O  OD1  . ASP B 1 177 ? 21.525  30.363  6.863   1.00 13.80  ?  400  ASP B OD1  1 
ATOM   7988  O  OD2  . ASP B 1 177 ? 23.195  31.723  7.197   1.00 10.91  -1 400  ASP B OD2  1 
ATOM   7989  H  H    . ASP B 1 177 ? 24.659  28.488  4.067   1.00 8.32   ?  400  ASP B H    1 
ATOM   7990  H  HA   . ASP B 1 177 ? 22.186  28.501  5.174   1.00 9.27   ?  400  ASP B HA   1 
ATOM   7991  H  HB2  . ASP B 1 177 ? 24.048  29.152  6.508   1.00 10.51  ?  400  ASP B HB2  1 
ATOM   7992  H  HB3  . ASP B 1 177 ? 24.322  30.345  5.494   1.00 10.51  ?  400  ASP B HB3  1 
ATOM   7993  N  N    . ASP B 1 178 ? 23.138  30.610  2.943   1.00 8.86   ?  401  ASP B N    1 
ATOM   7994  C  CA   . ASP B 1 178 ? 22.643  31.707  2.116   1.00 9.54   ?  401  ASP B CA   1 
ATOM   7995  C  C    . ASP B 1 178 ? 21.648  31.250  1.052   1.00 10.45  ?  401  ASP B C    1 
ATOM   7996  O  O    . ASP B 1 178 ? 20.809  32.043  0.612   1.00 12.21  ?  401  ASP B O    1 
ATOM   7997  C  CB   . ASP B 1 178 ? 23.810  32.414  1.427   1.00 9.93   ?  401  ASP B CB   1 
ATOM   7998  C  CG   . ASP B 1 178 ? 24.608  33.315  2.361   1.00 11.30  ?  401  ASP B CG   1 
ATOM   7999  O  OD1  . ASP B 1 178 ? 24.118  33.617  3.463   1.00 12.28  ?  401  ASP B OD1  1 
ATOM   8000  O  OD2  . ASP B 1 178 ? 25.731  33.717  1.988   1.00 12.24  -1 401  ASP B OD2  1 
ATOM   8001  H  H    . ASP B 1 178 ? 23.976  30.438  2.849   1.00 10.63  ?  401  ASP B H    1 
ATOM   8002  H  HA   . ASP B 1 178 ? 22.189  32.329  2.705   1.00 11.45  ?  401  ASP B HA   1 
ATOM   8003  H  HB2  . ASP B 1 178 ? 24.415  31.746  1.070   1.00 11.92  ?  401  ASP B HB2  1 
ATOM   8004  H  HB3  . ASP B 1 178 ? 23.462  32.965  0.708   1.00 11.92  ?  401  ASP B HB3  1 
ATOM   8005  N  N    . ASN B 1 179 ? 21.708  29.992  0.618   1.00 9.20   ?  402  ASN B N    1 
ATOM   8006  C  CA   . ASN B 1 179 ? 20.803  29.501  -0.416  1.00 10.01  ?  402  ASN B CA   1 
ATOM   8007  C  C    . ASN B 1 179 ? 19.644  28.696  0.140   1.00 9.77   ?  402  ASN B C    1 
ATOM   8008  O  O    . ASN B 1 179 ? 18.897  28.070  -0.622  1.00 11.71  ?  402  ASN B O    1 
ATOM   8009  C  CB   . ASN B 1 179 ? 21.590  28.763  -1.486  1.00 11.98  ?  402  ASN B CB   1 
ATOM   8010  C  CG   . ASN B 1 179 ? 22.606  29.673  -2.140  1.00 14.26  ?  402  ASN B CG   1 
ATOM   8011  O  OD1  . ASN B 1 179 ? 22.235  30.670  -2.769  1.00 16.31  ?  402  ASN B OD1  1 
ATOM   8012  N  ND2  . ASN B 1 179 ? 23.884  29.381  -1.947  1.00 14.47  ?  402  ASN B ND2  1 
ATOM   8013  H  H    . ASN B 1 179 ? 22.265  29.405  0.909   1.00 11.04  ?  402  ASN B H    1 
ATOM   8014  H  HA   . ASN B 1 179 ? 20.389  30.252  -0.868  1.00 12.01  ?  402  ASN B HA   1 
ATOM   8015  H  HB2  . ASN B 1 179 ? 22.061  28.017  -1.083  1.00 14.38  ?  402  ASN B HB2  1 
ATOM   8016  H  HB3  . ASN B 1 179 ? 20.982  28.441  -2.169  1.00 14.38  ?  402  ASN B HB3  1 
ATOM   8017  H  HD21 . ASN B 1 179 ? 24.496  29.872  -2.301  1.00 17.37  ?  402  ASN B HD21 1 
ATOM   8018  H  HD22 . ASN B 1 179 ? 24.103  28.700  -1.469  1.00 17.37  ?  402  ASN B HD22 1 
ATOM   8019  N  N    . PHE B 1 180 ? 19.440  28.741  1.445   1.00 7.34   ?  403  PHE B N    1 
ATOM   8020  C  CA   . PHE B 1 180 ? 18.302  28.104  2.094   1.00 7.00   ?  403  PHE B CA   1 
ATOM   8021  C  C    . PHE B 1 180 ? 17.208  29.153  2.277   1.00 6.45   ?  403  PHE B C    1 
ATOM   8022  O  O    . PHE B 1 180 ? 17.366  30.105  3.050   1.00 7.48   ?  403  PHE B O    1 
ATOM   8023  C  CB   . PHE B 1 180 ? 18.743  27.564  3.448   1.00 7.38   ?  403  PHE B CB   1 
ATOM   8024  C  CG   . PHE B 1 180 ? 17.614  27.113  4.332   1.00 6.76   ?  403  PHE B CG   1 
ATOM   8025  C  CD1  . PHE B 1 180 ? 16.735  26.131  3.914   1.00 7.20   ?  403  PHE B CD1  1 
ATOM   8026  C  CD2  . PHE B 1 180 ? 17.457  27.641  5.610   1.00 6.83   ?  403  PHE B CD2  1 
ATOM   8027  C  CE1  . PHE B 1 180 ? 15.702  25.704  4.755   1.00 7.60   ?  403  PHE B CE1  1 
ATOM   8028  C  CE2  . PHE B 1 180 ? 16.454  27.209  6.429   1.00 7.44   ?  403  PHE B CE2  1 
ATOM   8029  C  CZ   . PHE B 1 180 ? 15.578  26.241  6.003   1.00 7.69   ?  403  PHE B CZ   1 
ATOM   8030  H  H    . PHE B 1 180 ? 19.963  29.146  1.995   1.00 8.81   ?  403  PHE B H    1 
ATOM   8031  H  HA   . PHE B 1 180 ? 17.955  27.385  1.544   1.00 8.40   ?  403  PHE B HA   1 
ATOM   8032  H  HB2  . PHE B 1 180 ? 19.325  26.801  3.302   1.00 8.86   ?  403  PHE B HB2  1 
ATOM   8033  H  HB3  . PHE B 1 180 ? 19.224  28.263  3.919   1.00 8.86   ?  403  PHE B HB3  1 
ATOM   8034  H  HD1  . PHE B 1 180 ? 16.832  25.753  3.069   1.00 8.64   ?  403  PHE B HD1  1 
ATOM   8035  H  HD2  . PHE B 1 180 ? 18.044  28.297  5.910   1.00 8.19   ?  403  PHE B HD2  1 
ATOM   8036  H  HE1  . PHE B 1 180 ? 15.101  25.055  4.465   1.00 9.12   ?  403  PHE B HE1  1 
ATOM   8037  H  HE2  . PHE B 1 180 ? 16.364  27.573  7.281   1.00 8.93   ?  403  PHE B HE2  1 
ATOM   8038  H  HZ   . PHE B 1 180 ? 14.898  25.951  6.567   1.00 9.23   ?  403  PHE B HZ   1 
ATOM   8039  N  N    . LYS B 1 181 ? 16.097  28.958  1.584   1.00 5.98   ?  404  LYS B N    1 
ATOM   8040  C  CA   . LYS B 1 181 ? 14.966  29.885  1.560   1.00 6.52   ?  404  LYS B CA   1 
ATOM   8041  C  C    . LYS B 1 181 ? 13.741  29.090  1.997   1.00 6.00   ?  404  LYS B C    1 
ATOM   8042  O  O    . LYS B 1 181 ? 13.078  28.438  1.182   1.00 6.28   ?  404  LYS B O    1 
ATOM   8043  C  CB   . LYS B 1 181 ? 14.773  30.497  0.171   1.00 8.64   ?  404  LYS B CB   1 
ATOM   8044  C  CG   . LYS B 1 181 ? 15.979  31.253  -0.377  1.00 11.16  ?  404  LYS B CG   1 
ATOM   8045  C  CD   . LYS B 1 181 ? 16.335  32.449  0.470   1.00 15.77  ?  404  LYS B CD   1 
ATOM   8046  C  CE   . LYS B 1 181 ? 17.480  33.180  -0.184  1.00 20.79  ?  404  LYS B CE   1 
ATOM   8047  N  NZ   . LYS B 1 181 ? 18.014  34.227  0.684   1.00 23.86  ?  404  LYS B NZ   1 
ATOM   8048  H  H    . LYS B 1 181 ? 15.964  28.263  1.094   1.00 7.18   ?  404  LYS B H    1 
ATOM   8049  H  HA   . LYS B 1 181 ? 15.123  30.610  2.186   1.00 7.82   ?  404  LYS B HA   1 
ATOM   8050  H  HB2  . LYS B 1 181 ? 14.570  29.783  -0.453  1.00 10.37  ?  404  LYS B HB2  1 
ATOM   8051  H  HB3  . LYS B 1 181 ? 14.032  31.122  0.211   1.00 10.37  ?  404  LYS B HB3  1 
ATOM   8052  H  HG2  . LYS B 1 181 ? 16.745  30.659  -0.398  1.00 13.39  ?  404  LYS B HG2  1 
ATOM   8053  H  HG3  . LYS B 1 181 ? 15.779  31.567  -1.273  1.00 13.39  ?  404  LYS B HG3  1 
ATOM   8054  H  HD2  . LYS B 1 181 ? 15.574  33.047  0.536   1.00 18.93  ?  404  LYS B HD2  1 
ATOM   8055  H  HD3  . LYS B 1 181 ? 16.608  32.160  1.354   1.00 18.93  ?  404  LYS B HD3  1 
ATOM   8056  H  HE2  . LYS B 1 181 ? 18.194  32.551  -0.377  1.00 24.95  ?  404  LYS B HE2  1 
ATOM   8057  H  HE3  . LYS B 1 181 ? 17.171  33.593  -1.005  1.00 24.95  ?  404  LYS B HE3  1 
ATOM   8058  H  HZ1  . LYS B 1 181 ? 18.321  33.870  1.439   1.00 28.64  ?  404  LYS B HZ1  1 
ATOM   8059  H  HZ2  . LYS B 1 181 ? 18.680  34.652  0.274   1.00 28.64  ?  404  LYS B HZ2  1 
ATOM   8060  H  HZ3  . LYS B 1 181 ? 17.375  34.815  0.881   1.00 28.64  ?  404  LYS B HZ3  1 
ATOM   8061  N  N    . GLN B 1 182 ? 13.459  29.136  3.303   1.00 5.62   ?  405  GLN B N    1 
ATOM   8062  C  CA   . GLN B 1 182 ? 12.467  28.231  3.867   1.00 4.94   ?  405  GLN B CA   1 
ATOM   8063  C  C    . GLN B 1 182 ? 11.053  28.521  3.398   1.00 5.94   ?  405  GLN B C    1 
ATOM   8064  O  O    . GLN B 1 182 ? 10.200  27.636  3.510   1.00 6.57   ?  405  GLN B O    1 
ATOM   8065  C  CB   . GLN B 1 182 ? 12.510  28.240  5.389   1.00 5.60   ?  405  GLN B CB   1 
ATOM   8066  C  CG   . GLN B 1 182 ? 11.965  29.494  6.047   1.00 6.06   ?  405  GLN B CG   1 
ATOM   8067  C  CD   . GLN B 1 182 ? 11.576  29.267  7.496   1.00 5.85   ?  405  GLN B CD   1 
ATOM   8068  O  OE1  . GLN B 1 182 ? 11.055  28.210  7.842   1.00 6.14   ?  405  GLN B OE1  1 
ATOM   8069  N  NE2  . GLN B 1 182 ? 11.808  30.265  8.341   1.00 6.33   ?  405  GLN B NE2  1 
ATOM   8070  H  H    . GLN B 1 182 ? 13.823  29.673  3.868   1.00 6.74   ?  405  GLN B H    1 
ATOM   8071  H  HA   . GLN B 1 182 ? 12.701  27.337  3.572   1.00 5.93   ?  405  GLN B HA   1 
ATOM   8072  H  HB2  . GLN B 1 182 ? 11.986  27.491  5.714   1.00 6.73   ?  405  GLN B HB2  1 
ATOM   8073  H  HB3  . GLN B 1 182 ? 13.434  28.145  5.669   1.00 6.73   ?  405  GLN B HB3  1 
ATOM   8074  H  HG2  . GLN B 1 182 ? 12.644  30.186  6.023   1.00 7.28   ?  405  GLN B HG2  1 
ATOM   8075  H  HG3  . GLN B 1 182 ? 11.175  29.787  5.566   1.00 7.28   ?  405  GLN B HG3  1 
ATOM   8076  H  HE21 . GLN B 1 182 ? 12.163  30.995  8.058   1.00 7.60   ?  405  GLN B HE21 1 
ATOM   8077  H  HE22 . GLN B 1 182 ? 11.603  30.180  9.172   1.00 7.60   ?  405  GLN B HE22 1 
ATOM   8078  N  N    . TRP B 1 183 ? 10.788  29.727  2.889   1.00 5.89   ?  406  TRP B N    1 
ATOM   8079  C  CA   . TRP B 1 183 ? 9.453   30.099  2.446   1.00 7.28   ?  406  TRP B CA   1 
ATOM   8080  C  C    . TRP B 1 183 ? 9.324   30.074  0.927   1.00 7.84   ?  406  TRP B C    1 
ATOM   8081  O  O    . TRP B 1 183 ? 8.288   30.472  0.400   1.00 11.46  ?  406  TRP B O    1 
ATOM   8082  C  CB   . TRP B 1 183 ? 9.011   31.453  3.013   1.00 8.38   ?  406  TRP B CB   1 
ATOM   8083  C  CG   . TRP B 1 183 ? 9.009   31.483  4.506   1.00 7.45   ?  406  TRP B CG   1 
ATOM   8084  C  CD1  . TRP B 1 183 ? 9.699   32.353  5.299   1.00 8.12   ?  406  TRP B CD1  1 
ATOM   8085  C  CD2  . TRP B 1 183 ? 8.310   30.598  5.391   1.00 6.93   ?  406  TRP B CD2  1 
ATOM   8086  N  NE1  . TRP B 1 183 ? 9.457   32.078  6.611   1.00 8.24   ?  406  TRP B NE1  1 
ATOM   8087  C  CE2  . TRP B 1 183 ? 8.613   31.005  6.700   1.00 7.35   ?  406  TRP B CE2  1 
ATOM   8088  C  CE3  . TRP B 1 183 ? 7.445   29.521  5.210   1.00 7.57   ?  406  TRP B CE3  1 
ATOM   8089  C  CZ2  . TRP B 1 183 ? 8.092   30.385  7.820   1.00 7.60   ?  406  TRP B CZ2  1 
ATOM   8090  C  CZ3  . TRP B 1 183 ? 6.944   28.879  6.331   1.00 8.24   ?  406  TRP B CZ3  1 
ATOM   8091  C  CH2  . TRP B 1 183 ? 7.278   29.313  7.628   1.00 8.30   ?  406  TRP B CH2  1 
ATOM   8092  H  H    . TRP B 1 183 ? 11.375  30.348  2.791   1.00 7.07   ?  406  TRP B H    1 
ATOM   8093  H  HA   . TRP B 1 183 ? 8.830   29.452  2.811   1.00 8.74   ?  406  TRP B HA   1 
ATOM   8094  H  HB2  . TRP B 1 183 ? 9.620   32.141  2.700   1.00 10.06  ?  406  TRP B HB2  1 
ATOM   8095  H  HB3  . TRP B 1 183 ? 8.110   31.644  2.708   1.00 10.06  ?  406  TRP B HB3  1 
ATOM   8096  H  HD1  . TRP B 1 183 ? 10.253  33.033  4.989   1.00 9.75   ?  406  TRP B HD1  1 
ATOM   8097  H  HE1  . TRP B 1 183 ? 9.783   32.512  7.279   1.00 9.89   ?  406  TRP B HE1  1 
ATOM   8098  H  HE3  . TRP B 1 183 ? 7.208   29.240  4.356   1.00 9.09   ?  406  TRP B HE3  1 
ATOM   8099  H  HZ2  . TRP B 1 183 ? 8.291   30.691  8.676   1.00 9.12   ?  406  TRP B HZ2  1 
ATOM   8100  H  HZ3  . TRP B 1 183 ? 6.378   28.149  6.224   1.00 9.89   ?  406  TRP B HZ3  1 
ATOM   8101  H  HH2  . TRP B 1 183 ? 6.937   28.859  8.365   1.00 9.96   ?  406  TRP B HH2  1 
ATOM   8102  N  N    . GLU B 1 184 ? 10.334  29.611  0.207   1.00 6.76   ?  407  GLU B N    1 
ATOM   8103  C  CA   . GLU B 1 184 ? 10.258  29.461  -1.236  1.00 6.61   ?  407  GLU B CA   1 
ATOM   8104  C  C    . GLU B 1 184 ? 10.117  27.979  -1.546  1.00 6.30   ?  407  GLU B C    1 
ATOM   8105  O  O    . GLU B 1 184 ? 11.019  27.194  -1.242  1.00 7.33   ?  407  GLU B O    1 
ATOM   8106  C  CB   . GLU B 1 184 ? 11.486  30.061  -1.923  1.00 7.35   ?  407  GLU B CB   1 
ATOM   8107  C  CG   . GLU B 1 184 ? 11.593  31.560  -1.677  1.00 8.80   ?  407  GLU B CG   1 
ATOM   8108  C  CD   . GLU B 1 184 ? 12.796  32.215  -2.333  1.00 10.76  ?  407  GLU B CD   1 
ATOM   8109  O  OE1  . GLU B 1 184 ? 13.365  31.640  -3.269  1.00 11.41  ?  407  GLU B OE1  1 
ATOM   8110  O  OE2  . GLU B 1 184 ? 13.163  33.327  -1.889  1.00 13.70  -1 407  GLU B OE2  1 
ATOM   8111  H  H    . GLU B 1 184 ? 11.090  29.372  0.541   1.00 8.11   ?  407  GLU B H    1 
ATOM   8112  H  HA   . GLU B 1 184 ? 9.479   29.926  -1.580  1.00 7.94   ?  407  GLU B HA   1 
ATOM   8113  H  HB2  . GLU B 1 184 ? 12.286  29.637  -1.576  1.00 8.82   ?  407  GLU B HB2  1 
ATOM   8114  H  HB3  . GLU B 1 184 ? 11.421  29.914  -2.880  1.00 8.82   ?  407  GLU B HB3  1 
ATOM   8115  H  HG2  . GLU B 1 184 ? 10.797  31.990  -2.027  1.00 10.56  ?  407  GLU B HG2  1 
ATOM   8116  H  HG3  . GLU B 1 184 ? 11.659  31.713  -0.721  1.00 10.56  ?  407  GLU B HG3  1 
ATOM   8117  N  N    . LEU B 1 185 ? 8.973   27.590  -2.109  1.00 6.61   ?  408  LEU B N    1 
ATOM   8118  C  CA   . LEU B 1 185 ? 8.786   26.192  -2.466  1.00 6.55   ?  408  LEU B CA   1 
ATOM   8119  C  C    . LEU B 1 185 ? 9.721   25.800  -3.609  1.00 6.49   ?  408  LEU B C    1 
ATOM   8120  O  O    . LEU B 1 185 ? 9.994   26.602  -4.505  1.00 7.73   ?  408  LEU B O    1 
ATOM   8121  C  CB   . LEU B 1 185 ? 7.350   25.925  -2.904  1.00 6.97   ?  408  LEU B CB   1 
ATOM   8122  C  CG   . LEU B 1 185 ? 6.312   26.076  -1.798  1.00 7.00   ?  408  LEU B CG   1 
ATOM   8123  C  CD1  . LEU B 1 185 ? 4.927   25.907  -2.381  1.00 9.05   ?  408  LEU B CD1  1 
ATOM   8124  C  CD2  . LEU B 1 185 ? 6.552   25.048  -0.697  1.00 7.78   ?  408  LEU B CD2  1 
ATOM   8125  H  H    . LEU B 1 185 ? 8.309   28.106  -2.289  1.00 7.93   ?  408  LEU B H    1 
ATOM   8126  H  HA   . LEU B 1 185 ? 8.983   25.646  -1.688  1.00 7.87   ?  408  LEU B HA   1 
ATOM   8127  H  HB2  . LEU B 1 185 ? 7.121   26.552  -3.608  1.00 8.36   ?  408  LEU B HB2  1 
ATOM   8128  H  HB3  . LEU B 1 185 ? 7.294   25.016  -3.238  1.00 8.36   ?  408  LEU B HB3  1 
ATOM   8129  H  HG   . LEU B 1 185 ? 6.382   26.958  -1.402  1.00 8.40   ?  408  LEU B HG   1 
ATOM   8130  H  HD11 . LEU B 1 185 ? 4.272   26.010  -1.673  1.00 10.86  ?  408  LEU B HD11 1 
ATOM   8131  H  HD12 . LEU B 1 185 ? 4.787   26.583  -3.062  1.00 10.86  ?  408  LEU B HD12 1 
ATOM   8132  H  HD13 . LEU B 1 185 ? 4.855   25.023  -2.773  1.00 10.86  ?  408  LEU B HD13 1 
ATOM   8133  H  HD21 . LEU B 1 185 ? 5.789   25.042  -0.098  1.00 9.34   ?  408  LEU B HD21 1 
ATOM   8134  H  HD22 . LEU B 1 185 ? 6.663   24.173  -1.100  1.00 9.34   ?  408  LEU B HD22 1 
ATOM   8135  H  HD23 . LEU B 1 185 ? 7.354   25.291  -0.208  1.00 9.34   ?  408  LEU B HD23 1 
ATOM   8136  N  N    . PRO B 1 186 ? 10.191  24.558  -3.622  1.00 6.50   ?  409  PRO B N    1 
ATOM   8137  C  CA   . PRO B 1 186 ? 10.907  24.061  -4.799  1.00 7.20   ?  409  PRO B CA   1 
ATOM   8138  C  C    . PRO B 1 186 ? 9.923   23.835  -5.935  1.00 6.31   ?  409  PRO B C    1 
ATOM   8139  O  O    . PRO B 1 186 ? 8.711   23.853  -5.734  1.00 7.28   ?  409  PRO B O    1 
ATOM   8140  C  CB   . PRO B 1 186 ? 11.514  22.756  -4.290  1.00 9.04   ?  409  PRO B CB   1 
ATOM   8141  C  CG   . PRO B 1 186 ? 10.580  22.292  -3.242  1.00 9.30   ?  409  PRO B CG   1 
ATOM   8142  C  CD   . PRO B 1 186 ? 9.930   23.491  -2.634  1.00 7.14   ?  409  PRO B CD   1 
ATOM   8143  H  HA   . PRO B 1 186 ? 11.619  24.653  -5.088  1.00 8.64   ?  409  PRO B HA   1 
ATOM   8144  H  HB2  . PRO B 1 186 ? 11.573  22.113  -5.014  1.00 10.85  ?  409  PRO B HB2  1 
ATOM   8145  H  HB3  . PRO B 1 186 ? 12.396  22.921  -3.921  1.00 10.85  ?  409  PRO B HB3  1 
ATOM   8146  H  HG2  . PRO B 1 186 ? 9.911   21.717  -3.646  1.00 11.16  ?  409  PRO B HG2  1 
ATOM   8147  H  HG3  . PRO B 1 186 ? 11.076  21.802  -2.568  1.00 11.16  ?  409  PRO B HG3  1 
ATOM   8148  H  HD2  . PRO B 1 186 ? 8.977   23.348  -2.523  1.00 8.57   ?  409  PRO B HD2  1 
ATOM   8149  H  HD3  . PRO B 1 186 ? 10.334  23.706  -1.779  1.00 8.57   ?  409  PRO B HD3  1 
ATOM   8150  N  N    . ASN B 1 187 ? 10.465  23.613  -7.139  1.00 6.73   ?  410  ASN B N    1 
ATOM   8151  C  CA   . ASN B 1 187 ? 9.668   23.165  -8.280  1.00 7.58   ?  410  ASN B CA   1 
ATOM   8152  C  C    . ASN B 1 187 ? 9.620   21.646  -8.197  1.00 6.96   ?  410  ASN B C    1 
ATOM   8153  O  O    . ASN B 1 187 ? 10.581  20.962  -8.568  1.00 8.04   ?  410  ASN B O    1 
ATOM   8154  C  CB   . ASN B 1 187 ? 10.290  23.574  -9.610  1.00 9.30   ?  410  ASN B CB   1 
ATOM   8155  C  CG   . ASN B 1 187 ? 10.196  25.057  -9.891  1.00 11.81  ?  410  ASN B CG   1 
ATOM   8156  O  OD1  . ASN B 1 187 ? 10.368  25.895  -9.011  1.00 15.09  ?  410  ASN B OD1  1 
ATOM   8157  N  ND2  . ASN B 1 187 ? 9.943   25.387  -11.143 1.00 14.32  ?  410  ASN B ND2  1 
ATOM   8158  H  H    . ASN B 1 187 ? 11.300  23.716  -7.317  1.00 8.08   ?  410  ASN B H    1 
ATOM   8159  H  HA   . ASN B 1 187 ? 8.783   23.559  -8.221  1.00 9.09   ?  410  ASN B HA   1 
ATOM   8160  H  HB2  . ASN B 1 187 ? 11.229  23.332  -9.604  1.00 11.16  ?  410  ASN B HB2  1 
ATOM   8161  H  HB3  . ASN B 1 187 ? 9.832   23.107  -10.327 1.00 11.16  ?  410  ASN B HB3  1 
ATOM   8162  H  HD21 . ASN B 1 187 ? 9.843   24.773  -11.737 1.00 17.18  ?  410  ASN B HD21 1 
ATOM   8163  H  HD22 . ASN B 1 187 ? 9.877   26.215  -11.364 1.00 17.18  ?  410  ASN B HD22 1 
ATOM   8164  N  N    . TYR B 1 188 ? 8.520   21.103  -7.691  1.00 6.34   ?  411  TYR B N    1 
ATOM   8165  C  CA   . TYR B 1 188 ? 8.428   19.657  -7.544  1.00 6.30   ?  411  TYR B CA   1 
ATOM   8166  C  C    . TYR B 1 188 ? 8.476   18.930  -8.887  1.00 7.25   ?  411  TYR B C    1 
ATOM   8167  O  O    . TYR B 1 188 ? 8.827   17.742  -8.913  1.00 7.33   ?  411  TYR B O    1 
ATOM   8168  C  CB   . TYR B 1 188 ? 7.167   19.286  -6.784  1.00 6.98   ?  411  TYR B CB   1 
ATOM   8169  C  CG   . TYR B 1 188 ? 7.063   19.826  -5.364  1.00 6.95   ?  411  TYR B CG   1 
ATOM   8170  C  CD1  . TYR B 1 188 ? 7.904   19.385  -4.354  1.00 6.81   ?  411  TYR B CD1  1 
ATOM   8171  C  CD2  . TYR B 1 188 ? 6.104   20.760  -5.029  1.00 7.58   ?  411  TYR B CD2  1 
ATOM   8172  C  CE1  . TYR B 1 188 ? 7.791   19.855  -3.057  1.00 6.47   ?  411  TYR B CE1  1 
ATOM   8173  C  CE2  . TYR B 1 188 ? 5.996   21.252  -3.741  1.00 7.93   ?  411  TYR B CE2  1 
ATOM   8174  C  CZ   . TYR B 1 188 ? 6.833   20.795  -2.757  1.00 6.36   ?  411  TYR B CZ   1 
ATOM   8175  O  OH   . TYR B 1 188 ? 6.686   21.269  -1.472  1.00 7.27   ?  411  TYR B OH   1 
ATOM   8176  H  H    . TYR B 1 188 ? 7.827   21.540  -7.430  1.00 7.61   ?  411  TYR B H    1 
ATOM   8177  H  HA   . TYR B 1 188 ? 9.185   19.351  -7.021  1.00 7.57   ?  411  TYR B HA   1 
ATOM   8178  H  HB2  . TYR B 1 188 ? 6.404   19.627  -7.277  1.00 8.38   ?  411  TYR B HB2  1 
ATOM   8179  H  HB3  . TYR B 1 188 ? 7.120   18.319  -6.727  1.00 8.38   ?  411  TYR B HB3  1 
ATOM   8180  H  HD1  . TYR B 1 188 ? 8.562   18.758  -4.554  1.00 8.17   ?  411  TYR B HD1  1 
ATOM   8181  H  HD2  . TYR B 1 188 ? 5.518   21.065  -5.684  1.00 9.10   ?  411  TYR B HD2  1 
ATOM   8182  H  HE1  . TYR B 1 188 ? 8.359   19.537  -2.392  1.00 7.76   ?  411  TYR B HE1  1 
ATOM   8183  H  HE2  . TYR B 1 188 ? 5.354   21.895  -3.542  1.00 9.52   ?  411  TYR B HE2  1 
ATOM   8184  H  HH   . TYR B 1 188 ? 6.119   21.888  -1.457  1.00 8.73   ?  411  TYR B HH   1 
ATOM   8185  N  N    . SER B 1 189 ? 8.121   19.599  -9.992  1.00 7.46   ?  412  SER B N    1 
ATOM   8186  C  CA   . SER B 1 189 ? 8.213   19.039  -11.334 1.00 8.41   ?  412  SER B CA   1 
ATOM   8187  C  C    . SER B 1 189 ? 9.271   19.727  -12.186 1.00 9.06   ?  412  SER B C    1 
ATOM   8188  O  O    . SER B 1 189 ? 9.244   19.601  -13.413 1.00 11.83  ?  412  SER B O    1 
ATOM   8189  C  CB   . SER B 1 189 ? 6.865   19.096  -12.047 1.00 9.66   ?  412  SER B CB   1 
ATOM   8190  O  OG   . SER B 1 189 ? 5.927   18.282  -11.397 1.00 10.69  ?  412  SER B OG   1 
ATOM   8191  H  H    . SER B 1 189 ? 7.816   20.403  -9.983  1.00 8.95   ?  412  SER B H    1 
ATOM   8192  H  HA   . SER B 1 189 ? 8.463   18.106  -11.239 1.00 10.09  ?  412  SER B HA   1 
ATOM   8193  H  HB2  . SER B 1 189 ? 6.544   20.011  -12.046 1.00 11.59  ?  412  SER B HB2  1 
ATOM   8194  H  HB3  . SER B 1 189 ? 6.976   18.784  -12.959 1.00 11.59  ?  412  SER B HB3  1 
ATOM   8195  H  HG   . SER B 1 189 ? 5.197   18.298  -11.812 1.00 12.83  ?  412  SER B HG   1 
ATOM   8196  N  N    . GLY B 1 190 ? 10.198  20.456  -11.583 1.00 8.23   ?  413  GLY B N    1 
ATOM   8197  C  CA   . GLY B 1 190 ? 11.225  21.086  -12.382 1.00 11.12  ?  413  GLY B CA   1 
ATOM   8198  C  C    . GLY B 1 190 ? 10.788  22.316  -13.164 1.00 11.81  ?  413  GLY B C    1 
ATOM   8199  O  O    . GLY B 1 190 ? 9.728   22.953  -12.946 1.00 11.69  ?  413  GLY B O    1 
ATOM   8200  H  H    . GLY B 1 190 ? 10.249  20.596  -10.736 1.00 9.88   ?  413  GLY B H    1 
ATOM   8201  H  HA2  . GLY B 1 190 ? 11.950  21.355  -11.797 1.00 13.35  ?  413  GLY B HA2  1 
ATOM   8202  H  HA3  . GLY B 1 190 ? 11.560  20.437  -13.021 1.00 13.35  ?  413  GLY B HA3  1 
ATOM   8203  N  N    . ALA B 1 191 ? 11.653  22.645  -14.111 1.00 12.77  ?  414  ALA B N    1 
ATOM   8204  C  CA   . ALA B 1 191 ? 11.608  23.942  -14.736 1.00 13.28  ?  414  ALA B CA   1 
ATOM   8205  C  C    . ALA B 1 191 ? 10.343  24.065  -15.569 1.00 13.30  ?  414  ALA B C    1 
ATOM   8206  O  O    . ALA B 1 191 ? 9.876   23.111  -16.206 1.00 14.59  ?  414  ALA B O    1 
ATOM   8207  C  CB   . ALA B 1 191 ? 12.852  24.155  -15.596 1.00 15.17  ?  414  ALA B CB   1 
ATOM   8208  H  H    . ALA B 1 191 ? 12.275  22.130  -14.407 1.00 15.32  ?  414  ALA B H    1 
ATOM   8209  H  HA   . ALA B 1 191 ? 11.598  24.641  -14.063 1.00 15.94  ?  414  ALA B HA   1 
ATOM   8210  H  HB1  . ALA B 1 191 ? 12.798  25.027  -16.018 1.00 18.20  ?  414  ALA B HB1  1 
ATOM   8211  H  HB2  . ALA B 1 191 ? 13.638  24.110  -15.031 1.00 18.20  ?  414  ALA B HB2  1 
ATOM   8212  H  HB3  . ALA B 1 191 ? 12.890  23.462  -16.273 1.00 18.20  ?  414  ALA B HB3  1 
ATOM   8213  N  N    . LEU B 1 192 ? 9.774   25.248  -15.511 1.00 11.12  ?  415  LEU B N    1 
ATOM   8214  C  CA   . LEU B 1 192 ? 8.652   25.715  -16.304 1.00 9.12   ?  415  LEU B CA   1 
ATOM   8215  C  C    . LEU B 1 192 ? 7.334   25.044  -15.963 1.00 8.49   ?  415  LEU B C    1 
ATOM   8216  O  O    . LEU B 1 192 ? 6.334   25.305  -16.640 1.00 10.24  ?  415  LEU B O    1 
ATOM   8217  C  CB   . LEU B 1 192 ? 8.932   25.652  -17.806 1.00 10.69  ?  415  LEU B CB   1 
ATOM   8218  C  CG   . LEU B 1 192 ? 10.064  26.567  -18.271 1.00 13.88  ?  415  LEU B CG   1 
ATOM   8219  C  CD1  . LEU B 1 192 ? 10.392  26.304  -19.738 1.00 15.07  ?  415  LEU B CD1  1 
ATOM   8220  C  CD2  . LEU B 1 192 ? 9.696   28.023  -18.058 1.00 17.12  ?  415  LEU B CD2  1 
ATOM   8221  H  H    . LEU B 1 192 ? 10.044  25.857  -14.967 1.00 13.35  ?  415  LEU B H    1 
ATOM   8222  H  HA   . LEU B 1 192 ? 8.524   26.651  -16.088 1.00 10.94  ?  415  LEU B HA   1 
ATOM   8223  H  HB2  . LEU B 1 192 ? 9.174   24.741  -18.038 1.00 12.83  ?  415  LEU B HB2  1 
ATOM   8224  H  HB3  . LEU B 1 192 ? 8.128   25.912  -18.282 1.00 12.83  ?  415  LEU B HB3  1 
ATOM   8225  H  HG   . LEU B 1 192 ? 10.857  26.379  -17.745 1.00 16.66  ?  415  LEU B HG   1 
ATOM   8226  H  HD11 . LEU B 1 192 ? 11.118  26.888  -20.009 1.00 18.08  ?  415  LEU B HD11 1 
ATOM   8227  H  HD12 . LEU B 1 192 ? 10.658  25.376  -19.841 1.00 18.08  ?  415  LEU B HD12 1 
ATOM   8228  H  HD13 . LEU B 1 192 ? 9.605   26.483  -20.275 1.00 18.08  ?  415  LEU B HD13 1 
ATOM   8229  H  HD21 . LEU B 1 192 ? 10.314  28.581  -18.557 1.00 20.55  ?  415  LEU B HD21 1 
ATOM   8230  H  HD22 . LEU B 1 192 ? 8.791   28.169  -18.374 1.00 20.55  ?  415  LEU B HD22 1 
ATOM   8231  H  HD23 . LEU B 1 192 ? 9.755   28.229  -17.112 1.00 20.55  ?  415  LEU B HD23 1 
ATOM   8232  N  N    . THR B 1 193 ? 7.269   24.249  -14.901 1.00 8.37   ?  416  THR B N    1 
ATOM   8233  C  CA   . THR B 1 193 ? 6.046   23.544  -14.535 1.00 9.08   ?  416  THR B CA   1 
ATOM   8234  C  C    . THR B 1 193 ? 5.629   23.985  -13.145 1.00 8.87   ?  416  THR B C    1 
ATOM   8235  O  O    . THR B 1 193 ? 6.463   24.069  -12.242 1.00 8.60   ?  416  THR B O    1 
ATOM   8236  C  CB   . THR B 1 193 ? 6.254   22.027  -14.612 1.00 11.22  ?  416  THR B CB   1 
ATOM   8237  O  OG1  . THR B 1 193 ? 6.627   21.675  -15.949 1.00 14.39  ?  416  THR B OG1  1 
ATOM   8238  C  CG2  . THR B 1 193 ? 4.980   21.280  -14.258 1.00 11.33  ?  416  THR B CG2  1 
ATOM   8239  H  H    . THR B 1 193 ? 7.930   24.100  -14.371 1.00 10.04  ?  416  THR B H    1 
ATOM   8240  H  HA   . THR B 1 193 ? 5.324   23.770  -15.142 1.00 10.90  ?  416  THR B HA   1 
ATOM   8241  H  HB   . THR B 1 193 ? 6.945   21.768  -13.983 1.00 13.46  ?  416  THR B HB   1 
ATOM   8242  H  HG1  . THR B 1 193 ? 6.731   20.843  -16.009 1.00 17.27  ?  416  THR B HG1  1 
ATOM   8243  H  HG21 . THR B 1 193 ? 5.096   20.331  -14.421 1.00 13.60  ?  416  THR B HG21 1 
ATOM   8244  H  HG22 . THR B 1 193 ? 4.765   21.416  -13.322 1.00 13.60  ?  416  THR B HG22 1 
ATOM   8245  H  HG23 . THR B 1 193 ? 4.244   21.605  -14.800 1.00 13.60  ?  416  THR B HG23 1 
ATOM   8246  N  N    . LEU B 1 194 ? 4.355   24.324  -12.994 1.00 8.41   ?  417  LEU B N    1 
ATOM   8247  C  CA   . LEU B 1 194 ? 3.840   24.801  -11.722 1.00 8.08   ?  417  LEU B CA   1 
ATOM   8248  C  C    . LEU B 1 194 ? 3.625   23.633  -10.758 1.00 7.73   ?  417  LEU B C    1 
ATOM   8249  O  O    . LEU B 1 194 ? 3.458   22.474  -11.156 1.00 8.89   ?  417  LEU B O    1 
ATOM   8250  C  CB   . LEU B 1 194 ? 2.520   25.533  -11.933 1.00 7.90   ?  417  LEU B CB   1 
ATOM   8251  C  CG   . LEU B 1 194 ? 2.591   26.773  -12.832 1.00 8.63   ?  417  LEU B CG   1 
ATOM   8252  C  CD1  . LEU B 1 194 ? 1.238   27.442  -12.936 1.00 9.55   ?  417  LEU B CD1  1 
ATOM   8253  C  CD2  . LEU B 1 194 ? 3.659   27.738  -12.313 1.00 9.53   ?  417  LEU B CD2  1 
ATOM   8254  H  H    . LEU B 1 194 ? 3.766   24.286  -13.618 1.00 10.10  ?  417  LEU B H    1 
ATOM   8255  H  HA   . LEU B 1 194 ? 4.478   25.414  -11.325 1.00 9.70   ?  417  LEU B HA   1 
ATOM   8256  H  HB2  . LEU B 1 194 ? 1.891   24.917  -12.339 1.00 9.48   ?  417  LEU B HB2  1 
ATOM   8257  H  HB3  . LEU B 1 194 ? 2.191   25.822  -11.068 1.00 9.48   ?  417  LEU B HB3  1 
ATOM   8258  H  HG   . LEU B 1 194 ? 2.844   26.507  -13.730 1.00 10.35  ?  417  LEU B HG   1 
ATOM   8259  H  HD11 . LEU B 1 194 ? 1.310   28.211  -13.523 1.00 11.46  ?  417  LEU B HD11 1 
ATOM   8260  H  HD12 . LEU B 1 194 ? 0.599   26.808  -13.298 1.00 11.46  ?  417  LEU B HD12 1 
ATOM   8261  H  HD13 . LEU B 1 194 ? 0.957   27.725  -12.052 1.00 11.46  ?  417  LEU B HD13 1 
ATOM   8262  H  HD21 . LEU B 1 194 ? 3.565   28.589  -12.769 1.00 11.44  ?  417  LEU B HD21 1 
ATOM   8263  H  HD22 . LEU B 1 194 ? 3.538   27.860  -11.358 1.00 11.44  ?  417  LEU B HD22 1 
ATOM   8264  H  HD23 . LEU B 1 194 ? 4.536   27.364  -12.490 1.00 11.44  ?  417  LEU B HD23 1 
ATOM   8265  N  N    . ASN B 1 195 ? 3.652   23.949  -9.468  1.00 7.14   ?  418  ASN B N    1 
ATOM   8266  C  CA   . ASN B 1 195 ? 3.318   22.973  -8.447  1.00 6.63   ?  418  ASN B CA   1 
ATOM   8267  C  C    . ASN B 1 195 ? 1.813   22.749  -8.379  1.00 7.60   ?  418  ASN B C    1 
ATOM   8268  O  O    . ASN B 1 195 ? 1.020   23.594  -8.789  1.00 7.86   ?  418  ASN B O    1 
ATOM   8269  C  CB   . ASN B 1 195 ? 3.851   23.436  -7.098  1.00 6.14   ?  418  ASN B CB   1 
ATOM   8270  C  CG   . ASN B 1 195 ? 5.363   23.452  -7.043  1.00 6.51   ?  418  ASN B CG   1 
ATOM   8271  O  OD1  . ASN B 1 195 ? 6.038   22.669  -7.716  1.00 7.52   ?  418  ASN B OD1  1 
ATOM   8272  N  ND2  . ASN B 1 195 ? 5.909   24.332  -6.201  1.00 7.38   ?  418  ASN B ND2  1 
ATOM   8273  H  H    . ASN B 1 195 ? 3.861   24.724  -9.161  1.00 8.57   ?  418  ASN B H    1 
ATOM   8274  H  HA   . ASN B 1 195 ? 3.727   22.120  -8.663  1.00 7.96   ?  418  ASN B HA   1 
ATOM   8275  H  HB2  . ASN B 1 195 ? 3.535   24.336  -6.924  1.00 7.37   ?  418  ASN B HB2  1 
ATOM   8276  H  HB3  . ASN B 1 195 ? 3.532   22.834  -6.407  1.00 7.37   ?  418  ASN B HB3  1 
ATOM   8277  H  HD21 . ASN B 1 195 ? 6.764   24.385  -6.129  1.00 8.86   ?  418  ASN B HD21 1 
ATOM   8278  H  HD22 . ASN B 1 195 ? 5.405   24.847  -5.731  1.00 8.86   ?  418  ASN B HD22 1 
ATOM   8279  N  N    . MET B 1 196 ? 1.437   21.587  -7.833  1.00 7.83   ?  419  MET B N    1 
ATOM   8280  C  CA   A MET B 1 196 ? 0.050   21.163  -7.745  0.74 9.14   ?  419  MET B CA   1 
ATOM   8281  C  CA   B MET B 1 196 ? 0.061   21.124  -7.761  0.26 8.60   ?  419  MET B CA   1 
ATOM   8282  C  C    . MET B 1 196 ? -0.203  20.531  -6.383  1.00 8.01   ?  419  MET B C    1 
ATOM   8283  O  O    . MET B 1 196 ? 0.726   20.213  -5.640  1.00 9.10   ?  419  MET B O    1 
ATOM   8284  C  CB   A MET B 1 196 ? -0.299  20.147  -8.846  0.74 11.69  ?  419  MET B CB   1 
ATOM   8285  C  CB   B MET B 1 196 ? -0.186  20.019  -8.798  0.26 10.08  ?  419  MET B CB   1 
ATOM   8286  C  CG   A MET B 1 196 ? -0.097  20.674  -10.248 0.74 13.28  ?  419  MET B CG   1 
ATOM   8287  C  CG   B MET B 1 196 ? 0.079   20.447  -10.219 0.26 11.30  ?  419  MET B CG   1 
ATOM   8288  S  SD   A MET B 1 196 ? -0.519  19.502  -11.549 0.74 16.22  ?  419  MET B SD   1 
ATOM   8289  S  SD   B MET B 1 196 ? -1.264  21.468  -10.817 0.26 13.47  ?  419  MET B SD   1 
ATOM   8290  C  CE   A MET B 1 196 ? -2.275  19.248  -11.309 0.74 16.52  ?  419  MET B CE   1 
ATOM   8291  C  CE   B MET B 1 196 ? -2.493  20.217  -11.174 0.26 13.92  ?  419  MET B CE   1 
ATOM   8292  H  H    A MET B 1 196 ? 1.987   21.016  -7.500  0.74 9.40   ?  419  MET B H    1 
ATOM   8293  H  H    B MET B 1 196 ? 1.991   21.029  -7.484  0.26 9.40   ?  419  MET B H    1 
ATOM   8294  H  HA   A MET B 1 196 ? -0.512  21.947  -7.848  0.74 10.97  ?  419  MET B HA   1 
ATOM   8295  H  HA   B MET B 1 196 ? -0.526  21.880  -7.919  0.26 10.32  ?  419  MET B HA   1 
ATOM   8296  H  HB2  A MET B 1 196 ? 0.266   19.366  -8.739  0.74 14.03  ?  419  MET B HB2  1 
ATOM   8297  H  HB2  B MET B 1 196 ? 0.399   19.271  -8.600  0.26 12.10  ?  419  MET B HB2  1 
ATOM   8298  H  HB3  A MET B 1 196 ? -1.232  19.897  -8.755  0.74 14.03  ?  419  MET B HB3  1 
ATOM   8299  H  HB3  B MET B 1 196 ? -1.113  19.740  -8.741  0.26 12.10  ?  419  MET B HB3  1 
ATOM   8300  H  HG2  A MET B 1 196 ? -0.656  21.458  -10.368 0.74 15.94  ?  419  MET B HG2  1 
ATOM   8301  H  HG2  B MET B 1 196 ? 0.901   20.960  -10.256 0.26 13.56  ?  419  MET B HG2  1 
ATOM   8302  H  HG3  A MET B 1 196 ? 0.837   20.911  -10.359 0.74 15.94  ?  419  MET B HG3  1 
ATOM   8303  H  HG3  B MET B 1 196 ? 0.151   19.663  -10.786 0.26 13.56  ?  419  MET B HG3  1 
ATOM   8304  H  HE1  A MET B 1 196 ? -2.608  18.667  -12.010 0.74 19.83  ?  419  MET B HE1  1 
ATOM   8305  H  HE1  B MET B 1 196 ? -2.048  19.365  -11.304 0.26 16.71  ?  419  MET B HE1  1 
ATOM   8306  H  HE2  A MET B 1 196 ? -2.419  18.838  -10.442 0.74 19.83  ?  419  MET B HE2  1 
ATOM   8307  H  HE2  B MET B 1 196 ? -3.109  20.158  -10.427 0.26 16.71  ?  419  MET B HE2  1 
ATOM   8308  H  HE3  A MET B 1 196 ? -2.726  20.106  -11.348 0.74 19.83  ?  419  MET B HE3  1 
ATOM   8309  H  HE3  B MET B 1 196 ? -2.973  20.467  -11.979 0.26 16.71  ?  419  MET B HE3  1 
ATOM   8310  N  N    . GLY B 1 197 ? -1.485  20.347  -6.058  1.00 7.96   ?  420  GLY B N    1 
ATOM   8311  C  CA   . GLY B 1 197 ? -1.886  19.664  -4.834  1.00 8.28   ?  420  GLY B CA   1 
ATOM   8312  C  C    . GLY B 1 197 ? -1.481  20.350  -3.547  1.00 7.86   ?  420  GLY B C    1 
ATOM   8313  O  O    . GLY B 1 197 ? -1.359  19.688  -2.515  1.00 8.73   ?  420  GLY B O    1 
ATOM   8314  H  H    . GLY B 1 197 ? -2.148  20.613  -6.537  1.00 9.55   ?  420  GLY B H    1 
ATOM   8315  H  HA2  . GLY B 1 197 ? -2.852  19.579  -4.830  1.00 9.94   ?  420  GLY B HA2  1 
ATOM   8316  H  HA3  . GLY B 1 197 ? -1.492  18.777  -4.831  1.00 9.94   ?  420  GLY B HA3  1 
ATOM   8317  N  N    . LEU B 1 198 ? -1.277  21.659  -3.578  1.00 7.61   ?  421  LEU B N    1 
ATOM   8318  C  CA   . LEU B 1 198 ? -0.666  22.366  -2.461  1.00 7.14   ?  421  LEU B CA   1 
ATOM   8319  C  C    . LEU B 1 198 ? -1.629  22.627  -1.312  1.00 7.62   ?  421  LEU B C    1 
ATOM   8320  O  O    . LEU B 1 198 ? -2.795  22.986  -1.508  1.00 9.02   ?  421  LEU B O    1 
ATOM   8321  C  CB   . LEU B 1 198 ? -0.152  23.724  -2.941  1.00 6.66   ?  421  LEU B CB   1 
ATOM   8322  C  CG   . LEU B 1 198 ? 0.977   23.727  -3.964  1.00 7.26   ?  421  LEU B CG   1 
ATOM   8323  C  CD1  . LEU B 1 198 ? 1.352   25.159  -4.281  1.00 8.68   ?  421  LEU B CD1  1 
ATOM   8324  C  CD2  . LEU B 1 198 ? 2.198   22.959  -3.503  1.00 7.83   ?  421  LEU B CD2  1 
ATOM   8325  H  H    . LEU B 1 198 ? -1.484  22.167  -4.241  1.00 9.13   ?  421  LEU B H    1 
ATOM   8326  H  HA   . LEU B 1 198 ? 0.051   21.807  -2.125  1.00 8.57   ?  421  LEU B HA   1 
ATOM   8327  H  HB2  . LEU B 1 198 ? -0.897  24.198  -3.344  1.00 7.99   ?  421  LEU B HB2  1 
ATOM   8328  H  HB3  . LEU B 1 198 ? 0.170   24.210  -2.166  1.00 7.99   ?  421  LEU B HB3  1 
ATOM   8329  H  HG   . LEU B 1 198 ? 0.660   23.275  -4.762  1.00 8.72   ?  421  LEU B HG   1 
ATOM   8330  H  HD11 . LEU B 1 198 ? 2.005   25.163  -4.998  1.00 10.42  ?  421  LEU B HD11 1 
ATOM   8331  H  HD12 . LEU B 1 198 ? 0.556   25.641  -4.555  1.00 10.42  ?  421  LEU B HD12 1 
ATOM   8332  H  HD13 . LEU B 1 198 ? 1.731   25.569  -3.487  1.00 10.42  ?  421  LEU B HD13 1 
ATOM   8333  H  HD21 . LEU B 1 198 ? 2.909   23.079  -4.152  1.00 9.40   ?  421  LEU B HD21 1 
ATOM   8334  H  HD22 . LEU B 1 198 ? 2.478   23.301  -2.639  1.00 9.40   ?  421  LEU B HD22 1 
ATOM   8335  H  HD23 . LEU B 1 198 ? 1.971   22.019  -3.430  1.00 9.40   ?  421  LEU B HD23 1 
ATOM   8336  N  N    . ALA B 1 199 ? -1.108  22.529  -0.105  1.00 7.33   ?  422  ALA B N    1 
ATOM   8337  C  CA   . ALA B 1 199 ? -1.766  23.156  1.026   1.00 7.56   ?  422  ALA B CA   1 
ATOM   8338  C  C    . ALA B 1 199 ? -1.752  24.668  0.807   1.00 8.16   ?  422  ALA B C    1 
ATOM   8339  O  O    . ALA B 1 199 ? -0.764  25.213  0.302   1.00 8.27   ?  422  ALA B O    1 
ATOM   8340  C  CB   . ALA B 1 199 ? -1.028  22.794  2.313   1.00 7.65   ?  422  ALA B CB   1 
ATOM   8341  H  H    . ALA B 1 199 ? -0.382  22.109  0.086   1.00 8.80   ?  422  ALA B H    1 
ATOM   8342  H  HA   . ALA B 1 199 ? -2.684  22.856  1.114   1.00 9.08   ?  422  ALA B HA   1 
ATOM   8343  H  HB1  . ALA B 1 199 ? -1.477  23.214  3.063   1.00 9.18   ?  422  ALA B HB1  1 
ATOM   8344  H  HB2  . ALA B 1 199 ? -1.034  21.830  2.420   1.00 9.18   ?  422  ALA B HB2  1 
ATOM   8345  H  HB3  . ALA B 1 199 ? -0.114  23.115  2.254   1.00 9.18   ?  422  ALA B HB3  1 
ATOM   8346  N  N    . PRO B 1 200 ? -2.822  25.373  1.157   1.00 10.28  ?  423  PRO B N    1 
ATOM   8347  C  CA   . PRO B 1 200 ? -2.900  26.804  0.841   1.00 11.38  ?  423  PRO B CA   1 
ATOM   8348  C  C    . PRO B 1 200 ? -1.954  27.634  1.690   1.00 10.60  ?  423  PRO B C    1 
ATOM   8349  O  O    . PRO B 1 200 ? -1.495  27.230  2.759   1.00 10.78  ?  423  PRO B O    1 
ATOM   8350  C  CB   . PRO B 1 200 ? -4.358  27.167  1.151   1.00 13.99  ?  423  PRO B CB   1 
ATOM   8351  C  CG   . PRO B 1 200 ? -4.767  26.190  2.172   1.00 14.63  ?  423  PRO B CG   1 
ATOM   8352  C  CD   . PRO B 1 200 ? -4.067  24.883  1.775   1.00 12.54  ?  423  PRO B CD   1 
ATOM   8353  H  HA   . PRO B 1 200 ? -2.709  26.947  -0.099  1.00 13.66  ?  423  PRO B HA   1 
ATOM   8354  H  HB2  . PRO B 1 200 ? -4.410  28.073  1.493   1.00 16.79  ?  423  PRO B HB2  1 
ATOM   8355  H  HB3  . PRO B 1 200 ? -4.899  27.083  0.350   1.00 16.79  ?  423  PRO B HB3  1 
ATOM   8356  H  HG2  . PRO B 1 200 ? -4.477  26.487  3.049   1.00 17.56  ?  423  PRO B HG2  1 
ATOM   8357  H  HG3  . PRO B 1 200 ? -5.732  26.084  2.161   1.00 17.56  ?  423  PRO B HG3  1 
ATOM   8358  H  HD2  . PRO B 1 200 ? -3.879  24.337  2.554   1.00 15.05  ?  423  PRO B HD2  1 
ATOM   8359  H  HD3  . PRO B 1 200 ? -4.599  24.381  1.138   1.00 15.05  ?  423  PRO B HD3  1 
ATOM   8360  N  N    . SER B 1 201 ? -1.653  28.822  1.191   1.00 11.76  ?  424  SER B N    1 
ATOM   8361  C  CA   . SER B 1 201 ? -0.915  29.775  2.008   1.00 12.14  ?  424  SER B CA   1 
ATOM   8362  C  C    . SER B 1 201 ? -1.774  30.210  3.191   1.00 11.89  ?  424  SER B C    1 
ATOM   8363  O  O    . SER B 1 201 ? -3.007  30.155  3.141   1.00 14.09  ?  424  SER B O    1 
ATOM   8364  C  CB   . SER B 1 201 ? -0.510  30.977  1.165   1.00 13.95  ?  424  SER B CB   1 
ATOM   8365  O  OG   . SER B 1 201 ? -1.647  31.716  0.797   1.00 17.07  ?  424  SER B OG   1 
ATOM   8366  H  H    . SER B 1 201 ? -1.858  29.096  0.402   1.00 14.12  ?  424  SER B H    1 
ATOM   8367  H  HA   . SER B 1 201 ? -0.103  29.372  2.354   1.00 14.56  ?  424  SER B HA   1 
ATOM   8368  H  HB2  . SER B 1 201 ? 0.084   31.544  1.683   1.00 16.74  ?  424  SER B HB2  1 
ATOM   8369  H  HB3  . SER B 1 201 ? -0.058  30.668  0.365   1.00 16.74  ?  424  SER B HB3  1 
ATOM   8370  H  HG   . SER B 1 201 ? -2.172  31.234  0.352   1.00 20.48  ?  424  SER B HG   1 
ATOM   8371  N  N    . VAL B 1 202 ? -1.119  30.628  4.268   1.00 9.95   ?  425  VAL B N    1 
ATOM   8372  C  CA   . VAL B 1 202 ? -1.799  31.056  5.483   1.00 10.40  ?  425  VAL B CA   1 
ATOM   8373  C  C    . VAL B 1 202 ? -1.317  32.451  5.838   1.00 10.00  ?  425  VAL B C    1 
ATOM   8374  O  O    . VAL B 1 202 ? -0.164  32.819  5.586   1.00 9.94   ?  425  VAL B O    1 
ATOM   8375  C  CB   . VAL B 1 202 ? -1.564  30.084  6.667   1.00 11.78  ?  425  VAL B CB   1 
ATOM   8376  C  CG1  . VAL B 1 202 ? -2.103  28.702  6.329   1.00 13.88  ?  425  VAL B CG1  1 
ATOM   8377  C  CG2  . VAL B 1 202 ? -0.090  29.997  7.025   1.00 11.51  ?  425  VAL B CG2  1 
ATOM   8378  H  H    . VAL B 1 202 ? -0.261  30.674  4.319   1.00 11.94  ?  425  VAL B H    1 
ATOM   8379  H  HA   . VAL B 1 202 ? -2.753  31.089  5.313   1.00 12.48  ?  425  VAL B HA   1 
ATOM   8380  H  HB   . VAL B 1 202 ? -2.039  30.426  7.440   1.00 14.14  ?  425  VAL B HB   1 
ATOM   8381  H  HG11 . VAL B 1 202 ? -1.968  28.115  7.090   1.00 16.66  ?  425  VAL B HG11 1 
ATOM   8382  H  HG12 . VAL B 1 202 ? -3.050  28.772  6.129   1.00 16.66  ?  425  VAL B HG12 1 
ATOM   8383  H  HG13 . VAL B 1 202 ? -1.627  28.357  5.557   1.00 16.66  ?  425  VAL B HG13 1 
ATOM   8384  H  HG21 . VAL B 1 202 ? 0.035   29.295  7.683   1.00 13.82  ?  425  VAL B HG21 1 
ATOM   8385  H  HG22 . VAL B 1 202 ? 0.418   29.795  6.224   1.00 13.82  ?  425  VAL B HG22 1 
ATOM   8386  H  HG23 . VAL B 1 202 ? 0.196   30.848  7.392   1.00 13.82  ?  425  VAL B HG23 1 
ATOM   8387  N  N    . PHE B 1 203 ? -2.206  33.229  6.432   1.00 10.85  ?  426  PHE B N    1 
ATOM   8388  C  CA   . PHE B 1 203 ? -1.859  34.583  6.833   1.00 10.82  ?  426  PHE B CA   1 
ATOM   8389  C  C    . PHE B 1 203 ? -2.858  35.066  7.872   1.00 10.34  ?  426  PHE B C    1 
ATOM   8390  O  O    . PHE B 1 203 ? -4.004  34.591  7.914   1.00 11.10  ?  426  PHE B O    1 
ATOM   8391  C  CB   . PHE B 1 203 ? -1.831  35.530  5.625   1.00 13.78  ?  426  PHE B CB   1 
ATOM   8392  C  CG   . PHE B 1 203 ? -2.981  35.334  4.701   1.00 18.31  ?  426  PHE B CG   1 
ATOM   8393  C  CD1  . PHE B 1 203 ? -2.937  34.355  3.717   1.00 19.35  ?  426  PHE B CD1  1 
ATOM   8394  C  CD2  . PHE B 1 203 ? -4.109  36.109  4.815   1.00 20.64  ?  426  PHE B CD2  1 
ATOM   8395  C  CE1  . PHE B 1 203 ? -3.996  34.155  2.873   1.00 21.92  ?  426  PHE B CE1  1 
ATOM   8396  C  CE2  . PHE B 1 203 ? -5.176  35.920  3.961   1.00 22.21  ?  426  PHE B CE2  1 
ATOM   8397  C  CZ   . PHE B 1 203 ? -5.117  34.938  2.989   1.00 22.38  ?  426  PHE B CZ   1 
ATOM   8398  H  H    . PHE B 1 203 ? -3.014  32.997  6.613   1.00 13.02  ?  426  PHE B H    1 
ATOM   8399  H  HA   . PHE B 1 203 ? -0.981  34.579  7.246   1.00 12.99  ?  426  PHE B HA   1 
ATOM   8400  H  HB2  . PHE B 1 203 ? -1.856  36.446  5.944   1.00 16.54  ?  426  PHE B HB2  1 
ATOM   8401  H  HB3  . PHE B 1 203 ? -1.015  35.376  5.124   1.00 16.54  ?  426  PHE B HB3  1 
ATOM   8402  H  HD1  . PHE B 1 203 ? -2.176  33.828  3.629   1.00 23.22  ?  426  PHE B HD1  1 
ATOM   8403  H  HD2  . PHE B 1 203 ? -4.154  36.765  5.472   1.00 24.77  ?  426  PHE B HD2  1 
ATOM   8404  H  HE1  . PHE B 1 203 ? -3.957  33.491  2.223   1.00 26.30  ?  426  PHE B HE1  1 
ATOM   8405  H  HE2  . PHE B 1 203 ? -5.934  36.453  4.038   1.00 26.66  ?  426  PHE B HE2  1 
ATOM   8406  H  HZ   . PHE B 1 203 ? -5.837  34.809  2.415   1.00 26.86  ?  426  PHE B HZ   1 
ATOM   8407  N  N    . PRO B 1 204 ? -2.461  36.019  8.714   1.00 10.50  ?  427  PRO B N    1 
ATOM   8408  C  CA   . PRO B 1 204 ? -3.423  36.615  9.649   1.00 11.66  ?  427  PRO B CA   1 
ATOM   8409  C  C    . PRO B 1 204 ? -4.356  37.552  8.902   1.00 12.28  ?  427  PRO B C    1 
ATOM   8410  O  O    . PRO B 1 204 ? -3.926  38.361  8.075   1.00 16.25  ?  427  PRO B O    1 
ATOM   8411  C  CB   . PRO B 1 204 ? -2.541  37.388  10.637  1.00 13.23  ?  427  PRO B CB   1 
ATOM   8412  C  CG   . PRO B 1 204 ? -1.142  37.091  10.268  1.00 14.26  ?  427  PRO B CG   1 
ATOM   8413  C  CD   . PRO B 1 204 ? -1.133  36.634  8.837   1.00 11.99  ?  427  PRO B CD   1 
ATOM   8414  H  HA   . PRO B 1 204 ? -3.924  35.932  10.122  1.00 13.99  ?  427  PRO B HA   1 
ATOM   8415  H  HB2  . PRO B 1 204 ? -2.721  38.338  10.558  1.00 15.87  ?  427  PRO B HB2  1 
ATOM   8416  H  HB3  . PRO B 1 204 ? -2.727  37.089  11.541  1.00 15.87  ?  427  PRO B HB3  1 
ATOM   8417  H  HG2  . PRO B 1 204 ? -0.607  37.894  10.369  1.00 17.11  ?  427  PRO B HG2  1 
ATOM   8418  H  HG3  . PRO B 1 204 ? -0.801  36.391  10.847  1.00 17.11  ?  427  PRO B HG3  1 
ATOM   8419  H  HD2  . PRO B 1 204 ? -1.035  37.384  8.230   1.00 14.40  ?  427  PRO B HD2  1 
ATOM   8420  H  HD3  . PRO B 1 204 ? -0.429  35.986  8.679   1.00 14.40  ?  427  PRO B HD3  1 
ATOM   8421  N  N    . THR B 1 205 ? -5.641  37.446  9.190   1.00 11.35  ?  428  THR B N    1 
ATOM   8422  C  CA   . THR B 1 205 ? -6.607  38.377  8.642   1.00 12.48  ?  428  THR B CA   1 
ATOM   8423  C  C    . THR B 1 205 ? -6.999  39.459  9.634   1.00 11.95  ?  428  THR B C    1 
ATOM   8424  O  O    . THR B 1 205 ? -7.409  40.543  9.211   1.00 13.83  ?  428  THR B O    1 
ATOM   8425  C  CB   . THR B 1 205 ? -7.850  37.614  8.178   1.00 14.07  ?  428  THR B CB   1 
ATOM   8426  O  OG1  . THR B 1 205 ? -8.353  36.833  9.257   1.00 14.73  ?  428  THR B OG1  1 
ATOM   8427  C  CG2  . THR B 1 205 ? -7.496  36.666  7.040   1.00 15.56  ?  428  THR B CG2  1 
ATOM   8428  H  H    . THR B 1 205 ? -5.979  36.842  9.701   1.00 13.62  ?  428  THR B H    1 
ATOM   8429  H  HA   . THR B 1 205 ? -6.235  38.820  7.863   1.00 14.98  ?  428  THR B HA   1 
ATOM   8430  H  HB   . THR B 1 205 ? -8.520  38.246  7.873   1.00 16.89  ?  428  THR B HB   1 
ATOM   8431  H  HG1  . THR B 1 205 ? -8.575  37.333  9.894   1.00 17.68  ?  428  THR B HG1  1 
ATOM   8432  H  HG21 . THR B 1 205 ? -8.296  36.224  6.716   1.00 18.68  ?  428  THR B HG21 1 
ATOM   8433  H  HG22 . THR B 1 205 ? -7.093  37.161  6.310   1.00 18.68  ?  428  THR B HG22 1 
ATOM   8434  H  HG23 . THR B 1 205 ? -6.869  35.995  7.350   1.00 18.68  ?  428  THR B HG23 1 
ATOM   8435  N  N    . TYR B 1 206 ? -6.857  39.217  10.905  1.00 10.21  ?  429  TYR B N    1 
ATOM   8436  C  CA   . TYR B 1 206 ? -7.307  40.180  11.903  1.00 10.74  ?  429  TYR B CA   1 
ATOM   8437  C  C    . TYR B 1 206 ? -6.226  41.229  12.124  1.00 10.97  ?  429  TYR B C    1 
ATOM   8438  O  O    . TYR B 1 206 ? -5.057  40.879  12.297  1.00 10.95  ?  429  TYR B O    1 
ATOM   8439  C  CB   . TYR B 1 206 ? -7.603  39.444  13.214  1.00 12.88  ?  429  TYR B CB   1 
ATOM   8440  C  CG   . TYR B 1 206 ? -8.346  40.274  14.232  1.00 15.60  ?  429  TYR B CG   1 
ATOM   8441  C  CD1  . TYR B 1 206 ? -7.668  41.114  15.101  1.00 18.11  ?  429  TYR B CD1  1 
ATOM   8442  C  CD2  . TYR B 1 206 ? -9.728  40.243  14.302  1.00 19.39  ?  429  TYR B CD2  1 
ATOM   8443  C  CE1  . TYR B 1 206 ? -8.349  41.895  16.019  1.00 19.95  ?  429  TYR B CE1  1 
ATOM   8444  C  CE2  . TYR B 1 206 ? -10.420 41.015  15.223  1.00 21.47  ?  429  TYR B CE2  1 
ATOM   8445  C  CZ   . TYR B 1 206 ? -9.729  41.830  16.085  1.00 20.60  ?  429  TYR B CZ   1 
ATOM   8446  O  OH   . TYR B 1 206 ? -10.437 42.601  16.993  1.00 22.61  ?  429  TYR B OH   1 
ATOM   8447  H  H    . TYR B 1 206 ? -6.504  38.504  11.232  1.00 12.26  ?  429  TYR B H    1 
ATOM   8448  H  HA   . TYR B 1 206 ? -8.113  40.632  11.607  1.00 12.89  ?  429  TYR B HA   1 
ATOM   8449  H  HB2  . TYR B 1 206 ? -8.145  38.664  13.017  1.00 15.46  ?  429  TYR B HB2  1 
ATOM   8450  H  HB3  . TYR B 1 206 ? -6.762  39.171  13.614  1.00 15.46  ?  429  TYR B HB3  1 
ATOM   8451  H  HD1  . TYR B 1 206 ? -6.739  41.153  15.067  1.00 21.73  ?  429  TYR B HD1  1 
ATOM   8452  H  HD2  . TYR B 1 206 ? -10.202 39.693  13.720  1.00 23.28  ?  429  TYR B HD2  1 
ATOM   8453  H  HE1  . TYR B 1 206 ? -7.880  42.461  16.589  1.00 23.94  ?  429  TYR B HE1  1 
ATOM   8454  H  HE2  . TYR B 1 206 ? -11.349 40.982  15.256  1.00 25.77  ?  429  TYR B HE2  1 
ATOM   8455  H  HH   . TYR B 1 206 ? -9.907  43.071  17.445  1.00 27.14  ?  429  TYR B HH   1 
ATOM   8456  N  N    . PRO B 1 207 ? -6.568  42.521  12.117  1.00 11.90  ?  430  PRO B N    1 
ATOM   8457  C  CA   A PRO B 1 207 ? -5.534  43.549  12.301  0.66 12.96  ?  430  PRO B CA   1 
ATOM   8458  C  CA   B PRO B 1 207 ? -5.531  43.547  12.299  0.34 12.92  ?  430  PRO B CA   1 
ATOM   8459  C  C    . PRO B 1 207 ? -4.789  43.366  13.615  1.00 13.70  ?  430  PRO B C    1 
ATOM   8460  O  O    . PRO B 1 207 ? -5.384  43.103  14.658  1.00 16.07  ?  430  PRO B O    1 
ATOM   8461  C  CB   A PRO B 1 207 ? -6.330  44.860  12.285  0.66 13.96  ?  430  PRO B CB   1 
ATOM   8462  C  CB   B PRO B 1 207 ? -6.325  44.859  12.280  0.34 13.45  ?  430  PRO B CB   1 
ATOM   8463  C  CG   A PRO B 1 207 ? -7.559  44.551  11.502  0.66 13.31  ?  430  PRO B CG   1 
ATOM   8464  C  CG   B PRO B 1 207 ? -7.696  44.469  12.697  0.34 13.13  ?  430  PRO B CG   1 
ATOM   8465  C  CD   A PRO B 1 207 ? -7.882  43.111  11.784  0.66 12.64  ?  430  PRO B CD   1 
ATOM   8466  C  CD   B PRO B 1 207 ? -7.920  43.110  12.110  0.34 12.65  ?  430  PRO B CD   1 
ATOM   8467  H  HA   A PRO B 1 207 ? -4.903  43.534  11.565  0.66 15.56  ?  430  PRO B HA   1 
ATOM   8468  H  HA   B PRO B 1 207 ? -4.900  43.528  11.563  0.34 15.50  ?  430  PRO B HA   1 
ATOM   8469  H  HB2  A PRO B 1 207 ? -6.552  45.124  13.191  0.66 16.75  ?  430  PRO B HB2  1 
ATOM   8470  H  HB2  B PRO B 1 207 ? -5.936  45.492  12.904  0.34 16.15  ?  430  PRO B HB2  1 
ATOM   8471  H  HB3  A PRO B 1 207 ? -5.810  45.557  11.854  0.66 16.75  ?  430  PRO B HB3  1 
ATOM   8472  H  HB3  B PRO B 1 207 ? -6.325  45.234  11.385  0.34 16.15  ?  430  PRO B HB3  1 
ATOM   8473  H  HG2  A PRO B 1 207 ? -8.284  45.127  11.792  0.66 15.98  ?  430  PRO B HG2  1 
ATOM   8474  H  HG2  B PRO B 1 207 ? -7.749  44.439  13.665  0.34 15.76  ?  430  PRO B HG2  1 
ATOM   8475  H  HG3  A PRO B 1 207 ? -7.386  44.685  10.557  0.66 15.98  ?  430  PRO B HG3  1 
ATOM   8476  H  HG3  B PRO B 1 207 ? -8.339  45.106  12.349  0.34 15.76  ?  430  PRO B HG3  1 
ATOM   8477  H  HD2  A PRO B 1 207 ? -8.493  43.036  12.533  0.66 15.18  ?  430  PRO B HD2  1 
ATOM   8478  H  HD2  B PRO B 1 207 ? -8.527  42.590  12.660  0.34 15.18  ?  430  PRO B HD2  1 
ATOM   8479  H  HD3  A PRO B 1 207 ? -8.262  42.684  11.001  0.66 15.18  ?  430  PRO B HD3  1 
ATOM   8480  H  HD3  B PRO B 1 207 ? -8.265  43.175  11.206  0.34 15.18  ?  430  PRO B HD3  1 
ATOM   8481  N  N    . GLY B 1 208 ? -3.472  43.489  13.560  1.00 14.18  ?  431  GLY B N    1 
ATOM   8482  C  CA   . GLY B 1 208 ? -2.678  43.367  14.763  1.00 13.43  ?  431  GLY B CA   1 
ATOM   8483  C  C    . GLY B 1 208 ? -2.204  41.964  15.075  1.00 11.98  ?  431  GLY B C    1 
ATOM   8484  O  O    . GLY B 1 208 ? -1.464  41.780  16.049  1.00 13.05  ?  431  GLY B O    1 
ATOM   8485  H  H    . GLY B 1 208 ? -3.022  43.641  12.843  1.00 17.02  ?  431  GLY B H    1 
ATOM   8486  H  HA2  . GLY B 1 208 ? -1.894  43.931  14.676  1.00 16.11  ?  431  GLY B HA2  1 
ATOM   8487  H  HA3  . GLY B 1 208 ? -3.206  43.675  15.516  1.00 16.11  ?  431  GLY B HA3  1 
ATOM   8488  N  N    . GLU B 1 209 ? -2.559  40.980  14.269  1.00 9.51   ?  432  GLU B N    1 
ATOM   8489  C  CA   . GLU B 1 209 ? -2.128  39.608  14.512  1.00 7.64   ?  432  GLU B CA   1 
ATOM   8490  C  C    . GLU B 1 209 ? -0.960  39.183  13.626  1.00 6.88   ?  432  GLU B C    1 
ATOM   8491  O  O    . GLU B 1 209 ? -0.792  39.668  12.499  1.00 8.24   ?  432  GLU B O    1 
ATOM   8492  C  CB   . GLU B 1 209 ? -3.296  38.625  14.353  1.00 7.75   ?  432  GLU B CB   1 
ATOM   8493  C  CG   . GLU B 1 209 ? -4.344  38.775  15.444  1.00 8.61   ?  432  GLU B CG   1 
ATOM   8494  C  CD   . GLU B 1 209 ? -5.437  37.731  15.430  1.00 8.65   ?  432  GLU B CD   1 
ATOM   8495  O  OE1  . GLU B 1 209 ? -5.336  36.764  14.650  1.00 8.80   ?  432  GLU B OE1  1 
ATOM   8496  O  OE2  . GLU B 1 209 ? -6.390  37.885  16.222  1.00 9.24   -1 432  GLU B OE2  1 
ATOM   8497  H  H    . GLU B 1 209 ? -3.051  41.078  13.570  1.00 11.42  ?  432  GLU B H    1 
ATOM   8498  H  HA   . GLU B 1 209 ? -1.805  39.563  15.426  1.00 9.17   ?  432  GLU B HA   1 
ATOM   8499  H  HB2  . GLU B 1 209 ? -3.728  38.782  13.499  1.00 9.31   ?  432  GLU B HB2  1 
ATOM   8500  H  HB3  . GLU B 1 209 ? -2.953  37.718  14.389  1.00 9.31   ?  432  GLU B HB3  1 
ATOM   8501  H  HG2  . GLU B 1 209 ? -3.901  38.719  16.306  1.00 10.33  ?  432  GLU B HG2  1 
ATOM   8502  H  HG3  . GLU B 1 209 ? -4.769  39.641  15.345  1.00 10.33  ?  432  GLU B HG3  1 
ATOM   8503  N  N    . GLN B 1 210 ? -0.173  38.247  14.161  1.00 6.54   ?  433  GLN B N    1 
ATOM   8504  C  CA   . GLN B 1 210 ? 0.914   37.584  13.460  1.00 6.31   ?  433  GLN B CA   1 
ATOM   8505  C  C    . GLN B 1 210 ? 0.743   36.080  13.610  1.00 6.31   ?  433  GLN B C    1 
ATOM   8506  O  O    . GLN B 1 210 ? 0.069   35.602  14.522  1.00 6.80   ?  433  GLN B O    1 
ATOM   8507  C  CB   . GLN B 1 210 ? 2.277   37.989  14.049  1.00 7.17   ?  433  GLN B CB   1 
ATOM   8508  C  CG   . GLN B 1 210 ? 2.615   39.440  13.729  1.00 8.38   ?  433  GLN B CG   1 
ATOM   8509  C  CD   . GLN B 1 210 ? 3.912   39.963  14.324  1.00 8.78   ?  433  GLN B CD   1 
ATOM   8510  O  OE1  . GLN B 1 210 ? 4.322   41.083  14.011  1.00 10.30  ?  433  GLN B OE1  1 
ATOM   8511  N  NE2  . GLN B 1 210 ? 4.549   39.187  15.188  1.00 9.07   ?  433  GLN B NE2  1 
ATOM   8512  H  H    . GLN B 1 210 ? -0.258  37.969  14.970  1.00 7.85   ?  433  GLN B H    1 
ATOM   8513  H  HA   . GLN B 1 210 ? 0.892   37.820  12.520  1.00 7.58   ?  433  GLN B HA   1 
ATOM   8514  H  HB2  . GLN B 1 210 ? 2.253   37.886  15.014  1.00 8.60   ?  433  GLN B HB2  1 
ATOM   8515  H  HB3  . GLN B 1 210 ? 2.970   37.423  13.673  1.00 8.60   ?  433  GLN B HB3  1 
ATOM   8516  H  HG2  . GLN B 1 210 ? 2.683   39.531  12.766  1.00 10.06  ?  433  GLN B HG2  1 
ATOM   8517  H  HG3  . GLN B 1 210 ? 1.898   40.000  14.066  1.00 10.06  ?  433  GLN B HG3  1 
ATOM   8518  H  HE21 . GLN B 1 210 ? 4.225   38.418  15.395  1.00 10.89  ?  433  GLN B HE21 1 
ATOM   8519  H  HE22 . GLN B 1 210 ? 5.285   39.454  15.543  1.00 10.89  ?  433  GLN B HE22 1 
ATOM   8520  N  N    . ILE B 1 211 ? 1.370   35.327  12.706  1.00 6.21   ?  434  ILE B N    1 
ATOM   8521  C  CA   . ILE B 1 211 ? 1.442   33.885  12.870  1.00 5.85   ?  434  ILE B CA   1 
ATOM   8522  C  C    . ILE B 1 211 ? 2.439   33.557  13.975  1.00 5.97   ?  434  ILE B C    1 
ATOM   8523  O  O    . ILE B 1 211 ? 3.503   34.177  14.076  1.00 6.20   ?  434  ILE B O    1 
ATOM   8524  C  CB   . ILE B 1 211 ? 1.856   33.213  11.551  1.00 6.51   ?  434  ILE B CB   1 
ATOM   8525  C  CG1  . ILE B 1 211 ? 0.813   33.486  10.472  1.00 8.59   ?  434  ILE B CG1  1 
ATOM   8526  C  CG2  . ILE B 1 211 ? 2.042   31.715  11.754  1.00 6.88   ?  434  ILE B CG2  1 
ATOM   8527  C  CD1  . ILE B 1 211 ? 1.293   33.206  9.070   1.00 10.74  ?  434  ILE B CD1  1 
ATOM   8528  H  H    . ILE B 1 211 ? 1.755   35.628  11.998  1.00 7.46   ?  434  ILE B H    1 
ATOM   8529  H  HA   . ILE B 1 211 ? 0.567   33.552  13.121  1.00 7.02   ?  434  ILE B HA   1 
ATOM   8530  H  HB   . ILE B 1 211 ? 2.702   33.589  11.264  1.00 7.81   ?  434  ILE B HB   1 
ATOM   8531  H  HG12 . ILE B 1 211 ? 0.040   32.924  10.637  1.00 10.31  ?  434  ILE B HG12 1 
ATOM   8532  H  HG13 . ILE B 1 211 ? 0.559   34.421  10.515  1.00 10.31  ?  434  ILE B HG13 1 
ATOM   8533  H  HG21 . ILE B 1 211 ? 2.077   31.281  10.887  1.00 8.25   ?  434  ILE B HG21 1 
ATOM   8534  H  HG22 . ILE B 1 211 ? 2.871   31.562  12.233  1.00 8.25   ?  434  ILE B HG22 1 
ATOM   8535  H  HG23 . ILE B 1 211 ? 1.294   31.370  12.266  1.00 8.25   ?  434  ILE B HG23 1 
ATOM   8536  H  HD11 . ILE B 1 211 ? 0.604   33.473  8.441   1.00 12.89  ?  434  ILE B HD11 1 
ATOM   8537  H  HD12 . ILE B 1 211 ? 2.104   33.712  8.906   1.00 12.89  ?  434  ILE B HD12 1 
ATOM   8538  H  HD13 . ILE B 1 211 ? 1.471   32.256  8.981   1.00 12.89  ?  434  ILE B HD13 1 
ATOM   8539  N  N    . LEU B 1 212 ? 2.113   32.551  14.776  1.00 5.60   ?  435  LEU B N    1 
ATOM   8540  C  CA   . LEU B 1 212 ? 3.021   31.986  15.764  1.00 5.70   ?  435  LEU B CA   1 
ATOM   8541  C  C    . LEU B 1 212 ? 3.576   30.682  15.204  1.00 5.36   ?  435  LEU B C    1 
ATOM   8542  O  O    . LEU B 1 212 ? 2.809   29.823  14.778  1.00 7.35   ?  435  LEU B O    1 
ATOM   8543  C  CB   . LEU B 1 212 ? 2.280   31.699  17.064  1.00 5.72   ?  435  LEU B CB   1 
ATOM   8544  C  CG   . LEU B 1 212 ? 3.154   31.182  18.211  1.00 6.94   ?  435  LEU B CG   1 
ATOM   8545  C  CD1  . LEU B 1 212 ? 4.118   32.235  18.721  1.00 8.57   ?  435  LEU B CD1  1 
ATOM   8546  C  CD2  . LEU B 1 212 ? 2.276   30.662  19.335  1.00 7.49   ?  435  LEU B CD2  1 
ATOM   8547  H  H    . LEU B 1 212 ? 1.344   32.166  14.766  1.00 6.72   ?  435  LEU B H    1 
ATOM   8548  H  HA   . LEU B 1 212 ? 3.747   32.602  15.949  1.00 6.84   ?  435  LEU B HA   1 
ATOM   8549  H  HB2  . LEU B 1 212 ? 1.862   32.520  17.365  1.00 6.87   ?  435  LEU B HB2  1 
ATOM   8550  H  HB3  . LEU B 1 212 ? 1.604   31.027  16.888  1.00 6.87   ?  435  LEU B HB3  1 
ATOM   8551  H  HG   . LEU B 1 212 ? 3.699   30.453  17.875  1.00 8.34   ?  435  LEU B HG   1 
ATOM   8552  H  HD11 . LEU B 1 212 ? 4.595   31.882  19.489  1.00 10.28  ?  435  LEU B HD11 1 
ATOM   8553  H  HD12 . LEU B 1 212 ? 4.745   32.458  18.016  1.00 10.28  ?  435  LEU B HD12 1 
ATOM   8554  H  HD13 . LEU B 1 212 ? 3.616   33.024  18.979  1.00 10.28  ?  435  LEU B HD13 1 
ATOM   8555  H  HD21 . LEU B 1 212 ? 2.842   30.327  20.049  1.00 8.99   ?  435  LEU B HD21 1 
ATOM   8556  H  HD22 . LEU B 1 212 ? 1.723   31.388  19.665  1.00 8.99   ?  435  LEU B HD22 1 
ATOM   8557  H  HD23 . LEU B 1 212 ? 1.716   29.948  18.994  1.00 8.99   ?  435  LEU B HD23 1 
ATOM   8558  N  N    . PHE B 1 213 ? 4.892   30.553  15.201  1.00 5.38   ?  436  PHE B N    1 
ATOM   8559  C  CA   . PHE B 1 213 ? 5.613   29.417  14.643  1.00 5.59   ?  436  PHE B CA   1 
ATOM   8560  C  C    . PHE B 1 213 ? 6.373   28.660  15.730  1.00 5.69   ?  436  PHE B C    1 
ATOM   8561  O  O    . PHE B 1 213 ? 6.682   29.202  16.795  1.00 6.26   ?  436  PHE B O    1 
ATOM   8562  C  CB   . PHE B 1 213 ? 6.653   29.883  13.611  1.00 6.98   ?  436  PHE B CB   1 
ATOM   8563  C  CG   . PHE B 1 213 ? 6.081   30.630  12.436  1.00 6.72   ?  436  PHE B CG   1 
ATOM   8564  C  CD1  . PHE B 1 213 ? 5.688   29.972  11.294  1.00 7.15   ?  436  PHE B CD1  1 
ATOM   8565  C  CD2  . PHE B 1 213 ? 6.017   32.013  12.463  1.00 8.39   ?  436  PHE B CD2  1 
ATOM   8566  C  CE1  . PHE B 1 213 ? 5.198   30.690  10.197  1.00 8.35   ?  436  PHE B CE1  1 
ATOM   8567  C  CE2  . PHE B 1 213 ? 5.554   32.728  11.387  1.00 9.29   ?  436  PHE B CE2  1 
ATOM   8568  C  CZ   . PHE B 1 213 ? 5.153   32.067  10.253  1.00 9.60   ?  436  PHE B CZ   1 
ATOM   8569  H  H    . PHE B 1 213 ? 5.422   31.143  15.535  1.00 6.46   ?  436  PHE B H    1 
ATOM   8570  H  HA   . PHE B 1 213 ? 4.963   28.823  14.234  1.00 6.71   ?  436  PHE B HA   1 
ATOM   8571  H  HB2  . PHE B 1 213 ? 7.283   30.473  14.054  1.00 8.37   ?  436  PHE B HB2  1 
ATOM   8572  H  HB3  . PHE B 1 213 ? 7.115   29.103  13.265  1.00 8.37   ?  436  PHE B HB3  1 
ATOM   8573  H  HD1  . PHE B 1 213 ? 5.748   29.045  11.250  1.00 8.58   ?  436  PHE B HD1  1 
ATOM   8574  H  HD2  . PHE B 1 213 ? 6.293   32.467  13.226  1.00 10.07  ?  436  PHE B HD2  1 
ATOM   8575  H  HE1  . PHE B 1 213 ? 4.906   30.243  9.436   1.00 10.02  ?  436  PHE B HE1  1 
ATOM   8576  H  HE2  . PHE B 1 213 ? 5.513   33.657  11.425  1.00 11.15  ?  436  PHE B HE2  1 
ATOM   8577  H  HZ   . PHE B 1 213 ? 4.850   32.550  9.519   1.00 11.52  ?  436  PHE B HZ   1 
ATOM   8578  N  N    . PHE B 1 214 ? 6.707   27.412  15.409  1.00 5.36   ?  437  PHE B N    1 
ATOM   8579  C  CA   . PHE B 1 214 ? 7.565   26.559  16.214  1.00 5.15   ?  437  PHE B CA   1 
ATOM   8580  C  C    . PHE B 1 214 ? 8.873   26.419  15.445  1.00 5.16   ?  437  PHE B C    1 
ATOM   8581  O  O    . PHE B 1 214 ? 8.900   25.889  14.326  1.00 5.83   ?  437  PHE B O    1 
ATOM   8582  C  CB   . PHE B 1 214 ? 6.889   25.201  16.441  1.00 5.51   ?  437  PHE B CB   1 
ATOM   8583  C  CG   . PHE B 1 214 ? 5.555   25.308  17.163  1.00 5.59   ?  437  PHE B CG   1 
ATOM   8584  C  CD1  . PHE B 1 214 ? 4.392   25.604  16.459  1.00 5.90   ?  437  PHE B CD1  1 
ATOM   8585  C  CD2  . PHE B 1 214 ? 5.459   25.106  18.520  1.00 6.04   ?  437  PHE B CD2  1 
ATOM   8586  C  CE1  . PHE B 1 214 ? 3.177   25.720  17.097  1.00 6.27   ?  437  PHE B CE1  1 
ATOM   8587  C  CE2  . PHE B 1 214 ? 4.236   25.207  19.165  1.00 6.79   ?  437  PHE B CE2  1 
ATOM   8588  C  CZ   . PHE B 1 214 ? 3.097   25.532  18.455  1.00 6.57   ?  437  PHE B CZ   1 
ATOM   8589  H  H    . PHE B 1 214 ? 6.432   27.021  14.694  1.00 6.43   ?  437  PHE B H    1 
ATOM   8590  H  HA   . PHE B 1 214 ? 7.749   26.941  17.086  1.00 6.19   ?  437  PHE B HA   1 
ATOM   8591  H  HB2  . PHE B 1 214 ? 6.730   24.782  15.581  1.00 6.61   ?  437  PHE B HB2  1 
ATOM   8592  H  HB3  . PHE B 1 214 ? 7.475   24.644  16.977  1.00 6.61   ?  437  PHE B HB3  1 
ATOM   8593  H  HD1  . PHE B 1 214 ? 4.436   25.727  15.538  1.00 7.09   ?  437  PHE B HD1  1 
ATOM   8594  H  HD2  . PHE B 1 214 ? 6.222   24.899  19.010  1.00 7.25   ?  437  PHE B HD2  1 
ATOM   8595  H  HE1  . PHE B 1 214 ? 2.412   25.924  16.609  1.00 7.52   ?  437  PHE B HE1  1 
ATOM   8596  H  HE2  . PHE B 1 214 ? 4.182   25.055  20.081  1.00 8.15   ?  437  PHE B HE2  1 
ATOM   8597  H  HZ   . PHE B 1 214 ? 2.282   25.623  18.893  1.00 7.89   ?  437  PHE B HZ   1 
ATOM   8598  N  N    . ARG B 1 215 ? 9.955   26.936  16.012  1.00 5.45   ?  438  ARG B N    1 
ATOM   8599  C  CA   . ARG B 1 215 ? 11.217  27.102  15.315  1.00 5.56   ?  438  ARG B CA   1 
ATOM   8600  C  C    . ARG B 1 215 ? 12.264  26.102  15.789  1.00 5.62   ?  438  ARG B C    1 
ATOM   8601  O  O    . ARG B 1 215 ? 12.404  25.848  16.995  1.00 6.18   ?  438  ARG B O    1 
ATOM   8602  C  CB   . ARG B 1 215 ? 11.764  28.518  15.572  1.00 6.00   ?  438  ARG B CB   1 
ATOM   8603  C  CG   . ARG B 1 215 ? 13.123  28.767  14.948  1.00 7.06   ?  438  ARG B CG   1 
ATOM   8604  C  CD   . ARG B 1 215 ? 13.504  30.235  14.974  1.00 7.13   ?  438  ARG B CD   1 
ATOM   8605  N  NE   . ARG B 1 215 ? 12.688  30.984  14.032  1.00 6.90   ?  438  ARG B NE   1 
ATOM   8606  C  CZ   . ARG B 1 215 ? 12.943  32.213  13.609  1.00 8.04   ?  438  ARG B CZ   1 
ATOM   8607  N  NH1  . ARG B 1 215 ? 13.946  32.924  14.102  1.00 9.91   ?  438  ARG B NH1  1 
ATOM   8608  N  NH2  . ARG B 1 215 ? 12.185  32.733  12.655  1.00 7.59   ?  438  ARG B NH2  1 
ATOM   8609  H  H    . ARG B 1 215 ? 9.981   27.206  16.828  1.00 6.54   ?  438  ARG B H    1 
ATOM   8610  H  HA   . ARG B 1 215 ? 11.068  26.949  14.369  1.00 6.67   ?  438  ARG B HA   1 
ATOM   8611  H  HB2  . ARG B 1 215 ? 11.144  29.165  15.199  1.00 7.21   ?  438  ARG B HB2  1 
ATOM   8612  H  HB3  . ARG B 1 215 ? 11.848  28.652  16.529  1.00 7.21   ?  438  ARG B HB3  1 
ATOM   8613  H  HG2  . ARG B 1 215 ? 13.795  28.271  15.440  1.00 8.47   ?  438  ARG B HG2  1 
ATOM   8614  H  HG3  . ARG B 1 215 ? 13.107  28.476  14.022  1.00 8.47   ?  438  ARG B HG3  1 
ATOM   8615  H  HD2  . ARG B 1 215 ? 13.360  30.593  15.864  1.00 8.56   ?  438  ARG B HD2  1 
ATOM   8616  H  HD3  . ARG B 1 215 ? 14.436  30.334  14.724  1.00 8.56   ?  438  ARG B HD3  1 
ATOM   8617  H  HE   . ARG B 1 215 ? 11.983  30.599  13.726  1.00 8.29   ?  438  ARG B HE   1 
ATOM   8618  H  HH11 . ARG B 1 215 ? 14.451  32.589  14.712  1.00 11.89  ?  438  ARG B HH11 1 
ATOM   8619  H  HH12 . ARG B 1 215 ? 14.093  33.720  13.811  1.00 11.89  ?  438  ARG B HH12 1 
ATOM   8620  H  HH21 . ARG B 1 215 ? 11.540  32.274  12.321  1.00 9.11   ?  438  ARG B HH21 1 
ATOM   8621  H  HH22 . ARG B 1 215 ? 12.339  33.530  12.371  1.00 9.11   ?  438  ARG B HH22 1 
ATOM   8622  N  N    . SER B 1 216 ? 13.038  25.579  14.835  1.00 5.40   ?  439  SER B N    1 
ATOM   8623  C  CA   . SER B 1 216 ? 14.208  24.780  15.125  1.00 5.34   ?  439  SER B CA   1 
ATOM   8624  C  C    . SER B 1 216 ? 15.402  25.253  14.311  1.00 5.20   ?  439  SER B C    1 
ATOM   8625  O  O    . SER B 1 216 ? 15.279  25.564  13.123  1.00 6.32   ?  439  SER B O    1 
ATOM   8626  C  CB   . SER B 1 216 ? 14.011  23.300  14.750  1.00 6.01   ?  439  SER B CB   1 
ATOM   8627  O  OG   . SER B 1 216 ? 12.880  22.756  15.404  1.00 6.83   ?  439  SER B OG   1 
ATOM   8628  H  H    . SER B 1 216 ? 12.894  25.682  13.994  1.00 6.48   ?  439  SER B H    1 
ATOM   8629  H  HA   . SER B 1 216 ? 14.382  24.876  16.075  1.00 6.41   ?  439  SER B HA   1 
ATOM   8630  H  HB2  . SER B 1 216 ? 13.882  23.233  13.791  1.00 7.21   ?  439  SER B HB2  1 
ATOM   8631  H  HB3  . SER B 1 216 ? 14.799  22.800  15.015  1.00 7.21   ?  439  SER B HB3  1 
ATOM   8632  H  HG   . SER B 1 216 ? 13.094  22.486  16.171  1.00 8.20   ?  439  SER B HG   1 
ATOM   8633  N  N    . TYR B 1 217 ? 16.569  25.282  14.952  1.00 5.70   ?  440  TYR B N    1 
ATOM   8634  C  CA   A TYR B 1 217 ? 17.836  25.495  14.258  0.61 6.67   ?  440  TYR B CA   1 
ATOM   8635  C  CA   B TYR B 1 217 ? 17.796  25.521  14.211  0.39 6.94   ?  440  TYR B CA   1 
ATOM   8636  C  C    . TYR B 1 217 ? 18.258  24.219  13.559  1.00 7.25   ?  440  TYR B C    1 
ATOM   8637  O  O    . TYR B 1 217 ? 17.899  23.111  13.980  1.00 11.05  ?  440  TYR B O    1 
ATOM   8638  C  CB   A TYR B 1 217 ? 18.926  25.916  15.239  0.61 7.58   ?  440  TYR B CB   1 
ATOM   8639  C  CB   B TYR B 1 217 ? 18.813  26.232  15.113  0.39 7.72   ?  440  TYR B CB   1 
ATOM   8640  C  CG   A TYR B 1 217 ? 18.689  27.307  15.743  0.61 8.42   ?  440  TYR B CG   1 
ATOM   8641  C  CG   B TYR B 1 217 ? 18.381  27.677  15.369  0.39 8.62   ?  440  TYR B CG   1 
ATOM   8642  C  CD1  A TYR B 1 217 ? 18.963  28.404  14.942  0.61 9.03   ?  440  TYR B CD1  1 
ATOM   8643  C  CD1  B TYR B 1 217 ? 17.389  27.986  16.303  0.39 9.17   ?  440  TYR B CD1  1 
ATOM   8644  C  CD2  A TYR B 1 217 ? 18.168  27.530  17.005  0.61 10.06  ?  440  TYR B CD2  1 
ATOM   8645  C  CD2  B TYR B 1 217 ? 18.923  28.719  14.634  0.39 9.45   ?  440  TYR B CD2  1 
ATOM   8646  C  CE1  A TYR B 1 217 ? 18.730  29.680  15.376  0.61 10.20  ?  440  TYR B CE1  1 
ATOM   8647  C  CE1  B TYR B 1 217 ? 16.977  29.294  16.507  0.39 10.88  ?  440  TYR B CE1  1 
ATOM   8648  C  CE2  A TYR B 1 217 ? 17.930  28.810  17.449  0.61 11.41  ?  440  TYR B CE2  1 
ATOM   8649  C  CE2  B TYR B 1 217 ? 18.516  30.021  14.834  0.39 10.15  ?  440  TYR B CE2  1 
ATOM   8650  C  CZ   A TYR B 1 217 ? 18.224  29.887  16.633  0.61 11.71  ?  440  TYR B CZ   1 
ATOM   8651  C  CZ   B TYR B 1 217 ? 17.542  30.307  15.766  0.39 11.14  ?  440  TYR B CZ   1 
ATOM   8652  O  OH   A TYR B 1 217 ? 17.993  31.183  17.058  0.61 14.06  ?  440  TYR B OH   1 
ATOM   8653  O  OH   B TYR B 1 217 ? 17.148  31.619  15.959  0.39 12.92  ?  440  TYR B OH   1 
ATOM   8654  H  H    A TYR B 1 217 ? 16.655  25.178  15.802  0.61 6.84   ?  440  TYR B H    1 
ATOM   8655  H  H    B TYR B 1 217 ? 16.671  25.167  15.799  0.39 6.84   ?  440  TYR B H    1 
ATOM   8656  H  HA   A TYR B 1 217 ? 17.731  26.202  13.602  0.61 8.01   ?  440  TYR B HA   1 
ATOM   8657  H  HA   B TYR B 1 217 ? 17.685  26.132  13.466  0.39 8.32   ?  440  TYR B HA   1 
ATOM   8658  H  HB2  A TYR B 1 217 ? 18.930  25.311  15.996  0.61 9.10   ?  440  TYR B HB2  1 
ATOM   8659  H  HB2  B TYR B 1 217 ? 18.871  25.770  15.964  0.39 9.26   ?  440  TYR B HB2  1 
ATOM   8660  H  HB3  A TYR B 1 217 ? 19.787  25.894  14.792  0.61 9.10   ?  440  TYR B HB3  1 
ATOM   8661  H  HB3  B TYR B 1 217 ? 19.681  26.240  14.680  0.39 9.26   ?  440  TYR B HB3  1 
ATOM   8662  H  HD1  A TYR B 1 217 ? 19.313  28.270  14.091  0.61 10.83  ?  440  TYR B HD1  1 
ATOM   8663  H  HD1  B TYR B 1 217 ? 16.998  27.302  16.797  0.39 11.01  ?  440  TYR B HD1  1 
ATOM   8664  H  HD2  A TYR B 1 217 ? 17.977  26.807  17.558  0.61 12.07  ?  440  TYR B HD2  1 
ATOM   8665  H  HD2  B TYR B 1 217 ? 19.572  28.536  13.994  0.39 11.35  ?  440  TYR B HD2  1 
ATOM   8666  H  HE1  A TYR B 1 217 ? 18.914  30.404  14.821  0.61 12.24  ?  440  TYR B HE1  1 
ATOM   8667  H  HE1  B TYR B 1 217 ? 16.323  29.486  17.141  0.39 13.05  ?  440  TYR B HE1  1 
ATOM   8668  H  HE2  A TYR B 1 217 ? 17.572  28.951  18.296  0.61 13.69  ?  440  TYR B HE2  1 
ATOM   8669  H  HE2  B TYR B 1 217 ? 18.901  30.708  14.338  0.39 12.19  ?  440  TYR B HE2  1 
ATOM   8670  H  HH   A TYR B 1 217 ? 17.683  31.178  17.839  0.61 16.87  ?  440  TYR B HH   1 
ATOM   8671  H  HH   B TYR B 1 217 ? 16.541  31.653  16.539  0.39 15.50  ?  440  TYR B HH   1 
ATOM   8672  N  N    . LEU B 1 218 ? 19.005  24.369  12.471  1.00 6.22   ?  441  LEU B N    1 
ATOM   8673  C  CA   . LEU B 1 218 ? 19.429  23.228  11.683  1.00 6.49   ?  441  LEU B CA   1 
ATOM   8674  C  C    . LEU B 1 218 ? 20.943  23.149  11.585  1.00 5.97   ?  441  LEU B C    1 
ATOM   8675  O  O    . LEU B 1 218 ? 21.608  24.180  11.439  1.00 6.16   ?  441  LEU B O    1 
ATOM   8676  C  CB   . LEU B 1 218 ? 18.886  23.320  10.252  1.00 7.48   ?  441  LEU B CB   1 
ATOM   8677  C  CG   . LEU B 1 218 ? 17.369  23.336  10.136  1.00 9.17   ?  441  LEU B CG   1 
ATOM   8678  C  CD1  . LEU B 1 218 ? 16.935  23.410  8.687   1.00 12.28  ?  441  LEU B CD1  1 
ATOM   8679  C  CD2  . LEU B 1 218 ? 16.755  22.111  10.768  1.00 11.38  ?  441  LEU B CD2  1 
ATOM   8680  H  H    . LEU B 1 218 ? 19.277  25.128  12.170  1.00 7.47   ?  441  LEU B H    1 
ATOM   8681  H  HA   . LEU B 1 218 ? 19.098  22.426  12.115  1.00 7.78   ?  441  LEU B HA   1 
ATOM   8682  H  HB2  . LEU B 1 218 ? 19.217  24.139  9.851   1.00 8.98   ?  441  LEU B HB2  1 
ATOM   8683  H  HB3  . LEU B 1 218 ? 19.208  22.553  9.753   1.00 8.98   ?  441  LEU B HB3  1 
ATOM   8684  H  HG   . LEU B 1 218 ? 17.050  24.123  10.605  1.00 11.01  ?  441  LEU B HG   1 
ATOM   8685  H  HD11 . LEU B 1 218 ? 15.967  23.462  8.649   1.00 14.73  ?  441  LEU B HD11 1 
ATOM   8686  H  HD12 . LEU B 1 218 ? 17.325  24.199  8.280   1.00 14.73  ?  441  LEU B HD12 1 
ATOM   8687  H  HD13 . LEU B 1 218 ? 17.242  22.614  8.225   1.00 14.73  ?  441  LEU B HD13 1 
ATOM   8688  H  HD21 . LEU B 1 218 ? 15.823  22.052  10.503  1.00 13.65  ?  441  LEU B HD21 1 
ATOM   8689  H  HD22 . LEU B 1 218 ? 17.235  21.325  10.464  1.00 13.65  ?  441  LEU B HD22 1 
ATOM   8690  H  HD23 . LEU B 1 218 ? 16.820  22.186  11.732  1.00 13.65  ?  441  LEU B HD23 1 
ATOM   8691  N  N    . PRO B 1 219 ? 21.498  21.946  11.591  1.00 5.30   ?  442  PRO B N    1 
ATOM   8692  C  CA   . PRO B 1 219 ? 22.942  21.799  11.413  1.00 5.41   ?  442  PRO B CA   1 
ATOM   8693  C  C    . PRO B 1 219 ? 23.386  22.185  10.011  1.00 5.25   ?  442  PRO B C    1 
ATOM   8694  O  O    . PRO B 1 219 ? 22.627  22.073  9.036   1.00 5.60   ?  442  PRO B O    1 
ATOM   8695  C  CB   . PRO B 1 219 ? 23.178  20.301  11.638  1.00 8.16   ?  442  PRO B CB   1 
ATOM   8696  C  CG   . PRO B 1 219 ? 22.006  19.822  12.405  1.00 7.90   ?  442  PRO B CG   1 
ATOM   8697  C  CD   . PRO B 1 219 ? 20.861  20.662  11.948  1.00 6.51   ?  442  PRO B CD   1 
ATOM   8698  H  HA   . PRO B 1 219 ? 23.417  22.327  12.074  1.00 6.49   ?  442  PRO B HA   1 
ATOM   8699  H  HB2  . PRO B 1 219 ? 23.239  19.847  10.782  1.00 9.80   ?  442  PRO B HB2  1 
ATOM   8700  H  HB3  . PRO B 1 219 ? 23.996  20.170  12.141  1.00 9.80   ?  442  PRO B HB3  1 
ATOM   8701  H  HG2  . PRO B 1 219 ? 21.846  18.885  12.210  1.00 9.48   ?  442  PRO B HG2  1 
ATOM   8702  H  HG3  . PRO B 1 219 ? 22.164  19.941  13.354  1.00 9.48   ?  442  PRO B HG3  1 
ATOM   8703  H  HD2  . PRO B 1 219 ? 20.429  20.265  11.175  1.00 7.81   ?  442  PRO B HD2  1 
ATOM   8704  H  HD3  . PRO B 1 219 ? 20.216  20.784  12.662  1.00 7.81   ?  442  PRO B HD3  1 
ATOM   8705  N  N    . LEU B 1 220 ? 24.671  22.571  9.905   1.00 5.29   ?  443  LEU B N    1 
ATOM   8706  C  CA   . LEU B 1 220 ? 25.336  22.833  8.638   1.00 4.81   ?  443  LEU B CA   1 
ATOM   8707  C  C    . LEU B 1 220 ? 26.513  21.887  8.456   1.00 4.83   ?  443  LEU B C    1 
ATOM   8708  O  O    . LEU B 1 220 ? 27.241  21.586  9.406   1.00 5.00   ?  443  LEU B O    1 
ATOM   8709  C  CB   . LEU B 1 220 ? 25.844  24.282  8.583   1.00 5.50   ?  443  LEU B CB   1 
ATOM   8710  C  CG   . LEU B 1 220 ? 24.785  25.320  8.264   1.00 5.69   ?  443  LEU B CG   1 
ATOM   8711  C  CD1  . LEU B 1 220 ? 25.248  26.695  8.653   1.00 6.16   ?  443  LEU B CD1  1 
ATOM   8712  C  CD2  . LEU B 1 220 ? 24.436  25.258  6.786   1.00 6.61   ?  443  LEU B CD2  1 
ATOM   8713  H  H    . LEU B 1 220 ? 25.187  22.688  10.583  1.00 6.35   ?  443  LEU B H    1 
ATOM   8714  H  HA   . LEU B 1 220 ? 24.709  22.683  7.913   1.00 5.78   ?  443  LEU B HA   1 
ATOM   8715  H  HB2  . LEU B 1 220 ? 26.223  24.507  9.447   1.00 6.60   ?  443  LEU B HB2  1 
ATOM   8716  H  HB3  . LEU B 1 220 ? 26.526  24.341  7.896   1.00 6.60   ?  443  LEU B HB3  1 
ATOM   8717  H  HG   . LEU B 1 220 ? 23.984  25.134  8.777   1.00 6.83   ?  443  LEU B HG   1 
ATOM   8718  H  HD11 . LEU B 1 220 ? 24.597  27.345  8.347   1.00 7.40   ?  443  LEU B HD11 1 
ATOM   8719  H  HD12 . LEU B 1 220 ? 25.332  26.739  9.618   1.00 7.40   ?  443  LEU B HD12 1 
ATOM   8720  H  HD13 . LEU B 1 220 ? 26.108  26.867  8.238   1.00 7.40   ?  443  LEU B HD13 1 
ATOM   8721  H  HD21 . LEU B 1 220 ? 23.799  25.960  6.582   1.00 7.94   ?  443  LEU B HD21 1 
ATOM   8722  H  HD22 . LEU B 1 220 ? 25.245  25.383  6.265   1.00 7.94   ?  443  LEU B HD22 1 
ATOM   8723  H  HD23 . LEU B 1 220 ? 24.047  24.391  6.589   1.00 7.94   ?  443  LEU B HD23 1 
ATOM   8724  N  N    . LYS B 1 221 ? 26.727  21.480  7.203   1.00 4.94   ?  444  LYS B N    1 
ATOM   8725  C  CA   . LYS B 1 221 ? 27.898  20.696  6.846   1.00 4.94   ?  444  LYS B CA   1 
ATOM   8726  C  C    . LYS B 1 221 ? 29.188  21.478  7.054   1.00 5.34   ?  444  LYS B C    1 
ATOM   8727  O  O    . LYS B 1 221 ? 30.226  20.893  7.387   1.00 5.69   ?  444  LYS B O    1 
ATOM   8728  C  CB   . LYS B 1 221 ? 27.753  20.235  5.384   1.00 5.41   ?  444  LYS B CB   1 
ATOM   8729  C  CG   . LYS B 1 221 ? 29.006  19.612  4.759   1.00 5.88   ?  444  LYS B CG   1 
ATOM   8730  C  CD   . LYS B 1 221 ? 29.487  18.352  5.479   1.00 6.36   ?  444  LYS B CD   1 
ATOM   8731  C  CE   . LYS B 1 221 ? 30.882  17.989  5.014   1.00 6.46   ?  444  LYS B CE   1 
ATOM   8732  N  NZ   . LYS B 1 221 ? 31.364  16.762  5.693   1.00 5.98   ?  444  LYS B NZ   1 
ATOM   8733  H  H    . LYS B 1 221 ? 26.205  21.647  6.540   1.00 5.93   ?  444  LYS B H    1 
ATOM   8734  H  HA   . LYS B 1 221 ? 27.954  19.911  7.412   1.00 5.93   ?  444  LYS B HA   1 
ATOM   8735  H  HB2  . LYS B 1 221 ? 27.049  19.570  5.343   1.00 6.50   ?  444  LYS B HB2  1 
ATOM   8736  H  HB3  . LYS B 1 221 ? 27.514  21.005  4.845   1.00 6.50   ?  444  LYS B HB3  1 
ATOM   8737  H  HG2  . LYS B 1 221 ? 28.810  19.371  3.840   1.00 7.06   ?  444  LYS B HG2  1 
ATOM   8738  H  HG3  . LYS B 1 221 ? 29.725  20.262  4.786   1.00 7.06   ?  444  LYS B HG3  1 
ATOM   8739  H  HD2  . LYS B 1 221 ? 29.510  18.511  6.436   1.00 7.64   ?  444  LYS B HD2  1 
ATOM   8740  H  HD3  . LYS B 1 221 ? 28.891  17.614  5.280   1.00 7.64   ?  444  LYS B HD3  1 
ATOM   8741  H  HE2  . LYS B 1 221 ? 30.872  17.829  4.058   1.00 7.75   ?  444  LYS B HE2  1 
ATOM   8742  H  HE3  . LYS B 1 221 ? 31.491  18.715  5.223   1.00 7.75   ?  444  LYS B HE3  1 
ATOM   8743  H  HZ1  . LYS B 1 221 ? 32.184  16.561  5.411   1.00 7.17   ?  444  LYS B HZ1  1 
ATOM   8744  H  HZ2  . LYS B 1 221 ? 31.384  16.888  6.573   1.00 7.17   ?  444  LYS B HZ2  1 
ATOM   8745  H  HZ3  . LYS B 1 221 ? 30.821  16.080  5.511   1.00 7.17   ?  444  LYS B HZ3  1 
ATOM   8746  N  N    . GLY B 1 222 ? 29.149  22.788  6.842   1.00 5.41   ?  445  GLY B N    1 
ATOM   8747  C  CA   . GLY B 1 222 ? 30.334  23.617  6.890   1.00 5.75   ?  445  GLY B CA   1 
ATOM   8748  C  C    . GLY B 1 222 ? 29.942  25.068  6.758   1.00 5.88   ?  445  GLY B C    1 
ATOM   8749  O  O    . GLY B 1 222 ? 28.773  25.403  6.579   1.00 6.18   ?  445  GLY B O    1 
ATOM   8750  H  H    . GLY B 1 222 ? 28.431  23.226  6.664   1.00 6.49   ?  445  GLY B H    1 
ATOM   8751  H  HA2  . GLY B 1 222 ? 30.795  23.489  7.734   1.00 6.90   ?  445  GLY B HA2  1 
ATOM   8752  H  HA3  . GLY B 1 222 ? 30.934  23.383  6.164   1.00 6.90   ?  445  GLY B HA3  1 
ATOM   8753  N  N    . GLY B 1 223 ? 30.952  25.919  6.827   1.00 6.19   ?  446  GLY B N    1 
ATOM   8754  C  CA   . GLY B 1 223 ? 30.728  27.345  6.669   1.00 6.67   ?  446  GLY B CA   1 
ATOM   8755  C  C    . GLY B 1 223 ? 30.065  27.981  7.879   1.00 5.98   ?  446  GLY B C    1 
ATOM   8756  O  O    . GLY B 1 223 ? 30.059  27.453  8.991   1.00 6.55   ?  446  GLY B O    1 
ATOM   8757  H  H    . GLY B 1 223 ? 31.772  25.699  6.964   1.00 7.43   ?  446  GLY B H    1 
ATOM   8758  H  HA2  . GLY B 1 223 ? 31.579  27.787  6.523   1.00 8.00   ?  446  GLY B HA2  1 
ATOM   8759  H  HA3  . GLY B 1 223 ? 30.158  27.495  5.899   1.00 8.00   ?  446  GLY B HA3  1 
ATOM   8760  N  N    . TYR B 1 224 ? 29.491  29.157  7.636   1.00 5.45   ?  447  TYR B N    1 
ATOM   8761  C  CA   . TYR B 1 224 ? 28.981  30.026  8.683   1.00 6.46   ?  447  TYR B CA   1 
ATOM   8762  C  C    . TYR B 1 224 ? 27.463  30.094  8.642   1.00 6.32   ?  447  TYR B C    1 
ATOM   8763  O  O    . TYR B 1 224 ? 26.834  29.906  7.591   1.00 6.97   ?  447  TYR B O    1 
ATOM   8764  C  CB   . TYR B 1 224 ? 29.627  31.429  8.564   1.00 7.76   ?  447  TYR B CB   1 
ATOM   8765  C  CG   . TYR B 1 224 ? 31.103  31.302  8.862   1.00 7.19   ?  447  TYR B CG   1 
ATOM   8766  C  CD1  . TYR B 1 224 ? 32.004  30.963  7.867   1.00 8.02   ?  447  TYR B CD1  1 
ATOM   8767  C  CD2  . TYR B 1 224 ? 31.576  31.407  10.162  1.00 8.54   ?  447  TYR B CD2  1 
ATOM   8768  C  CE1  . TYR B 1 224 ? 33.346  30.756  8.159   1.00 10.17  ?  447  TYR B CE1  1 
ATOM   8769  C  CE2  . TYR B 1 224 ? 32.906  31.214  10.465  1.00 10.01  ?  447  TYR B CE2  1 
ATOM   8770  C  CZ   . TYR B 1 224 ? 33.796  30.881  9.458   1.00 10.98  ?  447  TYR B CZ   1 
ATOM   8771  O  OH   . TYR B 1 224 ? 35.130  30.676  9.752   1.00 14.83  ?  447  TYR B OH   1 
ATOM   8772  H  H    . TYR B 1 224 ? 29.384  29.480  6.846   1.00 6.54   ?  447  TYR B H    1 
ATOM   8773  H  HA   . TYR B 1 224 ? 29.204  29.670  9.558   1.00 7.76   ?  447  TYR B HA   1 
ATOM   8774  H  HB2  . TYR B 1 224 ? 29.512  31.772  7.665   1.00 9.31   ?  447  TYR B HB2  1 
ATOM   8775  H  HB3  . TYR B 1 224 ? 29.224  32.035  9.205   1.00 9.31   ?  447  TYR B HB3  1 
ATOM   8776  H  HD1  . TYR B 1 224 ? 31.706  30.873  6.991   1.00 9.63   ?  447  TYR B HD1  1 
ATOM   8777  H  HD2  . TYR B 1 224 ? 30.981  31.613  10.846  1.00 10.25  ?  447  TYR B HD2  1 
ATOM   8778  H  HE1  . TYR B 1 224 ? 33.942  30.534  7.479   1.00 12.21  ?  447  TYR B HE1  1 
ATOM   8779  H  HE2  . TYR B 1 224 ? 33.205  31.307  11.340  1.00 12.01  ?  447  TYR B HE2  1 
ATOM   8780  H  HH   . TYR B 1 224 ? 35.253  30.731  10.581  1.00 17.79  ?  447  TYR B HH   1 
ATOM   8781  N  N    . GLY B 1 225 ? 26.879  30.359  9.808   1.00 6.25   ?  448  GLY B N    1 
ATOM   8782  C  CA   . GLY B 1 225 ? 25.465  30.643  9.924   1.00 6.98   ?  448  GLY B CA   1 
ATOM   8783  C  C    . GLY B 1 225 ? 24.783  29.802  10.987  1.00 6.17   ?  448  GLY B C    1 
ATOM   8784  O  O    . GLY B 1 225 ? 25.338  28.847  11.537  1.00 6.57   ?  448  GLY B O    1 
ATOM   8785  H  H    . GLY B 1 225 ? 27.297  30.378  10.560  1.00 7.50   ?  448  GLY B H    1 
ATOM   8786  H  HA2  . GLY B 1 225 ? 25.345  31.578  10.152  1.00 8.38   ?  448  GLY B HA2  1 
ATOM   8787  H  HA3  . GLY B 1 225 ? 25.033  30.467  9.074   1.00 8.38   ?  448  GLY B HA3  1 
ATOM   8788  N  N    . SER B 1 226 ? 23.534  30.191  11.239  1.00 6.02   ?  449  SER B N    1 
ATOM   8789  C  CA   A SER B 1 226 ? 22.634  29.530  12.182  0.87 6.55   ?  449  SER B CA   1 
ATOM   8790  C  CA   B SER B 1 226 ? 22.642  29.499  12.174  0.13 6.40   ?  449  SER B CA   1 
ATOM   8791  C  C    . SER B 1 226 ? 21.255  29.429  11.550  1.00 6.55   ?  449  SER B C    1 
ATOM   8792  O  O    . SER B 1 226 ? 20.303  30.070  12.014  1.00 7.36   ?  449  SER B O    1 
ATOM   8793  C  CB   A SER B 1 226 ? 22.561  30.321  13.488  0.87 7.41   ?  449  SER B CB   1 
ATOM   8794  C  CB   B SER B 1 226 ? 22.617  30.210  13.526  0.13 6.51   ?  449  SER B CB   1 
ATOM   8795  O  OG   A SER B 1 226 ? 23.817  30.336  14.135  0.87 7.58   ?  449  SER B OG   1 
ATOM   8796  O  OG   B SER B 1 226 ? 22.535  31.607  13.346  0.13 6.46   ?  449  SER B OG   1 
ATOM   8797  H  H    A SER B 1 226 ? 23.168  30.868  10.856  0.87 7.23   ?  449  SER B H    1 
ATOM   8798  H  H    B SER B 1 226 ? 23.167  30.874  10.868  0.13 7.23   ?  449  SER B H    1 
ATOM   8799  H  HA   A SER B 1 226 ? 22.962  28.636  12.365  0.87 7.87   ?  449  SER B HA   1 
ATOM   8800  H  HA   B SER B 1 226 ? 22.958  28.594  12.319  0.13 7.68   ?  449  SER B HA   1 
ATOM   8801  H  HB2  A SER B 1 226 ? 22.295  31.233  13.291  0.87 8.89   ?  449  SER B HB2  1 
ATOM   8802  H  HB2  B SER B 1 226 ? 21.844  29.909  14.029  0.13 7.82   ?  449  SER B HB2  1 
ATOM   8803  H  HB3  A SER B 1 226 ? 21.909  29.905  14.073  0.87 8.89   ?  449  SER B HB3  1 
ATOM   8804  H  HB3  B SER B 1 226 ? 23.430  29.999  14.011  0.13 7.82   ?  449  SER B HB3  1 
ATOM   8805  H  HG   A SER B 1 226 ? 24.388  30.708  13.644  0.87 9.09   ?  449  SER B HG   1 
ATOM   8806  H  HG   B SER B 1 226 ? 23.237  31.891  12.981  0.13 7.75   ?  449  SER B HG   1 
ATOM   8807  N  N    . PRO B 1 227 ? 21.106  28.633  10.493  1.00 6.28   ?  450  PRO B N    1 
ATOM   8808  C  CA   . PRO B 1 227 ? 19.812  28.545  9.805   1.00 6.01   ?  450  PRO B CA   1 
ATOM   8809  C  C    . PRO B 1 227 ? 18.750  27.909  10.678  1.00 5.68   ?  450  PRO B C    1 
ATOM   8810  O  O    . PRO B 1 227 ? 19.039  27.103  11.572  1.00 6.21   ?  450  PRO B O    1 
ATOM   8811  C  CB   . PRO B 1 227 ? 20.122  27.678  8.576   1.00 6.83   ?  450  PRO B CB   1 
ATOM   8812  C  CG   . PRO B 1 227 ? 21.324  26.873  8.988   1.00 6.64   ?  450  PRO B CG   1 
ATOM   8813  C  CD   . PRO B 1 227 ? 22.136  27.805  9.848   1.00 6.71   ?  450  PRO B CD   1 
ATOM   8814  H  HA   . PRO B 1 227 ? 19.512  29.423  9.521   1.00 7.21   ?  450  PRO B HA   1 
ATOM   8815  H  HB2  . PRO B 1 227 ? 19.367  27.103  8.375   1.00 8.20   ?  450  PRO B HB2  1 
ATOM   8816  H  HB3  . PRO B 1 227 ? 20.322  28.242  7.813   1.00 8.20   ?  450  PRO B HB3  1 
ATOM   8817  H  HG2  . PRO B 1 227 ? 21.043  26.092  9.491   1.00 7.97   ?  450  PRO B HG2  1 
ATOM   8818  H  HG3  . PRO B 1 227 ? 21.824  26.600  8.203   1.00 7.97   ?  450  PRO B HG3  1 
ATOM   8819  H  HD2  . PRO B 1 227 ? 22.648  27.311  10.508  1.00 8.06   ?  450  PRO B HD2  1 
ATOM   8820  H  HD3  . PRO B 1 227 ? 22.730  28.348  9.307   1.00 8.06   ?  450  PRO B HD3  1 
ATOM   8821  N  N    . PHE B 1 228 ? 17.502  28.280  10.404  1.00 6.11   ?  451  PHE B N    1 
ATOM   8822  C  CA   . PHE B 1 228 ? 16.359  27.810  11.182  1.00 6.34   ?  451  PHE B CA   1 
ATOM   8823  C  C    . PHE B 1 228 ? 15.168  27.559  10.269  1.00 6.23   ?  451  PHE B C    1 
ATOM   8824  O  O    . PHE B 1 228 ? 15.063  28.113  9.167   1.00 6.29   ?  451  PHE B O    1 
ATOM   8825  C  CB   . PHE B 1 228 ? 15.996  28.816  12.289  1.00 7.36   ?  451  PHE B CB   1 
ATOM   8826  C  CG   . PHE B 1 228 ? 15.773  30.196  11.770  1.00 7.44   ?  451  PHE B CG   1 
ATOM   8827  C  CD1  . PHE B 1 228 ? 14.565  30.546  11.200  1.00 8.43   ?  451  PHE B CD1  1 
ATOM   8828  C  CD2  . PHE B 1 228 ? 16.788  31.129  11.786  1.00 9.79   ?  451  PHE B CD2  1 
ATOM   8829  C  CE1  . PHE B 1 228 ? 14.364  31.807  10.678  1.00 9.20   ?  451  PHE B CE1  1 
ATOM   8830  C  CE2  . PHE B 1 228 ? 16.581  32.398  11.276  1.00 10.59  ?  451  PHE B CE2  1 
ATOM   8831  C  CZ   . PHE B 1 228 ? 15.366  32.732  10.715  1.00 10.54  ?  451  PHE B CZ   1 
ATOM   8832  H  H    . PHE B 1 228 ? 17.288  28.810  9.762   1.00 7.33   ?  451  PHE B H    1 
ATOM   8833  H  HA   . PHE B 1 228 ? 16.580  26.961  11.596  1.00 7.61   ?  451  PHE B HA   1 
ATOM   8834  H  HB2  . PHE B 1 228 ? 15.179  28.524  12.724  1.00 8.83   ?  451  PHE B HB2  1 
ATOM   8835  H  HB3  . PHE B 1 228 ? 16.720  28.852  12.933  1.00 8.83   ?  451  PHE B HB3  1 
ATOM   8836  H  HD1  . PHE B 1 228 ? 13.876  29.922  11.168  1.00 10.12  ?  451  PHE B HD1  1 
ATOM   8837  H  HD2  . PHE B 1 228 ? 17.617  30.904  12.142  1.00 11.74  ?  451  PHE B HD2  1 
ATOM   8838  H  HE1  . PHE B 1 228 ? 13.543  32.027  10.300  1.00 11.05  ?  451  PHE B HE1  1 
ATOM   8839  H  HE2  . PHE B 1 228 ? 17.264  33.028  11.311  1.00 12.71  ?  451  PHE B HE2  1 
ATOM   8840  H  HZ   . PHE B 1 228 ? 15.230  33.583  10.364  1.00 12.66  ?  451  PHE B HZ   1 
ATOM   8841  N  N    . ILE B 1 229 ? 14.252  26.735  10.756  1.00 5.37   ?  452  ILE B N    1 
ATOM   8842  C  CA   . ILE B 1 229 ? 13.051  26.383  10.010  1.00 5.00   ?  452  ILE B CA   1 
ATOM   8843  C  C    . ILE B 1 229 ? 11.863  26.488  10.959  1.00 4.69   ?  452  ILE B C    1 
ATOM   8844  O  O    . ILE B 1 229 ? 11.914  26.036  12.105  1.00 5.53   ?  452  ILE B O    1 
ATOM   8845  C  CB   . ILE B 1 229 ? 13.187  25.001  9.327   1.00 5.10   ?  452  ILE B CB   1 
ATOM   8846  C  CG1  . ILE B 1 229 ? 12.090  24.789  8.273   1.00 5.96   ?  452  ILE B CG1  1 
ATOM   8847  C  CG2  . ILE B 1 229 ? 13.244  23.863  10.321  1.00 6.53   ?  452  ILE B CG2  1 
ATOM   8848  C  CD1  . ILE B 1 229 ? 12.368  23.634  7.317   1.00 6.60   ?  452  ILE B CD1  1 
ATOM   8849  H  H    . ILE B 1 229 ? 14.303  26.361  11.528  1.00 6.44   ?  452  ILE B H    1 
ATOM   8850  H  HA   . ILE B 1 229 ? 12.889  27.017  9.294   1.00 6.00   ?  452  ILE B HA   1 
ATOM   8851  H  HB   . ILE B 1 229 ? 14.041  25.001  8.866   1.00 6.13   ?  452  ILE B HB   1 
ATOM   8852  H  HG12 . ILE B 1 229 ? 11.254  24.602  8.727   1.00 7.15   ?  452  ILE B HG12 1 
ATOM   8853  H  HG13 . ILE B 1 229 ? 12.007  25.597  7.743   1.00 7.15   ?  452  ILE B HG13 1 
ATOM   8854  H  HG21 . ILE B 1 229 ? 13.467  23.044  9.851   1.00 7.84   ?  452  ILE B HG21 1 
ATOM   8855  H  HG22 . ILE B 1 229 ? 13.923  24.058  10.985  1.00 7.84   ?  452  ILE B HG22 1 
ATOM   8856  H  HG23 . ILE B 1 229 ? 12.378  23.774  10.749  1.00 7.84   ?  452  ILE B HG23 1 
ATOM   8857  H  HD11 . ILE B 1 229 ? 11.659  23.592  6.657   1.00 7.92   ?  452  ILE B HD11 1 
ATOM   8858  H  HD12 . ILE B 1 229 ? 13.220  23.785  6.879   1.00 7.92   ?  452  ILE B HD12 1 
ATOM   8859  H  HD13 . ILE B 1 229 ? 12.399  22.807  7.823   1.00 7.92   ?  452  ILE B HD13 1 
ATOM   8860  N  N    . ASP B 1 230 ? 10.793  27.098  10.469  1.00 5.15   ?  453  ASP B N    1 
ATOM   8861  C  CA   . ASP B 1 230 ? 9.601   27.413  11.238  1.00 5.23   ?  453  ASP B CA   1 
ATOM   8862  C  C    . ASP B 1 230 ? 8.431   26.566  10.749  1.00 5.11   ?  453  ASP B C    1 
ATOM   8863  O  O    . ASP B 1 230 ? 8.117   26.569  9.555   1.00 6.07   ?  453  ASP B O    1 
ATOM   8864  C  CB   . ASP B 1 230 ? 9.258   28.892  11.046  1.00 5.37   ?  453  ASP B CB   1 
ATOM   8865  C  CG   . ASP B 1 230 ? 10.246  29.804  11.707  1.00 6.72   ?  453  ASP B CG   1 
ATOM   8866  O  OD1  . ASP B 1 230 ? 10.544  29.567  12.890  1.00 7.95   ?  453  ASP B OD1  1 
ATOM   8867  O  OD2  . ASP B 1 230 ? 10.726  30.760  11.039  1.00 7.31   -1 453  ASP B OD2  1 
ATOM   8868  H  H    . ASP B 1 230 ? 10.732  27.353  9.650   1.00 6.18   ?  453  ASP B H    1 
ATOM   8869  H  HA   . ASP B 1 230 ? 9.750   27.216  12.176  1.00 6.28   ?  453  ASP B HA   1 
ATOM   8870  H  HB2  . ASP B 1 230 ? 9.250   29.094  10.098  1.00 6.44   ?  453  ASP B HB2  1 
ATOM   8871  H  HB3  . ASP B 1 230 ? 8.385   29.066  11.430  1.00 6.44   ?  453  ASP B HB3  1 
ATOM   8872  N  N    . CYS B 1 231 ? 7.794   25.850  11.660  1.00 5.11   ?  454  CYS B N    1 
ATOM   8873  C  CA   . CYS B 1 231 ? 6.621   25.064  11.300  1.00 5.07   ?  454  CYS B CA   1 
ATOM   8874  C  C    . CYS B 1 231 ? 5.366   25.638  11.953  1.00 5.29   ?  454  CYS B C    1 
ATOM   8875  O  O    . CYS B 1 231 ? 5.421   26.383  12.937  1.00 5.34   ?  454  CYS B O    1 
ATOM   8876  C  CB   . CYS B 1 231 ? 6.810   23.574  11.621  1.00 5.09   ?  454  CYS B CB   1 
ATOM   8877  S  SG   . CYS B 1 231 ? 6.824   23.128  13.362  1.00 5.70   ?  454  CYS B SG   1 
ATOM   8878  H  H    . CYS B 1 231 ? 8.020   25.801  12.488  1.00 6.14   ?  454  CYS B H    1 
ATOM   8879  H  HA   . CYS B 1 231 ? 6.483   25.118  10.341  1.00 6.08   ?  454  CYS B HA   1 
ATOM   8880  H  HB2  . CYS B 1 231 ? 6.083   23.082  11.207  1.00 6.12   ?  454  CYS B HB2  1 
ATOM   8881  H  HB3  . CYS B 1 231 ? 7.658   23.290  11.246  1.00 6.12   ?  454  CYS B HB3  1 
ATOM   8882  H  HG   . CYS B 1 231 ? 5.769   23.423  13.850  1.00 6.84   ?  454  CYS B HG   1 
ATOM   8883  N  N    . LEU B 1 232 ? 4.226   25.299  11.368  1.00 5.03   ?  455  LEU B N    1 
ATOM   8884  C  CA   . LEU B 1 232 ? 2.949   25.850  11.826  1.00 5.37   ?  455  LEU B CA   1 
ATOM   8885  C  C    . LEU B 1 232 ? 2.430   25.154  13.086  1.00 5.65   ?  455  LEU B C    1 
ATOM   8886  O  O    . LEU B 1 232 ? 1.861   25.802  13.959  1.00 6.08   ?  455  LEU B O    1 
ATOM   8887  C  CB   . LEU B 1 232 ? 1.899   25.780  10.713  1.00 6.10   ?  455  LEU B CB   1 
ATOM   8888  C  CG   . LEU B 1 232 ? 2.249   26.562  9.459   1.00 6.42   ?  455  LEU B CG   1 
ATOM   8889  C  CD1  . LEU B 1 232 ? 1.139   26.405  8.441   1.00 7.71   ?  455  LEU B CD1  1 
ATOM   8890  C  CD2  . LEU B 1 232 ? 2.539   28.028  9.730   1.00 7.99   ?  455  LEU B CD2  1 
ATOM   8891  H  H    . LEU B 1 232 ? 4.159   24.755  10.705  1.00 6.04   ?  455  LEU B H    1 
ATOM   8892  H  HA   . LEU B 1 232 ? 3.093   26.784  12.043  1.00 6.45   ?  455  LEU B HA   1 
ATOM   8893  H  HB2  . LEU B 1 232 ? 1.784   24.852  10.456  1.00 7.32   ?  455  LEU B HB2  1 
ATOM   8894  H  HB3  . LEU B 1 232 ? 1.064   26.135  11.055  1.00 7.32   ?  455  LEU B HB3  1 
ATOM   8895  H  HG   . LEU B 1 232 ? 3.073   26.199  9.098   1.00 7.71   ?  455  LEU B HG   1 
ATOM   8896  H  HD11 . LEU B 1 232 ? 1.371   26.904  7.642   1.00 9.25   ?  455  LEU B HD11 1 
ATOM   8897  H  HD12 . LEU B 1 232 ? 1.038   25.465  8.226   1.00 9.25   ?  455  LEU B HD12 1 
ATOM   8898  H  HD13 . LEU B 1 232 ? 0.314   26.749  8.817   1.00 9.25   ?  455  LEU B HD13 1 
ATOM   8899  H  HD21 . LEU B 1 232 ? 2.613   28.497  8.884   1.00 9.59   ?  455  LEU B HD21 1 
ATOM   8900  H  HD22 . LEU B 1 232 ? 1.812   28.403  10.253  1.00 9.59   ?  455  LEU B HD22 1 
ATOM   8901  H  HD23 . LEU B 1 232 ? 3.371   28.100  10.223  1.00 9.59   ?  455  LEU B HD23 1 
ATOM   8902  N  N    . VAL B 1 233 ? 2.589   23.834  13.170  1.00 5.42   ?  456  VAL B N    1 
ATOM   8903  C  CA   . VAL B 1 233 ? 2.313   23.062  14.382  1.00 5.68   ?  456  VAL B CA   1 
ATOM   8904  C  C    . VAL B 1 233 ? 3.362   21.973  14.493  1.00 5.39   ?  456  VAL B C    1 
ATOM   8905  O  O    . VAL B 1 233 ? 3.927   21.535  13.485  1.00 5.77   ?  456  VAL B O    1 
ATOM   8906  C  CB   . VAL B 1 233 ? 0.900   22.420  14.374  1.00 6.19   ?  456  VAL B CB   1 
ATOM   8907  C  CG1  . VAL B 1 233 ? -0.201  23.476  14.268  1.00 6.69   ?  456  VAL B CG1  1 
ATOM   8908  C  CG2  . VAL B 1 233 ? 0.782   21.372  13.264  1.00 7.22   ?  456  VAL B CG2  1 
ATOM   8909  H  H    . VAL B 1 233 ? 2.865   23.346  12.518  1.00 6.51   ?  456  VAL B H    1 
ATOM   8910  H  HA   . VAL B 1 233 ? 2.362   23.643  15.158  1.00 6.81   ?  456  VAL B HA   1 
ATOM   8911  H  HB   . VAL B 1 233 ? 0.771   21.967  15.221  1.00 7.42   ?  456  VAL B HB   1 
ATOM   8912  H  HG11 . VAL B 1 233 ? -1.065  23.039  14.326  1.00 8.03   ?  456  VAL B HG11 1 
ATOM   8913  H  HG12 . VAL B 1 233 ? -0.102  24.110  14.995  1.00 8.03   ?  456  VAL B HG12 1 
ATOM   8914  H  HG13 . VAL B 1 233 ? -0.119  23.934  13.417  1.00 8.03   ?  456  VAL B HG13 1 
ATOM   8915  H  HG21 . VAL B 1 233 ? -0.145  21.101  13.183  1.00 8.67   ?  456  VAL B HG21 1 
ATOM   8916  H  HG22 . VAL B 1 233 ? 1.088   21.760  12.430  1.00 8.67   ?  456  VAL B HG22 1 
ATOM   8917  H  HG23 . VAL B 1 233 ? 1.332   20.607  13.494  1.00 8.67   ?  456  VAL B HG23 1 
ATOM   8918  N  N    . PRO B 1 234 ? 3.625   21.496  15.712  1.00 5.38   ?  457  PRO B N    1 
ATOM   8919  C  CA   . PRO B 1 234 ? 4.563   20.373  15.870  1.00 5.57   ?  457  PRO B CA   1 
ATOM   8920  C  C    . PRO B 1 234 ? 4.052   19.108  15.207  1.00 5.37   ?  457  PRO B C    1 
ATOM   8921  O  O    . PRO B 1 234 ? 2.854   18.912  15.031  1.00 5.41   ?  457  PRO B O    1 
ATOM   8922  C  CB   . PRO B 1 234 ? 4.627   20.183  17.388  1.00 7.10   ?  457  PRO B CB   1 
ATOM   8923  C  CG   . PRO B 1 234 ? 4.201   21.511  17.964  1.00 7.36   ?  457  PRO B CG   1 
ATOM   8924  C  CD   . PRO B 1 234 ? 3.169   22.016  17.014  1.00 6.43   ?  457  PRO B CD   1 
ATOM   8925  H  HA   . PRO B 1 234 ? 5.434   20.608  15.513  1.00 6.69   ?  457  PRO B HA   1 
ATOM   8926  H  HB2  . PRO B 1 234 ? 4.021   19.477  17.659  1.00 8.52   ?  457  PRO B HB2  1 
ATOM   8927  H  HB3  . PRO B 1 234 ? 5.533   19.963  17.656  1.00 8.52   ?  457  PRO B HB3  1 
ATOM   8928  H  HG2  . PRO B 1 234 ? 3.827   21.385  18.850  1.00 8.83   ?  457  PRO B HG2  1 
ATOM   8929  H  HG3  . PRO B 1 234 ? 4.960   22.114  18.007  1.00 8.83   ?  457  PRO B HG3  1 
ATOM   8930  H  HD2  . PRO B 1 234 ? 2.293   21.665  17.238  1.00 7.72   ?  457  PRO B HD2  1 
ATOM   8931  H  HD3  . PRO B 1 234 ? 3.147   22.986  17.011  1.00 7.72   ?  457  PRO B HD3  1 
ATOM   8932  N  N    . GLN B 1 235 ? 4.980   18.214  14.881  1.00 5.59   ?  458  GLN B N    1 
ATOM   8933  C  CA   . GLN B 1 235 ? 4.571   16.955  14.266  1.00 5.55   ?  458  GLN B CA   1 
ATOM   8934  C  C    . GLN B 1 235 ? 3.637   16.167  15.182  1.00 5.24   ?  458  GLN B C    1 
ATOM   8935  O  O    . GLN B 1 235 ? 2.735   15.478  14.705  1.00 5.92   ?  458  GLN B O    1 
ATOM   8936  C  CB   . GLN B 1 235 ? 5.802   16.124  13.883  1.00 6.05   ?  458  GLN B CB   1 
ATOM   8937  C  CG   . GLN B 1 235 ? 5.458   14.821  13.187  1.00 6.41   ?  458  GLN B CG   1 
ATOM   8938  C  CD   . GLN B 1 235 ? 4.807   15.026  11.827  1.00 6.64   ?  458  GLN B CD   1 
ATOM   8939  O  OE1  . GLN B 1 235 ? 4.922   16.092  11.194  1.00 6.78   ?  458  GLN B OE1  1 
ATOM   8940  N  NE2  . GLN B 1 235 ? 4.121   13.991  11.347  1.00 8.05   ?  458  GLN B NE2  1 
ATOM   8941  H  H    . GLN B 1 235 ? 5.827   18.308  15.002  1.00 6.71   ?  458  GLN B H    1 
ATOM   8942  H  HA   . GLN B 1 235 ? 4.090   17.146  13.446  1.00 6.66   ?  458  GLN B HA   1 
ATOM   8943  H  HB2  . GLN B 1 235 ? 6.357   16.644  13.282  1.00 7.26   ?  458  GLN B HB2  1 
ATOM   8944  H  HB3  . GLN B 1 235 ? 6.297   15.909  14.689  1.00 7.26   ?  458  GLN B HB3  1 
ATOM   8945  H  HG2  . GLN B 1 235 ? 6.272   14.310  13.054  1.00 7.70   ?  458  GLN B HG2  1 
ATOM   8946  H  HG3  . GLN B 1 235 ? 4.840   14.321  13.742  1.00 7.70   ?  458  GLN B HG3  1 
ATOM   8947  H  HE21 . GLN B 1 235 ? 4.068   13.263  11.802  1.00 9.66   ?  458  GLN B HE21 1 
ATOM   8948  H  HE22 . GLN B 1 235 ? 3.732   14.050  10.583  1.00 9.66   ?  458  GLN B HE22 1 
ATOM   8949  N  N    . GLU B 1 236 ? 3.833   16.253  16.497  1.00 5.36   ?  459  GLU B N    1 
ATOM   8950  C  CA   . GLU B 1 236 ? 2.980   15.508  17.421  1.00 6.21   ?  459  GLU B CA   1 
ATOM   8951  C  C    . GLU B 1 236 ? 1.557   16.054  17.407  1.00 5.86   ?  459  GLU B C    1 
ATOM   8952  O  O    . GLU B 1 236 ? 0.607   15.313  17.705  1.00 6.74   ?  459  GLU B O    1 
ATOM   8953  C  CB   . GLU B 1 236 ? 3.588   15.507  18.816  1.00 6.98   ?  459  GLU B CB   1 
ATOM   8954  C  CG   . GLU B 1 236 ? 4.862   14.648  18.920  1.00 7.29   ?  459  GLU B CG   1 
ATOM   8955  C  CD   . GLU B 1 236 ? 6.092   15.304  18.293  1.00 7.58   ?  459  GLU B CD   1 
ATOM   8956  O  OE1  . GLU B 1 236 ? 6.078   16.529  18.051  1.00 6.74   ?  459  GLU B OE1  1 
ATOM   8957  O  OE2  . GLU B 1 236 ? 7.077   14.585  18.016  1.00 9.63   -1 459  GLU B OE2  1 
ATOM   8958  H  H    . GLU B 1 236 ? 4.443   16.727  16.875  1.00 6.44   ?  459  GLU B H    1 
ATOM   8959  H  HA   . GLU B 1 236 ? 2.931   14.578  17.150  1.00 7.45   ?  459  GLU B HA   1 
ATOM   8960  H  HB2  . GLU B 1 236 ? 3.820   16.417  19.059  1.00 8.38   ?  459  GLU B HB2  1 
ATOM   8961  H  HB3  . GLU B 1 236 ? 2.937   15.153  19.442  1.00 8.38   ?  459  GLU B HB3  1 
ATOM   8962  H  HG2  . GLU B 1 236 ? 5.056   14.488  19.857  1.00 8.74   ?  459  GLU B HG2  1 
ATOM   8963  H  HG3  . GLU B 1 236 ? 4.710   13.806  18.464  1.00 8.74   ?  459  GLU B HG3  1 
ATOM   8964  N  N    . TRP B 1 237 ? 1.383   17.339  17.066  1.00 5.65   ?  460  TRP B N    1 
ATOM   8965  C  CA   . TRP B 1 237 ? 0.028   17.860  16.877  1.00 5.40   ?  460  TRP B CA   1 
ATOM   8966  C  C    . TRP B 1 237 ? -0.608  17.304  15.608  1.00 5.50   ?  460  TRP B C    1 
ATOM   8967  O  O    . TRP B 1 237 ? -1.796  16.987  15.601  1.00 6.12   ?  460  TRP B O    1 
ATOM   8968  C  CB   . TRP B 1 237 ? -0.007  19.382  16.845  1.00 5.72   ?  460  TRP B CB   1 
ATOM   8969  C  CG   . TRP B 1 237 ? 0.276   20.105  18.125  1.00 5.72   ?  460  TRP B CG   1 
ATOM   8970  C  CD1  . TRP B 1 237 ? 1.010   19.693  19.198  1.00 6.44   ?  460  TRP B CD1  1 
ATOM   8971  C  CD2  . TRP B 1 237 ? -0.169  21.429  18.422  1.00 5.34   ?  460  TRP B CD2  1 
ATOM   8972  N  NE1  . TRP B 1 237 ? 1.055   20.689  20.142  1.00 6.61   ?  460  TRP B NE1  1 
ATOM   8973  C  CE2  . TRP B 1 237 ? 0.334   21.765  19.691  1.00 5.41   ?  460  TRP B CE2  1 
ATOM   8974  C  CE3  . TRP B 1 237 ? -0.951  22.356  17.739  1.00 6.12   ?  460  TRP B CE3  1 
ATOM   8975  C  CZ2  . TRP B 1 237 ? 0.087   23.002  20.294  1.00 6.12   ?  460  TRP B CZ2  1 
ATOM   8976  C  CZ3  . TRP B 1 237 ? -1.209  23.579  18.335  1.00 6.34   ?  460  TRP B CZ3  1 
ATOM   8977  C  CH2  . TRP B 1 237 ? -0.689  23.895  19.602  1.00 6.81   ?  460  TRP B CH2  1 
ATOM   8978  H  H    . TRP B 1 237 ? 2.014   17.910  16.943  1.00 6.78   ?  460  TRP B H    1 
ATOM   8979  H  HA   . TRP B 1 237 ? -0.491  17.581  17.648  1.00 6.49   ?  460  TRP B HA   1 
ATOM   8980  H  HB2  . TRP B 1 237 ? 0.655   19.682  16.202  1.00 6.86   ?  460  TRP B HB2  1 
ATOM   8981  H  HB3  . TRP B 1 237 ? -0.893  19.653  16.560  1.00 6.86   ?  460  TRP B HB3  1 
ATOM   8982  H  HD1  . TRP B 1 237 ? 1.419   18.862  19.279  1.00 7.73   ?  460  TRP B HD1  1 
ATOM   8983  H  HE1  . TRP B 1 237 ? 1.469   20.646  20.894  1.00 7.94   ?  460  TRP B HE1  1 
ATOM   8984  H  HE3  . TRP B 1 237 ? -1.294  22.158  16.898  1.00 7.34   ?  460  TRP B HE3  1 
ATOM   8985  H  HZ2  . TRP B 1 237 ? 0.435   23.211  21.130  1.00 7.35   ?  460  TRP B HZ2  1 
ATOM   8986  H  HZ3  . TRP B 1 237 ? -1.735  24.203  17.888  1.00 7.61   ?  460  TRP B HZ3  1 
ATOM   8987  H  HH2  . TRP B 1 237 ? -0.876  24.724  19.979  1.00 8.17   ?  460  TRP B HH2  1 
ATOM   8988  N  N    . VAL B 1 238 ? 0.168   17.176  14.524  1.00 5.51   ?  461  VAL B N    1 
ATOM   8989  C  CA   . VAL B 1 238 ? -0.341  16.532  13.313  1.00 6.31   ?  461  VAL B CA   1 
ATOM   8990  C  C    . VAL B 1 238 ? -0.889  15.158  13.665  1.00 6.41   ?  461  VAL B C    1 
ATOM   8991  O  O    . VAL B 1 238 ? -2.014  14.801  13.308  1.00 6.67   ?  461  VAL B O    1 
ATOM   8992  C  CB   . VAL B 1 238 ? 0.754   16.432  12.235  1.00 6.33   ?  461  VAL B CB   1 
ATOM   8993  C  CG1  . VAL B 1 238 ? 0.283   15.593  11.049  1.00 7.47   ?  461  VAL B CG1  1 
ATOM   8994  C  CG2  . VAL B 1 238 ? 1.193   17.822  11.777  1.00 7.48   ?  461  VAL B CG2  1 
ATOM   8995  H  H    . VAL B 1 238 ? 0.982   17.450  14.467  1.00 6.62   ?  461  VAL B H    1 
ATOM   8996  H  HA   . VAL B 1 238 ? -1.057  17.076  12.950  1.00 7.57   ?  461  VAL B HA   1 
ATOM   8997  H  HB   . VAL B 1 238 ? 1.525   15.989  12.623  1.00 7.59   ?  461  VAL B HB   1 
ATOM   8998  H  HG11 . VAL B 1 238 ? 0.886   15.733  10.302  1.00 8.97   ?  461  VAL B HG11 1 
ATOM   8999  H  HG12 . VAL B 1 238 ? 0.284   14.657  11.304  1.00 8.97   ?  461  VAL B HG12 1 
ATOM   9000  H  HG13 . VAL B 1 238 ? -0.615  15.867  10.804  1.00 8.97   ?  461  VAL B HG13 1 
ATOM   9001  H  HG21 . VAL B 1 238 ? 1.882   17.729  11.101  1.00 8.97   ?  461  VAL B HG21 1 
ATOM   9002  H  HG22 . VAL B 1 238 ? 0.427   18.289  11.406  1.00 8.97   ?  461  VAL B HG22 1 
ATOM   9003  H  HG23 . VAL B 1 238 ? 1.540   18.311  12.539  1.00 8.97   ?  461  VAL B HG23 1 
ATOM   9004  N  N    . ALA B 1 239 ? -0.096  14.361  14.383  1.00 6.19   ?  462  ALA B N    1 
ATOM   9005  C  CA   . ALA B 1 239 ? -0.507  12.996  14.684  1.00 6.86   ?  462  ALA B CA   1 
ATOM   9006  C  C    . ALA B 1 239 ? -1.712  12.972  15.609  1.00 6.66   ?  462  ALA B C    1 
ATOM   9007  O  O    . ALA B 1 239 ? -2.557  12.081  15.503  1.00 7.22   ?  462  ALA B O    1 
ATOM   9008  C  CB   . ALA B 1 239 ? 0.660   12.206  15.285  1.00 7.96   ?  462  ALA B CB   1 
ATOM   9009  H  H    . ALA B 1 239 ? 0.671   14.585  14.701  1.00 7.43   ?  462  ALA B H    1 
ATOM   9010  H  HA   . ALA B 1 239 ? -0.757  12.554  13.858  1.00 8.24   ?  462  ALA B HA   1 
ATOM   9011  H  HB1  . ALA B 1 239 ? 0.362   11.305  15.483  1.00 9.56   ?  462  ALA B HB1  1 
ATOM   9012  H  HB2  . ALA B 1 239 ? 1.388   12.182  14.645  1.00 9.56   ?  462  ALA B HB2  1 
ATOM   9013  H  HB3  . ALA B 1 239 ? 0.951   12.644  16.100  1.00 9.56   ?  462  ALA B HB3  1 
ATOM   9014  N  N    . HIS B 1 240 ? -1.793  13.930  16.530  1.00 6.27   ?  463  HIS B N    1 
ATOM   9015  C  CA   . HIS B 1 240 ? -2.924  14.002  17.441  1.00 6.70   ?  463  HIS B CA   1 
ATOM   9016  C  C    . HIS B 1 240 ? -4.214  14.344  16.705  1.00 6.39   ?  463  HIS B C    1 
ATOM   9017  O  O    . HIS B 1 240 ? -5.225  13.654  16.849  1.00 6.96   ?  463  HIS B O    1 
ATOM   9018  C  CB   . HIS B 1 240 ? -2.616  15.055  18.500  1.00 7.31   ?  463  HIS B CB   1 
ATOM   9019  C  CG   . HIS B 1 240 ? -3.579  15.090  19.635  1.00 7.88   ?  463  HIS B CG   1 
ATOM   9020  N  ND1  . HIS B 1 240 ? -3.484  14.241  20.714  1.00 10.24  ?  463  HIS B ND1  1 
ATOM   9021  C  CD2  . HIS B 1 240 ? -4.634  15.904  19.883  1.00 8.19   ?  463  HIS B CD2  1 
ATOM   9022  C  CE1  . HIS B 1 240 ? -4.449  14.519  21.571  1.00 10.43  ?  463  HIS B CE1  1 
ATOM   9023  N  NE2  . HIS B 1 240 ? -5.162  15.522  21.089  1.00 9.08   ?  463  HIS B NE2  1 
ATOM   9024  H  H    . HIS B 1 240 ? -1.207  14.548  16.646  1.00 7.52   ?  463  HIS B H    1 
ATOM   9025  H  HA   . HIS B 1 240 ? -3.056  13.140  17.868  1.00 8.04   ?  463  HIS B HA   1 
ATOM   9026  H  HB2  . HIS B 1 240 ? -1.737  14.875  18.868  1.00 8.77   ?  463  HIS B HB2  1 
ATOM   9027  H  HB3  . HIS B 1 240 ? -2.627  15.929  18.079  1.00 8.77   ?  463  HIS B HB3  1 
ATOM   9028  H  HD1  . HIS B 1 240 ? -2.891  13.627  20.814  1.00 12.28  ?  463  HIS B HD1  1 
ATOM   9029  H  HD2  . HIS B 1 240 ? -4.942  16.591  19.338  1.00 9.83   ?  463  HIS B HD2  1 
ATOM   9030  H  HE1  . HIS B 1 240 ? -4.602  14.082  22.377  1.00 12.51  ?  463  HIS B HE1  1 
ATOM   9031  N  N    . PHE B 1 241 ? -4.191  15.411  15.897  1.00 5.89   ?  464  PHE B N    1 
ATOM   9032  C  CA   . PHE B 1 241 ? -5.397  15.817  15.186  1.00 6.01   ?  464  PHE B CA   1 
ATOM   9033  C  C    . PHE B 1 241 ? -5.830  14.743  14.196  1.00 6.11   ?  464  PHE B C    1 
ATOM   9034  O  O    . PHE B 1 241 ? -7.023  14.460  14.044  1.00 6.69   ?  464  PHE B O    1 
ATOM   9035  C  CB   . PHE B 1 241 ? -5.166  17.148  14.459  1.00 6.69   ?  464  PHE B CB   1 
ATOM   9036  C  CG   . PHE B 1 241 ? -4.809  18.313  15.356  1.00 6.86   ?  464  PHE B CG   1 
ATOM   9037  C  CD1  . PHE B 1 241 ? -5.190  18.349  16.700  1.00 8.07   ?  464  PHE B CD1  1 
ATOM   9038  C  CD2  . PHE B 1 241 ? -4.119  19.382  14.839  1.00 7.22   ?  464  PHE B CD2  1 
ATOM   9039  C  CE1  . PHE B 1 241 ? -4.860  19.432  17.507  1.00 8.55   ?  464  PHE B CE1  1 
ATOM   9040  C  CE2  . PHE B 1 241 ? -3.801  20.468  15.632  1.00 8.06   ?  464  PHE B CE2  1 
ATOM   9041  C  CZ   . PHE B 1 241 ? -4.168  20.490  16.971  1.00 8.52   ?  464  PHE B CZ   1 
ATOM   9042  H  H    . PHE B 1 241 ? -3.502  15.904  15.749  1.00 7.06   ?  464  PHE B H    1 
ATOM   9043  H  HA   . PHE B 1 241 ? -6.110  15.949  15.831  1.00 7.21   ?  464  PHE B HA   1 
ATOM   9044  H  HB2  . PHE B 1 241 ? -4.438  17.031  13.829  1.00 8.03   ?  464  PHE B HB2  1 
ATOM   9045  H  HB3  . PHE B 1 241 ? -5.979  17.384  13.985  1.00 8.03   ?  464  PHE B HB3  1 
ATOM   9046  H  HD1  . PHE B 1 241 ? -5.671  17.639  17.059  1.00 9.68   ?  464  PHE B HD1  1 
ATOM   9047  H  HD2  . PHE B 1 241 ? -3.863  19.375  13.945  1.00 8.67   ?  464  PHE B HD2  1 
ATOM   9048  H  HE1  . PHE B 1 241 ? -5.107  19.440  18.403  1.00 10.26  ?  464  PHE B HE1  1 
ATOM   9049  H  HE2  . PHE B 1 241 ? -3.340  21.188  15.267  1.00 9.68   ?  464  PHE B HE2  1 
ATOM   9050  H  HZ   . PHE B 1 241 ? -3.945  21.219  17.504  1.00 10.23  ?  464  PHE B HZ   1 
ATOM   9051  N  N    . TYR B 1 242 ? -4.866  14.128  13.512  1.00 6.04   ?  465  TYR B N    1 
ATOM   9052  C  CA   . TYR B 1 242 ? -5.161  13.050  12.575  1.00 7.04   ?  465  TYR B CA   1 
ATOM   9053  C  C    . TYR B 1 242 ? -5.909  11.911  13.258  1.00 6.97   ?  465  TYR B C    1 
ATOM   9054  O  O    . TYR B 1 242 ? -6.890  11.390  12.718  1.00 8.27   ?  465  TYR B O    1 
ATOM   9055  C  CB   . TYR B 1 242 ? -3.849  12.557  11.998  1.00 7.33   ?  465  TYR B CB   1 
ATOM   9056  C  CG   . TYR B 1 242 ? -3.911  11.370  11.085  1.00 8.32   ?  465  TYR B CG   1 
ATOM   9057  C  CD1  . TYR B 1 242 ? -4.349  11.500  9.778   1.00 9.80   ?  465  TYR B CD1  1 
ATOM   9058  C  CD2  . TYR B 1 242 ? -3.472  10.128  11.520  1.00 9.84   ?  465  TYR B CD2  1 
ATOM   9059  C  CE1  . TYR B 1 242 ? -4.359  10.420  8.927   1.00 10.85  ?  465  TYR B CE1  1 
ATOM   9060  C  CE2  . TYR B 1 242 ? -3.470  9.052   10.671  1.00 11.67  ?  465  TYR B CE2  1 
ATOM   9061  C  CZ   . TYR B 1 242 ? -3.918  9.201   9.376   1.00 11.73  ?  465  TYR B CZ   1 
ATOM   9062  O  OH   . TYR B 1 242 ? -3.922  8.141   8.513   1.00 14.54  ?  465  TYR B OH   1 
ATOM   9063  H  H    . TYR B 1 242 ? -4.030  14.319  13.572  1.00 7.25   ?  465  TYR B H    1 
ATOM   9064  H  HA   . TYR B 1 242 ? -5.727  13.378  11.860  1.00 8.45   ?  465  TYR B HA   1 
ATOM   9065  H  HB2  . TYR B 1 242 ? -3.454  13.283  11.490  1.00 8.79   ?  465  TYR B HB2  1 
ATOM   9066  H  HB3  . TYR B 1 242 ? -3.269  12.315  12.737  1.00 8.79   ?  465  TYR B HB3  1 
ATOM   9067  H  HD1  . TYR B 1 242 ? -4.640  12.329  9.472   1.00 11.77  ?  465  TYR B HD1  1 
ATOM   9068  H  HD2  . TYR B 1 242 ? -3.175  10.024  12.395  1.00 11.81  ?  465  TYR B HD2  1 
ATOM   9069  H  HE1  . TYR B 1 242 ? -4.662  10.516  8.053   1.00 13.02  ?  465  TYR B HE1  1 
ATOM   9070  H  HE2  . TYR B 1 242 ? -3.168  8.224   10.968  1.00 14.01  ?  465  TYR B HE2  1 
ATOM   9071  H  HH   . TYR B 1 242 ? -3.601  7.462   8.890   1.00 17.45  ?  465  TYR B HH   1 
ATOM   9072  N  N    . GLN B 1 243 ? -5.440  11.484  14.437  1.00 6.96   ?  466  GLN B N    1 
ATOM   9073  C  CA   . GLN B 1 243 ? -6.103  10.387  15.132  1.00 7.15   ?  466  GLN B CA   1 
ATOM   9074  C  C    . GLN B 1 243 ? -7.436  10.818  15.720  1.00 7.89   ?  466  GLN B C    1 
ATOM   9075  O  O    . GLN B 1 243 ? -8.422  10.078  15.639  1.00 9.71   ?  466  GLN B O    1 
ATOM   9076  C  CB   . GLN B 1 243 ? -5.236  9.873   16.266  1.00 7.52   ?  466  GLN B CB   1 
ATOM   9077  C  CG   . GLN B 1 243 ? -3.997  9.170   15.821  1.00 7.79   ?  466  GLN B CG   1 
ATOM   9078  C  CD   . GLN B 1 243 ? -3.229  8.688   17.001  1.00 8.59   ?  466  GLN B CD   1 
ATOM   9079  O  OE1  . GLN B 1 243 ? -3.541  7.653   17.591  1.00 9.66   ?  466  GLN B OE1  1 
ATOM   9080  N  NE2  . GLN B 1 243 ? -2.235  9.468   17.400  1.00 9.75   ?  466  GLN B NE2  1 
ATOM   9081  H  H    . GLN B 1 243 ? -4.754  11.808  14.843  1.00 8.35   ?  466  GLN B H    1 
ATOM   9082  H  HA   . GLN B 1 243 ? -6.245  9.679   14.484  1.00 8.58   ?  466  GLN B HA   1 
ATOM   9083  H  HB2  . GLN B 1 243 ? -4.966  10.626  16.815  1.00 9.03   ?  466  GLN B HB2  1 
ATOM   9084  H  HB3  . GLN B 1 243 ? -5.756  9.247   16.795  1.00 9.03   ?  466  GLN B HB3  1 
ATOM   9085  H  HG2  . GLN B 1 243 ? -4.235  8.406   15.272  1.00 9.35   ?  466  GLN B HG2  1 
ATOM   9086  H  HG3  . GLN B 1 243 ? -3.439  9.781   15.315  1.00 9.35   ?  466  GLN B HG3  1 
ATOM   9087  H  HE21 . GLN B 1 243 ? -2.069  10.201  16.982  1.00 11.70  ?  466  GLN B HE21 1 
ATOM   9088  H  HE22 . GLN B 1 243 ? -1.756  9.241   18.077  1.00 11.70  ?  466  GLN B HE22 1 
ATOM   9089  N  N    . GLU B 1 244 ? -7.474  11.984  16.358  1.00 8.41   ?  467  GLU B N    1 
ATOM   9090  C  CA   . GLU B 1 244 ? -8.684  12.374  17.068  1.00 9.40   ?  467  GLU B CA   1 
ATOM   9091  C  C    . GLU B 1 244 ? -9.808  12.698  16.096  1.00 9.46   ?  467  GLU B C    1 
ATOM   9092  O  O    . GLU B 1 244 ? -10.975 12.416  16.373  1.00 10.23  ?  467  GLU B O    1 
ATOM   9093  C  CB   . GLU B 1 244 ? -8.410  13.595  17.956  1.00 10.43  ?  467  GLU B CB   1 
ATOM   9094  C  CG   . GLU B 1 244 ? -7.541  13.300  19.174  1.00 13.57  ?  467  GLU B CG   1 
ATOM   9095  C  CD   . GLU B 1 244 ? -8.293  12.593  20.274  1.00 18.26  ?  467  GLU B CD   1 
ATOM   9096  O  OE1  . GLU B 1 244 ? -9.450  12.962  20.537  1.00 20.03  ?  467  GLU B OE1  1 
ATOM   9097  O  OE2  . GLU B 1 244 ? -7.718  11.675  20.885  1.00 22.09  -1 467  GLU B OE2  1 
ATOM   9098  H  H    . GLU B 1 244 ? -6.829  12.552  16.395  1.00 10.09  ?  467  GLU B H    1 
ATOM   9099  H  HA   . GLU B 1 244 ? -8.959  11.636  17.634  1.00 11.29  ?  467  GLU B HA   1 
ATOM   9100  H  HB2  . GLU B 1 244 ? -7.955  14.267  17.426  1.00 12.52  ?  467  GLU B HB2  1 
ATOM   9101  H  HB3  . GLU B 1 244 ? -9.257  13.942  18.276  1.00 12.52  ?  467  GLU B HB3  1 
ATOM   9102  H  HG2  . GLU B 1 244 ? -6.802  12.733  18.904  1.00 16.29  ?  467  GLU B HG2  1 
ATOM   9103  H  HG3  . GLU B 1 244 ? -7.204  14.137  19.531  1.00 16.29  ?  467  GLU B HG3  1 
ATOM   9104  N  N    . SER B 1 245 ? -9.480  13.326  14.980  1.00 11.32  ?  468  SER B N    1 
ATOM   9105  C  CA   A SER B 1 245 ? -10.478 13.745  14.002  0.25 12.47  ?  468  SER B CA   1 
ATOM   9106  C  CA   B SER B 1 245 ? -10.465 13.782  14.001  0.75 13.24  ?  468  SER B CA   1 
ATOM   9107  C  C    . SER B 1 245 ? -11.677 14.401  14.686  1.00 11.95  ?  468  SER B C    1 
ATOM   9108  O  O    . SER B 1 245 ? -12.836 14.107  14.384  1.00 12.84  ?  468  SER B O    1 
ATOM   9109  C  CB   A SER B 1 245 ? -10.911 12.559  13.137  0.25 13.95  ?  468  SER B CB   1 
ATOM   9110  C  CB   B SER B 1 245 ? -10.856 12.661  13.047  0.75 16.09  ?  468  SER B CB   1 
ATOM   9111  O  OG   A SER B 1 245 ? -11.770 12.958  12.085  0.25 15.04  ?  468  SER B OG   1 
ATOM   9112  O  OG   B SER B 1 245 ? -9.735  12.262  12.277  0.75 18.07  ?  468  SER B OG   1 
ATOM   9113  H  H    A SER B 1 245 ? -8.673  13.525  14.760  0.25 13.58  ?  468  SER B H    1 
ATOM   9114  H  H    B SER B 1 245 ? -8.670  13.507  14.756  0.75 13.58  ?  468  SER B H    1 
ATOM   9115  H  HA   A SER B 1 245 ? -10.080 14.412  13.421  0.25 14.96  ?  468  SER B HA   1 
ATOM   9116  H  HA   B SER B 1 245 ? -10.058 14.481  13.466  0.75 15.90  ?  468  SER B HA   1 
ATOM   9117  H  HB2  A SER B 1 245 ? -10.120 12.147  12.755  0.25 16.74  ?  468  SER B HB2  1 
ATOM   9118  H  HB2  B SER B 1 245 ? -11.176 11.903  13.560  0.75 19.31  ?  468  SER B HB2  1 
ATOM   9119  H  HB3  A SER B 1 245 ? -11.380 11.921  13.697  0.25 16.74  ?  468  SER B HB3  1 
ATOM   9120  H  HB3  B SER B 1 245 ? -11.553 12.978  12.452  0.75 19.31  ?  468  SER B HB3  1 
ATOM   9121  H  HG   A SER B 1 245 ? -12.464 13.311  12.398  0.25 18.05  ?  468  SER B HG   1 
ATOM   9122  H  HG   B SER B 1 245 ? -9.138  11.951  12.780  0.75 21.68  ?  468  SER B HG   1 
ATOM   9123  N  N    . ALA B 1 246 ? -11.394 15.292  15.621  1.00 11.71  ?  469  ALA B N    1 
ATOM   9124  C  CA   . ALA B 1 246 ? -12.455 15.935  16.387  1.00 11.36  ?  469  ALA B CA   1 
ATOM   9125  C  C    . ALA B 1 246 ? -13.167 16.988  15.549  1.00 11.59  ?  469  ALA B C    1 
ATOM   9126  O  O    . ALA B 1 246 ? -12.505 17.790  14.883  1.00 13.41  ?  469  ALA B O    1 
ATOM   9127  C  CB   . ALA B 1 246 ? -11.875 16.566  17.647  1.00 14.38  ?  469  ALA B CB   1 
ATOM   9128  H  H    . ALA B 1 246 ? -10.600 15.543  15.833  1.00 14.05  ?  469  ALA B H    1 
ATOM   9129  H  HA   . ALA B 1 246 ? -13.116 15.273  16.645  1.00 13.64  ?  469  ALA B HA   1 
ATOM   9130  H  HB1  . ALA B 1 246 ? -12.590 16.992  18.146  1.00 17.26  ?  469  ALA B HB1  1 
ATOM   9131  H  HB2  . ALA B 1 246 ? -11.462 15.874  18.186  1.00 17.26  ?  469  ALA B HB2  1 
ATOM   9132  H  HB3  . ALA B 1 246 ? -11.211 17.227  17.392  1.00 17.26  ?  469  ALA B HB3  1 
ATOM   9133  N  N    . PRO B 1 247 ? -14.500 17.029  15.560  1.00 10.48  ?  470  PRO B N    1 
ATOM   9134  C  CA   A PRO B 1 247 ? -15.216 18.042  14.776  0.64 10.85  ?  470  PRO B CA   1 
ATOM   9135  C  CA   B PRO B 1 247 ? -15.214 18.040  14.773  0.36 10.80  ?  470  PRO B CA   1 
ATOM   9136  C  C    . PRO B 1 247 ? -14.857 19.445  15.235  1.00 11.35  ?  470  PRO B C    1 
ATOM   9137  O  O    . PRO B 1 247 ? -14.776 19.724  16.429  1.00 12.41  ?  470  PRO B O    1 
ATOM   9138  C  CB   A PRO B 1 247 ? -16.688 17.709  15.048  0.64 12.51  ?  470  PRO B CB   1 
ATOM   9139  C  CB   B PRO B 1 247 ? -16.688 17.717  15.048  0.36 11.57  ?  470  PRO B CB   1 
ATOM   9140  C  CG   A PRO B 1 247 ? -16.666 16.240  15.356  0.64 12.67  ?  470  PRO B CG   1 
ATOM   9141  C  CG   B PRO B 1 247 ? -16.676 17.099  16.399  0.36 11.43  ?  470  PRO B CG   1 
ATOM   9142  C  CD   A PRO B 1 247 ? -15.418 16.034  16.142  0.64 12.30  ?  470  PRO B CD   1 
ATOM   9143  C  CD   B PRO B 1 247 ? -15.403 16.301  16.470  0.36 11.22  ?  470  PRO B CD   1 
ATOM   9144  H  HA   A PRO B 1 247 ? -15.028 17.952  13.829  0.64 13.02  ?  470  PRO B HA   1 
ATOM   9145  H  HA   B PRO B 1 247 ? -15.024 17.946  13.827  0.36 12.96  ?  470  PRO B HA   1 
ATOM   9146  H  HB2  A PRO B 1 247 ? -17.015 18.223  15.803  0.64 15.01  ?  470  PRO B HB2  1 
ATOM   9147  H  HB2  B PRO B 1 247 ? -17.215 18.531  15.039  0.36 13.88  ?  470  PRO B HB2  1 
ATOM   9148  H  HB3  A PRO B 1 247 ? -17.226 17.896  14.262  0.64 15.01  ?  470  PRO B HB3  1 
ATOM   9149  H  HB3  B PRO B 1 247 ? -17.023 17.097  14.382  0.36 13.88  ?  470  PRO B HB3  1 
ATOM   9150  H  HG2  A PRO B 1 247 ? -17.448 15.998  15.877  0.64 15.21  ?  470  PRO B HG2  1 
ATOM   9151  H  HG2  B PRO B 1 247 ? -16.685 17.793  17.077  0.36 13.72  ?  470  PRO B HG2  1 
ATOM   9152  H  HG3  A PRO B 1 247 ? -16.645 15.728  14.532  0.64 15.21  ?  470  PRO B HG3  1 
ATOM   9153  H  HG3  B PRO B 1 247 ? -17.450 16.524  16.503  0.36 13.72  ?  470  PRO B HG3  1 
ATOM   9154  H  HD2  A PRO B 1 247 ? -15.569 16.210  17.084  0.64 14.77  ?  470  PRO B HD2  1 
ATOM   9155  H  HD2  B PRO B 1 247 ? -15.051 16.292  17.373  0.36 13.47  ?  470  PRO B HD2  1 
ATOM   9156  H  HD3  A PRO B 1 247 ? -15.077 15.134  16.022  0.64 14.77  ?  470  PRO B HD3  1 
ATOM   9157  H  HD3  B PRO B 1 247 ? -15.547 15.393  16.160  0.36 13.47  ?  470  PRO B HD3  1 
ATOM   9158  N  N    . ALA B 1 248 ? -14.641 20.334  14.262  1.00 10.62  ?  471  ALA B N    1 
ATOM   9159  C  CA   . ALA B 1 248 ? -14.373 21.738  14.542  1.00 10.92  ?  471  ALA B CA   1 
ATOM   9160  C  C    . ALA B 1 248 ? -15.709 22.435  14.729  1.00 10.12  ?  471  ALA B C    1 
ATOM   9161  O  O    . ALA B 1 248 ? -16.432 22.677  13.755  1.00 11.96  ?  471  ALA B O    1 
ATOM   9162  C  CB   . ALA B 1 248 ? -13.614 22.371  13.385  1.00 12.93  ?  471  ALA B CB   1 
ATOM   9163  H  H    . ALA B 1 248 ? -14.644 20.143  13.424  1.00 12.74  ?  471  ALA B H    1 
ATOM   9164  H  HA   . ALA B 1 248 ? -13.840 21.818  15.348  1.00 13.11  ?  471  ALA B HA   1 
ATOM   9165  H  HB1  . ALA B 1 248 ? -13.429 23.299  13.599  1.00 15.51  ?  471  ALA B HB1  1 
ATOM   9166  H  HB2  . ALA B 1 248 ? -12.783 21.890  13.252  1.00 15.51  ?  471  ALA B HB2  1 
ATOM   9167  H  HB3  . ALA B 1 248 ? -14.159 22.319  12.584  1.00 15.51  ?  471  ALA B HB3  1 
ATOM   9168  N  N    . GLN B 1 249 ? -16.059 22.752  15.972  1.00 9.50   ?  472  GLN B N    1 
ATOM   9169  C  CA   A GLN B 1 249 ? -17.371 23.343  16.218  0.34 8.96   ?  472  GLN B CA   1 
ATOM   9170  C  CA   B GLN B 1 249 ? -17.364 23.360  16.249  0.66 9.89   ?  472  GLN B CA   1 
ATOM   9171  C  C    . GLN B 1 249 ? -17.502 24.701  15.542  1.00 8.70   ?  472  GLN B C    1 
ATOM   9172  O  O    . GLN B 1 249 ? -18.581 25.051  15.048  1.00 8.97   ?  472  GLN B O    1 
ATOM   9173  C  CB   A GLN B 1 249 ? -17.646 23.426  17.715  0.34 8.61   ?  472  GLN B CB   1 
ATOM   9174  C  CB   B GLN B 1 249 ? -17.546 23.505  17.763  0.66 11.58  ?  472  GLN B CB   1 
ATOM   9175  C  CG   A GLN B 1 249 ? -17.902 22.064  18.358  0.34 8.58   ?  472  GLN B CG   1 
ATOM   9176  C  CG   B GLN B 1 249 ? -18.857 24.114  18.246  0.66 13.52  ?  472  GLN B CG   1 
ATOM   9177  C  CD   A GLN B 1 249 ? -19.203 21.431  17.867  0.34 9.32   ?  472  GLN B CD   1 
ATOM   9178  C  CD   B GLN B 1 249 ? -19.951 23.089  18.479  0.66 13.95  ?  472  GLN B CD   1 
ATOM   9179  O  OE1  A GLN B 1 249 ? -20.096 22.124  17.379  0.34 9.35   ?  472  GLN B OE1  1 
ATOM   9180  O  OE1  B GLN B 1 249 ? -19.733 21.876  18.328  0.66 16.42  ?  472  GLN B OE1  1 
ATOM   9181  N  NE2  A GLN B 1 249 ? -19.311 20.111  17.984  0.34 11.32  ?  472  GLN B NE2  1 
ATOM   9182  N  NE2  B GLN B 1 249 ? -21.141 23.571  18.853  0.66 9.90   ?  472  GLN B NE2  1 
ATOM   9183  H  H    A GLN B 1 249 ? -15.571 22.639  16.671  0.34 11.41  ?  472  GLN B H    1 
ATOM   9184  H  H    B GLN B 1 249 ? -15.568 22.629  16.668  0.66 11.41  ?  472  GLN B H    1 
ATOM   9185  H  HA   A GLN B 1 249 ? -18.052 22.767  15.839  0.34 10.75  ?  472  GLN B HA   1 
ATOM   9186  H  HA   B GLN B 1 249 ? -18.070 22.783  15.918  0.66 11.87  ?  472  GLN B HA   1 
ATOM   9187  H  HB2  A GLN B 1 249 ? -16.877 23.823  18.154  0.34 10.34  ?  472  GLN B HB2  1 
ATOM   9188  H  HB2  B GLN B 1 249 ? -17.483 22.621  18.158  0.66 13.90  ?  472  GLN B HB2  1 
ATOM   9189  H  HB3  A GLN B 1 249 ? -18.431 23.976  17.860  0.34 10.34  ?  472  GLN B HB3  1 
ATOM   9190  H  HB3  B GLN B 1 249 ? -16.832 24.070  18.097  0.66 13.90  ?  472  GLN B HB3  1 
ATOM   9191  H  HG2  A GLN B 1 249 ? -17.172 21.465  18.136  0.34 10.30  ?  472  GLN B HG2  1 
ATOM   9192  H  HG2  B GLN B 1 249 ? -18.698 24.574  19.085  0.66 16.23  ?  472  GLN B HG2  1 
ATOM   9193  H  HG3  A GLN B 1 249 ? -17.962 22.172  19.320  0.34 10.30  ?  472  GLN B HG3  1 
ATOM   9194  H  HG3  B GLN B 1 249 ? -19.175 24.742  17.579  0.66 16.23  ?  472  GLN B HG3  1 
ATOM   9195  H  HE21 A GLN B 1 249 ? -18.666 19.655  18.323  0.34 13.59  ?  472  GLN B HE21 1 
ATOM   9196  H  HE21 B GLN B 1 249 ? -21.252 24.418  18.949  0.66 11.88  ?  472  GLN B HE21 1 
ATOM   9197  H  HE22 A GLN B 1 249 ? -20.027 19.713  17.720  0.34 13.59  ?  472  GLN B HE22 1 
ATOM   9198  H  HE22 B GLN B 1 249 ? -21.796 23.033  18.998  0.66 11.88  ?  472  GLN B HE22 1 
ATOM   9199  N  N    . THR B 1 250 ? -16.418 25.478  15.509  1.00 8.67   ?  473  THR B N    1 
ATOM   9200  C  CA   . THR B 1 250 ? -16.295 26.693  14.723  1.00 7.98   ?  473  THR B CA   1 
ATOM   9201  C  C    . THR B 1 250 ? -14.955 26.597  14.006  1.00 7.26   ?  473  THR B C    1 
ATOM   9202  O  O    . THR B 1 250 ? -14.220 25.619  14.156  1.00 8.36   ?  473  THR B O    1 
ATOM   9203  C  CB   . THR B 1 250 ? -16.321 27.962  15.575  1.00 7.94   ?  473  THR B CB   1 
ATOM   9204  O  OG1  . THR B 1 250 ? -15.129 27.992  16.362  1.00 8.06   ?  473  THR B OG1  1 
ATOM   9205  C  CG2  . THR B 1 250 ? -17.552 28.022  16.479  1.00 8.99   ?  473  THR B CG2  1 
ATOM   9206  H  H    . THR B 1 250 ? -15.706 25.307  15.959  1.00 10.41  ?  473  THR B H    1 
ATOM   9207  H  HA   . THR B 1 250 ? -17.038 26.749  14.103  1.00 9.58   ?  473  THR B HA   1 
ATOM   9208  H  HB   . THR B 1 250 ? -16.369 28.742  15.001  1.00 9.53   ?  473  THR B HB   1 
ATOM   9209  H  HG1  . THR B 1 250 ? -15.107 28.694  16.824  1.00 9.68   ?  473  THR B HG1  1 
ATOM   9210  H  HG21 . THR B 1 250 ? -17.549 28.846  16.990  1.00 10.79  ?  473  THR B HG21 1 
ATOM   9211  H  HG22 . THR B 1 250 ? -18.360 27.988  15.942  1.00 10.79  ?  473  THR B HG22 1 
ATOM   9212  H  HG23 . THR B 1 250 ? -17.550 27.271  17.092  1.00 10.79  ?  473  THR B HG23 1 
ATOM   9213  N  N    . ASP B 1 251 ? -14.612 27.632  13.257  1.00 7.27   ?  474  ASP B N    1 
ATOM   9214  C  CA   . ASP B 1 251 ? -13.356 27.618  12.525  1.00 7.62   ?  474  ASP B CA   1 
ATOM   9215  C  C    . ASP B 1 251 ? -12.172 28.179  13.316  1.00 6.77   ?  474  ASP B C    1 
ATOM   9216  O  O    . ASP B 1 251 ? -11.076 28.257  12.766  1.00 6.78   ?  474  ASP B O    1 
ATOM   9217  C  CB   . ASP B 1 251 ? -13.495 28.335  11.184  1.00 8.85   ?  474  ASP B CB   1 
ATOM   9218  C  CG   . ASP B 1 251 ? -14.371 27.565  10.194  1.00 11.94  ?  474  ASP B CG   1 
ATOM   9219  O  OD1  . ASP B 1 251 ? -14.658 26.366  10.417  1.00 13.00  -1 474  ASP B OD1  1 
ATOM   9220  O  OD2  . ASP B 1 251 ? -14.793 28.179  9.191   1.00 14.88  ?  474  ASP B OD2  1 
ATOM   9221  H  H    . ASP B 1 251 ? -15.083 28.345  13.157  1.00 8.73   ?  474  ASP B H    1 
ATOM   9222  H  HA   . ASP B 1 251 ? -13.142 26.693  12.326  1.00 9.14   ?  474  ASP B HA   1 
ATOM   9223  H  HB2  . ASP B 1 251 ? -13.899 29.204  11.330  1.00 10.62  ?  474  ASP B HB2  1 
ATOM   9224  H  HB3  . ASP B 1 251 ? -12.616 28.440  10.788  1.00 10.62  ?  474  ASP B HB3  1 
ATOM   9225  N  N    . VAL B 1 252 ? -12.366 28.579  14.571  1.00 6.69   ?  475  VAL B N    1 
ATOM   9226  C  CA   . VAL B 1 252 ? -11.289 29.135  15.385  1.00 6.92   ?  475  VAL B CA   1 
ATOM   9227  C  C    . VAL B 1 252 ? -11.428 28.608  16.804  1.00 6.67   ?  475  VAL B C    1 
ATOM   9228  O  O    . VAL B 1 252 ? -12.459 28.829  17.450  1.00 8.09   ?  475  VAL B O    1 
ATOM   9229  C  CB   . VAL B 1 252 ? -11.286 30.676  15.416  1.00 8.01   ?  475  VAL B CB   1 
ATOM   9230  C  CG1  . VAL B 1 252 ? -10.100 31.176  16.234  1.00 9.26   ?  475  VAL B CG1  1 
ATOM   9231  C  CG2  . VAL B 1 252 ? -11.271 31.253  14.005  1.00 8.50   ?  475  VAL B CG2  1 
ATOM   9232  H  H    . VAL B 1 252 ? -13.122 28.538  14.978  1.00 8.03   ?  475  VAL B H    1 
ATOM   9233  H  HA   . VAL B 1 252 ? -10.447 28.827  15.013  1.00 8.31   ?  475  VAL B HA   1 
ATOM   9234  H  HB   . VAL B 1 252 ? -12.100 30.988  15.841  1.00 9.61   ?  475  VAL B HB   1 
ATOM   9235  H  HG11 . VAL B 1 252 ? -9.999  32.131  16.094  1.00 11.12  ?  475  VAL B HG11 1 
ATOM   9236  H  HG12 . VAL B 1 252 ? -10.265 30.995  17.173  1.00 11.12  ?  475  VAL B HG12 1 
ATOM   9237  H  HG13 . VAL B 1 252 ? -9.298  30.713  15.944  1.00 11.12  ?  475  VAL B HG13 1 
ATOM   9238  H  HG21 . VAL B 1 252 ? -11.193 32.219  14.060  1.00 10.20  ?  475  VAL B HG21 1 
ATOM   9239  H  HG22 . VAL B 1 252 ? -10.514 30.887  13.522  1.00 10.20  ?  475  VAL B HG22 1 
ATOM   9240  H  HG23 . VAL B 1 252 ? -12.097 31.013  13.557  1.00 10.20  ?  475  VAL B HG23 1 
ATOM   9241  N  N    . ALA B 1 253 ? -10.374 27.980  17.304  1.00 6.32   ?  476  ALA B N    1 
ATOM   9242  C  CA   . ALA B 1 253 ? -10.282 27.567  18.694  1.00 7.72   ?  476  ALA B CA   1 
ATOM   9243  C  C    . ALA B 1 253 ? -9.453  28.589  19.458  1.00 7.12   ?  476  ALA B C    1 
ATOM   9244  O  O    . ALA B 1 253 ? -8.346  28.939  19.040  1.00 8.46   ?  476  ALA B O    1 
ATOM   9245  C  CB   . ALA B 1 253 ? -9.605  26.201  18.779  1.00 8.80   ?  476  ALA B CB   1 
ATOM   9246  H  H    . ALA B 1 253 ? -9.678  27.776  16.842  1.00 7.58   ?  476  ALA B H    1 
ATOM   9247  H  HA   . ALA B 1 253 ? -11.165 27.516  19.091  1.00 9.27   ?  476  ALA B HA   1 
ATOM   9248  H  HB1  . ALA B 1 253 ? -9.520  25.948  19.711  1.00 10.56  ?  476  ALA B HB1  1 
ATOM   9249  H  HB2  . ALA B 1 253 ? -10.148 25.550  18.307  1.00 10.56  ?  476  ALA B HB2  1 
ATOM   9250  H  HB3  . ALA B 1 253 ? -8.727  26.258  18.370  1.00 10.56  ?  476  ALA B HB3  1 
ATOM   9251  N  N    . LEU B 1 254 ? -9.982  29.060  20.573  1.00 6.77   ?  477  LEU B N    1 
ATOM   9252  C  CA   . LEU B 1 254 ? -9.204  29.884  21.479  1.00 7.19   ?  477  LEU B CA   1 
ATOM   9253  C  C    . LEU B 1 254 ? -8.363  28.953  22.335  1.00 6.93   ?  477  LEU B C    1 
ATOM   9254  O  O    . LEU B 1 254 ? -8.898  28.044  22.978  1.00 8.33   ?  477  LEU B O    1 
ATOM   9255  C  CB   . LEU B 1 254 ? -10.132 30.706  22.377  1.00 7.74   ?  477  LEU B CB   1 
ATOM   9256  C  CG   . LEU B 1 254 ? -9.436  31.647  23.378  1.00 8.93   ?  477  LEU B CG   1 
ATOM   9257  C  CD1  . LEU B 1 254 ? -8.602  32.674  22.633  1.00 9.05   ?  477  LEU B CD1  1 
ATOM   9258  C  CD2  . LEU B 1 254 ? -10.492 32.315  24.255  1.00 9.95   ?  477  LEU B CD2  1 
ATOM   9259  H  H    . LEU B 1 254 ? -10.791 28.917  20.828  1.00 8.13   ?  477  LEU B H    1 
ATOM   9260  H  HA   . LEU B 1 254 ? -8.637  30.493  20.980  1.00 8.63   ?  477  LEU B HA   1 
ATOM   9261  H  HB2  . LEU B 1 254 ? -10.695 31.255  21.809  1.00 9.29   ?  477  LEU B HB2  1 
ATOM   9262  H  HB3  . LEU B 1 254 ? -10.679 30.092  22.891  1.00 9.29   ?  477  LEU B HB3  1 
ATOM   9263  H  HG   . LEU B 1 254 ? -8.835  31.148  23.954  1.00 10.72  ?  477  LEU B HG   1 
ATOM   9264  H  HD11 . LEU B 1 254 ? -8.282  33.338  23.263  1.00 10.86  ?  477  LEU B HD11 1 
ATOM   9265  H  HD12 . LEU B 1 254 ? -7.851  32.226  22.214  1.00 10.86  ?  477  LEU B HD12 1 
ATOM   9266  H  HD13 . LEU B 1 254 ? -9.154  33.098  21.957  1.00 10.86  ?  477  LEU B HD13 1 
ATOM   9267  H  HD21 . LEU B 1 254 ? -10.052 32.906  24.886  1.00 11.94  ?  477  LEU B HD21 1 
ATOM   9268  H  HD22 . LEU B 1 254 ? -11.095 32.825  23.691  1.00 11.94  ?  477  LEU B HD22 1 
ATOM   9269  H  HD23 . LEU B 1 254 ? -10.986 31.630  24.733  1.00 11.94  ?  477  LEU B HD23 1 
ATOM   9270  N  N    . ILE B 1 255 ? -7.049  29.167  22.332  1.00 6.97   ?  478  ILE B N    1 
ATOM   9271  C  CA   . ILE B 1 255 ? -6.109  28.339  23.077  1.00 6.66   ?  478  ILE B CA   1 
ATOM   9272  C  C    . ILE B 1 255 ? -5.301  29.237  23.995  1.00 7.18   ?  478  ILE B C    1 
ATOM   9273  O  O    . ILE B 1 255 ? -5.026  30.401  23.689  1.00 8.01   ?  478  ILE B O    1 
ATOM   9274  C  CB   . ILE B 1 255 ? -5.220  27.491  22.132  1.00 7.27   ?  478  ILE B CB   1 
ATOM   9275  C  CG1  . ILE B 1 255 ? -4.319  28.358  21.251  1.00 7.53   ?  478  ILE B CG1  1 
ATOM   9276  C  CG2  . ILE B 1 255 ? -6.091  26.615  21.246  1.00 8.58   ?  478  ILE B CG2  1 
ATOM   9277  C  CD1  . ILE B 1 255 ? -3.332  27.564  20.431  1.00 7.59   ?  478  ILE B CD1  1 
ATOM   9278  H  H    . ILE B 1 255 ? -6.670  29.803  21.894  1.00 8.37   ?  478  ILE B H    1 
ATOM   9279  H  HA   . ILE B 1 255 ? -6.589  27.715  23.644  1.00 7.99   ?  478  ILE B HA   1 
ATOM   9280  H  HB   . ILE B 1 255 ? -4.651  26.944  22.696  1.00 8.72   ?  478  ILE B HB   1 
ATOM   9281  H  HG12 . ILE B 1 255 ? -4.874  28.864  20.638  1.00 9.03   ?  478  ILE B HG12 1 
ATOM   9282  H  HG13 . ILE B 1 255 ? -3.815  28.962  21.819  1.00 9.03   ?  478  ILE B HG13 1 
ATOM   9283  H  HG21 . ILE B 1 255 ? -5.525  25.993  20.763  1.00 10.29  ?  478  ILE B HG21 1 
ATOM   9284  H  HG22 . ILE B 1 255 ? -6.718  26.127  21.803  1.00 10.29  ?  478  ILE B HG22 1 
ATOM   9285  H  HG23 . ILE B 1 255 ? -6.574  27.178  20.621  1.00 10.29  ?  478  ILE B HG23 1 
ATOM   9286  H  HD11 . ILE B 1 255 ? -2.711  28.175  20.006  1.00 9.11   ?  478  ILE B HD11 1 
ATOM   9287  H  HD12 . ILE B 1 255 ? -2.852  26.957  21.016  1.00 9.11   ?  478  ILE B HD12 1 
ATOM   9288  H  HD13 . ILE B 1 255 ? -3.815  27.061  19.757  1.00 9.11   ?  478  ILE B HD13 1 
ATOM   9289  N  N    . ARG B 1 256 ? -4.924  28.688  25.138  1.00 7.11   ?  479  ARG B N    1 
ATOM   9290  C  CA   . ARG B 1 256 ? -4.139  29.409  26.128  1.00 6.97   ?  479  ARG B CA   1 
ATOM   9291  C  C    . ARG B 1 256 ? -2.864  28.628  26.424  1.00 7.51   ?  479  ARG B C    1 
ATOM   9292  O  O    . ARG B 1 256 ? -2.898  27.406  26.572  1.00 7.82   ?  479  ARG B O    1 
ATOM   9293  C  CB   . ARG B 1 256 ? -4.913  29.605  27.431  1.00 9.44   ?  479  ARG B CB   1 
ATOM   9294  C  CG   . ARG B 1 256 ? -5.671  30.905  27.542  1.00 12.45  ?  479  ARG B CG   1 
ATOM   9295  C  CD   . ARG B 1 256 ? -6.853  30.973  26.617  1.00 14.89  ?  479  ARG B CD   1 
ATOM   9296  N  NE   . ARG B 1 256 ? -7.615  32.207  26.813  1.00 15.73  ?  479  ARG B NE   1 
ATOM   9297  C  CZ   . ARG B 1 256 ? -8.597  32.368  27.690  1.00 18.98  ?  479  ARG B CZ   1 
ATOM   9298  N  NH1  . ARG B 1 256 ? -8.981  31.383  28.489  1.00 21.34  ?  479  ARG B NH1  1 
ATOM   9299  N  NH2  . ARG B 1 256 ? -9.216  33.545  27.759  1.00 19.78  ?  479  ARG B NH2  1 
ATOM   9300  H  H    . ARG B 1 256 ? -5.115  27.882  25.369  1.00 8.53   ?  479  ARG B H    1 
ATOM   9301  H  HA   . ARG B 1 256 ? -3.909  30.283  25.774  1.00 8.36   ?  479  ARG B HA   1 
ATOM   9302  H  HB2  . ARG B 1 256 ? -5.558  28.886  27.515  1.00 11.32  ?  479  ARG B HB2  1 
ATOM   9303  H  HB3  . ARG B 1 256 ? -4.283  29.574  28.168  1.00 11.32  ?  479  ARG B HB3  1 
ATOM   9304  H  HG2  . ARG B 1 256 ? -5.996  31.004  28.451  1.00 14.94  ?  479  ARG B HG2  1 
ATOM   9305  H  HG3  . ARG B 1 256 ? -5.075  31.638  27.321  1.00 14.94  ?  479  ARG B HG3  1 
ATOM   9306  H  HD2  . ARG B 1 256 ? -6.544  30.948  25.698  1.00 17.87  ?  479  ARG B HD2  1 
ATOM   9307  H  HD3  . ARG B 1 256 ? -7.441  30.221  26.790  1.00 17.87  ?  479  ARG B HD3  1 
ATOM   9308  H  HE   . ARG B 1 256 ? -7.410  32.881  26.320  1.00 18.88  ?  479  ARG B HE   1 
ATOM   9309  H  HH11 . ARG B 1 256 ? -8.591  30.617  28.446  1.00 25.61  ?  479  ARG B HH11 1 
ATOM   9310  H  HH12 . ARG B 1 256 ? -9.620  31.509  29.051  1.00 25.61  ?  479  ARG B HH12 1 
ATOM   9311  H  HH21 . ARG B 1 256 ? -8.978  34.187  27.240  1.00 23.74  ?  479  ARG B HH21 1 
ATOM   9312  H  HH22 . ARG B 1 256 ? -9.855  33.662  28.324  1.00 23.74  ?  479  ARG B HH22 1 
ATOM   9313  N  N    . TYR B 1 257 ? -1.738  29.337  26.484  1.00 7.61   ?  480  TYR B N    1 
ATOM   9314  C  CA   . TYR B 1 257 ? -0.478  28.704  26.879  1.00 7.37   ?  480  TYR B CA   1 
ATOM   9315  C  C    . TYR B 1 257 ? -0.428  28.712  28.394  1.00 8.19   ?  480  TYR B C    1 
ATOM   9316  O  O    . TYR B 1 257 ? -0.597  29.774  29.006  1.00 9.92   ?  480  TYR B O    1 
ATOM   9317  C  CB   . TYR B 1 257 ? 0.708   29.505  26.351  1.00 8.23   ?  480  TYR B CB   1 
ATOM   9318  C  CG   . TYR B 1 257 ? 1.957   28.706  26.019  1.00 8.51   ?  480  TYR B CG   1 
ATOM   9319  C  CD1  . TYR B 1 257 ? 1.967   27.835  24.944  1.00 8.85   ?  480  TYR B CD1  1 
ATOM   9320  C  CD2  . TYR B 1 257 ? 3.134   28.867  26.734  1.00 9.78   ?  480  TYR B CD2  1 
ATOM   9321  C  CE1  . TYR B 1 257 ? 3.087   27.126  24.588  1.00 9.60   ?  480  TYR B CE1  1 
ATOM   9322  C  CE2  . TYR B 1 257 ? 4.280   28.139  26.397  1.00 9.94   ?  480  TYR B CE2  1 
ATOM   9323  C  CZ   . TYR B 1 257 ? 4.239   27.283  25.306  1.00 8.93   ?  480  TYR B CZ   1 
ATOM   9324  O  OH   . TYR B 1 257 ? 5.338   26.560  24.903  1.00 10.27  ?  480  TYR B OH   1 
ATOM   9325  H  H    . TYR B 1 257 ? -1.677  30.176  26.304  1.00 9.14   ?  480  TYR B H    1 
ATOM   9326  H  HA   . TYR B 1 257 ? -0.422  27.802  26.526  1.00 8.84   ?  480  TYR B HA   1 
ATOM   9327  H  HB2  . TYR B 1 257 ? 0.431   29.955  25.538  1.00 9.87   ?  480  TYR B HB2  1 
ATOM   9328  H  HB3  . TYR B 1 257 ? 0.956   30.158  27.024  1.00 9.87   ?  480  TYR B HB3  1 
ATOM   9329  H  HD1  . TYR B 1 257 ? 1.189   27.727  24.445  1.00 10.62  ?  480  TYR B HD1  1 
ATOM   9330  H  HD2  . TYR B 1 257 ? 3.162   29.466  27.445  1.00 11.73  ?  480  TYR B HD2  1 
ATOM   9331  H  HE1  . TYR B 1 257 ? 3.062   26.542  23.864  1.00 11.52  ?  480  TYR B HE1  1 
ATOM   9332  H  HE2  . TYR B 1 257 ? 5.059   28.228  26.898  1.00 11.93  ?  480  TYR B HE2  1 
ATOM   9333  H  HH   . TYR B 1 257 ? 5.148   26.103  24.224  1.00 12.33  ?  480  TYR B HH   1 
ATOM   9334  N  N    . VAL B 1 258 ? -0.212  27.549  29.001  1.00 7.77   ?  481  VAL B N    1 
ATOM   9335  C  CA   A VAL B 1 258 ? -0.328  27.405  30.445  0.55 8.59   ?  481  VAL B CA   1 
ATOM   9336  C  CA   B VAL B 1 258 ? -0.334  27.396  30.444  0.45 9.04   ?  481  VAL B CA   1 
ATOM   9337  C  C    . VAL B 1 258 ? 0.949   26.823  31.013  1.00 8.76   ?  481  VAL B C    1 
ATOM   9338  O  O    . VAL B 1 258 ? 1.639   26.017  30.370  1.00 9.15   ?  481  VAL B O    1 
ATOM   9339  C  CB   A VAL B 1 258 ? -1.529  26.519  30.843  0.55 9.57   ?  481  VAL B CB   1 
ATOM   9340  C  CB   B VAL B 1 258 ? -1.545  26.500  30.798  0.45 10.75  ?  481  VAL B CB   1 
ATOM   9341  C  CG1  A VAL B 1 258 ? -2.809  27.052  30.220  0.55 9.42   ?  481  VAL B CG1  1 
ATOM   9342  C  CG1  B VAL B 1 258 ? -1.335  25.078  30.319  0.45 11.92  ?  481  VAL B CG1  1 
ATOM   9343  C  CG2  A VAL B 1 258 ? -1.305  25.080  30.446  0.55 11.20  ?  481  VAL B CG2  1 
ATOM   9344  C  CG2  B VAL B 1 258 ? -1.830  26.530  32.294  0.45 11.72  ?  481  VAL B CG2  1 
ATOM   9345  H  H    A VAL B 1 258 ? 0.005   26.824  28.593  0.55 9.32   ?  481  VAL B H    1 
ATOM   9346  H  H    B VAL B 1 258 ? 0.009   26.826  28.592  0.45 9.32   ?  481  VAL B H    1 
ATOM   9347  H  HA   A VAL B 1 258 ? -0.447  28.289  30.824  0.55 10.31  ?  481  VAL B HA   1 
ATOM   9348  H  HA   B VAL B 1 258 ? -0.454  28.269  30.850  0.45 10.86  ?  481  VAL B HA   1 
ATOM   9349  H  HB   A VAL B 1 258 ? -1.622  26.546  31.808  0.55 11.48  ?  481  VAL B HB   1 
ATOM   9350  H  HB   B VAL B 1 258 ? -2.323  26.854  30.340  0.45 12.90  ?  481  VAL B HB   1 
ATOM   9351  H  HG11 A VAL B 1 258 ? -3.566  26.579  30.601  0.55 11.31  ?  481  VAL B HG11 1 
ATOM   9352  H  HG11 B VAL B 1 258 ? -2.160  24.581  30.436  0.45 14.30  ?  481  VAL B HG11 1 
ATOM   9353  H  HG12 A VAL B 1 258 ? -2.881  28.000  30.410  0.55 11.31  ?  481  VAL B HG12 1 
ATOM   9354  H  HG12 B VAL B 1 258 ? -1.089  25.095  29.381  0.45 14.30  ?  481  VAL B HG12 1 
ATOM   9355  H  HG13 A VAL B 1 258 ? -2.777  26.907  29.261  0.55 11.31  ?  481  VAL B HG13 1 
ATOM   9356  H  HG13 B VAL B 1 258 ? -0.626  24.671  30.840  0.45 14.30  ?  481  VAL B HG13 1 
ATOM   9357  H  HG21 A VAL B 1 258 ? -2.149  24.604  30.493  0.55 13.44  ?  481  VAL B HG21 1 
ATOM   9358  H  HG21 B VAL B 1 258 ? -2.656  26.051  32.468  0.45 14.07  ?  481  VAL B HG21 1 
ATOM   9359  H  HG22 A VAL B 1 258 ? -0.959  25.052  29.540  0.55 13.44  ?  481  VAL B HG22 1 
ATOM   9360  H  HG22 B VAL B 1 258 ? -1.096  26.105  32.764  0.45 14.07  ?  481  VAL B HG22 1 
ATOM   9361  H  HG23 A VAL B 1 258 ? -0.665  24.680  31.056  0.55 13.44  ?  481  VAL B HG23 1 
ATOM   9362  H  HG23 B VAL B 1 258 ? -1.917  27.453  32.580  0.45 14.07  ?  481  VAL B HG23 1 
ATOM   9363  N  N    . ASN B 1 259 ? 1.251   27.234  32.242  1.00 9.18   ?  482  ASN B N    1 
ATOM   9364  C  CA   . ASN B 1 259 ? 2.298   26.632  33.049  1.00 9.92   ?  482  ASN B CA   1 
ATOM   9365  C  C    . ASN B 1 259 ? 1.607   25.626  33.960  1.00 10.04  ?  482  ASN B C    1 
ATOM   9366  O  O    . ASN B 1 259 ? 0.852   26.033  34.852  1.00 10.75  ?  482  ASN B O    1 
ATOM   9367  C  CB   . ASN B 1 259 ? 2.991   27.712  33.875  1.00 9.33   ?  482  ASN B CB   1 
ATOM   9368  C  CG   . ASN B 1 259 ? 4.098   27.158  34.764  1.00 10.28  ?  482  ASN B CG   1 
ATOM   9369  O  OD1  . ASN B 1 259 ? 3.987   26.054  35.297  1.00 10.37  ?  482  ASN B OD1  1 
ATOM   9370  N  ND2  . ASN B 1 259 ? 5.170   27.935  34.937  1.00 10.54  ?  482  ASN B ND2  1 
ATOM   9371  H  H    . ASN B 1 259 ? 0.849   27.881  32.641  1.00 11.01  ?  482  ASN B H    1 
ATOM   9372  H  HA   . ASN B 1 259 ? 2.966   26.188  32.504  1.00 11.91  ?  482  ASN B HA   1 
ATOM   9373  H  HB2  . ASN B 1 259 ? 3.386   28.364  33.275  1.00 11.20  ?  482  ASN B HB2  1 
ATOM   9374  H  HB3  . ASN B 1 259 ? 2.335   28.141  34.447  1.00 11.20  ?  482  ASN B HB3  1 
ATOM   9375  H  HD21 . ASN B 1 259 ? 5.821   27.665  35.430  1.00 12.64  ?  482  ASN B HD21 1 
ATOM   9376  H  HD22 . ASN B 1 259 ? 5.209   28.704  34.555  1.00 12.64  ?  482  ASN B HD22 1 
ATOM   9377  N  N    . PRO B 1 260 ? 1.796   24.320  33.761  1.00 10.42  ?  483  PRO B N    1 
ATOM   9378  C  CA   . PRO B 1 260 ? 1.069   23.337  34.583  1.00 11.74  ?  483  PRO B CA   1 
ATOM   9379  C  C    . PRO B 1 260 ? 1.523   23.299  36.024  1.00 12.88  ?  483  PRO B C    1 
ATOM   9380  O  O    . PRO B 1 260 ? 0.758   22.838  36.877  1.00 15.24  ?  483  PRO B O    1 
ATOM   9381  C  CB   . PRO B 1 260 ? 1.357   22.006  33.875  1.00 12.97  ?  483  PRO B CB   1 
ATOM   9382  C  CG   . PRO B 1 260 ? 2.689   22.221  33.232  1.00 12.16  ?  483  PRO B CG   1 
ATOM   9383  C  CD   . PRO B 1 260 ? 2.667   23.665  32.772  1.00 10.62  ?  483  PRO B CD   1 
ATOM   9384  H  HA   . PRO B 1 260 ? 0.116   23.519  34.553  1.00 14.09  ?  483  PRO B HA   1 
ATOM   9385  H  HB2  . PRO B 1 260 ? 1.393   21.284  34.523  1.00 15.57  ?  483  PRO B HB2  1 
ATOM   9386  H  HB3  . PRO B 1 260 ? 0.673   21.824  33.213  1.00 15.57  ?  483  PRO B HB3  1 
ATOM   9387  H  HG2  . PRO B 1 260 ? 3.397   22.074  33.879  1.00 14.60  ?  483  PRO B HG2  1 
ATOM   9388  H  HG3  . PRO B 1 260 ? 2.796   21.618  32.480  1.00 14.60  ?  483  PRO B HG3  1 
ATOM   9389  H  HD2  . PRO B 1 260 ? 3.558   24.047  32.789  1.00 12.75  ?  483  PRO B HD2  1 
ATOM   9390  H  HD3  . PRO B 1 260 ? 2.292   23.737  31.880  1.00 12.75  ?  483  PRO B HD3  1 
ATOM   9391  N  N    . GLU B 1 261 ? 2.744   23.740  36.325  0.83 11.53  ?  484  GLU B N    1 
ATOM   9392  C  CA   . GLU B 1 261 ? 3.215   23.723  37.708  0.83 12.46  ?  484  GLU B CA   1 
ATOM   9393  C  C    . GLU B 1 261 ? 2.564   24.831  38.533  0.83 12.31  ?  484  GLU B C    1 
ATOM   9394  O  O    . GLU B 1 261 ? 2.130   24.603  39.665  0.83 14.69  ?  484  GLU B O    1 
ATOM   9395  C  CB   . GLU B 1 261 ? 4.738   23.844  37.740  0.83 14.58  ?  484  GLU B CB   1 
ATOM   9396  C  CG   . GLU B 1 261 ? 5.336   23.761  39.142  0.83 17.99  ?  484  GLU B CG   1 
ATOM   9397  C  CD   . GLU B 1 261 ? 6.849   23.655  39.134  0.83 21.67  ?  484  GLU B CD   1 
ATOM   9398  O  OE1  . GLU B 1 261 ? 7.499   24.295  38.283  0.83 22.91  ?  484  GLU B OE1  1 
ATOM   9399  O  OE2  . GLU B 1 261 ? 7.390   22.925  39.989  0.83 23.99  -1 484  GLU B OE2  1 
ATOM   9400  H  H    . GLU B 1 261 ? 3.311   24.050  35.757  0.83 13.84  ?  484  GLU B H    1 
ATOM   9401  H  HA   . GLU B 1 261 ? 2.971   22.875  38.110  0.83 14.96  ?  484  GLU B HA   1 
ATOM   9402  H  HB2  . GLU B 1 261 ? 5.119   23.123  37.214  0.83 17.50  ?  484  GLU B HB2  1 
ATOM   9403  H  HB3  . GLU B 1 261 ? 4.991   24.700  37.362  0.83 17.50  ?  484  GLU B HB3  1 
ATOM   9404  H  HG2  . GLU B 1 261 ? 5.095   24.560  39.636  0.83 21.59  ?  484  GLU B HG2  1 
ATOM   9405  H  HG3  . GLU B 1 261 ? 4.984   22.975  39.590  0.83 21.59  ?  484  GLU B HG3  1 
ATOM   9406  N  N    . THR B 1 262 ? 2.504   26.049  37.995  1.00 12.41  ?  485  THR B N    1 
ATOM   9407  C  CA   . THR B 1 262 ? 1.842   27.141  38.699  1.00 12.86  ?  485  THR B CA   1 
ATOM   9408  C  C    . THR B 1 262 ? 0.341   27.160  38.447  1.00 13.28  ?  485  THR B C    1 
ATOM   9409  O  O    . THR B 1 262 ? -0.398  27.788  39.216  1.00 15.18  ?  485  THR B O    1 
ATOM   9410  C  CB   . THR B 1 262 ? 2.427   28.487  38.264  1.00 12.51  ?  485  THR B CB   1 
ATOM   9411  O  OG1  . THR B 1 262 ? 2.086   28.702  36.893  1.00 11.83  ?  485  THR B OG1  1 
ATOM   9412  C  CG2  . THR B 1 262 ? 3.953   28.528  38.433  1.00 13.48  ?  485  THR B CG2  1 
ATOM   9413  H  H    . THR B 1 262 ? 2.837   26.265  37.232  1.00 14.90  ?  485  THR B H    1 
ATOM   9414  H  HA   . THR B 1 262 ? 1.999   27.041  39.651  1.00 15.43  ?  485  THR B HA   1 
ATOM   9415  H  HB   . THR B 1 262 ? 2.065   29.194  38.820  1.00 15.01  ?  485  THR B HB   1 
ATOM   9416  H  HG1  . THR B 1 262 ? 2.412   29.429  36.627  1.00 14.20  ?  485  THR B HG1  1 
ATOM   9417  H  HG21 . THR B 1 262 ? 4.289   29.409  38.203  1.00 16.17  ?  485  THR B HG21 1 
ATOM   9418  H  HG22 . THR B 1 262 ? 4.190   28.332  39.353  1.00 16.17  ?  485  THR B HG22 1 
ATOM   9419  H  HG23 . THR B 1 262 ? 4.369   27.871  37.854  1.00 16.17  ?  485  THR B HG23 1 
ATOM   9420  N  N    . GLY B 1 263 ? -0.117  26.509  37.373  1.00 13.06  ?  486  GLY B N    1 
ATOM   9421  C  CA   . GLY B 1 263 ? -1.504  26.551  36.968  1.00 12.97  ?  486  GLY B CA   1 
ATOM   9422  C  C    . GLY B 1 263 ? -1.928  27.807  36.233  1.00 12.66  ?  486  GLY B C    1 
ATOM   9423  O  O    . GLY B 1 263 ? -3.108  27.933  35.879  1.00 15.81  ?  486  GLY B O    1 
ATOM   9424  H  H    . GLY B 1 263 ? 0.376   26.028  36.857  1.00 15.67  ?  486  GLY B H    1 
ATOM   9425  H  HA2  . GLY B 1 263 ? -1.679  25.796  36.385  1.00 15.56  ?  486  GLY B HA2  1 
ATOM   9426  H  HA3  . GLY B 1 263 ? -2.059  26.473  37.760  1.00 15.56  ?  486  GLY B HA3  1 
ATOM   9427  N  N    . ARG B 1 264 ? -1.023  28.745  36.001  1.00 11.45  ?  487  ARG B N    1 
ATOM   9428  C  CA   . ARG B 1 264 ? -1.407  30.033  35.440  1.00 10.66  ?  487  ARG B CA   1 
ATOM   9429  C  C    . ARG B 1 264 ? -1.330  30.037  33.916  1.00 10.15  ?  487  ARG B C    1 
ATOM   9430  O  O    . ARG B 1 264 ? -0.462  29.414  33.304  1.00 10.52  ?  487  ARG B O    1 
ATOM   9431  C  CB   . ARG B 1 264 ? -0.532  31.147  36.016  1.00 11.02  ?  487  ARG B CB   1 
ATOM   9432  C  CG   . ARG B 1 264 ? -0.793  31.400  37.488  1.00 12.09  ?  487  ARG B CG   1 
ATOM   9433  C  CD   . ARG B 1 264 ? -0.132  32.689  37.986  1.00 13.55  ?  487  ARG B CD   1 
ATOM   9434  N  NE   . ARG B 1 264 ? 1.320   32.603  38.042  1.00 13.12  ?  487  ARG B NE   1 
ATOM   9435  C  CZ   . ARG B 1 264 ? 1.997   32.054  39.041  1.00 13.10  ?  487  ARG B CZ   1 
ATOM   9436  N  NH1  . ARG B 1 264 ? 1.377   31.521  40.080  1.00 14.29  ?  487  ARG B NH1  1 
ATOM   9437  N  NH2  . ARG B 1 264 ? 3.324   32.036  38.995  1.00 13.21  ?  487  ARG B NH2  1 
ATOM   9438  H  H    . ARG B 1 264 ? -0.182  28.662  36.159  1.00 13.74  ?  487  ARG B H    1 
ATOM   9439  H  HA   . ARG B 1 264 ? -2.331  30.211  35.675  1.00 12.80  ?  487  ARG B HA   1 
ATOM   9440  H  HB2  . ARG B 1 264 ? 0.400   30.899  35.915  1.00 13.22  ?  487  ARG B HB2  1 
ATOM   9441  H  HB3  . ARG B 1 264 ? -0.711  31.969  35.535  1.00 13.22  ?  487  ARG B HB3  1 
ATOM   9442  H  HG2  . ARG B 1 264 ? -1.749  31.476  37.633  1.00 14.51  ?  487  ARG B HG2  1 
ATOM   9443  H  HG3  . ARG B 1 264 ? -0.437  30.660  38.006  1.00 14.51  ?  487  ARG B HG3  1 
ATOM   9444  H  HD2  . ARG B 1 264 ? -0.365  33.414  37.385  1.00 16.26  ?  487  ARG B HD2  1 
ATOM   9445  H  HD3  . ARG B 1 264 ? -0.454  32.882  38.880  1.00 16.26  ?  487  ARG B HD3  1 
ATOM   9446  H  HE   . ARG B 1 264 ? 1.768   32.930  37.384  1.00 15.75  ?  487  ARG B HE   1 
ATOM   9447  H  HH11 . ARG B 1 264 ? 0.518   31.526  40.117  1.00 17.15  ?  487  ARG B HH11 1 
ATOM   9448  H  HH12 . ARG B 1 264 ? 1.834   31.169  40.718  1.00 17.15  ?  487  ARG B HH12 1 
ATOM   9449  H  HH21 . ARG B 1 264 ? 3.735   32.379  38.322  1.00 15.86  ?  487  ARG B HH21 1 
ATOM   9450  H  HH22 . ARG B 1 264 ? 3.772   31.682  39.638  1.00 15.86  ?  487  ARG B HH22 1 
ATOM   9451  N  N    . VAL B 1 265 ? -2.257  30.771  33.314  1.00 10.72  ?  488  VAL B N    1 
ATOM   9452  C  CA   . VAL B 1 265 ? -2.242  31.051  31.887  1.00 10.76  ?  488  VAL B CA   1 
ATOM   9453  C  C    . VAL B 1 265 ? -1.254  32.174  31.622  1.00 10.39  ?  488  VAL B C    1 
ATOM   9454  O  O    . VAL B 1 265 ? -1.201  33.152  32.371  1.00 13.67  ?  488  VAL B O    1 
ATOM   9455  C  CB   . VAL B 1 265 ? -3.659  31.452  31.432  1.00 14.46  ?  488  VAL B CB   1 
ATOM   9456  C  CG1  . VAL B 1 265 ? -3.666  31.896  29.993  1.00 16.45  ?  488  VAL B CG1  1 
ATOM   9457  C  CG2  . VAL B 1 265 ? -4.620  30.306  31.630  1.00 16.07  ?  488  VAL B CG2  1 
ATOM   9458  H  H    . VAL B 1 265 ? -2.924  31.128  33.723  1.00 12.87  ?  488  VAL B H    1 
ATOM   9459  H  HA   . VAL B 1 265 ? -1.959  30.264  31.396  1.00 12.91  ?  488  VAL B HA   1 
ATOM   9460  H  HB   . VAL B 1 265 ? -3.952  32.200  31.975  1.00 17.35  ?  488  VAL B HB   1 
ATOM   9461  H  HG11 . VAL B 1 265 ? -4.571  32.137  29.741  1.00 19.74  ?  488  VAL B HG11 1 
ATOM   9462  H  HG12 . VAL B 1 265 ? -3.080  32.663  29.896  1.00 19.74  ?  488  VAL B HG12 1 
ATOM   9463  H  HG13 . VAL B 1 265 ? -3.351  31.166  29.436  1.00 19.74  ?  488  VAL B HG13 1 
ATOM   9464  H  HG21 . VAL B 1 265 ? -5.503  30.580  31.337  1.00 19.28  ?  488  VAL B HG21 1 
ATOM   9465  H  HG22 . VAL B 1 265 ? -4.319  29.547  31.108  1.00 19.28  ?  488  VAL B HG22 1 
ATOM   9466  H  HG23 . VAL B 1 265 ? -4.643  30.072  32.571  1.00 19.28  ?  488  VAL B HG23 1 
ATOM   9467  N  N    . LEU B 1 266 ? -0.491  32.053  30.536  1.00 9.05   ?  489  LEU B N    1 
ATOM   9468  C  CA   . LEU B 1 266 ? 0.553   33.018  30.191  1.00 9.48   ?  489  LEU B CA   1 
ATOM   9469  C  C    . LEU B 1 266 ? 0.166   33.955  29.048  1.00 8.35   ?  489  LEU B C    1 
ATOM   9470  O  O    . LEU B 1 266 ? 0.398   35.164  29.129  1.00 8.94   ?  489  LEU B O    1 
ATOM   9471  C  CB   . LEU B 1 266 ? 1.838   32.267  29.837  1.00 11.92  ?  489  LEU B CB   1 
ATOM   9472  C  CG   . LEU B 1 266 ? 2.216   31.277  30.945  1.00 15.46  ?  489  LEU B CG   1 
ATOM   9473  C  CD1  . LEU B 1 266 ? 3.304   30.398  30.464  1.00 18.57  ?  489  LEU B CD1  1 
ATOM   9474  C  CD2  . LEU B 1 266 ? 2.609   32.038  32.179  1.00 16.66  ?  489  LEU B CD2  1 
ATOM   9475  H  H    . LEU B 1 266 ? -0.560  31.407  29.972  1.00 10.86  ?  489  LEU B H    1 
ATOM   9476  H  HA   . LEU B 1 266 ? 0.731   33.580  30.961  1.00 11.38  ?  489  LEU B HA   1 
ATOM   9477  H  HB2  . LEU B 1 266 ? 1.705   31.772  29.013  1.00 14.30  ?  489  LEU B HB2  1 
ATOM   9478  H  HB3  . LEU B 1 266 ? 2.563   32.902  29.729  1.00 14.30  ?  489  LEU B HB3  1 
ATOM   9479  H  HG   . LEU B 1 266 ? 1.464   30.710  31.179  1.00 18.56  ?  489  LEU B HG   1 
ATOM   9480  H  HD11 . LEU B 1 266 ? 3.672   29.910  31.217  1.00 22.29  ?  489  LEU B HD11 1 
ATOM   9481  H  HD12 . LEU B 1 266 ? 2.944   29.776  29.812  1.00 22.29  ?  489  LEU B HD12 1 
ATOM   9482  H  HD13 . LEU B 1 266 ? 3.994   30.943  30.054  1.00 22.29  ?  489  LEU B HD13 1 
ATOM   9483  H  HD21 . LEU B 1 266 ? 3.025   31.427  32.807  1.00 20.00  ?  489  LEU B HD21 1 
ATOM   9484  H  HD22 . LEU B 1 266 ? 3.235   32.737  31.934  1.00 20.00  ?  489  LEU B HD22 1 
ATOM   9485  H  HD23 . LEU B 1 266 ? 1.814   32.429  32.575  1.00 20.00  ?  489  LEU B HD23 1 
ATOM   9486  N  N    . PHE B 1 267 ? -0.448  33.423  27.997  1.00 7.93   ?  490  PHE B N    1 
ATOM   9487  C  CA   . PHE B 1 267 ? -0.952  34.229  26.892  1.00 7.69   ?  490  PHE B CA   1 
ATOM   9488  C  C    . PHE B 1 267 ? -1.978  33.386  26.154  1.00 7.07   ?  490  PHE B C    1 
ATOM   9489  O  O    . PHE B 1 267 ? -2.127  32.191  26.421  1.00 7.04   ?  490  PHE B O    1 
ATOM   9490  C  CB   . PHE B 1 267 ? 0.178   34.736  25.966  1.00 7.64   ?  490  PHE B CB   1 
ATOM   9491  C  CG   . PHE B 1 267 ? 0.818   33.674  25.078  1.00 7.24   ?  490  PHE B CG   1 
ATOM   9492  C  CD1  . PHE B 1 267 ? 1.866   32.890  25.536  1.00 8.00   ?  490  PHE B CD1  1 
ATOM   9493  C  CD2  . PHE B 1 267 ? 0.408   33.502  23.771  1.00 7.73   ?  490  PHE B CD2  1 
ATOM   9494  C  CE1  . PHE B 1 267 ? 2.443   31.934  24.723  1.00 8.18   ?  490  PHE B CE1  1 
ATOM   9495  C  CE2  . PHE B 1 267 ? 0.981   32.554  22.964  1.00 8.37   ?  490  PHE B CE2  1 
ATOM   9496  C  CZ   . PHE B 1 267 ? 2.000   31.771  23.445  1.00 8.19   ?  490  PHE B CZ   1 
ATOM   9497  H  H    . PHE B 1 267 ? -0.589  32.581  27.898  1.00 9.52   ?  490  PHE B H    1 
ATOM   9498  H  HA   . PHE B 1 267 ? -1.392  35.022  27.235  1.00 9.23   ?  490  PHE B HA   1 
ATOM   9499  H  HB2  . PHE B 1 267 ? -0.188  35.419  25.383  1.00 9.18   ?  490  PHE B HB2  1 
ATOM   9500  H  HB3  . PHE B 1 267 ? 0.881   35.113  26.519  1.00 9.18   ?  490  PHE B HB3  1 
ATOM   9501  H  HD1  . PHE B 1 267 ? 2.185   33.010  26.401  1.00 9.60   ?  490  PHE B HD1  1 
ATOM   9502  H  HD2  . PHE B 1 267 ? -0.271  34.040  23.432  1.00 9.28   ?  490  PHE B HD2  1 
ATOM   9503  H  HE1  . PHE B 1 267 ? 3.133   31.401  25.048  1.00 9.81   ?  490  PHE B HE1  1 
ATOM   9504  H  HE2  . PHE B 1 267 ? 0.680   32.441  22.091  1.00 10.04  ?  490  PHE B HE2  1 
ATOM   9505  H  HZ   . PHE B 1 267 ? 2.390   31.127  22.898  1.00 9.83   ?  490  PHE B HZ   1 
ATOM   9506  N  N    . GLU B 1 268 ? -2.696  34.023  25.239  1.00 6.96   ?  491  GLU B N    1 
ATOM   9507  C  CA   . GLU B 1 268 ? -3.711  33.338  24.461  1.00 6.70   ?  491  GLU B CA   1 
ATOM   9508  C  C    . GLU B 1 268 ? -3.477  33.545  22.969  1.00 6.67   ?  491  GLU B C    1 
ATOM   9509  O  O    . GLU B 1 268 ? -2.767  34.463  22.546  1.00 7.05   ?  491  GLU B O    1 
ATOM   9510  C  CB   . GLU B 1 268 ? -5.126  33.759  24.864  1.00 7.39   ?  491  GLU B CB   1 
ATOM   9511  C  CG   . GLU B 1 268 ? -5.419  35.222  24.656  1.00 7.78   ?  491  GLU B CG   1 
ATOM   9512  C  CD   . GLU B 1 268 ? -6.842  35.605  25.020  1.00 8.80   ?  491  GLU B CD   1 
ATOM   9513  O  OE1  . GLU B 1 268 ? -7.541  34.777  25.634  1.00 10.55  ?  491  GLU B OE1  1 
ATOM   9514  O  OE2  . GLU B 1 268 ? -7.244  36.740  24.697  1.00 9.73   -1 491  GLU B OE2  1 
ATOM   9515  H  H    . GLU B 1 268 ? -2.612  34.858  25.052  1.00 8.36   ?  491  GLU B H    1 
ATOM   9516  H  HA   . GLU B 1 268 ? -3.636  32.384  24.623  1.00 8.05   ?  491  GLU B HA   1 
ATOM   9517  H  HB2  . GLU B 1 268 ? -5.763  33.254  24.335  1.00 8.87   ?  491  GLU B HB2  1 
ATOM   9518  H  HB3  . GLU B 1 268 ? -5.251  33.566  25.806  1.00 8.87   ?  491  GLU B HB3  1 
ATOM   9519  H  HG2  . GLU B 1 268 ? -4.819  35.745  25.209  1.00 9.34   ?  491  GLU B HG2  1 
ATOM   9520  H  HG3  . GLU B 1 268 ? -5.283  35.440  23.720  1.00 9.34   ?  491  GLU B HG3  1 
ATOM   9521  N  N    . ALA B 1 269 ? -4.093  32.666  22.180  1.00 6.50   ?  492  ALA B N    1 
ATOM   9522  C  CA   . ALA B 1 269 ? -3.884  32.622  20.745  1.00 6.03   ?  492  ALA B CA   1 
ATOM   9523  C  C    . ALA B 1 269 ? -5.110  32.005  20.076  1.00 6.09   ?  492  ALA B C    1 
ATOM   9524  O  O    . ALA B 1 269 ? -5.962  31.389  20.725  1.00 6.54   ?  492  ALA B O    1 
ATOM   9525  C  CB   . ALA B 1 269 ? -2.643  31.793  20.394  1.00 6.74   ?  492  ALA B CB   1 
ATOM   9526  H  H    . ALA B 1 269 ? -4.649  32.074  22.463  1.00 7.81   ?  492  ALA B H    1 
ATOM   9527  H  HA   . ALA B 1 269 ? -3.773  33.529  20.420  1.00 7.24   ?  492  ALA B HA   1 
ATOM   9528  H  HB1  . ALA B 1 269 ? -2.510  31.813  19.434  1.00 8.09   ?  492  ALA B HB1  1 
ATOM   9529  H  HB2  . ALA B 1 269 ? -1.872  32.175  20.842  1.00 8.09   ?  492  ALA B HB2  1 
ATOM   9530  H  HB3  . ALA B 1 269 ? -2.778  30.880  20.691  1.00 8.09   ?  492  ALA B HB3  1 
ATOM   9531  N  N    . LYS B 1 270 ? -5.189  32.177  18.758  1.00 5.82   ?  493  LYS B N    1 
ATOM   9532  C  CA   . LYS B 1 270 ? -6.197  31.543  17.933  1.00 6.23   ?  493  LYS B CA   1 
ATOM   9533  C  C    . LYS B 1 270 ? -5.578  30.383  17.169  1.00 6.15   ?  493  LYS B C    1 
ATOM   9534  O  O    . LYS B 1 270 ? -4.604  30.568  16.440  1.00 7.39   ?  493  LYS B O    1 
ATOM   9535  C  CB   . LYS B 1 270 ? -6.745  32.534  16.915  1.00 7.22   ?  493  LYS B CB   1 
ATOM   9536  C  CG   . LYS B 1 270 ? -7.612  33.583  17.467  1.00 9.10   ?  493  LYS B CG   1 
ATOM   9537  C  CD   . LYS B 1 270 ? -7.854  34.595  16.344  1.00 11.55  ?  493  LYS B CD   1 
ATOM   9538  C  CE   . LYS B 1 270 ? -8.920  35.575  16.680  1.00 11.37  ?  493  LYS B CE   1 
ATOM   9539  N  NZ   . LYS B 1 270 ? -8.849  36.765  15.812  1.00 9.70   ?  493  LYS B NZ   1 
ATOM   9540  H  H    . LYS B 1 270 ? -4.649  32.674  18.309  1.00 6.99   ?  493  LYS B H    1 
ATOM   9541  H  HA   . LYS B 1 270 ? -6.911  31.216  18.503  1.00 7.48   ?  493  LYS B HA   1 
ATOM   9542  H  HB2  . LYS B 1 270 ? -5.996  32.974  16.483  1.00 8.66   ?  493  LYS B HB2  1 
ATOM   9543  H  HB3  . LYS B 1 270 ? -7.265  32.044  16.259  1.00 8.66   ?  493  LYS B HB3  1 
ATOM   9544  H  HG2  . LYS B 1 270 ? -8.459  33.207  17.753  1.00 10.93  ?  493  LYS B HG2  1 
ATOM   9545  H  HG3  . LYS B 1 270 ? -7.176  34.025  18.213  1.00 10.93  ?  493  LYS B HG3  1 
ATOM   9546  H  HD2  . LYS B 1 270 ? -7.035  35.087  16.179  1.00 13.86  ?  493  LYS B HD2  1 
ATOM   9547  H  HD3  . LYS B 1 270 ? -8.124  34.120  15.543  1.00 13.86  ?  493  LYS B HD3  1 
ATOM   9548  H  HE2  . LYS B 1 270 ? -9.788  35.160  16.558  1.00 13.64  ?  493  LYS B HE2  1 
ATOM   9549  H  HE3  . LYS B 1 270 ? -8.815  35.862  17.600  1.00 13.64  ?  493  LYS B HE3  1 
ATOM   9550  H  HZ1  . LYS B 1 270 ? -8.945  36.527  14.960  1.00 11.65  ?  493  LYS B HZ1  1 
ATOM   9551  H  HZ2  . LYS B 1 270 ? -9.496  37.337  16.027  1.00 11.65  ?  493  LYS B HZ2  1 
ATOM   9552  H  HZ3  . LYS B 1 270 ? -8.062  37.169  15.912  1.00 11.65  ?  493  LYS B HZ3  1 
ATOM   9553  N  N    . LEU B 1 271 ? -6.176  29.209  17.293  1.00 5.81   ?  494  LEU B N    1 
ATOM   9554  C  CA   . LEU B 1 271 ? -5.835  28.053  16.478  1.00 5.82   ?  494  LEU B CA   1 
ATOM   9555  C  C    . LEU B 1 271 ? -6.896  27.944  15.382  1.00 5.50   ?  494  LEU B C    1 
ATOM   9556  O  O    . LEU B 1 271 ? -8.059  27.608  15.642  1.00 6.59   ?  494  LEU B O    1 
ATOM   9557  C  CB   . LEU B 1 271 ? -5.758  26.786  17.318  1.00 7.26   ?  494  LEU B CB   1 
ATOM   9558  C  CG   . LEU B 1 271 ? -5.568  25.498  16.517  1.00 7.91   ?  494  LEU B CG   1 
ATOM   9559  C  CD1  . LEU B 1 271 ? -4.280  25.476  15.720  1.00 8.59   ?  494  LEU B CD1  1 
ATOM   9560  C  CD2  . LEU B 1 271 ? -5.610  24.305  17.457  1.00 9.67   ?  494  LEU B CD2  1 
ATOM   9561  H  H    . LEU B 1 271 ? -6.803  29.052  17.861  1.00 6.98   ?  494  LEU B H    1 
ATOM   9562  H  HA   . LEU B 1 271 ? -4.965  28.177  16.067  1.00 6.99   ?  494  LEU B HA   1 
ATOM   9563  H  HB2  . LEU B 1 271 ? -5.006  26.867  17.926  1.00 8.71   ?  494  LEU B HB2  1 
ATOM   9564  H  HB3  . LEU B 1 271 ? -6.583  26.700  17.820  1.00 8.71   ?  494  LEU B HB3  1 
ATOM   9565  H  HG   . LEU B 1 271 ? -6.290  25.445  15.872  1.00 9.50   ?  494  LEU B HG   1 
ATOM   9566  H  HD11 . LEU B 1 271 ? -4.196  24.616  15.279  1.00 10.31  ?  494  LEU B HD11 1 
ATOM   9567  H  HD12 . LEU B 1 271 ? -4.305  26.185  15.059  1.00 10.31  ?  494  LEU B HD12 1 
ATOM   9568  H  HD13 . LEU B 1 271 ? -3.533  25.612  16.323  1.00 10.31  ?  494  LEU B HD13 1 
ATOM   9569  H  HD21 . LEU B 1 271 ? -5.472  23.494  16.944  1.00 11.61  ?  494  LEU B HD21 1 
ATOM   9570  H  HD22 . LEU B 1 271 ? -4.909  24.401  18.120  1.00 11.61  ?  494  LEU B HD22 1 
ATOM   9571  H  HD23 . LEU B 1 271 ? -6.476  24.278  17.894  1.00 11.61  ?  494  LEU B HD23 1 
ATOM   9572  N  N    . HIS B 1 272 ? -6.501  28.291  14.169  1.00 5.65   ?  495  HIS B N    1 
ATOM   9573  C  CA   . HIS B 1 272 ? -7.404  28.261  13.030  1.00 5.51   ?  495  HIS B CA   1 
ATOM   9574  C  C    . HIS B 1 272 ? -7.602  26.840  12.542  1.00 5.95   ?  495  HIS B C    1 
ATOM   9575  O  O    . HIS B 1 272 ? -6.673  26.032  12.517  1.00 6.63   ?  495  HIS B O    1 
ATOM   9576  C  CB   . HIS B 1 272 ? -6.819  29.144  11.933  1.00 5.59   ?  495  HIS B CB   1 
ATOM   9577  C  CG   . HIS B 1 272 ? -6.707  30.555  12.365  1.00 5.68   ?  495  HIS B CG   1 
ATOM   9578  N  ND1  . HIS B 1 272 ? -7.750  31.443  12.268  1.00 7.94   ?  495  HIS B ND1  1 
ATOM   9579  C  CD2  . HIS B 1 272 ? -5.702  31.200  12.998  1.00 7.02   ?  495  HIS B CD2  1 
ATOM   9580  C  CE1  . HIS B 1 272 ? -7.383  32.592  12.813  1.00 7.66   ?  495  HIS B CE1  1 
ATOM   9581  N  NE2  . HIS B 1 272 ? -6.135  32.478  13.236  1.00 7.86   ?  495  HIS B NE2  1 
ATOM   9582  H  H    . HIS B 1 272 ? -5.705  28.551  13.976  1.00 6.79   ?  495  HIS B H    1 
ATOM   9583  H  HA   . HIS B 1 272 ? -8.281  28.598  13.270  1.00 6.62   ?  495  HIS B HA   1 
ATOM   9584  H  HB2  . HIS B 1 272 ? -5.933  28.824  11.704  1.00 6.71   ?  495  HIS B HB2  1 
ATOM   9585  H  HB3  . HIS B 1 272 ? -7.396  29.109  11.154  1.00 6.71   ?  495  HIS B HB3  1 
ATOM   9586  H  HD2  . HIS B 1 272 ? -4.874  30.844  13.227  1.00 8.43   ?  495  HIS B HD2  1 
ATOM   9587  H  HE1  . HIS B 1 272 ? -7.913  33.352  12.885  1.00 9.20   ?  495  HIS B HE1  1 
ATOM   9588  H  HE2  . HIS B 1 272 ? -5.671  33.103  13.601  1.00 9.43   ?  495  HIS B HE2  1 
ATOM   9589  N  N    . ARG B 1 273 ? -8.823  26.558  12.098  1.00 6.18   ?  496  ARG B N    1 
ATOM   9590  C  CA   . ARG B 1 273 ? -9.153  25.206  11.645  1.00 6.69   ?  496  ARG B CA   1 
ATOM   9591  C  C    . ARG B 1 273 ? -8.210  24.718  10.561  1.00 6.89   ?  496  ARG B C    1 
ATOM   9592  O  O    . ARG B 1 273 ? -7.890  23.522  10.505  1.00 7.24   ?  496  ARG B O    1 
ATOM   9593  C  CB   . ARG B 1 273 ? -10.594 25.216  11.130  1.00 8.21   ?  496  ARG B CB   1 
ATOM   9594  C  CG   . ARG B 1 273 ? -11.062 23.924  10.513  1.00 10.86  ?  496  ARG B CG   1 
ATOM   9595  C  CD   . ARG B 1 273 ? -12.466 24.082  10.029  1.00 13.34  ?  496  ARG B CD   1 
ATOM   9596  N  NE   . ARG B 1 273 ? -12.932 22.845  9.440   1.00 16.03  ?  496  ARG B NE   1 
ATOM   9597  C  CZ   . ARG B 1 273 ? -14.175 22.661  9.033   1.00 17.63  ?  496  ARG B CZ   1 
ATOM   9598  N  NH1  . ARG B 1 273 ? -15.086 23.614  9.168   1.00 18.91  ?  496  ARG B NH1  1 
ATOM   9599  N  NH2  . ARG B 1 273 ? -14.513 21.496  8.490   1.00 19.51  ?  496  ARG B NH2  1 
ATOM   9600  H  H    . ARG B 1 273 ? -9.472  27.120  12.049  1.00 7.42   ?  496  ARG B H    1 
ATOM   9601  H  HA   . ARG B 1 273 ? -9.078  24.584  12.385  1.00 8.03   ?  496  ARG B HA   1 
ATOM   9602  H  HB2  . ARG B 1 273 ? -11.184 25.413  11.874  1.00 9.86   ?  496  ARG B HB2  1 
ATOM   9603  H  HB3  . ARG B 1 273 ? -10.672 25.906  10.453  1.00 9.86   ?  496  ARG B HB3  1 
ATOM   9604  H  HG2  . ARG B 1 273 ? -10.495 23.694  9.761   1.00 13.03  ?  496  ARG B HG2  1 
ATOM   9605  H  HG3  . ARG B 1 273 ? -11.037 23.216  11.176  1.00 13.03  ?  496  ARG B HG3  1 
ATOM   9606  H  HD2  . ARG B 1 273 ? -13.045 24.309  10.773  1.00 16.01  ?  496  ARG B HD2  1 
ATOM   9607  H  HD3  . ARG B 1 273 ? -12.503 24.780  9.355   1.00 16.01  ?  496  ARG B HD3  1 
ATOM   9608  H  HE   . ARG B 1 273 ? -12.372 22.198  9.351   1.00 19.24  ?  496  ARG B HE   1 
ATOM   9609  H  HH11 . ARG B 1 273 ? -14.872 24.366  9.526   1.00 22.69  ?  496  ARG B HH11 1 
ATOM   9610  H  HH12 . ARG B 1 273 ? -15.891 23.480  8.899   1.00 22.69  ?  496  ARG B HH12 1 
ATOM   9611  H  HH21 . ARG B 1 273 ? -13.926 20.873  8.408   1.00 23.41  ?  496  ARG B HH21 1 
ATOM   9612  H  HH22 . ARG B 1 273 ? -15.320 21.365  8.222   1.00 23.41  ?  496  ARG B HH22 1 
ATOM   9613  N  N    . GLN B 1 274 ? -7.740  25.624  9.706   0.90 6.44   ?  497  GLN B N    1 
ATOM   9614  C  CA   . GLN B 1 274 ? -6.806  25.251  8.660   0.90 7.34   ?  497  GLN B CA   1 
ATOM   9615  C  C    . GLN B 1 274 ? -5.495  24.690  9.184   0.90 7.12   ?  497  GLN B C    1 
ATOM   9616  O  O    . GLN B 1 274 ? -4.780  24.047  8.412   0.90 8.23   ?  497  GLN B O    1 
ATOM   9617  C  CB   . GLN B 1 274 ? -6.479  26.483  7.813   0.90 10.83  ?  497  GLN B CB   1 
ATOM   9618  C  CG   . GLN B 1 274 ? -7.591  26.953  6.891   0.90 16.69  ?  497  GLN B CG   1 
ATOM   9619  C  CD   . GLN B 1 274 ? -7.309  28.326  6.313   0.90 21.52  ?  497  GLN B CD   1 
ATOM   9620  O  OE1  . GLN B 1 274 ? -7.660  29.355  6.907   0.90 23.41  ?  497  GLN B OE1  1 
ATOM   9621  N  NE2  . GLN B 1 274 ? -6.666  28.354  5.152   0.90 23.38  ?  497  GLN B NE2  1 
ATOM   9622  H  H    . GLN B 1 274 ? -7.949  26.458  9.714   0.90 7.73   ?  497  GLN B H    1 
ATOM   9623  H  HA   . GLN B 1 274 ? -7.232  24.568  8.119   0.90 8.81   ?  497  GLN B HA   1 
ATOM   9624  H  HB2  . GLN B 1 274 ? -6.269  27.217  8.410   0.90 13.00  ?  497  GLN B HB2  1 
ATOM   9625  H  HB3  . GLN B 1 274 ? -5.711  26.276  7.257   0.90 13.00  ?  497  GLN B HB3  1 
ATOM   9626  H  HG2  . GLN B 1 274 ? -7.681  26.327  6.156   0.90 20.02  ?  497  GLN B HG2  1 
ATOM   9627  H  HG3  . GLN B 1 274 ? -8.421  26.999  7.391   0.90 20.02  ?  497  GLN B HG3  1 
ATOM   9628  H  HE21 . GLN B 1 274 ? -6.435  27.618  4.771   0.90 28.06  ?  497  GLN B HE21 1 
ATOM   9629  H  HE22 . GLN B 1 274 ? -6.482  29.107  4.781   0.90 28.06  ?  497  GLN B HE22 1 
ATOM   9630  N  N    . GLY B 1 275 ? -5.155  24.926  10.452  1.00 6.62   ?  498  GLY B N    1 
ATOM   9631  C  CA   . GLY B 1 275 ? -3.981  24.322  11.066  1.00 7.05   ?  498  GLY B CA   1 
ATOM   9632  C  C    . GLY B 1 275 ? -2.828  25.269  11.328  1.00 6.67   ?  498  GLY B C    1 
ATOM   9633  O  O    . GLY B 1 275 ? -1.658  24.906  11.166  1.00 7.59   ?  498  GLY B O    1 
ATOM   9634  H  H    . GLY B 1 275 ? -5.596  25.439  10.983  1.00 7.95   ?  498  GLY B H    1 
ATOM   9635  H  HA2  . GLY B 1 275 ? -4.241  23.935  11.916  1.00 8.46   ?  498  GLY B HA2  1 
ATOM   9636  H  HA3  . GLY B 1 275 ? -3.655  23.618  10.484  1.00 8.46   ?  498  GLY B HA3  1 
ATOM   9637  N  N    . PHE B 1 276 ? -3.124  26.482  11.786  1.00 6.67   ?  499  PHE B N    1 
ATOM   9638  C  CA   . PHE B 1 276 ? -2.070  27.421  12.141  1.00 6.33   ?  499  PHE B CA   1 
ATOM   9639  C  C    . PHE B 1 276 ? -2.578  28.314  13.257  1.00 5.75   ?  499  PHE B C    1 
ATOM   9640  O  O    . PHE B 1 276 ? -3.786  28.410  13.500  1.00 6.76   ?  499  PHE B O    1 
ATOM   9641  C  CB   . PHE B 1 276 ? -1.553  28.226  10.944  1.00 7.32   ?  499  PHE B CB   1 
ATOM   9642  C  CG   . PHE B 1 276 ? -2.517  29.243  10.398  1.00 7.59   ?  499  PHE B CG   1 
ATOM   9643  C  CD1  . PHE B 1 276 ? -3.598  28.880  9.601   1.00 8.61   ?  499  PHE B CD1  1 
ATOM   9644  C  CD2  . PHE B 1 276 ? -2.334  30.590  10.667  1.00 9.00   ?  499  PHE B CD2  1 
ATOM   9645  C  CE1  . PHE B 1 276 ? -4.459  29.851  9.088   1.00 10.25  ?  499  PHE B CE1  1 
ATOM   9646  C  CE2  . PHE B 1 276 ? -3.188  31.533  10.151  1.00 10.54  ?  499  PHE B CE2  1 
ATOM   9647  C  CZ   . PHE B 1 276 ? -4.248  31.160  9.373   1.00 10.50  ?  499  PHE B CZ   1 
ATOM   9648  H  H    . PHE B 1 276 ? -3.923  26.781  11.899  1.00 8.00   ?  499  PHE B H    1 
ATOM   9649  H  HA   . PHE B 1 276 ? -1.305  26.930  12.477  1.00 7.60   ?  499  PHE B HA   1 
ATOM   9650  H  HB2  . PHE B 1 276 ? -0.752  28.701  11.216  1.00 8.79   ?  499  PHE B HB2  1 
ATOM   9651  H  HB3  . PHE B 1 276 ? -1.345  27.609  10.225  1.00 8.79   ?  499  PHE B HB3  1 
ATOM   9652  H  HD1  . PHE B 1 276 ? -3.747  27.983  9.408   1.00 10.33  ?  499  PHE B HD1  1 
ATOM   9653  H  HD2  . PHE B 1 276 ? -1.623  30.858  11.203  1.00 10.80  ?  499  PHE B HD2  1 
ATOM   9654  H  HE1  . PHE B 1 276 ? -5.177  29.601  8.552   1.00 12.31  ?  499  PHE B HE1  1 
ATOM   9655  H  HE2  . PHE B 1 276 ? -3.044  32.434  10.333  1.00 12.65  ?  499  PHE B HE2  1 
ATOM   9656  H  HZ   . PHE B 1 276 ? -4.827  31.807  9.038   1.00 12.60  ?  499  PHE B HZ   1 
ATOM   9657  N  N    . ILE B 1 277 ? -1.636  28.983  13.916  1.00 5.67   ?  500  ILE B N    1 
ATOM   9658  C  CA   . ILE B 1 277 ? -1.899  29.786  15.105  1.00 5.47   ?  500  ILE B CA   1 
ATOM   9659  C  C    . ILE B 1 277 ? -1.604  31.251  14.822  1.00 5.91   ?  500  ILE B C    1 
ATOM   9660  O  O    . ILE B 1 277 ? -0.573  31.579  14.217  1.00 6.29   ?  500  ILE B O    1 
ATOM   9661  C  CB   . ILE B 1 277 ? -1.003  29.314  16.269  1.00 5.89   ?  500  ILE B CB   1 
ATOM   9662  C  CG1  . ILE B 1 277 ? -1.230  27.834  16.582  1.00 6.04   ?  500  ILE B CG1  1 
ATOM   9663  C  CG2  . ILE B 1 277 ? -1.245  30.170  17.496  1.00 6.09   ?  500  ILE B CG2  1 
ATOM   9664  C  CD1  . ILE B 1 277 ? -0.248  27.237  17.586  1.00 7.58   ?  500  ILE B CD1  1 
ATOM   9665  H  H    . ILE B 1 277 ? -0.808  28.986  13.685  1.00 6.80   ?  500  ILE B H    1 
ATOM   9666  H  HA   . ILE B 1 277 ? -2.838  29.706  15.332  1.00 6.56   ?  500  ILE B HA   1 
ATOM   9667  H  HB   . ILE B 1 277 ? -0.077  29.415  15.996  1.00 7.07   ?  500  ILE B HB   1 
ATOM   9668  H  HG12 . ILE B 1 277 ? -2.122  27.729  16.949  1.00 7.25   ?  500  ILE B HG12 1 
ATOM   9669  H  HG13 . ILE B 1 277 ? -1.149  27.328  15.758  1.00 7.25   ?  500  ILE B HG13 1 
ATOM   9670  H  HG21 . ILE B 1 277 ? -0.806  29.761  18.258  1.00 7.31   ?  500  ILE B HG21 1 
ATOM   9671  H  HG22 . ILE B 1 277 ? -0.880  31.056  17.340  1.00 7.31   ?  500  ILE B HG22 1 
ATOM   9672  H  HG23 . ILE B 1 277 ? -2.200  30.230  17.656  1.00 7.31   ?  500  ILE B HG23 1 
ATOM   9673  H  HD11 . ILE B 1 277 ? -0.313  26.270  17.555  1.00 9.10   ?  500  ILE B HD11 1 
ATOM   9674  H  HD12 . ILE B 1 277 ? 0.652   27.515  17.351  1.00 9.10   ?  500  ILE B HD12 1 
ATOM   9675  H  HD13 . ILE B 1 277 ? -0.471  27.556  18.474  1.00 9.10   ?  500  ILE B HD13 1 
ATOM   9676  N  N    . THR B 1 278 ? -2.467  32.143  15.315  1.00 6.28   ?  501  THR B N    1 
ATOM   9677  C  CA   . THR B 1 278 ? -2.155  33.570  15.325  1.00 6.06   ?  501  THR B CA   1 
ATOM   9678  C  C    . THR B 1 278 ? -2.214  34.127  16.743  1.00 5.87   ?  501  THR B C    1 
ATOM   9679  O  O    . THR B 1 278 ? -2.931  33.616  17.616  1.00 5.99   ?  501  THR B O    1 
ATOM   9680  C  CB   . THR B 1 278 ? -3.062  34.384  14.384  1.00 6.35   ?  501  THR B CB   1 
ATOM   9681  O  OG1  . THR B 1 278 ? -4.427  34.233  14.771  1.00 6.50   ?  501  THR B OG1  1 
ATOM   9682  C  CG2  . THR B 1 278 ? -2.867  33.942  12.932  1.00 7.36   ?  501  THR B CG2  1 
ATOM   9683  H  H    . THR B 1 278 ? -3.235  31.944  15.646  1.00 7.54   ?  501  THR B H    1 
ATOM   9684  H  HA   . THR B 1 278 ? -1.245  33.684  15.007  1.00 7.28   ?  501  THR B HA   1 
ATOM   9685  H  HB   . THR B 1 278 ? -2.828  35.324  14.442  1.00 7.62   ?  501  THR B HB   1 
ATOM   9686  H  HG1  . THR B 1 278 ? -4.912  34.752  14.322  1.00 7.81   ?  501  THR B HG1  1 
ATOM   9687  H  HG21 . THR B 1 278 ? -3.437  34.466  12.347  1.00 8.84   ?  501  THR B HG21 1 
ATOM   9688  H  HG22 . THR B 1 278 ? -1.943  34.070  12.667  1.00 8.84   ?  501  THR B HG22 1 
ATOM   9689  H  HG23 . THR B 1 278 ? -3.095  33.004  12.837  1.00 8.84   ?  501  THR B HG23 1 
ATOM   9690  N  N    . VAL B 1 279 ? -1.444  35.195  16.944  1.00 6.25   ?  502  VAL B N    1 
ATOM   9691  C  CA   . VAL B 1 279 ? -1.321  35.896  18.212  1.00 6.77   ?  502  VAL B CA   1 
ATOM   9692  C  C    . VAL B 1 279 ? -1.411  37.392  17.940  1.00 6.34   ?  502  VAL B C    1 
ATOM   9693  O  O    . VAL B 1 279 ? -1.095  37.871  16.850  1.00 7.30   ?  502  VAL B O    1 
ATOM   9694  C  CB   . VAL B 1 279 ? 0.013   35.569  18.933  1.00 6.80   ?  502  VAL B CB   1 
ATOM   9695  C  CG1  . VAL B 1 279 ? -0.028  34.139  19.474  1.00 7.22   ?  502  VAL B CG1  1 
ATOM   9696  C  CG2  . VAL B 1 279 ? 1.229   35.812  18.007  1.00 7.76   ?  502  VAL B CG2  1 
ATOM   9697  H  H    . VAL B 1 279 ? -0.961  35.548  16.326  1.00 7.50   ?  502  VAL B H    1 
ATOM   9698  H  HA   . VAL B 1 279 ? -2.053  35.639  18.795  1.00 8.13   ?  502  VAL B HA   1 
ATOM   9699  H  HB   . VAL B 1 279 ? 0.127   36.167  19.688  1.00 8.16   ?  502  VAL B HB   1 
ATOM   9700  H  HG11 . VAL B 1 279 ? 0.816   33.941  19.909  1.00 8.67   ?  502  VAL B HG11 1 
ATOM   9701  H  HG12 . VAL B 1 279 ? -0.755  34.064  20.113  1.00 8.67   ?  502  VAL B HG12 1 
ATOM   9702  H  HG13 . VAL B 1 279 ? -0.172  33.526  18.736  1.00 8.67   ?  502  VAL B HG13 1 
ATOM   9703  H  HG21 . VAL B 1 279 ? 2.042   35.589  18.487  1.00 9.32   ?  502  VAL B HG21 1 
ATOM   9704  H  HG22 . VAL B 1 279 ? 1.145   35.251  17.220  1.00 9.32   ?  502  VAL B HG22 1 
ATOM   9705  H  HG23 . VAL B 1 279 ? 1.245   36.747  17.746  1.00 9.32   ?  502  VAL B HG23 1 
ATOM   9706  N  N    . ALA B 1 280 ? -1.810  38.138  18.970  1.00 6.83   ?  503  ALA B N    1 
ATOM   9707  C  CA   . ALA B 1 280 ? -1.838  39.600  18.916  1.00 7.48   ?  503  ALA B CA   1 
ATOM   9708  C  C    . ALA B 1 280 ? -0.480  40.105  19.383  1.00 7.56   ?  503  ALA B C    1 
ATOM   9709  O  O    . ALA B 1 280 ? -0.214  40.272  20.572  1.00 8.45   ?  503  ALA B O    1 
ATOM   9710  C  CB   . ALA B 1 280 ? -2.982  40.144  19.764  1.00 9.29   ?  503  ALA B CB   1 
ATOM   9711  H  H    . ALA B 1 280 ? -2.074  37.816  19.723  1.00 8.20   ?  503  ALA B H    1 
ATOM   9712  H  HA   . ALA B 1 280 ? -1.975  39.896  18.003  1.00 8.98   ?  503  ALA B HA   1 
ATOM   9713  H  HB1  . ALA B 1 280 ? -2.973  41.113  19.722  1.00 11.15  ?  503  ALA B HB1  1 
ATOM   9714  H  HB2  . ALA B 1 280 ? -3.822  39.806  19.415  1.00 11.15  ?  503  ALA B HB2  1 
ATOM   9715  H  HB3  . ALA B 1 280 ? -2.863  39.852  20.681  1.00 11.15  ?  503  ALA B HB3  1 
ATOM   9716  N  N    . LYS B 1 281 ? 0.399   40.360  18.421  1.00 9.05   ?  504  LYS B N    1 
ATOM   9717  C  CA   . LYS B 1 281 ? 1.722   40.892  18.691  1.00 9.62   ?  504  LYS B CA   1 
ATOM   9718  C  C    . LYS B 1 281 ? 2.205   41.603  17.441  1.00 10.62  ?  504  LYS B C    1 
ATOM   9719  O  O    . LYS B 1 281 ? 1.891   41.198  16.323  1.00 11.65  ?  504  LYS B O    1 
ATOM   9720  C  CB   . LYS B 1 281 ? 2.726   39.794  19.087  1.00 10.31  ?  504  LYS B CB   1 
ATOM   9721  C  CG   . LYS B 1 281 ? 4.110   40.354  19.447  1.00 10.71  ?  504  LYS B CG   1 
ATOM   9722  C  CD   . LYS B 1 281 ? 5.031   39.359  20.144  1.00 11.43  ?  504  LYS B CD   1 
ATOM   9723  C  CE   . LYS B 1 281 ? 6.401   39.974  20.397  1.00 11.81  ?  504  LYS B CE   1 
ATOM   9724  N  NZ   . LYS B 1 281 ? 7.340   39.032  21.082  1.00 11.92  ?  504  LYS B NZ   1 
ATOM   9725  H  H    . LYS B 1 281 ? 0.246   40.230  17.585  1.00 10.86  ?  504  LYS B H    1 
ATOM   9726  H  HA   . LYS B 1 281 ? 1.668   41.524  19.425  1.00 11.55  ?  504  LYS B HA   1 
ATOM   9727  H  HB2  . LYS B 1 281 ? 2.385   39.319  19.861  1.00 12.38  ?  504  LYS B HB2  1 
ATOM   9728  H  HB3  . LYS B 1 281 ? 2.834   39.182  18.343  1.00 12.38  ?  504  LYS B HB3  1 
ATOM   9729  H  HG2  . LYS B 1 281 ? 4.550   40.639  18.631  1.00 12.85  ?  504  LYS B HG2  1 
ATOM   9730  H  HG3  . LYS B 1 281 ? 3.993   41.111  20.042  1.00 12.85  ?  504  LYS B HG3  1 
ATOM   9731  H  HD2  . LYS B 1 281 ? 4.646   39.104  20.997  1.00 13.72  ?  504  LYS B HD2  1 
ATOM   9732  H  HD3  . LYS B 1 281 ? 5.145   38.576  19.583  1.00 13.72  ?  504  LYS B HD3  1 
ATOM   9733  H  HE2  . LYS B 1 281 ? 6.796   40.227  19.548  1.00 14.17  ?  504  LYS B HE2  1 
ATOM   9734  H  HE3  . LYS B 1 281 ? 6.297   40.757  20.961  1.00 14.17  ?  504  LYS B HE3  1 
ATOM   9735  H  HZ1  . LYS B 1 281 ? 8.129   39.426  21.206  1.00 14.30  ?  504  LYS B HZ1  1 
ATOM   9736  H  HZ2  . LYS B 1 281 ? 7.009   38.794  21.873  1.00 14.30  ?  504  LYS B HZ2  1 
ATOM   9737  H  HZ3  . LYS B 1 281 ? 7.455   38.303  20.585  1.00 14.30  ?  504  LYS B HZ3  1 
ATOM   9738  N  N    . SER B 1 282 ? 2.966   42.661  17.639  1.00 11.28  ?  505  SER B N    1 
ATOM   9739  C  CA   A SER B 1 282 ? 3.586   43.406  16.549  0.39 13.23  ?  505  SER B CA   1 
ATOM   9740  C  CA   B SER B 1 282 ? 3.585   43.403  16.547  0.61 13.18  ?  505  SER B CA   1 
ATOM   9741  C  C    . SER B 1 282 ? 5.094   43.366  16.751  1.00 13.49  ?  505  SER B C    1 
ATOM   9742  O  O    . SER B 1 282 ? 5.606   43.918  17.731  1.00 16.55  ?  505  SER B O    1 
ATOM   9743  C  CB   A SER B 1 282 ? 3.092   44.851  16.531  0.39 15.39  ?  505  SER B CB   1 
ATOM   9744  C  CB   B SER B 1 282 ? 3.068   44.842  16.512  0.61 15.48  ?  505  SER B CB   1 
ATOM   9745  O  OG   A SER B 1 282 ? 3.622   45.549  15.418  0.39 17.30  ?  505  SER B OG   1 
ATOM   9746  O  OG   B SER B 1 282 ? 1.710   44.898  16.086  0.61 17.33  ?  505  SER B OG   1 
ATOM   9747  H  H    A SER B 1 282 ? 3.145   42.980  18.417  0.39 13.54  ?  505  SER B H    1 
ATOM   9748  H  H    B SER B 1 282 ? 3.145   42.981  18.417  0.61 13.54  ?  505  SER B H    1 
ATOM   9749  H  HA   A SER B 1 282 ? 3.367   42.986  15.703  0.39 15.88  ?  505  SER B HA   1 
ATOM   9750  H  HA   B SER B 1 282 ? 3.377   42.980  15.700  0.61 15.82  ?  505  SER B HA   1 
ATOM   9751  H  HB2  A SER B 1 282 ? 2.124   44.853  16.473  0.39 18.47  ?  505  SER B HB2  1 
ATOM   9752  H  HB2  B SER B 1 282 ? 3.133   45.220  17.403  0.61 18.58  ?  505  SER B HB2  1 
ATOM   9753  H  HB3  A SER B 1 282 ? 3.377   45.293  17.346  0.39 18.47  ?  505  SER B HB3  1 
ATOM   9754  H  HB3  B SER B 1 282 ? 3.612   45.355  15.894  0.61 18.58  ?  505  SER B HB3  1 
ATOM   9755  H  HG   A SER B 1 282 ? 4.461   45.562  15.461  0.39 20.76  ?  505  SER B HG   1 
ATOM   9756  H  HG   B SER B 1 282 ? 1.227   44.449  16.606  0.61 20.80  ?  505  SER B HG   1 
ATOM   9757  N  N    . GLY B 1 283 ? 5.797   42.720  15.837  1.00 11.89  ?  506  GLY B N    1 
ATOM   9758  C  CA   . GLY B 1 283 ? 7.246   42.678  15.856  1.00 12.79  ?  506  GLY B CA   1 
ATOM   9759  C  C    . GLY B 1 283 ? 7.777   41.316  16.272  1.00 11.16  ?  506  GLY B C    1 
ATOM   9760  O  O    . GLY B 1 283 ? 7.044   40.350  16.459  1.00 12.37  ?  506  GLY B O    1 
ATOM   9761  H  H    . GLY B 1 283 ? 5.448   42.288  15.180  1.00 14.27  ?  506  GLY B H    1 
ATOM   9762  H  HA2  . GLY B 1 283 ? 7.586   42.881  14.970  1.00 15.35  ?  506  GLY B HA2  1 
ATOM   9763  H  HA3  . GLY B 1 283 ? 7.579   43.340  16.482  1.00 15.35  ?  506  GLY B HA3  1 
ATOM   9764  N  N    . ASP B 1 284 ? 9.097   41.282  16.381  0.80 10.07  ?  507  ASP B N    1 
ATOM   9765  C  CA   . ASP B 1 284 ? 9.866   40.081  16.687  0.80 9.70   ?  507  ASP B CA   1 
ATOM   9766  C  C    . ASP B 1 284 ? 10.697  40.469  17.900  0.80 10.78  ?  507  ASP B C    1 
ATOM   9767  O  O    . ASP B 1 284 ? 11.577  41.336  17.806  0.80 12.61  ?  507  ASP B O    1 
ATOM   9768  C  CB   . ASP B 1 284 ? 10.747  39.701  15.493  0.80 10.45  ?  507  ASP B CB   1 
ATOM   9769  C  CG   . ASP B 1 284 ? 11.549  38.432  15.719  0.80 11.54  ?  507  ASP B CG   1 
ATOM   9770  O  OD1  . ASP B 1 284 ? 11.395  37.801  16.776  0.80 11.67  ?  507  ASP B OD1  1 
ATOM   9771  O  OD2  . ASP B 1 284 ? 12.348  38.071  14.825  0.80 13.19  -1 507  ASP B OD2  1 
ATOM   9772  H  H    . ASP B 1 284 ? 9.595   41.975  16.278  0.80 12.08  ?  507  ASP B H    1 
ATOM   9773  H  HA   . ASP B 1 284 ? 9.308   39.314  16.891  0.80 11.64  ?  507  ASP B HA   1 
ATOM   9774  H  HB2  . ASP B 1 284 ? 10.181  39.561  14.718  0.80 12.54  ?  507  ASP B HB2  1 
ATOM   9775  H  HB3  . ASP B 1 284 ? 11.372  40.422  15.323  0.80 12.54  ?  507  ASP B HB3  1 
ATOM   9776  N  N    . SER B 1 285 ? 10.396  39.863  19.040  1.00 11.12  ?  508  SER B N    1 
ATOM   9777  C  CA   . SER B 1 285 ? 11.136  40.089  20.274  1.00 10.91  ?  508  SER B CA   1 
ATOM   9778  C  C    . SER B 1 285 ? 11.040  38.823  21.116  1.00 10.72  ?  508  SER B C    1 
ATOM   9779  O  O    . SER B 1 285 ? 10.177  37.978  20.867  1.00 10.90  ?  508  SER B O    1 
ATOM   9780  C  CB   . SER B 1 285 ? 10.623  41.317  21.042  1.00 11.41  ?  508  SER B CB   1 
ATOM   9781  O  OG   . SER B 1 285 ? 9.276   41.178  21.465  1.00 11.91  ?  508  SER B OG   1 
ATOM   9782  H  H    . SER B 1 285 ? 9.751   39.301  19.127  1.00 13.34  ?  508  SER B H    1 
ATOM   9783  H  HA   . SER B 1 285 ? 12.071  40.251  20.074  1.00 13.09  ?  508  SER B HA   1 
ATOM   9784  H  HB2  . SER B 1 285 ? 11.180  41.444  21.826  1.00 13.69  ?  508  SER B HB2  1 
ATOM   9785  H  HB3  . SER B 1 285 ? 10.685  42.091  20.462  1.00 13.69  ?  508  SER B HB3  1 
ATOM   9786  H  HG   . SER B 1 285 ? 8.762   41.211  20.801  1.00 14.30  ?  508  SER B HG   1 
ATOM   9787  N  N    . PRO B 1 286 ? 11.924  38.658  22.099  1.00 11.23  ?  509  PRO B N    1 
ATOM   9788  C  CA   . PRO B 1 286 ? 11.935  37.424  22.897  1.00 11.78  ?  509  PRO B CA   1 
ATOM   9789  C  C    . PRO B 1 286 ? 10.563  37.062  23.442  1.00 11.46  ?  509  PRO B C    1 
ATOM   9790  O  O    . PRO B 1 286 ? 9.835   37.910  23.957  1.00 11.73  ?  509  PRO B O    1 
ATOM   9791  C  CB   . PRO B 1 286 ? 12.932  37.751  24.016  1.00 12.82  ?  509  PRO B CB   1 
ATOM   9792  C  CG   . PRO B 1 286 ? 13.889  38.693  23.370  1.00 13.19  ?  509  PRO B CG   1 
ATOM   9793  C  CD   . PRO B 1 286 ? 13.048  39.552  22.445  1.00 12.10  ?  509  PRO B CD   1 
ATOM   9794  H  HA   . PRO B 1 286 ? 12.260  36.683  22.362  1.00 14.14  ?  509  PRO B HA   1 
ATOM   9795  H  HB2  . PRO B 1 286 ? 12.475  38.170  24.762  1.00 15.38  ?  509  PRO B HB2  1 
ATOM   9796  H  HB3  . PRO B 1 286 ? 13.380  36.943  24.313  1.00 15.38  ?  509  PRO B HB3  1 
ATOM   9797  H  HG2  . PRO B 1 286 ? 14.323  39.236  24.046  1.00 15.83  ?  509  PRO B HG2  1 
ATOM   9798  H  HG3  . PRO B 1 286 ? 14.553  38.194  22.868  1.00 15.83  ?  509  PRO B HG3  1 
ATOM   9799  H  HD2  . PRO B 1 286 ? 12.732  40.347  22.903  1.00 14.52  ?  509  PRO B HD2  1 
ATOM   9800  H  HD3  . PRO B 1 286 ? 13.549  39.802  21.653  1.00 14.52  ?  509  PRO B HD3  1 
ATOM   9801  N  N    . ILE B 1 287 ? 10.211  35.785  23.318  1.00 10.96  ?  510  ILE B N    1 
ATOM   9802  C  CA   . ILE B 1 287 ? 8.969   35.229  23.845  1.00 10.26  ?  510  ILE B CA   1 
ATOM   9803  C  C    . ILE B 1 287 ? 9.295   34.553  25.173  1.00 10.05  ?  510  ILE B C    1 
ATOM   9804  O  O    . ILE B 1 287 ? 9.917   33.485  25.220  1.00 11.72  ?  510  ILE B O    1 
ATOM   9805  C  CB   . ILE B 1 287 ? 8.322   34.257  22.848  1.00 9.97   ?  510  ILE B CB   1 
ATOM   9806  C  CG1  . ILE B 1 287 ? 7.980   35.010  21.559  1.00 10.45  ?  510  ILE B CG1  1 
ATOM   9807  C  CG2  . ILE B 1 287 ? 7.088   33.611  23.451  1.00 10.86  ?  510  ILE B CG2  1 
ATOM   9808  C  CD1  . ILE B 1 287 ? 7.565   34.112  20.419  1.00 10.75  ?  510  ILE B CD1  1 
ATOM   9809  H  H    . ILE B 1 287 ? 10.695  35.199  22.915  1.00 13.15  ?  510  ILE B H    1 
ATOM   9810  H  HA   . ILE B 1 287 ? 8.338   35.945  24.020  1.00 12.32  ?  510  ILE B HA   1 
ATOM   9811  H  HB   . ILE B 1 287 ? 8.951   33.548  22.640  1.00 11.96  ?  510  ILE B HB   1 
ATOM   9812  H  HG12 . ILE B 1 287 ? 7.246   35.618  21.739  1.00 12.54  ?  510  ILE B HG12 1 
ATOM   9813  H  HG13 . ILE B 1 287 ? 8.761   35.509  21.273  1.00 12.54  ?  510  ILE B HG13 1 
ATOM   9814  H  HG21 . ILE B 1 287 ? 6.636   33.095  22.766  1.00 13.03  ?  510  ILE B HG21 1 
ATOM   9815  H  HG22 . ILE B 1 287 ? 7.359   33.030  24.178  1.00 13.03  ?  510  ILE B HG22 1 
ATOM   9816  H  HG23 . ILE B 1 287 ? 6.499   34.306  23.784  1.00 13.03  ?  510  ILE B HG23 1 
ATOM   9817  H  HD11 . ILE B 1 287 ? 7.536   34.632  19.601  1.00 12.90  ?  510  ILE B HD11 1 
ATOM   9818  H  HD12 . ILE B 1 287 ? 8.212   33.394  20.331  1.00 12.90  ?  510  ILE B HD12 1 
ATOM   9819  H  HD13 . ILE B 1 287 ? 6.688   33.745  20.609  1.00 12.90  ?  510  ILE B HD13 1 
ATOM   9820  N  N    . ASN B 1 288 ? 8.892   35.178  26.264  1.00 9.18   ?  511  ASN B N    1 
ATOM   9821  C  CA   . ASN B 1 288 ? 9.329   34.772  27.601  1.00 8.98   ?  511  ASN B CA   1 
ATOM   9822  C  C    . ASN B 1 288 ? 8.277   33.850  28.195  1.00 8.73   ?  511  ASN B C    1 
ATOM   9823  O  O    . ASN B 1 288 ? 7.309   34.288  28.821  1.00 9.00   ?  511  ASN B O    1 
ATOM   9824  C  CB   . ASN B 1 288 ? 9.609   36.006  28.440  1.00 9.42   ?  511  ASN B CB   1 
ATOM   9825  C  CG   . ASN B 1 288 ? 10.848  36.725  27.976  1.00 9.78   ?  511  ASN B CG   1 
ATOM   9826  O  OD1  . ASN B 1 288 ? 11.893  36.104  27.789  1.00 11.67  ?  511  ASN B OD1  1 
ATOM   9827  N  ND2  . ASN B 1 288 ? 10.744  38.022  27.765  1.00 9.60   ?  511  ASN B ND2  1 
ATOM   9828  H  H    . ASN B 1 288 ? 8.356   35.851  26.263  1.00 11.02  ?  511  ASN B H    1 
ATOM   9829  H  HA   . ASN B 1 288 ? 10.145  34.250  27.547  1.00 10.78  ?  511  ASN B HA   1 
ATOM   9830  H  HB2  . ASN B 1 288 ? 8.859   36.617  28.372  1.00 11.31  ?  511  ASN B HB2  1 
ATOM   9831  H  HB3  . ASN B 1 288 ? 9.739   35.742  29.365  1.00 11.31  ?  511  ASN B HB3  1 
ATOM   9832  H  HD21 . ASN B 1 288 ? 11.428  38.471  27.499  1.00 11.52  ?  511  ASN B HD21 1 
ATOM   9833  H  HD22 . ASN B 1 288 ? 9.992   38.420  27.892  1.00 11.52  ?  511  ASN B HD22 1 
ATOM   9834  N  N    . VAL B 1 289 ? 8.470   32.551  27.968  1.00 9.02   ?  512  VAL B N    1 
ATOM   9835  C  CA   . VAL B 1 289 ? 7.578   31.500  28.455  1.00 9.64   ?  512  VAL B CA   1 
ATOM   9836  C  C    . VAL B 1 289 ? 8.405   30.409  29.124  1.00 10.42  ?  512  VAL B C    1 
ATOM   9837  O  O    . VAL B 1 289 ? 9.596   30.240  28.827  1.00 11.43  ?  512  VAL B O    1 
ATOM   9838  C  CB   . VAL B 1 289 ? 6.728   30.893  27.314  1.00 10.65  ?  512  VAL B CB   1 
ATOM   9839  C  CG1  . VAL B 1 289 ? 5.732   31.908  26.784  1.00 11.25  ?  512  VAL B CG1  1 
ATOM   9840  C  CG2  . VAL B 1 289 ? 7.612   30.363  26.176  1.00 12.23  ?  512  VAL B CG2  1 
ATOM   9841  H  H    . VAL B 1 289 ? 9.135   32.241  27.519  1.00 10.83  ?  512  VAL B H    1 
ATOM   9842  H  HA   . VAL B 1 289 ? 6.987   31.889  29.119  1.00 11.57  ?  512  VAL B HA   1 
ATOM   9843  H  HB   . VAL B 1 289 ? 6.233   30.141  27.677  1.00 12.78  ?  512  VAL B HB   1 
ATOM   9844  H  HG11 . VAL B 1 289 ? 5.222   31.505  26.064  1.00 13.50  ?  512  VAL B HG11 1 
ATOM   9845  H  HG12 . VAL B 1 289 ? 5.138   32.173  27.503  1.00 13.50  ?  512  VAL B HG12 1 
ATOM   9846  H  HG13 . VAL B 1 289 ? 6.216   32.682  26.453  1.00 13.50  ?  512  VAL B HG13 1 
ATOM   9847  H  HG21 . VAL B 1 289 ? 7.044   30.015  25.471  1.00 14.67  ?  512  VAL B HG21 1 
ATOM   9848  H  HG22 . VAL B 1 289 ? 8.156   31.090  25.835  1.00 14.67  ?  512  VAL B HG22 1 
ATOM   9849  H  HG23 . VAL B 1 289 ? 8.181   29.658  26.521  1.00 14.67  ?  512  VAL B HG23 1 
ATOM   9850  N  N    . PRO B 1 290 ? 7.794   29.636  30.020  1.00 10.49  ?  513  PRO B N    1 
ATOM   9851  C  CA   . PRO B 1 290 ? 8.521   28.573  30.716  1.00 10.90  ?  513  PRO B CA   1 
ATOM   9852  C  C    . PRO B 1 290 ? 8.685   27.342  29.839  1.00 9.92   ?  513  PRO B C    1 
ATOM   9853  O  O    . PRO B 1 290 ? 7.846   27.041  28.982  1.00 10.20  ?  513  PRO B O    1 
ATOM   9854  C  CB   . PRO B 1 290 ? 7.614   28.274  31.916  1.00 11.53  ?  513  PRO B CB   1 
ATOM   9855  C  CG   . PRO B 1 290 ? 6.250   28.576  31.420  1.00 11.23  ?  513  PRO B CG   1 
ATOM   9856  C  CD   . PRO B 1 290 ? 6.416   29.777  30.524  1.00 11.77  ?  513  PRO B CD   1 
ATOM   9857  H  HA   . PRO B 1 290 ? 9.390   28.876  31.022  1.00 13.08  ?  513  PRO B HA   1 
ATOM   9858  H  HB2  . PRO B 1 290 ? 7.695   27.342  32.172  1.00 13.84  ?  513  PRO B HB2  1 
ATOM   9859  H  HB3  . PRO B 1 290 ? 7.849   28.845  32.663  1.00 13.84  ?  513  PRO B HB3  1 
ATOM   9860  H  HG2  . PRO B 1 290 ? 5.904   27.819  30.923  1.00 13.48  ?  513  PRO B HG2  1 
ATOM   9861  H  HG3  . PRO B 1 290 ? 5.665   28.779  32.166  1.00 13.48  ?  513  PRO B HG3  1 
ATOM   9862  H  HD2  . PRO B 1 290 ? 5.777   29.754  29.794  1.00 14.12  ?  513  PRO B HD2  1 
ATOM   9863  H  HD3  . PRO B 1 290 ? 6.315   30.600  31.027  1.00 14.12  ?  513  PRO B HD3  1 
ATOM   9864  N  N    . ALA B 1 291 ? 9.764   26.602  30.101  1.00 10.98  ?  514  ALA B N    1 
ATOM   9865  C  CA   . ALA B 1 291 ? 10.018  25.380  29.346  1.00 11.71  ?  514  ALA B CA   1 
ATOM   9866  C  C    . ALA B 1 291 ? 8.948   24.320  29.564  1.00 10.40  ?  514  ALA B C    1 
ATOM   9867  O  O    . ALA B 1 291 ? 8.782   23.442  28.715  1.00 11.03  ?  514  ALA B O    1 
ATOM   9868  C  CB   . ALA B 1 291 ? 11.388  24.817  29.711  1.00 13.18  ?  514  ALA B CB   1 
ATOM   9869  H  H    . ALA B 1 291 ? 10.353  26.783  30.701  1.00 13.17  ?  514  ALA B H    1 
ATOM   9870  H  HA   . ALA B 1 291 ? 10.021  25.600  28.401  1.00 14.05  ?  514  ALA B HA   1 
ATOM   9871  H  HB1  . ALA B 1 291 ? 11.542  24.006  29.201  1.00 15.82  ?  514  ALA B HB1  1 
ATOM   9872  H  HB2  . ALA B 1 291 ? 12.067  25.476  29.498  1.00 15.82  ?  514  ALA B HB2  1 
ATOM   9873  H  HB3  . ALA B 1 291 ? 11.406  24.619  30.660  1.00 15.82  ?  514  ALA B HB3  1 
ATOM   9874  N  N    . ASN B 1 292 ? 8.222   24.369  30.678  1.00 10.04  ?  515  ASN B N    1 
ATOM   9875  C  CA   . ASN B 1 292 ? 7.182   23.383  30.938  1.00 9.96   ?  515  ASN B CA   1 
ATOM   9876  C  C    . ASN B 1 292 ? 5.836   23.733  30.303  1.00 9.89   ?  515  ASN B C    1 
ATOM   9877  O  O    . ASN B 1 292 ? 4.863   23.008  30.521  1.00 10.91  ?  515  ASN B O    1 
ATOM   9878  C  CB   . ASN B 1 292 ? 7.013   23.165  32.444  1.00 10.89  ?  515  ASN B CB   1 
ATOM   9879  C  CG   . ASN B 1 292 ? 6.365   24.348  33.160  1.00 11.22  ?  515  ASN B CG   1 
ATOM   9880  O  OD1  . ASN B 1 292 ? 5.986   25.349  32.548  1.00 11.32  ?  515  ASN B OD1  1 
ATOM   9881  N  ND2  . ASN B 1 292 ? 6.190   24.207  34.466  1.00 12.62  ?  515  ASN B ND2  1 
ATOM   9882  H  H    . ASN B 1 292 ? 8.313   24.961  31.295  1.00 12.05  ?  515  ASN B H    1 
ATOM   9883  H  HA   . ASN B 1 292 ? 7.468   22.539  30.554  1.00 11.96  ?  515  ASN B HA   1 
ATOM   9884  H  HB2  . ASN B 1 292 ? 6.451   22.387  32.587  1.00 13.07  ?  515  ASN B HB2  1 
ATOM   9885  H  HB3  . ASN B 1 292 ? 7.887   23.020  32.840  1.00 13.07  ?  515  ASN B HB3  1 
ATOM   9886  H  HD21 . ASN B 1 292 ? 5.829   24.841  34.922  1.00 15.14  ?  515  ASN B HD21 1 
ATOM   9887  H  HD22 . ASN B 1 292 ? 6.436   23.482  34.857  1.00 15.14  ?  515  ASN B HD22 1 
ATOM   9888  N  N    . GLY B 1 293 ? 5.742   24.815  29.548  1.00 9.19   ?  516  GLY B N    1 
ATOM   9889  C  CA   . GLY B 1 293 ? 4.455   25.291  29.091  1.00 7.72   ?  516  GLY B CA   1 
ATOM   9890  C  C    . GLY B 1 293 ? 3.901   24.535  27.896  1.00 6.92   ?  516  GLY B C    1 
ATOM   9891  O  O    . GLY B 1 293 ? 4.617   23.910  27.108  1.00 7.71   ?  516  GLY B O    1 
ATOM   9892  H  H    . GLY B 1 293 ? 6.410   25.290  29.287  1.00 11.02  ?  516  GLY B H    1 
ATOM   9893  H  HA2  . GLY B 1 293 ? 3.816   25.212  29.816  1.00 9.27   ?  516  GLY B HA2  1 
ATOM   9894  H  HA3  . GLY B 1 293 ? 4.537   26.225  28.841  1.00 9.27   ?  516  GLY B HA3  1 
ATOM   9895  N  N    . TYR B 1 294 ? 2.577   24.602  27.753  1.00 6.87   ?  517  TYR B N    1 
ATOM   9896  C  CA   . TYR B 1 294 ? 1.924   24.007  26.597  1.00 6.52   ?  517  TYR B CA   1 
ATOM   9897  C  C    . TYR B 1 294 ? 0.586   24.687  26.374  1.00 6.55   ?  517  TYR B C    1 
ATOM   9898  O  O    . TYR B 1 294 ? 0.025   25.308  27.274  1.00 7.23   ?  517  TYR B O    1 
ATOM   9899  C  CB   . TYR B 1 294 ? 1.745   22.491  26.750  1.00 7.43   ?  517  TYR B CB   1 
ATOM   9900  C  CG   . TYR B 1 294 ? 0.920   22.074  27.948  1.00 8.97   ?  517  TYR B CG   1 
ATOM   9901  C  CD1  . TYR B 1 294 ? -0.470  22.028  27.892  1.00 9.22   ?  517  TYR B CD1  1 
ATOM   9902  C  CD2  . TYR B 1 294 ? 1.538   21.704  29.135  1.00 11.46  ?  517  TYR B CD2  1 
ATOM   9903  C  CE1  . TYR B 1 294 ? -1.221  21.647  28.994  1.00 11.08  ?  517  TYR B CE1  1 
ATOM   9904  C  CE2  . TYR B 1 294 ? 0.804   21.311  30.229  1.00 12.17  ?  517  TYR B CE2  1 
ATOM   9905  C  CZ   . TYR B 1 294 ? -0.577  21.284  30.158  1.00 12.80  ?  517  TYR B CZ   1 
ATOM   9906  O  OH   . TYR B 1 294 ? -1.308  20.896  31.262  1.00 15.87  ?  517  TYR B OH   1 
ATOM   9907  H  H    . TYR B 1 294 ? 2.043   24.983  28.309  1.00 8.25   ?  517  TYR B H    1 
ATOM   9908  H  HA   . TYR B 1 294 ? 2.476   24.165  25.816  1.00 7.82   ?  517  TYR B HA   1 
ATOM   9909  H  HB2  . TYR B 1 294 ? 1.302   22.151  25.957  1.00 8.91   ?  517  TYR B HB2  1 
ATOM   9910  H  HB3  . TYR B 1 294 ? 2.620   22.084  26.842  1.00 8.91   ?  517  TYR B HB3  1 
ATOM   9911  H  HD1  . TYR B 1 294 ? -0.904  22.256  27.102  1.00 11.07  ?  517  TYR B HD1  1 
ATOM   9912  H  HD2  . TYR B 1 294 ? 2.466   21.723  29.192  1.00 13.75  ?  517  TYR B HD2  1 
ATOM   9913  H  HE1  . TYR B 1 294 ? -2.150  21.636  28.949  1.00 13.29  ?  517  TYR B HE1  1 
ATOM   9914  H  HE2  . TYR B 1 294 ? 1.235   21.064  31.015  1.00 14.60  ?  517  TYR B HE2  1 
ATOM   9915  H  HH   . TYR B 1 294 ? -2.129  20.929  31.088  1.00 19.04  ?  517  TYR B HH   1 
ATOM   9916  N  N    . PHE B 1 295 ? 0.090   24.573  25.152  1.00 6.51   ?  518  PHE B N    1 
ATOM   9917  C  CA   . PHE B 1 295 ? -1.216  25.101  24.810  1.00 6.22   ?  518  PHE B CA   1 
ATOM   9918  C  C    . PHE B 1 295 ? -2.341  24.169  25.239  1.00 6.87   ?  518  PHE B C    1 
ATOM   9919  O  O    . PHE B 1 295 ? -2.251  22.945  25.106  1.00 8.44   ?  518  PHE B O    1 
ATOM   9920  C  CB   . PHE B 1 295 ? -1.310  25.303  23.299  1.00 6.37   ?  518  PHE B CB   1 
ATOM   9921  C  CG   . PHE B 1 295 ? -0.695  26.572  22.802  1.00 6.63   ?  518  PHE B CG   1 
ATOM   9922  C  CD1  . PHE B 1 295 ? -1.267  27.788  23.133  1.00 7.05   ?  518  PHE B CD1  1 
ATOM   9923  C  CD2  . PHE B 1 295 ? 0.419   26.562  21.976  1.00 7.17   ?  518  PHE B CD2  1 
ATOM   9924  C  CE1  . PHE B 1 295 ? -0.732  28.958  22.664  1.00 8.36   ?  518  PHE B CE1  1 
ATOM   9925  C  CE2  . PHE B 1 295 ? 0.946   27.739  21.498  1.00 7.63   ?  518  PHE B CE2  1 
ATOM   9926  C  CZ   . PHE B 1 295 ? 0.365   28.936  21.847  1.00 7.97   ?  518  PHE B CZ   1 
ATOM   9927  H  H    . PHE B 1 295 ? 0.495   24.189  24.497  1.00 7.81   ?  518  PHE B H    1 
ATOM   9928  H  HA   . PHE B 1 295 ? -1.332  25.946  25.271  1.00 7.46   ?  518  PHE B HA   1 
ATOM   9929  H  HB2  . PHE B 1 295 ? -0.856  24.567  22.861  1.00 7.65   ?  518  PHE B HB2  1 
ATOM   9930  H  HB3  . PHE B 1 295 ? -2.247  25.314  23.047  1.00 7.65   ?  518  PHE B HB3  1 
ATOM   9931  H  HD1  . PHE B 1 295 ? -2.021  27.810  23.677  1.00 8.46   ?  518  PHE B HD1  1 
ATOM   9932  H  HD2  . PHE B 1 295 ? 0.812   25.753  21.743  1.00 8.61   ?  518  PHE B HD2  1 
ATOM   9933  H  HE1  . PHE B 1 295 ? -1.117  29.771  22.902  1.00 10.03  ?  518  PHE B HE1  1 
ATOM   9934  H  HE2  . PHE B 1 295 ? 1.691   27.726  20.941  1.00 9.15   ?  518  PHE B HE2  1 
ATOM   9935  H  HZ   . PHE B 1 295 ? 0.720   29.734  21.527  1.00 9.57   ?  518  PHE B HZ   1 
ATOM   9936  N  N    . ARG B 1 296 ? -3.427  24.779  25.699  1.00 7.32   ?  519  ARG B N    1 
ATOM   9937  C  CA   . ARG B 1 296 ? -4.637  24.107  26.143  1.00 7.89   ?  519  ARG B CA   1 
ATOM   9938  C  C    . ARG B 1 296 ? -5.821  24.728  25.417  1.00 7.21   ?  519  ARG B C    1 
ATOM   9939  O  O    . ARG B 1 296 ? -5.966  25.954  25.378  1.00 8.04   ?  519  ARG B O    1 
ATOM   9940  C  CB   . ARG B 1 296 ? -4.784  24.303  27.652  1.00 10.56  ?  519  ARG B CB   1 
ATOM   9941  C  CG   . ARG B 1 296 ? -5.979  23.659  28.320  1.00 13.04  ?  519  ARG B CG   1 
ATOM   9942  C  CD   . ARG B 1 296 ? -6.059  24.127  29.785  1.00 15.66  ?  519  ARG B CD   1 
ATOM   9943  N  NE   . ARG B 1 296 ? -6.471  25.523  29.871  1.00 18.91  ?  519  ARG B NE   1 
ATOM   9944  C  CZ   . ARG B 1 296 ? -6.334  26.299  30.938  1.00 22.26  ?  519  ARG B CZ   1 
ATOM   9945  N  NH1  . ARG B 1 296 ? -5.758  25.859  32.047  1.00 22.64  ?  519  ARG B NH1  1 
ATOM   9946  N  NH2  . ARG B 1 296 ? -6.788  27.551  30.890  1.00 23.89  ?  519  ARG B NH2  1 
ATOM   9947  H  H    . ARG B 1 296 ? -3.489  25.634  25.767  1.00 8.78   ?  519  ARG B H    1 
ATOM   9948  H  HA   . ARG B 1 296 ? -4.615  23.159  25.936  1.00 9.47   ?  519  ARG B HA   1 
ATOM   9949  H  HB2  . ARG B 1 296 ? -3.993  23.939  28.079  1.00 12.67  ?  519  ARG B HB2  1 
ATOM   9950  H  HB3  . ARG B 1 296 ? -4.846  25.256  27.824  1.00 12.67  ?  519  ARG B HB3  1 
ATOM   9951  H  HG2  . ARG B 1 296 ? -6.793  23.920  27.862  1.00 15.65  ?  519  ARG B HG2  1 
ATOM   9952  H  HG3  . ARG B 1 296 ? -5.884  22.693  28.304  1.00 15.65  ?  519  ARG B HG3  1 
ATOM   9953  H  HD2  . ARG B 1 296 ? -6.708  23.585  30.261  1.00 18.80  ?  519  ARG B HD2  1 
ATOM   9954  H  HD3  . ARG B 1 296 ? -5.186  24.039  30.199  1.00 18.80  ?  519  ARG B HD3  1 
ATOM   9955  H  HE   . ARG B 1 296 ? -6.834  25.872  29.173  1.00 22.69  ?  519  ARG B HE   1 
ATOM   9956  H  HH11 . ARG B 1 296 ? -5.463  25.052  32.086  1.00 27.17  ?  519  ARG B HH11 1 
ATOM   9957  H  HH12 . ARG B 1 296 ? -5.679  26.379  32.726  1.00 27.17  ?  519  ARG B HH12 1 
ATOM   9958  H  HH21 . ARG B 1 296 ? -7.164  27.845  30.174  1.00 28.67  ?  519  ARG B HH21 1 
ATOM   9959  H  HH22 . ARG B 1 296 ? -6.705  28.065  31.574  1.00 28.67  ?  519  ARG B HH22 1 
ATOM   9960  N  N    . PHE B 1 297 ? -6.678  23.886  24.853  1.00 7.13   ?  520  PHE B N    1 
ATOM   9961  C  CA   . PHE B 1 297 ? -7.916  24.366  24.265  1.00 7.60   ?  520  PHE B CA   1 
ATOM   9962  C  C    . PHE B 1 297 ? -8.813  24.957  25.345  1.00 8.94   ?  520  PHE B C    1 
ATOM   9963  O  O    . PHE B 1 297 ? -9.011  24.353  26.398  1.00 12.33  ?  520  PHE B O    1 
ATOM   9964  C  CB   . PHE B 1 297 ? -8.634  23.207  23.583  1.00 9.42   ?  520  PHE B CB   1 
ATOM   9965  C  CG   . PHE B 1 297 ? -10.024 23.560  23.132  1.00 10.93  ?  520  PHE B CG   1 
ATOM   9966  C  CD1  . PHE B 1 297 ? -10.211 24.290  21.986  1.00 10.84  ?  520  PHE B CD1  1 
ATOM   9967  C  CD2  . PHE B 1 297 ? -11.140 23.208  23.875  1.00 12.83  ?  520  PHE B CD2  1 
ATOM   9968  C  CE1  . PHE B 1 297 ? -11.479 24.640  21.565  1.00 11.24  ?  520  PHE B CE1  1 
ATOM   9969  C  CE2  . PHE B 1 297 ? -12.402 23.568  23.456  1.00 13.62  ?  520  PHE B CE2  1 
ATOM   9970  C  CZ   . PHE B 1 297 ? -12.563 24.278  22.295  1.00 12.02  ?  520  PHE B CZ   1 
ATOM   9971  H  H    . PHE B 1 297 ? -6.564  23.036  24.798  1.00 8.55   ?  520  PHE B H    1 
ATOM   9972  H  HA   . PHE B 1 297 ? -7.723  25.053  23.608  1.00 9.13   ?  520  PHE B HA   1 
ATOM   9973  H  HB2  . PHE B 1 297 ? -8.126  22.938  22.802  1.00 11.31  ?  520  PHE B HB2  1 
ATOM   9974  H  HB3  . PHE B 1 297 ? -8.701  22.467  24.206  1.00 11.31  ?  520  PHE B HB3  1 
ATOM   9975  H  HD1  . PHE B 1 297 ? -9.473  24.552  21.485  1.00 13.01  ?  520  PHE B HD1  1 
ATOM   9976  H  HD2  . PHE B 1 297 ? -11.036 22.725  24.663  1.00 15.40  ?  520  PHE B HD2  1 
ATOM   9977  H  HE1  . PHE B 1 297 ? -11.590 25.126  20.780  1.00 13.49  ?  520  PHE B HE1  1 
ATOM   9978  H  HE2  . PHE B 1 297 ? -13.146 23.329  23.961  1.00 16.34  ?  520  PHE B HE2  1 
ATOM   9979  H  HZ   . PHE B 1 297 ? -13.416 24.511  22.007  1.00 14.43  ?  520  PHE B HZ   1 
ATOM   9980  N  N    . ASP B 1 298 ? -9.365  26.137  25.088  1.00 8.22   ?  521  ASP B N    1 
ATOM   9981  C  CA   A ASP B 1 298 ? -10.283 26.828  25.997  0.52 9.02   ?  521  ASP B CA   1 
ATOM   9982  C  CA   B ASP B 1 298 ? -10.314 26.679  26.039  0.48 10.07  ?  521  ASP B CA   1 
ATOM   9983  C  C    . ASP B 1 298 ? -11.725 26.808  25.510  1.00 9.51   ?  521  ASP B C    1 
ATOM   9984  O  O    . ASP B 1 298 ? -12.644 26.411  26.231  1.00 11.23  ?  521  ASP B O    1 
ATOM   9985  C  CB   A ASP B 1 298 ? -9.849  28.301  26.150  0.52 8.93   ?  521  ASP B CB   1 
ATOM   9986  C  CB   B ASP B 1 298 ? -9.792  27.961  26.674  0.48 11.85  ?  521  ASP B CB   1 
ATOM   9987  C  CG   A ASP B 1 298 ? -10.730 29.083  27.125  0.52 9.80   ?  521  ASP B CG   1 
ATOM   9988  C  CG   B ASP B 1 298 ? -8.791  27.659  27.777  0.48 13.15  ?  521  ASP B CG   1 
ATOM   9989  O  OD1  A ASP B 1 298 ? -10.476 29.014  28.345  0.52 12.55  ?  521  ASP B OD1  1 
ATOM   9990  O  OD1  B ASP B 1 298 ? -8.617  26.448  28.083  0.48 13.62  -1 521  ASP B OD1  1 
ATOM   9991  O  OD2  A ASP B 1 298 ? -11.674 29.766  26.671  0.52 9.43   -1 521  ASP B OD2  1 
ATOM   9992  O  OD2  B ASP B 1 298 ? -8.186  28.599  28.329  0.48 14.25  -1 521  ASP B OD2  1 
ATOM   9993  H  H    A ASP B 1 298 ? -9.219  26.579  24.365  0.52 9.87   ?  521  ASP B H    1 
ATOM   9994  H  H    B ASP B 1 298 ? -9.208  26.621  24.395  0.48 9.87   ?  521  ASP B H    1 
ATOM   9995  H  HA   A ASP B 1 298 ? -10.243 26.390  26.861  0.52 10.82  ?  521  ASP B HA   1 
ATOM   9996  H  HA   B ASP B 1 298 ? -10.393 26.064  26.785  0.48 12.08  ?  521  ASP B HA   1 
ATOM   9997  H  HB2  A ASP B 1 298 ? -8.938  28.329  26.481  0.52 10.72  ?  521  ASP B HB2  1 
ATOM   9998  H  HB2  B ASP B 1 298 ? -9.350  28.498  25.998  0.48 14.22  ?  521  ASP B HB2  1 
ATOM   9999  H  HB3  A ASP B 1 298 ? -9.900  28.737  25.284  0.52 10.72  ?  521  ASP B HB3  1 
ATOM   10000 H  HB3  B ASP B 1 298 ? -10.532 28.455  27.058  0.48 14.22  ?  521  ASP B HB3  1 
ATOM   10001 N  N    . SER B 1 299 ? -11.943 27.263  24.279  1.00 8.52   ?  522  SER B N    1 
ATOM   10002 C  CA   . SER B 1 299 ? -13.303 27.446  23.804  1.00 9.64   ?  522  SER B CA   1 
ATOM   10003 C  C    . SER B 1 299 ? -13.286 27.706  22.306  1.00 8.77   ?  522  SER B C    1 
ATOM   10004 O  O    . SER B 1 299 ? -12.255 28.036  21.724  1.00 9.09   ?  522  SER B O    1 
ATOM   10005 C  CB   . SER B 1 299 ? -14.001 28.600  24.535  1.00 10.99  ?  522  SER B CB   1 
ATOM   10006 O  OG   . SER B 1 299 ? -13.259 29.792  24.391  1.00 12.25  ?  522  SER B OG   1 
ATOM   10007 H  H    . SER B 1 299 ? -11.329 27.467  23.713  1.00 10.23  ?  522  SER B H    1 
ATOM   10008 H  HA   . SER B 1 299 ? -13.800 26.628  23.957  1.00 11.57  ?  522  SER B HA   1 
ATOM   10009 H  HB2  . SER B 1 299 ? -14.885 28.728  24.155  1.00 13.19  ?  522  SER B HB2  1 
ATOM   10010 H  HB3  . SER B 1 299 ? -14.073 28.382  25.477  1.00 13.19  ?  522  SER B HB3  1 
ATOM   10011 H  HG   . SER B 1 299 ? -12.487 29.688  24.704  1.00 14.70  ?  522  SER B HG   1 
ATOM   10012 N  N    . TRP B 1 300 ? -14.452 27.570  21.702  1.00 8.92   ?  523  TRP B N    1 
ATOM   10013 C  CA   . TRP B 1 300 ? -14.645 27.847  20.287  1.00 8.56   ?  523  TRP B CA   1 
ATOM   10014 C  C    . TRP B 1 300 ? -15.066 29.294  20.105  1.00 9.63   ?  523  TRP B C    1 
ATOM   10015 O  O    . TRP B 1 300 ? -16.027 29.746  20.734  1.00 11.41  ?  523  TRP B O    1 
ATOM   10016 C  CB   . TRP B 1 300 ? -15.710 26.916  19.717  1.00 9.01   ?  523  TRP B CB   1 
ATOM   10017 C  CG   . TRP B 1 300 ? -15.294 25.483  19.715  1.00 8.57   ?  523  TRP B CG   1 
ATOM   10018 C  CD1  . TRP B 1 300 ? -15.739 24.485  20.543  1.00 9.73   ?  523  TRP B CD1  1 
ATOM   10019 C  CD2  . TRP B 1 300 ? -14.344 24.872  18.829  1.00 8.33   ?  523  TRP B CD2  1 
ATOM   10020 N  NE1  . TRP B 1 300 ? -15.124 23.295  20.219  1.00 10.09  ?  523  TRP B NE1  1 
ATOM   10021 C  CE2  . TRP B 1 300 ? -14.259 23.508  19.177  1.00 9.36   ?  523  TRP B CE2  1 
ATOM   10022 C  CE3  . TRP B 1 300 ? -13.562 25.346  17.774  1.00 8.72   ?  523  TRP B CE3  1 
ATOM   10023 C  CZ2  . TRP B 1 300 ? -13.428 22.622  18.507  1.00 9.57   ?  523  TRP B CZ2  1 
ATOM   10024 C  CZ3  . TRP B 1 300 ? -12.732 24.461  17.108  1.00 9.10   ?  523  TRP B CZ3  1 
ATOM   10025 C  CH2  . TRP B 1 300 ? -12.663 23.113  17.488  1.00 9.13   ?  523  TRP B CH2  1 
ATOM   10026 H  H    . TRP B 1 300 ? -15.169 27.311  22.099  1.00 10.71  ?  523  TRP B H    1 
ATOM   10027 H  HA   . TRP B 1 300 ? -13.815 27.705  19.804  1.00 10.28  ?  523  TRP B HA   1 
ATOM   10028 H  HB2  . TRP B 1 300 ? -16.514 26.993  20.254  1.00 10.81  ?  523  TRP B HB2  1 
ATOM   10029 H  HB3  . TRP B 1 300 ? -15.896 27.175  18.801  1.00 10.81  ?  523  TRP B HB3  1 
ATOM   10030 H  HD1  . TRP B 1 300 ? -16.363 24.595  21.223  1.00 11.67  ?  523  TRP B HD1  1 
ATOM   10031 H  HE1  . TRP B 1 300 ? -15.261 22.540  20.608  1.00 12.11  ?  523  TRP B HE1  1 
ATOM   10032 H  HE3  . TRP B 1 300 ? -13.598 26.241  17.523  1.00 10.47  ?  523  TRP B HE3  1 
ATOM   10033 H  HZ2  . TRP B 1 300 ? -13.393 21.723  18.744  1.00 11.48  ?  523  TRP B HZ2  1 
ATOM   10034 H  HZ3  . TRP B 1 300 ? -12.214 24.764  16.398  1.00 10.92  ?  523  TRP B HZ3  1 
ATOM   10035 H  HH2  . TRP B 1 300 ? -12.084 22.542  17.037  1.00 10.96  ?  523  TRP B HH2  1 
ATOM   10036 N  N    . VAL B 1 301 ? -14.338 30.019  19.255  1.00 8.84   ?  524  VAL B N    1 
ATOM   10037 C  CA   . VAL B 1 301 ? -14.617 31.425  18.969  1.00 9.31   ?  524  VAL B CA   1 
ATOM   10038 C  C    . VAL B 1 301 ? -14.718 31.610  17.454  1.00 8.79   ?  524  VAL B C    1 
ATOM   10039 O  O    . VAL B 1 301 ? -15.014 30.660  16.721  1.00 10.02  ?  524  VAL B O    1 
ATOM   10040 C  CB   . VAL B 1 301 ? -13.585 32.350  19.647  1.00 9.35   ?  524  VAL B CB   1 
ATOM   10041 C  CG1  . VAL B 1 301 ? -13.625 32.171  21.171  1.00 10.99  ?  524  VAL B CG1  1 
ATOM   10042 C  CG2  . VAL B 1 301 ? -12.173 32.128  19.128  1.00 9.44   ?  524  VAL B CG2  1 
ATOM   10043 H  H    . VAL B 1 301 ? -13.661 29.711  18.823  1.00 10.60  ?  524  VAL B H    1 
ATOM   10044 H  HA   . VAL B 1 301 ? -15.480 31.677  19.334  1.00 11.18  ?  524  VAL B HA   1 
ATOM   10045 H  HB   . VAL B 1 301 ? -13.826 33.263  19.426  1.00 11.23  ?  524  VAL B HB   1 
ATOM   10046 H  HG11 . VAL B 1 301 ? -13.005 32.796  21.579  1.00 13.19  ?  524  VAL B HG11 1 
ATOM   10047 H  HG12 . VAL B 1 301 ? -14.526 32.346  21.485  1.00 13.19  ?  524  VAL B HG12 1 
ATOM   10048 H  HG13 . VAL B 1 301 ? -13.369 31.262  21.389  1.00 13.19  ?  524  VAL B HG13 1 
ATOM   10049 H  HG21 . VAL B 1 301 ? -11.563 32.704  19.616  1.00 11.33  ?  524  VAL B HG21 1 
ATOM   10050 H  HG22 . VAL B 1 301 ? -11.930 31.199  19.263  1.00 11.33  ?  524  VAL B HG22 1 
ATOM   10051 H  HG23 . VAL B 1 301 ? -12.146 32.344  18.183  1.00 11.33  ?  524  VAL B HG23 1 
ATOM   10052 N  N    . ASN B 1 302 ? -14.526 32.830  16.958  1.00 9.14   ?  525  ASN B N    1 
ATOM   10053 C  CA   . ASN B 1 302 ? -14.510 33.038  15.509  1.00 9.54   ?  525  ASN B CA   1 
ATOM   10054 C  C    . ASN B 1 302 ? -13.346 33.956  15.149  1.00 8.74   ?  525  ASN B C    1 
ATOM   10055 O  O    . ASN B 1 302 ? -12.565 34.381  16.005  1.00 8.99   ?  525  ASN B O    1 
ATOM   10056 C  CB   . ASN B 1 302 ? -15.868 33.512  14.957  1.00 10.46  ?  525  ASN B CB   1 
ATOM   10057 C  CG   . ASN B 1 302 ? -16.245 34.906  15.417  1.00 12.22  ?  525  ASN B CG   1 
ATOM   10058 O  OD1  . ASN B 1 302 ? -15.389 35.703  15.767  1.00 12.72  ?  525  ASN B OD1  1 
ATOM   10059 N  ND2  . ASN B 1 302 ? -17.530 35.215  15.372  1.00 14.87  ?  525  ASN B ND2  1 
ATOM   10060 H  H    . ASN B 1 302 ? -14.406 33.539  17.429  1.00 10.97  ?  525  ASN B H    1 
ATOM   10061 H  HA   . ASN B 1 302 ? -14.339 32.185  15.079  1.00 11.45  ?  525  ASN B HA   1 
ATOM   10062 H  HB2  . ASN B 1 302 ? -15.829 33.518  13.988  1.00 12.55  ?  525  ASN B HB2  1 
ATOM   10063 H  HB3  . ASN B 1 302 ? -16.560 32.902  15.258  1.00 12.55  ?  525  ASN B HB3  1 
ATOM   10064 H  HD21 . ASN B 1 302 ? -17.794 35.994  15.623  1.00 17.85  ?  525  ASN B HD21 1 
ATOM   10065 H  HD22 . ASN B 1 302 ? -18.102 34.637  15.093  1.00 17.85  ?  525  ASN B HD22 1 
ATOM   10066 N  N    . GLN B 1 303 ? -13.220 34.255  13.853  1.00 8.63   ?  526  GLN B N    1 
ATOM   10067 C  CA   . GLN B 1 303 ? -12.077 35.014  13.369  1.00 9.52   ?  526  GLN B CA   1 
ATOM   10068 C  C    . GLN B 1 303 ? -12.051 36.441  13.893  1.00 10.37  ?  526  GLN B C    1 
ATOM   10069 O  O    . GLN B 1 303 ? -11.009 37.097  13.807  1.00 11.95  ?  526  GLN B O    1 
ATOM   10070 C  CB   . GLN B 1 303 ? -12.073 35.038  11.843  1.00 9.55   ?  526  GLN B CB   1 
ATOM   10071 C  CG   . GLN B 1 303 ? -13.280 35.733  11.247  1.00 10.28  ?  526  GLN B CG   1 
ATOM   10072 C  CD   . GLN B 1 303 ? -13.135 35.927  9.757   1.00 11.74  ?  526  GLN B CD   1 
ATOM   10073 O  OE1  . GLN B 1 303 ? -12.143 36.504  9.286   1.00 13.58  ?  526  GLN B OE1  1 
ATOM   10074 N  NE2  . GLN B 1 303 ? -14.104 35.446  9.004   1.00 12.34  ?  526  GLN B NE2  1 
ATOM   10075 H  H    . GLN B 1 303 ? -13.781 34.030  13.241  1.00 10.36  ?  526  GLN B H    1 
ATOM   10076 H  HA   . GLN B 1 303 ? -11.270 34.569  13.673  1.00 11.43  ?  526  GLN B HA   1 
ATOM   10077 H  HB2  . GLN B 1 303 ? -11.280 35.508  11.539  1.00 11.47  ?  526  GLN B HB2  1 
ATOM   10078 H  HB3  . GLN B 1 303 ? -12.063 34.126  11.515  1.00 11.47  ?  526  GLN B HB3  1 
ATOM   10079 H  HG2  . GLN B 1 303 ? -14.070 35.195  11.408  1.00 12.34  ?  526  GLN B HG2  1 
ATOM   10080 H  HG3  . GLN B 1 303 ? -13.382 36.605  11.659  1.00 12.34  ?  526  GLN B HG3  1 
ATOM   10081 H  HE21 . GLN B 1 303 ? -14.773 35.046  9.367   1.00 14.81  ?  526  GLN B HE21 1 
ATOM   10082 H  HE22 . GLN B 1 303 ? -14.066 35.532  8.149   1.00 14.81  ?  526  GLN B HE22 1 
ATOM   10083 N  N    . PHE B 1 304 ? -13.166 36.937  14.421  1.00 10.90  ?  527  PHE B N    1 
ATOM   10084 C  CA   . PHE B 1 304 ? -13.252 38.302  14.923  1.00 12.06  ?  527  PHE B CA   1 
ATOM   10085 C  C    . PHE B 1 304 ? -12.990 38.409  16.419  1.00 12.00  ?  527  PHE B C    1 
ATOM   10086 O  O    . PHE B 1 304 ? -13.117 39.504  16.972  1.00 13.13  ?  527  PHE B O    1 
ATOM   10087 C  CB   . PHE B 1 304 ? -14.608 38.897  14.546  1.00 13.26  ?  527  PHE B CB   1 
ATOM   10088 C  CG   . PHE B 1 304 ? -14.868 38.836  13.076  1.00 13.76  ?  527  PHE B CG   1 
ATOM   10089 C  CD1  . PHE B 1 304 ? -14.050 39.521  12.194  1.00 14.96  ?  527  PHE B CD1  1 
ATOM   10090 C  CD2  . PHE B 1 304 ? -15.888 38.048  12.564  1.00 14.34  ?  527  PHE B CD2  1 
ATOM   10091 C  CE1  . PHE B 1 304 ? -14.257 39.442  10.829  1.00 15.93  ?  527  PHE B CE1  1 
ATOM   10092 C  CE2  . PHE B 1 304 ? -16.102 37.969  11.194  1.00 15.10  ?  527  PHE B CE2  1 
ATOM   10093 C  CZ   . PHE B 1 304 ? -15.288 38.667  10.326  1.00 15.70  ?  527  PHE B CZ   1 
ATOM   10094 H  H    . PHE B 1 304 ? -13.898 36.494  14.499  1.00 13.08  ?  527  PHE B H    1 
ATOM   10095 H  HA   . PHE B 1 304 ? -12.571 38.843  14.494  1.00 14.47  ?  527  PHE B HA   1 
ATOM   10096 H  HB2  . PHE B 1 304 ? -15.308 38.400  14.997  1.00 15.91  ?  527  PHE B HB2  1 
ATOM   10097 H  HB3  . PHE B 1 304 ? -14.632 39.827  14.819  1.00 15.91  ?  527  PHE B HB3  1 
ATOM   10098 H  HD1  . PHE B 1 304 ? -13.352 40.040  12.524  1.00 17.95  ?  527  PHE B HD1  1 
ATOM   10099 H  HD2  . PHE B 1 304 ? -16.434 37.567  13.144  1.00 17.21  ?  527  PHE B HD2  1 
ATOM   10100 H  HE1  . PHE B 1 304 ? -13.702 39.910  10.248  1.00 19.12  ?  527  PHE B HE1  1 
ATOM   10101 H  HE2  . PHE B 1 304 ? -16.794 37.445  10.862  1.00 18.12  ?  527  PHE B HE2  1 
ATOM   10102 H  HZ   . PHE B 1 304 ? -15.432 38.618  9.409   1.00 18.84  ?  527  PHE B HZ   1 
ATOM   10103 N  N    . TYR B 1 305 ? -12.593 37.321  17.069  1.00 11.38  ?  528  TYR B N    1 
ATOM   10104 C  CA   . TYR B 1 305 ? -12.268 37.380  18.487  1.00 10.68  ?  528  TYR B CA   1 
ATOM   10105 C  C    . TYR B 1 305 ? -11.050 38.273  18.685  1.00 10.36  ?  528  TYR B C    1 
ATOM   10106 O  O    . TYR B 1 305 ? -10.046 38.141  17.983  1.00 11.16  ?  528  TYR B O    1 
ATOM   10107 C  CB   . TYR B 1 305 ? -11.971 35.969  19.024  1.00 10.46  ?  528  TYR B CB   1 
ATOM   10108 C  CG   . TYR B 1 305 ? -11.850 35.912  20.533  1.00 11.18  ?  528  TYR B CG   1 
ATOM   10109 C  CD1  . TYR B 1 305 ? -12.973 35.730  21.325  1.00 13.19  ?  528  TYR B CD1  1 
ATOM   10110 C  CD2  . TYR B 1 305 ? -10.618 36.058  21.159  1.00 11.54  ?  528  TYR B CD2  1 
ATOM   10111 C  CE1  . TYR B 1 305 ? -12.883 35.706  22.695  1.00 14.07  ?  528  TYR B CE1  1 
ATOM   10112 C  CE2  . TYR B 1 305 ? -10.517 36.027  22.535  1.00 12.86  ?  528  TYR B CE2  1 
ATOM   10113 C  CZ   . TYR B 1 305 ? -11.657 35.842  23.288  1.00 14.32  ?  528  TYR B CZ   1 
ATOM   10114 O  OH   . TYR B 1 305 ? -11.600 35.821  24.651  1.00 16.04  ?  528  TYR B OH   1 
ATOM   10115 H  H    . TYR B 1 305 ? -12.505 36.542  16.715  1.00 13.65  ?  528  TYR B H    1 
ATOM   10116 H  HA   . TYR B 1 305 ? -13.019 37.741  18.983  1.00 12.82  ?  528  TYR B HA   1 
ATOM   10117 H  HB2  . TYR B 1 305 ? -12.692 35.376  18.761  1.00 12.56  ?  528  TYR B HB2  1 
ATOM   10118 H  HB3  . TYR B 1 305 ? -11.132 35.660  18.646  1.00 12.56  ?  528  TYR B HB3  1 
ATOM   10119 H  HD1  . TYR B 1 305 ? -13.803 35.623  20.921  1.00 15.83  ?  528  TYR B HD1  1 
ATOM   10120 H  HD2  . TYR B 1 305 ? -9.853  36.178  20.644  1.00 13.85  ?  528  TYR B HD2  1 
ATOM   10121 H  HE1  . TYR B 1 305 ? -13.647 35.598  23.214  1.00 16.88  ?  528  TYR B HE1  1 
ATOM   10122 H  HE2  . TYR B 1 305 ? -9.691  36.130  22.950  1.00 15.43  ?  528  TYR B HE2  1 
ATOM   10123 H  HH   . TYR B 1 305 ? -12.371 35.723  24.969  1.00 19.25  ?  528  TYR B HH   1 
ATOM   10124 N  N    . SER B 1 306 ? -11.120 39.164  19.669  1.00 9.61   ?  529  SER B N    1 
ATOM   10125 C  CA   A SER B 1 306 ? -10.033 40.092  19.953  0.40 9.76   ?  529  SER B CA   1 
ATOM   10126 C  CA   B SER B 1 306 ? -10.039 40.098  19.958  0.60 10.17  ?  529  SER B CA   1 
ATOM   10127 C  C    . SER B 1 306 ? -9.147  39.511  21.044  1.00 9.45   ?  529  SER B C    1 
ATOM   10128 O  O    . SER B 1 306 ? -9.529  39.472  22.217  1.00 11.51  ?  529  SER B O    1 
ATOM   10129 C  CB   A SER B 1 306 ? -10.594 41.443  20.370  0.40 10.47  ?  529  SER B CB   1 
ATOM   10130 C  CB   B SER B 1 306 ? -10.640 41.422  20.415  0.60 11.77  ?  529  SER B CB   1 
ATOM   10131 O  OG   A SER B 1 306 ? -11.205 42.073  19.264  0.40 11.66  ?  529  SER B OG   1 
ATOM   10132 O  OG   B SER B 1 306 ? -9.638  42.384  20.674  0.60 14.00  ?  529  SER B OG   1 
ATOM   10133 H  H    A SER B 1 306 ? -11.797 39.251  20.193  0.40 11.54  ?  529  SER B H    1 
ATOM   10134 H  H    B SER B 1 306 ? -11.797 39.248  20.193  0.60 11.54  ?  529  SER B H    1 
ATOM   10135 H  HA   A SER B 1 306 ? -9.490  40.202  19.157  0.40 11.72  ?  529  SER B HA   1 
ATOM   10136 H  HA   B SER B 1 306 ? -9.496  40.234  19.167  0.60 12.21  ?  529  SER B HA   1 
ATOM   10137 H  HB2  A SER B 1 306 ? -11.254 41.313  21.068  0.40 12.56  ?  529  SER B HB2  1 
ATOM   10138 H  HB2  B SER B 1 306 ? -11.224 41.758  19.717  0.60 14.12  ?  529  SER B HB2  1 
ATOM   10139 H  HB3  A SER B 1 306 ? -9.871  42.002  20.696  0.40 12.56  ?  529  SER B HB3  1 
ATOM   10140 H  HB3  B SER B 1 306 ? -11.148 41.272  21.228  0.60 14.12  ?  529  SER B HB3  1 
ATOM   10141 H  HG   A SER B 1 306 ? -11.505 42.825  19.491  0.40 13.99  ?  529  SER B HG   1 
ATOM   10142 H  HG   B SER B 1 306 ? -9.180  42.515  19.982  0.60 16.80  ?  529  SER B HG   1 
ATOM   10143 N  N    . LEU B 1 307 ? -7.962  39.066  20.657  1.00 8.71   ?  530  LEU B N    1 
ATOM   10144 C  CA   . LEU B 1 307 ? -7.046  38.474  21.608  1.00 8.91   ?  530  LEU B CA   1 
ATOM   10145 C  C    . LEU B 1 307 ? -6.419  39.529  22.512  1.00 9.82   ?  530  LEU B C    1 
ATOM   10146 O  O    . LEU B 1 307 ? -6.125  40.650  22.098  1.00 10.85  ?  530  LEU B O    1 
ATOM   10147 C  CB   . LEU B 1 307 ? -5.909  37.771  20.860  1.00 8.63   ?  530  LEU B CB   1 
ATOM   10148 C  CG   . LEU B 1 307 ? -6.269  36.504  20.078  1.00 8.22   ?  530  LEU B CG   1 
ATOM   10149 C  CD1  . LEU B 1 307 ? -5.119  36.116  19.179  1.00 8.10   ?  530  LEU B CD1  1 
ATOM   10150 C  CD2  . LEU B 1 307 ? -6.629  35.358  21.011  1.00 9.14   ?  530  LEU B CD2  1 
ATOM   10151 H  H    . LEU B 1 307 ? -7.667  39.096  19.850  1.00 10.46  ?  530  LEU B H    1 
ATOM   10152 H  HA   . LEU B 1 307 ? -7.536  37.840  22.155  1.00 10.69  ?  530  LEU B HA   1 
ATOM   10153 H  HB2  . LEU B 1 307 ? -5.537  38.401  20.222  1.00 10.35  ?  530  LEU B HB2  1 
ATOM   10154 H  HB3  . LEU B 1 307 ? -5.234  37.520  21.510  1.00 10.35  ?  530  LEU B HB3  1 
ATOM   10155 H  HG   . LEU B 1 307 ? -7.050  36.682  19.531  1.00 9.87   ?  530  LEU B HG   1 
ATOM   10156 H  HD11 . LEU B 1 307 ? -5.352  35.306  18.699  1.00 9.72   ?  530  LEU B HD11 1 
ATOM   10157 H  HD12 . LEU B 1 307 ? -4.952  36.836  18.552  1.00 9.72   ?  530  LEU B HD12 1 
ATOM   10158 H  HD13 . LEU B 1 307 ? -4.331  35.962  19.724  1.00 9.72   ?  530  LEU B HD13 1 
ATOM   10159 H  HD21 . LEU B 1 307 ? -6.889  34.589  20.481  1.00 10.96  ?  530  LEU B HD21 1 
ATOM   10160 H  HD22 . LEU B 1 307 ? -5.857  35.140  21.555  1.00 10.96  ?  530  LEU B HD22 1 
ATOM   10161 H  HD23 . LEU B 1 307 ? -7.367  35.633  21.578  1.00 10.96  ?  530  LEU B HD23 1 
ATOM   10162 N  N    . ALA B 1 308 ? -6.141  39.128  23.743  1.00 9.26   ?  531  ALA B N    1 
ATOM   10163 C  CA   . ALA B 1 308 ? -5.300  39.930  24.603  1.00 9.88   ?  531  ALA B CA   1 
ATOM   10164 C  C    . ALA B 1 308 ? -3.896  40.036  24.014  1.00 9.64   ?  531  ALA B C    1 
ATOM   10165 O  O    . ALA B 1 308 ? -3.363  39.060  23.474  1.00 8.74   ?  531  ALA B O    1 
ATOM   10166 C  CB   . ALA B 1 308 ? -5.214  39.277  25.979  1.00 10.88  ?  531  ALA B CB   1 
ATOM   10167 H  H    . ALA B 1 308 ? -6.427  38.400  24.099  1.00 11.11  ?  531  ALA B H    1 
ATOM   10168 H  HA   . ALA B 1 308 ? -5.672  40.822  24.687  1.00 11.86  ?  531  ALA B HA   1 
ATOM   10169 H  HB1  . ALA B 1 308 ? -4.645  39.818  26.550  1.00 13.06  ?  531  ALA B HB1  1 
ATOM   10170 H  HB2  . ALA B 1 308 ? -6.105  39.220  26.358  1.00 13.06  ?  531  ALA B HB2  1 
ATOM   10171 H  HB3  . ALA B 1 308 ? -4.837  38.388  25.883  1.00 13.06  ?  531  ALA B HB3  1 
ATOM   10172 N  N    . PRO B 1 309 ? -3.250  41.189  24.142  1.00 12.12  ?  532  PRO B N    1 
ATOM   10173 C  CA   . PRO B 1 309 ? -1.898  41.350  23.597  1.00 13.05  ?  532  PRO B CA   1 
ATOM   10174 C  C    . PRO B 1 309 ? -0.917  40.400  24.254  1.00 11.43  ?  532  PRO B C    1 
ATOM   10175 O  O    . PRO B 1 309 ? -0.826  40.318  25.479  1.00 13.77  ?  532  PRO B O    1 
ATOM   10176 C  CB   . PRO B 1 309 ? -1.562  42.807  23.930  1.00 15.68  ?  532  PRO B CB   1 
ATOM   10177 C  CG   . PRO B 1 309 ? -2.500  43.190  25.023  1.00 17.21  ?  532  PRO B CG   1 
ATOM   10178 C  CD   . PRO B 1 309 ? -3.734  42.404  24.829  1.00 15.35  ?  532  PRO B CD   1 
ATOM   10179 H  HA   . PRO B 1 309 ? -1.899  41.211  22.637  1.00 15.66  ?  532  PRO B HA   1 
ATOM   10180 H  HB2  . PRO B 1 309 ? -0.641  42.872  24.226  1.00 18.81  ?  532  PRO B HB2  1 
ATOM   10181 H  HB3  . PRO B 1 309 ? -1.699  43.363  23.147  1.00 18.81  ?  532  PRO B HB3  1 
ATOM   10182 H  HG2  . PRO B 1 309 ? -2.096  42.983  25.881  1.00 20.66  ?  532  PRO B HG2  1 
ATOM   10183 H  HG3  . PRO B 1 309 ? -2.690  44.140  24.967  1.00 20.66  ?  532  PRO B HG3  1 
ATOM   10184 H  HD2  . PRO B 1 309 ? -4.140  42.181  25.681  1.00 18.42  ?  532  PRO B HD2  1 
ATOM   10185 H  HD3  . PRO B 1 309 ? -4.368  42.885  24.275  1.00 18.42  ?  532  PRO B HD3  1 
ATOM   10186 N  N    . MET B 1 310 ? -0.175  39.680  23.431  1.00 9.32   ?  533  MET B N    1 
ATOM   10187 C  CA   . MET B 1 310 ? 0.852   38.790  23.932  1.00 10.85  ?  533  MET B CA   1 
ATOM   10188 C  C    . MET B 1 310 ? 2.080   39.607  24.320  1.00 11.73  ?  533  MET B C    1 
ATOM   10189 O  O    . MET B 1 310 ? 2.686   39.316  25.357  1.00 12.31  ?  533  MET B O    1 
ATOM   10190 C  CB   . MET B 1 310 ? 1.169   37.797  22.816  1.00 12.53  ?  533  MET B CB   1 
ATOM   10191 C  CG   . MET B 1 310 ? 2.319   36.876  23.031  1.00 14.36  ?  533  MET B CG   1 
ATOM   10192 S  SD   . MET B 1 310 ? 2.655   36.066  21.469  1.00 12.88  ?  533  MET B SD   1 
ATOM   10193 C  CE   . MET B 1 310 ? 3.924   34.936  22.061  1.00 17.22  ?  533  MET B CE   1 
ATOM   10194 O  OXT  . MET B 1 310 ? 2.472   40.548  23.611  1.00 14.75  ?  533  MET B OXT  1 
ATOM   10195 H  H    . MET B 1 310 ? -0.247  39.691  22.574  1.00 11.19  ?  533  MET B H    1 
ATOM   10196 H  HA   . MET B 1 310 ? 0.566   38.295  24.715  1.00 13.02  ?  533  MET B HA   1 
ATOM   10197 H  HB2  . MET B 1 310 ? 0.385   37.242  22.679  1.00 15.04  ?  533  MET B HB2  1 
ATOM   10198 H  HB3  . MET B 1 310 ? 1.361   38.304  22.011  1.00 15.04  ?  533  MET B HB3  1 
ATOM   10199 H  HG2  . MET B 1 310 ? 3.102   37.376  23.311  1.00 17.23  ?  533  MET B HG2  1 
ATOM   10200 H  HG3  . MET B 1 310 ? 2.095   36.209  23.699  1.00 17.23  ?  533  MET B HG3  1 
ATOM   10201 H  HE1  . MET B 1 310 ? 4.228   34.386  21.322  1.00 20.66  ?  533  MET B HE1  1 
ATOM   10202 H  HE2  . MET B 1 310 ? 4.665   35.452  22.416  1.00 20.66  ?  533  MET B HE2  1 
ATOM   10203 H  HE3  . MET B 1 310 ? 3.548   34.375  22.758  1.00 20.66  ?  533  MET B HE3  1 
HETATM 10204 C  C1   . EDO C 2 .   ? 13.625  -10.963 19.348  1.00 17.27  ?  601  EDO A C1   1 
HETATM 10205 O  O1   . EDO C 2 .   ? 14.838  -10.254 19.133  1.00 11.27  ?  601  EDO A O1   1 
HETATM 10206 C  C2   . EDO C 2 .   ? 13.845  -12.025 20.410  1.00 31.75  ?  601  EDO A C2   1 
HETATM 10207 O  O2   . EDO C 2 .   ? 14.977  -12.818 20.036  1.00 34.52  ?  601  EDO A O2   1 
HETATM 10208 H  H11  . EDO C 2 .   ? 13.298  -11.431 18.417  1.00 20.72  ?  601  EDO A H11  1 
HETATM 10209 H  H12  . EDO C 2 .   ? 12.843  -10.273 19.669  1.00 20.72  ?  601  EDO A H12  1 
HETATM 10210 H  HO1  . EDO C 2 .   ? 14.704  -9.589  18.444  1.00 13.52  ?  601  EDO A HO1  1 
HETATM 10211 H  H21  . EDO C 2 .   ? 14.021  -11.555 21.380  1.00 38.10  ?  601  EDO A H21  1 
HETATM 10212 H  H22  . EDO C 2 .   ? 12.958  -12.656 20.499  1.00 38.10  ?  601  EDO A H22  1 
HETATM 10213 H  HO2  . EDO C 2 .   ? 15.116  -13.511 20.695  1.00 41.43  ?  601  EDO A HO2  1 
HETATM 10214 C  C1   . EDO D 2 .   ? -1.122  8.607   6.147   1.00 16.06  ?  602  EDO A C1   1 
HETATM 10215 O  O1   . EDO D 2 .   ? -0.342  7.671   6.891   1.00 14.85  ?  602  EDO A O1   1 
HETATM 10216 C  C2   . EDO D 2 .   ? -0.215  9.312   5.145   1.00 18.10  ?  602  EDO A C2   1 
HETATM 10217 O  O2   . EDO D 2 .   ? 0.402   8.340   4.294   1.00 26.22  ?  602  EDO A O2   1 
HETATM 10218 H  H11  . EDO D 2 .   ? -1.574  9.337   6.821   1.00 19.28  ?  602  EDO A H11  1 
HETATM 10219 H  H12  . EDO D 2 .   ? -1.928  8.090   5.623   1.00 19.28  ?  602  EDO A H12  1 
HETATM 10220 H  HO1  . EDO D 2 .   ? -0.918  7.172   7.486   1.00 17.82  ?  602  EDO A HO1  1 
HETATM 10221 H  H21  . EDO D 2 .   ? -0.798  10.013  4.545   1.00 21.73  ?  602  EDO A H21  1 
HETATM 10222 H  H22  . EDO D 2 .   ? 0.552   9.880   5.675   1.00 21.73  ?  602  EDO A H22  1 
HETATM 10223 H  HO2  . EDO D 2 .   ? 0.940   8.790   3.628   1.00 31.47  ?  602  EDO A HO2  1 
HETATM 10224 C  C1   A EDO E 2 .   ? 13.252  7.652   33.619  0.72 15.51  ?  603  EDO A C1   1 
HETATM 10225 O  O1   A EDO E 2 .   ? 13.832  6.450   34.132  0.72 16.96  ?  603  EDO A O1   1 
HETATM 10226 C  C2   A EDO E 2 .   ? 13.183  7.680   32.091  0.72 8.17   ?  603  EDO A C2   1 
HETATM 10227 O  O2   A EDO E 2 .   ? 12.718  8.994   31.810  0.72 11.05  ?  603  EDO A O2   1 
HETATM 10228 H  H11  A EDO E 2 .   ? 13.842  8.505   33.963  0.72 18.62  ?  603  EDO A H11  1 
HETATM 10229 H  H12  A EDO E 2 .   ? 12.243  7.758   34.022  0.72 18.62  ?  603  EDO A H12  1 
HETATM 10230 H  HO1  A EDO E 2 .   ? 13.888  6.505   35.096  0.72 20.35  ?  603  EDO A HO1  1 
HETATM 10231 H  H21  A EDO E 2 .   ? 12.494  6.923   31.709  0.72 9.81   ?  603  EDO A H21  1 
HETATM 10232 H  H22  A EDO E 2 .   ? 14.162  7.499   31.644  0.72 9.81   ?  603  EDO A H22  1 
HETATM 10233 H  HO2  A EDO E 2 .   ? 12.638  9.110   30.853  0.72 13.27  ?  603  EDO A HO2  1 
HETATM 10234 C  C1   A EDO F 2 .   ? 34.163  26.133  7.869   0.63 27.60  ?  604  EDO A C1   1 
HETATM 10235 O  O1   A EDO F 2 .   ? 33.472  24.884  7.870   0.63 13.07  ?  604  EDO A O1   1 
HETATM 10236 C  C2   A EDO F 2 .   ? 33.890  26.753  9.226   0.63 13.30  ?  604  EDO A C2   1 
HETATM 10237 O  O2   A EDO F 2 .   ? 33.897  25.700  10.200  0.63 15.56  ?  604  EDO A O2   1 
HETATM 10238 H  H11  A EDO F 2 .   ? 35.234  25.985  7.718   0.63 33.12  ?  604  EDO A H11  1 
HETATM 10239 H  H12  A EDO F 2 .   ? 33.797  26.778  7.067   0.63 33.12  ?  604  EDO A H12  1 
HETATM 10240 H  HO1  A EDO F 2 .   ? 33.614  24.437  7.024   0.63 15.69  ?  604  EDO A HO1  1 
HETATM 10241 H  H21  A EDO F 2 .   ? 32.923  27.260  9.224   0.63 15.96  ?  604  EDO A H21  1 
HETATM 10242 H  H22  A EDO F 2 .   ? 34.657  27.494  9.465   0.63 15.96  ?  604  EDO A H22  1 
HETATM 10243 H  HO2  A EDO F 2 .   ? 33.524  26.026  11.031  0.63 18.67  ?  604  EDO A HO2  1 
HETATM 10244 C  C1   . EDO G 2 .   ? 25.399  21.663  18.066  1.00 28.16  ?  605  EDO A C1   1 
HETATM 10245 O  O1   . EDO G 2 .   ? 24.042  22.058  18.306  1.00 52.22  ?  605  EDO A O1   1 
HETATM 10246 C  C2   . EDO G 2 .   ? 25.608  21.458  16.573  1.00 63.50  ?  605  EDO A C2   1 
HETATM 10247 O  O2   . EDO G 2 .   ? 24.482  20.782  15.977  1.00 27.64  ?  605  EDO A O2   1 
HETATM 10248 H  H11  . EDO G 2 .   ? 25.617  20.737  18.602  1.00 33.79  ?  605  EDO A H11  1 
HETATM 10249 H  H12  . EDO G 2 .   ? 26.081  22.432  18.434  1.00 33.79  ?  605  EDO A H12  1 
HETATM 10250 H  HO1  . EDO G 2 .   ? 23.906  22.186  19.255  1.00 62.67  ?  605  EDO A HO1  1 
HETATM 10251 H  H21  . EDO G 2 .   ? 25.747  22.427  16.090  1.00 76.21  ?  605  EDO A H21  1 
HETATM 10252 H  H22  . EDO G 2 .   ? 26.513  20.869  16.411  1.00 76.21  ?  605  EDO A H22  1 
HETATM 10253 H  HO2  . EDO G 2 .   ? 24.624  20.698  15.024  1.00 33.17  ?  605  EDO A HO2  1 
HETATM 10254 C  C1   . EDO H 2 .   ? 0.822   -21.111 22.473  1.00 24.42  ?  606  EDO A C1   1 
HETATM 10255 O  O1   . EDO H 2 .   ? 2.169   -21.060 22.002  1.00 33.49  ?  606  EDO A O1   1 
HETATM 10256 C  C2   . EDO H 2 .   ? -0.042  -21.872 21.477  1.00 72.08  ?  606  EDO A C2   1 
HETATM 10257 O  O2   . EDO H 2 .   ? -0.707  -20.929 20.634  1.00 24.00  ?  606  EDO A O2   1 
HETATM 10258 H  H11  . EDO H 2 .   ? 0.789   -21.606 23.446  1.00 29.31  ?  606  EDO A H11  1 
HETATM 10259 H  H12  . EDO H 2 .   ? 0.435   -20.097 22.600  1.00 29.31  ?  606  EDO A H12  1 
HETATM 10260 H  HO1  . EDO H 2 .   ? 2.712   -20.562 22.630  1.00 40.19  ?  606  EDO A HO1  1 
HETATM 10261 H  H21  . EDO H 2 .   ? -0.775  -22.483 22.008  1.00 86.50  ?  606  EDO A H21  1 
HETATM 10262 H  H22  . EDO H 2 .   ? 0.579   -22.540 20.876  1.00 86.50  ?  606  EDO A H22  1 
HETATM 10263 H  HO2  . EDO H 2 .   ? -1.163  -21.399 19.922  1.00 28.80  ?  606  EDO A HO2  1 
HETATM 10264 C  C1   . EDO I 2 .   ? 37.277  10.135  6.915   1.00 30.27  ?  607  EDO A C1   1 
HETATM 10265 O  O1   . EDO I 2 .   ? 37.806  8.863   6.522   1.00 29.75  ?  607  EDO A O1   1 
HETATM 10266 C  C2   . EDO I 2 .   ? 35.907  10.321  6.272   1.00 61.24  ?  607  EDO A C2   1 
HETATM 10267 O  O2   . EDO I 2 .   ? 34.939  9.453   6.879   1.00 23.14  ?  607  EDO A O2   1 
HETATM 10268 H  H11  . EDO I 2 .   ? 37.951  10.934  6.597   1.00 36.33  ?  607  EDO A H11  1 
HETATM 10269 H  H12  . EDO I 2 .   ? 37.189  10.183  8.002   1.00 36.33  ?  607  EDO A H12  1 
HETATM 10270 H  HO1  . EDO I 2 .   ? 38.752  8.832   6.720   1.00 35.70  ?  607  EDO A HO1  1 
HETATM 10271 H  H21  . EDO I 2 .   ? 35.973  10.105  5.204   1.00 73.49  ?  607  EDO A H21  1 
HETATM 10272 H  H22  . EDO I 2 .   ? 35.589  11.360  6.386   1.00 73.49  ?  607  EDO A H22  1 
HETATM 10273 H  HO2  . EDO I 2 .   ? 34.084  9.569   6.443   1.00 27.77  ?  607  EDO A HO2  1 
HETATM 10274 C  C1   A EDO J 2 .   ? 31.663  -7.430  21.270  0.72 26.23  ?  608  EDO A C1   1 
HETATM 10275 O  O1   A EDO J 2 .   ? 32.787  -7.414  22.155  0.72 49.36  ?  608  EDO A O1   1 
HETATM 10276 C  C2   A EDO J 2 .   ? 30.378  -7.198  22.049  0.72 29.29  ?  608  EDO A C2   1 
HETATM 10277 O  O2   A EDO J 2 .   ? 29.232  -7.570  21.278  0.72 104.79 ?  608  EDO A O2   1 
HETATM 10278 H  H11  A EDO J 2 .   ? 31.613  -8.392  20.757  0.72 31.48  ?  608  EDO A H11  1 
HETATM 10279 H  H12  A EDO J 2 .   ? 31.780  -6.652  20.513  0.72 31.48  ?  608  EDO A H12  1 
HETATM 10280 H  HO1  A EDO J 2 .   ? 33.600  -7.529  21.644  0.72 59.24  ?  608  EDO A HO1  1 
HETATM 10281 H  H21  A EDO J 2 .   ? 30.305  -6.143  22.323  0.72 35.15  ?  608  EDO A H21  1 
HETATM 10282 H  H22  A EDO J 2 .   ? 30.402  -7.783  22.970  0.72 35.15  ?  608  EDO A H22  1 
HETATM 10283 H  HO2  A EDO J 2 .   ? 28.430  -7.405  21.794  0.72 125.75 ?  608  EDO A HO2  1 
HETATM 10284 C  C1   B EDO K 2 .   ? 33.292  -1.793  29.282  0.88 20.44  ?  609  EDO A C1   1 
HETATM 10285 O  O1   B EDO K 2 .   ? 34.451  -1.861  28.446  0.88 41.86  ?  609  EDO A O1   1 
HETATM 10286 C  C2   B EDO K 2 .   ? 32.227  -2.776  28.797  0.88 27.15  ?  609  EDO A C2   1 
HETATM 10287 O  O2   B EDO K 2 .   ? 32.297  -2.978  27.380  0.88 22.96  ?  609  EDO A O2   1 
HETATM 10288 H  H11  B EDO K 2 .   ? 32.889  -0.778  29.268  0.88 24.53  ?  609  EDO A H11  1 
HETATM 10289 H  H12  B EDO K 2 .   ? 33.569  -2.030  30.312  0.88 24.53  ?  609  EDO A H12  1 
HETATM 10290 H  HO1  B EDO K 2 .   ? 35.122  -1.247  28.774  0.88 50.23  ?  609  EDO A HO1  1 
HETATM 10291 H  H21  B EDO K 2 .   ? 31.238  -2.394  29.058  0.88 32.58  ?  609  EDO A H21  1 
HETATM 10292 H  H22  B EDO K 2 .   ? 32.363  -3.733  29.304  0.88 32.58  ?  609  EDO A H22  1 
HETATM 10293 H  HO2  B EDO K 2 .   ? 31.411  -2.897  26.999  0.88 27.55  ?  609  EDO A HO2  1 
HETATM 10294 C  C1   . EDO L 2 .   ? -5.603  14.009  27.773  1.00 56.07  ?  610  EDO A C1   1 
HETATM 10295 O  O1   . EDO L 2 .   ? -6.316  12.849  28.222  1.00 20.41  ?  610  EDO A O1   1 
HETATM 10296 C  C2   . EDO L 2 .   ? -4.149  13.906  28.213  1.00 26.76  ?  610  EDO A C2   1 
HETATM 10297 O  O2   . EDO L 2 .   ? -4.119  13.733  29.634  1.00 19.72  ?  610  EDO A O2   1 
HETATM 10298 H  H11  . EDO L 2 .   ? -6.056  14.910  28.192  1.00 67.29  ?  610  EDO A H11  1 
HETATM 10299 H  H12  . EDO L 2 .   ? -5.658  14.081  26.684  1.00 67.29  ?  610  EDO A H12  1 
HETATM 10300 H  HO1  . EDO L 2 .   ? -7.241  12.913  27.948  1.00 24.49  ?  610  EDO A HO1  1 
HETATM 10301 H  H21  . EDO L 2 .   ? -3.606  14.810  27.932  1.00 32.12  ?  610  EDO A H21  1 
HETATM 10302 H  H22  . EDO L 2 .   ? -3.666  13.058  27.721  1.00 32.12  ?  610  EDO A H22  1 
HETATM 10303 H  HO2  . EDO L 2 .   ? -3.201  13.670  29.931  1.00 23.67  ?  610  EDO A HO2  1 
HETATM 10304 CL CL   . CL  M 3 .   ? 20.946  -9.825  4.592   0.88 13.15  ?  611  CL  A CL   1 
HETATM 10305 CL CL   . CL  N 3 .   ? 3.007   -11.379 33.793  1.00 45.23  ?  612  CL  A CL   1 
HETATM 10306 C  C1   . EDO O 2 .   ? 31.359  -4.046  1.544   1.00 13.53  ?  601  EDO B C1   1 
HETATM 10307 O  O1   . EDO O 2 .   ? 31.308  -3.130  2.640   1.00 13.26  ?  601  EDO B O1   1 
HETATM 10308 C  C2   . EDO O 2 .   ? 29.943  -4.363  1.066   1.00 11.97  ?  601  EDO B C2   1 
HETATM 10309 O  O2   . EDO O 2 .   ? 29.278  -3.213  0.496   1.00 11.91  ?  601  EDO B O2   1 
HETATM 10310 H  H11  . EDO O 2 .   ? 31.858  -4.966  1.855   1.00 16.24  ?  601  EDO B H11  1 
HETATM 10311 H  H12  . EDO O 2 .   ? 31.936  -3.610  0.726   1.00 16.24  ?  601  EDO B H12  1 
HETATM 10312 H  HO1  . EDO O 2 .   ? 32.207  -2.939  2.942   1.00 15.91  ?  601  EDO B HO1  1 
HETATM 10313 H  H21  . EDO O 2 .   ? 29.990  -5.156  0.316   1.00 14.37  ?  601  EDO B H21  1 
HETATM 10314 H  H22  . EDO O 2 .   ? 29.356  -4.733  1.909   1.00 14.37  ?  601  EDO B H22  1 
HETATM 10315 H  HO2  . EDO O 2 .   ? 28.332  -3.396  0.414   1.00 14.29  ?  601  EDO B HO2  1 
HETATM 10316 C  C1   . EDO P 2 .   ? 9.189   33.478  10.193  1.00 15.33  ?  602  EDO B C1   1 
HETATM 10317 O  O1   . EDO P 2 .   ? 10.131  32.780  9.386   1.00 11.20  ?  602  EDO B O1   1 
HETATM 10318 C  C2   . EDO P 2 .   ? 8.457   34.506  9.343   1.00 46.77  ?  602  EDO B C2   1 
HETATM 10319 O  O2   . EDO P 2 .   ? 9.409   35.334  8.668   1.00 36.46  ?  602  EDO B O2   1 
HETATM 10320 H  H11  . EDO P 2 .   ? 8.473   32.774  10.622  1.00 18.39  ?  602  EDO B H11  1 
HETATM 10321 H  H12  . EDO P 2 .   ? 9.703   33.977  11.017  1.00 18.39  ?  602  EDO B H12  1 
HETATM 10322 H  HO1  . EDO P 2 .   ? 10.590  32.120  9.924   1.00 13.44  ?  602  EDO B HO1  1 
HETATM 10323 H  H21  . EDO P 2 .   ? 7.814   35.121  9.976   1.00 56.12  ?  602  EDO B H21  1 
HETATM 10324 H  H22  . EDO P 2 .   ? 7.823   33.999  8.612   1.00 56.12  ?  602  EDO B H22  1 
HETATM 10325 H  HO2  . EDO P 2 .   ? 8.943   35.988  8.130   1.00 43.76  ?  602  EDO B HO2  1 
HETATM 10326 C  C1   . EDO Q 2 .   ? 11.594  13.180  30.172  1.00 16.50  ?  603  EDO B C1   1 
HETATM 10327 O  O1   . EDO Q 2 .   ? 12.646  14.153  30.229  1.00 25.31  ?  603  EDO B O1   1 
HETATM 10328 C  C2   . EDO Q 2 .   ? 10.245  13.875  30.060  1.00 15.21  ?  603  EDO B C2   1 
HETATM 10329 O  O2   . EDO Q 2 .   ? 10.278  14.809  28.972  1.00 15.56  ?  603  EDO B O2   1 
HETATM 10330 H  H11  . EDO Q 2 .   ? 11.744  12.525  29.311  1.00 19.80  ?  603  EDO B H11  1 
HETATM 10331 H  H12  . EDO Q 2 .   ? 11.616  12.561  31.071  1.00 19.80  ?  603  EDO B H12  1 
HETATM 10332 H  HO1  . EDO Q 2 .   ? 13.499  13.703  30.303  1.00 30.37  ?  603  EDO B HO1  1 
HETATM 10333 H  H21  . EDO Q 2 .   ? 10.018  14.397  30.991  1.00 18.25  ?  603  EDO B H21  1 
HETATM 10334 H  H22  . EDO Q 2 .   ? 9.459   13.135  29.890  1.00 18.25  ?  603  EDO B H22  1 
HETATM 10335 H  HO2  . EDO Q 2 .   ? 9.426   15.263  28.911  1.00 18.67  ?  603  EDO B HO2  1 
HETATM 10336 C  C1   A EDO R 2 .   ? 27.594  19.176  -2.799  0.79 17.81  ?  604  EDO B C1   1 
HETATM 10337 O  O1   A EDO R 2 .   ? 28.065  19.963  -3.899  0.79 24.53  ?  604  EDO B O1   1 
HETATM 10338 C  C2   A EDO R 2 .   ? 27.713  17.705  -3.178  0.79 17.96  ?  604  EDO B C2   1 
HETATM 10339 O  O2   A EDO R 2 .   ? 27.113  17.527  -4.469  0.79 23.97  ?  604  EDO B O2   1 
HETATM 10340 H  H11  A EDO R 2 .   ? 28.186  19.384  -1.906  0.79 21.38  ?  604  EDO B H11  1 
HETATM 10341 H  H12  A EDO R 2 .   ? 26.554  19.424  -2.578  0.79 21.38  ?  604  EDO B H12  1 
HETATM 10342 H  HO1  A EDO R 2 .   ? 27.992  20.902  -3.678  0.79 29.44  ?  604  EDO B HO1  1 
HETATM 10343 H  H21  A EDO R 2 .   ? 27.207  17.082  -2.437  0.79 21.55  ?  604  EDO B H21  1 
HETATM 10344 H  H22  A EDO R 2 .   ? 28.763  17.406  -3.205  0.79 21.55  ?  604  EDO B H22  1 
HETATM 10345 H  HO2  A EDO R 2 .   ? 27.444  16.712  -4.869  0.79 28.76  ?  604  EDO B HO2  1 
HETATM 10346 C  C1   A EDO S 2 .   ? 15.258  -5.794  4.459   0.98 80.77  ?  605  EDO B C1   1 
HETATM 10347 O  O1   A EDO S 2 .   ? 15.829  -7.089  4.687   0.98 67.02  ?  605  EDO B O1   1 
HETATM 10348 C  C2   A EDO S 2 .   ? 16.260  -4.728  4.891   0.98 44.46  ?  605  EDO B C2   1 
HETATM 10349 O  O2   A EDO S 2 .   ? 16.107  -3.512  4.139   0.98 31.42  ?  605  EDO B O2   1 
HETATM 10350 H  H11  A EDO S 2 .   ? 15.016  -5.673  3.401   0.98 96.93  ?  605  EDO B H11  1 
HETATM 10351 H  H12  A EDO S 2 .   ? 14.332  -5.689  5.029   0.98 96.93  ?  605  EDO B H12  1 
HETATM 10352 H  HO1  A EDO S 2 .   ? 15.174  -7.770  4.480   0.98 80.43  ?  605  EDO B HO1  1 
HETATM 10353 H  H21  A EDO S 2 .   ? 17.273  -5.110  4.755   0.98 53.35  ?  605  EDO B H21  1 
HETATM 10354 H  H22  A EDO S 2 .   ? 16.122  -4.514  5.953   0.98 53.35  ?  605  EDO B H22  1 
HETATM 10355 H  HO2  A EDO S 2 .   ? 16.591  -2.798  4.577   0.98 37.71  ?  605  EDO B HO2  1 
HETATM 10356 C  C1   . EDO T 2 .   ? 18.866  1.341   4.251   0.90 32.99  ?  606  EDO B C1   1 
HETATM 10357 O  O1   . EDO T 2 .   ? 19.649  0.210   4.663   0.90 22.77  ?  606  EDO B O1   1 
HETATM 10358 C  C2   . EDO T 2 .   ? 18.799  1.428   2.726   0.90 50.88  ?  606  EDO B C2   1 
HETATM 10359 O  O2   . EDO T 2 .   ? 17.629  0.771   2.218   0.90 37.91  ?  606  EDO B O2   1 
HETATM 10360 H  H11  . EDO T 2 .   ? 19.309  2.257   4.649   0.90 39.60  ?  606  EDO B H11  1 
HETATM 10361 H  H12  . EDO T 2 .   ? 17.856  1.253   4.656   0.90 39.60  ?  606  EDO B H12  1 
HETATM 10362 H  HO1  . EDO T 2 .   ? 19.602  0.118   5.625   0.90 27.32  ?  606  EDO B HO1  1 
HETATM 10363 H  H21  . EDO T 2 .   ? 19.690  0.964   2.298   0.90 61.05  ?  606  EDO B H21  1 
HETATM 10364 H  H22  . EDO T 2 .   ? 18.787  2.476   2.423   0.90 61.05  ?  606  EDO B H22  1 
HETATM 10365 H  HO2  . EDO T 2 .   ? 17.624  0.824   1.252   0.90 45.50  ?  606  EDO B HO2  1 
HETATM 10366 C  C1   C EDO U 2 .   ? 6.249   11.512  17.640  0.70 34.04  ?  607  EDO B C1   1 
HETATM 10367 O  O1   C EDO U 2 .   ? 7.010   10.318  17.852  0.70 33.90  ?  607  EDO B O1   1 
HETATM 10368 C  C2   C EDO U 2 .   ? 6.609   12.143  16.308  0.70 21.91  ?  607  EDO B C2   1 
HETATM 10369 O  O2   C EDO U 2 .   ? 7.985   12.543  16.362  0.70 31.41  ?  607  EDO B O2   1 
HETATM 10370 H  H11  C EDO U 2 .   ? 6.449   12.221  18.446  0.70 40.85  ?  607  EDO B H11  1 
HETATM 10371 H  H12  C EDO U 2 .   ? 5.184   11.275  17.657  0.70 40.85  ?  607  EDO B H12  1 
HETATM 10372 H  HO1  C EDO U 2 .   ? 6.770   9.930   18.705  0.70 40.68  ?  607  EDO B HO1  1 
HETATM 10373 H  H21  C EDO U 2 .   ? 5.972   13.009  16.116  0.70 26.29  ?  607  EDO B H21  1 
HETATM 10374 H  H22  C EDO U 2 .   ? 6.456   11.427  15.498  0.70 26.29  ?  607  EDO B H22  1 
HETATM 10375 H  HO2  C EDO U 2 .   ? 8.240   12.935  15.515  0.70 37.70  ?  607  EDO B HO2  1 
HETATM 10376 CL CL   . CL  V 3 .   ? 25.430  32.699  13.015  0.86 10.31  ?  608  CL  B CL   1 
HETATM 10377 O  O    B HOH W 4 .   ? 31.169  1.872   29.678  0.41 10.91  ?  701  HOH A O    1 
HETATM 10378 O  O    B HOH W 4 .   ? -10.792 -13.164 24.442  0.59 22.48  ?  702  HOH A O    1 
HETATM 10379 O  O    B HOH W 4 .   ? 27.761  -7.869  8.839   0.60 9.11   ?  703  HOH A O    1 
HETATM 10380 O  O    B HOH W 4 .   ? 45.456  16.997  11.145  0.99 30.81  ?  704  HOH A O    1 
HETATM 10381 O  O    . HOH W 4 .   ? 9.491   -12.967 20.890  1.00 40.05  ?  705  HOH A O    1 
HETATM 10382 O  O    . HOH W 4 .   ? 32.605  37.971  16.495  1.00 26.07  ?  706  HOH A O    1 
HETATM 10383 O  O    B HOH W 4 .   ? 3.770   6.804   7.086   0.85 27.21  ?  707  HOH A O    1 
HETATM 10384 O  O    . HOH W 4 .   ? 24.211  22.657  14.624  1.00 17.45  ?  708  HOH A O    1 
HETATM 10385 O  O    . HOH W 4 .   ? 30.595  43.227  11.072  1.00 49.65  ?  709  HOH A O    1 
HETATM 10386 O  O    . HOH W 4 .   ? 40.646  5.613   9.921   1.00 34.48  ?  710  HOH A O    1 
HETATM 10387 O  O    . HOH W 4 .   ? -7.440  -0.246  3.789   1.00 48.21  ?  711  HOH A O    1 
HETATM 10388 O  O    . HOH W 4 .   ? 39.625  11.006  27.796  1.00 40.12  ?  712  HOH A O    1 
HETATM 10389 O  O    . HOH W 4 .   ? -14.511 -7.835  25.871  1.00 45.49  ?  713  HOH A O    1 
HETATM 10390 O  O    B HOH W 4 .   ? 15.294  4.554   36.721  0.41 8.27   ?  714  HOH A O    1 
HETATM 10391 O  O    . HOH W 4 .   ? -13.080 -2.310  22.242  1.00 45.02  ?  715  HOH A O    1 
HETATM 10392 O  O    . HOH W 4 .   ? 37.386  14.160  6.121   1.00 48.99  ?  716  HOH A O    1 
HETATM 10393 O  O    B HOH W 4 .   ? 28.947  37.620  7.012   0.52 21.43  ?  717  HOH A O    1 
HETATM 10394 O  O    . HOH W 4 .   ? 1.539   10.750  34.675  1.00 11.72  ?  718  HOH A O    1 
HETATM 10395 O  O    . HOH W 4 .   ? -14.868 -7.380  22.526  1.00 47.26  ?  719  HOH A O    1 
HETATM 10396 O  O    . HOH W 4 .   ? 20.126  4.602   40.846  1.00 27.10  ?  720  HOH A O    1 
HETATM 10397 O  O    . HOH W 4 .   ? 17.467  15.142  16.882  1.00 26.75  ?  721  HOH A O    1 
HETATM 10398 O  O    A HOH W 4 .   ? 13.882  5.753   36.491  0.99 20.63  ?  722  HOH A O    1 
HETATM 10399 O  O    . HOH W 4 .   ? 35.400  5.285   12.695  1.00 48.84  ?  723  HOH A O    1 
HETATM 10400 O  O    . HOH W 4 .   ? 38.965  21.313  25.711  1.00 32.13  ?  724  HOH A O    1 
HETATM 10401 O  O    A HOH W 4 .   ? 19.657  -8.053  28.572  0.61 19.43  ?  725  HOH A O    1 
HETATM 10402 O  O    . HOH W 4 .   ? 18.576  16.861  19.579  1.00 19.80  ?  726  HOH A O    1 
HETATM 10403 O  O    . HOH W 4 .   ? 4.477   0.961   27.123  1.00 42.67  ?  727  HOH A O    1 
HETATM 10404 O  O    . HOH W 4 .   ? 4.147   2.905   37.828  1.00 46.11  ?  728  HOH A O    1 
HETATM 10405 O  O    . HOH W 4 .   ? 14.300  -15.378 19.587  1.00 27.92  ?  729  HOH A O    1 
HETATM 10406 O  O    . HOH W 4 .   ? 22.326  6.225   39.836  1.00 31.14  ?  730  HOH A O    1 
HETATM 10407 O  O    . HOH W 4 .   ? 8.058   -18.831 25.242  1.00 31.80  ?  731  HOH A O    1 
HETATM 10408 O  O    . HOH W 4 .   ? 29.321  -8.787  10.516  1.00 23.05  ?  732  HOH A O    1 
HETATM 10409 O  O    A HOH W 4 .   ? 13.811  -13.937 28.780  0.72 13.90  ?  733  HOH A O    1 
HETATM 10410 O  O    . HOH W 4 .   ? 20.029  16.858  39.557  1.00 36.01  ?  734  HOH A O    1 
HETATM 10411 O  O    C HOH W 4 .   ? 46.256  14.059  20.119  0.61 21.29  ?  735  HOH A O    1 
HETATM 10412 O  O    . HOH W 4 .   ? 5.300   -23.035 23.808  1.00 41.78  ?  736  HOH A O    1 
HETATM 10413 O  O    . HOH W 4 .   ? 34.817  29.407  15.491  1.00 20.45  ?  737  HOH A O    1 
HETATM 10414 O  O    A HOH W 4 .   ? 20.261  -10.059 27.594  0.46 18.38  ?  738  HOH A O    1 
HETATM 10415 O  O    . HOH W 4 .   ? 9.555   -20.195 10.541  1.00 41.14  ?  739  HOH A O    1 
HETATM 10416 O  O    . HOH W 4 .   ? 24.398  24.525  18.880  1.00 27.79  ?  740  HOH A O    1 
HETATM 10417 O  O    . HOH W 4 .   ? 18.571  12.122  23.863  1.00 12.38  ?  741  HOH A O    1 
HETATM 10418 O  O    . HOH W 4 .   ? 12.064  10.962  33.325  1.00 27.33  ?  742  HOH A O    1 
HETATM 10419 O  O    B HOH W 4 .   ? 29.459  -5.326  20.635  0.88 14.60  ?  743  HOH A O    1 
HETATM 10420 O  O    A HOH W 4 .   ? 13.787  -9.778  10.218  0.59 23.18  ?  744  HOH A O    1 
HETATM 10421 O  O    B HOH W 4 .   ? 12.265  -13.545 27.651  0.82 43.84  ?  745  HOH A O    1 
HETATM 10422 O  O    A HOH W 4 .   ? 29.544  -10.312 19.161  1.00 55.02  ?  746  HOH A O    1 
HETATM 10423 O  O    . HOH W 4 .   ? -3.999  12.360  24.409  1.00 18.12  ?  747  HOH A O    1 
HETATM 10424 O  O    . HOH W 4 .   ? 33.347  -7.619  0.301   1.00 13.74  ?  748  HOH A O    1 
HETATM 10425 O  O    A HOH W 4 .   ? -10.170 -15.037 24.214  1.00 28.85  ?  749  HOH A O    1 
HETATM 10426 O  O    . HOH W 4 .   ? -5.702  -19.605 33.091  1.00 29.89  ?  750  HOH A O    1 
HETATM 10427 O  O    A HOH W 4 .   ? 35.578  -3.145  25.485  0.90 34.63  ?  751  HOH A O    1 
HETATM 10428 O  O    . HOH W 4 .   ? 1.165   -15.630 34.104  1.00 19.22  ?  752  HOH A O    1 
HETATM 10429 O  O    . HOH W 4 .   ? -4.224  5.725   10.565  1.00 18.77  ?  753  HOH A O    1 
HETATM 10430 O  O    B HOH W 4 .   ? -0.240  8.055   1.791   0.44 22.02  ?  754  HOH A O    1 
HETATM 10431 O  O    . HOH W 4 .   ? 19.405  14.968  14.781  1.00 18.48  ?  755  HOH A O    1 
HETATM 10432 O  O    A HOH W 4 .   ? 15.215  1.604   9.120   0.87 18.67  ?  756  HOH A O    1 
HETATM 10433 O  O    . HOH W 4 .   ? -0.430  -1.462  10.873  1.00 11.25  ?  757  HOH A O    1 
HETATM 10434 O  O    . HOH W 4 .   ? -0.093  -4.421  40.989  1.00 38.92  ?  758  HOH A O    1 
HETATM 10435 O  O    A HOH W 4 .   ? 13.822  -16.954 15.183  0.99 34.36  ?  759  HOH A O    1 
HETATM 10436 O  O    A HOH W 4 .   ? 26.630  28.595  19.380  0.33 11.14  ?  760  HOH A O    1 
HETATM 10437 O  O    A HOH W 4 .   ? 20.096  18.147  15.045  0.89 16.46  ?  761  HOH A O    1 
HETATM 10438 O  O    . HOH W 4 .   ? 34.589  -5.729  14.044  1.00 25.72  ?  762  HOH A O    1 
HETATM 10439 O  O    . HOH W 4 .   ? 9.298   -7.902  34.665  1.00 28.59  ?  763  HOH A O    1 
HETATM 10440 O  O    . HOH W 4 .   ? 20.430  -7.281  31.242  1.00 17.36  ?  764  HOH A O    1 
HETATM 10441 O  O    . HOH W 4 .   ? 17.581  -12.564 19.788  1.00 32.59  ?  765  HOH A O    1 
HETATM 10442 O  O    . HOH W 4 .   ? 25.249  -9.882  9.856   1.00 41.05  ?  766  HOH A O    1 
HETATM 10443 O  O    . HOH W 4 .   ? -12.544 -11.640 26.927  1.00 26.54  ?  767  HOH A O    1 
HETATM 10444 O  O    . HOH W 4 .   ? -10.717 2.389   16.942  1.00 28.66  ?  768  HOH A O    1 
HETATM 10445 O  O    . HOH W 4 .   ? 41.026  19.856  8.760   1.00 42.90  ?  769  HOH A O    1 
HETATM 10446 O  O    . HOH W 4 .   ? -6.375  6.951   27.596  1.00 11.05  ?  770  HOH A O    1 
HETATM 10447 O  O    A HOH W 4 .   ? 28.881  -9.469  23.261  0.69 23.27  ?  771  HOH A O    1 
HETATM 10448 O  O    C HOH W 4 .   ? 18.864  13.201  27.140  0.55 10.68  ?  772  HOH A O    1 
HETATM 10449 O  O    . HOH W 4 .   ? 36.244  32.072  6.597   1.00 29.06  ?  773  HOH A O    1 
HETATM 10450 O  O    A HOH W 4 .   ? 15.955  -1.574  38.437  0.60 21.94  ?  774  HOH A O    1 
HETATM 10451 O  O    B HOH W 4 .   ? 4.260   8.965   14.124  0.86 63.45  ?  775  HOH A O    1 
HETATM 10452 O  O    . HOH W 4 .   ? 26.815  16.456  31.663  1.00 14.91  ?  776  HOH A O    1 
HETATM 10453 O  O    . HOH W 4 .   ? -0.559  -19.876 17.987  1.00 17.04  ?  777  HOH A O    1 
HETATM 10454 O  O    . HOH W 4 .   ? 36.198  23.634  10.394  1.00 12.58  ?  778  HOH A O    1 
HETATM 10455 O  O    B HOH W 4 .   ? 21.960  20.518  16.770  0.74 39.35  ?  779  HOH A O    1 
HETATM 10456 O  O    . HOH W 4 .   ? 31.012  -9.263  -2.271  1.00 13.71  ?  780  HOH A O    1 
HETATM 10457 O  O    . HOH W 4 .   ? 14.778  14.446  24.914  1.00 12.78  ?  781  HOH A O    1 
HETATM 10458 O  O    . HOH W 4 .   ? 39.973  21.813  10.486  1.00 24.59  ?  782  HOH A O    1 
HETATM 10459 O  O    B HOH W 4 .   ? 15.385  -11.844 17.068  0.99 56.73  ?  783  HOH A O    1 
HETATM 10460 O  O    . HOH W 4 .   ? 32.487  -10.053 22.362  1.00 46.40  ?  784  HOH A O    1 
HETATM 10461 O  O    . HOH W 4 .   ? 11.685  -8.656  6.202   1.00 31.83  ?  785  HOH A O    1 
HETATM 10462 O  O    . HOH W 4 .   ? 29.648  23.962  25.384  1.00 21.78  ?  786  HOH A O    1 
HETATM 10463 O  O    A HOH W 4 .   ? 3.075   -18.016 9.926   0.71 11.80  ?  787  HOH A O    1 
HETATM 10464 O  O    . HOH W 4 .   ? 30.063  -0.819  27.390  1.00 11.26  ?  788  HOH A O    1 
HETATM 10465 O  O    . HOH W 4 .   ? 10.513  3.875   38.570  1.00 43.65  ?  789  HOH A O    1 
HETATM 10466 O  O    . HOH W 4 .   ? 1.444   -6.162  6.881   1.00 25.92  ?  790  HOH A O    1 
HETATM 10467 O  O    . HOH W 4 .   ? -14.185 -4.235  15.286  1.00 41.85  ?  791  HOH A O    1 
HETATM 10468 O  O    . HOH W 4 .   ? -10.973 2.568   25.945  1.00 19.20  ?  792  HOH A O    1 
HETATM 10469 O  O    A HOH W 4 .   ? 36.039  26.658  11.483  0.90 27.19  ?  793  HOH A O    1 
HETATM 10470 O  O    . HOH W 4 .   ? 7.123   1.200   38.115  1.00 42.30  ?  794  HOH A O    1 
HETATM 10471 O  O    . HOH W 4 .   ? 33.944  40.542  9.810   1.00 9.24   ?  795  HOH A O    1 
HETATM 10472 O  O    . HOH W 4 .   ? -2.457  -17.250 26.671  1.00 14.38  ?  796  HOH A O    1 
HETATM 10473 O  O    . HOH W 4 .   ? -4.814  16.221  30.338  1.00 19.69  ?  797  HOH A O    1 
HETATM 10474 O  O    . HOH W 4 .   ? 33.102  1.123   8.252   1.00 25.00  ?  798  HOH A O    1 
HETATM 10475 O  O    . HOH W 4 .   ? -12.471 -8.781  32.158  1.00 34.90  ?  799  HOH A O    1 
HETATM 10476 O  O    . HOH W 4 .   ? 5.226   -20.529 23.312  1.00 23.13  ?  800  HOH A O    1 
HETATM 10477 O  O    . HOH W 4 .   ? 7.704   -11.213 11.941  1.00 14.27  ?  801  HOH A O    1 
HETATM 10478 O  O    B HOH W 4 .   ? -3.982  -21.441 27.129  0.99 32.53  ?  802  HOH A O    1 
HETATM 10479 O  O    . HOH W 4 .   ? 33.502  20.184  27.015  1.00 19.56  ?  803  HOH A O    1 
HETATM 10480 O  O    . HOH W 4 .   ? 29.819  -4.675  15.914  1.00 11.54  ?  804  HOH A O    1 
HETATM 10481 O  O    . HOH W 4 .   ? 19.035  13.100  30.414  1.00 16.97  ?  805  HOH A O    1 
HETATM 10482 O  O    . HOH W 4 .   ? 7.114   -2.735  6.353   1.00 40.34  ?  806  HOH A O    1 
HETATM 10483 O  O    . HOH W 4 .   ? 8.444   -0.893  29.896  1.00 13.95  ?  807  HOH A O    1 
HETATM 10484 O  O    . HOH W 4 .   ? 34.121  33.640  3.770   1.00 10.03  ?  808  HOH A O    1 
HETATM 10485 O  O    . HOH W 4 .   ? 33.651  -4.958  25.759  1.00 32.55  ?  809  HOH A O    1 
HETATM 10486 O  O    . HOH W 4 .   ? 0.545   -11.819 4.426   1.00 23.62  ?  810  HOH A O    1 
HETATM 10487 O  O    . HOH W 4 .   ? 0.073   -4.123  10.530  1.00 13.07  ?  811  HOH A O    1 
HETATM 10488 O  O    A HOH W 4 .   ? 4.962   5.321   6.148   0.28 7.23   ?  812  HOH A O    1 
HETATM 10489 O  O    A HOH W 4 .   ? 24.702  -9.429  15.473  0.76 22.25  ?  813  HOH A O    1 
HETATM 10490 O  O    . HOH W 4 .   ? 2.847   -15.856 37.691  1.00 27.80  ?  814  HOH A O    1 
HETATM 10491 O  O    . HOH W 4 .   ? 7.524   -0.155  27.415  1.00 8.25   ?  815  HOH A O    1 
HETATM 10492 O  O    . HOH W 4 .   ? -8.732  3.367   33.448  1.00 15.75  ?  816  HOH A O    1 
HETATM 10493 O  O    C HOH W 4 .   ? 40.950  14.370  25.878  1.00 41.47  ?  817  HOH A O    1 
HETATM 10494 O  O    B HOH W 4 .   ? -7.986  -14.775 34.285  0.79 42.50  ?  818  HOH A O    1 
HETATM 10495 O  O    . HOH W 4 .   ? 2.641   -14.098 30.071  1.00 11.18  ?  819  HOH A O    1 
HETATM 10496 O  O    . HOH W 4 .   ? 19.961  3.164   27.251  1.00 6.71   ?  820  HOH A O    1 
HETATM 10497 O  O    . HOH W 4 .   ? -10.167 3.579   13.063  1.00 25.26  ?  821  HOH A O    1 
HETATM 10498 O  O    . HOH W 4 .   ? 34.834  9.036   27.764  1.00 11.71  ?  822  HOH A O    1 
HETATM 10499 O  O    . HOH W 4 .   ? 0.375   -13.381 31.557  1.00 14.74  ?  823  HOH A O    1 
HETATM 10500 O  O    . HOH W 4 .   ? 32.469  30.828  15.103  1.00 7.72   ?  824  HOH A O    1 
HETATM 10501 O  O    . HOH W 4 .   ? -8.705  10.345  27.085  1.00 24.81  ?  825  HOH A O    1 
HETATM 10502 O  O    . HOH W 4 .   ? -2.592  3.138   37.508  1.00 13.30  ?  826  HOH A O    1 
HETATM 10503 O  O    . HOH W 4 .   ? 4.940   -19.229 35.129  1.00 21.89  ?  827  HOH A O    1 
HETATM 10504 O  O    . HOH W 4 .   ? 7.869   -20.290 22.735  1.00 18.86  ?  828  HOH A O    1 
HETATM 10505 O  O    . HOH W 4 .   ? -7.284  -13.633 11.984  1.00 12.22  ?  829  HOH A O    1 
HETATM 10506 O  O    . HOH W 4 .   ? 36.488  26.341  15.919  1.00 30.27  ?  830  HOH A O    1 
HETATM 10507 O  O    . HOH W 4 .   ? 2.623   1.097   36.550  1.00 15.78  ?  831  HOH A O    1 
HETATM 10508 O  O    . HOH W 4 .   ? 0.564   -15.397 10.657  1.00 8.68   ?  832  HOH A O    1 
HETATM 10509 O  O    B HOH W 4 .   ? 25.391  -6.314  29.422  0.69 20.26  ?  833  HOH A O    1 
HETATM 10510 O  O    . HOH W 4 .   ? 34.746  2.078   16.963  1.00 30.74  ?  834  HOH A O    1 
HETATM 10511 O  O    . HOH W 4 .   ? -9.619  -17.103 24.936  1.00 44.66  ?  835  HOH A O    1 
HETATM 10512 O  O    B HOH W 4 .   ? 26.178  38.552  11.420  1.00 51.69  ?  836  HOH A O    1 
HETATM 10513 O  O    . HOH W 4 .   ? 1.169   -7.880  38.264  1.00 20.89  ?  837  HOH A O    1 
HETATM 10514 O  O    . HOH W 4 .   ? 38.039  35.847  12.871  1.00 14.03  ?  838  HOH A O    1 
HETATM 10515 O  O    . HOH W 4 .   ? 8.473   14.187  32.929  1.00 31.07  ?  839  HOH A O    1 
HETATM 10516 O  O    . HOH W 4 .   ? 0.723   -18.682 14.296  1.00 14.28  ?  840  HOH A O    1 
HETATM 10517 O  O    . HOH W 4 .   ? 33.940  -3.556  40.728  1.00 7.94   ?  841  HOH A O    1 
HETATM 10518 O  O    . HOH W 4 .   ? 1.416   0.054   8.028   1.00 16.24  ?  842  HOH A O    1 
HETATM 10519 O  O    . HOH W 4 .   ? 1.571   8.473   35.356  1.00 20.56  ?  843  HOH A O    1 
HETATM 10520 O  O    . HOH W 4 .   ? 6.816   13.033  21.661  1.00 12.84  ?  844  HOH A O    1 
HETATM 10521 O  O    . HOH W 4 .   ? 34.781  22.500  7.748   1.00 11.04  ?  845  HOH A O    1 
HETATM 10522 O  O    . HOH W 4 .   ? 28.328  -4.292  28.196  1.00 15.61  ?  846  HOH A O    1 
HETATM 10523 O  O    . HOH W 4 .   ? 31.473  1.316   3.637   1.00 16.57  ?  847  HOH A O    1 
HETATM 10524 O  O    . HOH W 4 .   ? 18.329  -9.975  9.399   1.00 18.01  ?  848  HOH A O    1 
HETATM 10525 O  O    . HOH W 4 .   ? 33.311  11.284  31.888  1.00 20.16  ?  849  HOH A O    1 
HETATM 10526 O  O    A HOH W 4 .   ? 27.052  35.107  16.858  0.99 29.88  ?  850  HOH A O    1 
HETATM 10527 O  O    . HOH W 4 .   ? -5.807  3.772   11.820  1.00 16.95  ?  851  HOH A O    1 
HETATM 10528 O  O    . HOH W 4 .   ? 18.237  2.262   22.010  1.00 7.51   ?  852  HOH A O    1 
HETATM 10529 O  O    . HOH W 4 .   ? 35.323  32.723  17.451  1.00 27.37  ?  853  HOH A O    1 
HETATM 10530 O  O    . HOH W 4 .   ? 17.322  2.259   41.827  1.00 29.18  ?  854  HOH A O    1 
HETATM 10531 O  O    . HOH W 4 .   ? 26.895  29.905  22.475  1.00 25.56  ?  855  HOH A O    1 
HETATM 10532 O  O    . HOH W 4 .   ? 33.569  -3.419  14.832  1.00 21.60  ?  856  HOH A O    1 
HETATM 10533 O  O    . HOH W 4 .   ? 26.310  2.691   36.236  1.00 13.33  ?  857  HOH A O    1 
HETATM 10534 O  O    . HOH W 4 .   ? 36.471  31.954  14.908  1.00 44.36  ?  858  HOH A O    1 
HETATM 10535 O  O    . HOH W 4 .   ? -1.175  1.936   17.327  1.00 6.87   ?  859  HOH A O    1 
HETATM 10536 O  O    . HOH W 4 .   ? 31.071  -6.082  8.756   1.00 18.20  ?  860  HOH A O    1 
HETATM 10537 O  O    A HOH W 4 .   ? 33.346  14.348  6.036   1.00 7.79   ?  861  HOH A O    1 
HETATM 10538 O  O    . HOH W 4 .   ? 18.343  10.056  12.280  1.00 8.88   ?  862  HOH A O    1 
HETATM 10539 O  O    B HOH W 4 .   ? 13.587  -14.919 16.060  0.95 59.41  ?  863  HOH A O    1 
HETATM 10540 O  O    . HOH W 4 .   ? 28.750  5.169   38.018  1.00 13.86  ?  864  HOH A O    1 
HETATM 10541 O  O    . HOH W 4 .   ? -1.384  13.473  32.361  1.00 24.61  ?  865  HOH A O    1 
HETATM 10542 O  O    . HOH W 4 .   ? 24.379  20.520  25.360  1.00 15.68  ?  866  HOH A O    1 
HETATM 10543 O  O    . HOH W 4 .   ? 34.389  22.146  24.394  1.00 13.22  ?  867  HOH A O    1 
HETATM 10544 O  O    . HOH W 4 .   ? 12.303  5.660   23.653  1.00 5.90   ?  868  HOH A O    1 
HETATM 10545 O  O    B HOH W 4 .   ? 23.088  -11.590 22.994  0.58 12.51  ?  869  HOH A O    1 
HETATM 10546 O  O    . HOH W 4 .   ? 26.081  22.996  12.522  1.00 6.42   ?  870  HOH A O    1 
HETATM 10547 O  O    . HOH W 4 .   ? 27.159  0.894   39.780  1.00 12.82  ?  871  HOH A O    1 
HETATM 10548 O  O    . HOH W 4 .   ? 12.496  1.228   9.184   1.00 13.92  ?  872  HOH A O    1 
HETATM 10549 O  O    A HOH W 4 .   ? 30.262  36.715  7.332   0.50 15.20  ?  873  HOH A O    1 
HETATM 10550 O  O    . HOH W 4 .   ? 20.986  19.249  35.577  1.00 32.64  ?  874  HOH A O    1 
HETATM 10551 O  O    . HOH W 4 .   ? 37.759  6.211   5.795   1.00 35.70  ?  875  HOH A O    1 
HETATM 10552 O  O    . HOH W 4 .   ? 5.141   -20.442 14.241  1.00 23.10  ?  876  HOH A O    1 
HETATM 10553 O  O    . HOH W 4 .   ? -6.694  1.818   19.723  1.00 8.72   ?  877  HOH A O    1 
HETATM 10554 O  O    B HOH W 4 .   ? 16.975  -7.832  4.032   0.91 23.54  ?  878  HOH A O    1 
HETATM 10555 O  O    . HOH W 4 .   ? 6.617   2.542   9.708   1.00 24.67  ?  879  HOH A O    1 
HETATM 10556 O  O    . HOH W 4 .   ? 34.345  11.241  9.299   1.00 11.23  ?  880  HOH A O    1 
HETATM 10557 O  O    . HOH W 4 .   ? -6.846  6.041   21.029  1.00 15.14  ?  881  HOH A O    1 
HETATM 10558 O  O    . HOH W 4 .   ? 18.388  5.717   9.638   1.00 12.73  ?  882  HOH A O    1 
HETATM 10559 O  O    . HOH W 4 .   ? 13.868  -11.577 29.758  1.00 13.67  ?  883  HOH A O    1 
HETATM 10560 O  O    . HOH W 4 .   ? 32.833  3.455   36.919  1.00 19.79  ?  884  HOH A O    1 
HETATM 10561 O  O    . HOH W 4 .   ? 27.629  -2.971  15.838  1.00 9.86   ?  885  HOH A O    1 
HETATM 10562 O  O    . HOH W 4 .   ? 35.934  1.985   31.608  1.00 15.84  ?  886  HOH A O    1 
HETATM 10563 O  O    . HOH W 4 .   ? -4.832  10.649  34.361  1.00 24.81  ?  887  HOH A O    1 
HETATM 10564 O  O    . HOH W 4 .   ? -8.689  -4.135  4.409   1.00 19.70  ?  888  HOH A O    1 
HETATM 10565 O  O    . HOH W 4 .   ? 3.028   10.546  32.861  1.00 12.34  ?  889  HOH A O    1 
HETATM 10566 O  O    . HOH W 4 .   ? 6.174   -5.874  23.810  1.00 7.03   ?  890  HOH A O    1 
HETATM 10567 O  O    . HOH W 4 .   ? 35.386  -0.305  20.720  1.00 20.34  ?  891  HOH A O    1 
HETATM 10568 O  O    . HOH W 4 .   ? 25.008  32.954  20.848  1.00 42.69  ?  892  HOH A O    1 
HETATM 10569 O  O    . HOH W 4 .   ? 18.197  -6.181  26.939  1.00 10.10  ?  893  HOH A O    1 
HETATM 10570 O  O    . HOH W 4 .   ? -0.944  -22.416 28.268  1.00 47.10  ?  894  HOH A O    1 
HETATM 10571 O  O    . HOH W 4 .   ? -3.478  2.242   32.208  1.00 12.91  ?  895  HOH A O    1 
HETATM 10572 O  O    . HOH W 4 .   ? 28.265  0.266   33.830  1.00 9.75   ?  896  HOH A O    1 
HETATM 10573 O  O    . HOH W 4 .   ? 9.208   -14.467 23.749  1.00 11.06  ?  897  HOH A O    1 
HETATM 10574 O  O    . HOH W 4 .   ? 4.443   -9.204  9.217   1.00 17.34  ?  898  HOH A O    1 
HETATM 10575 O  O    . HOH W 4 .   ? 24.264  15.766  13.706  1.00 10.22  ?  899  HOH A O    1 
HETATM 10576 O  O    C HOH W 4 .   ? 15.254  6.010   34.972  0.51 15.57  ?  900  HOH A O    1 
HETATM 10577 O  O    . HOH W 4 .   ? 9.373   8.249   35.563  1.00 24.56  ?  901  HOH A O    1 
HETATM 10578 O  O    . HOH W 4 .   ? -5.691  2.149   9.652   1.00 15.39  ?  902  HOH A O    1 
HETATM 10579 O  O    . HOH W 4 .   ? 44.007  13.004  9.366   1.00 32.62  ?  903  HOH A O    1 
HETATM 10580 O  O    A HOH W 4 .   ? 21.548  -15.910 24.480  0.99 49.87  ?  904  HOH A O    1 
HETATM 10581 O  O    . HOH W 4 .   ? 24.246  20.477  20.581  1.00 26.29  ?  905  HOH A O    1 
HETATM 10582 O  O    . HOH W 4 .   ? 1.292   9.546   20.492  1.00 11.23  ?  906  HOH A O    1 
HETATM 10583 O  O    . HOH W 4 .   ? 46.471  11.569  15.585  1.00 21.64  ?  907  HOH A O    1 
HETATM 10584 O  O    . HOH W 4 .   ? 31.499  -1.530  7.911   1.00 15.21  ?  908  HOH A O    1 
HETATM 10585 O  O    C HOH W 4 .   ? 11.305  13.071  16.473  0.48 16.06  ?  909  HOH A O    1 
HETATM 10586 O  O    . HOH W 4 .   ? 8.119   -3.959  37.483  1.00 33.07  ?  910  HOH A O    1 
HETATM 10587 O  O    . HOH W 4 .   ? -10.244 -12.082 11.275  1.00 23.97  ?  911  HOH A O    1 
HETATM 10588 O  O    . HOH W 4 .   ? 34.052  14.160  31.344  1.00 37.51  ?  912  HOH A O    1 
HETATM 10589 O  O    B HOH W 4 .   ? 16.128  9.005   11.260  0.26 9.53   ?  913  HOH A O    1 
HETATM 10590 O  O    . HOH W 4 .   ? 20.695  15.371  21.060  1.00 13.02  ?  914  HOH A O    1 
HETATM 10591 O  O    . HOH W 4 .   ? -9.921  -8.287  7.960   1.00 14.83  ?  915  HOH A O    1 
HETATM 10592 O  O    A HOH W 4 .   ? 26.426  26.257  19.393  1.00 16.63  ?  916  HOH A O    1 
HETATM 10593 O  O    . HOH W 4 .   ? 20.623  15.363  35.150  1.00 18.41  ?  917  HOH A O    1 
HETATM 10594 O  O    . HOH W 4 .   ? -12.667 -9.624  29.184  1.00 23.68  ?  918  HOH A O    1 
HETATM 10595 O  O    . HOH W 4 .   ? 10.423  -11.386 12.009  1.00 19.91  ?  919  HOH A O    1 
HETATM 10596 O  O    . HOH W 4 .   ? -3.912  -13.803 8.617   1.00 8.44   ?  920  HOH A O    1 
HETATM 10597 O  O    . HOH W 4 .   ? 26.127  8.013   40.574  1.00 38.84  ?  921  HOH A O    1 
HETATM 10598 O  O    . HOH W 4 .   ? 15.986  -17.966 23.504  1.00 38.24  ?  922  HOH A O    1 
HETATM 10599 O  O    . HOH W 4 .   ? -2.381  5.875   29.858  1.00 8.82   ?  923  HOH A O    1 
HETATM 10600 O  O    A HOH W 4 .   ? 16.982  7.787   11.198  0.81 9.73   ?  924  HOH A O    1 
HETATM 10601 O  O    A HOH W 4 .   ? 31.822  0.999   28.523  0.97 11.30  ?  925  HOH A O    1 
HETATM 10602 O  O    . HOH W 4 .   ? 12.922  -14.060 11.790  1.00 32.93  ?  926  HOH A O    1 
HETATM 10603 O  O    . HOH W 4 .   ? -11.494 -12.937 14.634  1.00 22.88  ?  927  HOH A O    1 
HETATM 10604 O  O    . HOH W 4 .   ? 27.149  -10.437 12.957  1.00 45.52  ?  928  HOH A O    1 
HETATM 10605 O  O    . HOH W 4 .   ? 36.407  1.598   35.361  1.00 36.10  ?  929  HOH A O    1 
HETATM 10606 O  O    . HOH W 4 .   ? 8.708   -0.279  6.218   1.00 45.41  ?  930  HOH A O    1 
HETATM 10607 O  O    . HOH W 4 .   ? -3.120  7.563   36.730  1.00 26.23  ?  931  HOH A O    1 
HETATM 10608 O  O    . HOH W 4 .   ? -8.075  1.831   39.346  1.00 45.62  ?  932  HOH A O    1 
HETATM 10609 O  O    . HOH W 4 .   ? 9.762   -17.131 25.247  1.00 34.27  ?  933  HOH A O    1 
HETATM 10610 O  O    . HOH W 4 .   ? 27.322  35.993  5.509   1.00 16.87  ?  934  HOH A O    1 
HETATM 10611 O  O    . HOH W 4 .   ? 2.059   -23.666 23.046  1.00 36.10  ?  935  HOH A O    1 
HETATM 10612 O  O    A HOH W 4 .   ? -16.869 -6.565  10.437  1.00 44.79  ?  936  HOH A O    1 
HETATM 10613 O  O    . HOH W 4 .   ? 25.530  21.137  22.888  1.00 19.59  ?  937  HOH A O    1 
HETATM 10614 O  O    . HOH W 4 .   ? 27.689  22.983  24.360  1.00 35.66  ?  938  HOH A O    1 
HETATM 10615 O  O    . HOH W 4 .   ? -3.933  5.600   27.551  1.00 10.65  ?  939  HOH A O    1 
HETATM 10616 O  O    A HOH W 4 .   ? -0.246  2.926   6.956   0.84 19.67  ?  940  HOH A O    1 
HETATM 10617 O  O    . HOH W 4 .   ? 27.553  33.322  21.390  1.00 40.12  ?  941  HOH A O    1 
HETATM 10618 O  O    . HOH W 4 .   ? 18.831  -4.046  25.337  1.00 9.21   ?  942  HOH A O    1 
HETATM 10619 O  O    . HOH W 4 .   ? 38.054  2.080   22.696  1.00 28.79  ?  943  HOH A O    1 
HETATM 10620 O  O    . HOH W 4 .   ? 34.797  3.630   34.014  1.00 24.75  ?  944  HOH A O    1 
HETATM 10621 O  O    A HOH W 4 .   ? 11.209  -15.158 27.914  0.57 23.58  ?  945  HOH A O    1 
HETATM 10622 O  O    . HOH W 4 .   ? 6.361   -15.269 14.689  1.00 12.39  ?  946  HOH A O    1 
HETATM 10623 O  O    . HOH W 4 .   ? 5.834   -18.649 28.038  1.00 19.81  ?  947  HOH A O    1 
HETATM 10624 O  O    . HOH W 4 .   ? -9.932  8.150   27.631  1.00 21.16  ?  948  HOH A O    1 
HETATM 10625 O  O    . HOH W 4 .   ? 49.072  5.394   16.151  1.00 44.71  ?  949  HOH A O    1 
HETATM 10626 O  O    . HOH W 4 .   ? 23.244  13.696  25.349  1.00 11.12  ?  950  HOH A O    1 
HETATM 10627 O  O    . HOH W 4 .   ? 33.129  36.397  19.022  1.00 36.97  ?  951  HOH A O    1 
HETATM 10628 O  O    . HOH W 4 .   ? 26.490  16.913  37.306  1.00 42.08  ?  952  HOH A O    1 
HETATM 10629 O  O    . HOH W 4 .   ? 23.918  2.840   34.901  1.00 9.66   ?  953  HOH A O    1 
HETATM 10630 O  O    . HOH W 4 .   ? -2.448  -14.591 21.111  1.00 8.01   ?  954  HOH A O    1 
HETATM 10631 O  O    . HOH W 4 .   ? -8.166  -19.290 31.637  1.00 49.17  ?  955  HOH A O    1 
HETATM 10632 O  O    . HOH W 4 .   ? 10.069  7.004   37.962  1.00 48.60  ?  956  HOH A O    1 
HETATM 10633 O  O    . HOH W 4 .   ? 26.403  38.434  8.121   1.00 28.98  ?  957  HOH A O    1 
HETATM 10634 O  O    . HOH W 4 .   ? 23.592  -13.741 21.601  1.00 43.66  ?  958  HOH A O    1 
HETATM 10635 O  O    . HOH W 4 .   ? 23.056  -8.274  13.441  1.00 14.75  ?  959  HOH A O    1 
HETATM 10636 O  O    . HOH W 4 .   ? -3.828  -2.677  38.648  1.00 20.34  ?  960  HOH A O    1 
HETATM 10637 O  O    . HOH W 4 .   ? 2.002   -9.321  7.092   1.00 48.31  ?  961  HOH A O    1 
HETATM 10638 O  O    . HOH W 4 .   ? 21.652  -8.123  17.927  1.00 7.92   ?  962  HOH A O    1 
HETATM 10639 O  O    . HOH W 4 .   ? 3.937   -7.008  10.714  1.00 15.30  ?  963  HOH A O    1 
HETATM 10640 O  O    . HOH W 4 .   ? 1.086   -7.832  33.865  1.00 14.82  ?  964  HOH A O    1 
HETATM 10641 O  O    . HOH W 4 .   ? 33.489  0.742   14.590  1.00 26.57  ?  965  HOH A O    1 
HETATM 10642 O  O    . HOH W 4 .   ? 4.373   -12.058 31.040  1.00 16.21  ?  966  HOH A O    1 
HETATM 10643 O  O    . HOH W 4 .   ? 43.120  16.935  23.235  1.00 31.15  ?  967  HOH A O    1 
HETATM 10644 O  O    C HOH W 4 .   ? 38.562  8.959   24.016  0.72 28.98  ?  968  HOH A O    1 
HETATM 10645 O  O    . HOH W 4 .   ? 1.197   -15.969 13.413  1.00 11.99  ?  969  HOH A O    1 
HETATM 10646 O  O    A HOH W 4 .   ? 21.840  -9.938  8.898   0.46 12.87  ?  970  HOH A O    1 
HETATM 10647 O  O    . HOH W 4 .   ? -2.057  -5.051  3.901   1.00 25.00  ?  971  HOH A O    1 
HETATM 10648 O  O    . HOH W 4 .   ? 32.396  5.567   23.077  1.00 9.35   ?  972  HOH A O    1 
HETATM 10649 O  O    . HOH W 4 .   ? 30.486  31.245  25.167  1.00 22.24  ?  973  HOH A O    1 
HETATM 10650 O  O    A HOH W 4 .   ? 29.740  15.990  30.708  0.99 27.09  ?  974  HOH A O    1 
HETATM 10651 O  O    . HOH W 4 .   ? 29.976  33.760  6.014   1.00 10.29  ?  975  HOH A O    1 
HETATM 10652 O  O    . HOH W 4 .   ? -14.809 -3.961  24.967  1.00 49.66  ?  976  HOH A O    1 
HETATM 10653 O  O    B HOH W 4 .   ? 14.990  -3.060  37.391  0.65 23.35  ?  977  HOH A O    1 
HETATM 10654 O  O    . HOH W 4 .   ? 32.106  -11.822 16.007  1.00 48.56  ?  978  HOH A O    1 
HETATM 10655 O  O    . HOH W 4 .   ? 33.151  41.472  13.670  1.00 28.35  ?  979  HOH A O    1 
HETATM 10656 O  O    . HOH W 4 .   ? 11.278  -0.944  24.170  1.00 7.28   ?  980  HOH A O    1 
HETATM 10657 O  O    . HOH W 4 .   ? 21.622  11.444  25.185  1.00 11.67  ?  981  HOH A O    1 
HETATM 10658 O  O    . HOH W 4 .   ? 19.481  -7.894  16.269  1.00 8.00   ?  982  HOH A O    1 
HETATM 10659 O  O    . HOH W 4 .   ? 2.656   -17.145 5.633   1.00 9.92   ?  983  HOH A O    1 
HETATM 10660 O  O    . HOH W 4 .   ? 14.006  3.104   35.523  1.00 15.76  ?  984  HOH A O    1 
HETATM 10661 O  O    . HOH W 4 .   ? 44.214  18.199  7.397   1.00 32.80  ?  985  HOH A O    1 
HETATM 10662 O  O    . HOH W 4 .   ? 33.927  5.153   19.693  1.00 13.55  ?  986  HOH A O    1 
HETATM 10663 O  O    . HOH W 4 .   ? -9.844  -17.128 27.966  1.00 30.86  ?  987  HOH A O    1 
HETATM 10664 O  O    . HOH W 4 .   ? 29.811  -7.971  7.342   1.00 12.91  ?  988  HOH A O    1 
HETATM 10665 O  O    B HOH W 4 .   ? 4.340   -3.749  8.318   0.85 61.74  ?  989  HOH A O    1 
HETATM 10666 O  O    . HOH W 4 .   ? 37.345  25.652  22.271  1.00 23.58  ?  990  HOH A O    1 
HETATM 10667 O  O    . HOH W 4 .   ? 19.448  1.008   40.543  1.00 15.60  ?  991  HOH A O    1 
HETATM 10668 O  O    . HOH W 4 .   ? 27.998  -12.174 23.634  1.00 37.61  ?  992  HOH A O    1 
HETATM 10669 O  O    . HOH W 4 .   ? 14.073  -18.380 30.806  1.00 39.46  ?  993  HOH A O    1 
HETATM 10670 O  O    . HOH W 4 .   ? 2.476   -13.406 3.497   1.00 38.19  ?  994  HOH A O    1 
HETATM 10671 O  O    . HOH W 4 .   ? 39.959  35.044  9.100   1.00 16.68  ?  995  HOH A O    1 
HETATM 10672 O  O    . HOH W 4 .   ? -1.155  -0.825  17.052  1.00 7.56   ?  996  HOH A O    1 
HETATM 10673 O  O    . HOH W 4 .   ? -3.219  4.727   7.142   1.00 39.38  ?  997  HOH A O    1 
HETATM 10674 O  O    . HOH W 4 .   ? 32.141  11.940  36.008  1.00 31.29  ?  998  HOH A O    1 
HETATM 10675 O  O    . HOH W 4 .   ? 8.783   -23.063 19.085  1.00 39.54  ?  999  HOH A O    1 
HETATM 10676 O  O    . HOH W 4 .   ? -5.852  13.621  33.147  1.00 44.29  ?  1000 HOH A O    1 
HETATM 10677 O  O    B HOH W 4 .   ? 21.680  -7.219  28.868  0.84 23.52  ?  1001 HOH A O    1 
HETATM 10678 O  O    . HOH W 4 .   ? 36.675  5.713   30.674  1.00 17.98  ?  1002 HOH A O    1 
HETATM 10679 O  O    B HOH W 4 .   ? 22.392  -9.045  9.780   0.57 13.13  ?  1003 HOH A O    1 
HETATM 10680 O  O    . HOH W 4 .   ? 40.679  20.263  14.240  1.00 22.83  ?  1004 HOH A O    1 
HETATM 10681 O  O    . HOH W 4 .   ? 33.229  7.126   6.984   1.00 20.45  ?  1005 HOH A O    1 
HETATM 10682 O  O    . HOH W 4 .   ? 11.491  5.536   36.367  1.00 26.89  ?  1006 HOH A O    1 
HETATM 10683 O  O    A HOH W 4 .   ? 14.916  3.125   38.658  1.00 36.68  ?  1007 HOH A O    1 
HETATM 10684 O  O    . HOH W 4 .   ? -10.347 -10.937 8.787   1.00 16.39  ?  1008 HOH A O    1 
HETATM 10685 O  O    B HOH W 4 .   ? 31.344  15.564  31.145  0.53 17.97  ?  1009 HOH A O    1 
HETATM 10686 O  O    . HOH W 4 .   ? -7.339  -8.129  7.005   1.00 15.84  ?  1010 HOH A O    1 
HETATM 10687 O  O    . HOH W 4 .   ? 21.605  14.025  44.615  1.00 53.83  ?  1011 HOH A O    1 
HETATM 10688 O  O    A HOH W 4 .   ? -8.137  -13.217 33.307  0.96 20.42  ?  1012 HOH A O    1 
HETATM 10689 O  O    . HOH W 4 .   ? 32.722  12.010  7.215   1.00 8.05   ?  1013 HOH A O    1 
HETATM 10690 O  O    . HOH W 4 .   ? -3.660  1.300   39.243  1.00 26.69  ?  1014 HOH A O    1 
HETATM 10691 O  O    . HOH W 4 .   ? 35.218  28.031  22.935  1.00 19.36  ?  1015 HOH A O    1 
HETATM 10692 O  O    . HOH W 4 .   ? -2.541  -7.218  39.952  1.00 20.40  ?  1016 HOH A O    1 
HETATM 10693 O  O    . HOH W 4 .   ? 1.625   3.948   38.753  1.00 43.29  ?  1017 HOH A O    1 
HETATM 10694 O  O    . HOH W 4 .   ? 14.876  -12.929 13.028  1.00 20.63  ?  1018 HOH A O    1 
HETATM 10695 O  O    . HOH W 4 .   ? 21.711  -9.550  21.785  1.00 8.39   ?  1019 HOH A O    1 
HETATM 10696 O  O    B HOH W 4 .   ? 36.671  9.874   25.801  0.82 18.83  ?  1020 HOH A O    1 
HETATM 10697 O  O    . HOH W 4 .   ? -0.509  -0.456  14.415  1.00 13.65  ?  1021 HOH A O    1 
HETATM 10698 O  O    A HOH W 4 .   ? 13.302  -0.756  6.123   1.00 32.89  ?  1022 HOH A O    1 
HETATM 10699 O  O    . HOH W 4 .   ? 9.205   -15.154 10.605  1.00 25.59  ?  1023 HOH A O    1 
HETATM 10700 O  O    A HOH W 4 .   ? 2.413   8.464   7.399   1.00 14.21  ?  1024 HOH A O    1 
HETATM 10701 O  O    . HOH W 4 .   ? 27.587  -10.125 8.545   1.00 33.77  ?  1025 HOH A O    1 
HETATM 10702 O  O    . HOH W 4 .   ? 33.769  5.653   3.689   1.00 15.16  ?  1026 HOH A O    1 
HETATM 10703 O  O    . HOH W 4 .   ? 12.398  -8.652  35.919  1.00 38.33  ?  1027 HOH A O    1 
HETATM 10704 O  O    . HOH W 4 .   ? 27.839  14.970  33.758  1.00 17.25  ?  1028 HOH A O    1 
HETATM 10705 O  O    . HOH W 4 .   ? 8.654   -2.325  33.103  1.00 16.13  ?  1029 HOH A O    1 
HETATM 10706 O  O    . HOH W 4 .   ? 21.659  23.049  14.660  1.00 14.01  ?  1030 HOH A O    1 
HETATM 10707 O  O    . HOH W 4 .   ? 14.957  -7.150  36.079  1.00 20.85  ?  1031 HOH A O    1 
HETATM 10708 O  O    . HOH W 4 .   ? 1.892   -21.277 17.704  1.00 14.05  ?  1032 HOH A O    1 
HETATM 10709 O  O    . HOH W 4 .   ? 10.067  -21.254 14.792  1.00 28.79  ?  1033 HOH A O    1 
HETATM 10710 O  O    A HOH W 4 .   ? -3.318  -19.677 25.453  1.00 30.81  ?  1034 HOH A O    1 
HETATM 10711 O  O    . HOH W 4 .   ? 39.594  16.302  7.739   1.00 31.92  ?  1035 HOH A O    1 
HETATM 10712 O  O    . HOH W 4 .   ? 6.197   -11.470 9.624   1.00 16.86  ?  1036 HOH A O    1 
HETATM 10713 O  O    A HOH W 4 .   ? 3.189   7.805   3.574   1.00 33.52  ?  1037 HOH A O    1 
HETATM 10714 O  O    A HOH W 4 .   ? 26.281  -6.833  28.550  0.50 9.23   ?  1038 HOH A O    1 
HETATM 10715 O  O    . HOH W 4 .   ? -9.879  1.879   31.302  1.00 16.00  ?  1039 HOH A O    1 
HETATM 10716 O  O    A HOH W 4 .   ? -3.915  -22.385 28.772  0.94 40.27  ?  1040 HOH A O    1 
HETATM 10717 O  O    B HOH W 4 .   ? -10.253 1.158   23.227  0.89 26.33  ?  1041 HOH A O    1 
HETATM 10718 O  O    . HOH W 4 .   ? -1.850  11.229  23.315  1.00 17.96  ?  1042 HOH A O    1 
HETATM 10719 O  O    A HOH W 4 .   ? -7.310  -20.104 24.553  1.00 52.25  ?  1043 HOH A O    1 
HETATM 10720 O  O    . HOH W 4 .   ? 7.840   -13.206 13.881  1.00 11.50  ?  1044 HOH A O    1 
HETATM 10721 O  O    . HOH W 4 .   ? 4.280   -23.947 16.484  1.00 45.54  ?  1045 HOH A O    1 
HETATM 10722 O  O    . HOH W 4 .   ? -2.952  14.647  25.358  1.00 20.08  ?  1046 HOH A O    1 
HETATM 10723 O  O    . HOH W 4 .   ? 28.669  35.125  19.379  1.00 34.58  ?  1047 HOH A O    1 
HETATM 10724 O  O    B HOH W 4 .   ? 12.513  -10.012 10.511  0.75 15.00  ?  1048 HOH A O    1 
HETATM 10725 O  O    . HOH W 4 .   ? -12.770 -4.268  31.555  1.00 18.57  ?  1049 HOH A O    1 
HETATM 10726 O  O    C HOH W 4 .   ? 39.295  19.153  18.736  0.70 16.47  ?  1050 HOH A O    1 
HETATM 10727 O  O    . HOH W 4 .   ? 0.418   -9.302  5.161   1.00 37.57  ?  1051 HOH A O    1 
HETATM 10728 O  O    . HOH W 4 .   ? -2.150  -11.400 39.107  1.00 13.96  ?  1052 HOH A O    1 
HETATM 10729 O  O    . HOH W 4 .   ? 29.228  26.889  25.589  1.00 26.59  ?  1053 HOH A O    1 
HETATM 10730 O  O    . HOH W 4 .   ? 6.000   -21.430 27.373  1.00 38.19  ?  1054 HOH A O    1 
HETATM 10731 O  O    A HOH W 4 .   ? 28.071  12.274  35.159  0.60 16.39  ?  1055 HOH A O    1 
HETATM 10732 O  O    . HOH W 4 .   ? 7.425   9.485   33.997  1.00 14.46  ?  1056 HOH A O    1 
HETATM 10733 O  O    A HOH W 4 .   ? 22.801  -6.890  29.581  0.58 10.93  ?  1057 HOH A O    1 
HETATM 10734 O  O    . HOH W 4 .   ? 0.494   5.169   5.524   1.00 29.87  ?  1058 HOH A O    1 
HETATM 10735 O  O    . HOH W 4 .   ? 30.751  41.648  13.191  1.00 41.26  ?  1059 HOH A O    1 
HETATM 10736 O  O    . HOH W 4 .   ? -2.386  -9.888  36.688  1.00 9.84   ?  1060 HOH A O    1 
HETATM 10737 O  O    . HOH W 4 .   ? 33.730  29.640  19.840  1.00 13.37  ?  1061 HOH A O    1 
HETATM 10738 O  O    . HOH W 4 .   ? -3.972  -7.767  37.610  1.00 12.94  ?  1062 HOH A O    1 
HETATM 10739 O  O    . HOH W 4 .   ? 24.073  34.209  10.660  1.00 16.24  ?  1063 HOH A O    1 
HETATM 10740 O  O    . HOH W 4 .   ? 22.498  26.134  17.462  1.00 29.13  ?  1064 HOH A O    1 
HETATM 10741 O  O    . HOH W 4 .   ? 21.039  -5.948  34.186  1.00 11.75  ?  1065 HOH A O    1 
HETATM 10742 O  O    . HOH W 4 .   ? -1.461  9.410   20.312  1.00 11.90  ?  1066 HOH A O    1 
HETATM 10743 O  O    . HOH W 4 .   ? 16.768  18.100  22.443  1.00 22.40  ?  1067 HOH A O    1 
HETATM 10744 O  O    . HOH W 4 .   ? -7.520  1.576   22.358  1.00 8.81   ?  1068 HOH A O    1 
HETATM 10745 O  O    . HOH W 4 .   ? -14.242 -9.641  14.063  1.00 21.98  ?  1069 HOH A O    1 
HETATM 10746 O  O    . HOH W 4 .   ? 18.507  -10.071 17.851  1.00 10.01  ?  1070 HOH A O    1 
HETATM 10747 O  O    . HOH W 4 .   ? -12.789 -0.998  15.921  1.00 49.17  ?  1071 HOH A O    1 
HETATM 10748 O  O    . HOH W 4 .   ? -17.031 -8.704  8.517   1.00 25.38  ?  1072 HOH A O    1 
HETATM 10749 O  O    . HOH W 4 .   ? 14.305  7.348   24.630  1.00 6.20   ?  1073 HOH A O    1 
HETATM 10750 O  O    . HOH W 4 .   ? 35.422  1.383   10.248  1.00 41.20  ?  1074 HOH A O    1 
HETATM 10751 O  O    . HOH W 4 .   ? 23.020  -4.232  33.331  1.00 8.37   ?  1075 HOH A O    1 
HETATM 10752 O  O    . HOH W 4 .   ? -9.114  -17.122 30.381  1.00 22.16  ?  1076 HOH A O    1 
HETATM 10753 O  O    . HOH W 4 .   ? 12.738  1.009   36.713  1.00 21.77  ?  1077 HOH A O    1 
HETATM 10754 O  O    . HOH W 4 .   ? 34.021  -4.583  10.137  1.00 34.00  ?  1078 HOH A O    1 
HETATM 10755 O  O    A HOH W 4 .   ? 34.324  -2.210  10.965  1.00 43.36  ?  1079 HOH A O    1 
HETATM 10756 O  O    . HOH W 4 .   ? 34.009  10.431  4.164   1.00 40.34  ?  1080 HOH A O    1 
HETATM 10757 O  O    A HOH W 4 .   ? 5.895   -9.861  34.360  1.00 49.53  ?  1081 HOH A O    1 
HETATM 10758 O  O    . HOH W 4 .   ? -8.670  8.956   36.232  1.00 28.64  ?  1082 HOH A O    1 
HETATM 10759 O  O    . HOH W 4 .   ? 3.096   -5.896  34.239  1.00 12.64  ?  1083 HOH A O    1 
HETATM 10760 O  O    . HOH W 4 .   ? 45.567  9.827   13.895  1.00 39.63  ?  1084 HOH A O    1 
HETATM 10761 O  O    B HOH W 4 .   ? 7.451   -10.844 33.773  0.99 40.37  ?  1085 HOH A O    1 
HETATM 10762 O  O    A HOH W 4 .   ? 14.466  11.405  13.373  1.00 16.09  ?  1086 HOH A O    1 
HETATM 10763 O  O    . HOH W 4 .   ? 39.587  3.134   16.898  1.00 41.98  ?  1087 HOH A O    1 
HETATM 10764 O  O    . HOH W 4 .   ? 9.840   -17.178 30.094  1.00 52.58  ?  1088 HOH A O    1 
HETATM 10765 O  O    B HOH W 4 .   ? -1.126  -19.444 26.018  0.62 27.52  ?  1089 HOH A O    1 
HETATM 10766 O  O    A HOH W 4 .   ? 14.451  -17.750 19.144  1.00 53.16  ?  1090 HOH A O    1 
HETATM 10767 O  O    A HOH W 4 .   ? 8.065   -9.730  33.109  0.73 17.14  ?  1091 HOH A O    1 
HETATM 10768 O  O    . HOH W 4 .   ? 36.800  19.378  6.385   1.00 24.87  ?  1092 HOH A O    1 
HETATM 10769 O  O    B HOH W 4 .   ? 20.412  -11.021 26.648  0.73 16.04  ?  1093 HOH A O    1 
HETATM 10770 O  O    A HOH W 4 .   ? 15.057  -12.858 15.724  1.00 17.83  ?  1094 HOH A O    1 
HETATM 10771 O  O    . HOH W 4 .   ? -4.151  -2.878  4.797   1.00 19.40  ?  1095 HOH A O    1 
HETATM 10772 O  O    A HOH W 4 .   ? 5.404   -5.545  7.076   0.94 41.15  ?  1096 HOH A O    1 
HETATM 10773 O  O    . HOH W 4 .   ? 3.825   -11.484 6.491   1.00 33.85  ?  1097 HOH A O    1 
HETATM 10774 O  O    . HOH W 4 .   ? -1.331  -23.461 18.980  1.00 51.97  ?  1098 HOH A O    1 
HETATM 10775 O  O    . HOH W 4 .   ? 23.399  15.798  43.144  1.00 34.24  ?  1099 HOH A O    1 
HETATM 10776 O  O    . HOH W 4 .   ? 13.899  21.883  29.880  1.00 36.71  ?  1100 HOH A O    1 
HETATM 10777 O  O    . HOH W 4 .   ? 30.858  -3.970  18.494  1.00 13.14  ?  1101 HOH A O    1 
HETATM 10778 O  O    . HOH W 4 .   ? 9.986   -3.643  5.867   1.00 40.53  ?  1102 HOH A O    1 
HETATM 10779 O  O    . HOH W 4 .   ? -7.873  -15.749 37.245  1.00 32.01  ?  1103 HOH A O    1 
HETATM 10780 O  O    . HOH W 4 .   ? 46.997  10.626  20.058  1.00 33.71  ?  1104 HOH A O    1 
HETATM 10781 O  O    . HOH W 4 .   ? 28.465  -5.233  8.775   1.00 13.76  ?  1105 HOH A O    1 
HETATM 10782 O  O    . HOH W 4 .   ? 14.714  -12.142 32.432  1.00 25.10  ?  1106 HOH A O    1 
HETATM 10783 O  O    . HOH W 4 .   ? 20.337  -8.159  13.679  1.00 10.12  ?  1107 HOH A O    1 
HETATM 10784 O  O    B HOH W 4 .   ? 16.637  -10.560 34.526  1.00 40.65  ?  1108 HOH A O    1 
HETATM 10785 O  O    . HOH W 4 .   ? 26.954  -4.971  31.429  1.00 26.46  ?  1109 HOH A O    1 
HETATM 10786 O  O    . HOH W 4 .   ? -6.548  -11.083 39.523  1.00 24.79  ?  1110 HOH A O    1 
HETATM 10787 O  O    A HOH W 4 .   ? 17.683  -8.572  34.775  1.00 39.92  ?  1111 HOH A O    1 
HETATM 10788 O  O    B HOH W 4 .   ? 36.859  17.167  29.479  1.00 30.77  ?  1112 HOH A O    1 
HETATM 10789 O  O    . HOH W 4 .   ? 40.862  25.237  11.217  1.00 36.21  ?  1113 HOH A O    1 
HETATM 10790 O  O    A HOH W 4 .   ? 42.021  20.038  11.511  1.00 49.20  ?  1114 HOH A O    1 
HETATM 10791 O  O    B HOH W 4 .   ? -10.420 -8.583  35.537  1.00 46.44  ?  1115 HOH A O    1 
HETATM 10792 O  O    . HOH W 4 .   ? 28.114  -11.798 17.053  1.00 43.60  ?  1116 HOH A O    1 
HETATM 10793 O  O    . HOH W 4 .   ? 5.823   -0.572  7.564   1.00 45.47  ?  1117 HOH A O    1 
HETATM 10794 O  O    . HOH W 4 .   ? 35.047  4.661   17.125  1.00 25.50  ?  1118 HOH A O    1 
HETATM 10795 O  O    B HOH W 4 .   ? 29.000  20.083  26.929  1.00 19.21  ?  1119 HOH A O    1 
HETATM 10796 O  O    A HOH W 4 .   ? 42.890  19.721  7.830   0.57 41.20  ?  1120 HOH A O    1 
HETATM 10797 O  O    . HOH W 4 .   ? 5.136   -26.179 20.478  1.00 49.56  ?  1121 HOH A O    1 
HETATM 10798 O  O    B HOH W 4 .   ? 15.267  0.846   39.034  1.00 46.43  ?  1122 HOH A O    1 
HETATM 10799 O  O    A HOH W 4 .   ? 25.832  37.588  12.906  1.00 42.62  ?  1123 HOH A O    1 
HETATM 10800 O  O    B HOH W 4 .   ? 41.651  18.530  20.198  1.00 49.60  ?  1124 HOH A O    1 
HETATM 10801 O  O    . HOH W 4 .   ? -3.120  -9.817  6.288   1.00 16.86  ?  1125 HOH A O    1 
HETATM 10802 O  O    . HOH W 4 .   ? 32.840  -4.470  17.465  1.00 23.14  ?  1126 HOH A O    1 
HETATM 10803 O  O    . HOH W 4 .   ? -7.756  1.429   5.673   1.00 34.65  ?  1127 HOH A O    1 
HETATM 10804 O  O    . HOH W 4 .   ? 16.387  23.418  25.904  1.00 42.54  ?  1128 HOH A O    1 
HETATM 10805 O  O    . HOH W 4 .   ? 13.711  8.140   36.951  1.00 41.47  ?  1129 HOH A O    1 
HETATM 10806 O  O    . HOH W 4 .   ? -13.837 -12.562 21.108  1.00 31.67  ?  1130 HOH A O    1 
HETATM 10807 O  O    A HOH W 4 .   ? -7.850  8.438   22.825  1.00 42.38  ?  1131 HOH A O    1 
HETATM 10808 O  O    . HOH W 4 .   ? 35.229  2.793   13.281  1.00 37.73  ?  1132 HOH A O    1 
HETATM 10809 O  O    B HOH W 4 .   ? 21.585  17.427  15.659  0.18 3.88   ?  1133 HOH A O    1 
HETATM 10810 O  O    . HOH W 4 .   ? -11.943 -0.479  13.913  1.00 49.17  ?  1134 HOH A O    1 
HETATM 10811 O  O    . HOH W 4 .   ? -13.610 -10.238 25.404  1.00 42.30  ?  1135 HOH A O    1 
HETATM 10812 O  O    A HOH W 4 .   ? 42.510  19.297  22.109  1.00 24.09  ?  1136 HOH A O    1 
HETATM 10813 O  O    . HOH W 4 .   ? 21.313  23.782  17.476  1.00 55.29  ?  1137 HOH A O    1 
HETATM 10814 O  O    . HOH W 4 .   ? 17.029  11.234  14.466  1.00 10.81  ?  1138 HOH A O    1 
HETATM 10815 O  O    . HOH W 4 .   ? 24.050  -12.117 26.899  1.00 41.36  ?  1139 HOH A O    1 
HETATM 10816 O  O    A HOH W 4 .   ? 21.366  20.140  20.271  1.00 40.80  ?  1140 HOH A O    1 
HETATM 10817 O  O    . HOH W 4 .   ? 14.973  24.334  29.612  1.00 42.82  ?  1141 HOH A O    1 
HETATM 10818 O  O    . HOH W 4 .   ? 43.700  7.184   27.853  1.00 43.72  ?  1142 HOH A O    1 
HETATM 10819 O  O    . HOH W 4 .   ? 23.621  24.173  21.495  1.00 47.43  ?  1143 HOH A O    1 
HETATM 10820 O  O    B HOH W 4 .   ? 24.549  28.491  18.752  0.98 48.89  ?  1144 HOH A O    1 
HETATM 10821 O  O    . HOH W 4 .   ? -12.541 -14.256 23.052  1.00 36.16  ?  1145 HOH A O    1 
HETATM 10822 O  O    B HOH W 4 .   ? 9.433   1.894   38.916  1.00 53.84  ?  1146 HOH A O    1 
HETATM 10823 O  O    B HOH W 4 .   ? 26.395  -10.461 16.320  1.00 48.26  ?  1147 HOH A O    1 
HETATM 10824 O  O    . HOH W 4 .   ? -1.815  -22.716 31.604  1.00 44.57  ?  1148 HOH A O    1 
HETATM 10825 O  O    . HOH W 4 .   ? 37.636  27.801  21.093  1.00 48.85  ?  1149 HOH A O    1 
HETATM 10826 O  O    . HOH W 4 .   ? -9.076  7.394   39.173  1.00 42.07  ?  1150 HOH A O    1 
HETATM 10827 O  O    . HOH W 4 .   ? 22.285  -12.663 18.652  1.00 35.36  ?  1151 HOH A O    1 
HETATM 10828 O  O    . HOH W 4 .   ? -13.251 -2.195  29.490  1.00 53.84  ?  1152 HOH A O    1 
HETATM 10829 O  O    . HOH W 4 .   ? -12.230 -15.992 28.214  1.00 38.97  ?  1153 HOH A O    1 
HETATM 10830 O  O    . HOH W 4 .   ? -1.554  -21.231 23.994  1.00 27.99  ?  1154 HOH A O    1 
HETATM 10831 O  O    . HOH W 4 .   ? 24.149  6.816   41.722  1.00 39.47  ?  1155 HOH A O    1 
HETATM 10832 O  O    . HOH W 4 .   ? 30.002  14.561  34.914  1.00 37.82  ?  1156 HOH A O    1 
HETATM 10833 O  O    . HOH W 4 .   ? 1.546   -18.207 35.207  1.00 36.87  ?  1157 HOH A O    1 
HETATM 10834 O  O    . HOH W 4 .   ? -13.689 2.972   36.846  1.00 48.41  ?  1158 HOH A O    1 
HETATM 10835 O  O    A HOH W 4 .   ? -1.851  9.054   1.710   0.79 30.78  ?  1159 HOH A O    1 
HETATM 10836 O  O    . HOH W 4 .   ? 1.436   12.984  34.218  1.00 47.56  ?  1160 HOH A O    1 
HETATM 10837 O  O    A HOH W 4 .   ? -10.825 -3.937  37.837  0.99 49.47  ?  1161 HOH A O    1 
HETATM 10838 O  O    . HOH W 4 .   ? 10.080  -7.074  37.668  1.00 43.62  ?  1162 HOH A O    1 
HETATM 10839 O  O    . HOH W 4 .   ? 33.285  -10.264 -0.753  1.00 14.54  ?  1163 HOH A O    1 
HETATM 10840 O  O    B HOH W 4 .   ? -7.757  9.501   24.362  1.00 48.30  ?  1164 HOH A O    1 
HETATM 10841 O  O    B HOH W 4 .   ? 10.625  -17.185 27.705  0.76 35.12  ?  1165 HOH A O    1 
HETATM 10842 O  O    A HOH W 4 .   ? -12.892 -0.182  32.193  0.79 34.69  ?  1166 HOH A O    1 
HETATM 10843 O  O    B HOH W 4 .   ? 39.920  15.436  27.769  1.00 52.13  ?  1167 HOH A O    1 
HETATM 10844 O  O    . HOH W 4 .   ? 24.045  -10.791 12.710  1.00 43.48  ?  1168 HOH A O    1 
HETATM 10845 O  O    C HOH W 4 .   ? 15.584  -10.909 9.489   1.00 32.24  ?  1169 HOH A O    1 
HETATM 10846 O  O    . HOH W 4 .   ? 15.169  9.907   39.026  1.00 57.40  ?  1170 HOH A O    1 
HETATM 10847 O  O    . HOH W 4 .   ? 43.467  8.683   10.618  1.00 28.42  ?  1171 HOH A O    1 
HETATM 10848 O  O    . HOH W 4 .   ? -12.920 10.004  33.506  1.00 52.65  ?  1172 HOH A O    1 
HETATM 10849 O  O    . HOH W 4 .   ? 27.976  -10.539 10.808  1.00 37.02  ?  1173 HOH A O    1 
HETATM 10850 O  O    . HOH W 4 .   ? -16.488 -8.207  12.750  1.00 42.30  ?  1174 HOH A O    1 
HETATM 10851 O  O    B HOH W 4 .   ? 9.912   -22.258 22.430  0.81 32.55  ?  1175 HOH A O    1 
HETATM 10852 O  O    B HOH W 4 .   ? 34.563  -0.765  9.530   1.00 40.32  ?  1176 HOH A O    1 
HETATM 10853 O  O    . HOH W 4 .   ? -2.517  1.602   6.057   1.00 25.14  ?  1177 HOH A O    1 
HETATM 10854 O  O    B HOH W 4 .   ? 2.581   11.949  20.982  0.41 11.93  ?  1178 HOH A O    1 
HETATM 10855 O  O    A HOH W 4 .   ? 22.008  -11.862 24.073  1.00 53.04  ?  1179 HOH A O    1 
HETATM 10856 O  O    . HOH W 4 .   ? -0.183  11.317  36.304  1.00 33.36  ?  1180 HOH A O    1 
HETATM 10857 O  O    . HOH W 4 .   ? 3.255   -24.642 27.092  1.00 41.20  ?  1181 HOH A O    1 
HETATM 10858 O  O    C HOH W 4 .   ? 46.252  12.099  22.228  0.74 35.95  ?  1182 HOH A O    1 
HETATM 10859 O  O    . HOH W 4 .   ? 20.400  -9.969  11.544  1.00 18.88  ?  1183 HOH A O    1 
HETATM 10860 O  O    . HOH W 4 .   ? 37.424  26.584  13.279  1.00 37.39  ?  1184 HOH A O    1 
HETATM 10861 O  O    B HOH W 4 .   ? 46.367  13.695  10.378  1.00 50.48  ?  1185 HOH A O    1 
HETATM 10862 O  O    A HOH W 4 .   ? 17.273  -12.340 17.235  0.88 23.58  ?  1186 HOH A O    1 
HETATM 10863 O  O    . HOH W 4 .   ? 8.450   -18.514 28.662  1.00 46.30  ?  1187 HOH A O    1 
HETATM 10864 O  O    A HOH W 4 .   ? 2.576   -4.787  36.792  1.00 30.20  ?  1188 HOH A O    1 
HETATM 10865 O  O    . HOH W 4 .   ? 35.214  5.396   6.042   1.00 24.90  ?  1189 HOH A O    1 
HETATM 10866 O  O    . HOH W 4 .   ? 34.952  -5.492  19.077  1.00 38.70  ?  1190 HOH A O    1 
HETATM 10867 O  O    A HOH W 4 .   ? 4.116   -1.230  35.975  0.83 18.17  ?  1191 HOH A O    1 
HETATM 10868 O  O    . HOH W 4 .   ? 28.119  38.306  4.528   1.00 22.54  ?  1192 HOH A O    1 
HETATM 10869 O  O    A HOH W 4 .   ? 38.447  15.664  29.259  1.00 54.49  ?  1193 HOH A O    1 
HETATM 10870 O  O    B HOH W 4 .   ? 48.166  8.769   19.478  0.97 34.97  ?  1194 HOH A O    1 
HETATM 10871 O  O    . HOH W 4 .   ? -1.250  -7.395  3.726   1.00 32.44  ?  1195 HOH A O    1 
HETATM 10872 O  O    . HOH W 4 .   ? 11.541  -20.669 16.990  1.00 43.75  ?  1196 HOH A O    1 
HETATM 10873 O  O    . HOH W 4 .   ? -8.774  -9.434  37.045  1.00 29.82  ?  1197 HOH A O    1 
HETATM 10874 O  O    A HOH W 4 .   ? 36.880  9.302   24.470  0.60 16.77  ?  1198 HOH A O    1 
HETATM 10875 O  O    B HOH W 4 .   ? 20.168  18.343  20.880  1.00 59.86  ?  1199 HOH A O    1 
HETATM 10876 O  O    A HOH W 4 .   ? 27.517  21.586  26.325  1.00 37.56  ?  1200 HOH A O    1 
HETATM 10877 O  O    . HOH W 4 .   ? 2.270   14.367  32.281  1.00 39.63  ?  1201 HOH A O    1 
HETATM 10878 O  O    A HOH W 4 .   ? 26.566  41.874  6.267   1.00 44.77  ?  1202 HOH A O    1 
HETATM 10879 O  O    . HOH W 4 .   ? -10.000 2.283   6.948   1.00 41.67  ?  1203 HOH A O    1 
HETATM 10880 O  O    . HOH W 4 .   ? 5.077   11.332  34.322  1.00 30.05  ?  1204 HOH A O    1 
HETATM 10881 O  O    . HOH W 4 .   ? -9.904  -11.416 34.362  1.00 39.08  ?  1205 HOH A O    1 
HETATM 10882 O  O    C HOH W 4 .   ? 20.435  20.921  18.582  0.99 52.57  ?  1206 HOH A O    1 
HETATM 10883 O  O    . HOH W 4 .   ? -8.183  -17.599 35.070  1.00 44.66  ?  1207 HOH A O    1 
HETATM 10884 O  O    B HOH W 4 .   ? 35.110  13.985  4.804   1.00 42.97  ?  1208 HOH A O    1 
HETATM 10885 O  O    B HOH W 4 .   ? 10.460  2.182   6.158   1.00 51.29  ?  1209 HOH A O    1 
HETATM 10886 O  O    B HOH W 4 .   ? 15.210  0.172   6.792   0.64 25.04  ?  1210 HOH A O    1 
HETATM 10887 O  O    . HOH W 4 .   ? 44.425  10.361  9.017   1.00 47.74  ?  1211 HOH A O    1 
HETATM 10888 O  O    . HOH W 4 .   ? 16.684  14.628  30.892  1.00 26.94  ?  1212 HOH A O    1 
HETATM 10889 O  O    B HOH W 4 .   ? 5.047   -2.166  36.239  0.92 45.29  ?  1213 HOH A O    1 
HETATM 10890 O  O    B HOH W 4 .   ? 19.224  12.886  35.583  0.95 39.44  ?  1214 HOH A O    1 
HETATM 10891 O  O    . HOH W 4 .   ? 35.324  30.258  17.814  1.00 25.62  ?  1215 HOH A O    1 
HETATM 10892 O  O    . HOH W 4 .   ? 32.202  20.142  30.156  1.00 45.30  ?  1216 HOH A O    1 
HETATM 10893 O  O    . HOH W 4 .   ? 36.167  0.484   18.222  1.00 44.50  ?  1217 HOH A O    1 
HETATM 10894 O  O    . HOH W 4 .   ? 20.679  -11.335 7.100   1.00 39.67  ?  1218 HOH A O    1 
HETATM 10895 O  O    . HOH W 4 .   ? 6.722   3.301   6.912   1.00 22.71  ?  1219 HOH A O    1 
HETATM 10896 O  O    A HOH W 4 .   ? 17.991  19.893  20.406  1.00 66.33  ?  1220 HOH A O    1 
HETATM 10897 O  O    . HOH W 4 .   ? 40.238  4.379   23.409  1.00 37.38  ?  1221 HOH A O    1 
HETATM 10898 O  O    . HOH W 4 .   ? 7.354   -6.762  6.407   1.00 56.51  ?  1222 HOH A O    1 
HETATM 10899 O  O    . HOH W 4 .   ? 2.276   7.997   0.892   1.00 32.87  ?  1223 HOH A O    1 
HETATM 10900 O  O    . HOH W 4 .   ? 39.208  22.531  7.172   1.00 40.17  ?  1224 HOH A O    1 
HETATM 10901 O  O    . HOH W 4 .   ? 2.908   -11.046 40.392  1.00 34.83  ?  1225 HOH A O    1 
HETATM 10902 O  O    . HOH W 4 .   ? 37.967  29.050  18.644  1.00 54.62  ?  1226 HOH A O    1 
HETATM 10903 O  O    . HOH W 4 .   ? -15.177 -8.452  28.486  1.00 42.22  ?  1227 HOH A O    1 
HETATM 10904 O  O    . HOH W 4 .   ? 37.449  -3.673  26.688  1.00 51.22  ?  1228 HOH A O    1 
HETATM 10905 O  O    A HOH W 4 .   ? 7.485   -1.859  35.336  0.85 29.58  ?  1229 HOH A O    1 
HETATM 10906 O  O    B HOH W 4 .   ? 16.233  2.067   7.394   0.93 36.13  ?  1230 HOH A O    1 
HETATM 10907 O  O    . HOH W 4 .   ? -13.430 -10.663 19.234  1.00 45.66  ?  1231 HOH A O    1 
HETATM 10908 O  O    . HOH W 4 .   ? -3.529  -0.497  3.773   1.00 47.29  ?  1232 HOH A O    1 
HETATM 10909 O  O    . HOH W 4 .   ? -16.627 -1.605  9.245   1.00 49.52  ?  1233 HOH A O    1 
HETATM 10910 O  O    . HOH W 4 .   ? 32.168  15.338  33.448  1.00 38.97  ?  1234 HOH A O    1 
HETATM 10911 O  O    A HOH W 4 .   ? 42.288  15.100  26.213  1.00 42.95  ?  1235 HOH A O    1 
HETATM 10912 O  O    . HOH W 4 .   ? 22.720  35.793  7.096   1.00 45.01  ?  1236 HOH A O    1 
HETATM 10913 O  O    . HOH W 4 .   ? 35.311  -1.460  14.388  1.00 44.61  ?  1237 HOH A O    1 
HETATM 10914 O  O    B HOH W 4 .   ? -8.888  -19.826 24.110  1.00 53.51  ?  1238 HOH A O    1 
HETATM 10915 O  O    . HOH W 4 .   ? 9.419   16.470  32.942  1.00 50.63  ?  1239 HOH A O    1 
HETATM 10916 O  O    . HOH W 4 .   ? -12.419 1.935   30.771  1.00 38.83  ?  1240 HOH A O    1 
HETATM 10917 O  O    . HOH W 4 .   ? 3.474   -21.597 34.641  1.00 24.23  ?  1241 HOH A O    1 
HETATM 10918 O  O    A HOH W 4 .   ? 8.480   -22.783 21.491  0.54 25.62  ?  1242 HOH A O    1 
HETATM 10919 O  O    . HOH W 4 .   ? 1.698   -25.075 20.602  1.00 54.75  ?  1243 HOH A O    1 
HETATM 10920 O  O    . HOH W 4 .   ? 2.969   4.899   4.478   1.00 25.84  ?  1244 HOH A O    1 
HETATM 10921 O  O    . HOH W 4 .   ? 36.583  -1.658  22.554  1.00 30.14  ?  1245 HOH A O    1 
HETATM 10922 O  O    . HOH W 4 .   ? 27.731  7.571   38.858  1.00 24.00  ?  1246 HOH A O    1 
HETATM 10923 O  O    . HOH W 4 .   ? 39.303  8.939   29.522  1.00 52.62  ?  1247 HOH A O    1 
HETATM 10924 O  O    . HOH W 4 .   ? -10.179 -19.907 27.016  1.00 52.10  ?  1248 HOH A O    1 
HETATM 10925 O  O    . HOH W 4 .   ? 15.587  -19.876 21.889  1.00 57.14  ?  1249 HOH A O    1 
HETATM 10926 O  O    . HOH W 4 .   ? 32.475  -4.036  8.029   1.00 21.41  ?  1250 HOH A O    1 
HETATM 10927 O  O    C HOH W 4 .   ? 16.176  13.595  27.031  0.46 10.46  ?  1251 HOH A O    1 
HETATM 10928 O  O    . HOH W 4 .   ? 5.685   -22.558 12.601  1.00 36.31  ?  1252 HOH A O    1 
HETATM 10929 O  O    . HOH W 4 .   ? -5.913  -7.144  4.309   1.00 29.60  ?  1253 HOH A O    1 
HETATM 10930 O  O    B HOH W 4 .   ? 34.034  -7.062  21.003  0.73 24.31  ?  1254 HOH A O    1 
HETATM 10931 O  O    . HOH W 4 .   ? 36.962  1.900   37.578  1.00 39.36  ?  1255 HOH A O    1 
HETATM 10932 O  O    . HOH W 4 .   ? 40.420  24.005  9.418   1.00 83.29  ?  1256 HOH A O    1 
HETATM 10933 O  O    . HOH W 4 .   ? -2.114  -21.978 16.501  1.00 28.21  ?  1257 HOH A O    1 
HETATM 10934 O  O    . HOH W 4 .   ? 24.877  33.911  15.943  1.00 36.04  ?  1258 HOH A O    1 
HETATM 10935 O  O    B HOH W 4 .   ? 8.711   -1.837  35.798  0.31 9.04   ?  1259 HOH A O    1 
HETATM 10936 O  O    . HOH W 4 .   ? 4.740   7.862   36.950  1.00 45.33  ?  1260 HOH A O    1 
HETATM 10937 O  O    . HOH W 4 .   ? 34.372  30.436  22.344  1.00 22.33  ?  1261 HOH A O    1 
HETATM 10938 O  O    . HOH W 4 .   ? -5.572  -10.245 7.491   1.00 16.91  ?  1262 HOH A O    1 
HETATM 10939 O  O    . HOH W 4 .   ? 49.741  6.856   18.185  1.00 35.39  ?  1263 HOH A O    1 
HETATM 10940 O  O    . HOH W 4 .   ? 29.532  18.528  29.388  1.00 47.08  ?  1264 HOH A O    1 
HETATM 10941 O  O    . HOH W 4 .   ? 32.648  40.746  16.255  1.00 40.47  ?  1265 HOH A O    1 
HETATM 10942 O  O    . HOH W 4 .   ? 36.628  20.213  29.766  1.00 46.77  ?  1266 HOH A O    1 
HETATM 10943 O  O    . HOH W 4 .   ? 19.860  17.390  36.946  1.00 32.63  ?  1267 HOH A O    1 
HETATM 10944 O  O    . HOH W 4 .   ? 33.102  30.889  24.798  1.00 16.50  ?  1268 HOH A O    1 
HETATM 10945 O  O    . HOH W 4 .   ? 20.859  -10.514 19.271  1.00 13.76  ?  1269 HOH A O    1 
HETATM 10946 O  O    C HOH W 4 .   ? 22.283  28.362  17.646  1.00 44.97  ?  1270 HOH A O    1 
HETATM 10947 O  O    . HOH W 4 .   ? 36.695  8.377   29.772  1.00 22.36  ?  1271 HOH A O    1 
HETATM 10948 O  O    . HOH W 4 .   ? 17.786  12.327  33.485  1.00 29.37  ?  1272 HOH A O    1 
HETATM 10949 O  O    . HOH W 4 .   ? 2.230   -20.884 14.921  1.00 16.82  ?  1273 HOH A O    1 
HETATM 10950 O  O    . HOH W 4 .   ? -13.248 -3.711  34.307  1.00 43.05  ?  1274 HOH A O    1 
HETATM 10951 O  O    . HOH W 4 .   ? 36.064  28.045  25.738  1.00 22.21  ?  1275 HOH A O    1 
HETATM 10952 O  O    . HOH W 4 .   ? -6.076  -4.479  3.698   1.00 27.76  ?  1276 HOH A O    1 
HETATM 10953 O  O    . HOH W 4 .   ? -5.830  -14.816 40.291  1.00 29.09  ?  1277 HOH A O    1 
HETATM 10954 O  O    . HOH W 4 .   ? 34.241  -5.793  29.823  1.00 41.70  ?  1278 HOH A O    1 
HETATM 10955 O  O    . HOH W 4 .   ? 0.201   -9.293  36.102  1.00 13.20  ?  1279 HOH A O    1 
HETATM 10956 O  O    . HOH W 4 .   ? -6.591  -8.581  38.389  1.00 18.84  ?  1280 HOH A O    1 
HETATM 10957 O  O    . HOH W 4 .   ? 33.456  2.805   3.307   1.00 29.13  ?  1281 HOH A O    1 
HETATM 10958 O  O    . HOH W 4 .   ? 24.142  -5.916  31.561  1.00 22.12  ?  1282 HOH A O    1 
HETATM 10959 O  O    . HOH W 4 .   ? 36.781  23.084  6.000   1.00 19.92  ?  1283 HOH A O    1 
HETATM 10960 O  O    . HOH W 4 .   ? -2.089  -21.422 13.875  1.00 21.61  ?  1284 HOH A O    1 
HETATM 10961 O  O    C HOH W 4 .   ? 3.393   -3.290  37.490  0.93 38.37  ?  1285 HOH A O    1 
HETATM 10962 O  O    . HOH W 4 .   ? 2.482   1.289   5.671   1.00 33.77  ?  1286 HOH A O    1 
HETATM 10963 O  O    . HOH W 4 .   ? -8.058  15.529  31.074  1.00 53.66  ?  1287 HOH A O    1 
HETATM 10964 O  O    . HOH W 4 .   ? 32.885  18.470  32.052  1.00 44.90  ?  1288 HOH A O    1 
HETATM 10965 O  O    . HOH W 4 .   ? 10.158  -17.826 8.616   1.00 51.07  ?  1289 HOH A O    1 
HETATM 10966 O  O    A HOH W 4 .   ? 15.357  -5.181  37.746  0.94 38.79  ?  1290 HOH A O    1 
HETATM 10967 O  O    B HOH W 4 .   ? -18.614 -5.775  10.959  1.00 56.65  ?  1291 HOH A O    1 
HETATM 10968 O  O    . HOH W 4 .   ? 36.699  22.811  25.669  1.00 28.26  ?  1292 HOH A O    1 
HETATM 10969 O  O    . HOH W 4 .   ? 33.021  0.401   6.070   1.00 32.89  ?  1293 HOH A O    1 
HETATM 10970 O  O    . HOH W 4 .   ? -5.510  -22.377 23.698  1.00 51.14  ?  1294 HOH A O    1 
HETATM 10971 O  O    . HOH W 4 .   ? 39.283  19.327  6.583   1.00 43.04  ?  1295 HOH A O    1 
HETATM 10972 O  O    . HOH W 4 .   ? -0.711  8.941   37.210  1.00 40.27  ?  1296 HOH A O    1 
HETATM 10973 O  O    . HOH W 4 .   ? -3.689  -8.326  4.078   1.00 22.02  ?  1297 HOH A O    1 
HETATM 10974 O  O    B HOH W 4 .   ? 25.416  5.143   40.619  0.62 27.40  ?  1298 HOH A O    1 
HETATM 10975 O  O    . HOH W 4 .   ? -14.370 -6.728  31.781  1.00 59.25  ?  1299 HOH A O    1 
HETATM 10976 O  O    B HOH W 4 .   ? 38.393  -2.496  29.987  0.65 32.17  ?  1300 HOH A O    1 
HETATM 10977 O  O    A HOH W 4 .   ? -9.105  -19.966 22.046  0.99 37.90  ?  1301 HOH A O    1 
HETATM 10978 O  O    . HOH W 4 .   ? 2.065   -5.209  4.575   1.00 32.27  ?  1302 HOH A O    1 
HETATM 10979 O  O    A HOH W 4 .   ? 12.326  2.678   6.832   0.85 29.90  ?  1303 HOH A O    1 
HETATM 10980 O  O    . HOH W 4 .   ? 40.112  2.778   25.334  1.00 46.36  ?  1304 HOH A O    1 
HETATM 10981 O  O    . HOH W 4 .   ? 17.855  25.693  33.173  1.00 39.66  ?  1305 HOH A O    1 
HETATM 10982 O  O    . HOH W 4 .   ? 36.862  17.066  5.368   1.00 32.30  ?  1306 HOH A O    1 
HETATM 10983 O  O    . HOH W 4 .   ? -6.276  -12.801 9.502   1.00 13.70  ?  1307 HOH A O    1 
HETATM 10984 O  O    B HOH W 4 .   ? 29.433  -10.093 21.500  0.54 24.61  ?  1308 HOH A O    1 
HETATM 10985 O  O    . HOH W 4 .   ? -8.450  4.275   11.545  1.00 28.16  ?  1309 HOH A O    1 
HETATM 10986 O  O    . HOH W 4 .   ? 31.397  4.886   38.817  1.00 21.86  ?  1310 HOH A O    1 
HETATM 10987 O  O    . HOH W 4 .   ? 39.311  5.037   30.795  1.00 37.02  ?  1311 HOH A O    1 
HETATM 10988 O  O    . HOH W 4 .   ? -14.137 -12.010 12.679  1.00 43.85  ?  1312 HOH A O    1 
HETATM 10989 O  O    . HOH W 4 .   ? 30.782  -8.167  -4.339  1.00 4.48   ?  1313 HOH A O    1 
HETATM 10990 O  O    . HOH W 4 .   ? -3.004  5.652   38.297  1.00 28.70  ?  1314 HOH A O    1 
HETATM 10991 O  O    A HOH W 4 .   ? 3.017   -2.209  7.672   0.97 27.81  ?  1315 HOH A O    1 
HETATM 10992 O  O    A HOH W 4 .   ? -9.536  -15.567 32.624  0.97 39.03  ?  1316 HOH A O    1 
HETATM 10993 O  O    . HOH W 4 .   ? -10.365 11.326  28.921  1.00 51.80  ?  1317 HOH A O    1 
HETATM 10994 O  O    . HOH W 4 .   ? 35.096  -6.516  26.959  1.00 47.33  ?  1318 HOH A O    1 
HETATM 10995 O  O    A HOH W 4 .   ? -10.035 2.649   22.802  0.59 21.85  ?  1319 HOH A O    1 
HETATM 10996 O  O    B HOH W 4 .   ? -13.632 -0.915  33.668  0.62 35.35  ?  1320 HOH A O    1 
HETATM 10997 O  O    . HOH W 4 .   ? -4.593  2.779   7.245   1.00 37.16  ?  1321 HOH A O    1 
HETATM 10998 O  O    . HOH W 4 .   ? 8.918   11.800  33.711  1.00 39.32  ?  1322 HOH A O    1 
HETATM 10999 O  O    . HOH W 4 .   ? -9.343  5.296   20.382  1.00 28.03  ?  1323 HOH A O    1 
HETATM 11000 O  O    . HOH W 4 .   ? 2.464   -5.125  9.321   1.00 17.14  ?  1324 HOH A O    1 
HETATM 11001 O  O    A HOH W 4 .   ? -8.574  -8.622  4.106   0.94 16.01  ?  1325 HOH A O    1 
HETATM 11002 O  O    . HOH W 4 .   ? -5.694  17.584  28.067  1.00 16.44  ?  1326 HOH A O    1 
HETATM 11003 O  O    . HOH W 4 .   ? -7.548  -6.689  40.290  1.00 40.37  ?  1327 HOH A O    1 
HETATM 11004 O  O    . HOH W 4 .   ? -10.842 -17.726 23.028  1.00 48.01  ?  1328 HOH A O    1 
HETATM 11005 O  O    . HOH W 4 .   ? 14.545  21.216  25.704  1.00 48.90  ?  1329 HOH A O    1 
HETATM 11006 O  O    . HOH W 4 .   ? 1.775   -23.886 18.255  1.00 26.53  ?  1330 HOH A O    1 
HETATM 11007 O  O    . HOH W 4 .   ? 39.807  4.880   7.764   1.00 29.09  ?  1331 HOH A O    1 
HETATM 11008 O  O    B HOH W 4 .   ? 22.270  -10.817 29.258  1.00 68.62  ?  1332 HOH A O    1 
HETATM 11009 O  O    B HOH W 4 .   ? 37.664  25.786  10.616  1.00 37.27  ?  1333 HOH A O    1 
HETATM 11010 O  O    . HOH W 4 .   ? 2.742   -23.404 14.415  1.00 62.47  ?  1334 HOH A O    1 
HETATM 11011 O  O    . HOH W 4 .   ? 34.321  10.173  36.100  1.00 38.07  ?  1335 HOH A O    1 
HETATM 11012 O  O    . HOH W 4 .   ? 10.986  -22.504 18.107  1.00 49.80  ?  1336 HOH A O    1 
HETATM 11013 O  O    B HOH W 4 .   ? 47.236  11.169  22.917  0.75 36.51  ?  1337 HOH A O    1 
HETATM 11014 O  O    B HOH W 4 .   ? 14.604  -19.996 19.162  1.00 52.95  ?  1338 HOH A O    1 
HETATM 11015 O  O    . HOH W 4 .   ? -12.404 -11.185 31.356  1.00 56.83  ?  1339 HOH A O    1 
HETATM 11016 O  O    . HOH W 4 .   ? -2.568  11.478  2.803   1.00 32.57  ?  1340 HOH A O    1 
HETATM 11017 O  O    . HOH W 4 .   ? 10.603  -4.781  38.814  1.00 44.12  ?  1341 HOH A O    1 
HETATM 11018 O  O    . HOH W 4 .   ? 26.503  27.247  22.004  1.00 25.30  ?  1342 HOH A O    1 
HETATM 11019 O  O    . HOH W 4 .   ? 3.833   -9.429  5.353   1.00 42.83  ?  1343 HOH A O    1 
HETATM 11020 O  O    A HOH W 4 .   ? 36.166  -2.850  29.006  1.00 51.80  ?  1344 HOH A O    1 
HETATM 11021 O  O    . HOH W 4 .   ? -9.374  2.455   19.269  1.00 15.94  ?  1345 HOH A O    1 
HETATM 11022 O  O    . HOH W 4 .   ? -12.269 -3.764  -1.837  1.00 45.94  ?  1346 HOH A O    1 
HETATM 11023 O  O    . HOH W 4 .   ? -0.869  -23.411 24.832  1.00 43.66  ?  1347 HOH A O    1 
HETATM 11024 O  O    . HOH W 4 .   ? -11.419 1.733   20.947  1.00 42.44  ?  1348 HOH A O    1 
HETATM 11025 O  O    . HOH W 4 .   ? -12.828 1.549   27.918  1.00 45.65  ?  1349 HOH A O    1 
HETATM 11026 O  O    . HOH W 4 .   ? -12.265 4.785   25.218  1.00 27.85  ?  1350 HOH A O    1 
HETATM 11027 O  O    . HOH W 4 .   ? 38.542  1.072   31.905  1.00 36.99  ?  1351 HOH A O    1 
HETATM 11028 O  O    . HOH W 4 .   ? -14.889 -10.331 16.359  1.00 53.08  ?  1352 HOH A O    1 
HETATM 11029 O  O    . HOH W 4 .   ? -10.699 -6.030  39.343  1.00 34.43  ?  1353 HOH A O    1 
HETATM 11030 O  O    . HOH W 4 .   ? -11.728 7.419   25.693  1.00 28.90  ?  1354 HOH A O    1 
HETATM 11031 O  O    . HOH W 4 .   ? 13.481  -18.987 17.052  1.00 39.74  ?  1355 HOH A O    1 
HETATM 11032 O  O    . HOH W 4 .   ? 5.091   -7.898  7.117   1.00 35.64  ?  1356 HOH A O    1 
HETATM 11033 O  O    B HOH W 4 .   ? -11.697 -3.982  36.143  1.00 41.85  ?  1357 HOH A O    1 
HETATM 11034 O  O    . HOH W 4 .   ? 36.024  6.207   33.150  1.00 29.29  ?  1358 HOH A O    1 
HETATM 11035 O  O    . HOH W 4 .   ? -1.937  16.336  32.993  1.00 43.42  ?  1359 HOH A O    1 
HETATM 11036 O  O    . HOH W 4 .   ? 38.108  21.707  28.739  1.00 50.30  ?  1360 HOH A O    1 
HETATM 11037 O  O    . HOH W 4 .   ? 16.991  -13.349 11.646  1.00 37.30  ?  1361 HOH A O    1 
HETATM 11038 O  O    . HOH W 4 .   ? 2.870   11.589  36.491  1.00 40.50  ?  1362 HOH A O    1 
HETATM 11039 O  O    A HOH W 4 .   ? 35.264  9.171   33.346  1.00 38.78  ?  1363 HOH A O    1 
HETATM 11040 O  O    . HOH W 4 .   ? 7.708   -12.233 7.394   1.00 29.09  ?  1364 HOH A O    1 
HETATM 11041 O  O    . HOH W 4 .   ? -0.032  -3.557  1.958   1.00 45.75  ?  1365 HOH A O    1 
HETATM 11042 O  O    . HOH W 4 .   ? -4.215  -24.182 19.708  1.00 43.69  ?  1366 HOH A O    1 
HETATM 11043 O  O    . HOH W 4 .   ? -7.802  3.119   8.318   1.00 34.01  ?  1367 HOH A O    1 
HETATM 11044 O  O    . HOH W 4 .   ? -9.962  3.970   9.360   1.00 44.02  ?  1368 HOH A O    1 
HETATM 11045 O  O    A HOH W 4 .   ? 9.500   -0.776  37.008  1.00 42.88  ?  1369 HOH A O    1 
HETATM 11046 O  O    A HOH W 4 .   ? -11.119 -7.667  37.502  1.00 45.64  ?  1370 HOH A O    1 
HETATM 11047 O  O    . HOH W 4 .   ? 3.197   -3.065  4.956   1.00 64.30  ?  1371 HOH A O    1 
HETATM 11048 O  O    . HOH W 4 .   ? 20.231  -13.217 21.159  1.00 41.98  ?  1372 HOH A O    1 
HETATM 11049 O  O    . HOH W 4 .   ? 26.592  25.828  23.891  1.00 45.66  ?  1373 HOH A O    1 
HETATM 11050 O  O    . HOH W 4 .   ? 29.702  9.443   39.251  1.00 34.91  ?  1374 HOH A O    1 
HETATM 11051 O  O    . HOH W 4 .   ? -8.370  17.715  28.205  1.00 31.78  ?  1375 HOH A O    1 
HETATM 11052 O  O    . HOH W 4 .   ? 39.084  -3.601  33.718  1.00 34.96  ?  1376 HOH A O    1 
HETATM 11053 O  O    . HOH W 4 .   ? 14.238  24.827  27.383  1.00 55.39  ?  1377 HOH A O    1 
HETATM 11054 O  O    . HOH W 4 .   ? 0.016   -23.036 14.344  1.00 37.02  ?  1378 HOH A O    1 
HETATM 11055 O  O    B HOH W 4 .   ? -11.717 -15.020 31.686  1.00 51.27  ?  1379 HOH A O    1 
HETATM 11056 O  O    A HOH W 4 .   ? 39.156  -0.992  30.715  0.90 39.10  ?  1380 HOH A O    1 
HETATM 11057 O  O    . HOH W 4 .   ? -0.034  -24.553 16.509  1.00 53.41  ?  1381 HOH A O    1 
HETATM 11058 O  O    . HOH W 4 .   ? 36.156  -1.022  7.312   1.00 56.47  ?  1382 HOH A O    1 
HETATM 11059 O  O    C HOH X 4 .   ? 12.075  20.691  -9.979  0.33 5.79   ?  701  HOH B O    1 
HETATM 11060 O  O    A HOH X 4 .   ? 10.104  9.290   13.673  0.59 13.74  ?  702  HOH B O    1 
HETATM 11061 O  O    B HOH X 4 .   ? 12.681  15.917  25.634  0.81 21.98  ?  703  HOH B O    1 
HETATM 11062 O  O    . HOH X 4 .   ? -3.136  17.893  -2.016  1.00 17.42  ?  704  HOH B O    1 
HETATM 11063 O  O    . HOH X 4 .   ? 19.958  2.174   -14.676 1.00 31.14  ?  705  HOH B O    1 
HETATM 11064 O  O    B HOH X 4 .   ? 22.445  -11.509 8.725   0.61 32.67  ?  706  HOH B O    1 
HETATM 11065 O  O    A HOH X 4 .   ? -10.710 19.953  25.674  0.40 11.20  ?  707  HOH B O    1 
HETATM 11066 O  O    . HOH X 4 .   ? -10.268 11.696  10.080  1.00 16.68  ?  708  HOH B O    1 
HETATM 11067 O  O    . HOH X 4 .   ? 13.976  12.134  8.253   1.00 14.97  ?  709  HOH B O    1 
HETATM 11068 O  O    . HOH X 4 .   ? 35.539  3.914   -4.258  1.00 47.45  ?  710  HOH B O    1 
HETATM 11069 O  O    B HOH X 4 .   ? -9.828  35.582  26.260  0.29 15.09  ?  711  HOH B O    1 
HETATM 11070 O  O    B HOH X 4 .   ? 36.276  29.107  11.174  0.60 27.53  ?  712  HOH B O    1 
HETATM 11071 O  O    . HOH X 4 .   ? -10.996 29.681  30.607  1.00 43.84  ?  713  HOH B O    1 
HETATM 11072 O  O    . HOH X 4 .   ? 22.822  15.961  -13.693 1.00 51.55  ?  714  HOH B O    1 
HETATM 11073 O  O    . HOH X 4 .   ? 16.617  -5.943  1.703   1.00 43.19  ?  715  HOH B O    1 
HETATM 11074 O  O    C HOH X 4 .   ? 6.800   20.857  -18.243 0.92 35.72  ?  716  HOH B O    1 
HETATM 11075 O  O    . HOH X 4 .   ? 35.172  6.614   -10.014 1.00 57.65  ?  717  HOH B O    1 
HETATM 11076 O  O    . HOH X 4 .   ? -2.647  5.987   -7.433  1.00 42.02  ?  718  HOH B O    1 
HETATM 11077 O  O    . HOH X 4 .   ? 2.252   46.989  13.982  1.00 61.08  ?  719  HOH B O    1 
HETATM 11078 O  O    . HOH X 4 .   ? -3.403  17.839  -8.298  1.00 30.74  ?  720  HOH B O    1 
HETATM 11079 O  O    A HOH X 4 .   ? 8.292   -0.311  -5.332  0.94 40.49  ?  721  HOH B O    1 
HETATM 11080 O  O    . HOH X 4 .   ? 13.209  7.351   8.456   1.00 23.71  ?  722  HOH B O    1 
HETATM 11081 O  O    . HOH X 4 .   ? 14.770  34.968  -2.813  1.00 35.54  ?  723  HOH B O    1 
HETATM 11082 O  O    . HOH X 4 .   ? 37.151  12.285  -8.464  1.00 64.89  ?  724  HOH B O    1 
HETATM 11083 O  O    . HOH X 4 .   ? -9.527  21.052  3.706   1.00 39.87  ?  725  HOH B O    1 
HETATM 11084 O  O    . HOH X 4 .   ? 12.041  5.691   5.924   1.00 27.63  ?  726  HOH B O    1 
HETATM 11085 O  O    . HOH X 4 .   ? 28.667  -12.914 6.195   1.00 32.41  ?  727  HOH B O    1 
HETATM 11086 O  O    . HOH X 4 .   ? -9.621  24.692  29.567  1.00 49.32  ?  728  HOH B O    1 
HETATM 11087 O  O    . HOH X 4 .   ? 30.505  0.317   -4.673  1.00 33.42  ?  729  HOH B O    1 
HETATM 11088 O  O    . HOH X 4 .   ? 20.037  34.456  2.170   1.00 48.68  ?  730  HOH B O    1 
HETATM 11089 O  O    . HOH X 4 .   ? 24.644  26.231  -2.790  1.00 24.43  ?  731  HOH B O    1 
HETATM 11090 O  O    . HOH X 4 .   ? 16.389  30.067  -4.043  1.00 56.46  ?  732  HOH B O    1 
HETATM 11091 O  O    . HOH X 4 .   ? -12.883 11.438  10.381  1.00 50.80  ?  733  HOH B O    1 
HETATM 11092 O  O    B HOH X 4 .   ? 31.706  0.317   0.849   0.62 24.14  ?  734  HOH B O    1 
HETATM 11093 O  O    . HOH X 4 .   ? 8.950   10.432  3.461   1.00 14.06  ?  735  HOH B O    1 
HETATM 11094 O  O    . HOH X 4 .   ? -2.656  28.815  39.807  1.00 36.73  ?  736  HOH B O    1 
HETATM 11095 O  O    . HOH X 4 .   ? 1.844   41.543  10.308  1.00 44.39  ?  737  HOH B O    1 
HETATM 11096 O  O    . HOH X 4 .   ? 14.360  36.642  15.480  1.00 30.60  ?  738  HOH B O    1 
HETATM 11097 O  O    . HOH X 4 .   ? 9.375   37.827  9.507   1.00 25.12  ?  739  HOH B O    1 
HETATM 11098 O  O    A HOH X 4 .   ? 18.104  21.027  15.446  0.75 17.58  ?  740  HOH B O    1 
HETATM 11099 O  O    . HOH X 4 .   ? 0.492   1.836   -1.105  1.00 54.80  ?  741  HOH B O    1 
HETATM 11100 O  O    . HOH X 4 .   ? 15.657  32.313  -4.184  1.00 25.48  ?  742  HOH B O    1 
HETATM 11101 O  O    . HOH X 4 .   ? 13.330  42.961  18.737  1.00 48.33  ?  743  HOH B O    1 
HETATM 11102 O  O    . HOH X 4 .   ? 22.938  -14.882 -2.338  1.00 26.53  ?  744  HOH B O    1 
HETATM 11103 O  O    B HOH X 4 .   ? -9.525  22.117  27.556  0.63 18.93  ?  745  HOH B O    1 
HETATM 11104 O  O    . HOH X 4 .   ? 11.212  28.759  27.482  1.00 22.83  ?  746  HOH B O    1 
HETATM 11105 O  O    A HOH X 4 .   ? 14.068  21.730  22.610  0.72 29.74  ?  747  HOH B O    1 
HETATM 11106 O  O    . HOH X 4 .   ? -13.424 42.020  16.469  1.00 31.70  ?  748  HOH B O    1 
HETATM 11107 O  O    B HOH X 4 .   ? 1.552   35.906  6.377   0.75 29.68  ?  749  HOH B O    1 
HETATM 11108 O  O    . HOH X 4 .   ? 34.034  -12.936 4.683   1.00 26.92  ?  750  HOH B O    1 
HETATM 11109 O  O    . HOH X 4 .   ? -5.477  30.619  3.780   1.00 35.96  ?  751  HOH B O    1 
HETATM 11110 O  O    A HOH X 4 .   ? -9.547  37.200  25.802  0.96 20.88  ?  752  HOH B O    1 
HETATM 11111 O  O    . HOH X 4 .   ? 4.921   16.822  29.631  1.00 20.12  ?  753  HOH B O    1 
HETATM 11112 O  O    . HOH X 4 .   ? 18.158  33.583  14.575  1.00 27.39  ?  754  HOH B O    1 
HETATM 11113 O  O    . HOH X 4 .   ? 34.742  17.658  -2.926  1.00 18.83  ?  755  HOH B O    1 
HETATM 11114 O  O    B HOH X 4 .   ? 21.959  23.252  -6.987  0.54 15.01  ?  756  HOH B O    1 
HETATM 11115 O  O    . HOH X 4 .   ? 4.171   29.859  -2.423  1.00 18.36  ?  757  HOH B O    1 
HETATM 11116 O  O    A HOH X 4 .   ? 1.794   36.470  4.128   0.95 18.62  ?  758  HOH B O    1 
HETATM 11117 O  O    . HOH X 4 .   ? -9.955  39.195  24.789  1.00 47.19  ?  759  HOH B O    1 
HETATM 11118 O  O    . HOH X 4 .   ? 2.835   42.709  12.582  1.00 18.25  ?  760  HOH B O    1 
HETATM 11119 O  O    . HOH X 4 .   ? 11.694  26.821  -6.755  1.00 17.40  ?  761  HOH B O    1 
HETATM 11120 O  O    A HOH X 4 .   ? 31.672  -0.707  1.683   0.66 13.45  ?  762  HOH B O    1 
HETATM 11121 O  O    . HOH X 4 .   ? -5.468  10.322  20.702  1.00 20.93  ?  763  HOH B O    1 
HETATM 11122 O  O    A HOH X 4 .   ? 9.894   40.523  24.311  0.82 13.27  ?  764  HOH B O    1 
HETATM 11123 O  O    . HOH X 4 .   ? 3.847   9.509   -0.993  1.00 17.05  ?  765  HOH B O    1 
HETATM 11124 O  O    . HOH X 4 .   ? -0.636  18.766  32.673  1.00 27.23  ?  766  HOH B O    1 
HETATM 11125 O  O    . HOH X 4 .   ? 19.517  -12.599 1.097   1.00 28.19  ?  767  HOH B O    1 
HETATM 11126 O  O    . HOH X 4 .   ? 7.192   23.992  26.512  1.00 10.83  ?  768  HOH B O    1 
HETATM 11127 O  O    . HOH X 4 .   ? -10.197 38.013  10.748  1.00 17.55  ?  769  HOH B O    1 
HETATM 11128 O  O    . HOH X 4 .   ? 24.760  -11.196 -5.562  1.00 24.35  ?  770  HOH B O    1 
HETATM 11129 O  O    . HOH X 4 .   ? 33.038  -12.407 0.825   1.00 9.00   ?  771  HOH B O    1 
HETATM 11130 O  O    C HOH X 4 .   ? 6.596   9.301   1.161   0.46 14.26  ?  772  HOH B O    1 
HETATM 11131 O  O    . HOH X 4 .   ? 16.712  27.679  -9.439  1.00 46.72  ?  773  HOH B O    1 
HETATM 11132 O  O    A HOH X 4 .   ? 14.129  17.108  25.274  0.46 10.68  ?  774  HOH B O    1 
HETATM 11133 O  O    . HOH X 4 .   ? -2.410  21.795  12.577  1.00 41.46  ?  775  HOH B O    1 
HETATM 11134 O  O    . HOH X 4 .   ? -2.221  23.424  7.656   1.00 11.46  ?  776  HOH B O    1 
HETATM 11135 O  O    . HOH X 4 .   ? 36.310  10.396  -6.959  1.00 29.93  ?  777  HOH B O    1 
HETATM 11136 O  O    . HOH X 4 .   ? -5.313  27.994  34.377  1.00 40.67  ?  778  HOH B O    1 
HETATM 11137 O  O    . HOH X 4 .   ? -6.694  39.678  18.179  1.00 13.97  ?  779  HOH B O    1 
HETATM 11138 O  O    . HOH X 4 .   ? 11.378  31.855  23.679  1.00 16.40  ?  780  HOH B O    1 
HETATM 11139 O  O    . HOH X 4 .   ? -8.739  41.663  7.173   1.00 20.96  ?  781  HOH B O    1 
HETATM 11140 O  O    . HOH X 4 .   ? 7.042   19.358  0.374   1.00 6.51   ?  782  HOH B O    1 
HETATM 11141 O  O    . HOH X 4 .   ? 0.270   45.889  14.051  1.00 51.21  ?  783  HOH B O    1 
HETATM 11142 O  O    B HOH X 4 .   ? 17.155  13.692  13.317  0.39 10.60  ?  784  HOH B O    1 
HETATM 11143 O  O    . HOH X 4 .   ? -19.981 26.816  13.589  1.00 25.16  ?  785  HOH B O    1 
HETATM 11144 O  O    . HOH X 4 .   ? 10.479  22.507  26.853  1.00 16.40  ?  786  HOH B O    1 
HETATM 11145 O  O    . HOH X 4 .   ? 13.264  23.407  -7.601  1.00 10.43  ?  787  HOH B O    1 
HETATM 11146 O  O    . HOH X 4 .   ? -6.124  36.548  12.088  1.00 9.43   ?  788  HOH B O    1 
HETATM 11147 O  O    . HOH X 4 .   ? -0.853  22.646  9.945   1.00 8.15   ?  789  HOH B O    1 
HETATM 11148 O  O    . HOH X 4 .   ? 22.363  32.314  9.688   1.00 10.49  ?  790  HOH B O    1 
HETATM 11149 O  O    . HOH X 4 .   ? -13.529 30.359  8.241   1.00 22.61  ?  791  HOH B O    1 
HETATM 11150 O  O    . HOH X 4 .   ? 16.077  13.633  -11.616 1.00 10.66  ?  792  HOH B O    1 
HETATM 11151 O  O    . HOH X 4 .   ? 5.586   8.069   5.849   1.00 13.11  ?  793  HOH B O    1 
HETATM 11152 O  O    A HOH X 4 .   ? 12.399  34.100  0.577   0.91 16.78  ?  794  HOH B O    1 
HETATM 11153 O  O    . HOH X 4 .   ? 3.127   18.722  30.143  1.00 15.66  ?  795  HOH B O    1 
HETATM 11154 O  O    . HOH X 4 .   ? 5.076   41.215  23.411  1.00 13.52  ?  796  HOH B O    1 
HETATM 11155 O  O    . HOH X 4 .   ? -1.371  16.255  -9.503  1.00 28.57  ?  797  HOH B O    1 
HETATM 11156 O  O    . HOH X 4 .   ? 24.862  -8.374  -1.802  1.00 6.48   ?  798  HOH B O    1 
HETATM 11157 O  O    . HOH X 4 .   ? 26.296  -20.282 2.801   1.00 16.56  ?  799  HOH B O    1 
HETATM 11158 O  O    . HOH X 4 .   ? 26.601  -19.405 0.210   1.00 12.83  ?  800  HOH B O    1 
HETATM 11159 O  O    . HOH X 4 .   ? 24.349  20.754  -4.913  1.00 25.70  ?  801  HOH B O    1 
HETATM 11160 O  O    . HOH X 4 .   ? 11.269  33.790  19.462  1.00 13.55  ?  802  HOH B O    1 
HETATM 11161 O  O    B HOH X 4 .   ? -2.067  16.004  0.733   0.72 15.34  ?  803  HOH B O    1 
HETATM 11162 O  O    . HOH X 4 .   ? -14.698 32.057  24.728  1.00 22.37  ?  804  HOH B O    1 
HETATM 11163 O  O    . HOH X 4 .   ? 1.390   42.454  22.022  1.00 17.05  ?  805  HOH B O    1 
HETATM 11164 O  O    . HOH X 4 .   ? 1.413   3.103   -5.713  1.00 30.44  ?  806  HOH B O    1 
HETATM 11165 O  O    . HOH X 4 .   ? -4.595  25.789  35.157  1.00 40.12  ?  807  HOH B O    1 
HETATM 11166 O  O    . HOH X 4 .   ? 10.765  20.858  -17.418 1.00 27.33  ?  808  HOH B O    1 
HETATM 11167 O  O    . HOH X 4 .   ? 25.212  33.121  6.051   1.00 11.92  ?  809  HOH B O    1 
HETATM 11168 O  O    . HOH X 4 .   ? -0.583  43.620  17.831  1.00 23.54  ?  810  HOH B O    1 
HETATM 11169 O  O    . HOH X 4 .   ? 15.663  -7.473  -2.288  1.00 21.51  ?  811  HOH B O    1 
HETATM 11170 O  O    A HOH X 4 .   ? 21.477  22.786  -7.886  0.78 15.69  ?  812  HOH B O    1 
HETATM 11171 O  O    . HOH X 4 .   ? 8.690   12.379  18.973  1.00 20.07  ?  813  HOH B O    1 
HETATM 11172 O  O    . HOH X 4 .   ? 22.439  -0.254  4.731   1.00 7.48   ?  814  HOH B O    1 
HETATM 11173 O  O    . HOH X 4 .   ? -4.629  16.673  25.583  1.00 12.38  ?  815  HOH B O    1 
HETATM 11174 O  O    . HOH X 4 .   ? 8.042   5.972   -7.796  1.00 13.63  ?  816  HOH B O    1 
HETATM 11175 O  O    . HOH X 4 .   ? 4.195   17.392  -13.283 1.00 14.45  ?  817  HOH B O    1 
HETATM 11176 O  O    . HOH X 4 .   ? 25.642  4.392   -11.068 1.00 14.71  ?  818  HOH B O    1 
HETATM 11177 O  O    . HOH X 4 .   ? -6.816  15.676  -2.904  1.00 56.28  ?  819  HOH B O    1 
HETATM 11178 O  O    . HOH X 4 .   ? 14.846  14.966  28.863  1.00 24.83  ?  820  HOH B O    1 
HETATM 11179 O  O    A HOH X 4 .   ? 5.656   30.597  -0.395  0.98 45.50  ?  821  HOH B O    1 
HETATM 11180 O  O    . HOH X 4 .   ? 0.333   34.565  34.111  1.00 24.61  ?  822  HOH B O    1 
HETATM 11181 O  O    . HOH X 4 .   ? -7.895  12.002  10.146  1.00 13.86  ?  823  HOH B O    1 
HETATM 11182 O  O    A HOH X 4 .   ? 18.217  25.740  -10.857 1.00 51.97  ?  824  HOH B O    1 
HETATM 11183 O  O    . HOH X 4 .   ? 2.942   36.916  10.849  1.00 11.10  ?  825  HOH B O    1 
HETATM 11184 O  O    . HOH X 4 .   ? 15.916  2.280   -10.201 1.00 17.26  ?  826  HOH B O    1 
HETATM 11185 O  O    . HOH X 4 .   ? 16.453  -2.110  1.834   1.00 33.61  ?  827  HOH B O    1 
HETATM 11186 O  O    . HOH X 4 .   ? -3.579  20.744  26.001  1.00 8.05   ?  828  HOH B O    1 
HETATM 11187 O  O    . HOH X 4 .   ? -3.978  20.475  30.939  1.00 23.49  ?  829  HOH B O    1 
HETATM 11188 O  O    . HOH X 4 .   ? 7.700   26.666  26.259  1.00 10.99  ?  830  HOH B O    1 
HETATM 11189 O  O    . HOH X 4 .   ? 31.369  -10.106 6.616   1.00 23.49  ?  831  HOH B O    1 
HETATM 11190 O  O    . HOH X 4 .   ? 12.473  20.004  21.847  1.00 22.79  ?  832  HOH B O    1 
HETATM 11191 O  O    . HOH X 4 .   ? 5.309   26.086  -19.043 1.00 8.74   ?  833  HOH B O    1 
HETATM 11192 O  O    . HOH X 4 .   ? 11.211  35.293  6.621   1.00 36.01  ?  834  HOH B O    1 
HETATM 11193 O  O    . HOH X 4 .   ? 12.754  34.357  29.699  1.00 19.57  ?  835  HOH B O    1 
HETATM 11194 O  O    B HOH X 4 .   ? -1.028  13.478  3.120   0.62 9.61   ?  836  HOH B O    1 
HETATM 11195 O  O    B HOH X 4 .   ? 4.674   23.997  24.237  0.33 8.57   ?  837  HOH B O    1 
HETATM 11196 O  O    . HOH X 4 .   ? 33.967  12.583  -11.514 1.00 26.81  ?  838  HOH B O    1 
HETATM 11197 O  O    . HOH X 4 .   ? 11.936  11.309  -12.988 1.00 15.84  ?  839  HOH B O    1 
HETATM 11198 O  O    . HOH X 4 .   ? 3.986   19.835  -10.265 1.00 13.36  ?  840  HOH B O    1 
HETATM 11199 O  O    . HOH X 4 .   ? 19.011  32.197  3.667   1.00 35.88  ?  841  HOH B O    1 
HETATM 11200 O  O    A HOH X 4 .   ? 16.480  7.588   8.701   0.51 12.29  ?  842  HOH B O    1 
HETATM 11201 O  O    . HOH X 4 .   ? 6.967   26.672  37.046  1.00 21.41  ?  843  HOH B O    1 
HETATM 11202 O  O    . HOH X 4 .   ? 7.508   19.098  -15.724 1.00 19.54  ?  844  HOH B O    1 
HETATM 11203 O  O    . HOH X 4 .   ? 12.467  39.358  12.416  1.00 35.89  ?  845  HOH B O    1 
HETATM 11204 O  O    . HOH X 4 .   ? 1.780   21.608  -13.133 1.00 13.16  ?  846  HOH B O    1 
HETATM 11205 O  O    . HOH X 4 .   ? 1.923   36.168  31.164  1.00 11.36  ?  847  HOH B O    1 
HETATM 11206 O  O    . HOH X 4 .   ? 19.996  32.694  12.718  1.00 15.15  ?  848  HOH B O    1 
HETATM 11207 O  O    . HOH X 4 .   ? 36.778  29.631  7.836   1.00 35.17  ?  849  HOH B O    1 
HETATM 11208 O  O    . HOH X 4 .   ? 7.806   37.932  25.791  1.00 8.16   ?  850  HOH B O    1 
HETATM 11209 O  O    A HOH X 4 .   ? 32.060  8.365   3.198   1.00 7.83   ?  851  HOH B O    1 
HETATM 11210 O  O    . HOH X 4 .   ? 21.665  34.773  3.827   1.00 45.61  ?  852  HOH B O    1 
HETATM 11211 O  O    . HOH X 4 .   ? 3.341   30.827  35.710  1.00 12.59  ?  853  HOH B O    1 
HETATM 11212 O  O    . HOH X 4 .   ? 18.000  28.883  -3.077  1.00 26.30  ?  854  HOH B O    1 
HETATM 11213 O  O    . HOH X 4 .   ? 10.196  19.507  28.814  1.00 20.62  ?  855  HOH B O    1 
HETATM 11214 O  O    . HOH X 4 .   ? 1.050   28.343  13.284  1.00 6.00   ?  856  HOH B O    1 
HETATM 11215 O  O    . HOH X 4 .   ? -13.318 34.193  26.036  1.00 26.28  ?  857  HOH B O    1 
HETATM 11216 O  O    . HOH X 4 .   ? 24.509  18.028  -5.169  1.00 19.17  ?  858  HOH B O    1 
HETATM 11217 O  O    . HOH X 4 .   ? 10.060  20.272  4.992   1.00 6.56   ?  859  HOH B O    1 
HETATM 11218 O  O    . HOH X 4 .   ? -6.013  20.245  -6.696  1.00 27.32  ?  860  HOH B O    1 
HETATM 11219 O  O    . HOH X 4 .   ? -9.553  15.693  20.791  1.00 23.05  ?  861  HOH B O    1 
HETATM 11220 O  O    . HOH X 4 .   ? -10.593 13.914  9.633   1.00 20.48  ?  862  HOH B O    1 
HETATM 11221 O  O    . HOH X 4 .   ? 5.120   16.850  8.560   1.00 5.82   ?  863  HOH B O    1 
HETATM 11222 O  O    . HOH X 4 .   ? 27.938  34.139  3.569   1.00 12.14  ?  864  HOH B O    1 
HETATM 11223 O  O    . HOH X 4 .   ? 30.164  11.499  0.352   1.00 10.95  ?  865  HOH B O    1 
HETATM 11224 O  O    . HOH X 4 .   ? 1.626   20.635  23.069  1.00 7.19   ?  866  HOH B O    1 
HETATM 11225 O  O    . HOH X 4 .   ? 7.077   22.250  -10.232 1.00 9.94   ?  867  HOH B O    1 
HETATM 11226 O  O    . HOH X 4 .   ? -8.784  16.539  16.078  1.00 14.03  ?  868  HOH B O    1 
HETATM 11227 O  O    . HOH X 4 .   ? -16.651 26.902  7.609   1.00 45.43  ?  869  HOH B O    1 
HETATM 11228 O  O    . HOH X 4 .   ? 18.362  0.640   -9.524  1.00 10.37  ?  870  HOH B O    1 
HETATM 11229 O  O    . HOH X 4 .   ? 16.485  21.317  17.600  1.00 15.46  ?  871  HOH B O    1 
HETATM 11230 O  O    A HOH X 4 .   ? -1.928  16.500  -0.724  0.47 14.31  ?  872  HOH B O    1 
HETATM 11231 O  O    . HOH X 4 .   ? 8.191   37.827  18.753  1.00 11.13  ?  873  HOH B O    1 
HETATM 11232 O  O    . HOH X 4 .   ? 15.387  30.578  4.912   1.00 7.26   ?  874  HOH B O    1 
HETATM 11233 O  O    . HOH X 4 .   ? 36.915  10.273  -2.057  1.00 43.20  ?  875  HOH B O    1 
HETATM 11234 O  O    . HOH X 4 .   ? 31.371  4.056   -9.044  1.00 37.84  ?  876  HOH B O    1 
HETATM 11235 O  O    . HOH X 4 .   ? 33.836  2.949   0.552   1.00 28.48  ?  877  HOH B O    1 
HETATM 11236 O  O    . HOH X 4 .   ? 6.625   36.322  30.560  1.00 8.27   ?  878  HOH B O    1 
HETATM 11237 O  O    . HOH X 4 .   ? -6.271  42.022  19.705  1.00 27.03  ?  879  HOH B O    1 
HETATM 11238 O  O    . HOH X 4 .   ? 17.748  12.521  10.920  1.00 8.39   ?  880  HOH B O    1 
HETATM 11239 O  O    . HOH X 4 .   ? 14.880  -1.496  -6.427  1.00 18.88  ?  881  HOH B O    1 
HETATM 11240 O  O    . HOH X 4 .   ? -2.885  38.785  5.549   1.00 44.46  ?  882  HOH B O    1 
HETATM 11241 O  O    . HOH X 4 .   ? 19.836  16.951  12.578  1.00 13.23  ?  883  HOH B O    1 
HETATM 11242 O  O    . HOH X 4 .   ? -15.037 19.372  11.557  1.00 15.84  ?  884  HOH B O    1 
HETATM 11243 O  O    . HOH X 4 .   ? 29.832  11.211  -16.424 1.00 34.86  ?  885  HOH B O    1 
HETATM 11244 O  O    . HOH X 4 .   ? 36.842  20.353  -8.185  1.00 47.14  ?  886  HOH B O    1 
HETATM 11245 O  O    A HOH X 4 .   ? 3.156   9.560   14.158  0.77 10.19  ?  887  HOH B O    1 
HETATM 11246 O  O    . HOH X 4 .   ? 30.080  21.581  1.930   1.00 7.62   ?  888  HOH B O    1 
HETATM 11247 O  O    . HOH X 4 .   ? 4.827   20.376  31.390  1.00 14.38  ?  889  HOH B O    1 
HETATM 11248 O  O    . HOH X 4 .   ? -7.970  19.191  0.714   1.00 48.99  ?  890  HOH B O    1 
HETATM 11249 O  O    . HOH X 4 .   ? 0.671   12.989  19.217  1.00 10.76  ?  891  HOH B O    1 
HETATM 11250 O  O    . HOH X 4 .   ? 1.221   34.077  3.538   1.00 13.06  ?  892  HOH B O    1 
HETATM 11251 O  O    . HOH X 4 .   ? -8.700  35.807  12.964  1.00 13.23  ?  893  HOH B O    1 
HETATM 11252 O  O    . HOH X 4 .   ? -4.001  24.294  -3.639  1.00 25.53  ?  894  HOH B O    1 
HETATM 11253 O  O    B HOH X 4 .   ? 8.608   28.843  -5.381  0.97 30.01  ?  895  HOH B O    1 
HETATM 11254 O  O    . HOH X 4 .   ? 13.655  20.647  -14.786 1.00 16.21  ?  896  HOH B O    1 
HETATM 11255 O  O    . HOH X 4 .   ? 15.280  1.830   1.179   1.00 37.94  ?  897  HOH B O    1 
HETATM 11256 O  O    . HOH X 4 .   ? -12.333 38.473  7.335   1.00 27.14  ?  898  HOH B O    1 
HETATM 11257 O  O    . HOH X 4 .   ? -3.323  6.769   -11.838 1.00 32.60  ?  899  HOH B O    1 
HETATM 11258 O  O    . HOH X 4 .   ? 35.284  8.684   -0.231  1.00 30.31  ?  900  HOH B O    1 
HETATM 11259 O  O    . HOH X 4 .   ? 12.908  33.986  17.257  1.00 20.19  ?  901  HOH B O    1 
HETATM 11260 O  O    . HOH X 4 .   ? 20.422  6.794   5.450   1.00 10.79  ?  902  HOH B O    1 
HETATM 11261 O  O    . HOH X 4 .   ? 8.300   10.487  -14.636 1.00 29.97  ?  903  HOH B O    1 
HETATM 11262 O  O    . HOH X 4 .   ? 29.258  23.456  3.876   1.00 7.04   ?  904  HOH B O    1 
HETATM 11263 O  O    B HOH X 4 .   ? 33.479  12.623  -0.217  0.99 30.30  ?  905  HOH B O    1 
HETATM 11264 O  O    . HOH X 4 .   ? -5.999  14.199  3.438   1.00 21.60  ?  906  HOH B O    1 
HETATM 11265 O  O    . HOH X 4 .   ? -14.750 18.882  19.084  1.00 28.53  ?  907  HOH B O    1 
HETATM 11266 O  O    A HOH X 4 .   ? 17.766  14.823  12.697  0.66 8.07   ?  908  HOH B O    1 
HETATM 11267 O  O    C HOH X 4 .   ? 28.771  15.666  -5.783  0.81 13.13  ?  909  HOH B O    1 
HETATM 11268 O  O    . HOH X 4 .   ? -9.712  9.108   13.365  1.00 31.92  ?  910  HOH B O    1 
HETATM 11269 O  O    . HOH X 4 .   ? 15.183  5.193   -13.947 1.00 39.63  ?  911  HOH B O    1 
HETATM 11270 O  O    . HOH X 4 .   ? 17.460  -3.783  -0.053  1.00 17.09  ?  912  HOH B O    1 
HETATM 11271 O  O    B HOH X 4 .   ? 10.706  8.869   -1.083  1.00 11.16  ?  913  HOH B O    1 
HETATM 11272 O  O    A HOH X 4 .   ? -11.027 21.381  7.978   0.99 16.22  ?  914  HOH B O    1 
HETATM 11273 O  O    . HOH X 4 .   ? -17.694 22.624  9.031   1.00 53.00  ?  915  HOH B O    1 
HETATM 11274 O  O    . HOH X 4 .   ? 0.242   28.264  41.893  1.00 39.89  ?  916  HOH B O    1 
HETATM 11275 O  O    . HOH X 4 .   ? 11.503  2.067   -1.952  1.00 14.65  ?  917  HOH B O    1 
HETATM 11276 O  O    B HOH X 4 .   ? -1.316  34.292  -0.235  0.51 24.39  ?  918  HOH B O    1 
HETATM 11277 O  O    B HOH X 4 .   ? -16.057 37.203  18.030  1.00 47.64  ?  919  HOH B O    1 
HETATM 11278 O  O    . HOH X 4 .   ? 24.006  -20.771 -0.073  1.00 50.15  ?  920  HOH B O    1 
HETATM 11279 O  O    . HOH X 4 .   ? 29.025  7.853   -15.802 1.00 29.93  ?  921  HOH B O    1 
HETATM 11280 O  O    . HOH X 4 .   ? 21.112  25.408  1.649   1.00 8.15   ?  922  HOH B O    1 
HETATM 11281 O  O    . HOH X 4 .   ? 6.180   28.719  1.893   1.00 9.81   ?  923  HOH B O    1 
HETATM 11282 O  O    A HOH X 4 .   ? 10.707  6.614   -9.605  0.54 17.47  ?  924  HOH B O    1 
HETATM 11283 O  O    . HOH X 4 .   ? -11.902 12.752  19.189  1.00 28.28  ?  925  HOH B O    1 
HETATM 11284 O  O    . HOH X 4 .   ? -7.924  15.069  1.763   1.00 41.00  ?  926  HOH B O    1 
HETATM 11285 O  O    . HOH X 4 .   ? 27.262  2.678   -9.688  1.00 14.63  ?  927  HOH B O    1 
HETATM 11286 O  O    . HOH X 4 .   ? 17.995  -0.412  6.847   1.00 15.20  ?  928  HOH B O    1 
HETATM 11287 O  O    B HOH X 4 .   ? 28.454  16.521  -4.079  0.92 34.83  ?  929  HOH B O    1 
HETATM 11288 O  O    . HOH X 4 .   ? 23.221  30.738  16.853  1.00 24.36  ?  930  HOH B O    1 
HETATM 11289 O  O    . HOH X 4 .   ? 32.849  21.111  6.397   1.00 11.89  ?  931  HOH B O    1 
HETATM 11290 O  O    . HOH X 4 .   ? 25.994  36.472  1.477   1.00 21.89  ?  932  HOH B O    1 
HETATM 11291 O  O    B HOH X 4 .   ? 9.493   25.646  39.744  1.00 45.61  ?  933  HOH B O    1 
HETATM 11292 O  O    . HOH X 4 .   ? -5.714  34.483  10.152  1.00 16.19  ?  934  HOH B O    1 
HETATM 11293 O  O    B HOH X 4 .   ? 13.479  21.597  -9.677  1.00 10.92  ?  935  HOH B O    1 
HETATM 11294 O  O    . HOH X 4 .   ? 16.453  22.407  22.146  1.00 39.10  ?  936  HOH B O    1 
HETATM 11295 O  O    . HOH X 4 .   ? 30.734  -0.705  -0.965  1.00 13.79  ?  937  HOH B O    1 
HETATM 11296 O  O    . HOH X 4 .   ? 15.205  30.469  7.619   1.00 7.95   ?  938  HOH B O    1 
HETATM 11297 O  O    . HOH X 4 .   ? -18.592 29.866  19.562  1.00 32.12  ?  939  HOH B O    1 
HETATM 11298 O  O    . HOH X 4 .   ? 2.469   33.534  35.637  1.00 16.15  ?  940  HOH B O    1 
HETATM 11299 O  O    . HOH X 4 .   ? 18.160  17.020  -6.688  1.00 7.83   ?  941  HOH B O    1 
HETATM 11300 O  O    . HOH X 4 .   ? -2.638  41.043  10.849  1.00 23.94  ?  942  HOH B O    1 
HETATM 11301 O  O    . HOH X 4 .   ? 0.730   43.030  14.207  1.00 22.81  ?  943  HOH B O    1 
HETATM 11302 O  O    . HOH X 4 .   ? 14.219  1.464   -1.274  1.00 20.17  ?  944  HOH B O    1 
HETATM 11303 O  O    . HOH X 4 .   ? 7.812   26.548  2.384   1.00 9.75   ?  945  HOH B O    1 
HETATM 11304 O  O    . HOH X 4 .   ? 26.587  10.410  -17.243 1.00 48.90  ?  946  HOH B O    1 
HETATM 11305 O  O    . HOH X 4 .   ? 22.907  33.411  -2.604  1.00 49.82  ?  947  HOH B O    1 
HETATM 11306 O  O    . HOH X 4 .   ? 29.681  -14.535 -3.529  1.00 7.88   ?  948  HOH B O    1 
HETATM 11307 O  O    A HOH X 4 .   ? 25.455  22.207  -2.320  0.65 15.65  ?  949  HOH B O    1 
HETATM 11308 O  O    . HOH X 4 .   ? -16.758 31.254  23.013  1.00 28.11  ?  950  HOH B O    1 
HETATM 11309 O  O    B HOH X 4 .   ? 11.365  6.981   -11.165 0.75 24.51  ?  951  HOH B O    1 
HETATM 11310 O  O    B HOH X 4 .   ? -16.945 21.341  11.314  0.90 21.61  ?  952  HOH B O    1 
HETATM 11311 O  O    . HOH X 4 .   ? 9.791   29.596  23.186  1.00 14.37  ?  953  HOH B O    1 
HETATM 11312 O  O    . HOH X 4 .   ? -16.655 24.996  11.887  1.00 18.77  ?  954  HOH B O    1 
HETATM 11313 O  O    . HOH X 4 .   ? 33.989  -9.566  3.183   1.00 22.39  ?  955  HOH B O    1 
HETATM 11314 O  O    A HOH X 4 .   ? 13.217  37.977  18.944  0.54 13.48  ?  956  HOH B O    1 
HETATM 11315 O  O    B HOH X 4 .   ? 6.887   29.740  -1.962  0.63 16.22  ?  957  HOH B O    1 
HETATM 11316 O  O    . HOH X 4 .   ? -2.252  37.102  21.622  1.00 7.51   ?  958  HOH B O    1 
HETATM 11317 O  O    . HOH X 4 .   ? 25.918  30.124  3.314   1.00 8.24   ?  959  HOH B O    1 
HETATM 11318 O  O    C HOH X 4 .   ? 7.078   40.426  5.939   1.00 34.56  ?  960  HOH B O    1 
HETATM 11319 O  O    . HOH X 4 .   ? 14.817  35.490  13.221  1.00 20.80  ?  961  HOH B O    1 
HETATM 11320 O  O    . HOH X 4 .   ? 20.105  26.140  -2.775  1.00 17.94  ?  962  HOH B O    1 
HETATM 11321 O  O    . HOH X 4 .   ? -2.712  35.535  32.772  1.00 29.09  ?  963  HOH B O    1 
HETATM 11322 O  O    . HOH X 4 .   ? -3.648  21.412  -7.578  1.00 16.28  ?  964  HOH B O    1 
HETATM 11323 O  O    . HOH X 4 .   ? 9.803   11.119  0.293   1.00 11.65  ?  965  HOH B O    1 
HETATM 11324 O  O    . HOH X 4 .   ? 29.840  -5.247  -2.482  1.00 12.67  ?  966  HOH B O    1 
HETATM 11325 O  O    . HOH X 4 .   ? 13.018  39.683  27.295  1.00 10.60  ?  967  HOH B O    1 
HETATM 11326 O  O    . HOH X 4 .   ? 3.563   19.681  -7.529  1.00 9.36   ?  968  HOH B O    1 
HETATM 11327 O  O    . HOH X 4 .   ? 6.071   38.469  23.578  1.00 11.76  ?  969  HOH B O    1 
HETATM 11328 O  O    . HOH X 4 .   ? 21.810  17.457  -5.728  1.00 11.65  ?  970  HOH B O    1 
HETATM 11329 O  O    . HOH X 4 .   ? 27.302  31.511  5.272   1.00 8.46   ?  971  HOH B O    1 
HETATM 11330 O  O    A HOH X 4 .   ? -14.065 15.097  12.000  1.00 30.45  ?  972  HOH B O    1 
HETATM 11331 O  O    . HOH X 4 .   ? 7.815   43.079  19.904  1.00 26.00  ?  973  HOH B O    1 
HETATM 11332 O  O    . HOH X 4 .   ? -10.020 30.231  10.981  1.00 12.28  ?  974  HOH B O    1 
HETATM 11333 O  O    . HOH X 4 .   ? 14.351  -0.410  -4.050  1.00 30.81  ?  975  HOH B O    1 
HETATM 11334 O  O    . HOH X 4 .   ? -8.330  44.051  18.742  1.00 49.65  ?  976  HOH B O    1 
HETATM 11335 O  O    . HOH X 4 .   ? -8.005  16.946  18.831  1.00 14.71  ?  977  HOH B O    1 
HETATM 11336 O  O    . HOH X 4 .   ? -3.183  19.358  -0.100  1.00 18.54  ?  978  HOH B O    1 
HETATM 11337 O  O    A HOH X 4 .   ? 14.588  -4.328  -6.172  0.93 24.92  ?  979  HOH B O    1 
HETATM 11338 O  O    . HOH X 4 .   ? 4.002   23.472  9.079   1.00 6.81   ?  980  HOH B O    1 
HETATM 11339 O  O    A HOH X 4 .   ? 9.958   29.341  -5.360  0.90 17.99  ?  981  HOH B O    1 
HETATM 11340 O  O    . HOH X 4 .   ? 19.065  -12.608 -2.016  1.00 28.25  ?  982  HOH B O    1 
HETATM 11341 O  O    . HOH X 4 .   ? 30.702  10.707  2.880   1.00 8.08   ?  983  HOH B O    1 
HETATM 11342 O  O    B HOH X 4 .   ? -6.018  14.338  24.402  0.46 19.08  ?  984  HOH B O    1 
HETATM 11343 O  O    . HOH X 4 .   ? 29.871  21.311  -0.926  1.00 7.93   ?  985  HOH B O    1 
HETATM 11344 O  O    A HOH X 4 .   ? -7.013  13.476  23.679  0.71 21.26  ?  986  HOH B O    1 
HETATM 11345 O  O    . HOH X 4 .   ? 12.132  34.048  22.066  1.00 15.16  ?  987  HOH B O    1 
HETATM 11346 O  O    . HOH X 4 .   ? -13.321 18.797  7.311   1.00 41.10  ?  988  HOH B O    1 
HETATM 11347 O  O    A HOH X 4 .   ? -15.310 35.578  18.641  0.93 19.53  ?  989  HOH B O    1 
HETATM 11348 O  O    A HOH X 4 .   ? 18.782  12.746  -11.738 0.64 16.09  ?  990  HOH B O    1 
HETATM 11349 O  O    . HOH X 4 .   ? 1.863   23.421  23.196  1.00 8.08   ?  991  HOH B O    1 
HETATM 11350 O  O    . HOH X 4 .   ? 11.517  14.031  26.489  1.00 12.74  ?  992  HOH B O    1 
HETATM 11351 O  O    . HOH X 4 .   ? 27.324  -10.652 -4.612  1.00 11.71  ?  993  HOH B O    1 
HETATM 11352 O  O    . HOH X 4 .   ? 7.961   17.667  31.152  1.00 30.40  ?  994  HOH B O    1 
HETATM 11353 O  O    B HOH X 4 .   ? 11.029  35.242  -2.242  0.78 29.75  ?  995  HOH B O    1 
HETATM 11354 O  O    . HOH X 4 .   ? 11.411  27.819  32.140  1.00 21.70  ?  996  HOH B O    1 
HETATM 11355 O  O    . HOH X 4 .   ? 1.277   7.119   -5.068  1.00 17.38  ?  997  HOH B O    1 
HETATM 11356 O  O    . HOH X 4 .   ? 14.883  16.914  -14.815 1.00 17.97  ?  998  HOH B O    1 
HETATM 11357 O  O    . HOH X 4 .   ? 27.168  27.602  5.603   1.00 7.05   ?  999  HOH B O    1 
HETATM 11358 O  O    . HOH X 4 .   ? 16.886  -11.080 -2.608  1.00 34.72  ?  1000 HOH B O    1 
HETATM 11359 O  O    . HOH X 4 .   ? -4.780  21.568  0.048   1.00 22.35  ?  1001 HOH B O    1 
HETATM 11360 O  O    . HOH X 4 .   ? 6.988   7.642   -9.842  1.00 18.07  ?  1002 HOH B O    1 
HETATM 11361 O  O    . HOH X 4 .   ? 5.764   30.689  34.273  1.00 13.95  ?  1003 HOH B O    1 
HETATM 11362 O  O    B HOH X 4 .   ? 5.729   31.895  37.388  0.82 32.87  ?  1004 HOH B O    1 
HETATM 11363 O  O    . HOH X 4 .   ? -5.747  7.988   19.437  1.00 20.46  ?  1005 HOH B O    1 
HETATM 11364 O  O    . HOH X 4 .   ? 15.554  -8.801  -6.701  1.00 30.71  ?  1006 HOH B O    1 
HETATM 11365 O  O    . HOH X 4 .   ? 8.744   4.494   5.768   1.00 19.40  ?  1007 HOH B O    1 
HETATM 11366 O  O    . HOH X 4 .   ? 11.923  31.896  29.317  1.00 26.84  ?  1008 HOH B O    1 
HETATM 11367 O  O    . HOH X 4 .   ? 9.822   35.759  18.103  1.00 10.99  ?  1009 HOH B O    1 
HETATM 11368 O  O    . HOH X 4 .   ? -6.717  45.307  15.989  1.00 50.92  ?  1010 HOH B O    1 
HETATM 11369 O  O    A HOH X 4 .   ? 6.501   10.248  14.381  0.92 17.80  ?  1011 HOH B O    1 
HETATM 11370 O  O    . HOH X 4 .   ? -2.894  29.488  -1.344  1.00 22.99  ?  1012 HOH B O    1 
HETATM 11371 O  O    . HOH X 4 .   ? 22.283  4.384   -15.983 1.00 45.80  ?  1013 HOH B O    1 
HETATM 11372 O  O    A HOH X 4 .   ? -5.328  16.970  1.272   0.57 15.25  ?  1014 HOH B O    1 
HETATM 11373 O  O    . HOH X 4 .   ? 12.465  32.043  2.388   1.00 8.85   ?  1015 HOH B O    1 
HETATM 11374 O  O    . HOH X 4 .   ? 31.411  -12.315 -3.431  1.00 7.73   ?  1016 HOH B O    1 
HETATM 11375 O  O    . HOH X 4 .   ? 17.739  0.502   -13.937 1.00 28.97  ?  1017 HOH B O    1 
HETATM 11376 O  O    . HOH X 4 .   ? 18.914  30.755  5.506   1.00 18.04  ?  1018 HOH B O    1 
HETATM 11377 O  O    C HOH X 4 .   ? 30.170  1.618   -7.187  0.56 17.10  ?  1019 HOH B O    1 
HETATM 11378 O  O    . HOH X 4 .   ? 14.482  25.572  -9.439  1.00 36.11  ?  1020 HOH B O    1 
HETATM 11379 O  O    A HOH X 4 .   ? 13.343  1.753   -5.790  0.72 17.98  ?  1021 HOH B O    1 
HETATM 11380 O  O    . HOH X 4 .   ? -19.162 33.478  13.695  1.00 18.42  ?  1022 HOH B O    1 
HETATM 11381 O  O    A HOH X 4 .   ? 4.369   22.948  24.368  0.62 9.27   ?  1023 HOH B O    1 
HETATM 11382 O  O    . HOH X 4 .   ? -1.902  22.071  35.964  1.00 58.93  ?  1024 HOH B O    1 
HETATM 11383 O  O    . HOH X 4 .   ? 24.885  5.932   -15.404 1.00 22.79  ?  1025 HOH B O    1 
HETATM 11384 O  O    . HOH X 4 .   ? 3.155   43.785  20.323  1.00 12.53  ?  1026 HOH B O    1 
HETATM 11385 O  O    . HOH X 4 .   ? 11.121  18.904  -15.533 1.00 25.62  ?  1027 HOH B O    1 
HETATM 11386 O  O    A HOH X 4 .   ? 5.325   46.305  19.391  0.90 36.57  ?  1028 HOH B O    1 
HETATM 11387 O  O    . HOH X 4 .   ? -16.213 33.867  10.270  1.00 11.76  ?  1029 HOH B O    1 
HETATM 11388 O  O    . HOH X 4 .   ? 8.343   22.670  36.004  1.00 49.94  ?  1030 HOH B O    1 
HETATM 11389 O  O    . HOH X 4 .   ? 30.090  30.130  4.945   1.00 8.09   ?  1031 HOH B O    1 
HETATM 11390 O  O    . HOH X 4 .   ? -9.085  28.312  9.237   1.00 11.78  ?  1032 HOH B O    1 
HETATM 11391 O  O    C HOH X 4 .   ? 15.349  32.656  16.653  0.77 16.27  ?  1033 HOH B O    1 
HETATM 11392 O  O    . HOH X 4 .   ? -4.592  24.768  5.496   1.00 15.57  ?  1034 HOH B O    1 
HETATM 11393 O  O    . HOH X 4 .   ? 22.049  20.564  -11.226 1.00 31.15  ?  1035 HOH B O    1 
HETATM 11394 O  O    . HOH X 4 .   ? 6.025   10.323  -10.936 1.00 20.99  ?  1036 HOH B O    1 
HETATM 11395 O  O    . HOH X 4 .   ? -12.138 39.476  23.551  1.00 32.18  ?  1037 HOH B O    1 
HETATM 11396 O  O    . HOH X 4 .   ? 14.552  36.908  26.854  1.00 49.15  ?  1038 HOH B O    1 
HETATM 11397 O  O    . HOH X 4 .   ? -0.881  13.148  21.509  1.00 11.19  ?  1039 HOH B O    1 
HETATM 11398 O  O    . HOH X 4 .   ? 33.901  -16.112 2.217   1.00 32.16  ?  1040 HOH B O    1 
HETATM 11399 O  O    . HOH X 4 .   ? -5.098  11.768  -5.041  1.00 41.81  ?  1041 HOH B O    1 
HETATM 11400 O  O    A HOH X 4 .   ? -1.099  32.939  -1.819  1.00 45.05  ?  1042 HOH B O    1 
HETATM 11401 O  O    . HOH X 4 .   ? 10.422  43.877  15.983  1.00 29.00  ?  1043 HOH B O    1 
HETATM 11402 O  O    A HOH X 4 .   ? 35.903  30.078  12.526  0.57 16.55  ?  1044 HOH B O    1 
HETATM 11403 O  O    . HOH X 4 .   ? 11.715  17.368  29.194  1.00 26.77  ?  1045 HOH B O    1 
HETATM 11404 O  O    . HOH X 4 .   ? 33.997  17.234  4.458   1.00 12.11  ?  1046 HOH B O    1 
HETATM 11405 O  O    . HOH X 4 .   ? 3.424   5.605   -11.237 1.00 34.57  ?  1047 HOH B O    1 
HETATM 11406 O  O    . HOH X 4 .   ? 37.272  17.968  -4.426  1.00 36.83  ?  1048 HOH B O    1 
HETATM 11407 O  O    . HOH X 4 .   ? 2.131   39.308  9.650   1.00 24.51  ?  1049 HOH B O    1 
HETATM 11408 O  O    . HOH X 4 .   ? 2.276   28.482  -4.795  1.00 12.56  ?  1050 HOH B O    1 
HETATM 11409 O  O    . HOH X 4 .   ? -16.700 26.639  23.396  1.00 15.89  ?  1051 HOH B O    1 
HETATM 11410 O  O    A HOH X 4 .   ? -12.416 32.362  27.901  1.00 41.30  ?  1052 HOH B O    1 
HETATM 11411 O  O    . HOH X 4 .   ? -6.198  20.965  25.056  1.00 8.03   ?  1053 HOH B O    1 
HETATM 11412 O  O    . HOH X 4 .   ? -3.375  11.396  19.866  1.00 16.93  ?  1054 HOH B O    1 
HETATM 11413 O  O    . HOH X 4 .   ? -13.647 39.531  21.189  1.00 20.58  ?  1055 HOH B O    1 
HETATM 11414 O  O    . HOH X 4 .   ? 4.208   26.749  -5.863  1.00 8.33   ?  1056 HOH B O    1 
HETATM 11415 O  O    B HOH X 4 .   ? 34.764  6.374   -2.858  1.00 27.11  ?  1057 HOH B O    1 
HETATM 11416 O  O    . HOH X 4 .   ? -6.028  13.003  5.869   1.00 15.35  ?  1058 HOH B O    1 
HETATM 11417 O  O    . HOH X 4 .   ? -22.593 26.051  18.072  1.00 25.21  ?  1059 HOH B O    1 
HETATM 11418 O  O    . HOH X 4 .   ? 0.114   40.550  2.920   1.00 43.66  ?  1060 HOH B O    1 
HETATM 11419 O  O    B HOH X 4 .   ? -17.046 21.142  6.964   0.98 39.88  ?  1061 HOH B O    1 
HETATM 11420 O  O    . HOH X 4 .   ? 21.801  -0.565  -13.070 1.00 13.87  ?  1062 HOH B O    1 
HETATM 11421 O  O    . HOH X 4 .   ? -11.547 9.493   16.549  1.00 44.47  ?  1063 HOH B O    1 
HETATM 11422 O  O    . HOH X 4 .   ? 21.360  34.643  -0.744  1.00 49.25  ?  1064 HOH B O    1 
HETATM 11423 O  O    B HOH X 4 .   ? 11.525  31.526  26.947  0.48 22.91  ?  1065 HOH B O    1 
HETATM 11424 O  O    . HOH X 4 .   ? 13.355  32.622  7.360   1.00 9.39   ?  1066 HOH B O    1 
HETATM 11425 O  O    . HOH X 4 .   ? -8.460  33.851  9.367   1.00 29.89  ?  1067 HOH B O    1 
HETATM 11426 O  O    A HOH X 4 .   ? 7.048   29.492  -3.379  0.73 14.16  ?  1068 HOH B O    1 
HETATM 11427 O  O    . HOH X 4 .   ? 29.265  -18.065 3.224   1.00 16.11  ?  1069 HOH B O    1 
HETATM 11428 O  O    . HOH X 4 .   ? -4.934  15.273  -9.312  1.00 52.32  ?  1070 HOH B O    1 
HETATM 11429 O  O    . HOH X 4 .   ? 13.610  27.983  24.334  1.00 41.91  ?  1071 HOH B O    1 
HETATM 11430 O  O    . HOH X 4 .   ? 12.935  35.368  11.448  1.00 16.76  ?  1072 HOH B O    1 
HETATM 11431 O  O    B HOH X 4 .   ? -3.855  16.566  -0.764  0.84 17.89  ?  1073 HOH B O    1 
HETATM 11432 O  O    . HOH X 4 .   ? 19.455  11.442  -14.952 1.00 46.59  ?  1074 HOH B O    1 
HETATM 11433 O  O    . HOH X 4 .   ? -17.238 29.611  10.168  1.00 24.89  ?  1075 HOH B O    1 
HETATM 11434 O  O    . HOH X 4 .   ? 5.581   15.178  6.400   1.00 6.47   ?  1076 HOH B O    1 
HETATM 11435 O  O    . HOH X 4 .   ? 15.330  -10.538 -0.015  1.00 38.16  ?  1077 HOH B O    1 
HETATM 11436 O  O    . HOH X 4 .   ? 21.822  -6.896  -5.959  1.00 16.36  ?  1078 HOH B O    1 
HETATM 11437 O  O    B HOH X 4 .   ? 24.189  3.159   -14.748 1.00 36.37  ?  1079 HOH B O    1 
HETATM 11438 O  O    . HOH X 4 .   ? 24.635  36.279  4.777   1.00 26.36  ?  1080 HOH B O    1 
HETATM 11439 O  O    . HOH X 4 .   ? 21.221  33.887  6.459   1.00 38.35  ?  1081 HOH B O    1 
HETATM 11440 O  O    B HOH X 4 .   ? -14.959 20.915  22.074  0.49 9.53   ?  1082 HOH B O    1 
HETATM 11441 O  O    . HOH X 4 .   ? -16.129 30.183  12.686  1.00 12.47  ?  1083 HOH B O    1 
HETATM 11442 O  O    . HOH X 4 .   ? 5.231   11.306  20.089  1.00 13.43  ?  1084 HOH B O    1 
HETATM 11443 O  O    . HOH X 4 .   ? -14.516 32.286  11.954  1.00 8.27   ?  1085 HOH B O    1 
HETATM 11444 O  O    . HOH X 4 .   ? 0.231   9.463   -3.759  1.00 49.27  ?  1086 HOH B O    1 
HETATM 11445 O  O    . HOH X 4 .   ? 7.634   33.433  0.194   1.00 21.42  ?  1087 HOH B O    1 
HETATM 11446 O  O    . HOH X 4 .   ? 8.216   27.671  -7.801  1.00 30.96  ?  1088 HOH B O    1 
HETATM 11447 O  O    . HOH X 4 .   ? -14.185 41.560  19.606  1.00 41.10  ?  1089 HOH B O    1 
HETATM 11448 O  O    A HOH X 4 .   ? -0.906  14.799  2.693   0.88 13.54  ?  1090 HOH B O    1 
HETATM 11449 O  O    . HOH X 4 .   ? 19.271  23.727  18.507  1.00 36.65  ?  1091 HOH B O    1 
HETATM 11450 O  O    B HOH X 4 .   ? 12.464  7.247   3.573   0.93 13.53  ?  1092 HOH B O    1 
HETATM 11451 O  O    . HOH X 4 .   ? 13.069  8.731   -13.507 1.00 32.73  ?  1093 HOH B O    1 
HETATM 11452 O  O    . HOH X 4 .   ? 18.487  30.909  20.057  1.00 52.24  ?  1094 HOH B O    1 
HETATM 11453 O  O    . HOH X 4 .   ? -10.818 33.978  8.194   1.00 53.49  ?  1095 HOH B O    1 
HETATM 11454 O  O    . HOH X 4 .   ? -4.211  32.147  35.219  1.00 21.43  ?  1096 HOH B O    1 
HETATM 11455 O  O    B HOH X 4 .   ? 13.182  34.164  25.809  0.96 41.06  ?  1097 HOH B O    1 
HETATM 11456 O  O    B HOH X 4 .   ? 17.506  6.122   -15.055 0.86 57.23  ?  1098 HOH B O    1 
HETATM 11457 O  O    . HOH X 4 .   ? -5.378  41.956  17.498  1.00 45.83  ?  1099 HOH B O    1 
HETATM 11458 O  O    A HOH X 4 .   ? -14.989 20.411  21.245  0.63 10.06  ?  1100 HOH B O    1 
HETATM 11459 O  O    . HOH X 4 .   ? 28.636  -7.792  -3.027  1.00 11.68  ?  1101 HOH B O    1 
HETATM 11460 O  O    A HOH X 4 .   ? -5.024  19.554  -2.749  1.00 39.77  ?  1102 HOH B O    1 
HETATM 11461 O  O    B HOH X 4 .   ? -11.166 14.433  24.084  0.99 36.01  ?  1103 HOH B O    1 
HETATM 11462 O  O    . HOH X 4 .   ? 18.615  29.742  -5.487  1.00 48.58  ?  1104 HOH B O    1 
HETATM 11463 O  O    . HOH X 4 .   ? -18.446 38.147  15.467  1.00 28.09  ?  1105 HOH B O    1 
HETATM 11464 O  O    A HOH X 4 .   ? 36.395  7.758   -3.866  1.00 45.73  ?  1106 HOH B O    1 
HETATM 11465 O  O    . HOH X 4 .   ? -1.554  31.122  40.955  1.00 23.17  ?  1107 HOH B O    1 
HETATM 11466 O  O    A HOH X 4 .   ? -5.039  32.058  5.936   0.95 19.46  ?  1108 HOH B O    1 
HETATM 11467 O  O    . HOH X 4 .   ? 0.266   2.982   -3.174  1.00 48.14  ?  1109 HOH B O    1 
HETATM 11468 O  O    . HOH X 4 .   ? 12.549  34.699  8.946   1.00 24.97  ?  1110 HOH B O    1 
HETATM 11469 O  O    B HOH X 4 .   ? -5.965  33.667  5.671   0.97 51.88  ?  1111 HOH B O    1 
HETATM 11470 O  O    . HOH X 4 .   ? 18.080  13.469  -16.033 1.00 35.86  ?  1112 HOH B O    1 
HETATM 11471 O  O    B HOH X 4 .   ? 13.472  23.341  23.568  0.92 38.36  ?  1113 HOH B O    1 
HETATM 11472 O  O    A HOH X 4 .   ? -9.975  9.662   20.042  0.97 38.88  ?  1114 HOH B O    1 
HETATM 11473 O  O    . HOH X 4 .   ? 29.489  17.710  -7.280  1.00 27.84  ?  1115 HOH B O    1 
HETATM 11474 O  O    . HOH X 4 .   ? -4.861  22.902  32.645  1.00 44.99  ?  1116 HOH B O    1 
HETATM 11475 O  O    . HOH X 4 .   ? 6.208   37.490  -1.205  1.00 33.87  ?  1117 HOH B O    1 
HETATM 11476 O  O    . HOH X 4 .   ? 9.644   25.596  33.219  1.00 16.05  ?  1118 HOH B O    1 
HETATM 11477 O  O    . HOH X 4 .   ? 19.196  31.366  -3.287  1.00 53.41  ?  1119 HOH B O    1 
HETATM 11478 O  O    A HOH X 4 .   ? -7.421  32.508  7.048   1.00 34.38  ?  1120 HOH B O    1 
HETATM 11479 O  O    B HOH X 4 .   ? 13.669  36.549  18.590  1.00 56.40  ?  1121 HOH B O    1 
HETATM 11480 O  O    A HOH X 4 .   ? -0.409  34.595  1.264   0.91 22.81  ?  1122 HOH B O    1 
HETATM 11481 O  O    . HOH X 4 .   ? 31.029  15.439  2.749   1.00 24.11  ?  1123 HOH B O    1 
HETATM 11482 O  O    . HOH X 4 .   ? -5.142  30.850  0.891   1.00 44.69  ?  1124 HOH B O    1 
HETATM 11483 O  O    . HOH X 4 .   ? -1.131  46.145  16.839  1.00 37.93  ?  1125 HOH B O    1 
HETATM 11484 O  O    . HOH X 4 .   ? -4.514  25.673  -1.760  1.00 42.78  ?  1126 HOH B O    1 
HETATM 11485 O  O    . HOH X 4 .   ? -1.773  43.908  10.871  1.00 46.68  ?  1127 HOH B O    1 
HETATM 11486 O  O    . HOH X 4 .   ? -8.599  8.280   18.295  1.00 30.78  ?  1128 HOH B O    1 
HETATM 11487 O  O    . HOH X 4 .   ? 21.075  -14.630 4.799   1.00 41.27  ?  1129 HOH B O    1 
HETATM 11488 O  O    B HOH X 4 .   ? 15.291  8.321   8.901   0.95 30.88  ?  1130 HOH B O    1 
HETATM 11489 O  O    B HOH X 4 .   ? 32.934  2.548   -7.722  0.97 57.76  ?  1131 HOH B O    1 
HETATM 11490 O  O    . HOH X 4 .   ? 17.779  30.691  8.284   1.00 14.43  ?  1132 HOH B O    1 
HETATM 11491 O  O    . HOH X 4 .   ? 0.861   39.242  7.234   1.00 37.61  ?  1133 HOH B O    1 
HETATM 11492 O  O    . HOH X 4 .   ? 15.590  1.519   4.618   1.00 41.98  ?  1134 HOH B O    1 
HETATM 11493 O  O    . HOH X 4 .   ? -9.419  35.213  30.536  1.00 32.97  ?  1135 HOH B O    1 
HETATM 11494 O  O    . HOH X 4 .   ? 3.269   5.516   1.904   1.00 28.06  ?  1136 HOH B O    1 
HETATM 11495 O  O    B HOH X 4 .   ? -13.731 34.319  5.967   0.83 37.38  ?  1137 HOH B O    1 
HETATM 11496 O  O    A HOH X 4 .   ? 1.497   0.321   3.405   0.80 31.81  ?  1138 HOH B O    1 
HETATM 11497 O  O    . HOH X 4 .   ? 8.960   32.351  31.416  1.00 14.89  ?  1139 HOH B O    1 
HETATM 11498 O  O    B HOH X 4 .   ? 33.807  12.619  3.237   0.89 28.76  ?  1140 HOH B O    1 
HETATM 11499 O  O    . HOH X 4 .   ? 0.543   7.769   -13.595 1.00 47.52  ?  1141 HOH B O    1 
HETATM 11500 O  O    . HOH X 4 .   ? 11.582  37.967  10.701  1.00 40.75  ?  1142 HOH B O    1 
HETATM 11501 O  O    A HOH X 4 .   ? -8.619  20.469  26.292  1.00 25.61  ?  1143 HOH B O    1 
HETATM 11502 O  O    . HOH X 4 .   ? -8.851  41.914  24.314  1.00 45.64  ?  1144 HOH B O    1 
HETATM 11503 O  O    . HOH X 4 .   ? -5.193  7.404   -9.185  1.00 39.26  ?  1145 HOH B O    1 
HETATM 11504 O  O    . HOH X 4 .   ? -8.408  26.412  3.126   1.00 39.71  ?  1146 HOH B O    1 
HETATM 11505 O  O    . HOH X 4 .   ? 23.086  -14.715 -5.157  1.00 27.96  ?  1147 HOH B O    1 
HETATM 11506 O  O    . HOH X 4 .   ? -8.089  30.500  31.663  1.00 40.62  ?  1148 HOH B O    1 
HETATM 11507 O  O    . HOH X 4 .   ? 6.397   21.146  35.728  1.00 37.81  ?  1149 HOH B O    1 
HETATM 11508 O  O    B HOH X 4 .   ? 13.071  2.782   -6.771  0.72 16.77  ?  1150 HOH B O    1 
HETATM 11509 O  O    . HOH X 4 .   ? 30.982  -16.044 5.401   1.00 56.21  ?  1151 HOH B O    1 
HETATM 11510 O  O    . HOH X 4 .   ? 22.321  26.725  -4.279  1.00 26.06  ?  1152 HOH B O    1 
HETATM 11511 O  O    B HOH X 4 .   ? 33.440  8.283   2.634   0.69 17.43  ?  1153 HOH B O    1 
HETATM 11512 O  O    . HOH X 4 .   ? 22.666  8.845   -15.571 1.00 52.51  ?  1154 HOH B O    1 
HETATM 11513 O  O    A HOH X 4 .   ? 25.725  3.775   -13.656 0.99 25.23  ?  1155 HOH B O    1 
HETATM 11514 O  O    A HOH X 4 .   ? -7.534  8.463   11.099  1.00 41.39  ?  1156 HOH B O    1 
HETATM 11515 O  O    . HOH X 4 .   ? 23.947  -19.258 -3.548  1.00 30.76  ?  1157 HOH B O    1 
HETATM 11516 O  O    . HOH X 4 .   ? 17.316  -8.416  -8.469  1.00 16.32  ?  1158 HOH B O    1 
HETATM 11517 O  O    . HOH X 4 .   ? -0.734  43.650  20.454  1.00 25.31  ?  1159 HOH B O    1 
HETATM 11518 O  O    B HOH X 4 .   ? -5.284  21.529  -3.351  1.00 43.22  ?  1160 HOH B O    1 
HETATM 11519 O  O    . HOH X 4 .   ? -4.758  30.214  37.839  1.00 35.36  ?  1161 HOH B O    1 
HETATM 11520 O  O    . HOH X 4 .   ? 15.198  11.370  10.627  1.00 10.85  ?  1162 HOH B O    1 
HETATM 11521 O  O    . HOH X 4 .   ? 31.476  -2.917  -2.150  1.00 20.80  ?  1163 HOH B O    1 
HETATM 11522 O  O    B HOH X 4 .   ? 12.396  11.428  14.259  0.83 31.18  ?  1164 HOH B O    1 
HETATM 11523 O  O    . HOH X 4 .   ? -19.407 24.731  21.609  1.00 43.61  ?  1165 HOH B O    1 
HETATM 11524 O  O    . HOH X 4 .   ? -10.096 36.835  28.363  1.00 37.69  ?  1166 HOH B O    1 
HETATM 11525 O  O    . HOH X 4 .   ? 7.886   7.829   -12.225 1.00 33.23  ?  1167 HOH B O    1 
HETATM 11526 O  O    . HOH X 4 .   ? -16.937 34.078  19.135  1.00 30.28  ?  1168 HOH B O    1 
HETATM 11527 O  O    B HOH X 4 .   ? 34.311  26.854  6.833   0.84 31.19  ?  1169 HOH B O    1 
HETATM 11528 O  O    . HOH X 4 .   ? 6.677   45.481  13.725  1.00 38.26  ?  1170 HOH B O    1 
HETATM 11529 O  O    A HOH X 4 .   ? 32.429  13.415  1.642   0.99 30.66  ?  1171 HOH B O    1 
HETATM 11530 O  O    B HOH X 4 .   ? 1.053   10.534  17.991  0.41 11.38  ?  1172 HOH B O    1 
HETATM 11531 O  O    B HOH X 4 .   ? -0.660  31.159  -2.718  1.00 43.50  ?  1173 HOH B O    1 
HETATM 11532 O  O    . HOH X 4 .   ? 12.408  17.225  31.922  1.00 54.88  ?  1174 HOH B O    1 
HETATM 11533 O  O    . HOH X 4 .   ? 13.420  2.380   3.720   1.00 39.80  ?  1175 HOH B O    1 
HETATM 11534 O  O    A HOH X 4 .   ? 5.599   45.338  9.969   0.99 38.42  ?  1176 HOH B O    1 
HETATM 11535 O  O    . HOH X 4 .   ? 33.681  -4.102  5.064   1.00 54.94  ?  1177 HOH B O    1 
HETATM 11536 O  O    . HOH X 4 .   ? 14.966  40.606  17.101  1.00 59.26  ?  1178 HOH B O    1 
HETATM 11537 O  O    . HOH X 4 .   ? 9.838   21.164  31.210  1.00 25.80  ?  1179 HOH B O    1 
HETATM 11538 O  O    A HOH X 4 .   ? 16.253  34.104  3.757   1.00 49.96  ?  1180 HOH B O    1 
HETATM 11539 O  O    . HOH X 4 .   ? -18.354 31.765  17.266  1.00 24.28  ?  1181 HOH B O    1 
HETATM 11540 O  O    . HOH X 4 .   ? 14.141  -1.267  0.978   1.00 52.77  ?  1182 HOH B O    1 
HETATM 11541 O  O    . HOH X 4 .   ? -18.138 24.848  7.803   1.00 53.78  ?  1183 HOH B O    1 
HETATM 11542 O  O    . HOH X 4 .   ? -13.904 38.508  25.174  1.00 45.07  ?  1184 HOH B O    1 
HETATM 11543 O  O    B HOH X 4 .   ? 7.472   32.508  -2.437  0.98 41.24  ?  1185 HOH B O    1 
HETATM 11544 O  O    . HOH X 4 .   ? 9.710   43.297  13.464  1.00 38.49  ?  1186 HOH B O    1 
HETATM 11545 O  O    B HOH X 4 .   ? 20.043  20.662  15.524  0.75 25.26  ?  1187 HOH B O    1 
HETATM 11546 O  O    . HOH X 4 .   ? 19.491  32.671  9.637   1.00 32.93  ?  1188 HOH B O    1 
HETATM 11547 O  O    . HOH X 4 .   ? -7.615  33.244  31.287  1.00 46.29  ?  1189 HOH B O    1 
HETATM 11548 O  O    . HOH X 4 .   ? 22.178  28.838  -5.901  1.00 38.12  ?  1190 HOH B O    1 
HETATM 11549 O  O    B HOH X 4 .   ? 4.450   44.848  11.848  0.92 33.07  ?  1191 HOH B O    1 
HETATM 11550 O  O    . HOH X 4 .   ? -10.681 40.662  10.809  1.00 28.67  ?  1192 HOH B O    1 
HETATM 11551 O  O    . HOH X 4 .   ? -16.659 39.970  17.714  1.00 44.26  ?  1193 HOH B O    1 
HETATM 11552 O  O    . HOH X 4 .   ? 32.258  19.854  1.961   1.00 10.20  ?  1194 HOH B O    1 
HETATM 11553 O  O    A HOH X 4 .   ? 15.492  1.986   -12.977 0.94 29.51  ?  1195 HOH B O    1 
HETATM 11554 O  O    . HOH X 4 .   ? 15.535  34.309  17.883  1.00 51.18  ?  1196 HOH B O    1 
HETATM 11555 O  O    . HOH X 4 .   ? -9.622  23.778  7.129   1.00 22.60  ?  1197 HOH B O    1 
HETATM 11556 O  O    . HOH X 4 .   ? 14.548  19.215  23.525  1.00 23.26  ?  1198 HOH B O    1 
HETATM 11557 O  O    B HOH X 4 .   ? -9.891  45.335  14.538  0.67 31.88  ?  1199 HOH B O    1 
HETATM 11558 O  O    A HOH X 4 .   ? 23.460  24.718  -6.332  0.90 35.22  ?  1200 HOH B O    1 
HETATM 11559 O  O    A HOH X 4 .   ? 9.686   34.283  -2.914  0.71 27.00  ?  1201 HOH B O    1 
HETATM 11560 O  O    . HOH X 4 .   ? 12.111  30.135  31.610  1.00 42.65  ?  1202 HOH B O    1 
HETATM 11561 O  O    . HOH X 4 .   ? 15.796  38.397  16.290  1.00 60.46  ?  1203 HOH B O    1 
HETATM 11562 O  O    . HOH X 4 .   ? 13.962  24.213  -11.584 1.00 28.66  ?  1204 HOH B O    1 
HETATM 11563 O  O    B HOH X 4 .   ? 28.550  -19.973 4.553   0.62 30.28  ?  1205 HOH B O    1 
HETATM 11564 O  O    A HOH X 4 .   ? 8.418   29.837  34.823  0.58 19.03  ?  1206 HOH B O    1 
HETATM 11565 O  O    B HOH X 4 .   ? 15.528  2.036   -14.948 1.00 43.22  ?  1207 HOH B O    1 
HETATM 11566 O  O    . HOH X 4 .   ? -11.037 14.937  26.784  1.00 42.89  ?  1208 HOH B O    1 
HETATM 11567 O  O    . HOH X 4 .   ? -4.726  14.421  -0.781  1.00 58.63  ?  1209 HOH B O    1 
HETATM 11568 O  O    . HOH X 4 .   ? -12.021 22.803  28.127  1.00 45.60  ?  1210 HOH B O    1 
HETATM 11569 O  O    B HOH X 4 .   ? 19.804  13.406  -11.159 0.38 8.26   ?  1211 HOH B O    1 
HETATM 11570 O  O    C HOH X 4 .   ? 15.371  -1.441  5.090   1.00 48.95  ?  1212 HOH B O    1 
HETATM 11571 O  O    A HOH X 4 .   ? 10.394  -0.360  -5.828  1.00 52.28  ?  1213 HOH B O    1 
HETATM 11572 O  O    . HOH X 4 .   ? -1.128  10.557  -0.541  1.00 39.88  ?  1214 HOH B O    1 
HETATM 11573 O  O    . HOH X 4 .   ? 32.810  17.105  1.771   1.00 17.28  ?  1215 HOH B O    1 
HETATM 11574 O  O    . HOH X 4 .   ? 14.573  35.912  1.261   1.00 31.46  ?  1216 HOH B O    1 
HETATM 11575 O  O    . HOH X 4 .   ? -11.199 40.895  8.464   1.00 32.43  ?  1217 HOH B O    1 
HETATM 11576 O  O    . HOH X 4 .   ? 19.314  -0.667  -11.810 1.00 17.28  ?  1218 HOH B O    1 
HETATM 11577 O  O    A HOH X 4 .   ? 21.438  13.443  -12.208 1.00 32.06  ?  1219 HOH B O    1 
HETATM 11578 O  O    A HOH X 4 .   ? -11.319 27.176  7.733   1.00 34.37  ?  1220 HOH B O    1 
HETATM 11579 O  O    . HOH X 4 .   ? 3.525   11.228  16.357  1.00 13.10  ?  1221 HOH B O    1 
HETATM 11580 O  O    . HOH X 4 .   ? 10.244  23.365  33.894  1.00 47.03  ?  1222 HOH B O    1 
HETATM 11581 O  O    . HOH X 4 .   ? 20.949  24.454  -9.658  1.00 30.86  ?  1223 HOH B O    1 
HETATM 11582 O  O    . HOH X 4 .   ? -18.194 30.934  14.408  1.00 18.73  ?  1224 HOH B O    1 
HETATM 11583 O  O    . HOH X 4 .   ? -15.808 31.011  27.149  1.00 31.46  ?  1225 HOH B O    1 
HETATM 11584 O  O    . HOH X 4 .   ? -19.613 37.229  12.676  1.00 15.95  ?  1226 HOH B O    1 
HETATM 11585 O  O    . HOH X 4 .   ? 30.903  5.506   -11.252 1.00 45.39  ?  1227 HOH B O    1 
HETATM 11586 O  O    . HOH X 4 .   ? 9.018   44.893  20.114  1.00 52.41  ?  1228 HOH B O    1 
HETATM 11587 O  O    . HOH X 4 .   ? 8.969   26.948  35.494  1.00 27.29  ?  1229 HOH B O    1 
HETATM 11588 O  O    A HOH X 4 .   ? 19.322  7.618   -15.318 1.00 48.04  ?  1230 HOH B O    1 
HETATM 11589 O  O    . HOH X 4 .   ? 15.090  40.398  19.452  1.00 48.88  ?  1231 HOH B O    1 
HETATM 11590 O  O    . HOH X 4 .   ? 33.313  10.534  -13.082 1.00 28.89  ?  1232 HOH B O    1 
HETATM 11591 O  O    . HOH X 4 .   ? 34.283  -0.886  1.184   1.00 28.68  ?  1233 HOH B O    1 
HETATM 11592 O  O    . HOH X 4 .   ? 12.203  0.769   -4.575  1.00 31.08  ?  1234 HOH B O    1 
HETATM 11593 O  O    C HOH X 4 .   ? 4.888   8.953   3.459   0.31 9.44   ?  1235 HOH B O    1 
HETATM 11594 O  O    A HOH X 4 .   ? 14.457  -7.471  -4.726  1.00 38.49  ?  1236 HOH B O    1 
HETATM 11595 O  O    A HOH X 4 .   ? 11.178  3.963   -8.545  1.00 46.37  ?  1237 HOH B O    1 
HETATM 11596 O  O    . HOH X 4 .   ? 9.415   20.477  -19.258 1.00 31.18  ?  1238 HOH B O    1 
HETATM 11597 O  O    . HOH X 4 .   ? -9.191  12.299  25.148  1.00 49.51  ?  1239 HOH B O    1 
HETATM 11598 O  O    . HOH X 4 .   ? -6.926  24.341  4.580   1.00 36.78  ?  1240 HOH B O    1 
HETATM 11599 O  O    B HOH X 4 .   ? 4.054   47.607  18.427  0.75 44.74  ?  1241 HOH B O    1 
HETATM 11600 O  O    B HOH X 4 .   ? -6.338  17.029  -0.452  1.00 65.10  ?  1242 HOH B O    1 
HETATM 11601 O  O    . HOH X 4 .   ? -18.459 34.862  11.409  1.00 15.15  ?  1243 HOH B O    1 
HETATM 11602 O  O    B HOH X 4 .   ? 11.194  4.397   -10.646 0.74 26.92  ?  1244 HOH B O    1 
HETATM 11603 O  O    . HOH X 4 .   ? 1.914   45.184  3.421   1.00 42.42  ?  1245 HOH B O    1 
HETATM 11604 O  O    . HOH X 4 .   ? -3.531  17.577  32.144  1.00 29.57  ?  1246 HOH B O    1 
HETATM 11605 O  O    . HOH X 4 .   ? 1.504   18.161  32.428  1.00 27.55  ?  1247 HOH B O    1 
HETATM 11606 O  O    . HOH X 4 .   ? 13.837  32.986  4.643   1.00 15.24  ?  1248 HOH B O    1 
HETATM 11607 O  O    . HOH X 4 .   ? 22.246  11.301  -13.730 1.00 53.05  ?  1249 HOH B O    1 
HETATM 11608 O  O    . HOH X 4 .   ? 15.659  14.229  -14.263 1.00 21.58  ?  1250 HOH B O    1 
HETATM 11609 O  O    . HOH X 4 .   ? 14.163  17.528  27.994  1.00 23.89  ?  1251 HOH B O    1 
HETATM 11610 O  O    B HOH X 4 .   ? -9.251  44.155  8.591   0.91 22.54  ?  1252 HOH B O    1 
HETATM 11611 O  O    . HOH X 4 .   ? 33.561  -8.589  5.491   1.00 47.86  ?  1253 HOH B O    1 
HETATM 11612 O  O    . HOH X 4 .   ? 18.636  -11.296 3.453   1.00 42.21  ?  1254 HOH B O    1 
HETATM 11613 O  O    . HOH X 4 .   ? 1.587   44.542  24.240  1.00 27.54  ?  1255 HOH B O    1 
HETATM 11614 O  O    . HOH X 4 .   ? 5.429   43.402  21.841  1.00 16.35  ?  1256 HOH B O    1 
HETATM 11615 O  O    . HOH X 4 .   ? 12.667  21.092  27.745  1.00 33.36  ?  1257 HOH B O    1 
HETATM 11616 O  O    B HOH X 4 .   ? 34.665  13.981  -1.001  0.63 19.49  ?  1258 HOH B O    1 
HETATM 11617 O  O    . HOH X 4 .   ? 6.381   32.810  32.604  1.00 16.41  ?  1259 HOH B O    1 
HETATM 11618 O  O    A HOH X 4 .   ? 0.918   10.178  -1.855  0.96 26.37  ?  1260 HOH B O    1 
HETATM 11619 O  O    . HOH X 4 .   ? -0.529  5.108   -5.749  1.00 30.28  ?  1261 HOH B O    1 
HETATM 11620 O  O    A HOH X 4 .   ? 13.597  32.146  26.683  1.00 44.70  ?  1262 HOH B O    1 
HETATM 11621 O  O    B HOH X 4 .   ? -16.342 14.881  27.122  1.00 49.78  ?  1263 HOH B O    1 
HETATM 11622 O  O    . HOH X 4 .   ? 33.028  -6.448  4.553   1.00 34.06  ?  1264 HOH B O    1 
HETATM 11623 O  O    . HOH X 4 .   ? 19.957  -7.736  -8.061  1.00 19.96  ?  1265 HOH B O    1 
HETATM 11624 O  O    . HOH X 4 .   ? -16.201 23.756  24.264  1.00 45.11  ?  1266 HOH B O    1 
HETATM 11625 O  O    . HOH X 4 .   ? 35.114  -3.584  0.883   1.00 36.07  ?  1267 HOH B O    1 
HETATM 11626 O  O    . HOH X 4 .   ? 20.262  29.496  -7.667  1.00 51.61  ?  1268 HOH B O    1 
HETATM 11627 O  O    . HOH X 4 .   ? -3.028  23.642  34.387  1.00 55.07  ?  1269 HOH B O    1 
HETATM 11628 O  O    C HOH X 4 .   ? -12.369 19.427  26.983  0.81 49.30  ?  1270 HOH B O    1 
HETATM 11629 O  O    . HOH X 4 .   ? 6.295   28.495  -5.526  1.00 23.72  ?  1271 HOH B O    1 
HETATM 11630 O  O    . HOH X 4 .   ? 13.813  43.025  20.984  1.00 47.06  ?  1272 HOH B O    1 
HETATM 11631 O  O    . HOH X 4 .   ? 13.523  27.773  28.518  1.00 30.15  ?  1273 HOH B O    1 
HETATM 11632 O  O    . HOH X 4 .   ? 3.027   14.886  -13.080 1.00 27.31  ?  1274 HOH B O    1 
HETATM 11633 O  O    . HOH X 4 .   ? -7.436  19.540  -8.865  1.00 56.24  ?  1275 HOH B O    1 
HETATM 11634 O  O    . HOH X 4 .   ? 1.491   -3.176  -1.979  1.00 53.89  ?  1276 HOH B O    1 
HETATM 11635 O  O    . HOH X 4 .   ? 3.665   43.998  25.798  1.00 20.06  ?  1277 HOH B O    1 
HETATM 11636 O  O    . HOH X 4 .   ? 15.728  25.354  -12.889 1.00 47.88  ?  1278 HOH B O    1 
HETATM 11637 O  O    B HOH X 4 .   ? 10.467  -2.520  -5.256  1.00 36.46  ?  1279 HOH B O    1 
HETATM 11638 O  O    B HOH X 4 .   ? 10.707  34.424  1.429   0.68 32.68  ?  1280 HOH B O    1 
HETATM 11639 O  O    . HOH X 4 .   ? 2.275   46.322  20.080  1.00 27.77  ?  1281 HOH B O    1 
HETATM 11640 O  O    . HOH X 4 .   ? -16.933 33.770  21.871  1.00 50.01  ?  1282 HOH B O    1 
HETATM 11641 O  O    . HOH X 4 .   ? 9.406   34.884  -0.552  1.00 50.47  ?  1283 HOH B O    1 
HETATM 11642 O  O    . HOH X 4 .   ? 10.272  30.700  33.348  1.00 22.96  ?  1284 HOH B O    1 
HETATM 11643 O  O    . HOH X 4 .   ? 12.091  24.397  25.857  1.00 32.50  ?  1285 HOH B O    1 
HETATM 11644 O  O    . HOH X 4 .   ? -8.293  15.605  -0.994  1.00 66.97  ?  1286 HOH B O    1 
HETATM 11645 O  O    . HOH X 4 .   ? 4.449   35.323  31.886  1.00 12.83  ?  1287 HOH B O    1 
HETATM 11646 O  O    . HOH X 4 .   ? 5.088   17.640  -15.804 1.00 21.92  ?  1288 HOH B O    1 
HETATM 11647 O  O    . HOH X 4 .   ? -12.364 31.709  10.313  1.00 14.04  ?  1289 HOH B O    1 
HETATM 11648 O  O    A HOH X 4 .   ? 7.213   31.110  37.057  0.83 13.62  ?  1290 HOH B O    1 
HETATM 11649 O  O    . HOH X 4 .   ? -19.742 27.548  19.848  1.00 46.02  ?  1291 HOH B O    1 
HETATM 11650 O  O    B HOH X 4 .   ? -12.994 32.487  29.709  1.00 62.39  ?  1292 HOH B O    1 
HETATM 11651 O  O    B HOH X 4 .   ? 34.906  5.583   1.290   0.65 30.66  ?  1293 HOH B O    1 
HETATM 11652 O  O    A HOH X 4 .   ? -11.257 44.739  13.308  0.86 37.68  ?  1294 HOH B O    1 
HETATM 11653 O  O    . HOH X 4 .   ? 8.970   17.933  -17.409 1.00 35.05  ?  1295 HOH B O    1 
HETATM 11654 O  O    A HOH X 4 .   ? -18.892 14.632  28.807  0.97 45.96  ?  1296 HOH B O    1 
HETATM 11655 O  O    . HOH X 4 .   ? 25.636  34.039  -2.365  1.00 37.64  ?  1297 HOH B O    1 
HETATM 11656 O  O    . HOH X 4 .   ? 7.348   19.729  32.008  1.00 31.48  ?  1298 HOH B O    1 
HETATM 11657 O  O    A HOH X 4 .   ? -7.149  32.958  4.461   1.00 65.12  ?  1299 HOH B O    1 
HETATM 11658 O  O    B HOH X 4 .   ? -11.192 25.589  6.493   0.98 32.66  ?  1300 HOH B O    1 
HETATM 11659 O  O    . HOH X 4 .   ? 33.829  20.064  4.162   1.00 10.58  ?  1301 HOH B O    1 
HETATM 11660 O  O    . HOH X 4 .   ? 21.298  0.331   -15.775 1.00 27.08  ?  1302 HOH B O    1 
HETATM 11661 O  O    . HOH X 4 .   ? 9.165   12.304  -16.312 1.00 41.95  ?  1303 HOH B O    1 
HETATM 11662 O  O    . HOH X 4 .   ? -4.203  43.603  19.006  1.00 34.41  ?  1304 HOH B O    1 
HETATM 11663 O  O    . HOH X 4 .   ? -6.449  12.855  -3.054  1.00 61.24  ?  1305 HOH B O    1 
HETATM 11664 O  O    . HOH X 4 .   ? 20.890  19.851  -14.472 1.00 46.10  ?  1306 HOH B O    1 
HETATM 11665 O  O    . HOH X 4 .   ? -13.545 21.056  26.009  1.00 43.96  ?  1307 HOH B O    1 
HETATM 11666 O  O    . HOH X 4 .   ? 16.821  17.473  -16.877 1.00 27.79  ?  1308 HOH B O    1 
HETATM 11667 O  O    . HOH X 4 .   ? 10.095  27.728  25.179  1.00 16.70  ?  1309 HOH B O    1 
HETATM 11668 O  O    . HOH X 4 .   ? 23.608  20.985  -8.281  1.00 43.58  ?  1310 HOH B O    1 
HETATM 11669 O  O    . HOH X 4 .   ? -1.198  0.188   2.706   1.00 54.55  ?  1311 HOH B O    1 
HETATM 11670 O  O    . HOH X 4 .   ? 15.636  -4.853  -1.941  1.00 23.69  ?  1312 HOH B O    1 
HETATM 11671 O  O    . HOH X 4 .   ? -21.653 33.653  14.432  1.00 21.67  ?  1313 HOH B O    1 
HETATM 11672 O  O    . HOH X 4 .   ? 18.852  19.378  -16.781 1.00 43.90  ?  1314 HOH B O    1 
HETATM 11673 O  O    . HOH X 4 .   ? -3.914  46.010  17.798  1.00 52.17  ?  1315 HOH B O    1 
HETATM 11674 O  O    . HOH X 4 .   ? -15.816 37.785  20.219  1.00 34.17  ?  1316 HOH B O    1 
HETATM 11675 O  O    . HOH X 4 .   ? 23.002  18.414  -12.843 1.00 32.34  ?  1317 HOH B O    1 
HETATM 11676 O  O    B HOH X 4 .   ? 18.550  19.735  18.451  0.60 34.32  ?  1318 HOH B O    1 
HETATM 11677 O  O    . HOH X 4 .   ? 18.245  27.465  20.645  1.00 57.46  ?  1319 HOH B O    1 
HETATM 11678 O  O    . HOH X 4 .   ? -10.630 17.774  27.439  1.00 36.45  ?  1320 HOH B O    1 
HETATM 11679 O  O    . HOH X 4 .   ? 5.218   1.233   5.575   1.00 30.47  ?  1321 HOH B O    1 
HETATM 11680 O  O    . HOH X 4 .   ? 19.553  -12.133 -10.066 1.00 39.41  ?  1322 HOH B O    1 
HETATM 11681 O  O    . HOH X 4 .   ? -4.998  12.422  1.717   1.00 55.74  ?  1323 HOH B O    1 
HETATM 11682 O  O    . HOH X 4 .   ? 15.062  21.280  -17.107 1.00 25.29  ?  1324 HOH B O    1 
HETATM 11683 O  O    . HOH X 4 .   ? -4.836  10.679  4.819   1.00 29.67  ?  1325 HOH B O    1 
HETATM 11684 O  O    . HOH X 4 .   ? 12.027  13.255  -15.203 1.00 37.21  ?  1326 HOH B O    1 
HETATM 11685 O  O    . HOH X 4 .   ? -4.880  20.190  28.436  1.00 13.51  ?  1327 HOH B O    1 
HETATM 11686 O  O    . HOH X 4 .   ? -5.080  47.753  14.294  1.00 45.10  ?  1328 HOH B O    1 
HETATM 11687 O  O    B HOH X 4 .   ? -8.846  7.437   11.345  1.00 43.59  ?  1329 HOH B O    1 
HETATM 11688 O  O    . HOH X 4 .   ? -7.420  21.027  29.315  1.00 32.79  ?  1330 HOH B O    1 
HETATM 11689 O  O    . HOH X 4 .   ? 10.697  41.665  11.942  1.00 46.65  ?  1331 HOH B O    1 
HETATM 11690 O  O    . HOH X 4 .   ? 11.795  2.292   -12.268 1.00 43.29  ?  1332 HOH B O    1 
HETATM 11691 O  O    . HOH X 4 .   ? 9.333   24.829  43.787  1.00 50.61  ?  1333 HOH B O    1 
HETATM 11692 O  O    . HOH X 4 .   ? -8.071  21.768  -5.790  1.00 53.45  ?  1334 HOH B O    1 
HETATM 11693 O  O    A HOH X 4 .   ? 34.864  5.640   -0.673  1.00 44.12  ?  1335 HOH B O    1 
HETATM 11694 O  O    A HOH X 4 .   ? -6.773  22.506  1.001   1.00 32.47  ?  1336 HOH B O    1 
HETATM 11695 O  O    . HOH X 4 .   ? 14.320  26.625  31.381  1.00 59.72  ?  1337 HOH B O    1 
HETATM 11696 O  O    . HOH X 4 .   ? 34.861  16.648  -0.055  1.00 22.12  ?  1338 HOH B O    1 
HETATM 11697 O  O    . HOH X 4 .   ? 12.498  16.507  -15.879 1.00 33.37  ?  1339 HOH B O    1 
HETATM 11698 O  O    . HOH X 4 .   ? 13.445  30.311  24.452  1.00 44.55  ?  1340 HOH B O    1 
HETATM 11699 O  O    . HOH X 4 .   ? -16.274 33.493  24.017  1.00 64.94  ?  1341 HOH B O    1 
HETATM 11700 O  O    A HOH X 4 .   ? 2.812   11.245  18.946  0.70 10.84  ?  1342 HOH B O    1 
HETATM 11701 O  O    . HOH X 4 .   ? -20.547 29.408  14.603  1.00 31.33  ?  1343 HOH B O    1 
HETATM 11702 O  O    B HOH X 4 .   ? 19.185  26.109  -12.884 1.00 41.29  ?  1344 HOH B O    1 
HETATM 11703 O  O    . HOH X 4 .   ? 16.209  26.001  25.776  1.00 55.39  ?  1345 HOH B O    1 
HETATM 11704 O  O    . HOH X 4 .   ? 11.692  35.622  4.092   1.00 31.06  ?  1346 HOH B O    1 
HETATM 11705 O  O    B HOH X 4 .   ? 14.645  35.423  4.032   0.66 25.50  ?  1347 HOH B O    1 
HETATM 11706 O  O    B HOH X 4 .   ? -7.763  23.036  2.894   1.00 39.40  ?  1348 HOH B O    1 
HETATM 11707 O  O    . HOH X 4 .   ? 4.663   19.377  33.822  1.00 33.51  ?  1349 HOH B O    1 
HETATM 11708 O  O    . HOH X 4 .   ? 15.505  35.333  24.518  1.00 42.35  ?  1350 HOH B O    1 
HETATM 11709 O  O    . HOH X 4 .   ? 14.978  34.775  22.209  1.00 27.72  ?  1351 HOH B O    1 
HETATM 11710 O  O    C HOH X 4 .   ? 16.531  17.052  29.145  0.69 19.78  ?  1352 HOH B O    1 
HETATM 11711 O  O    . HOH X 4 .   ? 13.598  27.928  -17.227 1.00 34.59  ?  1353 HOH B O    1 
HETATM 11712 O  O    . HOH X 4 .   ? 14.004  -3.312  -3.342  1.00 43.06  ?  1354 HOH B O    1 
HETATM 11713 O  O    . HOH X 4 .   ? 17.055  36.304  12.140  1.00 45.05  ?  1355 HOH B O    1 
HETATM 11714 O  O    . HOH X 4 .   ? -8.868  13.393  -0.032  1.00 49.50  ?  1356 HOH B O    1 
HETATM 11715 O  O    . HOH X 4 .   ? 6.138   45.803  22.392  1.00 51.09  ?  1357 HOH B O    1 
HETATM 11716 O  O    . HOH X 4 .   ? 4.267   45.443  23.918  1.00 36.33  ?  1358 HOH B O    1 
HETATM 11717 O  O    . HOH X 4 .   ? -11.133 8.367   23.262  1.00 43.89  ?  1359 HOH B O    1 
HETATM 11718 O  O    . HOH X 4 .   ? 4.153   12.965  -14.966 1.00 34.21  ?  1360 HOH B O    1 
HETATM 11719 O  O    . HOH X 4 .   ? 13.959  26.248  -18.850 1.00 40.98  ?  1361 HOH B O    1 
HETATM 11720 O  O    . HOH X 4 .   ? 16.409  24.075  -16.615 1.00 40.25  ?  1362 HOH B O    1 
HETATM 11721 O  O    . HOH X 4 .   ? 5.221   15.418  -17.361 1.00 34.30  ?  1363 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 
11    N N   . LYS A 2   ? 0.2098 0.2266 0.2631 0.0517  0.0189  -0.0240 225 LYS A N   
12    C CA  . LYS A 2   ? 0.1780 0.2092 0.2640 0.0415  0.0282  -0.0074 225 LYS A CA  
13    C C   . LYS A 2   ? 0.1359 0.1890 0.2195 0.0397  0.0339  0.0170  225 LYS A C   
14    O O   . LYS A 2   ? 0.1517 0.1873 0.1966 0.0279  0.0488  0.0280  225 LYS A O   
15    C CB  . LYS A 2   ? 0.1815 0.2084 0.3079 0.0405  0.0165  -0.0091 225 LYS A CB  
16    C CG  . LYS A 2   ? 0.1821 0.2224 0.3410 0.0361  0.0093  -0.0077 225 LYS A CG  
17    C CD  . LYS A 2   ? 0.1800 0.2332 0.3664 0.0412  0.0051  -0.0117 225 LYS A CD  
18    C CE  . LYS A 2   ? 0.1873 0.2408 0.3853 0.0556  0.0318  -0.0067 225 LYS A CE  
19    N NZ  . LYS A 2   ? 0.1723 0.2214 0.3893 0.0854  0.0562  0.0091  225 LYS A NZ  
33    N N   . PRO A 3   ? 0.1273 0.1859 0.2167 0.0515  0.0438  0.0291  226 PRO A N   
34    C CA  . PRO A 3   ? 0.1305 0.1747 0.2112 0.0376  0.0322  0.0204  226 PRO A CA  
35    C C   . PRO A 3   ? 0.1364 0.1428 0.1736 0.0194  0.0561  0.0226  226 PRO A C   
36    O O   . PRO A 3   ? 0.1376 0.1335 0.1941 0.0208  0.0410  0.0296  226 PRO A O   
37    C CB  . PRO A 3   ? 0.1580 0.2113 0.2448 0.0271  0.0395  0.0096  226 PRO A CB  
38    C CG  . PRO A 3   ? 0.1704 0.2241 0.2545 0.0343  0.0493  0.0107  226 PRO A CG  
39    C CD  . PRO A 3   ? 0.1647 0.2088 0.2413 0.0476  0.0467  0.0187  226 PRO A CD  
47    N N   . PHE A 4   ? 0.1225 0.1273 0.1436 0.0161  0.0428  0.0191  227 PHE A N   
48    C CA  . PHE A 4   ? 0.1057 0.1243 0.1467 0.0160  0.0149  0.0263  227 PHE A CA  
49    C C   . PHE A 4   ? 0.0932 0.1251 0.1495 0.0087  -0.0012 0.0185  227 PHE A C   
50    O O   . PHE A 4   ? 0.1059 0.1443 0.1644 -0.0102 0.0070  0.0258  227 PHE A O   
51    C CB  . PHE A 4   ? 0.1093 0.1280 0.1347 0.0125  0.0169  0.0253  227 PHE A CB  
52    C CG  . PHE A 4   ? 0.0913 0.1150 0.1328 0.0041  0.0012  0.0224  227 PHE A CG  
53    C CD1 . PHE A 4   ? 0.1087 0.1077 0.1511 0.0021  0.0073  0.0093  227 PHE A CD1 
54    C CD2 . PHE A 4   ? 0.0982 0.1151 0.1607 -0.0099 0.0075  0.0091  227 PHE A CD2 
55    C CE1 . PHE A 4   ? 0.0901 0.1023 0.1445 -0.0098 -0.0143 0.0108  227 PHE A CE1 
56    C CE2 . PHE A 4   ? 0.1019 0.1113 0.1624 0.0060  0.0032  0.0003  227 PHE A CE2 
57    C CZ  . PHE A 4   ? 0.1074 0.1109 0.1390 0.0008  -0.0073 0.0094  227 PHE A CZ  
67    N N   . THR A 5   ? 0.0965 0.1214 0.1181 -0.0063 0.0150  0.0049  228 THR A N   
68    C CA  . THR A 5   ? 0.0948 0.1104 0.1070 -0.0050 0.0100  0.0107  228 THR A CA  
69    C C   . THR A 5   ? 0.0762 0.0954 0.1019 -0.0051 -0.0079 0.0080  228 THR A C   
70    O O   . THR A 5   ? 0.0900 0.0966 0.1090 -0.0136 0.0004  -0.0006 228 THR A O   
71    C CB  . THR A 5   ? 0.0913 0.1216 0.1316 0.0086  -0.0017 0.0026  228 THR A CB  
72    O OG1 . THR A 5   ? 0.1019 0.1083 0.1433 0.0027  0.0096  0.0063  228 THR A OG1 
73    C CG2 . THR A 5   ? 0.0835 0.1404 0.1564 0.0025  -0.0154 0.0003  228 THR A CG2 
81    N N   . ILE A 6   ? 0.0819 0.1070 0.0971 -0.0034 -0.0007 0.0029  229 ILE A N   
82    C CA  . ILE A 6   ? 0.0775 0.1039 0.0993 -0.0132 -0.0025 0.0081  229 ILE A CA  
83    C C   . ILE A 6   ? 0.0739 0.0808 0.1047 -0.0075 -0.0069 0.0009  229 ILE A C   
84    O O   . ILE A 6   ? 0.0612 0.0804 0.1173 -0.0102 -0.0237 0.0165  229 ILE A O   
85    C CB  . ILE A 6   ? 0.1065 0.0954 0.1132 -0.0029 0.0010  0.0240  229 ILE A CB  
86    C CG1 . ILE A 6   ? 0.1285 0.0986 0.1288 -0.0044 0.0175  0.0283  229 ILE A CG1 
87    C CG2 . ILE A 6   ? 0.1324 0.0877 0.1277 -0.0028 0.0075  0.0100  229 ILE A CG2 
88    C CD1 . ILE A 6   ? 0.1463 0.1053 0.1365 0.0000  -0.0080 0.0306  229 ILE A CD1 
100   N N   . PRO A 7   ? 0.0565 0.0757 0.0999 0.0002  -0.0140 0.0076  230 PRO A N   
101   C CA  . PRO A 7   ? 0.0599 0.0761 0.0966 -0.0133 -0.0097 0.0070  230 PRO A CA  
102   C C   . PRO A 7   ? 0.0601 0.0742 0.1052 -0.0091 -0.0205 0.0119  230 PRO A C   
103   O O   . PRO A 7   ? 0.0807 0.0796 0.1067 -0.0081 -0.0206 0.0087  230 PRO A O   
104   C CB  . PRO A 7   ? 0.0732 0.0943 0.0949 -0.0002 -0.0206 0.0038  230 PRO A CB  
105   C CG  . PRO A 7   ? 0.0785 0.0954 0.0914 -0.0065 -0.0150 0.0004  230 PRO A CG  
106   C CD  . PRO A 7   ? 0.0811 0.0857 0.0986 0.0051  -0.0098 0.0136  230 PRO A CD  
114   N N   . ILE A 8   ? 0.0758 0.0688 0.1140 -0.0065 -0.0300 0.0099  231 ILE A N   
115   C CA  . ILE A 8   ? 0.0854 0.0866 0.1183 -0.0031 -0.0423 0.0148  231 ILE A CA  
116   C C   . ILE A 8   ? 0.0961 0.1070 0.1127 -0.0215 -0.0366 0.0120  231 ILE A C   
117   O O   . ILE A 8   ? 0.0941 0.1329 0.1290 -0.0280 -0.0386 -0.0120 231 ILE A O   
118   C CB  . ILE A 8   ? 0.1067 0.1095 0.1311 -0.0164 -0.0453 0.0101  231 ILE A CB  
119   C CG1 . ILE A 8   ? 0.1251 0.1188 0.1425 -0.0058 -0.0448 0.0220  231 ILE A CG1 
120   C CG2 . ILE A 8   ? 0.1134 0.1235 0.1537 -0.0032 -0.0258 0.0047  231 ILE A CG2 
121   C CD1 . ILE A 8   ? 0.1322 0.1407 0.1608 -0.0081 -0.0551 0.0167  231 ILE A CD1 
133   N N   . LEU A 9   ? 0.0836 0.0946 0.1103 -0.0278 -0.0278 0.0201  232 LEU A N   
134   C CA  . LEU A 9   ? 0.0774 0.0810 0.1099 -0.0203 -0.0277 0.0211  232 LEU A CA  
135   C C   . LEU A 9   ? 0.0876 0.0868 0.1040 -0.0230 -0.0374 0.0161  232 LEU A C   
136   O O   . LEU A 9   ? 0.0977 0.0884 0.1128 -0.0139 -0.0242 0.0241  232 LEU A O   
137   C CB  . LEU A 9   ? 0.0972 0.0775 0.0911 -0.0103 -0.0275 0.0163  232 LEU A CB  
138   C CG  . LEU A 9   ? 0.0839 0.0869 0.1262 -0.0183 -0.0259 0.0107  232 LEU A CG  
139   C CD1 . LEU A 9   ? 0.0898 0.0898 0.1674 -0.0152 -0.0383 -0.0002 232 LEU A CD1 
140   C CD2 . LEU A 9   ? 0.1185 0.1092 0.1364 -0.0183 -0.0210 0.0243  232 LEU A CD2 
152   N N   . THR A 10  ? 0.1045 0.0871 0.0946 -0.0164 -0.0377 0.0118  233 THR A N   
153   C CA  . THR A 10  ? 0.1417 0.0965 0.1113 -0.0099 -0.0218 0.0000  233 THR A CA  
154   C C   . THR A 10  ? 0.1426 0.1025 0.1249 -0.0027 -0.0031 0.0040  233 THR A C   
155   O O   . THR A 10  ? 0.1200 0.0980 0.1091 -0.0006 -0.0117 0.0021  233 THR A O   
156   C CB  . THR A 10  ? 0.1637 0.1055 0.1181 -0.0248 -0.0373 -0.0086 233 THR A CB  
157   O OG1 . THR A 10  ? 0.1899 0.1202 0.0971 -0.0278 -0.0130 0.0030  233 THR A OG1 
158   C CG2 . THR A 10  ? 0.1723 0.1120 0.1359 -0.0180 -0.0303 0.0018  233 THR A CG2 
166   N N   . ILE A 11  ? 0.1524 0.1176 0.1522 0.0079  -0.0075 -0.0030 234 ILE A N   
167   C CA  . ILE A 11  ? 0.1870 0.1642 0.2099 0.0217  0.0094  -0.0153 234 ILE A CA  
168   C C   . ILE A 11  ? 0.1668 0.1759 0.2045 0.0042  0.0044  -0.0539 234 ILE A C   
169   O O   . ILE A 11  ? 0.1578 0.1848 0.2204 0.0176  0.0320  -0.0761 234 ILE A O   
170   C CB  . ILE A 11  ? 0.2309 0.2149 0.2671 0.0284  0.0267  -0.0099 234 ILE A CB  
171   C CG1 . ILE A 11  ? 0.2525 0.2347 0.2652 0.0343  0.0024  0.0032  234 ILE A CG1 
172   C CG2 . ILE A 11  ? 0.2772 0.2376 0.2989 0.0464  0.0537  -0.0187 234 ILE A CG2 
173   C CD1 . ILE A 11  ? 0.2522 0.2440 0.2447 0.0199  -0.0322 -0.0192 234 ILE A CD1 
185   N N   . GLY A 12  ? 0.1844 0.1958 0.1817 -0.0323 0.0305  -0.0634 235 GLY A N   
186   C CA  . GLY A 12  ? 0.1979 0.2192 0.1726 -0.0582 0.0515  -0.0441 235 GLY A CA  
187   C C   . GLY A 12  ? 0.1771 0.2161 0.1526 -0.0601 0.0129  -0.0064 235 GLY A C   
188   O O   . GLY A 12  ? 0.2286 0.2676 0.1499 -0.0585 0.0081  0.0035  235 GLY A O   
192   N N   . GLU A 13  ? 0.1310 0.1642 0.1170 -0.0212 -0.0343 0.0060  236 GLU A N   
193   C CA  . GLU A 13  ? 0.1309 0.1305 0.1033 -0.0331 -0.0181 0.0323  236 GLU A CA  
194   C C   . GLU A 13  ? 0.1094 0.1146 0.0992 -0.0143 -0.0413 0.0257  236 GLU A C   
195   O O   . GLU A 13  ? 0.1414 0.0930 0.1293 -0.0060 -0.0477 0.0211  236 GLU A O   
196   C CB  . GLU A 13  ? 0.1276 0.1233 0.0991 -0.0328 -0.0336 0.0400  236 GLU A CB  
197   C CG  . GLU A 13  ? 0.1313 0.1260 0.0993 -0.0264 -0.0468 0.0396  236 GLU A CG  
198   C CD  . GLU A 13  ? 0.1332 0.1337 0.1040 -0.0382 -0.0640 0.0226  236 GLU A CD  
199   O OE1 . GLU A 13  ? 0.1358 0.1289 0.1156 -0.0293 -0.0493 0.0374  236 GLU A OE1 
200   O OE2 . GLU A 13  ? 0.1419 0.1544 0.1239 -0.0311 -0.0569 0.0215  236 GLU A OE2 
207   N N   . MET A 14  ? 0.0933 0.1152 0.0806 -0.0052 -0.0100 0.0173  237 MET A N   
208   C CA  . MET A 14  ? 0.0768 0.1061 0.0904 0.0018  -0.0036 0.0101  237 MET A CA  
209   C C   . MET A 14  ? 0.0857 0.1119 0.0993 -0.0015 0.0023  -0.0078 237 MET A C   
210   O O   . MET A 14  ? 0.0744 0.1396 0.1237 -0.0084 -0.0056 -0.0243 237 MET A O   
211   C CB  . MET A 14  ? 0.0594 0.1016 0.0894 0.0013  -0.0024 0.0190  237 MET A CB  
212   C CG  . MET A 14  ? 0.0585 0.1063 0.0949 -0.0079 -0.0003 0.0223  237 MET A CG  
213   S SD  . MET A 14  ? 0.0744 0.1056 0.1019 -0.0097 -0.0168 0.0228  237 MET A SD  
214   C CE  . MET A 14  ? 0.0609 0.1189 0.1137 -0.0158 -0.0354 0.0189  237 MET A CE  
224   N N   . THR A 15  ? 0.0765 0.1011 0.0867 0.0156  -0.0041 0.0162  238 THR A N   
225   C CA  A THR A 15  ? 0.0683 0.0902 0.1002 0.0113  0.0099  0.0156  238 THR A CA  
226   C CA  B THR A 15  ? 0.0803 0.0951 0.0946 0.0090  0.0014  0.0126  238 THR A CA  
227   C C   . THR A 15  ? 0.0606 0.0832 0.0834 0.0004  0.0076  0.0089  238 THR A C   
228   O O   . THR A 15  ? 0.0795 0.0874 0.0989 0.0060  0.0004  0.0112  238 THR A O   
229   C CB  A THR A 15  ? 0.0529 0.0866 0.1312 0.0164  0.0197  0.0280  238 THR A CB  
230   C CB  B THR A 15  ? 0.0770 0.0988 0.1074 0.0118  -0.0048 0.0077  238 THR A CB  
231   O OG1 A THR A 15  ? 0.0547 0.0954 0.1395 0.0232  0.0269  0.0384  238 THR A OG1 
232   O OG1 B THR A 15  ? 0.0874 0.1037 0.1229 -0.0073 -0.0154 -0.0134 238 THR A OG1 
233   C CG2 A THR A 15  ? 0.0657 0.0859 0.1423 0.0033  0.0335  0.0190  238 THR A CG2 
234   C CG2 B THR A 15  ? 0.0732 0.1047 0.1188 0.0113  0.0067  0.0027  238 THR A CG2 
249   N N   . ASN A 16  ? 0.0509 0.0758 0.0773 -0.0030 -0.0090 0.0031  239 ASN A N   
250   C CA  . ASN A 16  ? 0.0573 0.0655 0.0672 -0.0068 -0.0053 0.0056  239 ASN A CA  
251   C C   . ASN A 16  ? 0.0462 0.0775 0.0814 -0.0112 -0.0133 0.0087  239 ASN A C   
252   O O   . ASN A 16  ? 0.0847 0.0914 0.0919 -0.0202 -0.0022 0.0049  239 ASN A O   
253   C CB  . ASN A 16  ? 0.0620 0.0702 0.0707 -0.0090 -0.0072 -0.0061 239 ASN A CB  
254   C CG  . ASN A 16  ? 0.0541 0.0686 0.0897 -0.0027 -0.0068 0.0016  239 ASN A CG  
255   O OD1 . ASN A 16  ? 0.0671 0.0788 0.0846 0.0120  -0.0192 -0.0061 239 ASN A OD1 
256   N ND2 . ASN A 16  ? 0.0749 0.0675 0.1078 0.0085  -0.0117 -0.0014 239 ASN A ND2 
263   N N   . SER A 17  ? 0.0673 0.0701 0.0712 -0.0006 -0.0104 -0.0033 240 SER A N   
264   C CA  . SER A 17  ? 0.0580 0.0743 0.0681 0.0010  -0.0088 -0.0040 240 SER A CA  
265   C C   . SER A 17  ? 0.0614 0.0682 0.0708 0.0105  -0.0110 0.0024  240 SER A C   
266   O O   . SER A 17  ? 0.0674 0.0779 0.0826 -0.0034 -0.0282 -0.0113 240 SER A O   
267   C CB  . SER A 17  ? 0.0671 0.0800 0.0651 0.0007  -0.0156 -0.0020 240 SER A CB  
268   O OG  . SER A 17  ? 0.0620 0.0770 0.0767 -0.0033 0.0045  0.0039  240 SER A OG  
274   N N   . ARG A 18  ? 0.0510 0.0606 0.0766 0.0119  -0.0131 0.0009  241 ARG A N   
275   C CA  . ARG A 18  ? 0.0564 0.0636 0.0729 0.0017  -0.0195 -0.0010 241 ARG A CA  
276   C C   . ARG A 18  ? 0.0629 0.0621 0.0803 0.0014  -0.0197 -0.0026 241 ARG A C   
277   O O   . ARG A 18  ? 0.0580 0.0678 0.0863 0.0024  -0.0193 0.0129  241 ARG A O   
278   C CB  . ARG A 18  ? 0.0516 0.0585 0.0792 0.0086  -0.0151 0.0161  241 ARG A CB  
279   C CG  . ARG A 18  ? 0.0651 0.0572 0.0827 -0.0047 -0.0114 0.0160  241 ARG A CG  
280   C CD  . ARG A 18  ? 0.0514 0.0664 0.0773 -0.0019 -0.0194 0.0075  241 ARG A CD  
281   N NE  . ARG A 18  ? 0.0428 0.0659 0.0910 0.0034  -0.0204 -0.0010 241 ARG A NE  
282   C CZ  . ARG A 18  ? 0.0531 0.0682 0.0928 0.0040  -0.0226 0.0051  241 ARG A CZ  
283   N NH1 . ARG A 18  ? 0.0541 0.0710 0.1161 -0.0021 -0.0082 -0.0107 241 ARG A NH1 
284   N NH2 . ARG A 18  ? 0.0590 0.0763 0.1058 0.0019  -0.0100 -0.0069 241 ARG A NH2 
298   N N   . PHE A 19  ? 0.0600 0.0672 0.0834 -0.0063 -0.0159 0.0050  242 PHE A N   
299   C CA  . PHE A 19  ? 0.0623 0.0667 0.0879 -0.0116 -0.0063 0.0116  242 PHE A CA  
300   C C   . PHE A 19  ? 0.0771 0.0699 0.0835 -0.0264 0.0032  0.0049  242 PHE A C   
301   O O   . PHE A 19  ? 0.0740 0.0838 0.0888 -0.0185 -0.0005 0.0143  242 PHE A O   
302   C CB  . PHE A 19  ? 0.0688 0.0676 0.0962 -0.0127 -0.0051 0.0072  242 PHE A CB  
303   C CG  . PHE A 19  ? 0.0769 0.0825 0.0842 -0.0065 -0.0043 -0.0048 242 PHE A CG  
304   C CD1 . PHE A 19  ? 0.0853 0.1036 0.1097 -0.0042 -0.0102 -0.0114 242 PHE A CD1 
305   C CD2 . PHE A 19  ? 0.0958 0.0990 0.1046 0.0174  0.0358  0.0084  242 PHE A CD2 
306   C CE1 . PHE A 19  ? 0.0938 0.1197 0.1382 -0.0137 -0.0010 -0.0385 242 PHE A CE1 
307   C CE2 . PHE A 19  ? 0.1266 0.1113 0.1399 -0.0044 0.0546  -0.0178 242 PHE A CE2 
308   C CZ  . PHE A 19  ? 0.1134 0.1087 0.1499 -0.0238 0.0496  -0.0431 242 PHE A CZ  
318   N N   . PRO A 20  ? 0.0714 0.0808 0.0973 -0.0156 -0.0249 0.0141  243 PRO A N   
319   C CA  . PRO A 20  ? 0.0847 0.0856 0.1167 -0.0077 -0.0271 0.0151  243 PRO A CA  
320   C C   . PRO A 20  ? 0.0865 0.0886 0.0993 -0.0126 -0.0178 0.0250  243 PRO A C   
321   O O   . PRO A 20  ? 0.1019 0.1127 0.1196 -0.0375 -0.0256 0.0405  243 PRO A O   
322   C CB  . PRO A 20  ? 0.0886 0.0765 0.1431 -0.0176 -0.0269 0.0238  243 PRO A CB  
323   C CG  . PRO A 20  ? 0.0871 0.0828 0.1429 -0.0119 -0.0392 0.0223  243 PRO A CG  
324   C CD  . PRO A 20  ? 0.0637 0.0758 0.1146 -0.0176 -0.0205 0.0201  243 PRO A CD  
332   N N   . VAL A 21  ? 0.0735 0.0899 0.0924 -0.0198 -0.0084 0.0174  244 VAL A N   
333   C CA  . VAL A 21  ? 0.0743 0.0805 0.0972 -0.0001 -0.0089 0.0209  244 VAL A CA  
334   C C   . VAL A 21  ? 0.0746 0.0748 0.0903 -0.0015 -0.0125 0.0136  244 VAL A C   
335   O O   . VAL A 21  ? 0.0740 0.0811 0.0755 -0.0095 -0.0188 0.0117  244 VAL A O   
336   C CB  . VAL A 21  ? 0.0816 0.0911 0.1240 -0.0038 0.0002  -0.0005 244 VAL A CB  
337   C CG1 . VAL A 21  ? 0.0967 0.1197 0.1328 -0.0034 -0.0042 0.0073  244 VAL A CG1 
338   C CG2 . VAL A 21  ? 0.0909 0.0842 0.1226 0.0044  -0.0120 0.0004  244 VAL A CG2 
348   N N   . PRO A 22  ? 0.0939 0.0782 0.0911 -0.0104 -0.0139 0.0153  245 PRO A N   
349   C CA  . PRO A 22  ? 0.0907 0.0782 0.0867 0.0015  -0.0205 0.0111  245 PRO A CA  
350   C C   . PRO A 22  ? 0.0806 0.0754 0.0928 -0.0058 -0.0075 0.0126  245 PRO A C   
351   O O   . PRO A 22  ? 0.0793 0.0728 0.1041 0.0082  -0.0130 -0.0052 245 PRO A O   
352   C CB  . PRO A 22  ? 0.1132 0.0886 0.0956 -0.0085 -0.0196 0.0089  245 PRO A CB  
353   C CG  . PRO A 22  ? 0.1236 0.0897 0.1051 -0.0179 -0.0195 0.0168  245 PRO A CG  
354   C CD  . PRO A 22  ? 0.1090 0.0879 0.0967 -0.0197 -0.0095 0.0153  245 PRO A CD  
362   N N   . ILE A 23  ? 0.0808 0.0789 0.1190 0.0091  -0.0178 0.0334  246 ILE A N   
363   C CA  . ILE A 23  ? 0.0772 0.0808 0.1140 0.0057  -0.0219 0.0268  246 ILE A CA  
364   C C   . ILE A 23  ? 0.0924 0.1028 0.1024 0.0135  -0.0138 0.0248  246 ILE A C   
365   O O   . ILE A 23  ? 0.1278 0.1265 0.1056 0.0406  -0.0272 0.0188  246 ILE A O   
366   C CB  . ILE A 23  ? 0.1016 0.0924 0.1083 -0.0133 -0.0087 -0.0057 246 ILE A CB  
367   C CG1 . ILE A 23  ? 0.1583 0.1036 0.1556 -0.0338 0.0269  -0.0142 246 ILE A CG1 
368   C CG2 . ILE A 23  ? 0.1050 0.0807 0.1051 -0.0094 0.0046  -0.0107 246 ILE A CG2 
369   C CD1 . ILE A 23  ? 0.1719 0.1162 0.1655 -0.0119 0.0269  0.0100  246 ILE A CD1 
381   N N   . ASP A 24  ? 0.0776 0.0917 0.0820 -0.0049 -0.0250 0.0168  247 ASP A N   
382   C CA  . ASP A 24  ? 0.0746 0.1024 0.0959 -0.0178 -0.0288 0.0137  247 ASP A CA  
383   C C   . ASP A 24  ? 0.0907 0.1101 0.0974 -0.0071 -0.0167 0.0137  247 ASP A C   
384   O O   . ASP A 24  ? 0.1139 0.1387 0.1089 -0.0254 -0.0176 0.0119  247 ASP A O   
385   C CB  . ASP A 24  ? 0.0869 0.1274 0.1095 -0.0127 -0.0208 0.0101  247 ASP A CB  
386   C CG  . ASP A 24  ? 0.0878 0.1653 0.1324 -0.0101 -0.0221 0.0472  247 ASP A CG  
387   O OD1 . ASP A 24  ? 0.1202 0.2525 0.1915 -0.0450 -0.0503 0.0949  247 ASP A OD1 
388   O OD2 . ASP A 24  ? 0.0838 0.1292 0.1264 -0.0105 -0.0176 0.0325  247 ASP A OD2 
393   N N   . MET A 25  ? 0.0902 0.0891 0.0956 -0.0105 -0.0185 0.0024  248 MET A N   
394   C CA  . MET A 25  ? 0.1043 0.0776 0.0996 -0.0122 -0.0203 0.0079  248 MET A CA  
395   C C   . MET A 25  ? 0.0942 0.0762 0.0975 -0.0199 -0.0357 0.0017  248 MET A C   
396   O O   . MET A 25  ? 0.1057 0.0884 0.1020 -0.0335 -0.0188 0.0108  248 MET A O   
397   C CB  . MET A 25  ? 0.1503 0.1008 0.1017 0.0053  -0.0046 -0.0110 248 MET A CB  
398   C CG  . MET A 25  ? 0.1946 0.1403 0.1596 0.0431  -0.0279 -0.0370 248 MET A CG  
399   S SD  . MET A 25  ? 0.2458 0.2307 0.2465 0.0542  -0.0310 -0.0666 248 MET A SD  
400   C CE  . MET A 25  ? 0.2750 0.2431 0.2833 0.0233  0.0006  -0.0548 248 MET A CE  
410   N N   . LEU A 26  ? 0.1060 0.0859 0.0885 -0.0263 -0.0360 0.0007  249 LEU A N   
411   C CA  . LEU A 26  ? 0.1059 0.0862 0.0938 -0.0204 -0.0239 -0.0002 249 LEU A CA  
412   C C   . LEU A 26  ? 0.1156 0.0825 0.0872 -0.0111 -0.0251 -0.0048 249 LEU A C   
413   O O   . LEU A 26  ? 0.1664 0.0867 0.0979 0.0010  0.0003  -0.0054 249 LEU A O   
414   C CB  . LEU A 26  ? 0.1034 0.0904 0.1128 -0.0302 -0.0226 0.0013  249 LEU A CB  
415   C CG  . LEU A 26  ? 0.1012 0.1123 0.1340 -0.0282 -0.0160 0.0083  249 LEU A CG  
416   C CD1 . LEU A 26  ? 0.0872 0.1382 0.1411 -0.0279 -0.0213 -0.0024 249 LEU A CD1 
417   C CD2 . LEU A 26  ? 0.1199 0.1129 0.1819 -0.0074 -0.0229 -0.0198 249 LEU A CD2 
429   N N   . HIS A 27  ? 0.0952 0.0730 0.0913 -0.0025 -0.0194 -0.0066 250 HIS A N   
430   C CA  . HIS A 27  ? 0.1031 0.0758 0.1140 0.0037  -0.0123 0.0094  250 HIS A CA  
431   C C   . HIS A 27  ? 0.0837 0.0642 0.1167 -0.0018 -0.0250 -0.0015 250 HIS A C   
432   O O   . HIS A 27  ? 0.1030 0.0715 0.1044 -0.0129 -0.0117 -0.0026 250 HIS A O   
433   C CB  . HIS A 27  ? 0.1146 0.1060 0.1340 -0.0039 0.0009  0.0089  250 HIS A CB  
434   C CG  . HIS A 27  ? 0.1326 0.1285 0.1511 -0.0143 -0.0175 -0.0027 250 HIS A CG  
435   N ND1 . HIS A 27  ? 0.1293 0.1296 0.1529 -0.0112 -0.0242 -0.0155 250 HIS A ND1 
436   C CD2 . HIS A 27  ? 0.1235 0.1255 0.1652 -0.0023 -0.0157 -0.0190 250 HIS A CD2 
437   C CE1 . HIS A 27  ? 0.1318 0.1209 0.1576 0.0004  -0.0142 -0.0001 250 HIS A CE1 
438   N NE2 . HIS A 27  ? 0.1357 0.1284 0.1690 0.0050  -0.0232 -0.0124 250 HIS A NE2 
446   N N   . THR A 28  ? 0.1008 0.0693 0.0988 -0.0108 -0.0195 -0.0098 251 THR A N   
447   C CA  . THR A 28  ? 0.1038 0.0740 0.1037 -0.0091 -0.0134 -0.0149 251 THR A CA  
448   C C   . THR A 28  ? 0.1221 0.0824 0.1117 -0.0051 -0.0272 -0.0087 251 THR A C   
449   O O   . THR A 28  ? 0.1492 0.1008 0.1239 0.0178  -0.0273 -0.0252 251 THR A O   
450   C CB  . THR A 28  ? 0.1027 0.0851 0.1069 0.0062  0.0021  0.0022  251 THR A CB  
451   O OG1 . THR A 28  ? 0.1252 0.0772 0.1079 0.0030  -0.0107 0.0026  251 THR A OG1 
452   C CG2 . THR A 28  ? 0.0905 0.0991 0.1267 -0.0082 0.0061  0.0014  251 THR A CG2 
460   N N   . SER A 29  ? 0.1284 0.0898 0.1189 0.0088  -0.0272 -0.0008 252 SER A N   
461   C CA  . SER A 29  ? 0.1310 0.1203 0.1462 0.0238  -0.0206 0.0011  252 SER A CA  
462   C C   . SER A 29  ? 0.1442 0.1366 0.1449 0.0246  -0.0380 0.0095  252 SER A C   
463   O O   . SER A 29  ? 0.1275 0.1494 0.1388 0.0140  -0.0448 0.0144  252 SER A O   
464   C CB  . SER A 29  ? 0.1417 0.1290 0.1718 0.0237  -0.0023 0.0002  252 SER A CB  
465   O OG  . SER A 29  ? 0.1402 0.1567 0.1978 -0.0019 -0.0195 -0.0047 252 SER A OG  
471   N N   . PRO A 30  ? 0.1697 0.1512 0.1605 0.0277  -0.0505 0.0251  253 PRO A N   
472   C CA  . PRO A 30  ? 0.1767 0.1495 0.1845 0.0216  -0.0505 0.0291  253 PRO A CA  
473   C C   . PRO A 30  ? 0.1635 0.1464 0.1988 0.0190  -0.0641 0.0347  253 PRO A C   
474   O O   . PRO A 30  ? 0.2030 0.1737 0.2214 -0.0096 -0.0183 0.0141  253 PRO A O   
475   C CB  . PRO A 30  ? 0.1849 0.1516 0.2203 0.0245  -0.0426 0.0414  253 PRO A CB  
476   C CG  . PRO A 30  ? 0.1858 0.1544 0.2291 0.0258  -0.0242 0.0351  253 PRO A CG  
477   C CD  . PRO A 30  ? 0.1731 0.1599 0.1941 0.0217  -0.0345 0.0287  253 PRO A CD  
485   N N   . THR A 31  ? 0.1625 0.1426 0.2227 0.0145  -0.0656 0.0287  254 THR A N   
486   C CA  . THR A 31  ? 0.1750 0.1538 0.2242 0.0033  -0.0712 0.0259  254 THR A CA  
487   C C   . THR A 31  ? 0.2021 0.1804 0.2321 0.0021  -0.0652 0.0170  254 THR A C   
488   O O   . THR A 31  ? 0.1937 0.1807 0.2364 0.0127  -0.0557 0.0230  254 THR A O   
489   C CB  . THR A 31  ? 0.1765 0.1556 0.2435 -0.0030 -0.0581 0.0282  254 THR A CB  
490   O OG1 . THR A 31  ? 0.1896 0.1825 0.2433 0.0109  -0.0593 0.0061  254 THR A OG1 
491   C CG2 . THR A 31  ? 0.1965 0.1579 0.2694 -0.0062 -0.0445 0.0286  254 THR A CG2 
499   N N   . GLU A 32  ? 0.2364 0.1817 0.2344 0.0180  -0.0860 0.0270  255 GLU A N   
500   C CA  . GLU A 32  ? 0.2712 0.2122 0.2600 0.0239  -0.1077 0.0148  255 GLU A CA  
501   C C   . GLU A 32  ? 0.3002 0.1809 0.2761 0.0387  -0.1276 0.0117  255 GLU A C   
502   O O   . GLU A 32  ? 0.3317 0.1970 0.2880 0.0353  -0.1399 0.0167  255 GLU A O   
514   N N   . ASN A 33  ? 0.2838 0.1553 0.2745 0.0577  -0.1404 -0.0048 256 ASN A N   
515   C CA  . ASN A 33  ? 0.2990 0.1707 0.3132 0.0693  -0.1199 -0.0181 256 ASN A CA  
516   C C   . ASN A 33  ? 0.2660 0.1769 0.3018 0.0868  -0.1109 -0.0310 256 ASN A C   
517   O O   . ASN A 33  ? 0.2752 0.1924 0.3277 0.0919  -0.0753 -0.0352 256 ASN A O   
518   C CB  . ASN A 33  ? 0.3447 0.1939 0.3521 0.0548  -0.0746 -0.0307 256 ASN A CB  
519   C CG  . ASN A 33  ? 0.3850 0.2241 0.3871 0.0362  -0.0378 -0.0309 256 ASN A CG  
520   O OD1 . ASN A 33  ? 0.4066 0.2335 0.4041 0.0350  -0.0198 -0.0224 256 ASN A OD1 
521   N ND2 . ASN A 33  ? 0.4026 0.2370 0.4146 0.0365  -0.0172 -0.0299 256 ASN A ND2 
528   N N   . ILE A 34  ? 0.2437 0.1697 0.2624 0.0844  -0.1117 -0.0410 257 ILE A N   
529   C CA  . ILE A 34  ? 0.2497 0.1906 0.2580 0.0750  -0.0633 -0.0353 257 ILE A CA  
530   C C   . ILE A 34  ? 0.2025 0.1689 0.2260 0.0564  -0.0685 -0.0371 257 ILE A C   
531   O O   . ILE A 34  ? 0.2632 0.1804 0.2669 -0.0013 -0.0012 -0.0698 257 ILE A O   
532   C CB  . ILE A 34  ? 0.3053 0.2327 0.2870 0.0758  -0.0005 -0.0427 257 ILE A CB  
533   C CG1 . ILE A 34  ? 0.3047 0.2420 0.2721 0.0577  -0.0164 -0.0358 257 ILE A CG1 
534   C CG2 . ILE A 34  ? 0.3397 0.2559 0.3011 0.0784  0.0351  -0.0525 257 ILE A CG2 
535   C CD1 . ILE A 34  ? 0.3044 0.2397 0.2774 0.0461  -0.0108 -0.0214 257 ILE A CD1 
547   N N   . VAL A 35  ? 0.1720 0.1657 0.2204 0.0682  -0.0530 -0.0180 258 VAL A N   
548   C CA  . VAL A 35  ? 0.1583 0.1461 0.1681 0.0584  -0.0554 0.0079  258 VAL A CA  
549   C C   . VAL A 35  ? 0.1231 0.1282 0.1638 0.0178  -0.0509 0.0194  258 VAL A C   
550   O O   . VAL A 35  ? 0.1154 0.1586 0.1995 0.0025  -0.0241 0.0376  258 VAL A O   
551   C CB  . VAL A 35  ? 0.1962 0.1716 0.1736 0.0643  -0.0689 0.0143  258 VAL A CB  
552   C CG1 . VAL A 35  ? 0.1971 0.1745 0.1804 0.0433  -0.0750 -0.0027 258 VAL A CG1 
553   C CG2 . VAL A 35  ? 0.2367 0.2023 0.2166 0.0773  -0.0423 0.0292  258 VAL A CG2 
563   N N   . VAL A 36  ? 0.1021 0.0949 0.1142 0.0012  -0.0598 0.0145  259 VAL A N   
564   C CA  . VAL A 36  ? 0.0945 0.0814 0.1101 0.0006  -0.0437 0.0211  259 VAL A CA  
565   C C   . VAL A 36  ? 0.0797 0.0799 0.1041 -0.0044 -0.0332 0.0062  259 VAL A C   
566   O O   . VAL A 36  ? 0.0892 0.0941 0.1320 -0.0153 -0.0117 0.0015  259 VAL A O   
567   C CB  . VAL A 36  ? 0.1084 0.0904 0.1236 -0.0096 -0.0398 0.0052  259 VAL A CB  
568   C CG1 . VAL A 36  ? 0.1167 0.0986 0.1279 0.0029  -0.0489 0.0293  259 VAL A CG1 
569   C CG2 . VAL A 36  ? 0.1260 0.1103 0.1642 -0.0305 -0.0218 -0.0141 259 VAL A CG2 
579   N N   . GLN A 37  ? 0.0780 0.0774 0.0891 -0.0100 -0.0154 0.0054  260 GLN A N   
580   C CA  . GLN A 37  ? 0.0848 0.0895 0.0850 -0.0036 -0.0259 0.0172  260 GLN A CA  
581   C C   . GLN A 37  ? 0.0593 0.0786 0.0715 0.0004  -0.0239 0.0141  260 GLN A C   
582   O O   . GLN A 37  ? 0.0656 0.0889 0.0820 0.0043  -0.0202 0.0035  260 GLN A O   
583   C CB  . GLN A 37  ? 0.1021 0.1072 0.0820 -0.0021 -0.0342 0.0117  260 GLN A CB  
584   C CG  . GLN A 37  ? 0.1069 0.1187 0.1144 0.0170  -0.0280 0.0097  260 GLN A CG  
585   C CD  . GLN A 37  ? 0.1374 0.1385 0.1275 0.0192  -0.0231 0.0001  260 GLN A CD  
586   O OE1 . GLN A 37  ? 0.1918 0.1644 0.1296 0.0551  -0.0421 0.0114  260 GLN A OE1 
587   N NE2 . GLN A 37  ? 0.1486 0.1379 0.1116 0.0004  -0.0144 0.0030  260 GLN A NE2 
596   N N   . PRO A 38  ? 0.0608 0.0617 0.0826 -0.0070 -0.0212 0.0026  261 PRO A N   
597   C CA  . PRO A 38  ? 0.0624 0.0640 0.0955 -0.0019 -0.0122 0.0051  261 PRO A CA  
598   C C   . PRO A 38  ? 0.0535 0.0750 0.0861 -0.0097 -0.0280 0.0137  261 PRO A C   
599   O O   . PRO A 38  ? 0.0680 0.0820 0.0791 -0.0087 -0.0139 0.0127  261 PRO A O   
600   C CB  . PRO A 38  ? 0.0709 0.0681 0.0945 -0.0079 -0.0216 0.0102  261 PRO A CB  
601   C CG  . PRO A 38  ? 0.0717 0.0747 0.0860 -0.0054 -0.0208 0.0107  261 PRO A CG  
602   C CD  . PRO A 38  ? 0.0648 0.0783 0.0900 -0.0084 -0.0125 -0.0003 261 PRO A CD  
610   N N   . GLN A 39  ? 0.0684 0.0696 0.0837 -0.0137 -0.0164 0.0086  262 GLN A N   
611   C CA  . GLN A 39  ? 0.0667 0.0688 0.0833 -0.0078 -0.0194 0.0029  262 GLN A CA  
612   C C   . GLN A 39  ? 0.0671 0.0732 0.0845 0.0023  -0.0225 0.0020  262 GLN A C   
613   O O   . GLN A 39  ? 0.0745 0.0749 0.0883 0.0042  -0.0192 -0.0007 262 GLN A O   
614   C CB  . GLN A 39  ? 0.0567 0.0719 0.1107 0.0016  -0.0368 0.0066  262 GLN A CB  
615   C CG  . GLN A 39  ? 0.0699 0.0742 0.1054 0.0057  -0.0288 0.0073  262 GLN A CG  
616   C CD  . GLN A 39  ? 0.0773 0.0810 0.0884 0.0074  -0.0477 0.0011  262 GLN A CD  
617   O OE1 . GLN A 39  ? 0.0866 0.0874 0.1021 0.0089  -0.0393 -0.0114 262 GLN A OE1 
618   N NE2 . GLN A 39  ? 0.0794 0.0682 0.0916 -0.0054 -0.0246 0.0136  262 GLN A NE2 
627   N N   . ASN A 40  ? 0.0720 0.0669 0.0792 0.0084  -0.0099 0.0032  263 ASN A N   
628   C CA  . ASN A 40  ? 0.0689 0.0677 0.0914 0.0089  -0.0116 -0.0029 263 ASN A CA  
629   C C   . ASN A 40  ? 0.0679 0.0684 0.0843 -0.0012 -0.0213 0.0010  263 ASN A C   
630   O O   . ASN A 40  ? 0.0630 0.0712 0.0995 -0.0107 -0.0260 0.0039  263 ASN A O   
631   C CB  . ASN A 40  ? 0.0397 0.0676 0.1062 0.0022  -0.0203 0.0010  263 ASN A CB  
632   C CG  . ASN A 40  ? 0.0597 0.0758 0.0849 0.0014  -0.0285 0.0132  263 ASN A CG  
633   O OD1 . ASN A 40  ? 0.0667 0.0813 0.0942 0.0065  -0.0048 -0.0088 263 ASN A OD1 
634   N ND2 . ASN A 40  ? 0.0568 0.0866 0.1034 -0.0170 -0.0166 0.0031  263 ASN A ND2 
641   N N   . GLY A 41  ? 0.0645 0.0742 0.0810 -0.0057 -0.0132 0.0031  264 GLY A N   
642   C CA  . GLY A 41  ? 0.0702 0.0829 0.0975 -0.0024 -0.0153 -0.0032 264 GLY A CA  
643   C C   . GLY A 41  ? 0.0670 0.0750 0.0976 -0.0083 -0.0221 -0.0116 264 GLY A C   
644   O O   . GLY A 41  ? 0.0674 0.0920 0.0860 -0.0109 -0.0197 -0.0099 264 GLY A O   
648   N N   . ARG A 42  ? 0.0674 0.0760 0.0840 -0.0063 0.0031  -0.0068 265 ARG A N   
649   C CA  . ARG A 42  ? 0.0671 0.0770 0.0780 -0.0089 -0.0147 -0.0098 265 ARG A CA  
650   C C   . ARG A 42  ? 0.0774 0.0837 0.0809 -0.0118 -0.0103 -0.0007 265 ARG A C   
651   O O   . ARG A 42  ? 0.0952 0.0868 0.0851 -0.0101 -0.0237 -0.0033 265 ARG A O   
652   C CB  . ARG A 42  ? 0.0699 0.0942 0.0892 -0.0118 -0.0101 0.0036  265 ARG A CB  
653   C CG  . ARG A 42  ? 0.0829 0.0991 0.0802 0.0011  -0.0082 0.0130  265 ARG A CG  
654   C CD  . ARG A 42  ? 0.1015 0.1058 0.0815 0.0047  -0.0081 -0.0004 265 ARG A CD  
655   N NE  . ARG A 42  ? 0.0969 0.1056 0.1029 -0.0168 -0.0306 -0.0001 265 ARG A NE  
656   C CZ  . ARG A 42  ? 0.1213 0.1373 0.1286 -0.0411 -0.0024 0.0100  265 ARG A CZ  
657   N NH1 . ARG A 42  ? 0.1457 0.1458 0.1245 -0.0513 -0.0165 0.0258  265 ARG A NH1 
658   N NH2 . ARG A 42  ? 0.1455 0.1516 0.1430 -0.0489 -0.0053 0.0287  265 ARG A NH2 
672   N N   . CYS A 43  ? 0.0749 0.0867 0.0970 -0.0046 -0.0059 -0.0103 266 CYS A N   
673   C CA  . CYS A 43  ? 0.0690 0.0959 0.1113 -0.0042 0.0062  0.0021  266 CYS A CA  
674   C C   . CYS A 43  ? 0.0798 0.0776 0.1143 -0.0031 0.0161  -0.0036 266 CYS A C   
675   O O   . CYS A 43  ? 0.0885 0.0905 0.1180 -0.0175 0.0076  -0.0170 266 CYS A O   
676   C CB  . CYS A 43  ? 0.0759 0.0942 0.1140 -0.0081 0.0019  0.0038  266 CYS A CB  
677   S SG  . CYS A 43  ? 0.0963 0.1041 0.1344 0.0069  0.0046  0.0220  266 CYS A SG  
683   N N   . THR A 44  ? 0.0742 0.0813 0.1011 0.0012  0.0061  -0.0017 267 THR A N   
684   C CA  . THR A 44  ? 0.0919 0.0828 0.0959 -0.0037 0.0055  -0.0060 267 THR A CA  
685   C C   . THR A 44  ? 0.0727 0.0838 0.0977 0.0011  0.0146  -0.0022 267 THR A C   
686   O O   . THR A 44  ? 0.0840 0.0783 0.1131 0.0044  0.0057  0.0065  267 THR A O   
687   C CB  . THR A 44  ? 0.0940 0.0867 0.1014 0.0006  -0.0048 -0.0048 267 THR A CB  
688   O OG1 . THR A 44  ? 0.0852 0.0994 0.1117 -0.0046 0.0019  -0.0121 267 THR A OG1 
689   C CG2 . THR A 44  ? 0.1096 0.1045 0.1136 0.0107  -0.0082 0.0102  267 THR A CG2 
697   N N   . ILE A 45  ? 0.0852 0.0866 0.0968 -0.0105 0.0131  0.0037  268 ILE A N   
698   C CA  . ILE A 45  ? 0.0702 0.0872 0.1043 0.0024  -0.0118 0.0015  268 ILE A CA  
699   C C   . ILE A 45  ? 0.0774 0.0918 0.1049 0.0102  -0.0179 0.0128  268 ILE A C   
700   O O   . ILE A 45  ? 0.0992 0.0942 0.1224 0.0251  -0.0099 -0.0032 268 ILE A O   
701   C CB  . ILE A 45  ? 0.0915 0.0965 0.1123 -0.0058 -0.0203 -0.0089 268 ILE A CB  
702   C CG1 . ILE A 45  ? 0.0891 0.0973 0.1532 -0.0166 -0.0044 -0.0046 268 ILE A CG1 
703   C CG2 . ILE A 45  ? 0.1447 0.0938 0.1228 -0.0065 -0.0040 -0.0067 268 ILE A CG2 
704   C CD1 . ILE A 45  ? 0.1277 0.1171 0.1946 -0.0139 0.0174  0.0029  268 ILE A CD1 
716   N N   . ASP A 46  ? 0.0853 0.0966 0.1006 0.0176  -0.0085 0.0079  269 ASP A N   
717   C CA  . ASP A 46  ? 0.0990 0.1031 0.1103 0.0212  0.0058  0.0050  269 ASP A CA  
718   C C   . ASP A 46  ? 0.0874 0.0907 0.1310 0.0304  -0.0040 -0.0050 269 ASP A C   
719   O O   . ASP A 46  ? 0.1117 0.1030 0.1546 0.0067  0.0143  -0.0152 269 ASP A O   
720   C CB  . ASP A 46  ? 0.1224 0.1437 0.1241 0.0131  0.0186  0.0171  269 ASP A CB  
721   C CG  . ASP A 46  ? 0.1383 0.1909 0.1276 0.0026  0.0336  0.0238  269 ASP A CG  
722   O OD1 . ASP A 46  ? 0.1235 0.2014 0.1205 0.0069  0.0228  0.0148  269 ASP A OD1 
723   O OD2 . ASP A 46  ? 0.1875 0.2384 0.1678 0.0177  0.0336  0.0542  269 ASP A OD2 
728   N N   . GLY A 47  ? 0.0773 0.0840 0.1300 0.0094  -0.0062 -0.0101 270 GLY A N   
729   C CA  . GLY A 47  ? 0.0884 0.0966 0.1448 0.0091  -0.0103 -0.0100 270 GLY A CA  
730   C C   . GLY A 47  ? 0.0945 0.0941 0.1297 0.0004  -0.0129 -0.0063 270 GLY A C   
731   O O   . GLY A 47  ? 0.1003 0.0948 0.1389 0.0049  -0.0186 -0.0081 270 GLY A O   
735   N N   . GLU A 48  ? 0.0893 0.0968 0.1068 -0.0064 -0.0179 -0.0075 271 GLU A N   
736   C CA  . GLU A 48  ? 0.1123 0.1009 0.1004 0.0069  -0.0284 -0.0142 271 GLU A CA  
737   C C   . GLU A 48  ? 0.0894 0.0815 0.0984 0.0072  -0.0351 -0.0021 271 GLU A C   
738   O O   . GLU A 48  ? 0.0872 0.0806 0.1158 -0.0008 -0.0162 -0.0033 271 GLU A O   
739   C CB  . GLU A 48  ? 0.1516 0.1540 0.1129 -0.0055 -0.0375 -0.0169 271 GLU A CB  
740   C CG  . GLU A 48  ? 0.2299 0.2267 0.1532 -0.0024 -0.0321 -0.0073 271 GLU A CG  
741   C CD  . GLU A 48  ? 0.2925 0.2940 0.1928 -0.0188 -0.0481 -0.0060 271 GLU A CD  
742   O OE1 . GLU A 48  ? 0.3185 0.3208 0.2233 -0.0286 -0.0289 0.0037  271 GLU A OE1 
743   O OE2 . GLU A 48  ? 0.3310 0.3261 0.1959 -0.0118 -0.0508 -0.0119 271 GLU A OE2 
750   N N   . LEU A 49  ? 0.1070 0.0701 0.1107 0.0139  -0.0129 -0.0155 272 LEU A N   
751   C CA  . LEU A 49  ? 0.0937 0.0824 0.1066 -0.0044 -0.0171 -0.0041 272 LEU A CA  
752   C C   . LEU A 49  ? 0.1045 0.0801 0.0933 0.0023  -0.0132 0.0045  272 LEU A C   
753   O O   . LEU A 49  ? 0.1009 0.1005 0.0960 0.0160  -0.0280 -0.0150 272 LEU A O   
754   C CB  . LEU A 49  ? 0.0947 0.0883 0.1171 0.0016  -0.0224 -0.0111 272 LEU A CB  
755   C CG  . LEU A 49  ? 0.0897 0.0873 0.1198 0.0133  -0.0138 -0.0066 272 LEU A CG  
756   C CD1 . LEU A 49  ? 0.1159 0.0963 0.1365 0.0127  -0.0031 0.0059  272 LEU A CD1 
757   C CD2 . LEU A 49  ? 0.1086 0.1085 0.1192 0.0110  -0.0128 -0.0058 272 LEU A CD2 
769   N N   . LEU A 50  ? 0.0897 0.0864 0.0910 -0.0011 -0.0254 0.0004  273 LEU A N   
770   C CA  . LEU A 50  ? 0.0924 0.0880 0.0777 -0.0010 -0.0261 0.0011  273 LEU A CA  
771   C C   . LEU A 50  ? 0.0896 0.0915 0.0891 -0.0016 -0.0230 -0.0112 273 LEU A C   
772   O O   . LEU A 50  ? 0.0837 0.0866 0.0821 -0.0080 -0.0193 0.0001  273 LEU A O   
773   C CB  . LEU A 50  ? 0.1000 0.0967 0.0817 0.0030  -0.0179 0.0198  273 LEU A CB  
774   C CG  . LEU A 50  ? 0.1269 0.1159 0.1357 0.0008  0.0232  0.0338  273 LEU A CG  
775   C CD1 . LEU A 50  ? 0.1353 0.1261 0.1743 -0.0028 0.0228  0.0395  273 LEU A CD1 
776   C CD2 . LEU A 50  ? 0.1836 0.1446 0.1749 -0.0012 0.0596  0.0184  273 LEU A CD2 
788   N N   . GLY A 51  ? 0.0797 0.0820 0.1013 0.0091  -0.0320 0.0019  274 GLY A N   
789   C CA  . GLY A 51  ? 0.0853 0.0855 0.1077 0.0119  -0.0298 -0.0033 274 GLY A CA  
790   C C   . GLY A 51  ? 0.0789 0.0932 0.0972 0.0115  -0.0337 -0.0090 274 GLY A C   
791   O O   . GLY A 51  ? 0.0951 0.1032 0.1099 -0.0041 -0.0254 -0.0224 274 GLY A O   
795   N N   . THR A 52  ? 0.0817 0.0819 0.0853 0.0064  -0.0314 -0.0180 275 THR A N   
796   C CA  . THR A 52  ? 0.0717 0.0722 0.1087 0.0005  -0.0346 -0.0060 275 THR A CA  
797   C C   . THR A 52  ? 0.0736 0.0687 0.0972 -0.0010 -0.0282 -0.0160 275 THR A C   
798   O O   . THR A 52  ? 0.0768 0.0872 0.0792 -0.0098 -0.0239 0.0053  275 THR A O   
799   C CB  . THR A 52  ? 0.0698 0.0772 0.1083 0.0087  -0.0338 0.0011  275 THR A CB  
800   O OG1 . THR A 52  ? 0.0779 0.0825 0.0916 0.0029  -0.0266 -0.0013 275 THR A OG1 
801   C CG2 . THR A 52  ? 0.0730 0.0726 0.1155 -0.0002 -0.0268 -0.0067 275 THR A CG2 
809   N N   . THR A 53  ? 0.0598 0.0676 0.0903 -0.0133 -0.0198 -0.0007 276 THR A N   
810   C CA  . THR A 53  ? 0.0644 0.0782 0.0954 -0.0122 -0.0195 -0.0063 276 THR A CA  
811   C C   . THR A 53  ? 0.0699 0.0853 0.1017 -0.0079 -0.0240 -0.0089 276 THR A C   
812   O O   . THR A 53  ? 0.0988 0.0926 0.1038 0.0134  -0.0214 -0.0102 276 THR A O   
813   C CB  . THR A 53  ? 0.0668 0.0834 0.0998 -0.0062 -0.0256 0.0024  276 THR A CB  
814   O OG1 . THR A 53  ? 0.0717 0.0727 0.1146 -0.0070 -0.0373 0.0101  276 THR A OG1 
815   C CG2 . THR A 53  ? 0.0686 0.0976 0.0869 -0.0207 -0.0119 -0.0037 276 THR A CG2 
823   N N   . GLN A 54  ? 0.0668 0.0744 0.0866 0.0003  -0.0121 -0.0034 277 GLN A N   
824   C CA  . GLN A 54  ? 0.0742 0.0820 0.0897 0.0040  -0.0269 0.0009  277 GLN A CA  
825   C C   . GLN A 54  ? 0.0590 0.0916 0.1138 0.0045  -0.0236 -0.0081 277 GLN A C   
826   O O   . GLN A 54  ? 0.0681 0.1056 0.1186 0.0049  -0.0398 -0.0129 277 GLN A O   
827   C CB  . GLN A 54  ? 0.0795 0.0931 0.1070 -0.0034 -0.0341 -0.0047 277 GLN A CB  
828   C CG  . GLN A 54  ? 0.0838 0.0947 0.1030 -0.0064 -0.0227 -0.0105 277 GLN A CG  
829   C CD  . GLN A 54  ? 0.0759 0.0942 0.0983 0.0099  -0.0156 0.0022  277 GLN A CD  
830   O OE1 . GLN A 54  ? 0.0938 0.0887 0.1204 0.0163  -0.0083 0.0039  277 GLN A OE1 
831   N NE2 . GLN A 54  ? 0.0848 0.1012 0.0937 0.0090  -0.0159 0.0050  277 GLN A NE2 
840   N N   . LEU A 55  ? 0.0659 0.0889 0.1281 0.0165  -0.0269 -0.0068 278 LEU A N   
841   C CA  . LEU A 55  ? 0.0592 0.0938 0.1189 0.0149  -0.0302 -0.0123 278 LEU A CA  
842   C C   . LEU A 55  ? 0.0821 0.0996 0.1185 0.0304  -0.0169 -0.0050 278 LEU A C   
843   O O   . LEU A 55  ? 0.0977 0.1077 0.1171 0.0153  -0.0399 -0.0082 278 LEU A O   
844   C CB  . LEU A 55  ? 0.0849 0.1093 0.1220 0.0110  -0.0269 -0.0165 278 LEU A CB  
845   C CG  . LEU A 55  ? 0.1261 0.1204 0.1657 -0.0309 0.0145  -0.0363 278 LEU A CG  
846   C CD1 . LEU A 55  ? 0.1318 0.1384 0.1874 -0.0398 0.0185  -0.0391 278 LEU A CD1 
847   C CD2 . LEU A 55  ? 0.1478 0.1309 0.1934 -0.0200 0.0249  -0.0181 278 LEU A CD2 
859   N N   . ILE A 56  ? 0.0843 0.1206 0.1037 0.0363  -0.0046 0.0175  279 ILE A N   
860   C CA  . ILE A 56  ? 0.1126 0.1271 0.1104 0.0367  -0.0092 0.0198  279 ILE A CA  
861   C C   . ILE A 56  ? 0.0916 0.1321 0.1049 0.0116  -0.0100 0.0155  279 ILE A C   
862   O O   . ILE A 56  ? 0.0736 0.1126 0.1016 0.0149  -0.0197 0.0180  279 ILE A O   
863   C CB  . ILE A 56  ? 0.1853 0.1204 0.1592 0.0527  0.0338  0.0330  279 ILE A CB  
864   C CG1 . ILE A 56  ? 0.1854 0.1291 0.1876 0.0401  0.0341  0.0394  279 ILE A CG1 
865   C CG2 . ILE A 56  ? 0.2057 0.1344 0.1827 0.0357  0.0347  0.0327  279 ILE A CG2 
866   C CD1 . ILE A 56  ? 0.1754 0.1332 0.1991 0.0371  0.0036  0.0295  279 ILE A CD1 
878   N N   . THR A 57  ? 0.0967 0.1505 0.1002 -0.0028 -0.0391 0.0282  280 THR A N   
879   C CA  A THR A 57  ? 0.1238 0.1436 0.0992 -0.0220 -0.0428 0.0284  280 THR A CA  
880   C CA  B THR A 57  ? 0.1188 0.1519 0.0918 -0.0161 -0.0396 0.0187  280 THR A CA  
881   C C   . THR A 57  ? 0.1057 0.1315 0.0792 0.0001  -0.0456 0.0209  280 THR A C   
882   O O   . THR A 57  ? 0.1209 0.1203 0.0991 0.0128  -0.0268 0.0005  280 THR A O   
883   C CB  A THR A 57  ? 0.1693 0.1533 0.1119 -0.0548 -0.0402 0.0243  280 THR A CB  
884   C CB  B THR A 57  ? 0.1508 0.1722 0.0952 -0.0350 -0.0267 0.0102  280 THR A CB  
885   O OG1 A THR A 57  ? 0.1704 0.1593 0.1269 -0.0658 -0.0557 0.0349  280 THR A OG1 
886   O OG1 B THR A 57  ? 0.1620 0.1768 0.1136 -0.0438 -0.0244 0.0177  280 THR A OG1 
887   C CG2 A THR A 57  ? 0.1875 0.1618 0.1063 -0.0673 -0.0475 0.0177  280 THR A CG2 
888   C CG2 B THR A 57  ? 0.1479 0.1886 0.0887 -0.0297 -0.0561 -0.0013 280 THR A CG2 
903   N N   . SER A 58  ? 0.1112 0.1388 0.1002 0.0045  -0.0031 0.0545  281 SER A N   
904   C CA  A SER A 58  ? 0.1086 0.1580 0.1251 -0.0058 -0.0051 0.0608  281 SER A CA  
905   C CA  B SER A 58  ? 0.1181 0.1507 0.1324 -0.0099 0.0097  0.0551  281 SER A CA  
906   C C   . SER A 58  ? 0.1052 0.1651 0.1348 -0.0195 0.0080  0.0631  281 SER A C   
907   O O   . SER A 58  ? 0.1205 0.2509 0.1601 -0.0097 0.0236  0.0763  281 SER A O   
908   C CB  A SER A 58  ? 0.1187 0.1738 0.1230 0.0040  -0.0281 0.0569  281 SER A CB  
909   C CB  B SER A 58  ? 0.1429 0.1500 0.1538 -0.0106 0.0194  0.0419  281 SER A CB  
910   O OG  A SER A 58  ? 0.1168 0.1833 0.1394 0.0131  -0.0379 0.0528  281 SER A OG  
911   O OG  B SER A 58  ? 0.1576 0.1479 0.1792 -0.0133 0.0384  0.0302  281 SER A OG  
922   N N   . ASN A 59  ? 0.0822 0.1032 0.1351 0.0006  -0.0010 0.0372  282 ASN A N   
923   C CA  . ASN A 59  ? 0.0573 0.0762 0.1536 -0.0033 -0.0030 0.0139  282 ASN A CA  
924   C C   . ASN A 59  ? 0.0425 0.0715 0.1215 -0.0025 -0.0116 0.0065  282 ASN A C   
925   O O   . ASN A 59  ? 0.0795 0.0623 0.1368 -0.0169 -0.0136 -0.0057 282 ASN A O   
926   C CB  . ASN A 59  ? 0.0967 0.0960 0.1597 -0.0027 -0.0039 0.0117  282 ASN A CB  
927   C CG  . ASN A 59  ? 0.1137 0.0974 0.1815 0.0211  -0.0284 0.0186  282 ASN A CG  
928   O OD1 . ASN A 59  ? 0.1354 0.0873 0.2398 -0.0029 -0.0110 0.0024  282 ASN A OD1 
929   N ND2 . ASN A 59  ? 0.1376 0.1005 0.1634 0.0266  -0.0394 -0.0009 282 ASN A ND2 
936   N N   . ILE A 60  ? 0.0448 0.0708 0.1149 -0.0026 -0.0188 0.0047  283 ILE A N   
937   C CA  . ILE A 60  ? 0.0640 0.0715 0.1029 0.0011  -0.0113 -0.0035 283 ILE A CA  
938   C C   . ILE A 60  ? 0.0573 0.0671 0.0857 -0.0022 -0.0156 -0.0051 283 ILE A C   
939   O O   . ILE A 60  ? 0.0636 0.0883 0.0767 -0.0050 -0.0155 0.0029  283 ILE A O   
940   C CB  . ILE A 60  ? 0.0750 0.0772 0.0957 -0.0044 -0.0087 -0.0053 283 ILE A CB  
941   C CG1 . ILE A 60  ? 0.0674 0.0792 0.1166 -0.0093 -0.0158 -0.0052 283 ILE A CG1 
942   C CG2 . ILE A 60  ? 0.0765 0.0654 0.1377 -0.0056 -0.0068 -0.0169 283 ILE A CG2 
943   C CD1 . ILE A 60  ? 0.0717 0.0945 0.1325 -0.0088 -0.0148 0.0097  283 ILE A CD1 
955   N N   . CYS A 61  ? 0.0645 0.0692 0.0950 -0.0001 -0.0040 0.0034  284 CYS A N   
956   C CA  . CYS A 61  ? 0.0680 0.0712 0.1017 0.0063  -0.0044 0.0016  284 CYS A CA  
957   C C   . CYS A 61  ? 0.0737 0.0776 0.0984 -0.0001 -0.0170 -0.0019 284 CYS A C   
958   O O   . CYS A 61  ? 0.0785 0.0823 0.1086 -0.0056 -0.0058 -0.0002 284 CYS A O   
959   C CB  . CYS A 61  ? 0.0708 0.0644 0.1073 -0.0004 -0.0078 -0.0013 284 CYS A CB  
960   S SG  . CYS A 61  ? 0.0868 0.0635 0.1116 -0.0016 -0.0223 0.0021  284 CYS A SG  
966   N N   . SER A 62  ? 0.0686 0.0701 0.0876 -0.0105 -0.0130 -0.0151 285 SER A N   
967   C CA  A SER A 62  ? 0.0849 0.0724 0.0810 -0.0156 -0.0092 -0.0049 285 SER A CA  
968   C CA  B SER A 62  ? 0.0877 0.0806 0.0881 -0.0188 -0.0116 -0.0055 285 SER A CA  
969   C C   . SER A 62  ? 0.0956 0.0820 0.0759 -0.0246 -0.0093 -0.0060 285 SER A C   
970   O O   . SER A 62  ? 0.1309 0.1233 0.0964 -0.0622 -0.0157 -0.0058 285 SER A O   
971   C CB  A SER A 62  ? 0.0872 0.0725 0.1050 -0.0065 -0.0054 0.0091  285 SER A CB  
972   C CB  B SER A 62  ? 0.0980 0.0918 0.1074 -0.0185 -0.0124 0.0057  285 SER A CB  
973   O OG  A SER A 62  ? 0.0703 0.0782 0.1107 0.0004  -0.0075 0.0031  285 SER A OG  
974   O OG  B SER A 62  ? 0.0967 0.1006 0.1295 -0.0201 -0.0243 0.0083  285 SER A OG  
985   N N   . PHE A 63  ? 0.0745 0.0675 0.0801 -0.0319 -0.0156 -0.0118 286 PHE A N   
986   C CA  . PHE A 63  ? 0.0908 0.0696 0.0922 -0.0195 -0.0185 -0.0059 286 PHE A CA  
987   C C   . PHE A 63  ? 0.0935 0.0674 0.0920 -0.0242 -0.0272 -0.0132 286 PHE A C   
988   O O   . PHE A 63  ? 0.0921 0.0754 0.0942 -0.0188 0.0012  -0.0047 286 PHE A O   
989   C CB  . PHE A 63  ? 0.0940 0.0672 0.0906 -0.0205 -0.0246 0.0190  286 PHE A CB  
990   C CG  . PHE A 63  ? 0.0936 0.0683 0.1237 -0.0124 -0.0334 0.0139  286 PHE A CG  
991   C CD1 . PHE A 63  ? 0.0958 0.0761 0.1144 -0.0161 -0.0347 0.0188  286 PHE A CD1 
992   C CD2 . PHE A 63  ? 0.1078 0.0710 0.1514 0.0027  0.0089  0.0084  286 PHE A CD2 
993   C CE1 . PHE A 63  ? 0.0992 0.0863 0.1337 -0.0050 -0.0382 0.0220  286 PHE A CE1 
994   C CE2 . PHE A 63  ? 0.1024 0.0880 0.1773 -0.0090 0.0076  0.0013  286 PHE A CE2 
995   C CZ  . PHE A 63  ? 0.0973 0.0802 0.1564 -0.0100 -0.0178 0.0201  286 PHE A CZ  
1005  N N   . ARG A 64  ? 0.0827 0.0715 0.0882 -0.0282 -0.0277 0.0040  287 ARG A N   
1006  C CA  A ARG A 64  ? 0.0801 0.0729 0.1123 -0.0203 -0.0275 0.0054  287 ARG A CA  
1007  C CA  B ARG A 64  ? 0.0897 0.0690 0.1014 -0.0196 -0.0291 0.0071  287 ARG A CA  
1008  C C   . ARG A 64  ? 0.0791 0.0705 0.1007 -0.0228 -0.0132 0.0013  287 ARG A C   
1009  O O   . ARG A 64  ? 0.1014 0.0874 0.0895 -0.0343 -0.0233 0.0085  287 ARG A O   
1010  C CB  A ARG A 64  ? 0.1008 0.1018 0.1524 -0.0223 -0.0318 -0.0025 287 ARG A CB  
1011  C CB  B ARG A 64  ? 0.1322 0.1005 0.1199 -0.0241 -0.0292 -0.0025 287 ARG A CB  
1012  C CG  A ARG A 64  ? 0.1175 0.1199 0.1821 -0.0302 -0.0275 -0.0010 287 ARG A CG  
1013  C CG  B ARG A 64  ? 0.1617 0.1119 0.1084 -0.0376 -0.0321 -0.0009 287 ARG A CG  
1014  C CD  A ARG A 64  ? 0.1292 0.1271 0.2139 -0.0157 -0.0188 -0.0082 287 ARG A CD  
1015  C CD  B ARG A 64  ? 0.1762 0.1170 0.1367 -0.0354 -0.0117 0.0097  287 ARG A CD  
1016  N NE  A ARG A 64  ? 0.1371 0.1362 0.2474 0.0041  -0.0116 -0.0095 287 ARG A NE  
1017  N NE  B ARG A 64  ? 0.1832 0.1119 0.1484 -0.0430 -0.0127 0.0183  287 ARG A NE  
1018  C CZ  A ARG A 64  ? 0.1428 0.1465 0.2620 0.0220  0.0077  -0.0080 287 ARG A CZ  
1019  C CZ  B ARG A 64  ? 0.2119 0.1129 0.1318 -0.0410 -0.0249 0.0415  287 ARG A CZ  
1020  N NH1 A ARG A 64  ? 0.1508 0.1438 0.2505 0.0303  0.0091  0.0001  287 ARG A NH1 
1021  N NH1 B ARG A 64  ? 0.2047 0.1228 0.1378 -0.0436 -0.0127 0.0407  287 ARG A NH1 
1022  N NH2 A ARG A 64  ? 0.1385 0.1602 0.2861 0.0159  0.0165  -0.0223 287 ARG A NH2 
1023  N NH2 B ARG A 64  ? 0.2646 0.0816 0.1420 -0.0219 0.0050  0.0272  287 ARG A NH2 
1050  N N   . GLY A 65  ? 0.0826 0.0757 0.0861 -0.0261 -0.0229 0.0014  288 GLY A N   
1051  C CA  . GLY A 65  ? 0.0841 0.0808 0.0839 -0.0268 -0.0175 0.0112  288 GLY A CA  
1052  C C   . GLY A 65  ? 0.0875 0.0840 0.0946 -0.0275 -0.0183 0.0065  288 GLY A C   
1053  O O   . GLY A 65  ? 0.0995 0.0823 0.1013 -0.0230 -0.0146 0.0113  288 GLY A O   
1057  N N   . SER A 66  ? 0.0830 0.0877 0.1226 -0.0216 -0.0026 0.0156  289 SER A N   
1058  C CA  A SER A 66  ? 0.0860 0.0968 0.1237 -0.0256 -0.0193 0.0058  289 SER A CA  
1059  C CA  B SER A 66  ? 0.0954 0.0877 0.1194 -0.0213 -0.0013 0.0149  289 SER A CA  
1060  C C   . SER A 66  ? 0.0944 0.0844 0.1056 -0.0219 -0.0170 0.0139  289 SER A C   
1061  O O   . SER A 66  ? 0.1048 0.0906 0.1269 -0.0260 -0.0110 0.0351  289 SER A O   
1062  C CB  A SER A 66  ? 0.0946 0.1086 0.1353 -0.0270 -0.0302 -0.0095 289 SER A CB  
1063  C CB  B SER A 66  ? 0.1131 0.0882 0.1300 -0.0182 0.0177  0.0157  289 SER A CB  
1064  O OG  A SER A 66  ? 0.1257 0.1264 0.1539 -0.0187 -0.0351 -0.0315 289 SER A OG  
1065  O OG  B SER A 66  ? 0.1355 0.0940 0.1389 -0.0077 0.0290  0.0161  289 SER A OG  
1076  N N   . ILE A 67  ? 0.0999 0.0795 0.1021 -0.0186 -0.0079 0.0108  290 ILE A N   
1077  C CA  . ILE A 67  ? 0.0763 0.0804 0.1165 -0.0190 -0.0300 0.0160  290 ILE A CA  
1078  C C   . ILE A 67  ? 0.1020 0.0961 0.1135 -0.0237 -0.0258 0.0254  290 ILE A C   
1079  O O   . ILE A 67  ? 0.0899 0.0932 0.1164 -0.0138 -0.0155 0.0066  290 ILE A O   
1080  C CB  . ILE A 67  ? 0.0832 0.0801 0.1235 -0.0143 -0.0265 0.0217  290 ILE A CB  
1081  C CG1 . ILE A 67  ? 0.0811 0.0833 0.1227 -0.0131 -0.0234 0.0132  290 ILE A CG1 
1082  C CG2 . ILE A 67  ? 0.0872 0.0958 0.1319 -0.0227 -0.0435 0.0240  290 ILE A CG2 
1083  C CD1 . ILE A 67  ? 0.0740 0.0880 0.1235 -0.0196 -0.0322 0.0143  290 ILE A CD1 
1095  N N   A SER A 68  ? 0.1292 0.1100 0.1327 -0.0239 -0.0480 0.0241  291 SER A N   
1096  N N   B SER A 68  ? 0.1171 0.1172 0.1267 -0.0420 -0.0632 0.0172  291 SER A N   
1097  C CA  A SER A 68  ? 0.1577 0.1338 0.1637 -0.0226 -0.0521 0.0143  291 SER A CA  
1098  C CA  B SER A 68  ? 0.1427 0.1557 0.1662 -0.0498 -0.0743 0.0034  291 SER A CA  
1099  C C   A SER A 68  ? 0.1632 0.1713 0.1853 -0.0323 -0.0717 0.0019  291 SER A C   
1100  C C   B SER A 68  ? 0.1584 0.1886 0.2041 -0.0632 -0.0638 -0.0239 291 SER A C   
1101  O O   A SER A 68  ? 0.1752 0.1724 0.1876 -0.0336 -0.0658 0.0162  291 SER A O   
1102  O O   B SER A 68  ? 0.1694 0.2235 0.2443 -0.0814 -0.0558 -0.0535 291 SER A O   
1103  C CB  A SER A 68  ? 0.1834 0.1393 0.1822 -0.0163 -0.0234 0.0060  291 SER A CB  
1104  C CB  B SER A 68  ? 0.1606 0.1936 0.1795 -0.0383 -0.0756 0.0011  291 SER A CB  
1105  O OG  A SER A 68  ? 0.2037 0.1439 0.1925 -0.0085 -0.0014 0.0099  291 SER A OG  
1106  O OG  B SER A 68  ? 0.1959 0.2222 0.2031 -0.0296 -0.0391 0.0179  291 SER A OG  
1117  N N   . GLY A 69  ? 0.1569 0.1958 0.2096 -0.0400 -0.0817 -0.0261 292 GLY A N   
1118  C CA  . GLY A 69  ? 0.1493 0.2207 0.2554 -0.0611 -0.0564 -0.0490 292 GLY A CA  
1119  C C   . GLY A 69  ? 0.1299 0.2113 0.2543 -0.0465 -0.0684 -0.0260 292 GLY A C   
1120  O O   . GLY A 69  ? 0.1191 0.1355 0.2059 -0.0368 -0.0429 0.0209  292 GLY A O   
1125  N N   . HIS A 70  ? 0.1567 0.2616 0.3180 -0.0576 -0.0678 -0.0342 293 HIS A N   
1126  C CA  . HIS A 70  ? 0.1704 0.2567 0.3123 -0.0650 -0.1063 0.0098  293 HIS A CA  
1127  C C   . HIS A 70  ? 0.2537 0.3174 0.3377 -0.0929 -0.1513 0.0418  293 HIS A C   
1128  O O   . HIS A 70  ? 0.2769 0.3289 0.3259 -0.1120 -0.1549 0.0725  293 HIS A O   
1129  C CB  . HIS A 70  ? 0.1430 0.1963 0.3298 -0.0399 -0.0607 0.0553  293 HIS A CB  
1130  C CG  . HIS A 70  ? 0.1292 0.1541 0.3215 -0.0354 -0.0429 0.0721  293 HIS A CG  
1131  N ND1 . HIS A 70  ? 0.1319 0.1533 0.3302 -0.0275 -0.0366 0.0611  293 HIS A ND1 
1132  C CD2 . HIS A 70  ? 0.1515 0.1418 0.3345 -0.0393 -0.0168 0.0557  293 HIS A CD2 
1133  C CE1 . HIS A 70  ? 0.1425 0.1507 0.3369 -0.0319 -0.0292 0.0435  293 HIS A CE1 
1134  N NE2 . HIS A 70  ? 0.1519 0.1511 0.3445 -0.0460 -0.0094 0.0362  293 HIS A NE2 
1142  N N   . GLU A 71  ? 0.3226 0.3644 0.3828 -0.0987 -0.1924 0.0504  294 GLU A N   
1143  C CA  . GLU A 71  ? 0.4302 0.4477 0.4690 -0.0666 -0.1739 0.0439  294 GLU A CA  
1144  C C   . GLU A 71  ? 0.5166 0.5278 0.5417 -0.0532 -0.1786 0.0392  294 GLU A C   
1145  O O   . GLU A 71  ? 0.5223 0.5344 0.5622 -0.0534 -0.1649 0.0340  294 GLU A O   
1146  C CB  . GLU A 71  ? 0.4635 0.4554 0.4915 -0.0369 -0.1226 0.0461  294 GLU A CB  
1147  C CG  . GLU A 71  ? 0.4742 0.4549 0.4968 -0.0140 -0.1022 0.0514  294 GLU A CG  
1148  C CD  . GLU A 71  ? 0.4756 0.4566 0.4937 -0.0025 -0.0993 0.0494  294 GLU A CD  
1149  O OE1 . GLU A 71  ? 0.4914 0.4618 0.5081 -0.0033 -0.0767 0.0389  294 GLU A OE1 
1150  O OE2 . GLU A 71  ? 0.4593 0.4515 0.4773 0.0087  -0.1220 0.0576  294 GLU A OE2 
1190  N N   . GLN A 76  ? 0.4093 0.4234 0.4377 0.0378  -0.0360 0.0224  299 GLN A N   
1191  C CA  . GLN A 76  ? 0.2989 0.3275 0.3493 0.0460  -0.0419 0.0270  299 GLN A CA  
1192  C C   . GLN A 76  ? 0.2142 0.2499 0.2914 0.0465  -0.0415 0.0240  299 GLN A C   
1193  O O   . GLN A 76  ? 0.2342 0.2497 0.3276 0.0791  -0.0266 0.0210  299 GLN A O   
1194  C CB  . GLN A 76  ? 0.3037 0.3143 0.3484 0.0293  0.0051  0.0335  299 GLN A CB  
1195  C CG  . GLN A 76  ? 0.3017 0.3054 0.3394 0.0318  0.0323  0.0568  299 GLN A CG  
1196  C CD  . GLN A 76  ? 0.2950 0.2897 0.3301 0.0427  0.0643  0.0930  299 GLN A CD  
1197  O OE1 . GLN A 76  ? 0.2963 0.2725 0.3043 0.0796  0.1161  0.1329  299 GLN A OE1 
1198  N NE2 . GLN A 76  ? 0.2940 0.2845 0.3368 0.0196  0.0251  0.1050  299 GLN A NE2 
1207  N N   . HIS A 77  ? 0.1168 0.1631 0.2158 0.0115  -0.0174 0.0384  300 HIS A N   
1208  C CA  . HIS A 77  ? 0.0766 0.1312 0.1990 0.0023  -0.0201 0.0469  300 HIS A CA  
1209  C C   . HIS A 77  ? 0.0618 0.1271 0.1908 0.0026  -0.0138 0.0310  300 HIS A C   
1210  O O   . HIS A 77  ? 0.0722 0.1442 0.1773 -0.0097 -0.0170 0.0349  300 HIS A O   
1211  C CB  . HIS A 77  ? 0.0803 0.1384 0.2090 0.0032  0.0059  0.0564  300 HIS A CB  
1212  C CG  . HIS A 77  ? 0.0917 0.1544 0.2424 0.0177  0.0192  0.0637  300 HIS A CG  
1213  N ND1 . HIS A 77  ? 0.1208 0.1723 0.2563 0.0039  0.0474  0.0588  300 HIS A ND1 
1214  C CD2 . HIS A 77  ? 0.1209 0.1726 0.2700 0.0220  0.0323  0.0601  300 HIS A CD2 
1215  C CE1 . HIS A 77  ? 0.1180 0.1787 0.2712 0.0111  0.0536  0.0649  300 HIS A CE1 
1216  N NE2 . HIS A 77  ? 0.1353 0.1893 0.2783 0.0177  0.0445  0.0657  300 HIS A NE2 
1224  N N   A LEU A 78  ? 0.0546 0.1083 0.1794 -0.0007 -0.0252 0.0232  301 LEU A N   
1225  C CA  A LEU A 78  ? 0.0730 0.1082 0.1818 -0.0148 -0.0332 0.0146  301 LEU A CA  
1226  C C   A LEU A 78  ? 0.0722 0.0899 0.1829 -0.0166 -0.0360 0.0124  301 LEU A C   
1227  O O   A LEU A 78  ? 0.0720 0.1130 0.2127 -0.0195 -0.0355 -0.0070 301 LEU A O   
1228  C CB  A LEU A 78  ? 0.0925 0.1293 0.2134 0.0020  -0.0436 0.0314  301 LEU A CB  
1229  C CG  A LEU A 78  ? 0.1457 0.1440 0.2406 0.0113  -0.0529 0.0467  301 LEU A CG  
1230  C CD1 A LEU A 78  ? 0.1801 0.1661 0.2664 0.0238  -0.0407 0.0541  301 LEU A CD1 
1231  C CD2 A LEU A 78  ? 0.1930 0.1510 0.2637 0.0176  -0.0562 0.0348  301 LEU A CD2 
1243  N N   . TRP A 79  ? 0.0736 0.0858 0.1627 -0.0197 -0.0364 0.0224  302 TRP A N   
1244  C CA  . TRP A 79  ? 0.0836 0.0898 0.1382 -0.0241 -0.0429 0.0230  302 TRP A CA  
1245  C C   . TRP A 79  ? 0.0765 0.0893 0.1289 -0.0182 -0.0321 0.0255  302 TRP A C   
1246  O O   . TRP A 79  ? 0.0895 0.0966 0.1430 -0.0283 -0.0177 0.0095  302 TRP A O   
1247  C CB  . TRP A 79  ? 0.0877 0.0749 0.1329 -0.0174 -0.0297 0.0263  302 TRP A CB  
1248  C CG  . TRP A 79  ? 0.0810 0.0830 0.1371 -0.0066 -0.0219 0.0301  302 TRP A CG  
1249  C CD1 . TRP A 79  ? 0.0829 0.0918 0.1310 -0.0117 -0.0192 0.0202  302 TRP A CD1 
1250  C CD2 . TRP A 79  ? 0.0813 0.0907 0.1365 -0.0049 -0.0294 0.0261  302 TRP A CD2 
1251  N NE1 . TRP A 79  ? 0.0737 0.1006 0.1373 -0.0082 -0.0007 0.0107  302 TRP A NE1 
1252  C CE2 . TRP A 79  ? 0.0604 0.1077 0.1453 -0.0187 -0.0217 0.0265  302 TRP A CE2 
1253  C CE3 . TRP A 79  ? 0.0654 0.1080 0.1589 -0.0195 -0.0384 0.0289  302 TRP A CE3 
1254  C CZ2 . TRP A 79  ? 0.0744 0.1246 0.1694 -0.0064 -0.0084 0.0385  302 TRP A CZ2 
1255  C CZ3 . TRP A 79  ? 0.0687 0.1150 0.1939 -0.0167 -0.0420 0.0247  302 TRP A CZ3 
1256  C CH2 . TRP A 79  ? 0.0759 0.1271 0.1882 -0.0166 -0.0271 0.0424  302 TRP A CH2 
1267  N N   . HIS A 80  ? 0.0785 0.0866 0.1317 -0.0357 -0.0406 0.0193  303 HIS A N   
1268  C CA  . HIS A 80  ? 0.1029 0.0908 0.1149 -0.0263 -0.0391 0.0209  303 HIS A CA  
1269  C C   . HIS A 80  ? 0.0905 0.0807 0.1086 -0.0244 -0.0380 0.0290  303 HIS A C   
1270  O O   . HIS A 80  ? 0.0949 0.0856 0.1400 -0.0209 -0.0331 0.0258  303 HIS A O   
1271  C CB  . HIS A 80  ? 0.1045 0.1062 0.1254 -0.0273 -0.0607 0.0234  303 HIS A CB  
1272  C CG  . HIS A 80  ? 0.1444 0.1326 0.1359 -0.0267 -0.0514 0.0267  303 HIS A CG  
1273  N ND1 . HIS A 80  ? 0.1880 0.1614 0.1684 -0.0150 -0.0178 0.0294  303 HIS A ND1 
1274  C CD2 . HIS A 80  ? 0.1719 0.1434 0.1613 -0.0283 -0.0395 0.0259  303 HIS A CD2 
1275  C CE1 . HIS A 80  ? 0.1846 0.1671 0.1578 -0.0137 -0.0298 0.0330  303 HIS A CE1 
1276  N NE2 . HIS A 80  ? 0.1809 0.1589 0.1645 -0.0358 -0.0390 0.0170  303 HIS A NE2 
1284  N N   . PHE A 81  ? 0.0819 0.0823 0.1093 -0.0290 -0.0325 0.0306  304 PHE A N   
1285  C CA  . PHE A 81  ? 0.0768 0.0768 0.1047 -0.0251 -0.0305 0.0321  304 PHE A CA  
1286  C C   . PHE A 81  ? 0.0841 0.0763 0.1019 -0.0201 -0.0370 0.0279  304 PHE A C   
1287  O O   . PHE A 81  ? 0.1051 0.0719 0.1095 -0.0184 -0.0164 0.0297  304 PHE A O   
1288  C CB  . PHE A 81  ? 0.0950 0.0758 0.1091 -0.0185 -0.0253 0.0237  304 PHE A CB  
1289  C CG  . PHE A 81  ? 0.0881 0.0868 0.1158 -0.0172 -0.0310 0.0176  304 PHE A CG  
1290  C CD1 . PHE A 81  ? 0.0933 0.0906 0.1122 -0.0086 -0.0338 0.0141  304 PHE A CD1 
1291  C CD2 . PHE A 81  ? 0.1103 0.1233 0.1474 0.0095  -0.0424 -0.0011 304 PHE A CD2 
1292  C CE1 . PHE A 81  ? 0.0906 0.0998 0.1174 -0.0041 -0.0258 0.0066  304 PHE A CE1 
1293  C CE2 . PHE A 81  ? 0.1113 0.1469 0.1498 0.0166  -0.0521 0.0017  304 PHE A CE2 
1294  C CZ  . PHE A 81  ? 0.0905 0.1299 0.1457 0.0124  -0.0464 0.0108  304 PHE A CZ  
1304  N N   . ASN A 82  ? 0.0932 0.0900 0.1020 -0.0313 -0.0271 0.0154  305 ASN A N   
1305  C CA  . ASN A 82  ? 0.1071 0.1027 0.1142 -0.0294 -0.0189 0.0133  305 ASN A CA  
1306  C C   . ASN A 82  ? 0.0999 0.1011 0.1061 -0.0170 -0.0143 0.0228  305 ASN A C   
1307  O O   . ASN A 82  ? 0.1183 0.1207 0.1490 -0.0059 -0.0065 0.0571  305 ASN A O   
1308  C CB  . ASN A 82  ? 0.1306 0.1164 0.1540 -0.0370 -0.0076 0.0015  305 ASN A CB  
1309  C CG  . ASN A 82  ? 0.1656 0.1388 0.2309 -0.0596 0.0055  -0.0374 305 ASN A CG  
1310  O OD1 . ASN A 82  ? 0.2297 0.1576 0.3124 -0.0526 0.0406  -0.0409 305 ASN A OD1 
1311  N ND2 . ASN A 82  ? 0.1398 0.1626 0.2197 -0.0446 -0.0360 -0.0375 305 ASN A ND2 
1318  N N   . ILE A 83  ? 0.1034 0.0910 0.0870 -0.0151 -0.0144 0.0155  306 ILE A N   
1319  C CA  . ILE A 83  ? 0.1015 0.0917 0.0866 -0.0118 -0.0169 0.0055  306 ILE A CA  
1320  C C   . ILE A 83  ? 0.1243 0.0983 0.0838 -0.0151 -0.0220 -0.0050 306 ILE A C   
1321  O O   . ILE A 83  ? 0.1505 0.1326 0.0910 0.0081  -0.0126 0.0020  306 ILE A O   
1322  C CB  . ILE A 83  ? 0.0948 0.0794 0.0952 -0.0147 -0.0236 0.0052  306 ILE A CB  
1323  C CG1 . ILE A 83  ? 0.1168 0.0746 0.1039 -0.0106 -0.0226 0.0061  306 ILE A CG1 
1324  C CG2 . ILE A 83  ? 0.1161 0.0916 0.1061 -0.0199 -0.0100 -0.0010 306 ILE A CG2 
1325  C CD1 . ILE A 83  ? 0.1063 0.0771 0.1117 -0.0136 -0.0164 0.0017  306 ILE A CD1 
1337  N N   . THR A 84  ? 0.1051 0.1010 0.0974 -0.0218 -0.0155 -0.0040 307 THR A N   
1338  C CA  . THR A 84  ? 0.1033 0.1295 0.0839 -0.0266 -0.0066 -0.0010 307 THR A CA  
1339  C C   . THR A 84  ? 0.1179 0.1749 0.0796 -0.0494 -0.0017 -0.0249 307 THR A C   
1340  O O   . THR A 84  ? 0.1562 0.2259 0.1112 -0.0824 0.0123  -0.0544 307 THR A O   
1341  C CB  . THR A 84  ? 0.1253 0.1342 0.1209 -0.0051 -0.0186 0.0066  307 THR A CB  
1342  O OG1 . THR A 84  ? 0.1362 0.1565 0.1425 0.0111  -0.0238 0.0236  307 THR A OG1 
1343  C CG2 . THR A 84  ? 0.1357 0.1337 0.1338 -0.0232 -0.0086 0.0027  307 THR A CG2 
1351  N N   A ASN A 85  ? 0.1040 0.1839 0.1082 -0.0463 -0.0009 -0.0024 308 ASN A N   
1352  N N   B ASN A 85  ? 0.1048 0.1657 0.0821 -0.0465 -0.0228 -0.0188 308 ASN A N   
1353  C CA  A ASN A 85  ? 0.1058 0.1931 0.1492 -0.0297 0.0002  0.0139  308 ASN A CA  
1354  C CA  B ASN A 85  ? 0.0923 0.1461 0.0803 -0.0305 -0.0379 0.0045  308 ASN A CA  
1355  C C   A ASN A 85  ? 0.1124 0.1850 0.1631 -0.0153 -0.0187 0.0133  308 ASN A C   
1356  C C   B ASN A 85  ? 0.0992 0.1156 0.0894 -0.0067 -0.0318 0.0139  308 ASN A C   
1357  O O   A ASN A 85  ? 0.0920 0.1921 0.1638 -0.0080 -0.0185 0.0182  308 ASN A O   
1358  O O   B ASN A 85  ? 0.0899 0.1167 0.1001 0.0038  -0.0334 0.0054  308 ASN A O   
1359  C CB  A ASN A 85  ? 0.1148 0.1911 0.1657 -0.0124 0.0161  0.0268  308 ASN A CB  
1360  C CB  B ASN A 85  ? 0.0892 0.1489 0.0986 -0.0434 -0.0315 -0.0109 308 ASN A CB  
1361  C CG  A ASN A 85  ? 0.1128 0.1715 0.1548 -0.0051 0.0175  0.0249  308 ASN A CG  
1362  C CG  B ASN A 85  ? 0.0981 0.1377 0.0996 -0.0443 -0.0136 -0.0303 308 ASN A CG  
1363  O OD1 A ASN A 85  ? 0.1232 0.1707 0.1622 -0.0195 0.0273  0.0064  308 ASN A OD1 
1364  O OD1 B ASN A 85  ? 0.1096 0.1340 0.1029 -0.0533 -0.0094 -0.0405 308 ASN A OD1 
1365  N ND2 A ASN A 85  ? 0.1264 0.1655 0.1653 0.0083  0.0306  0.0298  308 ASN A ND2 
1366  N ND2 B ASN A 85  ? 0.1075 0.1411 0.1081 -0.0252 0.0034  -0.0262 308 ASN A ND2 
1379  N N   A PRO A 86  ? 0.1351 0.1758 0.1793 -0.0252 -0.0308 0.0239  309 PRO A N   
1380  N N   B PRO A 86  ? 0.0971 0.0880 0.0972 0.0228  -0.0165 0.0252  309 PRO A N   
1381  C CA  A PRO A 86  ? 0.1502 0.1816 0.1953 -0.0181 -0.0263 0.0208  309 PRO A CA  
1382  C CA  B PRO A 86  ? 0.1051 0.0843 0.1117 0.0281  -0.0124 0.0178  309 PRO A CA  
1383  C C   A PRO A 86  ? 0.1699 0.1872 0.2040 0.0098  -0.0344 0.0141  309 PRO A C   
1384  C C   B PRO A 86  ? 0.1100 0.0837 0.1211 0.0193  -0.0173 0.0265  309 PRO A C   
1385  O O   A PRO A 86  ? 0.1905 0.1841 0.1970 0.0200  -0.0345 0.0242  309 PRO A O   
1386  O O   B PRO A 86  ? 0.1259 0.0940 0.1216 0.0149  -0.0094 0.0371  309 PRO A O   
1387  C CB  A PRO A 86  ? 0.1559 0.1896 0.2039 -0.0241 -0.0270 0.0216  309 PRO A CB  
1388  C CB  B PRO A 86  ? 0.0969 0.0873 0.1189 0.0395  -0.0094 -0.0033 309 PRO A CB  
1389  C CG  A PRO A 86  ? 0.1512 0.1860 0.1925 -0.0254 -0.0422 0.0215  309 PRO A CG  
1390  C CG  B PRO A 86  ? 0.0948 0.0858 0.1179 0.0427  0.0076  -0.0055 309 PRO A CG  
1391  C CD  A PRO A 86  ? 0.1502 0.1791 0.1925 -0.0347 -0.0350 0.0072  309 PRO A CD  
1392  C CD  B PRO A 86  ? 0.0926 0.0837 0.1069 0.0331  -0.0049 0.0171  309 PRO A CD  
1407  N N   A ASN A 87  ? 0.1700 0.1823 0.2209 0.0288  -0.0291 0.0050  310 ASN A N   
1408  N N   B ASN A 87  ? 0.1126 0.0819 0.1327 0.0092  -0.0339 -0.0037 310 ASN A N   
1409  C CA  A ASN A 87  ? 0.1786 0.1943 0.2451 0.0605  -0.0125 0.0058  310 ASN A CA  
1410  C CA  B ASN A 87  ? 0.1283 0.0926 0.1496 -0.0028 -0.0245 -0.0210 310 ASN A CA  
1411  C C   A ASN A 87  ? 0.1922 0.1683 0.2501 0.0654  -0.0138 0.0179  310 ASN A C   
1412  C C   B ASN A 87  ? 0.1578 0.1114 0.1613 -0.0066 -0.0154 -0.0251 310 ASN A C   
1413  O O   A ASN A 87  ? 0.2049 0.1513 0.2619 0.0837  -0.0122 0.0216  310 ASN A O   
1414  O O   B ASN A 87  ? 0.1736 0.1217 0.1593 -0.0109 -0.0160 -0.0272 310 ASN A O   
1415  C CB  A ASN A 87  ? 0.1703 0.2353 0.2481 0.0703  -0.0086 -0.0042 310 ASN A CB  
1416  C CB  B ASN A 87  ? 0.1227 0.0965 0.1591 0.0016  -0.0122 -0.0332 310 ASN A CB  
1417  C CG  A ASN A 87  ? 0.1762 0.2692 0.2527 0.0682  0.0108  -0.0031 310 ASN A CG  
1418  C CG  B ASN A 87  ? 0.1168 0.1062 0.1555 0.0115  -0.0032 -0.0431 310 ASN A CG  
1419  O OD1 A ASN A 87  ? 0.1564 0.2637 0.2333 0.0528  -0.0188 -0.0130 310 ASN A OD1 
1420  O OD1 B ASN A 87  ? 0.1095 0.1151 0.1462 0.0041  -0.0118 -0.0447 310 ASN A OD1 
1421  N ND2 A ASN A 87  ? 0.1939 0.2891 0.2696 0.0532  0.0225  -0.0106 310 ASN A ND2 
1422  N ND2 B ASN A 87  ? 0.1271 0.1204 0.1741 0.0145  0.0187  -0.0402 310 ASN A ND2 
1435  N N   A GLY A 88  ? 0.1914 0.1517 0.2487 0.0554  -0.0132 0.0237  311 GLY A N   
1436  N N   B GLY A 88  ? 0.1760 0.1169 0.1704 -0.0157 -0.0121 -0.0326 311 GLY A N   
1437  C CA  A GLY A 88  ? 0.2055 0.1427 0.2378 0.0533  -0.0015 0.0357  311 GLY A CA  
1438  C CA  B GLY A 88  ? 0.1875 0.1238 0.1653 -0.0106 0.0030  -0.0301 311 GLY A CA  
1439  C C   A GLY A 88  ? 0.2314 0.1592 0.2471 0.0443  0.0600  -0.0009 311 GLY A C   
1440  C C   B GLY A 88  ? 0.2096 0.1328 0.1693 -0.0138 0.0381  -0.0274 311 GLY A C   
1441  O O   A GLY A 88  ? 0.2490 0.1592 0.2678 0.0194  0.0665  -0.0224 311 GLY A O   
1442  O O   B GLY A 88  ? 0.2342 0.1347 0.1412 -0.0232 0.0569  -0.0248 311 GLY A O   
1449  N N   A THR A 89  ? 0.2184 0.1743 0.2474 0.0601  0.0824  -0.0002 312 THR A N   
1450  N N   B THR A 89  ? 0.2220 0.1438 0.1958 0.0015  0.0770  -0.0222 312 THR A N   
1451  C CA  A THR A 89  ? 0.2003 0.1770 0.2295 0.0510  0.0771  -0.0206 312 THR A CA  
1452  C CA  B THR A 89  ? 0.2242 0.1601 0.2152 0.0008  0.0938  -0.0277 312 THR A CA  
1453  C C   A THR A 89  ? 0.1736 0.1728 0.1892 0.0196  0.0407  -0.0258 312 THR A C   
1454  C C   B THR A 89  ? 0.2167 0.1743 0.1995 -0.0089 0.0738  -0.0394 312 THR A C   
1455  O O   A THR A 89  ? 0.1353 0.1567 0.1321 0.0181  0.0040  -0.0086 312 THR A O   
1456  O O   B THR A 89  ? 0.2207 0.1747 0.1816 -0.0052 0.0831  -0.0315 312 THR A O   
1457  C CB  A THR A 89  ? 0.1962 0.1839 0.2458 0.0622  0.0883  -0.0033 312 THR A CB  
1458  C CB  B THR A 89  ? 0.2276 0.1610 0.2352 0.0038  0.1063  -0.0117 312 THR A CB  
1459  O OG1 A THR A 89  ? 0.1671 0.1857 0.2139 0.0505  0.0561  0.0076  312 THR A OG1 
1460  O OG1 B THR A 89  ? 0.2205 0.1620 0.2389 0.0029  0.0938  -0.0025 312 THR A OG1 
1461  C CG2 A THR A 89  ? 0.2092 0.1924 0.2552 0.0726  0.1095  0.0054  312 THR A CG2 
1462  C CG2 B THR A 89  ? 0.2420 0.1641 0.2460 0.0066  0.1214  -0.0089 312 THR A CG2 
1477  N N   . PRO A 90  ? 0.2113 0.1873 0.2001 -0.0286 0.0480  -0.0710 313 PRO A N   
1478  C CA  . PRO A 90  ? 0.2037 0.2014 0.1661 -0.0479 -0.0146 -0.0848 313 PRO A CA  
1479  C C   . PRO A 90  ? 0.2016 0.1960 0.1534 -0.0178 -0.0328 -0.0757 313 PRO A C   
1480  O O   . PRO A 90  ? 0.1954 0.2035 0.1875 -0.0319 -0.0047 -0.0651 313 PRO A O   
1481  C CB  . PRO A 90  ? 0.2441 0.2319 0.1963 -0.0769 0.0123  -0.0870 313 PRO A CB  
1482  C CG  . PRO A 90  ? 0.2604 0.2347 0.2059 -0.0853 0.0251  -0.1000 313 PRO A CG  
1483  C CD  . PRO A 90  ? 0.2479 0.2121 0.2201 -0.0619 0.0437  -0.0929 313 PRO A CD  
1491  N N   . PHE A 91  ? 0.2204 0.1796 0.1637 0.0114  -0.0328 -0.0608 314 PHE A N   
1492  C CA  . PHE A 91  ? 0.2691 0.1744 0.1656 0.0526  -0.0587 -0.0502 314 PHE A CA  
1493  C C   . PHE A 91  ? 0.3298 0.1858 0.1690 0.0676  -0.0723 -0.0448 314 PHE A C   
1494  O O   . PHE A 91  ? 0.3303 0.2200 0.1611 0.0639  -0.0965 -0.0612 314 PHE A O   
1495  C CB  . PHE A 91  ? 0.2687 0.1683 0.1605 0.0547  -0.0786 -0.0543 314 PHE A CB  
1496  C CG  . PHE A 91  ? 0.2718 0.1570 0.1414 0.0644  -0.0770 -0.0501 314 PHE A CG  
1497  C CD1 . PHE A 91  ? 0.2825 0.1501 0.1501 0.0567  -0.0505 -0.0508 314 PHE A CD1 
1498  C CD2 . PHE A 91  ? 0.2826 0.1672 0.1510 0.0649  -0.0723 -0.0534 314 PHE A CD2 
1499  C CE1 . PHE A 91  ? 0.3010 0.1586 0.1567 0.0507  -0.0339 -0.0407 314 PHE A CE1 
1500  C CE2 . PHE A 91  ? 0.3008 0.1696 0.1551 0.0601  -0.0602 -0.0463 314 PHE A CE2 
1501  C CZ  . PHE A 91  ? 0.3035 0.1672 0.1459 0.0560  -0.0460 -0.0482 314 PHE A CZ  
1511  N N   . ASP A 92  ? 0.3996 0.1669 0.1481 0.0625  -0.0685 -0.0212 315 ASP A N   
1512  C CA  . ASP A 92  ? 0.4764 0.1665 0.1661 0.0624  -0.0534 -0.0275 315 ASP A CA  
1513  C C   . ASP A 92  ? 0.5134 0.1714 0.1844 0.0466  -0.0621 -0.0441 315 ASP A C   
1514  O O   . ASP A 92  ? 0.5399 0.1731 0.1840 0.0391  -0.0389 -0.0395 315 ASP A O   
1515  C CB  . ASP A 92  ? 0.5114 0.1661 0.1717 0.0676  -0.0238 -0.0305 315 ASP A CB  
1516  C CG  . ASP A 92  ? 0.5494 0.1861 0.1883 0.0632  0.0028  -0.0289 315 ASP A CG  
1517  O OD1 . ASP A 92  ? 0.5526 0.1907 0.1806 0.0562  -0.0085 -0.0424 315 ASP A OD1 
1518  O OD2 . ASP A 92  ? 0.5672 0.2072 0.2244 0.0605  0.0435  -0.0088 315 ASP A OD2 
1523  N N   . PRO A 93  ? 0.5359 0.1729 0.2137 0.0603  -0.0819 -0.0470 316 PRO A N   
1524  C CA  A PRO A 93  ? 0.5468 0.1758 0.2214 0.0540  -0.0876 -0.0487 316 PRO A CA  
1525  C CA  B PRO A 93  ? 0.5458 0.1759 0.2250 0.0548  -0.0841 -0.0505 316 PRO A CA  
1526  C C   . PRO A 93  ? 0.5541 0.1759 0.2346 0.0499  -0.0946 -0.0460 316 PRO A C   
1527  O O   . PRO A 93  ? 0.5570 0.1733 0.2576 0.0444  -0.1258 -0.0405 316 PRO A O   
1528  C CB  A PRO A 93  ? 0.5499 0.1802 0.2204 0.0583  -0.0834 -0.0443 316 PRO A CB  
1529  C CB  B PRO A 93  ? 0.5513 0.1779 0.2294 0.0615  -0.0733 -0.0521 316 PRO A CB  
1530  C CG  A PRO A 93  ? 0.5459 0.1813 0.2107 0.0563  -0.0880 -0.0490 316 PRO A CG  
1531  C CG  B PRO A 93  ? 0.5418 0.1820 0.2267 0.0604  -0.0681 -0.0575 316 PRO A CG  
1532  C CD  A PRO A 93  ? 0.5438 0.1769 0.2187 0.0595  -0.0863 -0.0482 316 PRO A CD  
1533  C CD  B PRO A 93  ? 0.5377 0.1772 0.2204 0.0635  -0.0786 -0.0517 316 PRO A CD  
1548  N N   . THR A 94  ? 0.5645 0.1955 0.2304 0.0386  -0.0731 -0.0495 317 THR A N   
1549  C CA  . THR A 94  ? 0.5726 0.2070 0.2330 0.0215  -0.0542 -0.0568 317 THR A CA  
1550  C C   . THR A 94  ? 0.5668 0.2157 0.2454 0.0218  -0.0220 -0.0478 317 THR A C   
1551  O O   . THR A 94  ? 0.5792 0.2290 0.2598 0.0136  -0.0091 -0.0484 317 THR A O   
1552  C CB  . THR A 94  ? 0.5934 0.2208 0.2284 0.0046  -0.0563 -0.0625 317 THR A CB  
1553  O OG1 . THR A 94  ? 0.5956 0.2202 0.2290 -0.0014 -0.0439 -0.0721 317 THR A OG1 
1554  C CG2 . THR A 94  ? 0.5933 0.2372 0.2379 -0.0099 -0.0563 -0.0545 317 THR A CG2 
1562  N N   A GLU A 95  ? 0.5414 0.2161 0.2349 0.0328  -0.0205 -0.0519 318 GLU A N   
1563  C CA  A GLU A 95  ? 0.5050 0.2305 0.2438 0.0402  -0.0089 -0.0371 318 GLU A CA  
1564  C C   A GLU A 95  ? 0.4400 0.2193 0.2087 0.0369  -0.0096 -0.0438 318 GLU A C   
1565  O O   A GLU A 95  ? 0.4236 0.2099 0.2011 0.0475  -0.0301 -0.0452 318 GLU A O   
1566  C CB  A GLU A 95  ? 0.5345 0.2594 0.2907 0.0404  0.0124  -0.0170 318 GLU A CB  
1567  C CG  A GLU A 95  ? 0.5603 0.2933 0.3305 0.0388  0.0304  -0.0019 318 GLU A CG  
1568  C CD  A GLU A 95  ? 0.5814 0.3178 0.3583 0.0393  0.0417  0.0148  318 GLU A CD  
1569  O OE1 A GLU A 95  ? 0.5934 0.3267 0.3807 0.0439  0.0484  0.0235  318 GLU A OE1 
1570  O OE2 A GLU A 95  ? 0.5957 0.3326 0.3645 0.0262  0.0498  0.0140  318 GLU A OE2 
1577  N N   . ASP A 96  ? 0.3982 0.2284 0.2061 0.0325  0.0346  -0.0312 319 ASP A N   
1578  C CA  . ASP A 96  ? 0.3540 0.2316 0.2123 0.0148  0.0503  -0.0213 319 ASP A CA  
1579  C C   . ASP A 96  ? 0.2955 0.1993 0.2033 0.0006  0.0513  -0.0182 319 ASP A C   
1580  O O   . ASP A 96  ? 0.3066 0.2037 0.2160 -0.0096 0.0880  -0.0269 319 ASP A O   
1581  C CB  . ASP A 96  ? 0.3708 0.2587 0.2398 0.0060  0.0650  -0.0213 319 ASP A CB  
1582  C CG  . ASP A 96  ? 0.3866 0.2860 0.2605 -0.0042 0.0759  -0.0228 319 ASP A CG  
1583  O OD1 . ASP A 96  ? 0.3886 0.2902 0.2604 -0.0029 0.0834  -0.0339 319 ASP A OD1 
1584  O OD2 . ASP A 96  ? 0.4003 0.3072 0.2911 -0.0126 0.0703  -0.0182 319 ASP A OD2 
1589  N N   . VAL A 97  ? 0.2360 0.1694 0.1924 0.0077  0.0374  -0.0035 320 VAL A N   
1590  C CA  A VAL A 97  ? 0.2000 0.1524 0.1953 0.0156  0.0229  0.0120  320 VAL A CA  
1591  C CA  B VAL A 97  ? 0.1955 0.1527 0.1901 0.0115  0.0240  0.0142  320 VAL A CA  
1592  C C   . VAL A 97  ? 0.1590 0.1319 0.1554 0.0027  -0.0121 0.0167  320 VAL A C   
1593  O O   . VAL A 97  ? 0.1778 0.1445 0.1370 0.0205  -0.0260 0.0115  320 VAL A O   
1594  C CB  A VAL A 97  ? 0.2020 0.1683 0.2471 0.0427  0.0171  0.0159  320 VAL A CB  
1595  C CB  B VAL A 97  ? 0.1884 0.1600 0.2305 0.0266  0.0310  0.0226  320 VAL A CB  
1596  C CG1 A VAL A 97  ? 0.2087 0.1813 0.2521 0.0535  0.0117  0.0270  320 VAL A CG1 
1597  C CG1 B VAL A 97  ? 0.2022 0.1613 0.2418 0.0224  0.0425  0.0160  320 VAL A CG1 
1598  C CG2 A VAL A 97  ? 0.2097 0.1645 0.2672 0.0486  0.0181  0.0101  320 VAL A CG2 
1599  C CG2 B VAL A 97  ? 0.1673 0.1650 0.2352 0.0416  0.0189  0.0375  320 VAL A CG2 
1618  N N   . PRO A 98  ? 0.1025 0.1012 0.1445 -0.0019 -0.0243 0.0227  321 PRO A N   
1619  C CA  . PRO A 98  ? 0.0975 0.0825 0.1281 -0.0040 -0.0279 0.0172  321 PRO A CA  
1620  C C   . PRO A 98  ? 0.0983 0.0904 0.1216 -0.0007 -0.0466 -0.0035 321 PRO A C   
1621  O O   . PRO A 98  ? 0.1038 0.0911 0.1286 0.0001  -0.0390 0.0191  321 PRO A O   
1622  C CB  . PRO A 98  ? 0.0948 0.0918 0.1416 -0.0187 -0.0320 -0.0007 321 PRO A CB  
1623  C CG  . PRO A 98  ? 0.0933 0.1011 0.1592 -0.0007 -0.0366 0.0192  321 PRO A CG  
1624  C CD  . PRO A 98  ? 0.0940 0.1097 0.1465 -0.0057 -0.0372 0.0193  321 PRO A CD  
1632  N N   . ALA A 99  ? 0.0922 0.0850 0.1121 0.0116  -0.0345 0.0112  322 ALA A N   
1633  C CA  . ALA A 99  ? 0.0705 0.0873 0.1168 0.0026  -0.0359 0.0096  322 ALA A CA  
1634  C C   . ALA A 99  ? 0.0802 0.0866 0.0950 -0.0034 -0.0278 -0.0031 322 ALA A C   
1635  O O   . ALA A 99  ? 0.0956 0.0861 0.0958 0.0021  -0.0236 0.0047  322 ALA A O   
1636  C CB  . ALA A 99  ? 0.0701 0.0763 0.1306 0.0055  -0.0241 0.0051  322 ALA A CB  
1642  N N   . PRO A 100 ? 0.0688 0.0758 0.1131 0.0003  -0.0267 -0.0078 323 PRO A N   
1643  C CA  . PRO A 100 ? 0.0855 0.0733 0.1073 -0.0030 -0.0145 -0.0070 323 PRO A CA  
1644  C C   . PRO A 100 ? 0.0752 0.0680 0.1046 0.0145  -0.0144 -0.0007 323 PRO A C   
1645  O O   . PRO A 100 ? 0.0709 0.0779 0.1171 0.0081  -0.0249 -0.0206 323 PRO A O   
1646  C CB  . PRO A 100 ? 0.0871 0.0829 0.1102 -0.0083 -0.0277 -0.0009 323 PRO A CB  
1647  C CG  . PRO A 100 ? 0.0793 0.0839 0.1143 -0.0170 -0.0185 -0.0080 323 PRO A CG  
1648  C CD  . PRO A 100 ? 0.0777 0.0888 0.1238 -0.0042 -0.0295 -0.0174 323 PRO A CD  
1656  N N   . LEU A 101 ? 0.0860 0.0637 0.0847 0.0230  -0.0126 -0.0152 324 LEU A N   
1657  C CA  . LEU A 101 ? 0.0782 0.0865 0.0962 0.0119  -0.0234 -0.0058 324 LEU A CA  
1658  C C   . LEU A 101 ? 0.0756 0.0711 0.0954 0.0103  -0.0307 0.0157  324 LEU A C   
1659  O O   . LEU A 101 ? 0.1013 0.0816 0.1093 -0.0028 -0.0251 -0.0027 324 LEU A O   
1660  C CB  . LEU A 101 ? 0.0984 0.1013 0.1059 0.0233  -0.0258 -0.0145 324 LEU A CB  
1661  C CG  . LEU A 101 ? 0.1095 0.1033 0.0925 0.0265  -0.0108 -0.0130 324 LEU A CG  
1662  C CD1 . LEU A 101 ? 0.1264 0.1136 0.0879 0.0163  -0.0082 -0.0244 324 LEU A CD1 
1663  C CD2 . LEU A 101 ? 0.1073 0.1093 0.0921 0.0185  -0.0100 -0.0133 324 LEU A CD2 
1675  N N   . GLY A 102 ? 0.0719 0.0695 0.1057 0.0052  -0.0263 -0.0002 325 GLY A N   
1676  C CA  . GLY A 102 ? 0.0635 0.0760 0.0948 -0.0046 -0.0259 0.0129  325 GLY A CA  
1677  C C   . GLY A 102 ? 0.0698 0.0669 0.1051 -0.0101 -0.0258 -0.0028 325 GLY A C   
1678  O O   . GLY A 102 ? 0.0686 0.0762 0.1110 0.0091  -0.0246 0.0021  325 GLY A O   
1682  N N   . THR A 103 ? 0.0641 0.0621 0.0967 -0.0010 -0.0242 -0.0124 326 THR A N   
1683  C CA  . THR A 103 ? 0.0563 0.0749 0.1039 0.0102  -0.0249 0.0011  326 THR A CA  
1684  C C   . THR A 103 ? 0.0562 0.0622 0.0926 0.0036  -0.0206 0.0007  326 THR A C   
1685  O O   . THR A 103 ? 0.0623 0.0690 0.0931 -0.0031 -0.0259 0.0008  326 THR A O   
1686  C CB  . THR A 103 ? 0.0610 0.0761 0.1038 0.0031  -0.0238 0.0078  326 THR A CB  
1687  O OG1 . THR A 103 ? 0.0769 0.0785 0.1145 -0.0101 -0.0313 -0.0034 326 THR A OG1 
1688  C CG2 . THR A 103 ? 0.0685 0.0762 0.0989 -0.0086 -0.0191 -0.0058 326 THR A CG2 
1696  N N   . PRO A 104 ? 0.0484 0.0641 0.1061 -0.0049 -0.0140 -0.0001 327 PRO A N   
1697  C CA  A PRO A 104 ? 0.0562 0.0669 0.1080 -0.0022 -0.0247 -0.0031 327 PRO A CA  
1698  C CA  B PRO A 104 ? 0.0517 0.0670 0.1158 -0.0025 -0.0135 -0.0005 327 PRO A CA  
1699  C C   . PRO A 104 ? 0.0586 0.0728 0.1089 -0.0029 -0.0302 0.0029  327 PRO A C   
1700  O O   . PRO A 104 ? 0.0748 0.0664 0.1135 -0.0133 -0.0351 -0.0002 327 PRO A O   
1701  C CB  A PRO A 104 ? 0.0734 0.0732 0.0902 -0.0065 -0.0243 -0.0019 327 PRO A CB  
1702  C CB  B PRO A 104 ? 0.0587 0.0725 0.1152 -0.0068 0.0088  0.0057  327 PRO A CB  
1703  C CG  A PRO A 104 ? 0.0804 0.0787 0.0757 -0.0052 -0.0318 -0.0134 327 PRO A CG  
1704  C CG  B PRO A 104 ? 0.0599 0.0811 0.1105 -0.0087 0.0198  0.0006  327 PRO A CG  
1705  C CD  A PRO A 104 ? 0.0680 0.0737 0.0894 -0.0092 -0.0181 -0.0032 327 PRO A CD  
1706  C CD  B PRO A 104 ? 0.0595 0.0759 0.1068 -0.0124 0.0071  0.0027  327 PRO A CD  
1721  N N   . ASP A 105 ? 0.0597 0.0744 0.0905 -0.0155 -0.0335 0.0053  328 ASP A N   
1722  C CA  . ASP A 105 ? 0.0752 0.0718 0.0820 -0.0118 -0.0190 0.0016  328 ASP A CA  
1723  C C   . ASP A 105 ? 0.0782 0.0707 0.0844 -0.0075 -0.0142 0.0079  328 ASP A C   
1724  O O   . ASP A 105 ? 0.0831 0.0647 0.1123 -0.0038 0.0046  0.0116  328 ASP A O   
1725  C CB  . ASP A 105 ? 0.0668 0.0679 0.0835 0.0001  -0.0299 -0.0019 328 ASP A CB  
1726  C CG  . ASP A 105 ? 0.0696 0.0688 0.1019 -0.0003 -0.0049 -0.0044 328 ASP A CG  
1727  O OD1 . ASP A 105 ? 0.0669 0.0680 0.0834 -0.0081 -0.0196 0.0041  328 ASP A OD1 
1728  O OD2 . ASP A 105 ? 0.0727 0.0853 0.0930 -0.0131 -0.0099 0.0025  328 ASP A OD2 
1733  N N   . PHE A 106 ? 0.0615 0.0663 0.1017 -0.0009 -0.0149 0.0108  329 PHE A N   
1734  C CA  . PHE A 106 ? 0.0625 0.0581 0.1042 -0.0081 -0.0128 0.0046  329 PHE A CA  
1735  C C   . PHE A 106 ? 0.0659 0.0577 0.1078 -0.0081 -0.0027 0.0131  329 PHE A C   
1736  O O   . PHE A 106 ? 0.0780 0.0629 0.1218 0.0057  -0.0116 0.0091  329 PHE A O   
1737  C CB  . PHE A 106 ? 0.0864 0.0589 0.1217 0.0037  -0.0115 -0.0024 329 PHE A CB  
1738  C CG  . PHE A 106 ? 0.0847 0.0726 0.1070 0.0022  -0.0120 -0.0051 329 PHE A CG  
1739  C CD1 . PHE A 106 ? 0.1002 0.0928 0.1122 0.0044  -0.0144 0.0065  329 PHE A CD1 
1740  C CD2 . PHE A 106 ? 0.1040 0.0756 0.1074 -0.0051 -0.0263 0.0040  329 PHE A CD2 
1741  C CE1 . PHE A 106 ? 0.1143 0.1207 0.1080 -0.0086 -0.0049 0.0006  329 PHE A CE1 
1742  C CE2 . PHE A 106 ? 0.1331 0.0963 0.1133 -0.0039 -0.0278 0.0084  329 PHE A CE2 
1743  C CZ  . PHE A 106 ? 0.1354 0.0982 0.1076 -0.0056 -0.0068 0.0152  329 PHE A CZ  
1753  N N   . ARG A 107 ? 0.0627 0.0619 0.1267 -0.0034 -0.0106 0.0175  330 ARG A N   
1754  C CA  . ARG A 107 ? 0.0704 0.0633 0.1032 0.0123  -0.0178 0.0146  330 ARG A CA  
1755  C C   . ARG A 107 ? 0.0870 0.0694 0.0949 0.0033  -0.0249 0.0099  330 ARG A C   
1756  O O   . ARG A 107 ? 0.1011 0.0827 0.0982 -0.0059 -0.0164 0.0096  330 ARG A O   
1757  C CB  . ARG A 107 ? 0.0750 0.0764 0.1193 0.0047  -0.0136 0.0061  330 ARG A CB  
1758  C CG  . ARG A 107 ? 0.1060 0.0769 0.1226 -0.0036 -0.0170 0.0137  330 ARG A CG  
1759  C CD  . ARG A 107 ? 0.1185 0.1090 0.1406 0.0234  -0.0225 0.0495  330 ARG A CD  
1760  N NE  . ARG A 107 ? 0.1404 0.1434 0.1873 0.0155  -0.0255 0.0608  330 ARG A NE  
1761  C CZ  . ARG A 107 ? 0.1693 0.1483 0.1883 0.0156  -0.0034 0.0484  330 ARG A CZ  
1762  N NH1 . ARG A 107 ? 0.1800 0.1472 0.1608 0.0082  -0.0090 0.0217  330 ARG A NH1 
1763  N NH2 . ARG A 107 ? 0.2016 0.1476 0.1902 0.0026  0.0168  0.0601  330 ARG A NH2 
1777  N N   . GLY A 108 ? 0.0889 0.0668 0.0989 -0.0091 -0.0198 0.0042  331 GLY A N   
1778  C CA  . GLY A 108 ? 0.0990 0.0776 0.1130 -0.0059 -0.0111 0.0069  331 GLY A CA  
1779  C C   . GLY A 108 ? 0.0874 0.0738 0.0982 -0.0054 -0.0207 0.0006  331 GLY A C   
1780  O O   . GLY A 108 ? 0.0975 0.0923 0.1013 -0.0151 -0.0128 0.0074  331 GLY A O   
1784  N N   . GLN A 109 ? 0.0741 0.0725 0.0950 -0.0020 -0.0090 0.0117  332 GLN A N   
1785  C CA  . GLN A 109 ? 0.0720 0.0750 0.1040 0.0032  -0.0158 0.0076  332 GLN A CA  
1786  C C   . GLN A 109 ? 0.0664 0.0632 0.0938 -0.0002 -0.0242 0.0091  332 GLN A C   
1787  O O   . GLN A 109 ? 0.0746 0.0859 0.1010 0.0033  -0.0219 0.0030  332 GLN A O   
1788  C CB  . GLN A 109 ? 0.0745 0.0886 0.1305 -0.0024 -0.0057 0.0108  332 GLN A CB  
1789  C CG  . GLN A 109 ? 0.0871 0.1021 0.1472 0.0323  -0.0061 0.0236  332 GLN A CG  
1790  C CD  . GLN A 109 ? 0.1324 0.1014 0.1566 0.0194  -0.0317 0.0299  332 GLN A CD  
1791  O OE1 . GLN A 109 ? 0.1511 0.1224 0.1720 -0.0215 -0.0346 0.0344  332 GLN A OE1 
1792  N NE2 . GLN A 109 ? 0.2077 0.1189 0.1580 -0.0162 -0.0290 0.0246  332 GLN A NE2 
1801  N N   . LEU A 110 ? 0.0729 0.0562 0.0915 -0.0017 -0.0288 0.0126  333 LEU A N   
1802  C CA  . LEU A 110 ? 0.0700 0.0622 0.1018 0.0008  -0.0139 0.0045  333 LEU A CA  
1803  C C   . LEU A 110 ? 0.0777 0.0715 0.0936 -0.0030 -0.0312 0.0059  333 LEU A C   
1804  O O   . LEU A 110 ? 0.0696 0.0997 0.1295 -0.0190 -0.0309 0.0232  333 LEU A O   
1805  C CB  . LEU A 110 ? 0.0739 0.0759 0.1169 -0.0130 -0.0013 0.0218  333 LEU A CB  
1806  C CG  . LEU A 110 ? 0.0769 0.1004 0.1106 0.0089  -0.0187 0.0240  333 LEU A CG  
1807  C CD1 . LEU A 110 ? 0.0727 0.1181 0.1352 0.0114  -0.0097 0.0112  333 LEU A CD1 
1808  C CD2 . LEU A 110 ? 0.0883 0.1168 0.1382 0.0069  -0.0222 0.0078  333 LEU A CD2 
1820  N N   . TYR A 111 ? 0.0736 0.0527 0.0915 -0.0067 -0.0256 0.0102  334 TYR A N   
1821  C CA  . TYR A 111 ? 0.0819 0.0509 0.1053 0.0033  -0.0116 0.0137  334 TYR A CA  
1822  C C   . TYR A 111 ? 0.0608 0.0489 0.0759 -0.0059 -0.0203 -0.0040 334 TYR A C   
1823  O O   . TYR A 111 ? 0.0713 0.0524 0.0930 -0.0042 -0.0104 0.0022  334 TYR A O   
1824  C CB  . TYR A 111 ? 0.0859 0.0492 0.1239 -0.0018 -0.0109 0.0086  334 TYR A CB  
1825  C CG  . TYR A 111 ? 0.0756 0.0386 0.1164 0.0024  -0.0109 -0.0045 334 TYR A CG  
1826  C CD1 . TYR A 111 ? 0.0844 0.0491 0.1162 -0.0004 -0.0132 -0.0071 334 TYR A CD1 
1827  C CD2 . TYR A 111 ? 0.0606 0.0665 0.1140 0.0094  -0.0225 -0.0020 334 TYR A CD2 
1828  C CE1 . TYR A 111 ? 0.0829 0.0556 0.1183 0.0068  -0.0110 -0.0012 334 TYR A CE1 
1829  C CE2 . TYR A 111 ? 0.0637 0.0841 0.1197 0.0190  -0.0245 -0.0036 334 TYR A CE2 
1830  C CZ  . TYR A 111 ? 0.0766 0.0727 0.1151 0.0184  -0.0102 -0.0010 334 TYR A CZ  
1831  O OH  . TYR A 111 ? 0.0778 0.0901 0.1001 0.0093  -0.0135 0.0000  334 TYR A OH  
1841  N N   . GLY A 112 ? 0.0555 0.0539 0.0862 0.0015  -0.0093 0.0041  335 GLY A N   
1842  C CA  . GLY A 112 ? 0.0621 0.0564 0.0829 -0.0010 -0.0160 -0.0053 335 GLY A CA  
1843  C C   . GLY A 112 ? 0.0488 0.0564 0.1115 0.0092  -0.0102 0.0097  335 GLY A C   
1844  O O   . GLY A 112 ? 0.0615 0.0548 0.1052 -0.0003 -0.0034 0.0081  335 GLY A O   
1848  N N   . VAL A 113 ? 0.0483 0.0431 0.0985 -0.0022 -0.0112 0.0013  336 VAL A N   
1849  C CA  . VAL A 113 ? 0.0553 0.0474 0.0986 -0.0036 0.0007  0.0035  336 VAL A CA  
1850  C C   . VAL A 113 ? 0.0476 0.0576 0.0896 -0.0014 -0.0019 -0.0002 336 VAL A C   
1851  O O   . VAL A 113 ? 0.0477 0.0577 0.1027 -0.0054 -0.0066 -0.0015 336 VAL A O   
1852  C CB  . VAL A 113 ? 0.0601 0.0571 0.0944 0.0042  -0.0156 0.0042  336 VAL A CB  
1853  C CG1 . VAL A 113 ? 0.0706 0.0518 0.0927 0.0068  -0.0065 0.0084  336 VAL A CG1 
1854  C CG2 . VAL A 113 ? 0.1176 0.0707 0.1086 0.0161  -0.0084 -0.0038 336 VAL A CG2 
1864  N N   . ILE A 114 ? 0.0526 0.0465 0.0884 -0.0027 0.0056  -0.0096 337 ILE A N   
1865  C CA  . ILE A 114 ? 0.0665 0.0577 0.0826 -0.0014 -0.0009 -0.0006 337 ILE A CA  
1866  C C   . ILE A 114 ? 0.0485 0.0641 0.0673 -0.0051 -0.0077 0.0032  337 ILE A C   
1867  O O   . ILE A 114 ? 0.0694 0.0532 0.0754 -0.0040 -0.0028 -0.0025 337 ILE A O   
1868  C CB  . ILE A 114 ? 0.0577 0.0813 0.0971 -0.0039 -0.0118 -0.0094 337 ILE A CB  
1869  C CG1 . ILE A 114 ? 0.0679 0.0875 0.0991 -0.0040 -0.0364 -0.0211 337 ILE A CG1 
1870  C CG2 . ILE A 114 ? 0.0608 0.0925 0.1283 -0.0042 -0.0181 0.0090  337 ILE A CG2 
1871  C CD1 . ILE A 114 ? 0.0880 0.0928 0.1117 0.0052  -0.0317 -0.0195 337 ILE A CD1 
1883  N N   . SER A 115 ? 0.0560 0.0553 0.0742 0.0070  -0.0085 0.0075  338 SER A N   
1884  C CA  A SER A 115 ? 0.0515 0.0617 0.0880 -0.0020 -0.0086 -0.0013 338 SER A CA  
1885  C CA  B SER A 115 ? 0.0476 0.0555 0.0868 -0.0062 -0.0086 0.0027  338 SER A CA  
1886  C C   . SER A 115 ? 0.0484 0.0628 0.0807 -0.0044 -0.0135 0.0078  338 SER A C   
1887  O O   . SER A 115 ? 0.0919 0.0736 0.0781 -0.0283 0.0030  0.0083  338 SER A O   
1888  C CB  A SER A 115 ? 0.0647 0.0724 0.0767 0.0072  -0.0035 -0.0049 338 SER A CB  
1889  C CB  B SER A 115 ? 0.0568 0.0553 0.0742 -0.0024 -0.0025 0.0083  338 SER A CB  
1890  O OG  A SER A 115 ? 0.0703 0.0852 0.0754 0.0089  -0.0042 -0.0131 338 SER A OG  
1891  O OG  B SER A 115 ? 0.0563 0.0683 0.0780 -0.0036 -0.0066 -0.0043 338 SER A OG  
1902  N N   . GLN A 116 ? 0.0735 0.0633 0.0722 -0.0171 -0.0024 0.0043  339 GLN A N   
1903  C CA  . GLN A 116 ? 0.0558 0.0588 0.0772 -0.0118 -0.0103 -0.0012 339 GLN A CA  
1904  C C   . GLN A 116 ? 0.0665 0.0657 0.0883 -0.0176 -0.0131 0.0008  339 GLN A C   
1905  O O   . GLN A 116 ? 0.0591 0.0639 0.0900 -0.0191 -0.0116 -0.0005 339 GLN A O   
1906  C CB  . GLN A 116 ? 0.0745 0.0620 0.0916 -0.0168 -0.0086 0.0107  339 GLN A CB  
1907  C CG  . GLN A 116 ? 0.0706 0.0714 0.1015 -0.0053 -0.0170 0.0128  339 GLN A CG  
1908  C CD  . GLN A 116 ? 0.0599 0.0867 0.1146 -0.0072 -0.0198 0.0245  339 GLN A CD  
1909  O OE1 . GLN A 116 ? 0.0625 0.0988 0.1213 -0.0173 -0.0239 0.0249  339 GLN A OE1 
1910  N NE2 . GLN A 116 ? 0.0380 0.0942 0.1133 -0.0105 -0.0197 0.0188  339 GLN A NE2 
1919  N N   . ARG A 117 ? 0.0784 0.0529 0.0840 -0.0122 -0.0027 0.0082  340 ARG A N   
1920  C CA  . ARG A 117 ? 0.0759 0.0640 0.0934 -0.0112 -0.0126 0.0044  340 ARG A CA  
1921  C C   . ARG A 117 ? 0.0837 0.0614 0.0885 -0.0109 -0.0049 0.0002  340 ARG A C   
1922  O O   . ARG A 117 ? 0.1008 0.0714 0.0898 -0.0163 0.0000  0.0027  340 ARG A O   
1923  C CB  . ARG A 117 ? 0.0839 0.0648 0.0928 -0.0053 -0.0066 0.0106  340 ARG A CB  
1924  C CG  . ARG A 117 ? 0.1003 0.0716 0.1151 0.0036  -0.0139 -0.0034 340 ARG A CG  
1925  C CD  . ARG A 117 ? 0.1175 0.1011 0.1159 0.0069  -0.0243 -0.0145 340 ARG A CD  
1926  N NE  . ARG A 117 ? 0.1103 0.1041 0.1179 -0.0177 -0.0149 -0.0047 340 ARG A NE  
1927  C CZ  . ARG A 117 ? 0.0952 0.0953 0.1425 -0.0108 0.0033  0.0170  340 ARG A CZ  
1928  N NH1 . ARG A 117 ? 0.1228 0.1292 0.1740 -0.0278 0.0398  -0.0065 340 ARG A NH1 
1929  N NH2 . ARG A 117 ? 0.0750 0.0898 0.1316 -0.0127 -0.0141 0.0066  340 ARG A NH2 
1943  N N   . ASP A 118 ? 0.0878 0.0693 0.0967 -0.0207 -0.0131 0.0091  341 ASP A N   
1944  C CA  . ASP A 118 ? 0.0910 0.0786 0.1005 -0.0375 -0.0268 -0.0007 341 ASP A CA  
1945  C C   . ASP A 118 ? 0.1142 0.0739 0.1041 -0.0141 -0.0235 -0.0103 341 ASP A C   
1946  O O   . ASP A 118 ? 0.1246 0.0789 0.1058 0.0027  -0.0104 -0.0121 341 ASP A O   
1947  C CB  . ASP A 118 ? 0.1214 0.1538 0.1164 -0.0477 -0.0297 0.0116  341 ASP A CB  
1948  C CG  . ASP A 118 ? 0.1047 0.2128 0.1276 -0.0383 -0.0148 0.0117  341 ASP A CG  
1949  O OD1 . ASP A 118 ? 0.1419 0.2546 0.1414 0.0122  0.0028  -0.0286 341 ASP A OD1 
1950  O OD2 . ASP A 118 ? 0.1580 0.2727 0.1712 -0.0224 -0.0200 0.0084  341 ASP A OD2 
1955  N N   . ARG A 119 ? 0.1399 0.0895 0.1015 -0.0050 -0.0229 -0.0129 342 ARG A N   
1956  C CA  . ARG A 119 ? 0.1640 0.1141 0.1193 -0.0056 -0.0126 -0.0326 342 ARG A CA  
1957  C C   . ARG A 119 ? 0.1916 0.1207 0.1387 -0.0064 0.0077  -0.0329 342 ARG A C   
1958  O O   . ARG A 119 ? 0.2133 0.1253 0.1806 0.0053  0.0246  -0.0158 342 ARG A O   
1959  C CB  . ARG A 119 ? 0.1950 0.1511 0.1410 0.0101  -0.0046 -0.0402 342 ARG A CB  
1960  C CG  . ARG A 119 ? 0.2098 0.1691 0.1375 0.0082  -0.0055 -0.0277 342 ARG A CG  
1961  C CD  . ARG A 119 ? 0.1981 0.1636 0.1112 0.0204  -0.0464 -0.0218 342 ARG A CD  
1962  N NE  . ARG A 119 ? 0.1874 0.1644 0.1355 0.0147  -0.0493 -0.0406 342 ARG A NE  
1963  C CZ  . ARG A 119 ? 0.1813 0.1405 0.1287 0.0075  -0.0621 -0.0337 342 ARG A CZ  
1964  N NH1 . ARG A 119 ? 0.1725 0.1439 0.1170 0.0149  -0.0596 -0.0060 342 ARG A NH1 
1965  N NH2 . ARG A 119 ? 0.2024 0.1366 0.1616 0.0020  -0.0300 -0.0484 342 ARG A NH2 
1979  N N   . GLU A 120 ? 0.1940 0.1198 0.1246 -0.0201 0.0173  -0.0360 343 GLU A N   
1980  C CA  . GLU A 120 ? 0.1938 0.1360 0.1533 -0.0343 0.0227  -0.0329 343 GLU A CA  
1981  C C   . GLU A 120 ? 0.1698 0.1131 0.1170 -0.0204 0.0120  -0.0188 343 GLU A C   
1982  O O   . GLU A 120 ? 0.1686 0.1246 0.1165 -0.0112 0.0064  -0.0158 343 GLU A O   
1994  N N   . GLY A 121 ? 0.1665 0.1078 0.1388 -0.0118 0.0460  -0.0120 344 GLY A N   
1995  C CA  . GLY A 121 ? 0.1406 0.1102 0.1399 -0.0287 0.0139  -0.0018 344 GLY A CA  
1996  C C   . GLY A 121 ? 0.1386 0.1221 0.1245 -0.0327 -0.0084 -0.0108 344 GLY A C   
1997  O O   . GLY A 121 ? 0.1628 0.1546 0.1236 -0.0501 -0.0208 -0.0044 344 GLY A O   
2001  N N   . THR A 122 ? 0.1239 0.1087 0.1133 -0.0147 0.0007  0.0058  345 THR A N   
2002  C CA  . THR A 122 ? 0.0968 0.1096 0.1428 -0.0299 -0.0106 0.0069  345 THR A CA  
2003  C C   . THR A 122 ? 0.0916 0.1123 0.1341 -0.0286 -0.0251 0.0049  345 THR A C   
2004  O O   . THR A 122 ? 0.1121 0.1235 0.1276 -0.0354 -0.0006 0.0016  345 THR A O   
2005  C CB  . THR A 122 ? 0.1135 0.0980 0.1364 -0.0309 -0.0077 0.0252  345 THR A CB  
2006  O OG1 . THR A 122 ? 0.1196 0.1049 0.1414 -0.0331 0.0071  0.0297  345 THR A OG1 
2007  C CG2 . THR A 122 ? 0.1235 0.0926 0.1419 -0.0124 -0.0017 0.0319  345 THR A CG2 
2015  N N   . PRO A 123 ? 0.1278 0.1162 0.1354 -0.0330 -0.0405 0.0082  346 PRO A N   
2016  C CA  A PRO A 123 ? 0.1542 0.1142 0.1507 -0.0309 -0.0317 0.0041  346 PRO A CA  
2017  C CA  B PRO A 123 ? 0.1453 0.1152 0.1471 -0.0297 -0.0360 -0.0015 346 PRO A CA  
2018  C C   . PRO A 123 ? 0.1379 0.0977 0.1442 -0.0242 -0.0418 0.0044  346 PRO A C   
2019  O O   . PRO A 123 ? 0.1729 0.1064 0.1545 0.0042  -0.0210 0.0141  346 PRO A O   
2020  C CB  A PRO A 123 ? 0.1752 0.1326 0.1595 -0.0329 -0.0189 0.0097  346 PRO A CB  
2021  C CB  B PRO A 123 ? 0.1472 0.1344 0.1499 -0.0302 -0.0352 -0.0077 346 PRO A CB  
2022  C CG  A PRO A 123 ? 0.1701 0.1374 0.1603 -0.0302 -0.0194 0.0222  346 PRO A CG  
2023  C CG  B PRO A 123 ? 0.1220 0.1389 0.1442 -0.0282 -0.0529 -0.0073 346 PRO A CG  
2024  C CD  A PRO A 123 ? 0.1432 0.1299 0.1368 -0.0365 -0.0404 0.0170  346 PRO A CD  
2025  C CD  B PRO A 123 ? 0.1247 0.1298 0.1424 -0.0353 -0.0437 0.0031  346 PRO A CD  
2040  N N   . SER A 124 ? 0.1165 0.0949 0.1554 -0.0320 -0.0277 0.0275  347 SER A N   
2041  C CA  . SER A 124 ? 0.1211 0.1034 0.1581 -0.0244 -0.0017 0.0317  347 SER A CA  
2042  C C   . SER A 124 ? 0.1190 0.1054 0.1485 -0.0074 0.0091  0.0332  347 SER A C   
2043  O O   . SER A 124 ? 0.1122 0.1154 0.1568 0.0056  0.0033  0.0452  347 SER A O   
2044  C CB  . SER A 124 ? 0.1253 0.1329 0.1802 -0.0037 0.0003  0.0614  347 SER A CB  
2045  O OG  . SER A 124 ? 0.1226 0.1380 0.1894 -0.0003 0.0134  0.0653  347 SER A OG  
2051  N N   . GLU A 125 ? 0.0992 0.0811 0.1379 -0.0098 -0.0142 0.0178  348 GLU A N   
2052  C CA  . GLU A 125 ? 0.1075 0.0877 0.1436 -0.0016 -0.0192 0.0245  348 GLU A CA  
2053  C C   . GLU A 125 ? 0.1099 0.0921 0.1380 -0.0115 -0.0065 0.0085  348 GLU A C   
2054  O O   . GLU A 125 ? 0.1100 0.1113 0.1562 -0.0228 0.0026  -0.0128 348 GLU A O   
2055  C CB  . GLU A 125 ? 0.1084 0.0943 0.1510 -0.0072 -0.0177 0.0319  348 GLU A CB  
2056  C CG  . GLU A 125 ? 0.1211 0.1049 0.1409 -0.0144 -0.0035 0.0192  348 GLU A CG  
2057  C CD  . GLU A 125 ? 0.1273 0.1104 0.1377 -0.0231 0.0102  0.0185  348 GLU A CD  
2058  O OE1 . GLU A 125 ? 0.1106 0.1064 0.1514 -0.0142 -0.0027 0.0265  348 GLU A OE1 
2059  O OE2 . GLU A 125 ? 0.1459 0.1511 0.1528 -0.0242 0.0251  0.0232  348 GLU A OE2 
2066  N N   . ASN A 126 ? 0.1308 0.0929 0.1698 -0.0160 0.0092  0.0203  349 ASN A N   
2067  C CA  A ASN A 126 ? 0.1378 0.1103 0.1868 0.0001  0.0067  0.0159  349 ASN A CA  
2068  C CA  B ASN A 126 ? 0.1373 0.1153 0.1769 0.0035  0.0025  0.0082  349 ASN A CA  
2069  C C   . ASN A 126 ? 0.1250 0.0994 0.1730 -0.0047 0.0064  -0.0040 349 ASN A C   
2070  O O   . ASN A 126 ? 0.1541 0.1130 0.1936 0.0091  0.0179  -0.0012 349 ASN A O   
2071  C CB  A ASN A 126 ? 0.1724 0.1313 0.2163 0.0185  0.0150  0.0371  349 ASN A CB  
2072  C CB  B ASN A 126 ? 0.1753 0.1443 0.1853 0.0245  0.0079  0.0155  349 ASN A CB  
2073  C CG  A ASN A 126 ? 0.2149 0.1433 0.2483 0.0269  0.0302  0.0454  349 ASN A CG  
2074  C CG  B ASN A 126 ? 0.2214 0.1549 0.1993 0.0332  0.0242  0.0144  349 ASN A CG  
2075  O OD1 A ASN A 126 ? 0.2422 0.1344 0.2775 0.0222  0.0487  0.0573  349 ASN A OD1 
2076  O OD1 B ASN A 126 ? 0.2234 0.1674 0.1918 0.0309  0.0313  0.0206  349 ASN A OD1 
2077  N ND2 A ASN A 126 ? 0.2259 0.1564 0.2481 0.0519  0.0230  0.0597  349 ASN A ND2 
2078  N ND2 B ASN A 126 ? 0.2509 0.1549 0.2116 0.0308  0.0237  0.0127  349 ASN A ND2 
2091  N N   . ASN A 127 ? 0.1150 0.0740 0.1282 -0.0050 0.0107  -0.0062 350 ASN A N   
2092  C CA  . ASN A 127 ? 0.1177 0.0839 0.1383 -0.0121 0.0197  -0.0148 350 ASN A CA  
2093  C C   . ASN A 127 ? 0.0946 0.0757 0.1215 -0.0039 0.0104  -0.0199 350 ASN A C   
2094  O O   . ASN A 127 ? 0.1160 0.0960 0.1228 -0.0083 0.0194  -0.0299 350 ASN A O   
2095  C CB  . ASN A 127 ? 0.1978 0.1232 0.1725 -0.0199 0.0372  -0.0309 350 ASN A CB  
2096  C CG  . ASN A 127 ? 0.2777 0.1692 0.2290 0.0051  0.0430  -0.0222 350 ASN A CG  
2097  O OD1 . ASN A 127 ? 0.3253 0.2013 0.2354 0.0073  0.0195  -0.0152 350 ASN A OD1 
2098  N ND2 . ASN A 127 ? 0.3103 0.1954 0.2497 0.0095  0.0624  -0.0102 350 ASN A ND2 
2105  N N   . GLN A 128 ? 0.1092 0.0781 0.1334 -0.0066 0.0034  0.0050  351 GLN A N   
2106  C CA  . GLN A 128 ? 0.0926 0.0769 0.1201 -0.0026 0.0076  -0.0032 351 GLN A CA  
2107  C C   . GLN A 128 ? 0.0819 0.0711 0.1179 -0.0163 -0.0105 -0.0160 351 GLN A C   
2108  O O   . GLN A 128 ? 0.0839 0.0763 0.1470 -0.0126 -0.0158 -0.0148 351 GLN A O   
2109  C CB  . GLN A 128 ? 0.0821 0.0899 0.1204 -0.0090 -0.0042 0.0016  351 GLN A CB  
2110  C CG  . GLN A 128 ? 0.1018 0.1094 0.1425 -0.0100 -0.0080 -0.0046 351 GLN A CG  
2111  C CD  . GLN A 128 ? 0.1111 0.1318 0.1421 -0.0044 0.0058  -0.0047 351 GLN A CD  
2112  O OE1 . GLN A 128 ? 0.1375 0.1519 0.1391 -0.0123 0.0140  -0.0191 351 GLN A OE1 
2113  N NE2 . GLN A 128 ? 0.1215 0.1327 0.1593 -0.0078 -0.0037 -0.0092 351 GLN A NE2 
2122  N N   . LYS A 129 ? 0.0830 0.0602 0.1344 -0.0152 -0.0153 -0.0025 352 LYS A N   
2123  C CA  A LYS A 129 ? 0.0917 0.0625 0.1217 -0.0087 -0.0103 0.0007  352 LYS A CA  
2124  C CA  B LYS A 129 ? 0.0869 0.0649 0.1192 -0.0117 -0.0173 0.0025  352 LYS A CA  
2125  C C   . LYS A 129 ? 0.0720 0.0597 0.1134 -0.0152 -0.0293 0.0038  352 LYS A C   
2126  O O   . LYS A 129 ? 0.0683 0.0695 0.1174 -0.0128 -0.0035 -0.0020 352 LYS A O   
2127  C CB  A LYS A 129 ? 0.1009 0.0929 0.1240 0.0143  0.0107  -0.0092 352 LYS A CB  
2128  C CB  B LYS A 129 ? 0.0933 0.0876 0.1164 -0.0005 -0.0077 0.0009  352 LYS A CB  
2129  C CG  A LYS A 129 ? 0.1376 0.1076 0.1140 0.0225  0.0117  -0.0118 352 LYS A CG  
2130  C CG  B LYS A 129 ? 0.1159 0.1052 0.1211 0.0035  -0.0004 0.0046  352 LYS A CG  
2131  C CD  A LYS A 129 ? 0.1530 0.1325 0.1109 0.0303  0.0190  -0.0226 352 LYS A CD  
2132  C CD  B LYS A 129 ? 0.1367 0.1199 0.1192 -0.0109 -0.0070 -0.0039 352 LYS A CD  
2133  C CE  A LYS A 129 ? 0.1761 0.1582 0.1172 0.0328  0.0657  -0.0187 352 LYS A CE  
2134  C CE  B LYS A 129 ? 0.1599 0.1329 0.1286 -0.0288 0.0000  -0.0087 352 LYS A CE  
2135  N NZ  A LYS A 129 ? 0.2008 0.1752 0.1427 0.0211  0.0726  -0.0025 352 LYS A NZ  
2136  N NZ  B LYS A 129 ? 0.1878 0.1462 0.1426 -0.0390 0.0162  -0.0042 352 LYS A NZ  
2163  N N   . ALA A 130 ? 0.0785 0.0555 0.1010 -0.0284 -0.0165 0.0004  353 ALA A N   
2164  C CA  . ALA A 130 ? 0.0790 0.0604 0.1047 -0.0163 -0.0109 -0.0017 353 ALA A CA  
2165  C C   . ALA A 130 ? 0.0751 0.0697 0.0962 -0.0100 -0.0025 0.0055  353 ALA A C   
2166  O O   . ALA A 130 ? 0.0996 0.0629 0.0886 -0.0105 -0.0073 0.0021  353 ALA A O   
2167  C CB  . ALA A 130 ? 0.0839 0.0736 0.1086 -0.0119 -0.0030 0.0065  353 ALA A CB  
2173  N N   . ASN A 131 ? 0.0547 0.0574 0.1071 -0.0088 0.0026  -0.0030 354 ASN A N   
2174  C CA  . ASN A 131 ? 0.0522 0.0591 0.0944 -0.0151 -0.0005 0.0007  354 ASN A CA  
2175  C C   . ASN A 131 ? 0.0593 0.0653 0.0767 -0.0114 -0.0138 0.0024  354 ASN A C   
2176  O O   . ASN A 131 ? 0.0577 0.0663 0.0941 0.0005  0.0038  0.0062  354 ASN A O   
2177  C CB  . ASN A 131 ? 0.0458 0.0646 0.0932 -0.0113 0.0050  0.0060  354 ASN A CB  
2178  C CG  . ASN A 131 ? 0.0589 0.0684 0.0889 -0.0142 -0.0011 0.0095  354 ASN A CG  
2179  O OD1 . ASN A 131 ? 0.0585 0.0655 0.0933 -0.0070 -0.0017 0.0041  354 ASN A OD1 
2180  N ND2 . ASN A 131 ? 0.0675 0.0664 0.1096 -0.0085 0.0019  0.0154  354 ASN A ND2 
2187  N N   . ARG A 132 ? 0.0587 0.0442 0.0762 0.0028  -0.0009 0.0003  355 ARG A N   
2188  C CA  . ARG A 132 ? 0.0708 0.0553 0.0781 -0.0073 -0.0113 0.0054  355 ARG A CA  
2189  C C   . ARG A 132 ? 0.0734 0.0480 0.0818 0.0041  -0.0094 0.0049  355 ARG A C   
2190  O O   . ARG A 132 ? 0.0864 0.0573 0.0790 -0.0135 0.0038  0.0064  355 ARG A O   
2191  C CB  . ARG A 132 ? 0.0648 0.0677 0.1000 0.0001  -0.0165 0.0148  355 ARG A CB  
2192  C CG  . ARG A 132 ? 0.0769 0.0685 0.1094 -0.0018 -0.0138 0.0256  355 ARG A CG  
2193  C CD  . ARG A 132 ? 0.0842 0.0786 0.1060 -0.0069 -0.0282 0.0139  355 ARG A CD  
2194  N NE  . ARG A 132 ? 0.0951 0.0936 0.1236 -0.0213 -0.0292 0.0253  355 ARG A NE  
2195  C CZ  . ARG A 132 ? 0.1202 0.0954 0.1278 -0.0181 -0.0165 0.0171  355 ARG A CZ  
2196  N NH1 . ARG A 132 ? 0.1074 0.0859 0.1285 -0.0077 -0.0223 0.0088  355 ARG A NH1 
2197  N NH2 . ARG A 132 ? 0.1465 0.0974 0.1128 -0.0200 -0.0046 0.0126  355 ARG A NH2 
2211  N N   . SER A 133 ? 0.0689 0.0508 0.0762 -0.0087 -0.0108 0.0037  356 SER A N   
2212  C CA  . SER A 133 ? 0.0767 0.0537 0.0745 -0.0049 -0.0034 0.0041  356 SER A CA  
2213  C C   . SER A 133 ? 0.0611 0.0667 0.0635 -0.0022 -0.0102 0.0115  356 SER A C   
2214  O O   . SER A 133 ? 0.0613 0.0623 0.0766 -0.0053 -0.0056 0.0042  356 SER A O   
2215  C CB  . SER A 133 ? 0.0616 0.0583 0.0820 -0.0025 -0.0151 0.0161  356 SER A CB  
2216  O OG  . SER A 133 ? 0.0659 0.0675 0.1047 -0.0049 -0.0047 0.0098  356 SER A OG  
2222  N N   . HIS A 134 ? 0.0477 0.0556 0.0763 -0.0002 -0.0060 0.0105  357 HIS A N   
2223  C CA  . HIS A 134 ? 0.0458 0.0574 0.0748 0.0008  -0.0133 0.0119  357 HIS A CA  
2224  C C   . HIS A 134 ? 0.0536 0.0541 0.0784 -0.0019 -0.0090 -0.0005 357 HIS A C   
2225  O O   . HIS A 134 ? 0.0676 0.0594 0.0903 -0.0105 0.0034  -0.0009 357 HIS A O   
2226  C CB  . HIS A 134 ? 0.0661 0.0724 0.1065 0.0012  -0.0032 0.0034  357 HIS A CB  
2227  C CG  . HIS A 134 ? 0.0627 0.0760 0.1018 -0.0130 -0.0070 0.0086  357 HIS A CG  
2228  N ND1 . HIS A 134 ? 0.0526 0.0775 0.1217 -0.0122 -0.0038 0.0099  357 HIS A ND1 
2229  C CD2 . HIS A 134 ? 0.0673 0.0896 0.1279 -0.0019 -0.0174 0.0150  357 HIS A CD2 
2230  C CE1 . HIS A 134 ? 0.0604 0.0865 0.1261 -0.0130 -0.0245 0.0116  357 HIS A CE1 
2231  N NE2 . HIS A 134 ? 0.0690 0.0828 0.1476 -0.0170 -0.0258 0.0162  357 HIS A NE2 
2239  N N   . GLN A 135 ? 0.0685 0.0556 0.0837 -0.0023 0.0026  -0.0092 358 GLN A N   
2240  C CA  . GLN A 135 ? 0.0616 0.0467 0.1009 0.0107  0.0064  0.0028  358 GLN A CA  
2241  C C   . GLN A 135 ? 0.0438 0.0540 0.1099 0.0050  -0.0151 0.0056  358 GLN A C   
2242  O O   . GLN A 135 ? 0.0492 0.0761 0.1212 -0.0093 -0.0143 0.0051  358 GLN A O   
2243  C CB  . GLN A 135 ? 0.0731 0.0548 0.0944 -0.0045 0.0073  0.0029  358 GLN A CB  
2244  C CG  . GLN A 135 ? 0.0842 0.0710 0.1069 0.0011  0.0020  0.0024  358 GLN A CG  
2245  C CD  . GLN A 135 ? 0.0976 0.0759 0.0949 -0.0123 0.0106  0.0121  358 GLN A CD  
2246  O OE1 . GLN A 135 ? 0.1033 0.0625 0.1097 -0.0188 0.0117  -0.0109 358 GLN A OE1 
2247  N NE2 . GLN A 135 ? 0.1172 0.0816 0.1154 -0.0372 0.0242  -0.0117 358 GLN A NE2 
2256  N N   . GLY A 136 ? 0.0489 0.0644 0.1116 -0.0031 -0.0245 0.0271  359 GLY A N   
2257  C CA  . GLY A 136 ? 0.0731 0.0761 0.1274 -0.0174 -0.0295 0.0155  359 GLY A CA  
2258  C C   . GLY A 136 ? 0.0629 0.0715 0.1021 -0.0015 -0.0271 0.0123  359 GLY A C   
2259  O O   . GLY A 136 ? 0.0776 0.0706 0.1223 -0.0106 -0.0283 0.0201  359 GLY A O   
2263  N N   . VAL A 137 ? 0.0716 0.0670 0.1092 0.0008  -0.0246 0.0105  360 VAL A N   
2264  C CA  A VAL A 137 ? 0.0676 0.0667 0.1027 -0.0064 -0.0121 0.0047  360 VAL A CA  
2265  C CA  B VAL A 137 ? 0.0706 0.0672 0.0977 -0.0079 -0.0137 0.0093  360 VAL A CA  
2266  C C   . VAL A 137 ? 0.0766 0.0719 0.0992 -0.0084 -0.0092 0.0102  360 VAL A C   
2267  O O   . VAL A 137 ? 0.0890 0.0840 0.1024 -0.0209 -0.0210 0.0100  360 VAL A O   
2268  C CB  A VAL A 137 ? 0.0771 0.0730 0.1146 -0.0042 -0.0083 0.0126  360 VAL A CB  
2269  C CB  B VAL A 137 ? 0.0690 0.0652 0.0862 -0.0152 -0.0065 0.0115  360 VAL A CB  
2270  C CG1 A VAL A 137 ? 0.0760 0.0519 0.1226 -0.0141 -0.0354 0.0068  360 VAL A CG1 
2271  C CG1 B VAL A 137 ? 0.0736 0.0753 0.0910 -0.0266 0.0124  0.0045  360 VAL A CG1 
2272  C CG2 A VAL A 137 ? 0.1045 0.1046 0.1417 -0.0024 0.0058  0.0153  360 VAL A CG2 
2273  C CG2 B VAL A 137 ? 0.0698 0.0538 0.0781 -0.0132 -0.0132 0.0192  360 VAL A CG2 
2292  N N   . ILE A 138 ? 0.0568 0.0729 0.0982 0.0021  -0.0166 0.0169  361 ILE A N   
2293  C CA  . ILE A 138 ? 0.0720 0.0788 0.0846 0.0015  -0.0251 0.0211  361 ILE A CA  
2294  C C   . ILE A 138 ? 0.0737 0.0769 0.0842 -0.0044 -0.0229 0.0166  361 ILE A C   
2295  O O   . ILE A 138 ? 0.0965 0.0813 0.1114 -0.0077 -0.0301 0.0156  361 ILE A O   
2296  C CB  . ILE A 138 ? 0.0698 0.0849 0.1000 0.0016  -0.0243 0.0255  361 ILE A CB  
2297  C CG1 . ILE A 138 ? 0.0857 0.0910 0.1065 -0.0035 -0.0254 0.0038  361 ILE A CG1 
2298  C CG2 . ILE A 138 ? 0.0862 0.0925 0.1213 0.0016  -0.0093 0.0101  361 ILE A CG2 
2299  C CD1 . ILE A 138 ? 0.1060 0.1010 0.1045 -0.0038 -0.0238 0.0032  361 ILE A CD1 
2311  N N   . SER A 139 ? 0.0661 0.0790 0.0996 -0.0116 -0.0163 0.0206  362 SER A N   
2312  C CA  . SER A 139 ? 0.0753 0.0778 0.1110 -0.0044 -0.0090 0.0166  362 SER A CA  
2313  C C   . SER A 139 ? 0.0705 0.0787 0.1122 -0.0089 -0.0223 0.0127  362 SER A C   
2314  O O   . SER A 139 ? 0.0903 0.1001 0.1188 -0.0329 -0.0087 0.0112  362 SER A O   
2315  C CB  . SER A 139 ? 0.0801 0.0830 0.1273 -0.0036 -0.0203 0.0158  362 SER A CB  
2316  O OG  . SER A 139 ? 0.0950 0.0954 0.1550 0.0128  -0.0236 0.0306  362 SER A OG  
2322  N N   . THR A 140 ? 0.0607 0.0684 0.1038 0.0006  -0.0184 0.0108  363 THR A N   
2323  C CA  . THR A 140 ? 0.0536 0.0646 0.1183 -0.0050 -0.0188 0.0152  363 THR A CA  
2324  C C   . THR A 140 ? 0.0788 0.0768 0.1003 -0.0010 -0.0167 0.0067  363 THR A C   
2325  O O   . THR A 140 ? 0.1032 0.1041 0.1012 0.0033  -0.0022 0.0243  363 THR A O   
2326  C CB  . THR A 140 ? 0.0616 0.0641 0.1261 -0.0017 -0.0176 0.0038  363 THR A CB  
2327  O OG1 . THR A 140 ? 0.0680 0.0629 0.1289 -0.0019 -0.0227 -0.0018 363 THR A OG1 
2328  C CG2 . THR A 140 ? 0.0683 0.0755 0.1383 -0.0068 -0.0075 0.0132  363 THR A CG2 
2336  N N   . ILE A 141 ? 0.0860 0.0822 0.1155 0.0168  -0.0099 0.0270  364 ILE A N   
2337  C CA  . ILE A 141 ? 0.0917 0.1040 0.1559 0.0216  -0.0251 0.0236  364 ILE A CA  
2338  C C   . ILE A 141 ? 0.0894 0.1204 0.1455 0.0062  -0.0413 0.0157  364 ILE A C   
2339  O O   . ILE A 141 ? 0.1099 0.1234 0.1703 0.0062  -0.0565 0.0207  364 ILE A O   
2340  C CB  . ILE A 141 ? 0.1118 0.1031 0.1788 0.0108  -0.0208 0.0117  364 ILE A CB  
2341  C CG1 . ILE A 141 ? 0.1340 0.1088 0.1797 0.0212  -0.0145 0.0145  364 ILE A CG1 
2342  C CG2 . ILE A 141 ? 0.1082 0.0872 0.2096 0.0013  -0.0091 0.0209  364 ILE A CG2 
2343  C CD1 . ILE A 141 ? 0.1323 0.1173 0.1964 0.0363  -0.0019 0.0111  364 ILE A CD1 
2355  N N   . SER A 142 ? 0.0684 0.1299 0.1564 -0.0036 -0.0370 0.0369  365 SER A N   
2356  C CA  . SER A 142 ? 0.0755 0.1392 0.1470 -0.0175 -0.0263 0.0297  365 SER A CA  
2357  C C   . SER A 142 ? 0.0821 0.1201 0.1454 -0.0151 -0.0353 0.0309  365 SER A C   
2358  O O   . SER A 142 ? 0.0838 0.1015 0.1432 -0.0027 -0.0144 0.0328  365 SER A O   
2359  C CB  . SER A 142 ? 0.0839 0.1735 0.1509 -0.0350 -0.0146 0.0293  365 SER A CB  
2360  O OG  . SER A 142 ? 0.0883 0.1739 0.1759 -0.0339 -0.0283 0.0362  365 SER A OG  
2366  N N   . PRO A 143 ? 0.1008 0.1331 0.1555 0.0083  -0.0364 0.0145  366 PRO A N   
2367  C CA  A PRO A 143 ? 0.1089 0.1407 0.1583 0.0092  -0.0368 0.0151  366 PRO A CA  
2368  C CA  B PRO A 143 ? 0.1062 0.1434 0.1577 0.0089  -0.0488 0.0161  366 PRO A CA  
2369  C C   . PRO A 143 ? 0.0917 0.1356 0.1517 -0.0027 -0.0353 0.0156  366 PRO A C   
2370  O O   . PRO A 143 ? 0.1161 0.1305 0.1521 -0.0010 -0.0227 0.0291  366 PRO A O   
2371  C CB  A PRO A 143 ? 0.1347 0.1464 0.1817 0.0192  -0.0226 0.0140  366 PRO A CB  
2372  C CB  B PRO A 143 ? 0.1269 0.1541 0.1890 0.0186  -0.0524 0.0153  366 PRO A CB  
2373  C CG  A PRO A 143 ? 0.1287 0.1468 0.1892 0.0215  -0.0134 0.0194  366 PRO A CG  
2374  C CG  B PRO A 143 ? 0.1008 0.1602 0.1964 0.0108  -0.0661 0.0193  366 PRO A CG  
2375  C CD  A PRO A 143 ? 0.1119 0.1412 0.1792 0.0197  -0.0296 0.0206  366 PRO A CD  
2376  C CD  B PRO A 143 ? 0.0950 0.1538 0.1846 0.0114  -0.0603 0.0175  366 PRO A CD  
2391  N N   . LYS A 144 ? 0.0863 0.1270 0.1618 0.0030  -0.0180 0.0179  367 LYS A N   
2392  C CA  . LYS A 144 ? 0.0876 0.1192 0.1790 -0.0103 -0.0015 0.0267  367 LYS A CA  
2393  C C   . LYS A 144 ? 0.0923 0.0984 0.1318 -0.0099 -0.0170 0.0222  367 LYS A C   
2394  O O   . LYS A 144 ? 0.1008 0.0996 0.1271 -0.0081 -0.0258 0.0083  367 LYS A O   
2395  C CB  . LYS A 144 ? 0.1223 0.1563 0.2687 0.0055  0.0398  0.0268  367 LYS A CB  
2396  C CG  . LYS A 144 ? 0.1866 0.2107 0.3449 0.0222  0.0789  0.0216  367 LYS A CG  
2397  C CD  . LYS A 144 ? 0.2444 0.2616 0.3653 0.0464  0.0802  0.0256  367 LYS A CD  
2398  C CE  . LYS A 144 ? 0.3120 0.2984 0.4021 0.0433  0.1093  0.0222  367 LYS A CE  
2399  N NZ  . LYS A 144 ? 0.3709 0.3209 0.4214 0.0548  0.1233  0.0131  367 LYS A NZ  
2413  N N   . PHE A 145 ? 0.0891 0.0960 0.1116 -0.0048 -0.0107 0.0269  368 PHE A N   
2414  C CA  . PHE A 145 ? 0.0923 0.0826 0.1060 -0.0062 -0.0215 0.0241  368 PHE A CA  
2415  C C   . PHE A 145 ? 0.0777 0.0751 0.1071 -0.0167 -0.0265 0.0166  368 PHE A C   
2416  O O   . PHE A 145 ? 0.0925 0.0741 0.1088 -0.0207 -0.0128 0.0208  368 PHE A O   
2417  C CB  . PHE A 145 ? 0.1083 0.0840 0.0920 -0.0084 -0.0306 0.0196  368 PHE A CB  
2418  C CG  . PHE A 145 ? 0.0954 0.0728 0.1042 0.0085  -0.0182 0.0024  368 PHE A CG  
2419  C CD1 . PHE A 145 ? 0.0938 0.0688 0.1175 0.0175  -0.0175 0.0038  368 PHE A CD1 
2420  C CD2 . PHE A 145 ? 0.1033 0.0783 0.1060 0.0112  -0.0072 -0.0024 368 PHE A CD2 
2421  C CE1 . PHE A 145 ? 0.0897 0.0845 0.1227 0.0147  -0.0195 -0.0078 368 PHE A CE1 
2422  C CE2 . PHE A 145 ? 0.0864 0.0846 0.1303 -0.0036 -0.0046 -0.0221 368 PHE A CE2 
2423  C CZ  . PHE A 145 ? 0.0711 0.0850 0.1474 0.0126  -0.0162 -0.0289 368 PHE A CZ  
2433  N N   . VAL A 146 ? 0.0891 0.0696 0.0987 -0.0057 -0.0346 0.0124  369 VAL A N   
2434  C CA  . VAL A 146 ? 0.0928 0.0727 0.0887 -0.0082 -0.0282 0.0173  369 VAL A CA  
2435  C C   . VAL A 146 ? 0.0916 0.0809 0.0715 -0.0171 -0.0319 0.0164  369 VAL A C   
2436  O O   . VAL A 146 ? 0.0916 0.0876 0.0747 -0.0203 -0.0291 0.0070  369 VAL A O   
2437  C CB  . VAL A 146 ? 0.1060 0.0882 0.0942 -0.0147 -0.0381 0.0140  369 VAL A CB  
2438  C CG1 . VAL A 146 ? 0.1065 0.1147 0.1204 -0.0066 -0.0612 0.0152  369 VAL A CG1 
2439  C CG2 . VAL A 146 ? 0.1142 0.1067 0.0801 -0.0224 -0.0319 0.0166  369 VAL A CG2 
2449  N N   . PRO A 147 ? 0.0668 0.0768 0.0818 -0.0162 -0.0273 0.0138  370 PRO A N   
2450  C CA  . PRO A 147 ? 0.0776 0.0780 0.0933 -0.0060 -0.0214 0.0152  370 PRO A CA  
2451  C C   . PRO A 147 ? 0.0774 0.0777 0.0951 -0.0222 -0.0189 0.0119  370 PRO A C   
2452  O O   . PRO A 147 ? 0.1013 0.0751 0.0974 -0.0175 -0.0189 0.0134  370 PRO A O   
2453  C CB  . PRO A 147 ? 0.0862 0.0801 0.1029 -0.0141 -0.0177 0.0098  370 PRO A CB  
2454  C CG  . PRO A 147 ? 0.0791 0.0778 0.0913 -0.0134 -0.0144 0.0033  370 PRO A CG  
2455  C CD  . PRO A 147 ? 0.0679 0.0683 0.0954 -0.0135 -0.0196 0.0083  370 PRO A CD  
2463  N N   . LYS A 148 ? 0.0913 0.0948 0.0854 -0.0278 -0.0119 0.0034  371 LYS A N   
2464  C CA  . LYS A 148 ? 0.1212 0.1059 0.0900 -0.0480 -0.0070 -0.0038 371 LYS A CA  
2465  C C   . LYS A 148 ? 0.1222 0.1160 0.1094 -0.0339 -0.0223 -0.0120 371 LYS A C   
2466  O O   . LYS A 148 ? 0.1465 0.1548 0.1070 -0.0477 -0.0046 -0.0411 371 LYS A O   
2467  C CB  . LYS A 148 ? 0.1467 0.1333 0.0887 -0.0542 -0.0131 -0.0029 371 LYS A CB  
2468  C CG  . LYS A 148 ? 0.2013 0.1761 0.1407 -0.0519 0.0108  -0.0197 371 LYS A CG  
2469  C CD  . LYS A 148 ? 0.2185 0.2005 0.1708 -0.0527 -0.0041 -0.0147 371 LYS A CD  
2470  C CE  . LYS A 148 ? 0.2434 0.2302 0.2123 -0.0357 0.0295  -0.0070 371 LYS A CE  
2471  N NZ  . LYS A 148 ? 0.2513 0.2424 0.2340 -0.0471 0.0368  -0.0049 371 LYS A NZ  
2485  N N   . LEU A 149 ? 0.0990 0.1007 0.1140 -0.0286 -0.0492 -0.0012 372 LEU A N   
2486  C CA  . LEU A 149 ? 0.1274 0.1111 0.1368 -0.0258 -0.0442 0.0100  372 LEU A CA  
2487  C C   . LEU A 149 ? 0.1275 0.1112 0.1455 -0.0370 -0.0401 0.0104  372 LEU A C   
2488  O O   . LEU A 149 ? 0.1692 0.1281 0.1796 -0.0480 -0.0520 0.0282  372 LEU A O   
2489  C CB  . LEU A 149 ? 0.1487 0.1232 0.1289 -0.0351 -0.0593 0.0184  372 LEU A CB  
2490  C CG  . LEU A 149 ? 0.1829 0.1408 0.1542 -0.0259 -0.0489 0.0268  372 LEU A CG  
2491  C CD1 . LEU A 149 ? 0.1866 0.1589 0.1676 -0.0242 -0.0760 0.0214  372 LEU A CD1 
2492  C CD2 . LEU A 149 ? 0.2148 0.1562 0.1745 -0.0202 -0.0237 0.0316  372 LEU A CD2 
2504  N N   . GLY A 150 ? 0.1433 0.0987 0.1122 -0.0314 -0.0123 -0.0001 373 GLY A N   
2505  C CA  . GLY A 150 ? 0.1344 0.0849 0.1205 -0.0212 -0.0217 -0.0008 373 GLY A CA  
2506  C C   . GLY A 150 ? 0.1222 0.0777 0.1126 -0.0185 -0.0249 0.0046  373 GLY A C   
2507  O O   . GLY A 150 ? 0.1420 0.0752 0.1131 -0.0162 -0.0337 0.0072  373 GLY A O   
2511  N N   . SER A 151 ? 0.1091 0.0734 0.1100 -0.0213 -0.0369 0.0095  374 SER A N   
2512  C CA  . SER A 151 ? 0.1088 0.0794 0.1114 -0.0247 -0.0255 0.0041  374 SER A CA  
2513  C C   . SER A 151 ? 0.1023 0.0794 0.0954 -0.0108 -0.0440 0.0098  374 SER A C   
2514  O O   . SER A 151 ? 0.1130 0.0740 0.0945 -0.0143 -0.0238 0.0151  374 SER A O   
2515  C CB  . SER A 151 ? 0.1101 0.0968 0.1050 -0.0275 -0.0321 0.0173  374 SER A CB  
2516  O OG  . SER A 151 ? 0.1230 0.1048 0.1372 -0.0310 -0.0288 0.0239  374 SER A OG  
2522  N N   . VAL A 152 ? 0.0938 0.0665 0.0968 -0.0012 -0.0157 0.0140  375 VAL A N   
2523  C CA  . VAL A 152 ? 0.0968 0.0695 0.1015 -0.0132 -0.0083 0.0175  375 VAL A CA  
2524  C C   . VAL A 152 ? 0.0964 0.0718 0.1009 -0.0066 -0.0165 0.0264  375 VAL A C   
2525  O O   . VAL A 152 ? 0.1101 0.0753 0.1340 -0.0154 -0.0004 0.0181  375 VAL A O   
2526  C CB  . VAL A 152 ? 0.0928 0.0809 0.0956 -0.0266 -0.0267 0.0083  375 VAL A CB  
2527  C CG1 . VAL A 152 ? 0.0917 0.0824 0.1051 -0.0236 -0.0327 0.0140  375 VAL A CG1 
2528  C CG2 . VAL A 152 ? 0.1029 0.0907 0.0858 -0.0319 -0.0299 0.0064  375 VAL A CG2 
2538  N N   . MET A 153 ? 0.0921 0.0781 0.1221 -0.0072 -0.0065 0.0169  376 MET A N   
2539  C CA  B MET A 153 ? 0.0797 0.0912 0.1274 -0.0082 -0.0237 0.0277  376 MET A CA  
2540  C CA  C MET A 153 ? 0.0826 0.0851 0.1325 -0.0154 -0.0238 0.0207  376 MET A CA  
2541  C C   . MET A 153 ? 0.0772 0.0816 0.1224 -0.0237 -0.0290 0.0227  376 MET A C   
2542  O O   . MET A 153 ? 0.1107 0.0864 0.1287 -0.0387 -0.0215 0.0189  376 MET A O   
2543  C CB  B MET A 153 ? 0.0906 0.1378 0.1608 0.0193  -0.0196 0.0273  376 MET A CB  
2544  C CB  C MET A 153 ? 0.0920 0.1108 0.1654 -0.0058 -0.0266 0.0141  376 MET A CB  
2545  C CG  B MET A 153 ? 0.1117 0.1814 0.1946 0.0249  -0.0065 0.0264  376 MET A CG  
2546  C CG  C MET A 153 ? 0.1034 0.1336 0.1990 -0.0109 -0.0303 0.0045  376 MET A CG  
2547  S SD  B MET A 153 ? 0.1342 0.2190 0.2285 0.0469  -0.0014 0.0418  376 MET A SD  
2548  S SD  C MET A 153 ? 0.1230 0.1543 0.2353 -0.0011 -0.0251 0.0062  376 MET A SD  
2549  C CE  B MET A 153 ? 0.1389 0.2236 0.2398 0.0503  0.0198  0.0226  376 MET A CE  
2550  C CE  C MET A 153 ? 0.1301 0.1626 0.2546 -0.0008 -0.0295 0.0018  376 MET A CE  
2569  N N   . ILE A 154 ? 0.0860 0.0745 0.1110 -0.0224 -0.0276 0.0259  377 ILE A N   
2570  C CA  . ILE A 154 ? 0.0823 0.0771 0.1032 -0.0201 -0.0296 0.0195  377 ILE A CA  
2571  C C   . ILE A 154 ? 0.0810 0.0673 0.1068 -0.0137 -0.0257 0.0079  377 ILE A C   
2572  O O   . ILE A 154 ? 0.0818 0.0887 0.1391 -0.0204 -0.0268 0.0063  377 ILE A O   
2573  C CB  . ILE A 154 ? 0.0885 0.0808 0.1260 -0.0041 -0.0267 0.0084  377 ILE A CB  
2574  C CG1 . ILE A 154 ? 0.0800 0.0886 0.1246 -0.0044 -0.0349 0.0162  377 ILE A CG1 
2575  C CG2 . ILE A 154 ? 0.1009 0.0815 0.1332 -0.0045 -0.0157 0.0036  377 ILE A CG2 
2576  C CD1 . ILE A 154 ? 0.1089 0.1027 0.1343 0.0028  -0.0248 -0.0006 377 ILE A CD1 
2588  N N   . GLY A 155 ? 0.0838 0.0661 0.1114 -0.0174 -0.0210 0.0172  378 GLY A N   
2589  C CA  . GLY A 155 ? 0.0698 0.0828 0.1272 -0.0118 -0.0028 0.0145  378 GLY A CA  
2590  C C   . GLY A 155 ? 0.0571 0.0928 0.1237 -0.0086 -0.0064 0.0157  378 GLY A C   
2591  O O   . GLY A 155 ? 0.0715 0.1066 0.1236 -0.0227 -0.0212 0.0196  378 GLY A O   
2595  N N   . THR A 156 ? 0.0670 0.0999 0.1233 -0.0039 -0.0005 0.0155  379 THR A N   
2596  C CA  . THR A 156 ? 0.0682 0.1025 0.1313 -0.0132 0.0000  0.0252  379 THR A CA  
2597  C C   . THR A 156 ? 0.0709 0.0977 0.1376 -0.0183 0.0037  0.0169  379 THR A C   
2598  O O   . THR A 156 ? 0.1000 0.1159 0.1359 -0.0088 0.0106  0.0249  379 THR A O   
2599  C CB  . THR A 156 ? 0.0689 0.1026 0.1366 -0.0213 -0.0035 0.0203  379 THR A CB  
2600  O OG1 . THR A 156 ? 0.0684 0.1066 0.1512 -0.0167 0.0049  0.0133  379 THR A OG1 
2601  C CG2 . THR A 156 ? 0.0763 0.1028 0.1302 -0.0154 -0.0075 0.0117  379 THR A CG2 
2609  N N   . TRP A 157 ? 0.0605 0.0930 0.1451 0.0014  0.0054  0.0284  380 TRP A N   
2610  C CA  . TRP A 157 ? 0.0766 0.1035 0.1713 0.0057  0.0065  0.0184  380 TRP A CA  
2611  C C   . TRP A 157 ? 0.0750 0.1139 0.1761 0.0153  0.0083  0.0201  380 TRP A C   
2612  O O   . TRP A 157 ? 0.0863 0.1192 0.1674 -0.0050 0.0078  0.0144  380 TRP A O   
2613  C CB  . TRP A 157 ? 0.0922 0.1114 0.1815 -0.0073 0.0038  0.0101  380 TRP A CB  
2614  C CG  . TRP A 157 ? 0.1220 0.1122 0.2032 0.0077  0.0008  0.0146  380 TRP A CG  
2615  C CD1 . TRP A 157 ? 0.1603 0.1222 0.2575 0.0259  0.0411  0.0129  380 TRP A CD1 
2616  C CD2 . TRP A 157 ? 0.1137 0.1230 0.2082 0.0012  -0.0100 0.0218  380 TRP A CD2 
2617  N NE1 . TRP A 157 ? 0.1583 0.1259 0.2858 0.0191  0.0365  0.0094  380 TRP A NE1 
2618  C CE2 . TRP A 157 ? 0.1300 0.1270 0.2466 -0.0053 -0.0071 0.0239  380 TRP A CE2 
2619  C CE3 . TRP A 157 ? 0.1147 0.1393 0.2219 0.0031  0.0018  0.0488  380 TRP A CE3 
2620  C CZ2 . TRP A 157 ? 0.1298 0.1436 0.2484 -0.0110 0.0065  0.0423  380 TRP A CZ2 
2621  C CZ3 . TRP A 157 ? 0.1134 0.1644 0.2465 0.0100  0.0094  0.0594  380 TRP A CZ3 
2622  C CH2 . TRP A 157 ? 0.1189 0.1734 0.2659 0.0018  0.0103  0.0557  380 TRP A CH2 
2633  N N   . THR A 158 ? 0.0901 0.1351 0.1871 -0.0035 0.0202  0.0133  381 THR A N   
2634  C CA  . THR A 158 ? 0.1221 0.1679 0.2054 -0.0094 0.0516  0.0089  381 THR A CA  
2635  C C   . THR A 158 ? 0.0954 0.1597 0.2015 -0.0024 0.0185  0.0357  381 THR A C   
2636  O O   . THR A 158 ? 0.0827 0.1711 0.2533 -0.0216 0.0254  0.0333  381 THR A O   
2637  C CB  . THR A 158 ? 0.2058 0.2191 0.2375 -0.0116 0.0857  -0.0084 381 THR A CB  
2638  O OG1 . THR A 158 ? 0.2677 0.2666 0.2295 -0.0160 0.0941  -0.0054 381 THR A OG1 
2639  C CG2 . THR A 158 ? 0.2297 0.2319 0.2725 -0.0083 0.1201  -0.0173 381 THR A CG2 
2647  N N   . THR A 159 ? 0.0794 0.1404 0.1727 -0.0111 -0.0039 0.0316  382 THR A N   
2648  C CA  . THR A 159 ? 0.0685 0.1255 0.1926 -0.0016 -0.0127 0.0373  382 THR A CA  
2649  C C   . THR A 159 ? 0.0756 0.1214 0.1837 0.0132  0.0140  0.0344  382 THR A C   
2650  O O   . THR A 159 ? 0.0853 0.1289 0.1848 -0.0065 0.0246  0.0340  382 THR A O   
2651  C CB  . THR A 159 ? 0.1050 0.1416 0.2666 -0.0117 -0.0326 0.0209  382 THR A CB  
2652  O OG1 . THR A 159 ? 0.1285 0.1711 0.3079 -0.0048 -0.0747 0.0238  382 THR A OG1 
2653  C CG2 . THR A 159 ? 0.1004 0.1337 0.2982 -0.0201 -0.0051 0.0224  382 THR A CG2 
2661  N N   . ASP A 160 ? 0.0878 0.1278 0.1845 -0.0014 0.0349  0.0255  383 ASP A N   
2662  C CA  . ASP A 160 ? 0.0904 0.1536 0.1967 0.0086  0.0013  0.0252  383 ASP A CA  
2663  C C   . ASP A 160 ? 0.0748 0.1280 0.1608 -0.0170 -0.0007 0.0207  383 ASP A C   
2664  O O   . ASP A 160 ? 0.0859 0.1362 0.1783 -0.0185 -0.0226 0.0114  383 ASP A O   
2665  C CB  . ASP A 160 ? 0.0986 0.2107 0.2846 0.0041  -0.0055 0.0215  383 ASP A CB  
2666  C CG  . ASP A 160 ? 0.0951 0.2530 0.3359 -0.0378 0.0120  0.0226  383 ASP A CG  
2667  O OD1 . ASP A 160 ? 0.1617 0.2697 0.3866 -0.0504 0.0910  0.0435  383 ASP A OD1 
2668  O OD2 . ASP A 160 ? 0.1301 0.3015 0.4217 -0.0190 0.0681  0.0382  383 ASP A OD2 
2673  N N   . ASP A 161 ? 0.0737 0.1133 0.1468 -0.0067 -0.0106 0.0140  384 ASP A N   
2674  C CA  . ASP A 161 ? 0.0771 0.1175 0.1486 -0.0095 -0.0044 0.0123  384 ASP A CA  
2675  C C   . ASP A 161 ? 0.0776 0.1008 0.1257 -0.0134 -0.0095 0.0191  384 ASP A C   
2676  O O   . ASP A 161 ? 0.0819 0.0971 0.1160 -0.0029 -0.0081 0.0072  384 ASP A O   
2677  C CB  . ASP A 161 ? 0.0902 0.1159 0.1452 -0.0021 0.0056  0.0060  384 ASP A CB  
2678  C CG  . ASP A 161 ? 0.1029 0.1103 0.1422 -0.0225 -0.0148 0.0150  384 ASP A CG  
2679  O OD1 . ASP A 161 ? 0.1331 0.1209 0.1605 -0.0366 -0.0192 0.0181  384 ASP A OD1 
2680  O OD2 . ASP A 161 ? 0.1151 0.0931 0.1528 -0.0180 -0.0202 0.0057  384 ASP A OD2 
2685  N N   . ILE A 162 ? 0.0694 0.1136 0.1283 -0.0088 -0.0076 -0.0055 385 ILE A N   
2686  C CA  . ILE A 162 ? 0.0518 0.0990 0.1258 -0.0227 -0.0269 0.0029  385 ILE A CA  
2687  C C   . ILE A 162 ? 0.0617 0.1050 0.1209 -0.0158 -0.0328 0.0110  385 ILE A C   
2688  O O   . ILE A 162 ? 0.0827 0.1107 0.1436 -0.0045 -0.0433 -0.0101 385 ILE A O   
2689  C CB  . ILE A 162 ? 0.0583 0.0825 0.1235 -0.0228 -0.0123 0.0124  385 ILE A CB  
2690  C CG1 . ILE A 162 ? 0.0763 0.1020 0.1312 -0.0312 -0.0085 0.0200  385 ILE A CG1 
2691  C CG2 . ILE A 162 ? 0.0839 0.0810 0.1237 -0.0172 -0.0072 0.0161  385 ILE A CG2 
2692  C CD1 . ILE A 162 ? 0.0962 0.1094 0.1283 -0.0319 -0.0069 0.0196  385 ILE A CD1 
2704  N N   . LYS A 163 ? 0.0545 0.0958 0.1204 -0.0233 -0.0329 0.0116  386 LYS A N   
2705  C CA  . LYS A 163 ? 0.0572 0.0856 0.1175 -0.0234 -0.0224 0.0183  386 LYS A CA  
2706  C C   . LYS A 163 ? 0.0598 0.0917 0.1242 -0.0082 -0.0249 0.0139  386 LYS A C   
2707  O O   . LYS A 163 ? 0.0661 0.0981 0.1198 -0.0238 -0.0089 0.0158  386 LYS A O   
2708  C CB  . LYS A 163 ? 0.0754 0.0825 0.1286 -0.0289 -0.0165 0.0137  386 LYS A CB  
2709  C CG  . LYS A 163 ? 0.0835 0.0920 0.1338 -0.0338 -0.0189 0.0151  386 LYS A CG  
2710  C CD  . LYS A 163 ? 0.0789 0.1146 0.1230 -0.0283 -0.0168 0.0128  386 LYS A CD  
2711  C CE  . LYS A 163 ? 0.0995 0.1554 0.1456 -0.0300 -0.0111 0.0026  386 LYS A CE  
2712  N NZ  . LYS A 163 ? 0.1147 0.1800 0.1595 -0.0289 -0.0036 0.0007  386 LYS A NZ  
2726  N N   A ASN A 164 ? 0.0697 0.1066 0.1215 -0.0266 -0.0204 0.0136  387 ASN A N   
2727  C CA  A ASN A 164 ? 0.0711 0.1143 0.1029 -0.0374 -0.0238 0.0146  387 ASN A CA  
2728  C C   A ASN A 164 ? 0.0941 0.0987 0.1027 -0.0269 -0.0229 -0.0034 387 ASN A C   
2729  O O   A ASN A 164 ? 0.0882 0.1287 0.1357 -0.0426 -0.0102 -0.0477 387 ASN A O   
2730  C CB  A ASN A 164 ? 0.0812 0.1355 0.1260 -0.0524 -0.0272 0.0126  387 ASN A CB  
2731  C CG  A ASN A 164 ? 0.0861 0.1665 0.1621 -0.0439 -0.0473 0.0133  387 ASN A CG  
2732  O OD1 A ASN A 164 ? 0.0861 0.1804 0.1971 -0.0422 -0.0471 0.0178  387 ASN A OD1 
2733  N ND2 A ASN A 164 ? 0.1071 0.1963 0.2294 -0.0499 -0.0363 -0.0020 387 ASN A ND2 
2740  N N   . GLN A 165 ? 0.0821 0.0818 0.1065 -0.0280 -0.0288 0.0115  388 GLN A N   
2741  C CA  . GLN A 165 ? 0.0805 0.0691 0.1044 -0.0214 -0.0119 0.0059  388 GLN A CA  
2742  C C   . GLN A 165 ? 0.0795 0.0740 0.0928 -0.0237 -0.0187 0.0029  388 GLN A C   
2743  O O   . GLN A 165 ? 0.0764 0.0775 0.1111 -0.0270 -0.0190 0.0109  388 GLN A O   
2744  C CB  . GLN A 165 ? 0.0900 0.0750 0.0981 -0.0229 -0.0044 -0.0009 388 GLN A CB  
2745  C CG  . GLN A 165 ? 0.1190 0.0915 0.0874 -0.0406 0.0001  0.0058  388 GLN A CG  
2746  C CD  . GLN A 165 ? 0.1186 0.0964 0.1097 -0.0421 -0.0001 0.0070  388 GLN A CD  
2747  O OE1 . GLN A 165 ? 0.1316 0.0868 0.1087 -0.0322 -0.0162 0.0062  388 GLN A OE1 
2748  N NE2 . GLN A 165 ? 0.1499 0.1189 0.1771 -0.0582 0.0211  -0.0316 388 GLN A NE2 
2757  N N   . PRO A 166 ? 0.0855 0.0758 0.0930 -0.0294 -0.0208 -0.0021 389 PRO A N   
2758  C CA  . PRO A 166 ? 0.0816 0.0785 0.1007 -0.0146 -0.0241 -0.0041 389 PRO A CA  
2759  C C   . PRO A 166 ? 0.0862 0.0737 0.1005 -0.0123 -0.0239 0.0010  389 PRO A C   
2760  O O   . PRO A 166 ? 0.1058 0.0718 0.1024 -0.0249 -0.0162 0.0042  389 PRO A O   
2761  C CB  . PRO A 166 ? 0.0938 0.0829 0.1010 -0.0163 -0.0144 -0.0048 389 PRO A CB  
2762  C CG  . PRO A 166 ? 0.0972 0.0804 0.1130 -0.0073 -0.0115 0.0021  389 PRO A CG  
2763  C CD  . PRO A 166 ? 0.0990 0.0793 0.1085 -0.0182 -0.0214 0.0127  389 PRO A CD  
2771  N N   . SER A 167 ? 0.0854 0.0572 0.0830 -0.0137 -0.0128 0.0010  390 SER A N   
2772  C CA  . SER A 167 ? 0.0728 0.0685 0.0913 -0.0086 0.0022  -0.0081 390 SER A CA  
2773  C C   . SER A 167 ? 0.0757 0.0661 0.0940 -0.0175 0.0096  -0.0075 390 SER A C   
2774  O O   . SER A 167 ? 0.0806 0.0883 0.1047 -0.0380 -0.0037 0.0015  390 SER A O   
2775  C CB  . SER A 167 ? 0.0709 0.0692 0.1321 -0.0148 0.0031  -0.0089 390 SER A CB  
2776  O OG  . SER A 167 ? 0.0767 0.0801 0.1427 -0.0127 -0.0089 0.0043  390 SER A OG  
2782  N N   A LYS A 168 ? 0.0690 0.0667 0.0866 -0.0155 -0.0056 -0.0121 391 LYS A N   
2783  C CA  A LYS A 168 ? 0.0745 0.0679 0.0949 -0.0071 -0.0188 -0.0137 391 LYS A CA  
2784  C C   A LYS A 168 ? 0.0720 0.0691 0.0906 -0.0248 -0.0192 -0.0130 391 LYS A C   
2785  O O   A LYS A 168 ? 0.0959 0.0774 0.1077 -0.0309 0.0143  -0.0072 391 LYS A O   
2786  C CB  A LYS A 168 ? 0.0883 0.0979 0.1278 -0.0010 -0.0242 -0.0283 391 LYS A CB  
2787  C CG  A LYS A 168 ? 0.1098 0.1311 0.1665 0.0010  -0.0211 -0.0157 391 LYS A CG  
2788  C CD  A LYS A 168 ? 0.1412 0.1737 0.2045 0.0006  -0.0258 -0.0141 391 LYS A CD  
2789  C CE  A LYS A 168 ? 0.2038 0.2016 0.2288 0.0323  -0.0041 0.0165  391 LYS A CE  
2790  N NZ  A LYS A 168 ? 0.2601 0.2166 0.2614 0.0837  0.0527  0.0574  391 LYS A NZ  
2804  N N   . PHE A 169 ? 0.0792 0.0618 0.0870 -0.0206 -0.0091 0.0009  392 PHE A N   
2805  C CA  . PHE A 169 ? 0.0621 0.0717 0.0818 -0.0091 -0.0135 -0.0092 392 PHE A CA  
2806  C C   . PHE A 169 ? 0.0559 0.0727 0.1003 -0.0068 -0.0007 -0.0133 392 PHE A C   
2807  O O   . PHE A 169 ? 0.0660 0.0834 0.0981 -0.0164 0.0088  -0.0160 392 PHE A O   
2808  C CB  . PHE A 169 ? 0.0696 0.0748 0.0860 -0.0131 -0.0122 0.0015  392 PHE A CB  
2809  C CG  . PHE A 169 ? 0.0702 0.0658 0.0967 -0.0045 -0.0213 -0.0049 392 PHE A CG  
2810  C CD1 . PHE A 169 ? 0.0953 0.0840 0.1022 0.0085  -0.0061 -0.0015 392 PHE A CD1 
2811  C CD2 . PHE A 169 ? 0.0775 0.0786 0.1113 -0.0002 -0.0186 0.0052  392 PHE A CD2 
2812  C CE1 . PHE A 169 ? 0.1022 0.0881 0.0998 0.0267  -0.0093 -0.0010 392 PHE A CE1 
2813  C CE2 . PHE A 169 ? 0.1079 0.0695 0.1094 -0.0057 -0.0243 0.0064  392 PHE A CE2 
2814  C CZ  . PHE A 169 ? 0.1162 0.0699 0.0968 0.0114  -0.0118 -0.0079 392 PHE A CZ  
2824  N N   . THR A 170 ? 0.0514 0.0670 0.0922 -0.0080 -0.0165 -0.0155 393 THR A N   
2825  C CA  . THR A 170 ? 0.0556 0.0831 0.1005 -0.0032 -0.0104 -0.0250 393 THR A CA  
2826  C C   . THR A 170 ? 0.0541 0.0736 0.0814 -0.0082 -0.0035 -0.0115 393 THR A C   
2827  O O   . THR A 170 ? 0.0552 0.0667 0.0956 -0.0087 -0.0068 -0.0052 393 THR A O   
2828  C CB  . THR A 170 ? 0.0606 0.0803 0.1516 0.0132  -0.0289 -0.0171 393 THR A CB  
2829  O OG1 . THR A 170 ? 0.0946 0.0894 0.2055 0.0195  -0.0221 -0.0123 393 THR A OG1 
2830  C CG2 . THR A 170 ? 0.0725 0.0975 0.1575 0.0072  -0.0368 -0.0062 393 THR A CG2 
2838  N N   . PRO A 171 ? 0.0629 0.0697 0.0876 -0.0030 0.0060  -0.0007 394 PRO A N   
2839  C CA  . PRO A 171 ? 0.0615 0.0709 0.1024 -0.0207 -0.0068 -0.0025 394 PRO A CA  
2840  C C   . PRO A 171 ? 0.0484 0.0688 0.1158 -0.0033 -0.0058 -0.0001 394 PRO A C   
2841  O O   . PRO A 171 ? 0.0480 0.0822 0.1305 0.0080  -0.0130 -0.0060 394 PRO A O   
2842  C CB  . PRO A 171 ? 0.0936 0.0868 0.0941 -0.0319 -0.0115 -0.0020 394 PRO A CB  
2843  C CG  . PRO A 171 ? 0.0714 0.0914 0.1085 -0.0249 0.0032  -0.0003 394 PRO A CG  
2844  C CD  . PRO A 171 ? 0.0632 0.0923 0.1000 -0.0023 0.0023  -0.0029 394 PRO A CD  
2852  N N   . ILE A 172 ? 0.0508 0.0651 0.1078 -0.0039 -0.0260 -0.0020 395 ILE A N   
2853  C CA  . ILE A 172 ? 0.0736 0.0676 0.0967 -0.0001 -0.0199 -0.0030 395 ILE A CA  
2854  C C   . ILE A 172 ? 0.0735 0.0605 0.0961 -0.0005 -0.0064 -0.0017 395 ILE A C   
2855  O O   . ILE A 172 ? 0.0702 0.0668 0.1196 -0.0071 -0.0165 0.0004  395 ILE A O   
2856  C CB  . ILE A 172 ? 0.0953 0.0709 0.1012 -0.0201 -0.0179 0.0090  395 ILE A CB  
2857  C CG1 . ILE A 172 ? 0.1273 0.0873 0.1376 -0.0141 -0.0290 0.0283  395 ILE A CG1 
2858  C CG2 . ILE A 172 ? 0.1224 0.0898 0.1193 -0.0227 -0.0052 0.0127  395 ILE A CG2 
2859  C CD1 . ILE A 172 ? 0.1514 0.0939 0.1624 0.0091  -0.0224 0.0339  395 ILE A CD1 
2871  N N   . GLY A 173 ? 0.0612 0.0528 0.1029 -0.0039 -0.0123 -0.0013 396 GLY A N   
2872  C CA  . GLY A 173 ? 0.0685 0.0518 0.0965 -0.0029 0.0021  -0.0072 396 GLY A CA  
2873  C C   . GLY A 173 ? 0.0746 0.0543 0.1065 -0.0065 -0.0068 0.0007  396 GLY A C   
2874  O O   . GLY A 173 ? 0.0737 0.0554 0.1143 -0.0063 -0.0128 -0.0096 396 GLY A O   
2878  N N   . LEU A 174 ? 0.0732 0.0501 0.0886 -0.0050 -0.0214 -0.0091 397 LEU A N   
2879  C CA  . LEU A 174 ? 0.0674 0.0641 0.0879 -0.0039 -0.0137 0.0021  397 LEU A CA  
2880  C C   . LEU A 174 ? 0.0788 0.0611 0.0901 0.0038  -0.0026 0.0023  397 LEU A C   
2881  O O   . LEU A 174 ? 0.0995 0.0735 0.0827 -0.0086 -0.0072 -0.0098 397 LEU A O   
2882  C CB  . LEU A 174 ? 0.0774 0.0751 0.0971 0.0078  0.0009  0.0190  397 LEU A CB  
2883  C CG  . LEU A 174 ? 0.0713 0.0872 0.1046 -0.0011 -0.0094 0.0202  397 LEU A CG  
2884  C CD1 . LEU A 174 ? 0.1049 0.0850 0.1357 0.0029  0.0115  0.0308  397 LEU A CD1 
2885  C CD2 . LEU A 174 ? 0.1154 0.1151 0.1087 -0.0364 0.0123  0.0011  397 LEU A CD2 
2897  N N   . ASN A 175 ? 0.0600 0.0737 0.1043 0.0057  -0.0091 0.0171  398 ASN A N   
2898  C CA  A ASN A 175 ? 0.0554 0.0787 0.1254 -0.0037 -0.0096 0.0039  398 ASN A CA  
2899  C CA  B ASN A 175 ? 0.0605 0.0879 0.1189 -0.0059 -0.0122 0.0083  398 ASN A CA  
2900  C C   . ASN A 175 ? 0.0872 0.0825 0.1261 0.0028  0.0097  0.0023  398 ASN A C   
2901  O O   . ASN A 175 ? 0.1324 0.0809 0.1358 0.0082  0.0192  0.0090  398 ASN A O   
2902  C CB  A ASN A 175 ? 0.0674 0.1042 0.1397 -0.0067 -0.0064 0.0092  398 ASN A CB  
2903  C CB  B ASN A 175 ? 0.0662 0.1247 0.1206 -0.0173 -0.0219 0.0191  398 ASN A CB  
2904  C CG  A ASN A 175 ? 0.0730 0.1118 0.1668 -0.0007 -0.0020 0.0053  398 ASN A CG  
2905  C CG  B ASN A 175 ? 0.0672 0.1509 0.1379 -0.0249 -0.0337 0.0259  398 ASN A CG  
2906  O OD1 A ASN A 175 ? 0.0661 0.1087 0.1610 -0.0015 -0.0138 0.0051  398 ASN A OD1 
2907  O OD1 B ASN A 175 ? 0.0708 0.1466 0.1324 -0.0320 -0.0399 0.0349  398 ASN A OD1 
2908  N ND2 A ASN A 175 ? 0.0893 0.1225 0.1825 -0.0082 0.0201  -0.0025 398 ASN A ND2 
2909  N ND2 B ASN A 175 ? 0.0730 0.1532 0.1344 -0.0116 -0.0329 0.0203  398 ASN A ND2 
2922  N N   . ASP A 176 ? 0.1202 0.0707 0.1132 0.0028  -0.0011 0.0113  399 ASP A N   
2923  C CA  . ASP A 176 ? 0.1154 0.0735 0.1341 0.0124  0.0079  0.0100  399 ASP A CA  
2924  C C   . ASP A 176 ? 0.1147 0.0795 0.1331 0.0164  -0.0104 0.0269  399 ASP A C   
2925  O O   . ASP A 176 ? 0.1464 0.1056 0.1463 0.0322  0.0339  0.0326  399 ASP A O   
2926  C CB  . ASP A 176 ? 0.1270 0.0871 0.1588 0.0090  0.0145  0.0046  399 ASP A CB  
2927  C CG  . ASP A 176 ? 0.1359 0.1066 0.1727 0.0034  -0.0160 -0.0014 399 ASP A CG  
2928  O OD1 . ASP A 176 ? 0.1328 0.1108 0.1535 0.0079  -0.0241 0.0149  399 ASP A OD1 
2929  O OD2 . ASP A 176 ? 0.1942 0.1386 0.1937 -0.0226 -0.0005 -0.0037 399 ASP A OD2 
2934  N N   . ASP A 177 ? 0.1117 0.0955 0.1852 0.0079  -0.0192 0.0248  400 ASP A N   
2935  C CA  . ASP A 177 ? 0.1120 0.1076 0.1963 0.0008  -0.0152 0.0308  400 ASP A CA  
2936  C C   . ASP A 177 ? 0.1208 0.1074 0.2093 0.0091  -0.0078 0.0368  400 ASP A C   
2937  O O   . ASP A 177 ? 0.1488 0.1314 0.2312 -0.0076 0.0106  0.0443  400 ASP A O   
2938  C CB  . ASP A 177 ? 0.1397 0.1379 0.1913 -0.0190 -0.0109 0.0222  400 ASP A CB  
2939  C CG  . ASP A 177 ? 0.1672 0.1901 0.1852 -0.0191 -0.0264 -0.0076 400 ASP A CG  
2940  O OD1 . ASP A 177 ? 0.2156 0.2150 0.1875 -0.0476 -0.0177 -0.0210 400 ASP A OD1 
2941  O OD2 . ASP A 177 ? 0.1490 0.2190 0.2233 -0.0106 -0.0085 0.0155  400 ASP A OD2 
2946  N N   . ASP A 178 ? 0.1090 0.1003 0.1856 0.0280  -0.0094 0.0300  401 ASP A N   
2947  C CA  . ASP A 178 ? 0.1258 0.1247 0.1884 0.0506  0.0027  0.0388  401 ASP A CA  
2948  C C   . ASP A 178 ? 0.1317 0.1271 0.2020 0.0394  0.0141  0.0543  401 ASP A C   
2949  O O   . ASP A 178 ? 0.1789 0.1135 0.2145 0.0434  0.0151  0.0536  401 ASP A O   
2950  C CB  . ASP A 178 ? 0.1299 0.1651 0.1957 0.0507  0.0034  0.0407  401 ASP A CB  
2951  C CG  . ASP A 178 ? 0.1373 0.2082 0.2066 0.0451  0.0039  0.0261  401 ASP A CG  
2952  O OD1 . ASP A 178 ? 0.1776 0.2140 0.2010 0.0366  0.0219  0.0134  401 ASP A OD1 
2953  O OD2 . ASP A 178 ? 0.1662 0.2520 0.2475 0.0349  0.0196  0.0289  401 ASP A OD2 
2958  N N   . ASN A 179 ? 0.0938 0.1488 0.1985 0.0448  0.0195  0.0715  402 ASN A N   
2959  C CA  . ASN A 179 ? 0.1102 0.1870 0.1978 0.0524  0.0015  0.0801  402 ASN A CA  
2960  C C   . ASN A 179 ? 0.0843 0.1729 0.1668 0.0254  -0.0106 0.0443  402 ASN A C   
2961  O O   . ASN A 179 ? 0.1038 0.2145 0.1683 0.0278  -0.0217 0.0407  402 ASN A O   
2962  C CB  . ASN A 179 ? 0.1399 0.2454 0.2462 0.0716  0.0163  0.0834  402 ASN A CB  
2963  C CG  . ASN A 179 ? 0.1910 0.2848 0.2998 0.0697  0.0164  0.0789  402 ASN A CG  
2964  O OD1 . ASN A 179 ? 0.2234 0.2965 0.3208 0.0896  0.0042  0.0863  402 ASN A OD1 
2965  N ND2 . ASN A 179 ? 0.1961 0.3082 0.3119 0.0666  0.0166  0.0715  402 ASN A ND2 
2972  N N   . PHE A 180 ? 0.0854 0.1334 0.1451 0.0132  -0.0016 0.0252  403 PHE A N   
2973  C CA  . PHE A 180 ? 0.0873 0.1028 0.1259 0.0165  0.0085  0.0209  403 PHE A CA  
2974  C C   . PHE A 180 ? 0.0813 0.0855 0.1101 0.0037  -0.0082 0.0155  403 PHE A C   
2975  O O   . PHE A 180 ? 0.1184 0.0804 0.1096 -0.0155 0.0074  -0.0086 403 PHE A O   
2976  C CB  . PHE A 180 ? 0.0917 0.0991 0.1146 0.0050  -0.0005 0.0131  403 PHE A CB  
2977  C CG  . PHE A 180 ? 0.0752 0.0824 0.0975 -0.0105 -0.0028 0.0031  403 PHE A CG  
2978  C CD1 . PHE A 180 ? 0.0797 0.0894 0.1017 0.0034  -0.0098 0.0029  403 PHE A CD1 
2979  C CD2 . PHE A 180 ? 0.0914 0.0680 0.1104 -0.0023 0.0108  0.0056  403 PHE A CD2 
2980  C CE1 . PHE A 180 ? 0.0805 0.0934 0.1150 0.0064  0.0015  0.0104  403 PHE A CE1 
2981  C CE2 . PHE A 180 ? 0.0848 0.0739 0.1153 -0.0059 0.0098  0.0220  403 PHE A CE2 
2982  C CZ  . PHE A 180 ? 0.0840 0.0894 0.1234 0.0176  0.0077  0.0163  403 PHE A CZ  
2992  N N   . LYS A 181 ? 0.0702 0.0804 0.1006 0.0105  0.0005  0.0157  404 LYS A N   
2993  C CA  . LYS A 181 ? 0.0820 0.0680 0.1048 0.0033  -0.0115 0.0051  404 LYS A CA  
2994  C C   . LYS A 181 ? 0.0690 0.0532 0.1002 -0.0088 -0.0276 0.0001  404 LYS A C   
2995  O O   . LYS A 181 ? 0.0669 0.0740 0.1009 0.0038  -0.0280 -0.0106 404 LYS A O   
2996  C CB  . LYS A 181 ? 0.0952 0.0862 0.1292 0.0258  -0.0198 0.0276  404 LYS A CB  
2997  C CG  . LYS A 181 ? 0.1412 0.1119 0.1680 0.0456  -0.0270 0.0165  404 LYS A CG  
2998  C CD  . LYS A 181 ? 0.2203 0.1535 0.2301 0.0737  -0.0124 0.0018  404 LYS A CD  
2999  C CE  . LYS A 181 ? 0.3046 0.1969 0.3022 0.0612  0.0359  -0.0066 404 LYS A CE  
3000  N NZ  . LYS A 181 ? 0.3519 0.2252 0.3433 0.0615  0.0556  -0.0127 404 LYS A NZ  
3014  N N   . GLN A 182 ? 0.0626 0.0600 0.0943 -0.0201 -0.0072 -0.0024 405 GLN A N   
3015  C CA  . GLN A 182 ? 0.0584 0.0637 0.0822 0.0019  -0.0135 -0.0020 405 GLN A CA  
3016  C C   . GLN A 182 ? 0.0694 0.0737 0.0833 0.0077  -0.0177 -0.0124 405 GLN A C   
3017  O O   . GLN A 182 ? 0.0815 0.0787 0.0957 0.0159  -0.0132 -0.0044 405 GLN A O   
3018  C CB  . GLN A 182 ? 0.0733 0.0663 0.0845 0.0023  -0.0163 0.0007  405 GLN A CB  
3019  C CG  . GLN A 182 ? 0.0738 0.0686 0.0942 -0.0006 -0.0126 0.0037  405 GLN A CG  
3020  C CD  . GLN A 182 ? 0.0792 0.0753 0.0826 0.0003  -0.0124 -0.0028 405 GLN A CD  
3021  O OE1 . GLN A 182 ? 0.0653 0.0816 0.0944 0.0033  -0.0135 0.0012  405 GLN A OE1 
3022  N NE2 . GLN A 182 ? 0.0851 0.0916 0.0981 -0.0032 -0.0225 -0.0052 405 GLN A NE2 
3031  N N   . TRP A 183 ? 0.0698 0.0781 0.1016 0.0020  -0.0146 0.0087  406 TRP A N   
3032  C CA  . TRP A 183 ? 0.0620 0.1029 0.1175 -0.0093 -0.0133 0.0286  406 TRP A CA  
3033  C C   . TRP A 183 ? 0.0742 0.1279 0.1223 -0.0215 -0.0051 0.0429  406 TRP A C   
3034  O O   . TRP A 183 ? 0.1023 0.2196 0.1255 -0.0521 -0.0112 0.0519  406 TRP A O   
3035  C CB  . TRP A 183 ? 0.0890 0.0987 0.1352 -0.0190 -0.0155 0.0323  406 TRP A CB  
3036  C CG  . TRP A 183 ? 0.0859 0.0818 0.1140 -0.0286 -0.0241 0.0210  406 TRP A CG  
3037  C CD1 . TRP A 183 ? 0.1094 0.0806 0.1202 -0.0265 -0.0281 0.0147  406 TRP A CD1 
3038  C CD2 . TRP A 183 ? 0.0884 0.0953 0.0987 -0.0195 -0.0089 0.0044  406 TRP A CD2 
3039  N NE1 . TRP A 183 ? 0.1192 0.0907 0.1247 -0.0313 -0.0309 -0.0034 406 TRP A NE1 
3040  C CE2 . TRP A 183 ? 0.1057 0.1007 0.1043 -0.0203 -0.0269 0.0049  406 TRP A CE2 
3041  C CE3 . TRP A 183 ? 0.0890 0.1098 0.0901 -0.0206 -0.0052 0.0070  406 TRP A CE3 
3042  C CZ2 . TRP A 183 ? 0.0923 0.1188 0.1077 -0.0325 -0.0230 0.0039  406 TRP A CZ2 
3043  C CZ3 . TRP A 183 ? 0.0824 0.1254 0.1036 -0.0107 -0.0158 0.0067  406 TRP A CZ3 
3044  C CH2 . TRP A 183 ? 0.0730 0.1173 0.1154 -0.0198 -0.0223 0.0191  406 TRP A CH2 
3055  N N   . GLU A 184 ? 0.0819 0.0849 0.0936 -0.0042 -0.0133 0.0084  407 GLU A N   
3056  C CA  . GLU A 184 ? 0.0711 0.0789 0.0944 0.0040  -0.0310 0.0071  407 GLU A CA  
3057  C C   . GLU A 184 ? 0.0806 0.0791 0.0870 -0.0087 -0.0352 0.0045  407 GLU A C   
3058  O O   . GLU A 184 ? 0.1125 0.0847 0.1041 -0.0011 -0.0059 0.0100  407 GLU A O   
3059  C CB  . GLU A 184 ? 0.1030 0.0833 0.0951 0.0075  -0.0185 -0.0049 407 GLU A CB  
3060  C CG  . GLU A 184 ? 0.1190 0.0844 0.1149 -0.0031 -0.0130 0.0057  407 GLU A CG  
3061  C CD  . GLU A 184 ? 0.1480 0.1078 0.1477 0.0037  -0.0286 -0.0125 407 GLU A CD  
3062  O OE1 . GLU A 184 ? 0.1359 0.1380 0.1654 0.0167  -0.0113 0.0094  407 GLU A OE1 
3063  O OE2 . GLU A 184 ? 0.1792 0.1163 0.2282 0.0379  -0.0117 -0.0175 407 GLU A OE2 
3070  N N   . LEU A 185 ? 0.0862 0.0793 0.0817 -0.0014 -0.0121 0.0064  408 LEU A N   
3071  C CA  . LEU A 185 ? 0.0737 0.0927 0.0926 0.0064  -0.0134 0.0029  408 LEU A CA  
3072  C C   . LEU A 185 ? 0.0819 0.0965 0.0953 0.0007  -0.0170 0.0065  408 LEU A C   
3073  O O   . LEU A 185 ? 0.0809 0.0978 0.1107 -0.0037 -0.0284 0.0138  408 LEU A O   
3074  C CB  . LEU A 185 ? 0.0814 0.0979 0.1019 0.0026  -0.0105 0.0123  408 LEU A CB  
3075  C CG  . LEU A 185 ? 0.0662 0.1024 0.0998 0.0107  -0.0233 0.0132  408 LEU A CG  
3076  C CD1 . LEU A 185 ? 0.0944 0.1289 0.0988 0.0014  -0.0096 0.0114  408 LEU A CD1 
3077  C CD2 . LEU A 185 ? 0.0724 0.1155 0.1072 0.0022  -0.0202 -0.0043 408 LEU A CD2 
3089  N N   . PRO A 186 ? 0.0820 0.0934 0.0952 -0.0040 -0.0344 0.0051  409 PRO A N   
3090  C CA  . PRO A 186 ? 0.0912 0.1008 0.0970 -0.0129 -0.0191 0.0138  409 PRO A CA  
3091  C C   . PRO A 186 ? 0.0843 0.0867 0.0970 -0.0040 -0.0219 0.0199  409 PRO A C   
3092  O O   . PRO A 186 ? 0.0995 0.0967 0.1047 -0.0106 -0.0184 0.0131  409 PRO A O   
3093  C CB  . PRO A 186 ? 0.0989 0.1251 0.1309 -0.0209 -0.0134 0.0406  409 PRO A CB  
3094  C CG  . PRO A 186 ? 0.1069 0.1075 0.1475 -0.0203 -0.0146 0.0031  409 PRO A CG  
3095  C CD  . PRO A 186 ? 0.0986 0.0904 0.1098 -0.0092 -0.0229 0.0031  409 PRO A CD  
3103  N N   . ASN A 187 ? 0.0752 0.0953 0.1132 0.0016  -0.0358 0.0116  410 ASN A N   
3104  C CA  . ASN A 187 ? 0.0859 0.0796 0.1105 -0.0126 -0.0418 0.0190  410 ASN A CA  
3105  C C   . ASN A 187 ? 0.0843 0.0769 0.1080 -0.0042 -0.0340 0.0243  410 ASN A C   
3106  O O   . ASN A 187 ? 0.1099 0.0796 0.1461 -0.0101 -0.0049 0.0246  410 ASN A O   
3107  C CB  . ASN A 187 ? 0.1066 0.0898 0.1441 -0.0140 -0.0564 0.0251  410 ASN A CB  
3108  C CG  . ASN A 187 ? 0.1526 0.1214 0.1869 -0.0111 -0.0793 0.0301  410 ASN A CG  
3109  O OD1 . ASN A 187 ? 0.2005 0.1192 0.2293 0.0080  -0.0665 0.0304  410 ASN A OD1 
3110  N ND2 . ASN A 187 ? 0.1511 0.1295 0.2123 -0.0095 -0.0719 0.0531  410 ASN A ND2 
3117  N N   . TYR A 188 ? 0.0816 0.0727 0.1039 -0.0056 -0.0264 0.0292  411 TYR A N   
3118  C CA  . TYR A 188 ? 0.0777 0.0815 0.0989 -0.0140 -0.0373 0.0141  411 TYR A CA  
3119  C C   . TYR A 188 ? 0.0856 0.0823 0.1069 -0.0227 -0.0454 0.0275  411 TYR A C   
3120  O O   . TYR A 188 ? 0.1015 0.0789 0.1066 -0.0191 -0.0301 0.0229  411 TYR A O   
3121  C CB  . TYR A 188 ? 0.0897 0.0775 0.0998 -0.0054 -0.0325 0.0203  411 TYR A CB  
3122  C CG  . TYR A 188 ? 0.0866 0.0761 0.1064 -0.0050 -0.0457 0.0146  411 TYR A CG  
3123  C CD1 . TYR A 188 ? 0.0883 0.0744 0.1175 -0.0164 -0.0406 0.0110  411 TYR A CD1 
3124  C CD2 . TYR A 188 ? 0.0876 0.0867 0.1010 -0.0097 -0.0404 0.0222  411 TYR A CD2 
3125  C CE1 . TYR A 188 ? 0.0889 0.0737 0.1206 0.0024  -0.0406 0.0112  411 TYR A CE1 
3126  C CE2 . TYR A 188 ? 0.1028 0.0735 0.1204 -0.0037 -0.0356 0.0212  411 TYR A CE2 
3127  C CZ  . TYR A 188 ? 0.0876 0.0732 0.1167 -0.0052 -0.0403 0.0076  411 TYR A CZ  
3128  O OH  . TYR A 188 ? 0.0936 0.0839 0.1124 -0.0111 -0.0376 0.0076  411 TYR A OH  
3138  N N   . SER A 189 ? 0.0963 0.0910 0.1000 -0.0206 -0.0425 0.0291  412 SER A N   
3139  C CA  . SER A 189 ? 0.1017 0.1036 0.1159 -0.0227 -0.0436 0.0229  412 SER A CA  
3140  C C   . SER A 189 ? 0.0967 0.1158 0.1282 -0.0191 -0.0529 0.0407  412 SER A C   
3141  O O   . SER A 189 ? 0.1105 0.1614 0.1486 -0.0145 -0.0547 0.0270  412 SER A O   
3142  C CB  . SER A 189 ? 0.1289 0.1237 0.1168 -0.0137 -0.0490 0.0165  412 SER A CB  
3143  O OG  . SER A 189 ? 0.1407 0.1423 0.1234 0.0063  -0.0472 0.0222  412 SER A OG  
3149  N N   . GLY A 190 ? 0.0827 0.1018 0.1287 -0.0123 -0.0460 0.0381  413 GLY A N   
3150  C CA  . GLY A 190 ? 0.1144 0.1347 0.1711 -0.0135 -0.0095 0.0472  413 GLY A CA  
3151  C C   . GLY A 190 ? 0.1006 0.1378 0.1993 -0.0134 -0.0081 0.0508  413 GLY A C   
3152  O O   . GLY A 190 ? 0.0800 0.1313 0.1991 -0.0209 -0.0290 0.0541  413 GLY A O   
3156  N N   . ALA A 191 ? 0.1139 0.1484 0.1924 0.0065  0.0104  0.0367  414 ALA A N   
3157  C CA  . ALA A 191 ? 0.1362 0.1682 0.1753 0.0082  0.0241  0.0586  414 ALA A CA  
3158  C C   . ALA A 191 ? 0.1301 0.1530 0.1599 0.0092  -0.0195 0.0489  414 ALA A C   
3159  O O   . ALA A 191 ? 0.1500 0.1613 0.2019 -0.0166 -0.0204 0.0625  414 ALA A O   
3160  C CB  . ALA A 191 ? 0.1664 0.2062 0.2019 0.0246  0.0661  0.0876  414 ALA A CB  
3166  N N   . LEU A 192 ? 0.1165 0.1183 0.1423 -0.0054 -0.0078 0.0247  415 LEU A N   
3167  C CA  . LEU A 192 ? 0.1083 0.1067 0.1053 -0.0043 -0.0133 0.0347  415 LEU A CA  
3168  C C   . LEU A 192 ? 0.1019 0.0994 0.0891 -0.0010 -0.0235 0.0296  415 LEU A C   
3169  O O   . LEU A 192 ? 0.1257 0.1345 0.0956 0.0205  -0.0343 0.0437  415 LEU A O   
3170  C CB  . LEU A 192 ? 0.1198 0.1417 0.1274 0.0334  -0.0259 0.0407  415 LEU A CB  
3171  C CG  . LEU A 192 ? 0.1594 0.1989 0.1893 0.0592  -0.0156 0.0255  415 LEU A CG  
3172  C CD1 . LEU A 192 ? 0.1569 0.2332 0.1841 0.0589  -0.0280 0.0143  415 LEU A CD1 
3173  C CD2 . LEU A 192 ? 0.2033 0.2185 0.2515 0.0785  0.0230  0.0096  415 LEU A CD2 
3185  N N   . THR A 193 ? 0.0874 0.1111 0.0990 0.0022  -0.0301 0.0287  416 THR A N   
3186  C CA  . THR A 193 ? 0.0973 0.1131 0.1151 -0.0046 -0.0314 0.0272  416 THR A CA  
3187  C C   . THR A 193 ? 0.0827 0.1195 0.1114 0.0040  -0.0153 0.0149  416 THR A C   
3188  O O   . THR A 193 ? 0.0897 0.1278 0.0992 -0.0036 -0.0283 0.0338  416 THR A O   
3189  C CB  . THR A 193 ? 0.1143 0.1103 0.1833 -0.0043 -0.0561 0.0241  416 THR A CB  
3190  O OG1 . THR A 193 ? 0.1268 0.1090 0.2697 -0.0282 -0.0558 0.0133  416 THR A OG1 
3191  C CG2 . THR A 193 ? 0.1496 0.1203 0.1681 0.0092  -0.0480 0.0295  416 THR A CG2 
3199  N N   . LEU A 194 ? 0.0676 0.1302 0.1026 0.0016  -0.0206 0.0184  417 LEU A N   
3200  C CA  . LEU A 194 ? 0.0684 0.1172 0.1084 0.0041  -0.0141 0.0214  417 LEU A CA  
3201  C C   . LEU A 194 ? 0.0650 0.1051 0.1058 -0.0013 -0.0289 0.0162  417 LEU A C   
3202  O O   . LEU A 194 ? 0.0964 0.1020 0.1250 0.0011  -0.0439 0.0113  417 LEU A O   
3203  C CB  . LEU A 194 ? 0.0655 0.1112 0.0987 0.0092  -0.0189 0.0402  417 LEU A CB  
3204  C CG  . LEU A 194 ? 0.0798 0.1198 0.1098 0.0029  -0.0145 0.0367  417 LEU A CG  
3205  C CD1 . LEU A 194 ? 0.0993 0.1263 0.1137 0.0107  -0.0168 0.0410  417 LEU A CD1 
3206  C CD2 . LEU A 194 ? 0.0922 0.1273 0.1276 0.0247  0.0099  0.0432  417 LEU A CD2 
3218  N N   . ASN A 195 ? 0.0657 0.1042 0.0996 -0.0021 -0.0269 0.0374  418 ASN A N   
3219  C CA  . ASN A 195 ? 0.0767 0.0975 0.0854 0.0087  -0.0373 0.0297  418 ASN A CA  
3220  C C   . ASN A 195 ? 0.0722 0.1012 0.1007 0.0157  -0.0357 0.0091  418 ASN A C   
3221  O O   . ASN A 195 ? 0.1006 0.1093 0.0912 0.0168  -0.0206 0.0205  418 ASN A O   
3222  C CB  . ASN A 195 ? 0.0832 0.0863 0.0911 -0.0008 -0.0308 0.0232  418 ASN A CB  
3223  C CG  . ASN A 195 ? 0.0954 0.0881 0.0862 -0.0065 -0.0241 0.0247  418 ASN A CG  
3224  O OD1 . ASN A 195 ? 0.0837 0.0994 0.1099 -0.0116 -0.0327 0.0168  418 ASN A OD1 
3225  N ND2 . ASN A 195 ? 0.1009 0.1003 0.0923 -0.0168 -0.0054 0.0024  418 ASN A ND2 
3232  N N   . MET A 196 ? 0.0959 0.0999 0.1079 0.0207  -0.0213 0.0057  419 MET A N   
3233  C CA  A MET A 196 ? 0.0846 0.1212 0.1171 0.0148  -0.0489 -0.0115 419 MET A CA  
3234  C CA  B MET A 196 ? 0.1068 0.1133 0.1107 0.0173  -0.0286 0.0015  419 MET A CA  
3235  C C   . MET A 196 ? 0.1026 0.1081 0.1053 0.0095  -0.0328 -0.0020 419 MET A C   
3236  O O   . MET A 196 ? 0.1186 0.1122 0.1114 0.0109  -0.0380 0.0071  419 MET A O   
3237  C CB  A MET A 196 ? 0.0936 0.1697 0.1313 0.0205  -0.0571 -0.0320 419 MET A CB  
3238  C CB  B MET A 196 ? 0.1297 0.1391 0.1187 0.0248  -0.0261 0.0023  419 MET A CB  
3239  C CG  A MET A 196 ? 0.1237 0.2076 0.1680 0.0080  -0.0520 -0.0649 419 MET A CG  
3240  C CG  B MET A 196 ? 0.1615 0.1590 0.1303 0.0258  -0.0184 0.0035  419 MET A CG  
3241  S SD  A MET A 196 ? 0.1445 0.2508 0.2286 -0.0048 -0.0498 -0.0902 419 MET A SD  
3242  S SD  B MET A 196 ? 0.1936 0.1840 0.1585 0.0265  -0.0044 0.0008  419 MET A SD  
3243  C CE  A MET A 196 ? 0.1715 0.2458 0.2375 -0.0009 -0.0119 -0.0903 419 MET A CE  
3244  C CE  B MET A 196 ? 0.2009 0.1857 0.1648 0.0266  -0.0069 -0.0008 419 MET A CE  
3263  N N   . GLY A 197 ? 0.0981 0.1071 0.0999 0.0180  -0.0268 -0.0029 420 GLY A N   
3264  C CA  . GLY A 197 ? 0.1010 0.1113 0.1126 0.0152  -0.0286 -0.0059 420 GLY A CA  
3265  C C   . GLY A 197 ? 0.0870 0.1001 0.1176 0.0062  -0.0409 -0.0088 420 GLY A C   
3266  O O   . GLY A 197 ? 0.1004 0.1088 0.1388 0.0109  -0.0398 -0.0118 420 GLY A O   
3270  N N   . LEU A 198 ? 0.1005 0.0951 0.0879 0.0043  -0.0359 0.0054  421 LEU A N   
3271  C CA  . LEU A 198 ? 0.0832 0.0992 0.1120 0.0020  -0.0307 -0.0146 421 LEU A CA  
3272  C C   . LEU A 198 ? 0.0762 0.1074 0.1038 0.0065  -0.0239 -0.0231 421 LEU A C   
3273  O O   . LEU A 198 ? 0.0945 0.1338 0.1074 -0.0015 -0.0088 -0.0037 421 LEU A O   
3274  C CB  . LEU A 198 ? 0.0881 0.1023 0.0881 0.0107  -0.0401 -0.0013 421 LEU A CB  
3275  C CG  . LEU A 198 ? 0.0812 0.1025 0.1066 0.0046  -0.0255 0.0113  421 LEU A CG  
3276  C CD1 . LEU A 198 ? 0.1012 0.1108 0.1234 0.0165  -0.0319 0.0081  421 LEU A CD1 
3277  C CD2 . LEU A 198 ? 0.0829 0.1089 0.1099 -0.0011 -0.0236 0.0049  421 LEU A CD2 
3289  N N   . ALA A 199 ? 0.0705 0.1036 0.1010 0.0010  -0.0455 -0.0073 422 ALA A N   
3290  C CA  . ALA A 199 ? 0.0807 0.1129 0.1144 -0.0069 -0.0317 -0.0124 422 ALA A CA  
3291  C C   . ALA A 199 ? 0.1105 0.1175 0.1009 -0.0165 -0.0265 -0.0022 422 ALA A C   
3292  O O   . ALA A 199 ? 0.1225 0.0940 0.1110 -0.0114 -0.0146 0.0095  422 ALA A O   
3293  C CB  . ALA A 199 ? 0.0922 0.1084 0.1145 -0.0038 -0.0350 -0.0123 422 ALA A CB  
3299  N N   . PRO A 200 ? 0.1395 0.1503 0.1142 -0.0273 -0.0387 0.0142  423 PRO A N   
3300  C CA  . PRO A 200 ? 0.1483 0.1528 0.1176 -0.0363 -0.0419 0.0199  423 PRO A CA  
3301  C C   . PRO A 200 ? 0.1512 0.1452 0.1069 -0.0519 -0.0441 0.0206  423 PRO A C   
3302  O O   . PRO A 200 ? 0.1525 0.1601 0.1164 -0.0628 -0.0325 0.0327  423 PRO A O   
3303  C CB  . PRO A 200 ? 0.1762 0.1692 0.1613 -0.0327 0.0068  0.0144  423 PRO A CB  
3304  C CG  . PRO A 200 ? 0.1699 0.1884 0.1773 -0.0255 0.0138  0.0269  423 PRO A CG  
3305  C CD  . PRO A 200 ? 0.1681 0.1763 0.1471 -0.0225 -0.0074 0.0297  423 PRO A CD  
3313  N N   . SER A 201 ? 0.1583 0.1547 0.1033 -0.0529 -0.0521 0.0295  424 SER A N   
3314  C CA  A SER A 201 ? 0.1624 0.1638 0.1080 -0.0558 -0.0524 0.0184  424 SER A CA  
3315  C CA  B SER A 201 ? 0.1550 0.1598 0.1142 -0.0617 -0.0493 0.0188  424 SER A CA  
3316  C C   . SER A 201 ? 0.1500 0.1665 0.1253 -0.0702 -0.0273 -0.0003 424 SER A C   
3317  O O   . SER A 201 ? 0.1756 0.2058 0.1319 -0.0907 -0.0030 -0.0133 424 SER A O   
3318  C CB  A SER A 201 ? 0.1988 0.1680 0.1295 -0.0517 -0.0344 0.0306  424 SER A CB  
3319  C CB  B SER A 201 ? 0.1609 0.1580 0.1216 -0.0630 -0.0604 0.0288  424 SER A CB  
3320  O OG  A SER A 201 ? 0.2398 0.1832 0.1602 -0.0419 -0.0092 0.0488  424 SER A OG  
3321  O OG  B SER A 201 ? 0.1681 0.1603 0.1313 -0.0618 -0.0686 0.0425  424 SER A OG  
3332  N N   . VAL A 202 ? 0.1266 0.1499 0.1166 -0.0452 -0.0293 -0.0111 425 VAL A N   
3333  C CA  . VAL A 202 ? 0.1218 0.1357 0.1261 -0.0290 -0.0304 -0.0166 425 VAL A CA  
3334  C C   . VAL A 202 ? 0.1119 0.1286 0.1269 -0.0190 -0.0270 -0.0042 425 VAL A C   
3335  O O   . VAL A 202 ? 0.1394 0.1160 0.1150 -0.0091 -0.0092 0.0120  425 VAL A O   
3336  C CB  . VAL A 202 ? 0.1301 0.1282 0.1744 -0.0191 -0.0311 -0.0163 425 VAL A CB  
3337  C CG1 . VAL A 202 ? 0.1492 0.1472 0.2039 -0.0322 -0.0270 -0.0304 425 VAL A CG1 
3338  C CG2 . VAL A 202 ? 0.1303 0.1140 0.1855 -0.0026 -0.0517 0.0101  425 VAL A CG2 
3348  N N   . PHE A 203 ? 0.1132 0.1386 0.1422 -0.0123 -0.0170 -0.0137 426 PHE A N   
3349  C CA  . PHE A 203 ? 0.1225 0.1605 0.1426 -0.0050 -0.0433 0.0019  426 PHE A CA  
3350  C C   . PHE A 203 ? 0.1376 0.1360 0.1337 -0.0166 -0.0324 0.0120  426 PHE A C   
3351  O O   . PHE A 203 ? 0.1561 0.1289 0.1668 -0.0398 -0.0090 0.0012  426 PHE A O   
3352  C CB  . PHE A 203 ? 0.1617 0.2251 0.1505 -0.0053 -0.0469 0.0181  426 PHE A CB  
3353  C CG  . PHE A 203 ? 0.2357 0.2996 0.1817 -0.0116 -0.0280 0.0183  426 PHE A CG  
3354  C CD1 . PHE A 203 ? 0.2898 0.3288 0.1828 -0.0097 -0.0148 0.0062  426 PHE A CD1 
3355  C CD2 . PHE A 203 ? 0.2704 0.3317 0.2012 -0.0131 0.0120  0.0331  426 PHE A CD2 
3356  C CE1 . PHE A 203 ? 0.3114 0.3511 0.2072 -0.0115 -0.0079 0.0011  426 PHE A CE1 
3357  C CE2 . PHE A 203 ? 0.3002 0.3544 0.2156 -0.0158 0.0217  0.0116  426 PHE A CE2 
3358  C CZ  . PHE A 203 ? 0.3119 0.3611 0.2139 -0.0163 0.0129  0.0045  426 PHE A CZ  
3368  N N   . PRO A 204 ? 0.1537 0.1316 0.1306 -0.0289 -0.0315 0.0087  427 PRO A N   
3369  C CA  . PRO A 204 ? 0.1736 0.1406 0.1603 -0.0221 -0.0264 0.0252  427 PRO A CA  
3370  C C   . PRO A 204 ? 0.1903 0.1424 0.1878 0.0033  -0.0075 0.0590  427 PRO A C   
3371  O O   . PRO A 204 ? 0.2360 0.1915 0.2330 0.0311  0.0400  0.0944  427 PRO A O   
3372  C CB  . PRO A 204 ? 0.1923 0.1622 0.1577 -0.0391 -0.0198 -0.0029 427 PRO A CB  
3373  C CG  . PRO A 204 ? 0.2046 0.1604 0.1571 -0.0695 0.0056  -0.0275 427 PRO A CG  
3374  C CD  . PRO A 204 ? 0.1780 0.1436 0.1341 -0.0470 -0.0024 -0.0157 427 PRO A CD  
3382  N N   . THR A 205 ? 0.1759 0.1226 0.1751 -0.0090 -0.0223 0.0412  428 THR A N   
3383  C CA  . THR A 205 ? 0.1951 0.1353 0.1608 0.0026  -0.0450 0.0460  428 THR A CA  
3384  C C   . THR A 205 ? 0.1800 0.1187 0.1841 -0.0022 -0.0288 0.0530  428 THR A C   
3385  O O   . THR A 205 ? 0.2120 0.1370 0.2221 0.0004  -0.0396 0.0678  428 THR A O   
3386  C CB  . THR A 205 ? 0.2488 0.1728 0.1594 -0.0083 -0.0248 0.0009  428 THR A CB  
3387  O OG1 . THR A 205 ? 0.2704 0.1821 0.1626 0.0044  -0.0132 -0.0152 428 THR A OG1 
3388  C CG2 . THR A 205 ? 0.2748 0.2032 0.1730 -0.0229 -0.0040 -0.0055 428 THR A CG2 
3396  N N   . TYR A 206 ? 0.1573 0.1001 0.1773 -0.0148 -0.0275 0.0345  429 TYR A N   
3397  C CA  . TYR A 206 ? 0.1790 0.0932 0.1953 -0.0042 -0.0149 0.0448  429 TYR A CA  
3398  C C   . TYR A 206 ? 0.2073 0.0865 0.1682 -0.0125 0.0003  0.0388  429 TYR A C   
3399  O O   . TYR A 206 ? 0.1864 0.0926 0.1404 -0.0052 -0.0073 0.0313  429 TYR A O   
3400  C CB  . TYR A 206 ? 0.1834 0.0997 0.2465 -0.0070 -0.0070 0.0608  429 TYR A CB  
3401  C CG  . TYR A 206 ? 0.2067 0.1287 0.3063 -0.0488 0.0114  0.0444  429 TYR A CG  
3402  C CD1 . TYR A 206 ? 0.2324 0.1703 0.3674 -0.0550 0.0401  0.0024  429 TYR A CD1 
3403  C CD2 . TYR A 206 ? 0.2121 0.1707 0.3133 -0.0721 -0.0126 0.0634  429 TYR A CD2 
3404  C CE1 . TYR A 206 ? 0.2373 0.1974 0.3953 -0.0538 0.0271  0.0016  429 TYR A CE1 
3405  C CE2 . TYR A 206 ? 0.2265 0.1965 0.3435 -0.0714 -0.0237 0.0484  429 TYR A CE2 
3406  C CZ  . TYR A 206 ? 0.2270 0.2008 0.3901 -0.0641 -0.0112 0.0216  429 TYR A CZ  
3407  O OH  . TYR A 206 ? 0.2276 0.1974 0.4280 -0.0842 -0.0062 0.0158  429 TYR A OH  
3417  N N   . PRO A 207 ? 0.2363 0.0811 0.1523 -0.0024 -0.0125 0.0445  430 PRO A N   
3418  C CA  A PRO A 207 ? 0.2781 0.0938 0.1682 0.0014  0.0206  0.0472  430 PRO A CA  
3419  C CA  B PRO A 207 ? 0.2616 0.0865 0.1641 -0.0052 0.0067  0.0450  430 PRO A CA  
3420  C C   . PRO A 207 ? 0.2805 0.0969 0.1671 -0.0125 0.0217  0.0414  430 PRO A C   
3421  O O   . PRO A 207 ? 0.2759 0.1456 0.1762 -0.0457 0.0026  0.0379  430 PRO A O   
3422  C CB  A PRO A 207 ? 0.2968 0.1017 0.1852 0.0049  0.0371  0.0503  430 PRO A CB  
3423  C CB  B PRO A 207 ? 0.2601 0.0862 0.1728 -0.0034 0.0105  0.0458  430 PRO A CB  
3424  C CG  A PRO A 207 ? 0.2816 0.0982 0.1751 0.0045  0.0096  0.0507  430 PRO A CG  
3425  C CG  B PRO A 207 ? 0.2522 0.0841 0.1733 -0.0029 0.0031  0.0452  430 PRO A CG  
3426  C CD  A PRO A 207 ? 0.2552 0.0912 0.1620 0.0031  -0.0033 0.0517  430 PRO A CD  
3427  C CD  B PRO A 207 ? 0.2438 0.0823 0.1643 -0.0018 -0.0041 0.0469  430 PRO A CD  
3442  N N   . GLY A 208 ? 0.2840 0.0844 0.1606 -0.0205 0.0147  0.0182  431 GLY A N   
3443  C CA  . GLY A 208 ? 0.2675 0.0909 0.1387 -0.0157 0.0065  0.0202  431 GLY A CA  
3444  C C   . GLY A 208 ? 0.2358 0.0787 0.1357 -0.0238 -0.0114 0.0211  431 GLY A C   
3445  O O   . GLY A 208 ? 0.2584 0.0788 0.1649 -0.0374 -0.0202 0.0225  431 GLY A O   
3449  N N   . GLU A 209 ? 0.1694 0.0610 0.1347 -0.0262 -0.0293 0.0175  432 GLU A N   
3450  C CA  . GLU A 209 ? 0.1279 0.0657 0.1237 -0.0227 -0.0123 0.0158  432 GLU A CA  
3451  C C   . GLU A 209 ? 0.1182 0.0669 0.1064 -0.0173 -0.0295 0.0134  432 GLU A C   
3452  O O   . GLU A 209 ? 0.1267 0.0887 0.1203 -0.0109 -0.0261 0.0334  432 GLU A O   
3453  C CB  . GLU A 209 ? 0.1123 0.0714 0.1108 -0.0241 -0.0225 0.0137  432 GLU A CB  
3454  C CG  . GLU A 209 ? 0.1197 0.0920 0.1162 -0.0301 -0.0123 0.0195  432 GLU A CG  
3455  C CD  . GLU A 209 ? 0.1289 0.0927 0.1319 -0.0290 0.0061  0.0244  432 GLU A CD  
3456  O OE1 . GLU A 209 ? 0.1478 0.0798 0.1385 -0.0262 0.0025  0.0160  432 GLU A OE1 
3457  O OE2 . GLU A 209 ? 0.1371 0.1114 0.1347 -0.0253 0.0088  0.0276  432 GLU A OE2 
3464  N N   . GLN A 210 ? 0.1177 0.0616 0.0980 -0.0181 -0.0184 0.0264  433 GLN A N   
3465  C CA  . GLN A 210 ? 0.0916 0.0636 0.1004 0.0011  -0.0195 0.0055  433 GLN A CA  
3466  C C   . GLN A 210 ? 0.1025 0.0631 0.1072 -0.0045 -0.0265 0.0015  433 GLN A C   
3467  O O   . GLN A 210 ? 0.0973 0.0712 0.1188 -0.0066 -0.0118 0.0031  433 GLN A O   
3468  C CB  . GLN A 210 ? 0.0941 0.0712 0.1306 -0.0022 -0.0109 -0.0036 433 GLN A CB  
3469  C CG  . GLN A 210 ? 0.1248 0.0766 0.1516 0.0059  -0.0182 0.0008  433 GLN A CG  
3470  C CD  . GLN A 210 ? 0.1428 0.0823 0.1547 0.0099  -0.0070 -0.0065 433 GLN A CD  
3471  O OE1 . GLN A 210 ? 0.1805 0.0783 0.1670 0.0165  0.0099  -0.0212 433 GLN A OE1 
3472  N NE2 . GLN A 210 ? 0.1485 0.0853 0.1456 -0.0038 0.0116  -0.0207 433 GLN A NE2 
3481  N N   . ILE A 211 ? 0.0954 0.0557 0.0961 -0.0009 -0.0168 0.0087  434 ILE A N   
3482  C CA  . ILE A 211 ? 0.0888 0.0585 0.0980 -0.0082 -0.0134 0.0082  434 ILE A CA  
3483  C C   . ILE A 211 ? 0.0899 0.0579 0.0973 -0.0114 -0.0122 0.0026  434 ILE A C   
3484  O O   . ILE A 211 ? 0.1111 0.0662 0.0888 0.0028  -0.0183 -0.0003 434 ILE A O   
3485  C CB  . ILE A 211 ? 0.0982 0.0734 0.1032 -0.0155 -0.0152 0.0192  434 ILE A CB  
3486  C CG1 . ILE A 211 ? 0.1159 0.0997 0.1124 -0.0386 -0.0257 0.0251  434 ILE A CG1 
3487  C CG2 . ILE A 211 ? 0.1000 0.0836 0.1106 -0.0156 -0.0233 0.0040  434 ILE A CG2 
3488  C CD1 . ILE A 211 ? 0.1400 0.1474 0.1192 -0.0532 -0.0397 0.0249  434 ILE A CD1 
3500  N N   . LEU A 212 ? 0.0767 0.0626 0.0901 -0.0061 -0.0022 0.0072  435 LEU A N   
3501  C CA  . LEU A 212 ? 0.0758 0.0708 0.0914 -0.0135 -0.0137 0.0107  435 LEU A CA  
3502  C C   . LEU A 212 ? 0.0880 0.0684 0.0766 -0.0068 -0.0172 0.0086  435 LEU A C   
3503  O O   . LEU A 212 ? 0.1164 0.0729 0.0955 -0.0238 0.0116  0.0038  435 LEU A O   
3504  C CB  . LEU A 212 ? 0.0778 0.0795 0.1088 -0.0196 -0.0008 0.0034  435 LEU A CB  
3505  C CG  . LEU A 212 ? 0.0713 0.0910 0.1011 -0.0164 0.0012  0.0031  435 LEU A CG  
3506  C CD1 . LEU A 212 ? 0.0973 0.1170 0.1032 -0.0194 -0.0101 -0.0137 435 LEU A CD1 
3507  C CD2 . LEU A 212 ? 0.0937 0.1164 0.1139 0.0056  -0.0047 0.0096  435 LEU A CD2 
3519  N N   . PHE A 213 ? 0.0650 0.0606 0.0835 -0.0177 -0.0090 0.0025  436 PHE A N   
3520  C CA  . PHE A 213 ? 0.0593 0.0749 0.0914 -0.0016 -0.0116 0.0104  436 PHE A CA  
3521  C C   . PHE A 213 ? 0.0586 0.0709 0.0922 -0.0056 -0.0173 -0.0055 436 PHE A C   
3522  O O   . PHE A 213 ? 0.0719 0.0642 0.0938 -0.0179 -0.0222 -0.0031 436 PHE A O   
3523  C CB  . PHE A 213 ? 0.0717 0.0904 0.1026 -0.0039 -0.0154 0.0249  436 PHE A CB  
3524  C CG  . PHE A 213 ? 0.0864 0.1032 0.0859 -0.0110 -0.0075 0.0281  436 PHE A CG  
3525  C CD1 . PHE A 213 ? 0.0905 0.1264 0.0856 -0.0199 -0.0133 0.0199  436 PHE A CD1 
3526  C CD2 . PHE A 213 ? 0.0982 0.1111 0.1065 0.0149  0.0059  0.0358  436 PHE A CD2 
3527  C CE1 . PHE A 213 ? 0.1031 0.1449 0.1082 -0.0204 -0.0192 0.0107  436 PHE A CE1 
3528  C CE2 . PHE A 213 ? 0.1116 0.1288 0.1382 0.0191  0.0121  0.0505  436 PHE A CE2 
3529  C CZ  . PHE A 213 ? 0.1120 0.1470 0.1297 0.0187  -0.0200 0.0404  436 PHE A CZ  
3539  N N   . PHE A 214 ? 0.0710 0.0652 0.0711 -0.0131 -0.0122 -0.0020 437 PHE A N   
3540  C CA  . PHE A 214 ? 0.0680 0.0600 0.0615 -0.0082 -0.0095 -0.0051 437 PHE A CA  
3541  C C   . PHE A 214 ? 0.0685 0.0593 0.0715 -0.0045 -0.0053 0.0018  437 PHE A C   
3542  O O   . PHE A 214 ? 0.0686 0.0705 0.0877 -0.0096 -0.0165 -0.0020 437 PHE A O   
3543  C CB  . PHE A 214 ? 0.0669 0.0709 0.0946 -0.0049 -0.0001 0.0029  437 PHE A CB  
3544  C CG  . PHE A 214 ? 0.0603 0.0699 0.0839 -0.0057 -0.0104 0.0062  437 PHE A CG  
3545  C CD1 . PHE A 214 ? 0.0587 0.0750 0.0972 0.0013  -0.0022 -0.0080 437 PHE A CD1 
3546  C CD2 . PHE A 214 ? 0.0666 0.0821 0.0869 0.0038  -0.0091 0.0007  437 PHE A CD2 
3547  C CE1 . PHE A 214 ? 0.0600 0.0791 0.1054 -0.0103 0.0022  -0.0125 437 PHE A CE1 
3548  C CE2 . PHE A 214 ? 0.0737 0.0914 0.0988 -0.0041 -0.0058 -0.0031 437 PHE A CE2 
3549  C CZ  . PHE A 214 ? 0.0587 0.0866 0.1099 -0.0197 0.0036  -0.0177 437 PHE A CZ  
3559  N N   . ARG A 215 ? 0.0602 0.0646 0.0830 -0.0045 -0.0153 -0.0052 438 ARG A N   
3560  C CA  . ARG A 215 ? 0.0629 0.0700 0.0890 0.0005  -0.0116 0.0032  438 ARG A CA  
3561  C C   . ARG A 215 ? 0.0645 0.0655 0.0843 -0.0047 -0.0118 0.0004  438 ARG A C   
3562  O O   . ARG A 215 ? 0.0691 0.0773 0.0792 -0.0106 -0.0257 0.0074  438 ARG A O   
3563  C CB  . ARG A 215 ? 0.0731 0.0749 0.0952 -0.0020 -0.0066 -0.0081 438 ARG A CB  
3564  C CG  . ARG A 215 ? 0.0825 0.0831 0.1154 0.0039  -0.0061 -0.0144 438 ARG A CG  
3565  C CD  . ARG A 215 ? 0.0806 0.0819 0.1064 0.0088  -0.0205 -0.0039 438 ARG A CD  
3566  N NE  . ARG A 215 ? 0.0897 0.0748 0.1116 0.0120  -0.0181 -0.0182 438 ARG A NE  
3567  C CZ  . ARG A 215 ? 0.1031 0.0723 0.1377 0.0114  -0.0204 -0.0217 438 ARG A CZ  
3568  N NH1 . ARG A 215 ? 0.1353 0.0815 0.1526 0.0310  -0.0116 -0.0247 438 ARG A NH1 
3569  N NH2 . ARG A 215 ? 0.1095 0.0683 0.1406 0.0126  -0.0239 -0.0089 438 ARG A NH2 
3583  N N   . SER A 216 ? 0.0624 0.0589 0.0881 -0.0033 -0.0164 0.0020  439 SER A N   
3584  C CA  . SER A 216 ? 0.0735 0.0655 0.0793 0.0015  -0.0150 0.0085  439 SER A CA  
3585  C C   . SER A 216 ? 0.0656 0.0714 0.0799 -0.0054 -0.0149 -0.0090 439 SER A C   
3586  O O   . SER A 216 ? 0.0733 0.0919 0.0830 0.0057  -0.0193 -0.0041 439 SER A O   
3587  C CB  . SER A 216 ? 0.0673 0.0691 0.0947 0.0005  -0.0012 -0.0035 439 SER A CB  
3588  O OG  . SER A 216 ? 0.0800 0.0730 0.0894 0.0126  -0.0065 0.0044  439 SER A OG  
3594  N N   . TYR A 217 ? 0.0595 0.0756 0.0931 0.0071  -0.0019 -0.0072 440 TYR A N   
3595  C CA  . TYR A 217 ? 0.0659 0.0821 0.0895 0.0049  -0.0072 -0.0135 440 TYR A CA  
3596  C C   . TYR A 217 ? 0.0916 0.0804 0.1065 0.0121  0.0043  -0.0028 440 TYR A C   
3597  O O   . TYR A 217 ? 0.0921 0.0969 0.1562 0.0035  0.0107  -0.0157 440 TYR A O   
3598  C CB  . TYR A 217 ? 0.0842 0.1196 0.1167 -0.0087 -0.0013 -0.0255 440 TYR A CB  
3599  C CG  . TYR A 217 ? 0.0996 0.1344 0.1617 0.0018  -0.0150 -0.0489 440 TYR A CG  
3600  C CD1 . TYR A 217 ? 0.1316 0.1277 0.1777 -0.0044 -0.0090 -0.0573 440 TYR A CD1 
3601  C CD2 . TYR A 217 ? 0.1037 0.1473 0.2296 0.0102  -0.0286 -0.0559 440 TYR A CD2 
3602  C CE1 . TYR A 217 ? 0.1648 0.1262 0.2139 -0.0007 -0.0097 -0.0760 440 TYR A CE1 
3603  C CE2 . TYR A 217 ? 0.1522 0.1504 0.2620 -0.0109 -0.0238 -0.0686 440 TYR A CE2 
3604  C CZ  . TYR A 217 ? 0.1934 0.1424 0.2677 -0.0271 -0.0108 -0.0693 440 TYR A CZ  
3605  O OH  . TYR A 217 ? 0.2458 0.1658 0.3033 -0.0387 -0.0013 -0.0663 440 TYR A OH  
3615  N N   . LEU A 218 ? 0.0875 0.0747 0.1086 0.0066  0.0156  -0.0017 441 LEU A N   
3616  C CA  . LEU A 218 ? 0.0828 0.0797 0.1121 -0.0153 0.0076  -0.0021 441 LEU A CA  
3617  C C   . LEU A 218 ? 0.0785 0.0650 0.0985 -0.0093 -0.0108 -0.0130 441 LEU A C   
3618  O O   . LEU A 218 ? 0.1039 0.0631 0.1080 0.0088  0.0060  -0.0222 441 LEU A O   
3619  C CB  . LEU A 218 ? 0.1031 0.0903 0.1095 -0.0288 0.0025  -0.0001 441 LEU A CB  
3620  C CG  . LEU A 218 ? 0.1303 0.1314 0.1248 -0.0223 0.0263  -0.0188 441 LEU A CG  
3621  C CD1 . LEU A 218 ? 0.1505 0.1815 0.1453 -0.0246 0.0174  -0.0285 441 LEU A CD1 
3622  C CD2 . LEU A 218 ? 0.1817 0.1312 0.1521 -0.0249 0.0694  -0.0187 441 LEU A CD2 
3634  N N   . PRO A 219 ? 0.0747 0.0625 0.1025 -0.0099 -0.0008 -0.0148 442 PRO A N   
3635  C CA  . PRO A 219 ? 0.0704 0.0719 0.0786 -0.0087 -0.0037 0.0115  442 PRO A CA  
3636  C C   . PRO A 219 ? 0.0629 0.0645 0.0838 -0.0029 0.0007  -0.0016 442 PRO A C   
3637  O O   . PRO A 219 ? 0.0710 0.0642 0.0891 -0.0061 -0.0089 -0.0054 442 PRO A O   
3638  C CB  . PRO A 219 ? 0.0832 0.0903 0.1271 0.0007  -0.0025 0.0313  442 PRO A CB  
3639  C CG  . PRO A 219 ? 0.1221 0.0895 0.1322 0.0216  0.0362  0.0041  442 PRO A CG  
3640  C CD  . PRO A 219 ? 0.0791 0.0672 0.1331 -0.0036 0.0076  -0.0122 442 PRO A CD  
3648  N N   . LEU A 220 ? 0.0621 0.0723 0.0803 -0.0029 0.0004  -0.0125 443 LEU A N   
3649  C CA  . LEU A 220 ? 0.0608 0.0649 0.0861 0.0100  -0.0006 0.0003  443 LEU A CA  
3650  C C   . LEU A 220 ? 0.0609 0.0617 0.0747 0.0049  -0.0060 -0.0014 443 LEU A C   
3651  O O   . LEU A 220 ? 0.0692 0.0632 0.0849 -0.0016 -0.0147 0.0019  443 LEU A O   
3652  C CB  . LEU A 220 ? 0.0700 0.0620 0.0959 0.0023  -0.0046 0.0100  443 LEU A CB  
3653  C CG  . LEU A 220 ? 0.0892 0.0654 0.0909 0.0108  -0.0138 0.0036  443 LEU A CG  
3654  C CD1 . LEU A 220 ? 0.1166 0.0709 0.1066 0.0082  0.0180  -0.0008 443 LEU A CD1 
3655  C CD2 . LEU A 220 ? 0.1383 0.0750 0.1019 -0.0173 -0.0020 -0.0034 443 LEU A CD2 
3667  N N   . LYS A 221 ? 0.0652 0.0651 0.0734 0.0089  -0.0095 0.0061  444 LYS A N   
3668  C CA  . LYS A 221 ? 0.0704 0.0587 0.0832 -0.0007 0.0046  -0.0002 444 LYS A CA  
3669  C C   . LYS A 221 ? 0.0642 0.0575 0.0894 0.0017  0.0039  -0.0026 444 LYS A C   
3670  O O   . LYS A 221 ? 0.0613 0.0654 0.0990 -0.0010 0.0072  -0.0028 444 LYS A O   
3671  C CB  . LYS A 221 ? 0.0669 0.0602 0.0938 0.0072  -0.0031 -0.0053 444 LYS A CB  
3672  C CG  . LYS A 221 ? 0.0679 0.0618 0.0945 0.0015  -0.0054 -0.0075 444 LYS A CG  
3673  C CD  . LYS A 221 ? 0.0608 0.0705 0.0924 0.0044  -0.0070 -0.0016 444 LYS A CD  
3674  C CE  . LYS A 221 ? 0.0764 0.0787 0.1012 -0.0053 -0.0102 0.0064  444 LYS A CE  
3675  N NZ  . LYS A 221 ? 0.0636 0.0743 0.0988 -0.0106 -0.0119 0.0088  444 LYS A NZ  
3689  N N   . GLY A 222 ? 0.0823 0.0580 0.1021 0.0101  0.0020  0.0005  445 GLY A N   
3690  C CA  . GLY A 222 ? 0.0690 0.0672 0.1116 0.0018  -0.0057 -0.0133 445 GLY A CA  
3691  C C   . GLY A 222 ? 0.0739 0.0762 0.1126 0.0101  -0.0040 -0.0116 445 GLY A C   
3692  O O   . GLY A 222 ? 0.0918 0.0778 0.1215 0.0158  -0.0094 -0.0033 445 GLY A O   
3696  N N   . GLY A 223 ? 0.0947 0.0690 0.1275 0.0091  -0.0051 -0.0157 446 GLY A N   
3697  C CA  . GLY A 223 ? 0.0969 0.0680 0.1305 0.0165  -0.0096 -0.0062 446 GLY A CA  
3698  C C   . GLY A 223 ? 0.0831 0.0652 0.1086 0.0261  -0.0121 0.0065  446 GLY A C   
3699  O O   . GLY A 223 ? 0.0962 0.0685 0.1043 0.0124  -0.0106 -0.0043 446 GLY A O   
3703  N N   A TYR A 224 ? 0.0928 0.0670 0.1158 0.0154  -0.0181 0.0066  447 TYR A N   
3704  C CA  A TYR A 224 ? 0.0970 0.0784 0.1098 0.0222  -0.0011 0.0082  447 TYR A CA  
3705  C C   A TYR A 224 ? 0.1075 0.0969 0.1089 0.0300  -0.0009 0.0153  447 TYR A C   
3706  O O   A TYR A 224 ? 0.1414 0.1601 0.1121 0.0390  0.0016  0.0158  447 TYR A O   
3707  C CB  A TYR A 224 ? 0.0999 0.0714 0.1207 0.0142  0.0113  0.0010  447 TYR A CB  
3708  C CG  A TYR A 224 ? 0.0834 0.0631 0.0968 0.0048  -0.0005 -0.0167 447 TYR A CG  
3709  C CD1 A TYR A 224 ? 0.0907 0.0879 0.1138 0.0041  0.0064  -0.0155 447 TYR A CD1 
3710  C CD2 A TYR A 224 ? 0.1004 0.0615 0.1086 0.0123  0.0018  -0.0175 447 TYR A CD2 
3711  C CE1 A TYR A 224 ? 0.0874 0.0967 0.1189 0.0076  0.0031  -0.0075 447 TYR A CE1 
3712  C CE2 A TYR A 224 ? 0.1032 0.0869 0.1033 0.0291  -0.0048 -0.0117 447 TYR A CE2 
3713  C CZ  A TYR A 224 ? 0.0964 0.1053 0.1103 0.0295  0.0219  -0.0012 447 TYR A CZ  
3714  O OH  A TYR A 224 ? 0.1419 0.1592 0.1293 -0.0042 0.0441  0.0096  447 TYR A OH  
3724  N N   . GLY A 225 ? 0.0898 0.0741 0.1206 0.0307  0.0137  0.0052  448 GLY A N   
3725  C CA  . GLY A 225 ? 0.1185 0.0588 0.1259 0.0235  0.0375  0.0120  448 GLY A CA  
3726  C C   . GLY A 225 ? 0.1201 0.0508 0.1095 0.0093  0.0285  0.0047  448 GLY A C   
3727  O O   . GLY A 225 ? 0.0994 0.0587 0.1248 0.0144  0.0151  -0.0003 448 GLY A O   
3731  N N   . SER A 226 ? 0.1060 0.0659 0.1070 0.0027  0.0291  0.0098  449 SER A N   
3732  C CA  . SER A 226 ? 0.0896 0.0815 0.1103 0.0003  0.0092  -0.0055 449 SER A CA  
3733  C C   . SER A 226 ? 0.0704 0.0795 0.1168 -0.0005 0.0028  -0.0074 449 SER A C   
3734  O O   . SER A 226 ? 0.0833 0.0808 0.1254 -0.0042 0.0089  -0.0074 449 SER A O   
3735  C CB  . SER A 226 ? 0.1075 0.1028 0.1216 -0.0129 0.0193  -0.0066 449 SER A CB  
3736  O OG  . SER A 226 ? 0.1314 0.1047 0.1125 -0.0152 0.0073  -0.0072 449 SER A OG  
3742  N N   . PRO A 227 ? 0.0717 0.0841 0.1073 0.0028  0.0156  -0.0083 450 PRO A N   
3743  C CA  . PRO A 227 ? 0.0646 0.0858 0.0961 0.0143  0.0039  0.0069  450 PRO A CA  
3744  C C   . PRO A 227 ? 0.0727 0.0672 0.0989 0.0066  0.0053  -0.0008 450 PRO A C   
3745  O O   . PRO A 227 ? 0.0748 0.0725 0.1106 0.0113  0.0060  0.0048  450 PRO A O   
3746  C CB  . PRO A 227 ? 0.0716 0.1073 0.1038 0.0052  -0.0037 0.0136  450 PRO A CB  
3747  C CG  . PRO A 227 ? 0.0695 0.0986 0.1120 -0.0049 -0.0074 -0.0052 450 PRO A CG  
3748  C CD  . PRO A 227 ? 0.0742 0.0931 0.1020 -0.0046 -0.0056 -0.0033 450 PRO A CD  
3756  N N   . PHE A 228 ? 0.0707 0.0723 0.0869 0.0090  0.0073  0.0030  451 PHE A N   
3757  C CA  . PHE A 228 ? 0.0622 0.0831 0.0952 -0.0055 -0.0049 -0.0033 451 PHE A CA  
3758  C C   . PHE A 228 ? 0.0624 0.0736 0.0802 0.0006  -0.0110 0.0088  451 PHE A C   
3759  O O   . PHE A 228 ? 0.0769 0.0747 0.0867 -0.0005 0.0047  -0.0032 451 PHE A O   
3760  C CB  . PHE A 228 ? 0.0734 0.0926 0.0958 0.0012  -0.0104 -0.0114 451 PHE A CB  
3761  C CG  . PHE A 228 ? 0.0894 0.0858 0.1152 -0.0091 0.0034  -0.0069 451 PHE A CG  
3762  C CD1 . PHE A 228 ? 0.1034 0.0944 0.1204 -0.0275 -0.0179 0.0100  451 PHE A CD1 
3763  C CD2 . PHE A 228 ? 0.1113 0.0857 0.1437 0.0024  0.0096  -0.0025 451 PHE A CD2 
3764  C CE1 . PHE A 228 ? 0.1136 0.0984 0.1250 -0.0264 -0.0117 0.0113  451 PHE A CE1 
3765  C CE2 . PHE A 228 ? 0.1254 0.0948 0.1707 -0.0054 0.0129  0.0100  451 PHE A CE2 
3766  C CZ  . PHE A 228 ? 0.1213 0.0993 0.1595 -0.0101 0.0033  0.0246  451 PHE A CZ  
3776  N N   . ILE A 229 ? 0.0650 0.0716 0.0859 0.0007  -0.0046 0.0009  452 ILE A N   
3777  C CA  . ILE A 229 ? 0.0668 0.0643 0.0854 -0.0056 -0.0182 0.0104  452 ILE A CA  
3778  C C   . ILE A 229 ? 0.0555 0.0587 0.0853 0.0014  -0.0255 0.0100  452 ILE A C   
3779  O O   . ILE A 229 ? 0.0624 0.0722 0.0857 -0.0017 -0.0118 0.0028  452 ILE A O   
3780  C CB  . ILE A 229 ? 0.0672 0.0650 0.1047 -0.0055 -0.0075 0.0004  452 ILE A CB  
3781  C CG1 . ILE A 229 ? 0.0725 0.0804 0.1035 -0.0134 -0.0227 -0.0122 452 ILE A CG1 
3782  C CG2 . ILE A 229 ? 0.0965 0.0688 0.1130 0.0012  -0.0063 -0.0012 452 ILE A CG2 
3783  C CD1 . ILE A 229 ? 0.0789 0.0861 0.1029 0.0038  -0.0024 -0.0103 452 ILE A CD1 
3795  N N   . ASP A 230 ? 0.0597 0.0573 0.0981 -0.0008 -0.0099 0.0012  453 ASP A N   
3796  C CA  . ASP A 230 ? 0.0494 0.0656 0.0892 -0.0031 -0.0117 -0.0055 453 ASP A CA  
3797  C C   . ASP A 230 ? 0.0565 0.0678 0.0977 0.0019  -0.0196 0.0090  453 ASP A C   
3798  O O   . ASP A 230 ? 0.0722 0.0823 0.0856 0.0089  -0.0187 -0.0047 453 ASP A O   
3799  C CB  . ASP A 230 ? 0.0675 0.0675 0.0991 0.0001  -0.0067 -0.0034 453 ASP A CB  
3800  C CG  . ASP A 230 ? 0.0837 0.0781 0.1134 0.0170  -0.0265 -0.0021 453 ASP A CG  
3801  O OD1 . ASP A 230 ? 0.1069 0.0958 0.1236 0.0245  -0.0440 -0.0211 453 ASP A OD1 
3802  O OD2 . ASP A 230 ? 0.0935 0.0733 0.1232 0.0021  -0.0313 -0.0145 453 ASP A OD2 
3807  N N   . CYS A 231 ? 0.0589 0.0741 0.0706 -0.0035 -0.0087 -0.0018 454 CYS A N   
3808  C CA  . CYS A 231 ? 0.0618 0.0665 0.0738 -0.0028 -0.0145 -0.0055 454 CYS A CA  
3809  C C   . CYS A 231 ? 0.0593 0.0613 0.0893 -0.0054 -0.0193 -0.0004 454 CYS A C   
3810  O O   . CYS A 231 ? 0.0651 0.0770 0.0693 -0.0141 -0.0105 0.0018  454 CYS A O   
3811  C CB  . CYS A 231 ? 0.0633 0.0632 0.0946 -0.0073 0.0010  0.0115  454 CYS A CB  
3812  S SG  . CYS A 231 ? 0.0678 0.0661 0.0950 -0.0115 -0.0165 -0.0003 454 CYS A SG  
3818  N N   . LEU A 232 ? 0.0605 0.0521 0.0834 -0.0082 -0.0151 -0.0038 455 LEU A N   
3819  C CA  . LEU A 232 ? 0.0669 0.0627 0.0870 -0.0039 -0.0130 0.0002  455 LEU A CA  
3820  C C   . LEU A 232 ? 0.0599 0.0624 0.0872 -0.0054 -0.0234 0.0039  455 LEU A C   
3821  O O   . LEU A 232 ? 0.0723 0.0642 0.0880 -0.0063 -0.0236 0.0013  455 LEU A O   
3822  C CB  . LEU A 232 ? 0.0716 0.0743 0.0810 -0.0076 -0.0355 0.0127  455 LEU A CB  
3823  C CG  . LEU A 232 ? 0.0857 0.0939 0.0899 -0.0166 -0.0380 0.0196  455 LEU A CG  
3824  C CD1 . LEU A 232 ? 0.1025 0.1200 0.1032 -0.0256 -0.0347 0.0244  455 LEU A CD1 
3825  C CD2 . LEU A 232 ? 0.1007 0.1073 0.1176 -0.0017 -0.0421 0.0225  455 LEU A CD2 
3837  N N   . VAL A 233 ? 0.0592 0.0695 0.0909 0.0020  -0.0165 0.0148  456 VAL A N   
3838  C CA  . VAL A 233 ? 0.0661 0.0729 0.0726 0.0014  -0.0168 -0.0015 456 VAL A CA  
3839  C C   . VAL A 233 ? 0.0579 0.0621 0.0821 0.0022  -0.0243 -0.0027 456 VAL A C   
3840  O O   . VAL A 233 ? 0.0565 0.0617 0.1132 -0.0092 -0.0267 -0.0001 456 VAL A O   
3841  C CB  . VAL A 233 ? 0.0828 0.0642 0.0897 0.0009  -0.0072 0.0091  456 VAL A CB  
3842  C CG1 . VAL A 233 ? 0.0818 0.0701 0.0800 0.0069  0.0029  0.0144  456 VAL A CG1 
3843  C CG2 . VAL A 233 ? 0.1129 0.0698 0.1080 0.0011  0.0017  0.0153  456 VAL A CG2 
3853  N N   . PRO A 234 ? 0.0603 0.0568 0.0920 -0.0081 -0.0178 -0.0019 457 PRO A N   
3854  C CA  . PRO A 234 ? 0.0632 0.0714 0.0925 -0.0075 -0.0148 0.0009  457 PRO A CA  
3855  C C   . PRO A 234 ? 0.0536 0.0657 0.0833 -0.0093 -0.0188 0.0134  457 PRO A C   
3856  O O   . PRO A 234 ? 0.0730 0.0696 0.0741 -0.0063 -0.0113 0.0005  457 PRO A O   
3857  C CB  . PRO A 234 ? 0.0927 0.0754 0.0980 -0.0104 -0.0216 -0.0052 457 PRO A CB  
3858  C CG  . PRO A 234 ? 0.0798 0.0851 0.1223 -0.0204 -0.0335 0.0011  457 PRO A CG  
3859  C CD  . PRO A 234 ? 0.0683 0.0632 0.1027 -0.0111 -0.0300 -0.0027 457 PRO A CD  
3867  N N   . GLN A 235 ? 0.0618 0.0694 0.0824 -0.0009 -0.0128 -0.0035 458 GLN A N   
3868  C CA  . GLN A 235 ? 0.0694 0.0720 0.0804 -0.0024 -0.0085 0.0032  458 GLN A CA  
3869  C C   . GLN A 235 ? 0.0624 0.0683 0.0814 -0.0088 -0.0038 0.0028  458 GLN A C   
3870  O O   . GLN A 235 ? 0.0729 0.0713 0.0930 -0.0086 -0.0132 0.0006  458 GLN A O   
3871  C CB  . GLN A 235 ? 0.0596 0.0828 0.0817 -0.0083 -0.0171 0.0066  458 GLN A CB  
3872  C CG  . GLN A 235 ? 0.0628 0.0661 0.1079 -0.0095 -0.0127 0.0092  458 GLN A CG  
3873  C CD  . GLN A 235 ? 0.0633 0.0799 0.1279 0.0012  -0.0369 -0.0163 458 GLN A CD  
3874  O OE1 . GLN A 235 ? 0.0707 0.0860 0.1311 0.0025  -0.0431 -0.0183 458 GLN A OE1 
3875  N NE2 . GLN A 235 ? 0.1103 0.0905 0.1136 0.0103  -0.0318 -0.0257 458 GLN A NE2 
3884  N N   . GLU A 236 ? 0.0572 0.0665 0.0912 -0.0032 -0.0199 -0.0013 459 GLU A N   
3885  C CA  . GLU A 236 ? 0.0599 0.0717 0.0943 -0.0057 -0.0215 -0.0015 459 GLU A CA  
3886  C C   . GLU A 236 ? 0.0531 0.0720 0.1029 -0.0092 -0.0181 -0.0070 459 GLU A C   
3887  O O   . GLU A 236 ? 0.0721 0.0623 0.1192 0.0087  -0.0087 -0.0045 459 GLU A O   
3888  C CB  . GLU A 236 ? 0.0845 0.0942 0.0958 0.0215  0.0087  0.0178  459 GLU A CB  
3889  C CG  . GLU A 236 ? 0.0695 0.1148 0.0841 0.0117  -0.0021 0.0175  459 GLU A CG  
3890  C CD  . GLU A 236 ? 0.0877 0.1097 0.1009 0.0039  -0.0100 0.0290  459 GLU A CD  
3891  O OE1 . GLU A 236 ? 0.0849 0.0967 0.0945 0.0092  -0.0060 0.0118  459 GLU A OE1 
3892  O OE2 . GLU A 236 ? 0.0935 0.1217 0.1538 0.0026  0.0135  0.0389  459 GLU A OE2 
3899  N N   . TRP A 237 ? 0.0705 0.0556 0.0850 0.0016  -0.0088 0.0003  460 TRP A N   
3900  C CA  . TRP A 237 ? 0.0595 0.0610 0.0753 0.0021  -0.0145 0.0049  460 TRP A CA  
3901  C C   . TRP A 237 ? 0.0685 0.0636 0.0756 -0.0042 -0.0232 -0.0003 460 TRP A C   
3902  O O   . TRP A 237 ? 0.0861 0.0635 0.0894 -0.0070 -0.0024 -0.0156 460 TRP A O   
3903  C CB  . TRP A 237 ? 0.0681 0.0648 0.0871 -0.0113 -0.0099 0.0068  460 TRP A CB  
3904  C CG  . TRP A 237 ? 0.0667 0.0702 0.0803 -0.0114 -0.0204 0.0014  460 TRP A CG  
3905  C CD1 . TRP A 237 ? 0.0710 0.0679 0.0877 -0.0246 -0.0232 -0.0065 460 TRP A CD1 
3906  C CD2 . TRP A 237 ? 0.0647 0.0735 0.0827 -0.0051 -0.0168 0.0012  460 TRP A CD2 
3907  N NE1 . TRP A 237 ? 0.0739 0.0643 0.0818 -0.0080 -0.0271 0.0061  460 TRP A NE1 
3908  C CE2 . TRP A 237 ? 0.0753 0.0633 0.0827 -0.0018 -0.0255 0.0023  460 TRP A CE2 
3909  C CE3 . TRP A 237 ? 0.0689 0.0691 0.0873 -0.0017 -0.0241 0.0016  460 TRP A CE3 
3910  C CZ2 . TRP A 237 ? 0.0812 0.0735 0.0838 -0.0166 -0.0192 -0.0047 460 TRP A CZ2 
3911  C CZ3 . TRP A 237 ? 0.0806 0.0677 0.0986 -0.0157 -0.0198 0.0180  460 TRP A CZ3 
3912  C CH2 . TRP A 237 ? 0.0741 0.0727 0.1063 -0.0030 -0.0336 0.0034  460 TRP A CH2 
3923  N N   . VAL A 238 ? 0.0703 0.0663 0.0963 0.0060  -0.0263 -0.0115 461 VAL A N   
3924  C CA  . VAL A 238 ? 0.0715 0.0710 0.0924 -0.0042 -0.0166 -0.0040 461 VAL A CA  
3925  C C   . VAL A 238 ? 0.0767 0.0837 0.0957 -0.0002 -0.0109 -0.0079 461 VAL A C   
3926  O O   . VAL A 238 ? 0.0867 0.0934 0.0988 -0.0118 -0.0004 -0.0250 461 VAL A O   
3927  C CB  . VAL A 238 ? 0.0779 0.0727 0.1037 -0.0009 -0.0166 -0.0109 461 VAL A CB  
3928  C CG1 . VAL A 238 ? 0.0877 0.0874 0.1084 0.0012  -0.0199 -0.0028 461 VAL A CG1 
3929  C CG2 . VAL A 238 ? 0.0810 0.0842 0.0947 -0.0006 -0.0209 -0.0013 461 VAL A CG2 
3939  N N   . ALA A 239 ? 0.0690 0.0803 0.0964 -0.0061 -0.0139 -0.0126 462 ALA A N   
3940  C CA  . ALA A 239 ? 0.0803 0.0746 0.1145 0.0032  -0.0083 -0.0080 462 ALA A CA  
3941  C C   . ALA A 239 ? 0.0727 0.0730 0.0988 0.0008  -0.0035 -0.0023 462 ALA A C   
3942  O O   . ALA A 239 ? 0.0843 0.0753 0.1163 0.0198  0.0013  -0.0145 462 ALA A O   
3943  C CB  . ALA A 239 ? 0.1113 0.0860 0.1281 0.0004  0.0070  -0.0016 462 ALA A CB  
3949  N N   . HIS A 240 ? 0.0751 0.0686 0.0943 0.0048  -0.0019 0.0008  463 HIS A N   
3950  C CA  . HIS A 240 ? 0.0818 0.0719 0.0941 -0.0042 -0.0121 -0.0059 463 HIS A CA  
3951  C C   . HIS A 240 ? 0.0764 0.0702 0.1037 0.0003  -0.0088 -0.0035 463 HIS A C   
3952  O O   . HIS A 240 ? 0.0895 0.0740 0.1054 0.0098  -0.0087 0.0003  463 HIS A O   
3953  C CB  . HIS A 240 ? 0.0874 0.0787 0.0964 -0.0089 0.0015  -0.0023 463 HIS A CB  
3954  C CG  . HIS A 240 ? 0.0859 0.0909 0.0924 0.0077  -0.0154 0.0103  463 HIS A CG  
3955  N ND1 . HIS A 240 ? 0.0909 0.1104 0.1441 -0.0010 -0.0054 0.0421  463 HIS A ND1 
3956  C CD2 . HIS A 240 ? 0.0884 0.0833 0.1064 0.0042  -0.0230 -0.0009 463 HIS A CD2 
3957  C CE1 . HIS A 240 ? 0.0890 0.1104 0.1551 -0.0045 -0.0114 0.0321  463 HIS A CE1 
3958  N NE2 . HIS A 240 ? 0.0867 0.0947 0.1278 -0.0018 -0.0186 0.0126  463 HIS A NE2 
3966  N N   . PHE A 241 ? 0.0649 0.0741 0.0978 -0.0031 -0.0105 -0.0061 464 PHE A N   
3967  C CA  . PHE A 241 ? 0.0781 0.0708 0.0998 -0.0031 -0.0093 0.0006  464 PHE A CA  
3968  C C   . PHE A 241 ? 0.0661 0.0750 0.0850 0.0049  -0.0101 -0.0019 464 PHE A C   
3969  O O   . PHE A 241 ? 0.0870 0.0988 0.0771 -0.0055 0.0028  -0.0102 464 PHE A O   
3970  C CB  . PHE A 241 ? 0.0839 0.0708 0.1075 -0.0129 -0.0123 0.0056  464 PHE A CB  
3971  C CG  . PHE A 241 ? 0.0898 0.0704 0.0895 -0.0102 -0.0105 0.0212  464 PHE A CG  
3972  C CD1 . PHE A 241 ? 0.1092 0.0697 0.1173 -0.0034 -0.0150 0.0054  464 PHE A CD1 
3973  C CD2 . PHE A 241 ? 0.0746 0.0801 0.0804 -0.0131 -0.0067 0.0085  464 PHE A CD2 
3974  C CE1 . PHE A 241 ? 0.1162 0.0892 0.1020 -0.0032 -0.0257 0.0062  464 PHE A CE1 
3975  C CE2 . PHE A 241 ? 0.0914 0.0902 0.1025 -0.0121 -0.0084 -0.0056 464 PHE A CE2 
3976  C CZ  . PHE A 241 ? 0.1124 0.0848 0.0963 -0.0121 -0.0160 0.0082  464 PHE A CZ  
3986  N N   . TYR A 242 ? 0.0719 0.0719 0.0947 -0.0048 0.0004  -0.0039 465 TYR A N   
3987  C CA  . TYR A 242 ? 0.0819 0.0740 0.1182 -0.0108 -0.0018 -0.0135 465 TYR A CA  
3988  C C   . TYR A 242 ? 0.0964 0.0762 0.1060 0.0043  0.0004  -0.0122 465 TYR A C   
3989  O O   . TYR A 242 ? 0.1187 0.0925 0.1052 0.0274  -0.0041 -0.0169 465 TYR A O   
3990  C CB  . TYR A 242 ? 0.0903 0.0731 0.1361 -0.0028 -0.0166 -0.0122 465 TYR A CB  
3991  C CG  . TYR A 242 ? 0.1021 0.0875 0.1423 -0.0082 -0.0206 -0.0176 465 TYR A CG  
3992  C CD1 . TYR A 242 ? 0.1275 0.0977 0.1365 -0.0249 -0.0098 -0.0207 465 TYR A CD1 
3993  C CD2 . TYR A 242 ? 0.1467 0.0979 0.1648 -0.0153 -0.0291 -0.0226 465 TYR A CD2 
3994  C CE1 . TYR A 242 ? 0.1654 0.1103 0.1353 -0.0341 -0.0121 -0.0175 465 TYR A CE1 
3995  C CE2 . TYR A 242 ? 0.1825 0.1040 0.1806 -0.0445 -0.0432 -0.0123 465 TYR A CE2 
3996  C CZ  . TYR A 242 ? 0.1933 0.1093 0.1573 -0.0604 -0.0435 -0.0247 465 TYR A CZ  
3997  O OH  . TYR A 242 ? 0.2317 0.1292 0.2132 -0.0854 -0.0399 -0.0162 465 TYR A OH  
4007  N N   . GLN A 243 ? 0.1054 0.0670 0.1040 -0.0033 0.0051  -0.0038 466 GLN A N   
4008  C CA  . GLN A 243 ? 0.1078 0.0654 0.1137 0.0055  0.0146  -0.0034 466 GLN A CA  
4009  C C   . GLN A 243 ? 0.1029 0.0803 0.1045 0.0075  0.0061  -0.0099 466 GLN A C   
4010  O O   . GLN A 243 ? 0.1203 0.0888 0.1260 0.0136  0.0235  -0.0165 466 GLN A O   
4011  C CB  . GLN A 243 ? 0.1144 0.0634 0.1255 0.0073  0.0140  0.0045  466 GLN A CB  
4012  C CG  . GLN A 243 ? 0.1039 0.0662 0.1247 0.0081  -0.0049 0.0130  466 GLN A CG  
4013  C CD  . GLN A 243 ? 0.1274 0.0684 0.1192 0.0151  -0.0052 0.0129  466 GLN A CD  
4014  O OE1 . GLN A 243 ? 0.1468 0.0650 0.1196 0.0125  -0.0001 0.0141  466 GLN A OE1 
4015  N NE2 . GLN A 243 ? 0.1412 0.0828 0.1272 0.0093  -0.0086 -0.0059 466 GLN A NE2 
4024  N N   . GLU A 244 ? 0.0952 0.0767 0.1032 0.0109  -0.0005 -0.0052 467 GLU A N   
4025  C CA  . GLU A 244 ? 0.0968 0.0926 0.1277 0.0116  0.0055  0.0029  467 GLU A CA  
4026  C C   . GLU A 244 ? 0.0960 0.1014 0.1155 0.0064  0.0065  0.0004  467 GLU A C   
4027  O O   . GLU A 244 ? 0.1213 0.1006 0.1169 0.0006  0.0324  -0.0021 467 GLU A O   
4028  C CB  . GLU A 244 ? 0.0939 0.0893 0.1407 0.0049  -0.0055 0.0149  467 GLU A CB  
4029  C CG  . GLU A 244 ? 0.1016 0.1087 0.1661 -0.0025 -0.0123 0.0136  467 GLU A CG  
4030  C CD  . GLU A 244 ? 0.1181 0.1274 0.1977 0.0075  -0.0013 0.0289  467 GLU A CD  
4031  O OE1 . GLU A 244 ? 0.1122 0.1452 0.2033 0.0211  0.0113  0.0153  467 GLU A OE1 
4032  O OE2 . GLU A 244 ? 0.1417 0.1306 0.2488 0.0142  0.0069  0.0567  467 GLU A OE2 
4039  N N   . SER A 245 ? 0.0994 0.1167 0.1148 0.0172  -0.0037 -0.0007 468 SER A N   
4040  C CA  . SER A 245 ? 0.1314 0.1335 0.1242 -0.0030 -0.0011 0.0131  468 SER A CA  
4041  C C   . SER A 245 ? 0.1309 0.1234 0.1046 0.0037  0.0125  0.0018  468 SER A C   
4042  O O   . SER A 245 ? 0.1684 0.1448 0.1157 -0.0096 0.0226  -0.0155 468 SER A O   
4043  C CB  . SER A 245 ? 0.1676 0.1593 0.1423 -0.0490 -0.0017 0.0110  468 SER A CB  
4044  O OG  . SER A 245 ? 0.2003 0.1906 0.1695 -0.0537 -0.0074 0.0058  468 SER A OG  
4050  N N   . ALA A 246 ? 0.1129 0.1145 0.1073 0.0235  0.0217  -0.0012 469 ALA A N   
4051  C CA  . ALA A 246 ? 0.1218 0.1192 0.1202 0.0227  0.0167  0.0038  469 ALA A CA  
4052  C C   . ALA A 246 ? 0.1402 0.1200 0.1363 0.0049  0.0230  0.0034  469 ALA A C   
4053  O O   . ALA A 246 ? 0.1165 0.1255 0.1452 0.0162  0.0130  0.0065  469 ALA A O   
4054  C CB  . ALA A 246 ? 0.1335 0.1207 0.1326 0.0181  0.0168  -0.0119 469 ALA A CB  
4060  N N   . PRO A 247 ? 0.1657 0.1319 0.1395 -0.0045 0.0458  0.0095  470 PRO A N   
4061  C CA  . PRO A 247 ? 0.1869 0.1339 0.1400 -0.0093 0.0455  0.0144  470 PRO A CA  
4062  C C   . PRO A 247 ? 0.1828 0.1356 0.1383 -0.0153 0.0068  0.0247  470 PRO A C   
4063  O O   . PRO A 247 ? 0.2019 0.1446 0.1773 -0.0268 -0.0139 0.0273  470 PRO A O   
4064  C CB  . PRO A 247 ? 0.2133 0.1541 0.1734 -0.0035 0.0758  0.0141  470 PRO A CB  
4065  C CG  . PRO A 247 ? 0.2263 0.1641 0.1880 0.0032  0.0790  0.0166  470 PRO A CG  
4066  C CD  . PRO A 247 ? 0.1799 0.1378 0.1603 -0.0072 0.0569  0.0111  470 PRO A CD  
4074  N N   . ALA A 248 ? 0.1473 0.1404 0.1299 -0.0118 -0.0087 0.0204  471 ALA A N   
4075  C CA  . ALA A 248 ? 0.1619 0.1373 0.1271 -0.0102 0.0025  0.0253  471 ALA A CA  
4076  C C   . ALA A 248 ? 0.1649 0.1432 0.1164 -0.0163 0.0025  0.0141  471 ALA A C   
4077  O O   . ALA A 248 ? 0.1922 0.1715 0.1348 -0.0456 -0.0040 0.0108  471 ALA A O   
4078  C CB  . ALA A 248 ? 0.1837 0.1361 0.1517 -0.0043 0.0163  0.0271  471 ALA A CB  
4084  N N   . GLN A 249 ? 0.1474 0.1393 0.1048 0.0066  0.0193  0.0117  472 GLN A N   
4085  C CA  A GLN A 249 ? 0.1407 0.1461 0.1240 0.0009  0.0455  0.0105  472 GLN A CA  
4086  C CA  B GLN A 249 ? 0.1502 0.1398 0.1225 -0.0014 0.0398  0.0059  472 GLN A CA  
4087  C C   . GLN A 249 ? 0.1381 0.1346 0.1163 -0.0058 0.0435  0.0113  472 GLN A C   
4088  O O   . GLN A 249 ? 0.1720 0.1609 0.1260 0.0096  0.0648  0.0203  472 GLN A O   
4089  C CB  A GLN A 249 ? 0.1278 0.1622 0.1386 0.0040  0.0320  0.0091  472 GLN A CB  
4090  C CB  B GLN A 249 ? 0.1611 0.1440 0.1417 -0.0041 0.0414  -0.0044 472 GLN A CB  
4091  C CG  A GLN A 249 ? 0.1536 0.1915 0.1855 0.0159  0.0544  0.0173  472 GLN A CG  
4092  C CG  B GLN A 249 ? 0.1893 0.1548 0.1699 -0.0067 0.0580  -0.0119 472 GLN A CG  
4093  C CD  A GLN A 249 ? 0.1681 0.2142 0.2197 0.0187  0.0453  0.0363  472 GLN A CD  
4094  C CD  B GLN A 249 ? 0.2182 0.1625 0.1934 -0.0158 0.0671  -0.0155 472 GLN A CD  
4095  O OE1 A GLN A 249 ? 0.1661 0.2334 0.2588 0.0170  0.0333  0.0322  472 GLN A OE1 
4096  O OE1 B GLN A 249 ? 0.2322 0.1711 0.2102 -0.0260 0.0728  -0.0157 472 GLN A OE1 
4097  N NE2 A GLN A 249 ? 0.1679 0.2173 0.2168 0.0169  0.0306  0.0577  472 GLN A NE2 
4098  N NE2 B GLN A 249 ? 0.2248 0.1650 0.2004 -0.0194 0.0683  -0.0203 472 GLN A NE2 
4115  N N   . THR A 250 ? 0.1514 0.1188 0.0996 0.0030  0.0165  0.0210  473 THR A N   
4116  C CA  . THR A 250 ? 0.1479 0.1132 0.0923 -0.0128 0.0209  0.0157  473 THR A CA  
4117  C C   . THR A 250 ? 0.1449 0.1055 0.0863 -0.0157 0.0202  0.0076  473 THR A C   
4118  O O   . THR A 250 ? 0.1417 0.1104 0.1069 -0.0039 0.0066  0.0256  473 THR A O   
4119  C CB  . THR A 250 ? 0.1389 0.1231 0.0927 -0.0091 0.0221  0.0189  473 THR A CB  
4120  O OG1 . THR A 250 ? 0.1410 0.1254 0.0986 -0.0213 0.0161  0.0142  473 THR A OG1 
4121  C CG2 . THR A 250 ? 0.1477 0.1586 0.0994 -0.0068 0.0216  0.0192  473 THR A CG2 
4129  N N   . ASP A 251 ? 0.1446 0.1075 0.0807 -0.0179 0.0202  0.0093  474 ASP A N   
4130  C CA  . ASP A 251 ? 0.1265 0.1144 0.0872 0.0004  0.0028  0.0018  474 ASP A CA  
4131  C C   . ASP A 251 ? 0.1296 0.1005 0.0857 -0.0062 0.0118  0.0160  474 ASP A C   
4132  O O   . ASP A 251 ? 0.1159 0.1020 0.1009 -0.0042 -0.0116 0.0036  474 ASP A O   
4133  C CB  . ASP A 251 ? 0.1505 0.1381 0.1136 0.0089  -0.0133 0.0115  474 ASP A CB  
4134  C CG  . ASP A 251 ? 0.2023 0.1649 0.1242 0.0190  -0.0345 0.0105  474 ASP A CG  
4135  O OD1 . ASP A 251 ? 0.2149 0.1620 0.1205 0.0078  -0.0283 -0.0053 474 ASP A OD1 
4136  O OD2 . ASP A 251 ? 0.2299 0.1984 0.1526 0.0070  -0.0438 -0.0103 474 ASP A OD2 
4141  N N   . VAL A 252 ? 0.1338 0.0965 0.0779 -0.0152 0.0099  0.0080  475 VAL A N   
4142  C CA  . VAL A 252 ? 0.1265 0.0951 0.0968 -0.0265 0.0063  -0.0033 475 VAL A CA  
4143  C C   . VAL A 252 ? 0.0874 0.1036 0.0973 -0.0211 -0.0070 -0.0024 475 VAL A C   
4144  O O   . VAL A 252 ? 0.1034 0.1218 0.1155 -0.0340 0.0044  0.0044  475 VAL A O   
4145  C CB  . VAL A 252 ? 0.1324 0.0907 0.1292 -0.0122 0.0118  -0.0068 475 VAL A CB  
4146  C CG1 . VAL A 252 ? 0.1482 0.0993 0.1387 -0.0228 0.0074  -0.0094 475 VAL A CG1 
4147  C CG2 . VAL A 252 ? 0.1270 0.0837 0.1388 -0.0033 0.0066  0.0015  475 VAL A CG2 
4157  N N   . ALA A 253 ? 0.0851 0.1049 0.0952 -0.0201 -0.0098 0.0101  476 ALA A N   
4158  C CA  . ALA A 253 ? 0.1014 0.1197 0.0925 -0.0198 0.0118  0.0008  476 ALA A CA  
4159  C C   . ALA A 253 ? 0.0940 0.1221 0.0955 -0.0164 0.0039  0.0116  476 ALA A C   
4160  O O   . ALA A 253 ? 0.0731 0.1582 0.1099 -0.0111 -0.0047 -0.0203 476 ALA A O   
4161  C CB  . ALA A 253 ? 0.1152 0.1163 0.1097 0.0002  -0.0220 0.0060  476 ALA A CB  
4167  N N   . LEU A 254 ? 0.0729 0.1121 0.0993 -0.0199 0.0014  0.0073  477 LEU A N   
4168  C CA  . LEU A 254 ? 0.0876 0.0970 0.0982 -0.0150 0.0102  0.0108  477 LEU A CA  
4169  C C   . LEU A 254 ? 0.0895 0.0920 0.1014 -0.0116 0.0007  -0.0108 477 LEU A C   
4170  O O   . LEU A 254 ? 0.0871 0.1122 0.1066 0.0128  0.0036  -0.0074 477 LEU A O   
4171  C CB  . LEU A 254 ? 0.1042 0.1021 0.1178 -0.0197 0.0058  0.0093  477 LEU A CB  
4172  C CG  . LEU A 254 ? 0.1140 0.1220 0.1302 -0.0265 0.0075  0.0005  477 LEU A CG  
4173  C CD1 . LEU A 254 ? 0.1336 0.1209 0.1393 -0.0237 -0.0058 0.0006  477 LEU A CD1 
4174  C CD2 . LEU A 254 ? 0.1186 0.1371 0.1501 -0.0347 0.0099  0.0060  477 LEU A CD2 
4186  N N   . ILE A 255 ? 0.0855 0.0912 0.0999 -0.0182 -0.0084 -0.0054 478 ILE A N   
4187  C CA  . ILE A 255 ? 0.0949 0.0871 0.0898 -0.0125 -0.0149 0.0120  478 ILE A CA  
4188  C C   . ILE A 255 ? 0.0863 0.0877 0.1039 0.0004  -0.0180 0.0133  478 ILE A C   
4189  O O   . ILE A 255 ? 0.1115 0.0865 0.0951 -0.0067 -0.0158 0.0081  478 ILE A O   
4190  C CB  . ILE A 255 ? 0.0948 0.0958 0.0904 0.0111  -0.0055 0.0163  478 ILE A CB  
4191  C CG1 . ILE A 255 ? 0.0946 0.0963 0.0962 -0.0057 0.0004  0.0132  478 ILE A CG1 
4192  C CG2 . ILE A 255 ? 0.0904 0.1100 0.1006 0.0043  -0.0104 -0.0036 478 ILE A CG2 
4193  C CD1 . ILE A 255 ? 0.1040 0.1039 0.0795 -0.0024 -0.0134 0.0038  478 ILE A CD1 
4205  N N   . ARG A 256 ? 0.0926 0.0847 0.1124 -0.0029 -0.0135 0.0002  479 ARG A N   
4206  C CA  . ARG A 256 ? 0.1007 0.1008 0.1065 -0.0244 -0.0223 -0.0027 479 ARG A CA  
4207  C C   . ARG A 256 ? 0.1040 0.0827 0.1025 -0.0188 -0.0327 0.0033  479 ARG A C   
4208  O O   . ARG A 256 ? 0.1075 0.0827 0.1129 -0.0173 -0.0160 -0.0022 479 ARG A O   
4209  C CB  . ARG A 256 ? 0.1198 0.1354 0.1352 -0.0427 -0.0330 0.0153  479 ARG A CB  
4210  C CG  . ARG A 256 ? 0.1408 0.1590 0.1889 -0.0215 -0.0205 0.0272  479 ARG A CG  
4211  C CD  . ARG A 256 ? 0.1585 0.1563 0.2262 -0.0096 0.0040  0.0365  479 ARG A CD  
4212  N NE  . ARG A 256 ? 0.1696 0.1632 0.2471 -0.0019 0.0089  0.0607  479 ARG A NE  
4213  C CZ  . ARG A 256 ? 0.1847 0.1893 0.2880 -0.0087 -0.0008 0.0811  479 ARG A CZ  
4214  N NH1 . ARG A 256 ? 0.1887 0.2214 0.3397 0.0133  0.0304  0.0815  479 ARG A NH1 
4215  N NH2 . ARG A 256 ? 0.1953 0.2029 0.2921 -0.0355 0.0007  0.0840  479 ARG A NH2 
4229  N N   . TYR A 257 ? 0.1308 0.0749 0.0992 -0.0218 -0.0175 -0.0022 480 TYR A N   
4230  C CA  . TYR A 257 ? 0.1224 0.0744 0.0927 -0.0064 -0.0214 0.0050  480 TYR A CA  
4231  C C   . TYR A 257 ? 0.1197 0.0879 0.1117 -0.0166 -0.0133 -0.0087 480 TYR A C   
4232  O O   . TYR A 257 ? 0.1202 0.0958 0.1282 -0.0224 -0.0327 -0.0068 480 TYR A O   
4233  C CB  . TYR A 257 ? 0.1434 0.0859 0.1129 -0.0188 -0.0082 -0.0101 480 TYR A CB  
4234  C CG  . TYR A 257 ? 0.1476 0.0885 0.1225 -0.0109 0.0086  -0.0007 480 TYR A CG  
4235  C CD1 . TYR A 257 ? 0.1281 0.1011 0.1408 -0.0202 -0.0141 0.0010  480 TYR A CD1 
4236  C CD2 . TYR A 257 ? 0.1727 0.1024 0.1392 -0.0339 0.0079  -0.0105 480 TYR A CD2 
4237  C CE1 . TYR A 257 ? 0.1441 0.0987 0.1553 -0.0155 -0.0094 -0.0056 480 TYR A CE1 
4238  C CE2 . TYR A 257 ? 0.1637 0.1012 0.1475 -0.0367 0.0033  0.0031  480 TYR A CE2 
4239  C CZ  . TYR A 257 ? 0.1444 0.0937 0.1367 -0.0297 -0.0199 0.0105  480 TYR A CZ  
4240  O OH  . TYR A 257 ? 0.1633 0.1076 0.1484 -0.0381 -0.0013 -0.0054 480 TYR A OH  
4250  N N   A VAL A 258 ? 0.1013 0.0858 0.1028 -0.0237 -0.0233 -0.0060 481 VAL A N   
4251  C CA  A VAL A 258 ? 0.1019 0.1148 0.1138 -0.0215 -0.0467 -0.0014 481 VAL A CA  
4252  C C   A VAL A 258 ? 0.1251 0.1060 0.1042 -0.0249 -0.0561 -0.0037 481 VAL A C   
4253  O O   A VAL A 258 ? 0.1434 0.1139 0.0897 -0.0209 -0.0457 0.0019  481 VAL A O   
4254  C CB  A VAL A 258 ? 0.1371 0.1533 0.1414 -0.0074 -0.0423 0.0075  481 VAL A CB  
4255  C CG1 A VAL A 258 ? 0.1506 0.1711 0.1421 -0.0076 -0.0274 0.0102  481 VAL A CG1 
4256  C CG2 A VAL A 258 ? 0.1595 0.1745 0.1697 -0.0035 -0.0431 0.0027  481 VAL A CG2 
4266  N N   . ASN A 259 ? 0.1461 0.1128 0.1127 -0.0452 -0.0423 -0.0042 482 ASN A N   
4267  C CA  . ASN A 259 ? 0.1718 0.1246 0.1106 -0.0240 -0.0414 -0.0092 482 ASN A CA  
4268  C C   . ASN A 259 ? 0.1745 0.1170 0.1326 -0.0236 -0.0599 -0.0082 482 ASN A C   
4269  O O   . ASN A 259 ? 0.1591 0.1319 0.1503 -0.0123 -0.0527 -0.0242 482 ASN A O   
4270  C CB  . ASN A 259 ? 0.1795 0.1287 0.0957 -0.0171 -0.0582 -0.0133 482 ASN A CB  
4271  C CG  . ASN A 259 ? 0.1989 0.1325 0.1241 -0.0308 -0.0542 -0.0050 482 ASN A CG  
4272  O OD1 . ASN A 259 ? 0.2071 0.1232 0.1415 -0.0185 -0.0639 0.0147  482 ASN A OD1 
4273  N ND2 . ASN A 259 ? 0.2156 0.1442 0.1113 -0.0279 -0.0448 -0.0095 482 ASN A ND2 
4280  N N   . PRO A 260 ? 0.1928 0.1065 0.1623 -0.0139 -0.0736 -0.0020 483 PRO A N   
4281  C CA  . PRO A 260 ? 0.2216 0.1195 0.1981 0.0018  -0.0668 0.0029  483 PRO A CA  
4282  C C   . PRO A 260 ? 0.2220 0.1376 0.2220 0.0087  -0.1042 0.0069  483 PRO A C   
4283  O O   . PRO A 260 ? 0.2352 0.1746 0.2668 0.0064  -0.0789 -0.0026 483 PRO A O   
4284  C CB  . PRO A 260 ? 0.2358 0.1150 0.1937 0.0017  -0.0649 -0.0080 483 PRO A CB  
4285  C CG  . PRO A 260 ? 0.2353 0.1094 0.2002 -0.0068 -0.0452 0.0018  483 PRO A CG  
4286  C CD  . PRO A 260 ? 0.2122 0.1056 0.1730 -0.0296 -0.0597 0.0028  483 PRO A CD  
4294  N N   . GLU A 261 ? 0.2335 0.1270 0.2019 -0.0028 -0.1295 0.0058  484 GLU A N   
4295  C CA  . GLU A 261 ? 0.2432 0.1485 0.2088 -0.0137 -0.1341 0.0148  484 GLU A CA  
4296  C C   . GLU A 261 ? 0.2257 0.1524 0.2227 -0.0122 -0.1339 0.0176  484 GLU A C   
4297  O O   . GLU A 261 ? 0.2291 0.1711 0.2698 -0.0053 -0.1387 0.0217  484 GLU A O   
4298  C CB  . GLU A 261 ? 0.2723 0.1904 0.2140 -0.0066 -0.1413 0.0213  484 GLU A CB  
4299  C CG  . GLU A 261 ? 0.3126 0.2452 0.2359 0.0106  -0.1222 0.0280  484 GLU A CG  
4300  C CD  . GLU A 261 ? 0.3524 0.3013 0.2670 0.0157  -0.0890 0.0296  484 GLU A CD  
4301  O OE1 . GLU A 261 ? 0.3610 0.3109 0.2861 0.0327  -0.0688 0.0235  484 GLU A OE1 
4302  O OE2 . GLU A 261 ? 0.3857 0.3395 0.3051 0.0093  -0.0499 0.0303  484 GLU A OE2 
4309  N N   . THR A 262 ? 0.2155 0.1413 0.2321 -0.0181 -0.1234 0.0209  485 THR A N   
4310  C CA  . THR A 262 ? 0.1939 0.1503 0.2286 -0.0213 -0.1005 0.0093  485 THR A CA  
4311  C C   . THR A 262 ? 0.1848 0.1741 0.2421 -0.0262 -0.0947 0.0047  485 THR A C   
4312  O O   . THR A 262 ? 0.1820 0.1954 0.2683 -0.0382 -0.0979 0.0106  485 THR A O   
4313  C CB  . THR A 262 ? 0.2033 0.1487 0.2053 -0.0272 -0.0681 0.0105  485 THR A CB  
4314  O OG1 . THR A 262 ? 0.1920 0.1292 0.1740 -0.0238 -0.0906 -0.0110 485 THR A OG1 
4315  C CG2 . THR A 262 ? 0.2082 0.1579 0.1943 -0.0379 -0.0534 0.0158  485 THR A CG2 
4323  N N   . GLY A 263 ? 0.1836 0.1696 0.2170 -0.0005 -0.0721 0.0012  486 GLY A N   
4324  C CA  . GLY A 263 ? 0.1864 0.1736 0.1962 0.0136  -0.0503 -0.0097 486 GLY A CA  
4325  C C   . GLY A 263 ? 0.1943 0.1804 0.2056 0.0074  0.0058  -0.0067 486 GLY A C   
4326  O O   . GLY A 263 ? 0.2715 0.2032 0.2551 0.0162  0.0742  -0.0015 486 GLY A O   
4330  N N   . ARG A 264 ? 0.1414 0.1553 0.1651 -0.0113 -0.0418 -0.0245 487 ARG A N   
4331  C CA  . ARG A 264 ? 0.1338 0.1554 0.1512 -0.0184 -0.0393 -0.0156 487 ARG A CA  
4332  C C   . ARG A 264 ? 0.1303 0.1462 0.1362 -0.0384 -0.0477 -0.0124 487 ARG A C   
4333  O O   . ARG A 264 ? 0.1302 0.1389 0.1368 -0.0311 -0.0433 -0.0183 487 ARG A O   
4334  C CB  . ARG A 264 ? 0.1494 0.1659 0.1649 -0.0289 -0.0341 -0.0333 487 ARG A CB  
4335  C CG  . ARG A 264 ? 0.1672 0.1916 0.1538 -0.0434 -0.0273 -0.0461 487 ARG A CG  
4336  C CD  . ARG A 264 ? 0.1928 0.2032 0.1586 -0.0442 -0.0003 -0.0487 487 ARG A CD  
4337  N NE  . ARG A 264 ? 0.1831 0.1806 0.1467 -0.0429 -0.0056 -0.0279 487 ARG A NE  
4338  C CZ  . ARG A 264 ? 0.2179 0.1687 0.1683 -0.0545 0.0011  -0.0367 487 ARG A CZ  
4339  N NH1 . ARG A 264 ? 0.2398 0.1604 0.1957 -0.0421 0.0122  -0.0381 487 ARG A NH1 
4340  N NH2 . ARG A 264 ? 0.2266 0.1567 0.1560 -0.0824 -0.0045 -0.0406 487 ARG A NH2 
4354  N N   . VAL A 265 ? 0.1615 0.1536 0.1459 -0.0346 -0.0289 -0.0101 488 VAL A N   
4355  C CA  A VAL A 265 ? 0.1627 0.1536 0.1440 -0.0300 -0.0241 -0.0118 488 VAL A CA  
4356  C CA  B VAL A 265 ? 0.1570 0.1543 0.1476 -0.0241 -0.0313 -0.0088 488 VAL A CA  
4357  C C   . VAL A 265 ? 0.1526 0.1365 0.1450 -0.0380 -0.0319 -0.0218 488 VAL A C   
4358  O O   . VAL A 265 ? 0.1674 0.1613 0.2075 -0.0591 -0.0360 -0.0565 488 VAL A O   
4359  C CB  A VAL A 265 ? 0.1886 0.1649 0.1496 -0.0349 -0.0072 -0.0322 488 VAL A CB  
4360  C CB  B VAL A 265 ? 0.1629 0.1702 0.1548 -0.0072 -0.0333 -0.0070 488 VAL A CB  
4361  C CG1 A VAL A 265 ? 0.2007 0.1648 0.1407 -0.0263 -0.0159 -0.0286 488 VAL A CG1 
4362  C CG1 B VAL A 265 ? 0.1648 0.1771 0.1540 -0.0068 -0.0448 -0.0220 488 VAL A CG1 
4363  C CG2 A VAL A 265 ? 0.1997 0.1832 0.1910 -0.0411 0.0150  -0.0227 488 VAL A CG2 
4364  C CG2 B VAL A 265 ? 0.1588 0.1774 0.1581 0.0022  -0.0440 0.0130  488 VAL A CG2 
4383  N N   B LEU A 266 ? 0.1259 0.1111 0.1074 -0.0246 -0.0363 -0.0022 489 LEU A N   
4384  C CA  B LEU A 266 ? 0.1440 0.1220 0.1012 -0.0170 -0.0392 -0.0016 489 LEU A CA  
4385  C C   B LEU A 266 ? 0.1257 0.0961 0.1122 -0.0159 -0.0356 0.0066  489 LEU A C   
4386  O O   B LEU A 266 ? 0.1446 0.0865 0.1190 -0.0201 -0.0341 -0.0180 489 LEU A O   
4387  C CB  B LEU A 266 ? 0.1865 0.1692 0.1205 -0.0230 -0.0212 0.0092  489 LEU A CB  
4388  C CG  B LEU A 266 ? 0.2308 0.2166 0.1505 -0.0207 -0.0228 0.0143  489 LEU A CG  
4389  C CD1 B LEU A 266 ? 0.2712 0.2521 0.2058 -0.0092 -0.0078 0.0361  489 LEU A CD1 
4390  C CD2 B LEU A 266 ? 0.2583 0.2265 0.1520 -0.0007 -0.0072 0.0123  489 LEU A CD2 
4402  N N   . PHE A 267 ? 0.1131 0.0867 0.1007 -0.0208 -0.0514 0.0097  490 PHE A N   
4403  C CA  . PHE A 267 ? 0.1225 0.0848 0.0916 -0.0261 -0.0343 -0.0056 490 PHE A CA  
4404  C C   . PHE A 267 ? 0.1165 0.0784 0.0922 -0.0251 -0.0259 -0.0041 490 PHE A C   
4405  O O   . PHE A 267 ? 0.1260 0.0785 0.1003 -0.0235 -0.0216 -0.0046 490 PHE A O   
4406  C CB  . PHE A 267 ? 0.1194 0.0838 0.1090 -0.0303 -0.0208 -0.0027 490 PHE A CB  
4407  C CG  . PHE A 267 ? 0.1046 0.0782 0.0958 -0.0173 -0.0357 0.0076  490 PHE A CG  
4408  C CD1 . PHE A 267 ? 0.1180 0.0750 0.0963 -0.0166 -0.0312 0.0065  490 PHE A CD1 
4409  C CD2 . PHE A 267 ? 0.1098 0.0929 0.1172 -0.0214 -0.0338 0.0125  490 PHE A CD2 
4410  C CE1 . PHE A 267 ? 0.1260 0.0857 0.1084 -0.0171 -0.0118 0.0084  490 PHE A CE1 
4411  C CE2 . PHE A 267 ? 0.1234 0.1006 0.1061 -0.0338 -0.0316 0.0065  490 PHE A CE2 
4412  C CZ  . PHE A 267 ? 0.1188 0.0914 0.1254 -0.0334 0.0020  -0.0038 490 PHE A CZ  
4422  N N   . GLU A 268 ? 0.1106 0.0712 0.1021 -0.0180 -0.0266 -0.0037 491 GLU A N   
4423  C CA  . GLU A 268 ? 0.1019 0.0710 0.0966 -0.0143 -0.0175 -0.0112 491 GLU A CA  
4424  C C   . GLU A 268 ? 0.0964 0.0660 0.0977 -0.0170 -0.0002 -0.0004 491 GLU A C   
4425  O O   . GLU A 268 ? 0.1058 0.0757 0.0979 -0.0181 -0.0198 -0.0108 491 GLU A O   
4426  C CB  . GLU A 268 ? 0.1103 0.0841 0.1167 -0.0095 -0.0155 0.0010  491 GLU A CB  
4427  C CG  . GLU A 268 ? 0.1283 0.1018 0.1293 -0.0120 -0.0034 0.0017  491 GLU A CG  
4428  C CD  . GLU A 268 ? 0.1246 0.1137 0.1433 -0.0215 0.0048  -0.0063 491 GLU A CD  
4429  O OE1 . GLU A 268 ? 0.1404 0.1208 0.1631 -0.0325 0.0086  -0.0105 491 GLU A OE1 
4430  O OE2 . GLU A 268 ? 0.1229 0.1224 0.1432 -0.0157 0.0049  -0.0058 491 GLU A OE2 
4437  N N   . ALA A 269 ? 0.0700 0.0731 0.1081 -0.0084 -0.0008 -0.0094 492 ALA A N   
4438  C CA  . ALA A 269 ? 0.0797 0.0682 0.0866 -0.0167 -0.0071 0.0068  492 ALA A CA  
4439  C C   . ALA A 269 ? 0.0931 0.0731 0.0896 -0.0302 -0.0047 -0.0009 492 ALA A C   
4440  O O   . ALA A 269 ? 0.0988 0.0802 0.0971 -0.0175 -0.0046 0.0007  492 ALA A O   
4441  C CB  . ALA A 269 ? 0.0927 0.0718 0.0892 -0.0198 0.0000  -0.0033 492 ALA A CB  
4447  N N   . LYS A 270 ? 0.0931 0.0794 0.0756 -0.0104 -0.0003 0.0048  493 LYS A N   
4448  C CA  . LYS A 270 ? 0.0836 0.0902 0.0780 -0.0087 -0.0115 -0.0047 493 LYS A CA  
4449  C C   . LYS A 270 ? 0.0862 0.0827 0.1040 -0.0075 -0.0061 -0.0167 493 LYS A C   
4450  O O   . LYS A 270 ? 0.1051 0.1044 0.1321 -0.0024 0.0152  -0.0472 493 LYS A O   
4451  C CB  . LYS A 270 ? 0.1122 0.1040 0.0876 -0.0139 -0.0076 0.0068  493 LYS A CB  
4452  C CG  . LYS A 270 ? 0.1608 0.1146 0.1314 -0.0118 0.0075  0.0084  493 LYS A CG  
4453  C CD  . LYS A 270 ? 0.2018 0.1335 0.1731 0.0131  0.0355  0.0116  493 LYS A CD  
4454  C CE  . LYS A 270 ? 0.2030 0.1361 0.1592 0.0105  0.0176  0.0301  493 LYS A CE  
4455  N NZ  . LYS A 270 ? 0.1436 0.1013 0.1259 -0.0285 -0.0011 0.0296  493 LYS A NZ  
4469  N N   . LEU A 271 ? 0.0687 0.0782 0.0901 -0.0122 -0.0235 -0.0133 494 LEU A N   
4470  C CA  . LEU A 271 ? 0.0788 0.0783 0.0779 -0.0063 -0.0080 -0.0034 494 LEU A CA  
4471  C C   . LEU A 271 ? 0.0783 0.0825 0.0660 -0.0164 -0.0045 0.0050  494 LEU A C   
4472  O O   . LEU A 271 ? 0.0946 0.0911 0.0734 -0.0107 -0.0043 0.0112  494 LEU A O   
4473  C CB  . LEU A 271 ? 0.0813 0.0914 0.0815 -0.0007 -0.0044 0.0122  494 LEU A CB  
4474  C CG  . LEU A 271 ? 0.0854 0.0764 0.0966 -0.0054 -0.0084 0.0063  494 LEU A CG  
4475  C CD1 . LEU A 271 ? 0.1166 0.0654 0.1021 -0.0099 0.0045  0.0044  494 LEU A CD1 
4476  C CD2 . LEU A 271 ? 0.1068 0.0928 0.1100 0.0058  -0.0173 0.0272  494 LEU A CD2 
4488  N N   . HIS A 272 ? 0.0835 0.0758 0.0703 -0.0037 -0.0016 0.0063  495 HIS A N   
4489  C CA  . HIS A 272 ? 0.0986 0.0731 0.0790 -0.0069 -0.0020 0.0078  495 HIS A CA  
4490  C C   . HIS A 272 ? 0.1061 0.0739 0.0781 -0.0008 -0.0101 0.0003  495 HIS A C   
4491  O O   . HIS A 272 ? 0.1039 0.0764 0.0683 -0.0168 0.0036  0.0096  495 HIS A O   
4492  C CB  . HIS A 272 ? 0.1040 0.0732 0.0903 -0.0215 0.0036  0.0070  495 HIS A CB  
4493  C CG  . HIS A 272 ? 0.0950 0.0719 0.0895 -0.0134 -0.0242 0.0100  495 HIS A CG  
4494  N ND1 . HIS A 272 ? 0.1187 0.0795 0.1243 -0.0224 -0.0045 0.0240  495 HIS A ND1 
4495  C CD2 . HIS A 272 ? 0.1186 0.0804 0.1067 -0.0012 -0.0077 0.0106  495 HIS A CD2 
4496  C CE1 . HIS A 272 ? 0.1208 0.0753 0.1020 -0.0434 0.0108  0.0118  495 HIS A CE1 
4497  N NE2 . HIS A 272 ? 0.1176 0.0830 0.1078 -0.0240 0.0077  0.0046  495 HIS A NE2 
4505  N N   . ARG A 273 ? 0.1018 0.0857 0.0761 -0.0153 -0.0045 -0.0049 496 ARG A N   
4506  C CA  . ARG A 273 ? 0.1087 0.0896 0.0927 -0.0038 0.0007  0.0016  496 ARG A CA  
4507  C C   . ARG A 273 ? 0.1068 0.0847 0.0873 -0.0153 -0.0039 -0.0044 496 ARG A C   
4508  O O   . ARG A 273 ? 0.1194 0.0849 0.0952 -0.0111 0.0047  -0.0105 496 ARG A O   
4509  C CB  . ARG A 273 ? 0.1334 0.1122 0.0970 -0.0204 0.0028  -0.0113 496 ARG A CB  
4510  C CG  . ARG A 273 ? 0.1865 0.1265 0.1088 -0.0213 0.0297  -0.0141 496 ARG A CG  
4511  C CD  . ARG A 273 ? 0.2314 0.1387 0.1287 -0.0163 0.0383  -0.0085 496 ARG A CD  
4512  N NE  . ARG A 273 ? 0.2765 0.1519 0.1554 -0.0206 0.0558  -0.0154 496 ARG A NE  
4513  C CZ  . ARG A 273 ? 0.3380 0.1722 0.1681 -0.0325 0.0718  -0.0316 496 ARG A CZ  
4514  N NH1 . ARG A 273 ? 0.3747 0.1905 0.1798 -0.0396 0.0950  -0.0381 496 ARG A NH1 
4515  N NH2 . ARG A 273 ? 0.3645 0.1684 0.1858 -0.0376 0.0853  -0.0568 496 ARG A NH2 
4529  N N   . GLN A 274 ? 0.0947 0.0824 0.0904 -0.0162 -0.0362 0.0008  497 GLN A N   
4530  C CA  . GLN A 274 ? 0.1140 0.1045 0.0986 -0.0065 -0.0341 -0.0091 497 GLN A CA  
4531  C C   . GLN A 274 ? 0.0993 0.0965 0.1058 -0.0039 -0.0136 -0.0100 497 GLN A C   
4532  O O   . GLN A 274 ? 0.0984 0.1360 0.1229 -0.0238 -0.0044 0.0051  497 GLN A O   
4533  C CB  . GLN A 274 ? 0.1738 0.1635 0.1422 -0.0013 -0.0323 0.0119  497 GLN A CB  
4534  C CG  . GLN A 274 ? 0.2468 0.2122 0.2038 0.0012  -0.0404 0.0089  497 GLN A CG  
4535  C CD  . GLN A 274 ? 0.2912 0.2528 0.2583 -0.0055 -0.0464 0.0014  497 GLN A CD  
4536  O OE1 . GLN A 274 ? 0.3127 0.2591 0.2576 -0.0210 -0.0706 -0.0012 497 GLN A OE1 
4537  N NE2 . GLN A 274 ? 0.2839 0.2744 0.2991 -0.0082 -0.0497 0.0044  497 GLN A NE2 
4546  N N   . GLY A 275 ? 0.0974 0.0910 0.0958 -0.0140 -0.0130 -0.0055 498 GLY A N   
4547  C CA  . GLY A 275 ? 0.0773 0.0819 0.0922 -0.0131 -0.0210 0.0023  498 GLY A CA  
4548  C C   . GLY A 275 ? 0.0897 0.0784 0.0897 -0.0079 -0.0061 0.0090  498 GLY A C   
4549  O O   . GLY A 275 ? 0.1141 0.0823 0.1039 -0.0246 0.0271  0.0019  498 GLY A O   
4553  N N   . PHE A 276 ? 0.0802 0.0768 0.0884 -0.0134 0.0088  0.0100  499 PHE A N   
4554  C CA  . PHE A 276 ? 0.0719 0.0842 0.0866 -0.0220 -0.0049 -0.0077 499 PHE A CA  
4555  C C   . PHE A 276 ? 0.0737 0.0772 0.0727 -0.0067 0.0037  0.0066  499 PHE A C   
4556  O O   . PHE A 276 ? 0.0852 0.0878 0.0886 -0.0120 0.0041  -0.0148 499 PHE A O   
4557  C CB  . PHE A 276 ? 0.0896 0.1079 0.0900 -0.0098 -0.0155 -0.0003 499 PHE A CB  
4558  C CG  . PHE A 276 ? 0.0954 0.1005 0.1057 -0.0005 -0.0157 0.0046  499 PHE A CG  
4559  C CD1 . PHE A 276 ? 0.1087 0.1127 0.1121 -0.0071 -0.0164 0.0225  499 PHE A CD1 
4560  C CD2 . PHE A 276 ? 0.1078 0.1063 0.1220 -0.0186 -0.0270 0.0056  499 PHE A CD2 
4561  C CE1 . PHE A 276 ? 0.1138 0.1218 0.1185 0.0055  -0.0145 0.0281  499 PHE A CE1 
4562  C CE2 . PHE A 276 ? 0.1229 0.1092 0.1381 -0.0237 -0.0289 0.0128  499 PHE A CE2 
4563  C CZ  . PHE A 276 ? 0.1333 0.1262 0.1322 -0.0167 -0.0148 0.0365  499 PHE A CZ  
4573  N N   . ILE A 277 ? 0.0835 0.0723 0.0797 -0.0059 0.0019  0.0035  500 ILE A N   
4574  C CA  . ILE A 277 ? 0.0716 0.0662 0.0906 -0.0249 -0.0032 -0.0046 500 ILE A CA  
4575  C C   . ILE A 277 ? 0.0746 0.0646 0.0915 -0.0141 -0.0056 0.0009  500 ILE A C   
4576  O O   . ILE A 277 ? 0.0886 0.0617 0.0988 -0.0072 -0.0013 -0.0004 500 ILE A O   
4577  C CB  . ILE A 277 ? 0.0811 0.0663 0.0929 -0.0218 -0.0008 -0.0018 500 ILE A CB  
4578  C CG1 . ILE A 277 ? 0.0776 0.0720 0.1141 -0.0070 -0.0214 -0.0083 500 ILE A CG1 
4579  C CG2 . ILE A 277 ? 0.0982 0.0667 0.0821 -0.0146 -0.0124 0.0074  500 ILE A CG2 
4580  C CD1 . ILE A 277 ? 0.0968 0.0834 0.1189 -0.0066 -0.0185 0.0032  500 ILE A CD1 
4592  N N   . THR A 278 ? 0.0739 0.0742 0.0892 -0.0083 0.0058  0.0027  501 THR A N   
4593  C CA  . THR A 278 ? 0.0742 0.0678 0.0868 -0.0066 -0.0025 0.0075  501 THR A CA  
4594  C C   . THR A 278 ? 0.0688 0.0702 0.1058 0.0022  0.0020  0.0061  501 THR A C   
4595  O O   . THR A 278 ? 0.0895 0.0707 0.1006 -0.0129 -0.0049 0.0018  501 THR A O   
4596  C CB  . THR A 278 ? 0.0924 0.0709 0.0868 0.0020  -0.0056 0.0025  501 THR A CB  
4597  O OG1 . THR A 278 ? 0.1013 0.0901 0.1030 -0.0035 -0.0024 0.0168  501 THR A OG1 
4598  C CG2 . THR A 278 ? 0.0955 0.0917 0.0910 0.0051  -0.0285 -0.0009 501 THR A CG2 
4606  N N   . VAL A 279 ? 0.0782 0.0688 0.0971 0.0001  0.0001  -0.0040 502 VAL A N   
4607  C CA  . VAL A 279 ? 0.0824 0.0655 0.1056 -0.0190 -0.0064 -0.0033 502 VAL A CA  
4608  C C   . VAL A 279 ? 0.0974 0.0557 0.1168 -0.0016 -0.0191 0.0001  502 VAL A C   
4609  O O   . VAL A 279 ? 0.0927 0.0688 0.1325 -0.0028 -0.0166 0.0166  502 VAL A O   
4610  C CB  . VAL A 279 ? 0.0959 0.0642 0.0936 -0.0254 -0.0060 0.0006  502 VAL A CB  
4611  C CG1 . VAL A 279 ? 0.1010 0.0671 0.1026 -0.0204 -0.0021 0.0097  502 VAL A CG1 
4612  C CG2 . VAL A 279 ? 0.1012 0.0952 0.0955 -0.0164 0.0140  0.0073  502 VAL A CG2 
4622  N N   . ALA A 280 ? 0.1124 0.0623 0.1031 -0.0029 -0.0255 -0.0047 503 ALA A N   
4623  C CA  . ALA A 280 ? 0.1179 0.0655 0.1109 -0.0188 -0.0045 0.0025  503 ALA A CA  
4624  C C   . ALA A 280 ? 0.1234 0.0699 0.1185 -0.0342 -0.0116 -0.0101 503 ALA A C   
4625  O O   . ALA A 280 ? 0.1392 0.0978 0.1306 -0.0085 -0.0165 0.0033  503 ALA A O   
4626  C CB  . ALA A 280 ? 0.1174 0.0755 0.1228 -0.0196 0.0248  -0.0015 503 ALA A CB  
4632  N N   . LYS A 281 ? 0.1333 0.0986 0.1227 -0.0176 -0.0253 -0.0209 504 LYS A N   
4633  C CA  . LYS A 281 ? 0.1446 0.1042 0.1364 -0.0324 -0.0020 -0.0351 504 LYS A CA  
4634  C C   . LYS A 281 ? 0.1509 0.1141 0.1519 -0.0185 0.0107  -0.0255 504 LYS A C   
4635  O O   . LYS A 281 ? 0.1314 0.1364 0.1591 -0.0145 0.0114  -0.0315 504 LYS A O   
4636  C CB  . LYS A 281 ? 0.1591 0.1204 0.1313 -0.0401 0.0056  -0.0310 504 LYS A CB  
4637  C CG  . LYS A 281 ? 0.1530 0.1347 0.1361 -0.0380 0.0042  -0.0315 504 LYS A CG  
4638  C CD  . LYS A 281 ? 0.1643 0.1479 0.1574 -0.0369 0.0040  -0.0403 504 LYS A CD  
4639  C CE  . LYS A 281 ? 0.1578 0.1531 0.1547 -0.0339 -0.0249 -0.0360 504 LYS A CE  
4640  N NZ  . LYS A 281 ? 0.1567 0.1551 0.1726 -0.0250 -0.0066 -0.0206 504 LYS A NZ  
4654  N N   . SER A 282 ? 0.1522 0.1110 0.1676 -0.0222 0.0047  -0.0280 505 SER A N   
4655  C CA  A SER A 282 ? 0.1754 0.1267 0.1941 -0.0137 0.0078  -0.0235 505 SER A CA  
4656  C CA  B SER A 282 ? 0.1729 0.1372 0.2019 -0.0112 0.0183  -0.0348 505 SER A CA  
4657  C C   . SER A 282 ? 0.1684 0.1527 0.1904 -0.0131 0.0135  -0.0536 505 SER A C   
4658  O O   . SER A 282 ? 0.1909 0.2162 0.2121 -0.0380 0.0141  -0.0772 505 SER A O   
4659  C CB  A SER A 282 ? 0.2124 0.1255 0.2212 0.0028  0.0106  0.0002  505 SER A CB  
4660  C CB  B SER A 282 ? 0.2041 0.1569 0.2435 0.0104  0.0407  -0.0348 505 SER A CB  
4661  O OG  A SER A 282 ? 0.2465 0.1290 0.2395 0.0154  0.0188  0.0219  505 SER A OG  
4662  O OG  B SER A 282 ? 0.2331 0.1778 0.2755 0.0278  0.0696  -0.0385 505 SER A OG  
4673  N N   . GLY A 283 ? 0.1618 0.1347 0.1711 0.0025  0.0265  -0.0339 506 GLY A N   
4674  C CA  . GLY A 283 ? 0.1703 0.1310 0.1759 0.0065  0.0250  -0.0295 506 GLY A CA  
4675  C C   . GLY A 283 ? 0.1603 0.1350 0.1688 0.0107  0.0140  -0.0296 506 GLY A C   
4676  O O   . GLY A 283 ? 0.1944 0.1305 0.1855 0.0087  0.0357  -0.0268 506 GLY A O   
4680  N N   . ASP A 284 ? 0.1346 0.1562 0.1814 0.0287  -0.0114 -0.0258 507 ASP A N   
4681  C CA  . ASP A 284 ? 0.1590 0.1756 0.1801 0.0218  -0.0255 -0.0236 507 ASP A CA  
4682  C C   . ASP A 284 ? 0.1749 0.1798 0.1825 0.0233  -0.0059 -0.0349 507 ASP A C   
4683  O O   . ASP A 284 ? 0.2076 0.2005 0.2123 0.0282  0.0128  -0.0312 507 ASP A O   
4684  C CB  . ASP A 284 ? 0.1683 0.1784 0.1857 0.0030  -0.0281 -0.0220 507 ASP A CB  
4685  C CG  . ASP A 284 ? 0.1767 0.1969 0.2114 0.0030  -0.0127 -0.0301 507 ASP A CG  
4686  O OD1 . ASP A 284 ? 0.1841 0.2022 0.2006 0.0083  -0.0107 -0.0239 507 ASP A OD1 
4687  O OD2 . ASP A 284 ? 0.2005 0.2121 0.2542 -0.0074 -0.0091 -0.0360 507 ASP A OD2 
4692  N N   . SER A 285 ? 0.1463 0.1638 0.1597 0.0207  -0.0086 -0.0419 508 SER A N   
4693  C CA  . SER A 285 ? 0.1348 0.1486 0.1697 0.0001  -0.0205 -0.0400 508 SER A CA  
4694  C C   . SER A 285 ? 0.1123 0.1500 0.1777 -0.0091 -0.0333 -0.0439 508 SER A C   
4695  O O   . SER A 285 ? 0.1239 0.1464 0.1827 -0.0010 -0.0267 -0.0360 508 SER A O   
4696  C CB  . SER A 285 ? 0.1448 0.1428 0.1786 -0.0003 -0.0064 -0.0288 508 SER A CB  
4697  O OG  . SER A 285 ? 0.1333 0.1394 0.1704 -0.0172 -0.0063 -0.0255 508 SER A OG  
4703  N N   . PRO A 286 ? 0.1335 0.1572 0.1691 0.0000  -0.0195 -0.0268 509 PRO A N   
4704  C CA  . PRO A 286 ? 0.1321 0.1711 0.1607 -0.0032 -0.0192 -0.0264 509 PRO A CA  
4705  C C   . PRO A 286 ? 0.1192 0.1483 0.1820 -0.0164 -0.0180 -0.0107 509 PRO A C   
4706  O O   . PRO A 286 ? 0.1209 0.1368 0.1980 -0.0177 -0.0254 -0.0242 509 PRO A O   
4707  C CB  . PRO A 286 ? 0.1523 0.1815 0.1614 0.0016  0.0003  -0.0263 509 PRO A CB  
4708  C CG  . PRO A 286 ? 0.1780 0.1903 0.1779 -0.0056 0.0122  -0.0144 509 PRO A CG  
4709  C CD  . PRO A 286 ? 0.1694 0.1790 0.1673 -0.0041 0.0144  -0.0208 509 PRO A CD  
4717  N N   . ILE A 287 ? 0.1065 0.1312 0.1811 -0.0262 -0.0284 0.0074  510 ILE A N   
4718  C CA  . ILE A 287 ? 0.1113 0.1226 0.1715 -0.0312 -0.0419 0.0044  510 ILE A CA  
4719  C C   . ILE A 287 ? 0.1170 0.1170 0.1635 -0.0282 -0.0364 0.0094  510 ILE A C   
4720  O O   . ILE A 287 ? 0.1397 0.1051 0.1905 -0.0340 -0.0402 0.0205  510 ILE A O   
4721  C CB  . ILE A 287 ? 0.1266 0.1169 0.1596 -0.0204 -0.0585 0.0027  510 ILE A CB  
4722  C CG1 . ILE A 287 ? 0.1445 0.1259 0.1547 -0.0202 -0.0735 -0.0082 510 ILE A CG1 
4723  C CG2 . ILE A 287 ? 0.1293 0.1144 0.1620 -0.0171 -0.0450 -0.0097 510 ILE A CG2 
4724  C CD1 . ILE A 287 ? 0.1629 0.1329 0.1493 -0.0209 -0.0659 -0.0316 510 ILE A CD1 
4736  N N   . ASN A 288 ? 0.1032 0.1322 0.1523 -0.0136 -0.0342 0.0050  511 ASN A N   
4737  C CA  . ASN A 288 ? 0.1118 0.1370 0.1446 -0.0035 -0.0310 -0.0023 511 ASN A CA  
4738  C C   . ASN A 288 ? 0.1174 0.1264 0.1436 0.0011  -0.0261 -0.0124 511 ASN A C   
4739  O O   . ASN A 288 ? 0.1240 0.1130 0.1486 -0.0047 -0.0183 -0.0225 511 ASN A O   
4740  C CB  . ASN A 288 ? 0.1159 0.1356 0.1353 -0.0011 -0.0252 -0.0174 511 ASN A CB  
4741  C CG  . ASN A 288 ? 0.1293 0.1307 0.1358 0.0045  -0.0026 -0.0248 511 ASN A CG  
4742  O OD1 . ASN A 288 ? 0.1562 0.1389 0.1465 0.0056  0.0374  -0.0210 511 ASN A OD1 
4743  N ND2 . ASN A 288 ? 0.1301 0.1237 0.1236 0.0135  0.0029  -0.0212 511 ASN A ND2 
4750  N N   . VAL A 289 ? 0.1252 0.1174 0.1602 -0.0159 -0.0111 -0.0383 512 VAL A N   
4751  C CA  . VAL A 289 ? 0.1525 0.1243 0.1497 -0.0020 -0.0185 -0.0324 512 VAL A CA  
4752  C C   . VAL A 289 ? 0.1747 0.1223 0.1417 -0.0191 -0.0127 -0.0328 512 VAL A C   
4753  O O   . VAL A 289 ? 0.1912 0.1468 0.1710 -0.0336 -0.0009 -0.0204 512 VAL A O   
4754  C CB  . VAL A 289 ? 0.1603 0.1359 0.1556 0.0025  -0.0415 -0.0236 512 VAL A CB  
4755  C CG1 . VAL A 289 ? 0.1689 0.1551 0.1440 -0.0022 -0.0303 -0.0147 512 VAL A CG1 
4756  C CG2 . VAL A 289 ? 0.1931 0.1393 0.1614 -0.0134 -0.0484 -0.0378 512 VAL A CG2 
4766  N N   A PRO A 290 ? 0.2015 0.1086 0.1120 -0.0027 -0.0279 -0.0031 513 PRO A N   
4767  C CA  A PRO A 290 ? 0.2138 0.1115 0.1148 -0.0076 -0.0340 -0.0034 513 PRO A CA  
4768  C C   A PRO A 290 ? 0.2112 0.1106 0.1046 -0.0012 -0.0247 -0.0036 513 PRO A C   
4769  O O   A PRO A 290 ? 0.2196 0.1191 0.1241 -0.0056 -0.0304 -0.0069 513 PRO A O   
4770  C CB  A PRO A 290 ? 0.2219 0.1269 0.1292 -0.0143 -0.0445 -0.0052 513 PRO A CB  
4771  C CG  A PRO A 290 ? 0.2134 0.1201 0.1492 -0.0018 -0.0335 0.0003  513 PRO A CG  
4772  C CD  A PRO A 290 ? 0.2093 0.1120 0.1425 0.0014  -0.0204 0.0019  513 PRO A CD  
4780  N N   . ALA A 291 ? 0.2199 0.1366 0.0997 -0.0066 -0.0189 -0.0139 514 ALA A N   
4781  C CA  . ALA A 291 ? 0.2273 0.1518 0.1243 -0.0346 0.0151  -0.0078 514 ALA A CA  
4782  C C   . ALA A 291 ? 0.2063 0.1411 0.0953 -0.0471 -0.0093 -0.0009 514 ALA A C   
4783  O O   . ALA A 291 ? 0.2103 0.1581 0.0983 -0.0554 0.0029  -0.0044 514 ALA A O   
4784  C CB  . ALA A 291 ? 0.2525 0.1679 0.1362 -0.0500 0.0506  -0.0258 514 ALA A CB  
4790  N N   . ASN A 292 ? 0.2062 0.1169 0.1137 -0.0401 -0.0138 -0.0053 515 ASN A N   
4791  C CA  . ASN A 292 ? 0.1894 0.1228 0.1228 -0.0133 -0.0333 -0.0020 515 ASN A CA  
4792  C C   . ASN A 292 ? 0.1712 0.1124 0.1170 -0.0096 -0.0373 -0.0012 515 ASN A C   
4793  O O   . ASN A 292 ? 0.1656 0.1192 0.1516 -0.0069 -0.0099 -0.0210 515 ASN A O   
4794  C CB  . ASN A 292 ? 0.1960 0.1396 0.1454 -0.0074 -0.0437 -0.0032 515 ASN A CB  
4795  C CG  . ASN A 292 ? 0.2079 0.1365 0.1653 -0.0207 -0.0466 0.0067  515 ASN A CG  
4796  O OD1 . ASN A 292 ? 0.2039 0.1215 0.1793 -0.0403 -0.0390 0.0102  515 ASN A OD1 
4797  N ND2 . ASN A 292 ? 0.2326 0.1419 0.1811 -0.0339 -0.0566 0.0396  515 ASN A ND2 
4804  N N   . GLY A 293 ? 0.1679 0.1149 0.1106 -0.0038 -0.0168 0.0137  516 GLY A N   
4805  C CA  . GLY A 293 ? 0.1423 0.1085 0.0859 -0.0199 -0.0057 -0.0021 516 GLY A CA  
4806  C C   . GLY A 293 ? 0.1175 0.0967 0.0873 -0.0165 -0.0225 0.0037  516 GLY A C   
4807  O O   . GLY A 293 ? 0.1337 0.1095 0.0914 -0.0168 -0.0125 0.0071  516 GLY A O   
4811  N N   . TYR A 294 ? 0.0915 0.1022 0.1012 -0.0249 -0.0200 -0.0009 517 TYR A N   
4812  C CA  . TYR A 294 ? 0.0999 0.0986 0.0840 -0.0120 -0.0234 -0.0083 517 TYR A CA  
4813  C C   . TYR A 294 ? 0.1071 0.0839 0.0910 -0.0128 -0.0184 -0.0050 517 TYR A C   
4814  O O   . TYR A 294 ? 0.1072 0.0858 0.1025 -0.0154 -0.0335 -0.0049 517 TYR A O   
4815  C CB  . TYR A 294 ? 0.1109 0.0933 0.1046 -0.0144 -0.0271 0.0005  517 TYR A CB  
4816  C CG  . TYR A 294 ? 0.1273 0.0893 0.1229 -0.0007 -0.0461 0.0034  517 TYR A CG  
4817  C CD1 . TYR A 294 ? 0.1221 0.1057 0.1513 -0.0007 -0.0358 -0.0055 517 TYR A CD1 
4818  C CD2 . TYR A 294 ? 0.1424 0.1368 0.1609 0.0317  -0.0553 0.0050  517 TYR A CD2 
4819  C CE1 . TYR A 294 ? 0.1263 0.1407 0.1879 0.0087  -0.0335 -0.0257 517 TYR A CE1 
4820  C CE2 . TYR A 294 ? 0.1372 0.1704 0.1845 0.0369  -0.0615 -0.0001 517 TYR A CE2 
4821  C CZ  . TYR A 294 ? 0.1309 0.1740 0.2273 0.0233  -0.0464 -0.0213 517 TYR A CZ  
4822  O OH  . TYR A 294 ? 0.1495 0.2117 0.2633 0.0192  -0.0505 -0.0295 517 TYR A OH  
4832  N N   . PHE A 295 ? 0.0884 0.0828 0.0769 -0.0147 -0.0238 -0.0021 518 PHE A N   
4833  C CA  . PHE A 295 ? 0.1056 0.0696 0.0887 -0.0115 -0.0078 0.0114  518 PHE A CA  
4834  C C   . PHE A 295 ? 0.1041 0.0681 0.0784 -0.0078 -0.0089 0.0188  518 PHE A C   
4835  O O   . PHE A 295 ? 0.1020 0.0781 0.1141 -0.0029 -0.0012 0.0119  518 PHE A O   
4836  C CB  . PHE A 295 ? 0.1096 0.0791 0.0776 -0.0157 -0.0150 0.0009  518 PHE A CB  
4837  C CG  . PHE A 295 ? 0.1081 0.0781 0.0819 -0.0125 -0.0339 0.0102  518 PHE A CG  
4838  C CD1 . PHE A 295 ? 0.1367 0.0838 0.0818 -0.0047 -0.0353 -0.0044 518 PHE A CD1 
4839  C CD2 . PHE A 295 ? 0.0958 0.0784 0.1128 -0.0099 -0.0272 -0.0079 518 PHE A CD2 
4840  C CE1 . PHE A 295 ? 0.1308 0.0930 0.0913 0.0060  -0.0195 -0.0056 518 PHE A CE1 
4841  C CE2 . PHE A 295 ? 0.0800 0.0900 0.1312 0.0082  -0.0344 -0.0027 518 PHE A CE2 
4842  C CZ  . PHE A 295 ? 0.1077 0.0896 0.1293 0.0194  -0.0322 -0.0183 518 PHE A CZ  
4852  N N   . ARG A 296 ? 0.0926 0.0692 0.0981 -0.0084 -0.0028 0.0141  519 ARG A N   
4853  C CA  . ARG A 296 ? 0.0950 0.0924 0.1019 0.0090  -0.0161 0.0213  519 ARG A CA  
4854  C C   . ARG A 296 ? 0.0784 0.0787 0.1024 -0.0049 -0.0210 0.0087  519 ARG A C   
4855  O O   . ARG A 296 ? 0.1111 0.0795 0.1007 -0.0071 0.0113  0.0110  519 ARG A O   
4856  C CB  . ARG A 296 ? 0.1186 0.1438 0.1335 0.0193  -0.0049 0.0341  519 ARG A CB  
4857  C CG  . ARG A 296 ? 0.1360 0.1886 0.1646 0.0144  -0.0300 0.0206  519 ARG A CG  
4858  C CD  . ARG A 296 ? 0.1509 0.2394 0.2013 0.0005  -0.0442 0.0148  519 ARG A CD  
4859  N NE  . ARG A 296 ? 0.1915 0.2754 0.2458 -0.0169 -0.0282 -0.0142 519 ARG A NE  
4860  C CZ  . ARG A 296 ? 0.2218 0.2960 0.2536 -0.0184 -0.0062 -0.0219 519 ARG A CZ  
4861  N NH1 . ARG A 296 ? 0.2133 0.3202 0.2366 -0.0222 -0.0381 -0.0281 519 ARG A NH1 
4862  N NH2 . ARG A 296 ? 0.2438 0.2947 0.2663 -0.0309 0.0220  -0.0355 519 ARG A NH2 
4876  N N   . PHE A 297 ? 0.0844 0.0906 0.1067 -0.0093 -0.0012 0.0099  520 PHE A N   
4877  C CA  . PHE A 297 ? 0.0989 0.1098 0.1075 0.0064  -0.0042 0.0068  520 PHE A CA  
4878  C C   . PHE A 297 ? 0.0966 0.1558 0.1190 0.0041  -0.0160 0.0429  520 PHE A C   
4879  O O   . PHE A 297 ? 0.1049 0.1886 0.1850 0.0081  0.0084  0.0700  520 PHE A O   
4880  C CB  . PHE A 297 ? 0.1298 0.1095 0.1117 -0.0063 0.0047  -0.0077 520 PHE A CB  
4881  C CG  . PHE A 297 ? 0.1470 0.1341 0.1333 0.0023  0.0182  0.0051  520 PHE A CG  
4882  C CD1 . PHE A 297 ? 0.1230 0.1566 0.1262 -0.0224 -0.0055 0.0160  520 PHE A CD1 
4883  C CD2 . PHE A 297 ? 0.1919 0.1606 0.1560 0.0378  0.0605  0.0342  520 PHE A CD2 
4884  C CE1 . PHE A 297 ? 0.1393 0.1514 0.1190 -0.0301 0.0021  0.0279  520 PHE A CE1 
4885  C CE2 . PHE A 297 ? 0.2077 0.1730 0.1535 0.0432  0.0690  0.0382  520 PHE A CE2 
4886  C CZ  . PHE A 297 ? 0.1850 0.1616 0.1230 0.0102  0.0247  0.0114  520 PHE A CZ  
4896  N N   . ASP A 298 ? 0.0758 0.1612 0.1334 -0.0315 -0.0091 0.0322  521 ASP A N   
4897  C CA  A ASP A 298 ? 0.0904 0.1688 0.1549 -0.0323 -0.0078 0.0241  521 ASP A CA  
4898  C CA  B ASP A 298 ? 0.0868 0.1626 0.1581 -0.0296 -0.0042 0.0276  521 ASP A CA  
4899  C C   . ASP A 298 ? 0.0815 0.1653 0.1569 -0.0287 -0.0044 0.0194  521 ASP A C   
4900  O O   . ASP A 298 ? 0.0874 0.1962 0.1716 0.0031  0.0011  0.0301  521 ASP A O   
4901  C CB  A ASP A 298 ? 0.1262 0.1833 0.1737 -0.0564 -0.0032 0.0226  521 ASP A CB  
4902  C CB  B ASP A 298 ? 0.1098 0.1636 0.1834 -0.0368 0.0045  0.0350  521 ASP A CB  
4903  C CG  A ASP A 298 ? 0.1536 0.1976 0.1924 -0.0662 -0.0096 0.0288  521 ASP A CG  
4904  C CG  B ASP A 298 ? 0.1171 0.1603 0.2004 -0.0304 0.0038  0.0506  521 ASP A CG  
4905  O OD1 A ASP A 298 ? 0.1612 0.2217 0.2176 -0.0837 -0.0256 0.0301  521 ASP A OD1 
4906  O OD1 B ASP A 298 ? 0.1359 0.1707 0.2137 -0.0298 -0.0122 0.0445  521 ASP A OD1 
4907  O OD2 A ASP A 298 ? 0.1608 0.1822 0.1863 -0.0728 -0.0148 0.0324  521 ASP A OD2 
4908  O OD2 B ASP A 298 ? 0.1118 0.1541 0.2080 -0.0050 0.0191  0.0574  521 ASP A OD2 
4917  N N   . SER A 299 ? 0.0749 0.1556 0.1461 -0.0249 -0.0085 0.0193  522 SER A N   
4918  C CA  . SER A 299 ? 0.0920 0.1517 0.1439 -0.0236 0.0003  0.0126  522 SER A CA  
4919  C C   . SER A 299 ? 0.0946 0.1371 0.1282 -0.0121 0.0086  0.0123  522 SER A C   
4920  O O   . SER A 299 ? 0.0906 0.1363 0.1368 -0.0132 -0.0058 -0.0156 522 SER A O   
4921  C CB  . SER A 299 ? 0.1360 0.1707 0.1597 -0.0386 -0.0097 0.0124  522 SER A CB  
4922  O OG  . SER A 299 ? 0.1739 0.1690 0.1818 -0.0388 0.0141  0.0252  522 SER A OG  
4928  N N   . TRP A 300 ? 0.1064 0.1477 0.1337 0.0002  0.0069  0.0188  523 TRP A N   
4929  C CA  . TRP A 300 ? 0.1106 0.1485 0.1255 -0.0135 0.0056  0.0336  523 TRP A CA  
4930  C C   . TRP A 300 ? 0.1163 0.1424 0.1457 -0.0236 0.0168  0.0364  523 TRP A C   
4931  O O   . TRP A 300 ? 0.1227 0.1643 0.1783 -0.0096 0.0345  0.0374  523 TRP A O   
4932  C CB  . TRP A 300 ? 0.1193 0.1476 0.1185 -0.0133 -0.0003 0.0159  523 TRP A CB  
4933  C CG  . TRP A 300 ? 0.1281 0.1457 0.0989 -0.0021 0.0034  0.0194  523 TRP A CG  
4934  C CD1 . TRP A 300 ? 0.1551 0.1553 0.1083 0.0048  0.0128  0.0103  523 TRP A CD1 
4935  C CD2 . TRP A 300 ? 0.1427 0.1316 0.0936 -0.0032 0.0013  0.0163  523 TRP A CD2 
4936  N NE1 . TRP A 300 ? 0.1662 0.1498 0.1110 0.0208  0.0106  0.0067  523 TRP A NE1 
4937  C CE2 . TRP A 300 ? 0.1581 0.1362 0.1203 0.0043  0.0052  0.0093  523 TRP A CE2 
4938  C CE3 . TRP A 300 ? 0.1548 0.1261 0.0826 -0.0087 0.0049  0.0064  523 TRP A CE3 
4939  C CZ2 . TRP A 300 ? 0.1860 0.1306 0.1312 -0.0151 0.0310  0.0107  523 TRP A CZ2 
4940  C CZ3 . TRP A 300 ? 0.1674 0.1284 0.1112 -0.0155 0.0295  0.0068  523 TRP A CZ3 
4941  C CH2 . TRP A 300 ? 0.1691 0.1222 0.1256 -0.0103 0.0211  0.0079  523 TRP A CH2 
4952  N N   . VAL A 301 ? 0.1189 0.1174 0.1569 -0.0266 0.0207  0.0240  524 VAL A N   
4953  C CA  . VAL A 301 ? 0.1276 0.1210 0.1513 -0.0323 0.0036  0.0167  524 VAL A CA  
4954  C C   . VAL A 301 ? 0.1483 0.1193 0.1216 -0.0274 -0.0006 0.0184  524 VAL A C   
4955  O O   . VAL A 301 ? 0.1617 0.1229 0.1123 -0.0150 -0.0011 0.0181  524 VAL A O   
4956  C CB  . VAL A 301 ? 0.1245 0.1355 0.1453 -0.0331 -0.0132 0.0150  524 VAL A CB  
4957  C CG1 . VAL A 301 ? 0.1359 0.1567 0.1650 -0.0514 0.0047  0.0172  524 VAL A CG1 
4958  C CG2 . VAL A 301 ? 0.1297 0.1358 0.1222 -0.0195 -0.0171 0.0174  524 VAL A CG2 
4968  N N   . ASN A 302 ? 0.1717 0.1141 0.1259 -0.0329 -0.0215 0.0103  525 ASN A N   
4969  C CA  . ASN A 302 ? 0.1618 0.1205 0.1198 -0.0334 -0.0085 0.0114  525 ASN A CA  
4970  C C   . ASN A 302 ? 0.1789 0.1042 0.1113 -0.0235 -0.0146 0.0082  525 ASN A C   
4971  O O   . ASN A 302 ? 0.2065 0.0980 0.1058 -0.0252 -0.0244 0.0119  525 ASN A O   
4972  C CB  . ASN A 302 ? 0.1778 0.1425 0.1353 -0.0539 0.0087  0.0166  525 ASN A CB  
4973  C CG  . ASN A 302 ? 0.2414 0.1583 0.1652 -0.0642 0.0300  0.0143  525 ASN A CG  
4974  O OD1 . ASN A 302 ? 0.2508 0.1423 0.1492 -0.0477 -0.0031 0.0160  525 ASN A OD1 
4975  N ND2 . ASN A 302 ? 0.2817 0.1970 0.2290 -0.0800 0.0785  0.0034  525 ASN A ND2 
4982  N N   . GLN A 303 ? 0.1795 0.1179 0.1087 -0.0197 -0.0082 0.0156  526 GLN A N   
4983  C CA  . GLN A 303 ? 0.1995 0.1165 0.1298 -0.0105 -0.0179 0.0041  526 GLN A CA  
4984  C C   . GLN A 303 ? 0.2219 0.1175 0.1382 -0.0072 -0.0124 -0.0060 526 GLN A C   
4985  O O   . GLN A 303 ? 0.2456 0.1191 0.1646 0.0105  0.0029  -0.0057 526 GLN A O   
4986  C CB  . GLN A 303 ? 0.1990 0.1298 0.1247 0.0087  -0.0259 -0.0098 526 GLN A CB  
4987  C CG  . GLN A 303 ? 0.2032 0.1496 0.1319 0.0294  -0.0147 -0.0116 526 GLN A CG  
4988  C CD  . GLN A 303 ? 0.2165 0.1854 0.1496 0.0303  -0.0139 -0.0100 526 GLN A CD  
4989  O OE1 . GLN A 303 ? 0.2289 0.1994 0.1795 0.0596  -0.0175 -0.0025 526 GLN A OE1 
4990  N NE2 . GLN A 303 ? 0.2218 0.1911 0.1276 0.0173  -0.0183 -0.0051 526 GLN A NE2 
4999  N N   . PHE A 304 ? 0.2322 0.1283 0.1221 -0.0211 -0.0387 0.0034  527 PHE A N   
5000  C CA  . PHE A 304 ? 0.2629 0.1293 0.1286 -0.0268 -0.0202 0.0181  527 PHE A CA  
5001  C C   . PHE A 304 ? 0.2521 0.1293 0.1437 -0.0258 -0.0102 0.0027  527 PHE A C   
5002  O O   . PHE A 304 ? 0.2652 0.1367 0.1573 -0.0319 -0.0215 0.0002  527 PHE A O   
5003  C CB  . PHE A 304 ? 0.3003 0.1478 0.1334 -0.0198 -0.0292 0.0326  527 PHE A CB  
5004  C CG  . PHE A 304 ? 0.3261 0.1547 0.1444 -0.0108 -0.0220 0.0457  527 PHE A CG  
5005  C CD1 . PHE A 304 ? 0.3374 0.1687 0.1603 -0.0009 -0.0297 0.0474  527 PHE A CD1 
5006  C CD2 . PHE A 304 ? 0.3433 0.1735 0.1633 -0.0112 0.0037  0.0493  527 PHE A CD2 
5007  C CE1 . PHE A 304 ? 0.3404 0.1773 0.1692 0.0047  -0.0375 0.0507  527 PHE A CE1 
5008  C CE2 . PHE A 304 ? 0.3470 0.1723 0.1673 -0.0064 0.0057  0.0550  527 PHE A CE2 
5009  C CZ  . PHE A 304 ? 0.3501 0.1865 0.1683 -0.0020 -0.0176 0.0502  527 PHE A CZ  
5019  N N   . TYR A 305 ? 0.2142 0.1288 0.1339 -0.0274 -0.0251 0.0044  528 TYR A N   
5020  C CA  . TYR A 305 ? 0.1994 0.1223 0.1465 -0.0429 -0.0089 -0.0053 528 TYR A CA  
5021  C C   . TYR A 305 ? 0.1949 0.1144 0.1286 -0.0344 -0.0235 0.0111  528 TYR A C   
5022  O O   . TYR A 305 ? 0.2016 0.1149 0.1459 -0.0168 -0.0254 0.0010  528 TYR A O   
5023  C CB  . TYR A 305 ? 0.1778 0.1345 0.1624 -0.0421 -0.0115 -0.0128 528 TYR A CB  
5024  C CG  . TYR A 305 ? 0.1700 0.1561 0.1819 -0.0348 -0.0252 -0.0180 528 TYR A CG  
5025  C CD1 . TYR A 305 ? 0.1771 0.1843 0.1995 -0.0227 -0.0263 -0.0382 528 TYR A CD1 
5026  C CD2 . TYR A 305 ? 0.1664 0.1489 0.1793 -0.0356 -0.0407 -0.0064 528 TYR A CD2 
5027  C CE1 . TYR A 305 ? 0.1824 0.1941 0.2149 -0.0261 -0.0352 -0.0348 528 TYR A CE1 
5028  C CE2 . TYR A 305 ? 0.1793 0.1597 0.1914 -0.0322 -0.0429 -0.0032 528 TYR A CE2 
5029  C CZ  . TYR A 305 ? 0.1852 0.1927 0.2120 -0.0224 -0.0624 -0.0058 528 TYR A CZ  
5030  O OH  . TYR A 305 ? 0.1881 0.2200 0.2599 -0.0254 -0.0808 -0.0147 528 TYR A OH  
5040  N N   . SER A 306 ? 0.1993 0.1069 0.1313 -0.0452 -0.0158 0.0031  529 SER A N   
5041  C CA  A SER A 306 ? 0.1924 0.1133 0.1338 -0.0463 -0.0109 0.0064  529 SER A CA  
5042  C CA  B SER A 306 ? 0.1940 0.1094 0.1301 -0.0439 -0.0056 0.0053  529 SER A CA  
5043  C C   . SER A 306 ? 0.1672 0.1097 0.1329 -0.0463 -0.0078 0.0026  529 SER A C   
5044  O O   . SER A 306 ? 0.1756 0.1318 0.1322 -0.0422 -0.0065 0.0226  529 SER A O   
5045  C CB  A SER A 306 ? 0.2162 0.1251 0.1468 -0.0549 -0.0008 0.0110  529 SER A CB  
5046  C CB  B SER A 306 ? 0.2206 0.1143 0.1345 -0.0475 0.0129  0.0070  529 SER A CB  
5047  O OG  A SER A 306 ? 0.2382 0.1353 0.1706 -0.0640 0.0030  0.0129  529 SER A OG  
5048  O OG  B SER A 306 ? 0.2462 0.1181 0.1504 -0.0508 0.0230  0.0063  529 SER A OG  
5059  N N   . LEU A 307 ? 0.1424 0.1084 0.1364 -0.0391 -0.0071 0.0119  530 LEU A N   
5060  C CA  . LEU A 307 ? 0.1364 0.1019 0.1462 -0.0428 -0.0121 0.0007  530 LEU A CA  
5061  C C   . LEU A 307 ? 0.1402 0.1033 0.1584 -0.0373 -0.0002 0.0116  530 LEU A C   
5062  O O   . LEU A 307 ? 0.1611 0.0881 0.1670 -0.0205 -0.0036 0.0120  530 LEU A O   
5063  C CB  . LEU A 307 ? 0.1472 0.0864 0.1543 -0.0295 -0.0045 0.0045  530 LEU A CB  
5064  C CG  . LEU A 307 ? 0.1359 0.0721 0.1347 -0.0212 -0.0103 -0.0078 530 LEU A CG  
5065  C CD1 . LEU A 307 ? 0.1119 0.0797 0.1414 -0.0245 -0.0072 -0.0004 530 LEU A CD1 
5066  C CD2 . LEU A 307 ? 0.1545 0.0719 0.1648 -0.0088 -0.0028 -0.0048 530 LEU A CD2 
5078  N N   . ALA A 308 ? 0.1352 0.1041 0.1485 -0.0416 -0.0080 0.0203  531 ALA A N   
5079  C CA  . ALA A 308 ? 0.1396 0.1112 0.1500 -0.0532 -0.0209 0.0259  531 ALA A CA  
5080  C C   . ALA A 308 ? 0.1459 0.1016 0.1534 -0.0467 -0.0284 0.0317  531 ALA A C   
5081  O O   . ALA A 308 ? 0.1271 0.1012 0.1313 -0.0489 -0.0405 0.0339  531 ALA A O   
5082  C CB  . ALA A 308 ? 0.1588 0.1275 0.1605 -0.0510 0.0001  0.0157  531 ALA A CB  
5088  N N   . PRO A 309 ? 0.1873 0.0980 0.2033 -0.0389 0.0147  0.0058  532 PRO A N   
5089  C CA  A PRO A 309 ? 0.1880 0.1116 0.1925 -0.0360 0.0173  0.0060  532 PRO A CA  
5090  C CA  B PRO A 309 ? 0.1925 0.1099 0.1952 -0.0298 0.0141  0.0099  532 PRO A CA  
5091  C C   . PRO A 309 ? 0.1600 0.1274 0.1517 -0.0518 0.0040  -0.0008 532 PRO A C   
5092  O O   . PRO A 309 ? 0.1865 0.1763 0.1433 -0.0553 -0.0129 -0.0098 532 PRO A O   
5093  C CB  A PRO A 309 ? 0.2105 0.1184 0.2233 -0.0295 0.0333  0.0054  532 PRO A CB  
5094  C CB  B PRO A 309 ? 0.2199 0.1226 0.2327 -0.0225 0.0244  0.0074  532 PRO A CB  
5095  C CG  A PRO A 309 ? 0.2334 0.1275 0.2473 -0.0354 0.0458  -0.0001 532 PRO A CG  
5096  C CG  B PRO A 309 ? 0.2485 0.1397 0.2591 -0.0367 0.0311  -0.0048 532 PRO A CG  
5097  C CD  A PRO A 309 ? 0.2180 0.1075 0.2347 -0.0387 0.0394  0.0027  532 PRO A CD  
5098  C CD  B PRO A 309 ? 0.2154 0.1102 0.2225 -0.0444 0.0039  -0.0033 532 PRO A CD  
5185  N N   . THR B 5   ? 0.1231 0.1192 0.1741 0.0240  0.0042  -0.0018 228 THR B N   
5186  C CA  . THR B 5   ? 0.1069 0.1281 0.1499 0.0074  -0.0006 -0.0087 228 THR B CA  
5187  C C   . THR B 5   ? 0.0996 0.1141 0.1261 0.0279  -0.0051 0.0074  228 THR B C   
5188  O O   . THR B 5   ? 0.0916 0.1059 0.1433 0.0143  -0.0092 0.0021  228 THR B O   
5189  C CB  . THR B 5   ? 0.1144 0.1443 0.1459 -0.0047 0.0212  0.0048  228 THR B CB  
5190  O OG1 . THR B 5   ? 0.1086 0.1205 0.1553 0.0300  0.0123  0.0358  228 THR B OG1 
5191  C CG2 . THR B 5   ? 0.1357 0.1639 0.1598 -0.0079 0.0576  0.0018  228 THR B CG2 
5199  N N   . ILE B 6   ? 0.0861 0.1128 0.1004 0.0122  -0.0197 0.0025  229 ILE B N   
5200  C CA  . ILE B 6   ? 0.0753 0.1054 0.1144 0.0175  -0.0139 0.0128  229 ILE B CA  
5201  C C   . ILE B 6   ? 0.0773 0.0945 0.1087 -0.0053 -0.0048 0.0079  229 ILE B C   
5202  O O   . ILE B 6   ? 0.0957 0.0844 0.1120 0.0114  0.0123  0.0136  229 ILE B O   
5203  C CB  . ILE B 6   ? 0.1015 0.1054 0.1473 0.0227  -0.0051 0.0271  229 ILE B CB  
5204  C CG1 . ILE B 6   ? 0.1085 0.1182 0.1773 0.0290  -0.0064 0.0214  229 ILE B CG1 
5205  C CG2 . ILE B 6   ? 0.1215 0.0899 0.1529 0.0206  0.0143  0.0221  229 ILE B CG2 
5206  C CD1 . ILE B 6   ? 0.1325 0.1309 0.1727 0.0198  0.0100  -0.0058 229 ILE B CD1 
5218  N N   . PRO B 7   ? 0.0735 0.0948 0.0890 -0.0037 -0.0081 0.0079  230 PRO B N   
5219  C CA  . PRO B 7   ? 0.0773 0.0845 0.0810 0.0031  -0.0128 0.0056  230 PRO B CA  
5220  C C   . PRO B 7   ? 0.0789 0.0778 0.0833 0.0044  -0.0185 -0.0021 230 PRO B C   
5221  O O   . PRO B 7   ? 0.0983 0.0785 0.0999 -0.0031 -0.0097 0.0001  230 PRO B O   
5222  C CB  . PRO B 7   ? 0.0905 0.0918 0.0975 0.0054  -0.0071 0.0077  230 PRO B CB  
5223  C CG  . PRO B 7   ? 0.0948 0.0964 0.0851 0.0136  -0.0185 -0.0041 230 PRO B CG  
5224  C CD  . PRO B 7   ? 0.0954 0.1005 0.0863 0.0108  -0.0239 0.0039  230 PRO B CD  
5232  N N   . ILE B 8   ? 0.0838 0.0810 0.0801 0.0034  -0.0111 0.0030  231 ILE B N   
5233  C CA  . ILE B 8   ? 0.1028 0.0831 0.0847 0.0129  -0.0158 -0.0031 231 ILE B CA  
5234  C C   . ILE B 8   ? 0.1158 0.1001 0.1030 0.0072  -0.0278 -0.0058 231 ILE B C   
5235  O O   . ILE B 8   ? 0.1256 0.1299 0.1072 0.0059  -0.0307 -0.0307 231 ILE B O   
5236  C CB  . ILE B 8   ? 0.1183 0.0913 0.0980 0.0082  -0.0009 0.0104  231 ILE B CB  
5237  C CG1 . ILE B 8   ? 0.1686 0.1044 0.0978 0.0081  0.0023  0.0128  231 ILE B CG1 
5238  C CG2 . ILE B 8   ? 0.1116 0.1064 0.1223 0.0093  0.0010  -0.0013 231 ILE B CG2 
5239  C CD1 . ILE B 8   ? 0.2059 0.0985 0.1107 0.0149  0.0072  0.0197  231 ILE B CD1 
5251  N N   . LEU B 9   ? 0.0891 0.0955 0.0939 0.0160  -0.0236 -0.0108 232 LEU B N   
5252  C CA  . LEU B 9   ? 0.0898 0.0837 0.0928 0.0284  -0.0067 -0.0004 232 LEU B CA  
5253  C C   . LEU B 9   ? 0.0864 0.0846 0.0858 0.0233  -0.0147 -0.0120 232 LEU B C   
5254  O O   . LEU B 9   ? 0.0863 0.0992 0.0935 0.0160  -0.0257 -0.0003 232 LEU B O   
5255  C CB  . LEU B 9   ? 0.0968 0.0865 0.0964 0.0113  -0.0081 0.0027  232 LEU B CB  
5256  C CG  . LEU B 9   ? 0.1218 0.0847 0.1167 0.0101  -0.0005 0.0086  232 LEU B CG  
5257  C CD1 . LEU B 9   ? 0.1655 0.0930 0.1181 0.0014  0.0220  -0.0077 232 LEU B CD1 
5258  C CD2 . LEU B 9   ? 0.1413 0.0918 0.1335 0.0029  -0.0056 0.0169  232 LEU B CD2 
5270  N N   . THR B 10  ? 0.1029 0.0962 0.0955 0.0212  -0.0332 -0.0058 233 THR B N   
5271  C CA  . THR B 10  ? 0.1128 0.1114 0.1191 0.0057  -0.0441 -0.0153 233 THR B CA  
5272  C C   . THR B 10  ? 0.1119 0.1122 0.1421 0.0103  -0.0364 -0.0069 233 THR B C   
5273  O O   . THR B 10  ? 0.1004 0.1087 0.1165 0.0111  -0.0247 0.0038  233 THR B O   
5274  C CB  . THR B 10  ? 0.1298 0.1217 0.1302 0.0035  -0.0408 -0.0340 233 THR B CB  
5275  O OG1 . THR B 10  ? 0.1210 0.1470 0.1625 0.0291  -0.0612 -0.0443 233 THR B OG1 
5276  C CG2 . THR B 10  ? 0.1598 0.1375 0.1222 -0.0105 -0.0375 -0.0264 233 THR B CG2 
5284  N N   . ILE B 11  ? 0.1220 0.1335 0.1576 -0.0054 -0.0056 -0.0198 234 ILE B N   
5285  C CA  . ILE B 11  ? 0.1631 0.1748 0.2126 -0.0308 0.0260  -0.0192 234 ILE B CA  
5286  C C   . ILE B 11  ? 0.1378 0.1769 0.2114 -0.0632 0.0144  -0.0700 234 ILE B C   
5287  O O   . ILE B 11  ? 0.1345 0.2020 0.2092 -0.0743 0.0318  -0.0575 234 ILE B O   
5288  C CB  . ILE B 11  ? 0.2488 0.2309 0.2618 -0.0261 0.0733  -0.0086 234 ILE B CB  
5289  C CG1 . ILE B 11  ? 0.3112 0.2686 0.2716 -0.0224 0.0713  0.0093  234 ILE B CG1 
5290  C CG2 . ILE B 11  ? 0.2837 0.2494 0.2760 -0.0422 0.0796  -0.0226 234 ILE B CG2 
5291  C CD1 . ILE B 11  ? 0.3348 0.2811 0.2684 -0.0310 0.0804  -0.0163 234 ILE B CD1 
5303  N N   . GLY B 12  ? 0.1271 0.2057 0.2272 -0.0325 -0.0174 -0.0849 235 GLY B N   
5304  C CA  . GLY B 12  ? 0.1165 0.2331 0.2313 0.0147  -0.0251 -0.0746 235 GLY B CA  
5305  C C   . GLY B 12  ? 0.1187 0.2344 0.1988 0.0668  -0.0336 -0.0463 235 GLY B C   
5306  O O   . GLY B 12  ? 0.1494 0.2945 0.2286 0.0597  -0.0607 -0.0634 235 GLY B O   
5310  N N   . GLU B 13  ? 0.1146 0.1939 0.1227 0.0551  -0.0436 -0.0172 236 GLU B N   
5311  C CA  . GLU B 13  ? 0.1114 0.1583 0.0875 0.0497  -0.0302 -0.0075 236 GLU B CA  
5312  C C   . GLU B 13  ? 0.0953 0.1293 0.0904 0.0263  -0.0282 0.0017  236 GLU B C   
5313  O O   . GLU B 13  ? 0.1403 0.1059 0.1106 0.0282  -0.0315 0.0037  236 GLU B O   
5314  C CB  . GLU B 13  ? 0.1241 0.1445 0.0830 0.0506  -0.0290 -0.0013 236 GLU B CB  
5315  C CG  . GLU B 13  ? 0.1352 0.1466 0.0888 0.0514  -0.0337 0.0234  236 GLU B CG  
5316  C CD  . GLU B 13  ? 0.1505 0.1446 0.0980 0.0473  -0.0270 0.0153  236 GLU B CD  
5317  O OE1 . GLU B 13  ? 0.1409 0.1503 0.0987 0.0418  -0.0187 0.0180  236 GLU B OE1 
5318  O OE2 . GLU B 13  ? 0.1654 0.1787 0.1033 0.0318  -0.0344 0.0086  236 GLU B OE2 
5325  N N   . MET B 14  ? 0.0681 0.1256 0.0900 0.0078  -0.0184 0.0050  237 MET B N   
5326  C CA  . MET B 14  ? 0.0410 0.1158 0.0930 0.0088  -0.0174 -0.0076 237 MET B CA  
5327  C C   . MET B 14  ? 0.0536 0.1067 0.1092 0.0085  -0.0035 -0.0041 237 MET B C   
5328  O O   . MET B 14  ? 0.0640 0.1338 0.1200 -0.0134 0.0139  -0.0082 237 MET B O   
5329  C CB  . MET B 14  ? 0.0608 0.1036 0.0941 0.0091  -0.0146 -0.0098 237 MET B CB  
5330  C CG  . MET B 14  ? 0.0607 0.1068 0.0944 0.0198  -0.0172 -0.0100 237 MET B CG  
5331  S SD  . MET B 14  ? 0.0711 0.1186 0.0885 0.0256  -0.0074 0.0072  237 MET B SD  
5332  C CE  . MET B 14  ? 0.0800 0.1134 0.1036 0.0337  0.0144  -0.0057 237 MET B CE  
5342  N N   . THR B 15  ? 0.0661 0.1063 0.0997 0.0082  -0.0061 0.0059  238 THR B N   
5343  C CA  A THR B 15  ? 0.0631 0.0993 0.0916 0.0111  -0.0184 0.0065  238 THR B CA  
5344  C CA  B THR B 15  ? 0.0612 0.0981 0.1060 0.0066  -0.0027 0.0079  238 THR B CA  
5345  C C   . THR B 15  ? 0.0536 0.0903 0.0920 0.0041  -0.0047 -0.0007 238 THR B C   
5346  O O   . THR B 15  ? 0.0554 0.0926 0.1018 0.0047  -0.0017 0.0070  238 THR B O   
5347  C CB  A THR B 15  ? 0.0826 0.1072 0.1067 0.0096  -0.0070 0.0170  238 THR B CB  
5348  C CB  B THR B 15  ? 0.0820 0.1047 0.1461 0.0001  0.0318  0.0217  238 THR B CB  
5349  O OG1 A THR B 15  ? 0.0674 0.1007 0.1065 0.0105  0.0127  0.0167  238 THR B OG1 
5350  O OG1 B THR B 15  ? 0.0843 0.1165 0.1600 0.0178  0.0458  0.0434  238 THR B OG1 
5351  C CG2 A THR B 15  ? 0.0927 0.1174 0.1109 0.0072  -0.0122 0.0193  238 THR B CG2 
5352  C CG2 B THR B 15  ? 0.0792 0.1039 0.1599 -0.0163 0.0393  0.0057  238 THR B CG2 
5367  N N   . ASN B 16  ? 0.0495 0.0817 0.0740 0.0023  0.0019  0.0018  239 ASN B N   
5368  C CA  . ASN B 16  ? 0.0434 0.0727 0.0913 0.0022  -0.0055 0.0030  239 ASN B CA  
5369  C C   . ASN B 16  ? 0.0400 0.0798 0.0903 0.0034  -0.0127 -0.0075 239 ASN B C   
5370  O O   . ASN B 16  ? 0.0740 0.0903 0.1103 0.0123  -0.0180 -0.0152 239 ASN B O   
5371  C CB  . ASN B 16  ? 0.0453 0.0694 0.0896 0.0081  0.0065  -0.0045 239 ASN B CB  
5372  C CG  . ASN B 16  ? 0.0478 0.0670 0.0734 0.0179  -0.0117 -0.0136 239 ASN B CG  
5373  O OD1 . ASN B 16  ? 0.0610 0.0813 0.0778 0.0054  -0.0160 -0.0107 239 ASN B OD1 
5374  N ND2 . ASN B 16  ? 0.0692 0.0654 0.0812 0.0060  -0.0034 -0.0006 239 ASN B ND2 
5381  N N   . SER B 17  ? 0.0427 0.0676 0.0788 0.0068  -0.0026 -0.0071 240 SER B N   
5382  C CA  . SER B 17  ? 0.0484 0.0591 0.0821 0.0017  -0.0132 0.0058  240 SER B CA  
5383  C C   . SER B 17  ? 0.0391 0.0594 0.0800 0.0066  -0.0259 -0.0024 240 SER B C   
5384  O O   . SER B 17  ? 0.0693 0.0717 0.0698 -0.0099 -0.0186 -0.0054 240 SER B O   
5385  C CB  . SER B 17  ? 0.0554 0.0703 0.0788 0.0019  -0.0061 -0.0015 240 SER B CB  
5386  O OG  . SER B 17  ? 0.0480 0.0737 0.0943 0.0059  -0.0044 -0.0051 240 SER B OG  
5392  N N   . ARG B 18  ? 0.0481 0.0661 0.0756 0.0016  -0.0245 -0.0032 241 ARG B N   
5393  C CA  . ARG B 18  ? 0.0569 0.0644 0.0546 0.0079  -0.0070 0.0040  241 ARG B CA  
5394  C C   . ARG B 18  ? 0.0657 0.0747 0.0687 0.0061  -0.0134 -0.0061 241 ARG B C   
5395  O O   . ARG B 18  ? 0.0544 0.0766 0.0890 0.0125  -0.0073 0.0118  241 ARG B O   
5396  C CB  . ARG B 18  ? 0.0537 0.0627 0.0680 0.0060  -0.0137 0.0117  241 ARG B CB  
5397  C CG  . ARG B 18  ? 0.0456 0.0549 0.0830 0.0006  -0.0046 0.0045  241 ARG B CG  
5398  C CD  . ARG B 18  ? 0.0495 0.0637 0.0809 0.0022  -0.0065 0.0067  241 ARG B CD  
5399  N NE  . ARG B 18  ? 0.0838 0.0602 0.0713 0.0063  -0.0009 0.0061  241 ARG B NE  
5400  C CZ  . ARG B 18  ? 0.0621 0.0577 0.0870 0.0047  -0.0060 0.0096  241 ARG B CZ  
5401  N NH1 . ARG B 18  ? 0.0808 0.0590 0.0919 -0.0060 -0.0016 -0.0001 241 ARG B NH1 
5402  N NH2 . ARG B 18  ? 0.0755 0.0719 0.0781 -0.0078 0.0051  0.0026  241 ARG B NH2 
5416  N N   . PHE B 19  ? 0.0616 0.0813 0.0630 0.0096  -0.0092 -0.0158 242 PHE B N   
5417  C CA  . PHE B 19  ? 0.0600 0.0779 0.0861 0.0194  -0.0155 -0.0130 242 PHE B CA  
5418  C C   . PHE B 19  ? 0.0492 0.0861 0.0746 0.0073  -0.0061 -0.0172 242 PHE B C   
5419  O O   . PHE B 19  ? 0.0665 0.0823 0.0972 0.0241  -0.0074 -0.0070 242 PHE B O   
5420  C CB  . PHE B 19  ? 0.0599 0.0727 0.1011 0.0100  -0.0095 -0.0153 242 PHE B CB  
5421  C CG  . PHE B 19  ? 0.0636 0.0762 0.1117 0.0049  -0.0238 -0.0186 242 PHE B CG  
5422  C CD1 . PHE B 19  ? 0.0785 0.1092 0.1222 0.0004  -0.0138 -0.0336 242 PHE B CD1 
5423  C CD2 . PHE B 19  ? 0.0797 0.1001 0.1462 0.0152  -0.0148 -0.0053 242 PHE B CD2 
5424  C CE1 . PHE B 19  ? 0.0868 0.1169 0.1498 -0.0024 0.0273  -0.0470 242 PHE B CE1 
5425  C CE2 . PHE B 19  ? 0.0816 0.1025 0.1637 0.0014  0.0006  -0.0178 242 PHE B CE2 
5426  C CZ  . PHE B 19  ? 0.0917 0.1116 0.1762 -0.0050 0.0261  -0.0454 242 PHE B CZ  
5436  N N   . PRO B 20  ? 0.0622 0.0912 0.0673 0.0118  -0.0101 -0.0002 243 PRO B N   
5437  C CA  . PRO B 20  ? 0.0981 0.0914 0.0851 0.0070  -0.0175 -0.0047 243 PRO B CA  
5438  C C   . PRO B 20  ? 0.0943 0.0875 0.0859 0.0327  -0.0235 -0.0055 243 PRO B C   
5439  O O   . PRO B 20  ? 0.1097 0.1070 0.1063 0.0585  -0.0285 -0.0039 243 PRO B O   
5440  C CB  . PRO B 20  ? 0.1198 0.0886 0.0919 0.0158  -0.0102 -0.0067 243 PRO B CB  
5441  C CG  . PRO B 20  ? 0.1188 0.0887 0.0953 0.0242  0.0000  0.0030  243 PRO B CG  
5442  C CD  . PRO B 20  ? 0.0788 0.0828 0.0926 0.0198  -0.0081 0.0022  243 PRO B CD  
5450  N N   . VAL B 21  ? 0.0811 0.0814 0.0962 0.0194  -0.0088 -0.0048 244 VAL B N   
5451  C CA  . VAL B 21  ? 0.0733 0.0800 0.1016 0.0145  -0.0142 0.0036  244 VAL B CA  
5452  C C   . VAL B 21  ? 0.0675 0.0802 0.0968 0.0061  -0.0237 0.0025  244 VAL B C   
5453  O O   . VAL B 21  ? 0.0461 0.0981 0.0918 0.0108  -0.0182 -0.0029 244 VAL B O   
5454  C CB  . VAL B 21  ? 0.0824 0.0988 0.1016 0.0274  0.0152  0.0169  244 VAL B CB  
5455  C CG1 . VAL B 21  ? 0.0751 0.1259 0.1314 0.0143  -0.0017 0.0035  244 VAL B CG1 
5456  C CG2 . VAL B 21  ? 0.1145 0.0967 0.1069 0.0092  0.0179  -0.0031 244 VAL B CG2 
5466  N N   . PRO B 22  ? 0.0750 0.0744 0.1025 0.0177  -0.0135 0.0055  245 PRO B N   
5467  C CA  . PRO B 22  ? 0.0778 0.0836 0.0835 0.0136  -0.0274 -0.0012 245 PRO B CA  
5468  C C   . PRO B 22  ? 0.0765 0.0800 0.0886 0.0099  -0.0203 0.0108  245 PRO B C   
5469  O O   . PRO B 22  ? 0.0738 0.0761 0.1162 0.0066  -0.0044 0.0142  245 PRO B O   
5470  C CB  . PRO B 22  ? 0.1148 0.0970 0.1069 0.0145  -0.0297 0.0092  245 PRO B CB  
5471  C CG  . PRO B 22  ? 0.1215 0.1001 0.1274 0.0091  -0.0253 0.0035  245 PRO B CG  
5472  C CD  . PRO B 22  ? 0.0870 0.0976 0.1302 0.0405  -0.0176 0.0068  245 PRO B CD  
5480  N N   . ILE B 23  ? 0.0859 0.0797 0.1096 0.0156  -0.0086 0.0259  246 ILE B N   
5481  C CA  . ILE B 23  ? 0.0816 0.0755 0.1049 0.0119  -0.0014 0.0068  246 ILE B CA  
5482  C C   . ILE B 23  ? 0.0858 0.0874 0.1075 -0.0008 0.0025  0.0263  246 ILE B C   
5483  O O   . ILE B 23  ? 0.1167 0.1234 0.1062 -0.0170 -0.0186 0.0357  246 ILE B O   
5484  C CB  . ILE B 23  ? 0.0832 0.0801 0.1257 0.0006  -0.0141 -0.0016 246 ILE B CB  
5485  C CG1 . ILE B 23  ? 0.1116 0.0907 0.1690 -0.0029 -0.0072 -0.0121 246 ILE B CG1 
5486  C CG2 . ILE B 23  ? 0.0637 0.0929 0.1131 0.0035  -0.0039 -0.0046 246 ILE B CG2 
5487  C CD1 . ILE B 23  ? 0.1323 0.1068 0.1902 -0.0164 -0.0074 -0.0054 246 ILE B CD1 
5499  N N   . ASP B 24  ? 0.0706 0.0896 0.0987 0.0071  -0.0197 0.0116  247 ASP B N   
5500  C CA  . ASP B 24  ? 0.0724 0.1055 0.0958 0.0139  -0.0213 0.0092  247 ASP B CA  
5501  C C   . ASP B 24  ? 0.0707 0.1071 0.1088 0.0196  -0.0266 -0.0049 247 ASP B C   
5502  O O   . ASP B 24  ? 0.0989 0.1258 0.1096 0.0219  -0.0292 -0.0087 247 ASP B O   
5503  C CB  . ASP B 24  ? 0.0936 0.1381 0.1069 0.0254  -0.0275 0.0065  247 ASP B CB  
5504  C CG  . ASP B 24  ? 0.1106 0.1651 0.1129 0.0529  -0.0184 0.0239  247 ASP B CG  
5505  O OD1 . ASP B 24  ? 0.1752 0.2132 0.1613 0.0925  0.0199  0.0436  247 ASP B OD1 
5506  O OD2 . ASP B 24  ? 0.1225 0.1612 0.1105 0.0583  0.0055  0.0284  247 ASP B OD2 
5511  N N   . MET B 25  ? 0.0610 0.0906 0.0999 0.0263  -0.0142 -0.0050 248 MET B N   
5512  C CA  . MET B 25  ? 0.0627 0.0883 0.1125 0.0194  -0.0210 -0.0095 248 MET B CA  
5513  C C   . MET B 25  ? 0.0763 0.0792 0.1024 0.0112  -0.0245 -0.0180 248 MET B C   
5514  O O   . MET B 25  ? 0.0871 0.0870 0.1073 0.0216  -0.0304 -0.0310 248 MET B O   
5515  C CB  . MET B 25  ? 0.1057 0.1186 0.1414 -0.0176 -0.0241 -0.0084 248 MET B CB  
5516  C CG  . MET B 25  ? 0.1761 0.1461 0.1631 -0.0566 -0.0361 0.0040  248 MET B CG  
5517  S SD  . MET B 25  ? 0.2378 0.2035 0.2200 -0.0766 -0.0121 -0.0198 248 MET B SD  
5518  C CE  . MET B 25  ? 0.2656 0.2138 0.2506 -0.0427 0.0020  -0.0042 248 MET B CE  
5528  N N   . LEU B 26  ? 0.0864 0.0705 0.0963 0.0270  -0.0097 -0.0098 249 LEU B N   
5529  C CA  . LEU B 26  ? 0.0832 0.0704 0.1092 0.0079  -0.0210 -0.0155 249 LEU B CA  
5530  C C   . LEU B 26  ? 0.0767 0.0830 0.1333 -0.0008 -0.0313 -0.0086 249 LEU B C   
5531  O O   . LEU B 26  ? 0.1041 0.0929 0.1555 -0.0101 -0.0518 0.0021  249 LEU B O   
5532  C CB  . LEU B 26  ? 0.0945 0.0780 0.0964 0.0024  -0.0189 -0.0153 249 LEU B CB  
5533  C CG  . LEU B 26  ? 0.0930 0.1011 0.1120 -0.0057 -0.0036 -0.0157 249 LEU B CG  
5534  C CD1 . LEU B 26  ? 0.1052 0.1178 0.0985 0.0053  -0.0036 -0.0132 249 LEU B CD1 
5535  C CD2 . LEU B 26  ? 0.1349 0.1093 0.1146 -0.0401 0.0276  -0.0411 249 LEU B CD2 
5547  N N   . HIS B 27  ? 0.0677 0.0785 0.1281 0.0053  -0.0289 -0.0067 250 HIS B N   
5548  C CA  . HIS B 27  ? 0.0935 0.0799 0.1113 0.0128  -0.0081 0.0033  250 HIS B CA  
5549  C C   . HIS B 27  ? 0.0863 0.0789 0.0956 0.0011  -0.0135 -0.0088 250 HIS B C   
5550  O O   . HIS B 27  ? 0.0828 0.0857 0.1055 0.0020  -0.0171 -0.0083 250 HIS B O   
5551  C CB  . HIS B 27  ? 0.0955 0.1111 0.1427 0.0091  0.0011  0.0206  250 HIS B CB  
5552  C CG  . HIS B 27  ? 0.1188 0.1426 0.1292 -0.0038 -0.0022 -0.0013 250 HIS B CG  
5553  N ND1 . HIS B 27  ? 0.1274 0.1319 0.1272 -0.0226 0.0033  -0.0248 250 HIS B ND1 
5554  C CD2 . HIS B 27  ? 0.1207 0.1447 0.1315 -0.0260 -0.0025 -0.0133 250 HIS B CD2 
5555  C CE1 . HIS B 27  ? 0.1425 0.1345 0.1436 -0.0222 0.0009  -0.0037 250 HIS B CE1 
5556  N NE2 . HIS B 27  ? 0.1423 0.1460 0.1499 -0.0294 0.0130  -0.0186 250 HIS B NE2 
5564  N N   . THR B 28  ? 0.0658 0.0823 0.1073 -0.0113 -0.0349 -0.0051 251 THR B N   
5565  C CA  . THR B 28  ? 0.0811 0.0756 0.1095 -0.0080 -0.0349 -0.0044 251 THR B CA  
5566  C C   . THR B 28  ? 0.1024 0.0880 0.1240 -0.0114 -0.0193 0.0117  251 THR B C   
5567  O O   . THR B 28  ? 0.1110 0.1035 0.1263 -0.0272 -0.0259 -0.0001 251 THR B O   
5568  C CB  . THR B 28  ? 0.0737 0.0885 0.1240 0.0038  -0.0232 0.0046  251 THR B CB  
5569  O OG1 . THR B 28  ? 0.0888 0.0794 0.1234 0.0046  -0.0309 0.0044  251 THR B OG1 
5570  C CG2 . THR B 28  ? 0.0698 0.1065 0.1235 0.0187  -0.0073 -0.0012 251 THR B CG2 
5578  N N   . SER B 29  ? 0.1151 0.0943 0.1192 -0.0117 -0.0132 0.0127  252 SER B N   
5579  C CA  . SER B 29  ? 0.1156 0.1126 0.1248 -0.0173 -0.0033 0.0051  252 SER B CA  
5580  C C   . SER B 29  ? 0.1521 0.1363 0.1413 -0.0080 -0.0073 0.0178  252 SER B C   
5581  O O   . SER B 29  ? 0.1472 0.1439 0.1398 0.0014  -0.0119 0.0345  252 SER B O   
5582  C CB  . SER B 29  ? 0.1382 0.1157 0.1391 -0.0156 0.0079  -0.0025 252 SER B CB  
5583  O OG  . SER B 29  ? 0.1486 0.1479 0.1381 -0.0035 0.0137  -0.0111 252 SER B OG  
5589  N N   . PRO B 30  ? 0.1785 0.1323 0.1515 -0.0025 -0.0324 0.0295  253 PRO B N   
5590  C CA  . PRO B 30  ? 0.1843 0.1400 0.1349 0.0114  -0.0255 0.0245  253 PRO B CA  
5591  C C   . PRO B 30  ? 0.1607 0.1286 0.1364 0.0140  -0.0032 0.0281  253 PRO B C   
5592  O O   . PRO B 30  ? 0.1581 0.1611 0.1883 0.0057  -0.0055 0.0061  253 PRO B O   
5593  C CB  . PRO B 30  ? 0.2134 0.1436 0.1666 0.0155  -0.0176 0.0188  253 PRO B CB  
5594  C CG  . PRO B 30  ? 0.2132 0.1228 0.1872 0.0052  -0.0174 0.0343  253 PRO B CG  
5595  C CD  . PRO B 30  ? 0.2012 0.1225 0.1750 -0.0052 -0.0273 0.0276  253 PRO B CD  
5603  N N   . THR B 31  ? 0.1760 0.1254 0.1363 0.0192  0.0045  0.0233  254 THR B N   
5604  C CA  . THR B 31  ? 0.2077 0.1410 0.1405 0.0033  -0.0021 0.0151  254 THR B CA  
5605  C C   . THR B 31  ? 0.2538 0.1538 0.1615 0.0285  -0.0237 0.0213  254 THR B C   
5606  O O   . THR B 31  ? 0.2488 0.1609 0.1552 0.0268  -0.0103 0.0181  254 THR B O   
5607  C CB  . THR B 31  ? 0.2232 0.1514 0.1534 -0.0132 0.0038  0.0223  254 THR B CB  
5608  O OG1 . THR B 31  ? 0.2322 0.1796 0.1437 -0.0441 0.0019  0.0171  254 THR B OG1 
5609  C CG2 . THR B 31  ? 0.2458 0.1497 0.1726 -0.0117 0.0067  0.0257  254 THR B CG2 
5617  N N   . GLU B 32  ? 0.3194 0.1603 0.1821 0.0489  -0.0484 0.0348  255 GLU B N   
5618  C CA  . GLU B 32  ? 0.3909 0.1947 0.2325 0.0571  -0.0542 0.0360  255 GLU B CA  
5619  C C   . GLU B 32  ? 0.4182 0.1842 0.2259 0.0214  -0.0481 0.0435  255 GLU B C   
5620  O O   . GLU B 32  ? 0.4417 0.2058 0.2211 0.0247  -0.0643 0.0478  255 GLU B O   
5621  C CB  . GLU B 32  ? 0.4290 0.2441 0.2807 0.0941  -0.0583 0.0194  255 GLU B CB  
5622  C CG  . GLU B 32  ? 0.4691 0.2840 0.3284 0.1145  -0.0539 -0.0055 255 GLU B CG  
5623  C CD  . GLU B 32  ? 0.5075 0.3123 0.3655 0.1255  -0.0439 -0.0359 255 GLU B CD  
5624  O OE1 . GLU B 32  ? 0.5064 0.3136 0.3580 0.1372  -0.0766 -0.0391 255 GLU B OE1 
5625  O OE2 . GLU B 32  ? 0.5347 0.3276 0.3969 0.1236  -0.0178 -0.0472 255 GLU B OE2 
5632  N N   . ASN B 33  ? 0.4122 0.1583 0.2453 -0.0324 -0.0083 0.0374  256 ASN B N   
5633  C CA  . ASN B 33  ? 0.4205 0.1918 0.2973 -0.0658 0.0298  0.0307  256 ASN B CA  
5634  C C   . ASN B 33  ? 0.3836 0.2068 0.2657 -0.0934 0.0250  0.0241  256 ASN B C   
5635  O O   . ASN B 33  ? 0.4037 0.2377 0.2858 -0.0931 0.0505  0.0213  256 ASN B O   
5636  C CB  . ASN B 33  ? 0.4483 0.2276 0.3698 -0.0683 0.0475  0.0226  256 ASN B CB  
5637  C CG  . ASN B 33  ? 0.4689 0.2655 0.4372 -0.0511 0.0583  0.0171  256 ASN B CG  
5638  O OD1 . ASN B 33  ? 0.4876 0.2823 0.4557 -0.0440 0.0608  0.0244  256 ASN B OD1 
5639  N ND2 . ASN B 33  ? 0.4724 0.2859 0.4652 -0.0417 0.0632  0.0139  256 ASN B ND2 
5646  N N   . ILE B 34  ? 0.3259 0.1885 0.2142 -0.1087 -0.0114 0.0271  257 ILE B N   
5647  C CA  . ILE B 34  ? 0.2953 0.2056 0.2317 -0.0993 -0.0225 0.0203  257 ILE B CA  
5648  C C   . ILE B 34  ? 0.2709 0.1841 0.1963 -0.0708 -0.0111 0.0037  257 ILE B C   
5649  O O   . ILE B 34  ? 0.2791 0.2004 0.2643 -0.0464 -0.0010 -0.0316 257 ILE B O   
5650  C CB  . ILE B 34  ? 0.3097 0.2499 0.3151 -0.0979 -0.0298 0.0307  257 ILE B CB  
5651  C CG1 . ILE B 34  ? 0.3257 0.2669 0.3438 -0.0750 -0.0283 0.0386  257 ILE B CG1 
5652  C CG2 . ILE B 34  ? 0.3153 0.2698 0.3422 -0.1062 -0.0255 0.0315  257 ILE B CG2 
5653  C CD1 . ILE B 34  ? 0.3299 0.2679 0.3676 -0.0616 -0.0287 0.0474  257 ILE B CD1 
5665  N N   . VAL B 35  ? 0.2681 0.1702 0.1286 -0.0545 0.0156  0.0220  258 VAL B N   
5666  C CA  . VAL B 35  ? 0.2433 0.1492 0.1159 -0.0277 0.0015  0.0389  258 VAL B CA  
5667  C C   . VAL B 35  ? 0.2041 0.1342 0.1169 0.0083  0.0101  0.0185  258 VAL B C   
5668  O O   . VAL B 35  ? 0.2151 0.1654 0.1458 0.0382  0.0294  0.0185  258 VAL B O   
5669  C CB  . VAL B 35  ? 0.2810 0.1674 0.1277 -0.0294 -0.0183 0.0401  258 VAL B CB  
5670  C CG1 . VAL B 35  ? 0.2856 0.1722 0.1408 -0.0233 -0.0310 0.0371  258 VAL B CG1 
5671  C CG2 . VAL B 35  ? 0.3184 0.1882 0.1406 -0.0273 -0.0096 0.0391  258 VAL B CG2 
5681  N N   . VAL B 36  ? 0.1294 0.0846 0.0988 0.0072  -0.0206 -0.0002 259 VAL B N   
5682  C CA  . VAL B 36  ? 0.1048 0.0753 0.1025 -0.0003 -0.0182 0.0109  259 VAL B CA  
5683  C C   . VAL B 36  ? 0.0829 0.0825 0.0918 0.0074  -0.0174 0.0043  259 VAL B C   
5684  O O   . VAL B 36  ? 0.0879 0.0905 0.0995 0.0138  -0.0151 0.0048  259 VAL B O   
5685  C CB  . VAL B 36  ? 0.1151 0.0888 0.1022 -0.0019 -0.0139 -0.0105 259 VAL B CB  
5686  C CG1 . VAL B 36  ? 0.1002 0.0957 0.1090 0.0131  -0.0172 0.0081  259 VAL B CG1 
5687  C CG2 . VAL B 36  ? 0.1625 0.1050 0.1173 -0.0026 0.0108  -0.0182 259 VAL B CG2 
5697  N N   . GLN B 37  ? 0.0622 0.0858 0.0990 0.0057  -0.0052 -0.0046 260 GLN B N   
5698  C CA  . GLN B 37  ? 0.0858 0.0824 0.0879 0.0124  -0.0231 -0.0036 260 GLN B CA  
5699  C C   . GLN B 37  ? 0.0598 0.0763 0.0869 0.0062  -0.0215 -0.0122 260 GLN B C   
5700  O O   . GLN B 37  ? 0.0633 0.0722 0.0756 0.0053  -0.0089 0.0003  260 GLN B O   
5701  C CB  . GLN B 37  ? 0.0821 0.0937 0.0884 0.0182  -0.0237 0.0097  260 GLN B CB  
5702  C CG  . GLN B 37  ? 0.1126 0.1107 0.1097 -0.0043 -0.0257 0.0191  260 GLN B CG  
5703  C CD  . GLN B 37  ? 0.1392 0.1337 0.1261 -0.0087 -0.0373 0.0226  260 GLN B CD  
5704  O OE1 . GLN B 37  ? 0.2015 0.1756 0.1353 -0.0260 -0.0637 0.0456  260 GLN B OE1 
5705  N NE2 . GLN B 37  ? 0.1230 0.1369 0.1193 0.0073  -0.0472 -0.0007 260 GLN B NE2 
5714  N N   . PRO B 38  ? 0.0623 0.0635 0.0911 0.0093  -0.0112 0.0034  261 PRO B N   
5715  C CA  . PRO B 38  ? 0.0557 0.0591 0.0924 0.0123  -0.0114 -0.0007 261 PRO B CA  
5716  C C   . PRO B 38  ? 0.0559 0.0609 0.0836 0.0069  -0.0062 0.0164  261 PRO B C   
5717  O O   . PRO B 38  ? 0.0506 0.0783 0.0882 0.0128  -0.0061 0.0013  261 PRO B O   
5718  C CB  . PRO B 38  ? 0.0646 0.0589 0.0917 0.0039  -0.0220 0.0027  261 PRO B CB  
5719  C CG  . PRO B 38  ? 0.0799 0.0684 0.0924 -0.0008 -0.0296 0.0038  261 PRO B CG  
5720  C CD  . PRO B 38  ? 0.0664 0.0673 0.0903 0.0143  -0.0191 -0.0042 261 PRO B CD  
5728  N N   . GLN B 39  ? 0.0545 0.0725 0.0828 0.0038  -0.0097 0.0049  262 GLN B N   
5729  C CA  . GLN B 39  ? 0.0499 0.0772 0.0709 -0.0034 -0.0196 0.0023  262 GLN B CA  
5730  C C   . GLN B 39  ? 0.0577 0.0710 0.0767 -0.0040 -0.0134 -0.0003 262 GLN B C   
5731  O O   . GLN B 39  ? 0.0649 0.0768 0.0874 -0.0003 -0.0235 0.0016  262 GLN B O   
5732  C CB  . GLN B 39  ? 0.0654 0.0822 0.0575 -0.0057 -0.0107 -0.0005 262 GLN B CB  
5733  C CG  . GLN B 39  ? 0.0901 0.0751 0.0713 -0.0074 0.0030  0.0147  262 GLN B CG  
5734  C CD  . GLN B 39  ? 0.0852 0.0756 0.0696 -0.0049 -0.0098 0.0249  262 GLN B CD  
5735  O OE1 . GLN B 39  ? 0.0919 0.0882 0.0718 -0.0168 -0.0123 0.0105  262 GLN B OE1 
5736  N NE2 . GLN B 39  ? 0.0754 0.0836 0.0843 0.0106  -0.0108 0.0187  262 GLN B NE2 
5745  N N   . ASN B 40  ? 0.0611 0.0684 0.0766 0.0017  -0.0167 0.0042  263 ASN B N   
5746  C CA  . ASN B 40  ? 0.0582 0.0713 0.0789 0.0019  -0.0079 0.0055  263 ASN B CA  
5747  C C   . ASN B 40  ? 0.0498 0.0734 0.0668 0.0015  -0.0108 0.0001  263 ASN B C   
5748  O O   . ASN B 40  ? 0.0675 0.0686 0.0840 -0.0044 -0.0031 -0.0105 263 ASN B O   
5749  C CB  . ASN B 40  ? 0.0656 0.0690 0.0705 -0.0063 -0.0093 0.0056  263 ASN B CB  
5750  C CG  . ASN B 40  ? 0.0727 0.0741 0.0767 -0.0015 -0.0043 -0.0005 263 ASN B CG  
5751  O OD1 . ASN B 40  ? 0.0738 0.0766 0.0763 0.0046  -0.0172 -0.0033 263 ASN B OD1 
5752  N ND2 . ASN B 40  ? 0.0645 0.0729 0.0859 0.0002  0.0027  -0.0147 263 ASN B ND2 
5759  N N   . GLY B 41  ? 0.0712 0.0706 0.0774 0.0071  0.0002  -0.0076 264 GLY B N   
5760  C CA  . GLY B 41  ? 0.0402 0.0868 0.0699 0.0051  -0.0063 -0.0115 264 GLY B CA  
5761  C C   . GLY B 41  ? 0.0582 0.0809 0.0729 -0.0020 -0.0003 -0.0175 264 GLY B C   
5762  O O   . GLY B 41  ? 0.0564 0.0977 0.0820 0.0055  -0.0122 -0.0232 264 GLY B O   
5766  N N   . ARG B 42  ? 0.0609 0.0750 0.0724 0.0009  -0.0115 -0.0145 265 ARG B N   
5767  C CA  . ARG B 42  ? 0.0572 0.0825 0.0749 0.0109  -0.0150 -0.0077 265 ARG B CA  
5768  C C   . ARG B 42  ? 0.0582 0.0693 0.0883 0.0060  -0.0234 -0.0085 265 ARG B C   
5769  O O   . ARG B 42  ? 0.0665 0.0715 0.1074 0.0000  -0.0196 -0.0182 265 ARG B O   
5770  C CB  . ARG B 42  ? 0.0593 0.0947 0.0918 0.0051  -0.0242 -0.0210 265 ARG B CB  
5771  C CG  . ARG B 42  ? 0.0659 0.1094 0.0975 0.0129  -0.0177 -0.0044 265 ARG B CG  
5772  C CD  . ARG B 42  ? 0.0766 0.1109 0.0980 0.0087  -0.0303 -0.0052 265 ARG B CD  
5773  N NE  . ARG B 42  ? 0.0876 0.1140 0.0899 0.0038  -0.0156 -0.0194 265 ARG B NE  
5774  C CZ  . ARG B 42  ? 0.1034 0.1319 0.1214 0.0330  -0.0226 -0.0048 265 ARG B CZ  
5775  N NH1 . ARG B 42  ? 0.1138 0.1311 0.1210 0.0417  -0.0179 -0.0058 265 ARG B NH1 
5776  N NH2 . ARG B 42  ? 0.1379 0.1381 0.1353 0.0552  -0.0269 -0.0045 265 ARG B NH2 
5790  N N   . CYS B 43  ? 0.0643 0.0733 0.1079 -0.0092 0.0012  -0.0177 266 CYS B N   
5791  C CA  . CYS B 43  ? 0.0680 0.0758 0.1043 -0.0056 -0.0016 -0.0098 266 CYS B CA  
5792  C C   . CYS B 43  ? 0.0756 0.0815 0.1212 -0.0136 0.0146  -0.0020 266 CYS B C   
5793  O O   . CYS B 43  ? 0.0704 0.0952 0.1383 -0.0040 -0.0035 -0.0087 266 CYS B O   
5794  C CB  . CYS B 43  ? 0.0885 0.0872 0.1246 0.0046  0.0032  0.0060  266 CYS B CB  
5795  S SG  . CYS B 43  ? 0.0890 0.0980 0.1461 0.0153  0.0032  0.0193  266 CYS B SG  
5801  N N   . THR B 44  ? 0.0682 0.0746 0.1030 -0.0094 0.0059  0.0000  267 THR B N   
5802  C CA  . THR B 44  ? 0.0545 0.0727 0.1116 -0.0049 -0.0083 0.0068  267 THR B CA  
5803  C C   . THR B 44  ? 0.0402 0.0760 0.1167 -0.0024 -0.0056 0.0038  267 THR B C   
5804  O O   . THR B 44  ? 0.0556 0.0636 0.1226 0.0021  0.0006  0.0171  267 THR B O   
5805  C CB  . THR B 44  ? 0.0758 0.0730 0.1185 0.0041  -0.0063 0.0042  267 THR B CB  
5806  O OG1 . THR B 44  ? 0.0742 0.0746 0.1303 -0.0048 -0.0192 -0.0006 267 THR B OG1 
5807  C CG2 . THR B 44  ? 0.1043 0.0831 0.1188 0.0104  -0.0134 0.0076  267 THR B CG2 
5815  N N   . ILE B 45  ? 0.0504 0.0934 0.1060 0.0051  -0.0103 -0.0066 268 ILE B N   
5816  C CA  . ILE B 45  ? 0.0645 0.0898 0.1154 0.0005  -0.0155 -0.0030 268 ILE B CA  
5817  C C   . ILE B 45  ? 0.0768 0.0834 0.1172 -0.0024 0.0044  -0.0018 268 ILE B C   
5818  O O   . ILE B 45  ? 0.1078 0.0837 0.1221 -0.0108 0.0124  0.0024  268 ILE B O   
5819  C CB  . ILE B 45  ? 0.1009 0.0958 0.1175 -0.0016 -0.0027 -0.0101 268 ILE B CB  
5820  C CG1 . ILE B 45  ? 0.1057 0.0946 0.1395 0.0080  0.0322  -0.0050 268 ILE B CG1 
5821  C CG2 . ILE B 45  ? 0.1197 0.1011 0.1144 -0.0201 -0.0238 -0.0206 268 ILE B CG2 
5822  C CD1 . ILE B 45  ? 0.1689 0.1042 0.1610 0.0059  0.0581  -0.0052 268 ILE B CD1 
5834  N N   . ASP B 46  ? 0.0558 0.0880 0.1314 -0.0063 -0.0021 0.0072  269 ASP B N   
5835  C CA  . ASP B 46  ? 0.0609 0.1092 0.1459 -0.0155 -0.0163 -0.0048 269 ASP B CA  
5836  C C   . ASP B 46  ? 0.0694 0.0934 0.1278 -0.0283 0.0000  -0.0016 269 ASP B C   
5837  O O   . ASP B 46  ? 0.0835 0.1078 0.1842 -0.0252 -0.0047 -0.0155 269 ASP B O   
5838  C CB  . ASP B 46  ? 0.0526 0.1516 0.1814 -0.0112 -0.0228 0.0040  269 ASP B CB  
5839  C CG  . ASP B 46  ? 0.0702 0.2159 0.1930 0.0103  -0.0412 0.0163  269 ASP B CG  
5840  O OD1 . ASP B 46  ? 0.0767 0.2199 0.1984 -0.0012 -0.0199 0.0141  269 ASP B OD1 
5841  O OD2 . ASP B 46  ? 0.0800 0.2798 0.2291 0.0005  -0.0170 0.0508  269 ASP B OD2 
5846  N N   . GLY B 47  ? 0.0702 0.0815 0.1205 -0.0126 -0.0002 0.0067  270 GLY B N   
5847  C CA  . GLY B 47  ? 0.0806 0.0856 0.1143 -0.0045 -0.0069 0.0008  270 GLY B CA  
5848  C C   . GLY B 47  ? 0.0937 0.0816 0.1130 0.0013  -0.0092 -0.0073 270 GLY B C   
5849  O O   . GLY B 47  ? 0.1138 0.0852 0.1208 0.0011  -0.0049 -0.0031 270 GLY B O   
5853  N N   . GLU B 48  ? 0.0709 0.0863 0.1027 -0.0108 -0.0070 -0.0089 271 GLU B N   
5854  C CA  . GLU B 48  ? 0.0794 0.0931 0.1078 -0.0064 -0.0255 -0.0030 271 GLU B CA  
5855  C C   . GLU B 48  ? 0.0770 0.0658 0.0967 -0.0053 -0.0299 0.0070  271 GLU B C   
5856  O O   . GLU B 48  ? 0.0901 0.0649 0.1102 -0.0029 0.0004  -0.0053 271 GLU B O   
5857  C CB  . GLU B 48  ? 0.0870 0.1249 0.1390 0.0029  -0.0459 -0.0055 271 GLU B CB  
5858  C CG  . GLU B 48  ? 0.1854 0.1879 0.1858 0.0140  -0.0312 -0.0008 271 GLU B CG  
5859  C CD  . GLU B 48  ? 0.2566 0.2621 0.2436 0.0399  -0.0198 -0.0210 271 GLU B CD  
5860  O OE1 . GLU B 48  ? 0.2638 0.2965 0.2765 0.0667  -0.0428 -0.0199 271 GLU B OE1 
5861  O OE2 . GLU B 48  ? 0.2916 0.2932 0.2560 0.0246  -0.0278 -0.0300 271 GLU B OE2 
5868  N N   . LEU B 49  ? 0.0844 0.0658 0.1125 -0.0127 -0.0133 -0.0049 272 LEU B N   
5869  C CA  . LEU B 49  ? 0.0813 0.0801 0.1082 -0.0019 -0.0179 -0.0053 272 LEU B CA  
5870  C C   . LEU B 49  ? 0.0806 0.0827 0.0981 0.0012  -0.0161 -0.0011 272 LEU B C   
5871  O O   . LEU B 49  ? 0.0953 0.1051 0.1096 -0.0191 -0.0300 0.0014  272 LEU B O   
5872  C CB  . LEU B 49  ? 0.1055 0.0860 0.1163 -0.0053 -0.0232 -0.0031 272 LEU B CB  
5873  C CG  . LEU B 49  ? 0.0960 0.0959 0.1191 0.0038  -0.0282 0.0135  272 LEU B CG  
5874  C CD1 . LEU B 49  ? 0.1255 0.1043 0.1579 0.0057  -0.0087 0.0166  272 LEU B CD1 
5875  C CD2 . LEU B 49  ? 0.1193 0.1116 0.1212 0.0185  -0.0137 0.0130  272 LEU B CD2 
5887  N N   . LEU B 50  ? 0.0709 0.0844 0.0907 -0.0049 -0.0170 0.0161  273 LEU B N   
5888  C CA  . LEU B 50  ? 0.0672 0.0774 0.1071 -0.0127 -0.0200 0.0118  273 LEU B CA  
5889  C C   . LEU B 50  ? 0.0827 0.0750 0.1149 -0.0062 -0.0096 0.0057  273 LEU B C   
5890  O O   . LEU B 50  ? 0.0728 0.0829 0.1093 0.0044  -0.0170 -0.0038 273 LEU B O   
5891  C CB  . LEU B 50  ? 0.0789 0.0919 0.1341 -0.0040 -0.0099 0.0184  273 LEU B CB  
5892  C CG  . LEU B 50  ? 0.0817 0.1126 0.1918 -0.0106 -0.0100 0.0094  273 LEU B CG  
5893  C CD1 . LEU B 50  ? 0.0834 0.1240 0.2089 0.0065  -0.0100 0.0121  273 LEU B CD1 
5894  C CD2 . LEU B 50  ? 0.0996 0.1344 0.2378 -0.0017 -0.0026 0.0113  273 LEU B CD2 
5906  N N   . GLY B 51  ? 0.0684 0.0790 0.1038 0.0006  -0.0197 0.0149  274 GLY B N   
5907  C CA  . GLY B 51  ? 0.0843 0.0841 0.1016 -0.0009 0.0082  0.0085  274 GLY B CA  
5908  C C   . GLY B 51  ? 0.0733 0.0843 0.0874 0.0014  -0.0079 -0.0101 274 GLY B C   
5909  O O   . GLY B 51  ? 0.0731 0.0905 0.1176 -0.0010 -0.0194 -0.0144 274 GLY B O   
5913  N N   . THR B 52  ? 0.0792 0.0697 0.0685 -0.0111 -0.0052 -0.0054 275 THR B N   
5914  C CA  . THR B 52  ? 0.0819 0.0634 0.0741 -0.0131 0.0072  -0.0099 275 THR B CA  
5915  C C   . THR B 52  ? 0.0791 0.0672 0.0772 -0.0079 -0.0039 -0.0061 275 THR B C   
5916  O O   . THR B 52  ? 0.0848 0.0703 0.0784 0.0088  -0.0057 -0.0006 275 THR B O   
5917  C CB  . THR B 52  ? 0.0774 0.0793 0.0800 -0.0113 -0.0130 -0.0016 275 THR B CB  
5918  O OG1 . THR B 52  ? 0.0720 0.0795 0.0724 0.0003  -0.0069 -0.0073 275 THR B OG1 
5919  C CG2 . THR B 52  ? 0.1002 0.0958 0.0759 -0.0117 0.0024  -0.0014 275 THR B CG2 
5927  N N   . THR B 53  ? 0.0705 0.0826 0.0673 0.0021  -0.0119 0.0074  276 THR B N   
5928  C CA  . THR B 53  ? 0.0624 0.0811 0.0802 -0.0069 -0.0053 -0.0049 276 THR B CA  
5929  C C   . THR B 53  ? 0.0721 0.0820 0.0946 -0.0060 -0.0184 -0.0036 276 THR B C   
5930  O O   . THR B 53  ? 0.0811 0.0854 0.1094 -0.0099 -0.0305 0.0018  276 THR B O   
5931  C CB  . THR B 53  ? 0.0696 0.0835 0.0785 -0.0008 -0.0078 -0.0069 276 THR B CB  
5932  O OG1 . THR B 53  ? 0.0796 0.0824 0.0648 0.0034  -0.0125 -0.0058 276 THR B OG1 
5933  C CG2 . THR B 53  ? 0.0548 0.0943 0.0954 0.0079  -0.0012 -0.0084 276 THR B CG2 
5941  N N   . GLN B 54  ? 0.0611 0.0769 0.0967 -0.0110 -0.0158 0.0039  277 GLN B N   
5942  C CA  . GLN B 54  ? 0.0751 0.0814 0.0931 -0.0236 -0.0078 0.0013  277 GLN B CA  
5943  C C   . GLN B 54  ? 0.0777 0.0818 0.0926 -0.0205 -0.0115 0.0044  277 GLN B C   
5944  O O   . GLN B 54  ? 0.1062 0.0885 0.0916 -0.0215 -0.0059 -0.0003 277 GLN B O   
5945  C CB  . GLN B 54  ? 0.0946 0.0845 0.0826 -0.0166 -0.0049 -0.0066 277 GLN B CB  
5946  C CG  . GLN B 54  ? 0.0991 0.0877 0.0903 -0.0054 -0.0154 -0.0036 277 GLN B CG  
5947  C CD  . GLN B 54  ? 0.0869 0.0938 0.0990 -0.0027 -0.0117 0.0105  277 GLN B CD  
5948  O OE1 . GLN B 54  ? 0.0952 0.0962 0.1125 -0.0033 -0.0011 0.0103  277 GLN B OE1 
5949  N NE2 . GLN B 54  ? 0.0873 0.1043 0.1019 0.0022  -0.0186 0.0068  277 GLN B NE2 
5958  N N   . LEU B 55  ? 0.0854 0.0788 0.0828 -0.0003 0.0049  0.0029  278 LEU B N   
5959  C CA  . LEU B 55  ? 0.0975 0.0877 0.0922 -0.0128 0.0000  0.0061  278 LEU B CA  
5960  C C   . LEU B 55  ? 0.1266 0.0981 0.0986 -0.0111 -0.0125 0.0143  278 LEU B C   
5961  O O   . LEU B 55  ? 0.1453 0.1121 0.0940 -0.0156 -0.0134 0.0059  278 LEU B O   
5962  C CB  . LEU B 55  ? 0.0995 0.1056 0.1176 -0.0069 0.0106  0.0098  278 LEU B CB  
5963  C CG  . LEU B 55  ? 0.1230 0.1063 0.1671 -0.0123 0.0158  -0.0264 278 LEU B CG  
5964  C CD1 . LEU B 55  ? 0.1457 0.1328 0.1818 -0.0302 0.0403  -0.0426 278 LEU B CD1 
5965  C CD2 . LEU B 55  ? 0.1200 0.0915 0.1732 -0.0073 0.0259  -0.0030 278 LEU B CD2 
5977  N N   A ILE B 56  ? 0.1017 0.1218 0.1098 -0.0206 -0.0217 0.0432  279 ILE B N   
5978  C CA  A ILE B 56  ? 0.1029 0.1184 0.1186 0.0062  -0.0332 0.0443  279 ILE B CA  
5979  C C   A ILE B 56  ? 0.0933 0.1030 0.1078 0.0209  -0.0352 0.0089  279 ILE B C   
5980  O O   A ILE B 56  ? 0.0800 0.1078 0.0980 0.0039  -0.0169 0.0222  279 ILE B O   
5981  C CB  A ILE B 56  ? 0.1272 0.1129 0.1913 0.0120  -0.0284 0.0733  279 ILE B CB  
5982  C CG1 A ILE B 56  ? 0.1427 0.1365 0.2174 0.0052  -0.0145 0.0494  279 ILE B CG1 
5983  C CG2 A ILE B 56  ? 0.1633 0.1340 0.2243 0.0163  -0.0104 0.0725  279 ILE B CG2 
5984  C CD1 A ILE B 56  ? 0.1509 0.1499 0.2306 0.0063  -0.0044 0.0289  279 ILE B CD1 
6037  N N   . ASN B 59  ? 0.1097 0.0917 0.1286 -0.0023 -0.0030 0.0158  282 ASN B N   
6038  C CA  . ASN B 59  ? 0.1017 0.0665 0.1243 -0.0101 0.0047  -0.0057 282 ASN B CA  
6039  C C   . ASN B 59  ? 0.0873 0.0682 0.1022 -0.0025 0.0050  0.0014  282 ASN B C   
6040  O O   . ASN B 59  ? 0.1083 0.0661 0.1029 0.0044  0.0065  -0.0089 282 ASN B O   
6041  C CB  . ASN B 59  ? 0.1357 0.0772 0.1323 -0.0195 0.0160  -0.0059 282 ASN B CB  
6042  C CG  . ASN B 59  ? 0.1643 0.0833 0.1719 -0.0111 0.0248  0.0168  282 ASN B CG  
6043  O OD1 . ASN B 59  ? 0.1755 0.0838 0.1985 0.0091  0.0354  0.0152  282 ASN B OD1 
6044  N ND2 . ASN B 59  ? 0.1854 0.0824 0.1660 -0.0105 0.0237  0.0064  282 ASN B ND2 
6051  N N   . ILE B 60  ? 0.0661 0.0692 0.0894 -0.0054 -0.0074 -0.0001 283 ILE B N   
6052  C CA  . ILE B 60  ? 0.0594 0.0600 0.0864 0.0034  -0.0006 0.0048  283 ILE B CA  
6053  C C   . ILE B 60  ? 0.0613 0.0561 0.0927 -0.0017 -0.0078 -0.0046 283 ILE B C   
6054  O O   . ILE B 60  ? 0.0621 0.0669 0.1020 0.0036  -0.0174 -0.0021 283 ILE B O   
6055  C CB  . ILE B 60  ? 0.0638 0.0686 0.0857 0.0061  -0.0148 -0.0173 283 ILE B CB  
6056  C CG1 . ILE B 60  ? 0.0852 0.0711 0.0955 0.0172  0.0067  -0.0097 283 ILE B CG1 
6057  C CG2 . ILE B 60  ? 0.0787 0.0738 0.0954 0.0101  0.0026  -0.0223 283 ILE B CG2 
6058  C CD1 . ILE B 60  ? 0.1074 0.0840 0.1107 0.0154  0.0104  0.0077  283 ILE B CD1 
6070  N N   . CYS B 61  ? 0.0568 0.0664 0.0824 0.0102  -0.0078 0.0037  284 CYS B N   
6071  C CA  . CYS B 61  ? 0.0691 0.0615 0.0892 -0.0094 -0.0055 -0.0079 284 CYS B CA  
6072  C C   . CYS B 61  ? 0.0661 0.0704 0.0922 -0.0068 -0.0057 -0.0070 284 CYS B C   
6073  O O   . CYS B 61  ? 0.0694 0.0860 0.1127 -0.0092 -0.0142 0.0015  284 CYS B O   
6074  C CB  . CYS B 61  ? 0.0846 0.0701 0.0968 0.0041  -0.0158 0.0020  284 CYS B CB  
6075  S SG  . CYS B 61  ? 0.0972 0.0610 0.1061 0.0057  -0.0068 -0.0054 284 CYS B SG  
6081  N N   . SER B 62  ? 0.0664 0.0654 0.0950 0.0052  -0.0081 -0.0198 285 SER B N   
6082  C CA  A SER B 62  ? 0.0770 0.0664 0.0982 0.0126  -0.0141 -0.0203 285 SER B CA  
6083  C CA  B SER B 62  ? 0.0816 0.0715 0.1069 0.0121  -0.0093 -0.0242 285 SER B CA  
6084  C C   . SER B 62  ? 0.0778 0.0759 0.1152 0.0197  -0.0215 -0.0181 285 SER B C   
6085  O O   . SER B 62  ? 0.0915 0.1198 0.1342 0.0379  -0.0351 -0.0565 285 SER B O   
6086  C CB  A SER B 62  ? 0.0942 0.0703 0.1225 0.0063  -0.0014 -0.0084 285 SER B CB  
6087  C CB  B SER B 62  ? 0.1042 0.0780 0.1223 0.0085  0.0053  -0.0282 285 SER B CB  
6088  O OG  A SER B 62  ? 0.0937 0.0697 0.1158 -0.0050 -0.0080 -0.0134 285 SER B OG  
6089  O OG  B SER B 62  ? 0.1202 0.0821 0.1298 0.0031  0.0144  -0.0386 285 SER B OG  
6100  N N   . PHE B 63  ? 0.0650 0.0593 0.1029 0.0057  -0.0088 -0.0180 286 PHE B N   
6101  C CA  . PHE B 63  ? 0.0805 0.0612 0.1026 0.0047  -0.0220 -0.0211 286 PHE B CA  
6102  C C   . PHE B 63  ? 0.0762 0.0766 0.0951 0.0016  -0.0177 -0.0227 286 PHE B C   
6103  O O   . PHE B 63  ? 0.0665 0.0745 0.1155 -0.0037 -0.0292 -0.0175 286 PHE B O   
6104  C CB  . PHE B 63  ? 0.1079 0.0716 0.1108 0.0146  -0.0246 -0.0141 286 PHE B CB  
6105  C CG  . PHE B 63  ? 0.1066 0.0735 0.1112 0.0152  -0.0082 -0.0213 286 PHE B CG  
6106  C CD1 . PHE B 63  ? 0.1323 0.0778 0.1098 0.0395  -0.0130 -0.0106 286 PHE B CD1 
6107  C CD2 . PHE B 63  ? 0.1003 0.0782 0.1470 0.0149  0.0152  -0.0058 286 PHE B CD2 
6108  C CE1 . PHE B 63  ? 0.1453 0.0908 0.1121 0.0366  -0.0006 -0.0089 286 PHE B CE1 
6109  C CE2 . PHE B 63  ? 0.1035 0.0794 0.1471 0.0015  0.0471  -0.0045 286 PHE B CE2 
6110  C CZ  . PHE B 63  ? 0.1188 0.0841 0.1324 0.0201  0.0297  -0.0031 286 PHE B CZ  
6120  N N   . ARG B 64  ? 0.0823 0.0763 0.0995 0.0172  -0.0307 -0.0228 287 ARG B N   
6121  C CA  C ARG B 64  ? 0.1010 0.0778 0.1053 0.0215  -0.0187 -0.0201 287 ARG B CA  
6122  C CA  D ARG B 64  ? 0.1003 0.0680 0.1108 0.0162  -0.0171 -0.0224 287 ARG B CA  
6123  C C   . ARG B 64  ? 0.0872 0.0688 0.0946 0.0142  -0.0188 -0.0230 287 ARG B C   
6124  O O   . ARG B 64  ? 0.0835 0.0941 0.1051 0.0235  -0.0247 -0.0242 287 ARG B O   
6125  C CB  C ARG B 64  ? 0.1526 0.1070 0.1357 0.0192  0.0055  -0.0271 287 ARG B CB  
6126  C CB  D ARG B 64  ? 0.1621 0.0787 0.1554 0.0084  0.0238  -0.0283 287 ARG B CB  
6127  C CG  C ARG B 64  ? 0.1630 0.1285 0.1401 0.0326  -0.0064 -0.0194 287 ARG B CG  
6128  C CG  D ARG B 64  ? 0.1873 0.0875 0.1826 0.0170  0.0331  -0.0192 287 ARG B CG  
6129  C CD  C ARG B 64  ? 0.1704 0.1383 0.1547 0.0324  -0.0205 -0.0278 287 ARG B CD  
6130  C CD  D ARG B 64  ? 0.1955 0.0894 0.2160 -0.0026 0.0294  -0.0159 287 ARG B CD  
6131  N NE  C ARG B 64  ? 0.1666 0.1316 0.1692 0.0437  -0.0417 -0.0281 287 ARG B NE  
6132  N NE  D ARG B 64  ? 0.2171 0.1062 0.2527 -0.0036 0.0385  -0.0002 287 ARG B NE  
6133  C CZ  C ARG B 64  ? 0.1689 0.1356 0.1902 0.0517  -0.0681 -0.0071 287 ARG B CZ  
6134  C CZ  D ARG B 64  ? 0.2321 0.1199 0.2743 -0.0020 0.0412  0.0154  287 ARG B CZ  
6135  N NH1 C ARG B 64  ? 0.1802 0.1429 0.1998 0.0477  -0.0596 -0.0186 287 ARG B NH1 
6136  N NH1 D ARG B 64  ? 0.2276 0.1183 0.2671 0.0097  0.0293  0.0436  287 ARG B NH1 
6137  N NH2 C ARG B 64  ? 0.1713 0.1118 0.2094 0.0262  -0.1019 -0.0176 287 ARG B NH2 
6138  N NH2 D ARG B 64  ? 0.2441 0.1265 0.2978 -0.0051 0.0544  -0.0018 287 ARG B NH2 
6165  N N   . GLY B 65  ? 0.0674 0.0626 0.0923 0.0086  -0.0241 -0.0158 288 GLY B N   
6166  C CA  . GLY B 65  ? 0.0700 0.0761 0.0996 0.0139  -0.0268 -0.0144 288 GLY B CA  
6167  C C   . GLY B 65  ? 0.0691 0.0751 0.1049 0.0099  -0.0234 -0.0202 288 GLY B C   
6168  O O   . GLY B 65  ? 0.0681 0.0768 0.1143 0.0165  -0.0189 -0.0116 288 GLY B O   
6172  N N   . SER B 66  ? 0.0641 0.0758 0.1348 0.0155  -0.0194 -0.0152 289 SER B N   
6173  C CA  A SER B 66  ? 0.0835 0.0693 0.1119 0.0198  -0.0089 -0.0165 289 SER B CA  
6174  C CA  B SER B 66  ? 0.0840 0.0591 0.1238 0.0198  -0.0066 -0.0112 289 SER B CA  
6175  C C   . SER B 66  ? 0.0930 0.0576 0.1028 0.0307  -0.0079 -0.0005 289 SER B C   
6176  O O   . SER B 66  ? 0.1038 0.0882 0.1147 0.0393  0.0011  0.0054  289 SER B O   
6177  C CB  A SER B 66  ? 0.0985 0.0939 0.1018 0.0038  -0.0117 -0.0230 289 SER B CB  
6178  C CB  B SER B 66  ? 0.0979 0.0648 0.1373 0.0047  -0.0073 -0.0114 289 SER B CB  
6179  O OG  A SER B 66  ? 0.1177 0.1248 0.0971 -0.0041 -0.0093 -0.0344 289 SER B OG  
6180  O OG  B SER B 66  ? 0.1199 0.0819 0.1516 -0.0030 -0.0014 -0.0127 289 SER B OG  
6191  N N   . ILE B 67  ? 0.0950 0.0618 0.1035 0.0198  -0.0140 -0.0008 290 ILE B N   
6192  C CA  . ILE B 67  ? 0.0942 0.0562 0.1003 0.0193  -0.0093 -0.0041 290 ILE B CA  
6193  C C   . ILE B 67  ? 0.1049 0.0661 0.1101 0.0245  -0.0124 -0.0107 290 ILE B C   
6194  O O   . ILE B 67  ? 0.0963 0.0628 0.1187 0.0202  -0.0164 -0.0194 290 ILE B O   
6195  C CB  . ILE B 67  ? 0.0808 0.0641 0.1024 0.0181  -0.0142 -0.0043 290 ILE B CB  
6196  C CG1 . ILE B 67  ? 0.0909 0.0705 0.1020 0.0123  -0.0138 -0.0062 290 ILE B CG1 
6197  C CG2 . ILE B 67  ? 0.0834 0.0766 0.1132 0.0073  -0.0219 -0.0107 290 ILE B CG2 
6198  C CD1 . ILE B 67  ? 0.1082 0.0770 0.0950 0.0114  -0.0080 -0.0101 290 ILE B CD1 
6210  N N   A SER B 68  ? 0.1230 0.0901 0.1120 0.0269  -0.0195 -0.0074 291 SER B N   
6211  N N   B SER B 68  ? 0.1205 0.0781 0.1089 0.0345  -0.0250 -0.0057 291 SER B N   
6212  C CA  A SER B 68  ? 0.1465 0.1252 0.1108 0.0257  -0.0219 -0.0097 291 SER B CA  
6213  C CA  B SER B 68  ? 0.1440 0.0963 0.1107 0.0348  -0.0325 -0.0017 291 SER B CA  
6214  C C   A SER B 68  ? 0.1567 0.1334 0.1035 0.0236  -0.0159 -0.0149 291 SER B C   
6215  C C   B SER B 68  ? 0.1583 0.1204 0.1070 0.0221  -0.0208 -0.0046 291 SER B C   
6216  O O   A SER B 68  ? 0.1794 0.1526 0.1178 -0.0232 0.0132  -0.0384 291 SER B O   
6217  O O   B SER B 68  ? 0.1534 0.1232 0.1046 0.0164  -0.0382 0.0059  291 SER B O   
6218  C CB  A SER B 68  ? 0.1691 0.2028 0.1426 0.0073  0.0023  -0.0146 291 SER B CB  
6219  C CB  B SER B 68  ? 0.1605 0.1191 0.1333 0.0316  -0.0303 -0.0091 291 SER B CB  
6220  O OG  A SER B 68  ? 0.1783 0.2466 0.1651 0.0204  -0.0026 -0.0044 291 SER B OG  
6221  O OG  B SER B 68  ? 0.1714 0.1307 0.1392 0.0231  -0.0435 -0.0155 291 SER B OG  
6232  N N   . GLY B 69  ? 0.1585 0.1267 0.1022 0.0124  -0.0111 -0.0121 292 GLY B N   
6233  C CA  . GLY B 69  ? 0.1538 0.1444 0.1008 0.0028  0.0002  -0.0341 292 GLY B CA  
6234  C C   . GLY B 69  ? 0.1452 0.1223 0.0998 0.0067  0.0094  -0.0252 292 GLY B C   
6235  O O   . GLY B 69  ? 0.1374 0.1004 0.1034 0.0126  0.0107  -0.0080 292 GLY B O   
6240  N N   . HIS B 70  ? 0.1701 0.1430 0.0960 -0.0039 0.0265  -0.0258 293 HIS B N   
6241  C CA  . HIS B 70  ? 0.1991 0.1508 0.1167 -0.0254 0.0253  -0.0290 293 HIS B CA  
6242  C C   . HIS B 70  ? 0.2642 0.1648 0.1217 -0.0404 0.0195  -0.0294 293 HIS B C   
6243  O O   . HIS B 70  ? 0.2959 0.1741 0.1218 -0.0337 0.0275  -0.0228 293 HIS B O   
6244  C CB  . HIS B 70  ? 0.1857 0.1654 0.1298 -0.0330 0.0243  -0.0291 293 HIS B CB  
6245  C CG  . HIS B 70  ? 0.1754 0.1901 0.1386 -0.0341 0.0397  -0.0254 293 HIS B CG  
6246  N ND1 . HIS B 70  ? 0.2186 0.2232 0.1707 -0.0517 0.0652  -0.0328 293 HIS B ND1 
6247  C CD2 . HIS B 70  ? 0.1623 0.1867 0.1356 -0.0361 0.0270  -0.0357 293 HIS B CD2 
6248  C CE1 . HIS B 70  ? 0.2148 0.2181 0.1773 -0.0544 0.0765  -0.0447 293 HIS B CE1 
6249  N NE2 . HIS B 70  ? 0.1881 0.1986 0.1597 -0.0325 0.0517  -0.0441 293 HIS B NE2 
6257  N N   . GLU B 71  ? 0.3088 0.1720 0.1520 -0.0511 0.0475  -0.0154 294 GLU B N   
6258  C CA  . GLU B 71  ? 0.3469 0.2043 0.1865 -0.0597 0.0603  0.0032  294 GLU B CA  
6259  C C   . GLU B 71  ? 0.3500 0.2127 0.2004 -0.0813 0.0889  0.0004  294 GLU B C   
6260  O O   . GLU B 71  ? 0.3332 0.2046 0.1690 -0.0714 0.0640  -0.0075 294 GLU B O   
6261  C CB  . GLU B 71  ? 0.3980 0.2396 0.2512 -0.0379 0.0560  0.0332  294 GLU B CB  
6262  C CG  . GLU B 71  ? 0.4537 0.2845 0.3342 -0.0102 0.0578  0.0477  294 GLU B CG  
6263  C CD  . GLU B 71  ? 0.4933 0.3158 0.4021 0.0031  0.0669  0.0571  294 GLU B CD  
6264  O OE1 . GLU B 71  ? 0.5014 0.3359 0.4226 0.0105  0.0669  0.0489  294 GLU B OE1 
6265  O OE2 . GLU B 71  ? 0.5192 0.3341 0.4310 0.0111  0.0681  0.0676  294 GLU B OE2 
6272  N N   . GLY B 72  ? 0.3716 0.2433 0.2583 -0.1011 0.0917  -0.0155 295 GLY B N   
6273  C CA  . GLY B 72  ? 0.4131 0.2646 0.2960 -0.0974 0.0904  -0.0057 295 GLY B CA  
6274  C C   . GLY B 72  ? 0.4391 0.2830 0.3265 -0.0976 0.0724  0.0096  295 GLY B C   
6275  O O   . GLY B 72  ? 0.4555 0.2973 0.3391 -0.1002 0.0679  0.0184  295 GLY B O   
6279  N N   . ASN B 73  ? 0.4401 0.2866 0.3395 -0.0925 0.0571  0.0106  296 ASN B N   
6280  C CA  . ASN B 73  ? 0.4400 0.2980 0.3564 -0.0890 0.0622  0.0216  296 ASN B CA  
6281  C C   . ASN B 73  ? 0.4213 0.3045 0.3640 -0.1047 0.0625  0.0191  296 ASN B C   
6282  O O   . ASN B 73  ? 0.4039 0.3021 0.3547 -0.1216 0.0542  0.0128  296 ASN B O   
6283  C CB  . ASN B 73  ? 0.4577 0.3077 0.3742 -0.0650 0.0630  0.0284  296 ASN B CB  
6284  C CG  . ASN B 73  ? 0.4806 0.3200 0.3867 -0.0498 0.0682  0.0324  296 ASN B CG  
6285  O OD1 . ASN B 73  ? 0.4947 0.3218 0.3936 -0.0426 0.0684  0.0319  296 ASN B OD1 
6286  N ND2 . ASN B 73  ? 0.4832 0.3244 0.3892 -0.0432 0.0653  0.0389  296 ASN B ND2 
6293  N N   . ASP B 74  ? 0.4209 0.3103 0.3756 -0.1051 0.0672  0.0275  297 ASP B N   
6294  C CA  . ASP B 74  ? 0.4273 0.3216 0.3984 -0.0967 0.0735  0.0254  297 ASP B CA  
6295  C C   . ASP B 74  ? 0.4024 0.3184 0.3969 -0.0938 0.0654  0.0249  297 ASP B C   
6296  O O   . ASP B 74  ? 0.3912 0.3143 0.3902 -0.0981 0.0625  0.0303  297 ASP B O   
6297  C CB  . ASP B 74  ? 0.4525 0.3344 0.4212 -0.0906 0.0809  0.0161  297 ASP B CB  
6298  C CG  . ASP B 74  ? 0.4815 0.3522 0.4473 -0.0789 0.0905  0.0103  297 ASP B CG  
6299  O OD1 . ASP B 74  ? 0.4934 0.3640 0.4582 -0.0686 0.0971  0.0083  297 ASP B OD1 
6300  O OD2 . ASP B 74  ? 0.4893 0.3555 0.4577 -0.0875 0.0889  0.0123  297 ASP B OD2 
6305  N N   . ASP B 75  ? 0.3873 0.3159 0.3981 -0.0934 0.0628  0.0221  298 ASP B N   
6306  C CA  . ASP B 75  ? 0.3760 0.3110 0.3920 -0.0871 0.0568  0.0102  298 ASP B CA  
6307  C C   . ASP B 75  ? 0.3341 0.2706 0.3459 -0.0907 0.0655  -0.0049 298 ASP B C   
6308  O O   . ASP B 75  ? 0.3397 0.2774 0.3565 -0.0747 0.0629  -0.0011 298 ASP B O   
6309  C CB  . ASP B 75  ? 0.4057 0.3392 0.4256 -0.0811 0.0371  0.0103  298 ASP B CB  
6310  C CG  . ASP B 75  ? 0.4355 0.3627 0.4533 -0.0811 0.0249  0.0203  298 ASP B CG  
6311  O OD1 . ASP B 75  ? 0.4512 0.3634 0.4758 -0.0823 0.0291  0.0240  298 ASP B OD1 
6312  O OD2 . ASP B 75  ? 0.4455 0.3760 0.4524 -0.0866 0.0206  0.0274  298 ASP B OD2 
6317  N N   A GLN B 76  ? 0.2761 0.2245 0.2807 -0.0978 0.0565  -0.0238 299 GLN B N   
6318  C CA  A GLN B 76  ? 0.2599 0.2032 0.2429 -0.0797 0.0613  -0.0317 299 GLN B CA  
6319  C C   A GLN B 76  ? 0.2104 0.1639 0.1703 -0.0568 0.0560  -0.0088 299 GLN B C   
6320  O O   A GLN B 76  ? 0.2200 0.1753 0.1652 -0.0612 0.0649  -0.0119 299 GLN B O   
6321  C CB  A GLN B 76  ? 0.3080 0.2161 0.2830 -0.0800 0.0701  -0.0661 299 GLN B CB  
6322  C CG  A GLN B 76  ? 0.3511 0.2447 0.3253 -0.0789 0.0845  -0.0630 299 GLN B CG  
6323  C CD  A GLN B 76  ? 0.3679 0.2650 0.3432 -0.0763 0.0659  -0.0578 299 GLN B CD  
6324  O OE1 A GLN B 76  ? 0.3747 0.2596 0.3364 -0.0653 0.0751  -0.0682 299 GLN B OE1 
6325  N NE2 A GLN B 76  ? 0.3687 0.2865 0.3709 -0.0744 0.0525  -0.0426 299 GLN B NE2 
6334  N N   . HIS B 77  ? 0.1544 0.1241 0.1477 -0.0297 0.0346  0.0169  300 HIS B N   
6335  C CA  . HIS B 77  ? 0.1159 0.1075 0.1314 -0.0138 0.0358  0.0167  300 HIS B CA  
6336  C C   . HIS B 77  ? 0.1021 0.1085 0.1186 -0.0090 0.0373  0.0092  300 HIS B C   
6337  O O   . HIS B 77  ? 0.1113 0.1190 0.1149 0.0073  0.0276  -0.0041 300 HIS B O   
6338  C CB  . HIS B 77  ? 0.1085 0.1047 0.1227 0.0048  0.0241  0.0175  300 HIS B CB  
6339  C CG  . HIS B 77  ? 0.1105 0.1219 0.1313 0.0034  0.0268  -0.0019 300 HIS B CG  
6340  N ND1 . HIS B 77  ? 0.1348 0.1458 0.1594 -0.0015 0.0176  -0.0265 300 HIS B ND1 
6341  C CD2 . HIS B 77  ? 0.1237 0.1334 0.1487 -0.0074 0.0468  -0.0097 300 HIS B CD2 
6342  C CE1 . HIS B 77  ? 0.1204 0.1499 0.1809 -0.0028 0.0428  -0.0123 300 HIS B CE1 
6343  N NE2 . HIS B 77  ? 0.1266 0.1400 0.1737 0.0019  0.0453  -0.0127 300 HIS B NE2 
6351  N N   . LEU B 78  ? 0.1011 0.1031 0.1146 0.0030  0.0176  0.0063  301 LEU B N   
6352  C CA  . LEU B 78  ? 0.1233 0.0962 0.1198 0.0132  0.0128  0.0070  301 LEU B CA  
6353  C C   . LEU B 78  ? 0.1221 0.0949 0.1029 0.0056  0.0228  -0.0188 301 LEU B C   
6354  O O   . LEU B 78  ? 0.1422 0.1114 0.1235 -0.0123 0.0386  -0.0336 301 LEU B O   
6355  C CB  . LEU B 78  ? 0.1651 0.1127 0.1437 -0.0022 0.0001  0.0222  301 LEU B CB  
6356  C CG  . LEU B 78  ? 0.2192 0.1364 0.1878 0.0023  -0.0025 0.0378  301 LEU B CG  
6357  C CD1 . LEU B 78  ? 0.2362 0.1409 0.2121 -0.0114 0.0242  0.0460  301 LEU B CD1 
6358  C CD2 . LEU B 78  ? 0.2736 0.1504 0.1972 0.0132  -0.0018 0.0416  301 LEU B CD2 
6370  N N   . TRP B 79  ? 0.1032 0.0830 0.0962 0.0151  0.0166  -0.0100 302 TRP B N   
6371  C CA  . TRP B 79  ? 0.1020 0.0811 0.1015 0.0084  0.0118  -0.0129 302 TRP B CA  
6372  C C   . TRP B 79  ? 0.1000 0.0747 0.0973 0.0093  -0.0090 -0.0077 302 TRP B C   
6373  O O   . TRP B 79  ? 0.0974 0.0917 0.1179 0.0166  -0.0039 -0.0216 302 TRP B O   
6374  C CB  . TRP B 79  ? 0.0859 0.0692 0.1124 0.0091  -0.0045 -0.0029 302 TRP B CB  
6375  C CG  . TRP B 79  ? 0.0861 0.0706 0.1092 0.0207  -0.0025 0.0110  302 TRP B CG  
6376  C CD1 . TRP B 79  ? 0.0677 0.0706 0.1176 0.0112  0.0049  -0.0056 302 TRP B CD1 
6377  C CD2 . TRP B 79  ? 0.0949 0.0675 0.1131 0.0135  -0.0012 0.0066  302 TRP B CD2 
6378  N NE1 . TRP B 79  ? 0.0749 0.0656 0.1170 0.0059  -0.0008 -0.0010 302 TRP B NE1 
6379  C CE2 . TRP B 79  ? 0.0967 0.0704 0.1200 0.0191  0.0184  0.0057  302 TRP B CE2 
6380  C CE3 . TRP B 79  ? 0.1065 0.0805 0.1208 0.0124  0.0023  -0.0027 302 TRP B CE3 
6381  C CZ2 . TRP B 79  ? 0.1016 0.0781 0.1293 0.0091  0.0246  -0.0018 302 TRP B CZ2 
6382  C CZ3 . TRP B 79  ? 0.1051 0.0792 0.1125 0.0089  0.0178  -0.0162 302 TRP B CZ3 
6383  C CH2 . TRP B 79  ? 0.1006 0.0832 0.1350 0.0169  0.0224  -0.0007 302 TRP B CH2 
6394  N N   . HIS B 80  ? 0.0990 0.0723 0.0978 0.0179  -0.0022 -0.0189 303 HIS B N   
6395  C CA  . HIS B 80  ? 0.1076 0.0773 0.0989 0.0280  -0.0226 -0.0129 303 HIS B CA  
6396  C C   . HIS B 80  ? 0.0916 0.0711 0.1087 0.0196  -0.0115 -0.0048 303 HIS B C   
6397  O O   . HIS B 80  ? 0.1100 0.0754 0.1226 0.0209  -0.0033 -0.0108 303 HIS B O   
6398  C CB  . HIS B 80  ? 0.1243 0.0924 0.1045 0.0300  -0.0355 0.0000  303 HIS B CB  
6399  C CG  . HIS B 80  ? 0.1528 0.1242 0.1422 0.0209  -0.0227 -0.0044 303 HIS B CG  
6400  N ND1 . HIS B 80  ? 0.1783 0.1545 0.1861 0.0153  -0.0225 -0.0036 303 HIS B ND1 
6401  C CD2 . HIS B 80  ? 0.1667 0.1518 0.1692 0.0172  -0.0270 -0.0028 303 HIS B CD2 
6402  C CE1 . HIS B 80  ? 0.1519 0.1603 0.1806 0.0234  -0.0432 0.0033  303 HIS B CE1 
6403  N NE2 . HIS B 80  ? 0.1554 0.1684 0.1849 0.0208  -0.0470 -0.0070 303 HIS B NE2 
6411  N N   . PHE B 81  ? 0.0758 0.0686 0.1165 0.0156  -0.0199 0.0098  304 PHE B N   
6412  C CA  . PHE B 81  ? 0.0850 0.0720 0.1010 0.0270  -0.0086 0.0095  304 PHE B CA  
6413  C C   . PHE B 81  ? 0.0787 0.0688 0.0913 0.0240  -0.0089 0.0023  304 PHE B C   
6414  O O   . PHE B 81  ? 0.0703 0.0679 0.1156 0.0217  -0.0112 0.0044  304 PHE B O   
6415  C CB  . PHE B 81  ? 0.0816 0.0696 0.1013 0.0300  -0.0146 -0.0089 304 PHE B CB  
6416  C CG  . PHE B 81  ? 0.0916 0.0779 0.1052 0.0154  -0.0230 -0.0083 304 PHE B CG  
6417  C CD1 . PHE B 81  ? 0.0983 0.0861 0.1055 0.0082  -0.0168 0.0004  304 PHE B CD1 
6418  C CD2 . PHE B 81  ? 0.1313 0.1037 0.1093 -0.0094 -0.0087 -0.0066 304 PHE B CD2 
6419  C CE1 . PHE B 81  ? 0.1009 0.0997 0.1164 0.0127  -0.0192 -0.0025 304 PHE B CE1 
6420  C CE2 . PHE B 81  ? 0.1533 0.1254 0.1004 -0.0019 -0.0026 0.0068  304 PHE B CE2 
6421  C CZ  . PHE B 81  ? 0.1215 0.1167 0.1064 0.0004  0.0101  0.0056  304 PHE B CZ  
6431  N N   . ASN B 82  ? 0.0848 0.0690 0.1129 0.0099  -0.0135 -0.0196 305 ASN B N   
6432  C CA  . ASN B 82  ? 0.0944 0.0847 0.1251 0.0112  -0.0240 -0.0183 305 ASN B CA  
6433  C C   . ASN B 82  ? 0.0967 0.0857 0.1392 0.0154  -0.0044 0.0011  305 ASN B C   
6434  O O   . ASN B 82  ? 0.1232 0.1139 0.1412 0.0391  -0.0009 0.0288  305 ASN B O   
6435  C CB  . ASN B 82  ? 0.1035 0.1167 0.1660 0.0204  -0.0416 -0.0334 305 ASN B CB  
6436  C CG  . ASN B 82  ? 0.1527 0.1507 0.2132 -0.0091 -0.0021 -0.0621 305 ASN B CG  
6437  O OD1 . ASN B 82  ? 0.1904 0.1978 0.2135 -0.0193 0.0270  -0.0476 305 ASN B OD1 
6438  N ND2 . ASN B 82  ? 0.2185 0.1612 0.2772 -0.0016 0.0738  -0.0495 305 ASN B ND2 
6445  N N   . ILE B 83  ? 0.0685 0.0745 0.1159 0.0131  -0.0288 -0.0176 306 ILE B N   
6446  C CA  . ILE B 83  ? 0.0831 0.0781 0.1180 0.0043  -0.0142 -0.0082 306 ILE B CA  
6447  C C   . ILE B 83  ? 0.0970 0.0816 0.1222 0.0080  -0.0412 -0.0051 306 ILE B C   
6448  O O   . ILE B 83  ? 0.1082 0.1083 0.1395 -0.0145 -0.0485 0.0040  306 ILE B O   
6449  C CB  . ILE B 83  ? 0.0671 0.0820 0.1265 0.0092  -0.0163 -0.0002 306 ILE B CB  
6450  C CG1 . ILE B 83  ? 0.0906 0.0871 0.1239 0.0090  -0.0103 -0.0043 306 ILE B CG1 
6451  C CG2 . ILE B 83  ? 0.0880 0.0901 0.1277 0.0109  -0.0220 -0.0097 306 ILE B CG2 
6452  C CD1 . ILE B 83  ? 0.0962 0.0881 0.1241 0.0118  -0.0106 0.0080  306 ILE B CD1 
6464  N N   . THR B 84  ? 0.0880 0.0972 0.1142 0.0025  -0.0427 -0.0186 307 THR B N   
6465  C CA  . THR B 84  ? 0.0860 0.1151 0.1121 0.0034  -0.0244 -0.0183 307 THR B CA  
6466  C C   . THR B 84  ? 0.0900 0.1629 0.1301 0.0100  -0.0389 -0.0470 307 THR B C   
6467  O O   . THR B 84  ? 0.0967 0.2041 0.1750 0.0003  -0.0336 -0.0901 307 THR B O   
6468  C CB  . THR B 84  ? 0.0842 0.1183 0.1364 -0.0155 -0.0230 -0.0070 307 THR B CB  
6469  O OG1 . THR B 84  ? 0.1087 0.1360 0.1451 -0.0049 -0.0116 0.0207  307 THR B OG1 
6470  C CG2 . THR B 84  ? 0.1049 0.1342 0.1530 0.0000  -0.0087 -0.0052 307 THR B CG2 
6478  N N   A ASN B 85  ? 0.0931 0.1806 0.1273 0.0179  -0.0311 -0.0187 308 ASN B N   
6479  N N   B ASN B 85  ? 0.1010 0.1775 0.1311 0.0157  -0.0307 -0.0224 308 ASN B N   
6480  C CA  A ASN B 85  ? 0.1129 0.1785 0.1412 0.0128  -0.0374 -0.0114 308 ASN B CA  
6481  C CA  B ASN B 85  ? 0.1053 0.1642 0.1242 0.0259  -0.0385 0.0062  308 ASN B CA  
6482  C C   A ASN B 85  ? 0.1464 0.1523 0.1281 0.0106  -0.0169 0.0066  308 ASN B C   
6483  C C   B ASN B 85  ? 0.1188 0.1373 0.1143 0.0234  -0.0449 0.0175  308 ASN B C   
6484  O O   A ASN B 85  ? 0.1580 0.1350 0.1369 0.0156  -0.0110 0.0146  308 ASN B O   
6485  O O   B ASN B 85  ? 0.1359 0.1449 0.1327 0.0084  -0.0176 0.0228  308 ASN B O   
6486  C CB  A ASN B 85  ? 0.1050 0.1837 0.1597 0.0026  -0.0317 -0.0130 308 ASN B CB  
6487  C CB  B ASN B 85  ? 0.0930 0.1724 0.1352 0.0313  -0.0285 0.0010  308 ASN B CB  
6488  C CG  A ASN B 85  ? 0.1013 0.1761 0.1703 -0.0079 -0.0303 -0.0112 308 ASN B CG  
6489  C CG  B ASN B 85  ? 0.0798 0.1703 0.1473 0.0273  -0.0327 -0.0016 308 ASN B CG  
6490  O OD1 A ASN B 85  ? 0.0941 0.1690 0.1685 0.0017  -0.0457 -0.0291 308 ASN B OD1 
6491  O OD1 B ASN B 85  ? 0.0781 0.1644 0.1429 0.0314  -0.0479 -0.0079 308 ASN B OD1 
6492  N ND2 A ASN B 85  ? 0.0953 0.1621 0.1912 -0.0065 -0.0231 0.0018  308 ASN B ND2 
6493  N ND2 B ASN B 85  ? 0.0667 0.1647 0.1637 0.0266  -0.0278 -0.0010 308 ASN B ND2 
6506  N N   A PRO B 86  ? 0.1670 0.1497 0.1220 0.0111  -0.0107 0.0103  309 PRO B N   
6507  N N   B PRO B 86  ? 0.1382 0.1164 0.1230 0.0132  -0.0378 0.0201  309 PRO B N   
6508  C CA  A PRO B 86  ? 0.1750 0.1559 0.1340 0.0141  -0.0147 0.0108  309 PRO B CA  
6509  C CA  B PRO B 86  ? 0.1546 0.1057 0.1283 0.0131  -0.0323 0.0250  309 PRO B CA  
6510  C C   A PRO B 86  ? 0.1683 0.1598 0.1554 0.0088  -0.0115 0.0336  309 PRO B C   
6511  C C   B PRO B 86  ? 0.1709 0.1072 0.1406 0.0128  -0.0352 0.0283  309 PRO B C   
6512  O O   A PRO B 86  ? 0.1749 0.1600 0.1605 0.0289  -0.0069 0.0458  309 PRO B O   
6513  O O   B PRO B 86  ? 0.1803 0.1174 0.1512 0.0096  -0.0316 0.0470  309 PRO B O   
6514  C CB  A PRO B 86  ? 0.2010 0.1618 0.1377 0.0198  -0.0065 0.0019  309 PRO B CB  
6515  C CB  B PRO B 86  ? 0.1508 0.0991 0.1328 0.0094  -0.0376 0.0245  309 PRO B CB  
6516  C CG  A PRO B 86  ? 0.2063 0.1499 0.1127 0.0008  -0.0120 -0.0113 309 PRO B CG  
6517  C CG  B PRO B 86  ? 0.1607 0.1041 0.1365 0.0100  -0.0338 0.0287  309 PRO B CG  
6518  C CD  A PRO B 86  ? 0.1845 0.1439 0.1176 0.0071  0.0016  -0.0128 309 PRO B CD  
6519  C CD  B PRO B 86  ? 0.1575 0.1123 0.1303 0.0178  -0.0268 0.0175  309 PRO B CD  
6534  N N   A ASN B 87  ? 0.1562 0.1556 0.1640 0.0039  -0.0188 0.0467  310 ASN B N   
6535  N N   B ASN B 87  ? 0.1750 0.0993 0.1424 0.0066  -0.0407 0.0069  310 ASN B N   
6536  C CA  A ASN B 87  ? 0.1578 0.1767 0.2005 -0.0131 -0.0072 0.0465  310 ASN B CA  
6537  C CA  B ASN B 87  ? 0.1941 0.1042 0.1659 0.0077  -0.0234 -0.0010 310 ASN B CA  
6538  C C   A ASN B 87  ? 0.1787 0.1548 0.2058 -0.0218 -0.0054 0.0446  310 ASN B C   
6539  C C   B ASN B 87  ? 0.1996 0.1086 0.1827 0.0128  -0.0123 -0.0050 310 ASN B C   
6540  O O   A ASN B 87  ? 0.2120 0.1469 0.2225 -0.0216 0.0133  0.0561  310 ASN B O   
6541  O O   B ASN B 87  ? 0.2093 0.1140 0.2084 0.0055  0.0062  -0.0068 310 ASN B O   
6542  C CB  A ASN B 87  ? 0.1515 0.2189 0.2291 -0.0390 0.0049  0.0363  310 ASN B CB  
6543  C CB  B ASN B 87  ? 0.2061 0.1123 0.1724 0.0046  -0.0117 -0.0101 310 ASN B CB  
6544  C CG  A ASN B 87  ? 0.1354 0.2477 0.2298 -0.0530 0.0005  0.0491  310 ASN B CG  
6545  C CG  B ASN B 87  ? 0.2151 0.1107 0.1737 0.0056  -0.0196 -0.0233 310 ASN B CG  
6546  O OD1 A ASN B 87  ? 0.1421 0.2413 0.2070 -0.0392 -0.0122 0.0496  310 ASN B OD1 
6547  O OD1 B ASN B 87  ? 0.2099 0.1226 0.1671 0.0021  -0.0266 -0.0311 310 ASN B OD1 
6548  N ND2 A ASN B 87  ? 0.1703 0.2796 0.2663 -0.0519 0.0166  0.0518  310 ASN B ND2 
6549  N ND2 B ASN B 87  ? 0.2347 0.1129 0.1865 0.0093  -0.0138 -0.0237 310 ASN B ND2 
6562  N N   A GLY B 88  ? 0.1740 0.1513 0.2118 -0.0057 -0.0002 0.0486  311 GLY B N   
6563  N N   B GLY B 88  ? 0.2083 0.1153 0.1821 0.0201  -0.0173 -0.0107 311 GLY B N   
6564  C CA  A GLY B 88  ? 0.1615 0.1543 0.2293 -0.0030 -0.0122 0.0418  311 GLY B CA  
6565  C CA  B GLY B 88  ? 0.2208 0.1256 0.1802 0.0284  -0.0157 -0.0081 311 GLY B CA  
6566  C C   A GLY B 88  ? 0.1451 0.1615 0.2477 -0.0128 -0.0231 0.0204  311 GLY B C   
6567  C C   B GLY B 88  ? 0.2306 0.1360 0.1825 0.0347  -0.0164 -0.0053 311 GLY B C   
6568  O O   A GLY B 88  ? 0.1679 0.1653 0.2673 0.0076  -0.0074 0.0036  311 GLY B O   
6569  O O   B GLY B 88  ? 0.2288 0.1417 0.1760 0.0360  -0.0335 -0.0046 311 GLY B O   
6576  N N   A THR B 89  ? 0.1484 0.1666 0.2867 -0.0241 -0.0023 0.0343  312 THR B N   
6577  C CA  A THR B 89  ? 0.1478 0.1551 0.2936 -0.0443 -0.0015 0.0083  312 THR B CA  
6578  C C   A THR B 89  ? 0.1262 0.1369 0.2687 -0.0241 -0.0236 -0.0004 312 THR B C   
6579  O O   A THR B 89  ? 0.1131 0.1135 0.2413 -0.0225 -0.0320 0.0142  312 THR B O   
6580  C CB  A THR B 89  ? 0.1670 0.1700 0.3323 -0.0445 0.0243  0.0187  312 THR B CB  
6581  O OG1 A THR B 89  ? 0.1089 0.1800 0.3156 -0.0216 -0.0194 0.0442  312 THR B OG1 
6582  C CG2 A THR B 89  ? 0.2039 0.1771 0.3449 -0.0390 0.0385  0.0281  312 THR B CG2 
6590  N N   . PRO B 90  ? 0.1491 0.1565 0.2745 -0.0290 -0.0256 -0.0527 313 PRO B N   
6591  C CA  . PRO B 90  ? 0.1377 0.1695 0.2397 -0.0225 -0.0406 -0.0693 313 PRO B CA  
6592  C C   . PRO B 90  ? 0.1496 0.1671 0.2128 -0.0221 -0.0393 -0.0419 313 PRO B C   
6593  O O   . PRO B 90  ? 0.1552 0.1648 0.2252 -0.0083 -0.0243 -0.0443 313 PRO B O   
6594  C CB  . PRO B 90  ? 0.1608 0.1889 0.2735 -0.0197 -0.0352 -0.0762 313 PRO B CB  
6595  C CG  . PRO B 90  ? 0.1848 0.1909 0.2888 -0.0239 -0.0198 -0.0767 313 PRO B CG  
6596  C CD  . PRO B 90  ? 0.1755 0.1775 0.2905 -0.0228 -0.0118 -0.0671 313 PRO B CD  
6604  N N   . PHE B 91  ? 0.1551 0.1635 0.1817 -0.0200 -0.0544 -0.0154 314 PHE B N   
6605  C CA  . PHE B 91  ? 0.1692 0.1636 0.1975 -0.0373 -0.0711 0.0028  314 PHE B CA  
6606  C C   . PHE B 91  ? 0.2061 0.1699 0.2184 -0.0311 -0.0981 0.0067  314 PHE B C   
6607  O O   . PHE B 91  ? 0.2311 0.2094 0.2104 -0.0336 -0.0982 0.0044  314 PHE B O   
6608  C CB  . PHE B 91  ? 0.1716 0.1639 0.1990 -0.0509 -0.0570 -0.0068 314 PHE B CB  
6609  C CG  . PHE B 91  ? 0.1841 0.1585 0.1871 -0.0557 -0.0729 0.0016  314 PHE B CG  
6610  C CD1 . PHE B 91  ? 0.1726 0.1620 0.2099 -0.0474 -0.0717 0.0216  314 PHE B CD1 
6611  C CD2 . PHE B 91  ? 0.1871 0.1523 0.1806 -0.0660 -0.0798 -0.0051 314 PHE B CD2 
6612  C CE1 . PHE B 91  ? 0.1682 0.1591 0.2179 -0.0595 -0.0736 0.0212  314 PHE B CE1 
6613  C CE2 . PHE B 91  ? 0.1913 0.1672 0.1993 -0.0706 -0.0779 0.0049  314 PHE B CE2 
6614  C CZ  . PHE B 91  ? 0.1814 0.1663 0.2069 -0.0601 -0.0724 0.0170  314 PHE B CZ  
6624  N N   . ASP B 92  ? 0.2320 0.1524 0.2590 -0.0146 -0.1460 0.0206  315 ASP B N   
6625  C CA  . ASP B 92  ? 0.2837 0.1636 0.3010 -0.0300 -0.1662 0.0048  315 ASP B CA  
6626  C C   . ASP B 92  ? 0.3199 0.1827 0.3119 -0.0315 -0.1824 0.0009  315 ASP B C   
6627  O O   . ASP B 92  ? 0.3224 0.1878 0.3318 -0.0189 -0.1854 0.0072  315 ASP B O   
6628  C CB  . ASP B 92  ? 0.2921 0.1590 0.3343 -0.0332 -0.1730 0.0009  315 ASP B CB  
6629  C CG  . ASP B 92  ? 0.3049 0.1842 0.3911 -0.0318 -0.1831 -0.0099 315 ASP B CG  
6630  O OD1 . ASP B 92  ? 0.3061 0.1935 0.3676 -0.0161 -0.1958 -0.0071 315 ASP B OD1 
6631  O OD2 . ASP B 92  ? 0.3256 0.2072 0.4391 -0.0337 -0.1568 -0.0004 315 ASP B OD2 
6636  N N   . PRO B 93  ? 0.3470 0.1830 0.3241 -0.0565 -0.1786 0.0042  316 PRO B N   
6637  C CA  . PRO B 93  ? 0.3555 0.1914 0.3141 -0.0506 -0.1848 0.0034  316 PRO B CA  
6638  C C   . PRO B 93  ? 0.3758 0.1985 0.3102 -0.0475 -0.1807 0.0080  316 PRO B C   
6639  O O   . PRO B 93  ? 0.4108 0.1955 0.3070 -0.0356 -0.1413 0.0065  316 PRO B O   
6640  C CB  . PRO B 93  ? 0.3590 0.1965 0.3351 -0.0563 -0.1814 0.0089  316 PRO B CB  
6641  C CG  . PRO B 93  ? 0.3714 0.2018 0.3436 -0.0376 -0.1511 0.0311  316 PRO B CG  
6642  C CD  . PRO B 93  ? 0.3681 0.1911 0.3417 -0.0417 -0.1481 0.0313  316 PRO B CD  
6650  N N   . THR B 94  ? 0.3635 0.2086 0.3242 -0.0510 -0.1900 0.0001  317 THR B N   
6651  C CA  . THR B 94  ? 0.3647 0.2297 0.3606 -0.0419 -0.1633 -0.0070 317 THR B CA  
6652  C C   . THR B 94  ? 0.3591 0.2395 0.3790 -0.0529 -0.1419 -0.0078 317 THR B C   
6653  O O   . THR B 94  ? 0.3580 0.2443 0.3925 -0.0558 -0.1449 -0.0041 317 THR B O   
6654  C CB  . THR B 94  ? 0.3610 0.2458 0.3760 -0.0311 -0.1739 -0.0276 317 THR B CB  
6655  O OG1 . THR B 94  ? 0.3512 0.2336 0.3879 -0.0354 -0.1863 -0.0412 317 THR B OG1 
6656  C CG2 . THR B 94  ? 0.3616 0.2670 0.3765 -0.0234 -0.1784 -0.0392 317 THR B CG2 
6664  N N   . GLU B 95  ? 0.3491 0.2410 0.3662 -0.0712 -0.1308 -0.0212 318 GLU B N   
6665  C CA  . GLU B 95  ? 0.3484 0.2631 0.3869 -0.0709 -0.0807 -0.0218 318 GLU B CA  
6666  C C   . GLU B 95  ? 0.2821 0.2458 0.3486 -0.0732 -0.0921 -0.0299 318 GLU B C   
6667  O O   . GLU B 95  ? 0.2790 0.2379 0.3310 -0.0744 -0.0704 -0.0186 318 GLU B O   
6668  C CB  . GLU B 95  ? 0.4038 0.3005 0.4382 -0.0751 -0.0205 -0.0214 318 GLU B CB  
6669  C CG  . GLU B 95  ? 0.4503 0.3410 0.4884 -0.0731 0.0319  -0.0221 318 GLU B CG  
6670  C CD  . GLU B 95  ? 0.4841 0.3766 0.5202 -0.0799 0.0579  -0.0357 318 GLU B CD  
6671  O OE1 . GLU B 95  ? 0.5074 0.3931 0.5394 -0.0766 0.0713  -0.0347 318 GLU B OE1 
6672  O OE2 . GLU B 95  ? 0.5017 0.3978 0.5337 -0.0754 0.0660  -0.0379 318 GLU B OE2 
6679  N N   . ASP B 96  ? 0.2386 0.2448 0.3522 -0.0584 -0.0872 -0.0241 319 ASP B N   
6680  C CA  . ASP B 96  ? 0.1911 0.2431 0.3454 -0.0295 -0.0757 -0.0115 319 ASP B CA  
6681  C C   . ASP B 96  ? 0.1563 0.2105 0.3124 -0.0198 -0.0519 -0.0072 319 ASP B C   
6682  O O   . ASP B 96  ? 0.1428 0.2305 0.3460 -0.0214 -0.0395 -0.0120 319 ASP B O   
6683  C CB  . ASP B 96  ? 0.1960 0.2750 0.3675 -0.0161 -0.0763 -0.0004 319 ASP B CB  
6684  C CG  . ASP B 96  ? 0.2150 0.2983 0.3809 -0.0123 -0.0709 0.0071  319 ASP B CG  
6685  O OD1 . ASP B 96  ? 0.2281 0.3024 0.3783 -0.0081 -0.0794 0.0125  319 ASP B OD1 
6686  O OD2 . ASP B 96  ? 0.2398 0.3192 0.4053 -0.0102 -0.0372 0.0106  319 ASP B OD2 
6691  N N   . VAL B 97  ? 0.1434 0.1714 0.2746 -0.0117 -0.0294 -0.0028 320 VAL B N   
6692  C CA  . VAL B 97  ? 0.1280 0.1481 0.2445 -0.0054 -0.0346 0.0201  320 VAL B CA  
6693  C C   . VAL B 97  ? 0.1067 0.1332 0.1673 0.0063  -0.0368 0.0050  320 VAL B C   
6694  O O   . VAL B 97  ? 0.1283 0.1564 0.1426 -0.0009 -0.0514 0.0010  320 VAL B O   
6695  C CB  . VAL B 97  ? 0.2029 0.1780 0.3095 -0.0143 0.0423  0.0448  320 VAL B CB  
6696  C CG1 . VAL B 97  ? 0.2194 0.1887 0.3256 -0.0035 0.0512  0.0512  320 VAL B CG1 
6697  C CG2 . VAL B 97  ? 0.2244 0.1899 0.3138 -0.0157 0.0469  0.0544  320 VAL B CG2 
6707  N N   . PRO B 98  ? 0.0983 0.1134 0.1186 0.0126  -0.0228 0.0129  321 PRO B N   
6708  C CA  . PRO B 98  ? 0.1115 0.0988 0.1072 0.0118  0.0088  0.0149  321 PRO B CA  
6709  C C   . PRO B 98  ? 0.1260 0.0938 0.0809 0.0064  -0.0087 0.0078  321 PRO B C   
6710  O O   . PRO B 98  ? 0.1281 0.0963 0.0861 0.0127  -0.0107 0.0103  321 PRO B O   
6711  C CB  . PRO B 98  ? 0.1208 0.0906 0.0957 0.0197  0.0045  -0.0022 321 PRO B CB  
6712  C CG  . PRO B 98  ? 0.1294 0.1024 0.0973 0.0275  -0.0062 0.0256  321 PRO B CG  
6713  C CD  . PRO B 98  ? 0.1331 0.1128 0.1037 0.0230  -0.0045 0.0154  321 PRO B CD  
6721  N N   . ALA B 99  ? 0.1081 0.0903 0.0862 -0.0092 -0.0112 0.0142  322 ALA B N   
6722  C CA  . ALA B 99  ? 0.1079 0.0983 0.0765 -0.0013 -0.0089 0.0076  322 ALA B CA  
6723  C C   . ALA B 99  ? 0.1001 0.0934 0.0816 -0.0047 -0.0110 0.0000  322 ALA B C   
6724  O O   . ALA B 99  ? 0.0864 0.0833 0.1012 -0.0006 -0.0128 0.0067  322 ALA B O   
6725  C CB  . ALA B 99  ? 0.1202 0.1074 0.0755 -0.0166 -0.0075 -0.0016 322 ALA B CB  
6731  N N   . PRO B 100 ? 0.0910 0.0852 0.0894 0.0023  -0.0149 -0.0128 323 PRO B N   
6732  C CA  . PRO B 100 ? 0.0921 0.0706 0.1000 0.0015  -0.0261 0.0047  323 PRO B CA  
6733  C C   . PRO B 100 ? 0.0691 0.0639 0.1000 -0.0076 -0.0196 0.0069  323 PRO B C   
6734  O O   . PRO B 100 ? 0.0833 0.0775 0.0884 -0.0158 0.0021  -0.0072 323 PRO B O   
6735  C CB  . PRO B 100 ? 0.1073 0.0809 0.1042 0.0083  -0.0122 0.0048  323 PRO B CB  
6736  C CG  . PRO B 100 ? 0.0957 0.0852 0.1071 -0.0036 -0.0051 -0.0091 323 PRO B CG  
6737  C CD  . PRO B 100 ? 0.0985 0.0868 0.1010 0.0071  -0.0059 -0.0045 323 PRO B CD  
6745  N N   . LEU B 101 ? 0.0735 0.0653 0.0982 -0.0245 -0.0264 -0.0118 324 LEU B N   
6746  C CA  . LEU B 101 ? 0.0624 0.0726 0.0979 -0.0152 -0.0147 -0.0026 324 LEU B CA  
6747  C C   . LEU B 101 ? 0.0693 0.0793 0.1040 0.0045  -0.0117 0.0036  324 LEU B C   
6748  O O   . LEU B 101 ? 0.0863 0.0832 0.1185 0.0094  -0.0317 -0.0101 324 LEU B O   
6749  C CB  . LEU B 101 ? 0.0866 0.0968 0.1018 -0.0246 -0.0175 0.0014  324 LEU B CB  
6750  C CG  . LEU B 101 ? 0.0892 0.1009 0.0956 -0.0276 -0.0322 -0.0032 324 LEU B CG  
6751  C CD1 . LEU B 101 ? 0.0915 0.1034 0.1188 -0.0077 -0.0131 -0.0078 324 LEU B CD1 
6752  C CD2 . LEU B 101 ? 0.0948 0.1069 0.1134 -0.0313 -0.0263 0.0101  324 LEU B CD2 
6764  N N   . GLY B 102 ? 0.0725 0.0709 0.0721 -0.0023 -0.0140 -0.0074 325 GLY B N   
6765  C CA  . GLY B 102 ? 0.0720 0.0748 0.0749 0.0010  -0.0192 0.0019  325 GLY B CA  
6766  C C   . GLY B 102 ? 0.0661 0.0713 0.0811 0.0040  -0.0235 0.0021  325 GLY B C   
6767  O O   . GLY B 102 ? 0.0603 0.0900 0.0821 -0.0011 -0.0164 0.0056  325 GLY B O   
6771  N N   . THR B 103 ? 0.0721 0.0597 0.0791 0.0027  -0.0107 -0.0115 326 THR B N   
6772  C CA  . THR B 103 ? 0.0812 0.0735 0.0781 -0.0064 -0.0071 -0.0078 326 THR B CA  
6773  C C   . THR B 103 ? 0.0608 0.0659 0.0834 0.0015  -0.0230 0.0011  326 THR B C   
6774  O O   . THR B 103 ? 0.0593 0.0711 0.0852 0.0068  -0.0104 0.0073  326 THR B O   
6775  C CB  . THR B 103 ? 0.0776 0.0769 0.0983 -0.0125 -0.0120 -0.0134 326 THR B CB  
6776  O OG1 . THR B 103 ? 0.1021 0.0801 0.0967 -0.0227 -0.0031 -0.0169 326 THR B OG1 
6777  C CG2 . THR B 103 ? 0.0854 0.0817 0.0957 -0.0102 0.0005  -0.0255 326 THR B CG2 
6785  N N   . PRO B 104 ? 0.0632 0.0649 0.0942 0.0133  -0.0039 -0.0043 327 PRO B N   
6786  C CA  A PRO B 104 ? 0.0643 0.0677 0.0869 0.0101  -0.0115 -0.0014 327 PRO B CA  
6787  C CA  B PRO B 104 ? 0.0700 0.0693 0.0819 0.0099  -0.0065 -0.0012 327 PRO B CA  
6788  C C   . PRO B 104 ? 0.0753 0.0672 0.0722 -0.0050 -0.0039 -0.0103 327 PRO B C   
6789  O O   . PRO B 104 ? 0.0937 0.0647 0.0771 0.0049  -0.0015 -0.0052 327 PRO B O   
6790  C CB  A PRO B 104 ? 0.0683 0.0774 0.0934 0.0146  -0.0132 0.0033  327 PRO B CB  
6791  C CB  B PRO B 104 ? 0.0814 0.0809 0.0772 0.0152  -0.0022 0.0051  327 PRO B CB  
6792  C CG  A PRO B 104 ? 0.0647 0.0741 0.1011 0.0152  -0.0228 -0.0023 327 PRO B CG  
6793  C CG  B PRO B 104 ? 0.0872 0.0815 0.0800 0.0111  -0.0035 0.0011  327 PRO B CG  
6794  C CD  A PRO B 104 ? 0.0712 0.0740 0.1041 0.0198  -0.0010 -0.0040 327 PRO B CD  
6795  C CD  B PRO B 104 ? 0.0798 0.0772 0.0921 0.0144  0.0056  -0.0045 327 PRO B CD  
6810  N N   . ASP B 105 ? 0.0718 0.0583 0.0784 0.0077  -0.0065 -0.0066 328 ASP B N   
6811  C CA  . ASP B 105 ? 0.0719 0.0608 0.0859 0.0171  -0.0099 -0.0121 328 ASP B CA  
6812  C C   . ASP B 105 ? 0.0655 0.0671 0.0915 0.0135  -0.0255 -0.0031 328 ASP B C   
6813  O O   . ASP B 105 ? 0.0659 0.0679 0.1196 0.0131  0.0001  0.0019  328 ASP B O   
6814  C CB  . ASP B 105 ? 0.0587 0.0520 0.0773 0.0053  -0.0121 -0.0084 328 ASP B CB  
6815  C CG  . ASP B 105 ? 0.0586 0.0608 0.0962 0.0093  -0.0020 -0.0001 328 ASP B CG  
6816  O OD1 . ASP B 105 ? 0.0607 0.0744 0.0947 0.0081  -0.0146 0.0020  328 ASP B OD1 
6817  O OD2 . ASP B 105 ? 0.0655 0.0773 0.0911 0.0046  -0.0049 -0.0008 328 ASP B OD2 
6822  N N   . PHE B 106 ? 0.0565 0.0646 0.0910 0.0086  -0.0093 -0.0002 329 PHE B N   
6823  C CA  . PHE B 106 ? 0.0614 0.0632 0.0908 0.0143  -0.0104 0.0017  329 PHE B CA  
6824  C C   . PHE B 106 ? 0.0614 0.0655 0.0959 0.0049  -0.0051 -0.0018 329 PHE B C   
6825  O O   . PHE B 106 ? 0.0859 0.0575 0.1064 0.0030  0.0210  -0.0106 329 PHE B O   
6826  C CB  . PHE B 106 ? 0.0693 0.0649 0.1029 0.0068  -0.0102 -0.0034 329 PHE B CB  
6827  C CG  . PHE B 106 ? 0.0682 0.0790 0.0852 0.0036  -0.0148 -0.0063 329 PHE B CG  
6828  C CD1 . PHE B 106 ? 0.0842 0.0934 0.1101 0.0047  -0.0213 -0.0032 329 PHE B CD1 
6829  C CD2 . PHE B 106 ? 0.0661 0.0734 0.0893 -0.0016 -0.0041 0.0033  329 PHE B CD2 
6830  C CE1 . PHE B 106 ? 0.0988 0.1055 0.1339 0.0036  -0.0170 -0.0049 329 PHE B CE1 
6831  C CE2 . PHE B 106 ? 0.0849 0.0847 0.0987 0.0009  -0.0077 0.0063  329 PHE B CE2 
6832  C CZ  . PHE B 106 ? 0.0842 0.0833 0.1332 0.0158  -0.0368 -0.0005 329 PHE B CZ  
6842  N N   . ARG B 107 ? 0.0729 0.0680 0.0990 0.0125  0.0041  0.0036  330 ARG B N   
6843  C CA  . ARG B 107 ? 0.0708 0.0641 0.1001 0.0177  -0.0076 0.0017  330 ARG B CA  
6844  C C   . ARG B 107 ? 0.0679 0.0739 0.0901 -0.0029 -0.0168 -0.0109 330 ARG B C   
6845  O O   . ARG B 107 ? 0.0788 0.0809 0.1352 0.0164  -0.0283 -0.0206 330 ARG B O   
6846  C CB  . ARG B 107 ? 0.0982 0.0756 0.1279 0.0045  0.0018  0.0015  330 ARG B CB  
6847  C CG  . ARG B 107 ? 0.1238 0.0789 0.1457 0.0206  -0.0124 0.0106  330 ARG B CG  
6848  C CD  . ARG B 107 ? 0.1673 0.1133 0.2010 0.0244  0.0054  0.0496  330 ARG B CD  
6849  N NE  . ARG B 107 ? 0.2336 0.1446 0.2511 0.0663  0.0658  0.0582  330 ARG B NE  
6850  C CZ  . ARG B 107 ? 0.2600 0.1360 0.2830 0.0539  0.0567  0.0504  330 ARG B CZ  
6851  N NH1 . ARG B 107 ? 0.2679 0.1266 0.2761 0.0389  0.0130  0.0637  330 ARG B NH1 
6852  N NH2 . ARG B 107 ? 0.2643 0.1308 0.3014 0.0616  0.0663  0.0376  330 ARG B NH2 
6866  N N   . GLY B 108 ? 0.0591 0.0735 0.0987 0.0135  -0.0247 -0.0171 331 GLY B N   
6867  C CA  . GLY B 108 ? 0.0689 0.0782 0.1175 0.0199  -0.0071 -0.0164 331 GLY B CA  
6868  C C   . GLY B 108 ? 0.0534 0.0692 0.1069 0.0003  -0.0086 -0.0131 331 GLY B C   
6869  O O   . GLY B 108 ? 0.0755 0.0891 0.1030 0.0162  -0.0216 -0.0197 331 GLY B O   
6873  N N   . GLN B 109 ? 0.0570 0.0636 0.0959 -0.0008 -0.0223 -0.0044 332 GLN B N   
6874  C CA  . GLN B 109 ? 0.0628 0.0730 0.0950 0.0307  -0.0031 0.0055  332 GLN B CA  
6875  C C   . GLN B 109 ? 0.0587 0.0667 0.0917 0.0154  -0.0222 0.0130  332 GLN B C   
6876  O O   . GLN B 109 ? 0.0721 0.0784 0.0860 -0.0074 -0.0233 -0.0004 332 GLN B O   
6877  C CB  . GLN B 109 ? 0.0804 0.0741 0.1141 0.0047  -0.0115 0.0073  332 GLN B CB  
6878  C CG  . GLN B 109 ? 0.0905 0.0867 0.1374 0.0000  -0.0200 0.0181  332 GLN B CG  
6879  C CD  . GLN B 109 ? 0.1546 0.1099 0.1326 0.0032  -0.0224 0.0137  332 GLN B CD  
6880  O OE1 . GLN B 109 ? 0.1922 0.1338 0.1273 0.0381  -0.0179 -0.0003 332 GLN B OE1 
6881  N NE2 . GLN B 109 ? 0.2030 0.1396 0.1698 0.0089  -0.0143 -0.0160 332 GLN B NE2 
6890  N N   . LEU B 110 ? 0.0748 0.0635 0.0741 -0.0076 -0.0196 0.0143  333 LEU B N   
6891  C CA  . LEU B 110 ? 0.0570 0.0577 0.0708 -0.0002 -0.0186 -0.0040 333 LEU B CA  
6892  C C   . LEU B 110 ? 0.0767 0.0571 0.0626 0.0006  -0.0114 0.0010  333 LEU B C   
6893  O O   . LEU B 110 ? 0.0849 0.0782 0.0855 0.0317  -0.0127 -0.0027 333 LEU B O   
6894  C CB  . LEU B 110 ? 0.0687 0.0627 0.0997 0.0062  0.0044  0.0028  333 LEU B CB  
6895  C CG  . LEU B 110 ? 0.0788 0.0719 0.0926 0.0012  0.0018  0.0086  333 LEU B CG  
6896  C CD1 . LEU B 110 ? 0.0813 0.1015 0.0934 0.0154  -0.0073 0.0027  333 LEU B CD1 
6897  C CD2 . LEU B 110 ? 0.0689 0.1028 0.1054 -0.0020 0.0020  0.0104  333 LEU B CD2 
6909  N N   . TYR B 111 ? 0.0804 0.0449 0.0683 0.0153  -0.0054 -0.0038 334 TYR B N   
6910  C CA  . TYR B 111 ? 0.0585 0.0485 0.0844 0.0062  -0.0086 0.0064  334 TYR B CA  
6911  C C   . TYR B 111 ? 0.0532 0.0467 0.0722 -0.0093 -0.0111 -0.0005 334 TYR B C   
6912  O O   . TYR B 111 ? 0.0652 0.0499 0.0769 -0.0011 0.0041  0.0039  334 TYR B O   
6913  C CB  . TYR B 111 ? 0.0658 0.0557 0.1082 -0.0061 -0.0024 0.0036  334 TYR B CB  
6914  C CG  . TYR B 111 ? 0.0609 0.0506 0.1129 -0.0049 -0.0088 -0.0010 334 TYR B CG  
6915  C CD1 . TYR B 111 ? 0.0691 0.0465 0.0977 -0.0043 -0.0101 0.0018  334 TYR B CD1 
6916  C CD2 . TYR B 111 ? 0.0637 0.0629 0.1001 0.0057  -0.0149 0.0019  334 TYR B CD2 
6917  C CE1 . TYR B 111 ? 0.0684 0.0538 0.1162 0.0040  -0.0075 -0.0059 334 TYR B CE1 
6918  C CE2 . TYR B 111 ? 0.0608 0.0760 0.0965 -0.0037 -0.0066 -0.0196 334 TYR B CE2 
6919  C CZ  . TYR B 111 ? 0.0442 0.0695 0.1157 -0.0024 -0.0172 0.0012  334 TYR B CZ  
6920  O OH  . TYR B 111 ? 0.0643 0.0748 0.1164 0.0030  -0.0149 0.0044  334 TYR B OH  
6930  N N   . GLY B 112 ? 0.0644 0.0408 0.0734 0.0005  -0.0024 0.0114  335 GLY B N   
6931  C CA  . GLY B 112 ? 0.0690 0.0566 0.0837 -0.0003 0.0033  -0.0001 335 GLY B CA  
6932  C C   . GLY B 112 ? 0.0558 0.0494 0.0824 -0.0079 -0.0023 -0.0057 335 GLY B C   
6933  O O   . GLY B 112 ? 0.0563 0.0539 0.0900 0.0047  0.0051  0.0062  335 GLY B O   
6937  N N   . VAL B 113 ? 0.0590 0.0495 0.0909 0.0075  0.0049  -0.0039 336 VAL B N   
6938  C CA  . VAL B 113 ? 0.0461 0.0528 0.0959 0.0074  -0.0033 -0.0062 336 VAL B CA  
6939  C C   . VAL B 113 ? 0.0626 0.0433 0.0856 -0.0024 0.0091  0.0049  336 VAL B C   
6940  O O   . VAL B 113 ? 0.0548 0.0571 0.1049 -0.0059 0.0070  -0.0048 336 VAL B O   
6941  C CB  . VAL B 113 ? 0.0779 0.0659 0.0881 -0.0004 -0.0113 0.0019  336 VAL B CB  
6942  C CG1 . VAL B 113 ? 0.0916 0.0732 0.0962 0.0073  -0.0154 0.0172  336 VAL B CG1 
6943  C CG2 . VAL B 113 ? 0.1363 0.0806 0.1070 -0.0098 -0.0177 0.0094  336 VAL B CG2 
6953  N N   . ILE B 114 ? 0.0513 0.0533 0.0784 -0.0061 -0.0017 -0.0006 337 ILE B N   
6954  C CA  . ILE B 114 ? 0.0635 0.0455 0.0850 -0.0019 -0.0019 -0.0009 337 ILE B CA  
6955  C C   . ILE B 114 ? 0.0511 0.0481 0.0858 -0.0022 -0.0146 -0.0119 337 ILE B C   
6956  O O   . ILE B 114 ? 0.0438 0.0529 0.1104 0.0007  -0.0142 -0.0056 337 ILE B O   
6957  C CB  . ILE B 114 ? 0.0747 0.0734 0.0819 -0.0057 -0.0133 -0.0069 337 ILE B CB  
6958  C CG1 . ILE B 114 ? 0.1165 0.0789 0.0786 -0.0144 -0.0017 -0.0016 337 ILE B CG1 
6959  C CG2 . ILE B 114 ? 0.0886 0.0991 0.0900 -0.0006 0.0028  0.0042  337 ILE B CG2 
6960  C CD1 . ILE B 114 ? 0.1441 0.0977 0.0914 -0.0171 0.0254  0.0042  337 ILE B CD1 
6972  N N   . SER B 115 ? 0.0611 0.0410 0.0908 -0.0012 -0.0084 0.0076  338 SER B N   
6973  C CA  A SER B 115 ? 0.0552 0.0494 0.0949 -0.0058 -0.0004 0.0002  338 SER B CA  
6974  C CA  B SER B 115 ? 0.0526 0.0429 0.0925 0.0027  -0.0095 -0.0042 338 SER B CA  
6975  C C   . SER B 115 ? 0.0498 0.0532 0.0952 0.0036  -0.0073 -0.0022 338 SER B C   
6976  O O   . SER B 115 ? 0.0634 0.0720 0.1099 0.0193  -0.0228 -0.0162 338 SER B O   
6977  C CB  A SER B 115 ? 0.0636 0.0675 0.1028 -0.0217 0.0141  0.0022  338 SER B CB  
6978  C CB  B SER B 115 ? 0.0624 0.0615 0.0999 0.0057  -0.0135 -0.0035 338 SER B CB  
6979  O OG  A SER B 115 ? 0.0635 0.0734 0.1075 -0.0294 0.0220  0.0074  338 SER B OG  
6980  O OG  B SER B 115 ? 0.0645 0.0589 0.1040 0.0143  -0.0195 -0.0040 338 SER B OG  
6991  N N   . GLN B 116 ? 0.0591 0.0524 0.0901 0.0132  -0.0108 -0.0132 339 GLN B N   
6992  C CA  . GLN B 116 ? 0.0554 0.0579 0.0853 0.0118  -0.0048 -0.0100 339 GLN B CA  
6993  C C   . GLN B 116 ? 0.0497 0.0615 0.0960 0.0076  -0.0069 -0.0103 339 GLN B C   
6994  O O   . GLN B 116 ? 0.0597 0.0631 0.0932 0.0079  -0.0083 -0.0012 339 GLN B O   
6995  C CB  . GLN B 116 ? 0.0586 0.0647 0.0900 0.0077  -0.0091 0.0010  339 GLN B CB  
6996  C CG  . GLN B 116 ? 0.0771 0.0561 0.0971 0.0053  -0.0026 -0.0008 339 GLN B CG  
6997  C CD  . GLN B 116 ? 0.0793 0.0595 0.0913 0.0068  0.0101  -0.0061 339 GLN B CD  
6998  O OE1 . GLN B 116 ? 0.0818 0.0818 0.0850 0.0028  0.0062  -0.0083 339 GLN B OE1 
6999  N NE2 . GLN B 116 ? 0.0757 0.0641 0.1026 0.0071  0.0094  0.0068  339 GLN B NE2 
7008  N N   . ARG B 117 ? 0.0489 0.0556 0.1040 0.0044  -0.0199 -0.0016 340 ARG B N   
7009  C CA  . ARG B 117 ? 0.0660 0.0517 0.1042 0.0114  -0.0098 -0.0067 340 ARG B CA  
7010  C C   . ARG B 117 ? 0.0662 0.0487 0.1086 0.0094  -0.0144 -0.0024 340 ARG B C   
7011  O O   . ARG B 117 ? 0.0669 0.0727 0.0991 0.0150  -0.0191 0.0058  340 ARG B O   
7012  C CB  . ARG B 117 ? 0.0892 0.0675 0.1036 0.0038  -0.0040 -0.0076 340 ARG B CB  
7013  C CG  . ARG B 117 ? 0.0954 0.0669 0.1083 -0.0030 0.0066  -0.0144 340 ARG B CG  
7014  C CD  . ARG B 117 ? 0.1232 0.0841 0.1251 0.0026  0.0021  -0.0158 340 ARG B CD  
7015  N NE  . ARG B 117 ? 0.1458 0.0990 0.1165 0.0219  0.0009  -0.0149 340 ARG B NE  
7016  C CZ  . ARG B 117 ? 0.1185 0.1019 0.1332 0.0230  0.0058  -0.0018 340 ARG B CZ  
7017  N NH1 . ARG B 117 ? 0.1513 0.1348 0.1931 0.0183  0.0059  -0.0411 340 ARG B NH1 
7018  N NH2 . ARG B 117 ? 0.1038 0.1006 0.1118 0.0254  -0.0026 -0.0033 340 ARG B NH2 
7032  N N   . ASP B 118 ? 0.0663 0.0609 0.1028 0.0179  -0.0209 -0.0056 341 ASP B N   
7033  C CA  . ASP B 118 ? 0.0865 0.0628 0.1027 0.0120  -0.0030 -0.0100 341 ASP B CA  
7034  C C   . ASP B 118 ? 0.0844 0.0639 0.1022 0.0142  -0.0104 0.0025  341 ASP B C   
7035  O O   . ASP B 118 ? 0.0955 0.0690 0.1033 0.0010  -0.0116 -0.0028 341 ASP B O   
7036  C CB  . ASP B 118 ? 0.0889 0.0767 0.1276 0.0146  0.0034  -0.0116 341 ASP B CB  
7037  C CG  . ASP B 118 ? 0.0757 0.0877 0.1160 0.0170  -0.0208 0.0003  341 ASP B CG  
7038  O OD1 . ASP B 118 ? 0.1038 0.0915 0.1348 0.0116  -0.0025 -0.0013 341 ASP B OD1 
7039  O OD2 . ASP B 118 ? 0.0909 0.1113 0.1356 0.0053  0.0067  0.0029  341 ASP B OD2 
7044  N N   . ARG B 119 ? 0.0749 0.0824 0.1013 0.0034  -0.0098 -0.0005 342 ARG B N   
7045  C CA  . ARG B 119 ? 0.0865 0.1016 0.1499 -0.0137 -0.0342 0.0025  342 ARG B CA  
7046  C C   . ARG B 119 ? 0.1081 0.0938 0.1789 -0.0134 -0.0156 -0.0074 342 ARG B C   
7047  O O   . ARG B 119 ? 0.1274 0.0972 0.2211 -0.0237 -0.0195 -0.0094 342 ARG B O   
7048  C CB  . ARG B 119 ? 0.1118 0.1565 0.2093 -0.0249 -0.0575 0.0116  342 ARG B CB  
7049  C CG  . ARG B 119 ? 0.1325 0.1763 0.2012 -0.0282 -0.0693 -0.0017 342 ARG B CG  
7050  C CD  . ARG B 119 ? 0.1600 0.1714 0.1675 -0.0388 -0.0765 0.0161  342 ARG B CD  
7051  N NE  . ARG B 119 ? 0.1668 0.1396 0.1482 -0.0569 -0.0476 -0.0150 342 ARG B NE  
7052  C CZ  . ARG B 119 ? 0.1579 0.1296 0.1164 -0.0524 -0.0520 -0.0028 342 ARG B CZ  
7053  N NH1 . ARG B 119 ? 0.1705 0.1217 0.1340 -0.0420 -0.0207 -0.0085 342 ARG B NH1 
7054  N NH2 . ARG B 119 ? 0.1663 0.1356 0.1311 -0.0337 -0.0320 -0.0169 342 ARG B NH2 
7068  N N   . GLU B 120 ? 0.1032 0.0946 0.1774 -0.0127 -0.0414 -0.0107 343 GLU B N   
7069  C CA  . GLU B 120 ? 0.1239 0.1126 0.1822 0.0118  -0.0463 -0.0191 343 GLU B CA  
7070  C C   . GLU B 120 ? 0.0949 0.0982 0.1773 -0.0010 -0.0415 -0.0220 343 GLU B C   
7071  O O   . GLU B 120 ? 0.1041 0.1072 0.2005 -0.0152 -0.0572 -0.0057 343 GLU B O   
7083  N N   . GLY B 121 ? 0.0831 0.0988 0.1849 0.0006  -0.0225 0.0013  344 GLY B N   
7084  C CA  . GLY B 121 ? 0.0917 0.0951 0.1674 0.0239  -0.0093 -0.0024 344 GLY B CA  
7085  C C   . GLY B 121 ? 0.0955 0.0968 0.1337 0.0233  -0.0072 -0.0147 344 GLY B C   
7086  O O   . GLY B 121 ? 0.0925 0.1342 0.1394 0.0306  -0.0234 -0.0375 344 GLY B O   
7090  N N   . THR B 122 ? 0.0836 0.0887 0.1181 0.0192  -0.0027 0.0046  345 THR B N   
7091  C CA  . THR B 122 ? 0.0899 0.0693 0.1059 0.0174  0.0076  0.0009  345 THR B CA  
7092  C C   . THR B 122 ? 0.0928 0.0706 0.1060 0.0190  0.0004  0.0085  345 THR B C   
7093  O O   . THR B 122 ? 0.0977 0.0731 0.1218 0.0162  0.0053  0.0075  345 THR B O   
7094  C CB  . THR B 122 ? 0.0785 0.0663 0.0991 0.0216  0.0143  0.0065  345 THR B CB  
7095  O OG1 . THR B 122 ? 0.0705 0.0757 0.1142 0.0160  0.0148  0.0019  345 THR B OG1 
7096  C CG2 . THR B 122 ? 0.0859 0.0761 0.1034 0.0228  0.0026  -0.0061 345 THR B CG2 
7104  N N   . PRO B 123 ? 0.0958 0.0641 0.0987 0.0218  0.0049  -0.0025 346 PRO B N   
7105  C CA  . PRO B 123 ? 0.0991 0.0605 0.1149 0.0092  -0.0087 -0.0096 346 PRO B CA  
7106  C C   . PRO B 123 ? 0.1143 0.0634 0.1117 0.0144  0.0211  -0.0041 346 PRO B C   
7107  O O   . PRO B 123 ? 0.0987 0.0703 0.1073 0.0096  0.0004  0.0094  346 PRO B O   
7108  C CB  . PRO B 123 ? 0.1134 0.0706 0.1395 0.0099  -0.0063 -0.0142 346 PRO B CB  
7109  C CG  . PRO B 123 ? 0.1105 0.0795 0.1317 0.0082  -0.0073 -0.0142 346 PRO B CG  
7110  C CD  . PRO B 123 ? 0.1042 0.0789 0.1019 0.0136  -0.0088 -0.0085 346 PRO B CD  
7118  N N   . SER B 124 ? 0.0887 0.0609 0.1174 0.0126  0.0000  -0.0124 347 SER B N   
7119  C CA  . SER B 124 ? 0.0917 0.0719 0.1075 0.0176  0.0013  -0.0124 347 SER B CA  
7120  C C   . SER B 124 ? 0.0912 0.0662 0.1081 0.0212  -0.0077 0.0030  347 SER B C   
7121  O O   . SER B 124 ? 0.1058 0.1098 0.1167 0.0416  -0.0073 -0.0105 347 SER B O   
7122  C CB  . SER B 124 ? 0.0924 0.0717 0.1107 0.0046  -0.0105 -0.0164 347 SER B CB  
7123  O OG  . SER B 124 ? 0.0855 0.0714 0.1424 -0.0101 0.0024  -0.0021 347 SER B OG  
7129  N N   . GLU B 125 ? 0.1014 0.0682 0.1026 0.0237  0.0001  -0.0007 348 GLU B N   
7130  C CA  . GLU B 125 ? 0.1144 0.0742 0.0902 0.0233  -0.0095 -0.0064 348 GLU B CA  
7131  C C   . GLU B 125 ? 0.1346 0.0665 0.1063 0.0236  0.0074  -0.0019 348 GLU B C   
7132  O O   . GLU B 125 ? 0.1396 0.0848 0.1119 0.0151  0.0152  -0.0105 348 GLU B O   
7133  C CB  . GLU B 125 ? 0.1131 0.0796 0.1197 0.0263  -0.0093 -0.0168 348 GLU B CB  
7134  C CG  . GLU B 125 ? 0.1133 0.1007 0.1259 0.0138  0.0025  -0.0288 348 GLU B CG  
7135  C CD  . GLU B 125 ? 0.1284 0.1581 0.1283 -0.0041 0.0197  -0.0303 348 GLU B CD  
7136  O OE1 . GLU B 125 ? 0.1619 0.1961 0.1166 -0.0134 0.0115  -0.0326 348 GLU B OE1 
7137  O OE2 . GLU B 125 ? 0.1344 0.1904 0.1423 0.0016  0.0056  -0.0480 348 GLU B OE2 
7144  N N   . ASN B 126 ? 0.1474 0.0717 0.1372 0.0374  0.0209  0.0191  349 ASN B N   
7145  C CA  . ASN B 126 ? 0.1654 0.0855 0.1581 0.0113  0.0354  0.0167  349 ASN B CA  
7146  C C   . ASN B 126 ? 0.1337 0.0765 0.1564 -0.0015 0.0316  -0.0013 349 ASN B C   
7147  O O   . ASN B 126 ? 0.1571 0.0915 0.1744 0.0104  0.0468  0.0151  349 ASN B O   
7148  C CB  . ASN B 126 ? 0.2131 0.1309 0.1709 0.0064  0.0543  0.0323  349 ASN B CB  
7149  C CG  . ASN B 126 ? 0.2749 0.1734 0.2189 -0.0071 0.0900  0.0081  349 ASN B CG  
7150  O OD1 . ASN B 126 ? 0.2929 0.1838 0.2463 -0.0043 0.0995  0.0035  349 ASN B OD1 
7151  N ND2 . ASN B 126 ? 0.2953 0.1991 0.2323 -0.0151 0.1114  0.0096  349 ASN B ND2 
7158  N N   . ASN B 127 ? 0.1223 0.0644 0.1392 -0.0093 0.0138  -0.0016 350 ASN B N   
7159  C CA  . ASN B 127 ? 0.1076 0.0729 0.1568 -0.0198 -0.0023 -0.0192 350 ASN B CA  
7160  C C   . ASN B 127 ? 0.0932 0.0760 0.1610 -0.0003 -0.0022 -0.0105 350 ASN B C   
7161  O O   . ASN B 127 ? 0.0930 0.1012 0.2006 -0.0002 -0.0056 -0.0225 350 ASN B O   
7162  C CB  . ASN B 127 ? 0.1470 0.1061 0.1966 -0.0299 -0.0117 -0.0293 350 ASN B CB  
7163  C CG  . ASN B 127 ? 0.2077 0.1549 0.2469 -0.0522 0.0213  -0.0415 350 ASN B CG  
7164  O OD1 . ASN B 127 ? 0.2172 0.1853 0.2655 -0.0531 0.0135  -0.0339 350 ASN B OD1 
7165  N ND2 . ASN B 127 ? 0.2534 0.1781 0.2790 -0.0667 0.0432  -0.0496 350 ASN B ND2 
7172  N N   . GLN B 128 ? 0.0944 0.0762 0.1408 0.0146  0.0069  -0.0081 351 GLN B N   
7173  C CA  . GLN B 128 ? 0.0985 0.0728 0.1238 0.0136  0.0017  0.0042  351 GLN B CA  
7174  C C   . GLN B 128 ? 0.0879 0.0640 0.1106 0.0096  0.0119  0.0059  351 GLN B C   
7175  O O   . GLN B 128 ? 0.0898 0.0665 0.1214 0.0169  0.0300  0.0028  351 GLN B O   
7176  C CB  . GLN B 128 ? 0.1262 0.0824 0.1360 0.0061  0.0186  0.0145  351 GLN B CB  
7177  C CG  . GLN B 128 ? 0.1747 0.1347 0.1427 0.0217  0.0242  0.0249  351 GLN B CG  
7178  C CD  . GLN B 128 ? 0.2399 0.2041 0.1607 0.0355  0.0216  0.0322  351 GLN B CD  
7179  O OE1 . GLN B 128 ? 0.2779 0.2580 0.1864 -0.0024 -0.0084 0.0158  351 GLN B OE1 
7180  N NE2 . GLN B 128 ? 0.2959 0.2271 0.1896 0.0398  0.0398  0.0002  351 GLN B NE2 
7189  N N   . LYS B 129 ? 0.0936 0.0646 0.0974 0.0084  0.0126  -0.0034 352 LYS B N   
7190  C CA  . LYS B 129 ? 0.0820 0.0711 0.1323 0.0005  0.0093  0.0094  352 LYS B CA  
7191  C C   . LYS B 129 ? 0.0868 0.0541 0.0971 0.0176  0.0141  -0.0011 352 LYS B C   
7192  O O   . LYS B 129 ? 0.0912 0.0759 0.0914 -0.0001 0.0122  -0.0004 352 LYS B O   
7193  C CB  . LYS B 129 ? 0.1019 0.0831 0.1582 0.0145  0.0074  0.0177  352 LYS B CB  
7194  C CG  . LYS B 129 ? 0.1048 0.1198 0.1756 -0.0040 -0.0029 0.0394  352 LYS B CG  
7195  C CD  . LYS B 129 ? 0.1354 0.1465 0.1790 -0.0278 0.0007  0.0118  352 LYS B CD  
7196  C CE  . LYS B 129 ? 0.1347 0.1997 0.2291 -0.0400 -0.0084 0.0072  352 LYS B CE  
7197  N NZ  . LYS B 129 ? 0.1582 0.2403 0.2686 -0.0368 -0.0003 0.0044  352 LYS B NZ  
7211  N N   . ALA B 130 ? 0.0849 0.0516 0.0909 0.0174  0.0007  -0.0079 353 ALA B N   
7212  C CA  . ALA B 130 ? 0.0665 0.0589 0.0881 0.0166  -0.0036 -0.0019 353 ALA B CA  
7213  C C   . ALA B 130 ? 0.0586 0.0617 0.0922 0.0126  -0.0033 0.0141  353 ALA B C   
7214  O O   . ALA B 130 ? 0.0686 0.0678 0.0916 0.0133  -0.0077 -0.0092 353 ALA B O   
7215  C CB  . ALA B 130 ? 0.0878 0.0684 0.0934 0.0108  0.0021  -0.0121 353 ALA B CB  
7221  N N   . ASN B 131 ? 0.0544 0.0472 0.1046 0.0064  -0.0137 -0.0110 354 ASN B N   
7222  C CA  . ASN B 131 ? 0.0667 0.0458 0.1103 0.0101  -0.0044 -0.0106 354 ASN B CA  
7223  C C   . ASN B 131 ? 0.0728 0.0496 0.1027 0.0099  -0.0090 -0.0015 354 ASN B C   
7224  O O   . ASN B 131 ? 0.0671 0.0588 0.1139 0.0183  -0.0157 -0.0059 354 ASN B O   
7225  C CB  . ASN B 131 ? 0.0790 0.0513 0.1056 0.0108  -0.0024 -0.0055 354 ASN B CB  
7226  C CG  . ASN B 131 ? 0.0661 0.0612 0.1114 0.0072  -0.0133 -0.0084 354 ASN B CG  
7227  O OD1 . ASN B 131 ? 0.0737 0.0647 0.1141 0.0112  -0.0077 -0.0043 354 ASN B OD1 
7228  N ND2 . ASN B 131 ? 0.0843 0.0536 0.1314 0.0131  0.0231  0.0050  354 ASN B ND2 
7235  N N   . ARG B 132 ? 0.0513 0.0445 0.1031 0.0085  -0.0117 0.0092  355 ARG B N   
7236  C CA  . ARG B 132 ? 0.0526 0.0489 0.1173 0.0101  -0.0032 -0.0042 355 ARG B CA  
7237  C C   . ARG B 132 ? 0.0526 0.0503 0.1199 0.0029  -0.0008 -0.0017 355 ARG B C   
7238  O O   . ARG B 132 ? 0.0604 0.0571 0.1358 0.0085  -0.0187 -0.0003 355 ARG B O   
7239  C CB  . ARG B 132 ? 0.0672 0.0600 0.1094 0.0125  0.0059  -0.0051 355 ARG B CB  
7240  C CG  . ARG B 132 ? 0.0634 0.0546 0.1134 0.0090  0.0075  -0.0029 355 ARG B CG  
7241  C CD  . ARG B 132 ? 0.0722 0.0662 0.1194 0.0006  0.0129  -0.0007 355 ARG B CD  
7242  N NE  . ARG B 132 ? 0.0855 0.0670 0.1323 0.0140  0.0132  -0.0029 355 ARG B NE  
7243  C CZ  . ARG B 132 ? 0.0756 0.0638 0.1174 0.0102  0.0036  -0.0104 355 ARG B CZ  
7244  N NH1 . ARG B 132 ? 0.0832 0.0667 0.1065 0.0073  0.0074  -0.0126 355 ARG B NH1 
7245  N NH2 . ARG B 132 ? 0.0833 0.0541 0.1576 0.0211  -0.0104 0.0002  355 ARG B NH2 
7259  N N   . SER B 133 ? 0.0455 0.0452 0.1059 -0.0043 -0.0084 -0.0033 356 SER B N   
7260  C CA  . SER B 133 ? 0.0675 0.0520 0.0938 0.0078  -0.0164 0.0007  356 SER B CA  
7261  C C   . SER B 133 ? 0.0568 0.0528 0.1016 0.0103  -0.0103 0.0029  356 SER B C   
7262  O O   . SER B 133 ? 0.0643 0.0523 0.1150 -0.0022 0.0025  0.0098  356 SER B O   
7263  C CB  . SER B 133 ? 0.0646 0.0618 0.1026 0.0105  -0.0068 0.0022  356 SER B CB  
7264  O OG  . SER B 133 ? 0.0609 0.0634 0.1064 0.0054  -0.0043 -0.0001 356 SER B OG  
7270  N N   . HIS B 134 ? 0.0555 0.0506 0.0941 -0.0005 -0.0127 0.0107  357 HIS B N   
7271  C CA  . HIS B 134 ? 0.0659 0.0578 0.0801 -0.0024 -0.0002 0.0043  357 HIS B CA  
7272  C C   . HIS B 134 ? 0.0598 0.0502 0.0988 -0.0032 0.0006  0.0067  357 HIS B C   
7273  O O   . HIS B 134 ? 0.0593 0.0590 0.1193 0.0045  0.0028  -0.0044 357 HIS B O   
7274  C CB  . HIS B 134 ? 0.0791 0.0637 0.1054 0.0089  0.0144  0.0125  357 HIS B CB  
7275  C CG  . HIS B 134 ? 0.0702 0.0582 0.1040 0.0137  0.0097  -0.0021 357 HIS B CG  
7276  N ND1 . HIS B 134 ? 0.0649 0.0795 0.1209 0.0085  0.0154  -0.0086 357 HIS B ND1 
7277  C CD2 . HIS B 134 ? 0.0833 0.0645 0.1093 0.0067  0.0017  -0.0075 357 HIS B CD2 
7278  C CE1 . HIS B 134 ? 0.0791 0.0739 0.1366 0.0054  0.0256  -0.0134 357 HIS B CE1 
7279  N NE2 . HIS B 134 ? 0.0874 0.0741 0.1302 0.0053  0.0187  -0.0046 357 HIS B NE2 
7287  N N   . GLN B 135 ? 0.0518 0.0483 0.1040 0.0082  -0.0185 0.0058  358 GLN B N   
7288  C CA  . GLN B 135 ? 0.0565 0.0441 0.0949 -0.0001 -0.0121 0.0021  358 GLN B CA  
7289  C C   . GLN B 135 ? 0.0518 0.0590 0.0948 0.0053  -0.0090 -0.0014 358 GLN B C   
7290  O O   . GLN B 135 ? 0.0784 0.0744 0.0927 0.0213  -0.0071 0.0023  358 GLN B O   
7291  C CB  . GLN B 135 ? 0.0598 0.0532 0.0972 -0.0033 -0.0060 -0.0035 358 GLN B CB  
7292  C CG  . GLN B 135 ? 0.0867 0.0651 0.1088 -0.0017 0.0011  -0.0207 358 GLN B CG  
7293  C CD  . GLN B 135 ? 0.0710 0.0721 0.1448 0.0055  -0.0382 -0.0221 358 GLN B CD  
7294  O OE1 . GLN B 135 ? 0.0683 0.0730 0.1568 0.0016  -0.0333 -0.0226 358 GLN B OE1 
7295  N NE2 . GLN B 135 ? 0.0689 0.0837 0.1851 -0.0029 -0.0289 -0.0340 358 GLN B NE2 
7304  N N   . GLY B 136 ? 0.0580 0.0643 0.0888 0.0161  -0.0032 -0.0027 359 GLY B N   
7305  C CA  . GLY B 136 ? 0.0681 0.0635 0.1021 0.0167  -0.0106 -0.0026 359 GLY B CA  
7306  C C   . GLY B 136 ? 0.0664 0.0697 0.1019 0.0084  -0.0084 0.0034  359 GLY B C   
7307  O O   . GLY B 136 ? 0.0711 0.0731 0.0934 0.0186  0.0086  0.0060  359 GLY B O   
7311  N N   . VAL B 137 ? 0.0556 0.0617 0.0863 0.0031  -0.0072 -0.0009 360 VAL B N   
7312  C CA  . VAL B 137 ? 0.0763 0.0619 0.0853 0.0179  -0.0044 -0.0015 360 VAL B CA  
7313  C C   . VAL B 137 ? 0.0800 0.0561 0.0839 0.0196  -0.0115 0.0010  360 VAL B C   
7314  O O   . VAL B 137 ? 0.0755 0.0682 0.1027 0.0095  -0.0125 -0.0133 360 VAL B O   
7315  C CB  . VAL B 137 ? 0.0638 0.0641 0.1333 -0.0014 -0.0117 -0.0006 360 VAL B CB  
7316  C CG1 . VAL B 137 ? 0.0835 0.0628 0.1727 0.0075  0.0144  0.0000  360 VAL B CG1 
7317  C CG2 . VAL B 137 ? 0.1068 0.1122 0.1616 -0.0209 -0.0060 -0.0008 360 VAL B CG2 
7327  N N   . ILE B 138 ? 0.0777 0.0605 0.0775 0.0178  -0.0210 -0.0001 361 ILE B N   
7328  C CA  . ILE B 138 ? 0.0862 0.0604 0.0702 0.0067  -0.0041 0.0006  361 ILE B CA  
7329  C C   . ILE B 138 ? 0.0804 0.0667 0.0660 0.0111  -0.0120 0.0072  361 ILE B C   
7330  O O   . ILE B 138 ? 0.0809 0.0664 0.0925 0.0191  -0.0042 0.0089  361 ILE B O   
7331  C CB  . ILE B 138 ? 0.0927 0.0660 0.0660 0.0198  -0.0054 0.0047  361 ILE B CB  
7332  C CG1 . ILE B 138 ? 0.1000 0.0735 0.0906 0.0082  -0.0090 0.0130  361 ILE B CG1 
7333  C CG2 . ILE B 138 ? 0.0975 0.0784 0.0873 0.0037  -0.0192 -0.0125 361 ILE B CG2 
7334  C CD1 . ILE B 138 ? 0.1186 0.0757 0.0838 0.0054  -0.0109 0.0022  361 ILE B CD1 
7346  N N   . SER B 139 ? 0.0702 0.0628 0.0657 0.0151  0.0049  0.0030  362 SER B N   
7347  C CA  . SER B 139 ? 0.0658 0.0615 0.0876 0.0017  -0.0049 0.0002  362 SER B CA  
7348  C C   . SER B 139 ? 0.0661 0.0625 0.0972 0.0117  -0.0020 -0.0162 362 SER B C   
7349  O O   . SER B 139 ? 0.0851 0.0894 0.1222 0.0248  -0.0188 -0.0334 362 SER B O   
7350  C CB  . SER B 139 ? 0.0926 0.0722 0.1012 0.0041  0.0136  0.0048  362 SER B CB  
7351  O OG  . SER B 139 ? 0.1115 0.0857 0.1086 0.0130  0.0085  0.0256  362 SER B OG  
7357  N N   . THR B 140 ? 0.0614 0.0558 0.0981 0.0086  -0.0119 -0.0038 363 THR B N   
7358  C CA  . THR B 140 ? 0.0718 0.0588 0.0851 0.0058  -0.0034 0.0036  363 THR B CA  
7359  C C   . THR B 140 ? 0.0633 0.0811 0.1109 0.0105  -0.0154 0.0152  363 THR B C   
7360  O O   . THR B 140 ? 0.0883 0.1109 0.1145 0.0232  -0.0176 0.0274  363 THR B O   
7361  C CB  . THR B 140 ? 0.0707 0.0727 0.0969 -0.0024 -0.0065 0.0064  363 THR B CB  
7362  O OG1 . THR B 140 ? 0.0797 0.0690 0.0989 -0.0108 -0.0052 -0.0156 363 THR B OG1 
7363  C CG2 . THR B 140 ? 0.0952 0.0820 0.1018 -0.0098 0.0129  0.0039  363 THR B CG2 
7371  N N   . ILE B 141 ? 0.0632 0.0761 0.1230 0.0035  -0.0144 0.0173  364 ILE B N   
7372  C CA  . ILE B 141 ? 0.1111 0.0963 0.1331 0.0145  0.0137  0.0445  364 ILE B CA  
7373  C C   . ILE B 141 ? 0.1251 0.1118 0.1166 0.0100  0.0150  0.0302  364 ILE B C   
7374  O O   . ILE B 141 ? 0.1784 0.1215 0.1389 0.0107  0.0156  0.0371  364 ILE B O   
7375  C CB  . ILE B 141 ? 0.1444 0.1075 0.1593 0.0057  0.0277  0.0018  364 ILE B CB  
7376  C CG1 . ILE B 141 ? 0.1390 0.1096 0.1961 0.0055  0.0138  0.0114  364 ILE B CG1 
7377  C CG2 . ILE B 141 ? 0.1937 0.1045 0.1648 0.0150  0.0599  -0.0070 364 ILE B CG2 
7378  C CD1 . ILE B 141 ? 0.1532 0.1177 0.2315 0.0019  0.0530  0.0020  364 ILE B CD1 
7390  N N   . SER B 142 ? 0.1131 0.1299 0.1045 0.0370  0.0163  0.0186  365 SER B N   
7391  C CA  . SER B 142 ? 0.1127 0.1400 0.1083 0.0290  0.0290  0.0301  365 SER B CA  
7392  C C   . SER B 142 ? 0.1160 0.1122 0.1210 0.0281  0.0144  0.0307  365 SER B C   
7393  O O   . SER B 142 ? 0.1138 0.1049 0.1351 0.0262  0.0086  0.0232  365 SER B O   
7394  C CB  . SER B 142 ? 0.1288 0.1675 0.1150 0.0477  0.0446  0.0164  365 SER B CB  
7395  O OG  . SER B 142 ? 0.1593 0.1715 0.1282 0.0427  0.0401  -0.0056 365 SER B OG  
7401  N N   . PRO B 143 ? 0.1498 0.1243 0.1121 0.0228  -0.0073 0.0340  366 PRO B N   
7402  C CA  . PRO B 143 ? 0.1658 0.1398 0.1202 0.0213  -0.0148 0.0349  366 PRO B CA  
7403  C C   . PRO B 143 ? 0.1322 0.1278 0.1169 0.0215  0.0017  0.0122  366 PRO B C   
7404  O O   . PRO B 143 ? 0.1344 0.1370 0.1364 0.0180  -0.0025 0.0130  366 PRO B O   
7405  C CB  . PRO B 143 ? 0.2241 0.1677 0.1359 -0.0011 0.0070  0.0446  366 PRO B CB  
7406  C CG  . PRO B 143 ? 0.2368 0.1951 0.1529 -0.0097 0.0269  0.0447  366 PRO B CG  
7407  C CD  . PRO B 143 ? 0.2019 0.1656 0.1272 -0.0007 0.0277  0.0395  366 PRO B CD  
7415  N N   . LYS B 144 ? 0.1265 0.1195 0.1243 0.0274  0.0215  0.0156  367 LYS B N   
7416  C CA  . LYS B 144 ? 0.1310 0.1273 0.1487 0.0379  0.0404  0.0154  367 LYS B CA  
7417  C C   . LYS B 144 ? 0.0985 0.0985 0.1244 0.0334  0.0092  0.0199  367 LYS B C   
7418  O O   . LYS B 144 ? 0.1056 0.0925 0.1187 0.0216  -0.0032 0.0097  367 LYS B O   
7419  C CB  . LYS B 144 ? 0.1689 0.1729 0.2331 0.0294  0.0720  0.0255  367 LYS B CB  
7420  C CG  . LYS B 144 ? 0.2398 0.2264 0.3009 0.0302  0.1032  0.0300  367 LYS B CG  
7421  C CD  . LYS B 144 ? 0.3101 0.2740 0.3389 0.0216  0.1232  0.0275  367 LYS B CD  
7422  C CE  . LYS B 144 ? 0.3562 0.3005 0.3798 0.0240  0.1333  0.0191  367 LYS B CE  
7423  N NZ  . LYS B 144 ? 0.3981 0.3246 0.4100 0.0168  0.1418  0.0168  367 LYS B NZ  
7437  N N   . PHE B 145 ? 0.0901 0.0784 0.1236 0.0114  0.0101  0.0127  368 PHE B N   
7438  C CA  . PHE B 145 ? 0.0838 0.0845 0.0886 0.0146  -0.0053 0.0063  368 PHE B CA  
7439  C C   . PHE B 145 ? 0.0821 0.0892 0.0906 0.0184  -0.0066 -0.0139 368 PHE B C   
7440  O O   . PHE B 145 ? 0.0801 0.0916 0.1027 0.0260  -0.0101 -0.0069 368 PHE B O   
7441  C CB  . PHE B 145 ? 0.0861 0.0754 0.0859 0.0136  -0.0166 0.0125  368 PHE B CB  
7442  C CG  . PHE B 145 ? 0.0796 0.0793 0.0907 -0.0063 -0.0204 0.0096  368 PHE B CG  
7443  C CD1 . PHE B 145 ? 0.0775 0.0711 0.1057 -0.0037 -0.0174 0.0119  368 PHE B CD1 
7444  C CD2 . PHE B 145 ? 0.0986 0.0853 0.0968 -0.0120 -0.0013 -0.0010 368 PHE B CD2 
7445  C CE1 . PHE B 145 ? 0.1161 0.0764 0.0894 -0.0149 -0.0057 0.0121  368 PHE B CE1 
7446  C CE2 . PHE B 145 ? 0.1031 0.0741 0.0927 -0.0163 -0.0032 -0.0137 368 PHE B CE2 
7447  C CZ  . PHE B 145 ? 0.1196 0.0777 0.0976 -0.0369 0.0056  -0.0136 368 PHE B CZ  
7457  N N   . VAL B 146 ? 0.0969 0.0781 0.0868 0.0223  -0.0087 0.0027  369 VAL B N   
7458  C CA  . VAL B 146 ? 0.0762 0.0866 0.0904 0.0143  -0.0093 -0.0087 369 VAL B CA  
7459  C C   . VAL B 146 ? 0.0741 0.0720 0.0891 0.0148  -0.0158 -0.0141 369 VAL B C   
7460  O O   . VAL B 146 ? 0.0839 0.0818 0.0915 0.0269  -0.0267 -0.0124 369 VAL B O   
7461  C CB  . VAL B 146 ? 0.1036 0.0935 0.0838 0.0335  -0.0128 -0.0120 369 VAL B CB  
7462  C CG1 . VAL B 146 ? 0.1135 0.1060 0.0875 0.0426  -0.0068 0.0049  369 VAL B CG1 
7463  C CG2 . VAL B 146 ? 0.1337 0.0885 0.0798 0.0226  -0.0006 -0.0032 369 VAL B CG2 
7473  N N   . PRO B 147 ? 0.0806 0.0700 0.0882 0.0173  -0.0128 -0.0162 370 PRO B N   
7474  C CA  . PRO B 147 ? 0.0853 0.0741 0.0879 0.0172  -0.0171 0.0012  370 PRO B CA  
7475  C C   . PRO B 147 ? 0.0737 0.0912 0.0913 0.0222  -0.0223 -0.0017 370 PRO B C   
7476  O O   . PRO B 147 ? 0.0931 0.0785 0.1167 -0.0001 -0.0240 -0.0043 370 PRO B O   
7477  C CB  . PRO B 147 ? 0.0775 0.0678 0.0824 0.0079  -0.0192 -0.0026 370 PRO B CB  
7478  C CG  . PRO B 147 ? 0.0729 0.0604 0.0719 0.0215  -0.0110 -0.0127 370 PRO B CG  
7479  C CD  . PRO B 147 ? 0.0679 0.0684 0.0764 0.0218  -0.0217 -0.0084 370 PRO B CD  
7487  N N   . LYS B 148 ? 0.0689 0.1001 0.0979 0.0264  -0.0320 -0.0183 371 LYS B N   
7488  C CA  A LYS B 148 ? 0.0805 0.1227 0.1006 0.0232  -0.0384 -0.0303 371 LYS B CA  
7489  C CA  B LYS B 148 ? 0.0844 0.1188 0.0985 0.0175  -0.0319 -0.0343 371 LYS B CA  
7490  C C   . LYS B 148 ? 0.0932 0.1293 0.1023 0.0101  -0.0317 -0.0400 371 LYS B C   
7491  O O   . LYS B 148 ? 0.1048 0.1604 0.1343 0.0002  -0.0208 -0.0568 371 LYS B O   
7492  C CB  A LYS B 148 ? 0.0944 0.1420 0.1159 0.0276  -0.0381 -0.0250 371 LYS B CB  
7493  C CB  B LYS B 148 ? 0.0947 0.1277 0.1005 0.0148  -0.0288 -0.0421 371 LYS B CB  
7494  C CG  A LYS B 148 ? 0.1349 0.1701 0.1633 0.0191  -0.0247 -0.0245 371 LYS B CG  
7495  C CG  B LYS B 148 ? 0.1137 0.1391 0.1140 0.0068  -0.0241 -0.0524 371 LYS B CG  
7496  C CD  A LYS B 148 ? 0.1424 0.1833 0.1468 0.0192  -0.0146 -0.0221 371 LYS B CD  
7497  C CD  B LYS B 148 ? 0.1258 0.1482 0.1316 0.0027  -0.0255 -0.0489 371 LYS B CD  
7498  C CE  A LYS B 148 ? 0.1458 0.1915 0.1688 0.0339  0.0183  -0.0120 371 LYS B CE  
7499  C CE  B LYS B 148 ? 0.1350 0.1577 0.1458 -0.0057 -0.0195 -0.0415 371 LYS B CE  
7500  N NZ  A LYS B 148 ? 0.1504 0.2066 0.1696 0.0401  0.0085  -0.0099 371 LYS B NZ  
7501  N NZ  B LYS B 148 ? 0.1452 0.1624 0.1623 -0.0061 -0.0156 -0.0306 371 LYS B NZ  
7526  N N   . LEU B 149 ? 0.0983 0.1071 0.1017 0.0212  -0.0263 -0.0294 372 LEU B N   
7527  C CA  . LEU B 149 ? 0.1167 0.1195 0.1143 0.0276  -0.0272 -0.0202 372 LEU B CA  
7528  C C   . LEU B 149 ? 0.1309 0.1066 0.1198 0.0201  -0.0117 -0.0259 372 LEU B C   
7529  O O   . LEU B 149 ? 0.1995 0.1179 0.1330 0.0559  0.0191  -0.0268 372 LEU B O   
7530  C CB  . LEU B 149 ? 0.1027 0.1309 0.1097 0.0392  -0.0407 -0.0260 372 LEU B CB  
7531  C CG  . LEU B 149 ? 0.1511 0.1502 0.1174 0.0412  -0.0509 -0.0122 372 LEU B CG  
7532  C CD1 . LEU B 149 ? 0.1893 0.1550 0.1085 0.0343  -0.0322 -0.0158 372 LEU B CD1 
7533  C CD2 . LEU B 149 ? 0.1659 0.1608 0.1522 0.0593  -0.0368 0.0022  372 LEU B CD2 
7545  N N   . GLY B 150 ? 0.0991 0.0958 0.1165 0.0119  -0.0175 -0.0166 373 GLY B N   
7546  C CA  . GLY B 150 ? 0.0853 0.0919 0.1159 0.0097  -0.0295 -0.0126 373 GLY B CA  
7547  C C   . GLY B 150 ? 0.0889 0.0897 0.1015 0.0120  -0.0307 -0.0213 373 GLY B C   
7548  O O   . GLY B 150 ? 0.0968 0.0813 0.1202 0.0171  -0.0344 -0.0200 373 GLY B O   
7552  N N   . SER B 151 ? 0.0924 0.0861 0.1030 0.0246  -0.0234 -0.0249 374 SER B N   
7553  C CA  . SER B 151 ? 0.0877 0.0739 0.1064 0.0174  -0.0075 -0.0118 374 SER B CA  
7554  C C   . SER B 151 ? 0.0793 0.0651 0.0922 0.0196  -0.0160 -0.0096 374 SER B C   
7555  O O   . SER B 151 ? 0.0790 0.0665 0.1130 0.0260  -0.0279 -0.0064 374 SER B O   
7556  C CB  . SER B 151 ? 0.1116 0.0819 0.1087 0.0204  -0.0111 -0.0013 374 SER B CB  
7557  O OG  . SER B 151 ? 0.1297 0.0986 0.1231 0.0250  -0.0068 -0.0058 374 SER B OG  
7563  N N   . VAL B 152 ? 0.0959 0.0582 0.0890 0.0168  -0.0230 -0.0075 375 VAL B N   
7564  C CA  . VAL B 152 ? 0.0932 0.0499 0.0939 0.0147  -0.0239 -0.0025 375 VAL B CA  
7565  C C   . VAL B 152 ? 0.0902 0.0492 0.1000 0.0278  -0.0206 -0.0014 375 VAL B C   
7566  O O   . VAL B 152 ? 0.0963 0.0588 0.1469 0.0330  -0.0087 -0.0043 375 VAL B O   
7567  C CB  . VAL B 152 ? 0.0848 0.0610 0.1034 0.0292  -0.0185 -0.0091 375 VAL B CB  
7568  C CG1 . VAL B 152 ? 0.0881 0.0713 0.1010 0.0282  0.0037  -0.0027 375 VAL B CG1 
7569  C CG2 . VAL B 152 ? 0.0912 0.0637 0.1253 0.0340  -0.0196 -0.0074 375 VAL B CG2 
7579  N N   . MET B 153 ? 0.1001 0.0594 0.1048 0.0094  -0.0048 -0.0150 376 MET B N   
7580  C CA  A MET B 153 ? 0.1018 0.0713 0.0954 0.0134  0.0006  -0.0097 376 MET B CA  
7581  C CA  B MET B 153 ? 0.1057 0.0908 0.1096 0.0201  0.0053  0.0061  376 MET B CA  
7582  C C   . MET B 153 ? 0.0871 0.0737 0.0876 0.0235  -0.0052 -0.0004 376 MET B C   
7583  O O   . MET B 153 ? 0.1147 0.0771 0.1087 0.0259  -0.0041 -0.0248 376 MET B O   
7584  C CB  A MET B 153 ? 0.1099 0.1039 0.1229 0.0094  0.0012  0.0060  376 MET B CB  
7585  C CB  B MET B 153 ? 0.1215 0.1589 0.1609 0.0281  0.0135  0.0474  376 MET B CB  
7586  C CG  A MET B 153 ? 0.1410 0.1368 0.1482 0.0074  0.0066  0.0191  376 MET B CG  
7587  C CG  B MET B 153 ? 0.1502 0.2226 0.2091 0.0349  0.0254  0.0845  376 MET B CG  
7588  S SD  A MET B 153 ? 0.1849 0.1591 0.1713 -0.0024 0.0069  0.0126  376 MET B SD  
7589  S SD  B MET B 153 ? 0.1950 0.2826 0.2641 0.0386  0.0472  0.1137  376 MET B SD  
7590  C CE  A MET B 153 ? 0.1863 0.1650 0.1934 -0.0267 0.0154  0.0015  376 MET B CE  
7591  C CE  B MET B 153 ? 0.2098 0.2912 0.2749 0.0223  0.0687  0.1035  376 MET B CE  
7610  N N   . ILE B 154 ? 0.0829 0.0758 0.1037 0.0175  -0.0018 -0.0004 377 ILE B N   
7611  C CA  . ILE B 154 ? 0.0710 0.0725 0.0922 0.0074  -0.0135 -0.0049 377 ILE B CA  
7612  C C   . ILE B 154 ? 0.0769 0.0542 0.0972 -0.0062 -0.0007 -0.0026 377 ILE B C   
7613  O O   . ILE B 154 ? 0.1024 0.0807 0.1070 -0.0050 0.0123  -0.0148 377 ILE B O   
7614  C CB  . ILE B 154 ? 0.0915 0.0745 0.0963 -0.0025 -0.0136 0.0007  377 ILE B CB  
7615  C CG1 . ILE B 154 ? 0.0935 0.0699 0.0998 0.0021  -0.0164 0.0115  377 ILE B CG1 
7616  C CG2 . ILE B 154 ? 0.1055 0.0864 0.0886 -0.0021 0.0010  0.0102  377 ILE B CG2 
7617  C CD1 . ILE B 154 ? 0.1133 0.0865 0.1143 0.0021  0.0054  0.0223  377 ILE B CD1 
7629  N N   . GLY B 155 ? 0.0794 0.0557 0.0849 0.0048  0.0127  -0.0057 378 GLY B N   
7630  C CA  . GLY B 155 ? 0.0685 0.0735 0.0951 0.0040  0.0081  0.0030  378 GLY B CA  
7631  C C   . GLY B 155 ? 0.0694 0.0799 0.1049 -0.0010 0.0177  0.0048  378 GLY B C   
7632  O O   . GLY B 155 ? 0.0772 0.0949 0.0967 0.0239  0.0124  -0.0030 378 GLY B O   
7636  N N   . THR B 156 ? 0.0560 0.0801 0.0976 0.0165  0.0080  0.0022  379 THR B N   
7637  C CA  . THR B 156 ? 0.0603 0.0726 0.1157 0.0054  0.0034  -0.0021 379 THR B CA  
7638  C C   . THR B 156 ? 0.0698 0.0663 0.1168 0.0061  0.0041  -0.0008 379 THR B C   
7639  O O   . THR B 156 ? 0.0695 0.0824 0.1346 0.0025  0.0042  0.0036  379 THR B O   
7640  C CB  . THR B 156 ? 0.0782 0.0776 0.1050 -0.0081 0.0129  -0.0075 379 THR B CB  
7641  O OG1 . THR B 156 ? 0.0661 0.0857 0.1158 -0.0037 0.0223  -0.0135 379 THR B OG1 
7642  C CG2 . THR B 156 ? 0.0867 0.0757 0.1041 -0.0057 0.0083  0.0057  379 THR B CG2 
7650  N N   . TRP B 157 ? 0.0792 0.0692 0.1198 0.0099  0.0016  0.0010  380 TRP B N   
7651  C CA  . TRP B 157 ? 0.0852 0.0807 0.1550 -0.0074 0.0052  -0.0083 380 TRP B CA  
7652  C C   . TRP B 157 ? 0.0878 0.0785 0.1638 -0.0139 0.0032  -0.0063 380 TRP B C   
7653  O O   . TRP B 157 ? 0.0995 0.0948 0.1665 0.0025  0.0221  0.0010  380 TRP B O   
7654  C CB  . TRP B 157 ? 0.0866 0.0736 0.1701 -0.0093 0.0044  -0.0043 380 TRP B CB  
7655  C CG  . TRP B 157 ? 0.0956 0.0702 0.1566 -0.0007 0.0065  -0.0092 380 TRP B CG  
7656  C CD1 . TRP B 157 ? 0.1299 0.0786 0.1878 0.0001  0.0290  -0.0085 380 TRP B CD1 
7657  C CD2 . TRP B 157 ? 0.1195 0.0744 0.1504 0.0081  0.0110  0.0073  380 TRP B CD2 
7658  N NE1 . TRP B 157 ? 0.1404 0.0708 0.1734 -0.0029 0.0257  -0.0127 380 TRP B NE1 
7659  C CE2 . TRP B 157 ? 0.1304 0.0747 0.1665 0.0040  0.0138  0.0039  380 TRP B CE2 
7660  C CE3 . TRP B 157 ? 0.1513 0.0872 0.1400 0.0107  0.0164  0.0221  380 TRP B CE3 
7661  C CZ2 . TRP B 157 ? 0.1551 0.0900 0.1699 0.0082  0.0200  0.0167  380 TRP B CZ2 
7662  C CZ3 . TRP B 157 ? 0.1761 0.1077 0.1672 -0.0007 0.0319  0.0301  380 TRP B CZ3 
7663  C CH2 . TRP B 157 ? 0.1814 0.0991 0.1757 0.0053  0.0473  0.0216  380 TRP B CH2 
7674  N N   A THR B 158 ? 0.0795 0.0774 0.1814 0.0067  0.0002  -0.0181 381 THR B N   
7675  C CA  A THR B 158 ? 0.0922 0.0901 0.2083 0.0141  0.0179  0.0016  381 THR B CA  
7676  C C   A THR B 158 ? 0.0971 0.0779 0.1887 0.0024  0.0083  0.0011  381 THR B C   
7677  O O   A THR B 158 ? 0.1231 0.0905 0.2068 0.0093  0.0391  0.0125  381 THR B O   
7678  C CB  A THR B 158 ? 0.0952 0.1349 0.2651 -0.0158 -0.0050 -0.0118 381 THR B CB  
7679  O OG1 A THR B 158 ? 0.1222 0.1840 0.2911 -0.0104 -0.0399 -0.0027 381 THR B OG1 
7680  C CG2 A THR B 158 ? 0.1094 0.1353 0.2968 -0.0318 -0.0046 -0.0124 381 THR B CG2 
7688  N N   . THR B 159 ? 0.0965 0.0754 0.1564 0.0041  0.0050  0.0018  382 THR B N   
7689  C CA  . THR B 159 ? 0.1044 0.0882 0.1488 0.0189  0.0073  0.0060  382 THR B CA  
7690  C C   . THR B 159 ? 0.0812 0.0884 0.1582 0.0167  0.0149  0.0045  382 THR B C   
7691  O O   . THR B 159 ? 0.0890 0.0985 0.1705 0.0171  0.0193  -0.0142 382 THR B O   
7692  C CB  . THR B 159 ? 0.1764 0.1127 0.1370 0.0120  0.0212  0.0032  382 THR B CB  
7693  O OG1 . THR B 159 ? 0.2440 0.1474 0.1383 0.0065  0.0369  -0.0061 382 THR B OG1 
7694  C CG2 . THR B 159 ? 0.1869 0.1061 0.1439 0.0176  0.0428  0.0115  382 THR B CG2 
7702  N N   . ASP B 160 ? 0.0733 0.0912 0.1648 0.0191  0.0172  -0.0052 383 ASP B N   
7703  C CA  . ASP B 160 ? 0.1095 0.1044 0.1579 0.0062  0.0238  -0.0015 383 ASP B CA  
7704  C C   . ASP B 160 ? 0.0914 0.0973 0.1476 -0.0029 0.0123  -0.0040 383 ASP B C   
7705  O O   . ASP B 160 ? 0.1128 0.1103 0.1371 0.0080  0.0143  0.0017  383 ASP B O   
7706  C CB  . ASP B 160 ? 0.1724 0.1495 0.1825 -0.0166 0.0626  -0.0260 383 ASP B CB  
7707  C CG  . ASP B 160 ? 0.1698 0.2058 0.2344 0.0047  0.0952  -0.0523 383 ASP B CG  
7708  O OD1 . ASP B 160 ? 0.1490 0.2259 0.2620 0.0439  0.0445  -0.0376 383 ASP B OD1 
7709  O OD2 . ASP B 160 ? 0.2301 0.2638 0.2913 -0.0117 0.1458  -0.0485 383 ASP B OD2 
7714  N N   . ASP B 161 ? 0.0929 0.0899 0.1271 0.0069  0.0021  -0.0035 384 ASP B N   
7715  C CA  . ASP B 161 ? 0.0939 0.0823 0.1266 -0.0018 0.0250  -0.0107 384 ASP B CA  
7716  C C   . ASP B 161 ? 0.0901 0.0727 0.1179 0.0009  0.0198  -0.0101 384 ASP B C   
7717  O O   . ASP B 161 ? 0.0883 0.0810 0.1168 0.0001  0.0149  -0.0094 384 ASP B O   
7718  C CB  . ASP B 161 ? 0.1020 0.0927 0.1378 -0.0047 0.0091  -0.0005 384 ASP B CB  
7719  C CG  . ASP B 161 ? 0.1104 0.0887 0.1494 0.0155  0.0043  -0.0081 384 ASP B CG  
7720  O OD1 . ASP B 161 ? 0.1328 0.0921 0.1849 0.0236  0.0271  -0.0163 384 ASP B OD1 
7721  O OD2 . ASP B 161 ? 0.1336 0.0802 0.1678 0.0127  0.0186  -0.0006 384 ASP B OD2 
7726  N N   . ILE B 162 ? 0.0810 0.0769 0.1239 -0.0183 0.0148  -0.0105 385 ILE B N   
7727  C CA  . ILE B 162 ? 0.0772 0.0616 0.1071 -0.0026 0.0042  -0.0036 385 ILE B CA  
7728  C C   . ILE B 162 ? 0.0820 0.0660 0.1070 -0.0001 0.0111  0.0040  385 ILE B C   
7729  O O   . ILE B 162 ? 0.1249 0.0876 0.1155 -0.0104 0.0200  -0.0060 385 ILE B O   
7730  C CB  . ILE B 162 ? 0.0846 0.0769 0.1191 0.0031  -0.0057 -0.0104 385 ILE B CB  
7731  C CG1 . ILE B 162 ? 0.1011 0.0856 0.1279 0.0190  -0.0089 -0.0033 385 ILE B CG1 
7732  C CG2 . ILE B 162 ? 0.0910 0.0754 0.1133 0.0234  0.0089  -0.0045 385 ILE B CG2 
7733  C CD1 . ILE B 162 ? 0.1014 0.0994 0.1291 0.0272  -0.0252 -0.0064 385 ILE B CD1 
7745  N N   . LYS B 163 ? 0.0854 0.0670 0.1011 0.0000  0.0023  -0.0011 386 LYS B N   
7746  C CA  . LYS B 163 ? 0.0815 0.0652 0.0931 0.0015  -0.0021 -0.0189 386 LYS B CA  
7747  C C   . LYS B 163 ? 0.0731 0.0743 0.0797 0.0049  -0.0058 -0.0053 386 LYS B C   
7748  O O   . LYS B 163 ? 0.0826 0.0737 0.1024 0.0121  0.0028  -0.0087 386 LYS B O   
7749  C CB  . LYS B 163 ? 0.0902 0.0623 0.0930 0.0212  -0.0117 -0.0114 386 LYS B CB  
7750  C CG  . LYS B 163 ? 0.1282 0.0791 0.0917 0.0271  -0.0117 -0.0022 386 LYS B CG  
7751  C CD  . LYS B 163 ? 0.1233 0.0907 0.1299 0.0327  -0.0204 -0.0019 386 LYS B CD  
7752  C CE  . LYS B 163 ? 0.1091 0.0916 0.1470 0.0153  -0.0163 -0.0045 386 LYS B CE  
7753  N NZ  . LYS B 163 ? 0.1243 0.0901 0.1496 0.0116  -0.0150 -0.0146 386 LYS B NZ  
7767  N N   . ASN B 164 ? 0.0882 0.0689 0.0672 0.0139  -0.0033 -0.0066 387 ASN B N   
7768  C CA  . ASN B 164 ? 0.0995 0.0727 0.0898 0.0267  -0.0143 -0.0051 387 ASN B CA  
7769  C C   . ASN B 164 ? 0.0902 0.0687 0.0890 0.0205  -0.0106 -0.0201 387 ASN B C   
7770  O O   . ASN B 164 ? 0.1101 0.0906 0.0995 0.0062  -0.0036 -0.0257 387 ASN B O   
7771  C CB  . ASN B 164 ? 0.1102 0.0795 0.0950 0.0249  -0.0118 -0.0075 387 ASN B CB  
7772  C CG  . ASN B 164 ? 0.1604 0.0961 0.0854 0.0053  0.0039  -0.0052 387 ASN B CG  
7773  O OD1 . ASN B 164 ? 0.1959 0.0957 0.1147 0.0084  0.0389  -0.0015 387 ASN B OD1 
7774  N ND2 . ASN B 164 ? 0.2159 0.1136 0.1052 -0.0208 0.0395  -0.0023 387 ASN B ND2 
7781  N N   . GLN B 165 ? 0.0824 0.0538 0.0842 0.0161  -0.0207 -0.0124 388 GLN B N   
7782  C CA  . GLN B 165 ? 0.0646 0.0513 0.0926 0.0240  -0.0137 -0.0063 388 GLN B CA  
7783  C C   . GLN B 165 ? 0.0761 0.0610 0.0837 0.0143  -0.0160 -0.0089 388 GLN B C   
7784  O O   . GLN B 165 ? 0.0765 0.0602 0.0910 0.0195  -0.0030 0.0011  388 GLN B O   
7785  C CB  . GLN B 165 ? 0.0664 0.0539 0.1044 0.0143  -0.0093 -0.0126 388 GLN B CB  
7786  C CG  . GLN B 165 ? 0.0915 0.0746 0.1071 0.0164  -0.0016 -0.0014 388 GLN B CG  
7787  C CD  . GLN B 165 ? 0.0883 0.0801 0.1146 0.0127  0.0044  -0.0128 388 GLN B CD  
7788  O OE1 . GLN B 165 ? 0.0891 0.0733 0.1079 0.0123  0.0029  -0.0021 388 GLN B OE1 
7789  N NE2 . GLN B 165 ? 0.1325 0.0918 0.1752 0.0090  0.0584  -0.0422 388 GLN B NE2 
7798  N N   . PRO B 166 ? 0.0685 0.0536 0.0992 0.0094  -0.0153 -0.0252 389 PRO B N   
7799  C CA  . PRO B 166 ? 0.0707 0.0620 0.0929 0.0041  -0.0146 -0.0218 389 PRO B CA  
7800  C C   . PRO B 166 ? 0.0674 0.0676 0.0850 0.0222  -0.0165 -0.0118 389 PRO B C   
7801  O O   . PRO B 166 ? 0.0738 0.0647 0.1065 0.0257  -0.0220 -0.0121 389 PRO B O   
7802  C CB  . PRO B 166 ? 0.0842 0.0664 0.1043 -0.0066 -0.0140 -0.0260 389 PRO B CB  
7803  C CG  . PRO B 166 ? 0.1004 0.0725 0.1080 -0.0046 -0.0011 -0.0102 389 PRO B CG  
7804  C CD  . PRO B 166 ? 0.0904 0.0551 0.1006 0.0041  -0.0066 -0.0078 389 PRO B CD  
7812  N N   . SER B 167 ? 0.0627 0.0576 0.0947 0.0085  -0.0228 -0.0216 390 SER B N   
7813  C CA  . SER B 167 ? 0.0728 0.0643 0.0810 0.0149  -0.0141 -0.0112 390 SER B CA  
7814  C C   . SER B 167 ? 0.0664 0.0635 0.0897 0.0056  -0.0234 -0.0065 390 SER B C   
7815  O O   . SER B 167 ? 0.0628 0.0826 0.1053 0.0166  -0.0252 -0.0245 390 SER B O   
7816  C CB  . SER B 167 ? 0.0825 0.0731 0.1037 -0.0040 0.0009  -0.0184 390 SER B CB  
7817  O OG  . SER B 167 ? 0.0857 0.0772 0.1121 -0.0040 0.0095  -0.0219 390 SER B OG  
7823  N N   . LYS B 168 ? 0.0746 0.0563 0.0891 0.0153  -0.0105 -0.0111 391 LYS B N   
7824  C CA  A LYS B 168 ? 0.0773 0.0743 0.0903 0.0091  0.0031  -0.0184 391 LYS B CA  
7825  C CA  B LYS B 168 ? 0.0796 0.0760 0.0919 0.0155  -0.0064 -0.0105 391 LYS B CA  
7826  C C   . LYS B 168 ? 0.0627 0.0680 0.0865 0.0129  -0.0251 -0.0190 391 LYS B C   
7827  O O   . LYS B 168 ? 0.0645 0.0835 0.1216 0.0167  -0.0324 -0.0325 391 LYS B O   
7828  C CB  A LYS B 168 ? 0.1114 0.0980 0.1146 -0.0171 0.0366  -0.0203 391 LYS B CB  
7829  C CB  B LYS B 168 ? 0.1188 0.1025 0.1213 0.0022  0.0082  0.0040  391 LYS B CB  
7830  C CG  A LYS B 168 ? 0.1160 0.1223 0.1270 -0.0252 0.0408  -0.0263 391 LYS B CG  
7831  C CG  B LYS B 168 ? 0.1199 0.1244 0.1243 0.0153  -0.0191 0.0203  391 LYS B CG  
7832  C CD  A LYS B 168 ? 0.1052 0.1516 0.1273 -0.0141 0.0339  -0.0366 391 LYS B CD  
7833  C CD  B LYS B 168 ? 0.1382 0.1517 0.1383 0.0376  -0.0017 0.0230  391 LYS B CD  
7834  C CE  A LYS B 168 ? 0.0742 0.1640 0.1272 0.0079  0.0160  -0.0283 391 LYS B CE  
7835  C CE  B LYS B 168 ? 0.1542 0.1555 0.1719 0.0263  0.0086  0.0258  391 LYS B CE  
7836  N NZ  A LYS B 168 ? 0.0562 0.1714 0.1133 0.0232  -0.0060 -0.0516 391 LYS B NZ  
7837  N NZ  B LYS B 168 ? 0.1471 0.1696 0.2093 0.0143  -0.0073 0.0595  391 LYS B NZ  
7862  N N   . PHE B 169 ? 0.0598 0.0565 0.1044 0.0110  -0.0167 -0.0170 392 PHE B N   
7863  C CA  . PHE B 169 ? 0.0534 0.0657 0.0937 0.0111  -0.0094 -0.0137 392 PHE B CA  
7864  C C   . PHE B 169 ? 0.0488 0.0693 0.1062 -0.0016 -0.0072 -0.0190 392 PHE B C   
7865  O O   . PHE B 169 ? 0.0511 0.0770 0.1233 -0.0058 -0.0009 -0.0281 392 PHE B O   
7866  C CB  . PHE B 169 ? 0.0681 0.0725 0.1067 0.0196  -0.0244 -0.0071 392 PHE B CB  
7867  C CG  . PHE B 169 ? 0.0765 0.0688 0.0970 -0.0008 -0.0219 -0.0013 392 PHE B CG  
7868  C CD1 . PHE B 169 ? 0.0760 0.0842 0.1094 -0.0002 -0.0299 0.0000  392 PHE B CD1 
7869  C CD2 . PHE B 169 ? 0.0850 0.0763 0.1051 -0.0049 -0.0113 -0.0037 392 PHE B CD2 
7870  C CE1 . PHE B 169 ? 0.0737 0.0841 0.1173 0.0105  -0.0369 0.0159  392 PHE B CE1 
7871  C CE2 . PHE B 169 ? 0.0968 0.0757 0.0865 0.0046  -0.0049 -0.0048 392 PHE B CE2 
7872  C CZ  . PHE B 169 ? 0.0980 0.0701 0.1191 0.0125  -0.0193 0.0219  392 PHE B CZ  
7882  N N   . THR B 170 ? 0.0756 0.0676 0.0955 -0.0027 -0.0033 -0.0202 393 THR B N   
7883  C CA  . THR B 170 ? 0.0763 0.0733 0.0889 -0.0145 -0.0025 -0.0114 393 THR B CA  
7884  C C   . THR B 170 ? 0.0613 0.0715 0.0890 -0.0025 0.0066  -0.0131 393 THR B C   
7885  O O   . THR B 170 ? 0.0629 0.0698 0.0853 -0.0054 0.0076  0.0023  393 THR B O   
7886  C CB  . THR B 170 ? 0.1576 0.0774 0.1069 -0.0323 0.0185  -0.0111 393 THR B CB  
7887  O OG1 . THR B 170 ? 0.2438 0.0919 0.1325 -0.0324 0.0648  -0.0134 393 THR B OG1 
7888  C CG2 . THR B 170 ? 0.1751 0.0840 0.0985 -0.0128 0.0243  0.0091  393 THR B CG2 
7896  N N   . PRO B 171 ? 0.0617 0.0637 0.0884 -0.0003 -0.0089 0.0006  394 PRO B N   
7897  C CA  . PRO B 171 ? 0.0597 0.0562 0.0883 0.0079  -0.0080 -0.0013 394 PRO B CA  
7898  C C   . PRO B 171 ? 0.0631 0.0618 0.0823 -0.0031 0.0016  0.0017  394 PRO B C   
7899  O O   . PRO B 171 ? 0.0760 0.0741 0.0799 -0.0027 0.0011  0.0028  394 PRO B O   
7900  C CB  . PRO B 171 ? 0.0844 0.0818 0.1021 0.0121  -0.0089 -0.0041 394 PRO B CB  
7901  C CG  . PRO B 171 ? 0.0695 0.1069 0.1188 0.0196  -0.0008 -0.0119 394 PRO B CG  
7902  C CD  . PRO B 171 ? 0.0737 0.1021 0.1007 -0.0030 -0.0044 -0.0139 394 PRO B CD  
7910  N N   . ILE B 172 ? 0.0664 0.0603 0.0710 -0.0090 -0.0012 -0.0002 395 ILE B N   
7911  C CA  . ILE B 172 ? 0.0564 0.0618 0.0746 -0.0088 -0.0164 0.0063  395 ILE B CA  
7912  C C   . ILE B 172 ? 0.0520 0.0558 0.0890 -0.0061 -0.0081 -0.0005 395 ILE B C   
7913  O O   . ILE B 172 ? 0.0949 0.0570 0.0879 -0.0032 -0.0011 -0.0013 395 ILE B O   
7914  C CB  . ILE B 172 ? 0.0630 0.0662 0.1006 0.0097  -0.0172 0.0155  395 ILE B CB  
7915  C CG1 . ILE B 172 ? 0.0977 0.0752 0.1365 0.0208  -0.0021 0.0182  395 ILE B CG1 
7916  C CG2 . ILE B 172 ? 0.0730 0.1065 0.1270 0.0154  -0.0124 0.0059  395 ILE B CG2 
7917  C CD1 . ILE B 172 ? 0.1027 0.0893 0.1321 0.0049  -0.0143 0.0246  395 ILE B CD1 
7929  N N   . GLY B 173 ? 0.0607 0.0426 0.0897 -0.0042 -0.0051 -0.0003 396 GLY B N   
7930  C CA  . GLY B 173 ? 0.0586 0.0521 0.0825 -0.0088 -0.0073 -0.0118 396 GLY B CA  
7931  C C   . GLY B 173 ? 0.0568 0.0545 0.0746 -0.0005 -0.0041 -0.0070 396 GLY B C   
7932  O O   . GLY B 173 ? 0.0560 0.0583 0.0846 0.0101  -0.0046 -0.0094 396 GLY B O   
7936  N N   . LEU B 174 ? 0.0500 0.0588 0.0723 -0.0120 -0.0034 0.0055  397 LEU B N   
7937  C CA  . LEU B 174 ? 0.0519 0.0546 0.0739 0.0029  -0.0061 0.0053  397 LEU B CA  
7938  C C   . LEU B 174 ? 0.0570 0.0590 0.0723 0.0015  -0.0072 -0.0064 397 LEU B C   
7939  O O   . LEU B 174 ? 0.0548 0.0748 0.0849 0.0047  -0.0197 -0.0012 397 LEU B O   
7940  C CB  . LEU B 174 ? 0.0574 0.0631 0.0800 0.0034  -0.0057 0.0097  397 LEU B CB  
7941  C CG  . LEU B 174 ? 0.0771 0.0769 0.0865 0.0065  -0.0080 -0.0009 397 LEU B CG  
7942  C CD1 . LEU B 174 ? 0.0860 0.0937 0.1214 0.0205  -0.0062 -0.0090 397 LEU B CD1 
7943  C CD2 . LEU B 174 ? 0.0693 0.0971 0.1176 0.0105  -0.0280 -0.0079 397 LEU B CD2 
7955  N N   . ASN B 175 ? 0.0568 0.0706 0.0781 -0.0010 0.0032  -0.0035 398 ASN B N   
7956  C CA  . ASN B 175 ? 0.0503 0.0805 0.0989 0.0039  0.0100  -0.0010 398 ASN B CA  
7957  C C   . ASN B 175 ? 0.0493 0.0792 0.0985 -0.0113 -0.0023 -0.0006 398 ASN B C   
7958  O O   . ASN B 175 ? 0.0772 0.0852 0.1265 -0.0152 0.0124  0.0089  398 ASN B O   
7959  C CB  . ASN B 175 ? 0.0646 0.0741 0.1030 0.0030  0.0018  -0.0006 398 ASN B CB  
7960  C CG  . ASN B 175 ? 0.0764 0.0791 0.0935 0.0005  0.0174  0.0008  398 ASN B CG  
7961  O OD1 . ASN B 175 ? 0.0735 0.0862 0.1195 0.0119  0.0085  0.0195  398 ASN B OD1 
7962  N ND2 . ASN B 175 ? 0.0870 0.1041 0.0937 -0.0078 0.0157  0.0020  398 ASN B ND2 
7969  N N   . ASP B 176 ? 0.0635 0.0665 0.0987 -0.0098 0.0007  -0.0026 399 ASP B N   
7970  C CA  . ASP B 176 ? 0.0795 0.0837 0.0987 -0.0024 0.0019  0.0011  399 ASP B CA  
7971  C C   . ASP B 176 ? 0.0797 0.0821 0.0851 -0.0126 -0.0091 0.0027  399 ASP B C   
7972  O O   . ASP B 176 ? 0.0791 0.0761 0.1064 -0.0150 -0.0180 0.0094  399 ASP B O   
7973  C CB  . ASP B 176 ? 0.1018 0.1135 0.1199 -0.0196 0.0302  -0.0075 399 ASP B CB  
7974  C CG  . ASP B 176 ? 0.0841 0.1366 0.0957 -0.0329 0.0196  0.0040  399 ASP B CG  
7975  O OD1 . ASP B 176 ? 0.1016 0.1382 0.1129 -0.0178 0.0107  0.0231  399 ASP B OD1 
7976  O OD2 . ASP B 176 ? 0.1196 0.1851 0.1309 -0.0205 0.0235  0.0121  399 ASP B OD2 
7981  N N   . ASP B 177 ? 0.0789 0.0731 0.1115 -0.0146 -0.0128 0.0110  400 ASP B N   
7982  C CA  . ASP B 177 ? 0.0857 0.0777 0.1302 -0.0167 -0.0081 0.0006  400 ASP B CA  
7983  C C   . ASP B 177 ? 0.0771 0.0858 0.1249 -0.0071 -0.0169 0.0145  400 ASP B C   
7984  O O   . ASP B 177 ? 0.0898 0.1048 0.1287 0.0043  -0.0034 0.0193  400 ASP B O   
7985  C CB  . ASP B 177 ? 0.1238 0.0975 0.1113 -0.0099 0.0008  0.0030  400 ASP B CB  
7986  C CG  . ASP B 177 ? 0.1034 0.1215 0.1554 -0.0232 -0.0066 -0.0183 400 ASP B CG  
7987  O OD1 . ASP B 177 ? 0.1452 0.1651 0.2141 -0.0401 0.0458  -0.0547 400 ASP B OD1 
7988  O OD2 . ASP B 177 ? 0.1210 0.1210 0.1723 -0.0140 0.0335  -0.0215 400 ASP B OD2 
7993  N N   . ASP B 178 ? 0.0973 0.0944 0.1448 -0.0079 -0.0127 0.0339  401 ASP B N   
7994  C CA  . ASP B 178 ? 0.0837 0.1122 0.1664 -0.0009 -0.0112 0.0410  401 ASP B CA  
7995  C C   . ASP B 178 ? 0.0861 0.1332 0.1779 0.0108  -0.0184 0.0503  401 ASP B C   
7996  O O   . ASP B 178 ? 0.1031 0.1514 0.2093 0.0030  -0.0395 0.0595  401 ASP B O   
7997  C CB  . ASP B 178 ? 0.0949 0.1172 0.1653 -0.0042 0.0027  0.0468  401 ASP B CB  
7998  C CG  . ASP B 178 ? 0.1179 0.1273 0.1841 -0.0091 0.0035  0.0441  401 ASP B CG  
7999  O OD1 . ASP B 178 ? 0.1454 0.1352 0.1859 -0.0227 0.0192  0.0152  401 ASP B OD1 
8000  O OD2 . ASP B 178 ? 0.1238 0.1322 0.2089 -0.0093 0.0057  0.0325  401 ASP B OD2 
8005  N N   . ASN B 179 ? 0.0792 0.1377 0.1326 0.0123  -0.0179 0.0355  402 ASN B N   
8006  C CA  . ASN B 179 ? 0.0897 0.1605 0.1301 0.0071  -0.0057 0.0308  402 ASN B CA  
8007  C C   . ASN B 179 ? 0.0961 0.1567 0.1183 -0.0050 -0.0048 0.0054  402 ASN B C   
8008  O O   . ASN B 179 ? 0.1262 0.1961 0.1228 -0.0286 0.0174  0.0037  402 ASN B O   
8009  C CB  . ASN B 179 ? 0.1186 0.1946 0.1420 0.0094  0.0041  0.0535  402 ASN B CB  
8010  C CG  . ASN B 179 ? 0.1401 0.2340 0.1678 0.0042  0.0349  0.0704  402 ASN B CG  
8011  O OD1 . ASN B 179 ? 0.1646 0.2597 0.1952 0.0179  0.0509  0.1057  402 ASN B OD1 
8012  N ND2 . ASN B 179 ? 0.1353 0.2515 0.1631 -0.0021 0.0388  0.0569  402 ASN B ND2 
8019  N N   . PHE B 180 ? 0.0686 0.1167 0.0934 0.0053  0.0046  0.0017  403 PHE B N   
8020  C CA  . PHE B 180 ? 0.0569 0.1040 0.1050 0.0025  0.0014  -0.0037 403 PHE B CA  
8021  C C   . PHE B 180 ? 0.0732 0.0811 0.0908 -0.0033 -0.0016 -0.0022 403 PHE B C   
8022  O O   . PHE B 180 ? 0.0825 0.0964 0.1055 -0.0115 -0.0125 -0.0156 403 PHE B O   
8023  C CB  . PHE B 180 ? 0.0636 0.1040 0.1129 0.0021  -0.0110 0.0060  403 PHE B CB  
8024  C CG  . PHE B 180 ? 0.0683 0.0912 0.0972 0.0188  -0.0085 0.0167  403 PHE B CG  
8025  C CD1 . PHE B 180 ? 0.0689 0.1068 0.0979 0.0088  -0.0060 -0.0122 403 PHE B CD1 
8026  C CD2 . PHE B 180 ? 0.0674 0.0832 0.1088 0.0179  -0.0104 -0.0018 403 PHE B CD2 
8027  C CE1 . PHE B 180 ? 0.0712 0.1073 0.1102 0.0150  0.0009  0.0105  403 PHE B CE1 
8028  C CE2 . PHE B 180 ? 0.0800 0.0963 0.1064 0.0377  -0.0001 0.0223  403 PHE B CE2 
8029  C CZ  . PHE B 180 ? 0.0787 0.0977 0.1159 0.0203  0.0046  0.0228  403 PHE B CZ  
8039  N N   . LYS B 181 ? 0.0602 0.0848 0.0823 0.0001  -0.0149 -0.0156 404 LYS B N   
8040  C CA  . LYS B 181 ? 0.0669 0.0783 0.1024 -0.0018 -0.0344 -0.0008 404 LYS B CA  
8041  C C   . LYS B 181 ? 0.0676 0.0696 0.0908 -0.0047 -0.0179 -0.0116 404 LYS B C   
8042  O O   . LYS B 181 ? 0.0729 0.0822 0.0833 -0.0021 -0.0125 0.0032  404 LYS B O   
8043  C CB  . LYS B 181 ? 0.1047 0.0875 0.1360 0.0039  -0.0011 0.0157  404 LYS B CB  
8044  C CG  . LYS B 181 ? 0.1432 0.1254 0.1554 -0.0036 0.0080  0.0345  404 LYS B CG  
8045  C CD  . LYS B 181 ? 0.2078 0.1797 0.2119 -0.0480 0.0284  0.0408  404 LYS B CD  
8046  C CE  . LYS B 181 ? 0.2803 0.2224 0.2873 -0.0417 0.0398  0.0325  404 LYS B CE  
8047  N NZ  . LYS B 181 ? 0.3258 0.2467 0.3342 -0.0356 0.0390  0.0221  404 LYS B NZ  
8061  N N   . GLN B 182 ? 0.0661 0.0587 0.0886 0.0014  -0.0074 -0.0039 405 GLN B N   
8062  C CA  . GLN B 182 ? 0.0450 0.0625 0.0803 0.0008  -0.0087 0.0018  405 GLN B CA  
8063  C C   . GLN B 182 ? 0.0789 0.0707 0.0761 -0.0074 0.0027  0.0011  405 GLN B C   
8064  O O   . GLN B 182 ? 0.0900 0.0713 0.0883 -0.0097 -0.0027 0.0107  405 GLN B O   
8065  C CB  . GLN B 182 ? 0.0524 0.0708 0.0897 0.0000  -0.0090 -0.0022 405 GLN B CB  
8066  C CG  . GLN B 182 ? 0.0647 0.0698 0.0959 -0.0046 -0.0113 -0.0023 405 GLN B CG  
8067  C CD  . GLN B 182 ? 0.0669 0.0607 0.0946 0.0102  -0.0082 0.0047  405 GLN B CD  
8068  O OE1 . GLN B 182 ? 0.0771 0.0670 0.0892 0.0012  -0.0097 0.0071  405 GLN B OE1 
8069  N NE2 . GLN B 182 ? 0.0810 0.0743 0.0852 -0.0055 -0.0093 0.0006  405 GLN B NE2 
8078  N N   . TRP B 183 ? 0.0660 0.0652 0.0927 0.0175  -0.0015 -0.0018 406 TRP B N   
8079  C CA  . TRP B 183 ? 0.0840 0.0855 0.1073 0.0236  -0.0111 -0.0023 406 TRP B CA  
8080  C C   . TRP B 183 ? 0.0838 0.1262 0.0878 0.0291  -0.0168 0.0061  406 TRP B C   
8081  O O   . TRP B 183 ? 0.1157 0.2143 0.1053 0.0783  -0.0257 -0.0183 406 TRP B O   
8082  C CB  . TRP B 183 ? 0.1056 0.0914 0.1214 0.0367  0.0024  -0.0006 406 TRP B CB  
8083  C CG  . TRP B 183 ? 0.0946 0.0798 0.1086 0.0220  -0.0013 -0.0073 406 TRP B CG  
8084  C CD1 . TRP B 183 ? 0.1109 0.0798 0.1179 0.0190  0.0167  0.0025  406 TRP B CD1 
8085  C CD2 . TRP B 183 ? 0.0801 0.0842 0.0991 0.0191  -0.0143 -0.0023 406 TRP B CD2 
8086  N NE1 . TRP B 183 ? 0.1150 0.0882 0.1097 0.0083  -0.0102 -0.0059 406 TRP B NE1 
8087  C CE2 . TRP B 183 ? 0.0964 0.0848 0.0980 0.0246  -0.0122 -0.0089 406 TRP B CE2 
8088  C CE3 . TRP B 183 ? 0.0654 0.1050 0.1173 0.0107  -0.0118 -0.0056 406 TRP B CE3 
8089  C CZ2 . TRP B 183 ? 0.0971 0.0995 0.0920 0.0218  -0.0215 -0.0092 406 TRP B CZ2 
8090  C CZ3 . TRP B 183 ? 0.0779 0.1141 0.1211 0.0155  -0.0070 -0.0088 406 TRP B CZ3 
8091  C CH2 . TRP B 183 ? 0.0962 0.1001 0.1192 0.0130  -0.0093 0.0064  406 TRP B CH2 
8102  N N   . GLU B 184 ? 0.0839 0.0807 0.0921 0.0068  -0.0124 0.0036  407 GLU B N   
8103  C CA  . GLU B 184 ? 0.0757 0.0771 0.0985 0.0160  -0.0078 0.0020  407 GLU B CA  
8104  C C   . GLU B 184 ? 0.0781 0.0735 0.0877 0.0242  -0.0153 -0.0058 407 GLU B C   
8105  O O   . GLU B 184 ? 0.0763 0.0772 0.1252 0.0175  -0.0177 -0.0062 407 GLU B O   
8106  C CB  . GLU B 184 ? 0.0847 0.0884 0.1062 0.0119  -0.0020 0.0095  407 GLU B CB  
8107  C CG  . GLU B 184 ? 0.0994 0.1017 0.1332 0.0045  0.0035  0.0056  407 GLU B CG  
8108  C CD  . GLU B 184 ? 0.1354 0.1179 0.1554 -0.0064 0.0035  -0.0032 407 GLU B CD  
8109  O OE1 . GLU B 184 ? 0.1367 0.1353 0.1615 -0.0120 0.0158  0.0155  407 GLU B OE1 
8110  O OE2 . GLU B 184 ? 0.1790 0.1342 0.2075 -0.0141 0.0389  0.0072  407 GLU B OE2 
8117  N N   . LEU B 185 ? 0.0786 0.0766 0.0959 0.0260  -0.0218 -0.0024 408 LEU B N   
8118  C CA  . LEU B 185 ? 0.0789 0.0866 0.0835 0.0109  -0.0153 -0.0002 408 LEU B CA  
8119  C C   . LEU B 185 ? 0.0700 0.0850 0.0915 0.0000  -0.0071 0.0015  408 LEU B C   
8120  O O   . LEU B 185 ? 0.0965 0.0874 0.1099 0.0034  0.0150  0.0014  408 LEU B O   
8121  C CB  . LEU B 185 ? 0.0743 0.1007 0.0898 0.0039  -0.0188 0.0059  408 LEU B CB  
8122  C CG  . LEU B 185 ? 0.0670 0.1039 0.0951 -0.0025 -0.0109 0.0063  408 LEU B CG  
8123  C CD1 . LEU B 185 ? 0.0936 0.1351 0.1150 -0.0070 -0.0136 0.0075  408 LEU B CD1 
8124  C CD2 . LEU B 185 ? 0.0819 0.1155 0.0982 -0.0130 0.0017  0.0145  408 LEU B CD2 
8136  N N   . PRO B 186 ? 0.0782 0.0903 0.0786 0.0069  -0.0113 -0.0022 409 PRO B N   
8137  C CA  . PRO B 186 ? 0.0784 0.0959 0.0992 0.0174  -0.0074 0.0002  409 PRO B CA  
8138  C C   . PRO B 186 ? 0.0605 0.0825 0.0966 0.0132  -0.0089 -0.0044 409 PRO B C   
8139  O O   . PRO B 186 ? 0.0731 0.0979 0.1056 0.0198  -0.0239 -0.0086 409 PRO B O   
8140  C CB  . PRO B 186 ? 0.1111 0.1232 0.1090 0.0428  0.0050  0.0092  409 PRO B CB  
8141  C CG  . PRO B 186 ? 0.1103 0.1079 0.1353 0.0252  0.0057  -0.0052 409 PRO B CG  
8142  C CD  . PRO B 186 ? 0.0801 0.0891 0.1021 0.0108  -0.0211 -0.0141 409 PRO B CD  
8150  N N   . ASN B 187 ? 0.0794 0.0874 0.0890 0.0141  -0.0098 0.0141  410 ASN B N   
8151  C CA  . ASN B 187 ? 0.1059 0.0871 0.0948 0.0224  -0.0193 0.0174  410 ASN B CA  
8152  C C   . ASN B 187 ? 0.0928 0.0826 0.0892 0.0267  -0.0168 0.0065  410 ASN B C   
8153  O O   . ASN B 187 ? 0.0980 0.0853 0.1222 0.0263  0.0067  0.0071  410 ASN B O   
8154  C CB  . ASN B 187 ? 0.1508 0.0985 0.1039 0.0212  -0.0349 0.0158  410 ASN B CB  
8155  C CG  . ASN B 187 ? 0.2108 0.1165 0.1216 0.0257  -0.0149 0.0206  410 ASN B CG  
8156  O OD1 . ASN B 187 ? 0.2834 0.1345 0.1554 0.0153  0.0141  0.0235  410 ASN B OD1 
8157  N ND2 . ASN B 187 ? 0.2503 0.1381 0.1556 0.0456  0.0178  0.0294  410 ASN B ND2 
8164  N N   . TYR B 188 ? 0.0875 0.0769 0.0765 0.0321  -0.0247 0.0136  411 TYR B N   
8165  C CA  . TYR B 188 ? 0.0928 0.0705 0.0762 0.0226  -0.0132 -0.0054 411 TYR B CA  
8166  C C   . TYR B 188 ? 0.1007 0.0874 0.0875 0.0338  -0.0106 -0.0042 411 TYR B C   
8167  O O   . TYR B 188 ? 0.1027 0.0832 0.0925 0.0351  -0.0248 -0.0008 411 TYR B O   
8168  C CB  . TYR B 188 ? 0.1011 0.0639 0.1002 0.0250  -0.0062 0.0222  411 TYR B CB  
8169  C CG  . TYR B 188 ? 0.0954 0.0732 0.0955 0.0088  -0.0021 0.0148  411 TYR B CG  
8170  C CD1 . TYR B 188 ? 0.1016 0.0672 0.0898 0.0147  -0.0092 0.0099  411 TYR B CD1 
8171  C CD2 . TYR B 188 ? 0.1117 0.0896 0.0867 0.0269  -0.0154 0.0072  411 TYR B CD2 
8172  C CE1 . TYR B 188 ? 0.0983 0.0607 0.0867 0.0061  -0.0132 0.0108  411 TYR B CE1 
8173  C CE2 . TYR B 188 ? 0.1226 0.0825 0.0963 0.0250  -0.0193 0.0052  411 TYR B CE2 
8174  C CZ  . TYR B 188 ? 0.0976 0.0674 0.0766 0.0180  0.0010  0.0165  411 TYR B CZ  
8175  O OH  . TYR B 188 ? 0.1051 0.0787 0.0925 0.0136  0.0041  -0.0095 411 TYR B OH  
8185  N N   . SER B 189 ? 0.1126 0.0840 0.0869 0.0439  -0.0176 -0.0022 412 SER B N   
8186  C CA  . SER B 189 ? 0.1282 0.1087 0.0826 0.0463  -0.0137 0.0015  412 SER B CA  
8187  C C   . SER B 189 ? 0.1347 0.1287 0.0807 0.0518  -0.0252 0.0149  412 SER B C   
8188  O O   . SER B 189 ? 0.1743 0.1810 0.0943 0.0336  -0.0090 0.0124  412 SER B O   
8189  C CB  . SER B 189 ? 0.1401 0.1222 0.1046 0.0196  -0.0249 -0.0086 412 SER B CB  
8190  O OG  . SER B 189 ? 0.1538 0.1343 0.1181 0.0175  -0.0319 0.0001  412 SER B OG  
8196  N N   . GLY B 190 ? 0.1163 0.1098 0.0866 0.0493  -0.0080 0.0110  413 GLY B N   
8197  C CA  . GLY B 190 ? 0.1379 0.1336 0.1509 0.0435  0.0265  0.0072  413 GLY B CA  
8198  C C   . GLY B 190 ? 0.1386 0.1398 0.1704 0.0444  0.0360  0.0196  413 GLY B C   
8199  O O   . GLY B 190 ? 0.1585 0.1313 0.1543 0.0521  0.0214  0.0359  413 GLY B O   
8203  N N   . ALA B 191 ? 0.1482 0.1551 0.1817 0.0444  0.0284  0.0263  414 ALA B N   
8204  C CA  . ALA B 191 ? 0.1250 0.1899 0.1896 0.0469  -0.0135 0.0521  414 ALA B CA  
8205  C C   . ALA B 191 ? 0.1482 0.1831 0.1742 0.0364  0.0124  0.0353  414 ALA B C   
8206  O O   . ALA B 191 ? 0.1809 0.1790 0.1946 0.0763  0.0538  0.0517  414 ALA B O   
8207  C CB  . ALA B 191 ? 0.1318 0.2151 0.2293 0.0547  -0.0098 0.0778  414 ALA B CB  
8213  N N   . LEU B 192 ? 0.1299 0.1505 0.1423 0.0321  0.0062  0.0260  415 LEU B N   
8214  C CA  . LEU B 192 ? 0.0995 0.1388 0.1081 0.0374  -0.0310 0.0286  415 LEU B CA  
8215  C C   . LEU B 192 ? 0.1123 0.1242 0.0860 0.0336  -0.0166 0.0127  415 LEU B C   
8216  O O   . LEU B 192 ? 0.1305 0.1566 0.1019 0.0223  -0.0238 0.0370  415 LEU B O   
8217  C CB  . LEU B 192 ? 0.1106 0.1684 0.1272 0.0155  -0.0185 0.0391  415 LEU B CB  
8218  C CG  . LEU B 192 ? 0.1542 0.2154 0.1577 -0.0049 -0.0052 0.0404  415 LEU B CG  
8219  C CD1 . LEU B 192 ? 0.1622 0.2436 0.1667 -0.0250 0.0104  0.0418  415 LEU B CD1 
8220  C CD2 . LEU B 192 ? 0.2147 0.2287 0.2072 -0.0189 0.0439  0.0302  415 LEU B CD2 
8232  N N   . THR B 193 ? 0.1156 0.1055 0.0968 0.0440  -0.0093 0.0088  416 THR B N   
8233  C CA  . THR B 193 ? 0.1250 0.1128 0.1072 0.0289  -0.0007 0.0074  416 THR B CA  
8234  C C   . THR B 193 ? 0.1122 0.1187 0.1063 0.0271  -0.0012 0.0194  416 THR B C   
8235  O O   . THR B 193 ? 0.1081 0.1311 0.0878 0.0424  -0.0065 0.0184  416 THR B O   
8236  C CB  . THR B 193 ? 0.1837 0.1144 0.1281 0.0263  0.0183  0.0117  416 THR B CB  
8237  O OG1 . THR B 193 ? 0.2587 0.1326 0.1555 0.0123  0.0596  -0.0108 416 THR B OG1 
8238  C CG2 . THR B 193 ? 0.1764 0.1161 0.1379 0.0209  -0.0270 0.0019  416 THR B CG2 
8246  N N   . LEU B 194 ? 0.1078 0.1153 0.0966 0.0249  0.0005  0.0141  417 LEU B N   
8247  C CA  . LEU B 194 ? 0.1021 0.1124 0.0924 0.0295  -0.0001 0.0243  417 LEU B CA  
8248  C C   . LEU B 194 ? 0.1065 0.1104 0.0768 0.0267  -0.0121 0.0106  417 LEU B C   
8249  O O   . LEU B 194 ? 0.1400 0.1107 0.0870 0.0164  -0.0156 0.0051  417 LEU B O   
8250  C CB  . LEU B 194 ? 0.0992 0.1146 0.0864 0.0297  -0.0117 0.0238  417 LEU B CB  
8251  C CG  . LEU B 194 ? 0.0966 0.1275 0.1037 0.0280  -0.0144 0.0276  417 LEU B CG  
8252  C CD1 . LEU B 194 ? 0.0979 0.1445 0.1204 0.0384  -0.0160 0.0460  417 LEU B CD1 
8253  C CD2 . LEU B 194 ? 0.1041 0.1135 0.1445 0.0178  -0.0085 0.0277  417 LEU B CD2 
8265  N N   . ASN B 195 ? 0.0815 0.1151 0.0746 0.0188  -0.0216 0.0136  418 ASN B N   
8266  C CA  . ASN B 195 ? 0.0824 0.0955 0.0740 0.0211  -0.0152 0.0142  418 ASN B CA  
8267  C C   . ASN B 195 ? 0.0974 0.1049 0.0863 0.0128  -0.0153 0.0026  418 ASN B C   
8268  O O   . ASN B 195 ? 0.0841 0.1125 0.1021 0.0234  -0.0229 0.0139  418 ASN B O   
8269  C CB  . ASN B 195 ? 0.0931 0.0648 0.0753 0.0131  -0.0169 0.0062  418 ASN B CB  
8270  C CG  . ASN B 195 ? 0.0842 0.0874 0.0758 0.0227  -0.0186 0.0045  418 ASN B CG  
8271  O OD1 . ASN B 195 ? 0.1013 0.0911 0.0933 0.0196  -0.0209 -0.0056 418 ASN B OD1 
8272  N ND2 . ASN B 195 ? 0.0649 0.1043 0.1111 0.0166  -0.0139 -0.0109 418 ASN B ND2 
8279  N N   . MET B 196 ? 0.0938 0.1044 0.0994 -0.0026 -0.0255 0.0143  419 MET B N   
8280  C CA  A MET B 196 ? 0.1202 0.1279 0.0992 -0.0194 -0.0320 -0.0011 419 MET B CA  
8281  C CA  B MET B 196 ? 0.1086 0.1170 0.1011 -0.0139 -0.0350 0.0150  419 MET B CA  
8282  C C   . MET B 196 ? 0.0985 0.1169 0.0891 -0.0183 -0.0301 0.0038  419 MET B C   
8283  O O   . MET B 196 ? 0.1224 0.1298 0.0936 0.0015  -0.0232 0.0127  419 MET B O   
8284  C CB  A MET B 196 ? 0.1721 0.1705 0.1017 -0.0340 -0.0240 -0.0139 419 MET B CB  
8285  C CB  B MET B 196 ? 0.1366 0.1325 0.1140 -0.0213 -0.0434 0.0295  419 MET B CB  
8286  C CG  A MET B 196 ? 0.2015 0.1983 0.1049 -0.0397 -0.0311 -0.0327 419 MET B CG  
8287  C CG  B MET B 196 ? 0.1596 0.1418 0.1278 -0.0258 -0.0584 0.0378  419 MET B CG  
8288  S SD  A MET B 196 ? 0.2350 0.2331 0.1481 -0.0478 -0.0054 -0.0472 419 MET B SD  
8289  S SD  B MET B 196 ? 0.1896 0.1607 0.1617 -0.0262 -0.0465 0.0386  419 MET B SD  
8290  C CE  A MET B 196 ? 0.2332 0.2320 0.1626 -0.0503 -0.0159 -0.0465 419 MET B CE  
8291  C CE  B MET B 196 ? 0.1935 0.1641 0.1715 -0.0226 -0.0365 0.0363  419 MET B CE  
8310  N N   . GLY B 197 ? 0.0995 0.1147 0.0882 -0.0305 -0.0237 0.0066  420 GLY B N   
8311  C CA  . GLY B 197 ? 0.1067 0.1077 0.1001 -0.0239 -0.0064 0.0007  420 GLY B CA  
8312  C C   . GLY B 197 ? 0.0983 0.1073 0.0931 -0.0272 -0.0221 0.0101  420 GLY B C   
8313  O O   . GLY B 197 ? 0.1148 0.1123 0.1045 -0.0169 -0.0209 0.0124  420 GLY B O   
8317  N N   . LEU B 198 ? 0.0980 0.0951 0.0959 -0.0095 -0.0258 -0.0052 421 LEU B N   
8318  C CA  . LEU B 198 ? 0.0804 0.0954 0.0955 -0.0104 -0.0207 0.0021  421 LEU B CA  
8319  C C   . LEU B 198 ? 0.0913 0.1059 0.0924 -0.0011 -0.0115 -0.0062 421 LEU B C   
8320  O O   . LEU B 198 ? 0.0961 0.1386 0.1079 -0.0022 -0.0070 -0.0003 421 LEU B O   
8321  C CB  . LEU B 198 ? 0.0799 0.0893 0.0838 -0.0057 -0.0330 0.0052  421 LEU B CB  
8322  C CG  . LEU B 198 ? 0.0877 0.0936 0.0945 0.0012  -0.0092 -0.0047 421 LEU B CG  
8323  C CD1 . LEU B 198 ? 0.0988 0.0955 0.1356 -0.0073 0.0135  -0.0098 421 LEU B CD1 
8324  C CD2 . LEU B 198 ? 0.0986 0.1108 0.0882 -0.0014 0.0115  0.0038  421 LEU B CD2 
8336  N N   . ALA B 199 ? 0.0895 0.0951 0.0940 -0.0115 -0.0182 -0.0023 422 ALA B N   
8337  C CA  . ALA B 199 ? 0.0679 0.1193 0.1001 -0.0109 -0.0146 -0.0107 422 ALA B CA  
8338  C C   . ALA B 199 ? 0.0834 0.1325 0.0940 0.0131  -0.0236 -0.0077 422 ALA B C   
8339  O O   . ALA B 199 ? 0.1011 0.0997 0.1135 -0.0004 -0.0208 -0.0070 422 ALA B O   
8340  C CB  . ALA B 199 ? 0.0852 0.1138 0.0917 -0.0220 0.0023  -0.0197 422 ALA B CB  
8346  N N   . PRO B 200 ? 0.1020 0.1655 0.1232 0.0372  -0.0308 -0.0108 423 PRO B N   
8347  C CA  . PRO B 200 ? 0.1240 0.1759 0.1324 0.0557  -0.0360 -0.0142 423 PRO B CA  
8348  C C   . PRO B 200 ? 0.1151 0.1622 0.1253 0.0572  -0.0451 -0.0354 423 PRO B C   
8349  O O   . PRO B 200 ? 0.1257 0.1568 0.1271 0.0642  -0.0379 -0.0289 423 PRO B O   
8350  C CB  . PRO B 200 ? 0.1455 0.2022 0.1838 0.0547  -0.0139 -0.0123 423 PRO B CB  
8351  C CG  . PRO B 200 ? 0.1252 0.2183 0.2124 0.0492  0.0139  0.0003  423 PRO B CG  
8352  C CD  . PRO B 200 ? 0.1031 0.1953 0.1780 0.0481  -0.0050 0.0033  423 PRO B CD  
8360  N N   . SER B 201 ? 0.1399 0.1669 0.1401 0.0536  -0.0505 -0.0430 424 SER B N   
8361  C CA  . SER B 201 ? 0.1319 0.1714 0.1578 0.0587  -0.0533 -0.0477 424 SER B CA  
8362  C C   . SER B 201 ? 0.1040 0.1863 0.1613 0.0463  -0.0504 -0.0571 424 SER B C   
8363  O O   . SER B 201 ? 0.1159 0.2307 0.1889 0.0436  -0.0497 -0.0756 424 SER B O   
8364  C CB  . SER B 201 ? 0.1724 0.1769 0.1808 0.0812  -0.0676 -0.0258 424 SER B CB  
8365  O OG  . SER B 201 ? 0.2216 0.1990 0.2280 0.0753  -0.0613 -0.0079 424 SER B OG  
8371  N N   . VAL B 202 ? 0.0791 0.1630 0.1361 0.0295  -0.0316 -0.0447 425 VAL B N   
8372  C CA  . VAL B 202 ? 0.1057 0.1538 0.1355 0.0227  -0.0105 -0.0274 425 VAL B CA  
8373  C C   . VAL B 202 ? 0.1114 0.1465 0.1221 0.0279  -0.0147 -0.0096 425 VAL B C   
8374  O O   . VAL B 202 ? 0.1108 0.1304 0.1365 0.0261  -0.0163 -0.0019 425 VAL B O   
8375  C CB  . VAL B 202 ? 0.1525 0.1541 0.1411 -0.0015 0.0166  -0.0338 425 VAL B CB  
8376  C CG1 . VAL B 202 ? 0.2015 0.1569 0.1691 -0.0225 0.0325  -0.0607 425 VAL B CG1 
8377  C CG2 . VAL B 202 ? 0.1537 0.1504 0.1334 0.0126  0.0148  -0.0089 425 VAL B CG2 
8387  N N   . PHE B 203 ? 0.1174 0.1456 0.1490 0.0154  -0.0199 -0.0227 426 PHE B N   
8388  C CA  . PHE B 203 ? 0.1199 0.1382 0.1532 0.0244  -0.0213 -0.0093 426 PHE B CA  
8389  C C   . PHE B 203 ? 0.1062 0.1261 0.1606 0.0239  -0.0262 -0.0047 426 PHE B C   
8390  O O   . PHE B 203 ? 0.1201 0.1282 0.1735 0.0228  -0.0161 -0.0335 426 PHE B O   
8391  C CB  . PHE B 203 ? 0.1532 0.2013 0.1690 0.0311  -0.0249 -0.0082 426 PHE B CB  
8392  C CG  . PHE B 203 ? 0.2057 0.2828 0.2072 0.0498  -0.0388 -0.0137 426 PHE B CG  
8393  C CD1 . PHE B 203 ? 0.2294 0.3083 0.1973 0.0460  -0.0641 -0.0253 426 PHE B CD1 
8394  C CD2 . PHE B 203 ? 0.2342 0.3264 0.2234 0.0635  -0.0593 -0.0139 426 PHE B CD2 
8395  C CE1 . PHE B 203 ? 0.2622 0.3391 0.2315 0.0579  -0.0435 -0.0249 426 PHE B CE1 
8396  C CE2 . PHE B 203 ? 0.2554 0.3547 0.2340 0.0601  -0.0663 -0.0289 426 PHE B CE2 
8397  C CZ  . PHE B 203 ? 0.2595 0.3547 0.2362 0.0685  -0.0628 -0.0304 426 PHE B CZ  
8407  N N   . PRO B 204 ? 0.1064 0.1355 0.1573 0.0267  -0.0372 -0.0095 427 PRO B N   
8408  C CA  . PRO B 204 ? 0.1419 0.1413 0.1598 0.0364  -0.0253 0.0049  427 PRO B CA  
8409  C C   . PRO B 204 ? 0.1507 0.1351 0.1809 0.0397  -0.0108 0.0243  427 PRO B C   
8410  O O   . PRO B 204 ? 0.1689 0.1966 0.2521 0.0538  0.0126  0.0671  427 PRO B O   
8411  C CB  . PRO B 204 ? 0.1752 0.1612 0.1661 0.0289  -0.0178 -0.0151 427 PRO B CB  
8412  C CG  . PRO B 204 ? 0.1702 0.1763 0.1952 0.0466  -0.0293 -0.0387 427 PRO B CG  
8413  C CD  . PRO B 204 ? 0.1195 0.1575 0.1787 0.0413  -0.0419 -0.0191 427 PRO B CD  
8421  N N   . THR B 205 ? 0.1632 0.1191 0.1488 0.0309  -0.0329 0.0107  428 THR B N   
8422  C CA  . THR B 205 ? 0.1813 0.1341 0.1588 0.0215  -0.0415 0.0208  428 THR B CA  
8423  C C   . THR B 205 ? 0.1661 0.1195 0.1684 0.0183  -0.0357 0.0127  428 THR B C   
8424  O O   . THR B 205 ? 0.2078 0.1233 0.1944 0.0365  -0.0026 0.0195  428 THR B O   
8425  C CB  . THR B 205 ? 0.2083 0.1678 0.1585 0.0081  -0.0580 -0.0003 428 THR B CB  
8426  O OG1 . THR B 205 ? 0.2116 0.1792 0.1690 -0.0026 -0.0628 -0.0164 428 THR B OG1 
8427  C CG2 . THR B 205 ? 0.2293 0.1934 0.1685 0.0127  -0.0529 -0.0090 428 THR B CG2 
8435  N N   . TYR B 206 ? 0.1269 0.0969 0.1643 0.0173  -0.0396 -0.0020 429 TYR B N   
8436  C CA  . TYR B 206 ? 0.1471 0.0921 0.1689 0.0190  -0.0280 0.0044  429 TYR B CA  
8437  C C   . TYR B 206 ? 0.1345 0.0964 0.1858 0.0330  -0.0519 0.0153  429 TYR B C   
8438  O O   . TYR B 206 ? 0.1369 0.0866 0.1928 0.0288  -0.0519 0.0196  429 TYR B O   
8439  C CB  . TYR B 206 ? 0.2138 0.0871 0.1886 0.0412  -0.0019 0.0236  429 TYR B CB  
8440  C CG  . TYR B 206 ? 0.2675 0.1025 0.2227 0.0532  0.0087  0.0022  429 TYR B CG  
8441  C CD1 . TYR B 206 ? 0.3091 0.1468 0.2323 0.0793  0.0123  -0.0133 429 TYR B CD1 
8442  C CD2 . TYR B 206 ? 0.3046 0.1362 0.2960 0.0288  0.0765  -0.0407 429 TYR B CD2 
8443  C CE1 . TYR B 206 ? 0.3402 0.1681 0.2496 0.0766  0.0577  -0.0274 429 TYR B CE1 
8444  C CE2 . TYR B 206 ? 0.3275 0.1672 0.3210 0.0385  0.1074  -0.0397 429 TYR B CE2 
8445  C CZ  . TYR B 206 ? 0.3378 0.1656 0.2794 0.0720  0.1077  -0.0322 429 TYR B CZ  
8446  O OH  . TYR B 206 ? 0.3726 0.1857 0.3008 0.0679  0.1455  -0.0248 429 TYR B OH  
8456  N N   . PRO B 207 ? 0.1411 0.0964 0.2147 0.0368  -0.0643 0.0091  430 PRO B N   
8457  C CA  A PRO B 207 ? 0.1585 0.0922 0.2418 0.0351  -0.0651 0.0074  430 PRO B CA  
8458  C CA  B PRO B 207 ? 0.1535 0.0913 0.2461 0.0358  -0.0603 0.0048  430 PRO B CA  
8459  C C   . PRO B 207 ? 0.1642 0.0990 0.2573 0.0284  -0.0672 -0.0053 430 PRO B C   
8460  O O   . PRO B 207 ? 0.1984 0.1700 0.2421 0.0428  -0.0460 -0.0293 430 PRO B O   
8461  C CB  A PRO B 207 ? 0.1749 0.1023 0.2530 0.0446  -0.0656 0.0084  430 PRO B CB  
8462  C CB  B PRO B 207 ? 0.1577 0.0960 0.2575 0.0391  -0.0441 0.0034  430 PRO B CB  
8463  C CG  A PRO B 207 ? 0.1680 0.1105 0.2273 0.0436  -0.0745 0.0135  430 PRO B CG  
8464  C CG  B PRO B 207 ? 0.1470 0.0958 0.2561 0.0408  -0.0390 0.0059  430 PRO B CG  
8465  C CD  A PRO B 207 ? 0.1547 0.1070 0.2187 0.0424  -0.0669 0.0155  430 PRO B CD  
8466  C CD  B PRO B 207 ? 0.1432 0.0958 0.2417 0.0420  -0.0453 0.0114  430 PRO B CD  
8481  N N   . GLY B 208 ? 0.1785 0.0899 0.2702 0.0300  -0.0747 -0.0037 431 GLY B N   
8482  C CA  . GLY B 208 ? 0.1665 0.0973 0.2464 0.0282  -0.0911 -0.0021 431 GLY B CA  
8483  C C   . GLY B 208 ? 0.1441 0.0841 0.2269 0.0262  -0.0836 -0.0139 431 GLY B C   
8484  O O   . GLY B 208 ? 0.1724 0.0855 0.2378 0.0229  -0.0900 -0.0332 431 GLY B O   
8488  N N   . GLU B 209 ? 0.1094 0.0676 0.1844 0.0298  -0.0392 -0.0109 432 GLU B N   
8489  C CA  . GLU B 209 ? 0.0839 0.0746 0.1318 0.0292  -0.0316 0.0010  432 GLU B CA  
8490  C C   . GLU B 209 ? 0.0888 0.0629 0.1098 0.0106  -0.0280 0.0026  432 GLU B C   
8491  O O   . GLU B 209 ? 0.1059 0.0809 0.1261 0.0203  -0.0414 0.0171  432 GLU B O   
8492  C CB  . GLU B 209 ? 0.0903 0.0811 0.1232 0.0176  -0.0141 0.0019  432 GLU B CB  
8493  C CG  . GLU B 209 ? 0.0975 0.0780 0.1516 0.0079  -0.0084 0.0011  432 GLU B CG  
8494  C CD  . GLU B 209 ? 0.0999 0.0798 0.1490 0.0173  -0.0172 -0.0030 432 GLU B CD  
8495  O OE1 . GLU B 209 ? 0.1121 0.0784 0.1439 0.0219  -0.0279 -0.0087 432 GLU B OE1 
8496  O OE2 . GLU B 209 ? 0.0977 0.0987 0.1549 0.0075  -0.0106 -0.0081 432 GLU B OE2 
8503  N N   . GLN B 210 ? 0.0888 0.0621 0.0977 0.0193  -0.0271 0.0019  433 GLN B N   
8504  C CA  . GLN B 210 ? 0.0776 0.0606 0.1018 0.0093  -0.0156 0.0000  433 GLN B CA  
8505  C C   . GLN B 210 ? 0.0752 0.0630 0.1014 0.0054  -0.0182 0.0079  433 GLN B C   
8506  O O   . GLN B 210 ? 0.0897 0.0584 0.1104 -0.0003 -0.0068 0.0004  433 GLN B O   
8507  C CB  . GLN B 210 ? 0.0862 0.0706 0.1156 0.0056  -0.0168 -0.0023 433 GLN B CB  
8508  C CG  . GLN B 210 ? 0.0985 0.0732 0.1469 -0.0002 -0.0036 0.0006  433 GLN B CG  
8509  C CD  . GLN B 210 ? 0.0962 0.0763 0.1610 -0.0083 -0.0144 0.0050  433 GLN B CD  
8510  O OE1 . GLN B 210 ? 0.1237 0.0788 0.1888 -0.0236 -0.0097 0.0003  433 GLN B OE1 
8511  N NE2 . GLN B 210 ? 0.0999 0.0833 0.1614 -0.0123 -0.0268 -0.0090 433 GLN B NE2 
8520  N N   . ILE B 211 ? 0.0763 0.0602 0.0996 0.0067  -0.0131 0.0028  434 ILE B N   
8521  C CA  . ILE B 211 ? 0.0663 0.0658 0.0900 0.0044  -0.0061 0.0045  434 ILE B CA  
8522  C C   . ILE B 211 ? 0.0613 0.0708 0.0949 -0.0017 0.0013  0.0013  434 ILE B C   
8523  O O   . ILE B 211 ? 0.0660 0.0713 0.0982 -0.0137 -0.0113 0.0090  434 ILE B O   
8524  C CB  . ILE B 211 ? 0.0697 0.0799 0.0978 0.0125  -0.0215 0.0031  434 ILE B CB  
8525  C CG1 . ILE B 211 ? 0.1202 0.1001 0.1061 0.0296  -0.0227 -0.0023 434 ILE B CG1 
8526  C CG2 . ILE B 211 ? 0.0644 0.0763 0.1206 0.0074  0.0105  -0.0020 434 ILE B CG2 
8527  C CD1 . ILE B 211 ? 0.1576 0.1269 0.1238 0.0410  -0.0182 -0.0186 434 ILE B CD1 
8539  N N   . LEU B 212 ? 0.0459 0.0709 0.0958 0.0018  -0.0190 0.0006  435 LEU B N   
8540  C CA  . LEU B 212 ? 0.0491 0.0743 0.0930 0.0171  -0.0188 0.0003  435 LEU B CA  
8541  C C   . LEU B 212 ? 0.0522 0.0658 0.0856 0.0044  -0.0279 -0.0006 435 LEU B C   
8542  O O   . LEU B 212 ? 0.0703 0.0695 0.1394 0.0056  -0.0311 -0.0223 435 LEU B O   
8543  C CB  . LEU B 212 ? 0.0408 0.0677 0.1088 0.0091  -0.0123 0.0069  435 LEU B CB  
8544  C CG  . LEU B 212 ? 0.0727 0.0728 0.1183 0.0020  -0.0004 -0.0021 435 LEU B CG  
8545  C CD1 . LEU B 212 ? 0.0772 0.1047 0.1436 -0.0174 -0.0079 -0.0161 435 LEU B CD1 
8546  C CD2 . LEU B 212 ? 0.0804 0.1008 0.1035 0.0046  -0.0002 0.0114  435 LEU B CD2 
8558  N N   . PHE B 213 ? 0.0442 0.0574 0.1028 0.0051  -0.0186 -0.0088 436 PHE B N   
8559  C CA  . PHE B 213 ? 0.0605 0.0715 0.0804 0.0171  -0.0153 -0.0038 436 PHE B CA  
8560  C C   . PHE B 213 ? 0.0675 0.0632 0.0854 0.0100  -0.0049 -0.0090 436 PHE B C   
8561  O O   . PHE B 213 ? 0.0856 0.0711 0.0812 0.0067  -0.0154 -0.0062 436 PHE B O   
8562  C CB  . PHE B 213 ? 0.0803 0.0859 0.0988 0.0069  -0.0071 -0.0012 436 PHE B CB  
8563  C CG  . PHE B 213 ? 0.0621 0.0962 0.0969 0.0174  -0.0171 0.0131  436 PHE B CG  
8564  C CD1 . PHE B 213 ? 0.0509 0.1090 0.1116 0.0303  -0.0112 0.0185  436 PHE B CD1 
8565  C CD2 . PHE B 213 ? 0.0878 0.1037 0.1273 0.0250  -0.0094 0.0349  436 PHE B CD2 
8566  C CE1 . PHE B 213 ? 0.0628 0.1371 0.1174 0.0241  -0.0144 0.0111  436 PHE B CE1 
8567  C CE2 . PHE B 213 ? 0.0893 0.1147 0.1490 0.0134  0.0012  0.0341  436 PHE B CE2 
8568  C CZ  . PHE B 213 ? 0.0898 0.1441 0.1308 0.0343  0.0111  0.0300  436 PHE B CZ  
8578  N N   . PHE B 214 ? 0.0698 0.0549 0.0788 0.0037  -0.0173 -0.0116 437 PHE B N   
8579  C CA  . PHE B 214 ? 0.0704 0.0602 0.0651 0.0153  -0.0195 0.0009  437 PHE B CA  
8580  C C   . PHE B 214 ? 0.0593 0.0612 0.0754 0.0183  -0.0138 -0.0104 437 PHE B C   
8581  O O   . PHE B 214 ? 0.0721 0.0773 0.0722 0.0007  -0.0086 -0.0195 437 PHE B O   
8582  C CB  . PHE B 214 ? 0.0611 0.0724 0.0759 0.0028  -0.0225 0.0003  437 PHE B CB  
8583  C CG  . PHE B 214 ? 0.0673 0.0680 0.0772 0.0034  0.0014  -0.0111 437 PHE B CG  
8584  C CD1 . PHE B 214 ? 0.0554 0.0757 0.0932 -0.0011 -0.0038 -0.0197 437 PHE B CD1 
8585  C CD2 . PHE B 214 ? 0.0783 0.0670 0.0841 -0.0086 -0.0037 -0.0078 437 PHE B CD2 
8586  C CE1 . PHE B 214 ? 0.0626 0.0809 0.0948 0.0022  -0.0111 -0.0249 437 PHE B CE1 
8587  C CE2 . PHE B 214 ? 0.0867 0.0797 0.0917 -0.0146 0.0071  -0.0085 437 PHE B CE2 
8588  C CZ  . PHE B 214 ? 0.0668 0.0795 0.1035 -0.0089 0.0077  -0.0200 437 PHE B CZ  
8598  N N   . ARG B 215 ? 0.0604 0.0647 0.0820 -0.0028 -0.0150 -0.0100 438 ARG B N   
8599  C CA  . ARG B 215 ? 0.0618 0.0715 0.0779 0.0034  -0.0018 -0.0045 438 ARG B CA  
8600  C C   . ARG B 215 ? 0.0669 0.0632 0.0833 0.0060  -0.0102 -0.0103 438 ARG B C   
8601  O O   . ARG B 215 ? 0.0707 0.0806 0.0836 0.0051  -0.0088 -0.0057 438 ARG B O   
8602  C CB  . ARG B 215 ? 0.0482 0.0687 0.1113 -0.0011 -0.0043 -0.0085 438 ARG B CB  
8603  C CG  . ARG B 215 ? 0.0785 0.0768 0.1129 -0.0005 -0.0054 -0.0017 438 ARG B CG  
8604  C CD  . ARG B 215 ? 0.0863 0.0710 0.1136 0.0038  -0.0075 0.0050  438 ARG B CD  
8605  N NE  . ARG B 215 ? 0.0844 0.0686 0.1094 -0.0130 -0.0110 -0.0073 438 ARG B NE  
8606  C CZ  . ARG B 215 ? 0.1134 0.0781 0.1141 -0.0209 -0.0169 -0.0124 438 ARG B CZ  
8607  N NH1 . ARG B 215 ? 0.1404 0.0913 0.1448 -0.0359 -0.0213 0.0022  438 ARG B NH1 
8608  N NH2 . ARG B 215 ? 0.1076 0.0633 0.1176 -0.0149 -0.0120 0.0032  438 ARG B NH2 
8622  N N   . SER B 216 ? 0.0563 0.0652 0.0837 0.0089  -0.0058 0.0014  439 SER B N   
8623  C CA  . SER B 216 ? 0.0456 0.0692 0.0881 0.0087  -0.0094 -0.0077 439 SER B CA  
8624  C C   . SER B 216 ? 0.0584 0.0620 0.0772 -0.0024 -0.0160 -0.0053 439 SER B C   
8625  O O   . SER B 216 ? 0.0648 0.0871 0.0882 0.0001  -0.0114 0.0055  439 SER B O   
8626  C CB  . SER B 216 ? 0.0668 0.0739 0.0877 0.0030  -0.0156 -0.0081 439 SER B CB  
8627  O OG  . SER B 216 ? 0.0834 0.0743 0.1019 -0.0174 -0.0171 0.0029  439 SER B OG  
8633  N N   . TYR B 217 ? 0.0541 0.0747 0.0879 -0.0003 -0.0127 -0.0020 440 TYR B N   
8634  C CA  A TYR B 217 ? 0.0618 0.0829 0.1088 -0.0032 -0.0208 0.0062  440 TYR B CA  
8635  C CA  B TYR B 217 ? 0.0718 0.0815 0.1102 0.0015  -0.0095 0.0012  440 TYR B CA  
8636  C C   . TYR B 217 ? 0.0729 0.0742 0.1283 0.0017  0.0092  0.0124  440 TYR B C   
8637  O O   . TYR B 217 ? 0.1375 0.0881 0.1943 0.0152  0.0726  0.0244  440 TYR B O   
8638  C CB  A TYR B 217 ? 0.0702 0.1238 0.0941 -0.0119 -0.0303 0.0100  440 TYR B CB  
8639  C CB  B TYR B 217 ? 0.0881 0.1071 0.0979 0.0035  -0.0164 -0.0001 440 TYR B CB  
8640  C CG  A TYR B 217 ? 0.0828 0.1311 0.1060 -0.0270 -0.0412 -0.0067 440 TYR B CG  
8641  C CG  B TYR B 217 ? 0.1070 0.1185 0.1021 -0.0117 -0.0068 -0.0177 440 TYR B CG  
8642  C CD1 A TYR B 217 ? 0.1052 0.1210 0.1167 -0.0243 -0.0449 -0.0166 440 TYR B CD1 
8643  C CD1 B TYR B 217 ? 0.1218 0.1170 0.1096 -0.0198 0.0101  -0.0303 440 TYR B CD1 
8644  C CD2 A TYR B 217 ? 0.1180 0.1402 0.1240 -0.0265 -0.0064 -0.0250 440 TYR B CD2 
8645  C CD2 B TYR B 217 ? 0.1306 0.1147 0.1139 -0.0186 -0.0003 -0.0315 440 TYR B CD2 
8646  C CE1 A TYR B 217 ? 0.1269 0.1191 0.1414 -0.0285 -0.0153 -0.0306 440 TYR B CE1 
8647  C CE1 B TYR B 217 ? 0.1533 0.1250 0.1349 -0.0318 0.0332  -0.0402 440 TYR B CE1 
8648  C CE2 A TYR B 217 ? 0.1424 0.1426 0.1485 -0.0215 0.0049  -0.0415 440 TYR B CE2 
8649  C CE2 B TYR B 217 ? 0.1506 0.1152 0.1200 -0.0226 0.0115  -0.0378 440 TYR B CE2 
8650  C CZ  A TYR B 217 ? 0.1530 0.1297 0.1624 -0.0143 -0.0006 -0.0473 440 TYR B CZ  
8651  C CZ  B TYR B 217 ? 0.1691 0.1178 0.1365 -0.0335 0.0388  -0.0518 440 TYR B CZ  
8652  O OH  A TYR B 217 ? 0.1923 0.1438 0.1980 -0.0070 0.0030  -0.0664 440 TYR B OH  
8653  O OH  B TYR B 217 ? 0.1999 0.1294 0.1616 -0.0410 0.0682  -0.0680 440 TYR B OH  
8672  N N   . LEU B 218 ? 0.0517 0.0670 0.1178 -0.0047 0.0061  -0.0081 441 LEU B N   
8673  C CA  . LEU B 218 ? 0.0583 0.0741 0.1139 0.0002  0.0045  -0.0041 441 LEU B CA  
8674  C C   . LEU B 218 ? 0.0557 0.0691 0.1022 -0.0059 0.0014  -0.0003 441 LEU B C   
8675  O O   . LEU B 218 ? 0.0613 0.0595 0.1131 -0.0031 -0.0014 0.0062  441 LEU B O   
8676  C CB  . LEU B 218 ? 0.0647 0.0987 0.1208 -0.0007 0.0019  -0.0214 441 LEU B CB  
8677  C CG  . LEU B 218 ? 0.0539 0.1327 0.1619 -0.0035 -0.0162 -0.0096 441 LEU B CG  
8678  C CD1 . LEU B 218 ? 0.0849 0.1910 0.1905 0.0077  0.0068  -0.0198 441 LEU B CD1 
8679  C CD2 . LEU B 218 ? 0.0643 0.1435 0.2245 -0.0095 -0.0292 -0.0109 441 LEU B CD2 
8691  N N   . PRO B 219 ? 0.0515 0.0600 0.0898 -0.0032 -0.0006 -0.0010 442 PRO B N   
8692  C CA  . PRO B 219 ? 0.0544 0.0637 0.0873 0.0044  -0.0083 0.0129  442 PRO B CA  
8693  C C   . PRO B 219 ? 0.0444 0.0576 0.0976 0.0062  -0.0113 -0.0056 442 PRO B C   
8694  O O   . PRO B 219 ? 0.0588 0.0649 0.0893 -0.0022 -0.0106 -0.0135 442 PRO B O   
8695  C CB  . PRO B 219 ? 0.1044 0.0954 0.1104 0.0229  0.0327  0.0326  442 PRO B CB  
8696  C CG  . PRO B 219 ? 0.0815 0.0897 0.1289 0.0077  -0.0092 0.0153  442 PRO B CG  
8697  C CD  . PRO B 219 ? 0.0627 0.0699 0.1147 0.0006  -0.0084 0.0000  442 PRO B CD  
8705  N N   . LEU B 220 ? 0.0555 0.0639 0.0817 -0.0132 -0.0051 -0.0058 443 LEU B N   
8706  C CA  . LEU B 220 ? 0.0504 0.0546 0.0778 -0.0053 -0.0133 0.0032  443 LEU B CA  
8707  C C   . LEU B 220 ? 0.0443 0.0569 0.0823 -0.0185 -0.0188 -0.0010 443 LEU B C   
8708  O O   . LEU B 220 ? 0.0516 0.0608 0.0776 0.0004  -0.0051 -0.0055 443 LEU B O   
8709  C CB  . LEU B 220 ? 0.0569 0.0657 0.0864 -0.0112 -0.0210 0.0022  443 LEU B CB  
8710  C CG  . LEU B 220 ? 0.0671 0.0702 0.0787 -0.0097 -0.0066 -0.0045 443 LEU B CG  
8711  C CD1 . LEU B 220 ? 0.0802 0.0695 0.0844 -0.0090 0.0003  -0.0129 443 LEU B CD1 
8712  C CD2 . LEU B 220 ? 0.0866 0.0671 0.0975 -0.0055 -0.0078 0.0083  443 LEU B CD2 
8724  N N   . LYS B 221 ? 0.0601 0.0547 0.0730 0.0011  -0.0183 0.0071  444 LYS B N   
8725  C CA  . LYS B 221 ? 0.0583 0.0504 0.0791 0.0031  -0.0097 0.0026  444 LYS B CA  
8726  C C   . LYS B 221 ? 0.0618 0.0539 0.0871 0.0044  -0.0019 0.0010  444 LYS B C   
8727  O O   . LYS B 221 ? 0.0600 0.0547 0.1017 -0.0063 -0.0124 0.0002  444 LYS B O   
8728  C CB  . LYS B 221 ? 0.0518 0.0545 0.0994 0.0039  -0.0068 0.0058  444 LYS B CB  
8729  C CG  . LYS B 221 ? 0.0620 0.0550 0.1064 -0.0021 0.0040  -0.0072 444 LYS B CG  
8730  C CD  . LYS B 221 ? 0.0677 0.0592 0.1148 0.0074  0.0008  0.0060  444 LYS B CD  
8731  C CE  . LYS B 221 ? 0.0705 0.0741 0.1007 0.0156  0.0038  0.0165  444 LYS B CE  
8732  N NZ  . LYS B 221 ? 0.0500 0.0724 0.1046 0.0107  0.0013  -0.0020 444 LYS B NZ  
8746  N N   . GLY B 222 ? 0.0537 0.0434 0.1084 0.0045  -0.0034 0.0061  445 GLY B N   
8747  C CA  . GLY B 222 ? 0.0674 0.0482 0.1028 -0.0093 -0.0035 0.0083  445 GLY B CA  
8748  C C   . GLY B 222 ? 0.0729 0.0548 0.0959 -0.0130 -0.0029 0.0020  445 GLY B C   
8749  O O   . GLY B 222 ? 0.0648 0.0637 0.1062 0.0004  -0.0030 0.0025  445 GLY B O   
8753  N N   . GLY B 223 ? 0.0769 0.0472 0.1112 -0.0130 0.0157  -0.0035 446 GLY B N   
8754  C CA  . GLY B 223 ? 0.0756 0.0558 0.1219 -0.0108 0.0135  0.0025  446 GLY B CA  
8755  C C   . GLY B 223 ? 0.0714 0.0624 0.0934 -0.0166 0.0041  0.0045  446 GLY B C   
8756  O O   . GLY B 223 ? 0.0941 0.0649 0.0899 -0.0105 0.0080  0.0034  446 GLY B O   
8760  N N   . TYR B 224 ? 0.0680 0.0657 0.0732 -0.0087 -0.0023 -0.0035 447 TYR B N   
8761  C CA  . TYR B 224 ? 0.0756 0.0730 0.0970 -0.0051 0.0035  -0.0014 447 TYR B CA  
8762  C C   . TYR B 224 ? 0.0810 0.0678 0.0912 -0.0061 -0.0047 -0.0025 447 TYR B C   
8763  O O   . TYR B 224 ? 0.0830 0.0890 0.0928 -0.0134 0.0022  0.0063  447 TYR B O   
8764  C CB  . TYR B 224 ? 0.0965 0.0757 0.1224 -0.0293 0.0189  -0.0146 447 TYR B CB  
8765  C CG  . TYR B 224 ? 0.0813 0.0803 0.1116 -0.0341 0.0002  0.0045  447 TYR B CG  
8766  C CD1 . TYR B 224 ? 0.0831 0.0995 0.1223 -0.0201 -0.0028 -0.0055 447 TYR B CD1 
8767  C CD2 . TYR B 224 ? 0.1122 0.0879 0.1243 -0.0411 -0.0071 0.0066  447 TYR B CD2 
8768  C CE1 . TYR B 224 ? 0.0816 0.1311 0.1738 -0.0262 -0.0110 -0.0132 447 TYR B CE1 
8769  C CE2 . TYR B 224 ? 0.1079 0.1151 0.1573 -0.0480 -0.0133 0.0235  447 TYR B CE2 
8770  C CZ  . TYR B 224 ? 0.0730 0.1488 0.1954 -0.0266 -0.0437 0.0050  447 TYR B CZ  
8771  O OH  . TYR B 224 ? 0.1157 0.2045 0.2431 -0.0166 -0.0483 -0.0148 447 TYR B OH  
8781  N N   . GLY B 225 ? 0.0689 0.0687 0.0999 -0.0086 0.0039  0.0043  448 GLY B N   
8782  C CA  . GLY B 225 ? 0.0798 0.0768 0.1088 -0.0032 0.0086  0.0092  448 GLY B CA  
8783  C C   . GLY B 225 ? 0.0717 0.0610 0.1017 -0.0072 -0.0081 0.0044  448 GLY B C   
8784  O O   . GLY B 225 ? 0.0703 0.0725 0.1067 -0.0054 -0.0044 0.0108  448 GLY B O   
8788  N N   . SER B 226 ? 0.0551 0.0727 0.1009 0.0012  0.0025  0.0108  449 SER B N   
8789  C CA  A SER B 226 ? 0.0577 0.0777 0.1137 -0.0118 0.0012  -0.0019 449 SER B CA  
8790  C CA  B SER B 226 ? 0.0589 0.0735 0.1108 -0.0070 0.0038  0.0035  449 SER B CA  
8791  C C   . SER B 226 ? 0.0628 0.0736 0.1126 -0.0162 0.0056  -0.0002 449 SER B C   
8792  O O   . SER B 226 ? 0.0646 0.0878 0.1273 -0.0038 0.0010  0.0001  449 SER B O   
8793  C CB  A SER B 226 ? 0.0753 0.1062 0.1000 -0.0089 -0.0089 -0.0012 449 SER B CB  
8794  C CB  B SER B 226 ? 0.0590 0.0761 0.1125 -0.0040 -0.0013 0.0026  449 SER B CB  
8795  O OG  A SER B 226 ? 0.0832 0.1065 0.0981 -0.0239 -0.0122 -0.0041 449 SER B OG  
8796  O OG  B SER B 226 ? 0.0553 0.0747 0.1154 -0.0040 -0.0073 0.0018  449 SER B OG  
8807  N N   . PRO B 227 ? 0.0541 0.0676 0.1169 -0.0019 0.0013  -0.0066 450 PRO B N   
8808  C CA  . PRO B 227 ? 0.0597 0.0663 0.1022 -0.0011 -0.0059 0.0042  450 PRO B CA  
8809  C C   . PRO B 227 ? 0.0580 0.0562 0.1017 -0.0095 -0.0010 -0.0083 450 PRO B C   
8810  O O   . PRO B 227 ? 0.0600 0.0642 0.1118 -0.0010 0.0053  0.0097  450 PRO B O   
8811  C CB  . PRO B 227 ? 0.0868 0.0812 0.0915 -0.0015 0.0031  0.0022  450 PRO B CB  
8812  C CG  . PRO B 227 ? 0.0865 0.0753 0.0906 -0.0032 -0.0020 -0.0132 450 PRO B CG  
8813  C CD  . PRO B 227 ? 0.0818 0.0786 0.0947 -0.0021 0.0032  -0.0034 450 PRO B CD  
8821  N N   . PHE B 228 ? 0.0591 0.0715 0.1015 -0.0076 -0.0061 0.0052  451 PHE B N   
8822  C CA  . PHE B 228 ? 0.0649 0.0793 0.0965 -0.0131 -0.0082 0.0005  451 PHE B CA  
8823  C C   . PHE B 228 ? 0.0556 0.0831 0.0979 -0.0123 0.0038  0.0059  451 PHE B C   
8824  O O   . PHE B 228 ? 0.0720 0.0730 0.0943 -0.0094 -0.0008 -0.0057 451 PHE B O   
8825  C CB  . PHE B 228 ? 0.0745 0.0896 0.1154 -0.0181 -0.0073 -0.0141 451 PHE B CB  
8826  C CG  . PHE B 228 ? 0.0621 0.0814 0.1393 -0.0070 -0.0258 -0.0207 451 PHE B CG  
8827  C CD1 . PHE B 228 ? 0.0861 0.0948 0.1393 0.0014  -0.0118 -0.0271 451 PHE B CD1 
8828  C CD2 . PHE B 228 ? 0.0998 0.0835 0.1884 0.0000  -0.0122 -0.0165 451 PHE B CD2 
8829  C CE1 . PHE B 228 ? 0.1003 0.1043 0.1452 0.0217  -0.0016 -0.0212 451 PHE B CE1 
8830  C CE2 . PHE B 228 ? 0.1179 0.0895 0.1949 -0.0014 -0.0092 -0.0148 451 PHE B CE2 
8831  C CZ  . PHE B 228 ? 0.1257 0.1032 0.1718 0.0174  0.0084  -0.0026 451 PHE B CZ  
8841  N N   . ILE B 229 ? 0.0548 0.0743 0.0749 -0.0044 0.0005  0.0087  452 ILE B N   
8842  C CA  . ILE B 229 ? 0.0526 0.0717 0.0655 0.0039  -0.0096 0.0112  452 ILE B CA  
8843  C C   . ILE B 229 ? 0.0573 0.0620 0.0588 -0.0138 -0.0128 0.0015  452 ILE B C   
8844  O O   . ILE B 229 ? 0.0633 0.0817 0.0650 0.0003  -0.0059 0.0008  452 ILE B O   
8845  C CB  . ILE B 229 ? 0.0494 0.0726 0.0719 0.0069  -0.0024 0.0010  452 ILE B CB  
8846  C CG1 . ILE B 229 ? 0.0611 0.0901 0.0751 0.0088  0.0025  0.0101  452 ILE B CG1 
8847  C CG2 . ILE B 229 ? 0.0799 0.0765 0.0919 0.0124  -0.0043 -0.0052 452 ILE B CG2 
8848  C CD1 . ILE B 229 ? 0.0611 0.1009 0.0887 -0.0033 0.0019  -0.0035 452 ILE B CD1 
8860  N N   . ASP B 230 ? 0.0492 0.0720 0.0745 0.0015  -0.0170 0.0048  453 ASP B N   
8861  C CA  . ASP B 230 ? 0.0407 0.0742 0.0838 -0.0068 -0.0041 -0.0028 453 ASP B CA  
8862  C C   . ASP B 230 ? 0.0496 0.0665 0.0781 0.0015  0.0032  -0.0014 453 ASP B C   
8863  O O   . ASP B 230 ? 0.0652 0.0879 0.0774 -0.0088 -0.0104 0.0025  453 ASP B O   
8864  C CB  . ASP B 230 ? 0.0491 0.0723 0.0826 -0.0099 -0.0016 -0.0067 453 ASP B CB  
8865  C CG  . ASP B 230 ? 0.0765 0.0858 0.0929 -0.0066 -0.0128 0.0068  453 ASP B CG  
8866  O OD1 . ASP B 230 ? 0.1075 0.0977 0.0969 -0.0270 -0.0312 -0.0119 453 ASP B OD1 
8867  O OD2 . ASP B 230 ? 0.1021 0.0694 0.1061 -0.0224 0.0044  -0.0061 453 ASP B OD2 
8872  N N   . CYS B 231 ? 0.0525 0.0723 0.0694 -0.0071 -0.0023 -0.0054 454 CYS B N   
8873  C CA  . CYS B 231 ? 0.0441 0.0738 0.0746 0.0082  -0.0146 -0.0014 454 CYS B CA  
8874  C C   . CYS B 231 ? 0.0524 0.0656 0.0830 0.0088  -0.0141 0.0006  454 CYS B C   
8875  O O   . CYS B 231 ? 0.0608 0.0689 0.0732 0.0124  -0.0092 -0.0077 454 CYS B O   
8876  C CB  . CYS B 231 ? 0.0412 0.0694 0.0829 0.0098  -0.0071 -0.0069 454 CYS B CB  
8877  S SG  . CYS B 231 ? 0.0591 0.0694 0.0881 0.0043  -0.0087 -0.0100 454 CYS B SG  
8883  N N   . LEU B 232 ? 0.0482 0.0683 0.0746 -0.0003 -0.0169 -0.0086 455 LEU B N   
8884  C CA  . LEU B 232 ? 0.0564 0.0685 0.0793 0.0105  -0.0095 -0.0026 455 LEU B CA  
8885  C C   . LEU B 232 ? 0.0732 0.0659 0.0756 0.0059  -0.0061 -0.0097 455 LEU B C   
8886  O O   . LEU B 232 ? 0.0845 0.0554 0.0911 0.0069  -0.0130 -0.0024 455 LEU B O   
8887  C CB  . LEU B 232 ? 0.0717 0.0741 0.0860 0.0149  -0.0034 -0.0024 455 LEU B CB  
8888  C CG  . LEU B 232 ? 0.0697 0.0845 0.0899 0.0033  -0.0096 -0.0037 455 LEU B CG  
8889  C CD1 . LEU B 232 ? 0.0973 0.0927 0.1027 0.0123  -0.0038 -0.0076 455 LEU B CD1 
8890  C CD2 . LEU B 232 ? 0.1038 0.1082 0.0915 -0.0053 -0.0143 0.0165  455 LEU B CD2 
8902  N N   . VAL B 233 ? 0.0700 0.0632 0.0729 -0.0019 -0.0066 -0.0090 456 VAL B N   
8903  C CA  . VAL B 233 ? 0.0535 0.0760 0.0862 0.0009  -0.0089 -0.0100 456 VAL B CA  
8904  C C   . VAL B 233 ? 0.0630 0.0604 0.0813 0.0000  -0.0120 -0.0142 456 VAL B C   
8905  O O   . VAL B 233 ? 0.0674 0.0684 0.0832 0.0116  -0.0016 -0.0019 456 VAL B O   
8906  C CB  . VAL B 233 ? 0.0690 0.0635 0.1025 0.0118  -0.0024 0.0019  456 VAL B CB  
8907  C CG1 . VAL B 233 ? 0.0740 0.0765 0.1038 0.0070  0.0017  0.0094  456 VAL B CG1 
8908  C CG2 . VAL B 233 ? 0.0710 0.0773 0.1260 0.0107  -0.0139 -0.0108 456 VAL B CG2 
8918  N N   . PRO B 234 ? 0.0618 0.0610 0.0815 0.0015  -0.0011 -0.0142 457 PRO B N   
8919  C CA  . PRO B 234 ? 0.0624 0.0597 0.0896 0.0127  -0.0193 -0.0077 457 PRO B CA  
8920  C C   . PRO B 234 ? 0.0553 0.0652 0.0835 0.0146  -0.0130 0.0095  457 PRO B C   
8921  O O   . PRO B 234 ? 0.0536 0.0681 0.0839 0.0026  -0.0211 0.0058  457 PRO B O   
8922  C CB  . PRO B 234 ? 0.1044 0.0696 0.0958 0.0012  -0.0168 -0.0187 457 PRO B CB  
8923  C CG  . PRO B 234 ? 0.1132 0.0768 0.0897 -0.0012 -0.0061 -0.0031 457 PRO B CG  
8924  C CD  . PRO B 234 ? 0.0908 0.0658 0.0877 -0.0045 0.0020  -0.0112 457 PRO B CD  
8932  N N   . GLN B 235 ? 0.0619 0.0628 0.0877 0.0041  -0.0159 0.0062  458 GLN B N   
8933  C CA  . GLN B 235 ? 0.0648 0.0627 0.0834 0.0110  0.0036  -0.0018 458 GLN B CA  
8934  C C   . GLN B 235 ? 0.0481 0.0618 0.0890 0.0065  -0.0047 -0.0043 458 GLN B C   
8935  O O   . GLN B 235 ? 0.0628 0.0689 0.0931 0.0042  -0.0054 -0.0085 458 GLN B O   
8936  C CB  . GLN B 235 ? 0.0676 0.0785 0.0837 0.0135  -0.0069 -0.0035 458 GLN B CB  
8937  C CG  . GLN B 235 ? 0.0817 0.0771 0.0849 0.0168  0.0035  0.0018  458 GLN B CG  
8938  C CD  . GLN B 235 ? 0.0874 0.0779 0.0871 -0.0059 0.0128  0.0006  458 GLN B CD  
8939  O OE1 . GLN B 235 ? 0.1020 0.0668 0.0888 -0.0062 0.0115  -0.0093 458 GLN B OE1 
8940  N NE2 . GLN B 235 ? 0.1249 0.0892 0.0918 -0.0283 -0.0214 0.0024  458 GLN B NE2 
8949  N N   . GLU B 236 ? 0.0466 0.0719 0.0852 0.0042  -0.0109 -0.0056 459 GLU B N   
8950  C CA  . GLU B 236 ? 0.0723 0.0713 0.0922 -0.0020 -0.0127 0.0080  459 GLU B CA  
8951  C C   . GLU B 236 ? 0.0615 0.0696 0.0917 0.0031  -0.0093 0.0035  459 GLU B C   
8952  O O   . GLU B 236 ? 0.0839 0.0630 0.1091 0.0024  -0.0155 0.0072  459 GLU B O   
8953  C CB  . GLU B 236 ? 0.0674 0.0967 0.1012 -0.0045 -0.0109 0.0280  459 GLU B CB  
8954  C CG  . GLU B 236 ? 0.0670 0.1032 0.1066 -0.0010 -0.0212 0.0411  459 GLU B CG  
8955  C CD  . GLU B 236 ? 0.0645 0.1005 0.1230 0.0136  -0.0069 0.0322  459 GLU B CD  
8956  O OE1 . GLU B 236 ? 0.0571 0.0946 0.1043 0.0044  -0.0024 0.0155  459 GLU B OE1 
8957  O OE2 . GLU B 236 ? 0.0935 0.1067 0.1657 0.0250  -0.0019 0.0351  459 GLU B OE2 
8964  N N   . TRP B 237 ? 0.0621 0.0633 0.0894 0.0033  -0.0120 0.0010  460 TRP B N   
8965  C CA  . TRP B 237 ? 0.0592 0.0615 0.0847 -0.0031 -0.0093 0.0003  460 TRP B CA  
8966  C C   . TRP B 237 ? 0.0553 0.0690 0.0848 0.0045  -0.0191 0.0025  460 TRP B C   
8967  O O   . TRP B 237 ? 0.0559 0.0728 0.1040 0.0037  -0.0131 -0.0046 460 TRP B O   
8968  C CB  . TRP B 237 ? 0.0640 0.0584 0.0948 0.0112  -0.0236 -0.0003 460 TRP B CB  
8969  C CG  . TRP B 237 ? 0.0668 0.0702 0.0805 0.0144  -0.0234 -0.0016 460 TRP B CG  
8970  C CD1 . TRP B 237 ? 0.0800 0.0635 0.1011 0.0092  -0.0149 -0.0118 460 TRP B CD1 
8971  C CD2 . TRP B 237 ? 0.0511 0.0645 0.0874 0.0050  -0.0197 -0.0014 460 TRP B CD2 
8972  N NE1 . TRP B 237 ? 0.0915 0.0726 0.0872 -0.0030 -0.0116 0.0036  460 TRP B NE1 
8973  C CE2 . TRP B 237 ? 0.0651 0.0673 0.0733 0.0125  -0.0147 -0.0038 460 TRP B CE2 
8974  C CE3 . TRP B 237 ? 0.0781 0.0723 0.0821 0.0024  -0.0003 0.0011  460 TRP B CE3 
8975  C CZ2 . TRP B 237 ? 0.0764 0.0826 0.0736 0.0052  -0.0145 -0.0152 460 TRP B CZ2 
8976  C CZ3 . TRP B 237 ? 0.0774 0.0738 0.0896 0.0068  -0.0129 -0.0042 460 TRP B CZ3 
8977  C CH2 . TRP B 237 ? 0.0807 0.0805 0.0974 0.0084  -0.0054 -0.0167 460 TRP B CH2 
8988  N N   . VAL B 238 ? 0.0608 0.0707 0.0780 0.0069  -0.0057 -0.0090 461 VAL B N   
8989  C CA  . VAL B 238 ? 0.0724 0.0840 0.0832 0.0079  0.0071  -0.0125 461 VAL B CA  
8990  C C   . VAL B 238 ? 0.0662 0.0815 0.0957 0.0044  -0.0133 -0.0173 461 VAL B C   
8991  O O   . VAL B 238 ? 0.0599 0.0913 0.1022 -0.0048 -0.0150 -0.0122 461 VAL B O   
8992  C CB  . VAL B 238 ? 0.0849 0.0884 0.0671 -0.0029 -0.0118 -0.0046 461 VAL B CB  
8993  C CG1 . VAL B 238 ? 0.1031 0.0913 0.0894 0.0033  0.0054  0.0080  461 VAL B CG1 
8994  C CG2 . VAL B 238 ? 0.1038 0.1031 0.0772 0.0009  -0.0052 -0.0147 461 VAL B CG2 
9004  N N   . ALA B 239 ? 0.0623 0.0705 0.1022 -0.0001 -0.0161 -0.0172 462 ALA B N   
9005  C CA  . ALA B 239 ? 0.0779 0.0666 0.1162 -0.0102 -0.0111 -0.0121 462 ALA B CA  
9006  C C   . ALA B 239 ? 0.0641 0.0699 0.1191 -0.0038 -0.0254 -0.0059 462 ALA B C   
9007  O O   . ALA B 239 ? 0.0755 0.0716 0.1271 -0.0089 -0.0235 -0.0108 462 ALA B O   
9008  C CB  . ALA B 239 ? 0.0784 0.0735 0.1506 0.0171  -0.0050 0.0001  462 ALA B CB  
9014  N N   . HIS B 240 ? 0.0700 0.0648 0.1033 -0.0042 -0.0195 -0.0032 463 HIS B N   
9015  C CA  . HIS B 240 ? 0.0598 0.0759 0.1188 -0.0082 -0.0130 -0.0003 463 HIS B CA  
9016  C C   . HIS B 240 ? 0.0619 0.0743 0.1067 -0.0036 0.0023  -0.0041 463 HIS B C   
9017  O O   . HIS B 240 ? 0.0620 0.0911 0.1116 -0.0056 -0.0006 0.0016  463 HIS B O   
9018  C CB  . HIS B 240 ? 0.0698 0.0902 0.1177 -0.0036 -0.0093 0.0040  463 HIS B CB  
9019  C CG  . HIS B 240 ? 0.0891 0.0965 0.1138 -0.0039 -0.0067 0.0232  463 HIS B CG  
9020  N ND1 . HIS B 240 ? 0.1211 0.1324 0.1354 0.0399  0.0310  0.0513  463 HIS B ND1 
9021  C CD2 . HIS B 240 ? 0.0986 0.1008 0.1116 0.0020  -0.0090 0.0167  463 HIS B CD2 
9022  C CE1 . HIS B 240 ? 0.1347 0.1337 0.1277 0.0331  0.0555  0.0418  463 HIS B CE1 
9023  N NE2 . HIS B 240 ? 0.1047 0.1241 0.1160 0.0222  0.0100  0.0229  463 HIS B NE2 
9031  N N   . PHE B 241 ? 0.0596 0.0751 0.0889 -0.0040 -0.0074 0.0084  464 PHE B N   
9032  C CA  . PHE B 241 ? 0.0718 0.0721 0.0843 0.0022  -0.0104 0.0040  464 PHE B CA  
9033  C C   . PHE B 241 ? 0.0601 0.0698 0.1024 -0.0161 0.0022  0.0012  464 PHE B C   
9034  O O   . PHE B 241 ? 0.0550 0.0939 0.1053 -0.0059 -0.0134 0.0108  464 PHE B O   
9035  C CB  . PHE B 241 ? 0.0754 0.0773 0.1016 0.0166  -0.0207 0.0024  464 PHE B CB  
9036  C CG  . PHE B 241 ? 0.0672 0.0760 0.1176 0.0133  -0.0245 0.0115  464 PHE B CG  
9037  C CD1 . PHE B 241 ? 0.1038 0.0740 0.1288 0.0170  0.0030  0.0018  464 PHE B CD1 
9038  C CD2 . PHE B 241 ? 0.0719 0.0814 0.1212 -0.0019 -0.0169 -0.0021 464 PHE B CD2 
9039  C CE1 . PHE B 241 ? 0.1065 0.0857 0.1327 0.0155  0.0121  0.0022  464 PHE B CE1 
9040  C CE2 . PHE B 241 ? 0.0846 0.0853 0.1365 0.0148  -0.0117 -0.0052 464 PHE B CE2 
9041  C CZ  . PHE B 241 ? 0.1011 0.0857 0.1369 0.0105  -0.0062 -0.0117 464 PHE B CZ  
9051  N N   . TYR B 242 ? 0.0620 0.0744 0.0929 -0.0041 -0.0122 -0.0046 465 TYR B N   
9052  C CA  . TYR B 242 ? 0.0829 0.0711 0.1136 0.0007  -0.0025 0.0126  465 TYR B CA  
9053  C C   . TYR B 242 ? 0.0670 0.0716 0.1261 -0.0033 -0.0189 0.0073  465 TYR B C   
9054  O O   . TYR B 242 ? 0.0829 0.0899 0.1416 -0.0180 -0.0222 0.0159  465 TYR B O   
9055  C CB  . TYR B 242 ? 0.0929 0.0681 0.1174 -0.0143 -0.0048 -0.0056 465 TYR B CB  
9056  C CG  . TYR B 242 ? 0.1009 0.0867 0.1285 0.0143  -0.0256 -0.0193 465 TYR B CG  
9057  C CD1 . TYR B 242 ? 0.1267 0.1075 0.1383 0.0088  -0.0315 -0.0315 465 TYR B CD1 
9058  C CD2 . TYR B 242 ? 0.1530 0.0901 0.1306 0.0201  -0.0226 -0.0125 465 TYR B CD2 
9059  C CE1 . TYR B 242 ? 0.1542 0.1258 0.1324 0.0289  -0.0420 -0.0333 465 TYR B CE1 
9060  C CE2 . TYR B 242 ? 0.1977 0.1016 0.1442 0.0234  -0.0283 -0.0317 465 TYR B CE2 
9061  C CZ  . TYR B 242 ? 0.1902 0.1124 0.1430 0.0331  -0.0613 -0.0507 465 TYR B CZ  
9062  O OH  . TYR B 242 ? 0.2420 0.1247 0.1859 0.0490  -0.0664 -0.0535 465 TYR B OH  
9072  N N   . GLN B 243 ? 0.0659 0.0663 0.1321 -0.0032 -0.0220 0.0105  466 GLN B N   
9073  C CA  . GLN B 243 ? 0.0629 0.0694 0.1392 -0.0063 -0.0092 0.0150  466 GLN B CA  
9074  C C   . GLN B 243 ? 0.0678 0.0806 0.1513 -0.0060 -0.0172 0.0002  466 GLN B C   
9075  O O   . GLN B 243 ? 0.0918 0.0928 0.1845 -0.0220 0.0074  -0.0006 466 GLN B O   
9076  C CB  . GLN B 243 ? 0.0877 0.0667 0.1314 -0.0019 -0.0152 0.0240  466 GLN B CB  
9077  C CG  . GLN B 243 ? 0.0835 0.0717 0.1407 -0.0031 -0.0144 0.0204  466 GLN B CG  
9078  C CD  . GLN B 243 ? 0.0990 0.0754 0.1521 0.0084  -0.0191 0.0172  466 GLN B CD  
9079  O OE1 . GLN B 243 ? 0.1187 0.0831 0.1654 -0.0025 -0.0252 0.0299  466 GLN B OE1 
9080  N NE2 . GLN B 243 ? 0.1220 0.0850 0.1633 -0.0067 -0.0091 -0.0028 466 GLN B NE2 
9089  N N   . GLU B 244 ? 0.0799 0.0884 0.1512 -0.0039 0.0055  0.0070  467 GLU B N   
9090  C CA  . GLU B 244 ? 0.0878 0.1063 0.1631 0.0034  0.0181  0.0111  467 GLU B CA  
9091  C C   . GLU B 244 ? 0.0814 0.1186 0.1594 0.0220  0.0078  0.0380  467 GLU B C   
9092  O O   . GLU B 244 ? 0.0753 0.1289 0.1846 0.0004  0.0061  0.0298  467 GLU B O   
9093  C CB  . GLU B 244 ? 0.1038 0.1178 0.1748 0.0036  0.0214  0.0088  467 GLU B CB  
9094  C CG  . GLU B 244 ? 0.1293 0.1777 0.2088 0.0123  0.0181  0.0212  467 GLU B CG  
9095  C CD  . GLU B 244 ? 0.1818 0.2489 0.2631 0.0326  0.0471  0.0465  467 GLU B CD  
9096  O OE1 . GLU B 244 ? 0.1901 0.2931 0.2778 0.0027  0.0527  0.0314  467 GLU B OE1 
9097  O OE2 . GLU B 244 ? 0.2383 0.2785 0.3224 0.0519  0.0875  0.0737  467 GLU B OE2 
9104  N N   . SER B 245 ? 0.1030 0.1465 0.1805 0.0364  0.0253  0.0606  468 SER B N   
9105  C CA  A SER B 245 ? 0.1107 0.1686 0.1945 0.0348  0.0084  0.0566  468 SER B CA  
9106  C CA  B SER B 245 ? 0.1198 0.1820 0.2014 0.0526  0.0100  0.0586  468 SER B CA  
9107  C C   . SER B 245 ? 0.0871 0.1709 0.1961 0.0200  -0.0048 0.0484  468 SER B C   
9108  O O   . SER B 245 ? 0.1020 0.1968 0.1889 0.0213  -0.0027 0.0278  468 SER B O   
9109  C CB  A SER B 245 ? 0.1408 0.1889 0.2004 0.0428  -0.0009 0.0501  468 SER B CB  
9110  C CB  B SER B 245 ? 0.1665 0.2289 0.2158 0.0825  0.0046  0.0373  468 SER B CB  
9111  O OG  A SER B 245 ? 0.1603 0.2027 0.2083 0.0430  -0.0074 0.0442  468 SER B OG  
9112  O OG  B SER B 245 ? 0.1911 0.2659 0.2294 0.0919  0.0084  0.0180  468 SER B OG  
9123  N N   . ALA B 246 ? 0.0803 0.1483 0.2162 0.0125  0.0025  0.0475  469 ALA B N   
9124  C CA  . ALA B 246 ? 0.0888 0.1287 0.2142 0.0167  -0.0057 0.0340  469 ALA B CA  
9125  C C   . ALA B 246 ? 0.0901 0.1270 0.2234 0.0096  0.0114  0.0372  469 ALA B C   
9126  O O   . ALA B 246 ? 0.1114 0.1451 0.2531 0.0071  0.0493  0.0428  469 ALA B O   
9127  C CB  . ALA B 246 ? 0.1439 0.1568 0.2456 0.0110  0.0146  0.0142  469 ALA B CB  
9133  N N   . PRO B 247 ? 0.0657 0.1209 0.2115 0.0008  -0.0006 0.0274  470 PRO B N   
9134  C CA  A PRO B 247 ? 0.0785 0.1229 0.2110 -0.0020 -0.0088 0.0193  470 PRO B CA  
9135  C CA  B PRO B 247 ? 0.0801 0.1226 0.2076 0.0013  -0.0106 0.0177  470 PRO B CA  
9136  C C   . PRO B 247 ? 0.1064 0.1272 0.1976 0.0147  -0.0182 0.0209  470 PRO B C   
9137  O O   . PRO B 247 ? 0.1257 0.1550 0.1909 0.0180  -0.0128 0.0062  470 PRO B O   
9138  C CB  A PRO B 247 ? 0.0939 0.1403 0.2412 0.0066  0.0003  0.0298  470 PRO B CB  
9139  C CB  B PRO B 247 ? 0.0849 0.1302 0.2242 0.0032  -0.0102 0.0163  470 PRO B CB  
9140  C CG  A PRO B 247 ? 0.0900 0.1449 0.2466 -0.0082 0.0102  0.0358  470 PRO B CG  
9141  C CG  B PRO B 247 ? 0.0784 0.1306 0.2254 -0.0080 -0.0117 0.0125  470 PRO B CG  
9142  C CD  A PRO B 247 ? 0.0870 0.1385 0.2420 -0.0165 0.0250  0.0280  470 PRO B CD  
9143  C CD  B PRO B 247 ? 0.0765 0.1251 0.2249 -0.0119 0.0044  0.0130  470 PRO B CD  
9158  N N   . ALA B 248 ? 0.0987 0.1052 0.1995 0.0060  -0.0117 0.0175  471 ALA B N   
9159  C CA  . ALA B 248 ? 0.0865 0.1057 0.2229 0.0052  -0.0205 0.0179  471 ALA B CA  
9160  C C   . ALA B 248 ? 0.0854 0.1033 0.1958 0.0006  -0.0322 0.0148  471 ALA B C   
9161  O O   . ALA B 248 ? 0.1108 0.1362 0.2074 0.0196  -0.0358 0.0010  471 ALA B O   
9162  C CB  . ALA B 248 ? 0.0987 0.1219 0.2706 -0.0024 0.0119  0.0175  471 ALA B CB  
9168  N N   . GLN B 249 ? 0.0737 0.1157 0.1717 -0.0113 -0.0302 0.0274  472 GLN B N   
9169  C CA  A GLN B 249 ? 0.0608 0.1163 0.1633 -0.0130 -0.0204 0.0292  472 GLN B CA  
9170  C CA  B GLN B 249 ? 0.0713 0.1334 0.1710 -0.0086 -0.0192 0.0307  472 GLN B CA  
9171  C C   . GLN B 249 ? 0.0501 0.1238 0.1567 -0.0035 -0.0237 0.0205  472 GLN B C   
9172  O O   . GLN B 249 ? 0.0497 0.1320 0.1593 -0.0050 -0.0231 0.0273  472 GLN B O   
9173  C CB  A GLN B 249 ? 0.0619 0.1112 0.1541 -0.0248 -0.0152 0.0313  472 GLN B CB  
9174  C CB  B GLN B 249 ? 0.0949 0.1658 0.1792 -0.0144 -0.0063 0.0332  472 GLN B CB  
9175  C CG  A GLN B 249 ? 0.0793 0.1009 0.1460 -0.0294 -0.0089 0.0337  472 GLN B CG  
9176  C CG  B GLN B 249 ? 0.1371 0.1885 0.1882 -0.0255 0.0087  0.0291  472 GLN B CG  
9177  C CD  A GLN B 249 ? 0.0983 0.1022 0.1536 -0.0251 -0.0073 0.0180  472 GLN B CD  
9178  C CD  B GLN B 249 ? 0.1567 0.1892 0.1842 -0.0539 0.0187  0.0281  472 GLN B CD  
9179  O OE1 A GLN B 249 ? 0.1132 0.1190 0.1230 -0.0328 -0.0237 0.0000  472 GLN B OE1 
9180  O OE1 B GLN B 249 ? 0.2241 0.1899 0.2098 -0.0519 0.0585  0.0416  472 GLN B OE1 
9181  N NE2 A GLN B 249 ? 0.1178 0.1081 0.2042 -0.0232 0.0216  0.0240  472 GLN B NE2 
9182  N NE2 B GLN B 249 ? 0.0915 0.1632 0.1214 -0.0654 -0.0067 0.0239  472 GLN B NE2 
9199  N N   . THR B 250 ? 0.0758 0.1112 0.1425 -0.0081 -0.0210 0.0099  473 THR B N   
9200  C CA  . THR B 250 ? 0.0771 0.0956 0.1305 -0.0010 -0.0194 0.0135  473 THR B CA  
9201  C C   . THR B 250 ? 0.0669 0.0798 0.1291 -0.0005 -0.0342 0.0082  473 THR B C   
9202  O O   . THR B 250 ? 0.0718 0.0936 0.1522 0.0086  -0.0158 0.0199  473 THR B O   
9203  C CB  . THR B 250 ? 0.0637 0.0940 0.1439 -0.0007 -0.0314 0.0138  473 THR B CB  
9204  O OG1 . THR B 250 ? 0.0647 0.1041 0.1376 0.0041  -0.0367 -0.0122 473 THR B OG1 
9205  C CG2 . THR B 250 ? 0.0672 0.1105 0.1639 0.0133  -0.0235 0.0121  473 THR B CG2 
9213  N N   . ASP B 251 ? 0.0679 0.0792 0.1293 0.0101  -0.0320 0.0051  474 ASP B N   
9214  C CA  . ASP B 251 ? 0.0600 0.0975 0.1319 0.0015  -0.0271 -0.0017 474 ASP B CA  
9215  C C   . ASP B 251 ? 0.0551 0.0789 0.1231 0.0150  -0.0231 0.0033  474 ASP B C   
9216  O O   . ASP B 251 ? 0.0547 0.0900 0.1130 0.0100  -0.0162 0.0029  474 ASP B O   
9217  C CB  . ASP B 251 ? 0.0735 0.1351 0.1277 0.0054  -0.0334 0.0084  474 ASP B CB  
9218  C CG  . ASP B 251 ? 0.1401 0.1682 0.1452 0.0064  -0.0520 0.0179  474 ASP B CG  
9219  O OD1 . ASP B 251 ? 0.1581 0.1783 0.1576 0.0000  -0.0521 -0.0235 474 ASP B OD1 
9220  O OD2 . ASP B 251 ? 0.1965 0.2003 0.1685 0.0004  -0.0703 0.0315  474 ASP B OD2 
9225  N N   . VAL B 252 ? 0.0500 0.0854 0.1188 0.0054  -0.0274 -0.0002 475 VAL B N   
9226  C CA  . VAL B 252 ? 0.0563 0.0824 0.1242 -0.0022 -0.0138 -0.0083 475 VAL B CA  
9227  C C   . VAL B 252 ? 0.0489 0.0983 0.1062 0.0003  -0.0100 -0.0127 475 VAL B C   
9228  O O   . VAL B 252 ? 0.0668 0.1084 0.1321 0.0074  -0.0053 -0.0005 475 VAL B O   
9229  C CB  . VAL B 252 ? 0.0711 0.0794 0.1538 0.0030  -0.0241 -0.0051 475 VAL B CB  
9230  C CG1 . VAL B 252 ? 0.0860 0.0910 0.1750 -0.0095 -0.0170 -0.0083 475 VAL B CG1 
9231  C CG2 . VAL B 252 ? 0.0901 0.0813 0.1516 0.0133  -0.0080 -0.0100 475 VAL B CG2 
9241  N N   . ALA B 253 ? 0.0446 0.1047 0.0906 0.0000  -0.0044 -0.0037 476 ALA B N   
9242  C CA  . ALA B 253 ? 0.0728 0.1147 0.1060 -0.0200 -0.0037 0.0071  476 ALA B CA  
9243  C C   . ALA B 253 ? 0.0650 0.1119 0.0935 -0.0178 -0.0016 0.0002  476 ALA B C   
9244  O O   . ALA B 253 ? 0.0862 0.1488 0.0864 -0.0309 0.0023  -0.0189 476 ALA B O   
9245  C CB  . ALA B 253 ? 0.0970 0.1221 0.1152 -0.0243 -0.0336 0.0225  476 ALA B CB  
9251  N N   . LEU B 254 ? 0.0570 0.1096 0.0907 -0.0133 -0.0100 0.0013  477 LEU B N   
9252  C CA  . LEU B 254 ? 0.0659 0.1039 0.1033 0.0052  -0.0084 0.0083  477 LEU B CA  
9253  C C   . LEU B 254 ? 0.0776 0.0930 0.0928 -0.0027 -0.0109 0.0042  477 LEU B C   
9254  O O   . LEU B 254 ? 0.0927 0.1077 0.1159 -0.0046 -0.0052 0.0091  477 LEU B O   
9255  C CB  . LEU B 254 ? 0.0737 0.1161 0.1043 0.0068  -0.0189 0.0007  477 LEU B CB  
9256  C CG  . LEU B 254 ? 0.0861 0.1320 0.1213 0.0041  -0.0090 -0.0025 477 LEU B CG  
9257  C CD1 . LEU B 254 ? 0.0795 0.1342 0.1302 0.0126  -0.0155 -0.0033 477 LEU B CD1 
9258  C CD2 . LEU B 254 ? 0.1096 0.1429 0.1254 0.0226  -0.0050 -0.0013 477 LEU B CD2 
9270  N N   . ILE B 255 ? 0.0670 0.0878 0.1101 0.0052  -0.0136 -0.0020 478 ILE B N   
9271  C CA  . ILE B 255 ? 0.0670 0.0781 0.1078 0.0016  -0.0243 0.0034  478 ILE B CA  
9272  C C   . ILE B 255 ? 0.0770 0.0860 0.1097 -0.0026 -0.0231 0.0083  478 ILE B C   
9273  O O   . ILE B 255 ? 0.1066 0.0898 0.1081 -0.0125 -0.0262 0.0106  478 ILE B O   
9274  C CB  . ILE B 255 ? 0.0703 0.0882 0.1176 -0.0018 -0.0200 0.0057  478 ILE B CB  
9275  C CG1 . ILE B 255 ? 0.0772 0.0904 0.1183 0.0022  -0.0263 0.0093  478 ILE B CG1 
9276  C CG2 . ILE B 255 ? 0.0973 0.1147 0.1138 -0.0240 -0.0078 -0.0068 478 ILE B CG2 
9277  C CD1 . ILE B 255 ? 0.0992 0.0997 0.0893 -0.0106 -0.0295 -0.0060 478 ILE B CD1 
9289  N N   . ARG B 256 ? 0.0794 0.0889 0.1017 0.0068  -0.0322 0.0098  479 ARG B N   
9290  C CA  . ARG B 256 ? 0.0898 0.0867 0.0883 0.0063  -0.0241 -0.0066 479 ARG B CA  
9291  C C   . ARG B 256 ? 0.0953 0.0881 0.1018 -0.0003 -0.0305 -0.0134 479 ARG B C   
9292  O O   . ARG B 256 ? 0.1016 0.0891 0.1065 0.0043  -0.0321 -0.0101 479 ARG B O   
9293  C CB  . ARG B 256 ? 0.1198 0.1314 0.1073 0.0471  -0.0049 -0.0049 479 ARG B CB  
9294  C CG  . ARG B 256 ? 0.1509 0.1582 0.1639 0.0479  0.0218  0.0159  479 ARG B CG  
9295  C CD  . ARG B 256 ? 0.1751 0.1749 0.2156 0.0533  0.0290  0.0318  479 ARG B CD  
9296  N NE  . ARG B 256 ? 0.1796 0.1745 0.2436 0.0727  0.0244  0.0805  479 ARG B NE  
9297  C CZ  . ARG B 256 ? 0.2225 0.2148 0.2839 0.0831  0.0787  0.0917  479 ARG B CZ  
9298  N NH1 . ARG B 256 ? 0.2341 0.2426 0.3342 0.0811  0.1204  0.0967  479 ARG B NH1 
9299  N NH2 . ARG B 256 ? 0.2274 0.2425 0.2816 0.0967  0.0715  0.0833  479 ARG B NH2 
9313  N N   . TYR B 257 ? 0.0891 0.0754 0.1248 0.0074  -0.0245 -0.0174 480 TYR B N   
9314  C CA  . TYR B 257 ? 0.0895 0.0686 0.1218 0.0084  -0.0341 -0.0213 480 TYR B CA  
9315  C C   . TYR B 257 ? 0.0959 0.0937 0.1214 0.0051  -0.0339 -0.0174 480 TYR B C   
9316  O O   . TYR B 257 ? 0.1314 0.1102 0.1352 0.0055  -0.0239 -0.0342 480 TYR B O   
9317  C CB  . TYR B 257 ? 0.1088 0.0727 0.1310 -0.0031 -0.0131 -0.0221 480 TYR B CB  
9318  C CG  . TYR B 257 ? 0.0897 0.0917 0.1421 -0.0051 -0.0365 -0.0082 480 TYR B CG  
9319  C CD1 . TYR B 257 ? 0.0876 0.1098 0.1389 0.0105  -0.0214 -0.0119 480 TYR B CD1 
9320  C CD2 . TYR B 257 ? 0.1061 0.1010 0.1643 0.0057  -0.0221 -0.0283 480 TYR B CD2 
9321  C CE1 . TYR B 257 ? 0.1114 0.1170 0.1364 0.0029  -0.0266 -0.0261 480 TYR B CE1 
9322  C CE2 . TYR B 257 ? 0.0947 0.1079 0.1752 0.0067  -0.0206 -0.0285 480 TYR B CE2 
9323  C CZ  . TYR B 257 ? 0.0962 0.1036 0.1397 0.0133  -0.0370 -0.0116 480 TYR B CZ  
9324  O OH  . TYR B 257 ? 0.1101 0.1161 0.1640 0.0168  -0.0352 -0.0147 480 TYR B OH  
9334  N N   . VAL B 258 ? 0.0864 0.1059 0.1028 0.0102  -0.0405 -0.0293 481 VAL B N   
9335  C CA  A VAL B 258 ? 0.0985 0.1137 0.1143 0.0112  -0.0429 -0.0225 481 VAL B CA  
9336  C CA  B VAL B 258 ? 0.1038 0.1220 0.1178 0.0126  -0.0292 -0.0212 481 VAL B CA  
9337  C C   . VAL B 258 ? 0.1073 0.1129 0.1125 0.0195  -0.0293 -0.0124 481 VAL B C   
9338  O O   . VAL B 258 ? 0.1126 0.1240 0.1110 0.0161  -0.0318 -0.0191 481 VAL B O   
9339  C CB  A VAL B 258 ? 0.1150 0.1171 0.1314 -0.0075 -0.0339 -0.0093 481 VAL B CB  
9340  C CB  B VAL B 258 ? 0.1274 0.1424 0.1385 -0.0023 0.0000  -0.0101 481 VAL B CB  
9341  C CG1 A VAL B 258 ? 0.1056 0.1205 0.1318 -0.0167 -0.0441 -0.0113 481 VAL B CG1 
9342  C CG1 B VAL B 258 ? 0.1417 0.1484 0.1627 -0.0039 -0.0007 0.0028  481 VAL B CG1 
9343  C CG2 A VAL B 258 ? 0.1400 0.1258 0.1596 -0.0097 -0.0174 0.0025  481 VAL B CG2 
9344  C CG2 B VAL B 258 ? 0.1364 0.1623 0.1467 -0.0110 0.0229  -0.0115 481 VAL B CG2 
9363  N N   . ASN B 259 ? 0.1227 0.1141 0.1120 0.0193  -0.0384 -0.0253 482 ASN B N   
9364  C CA  . ASN B 259 ? 0.1347 0.1312 0.1110 0.0056  -0.0488 -0.0109 482 ASN B CA  
9365  C C   . ASN B 259 ? 0.1490 0.1134 0.1191 0.0055  -0.0377 -0.0187 482 ASN B C   
9366  O O   . ASN B 259 ? 0.1698 0.1166 0.1221 0.0015  -0.0272 -0.0251 482 ASN B O   
9367  C CB  . ASN B 259 ? 0.1188 0.1210 0.1147 0.0004  -0.0595 -0.0069 482 ASN B CB  
9368  C CG  . ASN B 259 ? 0.1460 0.1218 0.1227 -0.0012 -0.0496 -0.0129 482 ASN B CG  
9369  O OD1 . ASN B 259 ? 0.1604 0.1136 0.1199 -0.0063 -0.0353 -0.0064 482 ASN B OD1 
9370  N ND2 . ASN B 259 ? 0.1362 0.1345 0.1295 0.0103  -0.0545 -0.0086 482 ASN B ND2 
9377  N N   . PRO B 260 ? 0.1657 0.0966 0.1336 0.0039  -0.0204 -0.0171 483 PRO B N   
9378  C CA  . PRO B 260 ? 0.1962 0.1173 0.1324 -0.0067 -0.0287 -0.0124 483 PRO B CA  
9379  C C   . PRO B 260 ? 0.2173 0.1408 0.1312 -0.0015 -0.0195 0.0075  483 PRO B C   
9380  O O   . PRO B 260 ? 0.2309 0.1793 0.1687 -0.0044 0.0072  -0.0016 483 PRO B O   
9381  C CB  . PRO B 260 ? 0.2046 0.1284 0.1599 0.0096  -0.0248 -0.0223 483 PRO B CB  
9382  C CG  . PRO B 260 ? 0.1958 0.1206 0.1457 0.0181  -0.0237 -0.0308 483 PRO B CG  
9383  C CD  . PRO B 260 ? 0.1727 0.1059 0.1251 0.0249  -0.0210 -0.0287 483 PRO B CD  
9391  N N   . GLU B 261 ? 0.2080 0.1344 0.0957 0.0151  -0.0460 0.0088  484 GLU B N   
9392  C CA  . GLU B 261 ? 0.2249 0.1560 0.0926 0.0350  -0.0426 0.0181  484 GLU B CA  
9393  C C   . GLU B 261 ? 0.2183 0.1590 0.0904 0.0377  -0.0353 0.0154  484 GLU B C   
9394  O O   . GLU B 261 ? 0.2562 0.1712 0.1307 0.0354  -0.0073 0.0326  484 GLU B O   
9395  C CB  . GLU B 261 ? 0.2422 0.1974 0.1144 0.0440  -0.0509 0.0371  484 GLU B CB  
9396  C CG  . GLU B 261 ? 0.2733 0.2455 0.1648 0.0445  -0.0552 0.0447  484 GLU B CG  
9397  C CD  . GLU B 261 ? 0.3164 0.2886 0.2183 0.0411  -0.0438 0.0637  484 GLU B CD  
9398  O OE1 . GLU B 261 ? 0.3266 0.2998 0.2442 0.0359  -0.0378 0.0669  484 GLU B OE1 
9399  O OE2 . GLU B 261 ? 0.3459 0.3116 0.2540 0.0404  -0.0377 0.0651  484 GLU B OE2 
9406  N N   . THR B 262 ? 0.2125 0.1589 0.1002 0.0279  -0.0316 -0.0024 485 THR B N   
9407  C CA  . THR B 262 ? 0.2090 0.1590 0.1205 0.0303  -0.0179 -0.0144 485 THR B CA  
9408  C C   . THR B 262 ? 0.2068 0.1807 0.1172 0.0299  0.0024  -0.0054 485 THR B C   
9409  O O   . THR B 262 ? 0.2245 0.2060 0.1463 0.0345  0.0299  0.0063  485 THR B O   
9410  C CB  . THR B 262 ? 0.2004 0.1440 0.1308 0.0354  -0.0508 -0.0158 485 THR B CB  
9411  O OG1 . THR B 262 ? 0.1965 0.1281 0.1250 0.0291  -0.0403 -0.0227 485 THR B OG1 
9412  C CG2 . THR B 262 ? 0.2278 0.1475 0.1367 0.0175  -0.0491 -0.0255 485 THR B CG2 
9420  N N   . GLY B 263 ? 0.1859 0.1873 0.1230 0.0108  0.0003  -0.0226 486 GLY B N   
9421  C CA  . GLY B 263 ? 0.1711 0.1805 0.1411 -0.0087 -0.0033 -0.0104 486 GLY B CA  
9422  C C   . GLY B 263 ? 0.1450 0.1780 0.1581 -0.0084 -0.0236 -0.0020 486 GLY B C   
9423  O O   . GLY B 263 ? 0.1661 0.2092 0.2255 -0.0250 -0.0182 0.0030  486 GLY B O   
9427  N N   . ARG B 264 ? 0.1428 0.1523 0.1400 -0.0070 -0.0075 -0.0134 487 ARG B N   
9428  C CA  . ARG B 264 ? 0.1265 0.1421 0.1366 -0.0002 -0.0122 -0.0339 487 ARG B CA  
9429  C C   . ARG B 264 ? 0.1232 0.1365 0.1258 -0.0002 -0.0124 -0.0380 487 ARG B C   
9430  O O   . ARG B 264 ? 0.1335 0.1417 0.1246 0.0005  -0.0064 -0.0209 487 ARG B O   
9431  C CB  . ARG B 264 ? 0.1241 0.1471 0.1474 -0.0019 -0.0141 -0.0492 487 ARG B CB  
9432  C CG  . ARG B 264 ? 0.1462 0.1629 0.1501 -0.0064 -0.0258 -0.0656 487 ARG B CG  
9433  C CD  . ARG B 264 ? 0.1769 0.1787 0.1592 -0.0099 -0.0155 -0.0582 487 ARG B CD  
9434  N NE  . ARG B 264 ? 0.1795 0.1786 0.1406 -0.0020 -0.0235 -0.0548 487 ARG B NE  
9435  C CZ  . ARG B 264 ? 0.1787 0.1645 0.1547 -0.0002 -0.0369 -0.0547 487 ARG B CZ  
9436  N NH1 . ARG B 264 ? 0.1897 0.1747 0.1785 -0.0081 -0.0372 -0.0405 487 ARG B NH1 
9437  N NH2 . ARG B 264 ? 0.1756 0.1639 0.1626 -0.0009 -0.0559 -0.0666 487 ARG B NH2 
9451  N N   . VAL B 265 ? 0.1288 0.1418 0.1369 0.0130  -0.0120 -0.0339 488 VAL B N   
9452  C CA  . VAL B 265 ? 0.1306 0.1454 0.1327 -0.0015 -0.0304 -0.0242 488 VAL B CA  
9453  C C   . VAL B 265 ? 0.1500 0.1287 0.1160 -0.0196 -0.0288 -0.0420 488 VAL B C   
9454  O O   . VAL B 265 ? 0.1958 0.1619 0.1617 -0.0305 0.0198  -0.0645 488 VAL B O   
9455  C CB  . VAL B 265 ? 0.1695 0.1947 0.1850 -0.0204 -0.0298 -0.0123 488 VAL B CB  
9456  C CG1 . VAL B 265 ? 0.1950 0.2100 0.2200 -0.0134 -0.0220 -0.0125 488 VAL B CG1 
9457  C CG2 . VAL B 265 ? 0.1825 0.2210 0.2069 -0.0300 -0.0359 0.0018  488 VAL B CG2 
9467  N N   . LEU B 266 ? 0.1388 0.1061 0.0989 0.0011  -0.0452 -0.0207 489 LEU B N   
9468  C CA  . LEU B 266 ? 0.1276 0.1140 0.1186 0.0040  -0.0578 -0.0130 489 LEU B CA  
9469  C C   . LEU B 266 ? 0.1047 0.0937 0.1189 0.0015  -0.0435 -0.0114 489 LEU B C   
9470  O O   . LEU B 266 ? 0.1211 0.0876 0.1309 -0.0085 -0.0344 -0.0220 489 LEU B O   
9471  C CB  . LEU B 266 ? 0.1572 0.1574 0.1382 0.0200  -0.0716 0.0039  489 LEU B CB  
9472  C CG  . LEU B 266 ? 0.2187 0.1929 0.1759 0.0210  -0.0831 0.0119  489 LEU B CG  
9473  C CD1 . LEU B 266 ? 0.2606 0.2273 0.2178 0.0461  -0.0636 0.0439  489 LEU B CD1 
9474  C CD2 . LEU B 266 ? 0.2502 0.1881 0.1948 0.0182  -0.0907 0.0089  489 LEU B CD2 
9486  N N   . PHE B 267 ? 0.1035 0.0958 0.1021 0.0171  -0.0401 -0.0207 490 PHE B N   
9487  C CA  . PHE B 267 ? 0.0930 0.0910 0.1084 0.0068  -0.0386 -0.0225 490 PHE B CA  
9488  C C   . PHE B 267 ? 0.0826 0.0780 0.1078 0.0055  -0.0288 -0.0176 490 PHE B C   
9489  O O   . PHE B 267 ? 0.0872 0.0760 0.1044 -0.0005 -0.0336 -0.0156 490 PHE B O   
9490  C CB  . PHE B 267 ? 0.0799 0.0900 0.1206 0.0006  -0.0391 -0.0258 490 PHE B CB  
9491  C CG  . PHE B 267 ? 0.0715 0.0979 0.1057 0.0034  -0.0329 -0.0204 490 PHE B CG  
9492  C CD1 . PHE B 267 ? 0.0852 0.1007 0.1179 -0.0057 -0.0303 -0.0179 490 PHE B CD1 
9493  C CD2 . PHE B 267 ? 0.0716 0.1043 0.1178 0.0069  -0.0221 -0.0157 490 PHE B CD2 
9494  C CE1 . PHE B 267 ? 0.0816 0.1001 0.1290 -0.0128 -0.0299 -0.0183 490 PHE B CE1 
9495  C CE2 . PHE B 267 ? 0.0799 0.1082 0.1298 0.0007  -0.0235 -0.0209 490 PHE B CE2 
9496  C CZ  . PHE B 267 ? 0.0870 0.0906 0.1337 0.0076  -0.0201 -0.0153 490 PHE B CZ  
9506  N N   . GLU B 268 ? 0.0863 0.0755 0.1027 0.0036  -0.0254 -0.0117 491 GLU B N   
9507  C CA  . GLU B 268 ? 0.0640 0.0827 0.1080 -0.0057 -0.0187 -0.0068 491 GLU B CA  
9508  C C   . GLU B 268 ? 0.0704 0.0727 0.1105 -0.0002 -0.0225 -0.0038 491 GLU B C   
9509  O O   . GLU B 268 ? 0.0833 0.0775 0.1070 -0.0022 -0.0203 -0.0232 491 GLU B O   
9510  C CB  . GLU B 268 ? 0.0751 0.0928 0.1130 0.0063  -0.0133 -0.0096 491 GLU B CB  
9511  C CG  . GLU B 268 ? 0.0855 0.0969 0.1132 0.0064  -0.0169 -0.0065 491 GLU B CG  
9512  C CD  . GLU B 268 ? 0.1028 0.1014 0.1301 0.0032  -0.0140 -0.0122 491 GLU B CD  
9513  O OE1 . GLU B 268 ? 0.1133 0.1149 0.1726 0.0101  0.0102  -0.0133 491 GLU B OE1 
9514  O OE2 . GLU B 268 ? 0.1071 0.1172 0.1455 0.0165  -0.0076 -0.0067 491 GLU B OE2 
9521  N N   . ALA B 269 ? 0.0767 0.0785 0.0918 -0.0033 -0.0262 -0.0116 492 ALA B N   
9522  C CA  . ALA B 269 ? 0.0729 0.0624 0.0937 -0.0011 -0.0236 -0.0146 492 ALA B CA  
9523  C C   . ALA B 269 ? 0.0708 0.0633 0.0974 -0.0004 -0.0148 -0.0068 492 ALA B C   
9524  O O   . ALA B 269 ? 0.0667 0.0749 0.1070 -0.0039 -0.0252 0.0046  492 ALA B O   
9525  C CB  . ALA B 269 ? 0.0735 0.0763 0.1061 -0.0040 -0.0066 -0.0168 492 ALA B CB  
9531  N N   . LYS B 270 ? 0.0557 0.0670 0.0985 0.0069  -0.0175 -0.0050 493 LYS B N   
9532  C CA  . LYS B 270 ? 0.0645 0.0790 0.0934 -0.0114 -0.0166 -0.0095 493 LYS B CA  
9533  C C   . LYS B 270 ? 0.0518 0.0796 0.1025 -0.0035 -0.0203 -0.0134 493 LYS B C   
9534  O O   . LYS B 270 ? 0.0740 0.0818 0.1248 -0.0220 0.0111  -0.0360 493 LYS B O   
9535  C CB  . LYS B 270 ? 0.0736 0.0887 0.1119 -0.0060 -0.0346 -0.0012 493 LYS B CB  
9536  C CG  . LYS B 270 ? 0.1007 0.0966 0.1486 0.0004  -0.0433 0.0082  493 LYS B CG  
9537  C CD  . LYS B 270 ? 0.1273 0.1119 0.1996 -0.0180 -0.0076 0.0064  493 LYS B CD  
9538  C CE  . LYS B 270 ? 0.1190 0.1194 0.1935 0.0105  -0.0285 0.0230  493 LYS B CE  
9539  N NZ  . LYS B 270 ? 0.1112 0.0930 0.1646 0.0342  -0.0226 0.0030  493 LYS B NZ  
9553  N N   . LEU B 271 ? 0.0578 0.0728 0.0903 0.0046  -0.0121 -0.0045 494 LEU B N   
9554  C CA  . LEU B 271 ? 0.0538 0.0661 0.1013 -0.0019 -0.0156 -0.0137 494 LEU B CA  
9555  C C   . LEU B 271 ? 0.0434 0.0657 0.0999 0.0003  -0.0136 -0.0046 494 LEU B C   
9556  O O   . LEU B 271 ? 0.0666 0.0823 0.1016 -0.0066 -0.0204 0.0007  494 LEU B O   
9557  C CB  . LEU B 271 ? 0.0924 0.0803 0.1031 -0.0009 -0.0261 0.0067  494 LEU B CB  
9558  C CG  . LEU B 271 ? 0.1010 0.0784 0.1214 0.0057  -0.0331 0.0103  494 LEU B CG  
9559  C CD1 . LEU B 271 ? 0.1124 0.0769 0.1372 0.0031  -0.0178 -0.0028 494 LEU B CD1 
9560  C CD2 . LEU B 271 ? 0.1433 0.0936 0.1307 0.0190  -0.0215 0.0112  494 LEU B CD2 
9572  N N   . HIS B 272 ? 0.0348 0.0805 0.0995 0.0072  -0.0110 -0.0110 495 HIS B N   
9573  C CA  . HIS B 272 ? 0.0356 0.0778 0.0961 0.0073  -0.0210 0.0035  495 HIS B CA  
9574  C C   . HIS B 272 ? 0.0540 0.0761 0.0960 0.0037  -0.0148 0.0007  495 HIS B C   
9575  O O   . HIS B 272 ? 0.0580 0.0796 0.1144 0.0112  -0.0159 -0.0123 495 HIS B O   
9576  C CB  . HIS B 272 ? 0.0539 0.0777 0.0808 0.0068  -0.0069 -0.0029 495 HIS B CB  
9577  C CG  . HIS B 272 ? 0.0587 0.0670 0.0900 0.0097  -0.0037 0.0035  495 HIS B CG  
9578  N ND1 . HIS B 272 ? 0.0799 0.0803 0.1414 0.0048  0.0012  -0.0025 495 HIS B ND1 
9579  C CD2 . HIS B 272 ? 0.0699 0.0749 0.1221 0.0022  -0.0169 -0.0099 495 HIS B CD2 
9580  C CE1 . HIS B 272 ? 0.0733 0.0716 0.1463 0.0097  -0.0217 -0.0144 495 HIS B CE1 
9581  N NE2 . HIS B 272 ? 0.0875 0.0775 0.1336 0.0046  -0.0143 -0.0123 495 HIS B NE2 
9589  N N   . ARG B 273 ? 0.0492 0.0723 0.1133 -0.0025 -0.0110 -0.0037 496 ARG B N   
9590  C CA  . ARG B 273 ? 0.0483 0.0766 0.1293 0.0015  -0.0149 -0.0230 496 ARG B CA  
9591  C C   . ARG B 273 ? 0.0672 0.0802 0.1144 0.0065  -0.0194 -0.0206 496 ARG B C   
9592  O O   . ARG B 273 ? 0.0687 0.0796 0.1269 0.0093  -0.0234 -0.0208 496 ARG B O   
9593  C CB  . ARG B 273 ? 0.0596 0.0926 0.1599 0.0054  -0.0251 -0.0218 496 ARG B CB  
9594  C CG  . ARG B 273 ? 0.0735 0.1273 0.2117 -0.0046 -0.0271 -0.0261 496 ARG B CG  
9595  C CD  . ARG B 273 ? 0.0963 0.1547 0.2558 -0.0248 -0.0384 -0.0470 496 ARG B CD  
9596  N NE  . ARG B 273 ? 0.1317 0.1854 0.2920 -0.0121 -0.0415 -0.0591 496 ARG B NE  
9597  C CZ  . ARG B 273 ? 0.1483 0.2066 0.3149 -0.0184 -0.0604 -0.0696 496 ARG B CZ  
9598  N NH1 . ARG B 273 ? 0.1782 0.2150 0.3250 -0.0103 -0.0526 -0.0807 496 ARG B NH1 
9599  N NH2 . ARG B 273 ? 0.1758 0.2256 0.3398 -0.0475 -0.0602 -0.0672 496 ARG B NH2 
9613  N N   . GLN B 274 ? 0.0754 0.0826 0.0867 0.0125  -0.0272 -0.0118 497 GLN B N   
9614  C CA  . GLN B 274 ? 0.0896 0.1111 0.0783 0.0083  -0.0333 -0.0099 497 GLN B CA  
9615  C C   . GLN B 274 ? 0.0700 0.0994 0.1013 -0.0002 -0.0109 -0.0106 497 GLN B C   
9616  O O   . GLN B 274 ? 0.0837 0.1365 0.0927 0.0134  -0.0069 -0.0226 497 GLN B O   
9617  C CB  . GLN B 274 ? 0.1384 0.1606 0.1125 0.0083  -0.0350 0.0259  497 GLN B CB  
9618  C CG  . GLN B 274 ? 0.2453 0.2218 0.1668 0.0034  0.0051  0.0277  497 GLN B CG  
9619  C CD  . GLN B 274 ? 0.3329 0.2618 0.2227 0.0067  0.0383  0.0304  497 GLN B CD  
9620  O OE1 . GLN B 274 ? 0.3884 0.2700 0.2310 -0.0112 0.0277  0.0361  497 GLN B OE1 
9621  N NE2 . GLN B 274 ? 0.3542 0.2739 0.2604 0.0152  0.0741  0.0239  497 GLN B NE2 
9630  N N   . GLY B 275 ? 0.0540 0.0814 0.1163 -0.0031 -0.0204 -0.0063 498 GLY B N   
9631  C CA  . GLY B 275 ? 0.0773 0.0806 0.1100 -0.0057 -0.0126 -0.0110 498 GLY B CA  
9632  C C   . GLY B 275 ? 0.0718 0.0729 0.1088 0.0038  -0.0079 -0.0077 498 GLY B C   
9633  O O   . GLY B 275 ? 0.0630 0.0773 0.1480 0.0130  -0.0153 -0.0282 498 GLY B O   
9637  N N   . PHE B 276 ? 0.0784 0.0780 0.0970 0.0083  -0.0217 -0.0203 499 PHE B N   
9638  C CA  . PHE B 276 ? 0.0715 0.0792 0.0898 -0.0082 -0.0321 -0.0183 499 PHE B CA  
9639  C C   . PHE B 276 ? 0.0570 0.0641 0.0975 -0.0084 -0.0116 -0.0006 499 PHE B C   
9640  O O   . PHE B 276 ? 0.0436 0.0847 0.1284 -0.0030 -0.0142 -0.0257 499 PHE B O   
9641  C CB  . PHE B 276 ? 0.0799 0.0901 0.1082 -0.0042 -0.0111 -0.0145 499 PHE B CB  
9642  C CG  . PHE B 276 ? 0.0858 0.0971 0.1054 0.0141  -0.0108 -0.0170 499 PHE B CG  
9643  C CD1 . PHE B 276 ? 0.0916 0.1078 0.1277 0.0294  -0.0100 -0.0006 499 PHE B CD1 
9644  C CD2 . PHE B 276 ? 0.1193 0.1052 0.1173 0.0107  -0.0070 -0.0091 499 PHE B CD2 
9645  C CE1 . PHE B 276 ? 0.1211 0.1271 0.1414 0.0302  -0.0053 0.0107  499 PHE B CE1 
9646  C CE2 . PHE B 276 ? 0.1552 0.1158 0.1295 0.0253  -0.0040 -0.0112 499 PHE B CE2 
9647  C CZ  . PHE B 276 ? 0.1405 0.1259 0.1325 0.0470  -0.0008 0.0214  499 PHE B CZ  
9657  N N   . ILE B 277 ? 0.0469 0.0700 0.0983 0.0035  -0.0039 -0.0102 500 ILE B N   
9658  C CA  . ILE B 277 ? 0.0477 0.0686 0.0915 0.0074  -0.0045 -0.0170 500 ILE B CA  
9659  C C   . ILE B 277 ? 0.0691 0.0658 0.0896 0.0152  -0.0079 -0.0199 500 ILE B C   
9660  O O   . ILE B 277 ? 0.0577 0.0694 0.1119 0.0070  -0.0096 -0.0082 500 ILE B O   
9661  C CB  . ILE B 277 ? 0.0540 0.0669 0.1030 0.0093  0.0023  -0.0138 500 ILE B CB  
9662  C CG1 . ILE B 277 ? 0.0634 0.0614 0.1048 0.0026  -0.0076 -0.0052 500 ILE B CG1 
9663  C CG2 . ILE B 277 ? 0.0557 0.0804 0.0953 0.0147  -0.0098 -0.0082 500 ILE B CG2 
9664  C CD1 . ILE B 277 ? 0.0859 0.0796 0.1226 0.0129  -0.0092 0.0074  500 ILE B CD1 
9676  N N   . THR B 278 ? 0.0660 0.0656 0.1072 0.0098  -0.0093 0.0010  501 THR B N   
9677  C CA  . THR B 278 ? 0.0639 0.0626 0.1039 0.0043  -0.0139 -0.0001 501 THR B CA  
9678  C C   . THR B 278 ? 0.0592 0.0700 0.0940 0.0091  -0.0072 -0.0034 501 THR B C   
9679  O O   . THR B 278 ? 0.0631 0.0676 0.0969 0.0092  -0.0122 -0.0093 501 THR B O   
9680  C CB  . THR B 278 ? 0.0701 0.0588 0.1123 0.0007  -0.0167 -0.0017 501 THR B CB  
9681  O OG1 . THR B 278 ? 0.0658 0.0576 0.1237 0.0014  -0.0161 0.0051  501 THR B OG1 
9682  C CG2 . THR B 278 ? 0.1046 0.0815 0.0936 0.0055  -0.0174 0.0015  501 THR B CG2 
9690  N N   . VAL B 279 ? 0.0674 0.0698 0.1001 0.0020  -0.0015 -0.0138 502 VAL B N   
9691  C CA  . VAL B 279 ? 0.0777 0.0698 0.1098 0.0049  -0.0141 -0.0168 502 VAL B CA  
9692  C C   . VAL B 279 ? 0.0794 0.0610 0.1007 0.0020  -0.0148 -0.0131 502 VAL B C   
9693  O O   . VAL B 279 ? 0.0928 0.0642 0.1203 -0.0031 -0.0106 0.0056  502 VAL B O   
9694  C CB  . VAL B 279 ? 0.0741 0.0710 0.1134 0.0138  -0.0114 -0.0164 502 VAL B CB  
9695  C CG1 . VAL B 279 ? 0.0886 0.0757 0.1101 0.0078  -0.0179 -0.0033 502 VAL B CG1 
9696  C CG2 . VAL B 279 ? 0.0643 0.0931 0.1376 0.0112  -0.0142 -0.0074 502 VAL B CG2 
9706  N N   . ALA B 280 ? 0.0772 0.0571 0.1253 0.0095  -0.0122 -0.0080 503 ALA B N   
9707  C CA  . ALA B 280 ? 0.0840 0.0581 0.1420 0.0136  -0.0241 -0.0171 503 ALA B CA  
9708  C C   . ALA B 280 ? 0.0765 0.0674 0.1435 -0.0027 -0.0166 -0.0266 503 ALA B C   
9709  O O   . ALA B 280 ? 0.0813 0.1038 0.1361 -0.0089 -0.0195 -0.0101 503 ALA B O   
9710  C CB  . ALA B 280 ? 0.1104 0.0738 0.1688 0.0147  -0.0157 -0.0089 503 ALA B CB  
9716  N N   . LYS B 281 ? 0.0857 0.0909 0.1670 -0.0174 0.0019  -0.0380 504 LYS B N   
9717  C CA  . LYS B 281 ? 0.0898 0.0990 0.1768 -0.0144 -0.0069 -0.0442 504 LYS B CA  
9718  C C   . LYS B 281 ? 0.1010 0.1139 0.1886 -0.0065 -0.0084 -0.0329 504 LYS B C   
9719  O O   . LYS B 281 ? 0.1228 0.1327 0.1869 -0.0026 -0.0049 -0.0255 504 LYS B O   
9720  C CB  . LYS B 281 ? 0.0898 0.1234 0.1787 -0.0063 -0.0110 -0.0347 504 LYS B CB  
9721  C CG  . LYS B 281 ? 0.0899 0.1409 0.1761 0.0130  -0.0307 -0.0184 504 LYS B CG  
9722  C CD  . LYS B 281 ? 0.1172 0.1363 0.1809 -0.0032 -0.0101 -0.0391 504 LYS B CD  
9723  C CE  . LYS B 281 ? 0.1176 0.1395 0.1916 -0.0049 -0.0009 -0.0419 504 LYS B CE  
9724  N NZ  . LYS B 281 ? 0.1176 0.1474 0.1878 -0.0139 0.0139  -0.0558 504 LYS B NZ  
9738  N N   . SER B 282 ? 0.1127 0.1144 0.2016 -0.0246 -0.0160 -0.0347 505 SER B N   
9739  C CA  A SER B 282 ? 0.1337 0.1426 0.2264 -0.0339 0.0051  -0.0316 505 SER B CA  
9740  C CA  B SER B 282 ? 0.1374 0.1373 0.2261 -0.0317 0.0038  -0.0335 505 SER B CA  
9741  C C   . SER B 282 ? 0.1327 0.1551 0.2249 -0.0430 -0.0013 -0.0445 505 SER B C   
9742  O O   . SER B 282 ? 0.1562 0.2234 0.2492 -0.0581 0.0222  -0.0662 505 SER B O   
9743  C CB  A SER B 282 ? 0.1669 0.1585 0.2594 -0.0335 0.0346  -0.0128 505 SER B CB  
9744  C CB  B SER B 282 ? 0.1844 0.1429 0.2609 -0.0272 0.0349  -0.0161 505 SER B CB  
9745  O OG  A SER B 282 ? 0.1979 0.1742 0.2850 -0.0270 0.0524  0.0041  505 SER B OG  
9746  O OG  B SER B 282 ? 0.2288 0.1470 0.2827 -0.0133 0.0509  -0.0032 505 SER B OG  
9757  N N   . GLY B 283 ? 0.1285 0.1146 0.2087 -0.0359 -0.0201 -0.0167 506 GLY B N   
9758  C CA  . GLY B 283 ? 0.1520 0.1146 0.2194 -0.0342 -0.0085 -0.0030 506 GLY B CA  
9759  C C   . GLY B 283 ? 0.1229 0.1052 0.1959 -0.0341 -0.0352 0.0038  506 GLY B C   
9760  O O   . GLY B 283 ? 0.1219 0.1116 0.2365 -0.0277 -0.0359 0.0072  506 GLY B O   
9764  N N   . ASP B 284 ? 0.1089 0.1019 0.1718 -0.0434 -0.0242 0.0083  507 ASP B N   
9765  C CA  . ASP B 284 ? 0.1066 0.1129 0.1490 -0.0504 -0.0181 -0.0014 507 ASP B CA  
9766  C C   . ASP B 284 ? 0.1236 0.1229 0.1631 -0.0651 -0.0144 -0.0065 507 ASP B C   
9767  O O   . ASP B 284 ? 0.1428 0.1465 0.1897 -0.0764 -0.0138 0.0008  507 ASP B O   
9768  C CB  . ASP B 284 ? 0.1139 0.1278 0.1554 -0.0423 -0.0281 -0.0163 507 ASP B CB  
9769  C CG  . ASP B 284 ? 0.1323 0.1415 0.1648 -0.0286 -0.0194 -0.0177 507 ASP B CG  
9770  O OD1 . ASP B 284 ? 0.1311 0.1408 0.1717 -0.0287 -0.0275 -0.0299 507 ASP B OD1 
9771  O OD2 . ASP B 284 ? 0.1796 0.1591 0.1625 -0.0092 0.0020  -0.0089 507 ASP B OD2 
9776  N N   . SER B 285 ? 0.1186 0.1360 0.1679 -0.0715 -0.0109 -0.0097 508 SER B N   
9777  C CA  . SER B 285 ? 0.1229 0.1341 0.1574 -0.0414 -0.0047 -0.0219 508 SER B CA  
9778  C C   . SER B 285 ? 0.1273 0.1358 0.1442 -0.0293 0.0142  -0.0408 508 SER B C   
9779  O O   . SER B 285 ? 0.1364 0.1308 0.1470 -0.0304 0.0074  -0.0164 508 SER B O   
9780  C CB  . SER B 285 ? 0.1300 0.1355 0.1678 -0.0181 0.0035  -0.0106 508 SER B CB  
9781  O OG  . SER B 285 ? 0.1446 0.1357 0.1724 -0.0218 -0.0030 -0.0257 508 SER B OG  
9787  N N   . PRO B 286 ? 0.1254 0.1506 0.1507 -0.0081 0.0226  -0.0256 509 PRO B N   
9788  C CA  . PRO B 286 ? 0.1290 0.1662 0.1526 -0.0033 -0.0028 -0.0155 509 PRO B CA  
9789  C C   . PRO B 286 ? 0.1402 0.1518 0.1434 0.0124  0.0209  -0.0109 509 PRO B C   
9790  O O   . PRO B 286 ? 0.1559 0.1398 0.1499 -0.0044 0.0135  -0.0323 509 PRO B O   
9791  C CB  . PRO B 286 ? 0.1372 0.1855 0.1643 -0.0214 -0.0181 -0.0191 509 PRO B CB  
9792  C CG  . PRO B 286 ? 0.1436 0.1907 0.1667 -0.0076 -0.0063 -0.0041 509 PRO B CG  
9793  C CD  . PRO B 286 ? 0.1257 0.1773 0.1565 -0.0037 0.0055  -0.0064 509 PRO B CD  
9801  N N   . ILE B 287 ? 0.1453 0.1475 0.1235 0.0208  0.0130  -0.0176 510 ILE B N   
9802  C CA  . ILE B 287 ? 0.1544 0.1199 0.1156 0.0180  0.0008  -0.0123 510 ILE B CA  
9803  C C   . ILE B 287 ? 0.1528 0.1142 0.1147 0.0146  -0.0127 -0.0122 510 ILE B C   
9804  O O   . ILE B 287 ? 0.1773 0.1283 0.1397 0.0397  0.0032  -0.0045 510 ILE B O   
9805  C CB  . ILE B 287 ? 0.1660 0.1145 0.0984 0.0300  -0.0112 -0.0006 510 ILE B CB  
9806  C CG1 . ILE B 287 ? 0.1798 0.1174 0.0999 0.0135  -0.0108 -0.0062 510 ILE B CG1 
9807  C CG2 . ILE B 287 ? 0.1943 0.1100 0.1082 0.0246  0.0029  -0.0189 510 ILE B CG2 
9808  C CD1 . ILE B 287 ? 0.1823 0.1229 0.1033 0.0179  -0.0296 -0.0181 510 ILE B CD1 
9820  N N   . ASN B 288 ? 0.1292 0.1170 0.1026 -0.0073 -0.0272 -0.0098 511 ASN B N   
9821  C CA  . ASN B 288 ? 0.1223 0.1090 0.1099 -0.0089 -0.0212 -0.0067 511 ASN B CA  
9822  C C   . ASN B 288 ? 0.1150 0.1099 0.1068 -0.0131 -0.0006 -0.0044 511 ASN B C   
9823  O O   . ASN B 288 ? 0.1088 0.1122 0.1209 -0.0141 -0.0094 -0.0246 511 ASN B O   
9824  C CB  . ASN B 288 ? 0.1117 0.1220 0.1244 -0.0154 -0.0249 -0.0079 511 ASN B CB  
9825  C CG  . ASN B 288 ? 0.0975 0.1388 0.1353 -0.0155 -0.0208 -0.0085 511 ASN B CG  
9826  O OD1 . ASN B 288 ? 0.1154 0.1550 0.1729 -0.0104 -0.0145 -0.0050 511 ASN B OD1 
9827  N ND2 . ASN B 288 ? 0.0913 0.1421 0.1314 -0.0196 -0.0136 0.0126  511 ASN B ND2 
9834  N N   . VAL B 289 ? 0.1210 0.1052 0.1165 -0.0062 -0.0131 -0.0122 512 VAL B N   
9835  C CA  . VAL B 289 ? 0.1297 0.1029 0.1336 -0.0232 -0.0141 -0.0209 512 VAL B CA  
9836  C C   . VAL B 289 ? 0.1450 0.1097 0.1412 -0.0229 -0.0212 -0.0213 512 VAL B C   
9837  O O   . VAL B 289 ? 0.1417 0.1277 0.1648 0.0025  -0.0183 -0.0087 512 VAL B O   
9838  C CB  . VAL B 289 ? 0.1582 0.1159 0.1307 -0.0226 -0.0192 -0.0147 512 VAL B CB  
9839  C CG1 . VAL B 289 ? 0.1398 0.1389 0.1487 -0.0125 -0.0468 -0.0064 512 VAL B CG1 
9840  C CG2 . VAL B 289 ? 0.1885 0.1352 0.1408 -0.0205 -0.0276 -0.0173 512 VAL B CG2 
9850  N N   . PRO B 290 ? 0.1551 0.0993 0.1440 -0.0286 -0.0367 -0.0085 513 PRO B N   
9851  C CA  . PRO B 290 ? 0.1497 0.1176 0.1466 -0.0209 -0.0513 -0.0163 513 PRO B CA  
9852  C C   . PRO B 290 ? 0.1179 0.1161 0.1431 -0.0042 -0.0699 -0.0026 513 PRO B C   
9853  O O   . PRO B 290 ? 0.1231 0.1151 0.1493 -0.0058 -0.0600 -0.0118 513 PRO B O   
9854  C CB  . PRO B 290 ? 0.1959 0.1214 0.1209 -0.0207 -0.0373 -0.0112 513 PRO B CB  
9855  C CG  . PRO B 290 ? 0.2032 0.1083 0.1154 -0.0296 -0.0054 -0.0175 513 PRO B CG  
9856  C CD  . PRO B 290 ? 0.1893 0.1078 0.1501 -0.0205 -0.0128 0.0002  513 PRO B CD  
9864  N N   . ALA B 291 ? 0.1170 0.1442 0.1558 -0.0074 -0.0631 -0.0164 514 ALA B N   
9865  C CA  . ALA B 291 ? 0.1101 0.1493 0.1855 0.0106  -0.0510 -0.0142 514 ALA B CA  
9866  C C   . ALA B 291 ? 0.1043 0.1247 0.1661 0.0240  -0.0495 -0.0156 514 ALA B C   
9867  O O   . ALA B 291 ? 0.1039 0.1391 0.1759 0.0269  -0.0487 -0.0403 514 ALA B O   
9868  C CB  . ALA B 291 ? 0.1239 0.1640 0.2131 0.0044  -0.0412 -0.0342 514 ALA B CB  
9874  N N   . ASN B 292 ? 0.1176 0.1120 0.1520 0.0086  -0.0477 -0.0197 515 ASN B N   
9875  C CA  . ASN B 292 ? 0.1356 0.0934 0.1496 0.0193  -0.0392 -0.0138 515 ASN B CA  
9876  C C   . ASN B 292 ? 0.1277 0.0996 0.1486 0.0067  -0.0429 -0.0208 515 ASN B C   
9877  O O   . ASN B 292 ? 0.1504 0.1065 0.1578 -0.0075 -0.0363 -0.0257 515 ASN B O   
9878  C CB  . ASN B 292 ? 0.1684 0.1071 0.1383 0.0179  -0.0399 -0.0065 515 ASN B CB  
9879  C CG  . ASN B 292 ? 0.1741 0.1109 0.1412 0.0204  -0.0414 -0.0105 515 ASN B CG  
9880  O OD1 . ASN B 292 ? 0.1618 0.1077 0.1606 0.0279  -0.0406 -0.0153 515 ASN B OD1 
9881  N ND2 . ASN B 292 ? 0.1974 0.1277 0.1543 0.0448  -0.0297 -0.0050 515 ASN B ND2 
9888  N N   . GLY B 293 ? 0.1043 0.1055 0.1392 0.0020  -0.0480 -0.0090 516 GLY B N   
9889  C CA  . GLY B 293 ? 0.0817 0.1001 0.1115 0.0095  -0.0457 -0.0139 516 GLY B CA  
9890  C C   . GLY B 293 ? 0.0706 0.0953 0.0970 0.0016  -0.0248 -0.0059 516 GLY B C   
9891  O O   . GLY B 293 ? 0.0745 0.1154 0.1032 0.0059  -0.0158 -0.0098 516 GLY B O   
9895  N N   . TYR B 294 ? 0.0757 0.0870 0.0984 0.0111  -0.0164 -0.0075 517 TYR B N   
9896  C CA  . TYR B 294 ? 0.0765 0.0841 0.0870 0.0077  -0.0433 -0.0129 517 TYR B CA  
9897  C C   . TYR B 294 ? 0.0825 0.0794 0.0871 0.0025  -0.0283 -0.0120 517 TYR B C   
9898  O O   . TYR B 294 ? 0.0896 0.0926 0.0925 0.0026  -0.0163 -0.0124 517 TYR B O   
9899  C CB  . TYR B 294 ? 0.0935 0.0788 0.1100 0.0284  -0.0402 -0.0093 517 TYR B CB  
9900  C CG  . TYR B 294 ? 0.1413 0.0916 0.1077 -0.0042 -0.0336 -0.0060 517 TYR B CG  
9901  C CD1 . TYR B 294 ? 0.1387 0.0940 0.1177 -0.0042 -0.0124 0.0068  517 TYR B CD1 
9902  C CD2 . TYR B 294 ? 0.1829 0.1293 0.1232 -0.0198 -0.0235 -0.0012 517 TYR B CD2 
9903  C CE1 . TYR B 294 ? 0.1505 0.1297 0.1407 -0.0195 -0.0180 0.0013  517 TYR B CE1 
9904  C CE2 . TYR B 294 ? 0.1909 0.1540 0.1175 -0.0295 -0.0284 0.0091  517 TYR B CE2 
9905  C CZ  . TYR B 294 ? 0.1878 0.1564 0.1422 -0.0520 -0.0026 0.0013  517 TYR B CZ  
9906  O OH  . TYR B 294 ? 0.2382 0.1972 0.1675 -0.0622 0.0295  -0.0048 517 TYR B OH  
9916  N N   . PHE B 295 ? 0.0761 0.0835 0.0876 0.0169  -0.0187 -0.0134 518 PHE B N   
9917  C CA  . PHE B 295 ? 0.0614 0.0786 0.0961 0.0046  -0.0302 -0.0026 518 PHE B CA  
9918  C C   . PHE B 295 ? 0.0703 0.0807 0.1102 0.0088  -0.0259 0.0119  518 PHE B C   
9919  O O   . PHE B 295 ? 0.0871 0.0850 0.1486 0.0062  -0.0158 0.0003  518 PHE B O   
9920  C CB  . PHE B 295 ? 0.0636 0.0833 0.0951 0.0024  -0.0292 0.0034  518 PHE B CB  
9921  C CG  . PHE B 295 ? 0.0871 0.0824 0.0824 -0.0005 -0.0216 0.0037  518 PHE B CG  
9922  C CD1 . PHE B 295 ? 0.0868 0.0824 0.0985 0.0025  -0.0401 0.0003  518 PHE B CD1 
9923  C CD2 . PHE B 295 ? 0.0972 0.0777 0.0975 -0.0112 -0.0185 -0.0080 518 PHE B CD2 
9924  C CE1 . PHE B 295 ? 0.1086 0.0932 0.1158 -0.0083 -0.0288 0.0041  518 PHE B CE1 
9925  C CE2 . PHE B 295 ? 0.1072 0.0885 0.0941 -0.0261 -0.0102 -0.0118 518 PHE B CE2 
9926  C CZ  . PHE B 295 ? 0.1187 0.0841 0.1002 -0.0326 -0.0101 -0.0115 518 PHE B CZ  
9936  N N   . ARG B 296 ? 0.0687 0.0862 0.1232 0.0101  -0.0138 0.0029  519 ARG B N   
9937  C CA  . ARG B 296 ? 0.0798 0.1041 0.1160 0.0070  -0.0187 0.0218  519 ARG B CA  
9938  C C   . ARG B 296 ? 0.0718 0.0884 0.1139 0.0018  -0.0025 0.0112  519 ARG B C   
9939  O O   . ARG B 296 ? 0.0891 0.0809 0.1354 -0.0016 -0.0177 0.0035  519 ARG B O   
9940  C CB  . ARG B 296 ? 0.1125 0.1512 0.1374 0.0220  -0.0172 0.0396  519 ARG B CB  
9941  C CG  . ARG B 296 ? 0.1610 0.1947 0.1399 0.0206  -0.0056 0.0133  519 ARG B CG  
9942  C CD  . ARG B 296 ? 0.1955 0.2402 0.1594 0.0307  0.0058  0.0148  519 ARG B CD  
9943  N NE  . ARG B 296 ? 0.2270 0.2767 0.2148 0.0139  0.0325  -0.0227 519 ARG B NE  
9944  C CZ  . ARG B 296 ? 0.2648 0.3066 0.2743 -0.0123 0.0483  -0.0473 519 ARG B CZ  
9945  N NH1 . ARG B 296 ? 0.2607 0.3270 0.2725 -0.0259 0.0321  -0.0526 519 ARG B NH1 
9946  N NH2 . ARG B 296 ? 0.2891 0.3122 0.3065 -0.0282 0.0578  -0.0681 519 ARG B NH2 
9960  N N   . PHE B 297 ? 0.0695 0.0952 0.1061 0.0129  -0.0074 0.0057  520 PHE B N   
9961  C CA  . PHE B 297 ? 0.0554 0.1060 0.1276 0.0001  -0.0105 0.0014  520 PHE B CA  
9962  C C   . PHE B 297 ? 0.0766 0.1330 0.1299 0.0286  -0.0021 0.0349  520 PHE B C   
9963  O O   . PHE B 297 ? 0.1263 0.1748 0.1673 0.0467  0.0525  0.0720  520 PHE B O   
9964  C CB  . PHE B 297 ? 0.0797 0.1189 0.1593 0.0030  -0.0263 -0.0086 520 PHE B CB  
9965  C CG  . PHE B 297 ? 0.0923 0.1458 0.1772 0.0105  -0.0379 0.0103  520 PHE B CG  
9966  C CD1 . PHE B 297 ? 0.1070 0.1584 0.1465 0.0245  -0.0286 -0.0040 520 PHE B CD1 
9967  C CD2 . PHE B 297 ? 0.1102 0.1660 0.2113 -0.0121 -0.0563 0.0380  520 PHE B CD2 
9968  C CE1 . PHE B 297 ? 0.1166 0.1613 0.1494 0.0380  -0.0366 0.0011  520 PHE B CE1 
9969  C CE2 . PHE B 297 ? 0.1137 0.1736 0.2300 -0.0097 -0.0444 0.0339  520 PHE B CE2 
9970  C CZ  . PHE B 297 ? 0.1110 0.1578 0.1881 0.0053  -0.0631 -0.0007 520 PHE B CZ  
9980  N N   . ASP B 298 ? 0.0815 0.1309 0.0999 0.0317  -0.0045 0.0095  521 ASP B N   
9981  C CA  A ASP B 298 ? 0.0908 0.1437 0.1081 0.0258  -0.0082 -0.0001 521 ASP B CA  
9982  C CA  B ASP B 298 ? 0.0978 0.1515 0.1332 0.0317  -0.0009 -0.0004 521 ASP B CA  
9983  C C   . ASP B 298 ? 0.0912 0.1515 0.1187 0.0280  0.0002  0.0139  521 ASP B C   
9984  O O   . ASP B 298 ? 0.1071 0.1948 0.1246 0.0054  0.0224  0.0212  521 ASP B O   
9985  C CB  A ASP B 298 ? 0.0975 0.1550 0.0869 0.0292  -0.0255 -0.0218 521 ASP B CB  
9986  C CB  B ASP B 298 ? 0.1151 0.1660 0.1690 0.0470  -0.0060 -0.0117 521 ASP B CB  
9987  C CG  A ASP B 298 ? 0.1292 0.1665 0.0768 0.0452  -0.0188 -0.0232 521 ASP B CG  
9988  C CG  B ASP B 298 ? 0.1314 0.1693 0.1991 0.0613  -0.0149 0.0097  521 ASP B CG  
9989  O OD1 A ASP B 298 ? 0.1769 0.1948 0.1050 0.0447  -0.0062 -0.0454 521 ASP B OD1 
9990  O OD1 B ASP B 298 ? 0.1394 0.1741 0.2040 0.0608  -0.0230 0.0099  521 ASP B OD1 
9991  O OD2 A ASP B 298 ? 0.1164 0.1546 0.0872 0.0564  0.0098  -0.0091 521 ASP B OD2 
9992  O OD2 B ASP B 298 ? 0.1317 0.1844 0.2255 0.0478  -0.0092 0.0141  521 ASP B OD2 
10001 N N   . SER B 299 ? 0.0779 0.1304 0.1155 0.0258  -0.0062 -0.0023 522 SER B N   
10002 C CA  . SER B 299 ? 0.0757 0.1458 0.1447 0.0205  -0.0153 -0.0013 522 SER B CA  
10003 C C   . SER B 299 ? 0.0629 0.1382 0.1322 0.0172  -0.0058 0.0060  522 SER B C   
10004 O O   . SER B 299 ? 0.0554 0.1460 0.1439 0.0096  0.0022  -0.0057 522 SER B O   
10005 C CB  . SER B 299 ? 0.1004 0.1563 0.1609 0.0233  0.0005  -0.0125 522 SER B CB  
10006 O OG  . SER B 299 ? 0.1254 0.1533 0.1869 0.0413  -0.0039 -0.0080 522 SER B OG  
10012 N N   . TRP B 300 ? 0.0620 0.1482 0.1288 0.0013  -0.0011 0.0117  523 TRP B N   
10013 C CA  . TRP B 300 ? 0.0645 0.1378 0.1231 0.0116  -0.0067 0.0042  523 TRP B CA  
10014 C C   . TRP B 300 ? 0.0859 0.1446 0.1355 0.0242  0.0128  -0.0035 523 TRP B C   
10015 O O   . TRP B 300 ? 0.1067 0.1556 0.1713 0.0356  0.0368  0.0173  523 TRP B O   
10016 C CB  . TRP B 300 ? 0.0732 0.1345 0.1346 0.0022  -0.0021 0.0055  523 TRP B CB  
10017 C CG  . TRP B 300 ? 0.0606 0.1280 0.1371 0.0037  -0.0131 0.0195  523 TRP B CG  
10018 C CD1 . TRP B 300 ? 0.0735 0.1455 0.1505 -0.0052 -0.0093 0.0261  523 TRP B CD1 
10019 C CD2 . TRP B 300 ? 0.0514 0.1185 0.1467 -0.0128 -0.0134 0.0192  523 TRP B CD2 
10020 N NE1 . TRP B 300 ? 0.0806 0.1496 0.1533 -0.0102 -0.0133 0.0328  523 TRP B NE1 
10021 C CE2 . TRP B 300 ? 0.0655 0.1355 0.1547 -0.0020 -0.0302 0.0166  523 TRP B CE2 
10022 C CE3 . TRP B 300 ? 0.0562 0.1179 0.1574 -0.0057 -0.0227 0.0177  523 TRP B CE3 
10023 C CZ2 . TRP B 300 ? 0.0857 0.1212 0.1566 0.0112  -0.0333 0.0203  523 TRP B CZ2 
10024 C CZ3 . TRP B 300 ? 0.0799 0.1087 0.1572 0.0101  -0.0216 0.0167  523 TRP B CZ3 
10025 C CH2 . TRP B 300 ? 0.0818 0.1141 0.1511 0.0111  -0.0262 0.0108  523 TRP B CH2 
10036 N N   . VAL B 301 ? 0.0682 0.1342 0.1332 0.0287  -0.0038 -0.0036 524 VAL B N   
10037 C CA  . VAL B 301 ? 0.0884 0.1218 0.1436 0.0308  -0.0165 -0.0131 524 VAL B CA  
10038 C C   . VAL B 301 ? 0.0878 0.1039 0.1421 0.0524  -0.0157 -0.0097 524 VAL B C   
10039 O O   . VAL B 301 ? 0.1261 0.1125 0.1423 0.0133  -0.0288 -0.0080 524 VAL B O   
10040 C CB  . VAL B 301 ? 0.1039 0.1103 0.1412 0.0280  -0.0081 -0.0097 524 VAL B CB  
10041 C CG1 . VAL B 301 ? 0.1257 0.1354 0.1565 0.0317  0.0065  -0.0334 524 VAL B CG1 
10042 C CG2 . VAL B 301 ? 0.1052 0.1092 0.1442 0.0244  -0.0168 -0.0057 524 VAL B CG2 
10052 N N   . ASN B 302 ? 0.1058 0.1022 0.1393 0.0292  -0.0121 -0.0096 525 ASN B N   
10053 C CA  . ASN B 302 ? 0.0940 0.1137 0.1546 0.0156  -0.0301 -0.0040 525 ASN B CA  
10054 C C   . ASN B 302 ? 0.0902 0.0833 0.1587 0.0163  -0.0340 0.0095  525 ASN B C   
10055 O O   . ASN B 302 ? 0.1060 0.0902 0.1452 -0.0025 -0.0347 0.0104  525 ASN B O   
10056 C CB  . ASN B 302 ? 0.0728 0.1402 0.1843 0.0135  -0.0369 -0.0009 525 ASN B CB  
10057 C CG  . ASN B 302 ? 0.1002 0.1596 0.2043 0.0390  -0.0369 0.0047  525 ASN B CG  
10058 O OD1 . ASN B 302 ? 0.1311 0.1374 0.2150 0.0363  -0.0310 0.0042  525 ASN B OD1 
10059 N ND2 . ASN B 302 ? 0.1359 0.1903 0.2390 0.0471  -0.0283 -0.0180 525 ASN B ND2 
10066 N N   . GLN B 303 ? 0.0895 0.0809 0.1576 0.0089  -0.0417 0.0118  526 GLN B N   
10067 C CA  . GLN B 303 ? 0.1053 0.0960 0.1604 0.0005  -0.0554 0.0086  526 GLN B CA  
10068 C C   . GLN B 303 ? 0.1173 0.0972 0.1795 0.0022  -0.0632 0.0092  526 GLN B C   
10069 O O   . GLN B 303 ? 0.1282 0.1177 0.2083 -0.0073 -0.0548 0.0017  526 GLN B O   
10070 C CB  . GLN B 303 ? 0.1023 0.1079 0.1528 0.0019  -0.0476 0.0115  526 GLN B CB  
10071 C CG  . GLN B 303 ? 0.1150 0.1277 0.1479 -0.0072 -0.0384 0.0203  526 GLN B CG  
10072 C CD  . GLN B 303 ? 0.1323 0.1614 0.1523 -0.0132 -0.0312 0.0455  526 GLN B CD  
10073 O OE1 . GLN B 303 ? 0.1435 0.1972 0.1751 -0.0372 -0.0258 0.0622  526 GLN B OE1 
10074 N NE2 . GLN B 303 ? 0.1521 0.1713 0.1455 0.0001  -0.0329 0.0399  526 GLN B NE2 
10083 N N   . PHE B 304 ? 0.1358 0.0934 0.1850 0.0150  -0.0729 -0.0189 527 PHE B N   
10084 C CA  . PHE B 304 ? 0.1552 0.1029 0.1999 0.0386  -0.0703 -0.0066 527 PHE B CA  
10085 C C   . PHE B 304 ? 0.1437 0.1189 0.1933 0.0233  -0.0850 -0.0215 527 PHE B C   
10086 O O   . PHE B 304 ? 0.1669 0.1350 0.1971 0.0176  -0.0595 -0.0322 527 PHE B O   
10087 C CB  . PHE B 304 ? 0.1716 0.1239 0.2082 0.0439  -0.0682 -0.0028 527 PHE B CB  
10088 C CG  . PHE B 304 ? 0.1652 0.1415 0.2161 0.0475  -0.0849 0.0101  527 PHE B CG  
10089 C CD1 . PHE B 304 ? 0.1909 0.1395 0.2379 0.0467  -0.0726 0.0293  527 PHE B CD1 
10090 C CD2 . PHE B 304 ? 0.1463 0.1694 0.2292 0.0401  -0.0903 0.0107  527 PHE B CD2 
10091 C CE1 . PHE B 304 ? 0.1977 0.1587 0.2489 0.0319  -0.0706 0.0246  527 PHE B CE1 
10092 C CE2 . PHE B 304 ? 0.1611 0.1789 0.2337 0.0359  -0.0988 0.0206  527 PHE B CE2 
10093 C CZ  . PHE B 304 ? 0.1786 0.1742 0.2436 0.0290  -0.0966 0.0241  527 PHE B CZ  
10103 N N   . TYR B 305 ? 0.1364 0.1169 0.1790 0.0338  -0.0676 -0.0146 528 TYR B N   
10104 C CA  . TYR B 305 ? 0.1233 0.1150 0.1676 0.0260  -0.0523 -0.0249 528 TYR B CA  
10105 C C   . TYR B 305 ? 0.1192 0.1114 0.1632 0.0140  -0.0379 -0.0202 528 TYR B C   
10106 O O   . TYR B 305 ? 0.1414 0.1251 0.1577 0.0090  -0.0117 -0.0167 528 TYR B O   
10107 C CB  . TYR B 305 ? 0.1299 0.1129 0.1549 0.0167  -0.0377 -0.0215 528 TYR B CB  
10108 C CG  . TYR B 305 ? 0.1524 0.1220 0.1506 0.0194  -0.0089 -0.0308 528 TYR B CG  
10109 C CD1 . TYR B 305 ? 0.1851 0.1584 0.1578 0.0083  0.0142  -0.0403 528 TYR B CD1 
10110 C CD2 . TYR B 305 ? 0.1642 0.1251 0.1491 0.0444  0.0038  -0.0129 528 TYR B CD2 
10111 C CE1 . TYR B 305 ? 0.2019 0.1696 0.1630 -0.0043 0.0208  -0.0418 528 TYR B CE1 
10112 C CE2 . TYR B 305 ? 0.1876 0.1445 0.1564 0.0417  0.0030  -0.0141 528 TYR B CE2 
10113 C CZ  . TYR B 305 ? 0.2161 0.1679 0.1601 0.0082  0.0178  -0.0287 528 TYR B CZ  
10114 O OH  . TYR B 305 ? 0.2558 0.1868 0.1669 -0.0096 0.0392  -0.0380 528 TYR B OH  
10124 N N   . SER B 306 ? 0.1057 0.1035 0.1560 0.0166  -0.0385 -0.0226 529 SER B N   
10125 C CA  A SER B 306 ? 0.1151 0.1016 0.1543 0.0165  -0.0402 -0.0276 529 SER B CA  
10126 C CA  B SER B 306 ? 0.1187 0.1076 0.1602 0.0105  -0.0374 -0.0242 529 SER B CA  
10127 C C   . SER B 306 ? 0.1017 0.1019 0.1553 0.0155  -0.0288 -0.0181 529 SER B C   
10128 O O   . SER B 306 ? 0.1213 0.1412 0.1750 0.0342  -0.0076 -0.0128 529 SER B O   
10129 C CB  A SER B 306 ? 0.1308 0.0976 0.1692 0.0289  -0.0562 -0.0354 529 SER B CB  
10130 C CB  B SER B 306 ? 0.1410 0.1145 0.1916 0.0156  -0.0468 -0.0237 529 SER B CB  
10131 O OG  A SER B 306 ? 0.1507 0.1034 0.1889 0.0388  -0.0648 -0.0406 529 SER B OG  
10132 O OG  B SER B 306 ? 0.1706 0.1346 0.2268 0.0206  -0.0441 -0.0205 529 SER B OG  
10143 N N   . LEU B 307 ? 0.0856 0.0905 0.1549 0.0257  -0.0162 0.0013  530 LEU B N   
10144 C CA  . LEU B 307 ? 0.0931 0.0913 0.1542 0.0209  -0.0125 -0.0154 530 LEU B CA  
10145 C C   . LEU B 307 ? 0.1039 0.1034 0.1657 0.0215  -0.0069 -0.0196 530 LEU B C   
10146 O O   . LEU B 307 ? 0.1411 0.0998 0.1714 0.0196  -0.0215 -0.0133 530 LEU B O   
10147 C CB  . LEU B 307 ? 0.0881 0.0879 0.1517 0.0096  -0.0002 -0.0134 530 LEU B CB  
10148 C CG  . LEU B 307 ? 0.0905 0.0782 0.1436 -0.0055 -0.0081 -0.0178 530 LEU B CG  
10149 C CD1 . LEU B 307 ? 0.0939 0.0641 0.1498 0.0176  0.0049  -0.0112 530 LEU B CD1 
10150 C CD2 . LEU B 307 ? 0.1117 0.0760 0.1594 0.0117  -0.0008 0.0019  530 LEU B CD2 
10162 N N   . ALA B 308 ? 0.0995 0.1038 0.1485 0.0157  -0.0068 -0.0210 531 ALA B N   
10163 C CA  . ALA B 308 ? 0.1157 0.1126 0.1473 0.0195  -0.0193 -0.0271 531 ALA B CA  
10164 C C   . ALA B 308 ? 0.1220 0.0927 0.1515 0.0220  -0.0260 -0.0201 531 ALA B C   
10165 O O   . ALA B 308 ? 0.1227 0.0848 0.1246 0.0273  -0.0371 -0.0174 531 ALA B O   
10166 C CB  . ALA B 308 ? 0.1278 0.1406 0.1450 0.0062  -0.0100 -0.0382 531 ALA B CB  
10172 N N   . PRO B 309 ? 0.1511 0.0928 0.2166 0.0196  -0.0051 -0.0285 532 PRO B N   
10173 C CA  . PRO B 309 ? 0.1580 0.1216 0.2164 0.0079  -0.0033 -0.0269 532 PRO B CA  
10174 C C   . PRO B 309 ? 0.1288 0.1391 0.1665 -0.0061 -0.0111 -0.0515 532 PRO B C   
10175 O O   . PRO B 309 ? 0.1529 0.1822 0.1879 -0.0122 -0.0075 -0.0599 532 PRO B O   
10176 C CB  . PRO B 309 ? 0.1868 0.1392 0.2697 0.0035  0.0214  -0.0216 532 PRO B CB  
10177 C CG  . PRO B 309 ? 0.2153 0.1478 0.2909 -0.0087 0.0319  -0.0342 532 PRO B CG  
10178 C CD  . PRO B 309 ? 0.1996 0.1124 0.2711 0.0011  0.0255  -0.0366 532 PRO B CD  
# 
