data_9HY2
# 
_entry.id   9HY2 
# 
_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   9HY2         pdb_00009hy2 10.2210/pdb9hy2/pdb 
WWPDB D_1292144433 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HY2 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9HY3 unspecified 
PDB . 9HY5 unspecified 
PDB . 9HY1 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pozzi4@unisi.it 
_pdbx_contact_author.name_first         Cecilia 
_pdbx_contact_author.name_last          Pozzi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2574-3911 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Raucci, L.'    1 0000-0001-5771-0220 
'Orlandini, M.' 2 0000-0002-6112-4889 
'Pozzi, C.'     3 0000-0003-2574-3911 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            309 
_citation.language                  ? 
_citation.page_first                143118 
_citation.page_last                 143118 
_citation.title                     
;Structural and antigen-binding surface definition of an anti-CD93 monoclonal antibody for the treatment of degenerative vascular eye diseases.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2025.143118 
_citation.pdbx_database_id_PubMed   40228767 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Raucci, L.'    1  ? 
primary 'Perrone, C.D.' 2  ? 
primary 'Barbera, S.'   3  ? 
primary 'de Boer, L.J.' 4  ? 
primary 'Tosi, G.M.'    5  ? 
primary 'Brunetti, J.'  6  ? 
primary 'Bracci, L.'    7  ? 
primary 'Pozzi, C.'     8  ? 
primary 'Galvagni, F.'  9  ? 
primary 'Orlandini, M.' 10 ? 
# 
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 'sc-4E (scFv derived from the mAb 4E1 against CD93)' 28852.492 1   ? ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                                       62.068    2   ? ? ? ? 
3 non-polymer syn IMIDAZOLE                                            69.085    1   ? ? ? ? 
4 non-polymer syn 'SODIUM ION'                                         22.990    2   ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                       35.453    2   ? ? ? ? 
6 water       nat water                                                18.015    268 ? ? ? ? 
# 
_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       
;MDQEQLQQPGTELVKPGASVRLSCKTSGYTFASYTLHWVKQTPGQGLDWIGAIYPGNGDTSYNQKFKDKATLTADKSSST
AYMQLSNLTSEDSAVYYCARLDWYFDLWGAGTTVTVSAAGGGGSGGGGSGGGGSDIVLTQSPTSLAVSLGQRATISCKAS
QSVDYDGDSYMNWYQQKPGQPPRLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQNNEDPRTFGGGT
KLEIKLEMGSSHHHHHHSSGENLYFQGHM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQEQLQQPGTELVKPGASVRLSCKTSGYTFASYTLHWVKQTPGQGLDWIGAIYPGNGDTSYNQKFKDKATLTADKSSST
AYMQLSNLTSEDSAVYYCARLDWYFDLWGAGTTVTVSAAGGGGSGGGGSGGGGSDIVLTQSPTSLAVSLGQRATISCKAS
QSVDYDGDSYMNWYQQKPGQPPRLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQNNEDPRTFGGGT
KLEIKLEMGSSHHHHHHSSGENLYFQGHM
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL EDO 
3 IMIDAZOLE      IMD 
4 'SODIUM ION'   NA  
5 'CHLORIDE ION' CL  
6 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLN n 
1 4   GLU n 
1 5   GLN n 
1 6   LEU n 
1 7   GLN n 
1 8   GLN n 
1 9   PRO n 
1 10  GLY n 
1 11  THR n 
1 12  GLU n 
1 13  LEU n 
1 14  VAL n 
1 15  LYS n 
1 16  PRO n 
1 17  GLY n 
1 18  ALA n 
1 19  SER n 
1 20  VAL n 
1 21  ARG n 
1 22  LEU n 
1 23  SER n 
1 24  CYS n 
1 25  LYS n 
1 26  THR n 
1 27  SER n 
1 28  GLY n 
1 29  TYR n 
1 30  THR n 
1 31  PHE n 
1 32  ALA n 
1 33  SER n 
1 34  TYR n 
1 35  THR n 
1 36  LEU n 
1 37  HIS n 
1 38  TRP n 
1 39  VAL n 
1 40  LYS n 
1 41  GLN n 
1 42  THR n 
1 43  PRO n 
1 44  GLY n 
1 45  GLN n 
1 46  GLY n 
1 47  LEU n 
1 48  ASP n 
1 49  TRP n 
1 50  ILE n 
1 51  GLY n 
1 52  ALA n 
1 53  ILE n 
1 54  TYR n 
1 55  PRO n 
1 56  GLY n 
1 57  ASN n 
1 58  GLY n 
1 59  ASP n 
1 60  THR n 
1 61  SER n 
1 62  TYR n 
1 63  ASN n 
1 64  GLN n 
1 65  LYS n 
1 66  PHE n 
1 67  LYS n 
1 68  ASP n 
1 69  LYS n 
1 70  ALA n 
1 71  THR n 
1 72  LEU n 
1 73  THR n 
1 74  ALA n 
1 75  ASP n 
1 76  LYS n 
1 77  SER n 
1 78  SER n 
1 79  SER n 
1 80  THR n 
1 81  ALA n 
1 82  TYR n 
1 83  MET n 
1 84  GLN n 
1 85  LEU n 
1 86  SER n 
1 87  ASN n 
1 88  LEU n 
1 89  THR n 
1 90  SER n 
1 91  GLU n 
1 92  ASP n 
1 93  SER n 
1 94  ALA n 
1 95  VAL n 
1 96  TYR n 
1 97  TYR n 
1 98  CYS n 
1 99  ALA n 
1 100 ARG n 
1 101 LEU n 
1 102 ASP n 
1 103 TRP n 
1 104 TYR n 
1 105 PHE n 
1 106 ASP n 
1 107 LEU n 
1 108 TRP n 
1 109 GLY n 
1 110 ALA n 
1 111 GLY n 
1 112 THR n 
1 113 THR n 
1 114 VAL n 
1 115 THR n 
1 116 VAL n 
1 117 SER n 
1 118 ALA n 
1 119 ALA n 
1 120 GLY n 
1 121 GLY n 
1 122 GLY n 
1 123 GLY n 
1 124 SER n 
1 125 GLY n 
1 126 GLY n 
1 127 GLY n 
1 128 GLY n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 GLY n 
1 133 GLY n 
1 134 SER n 
1 135 ASP n 
1 136 ILE n 
1 137 VAL n 
1 138 LEU n 
1 139 THR n 
1 140 GLN n 
1 141 SER n 
1 142 PRO n 
1 143 THR n 
1 144 SER n 
1 145 LEU n 
1 146 ALA n 
1 147 VAL n 
1 148 SER n 
1 149 LEU n 
1 150 GLY n 
1 151 GLN n 
1 152 ARG n 
1 153 ALA n 
1 154 THR n 
1 155 ILE n 
1 156 SER n 
1 157 CYS n 
1 158 LYS n 
1 159 ALA n 
1 160 SER n 
1 161 GLN n 
1 162 SER n 
1 163 VAL n 
1 164 ASP n 
1 165 TYR n 
1 166 ASP n 
1 167 GLY n 
1 168 ASP n 
1 169 SER n 
1 170 TYR n 
1 171 MET n 
1 172 ASN n 
1 173 TRP n 
1 174 TYR n 
1 175 GLN n 
1 176 GLN n 
1 177 LYS n 
1 178 PRO n 
1 179 GLY n 
1 180 GLN n 
1 181 PRO n 
1 182 PRO n 
1 183 ARG n 
1 184 LEU n 
1 185 LEU n 
1 186 ILE n 
1 187 TYR n 
1 188 ALA n 
1 189 ALA n 
1 190 SER n 
1 191 ASN n 
1 192 LEU n 
1 193 GLU n 
1 194 SER n 
1 195 GLY n 
1 196 ILE n 
1 197 PRO n 
1 198 ALA n 
1 199 ARG n 
1 200 PHE n 
1 201 SER n 
1 202 GLY n 
1 203 SER n 
1 204 GLY n 
1 205 SER n 
1 206 GLY n 
1 207 THR n 
1 208 ASP n 
1 209 PHE n 
1 210 THR n 
1 211 LEU n 
1 212 ASN n 
1 213 ILE n 
1 214 HIS n 
1 215 PRO n 
1 216 VAL n 
1 217 GLU n 
1 218 GLU n 
1 219 GLU n 
1 220 ASP n 
1 221 ALA n 
1 222 ALA n 
1 223 THR n 
1 224 TYR n 
1 225 TYR n 
1 226 CYS n 
1 227 GLN n 
1 228 GLN n 
1 229 ASN n 
1 230 ASN n 
1 231 GLU n 
1 232 ASP n 
1 233 PRO n 
1 234 ARG n 
1 235 THR n 
1 236 PHE n 
1 237 GLY n 
1 238 GLY n 
1 239 GLY n 
1 240 THR n 
1 241 LYS n 
1 242 LEU n 
1 243 GLU n 
1 244 ILE n 
1 245 LYS n 
1 246 LEU n 
1 247 GLU n 
1 248 MET n 
1 249 GLY n 
1 250 SER n 
1 251 SER n 
1 252 HIS n 
1 253 HIS n 
1 254 HIS n 
1 255 HIS n 
1 256 HIS n 
1 257 HIS n 
1 258 SER n 
1 259 SER n 
1 260 GLY n 
1 261 GLU n 
1 262 ASN n 
1 263 LEU n 
1 264 TYR n 
1 265 PHE n 
1 266 GLN n 
1 267 GLY n 
1 268 HIS n 
1 269 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                   269 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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              pLysS 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_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 
IMD non-polymer         . IMIDAZOLE       ?                 'C3 H5 N2 1'     69.085  
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ?                 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  CYS 24  24  24  CYS CYS A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  HIS 37  37  37  HIS HIS A . n 
A 1 38  TRP 38  38  38  TRP TRP A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  TRP 49  49  49  TRP TRP A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  GLN 64  64  64  GLN GLN A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  MET 83  83  83  MET MET A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  CYS 98  98  98  CYS CYS A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 GLY 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 GLY 123 123 ?   ?   ?   A . n 
A 1 124 SER 124 124 ?   ?   ?   A . n 
A 1 125 GLY 125 125 ?   ?   ?   A . n 
A 1 126 GLY 126 126 ?   ?   ?   A . n 
A 1 127 GLY 127 127 ?   ?   ?   A . n 
A 1 128 GLY 128 128 ?   ?   ?   A . n 
A 1 129 SER 129 129 ?   ?   ?   A . n 
A 1 130 GLY 130 130 ?   ?   ?   A . n 
A 1 131 GLY 131 131 ?   ?   ?   A . n 
A 1 132 GLY 132 132 ?   ?   ?   A . n 
A 1 133 GLY 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 CYS 157 157 157 CYS CYS A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 MET 171 171 171 MET MET A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 TRP 173 173 173 TRP TRP A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ASN 191 191 191 ASN ASN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 GLU 231 231 231 GLU GLU A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 GLU 247 247 ?   ?   ?   A . n 
A 1 248 MET 248 248 ?   ?   ?   A . n 
A 1 249 GLY 249 249 ?   ?   ?   A . n 
A 1 250 SER 250 250 ?   ?   ?   A . n 
A 1 251 SER 251 251 ?   ?   ?   A . n 
A 1 252 HIS 252 252 ?   ?   ?   A . n 
A 1 253 HIS 253 253 ?   ?   ?   A . n 
A 1 254 HIS 254 254 ?   ?   ?   A . n 
A 1 255 HIS 255 255 ?   ?   ?   A . n 
A 1 256 HIS 256 256 ?   ?   ?   A . n 
A 1 257 HIS 257 257 ?   ?   ?   A . n 
A 1 258 SER 258 258 ?   ?   ?   A . n 
A 1 259 SER 259 259 ?   ?   ?   A . n 
A 1 260 GLY 260 260 ?   ?   ?   A . n 
A 1 261 GLU 261 261 ?   ?   ?   A . n 
A 1 262 ASN 262 262 ?   ?   ?   A . n 
A 1 263 LEU 263 263 ?   ?   ?   A . n 
A 1 264 TYR 264 264 ?   ?   ?   A . n 
A 1 265 PHE 265 265 ?   ?   ?   A . n 
A 1 266 GLN 266 266 ?   ?   ?   A . n 
A 1 267 GLY 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 MET 269 269 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 EDO 1   301 301 EDO EDO A . 
C 2 EDO 1   302 302 EDO EDO A . 
D 3 IMD 1   303 303 IMD IMD A . 
E 4 NA  1   304 1   NA  NA  A . 
F 4 NA  1   305 2   NA  NA  A . 
G 5 CL  1   306 1   CL  CL  A . 
H 5 CL  1   307 2   CL  CL  A . 
I 6 HOH 1   401 206 HOH HOH A . 
I 6 HOH 2   402 29  HOH HOH A . 
I 6 HOH 3   403 46  HOH HOH A . 
I 6 HOH 4   404 220 HOH HOH A . 
I 6 HOH 5   405 279 HOH HOH A . 
I 6 HOH 6   406 106 HOH HOH A . 
I 6 HOH 7   407 188 HOH HOH A . 
I 6 HOH 8   408 276 HOH HOH A . 
I 6 HOH 9   409 177 HOH HOH A . 
I 6 HOH 10  410 66  HOH HOH A . 
I 6 HOH 11  411 152 HOH HOH A . 
I 6 HOH 12  412 150 HOH HOH A . 
I 6 HOH 13  413 42  HOH HOH A . 
I 6 HOH 14  414 165 HOH HOH A . 
I 6 HOH 15  415 283 HOH HOH A . 
I 6 HOH 16  416 80  HOH HOH A . 
I 6 HOH 17  417 93  HOH HOH A . 
I 6 HOH 18  418 317 HOH HOH A . 
I 6 HOH 19  419 272 HOH HOH A . 
I 6 HOH 20  420 23  HOH HOH A . 
I 6 HOH 21  421 78  HOH HOH A . 
I 6 HOH 22  422 107 HOH HOH A . 
I 6 HOH 23  423 73  HOH HOH A . 
I 6 HOH 24  424 186 HOH HOH A . 
I 6 HOH 25  425 7   HOH HOH A . 
I 6 HOH 26  426 142 HOH HOH A . 
I 6 HOH 27  427 92  HOH HOH A . 
I 6 HOH 28  428 144 HOH HOH A . 
I 6 HOH 29  429 240 HOH HOH A . 
I 6 HOH 30  430 115 HOH HOH A . 
I 6 HOH 31  431 232 HOH HOH A . 
I 6 HOH 32  432 217 HOH HOH A . 
I 6 HOH 33  433 47  HOH HOH A . 
I 6 HOH 34  434 122 HOH HOH A . 
I 6 HOH 35  435 163 HOH HOH A . 
I 6 HOH 36  436 81  HOH HOH A . 
I 6 HOH 37  437 57  HOH HOH A . 
I 6 HOH 38  438 322 HOH HOH A . 
I 6 HOH 39  439 53  HOH HOH A . 
I 6 HOH 40  440 174 HOH HOH A . 
I 6 HOH 41  441 224 HOH HOH A . 
I 6 HOH 42  442 138 HOH HOH A . 
I 6 HOH 43  443 194 HOH HOH A . 
I 6 HOH 44  444 65  HOH HOH A . 
I 6 HOH 45  445 235 HOH HOH A . 
I 6 HOH 46  446 303 HOH HOH A . 
I 6 HOH 47  447 86  HOH HOH A . 
I 6 HOH 48  448 63  HOH HOH A . 
I 6 HOH 49  449 208 HOH HOH A . 
I 6 HOH 50  450 94  HOH HOH A . 
I 6 HOH 51  451 179 HOH HOH A . 
I 6 HOH 52  452 154 HOH HOH A . 
I 6 HOH 53  453 82  HOH HOH A . 
I 6 HOH 54  454 91  HOH HOH A . 
I 6 HOH 55  455 36  HOH HOH A . 
I 6 HOH 56  456 62  HOH HOH A . 
I 6 HOH 57  457 85  HOH HOH A . 
I 6 HOH 58  458 19  HOH HOH A . 
I 6 HOH 59  459 204 HOH HOH A . 
I 6 HOH 60  460 148 HOH HOH A . 
I 6 HOH 61  461 112 HOH HOH A . 
I 6 HOH 62  462 20  HOH HOH A . 
I 6 HOH 63  463 99  HOH HOH A . 
I 6 HOH 64  464 242 HOH HOH A . 
I 6 HOH 65  465 185 HOH HOH A . 
I 6 HOH 66  466 325 HOH HOH A . 
I 6 HOH 67  467 247 HOH HOH A . 
I 6 HOH 68  468 271 HOH HOH A . 
I 6 HOH 69  469 48  HOH HOH A . 
I 6 HOH 70  470 128 HOH HOH A . 
I 6 HOH 71  471 187 HOH HOH A . 
I 6 HOH 72  472 69  HOH HOH A . 
I 6 HOH 73  473 58  HOH HOH A . 
I 6 HOH 74  474 184 HOH HOH A . 
I 6 HOH 75  475 159 HOH HOH A . 
I 6 HOH 76  476 110 HOH HOH A . 
I 6 HOH 77  477 147 HOH HOH A . 
I 6 HOH 78  478 31  HOH HOH A . 
I 6 HOH 79  479 275 HOH HOH A . 
I 6 HOH 80  480 111 HOH HOH A . 
I 6 HOH 81  481 299 HOH HOH A . 
I 6 HOH 82  482 274 HOH HOH A . 
I 6 HOH 83  483 203 HOH HOH A . 
I 6 HOH 84  484 212 HOH HOH A . 
I 6 HOH 85  485 25  HOH HOH A . 
I 6 HOH 86  486 70  HOH HOH A . 
I 6 HOH 87  487 88  HOH HOH A . 
I 6 HOH 88  488 51  HOH HOH A . 
I 6 HOH 89  489 132 HOH HOH A . 
I 6 HOH 90  490 129 HOH HOH A . 
I 6 HOH 91  491 77  HOH HOH A . 
I 6 HOH 92  492 76  HOH HOH A . 
I 6 HOH 93  493 328 HOH HOH A . 
I 6 HOH 94  494 281 HOH HOH A . 
I 6 HOH 95  495 260 HOH HOH A . 
I 6 HOH 96  496 134 HOH HOH A . 
I 6 HOH 97  497 3   HOH HOH A . 
I 6 HOH 98  498 135 HOH HOH A . 
I 6 HOH 99  499 301 HOH HOH A . 
I 6 HOH 100 500 166 HOH HOH A . 
I 6 HOH 101 501 277 HOH HOH A . 
I 6 HOH 102 502 197 HOH HOH A . 
I 6 HOH 103 503 39  HOH HOH A . 
I 6 HOH 104 504 149 HOH HOH A . 
I 6 HOH 105 505 75  HOH HOH A . 
I 6 HOH 106 506 182 HOH HOH A . 
I 6 HOH 107 507 136 HOH HOH A . 
I 6 HOH 108 508 10  HOH HOH A . 
I 6 HOH 109 509 170 HOH HOH A . 
I 6 HOH 110 510 108 HOH HOH A . 
I 6 HOH 111 511 306 HOH HOH A . 
I 6 HOH 112 512 305 HOH HOH A . 
I 6 HOH 113 513 84  HOH HOH A . 
I 6 HOH 114 514 56  HOH HOH A . 
I 6 HOH 115 515 172 HOH HOH A . 
I 6 HOH 116 516 323 HOH HOH A . 
I 6 HOH 117 517 292 HOH HOH A . 
I 6 HOH 118 518 250 HOH HOH A . 
I 6 HOH 119 519 98  HOH HOH A . 
I 6 HOH 120 520 118 HOH HOH A . 
I 6 HOH 121 521 145 HOH HOH A . 
I 6 HOH 122 522 64  HOH HOH A . 
I 6 HOH 123 523 102 HOH HOH A . 
I 6 HOH 124 524 60  HOH HOH A . 
I 6 HOH 125 525 246 HOH HOH A . 
I 6 HOH 126 526 270 HOH HOH A . 
I 6 HOH 127 527 141 HOH HOH A . 
I 6 HOH 128 528 286 HOH HOH A . 
I 6 HOH 129 529 100 HOH HOH A . 
I 6 HOH 130 530 68  HOH HOH A . 
I 6 HOH 131 531 59  HOH HOH A . 
I 6 HOH 132 532 273 HOH HOH A . 
I 6 HOH 133 533 329 HOH HOH A . 
I 6 HOH 134 534 133 HOH HOH A . 
I 6 HOH 135 535 61  HOH HOH A . 
I 6 HOH 136 536 158 HOH HOH A . 
I 6 HOH 137 537 116 HOH HOH A . 
I 6 HOH 138 538 45  HOH HOH A . 
I 6 HOH 139 539 284 HOH HOH A . 
I 6 HOH 140 540 131 HOH HOH A . 
I 6 HOH 141 541 268 HOH HOH A . 
I 6 HOH 142 542 164 HOH HOH A . 
I 6 HOH 143 543 324 HOH HOH A . 
I 6 HOH 144 544 13  HOH HOH A . 
I 6 HOH 145 545 50  HOH HOH A . 
I 6 HOH 146 546 183 HOH HOH A . 
I 6 HOH 147 547 54  HOH HOH A . 
I 6 HOH 148 548 40  HOH HOH A . 
I 6 HOH 149 549 38  HOH HOH A . 
I 6 HOH 150 550 30  HOH HOH A . 
I 6 HOH 151 551 83  HOH HOH A . 
I 6 HOH 152 552 318 HOH HOH A . 
I 6 HOH 153 553 297 HOH HOH A . 
I 6 HOH 154 554 210 HOH HOH A . 
I 6 HOH 155 555 269 HOH HOH A . 
I 6 HOH 156 556 239 HOH HOH A . 
I 6 HOH 157 557 95  HOH HOH A . 
I 6 HOH 158 558 307 HOH HOH A . 
I 6 HOH 159 559 109 HOH HOH A . 
I 6 HOH 160 560 226 HOH HOH A . 
I 6 HOH 161 561 72  HOH HOH A . 
I 6 HOH 162 562 71  HOH HOH A . 
I 6 HOH 163 563 293 HOH HOH A . 
I 6 HOH 164 564 11  HOH HOH A . 
I 6 HOH 165 565 32  HOH HOH A . 
I 6 HOH 166 566 282 HOH HOH A . 
I 6 HOH 167 567 267 HOH HOH A . 
I 6 HOH 168 568 22  HOH HOH A . 
I 6 HOH 169 569 278 HOH HOH A . 
I 6 HOH 170 570 214 HOH HOH A . 
I 6 HOH 171 571 14  HOH HOH A . 
I 6 HOH 172 572 127 HOH HOH A . 
I 6 HOH 173 573 310 HOH HOH A . 
I 6 HOH 174 574 155 HOH HOH A . 
I 6 HOH 175 575 198 HOH HOH A . 
I 6 HOH 176 576 252 HOH HOH A . 
I 6 HOH 177 577 28  HOH HOH A . 
I 6 HOH 178 578 52  HOH HOH A . 
I 6 HOH 179 579 251 HOH HOH A . 
I 6 HOH 180 580 296 HOH HOH A . 
I 6 HOH 181 581 119 HOH HOH A . 
I 6 HOH 182 582 17  HOH HOH A . 
I 6 HOH 183 583 21  HOH HOH A . 
I 6 HOH 184 584 8   HOH HOH A . 
I 6 HOH 185 585 96  HOH HOH A . 
I 6 HOH 186 586 49  HOH HOH A . 
I 6 HOH 187 587 294 HOH HOH A . 
I 6 HOH 188 588 280 HOH HOH A . 
I 6 HOH 189 589 309 HOH HOH A . 
I 6 HOH 190 590 321 HOH HOH A . 
I 6 HOH 191 591 9   HOH HOH A . 
I 6 HOH 192 592 5   HOH HOH A . 
I 6 HOH 193 593 196 HOH HOH A . 
I 6 HOH 194 594 265 HOH HOH A . 
I 6 HOH 195 595 157 HOH HOH A . 
I 6 HOH 196 596 12  HOH HOH A . 
I 6 HOH 197 597 288 HOH HOH A . 
I 6 HOH 198 598 264 HOH HOH A . 
I 6 HOH 199 599 243 HOH HOH A . 
I 6 HOH 200 600 311 HOH HOH A . 
I 6 HOH 201 601 161 HOH HOH A . 
I 6 HOH 202 602 259 HOH HOH A . 
I 6 HOH 203 603 6   HOH HOH A . 
I 6 HOH 204 604 313 HOH HOH A . 
I 6 HOH 205 605 120 HOH HOH A . 
I 6 HOH 206 606 101 HOH HOH A . 
I 6 HOH 207 607 253 HOH HOH A . 
I 6 HOH 208 608 180 HOH HOH A . 
I 6 HOH 209 609 137 HOH HOH A . 
I 6 HOH 210 610 330 HOH HOH A . 
I 6 HOH 211 611 291 HOH HOH A . 
I 6 HOH 212 612 26  HOH HOH A . 
I 6 HOH 213 613 241 HOH HOH A . 
I 6 HOH 214 614 113 HOH HOH A . 
I 6 HOH 215 615 190 HOH HOH A . 
I 6 HOH 216 616 79  HOH HOH A . 
I 6 HOH 217 617 312 HOH HOH A . 
I 6 HOH 218 618 2   HOH HOH A . 
I 6 HOH 219 619 121 HOH HOH A . 
I 6 HOH 220 620 43  HOH HOH A . 
I 6 HOH 221 621 227 HOH HOH A . 
I 6 HOH 222 622 151 HOH HOH A . 
I 6 HOH 223 623 289 HOH HOH A . 
I 6 HOH 224 624 16  HOH HOH A . 
I 6 HOH 225 625 302 HOH HOH A . 
I 6 HOH 226 626 27  HOH HOH A . 
I 6 HOH 227 627 143 HOH HOH A . 
I 6 HOH 228 628 24  HOH HOH A . 
I 6 HOH 229 629 37  HOH HOH A . 
I 6 HOH 230 630 263 HOH HOH A . 
I 6 HOH 231 631 315 HOH HOH A . 
I 6 HOH 232 632 55  HOH HOH A . 
I 6 HOH 233 633 97  HOH HOH A . 
I 6 HOH 234 634 123 HOH HOH A . 
I 6 HOH 235 635 67  HOH HOH A . 
I 6 HOH 236 636 320 HOH HOH A . 
I 6 HOH 237 637 125 HOH HOH A . 
I 6 HOH 238 638 15  HOH HOH A . 
I 6 HOH 239 639 287 HOH HOH A . 
I 6 HOH 240 640 331 HOH HOH A . 
I 6 HOH 241 641 223 HOH HOH A . 
I 6 HOH 242 642 202 HOH HOH A . 
I 6 HOH 243 643 304 HOH HOH A . 
I 6 HOH 244 644 326 HOH HOH A . 
I 6 HOH 245 645 35  HOH HOH A . 
I 6 HOH 246 646 44  HOH HOH A . 
I 6 HOH 247 647 298 HOH HOH A . 
I 6 HOH 248 648 316 HOH HOH A . 
I 6 HOH 249 649 230 HOH HOH A . 
I 6 HOH 250 650 140 HOH HOH A . 
I 6 HOH 251 651 41  HOH HOH A . 
I 6 HOH 252 652 285 HOH HOH A . 
I 6 HOH 253 653 211 HOH HOH A . 
I 6 HOH 254 654 290 HOH HOH A . 
I 6 HOH 255 655 319 HOH HOH A . 
I 6 HOH 256 656 87  HOH HOH A . 
I 6 HOH 257 657 168 HOH HOH A . 
I 6 HOH 258 658 201 HOH HOH A . 
I 6 HOH 259 659 146 HOH HOH A . 
I 6 HOH 260 660 215 HOH HOH A . 
I 6 HOH 261 661 200 HOH HOH A . 
I 6 HOH 262 662 169 HOH HOH A . 
I 6 HOH 263 663 256 HOH HOH A . 
I 6 HOH 264 664 104 HOH HOH A . 
I 6 HOH 265 665 207 HOH HOH A . 
I 6 HOH 266 666 308 HOH HOH A . 
I 6 HOH 267 667 193 HOH HOH A . 
I 6 HOH 268 668 266 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 25 ? CD  ? A LYS 25 CD  
2 1 Y 1 A LYS 25 ? CE  ? A LYS 25 CE  
3 1 Y 1 A LYS 25 ? NZ  ? A LYS 25 NZ  
4 1 Y 1 A GLN 64 ? CD  ? A GLN 64 CD  
5 1 Y 1 A GLN 64 ? OE1 ? A GLN 64 OE1 
6 1 Y 1 A GLN 64 ? NE2 ? A GLN 64 NE2 
7 1 Y 1 A LYS 67 ? CD  ? A LYS 67 CD  
8 1 Y 1 A LYS 67 ? CE  ? A LYS 67 CE  
9 1 Y 1 A LYS 67 ? NZ  ? A LYS 67 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HY2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.420 
_cell.length_a_esd                 ? 
_cell.length_b                     64.420 
_cell.length_b_esd                 ? 
_cell.length_c                     161.124 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9HY2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 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                   9HY2 
_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             3.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.46 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'room temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '4.1 M NaCl, 0.1 M HEPES pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-20 
_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                    'Si(111)' 
_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   0.97630 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97630 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          34.8 
_reflns.entry_id                                       9HY2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               40.28 
_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                                     43566 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                19.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.11 
_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                                0.076 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.074 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2272 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               20.8 
_reflns_shell.pdbx_chi_squared                              1.04 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.917 
_reflns_shell.pdbx_Rpim_I_all                               0.418 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.437 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.870 
_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]                            -0.00 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.01 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               39.945 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.969 
_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                                 9HY2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             32.21 
_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                     41143 
_refine.ls_number_reflns_R_free                  2283 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.71 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17837 
_refine.ls_R_factor_R_free                       0.21148 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17656 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.077 
_refine.pdbx_overall_ESU_R_Free                  0.082 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.677 
_refine.overall_SU_ML                            0.074 
_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_analyze.entry_id                        9HY2 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        32.21 
_refine_hist.number_atoms_solvent             268 
_refine_hist.number_atoms_total               2045 
_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        1760 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         17 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  1859 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.131  1.803  2517 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.292  5.000  238  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.490  5.000  7    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.980 10.000 283  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.159  0.200  273  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1455 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.904  2.681  932  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.713  4.778  1164 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.960  2.947  927  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.095  31.12  2809 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             184 
_refine_ls_shell.number_reflns_R_work             2980 
_refine_ls_shell.percent_reflns_obs               99.91 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.401 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.378 
# 
_struct.entry_id                     9HY2 
_struct.title                        
'sc-4E (scFv derived from the mAb 4E1 against CD93) crystallized at pH 7.5 (monomeric state from gel filtration)' 
_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        9HY2 
_struct_keywords.text            'single-chain antibody fragment, scFv, monoclonal antibody 4E1 against CD93, sc-4E, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9HY2 
_struct_ref.pdbx_db_accession          9HY2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HY2 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 269 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9HY2 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  269 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       269 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1040  ? 
1 MORE         -26   ? 
1 'SSA (A^2)'  11020 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'monomeric state sample in solution (obtained from gel filtration)' 
# 
_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 30  ? TYR A 34  ? THR A 30  TYR A 34  5 ? 5 
HELX_P HELX_P2 AA2 GLN A 64  ? LYS A 67  ? GLN A 64  LYS A 67  5 ? 4 
HELX_P HELX_P3 AA3 LYS A 76  ? SER A 78  ? LYS A 76  SER A 78  5 ? 3 
HELX_P HELX_P4 AA4 THR A 89  ? SER A 93  ? THR A 89  SER A 93  5 ? 5 
HELX_P HELX_P5 AA5 ASP A 102 ? ASP A 106 ? ASP A 102 ASP A 106 5 ? 5 
HELX_P HELX_P6 AA6 GLU A 217 ? ALA A 221 ? GLU A 217 ALA A 221 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 24  SG ? ? ? 1_555 A CYS 98  SG ? ? A CYS 24  A CYS 98  1_555 ? ? ? ? ? ? ? 2.249 ? ? 
disulf2  disulf ? ? A CYS 157 SG ? ? ? 1_555 A CYS 226 SG ? ? A CYS 157 A CYS 226 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc1  metalc ? ? A SER 79  OG ? ? ? 1_555 E NA  .   NA ? ? A SER 79  A NA  304 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
metalc2  metalc ? ? A TYR 104 O  ? ? ? 1_555 F NA  .   NA ? ? A TYR 104 A NA  305 4_565 ? ? ? ? ? ? ? 2.583 ? ? 
metalc3  metalc ? ? A SER 141 OG ? ? ? 1_555 F NA  .   NA ? ? A SER 141 A NA  305 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc4  metalc ? ? E NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  304 A HOH 453 1_555 ? ? ? ? ? ? ? 2.472 ? ? 
metalc5  metalc ? ? E NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  304 A HOH 558 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc6  metalc ? ? E NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  304 A HOH 560 1_555 ? ? ? ? ? ? ? 2.440 ? ? 
metalc7  metalc ? ? E NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  304 A HOH 576 1_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc8  metalc ? ? E NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  304 A HOH 588 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc9  metalc ? ? F NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  305 A HOH 474 1_555 ? ? ? ? ? ? ? 2.415 ? ? 
metalc10 metalc ? ? F NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  305 A HOH 566 4_455 ? ? ? ? ? ? ? 2.432 ? ? 
metalc11 metalc ? ? F NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  305 A HOH 600 1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc12 metalc ? ? F NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  305 A HOH 605 1_555 ? ? ? ? ? ? ? 2.467 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 453 ? 1_555 104.5 ? 
2  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 558 ? 1_555 174.2 ? 
3  O  ? I HOH .   ? A HOH 453 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 558 ? 1_555 81.3  ? 
4  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 560 ? 1_555 84.2  ? 
5  O  ? I HOH .   ? A HOH 453 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 560 ? 1_555 87.6  ? 
6  O  ? I HOH .   ? A HOH 558 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 560 ? 1_555 96.2  ? 
7  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 576 ? 1_555 80.4  ? 
8  O  ? I HOH .   ? A HOH 453 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 576 ? 1_555 173.0 ? 
9  O  ? I HOH .   ? A HOH 558 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 576 ? 1_555 93.8  ? 
10 O  ? I HOH .   ? A HOH 560 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 576 ? 1_555 87.9  ? 
11 OG ? A SER 79  ? A SER 79  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 588 ? 1_555 98.1  ? 
12 O  ? I HOH .   ? A HOH 453 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 588 ? 1_555 93.2  ? 
13 O  ? I HOH .   ? A HOH 558 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 588 ? 1_555 81.3  ? 
14 O  ? I HOH .   ? A HOH 560 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 588 ? 1_555 177.2 ? 
15 O  ? I HOH .   ? A HOH 576 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O  ? I HOH .   ? A HOH 588 ? 1_555 91.0  ? 
16 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 OG ? A SER 141 ? A SER 141 ? 1_555 49.9  ? 
17 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 474 ? 1_555 52.5  ? 
18 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 474 ? 1_555 6.3   ? 
19 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 566 ? 4_455 50.8  ? 
20 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 566 ? 4_455 4.9   ? 
21 O  ? I HOH .   ? A HOH 474 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 566 ? 4_455 1.9   ? 
22 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 600 ? 1_555 46.5  ? 
23 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 600 ? 1_555 5.3   ? 
24 O  ? I HOH .   ? A HOH 474 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 600 ? 1_555 6.1   ? 
25 O  ? I HOH .   ? A HOH 566 ? 4_455 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 600 ? 1_555 4.3   ? 
26 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 605 ? 1_555 48.9  ? 
27 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 605 ? 1_555 1.0   ? 
28 O  ? I HOH .   ? A HOH 474 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 605 ? 1_555 6.5   ? 
29 O  ? I HOH .   ? A HOH 566 ? 4_455 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 605 ? 1_555 4.9   ? 
30 O  ? I HOH .   ? A HOH 600 ? 1_555 NA ? F NA . ? A NA 305 ? 4_565 O  ? I HOH .   ? A HOH 605 ? 1_555 4.5   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 24  ? CYS A 98  ? CYS A 24  ? 1_555 CYS A 98  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 157 ? CYS A 226 ? CYS A 157 ? 1_555 CYS A 226 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 141 A . ? SER 141 A PRO 142 A ? PRO 142 A 1 -6.44 
2 HIS 214 A . ? HIS 214 A PRO 215 A ? PRO 215 A 1 -5.59 
3 ASP 232 A . ? ASP 232 A PRO 233 A ? PRO 233 A 1 -5.99 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 5   ? GLN A 7   ? GLN A 5   GLN A 7   
AA1 2 VAL A 20  ? SER A 27  ? VAL A 20  SER A 27  
AA1 3 THR A 80  ? LEU A 85  ? THR A 80  LEU A 85  
AA1 4 ALA A 70  ? ASP A 75  ? ALA A 70  ASP A 75  
AA2 1 THR A 11  ? VAL A 14  ? THR A 11  VAL A 14  
AA2 2 THR A 112 ? VAL A 116 ? THR A 112 VAL A 116 
AA2 3 ALA A 94  ? ARG A 100 ? ALA A 94  ARG A 100 
AA2 4 LEU A 36  ? THR A 42  ? LEU A 36  THR A 42  
AA2 5 GLY A 46  ? ILE A 53  ? GLY A 46  ILE A 53  
AA2 6 THR A 60  ? TYR A 62  ? THR A 60  TYR A 62  
AA3 1 THR A 11  ? VAL A 14  ? THR A 11  VAL A 14  
AA3 2 THR A 112 ? VAL A 116 ? THR A 112 VAL A 116 
AA3 3 ALA A 94  ? ARG A 100 ? ALA A 94  ARG A 100 
AA3 4 LEU A 107 ? TRP A 108 ? LEU A 107 TRP A 108 
AA4 1 LEU A 138 ? SER A 141 ? LEU A 138 SER A 141 
AA4 2 ALA A 153 ? ALA A 159 ? ALA A 153 ALA A 159 
AA4 3 ASP A 208 ? ILE A 213 ? ASP A 208 ILE A 213 
AA4 4 PHE A 200 ? SER A 205 ? PHE A 200 SER A 205 
AA5 1 SER A 144 ? SER A 148 ? SER A 144 SER A 148 
AA5 2 THR A 240 ? LYS A 245 ? THR A 240 LYS A 245 
AA5 3 ALA A 222 ? GLN A 228 ? ALA A 222 GLN A 228 
AA5 4 MET A 171 ? GLN A 176 ? MET A 171 GLN A 176 
AA5 5 ARG A 183 ? TYR A 187 ? ARG A 183 TYR A 187 
AA5 6 ASN A 191 ? LEU A 192 ? ASN A 191 LEU A 192 
AA6 1 SER A 144 ? SER A 148 ? SER A 144 SER A 148 
AA6 2 THR A 240 ? LYS A 245 ? THR A 240 LYS A 245 
AA6 3 ALA A 222 ? GLN A 228 ? ALA A 222 GLN A 228 
AA6 4 THR A 235 ? PHE A 236 ? THR A 235 PHE A 236 
AA7 1 ASP A 164 ? TYR A 165 ? ASP A 164 TYR A 165 
AA7 2 ASP A 168 ? SER A 169 ? ASP A 168 SER A 169 
# 
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 GLN A 7   ? N GLN A 7   O LYS A 25  ? O LYS A 25  
AA1 2 3 N LEU A 22  ? N LEU A 22  O MET A 83  ? O MET A 83  
AA1 3 4 O THR A 80  ? O THR A 80  N ASP A 75  ? N ASP A 75  
AA2 1 2 N GLU A 12  ? N GLU A 12  O THR A 115 ? O THR A 115 
AA2 2 3 O VAL A 114 ? O VAL A 114 N ALA A 94  ? N ALA A 94  
AA2 3 4 O ALA A 99  ? O ALA A 99  N HIS A 37  ? N HIS A 37  
AA2 4 5 N TRP A 38  ? N TRP A 38  O ILE A 50  ? O ILE A 50  
AA2 5 6 N ALA A 52  ? N ALA A 52  O SER A 61  ? O SER A 61  
AA3 1 2 N GLU A 12  ? N GLU A 12  O THR A 115 ? O THR A 115 
AA3 2 3 O VAL A 114 ? O VAL A 114 N ALA A 94  ? N ALA A 94  
AA3 3 4 N ARG A 100 ? N ARG A 100 O LEU A 107 ? O LEU A 107 
AA4 1 2 N SER A 141 ? N SER A 141 O SER A 156 ? O SER A 156 
AA4 2 3 N ILE A 155 ? N ILE A 155 O LEU A 211 ? O LEU A 211 
AA4 3 4 O ASN A 212 ? O ASN A 212 N SER A 201 ? N SER A 201 
AA5 1 2 N LEU A 145 ? N LEU A 145 O GLU A 243 ? O GLU A 243 
AA5 2 3 O LEU A 242 ? O LEU A 242 N ALA A 222 ? N ALA A 222 
AA5 3 4 O THR A 223 ? O THR A 223 N GLN A 176 ? N GLN A 176 
AA5 4 5 N TRP A 173 ? N TRP A 173 O LEU A 185 ? O LEU A 185 
AA5 5 6 N TYR A 187 ? N TYR A 187 O ASN A 191 ? O ASN A 191 
AA6 1 2 N LEU A 145 ? N LEU A 145 O GLU A 243 ? O GLU A 243 
AA6 2 3 O LEU A 242 ? O LEU A 242 N ALA A 222 ? N ALA A 222 
AA6 3 4 N GLN A 228 ? N GLN A 228 O THR A 235 ? O THR A 235 
AA7 1 2 N TYR A 165 ? N TYR A 165 O ASP A 168 ? O ASP A 168 
# 
_pdbx_entry_details.entry_id                   9HY2 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     189 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             75.93 
_pdbx_validate_torsion.psi             -44.53 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 477 ? I HOH . 
2 1 A HOH 658 ? I HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -31.8660 
_pdbx_refine_tls.origin_y         6.3482 
_pdbx_refine_tls.origin_z         9.7771 
_pdbx_refine_tls.T[1][1]          0.1774 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0550 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0404 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0727 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0378 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0691 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.2030 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0237 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0035 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.4011 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0521 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.6385 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0373 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0251 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0389 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0123 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.1419 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0829 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0780 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0489 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.1046 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     3 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     303 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
_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                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       668 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.06 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ASP 2   ? A ASP 2   
3  1 Y 1 A GLY 121 ? A GLY 121 
4  1 Y 1 A GLY 122 ? A GLY 122 
5  1 Y 1 A GLY 123 ? A GLY 123 
6  1 Y 1 A SER 124 ? A SER 124 
7  1 Y 1 A GLY 125 ? A GLY 125 
8  1 Y 1 A GLY 126 ? A GLY 126 
9  1 Y 1 A GLY 127 ? A GLY 127 
10 1 Y 1 A GLY 128 ? A GLY 128 
11 1 Y 1 A SER 129 ? A SER 129 
12 1 Y 1 A GLY 130 ? A GLY 130 
13 1 Y 1 A GLY 131 ? A GLY 131 
14 1 Y 1 A GLY 132 ? A GLY 132 
15 1 Y 1 A GLY 133 ? A GLY 133 
16 1 Y 1 A GLU 247 ? A GLU 247 
17 1 Y 1 A MET 248 ? A MET 248 
18 1 Y 1 A GLY 249 ? A GLY 249 
19 1 Y 1 A SER 250 ? A SER 250 
20 1 Y 1 A SER 251 ? A SER 251 
21 1 Y 1 A HIS 252 ? A HIS 252 
22 1 Y 1 A HIS 253 ? A HIS 253 
23 1 Y 1 A HIS 254 ? A HIS 254 
24 1 Y 1 A HIS 255 ? A HIS 255 
25 1 Y 1 A HIS 256 ? A HIS 256 
26 1 Y 1 A HIS 257 ? A HIS 257 
27 1 Y 1 A SER 258 ? A SER 258 
28 1 Y 1 A SER 259 ? A SER 259 
29 1 Y 1 A GLY 260 ? A GLY 260 
30 1 Y 1 A GLU 261 ? A GLU 261 
31 1 Y 1 A ASN 262 ? A ASN 262 
32 1 Y 1 A LEU 263 ? A LEU 263 
33 1 Y 1 A TYR 264 ? A TYR 264 
34 1 Y 1 A PHE 265 ? A PHE 265 
35 1 Y 1 A GLN 266 ? A GLN 266 
36 1 Y 1 A GLY 267 ? A GLY 267 
37 1 Y 1 A HIS 268 ? A HIS 268 
38 1 Y 1 A MET 269 ? A MET 269 
# 
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 
IMD N1   N  Y N 194 
IMD C2   C  Y N 195 
IMD N3   N  Y N 196 
IMD C4   C  Y N 197 
IMD C5   C  Y N 198 
IMD HN1  H  N N 199 
IMD H2   H  N N 200 
IMD HN3  H  N N 201 
IMD H4   H  N N 202 
IMD H5   H  N N 203 
LEU N    N  N N 204 
LEU CA   C  N S 205 
LEU C    C  N N 206 
LEU O    O  N N 207 
LEU CB   C  N N 208 
LEU CG   C  N N 209 
LEU CD1  C  N N 210 
LEU CD2  C  N N 211 
LEU OXT  O  N N 212 
LEU H    H  N N 213 
LEU H2   H  N N 214 
LEU HA   H  N N 215 
LEU HB2  H  N N 216 
LEU HB3  H  N N 217 
LEU HG   H  N N 218 
LEU HD11 H  N N 219 
LEU HD12 H  N N 220 
LEU HD13 H  N N 221 
LEU HD21 H  N N 222 
LEU HD22 H  N N 223 
LEU HD23 H  N N 224 
LEU HXT  H  N N 225 
LYS N    N  N N 226 
LYS CA   C  N S 227 
LYS C    C  N N 228 
LYS O    O  N N 229 
LYS CB   C  N N 230 
LYS CG   C  N N 231 
LYS CD   C  N N 232 
LYS CE   C  N N 233 
LYS NZ   N  N N 234 
LYS OXT  O  N N 235 
LYS H    H  N N 236 
LYS H2   H  N N 237 
LYS HA   H  N N 238 
LYS HB2  H  N N 239 
LYS HB3  H  N N 240 
LYS HG2  H  N N 241 
LYS HG3  H  N N 242 
LYS HD2  H  N N 243 
LYS HD3  H  N N 244 
LYS HE2  H  N N 245 
LYS HE3  H  N N 246 
LYS HZ1  H  N N 247 
LYS HZ2  H  N N 248 
LYS HZ3  H  N N 249 
LYS HXT  H  N N 250 
MET N    N  N N 251 
MET CA   C  N S 252 
MET C    C  N N 253 
MET O    O  N N 254 
MET CB   C  N N 255 
MET CG   C  N N 256 
MET SD   S  N N 257 
MET CE   C  N N 258 
MET OXT  O  N N 259 
MET H    H  N N 260 
MET H2   H  N N 261 
MET HA   H  N N 262 
MET HB2  H  N N 263 
MET HB3  H  N N 264 
MET HG2  H  N N 265 
MET HG3  H  N N 266 
MET HE1  H  N N 267 
MET HE2  H  N N 268 
MET HE3  H  N N 269 
MET HXT  H  N N 270 
NA  NA   NA N N 271 
PHE N    N  N N 272 
PHE CA   C  N S 273 
PHE C    C  N N 274 
PHE O    O  N N 275 
PHE CB   C  N N 276 
PHE CG   C  Y N 277 
PHE CD1  C  Y N 278 
PHE CD2  C  Y N 279 
PHE CE1  C  Y N 280 
PHE CE2  C  Y N 281 
PHE CZ   C  Y N 282 
PHE OXT  O  N N 283 
PHE H    H  N N 284 
PHE H2   H  N N 285 
PHE HA   H  N N 286 
PHE HB2  H  N N 287 
PHE HB3  H  N N 288 
PHE HD1  H  N N 289 
PHE HD2  H  N N 290 
PHE HE1  H  N N 291 
PHE HE2  H  N N 292 
PHE HZ   H  N N 293 
PHE HXT  H  N N 294 
PRO N    N  N N 295 
PRO CA   C  N S 296 
PRO C    C  N N 297 
PRO O    O  N N 298 
PRO CB   C  N N 299 
PRO CG   C  N N 300 
PRO CD   C  N N 301 
PRO OXT  O  N N 302 
PRO H    H  N N 303 
PRO HA   H  N N 304 
PRO HB2  H  N N 305 
PRO HB3  H  N N 306 
PRO HG2  H  N N 307 
PRO HG3  H  N N 308 
PRO HD2  H  N N 309 
PRO HD3  H  N N 310 
PRO HXT  H  N N 311 
SER N    N  N N 312 
SER CA   C  N S 313 
SER C    C  N N 314 
SER O    O  N N 315 
SER CB   C  N N 316 
SER OG   O  N N 317 
SER OXT  O  N N 318 
SER H    H  N N 319 
SER H2   H  N N 320 
SER HA   H  N N 321 
SER HB2  H  N N 322 
SER HB3  H  N N 323 
SER HG   H  N N 324 
SER HXT  H  N N 325 
THR N    N  N N 326 
THR CA   C  N S 327 
THR C    C  N N 328 
THR O    O  N N 329 
THR CB   C  N R 330 
THR OG1  O  N N 331 
THR CG2  C  N N 332 
THR OXT  O  N N 333 
THR H    H  N N 334 
THR H2   H  N N 335 
THR HA   H  N N 336 
THR HB   H  N N 337 
THR HG1  H  N N 338 
THR HG21 H  N N 339 
THR HG22 H  N N 340 
THR HG23 H  N N 341 
THR HXT  H  N N 342 
TRP N    N  N N 343 
TRP CA   C  N S 344 
TRP C    C  N N 345 
TRP O    O  N N 346 
TRP CB   C  N N 347 
TRP CG   C  Y N 348 
TRP CD1  C  Y N 349 
TRP CD2  C  Y N 350 
TRP NE1  N  Y N 351 
TRP CE2  C  Y N 352 
TRP CE3  C  Y N 353 
TRP CZ2  C  Y N 354 
TRP CZ3  C  Y N 355 
TRP CH2  C  Y N 356 
TRP OXT  O  N N 357 
TRP H    H  N N 358 
TRP H2   H  N N 359 
TRP HA   H  N N 360 
TRP HB2  H  N N 361 
TRP HB3  H  N N 362 
TRP HD1  H  N N 363 
TRP HE1  H  N N 364 
TRP HE3  H  N N 365 
TRP HZ2  H  N N 366 
TRP HZ3  H  N N 367 
TRP HH2  H  N N 368 
TRP HXT  H  N N 369 
TYR N    N  N N 370 
TYR CA   C  N S 371 
TYR C    C  N N 372 
TYR O    O  N N 373 
TYR CB   C  N N 374 
TYR CG   C  Y N 375 
TYR CD1  C  Y N 376 
TYR CD2  C  Y N 377 
TYR CE1  C  Y N 378 
TYR CE2  C  Y N 379 
TYR CZ   C  Y N 380 
TYR OH   O  N N 381 
TYR OXT  O  N N 382 
TYR H    H  N N 383 
TYR H2   H  N N 384 
TYR HA   H  N N 385 
TYR HB2  H  N N 386 
TYR HB3  H  N N 387 
TYR HD1  H  N N 388 
TYR HD2  H  N N 389 
TYR HE1  H  N N 390 
TYR HE2  H  N N 391 
TYR HH   H  N N 392 
TYR HXT  H  N N 393 
VAL N    N  N N 394 
VAL CA   C  N S 395 
VAL C    C  N N 396 
VAL O    O  N N 397 
VAL CB   C  N N 398 
VAL CG1  C  N N 399 
VAL CG2  C  N N 400 
VAL OXT  O  N N 401 
VAL H    H  N N 402 
VAL H2   H  N N 403 
VAL HA   H  N N 404 
VAL HB   H  N N 405 
VAL HG11 H  N N 406 
VAL HG12 H  N N 407 
VAL HG13 H  N N 408 
VAL HG21 H  N N 409 
VAL HG22 H  N N 410 
VAL HG23 H  N N 411 
VAL HXT  H  N N 412 
# 
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 
IMD N1  C2   sing Y N 182 
IMD N1  C5   sing Y N 183 
IMD N1  HN1  sing N N 184 
IMD C2  N3   doub Y N 185 
IMD C2  H2   sing N N 186 
IMD N3  C4   sing Y N 187 
IMD N3  HN3  sing N N 188 
IMD C4  C5   doub Y N 189 
IMD C4  H4   sing N N 190 
IMD C5  H5   sing N N 191 
LEU N   CA   sing N N 192 
LEU N   H    sing N N 193 
LEU N   H2   sing N N 194 
LEU CA  C    sing N N 195 
LEU CA  CB   sing N N 196 
LEU CA  HA   sing N N 197 
LEU C   O    doub N N 198 
LEU C   OXT  sing N N 199 
LEU CB  CG   sing N N 200 
LEU CB  HB2  sing N N 201 
LEU CB  HB3  sing N N 202 
LEU CG  CD1  sing N N 203 
LEU CG  CD2  sing N N 204 
LEU CG  HG   sing N N 205 
LEU CD1 HD11 sing N N 206 
LEU CD1 HD12 sing N N 207 
LEU CD1 HD13 sing N N 208 
LEU CD2 HD21 sing N N 209 
LEU CD2 HD22 sing N N 210 
LEU CD2 HD23 sing N N 211 
LEU OXT HXT  sing N N 212 
LYS N   CA   sing N N 213 
LYS N   H    sing N N 214 
LYS N   H2   sing N N 215 
LYS CA  C    sing N N 216 
LYS CA  CB   sing N N 217 
LYS CA  HA   sing N N 218 
LYS C   O    doub N N 219 
LYS C   OXT  sing N N 220 
LYS CB  CG   sing N N 221 
LYS CB  HB2  sing N N 222 
LYS CB  HB3  sing N N 223 
LYS CG  CD   sing N N 224 
LYS CG  HG2  sing N N 225 
LYS CG  HG3  sing N N 226 
LYS CD  CE   sing N N 227 
LYS CD  HD2  sing N N 228 
LYS CD  HD3  sing N N 229 
LYS CE  NZ   sing N N 230 
LYS CE  HE2  sing N N 231 
LYS CE  HE3  sing N N 232 
LYS NZ  HZ1  sing N N 233 
LYS NZ  HZ2  sing N N 234 
LYS NZ  HZ3  sing N N 235 
LYS OXT HXT  sing N N 236 
MET N   CA   sing N N 237 
MET N   H    sing N N 238 
MET N   H2   sing N N 239 
MET CA  C    sing N N 240 
MET CA  CB   sing N N 241 
MET CA  HA   sing N N 242 
MET C   O    doub N N 243 
MET C   OXT  sing N N 244 
MET CB  CG   sing N N 245 
MET CB  HB2  sing N N 246 
MET CB  HB3  sing N N 247 
MET CG  SD   sing N N 248 
MET CG  HG2  sing N N 249 
MET CG  HG3  sing N N 250 
MET SD  CE   sing N N 251 
MET CE  HE1  sing N N 252 
MET CE  HE2  sing N N 253 
MET CE  HE3  sing N N 254 
MET OXT HXT  sing N N 255 
PHE N   CA   sing N N 256 
PHE N   H    sing N N 257 
PHE N   H2   sing N N 258 
PHE CA  C    sing N N 259 
PHE CA  CB   sing N N 260 
PHE CA  HA   sing N N 261 
PHE C   O    doub N N 262 
PHE C   OXT  sing N N 263 
PHE CB  CG   sing N N 264 
PHE CB  HB2  sing N N 265 
PHE CB  HB3  sing N N 266 
PHE CG  CD1  doub Y N 267 
PHE CG  CD2  sing Y N 268 
PHE CD1 CE1  sing Y N 269 
PHE CD1 HD1  sing N N 270 
PHE CD2 CE2  doub Y N 271 
PHE CD2 HD2  sing N N 272 
PHE CE1 CZ   doub Y N 273 
PHE CE1 HE1  sing N N 274 
PHE CE2 CZ   sing Y N 275 
PHE CE2 HE2  sing N N 276 
PHE CZ  HZ   sing N N 277 
PHE OXT HXT  sing N N 278 
PRO N   CA   sing N N 279 
PRO N   CD   sing N N 280 
PRO N   H    sing N N 281 
PRO CA  C    sing N N 282 
PRO CA  CB   sing N N 283 
PRO CA  HA   sing N N 284 
PRO C   O    doub N N 285 
PRO C   OXT  sing N N 286 
PRO CB  CG   sing N N 287 
PRO CB  HB2  sing N N 288 
PRO CB  HB3  sing N N 289 
PRO CG  CD   sing N N 290 
PRO CG  HG2  sing N N 291 
PRO CG  HG3  sing N N 292 
PRO CD  HD2  sing N N 293 
PRO CD  HD3  sing N N 294 
PRO OXT HXT  sing N N 295 
SER N   CA   sing N N 296 
SER N   H    sing N N 297 
SER N   H2   sing N N 298 
SER CA  C    sing N N 299 
SER CA  CB   sing N N 300 
SER CA  HA   sing N N 301 
SER C   O    doub N N 302 
SER C   OXT  sing N N 303 
SER CB  OG   sing N N 304 
SER CB  HB2  sing N N 305 
SER CB  HB3  sing N N 306 
SER OG  HG   sing N N 307 
SER OXT HXT  sing N N 308 
THR N   CA   sing N N 309 
THR N   H    sing N N 310 
THR N   H2   sing N N 311 
THR CA  C    sing N N 312 
THR CA  CB   sing N N 313 
THR CA  HA   sing N N 314 
THR C   O    doub N N 315 
THR C   OXT  sing N N 316 
THR CB  OG1  sing N N 317 
THR CB  CG2  sing N N 318 
THR CB  HB   sing N N 319 
THR OG1 HG1  sing N N 320 
THR CG2 HG21 sing N N 321 
THR CG2 HG22 sing N N 322 
THR CG2 HG23 sing N N 323 
THR OXT HXT  sing N N 324 
TRP N   CA   sing N N 325 
TRP N   H    sing N N 326 
TRP N   H2   sing N N 327 
TRP CA  C    sing N N 328 
TRP CA  CB   sing N N 329 
TRP CA  HA   sing N N 330 
TRP C   O    doub N N 331 
TRP C   OXT  sing N N 332 
TRP CB  CG   sing N N 333 
TRP CB  HB2  sing N N 334 
TRP CB  HB3  sing N N 335 
TRP CG  CD1  doub Y N 336 
TRP CG  CD2  sing Y N 337 
TRP CD1 NE1  sing Y N 338 
TRP CD1 HD1  sing N N 339 
TRP CD2 CE2  doub Y N 340 
TRP CD2 CE3  sing Y N 341 
TRP NE1 CE2  sing Y N 342 
TRP NE1 HE1  sing N N 343 
TRP CE2 CZ2  sing Y N 344 
TRP CE3 CZ3  doub Y N 345 
TRP CE3 HE3  sing N N 346 
TRP CZ2 CH2  doub Y N 347 
TRP CZ2 HZ2  sing N N 348 
TRP CZ3 CH2  sing Y N 349 
TRP CZ3 HZ3  sing N N 350 
TRP CH2 HH2  sing N N 351 
TRP OXT HXT  sing N N 352 
TYR N   CA   sing N N 353 
TYR N   H    sing N N 354 
TYR N   H2   sing N N 355 
TYR CA  C    sing N N 356 
TYR CA  CB   sing N N 357 
TYR CA  HA   sing N N 358 
TYR C   O    doub N N 359 
TYR C   OXT  sing N N 360 
TYR CB  CG   sing N N 361 
TYR CB  HB2  sing N N 362 
TYR CB  HB3  sing N N 363 
TYR CG  CD1  doub Y N 364 
TYR CG  CD2  sing Y N 365 
TYR CD1 CE1  sing Y N 366 
TYR CD1 HD1  sing N N 367 
TYR CD2 CE2  doub Y N 368 
TYR CD2 HD2  sing N N 369 
TYR CE1 CZ   doub Y N 370 
TYR CE1 HE1  sing N N 371 
TYR CE2 CZ   sing Y N 372 
TYR CE2 HE2  sing N N 373 
TYR CZ  OH   sing N N 374 
TYR OH  HH   sing N N 375 
TYR OXT HXT  sing N N 376 
VAL N   CA   sing N N 377 
VAL N   H    sing N N 378 
VAL N   H2   sing N N 379 
VAL CA  C    sing N N 380 
VAL CA  CB   sing N N 381 
VAL CA  HA   sing N N 382 
VAL C   O    doub N N 383 
VAL C   OXT  sing N N 384 
VAL CB  CG1  sing N N 385 
VAL CB  CG2  sing N N 386 
VAL CB  HB   sing N N 387 
VAL CG1 HG11 sing N N 388 
VAL CG1 HG12 sing N N 389 
VAL CG1 HG13 sing N N 390 
VAL CG2 HG21 sing N N 391 
VAL CG2 HG22 sing N N 392 
VAL CG2 HG23 sing N N 393 
VAL OXT HXT  sing N N 394 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           BC63C22000680007 
_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   7DET 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HY2 
_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]   0.015523 
_atom_sites.fract_transf_matrix[1][2]   0.008962 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017925 
_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]   0.006206 
_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 
N  
NA 
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   . GLN A 1 3   ? -11.733 13.033  14.949  1.00 62.80 ? 3   GLN A N   1 
ATOM   2    C  CA  . GLN A 1 3   ? -12.782 12.346  14.140  1.00 62.00 ? 3   GLN A CA  1 
ATOM   3    C  C   . GLN A 1 3   ? -14.183 12.792  14.591  1.00 52.22 ? 3   GLN A C   1 
ATOM   4    O  O   . GLN A 1 3   ? -14.435 13.112  15.759  1.00 55.78 ? 3   GLN A O   1 
ATOM   5    C  CB  . GLN A 1 3   ? -12.521 10.840  14.062  1.00 68.77 ? 3   GLN A CB  1 
ATOM   6    C  CG  . GLN A 1 3   ? -12.432 10.148  15.419  0.50 64.92 ? 3   GLN A CG  1 
ATOM   7    C  CD  . GLN A 1 3   ? -12.287 8.644   15.322  0.50 61.98 ? 3   GLN A CD  1 
ATOM   8    O  OE1 . GLN A 1 3   ? -12.527 8.028   14.275  0.50 56.23 ? 3   GLN A OE1 1 
ATOM   9    N  NE2 . GLN A 1 3   ? -11.913 8.035   16.437  0.50 62.51 ? 3   GLN A NE2 1 
ATOM   10   N  N   . GLU A 1 4   ? -15.058 12.904  13.597  1.00 46.06 ? 4   GLU A N   1 
ATOM   11   C  CA  . GLU A 1 4   ? -16.411 13.436  13.855  1.00 41.27 ? 4   GLU A CA  1 
ATOM   12   C  C   . GLU A 1 4   ? -17.246 12.411  14.616  1.00 42.52 ? 4   GLU A C   1 
ATOM   13   O  O   . GLU A 1 4   ? -17.241 11.235  14.236  1.00 41.60 ? 4   GLU A O   1 
ATOM   14   C  CB  . GLU A 1 4   ? -16.993 13.807  12.498  1.00 44.23 ? 4   GLU A CB  1 
ATOM   15   C  CG  . GLU A 1 4   ? -16.071 14.686  11.664  1.00 49.61 ? 4   GLU A CG  1 
ATOM   16   C  CD  . GLU A 1 4   ? -16.732 15.110  10.370  1.00 54.90 ? 4   GLU A CD  1 
ATOM   17   O  OE1 . GLU A 1 4   ? -17.933 15.431  10.404  1.00 51.64 ? 4   GLU A OE1 1 
ATOM   18   O  OE2 . GLU A 1 4   ? -16.047 15.113  9.332   1.00 66.89 ? 4   GLU A OE2 1 
ATOM   19   N  N   . GLN A 1 5   ? -17.914 12.872  15.663  1.00 34.58 ? 5   GLN A N   1 
ATOM   20   C  CA  . GLN A 1 5   ? -18.692 11.938  16.491  1.00 37.82 ? 5   GLN A CA  1 
ATOM   21   C  C   . GLN A 1 5   ? -19.983 12.572  16.983  1.00 35.94 ? 5   GLN A C   1 
ATOM   22   O  O   . GLN A 1 5   ? -19.987 13.785  17.229  1.00 35.59 ? 5   GLN A O   1 
ATOM   23   C  CB  . GLN A 1 5   ? -17.922 11.544  17.746  1.00 41.62 ? 5   GLN A CB  1 
ATOM   24   C  CG  . GLN A 1 5   ? -16.649 10.751  17.485  0.70 54.14 ? 5   GLN A CG  1 
ATOM   25   C  CD  . GLN A 1 5   ? -15.781 10.629  18.716  0.70 57.88 ? 5   GLN A CD  1 
ATOM   26   O  OE1 . GLN A 1 5   ? -16.273 10.403  19.826  0.70 56.47 ? 5   GLN A OE1 1 
ATOM   27   N  NE2 . GLN A 1 5   ? -14.479 10.785  18.529  0.70 66.83 ? 5   GLN A NE2 1 
ATOM   28   N  N   . LEU A 1 6   ? -21.029 11.762  17.080  1.00 33.48 ? 6   LEU A N   1 
ATOM   29   C  CA  . LEU A 1 6   ? -22.307 12.191  17.676  1.00 30.45 ? 6   LEU A CA  1 
ATOM   30   C  C   . LEU A 1 6   ? -22.469 11.241  18.863  1.00 34.66 ? 6   LEU A C   1 
ATOM   31   O  O   . LEU A 1 6   ? -22.682 10.050  18.621  1.00 36.06 ? 6   LEU A O   1 
ATOM   32   C  CB  . LEU A 1 6   ? -23.439 12.068  16.664  1.00 29.07 ? 6   LEU A CB  1 
ATOM   33   C  CG  . LEU A 1 6   ? -23.289 12.849  15.357  1.00 34.15 ? 6   LEU A CG  1 
ATOM   34   C  CD1 . LEU A 1 6   ? -24.514 12.614  14.499  1.00 27.48 ? 6   LEU A CD1 1 
ATOM   35   C  CD2 . LEU A 1 6   ? -23.123 14.324  15.639  1.00 33.73 ? 6   LEU A CD2 1 
ATOM   36   N  N   . GLN A 1 7   ? -22.340 11.744  20.085  1.00 31.28 ? 7   GLN A N   1 
ATOM   37   C  CA  . GLN A 1 7   ? -22.298 10.878  21.264  1.00 33.39 ? 7   GLN A CA  1 
ATOM   38   C  C   . GLN A 1 7   ? -23.618 11.002  22.040  1.00 33.05 ? 7   GLN A C   1 
ATOM   39   O  O   . GLN A 1 7   ? -23.995 12.088  22.488  1.00 34.44 ? 7   GLN A O   1 
ATOM   40   C  CB  . GLN A 1 7   ? -21.054 11.228  22.088  1.00 35.97 ? 7   GLN A CB  1 
ATOM   41   C  CG  . GLN A 1 7   ? -21.122 10.611  23.489  1.00 46.26 ? 7   GLN A CG  1 
ATOM   42   C  CD  . GLN A 1 7   ? -20.035 11.116  24.407  0.70 54.73 ? 7   GLN A CD  1 
ATOM   43   O  OE1 . GLN A 1 7   ? -18.846 11.099  24.062  0.70 57.61 ? 7   GLN A OE1 1 
ATOM   44   N  NE2 . GLN A 1 7   ? -20.442 11.579  25.577  0.70 57.21 ? 7   GLN A NE2 1 
ATOM   45   N  N   . GLN A 1 8   ? -24.323 9.864   22.185  1.00 30.44 ? 8   GLN A N   1 
ATOM   46   C  CA  . GLN A 1 8   ? -25.622 9.805   22.839  1.00 30.66 ? 8   GLN A CA  1 
ATOM   47   C  C   . GLN A 1 8   ? -25.533 8.848   24.041  1.00 30.88 ? 8   GLN A C   1 
ATOM   48   O  O   . GLN A 1 8   ? -24.963 7.769   23.884  1.00 31.40 ? 8   GLN A O   1 
ATOM   49   C  CB  . GLN A 1 8   ? -26.632 9.173   21.887  1.00 31.78 ? 8   GLN A CB  1 
ATOM   50   C  CG  . GLN A 1 8   ? -26.943 10.097  20.691  1.00 29.83 ? 8   GLN A CG  1 
ATOM   51   C  CD  . GLN A 1 8   ? -28.024 9.520   19.805  1.00 30.42 ? 8   GLN A CD  1 
ATOM   52   O  OE1 . GLN A 1 8   ? -27.719 8.888   18.784  1.00 29.60 ? 8   GLN A OE1 1 
ATOM   53   N  NE2 . GLN A 1 8   ? -29.266 9.658   20.242  1.00 30.56 ? 8   GLN A NE2 1 
ATOM   54   N  N   . PRO A 1 9   ? -26.172 9.115   25.210  1.00 42.67 ? 9   PRO A N   1 
ATOM   55   C  CA  . PRO A 1 9   ? -26.281 8.097   26.279  1.00 38.71 ? 9   PRO A CA  1 
ATOM   56   C  C   . PRO A 1 9   ? -26.924 6.760   25.865  1.00 46.18 ? 9   PRO A C   1 
ATOM   57   O  O   . PRO A 1 9   ? -27.729 6.697   24.928  1.00 37.83 ? 9   PRO A O   1 
ATOM   58   C  CB  . PRO A 1 9   ? -27.141 8.772   27.322  1.00 44.91 ? 9   PRO A CB  1 
ATOM   59   C  CG  . PRO A 1 9   ? -27.923 9.721   26.469  1.00 51.28 ? 9   PRO A CG  1 
ATOM   60   C  CD  . PRO A 1 9   ? -26.905 10.348  25.517  1.00 45.02 ? 9   PRO A CD  1 
ATOM   61   N  N   . GLY A 1 10  ? -26.617 5.653   26.571  1.00 43.58 ? 10  GLY A N   1 
ATOM   62   C  CA  . GLY A 1 10  ? -27.087 4.343   26.085  1.00 39.53 ? 10  GLY A CA  1 
ATOM   63   C  C   . GLY A 1 10  ? -28.601 4.072   26.281  1.00 44.71 ? 10  GLY A C   1 
ATOM   64   O  O   . GLY A 1 10  ? -29.248 3.398   25.422  1.00 35.52 ? 10  GLY A O   1 
ATOM   65   N  N   . THR A 1 11  ? -29.121 4.459   27.487  1.00 39.27 ? 11  THR A N   1 
ATOM   66   C  CA  . THR A 1 11  ? -30.469 4.141   27.962  1.00 39.32 ? 11  THR A CA  1 
ATOM   67   C  C   . THR A 1 11  ? -31.024 5.254   28.854  1.00 48.12 ? 11  THR A C   1 
ATOM   68   O  O   . THR A 1 11  ? -30.323 5.929   29.615  1.00 50.69 ? 11  THR A O   1 
ATOM   69   C  CB  . THR A 1 11  ? -30.505 2.871   28.860  1.00 41.40 ? 11  THR A CB  1 
ATOM   70   O  OG1 . THR A 1 11  ? -29.519 3.057   29.891  1.00 41.52 ? 11  THR A OG1 1 
ATOM   71   C  CG2 . THR A 1 11  ? -30.190 1.592   28.100  1.00 41.84 ? 11  THR A CG2 1 
ATOM   72   N  N   . GLU A 1 12  ? -32.352 5.328   28.850  1.00 44.13 ? 12  GLU A N   1 
ATOM   73   C  CA  . GLU A 1 12  ? -33.077 6.129   29.807  1.00 46.58 ? 12  GLU A CA  1 
ATOM   74   C  C   . GLU A 1 12  ? -34.283 5.294   30.226  1.00 48.29 ? 12  GLU A C   1 
ATOM   75   O  O   . GLU A 1 12  ? -35.049 4.884   29.336  1.00 37.87 ? 12  GLU A O   1 
ATOM   76   C  CB  . GLU A 1 12  ? -33.518 7.410   29.090  1.00 39.08 ? 12  GLU A CB  1 
ATOM   77   C  CG  . GLU A 1 12  ? -32.374 8.373   28.786  1.00 45.59 ? 12  GLU A CG  1 
ATOM   78   C  CD  . GLU A 1 12  ? -31.615 8.976   29.965  0.70 51.67 ? 12  GLU A CD  1 
ATOM   79   O  OE1 . GLU A 1 12  ? -32.037 9.005   31.149  0.70 49.79 ? 12  GLU A OE1 1 
ATOM   80   O  OE2 . GLU A 1 12  ? -30.500 9.433   29.653  0.70 54.67 ? 12  GLU A OE2 1 
ATOM   81   N  N   . LEU A 1 13  ? -34.435 5.091   31.561  1.00 45.87 ? 13  LEU A N   1 
ATOM   82   C  CA  . LEU A 1 13  ? -35.556 4.326   32.090  1.00 41.18 ? 13  LEU A CA  1 
ATOM   83   C  C   . LEU A 1 13  ? -36.549 5.267   32.765  1.00 40.85 ? 13  LEU A C   1 
ATOM   84   O  O   . LEU A 1 13  ? -36.232 5.836   33.790  1.00 39.88 ? 13  LEU A O   1 
ATOM   85   C  CB  . LEU A 1 13  ? -35.007 3.300   33.066  1.00 40.02 ? 13  LEU A CB  1 
ATOM   86   C  CG  . LEU A 1 13  ? -36.051 2.290   33.549  1.00 39.46 ? 13  LEU A CG  1 
ATOM   87   C  CD1 . LEU A 1 13  ? -36.414 1.292   32.499  1.00 37.38 ? 13  LEU A CD1 1 
ATOM   88   C  CD2 . LEU A 1 13  ? -35.489 1.488   34.682  1.00 39.93 ? 13  LEU A CD2 1 
ATOM   89   N  N   . VAL A 1 14  ? -37.766 5.411   32.225  1.00 38.18 ? 14  VAL A N   1 
ATOM   90   C  CA  . VAL A 1 14  ? -38.599 6.577   32.526  1.00 35.40 ? 14  VAL A CA  1 
ATOM   91   C  C   . VAL A 1 14  ? -40.029 6.102   32.786  1.00 39.62 ? 14  VAL A C   1 
ATOM   92   O  O   . VAL A 1 14  ? -40.421 5.032   32.314  1.00 40.38 ? 14  VAL A O   1 
ATOM   93   C  CB  . VAL A 1 14  ? -38.549 7.583   31.354  1.00 35.04 ? 14  VAL A CB  1 
ATOM   94   C  CG1 . VAL A 1 14  ? -37.130 8.112   31.187  1.00 38.33 ? 14  VAL A CG1 1 
ATOM   95   C  CG2 . VAL A 1 14  ? -38.983 6.917   30.041  1.00 36.44 ? 14  VAL A CG2 1 
ATOM   96   N  N   . LYS A 1 15  ? -40.801 6.895   33.550  1.00 42.77 ? 15  LYS A N   1 
ATOM   97   C  CA  . LYS A 1 15  ? -42.172 6.563   33.931  1.00 42.76 ? 15  LYS A CA  1 
ATOM   98   C  C   . LYS A 1 15  ? -43.150 7.146   32.908  1.00 43.07 ? 15  LYS A C   1 
ATOM   99   O  O   . LYS A 1 15  ? -42.884 8.193   32.313  1.00 45.24 ? 15  LYS A O   1 
ATOM   100  C  CB  . LYS A 1 15  ? -42.543 7.292   35.233  1.00 50.70 ? 15  LYS A CB  1 
ATOM   101  C  CG  . LYS A 1 15  ? -41.478 7.296   36.316  1.00 53.56 ? 15  LYS A CG  1 
ATOM   102  C  CD  . LYS A 1 15  ? -41.797 7.922   37.674  0.70 50.68 ? 15  LYS A CD  1 
ATOM   103  C  CE  . LYS A 1 15  ? -42.766 7.094   38.452  0.70 55.11 ? 15  LYS A CE  1 
ATOM   104  N  NZ  . LYS A 1 15  ? -42.831 7.395   39.895  0.70 57.56 ? 15  LYS A NZ  1 
ATOM   105  N  N   . PRO A 1 16  ? -44.316 6.499   32.670  1.00 42.08 ? 16  PRO A N   1 
ATOM   106  C  CA  . PRO A 1 16  ? -45.376 7.125   31.857  1.00 43.46 ? 16  PRO A CA  1 
ATOM   107  C  C   . PRO A 1 16  ? -45.733 8.494   32.416  1.00 44.69 ? 16  PRO A C   1 
ATOM   108  O  O   . PRO A 1 16  ? -45.739 8.674   33.623  1.00 43.79 ? 16  PRO A O   1 
ATOM   109  C  CB  . PRO A 1 16  ? -46.562 6.157   31.932  1.00 46.90 ? 16  PRO A CB  1 
ATOM   110  C  CG  . PRO A 1 16  ? -45.913 4.831   32.328  1.00 43.16 ? 16  PRO A CG  1 
ATOM   111  C  CD  . PRO A 1 16  ? -44.657 5.151   33.162  1.00 43.27 ? 16  PRO A CD  1 
ATOM   112  N  N   . GLY A 1 17  ? -45.958 9.464   31.530  1.00 43.15 ? 17  GLY A N   1 
ATOM   113  C  CA  . GLY A 1 17  ? -46.378 10.784  31.976  1.00 47.37 ? 17  GLY A CA  1 
ATOM   114  C  C   . GLY A 1 17  ? -45.202 11.740  32.177  1.00 46.20 ? 17  GLY A C   1 
ATOM   115  O  O   . GLY A 1 17  ? -45.412 12.935  32.117  1.00 48.05 ? 17  GLY A O   1 
ATOM   116  N  N   . ALA A 1 18  ? -43.973 11.222  32.396  1.00 44.76 ? 18  ALA A N   1 
ATOM   117  C  CA  . ALA A 1 18  ? -42.798 12.071  32.573  1.00 41.49 ? 18  ALA A CA  1 
ATOM   118  C  C   . ALA A 1 18  ? -42.364 12.665  31.222  1.00 42.88 ? 18  ALA A C   1 
ATOM   119  O  O   . ALA A 1 18  ? -42.949 12.331  30.175  1.00 42.42 ? 18  ALA A O   1 
ATOM   120  C  CB  . ALA A 1 18  ? -41.682 11.253  33.235  1.00 40.17 ? 18  ALA A CB  1 
ATOM   121  N  N   . SER A 1 19  ? -41.348 13.548  31.277  1.00 39.71 ? 19  SER A N   1 
ATOM   122  C  CA  . SER A 1 19  ? -40.604 14.065  30.136  1.00 42.80 ? 19  SER A CA  1 
ATOM   123  C  C   . SER A 1 19  ? -39.192 13.524  30.222  1.00 44.33 ? 19  SER A C   1 
ATOM   124  O  O   . SER A 1 19  ? -38.716 13.272  31.322  1.00 43.80 ? 19  SER A O   1 
ATOM   125  C  CB  . SER A 1 19  ? -40.496 15.580  30.186  1.00 43.27 ? 19  SER A CB  1 
ATOM   126  O  OG  . SER A 1 19  ? -41.768 16.095  29.851  1.00 61.44 ? 19  SER A OG  1 
ATOM   127  N  N   . VAL A 1 20  ? -38.515 13.381  29.078  1.00 39.97 ? 20  VAL A N   1 
ATOM   128  C  CA  . VAL A 1 20  ? -37.105 13.013  29.125  1.00 37.83 ? 20  VAL A CA  1 
ATOM   129  C  C   . VAL A 1 20  ? -36.356 13.873  28.100  1.00 36.89 ? 20  VAL A C   1 
ATOM   130  O  O   . VAL A 1 20  ? -36.896 14.218  27.046  1.00 37.93 ? 20  VAL A O   1 
ATOM   131  C  CB  . VAL A 1 20  ? -36.871 11.499  28.937  1.00 36.87 ? 20  VAL A CB  1 
ATOM   132  C  CG1 . VAL A 1 20  ? -37.288 11.018  27.550  1.00 37.40 ? 20  VAL A CG1 1 
ATOM   133  C  CG2 . VAL A 1 20  ? -35.432 11.100  29.217  1.00 39.29 ? 20  VAL A CG2 1 
ATOM   134  N  N   . ARG A 1 21  ? -35.136 14.255  28.450  1.00 37.28 ? 21  ARG A N   1 
ATOM   135  C  CA  . ARG A 1 21  ? -34.308 15.046  27.516  1.00 36.30 ? 21  ARG A CA  1 
ATOM   136  C  C   . ARG A 1 21  ? -33.146 14.184  27.034  1.00 37.57 ? 21  ARG A C   1 
ATOM   137  O  O   . ARG A 1 21  ? -32.331 13.762  27.860  1.00 37.97 ? 21  ARG A O   1 
ATOM   138  C  CB  . ARG A 1 21  ? -33.747 16.326  28.132  1.00 40.55 ? 21  ARG A CB  1 
ATOM   139  C  CG  . ARG A 1 21  ? -33.325 17.316  27.058  1.00 44.22 ? 21  ARG A CG  1 
ATOM   140  C  CD  . ARG A 1 21  ? -33.008 18.671  27.651  1.00 55.19 ? 21  ARG A CD  1 
ATOM   141  N  NE  . ARG A 1 21  ? -31.796 18.608  28.472  1.00 59.53 ? 21  ARG A NE  1 
ATOM   142  C  CZ  . ARG A 1 21  ? -30.939 19.607  28.606  1.00 67.19 ? 21  ARG A CZ  1 
ATOM   143  N  NH1 . ARG A 1 21  ? -31.141 20.740  27.958  1.00 63.47 ? 21  ARG A NH1 1 
ATOM   144  N  NH2 . ARG A 1 21  ? -29.878 19.463  29.376  1.00 61.51 ? 21  ARG A NH2 1 
ATOM   145  N  N   . LEU A 1 22  ? -33.099 13.945  25.728  1.00 36.41 ? 22  LEU A N   1 
ATOM   146  C  CA  . LEU A 1 22  ? -32.009 13.164  25.147  1.00 36.51 ? 22  LEU A CA  1 
ATOM   147  C  C   . LEU A 1 22  ? -30.931 14.118  24.653  1.00 38.29 ? 22  LEU A C   1 
ATOM   148  O  O   . LEU A 1 22  ? -31.295 15.177  24.143  1.00 33.58 ? 22  LEU A O   1 
ATOM   149  C  CB  . LEU A 1 22  ? -32.583 12.415  23.937  1.00 31.33 ? 22  LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 22  ? -33.711 11.430  24.294  1.00 36.37 ? 22  LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 22  ? -34.022 10.463  23.160  1.00 37.55 ? 22  LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 22  ? -33.401 10.645  25.534  1.00 34.94 ? 22  LEU A CD2 1 
ATOM   153  N  N   . SER A 1 23  ? -29.650 13.722  24.753  1.00 34.42 ? 23  SER A N   1 
ATOM   154  C  CA  . SER A 1 23  ? -28.584 14.632  24.328  1.00 33.42 ? 23  SER A CA  1 
ATOM   155  C  C   . SER A 1 23  ? -27.800 13.970  23.201  1.00 36.03 ? 23  SER A C   1 
ATOM   156  O  O   . SER A 1 23  ? -27.720 12.742  23.106  1.00 34.02 ? 23  SER A O   1 
ATOM   157  C  CB  . SER A 1 23  ? -27.692 15.026  25.467  1.00 37.67 ? 23  SER A CB  1 
ATOM   158  O  OG  . SER A 1 23  ? -27.283 13.826  26.130  1.00 40.26 ? 23  SER A OG  1 
ATOM   159  N  N   . CYS A 1 24  ? -27.227 14.812  22.344  1.00 32.51 ? 24  CYS A N   1 
ATOM   160  C  CA  . CYS A 1 24  ? -26.362 14.390  21.267  1.00 35.42 ? 24  CYS A CA  1 
ATOM   161  C  C   . CYS A 1 24  ? -25.167 15.343  21.310  1.00 35.57 ? 24  CYS A C   1 
ATOM   162  O  O   . CYS A 1 24  ? -25.298 16.471  20.837  1.00 33.92 ? 24  CYS A O   1 
ATOM   163  C  CB  . CYS A 1 24  ? -27.169 14.508  19.979  1.00 30.85 ? 24  CYS A CB  1 
ATOM   164  S  SG  . CYS A 1 24  ? -26.174 14.192  18.494  1.00 40.40 ? 24  CYS A SG  1 
ATOM   165  N  N   . LYS A 1 25  ? -24.043 14.907  21.913  1.00 34.99 ? 25  LYS A N   1 
ATOM   166  C  CA  . LYS A 1 25  ? -22.841 15.731  22.096  1.00 37.30 ? 25  LYS A CA  1 
ATOM   167  C  C   . LYS A 1 25  ? -21.944 15.576  20.872  1.00 40.36 ? 25  LYS A C   1 
ATOM   168  O  O   . LYS A 1 25  ? -21.501 14.455  20.593  1.00 37.92 ? 25  LYS A O   1 
ATOM   169  C  CB  . LYS A 1 25  ? -22.115 15.332  23.395  1.00 37.55 ? 25  LYS A CB  1 
ATOM   170  C  CG  . LYS A 1 25  ? -20.913 16.237  23.731  1.00 43.97 ? 25  LYS A CG  1 
ATOM   171  N  N   . THR A 1 26  ? -21.728 16.677  20.091  1.00 34.07 ? 26  THR A N   1 
ATOM   172  C  CA  . THR A 1 26  ? -21.043 16.516  18.822  1.00 35.32 ? 26  THR A CA  1 
ATOM   173  C  C   . THR A 1 26  ? -19.585 16.902  19.007  1.00 36.44 ? 26  THR A C   1 
ATOM   174  O  O   . THR A 1 26  ? -19.263 17.695  19.900  1.00 35.36 ? 26  THR A O   1 
ATOM   175  C  CB  . THR A 1 26  ? -21.694 17.400  17.749  1.00 33.36 ? 26  THR A CB  1 
ATOM   176  O  OG1 . THR A 1 26  ? -21.382 18.775  18.039  1.00 33.30 ? 26  THR A OG1 1 
ATOM   177  C  CG2 . THR A 1 26  ? -23.204 17.213  17.694  1.00 31.77 ? 26  THR A CG2 1 
ATOM   178  N  N   . SER A 1 27  ? -18.723 16.400  18.130  1.00 35.55 ? 27  SER A N   1 
ATOM   179  C  CA  . SER A 1 27  ? -17.325 16.815  18.139  1.00 35.69 ? 27  SER A CA  1 
ATOM   180  C  C   . SER A 1 27  ? -16.709 16.548  16.779  1.00 39.93 ? 27  SER A C   1 
ATOM   181  O  O   . SER A 1 27  ? -17.263 15.794  15.961  1.00 36.96 ? 27  SER A O   1 
ATOM   182  C  CB  . SER A 1 27  ? -16.510 16.133  19.251  1.00 42.55 ? 27  SER A CB  1 
ATOM   183  O  OG  . SER A 1 27  ? -16.595 14.716  19.137  1.00 44.93 ? 27  SER A OG  1 
ATOM   184  N  N   . GLY A 1 28  ? -15.556 17.184  16.536  1.00 38.47 ? 28  GLY A N   1 
ATOM   185  C  CA  . GLY A 1 28  ? -14.858 16.811  15.317  1.00 39.32 ? 28  GLY A CA  1 
ATOM   186  C  C   . GLY A 1 28  ? -15.241 17.659  14.105  1.00 41.06 ? 28  GLY A C   1 
ATOM   187  O  O   . GLY A 1 28  ? -14.649 17.442  13.061  1.00 38.45 ? 28  GLY A O   1 
ATOM   188  N  N   . TYR A 1 29  ? -16.247 18.545  14.207  1.00 36.97 ? 29  TYR A N   1 
ATOM   189  C  CA  . TYR A 1 29  ? -16.643 19.404  13.083  1.00 36.81 ? 29  TYR A CA  1 
ATOM   190  C  C   . TYR A 1 29  ? -17.378 20.617  13.668  1.00 36.21 ? 29  TYR A C   1 
ATOM   191  O  O   . TYR A 1 29  ? -17.678 20.658  14.863  1.00 34.76 ? 29  TYR A O   1 
ATOM   192  C  CB  . TYR A 1 29  ? -17.531 18.609  12.101  1.00 33.85 ? 29  TYR A CB  1 
ATOM   193  C  CG  . TYR A 1 29  ? -18.925 18.360  12.680  1.00 35.90 ? 29  TYR A CG  1 
ATOM   194  C  CD1 . TYR A 1 29  ? -19.190 17.289  13.539  1.00 33.70 ? 29  TYR A CD1 1 
ATOM   195  C  CD2 . TYR A 1 29  ? -19.975 19.234  12.406  1.00 34.10 ? 29  TYR A CD2 1 
ATOM   196  C  CE1 . TYR A 1 29  ? -20.458 17.093  14.078  1.00 33.90 ? 29  TYR A CE1 1 
ATOM   197  C  CE2 . TYR A 1 29  ? -21.259 19.024  12.886  1.00 34.04 ? 29  TYR A CE2 1 
ATOM   198  C  CZ  . TYR A 1 29  ? -21.495 17.953  13.744  1.00 35.24 ? 29  TYR A CZ  1 
ATOM   199  O  OH  . TYR A 1 29  ? -22.762 17.837  14.252  1.00 33.33 ? 29  TYR A OH  1 
ATOM   200  N  N   . THR A 1 30  ? -17.725 21.595  12.830  1.00 34.86 ? 30  THR A N   1 
ATOM   201  C  CA  . THR A 1 30  ? -18.414 22.815  13.302  1.00 34.91 ? 30  THR A CA  1 
ATOM   202  C  C   . THR A 1 30  ? -19.886 22.539  13.506  1.00 37.69 ? 30  THR A C   1 
ATOM   203  O  O   . THR A 1 30  ? -20.613 22.478  12.512  1.00 34.82 ? 30  THR A O   1 
ATOM   204  C  CB  . THR A 1 30  ? -18.180 23.986  12.346  1.00 37.99 ? 30  THR A CB  1 
ATOM   205  O  OG1 . THR A 1 30  ? -16.772 24.074  12.163  1.00 39.69 ? 30  THR A OG1 1 
ATOM   206  C  CG2 . THR A 1 30  ? -18.744 25.283  12.894  1.00 38.80 ? 30  THR A CG2 1 
ATOM   207  N  N   . PHE A 1 31  ? -20.321 22.448  14.759  1.00 35.28 ? 31  PHE A N   1 
ATOM   208  C  CA  . PHE A 1 31  ? -21.719 22.086  15.093  1.00 32.68 ? 31  PHE A CA  1 
ATOM   209  C  C   . PHE A 1 31  ? -22.728 23.025  14.491  1.00 38.82 ? 31  PHE A C   1 
ATOM   210  O  O   . PHE A 1 31  ? -23.776 22.566  14.041  1.00 33.00 ? 31  PHE A O   1 
ATOM   211  C  CB  . PHE A 1 31  ? -21.753 22.185  16.618  1.00 33.60 ? 31  PHE A CB  1 
ATOM   212  C  CG  . PHE A 1 31  ? -23.100 22.046  17.311  1.00 36.80 ? 31  PHE A CG  1 
ATOM   213  C  CD1 . PHE A 1 31  ? -23.803 20.851  17.272  1.00 38.38 ? 31  PHE A CD1 1 
ATOM   214  C  CD2 . PHE A 1 31  ? -23.645 23.104  18.027  1.00 35.71 ? 31  PHE A CD2 1 
ATOM   215  C  CE1 . PHE A 1 31  ? -25.021 20.726  17.914  1.00 39.33 ? 31  PHE A CE1 1 
ATOM   216  C  CE2 . PHE A 1 31  ? -24.864 22.974  18.664  1.00 32.70 ? 31  PHE A CE2 1 
ATOM   217  C  CZ  . PHE A 1 31  ? -25.549 21.786  18.607  1.00 37.60 ? 31  PHE A CZ  1 
ATOM   218  N  N   . ALA A 1 32  ? -22.439 24.319  14.514  1.00 37.59 ? 32  ALA A N   1 
ATOM   219  C  CA  . ALA A 1 32  ? -23.443 25.313  14.089  1.00 37.01 ? 32  ALA A CA  1 
ATOM   220  C  C   . ALA A 1 32  ? -23.712 25.237  12.594  1.00 36.28 ? 32  ALA A C   1 
ATOM   221  O  O   . ALA A 1 32  ? -24.757 25.726  12.178  1.00 42.05 ? 32  ALA A O   1 
ATOM   222  C  CB  . ALA A 1 32  ? -22.914 26.677  14.437  1.00 40.15 ? 32  ALA A CB  1 
ATOM   223  N  N   . SER A 1 33  ? -22.842 24.583  11.846  1.00 31.99 ? 33  SER A N   1 
ATOM   224  C  CA  . SER A 1 33  ? -22.921 24.647  10.392  1.00 33.25 ? 33  SER A CA  1 
ATOM   225  C  C   . SER A 1 33  ? -23.678 23.489  9.719   1.00 34.57 ? 33  SER A C   1 
ATOM   226  O  O   . SER A 1 33  ? -23.833 23.534  8.503   1.00 33.16 ? 33  SER A O   1 
ATOM   227  C  CB  . SER A 1 33  ? -21.535 24.804  9.783   1.00 35.32 ? 33  SER A CB  1 
ATOM   228  O  OG  . SER A 1 33  ? -20.918 26.022  10.237  1.00 39.51 ? 33  SER A OG  1 
ATOM   229  N  N   . TYR A 1 34  ? -24.142 22.439  10.442  1.00 31.41 ? 34  TYR A N   1 
ATOM   230  C  CA  . TYR A 1 34  ? -24.755 21.289  9.786   1.00 31.38 ? 34  TYR A CA  1 
ATOM   231  C  C   . TYR A 1 34  ? -26.066 20.947  10.466  1.00 35.77 ? 34  TYR A C   1 
ATOM   232  O  O   . TYR A 1 34  ? -26.113 20.817  11.690  1.00 32.79 ? 34  TYR A O   1 
ATOM   233  C  CB  . TYR A 1 34  ? -23.834 20.071  9.867   1.00 31.11 ? 34  TYR A CB  1 
ATOM   234  C  CG  . TYR A 1 34  ? -22.586 20.264  9.036   1.00 32.49 ? 34  TYR A CG  1 
ATOM   235  C  CD1 . TYR A 1 34  ? -21.479 20.966  9.519   1.00 32.61 ? 34  TYR A CD1 1 
ATOM   236  C  CD2 . TYR A 1 34  ? -22.544 19.734  7.746   1.00 29.84 ? 34  TYR A CD2 1 
ATOM   237  C  CE1 . TYR A 1 34  ? -20.366 21.183  8.715   1.00 33.56 ? 34  TYR A CE1 1 
ATOM   238  C  CE2 . TYR A 1 34  ? -21.433 19.928  6.936   1.00 31.18 ? 34  TYR A CE2 1 
ATOM   239  C  CZ  . TYR A 1 34  ? -20.354 20.671  7.418   1.00 33.44 ? 34  TYR A CZ  1 
ATOM   240  O  OH  . TYR A 1 34  ? -19.342 20.798  6.506   1.00 34.37 ? 34  TYR A OH  1 
ATOM   241  N  N   . THR A 1 35  ? -27.121 20.742  9.670   1.00 30.87 ? 35  THR A N   1 
ATOM   242  C  CA  . THR A 1 35  ? -28.403 20.318  10.216  1.00 31.75 ? 35  THR A CA  1 
ATOM   243  C  C   . THR A 1 35  ? -28.204 18.965  10.941  1.00 31.41 ? 35  THR A C   1 
ATOM   244  O  O   . THR A 1 35  ? -27.503 18.083  10.446  1.00 31.95 ? 35  THR A O   1 
ATOM   245  C  CB  . THR A 1 35  ? -29.383 20.215  9.030   1.00 30.98 ? 35  THR A CB  1 
ATOM   246  O  OG1 . THR A 1 35  ? -29.597 21.544  8.524   1.00 34.31 ? 35  THR A OG1 1 
ATOM   247  C  CG2 . THR A 1 35  ? -30.756 19.687  9.449   1.00 32.12 ? 35  THR A CG2 1 
ATOM   248  N  N   . LEU A 1 36  ? -28.856 18.782  12.109  1.00 31.70 ? 36  LEU A N   1 
ATOM   249  C  CA  . LEU A 1 36  ? -28.941 17.473  12.763  1.00 31.97 ? 36  LEU A CA  1 
ATOM   250  C  C   . LEU A 1 36  ? -30.387 17.013  12.764  1.00 33.39 ? 36  LEU A C   1 
ATOM   251  O  O   . LEU A 1 36  ? -31.321 17.820  13.000  1.00 36.22 ? 36  LEU A O   1 
ATOM   252  C  CB  . LEU A 1 36  ? -28.436 17.643  14.195  1.00 32.49 ? 36  LEU A CB  1 
ATOM   253  C  CG  . LEU A 1 36  ? -26.920 17.761  14.276  1.00 36.42 ? 36  LEU A CG  1 
ATOM   254  C  CD1 . LEU A 1 36  ? -26.585 18.011  15.751  1.00 39.08 ? 36  LEU A CD1 1 
ATOM   255  C  CD2 . LEU A 1 36  ? -26.260 16.476  13.807  1.00 35.52 ? 36  LEU A CD2 1 
ATOM   256  N  N   . HIS A 1 37  ? -30.576 15.730  12.450  1.00 28.75 ? 37  HIS A N   1 
ATOM   257  C  CA  . HIS A 1 37  ? -31.883 15.120  12.440  1.00 28.65 ? 37  HIS A CA  1 
ATOM   258  C  C   . HIS A 1 37  ? -32.033 14.092  13.583  1.00 30.00 ? 37  HIS A C   1 
ATOM   259  O  O   . HIS A 1 37  ? -31.038 13.545  14.046  1.00 30.10 ? 37  HIS A O   1 
ATOM   260  C  CB  . HIS A 1 37  ? -31.965 14.298  11.161  1.00 27.70 ? 37  HIS A CB  1 
ATOM   261  C  CG  . HIS A 1 37  ? -31.794 15.135  9.939   1.00 31.91 ? 37  HIS A CG  1 
ATOM   262  N  ND1 . HIS A 1 37  ? -32.904 15.470  9.177   1.00 31.54 ? 37  HIS A ND1 1 
ATOM   263  C  CD2 . HIS A 1 37  ? -30.710 15.706  9.340   1.00 32.54 ? 37  HIS A CD2 1 
ATOM   264  C  CE1 . HIS A 1 37  ? -32.485 16.227  8.129   1.00 34.80 ? 37  HIS A CE1 1 
ATOM   265  N  NE2 . HIS A 1 37  ? -31.176 16.393  8.219   1.00 32.30 ? 37  HIS A NE2 1 
ATOM   266  N  N   . TRP A 1 38  ? -33.267 13.832  14.026  1.00 31.16 ? 38  TRP A N   1 
ATOM   267  C  CA  . TRP A 1 38  ? -33.561 12.788  15.002  1.00 29.21 ? 38  TRP A CA  1 
ATOM   268  C  C   . TRP A 1 38  ? -34.533 11.784  14.383  1.00 31.86 ? 38  TRP A C   1 
ATOM   269  O  O   . TRP A 1 38  ? -35.430 12.172  13.615  1.00 30.01 ? 38  TRP A O   1 
ATOM   270  C  CB  . TRP A 1 38  ? -34.187 13.435  16.231  1.00 31.72 ? 38  TRP A CB  1 
ATOM   271  C  CG  . TRP A 1 38  ? -33.235 14.313  17.007  1.00 34.69 ? 38  TRP A CG  1 
ATOM   272  C  CD1 . TRP A 1 38  ? -32.933 15.635  16.804  1.00 37.53 ? 38  TRP A CD1 1 
ATOM   273  C  CD2 . TRP A 1 38  ? -32.504 13.912  18.183  1.00 34.44 ? 38  TRP A CD2 1 
ATOM   274  N  NE1 . TRP A 1 38  ? -32.085 16.082  17.781  1.00 36.85 ? 38  TRP A NE1 1 
ATOM   275  C  CE2 . TRP A 1 38  ? -31.765 15.050  18.611  1.00 35.96 ? 38  TRP A CE2 1 
ATOM   276  C  CE3 . TRP A 1 38  ? -32.381 12.708  18.901  1.00 35.37 ? 38  TRP A CE3 1 
ATOM   277  C  CZ2 . TRP A 1 38  ? -30.956 15.013  19.757  1.00 38.69 ? 38  TRP A CZ2 1 
ATOM   278  C  CZ3 . TRP A 1 38  ? -31.601 12.685  20.043  1.00 35.79 ? 38  TRP A CZ3 1 
ATOM   279  C  CH2 . TRP A 1 38  ? -30.905 13.821  20.466  1.00 36.51 ? 38  TRP A CH2 1 
ATOM   280  N  N   . VAL A 1 39  ? -34.350 10.503  14.741  1.00 29.00 ? 39  VAL A N   1 
ATOM   281  C  CA  . VAL A 1 39  ? -34.962 9.365   14.062  1.00 30.29 ? 39  VAL A CA  1 
ATOM   282  C  C   . VAL A 1 39  ? -35.366 8.374   15.145  1.00 32.55 ? 39  VAL A C   1 
ATOM   283  O  O   . VAL A 1 39  ? -34.505 8.058   15.980  1.00 29.87 ? 39  VAL A O   1 
ATOM   284  C  CB  . VAL A 1 39  ? -33.978 8.720   13.054  1.00 32.70 ? 39  VAL A CB  1 
ATOM   285  C  CG1 . VAL A 1 39  ? -34.494 7.380   12.473  1.00 29.86 ? 39  VAL A CG1 1 
ATOM   286  C  CG2 . VAL A 1 39  ? -33.603 9.673   11.905  1.00 31.26 ? 39  VAL A CG2 1 
ATOM   287  N  N   . LYS A 1 40  ? -36.611 7.895   15.087  1.00 29.89 ? 40  LYS A N   1 
ATOM   288  C  CA  . LYS A 1 40  ? -37.109 6.879   16.023  1.00 27.90 ? 40  LYS A CA  1 
ATOM   289  C  C   . LYS A 1 40  ? -37.005 5.499   15.377  1.00 30.97 ? 40  LYS A C   1 
ATOM   290  O  O   . LYS A 1 40  ? -37.323 5.325   14.200  1.00 33.75 ? 40  LYS A O   1 
ATOM   291  C  CB  . LYS A 1 40  ? -38.586 7.175   16.311  1.00 28.98 ? 40  LYS A CB  1 
ATOM   292  C  CG  . LYS A 1 40  ? -39.249 6.255   17.371  1.00 29.55 ? 40  LYS A CG  1 
ATOM   293  C  CD  . LYS A 1 40  ? -40.726 6.601   17.528  1.00 32.86 ? 40  LYS A CD  1 
ATOM   294  C  CE  . LYS A 1 40  ? -41.452 5.690   18.501  1.00 33.27 ? 40  LYS A CE  1 
ATOM   295  N  NZ  . LYS A 1 40  ? -42.775 6.297   18.729  1.00 33.55 ? 40  LYS A NZ  1 
ATOM   296  N  N   . GLN A 1 41  ? -36.583 4.485   16.158  1.00 28.51 ? 41  GLN A N   1 
ATOM   297  C  CA  . GLN A 1 41  ? -36.526 3.145   15.600  1.00 29.16 ? 41  GLN A CA  1 
ATOM   298  C  C   . GLN A 1 41  ? -37.383 2.227   16.467  1.00 33.51 ? 41  GLN A C   1 
ATOM   299  O  O   . GLN A 1 41  ? -37.218 2.237   17.704  1.00 32.15 ? 41  GLN A O   1 
ATOM   300  C  CB  . GLN A 1 41  ? -35.073 2.701   15.655  1.00 27.44 ? 41  GLN A CB  1 
ATOM   301  C  CG  . GLN A 1 41  ? -34.896 1.231   15.281  1.00 29.35 ? 41  GLN A CG  1 
ATOM   302  C  CD  . GLN A 1 41  ? -33.441 0.813   15.380  1.00 32.69 ? 41  GLN A CD  1 
ATOM   303  O  OE1 . GLN A 1 41  ? -32.817 0.967   16.424  1.00 31.20 ? 41  GLN A OE1 1 
ATOM   304  N  NE2 . GLN A 1 41  ? -32.829 0.347   14.298  1.00 29.25 ? 41  GLN A NE2 1 
ATOM   305  N  N   . THR A 1 42  ? -38.270 1.442   15.824  1.00 32.45 ? 42  THR A N   1 
ATOM   306  C  CA  . THR A 1 42  ? -39.010 0.373   16.491  1.00 32.03 ? 42  THR A CA  1 
ATOM   307  C  C   . THR A 1 42  ? -38.960 -0.890  15.640  1.00 33.96 ? 42  THR A C   1 
ATOM   308  O  O   . THR A 1 42  ? -38.714 -0.821  14.416  1.00 34.35 ? 42  THR A O   1 
ATOM   309  C  CB  . THR A 1 42  ? -40.474 0.743   16.760  1.00 38.32 ? 42  THR A CB  1 
ATOM   310  O  OG1 . THR A 1 42  ? -41.090 1.056   15.521  1.00 37.52 ? 42  THR A OG1 1 
ATOM   311  C  CG2 . THR A 1 42  ? -40.679 1.990   17.599  1.00 36.96 ? 42  THR A CG2 1 
ATOM   312  N  N   . PRO A 1 43  ? -39.174 -2.090  16.246  1.00 37.90 ? 43  PRO A N   1 
ATOM   313  C  CA  . PRO A 1 43  ? -39.154 -3.343  15.461  1.00 40.40 ? 43  PRO A CA  1 
ATOM   314  C  C   . PRO A 1 43  ? -40.203 -3.376  14.318  1.00 50.23 ? 43  PRO A C   1 
ATOM   315  O  O   . PRO A 1 43  ? -39.912 -3.705  13.151  1.00 50.73 ? 43  PRO A O   1 
ATOM   316  C  CB  . PRO A 1 43  ? -39.378 -4.442  16.539  1.00 43.64 ? 43  PRO A CB  1 
ATOM   317  C  CG  . PRO A 1 43  ? -39.168 -3.763  17.888  1.00 38.76 ? 43  PRO A CG  1 
ATOM   318  C  CD  . PRO A 1 43  ? -39.339 -2.268  17.698  1.00 36.82 ? 43  PRO A CD  1 
ATOM   319  N  N   . GLY A 1 44  ? -41.418 -2.889  14.629  1.00 44.47 ? 44  GLY A N   1 
ATOM   320  C  CA  . GLY A 1 44  ? -42.565 -2.984  13.735  1.00 45.41 ? 44  GLY A CA  1 
ATOM   321  C  C   . GLY A 1 44  ? -42.574 -1.877  12.679  1.00 50.54 ? 44  GLY A C   1 
ATOM   322  O  O   . GLY A 1 44  ? -42.885 -2.148  11.529  1.00 56.45 ? 44  GLY A O   1 
ATOM   323  N  N   . GLN A 1 45  ? -42.217 -0.648  13.055  1.00 43.40 ? 45  GLN A N   1 
ATOM   324  C  CA  . GLN A 1 45  ? -42.327 0.468   12.118  1.00 42.30 ? 45  GLN A CA  1 
ATOM   325  C  C   . GLN A 1 45  ? -40.997 0.842   11.483  1.00 43.01 ? 45  GLN A C   1 
ATOM   326  O  O   . GLN A 1 45  ? -40.961 1.789   10.689  1.00 54.15 ? 45  GLN A O   1 
ATOM   327  C  CB  . GLN A 1 45  ? -43.120 1.639   12.693  1.00 45.24 ? 45  GLN A CB  1 
ATOM   328  C  CG  . GLN A 1 45  ? -44.630 1.379   12.627  0.70 53.00 ? 45  GLN A CG  1 
ATOM   329  C  CD  . GLN A 1 45  ? -45.458 2.339   13.455  0.70 54.38 ? 45  GLN A CD  1 
ATOM   330  O  OE1 . GLN A 1 45  ? -45.229 3.551   13.457  0.70 52.99 ? 45  GLN A OE1 1 
ATOM   331  N  NE2 . GLN A 1 45  ? -46.402 1.795   14.207  0.70 60.26 ? 45  GLN A NE2 1 
ATOM   332  N  N   . GLY A 1 46  ? -39.898 0.148   11.819  1.00 38.18 ? 46  GLY A N   1 
ATOM   333  C  CA  . GLY A 1 46  ? -38.639 0.559   11.202  1.00 35.64 ? 46  GLY A CA  1 
ATOM   334  C  C   . GLY A 1 46  ? -38.204 1.936   11.710  1.00 37.05 ? 46  GLY A C   1 
ATOM   335  O  O   . GLY A 1 46  ? -38.291 2.227   12.898  1.00 35.58 ? 46  GLY A O   1 
ATOM   336  N  N   . LEU A 1 47  ? -37.790 2.785   10.781  1.00 32.21 ? 47  LEU A N   1 
ATOM   337  C  CA  . LEU A 1 47  ? -37.277 4.111   11.189  1.00 31.29 ? 47  LEU A CA  1 
ATOM   338  C  C   . LEU A 1 47  ? -38.300 5.202   10.861  1.00 33.91 ? 47  LEU A C   1 
ATOM   339  O  O   . LEU A 1 47  ? -38.995 5.078   9.848   1.00 34.33 ? 47  LEU A O   1 
ATOM   340  C  CB  . LEU A 1 47  ? -35.930 4.346   10.517  1.00 29.57 ? 47  LEU A CB  1 
ATOM   341  C  CG  . LEU A 1 47  ? -34.817 3.342   10.810  1.00 30.68 ? 47  LEU A CG  1 
ATOM   342  C  CD1 . LEU A 1 47  ? -33.605 3.714   9.987   1.00 35.03 ? 47  LEU A CD1 1 
ATOM   343  C  CD2 . LEU A 1 47  ? -34.477 3.405   12.275  1.00 33.63 ? 47  LEU A CD2 1 
ATOM   344  N  N   . ASP A 1 48  ? -38.404 6.193   11.733  1.00 32.59 ? 48  ASP A N   1 
ATOM   345  C  CA  . ASP A 1 48  ? -39.297 7.318   11.517  1.00 37.30 ? 48  ASP A CA  1 
ATOM   346  C  C   . ASP A 1 48  ? -38.529 8.617   11.734  1.00 36.02 ? 48  ASP A C   1 
ATOM   347  O  O   . ASP A 1 48  ? -37.945 8.840   12.798  1.00 32.07 ? 48  ASP A O   1 
ATOM   348  C  CB  . ASP A 1 48  ? -40.452 7.321   12.497  1.00 44.42 ? 48  ASP A CB  1 
ATOM   349  C  CG  . ASP A 1 48  ? -41.808 7.044   11.871  1.00 60.68 ? 48  ASP A CG  1 
ATOM   350  O  OD1 . ASP A 1 48  ? -41.838 6.801   10.655  1.00 76.00 ? 48  ASP A OD1 1 
ATOM   351  O  OD2 . ASP A 1 48  ? -42.816 7.071   12.604  1.00 55.96 ? 48  ASP A OD2 1 
ATOM   352  N  N   . TRP A 1 49  ? -38.627 9.528   10.745  1.00 30.71 ? 49  TRP A N   1 
ATOM   353  C  CA  . TRP A 1 49  ? -37.997 10.838  10.854  1.00 30.44 ? 49  TRP A CA  1 
ATOM   354  C  C   . TRP A 1 49  ? -38.779 11.757  11.809  1.00 34.00 ? 49  TRP A C   1 
ATOM   355  O  O   . TRP A 1 49  ? -39.957 12.042  11.615  1.00 33.13 ? 49  TRP A O   1 
ATOM   356  C  CB  . TRP A 1 49  ? -37.833 11.466  9.449   1.00 29.45 ? 49  TRP A CB  1 
ATOM   357  C  CG  . TRP A 1 49  ? -37.180 12.829  9.494   1.00 33.82 ? 49  TRP A CG  1 
ATOM   358  C  CD1 . TRP A 1 49  ? -35.857 13.153  9.677   1.00 34.25 ? 49  TRP A CD1 1 
ATOM   359  C  CD2 . TRP A 1 49  ? -37.866 14.099  9.355   1.00 32.82 ? 49  TRP A CD2 1 
ATOM   360  N  NE1 . TRP A 1 49  ? -35.671 14.517  9.592   1.00 34.23 ? 49  TRP A NE1 1 
ATOM   361  C  CE2 . TRP A 1 49  ? -36.891 15.123  9.432   1.00 35.66 ? 49  TRP A CE2 1 
ATOM   362  C  CE3 . TRP A 1 49  ? -39.209 14.463  9.205   1.00 36.85 ? 49  TRP A CE3 1 
ATOM   363  C  CZ2 . TRP A 1 49  ? -37.214 16.485  9.308   1.00 37.89 ? 49  TRP A CZ2 1 
ATOM   364  C  CZ3 . TRP A 1 49  ? -39.527 15.814  9.129   1.00 39.04 ? 49  TRP A CZ3 1 
ATOM   365  C  CH2 . TRP A 1 49  ? -38.538 16.808  9.147   1.00 38.28 ? 49  TRP A CH2 1 
ATOM   366  N  N   . ILE A 1 50  ? -38.146 12.190  12.900  1.00 30.99 ? 50  ILE A N   1 
ATOM   367  C  CA  . ILE A 1 50  ? -38.867 13.026  13.851  1.00 30.56 ? 50  ILE A CA  1 
ATOM   368  C  C   . ILE A 1 50  ? -38.809 14.498  13.448  1.00 32.37 ? 50  ILE A C   1 
ATOM   369  O  O   . ILE A 1 50  ? -39.834 15.207  13.476  1.00 32.92 ? 50  ILE A O   1 
ATOM   370  C  CB  . ILE A 1 50  ? -38.246 12.840  15.244  1.00 31.89 ? 50  ILE A CB  1 
ATOM   371  C  CG1 . ILE A 1 50  ? -38.548 11.432  15.750  1.00 33.50 ? 50  ILE A CG1 1 
ATOM   372  C  CG2 . ILE A 1 50  ? -38.760 13.923  16.184  1.00 33.92 ? 50  ILE A CG2 1 
ATOM   373  C  CD1 . ILE A 1 50  ? -37.610 11.023  16.893  1.00 28.85 ? 50  ILE A CD1 1 
ATOM   374  N  N   . GLY A 1 51  ? -37.605 14.973  13.156  1.00 30.04 ? 51  GLY A N   1 
ATOM   375  C  CA  . GLY A 1 51  ? -37.478 16.372  12.785  1.00 32.79 ? 51  GLY A CA  1 
ATOM   376  C  C   . GLY A 1 51  ? -36.010 16.723  12.726  1.00 31.24 ? 51  GLY A C   1 
ATOM   377  O  O   . GLY A 1 51  ? -35.155 15.831  12.862  1.00 31.80 ? 51  GLY A O   1 
ATOM   378  N  N   . ALA A 1 52  ? -35.719 18.001  12.506  1.00 30.38 ? 52  ALA A N   1 
ATOM   379  C  CA  . ALA A 1 52  ? -34.347 18.423  12.312  1.00 30.67 ? 52  ALA A CA  1 
ATOM   380  C  C   . ALA A 1 52  ? -34.177 19.835  12.891  1.00 32.94 ? 52  ALA A C   1 
ATOM   381  O  O   . ALA A 1 52  ? -35.163 20.591  13.015  1.00 33.76 ? 52  ALA A O   1 
ATOM   382  C  CB  . ALA A 1 52  ? -33.982 18.422  10.827  1.00 33.84 ? 52  ALA A CB  1 
ATOM   383  N  N   . ILE A 1 53  ? -32.935 20.176  13.212  1.00 33.43 ? 53  ILE A N   1 
ATOM   384  C  CA  . ILE A 1 53  ? -32.584 21.489  13.747  1.00 33.33 ? 53  ILE A CA  1 
ATOM   385  C  C   . ILE A 1 53  ? -31.334 21.961  13.015  1.00 35.17 ? 53  ILE A C   1 
ATOM   386  O  O   . ILE A 1 53  ? -30.437 21.145  12.757  1.00 34.49 ? 53  ILE A O   1 
ATOM   387  C  CB  . ILE A 1 53  ? -32.405 21.468  15.298  1.00 36.79 ? 53  ILE A CB  1 
ATOM   388  C  CG1 . ILE A 1 53  ? -32.215 22.899  15.883  1.00 35.57 ? 53  ILE A CG1 1 
ATOM   389  C  CG2 . ILE A 1 53  ? -31.301 20.516  15.820  1.00 34.43 ? 53  ILE A CG2 1 
ATOM   390  C  CD1 . ILE A 1 53  ? -32.399 22.923  17.395  1.00 36.74 ? 53  ILE A CD1 1 
ATOM   391  N  N   . TYR A 1 54  ? -31.291 23.271  12.657  1.00 34.35 ? 54  TYR A N   1 
ATOM   392  C  CA  . TYR A 1 54  ? -30.049 23.859  12.214  1.00 35.39 ? 54  TYR A CA  1 
ATOM   393  C  C   . TYR A 1 54  ? -29.415 24.538  13.421  1.00 38.60 ? 54  TYR A C   1 
ATOM   394  O  O   . TYR A 1 54  ? -29.968 25.519  13.923  1.00 39.73 ? 54  TYR A O   1 
ATOM   395  C  CB  . TYR A 1 54  ? -30.268 24.914  11.119  1.00 37.03 ? 54  TYR A CB  1 
ATOM   396  C  CG  . TYR A 1 54  ? -28.933 25.419  10.595  1.00 34.15 ? 54  TYR A CG  1 
ATOM   397  C  CD1 . TYR A 1 54  ? -28.086 24.597  9.861   1.00 35.98 ? 54  TYR A CD1 1 
ATOM   398  C  CD2 . TYR A 1 54  ? -28.525 26.738  10.820  1.00 34.81 ? 54  TYR A CD2 1 
ATOM   399  C  CE1 . TYR A 1 54  ? -26.872 25.041  9.359   1.00 40.14 ? 54  TYR A CE1 1 
ATOM   400  C  CE2 . TYR A 1 54  ? -27.316 27.194  10.322  1.00 37.14 ? 54  TYR A CE2 1 
ATOM   401  C  CZ  . TYR A 1 54  ? -26.494 26.352  9.593   1.00 38.79 ? 54  TYR A CZ  1 
ATOM   402  O  OH  . TYR A 1 54  ? -25.293 26.819  9.123   1.00 39.05 ? 54  TYR A OH  1 
ATOM   403  N  N   . PRO A 1 55  ? -28.278 24.038  13.959  1.00 34.70 ? 55  PRO A N   1 
ATOM   404  C  CA  . PRO A 1 55  ? -27.813 24.540  15.269  1.00 35.57 ? 55  PRO A CA  1 
ATOM   405  C  C   . PRO A 1 55  ? -27.297 25.990  15.219  1.00 40.19 ? 55  PRO A C   1 
ATOM   406  O  O   . PRO A 1 55  ? -27.302 26.665  16.224  1.00 41.26 ? 55  PRO A O   1 
ATOM   407  C  CB  . PRO A 1 55  ? -26.681 23.564  15.604  1.00 34.79 ? 55  PRO A CB  1 
ATOM   408  C  CG  . PRO A 1 55  ? -27.071 22.268  14.868  1.00 33.33 ? 55  PRO A CG  1 
ATOM   409  C  CD  . PRO A 1 55  ? -27.506 22.862  13.512  1.00 34.10 ? 55  PRO A CD  1 
ATOM   410  N  N   . GLY A 1 56  ? -26.856 26.453  14.058  1.00 37.18 ? 56  GLY A N   1 
ATOM   411  C  CA  . GLY A 1 56  ? -26.349 27.808  13.902  1.00 45.16 ? 56  GLY A CA  1 
ATOM   412  C  C   . GLY A 1 56  ? -27.359 28.854  14.385  1.00 48.96 ? 56  GLY A C   1 
ATOM   413  O  O   . GLY A 1 56  ? -26.961 29.834  14.985  1.00 50.84 ? 56  GLY A O   1 
ATOM   414  N  N   . ASN A 1 57  ? -28.659 28.651  14.139  1.00 44.53 ? 57  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 57  ? -29.659 29.638  14.535  1.00 47.61 ? 57  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 57  ? -30.825 29.022  15.305  1.00 48.28 ? 57  ASN A C   1 
ATOM   417  O  O   . ASN A 1 57  ? -31.714 29.748  15.735  1.00 48.22 ? 57  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 57  ? -30.158 30.446  13.346  1.00 44.80 ? 57  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 57  ? -30.780 29.583  12.275  1.00 47.73 ? 57  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 57  ? -31.210 28.466  12.558  1.00 43.77 ? 57  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 57  ? -30.853 30.070  11.048  1.00 44.18 ? 57  ASN A ND2 1 
ATOM   422  N  N   . GLY A 1 58  ? -30.859 27.688  15.466  1.00 44.07 ? 58  GLY A N   1 
ATOM   423  C  CA  . GLY A 1 58  ? -31.956 27.060  16.200  1.00 42.63 ? 58  GLY A CA  1 
ATOM   424  C  C   . GLY A 1 58  ? -33.242 26.869  15.373  1.00 40.21 ? 58  GLY A C   1 
ATOM   425  O  O   . GLY A 1 58  ? -34.272 26.475  15.890  1.00 39.12 ? 58  GLY A O   1 
ATOM   426  N  N   . ASP A 1 59  ? -33.211 27.083  14.057  1.00 39.33 ? 59  ASP A N   1 
ATOM   427  C  CA  . ASP A 1 59  ? -34.422 26.817  13.297  1.00 39.27 ? 59  ASP A CA  1 
ATOM   428  C  C   . ASP A 1 59  ? -34.780 25.320  13.351  1.00 35.40 ? 59  ASP A C   1 
ATOM   429  O  O   . ASP A 1 59  ? -33.880 24.491  13.202  1.00 40.16 ? 59  ASP A O   1 
ATOM   430  C  CB  . ASP A 1 59  ? -34.154 27.192  11.854  1.00 37.89 ? 59  ASP A CB  1 
ATOM   431  C  CG  . ASP A 1 59  ? -34.226 28.692  11.572  1.00 51.57 ? 59  ASP A CG  1 
ATOM   432  O  OD1 . ASP A 1 59  ? -34.522 29.447  12.542  1.00 49.22 ? 59  ASP A OD1 1 
ATOM   433  O  OD2 . ASP A 1 59  ? -34.033 29.082  10.374  1.00 52.04 ? 59  ASP A OD2 1 
ATOM   434  N  N   . THR A 1 60  ? -36.070 24.967  13.515  1.00 37.20 ? 60  THR A N   1 
ATOM   435  C  CA  . THR A 1 60  ? -36.468 23.556  13.574  1.00 37.07 ? 60  THR A CA  1 
ATOM   436  C  C   . THR A 1 60  ? -37.507 23.267  12.494  1.00 45.97 ? 60  THR A C   1 
ATOM   437  O  O   . THR A 1 60  ? -38.205 24.191  12.054  1.00 46.86 ? 60  THR A O   1 
ATOM   438  C  CB  . THR A 1 60  ? -36.973 23.227  14.973  1.00 40.10 ? 60  THR A CB  1 
ATOM   439  O  OG1 . THR A 1 60  ? -37.930 24.234  15.284  1.00 42.14 ? 60  THR A OG1 1 
ATOM   440  C  CG2 . THR A 1 60  ? -35.836 23.308  15.958  1.00 38.94 ? 60  THR A CG2 1 
ATOM   441  N  N   . SER A 1 61  ? -37.561 22.010  12.018  1.00 36.91 ? 61  SER A N   1 
ATOM   442  C  CA  . SER A 1 61  ? -38.681 21.430  11.270  1.00 38.93 ? 61  SER A CA  1 
ATOM   443  C  C   . SER A 1 61  ? -39.111 20.126  11.922  1.00 37.96 ? 61  SER A C   1 
ATOM   444  O  O   . SER A 1 61  ? -38.254 19.366  12.368  1.00 37.76 ? 61  SER A O   1 
ATOM   445  C  CB  . SER A 1 61  ? -38.316 21.091  9.839   1.00 40.66 ? 61  SER A CB  1 
ATOM   446  O  OG  . SER A 1 61  ? -38.016 22.289  9.150   1.00 49.94 ? 61  SER A OG  1 
ATOM   447  N  N   . TYR A 1 62  ? -40.417 19.867  11.990  1.00 39.49 ? 62  TYR A N   1 
ATOM   448  C  CA  . TYR A 1 62  ? -40.872 18.639  12.639  1.00 36.98 ? 62  TYR A CA  1 
ATOM   449  C  C   . TYR A 1 62  ? -41.756 17.876  11.665  1.00 41.21 ? 62  TYR A C   1 
ATOM   450  O  O   . TYR A 1 62  ? -42.516 18.486  10.913  1.00 38.41 ? 62  TYR A O   1 
ATOM   451  C  CB  . TYR A 1 62  ? -41.786 18.947  13.820  1.00 37.78 ? 62  TYR A CB  1 
ATOM   452  C  CG  . TYR A 1 62  ? -41.031 19.624  14.959  1.00 40.84 ? 62  TYR A CG  1 
ATOM   453  C  CD1 . TYR A 1 62  ? -40.836 21.008  14.998  1.00 41.54 ? 62  TYR A CD1 1 
ATOM   454  C  CD2 . TYR A 1 62  ? -40.461 18.857  15.965  1.00 40.34 ? 62  TYR A CD2 1 
ATOM   455  C  CE1 . TYR A 1 62  ? -40.131 21.595  16.042  1.00 44.63 ? 62  TYR A CE1 1 
ATOM   456  C  CE2 . TYR A 1 62  ? -39.757 19.430  17.001  1.00 40.31 ? 62  TYR A CE2 1 
ATOM   457  C  CZ  . TYR A 1 62  ? -39.582 20.796  17.038  1.00 39.57 ? 62  TYR A CZ  1 
ATOM   458  O  OH  . TYR A 1 62  ? -38.857 21.324  18.065  1.00 39.07 ? 62  TYR A OH  1 
ATOM   459  N  N   . ASN A 1 63  ? -41.632 16.558  11.659  1.00 35.97 ? 63  ASN A N   1 
ATOM   460  C  CA  . ASN A 1 63  ? -42.658 15.687  11.126  1.00 36.99 ? 63  ASN A CA  1 
ATOM   461  C  C   . ASN A 1 63  ? -43.960 16.010  11.866  1.00 40.13 ? 63  ASN A C   1 
ATOM   462  O  O   . ASN A 1 63  ? -43.973 16.086  13.104  1.00 39.47 ? 63  ASN A O   1 
ATOM   463  C  CB  . ASN A 1 63  ? -42.301 14.240  11.465  1.00 37.30 ? 63  ASN A CB  1 
ATOM   464  C  CG  . ASN A 1 63  ? -43.116 13.226  10.714  1.00 40.55 ? 63  ASN A CG  1 
ATOM   465  O  OD1 . ASN A 1 63  ? -44.302 13.478  10.463  1.00 43.43 ? 63  ASN A OD1 1 
ATOM   466  N  ND2 . ASN A 1 63  ? -42.526 12.076  10.379  1.00 34.55 ? 63  ASN A ND2 1 
ATOM   467  N  N   . GLN A 1 64  ? -45.054 16.209  11.110  1.00 38.85 ? 64  GLN A N   1 
ATOM   468  C  CA  . GLN A 1 64  ? -46.356 16.549  11.662  1.00 43.85 ? 64  GLN A CA  1 
ATOM   469  C  C   . GLN A 1 64  ? -46.660 15.596  12.816  1.00 43.69 ? 64  GLN A C   1 
ATOM   470  O  O   . GLN A 1 64  ? -47.136 16.009  13.879  1.00 43.89 ? 64  GLN A O   1 
ATOM   471  C  CB  . GLN A 1 64  ? -47.464 16.506  10.595  1.00 47.45 ? 64  GLN A CB  1 
ATOM   472  C  CG  . GLN A 1 64  ? -48.781 17.164  11.005  1.00 55.65 ? 64  GLN A CG  1 
ATOM   473  N  N   . LYS A 1 65  ? -46.351 14.308  12.618  1.00 41.62 ? 65  LYS A N   1 
ATOM   474  C  CA  . LYS A 1 65  ? -46.744 13.346  13.643  1.00 43.56 ? 65  LYS A CA  1 
ATOM   475  C  C   . LYS A 1 65  ? -45.999 13.533  14.960  1.00 42.72 ? 65  LYS A C   1 
ATOM   476  O  O   . LYS A 1 65  ? -46.461 13.033  15.980  1.00 44.51 ? 65  LYS A O   1 
ATOM   477  C  CB  . LYS A 1 65  ? -46.844 11.914  13.126  1.00 47.42 ? 65  LYS A CB  1 
ATOM   478  C  CG  . LYS A 1 65  ? -45.547 11.309  12.679  1.00 56.59 ? 65  LYS A CG  1 
ATOM   479  C  CD  . LYS A 1 65  ? -45.654 9.868   12.179  1.00 65.93 ? 65  LYS A CD  1 
ATOM   480  C  CE  . LYS A 1 65  ? -46.209 8.996   13.256  1.00 67.87 ? 65  LYS A CE  1 
ATOM   481  N  NZ  . LYS A 1 65  ? -45.611 7.659   13.281  1.00 63.85 ? 65  LYS A NZ  1 
ATOM   482  N  N   . PHE A 1 66  ? -44.881 14.257  14.979  1.00 38.77 ? 66  PHE A N   1 
ATOM   483  C  CA  . PHE A 1 66  ? -44.154 14.360  16.240  1.00 37.55 ? 66  PHE A CA  1 
ATOM   484  C  C   . PHE A 1 66  ? -44.214 15.772  16.805  1.00 39.05 ? 66  PHE A C   1 
ATOM   485  O  O   . PHE A 1 66  ? -43.503 16.048  17.765  1.00 42.92 ? 66  PHE A O   1 
ATOM   486  C  CB  . PHE A 1 66  ? -42.654 14.027  16.055  1.00 33.26 ? 66  PHE A CB  1 
ATOM   487  C  CG  . PHE A 1 66  ? -42.480 12.521  15.864  1.00 37.28 ? 66  PHE A CG  1 
ATOM   488  C  CD1 . PHE A 1 66  ? -42.483 11.663  16.973  1.00 36.86 ? 66  PHE A CD1 1 
ATOM   489  C  CD2 . PHE A 1 66  ? -42.368 11.953  14.600  1.00 34.84 ? 66  PHE A CD2 1 
ATOM   490  C  CE1 . PHE A 1 66  ? -42.357 10.285  16.800  1.00 36.65 ? 66  PHE A CE1 1 
ATOM   491  C  CE2 . PHE A 1 66  ? -42.215 10.581  14.437  1.00 37.60 ? 66  PHE A CE2 1 
ATOM   492  C  CZ  . PHE A 1 66  ? -42.225 9.739   15.544  1.00 39.65 ? 66  PHE A CZ  1 
ATOM   493  N  N   . LYS A 1 67  ? -45.023 16.662  16.203  1.00 43.53 ? 67  LYS A N   1 
ATOM   494  C  CA  . LYS A 1 67  ? -44.943 18.086  16.507  1.00 44.27 ? 67  LYS A CA  1 
ATOM   495  C  C   . LYS A 1 67  ? -45.195 18.352  17.994  1.00 43.88 ? 67  LYS A C   1 
ATOM   496  O  O   . LYS A 1 67  ? -44.570 19.253  18.550  1.00 56.01 ? 67  LYS A O   1 
ATOM   497  C  CB  . LYS A 1 67  ? -45.751 19.007  15.571  1.00 46.54 ? 67  LYS A CB  1 
ATOM   498  C  CG  . LYS A 1 67  ? -47.250 18.769  15.537  1.00 54.67 ? 67  LYS A CG  1 
ATOM   499  N  N   . ASP A 1 68  ? -46.060 17.566  18.653  1.00 44.65 ? 68  ASP A N   1 
ATOM   500  C  CA  . ASP A 1 68  ? -46.313 17.856  20.064  1.00 49.54 ? 68  ASP A CA  1 
ATOM   501  C  C   . ASP A 1 68  ? -45.428 17.013  20.980  1.00 47.91 ? 68  ASP A C   1 
ATOM   502  O  O   . ASP A 1 68  ? -45.034 17.470  22.048  1.00 52.44 ? 68  ASP A O   1 
ATOM   503  C  CB  . ASP A 1 68  ? -47.791 17.815  20.414  1.00 55.35 ? 68  ASP A CB  1 
ATOM   504  C  CG  . ASP A 1 68  ? -48.603 18.826  19.609  1.00 65.20 ? 68  ASP A CG  1 
ATOM   505  O  OD1 . ASP A 1 68  ? -48.172 20.006  19.553  1.00 63.79 ? 68  ASP A OD1 1 
ATOM   506  O  OD2 . ASP A 1 68  ? -49.602 18.410  18.986  1.00 63.33 ? 68  ASP A OD2 1 
ATOM   507  N  N   . LYS A 1 69  ? -45.082 15.821  20.512  1.00 43.09 ? 69  LYS A N   1 
ATOM   508  C  CA  . LYS A 1 69  ? -44.241 14.901  21.265  1.00 39.95 ? 69  LYS A CA  1 
ATOM   509  C  C   . LYS A 1 69  ? -42.823 15.437  21.428  1.00 42.21 ? 69  LYS A C   1 
ATOM   510  O  O   . LYS A 1 69  ? -42.284 15.308  22.518  1.00 41.99 ? 69  LYS A O   1 
ATOM   511  C  CB  . LYS A 1 69  ? -44.187 13.531  20.579  1.00 39.99 ? 69  LYS A CB  1 
ATOM   512  C  CG  . LYS A 1 69  ? -43.351 12.440  21.285  1.00 39.80 ? 69  LYS A CG  1 
ATOM   513  C  CD  . LYS A 1 69  ? -43.883 12.225  22.702  1.00 36.22 ? 69  LYS A CD  1 
ATOM   514  C  CE  . LYS A 1 69  ? -45.273 11.597  22.720  1.00 37.12 ? 69  LYS A CE  1 
ATOM   515  N  NZ  . LYS A 1 69  ? -45.659 11.192  24.106  1.00 39.78 ? 69  LYS A NZ  1 
ATOM   516  N  N   . ALA A 1 70  ? -42.192 15.960  20.356  1.00 36.50 ? 70  ALA A N   1 
ATOM   517  C  CA  . ALA A 1 70  ? -40.775 16.293  20.443  1.00 40.65 ? 70  ALA A CA  1 
ATOM   518  C  C   . ALA A 1 70  ? -40.495 17.796  20.431  1.00 41.69 ? 70  ALA A C   1 
ATOM   519  O  O   . ALA A 1 70  ? -41.155 18.531  19.708  1.00 45.00 ? 70  ALA A O   1 
ATOM   520  C  CB  . ALA A 1 70  ? -40.064 15.644  19.289  1.00 37.22 ? 70  ALA A CB  1 
ATOM   521  N  N   . THR A 1 71  ? -39.447 18.244  21.148  1.00 43.19 ? 71  THR A N   1 
ATOM   522  C  CA  . THR A 1 71  ? -38.944 19.620  21.037  1.00 40.53 ? 71  THR A CA  1 
ATOM   523  C  C   . THR A 1 71  ? -37.428 19.552  20.837  1.00 39.84 ? 71  THR A C   1 
ATOM   524  O  O   . THR A 1 71  ? -36.726 18.915  21.646  1.00 40.02 ? 71  THR A O   1 
ATOM   525  C  CB  . THR A 1 71  ? -39.259 20.457  22.298  1.00 40.85 ? 71  THR A CB  1 
ATOM   526  O  OG1 . THR A 1 71  ? -40.661 20.319  22.535  1.00 44.37 ? 71  THR A OG1 1 
ATOM   527  C  CG2 . THR A 1 71  ? -38.784 21.897  22.156  1.00 39.70 ? 71  THR A CG2 1 
ATOM   528  N  N   . LEU A 1 72  ? -36.941 20.121  19.726  1.00 37.47 ? 72  LEU A N   1 
ATOM   529  C  CA  . LEU A 1 72  ? -35.510 20.090  19.462  1.00 36.15 ? 72  LEU A CA  1 
ATOM   530  C  C   . LEU A 1 72  ? -34.855 21.401  19.876  1.00 39.17 ? 72  LEU A C   1 
ATOM   531  O  O   . LEU A 1 72  ? -35.376 22.441  19.516  1.00 37.26 ? 72  LEU A O   1 
ATOM   532  C  CB  . LEU A 1 72  ? -35.337 19.849  17.965  1.00 33.64 ? 72  LEU A CB  1 
ATOM   533  C  CG  . LEU A 1 72  ? -35.943 18.556  17.421  1.00 34.39 ? 72  LEU A CG  1 
ATOM   534  C  CD1 . LEU A 1 72  ? -35.443 18.397  15.968  1.00 36.21 ? 72  LEU A CD1 1 
ATOM   535  C  CD2 . LEU A 1 72  ? -35.595 17.334  18.316  1.00 33.76 ? 72  LEU A CD2 1 
ATOM   536  N  N   . THR A 1 73  ? -33.771 21.365  20.663  1.00 35.01 ? 73  THR A N   1 
ATOM   537  C  CA  . THR A 1 73  ? -33.000 22.576  20.907  1.00 37.42 ? 73  THR A CA  1 
ATOM   538  C  C   . THR A 1 73  ? -31.525 22.304  20.596  1.00 37.20 ? 73  THR A C   1 
ATOM   539  O  O   . THR A 1 73  ? -31.110 21.170  20.406  1.00 36.16 ? 73  THR A O   1 
ATOM   540  C  CB  . THR A 1 73  ? -33.210 23.034  22.358  1.00 40.61 ? 73  THR A CB  1 
ATOM   541  O  OG1 . THR A 1 73  ? -32.889 21.914  23.182  1.00 40.22 ? 73  THR A OG1 1 
ATOM   542  C  CG2 . THR A 1 73  ? -34.638 23.439  22.670  1.00 41.63 ? 73  THR A CG2 1 
ATOM   543  N  N   . ALA A 1 74  ? -30.701 23.347  20.609  1.00 37.57 ? 74  ALA A N   1 
ATOM   544  C  CA  . ALA A 1 74  ? -29.264 23.210  20.422  1.00 39.52 ? 74  ALA A CA  1 
ATOM   545  C  C   . ALA A 1 74  ? -28.534 24.165  21.357  1.00 48.74 ? 74  ALA A C   1 
ATOM   546  O  O   . ALA A 1 74  ? -28.972 25.304  21.568  1.00 47.40 ? 74  ALA A O   1 
ATOM   547  C  CB  . ALA A 1 74  ? -28.916 23.571  19.001  1.00 38.22 ? 74  ALA A CB  1 
ATOM   548  N  N   . ASP A 1 75  ? -27.396 23.707  21.878  1.00 42.02 ? 75  ASP A N   1 
ATOM   549  C  CA  . ASP A 1 75  ? -26.592 24.558  22.742  1.00 45.36 ? 75  ASP A CA  1 
ATOM   550  C  C   . ASP A 1 75  ? -25.195 24.720  22.163  1.00 40.41 ? 75  ASP A C   1 
ATOM   551  O  O   . ASP A 1 75  ? -24.327 23.860  22.324  1.00 38.10 ? 75  ASP A O   1 
ATOM   552  C  CB  . ASP A 1 75  ? -26.601 24.051  24.170  1.00 48.43 ? 75  ASP A CB  1 
ATOM   553  C  CG  . ASP A 1 75  ? -25.675 24.791  25.128  1.00 58.13 ? 75  ASP A CG  1 
ATOM   554  O  OD1 . ASP A 1 75  ? -24.924 25.667  24.672  1.00 60.41 ? 75  ASP A OD1 1 
ATOM   555  O  OD2 . ASP A 1 75  ? -25.689 24.445  26.314  1.00 59.71 ? 75  ASP A OD2 1 
ATOM   556  N  N   . LYS A 1 76  ? -24.988 25.847  21.462  1.00 43.26 ? 76  LYS A N   1 
ATOM   557  C  CA  . LYS A 1 76  ? -23.710 26.093  20.808  1.00 45.12 ? 76  LYS A CA  1 
ATOM   558  C  C   . LYS A 1 76  ? -22.540 26.086  21.793  1.00 43.45 ? 76  LYS A C   1 
ATOM   559  O  O   . LYS A 1 76  ? -21.448 25.699  21.422  1.00 45.83 ? 76  LYS A O   1 
ATOM   560  C  CB  . LYS A 1 76  ? -23.728 27.339  19.917  1.00 45.28 ? 76  LYS A CB  1 
ATOM   561  C  CG  . LYS A 1 76  ? -24.485 27.113  18.644  1.00 51.33 ? 76  LYS A CG  1 
ATOM   562  C  CD  . LYS A 1 76  ? -24.430 28.345  17.733  1.00 56.02 ? 76  LYS A CD  1 
ATOM   563  C  CE  . LYS A 1 76  ? -25.313 29.429  18.295  1.00 59.04 ? 76  LYS A CE  1 
ATOM   564  N  NZ  . LYS A 1 76  ? -25.326 30.605  17.422  1.00 62.31 ? 76  LYS A NZ  1 
ATOM   565  N  N   . SER A 1 77  ? -22.755 26.465  23.055  1.00 46.08 ? 77  SER A N   1 
ATOM   566  C  CA  . SER A 1 77  ? -21.608 26.608  23.941  1.00 50.60 ? 77  SER A CA  1 
ATOM   567  C  C   . SER A 1 77  ? -21.020 25.243  24.281  1.00 52.02 ? 77  SER A C   1 
ATOM   568  O  O   . SER A 1 77  ? -19.829 25.145  24.560  1.00 55.51 ? 77  SER A O   1 
ATOM   569  C  CB  . SER A 1 77  ? -21.916 27.426  25.188  1.00 52.67 ? 77  SER A CB  1 
ATOM   570  O  OG  . SER A 1 77  ? -22.967 26.838  25.947  1.00 51.58 ? 77  SER A OG  1 
ATOM   571  N  N   . SER A 1 78  ? -21.851 24.193  24.216  1.00 45.99 ? 78  SER A N   1 
ATOM   572  C  CA  . SER A 1 78  ? -21.395 22.847  24.524  1.00 44.42 ? 78  SER A CA  1 
ATOM   573  C  C   . SER A 1 78  ? -21.418 21.934  23.289  1.00 43.47 ? 78  SER A C   1 
ATOM   574  O  O   . SER A 1 78  ? -21.115 20.742  23.420  1.00 41.74 ? 78  SER A O   1 
ATOM   575  C  CB  . SER A 1 78  ? -22.215 22.254  25.641  1.00 46.43 ? 78  SER A CB  1 
ATOM   576  O  OG  . SER A 1 78  ? -23.569 22.090  25.222  1.00 42.60 ? 78  SER A OG  1 
ATOM   577  N  N   . SER A 1 79  ? -21.693 22.499  22.095  1.00 40.29 ? 79  SER A N   1 
ATOM   578  C  CA  . SER A 1 79  ? -21.805 21.716  20.876  1.00 37.77 ? 79  SER A CA  1 
ATOM   579  C  C   . SER A 1 79  ? -22.763 20.522  21.053  1.00 35.44 ? 79  SER A C   1 
ATOM   580  O  O   . SER A 1 79  ? -22.466 19.452  20.513  1.00 36.21 ? 79  SER A O   1 
ATOM   581  C  CB  . SER A 1 79  ? -20.456 21.210  20.388  1.00 39.24 ? 79  SER A CB  1 
ATOM   582  O  OG  . SER A 1 79  ? -19.568 22.288  20.141  1.00 45.75 ? 79  SER A OG  1 
ATOM   583  N  N   . THR A 1 80  ? -23.905 20.692  21.749  1.00 33.39 ? 80  THR A N   1 
ATOM   584  C  CA  . THR A 1 80  ? -24.812 19.566  22.047  1.00 33.83 ? 80  THR A CA  1 
ATOM   585  C  C   . THR A 1 80  ? -26.220 19.929  21.565  1.00 36.13 ? 80  THR A C   1 
ATOM   586  O  O   . THR A 1 80  ? -26.677 21.061  21.786  1.00 37.58 ? 80  THR A O   1 
ATOM   587  C  CB  . THR A 1 80  ? -24.844 19.384  23.577  1.00 38.33 ? 80  THR A CB  1 
ATOM   588  O  OG1 . THR A 1 80  ? -23.540 18.983  23.964  1.00 35.91 ? 80  THR A OG1 1 
ATOM   589  C  CG2 . THR A 1 80  ? -25.745 18.241  24.004  1.00 37.15 ? 80  THR A CG2 1 
ATOM   590  N  N   . ALA A 1 81  ? -26.886 18.988  20.886  1.00 33.21 ? 81  ALA A N   1 
ATOM   591  C  CA  . ALA A 1 81  ? -28.287 19.073  20.517  1.00 35.88 ? 81  ALA A CA  1 
ATOM   592  C  C   . ALA A 1 81  ? -29.082 18.234  21.500  1.00 33.85 ? 81  ALA A C   1 
ATOM   593  O  O   . ALA A 1 81  ? -28.573 17.254  22.071  1.00 36.41 ? 81  ALA A O   1 
ATOM   594  C  CB  . ALA A 1 81  ? -28.470 18.533  19.080  1.00 35.14 ? 81  ALA A CB  1 
ATOM   595  N  N   . TYR A 1 82  ? -30.336 18.618  21.696  1.00 34.56 ? 82  TYR A N   1 
ATOM   596  C  CA  . TYR A 1 82  ? -31.176 17.918  22.648  1.00 36.05 ? 82  TYR A CA  1 
ATOM   597  C  C   . TYR A 1 82  ? -32.554 17.720  22.049  1.00 36.67 ? 82  TYR A C   1 
ATOM   598  O  O   . TYR A 1 82  ? -33.018 18.535  21.235  1.00 36.55 ? 82  TYR A O   1 
ATOM   599  C  CB  . TYR A 1 82  ? -31.461 18.816  23.845  1.00 39.05 ? 82  TYR A CB  1 
ATOM   600  C  CG  . TYR A 1 82  ? -30.237 19.122  24.676  1.00 42.80 ? 82  TYR A CG  1 
ATOM   601  C  CD1 . TYR A 1 82  ? -29.810 18.204  25.605  1.00 41.46 ? 82  TYR A CD1 1 
ATOM   602  C  CD2 . TYR A 1 82  ? -29.475 20.268  24.465  1.00 41.59 ? 82  TYR A CD2 1 
ATOM   603  C  CE1 . TYR A 1 82  ? -28.696 18.433  26.390  1.00 46.15 ? 82  TYR A CE1 1 
ATOM   604  C  CE2 . TYR A 1 82  ? -28.318 20.488  25.199  1.00 42.74 ? 82  TYR A CE2 1 
ATOM   605  C  CZ  . TYR A 1 82  ? -27.956 19.584  26.191  1.00 49.89 ? 82  TYR A CZ  1 
ATOM   606  O  OH  . TYR A 1 82  ? -26.864 19.716  26.989  1.00 45.85 ? 82  TYR A OH  1 
ATOM   607  N  N   . MET A 1 83  ? -33.178 16.592  22.394  1.00 31.42 ? 83  MET A N   1 
ATOM   608  C  CA  . MET A 1 83  ? -34.561 16.383  22.022  1.00 33.06 ? 83  MET A CA  1 
ATOM   609  C  C   . MET A 1 83  ? -35.309 16.057  23.299  1.00 35.54 ? 83  MET A C   1 
ATOM   610  O  O   . MET A 1 83  ? -34.949 15.120  24.022  1.00 34.93 ? 83  MET A O   1 
ATOM   611  C  CB  . MET A 1 83  ? -34.745 15.183  21.082  1.00 32.79 ? 83  MET A CB  1 
ATOM   612  C  CG  . MET A 1 83  ? -36.191 14.830  20.879  1.00 33.17 ? 83  MET A CG  1 
ATOM   613  S  SD  . MET A 1 83  ? -36.461 13.731  19.480  1.00 37.59 ? 83  MET A SD  1 
ATOM   614  C  CE  . MET A 1 83  ? -35.731 12.223  20.159  1.00 38.97 ? 83  MET A CE  1 
ATOM   615  N  N   . GLN A 1 84  ? -36.338 16.850  23.565  1.00 37.24 ? 84  GLN A N   1 
ATOM   616  C  CA  . GLN A 1 84  ? -37.182 16.547  24.694  1.00 33.61 ? 84  GLN A CA  1 
ATOM   617  C  C   . GLN A 1 84  ? -38.370 15.722  24.219  1.00 37.27 ? 84  GLN A C   1 
ATOM   618  O  O   . GLN A 1 84  ? -38.994 16.074  23.230  1.00 40.21 ? 84  GLN A O   1 
ATOM   619  C  CB  . GLN A 1 84  ? -37.692 17.817  25.361  1.00 37.02 ? 84  GLN A CB  1 
ATOM   620  C  CG  . GLN A 1 84  ? -38.566 17.478  26.576  1.00 47.05 ? 84  GLN A CG  1 
ATOM   621  C  CD  . GLN A 1 84  ? -39.697 18.461  26.850  1.00 57.86 ? 84  GLN A CD  1 
ATOM   622  O  OE1 . GLN A 1 84  ? -40.565 18.746  26.010  1.00 61.80 ? 84  GLN A OE1 1 
ATOM   623  N  NE2 . GLN A 1 84  ? -39.716 18.965  28.072  1.00 59.95 ? 84  GLN A NE2 1 
ATOM   624  N  N   . LEU A 1 85  ? -38.683 14.629  24.920  1.00 33.09 ? 85  LEU A N   1 
ATOM   625  C  CA  . LEU A 1 85  ? -39.917 13.918  24.629  1.00 37.09 ? 85  LEU A CA  1 
ATOM   626  C  C   . LEU A 1 85  ? -40.855 14.123  25.815  1.00 39.88 ? 85  LEU A C   1 
ATOM   627  O  O   . LEU A 1 85  ? -40.459 13.880  26.944  1.00 42.97 ? 85  LEU A O   1 
ATOM   628  C  CB  . LEU A 1 85  ? -39.622 12.433  24.396  1.00 38.46 ? 85  LEU A CB  1 
ATOM   629  C  CG  . LEU A 1 85  ? -38.706 12.125  23.209  1.00 36.93 ? 85  LEU A CG  1 
ATOM   630  C  CD1 . LEU A 1 85  ? -38.371 10.657  23.361  1.00 36.61 ? 85  LEU A CD1 1 
ATOM   631  C  CD2 . LEU A 1 85  ? -39.357 12.337  21.816  1.00 37.20 ? 85  LEU A CD2 1 
ATOM   632  N  N   . SER A 1 86  ? -42.085 14.583  25.551  1.00 40.05 ? 86  SER A N   1 
ATOM   633  C  CA  . SER A 1 86  ? -42.980 14.931  26.642  1.00 41.75 ? 86  SER A CA  1 
ATOM   634  C  C   . SER A 1 86  ? -44.150 13.941  26.697  1.00 42.33 ? 86  SER A C   1 
ATOM   635  O  O   . SER A 1 86  ? -44.433 13.251  25.712  1.00 42.12 ? 86  SER A O   1 
ATOM   636  C  CB  . SER A 1 86  ? -43.455 16.370  26.456  1.00 44.05 ? 86  SER A CB  1 
ATOM   637  O  OG  . SER A 1 86  ? -44.076 16.495  25.180  1.00 46.83 ? 86  SER A OG  1 
ATOM   638  N  N   . ASN A 1 87  ? -44.832 13.888  27.855  1.00 42.39 ? 87  ASN A N   1 
ATOM   639  C  CA  . ASN A 1 87  ? -46.037 13.077  28.026  1.00 43.59 ? 87  ASN A CA  1 
ATOM   640  C  C   . ASN A 1 87  ? -45.773 11.645  27.578  1.00 43.48 ? 87  ASN A C   1 
ATOM   641  O  O   . ASN A 1 87  ? -46.515 11.090  26.743  1.00 41.80 ? 87  ASN A O   1 
ATOM   642  C  CB  . ASN A 1 87  ? -47.210 13.693  27.264  1.00 48.61 ? 87  ASN A CB  1 
ATOM   643  C  CG  . ASN A 1 87  ? -47.554 15.053  27.818  1.00 55.75 ? 87  ASN A CG  1 
ATOM   644  O  OD1 . ASN A 1 87  ? -47.831 15.167  29.015  1.00 55.74 ? 87  ASN A OD1 1 
ATOM   645  N  ND2 . ASN A 1 87  ? -47.493 16.094  26.999  1.00 51.90 ? 87  ASN A ND2 1 
ATOM   646  N  N   . LEU A 1 88  ? -44.696 11.050  28.128  1.00 40.42 ? 88  LEU A N   1 
ATOM   647  C  CA  . LEU A 1 88  ? -44.281 9.729   27.687  1.00 40.76 ? 88  LEU A CA  1 
ATOM   648  C  C   . LEU A 1 88  ? -45.413 8.715   27.865  1.00 43.33 ? 88  LEU A C   1 
ATOM   649  O  O   . LEU A 1 88  ? -46.071 8.663   28.921  1.00 42.81 ? 88  LEU A O   1 
ATOM   650  C  CB  . LEU A 1 88  ? -43.050 9.333   28.507  1.00 40.14 ? 88  LEU A CB  1 
ATOM   651  C  CG  . LEU A 1 88  ? -41.764 10.067  28.120  1.00 39.97 ? 88  LEU A CG  1 
ATOM   652  C  CD1 . LEU A 1 88  ? -40.662 9.810   29.107  1.00 37.24 ? 88  LEU A CD1 1 
ATOM   653  C  CD2 . LEU A 1 88  ? -41.307 9.703   26.722  1.00 38.09 ? 88  LEU A CD2 1 
ATOM   654  N  N   . THR A 1 89  ? -45.563 7.833   26.871  1.00 41.11 ? 89  THR A N   1 
ATOM   655  C  CA  . THR A 1 89  ? -46.439 6.660   26.954  1.00 42.36 ? 89  THR A CA  1 
ATOM   656  C  C   . THR A 1 89  ? -45.664 5.439   26.457  1.00 41.56 ? 89  THR A C   1 
ATOM   657  O  O   . THR A 1 89  ? -44.551 5.584   25.962  1.00 39.90 ? 89  THR A O   1 
ATOM   658  C  CB  . THR A 1 89  ? -47.694 6.863   26.102  1.00 42.11 ? 89  THR A CB  1 
ATOM   659  O  OG1 . THR A 1 89  ? -47.215 6.739   24.759  1.00 45.74 ? 89  THR A OG1 1 
ATOM   660  C  CG2 . THR A 1 89  ? -48.337 8.213   26.350  1.00 45.62 ? 89  THR A CG2 1 
ATOM   661  N  N   . SER A 1 90  ? -46.255 4.238   26.532  1.00 41.71 ? 90  SER A N   1 
ATOM   662  C  CA  . SER A 1 90  ? -45.611 3.018   26.072  1.00 41.97 ? 90  SER A CA  1 
ATOM   663  C  C   . SER A 1 90  ? -45.221 3.122   24.597  1.00 40.03 ? 90  SER A C   1 
ATOM   664  O  O   . SER A 1 90  ? -44.299 2.443   24.141  1.00 37.82 ? 90  SER A O   1 
ATOM   665  C  CB  . SER A 1 90  ? -46.542 1.843   26.255  1.00 47.29 ? 90  SER A CB  1 
ATOM   666  O  OG  . SER A 1 90  ? -46.794 1.721   27.643  1.00 48.59 ? 90  SER A OG  1 
ATOM   667  N  N   . GLU A 1 91  ? -45.962 3.943   23.853  1.00 39.21 ? 91  GLU A N   1 
ATOM   668  C  CA  . GLU A 1 91  ? -45.751 4.098   22.416  1.00 43.04 ? 91  GLU A CA  1 
ATOM   669  C  C   . GLU A 1 91  ? -44.433 4.823   22.105  1.00 38.06 ? 91  GLU A C   1 
ATOM   670  O  O   . GLU A 1 91  ? -44.005 4.828   20.930  1.00 38.34 ? 91  GLU A O   1 
ATOM   671  C  CB  . GLU A 1 91  ? -46.995 4.739   21.781  1.00 41.19 ? 91  GLU A CB  1 
ATOM   672  C  CG  . GLU A 1 91  ? -48.159 3.749   21.715  1.00 43.02 ? 91  GLU A CG  1 
ATOM   673  C  CD  . GLU A 1 91  ? -48.632 3.167   23.059  0.50 51.72 ? 91  GLU A CD  1 
ATOM   674  O  OE1 . GLU A 1 91  ? -49.259 3.910   23.858  0.50 52.32 ? 91  GLU A OE1 1 
ATOM   675  O  OE2 . GLU A 1 91  ? -48.345 1.967   23.360  0.50 56.62 ? 91  GLU A OE2 1 
ATOM   676  N  N   . ASP A 1 92  ? -43.826 5.446   23.136  1.00 34.31 ? 92  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? -42.551 6.152   23.023  1.00 32.80 ? 92  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? -41.340 5.227   23.284  1.00 35.51 ? 92  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? -40.194 5.589   22.966  1.00 34.47 ? 92  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? -42.544 7.393   23.899  1.00 32.82 ? 92  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? -43.662 8.396   23.575  1.00 36.81 ? 92  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? -43.860 8.700   22.352  1.00 40.66 ? 92  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? -44.317 8.896   24.548  1.00 41.53 ? 92  ASP A OD2 1 
ATOM   684  N  N   . SER A 1 93  ? -41.549 4.037   23.848  1.00 34.31 ? 93  SER A N   1 
ATOM   685  C  CA  . SER A 1 93  ? -40.424 3.118   24.027  1.00 33.83 ? 93  SER A CA  1 
ATOM   686  C  C   . SER A 1 93  ? -39.826 2.788   22.655  1.00 34.82 ? 93  SER A C   1 
ATOM   687  O  O   . SER A 1 93  ? -40.532 2.253   21.785  1.00 34.62 ? 93  SER A O   1 
ATOM   688  C  CB  . SER A 1 93  ? -40.842 1.851   24.695  1.00 36.46 ? 93  SER A CB  1 
ATOM   689  O  OG  . SER A 1 93  ? -41.276 2.136   26.016  1.00 36.66 ? 93  SER A OG  1 
ATOM   690  N  N   . ALA A 1 94  ? -38.534 3.077   22.480  1.00 32.84 ? 94  ALA A N   1 
ATOM   691  C  CA  . ALA A 1 94  ? -37.924 2.987   21.161  1.00 31.60 ? 94  ALA A CA  1 
ATOM   692  C  C   . ALA A 1 94  ? -36.440 3.338   21.281  1.00 31.81 ? 94  ALA A C   1 
ATOM   693  O  O   . ALA A 1 94  ? -35.995 3.815   22.319  1.00 33.17 ? 94  ALA A O   1 
ATOM   694  C  CB  . ALA A 1 94  ? -38.622 3.968   20.191  1.00 29.72 ? 94  ALA A CB  1 
ATOM   695  N  N   . VAL A 1 95  ? -35.684 3.187   20.181  1.00 28.15 ? 95  VAL A N   1 
ATOM   696  C  CA  . VAL A 1 95  ? -34.344 3.748   20.153  1.00 29.10 ? 95  VAL A CA  1 
ATOM   697  C  C   . VAL A 1 95  ? -34.401 5.038   19.328  1.00 31.23 ? 95  VAL A C   1 
ATOM   698  O  O   . VAL A 1 95  ? -35.050 5.068   18.269  1.00 29.63 ? 95  VAL A O   1 
ATOM   699  C  CB  . VAL A 1 95  ? -33.329 2.759   19.573  1.00 29.04 ? 95  VAL A CB  1 
ATOM   700  C  CG1 . VAL A 1 95  ? -31.950 3.418   19.529  1.00 28.02 ? 95  VAL A CG1 1 
ATOM   701  C  CG2 . VAL A 1 95  ? -33.277 1.444   20.408  1.00 28.63 ? 95  VAL A CG2 1 
ATOM   702  N  N   . TYR A 1 96  ? -33.753 6.094   19.811  1.00 28.95 ? 96  TYR A N   1 
ATOM   703  C  CA  . TYR A 1 96  ? -33.743 7.416   19.162  1.00 29.23 ? 96  TYR A CA  1 
ATOM   704  C  C   . TYR A 1 96  ? -32.312 7.769   18.754  1.00 32.13 ? 96  TYR A C   1 
ATOM   705  O  O   . TYR A 1 96  ? -31.395 7.793   19.579  1.00 28.81 ? 96  TYR A O   1 
ATOM   706  C  CB  . TYR A 1 96  ? -34.300 8.505   20.082  1.00 31.14 ? 96  TYR A CB  1 
ATOM   707  C  CG  . TYR A 1 96  ? -35.758 8.275   20.434  1.00 29.03 ? 96  TYR A CG  1 
ATOM   708  C  CD1 . TYR A 1 96  ? -36.135 7.457   21.513  1.00 29.17 ? 96  TYR A CD1 1 
ATOM   709  C  CD2 . TYR A 1 96  ? -36.764 8.828   19.644  1.00 28.97 ? 96  TYR A CD2 1 
ATOM   710  C  CE1 . TYR A 1 96  ? -37.472 7.214   21.785  1.00 31.93 ? 96  TYR A CE1 1 
ATOM   711  C  CE2 . TYR A 1 96  ? -38.106 8.641   19.953  1.00 29.23 ? 96  TYR A CE2 1 
ATOM   712  C  CZ  . TYR A 1 96  ? -38.457 7.798   20.995  1.00 31.26 ? 96  TYR A CZ  1 
ATOM   713  O  OH  . TYR A 1 96  ? -39.776 7.602   21.212  1.00 32.23 ? 96  TYR A OH  1 
ATOM   714  N  N   . TYR A 1 97  ? -32.076 8.082   17.465  1.00 28.25 ? 97  TYR A N   1 
ATOM   715  C  CA  . TYR A 1 97  ? -30.727 8.410   17.015  1.00 28.63 ? 97  TYR A CA  1 
ATOM   716  C  C   . TYR A 1 97  ? -30.684 9.892   16.624  1.00 29.03 ? 97  TYR A C   1 
ATOM   717  O  O   . TYR A 1 97  ? -31.688 10.410  16.133  1.00 31.69 ? 97  TYR A O   1 
ATOM   718  C  CB  . TYR A 1 97  ? -30.537 7.712   15.646  1.00 29.36 ? 97  TYR A CB  1 
ATOM   719  C  CG  . TYR A 1 97  ? -30.484 6.193   15.822  1.00 27.59 ? 97  TYR A CG  1 
ATOM   720  C  CD1 . TYR A 1 97  ? -29.287 5.556   16.166  1.00 30.18 ? 97  TYR A CD1 1 
ATOM   721  C  CD2 . TYR A 1 97  ? -31.610 5.389   15.668  1.00 29.99 ? 97  TYR A CD2 1 
ATOM   722  C  CE1 . TYR A 1 97  ? -29.210 4.184   16.435  1.00 31.43 ? 97  TYR A CE1 1 
ATOM   723  C  CE2 . TYR A 1 97  ? -31.542 4.012   15.920  1.00 33.01 ? 97  TYR A CE2 1 
ATOM   724  C  CZ  . TYR A 1 97  ? -30.348 3.398   16.301  1.00 31.01 ? 97  TYR A CZ  1 
ATOM   725  O  OH  . TYR A 1 97  ? -30.300 2.031   16.543  1.00 29.45 ? 97  TYR A OH  1 
ATOM   726  N  N   . CYS A 1 98  ? -29.551 10.577  16.841  1.00 29.52 ? 98  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 98  ? -29.302 11.820  16.100  1.00 31.83 ? 98  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 98  ? -28.337 11.535  14.954  1.00 34.02 ? 98  CYS A C   1 
ATOM   729  O  O   . CYS A 1 98  ? -27.533 10.608  15.031  1.00 31.05 ? 98  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 98  ? -28.795 12.916  17.033  1.00 35.65 ? 98  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 98  ? -27.215 12.358  17.712  1.00 41.54 ? 98  CYS A SG  1 
ATOM   732  N  N   . ALA A 1 99  ? -28.472 12.245  13.804  1.00 28.94 ? 99  ALA A N   1 
ATOM   733  C  CA  . ALA A 1 99  ? -27.647 11.936  12.658  1.00 26.91 ? 99  ALA A CA  1 
ATOM   734  C  C   . ALA A 1 99  ? -27.594 13.150  11.724  1.00 27.56 ? 99  ALA A C   1 
ATOM   735  O  O   . ALA A 1 99  ? -28.520 13.986  11.721  1.00 31.03 ? 99  ALA A O   1 
ATOM   736  C  CB  . ALA A 1 99  ? -28.278 10.788  11.911  1.00 26.51 ? 99  ALA A CB  1 
ATOM   737  N  N   . ARG A 1 100 ? -26.548 13.185  10.894  1.00 29.34 ? 100 ARG A N   1 
ATOM   738  C  CA  . ARG A 1 100 ? -26.582 13.994  9.676   1.00 28.85 ? 100 ARG A CA  1 
ATOM   739  C  C   . ARG A 1 100 ? -27.054 13.046  8.588   1.00 29.79 ? 100 ARG A C   1 
ATOM   740  O  O   . ARG A 1 100 ? -26.407 11.999  8.372   1.00 28.53 ? 100 ARG A O   1 
ATOM   741  C  CB  . ARG A 1 100 ? -25.220 14.621  9.353   1.00 30.16 ? 100 ARG A CB  1 
ATOM   742  C  CG  . ARG A 1 100 ? -24.758 15.447  10.545  1.00 33.42 ? 100 ARG A CG  1 
ATOM   743  C  CD  . ARG A 1 100 ? -23.501 16.205  10.077  1.00 30.63 ? 100 ARG A CD  1 
ATOM   744  N  NE  . ARG A 1 100 ? -22.473 15.331  9.489   1.00 31.85 ? 100 ARG A NE  1 
ATOM   745  C  CZ  . ARG A 1 100 ? -21.168 15.447  9.624   1.00 37.42 ? 100 ARG A CZ  1 
ATOM   746  N  NH1 . ARG A 1 100 ? -20.673 16.304  10.528  1.00 40.95 ? 100 ARG A NH1 1 
ATOM   747  N  NH2 . ARG A 1 100 ? -20.341 14.701  8.899   1.00 32.90 ? 100 ARG A NH2 1 
ATOM   748  N  N   . LEU A 1 101 ? -28.215 13.377  7.987   1.00 29.39 ? 101 LEU A N   1 
ATOM   749  C  CA  . LEU A 1 101 ? -28.892 12.433  7.095   1.00 32.35 ? 101 LEU A CA  1 
ATOM   750  C  C   . LEU A 1 101 ? -28.540 12.664  5.648   1.00 30.83 ? 101 LEU A C   1 
ATOM   751  O  O   . LEU A 1 101 ? -28.683 11.723  4.865   1.00 31.79 ? 101 LEU A O   1 
ATOM   752  C  CB  . LEU A 1 101 ? -30.408 12.318  7.220   1.00 32.43 ? 101 LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 101 ? -30.838 11.741  8.579   1.00 30.46 ? 101 LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 101 ? -32.405 11.735  8.631   1.00 30.32 ? 101 LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 101 ? -30.272 10.313  8.807   1.00 32.95 ? 101 LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 102 ? -28.082 13.860  5.292   1.00 32.54 ? 102 ASP A N   1 
ATOM   757  C  CA  . ASP A 1 102 ? -27.815 13.983  3.855   1.00 33.21 ? 102 ASP A CA  1 
ATOM   758  C  C   . ASP A 1 102 ? -26.657 13.052  3.506   1.00 35.69 ? 102 ASP A C   1 
ATOM   759  O  O   . ASP A 1 102 ? -25.715 12.916  4.275   1.00 33.23 ? 102 ASP A O   1 
ATOM   760  C  CB  . ASP A 1 102 ? -27.437 15.426  3.505   1.00 38.90 ? 102 ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 102 ? -28.590 16.402  3.698   1.00 45.60 ? 102 ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 102 ? -29.754 16.016  3.391   1.00 47.54 ? 102 ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 102 ? -28.312 17.524  4.105   1.00 51.78 ? 102 ASP A OD2 1 
ATOM   764  N  N   . TRP A 1 103 ? -26.730 12.353  2.377   1.00 30.51 ? 103 TRP A N   1 
ATOM   765  C  CA  . TRP A 1 103 ? -25.797 11.241  2.207   1.00 30.59 ? 103 TRP A CA  1 
ATOM   766  C  C   . TRP A 1 103 ? -24.344 11.705  2.252   1.00 33.75 ? 103 TRP A C   1 
ATOM   767  O  O   . TRP A 1 103 ? -23.457 10.965  2.695   1.00 30.95 ? 103 TRP A O   1 
ATOM   768  C  CB  . TRP A 1 103 ? -26.081 10.430  0.916   1.00 29.33 ? 103 TRP A CB  1 
ATOM   769  C  CG  . TRP A 1 103 ? -25.990 11.146  -0.423  1.00 34.82 ? 103 TRP A CG  1 
ATOM   770  C  CD1 . TRP A 1 103 ? -27.035 11.649  -1.169  1.00 38.76 ? 103 TRP A CD1 1 
ATOM   771  C  CD2 . TRP A 1 103 ? -24.792 11.435  -1.185  1.00 32.63 ? 103 TRP A CD2 1 
ATOM   772  N  NE1 . TRP A 1 103 ? -26.580 12.191  -2.352  1.00 38.08 ? 103 TRP A NE1 1 
ATOM   773  C  CE2 . TRP A 1 103 ? -25.204 12.103  -2.367  1.00 36.37 ? 103 TRP A CE2 1 
ATOM   774  C  CE3 . TRP A 1 103 ? -23.436 11.145  -1.004  1.00 30.86 ? 103 TRP A CE3 1 
ATOM   775  C  CZ2 . TRP A 1 103 ? -24.276 12.517  -3.321  1.00 38.65 ? 103 TRP A CZ2 1 
ATOM   776  C  CZ3 . TRP A 1 103 ? -22.516 11.587  -1.933  1.00 35.35 ? 103 TRP A CZ3 1 
ATOM   777  C  CH2 . TRP A 1 103 ? -22.941 12.235  -3.084  1.00 36.33 ? 103 TRP A CH2 1 
ATOM   778  N  N   . TYR A 1 104 ? -24.072 12.854  1.608   1.00 30.11 ? 104 TYR A N   1 
ATOM   779  C  CA  . TYR A 1 104 ? -22.709 13.346  1.566   1.00 28.42 ? 104 TYR A CA  1 
ATOM   780  C  C   . TYR A 1 104 ? -22.136 13.713  2.930   1.00 29.83 ? 104 TYR A C   1 
ATOM   781  O  O   . TYR A 1 104 ? -20.926 13.827  2.981   1.00 33.21 ? 104 TYR A O   1 
ATOM   782  C  CB  . TYR A 1 104 ? -22.512 14.457  0.499   1.00 31.98 ? 104 TYR A CB  1 
ATOM   783  C  CG  . TYR A 1 104 ? -23.731 15.367  0.421   1.00 31.48 ? 104 TYR A CG  1 
ATOM   784  C  CD1 . TYR A 1 104 ? -23.931 16.379  1.351   1.00 31.35 ? 104 TYR A CD1 1 
ATOM   785  C  CD2 . TYR A 1 104 ? -24.708 15.156  -0.536  1.00 31.95 ? 104 TYR A CD2 1 
ATOM   786  C  CE1 . TYR A 1 104 ? -25.056 17.195  1.313   1.00 31.38 ? 104 TYR A CE1 1 
ATOM   787  C  CE2 . TYR A 1 104 ? -25.801 16.008  -0.631  1.00 35.61 ? 104 TYR A CE2 1 
ATOM   788  C  CZ  . TYR A 1 104 ? -25.971 17.025  0.290   1.00 37.61 ? 104 TYR A CZ  1 
ATOM   789  O  OH  . TYR A 1 104 ? -27.018 17.897  0.244   1.00 38.15 ? 104 TYR A OH  1 
ATOM   790  N  N   . PHE A 1 105 ? -22.965 13.903  3.971   1.00 29.14 ? 105 PHE A N   1 
ATOM   791  C  CA  . PHE A 1 105 ? -22.464 14.225  5.319   1.00 29.44 ? 105 PHE A CA  1 
ATOM   792  C  C   . PHE A 1 105 ? -22.759 13.096  6.337   1.00 28.99 ? 105 PHE A C   1 
ATOM   793  O  O   . PHE A 1 105 ? -22.681 13.332  7.557   1.00 29.26 ? 105 PHE A O   1 
ATOM   794  C  CB  . PHE A 1 105 ? -23.014 15.549  5.846   1.00 30.15 ? 105 PHE A CB  1 
ATOM   795  C  CG  . PHE A 1 105 ? -22.708 16.750  4.946   1.00 29.89 ? 105 PHE A CG  1 
ATOM   796  C  CD1 . PHE A 1 105 ? -21.525 16.809  4.213   1.00 29.87 ? 105 PHE A CD1 1 
ATOM   797  C  CD2 . PHE A 1 105 ? -23.632 17.787  4.822   1.00 29.78 ? 105 PHE A CD2 1 
ATOM   798  C  CE1 . PHE A 1 105 ? -21.243 17.924  3.408   1.00 31.33 ? 105 PHE A CE1 1 
ATOM   799  C  CE2 . PHE A 1 105 ? -23.344 18.919  4.001   1.00 29.13 ? 105 PHE A CE2 1 
ATOM   800  C  CZ  . PHE A 1 105 ? -22.187 18.928  3.272   1.00 32.03 ? 105 PHE A CZ  1 
ATOM   801  N  N   . ASP A 1 106 ? -23.113 11.904  5.842   1.00 29.98 ? 106 ASP A N   1 
ATOM   802  C  CA  . ASP A 1 106 ? -23.694 10.820  6.646   1.00 27.97 ? 106 ASP A CA  1 
ATOM   803  C  C   . ASP A 1 106 ? -22.892 10.576  7.906   1.00 27.76 ? 106 ASP A C   1 
ATOM   804  O  O   . ASP A 1 106 ? -21.674 10.358  7.845   1.00 31.44 ? 106 ASP A O   1 
ATOM   805  C  CB  . ASP A 1 106 ? -23.663 9.486   5.910   1.00 26.77 ? 106 ASP A CB  1 
ATOM   806  C  CG  . ASP A 1 106 ? -24.323 8.325   6.681   1.00 26.68 ? 106 ASP A CG  1 
ATOM   807  O  OD1 . ASP A 1 106 ? -25.543 8.430   6.859   1.00 32.22 ? 106 ASP A OD1 1 
ATOM   808  O  OD2 . ASP A 1 106 ? -23.576 7.371   7.066   1.00 31.14 ? 106 ASP A OD2 1 
ATOM   809  N  N   . LEU A 1 107 ? -23.579 10.681  9.062   1.00 29.38 ? 107 LEU A N   1 
ATOM   810  C  CA  . LEU A 1 107 ? -22.932 10.474  10.355  1.00 29.14 ? 107 LEU A CA  1 
ATOM   811  C  C   . LEU A 1 107 ? -24.055 10.133  11.319  1.00 27.91 ? 107 LEU A C   1 
ATOM   812  O  O   . LEU A 1 107 ? -25.023 10.890  11.403  1.00 28.42 ? 107 LEU A O   1 
ATOM   813  C  CB  . LEU A 1 107 ? -22.276 11.793  10.779  1.00 30.14 ? 107 LEU A CB  1 
ATOM   814  C  CG  . LEU A 1 107 ? -21.627 11.780  12.181  1.00 33.23 ? 107 LEU A CG  1 
ATOM   815  C  CD1 . LEU A 1 107 ? -20.474 10.809  12.062  1.00 38.47 ? 107 LEU A CD1 1 
ATOM   816  C  CD2 . LEU A 1 107 ? -21.117 13.189  12.465  1.00 34.82 ? 107 LEU A CD2 1 
ATOM   817  N  N   . TRP A 1 108 ? -23.900 9.075   12.166  1.00 29.92 ? 108 TRP A N   1 
ATOM   818  C  CA  . TRP A 1 108 ? -24.980 8.687   13.078  1.00 27.73 ? 108 TRP A CA  1 
ATOM   819  C  C   . TRP A 1 108 ? -24.425 8.540   14.498  1.00 26.53 ? 108 TRP A C   1 
ATOM   820  O  O   . TRP A 1 108 ? -23.318 8.041   14.674  1.00 29.37 ? 108 TRP A O   1 
ATOM   821  C  CB  . TRP A 1 108 ? -25.568 7.315   12.708  1.00 27.83 ? 108 TRP A CB  1 
ATOM   822  C  CG  . TRP A 1 108 ? -26.342 7.317   11.415  1.00 30.12 ? 108 TRP A CG  1 
ATOM   823  C  CD1 . TRP A 1 108 ? -25.843 7.467   10.152  1.00 29.87 ? 108 TRP A CD1 1 
ATOM   824  C  CD2 . TRP A 1 108 ? -27.767 7.142   11.276  1.00 30.01 ? 108 TRP A CD2 1 
ATOM   825  N  NE1 . TRP A 1 108 ? -26.867 7.358   9.248   1.00 28.39 ? 108 TRP A NE1 1 
ATOM   826  C  CE2 . TRP A 1 108 ? -28.054 7.185   9.888   1.00 30.01 ? 108 TRP A CE2 1 
ATOM   827  C  CE3 . TRP A 1 108 ? -28.827 6.937   12.163  1.00 30.14 ? 108 TRP A CE3 1 
ATOM   828  C  CZ2 . TRP A 1 108 ? -29.344 7.058   9.374   1.00 32.26 ? 108 TRP A CZ2 1 
ATOM   829  C  CZ3 . TRP A 1 108 ? -30.100 6.802   11.663  1.00 29.92 ? 108 TRP A CZ3 1 
ATOM   830  C  CH2 . TRP A 1 108 ? -30.358 6.847   10.280  1.00 32.45 ? 108 TRP A CH2 1 
ATOM   831  N  N   . GLY A 1 109 ? -25.217 8.989   15.436  1.00 29.27 ? 109 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 109 ? -24.965 8.593   16.803  1.00 26.14 ? 109 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 109 ? -25.331 7.126   17.046  1.00 30.42 ? 109 GLY A C   1 
ATOM   834  O  O   . GLY A 1 109 ? -25.913 6.462   16.210  1.00 29.00 ? 109 GLY A O   1 
ATOM   835  N  N   . ALA A 1 110 ? -25.009 6.588   18.242  1.00 29.66 ? 110 ALA A N   1 
ATOM   836  C  CA  . ALA A 1 110 ? -25.241 5.150   18.440  1.00 30.53 ? 110 ALA A CA  1 
ATOM   837  C  C   . ALA A 1 110 ? -26.664 4.863   18.910  1.00 29.07 ? 110 ALA A C   1 
ATOM   838  O  O   . ALA A 1 110 ? -27.060 3.674   19.017  1.00 31.94 ? 110 ALA A O   1 
ATOM   839  C  CB  . ALA A 1 110 ? -24.205 4.702   19.472  1.00 30.18 ? 110 ALA A CB  1 
ATOM   840  N  N   . GLY A 1 111 ? -27.421 5.931   19.246  1.00 27.84 ? 111 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 111 ? -28.825 5.853   19.647  1.00 27.89 ? 111 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 111 ? -28.987 5.686   21.181  1.00 30.79 ? 111 GLY A C   1 
ATOM   843  O  O   . GLY A 1 111 ? -28.143 5.072   21.854  1.00 35.27 ? 111 GLY A O   1 
ATOM   844  N  N   . THR A 1 112 ? -30.056 6.294   21.708  1.00 30.71 ? 112 THR A N   1 
ATOM   845  C  CA  . THR A 1 112 ? -30.453 6.186   23.108  1.00 28.35 ? 112 THR A CA  1 
ATOM   846  C  C   . THR A 1 112 ? -31.718 5.347   23.137  1.00 30.93 ? 112 THR A C   1 
ATOM   847  O  O   . THR A 1 112 ? -32.738 5.742   22.577  1.00 30.59 ? 112 THR A O   1 
ATOM   848  C  CB  . THR A 1 112 ? -30.684 7.558   23.725  1.00 30.63 ? 112 THR A CB  1 
ATOM   849  O  OG1 . THR A 1 112 ? -29.472 8.295   23.641  1.00 31.90 ? 112 THR A OG1 1 
ATOM   850  C  CG2 . THR A 1 112 ? -31.139 7.454   25.187  1.00 31.92 ? 112 THR A CG2 1 
ATOM   851  N  N   . THR A 1 113 ? -31.678 4.250   23.928  1.00 28.38 ? 113 THR A N   1 
ATOM   852  C  CA  . THR A 1 113 ? -32.890 3.459   24.104  1.00 29.91 ? 113 THR A CA  1 
ATOM   853  C  C   . THR A 1 113 ? -33.721 4.139   25.190  1.00 37.39 ? 113 THR A C   1 
ATOM   854  O  O   . THR A 1 113 ? -33.232 4.327   26.300  1.00 36.54 ? 113 THR A O   1 
ATOM   855  C  CB  . THR A 1 113 ? -32.535 2.060   24.610  1.00 31.62 ? 113 THR A CB  1 
ATOM   856  O  OG1 . THR A 1 113 ? -31.776 1.391   23.618  1.00 30.75 ? 113 THR A OG1 1 
ATOM   857  C  CG2 . THR A 1 113 ? -33.760 1.200   24.912  1.00 30.96 ? 113 THR A CG2 1 
ATOM   858  N  N   . VAL A 1 114 ? -34.975 4.480   24.889  1.00 32.83 ? 114 VAL A N   1 
ATOM   859  C  CA  . VAL A 1 114 ? -35.816 5.088   25.910  1.00 32.02 ? 114 VAL A CA  1 
ATOM   860  C  C   . VAL A 1 114 ? -36.851 4.030   26.256  1.00 35.96 ? 114 VAL A C   1 
ATOM   861  O  O   . VAL A 1 114 ? -37.559 3.550   25.360  1.00 31.91 ? 114 VAL A O   1 
ATOM   862  C  CB  . VAL A 1 114 ? -36.541 6.333   25.385  1.00 32.27 ? 114 VAL A CB  1 
ATOM   863  C  CG1 . VAL A 1 114 ? -37.583 6.800   26.402  1.00 33.77 ? 114 VAL A CG1 1 
ATOM   864  C  CG2 . VAL A 1 114 ? -35.539 7.435   24.996  1.00 30.63 ? 114 VAL A CG2 1 
ATOM   865  N  N   . THR A 1 115 ? -36.888 3.638   27.545  1.00 33.78 ? 115 THR A N   1 
ATOM   866  C  CA  . THR A 1 115 ? -37.765 2.543   27.964  1.00 36.71 ? 115 THR A CA  1 
ATOM   867  C  C   . THR A 1 115 ? -38.808 3.128   28.913  1.00 37.30 ? 115 THR A C   1 
ATOM   868  O  O   . THR A 1 115 ? -38.445 3.529   30.027  1.00 34.18 ? 115 THR A O   1 
ATOM   869  C  CB  . THR A 1 115 ? -36.963 1.484   28.721  1.00 36.36 ? 115 THR A CB  1 
ATOM   870  O  OG1 . THR A 1 115 ? -35.991 0.990   27.805  1.00 35.26 ? 115 THR A OG1 1 
ATOM   871  C  CG2 . THR A 1 115 ? -37.823 0.316   29.192  1.00 35.11 ? 115 THR A CG2 1 
ATOM   872  N  N   . VAL A 1 116 ? -40.062 3.227   28.441  1.00 33.05 ? 116 VAL A N   1 
ATOM   873  C  CA  . VAL A 1 116 ? -41.116 3.761   29.284  1.00 34.99 ? 116 VAL A CA  1 
ATOM   874  C  C   . VAL A 1 116 ? -41.689 2.572   30.070  1.00 35.90 ? 116 VAL A C   1 
ATOM   875  O  O   . VAL A 1 116 ? -42.223 1.619   29.499  1.00 34.40 ? 116 VAL A O   1 
ATOM   876  C  CB  . VAL A 1 116 ? -42.182 4.477   28.455  1.00 37.42 ? 116 VAL A CB  1 
ATOM   877  C  CG1 . VAL A 1 116 ? -43.300 4.990   29.370  1.00 39.98 ? 116 VAL A CG1 1 
ATOM   878  C  CG2 . VAL A 1 116 ? -41.564 5.637   27.668  1.00 34.91 ? 116 VAL A CG2 1 
ATOM   879  N  N   . SER A 1 117 ? -41.534 2.603   31.404  1.00 36.60 ? 117 SER A N   1 
ATOM   880  C  CA  . SER A 1 117 ? -41.646 1.375   32.160  1.00 36.78 ? 117 SER A CA  1 
ATOM   881  C  C   . SER A 1 117 ? -42.670 1.584   33.275  1.00 42.61 ? 117 SER A C   1 
ATOM   882  O  O   . SER A 1 117 ? -42.545 2.531   34.057  1.00 38.84 ? 117 SER A O   1 
ATOM   883  C  CB  . SER A 1 117 ? -40.265 1.064   32.707  1.00 37.36 ? 117 SER A CB  1 
ATOM   884  O  OG  . SER A 1 117 ? -40.273 0.029   33.678  1.00 38.52 ? 117 SER A OG  1 
ATOM   885  N  N   . ALA A 1 118 ? -43.724 0.753   33.289  1.00 45.83 ? 118 ALA A N   1 
ATOM   886  C  CA  . ALA A 1 118 ? -44.665 0.708   34.404  1.00 43.68 ? 118 ALA A CA  1 
ATOM   887  C  C   . ALA A 1 118 ? -45.297 -0.676  34.438  1.00 48.84 ? 118 ALA A C   1 
ATOM   888  O  O   . ALA A 1 118 ? -46.010 -1.046  33.513  1.00 47.03 ? 118 ALA A O   1 
ATOM   889  C  CB  . ALA A 1 118 ? -45.709 1.802   34.242  1.00 44.58 ? 118 ALA A CB  1 
ATOM   890  N  N   . ALA A 1 119 ? -44.980 -1.456  35.477  1.00 48.29 ? 119 ALA A N   1 
ATOM   891  C  CA  . ALA A 1 119 ? -45.424 -2.840  35.606  1.00 56.39 ? 119 ALA A CA  1 
ATOM   892  C  C   . ALA A 1 119 ? -46.937 -2.935  35.855  1.00 62.24 ? 119 ALA A C   1 
ATOM   893  O  O   . ALA A 1 119 ? -47.566 -1.986  36.350  1.00 61.50 ? 119 ALA A O   1 
ATOM   894  C  CB  . ALA A 1 119 ? -44.647 -3.526  36.718  1.00 60.60 ? 119 ALA A CB  1 
ATOM   895  N  N   . GLY A 1 120 ? -47.502 -4.102  35.505  0.70 58.90 ? 120 GLY A N   1 
ATOM   896  C  CA  . GLY A 1 120 ? -48.916 -4.406  35.680  0.70 70.45 ? 120 GLY A CA  1 
ATOM   897  C  C   . GLY A 1 120 ? -49.168 -5.159  36.978  0.70 72.88 ? 120 GLY A C   1 
ATOM   898  O  O   . GLY A 1 120 ? -49.412 -4.463  37.989  0.70 70.60 ? 120 GLY A O   1 
ATOM   899  N  N   . SER A 1 134 ? -50.530 11.375  2.591   1.00 60.45 ? 134 SER A N   1 
ATOM   900  C  CA  . SER A 1 134 ? -49.694 11.618  1.385   1.00 56.66 ? 134 SER A CA  1 
ATOM   901  C  C   . SER A 1 134 ? -48.188 11.658  1.697   1.00 50.81 ? 134 SER A C   1 
ATOM   902  O  O   . SER A 1 134 ? -47.372 12.056  0.866   1.00 50.18 ? 134 SER A O   1 
ATOM   903  C  CB  . SER A 1 134 ? -50.156 12.841  0.623   1.00 63.42 ? 134 SER A CB  1 
ATOM   904  O  OG  . SER A 1 134 ? -49.722 14.030  1.267   1.00 63.02 ? 134 SER A OG  1 
ATOM   905  N  N   . ASP A 1 135 ? -47.775 11.169  2.870   1.00 49.95 ? 135 ASP A N   1 
ATOM   906  C  CA  . ASP A 1 135 ? -46.363 10.862  3.045   1.00 46.99 ? 135 ASP A CA  1 
ATOM   907  C  C   . ASP A 1 135 ? -46.019 9.696   2.133   1.00 42.88 ? 135 ASP A C   1 
ATOM   908  O  O   . ASP A 1 135 ? -46.853 8.815   1.937   1.00 43.91 ? 135 ASP A O   1 
ATOM   909  C  CB  . ASP A 1 135 ? -46.096 10.367  4.459   1.00 45.27 ? 135 ASP A CB  1 
ATOM   910  C  CG  . ASP A 1 135 ? -46.204 11.441  5.535   1.00 57.47 ? 135 ASP A CG  1 
ATOM   911  O  OD1 . ASP A 1 135 ? -46.383 12.634  5.151   1.00 60.33 ? 135 ASP A OD1 1 
ATOM   912  O  OD2 . ASP A 1 135 ? -46.108 11.084  6.761   1.00 55.35 ? 135 ASP A OD2 1 
ATOM   913  N  N   . ILE A 1 136 ? -44.783 9.655   1.628   1.00 38.28 ? 136 ILE A N   1 
ATOM   914  C  CA  . ILE A 1 136 ? -44.369 8.542   0.795   1.00 35.95 ? 136 ILE A CA  1 
ATOM   915  C  C   . ILE A 1 136 ? -44.151 7.325   1.690   1.00 40.43 ? 136 ILE A C   1 
ATOM   916  O  O   . ILE A 1 136 ? -43.410 7.418   2.672   1.00 41.63 ? 136 ILE A O   1 
ATOM   917  C  CB  . ILE A 1 136 ? -43.123 8.941   -0.018  1.00 36.56 ? 136 ILE A CB  1 
ATOM   918  C  CG1 . ILE A 1 136 ? -43.416 10.159  -0.857  1.00 40.55 ? 136 ILE A CG1 1 
ATOM   919  C  CG2 . ILE A 1 136 ? -42.719 7.788   -0.939  1.00 40.53 ? 136 ILE A CG2 1 
ATOM   920  C  CD1 . ILE A 1 136 ? -42.265 10.554  -1.757  1.00 38.76 ? 136 ILE A CD1 1 
ATOM   921  N  N   . VAL A 1 137 ? -44.837 6.213   1.386   1.00 38.01 ? 137 VAL A N   1 
ATOM   922  C  CA  . VAL A 1 137 ? -44.681 4.979   2.154   1.00 37.62 ? 137 VAL A CA  1 
ATOM   923  C  C   . VAL A 1 137 ? -43.676 4.097   1.419   1.00 38.61 ? 137 VAL A C   1 
ATOM   924  O  O   . VAL A 1 137 ? -43.782 3.933   0.199   1.00 35.91 ? 137 VAL A O   1 
ATOM   925  C  CB  . VAL A 1 137 ? -46.019 4.248   2.323   1.00 39.61 ? 137 VAL A CB  1 
ATOM   926  C  CG1 . VAL A 1 137 ? -45.858 2.906   3.046   1.00 42.31 ? 137 VAL A CG1 1 
ATOM   927  C  CG2 . VAL A 1 137 ? -47.016 5.168   3.023   1.00 42.81 ? 137 VAL A CG2 1 
ATOM   928  N  N   . LEU A 1 138 ? -42.694 3.564   2.168   1.00 34.43 ? 138 LEU A N   1 
ATOM   929  C  CA  . LEU A 1 138 ? -41.716 2.621   1.643   1.00 32.44 ? 138 LEU A CA  1 
ATOM   930  C  C   . LEU A 1 138 ? -41.988 1.230   2.202   1.00 35.86 ? 138 LEU A C   1 
ATOM   931  O  O   . LEU A 1 138 ? -42.078 1.050   3.417   1.00 36.91 ? 138 LEU A O   1 
ATOM   932  C  CB  . LEU A 1 138 ? -40.266 3.011   1.943   1.00 29.96 ? 138 LEU A CB  1 
ATOM   933  C  CG  . LEU A 1 138 ? -39.851 4.413   1.509   1.00 32.22 ? 138 LEU A CG  1 
ATOM   934  C  CD1 . LEU A 1 138 ? -38.427 4.802   1.815   1.00 33.90 ? 138 LEU A CD1 1 
ATOM   935  C  CD2 . LEU A 1 138 ? -40.016 4.550   0.020   1.00 33.90 ? 138 LEU A CD2 1 
ATOM   936  N  N   . THR A 1 139 ? -42.126 0.250   1.302   1.00 32.57 ? 139 THR A N   1 
ATOM   937  C  CA  . THR A 1 139 ? -42.365 -1.133  1.694   1.00 34.78 ? 139 THR A CA  1 
ATOM   938  C  C   . THR A 1 139 ? -41.183 -1.980  1.254   1.00 33.38 ? 139 THR A C   1 
ATOM   939  O  O   . THR A 1 139 ? -40.887 -2.020  0.064   1.00 35.13 ? 139 THR A O   1 
ATOM   940  C  CB  . THR A 1 139 ? -43.637 -1.663  1.012   1.00 36.83 ? 139 THR A CB  1 
ATOM   941  O  OG1 . THR A 1 139 ? -44.702 -0.833  1.474   1.00 38.55 ? 139 THR A OG1 1 
ATOM   942  C  CG2 . THR A 1 139 ? -43.942 -3.081  1.439   1.00 39.01 ? 139 THR A CG2 1 
ATOM   943  N  N   . GLN A 1 140 ? -40.572 -2.688  2.206   1.00 29.09 ? 140 GLN A N   1 
ATOM   944  C  CA  . GLN A 1 140 ? -39.480 -3.612  1.960   1.00 30.37 ? 140 GLN A CA  1 
ATOM   945  C  C   . GLN A 1 140 ? -40.017 -5.040  1.861   1.00 33.41 ? 140 GLN A C   1 
ATOM   946  O  O   . GLN A 1 140 ? -40.914 -5.436  2.600   1.00 33.08 ? 140 GLN A O   1 
ATOM   947  C  CB  . GLN A 1 140 ? -38.399 -3.531  3.053   1.00 32.36 ? 140 GLN A CB  1 
ATOM   948  C  CG  . GLN A 1 140 ? -37.857 -2.108  3.141   1.00 33.74 ? 140 GLN A CG  1 
ATOM   949  C  CD  . GLN A 1 140 ? -36.644 -1.962  4.041   1.00 33.85 ? 140 GLN A CD  1 
ATOM   950  O  OE1 . GLN A 1 140 ? -36.483 -0.896  4.614   1.00 33.03 ? 140 GLN A OE1 1 
ATOM   951  N  NE2 . GLN A 1 140 ? -35.735 -2.939  4.058   1.00 31.55 ? 140 GLN A NE2 1 
ATOM   952  N  N   . SER A 1 141 ? -39.374 -5.845  1.023   1.00 31.43 ? 141 SER A N   1 
ATOM   953  C  CA  . SER A 1 141 ? -39.799 -7.229  0.880   1.00 32.65 ? 141 SER A CA  1 
ATOM   954  C  C   . SER A 1 141 ? -38.566 -8.035  0.536   1.00 33.23 ? 141 SER A C   1 
ATOM   955  O  O   . SER A 1 141 ? -37.858 -7.657  -0.397  1.00 34.50 ? 141 SER A O   1 
ATOM   956  C  CB  . SER A 1 141 ? -40.817 -7.350  -0.254  1.00 36.54 ? 141 SER A CB  1 
ATOM   957  O  OG  . SER A 1 141 ? -41.247 -8.705  -0.177  1.00 40.62 ? 141 SER A OG  1 
ATOM   958  N  N   . PRO A 1 142 ? -38.203 -9.130  1.239   1.00 31.10 ? 142 PRO A N   1 
ATOM   959  C  CA  . PRO A 1 142 ? -38.869 -9.570  2.469   1.00 31.93 ? 142 PRO A CA  1 
ATOM   960  C  C   . PRO A 1 142 ? -38.465 -8.715  3.669   1.00 35.77 ? 142 PRO A C   1 
ATOM   961  O  O   . PRO A 1 142 ? -37.620 -7.826  3.570   1.00 32.97 ? 142 PRO A O   1 
ATOM   962  C  CB  . PRO A 1 142 ? -38.340 -11.002 2.549   1.00 33.19 ? 142 PRO A CB  1 
ATOM   963  C  CG  . PRO A 1 142 ? -36.929 -10.930 2.064   1.00 34.69 ? 142 PRO A CG  1 
ATOM   964  C  CD  . PRO A 1 142 ? -37.042 -9.961  0.903   1.00 31.92 ? 142 PRO A CD  1 
ATOM   965  N  N   . THR A 1 143 ? -39.122 -8.957  4.797   1.00 33.81 ? 143 THR A N   1 
ATOM   966  C  CA  . THR A 1 143 ? -38.739 -8.193  5.986   1.00 37.77 ? 143 THR A CA  1 
ATOM   967  C  C   . THR A 1 143 ? -37.722 -8.995  6.811   1.00 35.26 ? 143 THR A C   1 
ATOM   968  O  O   . THR A 1 143 ? -37.066 -8.420  7.694   1.00 34.92 ? 143 THR A O   1 
ATOM   969  C  CB  . THR A 1 143 ? -39.984 -7.872  6.819   1.00 39.82 ? 143 THR A CB  1 
ATOM   970  O  OG1 . THR A 1 143 ? -40.560 -9.122  7.148   1.00 46.46 ? 143 THR A OG1 1 
ATOM   971  C  CG2 . THR A 1 143 ? -41.065 -7.115  6.074   1.00 39.91 ? 143 THR A CG2 1 
ATOM   972  N  N   . SER A 1 144 ? -37.557 -10.301 6.516   1.00 33.77 ? 144 SER A N   1 
ATOM   973  C  CA  . SER A 1 144 ? -36.403 -11.025 7.043   1.00 36.40 ? 144 SER A CA  1 
ATOM   974  C  C   . SER A 1 144 ? -36.030 -12.165 6.127   1.00 36.47 ? 144 SER A C   1 
ATOM   975  O  O   . SER A 1 144 ? -36.892 -12.710 5.428   1.00 36.54 ? 144 SER A O   1 
ATOM   976  C  CB  . SER A 1 144 ? -36.587 -11.523 8.467   1.00 42.99 ? 144 SER A CB  1 
ATOM   977  O  OG  . SER A 1 144 ? -37.713 -12.380 8.502   1.00 51.93 ? 144 SER A OG  1 
ATOM   978  N  N   . LEU A 1 145 ? -34.754 -12.509 6.162   1.00 35.50 ? 145 LEU A N   1 
ATOM   979  C  CA  . LEU A 1 145 ? -34.283 -13.594 5.332   1.00 40.35 ? 145 LEU A CA  1 
ATOM   980  C  C   . LEU A 1 145 ? -32.968 -14.138 5.872   1.00 39.31 ? 145 LEU A C   1 
ATOM   981  O  O   . LEU A 1 145 ? -32.178 -13.407 6.494   1.00 37.73 ? 145 LEU A O   1 
ATOM   982  C  CB  . LEU A 1 145 ? -34.229 -13.249 3.835   1.00 39.70 ? 145 LEU A CB  1 
ATOM   983  C  CG  . LEU A 1 145 ? -33.012 -12.438 3.400   1.00 38.32 ? 145 LEU A CG  1 
ATOM   984  C  CD1 . LEU A 1 145 ? -32.879 -12.440 1.883   1.00 40.43 ? 145 LEU A CD1 1 
ATOM   985  C  CD2 . LEU A 1 145 ? -33.136 -10.996 3.931   1.00 37.15 ? 145 LEU A CD2 1 
ATOM   986  N  N   . ALA A 1 146 ? -32.743 -15.443 5.622   1.00 36.54 ? 146 ALA A N   1 
ATOM   987  C  CA  . ALA A 1 146 ? -31.476 -16.068 5.966   1.00 34.26 ? 146 ALA A CA  1 
ATOM   988  C  C   . ALA A 1 146 ? -30.879 -16.561 4.657   1.00 38.65 ? 146 ALA A C   1 
ATOM   989  O  O   . ALA A 1 146 ? -31.546 -17.308 3.959   1.00 37.59 ? 146 ALA A O   1 
ATOM   990  C  CB  . ALA A 1 146 ? -31.722 -17.253 6.931   1.00 37.60 ? 146 ALA A CB  1 
ATOM   991  N  N   . VAL A 1 147 ? -29.580 -16.333 4.445   1.00 39.35 ? 147 VAL A N   1 
ATOM   992  C  CA  . VAL A 1 147 ? -28.910 -16.662 3.201   1.00 41.74 ? 147 VAL A CA  1 
ATOM   993  C  C   . VAL A 1 147 ? -27.612 -17.393 3.554   1.00 42.60 ? 147 VAL A C   1 
ATOM   994  O  O   . VAL A 1 147 ? -26.919 -17.017 4.514   1.00 45.10 ? 147 VAL A O   1 
ATOM   995  C  CB  . VAL A 1 147 ? -28.646 -15.315 2.468   1.00 40.97 ? 147 VAL A CB  1 
ATOM   996  C  CG1 . VAL A 1 147 ? -27.688 -15.507 1.293   1.00 40.67 ? 147 VAL A CG1 1 
ATOM   997  C  CG2 . VAL A 1 147 ? -29.956 -14.652 1.975   1.00 40.86 ? 147 VAL A CG2 1 
ATOM   998  N  N   . SER A 1 148 ? -27.259 -18.438 2.781   1.00 40.24 ? 148 SER A N   1 
ATOM   999  C  CA  . SER A 1 148 ? -26.041 -19.170 3.099   1.00 41.45 ? 148 SER A CA  1 
ATOM   1000 C  C   . SER A 1 148 ? -24.801 -18.409 2.665   1.00 43.36 ? 148 SER A C   1 
ATOM   1001 O  O   . SER A 1 148 ? -24.812 -17.623 1.692   1.00 43.57 ? 148 SER A O   1 
ATOM   1002 C  CB  . SER A 1 148 ? -26.047 -20.546 2.487   1.00 56.01 ? 148 SER A CB  1 
ATOM   1003 O  OG  . SER A 1 148 ? -27.161 -21.277 2.972   1.00 56.71 ? 148 SER A OG  1 
ATOM   1004 N  N   . LEU A 1 149 ? -23.718 -18.653 3.386   1.00 40.04 ? 149 LEU A N   1 
ATOM   1005 C  CA  . LEU A 1 149 ? -22.453 -18.037 3.017   1.00 43.48 ? 149 LEU A CA  1 
ATOM   1006 C  C   . LEU A 1 149 ? -22.218 -18.231 1.533   1.00 47.10 ? 149 LEU A C   1 
ATOM   1007 O  O   . LEU A 1 149 ? -22.432 -19.332 1.004   1.00 44.61 ? 149 LEU A O   1 
ATOM   1008 C  CB  . LEU A 1 149 ? -21.250 -18.570 3.780   1.00 45.38 ? 149 LEU A CB  1 
ATOM   1009 C  CG  . LEU A 1 149 ? -21.052 -18.049 5.191   1.00 54.45 ? 149 LEU A CG  1 
ATOM   1010 C  CD1 . LEU A 1 149 ? -19.697 -18.597 5.622   1.00 61.00 ? 149 LEU A CD1 1 
ATOM   1011 C  CD2 . LEU A 1 149 ? -21.077 -16.525 5.317   1.00 57.36 ? 149 LEU A CD2 1 
ATOM   1012 N  N   . GLY A 1 150 ? -21.778 -17.143 0.882   1.00 42.41 ? 150 GLY A N   1 
ATOM   1013 C  CA  . GLY A 1 150 ? -21.459 -17.184 -0.539  1.00 44.21 ? 150 GLY A CA  1 
ATOM   1014 C  C   . GLY A 1 150 ? -22.673 -17.112 -1.455  1.00 42.65 ? 150 GLY A C   1 
ATOM   1015 O  O   . GLY A 1 150 ? -22.496 -17.046 -2.663  1.00 44.59 ? 150 GLY A O   1 
ATOM   1016 N  N   . GLN A 1 151 ? -23.899 -17.095 -0.925  1.00 40.35 ? 151 GLN A N   1 
ATOM   1017 C  CA  . GLN A 1 151 ? -25.064 -17.032 -1.803  1.00 40.61 ? 151 GLN A CA  1 
ATOM   1018 C  C   . GLN A 1 151 ? -25.524 -15.576 -1.965  1.00 42.91 ? 151 GLN A C   1 
ATOM   1019 O  O   . GLN A 1 151 ? -24.820 -14.657 -1.546  1.00 41.44 ? 151 GLN A O   1 
ATOM   1020 C  CB  . GLN A 1 151 ? -26.165 -17.905 -1.213  1.00 43.09 ? 151 GLN A CB  1 
ATOM   1021 C  CG  . GLN A 1 151 ? -25.848 -19.405 -1.218  1.00 47.81 ? 151 GLN A CG  1 
ATOM   1022 C  CD  . GLN A 1 151 ? -25.780 -19.971 -2.613  0.70 55.99 ? 151 GLN A CD  1 
ATOM   1023 O  OE1 . GLN A 1 151 ? -24.701 -20.085 -3.198  0.70 60.23 ? 151 GLN A OE1 1 
ATOM   1024 N  NE2 . GLN A 1 151 ? -26.942 -20.259 -3.182  0.70 61.44 ? 151 GLN A NE2 1 
ATOM   1025 N  N   . ARG A 1 152 ? -26.703 -15.346 -2.560  1.00 39.15 ? 152 ARG A N   1 
ATOM   1026 C  CA  . ARG A 1 152 ? -27.110 -13.969 -2.887  1.00 36.90 ? 152 ARG A CA  1 
ATOM   1027 C  C   . ARG A 1 152 ? -28.309 -13.564 -2.030  1.00 34.58 ? 152 ARG A C   1 
ATOM   1028 O  O   . ARG A 1 152 ? -29.230 -14.372 -1.802  1.00 34.59 ? 152 ARG A O   1 
ATOM   1029 C  CB  . ARG A 1 152 ? -27.495 -13.885 -4.372  1.00 34.75 ? 152 ARG A CB  1 
ATOM   1030 C  CG  . ARG A 1 152 ? -28.130 -12.571 -4.809  1.00 36.38 ? 152 ARG A CG  1 
ATOM   1031 C  CD  . ARG A 1 152 ? -28.399 -12.589 -6.324  1.00 35.59 ? 152 ARG A CD  1 
ATOM   1032 N  NE  . ARG A 1 152 ? -27.123 -12.634 -7.058  1.00 35.26 ? 152 ARG A NE  1 
ATOM   1033 C  CZ  . ARG A 1 152 ? -26.332 -11.582 -7.266  1.00 37.55 ? 152 ARG A CZ  1 
ATOM   1034 N  NH1 . ARG A 1 152 ? -26.660 -10.354 -6.884  1.00 37.49 ? 152 ARG A NH1 1 
ATOM   1035 N  NH2 . ARG A 1 152 ? -25.207 -11.758 -7.923  1.00 44.04 ? 152 ARG A NH2 1 
ATOM   1036 N  N   . ALA A 1 153 ? -28.293 -12.327 -1.516  1.00 31.94 ? 153 ALA A N   1 
ATOM   1037 C  CA  . ALA A 1 153 ? -29.461 -11.757 -0.884  1.00 31.18 ? 153 ALA A CA  1 
ATOM   1038 C  C   . ALA A 1 153 ? -29.978 -10.637 -1.800  1.00 36.38 ? 153 ALA A C   1 
ATOM   1039 O  O   . ALA A 1 153 ? -29.180 -9.818  -2.277  1.00 37.41 ? 153 ALA A O   1 
ATOM   1040 C  CB  . ALA A 1 153 ? -29.092 -11.199 0.491   1.00 33.80 ? 153 ALA A CB  1 
ATOM   1041 N  N   . THR A 1 154 ? -31.300 -10.607 -2.034  1.00 33.59 ? 154 THR A N   1 
ATOM   1042 C  CA  . THR A 1 154 ? -31.925 -9.578  -2.852  1.00 34.74 ? 154 THR A CA  1 
ATOM   1043 C  C   . THR A 1 154 ? -33.090 -9.038  -2.041  1.00 34.18 ? 154 THR A C   1 
ATOM   1044 O  O   . THR A 1 154 ? -33.879 -9.819  -1.520  1.00 34.33 ? 154 THR A O   1 
ATOM   1045 C  CB  . THR A 1 154 ? -32.442 -10.258 -4.120  1.00 35.18 ? 154 THR A CB  1 
ATOM   1046 O  OG1 . THR A 1 154 ? -31.332 -10.856 -4.792  1.00 34.35 ? 154 THR A OG1 1 
ATOM   1047 C  CG2 . THR A 1 154 ? -33.155 -9.243  -4.980  1.00 32.53 ? 154 THR A CG2 1 
ATOM   1048 N  N   . ILE A 1 155 ? -33.174 -7.717  -1.903  1.00 30.26 ? 155 ILE A N   1 
ATOM   1049 C  CA  . ILE A 1 155 ? -34.197 -7.068  -1.106  1.00 31.08 ? 155 ILE A CA  1 
ATOM   1050 C  C   . ILE A 1 155 ? -34.817 -5.957  -1.934  1.00 33.44 ? 155 ILE A C   1 
ATOM   1051 O  O   . ILE A 1 155 ? -34.089 -5.155  -2.533  1.00 36.07 ? 155 ILE A O   1 
ATOM   1052 C  CB  . ILE A 1 155 ? -33.573 -6.499  0.202   1.00 30.86 ? 155 ILE A CB  1 
ATOM   1053 C  CG1 . ILE A 1 155 ? -32.913 -7.618  1.007   1.00 31.39 ? 155 ILE A CG1 1 
ATOM   1054 C  CG2 . ILE A 1 155 ? -34.617 -5.742  1.022   1.00 29.64 ? 155 ILE A CG2 1 
ATOM   1055 C  CD1 . ILE A 1 155 ? -32.052 -7.075  2.154   1.00 32.61 ? 155 ILE A CD1 1 
ATOM   1056 N  N   . SER A 1 156 ? -36.140 -5.896  -1.900  1.00 32.16 ? 156 SER A N   1 
ATOM   1057 C  CA  . SER A 1 156 ? -36.922 -4.936  -2.658  1.00 33.75 ? 156 SER A CA  1 
ATOM   1058 C  C   . SER A 1 156 ? -37.391 -3.816  -1.738  1.00 33.68 ? 156 SER A C   1 
ATOM   1059 O  O   . SER A 1 156 ? -37.731 -4.051  -0.585  1.00 30.86 ? 156 SER A O   1 
ATOM   1060 C  CB  . SER A 1 156 ? -38.126 -5.653  -3.210  1.00 35.59 ? 156 SER A CB  1 
ATOM   1061 O  OG  . SER A 1 156 ? -39.014 -4.750  -3.834  1.00 39.22 ? 156 SER A OG  1 
ATOM   1062 N  N   . CYS A 1 157 ? -37.406 -2.593  -2.281  1.00 34.17 ? 157 CYS A N   1 
ATOM   1063 C  CA  . CYS A 1 157 ? -38.014 -1.440  -1.640  1.00 32.63 ? 157 CYS A CA  1 
ATOM   1064 C  C   . CYS A 1 157 ? -38.921 -0.790  -2.685  1.00 38.11 ? 157 CYS A C   1 
ATOM   1065 O  O   . CYS A 1 157 ? -38.445 -0.400  -3.763  1.00 36.54 ? 157 CYS A O   1 
ATOM   1066 C  CB  . CYS A 1 157 ? -36.934 -0.421  -1.289  1.00 37.23 ? 157 CYS A CB  1 
ATOM   1067 S  SG  . CYS A 1 157 ? -37.623 1.012   -0.405  1.00 44.46 ? 157 CYS A SG  1 
ATOM   1068 N  N   . LYS A 1 158 ? -40.194 -0.628  -2.326  1.00 34.19 ? 158 LYS A N   1 
ATOM   1069 C  CA  . LYS A 1 158 ? -41.131 0.008   -3.238  1.00 35.72 ? 158 LYS A CA  1 
ATOM   1070 C  C   . LYS A 1 158 ? -41.762 1.221   -2.587  1.00 36.79 ? 158 LYS A C   1 
ATOM   1071 O  O   . LYS A 1 158 ? -42.160 1.127   -1.423  1.00 40.44 ? 158 LYS A O   1 
ATOM   1072 C  CB  . LYS A 1 158 ? -42.239 -0.970  -3.645  1.00 35.92 ? 158 LYS A CB  1 
ATOM   1073 C  CG  . LYS A 1 158 ? -41.700 -2.038  -4.610  1.00 38.55 ? 158 LYS A CG  1 
ATOM   1074 C  CD  . LYS A 1 158 ? -42.676 -3.174  -4.965  1.00 40.46 ? 158 LYS A CD  1 
ATOM   1075 C  CE  . LYS A 1 158 ? -42.058 -3.963  -6.101  0.70 39.76 ? 158 LYS A CE  1 
ATOM   1076 N  NZ  . LYS A 1 158 ? -43.009 -4.974  -6.635  0.70 43.43 ? 158 LYS A NZ  1 
ATOM   1077 N  N   . ALA A 1 159 ? -41.834 2.330   -3.355  1.00 33.02 ? 159 ALA A N   1 
ATOM   1078 C  CA  . ALA A 1 159 ? -42.352 3.582   -2.830  1.00 36.04 ? 159 ALA A CA  1 
ATOM   1079 C  C   . ALA A 1 159 ? -43.778 3.806   -3.338  1.00 40.63 ? 159 ALA A C   1 
ATOM   1080 O  O   . ALA A 1 159 ? -44.051 3.502   -4.495  1.00 38.34 ? 159 ALA A O   1 
ATOM   1081 C  CB  . ALA A 1 159 ? -41.491 4.753   -3.308  1.00 33.72 ? 159 ALA A CB  1 
ATOM   1082 N  N   . SER A 1 160 ? -44.602 4.496   -2.547  1.00 36.65 ? 160 SER A N   1 
ATOM   1083 C  CA  . SER A 1 160 ? -45.980 4.768   -2.902  1.00 40.03 ? 160 SER A CA  1 
ATOM   1084 C  C   . SER A 1 160 ? -46.074 5.844   -3.991  1.00 46.01 ? 160 SER A C   1 
ATOM   1085 O  O   . SER A 1 160 ? -47.063 5.887   -4.702  1.00 44.33 ? 160 SER A O   1 
ATOM   1086 C  CB  . SER A 1 160 ? -46.800 5.106   -1.694  1.00 37.69 ? 160 SER A CB  1 
ATOM   1087 O  OG  . SER A 1 160 ? -46.314 6.273   -1.058  1.00 40.26 ? 160 SER A OG  1 
ATOM   1088 N  N   . GLN A 1 161 ? -45.066 6.711   -4.120  1.00 42.20 ? 161 GLN A N   1 
ATOM   1089 C  CA  . GLN A 1 161 ? -44.976 7.714   -5.173  1.00 42.38 ? 161 GLN A CA  1 
ATOM   1090 C  C   . GLN A 1 161 ? -43.519 7.774   -5.647  1.00 44.70 ? 161 GLN A C   1 
ATOM   1091 O  O   . GLN A 1 161 ? -42.612 7.319   -4.935  1.00 41.55 ? 161 GLN A O   1 
ATOM   1092 C  CB  . GLN A 1 161 ? -45.292 9.119   -4.652  1.00 42.96 ? 161 GLN A CB  1 
ATOM   1093 C  CG  . GLN A 1 161 ? -46.675 9.291   -4.032  1.00 51.06 ? 161 GLN A CG  1 
ATOM   1094 C  CD  . GLN A 1 161 ? -46.829 10.608  -3.293  0.60 52.54 ? 161 GLN A CD  1 
ATOM   1095 O  OE1 . GLN A 1 161 ? -47.213 10.654  -2.120  0.60 52.19 ? 161 GLN A OE1 1 
ATOM   1096 N  NE2 . GLN A 1 161 ? -46.502 11.706  -3.957  0.60 52.44 ? 161 GLN A NE2 1 
ATOM   1097 N  N   . SER A 1 162 ? -43.281 8.355   -6.842  1.00 39.28 ? 162 SER A N   1 
ATOM   1098 C  CA  . SER A 1 162 ? -41.932 8.489   -7.388  1.00 42.51 ? 162 SER A CA  1 
ATOM   1099 C  C   . SER A 1 162 ? -41.009 9.203   -6.399  1.00 42.27 ? 162 SER A C   1 
ATOM   1100 O  O   . SER A 1 162 ? -41.394 10.192  -5.774  1.00 40.62 ? 162 SER A O   1 
ATOM   1101 C  CB  . SER A 1 162 ? -41.944 9.274   -8.687  1.00 47.71 ? 162 SER A CB  1 
ATOM   1102 O  OG  . SER A 1 162 ? -40.615 9.444   -9.170  1.00 46.21 ? 162 SER A OG  1 
ATOM   1103 N  N   . VAL A 1 163 ? -39.751 8.756   -6.330  1.00 38.30 ? 163 VAL A N   1 
ATOM   1104 C  CA  . VAL A 1 163 ? -38.794 9.469   -5.493  1.00 38.79 ? 163 VAL A CA  1 
ATOM   1105 C  C   . VAL A 1 163 ? -37.701 10.096  -6.342  1.00 41.89 ? 163 VAL A C   1 
ATOM   1106 O  O   . VAL A 1 163 ? -36.654 10.501  -5.809  1.00 40.95 ? 163 VAL A O   1 
ATOM   1107 C  CB  . VAL A 1 163 ? -38.197 8.552   -4.401  1.00 38.15 ? 163 VAL A CB  1 
ATOM   1108 C  CG1 . VAL A 1 163 ? -39.300 8.071   -3.445  1.00 39.66 ? 163 VAL A CG1 1 
ATOM   1109 C  CG2 . VAL A 1 163 ? -37.401 7.371   -4.997  1.00 34.94 ? 163 VAL A CG2 1 
ATOM   1110 N  N   . ASP A 1 164 ? -37.986 10.232  -7.640  1.00 40.39 ? 164 ASP A N   1 
ATOM   1111 C  CA  . ASP A 1 164 ? -36.993 10.738  -8.572  1.00 38.81 ? 164 ASP A CA  1 
ATOM   1112 C  C   . ASP A 1 164 ? -37.194 12.226  -8.875  1.00 39.39 ? 164 ASP A C   1 
ATOM   1113 O  O   . ASP A 1 164 ? -38.313 12.723  -8.887  1.00 39.97 ? 164 ASP A O   1 
ATOM   1114 C  CB  . ASP A 1 164 ? -37.062 10.001  -9.890  1.00 43.11 ? 164 ASP A CB  1 
ATOM   1115 C  CG  . ASP A 1 164 ? -36.556 8.569   -9.884  1.00 48.42 ? 164 ASP A CG  1 
ATOM   1116 O  OD1 . ASP A 1 164 ? -36.189 8.081   -8.786  1.00 49.54 ? 164 ASP A OD1 1 
ATOM   1117 O  OD2 . ASP A 1 164 ? -36.510 7.984   -10.992 1.00 52.19 ? 164 ASP A OD2 1 
ATOM   1118 N  N   . TYR A 1 165 ? -36.081 12.921  -9.140  1.00 35.95 ? 165 TYR A N   1 
ATOM   1119 C  CA  . TYR A 1 165 ? -36.112 14.306  -9.576  1.00 37.84 ? 165 TYR A CA  1 
ATOM   1120 C  C   . TYR A 1 165 ? -34.947 14.516  -10.516 1.00 41.98 ? 165 TYR A C   1 
ATOM   1121 O  O   . TYR A 1 165 ? -33.808 14.222  -10.171 1.00 41.96 ? 165 TYR A O   1 
ATOM   1122 C  CB  . TYR A 1 165 ? -36.003 15.202  -8.342  1.00 37.44 ? 165 TYR A CB  1 
ATOM   1123 C  CG  . TYR A 1 165 ? -35.814 16.628  -8.842  1.00 41.20 ? 165 TYR A CG  1 
ATOM   1124 C  CD1 . TYR A 1 165 ? -36.909 17.327  -9.345  1.00 43.52 ? 165 TYR A CD1 1 
ATOM   1125 C  CD2 . TYR A 1 165 ? -34.562 17.242  -8.872  1.00 38.98 ? 165 TYR A CD2 1 
ATOM   1126 C  CE1 . TYR A 1 165 ? -36.771 18.605  -9.877  1.00 44.01 ? 165 TYR A CE1 1 
ATOM   1127 C  CE2 . TYR A 1 165 ? -34.403 18.527  -9.389  1.00 46.39 ? 165 TYR A CE2 1 
ATOM   1128 C  CZ  . TYR A 1 165 ? -35.521 19.199  -9.875  1.00 48.45 ? 165 TYR A CZ  1 
ATOM   1129 O  OH  . TYR A 1 165 ? -35.439 20.461  -10.339 1.00 49.10 ? 165 TYR A OH  1 
ATOM   1130 N  N   . ASP A 1 166 ? -35.278 14.972  -11.721 1.00 47.95 ? 166 ASP A N   1 
ATOM   1131 C  CA  . ASP A 1 166 ? -34.273 15.306  -12.709 1.00 49.40 ? 166 ASP A CA  1 
ATOM   1132 C  C   . ASP A 1 166 ? -33.355 14.109  -12.970 1.00 49.22 ? 166 ASP A C   1 
ATOM   1133 O  O   . ASP A 1 166 ? -32.142 14.277  -13.032 1.00 50.00 ? 166 ASP A O   1 
ATOM   1134 C  CB  . ASP A 1 166 ? -33.551 16.577  -12.291 1.00 48.72 ? 166 ASP A CB  1 
ATOM   1135 C  CG  . ASP A 1 166 ? -32.595 17.144  -13.334 1.00 62.04 ? 166 ASP A CG  1 
ATOM   1136 O  OD1 . ASP A 1 166 ? -32.991 17.186  -14.518 1.00 56.69 ? 166 ASP A OD1 1 
ATOM   1137 O  OD2 . ASP A 1 166 ? -31.442 17.514  -12.963 1.00 60.14 ? 166 ASP A OD2 1 
ATOM   1138 N  N   . GLY A 1 167 ? -33.937 12.910  -13.141 1.00 45.10 ? 167 GLY A N   1 
ATOM   1139 C  CA  . GLY A 1 167 ? -33.144 11.743  -13.493 1.00 52.25 ? 167 GLY A CA  1 
ATOM   1140 C  C   . GLY A 1 167 ? -32.292 11.162  -12.347 1.00 56.30 ? 167 GLY A C   1 
ATOM   1141 O  O   . GLY A 1 167 ? -31.565 10.191  -12.559 1.00 54.43 ? 167 GLY A O   1 
ATOM   1142 N  N   . ASP A 1 168 ? -32.371 11.731  -11.135 1.00 46.45 ? 168 ASP A N   1 
ATOM   1143 C  CA  . ASP A 1 168 ? -31.732 11.140  -9.946  1.00 43.26 ? 168 ASP A CA  1 
ATOM   1144 C  C   . ASP A 1 168 ? -32.784 10.593  -8.986  1.00 41.22 ? 168 ASP A C   1 
ATOM   1145 O  O   . ASP A 1 168 ? -33.785 11.274  -8.789  1.00 40.38 ? 168 ASP A O   1 
ATOM   1146 C  CB  . ASP A 1 168 ? -31.014 12.213  -9.137  1.00 42.74 ? 168 ASP A CB  1 
ATOM   1147 C  CG  . ASP A 1 168 ? -29.901 12.919  -9.880  1.00 45.97 ? 168 ASP A CG  1 
ATOM   1148 O  OD1 . ASP A 1 168 ? -29.186 12.232  -10.617 1.00 53.18 ? 168 ASP A OD1 1 
ATOM   1149 O  OD2 . ASP A 1 168 ? -29.767 14.138  -9.704  1.00 46.90 ? 168 ASP A OD2 1 
ATOM   1150 N  N   . SER A 1 169 ? -32.512 9.421   -8.343  1.00 37.78 ? 169 SER A N   1 
ATOM   1151 C  CA  . SER A 1 169 ? -33.403 8.844   -7.346  1.00 35.14 ? 169 SER A CA  1 
ATOM   1152 C  C   . SER A 1 169 ? -32.974 9.296   -5.966  1.00 34.21 ? 169 SER A C   1 
ATOM   1153 O  O   . SER A 1 169 ? -31.823 9.070   -5.602  1.00 40.17 ? 169 SER A O   1 
ATOM   1154 C  CB  . SER A 1 169 ? -33.408 7.318   -7.425  1.00 33.91 ? 169 SER A CB  1 
ATOM   1155 O  OG  . SER A 1 169 ? -33.842 6.907   -8.718  1.00 39.29 ? 169 SER A OG  1 
ATOM   1156 N  N   . TYR A 1 170 ? -33.878 9.988   -5.262  1.00 31.10 ? 170 TYR A N   1 
ATOM   1157 C  CA  . TYR A 1 170 ? -33.616 10.466  -3.904  1.00 33.32 ? 170 TYR A CA  1 
ATOM   1158 C  C   . TYR A 1 170 ? -33.954 9.326   -2.941  1.00 33.32 ? 170 TYR A C   1 
ATOM   1159 O  O   . TYR A 1 170 ? -34.828 9.451   -2.081  1.00 33.97 ? 170 TYR A O   1 
ATOM   1160 C  CB  . TYR A 1 170 ? -34.400 11.734  -3.560  1.00 32.12 ? 170 TYR A CB  1 
ATOM   1161 C  CG  . TYR A 1 170 ? -33.699 12.916  -4.241  1.00 33.73 ? 170 TYR A CG  1 
ATOM   1162 C  CD1 . TYR A 1 170 ? -33.696 13.036  -5.655  1.00 33.94 ? 170 TYR A CD1 1 
ATOM   1163 C  CD2 . TYR A 1 170 ? -32.945 13.831  -3.509  1.00 38.29 ? 170 TYR A CD2 1 
ATOM   1164 C  CE1 . TYR A 1 170 ? -32.982 14.061  -6.280  1.00 37.88 ? 170 TYR A CE1 1 
ATOM   1165 C  CE2 . TYR A 1 170 ? -32.266 14.884  -4.134  1.00 40.38 ? 170 TYR A CE2 1 
ATOM   1166 C  CZ  . TYR A 1 170 ? -32.259 14.972  -5.520  1.00 41.06 ? 170 TYR A CZ  1 
ATOM   1167 O  OH  . TYR A 1 170 ? -31.596 16.017  -6.109  1.00 42.67 ? 170 TYR A OH  1 
ATOM   1168 N  N   . MET A 1 171 ? -33.201 8.241   -3.087  1.00 32.30 ? 171 MET A N   1 
ATOM   1169 C  CA  A MET A 1 171 ? -33.398 7.139   -2.161  0.70 33.96 ? 171 MET A CA  1 
ATOM   1170 C  CA  B MET A 1 171 ? -33.414 6.992   -2.364  0.30 33.20 ? 171 MET A CA  1 
ATOM   1171 C  C   . MET A 1 171 ? -32.060 6.501   -1.851  1.00 32.35 ? 171 MET A C   1 
ATOM   1172 O  O   . MET A 1 171 ? -31.147 6.422   -2.667  1.00 32.32 ? 171 MET A O   1 
ATOM   1173 C  CB  A MET A 1 171 ? -34.458 6.150   -2.668  0.70 34.13 ? 171 MET A CB  1 
ATOM   1174 C  CB  B MET A 1 171 ? -34.048 6.028   -3.384  0.30 31.92 ? 171 MET A CB  1 
ATOM   1175 C  CG  A MET A 1 171 ? -33.921 5.129   -3.631  0.70 29.65 ? 171 MET A CG  1 
ATOM   1176 C  CG  B MET A 1 171 ? -34.096 4.554   -3.055  0.30 33.75 ? 171 MET A CG  1 
ATOM   1177 S  SD  A MET A 1 171 ? -32.842 3.867   -2.907  0.70 35.79 ? 171 MET A SD  1 
ATOM   1178 S  SD  B MET A 1 171 ? -34.912 4.165   -1.498  0.30 36.57 ? 171 MET A SD  1 
ATOM   1179 C  CE  A MET A 1 171 ? -33.882 3.163   -1.629  0.70 30.92 ? 171 MET A CE  1 
ATOM   1180 C  CE  B MET A 1 171 ? -36.539 4.917   -1.522  0.30 31.92 ? 171 MET A CE  1 
ATOM   1181 N  N   . ASN A 1 172 ? -31.905 6.153   -0.548  1.00 29.76 ? 172 ASN A N   1 
ATOM   1182 C  CA  . ASN A 1 172 ? -30.649 5.591   -0.058  1.00 29.11 ? 172 ASN A CA  1 
ATOM   1183 C  C   . ASN A 1 172 ? -30.971 4.298   0.695   1.00 27.79 ? 172 ASN A C   1 
ATOM   1184 O  O   . ASN A 1 172 ? -32.105 4.108   1.143   1.00 30.40 ? 172 ASN A O   1 
ATOM   1185 C  CB  . ASN A 1 172 ? -29.934 6.485   0.988   1.00 25.45 ? 172 ASN A CB  1 
ATOM   1186 C  CG  . ASN A 1 172 ? -29.677 7.892   0.458   1.00 33.16 ? 172 ASN A CG  1 
ATOM   1187 O  OD1 . ASN A 1 172 ? -29.474 8.072   -0.753  1.00 29.67 ? 172 ASN A OD1 1 
ATOM   1188 N  ND2 . ASN A 1 172 ? -29.734 8.916   1.307   1.00 32.60 ? 172 ASN A ND2 1 
ATOM   1189 N  N   . TRP A 1 173 ? -29.975 3.409   0.784   1.00 29.22 ? 173 TRP A N   1 
ATOM   1190 C  CA  . TRP A 1 173 ? -30.038 2.293   1.728   1.00 29.59 ? 173 TRP A CA  1 
ATOM   1191 C  C   . TRP A 1 173 ? -29.044 2.499   2.876   1.00 30.44 ? 173 TRP A C   1 
ATOM   1192 O  O   . TRP A 1 173 ? -27.922 2.977   2.679   1.00 30.73 ? 173 TRP A O   1 
ATOM   1193 C  CB  . TRP A 1 173 ? -29.620 1.040   0.970   1.00 30.28 ? 173 TRP A CB  1 
ATOM   1194 C  CG  . TRP A 1 173 ? -30.580 0.611   -0.102  1.00 29.33 ? 173 TRP A CG  1 
ATOM   1195 C  CD1 . TRP A 1 173 ? -30.532 0.872   -1.456  1.00 30.79 ? 173 TRP A CD1 1 
ATOM   1196 C  CD2 . TRP A 1 173 ? -31.685 -0.287  0.106   1.00 27.75 ? 173 TRP A CD2 1 
ATOM   1197 N  NE1 . TRP A 1 173 ? -31.557 0.178   -2.068  1.00 31.37 ? 173 TRP A NE1 1 
ATOM   1198 C  CE2 . TRP A 1 173 ? -32.286 -0.519  -1.157  1.00 32.40 ? 173 TRP A CE2 1 
ATOM   1199 C  CE3 . TRP A 1 173 ? -32.238 -0.897  1.248   1.00 32.86 ? 173 TRP A CE3 1 
ATOM   1200 C  CZ2 . TRP A 1 173 ? -33.397 -1.361  -1.336  1.00 33.14 ? 173 TRP A CZ2 1 
ATOM   1201 C  CZ3 . TRP A 1 173 ? -33.350 -1.710  1.083   1.00 35.83 ? 173 TRP A CZ3 1 
ATOM   1202 C  CH2 . TRP A 1 173 ? -33.901 -1.932  -0.186  1.00 32.06 ? 173 TRP A CH2 1 
ATOM   1203 N  N   . TYR A 1 174 ? -29.454 2.015   4.053   1.00 29.19 ? 174 TYR A N   1 
ATOM   1204 C  CA  . TYR A 1 174 ? -28.676 2.091   5.280   1.00 31.26 ? 174 TYR A CA  1 
ATOM   1205 C  C   . TYR A 1 174 ? -28.520 0.645   5.784   1.00 30.51 ? 174 TYR A C   1 
ATOM   1206 O  O   . TYR A 1 174 ? -29.435 -0.207  5.608   1.00 30.37 ? 174 TYR A O   1 
ATOM   1207 C  CB  . TYR A 1 174 ? -29.398 2.929   6.335   1.00 28.09 ? 174 TYR A CB  1 
ATOM   1208 C  CG  . TYR A 1 174 ? -29.409 4.394   5.924   1.00 31.04 ? 174 TYR A CG  1 
ATOM   1209 C  CD1 . TYR A 1 174 ? -28.286 5.221   6.133   1.00 28.64 ? 174 TYR A CD1 1 
ATOM   1210 C  CD2 . TYR A 1 174 ? -30.456 4.891   5.133   1.00 30.18 ? 174 TYR A CD2 1 
ATOM   1211 C  CE1 . TYR A 1 174 ? -28.259 6.555   5.711   1.00 30.87 ? 174 TYR A CE1 1 
ATOM   1212 C  CE2 . TYR A 1 174 ? -30.466 6.227   4.755   1.00 32.69 ? 174 TYR A CE2 1 
ATOM   1213 C  CZ  . TYR A 1 174 ? -29.345 7.028   4.958   1.00 31.05 ? 174 TYR A CZ  1 
ATOM   1214 O  OH  . TYR A 1 174 ? -29.392 8.289   4.412   1.00 33.88 ? 174 TYR A OH  1 
ATOM   1215 N  N   . GLN A 1 175 ? -27.343 0.364   6.379   1.00 28.43 ? 175 GLN A N   1 
ATOM   1216 C  CA  . GLN A 1 175 ? -27.119 -0.915  7.012   1.00 28.56 ? 175 GLN A CA  1 
ATOM   1217 C  C   . GLN A 1 175 ? -26.904 -0.681  8.498   1.00 28.73 ? 175 GLN A C   1 
ATOM   1218 O  O   . GLN A 1 175 ? -26.126 0.211   8.891   1.00 34.14 ? 175 GLN A O   1 
ATOM   1219 C  CB  . GLN A 1 175 ? -25.823 -1.472  6.427   1.00 31.31 ? 175 GLN A CB  1 
ATOM   1220 C  CG  . GLN A 1 175 ? -25.335 -2.784  7.047   1.00 31.87 ? 175 GLN A CG  1 
ATOM   1221 C  CD  . GLN A 1 175 ? -23.952 -3.161  6.517   1.00 37.06 ? 175 GLN A CD  1 
ATOM   1222 O  OE1 . GLN A 1 175 ? -22.975 -2.393  6.616   1.00 36.21 ? 175 GLN A OE1 1 
ATOM   1223 N  NE2 . GLN A 1 175 ? -23.812 -4.360  5.962   1.00 31.95 ? 175 GLN A NE2 1 
ATOM   1224 N  N   . GLN A 1 176 ? -27.536 -1.515  9.298   1.00 27.50 ? 176 GLN A N   1 
ATOM   1225 C  CA  . GLN A 1 176 ? -27.185 -1.467  10.726  1.00 27.70 ? 176 GLN A CA  1 
ATOM   1226 C  C   . GLN A 1 176 ? -26.743 -2.859  11.184  1.00 33.63 ? 176 GLN A C   1 
ATOM   1227 O  O   . GLN A 1 176 ? -27.577 -3.758  11.329  1.00 32.44 ? 176 GLN A O   1 
ATOM   1228 C  CB  . GLN A 1 176 ? -28.368 -1.063  11.570  1.00 29.37 ? 176 GLN A CB  1 
ATOM   1229 C  CG  . GLN A 1 176 ? -27.916 -0.962  13.033  1.00 32.13 ? 176 GLN A CG  1 
ATOM   1230 C  CD  . GLN A 1 176 ? -28.920 -0.278  13.925  1.00 36.59 ? 176 GLN A CD  1 
ATOM   1231 O  OE1 . GLN A 1 176 ? -30.126 -0.314  13.669  1.00 34.42 ? 176 GLN A OE1 1 
ATOM   1232 N  NE2 . GLN A 1 176 ? -28.407 0.446   14.919  1.00 34.20 ? 176 GLN A NE2 1 
ATOM   1233 N  N   . LYS A 1 177 ? -25.423 -3.031  11.382  1.00 33.61 ? 177 LYS A N   1 
ATOM   1234 C  CA  . LYS A 1 177 ? -24.901 -4.299  11.872  1.00 33.74 ? 177 LYS A CA  1 
ATOM   1235 C  C   . LYS A 1 177 ? -25.222 -4.424  13.365  1.00 35.49 ? 177 LYS A C   1 
ATOM   1236 O  O   . LYS A 1 177 ? -25.479 -3.433  14.055  1.00 36.09 ? 177 LYS A O   1 
ATOM   1237 C  CB  . LYS A 1 177 ? -23.380 -4.394  11.668  1.00 36.99 ? 177 LYS A CB  1 
ATOM   1238 C  CG  . LYS A 1 177 ? -22.996 -4.500  10.197  1.00 36.75 ? 177 LYS A CG  1 
ATOM   1239 C  CD  . LYS A 1 177 ? -21.487 -4.540  9.991   1.00 39.42 ? 177 LYS A CD  1 
ATOM   1240 C  CE  . LYS A 1 177 ? -21.039 -4.548  8.564   1.00 48.67 ? 177 LYS A CE  1 
ATOM   1241 N  NZ  . LYS A 1 177 ? -19.568 -4.493  8.524   1.00 49.60 ? 177 LYS A NZ  1 
ATOM   1242 N  N   . PRO A 1 178 ? -25.264 -5.663  13.904  1.00 37.67 ? 178 PRO A N   1 
ATOM   1243 C  CA  . PRO A 1 178 ? -25.647 -5.891  15.297  1.00 37.48 ? 178 PRO A CA  1 
ATOM   1244 C  C   . PRO A 1 178 ? -24.695 -5.142  16.231  1.00 37.56 ? 178 PRO A C   1 
ATOM   1245 O  O   . PRO A 1 178 ? -23.467 -5.169  16.040  1.00 35.74 ? 178 PRO A O   1 
ATOM   1246 C  CB  . PRO A 1 178 ? -25.525 -7.433  15.423  1.00 40.22 ? 178 PRO A CB  1 
ATOM   1247 C  CG  . PRO A 1 178 ? -25.862 -7.915  14.012  1.00 43.58 ? 178 PRO A CG  1 
ATOM   1248 C  CD  . PRO A 1 178 ? -25.058 -6.929  13.161  1.00 40.97 ? 178 PRO A CD  1 
ATOM   1249 N  N   . GLY A 1 179 ? -25.328 -4.338  17.094  1.00 38.58 ? 179 GLY A N   1 
ATOM   1250 C  CA  . GLY A 1 179 ? -24.630 -3.578  18.112  1.00 40.26 ? 179 GLY A CA  1 
ATOM   1251 C  C   . GLY A 1 179 ? -23.952 -2.316  17.587  1.00 41.98 ? 179 GLY A C   1 
ATOM   1252 O  O   . GLY A 1 179 ? -23.333 -1.632  18.373  1.00 39.23 ? 179 GLY A O   1 
ATOM   1253 N  N   . GLN A 1 180 ? -24.061 -2.003  16.282  1.00 37.81 ? 180 GLN A N   1 
ATOM   1254 C  CA  A GLN A 1 180 ? -23.361 -0.863  15.694  0.70 37.51 ? 180 GLN A CA  1 
ATOM   1255 C  CA  B GLN A 1 180 ? -23.363 -0.878  15.674  0.30 37.54 ? 180 GLN A CA  1 
ATOM   1256 C  C   . GLN A 1 180 ? -24.393 0.204   15.312  1.00 37.30 ? 180 GLN A C   1 
ATOM   1257 O  O   . GLN A 1 180 ? -25.590 -0.077  15.178  1.00 36.39 ? 180 GLN A O   1 
ATOM   1258 C  CB  A GLN A 1 180 ? -22.582 -1.216  14.420  0.70 41.24 ? 180 GLN A CB  1 
ATOM   1259 C  CB  B GLN A 1 180 ? -22.522 -1.408  14.503  0.30 38.76 ? 180 GLN A CB  1 
ATOM   1260 C  CG  A GLN A 1 180 ? -21.315 -2.056  14.618  0.70 48.44 ? 180 GLN A CG  1 
ATOM   1261 C  CG  B GLN A 1 180 ? -21.701 -2.663  14.821  0.30 40.38 ? 180 GLN A CG  1 
ATOM   1262 C  CD  A GLN A 1 180 ? -20.282 -1.481  15.572  0.70 51.38 ? 180 GLN A CD  1 
ATOM   1263 C  CD  B GLN A 1 180 ? -20.615 -3.007  13.816  0.30 41.81 ? 180 GLN A CD  1 
ATOM   1264 O  OE1 A GLN A 1 180 ? -19.960 -2.108  16.585  0.70 57.93 ? 180 GLN A OE1 1 
ATOM   1265 O  OE1 B GLN A 1 180 ? -20.228 -2.193  12.971  0.30 45.06 ? 180 GLN A OE1 1 
ATOM   1266 N  NE2 A GLN A 1 180 ? -19.722 -0.312  15.274  0.70 54.81 ? 180 GLN A NE2 1 
ATOM   1267 N  NE2 B GLN A 1 180 ? -20.095 -4.228  13.894  0.30 39.49 ? 180 GLN A NE2 1 
ATOM   1268 N  N   . PRO A 1 181 ? -24.007 1.484   15.100  1.00 38.30 ? 181 PRO A N   1 
ATOM   1269 C  CA  . PRO A 1 181 ? -24.993 2.475   14.624  1.00 36.86 ? 181 PRO A CA  1 
ATOM   1270 C  C   . PRO A 1 181 ? -25.357 2.196   13.162  1.00 33.40 ? 181 PRO A C   1 
ATOM   1271 O  O   . PRO A 1 181 ? -24.588 1.568   12.449  1.00 35.88 ? 181 PRO A O   1 
ATOM   1272 C  CB  . PRO A 1 181 ? -24.296 3.847   14.777  1.00 37.54 ? 181 PRO A CB  1 
ATOM   1273 C  CG  . PRO A 1 181 ? -22.949 3.562   15.463  1.00 39.85 ? 181 PRO A CG  1 
ATOM   1274 C  CD  . PRO A 1 181 ? -22.658 2.055   15.302  1.00 39.72 ? 181 PRO A CD  1 
ATOM   1275 N  N   . PRO A 1 182 ? -26.478 2.715   12.630  1.00 33.01 ? 182 PRO A N   1 
ATOM   1276 C  CA  . PRO A 1 182 ? -26.741 2.603   11.183  1.00 32.11 ? 182 PRO A CA  1 
ATOM   1277 C  C   . PRO A 1 182 ? -25.650 3.381   10.463  1.00 31.91 ? 182 PRO A C   1 
ATOM   1278 O  O   . PRO A 1 182 ? -25.040 4.319   11.020  1.00 30.45 ? 182 PRO A O   1 
ATOM   1279 C  CB  . PRO A 1 182 ? -28.121 3.277   11.033  1.00 32.31 ? 182 PRO A CB  1 
ATOM   1280 C  CG  . PRO A 1 182 ? -28.670 3.292   12.459  1.00 34.73 ? 182 PRO A CG  1 
ATOM   1281 C  CD  . PRO A 1 182 ? -27.493 3.490   13.347  1.00 35.48 ? 182 PRO A CD  1 
ATOM   1282 N  N   . ARG A 1 183 ? -25.419 3.021   9.189   1.00 28.48 ? 183 ARG A N   1 
ATOM   1283 C  CA  . ARG A 1 183 ? -24.502 3.793   8.362   1.00 32.05 ? 183 ARG A CA  1 
ATOM   1284 C  C   . ARG A 1 183 ? -25.028 3.776   6.934   1.00 30.99 ? 183 ARG A C   1 
ATOM   1285 O  O   . ARG A 1 183 ? -25.713 2.819   6.558   1.00 28.33 ? 183 ARG A O   1 
ATOM   1286 C  CB  . ARG A 1 183 ? -23.083 3.193   8.387   1.00 34.41 ? 183 ARG A CB  1 
ATOM   1287 C  CG  . ARG A 1 183 ? -23.007 1.780   7.799   1.00 36.33 ? 183 ARG A CG  1 
ATOM   1288 C  CD  . ARG A 1 183 ? -21.570 1.220   7.880   1.00 36.68 ? 183 ARG A CD  1 
ATOM   1289 N  NE  . ARG A 1 183 ? -21.436 -0.072  7.192   1.00 35.74 ? 183 ARG A NE  1 
ATOM   1290 C  CZ  . ARG A 1 183 ? -20.286 -0.592  6.743   1.00 34.04 ? 183 ARG A CZ  1 
ATOM   1291 N  NH1 . ARG A 1 183 ? -19.161 0.120   6.819   1.00 35.63 ? 183 ARG A NH1 1 
ATOM   1292 N  NH2 . ARG A 1 183 ? -20.258 -1.799  6.175   1.00 35.82 ? 183 ARG A NH2 1 
ATOM   1293 N  N   . LEU A 1 184 ? -24.665 4.794   6.137   1.00 31.23 ? 184 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 184 ? -25.050 4.752   4.747   1.00 30.23 ? 184 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 184 ? -24.334 3.620   4.011   1.00 30.15 ? 184 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 184 ? -23.108 3.423   4.170   1.00 30.58 ? 184 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 184 ? -24.600 6.095   4.160   1.00 30.62 ? 184 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 184 ? -24.820 6.295   2.665   1.00 29.79 ? 184 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 184 ? -26.302 6.315   2.235   1.00 30.56 ? 184 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 184 ? -24.077 7.590   2.253   1.00 29.71 ? 184 LEU A CD2 1 
ATOM   1301 N  N   . LEU A 1 185 ? -25.105 2.952   3.126   1.00 27.20 ? 185 LEU A N   1 
ATOM   1302 C  CA  . LEU A 1 185 ? -24.583 1.825   2.397   1.00 28.50 ? 185 LEU A CA  1 
ATOM   1303 C  C   . LEU A 1 185 ? -24.532 2.218   0.922   1.00 27.69 ? 185 LEU A C   1 
ATOM   1304 O  O   . LEU A 1 185 ? -23.494 2.044   0.286   1.00 32.26 ? 185 LEU A O   1 
ATOM   1305 C  CB  . LEU A 1 185 ? -25.528 0.628   2.577   1.00 30.74 ? 185 LEU A CB  1 
ATOM   1306 C  CG  . LEU A 1 185 ? -25.072 -0.681  1.928   1.00 33.44 ? 185 LEU A CG  1 
ATOM   1307 C  CD1 . LEU A 1 185 ? -23.934 -1.348  2.797   1.00 31.01 ? 185 LEU A CD1 1 
ATOM   1308 C  CD2 . LEU A 1 185 ? -26.269 -1.728  1.809   1.00 31.61 ? 185 LEU A CD2 1 
ATOM   1309 N  N   . ILE A 1 186 ? -25.682 2.680   0.408   1.00 28.68 ? 186 ILE A N   1 
ATOM   1310 C  CA  . ILE A 1 186 ? -25.812 3.039   -1.032  1.00 28.24 ? 186 ILE A CA  1 
ATOM   1311 C  C   . ILE A 1 186 ? -26.556 4.371   -1.118  1.00 29.72 ? 186 ILE A C   1 
ATOM   1312 O  O   . ILE A 1 186 ? -27.598 4.541   -0.470  1.00 30.52 ? 186 ILE A O   1 
ATOM   1313 C  CB  . ILE A 1 186 ? -26.565 1.929   -1.814  1.00 32.89 ? 186 ILE A CB  1 
ATOM   1314 C  CG1 . ILE A 1 186 ? -25.676 0.686   -1.954  1.00 34.97 ? 186 ILE A CG1 1 
ATOM   1315 C  CG2 . ILE A 1 186 ? -27.033 2.394   -3.205  1.00 31.11 ? 186 ILE A CG2 1 
ATOM   1316 C  CD1 . ILE A 1 186 ? -26.390 -0.505  -2.542  1.00 40.22 ? 186 ILE A CD1 1 
ATOM   1317 N  N   . TYR A 1 187 ? -26.092 5.328   -1.956  1.00 30.63 ? 187 TYR A N   1 
ATOM   1318 C  CA  . TYR A 1 187 ? -26.864 6.567   -2.017  1.00 30.56 ? 187 TYR A CA  1 
ATOM   1319 C  C   . TYR A 1 187 ? -27.390 6.753   -3.436  1.00 30.75 ? 187 TYR A C   1 
ATOM   1320 O  O   . TYR A 1 187 ? -26.806 6.236   -4.396  1.00 32.31 ? 187 TYR A O   1 
ATOM   1321 C  CB  . TYR A 1 187 ? -26.054 7.799   -1.584  1.00 32.08 ? 187 TYR A CB  1 
ATOM   1322 C  CG  . TYR A 1 187 ? -24.784 8.045   -2.401  1.00 33.57 ? 187 TYR A CG  1 
ATOM   1323 C  CD1 . TYR A 1 187 ? -23.603 7.372   -2.095  1.00 36.57 ? 187 TYR A CD1 1 
ATOM   1324 C  CD2 . TYR A 1 187 ? -24.766 8.938   -3.472  1.00 35.50 ? 187 TYR A CD2 1 
ATOM   1325 C  CE1 . TYR A 1 187 ? -22.425 7.604   -2.785  1.00 41.81 ? 187 TYR A CE1 1 
ATOM   1326 C  CE2 . TYR A 1 187 ? -23.597 9.179   -4.185  1.00 35.98 ? 187 TYR A CE2 1 
ATOM   1327 C  CZ  . TYR A 1 187 ? -22.424 8.529   -3.819  1.00 42.40 ? 187 TYR A CZ  1 
ATOM   1328 O  OH  . TYR A 1 187 ? -21.258 8.660   -4.519  1.00 41.45 ? 187 TYR A OH  1 
ATOM   1329 N  N   . ALA A 1 188 ? -28.508 7.468   -3.521  1.00 31.20 ? 188 ALA A N   1 
ATOM   1330 C  CA  . ALA A 1 188 ? -29.109 7.774   -4.826  1.00 32.52 ? 188 ALA A CA  1 
ATOM   1331 C  C   . ALA A 1 188 ? -29.293 6.510   -5.673  1.00 36.67 ? 188 ALA A C   1 
ATOM   1332 O  O   . ALA A 1 188 ? -28.928 6.468   -6.859  1.00 33.45 ? 188 ALA A O   1 
ATOM   1333 C  CB  . ALA A 1 188 ? -28.344 8.880   -5.562  1.00 33.72 ? 188 ALA A CB  1 
ATOM   1334 N  N   . ALA A 1 189 ? -29.868 5.480   -5.052  1.00 34.02 ? 189 ALA A N   1 
ATOM   1335 C  CA  . ALA A 1 189 ? -30.286 4.221   -5.670  1.00 34.83 ? 189 ALA A CA  1 
ATOM   1336 C  C   . ALA A 1 189 ? -29.131 3.270   -5.980  1.00 31.52 ? 189 ALA A C   1 
ATOM   1337 O  O   . ALA A 1 189 ? -29.225 2.072   -5.710  1.00 34.27 ? 189 ALA A O   1 
ATOM   1338 C  CB  . ALA A 1 189 ? -31.267 4.377   -6.842  1.00 33.50 ? 189 ALA A CB  1 
ATOM   1339 N  N   . SER A 1 190 ? -28.038 3.768   -6.539  1.00 34.02 ? 190 SER A N   1 
ATOM   1340 C  CA  . SER A 1 190 ? -27.081 2.836   -7.104  1.00 30.52 ? 190 SER A CA  1 
ATOM   1341 C  C   . SER A 1 190 ? -25.617 3.168   -6.792  1.00 35.11 ? 190 SER A C   1 
ATOM   1342 O  O   . SER A 1 190 ? -24.757 2.423   -7.254  1.00 39.39 ? 190 SER A O   1 
ATOM   1343 C  CB  . SER A 1 190 ? -27.293 2.732   -8.610  1.00 35.61 ? 190 SER A CB  1 
ATOM   1344 O  OG  . SER A 1 190 ? -26.989 4.020   -9.134  1.00 35.95 ? 190 SER A OG  1 
ATOM   1345 N  N   . ASN A 1 191 ? -25.306 4.145   -5.909  1.00 34.94 ? 191 ASN A N   1 
ATOM   1346 C  CA  . ASN A 1 191 ? -23.904 4.502   -5.701  1.00 32.79 ? 191 ASN A CA  1 
ATOM   1347 C  C   . ASN A 1 191 ? -23.410 3.918   -4.387  1.00 33.58 ? 191 ASN A C   1 
ATOM   1348 O  O   . ASN A 1 191 ? -24.026 4.219   -3.357  1.00 35.41 ? 191 ASN A O   1 
ATOM   1349 C  CB  . ASN A 1 191 ? -23.763 6.033   -5.733  1.00 32.36 ? 191 ASN A CB  1 
ATOM   1350 C  CG  . ASN A 1 191 ? -24.216 6.603   -7.064  1.00 39.28 ? 191 ASN A CG  1 
ATOM   1351 O  OD1 . ASN A 1 191 ? -23.502 6.499   -8.073  1.00 44.11 ? 191 ASN A OD1 1 
ATOM   1352 N  ND2 . ASN A 1 191 ? -25.435 7.116   -7.127  1.00 39.91 ? 191 ASN A ND2 1 
ATOM   1353 N  N   . LEU A 1 192 ? -22.303 3.150   -4.411  1.00 34.70 ? 192 LEU A N   1 
ATOM   1354 C  CA  . LEU A 1 192 ? -21.759 2.641   -3.141  1.00 38.14 ? 192 LEU A CA  1 
ATOM   1355 C  C   . LEU A 1 192 ? -21.156 3.804   -2.362  1.00 39.21 ? 192 LEU A C   1 
ATOM   1356 O  O   . LEU A 1 192 ? -20.372 4.579   -2.906  1.00 36.49 ? 192 LEU A O   1 
ATOM   1357 C  CB  . LEU A 1 192 ? -20.706 1.533   -3.206  1.00 40.44 ? 192 LEU A CB  1 
ATOM   1358 C  CG  . LEU A 1 192 ? -21.084 0.274   -3.985  1.00 50.77 ? 192 LEU A CG  1 
ATOM   1359 C  CD1 . LEU A 1 192 ? -20.083 -0.840  -3.728  1.00 48.88 ? 192 LEU A CD1 1 
ATOM   1360 C  CD2 . LEU A 1 192 ? -22.487 -0.150  -3.590  1.00 55.47 ? 192 LEU A CD2 1 
ATOM   1361 N  N   . GLU A 1 193 ? -21.451 3.891   -1.057  1.00 33.62 ? 193 GLU A N   1 
ATOM   1362 C  CA  . GLU A 1 193 ? -20.741 4.851   -0.223  1.00 36.08 ? 193 GLU A CA  1 
ATOM   1363 C  C   . GLU A 1 193 ? -19.273 4.408   -0.131  1.00 36.83 ? 193 GLU A C   1 
ATOM   1364 O  O   . GLU A 1 193 ? -18.979 3.211   -0.245  1.00 35.87 ? 193 GLU A O   1 
ATOM   1365 C  CB  . GLU A 1 193 ? -21.529 4.880   1.105   1.00 33.45 ? 193 GLU A CB  1 
ATOM   1366 C  CG  . GLU A 1 193 ? -20.789 5.486   2.309   1.00 35.81 ? 193 GLU A CG  1 
ATOM   1367 C  CD  . GLU A 1 193 ? -20.472 6.993   2.282   1.00 44.63 ? 193 GLU A CD  1 
ATOM   1368 O  OE1 . GLU A 1 193 ? -20.119 7.486   1.191   1.00 44.64 ? 193 GLU A OE1 1 
ATOM   1369 O  OE2 . GLU A 1 193 ? -20.535 7.658   3.344   1.00 45.39 ? 193 GLU A OE2 1 
ATOM   1370 N  N   . SER A 1 194 ? -18.349 5.375   0.134   1.00 37.69 ? 194 SER A N   1 
ATOM   1371 C  CA  . SER A 1 194 ? -16.932 5.114   0.368   1.00 42.50 ? 194 SER A CA  1 
ATOM   1372 C  C   . SER A 1 194 ? -16.757 4.021   1.407   1.00 40.59 ? 194 SER A C   1 
ATOM   1373 O  O   . SER A 1 194 ? -17.384 4.051   2.479   1.00 38.69 ? 194 SER A O   1 
ATOM   1374 C  CB  . SER A 1 194 ? -16.176 6.356   0.868   1.00 44.66 ? 194 SER A CB  1 
ATOM   1375 O  OG  . SER A 1 194 ? -16.386 7.410   -0.051  1.00 57.22 ? 194 SER A OG  1 
ATOM   1376 N  N   . GLY A 1 195 ? -15.869 3.073   1.093   1.00 41.84 ? 195 GLY A N   1 
ATOM   1377 C  CA  . GLY A 1 195 ? -15.532 2.051   2.070   1.00 42.83 ? 195 GLY A CA  1 
ATOM   1378 C  C   . GLY A 1 195 ? -16.498 0.861   2.037   1.00 45.57 ? 195 GLY A C   1 
ATOM   1379 O  O   . GLY A 1 195 ? -16.281 -0.099  2.763   1.00 46.53 ? 195 GLY A O   1 
ATOM   1380 N  N   . ILE A 1 196 ? -17.582 0.935   1.253   1.00 41.54 ? 196 ILE A N   1 
ATOM   1381 C  CA  . ILE A 1 196 ? -18.525 -0.198  1.159   1.00 38.34 ? 196 ILE A CA  1 
ATOM   1382 C  C   . ILE A 1 196 ? -17.991 -1.167  0.104   1.00 43.69 ? 196 ILE A C   1 
ATOM   1383 O  O   . ILE A 1 196 ? -17.634 -0.757  -1.003  1.00 41.86 ? 196 ILE A O   1 
ATOM   1384 C  CB  . ILE A 1 196 ? -19.965 0.283   0.837   1.00 34.15 ? 196 ILE A CB  1 
ATOM   1385 C  CG1 . ILE A 1 196 ? -20.526 1.198   1.948   1.00 36.07 ? 196 ILE A CG1 1 
ATOM   1386 C  CG2 . ILE A 1 196 ? -20.920 -0.890  0.494   1.00 35.40 ? 196 ILE A CG2 1 
ATOM   1387 C  CD1 . ILE A 1 196 ? -20.462 0.616   3.353   1.00 37.59 ? 196 ILE A CD1 1 
ATOM   1388 N  N   . PRO A 1 197 ? -17.906 -2.480  0.407   1.00 42.13 ? 197 PRO A N   1 
ATOM   1389 C  CA  . PRO A 1 197 ? -17.404 -3.448  -0.571  1.00 39.52 ? 197 PRO A CA  1 
ATOM   1390 C  C   . PRO A 1 197 ? -18.251 -3.688  -1.809  1.00 44.04 ? 197 PRO A C   1 
ATOM   1391 O  O   . PRO A 1 197 ? -19.468 -3.541  -1.762  1.00 41.17 ? 197 PRO A O   1 
ATOM   1392 C  CB  . PRO A 1 197 ? -17.218 -4.762  0.239   1.00 42.15 ? 197 PRO A CB  1 
ATOM   1393 C  CG  . PRO A 1 197 ? -18.031 -4.560  1.504   1.00 44.15 ? 197 PRO A CG  1 
ATOM   1394 C  CD  . PRO A 1 197 ? -18.151 -3.061  1.746   1.00 39.24 ? 197 PRO A CD  1 
ATOM   1395 N  N   . ALA A 1 198 ? -17.570 -4.143  -2.864  1.00 41.61 ? 198 ALA A N   1 
ATOM   1396 C  CA  . ALA A 1 198 ? -18.140 -4.316  -4.185  1.00 43.37 ? 198 ALA A CA  1 
ATOM   1397 C  C   . ALA A 1 198 ? -19.206 -5.411  -4.219  1.00 42.93 ? 198 ALA A C   1 
ATOM   1398 O  O   . ALA A 1 198 ? -19.967 -5.471  -5.186  1.00 41.56 ? 198 ALA A O   1 
ATOM   1399 C  CB  . ALA A 1 198 ? -17.064 -4.603  -5.202  1.00 50.17 ? 198 ALA A CB  1 
ATOM   1400 N  N   . ARG A 1 199 ? -19.310 -6.247  -3.176  1.00 40.21 ? 199 ARG A N   1 
ATOM   1401 C  CA  . ARG A 1 199 ? -20.356 -7.267  -3.196  1.00 39.87 ? 199 ARG A CA  1 
ATOM   1402 C  C   . ARG A 1 199 ? -21.756 -6.669  -3.005  1.00 38.32 ? 199 ARG A C   1 
ATOM   1403 O  O   . ARG A 1 199 ? -22.744 -7.361  -3.274  1.00 38.19 ? 199 ARG A O   1 
ATOM   1404 C  CB  . ARG A 1 199 ? -20.104 -8.426  -2.235  1.00 36.00 ? 199 ARG A CB  1 
ATOM   1405 C  CG  . ARG A 1 199 ? -19.861 -7.834  -0.857  1.00 37.26 ? 199 ARG A CG  1 
ATOM   1406 C  CD  . ARG A 1 199 ? -19.554 -9.036  0.013   1.00 42.00 ? 199 ARG A CD  1 
ATOM   1407 N  NE  . ARG A 1 199 ? -19.582 -8.717  1.442   1.00 41.62 ? 199 ARG A NE  1 
ATOM   1408 C  CZ  . ARG A 1 199 ? -18.577 -8.182  2.093   1.00 42.87 ? 199 ARG A CZ  1 
ATOM   1409 N  NH1 . ARG A 1 199 ? -17.412 -8.013  1.492   1.00 41.69 ? 199 ARG A NH1 1 
ATOM   1410 N  NH2 . ARG A 1 199 ? -18.705 -7.857  3.368   1.00 43.59 ? 199 ARG A NH2 1 
ATOM   1411 N  N   . PHE A 1 200 ? -21.863 -5.387  -2.614  1.00 35.00 ? 200 PHE A N   1 
ATOM   1412 C  CA  . PHE A 1 200 ? -23.178 -4.769  -2.565  1.00 33.56 ? 200 PHE A CA  1 
ATOM   1413 C  C   . PHE A 1 200 ? -23.453 -4.019  -3.858  1.00 35.69 ? 200 PHE A C   1 
ATOM   1414 O  O   . PHE A 1 200 ? -22.552 -3.392  -4.423  1.00 38.31 ? 200 PHE A O   1 
ATOM   1415 C  CB  . PHE A 1 200 ? -23.172 -3.705  -1.478  1.00 31.52 ? 200 PHE A CB  1 
ATOM   1416 C  CG  . PHE A 1 200 ? -23.115 -4.311  -0.099  1.00 36.50 ? 200 PHE A CG  1 
ATOM   1417 C  CD1 . PHE A 1 200 ? -21.894 -4.633  0.490   1.00 38.93 ? 200 PHE A CD1 1 
ATOM   1418 C  CD2 . PHE A 1 200 ? -24.287 -4.581  0.588   1.00 36.11 ? 200 PHE A CD2 1 
ATOM   1419 C  CE1 . PHE A 1 200 ? -21.837 -5.169  1.770   1.00 36.82 ? 200 PHE A CE1 1 
ATOM   1420 C  CE2 . PHE A 1 200 ? -24.231 -5.126  1.845   1.00 33.47 ? 200 PHE A CE2 1 
ATOM   1421 C  CZ  . PHE A 1 200 ? -23.014 -5.420  2.452   1.00 35.07 ? 200 PHE A CZ  1 
ATOM   1422 N  N   . SER A 1 201 ? -24.717 -4.025  -4.312  1.00 36.07 ? 201 SER A N   1 
ATOM   1423 C  CA  . SER A 1 201 ? -25.089 -3.201  -5.443  1.00 35.24 ? 201 SER A CA  1 
ATOM   1424 C  C   . SER A 1 201 ? -26.556 -2.797  -5.331  1.00 38.14 ? 201 SER A C   1 
ATOM   1425 O  O   . SER A 1 201 ? -27.354 -3.463  -4.672  1.00 36.38 ? 201 SER A O   1 
ATOM   1426 C  CB  . SER A 1 201 ? -24.847 -3.867  -6.766  1.00 37.18 ? 201 SER A CB  1 
ATOM   1427 O  OG  . SER A 1 201 ? -25.696 -5.006  -6.826  1.00 44.03 ? 201 SER A OG  1 
ATOM   1428 N  N   . GLY A 1 202 ? -26.885 -1.659  -5.928  1.00 32.09 ? 202 GLY A N   1 
ATOM   1429 C  CA  . GLY A 1 202 ? -28.261 -1.181  -5.836  1.00 31.65 ? 202 GLY A CA  1 
ATOM   1430 C  C   . GLY A 1 202 ? -28.740 -0.829  -7.236  1.00 34.08 ? 202 GLY A C   1 
ATOM   1431 O  O   . GLY A 1 202 ? -27.911 -0.448  -8.039  1.00 32.62 ? 202 GLY A O   1 
ATOM   1432 N  N   . SER A 1 203 ? -30.047 -0.976  -7.478  1.00 31.46 ? 203 SER A N   1 
ATOM   1433 C  CA  . SER A 1 203 ? -30.613 -0.650  -8.768  1.00 34.83 ? 203 SER A CA  1 
ATOM   1434 C  C   . SER A 1 203 ? -31.991 -0.047  -8.517  1.00 36.66 ? 203 SER A C   1 
ATOM   1435 O  O   . SER A 1 203 ? -32.536 -0.074  -7.386  1.00 33.36 ? 203 SER A O   1 
ATOM   1436 C  CB  . SER A 1 203 ? -30.658 -1.922  -9.637  1.00 37.76 ? 203 SER A CB  1 
ATOM   1437 O  OG  . SER A 1 203 ? -31.654 -2.840  -9.186  1.00 36.81 ? 203 SER A OG  1 
ATOM   1438 N  N   . GLY A 1 204 ? -32.612 0.451   -9.584  1.00 33.92 ? 204 GLY A N   1 
ATOM   1439 C  CA  . GLY A 1 204 ? -33.986 0.917   -9.479  1.00 35.31 ? 204 GLY A CA  1 
ATOM   1440 C  C   . GLY A 1 204 ? -34.141 2.379   -9.910  1.00 35.60 ? 204 GLY A C   1 
ATOM   1441 O  O   . GLY A 1 204 ? -33.161 3.103   -10.138 1.00 35.91 ? 204 GLY A O   1 
ATOM   1442 N  N   . SER A 1 205 ? -35.400 2.781   -10.102 1.00 36.22 ? 205 SER A N   1 
ATOM   1443 C  CA  . SER A 1 205 ? -35.728 4.167   -10.399 1.00 42.08 ? 205 SER A CA  1 
ATOM   1444 C  C   . SER A 1 205 ? -37.220 4.302   -10.150 1.00 38.73 ? 205 SER A C   1 
ATOM   1445 O  O   . SER A 1 205 ? -37.902 3.296   -10.039 1.00 39.67 ? 205 SER A O   1 
ATOM   1446 C  CB  . SER A 1 205 ? -35.449 4.488   -11.871 1.00 41.86 ? 205 SER A CB  1 
ATOM   1447 O  OG  . SER A 1 205 ? -36.271 3.625   -12.636 1.00 44.02 ? 205 SER A OG  1 
ATOM   1448 N  N   . GLY A 1 206 ? -37.696 5.550   -10.064 1.00 40.30 ? 206 GLY A N   1 
ATOM   1449 C  CA  . GLY A 1 206 ? -39.120 5.784   -9.968  1.00 41.60 ? 206 GLY A CA  1 
ATOM   1450 C  C   . GLY A 1 206 ? -39.634 5.356   -8.596  1.00 40.64 ? 206 GLY A C   1 
ATOM   1451 O  O   . GLY A 1 206 ? -39.386 6.052   -7.634  1.00 39.50 ? 206 GLY A O   1 
ATOM   1452 N  N   . THR A 1 207 ? -40.385 4.240   -8.551  1.00 39.10 ? 207 THR A N   1 
ATOM   1453 C  CA  . THR A 1 207 ? -40.936 3.722   -7.295  1.00 36.65 ? 207 THR A CA  1 
ATOM   1454 C  C   . THR A 1 207 ? -40.340 2.365   -6.891  1.00 38.00 ? 207 THR A C   1 
ATOM   1455 O  O   . THR A 1 207 ? -40.787 1.836   -5.890  1.00 43.07 ? 207 THR A O   1 
ATOM   1456 C  CB  . THR A 1 207 ? -42.465 3.583   -7.387  1.00 42.37 ? 207 THR A CB  1 
ATOM   1457 O  OG1 . THR A 1 207 ? -42.731 2.733   -8.513  1.00 42.56 ? 207 THR A OG1 1 
ATOM   1458 C  CG2 . THR A 1 207 ? -43.199 4.892   -7.614  1.00 40.90 ? 207 THR A CG2 1 
ATOM   1459 N  N   . ASP A 1 208 ? -39.460 1.737   -7.690  1.00 35.11 ? 208 ASP A N   1 
ATOM   1460 C  CA  . ASP A 1 208 ? -39.023 0.357   -7.481  1.00 35.89 ? 208 ASP A CA  1 
ATOM   1461 C  C   . ASP A 1 208 ? -37.503 0.271   -7.418  1.00 35.65 ? 208 ASP A C   1 
ATOM   1462 O  O   . ASP A 1 208 ? -36.793 0.646   -8.365  1.00 34.96 ? 208 ASP A O   1 
ATOM   1463 C  CB  . ASP A 1 208 ? -39.525 -0.578  -8.578  1.00 38.96 ? 208 ASP A CB  1 
ATOM   1464 C  CG  . ASP A 1 208 ? -41.035 -0.693  -8.645  0.70 40.69 ? 208 ASP A CG  1 
ATOM   1465 O  OD1 . ASP A 1 208 ? -41.611 -1.320  -7.768  0.70 50.55 ? 208 ASP A OD1 1 
ATOM   1466 O  OD2 . ASP A 1 208 ? -41.615 -0.152  -9.570  0.70 52.10 ? 208 ASP A OD2 1 
ATOM   1467 N  N   . PHE A 1 209 ? -36.993 -0.240  -6.272  1.00 30.99 ? 209 PHE A N   1 
ATOM   1468 C  CA  . PHE A 1 209 ? -35.546 -0.259  -6.042  1.00 29.91 ? 209 PHE A CA  1 
ATOM   1469 C  C   . PHE A 1 209 ? -35.184 -1.641  -5.473  1.00 33.54 ? 209 PHE A C   1 
ATOM   1470 O  O   . PHE A 1 209 ? -36.036 -2.284  -4.829  1.00 33.97 ? 209 PHE A O   1 
ATOM   1471 C  CB  . PHE A 1 209 ? -35.167 0.821   -5.002  1.00 31.33 ? 209 PHE A CB  1 
ATOM   1472 C  CG  . PHE A 1 209 ? -35.506 2.192   -5.562  1.00 29.99 ? 209 PHE A CG  1 
ATOM   1473 C  CD1 . PHE A 1 209 ? -34.593 2.849   -6.400  1.00 30.23 ? 209 PHE A CD1 1 
ATOM   1474 C  CD2 . PHE A 1 209 ? -36.772 2.758   -5.367  1.00 32.59 ? 209 PHE A CD2 1 
ATOM   1475 C  CE1 . PHE A 1 209 ? -34.934 4.090   -6.983  1.00 32.63 ? 209 PHE A CE1 1 
ATOM   1476 C  CE2 . PHE A 1 209 ? -37.118 3.984   -5.974  1.00 33.25 ? 209 PHE A CE2 1 
ATOM   1477 C  CZ  . PHE A 1 209 ? -36.188 4.638   -6.776  1.00 32.32 ? 209 PHE A CZ  1 
ATOM   1478 N  N   . THR A 1 210 ? -33.938 -2.095  -5.705  1.00 32.69 ? 210 THR A N   1 
ATOM   1479 C  CA  . THR A 1 210 ? -33.505 -3.429  -5.270  1.00 32.80 ? 210 THR A CA  1 
ATOM   1480 C  C   . THR A 1 210 ? -32.090 -3.351  -4.716  1.00 35.52 ? 210 THR A C   1 
ATOM   1481 O  O   . THR A 1 210 ? -31.211 -2.786  -5.371  1.00 33.18 ? 210 THR A O   1 
ATOM   1482 C  CB  . THR A 1 210 ? -33.498 -4.400  -6.456  1.00 35.87 ? 210 THR A CB  1 
ATOM   1483 O  OG1 . THR A 1 210 ? -34.811 -4.354  -6.991  1.00 32.81 ? 210 THR A OG1 1 
ATOM   1484 C  CG2 . THR A 1 210 ? -33.250 -5.842  -6.024  1.00 36.21 ? 210 THR A CG2 1 
ATOM   1485 N  N   . LEU A 1 211 ? -31.850 -3.926  -3.523  1.00 30.36 ? 211 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 211 ? -30.497 -4.108  -3.035  1.00 29.17 ? 211 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 211 ? -30.082 -5.556  -3.292  1.00 30.25 ? 211 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 211 ? -30.829 -6.493  -2.987  1.00 30.81 ? 211 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 211 ? -30.512 -3.788  -1.526  1.00 27.09 ? 211 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 211 ? -29.194 -4.061  -0.802  1.00 32.79 ? 211 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 211 ? -28.054 -3.116  -1.228  1.00 33.18 ? 211 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 211 ? -29.484 -3.865  0.689   1.00 32.06 ? 211 LEU A CD2 1 
ATOM   1493 N  N   . ASN A 1 212 ? -28.838 -5.743  -3.756  1.00 31.80 ? 212 ASN A N   1 
ATOM   1494 C  CA  . ASN A 1 212 ? -28.244 -7.058  -3.988  1.00 33.47 ? 212 ASN A CA  1 
ATOM   1495 C  C   . ASN A 1 212 ? -26.933 -7.158  -3.228  1.00 36.61 ? 212 ASN A C   1 
ATOM   1496 O  O   . ASN A 1 212 ? -26.151 -6.207  -3.198  1.00 35.16 ? 212 ASN A O   1 
ATOM   1497 C  CB  . ASN A 1 212 ? -28.023 -7.341  -5.487  1.00 28.10 ? 212 ASN A CB  1 
ATOM   1498 C  CG  . ASN A 1 212 ? -29.223 -8.083  -6.045  1.00 33.88 ? 212 ASN A CG  1 
ATOM   1499 O  OD1 . ASN A 1 212 ? -29.305 -9.304  -5.855  1.00 35.16 ? 212 ASN A OD1 1 
ATOM   1500 N  ND2 . ASN A 1 212 ? -30.133 -7.410  -6.749  1.00 31.48 ? 212 ASN A ND2 1 
ATOM   1501 N  N   . ILE A 1 213 ? -26.718 -8.325  -2.623  1.00 35.46 ? 213 ILE A N   1 
ATOM   1502 C  CA  . ILE A 1 213 ? -25.469 -8.620  -1.941  1.00 34.49 ? 213 ILE A CA  1 
ATOM   1503 C  C   . ILE A 1 213 ? -25.054 -10.019 -2.388  1.00 35.02 ? 213 ILE A C   1 
ATOM   1504 O  O   . ILE A 1 213 ? -25.821 -10.976 -2.184  1.00 31.86 ? 213 ILE A O   1 
ATOM   1505 C  CB  . ILE A 1 213 ? -25.677 -8.618  -0.409  1.00 32.47 ? 213 ILE A CB  1 
ATOM   1506 C  CG1 . ILE A 1 213 ? -26.553 -7.473  0.084   1.00 32.79 ? 213 ILE A CG1 1 
ATOM   1507 C  CG2 . ILE A 1 213 ? -24.343 -8.744  0.336   1.00 36.86 ? 213 ILE A CG2 1 
ATOM   1508 C  CD1 . ILE A 1 213 ? -26.915 -7.599  1.559   1.00 35.74 ? 213 ILE A CD1 1 
ATOM   1509 N  N   . HIS A 1 214 ? -23.871 -10.128 -3.018  1.00 35.70 ? 214 HIS A N   1 
ATOM   1510 C  CA  . HIS A 1 214 ? -23.388 -11.425 -3.485  1.00 40.21 ? 214 HIS A CA  1 
ATOM   1511 C  C   . HIS A 1 214 ? -21.890 -11.327 -3.750  1.00 41.91 ? 214 HIS A C   1 
ATOM   1512 O  O   . HIS A 1 214 ? -21.467 -10.382 -4.414  1.00 41.90 ? 214 HIS A O   1 
ATOM   1513 C  CB  . HIS A 1 214 ? -24.052 -11.842 -4.808  1.00 37.75 ? 214 HIS A CB  1 
ATOM   1514 C  CG  . HIS A 1 214 ? -23.463 -13.115 -5.359  1.00 45.74 ? 214 HIS A CG  1 
ATOM   1515 N  ND1 . HIS A 1 214 ? -22.421 -13.139 -6.274  1.00 43.70 ? 214 HIS A ND1 1 
ATOM   1516 C  CD2 . HIS A 1 214 ? -23.735 -14.422 -5.074  1.00 45.96 ? 214 HIS A CD2 1 
ATOM   1517 C  CE1 . HIS A 1 214 ? -22.074 -14.410 -6.516  1.00 46.02 ? 214 HIS A CE1 1 
ATOM   1518 N  NE2 . HIS A 1 214 ? -22.883 -15.197 -5.835  1.00 46.08 ? 214 HIS A NE2 1 
ATOM   1519 N  N   . PRO A 1 215 ? -21.040 -12.265 -3.239  1.00 45.52 ? 215 PRO A N   1 
ATOM   1520 C  CA  . PRO A 1 215 ? -21.465 -13.343 -2.320  1.00 41.88 ? 215 PRO A CA  1 
ATOM   1521 C  C   . PRO A 1 215 ? -21.575 -12.851 -0.868  1.00 41.21 ? 215 PRO A C   1 
ATOM   1522 O  O   . PRO A 1 215 ? -20.687 -12.128 -0.401  1.00 44.16 ? 215 PRO A O   1 
ATOM   1523 C  CB  . PRO A 1 215 ? -20.302 -14.407 -2.447  1.00 42.19 ? 215 PRO A CB  1 
ATOM   1524 C  CG  . PRO A 1 215 ? -19.469 -13.924 -3.640  1.00 51.48 ? 215 PRO A CG  1 
ATOM   1525 C  CD  . PRO A 1 215 ? -19.616 -12.388 -3.620  1.00 46.57 ? 215 PRO A CD  1 
ATOM   1526 N  N   . VAL A 1 216 ? -22.636 -13.255 -0.166  1.00 38.00 ? 216 VAL A N   1 
ATOM   1527 C  CA  . VAL A 1 216 ? -22.834 -12.805 1.202   1.00 38.88 ? 216 VAL A CA  1 
ATOM   1528 C  C   . VAL A 1 216 ? -21.695 -13.364 2.055   1.00 41.18 ? 216 VAL A C   1 
ATOM   1529 O  O   . VAL A 1 216 ? -21.268 -14.517 1.871   1.00 39.71 ? 216 VAL A O   1 
ATOM   1530 C  CB  . VAL A 1 216 ? -24.192 -13.350 1.661   1.00 41.66 ? 216 VAL A CB  1 
ATOM   1531 C  CG1 . VAL A 1 216 ? -24.296 -13.346 3.175   1.00 47.59 ? 216 VAL A CG1 1 
ATOM   1532 C  CG2 . VAL A 1 216 ? -25.311 -12.508 1.081   1.00 40.77 ? 216 VAL A CG2 1 
ATOM   1533 N  N   . GLU A 1 217 ? -21.230 -12.549 3.010   1.00 39.69 ? 217 GLU A N   1 
ATOM   1534 C  CA  . GLU A 1 217 ? -20.277 -12.970 4.025   1.00 41.50 ? 217 GLU A CA  1 
ATOM   1535 C  C   . GLU A 1 217 ? -20.883 -12.766 5.405   1.00 42.74 ? 217 GLU A C   1 
ATOM   1536 O  O   . GLU A 1 217 ? -21.871 -12.051 5.538   1.00 36.93 ? 217 GLU A O   1 
ATOM   1537 C  CB  . GLU A 1 217 ? -19.111 -11.997 3.942   1.00 46.04 ? 217 GLU A CB  1 
ATOM   1538 C  CG  . GLU A 1 217 ? -18.309 -12.172 2.661   1.00 49.17 ? 217 GLU A CG  1 
ATOM   1539 C  CD  . GLU A 1 217 ? -16.988 -11.423 2.627   1.00 54.05 ? 217 GLU A CD  1 
ATOM   1540 O  OE1 . GLU A 1 217 ? -16.513 -10.831 3.632   1.00 64.69 ? 217 GLU A OE1 1 
ATOM   1541 O  OE2 . GLU A 1 217 ? -16.429 -11.467 1.517   1.00 56.00 ? 217 GLU A OE2 1 
ATOM   1542 N  N   . GLU A 1 218 ? -20.314 -13.433 6.404   1.00 42.08 ? 218 GLU A N   1 
ATOM   1543 C  CA  A GLU A 1 218 ? -20.801 -13.200 7.797   0.50 45.68 ? 218 GLU A CA  1 
ATOM   1544 C  CA  B GLU A 1 218 ? -20.817 -13.266 7.783   0.50 46.80 ? 218 GLU A CA  1 
ATOM   1545 C  C   . GLU A 1 218 ? -20.957 -11.725 8.320   1.00 42.70 ? 218 GLU A C   1 
ATOM   1546 O  O   . GLU A 1 218 ? -21.893 -11.188 9.062   1.00 43.66 ? 218 GLU A O   1 
ATOM   1547 C  CB  A GLU A 1 218 ? -19.885 -13.920 8.787   0.50 45.20 ? 218 GLU A CB  1 
ATOM   1548 C  CB  B GLU A 1 218 ? -20.230 -14.267 8.795   0.50 50.00 ? 218 GLU A CB  1 
ATOM   1549 C  CG  A GLU A 1 218 ? -19.788 -15.423 8.552   0.50 51.60 ? 218 GLU A CG  1 
ATOM   1550 C  CG  B GLU A 1 218 ? -21.016 -14.355 10.105  0.50 59.81 ? 218 GLU A CG  1 
ATOM   1551 C  CD  A GLU A 1 218 ? -18.578 -16.039 9.228   0.50 55.09 ? 218 GLU A CD  1 
ATOM   1552 C  CD  B GLU A 1 218 ? -21.160 -15.727 10.757  0.50 63.97 ? 218 GLU A CD  1 
ATOM   1553 O  OE1 A GLU A 1 218 ? -18.250 -15.597 10.349  0.50 53.65 ? 218 GLU A OE1 1 
ATOM   1554 O  OE1 B GLU A 1 218 ? -22.301 -16.223 10.956  0.50 60.18 ? 218 GLU A OE1 1 
ATOM   1555 O  OE2 A GLU A 1 218 ? -17.963 -16.952 8.639   0.50 54.33 ? 218 GLU A OE2 1 
ATOM   1556 O  OE2 B GLU A 1 218 ? -20.099 -16.305 11.075  0.50 64.96 ? 218 GLU A OE2 1 
ATOM   1557 N  N   . GLU A 1 219 ? -19.995 -10.933 7.842   1.00 43.53 ? 219 GLU A N   1 
ATOM   1558 C  CA  A GLU A 1 219 ? -20.079 -9.527  8.239   0.50 41.30 ? 219 GLU A CA  1 
ATOM   1559 C  CA  B GLU A 1 219 ? -20.033 -9.506  8.167   0.50 43.00 ? 219 GLU A CA  1 
ATOM   1560 C  C   . GLU A 1 219 ? -21.328 -8.853  7.652   1.00 40.63 ? 219 GLU A C   1 
ATOM   1561 O  O   . GLU A 1 219 ? -21.710 -7.779  8.098   1.00 40.43 ? 219 GLU A O   1 
ATOM   1562 C  CB  A GLU A 1 219 ? -18.847 -8.680  7.888   0.50 45.48 ? 219 GLU A CB  1 
ATOM   1563 C  CB  B GLU A 1 219 ? -18.726 -8.735  7.877   0.50 49.70 ? 219 GLU A CB  1 
ATOM   1564 C  CG  A GLU A 1 219 ? -17.798 -8.539  9.001   0.50 45.23 ? 219 GLU A CG  1 
ATOM   1565 C  CG  B GLU A 1 219 ? -18.208 -8.648  6.435   0.50 53.06 ? 219 GLU A CG  1 
ATOM   1566 C  CD  A GLU A 1 219 ? -17.990 -7.613  10.197  0.50 47.00 ? 219 GLU A CD  1 
ATOM   1567 C  CD  B GLU A 1 219 ? -16.839 -8.015  6.089   0.50 58.21 ? 219 GLU A CD  1 
ATOM   1568 O  OE1 A GLU A 1 219 ? -17.969 -8.173  11.318  0.50 50.98 ? 219 GLU A OE1 1 
ATOM   1569 O  OE1 B GLU A 1 219 ? -16.707 -6.961  5.378   0.50 48.34 ? 219 GLU A OE1 1 
ATOM   1570 O  OE2 A GLU A 1 219 ? -18.116 -6.370  10.060  0.50 42.77 ? 219 GLU A OE2 1 
ATOM   1571 O  OE2 B GLU A 1 219 ? -15.839 -8.634  6.517   0.50 62.46 ? 219 GLU A OE2 1 
ATOM   1572 N  N   . ASP A 1 220 ? -22.026 -9.478  6.691   1.00 41.18 ? 220 ASP A N   1 
ATOM   1573 C  CA  . ASP A 1 220 ? -23.168 -8.815  6.057   1.00 35.07 ? 220 ASP A CA  1 
ATOM   1574 C  C   . ASP A 1 220 ? -24.459 -8.961  6.860   1.00 34.77 ? 220 ASP A C   1 
ATOM   1575 O  O   . ASP A 1 220 ? -25.496 -8.348  6.544   1.00 34.41 ? 220 ASP A O   1 
ATOM   1576 C  CB  . ASP A 1 220 ? -23.324 -9.312  4.622   1.00 34.02 ? 220 ASP A CB  1 
ATOM   1577 C  CG  . ASP A 1 220 ? -22.074 -9.048  3.803   1.00 42.67 ? 220 ASP A CG  1 
ATOM   1578 O  OD1 . ASP A 1 220 ? -21.339 -8.070  4.157   1.00 43.26 ? 220 ASP A OD1 1 
ATOM   1579 O  OD2 . ASP A 1 220 ? -21.802 -9.809  2.820   1.00 43.29 ? 220 ASP A OD2 1 
ATOM   1580 N  N   . ALA A 1 221 ? -24.438 -9.776  7.932   1.00 36.52 ? 221 ALA A N   1 
ATOM   1581 C  CA  . ALA A 1 221 ? -25.627 -9.903  8.771   1.00 35.03 ? 221 ALA A CA  1 
ATOM   1582 C  C   . ALA A 1 221 ? -25.957 -8.557  9.435   1.00 37.64 ? 221 ALA A C   1 
ATOM   1583 O  O   . ALA A 1 221 ? -25.120 -7.965  10.136  1.00 38.89 ? 221 ALA A O   1 
ATOM   1584 C  CB  . ALA A 1 221 ? -25.449 -10.987 9.828   1.00 39.24 ? 221 ALA A CB  1 
ATOM   1585 N  N   . ALA A 1 222 ? -27.166 -8.054  9.213   1.00 33.61 ? 222 ALA A N   1 
ATOM   1586 C  CA  . ALA A 1 222 ? -27.474 -6.665  9.559   1.00 32.54 ? 222 ALA A CA  1 
ATOM   1587 C  C   . ALA A 1 222 ? -28.953 -6.452  9.279   1.00 33.90 ? 222 ALA A C   1 
ATOM   1588 O  O   . ALA A 1 222 ? -29.583 -7.301  8.620   1.00 34.14 ? 222 ALA A O   1 
ATOM   1589 C  CB  . ALA A 1 222 ? -26.611 -5.692  8.697   1.00 32.25 ? 222 ALA A CB  1 
ATOM   1590 N  N   . THR A 1 223 ? -29.479 -5.298  9.705   1.00 32.77 ? 223 THR A N   1 
ATOM   1591 C  CA  . THR A 1 223 ? -30.792 -4.863  9.259   1.00 33.43 ? 223 THR A CA  1 
ATOM   1592 C  C   . THR A 1 223 ? -30.576 -3.750  8.243   1.00 30.39 ? 223 THR A C   1 
ATOM   1593 O  O   . THR A 1 223 ? -29.756 -2.844  8.475   1.00 30.11 ? 223 THR A O   1 
ATOM   1594 C  CB  . THR A 1 223 ? -31.605 -4.363  10.447  1.00 35.71 ? 223 THR A CB  1 
ATOM   1595 O  OG1 . THR A 1 223 ? -31.799 -5.495  11.298  1.00 37.39 ? 223 THR A OG1 1 
ATOM   1596 C  CG2 . THR A 1 223 ? -32.942 -3.815  9.986   1.00 31.60 ? 223 THR A CG2 1 
ATOM   1597 N  N   . TYR A 1 224 ? -31.257 -3.877  7.088   1.00 29.25 ? 224 TYR A N   1 
ATOM   1598 C  CA  . TYR A 1 224 ? -31.139 -2.942  5.982   1.00 28.64 ? 224 TYR A CA  1 
ATOM   1599 C  C   . TYR A 1 224 ? -32.426 -2.111  5.892   1.00 28.12 ? 224 TYR A C   1 
ATOM   1600 O  O   . TYR A 1 224 ? -33.527 -2.670  5.892   1.00 28.97 ? 224 TYR A O   1 
ATOM   1601 C  CB  . TYR A 1 224 ? -30.896 -3.723  4.668   1.00 30.43 ? 224 TYR A CB  1 
ATOM   1602 C  CG  . TYR A 1 224 ? -29.545 -4.439  4.725   1.00 28.57 ? 224 TYR A CG  1 
ATOM   1603 C  CD1 . TYR A 1 224 ? -28.384 -3.804  4.286   1.00 29.88 ? 224 TYR A CD1 1 
ATOM   1604 C  CD2 . TYR A 1 224 ? -29.423 -5.707  5.338   1.00 29.45 ? 224 TYR A CD2 1 
ATOM   1605 C  CE1 . TYR A 1 224 ? -27.145 -4.422  4.350   1.00 31.12 ? 224 TYR A CE1 1 
ATOM   1606 C  CE2 . TYR A 1 224 ? -28.180 -6.341  5.390   1.00 30.40 ? 224 TYR A CE2 1 
ATOM   1607 C  CZ  . TYR A 1 224 ? -27.043 -5.702  4.895   1.00 32.44 ? 224 TYR A CZ  1 
ATOM   1608 O  OH  . TYR A 1 224 ? -25.800 -6.277  4.949   1.00 31.29 ? 224 TYR A OH  1 
ATOM   1609 N  N   . TYR A 1 225 ? -32.288 -0.771  5.738   1.00 28.21 ? 225 TYR A N   1 
ATOM   1610 C  CA  . TYR A 1 225 ? -33.414 0.132   5.622   1.00 28.40 ? 225 TYR A CA  1 
ATOM   1611 C  C   . TYR A 1 225 ? -33.253 0.962   4.342   1.00 30.00 ? 225 TYR A C   1 
ATOM   1612 O  O   . TYR A 1 225 ? -32.157 1.441   4.068   1.00 30.63 ? 225 TYR A O   1 
ATOM   1613 C  CB  . TYR A 1 225 ? -33.518 1.154   6.760   1.00 30.38 ? 225 TYR A CB  1 
ATOM   1614 C  CG  . TYR A 1 225 ? -33.725 0.560   8.156   1.00 30.35 ? 225 TYR A CG  1 
ATOM   1615 C  CD1 . TYR A 1 225 ? -35.000 0.181   8.620   1.00 28.70 ? 225 TYR A CD1 1 
ATOM   1616 C  CD2 . TYR A 1 225 ? -32.623 0.385   8.991   1.00 31.90 ? 225 TYR A CD2 1 
ATOM   1617 C  CE1 . TYR A 1 225 ? -35.179 -0.322  9.916   1.00 29.17 ? 225 TYR A CE1 1 
ATOM   1618 C  CE2 . TYR A 1 225 ? -32.789 -0.121  10.281  1.00 30.91 ? 225 TYR A CE2 1 
ATOM   1619 C  CZ  . TYR A 1 225 ? -34.060 -0.458  10.725  1.00 30.92 ? 225 TYR A CZ  1 
ATOM   1620 O  OH  . TYR A 1 225 ? -34.141 -0.893  12.032  1.00 31.84 ? 225 TYR A OH  1 
ATOM   1621 N  N   . CYS A 1 226 ? -34.361 1.152   3.589   1.00 31.04 ? 226 CYS A N   1 
ATOM   1622 C  CA  . CYS A 1 226 ? -34.335 2.108   2.495   1.00 30.44 ? 226 CYS A CA  1 
ATOM   1623 C  C   . CYS A 1 226 ? -34.892 3.404   3.076   1.00 31.18 ? 226 CYS A C   1 
ATOM   1624 O  O   . CYS A 1 226 ? -35.577 3.412   4.114   1.00 30.05 ? 226 CYS A O   1 
ATOM   1625 C  CB  . CYS A 1 226 ? -35.147 1.525   1.337   1.00 31.29 ? 226 CYS A CB  1 
ATOM   1626 S  SG  . CYS A 1 226 ? -36.897 1.231   1.734   1.00 36.97 ? 226 CYS A SG  1 
ATOM   1627 N  N   . GLN A 1 227 ? -34.605 4.514   2.393   1.00 30.87 ? 227 GLN A N   1 
ATOM   1628 C  CA  . GLN A 1 227 ? -35.065 5.815   2.840   1.00 29.69 ? 227 GLN A CA  1 
ATOM   1629 C  C   . GLN A 1 227 ? -35.295 6.666   1.579   1.00 31.00 ? 227 GLN A C   1 
ATOM   1630 O  O   . GLN A 1 227 ? -34.500 6.581   0.638   1.00 32.57 ? 227 GLN A O   1 
ATOM   1631 C  CB  . GLN A 1 227 ? -33.894 6.483   3.576   1.00 28.69 ? 227 GLN A CB  1 
ATOM   1632 C  CG  . GLN A 1 227 ? -34.235 7.887   4.044   1.00 31.13 ? 227 GLN A CG  1 
ATOM   1633 C  CD  . GLN A 1 227 ? -33.508 8.992   3.267   1.00 37.40 ? 227 GLN A CD  1 
ATOM   1634 O  OE1 . GLN A 1 227 ? -33.251 10.033  3.859   1.00 37.70 ? 227 GLN A OE1 1 
ATOM   1635 N  NE2 . GLN A 1 227 ? -33.235 8.878   1.955   1.00 35.89 ? 227 GLN A NE2 1 
ATOM   1636 N  N   . GLN A 1 228 ? -36.352 7.485   1.581   1.00 31.00 ? 228 GLN A N   1 
ATOM   1637 C  CA  . GLN A 1 228 ? -36.461 8.485   0.517   1.00 30.18 ? 228 GLN A CA  1 
ATOM   1638 C  C   . GLN A 1 228 ? -36.305 9.887   1.066   1.00 32.51 ? 228 GLN A C   1 
ATOM   1639 O  O   . GLN A 1 228 ? -36.728 10.194  2.175   1.00 29.62 ? 228 GLN A O   1 
ATOM   1640 C  CB  . GLN A 1 228 ? -37.787 8.413   -0.252  1.00 31.13 ? 228 GLN A CB  1 
ATOM   1641 C  CG  . GLN A 1 228 ? -39.041 8.740   0.574   1.00 33.37 ? 228 GLN A CG  1 
ATOM   1642 C  CD  . GLN A 1 228 ? -39.367 10.224  0.642   1.00 33.29 ? 228 GLN A CD  1 
ATOM   1643 O  OE1 . GLN A 1 228 ? -38.994 10.984  -0.241  1.00 35.61 ? 228 GLN A OE1 1 
ATOM   1644 N  NE2 . GLN A 1 228 ? -40.027 10.698  1.683   1.00 33.40 ? 228 GLN A NE2 1 
ATOM   1645 N  N   . ASN A 1 229 ? -35.768 10.785  0.239   1.00 31.01 ? 229 ASN A N   1 
ATOM   1646 C  CA  . ASN A 1 229 ? -35.627 12.174  0.699   1.00 31.47 ? 229 ASN A CA  1 
ATOM   1647 C  C   . ASN A 1 229 ? -36.010 13.090  -0.476  1.00 32.70 ? 229 ASN A C   1 
ATOM   1648 O  O   . ASN A 1 229 ? -35.512 14.214  -0.602  1.00 33.44 ? 229 ASN A O   1 
ATOM   1649 C  CB  . ASN A 1 229 ? -34.283 12.512  1.362   1.00 33.45 ? 229 ASN A CB  1 
ATOM   1650 C  CG  . ASN A 1 229 ? -33.081 12.394  0.428   1.00 37.66 ? 229 ASN A CG  1 
ATOM   1651 O  OD1 . ASN A 1 229 ? -32.731 11.281  0.013   1.00 38.48 ? 229 ASN A OD1 1 
ATOM   1652 N  ND2 . ASN A 1 229 ? -32.393 13.500  0.099   1.00 38.55 ? 229 ASN A ND2 1 
ATOM   1653 N  N   . ASN A 1 230 ? -36.960 12.615  -1.271  1.00 31.86 ? 230 ASN A N   1 
ATOM   1654 C  CA  . ASN A 1 230 ? -37.457 13.432  -2.390  1.00 37.71 ? 230 ASN A CA  1 
ATOM   1655 C  C   . ASN A 1 230 ? -38.494 14.429  -1.873  1.00 39.81 ? 230 ASN A C   1 
ATOM   1656 O  O   . ASN A 1 230 ? -38.514 15.579  -2.300  1.00 41.03 ? 230 ASN A O   1 
ATOM   1657 C  CB  . ASN A 1 230 ? -38.115 12.566  -3.457  1.00 36.67 ? 230 ASN A CB  1 
ATOM   1658 C  CG  . ASN A 1 230 ? -38.364 13.353  -4.723  1.00 40.91 ? 230 ASN A CG  1 
ATOM   1659 O  OD1 . ASN A 1 230 ? -37.531 14.181  -5.122  1.00 39.11 ? 230 ASN A OD1 1 
ATOM   1660 N  ND2 . ASN A 1 230 ? -39.521 13.121  -5.320  1.00 40.67 ? 230 ASN A ND2 1 
ATOM   1661 N  N   . GLU A 1 231 ? -39.377 13.978  -0.985  1.00 40.20 ? 231 GLU A N   1 
ATOM   1662 C  CA  . GLU A 1 231 ? -40.409 14.842  -0.428  1.00 46.08 ? 231 GLU A CA  1 
ATOM   1663 C  C   . GLU A 1 231 ? -40.299 14.838  1.094   1.00 47.59 ? 231 GLU A C   1 
ATOM   1664 O  O   . GLU A 1 231 ? -39.811 13.870  1.663   1.00 40.32 ? 231 GLU A O   1 
ATOM   1665 C  CB  . GLU A 1 231 ? -41.786 14.287  -0.803  1.00 43.47 ? 231 GLU A CB  1 
ATOM   1666 C  CG  . GLU A 1 231 ? -42.093 14.441  -2.289  1.00 58.23 ? 231 GLU A CG  1 
ATOM   1667 C  CD  . GLU A 1 231 ? -43.461 13.978  -2.780  1.00 68.34 ? 231 GLU A CD  1 
ATOM   1668 O  OE1 . GLU A 1 231 ? -44.372 13.775  -1.940  1.00 63.66 ? 231 GLU A OE1 1 
ATOM   1669 O  OE2 . GLU A 1 231 ? -43.613 13.799  -4.014  1.00 77.18 ? 231 GLU A OE2 1 
ATOM   1670 N  N   . ASP A 1 232 ? -40.794 15.901  1.745   1.00 46.60 ? 232 ASP A N   1 
ATOM   1671 C  CA  . ASP A 1 232 ? -40.939 15.924  3.201   1.00 42.41 ? 232 ASP A CA  1 
ATOM   1672 C  C   . ASP A 1 232 ? -42.271 15.323  3.612   1.00 41.02 ? 232 ASP A C   1 
ATOM   1673 O  O   . ASP A 1 232 ? -43.251 15.441  2.899   1.00 46.12 ? 232 ASP A O   1 
ATOM   1674 C  CB  . ASP A 1 232 ? -40.854 17.337  3.749   1.00 47.90 ? 232 ASP A CB  1 
ATOM   1675 C  CG  . ASP A 1 232 ? -39.487 17.971  3.551   1.00 58.39 ? 232 ASP A CG  1 
ATOM   1676 O  OD1 . ASP A 1 232 ? -38.526 17.445  4.131   1.00 55.99 ? 232 ASP A OD1 1 
ATOM   1677 O  OD2 . ASP A 1 232 ? -39.382 18.953  2.785   1.00 71.10 ? 232 ASP A OD2 1 
ATOM   1678 N  N   . PRO A 1 233 ? -42.349 14.603  4.754   1.00 37.42 ? 233 PRO A N   1 
ATOM   1679 C  CA  . PRO A 1 233 ? -41.158 14.275  5.544   1.00 34.75 ? 233 PRO A CA  1 
ATOM   1680 C  C   . PRO A 1 233 ? -40.357 13.158  4.879   1.00 34.83 ? 233 PRO A C   1 
ATOM   1681 O  O   . PRO A 1 233 ? -40.931 12.275  4.252   1.00 33.96 ? 233 PRO A O   1 
ATOM   1682 C  CB  . PRO A 1 233 ? -41.830 13.739  6.857   1.00 34.91 ? 233 PRO A CB  1 
ATOM   1683 C  CG  . PRO A 1 233 ? -43.102 13.058  6.368   1.00 36.01 ? 233 PRO A CG  1 
ATOM   1684 C  CD  . PRO A 1 233 ? -43.604 14.041  5.278   1.00 38.41 ? 233 PRO A CD  1 
ATOM   1685 N  N   . ARG A 1 234 ? -39.044 13.118  5.146   1.00 37.19 ? 234 ARG A N   1 
ATOM   1686 C  CA  A ARG A 1 234 ? -38.255 11.925  4.869   0.50 33.65 ? 234 ARG A CA  1 
ATOM   1687 C  CA  B ARG A 1 234 ? -38.245 11.926  4.895   0.50 33.99 ? 234 ARG A CA  1 
ATOM   1688 C  C   . ARG A 1 234 ? -38.966 10.721  5.486   1.00 31.33 ? 234 ARG A C   1 
ATOM   1689 O  O   . ARG A 1 234 ? -39.531 10.792  6.593   1.00 32.89 ? 234 ARG A O   1 
ATOM   1690 C  CB  A ARG A 1 234 ? -36.857 12.050  5.493   0.50 35.55 ? 234 ARG A CB  1 
ATOM   1691 C  CB  B ARG A 1 234 ? -36.930 11.993  5.680   0.50 35.96 ? 234 ARG A CB  1 
ATOM   1692 C  CG  A ARG A 1 234 ? -36.052 13.246  4.991   0.50 38.83 ? 234 ARG A CG  1 
ATOM   1693 C  CG  B ARG A 1 234 ? -35.911 12.899  5.008   0.50 41.82 ? 234 ARG A CG  1 
ATOM   1694 C  CD  A ARG A 1 234 ? -34.802 13.485  5.843   0.50 36.69 ? 234 ARG A CD  1 
ATOM   1695 C  CD  B ARG A 1 234 ? -34.684 13.024  5.901   0.50 38.13 ? 234 ARG A CD  1 
ATOM   1696 N  NE  A ARG A 1 234 ? -34.180 14.752  5.452   0.50 40.77 ? 234 ARG A NE  1 
ATOM   1697 N  NE  B ARG A 1 234 ? -33.530 13.128  5.008   0.50 37.18 ? 234 ARG A NE  1 
ATOM   1698 C  CZ  A ARG A 1 234 ? -33.059 14.855  4.764   0.50 42.25 ? 234 ARG A CZ  1 
ATOM   1699 C  CZ  B ARG A 1 234 ? -33.052 14.278  4.620   0.50 39.03 ? 234 ARG A CZ  1 
ATOM   1700 N  NH1 A ARG A 1 234 ? -32.406 13.759  4.381   0.50 41.83 ? 234 ARG A NH1 1 
ATOM   1701 N  NH1 B ARG A 1 234 ? -33.751 15.384  4.831   0.50 43.26 ? 234 ARG A NH1 1 
ATOM   1702 N  NH2 A ARG A 1 234 ? -32.580 16.084  4.454   0.50 38.09 ? 234 ARG A NH2 1 
ATOM   1703 N  NH2 B ARG A 1 234 ? -31.884 14.320  3.973   0.50 43.51 ? 234 ARG A NH2 1 
ATOM   1704 N  N   . THR A 1 235 ? -38.930 9.603   4.760   1.00 30.73 ? 235 THR A N   1 
ATOM   1705 C  CA  . THR A 1 235 ? -39.522 8.362   5.249   1.00 33.13 ? 235 THR A CA  1 
ATOM   1706 C  C   . THR A 1 235 ? -38.556 7.195   5.025   1.00 32.81 ? 235 THR A C   1 
ATOM   1707 O  O   . THR A 1 235 ? -37.691 7.276   4.138   1.00 31.24 ? 235 THR A O   1 
ATOM   1708 C  CB  . THR A 1 235 ? -40.941 8.118   4.710   1.00 34.14 ? 235 THR A CB  1 
ATOM   1709 O  OG1 . THR A 1 235 ? -40.754 8.122   3.293   1.00 34.73 ? 235 THR A OG1 1 
ATOM   1710 C  CG2 . THR A 1 235 ? -41.912 9.250   5.010   1.00 30.60 ? 235 THR A CG2 1 
ATOM   1711 N  N   . PHE A 1 236 ? -38.715 6.126   5.838   1.00 29.10 ? 236 PHE A N   1 
ATOM   1712 C  CA  . PHE A 1 236 ? -37.889 4.928   5.721   1.00 26.07 ? 236 PHE A CA  1 
ATOM   1713 C  C   . PHE A 1 236 ? -38.803 3.721   5.584   1.00 26.83 ? 236 PHE A C   1 
ATOM   1714 O  O   . PHE A 1 236 ? -39.956 3.731   6.061   1.00 30.42 ? 236 PHE A O   1 
ATOM   1715 C  CB  . PHE A 1 236 ? -37.103 4.703   7.034   1.00 26.91 ? 236 PHE A CB  1 
ATOM   1716 C  CG  . PHE A 1 236 ? -36.103 5.825   7.341   1.00 27.74 ? 236 PHE A CG  1 
ATOM   1717 C  CD1 . PHE A 1 236 ? -36.509 7.006   7.966   1.00 28.26 ? 236 PHE A CD1 1 
ATOM   1718 C  CD2 . PHE A 1 236 ? -34.742 5.667   7.039   1.00 26.26 ? 236 PHE A CD2 1 
ATOM   1719 C  CE1 . PHE A 1 236 ? -35.555 7.998   8.279   1.00 31.42 ? 236 PHE A CE1 1 
ATOM   1720 C  CE2 . PHE A 1 236 ? -33.799 6.645   7.377   1.00 28.32 ? 236 PHE A CE2 1 
ATOM   1721 C  CZ  . PHE A 1 236 ? -34.206 7.803   7.984   1.00 31.57 ? 236 PHE A CZ  1 
ATOM   1722 N  N   . GLY A 1 237 ? -38.261 2.601   5.056   1.00 28.31 ? 237 GLY A N   1 
ATOM   1723 C  CA  . GLY A 1 237 ? -38.941 1.295   5.080   1.00 28.71 ? 237 GLY A CA  1 
ATOM   1724 C  C   . GLY A 1 237 ? -38.890 0.696   6.488   1.00 35.23 ? 237 GLY A C   1 
ATOM   1725 O  O   . GLY A 1 237 ? -38.319 1.296   7.401   1.00 33.61 ? 237 GLY A O   1 
ATOM   1726 N  N   . GLY A 1 238 ? -39.573 -0.441  6.681   1.00 34.43 ? 238 GLY A N   1 
ATOM   1727 C  CA  . GLY A 1 238 ? -39.667 -1.004  8.018   1.00 33.11 ? 238 GLY A CA  1 
ATOM   1728 C  C   . GLY A 1 238 ? -38.425 -1.824  8.345   1.00 31.66 ? 238 GLY A C   1 
ATOM   1729 O  O   . GLY A 1 238 ? -38.300 -2.307  9.462   1.00 36.15 ? 238 GLY A O   1 
ATOM   1730 N  N   . GLY A 1 239 ? -37.518 -2.005  7.364   1.00 31.70 ? 239 GLY A N   1 
ATOM   1731 C  CA  . GLY A 1 239 ? -36.288 -2.745  7.601   1.00 33.50 ? 239 GLY A CA  1 
ATOM   1732 C  C   . GLY A 1 239 ? -36.353 -4.217  7.203   1.00 33.08 ? 239 GLY A C   1 
ATOM   1733 O  O   . GLY A 1 239 ? -37.408 -4.845  7.273   1.00 34.72 ? 239 GLY A O   1 
ATOM   1734 N  N   . THR A 1 240 ? -35.224 -4.758  6.752   1.00 30.41 ? 240 THR A N   1 
ATOM   1735 C  CA  . THR A 1 240 ? -35.138 -6.181  6.459   1.00 30.03 ? 240 THR A CA  1 
ATOM   1736 C  C   . THR A 1 240 ? -33.952 -6.713  7.254   1.00 29.09 ? 240 THR A C   1 
ATOM   1737 O  O   . THR A 1 240 ? -32.836 -6.225  7.079   1.00 30.64 ? 240 THR A O   1 
ATOM   1738 C  CB  . THR A 1 240 ? -34.826 -6.363  4.976   1.00 31.89 ? 240 THR A CB  1 
ATOM   1739 O  OG1 . THR A 1 240 ? -35.929 -5.825  4.267   1.00 34.29 ? 240 THR A OG1 1 
ATOM   1740 C  CG2 . THR A 1 240 ? -34.607 -7.816  4.629   1.00 35.16 ? 240 THR A CG2 1 
ATOM   1741 N  N   . LYS A 1 241 ? -34.206 -7.745  8.084   1.00 29.96 ? 241 LYS A N   1 
ATOM   1742 C  CA  . LYS A 1 241 ? -33.149 -8.379  8.847   1.00 31.62 ? 241 LYS A CA  1 
ATOM   1743 C  C   . LYS A 1 241 ? -32.547 -9.555  8.089   1.00 32.75 ? 241 LYS A C   1 
ATOM   1744 O  O   . LYS A 1 241 ? -33.228 -10.560 7.808   1.00 35.28 ? 241 LYS A O   1 
ATOM   1745 C  CB  . LYS A 1 241 ? -33.761 -8.734  10.215  1.00 34.52 ? 241 LYS A CB  1 
ATOM   1746 C  CG  . LYS A 1 241 ? -32.720 -9.559  10.939  1.00 43.00 ? 241 LYS A CG  1 
ATOM   1747 C  CD  . LYS A 1 241 ? -33.059 -9.625  12.411  1.00 53.19 ? 241 LYS A CD  1 
ATOM   1748 C  CE  . LYS A 1 241 ? -32.011 -10.427 13.113  1.00 65.24 ? 241 LYS A CE  1 
ATOM   1749 N  NZ  . LYS A 1 241 ? -32.334 -10.395 14.541  1.00 60.17 ? 241 LYS A NZ  1 
ATOM   1750 N  N   . LEU A 1 242 ? -31.268 -9.421  7.750   1.00 33.41 ? 242 LEU A N   1 
ATOM   1751 C  CA  . LEU A 1 242 ? -30.571 -10.495 7.068   1.00 34.72 ? 242 LEU A CA  1 
ATOM   1752 C  C   . LEU A 1 242 ? -29.689 -11.258 8.057   1.00 39.78 ? 242 LEU A C   1 
ATOM   1753 O  O   . LEU A 1 242 ? -28.815 -10.647 8.696   1.00 35.27 ? 242 LEU A O   1 
ATOM   1754 C  CB  . LEU A 1 242 ? -29.738 -9.885  5.954   1.00 33.91 ? 242 LEU A CB  1 
ATOM   1755 C  CG  . LEU A 1 242 ? -28.726 -10.824 5.306   1.00 36.84 ? 242 LEU A CG  1 
ATOM   1756 C  CD1 . LEU A 1 242 ? -29.505 -11.904 4.556   1.00 37.17 ? 242 LEU A CD1 1 
ATOM   1757 C  CD2 . LEU A 1 242 ? -27.820 -10.112 4.332   1.00 37.77 ? 242 LEU A CD2 1 
ATOM   1758 N  N   . GLU A 1 243 ? -29.865 -12.582 8.088   1.00 35.51 ? 243 GLU A N   1 
ATOM   1759 C  CA  . GLU A 1 243 ? -29.008 -13.449 8.927   1.00 38.72 ? 243 GLU A CA  1 
ATOM   1760 C  C   . GLU A 1 243 ? -28.285 -14.454 8.022   1.00 42.11 ? 243 GLU A C   1 
ATOM   1761 O  O   . GLU A 1 243 ? -28.703 -14.631 6.869   1.00 38.53 ? 243 GLU A O   1 
ATOM   1762 C  CB  . GLU A 1 243 ? -29.839 -14.178 9.978   1.00 39.29 ? 243 GLU A CB  1 
ATOM   1763 C  CG  . GLU A 1 243 ? -30.458 -13.239 11.005  1.00 48.34 ? 243 GLU A CG  1 
ATOM   1764 C  CD  . GLU A 1 243 ? -31.350 -13.930 12.017  0.70 55.20 ? 243 GLU A CD  1 
ATOM   1765 O  OE1 . GLU A 1 243 ? -30.814 -14.444 13.019  0.70 58.73 ? 243 GLU A OE1 1 
ATOM   1766 O  OE2 . GLU A 1 243 ? -32.578 -13.951 11.804  0.70 58.22 ? 243 GLU A OE2 1 
ATOM   1767 N  N   . ILE A 1 244 ? -27.234 -15.084 8.539   1.00 39.01 ? 244 ILE A N   1 
ATOM   1768 C  CA  . ILE A 1 244 ? -26.511 -16.128 7.762   1.00 41.97 ? 244 ILE A CA  1 
ATOM   1769 C  C   . ILE A 1 244 ? -27.156 -17.488 8.044   1.00 43.89 ? 244 ILE A C   1 
ATOM   1770 O  O   . ILE A 1 244 ? -27.363 -17.807 9.224   1.00 47.85 ? 244 ILE A O   1 
ATOM   1771 C  CB  . ILE A 1 244 ? -25.019 -16.160 8.115   1.00 49.48 ? 244 ILE A CB  1 
ATOM   1772 C  CG1 . ILE A 1 244 ? -24.373 -14.787 7.966   1.00 50.10 ? 244 ILE A CG1 1 
ATOM   1773 C  CG2 . ILE A 1 244 ? -24.289 -17.223 7.296   1.00 47.67 ? 244 ILE A CG2 1 
ATOM   1774 C  CD1 . ILE A 1 244 ? -24.624 -14.129 6.624   1.00 49.78 ? 244 ILE A CD1 1 
ATOM   1775 N  N   . LYS A 1 245 ? -27.468 -18.243 6.991   1.00 46.86 ? 245 LYS A N   1 
ATOM   1776 C  CA  . LYS A 1 245 ? -28.026 -19.607 7.155   1.00 42.28 ? 245 LYS A CA  1 
ATOM   1777 C  C   . LYS A 1 245 ? -26.840 -20.540 7.351   1.00 51.27 ? 245 LYS A C   1 
ATOM   1778 O  O   . LYS A 1 245 ? -26.072 -20.701 6.407   1.00 62.09 ? 245 LYS A O   1 
ATOM   1779 C  CB  . LYS A 1 245 ? -28.843 -20.061 5.944   1.00 44.05 ? 245 LYS A CB  1 
ATOM   1780 C  CG  . LYS A 1 245 ? -29.936 -21.078 6.200   0.80 45.12 ? 245 LYS A CG  1 
ATOM   1781 C  CD  . LYS A 1 245 ? -30.978 -21.072 5.088   0.80 46.69 ? 245 LYS A CD  1 
ATOM   1782 C  CE  . LYS A 1 245 ? -31.855 -22.280 5.129   0.80 48.97 ? 245 LYS A CE  1 
ATOM   1783 N  NZ  . LYS A 1 245 ? -31.304 -23.363 4.313   0.80 47.87 ? 245 LYS A NZ  1 
ATOM   1784 N  N   . LEU A 1 246 ? -26.724 -21.132 8.533   1.00 61.96 ? 246 LEU A N   1 
ATOM   1785 C  CA  . LEU A 1 246 ? -25.558 -21.982 8.868   1.00 74.47 ? 246 LEU A CA  1 
ATOM   1786 C  C   . LEU A 1 246 ? -25.608 -23.330 8.132   1.00 72.77 ? 246 LEU A C   1 
ATOM   1787 O  O   . LEU A 1 246 ? -26.688 -23.947 8.157   1.00 70.86 ? 246 LEU A O   1 
ATOM   1788 C  CB  . LEU A 1 246 ? -25.652 -22.135 10.381  1.00 68.83 ? 246 LEU A CB  1 
ATOM   1789 C  CG  . LEU A 1 246 ? -25.725 -20.826 11.172  1.00 80.48 ? 246 LEU A CG  1 
ATOM   1790 C  CD1 . LEU A 1 246 ? -25.698 -21.094 12.665  1.00 80.54 ? 246 LEU A CD1 1 
ATOM   1791 C  CD2 . LEU A 1 246 ? -24.592 -19.895 10.782  1.00 74.48 ? 246 LEU A CD2 1 
HETATM 1792 C  C1  . EDO B 2 .   ? -28.914 13.376  -5.288  1.00 42.01 ? 301 EDO A C1  1 
HETATM 1793 O  O1  . EDO B 2 .   ? -27.524 13.194  -5.001  1.00 40.83 ? 301 EDO A O1  1 
HETATM 1794 C  C2  . EDO B 2 .   ? -29.710 12.181  -4.856  1.00 43.49 ? 301 EDO A C2  1 
HETATM 1795 O  O2  . EDO B 2 .   ? -29.647 12.047  -3.414  1.00 39.01 ? 301 EDO A O2  1 
HETATM 1796 C  C1  . EDO C 2 .   ? -39.882 -7.289  -7.790  1.00 50.44 ? 302 EDO A C1  1 
HETATM 1797 O  O1  . EDO C 2 .   ? -40.858 -6.417  -8.314  1.00 44.37 ? 302 EDO A O1  1 
HETATM 1798 C  C2  . EDO C 2 .   ? -40.539 -7.873  -6.598  1.00 55.08 ? 302 EDO A C2  1 
HETATM 1799 O  O2  . EDO C 2 .   ? -40.282 -6.955  -5.590  1.00 50.39 ? 302 EDO A O2  1 
HETATM 1800 N  N1  . IMD D 3 .   ? -33.830 22.329  9.750   1.00 64.83 ? 303 IMD A N1  1 
HETATM 1801 C  C2  . IMD D 3 .   ? -34.608 22.066  8.665   1.00 65.65 ? 303 IMD A C2  1 
HETATM 1802 N  N3  . IMD D 3 .   ? -35.433 23.108  8.513   1.00 87.69 ? 303 IMD A N3  1 
HETATM 1803 C  C4  . IMD D 3 .   ? -35.203 24.029  9.501   1.00 67.03 ? 303 IMD A C4  1 
HETATM 1804 C  C5  . IMD D 3 .   ? -34.201 23.527  10.272  1.00 65.67 ? 303 IMD A C5  1 
HETATM 1805 NA NA  . NA  E 4 .   ? -17.787 21.674  18.619  1.00 46.88 ? 304 NA  A NA  1 
HETATM 1806 NA NA  . NA  F 4 .   ? -42.993 -9.134  -1.821  1.00 50.24 ? 305 NA  A NA  1 
HETATM 1807 CL CL  . CL  G 5 .   ? -41.526 -2.358  5.212   1.00 43.35 ? 306 CL  A CL  1 
HETATM 1808 CL CL  . CL  H 5 .   ? -42.501 -9.807  2.226   1.00 43.19 ? 307 CL  A CL  1 
HETATM 1809 O  O   . HOH I 6 .   ? -23.877 -20.320 5.807   1.00 59.76 ? 401 HOH A O   1 
HETATM 1810 O  O   . HOH I 6 .   ? -20.775 -0.701  11.240  1.00 46.01 ? 402 HOH A O   1 
HETATM 1811 O  O   . HOH I 6 .   ? -29.059 2.009   23.527  1.00 41.50 ? 403 HOH A O   1 
HETATM 1812 O  O   . HOH I 6 .   ? -44.103 15.685  29.957  1.00 57.06 ? 404 HOH A O   1 
HETATM 1813 O  O   . HOH I 6 .   ? -29.452 27.588  22.028  1.00 48.61 ? 405 HOH A O   1 
HETATM 1814 O  O   . HOH I 6 .   ? -43.836 18.708  23.779  1.00 58.90 ? 406 HOH A O   1 
HETATM 1815 O  O   . HOH I 6 .   ? -46.659 0.289   22.797  1.00 45.67 ? 407 HOH A O   1 
HETATM 1816 O  O   . HOH I 6 .   ? -12.660 16.150  12.467  1.00 57.76 ? 408 HOH A O   1 
HETATM 1817 O  O   . HOH I 6 .   ? -43.496 1.177   5.425   1.00 55.74 ? 409 HOH A O   1 
HETATM 1818 O  O   . HOH I 6 .   ? -35.369 16.838  6.112   1.00 42.87 ? 410 HOH A O   1 
HETATM 1819 O  O   . HOH I 6 .   ? -32.319 5.876   -10.411 1.00 44.66 ? 411 HOH A O   1 
HETATM 1820 O  O   . HOH I 6 .   ? -28.336 27.889  18.159  1.00 54.16 ? 412 HOH A O   1 
HETATM 1821 O  O   . HOH I 6 .   ? -28.601 5.641   31.423  1.00 48.68 ? 413 HOH A O   1 
HETATM 1822 O  O   . HOH I 6 .   ? -31.421 15.964  -8.619  1.00 47.43 ? 414 HOH A O   1 
HETATM 1823 O  O   . HOH I 6 .   ? -26.225 1.660   17.745  1.00 40.22 ? 415 HOH A O   1 
HETATM 1824 O  O   . HOH I 6 .   ? -38.743 22.532  6.737   1.00 55.37 ? 416 HOH A O   1 
HETATM 1825 O  O   . HOH I 6 .   ? -36.564 24.688  19.518  1.00 44.87 ? 417 HOH A O   1 
HETATM 1826 O  O   . HOH I 6 .   ? -45.184 8.772   7.302   1.00 51.82 ? 418 HOH A O   1 
HETATM 1827 O  O   A HOH I 6 .   ? -39.713 25.297  13.793  0.50 31.74 ? 419 HOH A O   1 
HETATM 1828 O  O   B HOH I 6 .   ? -41.123 24.402  13.745  0.50 34.78 ? 419 HOH A O   1 
HETATM 1829 O  O   . HOH I 6 .   ? -40.800 2.945   8.400   1.00 45.05 ? 420 HOH A O   1 
HETATM 1830 O  O   . HOH I 6 .   ? -30.803 10.352  -1.860  1.00 35.83 ? 421 HOH A O   1 
HETATM 1831 O  O   . HOH I 6 .   ? -29.810 13.597  -1.365  1.00 42.24 ? 422 HOH A O   1 
HETATM 1832 O  O   . HOH I 6 .   ? -43.299 1.778   21.853  1.00 38.07 ? 423 HOH A O   1 
HETATM 1833 O  O   . HOH I 6 .   ? -28.012 13.254  28.546  1.00 45.77 ? 424 HOH A O   1 
HETATM 1834 O  O   . HOH I 6 .   ? -37.679 -3.738  11.537  1.00 44.36 ? 425 HOH A O   1 
HETATM 1835 O  O   . HOH I 6 .   ? -19.659 9.719   -0.055  1.00 54.86 ? 426 HOH A O   1 
HETATM 1836 O  O   . HOH I 6 .   ? -38.890 23.919  18.203  1.00 47.30 ? 427 HOH A O   1 
HETATM 1837 O  O   . HOH I 6 .   ? -21.679 6.807   13.064  1.00 42.21 ? 428 HOH A O   1 
HETATM 1838 O  O   . HOH I 6 .   ? -33.911 -5.801  12.809  1.00 45.98 ? 429 HOH A O   1 
HETATM 1839 O  O   . HOH I 6 .   ? -22.615 5.271   11.262  1.00 40.75 ? 430 HOH A O   1 
HETATM 1840 O  O   . HOH I 6 .   ? -19.693 9.035   8.932   1.00 52.86 ? 431 HOH A O   1 
HETATM 1841 O  O   . HOH I 6 .   ? -14.702 2.881   -1.249  1.00 71.05 ? 432 HOH A O   1 
HETATM 1842 O  O   . HOH I 6 .   ? -41.585 17.858  23.761  1.00 43.57 ? 433 HOH A O   1 
HETATM 1843 O  O   . HOH I 6 .   ? -46.066 8.409   20.957  1.00 46.07 ? 434 HOH A O   1 
HETATM 1844 O  O   . HOH I 6 .   ? -46.333 12.488  8.978   1.00 50.06 ? 435 HOH A O   1 
HETATM 1845 O  O   . HOH I 6 .   ? -31.180 11.692  3.302   1.00 41.22 ? 436 HOH A O   1 
HETATM 1846 O  O   . HOH I 6 .   ? -21.058 4.081   5.697   1.00 33.55 ? 437 HOH A O   1 
HETATM 1847 O  O   . HOH I 6 .   ? -47.705 0.550   37.074  1.00 62.46 ? 438 HOH A O   1 
HETATM 1848 O  O   . HOH I 6 .   ? -27.052 9.420   4.915   1.00 32.70 ? 439 HOH A O   1 
HETATM 1849 O  O   . HOH I 6 .   ? -25.634 5.293   22.682  1.00 41.36 ? 440 HOH A O   1 
HETATM 1850 O  O   . HOH I 6 .   ? -20.660 24.735  19.080  1.00 61.77 ? 441 HOH A O   1 
HETATM 1851 O  O   . HOH I 6 .   ? -18.380 3.217   4.803   1.00 45.48 ? 442 HOH A O   1 
HETATM 1852 O  O   . HOH I 6 .   ? -42.987 2.845   36.672  1.00 52.52 ? 443 HOH A O   1 
HETATM 1853 O  O   . HOH I 6 .   ? -24.402 19.989  13.694  1.00 31.84 ? 444 HOH A O   1 
HETATM 1854 O  O   . HOH I 6 .   ? -49.164 0.556   28.079  1.00 64.70 ? 445 HOH A O   1 
HETATM 1855 O  O   . HOH I 6 .   ? -42.674 5.047   14.353  1.00 55.05 ? 446 HOH A O   1 
HETATM 1856 O  O   . HOH I 6 .   ? -21.022 6.845   5.853   1.00 39.30 ? 447 HOH A O   1 
HETATM 1857 O  O   . HOH I 6 .   ? -29.851 8.112   -8.769  1.00 35.22 ? 448 HOH A O   1 
HETATM 1858 O  O   . HOH I 6 .   ? -31.166 -2.799  13.518  1.00 44.35 ? 449 HOH A O   1 
HETATM 1859 O  O   . HOH I 6 .   ? -20.870 10.374  3.191   1.00 37.39 ? 450 HOH A O   1 
HETATM 1860 O  O   . HOH I 6 .   ? -28.641 -4.857  13.554  1.00 43.27 ? 451 HOH A O   1 
HETATM 1861 O  O   . HOH I 6 .   ? -38.921 24.901  9.549   1.00 58.04 ? 452 HOH A O   1 
HETATM 1862 O  O   . HOH I 6 .   ? -18.757 19.883  17.219  1.00 39.56 ? 453 HOH A O   1 
HETATM 1863 O  O   . HOH I 6 .   ? -33.724 2.274   28.542  1.00 39.30 ? 454 HOH A O   1 
HETATM 1864 O  O   . HOH I 6 .   ? -26.491 11.745  -7.044  1.00 45.25 ? 455 HOH A O   1 
HETATM 1865 O  O   . HOH I 6 .   ? -44.616 0.529   28.844  1.00 43.95 ? 456 HOH A O   1 
HETATM 1866 O  O   . HOH I 6 .   ? -29.672 10.888  22.737  1.00 33.11 ? 457 HOH A O   1 
HETATM 1867 O  O   . HOH I 6 .   ? -30.464 21.080  5.990   1.00 42.08 ? 458 HOH A O   1 
HETATM 1868 O  O   . HOH I 6 .   ? -42.050 22.012  24.147  1.00 56.86 ? 459 HOH A O   1 
HETATM 1869 O  O   . HOH I 6 .   ? -31.555 0.775   -4.994  1.00 36.62 ? 460 HOH A O   1 
HETATM 1870 O  O   . HOH I 6 .   ? -32.605 -1.106  22.901  1.00 37.17 ? 461 HOH A O   1 
HETATM 1871 O  O   A HOH I 6 .   ? -24.520 -7.264  -5.847  0.50 33.49 ? 462 HOH A O   1 
HETATM 1872 O  O   B HOH I 6 .   ? -22.985 -7.804  -6.439  0.50 38.55 ? 462 HOH A O   1 
HETATM 1873 O  O   . HOH I 6 .   ? -43.915 6.642   16.274  1.00 41.37 ? 463 HOH A O   1 
HETATM 1874 O  O   . HOH I 6 .   ? -25.001 12.736  25.091  1.00 53.81 ? 464 HOH A O   1 
HETATM 1875 O  O   . HOH I 6 .   ? -22.464 -8.200  10.752  1.00 44.53 ? 465 HOH A O   1 
HETATM 1876 O  O   . HOH I 6 .   ? -40.677 8.869   -11.846 1.00 57.63 ? 466 HOH A O   1 
HETATM 1877 O  O   . HOH I 6 .   ? -40.228 -11.431 9.029   1.00 68.17 ? 467 HOH A O   1 
HETATM 1878 O  O   . HOH I 6 .   ? -36.610 -1.765  12.837  1.00 39.25 ? 468 HOH A O   1 
HETATM 1879 O  O   . HOH I 6 .   ? -38.389 -3.298  -6.090  1.00 33.65 ? 469 HOH A O   1 
HETATM 1880 O  O   . HOH I 6 .   ? -30.144 18.021  6.102   1.00 38.79 ? 470 HOH A O   1 
HETATM 1881 O  O   . HOH I 6 .   ? -30.412 2.897   -10.211 1.00 58.03 ? 471 HOH A O   1 
HETATM 1882 O  O   . HOH I 6 .   ? -26.075 17.649  8.126   1.00 35.48 ? 472 HOH A O   1 
HETATM 1883 O  O   . HOH I 6 .   ? -42.159 8.689   20.179  1.00 35.36 ? 473 HOH A O   1 
HETATM 1884 O  O   . HOH I 6 .   ? -41.959 -7.842  -3.580  1.00 49.28 ? 474 HOH A O   1 
HETATM 1885 O  O   . HOH I 6 .   ? -34.910 20.071  23.597  1.00 44.22 ? 475 HOH A O   1 
HETATM 1886 O  O   . HOH I 6 .   ? -18.695 13.781  20.679  1.00 43.73 ? 476 HOH A O   1 
HETATM 1887 O  O   . HOH I 6 .   ? -42.826 -0.000  26.854  0.50 38.87 ? 477 HOH A O   1 
HETATM 1888 O  O   . HOH I 6 .   ? -19.905 10.728  5.747   1.00 39.12 ? 478 HOH A O   1 
HETATM 1889 O  O   . HOH I 6 .   ? -29.015 15.526  -11.981 1.00 48.16 ? 479 HOH A O   1 
HETATM 1890 O  O   . HOH I 6 .   ? -33.484 -12.559 -1.384  1.00 35.65 ? 480 HOH A O   1 
HETATM 1891 O  O   . HOH I 6 .   ? -40.356 2.506   -11.057 1.00 60.50 ? 481 HOH A O   1 
HETATM 1892 O  O   . HOH I 6 .   ? -40.632 9.330   8.677   1.00 29.77 ? 482 HOH A O   1 
HETATM 1893 O  O   . HOH I 6 .   ? -21.939 7.008   9.279   1.00 45.53 ? 483 HOH A O   1 
HETATM 1894 O  O   . HOH I 6 .   ? -21.556 -11.043 -7.881  1.00 53.19 ? 484 HOH A O   1 
HETATM 1895 O  O   . HOH I 6 .   ? -23.864 1.091   18.561  1.00 46.34 ? 485 HOH A O   1 
HETATM 1896 O  O   . HOH I 6 .   ? -31.754 -1.204  17.799  1.00 46.70 ? 486 HOH A O   1 
HETATM 1897 O  O   . HOH I 6 .   ? -37.816 15.571  6.066   1.00 38.46 ? 487 HOH A O   1 
HETATM 1898 O  O   . HOH I 6 .   ? -23.386 7.798   20.156  1.00 35.09 ? 488 HOH A O   1 
HETATM 1899 O  O   . HOH I 6 .   ? -28.084 16.125  6.921   1.00 38.08 ? 489 HOH A O   1 
HETATM 1900 O  O   . HOH I 6 .   ? -16.622 10.133  0.530   1.00 65.25 ? 490 HOH A O   1 
HETATM 1901 O  O   . HOH I 6 .   ? -42.530 4.208   5.078   1.00 41.36 ? 491 HOH A O   1 
HETATM 1902 O  O   . HOH I 6 .   ? -24.770 -0.374  -7.386  1.00 41.65 ? 492 HOH A O   1 
HETATM 1903 O  O   . HOH I 6 .   ? -41.031 -10.996 4.577   1.00 51.31 ? 493 HOH A O   1 
HETATM 1904 O  O   . HOH I 6 .   ? -32.326 -12.450 -6.872  1.00 45.72 ? 494 HOH A O   1 
HETATM 1905 O  O   . HOH I 6 .   ? -30.781 18.190  -10.321 1.00 56.63 ? 495 HOH A O   1 
HETATM 1906 O  O   . HOH I 6 .   ? -44.941 13.452  1.020   1.00 58.48 ? 496 HOH A O   1 
HETATM 1907 O  O   . HOH I 6 .   ? -40.610 6.615   7.854   1.00 33.01 ? 497 HOH A O   1 
HETATM 1908 O  O   . HOH I 6 .   ? -44.084 -0.090  -7.248  1.00 56.52 ? 498 HOH A O   1 
HETATM 1909 O  O   A HOH I 6 .   ? -17.036 1.779   -2.078  0.50 39.02 ? 499 HOH A O   1 
HETATM 1910 O  O   B HOH I 6 .   ? -17.422 3.309   -3.023  0.50 41.48 ? 499 HOH A O   1 
HETATM 1911 O  O   . HOH I 6 .   ? -37.565 11.252  32.916  1.00 52.87 ? 500 HOH A O   1 
HETATM 1912 O  O   . HOH I 6 .   ? -17.171 -1.406  5.529   1.00 48.25 ? 501 HOH A O   1 
HETATM 1913 O  O   . HOH I 6 .   ? -31.929 18.786  18.643  1.00 34.27 ? 502 HOH A O   1 
HETATM 1914 O  O   . HOH I 6 .   ? -29.760 -4.458  -7.132  1.00 35.68 ? 503 HOH A O   1 
HETATM 1915 O  O   . HOH I 6 .   ? -21.204 -5.569  5.473   1.00 37.08 ? 504 HOH A O   1 
HETATM 1916 O  O   . HOH I 6 .   ? -44.966 1.270   -0.413  1.00 38.78 ? 505 HOH A O   1 
HETATM 1917 O  O   . HOH I 6 .   ? -29.161 5.253   -10.482 1.00 51.05 ? 506 HOH A O   1 
HETATM 1918 O  O   . HOH I 6 .   ? -27.623 -2.825  16.376  1.00 64.15 ? 507 HOH A O   1 
HETATM 1919 O  O   . HOH I 6 .   ? -32.176 5.349   33.267  1.00 42.36 ? 508 HOH A O   1 
HETATM 1920 O  O   . HOH I 6 .   ? -17.829 7.909   4.184   1.00 54.44 ? 509 HOH A O   1 
HETATM 1921 O  O   . HOH I 6 .   ? -40.204 -4.309  7.164   1.00 49.21 ? 510 HOH A O   1 
HETATM 1922 O  O   . HOH I 6 .   ? -37.260 -15.288 4.272   1.00 47.33 ? 511 HOH A O   1 
HETATM 1923 O  O   . HOH I 6 .   ? -25.013 29.657  9.258   1.00 49.02 ? 512 HOH A O   1 
HETATM 1924 O  O   . HOH I 6 .   ? -43.062 11.849  2.399   1.00 42.64 ? 513 HOH A O   1 
HETATM 1925 O  O   . HOH I 6 .   ? -40.943 -4.262  -1.780  1.00 35.46 ? 514 HOH A O   1 
HETATM 1926 O  O   . HOH I 6 .   ? -14.725 -3.849  -2.915  1.00 61.96 ? 515 HOH A O   1 
HETATM 1927 O  O   . HOH I 6 .   ? -49.071 13.062  30.505  1.00 60.41 ? 516 HOH A O   1 
HETATM 1928 O  O   . HOH I 6 .   ? -46.170 -6.593  35.041  1.00 51.52 ? 517 HOH A O   1 
HETATM 1929 O  O   . HOH I 6 .   ? -18.318 8.635   14.762  1.00 49.47 ? 518 HOH A O   1 
HETATM 1930 O  O   . HOH I 6 .   ? -46.740 14.581  3.081   1.00 51.99 ? 519 HOH A O   1 
HETATM 1931 O  O   . HOH I 6 .   ? -46.850 14.815  18.403  1.00 47.14 ? 520 HOH A O   1 
HETATM 1932 O  O   . HOH I 6 .   ? -20.854 9.151   15.893  1.00 45.07 ? 521 HOH A O   1 
HETATM 1933 O  O   . HOH I 6 .   ? -23.716 -0.775  10.862  1.00 38.48 ? 522 HOH A O   1 
HETATM 1934 O  O   . HOH I 6 .   ? -43.795 -0.013  37.665  1.00 50.25 ? 523 HOH A O   1 
HETATM 1935 O  O   . HOH I 6 .   ? -34.910 -16.889 4.397   1.00 38.95 ? 524 HOH A O   1 
HETATM 1936 O  O   . HOH I 6 .   ? -16.154 9.705   12.044  1.00 56.32 ? 525 HOH A O   1 
HETATM 1937 O  O   . HOH I 6 .   ? -44.996 16.241  8.224   1.00 45.21 ? 526 HOH A O   1 
HETATM 1938 O  O   . HOH I 6 .   ? -19.279 -9.553  -6.117  1.00 57.19 ? 527 HOH A O   1 
HETATM 1939 O  O   . HOH I 6 .   ? -28.130 2.006   21.126  1.00 45.48 ? 528 HOH A O   1 
HETATM 1940 O  O   . HOH I 6 .   ? -14.453 19.045  18.459  1.00 43.17 ? 529 HOH A O   1 
HETATM 1941 O  O   . HOH I 6 .   ? -21.316 10.379  -6.848  1.00 50.93 ? 530 HOH A O   1 
HETATM 1942 O  O   . HOH I 6 .   ? -26.239 -15.257 -7.923  1.00 45.23 ? 531 HOH A O   1 
HETATM 1943 O  O   . HOH I 6 .   ? -42.873 4.356   9.477   1.00 68.84 ? 532 HOH A O   1 
HETATM 1944 O  O   A HOH I 6 .   ? -23.626 -9.401  -8.560  0.50 35.90 ? 533 HOH A O   1 
HETATM 1945 O  O   B HOH I 6 .   ? -24.799 -8.367  -7.648  0.50 35.63 ? 533 HOH A O   1 
HETATM 1946 O  O   . HOH I 6 .   ? -28.832 -9.923  11.520  1.00 42.67 ? 534 HOH A O   1 
HETATM 1947 O  O   . HOH I 6 .   ? -40.372 3.646   14.371  1.00 37.54 ? 535 HOH A O   1 
HETATM 1948 O  O   . HOH I 6 .   ? -15.164 -6.752  2.865   1.00 56.48 ? 536 HOH A O   1 
HETATM 1949 O  O   . HOH I 6 .   ? -30.090 15.589  28.291  1.00 54.67 ? 537 HOH A O   1 
HETATM 1950 O  O   . HOH I 6 .   ? -48.562 11.026  23.737  1.00 49.94 ? 538 HOH A O   1 
HETATM 1951 O  O   . HOH I 6 .   ? -32.212 -22.030 1.862   1.00 52.27 ? 539 HOH A O   1 
HETATM 1952 O  O   . HOH I 6 .   ? -26.523 7.963   -9.720  1.00 54.02 ? 540 HOH A O   1 
HETATM 1953 O  O   . HOH I 6 .   ? -37.992 15.840  -12.433 1.00 46.55 ? 541 HOH A O   1 
HETATM 1954 O  O   . HOH I 6 .   ? -43.298 9.513   9.144   1.00 41.91 ? 542 HOH A O   1 
HETATM 1955 O  O   . HOH I 6 .   ? -19.847 -17.749 -3.757  1.00 65.15 ? 543 HOH A O   1 
HETATM 1956 O  O   . HOH I 6 .   ? -29.116 -19.333 0.668   1.00 40.96 ? 544 HOH A O   1 
HETATM 1957 O  O   . HOH I 6 .   ? -27.086 27.879  21.010  1.00 52.40 ? 545 HOH A O   1 
HETATM 1958 O  O   A HOH I 6 .   ? -44.281 6.739   5.421   0.50 38.03 ? 546 HOH A O   1 
HETATM 1959 O  O   B HOH I 6 .   ? -43.449 5.958   7.055   0.50 32.80 ? 546 HOH A O   1 
HETATM 1960 O  O   . HOH I 6 .   ? -32.251 25.859  20.333  1.00 37.56 ? 547 HOH A O   1 
HETATM 1961 O  O   . HOH I 6 .   ? -29.399 12.008  1.115   1.00 34.95 ? 548 HOH A O   1 
HETATM 1962 O  O   . HOH I 6 .   ? -26.315 -14.224 11.236  1.00 37.70 ? 549 HOH A O   1 
HETATM 1963 O  O   . HOH I 6 .   ? -34.145 13.970  31.242  1.00 45.97 ? 550 HOH A O   1 
HETATM 1964 O  O   . HOH I 6 .   ? -22.334 -1.843  -6.958  1.00 53.69 ? 551 HOH A O   1 
HETATM 1965 O  O   . HOH I 6 .   ? -16.863 24.605  9.228   1.00 27.70 ? 552 HOH A O   1 
HETATM 1966 O  O   . HOH I 6 .   ? -39.851 26.673  11.794  1.00 64.99 ? 553 HOH A O   1 
HETATM 1967 O  O   . HOH I 6 .   ? -30.038 11.847  27.742  1.00 51.91 ? 554 HOH A O   1 
HETATM 1968 O  O   . HOH I 6 .   ? -37.980 27.261  13.280  1.00 47.65 ? 555 HOH A O   1 
HETATM 1969 O  O   . HOH I 6 .   ? -40.794 14.663  34.016  1.00 48.83 ? 556 HOH A O   1 
HETATM 1970 O  O   . HOH I 6 .   ? -45.680 9.198   -8.451  1.00 48.88 ? 557 HOH A O   1 
HETATM 1971 O  O   . HOH I 6 .   ? -15.864 21.231  17.204  1.00 57.07 ? 558 HOH A O   1 
HETATM 1972 O  O   . HOH I 6 .   ? -18.084 22.997  22.674  1.00 50.59 ? 559 HOH A O   1 
HETATM 1973 O  O   . HOH I 6 .   ? -17.288 19.962  20.285  1.00 49.65 ? 560 HOH A O   1 
HETATM 1974 O  O   . HOH I 6 .   ? -17.190 -11.803 7.059   1.00 50.45 ? 561 HOH A O   1 
HETATM 1975 O  O   . HOH I 6 .   ? -32.089 0.404   -12.580 1.00 46.03 ? 562 HOH A O   1 
HETATM 1976 O  O   . HOH I 6 .   ? -34.981 29.764  15.534  1.00 59.12 ? 563 HOH A O   1 
HETATM 1977 O  O   . HOH I 6 .   ? -17.682 -14.872 5.859   1.00 43.99 ? 564 HOH A O   1 
HETATM 1978 O  O   . HOH I 6 .   ? -20.640 2.765   -6.957  1.00 35.63 ? 565 HOH A O   1 
HETATM 1979 O  O   . HOH I 6 .   ? -18.530 11.898  3.058   1.00 52.43 ? 566 HOH A O   1 
HETATM 1980 O  O   . HOH I 6 .   ? -36.927 12.146  -12.967 1.00 38.90 ? 567 HOH A O   1 
HETATM 1981 O  O   . HOH I 6 .   ? -41.874 18.087  -0.156  1.00 41.41 ? 568 HOH A O   1 
HETATM 1982 O  O   . HOH I 6 .   ? -18.653 -1.872  9.889   1.00 43.72 ? 569 HOH A O   1 
HETATM 1983 O  O   . HOH I 6 .   ? -18.494 -15.760 1.267   1.00 54.17 ? 570 HOH A O   1 
HETATM 1984 O  O   . HOH I 6 .   ? -29.620 -7.305  12.588  1.00 33.92 ? 571 HOH A O   1 
HETATM 1985 O  O   . HOH I 6 .   ? -44.618 -0.050  -10.405 1.00 60.46 ? 572 HOH A O   1 
HETATM 1986 O  O   . HOH I 6 .   ? -34.603 1.049   -13.199 1.00 61.50 ? 573 HOH A O   1 
HETATM 1987 O  O   . HOH I 6 .   ? -30.486 18.733  2.010   1.00 59.72 ? 574 HOH A O   1 
HETATM 1988 O  O   . HOH I 6 .   ? -13.506 11.612  11.189  1.00 65.07 ? 575 HOH A O   1 
HETATM 1989 O  O   . HOH I 6 .   ? -16.578 23.282  20.041  1.00 51.75 ? 576 HOH A O   1 
HETATM 1990 O  O   . HOH I 6 .   ? -39.138 9.319   34.697  1.00 37.28 ? 577 HOH A O   1 
HETATM 1991 O  O   . HOH I 6 .   ? -23.895 4.101   -10.093 1.00 58.67 ? 578 HOH A O   1 
HETATM 1992 O  O   . HOH I 6 .   ? -22.528 6.222   25.177  1.00 64.73 ? 579 HOH A O   1 
HETATM 1993 O  O   . HOH I 6 .   ? -49.384 10.355  5.467   1.00 57.18 ? 580 HOH A O   1 
HETATM 1994 O  O   . HOH I 6 .   ? -39.985 -12.637 6.092   1.00 51.54 ? 581 HOH A O   1 
HETATM 1995 O  O   . HOH I 6 .   ? -48.455 4.426   28.799  1.00 41.40 ? 582 HOH A O   1 
HETATM 1996 O  O   A HOH I 6 .   ? -46.834 15.458  23.966  0.60 33.43 ? 583 HOH A O   1 
HETATM 1997 O  O   B HOH I 6 .   ? -47.563 14.479  23.001  0.40 29.78 ? 583 HOH A O   1 
HETATM 1998 O  O   . HOH I 6 .   ? -18.351 -4.213  5.387   1.00 40.77 ? 584 HOH A O   1 
HETATM 1999 O  O   . HOH I 6 .   ? -42.565 0.892   8.098   1.00 55.71 ? 585 HOH A O   1 
HETATM 2000 O  O   . HOH I 6 .   ? -24.257 6.164   28.638  1.00 46.70 ? 586 HOH A O   1 
HETATM 2001 O  O   . HOH I 6 .   ? -36.986 -6.542  10.269  1.00 59.05 ? 587 HOH A O   1 
HETATM 2002 O  O   . HOH I 6 .   ? -18.173 23.407  16.915  1.00 45.50 ? 588 HOH A O   1 
HETATM 2003 O  O   . HOH I 6 .   ? -20.802 -7.446  12.595  1.00 56.00 ? 589 HOH A O   1 
HETATM 2004 O  O   . HOH I 6 .   ? -49.997 6.988   -4.079  1.00 65.61 ? 590 HOH A O   1 
HETATM 2005 O  O   . HOH I 6 .   ? -16.598 21.337  9.847   1.00 35.91 ? 591 HOH A O   1 
HETATM 2006 O  O   . HOH I 6 .   ? -42.320 22.411  11.527  1.00 33.44 ? 592 HOH A O   1 
HETATM 2007 O  O   . HOH I 6 .   ? -29.391 16.677  -1.542  1.00 51.47 ? 593 HOH A O   1 
HETATM 2008 O  O   . HOH I 6 .   ? -49.734 11.351  26.546  1.00 54.61 ? 594 HOH A O   1 
HETATM 2009 O  O   . HOH I 6 .   ? -23.510 10.372  26.620  1.00 55.76 ? 595 HOH A O   1 
HETATM 2010 O  O   . HOH I 6 .   ? -20.219 25.723  16.460  1.00 39.26 ? 596 HOH A O   1 
HETATM 2011 O  O   . HOH I 6 .   ? -28.263 -17.537 -4.449  1.00 51.24 ? 597 HOH A O   1 
HETATM 2012 O  O   . HOH I 6 .   ? -18.431 2.527   8.925   1.00 50.80 ? 598 HOH A O   1 
HETATM 2013 O  O   . HOH I 6 .   ? -41.638 -4.272  9.361   1.00 59.15 ? 599 HOH A O   1 
HETATM 2014 O  O   . HOH I 6 .   ? -44.171 -7.317  -0.746  1.00 53.94 ? 600 HOH A O   1 
HETATM 2015 O  O   . HOH I 6 .   ? -21.516 2.583   11.666  1.00 53.69 ? 601 HOH A O   1 
HETATM 2016 O  O   . HOH I 6 .   ? -16.912 24.042  25.738  1.00 76.63 ? 602 HOH A O   1 
HETATM 2017 O  O   . HOH I 6 .   ? -36.997 -15.621 8.098   1.00 49.75 ? 603 HOH A O   1 
HETATM 2018 O  O   . HOH I 6 .   ? -30.245 27.846  19.798  1.00 57.44 ? 604 HOH A O   1 
HETATM 2019 O  O   . HOH I 6 .   ? -43.994 -10.648 -0.150  1.00 43.67 ? 605 HOH A O   1 
HETATM 2020 O  O   . HOH I 6 .   ? -19.101 13.532  5.993   1.00 42.99 ? 606 HOH A O   1 
HETATM 2021 O  O   . HOH I 6 .   ? -17.284 -6.943  14.384  0.60 48.84 ? 607 HOH A O   1 
HETATM 2022 O  O   . HOH I 6 .   ? -27.238 -1.104  17.959  1.00 56.21 ? 608 HOH A O   1 
HETATM 2023 O  O   . HOH I 6 .   ? -45.587 19.685  11.764  1.00 62.78 ? 609 HOH A O   1 
HETATM 2024 O  O   . HOH I 6 .   ? -16.548 -7.727  -1.792  1.00 32.01 ? 610 HOH A O   1 
HETATM 2025 O  O   . HOH I 6 .   ? -46.125 19.127  27.814  1.00 69.10 ? 611 HOH A O   1 
HETATM 2026 O  O   . HOH I 6 .   ? -35.234 16.545  1.960   1.00 62.13 ? 612 HOH A O   1 
HETATM 2027 O  O   . HOH I 6 .   ? -33.390 19.148  5.849   1.00 64.26 ? 613 HOH A O   1 
HETATM 2028 O  O   . HOH I 6 .   ? -18.787 8.898   -2.104  1.00 58.24 ? 614 HOH A O   1 
HETATM 2029 O  O   . HOH I 6 .   ? -46.747 7.626   9.999   1.00 65.06 ? 615 HOH A O   1 
HETATM 2030 O  O   . HOH I 6 .   ? -30.442 23.832  24.760  1.00 51.45 ? 616 HOH A O   1 
HETATM 2031 O  O   . HOH I 6 .   ? -20.922 7.116   17.944  1.00 62.03 ? 617 HOH A O   1 
HETATM 2032 O  O   . HOH I 6 .   ? -42.558 17.242  7.092   1.00 38.82 ? 618 HOH A O   1 
HETATM 2033 O  O   . HOH I 6 .   ? -28.879 30.760  17.808  1.00 61.44 ? 619 HOH A O   1 
HETATM 2034 O  O   . HOH I 6 .   ? -34.348 24.606  5.486   1.00 48.06 ? 620 HOH A O   1 
HETATM 2035 O  O   . HOH I 6 .   ? -35.655 -12.162 11.893  1.00 54.73 ? 621 HOH A O   1 
HETATM 2036 O  O   . HOH I 6 .   ? -41.523 16.598  -4.848  1.00 65.01 ? 622 HOH A O   1 
HETATM 2037 O  O   . HOH I 6 .   ? -37.576 -14.475 11.429  1.00 69.26 ? 623 HOH A O   1 
HETATM 2038 O  O   . HOH I 6 .   ? -26.544 30.777  11.511  1.00 43.98 ? 624 HOH A O   1 
HETATM 2039 O  O   . HOH I 6 .   ? -16.082 1.811   5.903   1.00 57.42 ? 625 HOH A O   1 
HETATM 2040 O  O   . HOH I 6 .   ? -37.303 17.026  30.002  1.00 50.33 ? 626 HOH A O   1 
HETATM 2041 O  O   . HOH I 6 .   ? -43.891 22.155  16.421  1.00 57.32 ? 627 HOH A O   1 
HETATM 2042 O  O   . HOH I 6 .   ? -42.437 5.214   -11.431 1.00 57.32 ? 628 HOH A O   1 
HETATM 2043 O  O   . HOH I 6 .   ? -26.079 19.401  6.343   1.00 47.09 ? 629 HOH A O   1 
HETATM 2044 O  O   . HOH I 6 .   ? -29.697 1.115   -11.727 1.00 66.93 ? 630 HOH A O   1 
HETATM 2045 O  O   . HOH I 6 .   ? -50.006 13.727  12.317  1.00 67.05 ? 631 HOH A O   1 
HETATM 2046 O  O   . HOH I 6 .   ? -35.541 -2.722  15.803  1.00 43.54 ? 632 HOH A O   1 
HETATM 2047 O  O   . HOH I 6 .   ? -13.633 4.905   3.430   1.00 54.56 ? 633 HOH A O   1 
HETATM 2048 O  O   . HOH I 6 .   ? -24.208 -7.166  19.285  1.00 59.05 ? 634 HOH A O   1 
HETATM 2049 O  O   A HOH I 6 .   ? -12.335 19.524  15.210  0.50 39.10 ? 635 HOH A O   1 
HETATM 2050 O  O   B HOH I 6 .   ? -13.556 20.496  14.960  0.50 38.64 ? 635 HOH A O   1 
HETATM 2051 O  O   . HOH I 6 .   ? -19.070 22.338  26.996  1.00 69.97 ? 636 HOH A O   1 
HETATM 2052 O  O   . HOH I 6 .   ? -31.471 2.028   32.988  1.00 56.13 ? 637 HOH A O   1 
HETATM 2053 O  O   . HOH I 6 .   ? -28.161 14.209  -13.760 1.00 55.00 ? 638 HOH A O   1 
HETATM 2054 O  O   . HOH I 6 .   ? -45.645 0.211   -2.808  1.00 58.75 ? 639 HOH A O   1 
HETATM 2055 O  O   A HOH I 6 .   ? -45.774 9.417   17.199  0.50 37.05 ? 640 HOH A O   1 
HETATM 2056 O  O   B HOH I 6 .   ? -46.270 10.228  18.784  0.50 43.22 ? 640 HOH A O   1 
HETATM 2057 O  O   . HOH I 6 .   ? -17.647 7.537   23.011  1.00 71.78 ? 641 HOH A O   1 
HETATM 2058 O  O   . HOH I 6 .   ? -22.616 -21.060 8.193   1.00 57.70 ? 642 HOH A O   1 
HETATM 2059 O  O   . HOH I 6 .   ? -26.545 -2.122  20.556  1.00 62.44 ? 643 HOH A O   1 
HETATM 2060 O  O   . HOH I 6 .   ? -36.195 18.418  0.526   1.00 60.40 ? 644 HOH A O   1 
HETATM 2061 O  O   . HOH I 6 .   ? -18.819 7.629   7.115   1.00 48.36 ? 645 HOH A O   1 
HETATM 2062 O  O   . HOH I 6 .   ? -35.398 19.243  7.285   1.00 49.56 ? 646 HOH A O   1 
HETATM 2063 O  O   . HOH I 6 .   ? -48.226 13.254  20.505  1.00 63.74 ? 647 HOH A O   1 
HETATM 2064 O  O   . HOH I 6 .   ? -25.221 0.988   21.576  1.00 54.02 ? 648 HOH A O   1 
HETATM 2065 O  O   . HOH I 6 .   ? -22.714 -3.600  -9.353  1.00 61.19 ? 649 HOH A O   1 
HETATM 2066 O  O   . HOH I 6 .   ? -37.109 -9.745  11.706  1.00 56.51 ? 650 HOH A O   1 
HETATM 2067 O  O   . HOH I 6 .   ? -45.676 -2.492  -2.265  1.00 41.10 ? 651 HOH A O   1 
HETATM 2068 O  O   . HOH I 6 .   ? -17.753 9.625   6.313   1.00 50.43 ? 652 HOH A O   1 
HETATM 2069 O  O   . HOH I 6 .   ? -17.559 10.876  9.140   1.00 61.16 ? 653 HOH A O   1 
HETATM 2070 O  O   . HOH I 6 .   ? -44.957 4.541   37.106  1.00 52.76 ? 654 HOH A O   1 
HETATM 2071 O  O   . HOH I 6 .   ? -21.253 6.691   21.091  1.00 53.72 ? 655 HOH A O   1 
HETATM 2072 O  O   . HOH I 6 .   ? -43.752 -4.789  -1.997  1.00 38.14 ? 656 HOH A O   1 
HETATM 2073 O  O   . HOH I 6 .   ? -21.297 2.365   18.851  1.00 44.99 ? 657 HOH A O   1 
HETATM 2074 O  O   . HOH I 6 .   ? -26.604 -0.000  26.854  0.50 68.05 ? 658 HOH A O   1 
HETATM 2075 O  O   . HOH I 6 .   ? -24.239 3.093   23.053  1.00 47.21 ? 659 HOH A O   1 
HETATM 2076 O  O   . HOH I 6 .   ? -18.985 7.423   12.464  1.00 57.97 ? 660 HOH A O   1 
HETATM 2077 O  O   . HOH I 6 .   ? -48.144 1.645   -2.791  1.00 64.43 ? 661 HOH A O   1 
HETATM 2078 O  O   . HOH I 6 .   ? -24.354 1.881   25.246  1.00 57.91 ? 662 HOH A O   1 
HETATM 2079 O  O   . HOH I 6 .   ? -47.971 1.929   -0.226  1.00 51.51 ? 663 HOH A O   1 
HETATM 2080 O  O   . HOH I 6 .   ? -19.026 28.532  13.767  1.00 55.08 ? 664 HOH A O   1 
HETATM 2081 O  O   . HOH I 6 .   ? -19.583 4.879   8.508   1.00 59.42 ? 665 HOH A O   1 
HETATM 2082 O  O   . HOH I 6 .   ? -33.577 27.123  23.086  1.00 56.78 ? 666 HOH A O   1 
HETATM 2083 O  O   . HOH I 6 .   ? -22.717 2.554   28.978  1.00 60.45 ? 667 HOH A O   1 
HETATM 2084 O  O   . HOH I 6 .   ? -52.003 0.892   -3.968  1.00 66.69 ? 668 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLN A 3   ? 0.8547 0.8292 0.7019 -0.0963 -0.0402 -0.0518 3   GLN A N   
2    C CA  . GLN A 3   ? 0.8454 0.8149 0.6954 -0.0932 -0.0396 -0.0468 3   GLN A CA  
3    C C   . GLN A 3   ? 0.7284 0.6826 0.5731 -0.0901 -0.0384 -0.0398 3   GLN A C   
4    O O   . GLN A 3   ? 0.7767 0.7251 0.6175 -0.0868 -0.0386 -0.0383 3   GLN A O   
5    C CB  . GLN A 3   ? 0.9252 0.9043 0.7835 -0.0872 -0.0419 -0.0483 3   GLN A CB  
6    C CG  . GLN A 3   ? 0.8756 0.8560 0.7352 -0.0794 -0.0443 -0.0485 3   GLN A CG  
7    C CD  . GLN A 3   ? 0.8335 0.8210 0.7002 -0.0730 -0.0465 -0.0493 3   GLN A CD  
8    O OE1 . GLN A 3   ? 0.7589 0.7482 0.6294 -0.0734 -0.0462 -0.0486 3   GLN A OE1 
9    N NE2 . GLN A 3   ? 0.8387 0.8296 0.7066 -0.0668 -0.0488 -0.0507 3   GLN A NE2 
10   N N   . GLU A 4   ? 0.6527 0.6003 0.4969 -0.0915 -0.0370 -0.0354 4   GLU A N   
11   C CA  . GLU A 4   ? 0.5983 0.5320 0.4374 -0.0896 -0.0356 -0.0290 4   GLU A CA  
12   C C   . GLU A 4   ? 0.6137 0.5449 0.4566 -0.0810 -0.0367 -0.0249 4   GLU A C   
13   O O   . GLU A 4   ? 0.5980 0.5352 0.4474 -0.0779 -0.0382 -0.0250 4   GLU A O   
14   C CB  . GLU A 4   ? 0.6369 0.5676 0.4759 -0.0937 -0.0344 -0.0266 4   GLU A CB  
15   C CG  . GLU A 4   ? 0.7061 0.6384 0.5404 -0.1026 -0.0329 -0.0304 4   GLU A CG  
16   C CD  . GLU A 4   ? 0.7756 0.7025 0.6077 -0.1067 -0.0315 -0.0274 4   GLU A CD  
17   O OE1 . GLU A 4   ? 0.7388 0.6549 0.5680 -0.1041 -0.0309 -0.0216 4   GLU A OE1 
18   O OE2 . GLU A 4   ? 0.9249 0.8584 0.7580 -0.1123 -0.0311 -0.0308 4   GLU A OE2 
19   N N   . GLN A 5   ? 0.5176 0.4401 0.3561 -0.0772 -0.0360 -0.0215 5   GLN A N   
20   C CA  . GLN A 5   ? 0.5583 0.4783 0.4002 -0.0694 -0.0368 -0.0174 5   GLN A CA  
21   C C   . GLN A 5   ? 0.5404 0.4479 0.3772 -0.0671 -0.0347 -0.0115 5   GLN A C   
22   O O   . GLN A 5   ? 0.5406 0.4416 0.3701 -0.0700 -0.0332 -0.0117 5   GLN A O   
23   C CB  . GLN A 5   ? 0.6056 0.5289 0.4468 -0.0650 -0.0382 -0.0201 5   GLN A CB  
24   C CG  . GLN A 5   ? 0.7584 0.6948 0.6038 -0.0662 -0.0405 -0.0267 5   GLN A CG  
25   C CD  . GLN A 5   ? 0.8057 0.7442 0.6493 -0.0618 -0.0421 -0.0290 5   GLN A CD  
26   O OE1 . GLN A 5   ? 0.7888 0.7237 0.6330 -0.0550 -0.0426 -0.0258 5   GLN A OE1 
27   N NE2 . GLN A 5   ? 0.9184 0.8618 0.7590 -0.0658 -0.0427 -0.0343 5   GLN A NE2 
28   N N   . LEU A 6   ? 0.5089 0.4134 0.3496 -0.0615 -0.0347 -0.0065 6   LEU A N   
29   C CA  . LEU A 6   ? 0.4749 0.3693 0.3127 -0.0576 -0.0328 -0.0005 6   LEU A CA  
30   C C   . LEU A 6   ? 0.5271 0.4223 0.3673 -0.0506 -0.0335 0.0008  6   LEU A C   
31   O O   . LEU A 6   ? 0.5413 0.4408 0.3880 -0.0479 -0.0348 0.0019  6   LEU A O   
32   C CB  . LEU A 6   ? 0.4573 0.3485 0.2986 -0.0582 -0.0321 0.0044  6   LEU A CB  
33   C CG  . LEU A 6   ? 0.5225 0.4131 0.3617 -0.0650 -0.0317 0.0033  6   LEU A CG  
34   C CD1 . LEU A 6   ? 0.4378 0.3251 0.2810 -0.0638 -0.0315 0.0090  6   LEU A CD1 
35   C CD2 . LEU A 6   ? 0.5231 0.4053 0.3532 -0.0676 -0.0297 0.0033  6   LEU A CD2 
36   N N   . GLN A 7   ? 0.4876 0.3786 0.3221 -0.0480 -0.0327 0.0005  7   GLN A N   
37   C CA  . GLN A 7   ? 0.5137 0.4057 0.3489 -0.0417 -0.0336 0.0009  7   GLN A CA  
38   C C   . GLN A 7   ? 0.5134 0.3960 0.3464 -0.0366 -0.0311 0.0073  7   GLN A C   
39   O O   . GLN A 7   ? 0.5357 0.4106 0.3621 -0.0369 -0.0289 0.0088  7   GLN A O   
40   C CB  . GLN A 7   ? 0.5468 0.4424 0.3773 -0.0424 -0.0350 -0.0048 7   GLN A CB  
41   C CG  . GLN A 7   ? 0.6784 0.5723 0.5070 -0.0356 -0.0355 -0.0038 7   GLN A CG  
42   C CD  . GLN A 7   ? 0.7869 0.6828 0.6096 -0.0361 -0.0369 -0.0089 7   GLN A CD  
43   O OE1 . GLN A 7   ? 0.8199 0.7247 0.6442 -0.0397 -0.0391 -0.0147 7   GLN A OE1 
44   N NE2 . GLN A 7   ? 0.8233 0.7113 0.6391 -0.0326 -0.0355 -0.0068 7   GLN A NE2 
45   N N   . GLN A 8   ? 0.4782 0.3616 0.3167 -0.0320 -0.0312 0.0110  8   GLN A N   
46   C CA  . GLN A 8   ? 0.4836 0.3597 0.3216 -0.0273 -0.0287 0.0172  8   GLN A CA  
47   C C   . GLN A 8   ? 0.4864 0.3627 0.3240 -0.0213 -0.0292 0.0178  8   GLN A C   
48   O O   . GLN A 8   ? 0.4895 0.3720 0.3314 -0.0204 -0.0317 0.0155  8   GLN A O   
49   C CB  . GLN A 8   ? 0.4950 0.3719 0.3405 -0.0275 -0.0284 0.0217  8   GLN A CB  
50   C CG  . GLN A 8   ? 0.4708 0.3462 0.3164 -0.0326 -0.0278 0.0223  8   GLN A CG  
51   C CD  . GLN A 8   ? 0.4756 0.3517 0.3283 -0.0326 -0.0277 0.0269  8   GLN A CD  
52   O OE1 . GLN A 8   ? 0.4617 0.3434 0.3194 -0.0355 -0.0298 0.0252  8   GLN A OE1 
53   N NE2 . GLN A 8   ? 0.4790 0.3498 0.3324 -0.0291 -0.0253 0.0327  8   GLN A NE2 
54   N N   . PRO A 9   ? 0.6396 0.5089 0.4724 -0.0168 -0.0268 0.0211  9   PRO A N   
55   C CA  . PRO A 9   ? 0.5898 0.4585 0.4223 -0.0109 -0.0270 0.0227  9   PRO A CA  
56   C C   . PRO A 9   ? 0.6810 0.5520 0.5213 -0.0090 -0.0274 0.0262  9   PRO A C   
57   O O   . PRO A 9   ? 0.5733 0.4447 0.4194 -0.0111 -0.0266 0.0293  9   PRO A O   
58   C CB  . PRO A 9   ? 0.6732 0.5332 0.4997 -0.0073 -0.0234 0.0268  9   PRO A CB  
59   C CG  . PRO A 9   ? 0.7546 0.6116 0.5823 -0.0106 -0.0213 0.0294  9   PRO A CG  
60   C CD  . PRO A 9   ? 0.6740 0.5352 0.5011 -0.0168 -0.0236 0.0240  9   PRO A CD  
61   N N   . GLY A 10  ? 0.6477 0.5200 0.4882 -0.0048 -0.0288 0.0259  10  GLY A N   
62   C CA  . GLY A 10  ? 0.5932 0.4676 0.4409 -0.0037 -0.0296 0.0285  10  GLY A CA  
63   C C   . GLY A 10  ? 0.6596 0.5287 0.5101 -0.0015 -0.0263 0.0357  10  GLY A C   
64   O O   . GLY A 10  ? 0.5403 0.4112 0.3980 -0.0031 -0.0266 0.0383  10  GLY A O   
65   N N   . THR A 11  ? 0.5947 0.4576 0.4396 0.0023  -0.0233 0.0387  11  THR A N   
66   C CA  . THR A 11  ? 0.5963 0.4545 0.4431 0.0052  -0.0198 0.0454  11  THR A CA  
67   C C   . THR A 11  ? 0.7118 0.5640 0.5522 0.0075  -0.0161 0.0478  11  THR A C   
68   O O   . THR A 11  ? 0.7480 0.5976 0.5803 0.0087  -0.0162 0.0447  11  THR A O   
69   C CB  . THR A 11  ? 0.6236 0.4798 0.4693 0.0098  -0.0199 0.0472  11  THR A CB  
70   O OG1 . THR A 11  ? 0.6285 0.4831 0.4658 0.0127  -0.0210 0.0435  11  THR A OG1 
71   C CG2 . THR A 11  ? 0.6258 0.4861 0.4776 0.0086  -0.0230 0.0460  11  THR A CG2 
72   N N   . GLU A 12  ? 0.6610 0.5106 0.5050 0.0085  -0.0126 0.0536  12  GLU A N   
73   C CA  . GLU A 12  ? 0.6958 0.5394 0.5344 0.0119  -0.0084 0.0569  12  GLU A CA  
74   C C   . GLU A 12  ? 0.7164 0.5587 0.5595 0.0149  -0.0053 0.0632  12  GLU A C   
75   O O   . GLU A 12  ? 0.5804 0.4262 0.4323 0.0126  -0.0052 0.0661  12  GLU A O   
76   C CB  . GLU A 12  ? 0.6009 0.4437 0.4401 0.0092  -0.0071 0.0574  12  GLU A CB  
77   C CG  . GLU A 12  ? 0.6853 0.5281 0.5186 0.0060  -0.0095 0.0514  12  GLU A CG  
78   C CD  . GLU A 12  ? 0.7675 0.6055 0.5901 0.0084  -0.0091 0.0482  12  GLU A CD  
79   O OE1 . GLU A 12  ? 0.7472 0.5800 0.5645 0.0130  -0.0063 0.0507  12  GLU A OE1 
80   O OE2 . GLU A 12  ? 0.8059 0.6459 0.6253 0.0050  -0.0120 0.0427  12  GLU A OE2 
81   N N   . LEU A 13  ? 0.6896 0.5269 0.5263 0.0196  -0.0027 0.0650  13  LEU A N   
82   C CA  . LEU A 13  ? 0.6297 0.4652 0.4697 0.0224  0.0007  0.0711  13  LEU A CA  
83   C C   . LEU A 13  ? 0.6278 0.4592 0.4649 0.0253  0.0059  0.0750  13  LEU A C   
84   O O   . LEU A 13  ? 0.6205 0.4467 0.4481 0.0285  0.0075  0.0738  13  LEU A O   
85   C CB  . LEU A 13  ? 0.6176 0.4504 0.4524 0.0256  0.0000  0.0705  13  LEU A CB  
86   C CG  . LEU A 13  ? 0.6100 0.4410 0.4483 0.0278  0.0032  0.0765  13  LEU A CG  
87   C CD1 . LEU A 13  ? 0.5787 0.4143 0.4272 0.0243  0.0013  0.0780  13  LEU A CD1 
88   C CD2 . LEU A 13  ? 0.6201 0.4465 0.4506 0.0317  0.0028  0.0760  13  LEU A CD2 
89   N N   . VAL A 14  ? 0.5906 0.4243 0.4355 0.0245  0.0086  0.0797  14  VAL A N   
90   C CA  . VAL A 14  ? 0.5571 0.3880 0.4000 0.0267  0.0128  0.0823  14  VAL A CA  
91   C C   . VAL A 14  ? 0.6077 0.4401 0.4575 0.0287  0.0173  0.0890  14  VAL A C   
92   O O   . VAL A 14  ? 0.6131 0.4499 0.4712 0.0267  0.0164  0.0913  14  VAL A O   
93   C CB  . VAL A 14  ? 0.5507 0.3839 0.3965 0.0231  0.0109  0.0804  14  VAL A CB  
94   C CG1 . VAL A 14  ? 0.5953 0.4270 0.4339 0.0209  0.0070  0.0738  14  VAL A CG1 
95   C CG2 . VAL A 14  ? 0.5622 0.4024 0.4198 0.0190  0.0085  0.0819  14  VAL A CG2 
96   N N   . LYS A 15  ? 0.6500 0.4788 0.4961 0.0327  0.0222  0.0920  15  LYS A N   
97   C CA  . LYS A 15  ? 0.6473 0.4779 0.4994 0.0350  0.0273  0.0984  15  LYS A CA  
98   C C   . LYS A 15  ? 0.6462 0.4823 0.5079 0.0334  0.0279  0.1011  15  LYS A C   
99   O O   . LYS A 15  ? 0.6746 0.5098 0.5344 0.0325  0.0264  0.0986  15  LYS A O   
100  C CB  . LYS A 15  ? 0.7529 0.5773 0.5960 0.0406  0.0326  0.1001  15  LYS A CB  
101  C CG  . LYS A 15  ? 0.7959 0.6131 0.6260 0.0430  0.0319  0.0964  15  LYS A CG  
102  C CD  . LYS A 15  ? 0.7651 0.5753 0.5850 0.0486  0.0371  0.0978  15  LYS A CD  
103  C CE  . LYS A 15  ? 0.8202 0.6308 0.6426 0.0514  0.0421  0.1035  15  LYS A CE  
104  N NZ  . LYS A 15  ? 0.8576 0.6608 0.6684 0.0567  0.0466  0.1044  15  LYS A NZ  
105  N N   . PRO A 16  ? 0.6282 0.4700 0.5005 0.0330  0.0302  0.1063  16  PRO A N   
106  C CA  . PRO A 16  ? 0.6410 0.4881 0.5222 0.0326  0.0314  0.1094  16  PRO A CA  
107  C C   . PRO A 16  ? 0.6601 0.5028 0.5348 0.0373  0.0353  0.1100  16  PRO A C   
108  O O   . PRO A 16  ? 0.6532 0.4905 0.5199 0.0415  0.0392  0.1106  16  PRO A O   
109  C CB  . PRO A 16  ? 0.6789 0.5323 0.5708 0.0323  0.0343  0.1151  16  PRO A CB  
110  C CG  . PRO A 16  ? 0.6328 0.4843 0.5226 0.0304  0.0327  0.1141  16  PRO A CG  
111  C CD  . PRO A 16  ? 0.6416 0.4848 0.5175 0.0328  0.0317  0.1094  16  PRO A CD  
112  N N   . GLY A 17  ? 0.6394 0.4834 0.5165 0.0365  0.0339  0.1094  17  GLY A N   
113  C CA  . GLY A 17  ? 0.6964 0.5357 0.5676 0.0412  0.0376  0.1102  17  GLY A CA  
114  C C   . GLY A 17  ? 0.6889 0.5194 0.5470 0.0413  0.0356  0.1046  17  GLY A C   
115  O O   . GLY A 17  ? 0.7152 0.5415 0.5687 0.0436  0.0370  0.1043  17  GLY A O   
116  N N   . ALA A 18  ? 0.6736 0.5013 0.5256 0.0387  0.0323  0.1002  18  ALA A N   
117  C CA  . ALA A 18  ? 0.6386 0.4590 0.4788 0.0381  0.0301  0.0947  18  ALA A CA  
118  C C   . ALA A 18  ? 0.6549 0.4768 0.4973 0.0334  0.0257  0.0918  18  ALA A C   
119  O O   . ALA A 18  ? 0.6433 0.4720 0.4962 0.0309  0.0241  0.0941  18  ALA A O   
120  C CB  . ALA A 18  ? 0.6245 0.4431 0.4588 0.0371  0.0279  0.0911  18  ALA A CB  
121  N N   . SER A 19  ? 0.6204 0.4358 0.4525 0.0322  0.0239  0.0868  19  SER A N   
122  C CA  . SER A 19  ? 0.6596 0.4753 0.4912 0.0271  0.0195  0.0830  19  SER A CA  
123  C C   . SER A 19  ? 0.6803 0.4964 0.5077 0.0235  0.0155  0.0775  19  SER A C   
124  O O   . SER A 19  ? 0.6768 0.4897 0.4976 0.0258  0.0165  0.0760  19  SER A O   
125  C CB  . SER A 19  ? 0.6715 0.4787 0.4935 0.0282  0.0207  0.0813  19  SER A CB  
126  O OG  . SER A 19  ? 0.8999 0.7076 0.7268 0.0312  0.0236  0.0861  19  SER A OG  
127  N N   . VAL A 20  ? 0.6225 0.4427 0.4535 0.0180  0.0111  0.0744  20  VAL A N   
128  C CA  . VAL A 20  ? 0.5966 0.4175 0.4233 0.0147  0.0074  0.0687  20  VAL A CA  
129  C C   . VAL A 20  ? 0.5858 0.4059 0.4098 0.0095  0.0044  0.0646  20  VAL A C   
130  O O   . VAL A 20  ? 0.5967 0.4185 0.4257 0.0074  0.0039  0.0664  20  VAL A O   
131  C CB  . VAL A 20  ? 0.5794 0.4076 0.4138 0.0133  0.0050  0.0688  20  VAL A CB  
132  C CG1 . VAL A 20  ? 0.5803 0.4152 0.4253 0.0095  0.0027  0.0703  20  VAL A CG1 
133  C CG2 . VAL A 20  ? 0.6115 0.4405 0.4409 0.0114  0.0015  0.0630  20  VAL A CG2 
134  N N   . ARG A 21  ? 0.5946 0.4118 0.4101 0.0075  0.0026  0.0591  21  ARG A N   
135  C CA  . ARG A 21  ? 0.5833 0.3999 0.3960 0.0020  0.0000  0.0549  21  ARG A CA  
136  C C   . ARG A 21  ? 0.5960 0.4197 0.4117 -0.0022 -0.0042 0.0503  21  ARG A C   
137  O O   . ARG A 21  ? 0.6020 0.4265 0.4141 -0.0012 -0.0053 0.0472  21  ARG A O   
138  C CB  . ARG A 21  ? 0.6442 0.4518 0.4444 0.0021  0.0011  0.0518  21  ARG A CB  
139  C CG  . ARG A 21  ? 0.6924 0.4978 0.4897 -0.0035 -0.0006 0.0489  21  ARG A CG  
140  C CD  . ARG A 21  ? 0.8391 0.6336 0.6240 -0.0033 0.0011  0.0471  21  ARG A CD  
141  N NE  . ARG A 21  ? 0.8962 0.6908 0.6747 -0.0046 -0.0004 0.0418  21  ARG A NE  
142  C CZ  . ARG A 21  ? 0.9981 0.7874 0.7674 -0.0086 -0.0014 0.0370  21  ARG A CZ  
143  N NH1 . ARG A 21  ? 0.9548 0.7373 0.7194 -0.0112 -0.0006 0.0372  21  ARG A NH1 
144  N NH2 . ARG A 21  ? 0.9270 0.7182 0.6919 -0.0097 -0.0034 0.0322  21  ARG A NH2 
145  N N   . LEU A 22  ? 0.5771 0.4063 0.3997 -0.0066 -0.0067 0.0498  22  LEU A N   
146  C CA  . LEU A 22  ? 0.5749 0.4114 0.4009 -0.0107 -0.0106 0.0453  22  LEU A CA  
147  C C   . LEU A 22  ? 0.5999 0.4350 0.4197 -0.0160 -0.0123 0.0400  22  LEU A C   
148  O O   . LEU A 22  ? 0.5430 0.3730 0.3595 -0.0178 -0.0111 0.0410  22  LEU A O   
149  C CB  . LEU A 22  ? 0.5038 0.3464 0.3401 -0.0128 -0.0120 0.0479  22  LEU A CB  
150  C CG  . LEU A 22  ? 0.5645 0.4091 0.4081 -0.0085 -0.0104 0.0534  22  LEU A CG  
151  C CD1 . LEU A 22  ? 0.5739 0.4253 0.4274 -0.0112 -0.0127 0.0547  22  LEU A CD1 
152  C CD2 . LEU A 22  ? 0.5472 0.3916 0.3886 -0.0046 -0.0098 0.0529  22  LEU A CD2 
153  N N   . SER A 23  ? 0.5498 0.3897 0.3683 -0.0186 -0.0151 0.0345  23  SER A N   
154  C CA  . SER A 23  ? 0.5392 0.3784 0.3519 -0.0241 -0.0165 0.0291  23  SER A CA  
155  C C   . SER A 23  ? 0.5671 0.4155 0.3862 -0.0290 -0.0197 0.0257  23  SER A C   
156  O O   . SER A 23  ? 0.5371 0.3922 0.3631 -0.0274 -0.0214 0.0258  23  SER A O   
157  C CB  . SER A 23  ? 0.5967 0.4334 0.4011 -0.0233 -0.0167 0.0250  23  SER A CB  
158  O OG  . SER A 23  ? 0.6264 0.4690 0.4342 -0.0201 -0.0184 0.0239  23  SER A OG  
159  N N   . CYS A 24  ? 0.5237 0.3717 0.3398 -0.0349 -0.0205 0.0226  24  CYS A N   
160  C CA  . CYS A 24  ? 0.5563 0.4125 0.3769 -0.0401 -0.0231 0.0187  24  CYS A CA  
161  C C   . CYS A 24  ? 0.5608 0.4164 0.3741 -0.0453 -0.0237 0.0129  24  CYS A C   
162  O O   . CYS A 24  ? 0.5438 0.3931 0.3517 -0.0490 -0.0224 0.0132  24  CYS A O   
163  C CB  . CYS A 24  ? 0.4973 0.3529 0.3221 -0.0424 -0.0228 0.0222  24  CYS A CB  
164  S SG  . CYS A 24  ? 0.6140 0.4782 0.4428 -0.0495 -0.0256 0.0175  24  CYS A SG  
165  N N   . LYS A 25  ? 0.5516 0.4134 0.3645 -0.0455 -0.0257 0.0079  25  LYS A N   
166  C CA  . LYS A 25  ? 0.5827 0.4452 0.3893 -0.0504 -0.0265 0.0021  25  LYS A CA  
167  C C   . LYS A 25  ? 0.6171 0.4883 0.4279 -0.0569 -0.0283 -0.0020 25  LYS A C   
168  O O   . LYS A 25  ? 0.5806 0.4615 0.3987 -0.0560 -0.0304 -0.0039 25  LYS A O   
169  C CB  . LYS A 25  ? 0.5856 0.4511 0.3900 -0.0470 -0.0279 -0.0010 25  LYS A CB  
170  C CG  . LYS A 25  ? 0.6690 0.5351 0.4665 -0.0520 -0.0288 -0.0071 25  LYS A CG  
171  N N   . THR A 26  ? 0.5403 0.4078 0.3464 -0.0634 -0.0273 -0.0033 26  THR A N   
172  C CA  . THR A 26  ? 0.5522 0.4273 0.3623 -0.0694 -0.0285 -0.0065 26  THR A CA  
173  C C   . THR A 26  ? 0.5653 0.4466 0.3726 -0.0747 -0.0297 -0.0135 26  THR A C   
174  O O   . THR A 26  ? 0.5557 0.4320 0.3558 -0.0753 -0.0291 -0.0152 26  THR A O   
175  C CB  . THR A 26  ? 0.5310 0.3986 0.3378 -0.0735 -0.0267 -0.0035 26  THR A CB  
176  O OG1 . THR A 26  ? 0.5363 0.3956 0.3332 -0.0776 -0.0252 -0.0051 26  THR A OG1 
177  C CG2 . THR A 26  ? 0.5125 0.3733 0.3213 -0.0681 -0.0254 0.0035  26  THR A CG2 
178  N N   . SER A 27  ? 0.5485 0.4406 0.3613 -0.0788 -0.0311 -0.0175 27  SER A N   
179  C CA  . SER A 27  ? 0.5485 0.4479 0.3596 -0.0848 -0.0321 -0.0243 27  SER A CA  
180  C C   . SER A 27  ? 0.5976 0.5059 0.4136 -0.0905 -0.0324 -0.0271 27  SER A C   
181  O O   . SER A 27  ? 0.5574 0.4677 0.3790 -0.0887 -0.0327 -0.0244 27  SER A O   
182  C CB  . SER A 27  ? 0.6318 0.5394 0.4453 -0.0809 -0.0344 -0.0282 27  SER A CB  
183  O OG  . SER A 27  ? 0.6564 0.5720 0.4785 -0.0756 -0.0362 -0.0275 27  SER A OG  
184  N N   . GLY A 28  ? 0.5782 0.4917 0.3918 -0.0976 -0.0324 -0.0327 28  GLY A N   
185  C CA  . GLY A 28  ? 0.5837 0.5075 0.4026 -0.1027 -0.0327 -0.0360 28  GLY A CA  
186  C C   . GLY A 28  ? 0.6096 0.5263 0.4240 -0.1090 -0.0304 -0.0339 28  GLY A C   
187  O O   . GLY A 28  ? 0.5729 0.4974 0.3905 -0.1138 -0.0303 -0.0367 28  GLY A O   
188  N N   . TYR A 29  ? 0.5652 0.4673 0.3721 -0.1086 -0.0287 -0.0289 29  TYR A N   
189  C CA  . TYR A 29  ? 0.5676 0.4617 0.3691 -0.1143 -0.0267 -0.0266 29  TYR A CA  
190  C C   . TYR A 29  ? 0.5687 0.4470 0.3601 -0.1139 -0.0249 -0.0230 29  TYR A C   
191  O O   . TYR A 29  ? 0.5523 0.4264 0.3419 -0.1088 -0.0252 -0.0219 29  TYR A O   
192  C CB  . TYR A 29  ? 0.5281 0.4228 0.3352 -0.1113 -0.0270 -0.0223 29  TYR A CB  
193  C CG  . TYR A 29  ? 0.5568 0.4428 0.3644 -0.1034 -0.0271 -0.0158 29  TYR A CG  
194  C CD1 . TYR A 29  ? 0.5252 0.4159 0.3392 -0.0959 -0.0286 -0.0149 29  TYR A CD1 
195  C CD2 . TYR A 29  ? 0.5404 0.4134 0.3417 -0.1032 -0.0255 -0.0106 29  TYR A CD2 
196  C CE1 . TYR A 29  ? 0.5300 0.4132 0.3445 -0.0892 -0.0283 -0.0090 29  TYR A CE1 
197  C CE2 . TYR A 29  ? 0.5416 0.4078 0.3440 -0.0961 -0.0253 -0.0047 29  TYR A CE2 
198  C CZ  . TYR A 29  ? 0.5527 0.4243 0.3619 -0.0893 -0.0266 -0.0040 29  TYR A CZ  
199  O OH  . TYR A 29  ? 0.5306 0.3952 0.3404 -0.0828 -0.0259 0.0018  29  TYR A OH  
200  N N   . THR A 30  ? 0.5573 0.4257 0.3414 -0.1190 -0.0230 -0.0208 30  THR A N   
201  C CA  . THR A 30  ? 0.5667 0.4193 0.3403 -0.1187 -0.0213 -0.0177 30  THR A CA  
202  C C   . THR A 30  ? 0.6041 0.4488 0.3789 -0.1105 -0.0211 -0.0108 30  THR A C   
203  O O   . THR A 30  ? 0.5686 0.4102 0.3443 -0.1103 -0.0208 -0.0069 30  THR A O   
204  C CB  . THR A 30  ? 0.6114 0.4556 0.3764 -0.1267 -0.0194 -0.0175 30  THR A CB  
205  O OG1 . THR A 30  ? 0.6300 0.4830 0.3949 -0.1347 -0.0194 -0.0241 30  THR A OG1 
206  C CG2 . THR A 30  ? 0.6311 0.4581 0.3846 -0.1259 -0.0176 -0.0144 30  THR A CG2 
207  N N   . PHE A 31  ? 0.5750 0.4161 0.3492 -0.1042 -0.0211 -0.0093 31  PHE A N   
208  C CA  . PHE A 31  ? 0.5428 0.3789 0.3198 -0.0958 -0.0208 -0.0031 31  PHE A CA  
209  C C   . PHE A 31  ? 0.6272 0.4502 0.3975 -0.0960 -0.0191 0.0019  31  PHE A C   
210  O O   . PHE A 31  ? 0.5523 0.3742 0.3270 -0.0915 -0.0192 0.0069  31  PHE A O   
211  C CB  . PHE A 31  ? 0.5568 0.3893 0.3303 -0.0913 -0.0205 -0.0037 31  PHE A CB  
212  C CG  . PHE A 31  ? 0.5994 0.4249 0.3737 -0.0826 -0.0195 0.0023  31  PHE A CG  
213  C CD1 . PHE A 31  ? 0.6138 0.4464 0.3981 -0.0770 -0.0205 0.0054  31  PHE A CD1 
214  C CD2 . PHE A 31  ? 0.5932 0.4054 0.3582 -0.0802 -0.0174 0.0047  31  PHE A CD2 
215  C CE1 . PHE A 31  ? 0.6271 0.4543 0.4126 -0.0695 -0.0193 0.0110  31  PHE A CE1 
216  C CE2 . PHE A 31  ? 0.5565 0.3631 0.3225 -0.0723 -0.0161 0.0103  31  PHE A CE2 
217  C CZ  . PHE A 31  ? 0.6124 0.4271 0.3891 -0.0671 -0.0170 0.0134  31  PHE A CZ  
218  N N   . ALA A 32  ? 0.6188 0.4314 0.3780 -0.1012 -0.0175 0.0005  32  ALA A N   
219  C CA  . ALA A 32  ? 0.6191 0.4170 0.3700 -0.1004 -0.0158 0.0053  32  ALA A CA  
220  C C   . ALA A 32  ? 0.6086 0.4076 0.3622 -0.1028 -0.0163 0.0080  32  ALA A C   
221  O O   . ALA A 32  ? 0.6856 0.4755 0.4364 -0.0993 -0.0155 0.0134  32  ALA A O   
222  C CB  . ALA A 32  ? 0.6671 0.4534 0.4048 -0.1063 -0.0141 0.0026  32  ALA A CB  
223  N N   . SER A 33  ? 0.5485 0.3590 0.3077 -0.1080 -0.0175 0.0044  33  SER A N   
224  C CA  . SER A 33  ? 0.5646 0.3753 0.3235 -0.1126 -0.0177 0.0055  33  SER A CA  
225  C C   . SER A 33  ? 0.5751 0.3937 0.3444 -0.1082 -0.0195 0.0088  33  SER A C   
226  O O   . SER A 33  ? 0.5576 0.3758 0.3263 -0.1115 -0.0199 0.0101  33  SER A O   
227  C CB  . SER A 33  ? 0.5893 0.4064 0.3463 -0.1218 -0.0176 -0.0004 33  SER A CB  
228  O OG  . SER A 33  ? 0.6489 0.4570 0.3951 -0.1270 -0.0158 -0.0031 33  SER A OG  
229  N N   . TYR A 34  ? 0.5298 0.3552 0.3082 -0.1012 -0.0207 0.0102  34  TYR A N   
230  C CA  . TYR A 34  ? 0.5236 0.3567 0.3118 -0.0980 -0.0224 0.0128  34  TYR A CA  
231  C C   . TYR A 34  ? 0.5788 0.4088 0.3712 -0.0896 -0.0225 0.0184  34  TYR A C   
232  O O   . TYR A 34  ? 0.5410 0.3706 0.3341 -0.0852 -0.0219 0.0182  34  TYR A O   
233  C CB  . TYR A 34  ? 0.5125 0.3599 0.3094 -0.0988 -0.0240 0.0080  34  TYR A CB  
234  C CG  . TYR A 34  ? 0.5290 0.3819 0.3236 -0.1070 -0.0239 0.0026  34  TYR A CG  
235  C CD1 . TYR A 34  ? 0.5324 0.3852 0.3214 -0.1119 -0.0228 -0.0022 34  TYR A CD1 
236  C CD2 . TYR A 34  ? 0.4923 0.3506 0.2906 -0.1099 -0.0249 0.0024  34  TYR A CD2 
237  C CE1 . TYR A 34  ? 0.5432 0.4014 0.3303 -0.1199 -0.0224 -0.0071 34  TYR A CE1 
238  C CE2 . TYR A 34  ? 0.5085 0.3718 0.3044 -0.1176 -0.0245 -0.0023 34  TYR A CE2 
239  C CZ  . TYR A 34  ? 0.5388 0.4022 0.3293 -0.1227 -0.0231 -0.0070 34  TYR A CZ  
240  O OH  . TYR A 34  ? 0.5491 0.4184 0.3383 -0.1303 -0.0224 -0.0114 34  TYR A OH  
241  N N   . THR A 35  ? 0.5163 0.3447 0.3118 -0.0873 -0.0233 0.0232  35  THR A N   
242  C CA  . THR A 35  ? 0.5261 0.3532 0.3270 -0.0796 -0.0234 0.0286  35  THR A CA  
243  C C   . THR A 35  ? 0.5150 0.3527 0.3256 -0.0760 -0.0244 0.0271  35  THR A C   
244  O O   . THR A 35  ? 0.5170 0.3641 0.3329 -0.0787 -0.0260 0.0237  35  THR A O   
245  C CB  . THR A 35  ? 0.5157 0.3419 0.3193 -0.0792 -0.0247 0.0332  35  THR A CB  
246  O OG1 . THR A 35  ? 0.5651 0.3799 0.3585 -0.0817 -0.0236 0.0349  35  THR A OG1 
247  C CG2 . THR A 35  ? 0.5276 0.3543 0.3384 -0.0718 -0.0249 0.0388  35  THR A CG2 
248  N N   . LEU A 36  ? 0.5186 0.3544 0.3312 -0.0695 -0.0234 0.0298  36  LEU A N   
249  C CA  . LEU A 36  ? 0.5162 0.3604 0.3378 -0.0653 -0.0243 0.0298  36  LEU A CA  
250  C C   . LEU A 36  ? 0.5323 0.3760 0.3603 -0.0597 -0.0243 0.0360  36  LEU A C   
251  O O   . LEU A 36  ? 0.5720 0.4078 0.3965 -0.0566 -0.0226 0.0403  36  LEU A O   
252  C CB  . LEU A 36  ? 0.5246 0.3671 0.3427 -0.0627 -0.0229 0.0275  36  LEU A CB  
253  C CG  . LEU A 36  ? 0.5741 0.4208 0.3887 -0.0679 -0.0236 0.0207  36  LEU A CG  
254  C CD1 . LEU A 36  ? 0.6102 0.4540 0.4206 -0.0647 -0.0224 0.0191  36  LEU A CD1 
255  C CD2 . LEU A 36  ? 0.5560 0.4146 0.3788 -0.0692 -0.0259 0.0176  36  LEU A CD2 
256  N N   . HIS A 37  ? 0.4677 0.3198 0.3049 -0.0586 -0.0261 0.0365  37  HIS A N   
257  C CA  . HIS A 37  ? 0.4636 0.3168 0.3080 -0.0540 -0.0263 0.0420  37  HIS A CA  
258  C C   . HIS A 37  ? 0.4775 0.3348 0.3276 -0.0491 -0.0259 0.0426  37  HIS A C   
259  O O   . HIS A 37  ? 0.4773 0.3388 0.3274 -0.0499 -0.0264 0.0383  37  HIS A O   
260  C CB  . HIS A 37  ? 0.4473 0.3069 0.2980 -0.0571 -0.0290 0.0419  37  HIS A CB  
261  C CG  . HIS A 37  ? 0.5036 0.3599 0.3490 -0.0622 -0.0298 0.0413  37  HIS A CG  
262  N ND1 . HIS A 37  ? 0.4996 0.3528 0.3460 -0.0613 -0.0304 0.0461  37  HIS A ND1 
263  C CD2 . HIS A 37  ? 0.5140 0.3694 0.3529 -0.0680 -0.0299 0.0368  37  HIS A CD2 
264  C CE1 . HIS A 37  ? 0.5440 0.3939 0.3841 -0.0665 -0.0310 0.0446  37  HIS A CE1 
265  N NE2 . HIS A 37  ? 0.5137 0.3646 0.3490 -0.0707 -0.0305 0.0391  37  HIS A NE2 
266  N N   . TRP A 38  ? 0.4909 0.3472 0.3457 -0.0441 -0.0248 0.0480  38  TRP A N   
267  C CA  . TRP A 38  ? 0.4631 0.3230 0.3236 -0.0397 -0.0242 0.0494  38  TRP A CA  
268  C C   . TRP A 38  ? 0.4917 0.3567 0.3619 -0.0388 -0.0257 0.0532  38  TRP A C   
269  O O   . TRP A 38  ? 0.4680 0.3320 0.3402 -0.0392 -0.0260 0.0568  38  TRP A O   
270  C CB  . TRP A 38  ? 0.4982 0.3519 0.3550 -0.0344 -0.0209 0.0524  38  TRP A CB  
271  C CG  . TRP A 38  ? 0.5407 0.3892 0.3879 -0.0350 -0.0196 0.0485  38  TRP A CG  
272  C CD1 . TRP A 38  ? 0.5819 0.4234 0.4203 -0.0374 -0.0187 0.0472  38  TRP A CD1 
273  C CD2 . TRP A 38  ? 0.5380 0.3873 0.3829 -0.0330 -0.0190 0.0456  38  TRP A CD2 
274  N NE1 . TRP A 38  ? 0.5769 0.4150 0.4081 -0.0372 -0.0176 0.0436  38  TRP A NE1 
275  C CE2 . TRP A 38  ? 0.5627 0.4059 0.3977 -0.0346 -0.0180 0.0424  38  TRP A CE2 
276  C CE3 . TRP A 38  ? 0.5467 0.4009 0.3963 -0.0300 -0.0195 0.0454  38  TRP A CE3 
277  C CZ2 . TRP A 38  ? 0.5991 0.4416 0.4293 -0.0331 -0.0175 0.0390  38  TRP A CZ2 
278  C CZ3 . TRP A 38  ? 0.5541 0.4071 0.3986 -0.0282 -0.0189 0.0423  38  TRP A CZ3 
279  C CH2 . TRP A 38  ? 0.5681 0.4158 0.4034 -0.0297 -0.0180 0.0391  38  TRP A CH2 
280  N N   . VAL A 39  ? 0.4520 0.3222 0.3277 -0.0376 -0.0266 0.0524  39  VAL A N   
281  C CA  . VAL A 39  ? 0.4636 0.3391 0.3481 -0.0382 -0.0286 0.0545  39  VAL A CA  
282  C C   . VAL A 39  ? 0.4902 0.3672 0.3792 -0.0339 -0.0274 0.0566  39  VAL A C   
283  O O   . VAL A 39  ? 0.4575 0.3342 0.3432 -0.0325 -0.0270 0.0534  39  VAL A O   
284  C CB  . VAL A 39  ? 0.4922 0.3725 0.3776 -0.0429 -0.0317 0.0496  39  VAL A CB  
285  C CG1 . VAL A 39  ? 0.4518 0.3370 0.3456 -0.0434 -0.0339 0.0511  39  VAL A CG1 
286  C CG2 . VAL A 39  ? 0.4760 0.3549 0.3568 -0.0477 -0.0327 0.0477  39  VAL A CG2 
287  N N   . LYS A 40  ? 0.4536 0.3321 0.3496 -0.0320 -0.0270 0.0618  40  LYS A N   
288  C CA  . LYS A 40  ? 0.4265 0.3062 0.3272 -0.0284 -0.0257 0.0644  40  LYS A CA  
289  C C   . LYS A 40  ? 0.4617 0.3461 0.3686 -0.0308 -0.0286 0.0634  40  LYS A C   
290  O O   . LYS A 40  ? 0.4948 0.3819 0.4056 -0.0341 -0.0310 0.0638  40  LYS A O   
291  C CB  . LYS A 40  ? 0.4388 0.3180 0.3441 -0.0254 -0.0233 0.0707  40  LYS A CB  
292  C CG  . LYS A 40  ? 0.4443 0.3243 0.3541 -0.0217 -0.0211 0.0742  40  LYS A CG  
293  C CD  . LYS A 40  ? 0.4841 0.3650 0.3994 -0.0191 -0.0186 0.0804  40  LYS A CD  
294  C CE  . LYS A 40  ? 0.4872 0.3694 0.4074 -0.0161 -0.0161 0.0841  40  LYS A CE  
295  N NZ  . LYS A 40  ? 0.4889 0.3721 0.4133 -0.0131 -0.0132 0.0896  40  LYS A NZ  
296  N N   . GLN A 41  ? 0.4304 0.3151 0.3377 -0.0289 -0.0284 0.0621  41  GLN A N   
297  C CA  . GLN A 41  ? 0.4358 0.3237 0.3483 -0.0307 -0.0310 0.0613  41  GLN A CA  
298  C C   . GLN A 41  ? 0.4896 0.3769 0.4066 -0.0277 -0.0293 0.0657  41  GLN A C   
299  O O   . GLN A 41  ? 0.4746 0.3589 0.3880 -0.0238 -0.0268 0.0662  41  GLN A O   
300  C CB  . GLN A 41  ? 0.4152 0.3039 0.3233 -0.0314 -0.0328 0.0552  41  GLN A CB  
301  C CG  . GLN A 41  ? 0.4373 0.3281 0.3496 -0.0323 -0.0353 0.0540  41  GLN A CG  
302  C CD  . GLN A 41  ? 0.4807 0.3727 0.3887 -0.0321 -0.0370 0.0478  41  GLN A CD  
303  O OE1 . GLN A 41  ? 0.4638 0.3542 0.3672 -0.0290 -0.0357 0.0462  41  GLN A OE1 
304  N NE2 . GLN A 41  ? 0.4357 0.3308 0.3448 -0.0354 -0.0398 0.0440  41  GLN A NE2 
305  N N   . THR A 42  ? 0.4727 0.3626 0.3973 -0.0296 -0.0306 0.0687  42  THR A N   
306  C CA  . THR A 42  ? 0.4660 0.3555 0.3952 -0.0278 -0.0293 0.0724  42  THR A CA  
307  C C   . THR A 42  ? 0.4885 0.3798 0.4221 -0.0311 -0.0326 0.0711  42  THR A C   
308  O O   . THR A 42  ? 0.4922 0.3859 0.4269 -0.0349 -0.0357 0.0687  42  THR A O   
309  C CB  . THR A 42  ? 0.5434 0.4341 0.4782 -0.0266 -0.0266 0.0787  42  THR A CB  
310  O OG1 . THR A 42  ? 0.5304 0.4248 0.4703 -0.0300 -0.0288 0.0799  42  THR A OG1 
311  C CG2 . THR A 42  ? 0.5284 0.4168 0.4590 -0.0229 -0.0230 0.0804  42  THR A CG2 
312  N N   . PRO A 43  ? 0.5382 0.4277 0.4739 -0.0300 -0.0321 0.0727  43  PRO A N   
313  C CA  . PRO A 43  ? 0.5685 0.4585 0.5077 -0.0331 -0.0353 0.0715  43  PRO A CA  
314  C C   . PRO A 43  ? 0.6892 0.5831 0.6359 -0.0373 -0.0371 0.0743  43  PRO A C   
315  O O   . PRO A 43  ? 0.6947 0.5903 0.6425 -0.0409 -0.0406 0.0714  43  PRO A O   
316  C CB  . PRO A 43  ? 0.6109 0.4970 0.5502 -0.0305 -0.0335 0.0738  43  PRO A CB  
317  C CG  . PRO A 43  ? 0.5516 0.4352 0.4856 -0.0258 -0.0298 0.0748  43  PRO A CG  
318  C CD  . PRO A 43  ? 0.5265 0.4125 0.4597 -0.0256 -0.0286 0.0752  43  PRO A CD  
319  N N   . GLY A 44  ? 0.6139 0.5099 0.5656 -0.0366 -0.0347 0.0797  44  GLY A N   
320  C CA  . GLY A 44  ? 0.6217 0.5221 0.5815 -0.0400 -0.0362 0.0830  44  GLY A CA  
321  C C   . GLY A 44  ? 0.6858 0.5892 0.6453 -0.0418 -0.0381 0.0820  44  GLY A C   
322  O O   . GLY A 44  ? 0.7584 0.6645 0.7216 -0.0457 -0.0414 0.0817  44  GLY A O   
323  N N   . GLN A 45  ? 0.5975 0.4997 0.5519 -0.0392 -0.0361 0.0813  45  GLN A N   
324  C CA  . GLN A 45  ? 0.5831 0.4872 0.5367 -0.0407 -0.0376 0.0810  45  GLN A CA  
325  C C   . GLN A 45  ? 0.5953 0.4975 0.5414 -0.0425 -0.0396 0.0751  45  GLN A C   
326  O O   . GLN A 45  ? 0.7369 0.6397 0.6808 -0.0440 -0.0408 0.0745  45  GLN A O   
327  C CB  . GLN A 45  ? 0.6201 0.5245 0.5741 -0.0373 -0.0343 0.0851  45  GLN A CB  
328  C CG  . GLN A 45  ? 0.7136 0.6227 0.6774 -0.0373 -0.0338 0.0909  45  GLN A CG  
329  C CD  . GLN A 45  ? 0.7305 0.6401 0.6954 -0.0328 -0.0298 0.0952  45  GLN A CD  
330  O OE1 . GLN A 45  ? 0.7155 0.6227 0.6750 -0.0308 -0.0288 0.0946  45  GLN A OE1 
331  N NE2 . GLN A 45  ? 0.8019 0.7141 0.7734 -0.0312 -0.0271 0.0996  45  GLN A NE2 
332  N N   . GLY A 46  ? 0.5361 0.4363 0.4781 -0.0422 -0.0401 0.0708  46  GLY A N   
333  C CA  . GLY A 46  ? 0.5062 0.4058 0.4418 -0.0441 -0.0418 0.0651  46  GLY A CA  
334  C C   . GLY A 46  ? 0.5270 0.4244 0.4562 -0.0421 -0.0394 0.0643  46  GLY A C   
335  O O   . GLY A 46  ? 0.5097 0.4048 0.4370 -0.0383 -0.0364 0.0660  46  GLY A O   
336  N N   . LEU A 47  ? 0.4668 0.3645 0.3925 -0.0449 -0.0407 0.0622  47  LEU A N   
337  C CA  . LEU A 47  ? 0.4585 0.3532 0.3771 -0.0437 -0.0386 0.0608  47  LEU A CA  
338  C C   . LEU A 47  ? 0.4917 0.3854 0.4111 -0.0434 -0.0378 0.0652  47  LEU A C   
339  O O   . LEU A 47  ? 0.4948 0.3908 0.4185 -0.0457 -0.0400 0.0672  47  LEU A O   
340  C CB  . LEU A 47  ? 0.4385 0.3336 0.3512 -0.0470 -0.0402 0.0547  47  LEU A CB  
341  C CG  . LEU A 47  ? 0.4521 0.3491 0.3642 -0.0472 -0.0414 0.0499  47  LEU A CG  
342  C CD1 . LEU A 47  ? 0.5086 0.4070 0.4154 -0.0506 -0.0427 0.0442  47  LEU A CD1 
343  C CD2 . LEU A 47  ? 0.4912 0.3858 0.4006 -0.0428 -0.0388 0.0501  47  LEU A CD2 
344  N N   . ASP A 48  ? 0.4777 0.3677 0.3928 -0.0402 -0.0348 0.0666  48  ASP A N   
345  C CA  . ASP A 48  ? 0.5381 0.4262 0.4528 -0.0390 -0.0337 0.0704  48  ASP A CA  
346  C C   . ASP A 48  ? 0.5269 0.4096 0.4320 -0.0389 -0.0321 0.0679  48  ASP A C   
347  O O   . ASP A 48  ? 0.4794 0.3592 0.3798 -0.0366 -0.0298 0.0661  48  ASP A O   
348  C CB  . ASP A 48  ? 0.6267 0.5148 0.5460 -0.0343 -0.0308 0.0758  48  ASP A CB  
349  C CG  . ASP A 48  ? 0.8282 0.7207 0.7564 -0.0344 -0.0320 0.0807  48  ASP A CG  
350  O OD1 . ASP A 48  ? 1.0207 0.9158 0.9510 -0.0383 -0.0355 0.0799  48  ASP A OD1 
351  O OD2 . ASP A 48  ? 0.7666 0.6603 0.6994 -0.0307 -0.0295 0.0853  48  ASP A OD2 
352  N N   . TRP A 49  ? 0.4614 0.3422 0.3632 -0.0414 -0.0334 0.0680  49  TRP A N   
353  C CA  . TRP A 49  ? 0.4632 0.3378 0.3554 -0.0418 -0.0319 0.0660  49  TRP A CA  
354  C C   . TRP A 49  ? 0.5106 0.3804 0.4006 -0.0367 -0.0285 0.0699  49  TRP A C   
355  O O   . TRP A 49  ? 0.4982 0.3683 0.3923 -0.0343 -0.0283 0.0748  49  TRP A O   
356  C CB  . TRP A 49  ? 0.4523 0.3257 0.3409 -0.0463 -0.0343 0.0650  49  TRP A CB  
357  C CG  . TRP A 49  ? 0.5135 0.3797 0.3916 -0.0474 -0.0327 0.0629  49  TRP A CG  
358  C CD1 . TRP A 49  ? 0.5221 0.3862 0.3930 -0.0504 -0.0321 0.0576  49  TRP A CD1 
359  C CD2 . TRP A 49  ? 0.5046 0.3643 0.3779 -0.0456 -0.0316 0.0663  49  TRP A CD2 
360  N NE1 . TRP A 49  ? 0.5273 0.3838 0.3891 -0.0513 -0.0308 0.0575  49  TRP A NE1 
361  C CE2 . TRP A 49  ? 0.5464 0.3995 0.4091 -0.0481 -0.0303 0.0628  49  TRP A CE2 
362  C CE3 . TRP A 49  ? 0.5547 0.4136 0.4316 -0.0420 -0.0315 0.0720  49  TRP A CE3 
363  C CZ2 . TRP A 49  ? 0.5800 0.4246 0.4349 -0.0472 -0.0291 0.0648  49  TRP A CZ2 
364  C CZ3 . TRP A 49  ? 0.5875 0.4385 0.4570 -0.0404 -0.0302 0.0739  49  TRP A CZ3 
365  C CH2 . TRP A 49  ? 0.5843 0.4277 0.4425 -0.0431 -0.0291 0.0703  49  TRP A CH2 
366  N N   . ILE A 50  ? 0.4759 0.3415 0.3598 -0.0348 -0.0260 0.0679  50  ILE A N   
367  C CA  . ILE A 50  ? 0.4731 0.3336 0.3543 -0.0297 -0.0226 0.0714  50  ILE A CA  
368  C C   . ILE A 50  ? 0.5015 0.3545 0.3740 -0.0303 -0.0220 0.0713  50  ILE A C   
369  O O   . ILE A 50  ? 0.5094 0.3593 0.3821 -0.0268 -0.0206 0.0757  50  ILE A O   
370  C CB  . ILE A 50  ? 0.4918 0.3504 0.3694 -0.0270 -0.0201 0.0692  50  ILE A CB  
371  C CG1 . ILE A 50  ? 0.5074 0.3720 0.3933 -0.0253 -0.0202 0.0705  50  ILE A CG1 
372  C CG2 . ILE A 50  ? 0.5217 0.3733 0.3937 -0.0223 -0.0165 0.0717  50  ILE A CG2 
373  C CD1 . ILE A 50  ? 0.4502 0.3137 0.3320 -0.0240 -0.0190 0.0671  50  ILE A CD1 
374  N N   . GLY A 51  ? 0.4756 0.3254 0.3403 -0.0346 -0.0227 0.0664  51  GLY A N   
375  C CA  . GLY A 51  ? 0.5163 0.3578 0.3716 -0.0358 -0.0220 0.0661  51  GLY A CA  
376  C C   . GLY A 51  ? 0.5002 0.3391 0.3474 -0.0407 -0.0224 0.0601  51  GLY A C   
377  O O   . GLY A 51  ? 0.5045 0.3492 0.3544 -0.0430 -0.0235 0.0563  51  GLY A O   
378  N N   . ALA A 52  ? 0.4954 0.3259 0.3328 -0.0425 -0.0215 0.0592  52  ALA A N   
379  C CA  . ALA A 52  ? 0.5024 0.3307 0.3321 -0.0482 -0.0218 0.0535  52  ALA A CA  
380  C C   . ALA A 52  ? 0.5387 0.3557 0.3570 -0.0476 -0.0193 0.0531  52  ALA A C   
381  O O   . ALA A 52  ? 0.5522 0.3624 0.3679 -0.0435 -0.0178 0.0575  52  ALA A O   
382  C CB  . ALA A 52  ? 0.5420 0.3723 0.3712 -0.0542 -0.0243 0.0520  52  ALA A CB  
383  N N   . ILE A 53  ? 0.5478 0.3629 0.3593 -0.0517 -0.0189 0.0478  53  ILE A N   
384  C CA  . ILE A 53  ? 0.5541 0.3582 0.3538 -0.0524 -0.0167 0.0465  53  ILE A CA  
385  C C   . ILE A 53  ? 0.5800 0.3831 0.3732 -0.0604 -0.0177 0.0413  53  ILE A C   
386  O O   . ILE A 53  ? 0.5668 0.3791 0.3645 -0.0642 -0.0193 0.0373  53  ILE A O   
387  C CB  . ILE A 53  ? 0.5992 0.4016 0.3969 -0.0482 -0.0147 0.0453  53  ILE A CB  
388  C CG1 . ILE A 53  ? 0.5923 0.3817 0.3771 -0.0483 -0.0123 0.0444  53  ILE A CG1 
389  C CG2 . ILE A 53  ? 0.5651 0.3765 0.3666 -0.0502 -0.0158 0.0403  53  ILE A CG2 
390  C CD1 . ILE A 53  ? 0.6089 0.3953 0.3916 -0.0426 -0.0101 0.0447  53  ILE A CD1 
391  N N   . TYR A 54  ? 0.5769 0.3688 0.3594 -0.0630 -0.0166 0.0416  54  TYR A N   
392  C CA  . TYR A 54  ? 0.5934 0.3829 0.3682 -0.0709 -0.0167 0.0365  54  TYR A CA  
393  C C   . TYR A 54  ? 0.6388 0.4221 0.4056 -0.0709 -0.0148 0.0333  54  TYR A C   
394  O O   . TYR A 54  ? 0.6597 0.4313 0.4185 -0.0678 -0.0129 0.0357  54  TYR A O   
395  C CB  . TYR A 54  ? 0.6202 0.4001 0.3865 -0.0745 -0.0166 0.0383  54  TYR A CB  
396  C CG  . TYR A 54  ? 0.5866 0.3653 0.3456 -0.0835 -0.0166 0.0329  54  TYR A CG  
397  C CD1 . TYR A 54  ? 0.6041 0.3940 0.3689 -0.0888 -0.0183 0.0291  54  TYR A CD1 
398  C CD2 . TYR A 54  ? 0.6035 0.3695 0.3496 -0.0869 -0.0147 0.0314  54  TYR A CD2 
399  C CE1 . TYR A 54  ? 0.6587 0.4487 0.4176 -0.0972 -0.0180 0.0242  54  TYR A CE1 
400  C CE2 . TYR A 54  ? 0.6352 0.4007 0.3750 -0.0957 -0.0145 0.0265  54  TYR A CE2 
401  C CZ  . TYR A 54  ? 0.6498 0.4277 0.3963 -0.1008 -0.0161 0.0229  54  TYR A CZ  
402  O OH  . TYR A 54  ? 0.6549 0.4330 0.3955 -0.1096 -0.0155 0.0180  54  TYR A OH  
403  N N   . PRO A 55  ? 0.5864 0.3771 0.3549 -0.0739 -0.0154 0.0279  55  PRO A N   
404  C CA  . PRO A 55  ? 0.6012 0.3869 0.3632 -0.0727 -0.0139 0.0253  55  PRO A CA  
405  C C   . PRO A 55  ? 0.6684 0.4415 0.4168 -0.0779 -0.0124 0.0232  55  PRO A C   
406  O O   . PRO A 55  ? 0.6873 0.4521 0.4283 -0.0757 -0.0108 0.0226  55  PRO A O   
407  C CB  . PRO A 55  ? 0.5850 0.3835 0.3533 -0.0752 -0.0155 0.0200  55  PRO A CB  
408  C CG  . PRO A 55  ? 0.5587 0.3685 0.3391 -0.0735 -0.0175 0.0219  55  PRO A CG  
409  C CD  . PRO A 55  ? 0.5711 0.3758 0.3486 -0.0770 -0.0175 0.0244  55  PRO A CD  
410  N N   . GLY A 56  ? 0.6321 0.4035 0.3768 -0.0848 -0.0129 0.0219  56  GLY A N   
411  C CA  . GLY A 56  ? 0.7417 0.5008 0.4732 -0.0905 -0.0115 0.0200  56  GLY A CA  
412  C C   . GLY A 56  ? 0.7982 0.5414 0.5205 -0.0852 -0.0094 0.0243  56  GLY A C   
413  O O   . GLY A 56  ? 0.8291 0.5617 0.5406 -0.0873 -0.0079 0.0222  56  GLY A O   
414  N N   . ASN A 57  ? 0.7412 0.4827 0.4678 -0.0784 -0.0093 0.0303  57  ASN A N   
415  C CA  . ASN A 57  ? 0.7878 0.5149 0.5062 -0.0727 -0.0073 0.0346  57  ASN A CA  
416  C C   . ASN A 57  ? 0.7925 0.5230 0.5188 -0.0628 -0.0067 0.0391  57  ASN A C   
417  O O   . ASN A 57  ? 0.7972 0.5170 0.5179 -0.0571 -0.0048 0.0428  57  ASN A O   
418  C CB  . ASN A 57  ? 0.7575 0.4750 0.4695 -0.0746 -0.0074 0.0379  57  ASN A CB  
419  C CG  . ASN A 57  ? 0.7878 0.5151 0.5104 -0.0733 -0.0095 0.0413  57  ASN A CG  
420  O OD1 . ASN A 57  ? 0.7297 0.4687 0.4644 -0.0688 -0.0105 0.0427  57  ASN A OD1 
421  N ND2 . ASN A 57  ? 0.7460 0.4684 0.4640 -0.0773 -0.0103 0.0427  57  ASN A ND2 
422  N N   . GLY A 58  ? 0.7301 0.4751 0.4693 -0.0607 -0.0081 0.0390  58  GLY A N   
423  C CA  . GLY A 58  ? 0.7080 0.4567 0.4549 -0.0519 -0.0072 0.0433  58  GLY A CA  
424  C C   . GLY A 58  ? 0.6747 0.4247 0.4281 -0.0476 -0.0078 0.0494  58  GLY A C   
425  O O   . GLY A 58  ? 0.6582 0.4105 0.4177 -0.0404 -0.0068 0.0535  58  GLY A O   
426  N N   . ASP A 59  ? 0.6641 0.4135 0.4166 -0.0521 -0.0095 0.0501  59  ASP A N   
427  C CA  . ASP A 59  ? 0.6603 0.4122 0.4196 -0.0479 -0.0105 0.0557  59  ASP A CA  
428  C C   . ASP A 59  ? 0.6012 0.3682 0.3754 -0.0454 -0.0120 0.0568  59  ASP A C   
429  O O   . ASP A 59  ? 0.6569 0.4329 0.4358 -0.0500 -0.0135 0.0529  59  ASP A O   
430  C CB  . ASP A 59  ? 0.6448 0.3944 0.4004 -0.0540 -0.0125 0.0555  59  ASP A CB  
431  C CG  . ASP A 59  ? 0.8283 0.5614 0.5695 -0.0550 -0.0111 0.0564  59  ASP A CG  
432  O OD1 . ASP A 59  ? 0.8042 0.5276 0.5384 -0.0506 -0.0087 0.0572  59  ASP A OD1 
433  O OD2 . ASP A 59  ? 0.8369 0.5666 0.5735 -0.0600 -0.0126 0.0566  59  ASP A OD2 
434  N N   . THR A 60  ? 0.6205 0.3904 0.4023 -0.0384 -0.0117 0.0621  60  THR A N   
435  C CA  . THR A 60  ? 0.6098 0.3932 0.4055 -0.0363 -0.0130 0.0635  60  THR A CA  
436  C C   . THR A 60  ? 0.7187 0.5062 0.5216 -0.0349 -0.0151 0.0681  60  THR A C   
437  O O   . THR A 60  ? 0.7342 0.5139 0.5321 -0.0327 -0.0148 0.0715  60  THR A O   
438  C CB  . THR A 60  ? 0.6466 0.4312 0.4456 -0.0297 -0.0104 0.0651  60  THR A CB  
439  O OG1 . THR A 60  ? 0.6774 0.4526 0.4712 -0.0241 -0.0081 0.0691  60  THR A OG1 
440  C CG2 . THR A 60  ? 0.6348 0.4172 0.4276 -0.0318 -0.0092 0.0600  60  THR A CG2 
441  N N   . SER A 61  ? 0.5963 0.3956 0.4102 -0.0364 -0.0174 0.0681  61  SER A N   
442  C CA  . SER A 61  ? 0.6165 0.4225 0.4402 -0.0341 -0.0194 0.0727  61  SER A CA  
443  C C   . SER A 61  ? 0.5966 0.4131 0.4323 -0.0310 -0.0193 0.0740  61  SER A C   
444  O O   . SER A 61  ? 0.5919 0.4131 0.4294 -0.0333 -0.0194 0.0702  61  SER A O   
445  C CB  . SER A 61  ? 0.6366 0.4465 0.4617 -0.0401 -0.0229 0.0714  61  SER A CB  
446  O OG  . SER A 61  ? 0.7613 0.5611 0.5751 -0.0430 -0.0230 0.0709  61  SER A OG  
447  N N   . TYR A 62  ? 0.6121 0.4324 0.4558 -0.0257 -0.0190 0.0792  62  TYR A N   
448  C CA  . TYR A 62  ? 0.5735 0.4032 0.4283 -0.0231 -0.0186 0.0807  62  TYR A CA  
449  C C   . TYR A 62  ? 0.6207 0.4589 0.4861 -0.0235 -0.0216 0.0840  62  TYR A C   
450  O O   . TYR A 62  ? 0.5859 0.4222 0.4511 -0.0223 -0.0227 0.0872  62  TYR A O   
451  C CB  . TYR A 62  ? 0.5839 0.4115 0.4400 -0.0158 -0.0149 0.0844  62  TYR A CB  
452  C CG  . TYR A 62  ? 0.6289 0.4481 0.4747 -0.0146 -0.0118 0.0814  62  TYR A CG  
453  C CD1 . TYR A 62  ? 0.6454 0.4532 0.4796 -0.0140 -0.0104 0.0808  62  TYR A CD1 
454  C CD2 . TYR A 62  ? 0.6209 0.4433 0.4682 -0.0143 -0.0105 0.0789  62  TYR A CD2 
455  C CE1 . TYR A 62  ? 0.6903 0.4904 0.5149 -0.0133 -0.0078 0.0778  62  TYR A CE1 
456  C CE2 . TYR A 62  ? 0.6260 0.4413 0.4641 -0.0133 -0.0081 0.0760  62  TYR A CE2 
457  C CZ  . TYR A 62  ? 0.6241 0.4284 0.4509 -0.0130 -0.0067 0.0753  62  TYR A CZ  
458  O OH  . TYR A 62  ? 0.6231 0.4205 0.4407 -0.0125 -0.0046 0.0721  62  TYR A OH  
459  N N   . ASN A 63  ? 0.5485 0.3955 0.4225 -0.0254 -0.0230 0.0830  63  ASN A N   
460  C CA  . ASN A 63  ? 0.5547 0.4103 0.4403 -0.0246 -0.0250 0.0868  63  ASN A CA  
461  C C   . ASN A 63  ? 0.5927 0.4489 0.4830 -0.0179 -0.0223 0.0922  63  ASN A C   
462  O O   . ASN A 63  ? 0.5855 0.4396 0.4744 -0.0140 -0.0186 0.0924  63  ASN A O   
463  C CB  . ASN A 63  ? 0.5538 0.4168 0.4467 -0.0265 -0.0256 0.0849  63  ASN A CB  
464  C CG  . ASN A 63  ? 0.5883 0.4600 0.4923 -0.0277 -0.0285 0.0875  63  ASN A CG  
465  O OD1 . ASN A 63  ? 0.6222 0.4962 0.5315 -0.0249 -0.0287 0.0922  63  ASN A OD1 
466  N ND2 . ASN A 63  ? 0.5095 0.3859 0.4171 -0.0317 -0.0307 0.0846  63  ASN A ND2 
467  N N   . GLN A 64  ? 0.5737 0.4331 0.4694 -0.0162 -0.0240 0.0964  64  GLN A N   
468  C CA  . GLN A 64  ? 0.6345 0.4958 0.5356 -0.0097 -0.0216 0.1017  64  GLN A CA  
469  C C   . GLN A 64  ? 0.6281 0.4952 0.5368 -0.0073 -0.0188 0.1028  64  GLN A C   
470  O O   . GLN A 64  ? 0.6315 0.4964 0.5394 -0.0018 -0.0147 0.1049  64  GLN A O   
471  C CB  . GLN A 64  ? 0.6755 0.5429 0.5845 -0.0092 -0.0249 0.1057  64  GLN A CB  
472  C CG  . GLN A 64  ? 0.7776 0.6461 0.6906 -0.0021 -0.0226 0.1111  64  GLN A CG  
473  N N   . LYS A 65  ? 0.5974 0.4712 0.5126 -0.0113 -0.0207 0.1012  65  LYS A N   
474  C CA  . LYS A 65  ? 0.6177 0.4968 0.5403 -0.0092 -0.0182 0.1028  65  LYS A CA  
475  C C   . LYS A 65  ? 0.6117 0.4847 0.5267 -0.0069 -0.0143 0.1004  65  LYS A C   
476  O O   . LYS A 65  ? 0.6321 0.5077 0.5514 -0.0036 -0.0112 0.1025  65  LYS A O   
477  C CB  . LYS A 65  ? 0.6607 0.5483 0.5929 -0.0134 -0.0211 0.1026  65  LYS A CB  
478  C CG  . LYS A 65  ? 0.7787 0.6648 0.7065 -0.0189 -0.0237 0.0972  65  LYS A CG  
479  C CD  . LYS A 65  ? 0.8916 0.7851 0.8283 -0.0227 -0.0266 0.0970  65  LYS A CD  
480  C CE  . LYS A 65  ? 0.9127 0.8099 0.8561 -0.0201 -0.0237 0.0995  65  LYS A CE  
481  N NZ  . LYS A 65  ? 0.8602 0.7595 0.8060 -0.0236 -0.0253 0.0969  65  LYS A NZ  
482  N N   . PHE A 66  ? 0.5680 0.4331 0.4718 -0.0086 -0.0144 0.0961  66  PHE A N   
483  C CA  . PHE A 66  ? 0.5566 0.4165 0.4534 -0.0067 -0.0112 0.0936  66  PHE A CA  
484  C C   . PHE A 66  ? 0.5819 0.4326 0.4691 -0.0027 -0.0081 0.0940  66  PHE A C   
485  O O   . PHE A 66  ? 0.6353 0.4804 0.5148 -0.0016 -0.0059 0.0913  66  PHE A O   
486  C CB  . PHE A 66  ? 0.5050 0.3629 0.3958 -0.0119 -0.0133 0.0875  66  PHE A CB  
487  C CG  . PHE A 66  ? 0.5505 0.4162 0.4495 -0.0148 -0.0154 0.0867  66  PHE A CG  
488  C CD1 . PHE A 66  ? 0.5437 0.4113 0.4454 -0.0124 -0.0133 0.0871  66  PHE A CD1 
489  C CD2 . PHE A 66  ? 0.5165 0.3870 0.4202 -0.0196 -0.0195 0.0857  66  PHE A CD2 
490  C CE1 . PHE A 66  ? 0.5367 0.4103 0.4453 -0.0149 -0.0152 0.0865  66  PHE A CE1 
491  C CE2 . PHE A 66  ? 0.5472 0.4238 0.4576 -0.0220 -0.0214 0.0848  66  PHE A CE2 
492  C CZ  . PHE A 66  ? 0.5718 0.4497 0.4848 -0.0196 -0.0192 0.0853  66  PHE A CZ  
493  N N   . LYS A 67  ? 0.6393 0.4881 0.5264 -0.0005 -0.0084 0.0971  67  LYS A N   
494  C CA  . LYS A 67  ? 0.6558 0.4941 0.5320 0.0025  -0.0062 0.0969  67  LYS A CA  
495  C C   . LYS A 67  ? 0.6532 0.4877 0.5261 0.0083  -0.0013 0.0980  67  LYS A C   
496  O O   . LYS A 67  ? 0.8140 0.6387 0.6754 0.0092  0.0004  0.0954  67  LYS A O   
497  C CB  . LYS A 67  ? 0.6855 0.5215 0.5612 0.0042  -0.0075 0.1001  67  LYS A CB  
498  C CG  . LYS A 67  ? 0.7821 0.6259 0.6691 0.0092  -0.0067 0.1059  67  LYS A CG  
499  N N   . ASP A 68  ? 0.6574 0.4991 0.5397 0.0119  0.0008  0.1015  68  ASP A N   
500  C CA  . ASP A 68  ? 0.7219 0.5597 0.6004 0.0176  0.0058  0.1025  68  ASP A CA  
501  C C   . ASP A 68  ? 0.7020 0.5400 0.5783 0.0158  0.0067  0.0993  68  ASP A C   
502  O O   . ASP A 68  ? 0.7645 0.5956 0.6323 0.0186  0.0097  0.0977  68  ASP A O   
503  C CB  . ASP A 68  ? 0.7907 0.6341 0.6781 0.0236  0.0088  0.1084  68  ASP A CB  
504  C CG  . ASP A 68  ? 0.9159 0.7577 0.8035 0.0264  0.0080  0.1113  68  ASP A CG  
505  O OD1 . ASP A 68  ? 0.9055 0.7365 0.7815 0.0274  0.0083  0.1094  68  ASP A OD1 
506  O OD2 . ASP A 68  ? 0.8853 0.7364 0.7843 0.0271  0.0067  0.1151  68  ASP A OD2 
507  N N   . LYS A 69  ? 0.6361 0.4815 0.5195 0.0113  0.0037  0.0981  69  LYS A N   
508  C CA  . LYS A 69  ? 0.5965 0.4428 0.4786 0.0096  0.0039  0.0952  69  LYS A CA  
509  C C   . LYS A 69  ? 0.6315 0.4703 0.5018 0.0068  0.0027  0.0894  69  LYS A C   
510  O O   . LYS A 69  ? 0.6317 0.4672 0.4965 0.0084  0.0047  0.0874  69  LYS A O   
511  C CB  . LYS A 69  ? 0.5907 0.4460 0.4828 0.0052  0.0006  0.0951  69  LYS A CB  
512  C CG  . LYS A 69  ? 0.5881 0.4445 0.4794 0.0038  0.0003  0.0922  69  LYS A CG  
513  C CD  . LYS A 69  ? 0.5432 0.3985 0.4342 0.0091  0.0050  0.0950  69  LYS A CD  
514  C CE  . LYS A 69  ? 0.5484 0.4109 0.4509 0.0113  0.0069  0.1008  69  LYS A CE  
515  N NZ  . LYS A 69  ? 0.5826 0.4443 0.4846 0.0157  0.0115  0.1031  69  LYS A NZ  
516  N N   . ALA A 70  ? 0.5611 0.3978 0.4278 0.0022  -0.0005 0.0865  70  ALA A N   
517  C CA  . ALA A 70  ? 0.6186 0.4502 0.4757 -0.0015 -0.0018 0.0806  70  ALA A CA  
518  C C   . ALA A 70  ? 0.6390 0.4603 0.4847 -0.0012 -0.0008 0.0792  70  ALA A C   
519  O O   . ALA A 70  ? 0.6817 0.5006 0.5273 -0.0005 -0.0010 0.0817  70  ALA A O   
520  C CB  . ALA A 70  ? 0.5721 0.4091 0.4329 -0.0078 -0.0062 0.0777  70  ALA A CB  
521  N N   . THR A 71  ? 0.6634 0.4785 0.4990 -0.0023 -0.0001 0.0747  71  THR A N   
522  C CA  . THR A 71  ? 0.6371 0.4419 0.4610 -0.0037 0.0002  0.0723  71  THR A CA  
523  C C   . THR A 71  ? 0.6301 0.4347 0.4486 -0.0100 -0.0022 0.0660  71  THR A C   
524  O O   . THR A 71  ? 0.6317 0.4390 0.4497 -0.0101 -0.0023 0.0631  71  THR A O   
525  C CB  . THR A 71  ? 0.6470 0.4428 0.4624 0.0019  0.0044  0.0732  71  THR A CB  
526  O OG1 . THR A 71  ? 0.6884 0.4867 0.5107 0.0080  0.0069  0.0791  71  THR A OG1 
527  C CG2 . THR A 71  ? 0.6406 0.4246 0.4432 0.0003  0.0048  0.0708  71  THR A CG2 
528  N N   . LEU A 72  ? 0.6019 0.4045 0.4171 -0.0153 -0.0045 0.0639  72  LEU A N   
529  C CA  . LEU A 72  ? 0.5864 0.3898 0.3971 -0.0217 -0.0067 0.0579  72  LEU A CA  
530  C C   . LEU A 72  ? 0.6328 0.4251 0.4301 -0.0233 -0.0054 0.0548  72  LEU A C   
531  O O   . LEU A 72  ? 0.6133 0.3973 0.4051 -0.0225 -0.0042 0.0569  72  LEU A O   
532  C CB  . LEU A 72  ? 0.5516 0.3598 0.3667 -0.0271 -0.0098 0.0574  72  LEU A CB  
533  C CG  . LEU A 72  ? 0.5534 0.3721 0.3812 -0.0264 -0.0116 0.0601  72  LEU A CG  
534  C CD1 . LEU A 72  ? 0.5745 0.3970 0.4040 -0.0328 -0.0149 0.0580  72  LEU A CD1 
535  C CD2 . LEU A 72  ? 0.5413 0.3669 0.3744 -0.0247 -0.0117 0.0587  72  LEU A CD2 
536  N N   . THR A 73  ? 0.5821 0.3738 0.3742 -0.0252 -0.0055 0.0499  73  THR A N   
537  C CA  . THR A 73  ? 0.6200 0.4019 0.3996 -0.0284 -0.0048 0.0462  73  THR A CA  
538  C C   . THR A 73  ? 0.6158 0.4031 0.3943 -0.0355 -0.0074 0.0399  73  THR A C   
539  O O   . THR A 73  ? 0.5963 0.3942 0.3831 -0.0368 -0.0095 0.0384  73  THR A O   
540  C CB  . THR A 73  ? 0.6654 0.4398 0.4378 -0.0230 -0.0018 0.0465  73  THR A CB  
541  O OG1 . THR A 73  ? 0.6560 0.4385 0.4338 -0.0210 -0.0023 0.0453  73  THR A OG1 
542  C CG2 . THR A 73  ? 0.6800 0.4488 0.4527 -0.0158 0.0012  0.0525  73  THR A CG2 
543  N N   . ALA A 74  ? 0.6265 0.4062 0.3945 -0.0402 -0.0073 0.0360  74  ALA A N   
544  C CA  . ALA A 74  ? 0.6500 0.4349 0.4164 -0.0471 -0.0094 0.0297  74  ALA A CA  
545  C C   . ALA A 74  ? 0.7736 0.5499 0.5282 -0.0487 -0.0084 0.0258  74  ALA A C   
546  O O   . ALA A 74  ? 0.7639 0.5277 0.5091 -0.0476 -0.0062 0.0273  74  ALA A O   
547  C CB  . ALA A 74  ? 0.6335 0.4189 0.3995 -0.0538 -0.0108 0.0287  74  ALA A CB  
548  N N   . ASP A 75  ? 0.6861 0.4692 0.4412 -0.0514 -0.0100 0.0206  75  ASP A N   
549  C CA  . ASP A 75  ? 0.7343 0.5105 0.4786 -0.0537 -0.0096 0.0162  75  ASP A CA  
550  C C   . ASP A 75  ? 0.6702 0.4518 0.4132 -0.0626 -0.0118 0.0100  75  ASP A C   
551  O O   . ASP A 75  ? 0.6351 0.4283 0.3840 -0.0642 -0.0140 0.0062  75  ASP A O   
552  C CB  . ASP A 75  ? 0.7729 0.5504 0.5169 -0.0479 -0.0092 0.0158  75  ASP A CB  
553  C CG  . ASP A 75  ? 0.9011 0.6730 0.6345 -0.0504 -0.0093 0.0107  75  ASP A CG  
554  O OD1 . ASP A 75  ? 0.9335 0.7014 0.6603 -0.0574 -0.0098 0.0070  75  ASP A OD1 
555  O OD2 . ASP A 75  ? 0.9216 0.6935 0.6534 -0.0455 -0.0091 0.0104  75  ASP A OD2 
556  N N   . LYS A 76  ? 0.7117 0.4849 0.4468 -0.0685 -0.0110 0.0091  76  LYS A N   
557  C CA  . LYS A 76  ? 0.7342 0.5121 0.4678 -0.0776 -0.0126 0.0035  76  LYS A CA  
558  C C   . LYS A 76  ? 0.7127 0.4947 0.4432 -0.0801 -0.0139 -0.0025 76  LYS A C   
559  O O   . LYS A 76  ? 0.7380 0.5307 0.4726 -0.0858 -0.0159 -0.0073 76  LYS A O   
560  C CB  . LYS A 76  ? 0.7431 0.5098 0.4675 -0.0836 -0.0113 0.0038  76  LYS A CB  
561  C CG  . LYS A 76  ? 0.8176 0.5853 0.5473 -0.0834 -0.0112 0.0082  76  LYS A CG  
562  C CD  . LYS A 76  ? 0.8841 0.6404 0.6039 -0.0896 -0.0100 0.0085  76  LYS A CD  
563  C CE  . LYS A 76  ? 0.9316 0.6708 0.6406 -0.0851 -0.0076 0.0120  76  LYS A CE  
564  N NZ  . LYS A 76  ? 0.9806 0.7074 0.6794 -0.0905 -0.0066 0.0127  76  LYS A NZ  
565  N N   . SER A 77  ? 0.7510 0.5253 0.4746 -0.0757 -0.0129 -0.0024 77  SER A N   
566  C CA  . SER A 77  ? 0.8086 0.5857 0.5279 -0.0789 -0.0144 -0.0085 77  SER A CA  
567  C C   . SER A 77  ? 0.8177 0.6109 0.5477 -0.0766 -0.0171 -0.0109 77  SER A C   
568  O O   . SER A 77  ? 0.8593 0.6602 0.5893 -0.0810 -0.0193 -0.0167 77  SER A O   
569  C CB  . SER A 77  ? 0.8431 0.6070 0.5509 -0.0753 -0.0128 -0.0083 77  SER A CB  
570  O OG  . SER A 77  ? 0.8289 0.5913 0.5395 -0.0656 -0.0115 -0.0035 77  SER A OG  
571  N N   . SER A 78  ? 0.7366 0.5351 0.4756 -0.0699 -0.0170 -0.0064 78  SER A N   
572  C CA  . SER A 78  ? 0.7088 0.5212 0.4575 -0.0670 -0.0195 -0.0080 78  SER A CA  
573  C C   . SER A 78  ? 0.6895 0.5125 0.4494 -0.0685 -0.0207 -0.0070 78  SER A C   
574  O O   . SER A 78  ? 0.6611 0.4953 0.4295 -0.0658 -0.0227 -0.0080 78  SER A O   
575  C CB  . SER A 78  ? 0.7349 0.5447 0.4842 -0.0579 -0.0187 -0.0043 78  SER A CB  
576  O OG  . SER A 78  ? 0.6868 0.4921 0.4397 -0.0533 -0.0164 0.0022  78  SER A OG  
577  N N   . SER A 79  ? 0.6507 0.4701 0.4100 -0.0731 -0.0196 -0.0055 79  SER A N   
578  C CA  . SER A 79  ? 0.6126 0.4408 0.3814 -0.0746 -0.0206 -0.0043 79  SER A CA  
579  C C   . SER A 79  ? 0.5789 0.4111 0.3565 -0.0669 -0.0208 0.0004  79  SER A C   
580  O O   . SER A 79  ? 0.5820 0.4252 0.3686 -0.0670 -0.0227 -0.0005 79  SER A O   
581  C CB  . SER A 79  ? 0.6252 0.4665 0.3990 -0.0804 -0.0230 -0.0104 79  SER A CB  
582  O OG  . SER A 79  ? 0.7111 0.5495 0.4775 -0.0884 -0.0227 -0.0148 79  SER A OG  
583  N N   . THR A 80  ? 0.5566 0.3802 0.3317 -0.0604 -0.0188 0.0055  80  THR A N   
584  C CA  . THR A 80  ? 0.5582 0.3855 0.3413 -0.0533 -0.0187 0.0100  80  THR A CA  
585  C C   . THR A 80  ? 0.5898 0.4096 0.3733 -0.0504 -0.0165 0.0164  80  THR A C   
586  O O   . THR A 80  ? 0.6146 0.4232 0.3898 -0.0500 -0.0143 0.0181  80  THR A O   
587  C CB  . THR A 80  ? 0.6174 0.4421 0.3969 -0.0475 -0.0181 0.0099  80  THR A CB  
588  O OG1 . THR A 80  ? 0.5838 0.4167 0.3637 -0.0500 -0.0207 0.0039  80  THR A OG1 
589  C CG2 . THR A 80  ? 0.5989 0.4268 0.3858 -0.0404 -0.0177 0.0145  80  THR A CG2 
590  N N   . ALA A 81  ? 0.5477 0.3734 0.3407 -0.0484 -0.0171 0.0199  81  ALA A N   
591  C CA  . ALA A 81  ? 0.5820 0.4032 0.3778 -0.0447 -0.0155 0.0262  81  ALA A CA  
592  C C   . ALA A 81  ? 0.5543 0.3769 0.3547 -0.0373 -0.0144 0.0299  81  ALA A C   
593  O O   . ALA A 81  ? 0.5832 0.4126 0.3875 -0.0357 -0.0157 0.0279  81  ALA A O   
594  C CB  . ALA A 81  ? 0.5679 0.3955 0.3714 -0.0479 -0.0172 0.0273  81  ALA A CB  
595  N N   . TYR A 82  ? 0.5656 0.3818 0.3655 -0.0327 -0.0119 0.0354  82  TYR A N   
596  C CA  . TYR A 82  ? 0.5829 0.3998 0.3867 -0.0259 -0.0102 0.0393  82  TYR A CA  
597  C C   . TYR A 82  ? 0.5883 0.4057 0.3991 -0.0230 -0.0091 0.0455  82  TYR A C   
598  O O   . TYR A 82  ? 0.5889 0.4019 0.3979 -0.0246 -0.0087 0.0473  82  TYR A O   
599  C CB  . TYR A 82  ? 0.6273 0.4344 0.4218 -0.0218 -0.0072 0.0401  82  TYR A CB  
600  C CG  . TYR A 82  ? 0.6782 0.4835 0.4645 -0.0237 -0.0080 0.0344  82  TYR A CG  
601  C CD1 . TYR A 82  ? 0.6589 0.4691 0.4470 -0.0210 -0.0088 0.0329  82  TYR A CD1 
602  C CD2 . TYR A 82  ? 0.6678 0.4671 0.4451 -0.0287 -0.0083 0.0305  82  TYR A CD2 
603  C CE1 . TYR A 82  ? 0.7209 0.5304 0.5020 -0.0225 -0.0100 0.0277  82  TYR A CE1 
604  C CE2 . TYR A 82  ? 0.6847 0.4837 0.4554 -0.0310 -0.0095 0.0250  82  TYR A CE2 
605  C CZ  . TYR A 82  ? 0.7728 0.5770 0.5455 -0.0276 -0.0103 0.0237  82  TYR A CZ  
606  O OH  . TYR A 82  ? 0.7234 0.5281 0.4902 -0.0291 -0.0118 0.0185  82  TYR A OH  
607  N N   . MET A 83  ? 0.5172 0.3403 0.3363 -0.0191 -0.0088 0.0486  83  MET A N   
608  C CA  . MET A 83  ? 0.5353 0.3593 0.3614 -0.0159 -0.0075 0.0546  83  MET A CA  
609  C C   . MET A 83  ? 0.5671 0.3895 0.3937 -0.0093 -0.0044 0.0581  83  MET A C   
610  O O   . MET A 83  ? 0.5575 0.3836 0.3860 -0.0078 -0.0047 0.0570  83  MET A O   
611  C CB  . MET A 83  ? 0.5252 0.3586 0.3621 -0.0180 -0.0101 0.0556  83  MET A CB  
612  C CG  . MET A 83  ? 0.5266 0.3621 0.3716 -0.0144 -0.0088 0.0619  83  MET A CG  
613  S SD  . MET A 83  ? 0.5757 0.4203 0.4320 -0.0182 -0.0123 0.0629  83  MET A SD  
614  C CE  . MET A 83  ? 0.5899 0.4405 0.4500 -0.0177 -0.0135 0.0603  83  MET A CE  
615  N N   . GLN A 84  ? 0.5913 0.4078 0.4157 -0.0053 -0.0013 0.0622  84  GLN A N   
616  C CA  . GLN A 84  ? 0.5452 0.3607 0.3708 0.0009  0.0020  0.0660  84  GLN A CA  
617  C C   . GLN A 84  ? 0.5853 0.4078 0.4228 0.0027  0.0024  0.0713  84  GLN A C   
618  O O   . GLN A 84  ? 0.6208 0.4444 0.4624 0.0016  0.0017  0.0737  84  GLN A O   
619  C CB  . GLN A 84  ? 0.5946 0.4002 0.4114 0.0050  0.0056  0.0676  84  GLN A CB  
620  C CG  . GLN A 84  ? 0.7215 0.5265 0.5394 0.0117  0.0097  0.0715  84  GLN A CG  
621  C CD  . GLN A 84  ? 0.8615 0.6602 0.6767 0.0169  0.0136  0.0756  84  GLN A CD  
622  O OE1 . GLN A 84  ? 0.9089 0.7094 0.7297 0.0174  0.0137  0.0791  84  GLN A OE1 
623  N NE2 . GLN A 84  ? 0.8933 0.6848 0.6998 0.0212  0.0169  0.0754  84  GLN A NE2 
624  N N   . LEU A 85  ? 0.5291 0.3561 0.3720 0.0054  0.0035  0.0733  85  LEU A N   
625  C CA  . LEU A 85  ? 0.5741 0.4072 0.4279 0.0073  0.0045  0.0787  85  LEU A CA  
626  C C   . LEU A 85  ? 0.6109 0.4408 0.4634 0.0137  0.0094  0.0828  85  LEU A C   
627  O O   . LEU A 85  ? 0.6528 0.4798 0.4999 0.0162  0.0112  0.0816  85  LEU A O   
628  C CB  . LEU A 85  ? 0.5864 0.4270 0.4479 0.0049  0.0020  0.0781  85  LEU A CB  
629  C CG  . LEU A 85  ? 0.5651 0.4095 0.4284 -0.0011 -0.0026 0.0740  85  LEU A CG  
630  C CD1 . LEU A 85  ? 0.5574 0.4072 0.4261 -0.0020 -0.0043 0.0732  85  LEU A CD1 
631  C CD2 . LEU A 85  ? 0.5653 0.4130 0.4351 -0.0039 -0.0045 0.0761  85  LEU A CD2 
632  N N   . SER A 86  ? 0.6112 0.4419 0.4683 0.0166  0.0117  0.0876  86  SER A N   
633  C CA  . SER A 86  ? 0.6344 0.4620 0.4898 0.0230  0.0168  0.0913  86  SER A CA  
634  C C   . SER A 86  ? 0.6349 0.4709 0.5024 0.0249  0.0186  0.0967  86  SER A C   
635  O O   . SER A 86  ? 0.6265 0.4699 0.5038 0.0214  0.0157  0.0979  86  SER A O   
636  C CB  . SER A 86  ? 0.6675 0.4887 0.5175 0.0257  0.0186  0.0924  86  SER A CB  
637  O OG  . SER A 86  ? 0.6986 0.5245 0.5563 0.0237  0.0163  0.0946  86  SER A OG  
638  N N   . ASN A 87  ? 0.6363 0.4711 0.5030 0.0302  0.0235  0.0998  87  ASN A N   
639  C CA  . ASN A 87  ? 0.6453 0.4878 0.5231 0.0323  0.0261  0.1052  87  ASN A CA  
640  C C   . ASN A 87  ? 0.6389 0.4883 0.5248 0.0276  0.0229  0.1050  87  ASN A C   
641  O O   . ASN A 87  ? 0.6113 0.4685 0.5084 0.0255  0.0215  0.1079  87  ASN A O   
642  C CB  . ASN A 87  ? 0.7049 0.5515 0.5902 0.0340  0.0268  0.1092  87  ASN A CB  
643  C CG  . ASN A 87  ? 0.8006 0.6397 0.6777 0.0396  0.0305  0.1099  87  ASN A CG  
644  O OD1 . ASN A 87  ? 0.8032 0.6389 0.6758 0.0443  0.0353  0.1112  87  ASN A OD1 
645  N ND2 . ASN A 87  ? 0.7542 0.5897 0.6281 0.0391  0.0286  0.1088  87  ASN A ND2 
646  N N   . LEU A 88  ? 0.6032 0.4495 0.4829 0.0261  0.0215  0.1013  88  LEU A N   
647  C CA  . LEU A 88  ? 0.6038 0.4552 0.4894 0.0219  0.0181  0.1003  88  LEU A CA  
648  C C   . LEU A 88  ? 0.6307 0.4885 0.5268 0.0226  0.0205  0.1056  88  LEU A C   
649  O O   . LEU A 88  ? 0.6248 0.4815 0.5200 0.0269  0.0254  0.1089  88  LEU A O   
650  C CB  . LEU A 88  ? 0.6008 0.4472 0.4772 0.0219  0.0172  0.0960  88  LEU A CB  
651  C CG  . LEU A 88  ? 0.6028 0.4450 0.4708 0.0193  0.0137  0.0900  88  LEU A CG  
652  C CD1 . LEU A 88  ? 0.5728 0.4104 0.4315 0.0203  0.0132  0.0861  88  LEU A CD1 
653  C CD2 . LEU A 88  ? 0.5754 0.4226 0.4491 0.0136  0.0086  0.0876  88  LEU A CD2 
654  N N   . THR A 89  ? 0.5973 0.4616 0.5027 0.0181  0.0170  0.1061  89  THR A N   
655  C CA  . THR A 89  ? 0.6079 0.4782 0.5232 0.0173  0.0183  0.1104  89  THR A CA  
656  C C   . THR A 89  ? 0.5967 0.4683 0.5138 0.0126  0.0140  0.1076  89  THR A C   
657  O O   . THR A 89  ? 0.5783 0.4475 0.4902 0.0103  0.0101  0.1027  89  THR A O   
658  C CB  . THR A 89  ? 0.5984 0.4763 0.5250 0.0165  0.0185  0.1145  89  THR A CB  
659  O OG1 . THR A 89  ? 0.6426 0.5230 0.5721 0.0115  0.0129  0.1117  89  THR A OG1 
660  C CG2 . THR A 89  ? 0.6442 0.5206 0.5685 0.0212  0.0218  0.1165  89  THR A CG2 
661  N N   . SER A 90  ? 0.5949 0.4704 0.5194 0.0111  0.0146  0.1107  90  SER A N   
662  C CA  . SER A 90  ? 0.5975 0.4734 0.5236 0.0070  0.0106  0.1084  90  SER A CA  
663  C C   . SER A 90  ? 0.5705 0.4499 0.5003 0.0024  0.0052  0.1054  90  SER A C   
664  O O   . SER A 90  ? 0.5434 0.4219 0.4715 -0.0005 0.0014  0.1015  90  SER A O   
665  C CB  . SER A 90  ? 0.6608 0.5405 0.5954 0.0057  0.0124  0.1130  90  SER A CB  
666  O OG  . SER A 90  ? 0.6801 0.5560 0.6100 0.0098  0.0174  0.1155  90  SER A OG  
667  N N   . GLU A 91  ? 0.5571 0.4406 0.4921 0.0019  0.0051  0.1072  91  GLU A N   
668  C CA  . GLU A 91  ? 0.6033 0.4901 0.5419 -0.0023 0.0003  0.1050  91  GLU A CA  
669  C C   . GLU A 91  ? 0.5450 0.4270 0.4741 -0.0031 -0.0023 0.0993  91  GLU A C   
670  O O   . GLU A 91  ? 0.5473 0.4313 0.4778 -0.0071 -0.0065 0.0965  91  GLU A O   
671  C CB  . GLU A 91  ? 0.5752 0.4677 0.5218 -0.0020 0.0009  0.1091  91  GLU A CB  
672  C CG  . GLU A 91  ? 0.5923 0.4916 0.5504 -0.0035 0.0019  0.1139  91  GLU A CG  
673  C CD  . GLU A 91  ? 0.7028 0.6011 0.6612 -0.0005 0.0070  0.1172  91  GLU A CD  
674  O OE1 . GLU A 91  ? 0.7107 0.6087 0.6682 0.0041  0.0116  0.1201  91  GLU A OE1 
675  O OE2 . GLU A 91  ? 0.7652 0.6622 0.7239 -0.0025 0.0065  0.1169  91  GLU A OE2 
676  N N   . ASP A 92  ? 0.5026 0.3786 0.4222 0.0004  0.0001  0.0975  92  ASP A N   
677  C CA  . ASP A 92  ? 0.4882 0.3597 0.3984 -0.0002 -0.0018 0.0920  92  ASP A CA  
678  C C   . ASP A 92  ? 0.5244 0.3944 0.4305 -0.0016 -0.0042 0.0876  92  ASP A C   
679  O O   . ASP A 92  ? 0.5137 0.3819 0.4138 -0.0034 -0.0068 0.0825  92  ASP A O   
680  C CB  . ASP A 92  ? 0.4930 0.3589 0.3950 0.0040  0.0016  0.0921  92  ASP A CB  
681  C CG  . ASP A 92  ? 0.5421 0.4090 0.4474 0.0059  0.0037  0.0960  92  ASP A CG  
682  O OD1 . ASP A 92  ? 0.5884 0.4584 0.4979 0.0028  0.0008  0.0959  92  ASP A OD1 
683  O OD2 . ASP A 92  ? 0.6034 0.4678 0.5066 0.0107  0.0082  0.0990  92  ASP A OD2 
684  N N   . SER A 93  ? 0.5079 0.3785 0.4169 -0.0008 -0.0034 0.0894  93  SER A N   
685  C CA  . SER A 93  ? 0.5036 0.3728 0.4089 -0.0018 -0.0060 0.0854  93  SER A CA  
686  C C   . SER A 93  ? 0.5138 0.3866 0.4223 -0.0067 -0.0109 0.0817  93  SER A C   
687  O O   . SER A 93  ? 0.5073 0.3841 0.4239 -0.0096 -0.0123 0.0840  93  SER A O   
688  C CB  . SER A 93  ? 0.5361 0.4047 0.4442 -0.0005 -0.0047 0.0883  93  SER A CB  
689  O OG  . SER A 93  ? 0.5413 0.4062 0.4451 0.0040  0.0000  0.0913  93  SER A OG  
690  N N   . ALA A 94  ? 0.4913 0.3628 0.3935 -0.0077 -0.0134 0.0761  94  ALA A N   
691  C CA  . ALA A 94  ? 0.4737 0.3487 0.3780 -0.0123 -0.0175 0.0723  94  ALA A CA  
692  C C   . ALA A 94  ? 0.4794 0.3532 0.3760 -0.0127 -0.0194 0.0661  94  ALA A C   
693  O O   . ALA A 94  ? 0.5001 0.3703 0.3899 -0.0096 -0.0176 0.0650  94  ALA A O   
694  C CB  . ALA A 94  ? 0.4481 0.3251 0.3557 -0.0146 -0.0176 0.0741  94  ALA A CB  
695  N N   . VAL A 95  ? 0.4317 0.3087 0.3292 -0.0167 -0.0229 0.0619  95  VAL A N   
696  C CA  . VAL A 95  ? 0.4458 0.3229 0.3368 -0.0178 -0.0245 0.0561  95  VAL A CA  
697  C C   . VAL A 95  ? 0.4733 0.3504 0.3627 -0.0209 -0.0245 0.0554  95  VAL A C   
698  O O   . VAL A 95  ? 0.4507 0.3298 0.3451 -0.0237 -0.0255 0.0574  95  VAL A O   
699  C CB  . VAL A 95  ? 0.4435 0.3242 0.3356 -0.0198 -0.0280 0.0514  95  VAL A CB  
700  C CG1 . VAL A 95  ? 0.4321 0.3141 0.3181 -0.0212 -0.0294 0.0452  95  VAL A CG1 
701  C CG2 . VAL A 95  ? 0.4385 0.3180 0.3314 -0.0163 -0.0281 0.0522  95  VAL A CG2 
702  N N   . TYR A 96  ? 0.4479 0.3220 0.3298 -0.0204 -0.0234 0.0528  96  TYR A N   
703  C CA  . TYR A 96  ? 0.4532 0.3255 0.3318 -0.0232 -0.0231 0.0521  96  TYR A CA  
704  C C   . TYR A 96  ? 0.4910 0.3651 0.3646 -0.0269 -0.0252 0.0456  96  TYR A C   
705  O O   . TYR A 96  ? 0.4508 0.3244 0.3195 -0.0255 -0.0253 0.0421  96  TYR A O   
706  C CB  . TYR A 96  ? 0.4811 0.3474 0.3544 -0.0199 -0.0196 0.0549  96  TYR A CB  
707  C CG  . TYR A 96  ? 0.4530 0.3184 0.3315 -0.0164 -0.0171 0.0614  96  TYR A CG  
708  C CD1 . TYR A 96  ? 0.4543 0.3193 0.3344 -0.0123 -0.0152 0.0638  96  TYR A CD1 
709  C CD2 . TYR A 96  ? 0.4508 0.3164 0.3332 -0.0173 -0.0166 0.0651  96  TYR A CD2 
710  C CE1 . TYR A 96  ? 0.4875 0.3526 0.3731 -0.0096 -0.0127 0.0697  96  TYR A CE1 
711  C CE2 . TYR A 96  ? 0.4522 0.3182 0.3402 -0.0141 -0.0143 0.0709  96  TYR A CE2 
712  C CZ  . TYR A 96  ? 0.4771 0.3433 0.3672 -0.0106 -0.0123 0.0732  96  TYR A CZ  
713  O OH  . TYR A 96  ? 0.4869 0.3545 0.3832 -0.0081 -0.0099 0.0789  96  TYR A OH  
714  N N   . TYR A 97  ? 0.4406 0.3171 0.3154 -0.0316 -0.0271 0.0438  97  TYR A N   
715  C CA  . TYR A 97  ? 0.4461 0.3250 0.3167 -0.0356 -0.0288 0.0377  97  TYR A CA  
716  C C   . TYR A 97  ? 0.4546 0.3291 0.3191 -0.0385 -0.0277 0.0373  97  TYR A C   
717  O O   . TYR A 97  ? 0.4890 0.3604 0.3546 -0.0386 -0.0268 0.0415  97  TYR A O   
718  C CB  . TYR A 97  ? 0.4517 0.3361 0.3275 -0.0396 -0.0316 0.0360  97  TYR A CB  
719  C CG  . TYR A 97  ? 0.4261 0.3144 0.3076 -0.0374 -0.0331 0.0358  97  TYR A CG  
720  C CD1 . TYR A 97  ? 0.4581 0.3502 0.3384 -0.0368 -0.0346 0.0307  97  TYR A CD1 
721  C CD2 . TYR A 97  ? 0.4544 0.3426 0.3422 -0.0357 -0.0332 0.0406  97  TYR A CD2 
722  C CE1 . TYR A 97  ? 0.4718 0.3662 0.3561 -0.0342 -0.0360 0.0306  97  TYR A CE1 
723  C CE2 . TYR A 97  ? 0.4906 0.3810 0.3825 -0.0337 -0.0345 0.0404  97  TYR A CE2 
724  C CZ  . TYR A 97  ? 0.4651 0.3580 0.3548 -0.0327 -0.0359 0.0354  97  TYR A CZ  
725  O OH  . TYR A 97  ? 0.4439 0.3379 0.3369 -0.0304 -0.0372 0.0354  97  TYR A OH  
726  N N   . CYS A 98  ? 0.4632 0.3372 0.3212 -0.0409 -0.0277 0.0324  98  CYS A N   
727  C CA  . CYS A 98  ? 0.4954 0.3661 0.3479 -0.0456 -0.0273 0.0310  98  CYS A CA  
728  C C   . CYS A 98  ? 0.5205 0.3974 0.3744 -0.0511 -0.0297 0.0263  98  CYS A C   
729  O O   . CYS A 98  ? 0.4798 0.3632 0.3368 -0.0511 -0.0313 0.0227  98  CYS A O   
730  C CB  . CYS A 98  ? 0.5486 0.4136 0.3923 -0.0453 -0.0255 0.0291  98  CYS A CB  
731  S SG  . CYS A 98  ? 0.6214 0.4929 0.4638 -0.0460 -0.0272 0.0222  98  CYS A SG  
732  N N   . ALA A 99  ? 0.4575 0.3325 0.3094 -0.0556 -0.0299 0.0267  99  ALA A N   
733  C CA  . ALA A 99  ? 0.4293 0.3103 0.2827 -0.0608 -0.0318 0.0226  99  ALA A CA  
734  C C   . ALA A 99  ? 0.4412 0.3175 0.2884 -0.0660 -0.0311 0.0225  99  ALA A C   
735  O O   . ALA A 99  ? 0.4887 0.3574 0.3327 -0.0648 -0.0298 0.0268  99  ALA A O   
736  C CB  . ALA A 99  ? 0.4202 0.3054 0.2814 -0.0599 -0.0336 0.0248  99  ALA A CB  
737  N N   . ARG A 100 ? 0.4626 0.3435 0.3084 -0.0715 -0.0320 0.0176  100 ARG A N   
738  C CA  . ARG A 100 ? 0.4589 0.3366 0.3004 -0.0769 -0.0319 0.0179  100 ARG A CA  
739  C C   . ARG A 100 ? 0.4672 0.3494 0.3150 -0.0773 -0.0340 0.0193  100 ARG A C   
740  O O   . ARG A 100 ? 0.4469 0.3371 0.2997 -0.0777 -0.0354 0.0158  100 ARG A O   
741  C CB  . ARG A 100 ? 0.4767 0.3565 0.3125 -0.0831 -0.0314 0.0120  100 ARG A CB  
742  C CG  . ARG A 100 ? 0.5214 0.3970 0.3514 -0.0825 -0.0297 0.0103  100 ARG A CG  
743  C CD  . ARG A 100 ? 0.4875 0.3646 0.3115 -0.0898 -0.0291 0.0049  100 ARG A CD  
744  N NE  . ARG A 100 ? 0.4974 0.3860 0.3266 -0.0928 -0.0305 -0.0001 100 ARG A NE  
745  C CZ  . ARG A 100 ? 0.5661 0.4612 0.3941 -0.0967 -0.0304 -0.0061 100 ARG A CZ  
746  N NH1 . ARG A 100 ? 0.6140 0.5056 0.4363 -0.0979 -0.0292 -0.0081 100 ARG A NH1 
747  N NH2 . ARG A 100 ? 0.5040 0.4093 0.3367 -0.0994 -0.0314 -0.0104 100 ARG A NH2 
748  N N   . LEU A 101 ? 0.4639 0.3410 0.3118 -0.0766 -0.0342 0.0245  101 LEU A N   
749  C CA  . LEU A 101 ? 0.4979 0.3787 0.3524 -0.0762 -0.0363 0.0267  101 LEU A CA  
750  C C   . LEU A 101 ? 0.4793 0.3610 0.3308 -0.0819 -0.0374 0.0249  101 LEU A C   
751  O O   . LEU A 101 ? 0.4882 0.3747 0.3447 -0.0826 -0.0395 0.0246  101 LEU A O   
752  C CB  . LEU A 101 ? 0.4986 0.3761 0.3572 -0.0717 -0.0367 0.0333  101 LEU A CB  
753  C CG  . LEU A 101 ? 0.4720 0.3501 0.3352 -0.0658 -0.0357 0.0353  101 LEU A CG  
754  C CD1 . LEU A 101 ? 0.4697 0.3450 0.3373 -0.0618 -0.0357 0.0420  101 LEU A CD1 
755  C CD2 . LEU A 101 ? 0.4989 0.3846 0.3683 -0.0648 -0.0371 0.0322  101 LEU A CD2 
756  N N   . ASP A 102 ? 0.5055 0.3821 0.3486 -0.0862 -0.0360 0.0237  102 ASP A N   
757  C CA  . ASP A 102 ? 0.5147 0.3921 0.3551 -0.0916 -0.0371 0.0223  102 ASP A CA  
758  C C   . ASP A 102 ? 0.5418 0.4287 0.3855 -0.0944 -0.0378 0.0164  102 ASP A C   
759  O O   . ASP A 102 ? 0.5091 0.4001 0.3532 -0.0943 -0.0369 0.0123  102 ASP A O   
760  C CB  . ASP A 102 ? 0.5927 0.4626 0.4227 -0.0963 -0.0352 0.0218  102 ASP A CB  
761  C CG  . ASP A 102 ? 0.6824 0.5420 0.5081 -0.0934 -0.0346 0.0276  102 ASP A CG  
762  O OD1 . ASP A 102 ? 0.7055 0.5646 0.5359 -0.0899 -0.0362 0.0324  102 ASP A OD1 
763  O OD2 . ASP A 102 ? 0.7656 0.6181 0.5834 -0.0948 -0.0326 0.0273  102 ASP A OD2 
764  N N   . TRP A 103 ? 0.4740 0.3647 0.3203 -0.0964 -0.0397 0.0158  103 TRP A N   
765  C CA  . TRP A 103 ? 0.4704 0.3704 0.3214 -0.0971 -0.0405 0.0106  103 TRP A CA  
766  C C   . TRP A 103 ? 0.5104 0.4144 0.3572 -0.1016 -0.0387 0.0046  103 TRP A C   
767  O O   . TRP A 103 ? 0.4711 0.3828 0.3219 -0.1006 -0.0389 0.0001  103 TRP A O   
768  C CB  . TRP A 103 ? 0.4527 0.3555 0.3062 -0.0988 -0.0427 0.0107  103 TRP A CB  
769  C CG  . TRP A 103 ? 0.5254 0.4253 0.3722 -0.1046 -0.0426 0.0105  103 TRP A CG  
770  C CD1 . TRP A 103 ? 0.5785 0.4718 0.4223 -0.1052 -0.0437 0.0154  103 TRP A CD1 
771  C CD2 . TRP A 103 ? 0.4982 0.4015 0.3401 -0.1105 -0.0413 0.0053  103 TRP A CD2 
772  N NE1 . TRP A 103 ? 0.5727 0.4644 0.4095 -0.1110 -0.0433 0.0137  103 TRP A NE1 
773  C CE2 . TRP A 103 ? 0.5495 0.4472 0.3849 -0.1145 -0.0416 0.0075  103 TRP A CE2 
774  C CE3 . TRP A 103 ? 0.4729 0.3841 0.3156 -0.1127 -0.0400 -0.0010 103 TRP A CE3 
775  C CZ2 . TRP A 103 ? 0.5800 0.4792 0.4093 -0.1209 -0.0402 0.0036  103 TRP A CZ2 
776  C CZ3 . TRP A 103 ? 0.5307 0.4441 0.3680 -0.1190 -0.0386 -0.0049 103 TRP A CZ3 
777  C CH2 . TRP A 103 ? 0.5474 0.4548 0.3780 -0.1231 -0.0386 -0.0025 103 TRP A CH2 
778  N N   . TYR A 104 ? 0.4686 0.3678 0.3074 -0.1070 -0.0372 0.0042  104 TYR A N   
779  C CA  . TYR A 104 ? 0.4472 0.3505 0.2819 -0.1122 -0.0353 -0.0014 104 TYR A CA  
780  C C   . TYR A 104 ? 0.4649 0.3689 0.2994 -0.1105 -0.0340 -0.0034 104 TYR A C   
781  O O   . TYR A 104 ? 0.5059 0.4162 0.3394 -0.1142 -0.0330 -0.0089 104 TYR A O   
782  C CB  . TYR A 104 ? 0.4972 0.3949 0.3228 -0.1191 -0.0339 -0.0013 104 TYR A CB  
783  C CG  . TYR A 104 ? 0.4967 0.3824 0.3170 -0.1178 -0.0339 0.0050  104 TYR A CG  
784  C CD1 . TYR A 104 ? 0.4992 0.3772 0.3147 -0.1166 -0.0324 0.0069  104 TYR A CD1 
785  C CD2 . TYR A 104 ? 0.5037 0.3860 0.3241 -0.1171 -0.0358 0.0091  104 TYR A CD2 
786  C CE1 . TYR A 104 ? 0.5048 0.3719 0.3155 -0.1146 -0.0324 0.0127  104 TYR A CE1 
787  C CE2 . TYR A 104 ? 0.5550 0.4271 0.3707 -0.1155 -0.0359 0.0148  104 TYR A CE2 
788  C CZ  . TYR A 104 ? 0.5845 0.4489 0.3954 -0.1141 -0.0342 0.0167  104 TYR A CZ  
789  O OH  . TYR A 104 ? 0.5964 0.4505 0.4024 -0.1121 -0.0342 0.0222  104 TYR A OH  
790  N N   . PHE A 105 ? 0.4579 0.3561 0.2930 -0.1053 -0.0341 0.0006  105 PHE A N   
791  C CA  . PHE A 105 ? 0.4619 0.3603 0.2962 -0.1033 -0.0330 -0.0012 105 PHE A CA  
792  C C   . PHE A 105 ? 0.4522 0.3548 0.2942 -0.0962 -0.0344 -0.0004 105 PHE A C   
793  O O   . PHE A 105 ? 0.4565 0.3574 0.2977 -0.0931 -0.0337 -0.0004 105 PHE A O   
794  C CB  . PHE A 105 ? 0.4772 0.3643 0.3039 -0.1034 -0.0313 0.0022  105 PHE A CB  
795  C CG  . PHE A 105 ? 0.4789 0.3600 0.2965 -0.1104 -0.0297 0.0016  105 PHE A CG  
796  C CD1 . PHE A 105 ? 0.4772 0.3645 0.2931 -0.1170 -0.0291 -0.0036 105 PHE A CD1 
797  C CD2 . PHE A 105 ? 0.4838 0.3528 0.2946 -0.1102 -0.0289 0.0066  105 PHE A CD2 
798  C CE1 . PHE A 105 ? 0.5007 0.3818 0.3076 -0.1238 -0.0274 -0.0040 105 PHE A CE1 
799  C CE2 . PHE A 105 ? 0.4810 0.3431 0.2823 -0.1167 -0.0274 0.0062  105 PHE A CE2 
800  C CZ  . PHE A 105 ? 0.5164 0.3846 0.3160 -0.1235 -0.0267 0.0011  105 PHE A CZ  
801  N N   . ASP A 106 ? 0.4610 0.3684 0.3097 -0.0938 -0.0363 0.0002  106 ASP A N   
802  C CA  . ASP A 106 ? 0.4326 0.3418 0.2881 -0.0871 -0.0376 0.0024  106 ASP A CA  
803  C C   . ASP A 106 ? 0.4283 0.3415 0.2849 -0.0842 -0.0373 -0.0009 106 ASP A C   
804  O O   . ASP A 106 ? 0.4722 0.3930 0.3293 -0.0865 -0.0375 -0.0066 106 ASP A O   
805  C CB  . ASP A 106 ? 0.4132 0.3288 0.2750 -0.0863 -0.0397 0.0011  106 ASP A CB  
806  C CG  . ASP A 106 ? 0.4096 0.3259 0.2780 -0.0798 -0.0410 0.0037  106 ASP A CG  
807  O OD1 . ASP A 106 ? 0.4815 0.3918 0.3509 -0.0773 -0.0410 0.0093  106 ASP A OD1 
808  O OD2 . ASP A 106 ? 0.4628 0.3855 0.3348 -0.0775 -0.0420 0.0000  106 ASP A OD2 
809  N N   . LEU A 107 ? 0.4505 0.3586 0.3071 -0.0792 -0.0368 0.0026  107 LEU A N   
810  C CA  . LEU A 107 ? 0.4465 0.3573 0.3033 -0.0759 -0.0367 0.0000  107 LEU A CA  
811  C C   . LEU A 107 ? 0.4320 0.3374 0.2908 -0.0695 -0.0364 0.0054  107 LEU A C   
812  O O   . LEU A 107 ? 0.4420 0.3397 0.2980 -0.0689 -0.0351 0.0101  107 LEU A O   
813  C CB  . LEU A 107 ? 0.4626 0.3704 0.3120 -0.0795 -0.0350 -0.0023 107 LEU A CB  
814  C CG  . LEU A 107 ? 0.5016 0.4112 0.3498 -0.0764 -0.0349 -0.0049 107 LEU A CG  
815  C CD1 . LEU A 107 ? 0.5624 0.4835 0.4156 -0.0766 -0.0367 -0.0106 107 LEU A CD1 
816  C CD2 . LEU A 107 ? 0.5259 0.4309 0.3660 -0.0808 -0.0332 -0.0068 107 LEU A CD2 
817  N N   . TRP A 108 ? 0.4549 0.3640 0.3179 -0.0645 -0.0375 0.0047  108 TRP A N   
818  C CA  . TRP A 108 ? 0.4282 0.3323 0.2932 -0.0587 -0.0369 0.0100  108 TRP A CA  
819  C C   . TRP A 108 ? 0.4133 0.3180 0.2764 -0.0547 -0.0367 0.0081  108 TRP A C   
820  O O   . TRP A 108 ? 0.4468 0.3582 0.3108 -0.0547 -0.0381 0.0031  108 TRP A O   
821  C CB  . TRP A 108 ? 0.4262 0.3329 0.2983 -0.0560 -0.0385 0.0121  108 TRP A CB  
822  C CG  . TRP A 108 ? 0.4547 0.3603 0.3292 -0.0591 -0.0391 0.0149  108 TRP A CG  
823  C CD1 . TRP A 108 ? 0.4506 0.3595 0.3245 -0.0642 -0.0400 0.0120  108 TRP A CD1 
824  C CD2 . TRP A 108 ? 0.4537 0.3549 0.3315 -0.0570 -0.0389 0.0211  108 TRP A CD2 
825  N NE1 . TRP A 108 ? 0.4319 0.3383 0.3082 -0.0653 -0.0406 0.0160  108 TRP A NE1 
826  C CE2 . TRP A 108 ? 0.4531 0.3551 0.3320 -0.0611 -0.0401 0.0215  108 TRP A CE2 
827  C CE3 . TRP A 108 ? 0.4560 0.3532 0.3359 -0.0523 -0.0378 0.0263  108 TRP A CE3 
828  C CZ2 . TRP A 108 ? 0.4813 0.3806 0.3636 -0.0606 -0.0405 0.0269  108 TRP A CZ2 
829  C CZ3 . TRP A 108 ? 0.4527 0.3476 0.3365 -0.0519 -0.0379 0.0315  108 TRP A CZ3 
830  C CH2 . TRP A 108 ? 0.4837 0.3799 0.3690 -0.0560 -0.0395 0.0318  108 TRP A CH2 
831  N N   . GLY A 109 ? 0.4512 0.3491 0.3118 -0.0512 -0.0349 0.0122  109 GLY A N   
832  C CA  . GLY A 109 ? 0.4120 0.3097 0.2714 -0.0462 -0.0349 0.0117  109 GLY A CA  
833  C C   . GLY A 109 ? 0.4634 0.3635 0.3288 -0.0416 -0.0361 0.0135  109 GLY A C   
834  O O   . GLY A 109 ? 0.4433 0.3445 0.3138 -0.0423 -0.0369 0.0157  109 GLY A O   
835  N N   . ALA A 110 ? 0.4540 0.3543 0.3183 -0.0369 -0.0364 0.0128  110 ALA A N   
836  C CA  . ALA A 110 ? 0.4628 0.3649 0.3321 -0.0328 -0.0377 0.0141  110 ALA A CA  
837  C C   . ALA A 110 ? 0.4458 0.3416 0.3169 -0.0293 -0.0359 0.0210  110 ALA A C   
838  O O   . ALA A 110 ? 0.4807 0.3767 0.3559 -0.0265 -0.0366 0.0230  110 ALA A O   
839  C CB  . ALA A 110 ? 0.4583 0.3633 0.3250 -0.0293 -0.0391 0.0102  110 ALA A CB  
840  N N   . GLY A 111 ? 0.4333 0.3233 0.3010 -0.0293 -0.0333 0.0245  111 GLY A N   
841  C CA  . GLY A 111 ? 0.4351 0.3198 0.3048 -0.0263 -0.0310 0.0311  111 GLY A CA  
842  C C   . GLY A 111 ? 0.4744 0.3550 0.3404 -0.0208 -0.0293 0.0329  111 GLY A C   
843  O O   . GLY A 111 ? 0.5311 0.4136 0.3951 -0.0184 -0.0307 0.0298  111 GLY A O   
844  N N   . THR A 112 ? 0.4757 0.3507 0.3403 -0.0187 -0.0262 0.0379  112 THR A N   
845  C CA  . THR A 112 ? 0.4486 0.3189 0.3096 -0.0134 -0.0239 0.0406  112 THR A CA  
846  C C   . THR A 112 ? 0.4794 0.3489 0.3467 -0.0111 -0.0224 0.0466  112 THR A C   
847  O O   . THR A 112 ? 0.4742 0.3428 0.3452 -0.0123 -0.0210 0.0505  112 THR A O   
848  C CB  . THR A 112 ? 0.4816 0.3462 0.3357 -0.0126 -0.0212 0.0415  112 THR A CB  
849  O OG1 . THR A 112 ? 0.4993 0.3650 0.3478 -0.0155 -0.0227 0.0357  112 THR A OG1 
850  C CG2 . THR A 112 ? 0.5011 0.3606 0.3511 -0.0070 -0.0184 0.0444  112 THR A CG2 
851  N N   . THR A 113 ? 0.4472 0.3162 0.3149 -0.0076 -0.0225 0.0474  113 THR A N   
852  C CA  . THR A 113 ? 0.4653 0.3328 0.3383 -0.0056 -0.0207 0.0533  113 THR A CA  
853  C C   . THR A 113 ? 0.5630 0.4252 0.4322 -0.0018 -0.0165 0.0575  113 THR A C   
854  O O   . THR A 113 ? 0.5557 0.4146 0.4178 0.0013  -0.0155 0.0562  113 THR A O   
855  C CB  . THR A 113 ? 0.4867 0.3543 0.3602 -0.0030 -0.0221 0.0528  113 THR A CB  
856  O OG1 . THR A 113 ? 0.4730 0.3454 0.3499 -0.0060 -0.0258 0.0488  113 THR A OG1 
857  C CG2 . THR A 113 ? 0.4774 0.3429 0.3557 -0.0013 -0.0199 0.0589  113 THR A CG2 
858  N N   . VAL A 114 ? 0.5039 0.3657 0.3778 -0.0020 -0.0140 0.0625  114 VAL A N   
859  C CA  . VAL A 114 ? 0.4962 0.3534 0.3669 0.0018  -0.0097 0.0666  114 VAL A CA  
860  C C   . VAL A 114 ? 0.5440 0.4016 0.4206 0.0037  -0.0077 0.0719  114 VAL A C   
861  O O   . VAL A 114 ? 0.4886 0.3500 0.3736 0.0011  -0.0085 0.0744  114 VAL A O   
862  C CB  . VAL A 114 ? 0.4994 0.3557 0.3709 0.0007  -0.0079 0.0686  114 VAL A CB  
863  C CG1 . VAL A 114 ? 0.5203 0.3726 0.3900 0.0053  -0.0031 0.0735  114 VAL A CG1 
864  C CG2 . VAL A 114 ? 0.4812 0.3362 0.3462 -0.0017 -0.0097 0.0635  114 VAL A CG2 
865  N N   . THR A 115 ? 0.5192 0.3728 0.3911 0.0079  -0.0053 0.0734  115 THR A N   
866  C CA  . THR A 115 ? 0.5549 0.4083 0.4315 0.0095  -0.0033 0.0783  115 THR A CA  
867  C C   . THR A 115 ? 0.5640 0.4143 0.4389 0.0133  0.0019  0.0832  115 THR A C   
868  O O   . THR A 115 ? 0.5290 0.3743 0.3952 0.0170  0.0039  0.0824  115 THR A O   
869  C CB  . THR A 115 ? 0.5529 0.4037 0.4247 0.0116  -0.0047 0.0764  115 THR A CB  
870  O OG1 . THR A 115 ? 0.5372 0.3914 0.4108 0.0085  -0.0095 0.0716  115 THR A OG1 
871  C CG2 . THR A 115 ? 0.5363 0.3857 0.4118 0.0130  -0.0025 0.0814  115 THR A CG2 
872  N N   . VAL A 116 ? 0.5064 0.3599 0.3895 0.0123  0.0041  0.0879  116 VAL A N   
873  C CA  . VAL A 116 ? 0.5318 0.3833 0.4143 0.0160  0.0095  0.0927  116 VAL A CA  
874  C C   . VAL A 116 ? 0.5429 0.3935 0.4275 0.0177  0.0121  0.0967  116 VAL A C   
875  O O   . VAL A 116 ? 0.5199 0.3743 0.4128 0.0149  0.0111  0.0991  116 VAL A O   
876  C CB  . VAL A 116 ? 0.5585 0.4143 0.4488 0.0148  0.0107  0.0958  116 VAL A CB  
877  C CG1 . VAL A 116 ? 0.5915 0.4460 0.4816 0.0192  0.0165  0.1008  116 VAL A CG1 
878  C CG2 . VAL A 116 ? 0.5279 0.3833 0.4149 0.0129  0.0080  0.0919  116 VAL A CG2 
879  N N   . SER A 117 ? 0.5565 0.4014 0.4325 0.0221  0.0152  0.0974  117 SER A N   
880  C CA  . SER A 117 ? 0.5600 0.4025 0.4350 0.0233  0.0165  0.0997  117 SER A CA  
881  C C   . SER A 117 ? 0.6351 0.4752 0.5085 0.0273  0.0229  0.1050  117 SER A C   
882  O O   . SER A 117 ? 0.5914 0.4275 0.4568 0.0310  0.0255  0.1043  117 SER A O   
883  C CB  . SER A 117 ? 0.5722 0.4099 0.4374 0.0249  0.0134  0.0949  117 SER A CB  
884  O OG  . SER A 117 ? 0.5897 0.4230 0.4508 0.0273  0.0150  0.0970  117 SER A OG  
885  N N   . ALA A 118 ? 0.6724 0.5151 0.5535 0.0262  0.0256  0.1101  118 ALA A N   
886  C CA  . ALA A 118 ? 0.6465 0.4871 0.5260 0.0297  0.0320  0.1153  118 ALA A CA  
887  C C   . ALA A 118 ? 0.7093 0.5512 0.5950 0.0273  0.0331  0.1193  118 ALA A C   
888  O O   . ALA A 118 ? 0.6805 0.5288 0.5774 0.0233  0.0322  0.1215  118 ALA A O   
889  C CB  . ALA A 118 ? 0.6546 0.4996 0.5393 0.0310  0.0357  0.1181  118 ALA A CB  
890  N N   . ALA A 119 ? 0.7072 0.5424 0.5850 0.0296  0.0347  0.1202  119 ALA A N   
891  C CA  . ALA A 119 ? 0.8090 0.6432 0.6903 0.0273  0.0356  0.1237  119 ALA A CA  
892  C C   . ALA A 119 ? 0.8788 0.7175 0.7684 0.0267  0.0417  0.1303  119 ALA A C   
893  O O   . ALA A 119 ? 0.8690 0.7094 0.7582 0.0298  0.0463  0.1323  119 ALA A O   
894  C CB  . ALA A 119 ? 0.8694 0.6944 0.7385 0.0306  0.0357  0.1229  119 ALA A CB  
895  N N   . GLY A 120 ? 0.8334 0.6739 0.7303 0.0225  0.0416  0.1334  120 GLY A N   
896  C CA  . GLY A 120 ? 0.9751 0.8205 0.8809 0.0208  0.0470  0.1396  120 GLY A CA  
897  C C   . GLY A 120 ? 1.0107 0.8491 0.9093 0.0229  0.0521  0.1434  120 GLY A C   
898  O O   . GLY A 120 ? 0.9845 0.8208 0.8769 0.0276  0.0572  0.1450  120 GLY A O   
899  N N   . SER A 134 ? 0.8066 0.7246 0.7653 -0.0355 -0.0585 0.1112  134 SER A N   
900  C CA  . SER A 134 ? 0.7637 0.6762 0.7128 -0.0402 -0.0620 0.1078  134 SER A CA  
901  C C   . SER A 134 ? 0.6956 0.6004 0.6345 -0.0431 -0.0595 0.1024  134 SER A C   
902  O O   . SER A 134 ? 0.6926 0.5918 0.6221 -0.0466 -0.0612 0.0993  134 SER A O   
903  C CB  . SER A 134 ? 0.8525 0.7610 0.7959 -0.0378 -0.0640 0.1103  134 SER A CB  
904  O OG  . SER A 134 ? 0.8537 0.7531 0.7876 -0.0342 -0.0601 0.1102  134 SER A OG  
905  N N   . ASP A 135 ? 0.6839 0.5889 0.6248 -0.0420 -0.0557 0.1009  135 ASP A N   
906  C CA  . ASP A 135 ? 0.6505 0.5509 0.5841 -0.0455 -0.0545 0.0954  135 ASP A CA  
907  C C   . ASP A 135 ? 0.5959 0.5006 0.5325 -0.0511 -0.0583 0.0926  135 ASP A C   
908  O O   . ASP A 135 ? 0.6035 0.5151 0.5498 -0.0517 -0.0604 0.0948  135 ASP A O   
909  C CB  . ASP A 135 ? 0.6276 0.5285 0.5639 -0.0431 -0.0503 0.0947  135 ASP A CB  
910  C CG  . ASP A 135 ? 0.7852 0.6810 0.7172 -0.0377 -0.0459 0.0965  135 ASP A CG  
911  O OD1 . ASP A 135 ? 0.8253 0.7160 0.7510 -0.0360 -0.0460 0.0979  135 ASP A OD1 
912  O OD2 . ASP A 135 ? 0.7575 0.6537 0.6917 -0.0352 -0.0423 0.0965  135 ASP A OD2 
913  N N   . ILE A 136 ? 0.5418 0.4423 0.4702 -0.0552 -0.0589 0.0875  136 ILE A N   
914  C CA  . ILE A 136 ? 0.5106 0.4145 0.4409 -0.0602 -0.0621 0.0843  136 ILE A CA  
915  C C   . ILE A 136 ? 0.5640 0.4714 0.5006 -0.0600 -0.0606 0.0829  136 ILE A C   
916  O O   . ILE A 136 ? 0.5812 0.4857 0.5145 -0.0583 -0.0571 0.0808  136 ILE A O   
917  C CB  . ILE A 136 ? 0.5235 0.4223 0.4430 -0.0643 -0.0629 0.0795  136 ILE A CB  
918  C CG1 . ILE A 136 ? 0.5778 0.4721 0.4905 -0.0644 -0.0642 0.0814  136 ILE A CG1 
919  C CG2 . ILE A 136 ? 0.5721 0.4742 0.4933 -0.0692 -0.0662 0.0760  136 ILE A CG2 
920  C CD1 . ILE A 136 ? 0.5604 0.4498 0.4624 -0.0691 -0.0649 0.0770  136 ILE A CD1 
921  N N   . VAL A 137 ? 0.5285 0.4416 0.4739 -0.0615 -0.0632 0.0843  137 VAL A N   
922  C CA  . VAL A 137 ? 0.5209 0.4366 0.4719 -0.0617 -0.0620 0.0831  137 VAL A CA  
923  C C   . VAL A 137 ? 0.5349 0.4497 0.4823 -0.0662 -0.0644 0.0778  137 VAL A C   
924  O O   . VAL A 137 ? 0.5006 0.4165 0.4472 -0.0698 -0.0682 0.0769  137 VAL A O   
925  C CB  . VAL A 137 ? 0.5402 0.4622 0.5026 -0.0609 -0.0631 0.0877  137 VAL A CB  
926  C CG1 . VAL A 137 ? 0.5722 0.4957 0.5396 -0.0616 -0.0621 0.0866  137 VAL A CG1 
927  C CG2 . VAL A 137 ? 0.5790 0.5025 0.5450 -0.0560 -0.0606 0.0929  137 VAL A CG2 
928  N N   . LEU A 138 ? 0.4834 0.3963 0.4284 -0.0658 -0.0621 0.0741  138 LEU A N   
929  C CA  . LEU A 138 ? 0.4591 0.3717 0.4014 -0.0692 -0.0638 0.0689  138 LEU A CA  
930  C C   . LEU A 138 ? 0.4995 0.4141 0.4486 -0.0690 -0.0640 0.0693  138 LEU A C   
931  O O   . LEU A 138 ? 0.5122 0.4264 0.4637 -0.0657 -0.0609 0.0708  138 LEU A O   
932  C CB  . LEU A 138 ? 0.4317 0.3408 0.3656 -0.0692 -0.0616 0.0639  138 LEU A CB  
933  C CG  . LEU A 138 ? 0.4640 0.3699 0.3900 -0.0698 -0.0608 0.0631  138 LEU A CG  
934  C CD1 . LEU A 138 ? 0.4889 0.3921 0.4070 -0.0703 -0.0586 0.0581  138 LEU A CD1 
935  C CD2 . LEU A 138 ? 0.4860 0.3922 0.4096 -0.0738 -0.0645 0.0627  138 LEU A CD2 
936  N N   . THR A 139 ? 0.4566 0.3727 0.4082 -0.0726 -0.0676 0.0679  139 THR A N   
937  C CA  . THR A 139 ? 0.4824 0.3993 0.4396 -0.0731 -0.0681 0.0680  139 THR A CA  
938  C C   . THR A 139 ? 0.4671 0.3817 0.4193 -0.0752 -0.0694 0.0620  139 THR A C   
939  O O   . THR A 139 ? 0.4904 0.4050 0.4393 -0.0786 -0.0724 0.0593  139 THR A O   
940  C CB  . THR A 139 ? 0.5046 0.4253 0.4694 -0.0757 -0.0715 0.0715  139 THR A CB  
941  O OG1 . THR A 139 ? 0.5237 0.4474 0.4935 -0.0731 -0.0700 0.0770  139 THR A OG1 
942  C CG2 . THR A 139 ? 0.5303 0.4510 0.5006 -0.0767 -0.0719 0.0719  139 THR A CG2 
943  N N   . GLN A 140 ? 0.4137 0.3262 0.3654 -0.0730 -0.0673 0.0601  140 GLN A N   
944  C CA  . GLN A 140 ? 0.4319 0.3423 0.3796 -0.0740 -0.0683 0.0546  140 GLN A CA  
945  C C   . GLN A 140 ? 0.4690 0.3786 0.4216 -0.0756 -0.0704 0.0553  140 GLN A C   
946  O O   . GLN A 140 ? 0.4627 0.3726 0.4213 -0.0745 -0.0694 0.0595  140 GLN A O   
947  C CB  . GLN A 140 ? 0.4591 0.3677 0.4027 -0.0703 -0.0650 0.0518  140 GLN A CB  
948  C CG  . GLN A 140 ? 0.4782 0.3872 0.4166 -0.0693 -0.0630 0.0509  140 GLN A CG  
949  C CD  . GLN A 140 ? 0.4815 0.3893 0.4151 -0.0664 -0.0604 0.0472  140 GLN A CD  
950  O OE1 . GLN A 140 ? 0.4721 0.3795 0.4030 -0.0646 -0.0580 0.0481  140 GLN A OE1 
951  N NE2 . GLN A 140 ? 0.4532 0.3605 0.3850 -0.0661 -0.0612 0.0427  140 GLN A NE2 
952  N N   . SER A 141 ? 0.4455 0.3535 0.3949 -0.0780 -0.0729 0.0507  141 SER A N   
953  C CA  . SER A 141 ? 0.4606 0.3665 0.4134 -0.0798 -0.0751 0.0508  141 SER A CA  
954  C C   . SER A 141 ? 0.4710 0.3737 0.4179 -0.0798 -0.0760 0.0445  141 SER A C   
955  O O   . SER A 141 ? 0.4884 0.3920 0.4304 -0.0814 -0.0772 0.0406  141 SER A O   
956  C CB  . SER A 141 ? 0.5079 0.4158 0.4644 -0.0843 -0.0789 0.0529  141 SER A CB  
957  O OG  . SER A 141 ? 0.5594 0.4646 0.5193 -0.0859 -0.0805 0.0533  141 SER A OG  
958  N N   . PRO A 142 ? 0.4453 0.3442 0.3920 -0.0777 -0.0753 0.0431  142 PRO A N   
959  C CA  . PRO A 142 ? 0.4550 0.3520 0.4062 -0.0753 -0.0732 0.0475  142 PRO A CA  
960  C C   . PRO A 142 ? 0.5037 0.4018 0.4536 -0.0708 -0.0693 0.0486  142 PRO A C   
961  O O   . PRO A 142 ? 0.4690 0.3690 0.4145 -0.0696 -0.0683 0.0458  142 PRO A O   
962  C CB  . PRO A 142 ? 0.4735 0.3649 0.4223 -0.0748 -0.0743 0.0442  142 PRO A CB  
963  C CG  . PRO A 142 ? 0.4949 0.3863 0.4368 -0.0736 -0.0748 0.0377  142 PRO A CG  
964  C CD  . PRO A 142 ? 0.4586 0.3544 0.3998 -0.0770 -0.0763 0.0370  142 PRO A CD  
965  N N   . THR A 143 ? 0.4780 0.3747 0.4316 -0.0685 -0.0670 0.0529  143 THR A N   
966  C CA  . THR A 143 ? 0.5287 0.4258 0.4804 -0.0640 -0.0632 0.0539  143 THR A CA  
967  C C   . THR A 143 ? 0.4999 0.3926 0.4470 -0.0604 -0.0622 0.0506  143 THR A C   
968  O O   . THR A 143 ? 0.4966 0.3895 0.4405 -0.0566 -0.0597 0.0497  143 THR A O   
969  C CB  . THR A 143 ? 0.5523 0.4507 0.5100 -0.0631 -0.0608 0.0605  143 THR A CB  
970  O OG1 . THR A 143 ? 0.6363 0.5313 0.5973 -0.0639 -0.0612 0.0626  143 THR A OG1 
971  C CG2 . THR A 143 ? 0.5501 0.4532 0.5130 -0.0660 -0.0619 0.0641  143 THR A CG2 
972  N N   . SER A 144 ? 0.4826 0.3713 0.4291 -0.0613 -0.0643 0.0486  144 SER A N   
973  C CA  . SER A 144 ? 0.5191 0.4038 0.4602 -0.0576 -0.0640 0.0444  144 SER A CA  
974  C C   . SER A 144 ? 0.5217 0.4031 0.4608 -0.0596 -0.0673 0.0404  144 SER A C   
975  O O   . SER A 144 ? 0.5219 0.4020 0.4644 -0.0637 -0.0693 0.0423  144 SER A O   
976  C CB  . SER A 144 ? 0.6040 0.4844 0.5450 -0.0537 -0.0615 0.0474  144 SER A CB  
977  O OG  . SER A 144 ? 0.7169 0.5939 0.6623 -0.0562 -0.0619 0.0516  144 SER A OG  
978  N N   . LEU A 145 ? 0.5116 0.3919 0.4454 -0.0566 -0.0677 0.0350  145 LEU A N   
979  C CA  . LEU A 145 ? 0.5751 0.4518 0.5061 -0.0577 -0.0705 0.0307  145 LEU A CA  
980  C C   . LEU A 145 ? 0.5644 0.4389 0.4900 -0.0525 -0.0701 0.0258  145 LEU A C   
981  O O   . LEU A 145 ? 0.5438 0.4221 0.4675 -0.0491 -0.0683 0.0242  145 LEU A O   
982  C CB  . LEU A 145 ? 0.5657 0.4460 0.4965 -0.0623 -0.0729 0.0279  145 LEU A CB  
983  C CG  . LEU A 145 ? 0.5478 0.4335 0.4747 -0.0612 -0.0725 0.0226  145 LEU A CG  
984  C CD1 . LEU A 145 ? 0.5744 0.4618 0.4997 -0.0655 -0.0750 0.0192  145 LEU A CD1 
985  C CD2 . LEU A 145 ? 0.5307 0.4216 0.4590 -0.0607 -0.0699 0.0253  145 LEU A CD2 
986  N N   . ALA A 146 ? 0.5323 0.4004 0.4554 -0.0518 -0.0721 0.0235  146 ALA A N   
987  C CA  . ALA A 146 ? 0.5058 0.3719 0.4237 -0.0466 -0.0723 0.0184  146 ALA A CA  
988  C C   . ALA A 146 ? 0.5623 0.4285 0.4775 -0.0484 -0.0749 0.0128  146 ALA A C   
989  O O   . ALA A 146 ? 0.5503 0.4116 0.4660 -0.0519 -0.0769 0.0136  146 ALA A O   
990  C CB  . ALA A 146 ? 0.5519 0.4087 0.4679 -0.0433 -0.0721 0.0207  146 ALA A CB  
991  N N   . VAL A 147 ? 0.5708 0.4417 0.4827 -0.0454 -0.0749 0.0069  147 VAL A N   
992  C CA  . VAL A 147 ? 0.6014 0.4738 0.5106 -0.0468 -0.0768 0.0012  147 VAL A CA  
993  C C   . VAL A 147 ? 0.6140 0.4855 0.5189 -0.0406 -0.0770 -0.0042 147 VAL A C   
994  O O   . VAL A 147 ? 0.6447 0.5196 0.5491 -0.0361 -0.0754 -0.0049 147 VAL A O   
995  C CB  . VAL A 147 ? 0.5881 0.4699 0.4985 -0.0503 -0.0759 -0.0002 147 VAL A CB  
996  C CG1 . VAL A 147 ? 0.5845 0.4694 0.4914 -0.0510 -0.0772 -0.0069 147 VAL A CG1 
997  C CG2 . VAL A 147 ? 0.5852 0.4675 0.4995 -0.0562 -0.0763 0.0050  147 VAL A CG2 
998  N N   . SER A 148 ? 0.5868 0.4537 0.4883 -0.0401 -0.0791 -0.0083 148 SER A N   
999  C CA  . SER A 148 ? 0.6038 0.4697 0.5012 -0.0336 -0.0794 -0.0136 148 SER A CA  
1000 C C   . SER A 148 ? 0.6245 0.5014 0.5215 -0.0323 -0.0785 -0.0194 148 SER A C   
1001 O O   . SER A 148 ? 0.6247 0.5078 0.5228 -0.0371 -0.0782 -0.0207 148 SER A O   
1002 C CB  . SER A 148 ? 0.7926 0.6494 0.6860 -0.0328 -0.0817 -0.0161 148 SER A CB  
1003 O OG  . SER A 148 ? 0.8048 0.6512 0.6984 -0.0342 -0.0823 -0.0107 148 SER A OG  
1004 N N   . LEU A 149 ? 0.5822 0.4616 0.4774 -0.0258 -0.0781 -0.0228 149 LEU A N   
1005 C CA  . LEU A 149 ? 0.6221 0.5126 0.5173 -0.0243 -0.0772 -0.0288 149 LEU A CA  
1006 C C   . LEU A 149 ? 0.6679 0.5601 0.5614 -0.0278 -0.0781 -0.0332 149 LEU A C   
1007 O O   . LEU A 149 ? 0.6400 0.5241 0.5306 -0.0272 -0.0799 -0.0344 149 LEU A O   
1008 C CB  . LEU A 149 ? 0.6462 0.5388 0.5393 -0.0164 -0.0774 -0.0331 149 LEU A CB  
1009 C CG  . LEU A 149 ? 0.7596 0.6549 0.6540 -0.0126 -0.0763 -0.0306 149 LEU A CG  
1010 C CD1 . LEU A 149 ? 0.8420 0.7412 0.7344 -0.0050 -0.0770 -0.0363 149 LEU A CD1 
1011 C CD2 . LEU A 149 ? 0.7923 0.6968 0.6900 -0.0168 -0.0742 -0.0292 149 LEU A CD2 
1012 N N   . GLY A 150 ? 0.6047 0.5069 0.4996 -0.0315 -0.0767 -0.0355 150 GLY A N   
1013 C CA  . GLY A 150 ? 0.6272 0.5322 0.5202 -0.0349 -0.0771 -0.0399 150 GLY A CA  
1014 C C   . GLY A 150 ? 0.6094 0.5088 0.5022 -0.0417 -0.0783 -0.0363 150 GLY A C   
1015 O O   . GLY A 150 ? 0.6340 0.5355 0.5247 -0.0451 -0.0786 -0.0395 150 GLY A O   
1016 N N   . GLN A 151 ? 0.5816 0.4746 0.4766 -0.0437 -0.0789 -0.0297 151 GLN A N   
1017 C CA  . GLN A 151 ? 0.5862 0.4749 0.4817 -0.0501 -0.0803 -0.0263 151 GLN A CA  
1018 C C   . GLN A 151 ? 0.6123 0.5074 0.5106 -0.0550 -0.0789 -0.0229 151 GLN A C   
1019 O O   . GLN A 151 ? 0.5908 0.4935 0.4899 -0.0539 -0.0768 -0.0241 151 GLN A O   
1020 C CB  . GLN A 151 ? 0.6208 0.4991 0.5173 -0.0499 -0.0818 -0.0212 151 GLN A CB  
1021 C CG  . GLN A 151 ? 0.6848 0.5544 0.5773 -0.0459 -0.0835 -0.0242 151 GLN A CG  
1022 C CD  . GLN A 151 ? 0.7906 0.6575 0.6793 -0.0488 -0.0854 -0.0283 151 GLN A CD  
1023 O OE1 . GLN A 151 ? 0.8440 0.7149 0.7295 -0.0465 -0.0851 -0.0345 151 GLN A OE1 
1024 N NE2 . GLN A 151 ? 0.8615 0.7222 0.7507 -0.0542 -0.0874 -0.0249 151 GLN A NE2 
1025 N N   . ARG A 152 ? 0.5652 0.4572 0.4648 -0.0605 -0.0802 -0.0186 152 ARG A N   
1026 C CA  . ARG A 152 ? 0.5343 0.4319 0.4357 -0.0650 -0.0792 -0.0158 152 ARG A CA  
1027 C C   . ARG A 152 ? 0.5042 0.3994 0.4102 -0.0659 -0.0789 -0.0086 152 ARG A C   
1028 O O   . ARG A 152 ? 0.5059 0.3945 0.4138 -0.0662 -0.0804 -0.0051 152 ARG A O   
1029 C CB  . ARG A 152 ? 0.5079 0.4051 0.4070 -0.0705 -0.0810 -0.0169 152 ARG A CB  
1030 C CG  . ARG A 152 ? 0.5269 0.4280 0.4272 -0.0754 -0.0806 -0.0132 152 ARG A CG  
1031 C CD  . ARG A 152 ? 0.5183 0.4186 0.4151 -0.0805 -0.0827 -0.0149 152 ARG A CD  
1032 N NE  . ARG A 152 ? 0.5145 0.4187 0.4063 -0.0799 -0.0816 -0.0218 152 ARG A NE  
1033 C CZ  . ARG A 152 ? 0.5418 0.4530 0.4318 -0.0809 -0.0792 -0.0240 152 ARG A CZ  
1034 N NH1 . ARG A 152 ? 0.5394 0.4537 0.4313 -0.0827 -0.0777 -0.0201 152 ARG A NH1 
1035 N NH2 . ARG A 152 ? 0.6241 0.5390 0.5101 -0.0804 -0.0781 -0.0303 152 ARG A NH2 
1036 N N   . ALA A 153 ? 0.4683 0.3688 0.3762 -0.0662 -0.0767 -0.0063 153 ALA A N   
1037 C CA  . ALA A 153 ? 0.4578 0.3570 0.3698 -0.0675 -0.0762 0.0004  153 ALA A CA  
1038 C C   . ALA A 153 ? 0.5225 0.4250 0.4346 -0.0726 -0.0764 0.0023  153 ALA A C   
1039 O O   . ALA A 153 ? 0.5349 0.4424 0.4440 -0.0738 -0.0752 -0.0009 153 ALA A O   
1040 C CB  . ALA A 153 ? 0.4898 0.3912 0.4031 -0.0633 -0.0735 0.0019  153 ALA A CB  
1041 N N   . THR A 154 ? 0.4869 0.3868 0.4023 -0.0757 -0.0780 0.0075  154 THR A N   
1042 C CA  . THR A 154 ? 0.5006 0.4030 0.4161 -0.0800 -0.0786 0.0100  154 THR A CA  
1043 C C   . THR A 154 ? 0.4919 0.3940 0.4128 -0.0798 -0.0778 0.0169  154 THR A C   
1044 O O   . THR A 154 ? 0.4936 0.3922 0.4184 -0.0790 -0.0786 0.0201  154 THR A O   
1045 C CB  . THR A 154 ? 0.5074 0.4072 0.4218 -0.0841 -0.0821 0.0092  154 THR A CB  
1046 O OG1 . THR A 154 ? 0.4987 0.3983 0.4079 -0.0837 -0.0825 0.0026  154 THR A OG1 
1047 C CG2 . THR A 154 ? 0.4732 0.3752 0.3875 -0.0883 -0.0832 0.0120  154 THR A CG2 
1048 N N   . ILE A 155 ? 0.4412 0.3466 0.3618 -0.0802 -0.0761 0.0190  155 ILE A N   
1049 C CA  . ILE A 155 ? 0.4500 0.3555 0.3752 -0.0794 -0.0748 0.0252  155 ILE A CA  
1050 C C   . ILE A 155 ? 0.4794 0.3870 0.4041 -0.0828 -0.0757 0.0278  155 ILE A C   
1051 O O   . ILE A 155 ? 0.5137 0.4232 0.4335 -0.0842 -0.0750 0.0248  155 ILE A O   
1052 C CB  . ILE A 155 ? 0.4470 0.3537 0.3717 -0.0751 -0.0713 0.0252  155 ILE A CB  
1053 C CG1 . ILE A 155 ? 0.4546 0.3590 0.3790 -0.0713 -0.0708 0.0225  155 ILE A CG1 
1054 C CG2 . ILE A 155 ? 0.4302 0.3369 0.3589 -0.0739 -0.0697 0.0315  155 ILE A CG2 
1055 C CD1 . ILE A 155 ? 0.4701 0.3762 0.3926 -0.0673 -0.0678 0.0211  155 ILE A CD1 
1056 N N   . SER A 156 ? 0.4615 0.3688 0.3915 -0.0838 -0.0769 0.0333  156 SER A N   
1057 C CA  . SER A 156 ? 0.4809 0.3900 0.4112 -0.0865 -0.0782 0.0365  156 SER A CA  
1058 C C   . SER A 156 ? 0.4790 0.3892 0.4114 -0.0839 -0.0754 0.0410  156 SER A C   
1059 O O   . SER A 156 ? 0.4420 0.3518 0.3786 -0.0808 -0.0735 0.0437  156 SER A O   
1060 C CB  . SER A 156 ? 0.5027 0.4114 0.4381 -0.0891 -0.0816 0.0397  156 SER A CB  
1061 O OG  . SER A 156 ? 0.5475 0.4583 0.4842 -0.0911 -0.0832 0.0434  156 SER A OG  
1062 N N   . CYS A 157 ? 0.4861 0.3972 0.4150 -0.0852 -0.0752 0.0418  157 CYS A N   
1063 C CA  . CYS A 157 ? 0.4660 0.3775 0.3963 -0.0830 -0.0731 0.0464  157 CYS A CA  
1064 C C   . CYS A 157 ? 0.5351 0.4474 0.4655 -0.0856 -0.0758 0.0495  157 CYS A C   
1065 O O   . CYS A 157 ? 0.5173 0.4290 0.4418 -0.0886 -0.0773 0.0469  157 CYS A O   
1066 C CB  . CYS A 157 ? 0.5268 0.4374 0.4504 -0.0819 -0.0701 0.0436  157 CYS A CB  
1067 S SG  . CYS A 157 ? 0.6186 0.5283 0.5423 -0.0793 -0.0675 0.0489  157 CYS A SG  
1068 N N   . LYS A 158 ? 0.4827 0.3966 0.4197 -0.0843 -0.0763 0.0552  158 LYS A N   
1069 C CA  . LYS A 158 ? 0.5014 0.4166 0.4392 -0.0860 -0.0790 0.0586  158 LYS A CA  
1070 C C   . LYS A 158 ? 0.5143 0.4298 0.4534 -0.0827 -0.0768 0.0633  158 LYS A C   
1071 O O   . LYS A 158 ? 0.5586 0.4749 0.5028 -0.0793 -0.0741 0.0659  158 LYS A O   
1072 C CB  . LYS A 158 ? 0.5003 0.4184 0.4459 -0.0879 -0.0826 0.0612  158 LYS A CB  
1073 C CG  . LYS A 158 ? 0.5350 0.4518 0.4777 -0.0919 -0.0857 0.0565  158 LYS A CG  
1074 C CD  . LYS A 158 ? 0.5562 0.4749 0.5059 -0.0943 -0.0893 0.0583  158 LYS A CD  
1075 C CE  . LYS A 158 ? 0.5498 0.4663 0.4944 -0.0982 -0.0925 0.0532  158 LYS A CE  
1076 N NZ  . LYS A 158 ? 0.5941 0.5118 0.5442 -0.1014 -0.0966 0.0547  158 LYS A NZ  
1077 N N   . ALA A 159 ? 0.4688 0.3829 0.4026 -0.0836 -0.0777 0.0641  159 ALA A N   
1078 C CA  . ALA A 159 ? 0.5076 0.4206 0.4409 -0.0802 -0.0756 0.0682  159 ALA A CA  
1079 C C   . ALA A 159 ? 0.5627 0.4790 0.5018 -0.0798 -0.0786 0.0735  159 ALA A C   
1080 O O   . ALA A 159 ? 0.5335 0.4510 0.4722 -0.0832 -0.0828 0.0731  159 ALA A O   
1081 C CB  . ALA A 159 ? 0.4834 0.3918 0.4060 -0.0812 -0.0744 0.0659  159 ALA A CB  
1082 N N   . SER A 160 ? 0.5105 0.4279 0.4538 -0.0756 -0.0766 0.0782  160 SER A N   
1083 C CA  . SER A 160 ? 0.5498 0.4714 0.4996 -0.0744 -0.0792 0.0834  160 SER A CA  
1084 C C   . SER A 160 ? 0.6290 0.5477 0.5715 -0.0752 -0.0817 0.0842  160 SER A C   
1085 O O   . SER A 160 ? 0.6051 0.5275 0.5517 -0.0755 -0.0855 0.0874  160 SER A O   
1086 C CB  . SER A 160 ? 0.5170 0.4411 0.4736 -0.0694 -0.0760 0.0880  160 SER A CB  
1087 O OG  . SER A 160 ? 0.5537 0.4725 0.5034 -0.0660 -0.0722 0.0880  160 SER A OG  
1088 N N   . GLN A 161 ? 0.5864 0.4987 0.5182 -0.0755 -0.0797 0.0815  161 GLN A N   
1089 C CA  . GLN A 161 ? 0.5930 0.5010 0.5160 -0.0768 -0.0817 0.0817  161 GLN A CA  
1090 C C   . GLN A 161 ? 0.6276 0.5305 0.5401 -0.0807 -0.0806 0.0760  161 GLN A C   
1091 O O   . GLN A 161 ? 0.5880 0.4905 0.5000 -0.0811 -0.0776 0.0723  161 GLN A O   
1092 C CB  . GLN A 161 ? 0.6031 0.5068 0.5222 -0.0723 -0.0791 0.0852  161 GLN A CB  
1093 C CG  . GLN A 161 ? 0.7008 0.6094 0.6296 -0.0674 -0.0791 0.0910  161 GLN A CG  
1094 C CD  . GLN A 161 ? 0.7227 0.6262 0.6473 -0.0623 -0.0756 0.0936  161 GLN A CD  
1095 O OE1 . GLN A 161 ? 0.7159 0.6212 0.6459 -0.0581 -0.0722 0.0958  161 GLN A OE1 
1096 N NE2 . GLN A 161 ? 0.7274 0.6238 0.6413 -0.0627 -0.0761 0.0935  161 GLN A NE2 
1097 N N   . SER A 162 ? 0.5631 0.4623 0.4670 -0.0836 -0.0829 0.0751  162 SER A N   
1098 C CA  . SER A 162 ? 0.6089 0.5037 0.5026 -0.0877 -0.0817 0.0698  162 SER A CA  
1099 C C   . SER A 162 ? 0.6088 0.4995 0.4975 -0.0862 -0.0766 0.0678  162 SER A C   
1100 O O   . SER A 162 ? 0.5894 0.4768 0.4768 -0.0826 -0.0746 0.0711  162 SER A O   
1101 C CB  . SER A 162 ? 0.6793 0.5697 0.5636 -0.0903 -0.0843 0.0703  162 SER A CB  
1102 O OG  . SER A 162 ? 0.6649 0.5514 0.5394 -0.0944 -0.0826 0.0651  162 SER A OG  
1103 N N   . VAL A 163 ? 0.5598 0.4504 0.4450 -0.0891 -0.0747 0.0623  163 VAL A N   
1104 C CA  . VAL A 163 ? 0.5689 0.4559 0.4487 -0.0883 -0.0703 0.0600  163 VAL A CA  
1105 C C   . VAL A 163 ? 0.6135 0.4961 0.4820 -0.0930 -0.0695 0.0561  163 VAL A C   
1106 O O   . VAL A 163 ? 0.6038 0.4845 0.4676 -0.0939 -0.0660 0.0527  163 VAL A O   
1107 C CB  . VAL A 163 ? 0.5576 0.4485 0.4432 -0.0870 -0.0679 0.0570  163 VAL A CB  
1108 C CG1 . VAL A 163 ? 0.5722 0.4664 0.4681 -0.0823 -0.0680 0.0613  163 VAL A CG1 
1109 C CG2 . VAL A 163 ? 0.5156 0.4101 0.4018 -0.0905 -0.0694 0.0518  163 VAL A CG2 
1110 N N   . ASP A 164 ? 0.5965 0.4776 0.4605 -0.0959 -0.0726 0.0568  164 ASP A N   
1111 C CA  . ASP A 164 ? 0.5814 0.4586 0.4345 -0.1007 -0.0719 0.0532  164 ASP A CA  
1112 C C   . ASP A 164 ? 0.5946 0.4637 0.4382 -0.1008 -0.0712 0.0562  164 ASP A C   
1113 O O   . ASP A 164 ? 0.6022 0.4691 0.4473 -0.0975 -0.0730 0.0615  164 ASP A O   
1114 C CB  . ASP A 164 ? 0.6355 0.5149 0.4875 -0.1043 -0.0757 0.0516  164 ASP A CB  
1115 C CG  . ASP A 164 ? 0.6987 0.5844 0.5566 -0.1057 -0.0763 0.0472  164 ASP A CG  
1116 O OD1 . ASP A 164 ? 0.7098 0.5986 0.5736 -0.1034 -0.0740 0.0456  164 ASP A OD1 
1117 O OD2 . ASP A 164 ? 0.7467 0.6335 0.6025 -0.1089 -0.0792 0.0454  164 ASP A OD2 
1118 N N   . TYR A 165 ? 0.5559 0.4204 0.3894 -0.1046 -0.0684 0.0528  165 TYR A N   
1119 C CA  . TYR A 165 ? 0.5865 0.4420 0.4090 -0.1058 -0.0675 0.0550  165 TYR A CA  
1120 C C   . TYR A 165 ? 0.6431 0.4963 0.4555 -0.1122 -0.0663 0.0505  165 TYR A C   
1121 O O   . TYR A 165 ? 0.6420 0.4983 0.4541 -0.1148 -0.0634 0.0454  165 TYR A O   
1122 C CB  . TYR A 165 ? 0.5834 0.4344 0.4046 -0.1027 -0.0638 0.0563  165 TYR A CB  
1123 C CG  . TYR A 165 ? 0.6389 0.4794 0.4469 -0.1048 -0.0626 0.0577  165 TYR A CG  
1124 C CD1 . TYR A 165 ? 0.6714 0.5060 0.4760 -0.1021 -0.0651 0.0632  165 TYR A CD1 
1125 C CD2 . TYR A 165 ? 0.6152 0.4516 0.4140 -0.1097 -0.0590 0.0536  165 TYR A CD2 
1126 C CE1 . TYR A 165 ? 0.6856 0.5095 0.4772 -0.1040 -0.0642 0.0648  165 TYR A CE1 
1127 C CE2 . TYR A 165 ? 0.7169 0.5426 0.5028 -0.1122 -0.0579 0.0550  165 TYR A CE2 
1128 C CZ  . TYR A 165 ? 0.7466 0.5655 0.5286 -0.1091 -0.0605 0.0607  165 TYR A CZ  
1129 O OH  . TYR A 165 ? 0.7630 0.5705 0.5320 -0.1109 -0.0595 0.0625  165 TYR A OH  
1130 N N   . ASP A 166 ? 0.7230 0.5712 0.5274 -0.1145 -0.0687 0.0524  166 ASP A N   
1131 C CA  . ASP A 166 ? 0.7463 0.5911 0.5396 -0.1208 -0.0673 0.0487  166 ASP A CA  
1132 C C   . ASP A 166 ? 0.7398 0.5930 0.5372 -0.1240 -0.0669 0.0428  166 ASP A C   
1133 O O   . ASP A 166 ? 0.7512 0.6048 0.5434 -0.1282 -0.0635 0.0381  166 ASP A O   
1134 C CB  . ASP A 166 ? 0.7434 0.5804 0.5272 -0.1227 -0.0630 0.0482  166 ASP A CB  
1135 C CG  . ASP A 166 ? 0.9180 0.7501 0.6889 -0.1296 -0.0613 0.0452  166 ASP A CG  
1136 O OD1 . ASP A 166 ? 0.8533 0.6823 0.6183 -0.1313 -0.0641 0.0469  166 ASP A OD1 
1137 O OD2 . ASP A 166 ? 0.8954 0.7271 0.6623 -0.1333 -0.0571 0.0411  166 ASP A OD2 
1138 N N   . GLY A 167 ? 0.6824 0.5422 0.4887 -0.1221 -0.0703 0.0429  167 GLY A N   
1139 C CA  . GLY A 167 ? 0.7696 0.6364 0.5790 -0.1248 -0.0703 0.0373  167 GLY A CA  
1140 C C   . GLY A 167 ? 0.8166 0.6895 0.6331 -0.1235 -0.0671 0.0332  167 GLY A C   
1141 O O   . GLY A 167 ? 0.7901 0.6688 0.6092 -0.1252 -0.0668 0.0283  167 GLY A O   
1142 N N   . ASP A 168 ? 0.6913 0.5628 0.5106 -0.1203 -0.0647 0.0350  168 ASP A N   
1143 C CA  . ASP A 168 ? 0.6466 0.5238 0.4732 -0.1182 -0.0623 0.0317  168 ASP A CA  
1144 C C   . ASP A 168 ? 0.6164 0.4959 0.4536 -0.1124 -0.0639 0.0356  168 ASP A C   
1145 O O   . ASP A 168 ? 0.6072 0.4824 0.4444 -0.1096 -0.0649 0.0409  168 ASP A O   
1146 C CB  . ASP A 168 ? 0.6427 0.5165 0.4645 -0.1188 -0.0582 0.0308  168 ASP A CB  
1147 C CG  . ASP A 168 ? 0.6880 0.5593 0.4993 -0.1249 -0.0556 0.0270  168 ASP A CG  
1148 O OD1 . ASP A 168 ? 0.7779 0.6540 0.5884 -0.1282 -0.0557 0.0226  168 ASP A OD1 
1149 O OD2 . ASP A 168 ? 0.7046 0.5689 0.5083 -0.1263 -0.0535 0.0285  168 ASP A OD2 
1150 N N   . SER A 169 ? 0.5678 0.4539 0.4135 -0.1104 -0.0639 0.0329  169 SER A N   
1151 C CA  . SER A 169 ? 0.5304 0.4188 0.3859 -0.1052 -0.0649 0.0362  169 SER A CA  
1152 C C   . SER A 169 ? 0.5183 0.4063 0.3751 -0.1025 -0.0613 0.0358  169 SER A C   
1153 O O   . SER A 169 ? 0.5931 0.4841 0.4489 -0.1037 -0.0591 0.0309  169 SER A O   
1154 C CB  . SER A 169 ? 0.5103 0.4047 0.3734 -0.1046 -0.0670 0.0339  169 SER A CB  
1155 O OG  . SER A 169 ? 0.5790 0.4733 0.4403 -0.1073 -0.0705 0.0342  169 SER A OG  
1156 N N   . TYR A 170 ? 0.4796 0.3640 0.3379 -0.0988 -0.0609 0.0409  170 TYR A N   
1157 C CA  . TYR A 170 ? 0.5078 0.3910 0.3670 -0.0957 -0.0576 0.0411  170 TYR A CA  
1158 C C   . TYR A 170 ? 0.5027 0.3911 0.3720 -0.0916 -0.0579 0.0415  170 TYR A C   
1159 O O   . TYR A 170 ? 0.5097 0.3972 0.3837 -0.0873 -0.0574 0.0457  170 TYR A O   
1160 C CB  . TYR A 170 ? 0.4962 0.3725 0.3517 -0.0933 -0.0566 0.0461  170 TYR A CB  
1161 C CG  . TYR A 170 ? 0.5225 0.3926 0.3663 -0.0977 -0.0552 0.0445  170 TYR A CG  
1162 C CD1 . TYR A 170 ? 0.5276 0.3961 0.3659 -0.1018 -0.0573 0.0442  170 TYR A CD1 
1163 C CD2 . TYR A 170 ? 0.5836 0.4496 0.4214 -0.0983 -0.0517 0.0427  170 TYR A CD2 
1164 C CE1 . TYR A 170 ? 0.5832 0.4457 0.4102 -0.1063 -0.0557 0.0425  170 TYR A CE1 
1165 C CE2 . TYR A 170 ? 0.6157 0.4757 0.4426 -0.1029 -0.0502 0.0411  170 TYR A CE2 
1166 C CZ  . TYR A 170 ? 0.6267 0.4851 0.4482 -0.1071 -0.0521 0.0409  170 TYR A CZ  
1167 O OH  . TYR A 170 ? 0.6531 0.5049 0.4633 -0.1119 -0.0503 0.0396  170 TYR A OH  
1168 N N   . MET A 171 ? 0.4872 0.3807 0.3592 -0.0930 -0.0585 0.0369  171 MET A N   
1169 C CA  A MET A 171 ? 0.5041 0.4017 0.3846 -0.0893 -0.0586 0.0370  171 MET A CA  
1170 C CA  B MET A 171 ? 0.4942 0.3922 0.3749 -0.0898 -0.0591 0.0368  171 MET A CA  
1171 C C   . MET A 171 ? 0.4825 0.3840 0.3625 -0.0902 -0.0573 0.0308  171 MET A C   
1172 O O   . MET A 171 ? 0.4830 0.3862 0.3587 -0.0940 -0.0574 0.0263  171 MET A O   
1173 C CB  A MET A 171 ? 0.5032 0.4029 0.3905 -0.0887 -0.0620 0.0399  171 MET A CB  
1174 C CB  B MET A 171 ? 0.4759 0.3761 0.3604 -0.0913 -0.0629 0.0375  171 MET A CB  
1175 C CG  A MET A 171 ? 0.4455 0.3483 0.3327 -0.0918 -0.0642 0.0357  171 MET A CG  
1176 C CG  B MET A 171 ? 0.4953 0.3996 0.3871 -0.0897 -0.0642 0.0361  171 MET A CG  
1177 S SD  A MET A 171 ? 0.5206 0.4278 0.4114 -0.0903 -0.0631 0.0302  171 MET A SD  
1178 S SD  B MET A 171 ? 0.5281 0.4329 0.4282 -0.0841 -0.0629 0.0403  171 MET A SD  
1179 C CE  A MET A 171 ? 0.4557 0.3632 0.3556 -0.0852 -0.0632 0.0348  171 MET A CE  
1180 C CE  B MET A 171 ? 0.4689 0.3715 0.3721 -0.0823 -0.0639 0.0478  171 MET A CE  
1181 N N   . ASN A 172 ? 0.4479 0.3508 0.3320 -0.0863 -0.0556 0.0307  172 ASN A N   
1182 C CA  . ASN A 172 ? 0.4384 0.3452 0.3224 -0.0861 -0.0544 0.0251  172 ASN A CA  
1183 C C   . ASN A 172 ? 0.4184 0.3275 0.3097 -0.0820 -0.0553 0.0257  172 ASN A C   
1184 O O   . ASN A 172 ? 0.4505 0.3579 0.3466 -0.0793 -0.0558 0.0307  172 ASN A O   
1185 C CB  . ASN A 172 ? 0.3936 0.2992 0.2739 -0.0850 -0.0513 0.0237  172 ASN A CB  
1186 C CG  . ASN A 172 ? 0.4953 0.3970 0.3676 -0.0887 -0.0499 0.0236  172 ASN A CG  
1187 O OD1 . ASN A 172 ? 0.4523 0.3539 0.3208 -0.0930 -0.0508 0.0223  172 ASN A OD1 
1188 N ND2 . ASN A 172 ? 0.4907 0.3882 0.3597 -0.0874 -0.0476 0.0253  172 ASN A ND2 
1189 N N   . TRP A 173 ? 0.4349 0.3481 0.3272 -0.0818 -0.0554 0.0207  173 TRP A N   
1190 C CA  . TRP A 173 ? 0.4374 0.3519 0.3350 -0.0775 -0.0557 0.0207  173 TRP A CA  
1191 C C   . TRP A 173 ? 0.4481 0.3642 0.3441 -0.0750 -0.0535 0.0176  173 TRP A C   
1192 O O   . TRP A 173 ? 0.4522 0.3711 0.3441 -0.0772 -0.0524 0.0130  173 TRP A O   
1193 C CB  . TRP A 173 ? 0.4445 0.3618 0.3438 -0.0785 -0.0579 0.0170  173 TRP A CB  
1194 C CG  . TRP A 173 ? 0.4325 0.3482 0.3337 -0.0808 -0.0606 0.0196  173 TRP A CG  
1195 C CD1 . TRP A 173 ? 0.4521 0.3680 0.3497 -0.0852 -0.0621 0.0183  173 TRP A CD1 
1196 C CD2 . TRP A 173 ? 0.4110 0.3251 0.3181 -0.0790 -0.0624 0.0235  173 TRP A CD2 
1197 N NE1 . TRP A 173 ? 0.4586 0.3731 0.3598 -0.0859 -0.0649 0.0212  173 TRP A NE1 
1198 C CE2 . TRP A 173 ? 0.4700 0.3836 0.3772 -0.0824 -0.0652 0.0244  173 TRP A CE2 
1199 C CE3 . TRP A 173 ? 0.4744 0.3873 0.3866 -0.0750 -0.0619 0.0265  173 TRP A CE3 
1200 C CZ2 . TRP A 173 ? 0.4781 0.3904 0.3906 -0.0823 -0.0676 0.0279  173 TRP A CZ2 
1201 C CZ3 . TRP A 173 ? 0.5107 0.4222 0.4281 -0.0749 -0.0639 0.0302  173 TRP A CZ3 
1202 C CH2 . TRP A 173 ? 0.4629 0.3744 0.3807 -0.0786 -0.0668 0.0308  173 TRP A CH2 
1203 N N   . TYR A 174 ? 0.4315 0.3464 0.3312 -0.0704 -0.0529 0.0201  174 TYR A N   
1204 C CA  . TYR A 174 ? 0.4577 0.3737 0.3562 -0.0672 -0.0512 0.0179  174 TYR A CA  
1205 C C   . TYR A 174 ? 0.4465 0.3638 0.3490 -0.0635 -0.0524 0.0167  174 TYR A C   
1206 O O   . TYR A 174 ? 0.4439 0.3592 0.3506 -0.0627 -0.0538 0.0199  174 TYR A O   
1207 C CB  . TYR A 174 ? 0.4191 0.3309 0.3171 -0.0646 -0.0491 0.0225  174 TYR A CB  
1208 C CG  . TYR A 174 ? 0.4589 0.3685 0.3517 -0.0678 -0.0478 0.0232  174 TYR A CG  
1209 C CD1 . TYR A 174 ? 0.4300 0.3408 0.3174 -0.0696 -0.0463 0.0190  174 TYR A CD1 
1210 C CD2 . TYR A 174 ? 0.4490 0.3556 0.3421 -0.0697 -0.0484 0.0275  174 TYR A CD2 
1211 C CE1 . TYR A 174 ? 0.4611 0.3687 0.3428 -0.0730 -0.0450 0.0195  174 TYR A CE1 
1212 C CE2 . TYR A 174 ? 0.4837 0.3871 0.3711 -0.0724 -0.0472 0.0282  174 TYR A CE2 
1213 C CZ  . TYR A 174 ? 0.4648 0.3684 0.3463 -0.0744 -0.0456 0.0241  174 TYR A CZ  
1214 O OH  . TYR A 174 ? 0.5040 0.4036 0.3794 -0.0777 -0.0446 0.0249  174 TYR A OH  
1215 N N   . GLN A 175 ? 0.4194 0.3401 0.3205 -0.0616 -0.0520 0.0119  175 GLN A N   
1216 C CA  . GLN A 175 ? 0.4201 0.3411 0.3238 -0.0573 -0.0530 0.0108  175 GLN A CA  
1217 C C   . GLN A 175 ? 0.4230 0.3429 0.3256 -0.0530 -0.0513 0.0116  175 GLN A C   
1218 O O   . GLN A 175 ? 0.4919 0.4141 0.3910 -0.0535 -0.0500 0.0090  175 GLN A O   
1219 C CB  . GLN A 175 ? 0.4534 0.3800 0.3561 -0.0581 -0.0541 0.0040  175 GLN A CB  
1220 C CG  . GLN A 175 ? 0.4598 0.3870 0.3641 -0.0533 -0.0553 0.0018  175 GLN A CG  
1221 C CD  . GLN A 175 ? 0.5236 0.4574 0.4268 -0.0535 -0.0561 -0.0052 175 GLN A CD  
1222 O OE1 . GLN A 175 ? 0.5119 0.4510 0.4129 -0.0548 -0.0550 -0.0091 175 GLN A OE1 
1223 N NE2 . GLN A 175 ? 0.4585 0.3923 0.3632 -0.0524 -0.0580 -0.0073 175 GLN A NE2 
1224 N N   . GLN A 176 ? 0.4077 0.3241 0.3128 -0.0491 -0.0515 0.0149  176 GLN A N   
1225 C CA  . GLN A 176 ? 0.4112 0.3266 0.3145 -0.0445 -0.0502 0.0149  176 GLN A CA  
1226 C C   . GLN A 176 ? 0.4859 0.4013 0.3904 -0.0404 -0.0517 0.0130  176 GLN A C   
1227 O O   . GLN A 176 ? 0.4714 0.3826 0.3785 -0.0387 -0.0522 0.0166  176 GLN A O   
1228 C CB  . GLN A 176 ? 0.4339 0.3440 0.3379 -0.0426 -0.0483 0.0213  176 GLN A CB  
1229 C CG  . GLN A 176 ? 0.4702 0.3791 0.3713 -0.0380 -0.0469 0.0209  176 GLN A CG  
1230 C CD  . GLN A 176 ? 0.5285 0.4327 0.4289 -0.0362 -0.0444 0.0265  176 GLN A CD  
1231 O OE1 . GLN A 176 ? 0.5008 0.4023 0.4046 -0.0370 -0.0437 0.0315  176 GLN A OE1 
1232 N NE2 . GLN A 176 ? 0.4999 0.4035 0.3958 -0.0341 -0.0429 0.0254  176 GLN A NE2 
1233 N N   . LYS A 177 ? 0.4848 0.4049 0.3872 -0.0387 -0.0525 0.0073  177 LYS A N   
1234 C CA  . LYS A 177 ? 0.4864 0.4062 0.3890 -0.0341 -0.0540 0.0051  177 LYS A CA  
1235 C C   . LYS A 177 ? 0.5107 0.4260 0.4118 -0.0291 -0.0529 0.0085  177 LYS A C   
1236 O O   . LYS A 177 ? 0.5192 0.4334 0.4183 -0.0292 -0.0510 0.0107  177 LYS A O   
1237 C CB  . LYS A 177 ? 0.5256 0.4529 0.4269 -0.0334 -0.0552 -0.0020 177 LYS A CB  
1238 C CG  . LYS A 177 ? 0.5207 0.4524 0.4233 -0.0377 -0.0562 -0.0057 177 LYS A CG  
1239 C CD  . LYS A 177 ? 0.5520 0.4921 0.4537 -0.0371 -0.0570 -0.0129 177 LYS A CD  
1240 C CE  . LYS A 177 ? 0.6673 0.6123 0.5697 -0.0415 -0.0575 -0.0168 177 LYS A CE  
1241 N NZ  . LYS A 177 ? 0.6761 0.6303 0.5781 -0.0407 -0.0578 -0.0236 177 LYS A NZ  
1242 N N   . PRO A 178 ? 0.5394 0.4511 0.4406 -0.0247 -0.0540 0.0092  178 PRO A N   
1243 C CA  . PRO A 178 ? 0.5395 0.4459 0.4386 -0.0201 -0.0528 0.0128  178 PRO A CA  
1244 C C   . PRO A 178 ? 0.5406 0.4505 0.4358 -0.0176 -0.0524 0.0098  178 PRO A C   
1245 O O   . PRO A 178 ? 0.5158 0.4320 0.4101 -0.0170 -0.0539 0.0039  178 PRO A O   
1246 C CB  . PRO A 178 ? 0.5753 0.4781 0.4746 -0.0163 -0.0547 0.0123  178 PRO A CB  
1247 C CG  . PRO A 178 ? 0.6165 0.5198 0.5193 -0.0205 -0.0561 0.0116  178 PRO A CG  
1248 C CD  . PRO A 178 ? 0.5808 0.4921 0.4836 -0.0242 -0.0563 0.0069  178 PRO A CD  
1249 N N   . GLY A 179 ? 0.5554 0.4618 0.4486 -0.0170 -0.0500 0.0138  179 GLY A N   
1250 C CA  . GLY A 179 ? 0.5776 0.4857 0.4664 -0.0147 -0.0493 0.0119  179 GLY A CA  
1251 C C   . GLY A 179 ? 0.5977 0.5118 0.4856 -0.0191 -0.0490 0.0080  179 GLY A C   
1252 O O   . GLY A 179 ? 0.5635 0.4791 0.4476 -0.0179 -0.0486 0.0060  179 GLY A O   
1253 N N   . GLN A 180 ? 0.5429 0.4599 0.4337 -0.0243 -0.0492 0.0070  180 GLN A N   
1254 C CA  A GLN A 180 ? 0.5378 0.4601 0.4272 -0.0288 -0.0489 0.0032  180 GLN A CA  
1255 C CA  B GLN A 180 ? 0.5382 0.4605 0.4276 -0.0289 -0.0489 0.0032  180 GLN A CA  
1256 C C   . GLN A 180 ? 0.5365 0.4548 0.4256 -0.0327 -0.0467 0.0076  180 GLN A C   
1257 O O   . GLN A 180 ? 0.5259 0.4392 0.4174 -0.0325 -0.0459 0.0129  180 GLN A O   
1258 C CB  A GLN A 180 ? 0.5820 0.5110 0.4739 -0.0321 -0.0506 -0.0017 180 GLN A CB  
1259 C CB  B GLN A 180 ? 0.5505 0.4796 0.4426 -0.0313 -0.0509 -0.0019 180 GLN A CB  
1260 C CG  A GLN A 180 ? 0.6710 0.6061 0.5631 -0.0287 -0.0528 -0.0075 180 GLN A CG  
1261 C CG  B GLN A 180 ? 0.5698 0.5018 0.4627 -0.0265 -0.0531 -0.0055 180 GLN A CG  
1262 C CD  A GLN A 180 ? 0.7078 0.6475 0.5968 -0.0269 -0.0529 -0.0112 180 GLN A CD  
1263 C CD  B GLN A 180 ? 0.5845 0.5247 0.4792 -0.0283 -0.0548 -0.0118 180 GLN A CD  
1264 O OE1 A GLN A 180 ? 0.7914 0.7304 0.6791 -0.0214 -0.0540 -0.0116 180 GLN A OE1 
1265 O OE1 B GLN A 180 ? 0.6240 0.5690 0.5188 -0.0335 -0.0541 -0.0144 180 GLN A OE1 
1266 N NE2 A GLN A 180 ? 0.7502 0.6944 0.6377 -0.0316 -0.0520 -0.0141 180 GLN A NE2 
1267 N NE2 B GLN A 180 ? 0.5543 0.4959 0.4501 -0.0239 -0.0568 -0.0143 180 GLN A NE2 
1268 N N   . PRO A 181 ? 0.5497 0.4697 0.4358 -0.0365 -0.0456 0.0058  181 PRO A N   
1269 C CA  . PRO A 181 ? 0.5331 0.4487 0.4186 -0.0399 -0.0437 0.0100  181 PRO A CA  
1270 C C   . PRO A 181 ? 0.4876 0.4046 0.3766 -0.0440 -0.0448 0.0103  181 PRO A C   
1271 O O   . PRO A 181 ? 0.5167 0.4390 0.4074 -0.0453 -0.0465 0.0060  181 PRO A O   
1272 C CB  . PRO A 181 ? 0.5431 0.4597 0.4234 -0.0430 -0.0425 0.0071  181 PRO A CB  
1273 C CG  . PRO A 181 ? 0.5710 0.4932 0.4496 -0.0410 -0.0438 0.0014  181 PRO A CG  
1274 C CD  . PRO A 181 ? 0.5667 0.4926 0.4498 -0.0378 -0.0461 -0.0001 181 PRO A CD  
1275 N N   . PRO A 182 ? 0.4838 0.3967 0.3737 -0.0461 -0.0438 0.0150  182 PRO A N   
1276 C CA  . PRO A 182 ? 0.4711 0.3856 0.3633 -0.0505 -0.0450 0.0149  182 PRO A CA  
1277 C C   . PRO A 182 ? 0.4682 0.3870 0.3569 -0.0551 -0.0450 0.0097  182 PRO A C   
1278 O O   . PRO A 182 ? 0.4512 0.3701 0.3355 -0.0558 -0.0437 0.0077  182 PRO A O   
1279 C CB  . PRO A 182 ? 0.4752 0.3842 0.3680 -0.0512 -0.0437 0.0211  182 PRO A CB  
1280 C CG  . PRO A 182 ? 0.5073 0.4123 0.3998 -0.0462 -0.0419 0.0248  182 PRO A CG  
1281 C CD  . PRO A 182 ? 0.5176 0.4245 0.4060 -0.0445 -0.0415 0.0203  182 PRO A CD  
1282 N N   . ARG A 183 ? 0.4232 0.3453 0.3134 -0.0586 -0.0464 0.0074  183 ARG A N   
1283 C CA  . ARG A 183 ? 0.4683 0.3941 0.3550 -0.0637 -0.0461 0.0030  183 ARG A CA  
1284 C C   . ARG A 183 ? 0.4550 0.3801 0.3424 -0.0678 -0.0469 0.0042  183 ARG A C   
1285 O O   . ARG A 183 ? 0.4202 0.3444 0.3116 -0.0664 -0.0485 0.0064  183 ARG A O   
1286 C CB  . ARG A 183 ? 0.4954 0.4291 0.3827 -0.0634 -0.0470 -0.0036 183 ARG A CB  
1287 C CG  . ARG A 183 ? 0.5173 0.4539 0.4089 -0.0617 -0.0491 -0.0052 183 ARG A CG  
1288 C CD  . ARG A 183 ? 0.5188 0.4637 0.4110 -0.0606 -0.0498 -0.0121 183 ARG A CD  
1289 N NE  . ARG A 183 ? 0.5051 0.4522 0.4005 -0.0591 -0.0517 -0.0141 183 ARG A NE  
1290 C CZ  . ARG A 183 ? 0.4808 0.4354 0.3770 -0.0592 -0.0525 -0.0202 183 ARG A CZ  
1291 N NH1 . ARG A 183 ? 0.4992 0.4608 0.3938 -0.0614 -0.0515 -0.0249 183 ARG A NH1 
1292 N NH2 . ARG A 183 ? 0.5023 0.4576 0.4008 -0.0573 -0.0542 -0.0217 183 ARG A NH2 
1293 N N   . LEU A 184 ? 0.4593 0.3848 0.3425 -0.0730 -0.0460 0.0026  184 LEU A N   
1294 C CA  . LEU A 184 ? 0.4468 0.3718 0.3298 -0.0769 -0.0470 0.0033  184 LEU A CA  
1295 C C   . LEU A 184 ? 0.4429 0.3740 0.3285 -0.0774 -0.0487 -0.0012 184 LEU A C   
1296 O O   . LEU A 184 ? 0.4465 0.3837 0.3317 -0.0775 -0.0483 -0.0068 184 LEU A O   
1297 C CB  . LEU A 184 ? 0.4542 0.3782 0.3309 -0.0823 -0.0454 0.0019  184 LEU A CB  
1298 C CG  . LEU A 184 ? 0.4447 0.3680 0.3192 -0.0871 -0.0461 0.0021  184 LEU A CG  
1299 C CD1 . LEU A 184 ? 0.4560 0.3732 0.3318 -0.0863 -0.0474 0.0085  184 LEU A CD1 
1300 C CD2 . LEU A 184 ? 0.4461 0.3688 0.3136 -0.0926 -0.0441 -0.0002 184 LEU A CD2 
1301 N N   . LEU A 185 ? 0.4054 0.3348 0.2933 -0.0780 -0.0505 0.0009  185 LEU A N   
1302 C CA  . LEU A 185 ? 0.4198 0.3534 0.3097 -0.0782 -0.0521 -0.0030 185 LEU A CA  
1303 C C   . LEU A 185 ? 0.4105 0.3445 0.2970 -0.0837 -0.0524 -0.0041 185 LEU A C   
1304 O O   . LEU A 185 ? 0.4671 0.4065 0.3521 -0.0860 -0.0521 -0.0095 185 LEU A O   
1305 C CB  . LEU A 185 ? 0.4475 0.3780 0.3423 -0.0746 -0.0541 0.0003  185 LEU A CB  
1306 C CG  . LEU A 185 ? 0.4800 0.4135 0.3767 -0.0739 -0.0560 -0.0035 185 LEU A CG  
1307 C CD1 . LEU A 185 ? 0.4474 0.3856 0.3452 -0.0697 -0.0557 -0.0082 185 LEU A CD1 
1308 C CD2 . LEU A 185 ? 0.4571 0.3858 0.3578 -0.0721 -0.0583 0.0006  185 LEU A CD2 
1309 N N   . ILE A 186 ? 0.4252 0.3537 0.3109 -0.0855 -0.0531 0.0009  186 ILE A N   
1310 C CA  . ILE A 186 ? 0.4212 0.3488 0.3031 -0.0905 -0.0538 0.0006  186 ILE A CA  
1311 C C   . ILE A 186 ? 0.4430 0.3650 0.3210 -0.0926 -0.0529 0.0053  186 ILE A C   
1312 O O   . ILE A 186 ? 0.4536 0.3715 0.3342 -0.0897 -0.0532 0.0105  186 ILE A O   
1313 C CB  . ILE A 186 ? 0.4794 0.4059 0.3644 -0.0902 -0.0567 0.0020  186 ILE A CB  
1314 C CG1 . ILE A 186 ? 0.5034 0.4348 0.3905 -0.0887 -0.0575 -0.0034 186 ILE A CG1 
1315 C CG2 . ILE A 186 ? 0.4589 0.3830 0.3399 -0.0949 -0.0578 0.0033  186 ILE A CG2 
1316 C CD1 . ILE A 186 ? 0.5695 0.4989 0.4596 -0.0879 -0.0603 -0.0023 186 ILE A CD1 
1317 N N   . TYR A 187 ? 0.4569 0.3783 0.3285 -0.0976 -0.0517 0.0037  187 TYR A N   
1318 C CA  . TYR A 187 ? 0.4596 0.3744 0.3269 -0.0990 -0.0510 0.0085  187 TYR A CA  
1319 C C   . TYR A 187 ? 0.4641 0.3762 0.3278 -0.1028 -0.0527 0.0101  187 TYR A C   
1320 O O   . TYR A 187 ? 0.4833 0.3988 0.3455 -0.1057 -0.0534 0.0063  187 TYR A O   
1321 C CB  . TYR A 187 ? 0.4812 0.3949 0.3426 -0.1014 -0.0480 0.0066  187 TYR A CB  
1322 C CG  . TYR A 187 ? 0.5002 0.4183 0.3569 -0.1068 -0.0467 0.0008  187 TYR A CG  
1323 C CD1 . TYR A 187 ? 0.5346 0.4607 0.3940 -0.1064 -0.0459 -0.0050 187 TYR A CD1 
1324 C CD2 . TYR A 187 ? 0.5284 0.4426 0.3776 -0.1120 -0.0460 0.0013  187 TYR A CD2 
1325 C CE1 . TYR A 187 ? 0.6005 0.5316 0.4562 -0.1112 -0.0443 -0.0103 187 TYR A CE1 
1326 C CE2 . TYR A 187 ? 0.5347 0.4530 0.3794 -0.1172 -0.0443 -0.0038 187 TYR A CE2 
1327 C CZ  . TYR A 187 ? 0.6118 0.5390 0.4601 -0.1169 -0.0433 -0.0097 187 TYR A CZ  
1328 O OH  . TYR A 187 ? 0.5989 0.5318 0.4439 -0.1218 -0.0415 -0.0152 187 TYR A OH  
1329 N N   . ALA A 188 ? 0.4723 0.3783 0.3346 -0.1022 -0.0534 0.0158  188 ALA A N   
1330 C CA  . ALA A 188 ? 0.4916 0.3942 0.3497 -0.1055 -0.0553 0.0180  188 ALA A CA  
1331 C C   . ALA A 188 ? 0.5417 0.4478 0.4035 -0.1059 -0.0582 0.0166  188 ALA A C   
1332 O O   . ALA A 188 ? 0.5024 0.4089 0.3594 -0.1099 -0.0590 0.0142  188 ALA A O   
1333 C CB  . ALA A 188 ? 0.5108 0.4108 0.3594 -0.1108 -0.0533 0.0159  188 ALA A CB  
1334 N N   . ALA A 189 ? 0.5049 0.4129 0.3746 -0.1019 -0.0598 0.0181  189 ALA A N   
1335 C CA  . ALA A 189 ? 0.5131 0.4232 0.3871 -0.1017 -0.0629 0.0176  189 ALA A CA  
1336 C C   . ALA A 189 ? 0.4696 0.3845 0.3434 -0.1027 -0.0626 0.0111  189 ALA A C   
1337 O O   . ALA A 189 ? 0.5019 0.4189 0.3811 -0.1001 -0.0640 0.0101  189 ALA A O   
1338 C CB  . ALA A 189 ? 0.4980 0.4050 0.3699 -0.1041 -0.0659 0.0211  189 ALA A CB  
1339 N N   . SER A 190 ? 0.5026 0.4194 0.3703 -0.1062 -0.0607 0.0067  190 SER A N   
1340 C CA  . SER A 190 ? 0.4569 0.3784 0.3242 -0.1073 -0.0608 0.0007  190 SER A CA  
1341 C C   . SER A 190 ? 0.5140 0.4408 0.3790 -0.1084 -0.0575 -0.0048 190 SER A C   
1342 O O   . SER A 190 ? 0.5667 0.4982 0.4315 -0.1090 -0.0573 -0.0101 190 SER A O   
1343 C CB  . SER A 190 ? 0.5234 0.4434 0.3859 -0.1114 -0.0627 0.0002  190 SER A CB  
1344 O OG  . SER A 190 ? 0.5310 0.4488 0.3859 -0.1155 -0.0608 0.0005  190 SER A OG  
1345 N N   . ASN A 191 ? 0.5124 0.4387 0.3762 -0.1082 -0.0550 -0.0041 191 ASN A N   
1346 C CA  . ASN A 191 ? 0.4841 0.4160 0.3456 -0.1100 -0.0520 -0.0096 191 ASN A CA  
1347 C C   . ASN A 191 ? 0.4907 0.4270 0.3582 -0.1052 -0.0515 -0.0116 191 ASN A C   
1348 O O   . ASN A 191 ? 0.5142 0.4471 0.3840 -0.1021 -0.0515 -0.0077 191 ASN A O   
1349 C CB  . ASN A 191 ? 0.4821 0.4104 0.3370 -0.1140 -0.0497 -0.0081 191 ASN A CB  
1350 C CG  . ASN A 191 ? 0.5735 0.4970 0.4216 -0.1186 -0.0503 -0.0061 191 ASN A CG  
1351 O OD1 . ASN A 191 ? 0.6351 0.5615 0.4791 -0.1226 -0.0496 -0.0101 191 ASN A OD1 
1352 N ND2 . ASN A 191 ? 0.5844 0.5006 0.4313 -0.1179 -0.0519 0.0000  191 ASN A ND2 
1353 N N   . LEU A 192 ? 0.5018 0.4454 0.3711 -0.1044 -0.0509 -0.0176 192 LEU A N   
1354 C CA  . LEU A 192 ? 0.5423 0.4901 0.4167 -0.0996 -0.0506 -0.0196 192 LEU A CA  
1355 C C   . LEU A 192 ? 0.5561 0.5053 0.4281 -0.1011 -0.0480 -0.0203 192 LEU A C   
1356 O O   . LEU A 192 ? 0.5223 0.4743 0.3898 -0.1060 -0.0459 -0.0234 192 LEU A O   
1357 C CB  . LEU A 192 ? 0.5678 0.5233 0.4451 -0.0974 -0.0508 -0.0258 192 LEU A CB  
1358 C CG  . LEU A 192 ? 0.6985 0.6530 0.5775 -0.0958 -0.0532 -0.0264 192 LEU A CG  
1359 C CD1 . LEU A 192 ? 0.6711 0.6324 0.5535 -0.0920 -0.0534 -0.0321 192 LEU A CD1 
1360 C CD2 . LEU A 192 ? 0.7595 0.7065 0.6414 -0.0929 -0.0556 -0.0202 192 LEU A CD2 
1361 N N   . GLU A 193 ? 0.4851 0.4324 0.3599 -0.0969 -0.0480 -0.0179 193 GLU A N   
1362 C CA  . GLU A 193 ? 0.5163 0.4655 0.3890 -0.0979 -0.0458 -0.0195 193 GLU A CA  
1363 C C   . GLU A 193 ? 0.5218 0.4813 0.3963 -0.0980 -0.0450 -0.0267 193 GLU A C   
1364 O O   . GLU A 193 ? 0.5067 0.4706 0.3853 -0.0947 -0.0464 -0.0294 193 GLU A O   
1365 C CB  . GLU A 193 ? 0.4837 0.4280 0.3590 -0.0928 -0.0463 -0.0150 193 GLU A CB  
1366 C CG  . GLU A 193 ? 0.5131 0.4597 0.3876 -0.0917 -0.0447 -0.0170 193 GLU A CG  
1367 C CD  . GLU A 193 ? 0.6278 0.5720 0.4960 -0.0968 -0.0423 -0.0171 193 GLU A CD  
1368 O OE1 . GLU A 193 ? 0.6289 0.5739 0.4931 -0.1024 -0.0414 -0.0189 193 GLU A OE1 
1369 O OE2 . GLU A 193 ? 0.6389 0.5801 0.5056 -0.0954 -0.0414 -0.0157 193 GLU A OE2 
1370 N N   . SER A 194 ? 0.5323 0.4956 0.4039 -0.1015 -0.0427 -0.0298 194 SER A N   
1371 C CA  . SER A 194 ? 0.5889 0.5631 0.4627 -0.1017 -0.0419 -0.0366 194 SER A CA  
1372 C C   . SER A 194 ? 0.5615 0.5392 0.4412 -0.0944 -0.0437 -0.0377 194 SER A C   
1373 O O   . SER A 194 ? 0.5388 0.5114 0.4195 -0.0904 -0.0445 -0.0340 194 SER A O   
1374 C CB  . SER A 194 ? 0.6167 0.5931 0.4871 -0.1059 -0.0395 -0.0386 194 SER A CB  
1375 O OG  . SER A 194 ? 0.7795 0.7510 0.6435 -0.1126 -0.0378 -0.0370 194 SER A OG  
1376 N N   . GLY A 195 ? 0.5733 0.5598 0.4565 -0.0926 -0.0443 -0.0431 195 GLY A N   
1377 C CA  . GLY A 195 ? 0.5829 0.5733 0.4711 -0.0856 -0.0460 -0.0448 195 GLY A CA  
1378 C C   . GLY A 195 ? 0.6188 0.6029 0.5094 -0.0805 -0.0484 -0.0414 195 GLY A C   
1379 O O   . GLY A 195 ? 0.6292 0.6152 0.5233 -0.0745 -0.0500 -0.0425 195 GLY A O   
1380 N N   . ILE A 196 ? 0.5711 0.5474 0.4597 -0.0829 -0.0488 -0.0369 196 ILE A N   
1381 C CA  . ILE A 196 ? 0.5318 0.5022 0.4228 -0.0789 -0.0511 -0.0337 196 ILE A CA  
1382 C C   . ILE A 196 ? 0.5978 0.5727 0.4895 -0.0789 -0.0519 -0.0382 196 ILE A C   
1383 O O   . ILE A 196 ? 0.5746 0.5522 0.4635 -0.0840 -0.0507 -0.0406 196 ILE A O   
1384 C CB  . ILE A 196 ? 0.4824 0.4432 0.3716 -0.0811 -0.0515 -0.0268 196 ILE A CB  
1385 C CG1 . ILE A 196 ? 0.5086 0.4647 0.3969 -0.0801 -0.0505 -0.0223 196 ILE A CG1 
1386 C CG2 . ILE A 196 ? 0.4992 0.4548 0.3909 -0.0784 -0.0539 -0.0240 196 ILE A CG2 
1387 C CD1 . ILE A 196 ? 0.5268 0.4830 0.4184 -0.0739 -0.0512 -0.0218 196 ILE A CD1 
1388 N N   . PRO A 197 ? 0.5769 0.5520 0.4718 -0.0733 -0.0538 -0.0396 197 PRO A N   
1389 C CA  . PRO A 197 ? 0.5426 0.5212 0.4378 -0.0728 -0.0545 -0.0440 197 PRO A CA  
1390 C C   . PRO A 197 ? 0.6025 0.5752 0.4953 -0.0763 -0.0555 -0.0418 197 PRO A C   
1391 O O   . PRO A 197 ? 0.5690 0.5335 0.4615 -0.0771 -0.0565 -0.0360 197 PRO A O   
1392 C CB  . PRO A 197 ? 0.5748 0.5531 0.4733 -0.0653 -0.0565 -0.0453 197 PRO A CB  
1393 C CG  . PRO A 197 ? 0.6019 0.5739 0.5015 -0.0624 -0.0571 -0.0397 197 PRO A CG  
1394 C CD  . PRO A 197 ? 0.5403 0.5127 0.4380 -0.0670 -0.0550 -0.0375 197 PRO A CD  
1395 N N   . ALA A 198 ? 0.5707 0.5479 0.4621 -0.0777 -0.0552 -0.0468 198 ALA A N   
1396 C CA  . ALA A 198 ? 0.5956 0.5686 0.4837 -0.0815 -0.0559 -0.0460 198 ALA A CA  
1397 C C   . ALA A 198 ? 0.5923 0.5568 0.4818 -0.0786 -0.0589 -0.0426 198 ALA A C   
1398 O O   . ALA A 198 ? 0.5775 0.5369 0.4644 -0.0819 -0.0601 -0.0404 198 ALA A O   
1399 C CB  . ALA A 198 ? 0.6798 0.6602 0.5661 -0.0832 -0.0546 -0.0526 198 ALA A CB  
1400 N N   . ARG A 199 ? 0.5574 0.5198 0.4503 -0.0726 -0.0602 -0.0417 199 ARG A N   
1401 C CA  . ARG A 199 ? 0.5557 0.5094 0.4496 -0.0705 -0.0629 -0.0382 199 ARG A CA  
1402 C C   . ARG A 199 ? 0.5382 0.4849 0.4326 -0.0731 -0.0636 -0.0309 199 ARG A C   
1403 O O   . ARG A 199 ? 0.5386 0.4785 0.4337 -0.0730 -0.0658 -0.0277 199 ARG A O   
1404 C CB  . ARG A 199 ? 0.5063 0.4586 0.4028 -0.0635 -0.0642 -0.0393 199 ARG A CB  
1405 C CG  . ARG A 199 ? 0.5206 0.4754 0.4194 -0.0607 -0.0630 -0.0377 199 ARG A CG  
1406 C CD  . ARG A 199 ? 0.5807 0.5338 0.4812 -0.0537 -0.0644 -0.0391 199 ARG A CD  
1407 N NE  . ARG A 199 ? 0.5753 0.5282 0.4776 -0.0502 -0.0638 -0.0365 199 ARG A NE  
1408 C CZ  . ARG A 199 ? 0.5884 0.5490 0.4913 -0.0484 -0.0626 -0.0397 199 ARG A CZ  
1409 N NH1 . ARG A 199 ? 0.5705 0.5402 0.4731 -0.0495 -0.0616 -0.0458 199 ARG A NH1 
1410 N NH2 . ARG A 199 ? 0.5976 0.5570 0.5015 -0.0456 -0.0623 -0.0369 199 ARG A NH2 
1411 N N   . PHE A 200 ? 0.4959 0.4441 0.3899 -0.0755 -0.0619 -0.0283 200 PHE A N   
1412 C CA  . PHE A 200 ? 0.4795 0.4215 0.3738 -0.0779 -0.0624 -0.0216 200 PHE A CA  
1413 C C   . PHE A 200 ? 0.5080 0.4495 0.3984 -0.0839 -0.0624 -0.0211 200 PHE A C   
1414 O O   . PHE A 200 ? 0.5406 0.4871 0.4276 -0.0869 -0.0605 -0.0250 200 PHE A O   
1415 C CB  . PHE A 200 ? 0.4532 0.3961 0.3482 -0.0772 -0.0605 -0.0190 200 PHE A CB  
1416 C CG  . PHE A 200 ? 0.5154 0.4575 0.4138 -0.0713 -0.0606 -0.0182 200 PHE A CG  
1417 C CD1 . PHE A 200 ? 0.5441 0.4921 0.4430 -0.0679 -0.0599 -0.0233 200 PHE A CD1 
1418 C CD2 . PHE A 200 ? 0.5116 0.4475 0.4128 -0.0692 -0.0615 -0.0123 200 PHE A CD2 
1419 C CE1 . PHE A 200 ? 0.5169 0.4638 0.4181 -0.0623 -0.0602 -0.0224 200 PHE A CE1 
1420 C CE2 . PHE A 200 ? 0.4779 0.4124 0.3813 -0.0639 -0.0615 -0.0114 200 PHE A CE2 
1421 C CZ  . PHE A 200 ? 0.4966 0.4362 0.3997 -0.0604 -0.0609 -0.0164 200 PHE A CZ  
1422 N N   . SER A 201 ? 0.5148 0.4503 0.4054 -0.0858 -0.0643 -0.0161 201 SER A N   
1423 C CA  . SER A 201 ? 0.5060 0.4403 0.3925 -0.0912 -0.0644 -0.0147 201 SER A CA  
1424 C C   . SER A 201 ? 0.5440 0.4726 0.4323 -0.0920 -0.0660 -0.0076 201 SER A C   
1425 O O   . SER A 201 ? 0.5213 0.4468 0.4142 -0.0890 -0.0674 -0.0043 201 SER A O   
1426 C CB  . SER A 201 ? 0.5316 0.4661 0.4148 -0.0937 -0.0659 -0.0184 201 SER A CB  
1427 O OG  . SER A 201 ? 0.6190 0.5488 0.5051 -0.0918 -0.0689 -0.0164 201 SER A OG  
1428 N N   . GLY A 202 ? 0.4691 0.3965 0.3536 -0.0959 -0.0655 -0.0053 202 GLY A N   
1429 C CA  . GLY A 202 ? 0.4645 0.3872 0.3508 -0.0963 -0.0669 0.0013  202 GLY A CA  
1430 C C   . GLY A 202 ? 0.4975 0.4180 0.3792 -0.1008 -0.0688 0.0023  202 GLY A C   
1431 O O   . GLY A 202 ? 0.4803 0.4027 0.3564 -0.1040 -0.0676 -0.0014 202 GLY A O   
1432 N N   . SER A 203 ? 0.4646 0.3816 0.3491 -0.1011 -0.0716 0.0074  203 SER A N   
1433 C CA  . SER A 203 ? 0.5095 0.4242 0.3897 -0.1050 -0.0739 0.0088  203 SER A CA  
1434 C C   . SER A 203 ? 0.5325 0.4444 0.4159 -0.1044 -0.0754 0.0158  203 SER A C   
1435 O O   . SER A 203 ? 0.4887 0.4005 0.3780 -0.1009 -0.0747 0.0192  203 SER A O   
1436 C CB  . SER A 203 ? 0.5467 0.4611 0.4269 -0.1062 -0.0768 0.0060  203 SER A CB  
1437 O OG  . SER A 203 ? 0.5329 0.4457 0.4200 -0.1040 -0.0794 0.0092  203 SER A OG  
1438 N N   . GLY A 204 ? 0.4998 0.4095 0.3794 -0.1075 -0.0776 0.0180  204 GLY A N   
1439 C CA  . GLY A 204 ? 0.5170 0.4247 0.4000 -0.1067 -0.0797 0.0246  204 GLY A CA  
1440 C C   . GLY A 204 ? 0.5236 0.4286 0.4003 -0.1084 -0.0789 0.0272  204 GLY A C   
1441 O O   . GLY A 204 ? 0.5301 0.4344 0.3997 -0.1103 -0.0763 0.0242  204 GLY A O   
1442 N N   . SER A 205 ? 0.5312 0.4346 0.4101 -0.1079 -0.0815 0.0328  205 SER A N   
1443 C CA  . SER A 205 ? 0.6084 0.5083 0.4818 -0.1085 -0.0810 0.0362  205 SER A CA  
1444 C C   . SER A 205 ? 0.5639 0.4639 0.4438 -0.1059 -0.0836 0.0426  205 SER A C   
1445 O O   . SER A 205 ? 0.5722 0.4751 0.4598 -0.1050 -0.0861 0.0437  205 SER A O   
1446 C CB  . SER A 205 ? 0.6096 0.5070 0.4737 -0.1129 -0.0828 0.0344  205 SER A CB  
1447 O OG  . SER A 205 ? 0.6355 0.5341 0.5028 -0.1140 -0.0874 0.0355  205 SER A OG  
1448 N N   . GLY A 206 ? 0.5857 0.4826 0.4626 -0.1047 -0.0830 0.0466  206 GLY A N   
1449 C CA  . GLY A 206 ? 0.6002 0.4976 0.4828 -0.1021 -0.0856 0.0527  206 GLY A CA  
1450 C C   . GLY A 206 ? 0.5835 0.4842 0.4763 -0.0978 -0.0839 0.0551  206 GLY A C   
1451 O O   . GLY A 206 ? 0.5699 0.4689 0.4620 -0.0951 -0.0803 0.0560  206 GLY A O   
1452 N N   . THR A 207 ? 0.5597 0.4646 0.4612 -0.0975 -0.0866 0.0563  207 THR A N   
1453 C CA  . THR A 207 ? 0.5244 0.4324 0.4356 -0.0939 -0.0851 0.0588  207 THR A CA  
1454 C C   . THR A 207 ? 0.5397 0.4496 0.4546 -0.0946 -0.0846 0.0548  207 THR A C   
1455 O O   . THR A 207 ? 0.6007 0.5127 0.5231 -0.0919 -0.0834 0.0568  207 THR A O   
1456 C CB  . THR A 207 ? 0.5929 0.5044 0.5125 -0.0926 -0.0883 0.0644  207 THR A CB  
1457 O OG1 . THR A 207 ? 0.5945 0.5077 0.5147 -0.0964 -0.0929 0.0630  207 THR A OG1 
1458 C CG2 . THR A 207 ? 0.5755 0.4856 0.4929 -0.0906 -0.0888 0.0690  207 THR A CG2 
1459 N N   . ASP A 208 ? 0.5049 0.4140 0.4149 -0.0979 -0.0857 0.0496  208 ASP A N   
1460 C CA  . ASP A 208 ? 0.5133 0.4237 0.4265 -0.0984 -0.0860 0.0460  208 ASP A CA  
1461 C C   . ASP A 208 ? 0.5127 0.4220 0.4196 -0.0990 -0.0832 0.0399  208 ASP A C   
1462 O O   . ASP A 208 ? 0.5071 0.4151 0.4062 -0.1019 -0.0835 0.0367  208 ASP A O   
1463 C CB  . ASP A 208 ? 0.5515 0.4626 0.4659 -0.1018 -0.0906 0.0453  208 ASP A CB  
1464 C CG  . ASP A 208 ? 0.5701 0.4836 0.4922 -0.1017 -0.0938 0.0509  208 ASP A CG  
1465 O OD1 . ASP A 208 ? 0.6917 0.6071 0.6219 -0.0998 -0.0933 0.0532  208 ASP A OD1 
1466 O OD2 . ASP A 208 ? 0.7153 0.6289 0.6352 -0.1034 -0.0968 0.0530  208 ASP A OD2 
1467 N N   . PHE A 209 ? 0.4524 0.3624 0.3625 -0.0961 -0.0805 0.0384  209 PHE A N   
1468 C CA  . PHE A 209 ? 0.4404 0.3504 0.3454 -0.0959 -0.0777 0.0328  209 PHE A CA  
1469 C C   . PHE A 209 ? 0.4847 0.3956 0.3939 -0.0941 -0.0777 0.0301  209 PHE A C   
1470 O O   . PHE A 209 ? 0.4880 0.3988 0.4039 -0.0922 -0.0785 0.0334  209 PHE A O   
1471 C CB  . PHE A 209 ? 0.4591 0.3687 0.3626 -0.0933 -0.0738 0.0339  209 PHE A CB  
1472 C CG  . PHE A 209 ? 0.4444 0.3519 0.3430 -0.0949 -0.0737 0.0366  209 PHE A CG  
1473 C CD1 . PHE A 209 ? 0.4506 0.3570 0.3406 -0.0982 -0.0730 0.0330  209 PHE A CD1 
1474 C CD2 . PHE A 209 ? 0.4765 0.3831 0.3787 -0.0932 -0.0746 0.0427  209 PHE A CD2 
1475 C CE1 . PHE A 209 ? 0.4840 0.3872 0.3684 -0.0998 -0.0731 0.0357  209 PHE A CE1 
1476 C CE2 . PHE A 209 ? 0.4875 0.3914 0.3844 -0.0944 -0.0750 0.0453  209 PHE A CE2 
1477 C CZ  . PHE A 209 ? 0.4794 0.3812 0.3671 -0.0978 -0.0743 0.0418  209 PHE A CZ  
1478 N N   . THR A 210 ? 0.4752 0.3868 0.3801 -0.0947 -0.0768 0.0240  210 THR A N   
1479 C CA  . THR A 210 ? 0.4756 0.3873 0.3832 -0.0927 -0.0770 0.0210  210 THR A CA  
1480 C C   . THR A 210 ? 0.5104 0.4241 0.4149 -0.0907 -0.0740 0.0159  210 THR A C   
1481 O O   . THR A 210 ? 0.4822 0.3976 0.3810 -0.0929 -0.0730 0.0122  210 THR A O   
1482 C CB  . THR A 210 ? 0.5154 0.4260 0.4212 -0.0956 -0.0802 0.0180  210 THR A CB  
1483 O OG1 . THR A 210 ? 0.4761 0.3856 0.3848 -0.0978 -0.0833 0.0227  210 THR A OG1 
1484 C CG2 . THR A 210 ? 0.5193 0.4285 0.4279 -0.0934 -0.0809 0.0155  210 THR A CG2 
1485 N N   . LEU A 211 ? 0.4440 0.3577 0.3519 -0.0867 -0.0725 0.0157  211 LEU A N   
1486 C CA  . LEU A 211 ? 0.4288 0.3449 0.3344 -0.0844 -0.0704 0.0104  211 LEU A CA  
1487 C C   . LEU A 211 ? 0.4426 0.3580 0.3487 -0.0833 -0.0721 0.0065  211 LEU A C   
1488 O O   . LEU A 211 ? 0.4495 0.3616 0.3594 -0.0820 -0.0738 0.0089  211 LEU A O   
1489 C CB  . LEU A 211 ? 0.4015 0.3177 0.3099 -0.0803 -0.0680 0.0128  211 LEU A CB  
1490 C CG  . LEU A 211 ? 0.4734 0.3923 0.3802 -0.0772 -0.0662 0.0078  211 LEU A CG  
1491 C CD1 . LEU A 211 ? 0.4785 0.4017 0.3804 -0.0794 -0.0643 0.0034  211 LEU A CD1 
1492 C CD2 . LEU A 211 ? 0.4636 0.3813 0.3733 -0.0730 -0.0643 0.0112  211 LEU A CD2 
1493 N N   . ASN A 212 ? 0.4626 0.3810 0.3646 -0.0835 -0.0714 0.0003  212 ASN A N   
1494 C CA  . ASN A 212 ? 0.4841 0.4019 0.3857 -0.0817 -0.0726 -0.0042 212 ASN A CA  
1495 C C   . ASN A 212 ? 0.5227 0.4446 0.4235 -0.0779 -0.0704 -0.0088 212 ASN A C   
1496 O O   . ASN A 212 ? 0.5035 0.4302 0.4021 -0.0788 -0.0682 -0.0110 212 ASN A O   
1497 C CB  . ASN A 212 ? 0.4175 0.3353 0.3148 -0.0855 -0.0743 -0.0077 212 ASN A CB  
1498 C CG  . ASN A 212 ? 0.4918 0.4044 0.3908 -0.0874 -0.0777 -0.0045 212 ASN A CG  
1499 O OD1 . ASN A 212 ? 0.5087 0.4179 0.4091 -0.0853 -0.0792 -0.0055 212 ASN A OD1 
1500 N ND2 . ASN A 212 ? 0.4619 0.3736 0.3605 -0.0914 -0.0791 -0.0007 212 ASN A ND2 
1501 N N   . ILE A 213 ? 0.5083 0.4281 0.4108 -0.0736 -0.0711 -0.0103 213 ILE A N   
1502 C CA  . ILE A 213 ? 0.4948 0.4186 0.3968 -0.0693 -0.0697 -0.0150 213 ILE A CA  
1503 C C   . ILE A 213 ? 0.5028 0.4242 0.4035 -0.0671 -0.0715 -0.0192 213 ILE A C   
1504 O O   . ILE A 213 ? 0.4645 0.3793 0.3667 -0.0658 -0.0733 -0.0166 213 ILE A O   
1505 C CB  . ILE A 213 ? 0.4688 0.3910 0.3738 -0.0649 -0.0686 -0.0117 213 ILE A CB  
1506 C CG1 . ILE A 213 ? 0.4726 0.3940 0.3793 -0.0667 -0.0674 -0.0059 213 ILE A CG1 
1507 C CG2 . ILE A 213 ? 0.5230 0.4502 0.4272 -0.0604 -0.0673 -0.0166 213 ILE A CG2 
1508 C CD1 . ILE A 213 ? 0.5099 0.4287 0.4193 -0.0624 -0.0665 -0.0023 213 ILE A CD1 
1509 N N   . HIS A 214 ? 0.5106 0.4373 0.4085 -0.0669 -0.0708 -0.0256 214 HIS A N   
1510 C CA  . HIS A 214 ? 0.5690 0.4935 0.4650 -0.0643 -0.0723 -0.0302 214 HIS A CA  
1511 C C   . HIS A 214 ? 0.5884 0.5213 0.4825 -0.0626 -0.0705 -0.0372 214 HIS A C   
1512 O O   . HIS A 214 ? 0.5869 0.5256 0.4793 -0.0665 -0.0689 -0.0390 214 HIS A O   
1513 C CB  . HIS A 214 ? 0.5402 0.4602 0.4337 -0.0686 -0.0744 -0.0300 214 HIS A CB  
1514 C CG  . HIS A 214 ? 0.6431 0.5607 0.5337 -0.0660 -0.0757 -0.0354 214 HIS A CG  
1515 N ND1 . HIS A 214 ? 0.6168 0.5397 0.5039 -0.0665 -0.0748 -0.0417 214 HIS A ND1 
1516 C CD2 . HIS A 214 ? 0.6484 0.5586 0.5389 -0.0626 -0.0777 -0.0354 214 HIS A CD2 
1517 C CE1 . HIS A 214 ? 0.6481 0.5671 0.5331 -0.0630 -0.0761 -0.0455 214 HIS A CE1 
1518 N NE2 . HIS A 214 ? 0.6511 0.5618 0.5378 -0.0608 -0.0781 -0.0417 214 HIS A NE2 
1519 N N   . PRO A 215 ? 0.6337 0.5676 0.5280 -0.0566 -0.0707 -0.0413 215 PRO A N   
1520 C CA  . PRO A 215 ? 0.5897 0.5162 0.4853 -0.0515 -0.0724 -0.0391 215 PRO A CA  
1521 C C   . PRO A 215 ? 0.5798 0.5071 0.4785 -0.0486 -0.0714 -0.0354 215 PRO A C   
1522 O O   . PRO A 215 ? 0.6143 0.5496 0.5137 -0.0473 -0.0696 -0.0378 215 PRO A O   
1523 C CB  . PRO A 215 ? 0.5936 0.5220 0.4873 -0.0460 -0.0728 -0.0458 215 PRO A CB  
1524 C CG  . PRO A 215 ? 0.7092 0.6457 0.6008 -0.0493 -0.0714 -0.0513 215 PRO A CG  
1525 C CD  . PRO A 215 ? 0.6447 0.5871 0.5376 -0.0545 -0.0694 -0.0486 215 PRO A CD  
1526 N N   . VAL A 216 ? 0.5414 0.4606 0.4415 -0.0477 -0.0724 -0.0297 216 VAL A N   
1527 C CA  . VAL A 216 ? 0.5518 0.4710 0.4543 -0.0450 -0.0713 -0.0259 216 VAL A CA  
1528 C C   . VAL A 216 ? 0.5802 0.5022 0.4820 -0.0381 -0.0711 -0.0301 216 VAL A C   
1529 O O   . VAL A 216 ? 0.5633 0.4822 0.4632 -0.0344 -0.0726 -0.0334 216 VAL A O   
1530 C CB  . VAL A 216 ? 0.5898 0.4993 0.4937 -0.0453 -0.0724 -0.0195 216 VAL A CB  
1531 C CG1 . VAL A 216 ? 0.6652 0.5727 0.5704 -0.0407 -0.0715 -0.0163 216 VAL A CG1 
1532 C CG2 . VAL A 216 ? 0.5781 0.4870 0.4838 -0.0515 -0.0723 -0.0148 216 VAL A CG2 
1533 N N   . GLU A 217 ? 0.5592 0.4866 0.4621 -0.0363 -0.0696 -0.0298 217 GLU A N   
1534 C CA  . GLU A 217 ? 0.5813 0.5114 0.4839 -0.0296 -0.0697 -0.0327 217 GLU A CA  
1535 C C   . GLU A 217 ? 0.5983 0.5238 0.5016 -0.0272 -0.0692 -0.0273 217 GLU A C   
1536 O O   . GLU A 217 ? 0.5251 0.4480 0.4297 -0.0310 -0.0682 -0.0220 217 GLU A O   
1537 C CB  . GLU A 217 ? 0.6346 0.5766 0.5378 -0.0305 -0.0681 -0.0374 217 GLU A CB  
1538 C CG  . GLU A 217 ? 0.6725 0.6206 0.5749 -0.0323 -0.0681 -0.0435 217 GLU A CG  
1539 C CD  . GLU A 217 ? 0.7299 0.6906 0.6332 -0.0324 -0.0666 -0.0491 217 GLU A CD  
1540 O OE1 . GLU A 217 ? 0.8625 0.8281 0.7671 -0.0305 -0.0658 -0.0492 217 GLU A OE1 
1541 O OE2 . GLU A 217 ? 0.7531 0.7189 0.6557 -0.0348 -0.0661 -0.0536 217 GLU A OE2 
1542 N N   . GLU A 218 ? 0.5904 0.5157 0.4928 -0.0205 -0.0698 -0.0287 218 GLU A N   
1543 C CA  A GLU A 218 ? 0.6377 0.5581 0.5397 -0.0174 -0.0693 -0.0239 218 GLU A CA  
1544 C CA  B GLU A 218 ? 0.6520 0.5720 0.5541 -0.0177 -0.0693 -0.0236 218 GLU A CA  
1545 C C   . GLU A 218 ? 0.5979 0.5231 0.5013 -0.0208 -0.0672 -0.0215 218 GLU A C   
1546 O O   . GLU A 218 ? 0.6118 0.5316 0.5155 -0.0214 -0.0662 -0.0157 218 GLU A O   
1547 C CB  A GLU A 218 ? 0.6317 0.5534 0.5319 -0.0097 -0.0703 -0.0270 218 GLU A CB  
1548 C CB  B GLU A 218 ? 0.6944 0.6111 0.5942 -0.0098 -0.0706 -0.0250 218 GLU A CB  
1549 C CG  A GLU A 218 ? 0.7144 0.6333 0.6127 -0.0056 -0.0723 -0.0311 218 GLU A CG  
1550 C CG  B GLU A 218 ? 0.8216 0.7306 0.7203 -0.0073 -0.0700 -0.0189 218 GLU A CG  
1551 C CD  A GLU A 218 ? 0.7592 0.6784 0.6553 0.0026  -0.0737 -0.0337 218 GLU A CD  
1552 C CD  B GLU A 218 ? 0.8786 0.7777 0.7741 -0.0015 -0.0715 -0.0175 218 GLU A CD  
1553 O OE1 A GLU A 218 ? 0.7404 0.6614 0.6363 0.0049  -0.0731 -0.0319 218 GLU A OE1 
1554 O OE1 B GLU A 218 ? 0.8340 0.7233 0.7291 -0.0028 -0.0713 -0.0120 218 GLU A OE1 
1555 O OE2 A GLU A 218 ? 0.7508 0.6682 0.6452 0.0068  -0.0753 -0.0376 218 GLU A OE2 
1556 O OE2 B GLU A 218 ? 0.8911 0.7926 0.7845 0.0045  -0.0729 -0.0220 218 GLU A OE2 
1557 N N   . GLU A 219 ? 0.6048 0.5400 0.5088 -0.0229 -0.0664 -0.0260 219 GLU A N   
1558 C CA  A GLU A 219 ? 0.5751 0.5143 0.4795 -0.0262 -0.0644 -0.0242 219 GLU A CA  
1559 C CA  B GLU A 219 ? 0.5965 0.5362 0.5009 -0.0264 -0.0644 -0.0246 219 GLU A CA  
1560 C C   . GLU A 219 ? 0.5678 0.5026 0.4730 -0.0322 -0.0634 -0.0190 219 GLU A C   
1561 O O   . GLU A 219 ? 0.5653 0.5003 0.4704 -0.0343 -0.0617 -0.0160 219 GLU A O   
1562 C CB  A GLU A 219 ? 0.6243 0.5748 0.5288 -0.0281 -0.0636 -0.0301 219 GLU A CB  
1563 C CB  B GLU A 219 ? 0.6776 0.6288 0.5821 -0.0278 -0.0637 -0.0307 219 GLU A CB  
1564 C CG  A GLU A 219 ? 0.6192 0.5757 0.5233 -0.0233 -0.0638 -0.0333 219 GLU A CG  
1565 C CG  B GLU A 219 ? 0.7180 0.6751 0.6230 -0.0321 -0.0635 -0.0353 219 GLU A CG  
1566 C CD  A GLU A 219 ? 0.6423 0.5980 0.5452 -0.0228 -0.0627 -0.0302 219 GLU A CD  
1567 C CD  B GLU A 219 ? 0.7789 0.7483 0.6844 -0.0335 -0.0626 -0.0418 219 GLU A CD  
1568 O OE1 A GLU A 219 ? 0.6943 0.6466 0.5961 -0.0170 -0.0636 -0.0289 219 GLU A OE1 
1569 O OE1 B GLU A 219 ? 0.6525 0.6264 0.5577 -0.0397 -0.0609 -0.0428 219 GLU A OE1 
1570 O OE2 A GLU A 219 ? 0.5880 0.5462 0.4907 -0.0279 -0.0609 -0.0293 219 GLU A OE2 
1571 O OE2 B GLU A 219 ? 0.8307 0.8055 0.7369 -0.0283 -0.0637 -0.0463 219 GLU A OE2 
1572 N N   . ASP A 220 ? 0.5761 0.5063 0.4820 -0.0347 -0.0644 -0.0177 220 ASP A N   
1573 C CA  . ASP A 220 ? 0.4995 0.4266 0.4064 -0.0403 -0.0637 -0.0131 220 ASP A CA  
1574 C C   . ASP A 220 ? 0.4978 0.4172 0.4061 -0.0394 -0.0634 -0.0061 220 ASP A C   
1575 O O   . ASP A 220 ? 0.4935 0.4106 0.4033 -0.0433 -0.0628 -0.0015 220 ASP A O   
1576 C CB  . ASP A 220 ? 0.4864 0.4129 0.3932 -0.0439 -0.0651 -0.0150 220 ASP A CB  
1577 C CG  . ASP A 220 ? 0.5936 0.5285 0.4990 -0.0453 -0.0649 -0.0217 220 ASP A CG  
1578 O OD1 . ASP A 220 ? 0.5990 0.5405 0.5039 -0.0458 -0.0632 -0.0238 220 ASP A OD1 
1579 O OD2 . ASP A 220 ? 0.6017 0.5367 0.5063 -0.0459 -0.0661 -0.0251 220 ASP A OD2 
1580 N N   . ALA A 221 ? 0.5215 0.4366 0.4293 -0.0340 -0.0637 -0.0049 221 ALA A N   
1581 C CA  . ALA A 221 ? 0.5046 0.4127 0.4136 -0.0331 -0.0629 0.0016  221 ALA A CA  
1582 C C   . ALA A 221 ? 0.5369 0.4470 0.4461 -0.0343 -0.0606 0.0048  221 ALA A C   
1583 O O   . ALA A 221 ? 0.5520 0.4662 0.4593 -0.0320 -0.0597 0.0024  221 ALA A O   
1584 C CB  . ALA A 221 ? 0.5602 0.4630 0.4675 -0.0271 -0.0635 0.0021  221 ALA A CB  
1585 N N   . ALA A 222 ? 0.4859 0.3933 0.3974 -0.0377 -0.0597 0.0101  222 ALA A N   
1586 C CA  . ALA A 222 ? 0.4718 0.3812 0.3832 -0.0394 -0.0575 0.0126  222 ALA A CA  
1587 C C   . ALA A 222 ? 0.4892 0.3949 0.4038 -0.0423 -0.0570 0.0188  222 ALA A C   
1588 O O   . ALA A 222 ? 0.4923 0.3953 0.4094 -0.0440 -0.0587 0.0202  222 ALA A O   
1589 C CB  . ALA A 222 ? 0.4666 0.3825 0.3761 -0.0430 -0.0575 0.0080  222 ALA A CB  
1590 N N   . THR A 223 ? 0.4748 0.3807 0.3895 -0.0431 -0.0550 0.0222  223 THR A N   
1591 C CA  . THR A 223 ? 0.4826 0.3868 0.4006 -0.0461 -0.0546 0.0275  223 THR A CA  
1592 C C   . THR A 223 ? 0.4434 0.3512 0.3599 -0.0504 -0.0547 0.0258  223 THR A C   
1593 O O   . THR A 223 ? 0.4402 0.3505 0.3531 -0.0503 -0.0535 0.0230  223 THR A O   
1594 C CB  . THR A 223 ? 0.5121 0.4136 0.4310 -0.0435 -0.0519 0.0328  223 THR A CB  
1595 O OG1 . THR A 223 ? 0.5344 0.4321 0.4541 -0.0400 -0.0518 0.0344  223 THR A OG1 
1596 C CG2 . THR A 223 ? 0.4590 0.3599 0.3817 -0.0463 -0.0515 0.0382  223 THR A CG2 
1597 N N   . TYR A 224 ? 0.4282 0.3360 0.3471 -0.0543 -0.0564 0.0271  224 TYR A N   
1598 C CA  . TYR A 224 ? 0.4203 0.3306 0.3373 -0.0586 -0.0569 0.0258  224 TYR A CA  
1599 C C   . TYR A 224 ? 0.4134 0.3221 0.3327 -0.0599 -0.0562 0.0318  224 TYR A C   
1600 O O   . TYR A 224 ? 0.4232 0.3302 0.3472 -0.0599 -0.0570 0.0360  224 TYR A O   
1601 C CB  . TYR A 224 ? 0.4425 0.3540 0.3596 -0.0617 -0.0596 0.0225  224 TYR A CB  
1602 C CG  . TYR A 224 ? 0.4190 0.3327 0.3336 -0.0599 -0.0601 0.0163  224 TYR A CG  
1603 C CD1 . TYR A 224 ? 0.4354 0.3536 0.3462 -0.0615 -0.0595 0.0111  224 TYR A CD1 
1604 C CD2 . TYR A 224 ? 0.4304 0.3419 0.3465 -0.0562 -0.0609 0.0156  224 TYR A CD2 
1605 C CE1 . TYR A 224 ? 0.4505 0.3720 0.3597 -0.0595 -0.0599 0.0053  224 TYR A CE1 
1606 C CE2 . TYR A 224 ? 0.4425 0.3563 0.3563 -0.0539 -0.0614 0.0099  224 TYR A CE2 
1607 C CZ  . TYR A 224 ? 0.4675 0.3868 0.3782 -0.0555 -0.0609 0.0046  224 TYR A CZ  
1608 O OH  . TYR A 224 ? 0.4523 0.3752 0.3613 -0.0530 -0.0614 -0.0011 224 TYR A OH  
1609 N N   . TYR A 225 ? 0.4155 0.3248 0.3314 -0.0614 -0.0548 0.0319  225 TYR A N   
1610 C CA  . TYR A 225 ? 0.4180 0.3257 0.3353 -0.0622 -0.0541 0.0372  225 TYR A CA  
1611 C C   . TYR A 225 ? 0.4391 0.3477 0.3529 -0.0666 -0.0553 0.0358  225 TYR A C   
1612 O O   . TYR A 225 ? 0.4483 0.3582 0.3571 -0.0683 -0.0547 0.0312  225 TYR A O   
1613 C CB  . TYR A 225 ? 0.4444 0.3501 0.3596 -0.0593 -0.0511 0.0395  225 TYR A CB  
1614 C CG  . TYR A 225 ? 0.4437 0.3480 0.3612 -0.0546 -0.0494 0.0414  225 TYR A CG  
1615 C CD1 . TYR A 225 ? 0.4215 0.3244 0.3445 -0.0527 -0.0488 0.0471  225 TYR A CD1 
1616 C CD2 . TYR A 225 ? 0.4644 0.3690 0.3785 -0.0522 -0.0484 0.0375  225 TYR A CD2 
1617 C CE1 . TYR A 225 ? 0.4276 0.3287 0.3518 -0.0486 -0.0468 0.0490  225 TYR A CE1 
1618 C CE2 . TYR A 225 ? 0.4522 0.3548 0.3673 -0.0478 -0.0468 0.0394  225 TYR A CE2 
1619 C CZ  . TYR A 225 ? 0.4515 0.3520 0.3713 -0.0461 -0.0459 0.0452  225 TYR A CZ  
1620 O OH  . TYR A 225 ? 0.4640 0.3621 0.3836 -0.0419 -0.0441 0.0468  225 TYR A OH  
1621 N N   . CYS A 226 ? 0.4517 0.3596 0.3681 -0.0685 -0.0568 0.0398  226 CYS A N   
1622 C CA  . CYS A 226 ? 0.4455 0.3531 0.3578 -0.0722 -0.0576 0.0394  226 CYS A CA  
1623 C C   . CYS A 226 ? 0.4564 0.3613 0.3669 -0.0704 -0.0554 0.0434  226 CYS A C   
1624 O O   . CYS A 226 ? 0.4412 0.3451 0.3553 -0.0667 -0.0537 0.0472  226 CYS A O   
1625 C CB  . CYS A 226 ? 0.4549 0.3633 0.3704 -0.0749 -0.0610 0.0411  226 CYS A CB  
1626 S SG  . CYS A 226 ? 0.5239 0.4324 0.4483 -0.0727 -0.0618 0.0481  226 CYS A SG  
1627 N N   . GLN A 227 ? 0.4551 0.3583 0.3596 -0.0730 -0.0551 0.0426  227 GLN A N   
1628 C CA  . GLN A 227 ? 0.4423 0.3418 0.3439 -0.0715 -0.0531 0.0460  227 GLN A CA  
1629 C C   . GLN A 227 ? 0.4611 0.3585 0.3580 -0.0751 -0.0546 0.0468  227 GLN A C   
1630 O O   . GLN A 227 ? 0.4821 0.3804 0.3749 -0.0791 -0.0557 0.0428  227 GLN A O   
1631 C CB  . GLN A 227 ? 0.4321 0.3301 0.3275 -0.0712 -0.0503 0.0422  227 GLN A CB  
1632 C CG  . GLN A 227 ? 0.4663 0.3593 0.3571 -0.0698 -0.0480 0.0451  227 GLN A CG  
1633 C CD  . GLN A 227 ? 0.5497 0.4395 0.4318 -0.0740 -0.0476 0.0425  227 GLN A CD  
1634 O OE1 . GLN A 227 ? 0.5568 0.4423 0.4333 -0.0733 -0.0452 0.0426  227 GLN A OE1 
1635 N NE2 . GLN A 227 ? 0.5309 0.4219 0.4108 -0.0784 -0.0497 0.0406  227 GLN A NE2 
1636 N N   . GLN A 228 ? 0.4620 0.3566 0.3592 -0.0734 -0.0545 0.0520  228 GLN A N   
1637 C CA  . GLN A 228 ? 0.4548 0.3459 0.3457 -0.0763 -0.0555 0.0528  228 GLN A CA  
1638 C C   . GLN A 228 ? 0.4885 0.3739 0.3726 -0.0749 -0.0526 0.0538  228 GLN A C   
1639 O O   . GLN A 228 ? 0.4518 0.3356 0.3378 -0.0707 -0.0504 0.0564  228 GLN A O   
1640 C CB  . GLN A 228 ? 0.4651 0.3571 0.3604 -0.0760 -0.0585 0.0576  228 GLN A CB  
1641 C CG  . GLN A 228 ? 0.4917 0.3835 0.3926 -0.0710 -0.0575 0.0635  228 GLN A CG  
1642 C CD  . GLN A 228 ? 0.4948 0.3806 0.3894 -0.0693 -0.0560 0.0663  228 GLN A CD  
1643 O OE1 . GLN A 228 ? 0.5281 0.4099 0.4149 -0.0722 -0.0568 0.0652  228 GLN A OE1 
1644 N NE2 . GLN A 228 ? 0.4958 0.3802 0.3928 -0.0644 -0.0536 0.0699  228 GLN A NE2 
1645 N N   . ASN A 229 ? 0.4738 0.3551 0.3493 -0.0786 -0.0526 0.0521  229 ASN A N   
1646 C CA  . ASN A 229 ? 0.4844 0.3588 0.3522 -0.0778 -0.0500 0.0531  229 ASN A CA  
1647 C C   . ASN A 229 ? 0.5040 0.3732 0.3652 -0.0802 -0.0515 0.0553  229 ASN A C   
1648 O O   . ASN A 229 ? 0.5186 0.3814 0.3705 -0.0821 -0.0498 0.0544  229 ASN A O   
1649 C CB  . ASN A 229 ? 0.5118 0.3850 0.3740 -0.0795 -0.0471 0.0481  229 ASN A CB  
1650 C CG  . ASN A 229 ? 0.5661 0.4412 0.4234 -0.0854 -0.0476 0.0427  229 ASN A CG  
1651 O OD1 . ASN A 229 ? 0.5729 0.4542 0.4348 -0.0868 -0.0493 0.0399  229 ASN A OD1 
1652 N ND2 . ASN A 229 ? 0.5824 0.4522 0.4301 -0.0891 -0.0460 0.0408  229 ASN A ND2 
1653 N N   . ASN A 230 ? 0.4908 0.3627 0.3568 -0.0799 -0.0548 0.0584  230 ASN A N   
1654 C CA  . ASN A 230 ? 0.5686 0.4357 0.4285 -0.0815 -0.0568 0.0610  230 ASN A CA  
1655 C C   . ASN A 230 ? 0.5971 0.4591 0.4564 -0.0766 -0.0559 0.0665  230 ASN A C   
1656 O O   . ASN A 230 ? 0.6180 0.4724 0.4683 -0.0772 -0.0555 0.0679  230 ASN A O   
1657 C CB  . ASN A 230 ? 0.5520 0.4240 0.4171 -0.0829 -0.0610 0.0623  230 ASN A CB  
1658 C CG  . ASN A 230 ? 0.6100 0.4769 0.4672 -0.0855 -0.0632 0.0639  230 ASN A CG  
1659 O OD1 . ASN A 230 ? 0.5926 0.4537 0.4394 -0.0888 -0.0617 0.0616  230 ASN A OD1 
1660 N ND2 . ASN A 230 ? 0.6047 0.4739 0.4666 -0.0839 -0.0668 0.0680  230 ASN A ND2 
1661 N N   . GLU A 231 ? 0.5976 0.4635 0.4661 -0.0716 -0.0555 0.0698  231 GLU A N   
1662 C CA  . GLU A 231 ? 0.6732 0.5353 0.5421 -0.0662 -0.0545 0.0749  231 GLU A CA  
1663 C C   . GLU A 231 ? 0.6913 0.5535 0.5631 -0.0622 -0.0507 0.0748  231 GLU A C   
1664 O O   . GLU A 231 ? 0.5959 0.4632 0.4727 -0.0628 -0.0499 0.0721  231 GLU A O   
1665 C CB  . GLU A 231 ? 0.6349 0.5031 0.5136 -0.0635 -0.0577 0.0797  231 GLU A CB  
1666 C CG  . GLU A 231 ? 0.8231 0.6906 0.6985 -0.0665 -0.0618 0.0807  231 GLU A CG  
1667 C CD  . GLU A 231 ? 0.9461 0.8197 0.8307 -0.0642 -0.0656 0.0853  231 GLU A CD  
1668 O OE1 . GLU A 231 ? 0.8824 0.7603 0.7759 -0.0595 -0.0646 0.0888  231 GLU A OE1 
1669 O OE2 . GLU A 231 ? 1.0583 0.9329 0.9413 -0.0674 -0.0695 0.0853  231 GLU A OE2 
1670 N N   . ASP A 232 ? 0.6821 0.5381 0.5501 -0.0578 -0.0484 0.0779  232 ASP A N   
1671 C CA  . ASP A 232 ? 0.6280 0.4840 0.4991 -0.0531 -0.0448 0.0788  232 ASP A CA  
1672 C C   . ASP A 232 ? 0.6044 0.4670 0.4870 -0.0482 -0.0454 0.0836  232 ASP A C   
1673 O O   . ASP A 232 ? 0.6673 0.5318 0.5533 -0.0470 -0.0479 0.0874  232 ASP A O   
1674 C CB  . ASP A 232 ? 0.7042 0.5501 0.5655 -0.0506 -0.0419 0.0797  232 ASP A CB  
1675 C CG  . ASP A 232 ? 0.8431 0.6823 0.6929 -0.0556 -0.0407 0.0747  232 ASP A CG  
1676 O OD1 . ASP A 232 ? 0.8117 0.6536 0.6619 -0.0578 -0.0393 0.0704  232 ASP A OD1 
1677 O OD2 . ASP A 232 ? 1.0096 0.8413 0.8503 -0.0577 -0.0412 0.0751  232 ASP A OD2 
1678 N N   . PRO A 233 ? 0.5552 0.4221 0.4444 -0.0456 -0.0432 0.0836  233 PRO A N   
1679 C CA  . PRO A 233 ? 0.5228 0.3887 0.4088 -0.0472 -0.0409 0.0788  233 PRO A CA  
1680 C C   . PRO A 233 ? 0.5212 0.3924 0.4096 -0.0524 -0.0434 0.0746  233 PRO A C   
1681 O O   . PRO A 233 ? 0.5057 0.3830 0.4017 -0.0535 -0.0462 0.0760  233 PRO A O   
1682 C CB  . PRO A 233 ? 0.5210 0.3905 0.4147 -0.0420 -0.0383 0.0815  233 PRO A CB  
1683 C CG  . PRO A 233 ? 0.5290 0.4057 0.4335 -0.0407 -0.0407 0.0859  233 PRO A CG  
1684 C CD  . PRO A 233 ? 0.5619 0.4351 0.4622 -0.0410 -0.0429 0.0882  233 PRO A CD  
1685 N N   . ARG A 234 ? 0.5536 0.4231 0.4363 -0.0553 -0.0422 0.0694  234 ARG A N   
1686 C CA  A ARG A 234 ? 0.5057 0.3809 0.3917 -0.0587 -0.0437 0.0652  234 ARG A CA  
1687 C CA  B ARG A 234 ? 0.5101 0.3853 0.3961 -0.0587 -0.0437 0.0652  234 ARG A CA  
1688 C C   . ARG A 234 ? 0.4708 0.3521 0.3673 -0.0558 -0.0440 0.0675  234 ARG A C   
1689 O O   . ARG A 234 ? 0.4897 0.3705 0.3892 -0.0512 -0.0415 0.0703  234 ARG A O   
1690 C CB  A ARG A 234 ? 0.5324 0.4059 0.4124 -0.0604 -0.0417 0.0598  234 ARG A CB  
1691 C CB  B ARG A 234 ? 0.5373 0.4110 0.4180 -0.0597 -0.0414 0.0601  234 ARG A CB  
1692 C CG  A ARG A 234 ? 0.5796 0.4469 0.4488 -0.0640 -0.0409 0.0572  234 ARG A CG  
1693 C CG  B ARG A 234 ? 0.6162 0.4855 0.4871 -0.0643 -0.0412 0.0563  234 ARG A CG  
1694 C CD  A ARG A 234 ? 0.5547 0.4206 0.4187 -0.0650 -0.0386 0.0524  234 ARG A CD  
1695 C CD  B ARG A 234 ? 0.5712 0.4397 0.4376 -0.0650 -0.0390 0.0516  234 ARG A CD  
1696 N NE  A ARG A 234 ? 0.6121 0.4712 0.4656 -0.0684 -0.0375 0.0506  234 ARG A NE  
1697 N NE  B ARG A 234 ? 0.5607 0.4301 0.4219 -0.0709 -0.0398 0.0465  234 ARG A NE  
1698 C CZ  A ARG A 234 ? 0.6322 0.4922 0.4808 -0.0740 -0.0379 0.0458  234 ARG A CZ  
1699 C CZ  B ARG A 234 ? 0.5890 0.4526 0.4411 -0.0741 -0.0388 0.0453  234 ARG A CZ  
1700 N NH1 A ARG A 234 ? 0.6226 0.4903 0.4762 -0.0761 -0.0395 0.0423  234 ARG A NH1 
1701 N NH1 B ARG A 234 ? 0.6467 0.5026 0.4942 -0.0718 -0.0375 0.0492  234 ARG A NH1 
1702 N NH2 A ARG A 234 ? 0.5852 0.4380 0.4238 -0.0773 -0.0366 0.0446  234 ARG A NH2 
1703 N NH2 B ARG A 234 ? 0.6467 0.5119 0.4944 -0.0796 -0.0390 0.0402  234 ARG A NH2 
1704 N N   . THR A 235 ? 0.4597 0.3463 0.3615 -0.0586 -0.0469 0.0661  235 THR A N   
1705 C CA  . THR A 235 ? 0.4853 0.3770 0.3964 -0.0567 -0.0474 0.0679  235 THR A CA  
1706 C C   . THR A 235 ? 0.4798 0.3747 0.3919 -0.0597 -0.0488 0.0630  235 THR A C   
1707 O O   . THR A 235 ? 0.4618 0.3563 0.3689 -0.0637 -0.0503 0.0589  235 THR A O   
1708 C CB  . THR A 235 ? 0.4943 0.3896 0.4132 -0.0559 -0.0495 0.0731  235 THR A CB  
1709 O OG1 . THR A 235 ? 0.5024 0.3981 0.4189 -0.0604 -0.0530 0.0714  235 THR A OG1 
1710 C CG2 . THR A 235 ? 0.4504 0.3431 0.3689 -0.0521 -0.0479 0.0779  235 THR A CG2 
1711 N N   . PHE A 236 ? 0.4300 0.3275 0.3479 -0.0575 -0.0482 0.0634  236 PHE A N   
1712 C CA  . PHE A 236 ? 0.3905 0.2905 0.3096 -0.0594 -0.0495 0.0592  236 PHE A CA  
1713 C C   . PHE A 236 ? 0.3960 0.2995 0.3238 -0.0594 -0.0514 0.0619  236 PHE A C   
1714 O O   . PHE A 236 ? 0.4393 0.3437 0.3727 -0.0569 -0.0505 0.0670  236 PHE A O   
1715 C CB  . PHE A 236 ? 0.4020 0.3010 0.3191 -0.0564 -0.0468 0.0569  236 PHE A CB  
1716 C CG  . PHE A 236 ? 0.4165 0.3123 0.3252 -0.0566 -0.0449 0.0537  236 PHE A CG  
1717 C CD1 . PHE A 236 ? 0.4255 0.3173 0.3308 -0.0541 -0.0423 0.0565  236 PHE A CD1 
1718 C CD2 . PHE A 236 ? 0.3988 0.2957 0.3029 -0.0592 -0.0455 0.0477  236 PHE A CD2 
1719 C CE1 . PHE A 236 ? 0.4694 0.3578 0.3665 -0.0547 -0.0406 0.0532  236 PHE A CE1 
1720 C CE2 . PHE A 236 ? 0.4282 0.3228 0.3250 -0.0599 -0.0437 0.0445  236 PHE A CE2 
1721 C CZ  . PHE A 236 ? 0.4721 0.3621 0.3653 -0.0579 -0.0413 0.0473  236 PHE A CZ  
1722 N N   . GLY A 237 ? 0.4139 0.3191 0.3427 -0.0619 -0.0537 0.0584  237 GLY A N   
1723 C CA  . GLY A 237 ? 0.4158 0.3231 0.3519 -0.0620 -0.0552 0.0602  237 GLY A CA  
1724 C C   . GLY A 237 ? 0.4980 0.4043 0.4361 -0.0582 -0.0526 0.0611  237 GLY A C   
1725 O O   . GLY A 237 ? 0.4796 0.3839 0.4135 -0.0554 -0.0498 0.0601  237 GLY A O   
1726 N N   . GLY A 238 ? 0.4855 0.3928 0.4299 -0.0581 -0.0534 0.0634  238 GLY A N   
1727 C CA  . GLY A 238 ? 0.4687 0.3745 0.4148 -0.0545 -0.0507 0.0650  238 GLY A CA  
1728 C C   . GLY A 238 ? 0.4524 0.3562 0.3943 -0.0538 -0.0510 0.0599  238 GLY A C   
1729 O O   . GLY A 238 ? 0.5099 0.4117 0.4516 -0.0506 -0.0489 0.0605  238 GLY A O   
1730 N N   . GLY A 239 ? 0.4538 0.3583 0.3923 -0.0566 -0.0535 0.0549  239 GLY A N   
1731 C CA  . GLY A 239 ? 0.4782 0.3816 0.4128 -0.0556 -0.0539 0.0497  239 GLY A CA  
1732 C C   . GLY A 239 ? 0.4724 0.3748 0.4097 -0.0569 -0.0563 0.0485  239 GLY A C   
1733 O O   . GLY A 239 ? 0.4916 0.3933 0.4343 -0.0575 -0.0567 0.0526  239 GLY A O   
1734 N N   . THR A 240 ? 0.4398 0.3422 0.3733 -0.0574 -0.0578 0.0429  240 THR A N   
1735 C CA  . THR A 240 ? 0.4353 0.3356 0.3700 -0.0580 -0.0600 0.0412  240 THR A CA  
1736 C C   . THR A 240 ? 0.4252 0.3240 0.3558 -0.0541 -0.0592 0.0371  240 THR A C   
1737 O O   . THR A 240 ? 0.4453 0.3468 0.3718 -0.0537 -0.0590 0.0324  240 THR A O   
1738 C CB  . THR A 240 ? 0.4587 0.3607 0.3922 -0.0621 -0.0630 0.0376  240 THR A CB  
1739 O OG1 . THR A 240 ? 0.4875 0.3909 0.4245 -0.0654 -0.0641 0.0415  240 THR A OG1 
1740 C CG2 . THR A 240 ? 0.5010 0.4000 0.4346 -0.0625 -0.0653 0.0351  240 THR A CG2 
1741 N N   . LYS A 241 ? 0.4372 0.3321 0.3691 -0.0514 -0.0588 0.0389  241 LYS A N   
1742 C CA  . LYS A 241 ? 0.4602 0.3531 0.3881 -0.0472 -0.0585 0.0353  241 LYS A CA  
1743 C C   . LYS A 241 ? 0.4755 0.3667 0.4019 -0.0478 -0.0612 0.0309  241 LYS A C   
1744 O O   . LYS A 241 ? 0.5082 0.3953 0.4368 -0.0493 -0.0627 0.0327  241 LYS A O   
1745 C CB  . LYS A 241 ? 0.4979 0.3867 0.4269 -0.0437 -0.0562 0.0399  241 LYS A CB  
1746 C CG  . LYS A 241 ? 0.6078 0.4936 0.5323 -0.0392 -0.0565 0.0364  241 LYS A CG  
1747 C CD  . LYS A 241 ? 0.7384 0.6206 0.6620 -0.0351 -0.0538 0.0403  241 LYS A CD  
1748 C CE  . LYS A 241 ? 0.8936 0.7727 0.8123 -0.0303 -0.0544 0.0368  241 LYS A CE  
1749 N NZ  . LYS A 241 ? 0.8312 0.7067 0.7482 -0.0264 -0.0518 0.0406  241 LYS A NZ  
1750 N N   . LEU A 242 ? 0.4841 0.3784 0.4067 -0.0468 -0.0619 0.0249  242 LEU A N   
1751 C CA  . LEU A 242 ? 0.5017 0.3948 0.4224 -0.0466 -0.0643 0.0202  242 LEU A CA  
1752 C C   . LEU A 242 ? 0.5678 0.4584 0.4853 -0.0409 -0.0640 0.0176  242 LEU A C   
1753 O O   . LEU A 242 ? 0.5101 0.4044 0.4253 -0.0380 -0.0628 0.0152  242 LEU A O   
1754 C CB  . LEU A 242 ? 0.4902 0.3890 0.4089 -0.0493 -0.0651 0.0151  242 LEU A CB  
1755 C CG  . LEU A 242 ? 0.5282 0.4272 0.4441 -0.0482 -0.0671 0.0089  242 LEU A CG  
1756 C CD1 . LEU A 242 ? 0.5339 0.4273 0.4510 -0.0506 -0.0694 0.0102  242 LEU A CD1 
1757 C CD2 . LEU A 242 ? 0.5385 0.4441 0.4523 -0.0507 -0.0672 0.0039  242 LEU A CD2 
1758 N N   . GLU A 243 ? 0.5160 0.4001 0.4330 -0.0395 -0.0655 0.0180  243 GLU A N   
1759 C CA  . GLU A 243 ? 0.5590 0.4399 0.4723 -0.0338 -0.0659 0.0151  243 GLU A CA  
1760 C C   . GLU A 243 ? 0.6030 0.4828 0.5140 -0.0335 -0.0684 0.0096  243 GLU A C   
1761 O O   . GLU A 243 ? 0.5576 0.4367 0.4697 -0.0378 -0.0699 0.0090  243 GLU A O   
1762 C CB  . GLU A 243 ? 0.5690 0.4416 0.4822 -0.0315 -0.0651 0.0200  243 GLU A CB  
1763 C CG  . GLU A 243 ? 0.6828 0.5565 0.5971 -0.0302 -0.0623 0.0247  243 GLU A CG  
1764 C CD  . GLU A 243 ? 0.7720 0.6383 0.6869 -0.0289 -0.0608 0.0305  243 GLU A CD  
1765 O OE1 . GLU A 243 ? 0.8192 0.6821 0.7301 -0.0238 -0.0601 0.0304  243 GLU A OE1 
1766 O OE2 . GLU A 243 ? 0.8095 0.6739 0.7285 -0.0329 -0.0604 0.0352  243 GLU A OE2 
1767 N N   . ILE A 244 ? 0.5652 0.4443 0.4725 -0.0279 -0.0689 0.0056  244 ILE A N   
1768 C CA  . ILE A 244 ? 0.6044 0.4812 0.5090 -0.0263 -0.0712 0.0005  244 ILE A CA  
1769 C C   . ILE A 244 ? 0.6331 0.4985 0.5359 -0.0248 -0.0722 0.0034  244 ILE A C   
1770 O O   . ILE A 244 ? 0.6853 0.5457 0.5867 -0.0210 -0.0713 0.0065  244 ILE A O   
1771 C CB  . ILE A 244 ? 0.6988 0.5805 0.6004 -0.0204 -0.0714 -0.0051 244 ILE A CB  
1772 C CG1 . ILE A 244 ? 0.7025 0.5955 0.6055 -0.0220 -0.0702 -0.0083 244 ILE A CG1 
1773 C CG2 . ILE A 244 ? 0.6780 0.5564 0.5765 -0.0177 -0.0736 -0.0102 244 ILE A CG2 
1774 C CD1 . ILE A 244 ? 0.6962 0.5936 0.6014 -0.0288 -0.0701 -0.0086 244 ILE A CD1 
1775 N N   . LYS A 245 ? 0.6723 0.5333 0.5746 -0.0277 -0.0742 0.0020  245 LYS A N   
1776 C CA  . LYS A 245 ? 0.6190 0.4685 0.5189 -0.0270 -0.0755 0.0039  245 LYS A CA  
1777 C C   . LYS A 245 ? 0.7356 0.5822 0.6302 -0.0206 -0.0769 -0.0017 245 LYS A C   
1778 O O   . LYS A 245 ? 0.8715 0.7224 0.7649 -0.0205 -0.0781 -0.0073 245 LYS A O   
1779 C CB  . LYS A 245 ? 0.6420 0.4879 0.5437 -0.0335 -0.0772 0.0051  245 LYS A CB  
1780 C CG  . LYS A 245 ? 0.6601 0.4939 0.5602 -0.0352 -0.0787 0.0076  245 LYS A CG  
1781 C CD  . LYS A 245 ? 0.6784 0.5130 0.5825 -0.0431 -0.0799 0.0100  245 LYS A CD  
1782 C CE  . LYS A 245 ? 0.7109 0.5347 0.6147 -0.0463 -0.0812 0.0133  245 LYS A CE  
1783 N NZ  . LYS A 245 ? 0.7018 0.5174 0.5995 -0.0443 -0.0835 0.0085  245 LYS A NZ  
1784 N N   . LEU A 246 ? 0.8746 0.7139 0.7657 -0.0152 -0.0767 0.0000  246 LEU A N   
1785 C CA  . LEU A 246 ? 1.0347 0.8735 0.9211 -0.0073 -0.0775 -0.0045 246 LEU A CA  
1786 C C   . LEU A 246 ? 1.0160 0.8503 0.8983 -0.0050 -0.0799 -0.0102 246 LEU A C   
1787 O O   . LEU A 246 ? 0.9969 0.8193 0.8760 -0.0056 -0.0812 -0.0087 246 LEU A O   
1788 C CB  . LEU A 246 ? 0.9667 0.7980 0.8502 -0.0027 -0.0766 -0.0002 246 LEU A CB  
1789 C CG  . LEU A 246 ? 1.1112 0.9493 0.9973 -0.0022 -0.0742 0.0029  246 LEU A CG  
1790 C CD1 . LEU A 246 ? 1.1156 0.9475 0.9970 0.0043  -0.0736 0.0053  246 LEU A CD1 
1791 C CD2 . LEU A 246 ? 1.0297 0.8816 0.9185 -0.0022 -0.0738 -0.0016 246 LEU A CD2 
1792 C C1  . EDO B .   ? 0.6319 0.5077 0.4565 -0.1151 -0.0480 0.0246  301 EDO A C1  
1793 O O1  . EDO B .   ? 0.6152 0.4965 0.4393 -0.1181 -0.0456 0.0184  301 EDO A O1  
1794 C C2  . EDO B .   ? 0.6454 0.5261 0.4807 -0.1100 -0.0505 0.0265  301 EDO A C2  
1795 O O2  . EDO B .   ? 0.5864 0.4689 0.4269 -0.1057 -0.0489 0.0265  301 EDO A O2  
1796 C C1  . EDO C .   ? 0.6921 0.5993 0.6248 -0.1044 -0.0971 0.0374  302 EDO A C1  
1797 O O1  . EDO C .   ? 0.6136 0.5238 0.5484 -0.1061 -0.0992 0.0417  302 EDO A O1  
1798 C C2  . EDO C .   ? 0.7482 0.6555 0.6888 -0.1023 -0.0958 0.0410  302 EDO A C2  
1799 O O2  . EDO C .   ? 0.6881 0.5971 0.6294 -0.0985 -0.0917 0.0429  302 EDO A O2  
1800 N N1  . IMD D .   ? 0.9551 0.7546 0.7534 -0.0599 -0.0215 0.0532  303 IMD A N1  
1801 C C2  . IMD D .   ? 0.9632 0.7652 0.7660 -0.0597 -0.0236 0.0567  303 IMD A C2  
1802 N N3  . IMD D .   ? 1.2476 1.0398 1.0443 -0.0566 -0.0228 0.0607  303 IMD A N3  
1803 C C4  . IMD D .   ? 0.9919 0.7749 0.7801 -0.0549 -0.0200 0.0598  303 IMD A C4  
1804 C C5  . IMD D .   ? 0.9726 0.7604 0.7619 -0.0571 -0.0193 0.0551  303 IMD A C5  
# 
